ENTRY       EC 1.1.1.1                  Enzyme
NAME        alcohol dehydrogenase;
            aldehyde reductase;
            ADH;
            alcohol dehydrogenase (NAD);
            aliphatic alcohol dehydrogenase;
            ethanol dehydrogenase;
            NAD-dependent alcohol dehydrogenase;
            NAD-specific aromatic alcohol dehydrogenase;
            NADH-alcohol dehydrogenase;
            NADH-aldehyde dehydrogenase;
            primary alcohol dehydrogenase;
            yeast alcohol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     alcohol:NAD+ oxidoreductase
REACTION    an alcohol + NAD+ = an aldehyde or ketone + NADH + H+ [RN:R07326
            R07327]
ALL_REAC    R07326 > R00623 R00754 R01036 R04805 R04880 R06917 R06927;
            R07327 > R00624;
            (other) R01041 R05233 R05234 R07105
SUBSTRATE   alcohol [CPD:C00069];
            NAD+ [CPD:C00003]
PRODUCT     aldehyde [CPD:C00071];
            ketone [CPD:C00709];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COFACTOR    Iron [CPD:C00023];
            Zinc [CPD:C00038]
COMMENT     A zinc protein. Acts on primary or secondary alcohols or
            hemi-acetals; the animal, but not the yeast, enzyme acts also on
            cyclic secondary alcohols.
REFERENCE   1
  AUTHORS   Branden, G.-I., Jornvall, H., Eklund, H. and Furugren, B.
  TITLE     Alcohol dehydrogenase.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 11, Academic
            Press, New York, 1975, p. 103-190.
  ORGANISM  horse, human [GN:hsa], rat [GN:rno], Saccharomyces cerevisiae
            [GN:sce]
REFERENCE   2  [PMID:320001]
  AUTHORS   Jornvall H.
  TITLE     Differences between alcohol dehydrogenases. Structural properties
            and evolutionary aspects.
  JOURNAL   Eur. J. Biochem. 72 (1977) 443-52.
  ORGANISM  horse, human [GN:hsa], rat [GN:rno], Bacillus stearotherrnophilus,
            Drosophila melanogaster [GN:dme]
REFERENCE   3
  AUTHORS   Negelein, E. and Wulff, H.-J.
  TITLE     Diphosphopyridinproteid ackohol, acetaldehyd.
  JOURNAL   Biochem. Z. 293 (1937) 351-389.
REFERENCE   4
  AUTHORS   Sund, H. and Theorell, H.
  TITLE     Alcohol dehydrogenase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 25-83.
  ORGANISM  horse, Saccharomyces cerevisiae [GN:sce]
REFERENCE   5  [PMID:13605979]
  AUTHORS   THEORELL H.
  TITLE     Kinetics and equilibria in the liver alcohol dehydrogenase system.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 20 (1958) 31-49.
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00071  Fatty acid metabolism
            PATH: map00120  Bile acid biosynthesis
            PATH: map00350  Tyrosine metabolism
            PATH: map00561  Glycerolipid metabolism
            PATH: map00624  1- and 2-Methylnaphthalene degradation
            PATH: map00641  3-Chloroacrylic acid degradation
            PATH: map00980  Metabolism of xenobiotics by cytochrome P450
ORTHOLOGY   KO: K00001  alcohol dehydrogenase
GENES       HSA: 124(ADH1A) 125(ADH1B) 126(ADH1C) 127(ADH4) 128(ADH5)
                 130(ADH6) 131(ADH7) 137872(ADHFE1)
            PTR: 461396(ADH1B) 471257(ADH7)
            MCC: 707682(ADH1A)
            MMU: 11522(Adh1) 11529(Adh7) 11532(Adh5) 26876(Adh4)
            RNO: 171178(Adh7) 24172(Adh1) 29646(Adh4)
            CFA: 474946(LOC474946) 478487(ADH4) 478489(ADH1C)
                 609781(LOC609781)
            GGA: 395979(ADH1B) 422705(RCJMB04_12i19) 426446(ADHFE1)
            XLA: 398993(MGC68507) 444547(MGC83376) 445841(adh3) 446738(adh6)
            XTR: 496906(adh6) 496916(adh1b) 497007(LOC497007)
            DRE: 116517(adh5)
            SPU: 579220(LOC579220)
            DME: Dmel_CG3425(T3dh) Dmel_CG3763(Fbp2) Dmel_CG4899(Pdh)
                 Dmel_CG6598(Fdh)
            CEL: D2063.1(dehydrogenase) H24K24.3 K12G11.3(sodh-1)
                 K12G11.4(sodh-2) Y38F1A.6
            ATH: AT1G22430 AT1G22440 AT1G32780 AT1G64710 AT5G42250
                 AT5G43940(ADH2)
            OSA: 4331130 4335572 4344469 4350053
            CME: CMS125C
            SCE: YBR145W(ADH5) YDL168W(SFA1) YGL256W(ADH4) YMR083W(ADH3)
                 YMR303C(ADH2) YOL086C(ADH1)
            AGO: AGOS_AAR084W AGOS_ABL033C AGOS_ACL148C AGOS_AER032W
            PIC: PICST_27980(ADH2) PICST_29252(FDH1) PICST_44171(IFR1)
                 PICST_67803(SAD2) PICST_68558(ADH1)
            CGR: CAGL0I07843g CAGL0J01441g CAGL0L01111g
            SPO: SPAC5H10.06c SPBC1773.06c SPCC13B11.01(adh1)
            ANI: AN2286.2 AN5913.2 AN7632.2 AN7636.2 AN8979.2
            AFM: AFUA_2G00970 AFUA_2G01040 AFUA_2G10960 AFUA_2G13270
                 AFUA_4G08240 AFUA_5G06240 AFUA_6G00510 AFUA_7G01010
                 AFUA_7G04380
            AOR: AO090003001407 AO090009000634 AO090011000117 AO090023000745
                 AO090026000555 AO090103000187 AO090701000350 AO090701000373
            ANG: An17g01530(adhA)
            CNE: CNE00710 CNG00600 CNM01690
            UMA: UM01885.1 UM02790.1 UM06244.1
            DDI: DDBDRAFT_0204255 DDBDRAFT_0217455
            CPV: cgd8_1720
            CHO: Chro.80199
            TET: TTHERM_00295700
            TCR: 506357.50 511277.60
            LMA: LmjF30.2090
            EHI: 105.t00016 106.t00017 11.t00007 124.t00001 189.t00002
                 22.t00017 22.t00022 328.t00004
            ECO: b0356(frmA) b1241(adhE) b1478(adhP)
            ECJ: JW0347(frmA) JW1228(adhE) JW1474(adhP) JW5648(yiaY)
            ECE: Z0456(adhC) Z2016(adhE) Z2232(adhP) Z5010(yiaY)
            ECS: ECs0411 ECs1741 ECs2082 ECs4466
            ECC: c0465(adhC) c1705(adhE) c1911(adhP) c4410(yiaY)
            ECI: UTI89_C0359(yahK) UTI89_C0376(adhC) UTI89_C0680
                 UTI89_C1438(adhE) UTI89_C1696(adhP) UTI89_C2777(eutG)
                 UTI89_C3684(yhdH) UTI89_C4131(yiaY) UTI89_C4465
            ECP: ECP_0421 ECP_0696 ECP_1287 ECP_1480 ECP_3691
            ECV: APECO1_1388 APECO1_1645(adhC) APECO1_1661(yahK) APECO1_2282
                 APECO1_2864(yiaY) APECO1_355(adhE) APECO1_614(adhP)
            ECW: EcE24377A_1389(adhE) EcE24377A_4087(adhB)
            ECX: EcHS_A0421 EcHS_A0651 EcHS_A1350 EcHS_A3794
            STY: STY1302(adh) STY1493(adhP) STY3830
            STT: t1482(adhP) t1660(adh) t3575
            SPT: SPA1129(adh) SPA1301(adhP) SPA3887
            SEC: SC1568(adhP) SC1622(adh3) SC1744(adhE) SC3934(adh2)
            STM: STM1627 STM1749(adhE)
            YPE: YPO1502 YPO2180(adhE)
            YPK: y2023(adhE) y2667(adhC)
            YPM: YP_1392(adhC) YP_1976(adhE)
            YPA: YPA_0797 YPA_1537
            YPN: YPN_1646 YPN_2477
            YPS: YPTB1517 YPTB2103(adhE)
            YPI: YpsIP31758_0587 YpsIP31758_1963(adhE) YpsIP31758_2422
                 YpsIP31758_2473
            SFL: SF1240(adhE) SF1747(adhP) SF3627(yiaY)
            SFX: S1326(adhE) S1880(adhP) S4141(yiaY)
            SFV: SFV_1253(adhE) SFV_3944(yiaY)
            SSN: SSON_0335(adhC) SSON_1939(adhE)
            SBO: SBO_1828(adhE) SBO_3589(yiaY)
            SDY: SDY_1295(adhE) SDY_1608(adhP)
            ECA: ECA2326(adhE) ECA2714(adhC) ECA3950
            PLU: plu1563 plu2496(adhE) plu4332(adhC)
            SGL: SG1372
            HIN: HI0185(adhC)
            PMU: PM1453(adh2)
            MSU: MS1386(adhC) MS1802(eutG) MS2190(eutG)
            APL: APL_1011(adh2) APL_1208(adhC) APL_1959(adhI)
            XFA: XF1746 XF2389
            XFT: PD1406(yahK)
            XCC: XCC2730 XCC3389 XCC3475(adhC) XCC3703(ybdR)
            XCB: XC_0686 XC_0775 XC_1384 XC_3774
            XCV: XCV0185 XCV0713 XCV0788 XCV2170 XCV2333 XCV3047 XCV3866
            XAC: XAC0201(adh) XAC0652(adhC) XAC0734 XAC2826 XAC2896
                 XAC3747(ybdR)
            XOO: XOO1535 XOO3867
            XOM: XOO_1325(XOO1325) XOO_1423(XOO1423) XOO_3647(XOO3647)
                 XOO_4231(XOO4231)
            VCH: VC2033
            VVU: VV1_0344 VV1_3111 VV2_0019
            VVY: VV0841 VV1175 VV2175 VVA0527
            VPA: VP2121 VPA0071 VPA0566
            VFI: VF0023 VF0918 VF1188
            PPR: PBPRA0784 PBPRA1103(adhE) PBPRA1480 PBPRA2519(yiaY)
            PAE: PA2119 PA2158 PA2188 PA3629(adhC) PA5427(adhA)
            PAU: PA14_71630(adhA)
            PAP: PSPA7_1510
            PPU: PP_1616 PP_3839
            PST: PSPTO_1558(adhC) PSPTO_4285(adhB)
            PSB: Psyr_1367 Psyr_2956 Psyr_3987
            PSP: PSPPH_3816(adhC) PSPPH_3994(adhB)
            PFL: PFL_1200 PFL_1399(adhB) PFL_1755 PFL_1906 PFL_4068(adh)
                 PFL_4742
            PFO: Pfl_1125 Pfl_1311 Pfl_3346
            PEN: PSEEN0727 PSEEN2613(adhC-1) PSEEN2959(adhB) PSEEN4196(adhC-2)
            PMY: Pmen_0381
            PAR: Psyc_0011 Psyc_1042 Psyc_1671(adhC) Psyc_2008(adh)
            PCR: Pcryo_0018 Pcryo_1428 Pcryo_1939
            ACI: ACIAD1879(adhC) ACIAD1950 ACIAD2015 ACIAD2929 ACIAD3339(adhA)
            SON: SO_1490(adhB) SO_2054(adhC) SO_2136(adhE) SO_A0161 SO_A0164
            SDN: Sden_2000 Sden_2578 Sden_3767
            SFR: Sfri_1898 Sfri_2798 Sfri_4059
            SSE: Ssed_2530
            SHE: Shewmr4_1786 Shewmr4_2762
            SHM: Shewmr7_2191 Shewmr7_2840
            SHN: Shewana3_1788 Shewana3_1837 Shewana3_2938
            ILO: IL0796 IL1773(adhC)
            CPS: CPS_0817 CPS_1431 CPS_3853
            PHA: PSHAa1386(adhC) PSHAa1488(yhdH) PSHAa2213(adhC)
                 PSHAb0511(adhP)
            PAT: Patl_0425 Patl_1438 Patl_1481
            LPN: lpg2492
            LPF: lpl2034 lpl2413
            LPP: lpp2558
            MCA: MCA0775
            TCX: Tcr_0211
            NOC: Noc_0592
            AEH: Mlg_2137
            HCH: HCH_01446(adhC) HCH_05054
            CSA: Csal_1091 Csal_1426 Csal_2912
            ABO: ABO_0061 ABO_0117(adhC) ABO_0817 ABO_1231(adhA)
                 ABO_1352(adhB) ABO_2419 ABO_2483
            MMW: Mmwyl1_0172 Mmwyl1_1672 Mmwyl1_4422
            AHA: AHA_1331 AHA_2616
            NME: NMB0546 NMB1304 NMB1395
            NMA: NMA0725(adhA) NMA1518(adhC)
            NMC: NMC0486(adhA) NMC1241(adhC)
            NGO: NGO0711 NGO1442(adhA)
            CVI: CV_0740(adhC) CV_0808 CV_1137(adhE) CV_2051 CV_2728
            RSO: RS00889(RSp0430) RSc0605(adhC2) RSc1505(RS03800)
                 RSc3130(adhA) RSp0069(adhC1)
            REU: Reut_B3677 Reut_B4000 Reut_B4710 Reut_B4833 Reut_B5201
                 Reut_C5952 Reut_C6082 Reut_C6089 Reut_C6321
            REH: H16_A0757(adh) H16_A3330 H16_A3501(rplK) H16_B0517
                 H16_B1433(adhP) H16_B1699 H16_B1745 H16_B1834 H16_B2470
            RME: Rmet_0545 Rmet_1093 Rmet_4784 Rmet_4943 Rmet_5102 Rmet_5545
                 Rmet_5645
            BMA: BMA0324 BMA2006 BMAA0132 BMAA0163 BMAA0709
            BMV: BMASAVP1_1300 BMASAVP1_1333 BMASAVP1_A0622
            BML: BMA10299_0753 BMA10299_A2456
            BMN: BMA10247_0070 BMA10247_A0157 BMA10247_A0189 BMA10247_A1718
            BXE: Bxe_A0713(flhA) Bxe_A1730 Bxe_A1872 Bxe_B1066 Bxe_B2290
                 Bxe_B2357 Bxe_B2518 Bxe_C0527 Bxe_C1266 Bxe_C1356
            BUR: Bcep18194_B2077 Bcep18194_B2551 Bcep18194_C6773
            BCN: Bcen_1392 Bcen_3928 Bcen_4360 Bcen_4742
            BCH: Bcen2424_4006 Bcen2424_4438
            BAM: Bamb_3412
            BPS: BPSL0820(flhA) BPSL2701 BPSS0840 BPSS1918 BPSS1944(adhA)
                 BPSS2024
            BPM: BURPS1710b_2237(eutG) BURPS1710b_3181 BURPS1710b_A1018
                 BURPS1710b_A1046(adhA) BURPS1710b_A1142 BURPS1710b_A2432
            BPL: BURPS1106A_0866 BURPS1106A_A1693
            BPD: BURPS668_0862
            BTE: BTH_I0686 BTH_I1436 BTH_II0428 BTH_II0459 BTH_II1565
            BPE: BP0777 BP2601 BP3751(adhI)
            BPA: BPP0339 BPP2723 BPP4251(adhI)
            BBR: BB0342 BB2775 BB4838(adhI)
            RFR: Rfer_0121 Rfer_2865
            POL: Bpro_1201 Bpro_3129 Bpro_5563
            MPT: Mpe_A0936 Mpe_A2064
            HAR: HEAR2367(adh)
            MMS: mma_0093 mma_0221 mma_1172
            NEU: NE0620 NE0820 NE0907(adhC1)
            NET: Neut_1385
            NMU: Nmul_A1937
            EBA: ebA3118 ebA4623(adhB) ebA5713(fdhG) p2A334
            AZO: azo0111(adhA) azo1971 azo2700 azo3181 azo3317(yhdH)
            DAR: Daro_1348
            TBD: Tbd_1767
            MFA: Mfla_0203
            GSU: GSU0573
            GME: Gmet_1046
            PCA: Pcar_0251 Pcar_0255 Pcar_1246 Pcar_1594 Pcar_2506 Pcar_2847
                 Pcar_2848
            DVU: DVU2396 DVU2405 DVU2885
            DDE: Dde_1164 Dde_3062 Dde_3126 Dde_3523 Dde_3534
            BBA: Bd0898(adhC) Bd2813(adh)
            DPS: DP0950 DP0951 DP0955 DP1034
            MXA: MXAN_6802(adh) MXAN_7094
            SAT: SYN_01159
            PUB: SAR11_0272(adhP) SAR11_0529 SAR11_1244(yhdH) SAR11_1287
            MLO: mlr0872 mlr1136 mlr1178
            MES: Meso_1317 Meso_1868 Meso_2263 Meso_2671
            SME: SMa1156 SMa1296(adhA1) SMa2113(adhC2) SMb20170(fdh) SMc00105
                 SMc01270(adhC1) SMc03929 SMc04270
            SMD: Smed_5260
            ATU: Atu0626(adhP) Atu1595 Atu1670(adhC) Atu2151(adh)
                 Atu4289(adhC) Atu5240(adhP)
            ATC: AGR_C_1112 AGR_C_2931(adh4) AGR_C_3072 AGR_C_3897
                 AGR_L_1150(adhE) AGR_pAT_339
            RET: RHE_CH00460 RHE_CH01189(ypch00392) RHE_CH02227(adhCch)
                 RHE_CH02474(ypch00832) RHE_CH02884(ypch00995)
                 RHE_CH03285(ypch01140) RHE_PB00029 RHE_PB00045(ypb00024)
                 RHE_PC00105(adhA1) RHE_PC00106(adhA2) RHE_PD00107(adhE)
                 RHE_PF00203(ypf00099) RHE_PF00365(ypf00190) RHE_PF00402(adhCf)
            RLE: RL0310 RL1325 RL1876(adh) RL2813 RL3344 RL3711 pRL100135
                 pRL110508 pRL120042 pRL120182 pRL120524(adhI) pRL120602
                 pRL90027(adhA) pRL90098
            BME: BMEI0925 BMEI1114 BMEI1746 BMEI1819 BMEII0553 BMEII0867
            BMF: BAB1_0128 BAB1_0204 BAB1_0871 BAB2_0506 BAB2_0821
            BMS: BR0203 BR0852 BR1061 BRA0401 BRA0734
            BMB: BruAb1_0127 BruAb1_0198 BruAb1_0864 BruAb2_0498 BruAb2_0800
            BJA: bll4101 bll5655 bll7898 blr2780 blr3675 blr4874 blr6070
                 blr6215(adhC)
            BRA: BRADO0250 BRADO0921(adh) BRADO2457 BRADO2816 BRADO2866(adhA)
                 BRADO3321 BRADO4151 BRADO4353 BRADO5171 BRADO5308
                 BRADO5486(adhC)
            BBT: BBta_0243 BBta_2803 BBta_3627 BBta_3825 BBta_4528
                 BBta_5308(adhA) BBta_5367 BBta_5638 BBta_5755 BBta_5970(adhC)
                 BBta_7131(adh)
            RPA: RPA0374 RPA0656(badC) RPA1205 RPA1955 RPA2018 RPA3067 RPA3655
            RPB: RPB_0946 RPB_1148 RPB_1871 RPB_2474 RPB_3357 RPB_3418
            RPC: RPC_0105 RPC_1030 RPC_1164 RPC_1965 RPC_2107 RPC_2307
                 RPC_2974 RPC_3411
            RPD: RPD_1250 RPD_1539 RPD_2034 RPD_2086 RPD_2972 RPD_3495
            RPE: RPE_0587 RPE_0609 RPE_1228 RPE_2019 RPE_3298 RPE_3649
                 RPE_3692 RPE_4678
            NWI: Nwi_1739
            NHA: Nham_1916 Nham_2346 Nham_2536
            BHE: BH07430(adh)
            BQU: BQ05280(adh)
            CCR: CC_2516 CC_3029
            SIL: SPO1889 SPO3399 SPO3850 SPOA0272
            SIT: TM1040_0040
            RSP: RSP_0960 RSP_1824(adh) RSP_2576(adhI) RSP_2799 RSP_3537
            JAN: Jann_3964
            RDE: RD1_1637(ccrA) RD1_2918(adhE) RD1_3806(flhA)
            MMR: Mmar10_2836
            HNE: HNE_0560
            ZMO: ZMO1236(adhA) ZMO1596(adhB) ZMO1722(adhC)
            GOX: GOX0313 GOX0314 GOX2018
            GBE: GbCGDNIH1_0098
            RRU: Rru_A0904 Rru_A0930
            ABA: Acid345_2645 Acid345_3044 Acid345_4584
            BSU: BG11902(adhB) BG11941(gbsB) BG13553(yogA)
            BHA: BH1829(adhB)
            BAN: BA2222 BA2267 BA2588 BA2647 BA3131(adhB) BA3566 BA4599
            BAR: GBAA2222 GBAA2267 GBAA2588 GBAA2647 GBAA3131(adhB) GBAA3566
                 GBAA4599
            BAA: BA_2770 BA_3097 BA_3165 BA_3633 BA_4058 BA_5039
            BAT: BAS2066 BAS2111 BAS2412 BAS2466 BAS2912 BAS3306 BAS4267
            BCE: BC0802 BC2220(adhA) BC2529 BC2660 BC3092 BC4365
            BCA: BCE_0198 BCE_0742 BCE_0877 BCE_1099 BCE_2252 BCE_2296(adhA)
                 BCE_2604 BCE_2677 BCE_3145(adhB) BCE_3521 BCE_4453
            BCZ: BCZK0168 BCZK0681 BCZK2005(gbsB) BCZK2048(adhB)
                 BCZK2331(adhB) BCZK2390 BCZK2838(adhB) BCZK3221 BCZK4115
            BTK: BT9727_0165 BT9727_2006(gbsB) BT9727_2050(adhB)
                 BT9727_2367(adhB) BT9727_2429 BT9727_2881(adhB) BT9727_3273
                 BT9727_4104
            BTL: BALH_0175 BALH_0616 BALH_0714 BALH_3956
            BLI: BL00199 BL02473(adhB) BL02563(gbsB) BL05087
            BLD: BLi00992(yogA) BLi03269(gbsB) BLi03502 BLi03831(adhB)
                 BLi04290
            BCL: ABC0046(adhA) ABC0979(gbsB) ABC3428(adhB)
            BAY: RBAM_005890
            BPU: BPUM_0461 BPUM_1147 BPUM_2734(gbsB) BPUM_2803(yugK)
                 BPUM_2804(yugJ) BPUM_2977
            OIH: OB1376 OB2738 OB2801
            GKA: GK0731 GK0938 GK2774
            SAU: SA0143(adhE) SA0562(adh1)
            SAV: SAV0148(adhE) SAV0605(adh1)
            SAM: MW0123(adhE) MW0568(adh1)
            SAR: SAR0150(adhE) SAR0613(adhA)
            SAS: SAS0123 SAS0573(adhA)
            SAC: SACOL0135 SACOL0237 SACOL0241 SACOL0660(adhA) SACOL2177
                 SACOL2178 SACOL2367
            SAB: SAB0089 SAB0557(adhA) SAB1296c
            SAA: SAUSA300_0055 SAUSA300_0151(adhE) SAUSA300_0250
                 SAUSA300_0594(adh) SAUSA300_2147
            SAO: SAOUHSC_00113 SAOUHSC_00608
            SEP: SE0375 SE0506 SE2098
            SER: SERP0197 SERP0257(adhA) SERP0389 SERP1785 SERP1786 SERP1962
                 SERP2112 SERP2469
            SHA: SH0373(adhC) SH0522
            SSP: SSP0237 SSP1623
            LMO: lmo1634
            LMF: LMOf2365_1656(adhE)
            LIN: lin1675
            LWE: lwe0565 lwe1650
            LLA: L13145(adhE) L190278(ypjA) L55758(adhA)
            LLC: LACR_1641 LACR_1990 LACR_2457
            LLM: llmg_0955 llmg_1991(adhA)
            SPY: SPy_0044(adhA) SPy_1111
            SPZ: M5005_Spy_0039(adh2) M5005_Spy_0040(adhA) M5005_Spy_0834
            SPM: spyM18_0043(adhE) spyM18_0045(adhP) spyM18_1073
            SPG: SpyM3_0036(adh2) SpyM3_0037(adh1) SpyM3_0772
            SPS: SPs0037 SPs0038 SPs0972
            SPH: MGAS10270_Spy0042 MGAS10270_Spy0043(adhA)
            SPI: MGAS10750_Spy0041 MGAS10750_Spy0042(adhA) MGAS10750_Spy0985
            SPJ: MGAS2096_Spy0041 MGAS2096_Spy0042(adhA) MGAS2096_Spy0043
                 MGAS2096_Spy0044
            SPK: MGAS9429_Spy0040(adh2) MGAS9429_Spy0041(adhA)
                 MGAS9429_Spy0953
            SPF: SpyM50039(adhE) SpyM50040(adhP)
            SPA: M6_Spy0088 M6_Spy0090(adhA) M6_Spy0832 M6_Spy0833
            SPB: M28_Spy0039 M28_Spy0040(adhA) M28_Spy0811
            SPN: SP_0285 SP_1855 SP_2026 SP_2055 SP_2157
            SPR: spr0262(adhP) spr1670(adhB) spr1837(adhE) spr1866(adh)
                 spr1963(adh2)
            SPD: SPD_0265 SPD_1834 SPD_1865 SPD_1985
            SAG: SAG0053(adhE) SAG0054(adhP) SAG0428 SAG1637(adh)
            SAN: gbs0053 gbs0054 gbs1684
            SAK: SAK_0086 SAK_0087 SAK_1651
            SMU: SMU.119(adh) SMU.148(adhE) SMU.1867c
            STC: str0882 str0936(adhB) str1879 str1881 str1882 str1884
            STL: stu0882 stu0936(adhB) stu1879 stu1880 stu1881 stu1882 stu1883
                 stu1884
            SSA: SSA_0068(adhE) SSA_0572 SSA_0921(adhB) SSA_1917(adh)
            SGO: SGO_0113(acdH) SGO_1774
            LPL: lp_1665(adh1) lp_2873(adh2) lp_3662(adhE)
            LJO: LJ1120 LJ1766
            LAC: LBA0461(adhE) LBA1114
            LSA: LSA0258 LSA0379(adhE) LSA0925(adh) LSA1364 LSA1702
            LSL: LSL_1901
            LBR: LVIS_0119 LVIS_0254 LVIS_0869
            LCA: LSEI_0775 LSEI_2787
            EFA: EF0900(adhE) EF1826
            OOE: OEOE_0527 OEOE_1248
            STH: STH2049
            CAC: CAC3375 CA_P0035(adhE) CA_P0162(adhE1)
            CPE: CPE0449(adh) CPE2531(adhE)
            CPF: CPF_0451 CPF_2855(adhE)
            CPR: CPR_0442 CPR_2540
            CTC: CTC01366 CTC01453
            CDF: CD0334(adhE) CD2966(adhE) CD3006
            CBO: CBO0345(aad)
            CBA: CLB_0388(adhE) CLB_1463 CLB_2063
            CBH: CLC_0403(adhE) CLC_1475 CLC_2068
            CBF: CLI_0416(adhE) CLI_1522 CLI_2169
            CKL: CKL_1067 CKL_1075 CKL_1077 CKL_1078 CKL_2967 CKL_2978
                 CKL_3000 CKL_3425
            CHY: CHY_0925
            DSY: DSY0565 DSY0623 DSY1101 DSY2755 DSY3044
            CSC: Csac_0407
            TTE: TTE0696(eutG)
            MTA: Moth_1911
            MPE: MYPE4620(gbsB)
            MTU: Rv0162c(adhE1) Rv0761c(adhB) Rv1530(adh) Rv1862(adhA)
            MTC: MT0171 MT0786 MT1581 MT1911
            MBO: Mb0167c(adhE1) Mb0784c(adhB) Mb1557(adh) Mb1893(adhA)
            MBB: BCG_0198c(adhE1) BCG_0813c(adhB) BCG_1582(adh) BCG_1898(adhA)
            MLE: ML2053
            MPA: MAP0595c(adhB) MAP1571(adhA_1) MAP1613c(adhA_2)
                 MAP3596c(adhE)
            MAV: MAV_0705 MAV_1614 MAV_1943 MAV_2646 MAV_5214
            MSM: MSMEG_0127 MSMEG_0217 MSMEG_0276 MSMEG_0303 MSMEG_0590(rhaD)
                 MSMEG_1138 MSMEG_1977 MSMEG_2048 MSMEG_3388 MSMEG_3464
                 MSMEG_3915 MSMEG_4167 MSMEG_5866 MSMEG_6242 MSMEG_6833
            MMC: Mmcs_0111 Mmcs_0137 Mmcs_1713
            CGL: NCgl0219(cgl0222) NCgl2449(cgl2537) NCgl2709(cgl2807)
            CGB: cg0273 cg3107(adhA)
            CEF: CE0053
            CDI: DIP2114(adhA)
            NFA: nfa12770 nfa16040 nfa20970 nfa28910 nfa35620 nfa38820
            RHA: RHA1_ro00325(adh1) RHA1_ro00447 RHA1_ro00525 RHA1_ro01205
                 RHA1_ro02150 RHA1_ro02497 RHA1_ro04547 RHA1_ro05321
                 RHA1_ro08443 RHA1_ro08627 RHA1_ro08635 RHA1_ro08965(adh2)
                 RHA1_ro11170(adhB)
            SCO: SCO0199(SCJ12.11c) SCO0259(SCF1.01) SCO5262(2SC7G11.24)
            SMA: SAV1141(adhA1) SAV1357(adhA2) SAV1393(adhA3) SAV2980
                 SAV414(pteB) SAV5335 SAV7169
            TWH: TWT326(adh)
            TWS: TW445(adh)
            LXX: Lxx22610(adh)
            AAU: AAur_0342(adhT) AAur_3063(adhA) AAur_3716(rhaD)
            PAC: PPA0539
            TFU: Tfu_1270 Tfu_1276 Tfu_1755
            FRA: Francci3_0264 Francci3_2240 Francci3_2514 Francci3_2945
                 Francci3_3750
            FAL: FRAAL0199 FRAAL0607 FRAAL1637 FRAAL3122 FRAAL3376(adhC)
                 FRAAL5274(adhC1) FRAAL5983
            ACE: Acel_0584
            SEN: SACE_0927(adh10) SACE_1535 SACE_2374 SACE_2733 SACE_2944
                 SACE_2945 SACE_3519(adh) SACE_4085(adh) SACE_4163(adh1)
                 SACE_4519 SACE_4852(adh1) SACE_6396
            BLO: BL1090 BL1131(badC) BL1575(adh2)
            BAD: BAD_0319 BAD_0514(badC)
            RXY: Rxyl_1958 Rxyl_3153
            RBA: RB10805 RB13260(yhdH) RB4131(yjjN) RB5320 RB5856(adh)
                 RB5948(adh)
            LIL: LA0296 LA0325 LA1616(adeH) LA2361 LA2629 LA3158
            LIC: LIC10253 LIC10282 LIC10958 LIC11357 LIC11586 LIC12166
            SYN: sll0990
            SYC: syc1059_d
            SYF: Synpcc7942_0459
            SYG: sync_2669
            CYA: CYA_0473(adhE) CYA_0992
            CYB: CYB_0241 CYB_0338
            TEL: tlr0227
            GVI: gll2836 gll4111 glr4425
            ANA: all0879 all2810 all5334
            AVA: Ava_1089 Ava_4482
            PMB: A9601_14521(adhC) A9601_14641
            PMC: P9515_14261
            PMF: P9303_19231
            PMG: P9301_14501
            PMH: P9215_14901(ribD)
            PME: NATL1_16841
            TER: Tery_2840
            BFR: BF1290
            SRU: SRU_0710 SRU_2306
            CHU: CHU_1246(adhP)
            GFO: GFO_0760 GFO_1574 GFO_2086
            CTE: CT1275
            CCH: Cag_0888 Cag_1128 Cag_1710
            DRA: DR_2279
            TTH: TTC0097 TTC1572
            TTJ: TTHA0466
            AAE: aq_1240(adh2) aq_1362(adh1)
            TMA: TM0111 TM0920
            MMP: MMP0802
            MAC: MA2630(adh)
            MBA: Mbar_A0784 Mbar_A2344
            MMA: MM_2769
            MSI: Msm_1380
            HAL: VNG1821G(adh4) VNG2617G(adh2)
            HMA: pNG7022(adh1) pNG7032(adh10) pNG7101(adh8) pNG7103(adh7)
                 pNG7278(adh12) pNG7289(adh6) pNG7314(adhC) pNG7351(adh13)
                 rrnAC0012(adh11) rrnAC0191(adh3) rrnAC1300(adh9)
                 rrnAC1402(adh4) rrnAC1975(adh5) rrnAC2172(adh14)
                 rrnAC3506(adh2)
            HWA: HQ1124A(adh) HQ1729A(adh) HQ2366A(adh) HQ3648A(adh)
            NPH: NP1260A(adh)
            TAC: Ta0832m Ta0841
            TVO: TVN0396 TVN0944 TVN1284
            PTO: PTO0846 PTO1151 PTO1249
            PHO: PH0743
            PAB: PAB1511
            PFU: PF0608
            TKO: TK1008
            APE: APE_1245.1 APE_1557.1 APE_1963.1 APE_2239.1
            IHO: Igni_0132
            SSO: SSO0472(adh-1) SSO0764(adh-2) SSO1646(adh-5) SSO2494(adh-8)
                 SSO2536(adh-10) SSO2878(adh-13)
            STO: ST0038 ST0053 ST0075 ST0480 ST2056 ST2577
            SAI: Saci_0911(adh) Saci_1115(adh) Saci_2057 Saci_2126(adh)
                 Saci_2145(adh) Saci_2205 Saci_2224(adh)
            PAI: PAE1921(zinC) PAE2051(zinC) PAE2332(zinC) PAE2931(zinC)
STRUCTURES  PDB: 1A4U  1A71  1A72  1ADB  1ADC  1ADF  1ADG  1AGN  1AXE  1AXG  
                 1B14  1B15  1B16  1B2L  1BTO  1CDO  1D1S  1D1T  1DEH  1E3E  
                 1E3I  1E3L  1EE2  1H2B  1HDX  1HDY  1HDZ  1HET  1HEU  1HF3  
                 1HLD  1HSO  1HSZ  1HT0  1HTB  1JU9  1JVB  1LDE  1LDY  1LLU  
                 1M6H  1M6W  1MA0  1MC5  1MG0  1MG5  1MGO  1MP0  1N8K  1N92  
                 1NTO  1NVG  1O2D  1P1R  1QLH  1QLJ  1QV6  1QV7  1R37  1RJW  
                 1SBY  1TEH  1U3T  1U3U  1U3V  1U3W  1VJ0  1YE3  2EER  2FZE  
                 2FZW  2HCY  2JHF  2JHG  2OHX  2OXI  3BTO  3HUD  5ADH  6ADH  
                 7ADH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.1
            ExPASy - ENZYME nomenclature database: 1.1.1.1
            ExplorEnz - The Enzyme Database: 1.1.1.1
            ERGO genome analysis and discovery system: 1.1.1.1
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.1
            BRENDA, the Enzyme Database: 1.1.1.1
            CAS: 9031-72-5
///
ENTRY       EC 1.1.1.2                  Enzyme
NAME        alcohol dehydrogenase (NADP+);
            aldehyde reductase (NADPH2);
            NADP-alcohol dehydrogenase;
            NADP+-aldehyde reductase;
            NADP+-dependent aldehyde reductase;
            NADPH-aldehyde reductase;
            NADPH-dependent aldehyde reductase;
            nonspecific succinic semialdehyde reductase;
            ALR 1;
            low-Km aldehyde reductase;
            high-Km aldehyde reductase;
            alcohol dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     alcohol:NADP+ oxidoreductase
REACTION    an alcohol + NADP+ = an aldehyde + NADPH + H+ [RN:R07328]
ALL_REAC    R07328 > R00625 R00746 R01041 R05231;
            (other) R01036
SUBSTRATE   alcohol [CPD:C00069];
            NADP+ [CPD:C00006]
PRODUCT     aldehyde [CPD:C00071];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    Zinc [CPD:C00038]
COMMENT     A zinc protein. Some members of this group oxidize only primary
            alcohols; others act also on secondary alcohols. May be identical
            with EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate
            reductase (NADPH)] and EC 1.1.1.55 [lactaldehyde reductase (NADPH)].
            A-specific with respect to NADPH.
REFERENCE   1  [PMID:4402936]
  AUTHORS   Bosron WF, Prairie RL.
  TITLE     Triphosphopyridine nucleotide-linked aldehyde reductase. I.
            Purification and properties of the enzyme from pig kidney cortex.
  JOURNAL   J. Biol. Chem. 247 (1972) 4480-5.
  ORGANISM  pig [GN:ssc]
REFERENCE   2
  AUTHORS   DeMoss, R.
  TITLE     Triphosphopyridine nucleotide-specific ethanol dehydrogenase from
            Leuconostoc mesenteroides.
  JOURNAL   Bacteriol. Proc. (1953) 81.
  ORGANISM  Leuconostoc mesenteroides [GN:lme]
REFERENCE   3
  AUTHORS   Reeves, R.E., Montalvo, F.E. and Lushbaugh, T.S.
  TITLE     Nicotinamide-adenine dinucleotide phosphate-dependent alcohol
            dehydrogenase. Enzyme from Entamoeba histolytica and some enzyme
            inhibitors.
  JOURNAL   Int. J. Biochem. 2 (1971) 55-64.
  ORGANISM  Entamoeba histolytica [GN:ehi]
REFERENCE   4  [PMID:4393513]
  AUTHORS   Tabakoff B, Erwin VG.
  TITLE     Purification and characterization of a reduced nicotinamide adenine
            dinucleotide phosphate-linked aldehyde reductase from brain.
  JOURNAL   J. Biol. Chem. 245 (1970) 3263-8.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00561  Glycerolipid metabolism
            PATH: map00930  Caprolactam degradation
ORTHOLOGY   KO: K00002  alcohol dehydrogenase (NADP+)
GENES       HSA: 10327(AKR1A1)
            RNO: 78959(Akr1a1)
            CFA: 610537(LOC610537)
            SSC: 396924(ALR1)
            GGA: 424599(AKR1A1)
            DRE: 799805(akr1a1b)
            SPU: 587281(LOC587281)
            OSA: 4338987
            CME: CMM296C
            PIC: PICST_29079(ADH4) PICST_45137(ADH7)
            CGR: CAGL0H06853g CAGL0M14047g
            ANI: AN2860.2
            AFM: AFUA_1G09750 AFUA_3G11900 AFUA_6G10260
            AOR: AO090003000751 AO090023000460
            CNE: CNC05140 CNK02370
            UMA: UM01861.1
            TET: TTHERM_00274500
            TCR: 504339.19 504425.60 508677.80 509331.210
            LMA: LmjF23.0360
            EHI: 25.t00045 73.t00013 81.t00034
            XFA: XF1136 XF1727 XF1734
            XFT: PD0423(adhP)
            XCC: XCC0029(yahK)
            XCB: XC_0029
            XCV: XCV0034
            XAC: XAC0031(yahK)
            XOO: XOO0280(yahK)
            XOM: XOO_0252(XOO0252)
            PAE: PA2275
            PPU: PP_2426
            PST: PSPTO_2182 PSPTO_2697
            PSB: Psyr_1992 Psyr_2431
            PSP: PSPPH_1961 PSPPH_2589
            PFL: PFL_1816 PFL_2420
            PFO: Pfl_4120
            SHN: Shewana3_1694
            ILO: IL1440
            PAT: Patl_1426
            LPN: lpg0612
            LPF: lpl0647
            LPP: lpp0663
            NOC: Noc_0435
            ABO: ABO_2414(AKR1A1)
            CVI: CV_2051
            RSO: RS05494(RSp1124) RSc0632(RS01534)
            BMA: BMA3240
            BXE: Bxe_B1754
            BPS: BPSL0192(adhC)
            BPM: BURPS1710b_0372(adhC)
            BTE: BTH_I0152
            RFR: Rfer_2439
            MMS: mma_1872
            HPY: HP1104(cad)
            HPJ: jhp1030 jhp1429
            HPA: HPAG1_1042
            HHE: HH1166(cad)
            HAC: Hac_0437(adhA)
            CJE: Cj1548c
            CJR: CJE1719
            CJU: C8J_1447
            ABU: Abu_1042
            BBA: Bd0900(adhA)
            SME: SMc00680
            ATU: Atu2022(adh)
            ATC: AGR_C_3663A
            RET: RHE_CH02758(adh)
            RLE: RL3212
            RPE: RPE_2083
            MMR: Mmar10_2303
            GBE: GbCGDNIH1_2346
            ABA: Acid345_1946
            BSU: BG12562(adhA)
            BLI: BL05196(adhA)
            BLD: BLi02097(adhA)
            OIH: OB0786
            CBF: CLI_2960(adh)
            MPN: MPN564(adh)
            MPE: MYPE5230(adhA)
            MTU: Rv3045(adhC)
            MTC: MT3130(adh)
            MBO: Mb3071(adhC)
            MBB: BCG_3069(adhC)
            MLE: ML1730(adhA)
            MPA: MAP3093(adhC)
            MAV: MAV_3911
            MSM: MSMEG_1037 MSMEG_2317
            MMC: Mmcs_1836
            CGL: NCgl0324(cgl0331)
            CGB: cg0400(adhC)
            CEF: CE0149 CE0338
            CJK: jk2055(adhA)
            NFA: nfa52260
            RHA: RHA1_ro02119
            SCO: SCO4945(2SCK31.05)
            SMA: SAV3314(adhA4)
            AAU: AAur_2040
            PAC: PPA1072
            SEN: SACE_1843(adhA) SACE_2652
            LIL: LA3172
            LIC: LIC10949(dkgA)
            SYN: slr0942
            AVA: Ava_2489
            SRU: SRU_1267
            MAC: MA0403 MA1901(adh)
            MBA: Mbar_A0771
            MST: Msp_0967(adh)
            HMA: pNG7101(adh8)
            HWA: HQ1729A(adh)
STRUCTURES  PDB: 1AE4  1BXZ  1C9W  1CWN  1HQT  1JQB  1KEV  1NXQ  1P0C  1P0F  
                 1PED  1UJM  1Y1P  1Y9A  1YKF  1ZJY  1ZJZ  1ZK0  1ZK1  1ZK2  
                 1ZK3  1ZK4  1ZZE  2ALR  2AO0  2B83  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.2
            ExPASy - ENZYME nomenclature database: 1.1.1.2
            ExplorEnz - The Enzyme Database: 1.1.1.2
            ERGO genome analysis and discovery system: 1.1.1.2
            BRENDA, the Enzyme Database: 1.1.1.2
            CAS: 9028-12-0
///
ENTRY       EC 1.1.1.3                  Enzyme
NAME        homoserine dehydrogenase;
            HSDH;
            HSD
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-homoserine:NAD(P)+ oxidoreductase
REACTION    L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
            [RN:R01773 R01775]
ALL_REAC    R01773 R01775
SUBSTRATE   L-homoserine [CPD:C00263];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     L-aspartate 4-semialdehyde [CPD:C00441];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The yeast enzyme acts most rapidly with NAD+; the Neurospora enzyme
            with NADP+. The enzyme from Escherichia coli is a multi-functional
            protein, which also catalyses the reaction of EC 2.7.2.4 (aspartate
            kinase).
REFERENCE   1  [PMID:14353905]
  AUTHORS   BLACK S, WRIGHT NG.
  TITLE     Homoserine dehydrogenase.
  JOURNAL   J. Biol. Chem. 213 (1955) 51-60.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:4551091]
  AUTHORS   Starnes WL, Munk P, Maul SB, Cunningham GN, Cox DJ, Shive W.
  TITLE     Threonine-sensitive aspartokinase-homoserine dehydrogenase complex,
            amino acid composition, molecular weight, and subunit composition of
            the complex.
  JOURNAL   Biochemistry. 11 (1972) 677-87.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4562990]
  AUTHORS   Veron M, Falcoz-Kelly F, Cohen GN.
  TITLE     The threonine-sensitive homoserine dehydrogenase and aspartokinase
            activities of Escherichia coli K12. The two catalytic activities are
            carried by two independent regions of the polypeptide chain.
  JOURNAL   Eur. J. Biochem. 28 (1972) 520-7.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K00003  homoserine dehydrogenase
GENES       ATH: AT1G31230(AK-HSDH_I)
            OSA: 4346642
            CME: CMN129C
            SCE: YJR139C(HOM6)
            AGO: AGOS_ABL080W
            PIC: PICST_57619(HOM6)
            CGR: CAGL0M00330g
            SPO: SPBC776.03
            ANI: AN2882.2
            AFM: AFUA_3G11640
            AOR: AO090003000721 AO090009000136
            CNE: CNJ02040
            LMA: LmjF07.0260
            ECO: b0002(thrA) b3940(metL)
            ECJ: JW0001(thrA) JW3911(metL)
            ECE: Z0002(thrA) Z5495(metL)
            ECS: ECs0002 ECs4869
            ECC: c0003(thrA) c4893(metL)
            ECI: UTI89_C0002(thrA) UTI89_C4525(metL)
            ECP: ECP_0002
            ECV: APECO1_1976(thrA) APECO1_2531(metL)
            ECW: EcE24377A_0001(thrA) EcE24377A_4480(metL)
            ECX: EcHS_A0003(thrA) EcHS_A4174
            STY: STY0002(thrA) STY3768(metL)
            STT: t0002(thrA) t3517(metL)
            SPT: SPA0002(thrA) SPA3944(metL)
            SEC: SC0002(thrA) SC3992(metL)
            STM: STM0002(thrA) STM4101(metL)
            YPE: YPO0116(metL) YPO0459(thrA)
            YPK: y0303(metL) y3718(thrA)
            YPM: YP_0118(metL) YP_3723(thrA)
            YPA: YPA_0265 YPA_4051
            YPN: YPN_0331 YPN_3738
            YPP: YPDSF_3174 YPDSF_3791
            YPS: YPTB0106(metM) YPTB0602(thrA)
            YPI: YpsIP31758_0122(metL) YpsIP31758_3476(thrA)
            SFL: SF0002(thrA) SF4018(metL)
            SFX: S0002(thrA) S3729(metL)
            SFV: SFV_0001(thrA) SFV_4010(metL)
            SSN: SSON_0002(thrA) SSON_4114(metL)
            SBO: SBO_0001(thrA) SBO_3960(metL)
            SDY: SDY_0002(thrA) SDY_3775(metL)
            ECA: ECA3891(thrA) ECA4251(metL)
            PLU: plu0563(thrA) plu4755(metL)
            BUC: BU194(thrA)
            BAS: BUsg188(thrA)
            BAB: bbp183(thrA)
            BCC: BCc_127(thrA)
            WBR: WGLp591(thrA)
            SGL: SG0404
            ENT: Ent638_0564 Ent638_4034
            SPE: Spro_0683 Spro_4785
            BFL: Bfl111(thrA)
            BPN: BPEN_115(thrA)
            HIT: NTHI0167(thrA)
            HSO: HS_1214(thrA)
            PMU: PM0113(thrA)
            MSU: MS1703(lysC)
            APL: APL_0250(thrA)
            ASU: Asuc_0801
            XFA: XF2225
            XFT: PD1273(lysC)
            XCC: XCC1800(metL) XCC2855
            XCB: XC_1253 XC_2389
            XCV: XCV1866(thrA) XCV3175(metL)
            XAC: XAC1820(metL) XAC3038
            XOO: XOO2242(metL)
            XOM: XOO_1718(XOO1718) XOO_2107(XOO2107)
            VCH: VC2364 VC2684
            VVU: VV1_0545 VV1_1365
            VVY: VV0650 VV3007
            VPA: VP0494 VP2764
            VFI: VF2118(thrA) VF2266(metL)
            PPR: PBPRA0262 PBPRA0552
            PAE: PA3736(hom)
            PAU: PA14_16070(hom)
            PPU: PP_0664 PP_1470(hom)
            PPF: Pput_0698 Pput_4251
            PST: PSPTO_1480(hom)
            PSB: Psyr_1290
            PSP: PSPPH_1360(hom)
            PFL: PFL_1103(hom) PFL_3809(hom)
            PFO: Pfl_1027
            PEN: PSEEN4252(hom)
            PMY: Pmen_2012 Pmen_3394
            PAR: Psyc_0253(hom)
            PCR: Pcryo_0279
            PRW: PsycPRwf_2010
            ACI: ACIAD0264(hom)
            SON: SO_3415(thrA) SO_4055(metL)
            SDN: Sden_0616 Sden_2740
            SFR: Sfri_2906 Sfri_3550
            SAZ: Sama_0905 Sama_3170
            SBL: Sbal_1227 Sbal_3775
            SBM: Shew185_0537 Shew185_1271
            SLO: Shew_0521 Shew_1079
            SPC: Sputcn32_0617 Sputcn32_2735
            SSE: Ssed_1175 Ssed_4040
            SPL: Spea_0561 Spea_1066
            SHE: Shewmr4_1138 Shewmr4_3438
            SHM: Shewmr7_0513 Shewmr7_1209
            SHN: Shewana3_1139 Shewana3_3613
            SHW: Sputw3181_1277 Sputw3181_3553
            ILO: IL2466(metL)
            CPS: CPS_0456(metL) CPS_4291(thrA)
            PHA: PSHAa2379(thrA) PSHAa2722(metL)
            PAT: Patl_3580
            SDE: Sde_1209
            PIN: Ping_1275
            MAQ: Maqu_2274
            MCA: MCA0597(hom)
            FTW: FTW_1648
            FTA: FTA_0521
            FTN: FTN_0525(thrA)
            TCX: Tcr_1251
            NOC: Noc_2454
            AEH: Mlg_1822
            HHA: Hhal_0125
            HCH: HCH_01779(thrA)
            CSA: Csal_3010
            ABO: ABO_0806(hom)
            MMW: Mmwyl1_3765
            AHA: AHA_0590 AHA_3018
            CRP: CRP_121
            RMA: Rmag_0769
            VOK: COSY_0706(thrA)
            NME: NMB1228
            NMA: NMA1395(hom)
            NMC: NMC1128(hom)
            NGO: NGO0779
            CVI: CV_0996(metL)
            RSO: RSc1327(RS02849)
            REU: Reut_A1993
            REH: H16_A2266(thrA)
            RME: Rmet_1966
            BMA: BMA1385(hom)
            BMV: BMASAVP1_A1875(hom)
            BML: BMA10299_A0022(hom)
            BMN: BMA10247_1147(hom)
            BXE: Bxe_A2381
            BVI: Bcep1808_1781
            BUR: Bcep18194_A5155
            BCN: Bcen_6225
            BCH: Bcen2424_1854
            BAM: Bamb_1792 Bamb_4289
            BPS: BPSL1477(hom)
            BPM: BURPS1710b_2396(hom)
            BPL: BURPS1106A_2270(hom)
            BPD: BURPS668_2232(hom)
            PNU: Pnuc_0438
            BPE: BP2784
            BPA: BPP2479
            BBR: BB1926
            RFR: Rfer_1912
            POL: Bpro_2190 Bpro_5333
            PNA: Pnap_2231
            AAV: Aave_0011 Aave_1238
            AJS: Ajs_3206 Ajs_4155
            VEI: Veis_2663
            MPT: Mpe_A1541
            HAR: HEAR2150(hom)
            MMS: mma_1312(thrA)
            NEU: NE2369
            NET: Neut_0865
            NMU: Nmul_A1551
            EBA: ebA4952(thrA)
            AZO: azo2081(hom)
            DAR: Daro_2386
            TBD: Tbd_0843
            MFA: Mfla_0904 Mfla_1048
            HPY: HP0822
            HPA: HPAG1_0808
            HHE: HH1750(hom)
            HAC: Hac_0726(hom)
            WSU: WS0450(HOM)
            TDN: Tmden_1904
            CJE: Cj0149c(hom)
            CJR: CJE0145(hom)
            CJJ: CJJ81176_0185(hom)
            CJU: C8J_0146(hom)
            CJD: JJD26997_0164(hom)
            CFF: CFF8240_0293
            CCV: CCV52592_0834
            CHA: CHAB381_0217
            CCO: CCC13826_1144
            ABU: Abu_0158(hom)
            NIS: NIS_1553
            SUN: SUN_0225
            GSU: GSU1693(hom)
            GME: Gmet_1629
            GUR: Gura_2178
            PCA: Pcar_1451
            PPD: Ppro_1294
            DVU: DVU0890(hom)
            DVL: Dvul_2094
            DDE: Dde_2731
            DPS: DP1732
            ADE: Adeh_1400 Adeh_1638 Adeh_3931
            AFW: Anae109_2173 Anae109_2430
            MXA: MXAN_0971 MXAN_2278
            SAT: SYN_00890
            SFU: Sfum_1218
            PUB: SAR11_0852 SAR11_1025(hom)
            MLO: mll0934
            MES: Meso_1922
            PLA: Plav_2946
            SME: SMc00293(thrA)
            SMD: Smed_1453
            ATU: Atu1588(hom)
            ATC: AGR_C_2919
            RET: RHE_CH01878(thrA)
            RLE: RL2097(hom) pRL80071(hom)
            BME: BMEI0725
            BMF: BAB1_1293
            BMS: BR1274(hom)
            BMB: BruAb1_1275(hom)
            BOV: BOV_1237(hom)
            OAN: Oant_1917
            BJA: blr4362(hom)
            BRA: BRADO3572(hom)
            BBT: BBta_3996(hom)
            RPA: RPA2504(HDH)
            RPB: RPB_2966
            RPC: RPC_2816
            RPD: RPD_2495
            RPE: RPE_2937
            NWI: Nwi_1647
            NHA: Nham_2309
            BHE: BH10030(metM)
            XAU: Xaut_3521
            CCR: CC_1383
            SIL: SPO1734(hom)
            SIT: TM1040_2164
            RSP: RSP_0403
            RSH: Rsph17029_2057
            RSQ: Rsph17025_0834
            JAN: Jann_2998
            RDE: RD1_2538(hom)
            PDE: Pden_3678
            MMR: Mmar10_1098 Mmar10_2618
            HNE: HNE_2310(hom)
            ZMO: ZMO0483(hom)
            NAR: Saro_0019
            SAL: Sala_0810
            SWI: Swit_4731
            ELI: ELI_13775
            GOX: GOX1517
            ACR: Acry_1298
            RRU: Rru_A2410
            MAG: amb3728
            MGM: Mmc1_1756
            ABA: Acid345_1481 Acid345_4165
            SUS: Acid_0526 Acid_7030
            BSU: BG10460(hom)
            BHA: BH1253 BH1737 BH3422(hom)
            BAN: BA1968(hom-1) BA2608 BA5654(hom-2)
            BAR: GBAA1968(hom-1) GBAA2608 GBAA5654(hom-2)
            BAA: BA_0512 BA_2468 BA_3119
            BAT: BAS1825 BAS2433 BAS5256
            BCE: BC1964 BC2548 BC5404
            BCA: BCE_2051(hom) BCE_2626 BCE_5533(hom)
            BCZ: BCZK1782(hom) BCZK2354(hom) BCZK5102(hom)
            BCY: Bcer98_1496 Bcer98_3923
            BTK: BT9727_1799(hom) BT9727_2388(hom) BT9727_5085(hom)
            BTL: BALH_1741(hom) BALH_2348(hom) BALH_4905(hom)
            BLI: BL02137(hom)
            BLD: BLi03414(hom)
            BCL: ABC0023 ABC1578 ABC2942(hom)
            BAY: RBAM_029370(hom)
            BPU: BPUM_1429 BPUM_2888(thrA)
            OIH: OB0466
            GKA: GK2964
            SAU: SA1164(dhoM)
            SAV: SAV1328(dhoM)
            SAM: MW1215(dhoM)
            SAR: SAR1338
            SAS: SAS1268
            SAC: SACOL1362(hom)
            SAB: SAB1186
            SAA: SAUSA300_1226
            SAO: SAOUHSC_01320
            SAJ: SaurJH9_1389
            SAH: SaurJH1_1416
            SEP: SE1009
            SER: SERP0897(hom)
            SHA: SH1579(dhoM)
            SSP: SSP1438
            LMO: lmo2547(hom)
            LMF: LMOf2365_2520(hom)
            LIN: lin2691(hom)
            LWE: lwe2496(hom)
            LLA: L0090(hom)
            LLC: LACR_1280
            LLM: llmg_1332(hom)
            SPN: SP_1361
            SPR: spr1219(hom)
            SPD: SPD_1195(hom)
            SAG: SAG1120(hom)
            SAN: gbs1187
            SAK: SAK_1205(hom)
            SMU: SMU.965
            STC: str0469(hom)
            STL: stu0469(hom)
            SSA: SSA_1043(hom)
            SGO: SGO_0801(hom)
            LPL: lp_0571(hom2) lp_2535(hom1)
            LAC: LBA1212
            LSL: LSL_1519(thrA)
            LDB: Ldb1350
            LBU: LBUL_1259
            LCA: LSEI_2151
            EFA: EF2422(hom)
            OOE: OEOE_1546
            STH: STH2739
            CAC: CAC0998
            CTC: CTC00886 CTC02355
            CNO: NT01CX_0896
            CTH: Cthe_0290 Cthe_1376
            CDF: CD1166(hom1) CD1580(hom2)
            CBO: CBO1641(hom) CBO1875(hom)
            CBA: CLB_1658(hom-1) CLB_1812(hom-2)
            CBH: CLC_1667(hom-1) CLC_1819(hom-2)
            CBF: CLI_1718(hom-1) CLI_1939(hom-2)
            CBE: Cbei_1551
            CKL: CKL_0859(hom1) CKL_1105(hom2)
            AMT: Amet_0566
            CHY: CHY_1912(hom)
            DSY: DSY1363
            DRM: Dred_1165
            SWO: Swol_1319
            CSC: Csac_0993
            TTE: TTE2620(thrA2)
            MTA: Moth_1307
            MTU: Rv1294(thrA)
            MTC: MT1333(thrA)
            MBO: Mb1326(thrA)
            MBB: BCG_1354(thrA)
            MLE: ML1129(hom)
            MPA: MAP2468c(thrA)
            MAV: MAV_1509
            MSM: MSMEG_4957
            MVA: Mvan_4348
            MGI: Mflv_2298
            MMC: Mmcs_3896
            MKM: Mkms_3970
            MJL: Mjls_3882
            CGL: NCgl1136(cgl1183)
            CGB: cg1337(hom)
            CEF: CE1289
            CDI: DIP1036(thrA)
            CJK: jk1352(hom)
            NFA: nfa10490(thrA)
            RHA: RHA1_ro01488(thrA)
            SCO: SCO5354(SCBAC5H2.23)
            SMA: SAV2918(thrA)
            TWH: TWT439(thrA)
            TWS: TW329(hom)
            LXX: Lxx06870(thrA)
            ART: Arth_2623 Arth_3560
            AAU: AAur_2612(thrA)
            PAC: PPA1258
            NCA: Noca_1744
            TFU: Tfu_2424
            FRA: Francci3_3725
            FAL: FRAAL5951(hom)
            ACE: Acel_0630
            KRA: Krad_1252
            SEN: SACE_6298(thrA)
            STP: Strop_3651
            BLO: BL1274(thrA)
            BAD: BAD_1416(thrA)
            RXY: Rxyl_1091
            RBA: RB8510(hom)
            LIL: LA3638(thrA)
            LIC: LIC10571(hom)
            LBJ: LBJ_2852(thrA)
            LBL: LBL_0219(thrA)
            SYN: sll0455(thrA)
            SYW: SYNW0711(thrA)
            SYC: syc2003_c(thrA)
            SYF: Synpcc7942_2090
            SYD: Syncc9605_1957
            SYE: Syncc9902_0704
            SYG: sync_0941(hom)
            SYR: SynRCC307_0723(thrA)
            SYX: SynWH7803_1606(thrA)
            CYA: CYA_1100(hom)
            CYB: CYB_1425(hom)
            TEL: tll0277(thrA)
            GVI: gll4295(thrA)
            ANA: all4120(thrA)
            AVA: Ava_0783
            PMA: Pro1150(thrA)
            PMM: PMM1051(thrA)
            PMT: PMT1143(thrA)
            PMN: PMN2A_0702
            PMI: PMT9312_1062
            PMB: A9601_11561(thrA)
            PMC: P9515_11421(thrA)
            PMF: P9303_08881(thrA)
            PMG: P9301_11571(thrA)
            PME: NATL1_15361(thrA)
            TER: Tery_4567
            BTH: BT_2403
            BFR: BF0608
            BFS: BF0558(thrA)
            SRU: SRU_0482 SRU_0691
            CHU: CHU_0073(thrA)
            GFO: GFO_0318(hom) GFO_1970(thrA)
            FJO: Fjoh_1492 Fjoh_1494 Fjoh_2575
            FPS: FP0255
            CTE: CT2030
            CCH: Cag_0142
            CPH: Cpha266_2542
            PVI: Cvib_1626
            PLT: Plut_1983
            DET: DET1206(metM)
            DEH: cbdb_A1123(metM)
            DEB: DehaBAV1_1016
            RRS: RoseRS_1971 RoseRS_2987
            RCA: Rcas_1559 Rcas_2086
            DRA: DR_1278
            DGE: Dgeo_0610
            TTH: TTC0115
            TTJ: TTHA0489
            AAE: aq_1812(thrA)
            TMA: TM0547
            MMP: MMP1702(hom)
            MMQ: MmarC5_1704
            MMZ: MmarC7_0977
            MAE: Maeo_1209
            MVN: Mevan_1004
            MAC: MA2572
            MBA: Mbar_A1898
            MMA: MM_2713
            MBU: Mbur_1087
            MTP: Mthe_0845
            MHU: Mhun_2292
            MEM: Memar_0971
            MBN: Mboo_1354
            MST: Msp_0487
            MSI: Msm_0154
            MKA: MK1554(thrA)
            HAL: VNG2650G(hom)
            HMA: rrnAC2408(hom)
            HWA: HQ3386A(hom)
            NPH: NP0302A(hom)
            TAC: Ta1179
            TVO: TVN0385
            PTO: PTO1417
            PAB: PAB0610(hom)
            PFU: PF1104
            TKO: TK1627
            RCI: LRC427(thrA)
            APE: APE_1144.1
            HBU: Hbut_0312
            SSO: SSO0657(thrA)
            STO: ST1519
            SAI: Saci_1636(hdh)
            MSE: Msed_2003
            PAI: PAE2868
            PIS: Pisl_0271
            PCL: Pcal_0379
            PAS: Pars_0949
STRUCTURES  PDB: 1EBF  1EBU  1Q7G  1TVE  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.3
            ExPASy - ENZYME nomenclature database: 1.1.1.3
            ExplorEnz - The Enzyme Database: 1.1.1.3
            ERGO genome analysis and discovery system: 1.1.1.3
            BRENDA, the Enzyme Database: 1.1.1.3
            CAS: 9028-13-1
///
ENTRY       EC 1.1.1.4                  Enzyme
NAME        (R,R)-butanediol dehydrogenase;
            butyleneglycol dehydrogenase;
            D-butanediol dehydrogenase;
            D-(-)-butanediol dehydrogenase;
            butylene glycol dehydrogenase;
            diacetyl (acetoin) reductase;
            D-aminopropanol dehydrogenase;
            D-aminopropanol dehydrogenase;
            1-amino-2-propanol dehydrogenase;
            2,3-butanediol dehydrogenase;
            D-1-amino-2-propanol dehydrogenase;
            (R)-diacetyl reductase;
            (R)-2,3-butanediol dehydrogenase;
            D-1-amino-2-propanol:NAD+ oxidoreductase;
            1-amino-2-propanol oxidoreductase;
            aminopropanol oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R,R)-butane-2,3-diol:NAD+ oxidoreductase
REACTION    (R,R)-butane-2,3-diol + NAD+ = (R)-acetoin + NADH + H+ [RN:R02946]
ALL_REAC    R02946
SUBSTRATE   (R,R)-butane-2,3-diol [CPD:C03044];
            NAD+ [CPD:C00003]
PRODUCT     (R)-acetoin [CPD:C00810];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also converts diacetyl into acetoin with NADH as reductant.
REFERENCE   1
  AUTHORS   Strecker, H.J. and Harary, I.
  TITLE     Bacterial butylene glycol dehydrogenase and diacetyl reductase.
  JOURNAL   J. Biol. Chem. 211 (1954) 263-270.
  ORGANISM  Aerobacter aerogenes, Staphylococcus aureus
REFERENCE   2
  AUTHORS   Taylor, M.B. and Juni, E.
  TITLE     Stereoisomeric specificities of 2,3-butanediol dehydrogenase.
  JOURNAL   Biochim. Biophys. Acta 39 (1960) 448-457.
  ORGANISM  Bacillus polymyxa, Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K00004  (R,R)-butanediol dehydrogenase
GENES       ATH: AT5G06580
            PIC: PICST_74116(SOR5) PICST_89701(SOR1)
            CGR: CAGL0D00198g
            AFM: AFUA_2G15930
            ACI: ACIAD1021
            NMC: NMC0547
            SME: SMc01455(dld)
            ATU: Atu2053
            ATC: AGR_C_3718
            BCE: BC0668
            BCA: BCE_3248(gutB)
            LLC: LACR_0974
            LLM: llmg_1642(butB)
            SPZ: M5005_Spy_0534
            SPH: MGAS10270_Spy0529
            SPI: MGAS10750_Spy0553
            SPJ: MGAS2096_Spy0546
            SPK: MGAS9429_Spy0525
            SPA: M6_Spy0555
            SSA: SSA_0572
            CNO: NT01CX_0344
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.4
            ExPASy - ENZYME nomenclature database: 1.1.1.4
            ExplorEnz - The Enzyme Database: 1.1.1.4
            ERGO genome analysis and discovery system: 1.1.1.4
            BRENDA, the Enzyme Database: 1.1.1.4
            CAS: 37250-09-2
///
ENTRY       EC 1.1.1.5                  Enzyme
NAME        acetoin dehydrogenase;
            diacetyl reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     acetoin:NAD+ oxidoreductase
REACTION    acetoin + NAD+ = diacetyl + NADH + H+ [RN:R02343]
ALL_REAC    R02343 > R02855;
            (other) R02856
SUBSTRATE   acetoin [CPD:C00466];
            NAD+ [CPD:C00003]
PRODUCT     diacetyl [CPD:C00741];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     NADP+ also acts as acceptor.
REFERENCE   1  [PMID:4152609]
  AUTHORS   Diez V, Burgos J, Martin R.
  TITLE     Pigeon liver diacetyl reductase: purification and some properties.
  JOURNAL   Biochim. Biophys. Acta. 350 (1974) 253-62.
  ORGANISM  pigeon
REFERENCE   2
  AUTHORS   Strecker, H.J. and Harary, I.
  TITLE     Bacterial butylene glycol dehydrogenase and diacetyl reductase.
  JOURNAL   J. Biol. Chem. 211 (1954) 263-270.
  ORGANISM  Aerobacter aerogenes, Staphylococcus aureus
PATHWAY     PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K03366  acetoin dehydrogenase
GENES       RNO: 171408(Dcxr)
            ECA: ECA0310(budC)
            ACI: ACIAD1022(budC)
            SFR: Sfri_0232
            ILO: IL0792
            NOC: Noc_0093
            BUR: Bcep18194_B2443
            AZO: azo1539(acoA1) azo3867(acoA2)
            PCA: Pcar_0903 Pcar_2068
            RET: RHE_CH02403
            RLE: RL2725
            GOX: GOX2036
            BLD: BLi02066
            BCL: ABC0681
            BPU: BPUM_2617 BPUM_2618 BPUM_2619
            SAU: SA0122(butA)
            SAV: SAV0126(butA)
            SAM: MW0100(butA)
            SAR: SAR0129
            SAS: SAS0101
            SAC: SACOL0111
            SAB: SAB0066
            SAA: SAUSA300_0129
            SAO: SAOUHSC_00086
            SEP: SE0197 SE2225
            SER: SERP2257 SERP2379
            LLA: L118271(butA)
            LLC: LACR_0363 LACR_0974
            LLM: llmg_0339(dar) llmg_1641(butA)
            SPZ: M5005_Spy_0534 M5005_Spy_0535
            SPH: MGAS10270_Spy0529
            SPI: MGAS10750_Spy0553
            SPJ: MGAS2096_Spy0546
            SPK: MGAS9429_Spy0525
            SPF: SpyM51329
            SPA: M6_Spy0555
            SPB: M28_Spy0513
            SAK: SAK_0674
            SMU: SMU.1322(budC)
            SGO: SGO_1096(butA) SGO_1132 SGO_1133(acoA)
            LSA: LSA0292(budC)
            LBR: LVIS_0187
            OOE: OEOE_0077
            MSM: MSMEG_5020
            CGL: NCgl2582(cgl2674)
            CGB: cg2958(butA)
            RHA: RHA1_ro04205(fadB1) RHA1_ro05279
            SEN: SACE_3985
STRUCTURES  PDB: 1GEG  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.5
            ExPASy - ENZYME nomenclature database: 1.1.1.5
            ExplorEnz - The Enzyme Database: 1.1.1.5
            ERGO genome analysis and discovery system: 1.1.1.5
            BRENDA, the Enzyme Database: 1.1.1.5
            CAS: 9028-49-3
///
ENTRY       EC 1.1.1.6                  Enzyme
NAME        glycerol dehydrogenase;
            glycerin dehydrogenase;
            NAD+-linked glycerol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     glycerol:NAD+ 2-oxidoreductase
REACTION    glycerol + NAD+ = glycerone + NADH + H+ [RN:R01034]
ALL_REAC    R01034
SUBSTRATE   glycerol [CPD:C00116];
            NAD+ [CPD:C00003]
PRODUCT     glycerone [CPD:C00184];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts on propane-1,2-diol.
REFERENCE   1  [PMID:13069498]
  AUTHORS   ASNIS RE, BRODIE AF.
  TITLE     A glycerol dehydrogenase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 203 (1953) 153-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Burton, R.M. and Kaplan, N.O.
  TITLE     A DPN specific glycerol dehydrogenase from Aerobacter aerogenes.
  JOURNAL   J. Am. Chem. Soc. 75 (1953) 1005-1007.
  ORGANISM  Aerobacter aerogenes
REFERENCE   3
  AUTHORS   Lin, E.C.C. and Magasanik, B.
  TITLE     The activation of glycerol dehydrogenase from Aerobacter aerogenes
            by monovalent cations.
  JOURNAL   J. Biol. Chem. 235 (1960) 1820-1823.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00561  Glycerolipid metabolism
ORTHOLOGY   KO: K00005  glycerol dehydrogenase
GENES       SPO: SPAC13F5.03c
            DDI: DDBDRAFT_0217165
            ECO: b3945(gldA)
            ECJ: JW5556(gldA)
            ECE: Z5500(gldA)
            ECS: ECs4874
            ECC: c4904(gldA)
            ECI: UTI89_C4536(gldA) UTI89_C5025(cgrD)
            ECP: ECP_4159
            ECV: APECO1_2102(cglD) APECO1_2521(gldA)
            ECW: EcE24377A_4485(gldA)
            ECX: EcHS_A4180(gldA)
            STY: STY3759(gldA)
            STT: t3509(gldA)
            SPT: SPA3953(gldA)
            SEC: SC3460(gldA) SC4000(gldA)
            STM: STM3529 STM4108(gldA)
            YPP: YPDSF_1420
            YEN: YE0539(gldA)
            SSN: SSON_4119(gldA)
            SBO: SBO_3965(gldA)
            SDY: SDY_3780(gldA)
            ECA: ECA0846(gldA) ECA1523
            PLU: plu4115(gldA)
            VVY: VV0158
            VPA: VP0363(gldH)
            AHA: AHA_2415 AHA_4005(gldA)
            REU: Reut_B4570
            SFU: Sfum_0519
            SME: SMc02038(gldA)
            BLI: BL03089
            BLD: BLi00828(gldA)
            BCL: ABC0560(gldA) ABC0879
            BAY: RBAM_005990
            BPU: BPUM_0204(gldA)
            OIH: OB0323(gldA) OB3328
            SEP: SE0235
            SER: SERP2346(gldA)
            SPY: SPy_2047(gldA)
            SPZ: M5005_Spy_1741(gldA)
            SPM: spyM18_2108(gldA)
            SPG: SpyM3_1747(gldA)
            SPS: SPs1745
            SPH: MGAS10270_Spy1810(gldA)
            SPI: MGAS10750_Spy1835(gldA)
            SPJ: MGAS2096_Spy1775(gldA)
            SPK: MGAS9429_Spy1750(gldA)
            SPF: SpyM51704(gldA)
            SPA: M6_Spy1741(gldA)
            SPB: M28_Spy1728(gldA)
            SPN: SP_0253
            SPR: spr0234(gldA)
            SPD: SPD_0237(gldA)
            SAG: SAG0333(gldA) SAG2046
            SAN: gbs0321 gbs2002
            SAK: SAK_0403(gldA) SAK_1985
            SMU: SMU.1309c SMU.495(gldA)
            SSA: SSA_0287(gldA)
            SGO: SGO_1786(gldA)
            LSL: LSL_0028(gldA)
            LBR: LVIS_2165
            EFA: EF1358
            STH: STH1267
            CPE: CPE0099(gldA)
            CPF: CPF_0094(gldA)
            CTC: CTC00596(gldA)
            CNO: NT01CX_0287 NT01CX_1239
            CBO: CBO0976(gldA1) CBO1999(gldA2)
            CBA: CLB_1016(dhaD) CLB_1939
            CBH: CLC_1030(dhaD) CLC_1945
            CBF: CLI_1062(dhaD) CLI_2065
            MTA: Moth_0464
            CDI: DIP1893
            TFU: Tfu_2801
            SYN: slr1167(gldA)
            SYW: SYNW0939
            SYC: syc1815_d(gldA) syc2433_d(gldA)
            SYF: Synpcc7942_1653 Synpcc7942_2285
            SYD: Syncc9605_1626
            SYE: Syncc9902_1388
            SYG: sync_0649 sync_1026
            SYR: SynRCC307_0551(gldH)
            SYX: SynWH7803_1536(gldA)
            TEL: tll2051(gldA)
            GVI: gll1456
            ANA: alr2764
            AVA: Ava_0016
            PMA: Pro1108(gldA)
            PMM: PMM1087(gldA)
            PMT: PMT1062(gldA)
            PMN: PMN2A_0661
            PMI: PMT9312_1098
            PMB: A9601_11931(gldA)
            PMC: P9515_11781(gldA)
            PMF: P9303_09901(gldA)
            PMG: P9301_11941(gldA)
            PMH: P9215_12231(gldA)
            PME: NATL1_14931(gldA)
            TER: Tery_1022
            SRU: SRU_1614(gldA)
            TMA: TM0423
            HAL: VNG6270G(gldA)
            HMA: rrnAC0175(gldA)
STRUCTURES  PDB: 1JPU  1JQ5  1JQA  1TA9  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.6
            ExPASy - ENZYME nomenclature database: 1.1.1.6
            ExplorEnz - The Enzyme Database: 1.1.1.6
            ERGO genome analysis and discovery system: 1.1.1.6
            BRENDA, the Enzyme Database: 1.1.1.6
            CAS: 9028-14-2
///
ENTRY       EC 1.1.1.7                  Enzyme
NAME        propanediol-phosphate dehydrogenase;
            PDP dehydrogenase;
            1,2-propanediol-1-phosphate:NAD+ oxidoreductase;
            propanediol phosphate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     propane-1,2-diol-1-phosphate:NAD+ oxidoreductase
REACTION    propane-1,2-diol 1-phosphate + NAD+ = hydroxyacetone phosphate +
            NADH + H+ [RN:R04236]
ALL_REAC    R04236
SUBSTRATE   propane-1,2-diol 1-phosphate [CPD:C03894];
            NAD+ [CPD:C00003]
PRODUCT     hydroxyacetone phosphate [CPD:C03505];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Sellinger, O.Z. and Miller, O.N.
  TITLE     The metabolism of acetol phosphate. II. 1,2-Propanediol-1-phosphate
            dehydrogenase.
  JOURNAL   J. Biol. Chem. 234 (1959) 1641-1646.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.7
            ExPASy - ENZYME nomenclature database: 1.1.1.7
            ExplorEnz - The Enzyme Database: 1.1.1.7
            ERGO genome analysis and discovery system: 1.1.1.7
            BRENDA, the Enzyme Database: 1.1.1.7
            CAS: 9028-15-3
///
ENTRY       EC 1.1.1.8                  Enzyme
NAME        glycerol-3-phosphate dehydrogenase (NAD+);
            alpha-glycerol phosphate dehydrogenase (NAD+);
            alpha-glycerophosphate dehydrogenase (NAD+);
            glycerol 1-phosphate dehydrogenase;
            glycerol phosphate dehydrogenase (NAD+);
            glycerophosphate dehydrogenase (NAD+);
            hydroglycerophosphate dehydrogenase;
            L-alpha-glycerol phosphate dehydrogenase;
            L-alpha-glycerophosphate dehydrogenase;
            L-glycerol phosphate dehydrogenase;
            L-glycerophosphate dehydrogenase;
            NAD+-alpha-glycerophosphate dehydrogenase;
            NAD+-dependent glycerol phosphate dehydrogenase;
            NAD+-dependent glycerol-3-phosphate dehydrogenase;
            NAD+-L-glycerol-3-phosphate dehydrogenase;
            NAD+-linked glycerol 3-phosphate dehydrogenase;
            NADH-dihydroxyacetone phosphate reductase;
            glycerol-3-phosphate dehydrogenase (NAD+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     sn-glycerol-3-phosphate:NAD+ 2-oxidoreductase
REACTION    sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
            [RN:R00842]
ALL_REAC    R00842
SUBSTRATE   sn-glycerol 3-phosphate [CPD:C00093];
            NAD+ [CPD:C00003]
PRODUCT     glycerone phosphate [CPD:C00111];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts on propane-1,2-diol phosphate and glycerone sulfate (but
            with a much lower affinity).
REFERENCE   1
  AUTHORS   Baranowski, T.
  TITLE     alpha-Glycerophosphate dehydrogenase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 85-96.
REFERENCE   2  [PMID:4307630]
  AUTHORS   Brosemer RW, Kuhn RW.
  TITLE     Comparative structural properties of honeybee and rabbit
            alpha-glycerophosphate dehydrogenases.
  JOURNAL   Biochemistry. 8 (1969) 2095-105.
  ORGANISM  Apis mellifera [GN:dame], rabbit
REFERENCE   3  [PMID:4340553]
  AUTHORS   O'Brien SJ, MacIntyre RJ.
  TITLE     The  -glycerophosphate cycle in Drosophila melanogaster. I.
            Biochemical and developmental aspects.
  JOURNAL   Biochem. Genet. 7 (1972) 141-61.
  ORGANISM  Drosophila melanogaster [GN:dme]
REFERENCE   4  [PMID:4200180]
  AUTHORS   Warkentin DL, Fondy TP.
  TITLE     Isolation and characterization of cytoplasmic L-glycerol-3-phosphate
            dehydrogenase from rabbit-renal-adipose tissue and its comparison
            with the skeletal-muscle enzyme.
  JOURNAL   Eur. J. Biochem. 36 (1973) 97-109.
  ORGANISM  rabbit
REFERENCE   5  [PMID:1499720]
  AUTHORS   Albertyn J, van Tonder A, Prior BA.
  TITLE     Purification and characterization of glycerol-3-phosphate
            dehydrogenase of Saccharomyces cerevisiae.
  JOURNAL   FEBS. Lett. 308 (1992) 130-2.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   6  [PMID:7671141]
  AUTHORS   Koekemoer TC, Litthauer D, Oelofsen W.
  TITLE     Isolation and characterization of adipose tissue
            glycerol-3-phosphate dehydrogenase.
  JOURNAL   Int. J. Biochem. Cell. Biol. 27 (1995) 625-32.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00006  glycerol-3-phosphate dehydrogenase (NAD+)
GENES       HSA: 2819(GPD1)
            MMU: 14555(Gpd1)
            RNO: 60666(Gpd1)
            CFA: 607942(GPD1)
            GGA: 420664(GPD1L)
            XLA: 399227(Gpd1)
            XTR: 448519(gpd1l)
            DME: Dmel_CG3215 Dmel_CG9042(Gpdh)
            CEL: F47G4.3(gpdh-1) K11H3.1(gpdh-2)
            ATH: AT5G40610
            OSA: 4323847
            CME: CMD113C
            SCE: YDL022W(GPD1) YOL059W(GPD2)
            AGO: AGOS_ADR311C
            PIC: PICST_83071(GPD2) PICST_90446(GPD1)
            CGR: CAGL0C05137g CAGL0K01683g
            SPO: SPAC23D3.04c SPBC215.05(gpd1)
            ANI: AN0351.2 AN6792.2
            AFM: AFUA_1G02150 AFUA_2G08250
            AOR: AO090005000883 AO090011000879
            CNE: CNC02480
            ECU: ECU05_0270
            PFA: PF11_0157 PFL0780w
            CPV: cgd2_210
            CHO: Chro.20028
            TAN: TA21330
            TPV: TP01_0302
            TBR: Tb927.8.3530
            LMA: LmjF10.0510
            VCO: VC0395_A2226(gpsA)
            NMC: NMC2041(gpsA)
            WOL: WD0731(gpsA)
            PUB: SAR11_1295(gpsA)
            BBK: BARBAKC583_1191(gpsA)
            BAY: RBAM_020990(gpsA)
            SAC: SACOL1514(gpsA)
            SAA: SAUSA300_1363(gpsA)
            MSM: MSMEG_2393(gpsA)
            AAU: AAur_2482
            CHU: CHU_1307(gpsA)
            GFO: GFO_3429(gpsA)
STRUCTURES  PDB: 1EVY  1EVZ  1JDJ  1M66  1M67  1N1E  1N1G  1WPQ  1X0V  1X0X  
                 1YJ8  1Z82  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.8
            ExPASy - ENZYME nomenclature database: 1.1.1.8
            ExplorEnz - The Enzyme Database: 1.1.1.8
            ERGO genome analysis and discovery system: 1.1.1.8
            BRENDA, the Enzyme Database: 1.1.1.8
            CAS: 9075-65-4
///
ENTRY       EC 1.1.1.9                  Enzyme
NAME        D-xylulose reductase;
            NAD+-dependent xylitol dehydrogenase;
            xylitol dehydrogenase;
            erythritol dehydrogenase;
            2,3-cis-polyol(DPN) dehydrogenase (C3-5);
            pentitol-DPN dehydrogenase;
            xylitol-2-dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     xylitol:NAD+ 2-oxidoreductase (D-xylulose-forming)
REACTION    xylitol + NAD+ = D-xylulose + NADH + H+ [RN:R01896]
ALL_REAC    R01896
SUBSTRATE   xylitol [CPD:C00379];
            NAD+ [CPD:C00003]
PRODUCT     D-xylulose [CPD:C00310];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts as an L-erythrulose reductase.
REFERENCE   1  [PMID:13692998]
  AUTHORS   CHIANG C, KNIGHT SG.
  TITLE     A new pathway of pentose metabolism.
  JOURNAL   Biochem. Biophys. Res. Commun. 3 (1960) 554-9.
  ORGANISM  Penicillium chrysogenum
REFERENCE   2
  AUTHORS   Hickman, J. and Ashwell, G.
  TITLE     A sensitive and stereospecific enzymatic assay for xylulose.
  JOURNAL   J. Biol. Chem. 234 (1959) 758-761.
  ORGANISM  guinea pig
REFERENCE   3  [PMID:13789254]
  AUTHORS   JAKOBY WB, FREDERICKS J.
  TITLE     Erythritol dehydrogenase from Aerobacter aerogenes.
  JOURNAL   Biochim. Biophys. Acta. 48 (1961) 26-32.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K05351  D-xylulose reductase
GENES       SCE: YLR070C(XYL2)
            PIC: PICST_86924(XYL2)
            AFM: AFUA_1G04820
            PLU: plu1960
            SGL: SG0610
            BMA: BMAA1076
            BUR: Bcep18194_B3068
            BPS: BPSS1235
            BPM: BURPS1710b_A0234
            BPD: BURPS668_A1742
            BTE: BTH_II1176
            MLO: mlr4915
            SME: SMc01992
            ATU: Atu4318
            ATC: AGR_L_1091
            RET: RHE_PE00268
            RLE: pRL110382
            RDE: RD1_3623(xdh)
            RRU: Rru_A0252
            BAD: BAD_0317
STRUCTURES  PDB: 1ZEM  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.9
            ExPASy - ENZYME nomenclature database: 1.1.1.9
            ExplorEnz - The Enzyme Database: 1.1.1.9
            ERGO genome analysis and discovery system: 1.1.1.9
            BRENDA, the Enzyme Database: 1.1.1.9
            CAS: 9028-16-4
///
ENTRY       EC 1.1.1.10                 Enzyme
NAME        L-xylulose reductase;
            xylitol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     xylitol:NADP+ 4-oxidoreductase (L-xylulose-forming)
REACTION    xylitol + NADP+ = L-xylulose + NADPH + H+ [RN:R01904]
ALL_REAC    R01904
SUBSTRATE   xylitol [CPD:C00379];
            NADP+ [CPD:C00006]
PRODUCT     L-xylulose [CPD:C00312];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:2981816]
  AUTHORS   Doten RC, Mortlock RP.
  TITLE     Characterization of xylitol-utilizing mutants of Erwinia uredovora.
  JOURNAL   J. Bacteriol. 161 (1985) 529-33.
  ORGANISM  Erwinia uredovora
REFERENCE   2
  AUTHORS   Hickman, J. and Ashwell, G.
  TITLE     A sensitive and stereospecific enzymatic assay for xylulose.
  JOURNAL   J. Biol. Chem. 234 (1959) 758-761.
  ORGANISM  guinea pig
REFERENCE   3  [PMID:13416220]
  AUTHORS   HOLLMANN S, TOUSTER O.
  TITLE     The L-xylulose-xylitol enzyme and other polyol dehydrogenases of
            guinea pig liver mitochondria.
  JOURNAL   J. Biol. Chem. 225 (1957) 87-102.
  ORGANISM  guinea pig
REFERENCE   4
  AUTHORS   Touster, O., Reynolds, V.H. and Hutcheson, R.M.
  TITLE     The reduction of L-xylulose to xylitol by guinea pig liver
            mitochondria.
  JOURNAL   J. Biol. Chem. 221 (1956) 697-709.
  ORGANISM  guinea pig
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K03331  L-xylulose reductase
GENES       HSA: 51181(DCXR)
            MMU: 67880(Dcxr)
            RNO: 171408(Dcxr)
            BPD: BURPS668_1913
            RLE: RL0634
            MSM: MSMEG_3262
STRUCTURES  PDB: 1PR9  1WNT  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.10
            ExPASy - ENZYME nomenclature database: 1.1.1.10
            ExplorEnz - The Enzyme Database: 1.1.1.10
            ERGO genome analysis and discovery system: 1.1.1.10
            BRENDA, the Enzyme Database: 1.1.1.10
            CAS: 9028-17-5
///
ENTRY       EC 1.1.1.11                 Enzyme
NAME        D-arabinitol 4-dehydrogenase;
            D-arabitol dehydrogenase;
            arabitol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-arabinitol:NAD+ 4-oxidoreductase
REACTION    D-arabinitol + NAD+ = D-xylulose + NADH + H+ [RN:R05604]
ALL_REAC    R05604;
            (other) R00868
SUBSTRATE   D-arabinitol [CPD:C01904];
            NAD+ [CPD:C00003]
PRODUCT     D-xylulose [CPD:C00310];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Lin, E.C.C.
  TITLE     An inducible D-arabitol dehydrogenase from Aerobacter aerogenes.
  JOURNAL   J. Biol. Chem. 236 (1961) 31-36.
  ORGANISM  Aerobacter aerogenes
REFERENCE   2
  AUTHORS   Wood, W.A., McDonough, M.J. and Jacobs, L.B.
  TITLE     Ribitol and D-arabitol utilization by Aerobacter aerogenes.
  JOURNAL   J. Biol. Chem. 236 (1961) 2190-2195.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K00007  D-arabinitol 4-dehydrogenase
GENES       YPE: YPO2325(dalD)
            YPK: y2008
            YPM: YP_2112(dalD)
            YPA: YPA_1674
            YPS: YPTB2244(dalD)
            RSO: RSc2129(dalD)
            BMA: BMA0344
            BXE: Bxe_A0730
            BUR: Bcep18194_A5916
            BAM: Bamb_2633
            BPS: BPSL0840(dalD)
            BPM: BURPS1710b_1047(dalD)
            BTE: BTH_I0703
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.11
            ExPASy - ENZYME nomenclature database: 1.1.1.11
            ExplorEnz - The Enzyme Database: 1.1.1.11
            ERGO genome analysis and discovery system: 1.1.1.11
            BRENDA, the Enzyme Database: 1.1.1.11
            CAS: 9028-18-6
///
ENTRY       EC 1.1.1.12                 Enzyme
NAME        L-arabinitol 4-dehydrogenase;
            pentitol-DPN dehydrogenase;
            L-arabitol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-arabinitol:NAD+ 4-oxidoreductase (L-xylulose-forming)
REACTION    L-arabinitol + NAD+ = L-xylulose + NADH + H+ [RN:R01903]
ALL_REAC    R01903
SUBSTRATE   L-arabinitol [CPD:C00532];
            NAD+ [CPD:C00003]
PRODUCT     L-xylulose [CPD:C00312];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13692998]
  AUTHORS   CHIANG C, KNIGHT SG.
  TITLE     A new pathway of pentose metabolism.
  JOURNAL   Biochem. Biophys. Res. Commun. 3 (1960) 554-9.
  ORGANISM  Penicillium chrysogenum
REFERENCE   2  [PMID:13692999]
  AUTHORS   CHIANG C, KNIGHT SG.
  TITLE     L-Arabinose metabolism by cell-free extracts of Penicillium
            chrysogenum.
  JOURNAL   Biochim. Biophys. Acta. 46 (1961) 271-8.
  ORGANISM  Penicillium chrysogenum
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.12
            ExPASy - ENZYME nomenclature database: 1.1.1.12
            ExplorEnz - The Enzyme Database: 1.1.1.12
            ERGO genome analysis and discovery system: 1.1.1.12
            BRENDA, the Enzyme Database: 1.1.1.12
            CAS: 9028-19-7
///
ENTRY       EC 1.1.1.13                 Enzyme
NAME        L-arabinitol 2-dehydrogenase;
            L-arabinitol dehydrogenase (ribulose-forming);
            L-arabinitol (ribulose-forming) dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-arabinitol:NAD+ 2-oxidoreductase (L-ribulose-forming)
REACTION    L-arabinitol + NAD+ = L-ribulose + NADH + H+ [RN:R02441]
ALL_REAC    R02441
SUBSTRATE   L-arabinitol [CPD:C00532];
            NAD+ [CPD:C00003]
PRODUCT     L-ribulose [CPD:C00508];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13692999]
  AUTHORS   CHIANG C, KNIGHT SG.
  TITLE     L-Arabinose metabolism by cell-free extracts of Penicillium
            chrysogenum.
  JOURNAL   Biochim. Biophys. Acta. 46 (1961) 271-8.
  ORGANISM  Penicillium chrysogenum
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
GENES       HIP: CGSHiEE_02840(thrA)
            HIQ: CGSHiGG_03050(thrA)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.13
            ExPASy - ENZYME nomenclature database: 1.1.1.13
            ExplorEnz - The Enzyme Database: 1.1.1.13
            ERGO genome analysis and discovery system: 1.1.1.13
            BRENDA, the Enzyme Database: 1.1.1.13
            CAS: 9028-20-0
///
ENTRY       EC 1.1.1.14                 Enzyme
NAME        L-iditol 2-dehydrogenase;
            polyol dehydrogenase;
            sorbitol dehydrogenase;
            L-iditol:NAD+ 5-oxidoreductase;
            L-iditol (sorbitol) dehydrogenase;
            glucitol dehydrogenase;
            L-iditol:NAD+ oxidoreductase;
            NAD+-dependent sorbitol dehydrogenase;
            NAD+-dependent sorbitol dehydrogenase;
            NAD+-sorbitol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-iditol:NAD+ 2-oxidoreductase
REACTION    L-iditol + NAD+ = L-sorbose + NADH + H+ [RN:R07145]
ALL_REAC    R07145;
            (other) R00875
SUBSTRATE   L-iditol [CPD:C01507];
            NAD+ [CPD:C00003]
PRODUCT     L-sorbose [CPD:C00247];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts on D-glucitol (giving D-fructose) and other closely
            related sugar alcohols.
REFERENCE   1
  AUTHORS   Bailey, J.P., Renz, C. and McGuinness, E.T.
  TITLE     Sorbitol dehydrogenase from horse liver: purification,
            characterization and comparative properties.
  JOURNAL   Comp. Biochem. Physiol. 69B (1981) 909-914.
  ORGANISM  horse
REFERENCE   2  [PMID:6852349]
  AUTHORS   Burnell JN, Holmes RS.
  TITLE     Purification and properties of sorbitol dehydrogenase from mouse
            liver.
  JOURNAL   Int. J. Biochem. 15 (1983) 507-11.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:667078]
  AUTHORS   Leissing N, McGuinness ET.
  TITLE     Rapid affinity purification and properties of rat liver sorbitol
            dehydrogenase.
  JOURNAL   Biochim. Biophys. Acta. 524 (1978) 254-61.
  ORGANISM  rat [GN:rno]
REFERENCE   4
  AUTHORS   Negm, F.B. and Loescher, W.H.
  TITLE     Detection and characterization of sorbitol dehydrogenase from apple
            callus tissue.
  JOURNAL   Plant Physiol. 64 (1979) 69-73.
  ORGANISM  Malus domestica
REFERENCE   5  [PMID:6870831]
  AUTHORS   O'Brien MM, Schofield PJ, Edwards MR.
  TITLE     Polyol-pathway enzymes of human brain. Partial purification and
            properties of sorbitol dehydrogenase.
  JOURNAL   Biochem. J. 211 (1983) 81-90.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K00008  L-iditol 2-dehydrogenase
GENES       HSA: 6652(SORD)
            MMU: 20322(Sord)
            RNO: 24788(Sord)
            CFA: 487535(SORD)
            GGA: 415332(SORD)
            XLA: 446317(sord)
            XTR: 496715(sord)
            SPU: 585570(LOC585570)
            DME: Dmel_CG1982(Sodh-1) Dmel_CG4649(Sodh-2)
            CEL: R04B5.5 R04B5.6
            ATH: AT5G51970
            OSA: 4346217
            CME: CMA009C
            SCE: YDL246C(SOR2) YJR159W(SOR1)
            AGO: AGOS_ABR229C
            PIC: PICST_40172(SOR3)
            CAL: CaO19_7676(CaO19.7676)
            SPO: SPBC1773.05c(tms1)
            ANI: AN8109.2 AN9064.2
            AFM: AFUA_1G11020 AFUA_1G11030 AFUA_1G14390 AFUA_1G16270
                 AFUA_7G02550 AFUA_8G02000
            AOR: AO090009000575 AO090020000647 AO090038000631 AO090103000393
                 AO090701000411
            CNE: CNA01050 CNG00100 CNH02960
            UMA: UM02150.1
            LMA: LmjF33.0520
            ECI: UTI89_C1970(ydjJ) UTI89_C1972(ydjL) UTI89_C2864(gutB)
            ECW: EcE24377A_1998(gutB)
            YPE: YPO2502(gutB)
            YPK: y1686
            YPM: YP_2317(gutB)
            YPA: YPA_1997
            YPN: YPN_2096
            YPS: YPTB2538(gutB)
            PAE: PA4153
            PPU: PP_0552(adh)
            PST: PSPTO_0363(polS)
            PSB: Psyr_4813
            PFL: PFL_2173
            HCH: HCH_02471
            RSO: RSc2147(polS)
            BMA: BMA0330 BMA1195
            BMN: BMA10247_0076
            BXE: Bxe_A0719
            BUR: Bcep18194_A3728 Bcep18194_A5929 Bcep18194_B0887
                 Bcep18194_B1325 Bcep18194_B3148 Bcep18194_C7277
                 Bcep18194_C7304
            BAM: Bamb_2646
            BPS: BPSL0826 BPSL1790
            BPM: BURPS1710b_1031(sdh) BURPS1710b_2072(gutB)
            BPL: BURPS1106A_0872
            BPD: BURPS668_0868
            BTE: BTH_I0692 BTH_I2432
            POL: Bpro_1286
            PCA: Pcar_0330
            MLO: mll4921 mlr3340
            MES: Meso_3781
            SME: SMc01500(smoS)
            ATU: Atu3164
            ATC: AGR_L_3292
            RET: RHE_CH02965(ypch01030) RHE_PC00218(smoS) RHE_PD00350
                 RHE_PE00181
            RLE: RL0650 RL0651 pRL110170
            BJA: bll5566
            BBT: BBta_2284
            SIT: TM1040_0427
            RSP: RSP_0095(smoS) RSP_0263(bchC)
            RDE: RD1_0514(gutB) RD1_3810(gutB)
            ABA: Acid345_1743 Acid345_1744
            BSU: BG10177(gutB)
            BHA: BH0187(gutB) BH0189
            BCZ: BCZK0739(gutB)
            BCL: ABC1039(gutB) ABC3342 ABC3344 ABC4080
            BAY: RBAM_006540(gutB) RBAM_017960(yjmD)
            BPU: BPUM_1170(gutB)
            OIH: OB2750 OB2752 OB3238 OB3258
            SAU: SA0239 SA0240
            SAV: SAV0248 SAV0250
            SAM: MW0224 MW0226
            SAR: SAR0243 SAR0245
            SAS: SAS0224 SAS0226
            SAC: SACOL0233(gutB) SACOL0235
            SAB: SAB0187 SAB0189
            SAA: SAUSA300_0242(gutB) SAUSA300_0244
            SAO: SAOUHSC_00217 SAOUHSC_00219
            SHA: SH0215(gutB)
            SSP: SSP0366
            LMO: lmo0506 lmo2663 lmo2664
            LMF: LMOf2365_0535 LMOf2365_2643 LMOf2365_2644
            LIN: lin0506 lin2812 lin2813
            LWE: lwe2612 lwe2613
            LPL: lp_3545(gutB)
            CPF: CPF_0732
            CBO: CBO3418
            CHY: CHY_1307(gutB)
            MSM: MSMEG_3605
            RHA: RHA1_ro02784 RHA1_ro02809 RHA1_ro03291
            PAC: PPA0918
            RBA: RB3488
            TDE: TDE0075
            TEL: tll0970 tlr1436
            GVI: glr0369 glr0940
            ANA: alr2335 alr5117
            AVA: Ava_0154 Ava_1615 Ava_2347
            DET: DET0125
            DEH: cbdb_A145
            DGE: Dgeo_2864
            SSO: SSO3237
            STO: ST2341
            SAI: Saci_0410
STRUCTURES  PDB: 1K2W  1PL6  1PL7  1PL8  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.14
            ExPASy - ENZYME nomenclature database: 1.1.1.14
            ExplorEnz - The Enzyme Database: 1.1.1.14
            ERGO genome analysis and discovery system: 1.1.1.14
            BRENDA, the Enzyme Database: 1.1.1.14
            CAS: 9028-21-1
///
ENTRY       EC 1.1.1.15                 Enzyme
NAME        D-iditol 2-dehydrogenase;
            D-sorbitol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-iditol:NAD+ 2-oxidoreductase
REACTION    D-iditol + NAD+ = D-sorbose + NADH + H+ [RN:R02896]
ALL_REAC    R02896;
            (other) R00875 R05831
SUBSTRATE   D-iditol [CPD:C01489];
            NAD+ [CPD:C00003]
PRODUCT     D-sorbose [CPD:C00764];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also converts xylitol into L-xylulose and L-glucitol into
            L-fructose.
REFERENCE   1
  AUTHORS   Shaw, D.R.D.
  TITLE     Polyol dehydrogenases. 3. Galactitol dehydrogenase and D-iditol
            dehydrogenase.
  JOURNAL   Biochem. J. 64 (1956) 394-405.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00051  Fructose and mannose metabolism
GENES       REH: H16_A1937(mtlD)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.15
            ExPASy - ENZYME nomenclature database: 1.1.1.15
            ExplorEnz - The Enzyme Database: 1.1.1.15
            ERGO genome analysis and discovery system: 1.1.1.15
            BRENDA, the Enzyme Database: 1.1.1.15
            CAS: 9028-22-2
///
ENTRY       EC 1.1.1.16                 Enzyme
NAME        galactitol 2-dehydrogenase;
            dulcitol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     galactitol:NAD+ 2-oxidoreductase
REACTION    galactitol + NAD+ = D-tagatose + NADH + H+ [RN:R02928]
ALL_REAC    R02928
SUBSTRATE   galactitol [CPD:C01697];
            NAD+ [CPD:C00003]
PRODUCT     D-tagatose [CPD:C00795];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also converts other alditols containing an L-threo-configuration
            adjacent to a primary alcohol group into the corresponding sugars.
REFERENCE   1
  AUTHORS   Shaw, D.R.D.
  TITLE     Polyol dehydrogenases. 3. Galactitol dehydrogenase and D-iditol
            dehydrogenase.
  JOURNAL   Biochem. J. 64 (1956) 394-405.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00052  Galactose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.16
            ExPASy - ENZYME nomenclature database: 1.1.1.16
            ExplorEnz - The Enzyme Database: 1.1.1.16
            ERGO genome analysis and discovery system: 1.1.1.16
            BRENDA, the Enzyme Database: 1.1.1.16
            CAS: 9028-23-3
///
ENTRY       EC 1.1.1.17                 Enzyme
NAME        mannitol-1-phosphate 5-dehydrogenase;
            hexose reductase;
            mannitol 1-phosphate dehydrogenase;
            D-mannitol-1-phosphate dehydrogenase;
            fructose 6-phosphate reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-mannitol-1-phosphate:NAD+ 5-oxidoreductase
REACTION    D-mannitol 1-phosphate + NAD+ = D-fructose 6-phosphate + NADH + H+
            [RN:R00758]
ALL_REAC    R00758 > R02703
SUBSTRATE   D-mannitol 1-phosphate [CPD:C00644];
            NAD+ [CPD:C00003]
PRODUCT     D-fructose 6-phosphate [CPD:C00085];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:14367396]
  AUTHORS   MARMUR J, HOTCHKISS RD.
  TITLE     Mannitol metabolism, a transferable property of pneumococcus.
  JOURNAL   J. Biol. Chem. 214 (1955) 383-96.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Wolfe, J.B. and Kaplan, N.O.
  TITLE     Hexose phosphate and hexose reductase. A. D-Mannitol-1-phosphate
            dehydrogenase from E. coli.
  JOURNAL   Methods Enzymol. 1 (1955) 346-348.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Wolfe, J.B. and Kaplan, N.O.
  TITLE     D-Mannitol 1-phosphate dehydrogenase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 218 (1956) 849-869.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K00009  mannitol-1-phosphate 5-dehydrogenase
GENES       ANI: AN5975.2
            AFM: AFUA_2G10660
            AOR: AO090011000576
            ECO: b3600(mtlD)
            ECJ: JW3574(mtlD)
            ECE: Z5024(mtlD)
            ECS: ECs4476
            ECC: c4417(mtlD)
            ECI: UTI89_C4138(mtlD)
            ECP: ECP_3698
            ECV: APECO1_2857(mtlD)
            STY: STY4110(mtlD)
            STT: t3833(mtlD)
            SPT: SPA3538(mtlD)
            SEC: SC3610(mtlD)
            STM: STM3686(mtlD)
            YPE: YPO4067(mtlD)
            YPK: y4086(mtlD)
            YPM: YP_3978(mtlD2)
            YPA: YPA_3015
            YPN: YPN_3714
            YPS: YPTB3919(mtlD)
            YPI: YpsIP31758_4127(mtlD)
            SFL: SF3634(mtlD)
            SFX: S4134(mtlD)
            SFV: SFV_3937(mtlD)
            SSN: SSON_3808(mtlD)
            SBO: SBO_3598(mtlD)
            ECA: ECA0088(mtlD)
            BUC: BU571(mtlD)
            BAS: BUsg551(mtlD)
            BAB: bbp516(mtlD)
            SGL: SG0015
            ENT: Ent638_0135
            KPN: KPN_03943(mtlD)
            HSO: HS_1251(mtlD)
            PMU: PM1062(mtlD)
            MSU: MS0410(mtlD)
            APL: APL_1629(mtlD)
            VCH: VCA1046
            VCO: VC0395_0195(mtlD)
            VVU: VV1_0639
            VVY: VV0504
            VPA: VP0369
            PPR: PBPRB0362
            AHA: AHA_0550
            ABU: Abu_1393
            BSU: BG11216(mtlD)
            BHA: BH3851(mtlD)
            BLI: BL02815(mtlD)
            BLD: BLi00507(mtlD)
            BCL: ABC2926(mtlD)
            BAY: RBAM_004250
            BPU: BPUM_0371
            OIH: OB2600
            GKA: GK1945
            GTN: GTNG_1844
            SAU: SA1963(mtlD)
            SAV: SAV2159(mtlD)
            SAM: MW2085(mtlD)
            SAR: SAR2247(mtlD)
            SAS: SAS2060
            SAC: SACOL2149(mtlD)
            SAB: SAB2039(mtlD)
            SAA: SAUSA300_2108(mtlD)
            SAO: SAOUHSC_02403
            SHA: SH0232(mtlD)
            SSP: SSP0725
            LLA: L33416(mtlD)
            LLC: LACR_0030
            LLM: llmg_0025(mtlD)
            SPN: SP_0397
            SPR: spr0359(mtlD)
            SPD: SPD_0363
            SMU: SMU.1182(mtlD)
            LPL: lp_0233(mtlD)
            LSL: LSL_1618(mtlD)
            LCA: LSEI_2885
            EFA: EF0413(mtlD)
            CAC: CAC0157(mtlD)
            CDF: CD2331(mtlD)
            TTE: TTE0342(mtlD)
            MPN: MPN652(mtlD)
            MPU: MYPU_7500(mtlD)
            MMY: MSC_0017(mtlD)
            MHY: mhp568(mtlD)
            MHJ: MHJ_0553(mtlD)
            MHP: MHP7448_0549(mtlD)
            MCP: MCAP_0032
            LXX: Lxx00800(mtlD)
            CMI: CMM_2589(mtlD)
            AAU: AAur_3858(mtlD)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.17
            ExPASy - ENZYME nomenclature database: 1.1.1.17
            ExplorEnz - The Enzyme Database: 1.1.1.17
            ERGO genome analysis and discovery system: 1.1.1.17
            BRENDA, the Enzyme Database: 1.1.1.17
            CAS: 9028-24-4
///
ENTRY       EC 1.1.1.18                 Enzyme
NAME        inositol 2-dehydrogenase;
            myo-inositol 2-dehydrogenase;
            myo-inositol:NAD+ oxidoreductase;
            inositol dehydrogenase;
            myo-inositol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     myo-inositol:NAD+ 2-oxidoreductase
REACTION    myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH +
            H+ [RN:R01183]
ALL_REAC    R01183
SUBSTRATE   myo-inositol [CPD:C00137];
            NAD+ [CPD:C00003]
PRODUCT     2,4,6/3,5-pentahydroxycyclohexanone [CPD:C00691];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:5905122]
  AUTHORS   Berman T, Magasanik B.
  TITLE     The pathway of myo-inositol degradation in Aerobacter aerogenes.
            Dehydrogenation and dehydration.
  JOURNAL   J. Biol. Chem. 241 (1966) 800-6.
  ORGANISM  Aerobacter aerogenes
REFERENCE   2  [PMID:13292912]
  AUTHORS   LARNER J, JACKSON WT, GRAVES DJ, STAMER JR.
  TITLE     Inositol dehydrogenase from Aerobacter aerogenes.
  JOURNAL   Arch. Biochem. Biophys. 60 (1956) 352-63.
  ORGANISM  Aerobacter aerogenes
REFERENCE   3  [PMID:4351258]
  AUTHORS   Vidal-Leiria M, van Uden N.
  TITLE     Inositol dehydrogenase from the yeast Cryptococcus melibiosum.
  JOURNAL   Biochim. Biophys. Acta. 293 (1973) 295-303.
  ORGANISM  Cryptococcus melibiosum
PATHWAY     PATH: map00031  Inositol metabolism
            PATH: map00562  Inositol phosphate metabolism
ORTHOLOGY   KO: K00010  myo-inositol 2-dehydrogenase
GENES       CME: CMF086C CMR475C
            PIC: PICST_64256 PICST_78306
            ANI: AN5984.2
            AFM: AFUA_2G10240
            AOR: AO090011000611 AO090011000612
            ANG: An04g10130(leu2B)
            STM: STM4425
            YPA: YPA_2521
            YPN: YPN_1064
            YPS: YPTB1073
            YEN: YE4026(idh)
            ECA: ECA1458(idhA)
            PLU: plu1804
            SPE: Spro_2393 Spro_4658
            HSO: HS_1576(iolG)
            PPR: PBPRB0470
            PST: PSPTO_3047 PSPTO_3494(iolG)
            PSB: Psyr_3268
            PSP: PSPPH_2336 PSPPH_3188(iolG)
            PFL: PFL_2591
            NOC: Noc_1755
            HCH: HCH_05773
            RSO: RSc1246(iolG)
            BMA: BMA0918
            BXE: Bxe_A1331 Bxe_A1332
            BVI: Bcep1808_1391
            BUR: Bcep18194_A3327 Bcep18194_A4572 Bcep18194_A4693
                 Bcep18194_A6014
            BCN: Bcen_0946 Bcen_2075
            BCH: Bcen2424_1428 Bcen2424_2686
            BAM: Bamb_1308 Bamb_2740 Bamb_3328 Bamb_3338
            BPS: BPSL1988 BPSL1989
            BPM: BURPS1710b_1836(idhA) BURPS1710b_1838
            BTE: BTH_I2641 BTH_I2642
            VEI: Veis_0056 Veis_1850
            CCV: CCV52592_1378
            MLO: mll1000 mll4991(idhA)
            SME: SMb20899(idhA)
            ATU: Atu4012(idhA) Atu4554(iolG)
            ATC: AGR_L_1682 AGR_L_628
            RET: RHE_CH01209(ypch00405) RHE_CH02357 RHE_CH03170(idhA)
                 RHE_CH03255(thuBch)
            RLE: RL1497 RL3622 RL3685 pRL110080 pRL90151
            BME: BMEI0661 BMEII0574 BMEII0938
            BMF: BAB1_1363 BAB2_0528 BAB2_0897
            BMS: BRA0711(idhA)
            BMB: BruAb2_0519(idhA)
            BOV: BOV_A0667(idhA)
            OAN: Oant_3835
            BRA: BRADO1384 BRADO2244(idhA)
            BBT: BBta_0488(idhA)
            NWI: Nwi_1076
            CCR: CC_1296
            SIT: TM1040_3352
            RSP: RSP_3283 RSP_3670
            RSH: Rsph17029_4015
            JAN: Jann_1416
            RDE: RD1_0217(idhA) RD1_0222 RD1_0674 RD1_3876
            PDE: Pden_1678
            GOX: GOX1187
            ACR: Acry_2320 Acry_2329
            SUS: Acid_1485
            BSU: BG10669(iolG)
            BHA: BH2220 BH2316(iolG)
            BCZ: pE33L466_0294(iolG) pE33L466_0299(iolG)
            BLI: BL00240(idh)
            BLD: BLi04245(idh)
            BCL: ABC0427(iolG) ABC0429
            BAY: RBAM_036720
            LPL: lp_3605(iolG1) lp_3606(iolG2) lp_3608(iolG3) lp_3612(iolG4)
            CPE: CPE0093
            CPF: CPF_0085
            CTC: CTC00511 CTC00513
            MHY: mhp144
            MHJ: MHJ_0228
            MHP: MHP7448_0228 MHP7448_0235
            MSM: MSMEG_4666
            MVA: Mvan_0387 Mvan_3968 Mvan_4020
            MGI: Mflv_2598 Mflv_2613
            CGL: NCgl0161(cgl0164) NCgl2029(cgl2110) NCgl2957(cgl3062)
            CGB: cg0204(iolG) cg2313(idhA3) cg3391(idhA1) cg3392(idhA2)
            RHA: RHA1_ro02992 RHA1_ro03886
            SCO: SCO6984(SC8F11.10c) SCO7254(SC5H1.38)
            SMA: SAV1234(iolG) SAV7188
            LXX: Lxx24320
            ART: Arth_0825 Arth_0833 Arth_0834
            PAC: PPA0136 PPA0463 PPA0466 PPA0469
            FRA: Francci3_3374
            FAL: FRAAL3556
            ACE: Acel_1805 Acel_1809 Acel_1814
            KRA: Krad_0276 Krad_4051 Krad_4156
            SEN: SACE_2908 SACE_2980(iolG) SACE_3276(idhA2) SACE_4537(iolG)
                 SACE_4657(iolG) SACE_5193(iolG)
            RXY: Rxyl_1723
            RBA: RB3338(idh)
            AVA: Ava_0798 Ava_1201 Ava_2363
            CHU: CHU_3128(yisS)
            CCH: Cag_0284 Cag_0723
            MBA: Mbar_A1138
            MMA: MM_1153
            RCI: RCIX1923(idhA)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.18
            ExPASy - ENZYME nomenclature database: 1.1.1.18
            ExplorEnz - The Enzyme Database: 1.1.1.18
            ERGO genome analysis and discovery system: 1.1.1.18
            BRENDA, the Enzyme Database: 1.1.1.18
            CAS: 9028-25-5
///
ENTRY       EC 1.1.1.19                 Enzyme
NAME        glucuronate reductase;
            aldehyde reductase;
            L-hexonate:NADP dehydrogenase;
            TPN-L-gulonate dehydrogenase;
            aldehyde reductase II;
            NADP-L-gulonate dehydrogenase;
            D-glucuronate dehydrogenase;
            D-glucuronate reductase;
            L-glucuronate reductase (incorrect)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-gulonate:NADP+ 6-oxidoreductase
REACTION    L-gulonate + NADP+ = D-glucuronate + NADPH + H+ [RN:R01481]
ALL_REAC    R01481
SUBSTRATE   L-gulonate [CPD:C00800];
            NADP+ [CPD:C00006]
PRODUCT     D-glucuronate [CPD:C00191];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also reduces D-galacturonate. May be identical with EC 1.1.1.2
            [alcohol dehydrogenase (NADP+)].
REFERENCE   1  [PMID:13913518]
  AUTHORS   SIVAK A, HOFFMANN-OSTENHOF O.
  TITLE     Enzymes of mesoinositol catabolism in the yeast Schwanniomyces
            accidentalis.
  JOURNAL   Biochim. Biophys. Acta. 53 (1961) 426-8.
  ORGANISM  Schwanniomyces occidentalis
REFERENCE   2
  AUTHORS   von Wartburg, J.P. and Wermoth, B.
  TITLE     Aldehyde reductase.
  JOURNAL   In: Jakoby, W.B. (Ed.), Enzymatic Basis of Detoxication, vol. 1,
            Academic Press, New York, 1980, p. 249-260.
  ORGANISM  human [GN:hsa], rat [GN:rno], pig [GN:ssc]
REFERENCE   3  [PMID:13787380]
  AUTHORS   YORK JL, GROLLMAN AP, BUBLITZ C.
  TITLE     TPN-L-gluonate dehydrogenase.
  JOURNAL   Biochim. Biophys. Acta. 47 (1961) 298-306.
  ORGANISM  rat [GN:rno], pig [GN:ssc]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00053  Ascorbate and aldarate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.19
            ExPASy - ENZYME nomenclature database: 1.1.1.19
            ExplorEnz - The Enzyme Database: 1.1.1.19
            ERGO genome analysis and discovery system: 1.1.1.19
            BRENDA, the Enzyme Database: 1.1.1.19
            CAS: 9028-29-9
///
ENTRY       EC 1.1.1.20                 Enzyme
NAME        glucuronolactone reductase;
            GRase;
            gulonolactone dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-gulono-1,4-lactone:NADP+ 1-oxidoreductase
REACTION    L-gulono-1,4-lactone + NADP+ = D-glucurono-3,6-lactone + NADPH + H+
            [RN:R03183]
ALL_REAC    R03183
SUBSTRATE   L-gulono-1,4-lactone [CPD:C01040];
            NADP+ [CPD:C00006]
PRODUCT     D-glucurono-3,6-lactone [CPD:C02670];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Suzuki, K., Mano, Y. and Shimazono, N.
  TITLE     Conversion of L-gulonolactone to L-ascorbic acid; properties of the
            microsomal enzyme in rat liver.
  JOURNAL   J. Biochem. (Tokyo) 48 (1960) 313-315.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
GENES       REH: H16_B1896(xdhC2)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.20
            ExPASy - ENZYME nomenclature database: 1.1.1.20
            ExplorEnz - The Enzyme Database: 1.1.1.20
            ERGO genome analysis and discovery system: 1.1.1.20
            BRENDA, the Enzyme Database: 1.1.1.20
            CAS: 9028-30-2
///
ENTRY       EC 1.1.1.21                 Enzyme
NAME        aldehyde reductase;
            aldose reductase;
            polyol dehydrogenase (NADP+);
            ALR2;
            alditol:NADP+ oxidoreductase;
            alditol:NADP+ 1-oxidoreductase;
            NADPH-aldopentose reductase;
            NADPH-aldose reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     alditol:NAD(P)+ 1-oxidoreductase
REACTION    alditol + NAD(P)+ = aldose + NAD(P)H + H+ [RN:R02819 R02820]
ALL_REAC    R02819 > R01036 R01093 R01758;
            R02820 > R01041 R01095 R01431 R01759 R01787;
            (other) R02531 R02577
SUBSTRATE   alditol [CPD:C00717];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     aldose [CPD:C01370];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
INHIBITOR   HOE-252 [CPD:C01426];
            Tolrestat [CPD:C01621];
            Zopolrestat [CPD:C01865];
            Salfredin [CPD:C05152]
COMMENT     Has wide specificity.
REFERENCE   1  [PMID:4216364]
  AUTHORS   Attwood MA, Doughty CC.
  TITLE     Purification and properties of calf liver aldose reductase.
  JOURNAL   Biochim. Biophys. Acta. 370 (1974) 358-68.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:36151]
  AUTHORS   Boghosian RA, McGuinness ET.
  TITLE     Affinity purification and properties of porcine brain aldose
            reductase.
  JOURNAL   Biochim. Biophys. Acta. 567 (1979) 278-86.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:14401390]
  AUTHORS   HERS HG.
  TITLE     [Aldose reductase.]
  JOURNAL   Biochim. Biophys. Acta. 37 (1960) 120-6.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:4381350]
  AUTHORS   Scher BM, Horecker BL.
  TITLE     Pentose metabolism in Candida. 3. The triphosphopyridine
            nucleotide-specific polyol dehydrogenase of Candida utilis.
  JOURNAL   Arch. Biochem. Biophys. 116 (1966) 117-28.
  ORGANISM  Candida utilis
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00051  Fructose and mannose metabolism
            PATH: map00052  Galactose metabolism
            PATH: map00561  Glycerolipid metabolism
            PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K00011  aldehyde reductase
GENES       HSA: 231(AKR1B1)
            MMU: 11677(Akr1b3) 11997(Akr1b7) 14187(Akr1b8)
            RNO: 24192(Akr1b4)
            CFA: 482334(LOC482334)
            BTA: 317748(AKR1B1)
            SSC: 396816(ALR2)
            GGA: 418169(AKR1B10) 418170(LOC418170) 418171(AKR1B1)
                 425137(LOC425137)
            XLA: 398904(MGC68609)
            XTR: 496546(akr1b7)
            SPU: 589385(LOC589385)
            SCE: YHR104W(GRE3)
            TET: TTHERM_00697540 TTHERM_01051730 TTHERM_01080350
                 TTHERM_01080360
            EHI: 248.t00014 466.t00004 609.t00002
            YPS: YPTB2971
            SBO: SBO_0196(yafB)
            SDY: SDY_0226(yafB)
            ACI: ACIAD3616(alrA)
            PAT: Patl_2877
            CVI: CV_0701
            REH: H16_A3186 H16_B2162
            RPA: RPA3161(yafB) RPA4297
            ABA: Acid345_2661
            SUS: Acid_2860
STRUCTURES  PDB: 1ABN  1ADS  1AH0  1AH3  1AH4  1AZ1  1AZ2  1DLA  1EF3  1EKO  
                 1EL3  1IEI  1JEZ  1K8C  1MAR  1MI3  1PWL  1PWM  1R38  1SM9  
                 1T40  1T41  1US0  1X96  1X97  1X98  1XGD  1Z3N  1Z89  1Z8A  
                 2ACQ  2ACR  2ACS  2ACU  2AGT  2BGQ  2BGS  2DUX  2DUZ  2DV0  
                 2F2K  2FZ8  2FZ9  2FZB  2FZD  2HV5  2HVN  2HVO  2I16  2I17  
                 2IKG  2IKH  2IKI  2IKJ  2INE  2INZ  2IPW  2IQ0  2IQD  2IS7  
                 2ISF  2J8T  2NVC  2NVD  2PEV  2PF8  2PFH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.21
            ExPASy - ENZYME nomenclature database: 1.1.1.21
            ExplorEnz - The Enzyme Database: 1.1.1.21
            ERGO genome analysis and discovery system: 1.1.1.21
            BRENDA, the Enzyme Database: 1.1.1.21
            CAS: 9028-31-3
///
ENTRY       EC 1.1.1.22                 Enzyme
NAME        UDP-glucose 6-dehydrogenase;
            UDP-glucose dehydrogenase;
            uridine diphosphoglucose dehydrogenase;
            UDPG dehydrogenase;
            UDPG:NAD oxidoreductase;
            UDP-alpha-D-glucose:NAD oxidoreductase;
            UDP-glucose:NAD+ oxidoreductase;
            uridine diphosphate glucose dehydrogenase;
            UDP-D-glucose dehydrogenase;
            uridine diphosphate D-glucose dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     UDP-glucose:NAD+ 6-oxidoreductase
REACTION    UDP-glucose + 2 NAD+ + H2O = UDP-glucuronate + 2 NADH + 2 H+
            [RN:R00286]
ALL_REAC    R00286
SUBSTRATE   UDP-glucose [CPD:C00029];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     UDP-glucuronate [CPD:C00167];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts on UDP-2-deoxyglucose.
REFERENCE   1  [PMID:1091296]
  AUTHORS   Druzhinina TN, Kusov YY, Shibaev VN, Kochetkov NK, Biely P, Kucar S,
            Bauer S.
  TITLE     Uridine diphosphate 2-deoxyglucose. Chemical synthesis, enzymic
            oxidation and epimerization.
  JOURNAL   Biochim. Biophys. Acta. 381 (1975) 301-7.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:13373402]
  AUTHORS   KALCKAR HM, MAXWELL ES, STROMINGER JL.
  TITLE     Some properties of uridine diphosphoglucose dehydrogenase.
  JOURNAL   Arch. Biochem. Biophys. 65 (1956) 2-10.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:13459898]
  AUTHORS   STROMINGER JL, MAPSON LW.
  TITLE     Uridine diphosphoglucose dehydrogenase of pea seedlings.
  JOURNAL   Biochem. J. 66 (1957) 567-72.
  ORGANISM  Pisum sativum
REFERENCE   4  [PMID:13398389]
  AUTHORS   AXELROD J, KALCKAR HM, MAXWELL ES, STROMINGER JL.
  TITLE     Enzymatic formation of uridine diphosphoglucuronic acid.
  JOURNAL   J. Biol. Chem. 224 (1957) 79-90.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00053  Ascorbate and aldarate metabolism
            PATH: map00500  Starch and sucrose metabolism
            PATH: map00520  Nucleotide sugars metabolism
ORTHOLOGY   KO: K00012  UDPglucose 6-dehydrogenase
GENES       HSA: 7358(UGDH)
            PTR: 471171(UGDH)
            MMU: 22235(Ugdh)
            RNO: 83472(Ugdh)
            CFA: 479107(UGDH)
            BTA: 281564(UGDH)
            GGA: 422792(UGDH) 771129(LOC771129)
            XLA: 379152(MGC52511)
            DRE: 116991(ugdh)
            SPU: 579664(LOC579664)
            DME: Dmel_CG10072(sgl)
            CEL: F29F11.1(sqv-4)
            ATH: AT1G26570(ATUGD1/UGD1) AT3G29360 AT5G15490 AT5G39320
            OSA: 4333156 4333410 4334169 4352147
            CME: CMB031C CMT471C
            ANI: AN9172.2
            AFM: AFUA_1G17020 AFUA_8G00920
            AOR: AO090001000557 AO090010000065
            CNE: CNL06460
            UMA: UM00118.1
            CPV: cgd8_920
            CHO: Chro.80111
            TET: TTHERM_00494360
            TCR: 509715.90 510105.100
            ECO: b2028(ugd)
            ECJ: JW2010(ugd)
            ECE: Z3190(ugd)
            ECS: ECs2829
            ECC: c2555(ugd)
            ECI: UTI89_C2301(ugd)
            ECP: ECP_2071
            ECV: APECO1_1125(ugd)
            ECW: EcE24377A_2319(ugd)
            ECX: EcHS_A2178(ugd)
            STY: STY2289(ugd)
            STT: t0793(ugd)
            SPT: SPA0791(ugd)
            SEC: SC2090(udg)
            STM: STM2080(udg)
            YPE: YPO2174
            YPK: y2147
            YPM: YP_1973(ugd)
            YPA: YPA_1532
            YPN: YPN_1641
            YPP: YPDSF_0960
            YPS: YPTB2100
            SSN: SSON_2099(ugd)
            SBO: SBO_0857(ugd)
            SDY: SDY_2213(ugd)
            ECA: ECA3147(ugd)
            PLU: plu2500
            WBR: WGLp368(ugd)
            SGL: SG1368
            ENT: Ent638_2641
            SPE: Spro_2708
            PMU: PM0776
            XFA: XF1606
            XFT: PD1167(ugd)
            XCC: XCC1503(ugd)
            XCB: XC_2733
            XCV: XCV1594(ugd1) XCV3705(ugd2)
            XAC: XAC1551(ugd) XAC3581(ugd)
            XOO: XOO2066(ugd)
            XOM: XOO_1946(XOO1946)
            VCH: VCA0780
            VCO: VC0395_0720(ugd)
            VVU: VV1_0774
            VVY: VV0365
            VPA: VP0236
            VFI: VF0198 VF0199
            PPR: PBPRA2657 PBPRA2675(ugd)
            PAE: PA2022 PA3559
            PAU: PA14_18300 PA14_38360(ugd)
            PPU: PP_2926
            PPF: Pput_2766
            PST: PSPTO_2891 PSPTO_5585
            PSB: Psyr_2696 Psyr_5105
            PSP: PSPPH_2809
            PFL: PFL_3050(udg) PFL_3078
            PFO: Pfl_2024 Pfl_2817 Pfl_2848 Pfl_4070
            PEN: PSEEN3359
            PMY: Pmen_2354
            PAR: Psyc_0110 Psyc_0650
            PCR: Pcryo_0119
            ACI: ACIAD0072(ugd) ACIAD0087 ACIAD0100
            SON: SO_4687(ugd)
            SFR: Sfri_1373
            SAZ: Sama_2236
            SPL: Spea_1418
            SHE: Shewmr4_1330 Shewmr4_3885
            SHM: Shewmr7_3978
            SHN: Shewana3_1387
            ILO: IL0538(ugd)
            CPS: CPS_0591(ugd)
            PHA: PSHAa0444(ugd)
            PAT: Patl_3200
            SDE: Sde_2115
            MAQ: Maqu_1710
            CBU: CBU_0680 CBU_0846(ugd)
            CBD: COXBU7E912_0911(ugd)
            MCA: MCA2487(ugd)
            TCX: Tcr_0609 Tcr_1510
            NOC: Noc_2015 Noc_2637
            AEH: Mlg_0289
            HHA: Hhal_2178
            HCH: HCH_04682(ugd) HCH_04938
            CSA: Csal_1761 Csal_1860
            ABO: ABO_0932(ugd1) ABO_0935(ugd2)
            AHA: AHA_0993 AHA_2880
            CVI: CV_3041(ugd) CV_4129(udg)
            RSO: RSc0913(ugd)
            REU: Reut_A2565
            RME: Rmet_0726
            BMA: BMA0423(ugd)
            BMV: BMASAVP1_A2567(ugd)
            BML: BMA10299_A0942(ugd)
            BMN: BMA10247_0206(ugd)
            BXE: Bxe_A0986 Bxe_A2245 Bxe_C1072
            BVI: Bcep1808_0972 Bcep1808_4202 Bcep1808_6511
            BUR: Bcep18194_A4164 Bcep18194_B0866 Bcep18194_B2275
            BCN: Bcen_0572 Bcen_4542
            BCH: Bcen2424_1051 Bcen2424_3821
            BAM: Bamb_0927 Bamb_5547
            BPS: BPSL2511(udg) BPSS1833(udg2)
            BPM: BURPS1710b_2988(udg) BURPS1710b_A0917(udg2)
            BPL: BURPS1106A_2941(udg) BURPS1106A_A2484(udg)
            BPD: BURPS668_2878(udg) BURPS668_A2622(udg)
            BTE: BTH_I1642 BTH_II0544
            PNU: Pnuc_0503
            BPE: BP3728(rkpK)
            BPA: BPP4227(rkpK)
            BBR: BB4815(rkpK)
            AJS: Ajs_0408
            MPT: Mpe_A0606
            NEU: NE1343(udg)
            NET: Neut_1093
            EBA: ebA899(ugd)
            AZO: azo1076(ugd) azo2232(udgH)
            DAR: Daro_1284
            TBD: Tbd_0961
            HHE: HH0644(kfiD)
            WSU: WS0583
            TDN: Tmden_1968
            CJE: Cj1441c(kfiD)
            CFF: CFF8240_1388
            CCV: CCV52592_1223
            ABU: Abu_0659(ugd)
            GSU: GSU1816(ugd)
            GME: Gmet_1430
            GUR: Gura_2308
            PCA: Pcar_1466 Pcar_1806
            PPD: Ppro_1022
            DVU: DVU1907(ugd)
            DVL: Dvul_1257
            DDE: Dde_2042
            LIP: LI0730(ugd)
            DPS: DP0014 DPPB70
            ADE: Adeh_1057 Adeh_2474 Adeh_4292 Adeh_4305
            AFW: Anae109_3213 Anae109_4447
            MXA: MXAN_1048
            SAT: SYN_00532 SYN_01124 SYN_02675
            SFU: Sfum_3370
            RPR: RP779(udg)
            RTY: RT0766(udg)
            RCO: RC1212(udg)
            RFE: RF_1245(udg)
            RBE: RBE_0075(udg)
            WOL: WD0620
            PUB: SAR11_1086(ugd)
            MLO: mlr5265
            MES: Meso_0484 Meso_2782
            PLA: Plav_1921
            SME: SMc02641(rkpK)
            SMD: Smed_0688 Smed_4589
            ATU: Atu4149(ugdH)
            ATC: AGR_L_1413
            RET: RHE_CH03238(rkpK) RHE_PE00044
            RLE: RL3667 pRL110056
            BME: BMEII0727
            BMF: BAB2_0692(ugd)
            BMS: BRA0545(ugd)
            BMB: BruAb2_0677(ugd)
            BOV: BOV_A0476(ugd)
            OAN: Oant_1714 Oant_4414
            BJA: bll8129(ugdH) blr2383(ugdH)
            BRA: BRADO0754(rkpK) BRADO5154
            BBT: BBta_5622 BBta_7353(rkpK)
            RPA: RPA4018
            RPB: RPB_1585
            RPC: RPC_4156
            RPD: RPD_1593
            RPE: RPE_1120 RPE_1513 RPE_3505 RPE_4206
            NWI: Nwi_0543 Nwi_2380
            NHA: Nham_1057 Nham_2755
            XAU: Xaut_3551
            CCR: CC_2379 CC_2382
            SIT: TM1040_3775
            RSP: RSP_0653
            RSH: Rsph17029_2306
            RSQ: Rsph17025_0579 Rsph17025_4095
            JAN: Jann_0076
            RDE: RD1_1493 RD1_B0057(ugd)
            MMR: Mmar10_2489
            HNE: HNE_3236
            ZMO: ZMO0819(ugd)
            NAR: Saro_3255
            SAL: Sala_1563
            SWI: Swit_4534
            ELI: ELI_01215
            GOX: GOX0924
            GBE: GbCGDNIH1_2221
            ACR: Acry_0210 Acry_1348
            RRU: Rru_A2116
            MAG: amb0576
            MGM: Mmc1_0333
            ABA: Acid345_3497 Acid345_3806
            SUS: Acid_0622 Acid_4597 Acid_6697 Acid_7497
            BSU: BG12691(tuaD)
            BHA: BH3708
            BAN: BA5434(ugd)
            BAR: GBAA5434(ugd) GBAA_pXO1_0130(ugd)
            BAA: BA_0287 BXA0130(ugd)
            BAT: BAS5049
            BCE: BC5202
            BCA: BCE_5308(ugd) BCE_5385(ugd)
            BCZ: BCZK4894(ugd)
            BCY: Bcer98_0429 Bcer98_2076
            BTK: BT9727_4879(ugd)
            BTL: BALH_0443(wecC) BALH_4694(ugd) BALH_4773(ugd)
            BLI: BL03352(tuaD)
            BLD: BLi03804(tuaD)
            BCL: ABC3167 ABC3686
            BAY: RBAM_032730(tuaD)
            BPU: BPUM_3208(tuaD) BPUM_3276(ywqF)
            OIH: OB2884 OB2929
            GKA: GK3254
            SSP: SSP0068
            LLM: llmg_1616(ugd)
            SPY: SPy_0542 SPy_2201(hasB)
            SPZ: M5005_Spy_0449 M5005_Spy_1852(hasB)
            SPM: spyM18_0608 spyM18_2237(hasB)
            SPG: SpyM3_0385 SpyM3_1852(hasB)
            SPS: SPs1468 SPs1848
            SPH: MGAS10270_Spy0450 MGAS10270_Spy1971(hasB) MGAS10270_Spy1972
            SPI: MGAS10750_Spy0469(hasB)
            SPJ: MGAS2096_Spy0468 MGAS2096_Spy1883(hasB)
            SPK: MGAS9429_Spy0448 MGAS9429_Spy1863(hasB)
            SPF: SpyM51415 SpyM51825(hasB)
            SPA: M6_Spy0483 M6_Spy1870
            SPB: M28_Spy0437 M28_Spy1885(hasB)
            SPR: spr0139(ugd) spr0318(cps2K)
            SPD: SPD_0143 SPD_0326(cps2K)
            LSL: LSL_0979(ugd)
            OOE: OEOE_1737
            STH: STH785
            CPE: CPE0494
            CTH: Cthe_1352
            CDF: CD2771(rkpK)
            CBE: Cbei_4708 Cbei_4738 Cbei_4880
            CKL: CKL_2099(rkpK)
            DSY: DSY2447
            DRM: Dred_3027
            SWO: Swol_0617 Swol_0705
            MMO: MMOB6010(udgA)
            MTU: Rv0322(udgA)
            MTC: MT0337(ugdA)
            MBO: Mb0330(udgA)
            MBB: BCG_0362(udgA)
            MPA: MAP3825(udgA)
            MAV: MAV_4092 MAV_4823
            MSM: MSMEG_0680 MSMEG_5982
            MVA: Mvan_0598
            MGI: Mflv_0289
            MMC: Mmcs_0931 Mmcs_3113
            MKM: Mkms_0948 Mkms_3173
            MJL: Mjls_0966
            CGL: NCgl0351(cgl0360) NCgl2750(cgl2847)
            CGB: cg0435(udgA1) cg3154(udgA2)
            CEF: CE2662
            CDI: DIP2141
            CJK: jk0173(udgA)
            NFA: nfa54240(ugd)
            RHA: RHA1_ro05446 RHA1_ro05455
            SCO: SCO3052(SCBAC19G2.07)
            SMA: SAV5025(udgA)
            LXX: Lxx03520(udgA)
            CMI: CMM_1429(udgA)
            ART: Arth_1069 Arth_3207
            AAU: AAur_1182 AAur_3170 AAur_4110
            PAC: PPA0593
            NCA: Noca_4579
            TFU: Tfu_2544
            FRA: Francci3_0709 Francci3_3549
            FAL: FRAAL1223(ugd) FRAAL5745(udgA)
            ACE: Acel_0408
            KRA: Krad_3900
            SEN: SACE_0095(rkpK) SACE_5565(rkpK) SACE_5566
            STP: Strop_0933 Strop_1504
            RXY: Rxyl_3115
            RBA: RB1784(ugdH)
            PCU: pc1695(rkpK)
            LIL: LA1459
            LIC: LIC12294(ugd)
            LBJ: LBJ_0959(ugd)
            LBL: LBL_2074(ugd)
            SYN: slr1299
            SYW: SYNW0199(Ugd)
            SYC: syc0570_d(ugd)
            SYF: Synpcc7942_0973 Synpcc7942_0974
            SYD: Syncc9605_0190
            SYE: Syncc9902_0222
            SYG: sync_0233
            SYR: SynRCC307_0187(ugd)
            SYX: SynWH7803_0244(ugd)
            CYA: CYA_0485
            CYB: CYB_1930
            TEL: tll0664
            GVI: gll0969 gll1798 gll2180 gll3719 glr1062
            ANA: alr0658
            AVA: Ava_4589
            PMA: Pro1312(ugd)
            PMM: PMM1261(ugd)
            PMT: PMT1904(ugd)
            PMN: PMN2A_0062
            PMI: PMT9312_1312
            PMB: A9601_13901(ugd)
            PMC: P9515_14211(ugd)
            PMF: P9303_25391(ugd)
            PMG: P9301_13981(ugd)
            PME: NATL1_06831(ugd) NATL1_08641(wecC)
            TER: Tery_2477
            BTH: BT_0379 BT_0599 BT_0829 BT_1341
            BFR: BF1839 BF2297 BF3920
            BFS: BF1904(wcfY) BF2386(rkpK)
            PGI: PG1143
            SRU: SRU_2709
            CHU: CHU_0901(ugd) CHU_3394(ugd)
            GFO: GFO_2038
            FPS: FP1295(ugd)
            CTE: CT1177
            CCH: Cag_0821
            CPH: Cpha266_1534
            PVI: Cvib_0945
            PLT: Plut_0956
            RRS: RoseRS_2396
            RCA: Rcas_3083
            DGE: Dgeo_2649
            AAE: aq_024(nsd)
            TPT: Tpet_0335
            TME: Tmel_1067 Tmel_1339
            FNO: Fnod_0023
            MJA: MJ1054
            MMQ: MmarC5_0495
            MMZ: MmarC7_1350
            MAE: Maeo_0414
            MVN: Mevan_0413
            MAC: MA4457
            MBA: Mbar_A1120
            MMA: MM_1132
            MBU: Mbur_1796
            MTP: Mthe_0952 Mthe_1081
            MHU: Mhun_2113 Mhun_3078
            MEM: Memar_0207 Memar_0699
            MBN: Mboo_1764
            MST: Msp_0210
            MSI: Msm_1612
            AFU: AF0302(ugd-1) AF0596(ugd-2)
            HAL: VNG0046G(ugd)
            HMA: rrnAC3239(ugd2)
            HWA: HQ2680A(ugd)
            NPH: NP2322A(ugd_2) NP4668A(ugd_1)
            PAB: PAB0770(ugd)
            PFU: PF0771 PF1355
            RCI: RCIX2404(ugd)
            IHO: Igni_0622
            SSO: SSO0810(ugd)
            MSE: Msed_1810
            PIS: Pisl_1505
            TPE: Tpen_1719
STRUCTURES  PDB: 1DLI  1DLJ  2O3J  2Q3E  2QG4  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.22
            ExPASy - ENZYME nomenclature database: 1.1.1.22
            ExplorEnz - The Enzyme Database: 1.1.1.22
            ERGO genome analysis and discovery system: 1.1.1.22
            BRENDA, the Enzyme Database: 1.1.1.22
            CAS: 9028-26-6
///
ENTRY       EC 1.1.1.23                 Enzyme
NAME        histidinol dehydrogenase;
            L-histidinol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-histidinol:NAD+ oxidoreductase
REACTION    L-histidinol + 2 NAD+ = L-histidine + 2 NADH + 2 H+ [RN:R01158]
ALL_REAC    R01158;
            (other) R01163 R03012
SUBSTRATE   L-histidinol [CPD:C00860];
            NAD+ [CPD:C00003]
PRODUCT     L-histidine [CPD:C00135];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also oxidizes L-histidinal. The Neurospora enzyme also catalyses the
            reactions of EC 3.5.4.19 (phosphoribosyl-AMP cyclohydrolase) and EC
            3.6.1.31 (phosphoribosyl-ATP diphosphatase).
REFERENCE   1
  AUTHORS   Adams, E.
  TITLE     Enzymatic synthesis of histidine from histidinol.
  JOURNAL   J. Biol. Chem. 209 (1954) 829-846.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Adams, E.
  TITLE     L-Histidinal, a biosynthetic precursor of histidine.
  JOURNAL   J. Biol. Chem. 217 (1955) 325-344.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4872177]
  AUTHORS   Yourno J, Ino I.
  TITLE     Purification and crystallization of histidinol dehydrogenase from
            Salmonella typhimurium LT-2.
  JOURNAL   J. Biol. Chem. 243 (1968) 3273-6.
  ORGANISM  Salmonella typhimurium
REFERENCE   4  [PMID:4872176]
  AUTHORS   Loper JC.
  TITLE     Histidinol dehydrogenase from Salmonella typhimurium.
            Crystallization and composition studies.
  JOURNAL   J. Biol. Chem. 243 (1968) 3264-72.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00340  Histidine metabolism
ORTHOLOGY   KO: K00013  histidinol dehydrogenase
GENES       CME: CMQ082C
            SCE: YCL030C(HIS4)
            AGO: AGOS_AFR703W
            PIC: PICST_89228(HIS2)
            SPO: SPBC1711.13(his2) SPBC29A3.02c(his7)
            ANI: AN0797.2
            AFM: AFUA_1G14570 AFUA_1G17660
            AOR: AO090003000477 AO090005000146
            ECO: b2020(hisD)
            ECJ: JW2002(hisD)
            ECE: Z3182(hisD)
            ECS: ECs2821
            ECC: c2547(hisD)
            ECI: UTI89_C2293(hisD)
            ECP: ECP_2063
            ECV: APECO1_1117(hisD)
            ECW: EcE24377A_2311(hisD)
            ECX: EcHS_A2159(hisD)
            STY: STY2281(hisD)
            STT: t0801(hisD)
            SPT: SPA0799(hisD)
            SEC: SC2082(hisD)
            STM: STM2072(hisD)
            YPE: YPO1548(hisD)
            YPK: y2621(hisD)
            YPM: YP_1437(hisD)
            YPA: YPA_0844
            YPN: YPN_2431
            YPP: YPDSF_1428
            YPS: YPTB1561(hisD)
            YPI: YpsIP31758_2429(hisD)
            SFL: SF2082(hisD)
            SFX: S2203(hisD)
            SFV: SFV_2080(hisD)
            SSN: SSON_2091(hisD)
            SBO: SBO_0846(hisD)
            SDY: SDY_2221(hisD)
            ECA: ECA2583(hisD)
            PLU: plu1569(hisD)
            BUC: BU100(hisD)
            BAS: BUsg093(hisD)
            BAB: bbp094(hisD)
            BCC: BCc_064(hisD)
            SGL: SG1129
            ENT: Ent638_2632
            SPE: Spro_1615
            BFL: Bfl463(hisD)
            BPN: BPEN_478(hisD)
            HIN: HI0469(hisD)
            HIT: NTHI0600(hisD)
            HIP: CGSHiEE_00645(hisD)
            HIQ: CGSHiGG_05590(hisD)
            PMU: PM1198(hisD)
            MSU: MS1892(hisD)
            APL: APL_2020(hisD)
            ASU: Asuc_0631
            XFA: XF2219
            XFT: PD1267(hisD)
            XCC: XCC1809(hisD)
            XCB: XC_2380
            XCV: XCV1875(hisD)
            XAC: XAC1829(hisD)
            XOO: XOO2256(hisD)
            XOM: XOO_2119(XOO2119)
            VCH: VC1133
            VCO: VC0395_A0703(hisD)
            VVU: VV1_2919
            VVY: VV1351
            VPA: VP1138
            VFI: VF1013
            PPR: PBPRA1091
            PAE: PA4448(hisD)
            PAU: PA14_57780(hisD)
            PPU: PP_0966(hisD)
            PPF: Pput_1005
            PST: PSPTO_4438(hisD)
            PSB: Psyr_4133
            PSP: PSPPH_4137(hisD)
            PFL: PFL_0929(hisD)
            PFO: Pfl_0871
            PEN: PSEEN1107(hisD)
            PMY: Pmen_0884
            PAR: Psyc_1902(hisD)
            PCR: Pcryo_2192
            PRW: PsycPRwf_0503
            ACI: ACIAD0663(hisD)
            SON: SO_2073(hisD)
            SDN: Sden_1617
            SFR: Sfri_1719
            SAZ: Sama_1942
            SBL: Sbal_2426
            SBM: Shew185_2419
            SLO: Shew_2198
            SPC: Sputcn32_2179
            SSE: Ssed_2542
            SPL: Spea_2457
            SHE: Shewmr4_1799
            SHM: Shewmr7_2178
            SHN: Shewana3_1853
            SHW: Sputw3181_1830
            ILO: IL1835(hisD)
            CPS: CPS_2061(hisD1) CPS_3890(hisD2)
            PHA: PSHAb0493(hisD)
            PAT: Patl_2881
            SDE: Sde_3168
            PIN: Ping_1656
            MAQ: Maqu_2701
            LPN: lpg1199
            LPF: lpl1207(hisD)
            LPP: lpp1201(hisD)
            MCA: MCA1963(hisD)
            TCX: Tcr_0989
            NOC: Noc_2778
            AEH: Mlg_2215
            HHA: Hhal_2112
            HCH: HCH_05305
            CSA: Csal_2212
            ABO: ABO_0562
            MMW: Mmwyl1_2406
            AHA: AHA_2195(hisD)
            BCI: BCI_0404(hisD)
            RMA: Rmag_0602
            VOK: COSY_0556(hisD)
            NME: NMB1581
            NMA: NMA1770(hisD)
            NMC: NMC1501(hisD)
            NGO: NGO1240
            CVI: CV_0611(hisD)
            RSO: RSc2952(hisD)
            REU: Reut_A3111 Reut_C6092
            REH: H16_A1694 H16_A3416(hisD)
            RME: Rmet_3248
            BMA: BMA2714(hisD)
            BMV: BMASAVP1_A3239(hisD)
            BML: BMA10299_A1788(hisD)
            BMN: BMA10247_2765(hisD)
            BXE: Bxe_A0398 Bxe_C0309
            BVI: Bcep1808_0404
            BUR: Bcep18194_A3523
            BCN: Bcen_1517 Bcen_2682
            BCH: Bcen2424_0425 Bcen2424_6312
            BAM: Bamb_0343
            BPS: BPSL3139(hisD)
            BPM: BURPS1710b_3693(hisD)
            BPL: BURPS1106A_3724(hisD)
            BPD: BURPS668_3666(hisD)
            BTE: BTH_I2993(hisD)
            PNU: Pnuc_0107
            BPE: BP3768(hisD)
            BPA: BPP4267(hisD)
            BBR: BB4854(hisD)
            RFR: Rfer_2946
            POL: Bpro_0804
            PNA: Pnap_0696
            AAV: Aave_1024
            AJS: Ajs_0760
            VEI: Veis_0208 Veis_0769
            MPT: Mpe_A0831
            HAR: HEAR3069(hisD)
            MMS: mma_3288(hisD)
            NEU: NE0872(hisD)
            NET: Neut_1206
            NMU: Nmul_A0819
            EBA: ebA1299(hisD)
            AZO: azo0818(hisD)
            DAR: Daro_3387
            TBD: Tbd_1713
            MFA: Mfla_0248
            HHE: HH1721(hisD)
            WSU: WS1587(hisD)
            TDN: Tmden_0497
            CJE: Cj1598(hisD)
            CJR: CJE1770(hisD)
            CJJ: CJJ81176_1585(hisD)
            CJU: C8J_1500(hisD)
            CJD: JJD26997_1951(hisD)
            CFF: CFF8240_0519(hisD)
            CCV: CCV52592_0109(hisD)
            CHA: CHAB381_1216(hisD)
            CCO: CCC13826_2188(hisD)
            ABU: Abu_0384(hisD)
            NIS: NIS_0566(hisD)
            SUN: SUN_1800(hisD)
            GSU: GSU3100(hisD)
            GME: Gmet_0384
            GUR: Gura_4057
            PCA: Pcar_2688
            PPD: Ppro_3042
            DVU: DVU0796(hisD)
            DVL: Dvul_2178
            DDE: Dde_1008
            DPS: DP1282
            ADE: Adeh_0712
            AFW: Anae109_0753
            MXA: MXAN_4229(hisD)
            SAT: SYN_01792
            SFU: Sfum_3299
            PUB: SAR11_0475(hisD) SAR11_0801(hisD2)
            MLO: mll6456 mlr6649 mlr7107
            MES: Meso_0190 Meso_1928
            PLA: Plav_0521
            SME: SMa0398(hisD2) SMc02307(hisD1)
            SMD: Smed_0208 Smed_1713 Smed_4290 Smed_6310
            ATU: Atu0537(hisD)
            ATC: AGR_C_948
            RET: RHE_CH00581(hisD)
            RLE: RL0613(hisD) pRL80041(hisD)
            BME: BMEI1668
            BMF: BAB1_0285(hisD)
            BMS: BR0252(hisD)
            BMB: BruAb1_0280(hisD)
            BOV: BOV_0270(hisD)
            OAN: Oant_0326 Oant_3581
            BJA: blr1256(hisD)
            BRA: BRADO6637(hisD)
            BBT: BBta_0897(hisD)
            RPA: RPA4531(hisD)
            RPB: RPB_4350
            RPC: RPC_4417
            RPD: RPD_4279
            RPE: RPE_4484
            NWI: Nwi_0247
            NHA: Nham_0286
            XAU: Xaut_1231
            CCR: CC_2346
            SIL: SPO0594(hisD-1) SPO0981 SPOA0202(hisD-2)
            SIT: TM1040_3563
            RSP: RSP_0632(hisD1) RSP_2155(hisD)
            RSH: Rsph17029_0829 Rsph17029_2284
            RSQ: Rsph17025_0593
            JAN: Jann_1104 Jann_1398 Jann_2883
            RDE: RD1_1068(hisD) RD1_3808(hisD) RD1_3948(hisD)
            PDE: Pden_1091 Pden_1959 Pden_3579
            MMR: Mmar10_1614
            HNE: HNE_1346(hisD)
            ZMO: ZMO1551(hisD)
            NAR: Saro_2920
            SAL: Sala_2026
            SWI: Swit_2776
            ELI: ELI_02595
            GOX: GOX0991
            GBE: GbCGDNIH1_1031
            ACR: Acry_2693
            RRU: Rru_A2771
            MAG: amb3342
            MGM: Mmc1_1220
            ABA: Acid345_3683
            SUS: Acid_3855
            BSU: BG12599(hisD)
            BHA: BH3582(hisD)
            BAN: BA1426(hisD)
            BAR: GBAA1426(hisD)
            BAA: BA_1946
            BAT: BAS1317
            BCE: BC1406
            BCA: BCE_1526(hisD)
            BCZ: BCZK1291(hisD)
            BCY: Bcer98_1129
            BTK: BT9727_1290(hisD)
            BLI: BL03408(hisD)
            BLD: BLi03736(hisD)
            BCL: ABC1168 ABC3048(hisD)
            BAY: RBAM_032120(hisD)
            BPU: BPUM_3126(hisD)
            OIH: OB0551
            GKA: GK3075
            SAU: SA2470
            SAV: SAV2678
            SAM: MW2597
            SAR: SAR2760(hisD)
            SAS: SAS2563
            SAC: SACOL2702(hisD)
            SAB: SAB2554c(hisD)
            SAA: SAUSA300_2611(hisD)
            SAO: SAOUHSC_03013
            SAJ: SaurJH9_2702
            SAH: SaurJH1_2759
            SEP: SE0272
            SER: SERP2305(hisD)
            SSP: SSP0429
            LMO: lmo0567(hisD)
            LMF: LMOf2365_0596(hisD)
            LIN: lin0576(hisD)
            LWE: lwe0533(hisD)
            LLA: L0067(hisD)
            LLC: LACR_1332
            LLM: llmg_1295(hisD)
            SMU: SMU.1270(hisD)
            SSA: SSA_1446(hisD)
            SGO: SGO_1408(hisD)
            LPL: lp_2559(hisD)
            LCA: LSEI_1433
            STH: STH2837(hisD)
            CAC: CAC0937(hisD)
            CNO: NT01CX_1062(hisD)
            CTH: Cthe_2882
            CDF: CD1582(hisD)
            CBA: CLB_1587(hisD)
            CBH: CLC_1598(hisD)
            CBF: CLI_1649(hisD)
            CBE: Cbei_1317
            CKL: CKL_1295(hisD)
            AMT: Amet_0572
            CHY: CHY_1085(hisD)
            DSY: DSY3913
            DRM: Dred_2355
            SWO: Swol_1768
            CSC: Csac_2025
            TTE: TTE2138(hisD)
            MTA: Moth_2035
            MTU: Rv1599(hisD)
            MTC: MT1635(hisD)
            MBO: Mb1625(hisD)
            MBB: BCG_1637(hisD)
            MLE: ML1257(hisD)
            MPA: MAP1293(hisD)
            MAV: MAV_3187(hisD)
            MSM: MSMEG_2012(hisD) MSMEG_3205(hisD) MSMEG_5656(hisD)
            MVA: Mvan_2804
            MGI: Mflv_3613
            MMC: Mmcs_3063
            MKM: Mkms_3122
            MJL: Mjls_3079
            CGL: NCgl2021(cgl2102)
            CGB: cg2305(hisD)
            CEF: CE2003(hisD)
            CDI: DIP1566(hisD)
            CJK: jk0786(hisD)
            NFA: nfa18450(hisD)
            RHA: RHA1_ro01031(hisD1) RHA1_ro04557(hisD2)
            SCO: SCO2054(hisD)
            SMA: SAV6153(hisD)
            LXX: Lxx15120(hisD)
            ART: Arth_1585 Arth_4260
            AAU: AAur_1724(hisD)
            PAC: PPA1152
            NCA: Noca_3045
            TFU: Tfu_1150
            FRA: Francci3_3027
            FAL: FRAAL5004(hisD)
            ACE: Acel_1058
            KRA: Krad_2498 Krad_3181
            SEN: SACE_3119(hisD2) SACE_5778(hisD)
            STP: Strop_3196
            BLO: BL1295(hisD)
            BAD: BAD_1129(hisD)
            RXY: Rxyl_1102
            RBA: RB1584(hisD)
            LIL: LA2515(hisD)
            LIC: LIC11453(hisD)
            LBJ: LBJ_1668(hisD)
            LBL: LBL_1887(hisD)
            SYN: slr0682(hisD) slr1848(hisD)
            SYW: SYNW0610(hisD)
            SYC: syc2504_c(hisD)
            SYF: Synpcc7942_1519
            SYD: Syncc9605_2070
            SYE: Syncc9902_0602
            SYG: sync_2362(hisD)
            SYR: SynRCC307_1962(hisD)
            SYX: SynWH7803_2065(hisD)
            CYA: CYA_0591(hisD)
            CYB: CYB_0073(hisD)
            TEL: tll2252(hisD)
            GVI: gll1324(hisD)
            ANA: all1591(hisD) alr3056(hisD)
            AVA: Ava_0855 Ava_4204
            PMA: Pro1643(hisD)
            PMM: PMM1488(hisD)
            PMT: PMT1510(hisD)
            PMN: PMN2A_1019
            PMI: PMT9312_1581
            PMB: A9601_16921(hisD)
            PMC: P9515_16681(hisD)
            PMF: P9303_04331(hisD)
            PMG: P9301_16791(hisD)
            PMH: P9215_17571(hisD)
            PME: NATL1_18891(hisD)
            TER: Tery_2942
            BTH: BT_0201
            BFR: BF3189
            BFS: BF3029(hisD)
            SRU: SRU_2127(hisD)
            CHU: CHU_1861(hisD)
            GFO: GFO_1763(hisD)
            FJO: Fjoh_2877
            FPS: FP0959(hisD)
            CTE: CT0546(hisD)
            CCH: Cag_1289
            CPH: Cpha266_0801
            PVI: Cvib_0596
            PLT: Plut_0554
            DET: DET0844(hisD)
            DEH: cbdb_A826(hisD)
            DEB: DehaBAV1_0763
            RRS: RoseRS_3179
            RCA: Rcas_2906
            DRA: DR_2140
            DGE: Dgeo_0584
            TTH: TTC0370
            TTJ: TTHA0722
            AAE: aq_782(hisD)
            TMA: TM1041
            TPT: Tpet_1709
            MMP: MMP0968(hisD)
            MMQ: MmarC5_0791
            MMZ: MmarC7_0213
            MAE: Maeo_0863
            MVN: Mevan_0291
            MAC: MA3201(hisD)
            MBA: Mbar_A3507
            MMA: MM_0424
            MBU: Mbur_1103
            MTP: Mthe_0843
            MHU: Mhun_2531
            MEM: Memar_1876
            MBN: Mboo_2149
            MST: Msp_0134(hisD)
            MSI: Msm_1238
            MKA: MK0711(hisD)
            HAL: VNG1444G(hisD)
            HMA: rrnAC0272(hisD)
            HWA: HQ2720A(hisD)
            NPH: NP2876A(hisD)
            PTO: PTO1336
            PFU: PF1659
            TKO: TK0244
            RCI: RCIX41(hisD)
            IHO: Igni_0384
            SSO: SSO0599(hisD)
            STO: ST1464
            SAI: Saci_1579
            MSE: Msed_1947
            PAI: PAE0988(hisD)
            PIS: Pisl_1215
            PCL: Pcal_0136
            PAS: Pars_0167
STRUCTURES  PDB: 1K75  1KAE  1KAH  1KAR  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.23
            ExPASy - ENZYME nomenclature database: 1.1.1.23
            ExplorEnz - The Enzyme Database: 1.1.1.23
            ERGO genome analysis and discovery system: 1.1.1.23
            BRENDA, the Enzyme Database: 1.1.1.23
            CAS: 9028-27-7
///
ENTRY       EC 1.1.1.24                 Enzyme
NAME        quinate dehydrogenase;
            quinic dehydrogenase;
            quinate:NAD oxidoreductase;
            quinate 5-dehydrogenase;
            quinate:NAD+ 5-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-quinate:NAD+ 3-oxidoreductase
REACTION    L-quinate + NAD+ = 3-dehydroquinate + NADH + H+ [RN:R01872]
ALL_REAC    R01872
SUBSTRATE   L-quinate [CPD:C00296];
            NAD+ [CPD:C00003]
PRODUCT     3-dehydroquinate [CPD:C00944];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The enzyme is specific for quinate as substrate; phenylpyruvate,
            phenylalanine, cinnamate and shikimate will not act as substrates.
            NAD+ cannot be replaced by NADP+.
REFERENCE   1
  AUTHORS   Gamborg, O.L.
  TITLE     Aromatic metabolism in plants. III. Quinate dehydrogenase from mung
            bean cell suspension cultures.
  JOURNAL   Biochim. Biophys. Acta 128 (1966) 483-491.
  ORGANISM  Vigna radiata
REFERENCE   2  [PMID:13208693]
  AUTHORS   MITSUHASHI S, DAVIS BD.
  TITLE     Aromatic biosynthesis. XIII. Conversion of quinic acid to
            5-dehydroquinic acid by quinic dehydrogenase.
  JOURNAL   Biochim. Biophys. Acta. 15 (1954) 268-80.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K09484  quinate dehydrogenase
GENES       ANI: AN1137.2
            AFM: AFUA_1G11590
            AOR: AO090038000263
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.24
            ExPASy - ENZYME nomenclature database: 1.1.1.24
            ExplorEnz - The Enzyme Database: 1.1.1.24
            ERGO genome analysis and discovery system: 1.1.1.24
            BRENDA, the Enzyme Database: 1.1.1.24
            CAS: 9028-28-8
///
ENTRY       EC 1.1.1.25                 Enzyme
NAME        shikimate dehydrogenase;
            dehydroshikimic reductase;
            shikimate oxidoreductase;
            shikimate:NADP+ oxidoreductase;
            5-dehydroshikimate reductase;
            shikimate 5-dehydrogenase;
            5-dehydroshikimic reductase;
            DHS reductase;
            shikimate:NADP+ 5-oxidoreductase;
            AroE
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     shikimate:NADP+ 3-oxidoreductase
REACTION    shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ [RN:R02413]
ALL_REAC    R02413;
            (other) R02414
SUBSTRATE   shikimate [CPD:C00493];
            NADP+ [CPD:C00006]
PRODUCT     3-dehydroshikimate [CPD:C02637];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     NAD+ cannot replace NADP+ [3]. In higher organisms, this enzyme
            forms part of a multienzyme complex with EC 4.2.1.10,
            3-dehydroquinate dehydratase [4].
REFERENCE   1  [PMID:13686342]
  AUTHORS   BALINSKY D, DAVIES DD.
  TITLE     Aromatic biosynthesis in higher plants. 1. Preparation and
            properties of dehydroshikimic reductase.
  JOURNAL   Biochem. J. 80 (1961) 292-6.
  ORGANISM  Escherichia coli [GN:eco], Aerobacter aerogenes, Saccharomyces
            cerevisiae [GN:sce], Euglena gracilis, spinach, Pisum sativum
REFERENCE   2  [PMID:13208693]
  AUTHORS   MITSUHASHI S, DAVIS BD.
  TITLE     Aromatic biosynthesis. XIII. Conversion of quinic acid to
            5-dehydroquinic acid by quinic dehydrogenase.
  JOURNAL   Biochim. Biophys. Acta. 15 (1954) 268-80.
  ORGANISM  Aerobacter aerogenes
REFERENCE   3  [PMID:14367339]
  AUTHORS   YANIV H, GILVARG C.
  TITLE     Aromatic biosynthesis. XIV. 5-Dehydroshikimic reductase.
  JOURNAL   J. Biol. Chem. 213 (1955) 787-95.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:3883995]
  AUTHORS   Chaudhuri S, Coggins JR.
  TITLE     The purification of shikimate dehydrogenase from Escherichia coli.
  JOURNAL   Biochem. J. 226 (1985) 217-23.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:3277621]
  AUTHORS   Anton IA, Coggins JR.
  TITLE     Sequencing and overexpression of the Escherichia coli aroE gene
            encoding shikimate dehydrogenase.
  JOURNAL   Biochem. J. 249 (1988) 319-26.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:12837789]
  AUTHORS   Ye S, Von Delft F, Brooun A, Knuth MW, Swanson RV, McRee DE.
  TITLE     The crystal structure of shikimate dehydrogenase (AroE) reveals a
            unique NADPH binding mode.
  JOURNAL   J. Bacteriol. 185 (2003) 4144-51.
  ORGANISM  Haemophilus influenzae
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K00014  shikimate 5-dehydrogenase
GENES       OSA: 4325444 4325446
            CME: CMK269C
            SCE: YDR127W(ARO1)
            AGO: AGOS_AGR066W
            CAL: CaO19_4704(CaO19.4704)
            SPO: SPAC1834.02(aro1)
            AFM: AFUA_1G11630 AFUA_1G13740 AFUA_3G14790 AFUA_3G14800
                 AFUA_3G14830
            AOR: AO090012000502
            CNE: CNB01990
            UMA: UM03607.1
            ECO: b3281(aroE)
            ECJ: JW3242(aroE)
            ECE: Z4652(aroE)
            ECS: ECs4147
            ECC: c4042(aroE)
            ECI: UTI89_C3726(aroE)
            ECP: ECP_1639 ECP_3369
            ECV: APECO1_3165 APECO1_768(ydiB)
            ECW: EcE24377A_3764(aroE)
            ECX: EcHS_A3475
            STY: STY3924 STY4396(aroE)
            STT: t3664 t4103(aroE)
            SPT: SPA3268(aroE)
            SEC: SC3337(aroE) SC3772(skd)
            STM: STM3401(aroE) STM3859(aroE)
            YPE: YPO0246(aroE) YPO1610
            YPK: y1769 y4028(aroE)
            YPM: YP_0245(aroE1) YP_2244(aroE2)
            YPA: YPA_1912 YPA_3226
            YPN: YPN_2019 YPN_3822
            YPP: YPDSF_0169 YPDSF_1837
            YPS: YPTB2454(aroE) YPTB3660(aroE)
            YPI: YpsIP31758_3877(aroE)
            YEN: YE1700
            SFL: SF3313(aroE)
            SFX: S3537(aroE)
            SFV: SFV_3302(aroE)
            SSN: SSON_3422(aroE)
            SBO: SBO_3275(aroE)
            SDY: SDY_3458(aroE)
            ECA: ECA3995(aroE)
            PLU: plu4691(aroE)
            BUC: BU493(aroE)
            BAS: BUsg474(aroE)
            BAB: bbp437(aroE)
            BCC: BCc_312(aroE)
            SGL: SG2242
            ENT: Ent638_3713
            BFL: Bfl221(aroE)
            BPN: BPEN_228(aroE)
            HIN: HI0607
            HIT: NTHI0776(aroE) NTHI0862
            HIP: CGSHiEE_08935(aroE)
            HIQ: CGSHiGG_06600(aroE)
            HDU: HD0415(aroE)
            HSO: HS_0006(aroE)
            PMU: PM1271(aroE) PM1429
            MSU: MS0133(aroE) MS2315(aroE)
            APL: APL_1139(aroE)
            XFA: XF0624
            XFT: PD1532(aroE)
            XCC: XCC3953(aroE)
            XCB: XC_4041
            XCV: XCV4126(aroE)
            XAC: XAC4034(aroE)
            XOM: XOO_0372(XOO0372)
            VCH: VC0056
            VCO: VC0395_A2464(aroE)
            VVU: VV1_1057
            VVY: VV3215
            VPA: VP3033
            VFI: VF2535(aroE)
            PPR: PBPRA3571
            PAE: PA0025(aroE) PA0244
            PAU: PA14_00290(aroE) PA14_03020(aroE)
            PPU: PP_0074(aroE-1) PP_2406 PP_2608 PP_3002(aroE-2) PP_3768
            PST: PSPTO_0169(aroE) PSPTO_2348 PSPTO_2685
            PSB: Psyr_0025(aroE) Psyr_2132(aroE) Psyr_2418(aroE)
            PSP: PSPPH_0027(aroE) PSPPH_2107 PSPPH_2576
            PFL: PFL_0028(aroE) PFL_4005(aroE) PFL_5382(aroE)
            PFO: Pfl_0023 Pfl_3713(aroE) Pfl_4903
            PEN: PSEEN0031(aroE) PSEEN2020 PSEEN3214
            PAR: Psyc_0139(aroE)
            PCR: Pcryo_0150
            ACI: ACIAD0418(aroE)
            SON: SO_0040(aroE)
            SDN: Sden_0034
            SFR: Sfri_0034
            SAZ: Sama_0052
            SBL: Sbal_0040
            SLO: Shew_3727
            SPC: Sputcn32_0032
            SHE: Shewmr4_0037
            SHM: Shewmr7_0035
            SHN: Shewana3_0043
            SHW: Sputw3181_0032
            ILO: IL0024(aroE)
            CPS: CPS_0030(aroE)
            PHA: PSHAa0031(aroE)
            PAT: Patl_0031
            SDE: Sde_0026
            PIN: Ping_0071 Ping_3002
            MAQ: Maqu_0048
            CBU: CBU_0010(aroE)
            CBD: COXBU7E912_0135(aroE)
            LPN: lpg2808(aroE)
            LPF: lpl2723(aroE)
            LPP: lpp2854(aroE)
            MCA: MCA2794(aroE)
            FTU: FTT0238(aroE1) FTT0411c(aroE2)
            FTF: FTF0238(aroE1) FTF0411c(aroE2)
            FTL: FTL_0173 FTL_0481
            FTH: FTH_0167(aroE1) FTH_0479(aroE2)
            FTN: FTN_0078(aroE) FTN_0511
            TCX: Tcr_0153
            NOC: Noc_2575
            AEH: Mlg_2825
            HHA: Hhal_1054
            HCH: HCH_00037(aroE)
            CSA: Csal_0293 Csal_2862
            ABO: ABO_0136(aroE)
            MMW: Mmwyl1_0070
            AHA: AHA_0266(aroE)
            DNO: DNO_0509(aroE)
            BCI: BCI_0418(aroE)
            RMA: Rmag_0435
            VOK: COSY_0405(aroE)
            NME: NMB0358
            NMA: NMA2129(aroE)
            NGO: NGO1602
            CVI: CV_3587(aroE)
            RSO: RSc2777(aroE1) RSp1398(aroE)
            REU: Reut_A2855 Reut_B5029
            REH: H16_A3161(aroE)
            RME: Rmet_3054
            BMA: BMA2494(aroE) BMAA0850
            BMV: BMASAVP1_1754 BMASAVP1_A0414(aroE)
            BML: BMA10299_2208 BMA10299_A1274(aroE)
            BMN: BMA10247_3291(aroE) BMA10247_A0893
            BXE: Bxe_A0539 Bxe_B0884 Bxe_C0879
            BVI: Bcep1808_0587 Bcep1808_4752
            BUR: Bcep18194_A3695 Bcep18194_B0345(aroE)
            BCN: Bcen_0130 Bcen_3064 Bcen_5532
            BCH: Bcen2424_0613 Bcen2424_5303 Bcen2424_5896
            BAM: Bamb_0514 Bamb_4664 Bamb_5913 Bamb_6532
            BPS: BPSL2976(aroE) BPSS0341(aroE)
            BPM: BURPS1710b_3493(aroE) BURPS1710b_A1897(aroE)
            BPL: BURPS1106A_3496(aroE) BURPS1106A_A0483(aroE)
            BPD: BURPS668_3458(aroE) BURPS668_A0580(aroE)
            BTE: BTH_I1171(aroE) BTH_II2057
            PNU: Pnuc_0217
            BPE: BP3004(aroE)
            BPA: BPP3924(aroE)
            BBR: BB4397(aroE)
            RFR: Rfer_3413
            POL: Bpro_1087 Bpro_1847 Bpro_4495 Bpro_4503
            PNA: Pnap_1555 Pnap_1561 Pnap_1649 Pnap_2706 Pnap_3407
            AAV: Aave_0841
            AJS: Ajs_3656
            VEI: Veis_2197
            MPT: Mpe_A3201
            HAR: HEAR2753(aroE)
            MMS: mma_2962
            NEU: NE1627(aroE1)
            NET: Neut_0496
            NMU: Nmul_A0538
            EBA: ebA1735(aroE)
            AZO: azo0707(aroE)
            DAR: Daro_3907
            TBD: Tbd_2504
            MFA: Mfla_2445
            HPY: HP1249(aroE)
            HPJ: jhp1170(aroE)
            HPA: HPAG1_1192
            HHE: HH1247(aroE)
            HAC: Hac_0244(aroE)
            WSU: WS2168(aroE)
            TDN: Tmden_1278
            CJE: Cj0405(aroE)
            CJR: CJE0454(aroE)
            CJJ: CJJ81176_0429(aroE)
            CJU: C8J_0380(aroE)
            CJD: JJD26997_1552(aroE)
            CFF: CFF8240_1138(aroE)
            CCV: CCV52592_1353(aroE)
            CHA: CHAB381_1649(aroE)
            CCO: CCC13826_0229(aroE) CCC13826_1951
            ABU: Abu_1073(aroE)
            NIS: NIS_1181(aroE)
            SUN: SUN_0470(aroE)
            GSU: GSU1490(aroE)
            GME: Gmet_1392
            PCA: Pcar_2150 Pcar_2192
            DVU: DVU0115(aroE)
            DDE: Dde_3564
            BBA: Bd1508(aroE)
            DPS: DP3012
            ADE: Adeh_0185
            SAT: SYN_01937
            SFU: Sfum_2721 Sfum_2761
            PUB: SAR11_0341(aroE)
            MLO: mlr4492
            MES: Meso_3480
            SME: SMb20037(aroE) SMc02791(aroE1)
            ATU: Atu0003(aroE) Atu4295(aroE) Atu4532(aroE)
            ATC: AGR_C_3 AGR_L_1139 AGR_L_673
            RET: RHE_CH00003(aroEch1) RHE_CH02291(aroEch2) RHE_PC00214(aroEc)
            RLE: RL0003 RL2845(aroE) RL2847 pRL110081
            BME: BMEI2058 BMEII0871
            BMF: BAB1_2070 BAB2_0033 BAB2_0825
            BMS: BR2069(aroE)
            BMB: BruAb1_2044(aroE) BruAb2_0034 BruAb2_0804
            BOV: BOV_1989(aroE)
            BJA: bll1059(aroE) bll3660 bll6391(aroE) bll6392 bll7412(aroE)
                 blr2257(aroE) blr3543 blr3858
            BRA: BRADO0968 BRADO2346(aroE) BRADO5598 BRADO5961(aroE)
            BBT: BBta_1809(aroE) BBta_6119 BBta_7088
            RPA: RPA4325(aroE)
            RPB: RPB_1302
            RPC: RPC_4117
            RPD: RPD_3919
            RPE: RPE_4171
            NWI: Nwi_2977
            NHA: Nham_1109
            BHE: BH00030(aroE)
            BQU: BQ00030(aroE)
            BBK: BARBAKC583_0006(aroE)
            CCR: CC_0003
            SIL: SPO2425 SPO3891(aroE)
            SIT: TM1040_2860
            RSP: RSP_1234(aroE)
            JAN: Jann_0196
            RDE: RD1_0438(aroE)
            PDE: Pden_4664
            MMR: Mmar10_2976
            HNE: HNE_0003(aroE)
            ZMO: ZMO0041(aroE)
            NAR: Saro_0115 Saro_1590
            SAL: Sala_2840
            ELI: ELI_12990
            GOX: GOX0859 GOX1959
            GBE: GbCGDNIH1_2144
            RRU: Rru_A3613
            MAG: amb4547
            MGM: Mmc1_0022
            SUS: Acid_7159
            BSU: BG11522(aroD)
            BHA: BH1324(aroD)
            BAN: BA4561(aroE)
            BAR: GBAA4561(aroE)
            BAA: BA_5005
            BAT: BAS4232
            BCE: BC4331(aroE)
            BCA: BCE_4415(aroE)
            BCZ: BCZK4080(aroE)
            BTK: BT9727_4070(aroE)
            BTL: BALH_3922(aroE)
            BLI: BL02079(aroD)
            BLD: BLi02759(aroD)
            BCL: ABC1638(aroD)
            BAY: RBAM_008060 RBAM_008070 RBAM_023960
            BPU: BPUM_2300 BPUM_3656
            OIH: OB1987
            GKA: GK2524(aroE)
            SAU: SA1424(aroE)
            SAV: SAV1596(aroE)
            SAM: MW1547(aroE)
            SAR: SAR1673(aroE)
            SAS: SAS1533
            SAC: SACOL1652(aroE)
            SAB: SAB1468c(aroE)
            SAA: SAUSA300_1555(aroE)
            SAO: SAOUHSC_01699
            SEP: SE1282
            SER: SERP1163(aroE)
            SHA: SH1319(aroE)
            SSP: SSP1162
            LMO: lmo0490 lmo1490 lmo2236
            LMF: LMOf2365_0520(aroE) LMOf2365_1509(aroE-2) LMOf2365_2269
            LIN: lin0493 lin1525 lin2338
            LWE: lwe0461 lwe1503(aroE)
            LLA: L0061(aroE)
            LLC: LACR_1921
            LLM: llmg_1939(aroE)
            SPY: SPy_0534(aroE.2) SPy_1584(aroE)
            SPZ: M5005_Spy_0441(aroE.2) M5005_Spy_1303(aroE)
            SPM: spyM18_0600(aroD) spyM18_1592(aroE)
            SPG: SpyM3_0378(aroE.2) SpyM3_1284(aroE.1)
            SPS: SPs0577 SPs1475
            SPH: MGAS10270_Spy0442(aroE2) MGAS10270_Spy1418(aroE)
            SPI: MGAS10750_Spy0461(aroE2) MGAS10750_Spy1412(aroE)
            SPJ: MGAS2096_Spy0460(aroE2) MGAS2096_Spy1323(aroE)
            SPK: MGAS9429_Spy0440(aroE2) MGAS9429_Spy1297(aroE)
            SPF: SpyM50552(aroE)
            SPA: M6_Spy0475 M6_Spy1321
            SPB: M28_Spy0429(aroE.2) M28_Spy1344(aroE)
            SPN: SP_1376
            SPR: spr1234(aroE)
            SPD: SPD_1210(aroE)
            SAG: SAG1680(aroE)
            SAN: gbs1724
            SAK: SAK_1692(aroE)
            SMU: SMU.778(aroE)
            STC: str0639(aroE)
            STL: stu0639(aroE)
            SSA: SSA_1469(aroE)
            SGO: SGO_1374(aroE)
            LPL: lp_1084(aroD1) lp_3494(aroE) lp_3498(aroD3) lp_3499(aroD4)
            LSA: LSA0892(aroE)
            LSL: LSL_1795(aroE)
            LCA: LSEI_0476 LSEI_0478
            EFA: EF1561(aroE)
            STH: STH1952
            CAC: CAC0897(aro)
            CPE: CPE0700(aroE)
            CPF: CPF_0693(aroE)
            CPR: CPR_0693(aroE)
            CTC: CTC01117
            CNO: NT01CX_0621(aroE)
            CDF: CD1837(aroE)
            CBA: CLB_2416(aroE)
            CBH: CLC_2398(aroE)
            CBF: CLI_2602(aroE)
            CKL: CKL_0790(aroE1) CKL_1008(aroE2) CKL_1014(aroE3)
            CHY: CHY_0623(aroE)
            DSY: DSY2394
            TTE: TTE1261(aroE)
            MTA: Moth_1558
            MTU: Rv2552c(aroE)
            MTC: MT2629(aroE)
            MBO: Mb2582c(aroE)
            MBB: BCG_2575c(aroE)
            MLE: ML0515(aroE)
            MPA: MAP1080(aroE)
            MAV: MAV_3428(aroE)
            MSM: MSMEG_3028(aroE) MSMEG_5457
            MVA: Mvan_4817
            MGI: Mflv_1916
            MMC: Mmcs_2349 Mmcs_4283
            MKM: Mkms_4369
            MJL: Mjls_4662
            CGL: NCgl0409(aroE) NCgl1087(aroE) NCgl1567(cgl1629)
            CGB: cg0504(aroE) cg1283(aroE) cg1835(aroE3)
            CEF: CE0443(aroE) CE1194 CE1745
            CDI: DIP1006 DIP1347
            CJK: jk1035(aroE)
            NFA: nfa36410
            RHA: RHA1_ro01342(aroE1) RHA1_ro01564(aroE2) RHA1_ro01853(aroE3)
                 RHA1_ro07138(aroE4)
            SCO: SCO1498(aroE)
            SMA: SAV1777(aroE2) SAV6853(aroE1)
            TWH: TWT373(aroE)
            TWS: TW396(aroE)
            LXX: Lxx00310(aroE) Lxx10940(aroE)
            ART: Arth_2889 Arth_3498 Arth_4080
            AAU: AAur_2278(aroE) AAur_2878(aroE) AAur_4046(aroE)
            PAC: PPA1181
            NCA: Noca_2410
            TFU: Tfu_2067
            FRA: Francci3_0433 Francci3_3211
            FAL: FRAAL0918 FRAAL5249(aroE)
            SEN: SACE_2055(aroE) SACE_2867(rifI)
            BLO: BL0704(aroE)
            BAD: BAD_0838(aroE)
            RXY: Rxyl_1362
            FNU: FN0044 FN0045
            RBA: RB6488
            CTR: CT370(aroE)
            CTA: CTA_0402(aroE)
            CMU: TC0649
            CPN: CPn1035(aroE)
            CPA: CP0817
            CPJ: CPj1035(aroE)
            CPT: CpB1075
            CCA: CCA00727(aroE)
            CAB: CAB694(aroE)
            CFE: CF0289(aroE)
            LIL: LA0638(aroE)
            LIC: LIC12949(aroE)
            LBJ: LBJ_2329(aroE)
            LBL: LBL_0779(aroE)
            SYN: slr1559(aroE)
            SYW: SYNW2509(aroE)
            SYC: syc1637_d(aroE)
            SYF: Synpcc7942_2467
            SYD: Syncc9605_2675
            SYE: Syncc9902_2304
            SYG: sync_2924(aroE)
            SYR: SynRCC307_2518(aroE)
            SYX: SynWH7803_2515(aroE)
            CYA: CYA_2729(aroE)
            CYB: CYB_1006(aroE)
            TEL: tll0590(aroE)
            GVI: gll3278(aroE)
            ANA: alr2057(aroK)
            AVA: Ava_3106(aroE)
            PMA: Pro1872(aroE)
            PMM: PMM1705(aroE)
            PMT: PMT2257(aroE)
            PMN: PMN2A_1314
            PMI: PMT9312_1798
            PMB: A9601_19151(aroE)
            PMC: P9515_18961(aroE)
            PMF: P9303_30051(aroE)
            PMG: P9301_18961(aroE)
            PME: NATL1_21871(aroE)
            TER: Tery_2187
            BTH: BT_4215
            BFR: BF0916
            BFS: BF0838(aroE)
            PGI: PG0978(aroE)
            SRU: SRU_2277(aroE)
            CHU: CHU_0006(aroE)
            GFO: GFO_0767(aroE)
            FPS: FP1769(aroE)
            CTE: CT1809(aroE)
            CCH: Cag_1345
            PLT: Plut_0483
            DET: DET0465(aroE)
            DEH: cbdb_A429(aroE)
            DRA: DR_0077 DR_1173
            DGE: Dgeo_1271 Dgeo_2374
            TTH: TTC0688
            TTJ: TTHA1050
            AAE: aq_901(aroE)
            TMA: TM0346
            MMP: MMP0936(aroE)
            MAE: Maeo_0450
            MAC: MA4594(aroE)
            MBA: Mbar_A0923
            MMA: MM_1274
            MBU: Mbur_1998
            MTP: Mthe_1501
            MHU: Mhun_1030
            MST: Msp_0647(aroE)
            MSI: Msm_1179
            MKA: MK0117(aroE)
            HAL: VNG0382G(aroE)
            HMA: rrnAC0707(aroE)
            HWA: HQ1245A(aroE)
            NPH: NP0806A(aroE)
            TAC: Ta0284
            TVO: TVN1317
            PTO: PTO0600(aroE)
            PAB: PAB0300(aroE)
            PFU: PF1693
            TKO: TK0265
            RCI: RCIX1312(aroE)
            APE: APE_0574.1
            SSO: SSO0306(aroE)
            STO: ST2273
            SAI: Saci_0185(aroE)
            PAI: PAE1913(aroE)
STRUCTURES  PDB: 1NPD  1NVT  1NYT  1O9B  1P74  1P77  1VI2  1WXD  2CY0  2D5C  
                 2EV9  2GPT  2HK7  2HK8  2HK9  2NLO  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.25
            ExPASy - ENZYME nomenclature database: 1.1.1.25
            ExplorEnz - The Enzyme Database: 1.1.1.25
            ERGO genome analysis and discovery system: 1.1.1.25
            BRENDA, the Enzyme Database: 1.1.1.25
            CAS: 9026-87-3
///
ENTRY       EC 1.1.1.26                 Enzyme
NAME        glyoxylate reductase;
            NADH-glyoxylate reductase;
            glyoxylic acid reductase;
            NADH-dependent glyoxylate reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     glycolate:NAD+ oxidoreductase
REACTION    glycolate + NAD+ = glyoxylate + NADH + H+ [RN:R00717]
ALL_REAC    R00717;
            (other) R01388
SUBSTRATE   glycolate [CPD:C00160];
            NAD+ [CPD:C00003]
PRODUCT     glyoxylate [CPD:C00048];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Reduces glyoxylate to glycolate or hydroxypyruvate to D-glycerate.
REFERENCE   1
  AUTHORS   Zelitch, I.
  TITLE     Oxidation and reduction of glycolic and glyoxylic acids in plants.
            II. Glyoxylic acid reductase.
  JOURNAL   J. Biol. Chem. 201 (1953) 719-726.
  ORGANISM  spinach
REFERENCE   2
  AUTHORS   Zelitch, I.
  TITLE     The isolation and action of crystalline glyoxylic acid reductase
            from tobacco leaves.
  JOURNAL   J. Biol. Chem. 216 (1955) 553-575.
  ORGANISM  Nicotiana tabacum
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K00015  glyoxylate reductase
GENES       HSA: 9380(GRHPR)
            CME: CMQ289C
            UMA: UM04061.1
            AHA: AHA_3354
            BUR: Bcep18194_A4216 Bcep18194_B1307
            BPM: BURPS1710b_2926
            BPL: BURPS1106A_0151(gyaR)
            BPD: BURPS668_2809
            HAR: HEAR0804
            PLA: Plav_2807 Plav_3643
            SMD: Smed_3380
            RLE: RL0145(gyaR) pRL110162(gyaR)
            OAN: Oant_0734
            BRA: BRADO0066 BRADO3050
            BBT: BBta_0073 BBta_5085
            RPB: RPB_0616
            RPE: RPE_0244
            NHA: Nham_0045
            XAU: Xaut_4126
            SIT: TM1040_0480
            RSH: Rsph17029_0987
            RSQ: Rsph17025_2187
            JAN: Jann_0915
            RDE: RD1_1164(gyaR) RD1_3437(gyaR) RD1_4247(gyaR)
            PDE: Pden_1941
            HNE: HNE_3433(gyaR)
            NAR: Saro_2308
            SAL: Sala_0778
            SWI: Swit_4583
            RRU: Rru_A1815 Rru_A3790
            CKL: CKL_0922(gyaR)
            MSM: MSMEG_0604 MSMEG_2529 MSMEG_2550 MSMEG_6299
            RHA: RHA1_ro04923
            AAU: AAur_4149
            AVA: Ava_4238
            PMG: P9301_12531
            RRS: RoseRS_0216
            RCA: Rcas_4324
            FNO: Fnod_1147
            PHO: PH0597
            PAB: PAB2374(gdh-like)
            PFU: PF0319
            TKO: TK0683
            APE: APE_1265.1 APE_1831.1 APE_2507.1
            MSE: Msed_0256
            TPE: Tpen_0823
STRUCTURES  PDB: 2DBQ  2DBR  2DBZ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.26
            ExPASy - ENZYME nomenclature database: 1.1.1.26
            ExplorEnz - The Enzyme Database: 1.1.1.26
            ERGO genome analysis and discovery system: 1.1.1.26
            BRENDA, the Enzyme Database: 1.1.1.26
            CAS: 9028-32-4
///
ENTRY       EC 1.1.1.27                 Enzyme
NAME        L-lactate dehydrogenase;
            lactic acid dehydrogenase;
            L(+)-nLDH;
            L-(+)-lactate dehydrogenase;
            L-lactic dehydrogenase;
            L-lactic acid dehydrogenase;
            lactate dehydrogenase;
            lactate dehydrogenase NAD+-dependent;
            lactic dehydrogenase;
            NAD+-lactate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-lactate:NAD+ oxidoreductase
REACTION    (S)-lactate + NAD+ = pyruvate + NADH + H+ [RN:R00703]
ALL_REAC    R00703;
            (other) R01000 R03104
SUBSTRATE   (S)-lactate [CPD:C00186];
            NAD+ [CPD:C00003]
PRODUCT     pyruvate [CPD:C00022];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also
            acts, more slowly, with the animal, but not the bacterial, enzyme.
REFERENCE   1  [PMID:13815938]
  AUTHORS   DENNIS D, KAPLAN NO.
  TITLE     D- and L-lactic acid dehydrogenases in Lactobacillus plantarum.
  JOURNAL   J. Biol. Chem. 235 (1960) 810-8.
  ORGANISM  Lactobacillus plantarum [GN:lpl]
REFERENCE   2  [PMID:4146647]
  AUTHORS   Adams MJ, Buehner M, Chandrasekhar K, Ford GC, Hackert ML, Liljas A,
            Rossmann MG, Smiley IE, Allison WS, Everse J, Kaplan NO, Taylor SS.
  TITLE     Structure-function relationships in lactate dehydrogenase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 70 (1973) 1968-72.
  ORGANISM  Squalus acanthius
REFERENCE   3
  AUTHORS   Holbrook, J.J., Liljas, A., Steindel, S.J. and Rossmann, M.G.
  TITLE     Lactate dehydrogenase.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 11, Academic
            Press, New York, 1975, p. 191-292.
REFERENCE   4  [PMID:114469]
  AUTHORS   Schar HP, Zuber H.
  TITLE     Structure and function of L-lactate dehydrogenases from thermophilic
            and mesophilic bacteria. I) Isolation and characterization of
            lactate dehydrogenases from thermophilic and mesophilic bacilli.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 360 (1979) 795-807.
  ORGANISM  Bacillus stearothermophilus, Bacillus caldotenax, Bacillus subtilis
            [GN:bsu]
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00272  Cysteine metabolism
            PATH: map00620  Pyruvate metabolism
            PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K00016  L-lactate dehydrogenase
GENES       HSA: 160287(LDHAL6A) 3939(LDHA) 3945(LDHB) 3948(LDHC)
                 92483(LDHAL6B)
            PTR: 451063(LDHA)
            MCC: 696854(LDHA)
            MMU: 106557(Ldhal6b) 16828(Ldha) 16832(Ldhb) 16833(Ldhc)
            RNO: 24533(Ldha) 24534(Ldhb) 29634(Ldhc) 369018(Ldhal6b)
            CFA: 476882(LDHA) 476883(LDHC) 477883(LOC477883) 479371(LOC479371)
                 482405(LOC482405) 484048(LDHAL6B) 490690(LOC490690)
                 609013(LOC609013) 610330(LOC610330) 611702(LOC611702)
            BTA: 281274(LDHA) 281275(LDHB)
            GGA: 373997(LDHB) 396221(LDHA)
            XLA: 380394(ldha) 380546(ldh2) 394355(ldha-B) 398121(ldha1)
            XTR: 394477(ldhb) 394758(ldha)
            DRE: 30496(ldha) 30497(ldhb)
            SPU: 586683(LOC586683)
            DME: Dmel_CG10160(ImpL3)
            CEL: F13D12.2(ldh-1)
            ATH: AT4G17260
            OSA: 4328012 4339856
            CME: CMA145C CMC188C CMI306C CMJ002C CMK006C
            SPO: SPAC186.08c
            ANI: AN5842.2
            AFM: AFUA_5G14800
            PFA: PF13_0141 PF13_0144
            ECI: UTI89_C4637
            ECV: APECO1_2404
            VVU: VV2_1457
            VVY: VVA0276
            VPA: VPA0147
            REH: H16_A0666(ldh)
            RME: Rmet_0559
            BPE: BP0379(ldh)
            BPA: BPP4051(ldh)
            BBR: BB4524(ldh) BB4684
            HHE: HH1571(mdh)
            CJE: Cj1167(ldh)
            CJR: CJE1301(ldh)
            CJJ: CJJ81176_1182(ldh)
            CJU: C8J_1111(ldh)
            DVU: DVU0600(ldh)
            OTS: OTBS_1845(mdh)
            RLE: pRL120231
            ABA: Acid345_1483
            BSU: BG19003(ldh)
            BHA: BH3937(lctE)
            BAN: BA1923(ldh-1) BA5125(ldh-2) BA5240(ldh-3)
            BAR: GBAA1923(ldh-1) GBAA5125(ldh-2) GBAA5240(ldh-3)
            BAA: BA_0106 BA_2427
            BAT: BAS1784 BAS4762 BAS4869
            BCE: BC1924(ldh) BC4870(ldh) BC4996(ldh)
            BCA: BCE_2007(ldh) BCE_5032(ldh) BCE_5135(ldh)
            BCZ: BCZK1741(ldh) BCZK4624(ldh) BCZK4723(ldh)
            BTK: BT9727_1763(ldh) BT9727_4600(ldh) BT9727_4708(ldh)
            BTL: BALH_1702(ldh) BALH_4435(ldhP) BALH_4532(ldhB)
            BLI: BL01703(ldh)
            BLD: BLi00366(ldh)
            BCL: ABC2872(ldh)
            BAY: RBAM_003290(ldh)
            BPU: BPUM_0277(ldh)
            OIH: OB3279
            GKA: GK0475(ldh)
            GTN: GTNG_0487(ldh)
            SAU: SA0232(lctE) SA2395
            SAV: SAV0241(lctE) SAV2602
            SAM: MW0217(lctE) MW2521
            SAR: SAR0234(ldh1) SAR2680(ldh2)
            SAS: SAS0217 SAS2487
            SAC: SACOL0222(ldh1) SACOL2618(ldh2)
            SAB: SAB0180 SAB2475c(ldh)
            SAA: SAUSA300_0235 SAUSA300_2537
            SAO: SAOUHSC_00206 SAOUHSC_02922
            SEP: SE2145
            SER: SERP2156(ldh)
            SHA: SH0525
            SSP: SSP0249 SSP1001
            LMO: lmo0210(ldh) lmo1534 lmo1667
            LMF: LMOf2365_0221(ldh-1) LMOf2365_1553(ldh-2) LMOf2365_1691
            LIN: lin0242(ldh) lin1569 lin1775
            LWE: lwe0172(ldh) lwe1034 lwe1547(ldhB)
            LLA: L0017(ldh) L0018(ldhB) L142159(ldhX)
            LLC: LACR_0421 LACR_1239 LACR_1455
            LLM: llmg_0392(ldhB) llmg_1120(ldh) llmg_1429(ldhX)
            SPY: SPy_1151(ldh)
            SPZ: M5005_Spy_0873(ldh)
            SPM: spyM18_1111(ldh)
            SPG: SpyM3_0809(ldh)
            SPS: SPs1008
            SPH: MGAS10270_Spy0987(ldh)
            SPI: MGAS10750_Spy1022(ldh)
            SPJ: MGAS2096_Spy0947(ldh)
            SPK: MGAS9429_Spy0991(ldh)
            SPF: SpyM50917(ldh)
            SPA: M6_Spy0869
            SPB: M28_Spy0847(ldh)
            SPN: SP_1220
            SPR: spr1100(ldh)
            SPD: SPD_1078(ldh)
            SAG: SAG0128 SAG0959(ldh)
            SAN: gbs0126 gbs0947
            SAK: SAK_0179 SAK_1054
            SMU: SMU.1115(ldh)
            STC: str0644(hdhL) str1280(ldh)
            STL: stu0644(hdhL) stu1280(ldh)
            STE: STER_1257
            SSA: SSA_1221(ldh)
            SGO: SGO_1232
            LPL: lp_0537(ldhL1) lp_1101(ldhL2) lp_2349(hicD3)
            LJO: LJ0274 LJ1403
            LAC: LBA0271 LBA0910(citH)
            LSA: LSA1606(ldh)
            LSL: LSL_1362(ldh)
            LDB: Ldb0120(ldh)
            LBU: LBUL_0100
            LBR: LVIS_0514
            LCA: LSEI_0634 LSEI_2549 LSEI_2607
            LGA: LGAS_0269
            PPE: PEPE_1554
            EFA: EF0255(ldh-1) EF0641(ldh-2)
            CAC: CAC0267 CAC3552
            CPE: CPE0103(ldh)
            CPF: CPF_0098(ldh)
            CPR: CPR_0102(ldh)
            CTC: CTC01998(ldh)
            CNO: NT01CX_0236
            CTH: Cthe_1053
            CDF: CD2164(ldh)
            CBO: CBO1519(ldh)
            CBA: CLB_1540(ldh)
            CBH: CLC_1552(ldh)
            CBF: CLI_1599(ldh)
            CSC: Csac_1027
            MTA: Moth_1826
            MGE: MG_460(ldh)
            MPN: MPN674(ldh)
            MPU: MYPU_7590(ldh)
            MPE: MYPE9640
            MGA: MGA_0746(mdh)
            MMY: MSC_0532(ldh)
            MMO: MMOB0410(ldh)
            MHY: mhp245(ictD) mhp469(ldh)
            MHJ: MHJ_0133(ldh)
            MHP: MHP7448_0137(ldh)
            MSY: MS53_0461(ldh)
            MCP: MCAP_0439(ldh)
            MFL: Mfl596
            MMC: Mmcs_0382
            CGL: NCgl2810(ldh)
            CGB: cg3219(ldh)
            CEF: CE2753
            CDI: DIP0427 DIP2255(ldh)
            CJK: jk0113(ldh)
            SMA: SAV339(ldhA)
            PAC: PPA0012 PPA0887 PPA1952
            BLO: BL0710(ldh1) BL1308(ldh2)
            BAD: BAD_1117(ldh2)
            FNU: FN1169
            RBA: RB2566(ldh) RB856(ldh)
            BBU: BB0087(ldh)
            BGA: BG0088(ldh)
            BAF: BAPKO_0088(ldh)
            TDE: TDE0351(ldh)
            LIL: LA1488
            CYA: CYA_2670
            CYB: CYB_2165
            GVI: gll3324
            SRU: SRU_0681
            CCH: Cag_0862
            DRA: DR_2364
            TTH: TTC0748
            TTJ: TTHA1113
            TMA: TM1867
            TPT: Tpet_0930
            MAE: Maeo_0610
            MHU: Mhun_2343
            MEM: Memar_2444
            MBN: Mboo_0492
STRUCTURES  PDB: 1A5Z  1CEQ  1CET  1EZ4  1HYE  1HYG  1HYH  1I0Z  1I10  1LDB  
                 1LDG  1LDM  1LDN  1LLC  1LLD  1LTH  1OC4  1PZE  1PZF  1PZG  
                 1PZH  1SOV  1SOW  1T24  1T25  1T26  1T2C  1T2D  1T2E  1T2F  
                 1U4O  1U4S  1U5A  1U5C  1V6A  1VBI  1X0A  1XIV  1Y6J  2A92  
                 2A94  2AA3  2EWD  2FM3  2FN7  2FNZ  2FRM  2LDB  2LDX  2V65  
                 2V6B  2V6M  2V7P  3LDH  5LDH  6LDH  8LDH  9LDB  9LDT  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.27
            ExPASy - ENZYME nomenclature database: 1.1.1.27
            ExplorEnz - The Enzyme Database: 1.1.1.27
            ERGO genome analysis and discovery system: 1.1.1.27
            BRENDA, the Enzyme Database: 1.1.1.27
            CAS: 9001-60-9
///
ENTRY       EC 1.1.1.28                 Enzyme
NAME        D-lactate dehydrogenase;
            lactic acid dehydrogenase;
            lactic acid dehydrogenase;
            D-specific lactic dehydrogenase;
            D-(-)-lactate dehydrogenase (NAD+);
            D-lactic acid dehydrogenase;
            D-lactic dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-lactate:NAD+ oxidoreductase
REACTION    (R)-lactate + NAD+ = pyruvate + NADH + H+ [RN:R00704]
ALL_REAC    R00704
SUBSTRATE   (R)-lactate [CPD:C00256];
            NAD+ [CPD:C00003]
PRODUCT     pyruvate [CPD:C00022];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13815938]
  AUTHORS   DENNIS D, KAPLAN NO.
  TITLE     D- and L-lactic acid dehydrogenases in Lactobacillus plantarum.
  JOURNAL   J. Biol. Chem. 235 (1960) 810-8.
  ORGANISM  Lactobacillus plantarum [GN:lpl]
PATHWAY     PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K00017  D-lactate dehydrogenase
            KO: K03777  D-lactate dehydrogenase
            KO: K03778  D-lactate dehydrogenase
GENES       HSA: 197257(LDHD)
            MMU: 52815(Ldhd)
            CFA: 610390(LDHD)
            DRE: 334208(ldhd)
            SPU: 591812(LOC591812)
            ANI: AN0628.2
            AFM: AFUA_1G17040
            AOR: AO090023000577
            CNE: CNA08110
            TET: TTHERM_01014570
            ECO: b1380(ldhA) b2133(dld)
            ECJ: JW1375(ldhA) JW2121(dld)
            ECE: Z2329(ldhA) Z3382(dld)
            ECS: ECs2002 ECs3020
            ECC: c1827(ldhA) c2664(dld)
            ECI: UTI89_C1623(ldhA) UTI89_C2407(dld)
            ECP: ECP_1406 ECP_2172
            ECV: APECO1_4416(dld) APECO1_554(ldhA)
            ECW: EcE24377A_1565(idhA) EcE24377A_2423(dld)
            ECX: EcHS_A1467 EcHS_A2268
            STY: STY1422(ldhA) STY2397(dld)
            STT: t0688(dld) t1550(ldhA)
            SPT: SPA0684(dld) SPA1239(ldhA)
            SEC: SC1642(ldhA) SC2183(dld)
            STM: STM1647(ldhA) STM2167(dld)
            YPE: YPO1177(dld) YPO2329(ldhA)
            YPK: y2004(ldhA) y3012(dld)
            YPM: YP_0960(dld) YP_2115(ldhA1)
            YPA: YPA_0888 YPA_1678
            YPN: YPN_1788 YPN_2800
            YPP: YPDSF_0817 YPDSF_2519
            YPS: YPTB1218(dld) YPTB2248(ldhA)
            YPI: YpsIP31758_1808(ldhA) YpsIP31758_2805(dld)
            SFL: SF1814(ldhA) SF2218(dld)
            SFX: S1459(ldhA) S2347(dld)
            SFV: SFV_1805(ldhA) SFV_2209(dld)
            SSN: SSON_1744(ldhA) SSON_2190(dld)
            SBO: SBO_1011(dld) SBO_1686(ldhA)
            SDY: SDY_1464(ldhA) SDY_2155(dld)
            ECA: ECA2000(ldhA) ECA3181(dld)
            PLU: plu2145(ldhA) plu2848(dld)
            ENT: Ent638_1942 Ent638_2732
            KPN: KPN_01449(ldhA)
            SPE: Spro_1364
            HIN: HI0085(ldhA) HI1649(dld)
            HIT: NTHI0099(ddh) NTHI1952(dld)
            HIP: CGSHiEE_03815
            HIQ: CGSHiGG_01955
            HSO: HS_0784(dld)
            MSU: MS2079(ldhA)
            APL: APL_0687(dld)
            ASU: Asuc_0005
            XFA: XF0347
            XFT: PD1708
            XCC: XCC0708(dld)
            XCB: XC_3526
            XCV: XCV0814
            XAC: XAC0762(dld)
            XOO: XOO3841(dld)
            XOM: XOO_3619(XOO3619)
            VCH: VCA0192
            VCO: VC0395_1085(ldhA)
            VVU: VV1_2200
            VVY: VV2174
            VPA: VPA0144 VPA1005
            VFI: VF1055
            PPR: PBPRA1210 PBPRA2224
            PAE: PA0927(ldhA)
            PAU: PA14_52270(ldhA)
            PPU: PP_1649(ldhA)
            PFL: PFL_4452(ldhA)
            PFO: Pfl_4223
            PEN: PSEEN1358(ldhA)
            PMY: Pmen_3636
            PRW: PsycPRwf_1080
            ACI: ACIAD0109(dld)
            SON: SO_0968(ldhA)
            SDN: Sden_3047
            SFR: Sfri_0518
            SHE: Shewmr4_0807
            SHM: Shewmr7_3216
            SHN: Shewana3_3319
            PAT: Patl_2088
            SDE: Sde_2866
            MAQ: Maqu_3853
            MCA: MCA0182
            TCX: Tcr_1607
            NOC: Noc_0352
            MMW: Mmwyl1_2752
            AHA: AHA_4145
            NME: NMB0997 NMB1685
            NMA: NMA1205(dld) NMA1944(ldhA)
            NMC: NMC0984(dld) NMC1603(ldhA)
            NGO: NGO0890 NGO1336
            RSO: RSc3131(ldhA)
            REU: Reut_B4140
            REH: H16_A1681(ldhA1) H16_A1682(ldhA2)
            BMA: BMA2050(ldhA)
            BMV: BMASAVP1_A0863(ldhA)
            BML: BMA10299_A2695(ldhA)
            BMN: BMA10247_1915(ldhA)
            BXE: Bxe_A3894 Bxe_B2160
            BVI: Bcep1808_6274
            BUR: Bcep18194_A3918
            BCH: Bcen2424_0825
            BAM: Bamb_0705
            BPS: BPSL2734(ldhA)
            BPM: BURPS1710b_3221
            BTE: BTH_I1402
            BPE: BP0651(dld)
            BBR: BB4787(dld)
            NEU: NE0899(ldhA) NE1009
            NET: Neut_1304 Neut_2388
            NMU: Nmul_A0193
            TBD: Tbd_1998
            MFA: Mfla_0399
            MXA: MXAN_7165(ldhA)
            MES: Meso_3888
            ATU: Atu3870(ldhA)
            ATC: AGR_L_1952
            BME: BMEII0185
            BMF: BAB2_1073
            RPB: RPB_2257
            RPC: RPC_4634
            RSP: RSP_0407
            RSH: Rsph17029_2061
            RSQ: Rsph17025_2329
            RDE: RD1_0074(dld)
            PDE: Pden_2928
            HNE: HNE_1654(dld)
            ZMO: ZMO0157(lhdA) ZMO0256 ZMO1237(ldhA)
            GOX: GOX1253 GOX2071
            MGM: Mmc1_3296
            SAU: SA2312(ddh) SA2346
            SAV: SAV2524(ddh) SAV2559
            SAM: MW2444(ddh) MW2480
            SAR: SAR2605(ddh) SAR2640
            SAS: SAS2410 SAS2445
            SAC: SACOL2535 SACOL2574
            SAB: SAB2398(ddh) SAB2432c
            SAA: SAUSA300_2463(ddh) SAUSA300_2496
            SAO: SAOUHSC_02830 SAOUHSC_02875
            SEP: SE2074 SE2121
            SER: SERP2087 SERP2133
            SHA: SH0493 SH0545(ddh)
            SSP: SSP0295
            LLC: LACR_C33
            SPY: SPy_1170(ddh)
            SPZ: M5005_Spy_0890(ddh)
            SPH: MGAS10270_Spy1004(ddh)
            SPI: MGAS10750_Spy1039(ddh)
            SPJ: MGAS2096_Spy0963(ddh)
            SPK: MGAS9429_Spy1007(ddh)
            SPB: M28_Spy0863(ddh)
            SAG: SAG0695(ldhA)
            SAN: gbs0668
            SAK: SAK_0821(ldhA)
            LPL: lp_2057(ldhD)
            LJO: LJ0045
            LAC: LBA0055(ldhD)
            LSL: LSL_0308(ldhA) LSL_1887(ldhD)
            LDB: Ldb0101(ldhA) Ldb1010 Ldb2021
            LBU: LBUL_0084 LBUL_0917 LBUL_1868
            LBR: LVIS_0201 LVIS_1352
            LCA: LSEI_0145 LSEI_2156
            LGA: LGAS_0043
            PPE: PEPE_0876
            EFA: EF2295
            OOE: OEOE_0413 OEOE_1182
            LME: LEUM_1756
            CAC: CAC1543 CAC2691
            CPE: CPE0530(ldhD)
            CPF: CPF_0510
            CPR: CPR_0499(idhA)
            CTC: CTC01840
            CDF: CD0394(ldhA)
            CBO: CBO3283(ldhA1) CBO3284(fldH)
            CBA: CLB_3339(ldhA-1) CLB_3340(ldhA-2)
            CBH: CLC_3225(ldhA-1) CLC_3226(ldhA-2)
            CBF: CLI_3453(ldhA-1) CLI_3454(ldhA-2)
            MPE: MYPE2650
            MMY: MSC_0034(ldh)
            CGL: NCgl0865(cgl0901)
            CGB: cg1027(dld)
            SCO: SCO2118(dldh2) SCO3594(dldH)
            STP: Strop_2972
            FNU: FN0511
            RBA: RB8859(ldhA)
            TPA: TP0037
            SYN: slr1556(ddh)
            SYC: syc0206_d(ldhA)
            SYF: Synpcc7942_1347
            TEL: tlr0711
            ANA: alr0058
            AVA: Ava_2660
            PMA: Pro1755(dld)
            BTH: BT_1575
            BFR: BF1459
            BFS: BF1389(ldhA)
            CHU: CHU_2980(ldhA)
            FJO: Fjoh_1917
            AAE: aq_1769(dld1) aq_727(ldhA)
            NPH: NP1452A(dld_2) NP3764A(dld_1)
            PAI: PAE2035
STRUCTURES  PDB: 1F0X  1J49  1J4A  2DLD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.28
            ExPASy - ENZYME nomenclature database: 1.1.1.28
            ExplorEnz - The Enzyme Database: 1.1.1.28
            ERGO genome analysis and discovery system: 1.1.1.28
            BRENDA, the Enzyme Database: 1.1.1.28
            CAS: 9028-36-8
///
ENTRY       EC 1.1.1.29                 Enzyme
NAME        glycerate dehydrogenase;
            D-glycerate dehydrogenase;
            hydroxypyruvate reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-glycerate:NAD+ oxidoreductase
REACTION    (R)-glycerate + NAD+ = hydroxypyruvate + NADH + H+ [RN:R01388]
ALL_REAC    R01388;
            (other) R00717
SUBSTRATE   (R)-glycerate [CPD:C00258];
            NAD+ [CPD:C00003]
PRODUCT     hydroxypyruvate [CPD:C00168];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13522707]
  AUTHORS   HOLZER H, HOLLDORF A.
  TITLE     [Isolation of D-glycerate dehydrogenase, some properties of the
            enzyme and its application to the enzymic-optic determination of
            hydroxypyruvate in presence of pyruvate.]
  JOURNAL   Biochem. Z. 329 (1957) 292-312.
REFERENCE   2  [PMID:13163046]
  AUTHORS   STAFFORD HA, MAGALDI A, VENNESLAND B.
  TITLE     The enzymatic reduction of hydroxypyruvic acid to D-glyceric acid in
            higher plants.
  JOURNAL   J. Biol. Chem. 207 (1954) 621-9.
  ORGANISM  Pisum sativum
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K00018  glycerate dehydrogenase
GENES       AFM: AFUA_1G13630 AFUA_6G10090
            ECI: UTI89_C3974
            ECV: APECO1_2994
            ECA: ECA2721(hprA)
            HIT: NTHI1577
            HIP: CGSHiEE_05360
            HIQ: CGSHiGG_00180
            PAE: PA4626(hprA)
            PAU: PA14_61210(hprA)
            PPU: PP_0762(hprA)
            PFL: PFL_5121
            PFO: Pfl_4711
            PEN: PSEEN0907
            PCR: Pcryo_2289
            ACI: ACIAD1301 ACIAD3278(hprA)
            SON: SO_3631(hprA)
            SDN: Sden_2881
            SHN: Shewana3_3201
            ILO: IL1569
            MAQ: Maqu_3054
            AEH: Mlg_1400
            HHA: Hhal_0010
            HCH: HCH_01519
            CSA: Csal_1842
            ABO: ABO_2391(hprA)
            AHA: AHA_3230
            NME: NMB0029
            NMA: NMA0274
            NMC: NMC0006
            CVI: CV_3789
            REH: H16_B0611(hprA)
            BXE: Bxe_B0983
            BUR: Bcep18194_A4851
            NEU: NE0101(hprA)
            NET: Neut_2243
            AZO: azo0826
            CFF: CFF8240_1663(hprA)
            CCV: CCV52592_1540
            CHA: CHAB381_0045
            GSU: GSU1672(hprA)
            GME: Gmet_2695
            PCA: Pcar_2462
            DVU: DVU1412
            DDE: Dde_1681
            LIP: LI1043(hprA)
            SAT: SYN_00869
            BJA: bll2918
            GBE: GbCGDNIH1_0049 GbCGDNIH1_0364
            LSL: LSL_1099(serA)
            CAC: CAC2945
            DSY: DSY0996
            RBA: RB6394
            TDE: TDE1616(hprA)
            BTH: BT_1207
            BFR: BF1882
            BFS: BF1944
            PGI: PG1190(hprA)
            TTH: TTC0124
            TTJ: TTHA0500
            MMP: MMP0870
            RCI: RCIX739(hprA)
STRUCTURES  PDB: 1GDH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.29
            ExPASy - ENZYME nomenclature database: 1.1.1.29
            ExplorEnz - The Enzyme Database: 1.1.1.29
            ERGO genome analysis and discovery system: 1.1.1.29
            BRENDA, the Enzyme Database: 1.1.1.29
            CAS: 9028-37-9
///
ENTRY       EC 1.1.1.30                 Enzyme
NAME        3-hydroxybutyrate dehydrogenase;
            NAD+-beta-hydroxybutyrate dehydrogenase;
            hydroxybutyrate oxidoreductase;
            beta-hydroxybutyrate dehydrogenase;
            D-beta-hydroxybutyrate dehydrogenase;
            D-3-hydroxybutyrate dehydrogenase;
            D-(-)-3-hydroxybutyrate dehydrogenase;
            beta-hydroxybutyric acid dehydrogenase;
            3-D-hydroxybutyrate dehydrogenase;
            beta-hydroxybutyric dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-3-hydroxybutanoate:NAD+ oxidoreductase
REACTION    (R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+ [RN:R01361]
ALL_REAC    R01361
SUBSTRATE   (R)-3-hydroxybutanoate [CPD:C01089];
            NAD+ [CPD:C00003]
PRODUCT     acetoacetate [CPD:C00164];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also oxidizes other 3-hydroxymonocarboxylic acids.
REFERENCE   1  [PMID:4291491]
  AUTHORS   Bergmeyer HU, Gawehn K, Klotzsch H, Krebs HA, Williamson DH.
  TITLE     Purification and properties of crystalline 3-hydroxybutyrate
            dehydrogenase from Rhodopseudomonas spheroides.
  JOURNAL   Biochem. J. 102 (1967) 423-31.
  ORGANISM  Rhodopseudomonas spheroides
REFERENCE   2  [PMID:4954074]
  AUTHORS   Delafield FP, Cooksey KE, Doudoroff M.
  TITLE     beta-Hydroxybutyric dehydrogenase and dimer hydrolase of Pseudomonas
            lemoignei.
  JOURNAL   J. Biol. Chem. 240 (1965) 4023-8.
  ORGANISM  Pseudomonas lemoignei
REFERENCE   3
  AUTHORS   Lehninger, A.L., Sudduth, H.C. and Wise, J.B.
  TITLE     D-beta-Hydroxybutyric dehydrogenase of mitochondria.
  JOURNAL   J. Biol. Chem. 235 (1960) 2450-2455.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00072  Synthesis and degradation of ketone bodies
            PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K00019  3-hydroxybutyrate dehydrogenase
GENES       HSA: 56898(BDH2) 622(BDH1)
            MMU: 71911(Bdh1)
            RNO: 117099(Bdh1)
            CFA: 488037(BDH1)
            GGA: 424891(BDH1)
            DME: Dmel_CG13377
            AFM: AFUA_5G09290
            DDI: DDBDRAFT_0184469
            TET: TTHERM_00039050 TTHERM_01005260
            TBR: Tb10.389.1850
            TCR: 506567.70 507049.60
            ECW: EcE24377A_1665(bdhA)
            XCC: XCC2162(hbdH1)
            XCB: XC_1956
            XCV: XCV2206(bdhA)
            XAC: XAC2045(hbdH1)
            XOO: XOO2218(hbdH1)
            XOM: XOO_2083(XOO2083)
            PAE: PA2003(bdhA)
            PAU: PA14_38590(bdhA)
            PPU: PP_3073(bdhA)
            PFL: PFL_3576
            PFO: Pfl_3079
            PEN: PSEEN3158(bdhA)
            PAR: Psyc_1428
            PCR: Pcryo_1592
            ACI: ACIAD2509(bdhA)
            SHN: Shewana3_3466
            CPS: CPS_0943(bdhA1) CPS_4091(bdhA2)
            PHA: PSHAa2944(bdhA)
            PAT: Patl_1976
            LPN: lpg2316(bdhA)
            LPF: lpl2236
            LPP: lpp2264
            FTL: FTL_1281
            ABO: ABO_1479
            CVI: CV_0695(bdhA)
            RSO: RSc1572(RS05259)
            REU: Reut_A1271 Reut_B3729
            REH: H16_A1334 H16_A1814
            RME: Rmet_0546 Rmet_1156
            BMA: BMAA0017(bdhA-1) BMAA0876(bdhA-2)
            BMV: BMASAVP1_1167(bdhA-1)
            BML: BMA10299_0018(bdhA-2) BMA10299_1447(bdhA-1)
            BMN: BMA10247_A0021(bdhA-1) BMA10247_A0918(bdhA-2)
            BXE: Bxe_B0969
            BPS: BPSS0017 BPSS0354
            BPM: BURPS1710b_A1524(bdhA-1) BURPS1710b_A1918(bdhA-2)
            BPL: BURPS1106A_A0021(bdhA) BURPS1106A_A0505(bdhA)
            BPD: BURPS668_A0023(bdhA) BURPS668_A0602(bdhA)
            BTE: BTH_II0019 BTH_II2038
            BPE: BP0229 BP2454
            BPA: BPP3441 BPP3638
            BBR: BB3891 BB4073
            RFR: Rfer_2069 Rfer_3285
            POL: Bpro_2705
            PNA: Pnap_2539
            AAV: Aave_1586
            AJS: Ajs_3151
            VEI: Veis_4364
            MPT: Mpe_A1576
            HAR: HEAR1805(bdhA)
            MMS: mma_1483(bdh)
            EBA: ebA5833
            ADE: Adeh_2140
            RFE: RF_1389 RF_1390
            RBE: RBE_1385
            MLO: mll3632 mlr2400
            MES: Meso_3335
            SME: SMb21010(bdhA)
            ATU: Atu2308(bdhA) Atu4131
            ATC: AGR_C_4198 AGR_L_1444
            RET: RHE_CH03123(bdhA)
            RLE: RL3569(bdhA) pRL90175(bdhA)
            BME: BMEI0268 BMEII1090
            BMF: BAB1_1789 BAB2_0146
            BMS: BR1779
            BMB: BruAb1_1762
            BJA: blr1488(bdhA) blr7029(bdhA)
            BRA: BRADO1076
            BBT: BBta_6971
            RPA: RPA4206
            RPB: RPB_1408
            RPC: RPC_1997 RPC_2000 RPC_4002
            RPD: RPD_1388
            RPE: RPE_1773
            NWI: Nwi_2755
            NHA: Nham_3554
            CCR: CC_3384
            SIL: SPO1015 SPO2065(bdh-1)
            SIT: TM1040_1342 TM1040_3270
            RSP: RSP_2857
            JAN: Jann_2311
            RDE: RD1_2738(bdhA)
            MMR: Mmar10_0826
            HNE: HNE_0125(bdhA)
            SAL: Sala_0938
            ELI: ELI_07105
            RRU: Rru_A1057
            MAG: amb2677
            BSU: BG11155(bdh)
            BAN: BA4249
            BAR: GBAA4249
            BAA: BA_4708
            BAT: BAS3941
            BCE: BC4030
            BCA: BCE_4084
            BCZ: BCZK3788
            BTK: BT9727_3773
            BCL: ABC3434(bdh)
            OIH: OB2631
            GKA: GK1983
            SSP: SSP2198
            SPY: SPy_1640
            SPZ: M5005_Spy_1347
            SPM: spyM18_1649
            SPG: SpyM3_1381 SpyM3_1382
            SPS: SPs0480 SPs0481
            SPH: MGAS10270_Spy1464
            SPI: MGAS10750_Spy1456
            SPJ: MGAS2096_Spy1368
            SPK: MGAS9429_Spy1342
            SPF: SpyM50444
            SPA: M6_Spy1393
            SPB: M28_Spy1388
            CDF: CD2679(bdhA)
            MSM: MSMEG_6026
            CEF: CE2393
            NFA: nfa28660
            RHA: RHA1_ro04778
            SCO: SCO1012(2SCG2.25c)
            SMA: SAV1420(bdhA)
            AAU: AAur_0392(bdh)
            TFU: Tfu_0081
            SEN: SACE_3718 SACE_6685
            RXY: Rxyl_2343
            DGE: Dgeo_0952
            TTH: TTC0333
            TTJ: TTHA0693
            HMA: rrnAC0648(bdhA)
STRUCTURES  PDB: 1WMB  1X1T  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.30
            ExPASy - ENZYME nomenclature database: 1.1.1.30
            ExplorEnz - The Enzyme Database: 1.1.1.30
            ERGO genome analysis and discovery system: 1.1.1.30
            BRENDA, the Enzyme Database: 1.1.1.30
            CAS: 9028-38-0
///
ENTRY       EC 1.1.1.31                 Enzyme
NAME        3-hydroxyisobutyrate dehydrogenase;
            beta-hydroxyisobutyrate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-hydroxy-2-methylpropanoate:NAD+ oxidoreductase
REACTION    3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate +
            NADH + H+ [RN:R02047]
ALL_REAC    R02047 > R05066
SUBSTRATE   3-hydroxy-2-methylpropanoate [CPD:C01188];
            NAD+ [CPD:C00003]
PRODUCT     2-methyl-3-oxopropanoate [CPD:C00349];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Robinson, W.G. and Coon, M.J.
  TITLE     Purification and properties of beta-hydroxyisobutyric dehydrogenase.
  JOURNAL   J. Biol. Chem. 225 (1957) 511-521.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
ORTHOLOGY   KO: K00020  3-hydroxyisobutyrate dehydrogenase
GENES       HSA: 11112(HIBADH)
            PTR: 463313(HIBADH)
            MMU: 58875(Hibadh)
            RNO: 63938(Hibadh)
            CFA: 479610(HIBADH)
            GGA: 420632(HIBADH)
            XLA: 431794(MGC84587) 495134(LOC495134)
            DME: Dmel_CG4747
            CEL: B0250.5
            ATH: AT4G20930 AT4G29120
            OSA: 4326545 4341837
            PIC: PICST_35865(HIB1)
            ANI: AN0593.2 AN2335.2
            AFM: AFUA_3G09470 AFUA_5G01250 AFUA_5G10280 AFUA_6G11020
            AOR: AO090010000515 AO090023000518
            UMA: UM02189.1
            DDI: DDB_0216217(hibA)
            TET: TTHERM_01123840
            TBR: Tb927.6.1570
            TCR: 505807.180 507017.40
            ECI: UTI89_C5030(ghbD)
            ECV: APECO1_2097(ghbD)
            YPA: YPA_3661
            YPP: YPDSF_0255
            PMU: PM1366
            MSU: MS1981(mmsB)
            APL: APL_1197
            XCC: XCC1264(mmsB)
            XCB: XC_2977
            XCV: XCV1367
            XAC: XAC1316(mmsB)
            XOO: XOO1846(mmsB)
            XOM: XOO_1742(XOO1742)
            VCH: VCA0007
            VVU: VV2_0489 VV2_1637
            VVY: VVA0448 VVA1038
            VPA: VPA0625 VPA1118 VPA1419
            VFI: VFA0173
            PPR: PBPRB1107
            PAE: PA0743 PA1576 PA3312 PA3569(mmsB)
            PAU: PA14_18140(mmsB) PA14_21180 PA14_54670
            PAP: PSPA7_1575(mmsB2) PSPA7_4777(mmsB1)
            PPU: PP_1143 PP_4666(mmsB)
            PPF: Pput_1177 Pput_4530
            PST: PSPTO_0783(mmsB) PSPTO_1880 PSPTO_5060
            PSB: Psyr_0466 Psyr_0690 Psyr_3525
            PSP: PSPPH_0457 PSPPH_3467
            PFL: PFL_0748(mmsB) PFL_1303 PFL_2928 PFL_3346
            PFO: Pfl_0696 Pfl_1251
            PEN: PSEEN0700(mmsB) PSEEN1291
            PMY: Pmen_1371 Pmen_3196
            PAR: Psyc_0904(mmsB)
            PCR: Pcryo_1513
            PRW: PsycPRwf_0297
            ACI: ACIAD0032 ACIAD1605(mmsB) ACIAD2316 ACIAD3074
            SON: SO_1682(mmsB) SO_2771(garR)
            SDN: Sden_1938
            SFR: Sfri_1343
            SAZ: Sama_1380
            SBL: Sbal_1500
            SBM: Shew185_1494
            SLO: Shew_1672
            SPC: Sputcn32_1402
            SSE: Ssed_1478
            SPL: Spea_2778
            SHE: Shewmr4_2592
            SHM: Shewmr7_2659
            SHN: Shewana3_2554 Shewana3_2766
            SHW: Sputw3181_2699
            ILO: IL0867(mmsB) IL1375
            CPS: CPS_2007 CPS_3424(mmsB)
            PHA: PSHAa1459 PSHAa1750
            PAT: Patl_0951 Patl_2175
            MAQ: Maqu_2129
            CBU: CBU_0926(mmsB)
            CBD: COXBU7E912_1148(mmsB)
            LPN: lpg0128
            LPF: lpl0127
            LPP: lpp0142
            FTU: FTT1666c
            FTF: FTF1666c
            FTL: FTL_0026 FTL_0027
            NOC: Noc_2077
            HCH: HCH_00638(mmsB) HCH_04751
            CSA: Csal_1707 Csal_3178
            ABO: ABO_0022(mmsB) ABO_1503(mmsB)
            MMW: Mmwyl1_0115 Mmwyl1_2547
            AHA: AHA_2083(mmsB)
            NME: NMB1584
            NMA: NMA1773
            NGO: NGO1243
            CVI: CV_2081(mmsB) CV_3944
            RSO: RSp0649(mmsB)
            REU: Reut_A1427 Reut_B3944 Reut_B4259 Reut_B5532 Reut_C5900
                 Reut_C5958
            REH: H16_A1239 H16_A3004 H16_B1190 H16_B1657 H16_B1750 H16_B2317
            RME: Rmet_1835 Rmet_4459
            BMA: BMAA2000
            BXE: Bxe_A1115 Bxe_A3575 Bxe_B0073 Bxe_B0704 Bxe_B1087 Bxe_B2130
                 Bxe_B2172 Bxe_C0245
            BVI: Bcep1808_3334 Bcep1808_4620
            BUR: Bcep18194_A3406 Bcep18194_A5291 Bcep18194_B0478
                 Bcep18194_B0717 Bcep18194_B1214 Bcep18194_B2034
                 Bcep18194_B2531 Bcep18194_C7141
            BCN: Bcen_3212 Bcen_3407 Bcen_4320 Bcen_6098
            BCH: Bcen2424_4046 Bcen2424_4656 Bcen2424_4960 Bcen2424_5155
            BAM: Bamb_0226 Bamb_3441 Bamb_4382 Bamb_4550
            BPS: BPSS0620(mmsB) BPSS2264
            BPM: BURPS1710b_0030 BURPS1710b_A0438 BURPS1710b_A1397
                 BURPS1710b_A2181(mmsB)
            BPL: BURPS1106A_A0829(mmsB)
            BPD: BURPS668_A0921(mmsB)
            BTE: BTH_II1800(mmsB) BTH_II2294
            PNU: Pnuc_1557 Pnuc_1634
            BPE: BP1447(mmsB) BP3053
            BPA: BPP0881 BPP1554(mmsB) BPP3779
            BBR: BB0653 BB0974 BB1031 BB2632(mmsB) BB4224
            RFR: Rfer_0446 Rfer_3876
            POL: Bpro_2471 Bpro_4883
            AAV: Aave_0633 Aave_2600
            AJS: Ajs_0417 Ajs_2005
            VEI: Veis_2971 Veis_3539
            MPT: Mpe_A3763
            MMS: mma_0819
            AZO: azo2540(mmsB)
            HPJ: jhp0585
            HPA: HPAG1_0625
            GSU: GSU1372 GSU1451
            GME: Gmet_1972
            SFU: Sfum_2944
            PUB: SAR11_0863 SAR11_1196(mmsB)
            MLO: mlr0552 mlr1203 mlr2606
            MES: Meso_1308
            PLA: Plav_2900
            SME: SMb20668 SMb20751 SMc00133
            SMD: Smed_4243 Smed_4270 Smed_4321
            ATU: Atu4129(mmsB)
            ATC: AGR_L_1448
            RET: RHE_CH02433(ypch00812) RHE_PE00281(ype00138)
                 RHE_PF00345(ypf00176)
            RLE: RL0271 RL2772 RL2854 pRL110152 pRL110406 pRL120616
            BME: BMEI0688 BMEI1024
            BMF: BAB1_1334
            BMS: BR0950 BR1314(mmsB)
            BMB: BruAb1_1315(mmsB)
            BOV: BOV_1276(mmsB)
            BJA: bll3740 bll6323 blr3957
            BRA: BRADO3016 BRADO3140 BRADO4737 BRADO5847 BRADO6607
            BBT: BBta_0929 BBta_1985 BBta_3463 BBta_3581 BBta_5125
            RPA: RPA1973 RPA3446
            RPB: RPB_2122 RPB_3005 RPB_3394
            RPC: RPC_2065 RPC_3091
            RPD: RPD_1854 RPD_2047 RPD_3299
            RPE: RPE_1979 RPE_2387
            NWI: Nwi_1213 Nwi_2156
            NHA: Nham_1470 Nham_2556
            XAU: Xaut_1027 Xaut_1538 Xaut_2189 Xaut_3451
            CCR: CC_1354 CC_1574
            SIL: SPO0792 SPO2213(mmsB-1) SPO2859 SPO3097(mmsB-2)
            SIT: TM1040_1101 TM1040_1353
            RSP: RSP_0154 RSP_2846 RSP_3171
            RSH: Rsph17029_1787
            RSQ: Rsph17025_1337
            JAN: Jann_1907 Jann_3485
            RDE: RD1_2540(garR) RD1_2751 RD1_2991(mmsB) RD1_3786(mmsB)
            PDE: Pden_3216 Pden_3256 Pden_4003
            MMR: Mmar10_1542 Mmar10_1552
            HNE: HNE_0895 HNE_1826(mmsB)
            NAR: Saro_0861 Saro_1098
            SAL: Sala_3056
            SWI: Swit_0647
            ELI: ELI_10045
            ACR: Acry_0625 Acry_2431 Acry_2697
            RRU: Rru_A1833
            MAG: amb3587
            MGM: Mmc1_3551
            SUS: Acid_7137
            BSU: BG12914(yfjR) BG13328(ykwC)
            BHA: BH2634
            BAN: BA2353(garR)
            BAR: GBAA2353(garR)
            BAA: BA_4720 BA_4721
            BAT: BAS2192 BAS3952 BAS3953
            BCE: BC2289 BC4042
            BCZ: BCZK2115(garR) BCZK3799
            BCY: Bcer98_1728
            BTK: BT9727_2129(garR) BT9727_3784
            BLI: BL00292(ykwC) BL03574
            BLD: BLi01606(ykwC)
            BCL: ABC1808 ABC2403 ABC3811
            BPU: BPUM_1286(ykwC) BPUM_3412
            OIH: OB0581 OB0815
            GKA: GK1027
            LMO: lmo1005
            LMF: LMOf2365_1026
            LIN: lin1004
            LWE: lwe0989
            LLA: L81616(ywjF)
            LLM: llmg_2494(ywjF)
            LPL: lp_2548(hibD)
            LSA: LSA0463
            LSL: LSL_0010(mmsB)
            LBR: LVIS_1796
            LCA: LSEI_0245
            EFA: EF2889(glxR)
            STH: STH938
            CAC: CAC3342
            CPE: CPE0393
            DSY: DSY4048
            MPE: MYPE3160
            MTU: Rv0751c(mmsB)
            MTC: MT0775(mmsB) MT0794
            MBO: Mb0773c(mmsB) Mb0793
            MBB: BCG_0802c(mmsB)
            MPA: MAP0604 MAP4213c(mmsB)
            MAV: MAV_4419(mmsB)
            MSM: MSMEG_1496(mmsB)
            MVA: Mvan_4822
            MMC: Mmcs_1062
            NFA: nfa10400 nfa46610
            RHA: RHA1_ro01539(mmsB1) RHA1_ro05332(mmsB2) RHA1_ro07079(mmsB3)
                 RHA1_ro08845
            SCO: SCO0907(SCM1.40c)
            SMA: SAV1542
            ART: Arth_0422 Arth_1322
            AAU: AAur_0501(mmsB) AAur_0651(mmsB)
            NCA: Noca_2159
            FRA: Francci3_0803
            FAL: FRAAL2958 FRAAL6073(mmsB)
            SEN: SACE_1371 SACE_1459(mmsB) SACE_3558
            RXY: Rxyl_0425
            RBA: RB13140(mmsB) RB3816
            TDE: TDE1000
            LIL: LA2054
            LIC: LIC11860(mmsB)
            SYN: slr0229(mmsB)
            SYW: SYNW2430
            SYC: syc2237_d(mmsB)
            SYF: Synpcc7942_1857
            SYD: Syncc9605_2461 Syncc9605_2601
            SYE: Syncc9902_2237
            SYG: sync_2712
            GVI: glr3759
            ANA: alr3358
            PMA: Pro1229(mmsB)
            PMT: PMT2105
            PMF: P9303_27951(mmsB)
            PME: NATL1_08981(mmsB)
            RCA: Rcas_2700
            DRA: DR_0499
            TTH: TTC1749
            TTJ: TTHA0237
            AAE: aq_038(hibD)
            MAC: MA0614
            TAC: Ta0161
            TVO: TVN0231
            PFU: PF0716
            RCI: RRC500(hibD)
            APE: APE_0756.1
            SSO: SSO0974 SSO1560
            STO: ST0619
            SAI: Saci_0385
            PAI: PAE1145
STRUCTURES  PDB: 1WP4  2CVZ  2GF2  2H78  2I9P  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.31
            ExPASy - ENZYME nomenclature database: 1.1.1.31
            ExplorEnz - The Enzyme Database: 1.1.1.31
            ERGO genome analysis and discovery system: 1.1.1.31
            BRENDA, the Enzyme Database: 1.1.1.31
            CAS: 9028-39-1
///
ENTRY       EC 1.1.1.32                 Enzyme
NAME        mevaldate reductase;
            mevalonic dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-mevalonate:NAD+ oxidoreductase
REACTION    (R)-mevalonate + NAD+ = mevaldate + NADH + H+ [RN:R02246]
ALL_REAC    R02246
SUBSTRATE   (R)-mevalonate [CPD:C00418];
            NAD+ [CPD:C00003]
PRODUCT     mevaldate [CPD:C00772];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Schlesinger, M.J. and Coon, M.J.
  TITLE     Reduction of mevaldic acid to mevalonic acid by a partial purified
            enzyme from liver.
  JOURNAL   J. Biol. Chem. 236 (1961) 2421-2424.
  ORGANISM  pig [GN:ssc]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.32
            ExPASy - ENZYME nomenclature database: 1.1.1.32
            ExplorEnz - The Enzyme Database: 1.1.1.32
            ERGO genome analysis and discovery system: 1.1.1.32
            BRENDA, the Enzyme Database: 1.1.1.32
            CAS: 9028-33-5
///
ENTRY       EC 1.1.1.33                 Enzyme
NAME        mevaldate reductase (NADPH);
            mevaldate (reduced nicotinamide adenine dinucleotide phosphate)
            reductase;
            mevaldate reductase (NADPH)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-mevalonate:NADP+ oxidoreductase
REACTION    (R)-mevalonate + NADP+ = mevaldate + NADPH + H+ [RN:R02247]
ALL_REAC    R02247
SUBSTRATE   (R)-mevalonate [CPD:C00418];
            NADP+ [CPD:C00006]
PRODUCT     mevaldate [CPD:C00772];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     May be identical with EC 1.1.1.2 [alcohol dehydrogenase (NADP+)].
REFERENCE   1
  AUTHORS   Coon, M.J., Kupiecki, F.P., Dekker, E.E., Schlesinger, M.J. and del
            Campillo, A.
  TITLE     The enzymic synthesis of branched-chain acids.
  JOURNAL   In: Wolstenholme, G.E.W. and O'Connor, M. (Eds.), CIBA Symposium on
            the Biosynthesis of Terpenes and Sterols, CIBA Symposium on the
            Biosynthesis of Terpenes and Sterols, London, 1959, p. 62-74.
REFERENCE   2
  AUTHORS   von Wartburg, J.P. and Wermoth, B.
  TITLE     Aldehyde reductase.
  JOURNAL   In: Jakoby, W.B. (Ed.), Enzymatic Basis of Detoxication, vol. 1,
            Academic Press, New York, 1980, p. 249-260.
  ORGANISM  human [GN:hsa], pig [GN:ssc], rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.33
            ExPASy - ENZYME nomenclature database: 1.1.1.33
            ExplorEnz - The Enzyme Database: 1.1.1.33
            ERGO genome analysis and discovery system: 1.1.1.33
            BRENDA, the Enzyme Database: 1.1.1.33
            CAS: 9028-34-6
///
ENTRY       EC 1.1.1.34                 Enzyme
NAME        hydroxymethylglutaryl-CoA reductase (NADPH);
            hydroxymethylglutaryl coenzyme A reductase (reduced nicotinamide
            adenine dinucleotide phosphate);
            3-hydroxy-3-methylglutaryl-CoA reductase;
            beta-hydroxy-beta-methylglutaryl coenzyme A reductase;
            hydroxymethylglutaryl CoA reductase (NADPH);
            S-3-hydroxy-3-methylglutaryl-CoA reductase;
            NADPH-hydroxymethylglutaryl-CoA reductase;
            HMGCoA reductase-mevalonate:NADP-oxidoreductase (acetylating-CoA);
            3-hydroxy-3-methylglutaryl CoA reductase (NADPH);
            hydroxymethylglutaryl-CoA reductase (NADPH2)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-mevalonate:NADP+ oxidoreductase (CoA-acylating)
REACTION    (R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA
            + 2 NADPH + 2 H+ [RN:R02082]
ALL_REAC    R02082
SUBSTRATE   (R)-mevalonate [CPD:C00418];
            CoA [CPD:C00010];
            NADP+ [CPD:C00006]
PRODUCT     (S)-3-hydroxy-3-methylglutaryl-CoA [CPD:C00356];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
INHIBITOR   Pravastatin [CPD:C01844]
COMMENT     The enzyme is inactivated by EC 2.7.11.31
            {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} and
            reactivated by EC 3.1.3.47 {[hydroxymethylglutaryl-CoA reductase
            (NADPH)]-phosphatase}.
REFERENCE   1
  AUTHORS   Bucher, N.L.R., Overath, P. and Lynen, F.
  TITLE     beta-Hydroxy-beta-methylglutaryl coenzyme A reductase, cleavage and
            condensing enzymes in relation to cholesterol formation in rat
            liver.
  JOURNAL   Biochim. Biophys. Acta 40 (1960) 491-501.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:13818862]
  AUTHORS   DURR IF, RUDNEY H.
  TITLE     The reduction of beta-hydroxy-beta-methyl-glutaryl coenzyme A to
            mevalonic acid.
  JOURNAL   J. Biol. Chem. 235 (1960) 2572-8.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:4985697]
  AUTHORS   Kawachi T, Rudney H.
  TITLE     Solubilization and purification of beta-hydroxy-beta-methylglutaryl
            coenzyme A reductase from rat liver.
  JOURNAL   Biochemistry. 9 (1970) 1700-5.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K00021  3-hydroxy-3-methylglutaryl-CoA reductase
GENES       HSA: 3156(HMGCR)
            PTR: 471516(HMGCR)
            MMU: 15357(Hmgcr)
            RNO: 25675(Hmgcr)
            CFA: 479182(HMGCR)
            BTA: 407159(hmg-coa-r)
            GGA: 395145(RCJMB04_14m24)
            SPU: 373355(LOC373355)
            DME: Dmel_CG10367(Hmgcr)
            CEL: F08F8.2
            OSA: 4347443
            SCE: YLR450W(HMG2) YML075C(HMG1)
            AGO: AGOS_AER152W
            CGR: CAGL0L11506g
            SPO: SPCC162.09c(hmg1)
            ANI: AN3817.2
            AFM: AFUA_1G11230 AFUA_2G03700
            AOR: AO090103000311 AO090120000217
            CNE: CNF04830
            UMA: UM03014.1
            ECU: ECU10_1720
            DDI: DDB_0191125(hmgA) DDB_0215357(hmgB)
            TBR: Tb927.6.4540
            TCR: 506831.40 509167.20
            LMA: LmjF30.3190
            VCH: VCA0723
            VCO: VC0395_0662
            VVU: VV2_0117
            VVY: VVA0625
            VPA: VPA0968
            VFI: VFA0841
            PAT: Patl_0427
            CBU: CBU_0030 CBU_0610
            CBD: COXBU7E912_0151 COXBU7E912_0622(hmgA)
            TCX: Tcr_1717
            DNO: DNO_0797
            CVI: CV_1806
            SUS: Acid_5728 Acid_6132
            SAU: SA2333(mvaA)
            SAV: SAV2545(mvaA)
            SAM: MW2466(mvaA)
            SAB: SAB2419c(mvaA)
            SEP: SE2109
            LWE: lwe0819(mvaA)
            LLA: L10433(mvaA)
            LLC: LACR_1664
            LLM: llmg_0931(mvaA)
            SPY: SPy_0880(mvaS.1)
            SPM: spyM18_0941(mvaS1)
            SPG: SpyM3_0599(mvaS.1)
            SPS: SPs1254
            SPH: MGAS10270_Spy0744
            SPI: MGAS10750_Spy0778
            SPJ: MGAS2096_Spy0758
            SPK: MGAS9429_Spy0742
            SPA: M6_Spy0703
            SPN: SP_1726
            SAG: SAG1317
            SAN: gbs1387
            STC: str0576(mvaA)
            STL: stu0576(mvaA)
            SSA: SSA_0337(mvaA)
            LPL: lp_0447(mvaA)
            LJO: LJ1608
            LSL: LSL_0224
            LBR: LVIS_0450
            EFA: EF1364
            NFA: nfa22110
            BGA: BG0708(mvaA)
            SRU: SRU_2422
            FPS: FP2341
            MMP: MMP0087(hmgA)
            MMQ: MmarC5_1589
            MAC: MA3073(hmgA)
            MBA: Mbar_A1972
            MMA: MM_0335
            MBU: Mbur_1098
            MHU: Mhun_3004
            MEM: Memar_2365
            MBN: Mboo_0137
            MTH: MTH562
            MST: Msp_0584(hmgA)
            MSI: Msm_0227
            MKA: MK0355(HMG1)
            AFU: AF1736(mvaA)
            HAL: VNG1875G(mvaA)
            HMA: rrnAC3412(mvaA)
            HWA: HQ3215A(hmgR)
            NPH: NP0368A(mvaA_2) NP2422A(mvaA_1)
            TAC: Ta0406m
            TVO: TVN1168
            PTO: PTO1143
            PAB: PAB2106(mvaA)
            PFU: PF1848
            TKO: TK0914
            RCI: RCIX1027(hmgA) RCIX376(hmgA)
            APE: APE_1869
            IHO: Igni_0476
            HBU: Hbut_1531
            SSO: SSO0531
            STO: ST1352
            SAI: Saci_1359
            PAI: PAE2182
            PIS: Pisl_0814
            PCL: Pcal_1085
            PAS: Pars_0796
STRUCTURES  PDB: 1DQ8  1DQ9  1DQA  1HW8  1HW9  1HWI  1HWJ  1HWK  1HWL  2Q1L  
                 2Q6B  2Q6C  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.34
            ExPASy - ENZYME nomenclature database: 1.1.1.34
            ExplorEnz - The Enzyme Database: 1.1.1.34
            ERGO genome analysis and discovery system: 1.1.1.34
            BRENDA, the Enzyme Database: 1.1.1.34
            CAS: 9028-35-7
///
ENTRY       EC 1.1.1.35                 Enzyme
NAME        3-hydroxyacyl-CoA dehydrogenase;
            beta-hydroxyacyl dehydrogenase;
            beta-keto-reductase;
            3-keto reductase;
            3-hydroxyacyl coenzyme A dehydrogenase;
            beta-hydroxyacyl-coenzyme A synthetase;
            beta-hydroxyacylcoenzyme A dehydrogenase;
            beta-hydroxybutyrylcoenzyme A dehydrogenase;
            3-hydroxyacetyl-coenzyme A dehydrogenase;
            L-3-hydroxyacyl coenzyme A dehydrogenase;
            L-3-hydroxyacyl CoA dehydrogenase;
            beta-hydroxyacyl CoA dehydrogenase;
            3beta-hydroxyacyl coenzyme A dehydrogenase;
            3-hydroxybutyryl-CoA dehydrogenase;
            beta-ketoacyl-CoA reductase;
            beta-hydroxy acid dehydrogenase;
            3-L-hydroxyacyl-CoA dehydrogenase;
            3-hydroxyisobutyryl-CoA dehydrogenase;
            1-specific DPN-linked beta-hydroxybutyric dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase
REACTION    (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+ [RN:R01778]
ALL_REAC    R01778 > R01975 R04203 R04737 R04739 R04741 R04743 R04745 R04748
            R06941 R07890 R07894 R07898;
            (other) R05066 R05575
SUBSTRATE   (S)-3-hydroxyacyl-CoA [CPD:C00640];
            NAD+ [CPD:C00003]
PRODUCT     3-oxoacyl-CoA [CPD:C00264];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and
            S-3-hydroxyacyl-hydrolipoate. Some enzymes act, more slowly, with
            NADP+. Broad specificity to acyl chain-length (cf. EC 1.1.1.211
            [long-chain-3-hydroxyacyl-CoA dehydrogenase]).
REFERENCE   1
  AUTHORS   Hillmer, P. and Gottschalk, G.
  TITLE     Solubilization and partial characterisation of particulate
            dehydrogenases from Clostridium kluyveri.
  JOURNAL   Biochim. Biophys. Acta 334 (1974) 12-23.
  ORGANISM  Clostridium kluyveri
REFERENCE   2  [PMID:13115428]
  AUTHORS   LEHNINGER AL, GREVILLE GD.
  TITLE     The enzymic oxidation of alpha- and 2-beta-hydroxybutyrate.
  JOURNAL   Biochim. Biophys. Acta. 12 (1953) 188-202.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Stern, J.R.
  TITLE     Crystalline beta-hydroxybutyrate dehydrogenase from pig heart.
  JOURNAL   Biochim. Biophys. Acta 26 (1957) 448-449.
  ORGANISM  pig [GN:ssc]
REFERENCE   4
  AUTHORS   Wakil, S.J., Green, D.E., Mii, S. and Mahler, H.R.
  TITLE     Studies on the fatty acid oxidizing system of animal tissues. VI.
            beta-Hydroxyacyl coenzyme A dehydrogenase.
  JOURNAL   J. Biol. Chem. 207 (1954) 631-638.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00062  Fatty acid elongation in mitochondria
            PATH: map00071  Fatty acid metabolism
            PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00310  Lysine degradation
            PATH: map00380  Tryptophan metabolism
            PATH: map00592  alpha-Linolenic acid metabolism
            PATH: map00632  Benzoate degradation via CoA ligation
            PATH: map00650  Butanoate metabolism
            PATH: map00930  Caprolactam degradation
ORTHOLOGY   KO: K00022  3-hydroxyacyl-CoA dehydrogenase
            KO: K07516  3-hydroxyacyl-CoA dehydrogenase
            KO: K07547  2-[hydroxy(phenyl)methyl]-succinyl-CoA dehydrogenase
                        BbsC subunit
            KO: K07548  2-[hydroxy(phenyl)methyl]-succinyl-CoA dehydrogenase
                        BbsD subunit
            KO: K10527  enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase
GENES       HSA: 1962(EHHADH) 3028(HSD17B10) 3033(HADH) 3295(HSD17B4)
            PTR: 460996(EHHADH) 462019(HSD17B4) 465649(HSD17B10)
            MMU: 15107(Hadh) 15108(Hsd17b10) 15488(Hsd17b4) 74147(Ehhadh)
            RNO: 113965(Hadhsc) 171142(Ehhadh) 63864(Hadh2) 79244(Hsd17b4)
            CFA: 474630(HSD17B4) 478506(HADH) 480930(HSD17B10) 488110(EHHADH)
            BTA: 281809(HADH2) 493643(HSD17B4)
            SSC: 397574(HSD17B4) 397604(HAD)
            GGA: 395785(HSD17B4) 420290(HADH) 424877(EHHADH)
            XLA: 380594(hadhsc) 444492(MGC81885) 446903(hadh2)
            XTR: 496484(hadhsc) 549265(hadh2)
            DRE: 393105(hsd17b4) 450078(hsd17b10)
            SPU: 579135(LOC579135) 581580(LOC581580)
            DME: Dmel_CG3415 Dmel_CG7113(scu)
            CEL: B0272.3 C29F3.1(ech-1) F01G10.2(ech-8) F01G10.3(ech-9)
                 F01G4.2(ard-1) F54C8.1 R09B5.6(hacd-1)
            ATH: AT3G06860(MFP2) AT4G29010(AIM1)
            OSA: 4326503 4328997
            ANI: AN7238.2
            AOR: AO090009000113
            CNE: CNC03600 CNH00460 CNI02410
            UMA: UM01099.1 UM03275.1
            DDI: DDBDRAFT_0168688
            CHO: Chro.30048
            TET: TTHERM_00016060 TTHERM_00085280 TTHERM_00085290
                 TTHERM_00085300 TTHERM_00085310 TTHERM_00317440
            TBR: Tb927.2.4130
            TCR: 507547.40 509701.10 509717.90 510105.240
            LMA: LmjF24.2030 LmjF26.1550
            ECO: b2341(yfcX) b3846(fadB)
            ECJ: JW2338(yfcX) JW3822(fadB)
            ECE: Z3604 Z5367(fadB)
            ECS: ECs3224 ECs4774
            ECC: c2886 c4793(fadB)
            ECI: UTI89_C2625 UTI89_C4431(fadB)
            ECP: ECP_2379 ECP_4059
            ECV: APECO1_2611(fadB) APECO1_4225
            ECW: EcE24377A_2637(fadJ) EcE24377A_4365(fadB)
            ECX: EcHS_A2492(fadJ) EcHS_A4069(fadB)
            STY: STY2620 STY3577(fadB)
            STT: t0476 t3315(fadB)
            SPT: SPA0476(yfcX) SPA3823(fadB)
            SEC: SC2390(yfcX) SC3880(fadB)
            STM: STM2388(yfcX) STM3983(fadB)
            YPE: YPO2747(faoA) YPO3766(fadB)
            YPK: y0464(fadB) y1580
            YPM: YP_2417(faoA) YP_3282(fadB)
            YPA: YPA_2097 YPA_3436
            YPN: YPN_0198 YPN_2200
            YPS: YPTB0267(fadB) YPTB2636(faoA)
            YPI: YpsIP31758_0283(fadB) YpsIP31758_1400(fadJ)
            SFL: SF2419 SF3922(fadB)
            SFX: S2554 S3830(fadB)
            SFV: SFV_2409 SFV_3654(fadB)
            SSN: SSON_2397 SSON_4019(fadB)
            SBO: SBO_2379
            SDY: SDY_2542 SDY_3899(fadB)
            ECA: ECA0208(fadB) ECA3078
            PLU: plu3200 plu4402(fadB)
            APL: APL_0888(fadJ)
            XCC: XCC1266(fadB) XCC1831(hadH2) XCC1979(fadB)
            XCB: XC_2205 XC_2358 XC_2975
            XCV: XCV1369(fadB) XCV1896 XCV2064(fadB)
            XAC: XAC1318(fadB) XAC1850(hadH2) XAC2013(fadB)
            XOO: XOO1848(fadB) XOO2537(fadB) XOO2904(hadH2)
            XOM: XOO_1744(XOO1744) XOO_2395(XOO2395) XOO_2754(XOO2754)
            VCH: VC1047 VC2758
            VVU: VV1_0981 VV1_1976
            VVY: VV0029 VV2440
            VPA: VP0030 VP2208
            VFI: VF0025 VF1810
            PPR: PBPRA0064 PBPRA0962
            PAE: PA1737 PA2554 PA3014(faoA) PA5188 PA5386
            PAU: PA14_31510 PA14_68530 PA14_71140
            PAP: PSPA7_2145(fadB)
            PPU: PP_0302 PP_2047 PP_2136(fadB) PP_2214(fadB2x)
            PST: PSPTO_3517(fadB)
            PSB: Psyr_2918 Psyr_3290
            PSP: PSPPH_3210(fadB)
            PFL: PFL_0290 PFL_1940(fadB) PFL_3067 PFL_5754(hbd-8)
            PFO: Pfl_0276 Pfl_2869 Pfl_3879 Pfl_5232
            PEN: PSEEN3548(fadB2x) PSEEN3728(fadB) PSEEN5183
            PAR: Psyc_0822 Psyc_1399 Psyc_1934(fadB)
            ACI: ACIAD0335(fadB) ACIAD1565 ACIAD2416
            SON: SO_0021(fadB) SO_3088
            SDN: Sden_0015 Sden_1530
            SFR: Sfri_0013
            SHE: Shewmr4_0018 Shewmr4_1408
            SHM: Shewmr7_0016 Shewmr7_1473
            SHN: Shewana3_0024 Shewana3_1461
            ILO: IL0011(fadB) IL0993
            CPS: CPS_0393(fadB) CPS_2720 CPS_3156(fadJ)
            PHA: PSHAa0011(fadB) PSHAa0967(fadJ)
            PAT: Patl_0201 Patl_1664 Patl_2321
            CBU: CBU_0847
            LPN: lpg0905 lpg1352(fadB)
            LPF: lpl0937 lpl1305
            LPP: lpp0967 lpp1306
            FTU: FTT1530(fadB)
            FTF: FTF1530(fadB)
            FTH: FTH_0584(fadB)
            FTA: FTA_1353
            NOC: Noc_1733
            AEH: Mlg_2111
            HCH: HCH_04756
            CSA: Csal_3173
            ABO: ABO_0656 ABO_1566(fadB)
            AHA: AHA_0139(fadB) AHA_2154(fadJ)
            CVI: CV_2720(fadB)
            RSO: RSc0474(RS04421) RSc1759(RS02946) RSc2534(RS05766)
            REU: Reut_A0447 Reut_A0589 Reut_A1405 Reut_A1668 Reut_B3564
                 Reut_B3956 Reut_B4554 Reut_C5942
            REH: H16_A0282(paaH1) H16_A0602 H16_A1102(paaH2) H16_B0388
                 H16_B1652
            RME: Rmet_0386 Rmet_0531 Rmet_1855 Rmet_5155 Rmet_5433 Rmet_5511
            BMA: BMA0198 BMA0380 BMA1438 BMA3041 BMAA0492
            BML: BMA10299_A1822
            BXE: Bxe_A0762 Bxe_A1391 Bxe_A4037 Bxe_B0826 Bxe_C0280 Bxe_C0922
            BUR: Bcep18194_A5880 Bcep18194_A6047 Bcep18194_C6651
                 Bcep18194_C7117
            BCN: Bcen_1600
            BCH: Bcen2424_6231
            BAM: Bamb_2597 Bamb_5970
            BPS: BPSL0063 BPSL0649 BPSL0874 BPSL1325 BPSL1424 BPSS0568
            BPM: BURPS1710b_0287(fadB) BURPS1710b_0633(pimF)
                 BURPS1710b_0858(fadB) BURPS1710b_1079 BURPS1710b_1576
                 BURPS1710b_2455 BURPS1710b_A2130
            BTE: BTH_I0062 BTH_I0565 BTH_I0738 BTH_I2142 BTH_I2807 BTH_II1847
            PNU: Pnuc_0471
            BPE: BP0669 BP2038 BP2770
            BPA: BPP1725 BPP2559 BPP4217
            BBR: BB0762 BB2004 BB3383 BB4805
            RFR: Rfer_0271 Rfer_0998 Rfer_2204 Rfer_2386 Rfer_2754 Rfer_3517
            POL: Bpro_2573 Bpro_3016 Bpro_3093 Bpro_3114 Bpro_3956
            AJS: Ajs_1606
            VEI: Veis_1285
            MPT: Mpe_A0417 Mpe_A1775 Mpe_A2489
            MMS: mma_3090
            NEU: NE1528
            NMU: Nmul_A0097
            EBA: c2A313(bbsD) c2A314(bbsC) ebA5126 ebA5320
            AZO: azo1338
            DAR: Daro_0710 Daro_2350
            BBA: Bd1836
            ADE: Adeh_0408
            MXA: MXAN_5136 MXAN_5371(fadJ)
            RPR: RP560(fadB)
            RTY: RT0547(fadB)
            RCO: RC0836 RC0837 RC0838 RC0839 RC0840 RC0841 RC0842
            RFE: RF_0890(fadB)
            AMA: AM752(fadB)
            PUB: SAR11_1333(fadB)
            MLO: mll4199 mlr2803 mlr5041 mlr5629
            MES: Meso_0021 Meso_1524
            SME: SMa1452 SMb21632 SMc01638 SMc02227(fadB)
            ATU: Atu0503(fadB) Atu1415 Atu5344
            ATC: AGR_C_2613 AGR_C_888 AGR_pAT_493
            RET: RHE_CH00559(fadB2) RHE_CH03794(hbdA) RHE_PC00067(ypc00039)
                 RHE_PC00126(ypc00064)
            RLE: pRL100300
            BME: BMEII0497 BMEII0816
            BMF: BAB2_0444 BAB2_0788 BAB2_0789
            BMS: BRA0449 BRA0793(fadB)
            BMB: BruAb2_0439(fadB)
            BOV: BOV_A0393
            BJA: bll7804 bll7821 blr1160(fadB) blr2428 blr7846
            BRA: BRADO0931(Hadh2) BRADO0964(hadH) BRADO0981(pimF) BRADO2315
                 BRADO6723
            BBT: BBta_0817 BBta_2678 BBta_7074(pimF) BBta_7091(hadH)
                 BBta_7121(hadh2)
            RPA: RPA0482 RPA0818 RPA1705 RPA2303 RPA3717(pimF)
            RPB: RPB_1684 RPB_1746 RPB_4604
            RPC: RPC_0735 RPC_2196 RPC_2226
            RPD: RPD_0807 RPD_3104 RPD_3553
            RPE: RPE_0674 RPE_3780 RPE_3825
            NHA: Nham_0357
            CCR: CC_0076 CC_0124 CC_3189
            SIL: SPO0739 SPO1436 SPO2487 SPO2705 SPO2920(fabJ-1)
                 SPOA0424(fabJ-2)
            SIT: TM1040_0921 TM1040_2186
            RSP: RSP_2196 RSP_3183 RSP_3535
            JAN: Jann_0664 Jann_3827
            RDE: RD1_2523 RD1_3147(hadH) RD1_3973(fadJ)
            PDE: Pden_2908
            MMR: Mmar10_0543 Mmar10_2653
            HNE: HNE_0672
            RRU: Rru_A1507
            MAG: amb3582
            ABA: Acid345_2469
            SUS: Acid_5696
            BSU: BG14024(yusL)
            BHA: BH3488
            BAN: BA5249
            BAR: GBAA5249
            BAA: BA_0114
            BAT: BAS4877
            BCE: BC5004
            BCA: BCE_5144
            BCZ: BCZK4734(fadB)
            BTK: BT9727_5027(hbd)
            BTL: BALH_4547(fadB)
            BLI: BL02180(yusL)
            BLD: BLi03466(yusL)
            BCL: ABC2990
            BPU: BPUM_2942
            OIH: OB0997 OB2395 OB2673
            GKA: GK3008
            SAU: SA0224
            SAV: SAV0232
            SAM: MW0208
            SAR: SAR0224(fadB)
            SAS: SAS0208
            SAC: SACOL0212
            SAB: SAB0171c
            SAA: SAUSA300_0226
            SAO: SAOUHSC_00196
            SEP: SE0220
            SER: SERP2360
            SSP: SSP0449 SSP2424
            CTC: CTC02426
            CHY: CHY_1609
            DSY: DSY3313 DSY3369 DSY4723
            MTU: Rv0860(fadB) Rv1144
            MTC: MT0484 MT0883 MT1177
            MBO: Mb0883(fadB) Mb1176
            MLE: ML2161(fadB) ML2461(fadB2)
            MPA: MAP0790(fadB_1) MAP1715(fadB_2) MAP2637c MAP3116c
                 MAP3962(fadB2)
            MAV: MAV_1812 MAV_2552 MAV_3936 MAV_5146
            MSM: MSMEG_0216 MSMEG_2279 MSMEG_4871 MSMEG_5183 MSMEG_5943
            CEF: CE0722
            CJK: jk0159(fadB1)
            NFA: nfa1180 nfa24240 nfa2860(fadB) nfa52290(fadB5)
            RHA: RHA1_ro00407 RHA1_ro02293 RHA1_ro02861(paaC) RHA1_ro03392
                 RHA1_ro03952 RHA1_ro04000 RHA1_ro06116(fadB2) RHA1_ro06852
                 RHA1_ro10317
            SCO: SCO0984(SCBAC19F3.11) SCO1591(SCI35.13) SCO6297(SCBAC8D1.10c)
                 SCO6732(SC5F2A.15) SCO6789(SC6A5.38)
            SMA: SAV1680(fadB1) SAV2045(fadC2) SAV2889(fadC4) SAV6748(fadC5)
                 SAV716(fadC6)
            LXX: Lxx04210(fadB)
            ART: Arth_0886
            TFU: Tfu_0275 Tfu_1279
            FRA: Francci3_1000 Francci3_1557 Francci3_3423 Francci3_3694
                 Francci3_4139
            FAL: FRAAL2831 FRAAL3114(fadB) FRAAL3518 FRAAL5547 FRAAL5917
            SEN: SACE_0092 SACE_1823 SACE_1902(fadB2) SACE_2849 SACE_3445
                 SACE_3866 SACE_5408 SACE_6362(fadB)
            RXY: Rxyl_1736
            RBA: RB1092(faoA)
            LIL: LA4138(had)
            LIC: LIC13300(fadB)
            LBJ: LBJ_2902(fadB)
            LBL: LBL_0161(fadB)
            SRU: SRU_1210 SRU_1459(yfcX)
            CHU: CHU_3591(fadB)
            GFO: GFO_0666 GFO_1047
            DRA: DR_1487 DR_2477 DR_A0143
            DGE: Dgeo_0617
            TTH: TTC0331 TTC0534
            TTJ: TTHA0691 TTHA0890
            MSI: Msm_0965
            AFU: AF0017(hbd-1) AF0285(hbd-2) AF1122(hbd-5) AF2273(hbd-10)
            HAL: VNG0681G(hbd1) VNG1313G(hbd2)
            HMA: rrnAC0264(hbd-1) rrnAC0771(paaH) rrnAC1083(hbd1)
                 rrnAC1982(hbd2) rrnB0238(hbd3)
            HWA: HQ2302A(hbd)
            NPH: NP1906A(hbd_4) NP2630A(hbd_1) NP2754A(hbd_2) NP4322A(hbd_3)
            TAC: Ta0291 Ta0476
            TVO: TVN0826 TVN1310
            APE: APE_1484.1
            SSO: SSO2514
            STO: ST0069
            SAI: Saci_1109 Saci_1134 Saci_2208 Saci_2218
            PAI: PAE1383
STRUCTURES  PDB: 1E3S  1E3W  1E6W  1F0Y  1F12  1F14  1F17  1IL0  1LSJ  1LSO  
                 1M75  1M76  1SO8  1U7T  1WDK  1WDL  1WDM  1ZBQ  1ZCJ  1ZEJ  
                 2D3T  2HDH  3HAD  3HDH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.35
            ExPASy - ENZYME nomenclature database: 1.1.1.35
            ExplorEnz - The Enzyme Database: 1.1.1.35
            ERGO genome analysis and discovery system: 1.1.1.35
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.35
            BRENDA, the Enzyme Database: 1.1.1.35
            CAS: 9028-40-4
///
ENTRY       EC 1.1.1.36                 Enzyme
NAME        acetoacetyl-CoA reductase;
            acetoacetyl coenzyme A reductase;
            hydroxyacyl coenzyme-A dehydrogenase;
            NADP+-linked acetoacetyl CoA reductase;
            NADPH:acetoacetyl-CoA reductase;
            D(-)-beta-hydroxybutyryl CoA-NADP+ oxidoreductase;
            short chain beta-ketoacetyl(acetoacetyl)-CoA reductase;
            beta-ketoacyl-CoA reductase;
            D-3-hydroxyacyl-CoA reductase;
            (R)-3-hydroxyacyl-CoA dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-3-hydroxyacyl-CoA:NADP+ oxidoreductase
REACTION    (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH + H+
            [RN:R01779]
ALL_REAC    R01779 > R01977
SUBSTRATE   (R)-3-hydroxyacyl-CoA [CPD:C01086];
            NADP+ [CPD:C00006]
PRODUCT     3-oxoacyl-CoA [CPD:C00264];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Wakil, S.J. and Bressler, R.
  TITLE     Studies on the mechanism of fatty acid synthesis. X. Reduced
            triphosphopyridine nucleotide-acetoacetyl coenzyme A reductase.
  JOURNAL   J. Biol. Chem. 237 (1962) 687-693.
  ORGANISM  pigeon
PATHWAY     PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K00023  acetoacetyl-CoA reductase
GENES       XFA: XF0319
            XFT: PD0262(fabG)
            XCC: XCC2294(phbB) XCC3355(phbB)
            XCB: XC_0809 XC_1821
            XCV: XCV2598(phbB) XCV3614(phbB)
            XAC: XAC2401(phbB) XAC3486(phbB)
            XOO: XOO1102(phbB) XOO2728(phbB)
            XOM: XOO_1000(XOO1000) XOO_2573(XOO2573)
            VCH: VCA0691
            VCO: VC0395_0631
            VVU: VV2_0742
            VVY: VVA1211
            VPA: VPA1205
            PPR: PBPRB1841(phbB)
            SON: SO_3263
            CPS: CPS_2625(phbB1) CPS_4092(phbB2)
            LPN: lpg0560(phaB) lpg0561(phaB) lpg1059(phaB)
            LPF: lpl0603 lpl0604 lpl1056 lpl2305
            LPP: lpp0620 lpp0621 lpp2322
            AEH: Mlg_2486
            HCH: HCH_04996(phbB)
            CSA: Csal_3029
            AHA: AHA_1951
            CVI: CV_2364(phaB)
            RSO: RSc1633(phbB)
            REU: Reut_A1349 Reut_B3865 Reut_B4127 Reut_C6018
            REH: H16_A1439(phaB1) H16_A2002(phaB2) H16_A2171(phaB3)
            RME: Rmet_1333 Rmet_1358 Rmet_5123
            BMA: BMA1320(phbB-1) BMAA0166(phbB-2)
            BMV: BMASAVP1_1337(phbB-1) BMASAVP1_A1809(phbB-2)
            BML: BMA10299_A0087(phbB-1)
            BMN: BMA10247_1080(phbB-2) BMA10247_A0193(phbB-1)
            BXE: Bxe_A2341 Bxe_B0354
            BUR: Bcep18194_A5090 Bcep18194_A6101
            BCN: Bcen_2157 Bcen_6290
            BCH: Bcen2424_1789 Bcen2424_2771
            BAM: Bamb_1727 Bamb_2823
            BPS: BPSL1536(phbB) BPSS1916(phbB)
            BPM: BURPS1710b_2329(phbB-1) BURPS1710b_A1014(phbB-2)
            BPL: BURPS1106A_2201(phbB) BURPS1106A_A2601(phbB)
            BPD: BURPS668_2164(phbB) BURPS668_A2744(phbB)
            BTE: BTH_I2257 BTH_II0461
            BPE: BP0772(fabG) BP1150(phbB)
            BPA: BPP0333(fabG) BPP3195(phbB)
            BBR: BB0336(fabG) BB3595(phbB) BB4750
            RFR: Rfer_2560
            POL: Bpro_1198 Bpro_2141
            MPT: Mpe_A1868
            HAR: HEAR0578(phbB) HEAR2345(phbB)
            MMS: mma_0556
            EBA: ebA4729(phbB) ebA4731(adh)
            AZO: azo1022(phbB1) azo1023(phbB2)
            DAR: Daro_1609 Daro_1610
            PCA: Pcar_1120
            RPR: RP035(phbB)
            RTY: RT0095(phbB)
            RCO: RC0054(phbB)
            RAK: A1C_00095
            RBO: A1I_07605
            MLO: mlr3848
            MES: Meso_3375
            SME: SMc03878(phbB)
            ATU: Atu2770(phbB)
            ATC: AGR_C_5024(phbB)
            RET: RHE_CH04019(phbB)
            RLE: RL4620(phaB)
            BJA: bll0225(phbB) blr3725(phbB)
            BRA: BRADO0563(phbB)
            BBT: BBta_7613(phbB)
            RPA: RPA0532
            RPB: RPB_0508
            RPC: RPC_0505
            RPD: RPD_0305
            RPE: RPE_0167
            NWI: Nwi_3061
            NHA: Nham_3689
            CCR: CC_0511
            SIL: SPO0325(phbB)
            SIT: TM1040_3736
            RSP: RSP_0747 RSP_3963
            JAN: Jann_0492
            RDE: RD1_3395(phbB)
            MMR: Mmar10_2384
            HNE: HNE_3404(phbB)
            NAR: Saro_3212
            SAL: Sala_2255
            ELI: ELI_12280
            GBE: GbCGDNIH1_0449 GbCGDNIH1_2279
            RRU: Rru_A0273 Rru_A1309
            MAG: amb0843
            MGM: Mmc1_1166
            BAN: BA1330
            BAR: GBAA1330
            BAA: BA_1853
            BAT: BAS1230
            BCE: BC1317(fabG)
            BCA: BCE_1429
            BTK: BT9727_1207(phaB)
            CGL: NCgl2358(cgl2444)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.36
            ExPASy - ENZYME nomenclature database: 1.1.1.36
            ExplorEnz - The Enzyme Database: 1.1.1.36
            ERGO genome analysis and discovery system: 1.1.1.36
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.36
            BRENDA, the Enzyme Database: 1.1.1.36
            CAS: 9028-41-5
///
ENTRY       EC 1.1.1.37                 Enzyme
NAME        malate dehydrogenase;
            malic dehydrogenase;
            L-malate dehydrogenase;
            NAD-L-malate dehydrogenase;
            malic acid dehydrogenase;
            NAD-dependent malic dehydrogenase;
            NAD-malate dehydrogenase;
            NAD-malic dehydrogenase;
            malate (NAD) dehydrogenase;
            NAD-dependent malate dehydrogenase;
            NAD-specific malate dehydrogenase;
            NAD-linked malate dehydrogenase;
            MDH;
            L-malate-NAD+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-malate:NAD+ oxidoreductase
REACTION    (S)-malate + NAD+ = oxaloacetate + NADH + H+ [RN:R00342]
ALL_REAC    R00342
SUBSTRATE   (S)-malate [CPD:C00149];
            NAD+ [CPD:C00003]
PRODUCT     oxaloacetate [CPD:C00036];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also oxidizes some other 2-hydroxydicarboxylic acids.
REFERENCE   1
  AUTHORS   Banaszak, L.J. and Bradshaw, R.A.
  TITLE     Malate dehydrogenase.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 11, Academic
            Press, New York, 1975, p. 369-396.
REFERENCE   2  [PMID:5637713]
  AUTHORS   Guha A, Englard S, Listowsky I.
  TITLE     Beef heart malic dehydrogenases. VII. Reactivity of sulfhydryl
            groups and conformation of the supernatant enzyme.
  JOURNAL   J. Biol. Chem. 243 (1968) 609-15.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:4313528]
  AUTHORS   McReynolds MS, Kitto GB.
  TITLE     Purification and properties of Drosophila malate dehydrogenases.
  JOURNAL   Biochim. Biophys. Acta. 198 (1970) 165-75.
  ORGANISM  Drosophila virilis, Drosophila melanogaster [GN:dme]
REFERENCE   4  [PMID:13345798]
  AUTHORS   WOLFE RG, NEILANDS JB.
  TITLE     Some molecular and kinetic properties of heart malic dehydrogenase.
  JOURNAL   J. Biol. Chem. 221 (1956) 61-9.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00620  Pyruvate metabolism
            PATH: map00630  Glyoxylate and dicarboxylate metabolism
            PATH: map00710  Carbon fixation
            PATH: map00720  Reductive carboxylate cycle (CO2 fixation)
ORTHOLOGY   KO: K00024  malate dehydrogenase
            KO: K00025  malate dehydrogenase
            KO: K00026  malate dehydrogenase
GENES       HSA: 4190(MDH1) 4191(MDH2)
            PTR: 463484(MDH2)
            MMU: 17448(Mdh2) 17449(Mdh1)
            RNO: 24551(Mdh1) 81829(Mdh2)
            CFA: 474614(MDH1) 482601(LOC482601) 482945(MDH2) 485162(LOC485162)
            BTA: 281306(MDH2)
            SSC: 396894(MDH1)
            GGA: 417517(MDH2) 421281(MDH1)
            XLA: 398872(MGC68659) 443751(MGC79037)
            XTR: 448318(mdh1) 496892(Mdh2)
            DRE: 335715(mdh1b) 406405(zgc:64133)
            SPU: 587163(LOC587163) 591635(LOC591635)
            DME: Dmel_CG10748 Dmel_CG10749 Dmel_CG5362 Dmel_CG7998
            CEL: F20H11.3(mdh-1) F46E10.10
            ATH: AT1G04410 AT1G53240 AT2G22780(PMDH1) AT3G15020 AT3G47520(MDH)
                 AT5G43330 AT5G56720
            OSA: 4326249 4327423 4334274 4336595 4348905 4352871
            CME: CMP193C CMT611C
            SCE: YDL078C(MDH3) YKL085W(MDH1) YOL126C(MDH2)
            AGO: AGOS_ADL164C AGOS_ADR152C AGOS_ADR252W
            PIC: PICST_40132(MDHM) PICST_66451(MDH1) PICST_78343(MDH2)
            CAL: CaO19_4602(CaO19.4602) CaO19_7481(CaO19.7481)
            CGR: CAGL0E01705g CAGL0L05236g CAGL0L06798g
            SPO: SPCC306.08c
            ANI: AN6499.2 AN6717.2
            AFM: AFUA_6G05210 AFUA_7G05740
            AOR: AO090005000438 AO090701000013
            CNE: CNG03100 CNG03490
            UMA: UM00403.1
            DDI: DDB_0230186(mdhA) DDB_0230187(mdhC) DDB_0230188(mdhB)
            PFA: PFF0895w
            CPV: cgd7_470
            CHO: Chro.70062
            TAN: TA09590
            TPV: TP01_1182
            TET: TTHERM_00030190 TTHERM_00052260 TTHERM_00237500
            TBR: Tb10.61.0980 Tb10.70.5110 Tb10.70.5120 Tb11.01.3040
            TCR: 506195.110 506937.10 507883.100 507883.109 510437.40
                 511293.69
            LMA: LmjF28.2860 LmjF34.0130 LmjF34.0140 LmjF34.0160
            EHI: 195.t00003 195.t00006 24.t00003 26.t00021 273.t00010
                 37.t00001 429.t00004 8.t00059
            ECO: b0801(ybiC) b3236(mdh)
            ECJ: JW0786(ybiC) JW3205(mdh)
            ECE: Z1022(ybiC) Z4595(mdh)
            ECS: ECs0879 ECs4109
            ECC: c0885(ybiC) c3991(mdh) c5039
            ECI: UTI89_C0804(ybiC) UTI89_C3667(mdh)
            ECP: ECP_0815 ECP_3319
            ECV: APECO1_1289(ybiC) APECO1_3208(mdh)
            ECW: EcE24377A_3719(mdh)
            ECX: EcHS_A3425
            STY: STY3539(mdh)
            STT: t3274(mdh)
            SPT: SPA3226(mdh)
            SEC: SC3297(mdh)
            STM: STM3081 STM3359(mdh)
            YPE: YPO3516(mdh)
            YPK: y0668(mdh)
            YPM: YP_0567(mdh)
            YPA: YPA_0066
            YPN: YPN_3260
            YPP: YPDSF_3565
            YPS: YPTB0460(mdh)
            YPI: YpsIP31758_3616(mdh)
            YEN: YE0414(mdh)
            SFL: SF0751(ybiC) SF3276(mdh)
            SFX: S0792(ybiC) S3491(mdh)
            SFV: SFV_0784(ybiC) SFV_3263(mdh)
            SSN: SSON_0780(ybiC) SSON_3378(mdh)
            SBO: SBO_0689(ybiC) SBO_3153(mdh)
            SDY: SDY_0798(ybiC) SDY_3412(mdh)
            ECA: ECA0685(mdh) ECA1527
            PLU: plu4547(mdh)
            SPE: Spro_3596
            HIN: HI1210(mdh)
            HIT: NTHI1381(mdh)
            HIP: CGSHiEE_05985
            HIQ: CGSHiGG_09775
            HDU: HD0264(mdh)
            HSO: HS_1055(mdh)
            PMU: PM0550(mdh_2)
            MSU: MS1266(mdh)
            APL: APL_1296(mdh)
            ASU: Asuc_0893
            XFA: XF1211
            XFT: PD0492(mdh)
            XCC: XCC0928(mdh)
            XCB: XC_3307
            XCV: XCV1034(mdh)
            XAC: XAC1006(mdh)
            XOO: XOO0971(mdh)
            XOM: XOO_0886(XOO0886)
            VCH: VC0432
            VCO: VC0395_A2850(mdh)
            VVU: VV1_0673
            VVY: VV0467
            VPA: VP0325
            VFI: VF0276 VF1252
            PPR: PBPRA0391(mdh)
            PAE: PA1252
            PAU: PA14_48020
            PPU: PP_0654(mdh) PP_3591
            PPF: Pput_1071
            PST: PSPTO_2359(allD)
            PSB: Psyr_2143
            PSP: PSPPH_2118
            PFL: PFL_1416 PFL_2200 PFL_2905 PFL_3547
            PFO: Pfl_2567
            PEN: PSEEN2621(mdh) PSEEN2669
            PMY: Pmen_3486
            PAR: Psyc_1763(mdh)
            PCR: Pcryo_2044
            PRW: PsycPRwf_1261
            ACI: ACIAD3155(mdh)
            SON: SO_0770(mdh)
            SDN: Sden_0826
            SFR: Sfri_3173
            SAZ: Sama_0672
            SBL: Sbal_0609
            SBM: Shew185_2999
            SLO: Shew_0867
            SSE: Ssed_3124
            SPL: Spea_1313
            SHE: Shewmr4_3339
            SHM: Shewmr7_0614
            SHN: Shewana3_3509
            SHW: Sputw3181_0722
            ILO: IL0472(mdh)
            CPS: CPS_4514(mdh)
            PHA: PSHAa2658(mdh)
            PAT: Patl_0539
            PIN: Ping_0297
            CBU: CBU_1241(mdh)
            CBD: COXBU7E912_1325(mdh)
            LPN: lpg2352(mdh)
            LPF: lpl2274(mdh)
            LPP: lpp2301(mdh)
            MCA: MCA0610(mdh)
            FTU: FTT0535c(mdh)
            FTF: FTF0535c(mdh)
            FTW: FTW_1007(mdh)
            FTL: FTL_0987
            FTH: FTH_0966(mdh)
            FTA: FTA_1040(mdh)
            FTN: FTN_0980(mdh)
            NOC: Noc_2802
            HCH: HCH_01978(mdh)
            ABO: ABO_1248(mdh)
            MMW: Mmwyl1_4148
            AHA: AHA_0659(mdh)
            CVI: CV_1062(mdh)
            RSO: RSc1998(mdh)
            REU: Reut_A1498 Reut_A2327 Reut_C6359
            REH: H16_A2634(mdh1) H16_B0334(mdh2)
            RME: Rmet_1634 Rmet_2489 Rmet_5095
            BMA: BMAA1423 BMAA1751(mdh)
            BMV: BMASAVP1_1619(mdh)
            BML: BMA10299_1827(mdh)
            BMN: BMA10247_A0497(mdh)
            BXE: Bxe_B2898
            BVI: Bcep1808_4408
            BUR: Bcep18194_B0783 Bcep18194_B1898 Bcep18194_B2154
            BCN: Bcen_3456 Bcen_4230 Bcen_4435
            BCH: Bcen2424_3932 Bcen2424_4136 Bcen2424_4910
            BAM: Bamb_3309
            BPS: BPSS0328 BPSS1722(mdh)
            BPM: BURPS1710b_A0795(mdh) BURPS1710b_A1882
            BTE: BTH_II0658 BTH_II2071
            BPE: BP2365(mdH) BP2521 BP2780
            BPA: BPP2552 BPP3232(mdH) BPP4084
            BBR: BB1997 BB2374 BB3684(mdH) BB4555
            RFR: Rfer_1803 Rfer_2403
            POL: Bpro_3598 Bpro_3968
            PNA: Pnap_3030
            VEI: Veis_4356
            MPT: Mpe_A2172 Mpe_B0497
            HAR: HEAR1780(mdh)
            MMS: mma_1504
            NEU: NE0773
            NET: Neut_1633
            NMU: Nmul_A0864
            EBA: ebA6695(mdh)
            AZO: azo1547(mdh)
            DAR: Daro_2867
            HHE: HH1571(mdh)
            WSU: WS1064(citH)
            TDN: Tmden_1048
            CJE: Cj0532(mdh)
            CJR: CJE0636(mdh)
            CJJ: CJJ81176_0557(mdh)
            CJU: C8J_0493(mdh)
            CJD: JJD26997_1398(mdh)
            CFF: CFF8240_0912
            CHA: CHAB381_1136
            CCO: CCC13826_2254
            ABU: Abu_1315(mdh)
            NIS: NIS_0835(mdh)
            SUN: SUN_0571 SUN_0572
            GSU: GSU1466(mdh)
            GME: Gmet_1360
            GUR: Gura_3124
            PCA: Pcar_1037
            PPD: Ppro_2327
            BBA: Bd0928(mdh)
            DPS: DP0661
            ADE: Adeh_1626 Adeh_2226
            AFW: Anae109_1524 Anae109_3133
            MXA: MXAN_3538(mdh)
            SFU: Sfum_0460
            RPR: RP376(mdh)
            RTY: RT0365(mdh)
            RCO: RC0520(mdh)
            RFE: RF_0590(mdh)
            RBE: RBE_0644(mdh)
            RAK: A1C_02825
            RBO: A1I_04320
            RRI: A1G_02950
            WOL: WD1121(mdh)
            WBM: Wbm0244
            AMA: AM564(mdh)
            APH: APH_0629(mdh)
            ERU: Erum4090(mdh) Erum4380
            ERW: ERWE_CDS_04240(mdh)
            ERG: ERGA_CDS_04180(mdh)
            ECN: Ecaj_0398
            ECH: ECH_0641(mdh)
            NSE: NSE_0956(mdh)
            PUB: SAR11_0240(mdh) SAR11_0966(yiaK)
            MLO: mll4308 mll5197 mlr9117 mlr9216
            MES: Meso_3395
            PLA: Plav_1168
            SME: SMa0265 SMa1459 SMb20261 SMc02035 SMc02479(mdh)
            SMD: Smed_0379
            ATU: Atu0164(mdh) Atu2639(mdh) Atu3208 Atu4676(mdh)
            ATC: AGR_C_268 AGR_C_4782 AGR_L_3209 AGR_L_410
            RET: RHE_CH03891(mdh) RHE_PF00366 RHE_PF00428(ypf00228)
            RLE: RL4439(mdh) pRL120513 pRL120601
            BME: BMEI0137 BMEII1005
            BMF: BAB1_1927(mdh) BAB2_0960
            BMS: BR1927(mdh) BRA0240
            BMB: BruAb1_1903(mdh) BruAb2_0939
            BOV: BOV_1856(mdh)
            OAN: Oant_3052
            BJA: bll0456(mdh) bll2917 bll6274 blr7581
            BRA: BRADO0403(mdh)
            BBT: BBta_0392(mdh)
            RPA: RPA0192(mdh) RPA3756
            RPB: RPB_0281 RPB_1710
            RPC: RPC_0194 RPC_1699 RPC_4584
            RPD: RPD_0535 RPD_3587
            RPE: RPE_0300
            NWI: Nwi_0419
            NHA: Nham_0545
            BHE: BH16570(mdh)
            BQU: BQ13450(mdh)
            BBK: BARBAKC583_0022(mdh)
            XAU: Xaut_3123
            CCR: CC_3655
            SIL: SPO0349(mdh) SPO3187
            SIT: TM1040_3323 TM1040_3386 TM1040_3517
            RSP: RSP_0968(mdh)
            RSH: Rsph17029_2628
            RSQ: Rsph17025_1152
            JAN: Jann_0818 Jann_2141
            RDE: RD1_1617(mdh) RD1_2049
            PDE: Pden_0561
            MMR: Mmar10_0711 Mmar10_2829
            HNE: HNE_3218(mdh)
            NAR: Saro_1182
            SAL: Sala_2230
            SWI: Swit_0405
            ELI: ELI_07980
            GBE: GbCGDNIH1_2071
            ACR: Acry_1194 Acry_3063
            RRU: Rru_A1210
            MAG: amb3957
            MGM: Mmc1_0813
            ABA: Acid345_1951
            SUS: Acid_1549 Acid_4704
            BSU: BG11386(mdh) BG13206(yjmC)
            BHA: BH3158(citH)
            BAN: BA4837(mdh)
            BAR: GBAA4837(mdh)
            BAA: BA_5260
            BAT: BAS4486
            BCE: BC4592
            BCA: BCE_4723(mdh)
            BCZ: BCZK4333(mdh) BCZK4344(mdh)
            BCY: Bcer98_0008
            BTK: BT9727_4321(mdh) BT9727_4332(mdh)
            BTL: BALH_4176(mdh) BALH_4186(mdh)
            BLI: BL00397(mdh)
            BLD: BLi03060(mdh)
            BCL: ABC2713(mdh)
            BAY: RBAM_026160
            BPU: BPUM_2554
            OIH: OB2166(citH) OB2846
            GKA: GK2734
            GTN: GTNG_2658
            SAJ: SaurJH9_0437
            SAH: SaurJH1_0448
            SEP: SE0461
            SER: SERP0347(mdh)
            SSP: SSP2027
            LPL: lp_3150
            LSA: LSA0444
            LRE: Lreu_0116
            STH: STH2543
            CAC: CAC0566
            CBE: Cbei_0331
            CKL: CKL_2769(mdh)
            AMT: Amet_0909
            DSY: DSY3584
            DRM: Dred_1867
            CSC: Csac_1713
            MTU: Rv1240(mdh)
            MTC: MT1278(mdh)
            MBO: Mb1272(mdh)
            MBB: BCG_1300(mdh)
            MLE: ML1091(mdh)
            MPA: MAP2541c(mdh)
            MAV: MAV_1380
            MVA: Mvan_3067
            MGI: Mflv_3339
            CGL: NCgl2297(cgl2380)
            CGB: cg2613(mdh)
            CEF: CE2285(mdh)
            CDI: DIP1787(mdh)
            CJK: jk0548(mdh)
            NFA: nfa36620(mdh)
            RHA: RHA1_ro06244(mdh)
            SCO: SCO4827(mdh)
            SMA: SAV3436(mdh)
            AAU: AAur_0570(mdh)
            PAC: PPA1740
            NCA: Noca_3578
            TFU: Tfu_0092
            FRA: Francci3_3441
            FAL: FRAAL5612(mdh)
            KRA: Krad_0742 Krad_1231
            SEN: SACE_3674(mdh)
            STP: Strop_0848 Strop_3837
            RBA: RB7652(mdh) RB856(ldh)
            CTR: CT376(mdhC)
            CTA: CTA_0410(mdhC)
            CMU: TC0655
            CPN: CPn1028(mdhC)
            CPA: CP0824
            CPJ: CPj1028(mdhC)
            CPT: CpB1067
            CCA: CCA00734(mdh)
            CFE: CF0282(mdhC)
            PCU: pc1772(mdh)
            LIL: LA2139(mdh)
            LIC: LIC11781(mdh)
            LBJ: LBJ_1874(mdh)
            LBL: LBL_1410(mdh)
            SYN: sll0891(citH)
            GVI: gll2542
            ANA: alr4322
            AVA: Ava_1273
            PMB: A9601_16921(hisD)
            PMC: P9515_16681(hisD)
            PMF: P9303_04331(hisD)
            PMG: P9301_16791(hisD)
            PMH: P9215_17571(hisD)
            PME: NATL1_18891(hisD)
            BTH: BT_2510 BT_3911
            BFR: BF0541 BF3978
            BFS: BF0489 BF3753(mdh)
            PGI: PG1949(mdh)
            SRU: SRU_1571(mdh)
            CHU: CHU_0320(ybiC) CHU_3020(mdh)
            GFO: GFO_2747(mdh)
            FJO: Fjoh_2217
            FPS: FP0528(mdh)
            CTE: CT1507(mdh)
            CPH: Cpha266_1900
            PLT: Plut_1510
            DET: DET0451(mdh)
            DEH: cbdb_A409(mdh)
            RRS: RoseRS_0697
            RCA: Rcas_0207
            DRA: DR_0325
            DGE: Dgeo_2161
            TTH: TTC0168
            TTJ: TTHA0536
            AAE: aq_1665(mdh2) aq_1782(mdh1)
            TPT: Tpet_1436
            TME: Tmel_1578
            FNO: Fnod_0116
            MJA: MJ0490(ldh)
            MMP: MMP0645(mdh)
            MMQ: MmarC5_0959
            MMZ: MmarC7_1669
            MAC: MA0819
            MBA: Mbar_A1748
            MMA: MM_1966
            MHU: Mhun_1155
            MTH: MTH188
            MST: Msp_0672
            MKA: MK1069(ldh)
            AFU: AF0855(mdhA)
            HAL: VNG2367G(mdhA)
            HMA: rrnAC2706(mdh)
            HWA: HQ3459A(mdhA)
            NPH: NP0498A(mdhA)
            TAC: Ta0952
            TVO: TVN1097
            PTO: PTO0994
            PHO: PH1277
            PAB: PAB1791
            APE: APE_0672.1
            SSO: SSO2585(sqdB)
            STO: ST1811 ST2090
            SAI: Saci_0246
            PAI: PAE2370
STRUCTURES  PDB: 1BDM  1BMD  1D3A  1EMD  1GT2  1GUY  1GUZ  1GV0  1GV1  1HLP  
                 1HR9  1IB6  1IE3  1IZ9  1MLD  1O6Z  1OJS  1OJU  1SEV  1SMK  
                 1UR5  1UXG  1UXH  1UXI  1UXJ  1UXK  1V9N  1WZE  1WZI  1Y7T  
                 2CMD  2CVQ  2D4A  2DFD  2HLP  2J5K  2J5Q  2J5R  2PWZ  4MDH  
                 5MDH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.37
            ExPASy - ENZYME nomenclature database: 1.1.1.37
            ExplorEnz - The Enzyme Database: 1.1.1.37
            ERGO genome analysis and discovery system: 1.1.1.37
            BRENDA, the Enzyme Database: 1.1.1.37
            CAS: 9001-64-3
///
ENTRY       EC 1.1.1.38                 Enzyme
NAME        malate dehydrogenase (oxaloacetate-decarboxylating);
            'malic' enzyme;
            pyruvic-malic carboxylase;
            NAD+-specific malic enzyme;
            NAD+-malic enzyme;
            NAD+-linked malic enzyme
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-malate:NAD+ oxidoreductase (oxaloacetate-decarboxylating)
REACTION    (S)-malate + NAD+ = pyruvate + CO2 + NADH [RN:R00214]
ALL_REAC    R00214;
            (other) R00216
SUBSTRATE   (S)-malate [CPD:C00149];
            NAD+ [CPD:C00003]
PRODUCT     pyruvate [CPD:C00022];
            CO2 [CPD:C00011];
            NADH [CPD:C00004]
COMMENT     Also decarboxylates added oxaloacetate.
REFERENCE   1
  AUTHORS   Kaufman, S., Korkes, S. and del Campillo, A.
  TITLE     Biosynthesis of dicarboxylic acids by carbon dioxide fixation. V.
            Further studies of the "malic" enzyme of Lactobacillus arabinosus.
  JOURNAL   J. Biol. Chem. 192 (1951) 301-312.
  ORGANISM  Lactobacillus arabinosus
PATHWAY     PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K00027  malate dehydrogenase (oxaloacetate-decarboxylating)
GENES       HSA: 4200(ME2)
            MMU: 107029(Me2)
            CFA: 476198(ME2)
            XLA: 398584(me2)
            SCE: YKL029C(MAE1)
            AGO: AGOS_AGL068W
            PIC: PICST_89732(MAE1)
            CGR: CAGL0L02035g
            SPO: SPCC794.12c(mae2)
            ANI: AN6933.2
            AFM: AFUA_7G02420
            AOR: AO090038000621
            CNE: CNF03780
            TET: TTHERM_00569410
            TBR: Tb11.02.3120 Tb11.02.3130
            TCR: 505183.20 505183.30 508647.270 508647.280
            LMA: LmjF24.0770
            EHI: 3.t00096 425.t00002
            ECO: b1479(maeA)
            ECJ: JW5238(sfcA)
            ECE: Z2231(sfcA)
            ECS: ECs2083
            ECC: c1912(sfcA)
            ECI: UTI89_C1697(sfcA)
            ECP: ECP_1481
            ECV: APECO1_615(sfcA)
            ECW: EcE24377A_1661(sfcA)
            ECX: EcHS_A1564(sfcA)
            STY: STY1494(sfcA)
            STT: t1481(sfcA)
            SPT: SPA1302(sfcA)
            SEC: SC1567(sfcA)
            STM: STM1566(sfcA)
            YPE: YPO1511(sfcA)
            YPK: y2658(sfcA)
            YPM: YP_1401(sfcA1)
            YPA: YPA_0806
            YPN: YPN_2468
            YPS: YPTB1526(sfcA)
            SFL: SF1746(sfcA)
            SFX: S1879(sfcA)
            SFV: SFV_1742(sfcA)
            SSN: SSON_1645(sfcA)
            SBO: SBO_1578(sfcA)
            ECA: ECA2831(sfcA)
            PLU: plu1546(maeA)
            SGL: SG0967
            ENT: Ent638_2047
            SPE: Spro_1567
            VCH: VC1188 VC2681
            VCO: VC0395_A0809(sfcA)
            VVU: VV1_1361 VV1_2801
            VVY: VV1464 VV2242 VV3010
            VPA: VP1258 VP2767
            VFI: VF1558
            PPR: PBPRA0259 PBPRA1997 PBPRB1354
            PAE: PA3471 PA5046
            PPU: PP_5085(maeB)
            PST: PSPTO_3924(sfcA) PSPTO_5134
            PSB: Psyr_0401 Psyr_1561
            PSP: PSPPH_1545
            PFL: PFL_0443
            PFO: Pfl_0403
            PAR: Psyc_1387
            ACI: ACIAD0166(sfcA)
            SON: SO_3855(sfcA) SO_4118
            SBM: Shew185_3634
            SSE: Ssed_3518
            SPL: Spea_3186
            SHN: Shewana3_3669
            ILO: IL0598(sfcA) IL2463
            CPS: CPS_0331 CPS_2051 CPS_4262(sfcA)
            CBU: CBU_0823(sfcA)
            CBD: COXBU7E912_0888(sfcA)
            LPN: lpg0651 lpg1280(sfcA) lpg2971(maeA)
            LPF: lpl0687 lpl1243(sfcA) lpl2901
            LPP: lpp0705 lpp1243(sfcA) lpp3043
            MCA: MCA1836(sfcA)
            FTU: FTT0917(maeA)
            FTF: FTF0917(maeA)
            FTW: FTW_1262
            FTL: FTL_0438
            FTH: FTH_0430(maeA)
            FTA: FTA_0460
            FTN: FTN_0443(maeA)
            HCH: HCH_05974(scfA)
            ABO: ABO_2239(maeB)
            AHA: AHA_1243 AHA_1278
            RMA: Rmag_0819
            NME: NMB0671
            NMA: NMA0870(maeA)
            NMC: NMC0620(maeA)
            NGO: NGO0240
            REH: H16_A3153(maeA)
            BPD: BURPS668_0794
            NEU: NE0438
            TBD: Tbd_1181
            HHE: HH1094
            CJE: Cj1287c
            CJR: CJE1479
            CJU: C8J_1230
            ABU: Abu_1076(maeA)
            GSU: GSU2308(scfA)
            BBA: Bd2834(sfcA)
            DPS: DP2203
            SAT: SYN_00517
            RTY: RT0361(tme)
            RCO: RC0507(tme)
            RFE: RF_0584(tme)
            RBE: RBE_0869(tme)
            OTS: OTBS_1313(maeA)
            BJA: bll6469
            BRA: BRADO5322
            BBT: BBta_5810
            RSP: RSP_1217
            ZMO: ZMO1955(yqkJ)
            GBE: GbCGDNIH1_2016
            SUS: Acid_2954
            BSU: BG11312(ywkA) BG11764(yqkJ) BG12614(malS) BG13922(ytsJ)
            BHA: BH0399 BH3168
            BAN: BA0579 BA1801(ykwA) BA3145 BA4848
            BAR: GBAA0579 GBAA1801(ykwA) GBAA3145 GBAA4848
            BAA: BA_1159 BA_2306 BA_5271
            BAT: BAS0548 BAS1668 BAS2923 BAS4497
            BCE: BC0580 BC1741 BC4604
            BCA: BCE_0642 BCE_1873(ykwA) BCE_4734
            BCZ: BCZK0492(sfcA) BCZK1615
            BCY: Bcer98_0499 Bcer98_3287
            BTK: BT9727_0490(sfcA) BT9727_1650
            BTL: BALH_0520(sfcA) BALH_1583(ykwA)
            BLI: BL00044(malS) BL00406(ytsJ) BL00922(mleA) BL03976(ywkA)
            BLD: BLi03071(ytsJ) BLi03139(malS) BLi03953(ywkA) BLi04137(mleA)
            BCL: ABC0918 ABC2723
            OIH: OB2176 OB3218
            GKA: GK1440 GK1534
            GTN: GTNG_1301
            SAU: SA1524
            SAV: SAV1702
            SAM: MW1645
            SAR: SAR0824 SAR1780
            SAS: SAS1629
            SAC: SACOL1749
            SAB: SAB0723 SAB1560c
            SAA: SAUSA300_1648
            SAO: SAOUHSC_01810
            SAJ: SaurJH9_1758
            SAH: SaurJH1_1792
            SEP: SE1377
            SER: SERP1265
            SHA: SH1223
            SSP: SSP1065
            LMO: lmo1915
            LMF: LMOf2365_1944(sfcA)
            LIN: lin2029
            LWE: lwe1934(malS)
            LLA: L121483(mleS) L3227(mae)
            LLM: llmg_1638(mleS)
            SPZ: M5005_Spy_0833
            SPB: M28_Spy0810
            SMU: SMU.137(mleS)
            SSA: SSA_0297(mleS)
            LPL: lp_1105(mae) lp_1118(mleS)
            LAC: LBA1075
            LSA: LSA0441(mleS)
            LSL: LSL_1313
            LBR: LVIS_2203
            LCA: LSEI_0740
            EFA: EF3316
            OOE: OEOE_0418 OEOE_1564
            STH: STH1319 STH2534
            CAC: CAC1589(malS) CAC1596(malS)
            CPE: CPE1151
            CPR: CPR_0140
            CTC: CTC00356 CTC02463
            CNO: NT01CX_2051
            CTH: Cthe_0344
            CDF: CD1005
            CBO: CBO0210
            CBE: Cbei_4008 Cbei_5075
            AMT: Amet_1304 Amet_2965 Amet_3229
            DSY: DSY1923
            DRM: Dred_2955
            CSC: Csac_2059
            TTE: TTE2332(sfcA)
            MTA: Moth_0401
            POY: PAM721(sfcA)
            AYW: AYWB_051(sfcA)
            MTU: Rv2332(mez)
            MTC: MT2394(sfcA)
            MBO: Mb2360(mez)
            MBB: BCG_2354(mez)
            MPA: MAP2540c
            MAV: MAV_1381
            MSM: MSMEG_5055
            MVA: Mvan_4481
            MGI: Mflv_2214
            MMC: Mmcs_3977
            MKM: Mkms_4051
            MJL: Mjls_3991
            NFA: nfa47090
            RHA: RHA1_ro00492 RHA1_ro02571 RHA1_ro06000 RHA1_ro08928
                 RHA1_ro11316
            SCO: SCO2951(SCE59.10c) SCO5261(2SC7G11.23)
            SMA: SAV1514(malS1) SAV2981 SAV3870(malS2) SAV5126
            ART: Arth_3432 Arth_3994
            AAU: AAur_3406 AAur_3836
            PAC: PPA0313 PPA0888
            NCA: Noca_0113 Noca_1727 Noca_2034
            TFU: Tfu_0562 Tfu_2390
            FRA: Francci3_3751
            FAL: FRAAL5985
            ACE: Acel_1647
            SEN: SACE_0563 SACE_6415
            STP: Strop_1448 Strop_3695
            RXY: Rxyl_1110
            RBA: RB307
            TDE: TDE2446
            SYN: slr0721(me)
            SYC: syc0256_c
            SYF: Synpcc7942_1297
            CYA: CYA_0662
            CYB: CYB_0613
            TEL: tll1440
            GVI: gll2149
            ANA: alr4596
            AVA: Ava_2458
            TER: Tery_3983
            SRU: SRU_1786
            CPH: Cpha266_1271
            PLT: Plut_0896
            RRS: RoseRS_2286
            RCA: Rcas_2490
            DRA: DR_2583 DR_A0276
            TMA: TM0542
            TPT: Tpet_0379
            FNO: Fnod_0471
            MAC: MA1735
            MBA: Mbar_A3045
            MMA: MM_2632
            MTP: Mthe_0409
            MHU: Mhun_0147
            TAC: Ta0456m
            TVO: TVN0768
            PTO: PTO0957
            PAB: PAB1792(mae)
            PFU: PF1026
            TKO: TK1963
            APE: APE_0392
            HBU: Hbut_0153
            SSO: SSO2869
            STO: ST0114 ST0278
            SAI: Saci_2154
            PAI: PAE1688(mae)
            PIS: Pisl_1691
            PCL: Pcal_0564
            PAS: Pars_2233
STRUCTURES  PDB: 1GZ3  1LLQ  1O0S  1PJL  1WW8  2DVM  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.38
            ExPASy - ENZYME nomenclature database: 1.1.1.38
            ExplorEnz - The Enzyme Database: 1.1.1.38
            ERGO genome analysis and discovery system: 1.1.1.38
            BRENDA, the Enzyme Database: 1.1.1.38
            CAS: 9080-52-8
///
ENTRY       EC 1.1.1.39                 Enzyme
NAME        malate dehydrogenase (decarboxylating);
            'malic' enzyme;
            pyruvic-malic carboxylase;
            NAD+-specific malic enzyme;
            NAD+-malic enzyme
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-malate:NAD+ oxidoreductase (decarboxylating)
REACTION    (S)-malate + NAD+ = pyruvate + CO2 + NADH [RN:R00214]
ALL_REAC    R00214;
            (other) R00216
SUBSTRATE   (S)-malate [CPD:C00149];
            NAD+ [CPD:C00003]
PRODUCT     pyruvate [CPD:C00022];
            CO2 [CPD:C00011];
            NADH [CPD:C00004]
COMMENT     Does not decarboxylate added oxaloacetate.
REFERENCE   1
  AUTHORS   Saz, H.J. and Hubbard, J.A.
  TITLE     The oxidative decarboxylation of malate by Ascoris lumbricoides.
  JOURNAL   J. Biol. Chem. 225 (1957) 921-933.
  ORGANISM  Ascaris lumbricoides
PATHWAY     PATH: map00620  Pyruvate metabolism
            PATH: map00710  Carbon fixation
ORTHOLOGY   KO: K00028  malate dehydrogenase (decarboxylating)
GENES       ATH: AT4G00570
            OSA: 4349051
            MLO: mlr0809
            SME: SMc00169(dme)
            ATU: Atu1652(maeB)
            ATC: AGR_C_3042
            BME: BMEI0967
            BMF: BAB1_1036
            BMS: BR1017(maeB)
            BMB: BruAb1_1022(maeB)
            BJA: blr4145(dme)
            BHE: BH07470
            BQU: BQ05320
            BBK: BARBAKC583_0622(dme)
            SIL: SPO2932
            RSP: RSP_1593
            BPU: BPUM_2635
            SPY: SPy_1110
            SPM: spyM18_1072
            SPG: SpyM3_0771
            SPS: SPs0971
            SPH: MGAS10270_Spy0949
            SPI: MGAS10750_Spy0984
            SPJ: MGAS2096_Spy0908
            SPK: MGAS9429_Spy0952
            SPA: M6_Spy0831
            SAG: SAG1919
            SAN: gbs1906
            SAK: SAK_1878
            LCA: LSEI_2866
            EFA: EF1206
STRUCTURES  PDB: 1DO8  1EFK  1EFL  1PJ2  1PJ3  1PJ4  1QR6  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.39
            ExPASy - ENZYME nomenclature database: 1.1.1.39
            ExplorEnz - The Enzyme Database: 1.1.1.39
            ERGO genome analysis and discovery system: 1.1.1.39
            BRENDA, the Enzyme Database: 1.1.1.39
            CAS: 9028-46-0
///
ENTRY       EC 1.1.1.40                 Enzyme
NAME        malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+);
            'malic' enzyme;
            pyruvic-malic carboxylase;
            malate dehydrogenase (decarboxylating, NADP+);
            NADP+-linked decarboxylating malic enzyme;
            NADP+-malic enzyme;
            NADP+-specific malic enzyme;
            NADP+-specific malate dehydrogenase;
            malate dehydrogenase (NADP+, decarboxylating);
            L-malate:NADP+ oxidoreductase;
            malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-malate:NADP+ oxidoreductase (oxaloacetate-decarboxylating)
REACTION    (S)-malate + NADP+ = pyruvate + CO2 + NADPH [RN:R00216]
ALL_REAC    R00216;
            (other) R00214
SUBSTRATE   (S)-malate [CPD:C00149];
            NADP+ [CPD:C00006]
PRODUCT     pyruvate [CPD:C00022];
            CO2 [CPD:C00011];
            NADPH [CPD:C00005]
COMMENT     Also decarboxylates added oxaloacetate.
REFERENCE   1  [PMID:13084629]
  AUTHORS   HARARY I, KOREY SR, OCHOA S.
  TITLE     Biosynthesis of dicarboxylic acids by carbon dioxide fixation. VII.
            Equilibrium of malic enzyme reaction.
  JOURNAL   J. Biol. Chem. 203 (1953) 595-604.
  ORGANISM  pigeon, Lactobacillus arabinosus
REFERENCE   2
  AUTHORS   Ochoa, S., Mehler, A.H. and Kornberg, A.
  TITLE     Biosynthesis of dicarboxylic acids by carbon dioxide fixation. I.
            Isolation and properties of an enzyme from pigeon liver catalyzing
            the reversible oxidative decarboxylation of l-malic acid.
  JOURNAL   J. Biol. Chem. 174 (1948) 979-1000.
  ORGANISM  pigeon
REFERENCE   3  [PMID:13563505]
  AUTHORS   RUTTER WJ, LARDY HA.
  TITLE     Purification and properties of pigeon liver malic enzyme.
  JOURNAL   J. Biol. Chem. 233 (1958) 374-82.
  ORGANISM  pigeon
REFERENCE   4
  AUTHORS   Strickland, R.G.
  TITLE     Some properties of the malic enzyme of pigeon liver. 1. Conversion
            of malate into pyruvate.
  JOURNAL   Biochem. J. 73 (1959) 646-654.
  ORGANISM  pigeon
REFERENCE   5
  AUTHORS   Strickland, R.G.
  TITLE     Some properties of the malic enzyme of pigeon liver. 2. Synthesis of
            malate from pyruvate.
  JOURNAL   Biochem. J. 73 (1959) 654-659.
  ORGANISM  pigeon
REFERENCE   6
  AUTHORS   Walker, D.A.
  TITLE     Physiological studies on acid metabolism. 7. Malic enzyme from
            Kalanchoe crenata: effects of carbon dioxide concentration.
  JOURNAL   Biochem. J. 74 (1960) 216-223.
  ORGANISM  Kalanchoe crenata
PATHWAY     PATH: map00620  Pyruvate metabolism
            PATH: map00710  Carbon fixation
ORTHOLOGY   KO: K00029  malate dehydrogenase
                        (oxaloacetate-decarboxylating)(NADP+)
GENES       HSA: 10873(ME3) 4199(ME1)
            PTR: 462853(ME1)
            MMU: 109264(Me3) 17436(Me1)
            RNO: 24552(Me1)
            CFA: 403709(ME1) 485151(ME3)
            BTA: 540985(LOC540985)
            GGA: 374189(ME1)
            XLA: 495390(LOC495390)
            SPU: 575178(LOC575178)
            DME: Dmel_CG10120(Men) Dmel_CG5889 Dmel_CG7964(Menl-1)
            CEL: Y48B6A.12
            ATH: AT1G79750(ATNADP-ME4) AT2G19900(ATNADP-ME1)
                 AT5G11670(ATNADP-ME2) AT5G25880(ATNADP-ME3)
            OSA: 4324717 4326552 4326769 4338007
            CME: CMJ051C
            AFM: AFUA_2G08280
            CNE: CNF03780 CNN01010
            UMA: UM02307.1
            CPV: cgd5_750
            CHO: Chro.50314
            ECO: b2463(maeB)
            ECJ: JW2447(maeB)
            ECE: Z3719
            ECS: ECs3325
            ECC: c2988
            ECI: UTI89_C2787(maeB)
            ECP: ECP_2475
            ECV: APECO1_4094
            ECW: EcE24377A_2741(maeB)
            ECX: EcHS_A2592
            STY: STY2709(maeB)
            STT: t0387(maeB)
            SPT: SPA0397(maeB)
            SEC: SC2467(maeB)
            STM: STM2472(maeB)
            YPE: YPO3034(maeB)
            YPK: y1449
            YPM: YP_2657(sfcA2)
            YPA: YPA_2222
            YPN: YPN_1351
            YPP: YPDSF_1463 YPDSF_2139
            YPS: YPTB2756(maeB)
            YPI: YpsIP31758_1277(maeB)
            SFL: SF2505
            SFX: S2656
            SFV: SFV_2507
            SSN: SSON_2543
            SBO: SBO_2478
            SDY: SDY_2645
            ECA: ECA0871(maeB)
            PLU: plu2719(maeB)
            ENT: Ent638_2958
            SPE: Spro_3472
            HIN: HI1245
            HIT: NTHI1920(mao2)
            HIQ: CGSHiGG_01795
            HDU: HD1247(maeA)
            HSO: HS_0465(mdh)
            PMU: PM0002(mdh_1)
            MSU: MS0390(sfcA)
            APL: APL_0486(maeB)
            ASU: Asuc_0669
            XFA: XF0977
            XFT: PD0272(maeB)
            XCC: XCC3345(maeB)
            XCB: XC_0821
            XCV: XCV3598(maeB)
            XAC: XAC3470(maeB)
            XOO: XOO1118(maeB)
            XOM: XOO_1015(XOO1015)
            VFI: VF2272
            PPF: Pput_4958
            PSP: PSPPH_0388(maeB)
            PEN: PSEEN0327
            PMY: Pmen_0540
            PAR: Psyc_1367(maeB)
            PCR: Pcryo_0982 Pcryo_0997
            PRW: PsycPRwf_1269
            ACI: ACIAD2287
            SDN: Sden_0736 Sden_3353
            SFR: Sfri_0833 Sfri_3757
            SAZ: Sama_0448 Sama_2621
            SBL: Sbal_0676 Sbal_3841
            SBM: Shew185_0478
            SLO: Shew_0383 Shew_2962
            SPC: Sputcn32_0554 Sputcn32_0784
            SSE: Ssed_0538
            SPL: Spea_3774
            SHE: Shewmr4_3188 Shewmr4_3492
            SHM: Shewmr7_0460 Shewmr7_0778
            SHN: Shewana3_0750
            SHW: Sputw3181_3391 Sputw3181_3618
            CPS: CPS_4881
            PHA: PSHAa1565(sfcA) PSHAa2725(maeB)
            PAT: Patl_0724 Patl_4187
            SDE: Sde_0661
            PIN: Ping_0537 Ping_1744
            MAQ: Maqu_0824
            NOC: Noc_0244 Noc_1582
            AEH: Mlg_0246
            HHA: Hhal_1029
            CSA: Csal_0605 Csal_2963
            MMW: Mmwyl1_4123
            AHA: AHA_4195
            VOK: COSY_0748(maeB)
            CVI: CV_0916(maeB)
            RSO: RSc2123(maeB1) RSc2767(maeB2)
            REU: Reut_A2441 Reut_A2847
            REH: H16_A1002(maeB)
            RME: Rmet_0878 Rmet_3046
            BMA: BMA2477(maeB1) BMA2586(maeB-2)
            BMV: BMASAVP1_A0396(maeB1) BMASAVP1_A3123(maeB-2)
            BML: BMA10299_A1256(maeB1) BMA10299_A1969(maeB-2)
            BMN: BMA10247_3309(maeB1) BMA10247_3524
            BXE: Bxe_A0283 Bxe_A0557 Bxe_A3355
            BVI: Bcep1808_0300 Bcep1808_0605 Bcep1808_3396
            BUR: Bcep18194_A3417 Bcep18194_A3713 Bcep18194_B2662
            BCN: Bcen_0148 Bcen_2788
            BCH: Bcen2424_0318 Bcen2424_0631 Bcen2424_3496
            BAM: Bamb_0237 Bamb_0532 Bamb_4462
            BPS: BPSL2959(maeB) BPSL3242
            BPM: BURPS1710b_0019(maeB-2) BURPS1710b_3474(maeB)
            BPL: BURPS1106A_3476 BURPS1106A_3849
            BPD: BURPS668_3439 BURPS668_3788
            BTE: BTH_I1189 BTH_I3110
            PNU: Pnuc_0224
            BPE: BP1064(maeB) BP1120(maeB) BP3456(maeB)
            BPA: BPP0832(maeB) BPP1160(maeB) BPP3221(maeB)
            BBR: BB0926(maeB) BB1376(maeB) BB3673(maeB)
            RFR: Rfer_0093 Rfer_1424
            POL: Bpro_1421 Bpro_4858
            PNA: Pnap_1010 Pnap_4071
            AAV: Aave_1095 Aave_4759
            AJS: Ajs_1112 Ajs_4106
            VEI: Veis_0807 Veis_1646
            MPT: Mpe_A0207
            HAR: HEAR0648
            MMS: mma_0611
            NET: Neut_0596
            EBA: ebA4043(maeB2) ebA4392(maeB1)
            AZO: azo0821(maeB1) azo3211(maeB2)
            DAR: Daro_0666 Daro_3943
            CFF: CFF8240_1560
            CHA: CHAB381_0112
            CCO: CCC13826_1940
            GSU: GSU1700(maeB)
            GME: Gmet_1637
            GUR: Gura_2073 Gura_3484
            DVU: DVU0414
            DVL: Dvul_2520
            DDE: Dde_1253 Dde_3637
            LIP: LI0351(mdh)
            BBA: Bd1833(mdh) Bd1834
            ADE: Adeh_3930
            AFW: Anae109_0502
            SFU: Sfum_2777
            RPR: RP373(tme)
            RAK: A1C_02765
            RBO: A1I_02555
            RRI: A1G_02875
            WOL: WD0488(maeB)
            WBM: Wbm0674
            AMA: AM024(maeB)
            APH: APH_0042
            ERU: Erum1200(maeB)
            ERW: ERWE_CDS_01170(tme)
            ERG: ERGA_CDS_01130(tme)
            ECN: Ecaj_0118
            ECH: ECH_0175
            NSE: NSE_0420
            PUB: SAR11_0375(maeB)
            MLO: mlr5329
            MES: Meso_4030
            PLA: Plav_3598
            SME: SMc01126(tme)
            SMD: Smed_0029 Smed_1558
            ATU: Atu3356
            ATC: AGR_L_2933
            RET: RHE_CH00389(tme) RHE_CH02355(dme)
            RLE: RL0407(maeB) RL2671(maeB)
            BME: BMEI1802 BMEI1803
            BOV: BOV_0984(maeB)
            OAN: Oant_0158 Oant_2100
            BJA: blr3726(tme)
            RPA: RPA3042(mao)
            RPB: RPB_2497
            RPC: RPC_2337
            RPD: RPD_2946
            RPE: RPE_3275
            NWI: Nwi_1587
            NHA: Nham_2110
            BHE: BH01010(maeB)
            BQU: BQ00940(maeB)
            BBK: BARBAKC583_1298
            XAU: Xaut_3143 Xaut_3937
            CCR: CC_2622 CC_3549
            SIL: SPO0012(maeB)
            SIT: TM1040_1573 TM1040_2877
            RSH: Rsph17029_0246 Rsph17029_2878
            RSQ: Rsph17025_0274 Rsph17025_2654
            JAN: Jann_0210
            RDE: RD1_0421(tme)
            PDE: Pden_0848 Pden_2224
            MMR: Mmar10_1333 Mmar10_3020
            HNE: HNE_0296(maeB)
            NAR: Saro_3291
            SAL: Sala_2792
            SWI: Swit_1904 Swit_2760
            ELI: ELI_14205
            ACR: Acry_2289
            RRU: Rru_A3542
            MAG: amb0289 amb0720
            MGM: Mmc1_0767
            SUS: Acid_4539
            BSU: BG12614(malS)
            BLI: BL00044(malS)
            BLD: BLi03139(malS)
            BPU: BPUM_2565 BPUM_3348(ywkA)
            LRE: Lreu_1532
            CAC: CAC1589(malS)
            CBO: CBO0246
            CKL: CKL_2408(maeB)
            CGL: NCgl2904(cgl3007)
            CGB: cg3335(mez)
            CEF: CE2839(malE)
            LIL: LA0181(maeB)
            LIC: LIC10160(maeB)
            BTH: BT_1969
            BFR: BF3605
            BFS: BF3408(maeB)
            PGI: PG0279(maeB)
            CHU: CHU_0027(maeB)
            GFO: GFO_0179(maeB)
            FJO: Fjoh_1651
            FPS: FP2123(maeB)
            RRS: RoseRS_3704
            RCA: Rcas_3529
            DGE: Dgeo_2154 Dgeo_2155
            TTH: TTC0144
            HAL: VNG1624G(mdh)
            HMA: rrnAC1754(maeB)
            HWA: HQ2736A(mdh)
            NPH: NP0132A(mdh_1) NP1772A(mdh_2)
            MSE: Msed_0031 Msed_1054
STRUCTURES  PDB: 1GQ2  1GZ4  2AW5  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.40
            ExPASy - ENZYME nomenclature database: 1.1.1.40
            ExplorEnz - The Enzyme Database: 1.1.1.40
            ERGO genome analysis and discovery system: 1.1.1.40
            BRENDA, the Enzyme Database: 1.1.1.40
            CAS: 9028-47-1
///
ENTRY       EC 1.1.1.41                 Enzyme
NAME        isocitrate dehydrogenase (NAD+);
            isocitric dehydrogenase;
            beta-ketoglutaric-isocitric carboxylase;
            isocitric acid dehydrogenase;
            NAD dependent isocitrate dehydrogenase;
            NAD isocitrate dehydrogenase;
            NAD-linked isocitrate dehydrogenase;
            NAD-specific isocitrate dehydrogenase;
            NAD isocitric dehydrogenase;
            isocitrate dehydrogenase (NAD);
            IDH (ambiguous);
            nicotinamide adenine dinucleotide isocitrate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     isocitrate:NAD+ oxidoreductase (decarboxylating)
REACTION    isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH [RN:R00709]
ALL_REAC    R00709
SUBSTRATE   isocitrate [CPD:C00311];
            NAD+ [CPD:C00003]
PRODUCT     2-oxoglutarate [CPD:C00026];
            CO2 [CPD:C00011];
            NADH [CPD:C00004]
COMMENT     Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.42, isocitrate
            dehydrogenase (NADP+), oxalosuccinate cannot be used as a substrate.
            In eukaryotes, isocitrate dehydrogenase exists in two forms: an
            NAD+-linked enzyme found only in mitochondria and displaying
            allosteric properties, and a non-allosteric, NADP+-linked enzyme
            that is found in both mitochondria and cytoplasm [7]. The enzyme
            from some species can also use NADP+ but much more slowly [9].
REFERENCE   1  [PMID:14063317]
  AUTHORS   HATHAWAY JA, ATKINSON DE.
  TITLE     THE EFFECT OF ADENYLIC ACID ON YEAST NICOTINAMIDE ADENINE
            DINUCLEOTIDE ISOCITRATE DEHYDROGENASE, A POSSIBLE METABOLIC CONTROL
            MECHANISM.
  JOURNAL   J. Biol. Chem. 238 (1963) 2875-81.
  ORGANISM  Acetobacter peroxydans
REFERENCE   2  [PMID:14832224]
  AUTHORS   KORNBERG A, PRICER WE Jr.
  TITLE     Di- and triphosphopyridine nucleotide isocitric dehydrogenases in
            yeast.
  JOURNAL   J. Biol. Chem. 189 (1951) 123-36.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Plaut, G.W.E.
  TITLE     Isocitrate dehydrogenases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 105-126.
REFERENCE   4  [PMID:13152105]
  AUTHORS   PLAUT GW, SUNG SC.
  TITLE     Diphosphopyridine nucleotide isocitric dehydrogenase from animal
            tissues.
  JOURNAL   J. Biol. Chem. 207 (1954) 305-14.
  ORGANISM  guinea pig
REFERENCE   5
  AUTHORS   Ramakrishnan, C.V. and Martin, S.M.
  TITLE     Isocitric dehydrogenase in Aspergillus niger.
  JOURNAL   Arch. Biochem. Biophys. 55 (1955) 403-407.
  ORGANISM  Aspergillus niger
REFERENCE   6  [PMID:13925783]
  AUTHORS   VICKERY HB.
  TITLE     A suggested new nomenclature for the isomers of isocitric acid.
  JOURNAL   J. Biol. Chem. 237 (1962) 1739-41.
REFERENCE   7  [PMID:8593959]
  AUTHORS   Camacho ML, Brown RA, Bonete MJ, Danson MJ, Hough DW.
  TITLE     Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus
            solfataricus: enzyme purification, characterisation and N-terminal
            sequence.
  JOURNAL   FEMS. Microbiol. Lett. 134 (1995) 85-90.
  ORGANISM  Haloferax volcanii, Sulfolobus solfataricus [GN:sso]
REFERENCE   8  [PMID:10601238]
  AUTHORS   Kim YO, Koh HJ, Kim SH, Jo SH, Huh JW, Jeong KS, Lee IJ, Song BJ,
            Huh TL.
  TITLE     Identification and functional characterization of a novel,
            tissue-specific NAD(+)-dependent isocitrate dehydrogenase beta
            subunit isoform.
  JOURNAL   J. Biol. Chem. 274 (1999) 36866-75.
  ORGANISM  human [GN:hsa]
REFERENCE   9  [PMID:12204383]
  AUTHORS   Inoue H, Tamura T, Ehara N, Nishito A, Nakayama Y, Maekawa M, Imada
            K, Tanaka H, Inagaki K.
  TITLE     Biochemical and molecular characterization of the NAD(+)-dependent
            isocitrate dehydrogenase from the chemolithotroph Acidithiobacillus
            thiooxidans.
  JOURNAL   FEMS. Microbiol. Lett. 214 (2002) 127-32.
  ORGANISM  Acidithiobacillus thiooxidans
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
ORTHOLOGY   KO: K00030  isocitrate dehydrogenase (NAD+)
GENES       HSA: 3419(IDH3A) 3420(IDH3B) 3421(IDH3G)
            PTR: 453565(IDH3A)
            MMU: 15929(Idh3g) 67834(Idh3a)
            RNO: 114096(Idh3a)
            CFA: 479066(IDH3A) 481081(IDH3G)
            BTA: 282446(IDH3A)
            GGA: 415362(IDH3A) 426573(RCJMB04_9n20)
            XLA: 443821(MGC79028) 444419(MGC82998) 444551(MGC83400)
            XTR: 394979(idh3a)
            DRE: 393926(idh3a)
            SPU: 578131(LOC578131) 587700(LOC587700)
            DME: Dmel_CG12233(l(1)G0156) Dmel_CG5028 Dmel_CG6439
            CEL: C30F12.7 C37E2.1 F35G12.2 F43G9.1
            ATH: AT4G35650 AT5G03290
            OSA: 4324442 4329858 4336169
            CME: CMS272C CMT412C
            SCE: YNL037C(IDH1) YOR136W(IDH2)
            AGO: AGOS_ADL223W AGOS_AFR137C
            PIC: PICST_42313(IDH2) PICST_91057(IDH1)
            CAL: CaO19.13213 CaO19_5791(CaO19.5791)
            CGR: CAGL0G02673g CAGL0I07227g
            SPO: SPAC11G7.03 SPBC902.05c
            ANI: AN1003.2 AN5790.2
            AFM: AFUA_1G12800 AFUA_6G06370
            AOR: AO090003000008 AO090012000629
            CNE: CNA04610 CNJ02060
            UMA: UM01328.1 UM01329.1
            DDI: DDB_0231288(idhA) DDB_0231294(idhB)
            TET: TTHERM_00344030
            XFA: XF2596
            XFT: PD1973(icdA)
            XCC: XCC0967(icd)
            XCB: XC_3268
            XCV: XCV1076
            XAC: XAC1046(icd)
            XOO: XOO1024(icd)
            XOM: XOO_0926(XOO0926)
            SON: SO_1538
            SDN: Sden_2561
            SFR: Sfri_2779
            SAZ: Sama_2423
            SBL: Sbal_1368
            SBM: Shew185_1354
            SLO: Shew_2760
            SPC: Sputcn32_1286
            SSE: Ssed_3318
            SPL: Spea_2980
            SHE: Shewmr4_2720
            SHM: Shewmr7_2791
            SHN: Shewana3_2890
            SHW: Sputw3181_2820
            ILO: IL0861
            CPS: CPS_3540
            PAT: Patl_3197
            MCA: MCA3071
            AEH: Mlg_0664
            CSA: Csal_1434
            ABO: ABO_0296(icd)
            REH: H16_B1016(icd3)
            BXE: Bxe_C0665
            RFR: Rfer_2380 Rfer_2411
            HAR: HEAR3270
            MMS: mma_3499
            MXA: MXAN_6337
            RAK: A1C_01920
            RBO: A1I_06360
            RCM: A1E_01530
            RRI: A1G_02020
            WOL: WD0791
            AMA: AM1131(icd)
            APH: APH_1166
            NSE: NSE_0172
            ACR: Acry_2029
            ABA: Acid345_4042
            SUS: Acid_2824 Acid_7350
            CAC: CAC0972(citC)
            CNO: NT01CX_0139
            AMT: Amet_1319
            CSC: Csac_0751
            MTA: Moth_0993
            RXY: Rxyl_1297
            LIL: LA4067(icd1)
            CYA: CYA_1467
            CYB: CYB_1678
            TEL: tlr0302
            GVI: gll3088(icd)
            SRU: SRU_1677
            DET: DET0450
            DEH: cbdb_A408
            DEB: DehaBAV1_0427
            MBU: Mbur_1073
            MTP: Mthe_0549
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.41
            ExPASy - ENZYME nomenclature database: 1.1.1.41
            ExplorEnz - The Enzyme Database: 1.1.1.41
            ERGO genome analysis and discovery system: 1.1.1.41
            BRENDA, the Enzyme Database: 1.1.1.41
            CAS: 9001-58-5
///
ENTRY       EC 1.1.1.42                 Enzyme
NAME        isocitrate dehydrogenase (NADP+);
            oxalosuccinate decarboxylase;
            oxalsuccinic decarboxylase;
            isocitrate (NADP) dehydrogenase;
            isocitrate (nicotinamide adenine dinucleotide phosphate)
            dehydrogenase;
            NADP-specific isocitrate dehydrogenase;
            NADP-linked isocitrate dehydrogenase;
            NADP-dependent isocitrate dehydrogenase;
            NADP isocitric dehydrogenase;
            isocitrate dehydrogenase (NADP-dependent);
            NADP-dependent isocitric dehydrogenase;
            triphosphopyridine nucleotide-linked isocitrate
            dehydrogenase-oxalosuccinate carboxylase;
            NADP+-linked isocitrate dehydrogenase;
            IDH (ambiguous);
            dual-cofactor-specific isocitrate dehydrogenase;
            NADP+-ICDH;
            NADP+-IDH;
            IDP;
            IDP1;
            IDP2;
            IDP3
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     isocitrate:NADP+ oxidoreductase (decarboxylating)
REACTION    (1) isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH [RN:R00267];
            (2) oxalosuccinate + NADP+ = 2-oxoglutarate + CO2 + NADPH
            [RN:R00268]
ALL_REAC    R00267 R00268;
            (other) R01899
SUBSTRATE   isocitrate [CPD:C00311];
            NADP+ [CPD:C00006];
            oxalosuccinate [CPD:C05379]
PRODUCT     2-oxoglutarate [CPD:C00026];
            CO2 [CPD:C00011];
            NADPH [CPD:C00005]
COMMENT     Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.41, isocitrate
            dehydrogenase (NAD+), oxalosuccinate can be used as a substrate. In
            eukaryotes, isocitrate dehydrogenase exists in two forms: an
            NAD+-linked enzyme found only in mitochondria and displaying
            allosteric properties, and a non-allosteric, NADP+-linked enzyme
            that is found in both mitochondria and cytoplasm [6]. The enzyme
            from some species can also use NAD+ but much more slowly [6,7].
REFERENCE   1  [PMID:13363868]
  AUTHORS   AGOSIN M, WEINBACH EC.
  TITLE     Partial purification and characterization of the isocitric
            dehydrogenase from Trypanosoma cruzi.
  JOURNAL   Biochim. Biophys. Acta. 21 (1956) 117-26.
  ORGANISM  Trypanosoma cruzi [GN:tcr]
REFERENCE   2  [PMID:13355848]
  AUTHORS   DIXON M, MOYLE J.
  TITLE     Purification of the isocitric enzyme (triphosphopyridine
            nucleotide-linked isocitric dehydrogenase-oxalosuccinic
            carboxylase).
  JOURNAL   Biochem. J. 63 (1956) 548-52.
  ORGANISM  pig [GN:ssc]
REFERENCE   3
  AUTHORS   Plaut, G.W.E.
  TITLE     Isocitrate dehydrogenases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 105-126.
REFERENCE   4  [PMID:13438885]
  AUTHORS   SIEBERT G, DUBUC J, WARNER RC, PLAUT GW.
  TITLE     The preparation of isocitric dehydrogenase from mammalian heart.
  JOURNAL   J. Biol. Chem. 226 (1957) 965-75.
  ORGANISM  pig [GN:ssc]
REFERENCE   5  [PMID:13925783]
  AUTHORS   VICKERY HB.
  TITLE     A suggested new nomenclature for the isomers of isocitric acid.
  JOURNAL   J. Biol. Chem. 237 (1962) 1739-41.
REFERENCE   6  [PMID:8593959]
  AUTHORS   Camacho ML, Brown RA, Bonete MJ, Danson MJ, Hough DW.
  TITLE     Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus
            solfataricus: enzyme purification, characterisation and N-terminal
            sequence.
  JOURNAL   FEMS. Microbiol. Lett. 134 (1995) 85-90.
  ORGANISM  Haloferax volcanii, Sulfolobus solfataricus [GN:sso]
REFERENCE   7  [PMID:9325430]
  AUTHORS   Steen IH, Lien T, Birkeland NK.
  TITLE     Biochemical and phylogenetic characterization of isocitrate
            dehydrogenase from a hyperthermophilic archaeon, Archaeoglobus
            fulgidus.
  JOURNAL   Arch. Microbiol. 168 (1997) 412-20.
  ORGANISM  Archaeoglobus fulgidus [GN:afu]
REFERENCE   8  [PMID:15254034]
  AUTHORS   Koh HJ, Lee SM, Son BG, Lee SH, Ryoo ZY, Chang KT, Park JW, Park DC,
            Song BJ, Veech RL, Song H, Huh TL.
  TITLE     Cytosolic NADP+-dependent isocitrate dehydrogenase plays a key role
            in lipid metabolism.
  JOURNAL   J. Biol. Chem. 279 (2004) 39968-74.
  ORGANISM  rat [GN:rno]
REFERENCE   9  [PMID:12207025]
  AUTHORS   Ceccarelli C, Grodsky NB, Ariyaratne N, Colman RF, Bahnson BJ.
  TITLE     Crystal structure of porcine mitochondrial NADP+-dependent
            isocitrate dehydrogenase complexed with Mn2+ and isocitrate.
            Insights into the enzyme mechanism.
  JOURNAL   J. Biol. Chem. 277 (2002) 43454-62.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00480  Glutathione metabolism
            PATH: map00720  Reductive carboxylate cycle (CO2 fixation)
ORTHOLOGY   KO: K00031  isocitrate dehydrogenase
GENES       HSA: 3417(IDH1) 3418(IDH2)
            MMU: 15926(Idh1) 269951(Idh2)
            RNO: 24479(Idh1)
            CFA: 479043(IDH2)
            BTA: 281235(IDH1) 327669(IDH2)
            GGA: 424112(IDH1) 431056(RCJMB04_7e11)
            XLA: 380013(MGC64442) 494713(LOC494713)
            XTR: 448026(MGC69505)
            DRE: 378971(idh1)
            SPU: 580429(LOC580429) 581147(LOC581147)
            DME: Dmel_CG7176(Idh)
            CEL: C34F6.8 F59B8.2
            ATH: AT1G54340(ICDH) AT1G65930 AT5G14590
            OSA: 4324176 4327213 4336353 4339674
            CME: CMT216C
            SCE: YDL066W(IDP1) YLR174W(IDP2) YNL009W(IDP3)
            AGO: AGOS_AAL022W AGOS_AER061C
            PIC: PICST_43870(IDP2) PICST_50442(LYS12) PICST_72104(IDP1)
            CGR: CAGL0B04917g CAGL0D00770g CAGL0H03663g
            SPO: SPAC6G10.08
            ANI: AN2999.2
            AFM: AFUA_3G08660
            AOR: AO090005001404
            ANG: An02g12430(icdA)
            CNE: CNB04090
            UMA: UM06111.1
            DDI: DDB_0231401(idhC) DDB_0231402(idhM)
            PFA: PF13_0242
            TAN: TA10850
            TPV: TP04_0620
            TET: TTHERM_00196200 TTHERM_00794110
            TBR: Tb11.03.0230 Tb927.8.3690
            TCR: 506925.319 511575.60
            LMA: LmjF10.0290 LmjF33.2550
            ECO: b1136(icdA)
            ECJ: JW1122(icd)
            ECE: Z1865(icdA)
            ECS: ECs1608
            ECC: c1517(icdA)
            ECI: UTI89_C1266(icdA)
            ECP: ECP_1131
            ECV: APECO1_218
            ECW: EcE24377A_1299(icd)
            ECX: EcHS_A1256
            STY: STY1278(icdA)
            STT: t1682(icdA)
            SPT: SPA1612(icdA)
            SEC: SC1189(icdA)
            STM: STM1238(icdA)
            YPE: YPO1641(icdA)
            YPK: y1802(icdA)
            YPM: YP_1771(icdA)
            YPA: YPA_1883
            YPN: YPN_1990
            YPS: YPTB2427(icdA)
            YPI: YpsIP31758_1615(icd)
            SFL: SF1155(icdA)
            SFX: S1238(icdA)
            SFV: SFV_1171(icdA)
            SSN: SSON_1154(icdA)
            SBO: SBO_1903(icdA)
            SDY: SDY_2016(icdA)
            ECA: ECA2439(icd)
            PLU: plu2801(icd)
            SGL: SG0700
            HSO: HS_1641(icd)
            PMU: PM1606(idp)
            MSU: MS2370(icd)
            XFA: XF2700
            XFT: PD2056(icd)
            XCC: XCC3782(icd)
            XCB: XC_3854
            XCV: XCV3960(icd)
            XAC: XAC3835(icd)
            XOO: XOO4167(icd)
            XOM: XOO_3943(XOO3943)
            VCH: VC1141
            VCO: VC0395_A0711(icd)
            VVU: VV1_2118
            VVY: VV2325
            VPA: VP1011
            VFI: VF1775
            PPR: PBPRA1149
            PAE: PA2623(icd) PA2624(idh)
            PAU: PA14_30180(idh) PA14_30190(icd)
            PAP: PSPA7_2583 PSPA7_2584(icd)
            PPU: PP_4011(icd) PP_4012
            PPF: Pput_1821
            PST: PSPTO_3356
            PSB: Psyr_3186
            PSP: PSPPH_3100
            PFL: PFL_3888(icd) PFL_3889
            PFO: Pfl_3593 Pfl_3594
            PEN: PSEEN2202(idh) PSEEN2204(icd)
            PMY: Pmen_2397
            PAR: Psyc_0287(icd2)
            PCR: Pcryo_0314 Pcryo_0315
            PRW: PsycPRwf_2086 PsycPRwf_2087
            ACI: ACIAD1187(idh) ACIAD1190(icd)
            SON: SO_2629(icd)
            SDN: Sden_1831
            SFR: Sfri_2257
            SAZ: Sama_2059
            SBL: Sbal_2475
            SBM: Shew185_2468
            SLO: Shew_1563
            SPC: Sputcn32_2230
            SSE: Ssed_1883
            SPL: Spea_2535
            SHE: Shewmr4_1606
            SHM: Shewmr7_1681
            SHN: Shewana3_1750 Shewana3_2424
            SHW: Sputw3181_1779
            ILO: IL1433
            CPS: CPS_1354 CPS_2896(icd) CPS_2897
            PHA: PSHAa1303(icd) PSHAa1727
            PAT: Patl_2377
            SDE: Sde_1684
            PIN: Ping_0983
            MAQ: Maqu_0090
            CBU: CBU_1200(icd)
            CBD: COXBU7E912_1288(icd)
            LPN: lpg0816(icd)
            LPF: lpl0849(icd)
            LPP: lpp0878(icd)
            FTU: FTT1526c(idh)
            FTF: FTF1526c(idh)
            FTW: FTW_0405(icd)
            FTL: FTL_0588
            FTH: FTH_0588
            FTA: FTA_0622
            FTN: FTN_1434(icd)
            TCX: Tcr_1101
            NOC: Noc_1378
            AEH: Mlg_1121
            HHA: Hhal_2290
            HCH: HCH_02336(icd) HCH_03212
            CSA: Csal_0525
            ABO: ABO_1281(icd) ABO_1282(icdA)
            MMW: Mmwyl1_3267
            AHA: AHA_1436(icd)
            VOK: COSY_0392(icd)
            NME: NMB0920
            NMA: NMA1116(icd)
            NMC: NMC0897(icd)
            NGO: NGO1082
            CVI: CV_3664
            RSO: RSc2490(icd)
            REU: Reut_A2756 Reut_B4201
            REH: H16_A3056(icd1) H16_B1931(icd2)
            RME: Rmet_2895 Rmet_3729
            BMA: BMA0486(icd)
            BMV: BMASAVP1_A0683(icd)
            BML: BMA10299_A1015(icd)
            BMN: BMA10247_0132(icd)
            BXE: Bxe_A0797 Bxe_B0532
            BVI: Bcep1808_2601
            BUR: Bcep18194_A5855 Bcep18194_A5856
            BCN: Bcen_1912 Bcen_1913
            BCH: Bcen2424_2523 Bcen2424_2524
            BAM: Bamb_2571 Bamb_2572
            BPS: BPSL0896(icd)
            BPM: BURPS1710b_1108(icd)
            BPL: BURPS1106A_0960(icd)
            BPD: BURPS668_0956(icd)
            BTE: BTH_I0759(icd)
            PNU: Pnuc_0366
            BPE: BP2488(icd)
            BPA: BPP3475(icd)
            BBR: BB3924(icd)
            RFR: Rfer_2761
            POL: Bpro_2942
            PNA: Pnap_3680
            AJS: Ajs_2300
            VEI: Veis_0624
            MPT: Mpe_A2468
            HAR: HEAR3467(idh)
            MMS: mma_3692
            NEU: NE1730(icd)
            NET: Neut_2045
            NMU: Nmul_A2245
            EBA: ebA829(icd) ebA832(icd2)
            AZO: azo1146(icd2) azo1147(icd1)
            DAR: Daro_3119 Daro_3120
            TBD: Tbd_0854
            MFA: Mfla_2139
            HPY: HP0027(icd)
            HPA: HPAG1_0025
            HHE: HH1196
            HAC: Hac_0041(icdA)
            WSU: WS1454
            TDN: Tmden_1047
            CJE: Cj0531(icd)
            CJR: CJE0635(icd)
            CJJ: CJJ81176_0556(icd)
            CJU: C8J_0492(icd)
            CJD: JJD26997_1399(icd)
            CFF: CFF8240_0913
            CHA: CHAB381_1135
            CCO: CCC13826_1088
            ABU: Abu_1314(icd)
            NIS: NIS_0834
            SUN: SUN_0570
            GSU: GSU1465(icd)
            GME: Gmet_1359
            GUR: Gura_2194
            PCA: Pcar_1038
            DVU: DVU0477(icd)
            DDE: Dde_3476
            BBA: Bd3723(icdA)
            ADE: Adeh_1625 Adeh_2227
            AFW: Anae109_1588
            MXA: MXAN_3537(icd)
            SAT: SYN_01410
            SFU: Sfum_3896
            RPR: RP265
            RTY: RT0256(icd)
            RCO: RC0353(icd)
            RFE: RF_1015(icd)
            RBE: RBE_0289(icd)
            WBM: Wbm0367(leuB)
            ERU: Erum8530(icd)
            ERW: ERWE_CDS_09040(icd)
            ECN: Ecaj_0890
            ECH: ECH_1114
            PUB: SAR11_0644(icdA)
            MLO: mll0036
            MES: Meso_1267
            PLA: Plav_2580
            SME: SMc00480(icd)
            SMD: Smed_1519
            ATU: Atu1870(icdA)
            ATC: AGR_C_3429
            RLE: RL2631(icd)
            BME: BMEI0791
            BMF: BAB1_1221
            BMS: BR1199
            BMB: BruAb1_1204
            BOV: BOV_1161
            OAN: Oant_1992
            BJA: blr5747(icdA)
            BRA: BRADO2759(icd)
            BBT: BBta_5427(icd)
            RPA: RPA3834(idh)
            RPB: RPB_3732
            RPC: RPC_1576
            RPD: RPD_1737
            RPE: RPE_1602
            NWI: Nwi_1294
            NHA: Nham_1623
            BHE: BH10050(icdA)
            BQU: BQ07780(icdA)
            BBK: BARBAKC583_0743
            XAU: Xaut_4569
            CCR: CC_2522
            SIL: SPOA0315(icd)
            SIT: TM1040_0477
            RSP: RSP_0446 RSP_1559(icd)
            RSH: Rsph17029_0210 Rsph17029_2099
            RSQ: Rsph17025_2367 Rsph17025_3039
            JAN: Jann_2371 Jann_2372
            RDE: RD1_2204(icd) RD1_2704(icd)
            PDE: Pden_2961
            MMR: Mmar10_1011
            HNE: HNE_1177
            ZMO: ZMO0544(citC)
            NAR: Saro_1282
            SAL: Sala_1964
            SWI: Swit_0457
            ELI: ELI_07700
            GOX: GOX1336
            GBE: GbCGDNIH1_1366 GbCGDNIH1_2050
            ACR: Acry_0565
            RRU: Rru_A0356
            MAG: amb0607 amb0608
            MGM: Mmc1_1603
            ABA: Acid345_1950
            BSU: BG10856(citC)
            BHA: BH3159(citC)
            BAN: BA4838(citC)
            BAR: GBAA4838(citC)
            BAA: BA_5261
            BAT: BAS4487
            BCE: BC4593
            BCA: BCE_4724(citC)
            BCZ: BCZK4334(citC)
            BTK: BT9727_4322(citC)
            BTL: BALH_4177(citC)
            BLI: BL00398(icd)
            BLD: BLi03061(icd)
            BCL: ABC2714(citC)
            BAY: RBAM_026170
            BPU: BPUM_2555
            OIH: OB2167(citC)
            GKA: GK2735
            SAU: SA1517(citC)
            SAV: SAV1694(citC)
            SAM: MW1638(citC)
            SAR: SAR1773(citC)
            SAS: SAS1622
            SAC: SACOL1741(icd)
            SAB: SAB1553c(citC)
            SAA: SAUSA300_1640(icd)
            SAO: SAOUHSC_01801
            SAJ: SaurJH9_1751
            SAH: SaurJH1_1785
            SEP: SE1370
            SER: SERP1257(icd)
            SHA: SH1231(citC)
            SSP: SSP1072
            LMO: lmo1566(citC)
            LMF: LMOf2365_1588(icd)
            LIN: lin1601(citC)
            LWE: lwe1579(citC)
            LLA: L71075(icd)
            LLC: LACR_0699
            LLM: llmg_0637(icd)
            SMU: SMU.672(idh)
            STC: str1266(icd)
            STL: stu1266(icd)
            SSA: SSA_0704
            SGO: SGO_1611(icd)
            STH: STH2544
            CTH: Cthe_0285
            CBE: Cbei_4199
            CKL: CKL_0546(idh)
            DSY: DSY3882
            DRM: Dred_3254
            TTE: TTE0387(icd)
            MTU: Rv0066c Rv3339c(icd1)
            MTC: MT0072(icd-1) MT3442(icd-2)
            MBO: Mb0067c(icd2) Mb3371c(icd1)
            MBB: BCG_0097c(icd2) BCG_3409c(icd1)
            MLE: ML2672(icd2)
            MPA: MAP3455c(icd1) MAP3456c(icd2)
            MAV: MAV_4311 MAV_4313 MAV_5105
            MSM: MSMEG_1654
            MVA: Mvan_3212
            MGI: Mflv_3455
            MMC: Mmcs_1209
            MKM: Mkms_1226
            MJL: Mjls_1236
            CGL: NCgl0634(cgl0664)
            CGB: cg0766(icd)
            CEF: CE0682(icd)
            CDI: DIP0631(icd)
            CJK: jk1693(icd)
            NFA: nfa9230
            RHA: RHA1_ro00618 RHA1_ro06238
            SCO: SCO7000(idh)
            SMA: SAV7214(icdA)
            LXX: Lxx19490(icd)
            CMI: CMM_2537(icdA)
            ART: Arth_1092
            AAU: AAur_1201
            PAC: PPA1738
            NCA: Noca_3575
            TFU: Tfu_2568
            FRA: Francci3_2203
            FAL: FRAAL3297(icd)
            ACE: Acel_0388
            KRA: Krad_3988
            SEN: SACE_6636(icd-2)
            STP: Strop_3793
            BLO: BL1499(icd1)
            BAD: BAD_0776(icd1)
            RBA: RB1593(icd)
            PCU: pc1783(icd)
            LIL: LA4171(icd2)
            LIC: LIC13328
            LBJ: LBJ_2800(leuB-2)
            LBL: LBL_0271(leuB-2)
            SYN: slr1289(icd)
            SYW: SYNW0166(icd)
            SYC: syc2372_d(icd)
            SYF: Synpcc7942_1719
            SYD: Syncc9605_0161
            SYE: Syncc9902_0191
            SYG: sync_0214(icd)
            SYR: SynRCC307_0153(icd)
            SYX: SynWH7803_0217(icd)
            GVI: gll3998
            ANA: alr1827(icd)
            AVA: Ava_4831
            PMA: Pro1752(icd)
            PMM: PMM1596(icd)
            PMT: PMT1935(icd)
            PMN: PMN2A_1170
            PMI: PMT9312_1688
            PMB: A9601_18051(icd)
            PMC: P9515_17831(icd)
            PMF: P9303_25761(icd)
            PMG: P9301_17881(icd)
            PMH: P9215_18691
            PME: NATL1_20451(icd)
            TER: Tery_0071
            BTH: BT_2071
            BFR: BF3754
            BFS: BF3542(icd)
            SRU: SRU_1973(icd)
            CHU: CHU_1228(icd)
            GFO: GFO_0618(icd)
            FJO: Fjoh_2181
            FPS: FP1872(icd)
            CTE: CT0351(icd)
            CCH: Cag_1410
            CPH: Cpha266_0680
            PVI: Cvib_0507
            PLT: Plut_0459
            DRA: DR_1540
            DGE: Dgeo_1166
            TTH: TTC1172
            TTJ: TTHA1535
            AAE: aq_1512(icd)
            TMA: TM1148
            TPT: Tpet_1602
            MAC: MA4265
            MBA: Mbar_A0623
            MMA: MM_0642 MM_1003
            AFU: AF0647(icd)
            HAL: VNG1873G(icd)
            HMA: rrnAC3419(icd)
            HWA: HQ3212A(icd)
            NPH: NP2430A(icd)
            TAC: Ta0117
            TVO: TVN0195
            PTO: PTO0168 PTO0426
            PFU: PF0202
            RCI: RCIX1801(icd)
            APE: APE_0689.1
            IHO: Igni_1064
            SSO: SSO2182(idh)
            STO: ST2166
            SAI: Saci_2375(icd)
            PAI: PAE1651
STRUCTURES  PDB: 1AI2  1AI3  1BL5  1CW1  1CW4  1CW7  1GRO  1GRP  1HJ6  1HQS  
                 1IDC  1IDD  1IDE  1IDF  1IKA  1ISO  1ITW  1J1W  1LWD  1P8F  
                 1PB1  1PB3  1SJS  1T09  1T0L  1TYO  1V94  1XGV  1XKD  1ZOR  
                 2B0T  2CMV  2D1C  2DHT  2IV0  3ICD  4ICD  5ICD  6ICD  7ICD  
                 8ICD  9ICD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.42
            ExPASy - ENZYME nomenclature database: 1.1.1.42
            ExplorEnz - The Enzyme Database: 1.1.1.42
            ERGO genome analysis and discovery system: 1.1.1.42
            BRENDA, the Enzyme Database: 1.1.1.42
            CAS: 9028-48-2
///
ENTRY       EC 1.1.1.43                 Enzyme
NAME        phosphogluconate 2-dehydrogenase;
            6-phosphogluconic dehydrogenase;
            phosphogluconate dehydrogenase;
            gluconate 6-phosphate dehydrogenase;
            6-phosphogluconate dehydrogenase (NAD+);
            2-keto-6-phosphogluconate reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     6-phospho-D-gluconate:NAD(P)+ 2-oxidoreductase
REACTION    6-phospho-D-gluconate + NAD(P)+ = 6-phospho-2-dehydro-D-gluconate +
            NAD(P)H + H+ [RN:R02032 R02034]
ALL_REAC    R02032 R02034
SUBSTRATE   6-phospho-D-gluconate [CPD:C00345];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     6-phospho-2-dehydro-D-gluconate [CPD:C01218];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13894458]
  AUTHORS   FRAMPTON EW, WOOD WA.
  TITLE     Carbohydrate oxidation by Pseudomonas fluorescens VI. Conversion of
            2-keto-6-phosphogluconate to pyruvate.
  JOURNAL   J. Biol. Chem. 236 (1961) 2571-7.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00030  Pentose phosphate pathway
            PATH: map00480  Glutathione metabolism
ORTHOLOGY   KO: K00032  phosphogluconate 2-dehydrogenase
GENES       REH: H16_B1813(kguD)
            BAY: RBAM_022170(yqjI)
            BPU: BPUM_2124(yqjI)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.43
            ExPASy - ENZYME nomenclature database: 1.1.1.43
            ExplorEnz - The Enzyme Database: 1.1.1.43
            ERGO genome analysis and discovery system: 1.1.1.43
            BRENDA, the Enzyme Database: 1.1.1.43
            CAS: 9001-82-5
///
ENTRY       EC 1.1.1.44                 Enzyme
NAME        phosphogluconate dehydrogenase (decarboxylating);
            phosphogluconic acid dehydrogenase;
            6-phosphogluconic dehydrogenase;
            6-phosphogluconic carboxylase;
            6-phosphogluconate dehydrogenase (decarboxylating);
            6-phospho-D-gluconate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     6-phospho-D-gluconate:NADP+ 2-oxidoreductase (decarboxylating)
REACTION    6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH
            [RN:R01528]
ALL_REAC    R01528
SUBSTRATE   6-phospho-D-gluconate [CPD:C00345];
            NADP+ [CPD:C00006]
PRODUCT     D-ribulose 5-phosphate [CPD:C00199];
            CO2 [CPD:C00011];
            NADPH [CPD:C00005]
COFACTOR    Manganese [CPD:C00034]
COMMENT     Certain preparations reduce NAD+ as well as NADP+.
REFERENCE   1  [PMID:14904376]
  AUTHORS   DICKENS F, GLOCK GE.
  TITLE     Direct oxidation of glucose-6-phosphate, 6-phosphogluconate and
            pentose-5-phosphates by enzymes of animal origin.
  JOURNAL   Biochem. J. 50 (1951) 81-95.
  ORGANISM  rat [GN:rno], rabbit
REFERENCE   2
  AUTHORS   Pontremoli, S., de Flora, A., Grazi, E., Mangiarotti, G.,
            Bonsignore, A. and Horecker, B.L.
  TITLE     Purification and properties of beta-L-hydroxy acid dehydrogenase.
            II. Isolation of beta-keto-L-gluconic acid, an intermediate in
            L-xylulose biosynthesis.
  JOURNAL   J. Biol. Chem. 236 (1961) 2975-2980.
  ORGANISM  Candida utilis
REFERENCE   3
  AUTHORS   Scott, D.B.M. and Cohen, S.S.
  TITLE     The oxidative pathway of carbohydrate metabolism in Escherichia
            coli. 1. The isolation and properties of glucose 6-phosphate
            dehydrogenase and 6-phosphogluconate dehydrogenase.
  JOURNAL   Biochem. J. 55 (1953) 23-33.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4
  AUTHORS   Scott, D.B.M. and Cohen, S.S.
  TITLE     The oxidative pathway of carbohydrate metabolism in Escherichia
            coli. 5. Isolation and identification of ribulose phosphate produced
            from 6-phosphogluconate by the dehydrogenase of E. coli.
  JOURNAL   Biochem. J. 65 (1957) 686-689.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00030  Pentose phosphate pathway
ORTHOLOGY   KO: K00033  6-phosphogluconate dehydrogenase
GENES       HSA: 5226(PGD)
            MMU: 110208(Pgd)
            CFA: 478236(PGD)
            GGA: 419450(PGD)
            XLA: 398848(MGC68486)
            SPU: 583873(LOC583873)
            DME: Dmel_CG3724(Pgd)
            CEL: T25B9.9
            ATH: AT1G64190
            OSA: 4339892
            CME: CML036C CML059C CMM231C CMS195C CMX012C
            SCE: YGR256W(GND2) YHR183W(GND1)
            AGO: AGOS_AFR129W
            PIC: PICST_69500(GND1)
            CGR: CAGL0M13343g
            SPO: SPBC660.16
            ANI: AN3954.2
            AFM: AFUA_6G08050 AFUA_6G08730
            AOR: AO090003000121
            CNE: CNK01050
            UMA: UM02577.1
            ECU: ECU05_0860
            DDI: DDB_0215011(gnd)
            PFA: PF14_0520
            TAN: TA19350
            TPV: TP01_0193
            TBR: Tb09.211.3180
            TCR: 507011.269 510663.70
            LMA: LmjF35.3340
            ECO: b2029(gnd)
            ECJ: JW2011(gnd)
            ECE: Z3191(gnd)
            ECS: ECs2830
            ECC: c2556(gnd)
            ECI: UTI89_C2302(gnd)
            ECP: ECP_2072
            ECV: APECO1_1126(gnd)
            ECW: EcE24377A_2320(gnd)
            ECX: EcHS_A2183(gnd)
            STY: STY2290(gnd)
            STT: t0792(gnd)
            SPT: SPA0790(gnd)
            SEC: SC2091(gnd)
            STM: STM2081(gnd)
            YPE: YPO1541(gnd)
            YPK: y2629(gnd)
            YPM: YP_1430(gnd)
            YPA: YPA_0836
            YPN: YPN_2439
            YPS: YPTB1553(gnd)
            YPI: YpsIP31758_2436(gnd)
            SFL: SF2091(gnd)
            SFX: S2212(gnd)
            SFV: SFV_2089(gnd)
            SSN: SSON_2100(gnd)
            SBO: SBO_0858(gnd)
            SDY: SDY_2212(gnd)
            ECA: ECA1444(gnd)
            PLU: plu1560(gnd)
            BUC: BU107(gnd)
            BAS: BUsg100(gnd)
            BAB: bbp101(gnd)
            BCC: BCc_071(gnsD)
            SGL: SG1122
            ENT: Ent638_2642
            SPE: Spro_1608
            BFL: Bfl470(gnd)
            BPN: BPEN_485(gnd)
            HIT: NTHI0681(gnd)
            HIP: CGSHiEE_00215
            HIQ: CGSHiGG_06060
            HDU: HD0833(gnd)
            HSO: HS_1654(gnd)
            PMU: PM1554(gnd)
            MSU: MS0013(gnd)
            APL: APL_1305(gnd)
            ASU: Asuc_0232
            XCC: XCC3439(gndA)
            XCB: XC_0725
            XCV: XCV0741(gndA)
            XAC: XAC0680(gndA)
            XOO: XOO3939(gndA)
            XOM: XOO_3717(XOO3717)
            VCH: VCA0898
            VCO: VC0395_0339(gnd)
            VVU: VV1_2682
            VVY: VV1607
            VPA: VP1708
            VFI: VFA0470
            PPR: PBPRA1444(gnd)
            PPU: PP_4043(gnd)
            PST: PSPTO_3122(gnd)
            PSB: Psyr_2989
            PSP: PSPPH_2251
            PFL: PFL_3144
            PFO: Pfl_2586
            PEN: PSEEN1939(gnd)
            SON: SO_1902(gnd)
            SDN: Sden_1935
            SFR: Sfri_2724
            SAZ: Sama_1365
            SBL: Sbal_2824
            SBM: Shew185_2842
            SLO: Shew_2561
            SPC: Sputcn32_1723
            SSE: Ssed_1461
            SPL: Spea_2794
            SHE: Shewmr4_1609
            SHM: Shewmr7_1684
            SHN: Shewana3_1677
            SHW: Sputw3181_2302
            CPS: CPS_2341(gnd)
            PHA: PSHAa1407
            PAT: Patl_2110
            SDE: Sde_0635
            PIN: Ping_2752 Ping_2937
            MCA: MCA1950(gnd)
            TCX: Tcr_1215
            NOC: Noc_2061
            CSA: Csal_0666
            DNO: DNO_1236(gnd)
            BCI: BCI_0397(gnd)
            CRP: CRP_039
            NME: NMB0015
            NMA: NMA0262(gnd)
            NMC: NMC2153(gnd)
            NGO: NGO1914
            BMA: BMAA0420(gnd)
            BML: BMA10299_1798(gnd)
            BMN: BMA10247_A0469(gnd)
            BXE: Bxe_B1341 Bxe_B2210
            BVI: Bcep1808_4384
            BUR: Bcep18194_B2181
            BCN: Bcen_4459
            BCH: Bcen2424_3907
            BAM: Bamb_3285
            BPS: BPSS1749(gnd)
            BPM: BURPS1710b_A0828(gnd)
            BPL: BURPS1106A_A2376(gnd)
            BPD: BURPS668_A2515(gnd)
            BTE: BTH_II0631(gnd)
            RFR: Rfer_4033
            PNA: Pnap_4501
            NEU: NE0397
            NET: Neut_2144 Neut_2432
            NMU: Nmul_A1623
            DAR: Daro_2069
            TBD: Tbd_2123
            MFA: Mfla_0918 Mfla_1062 Mfla_2599
            GME: Gmet_2620
            PCA: Pcar_0925
            DDE: Dde_3470
            ADE: Adeh_1438
            MXA: MXAN_0951(gnd)
            PUB: SAR11_0778(gnd)
            MLO: mll3321 mlr4206
            MES: Meso_3946
            SME: SMc04262(gnd)
            ATU: Atu1526(gnd) Atu4834
            ATC: AGR_C_2814 AGR_L_99
            RET: RHE_CH02468(gnd) RHE_CH03488(ypch01234)
            RLE: RL2807(gnd) RL3998(gntZ)
            BME: BMEII1124
            BMF: BAB2_0109(gnd)
            BMS: BRA0111(gnd)
            BMB: BruAb2_0109(gnd)
            BOV: BOV_A0101(gnd)
            BJA: blr6759
            BRA: BRADO5810
            BBT: BBta_6316 BBta_p0095
            RPA: RPA3635(gnd)
            RPB: RPB_1891
            RPC: RPC_3671
            RPD: RPD_3475
            RPE: RPE_3709
            NWI: Nwi_2642
            NHA: Nham_3270
            JAN: Jann_3252
            PDE: Pden_2393
            SAL: Sala_0114
            GOX: GOX1705
            GBE: GbCGDNIH1_0854
            ABA: Acid345_2811
            SUS: Acid_1206 Acid_7082
            BSU: BG10651(gntZ) BG11631(yqeC) BG11738(yqjI)
            BHA: BH2674
            BAN: BA0164(yqjI) BA3431
            BAR: GBAA0164(yqjI) GBAA3431
            BAA: BA_0746 BA_3929
            BAT: BAS0166 BAS3180
            BCE: BC2225 BC3372
            BCA: BCE_2304(gnd) BCE_3410
            BCZ: BCZK0157(gnd) BCZK3081(gnd)
            BTK: BT9727_0159(gntZ) BT9727_3164(gnd)
            BTL: BALH_0162(gntZ)
            BLI: BL00198(gntZ) BL01383(yqjI)
            BLD: BLi02567(yqjI) BLi04289(gntZ)
            BCL: ABC1926
            OIH: OB0185 OB3187(gntZ)
            GKA: GK2344
            SAU: SA1342(gnd)
            SAV: SAV1511(gnd)
            SAM: MW1464(gnd)
            SAR: SAR1589(gnd)
            SAS: SAS1450
            SAC: SACOL1554(gnd)
            SAB: SAB1384c(gnd)
            SAA: SAUSA300_1459(gnd)
            SAO: SAOUHSC_01605
            SAJ: SaurJH9_1569 SaurJH9_2765
            SAH: SaurJH1_1601 SaurJH1_2810
            SEP: SE1192
            SER: SERP1071(gnd)
            SHA: SH1406(gnd)
            SSP: SSP1244
            LMO: lmo1376
            LMF: LMOf2365_1395(gnd)
            LIN: lin1413
            LWE: lwe1392(gnd)
            LLA: L0046(gnd) L53699(gntZ)
            LLC: LACR_0642 LACR_2497
            LLM: llmg_0586(gnd) llmg_2469(gntZ)
            SPN: SP_0375
            SPR: spr0335(gnd)
            SPD: SPD_0343(gnd)
            SSA: SSA_1811(gnd)
            SGO: SGO_0503(gnd)
            LPL: lp_1251(gnd1) lp_1541(gnd2)
            LJO: LJ1852
            LAC: LBA1973
            LSA: LSA0297(gntZ) LSA1385(gndA)
            LSL: LSL_0645(gnd)
            LDB: Ldb2212(gnd)
            LBU: LBUL_2033
            LBR: LVIS_0094 LVIS_0144
            LCA: LSEI_0227 LSEI_1681
            LRE: Lreu_1766
            EFA: EF1049(gnd) EF3142
            OOE: OEOE_0892
            CTC: CTC01865
            TTE: TTE0195(gnd) TTE1941(gnd2)
            MTA: Moth_1283
            MCP: MCAP_0460
            MTU: Rv1122(gnd2) Rv1844c(gnd1)
            MTC: MT1154 MT1892(gnd)
            MBO: Mb1153(gnd2) Mb1875c(gnd1)
            MBB: BCG_1183(gnd2) BCG_1880c(gnd1)
            MLE: ML2065(gnd)
            MPA: MAP1557c(gnd) MAP2670c(gnd2)
            MAV: MAV_1253(gnd) MAV_2871(gnd)
            MSM: MSMEG_0002 MSMEG_3632(gnd)
            MMC: Mmcs_0003 Mmcs_2812
            CGL: NCgl1396(cgl1452)
            CGB: cg1643(gnd)
            CEF: CE1588
            CDI: DIP1213(gnd)
            CJK: jk0912(gnd)
            NFA: nfa11750(gnd) nfa54570(gnd2)
            RHA: RHA1_ro00556(gnd1) RHA1_ro03668(gnd2) RHA1_ro07246(gnd3)
                 RHA1_ro11061(gnd4) RHA1_ro11328(gnd5)
            SCO: SCO0975(SCBAC19F3.02) SCO3877(SCH18.14c) SCO6658(SC5A7.08c)
            SMA: SAV1771(gnd1) SAV4318(gnd2) SAV7249(gnd3)
            TWH: TWT492(gnd)
            TWS: TW272(gnd)
            LXX: Lxx00030(gnd) Lxx17380(gnd)
            CMI: CMM_0003(gndA1) CMM_2272(gndA2)
            AAU: AAur_2419(gnd)
            PAC: PPA1629
            TFU: Tfu_0003
            FRA: Francci3_0936
            FAL: FRAAL1567(gnd)
            ACE: Acel_1820
            SEN: SACE_0004(gnd2) SACE_4396(zwf3)
            BLO: BL0444(gnt)
            BAD: BAD_0197 BAD_0628(gnt)
            RXY: Rxyl_0050
            RBA: RB2817(6pgD)
            CTR: CT063(gnd)
            CTA: CTA_0068(gnd)
            CMU: TC0333
            CPN: CPn0360(gnd)
            CPA: CP0398
            CPJ: CPj0360(gnd)
            CPT: CpB0369
            CCA: CCA00432(gnd)
            CAB: CAB418(gnd)
            CFE: CF0576(gnd)
            PCU: pc0317(pgd)
            BGA: BG0571(gnd)
            BAF: BAPKO_0590(gnd)
            TPA: TP0331
            SYN: sll0329(gnd)
            SYW: SYNW1119(gnd)
            SYC: syc1460_c(gnd)
            SYF: Synpcc7942_0039
            SYD: Syncc9605_1256
            SYE: Syncc9902_1226
            SYG: sync_1688(gnd)
            SYR: SynRCC307_1252(gnd)
            SYX: SynWH7803_1297(gnd)
            CYA: CYA_0947(gnd)
            CYB: CYB_2481(gnd)
            TEL: tlr0576
            GVI: gll1117
            ANA: alr5275
            AVA: Ava_2527 Ava_C0152
            PMA: Pro0843(gnd)
            PMM: PMM0770(gnd)
            PMT: PMT0565(gnd)
            PMN: PMN2A_0176
            PMI: PMT9312_0778
            PMB: A9601_08321(gnd)
            PMC: P9515_08131(gnd)
            PMF: P9303_16871(gnd)
            PMG: P9301_08301(gnd)
            PMH: P9215_08641(gnd)
            PME: NATL1_08081(gnd)
            TER: Tery_1834
            BTH: BT_1222
            BFR: BF1853
            BFS: BF1919(gnd)
            SRU: SRU_0079(gnd)
            CHU: CHU_1404(gnd)
            FJO: Fjoh_4799
            CTE: CT1874
            CCH: Cag_1669
            PLT: Plut_0306
            DRA: DR_1595
            DGE: Dgeo_1973
            AAE: aq_498(gnd)
            TMA: TM0438
            TPT: Tpet_0482
            HMA: rrnAC2180(gnd)
            HWA: HQ1075A(gnd)
            NPH: NP0286A(gnd)
            RCI: RCIX2363(gnd)
STRUCTURES  PDB: 1PGJ  1PGN  1PGO  1PGP  1PGQ  2IYO  2IYP  2IZ0  2IZ1  2P4Q  
                 2PGD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.44
            ExPASy - ENZYME nomenclature database: 1.1.1.44
            ExplorEnz - The Enzyme Database: 1.1.1.44
            ERGO genome analysis and discovery system: 1.1.1.44
            BRENDA, the Enzyme Database: 1.1.1.44
            CAS: 9073-95-4
///
ENTRY       EC 1.1.1.45                 Enzyme
NAME        L-gulonate 3-dehydrogenase;
            L-3-aldonate dehydrogenase;
            L-3-aldonic dehydrogenase;
            L-gulonic acid dehydrogenase;
            L-beta-hydroxyacid dehydrogenase;
            L-beta-hydroxy-acid-NAD+-oxidoreductase;
            L-3-hydroxyacid dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-gulonate:NAD+ 3-oxidoreductase
REACTION    L-gulonate + NAD+ = 3-dehydro-L-gulonate + NADH + H+ [RN:R02640]
ALL_REAC    R02640
SUBSTRATE   L-gulonate [CPD:C00800];
            NAD+ [CPD:C00003]
PRODUCT     3-dehydro-L-gulonate [CPD:C00618];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also oxidizes other L-3-hydroxyacids.
REFERENCE   1
  AUTHORS   Dworsky, P. and Hoffmann-Ostenhof, O.
  TITLE     L-3-Aldonic acid dehydrogenase from Schwanniomyces occidentalis.
  JOURNAL   Acta Biochim. Pol. 11 (1964) 269-277.
  ORGANISM  Schwanniomyces occidentalis
REFERENCE   2
  AUTHORS   Smiley, J.D. and Ashwell, G.
  TITLE     Purification and properties of beta-L-hydroxy acid dehydrogenase.
            II. Isolation of beta-keto-L-gluconic acid, an intermediate in
            L-xylulose biosynthesis.
  JOURNAL   J. Biol. Chem. 236 (1961) 357-364.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
STRUCTURES  PDB: 2DPO  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.45
            ExPASy - ENZYME nomenclature database: 1.1.1.45
            ExplorEnz - The Enzyme Database: 1.1.1.45
            ERGO genome analysis and discovery system: 1.1.1.45
            BRENDA, the Enzyme Database: 1.1.1.45
            CAS: 9028-51-7
///
ENTRY       EC 1.1.1.46                 Enzyme
NAME        L-arabinose 1-dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-arabinose:NAD+ 1-oxidoreductase
REACTION    L-arabinose + NAD+ = L-arabinono-1,4-lactone + NADH + H+ [RN:R01757]
ALL_REAC    R01757
SUBSTRATE   L-arabinose [CPD:C00259];
            NAD+ [CPD:C00003]
PRODUCT     L-arabinono-1,4-lactone [CPD:C01114];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Weimberg, R. and Doudoroff, M.
  TITLE     The oxidation of L-arabinose by Pseudomonas saccharophila.
  JOURNAL   J. Biol. Chem. 217 (1955) 607-624.
  ORGANISM  Pseudomonas saccharophila
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.46
            ExPASy - ENZYME nomenclature database: 1.1.1.46
            ExplorEnz - The Enzyme Database: 1.1.1.46
            ERGO genome analysis and discovery system: 1.1.1.46
            BRENDA, the Enzyme Database: 1.1.1.46
            CAS: 9028-52-8
///
ENTRY       EC 1.1.1.47                 Enzyme
NAME        glucose 1-dehydrogenase;
            D-glucose dehydrogenase (NAD(P)+);
            hexose phosphate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     beta-D-glucose:NAD(P)+ 1-oxidoreductase
REACTION    beta-D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
            [RN:R01520 R01521]
ALL_REAC    R01520 R01521
SUBSTRATE   beta-D-glucose [CPD:C00221];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     D-glucono-1,5-lactone [CPD:C00198];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also oxidizes D-xylose.
REFERENCE   1  [PMID:810982]
  AUTHORS   Banauch D, Brummer W, Ebeling W, Metz H, Rindfrey H, Lang H, Leybold
            K, Rick W, Staudinger HJ.
  TITLE     [A glucose dehydrogenase for the determination of glucose
            concentrations in body fluids (author's transl)]
  JOURNAL   Z. Klin. Chem. Klin. Biochem. 13 (1975) 101-7.
  ORGANISM  Bacillus megaterium
REFERENCE   2
  AUTHORS   Brink, N.G.
  TITLE     Beef liver glucose dehydrogenase. 1. Purification and properties.
  JOURNAL   Acta Chem. Scand. 7 (1953) 1081-1089.
  ORGANISM  cow [GN:bta]
REFERENCE   3
  AUTHORS   Pauly, H.E. and Pfleiderer, G.
  TITLE     D-Glucose dehydrogenase from Bacillus megaterium M 1286:
            purification, properties and structure.
  JOURNAL   Hoppe-Seyler's Z. Physiol. Chem. 356 (1976) 1613-1623.
  ORGANISM  Bacillus megaterium
REFERENCE   4  [PMID:12981017]
  AUTHORS   STRECKER HJ, KORKES S.
  TITLE     Glucose dehydrogenase.
  JOURNAL   J. Biol. Chem. 196 (1952) 769-84.
  ORGANISM  cow [GN:bta]
REFERENCE   5  [PMID:4392298]
  AUTHORS   Thompson RE, Carper WR.
  TITLE     Glucose dehydrogenase from pig liver. I. Isolation and purification.
  JOURNAL   Biochim. Biophys. Acta. 198 (1970) 397-406.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00030  Pentose phosphate pathway
ORTHOLOGY   KO: K00034  glucose 1-dehydrogenase
GENES       HSA: 9563(H6PD)
            MMU: 100198(H6pd)
            RNO: 298655(H6pd_predicted)
            CFA: 489642(H6PD)
            GGA: 428188(H6PD)
            AFM: AFUA_1G15280 AFUA_6G03520 AFUA_7G04360
            UMA: UM05969.1
            TET: TTHERM_00079200
            PST: PSPTO_2492
            PSB: Psyr_2297
            PSP: PSPPH_2879
            PFL: PFL_4100
            PFO: Pfl_1840
            AHA: AHA_1994
            REU: Reut_B5464
            BMA: BMA1859
            BMV: BMASAVP1_A1103
            BML: BMA10299_A0763
            BXE: Bxe_B0443
            BPS: BPSL1186
            BPM: BURPS1710b_1408 BURPS1710b_A2499
            BTE: BTH_I1035
            TBD: Tbd_0924
            MFA: Mfla_1785
            BME: BMEI0861
            BMS: BR1122
            BJA: bll7157 bll7185(gdh)
            BRA: BRADO3388
            BBT: BBta_6708
            RDE: RD1_3328
            GOX: GOX2015
            BSU: BG10545(gdh) BG12761(ycdF)
            BAN: BA4968(gdH)
            BAR: GBAA4968(gdH)
            BAA: BA_5386
            BAT: BAS4612
            BCE: BC3460 BC4715
            BCA: BCE_4858(gdh)
            BCZ: BCZK4466(gdh) pE33L466_0368(gdh)
            BTK: BT9727_4448(gdh)
            BTL: BALH_3120 BALH_4289(gdh)
            BLI: BL01382(gdh) BL01687
            BLD: BLi00341(ycdF) BLi02566(gdh)
            BAY: RBAM_003090(ycdF) RBAM_004180(gdh) RBAM_013540(ykvO)
            BPU: BPUM_2122(gdh)
            OIH: OB3183
            SAA: SAUSA300_2416
            SEP: SE1830
            SER: SERP1839(gdh)
            SHA: SH0795
            SSP: SSP0656
            LAC: LBA1098
            LSL: LSL_0144(gdh)
            LCA: LSEI_2180
            EFA: EF2382(gdh)
            CGL: NCgl0689(fabG)
            RHA: RHA1_ro04900
            SMA: SAV1922(gdh)
            RBA: RB10002(gcd) RB7294(gdh)
            SYN: sll1709(gdh)
            SYG: sync_1918
            SYR: SynRCC307_1928(gdh)
            SYX: SynWH7803_0725(gdh)
            GVI: gll1114 gll1167
            ANA: all3836
            AVA: Ava_1863
            CHU: CHU_1661(gdh)
            HMA: rrnAC0011(ywfD1) rrnAC2741(ywfD2)
            HWA: HQ1663A(gdh)
            TAC: Ta0897
            TVO: TVN1019
            PTO: PTO0230 PTO0639 PTO1070
            PFU: PF1853
            RCI: RCIX1128(dhg)
            SSO: SSO3003(dhg-1) SSO3042(dhg-2) SSO3204(dhg-3)
            STO: ST1704
            SAI: Saci_1079
STRUCTURES  PDB: 1G6K  1GCO  1GEE  1RWB  1SPX  2B5V  2B5W  2CD9  2CDA  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.47
            ExPASy - ENZYME nomenclature database: 1.1.1.47
            ExplorEnz - The Enzyme Database: 1.1.1.47
            ERGO genome analysis and discovery system: 1.1.1.47
            BRENDA, the Enzyme Database: 1.1.1.47
            CAS: 9028-53-9
///
ENTRY       EC 1.1.1.48                 Enzyme
NAME        galactose 1-dehydrogenase;
            D-galactose dehydrogenase;
            beta-galactose dehydrogenase;
            NAD+-dependent D-galactose dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-galactose:NAD+ 1-oxidoreductase
REACTION    D-galactose + NAD+ = D-galactono-1,4-lactone + NADH + H+ [RN:R01094]
ALL_REAC    R01094;
            (other) R01097
SUBSTRATE   D-galactose [CPD:C00124];
            NAD+ [CPD:C00003]
PRODUCT     D-galactono-1,4-lactone [CPD:C03383];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13462997]
  AUTHORS   DE LEY J, DOUDOROFF M.
  TITLE     The metabolism of D-galactose in Pseudomonas saccharophila.
  JOURNAL   J. Biol. Chem. 227 (1957) 745-57.
  ORGANISM  Pseudomonas saccharophila
REFERENCE   2
  AUTHORS   Hu, A.S.L. and Cline, A.L.
  TITLE     The regulation of some sugar dehydrogenases in a pseudomonad.
  JOURNAL   Biochim. Biophys. Acta 93 (1964) 237-245.
  ORGANISM  Pseudomonas saccharophila
PATHWAY     PATH: map00052  Galactose metabolism
ORTHOLOGY   KO: K00035  D-galactose 1-dehydrogenase
GENES       XCC: XCC0744(dgd)
            XCB: XC_3491
            XCV: XCV0847
            XAC: XAC0797(dgd)
            XOO: XOO3804(dgd)
            XOM: XOO_3586(XOO3586)
            PST: PSPTO_4782(gal)
            PSB: Psyr_4331
            PSP: PSPPH_4371(gal)
            CSA: Csal_1017
            BVI: Bcep1808_3835
            BUR: Bcep18194_B0043
            BCN: Bcen_5217
            BCH: Bcen2424_5642
            BAM: Bamb_4922
            BTE: BTH_II1629
            MLO: mll0280
            SME: SMc00588(gal)
            SMD: Smed_0768
            ATU: Atu1113
            ATC: AGR_C_2059
            RET: RHE_CH01458(gal)
            RLE: RL1574
            BME: BMEII0355
            BMF: BAB2_0293
            BMS: BRA0941
            BMB: BruAb2_0292
            OAN: Oant_1420
            BJA: blr3205
            BRA: BRADO1814
            BBT: BBta_2134
            CCR: CC_0967
            PDE: Pden_4245
            SAL: Sala_0745
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.48
            ExPASy - ENZYME nomenclature database: 1.1.1.48
            ExplorEnz - The Enzyme Database: 1.1.1.48
            ERGO genome analysis and discovery system: 1.1.1.48
            BRENDA, the Enzyme Database: 1.1.1.48
            CAS: 9028-54-0
///
ENTRY       EC 1.1.1.49                 Enzyme
NAME        glucose-6-phosphate dehydrogenase;
            NADP-glucose-6-phosphate dehydrogenase;
            Zwischenferment;
            D-glucose 6-phosphate dehydrogenase;
            glucose 6-phosphate dehydrogenase (NADP);
            NADP-dependent glucose 6-phosphate dehydrogenase;
            6-phosphoglucose dehydrogenase;
            Entner-Doudoroff enzyme;
            glucose-6-phosphate 1-dehydrogenase;
            G6PDH;
            GPD
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-glucose-6-phosphate:NADP+ 1-oxidoreductase
REACTION    D-glucose 6-phosphate + NADP+ = D-glucono-1,5-lactone 6-phosphate +
            NADPH + H+ [RN:R00835]
ALL_REAC    R00835 > R02736
SUBSTRATE   D-glucose 6-phosphate [CPD:C00092];
            NADP+ [CPD:C00006]
PRODUCT     D-glucono-1,5-lactone 6-phosphate [CPD:C01236];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
INHIBITOR   Fatty acid [CPD:C00162]
COMMENT     Also acts slowly on beta-D-glucose and other sugars. Certain
            preparations reduce NAD+ as well as NADP+.
REFERENCE   1  [PMID:5363983]
  AUTHORS   Engel HJ, Domschke W, Alberti M, Domagk GF.
  TITLE     Protein structure and enzymatic activity. II. Purification and
            properties of a crystalline glucose-6-phosphate dehydrogenase from
            Candida utilis.
  JOURNAL   Biochim. Biophys. Acta. 191 (1969) 509-16.
  ORGANISM  Candida utilis
REFERENCE   2  [PMID:13252007]
  AUTHORS   GLASER L, BROWN DH.
  TITLE     Purification and properties of d-glucose-6-phosphate dehydrogenase.
  JOURNAL   J. Biol. Chem. 216 (1955) 67-79.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:13790996]
  AUTHORS   JULIAN GR, WOLFE RG, REITHEL FJ.
  TITLE     The enzymes of mammary gland. II. The preparation of glucose
            6-phosphate dehydrogenase.
  JOURNAL   J. Biol. Chem. 236 (1961) 754-8.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   4  [PMID:13729473]
  AUTHORS   NOLTMANN EA, GUBLER CJ, KUBY SA.
  TITLE     Glucose 6-phosphate dehydrogenase (Zwischenferment). I. Isolation of
            the crystalline enzyme from yeast.
  JOURNAL   J. Biol. Chem. 236 (1961) 1225-30.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   5  [PMID:11457850]
  AUTHORS   Miclet E, Stoven V, Michels PA, Opperdoes FR, Lallemand JY, Duffieux
            F.
  TITLE     NMR spectroscopic analysis of the first two steps of the
            pentose-phosphate pathway elucidates the role of
            6-phosphogluconolactonase.
  JOURNAL   J. Biol. Chem. 276 (2001) 34840-6.
  ORGANISM  Trypanosoma brucei [GN:tbr], Plasmodium falciparum [GN:pfa], human
            [GN:hsa]
PATHWAY     PATH: map00030  Pentose phosphate pathway
            PATH: map00480  Glutathione metabolism
ORTHOLOGY   KO: K00036  glucose-6-phosphate 1-dehydrogenase
GENES       HSA: 2539(G6PD)
            MMU: 14380(G6pd2) 14381(G6pdx)
            RNO: 24377(G6pdx)
            CFA: 481088(G6PD)
            BTA: 281179(G6PD)
            XLA: 379711(MGC69058)
            XTR: 550066(g6pd2)
            DRE: 570579(LOC570579)
            SPU: 590603(LOC590603)
            DME: Dmel_CG12529(Zw)
            CEL: B0035.5(glucose-6-phosphate-1-dehydrogenase)
            ATH: AT1G09420(G6PD4) AT1G24280(G6PD3) AT3G27300(G6PD5)
                 AT5G13110(G6PD2) AT5G35790(G6PD1) AT5G40760(G6PD6)
            OSA: 4329889 4332659 4333103 4336209 4342988
            CME: CMI224C CMR014C
            SCE: YNL241C(ZWF1)
            AGO: AGOS_ABL206C
            PIC: PICST_60598(SOL1) PICST_85065(ZWF1)
            CAL: CaO19_12218(CaO19.12218)
            CGR: CAGL0J07612g
            SPO: SPAC3A12.18(zwf1) SPAC3C7.13c SPCC794.01c
            ANI: AN2981.2
            AFM: AFUA_3G08470
            AOR: AO090005001427
            ANG: An02g12140(gsdA)
            CNE: CNG03280
            UMA: UM04930.1
            ECU: ECU08_1850
            DDI: DDBDRAFT_0217233
            PFA: PF14_0511
            TAN: TA05220
            TPV: TP03_0558
            TBR: Tb10.70.5200
            TCR: 509287.50
            LMA: LmjF34.0080
            ECO: b1852(zwf)
            ECJ: JW1841(zwf)
            ECE: Z2904(zwf)
            ECS: ECs2562
            ECC: c2265(zwf)
            ECI: UTI89_C2055(zwf)
            ECP: ECP_1796
            ECV: APECO1_902(zwf)
            ECW: EcE24377A_2082(zwf)
            ECX: EcHS_A1944(zwf)
            STY: STY2094(zwf)
            STT: t0991(zwf)
            SPT: SPA0983(zwf)
            SEC: SC1891(zwf)
            STM: STM1886(zwf)
            YPE: YPO2066(zwf)
            YPK: y2244(zwf)
            YPM: YP_1909(zwf)
            YPA: YPA_1449
            YPN: YPN_1543
            YPP: YPDSF_1056
            YPS: YPTB2049(zwf)
            YPI: YpsIP31758_2022(zwf)
            SFX: S1928(zwf)
            SFV: SFV_1854(zwf)
            SSN: SSON_1296(zwf)
            SBO: SBO_1160(zwf)
            SDY: SDY_1138(zwf)
            ECA: ECA2479(zwf)
            PLU: plu2122(zwf)
            BUC: BU320(zwf)
            BAS: BUsg312(zwf)
            BAB: bbp298(zwf)
            BCC: BCc_199(zwf)
            SGL: SG1270
            ENT: Ent638_2421
            SPE: Spro_2768
            BFL: Bfl449(zwf)
            BPN: BPEN_464(zwf)
            HIT: NTHI0686(zwf)
            HIP: CGSHiEE_00205
            HIQ: CGSHiGG_06085
            HDU: HD0838(zwf)
            HSO: HS_1651(zwf)
            PMU: PM1549(zwf)
            MSU: MS0016(zwf)
            APL: APL_1311(zwf)
            ASU: Asuc_0227
            XFA: XF1065
            XFT: PD0346(zwf)
            XCC: XCC2136(zwf) XCC3993(zwf)
            XCB: XC_1977 XC_4082
            XCV: XCV2237(zwf1) XCV4168(zwf2)
            XAC: XAC2071(zwf) XAC4081(zwf)
            XOO: XOO0467(zwf) XOO2314(zwf)
            XOM: XOO_0432(XOO0432) XOO_2191(XOO2191)
            VCH: VCA0896
            VCO: VC0395_0341(zwf)
            VVU: VV1_2684
            VVY: VV1605
            VPA: VP1710
            VFI: VFA0468
            PPR: PBPRA1442
            PAE: PA3183(zwf) PA5439
            PAU: PA14_23070(zwf) PA14_71800(zwf)
            PAP: PSPA7_1947(zwf2) PSPA7_6228(zwf1)
            PPU: PP_1022(zwf-1) PP_4042(zwf-2) PP_5351(zwf-3)
            PPF: Pput_1060 Pput_1796 Pput_5259
            PST: PSPTO_1300(zwf-1) PSPTO_3121(zwf-2)
            PSB: Psyr_1120 Psyr_2988
            PSP: PSPPH_1188(zwf1)
            PFL: PFL_3143(zwf) PFL_4610(zwf)
            PFO: Pfl_2587 Pfl_4363
            PEN: PSEEN1940(zwf-2) PSEEN4405(zwf-1) PSEEN5500(zwf-3)
            PMY: Pmen_3143 Pmen_4486
            SON: SO_2489(zwf)
            SDN: Sden_2079
            SFR: Sfri_1892
            SAZ: Sama_1812
            SBL: Sbal_2241
            SBM: Shew185_2130
            SLO: Shew_2048
            SPC: Sputcn32_1866
            SSE: Ssed_2070
            SPL: Spea_2335
            SHE: Shewmr4_2046
            SHM: Shewmr7_1929
            SHN: Shewana3_2151
            SHW: Sputw3181_2142
            CPS: CPS_2281(zwf)
            PHA: PSHAa1140(zwf)
            PAT: Patl_0970
            SDE: Sde_1380
            PIN: Ping_2754
            MAQ: Maqu_1834
            LPN: lpg0416(zwf)
            LPF: lpl0459(zwf)
            LPP: lpp0483(zwf)
            MCA: MCA0025(zwf-1) MCA2971(zwf-2)
            TCX: Tcr_1214
            NOC: Noc_0772 Noc_2062
            HCH: HCH_00347(zwf)
            CSA: Csal_2741
            MMW: Mmwyl1_1038
            DNO: DNO_1223(zwf)
            BCI: BCI_0309(zwf)
            NME: NMB1392
            NMA: NMA1609(zwf)
            NMC: NMC1331(zwf)
            NGO: NGO0715
            CVI: CV_0145(zwf)
            RSO: RSp1559(zwf)
            REU: Reut_A1650 Reut_B5329
            REH: H16_A0316(zwf1) H16_B1501(zwf2) H16_B2566(zwf3)
            RME: Rmet_5801
            BMA: BMA2130(zwf)
            BMV: BMASAVP1_A0780(zwf)
            BML: BMA10299_A2614(zwf)
            BMN: BMA10247_2000(zwf)
            BXE: Bxe_A3452 Bxe_B0215 Bxe_B1764
            BVI: Bcep1808_0883 Bcep1808_3601
            BUR: Bcep18194_A4070 Bcep18194_B0242
            BCN: Bcen_0488 Bcen_5455
            BCH: Bcen2424_0967 Bcen2424_5407
            BAM: Bamb_0827 Bamb_4748
            BPS: BPSL2612(zwf)
            BPM: BURPS1710b_3087(zwf)
            BPL: BURPS1106A_3053(zwf)
            BPD: BURPS668_2999(zwf)
            BTE: BTH_I1552(zwf)
            RFR: Rfer_1125 Rfer_4034
            POL: Bpro_0751
            PNA: Pnap_0653 Pnap_3694
            AAV: Aave_0942
            AJS: Ajs_0695
            VEI: Veis_4223
            HAR: HEAR1084(zwf)
            MMS: mma_2313(zwf)
            NEU: NE0398(zwf)
            NET: Neut_2143 Neut_2431
            NMU: Nmul_A0466
            DAR: Daro_2070
            MFA: Mfla_0917 Mfla_1061
            HPY: HP1101
            HPA: HPAG1_1039
            HAC: Hac_0441
            CJD: JJD26997_1270(zwf)
            GME: Gmet_2619
            PCA: Pcar_0924
            PPD: Ppro_2250
            DDE: Dde_3471
            ADE: Adeh_1439
            AFW: Anae109_0597 Anae109_3326
            MXA: MXAN_0953(zwf)
            MLO: mll6516 mlr4207
            MES: Meso_0159
            SME: SMc03070(zwf)
            SMD: Smed_0300
            ATU: Atu0600(zwf) Atu4835
            ATC: AGR_C_1065 AGR_L_98
            RET: RHE_CH00704(zwf1) RHE_CH01185(zwf2)
            RLE: RL0753(zwf) RL1315(zwf) pRL120561
            BME: BMEII0513
            BMF: BAB2_0460
            BMS: BRA0778(zwf)
            BMB: BruAb2_0454(zwf)
            BOV: BOV_A0728(zwf)
            OAN: Oant_3956
            BJA: blr6760(zwf)
            BRA: BRADO5811(zwf)
            BBT: BBta_6317(zwf) BBta_p0094(zwf)
            RPA: RPA3636(zwf)
            RPB: RPB_1890
            RPC: RPC_3672
            RPD: RPD_3476
            RPE: RPE_3710
            NWI: Nwi_2643
            NHA: Nham_3271
            BHE: BH03910(zwf)
            BQU: BQ02930(zwf)
            XAU: Xaut_1017 Xaut_1252
            CCR: CC_2057
            SIL: SPO2048(zwf-1) SPO3033(zwf-2)
            SIT: TM1040_0377
            RSP: RSP_2734(zwf)
            RSH: Rsph17029_1392
            RSQ: Rsph17025_1778
            JAN: Jann_1969
            RDE: RD1_2722(zwf)
            PDE: Pden_1952
            MMR: Mmar10_2642
            HNE: HNE_1738(zwf)
            ZMO: ZMO0367(zwf)
            NAR: Saro_1893
            SAL: Sala_0190
            SWI: Swit_1623 Swit_2887
            ELI: ELI_00545
            GOX: GOX0145
            GBE: GbCGDNIH1_0798 GbCGDNIH1_0853
            ACR: Acry_0465 Acry_1275
            ABA: Acid345_2812
            SUS: Acid_5281
            BSU: BG11739(zwf)
            BAN: BA3433(zwf)
            BAR: GBAA3433(zwf)
            BAA: BA_3931
            BAT: BAS3182
            BCA: BCE_3412(zwf)
            BCZ: BCZK3083(zwf) BCZK3084(g6pD)
            BTK: BT9727_3166(zwf)
            BTL: BALH_3052
            BLI: BL01964(zwf)
            BLD: BLi02555(zwf)
            BCL: ABC1924(zwf)
            BAY: RBAM_022160(zwf)
            BPU: BPUM_2116(zwf)
            OIH: OB2938
            GKA: GK2334
            GTN: GTNG_2264(zwf)
            SAU: SA1336
            SAV: SAV1505
            SAM: MW1459
            SAR: SAR1582(zwf)
            SAS: SAS1445
            SAC: SACOL1549(zwf)
            SAB: SAB1366
            SAA: SAUSA300_1454(zwf)
            SAO: SAOUHSC_01599
            SAJ: SaurJH9_1562 SaurJH9_2764
            SAH: SaurJH1_1593 SaurJH1_2809
            SEP: SE1188
            SER: SERP1067(zwf-2)
            SHA: SH1411
            SSP: SSP1248
            LMO: lmo1978
            LMF: LMOf2365_2002(zwf)
            LIN: lin2085
            LWE: lwe1997(zwf)
            LLA: L0044(zwf)
            LLC: LACR_2527
            LLM: llmg_2499
            SPN: SP_1243
            SPR: spr1122(zwf)
            SPD: SPD_1100(zwf)
            SSA: SSA_1555(gdh)
            SSU: SSU05_1184
            SSV: SSU98_1201
            SGO: SGO_0788(zwf)
            LPL: lp_2681(gpd)
            LJO: LJ0470
            LAC: LBA0413
            LSA: LSA0381(zwf)
            LSL: LSL_0462(zwf)
            LDB: Ldb1611(gpd)
            LBU: LBUL_1490
            LBR: LVIS_0097
            LCA: LSEI_0778
            LGA: LGAS_0417
            LRE: Lreu_1765
            PPE: PEPE_1267
            EFA: EF1004(zwf)
            OOE: OEOE_0135
            LME: LEUM_2016
            CTC: CTC01864
            AMT: Amet_3468
            TTE: TTE1005(zwf)
            MTA: Moth_2302
            MTU: Rv1121(zwf1) Rv1447c(zwf2)
            MTC: MT1153(zwf-1) MT1494(zwf-2)
            MBO: Mb1152(zwf1) Mb1482c(zwf2)
            MBB: BCG_1182(zwf1) BCG_1508c(zwf2)
            MPA: MAP1176c(zwf2) MAP2671c(zwf)
            MAV: MAV_1252(zwf) MAV_2733(zwf) MAV_3329(zwf)
            MSM: MSMEG_0314(zwf) MSMEG_3101(zwf)
            MVA: Mvan_2718
            MGI: Mflv_0266 Mflv_3694 Mflv_4263
            MMC: Mmcs_0459 Mmcs_2412 Mmcs_4976
            MKM: Mkms_0470 Mkms_2458
            MJL: Mjls_0446 Mjls_2452 Mjls_5357
            CGL: NCgl1514(cgl1576)
            CGB: cg1778(zwf)
            CEF: CE1696
            CDI: DIP1304(zwf)
            CJK: jk0994(zwf)
            NFA: nfa35750(zwf)
            RHA: RHA1_ro00555(zwf1) RHA1_ro02369(zwf2) RHA1_ro05641(zwf3)
                 RHA1_ro07184(zwf4) RHA1_ro11166 RHA1_ro11332(zwf5)
            SCO: SCO1937(SCC22.19) SCO6661(SC5A7.11c)
            SMA: SAV1768(zwf1) SAV6313(zwf2)
            TWH: TWT343(zwf)
            TWS: TW428(zwf)
            LXX: Lxx11590(zwf)
            CMI: CMM_1074(zwfB) CMM_1519(zwfA1) CMM_1737(zwfA2)
            ART: Arth_2094 Arth_2490
            AAU: AAur_2094(zwf) AAur_2459(zwf)
            PAC: PPA1563
            NCA: Noca_2538 Noca_4526
            TFU: Tfu_2005
            FRA: Francci3_1647
            FAL: FRAAL4576(zwf)
            ACE: Acel_1124
            KRA: Krad_0133 Krad_1200 Krad_2924
            SEN: SACE_2157(zwf)
            STP: Strop_3092
            BLO: BL0440(zwf2)
            BAD: BAD_0631(zwf2)
            RXY: Rxyl_0051
            RBA: RB2735(g6pD)
            CTR: CT185(zwf)
            CTA: CTA_0203(zwf)
            CMU: TC0457
            CPN: CPn0238(zwf)
            CPA: CP0524
            CPJ: CPj0238(zwf)
            CPT: CpB0244
            CCA: CCA00540(zwf)
            CAB: CAB526(zwf)
            CFE: CF0468(zwf)
            PCU: pc0821(zwf)
            BGA: BG0658(zwf)
            TPA: TP0478
            SYN: slr1843(zwf)
            SYW: SYNW0750(zwf)
            SYC: syc1768_d(zwf)
            SYF: Synpcc7942_2334
            SYD: Syncc9605_1918
            SYE: Syncc9902_0748
            SYG: sync_1002(zwf)
            SYR: SynRCC307_0759(zwf)
            SYX: SynWH7803_1561(zwf)
            CYA: CYA_1699(zwf)
            CYB: CYB_1985(zwf)
            TEL: tll0540(zwf)
            GVI: gll1170(zwf) glr3178(zwf)
            ANA: all4019(zwf)
            AVA: Ava_1682 Ava_C0151
            PMA: Pro1124(zwf)
            PMM: PMM1074(zwf)
            PMT: PMT1102(zwf)
            PMN: PMN2A_0676
            PMI: PMT9312_1085
            PMB: A9601_11801(zwf)
            PMC: P9515_11641(zwf)
            PMF: P9303_09401(zwf)
            PMG: P9301_11811(zwf)
            PMH: P9215_12101(zwf)
            PME: NATL1_15091(zwf)
            TER: Tery_0684
            BTH: BT_1221
            BFR: BF1854
            BFS: BF1920(zwf)
            SRU: SRU_0078(zwf)
            FJO: Fjoh_4800
            CTE: CT1873(zwf)
            CCH: Cag_1668
            CPH: Cpha266_2150
            PVI: Cvib_0375
            PLT: Plut_0307
            RRS: RoseRS_2562
            RCA: Rcas_1852
            DRA: DR_1596
            DGE: Dgeo_1974
            AAE: aq_497(gsdA)
            TMA: TM1155
            TPT: Tpet_1595
STRUCTURES  PDB: 1DPG  1E77  1E7M  1E7Y  1H93  1H94  1H9A  1H9B  1QKI  2BH9  
                 2BHL  2DPG  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.49
            ExPASy - ENZYME nomenclature database: 1.1.1.49
            ExplorEnz - The Enzyme Database: 1.1.1.49
            ERGO genome analysis and discovery system: 1.1.1.49
            BRENDA, the Enzyme Database: 1.1.1.49
            CAS: 9001-40-5
///
ENTRY       EC 1.1.1.50                 Enzyme
NAME        3alpha-hydroxysteroid dehydrogenase (B-specific);
            hydroxyprostaglandin dehydrogenase;
            3alpha-hydroxysteroid oxidoreductase;
            sterognost 3alpha
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3alpha-hydroxysteroid:NAD(P)+ oxidoreductase (B-specific)
REACTION    androsterone + NAD(P)+ = 5alpha-androstane-3,17-dione + NAD(P)H + H+
            [RN:R02476 R02477]
ALL_REAC    R02476 R02477;
            (other) R04309 R04310 R04818 R04819 R04824 R04825 R04829 R04830
            R04832 R04833 R04835 R04836 R04837 R04838 R04842 R04843 R04845
            R04846
SUBSTRATE   androsterone [CPD:C00523];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     5alpha-androstane-3,17-dione [CPD:C00674];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on other 3alpha-hydroxysteroids and on 9-, 11- and
            15-hydroxyprostaglandin. B-specific with respect to NAD+ or NADP+.
REFERENCE   1  [PMID:14406805]
  AUTHORS   JARABAK J, TALALAY P.
  TITLE     Stereospecificity of hydrogen transfer by pyridine nucleotide-linked
            hydroxysteroid dehydrogenases.
  JOURNAL   J. Biol. Chem. 235 (1960) 2147-51.
  ORGANISM  Pseudomonas testosteroni
REFERENCE   2  [PMID:13405910]
  AUTHORS   KOCHAKIAN CD, CARROLL BR, UHRI B.
  TITLE     Comparisons of the oxidation of C19-hydroxysteroids by guinea pig
            liver homogenates.
  JOURNAL   J. Biol. Chem. 224 (1957) 811-8.
  ORGANISM  guinea pig
REFERENCE   3
  AUTHORS   Marcus, P.I. and Talalay, P.
  TITLE     Induction and purification of alpha- and beta-hydroxysteroid
            dehydrogenases.
  JOURNAL   J. Biol. Chem. 218 (1956) 661-674.
  ORGANISM  Pseudomonas testosteroni
REFERENCE   4  [PMID:3479982]
  AUTHORS   Penning TM, Sharp RB.
  TITLE     Prostaglandin dehydrogenase activity of purified rat liver 3
            alpha-hydroxysteroid dehydrogenase.
  JOURNAL   Biochem. Biophys. Res. Commun. 148 (1987) 646-52.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00120  Bile acid biosynthesis
            PATH: map00140  C21-Steroid hormone metabolism
            PATH: map00150  Androgen and estrogen metabolism
ORTHOLOGY   KO: K00037  3-alpha-hydroxysteroid dehydrogenase
GENES       HSA: 1109(AKR1C4)
            XFA: XF2269
            XFT: PD1305(fabG)
            XCC: XCC0353
            XCB: XC_0365
            XCV: XCV0366
            XAC: XAC0353
            PHA: PSHAa2145(hsdA)
            RSO: RS05193(RSp0230)
            REH: H16_B0673
            RLE: pRL120488
            MSM: MSMEG_4862
STRUCTURES  PDB: 1AFS  1FJH  1FK8  1LWI  1RAL  2DKN  2FVL  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.50
            ExPASy - ENZYME nomenclature database: 1.1.1.50
            ExplorEnz - The Enzyme Database: 1.1.1.50
            ERGO genome analysis and discovery system: 1.1.1.50
            BRENDA, the Enzyme Database: 1.1.1.50
            CAS: 9028-56-2
///
ENTRY       EC 1.1.1.51                 Enzyme
NAME        3(or 17)beta-hydroxysteroid dehydrogenase;
            beta-hydroxy steroid dehydrogenase;
            17-ketoreductase;
            17beta-hydroxy steroid dehydrogenase;
            3beta-hydroxysteroid dehydrogenase;
            17beta-hydroxy steroid dehydrogenase;
            3beta-hydroxy steroid dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3(or 17)beta-hydroxysteroid:NAD(P)+ oxidoreductase
REACTION    testosterone + NAD(P)+ = androst-4-ene-3,17-dione + NAD(P)H + H+
            [RN:R01836 R01838]
ALL_REAC    R01836 R01838;
            (other) R02352 R02353 R03406 R03407
SUBSTRATE   testosterone [CPD:C00535];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     androst-4-ene-3,17-dione [CPD:C00280];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on other 3beta- or 17beta-hydroxysteroids. cf. EC
            1.1.1.209 3(or 17)alpha-hydroxysteroid dehydrogenase.
REFERENCE   1  [PMID:14214322]
  AUTHORS   DAHM K, BREUER H.
  TITLE     [PRECIPITATION OF A 17-BETA-HYDROXYSTEROID:NAD(P) OXIDOREDUCTASE
            FROM THE RAT ADRENAL GLAND.]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 336 (1964) 63-8.
REFERENCE   2  [PMID:13549484]
  AUTHORS   LYNN WS Jr, BROWN RH.
  TITLE     The conversion of progesterone to androgens by testes.
  JOURNAL   J. Biol. Chem. 232 (1958) 1015-30.
  ORGANISM  guinea pig
REFERENCE   3
  AUTHORS   Marcus, P.I. and Talalay, P.
  TITLE     Induction and purification of alpha- and beta-hydroxysteroid
            dehydrogenases.
  JOURNAL   J. Biol. Chem. 218 (1956) 661-674.
  ORGANISM  Pseudomonas testosteroni
REFERENCE   4  [PMID:193845]
  AUTHORS   Schultz RM, Groman EV, Engel LL.
  TITLE     3(17)beta-Hydroxysteroid dehydrogenase of Pseudomonas testosteroni.
            A convenient purification and demonstration of multiple molecular
            forms.
  JOURNAL   J. Biol. Chem. 252 (1977) 3775-83.
  ORGANISM  Pseudomonas testosteroni
REFERENCE   5
  AUTHORS   Talalay, P. and Dobson, M.M.
  TITLE     Purification and properties of a alpha-hydroxysteroid dehydrogenase.
  JOURNAL   J. Biol. Chem. 205 (1953) 823-837.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00150  Androgen and estrogen metabolism
ORTHOLOGY   KO: K05296  3(or 17)beta-hydroxysteroid dehydrogenase
GENES       REH: H16_B0642 H16_B0649
            BUR: Bcep18194_B1514
STRUCTURES  PDB: 1HXH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.51
            ExPASy - ENZYME nomenclature database: 1.1.1.51
            ExplorEnz - The Enzyme Database: 1.1.1.51
            ERGO genome analysis and discovery system: 1.1.1.51
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.51
            BRENDA, the Enzyme Database: 1.1.1.51
            CAS: 9015-81-0
///
ENTRY       EC 1.1.1.52                 Enzyme
NAME        3alpha-hydroxycholanate dehydrogenase;
            alpha-hydroxy-cholanate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3alpha-hydroxy-5beta-cholanate:NAD+ oxidoreductase
REACTION    3alpha-hydroxy-5beta-cholanate + NAD+ = 3-oxo-5beta-cholanate + NADH
            + H+ [RN:R04139]
ALL_REAC    R04139
SUBSTRATE   3alpha-hydroxy-5beta-cholanate [CPD:C03990];
            NAD+ [CPD:C00003]
PRODUCT     3-oxo-5beta-cholanate [CPD:C03070];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts on other 3alpha-hydroxysteroids with an acidic side-chain.
REFERENCE   1  [PMID:14377608]
  AUTHORS   HAYAISHI O, SATO Y, JAKOBY WB, STOHLMAN EF.
  TITLE     Reversible enzymatic oxidation of bile acids.
  JOURNAL   Arch. Biochem. 56 (1955) 554-5.
STRUCTURES  PDB: 1IHI  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.52
            ExPASy - ENZYME nomenclature database: 1.1.1.52
            ExplorEnz - The Enzyme Database: 1.1.1.52
            ERGO genome analysis and discovery system: 1.1.1.52
            BRENDA, the Enzyme Database: 1.1.1.52
            CAS: 9028-57-3
///
ENTRY       EC 1.1.1.53                 Enzyme
NAME        3alpha(or 20beta)-hydroxysteroid dehydrogenase;
            cortisone reductase;
            (R)-20-hydroxysteroid dehydrogenase;
            dehydrogenase, 20beta-hydroxy steroid;
            Delta4-3-ketosteroid hydrogenase;
            20beta-hydroxysteroid dehydrogenase;
            3alpha,20beta-hydroxysteroid:NAD+-oxidoreductase;
            NADH-20beta-hydroxysteroid dehydrogenase;
            20beta-HSD
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3alpha(or 20beta)-hydroxysteroid:NAD+ oxidoreductase
REACTION    androstan-3alpha,17beta-diol + NAD+ = 17beta-hydroxyandrostan-3-one
            + NADH + H+ [RN:R04330]
ALL_REAC    R04330;
            (other) R04818 R04819 R04824 R04825 R04831 R04834 R04844 R04847
SUBSTRATE   androstan-3alpha,17beta-diol [CPD:C03852];
            NAD+ [CPD:C00003]
PRODUCT     17beta-hydroxyandrostan-3-one [CPD:C03917];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The 3alpha-hydroxy group or 20beta-hydroxy group of pregnane and
            androstane steroids can act as donor.
REFERENCE   1  [PMID:718844]
  AUTHORS   Edwards CA, Orr JC.
  TITLE     Comparison of the 3alpha-and 20beta-hydroxysteroid dehydrogenase
            activities of the cortisone reductase of Streptomyces hydrogenans.
  JOURNAL   Biochemistry. 17 (1978) 4370-6.
  ORGANISM  Streptomyces hydrogenans
REFERENCE   2  [PMID:16526091]
  AUTHORS   Kung CC, Huang WN, Huang YC, Yeh KC.
  TITLE     Proteomic survey of copper-binding proteins in Arabidopsis roots by
            immobilized metal affinity chromatography and mass spectrometry.
  JOURNAL   Proteomics. 6 (2006) 2746-58.
REFERENCE   3  [PMID:16526091]
  AUTHORS   Kung CC, Huang WN, Huang YC, Yeh KC.
  TITLE     Proteomic survey of copper-binding proteins in Arabidopsis roots by
            immobilized metal affinity chromatography and mass spectrometry.
  JOURNAL   Proteomics. 6 (2006) 2746-58.
REFERENCE   4  [PMID:13549484]
  AUTHORS   LYNN WS Jr, BROWN RH.
  TITLE     The conversion of progesterone to androgens by testes.
  JOURNAL   J. Biol. Chem. 232 (1958) 1015-30.
  ORGANISM  guinea pig, rat [GN:rno]
REFERENCE   5  [PMID:6936053]
  AUTHORS   Strickler RC, Covey DF, Tobias B.
  TITLE     Study of 3 alpha, 20 beta-hydroxysteroid dehydrogenase with an
            enzyme-generated affinity alkylator: dual enzyme activity at a
            single active site.
  JOURNAL   Biochemistry. 19 (1980) 4950-4.
  ORGANISM  Streptomyces hydrogenans
REFERENCE   6  [PMID:6928375]
  AUTHORS   Sweet F, Samant BR.
  TITLE     Bifunctional enzyme activity at the same active site: study of 3
            alpha and 20 beta activity by affinity alkylation of 3 alpha, 20
            beta-hydroxysteroid dehydrogenase with 17-(bromoacetoxy)steroids.
  JOURNAL   Biochemistry. 19 (1980) 978-86.
  ORGANISM  Streptomyces hydrogenans
PATHWAY     PATH: map00120  Bile acid biosynthesis
            PATH: map00140  C21-Steroid hormone metabolism
ORTHOLOGY   KO: K00038  3alpha(or 20beta)-hydroxysteroid dehydrogenase
GENES       PHA: PSHAa0891
            BUR: Bcep18194_B1012 Bcep18194_B1510
            GME: Gmet_2226 Gmet_2249
            RLE: RL1197
            OIH: OB0329
            LBR: LVIS_0330
            MBO: Mb2025(fabG3)
            MBB: BCG_2019(fabG3)
            MPA: MAP1739c(fabG3_1)
            MAV: MAV_2509 MAV_5136
            MSM: MSMEG_2566 MSMEG_3515
            NFA: nfa48060
            SEN: SACE_4705
STRUCTURES  PDB: 1HDC  1N5D  1NFF  1NFQ  1NFR  2HSD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.53
            ExPASy - ENZYME nomenclature database: 1.1.1.53
            ExplorEnz - The Enzyme Database: 1.1.1.53
            ERGO genome analysis and discovery system: 1.1.1.53
            BRENDA, the Enzyme Database: 1.1.1.53
            CAS: 9028-42-6
///
ENTRY       EC 1.1.1.54                 Enzyme
NAME        allyl-alcohol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     allyl-alcohol:NADP+ oxidoreductase
REACTION    allyl alcohol + NADP+ = acrolein + NADPH + H+ [RN:R03572]
ALL_REAC    R03572
SUBSTRATE   allyl alcohol [CPD:C02001];
            NADP+ [CPD:C00006]
PRODUCT     acrolein [CPD:C01471];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on saturated primary alcohols.
REFERENCE   1
  AUTHORS   Otsuka, K.
  TITLE     Triphosphopyridine nucleotide-allyl and -ethyl alcohol
            dehydrogenases from Escherichia coli.
  JOURNAL   J. Gen. Appl. Microbiol. 4 (1958) 211-215.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.54
            ExPASy - ENZYME nomenclature database: 1.1.1.54
            ExplorEnz - The Enzyme Database: 1.1.1.54
            ERGO genome analysis and discovery system: 1.1.1.54
            BRENDA, the Enzyme Database: 1.1.1.54
            CAS: 9028-58-4
///
ENTRY       EC 1.1.1.55                 Enzyme
NAME        lactaldehyde reductase (NADPH);
            lactaldehyde (reduced nicotinamide adenine dinucleotide phosphate)
            reductase;
            NADP+-1,2-propanediol dehydrogenase;
            propanediol dehydrogenase;
            1,2-propanediol:NADP+ oxidoreductase;
            lactaldehyde reductase (NADPH)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     propane-1,2-diol:NADP+ oxidoreductase
REACTION    propane-1,2-diol + NADP+ = L-lactaldehyde + NADPH + H+ [RN:R02259]
ALL_REAC    R02259
SUBSTRATE   propane-1,2-diol [CPD:C00583];
            NADP+ [CPD:C00006]
PRODUCT     L-lactaldehyde [CPD:C00424];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     May be identical with EC 1.1.1.2 alcohol dehydrogenase (NADP+).
REFERENCE   1  [PMID:13830319]
  AUTHORS   GUPTA NK, ROBINSON WG.
  TITLE     The enzymatic conversion of lactaldehyde to propanediol.
  JOURNAL   J. Biol. Chem. 235 (1960) 1609-12.
  ORGANISM  Pseudomonas fluorescens, spinach, rat [GN:rno], cow [GN:bta], pig
            [GN:ssc]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.55
            ExPASy - ENZYME nomenclature database: 1.1.1.55
            ExplorEnz - The Enzyme Database: 1.1.1.55
            ERGO genome analysis and discovery system: 1.1.1.55
            BRENDA, the Enzyme Database: 1.1.1.55
            CAS: 9028-43-7
///
ENTRY       EC 1.1.1.56                 Enzyme
NAME        ribitol 2-dehydrogenase;
            adonitol dehydrogenase;
            ribitol dehydrogenase A (wild type);
            ribitol dehydrogenase B (mutant enzyme with different properties);
            ribitol dehydrogenase D (mutant enzyme with different properties)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     ribitol:NAD+ 2-oxidoreductase
REACTION    ribitol + NAD+ = D-ribulose + NADH + H+ [RN:R01893]
ALL_REAC    R01893 > R01895
SUBSTRATE   ribitol [CPD:C00474];
            NAD+ [CPD:C00003]
PRODUCT     D-ribulose [CPD:C00309];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13416220]
  AUTHORS   HOLLMANN S, TOUSTER O.
  TITLE     The L-xylulose-xylitol enzyme and other polyol dehydrogenases of
            guinea pig liver mitochondria.
  JOURNAL   J. Biol. Chem. 225 (1957) 87-102.
  ORGANISM  guinea pig
REFERENCE   2
  AUTHORS   Nordlie, R.C. and Fromm, H.J.
  TITLE     Ribitol dehydrogenase. II. Studies on the reaction mechanism.
  JOURNAL   J. Biol. Chem. 234 (1959) 2523-2531.
  ORGANISM  Aerobacter aerogenes
REFERENCE   3
  AUTHORS   Wood, W.A., McDonough, M.J. and Jacobs, L.B.
  TITLE     Ribitol and D-arabitol utilization by Aerobacter aerogenes.
  JOURNAL   J. Biol. Chem. 236 (1961) 2190-2195.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K00039  ribitol 2-dehydrogenase
GENES       PIC: PICST_36953(TSC10) PICST_53846(AYR3) PICST_80053(YIM4)
            BXE: Bxe_A0233
            ATU: Atu4323(rdh)
            ATC: AGR_L_1076
            RET: RHE_PC00223(ypc00125) RHE_PE00178(ype00081) RHE_PF00005(rdh)
            RLE: RL0644(rbtD) pRL100461(rbtD) pRL90116
            BME: BMEII0980
            BMF: BAB2_0935
            BMS: BRA0268
            BMB: BruAb2_0912
            BJA: bll6662(rdh)
            BRA: BRADO6647(rbtD)
            BBT: BBta_0884(rbtD)
            RSP: RSP_3704
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.56
            ExPASy - ENZYME nomenclature database: 1.1.1.56
            ExplorEnz - The Enzyme Database: 1.1.1.56
            ERGO genome analysis and discovery system: 1.1.1.56
            BRENDA, the Enzyme Database: 1.1.1.56
            CAS: 9014-23-7
///
ENTRY       EC 1.1.1.57                 Enzyme
NAME        fructuronate reductase;
            mannonate oxidoreductase;
            mannonic dehydrogenase;
            D-mannonate dehydrogenase;
            D-mannonate:NAD+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-mannonate:NAD+ 5-oxidoreductase
REACTION    D-mannonate + NAD+ = D-fructuronate + NADH + H+ [RN:R02454]
ALL_REAC    R02454
SUBSTRATE   D-mannonate [CPD:C00514];
            NAD+ [CPD:C00003]
PRODUCT     D-fructuronate [CPD:C00905];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also reduces D-tagaturonate.
REFERENCE   1
  AUTHORS   Hickman, J. and Ashwell, G.
  TITLE     Uronic acid metabolism in bacteria. II. Purification and properties
            of D-altronic acid and D-mannonic acid dehyrogenases in Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 235 (1960) 1566-1570.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:14409051]
  AUTHORS   KILGORE WW, STARR MP.
  TITLE     Catabolism of galacturonic and glucuronic acids by Erwinia
            carotovora.
  JOURNAL   J. Biol. Chem. 234 (1959) 2227-35.
  ORGANISM  Erwinia carotovora [GN:eca]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K00040  fructuronate reductase
GENES       ECO: b4323(uxuB)
            ECJ: JW4286(uxuB)
            ECE: Z5921(uxuB)
            ECS: ECs5282
            ECC: c5403(uxuB)
            ECI: UTI89_C5019(uxuB)
            ECP: ECP_4659
            ECV: APECO1_2108(uxuB)
            STY: STY1553 STY3307(uxuB)
            STT: t3057(uxuB)
            SPT: SPA1347(ydfI) SPA3004(uxuB)
            SEC: SC1525(ydfI) SC3077(uxuB)
            STM: STM1508(ydfI) STM3136
            YPE: YPO1280
            YPK: y2903
            YPM: YP_1309(mtlD1)
            YPA: YPA_0998
            YPN: YPN_2696
            YPS: YPTB1314
            SFL: SF4197(uxuB)
            SFX: S4453(uxuB)
            SFV: SFV_4203(uxuB)
            SSN: SSON_4478(uxuB)
            SBO: SBO_4374(uxuB)
            ECA: ECA0819(uxuB)
            PLU: plu0175(uxuB)
            SGL: SG1837
            XCC: XCC4107(mtlD)
            XCB: XC_4198
            XCV: XCV4338(mtlD)
            XAC: XAC4232(mtlD)
            XOO: XOO4424(mtlD)
            XOM: XOO_4167(XOO4167)
            VVU: VV2_1069
            VVY: VVA1593
            VPA: VPA1705
            PPR: PBPRB1880
            PSP: PSPPH_2593(uxuB)
            PMY: Pmen_4472
            PHA: PSHAb0208(uxuB)
            CSA: Csal_2979
            BMA: BMAA0768
            BPS: BPSS1476
            BPM: BURPS1710b_A0508
            POL: Bpro_3970
            SME: SMb20749(uxuB)
            ATU: Atu3530(uxuB)
            ATC: AGR_L_2604
            RET: RHE_CH00089(uxuB)
            RLE: RL0098
            BME: BMEII0478
            BMF: BAB2_0426
            BMB: BruAb2_0421
            BJA: blr6836(uxuB)
            BBT: BBta_2118
            SIL: SPO1724(uxuB)
            SIT: TM1040_3866
            RSP: RSP_0480(uxuB)
            RSH: Rsph17029_2132
            RSQ: Rsph17025_2405
            RDE: RD1_2933(uxuB)
            GTN: GTNG_1763(uxuB)
            LLA: L0241(uxuB)
            LLC: LACR_1746
            LLM: llmg_0858(uxuB)
            SPH: MGAS10270_Spy1169
            LBR: LVIS_0139
            MTA: Moth_0429
            MSM: MSMEG_5576
            CEF: CE2378
            RHA: RHA1_ro02788
            SEN: SACE_4940 SACE_5054(mtlD)
            RBA: RB2403(uxuB)
            TMA: TM0068
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.57
            ExPASy - ENZYME nomenclature database: 1.1.1.57
            ExplorEnz - The Enzyme Database: 1.1.1.57
            ERGO genome analysis and discovery system: 1.1.1.57
            BRENDA, the Enzyme Database: 1.1.1.57
            CAS: 9028-44-8
///
ENTRY       EC 1.1.1.58                 Enzyme
NAME        tagaturonate reductase;
            altronic oxidoreductase;
            altronate oxidoreductase;
            TagUAR;
            altronate dehydrogenase;
            D-tagaturonate reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-altronate:NAD+ 3-oxidoreductase
REACTION    D-altronate + NAD+ = D-tagaturonate + NADH + H+ [RN:R02555]
ALL_REAC    R02555
SUBSTRATE   D-altronate [CPD:C00817];
            NAD+ [CPD:C00003]
PRODUCT     D-tagaturonate [CPD:C00558];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Hickman, J. and Ashwell, G.
  TITLE     Uronic acid metabolism in bacteria. II. Purification and properties
            of D-altronic acid and D-mannonic acid dehyrogenases in Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 235 (1960) 1566-1570.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K00041  tagaturonate reductase
GENES       ECO: b1521(uxaB)
            ECJ: JW1514(uxaB)
            ECE: Z2184(uxaB)
            ECS: ECs2128
            ECI: UTI89_C1740(uxaB)
            ECP: ECP_1505
            ECV: APECO1_641(uxaB)
            ECW: EcE24377A_1721(uxaB)
            ECX: EcHS_A1603(uxaB)
            YPE: YPO0580(uxaB)
            YPK: y3599(uxaB)
            YPM: YP_2900(uxaB)
            YPA: YPA_3208 YPA_3209
            YPN: YPN_0449
            YPS: YPTB3477(uxaB)
            YPI: YpsIP31758_0492(uxaB)
            SFL: SF1572(uxaB)
            SFX: S1699(uxaB)
            SFV: SFV_1580(uxaB)
            SSN: SSON_1607(uxaB)
            ECA: ECA0646(uxaB1) ECA4383(uxaB2)
            MSU: MS0529(mtlD)
            PPR: PBPRB1516
            BAM: Bamb_1222
            BBA: Bd3477
            ATU: Atu2813(uxaB)
            ATC: AGR_C_5101
            BSU: BG13212(uxaB)
            BHA: BH0492
            BLI: BL00711(uxaB)
            BLD: BLi03513(uxaB)
            BCL: ABC0443(uxaB) ABC1154
            BAY: RBAM_012410(uxaB)
            BPU: BPUM_2985(uxaB)
            CAC: CAC0695
            BTH: BT_0825
            GFO: GFO_1705(uxaB)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.58
            ExPASy - ENZYME nomenclature database: 1.1.1.58
            ExplorEnz - The Enzyme Database: 1.1.1.58
            ERGO genome analysis and discovery system: 1.1.1.58
            BRENDA, the Enzyme Database: 1.1.1.58
            CAS: 9028-45-9
///
ENTRY       EC 1.1.1.59                 Enzyme
NAME        3-hydroxypropionate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-hydroxypropanoate:NAD+ oxidoreductase
REACTION    3-hydroxypropanoate + NAD+ = 3-oxopropanoate + NADH + H+ [RN:R01608]
ALL_REAC    R01608
SUBSTRATE   3-hydroxypropanoate [CPD:C01013];
            NAD+ [CPD:C00003]
PRODUCT     3-oxopropanoate [CPD:C00222];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Den, H., Robinson, W.G. and Coon, M.J.
  TITLE     Enzymatic conversion of beta-hydroxypropionate to malonic
            semialdehyde.
  JOURNAL   J. Biol. Chem. 234 (1959) 1666-1671.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00410  beta-Alanine metabolism
            PATH: map00640  Propanoate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.59
            ExPASy - ENZYME nomenclature database: 1.1.1.59
            ExplorEnz - The Enzyme Database: 1.1.1.59
            ERGO genome analysis and discovery system: 1.1.1.59
            BRENDA, the Enzyme Database: 1.1.1.59
            CAS: 9028-59-5
///
ENTRY       EC 1.1.1.60                 Enzyme
NAME        2-hydroxy-3-oxopropionate reductase;
            tartronate semialdehyde reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-glycerate:NAD(P)+ oxidoreductase
REACTION    (R)-glycerate + NAD(P)+ = 2-hydroxy-3-oxopropanoate + NAD(P)H + H+
            [RN:R01745 R01747]
ALL_REAC    R01745 R01747
SUBSTRATE   (R)-glycerate [CPD:C00258];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     2-hydroxy-3-oxopropanoate [CPD:C01146];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13900766]
  AUTHORS   GOTTO AM, KORNBERG HL.
  TITLE     The metabolism of C2 compounds in micro-organisms. 7. Preparation
            and properties of crystalline tartronic semialdehyde reductase.
  JOURNAL   Biochem. J. 81 (1961) 273-84.
  ORGANISM  Pseudomonas ovalis
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K00042  2-hydroxy-3-oxopropionate reductase
GENES       TET: TTHERM_00655560
            TCR: 505807.180 507017.40
            LMA: LmjF30.0180
            ECO: b0509(glxR) b3125(garR)
            ECJ: JW0497(glxR) JW5526(garR)
            ECE: Z0663(ybbQ) Z4477(yhaE)
            ECS: ECs0570 ECs4003
            ECC: c0624(ybbQ) c3880(yhaE)
            ECI: UTI89_C0538(ybbQ) UTI89_C3556(yhaE)
            ECP: ECP_0570 ECP_3215
            ECV: APECO1_1505(ybbQ) APECO1_3302(yhaE)
            ECW: EcE24377A_3603(garR)
            ECX: EcHS_A3314(garR)
            STY: STY0567(garR) STY3430(garR)
            STT: t2341(garR) t3168(garR)
            SPT: SPA2203 SPA3117(garR)
            SEC: SC0559(glxR) SC3195(garR)
            STM: STM0519(glxR) STM3248(garR)
            YPE: YPO3648
            YPK: y0219
            YPM: YP_3899(mmsB)
            YPN: YPN_3523
            YPS: YPTB3582
            SFL: SF3162(yhaE)
            SFX: S3377(yhaE)
            SFV: SFV_3165(yhaE)
            SSN: SSON_3280(yhaE)
            SBO: SBO_2990(yhaE)
            SDY: SDY_3319(yhaE)
            ECA: ECA0489 ECA3573(garR)
            SGL: SG0507
            ENT: Ent638_3567
            SPE: Spro_1492
            MSU: MS0692(mmsB)
            ASU: Asuc_0552 Asuc_1858
            VCO: VC0395_0123(garR)
            PPR: PBPRA2273
            PAE: PA1500
            PAU: PA14_45020(glxR)
            PAP: PSPA7_3831
            PPU: PP_4299(glxR)
            PPF: Pput_1570
            PFL: PFL_1699
            PFO: Pfl_1596
            PEN: PSEEN1670(glxR)
            PMY: Pmen_2771
            SDN: Sden_2289
            SFR: Sfri_1503
            PHA: PSHAa1254
            PIN: Ping_3356
            MAQ: Maqu_3742
            HCH: HCH_00576
            ABO: ABO_1232(yhaE)
            MMW: Mmwyl1_2549
            CVI: CV_3870
            RSO: RSc2429(RS02679) RSc3283(glxR)
            REU: Reut_A1500 Reut_A2701 Reut_A3293
            REH: H16_A3600
            RME: Rmet_1632 Rmet_2821 Rmet_3450
            BMA: BMAA0577(garR)
            BML: BMA10299_0890(garR)
            BMN: BMA10247_A1857(garR)
            BXE: Bxe_A2462 Bxe_B0972 Bxe_B0974 Bxe_C0957
            BVI: Bcep1808_1804 Bcep1808_1879
            BUR: Bcep18194_A5180 Bcep18194_A5264
            BCN: Bcen_6125 Bcen_6199
            BCH: Bcen2424_1880 Bcen2424_1953
            BAM: Bamb_1817 Bamb_1940
            BPS: BPSL1450(glxR) BPSS1415
            BPM: BURPS1710b_2426
            BPL: BURPS1106A_2301 BURPS1106A_A1920(garR)
            BPD: BURPS668_2261
            BTE: BTH_I2171 BTH_II0977
            PNU: Pnuc_0594 Pnuc_0958
            BPE: BP1169
            BPA: BPP1597 BPP3639
            BBR: BB2674 BB4074
            RFR: Rfer_0430 Rfer_3038
            POL: Bpro_0394 Bpro_1712 Bpro_3102 Bpro_4563
            PNA: Pnap_0274 Pnap_1600
            VEI: Veis_1704
            MPT: Mpe_A0975 Mpe_A2972
            HAR: HEAR0334(glxR)
            MMS: mma_0270(garR1) mma_0381(garR2)
            NEU: NE0676
            NET: Neut_1881
            NMU: Nmul_A0172
            EBA: ebA3883(tsaR) ebA3884
            AZO: azo3362(glxR1) azo3363(glxR2)
            DAR: Daro_3339 Daro_3340
            TBD: Tbd_0081
            GUR: Gura_0588 Gura_2805
            PPD: Ppro_2197
            MLO: mlr0254
            MES: Meso_4460
            SME: SMa0237 SMb20679(glxR)
            SMD: Smed_2487 Smed_4310 Smed_5561
            ATU: Atu2737
            ATC: AGR_C_4961
            RLE: RL3773 RL3800
            OAN: Oant_0460 Oant_3760
            BJA: blr3168
            BRA: BRADO6761(garR)
            XAU: Xaut_2369 Xaut_2433
            SIL: SPO2560(garR)
            RDE: RD1_0672(garR) RD1_0684(glxR)
            SWI: Swit_3270 Swit_4279
            GBE: GbCGDNIH1_0961
            ACR: Acry_1159 Acry_1592
            ABA: Acid345_1903
            SUS: Acid_3982
            BCA: BCE_2381(garR) BCE_4109
            BLD: BLi02105
            BPU: BPUM_3559
            CPF: CPF_0381(garR)
            CDF: CD2813(garR)
            DSY: DSY4169
            MSM: MSMEG_5477
            RHA: RHA1_ro02575 RHA1_ro03224 RHA1_ro04661
            SCO: SCO6205(SC2G5.26c)
            SMA: SAV2025(garR)
            ART: Arth_2453 Arth_3602
            AAU: AAur_2423 AAur_3507
            TFU: Tfu_1265
            SEN: SACE_1936 SACE_5376(glxR) SACE_6730
            RXY: Rxyl_1714 Rxyl_2852
            SYW: SYNW2331
            SYE: Syncc9902_2145
            AVA: Ava_3206
            PMN: PMN2A_0231
            PMF: P9303_27951(mmsB)
            PME: NATL1_08981(mmsB)
            DGE: Dgeo_2614
            PTO: PTO1147
STRUCTURES  PDB: 1YB4  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.60
            ExPASy - ENZYME nomenclature database: 1.1.1.60
            ExplorEnz - The Enzyme Database: 1.1.1.60
            ERGO genome analysis and discovery system: 1.1.1.60
            BRENDA, the Enzyme Database: 1.1.1.60
            CAS: 9028-68-6
///
ENTRY       EC 1.1.1.61                 Enzyme
NAME        4-hydroxybutyrate dehydrogenase;
            gamma-hydroxybutyrate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4-hydroxybutanoate:NAD+ oxidoreductase
REACTION    4-hydroxybutanoate + NAD+ = succinate semialdehyde + NADH + H+
            [RN:R01644]
ALL_REAC    R01644
SUBSTRATE   4-hydroxybutanoate [CPD:C00989];
            NAD+ [CPD:C00003]
PRODUCT     succinate semialdehyde [CPD:C00232];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Nirenberg, M.W. and Jakoby, W.B.
  TITLE     Enzymatic utilization of gamma-hydroxybutyric acid.
  JOURNAL   J. Biol. Chem. 235 (1960) 954-960.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K00043  4-hydroxybutyrate dehydrogenase
GENES       RSO: RSp0986(gbd2)
            REH: H16_A1553(gbd)
            BMA: BMAA0572
            BPM: BURPS1710b_1823(gbd1)
            BPA: BPP2084(gbd)
            BBR: BB1480(gbd)
            BME: BMEII1094
            RDE: RD1_2171(gbd)
            HNE: HNE_0174(gbd)
            CPF: CPF_0518
            CPR: CPR_0507
            CDF: CD2338(abfH)
            CKL: CKL_3014(4hbD)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.61
            ExPASy - ENZYME nomenclature database: 1.1.1.61
            ExplorEnz - The Enzyme Database: 1.1.1.61
            ERGO genome analysis and discovery system: 1.1.1.61
            BRENDA, the Enzyme Database: 1.1.1.61
            CAS: 9028-60-8
///
ENTRY       EC 1.1.1.62                 Enzyme
NAME        estradiol 17beta-dehydrogenase;
            20alpha-hydroxysteroid dehydrogenase;
            17beta,20alpha-hydroxysteroid dehydrogenase;
            17beta-estradiol dehydrogenase;
            estradiol dehydrogenase;
            estrogen 17-oxidoreductase;
            17beta-HSD
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     estradiol-17beta:NAD(P)+ 17-oxidoreductase
REACTION    estradiol-17beta + NAD(P)+ = estrone + NAD(P)H + H+ [RN:R02352
            R02353]
ALL_REAC    R02352 R02353;
            (other) R04681 R04682
SUBSTRATE   estradiol-17beta [CPD:C00951];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     estrone [CPD:C00468];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on (S)-20-hydroxypregn-4-en-3-one and related compounds,
            oxidizing the (S)-20-group. B-specific with respect to NAD(P)+ (cf.
            EC 1.1.1.149 20alpha-hydroxysteroid dehydrogenase).
REFERENCE   1  [PMID:4314937]
  AUTHORS   Kautsky MP, Hagerman DD.
  TITLE     17 Beta-estradiol dehydrogenase of ovine ovaries.
  JOURNAL   J. Biol. Chem. 245 (1970) 1978-84.
  ORGANISM  sheep
REFERENCE   2  [PMID:14413943]
  AUTHORS   LANGER LJ, ALEXANDER JA, ENGEL LL.
  TITLE     Human placental estradiol-17 beta dehydrogenase. II. Kinetics and
            substrate specificities.
  JOURNAL   J. Biol. Chem. 234 (1959) 2609-14.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00150  Androgen and estrogen metabolism
ORTHOLOGY   KO: K00044  estradiol 17beta-dehydrogenase
GENES       HSA: 3292(HSD17B1) 3294(HSD17B2) 51144(HSD17B12) 51478(HSD17B7)
                 7923(HSD17B8)
            PTR: 454269(HSD17B2) 454689(HSD17B1) 466046(LOC466046)
                 741010(HSD17B12) 746685(HSD17B8)
            MMU: 14979(H2-Ke6) 15485(Hsd17b1) 15486(Hsd17b2) 15490(Hsd17b7)
                 56348(Hsd17b12)
            RNO: 25322(Hsd17b1) 29540(Hsd17b7) 361802(Hsd17b8) 79243(Hsd17b2)
                 84013(Hsd17b12)
            CFA: 489690(HSD17B2) 607570(HSD17B1) 607895(HSD17B8)
                 609364(HSD17B7)
            BTA: 353107(HSD17B1) 532422(HKE6) 616219(HSD17B12)
            GGA: 395641(LOC395641) 415807(HSD17B2) 424367(HSD17B7)
            XLA: 379747(let-767co) 495218(LOC495218)
            XTR: 548963(hsd17b7) 549988(LOC549988)
            DRE: 322626(hsd17b12b) 327417(hsd17b12a) 402842(hsd17b1)
            PIC: PICST_40664(PXP18)
            TET: TTHERM_00024130 TTHERM_00024140 TTHERM_00024170
                 TTHERM_00024180 TTHERM_00024190 TTHERM_00024200
                 TTHERM_00418230 TTHERM_00802430
            BUR: Bcep18194_A3871 Bcep18194_A5812 Bcep18194_B0662
                 Bcep18194_B1144 Bcep18194_B1176 Bcep18194_B1177
                 Bcep18194_B1706
            MMS: mma_3088
            RET: RHE_PF00466
            RLE: RL3778
            BRA: BRADO4879
            BBT: BBta_3170
            RDE: RD1_2502
            MSM: MSMEG_3112
            AVA: Ava_1011
STRUCTURES  PDB: 1A27  1BHS  1DHT  1EQU  1FDS  1FDT  1FDU  1FDV  1FDW  1GZ6  
                 1I5R  1IKT  1IOL  1JTV  1QYV  1QYW  1QYX  1S1P  1S1R  1S2A  
                 1S2C  1XF0  1YB1  1ZQ5  2F38  2FGB  2HQ1  2PD6  3DHE  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.62
            ExPASy - ENZYME nomenclature database: 1.1.1.62
            ExplorEnz - The Enzyme Database: 1.1.1.62
            ERGO genome analysis and discovery system: 1.1.1.62
            BRENDA, the Enzyme Database: 1.1.1.62
            CAS: 9028-61-9
///
ENTRY       EC 1.1.1.63                 Enzyme
NAME        testosterone 17beta-dehydrogenase;
            17-ketoreductase;
            17beta-HSD
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     17beta-hydroxysteroid:NAD+ 17-oxidoreductase
REACTION    testosterone + NAD+ = androst-4-ene-3,17-dione + NADH + H+
            [RN:R01836]
ALL_REAC    R01836
SUBSTRATE   testosterone [CPD:C00535];
            NAD+ [CPD:C00003]
PRODUCT     androst-4-ene-3,17-dione [CPD:C00280];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13696735]
  AUTHORS   ENDAHL GL, KOCHAKIAN CD, HAMM D.
  TITLE     Separation of a triphosphopyridine nucleotide-specific from a
            diphosphopyridine nucleotide-specific 17 beta-hydroxy-(testosterone)
            dehydrogenase of guinea pig liver.
  JOURNAL   J. Biol. Chem. 235 (1960) 2792-6.
  ORGANISM  guinea pig
REFERENCE   2  [PMID:15436478]
  AUTHORS   SWEAT ML, SAMUELS LT, LUMRY R.
  TITLE     Preparation and characterization of the enzyme which converts
            testosterone to androstenedione.
  JOURNAL   J. Biol. Chem. 185 (1950) 75-84.
  ORGANISM  cow [GN:bta]
REFERENCE   3
  AUTHORS   Villee, C.A. and Spencer, J.M.
  TITLE     Some properties of the pyridine nucleotide-specific 17beta-hydroxy
            steroid dehydrogenase of guinea pig liver.
  JOURNAL   J. Biol. Chem. 235 (1960) 3615-3619.
  ORGANISM  guinea pig
PATHWAY     PATH: map00150  Androgen and estrogen metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.63
            ExPASy - ENZYME nomenclature database: 1.1.1.63
            ExplorEnz - The Enzyme Database: 1.1.1.63
            ERGO genome analysis and discovery system: 1.1.1.63
            BRENDA, the Enzyme Database: 1.1.1.63
            CAS: 9028-62-0
///
ENTRY       EC 1.1.1.64                 Enzyme
NAME        testosterone 17beta-dehydrogenase (NADP+);
            17-ketoreductase;
            NADP+-dependent testosterone-17beta-oxidoreductase;
            testosterone 17beta-dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     17beta-hydroxysteroid:NADP+ 17-oxidoreductase
REACTION    testosterone + NADP+ = androst-4-ene-3,17-dione + NADPH + H+
            [RN:R01838]
ALL_REAC    R01838
SUBSTRATE   testosterone [CPD:C00535];
            NADP+ [CPD:C00006]
PRODUCT     androst-4-ene-3,17-dione [CPD:C00280];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also oxidizes 3-hydroxyhexobarbital to 3-oxohexobarbital.
REFERENCE   1  [PMID:13696735]
  AUTHORS   ENDAHL GL, KOCHAKIAN CD, HAMM D.
  TITLE     Separation of a triphosphopyridine nucleotide-specific from a
            diphosphopyridine nucleotide-specific 17 beta-hydroxy-(testosterone)
            dehydrogenase of guinea pig liver.
  JOURNAL   J. Biol. Chem. 235 (1960) 2792-6.
  ORGANISM  guinea pig
REFERENCE   2  [PMID:15436478]
  AUTHORS   SWEAT ML, SAMUELS LT, LUMRY R.
  TITLE     Preparation and characterization of the enzyme which converts
            testosterone to androstenedione.
  JOURNAL   J. Biol. Chem. 185 (1950) 75-84.
  ORGANISM  cow [GN:bta]
REFERENCE   3
  AUTHORS   Villee, C.A. and Spencer, J.M.
  TITLE     Some properties of the pyridine nucleotide-specific 17beta-hydroxy
            steroid dehydrogenase of guinea pig liver.
  JOURNAL   J. Biol. Chem. 235 (1960) 3615-3619.
  ORGANISM  guinea pig
PATHWAY     PATH: map00150  Androgen and estrogen metabolism
ORTHOLOGY   KO: K10207  testosterone 17beta-dehydrogenase (NADP+)
GENES       HSA: 3293(HSD17B3)
            PTR: 742116(HSD17B3)
            MMU: 15487(Hsd17b3)
            RNO: 117182(Hsd17b3)
            CFA: 606956(HSD17B3)
            BTA: 616934(HSD17B3)
            TET: TTHERM_00706280
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.64
            ExPASy - ENZYME nomenclature database: 1.1.1.64
            ExplorEnz - The Enzyme Database: 1.1.1.64
            ERGO genome analysis and discovery system: 1.1.1.64
            BRENDA, the Enzyme Database: 1.1.1.64
            CAS: 9028-63-1
///
ENTRY       EC 1.1.1.65                 Enzyme
NAME        pyridoxine 4-dehydrogenase;
            pyridoxin dehydrogenase;
            pyridoxol dehydrogenase;
            pyridoxine dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     pyridoxine:NADP+ 4-oxidoreductase
REACTION    pyridoxine + NADP+ = pyridoxal + NADPH + H+ [RN:R01708]
ALL_REAC    R01708
SUBSTRATE   pyridoxine [CPD:C00314];
            NADP+ [CPD:C00006]
PRODUCT     pyridoxal [CPD:C00250];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also oxidizes pyridoxine phosphate.
REFERENCE   1  [PMID:13715611]
  AUTHORS   HOLZER H, SCHNEIDER S.
  TITLE     [Purification and characterization of a TPN-dependent pyridoxol
            dehydrogenase from brewers yeast.]
  JOURNAL   Biochim. Biophys. Acta. 48 (1961) 71-6.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00750  Vitamin B6 metabolism
ORTHOLOGY   KO: K05275  pyridoxine 4-dehydrogenase
GENES       PIC: PICST_59193(PLR1)
            SPO: SPAC9E9.11(plr)
            AFM: AFUA_1G10270
            CNE: CNA00960
            TET: TTHERM_00962020 TTHERM_00962050 TTHERM_00962060
                 TTHERM_00962070 TTHERM_00962090 TTHERM_01311290
            BUR: Bcep18194_B1236 Bcep18194_B2855
            RLE: RL2735 RL3415
            RPC: RPC_0451
            RDE: RD1_3755
            RRU: Rru_A1059 Rru_A2876
            FRA: Francci3_1517
            SEN: SACE_3303
            AVA: Ava_0134
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.65
            ExPASy - ENZYME nomenclature database: 1.1.1.65
            ExplorEnz - The Enzyme Database: 1.1.1.65
            ERGO genome analysis and discovery system: 1.1.1.65
            BRENDA, the Enzyme Database: 1.1.1.65
            CAS: 9028-64-2
///
ENTRY       EC 1.1.1.66                 Enzyme
NAME        omega-hydroxydecanoate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     10-hydroxydecanoate:NAD+ 10-oxidoreductase
REACTION    10-hydroxydecanoate + NAD+ = 10-oxodecanoate + NADH + H+ [RN:R03886]
ALL_REAC    R03886
SUBSTRATE   10-hydroxydecanoate [CPD:C02774];
            NAD+ [CPD:C00003]
PRODUCT     10-oxodecanoate [CPD:C02217];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts, more slowly, on 9-hydroxynonanoate and
            11-hydroxyundecanoate.
REFERENCE   1
  AUTHORS   Kamei, S., Wakabayashi, K. and Shimazono, M.
  TITLE     omega-Oxidation of fatty acids in vitro. II. omega-Hydroxy fatty
            acid-NAD oxidoreductase.
  JOURNAL   J. Biochem. (Tokyo) 56 (1964) 72-76.
  ORGANISM  rabbit
REFERENCE   2
  AUTHORS   Mitz, M.A. and Henrikson, R.L.
  TITLE     Omega hydroxy fatty acid dehydrogenase.
  JOURNAL   Biochim. Biophys. Acta 46 (1961) 45-50.
  ORGANISM  pig [GN:ssc], sheep, rat [GN:rno], horse
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.66
            ExPASy - ENZYME nomenclature database: 1.1.1.66
            ExplorEnz - The Enzyme Database: 1.1.1.66
            ERGO genome analysis and discovery system: 1.1.1.66
            BRENDA, the Enzyme Database: 1.1.1.66
            CAS: 9028-65-3
///
ENTRY       EC 1.1.1.67                 Enzyme
NAME        mannitol 2-dehydrogenase;
            D-mannitol dehydrogenase;
            mannitol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-mannitol:NAD+ 2-oxidoreductase
REACTION    D-mannitol + NAD+ = D-fructose + NADH + H+ [RN:R00868]
ALL_REAC    R00868
SUBSTRATE   D-mannitol [CPD:C00392];
            NAD+ [CPD:C00003]
PRODUCT     D-fructose [CPD:C00095];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Martinez, G., Barker, H.A. and Horecker, B.L.
  TITLE     A specific mannitol dehydrogenase from Lactobacillus brevis.
  JOURNAL   J. Biol. Chem. 238 (1963) 1598-1603.
  ORGANISM  Lactobacillus brevis [GN:lbr]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K00045  mannitol 2-dehydrogenase
GENES       PEN: PSEEN1989(mltD)
            MLO: mll4920 mlr4057
            SME: SMc01501(mtlK)
            ATU: Atu4451(mtlK)
            ATC: AGR_L_830
            RET: RHE_CH03678(mtlK)
            RLE: RL4214(mtlK)
            CCR: CC_1487
            SIT: TM1040_0426
            RSP: RSP_0096(mtlK)
            RDE: RD1_1481(mtlK)
            MPA: MAP3809c
            MAV: MAV_1052 MAV_4838
            CGL: NCgl0108(cgl0109)
            CGB: cg0143(mtlD)
            RHA: RHA1_ro02810
            DGE: Dgeo_2866
STRUCTURES  PDB: 1LJ8  1M2W  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.67
            ExPASy - ENZYME nomenclature database: 1.1.1.67
            ExplorEnz - The Enzyme Database: 1.1.1.67
            ERGO genome analysis and discovery system: 1.1.1.67
            BRENDA, the Enzyme Database: 1.1.1.67
            CAS: 9001-65-4
///
ENTRY       EC 1.1.1.68       Obsolete  Enzyme
NAME        Transferred to 1.5.1.20
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Transferred entry: now EC 1.5.1.20, methylenetetrahydrofolate
            reductase [NAD(P)H] (EC 1.1.1.68 created 1965, deleted 1978
            [transferred to EC 1.1.99.15, deleted 1980])
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.68
            ExPASy - ENZYME nomenclature database: 1.1.1.68
            ExplorEnz - The Enzyme Database: 1.1.1.68
            ERGO genome analysis and discovery system: 1.1.1.68
            BRENDA, the Enzyme Database: 1.1.1.68
///
ENTRY       EC 1.1.1.69                 Enzyme
NAME        gluconate 5-dehydrogenase;
            5-keto-D-gluconate 5-reductase;
            5-keto-D-gluconate 5-reductase;
            5-ketogluconate 5-reductase;
            5-ketogluconate reductase;
            5-keto-D-gluconate reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-gluconate:NAD(P)+ 5-oxidoreductase
REACTION    D-gluconate + NAD(P)+ = 5-dehydro-D-gluconate + NAD(P)H + H+
            [RN:R01738 R01740]
ALL_REAC    R01738 R01740
SUBSTRATE   D-gluconate [CPD:C00257];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     5-dehydro-D-gluconate [CPD:C01062];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Ameyama, M. and Adachi, O.
  TITLE     5-Keto-D-gluconate reductase from Gluconobacter suboxydans.
  JOURNAL   Methods Enzymol. 89 (1982) 198-202.
  ORGANISM  Gluconobacter suboxydans
REFERENCE   2  [PMID:16526094]
  AUTHORS   Foucher AL, McIntosh A, Douce G, Wastling J, Tait A, Turner CM.
  TITLE     A proteomic analysis of arsenical drug resistance in Trypanosoma
            brucei.
  JOURNAL   Proteomics. 6 (2006) 2726-32.
REFERENCE   3
  AUTHORS   Okamoto, K.
  TITLE     Enzymic studies on the formation of 5-ketogluconic acid by
            Acetobacter suboxydans. II. 5-Ketogluconate reductase.
  JOURNAL   J. Biochem. (Tokyo) 53 (1963) 448.
  ORGANISM  Acetobacter suboxydans
ORTHOLOGY   KO: K00046  gluconate 5-dehydrogenase
GENES       AFM: AFUA_1G14540 AFUA_1G17380 AFUA_4G13550 AFUA_5G08900
                 AFUA_6G09970 AFUA_6G10820 AFUA_6G13830 AFUA_7G04540
            UMA: UM00108.1
            ECO: b4266(idnO)
            ECJ: JW4223(idnO)
            ECC: c0321 c5367(idnO)
            ECI: UTI89_C4873(idnO)
            ECP: ECP_4515
            ECV: APECO1_2128(idnO)
            ECX: EcHS_A4522
            SPT: SPA4283(idnO)
            SEC: SC4339(idnO)
            STM: STM4483(idnO)
            YPE: YPO2539(idnO)
            YPK: y1645
            YPM: YP_2350(idnO)
            YPA: YPA_2031
            YPN: YPN_2134
            YPS: YPTB2571(idnO)
            YPI: YpsIP31758_1470(idnO)
            SSN: SSON_4451(idnO)
            SGL: SG1773
            MSU: MS0955(fabG)
            PFO: Pfl_2753
            SDE: Sde_0949
            CSA: Csal_1129
            RSO: RSp0947(idnO)
            REU: Reut_C6091
            RME: Rmet_5878
            BXE: Bxe_A2748
            BUR: Bcep18194_A3725
            BCH: Bcen2424_0641
            BTE: BTH_II0349
            BPE: BP0464(idnO)
            BPA: BPP4378(idnO)
            BBR: BB1512 BB4964(idnO)
            POL: Bpro_3524
            MLO: mlr3785
            SME: SMa0513(idnO1) SMb20692(idnO1) SMb20750
            ATU: Atu1407 Atu2417 Atu4086(idnO)
            ATC: AGR_C_2598 AGR_C_4386 AGR_L_1541
            RET: RHE_PC00144(idnO)
            RLE: RL2835 pRL100391(gno) pRL110084(gno) pRL80037
            BJA: blr5277
            BRA: BRADO6762(idnO)
            BBT: BBta_0777(idnO)
            CCR: CC_1286
            SIL: SPO0595(gno) SPO2417(idnO)
            RSP: RSP_2160(gno) RSP_7371
            RDE: RD1_1109(idnO) RD1_3809(gno) RD1_3945
            GOX: GOX2187
            BCZ: pE33L466_0134
            SPY: SPy_0636(idnO)
            SPZ: M5005_Spy_0524(idnO)
            SPM: spyM18_0699
            SPG: SpyM3_0448
            SPS: SPs1408
            SPF: SpyM51339(idnO)
            SPA: M6_Spy0545
            SPB: M28_Spy0503(idnO)
            SPN: SP_0320
            SPR: spr0290(gno)
            SAG: SAG1904
            SAN: gbs1891
            EFA: EF0426 EF2263
            CAC: CAC2607
            MSM: MSMEG_3420
            RHA: RHA1_ro03299(gno)
            SCO: SCO1681(SCI30A.02)
            SMA: SAV6627(kduD)
            AAU: AAur_2422
            FNU: FN1687
            RBA: RB6802
            BTH: BT_3232
            BFR: BF0072
            BFS: BF0083(gno)
            TTH: TTC0235
            MAC: MA0107(gno)
STRUCTURES  PDB: 1VL8  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.69
            ExPASy - ENZYME nomenclature database: 1.1.1.69
            ExplorEnz - The Enzyme Database: 1.1.1.69
            ERGO genome analysis and discovery system: 1.1.1.69
            BRENDA, the Enzyme Database: 1.1.1.69
            CAS: 9028-70-0
///
ENTRY       EC 1.1.1.70       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: D-glucuronolactone dehydrogenase. Now included with
            EC 1.2.1.3 aldehyde dehydrogenase (NAD+) (EC 1.1.1.70 created 1965,
            deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.70
            ExPASy - ENZYME nomenclature database: 1.1.1.70
            ExplorEnz - The Enzyme Database: 1.1.1.70
            ERGO genome analysis and discovery system: 1.1.1.70
            BRENDA, the Enzyme Database: 1.1.1.70
///
ENTRY       EC 1.1.1.71                 Enzyme
NAME        alcohol dehydrogenase [NAD(P)+];
            retinal reductase;
            aldehyde reductase (NADPH/NADH);
            alcohol dehydrogenase [NAD(P)]
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     alcohol:NAD(P)+ oxidoreductase
REACTION    an alcohol + NAD(P)+ = an aldehyde + NAD(P)H + H+ [RN:R07326 R07328]
ALL_REAC    R07326 > R00623 R00754;
            R07328 > R00625 R00746
SUBSTRATE   alcohol [CPD:C00069];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     aldehyde [CPD:C00071];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Reduces aliphatic aldehydes of carbon chain length from 2 to 14,
            with greatest activity on C4, C6 and C8 aldehydes; also reduces
            retinal to retinol.
REFERENCE   1  [PMID:4300551]
  AUTHORS   Fidge NH, Goodman DS.
  TITLE     The enzymatic reducation of retinal to retinol in rat intestine.
  JOURNAL   J. Biol. Chem. 243 (1968) 4372-9.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.71
            ExPASy - ENZYME nomenclature database: 1.1.1.71
            ExplorEnz - The Enzyme Database: 1.1.1.71
            ERGO genome analysis and discovery system: 1.1.1.71
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.71
            BRENDA, the Enzyme Database: 1.1.1.71
            CAS: 37250-10-5
///
ENTRY       EC 1.1.1.72                 Enzyme
NAME        glycerol dehydrogenase (NADP+);
            glycerol dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     glycerol:NADP+ oxidoreductase
REACTION    glycerol + NADP+ = D-glyceraldehyde + NADPH + H+ [RN:R01041]
ALL_REAC    R01041;
            (other) R01036
SUBSTRATE   glycerol [CPD:C00116];
            NADP+ [CPD:C00006]
PRODUCT     D-glyceraldehyde [CPD:C00577];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4400494]
  AUTHORS   Kormann AW, Hurst RO, Flynn TG.
  TITLE     Purification and properties of an NADP + -dependent glycerol
            dehydrogenase from rabbit skeletal muscle.
  JOURNAL   Biochim. Biophys. Acta. 258 (1972) 40-55.
  ORGANISM  rabbit
REFERENCE   2
  AUTHORS   Toews, C.J.
  TITLE     The kinetics and reaction mechanism of the nicotinamide-adinine
            dinucleotide phosphate-specific glycerol dehydrogenase of rat
            skeletal muscle.
  JOURNAL   Biochem. J. 105 (1967) 1067-1073.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00561  Glycerolipid metabolism
GENES       AFM: AFUA_4G11730
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.72
            ExPASy - ENZYME nomenclature database: 1.1.1.72
            ExplorEnz - The Enzyme Database: 1.1.1.72
            ERGO genome analysis and discovery system: 1.1.1.72
            BRENDA, the Enzyme Database: 1.1.1.72
            CAS: 37250-11-6
///
ENTRY       EC 1.1.1.73                 Enzyme
NAME        octanol dehydrogenase;
            1-octanol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     octanol:NAD+ oxidoreductase
REACTION    1-octanol + NAD+ = 1-octanal + NADH + H+ [RN:R02878]
ALL_REAC    R02878
SUBSTRATE   1-octanol [CPD:C00756];
            NAD+ [CPD:C00003]
PRODUCT     1-octanal [CPD:C01545];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Acts, less rapidly, on other long-chain alcohols.
REFERENCE   1  [PMID:4308448]
  AUTHORS   Roche B, Azoulay E.
  TITLE     [Regulation of the alcohol dehydrogenases Saccharomyces cerevisiae]
  JOURNAL   Eur. J. Biochem. 8 (1969) 426-34.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K00047  octanol dehydrogenase
GENES       DME: Dmel_CG6598(Fdh)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.73
            ExPASy - ENZYME nomenclature database: 1.1.1.73
            ExplorEnz - The Enzyme Database: 1.1.1.73
            ERGO genome analysis and discovery system: 1.1.1.73
            BRENDA, the Enzyme Database: 1.1.1.73
            CAS: 9031-31-6
///
ENTRY       EC 1.1.1.74       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: D-aminopropanol dehydrogenase (reaction due to EC
            1.1.1.4 (R,R)-butanediol dehydrogenase) (EC 1.1.1.74 created 1972,
            deleted 1976)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.74
            ExPASy - ENZYME nomenclature database: 1.1.1.74
            ExplorEnz - The Enzyme Database: 1.1.1.74
            ERGO genome analysis and discovery system: 1.1.1.74
            BRENDA, the Enzyme Database: 1.1.1.74
///
ENTRY       EC 1.1.1.75                 Enzyme
NAME        (R)-aminopropanol dehydrogenase;
            L-aminopropanol dehydrogenase;
            1-aminopropan-2-ol-NAD+ dehydrogenase;
            L(+)-1-aminopropan-2-ol:NAD+ oxidoreductase;
            1-aminopropan-2-ol-dehydrogenase;
            DL-1-aminopropan-2-ol: NAD+ dehydrogenase;
            L(+)-1-aminopropan-2-ol-NAD+/NADP+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-1-aminopropan-2-ol:NAD+ oxidoreductase
REACTION    (R)-1-aminopropan-2-ol + NAD+ = aminoacetone + NADH + H+ [RN:R03759]
ALL_REAC    R03759
SUBSTRATE   (R)-1-aminopropan-2-ol [CPD:C03194];
            NAD+ [CPD:C00003]
PRODUCT     aminoacetone [CPD:C01888];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COFACTOR    Potassium [CPD:C00238]
COMMENT     Requires K+.
REFERENCE   1  [PMID:4385233]
  AUTHORS   Dekker EE, Swain RR.
  TITLE     Formation of Dg-1-amino-2-propanol by a highly purified enzyme from
            Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 158 (1968) 306-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:5329339]
  AUTHORS   Tuner JM.
  TITLE     Microbial metabolism of amino ketones. Aminoacetone formation from
            1-aminopropan-2-ol by a dehydrgenase in Escerichia coli.
  JOURNAL   Biochem. J. 99 (1966) 427-33.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:5340733]
  AUTHORS   Turner JM.
  TITLE     Microbial metabolism of amino ketones. L-1-aminopropan-2-ol
            dehydrogenase and L-threonine dehydrogenase in Escherichia coli.
  JOURNAL   Biochem. J. 104 (1967) 112-21.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.75
            ExPASy - ENZYME nomenclature database: 1.1.1.75
            ExplorEnz - The Enzyme Database: 1.1.1.75
            ERGO genome analysis and discovery system: 1.1.1.75
            BRENDA, the Enzyme Database: 1.1.1.75
            CAS: 37250-13-8
///
ENTRY       EC 1.1.1.76                 Enzyme
NAME        (S,S)-butanediol dehydrogenase;
            L-butanediol dehydrogenase;
            L-BDH;
            L(+)-2,3-butanediol dehydrogenase (L-acetoin forming)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S,S)-butane-2,3-diol:NAD+ oxidoreductase
REACTION    (S,S)-butane-2,3-diol + NAD+ = acetoin + NADH + H+ [RN:R02344]
ALL_REAC    R02344 > R03707
SUBSTRATE   (S,S)-butane-2,3-diol [CPD:C03046];
            NAD+ [CPD:C00003]
PRODUCT     acetoin [CPD:C00466];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Taylor, M.B. and Juni, E.
  TITLE     Stereoisomeric specificities of 2,3-butanediol dehydrogenase.
  JOURNAL   Biochim. Biophys. Acta 39 (1960) 448-457.
  ORGANISM  Aerobacter aerogenes, Pseudomonas hydrophila, Bacillus subtilis
            [GN:bsu]
PATHWAY     PATH: map00650  Butanoate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.76
            ExPASy - ENZYME nomenclature database: 1.1.1.76
            ExplorEnz - The Enzyme Database: 1.1.1.76
            ERGO genome analysis and discovery system: 1.1.1.76
            BRENDA, the Enzyme Database: 1.1.1.76
            CAS: 37250-14-9
///
ENTRY       EC 1.1.1.77                 Enzyme
NAME        lactaldehyde reductase;
            propanediol:nicotinamide adenine dinucleotide (NAD+) oxidoreductase;
            L-lactaldehyde:propanediol oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)[or (S)]-propane-1,2-diol:NAD+ oxidoreductase
REACTION    (R)[or (S)]-propane-1,2-diol + NAD+ = (R)[or (S)]-lactaldehyde +
            NADH + H+ [RN:R02258 R03080]
ALL_REAC    R02258 R03080;
            (other) R01781 R02257
SUBSTRATE   (R)-propane-1,2-diol [CPD:C02912];
            (S)-propane-1,2-diol [CPD:C02917];
            NAD+ [CPD:C00003]
PRODUCT     (R)-lactaldehyde [CPD:C00937];
            (S)-lactaldehyde [CPD:C00424];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Ting, S.-M., Sellinger, O.Z. and Miller, O.N.
  TITLE     The metabolism of lactaldehyde. VI. The reduction of D- and
            L-lactaldehyde in rat liver.
  JOURNAL   Biochim. Biophys. Acta 89 (1964) 217-225.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00620  Pyruvate metabolism
            PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K00048  lactaldehyde reductase
GENES       ECO: b2799(fucO)
            ECJ: JW2770(fucO)
            ECE: Z4116(fucO)
            ECS: ECs3659
            ECC: c3367(fucO)
            ECI: UTI89_C3170(fucO)
            ECP: ECP_2782
            ECV: APECO1_3732(fucO)
            ECW: EcE24377A_3104(fucO)
            ECX: EcHS_A2943(fucO)
            STY: STY3112(fucO)
            STT: t2881(fucO)
            SPT: SPA2837(fucO)
            SEC: SC2912(fucO)
            STM: STM2973(fucO)
            YPI: YpsIP31758_3758(fucO)
            SFL: SF2813(fucO)
            SFX: S3008(fucO)
            SFV: SFV_2878(fucO)
            SSN: SSON_2956(fucO)
            SDY: SDY_3016(fucO)
            ECA: ECA0742(fucO)
            MSU: MS2325(eutG)
            APL: APL_1689
            CPF: CPF_1046(fucO)
            CPR: CPR_0927
            BLO: BL1673(fucO)
            BAD: BAD_0403(fucO)
            BTH: BT_3767
            BFR: BF0254
            BFS: BF0212(fucO)
STRUCTURES  PDB: 1RRM  2BI4  2BL4  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.77
            ExPASy - ENZYME nomenclature database: 1.1.1.77
            ExplorEnz - The Enzyme Database: 1.1.1.77
            ERGO genome analysis and discovery system: 1.1.1.77
            BRENDA, the Enzyme Database: 1.1.1.77
            CAS: 37250-15-0
///
ENTRY       EC 1.1.1.78                 Enzyme
NAME        methylglyoxal reductase (NADH-dependent);
            methylglyoxal reductase;
            D-lactaldehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-lactaldehyde:NAD+ oxidoreductase
REACTION    (R)-lactaldehyde + NAD+ = methylglyoxal + NADH + H+ [RN:R02527]
ALL_REAC    R02527
SUBSTRATE   (R)-lactaldehyde [CPD:C00937];
            NAD+ [CPD:C00003]
PRODUCT     methylglyoxal [CPD:C00546];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     This mammalian enzyme differs from the yeast enzyme, EC 1.1.1.283,
            methylglyoxal reductase (NADPH-dependent), in using NADH rather than
            NADPH as reductant. It oxidizes HO-CH2-CHOH-CHO (glyceraldehyde) as
            well as CH3-CHOH-CHO (lactaldehyde).
REFERENCE   1  [PMID:14323585]
  AUTHORS   TING SM, MILLER ON, SELLINGER OZ.
  TITLE     THE METABOLISM OF LACTALDEHYDE. VII. THE OXIDATION OF D-LACTALDEHYDE
            IN RAT LIVER.
  JOURNAL   Biochim. Biophys. Acta. 97 (1965) 407-15.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00620  Pyruvate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.78
            ExPASy - ENZYME nomenclature database: 1.1.1.78
            ExplorEnz - The Enzyme Database: 1.1.1.78
            ERGO genome analysis and discovery system: 1.1.1.78
            BRENDA, the Enzyme Database: 1.1.1.78
            CAS: 37250-16-1
///
ENTRY       EC 1.1.1.79                 Enzyme
NAME        glyoxylate reductase (NADP+);
            NADPH-glyoxylate reductase;
            glyoxylate reductase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     glycolate:NADP+ oxidoreductase
REACTION    glycolate + NADP+ = glyoxylate + NADPH + H+ [RN:R00465]
ALL_REAC    R00465;
            (other) R01392 R02527
SUBSTRATE   glycolate [CPD:C00160];
            NADP+ [CPD:C00006]
PRODUCT     glyoxylate [CPD:C00048];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also reduces hydroxypyruvate to glycerate; has some affinity for
            NAD+.
REFERENCE   1
  AUTHORS   Cartwright, L.N. and Hullin, R.P.
  TITLE     Purification and properties of two glyoxylate reductases from a
            species of Pseudomonas.
  JOURNAL   Biochem. J. 101 (1966) 781-791.
  ORGANISM  Pseudomonas
REFERENCE   2  [PMID:3548703]
  AUTHORS   Kleczkowski LA, Randall DD, Blevins DG.
  TITLE     Purification and characterization of a novel NADPH(NADH)-dependent
            glyoxylate reductase from spinach leaves. Comparison of
            immunological properties of leaf glyoxylate reductase and
            hydroxypyruvate reductase.
  JOURNAL   Biochem. J. 239 (1986) 653-9.
  ORGANISM  spinach
PATHWAY     PATH: map00620  Pyruvate metabolism
            PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K00049  glyoxylate reductase (NADP+)
GENES       HSA: 9380(GRHPR)
            MMU: 76238(Grhpr)
            CME: CMQ289C
            ECO: b1033(ghrA)
            BPL: BURPS1106A_0368(ghrA)
            BPD: BURPS668_0354(ghrA)
STRUCTURES  PDB: 2GCG  2H1S  2Q50  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.79
            ExPASy - ENZYME nomenclature database: 1.1.1.79
            ExplorEnz - The Enzyme Database: 1.1.1.79
            ERGO genome analysis and discovery system: 1.1.1.79
            BRENDA, the Enzyme Database: 1.1.1.79
            CAS: 37250-17-2
///
ENTRY       EC 1.1.1.80                 Enzyme
NAME        isopropanol dehydrogenase (NADP+);
            isopropanol dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     propan-2-ol:NADP+ oxidoreductase
REACTION    propan-2-ol + NADP+ = acetone + NADPH + H+ [RN:R01550]
ALL_REAC    R01550
SUBSTRATE   propan-2-ol [CPD:C01845];
            NADP+ [CPD:C00006]
PRODUCT     acetone [CPD:C00207];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on other short-chain secondary alcohols and, slowly, on
            primary alcohols.
REFERENCE   1
  AUTHORS   Hoshino, K.
  TITLE     Organism producing isopropanol from acetone. V. Enzymological
            [studies] on the oxidation-reduction of Lactobacillus brevis var.
            hofuensis. [in Japanese].
  JOURNAL   Nippon Nogei Kagaku Kaishi 34 (1960) 608-615.
  ORGANISM  Lactobacillus brevis [GN:lbr]
REFERENCE   2
  AUTHORS   Hoshino, K. and Udagawa, K.
  TITLE     Organism producing isopropanol from acetone. VI. Isopropanol
            dehydrogenase and alcohol dehydrogenase of Lactobacillus brevis var.
            hofuensis. [in Japanese].
  JOURNAL   Nippon Nogei Kagaku Kaishi 34 (1960) 616-619.
  ORGANISM  Lactobacillus brevis [GN:lbr]
PATHWAY     PATH: map00640  Propanoate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.80
            ExPASy - ENZYME nomenclature database: 1.1.1.80
            ExplorEnz - The Enzyme Database: 1.1.1.80
            ERGO genome analysis and discovery system: 1.1.1.80
            BRENDA, the Enzyme Database: 1.1.1.80
            CAS: 37250-18-3
///
ENTRY       EC 1.1.1.81                 Enzyme
NAME        hydroxypyruvate reductase;
            beta-hydroxypyruvate reductase;
            NADH:hydroxypyruvate reductase;
            D-glycerate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-glycerate:NADP+ 2-oxidoreductase
REACTION    D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H + H+ [RN:R01388
            R01392]
ALL_REAC    R01388 R01392
SUBSTRATE   D-glycerate [CPD:C00258];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     hydroxypyruvate [CPD:C00168];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Kleczkowski, L.A. and Edwards, G.E.
  TITLE     Identification of hydroxypyruvate and glyoxylate reductases in maize
            leaves.
  JOURNAL   Plant Physiol. 91 (1989) 278-286.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   2  [PMID:3281657]
  AUTHORS   Kleczkowski LA, Randall DD.
  TITLE     Purification and characterization of a novel NADPH(NADH)-dependent
            hydroxypyruvate reductase from spinach leaves. Comparison of
            immunological properties of leaf hydroxypyruvate reductases.
  JOURNAL   Biochem. J. 250 (1988) 145-52.
  ORGANISM  spinach
REFERENCE   3  [PMID:4385077]
  AUTHORS   Kohn LD, Jakoby WB.
  TITLE     Tartaric acid metabolism. VII. Crystalline hydroxypyruvate reductase
            (D-glycerate dehydrogenase).
  JOURNAL   J. Biol. Chem. 243 (1968) 2494-9.
  ORGANISM  Pseudomonas acidovorans
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K00050  hydroxypyruvate reductase
GENES       PIC: PICST_43416(MDH99)
            YPE: YPO2536
            YPK: y1651
            YPM: YP_2347(ldhA2)
            YPA: YPA_2028
            YPN: YPN_2131
            YPS: YPTB2568
            PPR: PBPRA2272
            PAE: PA1499
            PAU: PA14_45030(ttuD)
            PPU: PP_4300
            PPF: Pput_1569
            PFL: PFL_1698
            PFO: Pfl_1595
            PEN: PSEEN1669
            PMY: Pmen_2772
            PAT: Patl_0336
            AEH: Mlg_1319
            HHA: Hhal_1267
            CVI: CV_3660(ttuD)
            RSO: RSc0486(ttuD2) RSp1449(ttuD1)
            REU: Reut_A0463 Reut_A3294
            REH: H16_A2132(ttuD2) H16_A3601(ttuD1)
            RME: Rmet_0405 Rmet_3451
            PNU: Pnuc_1889
            RFR: Rfer_2329
            POL: Bpro_1434
            PNA: Pnap_1018
            AAV: Aave_1113
            AJS: Ajs_1122
            VEI: Veis_0928
            MPT: Mpe_A0976 Mpe_A3263
            HAR: HEAR0335
            MMS: mma_0382(ttuD)
            NEU: NE2456(ttuD2)
            NET: Neut_2458
            NMU: Nmul_A2230
            EBA: ebA4615(hfr)
            AZO: azo1162(ttuD)
            DAR: Daro_2118
            TBD: Tbd_0433
            DVU: DVU0765
            DVL: Dvul_2205
            DDE: Dde_2751
            BBA: Bd3195
            ADE: Adeh_3968
            SAT: SYN_00869
            SFU: Sfum_3915
            MLO: mlr5146
            MES: Meso_2839
            PLA: Plav_2031
            SME: SMa1406(ttuD3) SMb20678(ttuD2) SMc04389(ttuD1)
            SMD: Smed_3163 Smed_4311 Smed_5562
            ATU: Atu3232 Atu5334
            ATC: AGR_L_3166 AGR_pAT_bx66
            RET: RHE_CH01794(ttuD)
            RLE: RL0994 RL2008
            BME: BMEI1570
            BMF: BAB1_0384
            BMS: BR0355
            BMB: BruAb1_0381
            OAN: Oant_0461 Oant_4591
            BJA: blr7830
            BRA: BRADO0973
            BBT: BBta_7083
            RPA: RPA1797
            RPB: RPB_3567
            RPC: RPC_4629
            RPD: RPD_1897
            RPE: RPE_3720
            NWI: Nwi_0566
            NHA: Nham_0659
            XAU: Xaut_3104
            SIL: SPO1564
            SIT: TM1040_3471
            RSP: RSP_3071
            RSH: Rsph17029_3797
            JAN: Jann_3926
            RDE: RD1_1981(ttuD) RD1_3495 RD1_4241
            PDE: Pden_2195
            GBE: GbCGDNIH1_0364
            ACR: Acry_1160 Acry_2372
            RRU: Rru_A2464
            MAG: amb3175
            ABA: Acid345_1043
            SUS: Acid_0778
            RXY: Rxyl_2854
            LIL: LA2527(ttuD)
            SRU: SRU_1550
            RRS: RoseRS_1997
            RCA: Rcas_3272
            DRA: DR_1157
            DGE: Dgeo_2615
            TTH: TTC0124
            TTJ: TTHA0500
            TPT: Tpet_1207
            TME: Tmel_0085
            FNO: Fnod_1253
            HMA: pNG7015(ttuD)
            HWA: HQ1667A(gckA)
            NPH: NP1162A
            RCI: RCIX2676(ttuD)
            SMR: Smar_0737
            MSE: Msed_2013
            PCL: Pcal_1233
            PAS: Pars_0472
            TPE: Tpen_0207
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.81
            ExPASy - ENZYME nomenclature database: 1.1.1.81
            ExplorEnz - The Enzyme Database: 1.1.1.81
            ERGO genome analysis and discovery system: 1.1.1.81
            BRENDA, the Enzyme Database: 1.1.1.81
            CAS: 9059-44-3
///
ENTRY       EC 1.1.1.82                 Enzyme
NAME        malate dehydrogenase (NADP+);
            NADP+-malic enzyme;
            NADP+-malate dehydrogenase;
            malic dehydrogenase (nicotinamide adenine dinucleotide phosphate);
            malate NADP+ dehydrogenase;
            NADP+ malate dehydrogenase;
            NADP+-linked malate dehydrogenase;
            malate dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-malate:NADP+ oxidoreductase
REACTION    (S)-malate + NADP+ = oxaloacetate + NADPH + H+ [RN:R00343]
ALL_REAC    R00343
SUBSTRATE   (S)-malate [CPD:C00149];
            NADP+ [CPD:C00006]
PRODUCT     oxaloacetate [CPD:C00036];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
EFFECTOR    hn [CPD:C00205]
COMMENT     Activated by light.
REFERENCE   1  [PMID:5689906]
  AUTHORS   Connelly JL, Danner DJ, Bowden JA.
  TITLE     Branched chain alpha-keto acid metabolism. I. Isolation,
            purification, and partial characterization of bovine liver
            alpha-ketoisocaproic:alpha-keto-beta-methylvaleric acid
            dehydrogenase.
  JOURNAL   J. Biol. Chem. 243 (1968) 1198-203.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:4397919]
  AUTHORS   Johnson HS.
  TITLE     NADP-malate dehydrogenase: photoactivation in leaves of plants with
            Calvin cycle photosynthesis.
  JOURNAL   Biochem. Biophys. Res. Commun. 43 (1971) 703-9.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   3  [PMID:4395182]
  AUTHORS   Johnson HS, Hatch MD.
  TITLE     Properties and regulation of leaf nicotinamide-adenine dinucleotide
            phosphate-malate dehydrogenase and 'malic' enzyme in plants with the
            C4-dicarboxylic acid pathway of photosynthesis.
  JOURNAL   Biochem. J. 119 (1970) 273-80.
  ORGANISM  Zea mays [GN:ezma]
PATHWAY     PATH: map00620  Pyruvate metabolism
            PATH: map00710  Carbon fixation
ORTHOLOGY   KO: K00051  malate dehydrogenase (NADP+)
GENES       ATH: AT5G58330
            TET: TTHERM_01029960
            VFI: VF1252
            CSA: Csal_1771
            VEI: Veis_0890
            CGL: NCgl0631(cgl0661)
            CAB: CAB701
            MJA: MJ0490(ldh)
            MMP: MMP0645(mdh)
            MMZ: MmarC7_1086 MmarC7_1132
            MAE: Maeo_0718 Maeo_1197
            MVN: Mevan_1099 Mevan_1138 Mevan_1548
STRUCTURES  PDB: 1CIV  7MDH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.82
            ExPASy - ENZYME nomenclature database: 1.1.1.82
            ExplorEnz - The Enzyme Database: 1.1.1.82
            ERGO genome analysis and discovery system: 1.1.1.82
            BRENDA, the Enzyme Database: 1.1.1.82
            CAS: 37250-19-4
///
ENTRY       EC 1.1.1.83                 Enzyme
NAME        D-malate dehydrogenase (decarboxylating);
            D-malate dehydrogenase;
            D-malic enzyme;
            bifunctional L(+)-tartrate dehydrogenase-D(+)-malate
            (decarboxylating)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-malate:NAD+ oxidoreductase (decarboxylating)
REACTION    (R)-malate + NAD+ = pyruvate + CO2 + NADH [RN:R00215]
ALL_REAC    R00215
SUBSTRATE   (R)-malate [CPD:C00497];
            NAD+ [CPD:C00003]
PRODUCT     pyruvate [CPD:C00022];
            CO2 [CPD:C00011];
            NADH [CPD:C00004]
REFERENCE   1  [PMID:4889267]
  AUTHORS   Stern JR, O'Brien RW.
  TITLE     Oxidation D-malic and beta-alkylmalic acids wild-type and mutant
            strains of Salmonella typhimurium and by Aerobacter aerogenes.
  JOURNAL   J. Bacteriol. 98 (1969) 147-51.
  ORGANISM  Salmonella typhimurium, Aerobacter aerogenes
PATHWAY     PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K07246  D-malate dehydrogenase (decarboxylating)
GENES       ECO: b1800(yeaU)
            ECJ: JW1789(yeaU)
            ECE: Z2843(yeaU)
            ECS: ECs2509
            YPE: YPO2496
            YPM: YP_2311(leuB1)
            YPA: YPA_1991
            YPN: YPN_2090
            YPS: YPTB2532
            SSN: SSON_1361(yeaU)
            SBO: SBO_1288(yeaU)
            SDY: SDY_1701(yeaU)
            MSU: MS1105(leuB)
            PST: PSPTO_2662
            PSB: Psyr_2396
            PSP: PSPPH_2554
            PEN: PSEEN2132
            ABO: ABO_0510(tdh)
            RSO: RSp1612(ttuC)
            REU: Reut_B4115
            RME: Rmet_0404
            BMA: BMAA0011(ttuC)
            BPS: BPSS0011
            BPM: BURPS1710b_A1518
            BPE: BP2291
            BPA: BPP4066
            BBR: BB4539
            RFR: Rfer_2247
            POL: Bpro_3066
            MLO: mll7044
            SME: SMa1846
            ATU: Atu3402
            ATC: AGR_L_2841
            BJA: blr2916
            BRA: BRADO2534(yeaU) BRADO5094(ttuC)
            BBT: BBta_2879(yeaU) BBta_5565(ttuC)
            RPA: RPA1742(yeaU)
            RSP: RSP_3389 RSP_4031
            ACR: Acry_0182
            BSU: BG11222(ycsA)
            BHA: BH1070
            BLI: BL03389(ycsA)
            BLD: BLi03766(ycsA)
            OIH: OB0661
            STH: STH2344
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.83
            ExPASy - ENZYME nomenclature database: 1.1.1.83
            ExplorEnz - The Enzyme Database: 1.1.1.83
            ERGO genome analysis and discovery system: 1.1.1.83
            BRENDA, the Enzyme Database: 1.1.1.83
            CAS: 37250-20-7
///
ENTRY       EC 1.1.1.84                 Enzyme
NAME        dimethylmalate dehydrogenase;
            beta,beta-dimethylmalate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-3,3-dimethylmalate:NAD+ oxidoreductase (decarboxylating)
REACTION    (R)-3,3-dimethylmalate + NAD+ = 3-methyl-2-oxobutanoate + CO2 + NADH
            [RN:R01211]
ALL_REAC    R01211
SUBSTRATE   (R)-3,3-dimethylmalate [CPD:C01088];
            NAD+ [CPD:C00003]
PRODUCT     3-methyl-2-oxobutanoate [CPD:C00141];
            CO2 [CPD:C00011];
            NADH [CPD:C00004]
COFACTOR    NH3 [CPD:C00014];
            Manganese [CPD:C00034];
            Cobalt [CPD:C00175];
            Potassium [CPD:C00238];
            NH4+ [CPD:C01342]
COMMENT     Requires K+ or NH4+ and Mn2+ or Co2+; also acts on (R)-malate.
REFERENCE   1  [PMID:4287371]
  AUTHORS   Magee PT, Snell EE.
  TITLE     The bacterial degradation of pantothenic acid. IV. Enzymatic
            conversion of aldopantoate to alpha-ketoisovalerate.
  JOURNAL   Biochemistry. 5 (1966) 409-16.
  ORGANISM  Pseudomonas
PATHWAY     PATH: map00770  Pantothenate and CoA biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.84
            ExPASy - ENZYME nomenclature database: 1.1.1.84
            ExplorEnz - The Enzyme Database: 1.1.1.84
            ERGO genome analysis and discovery system: 1.1.1.84
            BRENDA, the Enzyme Database: 1.1.1.84
            CAS: 37250-21-8
///
ENTRY       EC 1.1.1.85                 Enzyme
NAME        3-isopropylmalate dehydrogenase;
            beta-isopropylmalic enzyme;
            beta-isopropylmalate dehydrogenase;
            threo-Ds-3-isopropylmalate dehydrogenase;
            3-carboxy-2-hydroxy-4-methylpentanoate:NAD+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (2R,3S)-3-isopropylmalate:NAD+ oxidoreductase
REACTION    (1) (1a) (2R,3S)-3-isopropylmalate + NAD+ =
            (2S)-2-isopropyl-3-oxosuccinate + NADH + H+ [RN:R04426];
            (2) (1b) (2S)-2-isopropyl-3-oxosuccinate = 4-methyl-2-oxopentanoate
            + CO2 (spontaneous)
ALL_REAC    R04426
SUBSTRATE   (2R,3S)-3-isopropylmalate [CPD:C04411];
            NAD+ [CPD:C00003];
            (2S)-2-isopropyl-3-oxosuccinate [CPD:C04236]
PRODUCT     (2S)-2-isopropyl-3-oxosuccinate [CPD:C04236];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            4-methyl-2-oxopentanoate [CPD:C00233];
            CO2 [CPD:C00011]
COMMENT     The product decarboxylates spontaneously to yield
            4-methyl-2-oxopentanoate.
REFERENCE   1
  AUTHORS   Burns, R.O., Umbarger, H.E. and Gross, S.R.
  TITLE     The biosynthesis of leucine. III. The conversion of
            alpha-hydroxy-beta-carboxyisocaproate to alpha-ketoisocaproate.
  JOURNAL   Biochemistry 2 (1963) 1053.
  ORGANISM  Salmonella typhimurium, Neurospora crassa [GN:dncr]
REFERENCE   2  [PMID:4889950]
  AUTHORS   Parsons SJ, Burns RO.
  TITLE     Purification and properties of beta-isopropylmalate dehydrogenase.
  JOURNAL   J. Biol. Chem. 244 (1969) 996-1003.
  ORGANISM  Salmonella typhimurium
REFERENCE   3  [PMID:10683439]
  AUTHORS   Nemeth A, Svingor A, Pocsik M, Dobo J, Magyar C, Szilagyi A, Gal P,
            Zavodszky P.
  TITLE     Mirror image mutations reveal the significance of an intersubunit
            ion cluster in the stability of 3-isopropylmalate dehydrogenase.
  JOURNAL   FEBS. Lett. 468 (2000) 48-52.
  ORGANISM  Thermus thermophilus, Escherichia coli [GN:eco]
REFERENCE   4  [PMID:14269331]
  AUTHORS   CALVO JM, STEVENS CM, KALYANPUR MG, UMBARGER HE.
  TITLE     THE ABSOLUTE CONFIGURATION OF ALPHA-HYDROXY-BETA-CARBOXYISOCAPROIC
            ACID (3-ISOPROPYLMALIC ACID), AN INTERMEDIATE IN LEUCINE
            BIOSYNTHESIS.
  JOURNAL   Biochemistry. 19 (1964) 2024-7.
  ORGANISM  Neurospora crassa [GN:dncr]
PATHWAY     PATH: map00290  Valine, leucine and isoleucine biosynthesis
ORTHOLOGY   KO: K00052  3-isopropylmalate dehydrogenase
GENES       ATH: AT1G31180 AT1G80560
            OSA: 4333613
            CME: CMM229C
            SCE: YCL018W(LEU2)
            AGO: AGOS_AAL012C
            PIC: PICST_68561(LEU2)
            CGR: CAGL0H03795g(LEU3_CANGA)
            SPO: SPBC1A4.02c SPBC1A4.02d(leu1)
            ANI: AN0912.2
            AFM: AFUA_1G15780 AFUA_6G13590
            AOR: AO090005001122
            ANG: An01g14130(leu2A) An04g10130(leu2B)
            CNE: CNA04310
            UMA: UM01245.1
            ECO: b0073(leuB)
            ECJ: JW5807(leuB)
            ECE: Z0082(leuB)
            ECS: ECs0077
            ECC: c0090(leuB)
            ECI: UTI89_C0080(leuB)
            ECP: ECP_0075
            ECV: APECO1_1910(leuB)
            ECW: EcE24377A_0076(leuB)
            ECX: EcHS_A0078(leuB)
            STY: STY0131(leuB)
            STT: t0116(leuB)
            SPT: SPA0114(leuB)
            SEC: SC0108(leuB)
            STM: STM0112(leuB)
            YPE: YPO0532(leuB)
            YPK: y3646(leuB)
            YPM: YP_3650(leuB2)
            YPA: YPA_3565
            YPN: YPN_0402
            YPP: YPDSF_3107
            YPS: YPTB0671(leuB)
            YPI: YpsIP31758_3406(leuB)
            SFL: SF0068(leuB)
            SFX: S0070(leuB)
            SFV: SFV_0065(leuB)
            SSN: SSON_0080(leuB)
            SBO: SBO_0060(leuB)
            SDY: SDY_0100(leuB)
            ECA: ECA3832(leuB)
            PLU: plu3674(leuB)
            BUC: BUpL05(leuB)
            BAB: bbp496(leuB)
            SGL: SG0436
            ENT: Ent638_0621
            SPE: Spro_0744
            BFL: Bfl132(leuB)
            BPN: BPEN_136(leuB)
            HIT: NTHI1161(leuB)
            HIP: CGSHiEE_07030
            HSO: HS_0391(leuB)
            PMU: PM1961(leuB)
            MSU: MS0598(leuB)
            APL: APL_0432(leuB)
            ASU: Asuc_1908
            XFA: XF2372
            XFT: PD1397(leuB)
            XCC: XCC3328(leuB)
            XCB: XC_0836
            XCV: XCV3584(leuB)
            XAC: XAC3456(leuB)
            XOO: XOO0940(leuB)
            XOM: XOO_0860(XOO0860)
            VCH: VC2491
            VCO: VC0395_A2066(leuB)
            VVU: VV1_0655
            VVY: VV0486
            VPA: VP0344
            VFI: VF0294
            PPR: PBPRA0418
            PAE: PA3118(leuB)
            PAU: PA14_23790(leuB)
            PAP: PSPA7_2015(leuB)
            PPU: PP_1988(leuB)
            PPF: Pput_3771
            PST: PSPTO_2175(leuB)
            PSB: Psyr_1985
            PSP: PSPPH_1954(leuB) PSPPH_2159
            PFL: PFL_2066(leuB)
            PFO: Pfl_1892
            PEN: PSEEN1652(leuB)
            PMY: Pmen_2721
            PAR: Psyc_1410(leuB)
            PCR: Pcryo_1571
            ACI: ACIAD0469(leuB)
            ACB: A1S_0420
            SON: SO_4235(leuB)
            SDN: Sden_0335
            SFR: Sfri_3819
            SAZ: Sama_0336
            SBL: Sbal_0387
            SBM: Shew185_0386
            SLO: Shew_3471
            SPC: Sputcn32_0472
            SSE: Ssed_0394
            SPL: Spea_3827
            SHE: Shewmr4_3587
            SHM: Shewmr7_0369
            SHN: Shewana3_3760
            SHW: Sputw3181_0375
            CPS: CPS_4209(leuB)
            PHA: PSHAa2893(leuB) PSHAb0465
            PAT: Patl_3269
            SDE: Sde_2084
            MAQ: Maqu_1563 Maqu_2209
            MCA: MCA2063(leuB)
            FTL: FTL_1887
            FTA: FTA_1997
            FTN: FTN_0059(leuB)
            TCX: Tcr_0797
            NOC: Noc_1014
            AEH: Mlg_0489 Mlg_1230
            HHA: Hhal_0829 Hhal_1810
            HCH: HCH_00651 HCH_02430(leuB)
            CSA: Csal_2451
            ABO: ABO_1467(leuB)
            MMW: Mmwyl1_2093
            AHA: AHA_0881(leuB) AHA_1152
            CRP: CRP_082
            RMA: Rmag_0099
            VOK: COSY_0103(leuB)
            NME: NMB1031
            NMA: NMA1456(leuB)
            NMC: NMC1182(leuB)
            NGO: NGO0674(leuB)
            CVI: CV_2778(leuB)
            RSO: RSc1988(leuB1) RSp0329(leuB2)
            REU: Reut_A2311
            REH: H16_A0477(leuB1) H16_A2133(leuB2) H16_A2619(leuB3)
            RME: Rmet_2472
            BMA: BMAA1726(leuB)
            BMV: BMASAVP1_1643(leuB)
            BML: BMA10299_1852(leuB)
            BMN: BMA10247_A0523(leuB)
            BXE: Bxe_B2887
            BVI: Bcep1808_4457
            BUR: Bcep18194_B2131
            BCN: Bcen_4415
            BCH: Bcen2424_3952
            BAM: Bamb_3343
            BPS: BPSS1705(leuB)
            BPM: BURPS1710b_A0775(leuB)
            BPL: BURPS1106A_A2313(leuB)
            BPD: BURPS668_A2451(leuB)
            BTE: BTH_II0674(leuB)
            PNU: Pnuc_0767
            BPE: BP1483(leuB)
            BPA: BPP1944(leuB)
            BBR: BB1014(leuB) BB2132(leuB)
            RFR: Rfer_1793
            POL: Bpro_3610
            PNA: Pnap_3041
            AAV: Aave_1221
            AJS: Ajs_3233
            VEI: Veis_1047 Veis_1349
            MPT: Mpe_A2162
            HAR: HEAR1217(leuB)
            MMS: mma_2169(leuB)
            NEU: NE0688(leuB)
            NET: Neut_1147
            NMU: Nmul_A1918
            EBA: ebA4760(leuB)
            AZO: azo1041(leuB)
            DAR: Daro_0864 Daro_3775
            TBD: Tbd_1920
            MFA: Mfla_1703
            HHE: HH1134(leuB)
            WSU: WS1813
            TDN: Tmden_1101
            CJE: Cj1718c(leuB)
            CJR: CJE1888(leuB)
            CJJ: CJJ81176_0016(leuB)
            CJU: C8J_1624(leuB)
            CJD: JJD26997_2095(leuB)
            CFF: CFF8240_1020(leuB)
            CCV: CCV52592_1365(leuB)
            CHA: CHAB381_1264(leuB)
            CCO: CCC13826_0036(leuB)
            ABU: Abu_1013(leuB)
            NIS: NIS_0727(leuB)
            SUN: SUN_1705(leuB)
            GSU: GSU2879(leuB)
            GME: Gmet_0602
            GUR: Gura_1045
            PCA: Pcar_1904
            PPD: Ppro_0045
            DVU: DVU2985(leuB)
            DVL: Dvul_0387
            DDE: Dde_3222
            BBA: Bd1264(leuB)
            DPS: DP1284
            ADE: Adeh_2070
            AFW: Anae109_1754
            MXA: MXAN_1283
            SAT: SYN_00088
            SFU: Sfum_2989 Sfum_3031
            PUB: SAR11_0250(leuB)
            MLO: mll4399
            MES: Meso_3381
            PLA: Plav_1425
            SME: SMc04405(leuB)
            ATU: Atu2791(leuB)
            ATC: AGR_C_5067
            RET: RHE_CH04093(leuB) RHE_PF00339(ypf00171)
            RLE: RL4707(leuB)
            BME: BMEII0271 BMEII0404
            BMF: BAB2_0346
            BMS: BRA0890(leuB)
            BMB: BruAb2_0342(leuB)
            BOV: BOV_A0834(leuB)
            BJA: bll0414(leuB) bll0504(leuB) bll6321(leuB) blr2741 blr2781
            BRA: BRADO0353(leuB) BRADO2458
            BBT: BBta_0340(leuB) BBta_2804
            RPA: RPA0227(leuB)
            RPB: RPB_0335
            RPC: RPC_0240
            RPD: RPD_0490
            RPE: RPE_0480
            NWI: Nwi_2795
            NHA: Nham_3595
            XAU: Xaut_2589
            CCR: CC_0193
            SIL: SPO0210(leuB)
            SIT: TM1040_3762
            RSP: RSP_0859(leuB)
            RSH: Rsph17029_2518
            RSQ: Rsph17025_0162
            JAN: Jann_0128
            RDE: RD1_0228(leuB) RD1_3789(leuB)
            PDE: Pden_0440
            MMR: Mmar10_0283
            HNE: HNE_0056(leuB)
            ZMO: ZMO0677(leuB)
            NAR: Saro_2662
            SAL: Sala_1085
            SWI: Swit_4494
            ELI: ELI_08335
            GOX: GOX0191
            GBE: GbCGDNIH1_1678
            ACR: Acry_1270 Acry_2147
            RRU: Rru_A1191
            MAG: amb4069
            MGM: Mmc1_1781
            ABA: Acid345_2917 Acid345_2964
            SUS: Acid_1530 Acid_4068
            BSU: BG10675(leuB)
            BHA: BH3057(leuB)
            BAN: BA1421(leuB)
            BAR: GBAA1421(leuB)
            BAA: BA_1941
            BAT: BAS1312
            BCE: BC1401
            BCA: BCE_1521(leuB)
            BCZ: BCZK1286(leuB)
            BCY: Bcer98_1124
            BTK: BT9727_1285(leuB)
            BTL: BALH_1256(leuB)
            BLI: BL00612(leuB)
            BLD: BLi02957(leuB)
            BCL: ABC0628 ABC2641(leuB)
            BAY: RBAM_025330(leuB)
            BPU: BPUM_2468(leuB)
            OIH: OB2619(leuB)
            GKA: GK2657
            SAU: SA1863(leuB)
            SAV: SAV2058(leuB)
            SAM: MW1982(leuB)
            SAR: SAR2145(leuB)
            SAS: SAS1963
            SAC: SACOL2047(leuB)
            SAB: SAB1943(leuB)
            SAA: SAUSA300_2011(leuB)
            SAO: SAOUHSC_02286
            SAJ: SaurJH9_2095
            SAH: SaurJH1_2132
            SEP: SE1659
            SER: SERP1670(leuB)
            SHA: SH0975(leuB)
            SSP: SSP0820
            LMO: lmo1988(leuB)
            LMF: LMOf2365_2011(leuB)
            LIN: lin2095(leuB)
            LWE: lwe2007(leuB)
            LLA: L0074(leuB)
            LLC: LACR_1320
            SPR: spr1135(leuB)
            SPD: SPD_1115(leuB)
            SMU: SMU.1383(leuB)
            STC: str1202(leuB)
            STL: stu1202(leuB)
            SSA: SSA_0977(leuB)
            SGO: SGO_0907(leuB)
            STH: STH3035
            CAC: CAC3171(leuB)
            CTH: Cthe_2209
            CDF: CD0992(leuB)
            CBE: Cbei_0216
            CKL: CKL_2157(leuB)
            AMT: Amet_3455
            CHY: CHY_0524(leuB)
            DSY: DSY1371 DSY3587
            DRM: Dred_0288
            SWO: Swol_2140
            CSC: Csac_1333
            TTE: TTE0019(leuB)
            MTA: Moth_2252
            MTU: Rv2995c(leuB)
            MTC: MT3073(leuB)
            MBO: Mb3019c(leuB)
            MBB: BCG_3016c(leuB)
            MLE: ML1691(leuB)
            MPA: MAP3032c(leuB)
            MAV: MAV_3845(leuB)
            MSM: MSMEG_2379(leuB) MSMEG_3285
            MVA: Mvan_2129
            MGI: Mflv_4233
            MMC: Mmcs_1911 Mmcs_2572
            MKM: Mkms_1957 Mkms_2617
            MJL: Mjls_1891 Mjls_2611
            CGL: NCgl1237(cgl1286)
            CGB: cg1453(leuB)
            CEF: CE1383(leuB)
            CDI: DIP1105(leuB)
            CJK: jk1288(leuB)
            NFA: nfa18790 nfa42200(leuB)
            RHA: RHA1_ro00322(leuB1) RHA1_ro00984(leuB2) RHA1_ro04803
                 RHA1_ro06490(leuB3) RHA1_ro08803
            SCO: SCO5522(leuB)
            SMA: SAV2718(leuB)
            LXX: Lxx13130(leuB)
            CMI: CMM_1104(leuB)
            ART: Arth_2530
            AAU: AAur_2498(leuB)
            NCA: Noca_3368
            TFU: Tfu_0615
            FRA: Francci3_3632
            FAL: FRAAL5843(leuB)
            ACE: Acel_0710
            KRA: Krad_1352 Krad_2488
            SEN: SACE_3196(leuB) SACE_3495(leuB1) SACE_4608 SACE_6154(leuB)
            STP: Strop_1239
            BLO: BL1218(leuB)
            BAD: BAD_1340(leuB)
            RXY: Rxyl_3130
            RBA: RB12597(leuB) RB3767(leuB)
            LIL: LA2152(leuB)
            LIC: LIC11768(leuB)
            LBJ: LBJ_1863(leuB-1)
            LBL: LBL_1421(leuB-1)
            SYN: slr1517(leuB)
            SYW: SYNW0784(leuB)
            SYC: syc2490_c(leuB)
            SYF: Synpcc7942_1505
            SYD: Syncc9605_1865
            SYE: Syncc9902_0788
            SYG: sync_1712(leuB)
            SYR: SynRCC307_0997(leuB)
            SYX: SynWH7803_1152(leuB)
            CYA: CYA_1798(leuB)
            CYB: CYB_1631(leuB)
            TEL: tlr1600(leuB)
            GVI: gll3551(leuB)
            ANA: alr1313(leuB)
            AVA: Ava_2987
            PMA: Pro0862(leuB)
            PMM: PMM0786(leuB)
            PMT: PMT0531(leuB)
            PMN: PMN2A_0194
            PMI: PMT9312_0794
            PMB: A9601_08501(leuB) A9601_16211
            PMC: P9515_07951(leuB) P9515_12211
            PMF: P9303_17341(leuB)
            PMG: P9301_08471(leuB)
            PMH: P9215_08811(leuB)
            PME: NATL1_08261(leuB) NATL1_11771
            TER: Tery_4403
            BTH: BT_1857
            BFR: BF3444(leuB)
            BFS: BF3263(leuB)
            SRU: SRU_2148(leuB)
            CHU: CHU_3744(leuB)
            GFO: GFO_2098(leuB)
            FJO: Fjoh_2864
            CTE: CT0615(leuB)
            CCH: Cag_1901
            CPH: Cpha266_0850
            PVI: Cvib_1173
            PLT: Plut_0603
            DET: DET0826(leuB)
            DEH: cbdb_A804(leuB)
            RRS: RoseRS_1057 RoseRS_1958
            RCA: Rcas_1546 Rcas_3471
            DRA: DR_1785
            DGE: Dgeo_1033 Dgeo_1458
            TTH: TTC0867
            TTJ: TTHA1230
            AAE: aq_244(leuB)
            TMA: TM0556
            TPT: Tpet_0364
            MJA: MJ0720
            MMP: MMP0539(leuB)
            MMQ: MmarC5_0688 MmarC5_1068
            MMZ: MmarC7_0128 MmarC7_1558
            MAE: Maeo_1416 Maeo_1484
            MVN: Mevan_0040 Mevan_1693
            MAC: MA0201(leuB) MA3748(leuB)
            MBA: Mbar_A0248 Mbar_A1339
            MMA: MM_1489
            MBU: Mbur_1632
            MTP: Mthe_0025 Mthe_0855
            MHU: Mhun_1797 Mhun_2363
            MEM: Memar_0637 Memar_1947
            MBN: Mboo_0602 Mboo_2077
            MST: Msp_1484(leuB)
            MSI: Msm_0373 Msm_1298
            MKA: MK0782(leuB_1) MK1215(leuB_2)
            HMA: rrnAC0340(ipmD)
            HWA: HQ2707A(leuB)
            NPH: NP2190A(leuB)
            PTO: PTO0910
            PAB: PAB0289(leuB-2) PAB2424(leuB-1)
            PFU: PF0940(leuB2)
            TKO: TK0280
            RCI: RCIX2644(leuB-2) RCIX993(leuB-1)
            IHO: Igni_0982
            SSO: SSO0723(leuB)
            STO: ST0433
            SAI: Saci_0600(leuB)
            MSE: Msed_0088
            PAI: PAE1995(leuB)
            PIS: Pisl_1815
            PCL: Pcal_1605
            PAS: Pars_2064
STRUCTURES  PDB: 1A05  1DPZ  1DR0  1DR8  1G2U  1GC8  1GC9  1HEX  1IDM  1IPD  
                 1OSI  1OSJ  1V53  1V5B  1VLC  1W0D  1WPW  1XAA  1XAB  1XAC  
                 1XAD  2AYQ  2G4O  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.85
            ExPASy - ENZYME nomenclature database: 1.1.1.85
            ExplorEnz - The Enzyme Database: 1.1.1.85
            ERGO genome analysis and discovery system: 1.1.1.85
            BRENDA, the Enzyme Database: 1.1.1.85
            CAS: 9030-97-1
///
ENTRY       EC 1.1.1.86                 Enzyme
NAME        ketol-acid reductoisomerase;
            dihydroxyisovalerate dehydrogenase (isomerizing);
            acetohydroxy acid isomeroreductase;
            ketol acid reductoisomerase;
            alpha-keto-beta-hydroxylacyl reductoisomerase;
            2-hydroxy-3-keto acid reductoisomerase;
            acetohydroxy acid reductoisomerase;
            acetolactate reductoisomerase;
            dihydroxyisovalerate (isomerizing) dehydrogenase;
            isomeroreductase;
            reductoisomerase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-2,3-dihydroxy-3-methylbutanoate:NADP+ oxidoreductase
            (isomerizing)
REACTION    (R)-2,3-dihydroxy-3-methylbutanoate + NADP+ =
            (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+ [RN:R04439]
ALL_REAC    R04439;
            (other) R03051 R04440 R05068 R05069 R05071
SUBSTRATE   (R)-2,3-dihydroxy-3-methylbutanoate [CPD:C04272];
            NADP+ [CPD:C00006]
PRODUCT     (S)-2-hydroxy-2-methyl-3-oxobutanoate [CPD:C06010];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also catalyses the reduction of 2-aceto-2-hydroxybutanoate to
            2,3-dihydroxy-3-methylpentanoate.
REFERENCE   1  [PMID:4388025]
  AUTHORS   Arfin SM, Umbarger HE.
  TITLE     Purification and properties of the acetohydroxy acid
            isomeroreductase of Salmonella typhimurium.
  JOURNAL   J. Biol. Chem. 244 (1969) 1118-27.
  ORGANISM  Salmonella typhimurium
REFERENCE   2
  AUTHORS   Hill, R.K., Sawada, S. and Arfin, S.M.
  TITLE     Stereochemistry of valine and isoleucine biosynthesis. IV.
            Synthesis, configuration, and enzymatic specificity of
            alpha-acetolactate and alpha-aceto-alpha-hydroxybutyrate.
  JOURNAL   Bioorg. Chem. 8 (1979) 175-189.
  ORGANISM  Salmonella typhimurium
REFERENCE   3
  AUTHORS   Kiritani, K., Narise, S. and Wagner, R.P.
  TITLE     The reductoisomerase of Neurospora crassa.
  JOURNAL   J. Biol. Chem. 241 (1966) 2047-2051.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   4  [PMID:5866387]
  AUTHORS   Satyanarayana T, Radhakrishnan AN.
  TITLE     Biosynthesis of valine and isoleucine in plants. 3. Reductoisomerase
            of Phaseolus radiatus.
  JOURNAL   Biochim. Biophys. Acta. 110 (1965) 380-8.
  ORGANISM  Phaseolus radiatus
PATHWAY     PATH: map00290  Valine, leucine and isoleucine biosynthesis
            PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K00053  ketol-acid reductoisomerase
GENES       ATH: AT3G58610
            OSA: 4325375 4339677
            CME: CMR121C
            SCE: YLR355C(ILV5)
            AGO: AGOS_ACL198W
            PIC: PICST_78299(ILV5)
            CGR: CAGL0B03047g
            SPO: SPBC56F2.12
            ANI: AN2526.2
            AFM: AFUA_3G14490
            AOR: AO090701000557
            CNE: CNF02480
            UMA: UM04741.1
            ECO: b3774(ilvC)
            ECJ: JW3747(ilvC)
            ECE: Z5285(ilvC)
            ECS: ECs4708
            ECC: c4696(ilvC)
            ECI: UTI89_C4330(ilvC)
            ECP: ECP_3967
            ECW: EcE24377A_4285(ilvC)
            ECX: EcHS_A3990
            STY: STY3648(ilvC)
            STT: t3389(ilvC)
            SPT: SPA3748(ilvC)
            SEC: SC3814(ilvC)
            STM: STM3909(ilvC)
            YPE: YPO3888(ilvC)
            YPK: y0345(ilvC)
            YPM: YP_3158(ilvC)
            YPA: YPA_0132
            YPN: YPN_0077
            YPP: YPDSF_3501
            YPS: YPTB0145(ilvC)
            YPI: YpsIP31758_0163(ilvC)
            SFL: SF3848(ilvY)
            SFX: S3910(ilvC)
            SFV: SFV_3729(ilvC)
            SSN: SSON_3945(ilvC)
            SBO: SBO_3785(ilvC)
            SDY: SDY_3974(ilvC)
            ECA: ECA4221(ilvC)
            PLU: plu4668(ilvC)
            BUC: BU599(ilvC)
            BAS: BUsg575(ilvC)
            BAB: bbp541(ilvC)
            BCC: BCc_388(ilvC)
            SGL: SG2391
            ENT: Ent638_4009
            SPE: Spro_4751
            BFL: Bfl588(ilvC)
            BPN: BPEN_609(ilvC)
            HIT: NTHI0804(ilvC)
            HIP: CGSHiEE_08680
            HIQ: CGSHiGG_06705
            HSO: HS_1671(ilvC)
            PMU: PM1284(ilvC)
            MSU: MS0045(ilvC)
            APL: APL_1853(ilvC)
            ASU: Asuc_0563
            XFA: XF1822
            XFT: PD1043(ilvC)
            XCC: XCC3323(ilvC)
            XCB: XC_0841
            XCV: XCV3579(ilvC)
            XAC: XAC3451(ilvC)
            XOO: XOO0946(ilvC)
            XOM: XOO_0865(XOO0865)
            VCH: VC0162
            VCO: VC0395_A2550(ilvC)
            VVU: VV1_1077
            VVY: VV0035
            VPA: VP0035
            VFI: VF2526 VF2528
            PPR: PBPRA0085
            PAE: PA4694(ilvC)
            PAU: PA14_62130(ilvC)
            PAP: PSPA7_5408(ilvC)
            PPU: PP_4678(ilvC)
            PPF: Pput_4542
            PST: PSPTO_0983(ilvC)
            PSB: Psyr_0848
            PSP: PSPPH_0874(ilvC)
            PFL: PFL_5253(ilvC)
            PFO: Pfl_4786
            PEN: PSEEN4709(ilvC)
            PMY: Pmen_1009
            PAR: Psyc_0529(ilvC)
            PCR: Pcryo_0524
            PRW: PsycPRwf_0611
            ACI: ACIAD3102(ilvC)
            SON: SO_4349(ilvC)
            SDN: Sden_3415
            SFR: Sfri_0421
            SAZ: Sama_3282
            SBL: Sbal_4032
            SBM: Shew185_4010
            SLO: Shew_0288
            SPC: Sputcn32_3615
            SSE: Ssed_4166
            SPL: Spea_0344
            SHE: Shewmr4_0361
            SHM: Shewmr7_3665
            SHN: Shewana3_0355
            SHW: Sputw3181_3755
            CPS: CPS_4839(ilvC)
            PHA: PSHAa0849(ilvC)
            PAT: Patl_4255
            SDE: Sde_2539
            PIN: Ping_0853
            MAQ: Maqu_0884
            MCA: MCA2272(ilvC)
            FTW: FTW_1086(ilvC)
            FTL: FTL_0916
            FTH: FTH_0896(ilvC)
            FTA: FTA_0966(ilvC)
            FTN: FTN_1040(ilvC)
            TCX: Tcr_0636
            NOC: Noc_2518
            AEH: Mlg_0544
            HHA: Hhal_0693
            HCH: HCH_05914(ilvC)
            CSA: Csal_0504
            ABO: ABO_0485(ilvC)
            MMW: Mmwyl1_3846
            AHA: AHA_0153(ilvC)
            CRP: CRP_125
            RMA: Rmag_0447
            VOK: COSY_0413(ilvC)
            NME: NMB1574
            NMA: NMA1763(ilvC)
            NMC: NMC1494(ilvC)
            NGO: NGO1233
            CVI: CV_0588(ilvC)
            RSO: RSc2075(ilvC)
            REU: Reut_A0949
            REH: H16_A1037(ilvC)
            RME: Rmet_0913
            BMA: BMA1846(ilvC)
            BMV: BMASAVP1_A1115(ilvC)
            BML: BMA10299_A0751(ilvC)
            BMN: BMA10247_0398(ilvC)
            BXE: Bxe_A3229
            BVI: Bcep1808_2347
            BUR: Bcep18194_A5590
            BCN: Bcen_1652
            BCH: Bcen2424_2263
            BAM: Bamb_2301
            BPS: BPSL1198(ilvC)
            BPM: BURPS1710b_1421(ilvC) BURPS1710b_A1855(ilvC)
            BPL: BURPS1106A_1283(ilvC) BURPS1106A_A0433(ilvC)
            BPD: BURPS668_1276(ilvC) BURPS668_A0529(ilvC)
            BTE: BTH_I1047(ilvC-1) BTH_II2094(ilvC-2)
            PNU: Pnuc_1061
            BPE: BP0791(ilvC)
            BPA: BPP3435(ilvC)
            BBR: BB3885(ilvC)
            RFR: Rfer_3324
            POL: Bpro_2319
            PNA: Pnap_1719
            AAV: Aave_3110
            AJS: Ajs_1771
            VEI: Veis_1747
            MPT: Mpe_A2103
            HAR: HEAR1239(ilvC)
            MMS: mma_2148
            NEU: NE1323(ilvC)
            NET: Neut_1260
            NMU: Nmul_A0472
            EBA: ebA7134(ilvC)
            AZO: azo3156(ilvC)
            DAR: Daro_3073
            TBD: Tbd_1989
            MFA: Mfla_2121
            HPY: HP0330
            HPA: HPAG1_0334
            HHE: HH1204(ilvC)
            HAC: Hac_0990(ilvC)
            WSU: WS1878(ilvC)
            TDN: Tmden_0541
            CJE: Cj0632(ilvC)
            CJR: CJE0735(ilvC)
            CJJ: CJJ81176_0660(ilvC)
            CJU: C8J_0591(ilvC)
            CJD: JJD26997_1367(ilvC)
            CFF: CFF8240_1127(ilvC)
            CCV: CCV52592_1581(ilvC)
            CHA: CHAB381_0374(ilvC)
            CCO: CCC13826_2003(ilvC)
            ABU: Abu_0237(ilvC)
            NIS: NIS_1161(ilvC)
            SUN: SUN_0443
            GSU: GSU1909(ilvC)
            GME: Gmet_1262
            GUR: Gura_3718
            PCA: Pcar_2518
            PPD: Ppro_2555
            DVU: DVU1378(ilvC)
            DVL: Dvul_1690
            DDE: Dde_2166
            DPS: DP0726
            ADE: Adeh_1976
            AFW: Anae109_1879
            SAT: SYN_01709
            SFU: Sfum_2984 Sfum_3026
            AMA: AM1310(ilvC)
            PUB: SAR11_0001(ilvC)
            MLO: mll1405
            MES: Meso_1496
            PLA: Plav_2466
            SME: SMc04346(ilvC)
            SMD: Smed_1962
            ATU: Atu2019(ilvC)
            ATC: AGR_C_3660
            RET: RHE_CH02744(ilvC)
            RLE: RL3205(ilvC)
            BME: BMEI0624
            BMF: BAB1_1399
            BMS: BR1380(ilvC)
            BMB: BruAb1_1376(ilvC)
            BOV: BOV_1337(ilvC)
            OAN: Oant_1813
            BJA: bll6497(ilvC)
            BRA: BRADO5559(ilvC)
            BBT: BBta_6082(ilvC)
            RPA: RPA2035(ilvC)
            RPB: RPB_3341
            RPC: RPC_3248
            RPD: RPD_2102
            RPE: RPE_2195
            NWI: Nwi_2341
            NHA: Nham_2720
            BHE: BH10890(ilvC)
            BQU: BQ08540(ilvC)
            BBK: BARBAKC583_0917(ilvC)
            XAU: Xaut_1490
            CCR: CC_2120
            SIL: SPO1366(ilvC)
            SIT: TM1040_2303
            RSP: RSP_1865
            RSH: Rsph17029_0514
            RSQ: Rsph17025_0651
            JAN: Jann_1238
            RDE: RD1_1954(ilvC)
            PDE: Pden_1760
            MMR: Mmar10_0290 Mmar10_2020
            HNE: HNE_0447(ilvC)
            ZMO: ZMO1141(ilvC)
            NAR: Saro_2263
            SAL: Sala_1472
            SWI: Swit_0611
            ELI: ELI_05505
            GOX: GOX1089
            GBE: GbCGDNIH1_1478
            ACR: Acry_2559
            RRU: Rru_A0469
            MAG: amb3509
            MGM: Mmc1_0900
            ABA: Acid345_3106
            SUS: Acid_0178
            BSU: BG10672(ilvC)
            BHA: BH3059(ilvC)
            BAN: BA1419(ilvC-1) BA1852(ilvC-2)
            BAR: GBAA1419(ilvC-1) GBAA1852(ilvC-2)
            BAA: BA_1939(ilvC) BA_2355(ilvC)
            BAT: BAS1310 BAS1716
            BCE: BC1399 BC1779
            BCA: BCE_1519(ilvC) BCE_1936(ilvC)
            BCZ: BCZK1284(ilvC) BCZK1668(ilvC)
            BCY: Bcer98_1122
            BTK: BT9727_1283(ilvC) BT9727_1693(ilvC)
            BLI: BL00610(ilvC)
            BLD: BLi02959(ilvC)
            BCL: ABC2643(ilvC)
            BAY: RBAM_025350
            BPU: BPUM_2470
            OIH: OB2621(ilvC)
            GKA: GK2659
            SAU: SA1861(ilvC)
            SAV: SAV2056(ilvC)
            SAM: MW1980(ilvC)
            SAR: SAR2143(ilvC)
            SAS: SAS1961
            SAC: SACOL2045(ilvC)
            SAB: SAB1941(ilvC)
            SAA: SAUSA300_2009(ilvC)
            SAO: SAOUHSC_02284
            SAJ: SaurJH9_2093
            SAH: SaurJH1_2130
            SEP: SE1657
            SER: SERP1668(ilvC)
            SHA: SH0977(ilvC)
            SSP: SSP0822
            LMO: lmo1986(ilvC)
            LMF: LMOf2365_2009(ilvC)
            LIN: lin2093(ilvC)
            LWE: lwe2005(ilvC)
            LLA: L0080(ilvC)
            LLC: LACR_1309
            LLM: llmg_1277(ilvC)
            SPN: SP_0447
            SPR: spr0403(ilvC)
            SPD: SPD_0406(ilvC)
            SMU: SMU.233(ilvC)
            STC: str1871(ilvC)
            STL: stu1871(ilvC)
            SSA: SSA_1968(ilvC)
            SGO: SGO_0528(ilvC)
            STH: STH2688
            CAC: CAC0091(ilvC)
            CNO: NT01CX_2028(ilvC)
            CTH: Cthe_2518
            CDF: CD1565(ilvC)
            CBE: Cbei_0218
            CKL: CKL_1080(ilvC1) CKL_1089(ilvC2)
            AMT: Amet_3402
            CHY: CHY_0519(ilvC)
            DSY: DSY1368
            DRM: Dred_0283
            SWO: Swol_2144
            CSC: Csac_1144
            TTE: TTE0015(ilvC)
            MTA: Moth_1350
            MTU: Rv3001c(ilvC)
            MTC: MT3081(ilvC)
            MBO: Mb3026c(ilvC)
            MBB: BCG_3023c(ilvC)
            MLE: ML1694(ilvC)
            MPA: MAP3036c(ilvC)
            MAV: MAV_3850(ilvC)
            MSM: MSMEG_2374(ilvC)
            MVA: Mvan_2124
            MGI: Mflv_4237
            MMC: Mmcs_1908
            MKM: Mkms_1954
            MJL: Mjls_1888
            CGL: NCgl1224(cgl1273)
            CGB: cg1437(ilvC)
            CEF: CE1367(ilvC)
            CDI: DIP1100(ilvC)
            CJK: jk1298(ilvC)
            NFA: nfa42300(ilvC)
            RHA: RHA1_ro06488(ilvC)
            SCO: SCO5514(ilvC) SCO7154(ilvC2)
            SMA: SAV2731(ilvC)
            TWH: TWT207(ilvC)
            TWS: TW565(ilvC)
            LXX: Lxx13170(ilvC)
            ART: Arth_2537
            AAU: AAur_2507(ilvC)
            PAC: PPA1372
            NCA: Noca_2140 Noca_3390
            TFU: Tfu_0613
            FRA: Francci3_3638
            FAL: FRAAL5849(ilvC)
            ACE: Acel_0708
            KRA: Krad_1337
            SEN: SACE_6157(ilvC)
            STP: Strop_1235
            BLO: BL0530(ilvC1) BL0531(ilvC2)
            BAD: BAD_0081(ilvC2) BAD_0082(ilvC1)
            RXY: Rxyl_3127
            RBA: RB9869(ilvC)
            LIL: LA4242(ilvC)
            LIC: LIC13393(ilvC)
            LBJ: LBJ_2914(ilvC)
            LBL: LBL_0149(ilvC)
            SYN: sll1363(ilvC)
            SYW: SYNW1650(ilvC)
            SYC: syc0010_c(ilvC)
            SYF: Synpcc7942_1552
            SYD: Syncc9605_0839
            SYE: Syncc9902_1550
            SYG: sync_0725(ilvC)
            SYR: SynRCC307_0594(ilvC)
            SYX: SynWH7803_1765(ilvC)
            CYA: CYA_0246(ilvC)
            CYB: CYB_1789(ilvC)
            TEL: tll2254(ilvC)
            GVI: gll2657(ilvC)
            ANA: all2315
            AVA: Ava_0133
            PMA: Pro1389(ilvC)
            PMM: PMM1315(ilvC)
            PMT: PMT0313
            PMN: PMN2A_0881
            PMI: PMT9312_1412
            PMB: A9601_15141(ilvC)
            PMC: P9515_14761(ilvC)
            PMF: P9303_20051(ilvC)
            PMG: P9301_15011(ilvC)
            PME: NATL1_17361(ilvC)
            TER: Tery_4335
            BTH: BT_2074
            BFR: BF3758
            BFS: BF3546
            SRU: SRU_2147(ilvC)
            CHU: CHU_1149(ilvC)
            GFO: GFO_2110(ilvC)
            FJO: Fjoh_2860
            FPS: FP0446(ilvC)
            CTE: CT0616(ilvC)
            CCH: Cag_1902
            CPH: Cpha266_0851
            PVI: Cvib_1172
            PLT: Plut_0604
            DET: DET0831(ilvC)
            DEH: cbdb_A811(ilvC)
            DEB: DehaBAV1_0750
            RRS: RoseRS_1966
            RCA: Rcas_1555
            DRA: DR_1519
            DGE: Dgeo_0600
            TTH: TTC0850
            TTJ: TTHA1211
            AAE: aq_1245(ilvC)
            TMA: TM0550
            TPT: Tpet_0370
            MMP: MMP0654(ilvC)
            MMQ: MmarC5_0922
            MMZ: MmarC7_1680
            MAE: Maeo_1175
            MVN: Mevan_1538
            MAC: MA3790(ilvC)
            MBA: Mbar_A0220
            MMA: MM_0668
            MBU: Mbur_0708
            MTP: Mthe_0112
            MHU: Mhun_1245
            MEM: Memar_2172
            MBN: Mboo_0481
            MST: Msp_0022(ilvC)
            MSI: Msm_1222
            MKA: MK0832(ilvC)
            HMA: rrnAC0332(ilvC)
            HWA: HQ2704A(ilvC)
            NPH: NP2198A(ilvC)
            PTO: PTO1073
            PAB: PAB0889(ilvC)
            PFU: PF0936
            RCI: LRC519(ilvC)
            IHO: Igni_0608
            SSO: SSO0576(ilvC-1) SSO1322(ilvC-2) SSO1942(ilvC-3)
            STO: ST1445
            SAI: Saci_1559
            MSE: Msed_1927
            PAI: PAE3298(ilvC)
            PIS: Pisl_0552
            PCL: Pcal_1755
            PAS: Pars_1722
STRUCTURES  PDB: 1NP3  1QMG  1YRL  1YVE  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.86
            ExPASy - ENZYME nomenclature database: 1.1.1.86
            ExplorEnz - The Enzyme Database: 1.1.1.86
            ERGO genome analysis and discovery system: 1.1.1.86
            BRENDA, the Enzyme Database: 1.1.1.86
            CAS: 9075-02-9
///
ENTRY       EC 1.1.1.87                 Enzyme
NAME        homoisocitrate dehydrogenase;
            2-hydroxy-3-carboxyadipate dehydrogenase;
            3-carboxy-2-hydroxyadipate dehydrogenase;
            homoisocitric dehydrogenase;
            (-)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase
            (decarboxylating);
            3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating);
            HICDH
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate:NAD+ oxidoreductase
            (decarboxylating)
REACTION    (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate +
            CO2 + NADH + H+ [RN:R01934]
ALL_REAC    R01934;
            (other) R01936 R04862
SUBSTRATE   (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate [CPD:C05662];
            NAD+ [CPD:C00003]
PRODUCT     2-oxoadipate [CPD:C00322];
            CO2 [CPD:C00011];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Forms part of the lysine biosynthesis pathway in fungi [3].
REFERENCE   1  [PMID:4284830]
  AUTHORS   Strassman M, Ceci LN.
  TITLE     Enzymatic formation of alpha-ketoadipic acid from homoisocitric
            acid.
  JOURNAL   J. Biol. Chem. 240 (1965) 4357-61.
  ORGANISM  Torulopsis utilis
REFERENCE   2  [PMID:4395693]
  AUTHORS   Rowley B, Tucci AF.
  TITLE     Homoisocitric dehydrogenase from yeast.
  JOURNAL   Arch. Biochem. Biophys. 141 (1970) 499-510.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:10714900]
  AUTHORS   Zabriskie TM, Jackson MD.
  TITLE     Lysine biosynthesis and metabolism in fungi.
  JOURNAL   Nat. Prod. Rep. 17 (2000) 85-97.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K05824  homoisocitrate dehydrogenase
GENES       SCE: YIL094C(LYS12)
            AGO: AGOS_ADL214C
            CGR: CAGL0G02585g
            SPO: SPAC31G5.04
            ANI: AN5206.2
            AFM: AFUA_6G07390
            AOR: AO090005001561
            CNE: CND03850
            UMA: UM04873.1
            DRA: DR_1674
            TTH: TTC1012
            TTJ: TTHA1378
STRUCTURES  PDB: 1X0L  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.87
            ExPASy - ENZYME nomenclature database: 1.1.1.87
            ExplorEnz - The Enzyme Database: 1.1.1.87
            ERGO genome analysis and discovery system: 1.1.1.87
            BRENDA, the Enzyme Database: 1.1.1.87
            CAS: 37250-23-0
///
ENTRY       EC 1.1.1.88                 Enzyme
NAME        hydroxymethylglutaryl-CoA reductase;
            beta-hydroxy-beta-methylglutaryl coenzyme A reductase;
            beta-hydroxy-beta-methylglutaryl CoA-reductase;
            3-hydroxy-3-methylglutaryl coenzyme A reductase;
            hydroxymethylglutaryl coenzyme A reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-mevalonate:NAD+ oxidoreductase (CoA-acylating)
REACTION    (R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2
            NADH + 2 H+ [RN:R02081]
ALL_REAC    R02081
SUBSTRATE   (R)-mevalonate [CPD:C00418];
            CoA [CPD:C00010];
            NAD+ [CPD:C00003]
PRODUCT     3-hydroxy-3-methylglutaryl-CoA [CPD:C00356];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Fimognari, G.M. and Rodwell, V.W.
  TITLE     Substrate-competitive inhibition of bacterial
            mevalonate:nicotinamide-adenine dinucleotide oxidoreductase
            (acylating CoA).
  JOURNAL   Biochemistry 4 (1965) 2086-2090.
  ORGANISM  Pseudomonas sp., Mycobacterium sp.
ORTHOLOGY   KO: K00054  hydroxymethylglutaryl-CoA reductase
GENES       PIC: PICST_72872(HMG1)
            PPF: Pput_3073
            LPN: lpg2052
            LPF: lpl2030
            LPP: lpp2035
            BCH: Bcen2424_3505
            BBA: Bd1627
            MXA: MXAN_5020
            SIL: SPOA0163(mvaA)
            OIH: OB0224
            SAR: SAR2625(mvaA)
            SAS: SAS2431
            SAC: SACOL2560
            SAA: SAUSA300_2483
            SAO: SAOUHSC_02859
            SER: SERP2121
            LMO: lmo0825
            LMF: LMOf2365_0844
            LIN: lin0821
            SPZ: M5005_Spy_0686
            SPH: MGAS10270_Spy0744
            SPI: MGAS10750_Spy0778
            SPJ: MGAS2096_Spy0758
            SPK: MGAS9429_Spy0742
            SPF: SpyM51122(mvaA)
            SPB: M28_Spy0666
            SPR: spr1570(mvaA)
            SPD: SPD_1536
            SAK: SAK_1348
            SMU: SMU.942(mvaA)
            SSA: SSA_0337(mvaA)
            SGO: SGO_0243
            LAC: LBA0627(hmdH)
            LSA: LSA1485(mvaA)
            LSL: LSL_0224
            LDB: Ldb0880(mvaA)
            LCA: LSEI_1786
            BBU: BB0685(mvaA)
            BAF: BAPKO_0729(mvaA)
            GFO: GFO_2973(hmgA)
            RRS: RoseRS_0431
            RCA: Rcas_0981
            MTP: Mthe_0936
            SMR: Smar_0178
            TPE: Tpen_0927
STRUCTURES  PDB: 1R31  1R7I  1T02  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.88
            ExPASy - ENZYME nomenclature database: 1.1.1.88
            ExplorEnz - The Enzyme Database: 1.1.1.88
            ERGO genome analysis and discovery system: 1.1.1.88
            BRENDA, the Enzyme Database: 1.1.1.88
            CAS: 37250-24-1
///
ENTRY       EC 1.1.1.89       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: dihydroxyisovalerate dehydrogenase (isomerizing). Now
            included with EC 1.1.1.86 ketol-acid reductoisomerase (EC 1.1.1.89
            created 1972, deleted 1976)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.89
            ExPASy - ENZYME nomenclature database: 1.1.1.89
            ExplorEnz - The Enzyme Database: 1.1.1.89
            ERGO genome analysis and discovery system: 1.1.1.89
            BRENDA, the Enzyme Database: 1.1.1.89
///
ENTRY       EC 1.1.1.90                 Enzyme
NAME        aryl-alcohol dehydrogenase;
            p-hydroxybenzyl alcohol dehydrogenase;
            benzyl alcohol dehydrogenase;
            coniferyl alcohol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     aryl-alcohol:NAD+ oxidoreductase
REACTION    an aromatic alcohol + NAD+ = an aromatic aldehyde + NADH + H+
            [RN:R01487]
ALL_REAC    R01487 > R01763 R02611 R04304 R05232 R05282 R05347 R05348;
            (other) R02229
SUBSTRATE   aromatic alcohol [CPD:C00947];
            NAD+ [CPD:C00003]
PRODUCT     aromatic aldehyde [CPD:C00193];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     A group of enzymes with broad specificity towards primary alcohols
            with an aromatic or cyclohex-1-ene ring, but with low or no activity
            towards short-chain aliphatic alcohols.
REFERENCE   1  [PMID:5778658]
  AUTHORS   Suhara K, Takemori S, Katagiri M.
  TITLE     The purification and properties of benzylalcohol dehydrogenase from
            Pseudomonas sp.
  JOURNAL   Arch. Biochem. Biophys. 130 (1969) 422-9.
  ORGANISM  Pseudomonas sp.
REFERENCE   2
  AUTHORS   Yamanaka, K. and Minoshima, R.
  TITLE     Identification and characterization of a nicotinamide adenine
            dinucleotide-dependent para-hydroxybenzyl alcohol-dehydrogenase from
            Rhodopseudomonas acidophila M402.
  JOURNAL   Agric. Biol. Chem. 48 (1984) 1161-1171.
  ORGANISM  Rhodopseudomonas acidophila
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
            PATH: map00621  Biphenyl degradation
            PATH: map00622  Toluene and xylene degradation
            PATH: map00930  Caprolactam degradation
ORTHOLOGY   KO: K00055  aryl-alcohol dehydrogenase
GENES       UMA: UM04694.1
            PAP: PSPA7_4414
            ACI: ACIAD1429(areB) ACIAD1578
            CSA: Csal_0349
            NEU: NE0742
            NMU: Nmul_A1473
            EBA: ebA3166(adh)
            SFU: Sfum_0304
            RET: RHE_PD00126(ypd00032)
            RLE: pRL120506(xylB)
            BBT: BBta_6644(xylB)
            CCR: CC_2396
            HNE: HNE_1493 HNE_2119
            BHA: BH2011
            LPL: lp_3054
            LSA: LSA0542
            LSL: LSL_1748(adhC)
            LBR: LVIS_0911
            MSM: MSMEG_2034 MSMEG_4039
            NFA: nfa25980
            RHA: RHA1_ro02648 RHA1_ro02661 RHA1_ro03285(xylB)
            SCO: SCO6442(SC9B5.09) SCO6782(SC6A5.31c)
            FAL: FRAAL4756(xylB)
STRUCTURES  PDB: 1F8F  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.90
            ExPASy - ENZYME nomenclature database: 1.1.1.90
            ExplorEnz - The Enzyme Database: 1.1.1.90
            ERGO genome analysis and discovery system: 1.1.1.90
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.90
            BRENDA, the Enzyme Database: 1.1.1.90
            CAS: 37250-26-3
///
ENTRY       EC 1.1.1.91                 Enzyme
NAME        aryl-alcohol dehydrogenase (NADP+);
            aryl alcohol dehydrogenase (nicotinamide adenine dinucleotide
            phosphate);
            coniferyl alcohol dehydrogenase;
            NADPH-linked benzaldehyde reductase;
            aryl-alcohol dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     aryl-alcohol:NADP+ oxidoreductase
REACTION    an aromatic alcohol + NADP+ = an aromatic aldehyde + NADPH + H+
            [RN:R01488]
ALL_REAC    R01488
SUBSTRATE   aromatic alcohol [CPD:C00947];
            NADP+ [CPD:C00006]
PRODUCT     aromatic aldehyde [CPD:C00193];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on some aliphatic aldehydes, but cinnamaldehyde was the
            best substrate found.
REFERENCE   1  [PMID:4389864]
  AUTHORS   Gross GG, Zenk MH.
  TITLE     [Reduction of aromatic acids to aldehydes and alcohols in the
            cell-free system. 2. Purification and properties of aryl-alcohol:
            NADP-oxidoreductase from Neurospora crassa]
  JOURNAL   Eur. J. Biochem. 8 (1969) 420-5.
  ORGANISM  Neurospora crassa [GN:dncr]
ORTHOLOGY   KO: K05882  aryl-alcohol dehydrogenase (NADP+)
GENES       TET: TTHERM_00962040
            BUR: Bcep18194_A4943 Bcep18194_A5541 Bcep18194_A6427
                 Bcep18194_B0520 Bcep18194_B1321 Bcep18194_B2226
                 Bcep18194_B2826 Bcep18194_B2914 Bcep18194_B3141
            BPM: BURPS1710b_A2461(mocA)
            RET: RHE_CH02454 RHE_CH02805 RHE_CH03774
            RLE: RL2789 RL2983 RL3262(mocA) RL4302 pRL120108
            BRA: BRADO6605
            BBT: BBta_0931
            RDE: RD1_3432
            GBE: GbCGDNIH1_0531
            CGL: NCgl0099(cgl0100)
            RHA: RHA1_ro00240 RHA1_ro01880
            ART: Arth_3453
            FRA: Francci3_3416
            FAL: FRAAL3972 FRAAL4438 FRAAL5526
            KRA: Krad_1519
            SEN: SACE_0624(mocA) SACE_0727(eryBII) SACE_1269
            AVA: Ava_0108 Ava_4145 Ava_5010
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.91
            ExPASy - ENZYME nomenclature database: 1.1.1.91
            ExplorEnz - The Enzyme Database: 1.1.1.91
            ERGO genome analysis and discovery system: 1.1.1.91
            BRENDA, the Enzyme Database: 1.1.1.91
            CAS: 37250-27-4
///
ENTRY       EC 1.1.1.92                 Enzyme
NAME        oxaloglycolate reductase (decarboxylating)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-glycerate:NAD(P)+ oxidoreductase (carboxylating)
REACTION    D-glycerate + NAD(P)+ + CO2 = 2-hydroxy-3-oxosuccinate + NAD(P)H + 2
            H+ [RN:R01749 R01750]
ALL_REAC    R01749 R01750
SUBSTRATE   D-glycerate [CPD:C00258];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            CO2 [CPD:C00011]
PRODUCT     2-hydroxy-3-oxosuccinate [CPD:C03459];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also reduces hydroxypyruvate to D-glycerate and glyoxylate to
            glycolate.
REFERENCE   1  [PMID:4385076]
  AUTHORS   Kohn LD, Jakoby WB.
  TITLE     Tartaric acid metabolism. VI. Crystalline oxaloglycolate reductive
            decarboxylase.
  JOURNAL   J. Biol. Chem. 243 (1968) 2486-93.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.92
            ExPASy - ENZYME nomenclature database: 1.1.1.92
            ExplorEnz - The Enzyme Database: 1.1.1.92
            ERGO genome analysis and discovery system: 1.1.1.92
            BRENDA, the Enzyme Database: 1.1.1.92
            CAS: 37250-28-5
///
ENTRY       EC 1.1.1.93                 Enzyme
NAME        tartrate dehydrogenase;
            mesotartrate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     tartrate:NAD+ oxidoreductase
REACTION    tartrate + NAD+ = oxaloglycolate + NADH + H+ [RN:R06180]
ALL_REAC    R06180 > R02545
SUBSTRATE   tartrate [CPD:C00898];
            NAD+ [CPD:C00003]
PRODUCT     oxaloglycolate [CPD:C03459];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COFACTOR    Manganese [CPD:C00034]
COMMENT     meso-tartrate and (R,R)-tartrate act as substrates. Requires Mn2+
            and a monovalent cation.
REFERENCE   1  [PMID:4297261]
  AUTHORS   Kohn LD, Packman PM, Allen RH, Jakoby WB.
  TITLE     Tartaric acid metabolism. V. Crystalline tartrate dehydrogenase.
  JOURNAL   J. Biol. Chem. 243 (1968) 2479-85.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K00056  tartrate dehydrogenase
GENES       ANI: AN4003.2 AN4822.2
            AFM: AFUA_1G04150 AFUA_8G01160
            AOR: AO090003000929 AO090020000210
            CNE: CNI00190 CNI00890
            EHI: 121.t00016
            ECO: b1800(yeaU)
            ECJ: JW1789(yeaU)
            ECE: Z2843(yeaU)
            ECS: ECs2509
            ECW: EcE24377A_2026(ttuC)
            ECX: EcHS_A1888(ttuC)
            YPE: YPO2496
            YPK: y1692
            YPM: YP_2311(leuB1)
            YPA: YPA_1991
            YPN: YPN_2090
            YPP: YPDSF_1907
            YPS: YPTB2532
            YPI: YpsIP31758_1512
            SSN: SSON_1361(yeaU)
            SBO: SBO_1288(yeaU)
            SDY: SDY_1701(yeaU)
            MSU: MS1105(leuB)
            PST: PSPTO_2662
            PSB: Psyr_2396
            PSP: PSPPH_1578 PSPPH_2554
            PFL: PFL_3649
            PEN: PSEEN2132
            CSA: Csal_2776
            ABO: ABO_0510(tdh)
            MMW: Mmwyl1_3080
            RSO: RSp0996(ttuC2) RSp1612(ttuC)
            REU: Reut_A0462 Reut_B4115 Reut_C5899
            RME: Rmet_0404
            BMA: BMAA0011(ttuC)
            BMV: BMASAVP1_1159(ttuC)
            BML: BMA10299_1440(ttuC)
            BMN: BMA10247_A0014(ttuC)
            BXE: Bxe_B1486 Bxe_B1620 Bxe_C0769 Bxe_C1229
            BVI: Bcep1808_3784
            BUR: Bcep18194_B3173
            BCN: Bcen_4654 Bcen_5152 Bcen_5538
            BCH: Bcen2424_3709 Bcen2424_5707 Bcen2424_5903
            BAM: Bamb_4976 Bamb_5440
            BPS: BPSS0011
            BPM: BURPS1710b_A1518
            BPL: BURPS1106A_A0014
            BPD: BURPS668_A0015
            BTE: BTH_II0013
            PNU: Pnuc_1028
            BPE: BP2291
            BPA: BPP2437 BPP4066
            BBR: BB1886 BB4539
            RFR: Rfer_0440 Rfer_0845 Rfer_2247
            POL: Bpro_1432 Bpro_3066
            PNA: Pnap_1016 Pnap_1632
            AAV: Aave_2087 Aave_2191
            AJS: Ajs_1120 Ajs_2860
            VEI: Veis_2698 Veis_3186
            MPT: Mpe_A0251
            HAR: HEAR3229(yeaU)
            MMS: mma_1237(ttuC)
            AZO: azo3860(yeaU)
            MLO: mll7044
            MES: Meso_4538
            SME: SMa1846
            SMD: Smed_5601
            ATU: Atu3402
            ATC: AGR_L_2841
            RLE: RL0995 pRL110153(ttuC)
            BJA: blr2916 blr6570
            BRA: BRADO2534(yeaU) BRADO5094(ttuC)
            BBT: BBta_2879(yeaU) BBta_5565(ttuC)
            RPA: RPA1742(yeaU)
            RPB: RPB_3626
            RPC: RPC_4630
            RPD: RPD_1841
            RSP: RSP_3388 RSP_3389 RSP_4031
            RSH: Rsph17029_3034 Rsph17029_3035
            PDE: Pden_4970
            NAR: Saro_2935
            MAG: amb3176
            BSU: BG11222(ycsA)
            BHA: BH1070
            BLI: BL03389(ycsA)
            BLD: BLi03766(ycsA)
            BCL: ABC0841
            BPU: BPUM_0399(ycsA)
            OIH: OB0661
            STH: STH2344
            MSM: MSMEG_1986
            MMC: Mmcs_2573
            MKM: Mkms_2618
            MJL: Mjls_2612
            RHA: RHA1_ro08803
            RXY: Rxyl_1183
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.93
            ExPASy - ENZYME nomenclature database: 1.1.1.93
            ExplorEnz - The Enzyme Database: 1.1.1.93
            ERGO genome analysis and discovery system: 1.1.1.93
            BRENDA, the Enzyme Database: 1.1.1.93
            CAS: 37250-29-6
///
ENTRY       EC 1.1.1.94                 Enzyme
NAME        glycerol-3-phosphate dehydrogenase [NAD(P)+];
            L-glycerol-3-phosphate:NAD(P)+ oxidoreductase;
            glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide
            (phosphate));
            glycerol 3-phosphate dehydrogenase (NADP+);
            glycerol-3-phosphate dehydrogenase [NAD(P)+]
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     sn-glycerol-3-phosphate:NAD(P)+ 2-oxidoreductase
REACTION    sn-glycerol 3-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H +
            H+ [RN:R00842 R00844]
ALL_REAC    R00842 R00844
SUBSTRATE   sn-glycerol 3-phosphate [CPD:C00093];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     glycerone phosphate [CPD:C00111];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The enzyme from Escherichia coli shows specificity for the B side of
            NADPH.
REFERENCE   1  [PMID:4389388]
  AUTHORS   Kito M, Pizer LI.
  TITLE     Purification and regulatory properties of the biosynthetic
            L-glycerol 3-phosphate dehydrogenase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 244 (1969) 3316-23.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:355254]
  AUTHORS   Edgar JR, Bell RM.
  TITLE     Biosynthesis in Escherichia coli fo sn-glycerol 3-phosphate, a
            precursor of phospholipid.
  JOURNAL   J. Biol. Chem. 253 (1978) 6348-53.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:28326]
  AUTHORS   Edgar JR, Bell RM.
  TITLE     Biosynthesis in Escherichia coli of sn-glycerol 3-phosphate, a
            precursor of phospholipid. Kinetic characterization of wild type and
            feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate
            dehydrogenase.
  JOURNAL   J. Biol. Chem. 253 (1978) 6354-63.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:6767719]
  AUTHORS   Edgar JR, Bell RM.
  TITLE     Biosynthesis in Escherichia coli of sn-glycerol-3-phosphate, a
            precursor of phospholipid. Further kinetic characterization of wild
            type and feedback-resistant forms of the biosynthetic
            sn-glycerol-3-phosphate dehydrogenase.
  JOURNAL   J. Biol. Chem. 255 (1980) 3492-7.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00057  glycerol-3-phosphate dehydrogenase (NAD(P)+)
GENES       XLA: 444456(MGC83663)
            ECO: b3608(gpsA)
            ECJ: JW3583(gpsA)
            ECE: Z5035(gpsA)
            ECS: ECs4486
            ECC: c4430(gpsA)
            ECI: UTI89_C4149(gpsA)
            ECP: ECP_3709
            ECV: APECO1_2847(gpsA)
            STY: STY4095(gpsA)
            STT: t3819(gpsA)
            SPT: SPA3552(gpsA)
            SEC: SC3623(gpsA)
            STM: STM3700(gpsA)
            YPE: YPO0068(gpsA)
            YPK: y0073(gpsA)
            YPM: YP_0068(gpsA)
            YPA: YPA_3474
            YPN: YPN_3782
            YPP: YPDSF_3837
            YPS: YPTB0064(gpsA)
            YPI: YpsIP31758_0079(gpsA)
            YEN: YE0081(gpsA)
            SFL: SF3647(gpsA)
            SFX: S4121(gpsA)
            SFV: SFV_3923(gpsA)
            SSN: SSON_3797(gpsA)
            SBO: SBO_3614(gpsA)
            SDY: SDY_4041(gpsA)
            ECA: ECA0173(gpsA)
            PLU: plu4838(gpsA)
            WBR: WGLp539(gpsA)
            SGL: SG2184
            ENT: Ent638_0127
            SPE: Spro_4815
            BFL: Bfl604(gpsA)
            BPN: BPEN_626(gpsA)
            HIN: HI0605(gpsA)
            HIT: NTHI0860(gpsA)
            HIP: CGSHiEE_02000(gpsA)
            HDU: HD0660(gpsA)
            HSO: HS_0155(gpsA)
            PMU: PM1431(gspA)
            MSU: MS2213(gpsA)
            APL: APL_1510(gpsA)
            ASU: Asuc_0385
            XFA: XF1802
            XFT: PD1064(gpsA)
            XCC: XCC0204(gpdA)
            XCB: XC_0214
            XCV: XCV0207(gpsA)
            XAC: XAC0222(gpdA)
            XOO: XOO4198(gpdA)
            XOM: XOO_3967(XOO3967)
            VCH: VC2651
            VVU: VV1_1277
            VVY: VV3087
            VPA: VP2832
            VFI: VF2348(gpsA)
            PPR: PBPRA0227
            PAE: PA1614(gpsA)
            PAU: PA14_43640(gpsA)
            PPU: PP_4169(gpsA)
            PPF: Pput_1698
            PST: PSPTO_2213(gpsA)
            PSB: Psyr_2022(gpsA)
            PSP: PSPPH_1994(gpsA)
            PFL: PFL_1741(gpsA)
            PFO: Pfl_4208(gpsA)
            PEN: PSEEN3618(gpsA)
            PMY: Pmen_2467
            PAR: Psyc_1286(gpsA)
            PCR: Pcryo_1096
            PRW: PsycPRwf_0931
            ACI: ACIAD1317(gpsA)
            ACB: A1S_2257
            SON: SO_0053(gpsA)
            SDN: Sden_3695
            SFR: Sfri_4018
            SAZ: Sama_0063
            SBL: Sbal_4329
            SBM: Shew185_0046
            SLO: Shew_3803
            SPC: Sputcn32_0043
            SSE: Ssed_4467
            SPL: Spea_4214
            SHE: Shewmr4_0048
            SHM: Shewmr7_0046
            SHN: Shewana3_0054
            SHW: Sputw3181_4035
            ILO: IL0236(gpsA)
            CPS: CPS_4387(gpsA)
            PHA: PSHAa0370(gpsA)
            PAT: Patl_3615
            SDE: Sde_2098
            PIN: Ping_3207
            MAQ: Maqu_1477
            CBU: CBU_1518(gpsA)
            CBD: COXBU7E912_0466(gpsA)
            LPN: lpg2309(gpsA)
            LPF: lpl2228(gpsA)
            LPP: lpp2257(gpsA)
            MCA: MCA2538(gpsA)
            FTU: FTT0871(gpsA)
            FTF: FTF0871(gpsA)
            FTW: FTW_1309(gpsA)
            FTL: FTL_0372
            FTH: FTH_0365(gpsA)
            FTA: FTA_0395
            FTN: FTN_0397(gpsA)
            TCX: Tcr_1952
            NOC: Noc_0035
            AEH: Mlg_2572
            HHA: Hhal_1214
            HCH: HCH_02763
            CSA: Csal_2490
            ABO: ABO_1488(gpsA)
            MMW: Mmwyl1_2121
            AHA: AHA_0296
            DNO: DNO_0293
            BCI: BCI_0173(gpsA)
            RMA: Rmag_0934
            VOK: COSY_0840(gpsA)
            NME: NMB2060
            NMA: NMA0375(gpsA)
            NGO: NGO2021
            CVI: CV_1129(gpsA)
            RSO: RSc0357(RS03324)
            REU: Reut_A0308(gpsA)
            REH: H16_A0336(gpsA)
            RME: Rmet_0255
            BMA: BMA3204(gpsA)
            BML: BMA10299_A1415(gpsA)
            BXE: Bxe_A4177
            BVI: Bcep1808_2953
            BUR: Bcep18194_A6182(gpsA)
            BCN: Bcen_2239
            BCH: Bcen2424_2853
            BAM: Bamb_2908
            BPS: BPSL0447(gpsA)
            BPM: BURPS1710b_0666(gpsA)
            BTE: BTH_I0420
            PNU: Pnuc_1944
            BPE: BP0603(gpsA)
            BPA: BPP0291(gpsA)
            BBR: BB0294(gpsA)
            RFR: Rfer_1313
            POL: Bpro_0890
            PNA: Pnap_0931
            AAV: Aave_3854
            AJS: Ajs_3501
            VEI: Veis_0042
            MPT: Mpe_A0717
            HAR: HEAR2970(gpsA)
            MMS: mma_3217(gpdA)
            NEU: NE2208(gpsA)
            NET: Neut_0660
            NMU: Nmul_A1126
            EBA: ebA1060(gpsA)
            AZO: azo2814(gpsA)
            DAR: Daro_0615
            TBD: Tbd_2404(gpsA)
            MFA: Mfla_2183
            HPY: HP0961
            HPJ: jhp0895(gpsA)
            HPA: HPAG1_0945
            HHE: HH0794(gpsA)
            HAC: Hac_1037(gpsA)
            WSU: WS2004
            TDN: Tmden_1330
            CJE: Cj1196c(gpsA)
            CJR: CJE1330(gpsA)
            CJJ: CJJ81176_1211(gpsA)
            CJU: C8J_1140(gpsA)
            CJD: JJD26997_0533(gpsA)
            CFF: CFF8240_0775
            CCV: CCV52592_0792
            CHA: CHAB381_0943
            ABU: Abu_0029(gpsA)
            NIS: NIS_0859(gpsA)
            SUN: SUN_1577(gpsA)
            GSU: GSU0006(gpsA)
            GME: Gmet_0008
            GUR: Gura_0007
            PCA: Pcar_0007
            PPD: Ppro_0007
            DVU: DVU3159(gpsA)
            DVL: Dvul_0226
            DDE: Dde_3178
            LIP: LI0828(gpsA)
            DPS: DP0651
            ADE: Adeh_0396
            AFW: Anae109_4181
            MXA: MXAN_1354(gpsA)
            SAT: SYN_01987
            SFU: Sfum_2691
            RPR: RP442(gpsA)
            RTY: RT0429(gpsA)
            RCO: RC0615(gpsA)
            RFE: RF_0677(gpsA)
            RBE: RBE_1225(gpsA)
            RAK: A1C_03305(gpsA)
            RBO: A1I_01190(gpsA)
            RRI: A1G_03470(gpsA)
            OTS: OTBS_1307(gpsA)
            WBM: Wbm0597
            AMA: AM985(gpsA)
            APH: APH_0198(gpsA)
            ERU: Erum6600(gpsA)
            ERW: ERWE_CDS_06920(gpsA)
            ERG: ERGA_CDS_06830(gpsA)
            ECN: Ecaj_0667
            ECH: ECH_0340(gpsA)
            NSE: NSE_0228(gpsA)
            MLO: mlr4225
            MES: Meso_3204
            PLA: Plav_1343
            SME: SMc03229(gpsA)
            SMD: Smed_2964
            ATU: Atu2650(gpsA)
            ATC: AGR_C_4804
            RET: RHE_CH03902(gpsA) RHE_PA00028(ypa00009)
            RLE: RL4493(gpsA)
            BME: BMEI0174
            BMF: BAB1_1889(gpsA)
            BMS: BR1889(gpsA)
            BMB: BruAb1_1866(gpsA)
            OAN: Oant_0973
            BJA: blr0568(gpsA)
            BRA: BRADO0303(gpsA)
            BBT: BBta_0290(gpsA)
            RPA: RPA0254(gpdA)
            RPB: RPB_0316
            RPC: RPC_0045
            RPD: RPD_0471
            RPE: RPE_0066
            NWI: Nwi_0469(gpsA)
            NHA: Nham_0560
            BHE: BH01260(gpsA)
            BQU: BQ01190(gpsA)
            XAU: Xaut_1156
            CCR: CC_0070
            SIL: SPO3855(gpsA)
            SIT: TM1040_2830
            RSP: RSP_1510
            RSH: Rsph17029_0162
            JAN: Jann_4079
            RDE: RD1_0469(gpsA)
            PDE: Pden_1999
            MMR: Mmar10_0038
            HNE: HNE_0982
            ZMO: ZMO1905(gpsA)
            NAR: Saro_2784
            SAL: Sala_0199 Sala_2874
            SWI: Swit_1932
            ELI: ELI_09165
            GOX: GOX1880
            GBE: GbCGDNIH1_2427
            RRU: Rru_A3571
            MAG: amb4006
            MGM: Mmc1_0741
            ABA: Acid345_2137
            SUS: Acid_0313
            BSU: BG11366(gpsA)
            BHA: BH1640(gpsA)
            BAN: BA1526(gpsA)
            BAR: GBAA1526(gpsA)
            BAA: BA_2046
            BAT: BAS1415
            BCE: BC1505(gpsA)
            BCA: BCE_1632(gpsA)
            BCZ: BCZK1387(gpsA)
            BCY: Bcer98_1228
            BTK: BT9727_1387(gpsA)
            BTL: BALH_1360(gpsA)
            BLI: BL02791(gpsA)
            BLD: BLi02420(gpsA)
            BCL: ABC1878(gpsA)
            BPU: BPUM_2014(gpsA)
            OIH: OB1796(gpsA)
            GKA: GK2220
            SAU: SA1306(gpsA)
            SAV: SAV1474(gpsA)
            SAM: MW1363(gpsA)
            SAR: SAR1483(gpsA)
            SAS: SAS1415
            SAA: SAUSA300_1363(gpsA)
            SAO: SAOUHSC_01491
            SAJ: SaurJH9_1531
            SAH: SaurJH1_1561
            SEP: SE1162
            SER: SERP1042(gpsA)
            SHA: SH1437(gpsA)
            SSP: SSP1272
            LMO: lmo1936(gpsA)
            LMF: LMOf2365_1965(gpsA)
            LIN: lin2050(gpsA)
            LWE: lwe1962(gpsA)
            LLA: L0016(gpdA)
            LLC: LACR_1461
            LLM: llmg_1114(gpsA)
            SPY: SPy_0226(gpsA)
            SPZ: M5005_Spy_0193 M5005_Spy_0194(gpsA)
            SPM: spyM18_0212(gpdA)
            SPG: SpyM3_0161(gpdA)
            SPS: SPs0167
            SPH: MGAS10270_Spy0193(gpsA)
            SPI: MGAS10750_Spy0189(gpsA)
            SPJ: MGAS2096_Spy0206(gpsA)
            SPK: MGAS9429_Spy0195(gpsA)
            SPF: SpyM50173(glyC)
            SPA: M6_Spy0225(gpsA)
            SPB: M28_Spy0188(gpsA)
            SPN: SP_2091
            SPR: spr1902(gpdA)
            SPD: SPD_1918(gpsA)
            SAG: SAG0407(gpsA)
            SAN: gbs0442
            SAK: SAK_0480(gpsA)
            SMU: SMU.323(gpsA)
            STC: str1832(gpsA)
            STL: stu1832(gpsA)
            SSA: SSA_2168(gpsA)
            SGO: SGO_0164
            LPL: lp_0756(gpsA)
            LJO: LJ0851
            LAC: LBA0678(gpdA)
            LSA: LSA0518(gps)
            LSL: LSL_0372(gpsA)
            LDB: Ldb0612(gpsA1) Ldb1959(gpsA2)
            LBU: LBUL_0547 LBUL_1823
            LBR: LVIS_0643
            LCA: LSEI_0947
            LRE: Lreu_0371
            EFA: EF1747(gpsA)
            OOE: OEOE_0564
            STH: STH1681
            CAC: CAC1712(gpsA)
            CPE: CPE1754(gpdA)
            CPF: CPF_2007
            CPR: CPR_1725
            CTC: CTC01139(gpsA)
            CTH: Cthe_1022
            CDF: CD2630(glyC)
            CBO: CBO2518(glyC)
            CBE: Cbei_1135
            AMT: Amet_2855
            CHY: CHY_1917(gpsA)
            DSY: DSY2249
            DRM: Dred_1162
            SWO: Swol_1323
            TTE: TTE1617(gpsA)
            MTA: Moth_1320
            MPU: MYPU_1240(gpsA)
            MPE: MYPE2300(gpsA)
            MGA: MGA_1133(GpsA)
            MMY: MSC_0409(gpsA)
            MMO: MMOB4820(gpsA)
            MSY: MS53_0654(gpsA)
            MCP: MCAP_0576(gpsA)
            UUR: UU382(gpsA)
            POY: PAM241(gpsA)
            AYW: AYWB_480(gpsA)
            MFL: Mfl200
            MTU: Rv0564c(gpsA) Rv2982c(gpdA2)
            MTC: MT0590(gpdA1) MT3060(gpsA)
            MBO: Mb0579c(gpsA) Mb3006c(gpsA)
            MBB: BCG_0609c(gpdA1) BCG_3003c(gpdA2)
            MLE: ML1679(gpdA)
            MPA: MAP3020c(gpdA2) MAP4061c(gpdA1)
            MAV: MAV_4577
            MSM: MSMEG_1140
            MVA: Mvan_0995 Mvan_2141
            MGI: Mflv_4221 Mflv_5249
            MMC: Mmcs_0774 Mmcs_1927
            MKM: Mkms_0788 Mkms_1973
            MJL: Mjls_0769 Mjls_1907
            CGL: NCgl1266(gpsA)
            CGB: cg1492(gpsA)
            CEF: CE1430
            CDI: DIP1130(gpsA)
            CJK: jk0920(gpsA2) jk1218(gpsA1)
            NFA: nfa42060
            RHA: RHA1_ro02396(gpdA1) RHA1_ro06505(gpdA2)
            SCO: SCO5559(gpsA)
            SMA: SAV2680(gpsA)
            TWH: TWT506(gpsA)
            TWS: TW256(gpsA)
            LXX: Lxx09700(gpdA)
            ART: Arth_2515
            AAU: AAur_2482
            PAC: PPA2315
            NCA: Noca_3293
            TFU: Tfu_0631
            FRA: Francci3_3614
            FAL: FRAAL5821(gpsA)
            ACE: Acel_1587
            KRA: Krad_1615
            SEN: SACE_6137(gpdA2)
            STP: Strop_1266
            BLO: BL0346
            BAD: BAD_0185
            FNU: FN0906
            CTR: CT714(gpdA)
            CTA: CTA_0776(gpsA)
            CMU: TC0087
            CPN: CPn0855(gpdA)
            CPA: CP1014
            CPJ: CPj0855(gpdA)
            CPT: CpB0884
            CCA: CCA00912(gpdA)
            CAB: CAB880
            CFE: CF0102(gpdA)
            PCU: pc0083(gpsA)
            BGA: BG0367(gpsA)
            BAF: BAPKO_0377(gpsA)
            TPA: TP1009
            TDE: TDE2090
            LIL: LA1112(gpsA1) LA3939(gpsA2) LA4264(gpsA3)
            LIC: LIC13145(gpsA) LIC13412(plsB)
            LBJ: LBJ_0395(gpsA)
            LBL: LBL_2682(gpsA)
            SYN: slr1755(gpsA)
            SYF: Synpcc7942_2522
            SYR: SynRCC307_1214
            CYA: CYA_0480
            CYB: CYB_0350
            TEL: tll2111
            GVI: glr3667(glpD)
            ANA: all1693
            AVA: Ava_1163
            TER: Tery_1811
            BTH: BT_2123
            BFR: BF3811
            BFS: BF3603
            PGI: PG1369(gpsA)
            SRU: SRU_1473 SRU_1481
            FPS: FP0141(gpsA)
            CTE: CT0092(gpsA)
            CCH: Cag_2026
            CPH: Cpha266_2580
            PVI: Cvib_1699
            PLT: Plut_2057
            DET: DET1397(gpsA)
            DEH: cbdb_A1356(gpsA)
            DEB: DehaBAV1_1206
            DRA: DR_2621
            DGE: Dgeo_2043
            TTH: TTC1378
            TTJ: TTHA1740
            AAE: aq_1634(gspA)
            TMA: TM0378(gpsA)
            TPT: Tpet_0529
            TME: Tmel_1790
            FNO: Fnod_1014
            MTH: MTH368
            MSI: Msm_1540
            AFU: AF0871(gpsA)
STRUCTURES  PDB: 1TXG  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.94
            ExPASy - ENZYME nomenclature database: 1.1.1.94
            ExplorEnz - The Enzyme Database: 1.1.1.94
            ERGO genome analysis and discovery system: 1.1.1.94
            BRENDA, the Enzyme Database: 1.1.1.94
            CAS: 37250-30-9
///
ENTRY       EC 1.1.1.95                 Enzyme
NAME        phosphoglycerate dehydrogenase;
            D-3-phosphoglycerate:NAD+ oxidoreductase;
            alpha-phosphoglycerate dehydrogenase;
            3-phosphoglycerate dehydrogenase;
            3-phosphoglyceric acid dehydrogenase;
            D-3-phosphoglycerate dehydrogenase;
            glycerate 3-phosphate dehydrogenase;
            glycerate-1,3-phosphate dehydrogenase;
            phosphoglycerate oxidoreductase;
            phosphoglyceric acid dehydrogenase;
            SerA;
            3-phosphoglycerate:NAD+ 2-oxidoreductase;
            SerA 3PG dehydrogenase;
            3PHP reductase;
            alphaKG reductase;
            D- and L-HGA
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-phospho-D-glycerate:NAD+ 2-oxidoreductase
REACTION    (1) 3-phospho-D-glycerate + NAD+ = 3-phosphonooxypyruvate + NADH +
            H+ [RN:R02607];
            (2) 2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH + H+
ALL_REAC    R02607 > R01513
SUBSTRATE   3-phospho-D-glycerate [CPD:C00197];
            NAD+ [CPD:C00003];
            2-hydroxyglutarate [CPD:C02630]
PRODUCT     3-phosphonooxypyruvate [CPD:C03232];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            2-oxoglutarate [CPD:C00026]
COMMENT     This enzyme catalyses the first committed step in the phosphoserine
            pathway of serine biosynthesis in Escherichia coli [2,3]. Reaction
            (1) occurs predominantly in the reverse direction and is inhibited
            by serine and glycine. The enzyme is unusual in that it also acts as
            a D- and L-2-hydroxyglutarate dehydrogenase (with the D-form being
            the better substrate) and as a 2-oxoglutarate reductase [3]. It has
            been postulated [3] that the cellular 2-oxoglutarate concentration
            may regulate serine biosynthesis and one-carbon metabolism directly
            by modulating the activity of this enzyme.
REFERENCE   1  [PMID:4384871]
  AUTHORS   Sugimoto E, Pizer LI.
  TITLE     The mechanism of end product inhibition of serine biosynthesis. I.
            Purification and kinetics of phosphoglycerate dehydrogenase.
  JOURNAL   J. Biol. Chem. 243 (1968) 2081-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:14086727]
  AUTHORS   PIZER LI.
  TITLE     THE PATHWAY AND CONTROL OF SERINE BIOSYNTHESIS IN ESCHERICHIA COLI.
  JOURNAL   J. Biol. Chem. 238 (1963) 3934-44.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:8550422]
  AUTHORS   Zhao G, Winkler ME.
  TITLE     A novel alpha-ketoglutarate reductase activity of the serA-encoded
            3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its
            possible implications for human 2-hydroxyglutaric aciduria.
  JOURNAL   J. Bacteriol. 178 (1996) 232-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:7719856]
  AUTHORS   Schuller DJ, Grant GA, Banaszak LJ.
  TITLE     The allosteric ligand site in the Vmax-type cooperative enzyme
            phosphoglycerate dehydrogenase.
  JOURNAL   Nat. Struct. Biol. 2 (1995) 69-76.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K00058  D-3-phosphoglycerate dehydrogenase
GENES       HSA: 26227(PHGDH)
            MMU: 236539(Phgdh)
            RNO: 58835(Phgdh)
            CFA: 607890(LOC607890)
            GGA: 424381(PHGDH)
            XTR: 493558(ctbp2)
            DRE: 321928(zgc:65956)
            SPU: 590971(LOC590971)
            DME: Dmel_CG6287
            CEL: C31C9.2
            ATH: AT3G19480 AT4G34200(EDA9)
            OSA: 4337230 4341713
            CME: CMC149C
            SCE: YER081W(SER3) YIL074C(SER33)
            AGO: AGOS_ACL032C
            PIC: PICST_43416(MDH99) PICST_87754(SER3)
            CGR: CAGL0M12837g
            SPO: SPCC4G3.01
            AFM: AFUA_1G14400 AFUA_2G04490 AFUA_4G11840 AFUA_5G05500
            AOR: AO090009000711
            CNE: CNA07520
            UMA: UM01233.1
            DDI: DDB_0230052(serA)
            LMA: LmjF03.0030
            EHI: 130.t00007 130.t00010 27.t00049 555.t00001 782.t00001
            ECO: b2913(serA)
            ECJ: JW2880(serA)
            ECE: Z4251(serA)
            ECS: ECs3784
            ECC: c3494(serA)
            ECI: UTI89_C1154(ycdW) UTI89_C3212 UTI89_C3299(serA)
            ECP: ECP_2824 ECP_2905
            ECV: APECO1_3616(serA) APECO1_3693
            ECW: EcE24377A_3240(serA)
            ECX: EcHS_A3071(serA)
            STY: STY3218(serA)
            STT: t2980(serA)
            SPT: SPA2933(serA)
            SEC: SC3003(serA)
            STM: STM3062(serA)
            YPE: YPO0914(serA) YPO1288
            YPK: y2896 y3301(serA)
            YPM: YP_1303(serA1) YP_3611(serA2)
            YPA: YPA_0353 YPA_1004
            YPN: YPN_2690 YPN_3113
            YPS: YPTB1320 YPTB3189(serA)
            YPI: YpsIP31758_0856(serA)
            SFL: SF2898(serA)
            SFX: S3098(serA)
            SFV: SFV_2960(serA)
            SSN: SSON_3065(serA)
            SBO: SBO_2700 SBO_3080(serA)
            SDY: SDY_3169(serA)
            ECA: ECA3905(serA)
            PLU: plu3605(serA)
            SGL: SG2009
            HIT: NTHI0596(serA)
            HSO: HS_0122(serA)
            PMU: PM1671(serA)
            MSU: MS1743(serA)
            APL: APL_1452(serA)
            XFA: XF2206
            XFT: PD1255(serA)
            XCC: XCC0020(serA) XCC1825(serA)
            XCB: XC_0020 XC_2364
            XCV: XCV0023(serA) XCV1890(serA)
            XAC: XAC0022(serA) XAC1844(serA)
            XOO: XOO2143(serA) XOO4585(serA)
            XOM: XOO_2012(XOO2012) XOO_4321(XOO4321)
            VCH: VC2481
            VCO: VC0395_A2057(serA)
            VVU: VV1_1546
            VVY: VV2851
            VPA: VP2593
            VFI: VF2106
            PPR: PBPRA3123 PBPRA3124
            PAE: PA0316(serA)
            PAU: PA14_04110(serA)
            PPU: PP_2533 PP_5155(serA)
            PST: PSPTO_5294(serA)
            PSB: Psyr_4852
            PSP: PSPPH_4885(serA)
            PFL: PFL_5911
            PFO: Pfl_2987 Pfl_5387
            PEN: PSEEN5248(serA)
            PAR: Psyc_0369(serA)
            ACI: ACIAD3302(serA)
            SON: SO_0862(serA)
            SDN: Sden_3097
            SFR: Sfri_0558
            SHE: Shewmr4_0718
            SHM: Shewmr7_3304
            SHN: Shewana3_0763 Shewana3_3416
            ILO: IL2104(serA)
            CPS: CPS_1544(serA)
            PHA: PSHAa0666(serA)
            PAT: Patl_1156
            SDE: Sde_1333 Sde_3388
            CBU: CBU_1732
            LPN: lpg0242(serA)
            LPF: lpl0296
            LPP: lpp0312
            FTU: FTT1230(serA)
            FTF: FTF1230(serA)
            FTL: FTL_0714
            FTH: FTH_0716(serA)
            FTA: FTA_0754
            TCX: Tcr_0627
            NOC: Noc_0173 Noc_2032
            AEH: Mlg_0925
            HCH: HCH_01646(serA)
            ABO: ABO_0068(serA)
            AHA: AHA_2731
            VOK: COSY_0580(serA)
            CVI: CV_1724
            RSO: RSc0016(serA1) RSp0505(serA2)
            REU: Reut_A3421 Reut_B3530 Reut_B4615 Reut_B4747 Reut_C5898
            REH: H16_A0185 H16_A3712(serA1) H16_B0347(serA2) H16_B0466(serA3)
                 H16_B0824(serA4) H16_B0841(serA5) H16_B1819(serA6)
            RME: Rmet_3578 Rmet_4234 Rmet_4537
            BXE: Bxe_A2676 Bxe_B1744 Bxe_B1896 Bxe_B2128
            BUR: Bcep18194_A3727 Bcep18194_A6308 Bcep18194_A6483
                 Bcep18194_B0500 Bcep18194_B0965 Bcep18194_B1312
                 Bcep18194_C7658
            BCN: Bcen_3835 Bcen_5465
            BCH: Bcen2424_3132 Bcen2424_4533 Bcen2424_5397
            BAM: Bamb_3187
            BPS: BPSL0116 BPSL1250(serA)
            BPM: BURPS1710b_0341(serA1) BURPS1710b_1481
            BPL: BURPS1106A_1345(serA)
            BPD: BURPS668_1338(serA)
            BTE: BTH_I0123 BTH_I2885(serA) BTH_II0982
            BPE: BP0155(serA)
            BPA: BPP2132 BPP4001(serA)
            BBR: BB1529 BB4474(serA) BB4731
            RFR: Rfer_1867 Rfer_2996
            POL: Bpro_2956 Bpro_5117
            MPT: Mpe_A1136
            HAR: HEAR3340 HEAR3458(tkrA)
            MMS: mma_3685(serA)
            NEU: NE0334 NE1688(serA)
            NET: Neut_0433 Neut_1571
            NMU: Nmul_A0428 Nmul_A2191
            EBA: ebA6869(serA)
            AZO: azo3099(serA)
            TBD: Tbd_0950
            MFA: Mfla_0724
            HPY: HP0096 HP0397(serA)
            HPA: HPAG1_0096 HPAG1_0820 HPAG1_0995 HPAG1_1378
            HHE: HH0135(serA) HH0178
            HAC: Hac_0455(serA) Hac_1481
            WSU: WS1313(serA) WS2143
            TDN: Tmden_0875
            CJE: Cj0891c(serA)
            CJR: CJE0970(serA)
            CJJ: CJJ81176_0900(serA)
            CJU: C8J_0828(serA)
            CJD: JJD26997_0922(serA)
            CFF: CFF8240_1248(serA)
            CCV: CCV52592_0512(serA)
            CHA: CHAB381_0480(serA)
            CCO: CCC13826_1569(serA)
            ABU: Abu_2048(serA)
            NIS: NIS_0664
            SUN: SUN_0551
            GSU: GSU1198(serA)
            GME: Gmet_2378
            PCA: Pcar_0417 Pcar_3115
            DVU: DVU0339
            DDE: Dde_3689
            LIP: LI0671(serA)
            BBA: Bd1461(serA) Bd2892(serA)
            DPS: DP1709
            ADE: Adeh_1262
            MXA: MXAN_6356(serA)
            SAT: SYN_00123
            SFU: Sfum_3136 Sfum_3649
            PUB: SAR11_1366(serA)
            MLO: mll1021 mll3875 mlr3367 mlr7269
            MES: Meso_3161
            SME: SMa1347 SMc00641(serA) SMc01622
            ATU: Atu3706(serA) Atu5399(serA)
            ATC: AGR_L_2264 AGR_pAT_578(serA)
            RET: RHE_CH03454(serA) RHE_PC00143 RHE_PF00336
                 RHE_PF00379(ypf00200)
            RLE: RL0189 RL3960 pRL100390 pRL120588 pRL120632
            BME: BMEI0349 BMEII0813
            BMF: BAB1_1697 BAB2_0783(serA-2)
            BMS: BR1685(serA-1) BRA0453(serA-2)
            BMB: BruAb1_1670(serA-1) BruAb2_0769(serA-2)
            BOV: BOV_1629(serA)
            BJA: bll7401(serA) bll7965 blr3173
            BRA: BRADO1153 BRADO1760(serA) BRADO2535 BRADO3813 BRADO3860
                 BRADO4794 BRADO4922 BRADO5741 BRADO5948(serA)
            BBT: BBta_1826(serA) BBta_2073(serA) BBta_2880 BBta_3129 BBta_3231
                 BBta_4121 BBta_6253 BBta_6900
            RPA: RPA1744(serA) RPA2975(serA1) RPA4308(serA2)
            RPB: RPB_1315
            RPC: RPC_1669 RPC_4106
            RPD: RPD_3905
            RPE: RPE_4160
            NWI: Nwi_2968
            NHA: Nham_1119
            CCR: CC_3215
            SIL: SPO3355(serA)
            SIT: TM1040_3021
            RSP: RSP_1352 RSP_3407(serA) RSP_3447
            JAN: Jann_0261
            RDE: RD1_0197(serA) RD1_1204 RD1_3633(serA)
            HNE: HNE_3126(serA)
            ZMO: ZMO1685(serA) ZMO1883(serA)
            NAR: Saro_2680
            SAL: Sala_0616
            ELI: ELI_01970
            GOX: GOX0065 GOX0218 GOX1300
            RRU: Rru_A2002 Rru_A2456
            MAG: amb3193
            MGM: Mmc1_1423
            ABA: Acid345_0115
            BSU: BG10509(serA) BG13475(yoaD)
            BHA: BH1602
            BAN: BA3320
            BAR: GBAA3320
            BAA: BA_3822
            BAT: BAS3078
            BCE: BC3248
            BCA: BCE_3284
            BCZ: BCZK1299(serA) BCZK2968(serA)
            BTK: BT9727_3022(serA)
            BTL: BALH_1270(serA) BALH_2945(serA)
            BLI: BL00647(serA)
            BLD: BLi02446(serA)
            BCL: ABC0220 ABC1843(serA)
            BAY: RBAM_021220(serA)
            BPU: BPUM_2039(serA)
            OIH: OB2626(serA)
            GKA: GK2247
            SAU: SA1545(serA)
            SAV: SAV1724(serA)
            SAM: MW1666(serA)
            SAR: SAR1801
            SAS: SAS1650
            SAC: SACOL1773(serA)
            SAB: SAB1582
            SAA: SAUSA300_1670(serA)
            SAO: SAOUHSC_01833
            SAJ: SaurJH9_1779
            SAH: SaurJH1_1814
            SEP: SE1401
            SER: SERP1288(serA)
            SHA: SH1200(serA)
            SSP: SSP1039
            LMO: lmo2824
            LMF: LMOf2365_2815
            LIN: lin2956
            LWE: lwe2754
            LLA: L0084(serA)
            LLC: LACR_0620
            LLM: llmg_0566(serA)
            SAG: SAG1566
            SAN: gbs1619
            SAK: SAK_1584
            SMU: SMU.1653(serA)
            STC: str1527(serA)
            STL: stu1527(serA)
            SSA: SSA_1713(serA) SSA_2085
            LPL: lp_0203(serA1) lp_2790(serA3)
            LSA: LSA0922(serA)
            LSL: LSL_0092(serA)
            STH: STH9
            CAC: CAC0015(serA) CAC0089(serA)
            CPE: CPE0054(serA)
            CPF: CPF_0061
            CPR: CPR_0064
            CTC: CTC00694
            CNO: NT01CX_0728(serA)
            CDF: CD0995(serA)
            CBO: CBO1127(serA)
            CBA: CLB_1164(serA)
            CBH: CLC_1176(serA)
            CBF: CLI_1213(serA)
            CKL: CKL_0436(serA)
            CHY: CHY_2698(serA)
            DSY: DSY0969 DSY4683
            SWO: Swol_0009
            TTE: TTE2613(serA2)
            MTA: Moth_0020
            MTU: Rv0728c(serA2) Rv2996c(serA1)
            MTC: MT0753 MT3074(serA)
            MBO: Mb0749c(serA2) Mb3020c(serA1)
            MBB: BCG_0778c(serA2) BCG_3017c(serA1)
            MLE: ML1692(serA)
            MPA: MAP3033c(serA) MAP4194c
            MAV: MAV_3847(serA)
            MSM: MSMEG_2378(serA)
            MVA: Mvan_2128
            MGI: Mflv_4234
            MMC: Mmcs_1910
            CGL: NCgl1235(cgl1284)
            CGB: cg1451(serA)
            CEF: CE1379
            CDI: DIP1104(serA)
            CJK: jk1291(serA)
            NFA: nfa42210(serA)
            RHA: RHA1_ro02903(serA1) RHA1_ro03298 RHA1_ro04630
                 RHA1_ro06489(serA2) RHA1_ro08844(serA3) RHA1_ro08891
            SCO: SCO5515(SC8D9.27)
            SMA: SAV2730(serA) SAV7481
            LXX: Lxx13140(serA)
            CMI: CMM_1100(serA)
            AAU: AAur_2506(serA)
            PAC: PPA1272 PPA2251
            NCA: Noca_3385
            TFU: Tfu_0614
            FRA: Francci3_3637
            FAL: FRAAL5848(serA) FRAAL6376
            ACE: Acel_0709
            SEN: SACE_2049(serA) SACE_4226(serA) SACE_4558(serA)
                 SACE_4605(serA) SACE_5219(serA) SACE_6155(serA)
            STP: Strop_1236
            BLO: BL1313(serA)
            BAD: BAD_1112(serA)
            RXY: Rxyl_0837
            FNU: FN0965
            RBA: RB10004(serA) RB6248(serA) RB6394
            LIL: LA1126 LA1629 LA1911(serA)
            LIC: LIC11992(serA) LIC12554
            LBJ: LBJ_1496
            LBL: LBL_1720
            SYN: sll1908(serA)
            SYW: SYNW0533(serA)
            SYC: syc2486_c(serA)
            SYF: Synpcc7942_1501
            SYD: Syncc9605_2150
            SYE: Syncc9902_0527
            SYG: sync_2256(serA)
            SYR: SynRCC307_1844(serA)
            SYX: SynWH7803_1981(serA)
            CYA: CYA_1354(serA)
            CYB: CYB_1383(serA)
            TEL: tlr0325(serA)
            GVI: glr2139(serA)
            ANA: alr1890
            AVA: Ava_3759
            PMA: Pro1436(serA)
            PMM: PMM1354(serA)
            PMT: PMT1431(serA)
            PMN: PMN2A_0926
            PMI: PMT9312_1452
            PMB: A9601_04421 A9601_15551(serA)
            PMC: P9515_04531 P9515_15151(serA)
            PMF: P9303_05241(serA) P9303_21511
            PMG: P9301_04111 P9301_15401(serA)
            PME: NATL1_04431 NATL1_17821(serA)
            TER: Tery_4196
            BTH: BT_1152
            BFR: BF2019
            BFS: BF2073(serA)
            PGI: PG1279
            CHU: CHU_0996(serA) CHU_1630(ldhA)
            GFO: GFO_0734(serA) GFO_1469(serA) GFO_3512(serA)
            FPS: FP0639(serA)
            CCH: Cag_1377
            DET: DET0599(serA)
            DEH: cbdb_A580(serA)
            RRS: RoseRS_0271
            DRA: DR_1291
            DGE: Dgeo_0710
            TTH: TTC0586 TTC1209
            TTJ: TTHA0952
            AAE: aq_1905(serA)
            TMA: TM0327 TM1401
            TME: Tmel_0112
            FNO: Fnod_0103
            MMP: MMP1588(serA)
            MMQ: MmarC5_1821
            MMZ: MmarC7_0835
            MAE: Maeo_0567
            MVN: Mevan_0900
            MAC: MA0592(serA)
            MBA: Mbar_A1431
            MMA: MM_1753
            MTP: Mthe_1224
            MHU: Mhun_3063
            MEM: Memar_1850
            MST: Msp_1145(serA)
            MSI: Msm_0457
            MKA: MK0297 MK0319 MK0320(serA)
            HAL: VNG2424G(serA1)
            HMA: rrnAC0362(serA4) rrnAC1762(serA2) rrnAC2056(serA3)
                 rrnAC2451(serA5) rrnAC2696(serA1)
            HWA: HQ1043A(serA) HQ2066A(serA) HQ2909A(serA)
            NPH: NP0272A(serA) NP4720A
            PTO: PTO0372
            PHO: PH0520
            PAB: PAB0514(serA-like) PAB1008
            PFU: PF0370 PF1394
            TKO: TK0551 TK1966
            RCI: RCIX1538(serA)
            SSO: SSO0905(serA-1) SSO3187(serA-2)
            STO: ST0694 ST1218
            SAI: Saci_0247 Saci_1368
            PAI: PAE1038(serA) PAE3320(serA)
STRUCTURES  PDB: 1PSD  1SC6  1WWK  1YBA  1YGY  2G76  2P9C  2P9E  2P9G  2PA3  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.95
            ExPASy - ENZYME nomenclature database: 1.1.1.95
            ExplorEnz - The Enzyme Database: 1.1.1.95
            ERGO genome analysis and discovery system: 1.1.1.95
            BRENDA, the Enzyme Database: 1.1.1.95
            CAS: 9075-29-0
///
ENTRY       EC 1.1.1.96                 Enzyme
NAME        diiodophenylpyruvate reductase;
            aromatic alpha-keto acid;
            KAR;
            2-oxo acid reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-(3,5-diiodo-4-hydroxyphenyl)lactate:NAD+ oxidoreductase
REACTION    3-(3,5-diiodo-4-hydroxyphenyl)lactate + NAD+ =
            3-(3,5-diiodo-4-hydroxyphenyl)pyruvate + NADH + H+ [RN:R03431]
ALL_REAC    R03431
SUBSTRATE   3-(3,5-diiodo-4-hydroxyphenyl)lactate [CPD:C04367];
            NAD+ [CPD:C00003]
PRODUCT     3-(3,5-diiodo-4-hydroxyphenyl)pyruvate [CPD:C01244];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Substrates contain an aromatic ring with a pyruvate side chain. The
            most active substrates are halogenated derivatives. Compounds with
            hydroxy or amino groups in the 3 or 5 position are inactive.
REFERENCE   1  [PMID:5935348]
  AUTHORS   Zannoni VG, Weber WW.
  TITLE     Isolation and properties of aromatic alpha-keto acid reductase.
  JOURNAL   J. Biol. Chem. 241 (1966) 1340-4.
  ORGANISM  guinea pig
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.96
            ExPASy - ENZYME nomenclature database: 1.1.1.96
            ExplorEnz - The Enzyme Database: 1.1.1.96
            ERGO genome analysis and discovery system: 1.1.1.96
            BRENDA, the Enzyme Database: 1.1.1.96
            CAS: 37250-31-0
///
ENTRY       EC 1.1.1.97                 Enzyme
NAME        3-hydroxybenzyl-alcohol dehydrogenase;
            m-hydroxybenzyl alcohol dehydrogenase;
            m-hydroxybenzyl alcohol (NADP+) dehydrogenase;
            m-hydroxybenzylalcohol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-hydroxybenzyl-alcohol:NADP+ oxidoreductase
REACTION    3-hydroxybenzyl alcohol + NADP+ = 3-hydroxybenzaldehyde + NADPH + H+
            [RN:R04136]
ALL_REAC    R04136
SUBSTRATE   3-hydroxybenzyl alcohol [CPD:C03351];
            NADP+ [CPD:C00006]
PRODUCT     3-hydroxybenzaldehyde [CPD:C03067];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4335290]
  AUTHORS   Forrester PI, Gaucher GM.
  TITLE     m-Hydroxybenzyl alcohol dehydrogenase from Penicillium urticae.
  JOURNAL   Biochemistry. 11 (1972) 1108-14.
  ORGANISM  Penicillium urticae
PATHWAY     PATH: map00622  Toluene and xylene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.97
            ExPASy - ENZYME nomenclature database: 1.1.1.97
            ExplorEnz - The Enzyme Database: 1.1.1.97
            ERGO genome analysis and discovery system: 1.1.1.97
            BRENDA, the Enzyme Database: 1.1.1.97
            CAS: 9075-73-4
///
ENTRY       EC 1.1.1.98                 Enzyme
NAME        (R)-2-hydroxy-fatty-acid dehydrogenase;
            D-2-hydroxy fatty acid dehydrogenase;
            2-hydroxy fatty acid oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-2-hydroxystearate:NAD+ oxidoreductase
REACTION    (R)-2-hydroxystearate + NAD+ = 2-oxostearate + NADH + H+ [RN:R03021]
ALL_REAC    R03021
SUBSTRATE   (R)-2-hydroxystearate [CPD:C03042];
            NAD+ [CPD:C00003]
PRODUCT     2-oxostearate [CPD:C00869];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:5443694]
  AUTHORS   Levis GM.
  TITLE     2-Hydroxy fatty acid oxidases of rat kidney.
  JOURNAL   Biochem. Biophys. Res. Commun. 38 (1970) 470-7.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.98
            ExPASy - ENZYME nomenclature database: 1.1.1.98
            ExplorEnz - The Enzyme Database: 1.1.1.98
            ERGO genome analysis and discovery system: 1.1.1.98
            BRENDA, the Enzyme Database: 1.1.1.98
            CAS: 37250-32-1
///
ENTRY       EC 1.1.1.99                 Enzyme
NAME        (S)-2-hydroxy-fatty-acid dehydrogenase;
            dehydrogenase, L-2-hydroxy fatty acid;
            L-2-hydroxy fatty acid dehydrogenase;
            2-hydroxy fatty acid oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-2-hydroxystearate:NAD+ oxidoreductase
REACTION    (S)-2-hydroxystearate + NAD+ = 2-oxostearate + NADH + H+ [RN:R03022]
ALL_REAC    R03022
SUBSTRATE   (S)-2-hydroxystearate [CPD:C03045];
            NAD+ [CPD:C00003]
PRODUCT     2-oxostearate [CPD:C00869];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4909888]
  AUTHORS   Huang WY, Tang J.
  TITLE     Carboxyl-terminal sequence of human gastricsin and pepsin.
  JOURNAL   J. Biol. Chem. 245 (1970) 2189-93.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.99
            ExPASy - ENZYME nomenclature database: 1.1.1.99
            ExplorEnz - The Enzyme Database: 1.1.1.99
            ERGO genome analysis and discovery system: 1.1.1.99
            BRENDA, the Enzyme Database: 1.1.1.99
            CAS: 37250-33-2
///
ENTRY       EC 1.1.1.100                Enzyme
NAME        3-oxoacyl-[acyl-carrier-protein] reductase;
            beta-ketoacyl-[acyl-carrier protein](ACP) reductase;
            beta-ketoacyl acyl carrier protein (ACP) reductase;
            beta-ketoacyl reductase;
            beta-ketoacyl thioester reductase;
            beta-ketoacyl-ACP reductase;
            beta-ketoacyl-acyl carrier protein reductase;
            3-ketoacyl acyl carrier protein reductase;
            NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase;
            3-oxoacyl-[ACP]reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase
REACTION    (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ =
            3-oxoacyl-[acyl-carrier-protein] + NADPH + H+ [RN:R02767]
ALL_REAC    R02767 > R04533 R04534 R04536 R04543 R04566 R04953 R04964 R07763
SUBSTRATE   (3R)-3-hydroxyacyl-[acyl-carrier-protein];
            NADP+ [CPD:C00006]
PRODUCT     3-oxoacyl-[acyl-carrier-protein];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Exhibits a marked preference for acyl-carrier-protein derivatives
            over CoA derivatives as substrates.
REFERENCE   1  [PMID:4561013]
  AUTHORS   Prescott DJ, Vagelos PR.
  TITLE     Acyl carrier protein.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 36 (1972) 269-311.
REFERENCE   2  [PMID:6756317]
  AUTHORS   Shimakata T, Stumpf PK.
  TITLE     Purification and characterizations of
            beta-Ketoacyl-[acyl-carrier-protein] reductase,
            beta-hydroxyacyl-[acylcarrier-protein] dehydrase, and
            enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea
            leaves.
  JOURNAL   Arch. Biochem. Biophys. 218 (1982) 77-91.
  ORGANISM  spinach
REFERENCE   3  [PMID:4381013]
  AUTHORS   Toomey RE, Wakil SJ.
  TITLE     Studies on the mechanism of fatty acid synthesis. XV. Preparation
            and general properties of beta-ketoacyl acyl carrier protein
            reductase from Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 116 (1966) 189-97.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00061  Fatty acid biosynthesis
            PATH: map01040  Polyunsaturated fatty acid biosynthesis
ORTHOLOGY   KO: K00059  3-oxoacyl-[acyl-carrier protein] reductase
GENES       HSA: 2194(FASN)
            MMU: 14104(Fasn)
            RNO: 50671(Fasn)
            BTA: 281152(FASN)
            GGA: 396061(FASN)
            XLA: 414681(MGC80021)
            XTR: 493259(MGC89688)
            CEL: F09E10.3(dhs-25) F32H2.5(fasn-1)
            ATH: AT1G24360 AT1G63380 AT3G03980 AT3G04000 AT4G13180
            OSA: 4329424 4335609 4340334 4342507 4343598
            CME: CMS393C
            SCE: YPL231W(FAS2)
            AGO: AGOS_AFL138W
            PIC: PICST_32277(FAB7) PICST_49034(OAR1) PICST_58869(SPS21)
                 PICST_61314(SPS24)
            CGR: CAGL0E06138g
            SPO: SPAC4A8.11c(lsd1)
            ANI: AN4934.2 AN5548.2 AN6450.2 AN7806.2
            AFM: AFUA_1G10100 AFUA_1G14380 AFUA_1G17700 AFUA_2G17560
                 AFUA_3G09510 AFUA_3G10540 AFUA_3G13450 AFUA_4G14010
                 AFUA_5G01580 AFUA_5G07470 AFUA_5G09150 AFUA_5G12480
                 AFUA_6G09140 AFUA_6G10520 AFUA_6G11210 AFUA_7G04980
                 AFUA_8G01550
            AOR: AO090003000520 AO090005000145 AO090010000429 AO090011000370
            CNE: CNE04360
            UMA: UM00092.1
            PFA: PFI1125c
            TAN: TA02925
            TET: TTHERM_00094240 TTHERM_01015920 TTHERM_01054150
            TBR: Tb927.2.5210
            TCR: 511627.150
            LMA: LmjF27.2440
            EHI: 12.t00050
            ECO: b1093(fabG)
            ECJ: JW1079(fabG)
            ECE: Z1732(fabG) Z4865
            ECS: ECs1471 ECs4340
            ECC: c1187(fabG) c5303
            ECI: UTI89_C1218(fabG)
            ECP: ECP_1085
            ECV: APECO1_174(fabG) APECO1_2182
            ECW: EcE24377A_1214(fabG)
            ECX: EcHS_A1215(fabG)
            STY: STY1234(fabG)
            STT: t1725(fabG)
            SPT: SPA1656(fabG)
            SEC: SC1143(fabG)
            STM: STM1195(fabG)
            YPE: YPO1456 YPO1599(fabG)
            YPK: y1758(fabG) y2713(fabG)
            YPM: YP_1348(fabG6) YP_2255(fabG10)
            YPA: YPA_0749 YPA_1926
            YPN: YPN_2030 YPN_2522
            YPP: YPDSF_1848
            YPS: YPTB1474 YPTB2471(fabG)
            YPI: YpsIP31758_1578(fabG)
            YEN: YE0910(fabG) YE1635(fabG)
            SFL: SF1097(fabG)
            SFX: S1177(fabG)
            SFV: SFV_1113(fabG)
            SSN: SSON_1113(fabG)
            SBO: SBO_1970(fabG)
            SDY: SDY_2057(fabG)
            ECA: ECA1797(fabG) ECA4492(fabG)
            PLU: plu1541 plu2833(fabG) plu4678
            BUC: BU351(fabG)
            BAS: BUsg339(fabG)
            BAB: bbp321(fabG)
            BCC: BCc_217(fabG)
            WBR: WGLp091(fabG)
            SGL: SG1060
            KPN: KPN_01091(fabG)
            BFL: Bfl404(fabG)
            BPN: BPEN_416(fabG)
            HIN: HI0155(fabG)
            HIT: NTHI0244(fabG)
            HIP: CGSHiEE_02510(fabG)
            HDU: HD0708(fabG)
            HSO: HS_0107(fabG) HS_0167(fabG)
            PMU: PM1916(fabG)
            MSU: MS1874(fabG)
            APL: APL_1992(fabG)
            XFA: XF0173 XF0671
            XFT: PD0141(fabG) PD1503(fabG)
            XCC: XCC0384 XCC0416 XCC1018(fabG) XCC4003(fabG)
            XCB: XC_0396 XC_0429 XC_3227 XC_4092
            XCV: XCV0060 XCV0399 XCV0459 XCV1146(fabG) XCV4178(fabG)
            XAC: XAC0083 XAC0384 XAC0433 XAC1127(fabG) XAC4090(fabG)
            XOO: XOO0234 XOO0459(fabG) XOO0881(fabG)
            XOM: XOO_0214(XOO0214) XOO_0422(XOO0422) XOO_0806(XOO0806)
            VCH: VC2021
            VCO: VC0395_A1607(fabG)
            VVU: VV1_0060 VV1_3009 VV2_0488
            VVY: VV1067 VV1275 VVA1037
            VPA: VP0882 VP2054 VPA0626 VPA1117 VPA1304
            VFI: VF0859(fabG) VF1740(fabG)
            PPR: PBPRA1195(fabG) PBPRB0105(fabG-2) PBPRB1106(fabG2)
                 PBPRB1562(fabG) PBPRB1667
            PAE: PA1470 PA2967(fabG) PA3387(rhlG) PA4389 PA4786 PA5524
            PAU: PA14_25660(fabG) PA14_57050 PA14_63270
            PAP: PSPA7_0908 PSPA7_2194(fabG)
            PPU: PP_0581 PP_1914(fabG) PP_2540 PP_2783
            PST: PSPTO_0743 PSPTO_3832(fabG) PSPTO_4380 PSPTO_5109
            PSB: Psyr_0423 Psyr_0644 Psyr_1647 Psyr_3542 Psyr_4075
            PSP: PSPPH_0413 PSPPH_1641(fabG) PSPPH_4080 PSPPH_4651
            PFL: PFL_0252(fabG) PFL_0462(fabG) PFL_0705(fabG) PFL_1796(fabG)
                 PFL_2864(fabG) PFL_2940(fabG) PFL_4338(fabG) PFL_4842(fabG)
            PFO: Pfl_0423 Pfl_0655 Pfl_2721 Pfl_4157 Pfl_4505
            PEN: PSEEN0346 PSEEN0663 PSEEN1512 PSEEN1618(fabG) PSEEN2587
                 PSEEN3288
            PAR: Psyc_0521(fabG) Psyc_1309 Psyc_1871
            PCR: Pcryo_0516 Pcryo_1069
            ACI: ACIAD0042 ACIAD0582(fabG) ACIAD0871(fabG) ACIAD1976
            SON: SO_1683 SO_2776(fabG-1) SO_4382(fabG-2)
            SDN: Sden_1937 Sden_2293 Sden_3106
            SFR: Sfri_0338 Sfri_1344 Sfri_1499
            SAZ: Sama_1980
            SBL: Sbal_1719
            SLO: Shew_1603
            SHE: Shewmr4_0336 Shewmr4_2396
            SHM: Shewmr7_2466 Shewmr7_3690
            SHN: Shewana3_0327 Shewana3_2558 Shewana3_2765
            SHW: Sputw3181_2440
            ILO: IL0142 IL0866 IL1340(fabG)
            CPS: CPS_0665 CPS_1608 CPS_2297(fabG)
            PHA: PSHAa0879 PSHAa0883(fabG) PSHAa0894 PSHAa0909 PSHAa1264
                 PSHAa1460 PSHAa1808(fabG) PSHAa1885 PSHAa2151 PSHAb0409
            PAT: Patl_0769 Patl_2122
            SDE: Sde_1629
            PIN: Ping_1089
            MAQ: Maqu_1867
            CBU: CBU_0495(fabG) CBU_0702 CBU_1514
            CBD: COXBU7E912_1581(fabG)
            LPN: lpg1395(fabG) lpg2231(fabG)
            LPF: lpl1346(fabG) lpl2157
            LPP: lpp1350(fabG) lpp2184
            MCA: MCA0927 MCA2001(fabG)
            FTU: FTT1375(fabG)
            FTF: FTF1375(fabG)
            FTW: FTW_0516(fabG)
            FTL: FTL_1139
            FTH: FTH_1114(fabG)
            FTA: FTA_1202(fabG)
            FTN: FTN_1339(fabG)
            TCX: Tcr_0712
            NOC: Noc_0460 Noc_0472 Noc_1665 Noc_1950
            AEH: Mlg_1421
            HHA: Hhal_1233
            HCH: HCH_00126 HCH_02144(fabG) HCH_04617 HCH_05141
            CSA: Csal_1601 Csal_2760
            ABO: ABO_0632 ABO_1069(fabG) ABO_1713(fabG)
            AHA: AHA_0770 AHA_2084 AHA_2251(fabG) AHA_3383
            DNO: DNO_1209(fabG)
            BCI: BCI_0434(fabG)
            RMA: Rmag_0916
            VOK: COSY_0822(fabG)
            NME: NMB1702 NMB1921
            NMA: NMA0533(fabG)
            NMC: NMC0302(fabG)
            NGO: NGO2163(fabG)
            CVI: CV_1546 CV_2707 CV_3414(fabG) CV_3576(fabG2) CV_3947
            RSO: RS05466(RSp0305) RSc0435(fabG) RSc0536(RS04930) RSc1052(fabG)
                 RSc2186(RS01413) RSp0359(fabG)
            REU: Reut_A1570 Reut_A1622 Reut_A2263 Reut_A2505 Reut_A2858
                 Reut_B3848 Reut_B3871 Reut_B3935 Reut_B4170 Reut_B4557
                 Reut_B4754 Reut_B4775 Reut_B5854 Reut_C6224 Reut_C6276
                 Reut_C6315 Reut_C6404
            REH: H16_A1287 H16_A2567(fabG) H16_B0361 H16_B0385 H16_B1075
                 H16_B1669 H16_B1904 H16_B2496 H16_B2510
            RME: Rmet_0791 Rmet_1911 Rmet_2428 Rmet_2533 Rmet_3057 Rmet_4391
                 Rmet_4544 Rmet_5028 Rmet_5524 Rmet_5825
            BMA: BMA0532(fabG) BMA1882 BMAA1104
            BMV: BMASAVP1_A2477(fabG)
            BML: BMA10299_A2804(fabG)
            BMN: BMA10247_1800(fabG)
            BXE: Bxe_A0939 Bxe_A1074 Bxe_A2099 Bxe_A2114 Bxe_A2692 Bxe_A2719
                 Bxe_A2775 Bxe_A3012 Bxe_A3257 Bxe_A3553 Bxe_A4299 Bxe_B0266
                 Bxe_B1028 Bxe_B1525 Bxe_B2157 Bxe_B2319 Bxe_B2694 Bxe_B2728
                 Bxe_C0296 Bxe_C0357 Bxe_C0589 Bxe_C0591 Bxe_C0616 Bxe_C0639
                 Bxe_C0705 Bxe_C0900
            BUR: Bcep18194_A3506 Bcep18194_A3702 Bcep18194_A4032
                 Bcep18194_A4235(fabG) Bcep18194_A4562 Bcep18194_A4607
                 Bcep18194_A4885 Bcep18194_A4896 Bcep18194_A4911
                 Bcep18194_A5141 Bcep18194_A5492 Bcep18194_A5540
                 Bcep18194_A5602 Bcep18194_A5619 Bcep18194_A5711
                 Bcep18194_A5746 Bcep18194_A5811 Bcep18194_A6088(fabG)
                 Bcep18194_A6265 Bcep18194_B0196 Bcep18194_B0244
                 Bcep18194_B0533 Bcep18194_B0563 Bcep18194_B0620
                 Bcep18194_B0623 Bcep18194_B0903 Bcep18194_B0911
                 Bcep18194_B0928 Bcep18194_B0958 Bcep18194_B1002
                 Bcep18194_B1106 Bcep18194_B1110 Bcep18194_B1174
                 Bcep18194_B1178 Bcep18194_B1189 Bcep18194_B1203
                 Bcep18194_B1218 Bcep18194_B1221 Bcep18194_B1229
                 Bcep18194_B1347 Bcep18194_B1406 Bcep18194_B1418
                 Bcep18194_B1440 Bcep18194_B1443 Bcep18194_B1452
                 Bcep18194_B1462 Bcep18194_B1464 Bcep18194_B1490
                 Bcep18194_B1508 Bcep18194_B1509 Bcep18194_B1513
                 Bcep18194_B1515 Bcep18194_B1733 Bcep18194_B1738
                 Bcep18194_B1790 Bcep18194_B2086 Bcep18194_B2225
                 Bcep18194_B2292 Bcep18194_B2504 Bcep18194_B2585
                 Bcep18194_B2649 Bcep18194_B2755 Bcep18194_B2903
                 Bcep18194_B3036 Bcep18194_B3095 Bcep18194_B3133
                 Bcep18194_B3149 Bcep18194_B3167 Bcep18194_C6694
                 Bcep18194_C6740 Bcep18194_C6757 Bcep18194_C6919
                 Bcep18194_C6936 Bcep18194_C7039 Bcep18194_C7070
                 Bcep18194_C7112 Bcep18194_C7115 Bcep18194_C7123
                 Bcep18194_C7132 Bcep18194_C7138 Bcep18194_C7160
                 Bcep18194_C7167 Bcep18194_C7178 Bcep18194_C7235
                 Bcep18194_C7276 Bcep18194_C7331 Bcep18194_C7556
                 Bcep18194_C7587 Bcep18194_C7589
            BCN: Bcen_0643 Bcen_2144
            BCH: Bcen2424_1123
            BAM: Bamb_0999 Bamb_1298 Bamb_2330 Bamb_2528 Bamb_2810 Bamb_3610
            BPS: BPSL1167 BPSL2440(fabG) BPSS1256
            BPM: BURPS1710b_1388 BURPS1710b_2905(fabG) BURPS1710b_A0256
                 BURPS1710b_A2301 BURPS1710b_A2378
            BPL: BURPS1106A_2851(fabG)
            BPD: BURPS668_2790(fabG)
            BTE: BTH_I1017 BTH_I1719(fabG) BTH_I2387 BTH_II1155
            BPE: BP0813 BP1128(fabG) BP1668 BP1672(fabG) BP1785(fabG)
                 BP2441(fabG) BP2554(fabG) BP3010
            BPA: BPP0607 BPP1392 BPP2016(fabG) BPP2100 BPP2625(fabG)
                 BPP3213(fabG) BPP3305(fabG) BPP3417 BPP3739
            BBR: BB0613 BB1496 BB2068(fabG) BB2264(fabG) BB2461 BB3665(fabG)
                 BB3756(fabG) BB3867 BB4185 BB4764(fabG) BB4780
            RFR: Rfer_1638 Rfer_1732 Rfer_3195 Rfer_3994 Rfer_4047
            POL: Bpro_1491 Bpro_3307 Bpro_3647 Bpro_3876 Bpro_3960 Bpro_4767
            MPT: Mpe_A0638 Mpe_A1327 Mpe_A3053
            HAR: HEAR0567 HEAR1809 HEAR2075(fabG) HEAR2427 HEAR2870 HEAR3191
            MMS: mma_0550 mma_1358(fabG) mma_2018 mma_2323 mma_2505
            NEU: NE1648(fabG1)
            NET: Neut_0468
            NMU: Nmul_A1074 Nmul_A1378
            EBA: ebA5300(bzdZ) ebA5457(fabG) ebA5789(ped2) ebA7075(fabG1)
            AZO: azo1625(fabG1) azo3914(fabG2)
            DAR: Daro_2017 Daro_4188
            TBD: Tbd_1549 Tbd_2756
            MFA: Mfla_1505 Mfla_2669
            HPY: HP0561(fabG)
            HPA: HPAG1_0540
            HHE: HH0732(fabG)
            HAC: Hac_0781(fabG)
            WSU: WS0631(fabG)
            TDN: Tmden_1613
            CJE: Cj0435(fabG)
            CJR: CJE0485(fabG)
            CJJ: CJJ81176_0461(fabG)
            CJU: C8J_0410(fabG)
            CJD: JJD26997_1509(fabG)
            CFF: CFF8240_1361(fabG)
            CCV: CCV52592_1043(fabG) CCV52592_1164
            CHA: CHAB381_0231(fabG)
            CCO: CCC13826_0562(fabG)
            ABU: Abu_2058(fabG)
            NIS: NIS_0313(fabG)
            SUN: SUN_2189(fabG)
            GSU: GSU0461(fabG-1) GSU1603(fabG-2)
            GME: Gmet_1601 Gmet_1694
            PCA: Pcar_1438 Pcar_2667
            DVU: DVU1206(fabG) DVU2561
            DDE: Dde_2429 Dde_2658
            LIP: LI0161(fabG) LI0419
            BBA: Bd0281(fabG) Bd0405(fabG) Bd0506 Bd1969(fabG) Bd2012(fabG)
                 Bd3814(linC)
            DPS: DP1847 DP2407 DP2790
            ADE: Adeh_2748 Adeh_2760 Adeh_3849
            MXA: MXAN_4770(fabG)
            SAT: SYN_01680 SYN_01696 SYN_02127
            SFU: Sfum_1374
            RPR: RP762(fabG)
            RTY: RT0748(fabG)
            RCO: RC1183(fabG)
            RFE: RF_0153(phbB) RF_1222(fabG)
            RBE: RBE_0116(fabG) RBE_1370(phbB)
            RAK: A1C_05935(fabG)
            RBO: A1I_07350(fabG)
            RCM: A1E_04870(fabG)
            RRI: A1G_06495(fabG)
            OTS: OTBS_0381(fabG)
            WOL: WD0650(fabG)
            WBM: Wbm0310
            AMA: AM584(fabG)
            APH: APH_0668(fabG)
            ERU: Erum3840(fabG)
            ERW: ERWE_CDS_03960(fabG)
            ERG: ERGA_CDS_03920(fabG)
            ECN: Ecaj_0374
            ECH: ECH_0669(fabG)
            NSE: NSE_0665(fabG)
            PUB: SAR11_0707(fabG)
            MLO: mll1017 mll1981 mll5243 mlr0808 mlr6807 mlr7850
            MES: Meso_1537 Meso_1768
            SME: SMa0854(nodG) SMa0959 SMb20493 SMb21474 SMc00572(fabG)
                 SMc01157
            ATU: Atu0990 Atu1095(fabG) Atu3333 Atu3531(fabG) Atu3813(fabG)
                 Atu4595 Atu4877 Atu5122(fabG)
            ATC: AGR_C_1817 AGR_C_2026 AGR_L_2039 AGR_L_2601 AGR_L_28
                 AGR_L_2975 AGR_L_561 AGR_pAT_178
            RET: RHE_CH00288 RHE_CH00343 RHE_CH01047(ypch00346)
                 RHE_CH01048(ypch00347) RHE_CH01307(ypch00443)
                 RHE_CH01443(fabG2) RHE_CH01762 RHE_CH02692 RHE_CH03007
                 RHE_CH03352(ypch01170) RHE_CH03691 RHE_CH03699 RHE_PE00207
                 RHE_PE00386 RHE_PF00008 RHE_PF00089 RHE_PF00142
                 RHE_PF00144(ypf00064)
            RLE: RL0294 RL0358(fabG) RL0359 RL0478(nodG) RL0481 RL0590 RL0975
                 RL1185 RL1193 RL1231 RL1264 RL1343 RL1399 RL1456 RL1558(fabG)
                 RL1588(fabG) RL1814 RL1854 RL1957 RL2295 RL2302 RL2358
                 RL2674(fabG) RL2785 RL3451 RL3779 RL3791 RL3833 RL3854 RL4048
                 RL4227 RL4235 RL4271 RL4430 pRL110155 pRL110166 pRL110303
                 pRL110503 pRL120119 pRL120143 pRL120144 pRL120292 pRL120549
                 pRL80048 pRL90210
            BME: BMEI0026(fabG) BMEI0032 BMEI1250 BMEI1477 BMEII0063 BMEII0514
            BMF: BAB1_0483(fabG) BAB1_0721 BAB1_2039 BAB1_2043 BAB2_0029
            BMS: BR0458(fabG) BR2039 BRA0030
            BMB: BruAb1_0480(fabG) BruAb1_2014 BruAb1_2018(fabG) BruAb2_0030
            BOV: BOV_0463(fabG)
            BJA: bll1230 bll2747(fabG) bll3028 bll3913(fabG) bll4020 bll6359
                 bll7782 bll7880 bll7886 blr1495 blr1893(fabG) blr3403
                 blr4083(fabG) blr5634 blr6288 blr7888
            BRA: BRADO0228 BRADO0281 BRADO0918 BRADO1083 BRADO1085 BRADO1160
                 BRADO1435 BRADO1794 BRADO2099 BRADO3093 BRADO3101 BRADO3102
                 BRADO3143 BRADO3311(fabG) BRADO3485 BRADO3494 BRADO3705
                 BRADO4311 BRADO4807 BRADO6290 BRADO6422 BRADO6424 BRADO6595
                 BRADO6654
            BBT: BBta_0225 BBta_0274 BBta_0879 BBta_0940 BBta_1152 BBta_1171
                 BBta_1210 BBta_1212 BBta_1600 BBta_2110 BBta_3238 BBta_3549
                 BBta_3550 BBta_3584 BBta_3818(fabG) BBta_4672 BBta_5003
                 BBta_5043 BBta_6672 BBta_6893 BBta_6963 BBta_6964 BBta_7134
                 BBta_7764
            RPA: RPA0109 RPA0479(fabG1) RPA0895 RPA0896 RPA1110 RPA1683
                 RPA1684 RPA1757 RPA2072 RPA2160 RPA2417 RPA3074(fabG2)
                 RPA3304(fabG3) RPA3474(fabG4) RPA3631 RPA4596(fabG5)
                 RPA4633(fixR2) RPA4657(kduD)
            RPB: RPB_0994 RPB_2093 RPB_2467 RPB_3242 RPB_3606 RPB_3848
                 RPB_3849 RPB_4075 RPB_4527 RPB_4528
            RPC: RPC_1926 RPC_2300 RPC_3013 RPC_3184 RPC_3793 RPC_3795
            RPD: RPD_1097 RPD_2979 RPD_3326 RPD_3811 RPD_4287 RPD_4365
            RPE: RPE_0118 RPE_1702 RPE_2271 RPE_3306 RPE_3560 RPE_3616
                 RPE_3689 RPE_3690 RPE_3916 RPE_3918 RPE_4716
            NWI: Nwi_0477 Nwi_0487 Nwi_1688 Nwi_2019 Nwi_2310 Nwi_2393
            BHE: BH05350(fabG)
            BQU: BQ04530(fabG)
            BBK: BARBAKC583_0497(fabG)
            CCR: CC_1675 CC_2836
            SIL: SPO2275(fabG) SPO2413 SPO2692
            SIT: TM1040_1051 TM1040_1803
            RSP: RSP_0610 RSP_2371 RSP_2461(fabG) RSP_2538(fabG)
                 RSP_3062(fabG) RSP_3440 RSP_3888(fabG) RSP_4004
            JAN: Jann_1626
            RDE: RD1_0288 RD1_0504 RD1_3039 RD1_3261 RD1_3756 RD1_3872
                 RD1_3996 RD1_4089
            MMR: Mmar10_1215
            HNE: HNE_0974 HNE_2158(fabG)
            ZMO: ZMO1222 ZMO1946
            GOX: GOX1399(fabG) GOX2040
            GBE: GbCGDNIH1_0029 GbCGDNIH1_0057 GbCGDNIH1_0927 GbCGDNIH1_1049
                 GbCGDNIH1_2211 GbCGDNIH1_2226
            RRU: Rru_A0403 Rru_A0416 Rru_A1264 Rru_A1306 Rru_A2218 Rru_A2512
                 Rru_A2747 Rru_A3017 Rru_A3667
            MAG: amb2106 amb2842
            MGM: Mmc1_1874
            ABA: Acid345_0026 Acid345_0265 Acid345_1374 Acid345_1606
                 Acid345_2262
            BSU: BG11535(fabG) BG13173(yjdA) BG13429(ymfI) BG13870(ytkK)
                 BG14030(yusR) BG14031(yusS) BG14063(yvaG) BG14144(yvrD)
            BHA: BH0506 BH0932 BH1842 BH2391 BH2491(fabG) BH3182 BH3896
            BAN: BA1958 BA3385 BA3440 BA3610 BA3921 BA3989(fabG) BA4874
            BAR: GBAA1958 GBAA3385 GBAA3440 GBAA3610 GBAA3921 GBAA3989(fabG)
                 GBAA4874
            BAA: BA_0755 BA_2462 BA_3884 BA_3937 BA_4102 BA_4392 BA_4460
                 BA_5295
            BAT: BAS0174 BAS1819 BAS3138 BAS3188 BAS3349 BAS3635 BAS3702
                 BAS4522
            BCE: BC0195(fabG) BC1062 BC1958(fabG) BC3327(fabG) BC3382
                 BC3556(fabG) BC3785(fabG) BC3849(fabG) BC4624(fabG)
            BCA: BCE_0194 BCE_2044 BCE_3355 BCE_3570 BCE_3820 BCE_3893(fabG)
                 BCE_4759
            BCZ: BCZK0164(fabG) BCZK1209(fabG) BCZK1775(fabG) BCZK3032
                 BCZK3090 BCZK3264 BCZK3545(fabG) BCZK3610(fabG) BCZK4369(fabG)
            BTK: BT9727_0164 BT9727_1793(fabG) BT9727_3125 BT9727_3169
                 BT9727_3314 BT9727_3527(fabG) BT9727_3592(fabG)
                 BT9727_4358(fabG)
            BTL: BALH_3007 BALH_4205(fabG)
            BLI: BL00414(ytkK) BL00741(yvrD) BL01678(yusR) BL02315(fabG)
                 BL02426 BL03119(yvaG) BL03573
            BLD: BLi00319 BLi01605 BLi01812(fabG) BLi01911(ymfI) BLi02819
                 BLi02826(yvaG) BLi03081(ytkK) BLi03500
            BCL: ABC0346 ABC0368 ABC1310 ABC2206 ABC2301(fabG) ABC2734(fabG)
                 ABC3114 ABC3532 ABC3620
            BAY: RBAM_015740(fabG) RBAM_018690 RBAM_022040
            BPU: BPUM_1490(fabG1) BPUM_2574(fabG2) BPUM_2971
            OIH: OB0671 OB1524(fabG) OB1618 OB1843(fabG) OB2792 OB3475(fabG)
            GKA: GK1026 GK1190(fabG) GK1289 GK1471 GK1655 GK2753 GK2778
            SAU: SA1074(fabG) SA1123
            SAV: SAV1231(fabG) SAV1280
            SAM: MW1114(fabG) MW1163
            SAR: SAR1207(fabG) SAR1256
            SAS: SAS1165 SAS1214
            SAC: SACOL1245(fabG1) SACOL1299
            SAB: SAB1095(fabG)
            SAA: SAUSA300_1124(fabG) SAUSA300_1173
            SAO: SAOUHSC_01199 SAOUHSC_01257
            SEP: SE0324 SE0906 SE0957
            SER: SERP0201 SERP0797(fabG) SERP0847
            SHA: SH0230 SH1633(ymfI) SH1683(fabG)
            SSP: SSP1485 SSP1530 SSP1538
            LMO: lmo1394 lmo1807(fabG) lmo2815
            LMF: LMOf2365_1413 LMOf2365_1835(fabG) LMOf2365_2806
            LIN: lin1431 lin1921(fabG) lin2948
            LWE: lwe1410 lwe1826(fabG) lwe2751
            LLA: L0185(fabG1) L1530(yiaB) L27694(fabG2)
            LLC: LACR_0824 LACR_0845 LACR_1474 LACR_1960
            LLM: llmg_0156(dltE) llmg_1784(fabG1)
            SPY: SPy_0440 SPy_1749(fabG)
            SPZ: M5005_Spy_0359(fabG) M5005_Spy_1490(fabG)
            SPM: spyM18_0483 spyM18_1821
            SPG: SpyM3_0309 SpyM3_1523(fabG)
            SPS: SPs0343 SPs1548
            SPH: MGAS10270_Spy0362 MGAS10270_Spy1558
            SPI: MGAS10750_Spy1549
            SPJ: MGAS2096_Spy0378 MGAS2096_Spy1518
            SPK: MGAS9429_Spy1492
            SPF: SpyM50355(fabG)
            SPA: M6_Spy0383 M6_Spy1484(fabG)
            SPB: M28_Spy0348(fabG) M28_Spy1479(fabG)
            SPN: SP_0421 SP_0793
            SPR: spr0381(fabG) spr0701(fabG)
            SPD: SPD_0384(fabG)
            SAG: SAG0348(fabG) SAG0664(cylG) SAG1544
            SAN: gbs0335 gbs0646(cylG) gbs1600
            SAK: SAK_0422(fabG) SAK_0792(cylG) SAK_1566
            SMU: SMU.1740(fabG)
            STC: str0387(fabG)
            STL: stu0387(fabG)
            SSA: SSA_1650 SSA_1936(fabG)
            SGO: SGO_1473 SGO_1693(fabG)
            LPL: lp_0159 lp_1674(fabG1) lp_2764
            LJO: LJ0836
            LAC: LBA0662(fabG)
            LSA: LSA0454 LSA0484 LSA0816(fabG)
            LSL: LSL_0148 LSL_0454(fabG) LSL_1133(fabG) LSL_1468
            LDB: Ldb0596 Ldb0903(fabG)
            LBU: LBUL_0532 LBUL_0821
            LBR: LVIS_0932 LVIS_1178
            LCA: LSEI_0919 LSEI_2057 LSEI_2115
            EFA: EF1667 EF1773 EF2881(fabG)
            OOE: OEOE_1589
            STH: STH1451 STH1990 STH577 STH805 STH968
            CAC: CAC2626(fabG) CAC3462(fabG) CAC3574(fabG)
            CPE: CPE1070(fabG) CPE1927
            CPF: CPF_1326(fabG) CPF_2182(fabG)
            CPR: CPR_1138(fabG) CPR_1893(fabG)
            CTC: CTC00130(fabG) CTC00798
            CNO: NT01CX_0355 NT01CX_0925(fabG)
            CDF: CD1182(fabG)
            CBO: CBO0502 CBO3600(fabG)
            CBA: CLB_0543(fabG-1) CLB_3680(fabG-2)
            CBH: CLC_0576(fabG-1) CLC_3578(fabG-2)
            CBF: CLI_0582(fabG-1) CLI_3825(fabG-2)
            CKL: CKL_0106(fabG1) CKL_2102(fabG2)
            CHY: CHY_1447(fabG)
            DSY: DSY1515 DSY2211 DSY2660
            SWO: Swol_1850
            TTE: TTE0051(fabG) TTE1472(fabG3) TTE2234(fabG5) TTE2709(fabG6)
            MTA: Moth_0426 Moth_0948 Moth_1258
            MTU: Rv0242c(fabG4) Rv1350(fabG2) Rv1483(fabG1)
            MTC: MT0256(fabG-1) MT0793 MT1393 MT1530(fabG-2) MT3606(fabG-3)
                 MT3664
            MBO: Mb0248c(fabG) Mb1385(fabG) Mb1519(fabG1) Mb3532c Mb3589c
            MBB: BCG_0280c(fabG4) BCG_1412(fabG2) BCG_1545(fabG1)
            MLE: ML1807(fabG1) ML2565(fabG4)
            MPA: MAP0508 MAP0561 MAP0603 MAP1209(fabG1) MAP2408c(fabG2_2)
                 MAP3328c MAP3692c(fabG4)
            MAV: MAV_1572 MAV_2665 MAV_3295(fabG) MAV_5088
            MSM: MSMEG_0121 MSMEG_0269 MSMEG_0283 MSMEG_0294(fabG) MSMEG_0715
                 MSMEG_1071 MSMEG_1689 MSMEG_2206(fabG) MSMEG_2536 MSMEG_2548
                 MSMEG_2852 MSMEG_3150(fabG) MSMEG_3823 MSMEG_3825 MSMEG_3830
                 MSMEG_4004 MSMEG_4163 MSMEG_4169 MSMEG_4835 MSMEG_5858
            MMC: Mmcs_2456
            CGL: NCgl0281(cgl0286) NCgl0315(cgl0321)
            CGB: cg0344(fabG1) cg0957(fas-IB) cg2743(fas-IA)
            CEF: CE2778
            CJK: jk0822(fabG2)
            NFA: nfa23600 nfa33940 nfa34110 nfa34770(fabG) nfa46620 nfa4850
                 nfa5340 nfa54610
            RHA: RHA1_ro00294 RHA1_ro00370 RHA1_ro00404 RHA1_ro01403
                 RHA1_ro01497 RHA1_ro01501 RHA1_ro01503 RHA1_ro01621
                 RHA1_ro02340 RHA1_ro02344 RHA1_ro02478 RHA1_ro02724
                 RHA1_ro02735 RHA1_ro02737 RHA1_ro02844 RHA1_ro03008
                 RHA1_ro03028 RHA1_ro03213 RHA1_ro03214 RHA1_ro04587
                 RHA1_ro04654 RHA1_ro04755 RHA1_ro05199 RHA1_ro05294
                 RHA1_ro05394 RHA1_ro05413 RHA1_ro05790 RHA1_ro05809
                 RHA1_ro06637 RHA1_ro06991 RHA1_ro07213(fabG1) RHA1_ro08448
                 RHA1_ro08469 RHA1_ro08503 RHA1_ro08508 RHA1_ro08631
                 RHA1_ro11023(fabG2) RHA1_ro11162(fabG3) RHA1_ro11180
            SCO: SCO0330(SCF12.09) SCO1346(2SCG61.28c) SCO1815(fabG)
                 SCO1831(SCI8.16) SCO4501(SCD35.08c) SCO4681(SCD31.06)
            SMA: SAV2387 SAV3653(fabG4) SAV5872(fabG5) SAV6197 SAV6435
                 SAV6462(fabG7) SAV7008(fabG8)
            TWH: TWT313(fabG)
            TWS: TW459(fabG)
            LXX: Lxx11740(fabG)
            AAU: AAur_2120(fabG)
            PAC: PPA1533 PPA1815(fabG)
            TFU: Tfu_1841 Tfu_1843 Tfu_2308
            FRA: Francci3_1897 Francci3_2119
            FAL: FRAAL0883 FRAAL1000(fabG) FRAAL2413 FRAAL2633 FRAAL2642(fabG)
                 FRAAL3113 FRAAL3322 FRAAL3362 FRAAL3528 FRAAL3539 FRAAL3540
                 FRAAL3542 FRAAL3618 FRAAL4385(fabG) FRAAL4518(fabG)
                 FRAAL4739(cad) FRAAL5306 FRAAL5558(fabG)
            SEN: SACE_0225 SACE_1913(fabG3) SACE_2515 SACE_2735(fabG)
                 SACE_2756 SACE_3371(fabG) SACE_3426 SACE_3681(fabG)
                 SACE_3687(fabG) SACE_3787(fabG1) SACE_4151 SACE_4767 SACE_4805
                 SACE_5381(fabG3) SACE_6255(fabG) SACE_7303(fabG)
            BLO: BL0512
            RXY: Rxyl_1381
            FNU: FN0216 FN0494 FN0899
            RBA: RB11488 RB316(fabG) RB3657 RB4981 RB6240(fabG) RB8029
                 RB8871(fabG) RB9574(fabG)
            CTR: CT237(fabG)
            CTA: CTA_0259(fabG)
            CMU: TC0508
            CPN: CPn0296(fabG)
            CPA: CP0462
            CPJ: CPj0296(fabG)
            CPT: CpB0305
            CCA: CCA00486(fabG)
            CAB: CAB472(fabG)
            CFE: CF0521(fabG1)
            PCU: pc1718(fabG)
            TDE: TDE0598(fabG)
            LIL: LA0020 LA0225 LA0971 LA1427 LA1975 LA2303 LA2324(fabG) LA2621
                 LA3484 LA4052 LB034 LB041 LB082 LB113 LB121 LB291
            LIC: LIC10194 LIC10700 LIC11364(dltE) LIC11618 LIC11634(csgA)
                 LIC12320 LIC13232 LIC20064(fabG) LIC20097
            LBJ: LBJ_0451 LBJ_1300 LBJ_2113
            LBL: LBL_0938 LBL_1525 LBL_2627
            SYN: slr0886(fabG1) slr1994(phaB)
            SYW: SYNW1852(fabG)
            SYC: syc0845_c(fabG)
            SYF: Synpcc7942_0684
            SYD: Syncc9605_0617
            SYE: Syncc9902_1745
            SYG: sync_0860 sync_2137(fabG-1)
            SYR: SynRCC307_0681(fabG)
            SYX: SynWH7803_1861(fabG)
            CYA: CYA_2483(fabG)
            CYB: CYB_2090(fabG)
            TEL: tlr1502
            GVI: glr3506
            ANA: alr1894(fabG)
            AVA: Ava_0311 Ava_0943 Ava_1572 Ava_1691 Ava_1800 Ava_1895
                 Ava_2428 Ava_2536 Ava_2596 Ava_2965 Ava_3459 Ava_3764(fabG)
                 Ava_3968 Ava_4328 Ava_4667 Ava_4758 Ava_4780 Ava_4906
                 Ava_C0109 Ava_C0112
            PMA: Pro0452(fabG)
            PMM: PMM0453(fabG)
            PMT: PMT1333(fabG)
            PMN: PMN2A_1785
            PMI: PMT9312_0453
            PMB: A9601_04161 A9601_05091 A9601_07571
            PMC: P9515_04211 P9515_05161 P9515_08791
            PMF: P9303_06521 P9303_07591
            PMG: P9301_04781 P9301_07551
            PMH: P9215_05331(fabG)
            PME: NATL1_01071 NATL1_05081 NATL1_05911
            TER: Tery_3438
            BTH: BT_3771
            BFR: BF4118
            BFS: BF3932(fabG)
            PGI: PG1239(fabG)
            SRU: SRU_0045(fabG) SRU_0736
            CHU: CHU_0327(fabG) CHU_1057(fabG) CHU_1085(fabG) CHU_1425(fabG)
                 CHU_2123
            GFO: GFO_1667(fabG) GFO_1767(fabG)
            FPS: FP0964 FP2285
            CTE: CT2116(fabG)
            CCH: Cag_0259 Cag_0350 Cag_0693 Cag_1639 Cag_1662
            PLT: Plut_0131
            DET: DET1277(fabG)
            DEH: cbdb_A1205(fabG)
            DRA: DR_0822 DR_1943
            DGE: Dgeo_0435 Dgeo_1963
            TTH: TTC0047 TTC0394 TTC1861
            TTJ: TTHA0415 TTHA0750 TTHB020
            AAE: aq_1716(fabG)
            TMA: TM1169 TM1724
            MAC: MA2686(fabG2) MA2687(fabG1)
            MBA: Mbar_A2512
            MMA: MM_3225
            MHU: Mhun_3155
            HAL: VNG1341G(fabG) VNG2158G(oxrA)
            HMA: pNG7030(fabG3) pNG7072(fabG7) pNG7335(fabG5) rrnAC0904(fabG1)
                 rrnAC1984(fabG4) rrnAC3004(fabG)
            HWA: HQ2309A(phaB) HQ2771A
            NPH: NP0726A NP1900A NP4370A
            TAC: Ta0251 Ta0822
            TVO: TVN0711 TVN1344
            PTO: PTO0990 PTO1324(fabG)
            PHO: PH1901
            PAB: PAB1085(fabG) PAB2177
            PFU: PF0149 PF1899
            TKO: TK0736 TK1677
            APE: APE_0912 APE_2503.1
            SSO: SSO0975(fabG-1) SSO2276(fabG-5) SSO2289(fabG) SSO2500(fabG)
                 SSO3114(fabG-10)
            STO: ST0070 ST1109 ST1299 ST1868 ST2239
            SAI: Saci_0158 Saci_0238 Saci_1104(gdh) Saci_1308 Saci_1965
            PAI: PAE0797 PAE2832
            NEQ: NEQ306
STRUCTURES  PDB: 1I01  1O5I  1Q7B  1Q7C  1ULS  1UZL  1UZM  1UZN  2A4K  2B4Q  
                 2C07  2FR0  2FR1  2NM0  2NTN  2P68  2PFF  2PH3  2PNF  2UVD  
                 2Z5L  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.100
            ExPASy - ENZYME nomenclature database: 1.1.1.100
            ExplorEnz - The Enzyme Database: 1.1.1.100
            ERGO genome analysis and discovery system: 1.1.1.100
            BRENDA, the Enzyme Database: 1.1.1.100
            CAS: 37250-34-3
///
ENTRY       EC 1.1.1.101                Enzyme
NAME        acylglycerone-phosphate reductase;
            palmitoyldihydroxyacetone-phosphate reductase;
            palmitoyl dihydroxyacetone phosphate reductase;
            palmitoyl-dihydroxyacetone-phosphate reductase;
            acyldihydroxyacetone phosphate reductase;
            palmitoyl dihydroxyacetone phosphate reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     1-palmitoylglycerol-3-phosphate:NADP+ oxidoreductase
REACTION    1-palmitoylglycerol 3-phosphate + NADP+ = palmitoylglycerone
            phosphate + NADPH + H+ [RN:R03357]
ALL_REAC    R03357;
            (other) R02756 R04360
SUBSTRATE   1-palmitoylglycerol 3-phosphate [CPD:C04036];
            NADP+ [CPD:C00006]
PRODUCT     palmitoylglycerone phosphate [CPD:C01192];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on alkylglycerone 3-phosphate and alkylglycerol
            3-phosphate.
REFERENCE   1  [PMID:4403490]
  AUTHORS   LaBelle EF Jr, Hajra AK.
  TITLE     Enzymatic reduction of alkyl and acyl derivatives of
            dihydroxyacetone phosphate by reduced pyridine nucleotides.
  JOURNAL   J. Biol. Chem. 247 (1972) 5825-34.
  ORGANISM  rat [GN:rno], guinea pig
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
            PATH: map00565  Ether lipid metabolism
ORTHOLOGY   KO: K06123  1-acylglycerone phosphate reductase
GENES       ATH: AT5G10050
            SCE: YIL124W(AYR1)
            AGO: AGOS_AER373C
            PIC: PICST_85576(AYR2)
            CAL: CaO19.6167(ayr1)
            CGR: CAGL0G08690g
            SPO: SPAC23D3.11
            DDI: DDBDRAFT_0188337
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.101
            ExPASy - ENZYME nomenclature database: 1.1.1.101
            ExplorEnz - The Enzyme Database: 1.1.1.101
            ERGO genome analysis and discovery system: 1.1.1.101
            BRENDA, the Enzyme Database: 1.1.1.101
            CAS: 37250-35-4
///
ENTRY       EC 1.1.1.102                Enzyme
NAME        3-dehydrosphinganine reductase;
            D-3-dehydrosphinganine reductase;
            D-3-oxosphinganine reductase;
            DSR;
            3-oxosphinganine reductase;
            3-oxosphinganine:NADPH oxidoreductase;
            D-3-oxosphinganine:B-NADPH oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-erythro-dihydrosphingosine:NADP+ 3-oxidoreductase
REACTION    sphinganine + NADP+ = 3-dehydrosphinganine + NADPH + H+ [RN:R02978]
ALL_REAC    R02978
SUBSTRATE   sphinganine [CPD:C00836];
            NADP+ [CPD:C00006]
PRODUCT     3-dehydrosphinganine [CPD:C02934];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4386961]
  AUTHORS   Stoffel W, LeKim D, Sticht G.
  TITLE     Biosynthesis of dihydrosphingosine in vitro.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 349 (1968) 664-70.
  ORGANISM  Hansenula ciferrii, rat [GN:rno]
REFERENCE   2  [PMID:4387676]
  AUTHORS   Stoffel W, LeKim D, Sticht G.
  TITLE     Metabolism of sphingosine bases. 8. Distribution, isolation and
            properties of D-3-oxosphinganine reductase. Stereospecificity of the
            NADPH-dependent reaction of 3-oxodihydrospingosine
            (2-amino-1-hydroxyoctadecane-3-one).
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 349 (1968) 1637-44.
PATHWAY     PATH: map00600  Sphingolipid metabolism
ORTHOLOGY   KO: K04708  3-dehydrosphinganine reductase
GENES       HSA: 2531(FVT1)
            MMU: 70750(Fvt1)
            GGA: 420902(RCJMB04_8j12)
            XLA: 414665(MGC81046)
            SCE: YBR265W(TSC10)
            AGO: AGOS_AEL164C
            TBR: Tb10.70.3240
            TAC: Ta0191
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.102
            ExPASy - ENZYME nomenclature database: 1.1.1.102
            ExplorEnz - The Enzyme Database: 1.1.1.102
            ERGO genome analysis and discovery system: 1.1.1.102
            BRENDA, the Enzyme Database: 1.1.1.102
            CAS: 37250-36-5
///
ENTRY       EC 1.1.1.103                Enzyme
NAME        L-threonine 3-dehydrogenase;
            L-threonine dehydrogenase;
            threonine 3-dehydrogenase;
            threonine dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-threonine:NAD+ oxidoreductase
REACTION    L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+
            [RN:R01465]
ALL_REAC    R01465
SUBSTRATE   L-threonine [CPD:C00188];
            NAD+ [CPD:C00003]
PRODUCT     L-2-amino-3-oxobutanoate [CPD:C03508];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The product spontaneously decarboxylates to aminoacetone.
REFERENCE   1  [PMID:4284408]
  AUTHORS   Green ML, Elliott WH.
  TITLE     The enzymic formation of aminoacetone from threonine and its further
            metabolism.
  JOURNAL   Biochem. J. 92 (1964) 537-49.
  ORGANISM  Staphylococcus aureus, rat [GN:rno], rabbit
REFERENCE   2  [PMID:14165492]
  AUTHORS   HARTSHORNE D, GREENBERG DM.
  TITLE     STUDIES ON LIVER THREONINE DEHYDROGENASE.
  JOURNAL   Arch. Biochem. Biophys. 105 (1964) 173-8.
  ORGANISM  frog
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K00060  threonine 3-dehydrogenase
GENES       MMU: 58865(Tdh)
            CME: CMR237C
            ECO: b3616(tdh)
            ECJ: JW3591(tdh)
            ECE: Z5043(tdh)
            ECS: ECs4494
            ECC: c4443(tdh)
            ECI: UTI89_C4162(tdh)
            ECP: ECP_3717
            ECV: APECO1_2839(tdh)
            ECW: EcE24377A_4120(tdh)
            ECX: EcHS_A3828(tdh)
            STY: STY4087(tdh)
            STT: t3811(tdh)
            SPT: SPA3560(tdh)
            SEC: SC3631(tdh)
            STM: STM3708(tdh)
            YPE: YPO0060(tdh)
            YPK: y0080(tdh)
            YPM: YP_0061(tdh1)
            YPA: YPA_3482
            YPN: YPN_3790
            YPP: YPDSF_3845
            YPS: YPTB0057(tdh)
            YPI: YpsIP31758_0072(tdh)
            YEN: YE0074(tdh)
            SFL: SF3656(tdh)
            SFX: S4111(tdh)
            SFV: SFV_3912(tdh)
            SSN: SSON_3788(tdh)
            SBO: SBO_3622(tdh)
            SDY: SDY_4049(tdh)
            ECA: ECA0168(tdh)
            PLU: plu4845(tdh)
            ENT: Ent638_0119
            KPN: KPN_03961(tdh)
            XCC: XCC0945(tdh)
            XCB: XC_3290
            XCV: XCV1052(tdh)
            XAC: XAC1022(tdh)
            XOO: XOO3684(tdh)
            XOM: XOO_3480(XOO3480)
            VCH: VCA0885
            VCO: VC0395_0353(tdh)
            VVU: VV2_1485
            VVY: VVA0305
            VPA: VPA1509
            VFI: VFA0417(tdh)
            PPR: PBPRA1730
            SON: SO_4673(tdh)
            SDN: Sden_3616
            SFR: Sfri_3939
            SAZ: Sama_0097
            SBL: Sbal_0057
            SLO: Shew_3710
            SPC: Sputcn32_3902
            SHE: Shewmr4_3901
            SHM: Shewmr7_3993
            SHN: Shewana3_4105
            SHW: Sputw3181_0049
            ILO: IL0269(tdh)
            CPS: CPS_0121(tdh)
            PHA: PSHAa2315(tdh)
            PAT: Patl_0062
            PIN: Ping_1853
            CBU: CBU_0112(tdh)
            CBD: COXBU7E912_1995(tdh)
            LPN: lpg0702(tdh)
            LPF: lpl0739(tdh)
            LPP: lpp0757(tdh)
            FTU: FTT0713c(tdh)
            FTF: FTF0713c(tdh)
            FTW: FTW_1528(tdh)
            FTL: FTL_1523
            FTH: FTH_1473(tdh)
            FTA: FTA_1607(tdh)
            FTN: FTN_0625(tdh)
            HCH: HCH_01632(tdh)
            AHA: AHA_4235(tdh)
            CVI: CV_1651(tdh)
            REH: H16_A1934(tdh)
            BMA: BMAA0006(tdh)
            BMV: BMASAVP1_1152(tdh)
            BML: BMA10299_1432(tdh)
            BMN: BMA10247_A0007(tdh)
            BXE: Bxe_B3020
            BVI: Bcep1808_3787
            BUR: Bcep18194_B3178(tdh)
            BCN: Bcen_5157
            BCH: Bcen2424_5702
            BAM: Bamb_4973
            BPS: BPSS0006(tdh)
            BPM: BURPS1710b_A1512(tdh)
            BPL: BURPS1106A_A0006(tdh)
            BPD: BURPS668_A0006(tdh)
            BTE: BTH_II0006(tdh)
            PCA: Pcar_2180
            ADE: Adeh_2095
            SAT: SYN_00564
            MLO: mlr8299
            MES: Meso_0444
            SME: SMc01564(tdh)
            RET: RHE_CH02951(tdh)
            RLE: RL3404(tdh)
            SIL: SPO3359(tdh)
            SIT: TM1040_3023
            RSP: RSP_2377(tdh) RSP_4033(tdh)
            RDE: RD1_0198(tdh)
            MMR: Mmar10_1594
            RRU: Rru_A2981
            ABA: Acid345_3920
            SUS: Acid_0475
            BSU: BG12685(tdh)
            BCE: BC0622
            BLI: BL03658(tdh)
            BLD: BLi01923(tdh)
            BAY: RBAM_016830(tdh)
            BPU: BPUM_1603(tdh)
            LSA: LSA0510 LSA0511
            STH: STH1873
            TTE: TTE2405(tdh3)
            SCO: SCO6799(tdh)
            SMA: SAV1628(tdh)
            AAU: AAur_1459(tdh) AAur_1903(tdh)
            PAC: PPA0402(tdh)
            SEN: SACE_6389(tdh)
            PCU: pc0810(tdh)
            AVA: Ava_3336 Ava_C0166
            FPS: FP0191(ltd)
            CCH: Cag_0401
            DRA: DR_1662
            DGE: Dgeo_0449
            TTH: TTC0201(tdh)
            TTJ: TTHA0569
            HWA: HQ2425A(tdh)
            NPH: NP1340A
            PHO: PH0655
            PAB: PAB2382
            PFU: PF0991
            TKO: TK0916
STRUCTURES  PDB: 2D8A  2DFV  2DQ4  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.103
            ExPASy - ENZYME nomenclature database: 1.1.1.103
            ExplorEnz - The Enzyme Database: 1.1.1.103
            ERGO genome analysis and discovery system: 1.1.1.103
            BRENDA, the Enzyme Database: 1.1.1.103
            CAS: 9067-99-6
///
ENTRY       EC 1.1.1.104                Enzyme
NAME        4-oxoproline reductase;
            hydroxy-L-proline oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4-hydroxy-L-proline:NAD+ oxidoreductase
REACTION    4-hydroxy-L-proline + NAD+ = 4-oxoproline + NADH + H+ [RN:R07146]
ALL_REAC    R07146 > R03290;
            (other) R03292
SUBSTRATE   4-hydroxy-L-proline [CPD:C01015];
            NAD+ [CPD:C00003]
PRODUCT     4-oxoproline [CPD:C01877];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Smith, T.E. and Mitoma, C.
  TITLE     Partial purification and some properties of 4-ketoproline reductase.
  JOURNAL   J. Biol. Chem. 237 (1962) 1177-1180.
  ORGANISM  rabbit
PATHWAY     PATH: map00330  Arginine and proline metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.104
            ExPASy - ENZYME nomenclature database: 1.1.1.104
            ExplorEnz - The Enzyme Database: 1.1.1.104
            ERGO genome analysis and discovery system: 1.1.1.104
            BRENDA, the Enzyme Database: 1.1.1.104
            CAS: 37250-37-6
///
ENTRY       EC 1.1.1.105                Enzyme
NAME        retinol dehydrogenase;
            retinol (vitamin A1) dehydrogenase;
            MDR;
            microsomal retinol dehydrogenase;
            all-trans retinol dehydrogenase;
            retinal reductase;
            retinene reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     retinol:NAD+ oxidoreductase
REACTION    retinol + NAD+ = retinal + NADH + H+ [RN:R02124]
ALL_REAC    R02124;
            (other) R03048
SUBSTRATE   retinol [CPD:C00473];
            NAD+ [CPD:C00003]
PRODUCT     retinal [CPD:C00376];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:5972368]
  AUTHORS   Koen AL, Shaw CR.
  TITLE     Retinol and alcohol dehydrogenases in retina and liver.
  JOURNAL   Biochim. Biophys. Acta. 128 (1966) 48-54.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00830  Retinol metabolism
ORTHOLOGY   KO: K00061  retinol dehydrogenase
GENES       HSA: 5959(RDH5)
            PTR: 467029(RDH5)
            MMU: 19682(Rdh5)
            CFA: 481099(RDH5)
            BTA: 281448(RDH5)
            GGA: 395452(LOC395452)
            XLA: 444623(MGC84134)
            XTR: 496830(LOC496830)
            CFF: CFF8240_1796
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.105
            ExPASy - ENZYME nomenclature database: 1.1.1.105
            ExplorEnz - The Enzyme Database: 1.1.1.105
            ERGO genome analysis and discovery system: 1.1.1.105
            BRENDA, the Enzyme Database: 1.1.1.105
            CAS: 9033-53-8
///
ENTRY       EC 1.1.1.106                Enzyme
NAME        pantoate 4-dehydrogenase;
            pantoate dehydrogenase;
            pantothenase;
            D-pantoate:NAD+ 4-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-pantoate:NAD+ 4-oxidoreductase
REACTION    (R)-pantoate + NAD+ = (R)-4-dehydropantoate + NADH + H+ [RN:R02471]
ALL_REAC    R02471
SUBSTRATE   (R)-pantoate [CPD:C00522];
            NAD+ [CPD:C00003]
PRODUCT     (R)-4-dehydropantoate [CPD:C01053];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4287370]
  AUTHORS   Goodhue CT, Snell EE.
  TITLE     The bacterial degradation of pantothenic acid. 3. Enzymatic
            formation of aldopantoic acid.
  JOURNAL   Biochemistry. 5 (1966) 403-8.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00770  Pantothenate and CoA biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.106
            ExPASy - ENZYME nomenclature database: 1.1.1.106
            ExplorEnz - The Enzyme Database: 1.1.1.106
            ERGO genome analysis and discovery system: 1.1.1.106
            BRENDA, the Enzyme Database: 1.1.1.106
            CAS: 37250-38-7
///
ENTRY       EC 1.1.1.107                Enzyme
NAME        pyridoxal 4-dehydrogenase;
            pyridoxal dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     pyridoxal:NAD+ 4-oxidoreductase
REACTION    pyridoxal + NAD+ = 4-pyridoxolactone + NADH + H+ [RN:R01707]
ALL_REAC    R01707
SUBSTRATE   pyridoxal [CPD:C00250];
            NAD+ [CPD:C00003]
PRODUCT     4-pyridoxolactone [CPD:C00971];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The enzyme acts on the hemiacetal form of the substrate.
REFERENCE   1  [PMID:4306030]
  AUTHORS   Burg RW, Snell EE.
  TITLE     The bacterial oxidation of vitamin B6. VI. Pyridoxal dehydrogenase
            and 4-pyridoxolactonase.
  JOURNAL   J. Biol. Chem. 244 (1969) 2585-9.
PATHWAY     PATH: map00750  Vitamin B6 metabolism
GENES       SMD: Smed_3152 Smed_3226
            OAN: Oant_0357
            XAU: Xaut_1060
            RSQ: Rsph17025_0945
            KRA: Krad_4195
            RRS: RoseRS_3434
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.107
            ExPASy - ENZYME nomenclature database: 1.1.1.107
            ExplorEnz - The Enzyme Database: 1.1.1.107
            ERGO genome analysis and discovery system: 1.1.1.107
            BRENDA, the Enzyme Database: 1.1.1.107
            CAS: 37250-39-8
///
ENTRY       EC 1.1.1.108                Enzyme
NAME        carnitine 3-dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     carnitine:NAD+ 3-oxidoreductase
REACTION    carnitine + NAD+ = 3-dehydrocarnitine + NADH + H+ [RN:R02395]
ALL_REAC    R02395
SUBSTRATE   carnitine [CPD:C00487];
            NAD+ [CPD:C00003]
PRODUCT     3-dehydrocarnitine [CPD:C02636];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4302217]
  AUTHORS   Aurich H, Kleber HP, Sorger H, Tauchert H.
  TITLE     [Purification and properties of carnitine dehydrogenase from
            Pseudomonas aeruginosa]
  JOURNAL   Eur. J. Biochem. 6 (1968) 196-201.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   2  [PMID:4310279]
  AUTHORS   Schopp W, Sorger H, Kleber HP, Aurich H.
  TITLE     [Kinetic studies of the reaction mechanism of carnitine
            dehydrogenase of Pseudomonas aeruginosa]
  JOURNAL   Eur. J. Biochem. 10 (1969) 56-60.
  ORGANISM  Pseudomonas aeruginosa
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.108
            ExPASy - ENZYME nomenclature database: 1.1.1.108
            ExplorEnz - The Enzyme Database: 1.1.1.108
            ERGO genome analysis and discovery system: 1.1.1.108
            BRENDA, the Enzyme Database: 1.1.1.108
            CAS: 9045-45-8
///
ENTRY       EC 1.1.1.109      Obsolete  Enzyme
NAME        Transferred to 1.3.1.28
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Transferred entry: now EC 1.3.1.28 2,3-dihydro-2,3-dihydroxybenzoate
            dehydrogenase (EC 1.1.1.109 created 1972, deleted 1976)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.109
            ExPASy - ENZYME nomenclature database: 1.1.1.109
            ExplorEnz - The Enzyme Database: 1.1.1.109
            ERGO genome analysis and discovery system: 1.1.1.109
            BRENDA, the Enzyme Database: 1.1.1.109
///
ENTRY       EC 1.1.1.110                Enzyme
NAME        indolelactate dehydrogenase;
            indolelactate:NAD+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (indol-3-yl)lactate:NAD+ oxidoreductase
REACTION    (indol-3-yl)lactate + NAD+ = (indol-3-yl)pyruvate + NADH + H+
            [RN:R01971]
ALL_REAC    R01971
SUBSTRATE   (indol-3-yl)lactate;
            NAD+ [CPD:C00003]
PRODUCT     (indol-3-yl)pyruvate [CPD:C00331];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4384683]
  AUTHORS   Jean M, DeMoss RD.
  TITLE     Indolelactate dehydrogenase from Clostridium sporogenes.
  JOURNAL   Can. J. Microbiol. 14 (1968) 429-35.
  ORGANISM  Clostridium sporogenes
PATHWAY     PATH: map00380  Tryptophan metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.110
            ExPASy - ENZYME nomenclature database: 1.1.1.110
            ExplorEnz - The Enzyme Database: 1.1.1.110
            ERGO genome analysis and discovery system: 1.1.1.110
            BRENDA, the Enzyme Database: 1.1.1.110
            CAS: 37250-41-2
///
ENTRY       EC 1.1.1.111                Enzyme
NAME        3-(imidazol-5-yl)lactate dehydrogenase;
            imidazol-5-yl lactate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-3-(imidazol-5-yl)lactate:NAD(P)+ oxidoreductase
REACTION    (S)-3-(imidazol-5-yl)lactate + NAD(P)+ = 3-(imidazol-5-yl)pyruvate +
            NAD(P)H + H+ [RN:R04185 R04186]
ALL_REAC    R04185 R04186
SUBSTRATE   (S)-3-(imidazol-5-yl)lactate [CPD:C03817];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     3-(imidazol-5-yl)pyruvate [CPD:C03277];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4303364]
  AUTHORS   Coote JG, Hassall H.
  TITLE     The role of imidazol-5-yl-lactate-nicotinamide-adenine dinucleotide
            phosphate oxidoreductase and histidine-2-oxoglutarate
            aminotransferase in the degradation of imidazol-5-yl-lactate by
            Pseudomonas acidovorans.
  JOURNAL   Biochem. J. 111 (1969) 237-9.
  ORGANISM  Pseudomonas acidovorans
REFERENCE   2  [PMID:4237631]
  AUTHORS   Cortese R, Brevet J, Hedegaard J, Roche J.
  TITLE     [Identification and purification of an alpha-ketoacid aromatic
            reductase of Escherichia coli B]
  JOURNAL   C. R. Seances. Soc. Biol. Fil. 162 (1968) 390-5.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.111
            ExPASy - ENZYME nomenclature database: 1.1.1.111
            ExplorEnz - The Enzyme Database: 1.1.1.111
            ERGO genome analysis and discovery system: 1.1.1.111
            BRENDA, the Enzyme Database: 1.1.1.111
            CAS: 37250-42-3
///
ENTRY       EC 1.1.1.112                Enzyme
NAME        indanol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     indan-1-ol:NAD(P)+ 1-oxidoreductase
REACTION    indan-1-ol + NAD(P)+ = indanone + NAD(P)H + H+ [RN:R03582 R03583]
ALL_REAC    R03582 R03583
SUBSTRATE   indan-1-ol [CPD:C01710];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     indanone [CPD:C01504];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     3(20)alpha-Hydroxysteroids are also oxidized, more slowly.
REFERENCE   1  [PMID:4397102]
  AUTHORS   Billings RE, Sullivan HR, McMahon RE.
  TITLE     The dehydrogenation of 1-indanol by a soluble oxidoreductase from
            bovine liver.
  JOURNAL   J. Biol. Chem. 246 (1971) 3512-7.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:2559080]
  AUTHORS   Hara A, Nakagawa M, Taniguchi H, Sawada H.
  TITLE     3(20)alpha-hydroxysteroid dehydrogenase activity of monkey liver
            indanol dehydrogenase.
  JOURNAL   J. Biochem. (Tokyo). 106 (1989) 900-3.
  ORGANISM  monkey
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.112
            ExPASy - ENZYME nomenclature database: 1.1.1.112
            ExplorEnz - The Enzyme Database: 1.1.1.112
            ERGO genome analysis and discovery system: 1.1.1.112
            BRENDA, the Enzyme Database: 1.1.1.112
            CAS: 37250-43-4
///
ENTRY       EC 1.1.1.113                Enzyme
NAME        L-xylose 1-dehydrogenase;
            L-xylose dehydrogenase;
            NADPH-xylose reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-xylose:NADP+ 1-oxidoreductase
REACTION    L-xylose + NADP+ = L-xylono-1,4-lactone + NADPH + H+ [RN:R03586]
ALL_REAC    R03586
SUBSTRATE   L-xylose [CPD:C01510];
            NADP+ [CPD:C00006]
PRODUCT     L-xylono-1,4-lactone [CPD:C02994];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also oxidizes D-arabinose and D-lyxose.
REFERENCE   1
  AUTHORS   Uehara, K. and Takeda, M.
  TITLE     L-Xylose dehydrogenase in bakers' yeast.
  JOURNAL   J. Biochem. (Tokyo) 52 (1962) 461-463.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.113
            ExPASy - ENZYME nomenclature database: 1.1.1.113
            ExplorEnz - The Enzyme Database: 1.1.1.113
            ERGO genome analysis and discovery system: 1.1.1.113
            BRENDA, the Enzyme Database: 1.1.1.113
            CAS: 37250-44-5
///
ENTRY       EC 1.1.1.114                Enzyme
NAME        apiose 1-reductase;
            D-apiose reductase;
            D-apiitol reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-apiitol:NAD+ 1-oxidoreductase
REACTION    D-apiitol + NAD+ = D-apiose + NADH + H+ [RN:R03577]
ALL_REAC    R03577
SUBSTRATE   D-apiitol [CPD:C01569];
            NAD+ [CPD:C00003]
PRODUCT     D-apiose [CPD:C01488];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Hanna, R., Picken, M. and Mendicino, J.
  TITLE     Purification of a specific D-apiitol dehydrogenase from a
            Micrococcus isolated from the surface of germinating parsley seeds.
  JOURNAL   Biochim. Biophys. Acta 315 (1973) 259-271.
  ORGANISM  Micrococcus
REFERENCE   2  [PMID:4314545]
  AUTHORS   Neal DL, Kindel PK.
  TITLE     D-apiose reductase from Aerobacter aerogenes.
  JOURNAL   J. Bacteriol. 101 (1970) 910-5.
  ORGANISM  Aerobacter aerogenes
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.114
            ExPASy - ENZYME nomenclature database: 1.1.1.114
            ExplorEnz - The Enzyme Database: 1.1.1.114
            ERGO genome analysis and discovery system: 1.1.1.114
            BRENDA, the Enzyme Database: 1.1.1.114
            CAS: 37250-45-6
///
ENTRY       EC 1.1.1.115                Enzyme
NAME        ribose 1-dehydrogenase (NADP+);
            D-ribose dehydrogenase (NADP+);
            NADP+-pentose-dehydrogenase;
            ribose 1-dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-ribose:NADP+ 1-oxidoreductase
REACTION    D-ribose + NADP+ + H2O = D-ribonate + NADPH + H+ [RN:R01079]
ALL_REAC    R01079
SUBSTRATE   D-ribose [CPD:C00121];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     D-ribonate [CPD:C01685];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts, more slowly, on D-xylose and other pentoses.
REFERENCE   1  [PMID:4381350]
  AUTHORS   Scher BM, Horecker BL.
  TITLE     Pentose metabolism in Candida. 3. The triphosphopyridine
            nucleotide-specific polyol dehydrogenase of Candida utilis.
  JOURNAL   Arch. Biochem. Biophys. 116 (1966) 117-28.
  ORGANISM  Candida utilis
REFERENCE   2  [PMID:4393642]
  AUTHORS   Schiwara HW, Domschke W, Domagk GF.
  TITLE     [Sugar dehydrogenases in mammalian liver. I. Differentiation of
            various sugar dehydrogenases from pig liver by disc electrophoresis
            and ion exchange chromatography]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 349 (1968) 1575-81.
  ORGANISM  pig [GN:ssc]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.115
            ExPASy - ENZYME nomenclature database: 1.1.1.115
            ExplorEnz - The Enzyme Database: 1.1.1.115
            ERGO genome analysis and discovery system: 1.1.1.115
            BRENDA, the Enzyme Database: 1.1.1.115
            CAS: 37250-46-7
///
ENTRY       EC 1.1.1.116                Enzyme
NAME        D-arabinose 1-dehydrogenase;
            NAD+-pentose-dehydrogenase;
            arabinose(fucose)dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-arabinose:NAD+ 1-oxidoreductase
REACTION    D-arabinose + NAD+ = D-arabinono-1,4-lactone + NADH + H+ [RN:R01574]
ALL_REAC    R01574
SUBSTRATE   D-arabinose [CPD:C00216];
            NAD+ [CPD:C00003]
PRODUCT     D-arabinono-1,4-lactone [CPD:C00652];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Palleroni, N.J. and Doudoroff, M.
  TITLE     Metabolism of carbohydrates by Pseudomonas saccharophilla. III.
            Oxidation of D-arabinose.
  JOURNAL   J. Bacteriol. 74 (1957) 180-185.
  ORGANISM  Pseudomonas saccharophila
REFERENCE   2  [PMID:4393642]
  AUTHORS   Schiwara HW, Domschke W, Domagk GF.
  TITLE     [Sugar dehydrogenases in mammalian liver. I. Differentiation of
            various sugar dehydrogenases from pig liver by disc electrophoresis
            and ion exchange chromatography]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 349 (1968) 1575-81.
  ORGANISM  pig [GN:ssc]
ORTHOLOGY   KO: K00062  D-arabinose 1-dehydrogenase
GENES       SCE: YBR149W(ARA1)
            PIC: PICST_59505(ARA1)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.116
            ExPASy - ENZYME nomenclature database: 1.1.1.116
            ExplorEnz - The Enzyme Database: 1.1.1.116
            ERGO genome analysis and discovery system: 1.1.1.116
            BRENDA, the Enzyme Database: 1.1.1.116
            CAS: 37250-47-8
///
ENTRY       EC 1.1.1.117                Enzyme
NAME        D-arabinose 1-dehydrogenase [NAD(P)+];
            D-arabinose 1-dehydrogenase [NAD(P)+]
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-arabinose:NAD(P)+ 1-oxidoreductase
REACTION    D-arabinose + NAD(P)+ = D-arabinono-1,4-lactone + NAD(P)H + H+
            [RN:R01574 R01575]
ALL_REAC    R01574 R01575
SUBSTRATE   D-arabinose [CPD:C00216];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     D-arabinono-1,4-lactone [CPD:C00652];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on L-galactose, 6-deoxy- and 3,6-dideoxy-L-galactose.
REFERENCE   1  [PMID:5845847]
  AUTHORS   Cline AL, Hu AS.
  TITLE     The isolation of three sugar dehydrogenases from a psuedomonad.
  JOURNAL   J. Biol. Chem. 240 (1965) 4488-92.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:5845848]
  AUTHORS   Cline AL, Hu AS.
  TITLE     Enzymatic characterization and comparison of three sugar
            dehydrogenases from a pseudomonad.
  JOURNAL   J. Biol. Chem. 240 (1965) 4493-7.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:5845849]
  AUTHORS   Cline AL, Hu AS.
  TITLE     Some physical properties of three sugar dehydrogenases from a
            pseudomonad.
  JOURNAL   J. Biol. Chem. 240 (1965) 4498-502.
  ORGANISM  Pseudomonas sp.
ORTHOLOGY   KO: K00063  D-arabinose 1-dehydrogenase
GENES       SCE: YBR149W(ARA1)
STRUCTURES  PDB: 2H6E  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.117
            ExPASy - ENZYME nomenclature database: 1.1.1.117
            ExplorEnz - The Enzyme Database: 1.1.1.117
            ERGO genome analysis and discovery system: 1.1.1.117
            BRENDA, the Enzyme Database: 1.1.1.117
            CAS: 37250-48-9
///
ENTRY       EC 1.1.1.118                Enzyme
NAME        glucose 1-dehydrogenase (NAD+);
            D-glucose:NAD+ oxidoreductase;
            D-aldohexose dehydrogenase;
            glucose 1-dehydrogenase (NAD+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-glucose:NAD+ 1-oxidoreductase
REACTION    D-glucose + NAD+ = D-glucono-1,5-lactone + NADH + H+ [RN:R00300]
ALL_REAC    R00300
SUBSTRATE   D-glucose [CPD:C00031];
            NAD+ [CPD:C00003]
PRODUCT     D-glucono-1,5-lactone [CPD:C00198];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Hu, A.S.L. and Cline, A.L.
  TITLE     The regulation of some sugar dehydrogenases in a pseudomonad.
  JOURNAL   Biochim. Biophys. Acta 93 (1964) 237-245.
  ORGANISM  Pseudomonas saccharophila
STRUCTURES  PDB: 2DTD  2DTE  2DTX  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.118
            ExPASy - ENZYME nomenclature database: 1.1.1.118
            ExplorEnz - The Enzyme Database: 1.1.1.118
            ERGO genome analysis and discovery system: 1.1.1.118
            BRENDA, the Enzyme Database: 1.1.1.118
            CAS: 37250-49-0
///
ENTRY       EC 1.1.1.119                Enzyme
NAME        glucose 1-dehydrogenase (NADP+);
            nicotinamide adenine dinucleotide phosphate-linked aldohexose
            dehydrogenase;
            NADP+-linked aldohexose dehydrogenase;
            NADP+-dependent glucose dehydrogenase;
            glucose 1-dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-glucose:NADP+ 1-oxidoreductase
REACTION    D-glucose + NADP+ = D-glucono-1,5-lactone + NADPH + H+ [RN:R07147]
ALL_REAC    R07147;
            (other) R00301
SUBSTRATE   D-glucose [CPD:C00031];
            NADP+ [CPD:C00006]
PRODUCT     D-glucono-1,5-lactone [CPD:C00198];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also oxidizes D-mannose, 2-deoxy-D-glucose and
            2-amino-2-deoxy-D-mannose.
REFERENCE   1
  AUTHORS   Adachi, O. and Ameyama, M.
  TITLE     D-Glucose dehydrogenase from Gluconobacter suboxydans.
  JOURNAL   Methods Enzymol. 89 (1982) 159-163.
  ORGANISM  Gluconobacter suboxydans
REFERENCE   2  [PMID:4384672]
  AUTHORS   Avigad G, Alroy Y, Englard S.
  TITLE     Purification and properties of a nicotinamide adenine dinucleotide
            phosphate-linked aldohexose dehydrogeanse from Gluconobacter
            cerinus.
  JOURNAL   J. Biol. Chem. 243 (1968) 1936-41.
  ORGANISM  Gluconobacter cerinus
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.119
            ExPASy - ENZYME nomenclature database: 1.1.1.119
            ExplorEnz - The Enzyme Database: 1.1.1.119
            ERGO genome analysis and discovery system: 1.1.1.119
            BRENDA, the Enzyme Database: 1.1.1.119
            CAS: 37250-50-3
///
ENTRY       EC 1.1.1.120                Enzyme
NAME        galactose 1-dehydrogenase (NADP+);
            D-galactose dehydrogenase (NADP+);
            galactose 1-dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-galactose:NADP+ 1-oxidoreductase
REACTION    D-galactose + NADP+ = D-galactonolactone + NADPH + H+ [RN:R07132]
ALL_REAC    R07132;
            (other) R01096 R01097
SUBSTRATE   D-galactose [CPD:C00124];
            NADP+ [CPD:C00006]
PRODUCT     D-galactonolactone [CPD:C15483];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on L-arabinose, 6-deoxy- and 2-deoxy-D-galactose.
REFERENCE   1  [PMID:5845847]
  AUTHORS   Cline AL, Hu AS.
  TITLE     The isolation of three sugar dehydrogenases from a psuedomonad.
  JOURNAL   J. Biol. Chem. 240 (1965) 4488-92.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:5845848]
  AUTHORS   Cline AL, Hu AS.
  TITLE     Enzymatic characterization and comparison of three sugar
            dehydrogenases from a pseudomonad.
  JOURNAL   J. Biol. Chem. 240 (1965) 4493-7.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:5845849]
  AUTHORS   Cline AL, Hu AS.
  TITLE     Some physical properties of three sugar dehydrogenases from a
            pseudomonad.
  JOURNAL   J. Biol. Chem. 240 (1965) 4498-502.
  ORGANISM  Pseudomonas sp.
REFERENCE   4  [PMID:4387016]
  AUTHORS   Schiwara HW, Domagk GF.
  TITLE     [Degradation of deoxysurgars by bacterial enzymes. V. Purification
            and characterization of an NADP-dependent abequose dehydrogenase
            from Pseudomonas putida]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 349 (1968) 1321-9.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00052  Galactose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.120
            ExPASy - ENZYME nomenclature database: 1.1.1.120
            ExplorEnz - The Enzyme Database: 1.1.1.120
            ERGO genome analysis and discovery system: 1.1.1.120
            BRENDA, the Enzyme Database: 1.1.1.120
            CAS: 37250-51-4
///
ENTRY       EC 1.1.1.121                Enzyme
NAME        aldose 1-dehydrogenase;
            aldose dehydrogenase;
            dehydrogenase, D-aldohexose
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-aldose:NAD+ 1-oxidoreductase
REACTION    D-aldose + NAD+ = D-aldonolactone + NADH + H+ [RN:R02847]
ALL_REAC    R02847
SUBSTRATE   D-aldose [CPD:C00737];
            NAD+ [CPD:C00003]
PRODUCT     D-aldonolactone [CPD:C00198];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Acts on D-glucose, 2-deoxy- and 6-deoxy-D-glucose, D-galactose,
            6-deoxy-D-galactose, 2-deoxy-L-arabinose and D-xylose.
REFERENCE   1  [PMID:5845847]
  AUTHORS   Cline AL, Hu AS.
  TITLE     The isolation of three sugar dehydrogenases from a psuedomonad.
  JOURNAL   J. Biol. Chem. 240 (1965) 4488-92.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:5845848]
  AUTHORS   Cline AL, Hu AS.
  TITLE     Enzymatic characterization and comparison of three sugar
            dehydrogenases from a pseudomonad.
  JOURNAL   J. Biol. Chem. 240 (1965) 4493-7.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:5845849]
  AUTHORS   Cline AL, Hu AS.
  TITLE     Some physical properties of three sugar dehydrogenases from a
            pseudomonad.
  JOURNAL   J. Biol. Chem. 240 (1965) 4498-502.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.121
            ExPASy - ENZYME nomenclature database: 1.1.1.121
            ExplorEnz - The Enzyme Database: 1.1.1.121
            ERGO genome analysis and discovery system: 1.1.1.121
            BRENDA, the Enzyme Database: 1.1.1.121
            CAS: 9076-61-3
///
ENTRY       EC 1.1.1.122                Enzyme
NAME        D-threo-aldose 1-dehydrogenase;
            L-fucose dehydrogenase;
            (2S,3R)-aldose dehydrogenase;
            dehydrogenase, L-fucose;
            L-fucose (D-arabinose) dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-threo-aldose:NAD+ 1-oxidoreductase
REACTION    a D-threo-aldose + NAD+ = a D-threo-aldono-1,5-lactone + NADH + H+
            [RN:R07148]
ALL_REAC    R07148;
            (other) R01756 R07675
SUBSTRATE   D-threo-aldose [CPD:C02143];
            NAD+ [CPD:C00003]
PRODUCT     D-threo-aldono-1,5-lactone [CPD:C00198];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Acts on L-fucose, D-arabinose and L-xylose; the animal enzyme was
            also shown to act on L-arabinose, and the enzyme from Pseudomonas
            caryophylli on L-glucose.
REFERENCE   1  [PMID:40609]
  AUTHORS   Sasajima KI, Sinskey AJ.
  TITLE     Oxidation of L-glucose by a Pseudomonad.
  JOURNAL   Biochim. Biophys. Acta. 571 (1979) 120-6.
  ORGANISM  Pseudomonas caryophylli
REFERENCE   2  [PMID:4309152]
  AUTHORS   Schachter H, Sarney J, McGuire EJ, Roseman S.
  TITLE     Isolation of diphosphopyridine nucleotide-dependent L-fucose
            dehydrogenase from pork liver.
  JOURNAL   J. Biol. Chem. 244 (1969) 4785-92.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K00064  D-threo-aldose 1-dehydrogenase
GENES       ATH: AT4G33670
            PIC: PICST_58212(YMT1)
            ECI: UTI89_C0319
            ECA: ECA0250
            XCC: XCC0141 XCC4065
            XCB: XC_0150 XC_4155
            XCV: XCV0143 XCV4282
            XAC: XAC0158 XAC4184
            XOO: XOO4539
            XOM: XOO_4276(XOO4276)
            PST: PSPTO_3075
            PFO: Pfl_3523
            BXE: Bxe_A2190
            BUR: Bcep18194_B0238
            POL: Bpro_2212
            MXA: MXAN_0697
            MLO: mll8482 mlr3332
            SME: SMa1403 SMc02775
            ATU: Atu3528
            ATC: AGR_L_2607
            RET: RHE_CH00494(ypch00182) RHE_PF00418(ypf00225)
            RLE: RL0520
            BJA: blr1124
            RSP: RSP_0351
            RDE: RD1_0506 RD1_3762
            BAN: BA3463 BA5079
            BAR: GBAA3463 GBAA5079
            BAA: BA_3961 BA_5496
            BAT: BAS3210 BAS4717
            BCE: BC3410
            BCZ: BCZK3116(fdh)
            BTK: BT9727_3188(fdh)
            BCL: ABC1415
            OIH: OB0307
            SEN: SACE_3934
            RBA: RB5820(fucO)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.122
            ExPASy - ENZYME nomenclature database: 1.1.1.122
            ExplorEnz - The Enzyme Database: 1.1.1.122
            ERGO genome analysis and discovery system: 1.1.1.122
            BRENDA, the Enzyme Database: 1.1.1.122
            CAS: 9082-70-6
///
ENTRY       EC 1.1.1.123                Enzyme
NAME        sorbose 5-dehydrogenase (NADP+);
            5-ketofructose reductase;
            5-keto-D-fructose reductase;
            sorbose (nicotinamide adenine dinucleotide phosphate) dehydrogenase;
            reduced nicotinamide adenine dinucleotide phosphate-linked
            reductase;
            sorbose 5-dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-sorbose:NADP+ 5-oxidoreductase
REACTION    L-sorbose + NADP+ = 5-dehydro-D-fructose + NADPH + H+ [RN:R01694]
ALL_REAC    R01694
SUBSTRATE   L-sorbose [CPD:C00247];
            NADP+ [CPD:C00006]
PRODUCT     5-dehydro-D-fructose [CPD:C00273];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4392628]
  AUTHORS   Englard S, Kaysen G, Avigad G.
  TITLE     5-keto-D-fructose. VI. A specific reduced nicotinamide adenine
            dinucleotide phosphate-linked reductase from yeast.
  JOURNAL   J. Biol. Chem. 245 (1970) 1311-8.
  ORGANISM  Gluconobacter cerinus, Saccharomyces cerevisiae [GN:sce], Torula
            utilis, Bacillus subtilis [GN:bsu], Aerobacter cloacae, Proteus
            vulgaris, Aerobacter aerogenes, Bacillus megaterium, Bacillus brevis
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.123
            ExPASy - ENZYME nomenclature database: 1.1.1.123
            ExplorEnz - The Enzyme Database: 1.1.1.123
            ERGO genome analysis and discovery system: 1.1.1.123
            BRENDA, the Enzyme Database: 1.1.1.123
            CAS: 37250-52-5
///
ENTRY       EC 1.1.1.124                Enzyme
NAME        fructose 5-dehydrogenase (NADP+);
            5-ketofructose reductase (NADP+);
            5-keto-D-fructose reductase (NADP+);
            fructose 5-(nicotinamide adenine dinucleotide phosphate)
            dehydrogenase;
            D-(-)fructose:(NADP+) 5-oxidoreductase;
            fructose 5-dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-fructose:NADP+ 5-oxidoreductase
REACTION    D-fructose + NADP+ = 5-dehydro-D-fructose + NADPH + H+ [RN:R00871]
ALL_REAC    R00871
SUBSTRATE   D-fructose [CPD:C00095];
            NADP+ [CPD:C00006]
PRODUCT     5-dehydro-D-fructose [CPD:C00273];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Ameyama, M., Matsushita, K., Shinagawa, E. and Adachi, O.
  TITLE     5-keto-D-Fructose reductase of Gluconobacter industrius
            Purification, crystallization and properties.
  JOURNAL   Agric. Biol. Chem. 45 (1981) 863-869.
  ORGANISM  Gluconobacter industrius
REFERENCE   2  [PMID:4379259]
  AUTHORS   Avigad G, Englard S, Pifko S.
  TITLE     5-Keto-D-fructose. IV. A specific reduced nicotinamide adenine
            dinucleotide phosphate-linked reductase from Gluconobacter cerinus.
  JOURNAL   J. Biol. Chem. 241 (1966) 373-8.
  ORGANISM  Gluconobacter cerinus
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.124
            ExPASy - ENZYME nomenclature database: 1.1.1.124
            ExplorEnz - The Enzyme Database: 1.1.1.124
            ERGO genome analysis and discovery system: 1.1.1.124
            BRENDA, the Enzyme Database: 1.1.1.124
            CAS: 37250-53-6
///
ENTRY       EC 1.1.1.125                Enzyme
NAME        2-deoxy-D-gluconate 3-dehydrogenase;
            2-deoxygluconate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-deoxy-D-gluconate:NAD+ 3-oxidoreductase
REACTION    2-deoxy-D-gluconate + NAD+ = 3-dehydro-2-deoxy-D-gluconate + NADH +
            H+ [RN:R04049]
ALL_REAC    R04049;
            (other) R01542
SUBSTRATE   2-deoxy-D-gluconate [CPD:C02782];
            NAD+ [CPD:C00003]
PRODUCT     3-dehydro-2-deoxy-D-gluconate [CPD:C03926];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Eichhorn, M.M. and Cynkin, M.A.
  TITLE     Microbial metabolism of 2-deoxyglucose; 2-deoxyglucose acid
            dehydrogenase.
  JOURNAL   Biochemistry 4 (1965) 159-165.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K00065  2-deoxy-D-gluconate 3-dehydrogenase
GENES       XLA: 447566(MGC84267)
            XTR: 448527(MGC79752)
            AFM: AFUA_1G14350
            UMA: UM05923.1
            ECO: b2842(kduD)
            ECJ: JW2810(kduD)
            ECE: Z4162(kduD)
            ECS: ECs3699
            ECC: c3439(kduD)
            ECI: UTI89_C3245
            ECP: ECP_2855
            ECV: APECO1_3664(kduD)
            ECW: EcE24377A_3164(kduD)
            ECX: EcHS_A2989(kduD)
            STY: STY3162(kduD)
            STT: t2927(kduD)
            SPT: SPA2884(kduD)
            SEC: SC2956(kduD)
            STM: STM3017(kduD)
            YPE: YPO0839(kduD2) YPO1724(kduD1)
            YPK: y1886(kduD) y3224(kduD)
            YPM: YP_1749(kduD) YP_3535(kduD2)
            YPA: YPA_0431 YPA_1794
            YPN: YPN_1906 YPN_3041
            YPS: YPTB2357(kduD1) YPTB3083(kduD2)
            YPI: YpsIP31758_0935(kduD2) YpsIP31758_1693(kduD1)
            SFL: SF2852(kduD)
            SFX: S3050(kduD)
            SFV: SFV_2920(kduD)
            SSN: SSON_3002(kduD)
            SBO: SBO_2734(kduD)
            ECA: ECA2401(kduD)
            MSU: MS0563(fabG)
            XCC: XCC0152(kduD)
            XCB: XC_0161
            XCV: XCV0153(kduD)
            XAC: XAC0169(kduD)
            VVU: VV2_0914 VV2_1093
            VVY: VV0552 VVA1401 VVA1616
            VPA: VPA0077
            VFI: VFA0997
            PPR: PBPRB0149(kduD) PBPRB1737
            PSB: Psyr_2568
            PSP: PSPPH_2726
            SDE: Sde_1283
            REU: Reut_B5289
            BMA: BMAA1811(kduD)
            BMV: BMASAVP1_0809(kduD)
            BML: BMA10299_1100(kduD)
            BMN: BMA10247_A2073(kduD)
            BPS: BPSS0258
            BPM: BURPS1710b_1870 BURPS1710b_A1794(kduD)
            BPL: BURPS1106A_A0363(kduD)
            NEU: NE1567(kduD)
            MLO: mll4054
            MES: Meso_0260
            SME: SMb21348
            ATU: Atu3141(kduD)
            ATC: AGR_L_3337
            RET: RHE_PE00399(ype00207)
            RLE: RL1748 pRL110529
            BME: BMEII0316
            BMF: BAB2_0253
            BMS: BRA0981
            BMB: BruAb2_0253
            BJA: bll1082(kduD) bll4353(kduD)
            BRA: BRADO3552
            BBT: BBta_3977
            RPA: RPA4786(rhlG)
            RPB: RPB_0770
            CCR: CC_1492
            RSP: RSP_0481
            RDE: RD1_3809(gno) RD1_3945
            MMR: Mmar10_0232
            SAL: Sala_3035
            BSU: BG11400(kduD)
            BHA: BH2167(kduD)
            BCZ: pE33L466_0344(kduD)
            BLI: BL02435(kduD)
            BLD: BLi03830(kduD)
            BCL: ABC0993(kduD) ABC1038 ABC1041
            BPU: BPUM_3247(kduD)
            OIH: OB2814
            SPH: MGAS10270_Spy0519(idnO)
            SPI: MGAS10750_Spy0543(idnO)
            SPJ: MGAS2096_Spy0536(idnO)
            SPK: MGAS9429_Spy0515(idnO)
            LSL: LSL_1793(kduD)
            LBR: LVIS_0326
            LCA: LSEI_2672
            CAC: CAC0361(kduD)
            CPF: CPF_0396(kduD)
            CPR: CPR_0392(kduD)
            MTC: MT1753.1
            MSM: MSMEG_3379 MSMEG_4117
            SCO: SCO3476(SCE65.12c)
            TFU: Tfu_1298
            FAL: FRAAL3120 FRAAL4773(kduD)
            SEN: SACE_0380(kduD)
            RXY: Rxyl_0537
            DET: DET0736
            DEH: cbdb_A689
            TTH: TT_P0037
            TTJ: TTHB080
STRUCTURES  PDB: 1X1E  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.125
            ExPASy - ENZYME nomenclature database: 1.1.1.125
            ExplorEnz - The Enzyme Database: 1.1.1.125
            ERGO genome analysis and discovery system: 1.1.1.125
            BRENDA, the Enzyme Database: 1.1.1.125
            CAS: 37250-54-7
///
ENTRY       EC 1.1.1.126                Enzyme
NAME        2-dehydro-3-deoxy-D-gluconate 6-dehydrogenase;
            2-keto-3-deoxy-D-gluconate dehydrogenase;
            2-keto-3-deoxygluconate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-dehydro-3-deoxy-D-gluconate:NADP+ 6-oxidoreductase
REACTION    2-dehydro-3-deoxy-D-gluconate + NADP+ =
            (4S,5S)-4,5-dihydroxy-2,6-dioxohexanoate + NADPH + H+ [RN:R01543]
ALL_REAC    R01543
SUBSTRATE   2-dehydro-3-deoxy-D-gluconate [CPD:C00204];
            NADP+ [CPD:C00006]
PRODUCT     (4S,5S)-4,5-dihydroxy-2,6-dioxohexanoate [CPD:C04471];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Preiss, J. and Ashwell, G.
  TITLE     Alginic acid metabolism in bacteria. II. The enzymatic reduction of
            4-deoxy-L-erythro-5-hexoseulose uronic acid to
            2-keto-3-deoxy-D-gluconic acid.
  JOURNAL   J. Biol. Chem. 237 (1962) 317-321.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.126
            ExPASy - ENZYME nomenclature database: 1.1.1.126
            ExplorEnz - The Enzyme Database: 1.1.1.126
            ERGO genome analysis and discovery system: 1.1.1.126
            BRENDA, the Enzyme Database: 1.1.1.126
            CAS: 37250-55-8
///
ENTRY       EC 1.1.1.127                Enzyme
NAME        2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase;
            2-keto-3-deoxygluconate 5-dehydrogenase;
            2-keto-3-deoxy-D-gluconate dehydrogenase;
            2-keto-3-deoxygluconate (nicotinamide adenine dinucleotide
            (phosphate)) dehydrogenase;
            2-keto-3-deoxy-D-gluconate (3-deoxy-D-glycero-2,5-hexodiulosonic
            acid) dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-dehydro-3-deoxy-D-gluconate:NAD+ 5-oxidoreductase
REACTION    2-dehydro-3-deoxy-D-gluconate + NAD+ =
            (4S)-4,6-dihydroxy-2,5-dioxohexanoate + NADH + H+ [RN:R01542]
ALL_REAC    R01542
SUBSTRATE   2-dehydro-3-deoxy-D-gluconate [CPD:C00204];
            NAD+ [CPD:C00003]
PRODUCT     (4S)-4,6-dihydroxy-2,5-dioxohexanoate [CPD:C04349];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The enzyme from Pseudomonas acts equally well on NAD+ or NADP+,
            while that from Erwinia chrysanthemi and Escherichia coli is more
            specific for NAD+.
REFERENCE   1
  AUTHORS   Condemine, G., Hugouvieux-Cotte-Pattat, N. and Robert-Baudouy, J.
  TITLE     An enzyme in the pectolytic pathway of Erwinia chrysanthemi:
            3-keto-3-deoxygluconate oxidoreductase.
  JOURNAL   J. Gen. Microbiol. 130 (1984) 2839-2844.
  ORGANISM  Erwinia chrysanthemi
REFERENCE   2
  AUTHORS   Preiss, J. and Ashwell, G.
  TITLE     Polygalacturonic acid metabolism in bacteria. II. Formation and
            metabolism of 3-deoxy-D-glycero-2,5-hexodiulosonic acid.
  JOURNAL   J. Biol. Chem. 238 (1963) 1577-1583.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.127
            ExPASy - ENZYME nomenclature database: 1.1.1.127
            ExplorEnz - The Enzyme Database: 1.1.1.127
            ERGO genome analysis and discovery system: 1.1.1.127
            BRENDA, the Enzyme Database: 1.1.1.127
            CAS: 37250-56-9
///
ENTRY       EC 1.1.1.128                Enzyme
NAME        L-idonate 2-dehydrogenase;
            5-ketogluconate 2-reductase;
            5-keto-D-gluconate 2-reductase;
            L-idonate dehydrogenase;
            5-ketogluconate 2-reductase;
            reductase, 5-ketogluconate 5- (L-idonate-forming);
            5KGR;
            5-ketoglucono-idono-reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-idonate:NADP+ 2-oxidoreductase
REACTION    L-idonate + NADP+ = 5-dehydro-D-gluconate + NADPH + H+ [RN:R05684]
ALL_REAC    R05684
SUBSTRATE   L-idonate [CPD:C00770];
            NADP+ [CPD:C00006]
PRODUCT     5-dehydro-D-gluconate [CPD:C01062];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Takagi, Y.
  TITLE     A new enzyme, 5-ketoglucono-idono-reductase.
  JOURNAL   Agric. Biol. Chem. 26 (1962) 719-720.
GENES       ECP: ECP_4516
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.128
            ExPASy - ENZYME nomenclature database: 1.1.1.128
            ExplorEnz - The Enzyme Database: 1.1.1.128
            ERGO genome analysis and discovery system: 1.1.1.128
            BRENDA, the Enzyme Database: 1.1.1.128
            CAS: 37250-57-0
///
ENTRY       EC 1.1.1.129                Enzyme
NAME        L-threonate 3-dehydrogenase;
            threonate dehydrogenase;
            L-threonic acid dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-threonate:NAD+ 3-oxidoreductase
REACTION    L-threonate + NAD+ = 3-dehydro-L-threonate + NADH + H+ [RN:R03733]
ALL_REAC    R03733
SUBSTRATE   L-threonate [CPD:C01620];
            NAD+ [CPD:C00003]
PRODUCT     3-dehydro-L-threonate [CPD:C03064];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:14154441]
  AUTHORS   ASPEN AJ, JAKOBY WB.
  TITLE     L-THREONIC ACID DEHYDROGENASE: PURIFICATION AND PROPERTIES.
  JOURNAL   J. Biol. Chem. 239 (1964) 710-3.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.129
            ExPASy - ENZYME nomenclature database: 1.1.1.129
            ExplorEnz - The Enzyme Database: 1.1.1.129
            ERGO genome analysis and discovery system: 1.1.1.129
            BRENDA, the Enzyme Database: 1.1.1.129
            CAS: 37250-59-2
///
ENTRY       EC 1.1.1.130                Enzyme
NAME        3-dehydro-L-gulonate 2-dehydrogenase;
            3-keto-L-gulonate dehydrogenase;
            3-ketogulonate dehydrogenase;
            3-keto-L-gulonate dehydrogenase;
            3-ketogulonate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-dehydro-L-gulonate:NAD(P)+ 2-oxidoreductase
REACTION    3-dehydro-L-gulonate + NAD(P)+ =
            (4R,5S)-4,5,6-trihydroxy-2,3-dioxohexanoate + NAD(P)H + H+
            [RN:R02637 R02639]
ALL_REAC    R02637 R02639
SUBSTRATE   3-dehydro-L-gulonate [CPD:C00618];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     (4R,5S)-4,5,6-trihydroxy-2,3-dioxohexanoate [CPD:C04575];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Volk, W.A. and Larsen, J.L.
  TITLE     beta-Keto-L-gulonic acid as an intermediate in the bacterial
            metabolism of ascorbic acid.
  JOURNAL   J. Biol. Chem. 237 (1962) 2454-2457.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K08092  3-dehydro-L-gulonate 2-dehydrogenase
GENES       ECO: b3575(yiaK)
            ECJ: JW3547(yiaK)
            ECC: c4396(yiaK)
            ECI: UTI89_C4117(yiaK)
            ECV: APECO1_2875(yiaK)
            ECW: EcE24377A_4072(dlgD)
            ECX: EcHS_A3779
            STY: STY4130
            STT: t3851
            SPT: SPA3519(yiaK)
            STM: STM3668(yiaK)
            SFL: SF3619(yiaK)
            SFX: S4150(yiaK)
            SFV: SFV_3965(yiaK)
            SBO: SBO_3583(yiaK)
            HIN: HI1031
            PMU: PM1256
            MSU: MS0054
            APL: APL_1573
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.130
            ExPASy - ENZYME nomenclature database: 1.1.1.130
            ExplorEnz - The Enzyme Database: 1.1.1.130
            ERGO genome analysis and discovery system: 1.1.1.130
            BRENDA, the Enzyme Database: 1.1.1.130
            CAS: 37250-61-6
///
ENTRY       EC 1.1.1.131                Enzyme
NAME        mannuronate reductase;
            mannonate dehydrogenase;
            mannonate (nicotinamide adenine dinucleotide
            (phosphate))dehydrogenase;
            mannonate dehydrogenase;
            mannuronate reductase;
            mannonate dehydrogenase (NAD(P)+);
            D-mannonate:nicotinamide adenine dinucleotide (phosphate
            oxidoreductase (D-mannuronate-forming))
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-mannonate:NAD(P)+ 6-oxidoreductase
REACTION    D-mannonate + NAD(P)+ = D-mannuronate + NAD(P)H + H+ [RN:R02455
            R02456]
ALL_REAC    R02455 R02456
SUBSTRATE   D-mannonate [CPD:C00514];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     D-mannuronate [CPD:C02024];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4388117]
  AUTHORS   Farmer JJ 3rd, Eagon RG.
  TITLE     Aldohexuronic acid catabolism by a soil Aeromonas.
  JOURNAL   J. Bacteriol. 97 (1969) 97-106.
  ORGANISM  Aeromonas sp.
GENES       HIP: CGSHiEE_03060
            HIQ: CGSHiGG_02770
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.131
            ExPASy - ENZYME nomenclature database: 1.1.1.131
            ExplorEnz - The Enzyme Database: 1.1.1.131
            ERGO genome analysis and discovery system: 1.1.1.131
            BRENDA, the Enzyme Database: 1.1.1.131
            CAS: 37250-62-7
///
ENTRY       EC 1.1.1.132                Enzyme
NAME        GDP-mannose 6-dehydrogenase;
            guanosine diphosphomannose dehydrogenase;
            GDP-mannose dehydrogenase;
            guanosine diphosphomannose dehydrogenase;
            guanosine diphospho-D-mannose dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     GDP-D-mannose:NAD+ 6-oxidoreductase
REACTION    GDP-D-mannose + 2 NAD+ + H2O = GDP-D-mannuronate + 2 NADH + 2 H+
            [RN:R00880]
ALL_REAC    R00880
SUBSTRATE   GDP-D-mannose [CPD:C00096];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     GDP-D-mannuronate [CPD:C00976];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts on the corresponding deoxynucleoside diphosphate
            derivative as a substrate.
REFERENCE   1
  AUTHORS   Preiss, J.
  TITLE     Sugar nucleotide reaction in Arthrobacter. II. Biosynthesis of
            guanosine diphosphomannuronate.
  JOURNAL   J. Biol. Chem. 239 (1964) 3127-3132.
  ORGANISM  Arthrobacter sp.
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K00066  GDPmannose 6-dehydrogenase
GENES       PAE: PA3540(algD)
            PAU: PA14_18580(algD)
            PPU: PP_1288(algD)
            PPF: Pput_4437
            PST: PSPTO_1243(algD)
            PSB: Psyr_1063
            PSP: PSPPH_1118(algD)
            PFL: PFL_1024(algD)
            PFO: Pfl_0960
            PEN: PSEEN3453(algD-2) PSEEN4535(algD)
            PMY: Pmen_1031 Pmen_1678
            ACI: ACIAD0087
            ABO: ABO_0384(algD) ABO_0908(wbpO)
            RFR: Rfer_0673
            EBA: ebA4268(algD)
            AZO: azo3269(algD)
            NIS: NIS_0191
            BJA: blr6296
            BRA: BRADO5154 BRADO7047
            BBT: BBta_5622
            NAR: Saro_3220
            ABA: Acid345_3792
            BTK: BT9727_4949
            CSC: Csac_2360
            MSM: MSMEG_5957(algD)
            MVA: Mvan_1699
            SCO: SCO0382(SCF62.08)
            TER: Tery_2263
STRUCTURES  PDB: 1MFZ  1MUU  1MV8  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.132
            ExPASy - ENZYME nomenclature database: 1.1.1.132
            ExplorEnz - The Enzyme Database: 1.1.1.132
            ERGO genome analysis and discovery system: 1.1.1.132
            BRENDA, the Enzyme Database: 1.1.1.132
            CAS: 37250-63-8
///
ENTRY       EC 1.1.1.133                Enzyme
NAME        dTDP-4-dehydrorhamnose reductase;
            dTDP-4-keto-L-rhamnose reductase;
            reductase, thymidine diphospho-4-ketorhamnose;
            dTDP-4-ketorhamnose reductase;
            TDP-4-keto-rhamnose reductase;
            thymidine diphospho-4-ketorhamnose reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     dTDP-6-deoxy-L-mannose:NADP+ 4-oxidoreductase
REACTION    dTDP-6-deoxy-L-mannose + NADP+ = dTDP-4-dehydro-6-deoxy-L-mannose +
            NADPH + H+ [RN:R02777]
ALL_REAC    R02777;
            (other) R04778
SUBSTRATE   dTDP-6-deoxy-L-mannose [CPD:C03319];
            NADP+ [CPD:C00006]
PRODUCT     dTDP-4-dehydro-6-deoxy-L-mannose [CPD:C00688];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     In the reverse direction, reduction on the 4-position of the hexose
            moiety takes place only while the substrate is bound to another
            enzyme that catalyses epimerization at C-3 and C-5; the complex has
            been referred to as dTDP-L-rhamnose synthase.
REFERENCE   1  [PMID:4384782]
  AUTHORS   Melo A, Glaser L.
  TITLE     The mechanism of 6-deoxyhexose synthesis. II. Conversion of
            deoxythymidine diphosphate 4-keto-6-deoxy-D-glucose to
            deoxythymidine diphosphate L-rhamnose.
  JOURNAL   J. Biol. Chem. 243 (1968) 1475-8.
  ORGANISM  Pseudomonas aeruginosa
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
            PATH: map00521  Streptomycin biosynthesis
            PATH: map00523  Polyketide sugar unit biosynthesis
ORTHOLOGY   KO: K00067  dTDP-4-dehydrorhamnose reductase
GENES       AFM: AFUA_5G02240
            ECO: b2040(rfbD)
            ECJ: JW2025(rfbD)
            ECI: UTI89_C2311(rfbD)
            ECV: APECO1_1130(rmlD)
            ECW: EcE24377A_2331(rfbD) EcE24377A_4099(mtlD)
            ECX: EcHS_A2180(rfbD) EcHS_A3807
            STY: STY2306(rfbD)
            STT: t0776(rfbD)
            SPT: SPA0770(rfbD)
            STM: STM2096(rfbD)
            SFL: SF2103(rfbD)
            SFX: S2226(rfbD)
            SFV: SFV_2097(rfbD)
            SBO: SBO_0867(rfbD)
            SDY: SDY_2205(rfbD)
            ECA: ECA1440(rfbD)
            ASU: Asuc_0830
            XFA: XF0258
            XFT: PD0211(rmlD)
            XCC: XCC0624(rmlD)
            XCB: XC_3610
            XCV: XCV3706(rmlD)
            XAC: XAC3582(rmlD)
            XOO: XOO0795(rmlD)
            XOM: XOO_0723(XOO0723)
            VVY: VV0302
            PAE: PA4069 PA5162(rmlD)
            PAU: PA14_11250 PA14_68190(rmlD)
            PAP: PSPA7_5901(rfbD)
            PPU: PP_0500 PP_1784(rmlD)
            PPF: Pput_3934
            PST: PSPTO_0677 PSPTO_1080(rfbD)
            PSB: Psyr_0925 Psyr_4476
            PSP: PSPPH_0968(rfbD) PSPPH_4520
            PFL: PFL_0302(rfbD) PFL_5105 PFL_5534
            PFO: Pfl_4057 Pfl_5031
            PEN: PSEEN0250(rmlD) PSEEN0574
            PMY: Pmen_4292
            PAR: Psyc_1213(rfbD)
            PCR: Pcryo_0627
            ACI: ACIAD0078(rmlD)
            SON: SO_1653(rfbD)
            SDN: Sden_2549 Sden_2661
            SFR: Sfri_2761 Sfri_2828
            SAZ: Sama_2239
            SBL: Sbal_1473 Sbal_2888
            SBM: Shew185_1468
            SLO: Shew_1403 Shew_3344 Shew_3705
            SPC: Sputcn32_2538 Sputcn32_3891
            SSE: Ssed_0106 Ssed_3011
            SPL: Spea_1437
            SHE: Shewmr4_2618
            SHM: Shewmr7_2685
            SHN: Shewana3_1381 Shewana3_2793
            SHW: Sputw3181_1465
            PAT: Patl_2129
            SDE: Sde_0997
            PIN: Ping_3463
            MAQ: Maqu_2630
            LPN: lpg0757
            LPF: lpl0794(rmlD)
            LPP: lpp0823(rmlD)
            MCA: MCA1285(rfbD)
            NOC: Noc_0776
            AEH: Mlg_2318
            HCH: HCH_01716 HCH_02410(rfbD)
            CSA: Csal_0454
            ABO: ABO_0911(rmlD)
            MMW: Mmwyl1_0840
            AHA: AHA_2907(rfbD)
            NME: NMB0756
            NMA: NMA0967(rfbD)
            NMC: NMC0708(rfbD)
            NGO: NGO0332
            CVI: CV_4011(rfbD)
            RSO: RSc0683(rfbD)
            REU: Reut_A0713
            REH: H16_A1850(rfbD) H16_A2908
            RME: Rmet_2734
            BMA: BMA1987(rfbD)
            BMV: BMASAVP1_A0926(rfbD)
            BML: BMA10299_A2756(rfbD)
            BMN: BMA10247_1849(rfbD)
            BXE: Bxe_A3802
            BVI: Bcep1808_0808 Bcep1808_3216
            BUR: Bcep18194_A3972 Bcep18194_C7602
            BCN: Bcen_0392 Bcen_5752 Bcen_6416
            BCH: Bcen2424_0874 Bcen2424_6116 Bcen2424_6651
            BAM: Bamb_0754 Bamb_3384
            BPS: BPSL2683(rmlD)
            BPM: BURPS1710b_3161(rfbD)
            BPL: BURPS1106A_3138(rfbD)
            BPD: BURPS668_3101(rfbD)
            BTE: BTH_I1472(rfbD)
            PNU: Pnuc_0254
            BPE: BP0108(rfbD)
            BPA: BPP0172(rfbD)
            BBR: BB0174(rfbD)
            RFR: Rfer_0714
            POL: Bpro_4021
            PNA: Pnap_3490
            AAV: Aave_4165
            AJS: Ajs_0538
            VEI: Veis_0697
            MPT: Mpe_A0627
            HAR: HEAR1146 HEAR1155(rfbD)
            MMS: mma_2250(rfbD1) mma_2259(rfbD2)
            NEU: NE1023(rfbD)
            NET: Neut_2401
            NMU: Nmul_A0265
            EBA: ebA2273(rmlD)
            AZO: azo1876
            DAR: Daro_1263 Daro_1741
            TBD: Tbd_1777
            MFA: Mfla_2011
            SUN: SUN_1715(rfbD)
            GSU: GSU2247 GSU2365(rfbD)
            GME: Gmet_2472
            GUR: Gura_3272
            PCA: Pcar_2594
            PPD: Ppro_2097
            DVU: DVU1363(rfbD)
            DVL: Dvul_1705
            DDE: Dde_2183
            LIP: LI1065(rfbD)
            DPS: DP2222
            MXA: MXAN_4612
            SAT: SYN_01394
            SFU: Sfum_2262
            RPR: RP332
            RTY: RT0322(rmlD)
            RCO: RC0456
            RFE: RF_0538
            RBE: RBE_0710
            RCM: A1E_03820
            MLO: mlr7553
            MES: Meso_2763
            SME: SMb21327(expA10)
            SMD: Smed_4724 Smed_4811
            ATU: Atu4616(rfbD)
            ATC: AGR_L_531
            RET: RHE_CH01513(rfbD)
            RLE: RL1624(rfbD)
            OAN: Oant_2718
            BRA: BRADO7026(rfbD)
            BBT: BBta_1072(rfbD)
            RPA: RPA0119(rmlD)
            RPB: RPB_1564
            RPC: RPC_4188
            RPD: RPD_0747 RPD_1573
            NWI: Nwi_0547
            NHA: Nham_1061 Nham_3053
            XAU: Xaut_3546 Xaut_3555
            CCR: CC_1140 CC_3615
            SIT: TM1040_3860
            RSP: RSP_3845(rmlD)
            RSH: Rsph17029_4077
            JAN: Jann_3842
            RDE: RD1_B0018(rfbD)
            PDE: Pden_2120
            MMR: Mmar10_2455
            HNE: HNE_0780(rfbD)
            NAR: Saro_3236
            SWI: Swit_4020
            GOX: GOX1050
            GBE: GbCGDNIH1_0105
            ACR: Acry_0611 Acry_1217
            RRU: Rru_A2734 Rru_B0049
            MAG: amb1473
            MGM: Mmc1_2124
            SUS: Acid_6309
            BSU: BG10619(spsK)
            BHA: BH3365(rfbD)
            BAN: BA1231(rfbD)
            BAR: GBAA1231(rfbD)
            BAA: BA_1766
            BAT: BAS1138
            BCE: BC1215
            BCA: BCE_1338(rfbD)
            BCZ: BCZK1112(rbfD)
            BTK: BT9727_1118(rbfD)
            BCL: ABC3688(spsK)
            BPU: BPUM_3427(spsK)
            OIH: OB1128
            LMO: lmo1084
            LLA: L320(rmlC)
            LLC: LACR_0205
            LLM: llmg_0210(rmlD)
            SPY: SPy_0784(rmlD)
            SPZ: M5005_Spy_0602(rmlD)
            SPM: spyM18_0843
            SPG: SpyM3_0521(rmlD)
            SPS: SPs1333
            SPH: MGAS10270_Spy0657(rmlD)
            SPI: MGAS10750_Spy0689(rmlD)
            SPJ: MGAS2096_Spy0666(rmlD)
            SPK: MGAS9429_Spy0656(rmlD)
            SPA: M6_Spy0619
            SPB: M28_Spy0581(rmlD)
            SPR: spr0323(cpsO)
            SPD: SPD_0331(rfbD)
            SAG: SAG1424(rfbD)
            SAN: gbs1494(rmlD)
            SAK: SAK_1459(rfbD)
            SMU: SMU.824
            STC: str1483(rmlD)
            STL: stu1483(rmlD)
            SSA: SSA_0858(rmlD)
            SGO: SGO_1020(rfbD)
            LPL: lp_1190(rfbD)
            LJO: LJ1052
            LSL: LSL_1569(rfbD)
            LDB: Ldb1974(rmlD)
            LBU: LBUL_1835
            LCA: LSEI_2012
            LRE: Lreu_1054
            EFA: EF2191
            OOE: OEOE_1445
            CAC: CAC2315 CA_P0122
            CPE: CPE0618(rfbD)
            CPF: CPF_0481(rfbD) CPF_0599(rfbD)
            CBE: Cbei_2579 Cbei_4752
            AMT: Amet_2451
            CHY: CHY_0978(rfbD)
            DRM: Dred_3036
            SWO: Swol_0727
            MTC: MT3366(strL)
            MBO: Mb3294c(rmlD)
            MLE: ML0751(rmlD)
            MPA: MAP3380c(rmlD)
            MAV: MAV_4231(rfbD)
            MSM: MSMEG_1825(rfbD)
            MVA: Mvan_1727
            MGI: Mflv_4736
            MMC: Mmcs_1319
            MKM: Mkms_1336
            MJL: Mjls_1355
            CGL: NCgl0326(cgl0333)
            CGB: cg0402(rmlCD)
            CEF: CE0343
            CDI: DIP0361
            CJK: jk1647(rmlD)
            NFA: nfa46380(rfbD)
            RHA: RHA1_ro06305(rfbD)
            TWH: TWT029(rmlD)
            TWS: TW032
            LXX: Lxx04900(strL) Lxx05090(rfbD)
            CMI: CMM_1009(rmlD)
            AAU: AAur_2164(rfbC) AAur_3161(rfbC)
            FRA: Francci3_0715
            FAL: FRAAL1230
            ACE: Acel_0416
            SEN: SACE_6479(rfbD)
            BLO: BL0228
            BAD: BAD_1508(rmlCD)
            RXY: Rxyl_3106
            FNU: FN1685 FN1698 FN1847
            PCU: pc0125(rfbD)
            LIL: LA1660(rmlD)
            LIC: LIC12125(rfbD)
            LBJ: LBJ_1182(rmlD)
            LBL: LBL_1236(rmlD)
            SYN: sll1395(rfbD)
            SYW: SYNW0647(rfbD)
            SYC: syc1994_c(rfbD)
            SYF: Synpcc7942_2099
            SYD: Syncc9605_2034
            SYE: Syncc9902_0635
            SYR: SynRCC307_0083(rfbD)
            SYX: SynWH7803_0104(rfbD)
            TEL: tlr0951(rfbD)
            GVI: glr3234(rfbD)
            ANA: alr4490(rfbD)
            AVA: Ava_3355 Ava_3653
            PMM: PMM1233(rfbD)
            PMT: PMT0114(rfbD)
            PMN: PMN2A_1234 PMN2A_1239
            PMF: P9303_00961(rfbD) P9303_23371(rfbD)
            PMH: P9215_14521(rfbD)
            PME: NATL1_08561(rfbD)
            TER: Tery_1344
            BTH: BT_1730
            BFR: BF1310
            BFS: BF1296(rmlD)
            PGI: PG1561(rfbD)
            SRU: SRU_0591(rfbD)
            CHU: CHU_0494(rfbD)
            GFO: GFO_1497 GFO_3286(rfbD)
            FJO: Fjoh_0332
            FPS: FP2478(rmlD)
            CTE: CT0307(rfbD)
            CCH: Cag_0515
            CPH: Cpha266_1996
            PVI: Cvib_0470
            PLT: Plut_0418
            RRS: RoseRS_1416
            RCA: Rcas_1699
            DRA: DR_A0044
            TME: Tmel_1071
            MMQ: MmarC5_1313
            MAE: Maeo_0381
            MAC: MA3778(rfbD)
            MBA: Mbar_A0232
            MMA: MM_1168
            MBU: Mbur_2231
            MTP: Mthe_0953
            MHU: Mhun_3073
            MEM: Memar_0187
            MBN: Mboo_1750
            MTH: MTH1792
            MST: Msp_1116
            MSI: Msm_1304
            AFU: AF0323a
            TVO: TVN0900
            PTO: PTO0308
            PAB: PAB0789
            RCI: LRC21(rfbD-2) RCIX199(rfbD-1)
            APE: APE_1179.1
            SSO: SSO0832(rfbD-1) SSO1783(rfbD-2) SSO2161(rfbD-3)
            STO: ST1970
            SAI: Saci_1705 Saci_2310
STRUCTURES  PDB: 1KBZ  1KC1  1KC3  1N2S  2GGS  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.133
            ExPASy - ENZYME nomenclature database: 1.1.1.133
            ExplorEnz - The Enzyme Database: 1.1.1.133
            ERGO genome analysis and discovery system: 1.1.1.133
            BRENDA, the Enzyme Database: 1.1.1.133
            CAS: 37250-64-9
///
ENTRY       EC 1.1.1.134                Enzyme
NAME        dTDP-6-deoxy-L-talose 4-dehydrogenase;
            thymidine diphospho-6-deoxy-L-talose dehydrogenase;
            TDP-6-deoxy-L-talose dehydrogenase;
            thymidine diphospho-6-deoxy-L-talose dehydrogenase;
            dTDP-6-deoxy-L-talose dehydrogenase (4-reductase)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     dTDP-6-deoxy-L-talose:NADP+ 4-oxidoreductase
REACTION    dTDP-6-deoxy-L-talose + NADP+ = dTDP-4-dehydro-6-deoxy-L-mannose +
            NADPH + H+ [RN:R02776]
ALL_REAC    R02776
SUBSTRATE   dTDP-6-deoxy-L-talose [CPD:C03187];
            NADP+ [CPD:C00006]
PRODUCT     dTDP-4-dehydro-6-deoxy-L-mannose [CPD:C00688];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Oxidation on the 4-position of the hexose moiety takes place only
            while the substrate is bound to another enzyme that catalyses
            epimerization at C-3 and C-5.
REFERENCE   1  [PMID:4199258]
  AUTHORS   Gaugler RW, Gabriel O.
  TITLE     Biological mechanisms involved in the formation of deoxy sugars.
            VII. Biosynthesis of 6-deoxy-L-talose.
  JOURNAL   J. Biol. Chem. 248 (1973) 6041-9.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.134
            ExPASy - ENZYME nomenclature database: 1.1.1.134
            ExplorEnz - The Enzyme Database: 1.1.1.134
            ERGO genome analysis and discovery system: 1.1.1.134
            BRENDA, the Enzyme Database: 1.1.1.134
            CAS: 37250-65-0
///
ENTRY       EC 1.1.1.135                Enzyme
NAME        GDP-6-deoxy-D-talose 4-dehydrogenase;
            guanosine diphospho-6-deoxy-D-talose dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     GDP-6-deoxy-D-talose:NAD(P)+ 4-oxidoreductase
REACTION    GDP-6-deoxy-D-talose + NAD(P)+ = GDP-4-dehydro-6-deoxy-D-mannose +
            NAD(P)H + H+ [RN:R03396 R03398]
ALL_REAC    R03396 R03398
SUBSTRATE   GDP-6-deoxy-D-talose [CPD:C02977];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     GDP-4-dehydro-6-deoxy-D-mannose [CPD:C01222];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Markovitz, A.
  TITLE     Biosynthesis of guanosine diphosphate D-rhamnose and guanosine
            diphosphate D-talomethylose from guanosine diphosphate
            alpha-D-mannose.
  JOURNAL   J. Biol. Chem. 239 (1964) 2091-2098.
PATHWAY     PATH: map00051  Fructose and mannose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.135
            ExPASy - ENZYME nomenclature database: 1.1.1.135
            ExplorEnz - The Enzyme Database: 1.1.1.135
            ERGO genome analysis and discovery system: 1.1.1.135
            BRENDA, the Enzyme Database: 1.1.1.135
            CAS: 37250-66-1
///
ENTRY       EC 1.1.1.136                Enzyme
NAME        UDP-N-acetylglucosamine 6-dehydrogenase;
            uridine diphosphoacetylglucosamine dehydrogenase;
            UDP-acetylglucosamine dehydrogenase;
            UDP-2-acetamido-2-deoxy-D-glucose:NAD oxidoreductase;
            UDP-GlcNAc dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     UDP-N-acetyl-D-glucosamine:NAD+ 6-oxidoreductase
REACTION    UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O =
            UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+
            [RN:R00421]
ALL_REAC    R00421
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate [CPD:C04573];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4312076]
  AUTHORS   Fan DF, John CE, Zalitis J, Feingold DS.
  TITLE     UDPacetylglucosamine dehydrogenase from Achromobacter
            georgiopolitanum.
  JOURNAL   Arch. Biochem. Biophys. 135 (1969) 45-9.
  ORGANISM  Achromobacter georgiopolitanum
PATHWAY     PATH: map00530  Aminosugars metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.136
            ExPASy - ENZYME nomenclature database: 1.1.1.136
            ExplorEnz - The Enzyme Database: 1.1.1.136
            ERGO genome analysis and discovery system: 1.1.1.136
            BRENDA, the Enzyme Database: 1.1.1.136
            CAS: 9054-83-5
///
ENTRY       EC 1.1.1.137                Enzyme
NAME        ribitol-5-phosphate 2-dehydrogenase;
            dehydrogenase, ribitol 5-phosphate
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-ribitol-5-phosphate:NAD(P)+ 2-oxidoreductase
REACTION    D-ribitol 5-phosphate + NAD(P)+ = D-ribulose 5-phosphate + NAD(P)H +
            H+ [RN:R01524 R01525]
ALL_REAC    R01524 R01525
SUBSTRATE   D-ribitol 5-phosphate [CPD:C01068];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     D-ribulose 5-phosphate [CPD:C00199];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13948358]
  AUTHORS   GLASER L.
  TITLE     Ribitol-5-phosphate dehydrogenase from Lactobacillus plantarum.
  JOURNAL   Biochim. Biophys. Acta. 67 (1963) 525-30.
  ORGANISM  Lactobacillus plantarum [GN:lpl]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K05352  ribitol-5-phosphate 2-dehydrogenase
GENES       LPL: lp_1817
            LSL: LSL_1953(tdh)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.137
            ExPASy - ENZYME nomenclature database: 1.1.1.137
            ExplorEnz - The Enzyme Database: 1.1.1.137
            ERGO genome analysis and discovery system: 1.1.1.137
            BRENDA, the Enzyme Database: 1.1.1.137
            CAS: 37250-67-2
///
ENTRY       EC 1.1.1.138                Enzyme
NAME        mannitol 2-dehydrogenase (NADP+);
            mannitol 2-dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-mannitol:NADP+ 2-oxidoreductase
REACTION    D-mannitol + NADP+ = D-fructose + NADPH + H+ [RN:R00870]
ALL_REAC    R00870
SUBSTRATE   D-mannitol [CPD:C00392];
            NADP+ [CPD:C00006]
PRODUCT     D-fructose [CPD:C00095];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:14109183]
  AUTHORS   EDMUNDOWICZ JM, WRISTON JC Jr.
  TITLE     MANNITOL DEHYDROGENASE FROM AGARICUS CAMPESTRIS.
  JOURNAL   J. Biol. Chem. 238 (1963) 3539-41.
  ORGANISM  Agaricus campestris
REFERENCE   2
  AUTHORS   Strobel, G.A. and Kosuge, T.
  TITLE     Polyol metabolism in Diplodia viticola Desm.
  JOURNAL   Arch. Biochem. Biophys. 109 (1965) 622-626.
  ORGANISM  Diplodia viticola
PATHWAY     PATH: map00051  Fructose and mannose metabolism
STRUCTURES  PDB: 1H5Q  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.138
            ExPASy - ENZYME nomenclature database: 1.1.1.138
            ExplorEnz - The Enzyme Database: 1.1.1.138
            ERGO genome analysis and discovery system: 1.1.1.138
            BRENDA, the Enzyme Database: 1.1.1.138
            CAS: 37250-68-3
///
ENTRY       EC 1.1.1.139      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: polyol dehydrogenase (NADP+). Now included with EC
            1.1.1.21 aldehyde reductase (EC 1.1.1.139 created 1972, deleted
            1978)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.139
            ExPASy - ENZYME nomenclature database: 1.1.1.139
            ExplorEnz - The Enzyme Database: 1.1.1.139
            ERGO genome analysis and discovery system: 1.1.1.139
            BRENDA, the Enzyme Database: 1.1.1.139
///
ENTRY       EC 1.1.1.140                Enzyme
NAME        sorbitol-6-phosphate 2-dehydrogenase;
            ketosephosphate reductase;
            ketosephosphate reductase;
            D-sorbitol 6-phosphate dehydrogenase;
            D-sorbitol-6-phosphate dehydrogenase;
            sorbitol-6-P-dehydrogenase;
            D-glucitol-6-phosphate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-sorbitol-6-phosphate:NAD+ 2-oxidoreductase
REACTION    D-sorbitol 6-phosphate + NAD+ = D-fructose 6-phosphate + NADH + H+
            [RN:R07133]
ALL_REAC    R07133 > R05607
SUBSTRATE   D-sorbitol 6-phosphate [CPD:C01096];
            NAD+ [CPD:C00003]
PRODUCT     D-fructose 6-phosphate [CPD:C00085];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4318899]
  AUTHORS   Du Toit PJ, Kotze JP.
  TITLE     The isolation and characterization of sorbitol-6-phosphate
            dehydrogenase from Clostridium pasteurianum.
  JOURNAL   Biochim. Biophys. Acta. 206 (1970) 333-42.
  ORGANISM  Clostridium pasteurianum
REFERENCE   2  [PMID:14465816]
  AUTHORS   LISS M, HORWITZ SB, KAPLAN NO.
  TITLE     D-Mannitol 1-phosphate dehydrogenase and D-sorbitol 6-phosphate
            dehydrogenase in Aerobacter aerogenes.
  JOURNAL   J. Biol. Chem. 237 (1962) 1342-50.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K00068  sorbitol-6-phosphate 2-dehydrogenase
GENES       ECO: b2705(srlD)
            ECJ: JW2674(srlD)
            ECE: Z4012(srlD) Z5618
            ECS: ECs3561 ECs5003
            ECC: c3259(srlD) c4986
            ECI: UTI89_C3067(srlD) UTI89_C4588
            ECP: ECP_2665 ECP_4238
            ECV: APECO1_2448 APECO1_3821(srlD)
            ECW: EcE24377A_2989(srlD)
            ECX: EcHS_A2841(srlD)
            STY: STY2956(srlD)
            STT: t2736(srlD)
            SPT: SPA2693(srlD)
            SEC: SC2768(srlD)
            STM: STM2835(srlD)
            YEN: YE1095(gutD)
            SFL: SF2728(srlD) SF4093
            SFX: S2919(srlD) S3637(sorD)
            SFV: SFV_2800(srlD) SFV_4098(sorD)
            SSN: SSON_4198(sorD)
            SBO: SBO_2813(srlD) SBO_4048(sorD)
            SDY: SDY_2902(srlD)
            HSO: HS_0676(srlD)
            PMU: PM1968
            CVI: CV_2258
            BLI: BL02488
            BLD: BLi03863
            BCL: ABC1160
            SMU: SMU.308
            LPL: lp_3623(srlD1) lp_3657(srlD2)
            LSL: LSL_1894
            LCA: LSEI_2729
            EFA: EF3310
            CDF: CD0768(gutD)
            CBO: CBO3413(gutD)
            CBA: CLB_3470(srlD)
            CBH: CLC_3358(srlD)
            CBF: CLI_3596(srlD)
            MMY: MSC_0020(srlD)
            MCP: MCAP_0029
            HMA: rrnAC0917(sorD)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.140
            ExPASy - ENZYME nomenclature database: 1.1.1.140
            ExplorEnz - The Enzyme Database: 1.1.1.140
            ERGO genome analysis and discovery system: 1.1.1.140
            BRENDA, the Enzyme Database: 1.1.1.140
            CAS: 37250-69-4
///
ENTRY       EC 1.1.1.141                Enzyme
NAME        15-hydroxyprostaglandin dehydrogenase (NAD+);
            NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type I);
            PGDH;
            11alpha,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase;
            15-OH-PGDH;
            15-hydroxyprostaglandin dehydrogenase;
            15-hydroxyprostanoic dehydrogenase;
            NAD+-specific 15-hydroxyprostaglandin dehydrogenase;
            prostaglandin dehydrogenase;
            15-hydroxyprostaglandin dehydrogenase (NAD+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate:NAD+
            15-oxidoreductase
REACTION    (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NAD+ =
            (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate + NADH + H+
            [RN:R02580]
ALL_REAC    R02580
SUBSTRATE   (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate
            [CPD:C00584];
            NAD+ [CPD:C00003]
PRODUCT     (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate [CPD:C04707];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Acts on prostaglandin E2, F2alpha and B1, but not on prostaglandin
            D2. cf. EC 1.1.1.196 15-hydroxyprostaglandin-D dehydrogenase (NADP+)
            and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+).
REFERENCE   1
  AUTHORS   Anggaard, E. and Samuelsson, B.
  TITLE     Purification and properties of a 15-hydroxyprostaglandin
            dehydrogenase from swine lung.
  JOURNAL   Prostaglandins 25 (1966) 293-300.
REFERENCE   2  [PMID:1117007]
  AUTHORS   Braithwaite SS, Jarabak J.
  TITLE     Studies on a 15-hydroxyprostaglandin dehydrogenase from human
            placenta. Purification and partial characterization.
  JOURNAL   J. Biol. Chem. 250 (1975) 2315-8.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:234431]
  AUTHORS   Lee SC, Levine L.
  TITLE     Prostaglandin metabolism. II. Identification of two
            15-hydroxyprostaglandin dehydrogenase types.
  JOURNAL   J. Biol. Chem. 250 (1975) 548-52.
  ORGANISM  monkey, chicken [GN:gga], dog [GN:cfa]
REFERENCE   4  [PMID:803247]
  AUTHORS   Lee SC, Pong SS, Katzen D, Wu KY, Levine L.
  TITLE     Distribution of prostaglandin E 9-KETOREDUCTASE AND TYPES I and II
            15-hydroxyprostaglandin dehydrogenase in swine kidney medulla and
            cortex.
  JOURNAL   Biochemistry. 14 (1975) 142-5.
  ORGANISM  pig [GN:ssc]
ORTHOLOGY   KO: K00069  15-hydroxyprostaglandin dehydrogenase (NAD)
GENES       HSA: 3248(HPGD)
            PTR: 461613(HPGD)
            MMU: 15446(Hpgd)
            RNO: 79242(Hpgd)
            CFA: 486073(HPGD)
            GGA: 422567(HPGD)
            XLA: 446811(hpgd)
            XTR: 493354(hpgd)
            DRE: 393297(zgc:56585)
            SPU: 591898(LOC591898)
            AFM: AFUA_3G09480
STRUCTURES  PDB: 2GDZ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.141
            ExPASy - ENZYME nomenclature database: 1.1.1.141
            ExplorEnz - The Enzyme Database: 1.1.1.141
            ERGO genome analysis and discovery system: 1.1.1.141
            BRENDA, the Enzyme Database: 1.1.1.141
            CAS: 9030-87-9
///
ENTRY       EC 1.1.1.142                Enzyme
NAME        D-pinitol dehydrogenase;
            5D-5-O-methyl-chiro-inositol:NADP+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     1D-3-O-methyl-chiro-inositol:NADP+ oxidoreductase
REACTION    1D-3-O-methyl-chiro-inositol + NADP+ =
            2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADPH + H+
            [RN:R03498]
ALL_REAC    R03498
SUBSTRATE   1D-3-O-methyl-chiro-inositol [CPD:C03844];
            NADP+ [CPD:C00006]
PRODUCT     2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone [CPD:C01295];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4389340]
  AUTHORS   Ruis H, Hoffmann-Ostenhof O.
  TITLE     Enzymic epimerization of sequoyitol to D-pinitol in Trifolium
            incarnatum.
  JOURNAL   Eur. J. Biochem. 7 (1969) 442-8.
  ORGANISM  Trifolium incarnatum
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.142
            ExPASy - ENZYME nomenclature database: 1.1.1.142
            ExplorEnz - The Enzyme Database: 1.1.1.142
            ERGO genome analysis and discovery system: 1.1.1.142
            BRENDA, the Enzyme Database: 1.1.1.142
            CAS: 37250-71-8
///
ENTRY       EC 1.1.1.143                Enzyme
NAME        sequoyitol dehydrogenase;
            D-pinitol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     5-O-methyl-myo-inositol:NAD+ oxidoreductase
REACTION    5-O-methyl-myo-inositol + NAD+ =
            2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADH + H+
            [RN:R03497]
ALL_REAC    R03497
SUBSTRATE   5-O-methyl-myo-inositol [CPD:C03365];
            NAD+ [CPD:C00003]
PRODUCT     2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone [CPD:C01295];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4389340]
  AUTHORS   Ruis H, Hoffmann-Ostenhof O.
  TITLE     Enzymic epimerization of sequoyitol to D-pinitol in Trifolium
            incarnatum.
  JOURNAL   Eur. J. Biochem. 7 (1969) 442-8.
  ORGANISM  Trifolium incarnatum
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.143
            ExPASy - ENZYME nomenclature database: 1.1.1.143
            ExplorEnz - The Enzyme Database: 1.1.1.143
            ERGO genome analysis and discovery system: 1.1.1.143
            BRENDA, the Enzyme Database: 1.1.1.143
            CAS: 37250-72-9
///
ENTRY       EC 1.1.1.144                Enzyme
NAME        perillyl-alcohol dehydrogenase;
            perillyl alcohol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     perillyl-alcohol:NAD+ oxidoreductase
REACTION    perillyl alcohol + NAD+ = perillyl aldehyde + NADH + H+ [RN:R03945]
ALL_REAC    R03945
SUBSTRATE   perillyl alcohol [CPD:C02452];
            NAD+ [CPD:C00003]
PRODUCT     perillyl aldehyde [CPD:C02576];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Oxidizes a number of primary alcohols with the alcohol group allylic
            to an endocyclic double bond and a 6-membered ring, either aromatic
            or hydroaromatic.
REFERENCE   1  [PMID:4289759]
  AUTHORS   Ballal NR, Bhattacharyya PK, Rangachari PN.
  TITLE     Perillyl alcohol dehydrogenase from a soil pseudomonad.
  JOURNAL   Biochem. Biophys. Res. Commun. 23 (1966) 473-8.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00903  Limonene and pinene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.144
            ExPASy - ENZYME nomenclature database: 1.1.1.144
            ExplorEnz - The Enzyme Database: 1.1.1.144
            ERGO genome analysis and discovery system: 1.1.1.144
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.144
            BRENDA, the Enzyme Database: 1.1.1.144
            CAS: 37250-73-0
///
ENTRY       EC 1.1.1.145                Enzyme
NAME        3beta-hydroxy-Delta5-steroid dehydrogenase;
            progesterone reductase;
            Delta5-3beta-hydroxysteroid dehydrogenase;
            3beta-hydroxy-5-ene steroid dehydrogenase;
            3beta-hydroxy steroid dehydrogenase/isomerase;
            3beta-hydroxy-Delta5-C27-steroid dehydrogenase/isomerase;
            3beta-hydroxy-Delta5-C27-steroid oxidoreductase;
            3beta-hydroxy-5-ene-steroid oxidoreductase;
            steroid-Delta5-3beta-ol dehydrogenase;
            3beta-HSDH;
            5-ene-3-beta-hydroxysteroid dehydrogenase;
            3beta-hydroxy-5-ene-steroid dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3beta-hydroxy-Delta5-steroid:NAD+ 3-oxidoreductase
REACTION    a 3beta-hydroxy-Delta5-steroid + NAD+ = a 3-oxo-Delta5-steroid +
            NADH + H+ [RN:R03176]
ALL_REAC    R03176;
            (other) R01837 R01839 R02216 R02217 R02499 R02500 R02840 R02842
            R03327 R03328 R04163 R04164 R04678 R04680 R04849 R04851 R07428
SUBSTRATE   3beta-hydroxy-Delta5-steroid [CPD:C03836];
            NAD+ [CPD:C00003]
PRODUCT     3-oxo-Delta5-steroid [CPD:C01034];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Acts on 3beta-hydroxyandrost-5-en-17-one to form
            androst-4-ene-3,17-dione and on 3beta-hydroxypregn-5-en-20-one to
            form progesterone.
REFERENCE   1  [PMID:4226148]
  AUTHORS   Cheatum SG, Watten JC.
  TITLE     Purification and properties of 3-beta-hydroxysteroid dehydrogenase
            and delta-5-3-ketosteroid isomerase from bovine corpora lutea.
  JOURNAL   Biochim. Biophys. Acta. 122 (1966) 1-13.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   Koritz, S.B.
  TITLE     The conversion of prepnenolone to progesterone by small particle
            from rat adrenal.
  JOURNAL   Biochemistry 3 (1964) 1098-1102.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Neville, A.M., Orr, J.C. and Engel, L.L.
  TITLE     Delta5-3beta-Hydroxy steroid dehydrogenase activities of bovine
            adrenal cortex.
  JOURNAL   Biochem. J. 107 (1968) 20.
PATHWAY     PATH: map00140  C21-Steroid hormone metabolism
            PATH: map00150  Androgen and estrogen metabolism
ORTHOLOGY   KO: K00070  3beta-hydroxy-delta5-steroid dehydrogenase
GENES       HSA: 3283(HSD3B1) 3284(HSD3B2)
            MMU: 15492(Hsd3b1) 15493(Hsd3b2) 15495(Hsd3b4) 15496(Hsd3b5)
                 15497(Hsd3b6)
            RNO: 24470(Hsd3b) 29632(Hsd3b6)
            CFA: 483146(HSD3B1)
            BTA: 281824(HSD3B)
            SSC: 445539(3B-HSD)
            GGA: 396015(HSD3B1)
            DRE: 373131(hsd3b1)
            RRU: Rru_A0016
            RBA: RB993
            AVA: Ava_2585
            CCH: Cag_0225
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.145
            ExPASy - ENZYME nomenclature database: 1.1.1.145
            ExplorEnz - The Enzyme Database: 1.1.1.145
            ERGO genome analysis and discovery system: 1.1.1.145
            BRENDA, the Enzyme Database: 1.1.1.145
            CAS: 9044-85-3
///
ENTRY       EC 1.1.1.146                Enzyme
NAME        11beta-hydroxysteroid dehydrogenase;
            corticosteroid 11beta-dehydrogenase;
            beta-hydroxysteroid dehydrogenase;
            11beta-hydroxy steroid dehydrogenase;
            corticosteroid 11-reductase;
            dehydrogenase, 11beta-hydroxy steroid
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     11beta-hydroxysteroid:NADP+ 11-oxidoreductase
REACTION    an 11beta-hydroxysteroid + NADP+ = an 11-oxosteroid + NADPH + H+
            [RN:R03203]
ALL_REAC    R03203 > R02836 R03848 R04758 R04840;
            (other) R02834 R03847 R04757 R04839
SUBSTRATE   11beta-hydroxysteroid [CPD:C01058];
            NADP+ [CPD:C00006]
PRODUCT     11-oxosteroid [CPD:C01985];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:2808402]
  AUTHORS   Agarwal AK, Monder C, Eckstein B, White PC.
  TITLE     Cloning and expression of rat cDNA encoding corticosteroid 11
            beta-dehydrogenase.
  JOURNAL   J. Biol. Chem. 264 (1989) 18939-43.
  ORGANISM  rat [GN:rno], human [GN:hsa]
REFERENCE   2  [PMID:4384445]
  AUTHORS   Bush IE, Hunter SA, Meigs RA.
  TITLE     Metabolism of 11-oxygenated steroids. Metabolism in vitro by
            preparations of liver.
  JOURNAL   Biochem. J. 107 (1968) 239-58.
  ORGANISM  rat [GN:rno], guinea pig, rabbit, cow [GN:bta]
REFERENCE   3  [PMID:3139396]
  AUTHORS   Lakshmi V, Monder C.
  TITLE     Purification and characterization of the corticosteroid 11
            beta-dehydrogenase component of the rat liver 11 beta-hydroxysteroid
            dehydrogenase complex.
  JOURNAL   Endocrinology. 123 (1988) 2390-8.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:2661206]
  AUTHORS   Phillips DM, Lakshmi V, Monder C.
  TITLE     Corticosteroid 11 beta-dehydrogenase in rat testis.
  JOURNAL   Endocrinology. 125 (1989) 209-16.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00140  C21-Steroid hormone metabolism
            PATH: map00150  Androgen and estrogen metabolism
ORTHOLOGY   KO: K00071  11beta-hydroxysteroid dehydrogenase
GENES       HSA: 3290(HSD11B1) 3291(HSD11B2)
            PTR: 468001(HSD11B2)
            MMU: 15483(Hsd11b1) 15484(Hsd11b2)
            RNO: 25116(Hsd11b1) 25117(Hsd11b2)
            CFA: 449023(HSD11B1) 489758(HSD11B2)
            BTA: 282434(HSD11B2) 282589(HSD11B1)
            SSC: 396948(HSD11B2) 397480(HSD11B1)
            GGA: 419861(HSD11B1)
            XLA: 379494(MGC64530) 379497(MGC64545)
            DRE: 393293(hsd11b3)
            SPU: 764876(LOC764876)
            ATH: AT3G47350
            TTH: TTC1745
STRUCTURES  PDB: 1XSE  1XU7  1XU9  1Y5M  1Y5R  2BEL  2ILT  2IRW  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.146
            ExPASy - ENZYME nomenclature database: 1.1.1.146
            ExplorEnz - The Enzyme Database: 1.1.1.146
            ERGO genome analysis and discovery system: 1.1.1.146
            BRENDA, the Enzyme Database: 1.1.1.146
            CAS: 9041-46-7
///
ENTRY       EC 1.1.1.147                Enzyme
NAME        16alpha-hydroxysteroid dehydrogenase;
            16alpha-hydroxy steroid dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     16alpha-hydroxysteroid:NAD(P)+ 16-oxidoreductase
REACTION    a 16alpha-hydroxysteroid + NAD(P)+ = a 16-oxosteroid + NAD(P)H + H+
            [RN:R03226 R03227]
ALL_REAC    R03226 R03227
SUBSTRATE   16alpha-hydroxysteroid [CPD:C01090];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     16-oxosteroid [CPD:C01986];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4380686]
  AUTHORS   Meigs RA, Ryan KJ.
  TITLE     16-alpha-hydroxysteroid dehydrogenase of rat kidney. Purification,
            assay, and properties.
  JOURNAL   J. Biol. Chem. 241 (1966) 4011-5.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.147
            ExPASy - ENZYME nomenclature database: 1.1.1.147
            ExplorEnz - The Enzyme Database: 1.1.1.147
            ERGO genome analysis and discovery system: 1.1.1.147
            BRENDA, the Enzyme Database: 1.1.1.147
            CAS: 37250-74-1
///
ENTRY       EC 1.1.1.148                Enzyme
NAME        estradiol 17alpha-dehydrogenase;
            17alpha-estradiol dehydrogenase;
            17alpha-hydroxy steroid dehydrogenase;
            17alpha-hydroxy steroid oxidoreductase;
            17alpha-hydroxysteroid oxidoreductase;
            estradiol 17alpha-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     17alpha-hydroxysteroid:NAD(P)+ 17-oxidoreductase
REACTION    estradiol-17alpha + NAD(P)+ = estrone + NAD(P)H + H+ [RN:R02347
            R02349]
ALL_REAC    R02347 R02349
SUBSTRATE   estradiol-17alpha [CPD:C02537];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     estrone [CPD:C00468];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4383682]
  AUTHORS   Renwick AG, Engel LL.
  TITLE     The partial purification of 17 alpha- and 17 beta-estradiol
            dehydrogenase activities from chicken liver.
  JOURNAL   Biochim. Biophys. Acta. 146 (1967) 336-48.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00150  Androgen and estrogen metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.148
            ExPASy - ENZYME nomenclature database: 1.1.1.148
            ExplorEnz - The Enzyme Database: 1.1.1.148
            ERGO genome analysis and discovery system: 1.1.1.148
            BRENDA, the Enzyme Database: 1.1.1.148
            CAS: 9044-91-1
///
ENTRY       EC 1.1.1.149                Enzyme
NAME        20alpha-hydroxysteroid dehydrogenase;
            20alpha-hydroxy steroid dehydrogenase;
            20alpha-hydroxy steroid dehydrogenase;
            20alpha-HSD;
            20alpha-HSDH
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     20alpha-hydroxysteroid:NAD(P)+ 20-oxidoreductase
REACTION    17alpha,20alpha-dihydroxypregn-4-en-3-one + NAD(P)+ =
            17alpha-hydroxyprogesterone + NAD(P)H + H+ [RN:R03324 R03325]
ALL_REAC    R03324 R03325;
            (other) R02207 R02209
SUBSTRATE   17alpha,20alpha-dihydroxypregn-4-en-3-one [CPD:C04518];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     17alpha-hydroxyprogesterone [CPD:C01176];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     A-specific with respect to NAD(P)+ (cf. EC 1.1.1.62 estradiol
            17beta-dehydrogenase).
REFERENCE   1  [PMID:4382486]
  AUTHORS   Shikita M, Inano H, Tamaoki B.
  TITLE     Further studies on 20-alpha-hydroxysteroid dehydrogenase of rat
            testes.
  JOURNAL   Biochemistry. 6 (1967) 1760-4.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6935192]
  AUTHORS   Strickler RC, Tobias B, Covey DF.
  TITLE     Human placental 17 beta-estradiol dehydrogenase and 20
            alpha-hydroxysteroid dehydrogenase. Two activities at a single
            enzyme active site.
  JOURNAL   J. Biol. Chem. 256 (1981) 316-21.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00140  C21-Steroid hormone metabolism
ORTHOLOGY   KO: K05295  20alpha-hydroxysteroid dehydrogenase
GENES       MMU: 105349(Akr1c18)
            RNO: 171516(Akr1c18)
            TBD: Tbd_2122
STRUCTURES  PDB: 1MRQ  1Q13  1Q5M  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.149
            ExPASy - ENZYME nomenclature database: 1.1.1.149
            ExplorEnz - The Enzyme Database: 1.1.1.149
            ERGO genome analysis and discovery system: 1.1.1.149
            BRENDA, the Enzyme Database: 1.1.1.149
            CAS: 9040-08-8
///
ENTRY       EC 1.1.1.150                Enzyme
NAME        21-hydroxysteroid dehydrogenase (NAD+);
            21-hydroxysteroid dehydrogenase (NAD+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     21-hydroxysteroid:NAD+ 21-oxidoreductase
REACTION    pregnan-21-ol + NAD+ = pregnan-21-al + NADH + H+ [RN:R03043]
ALL_REAC    R03043
SUBSTRATE   pregnan-21-ol [CPD:C00892];
            NAD+ [CPD:C00003]
PRODUCT     pregnan-21-al [CPD:C00891];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Acts on a number of 21-hydroxycorticosteroids.
REFERENCE   1  [PMID:14253469]
  AUTHORS   MONDER C, WHITE A.
  TITLE     THE 21-HYDROXYSTEROID DEHYDROGENASES OF LIVER. A NICOTINAMIDE
            ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE AND TWO NICOTINAMIDE
            ADENINE DINUCLEOTIDE DEHYDROGENASES.
  JOURNAL   J. Biol. Chem. 240 (1965) 71-7.
  ORGANISM  sheep
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.150
            ExPASy - ENZYME nomenclature database: 1.1.1.150
            ExplorEnz - The Enzyme Database: 1.1.1.150
            ERGO genome analysis and discovery system: 1.1.1.150
            BRENDA, the Enzyme Database: 1.1.1.150
            CAS: 37250-75-2
///
ENTRY       EC 1.1.1.151                Enzyme
NAME        21-hydroxysteroid dehydrogenase (NADP+);
            21-hydroxy steroid dehydrogenase;
            21-hydroxy steroid (nicotinamide adenine dinucleotide phosphate)
            dehydrogenase;
            21-hydroxy steroid dehydrogenase (nicotinamide adenine dinucleotide
            phosphate);
            NADP+-21-hydroxysteroid dehydrogenase;
            21-hydroxysteroid dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     21-hydroxysteroid:NADP+ 21-oxidoreductase
REACTION    pregnan-21-ol + NADP+ = pregnan-21-al + NADPH + H+ [RN:R03044]
ALL_REAC    R03044
SUBSTRATE   pregnan-21-ol [CPD:C00892];
            NADP+ [CPD:C00006]
PRODUCT     pregnan-21-al [CPD:C00891];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Acts on a number of 21-hydroxycorticosteroids.
REFERENCE   1  [PMID:14253469]
  AUTHORS   MONDER C, WHITE A.
  TITLE     THE 21-HYDROXYSTEROID DEHYDROGENASES OF LIVER. A NICOTINAMIDE
            ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE AND TWO NICOTINAMIDE
            ADENINE DINUCLEOTIDE DEHYDROGENASES.
  JOURNAL   J. Biol. Chem. 240 (1965) 71-7.
  ORGANISM  sheep
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.151
            ExPASy - ENZYME nomenclature database: 1.1.1.151
            ExplorEnz - The Enzyme Database: 1.1.1.151
            ERGO genome analysis and discovery system: 1.1.1.151
            BRENDA, the Enzyme Database: 1.1.1.151
            CAS: 37250-76-3
///
ENTRY       EC 1.1.1.152                Enzyme
NAME        3alpha-hydroxy-5beta-androstane-17-one 3alpha-dehydrogenase;
            etiocholanolone 3alpha-dehydrogenase;
            etiocholanolone 3alpha-dehydrogenase;
            3alpha-hydroxy-5beta-steroid dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3alpha-hydroxy-5beta-steroid:NAD+ 3-oxidoreductase
REACTION    3alpha-hydroxy-5beta-androstane-17-one + NAD+ =
            5beta-androstane-3,17-dione + NADH + H+ [RN:R04309]
ALL_REAC    R04309
SUBSTRATE   3alpha-hydroxy-5beta-androstane-17-one;
            NAD+ [CPD:C00003]
PRODUCT     5beta-androstane-3,17-dione [CPD:C03772];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:5365796]
  AUTHORS   Roe CR, Kaplan NO.
  TITLE     Purification and substrate specificities of bacterial hydroxysteroid
            dehydrogenases.
  JOURNAL   Biochemistry. 8 (1969) 5093-103.
  ORGANISM  Pseudomonas testosteroni
PATHWAY     PATH: map00150  Androgen and estrogen metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.152
            ExPASy - ENZYME nomenclature database: 1.1.1.152
            ExplorEnz - The Enzyme Database: 1.1.1.152
            ERGO genome analysis and discovery system: 1.1.1.152
            BRENDA, the Enzyme Database: 1.1.1.152
            CAS: 37250-77-4
///
ENTRY       EC 1.1.1.153                Enzyme
NAME        sepiapterin reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     7,8-dihydrobiopterin:NADP+ oxidoreductase
REACTION    7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH + H+ [RN:R02975]
ALL_REAC    R02975;
            (other) R01813 R04285
SUBSTRATE   7,8-dihydrobiopterin [CPD:C02953];
            NADP+ [CPD:C00006]
PRODUCT     sepiapterin [CPD:C00835];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Katoh, S.
  TITLE     Sepiapterin reductase from horse liver: purification and properties
            of the enzyme.
  JOURNAL   Arch. Biochem. Biophys. 146 (1971) 202-214.
  ORGANISM  horse, rat [GN:rno]
REFERENCE   2  [PMID:5969298]
  AUTHORS   Matsubara M, Katoh S, Akino M, Kaufman S.
  TITLE     Sepiapterin reductase.
  JOURNAL   Biochim. Biophys. Acta. 122 (1966) 202-12.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K00072  sepiapterin reductase
GENES       HSA: 6697(SPR)
            MMU: 20751(Spr)
            RNO: 29270(Spr)
            GGA: 425255(SPR)
            XLA: 380273(spr)
            SPU: 577750(LOC577750)
            DME: Dmel_CG12117(Sptr) Dmel_CG1474(Es2)
            DDI: DDB_0191275(sprA)
            DNO: DNO_0923
            BUR: Bcep18194_B0080
            BPM: BURPS1710b_A1673
            SYN: sll0330
            ANA: all0968(fabG)
STRUCTURES  PDB: 1NAS  1OAA  1SEP  1Z6Z  2BD0  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.153
            ExPASy - ENZYME nomenclature database: 1.1.1.153
            ExplorEnz - The Enzyme Database: 1.1.1.153
            ERGO genome analysis and discovery system: 1.1.1.153
            BRENDA, the Enzyme Database: 1.1.1.153
            CAS: 9059-48-7
///
ENTRY       EC 1.1.1.154                Enzyme
NAME        ureidoglycolate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-ureidoglycolate:NAD(P)+ oxidoreductase
REACTION    (S)-ureidoglycolate + NAD(P)+ = oxalureate + NAD(P)H + H+ [RN:R02935
            R02936]
ALL_REAC    R02935 R02936
SUBSTRATE   (S)-ureidoglycolate [CPD:C00603];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     oxalureate [CPD:C00802];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4399430]
  AUTHORS   van der Drift C, van Helvoort PE, Vogels GD.
  TITLE     S-ureidoglycolate dehydrogenase: purification and properties.
  JOURNAL   Arch. Biochem. Biophys. 145 (1971) 465-9.
  ORGANISM  Arthrobacter allantoicus
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K00073  ureidoglycolate dehydrogenase
GENES       AFM: AFUA_2G13800
            ECO: b0517(allD)
            ECJ: JW0505(allD)
            ECE: Z0672(ylbC)
            ECS: ECs0579
            ECC: c0631 c3753
            ECI: UTI89_C0545(allD) UTI89_C3439
            ECV: APECO1_1498(allD) APECO1_3406
            ECW: EcE24377A_0555(allD)
            ECX: EcHS_A0591
            STY: STY0576(allD)
            STT: t2333(allD)
            SPT: SPA2195(allD)
            SEC: SC0567(allD)
            STM: STM0528(allD)
            BLI: BL01097 BL01098
            BLD: BLi01129 BLi01130(yjmC)
            BCL: ABC4048
            EFA: EF0388(allD)
STRUCTURES  PDB: 1WTJ  1XRH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.154
            ExPASy - ENZYME nomenclature database: 1.1.1.154
            ExplorEnz - The Enzyme Database: 1.1.1.154
            ERGO genome analysis and discovery system: 1.1.1.154
            BRENDA, the Enzyme Database: 1.1.1.154
            CAS: 62213-62-1
///
ENTRY       EC 1.1.1.155      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: the enzyme is identical to EC 1.1.1.87,
            homoisocitrate dehydrogenase (EC 1.1.1.155 created 1976, deleted
            2004)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.155
            ExPASy - ENZYME nomenclature database: 1.1.1.155
            ExplorEnz - The Enzyme Database: 1.1.1.155
            ERGO genome analysis and discovery system: 1.1.1.155
            BRENDA, the Enzyme Database: 1.1.1.155
///
ENTRY       EC 1.1.1.156                Enzyme
NAME        glycerol 2-dehydrogenase (NADP+);
            dihydroxyacetone reductase;
            dihydroxyacetone (reduced nicotinamide adenine dinucleotide
            phosphate) reductase;
            dihydroxyacetone reductase (NADPH);
            DHA oxidoreductase;
            glycerol 2-dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     glycerol:NADP+ 2-oxidoreductase (glycerone-forming)
REACTION    glycerol + NADP+ = glycerone + NADPH + H+ [RN:R01039]
ALL_REAC    R01039
SUBSTRATE   glycerol [CPD:C00116];
            NADP+ [CPD:C00006]
PRODUCT     glycerone [CPD:C00184];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4146296]
  AUTHORS   Ben-Amotz A, Avron M.
  TITLE     NADP specific dihydroxyacetone reductase from Dunaliella parva.
  JOURNAL   FEBS. Lett. 29 (1973) 153-5.
  ORGANISM  Dunaliella parva
PATHWAY     PATH: map00561  Glycerolipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.156
            ExPASy - ENZYME nomenclature database: 1.1.1.156
            ExplorEnz - The Enzyme Database: 1.1.1.156
            ERGO genome analysis and discovery system: 1.1.1.156
            BRENDA, the Enzyme Database: 1.1.1.156
            CAS: 39342-20-6
///
ENTRY       EC 1.1.1.157                Enzyme
NAME        3-hydroxybutyryl-CoA dehydrogenase;
            beta-hydroxybutyryl coenzyme A dehydrogenase;
            L(+)-3-hydroxybutyryl-CoA dehydrogenase;
            BHBD;
            dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide adenine
            dinucleotide phosphate);
            L-(+)-3-hydroxybutyryl-CoA dehydrogenase;
            beta-hydroxybutyryl-CoA dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-3-hydroxybutanoyl-CoA:NADP+ oxidoreductase
REACTION    (S)-3-hydroxybutanoyl-CoA + NADP+ = 3-acetoacetyl-CoA + NADPH + H+
            [RN:R01976]
ALL_REAC    R01976;
            (other) R05576
SUBSTRATE   (S)-3-hydroxybutanoyl-CoA [CPD:C01144];
            NADP+ [CPD:C00006]
PRODUCT     3-acetoacetyl-CoA [CPD:C00332];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4405720]
  AUTHORS   Madan VK, Hillmer P, Gottschalk G.
  TITLE     Purification and properties of NADP-dependent
            L(+)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri.
  JOURNAL   Eur. J. Biochem. 32 (1973) 51-6.
  ORGANISM  Clostridium kluyveri
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
            PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K00074  3-hydroxybutyryl-CoA dehydrogenase
GENES       ATH: AT3G15290
            OSA: 4325632
            CME: CMC137C
            ANI: AN7008.2
            AFM: AFUA_4G04410
            AOR: AO090206000053
            CNE: CNG04300
            UMA: UM02105.1
            DDI: DDBDRAFT_0205217
            TET: TTHERM_00666640
            LMA: LmjF36.1140
            ECO: b1395(paaH)
            ECJ: JW1390(paaH)
            ECC: c2467(bhbD)
            ECI: UTI89_C2220
            ECP: ECP_1977
            SPE: Spro_1832 Spro_3079
            PAE: PA1628 PA3590
            PAU: PA14_43460(paaH)
            PPU: PP_3282(paaC) PP_3755(paaH)
            PPF: Pput_2008 Pput_2477
            PFL: PFL_2166(hbd-7)
            PEN: PSEEN2793(paaC) PSEEN3198(paaH)
            PAR: Psyc_1170(paaH)
            PCR: Pcryo_1235
            ACI: ACIAD1690(dcaH)
            PHA: PSHAa0399(bhbD)
            PIN: Ping_0657
            LPN: lpg1942
            LPF: lpl1912
            LPP: lpp1923
            HCH: HCH_02185(fadB) HCH_03438
            MMW: Mmwyl1_3099
            CVI: CV_2086(paaH)
            RSO: RSc0244(paaH1) RSc2013(paaH2)
            REU: Reut_A0255 Reut_A1010 Reut_C6280 Reut_C6369
            RME: Rmet_0212 Rmet_0974
            BXE: Bxe_A3184 Bxe_B0376 Bxe_B2944 Bxe_C0277 Bxe_C0331 Bxe_C0596
                 Bxe_C0888 Bxe_C1031
            BVI: Bcep1808_5069 Bcep1808_5645
            BUR: Bcep18194_A4407 Bcep18194_B0613 Bcep18194_B1317
                 Bcep18194_B1395 Bcep18194_B2488 Bcep18194_C6875
                 Bcep18194_C7698
            BCN: Bcen_1552 Bcen_3317 Bcen_3838 Bcen_4736
            BCH: Bcen2424_3627 Bcen2424_4530 Bcen2424_5050 Bcen2424_6277
            BAM: Bamb_3960 Bamb_5770
            BTE: BTH_II0337
            PNU: Pnuc_0750
            BPE: BP0217 BP3310(paaH)
            BPA: BPP0416 BPP1372 BPP2104 BPP2341 BPP4112(paaH)
            BBR: BB0418 BB1500 BB1792 BB2438 BB4583(paaH)
            RFR: Rfer_0224 Rfer_2272
            POL: Bpro_1632 Bpro_2957
            PNA: Pnap_1915 Pnap_2940
            AAV: Aave_3073 Aave_4261
            AJS: Ajs_1781 Ajs_3718
            MPT: Mpe_A0880 Mpe_A0900 Mpe_B0547
            HAR: HEAR2837(yusL)
            EBA: c2A173 ebA2315 ebA3543(paaH) ebA4742(hbdA) p2A392(ditN)
                 p2A408(had)
            AZO: azo0301(paaH1) azo1028(hbdA) azo3040(paaH2)
            DAR: Daro_0372(paaC) Daro_1549
            GME: Gmet_1717 Gmet_2072 Gmet_2203 Gmet_2269
            GUR: Gura_3042
            PCA: Pcar_0349
            BBA: Bd1850
            ADE: Adeh_1667
            AFW: Anae109_2134
            MXA: MXAN_2179 MXAN_3800(mmgB)
            SAT: SYN_01310
            SFU: Sfum_3583
            MLO: mlr3490 mlr6793
            MES: Meso_3035
            PLA: Plav_1606
            SME: SMc00727(hbdA)
            SMD: Smed_2534
            ATU: Atu3597(hbdA)
            ATC: AGR_L_2460(bhbD)
            RET: RHE_CH03794(hbdA)
            RLE: RL4321(hbdA)
            BME: BMEI0099 BMEII0215 BMEII1020
            BMF: BAB1_1970 BAB2_0216 BAB2_1045
            BMS: BR1969(hbd) BRA0223 BRA1086
            BMB: BruAb1_1945(hbd) BruAb2_1026
            BOV: BOV_1894(hbd)
            OAN: Oant_1013
            BJA: bll6223(hbdA) blr1379(hbdA) blr6087
            BRA: BRADO3444(hbdA) BRADO6490(hbdA)
            BBT: BBta_1142(hbdA) BBta_4257(hbdA)
            RPA: RPA4748(hbdA)
            RPB: RPB_0821
            RPC: RPC_4878
            RPD: RPD_0932
            RPE: RPE_4847
            NWI: Nwi_0755
            NHA: Nham_3479
            XAU: Xaut_2157
            CCR: CC_0715
            SIL: SPO0717(bhbD) SPO1467
            SIT: TM1040_2424
            RSP: RSP_1687(hbdA)
            RSH: Rsph17029_0321 Rsph17029_3650
            RSQ: Rsph17025_2559
            JAN: Jann_0543
            RDE: RD1_1385(bhbD)
            PDE: Pden_0197 Pden_2552 Pden_5086
            HNE: HNE_3469
            NAR: Saro_0554
            SAL: Sala_3089
            SWI: Swit_0750 Swit_2898
            ELI: ELI_14180
            GBE: GbCGDNIH1_2092
            ACR: Acry_0146
            RRU: Rru_A3079
            MAG: amb2596 amb3902
            ABA: Acid345_1212 Acid345_2761 Acid345_4328
            SUS: Acid_1104
            BSU: BG11320(mmgB)
            BHA: BH0204(hbd) BH1995 BH3800(mmgB)
            BAN: BA5588
            BAR: GBAA5588
            BAA: BA_0444
            BAT: BAS5192
            BCE: BC5343
            BCA: BCE_5474
            BCZ: BCZK5043(hbd) pE33L466_0384(hbd)
            BCY: Bcer98_3864
            BTL: BALH_4842(hbd)
            BLI: BL03926(mmgB)
            BLD: BLi03967(mmgB)
            BCL: ABC3890(mmgB)
            BAY: RBAM_022440
            BPU: BPUM_0632 BPUM_3372
            OIH: OB3012
            GKA: GK1319 GK2036 GK3395
            LSL: LSL_0136
            STH: STH214 STH2584 STH2912
            CAC: CAC2708(hbd)
            CPE: CPE2297
            CPF: CPF_2581(hbd)
            CPR: CPR_2283(hbd)
            CTC: CTC02423
            CNO: NT01CX_0470(bhbD) NT01CX_0604(bhbD)
            CDF: CD1058(hbd)
            CBO: CBO3201(hbd)
            CBA: CLB_3237(hbd)
            CBH: CLC_3111(hbd)
            CBF: CLI_3340(hbd)
            CBE: Cbei_0325
            CKL: CKL_0458(hbd1) CKL_2795(hbd2)
            AMT: Amet_4523
            CHY: CHY_1292(hbd1) CHY_1603(hbd2) CHY_1740(hbd3)
            DSY: DSY1566 DSY1717 DSY2491
            DRM: Dred_1493 Dred_1780 Dred_1890
            SWO: Swol_0307 Swol_0435 Swol_0791 Swol_1171 Swol_1485 Swol_1935
                 Swol_2030
            TTE: TTE0548(fadB)
            MTU: Rv0468(fadB2) Rv1715(fadB3)
            MTC: MT1754
            MBO: Mb0477(fadB2) Mb1742(fadB3a) Mb1743(fadB3b)
            MBB: BCG_0508(fadB2) BCG_1754(fadB3)
            MSM: MSMEG_0912 MSMEG_4110 MSMEG_4115 MSMEG_4116
            MVA: Mvan_0802
            MGI: Mflv_0106
            MMC: Mmcs_0637
            MKM: Mkms_0650
            MJL: Mjls_0630
            CEF: CE0323 CE2775
            CJK: jk0588(fadB2)
            NFA: nfa20450(fadB2)
            RHA: RHA1_ro02121(hbd1) RHA1_ro02208(hbd2) RHA1_ro05099(hbd3)
                 RHA1_ro11071
            SCO: SCO3834(SCH69.04c) SCO5385(2SC6G5.29)
            SMA: SAV2870(fadC3) SAV4359(paaH)
            ART: Arth_3266
            NCA: Noca_0861 Noca_1784 Noca_4074 Noca_4294 Noca_4392
            TFU: Tfu_2399
            FRA: Francci3_1000 Francci3_1550 Francci3_3694
            FAL: FRAAL1983
            ACE: Acel_0147 Acel_0658
            SEN: SACE_4006(paaH2)
            STP: Strop_0163 Strop_3618 Strop_3624
            BLO: BL0058
            RXY: Rxyl_1761 Rxyl_2336
            FNU: FN1019
            TDE: TDE0610
            PGI: PG1080
            SRU: SRU_1413
            CHU: CHU_2019(paaH)
            FJO: Fjoh_3448
            DRA: DR_1068
            DGE: Dgeo_1444
            TTH: TTC0898
            TTJ: TTHA1262
            TAC: Ta0947
            TVO: TVN1091
            PTO: PTO1021 PTO1504
            SSO: SSO0647(hdb-1) SSO2871(hdb-2) SSO2996(hdb-3)
            STO: ST1507 ST2094
            SAI: Saci_1078 Saci_1623
            MSE: Msed_1423
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.157
            ExPASy - ENZYME nomenclature database: 1.1.1.157
            ExplorEnz - The Enzyme Database: 1.1.1.157
            ERGO genome analysis and discovery system: 1.1.1.157
            BRENDA, the Enzyme Database: 1.1.1.157
            CAS: 39319-78-3
///
ENTRY       EC 1.1.1.158                Enzyme
NAME        UDP-N-acetylmuramate dehydrogenase;
            MurB reductase;
            UDP-N-acetylenolpyruvoylglucosamine reductase;
            UDP-N-acetylglucosamine-enoylpyruvate reductase;
            UDP-GlcNAc-enoylpyruvate reductase;
            uridine diphosphoacetylpyruvoylglucosamine reductase;
            uridine diphospho-N-acetylglucosamine-enolpyruvate reductase;
            uridine-5'-diphospho-N-acetyl-2-amino-2-deoxy-3-O-
            lactylglucose:NADP-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     UDP-N-acetylmuramate:NADP+ oxidoreductase
REACTION    UDP-N-acetylmuramate + NADP+ =
            UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + NADPH + H+
            [RN:R03192]
ALL_REAC    R03192;
            (other) R03191
SUBSTRATE   UDP-N-acetylmuramate [CPD:C01050];
            NADP+ [CPD:C00006]
PRODUCT     UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine [CPD:C04631];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Sodium dithionite, sodium borohydride and, to
            a lesser extent, NADH, can replace NADPH.
REFERENCE   1  [PMID:4717533]
  AUTHORS   Taku A, Anwar RA.
  TITLE     Biosynthesis of uridine diphospho-N-acetylmuramic acid. IV.
            Activation of uridine diphospho-N-acetylenolpyruvylglucosamine
            reductase by monovalent cations.
  JOURNAL   J. Biol. Chem. 248 (1973) 4971-6.
  ORGANISM  Enterobacter cloacae, Staphylococcus epidermidis
REFERENCE   2  [PMID:4394163]
  AUTHORS   Taku A, Gunetileke KG, Anwar RA.
  TITLE     Biosynthesis of uridine diphospho-N-acetylmuramic acid. 3.
            Purification and properties of uridine
            diphospho-N-acetylenolpyruvyl-glucosamine reductase.
  JOURNAL   J. Biol. Chem. 245 (1970) 5012-6.
  ORGANISM  Enterobacter cloacae
REFERENCE   3  [PMID:11699883]
  AUTHORS   van Heijenoort J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit.
  JOURNAL   Nat. Prod. Rep. 18 (2001) 503-19.
  ORGANISM  Enterobacter cloacae, Escherichia coli [GN:eco]
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K00075  UDP-N-acetylmuramate dehydrogenase
GENES       AFM: AFUA_2G09580
            AOR: AO090138000018
            ECO: b3972(murB)
            ECJ: JW3940(murB)
            ECE: Z5543(murB)
            ECS: ECs4899
            ECC: c4931(murB)
            ECI: UTI89_C3804(murB)
            ECP: ECP_4186
            ECV: APECO1_2495(murB)
            ECW: EcE24377A_4511(murB)
            ECX: EcHS_A4206
            STY: STY3742(murB)
            STT: t3489(murB)
            SPT: SPA3976(murB)
            SEC: SC4025(murB)
            STM: STM4137(murB)
            YPE: YPO3760(murB)
            YPK: y0471(murB)
            YPM: YP_3288(murB)
            YPA: YPA_3429
            YPN: YPN_0205
            YPP: YPDSF_3381
            YPS: YPTB0272(murB)
            YPI: YpsIP31758_3872(murB)
            SFL: SF4050(murB)
            SFX: S3690(murB)
            SFV: SFV_4045(murB)
            SSN: SSON_4145(murB)
            SBO: SBO_3992(murB)
            SDY: SDY_3756(murB)
            ECA: ECA0213(murB)
            PLU: plu4733(murB)
            BUC: BU045(murB)
            BAS: BUsg042(murB)
            BAB: bbp046(murB)
            WBR: WGLp512(murB)
            SGL: SG0124
            ENT: Ent638_3944
            SPE: Spro_0267
            BFL: Bfl183(murB)
            BPN: BPEN_189(murB)
            HIT: NTHI0375(murB)
            HIP: CGSHiEE_01715(murB)
            HDU: HD0081(murB)
            HSO: HS_1511(murB)
            PMU: PM1589(murB)
            MSU: MS0028(murB)
            APL: APL_1851(murB)
            ASU: Asuc_0451
            XFA: XF2572
            XFT: PD1953(murB)
            XCC: XCC1787(murB)
            XCB: XC_2449
            XCV: XCV1834(murB)
            XAC: XAC1804(murB)
            XOO: XOO2236(murB)
            XOM: XOO_2101(XOO2101)
            VCH: VC0318(murB)
            VCO: VC0395_A2716(murB)
            VVU: VV1_1197
            VVY: VV3170
            VPA: VP2932
            VFI: VF2426
            PPR: PBPRA3446
            PAE: PA2977(murB)
            PAU: PA14_25550(murB)
            PAP: PSPA7_2184(murB)
            PPU: PP_1904(murB)
            PPF: Pput_3810
            PST: PSPTO_3842(murB)
            PSB: Psyr_1637(murB)
            PSP: PSPPH_1631(murB)
            PFL: PFL_1782(murB)
            PFO: Pfl_4171(murB)
            PEN: PSEEN1607(murB)
            PMY: Pmen_1618
            PAR: Psyc_0948(murB)
            PCR: Pcryo_1470
            PRW: PsycPRwf_0774
            ACI: ACIAD1945(murB)
            SON: SO_0213(murB)
            SDN: Sden_0153
            SFR: Sfri_0131
            SAZ: Sama_0196
            SBL: Sbal_4175
            SBM: Shew185_0179
            SLO: Shew_0141
            SPC: Sputcn32_3776
            SSE: Ssed_4335
            SPL: Spea_0167
            SHE: Shewmr4_0181
            SHM: Shewmr7_0176
            SHN: Shewana3_0182
            SHW: Sputw3181_0139
            ILO: IL2004(murB)
            CPS: CPS_4746(murB)
            PHA: PSHAa2914(murB)
            PAT: Patl_3999
            SDE: Sde_2056
            PIN: Ping_0218
            MAQ: Maqu_1736
            CBU: CBU_0137(murB)
            CBD: COXBU7E912_1970(murB)
            LPN: lpg2613(murB)
            LPF: lpl2536(murB)
            LPP: lpp2666(murB)
            MCA: MCA2427(murB)
            FTU: FTT1304c(murB)
            FTF: FTF1304c(murB)
            FTW: FTW_0742(murB)
            FTL: FTL_0412
            FTH: FTH_0405(murB)
            FTA: FTA_0435(murB)
            FTN: FTN_0448(murB)
            TCX: Tcr_1294
            NOC: Noc_2859(murB)
            AEH: Mlg_2191
            HHA: Hhal_0761 Hhal_2089
            HCH: HCH_02708(murB)
            CSA: Csal_1591
            ABO: ABO_1059(murB)
            MMW: Mmwyl1_2155
            AHA: AHA_4041(murB)
            DNO: DNO_0436(murB)
            BCI: BCI_0504(murB)
            RMA: Rmag_0758
            VOK: COSY_0700(murB)
            NME: NMB0811
            NMA: NMA1021(murB)
            NMC: NMC0762(murB)
            NGO: NGO0394
            CVI: CV_1592(murB)
            RSO: RSc2550(murB)
            REU: Reut_A2761
            REH: H16_A3061(murB)
            RME: Rmet_2900
            BMA: BMA0374(murB)
            BMV: BMASAVP1_A0674(murB)
            BML: BMA10299_A2509(murB)
            BMN: BMA10247_0123(murB)
            BXE: Bxe_A0755
            BVI: Bcep1808_2647
            BUR: Bcep18194_A5886
            BCN: Bcen_1943
            BCH: Bcen2424_2554
            BAM: Bamb_2602
            BPS: BPSL0868(murB)
            BPM: BURPS1710b_1072(murB)
            BPL: BURPS1106A_0920(murB)
            BPD: BURPS668_0916(murB)
            BTE: BTH_I0731(murB)
            PNU: Pnuc_0289
            BPE: BP2510(murB)
            BPA: BPP3497(murB)
            BBR: BB3945(murB)
            RFR: Rfer_2691
            POL: Bpro_1597
            PNA: Pnap_1081
            AAV: Aave_1855
            AJS: Ajs_2749
            VEI: Veis_3463
            MPT: Mpe_A3038
            HAR: HEAR0866(murB)
            MMS: mma_0841
            NEU: NE0993(murB)
            NET: Neut_0244
            NMU: Nmul_A2492
            EBA: ebA3410(murB)
            AZO: azo3689(murB)
            DAR: Daro_0044
            TBD: Tbd_0121(murB)
            MFA: Mfla_2267
            HPY: HP1418(murB)
            HPJ: jhp1313(murB)
            HPA: HPAG1_1344
            HHE: HH0439(murB)
            HAC: Hac_0104(murB)
            WSU: WS1488(murB)
            TDN: Tmden_2006
            CJE: Cj1676(murB)
            CJR: CJE1848(murB)
            CJJ: CJJ81176_1672(murB)
            CJU: C8J_1577(murB)
            CJD: JJD26997_2050(murB)
            CFF: CFF8240_0204(murB)
            CCV: CCV52592_0618(murB)
            CHA: CHAB381_0339(murB)
            CCO: CCC13826_2096(murB)
            ABU: Abu_2234(murB)
            NIS: NIS_1661
            SUN: SUN_0080
            GSU: GSU3067(murB)
            GME: Gmet_0414
            GUR: Gura_3972
            PCA: Pcar_2200
            PPD: Ppro_3287
            DVU: DVU2502(murB)
            DVL: Dvul_0743
            DDE: Dde_1044
            LIP: LI1106
            BBA: Bd3233(murB)
            DPS: DP2896(murB)
            ADE: Adeh_3773
            AFW: Anae109_3886
            MXA: MXAN_5602(murB)
            SAT: SYN_01748
            SFU: Sfum_3471
            RPR: RP248(murB)
            RTY: RT0240(murB)
            RCO: RC0332(murB)
            RFE: RF_1036(murB)
            RBE: RBE_0962(murB)
            RAK: A1C_01805(murB)
            RBO: A1I_03845(murB)
            RCM: A1E_01425(murB)
            RRI: A1G_01905(murB)
            OTS: OTBS_0599(murB)
            WOL: WD0541(murB)
            WBM: Wbm0778
            AMA: AM701(murB)
            APH: APH_0745(murB)
            NSE: NSE_0590
            PUB: SAR11_0022(murB)
            MLO: mll1552
            MES: Meso_2005
            PLA: Plav_2423
            SME: SMc01868(murB)
            SMD: Smed_2080
            ATU: Atu2092(murB)
            ATC: AGR_C_3794
            RET: RHE_CH02845(murB)
            RLE: RL3305
            BME: BMEI0581(murB)
            BMF: BAB1_1448(murB)
            BMS: BR1429(murB)
            BMB: BruAb1_1424(murB)
            BOV: BOV_1386(murB)
            OAN: Oant_1746
            BJA: bll6600(murB)
            BRA: BRADO5657(murB)
            BBT: BBta_6170(murB)
            RPA: RPA3528(murB)
            RPB: RPB_1998
            RPC: RPC_3304
            RPD: RPD_3392
            RPE: RPE_2110
            NWI: Nwi_1054(murB)
            NHA: Nham_1282
            BHE: BH11220(murB)
            BQU: BQ08840(murB)
            BBK: BARBAKC583_0945(murB)
            XAU: Xaut_0324
            CCR: CC_2545
            SIL: SPO1200(murB)
            SIT: TM1040_0685
            RSP: RSP_2110(murB)
            RSH: Rsph17029_0786
            RSQ: Rsph17025_0696
            JAN: Jann_2754
            RDE: RD1_3352(murB)
            PDE: Pden_4491
            MMR: Mmar10_2076
            HNE: HNE_0397(murB)
            ZMO: ZMO0833(murB)
            NAR: Saro_1135
            SAL: Sala_1879
            SWI: Swit_3944
            ELI: ELI_01805
            GOX: GOX0160
            GBE: GbCGDNIH1_0427
            ACR: Acry_0065
            RRU: Rru_A0948
            MAG: amb3850
            MGM: Mmc1_0751
            ABA: Acid345_1879
            SUS: Acid_7881
            BSU: BG10228(murB)
            BHA: BH2564(murB)
            BAN: BA4048(murB-1) BA5315(murB-2)
            BAR: GBAA4048(murB-1) GBAA5315(murB-2)
            BAA: BA_0174(murB) BA_4518(murB)
            BAT: BAS3760 BAS4937
            BCE: BC3909(murB) BC5063(murB)
            BCA: BCE_3955(murB) BCE_5212(murB)
            BCZ: BCZK3668(murB) BCZK4798(murB)
            BCY: Bcer98_2559 Bcer98_3647
            BTK: BT9727_3651(murB) BT9727_4778(murB)
            BTL: BALH_3539(murB) BALH_4604(murB)
            BLI: BL02244(murB)
            BLD: BLi01740(murB)
            BCL: ABC3971(murB)
            BAY: RBAM_015090
            BPU: BPUM_1416
            OIH: OB0556
            GKA: GK0918
            SAU: SA0693
            SAV: SAV0738
            SAM: MW0700
            SAR: SAR0792(murB)
            SAS: SAS0703
            SAC: SACOL0801(murB)
            SAB: SAB0690c
            SAA: SAUSA300_0722(murB)
            SAO: SAOUHSC_00752
            SAJ: SaurJH9_0762
            SAH: SaurJH1_0779
            SEP: SE0520
            SER: SERP0405(murB)
            SHA: SH2153(murB)
            SSP: SSP1978
            LMO: lmo1420
            LMF: LMOf2365_1439(murB)
            LIN: lin1459
            LWE: lwe1437(murB)
            LLA: L173881(murB)
            LLC: LACR_1283
            LLM: llmg_1329(murB)
            SPY: SPy_1101(murB)
            SPZ: M5005_Spy_0825(murB)
            SPM: spyM18_1063(murB)
            SPG: SpyM3_0763(murB)
            SPS: SPs0963
            SPH: MGAS10270_Spy0941(murB)
            SPI: MGAS10750_Spy0976(murB)
            SPJ: MGAS2096_Spy0899(murB)
            SPK: MGAS9429_Spy0944(murB)
            SPF: SpyM50963(murB)
            SPA: M6_Spy0823(murB)
            SPB: M28_Spy0802(murB)
            SPN: SP_1390
            SPR: spr1247(murB)
            SPD: SPD_1222(murB)
            SAG: SAG1112(murB)
            SAN: gbs1179
            SAK: SAK_1197(murB)
            SMU: SMU.972(murB)
            STC: str1539(murB)
            STL: stu1539(murB)
            STE: STER_1497
            SSA: SSA_1047(murB)
            SGO: SGO_0804(murB)
            LPL: lp_0814(murB)
            LJO: LJ0887
            LAC: LBA0708(murB)
            LSA: LSA1337(murB)
            LSL: LSL_1148(murB)
            LDB: Ldb0646(murB)
            LBU: LBUL_0577
            LBR: LVIS_0681
            LCA: LSEI_1003
            LGA: LGAS_1293
            LRE: Lreu_0403
            PPE: PEPE_0474
            EFA: EF2489 EF2733(murB)
            OOE: OEOE_1658
            STH: STH1211 STH692
            CAC: CAC0510(murB)
            CPE: CPE0353(murB)
            CPF: CPF_0342(murB)
            CPR: CPR_0334(murB)
            CTC: CTC02496(murB)
            CNO: NT01CX_1283(murB)
            CTH: Cthe_0112
            CDF: CD3402(murB)
            CBO: CBO3378(murB)
            CBA: CLB_3434(murB)
            CBH: CLC_3321(murB)
            CBF: CLI_3562(murB)
            CBE: Cbei_4858
            CKL: CKL_3565(murB)
            AMT: Amet_4093
            CHY: CHY_2067(murB)
            DSY: DSY2906
            DRM: Dred_0677
            SWO: Swol_1015
            CSC: Csac_1159
            TTE: TTE1836(murB)
            MTA: Moth_0845
            MTU: Rv0482(murB)
            MTC: MT0500(murB)
            MBO: Mb0492(murB)
            MBB: BCG_0523(murB)
            MLE: ML2447(murB)
            MPA: MAP3975(murB)
            MAV: MAV_4668
            MSM: MSMEG_0928(murB)
            MVA: Mvan_0823
            MGI: Mflv_0090
            MMC: Mmcs_0653
            MKM: Mkms_0666
            MJL: Mjls_0646
            CGL: NCgl0346(cgl0353) NCgl0386(murB)
            CGB: cg0423(murB) cg0476(murB)
            CEF: CE0417
            CDI: DIP0384
            CJK: jk1919(murB)
            NFA: nfa51970(murB)
            RHA: RHA1_ro02086
            SCO: SCO4643(murB)
            SMA: SAV4905(murB)
            TWH: TWT718(murB)
            TWS: TW734(murB)
            LXX: Lxx02830(murB)
            ART: Arth_3024
            AAU: AAur_2999(murB)
            PAC: PPA1894(murB)
            NCA: Noca_0672
            TFU: Tfu_2664(murB)
            ACE: Acel_0291
            KRA: Krad_0667
            SEN: SACE_6978(murB)
            STP: Strop_0328
            BLO: BL1561(murB)
            BAD: BAD_0294(murB)
            RXY: Rxyl_2807
            FNU: FN1455
            RBA: RB2661(murB)
            CTR: CT831(murB)
            CTA: CTA_0906(murB)
            CMU: TC0218
            CPN: CPn0988(murB)
            CPA: CP0867
            CPJ: CPj0988(murB)
            CPT: CpB1024
            CCA: CCA00773(murB)
            CAB: CAB741
            CFE: CF0241(murB)
            PCU: pc1624(murB)
            BGA: BG0611(murB)
            BAF: BAPKO_0630(murB)
            TPA: TP0090
            TDE: TDE0093
            LIL: LA3930(murB)
            LIC: LIC13138(murB)
            LBJ: LBJ_0387(murB)
            LBL: LBL_2690(murB)
            SYN: slr1424
            SYW: SYNW0028(murB)
            SYC: syc2351_d(murB)
            SYF: Synpcc7942_1740
            SYD: Syncc9605_0028
            SYE: Syncc9902_0024
            SYG: sync_0027(murB)
            SYR: SynRCC307_0026(murB)
            SYX: SynWH7803_0027(murB)
            CYA: CYA_1875(murB)
            CYB: CYB_1560(murB)
            TEL: tll0370
            GVI: gll1780 glr2317
            ANA: alr5066
            AVA: Ava_2321
            PMA: Pro0021(murB)
            PMM: PMM0021(murB)
            PMT: PMT0026(murB)
            PMN: PMN2A_1348
            PMI: PMT9312_0021
            PMB: A9601_00201(murB)
            PMC: P9515_00201(murB)
            PMF: P9303_00251(murB)
            PMG: P9301_00201(murB)
            PMH: P9215_00201
            PME: NATL1_00201(murB)
            TER: Tery_4028
            BTH: BT_1368
            BFR: BF2985
            BFS: BF2861(murB)
            PGI: PG1342(murB)
            SRU: SRU_2184(murB)
            CHU: CHU_2214(murB)
            GFO: GFO_2930(murB)
            FJO: Fjoh_0218
            FPS: FP1996(murB)
            CCH: Cag_1430
            CPH: Cpha266_1255
            PVI: Cvib_0838
            PLT: Plut_1114
            RRS: RoseRS_3790
            RCA: Rcas_1091
            DRA: DR_0628
            DGE: Dgeo_1632
            TTH: TTC0721
            TTJ: TTHA1086
            AAE: aq_520(murB1)
            TMA: TM1714
            TPT: Tpet_1010
            TME: Tmel_1529
            FNO: Fnod_0268
            MBA: Mbar_A0023
STRUCTURES  PDB: 1HSK  1MBB  1MBT  1UXY  2GQT  2GQU  2MBR  2Q85  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.158
            ExPASy - ENZYME nomenclature database: 1.1.1.158
            ExplorEnz - The Enzyme Database: 1.1.1.158
            ERGO genome analysis and discovery system: 1.1.1.158
            BRENDA, the Enzyme Database: 1.1.1.158
            CAS: 39307-28-3
///
ENTRY       EC 1.1.1.159                Enzyme
NAME        7alpha-hydroxysteroid dehydrogenase;
            7alpha-hydroxy steroid dehydrogenase;
            7alpha-HSDH
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     7alpha-hydroxysteroid:NAD+ 7-oxidoreductase
REACTION    3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + NAD+ =
            3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
            [RN:R02792]
ALL_REAC    R02792
SUBSTRATE   3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate [CPD:C00695];
            NAD+ [CPD:C00003]
PRODUCT     3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate [CPD:C04643];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Catalyses the oxidation of the 7alpha-hydroxy group of bile acids
            and alcohols both in their free and conjugated forms. The
            Bacteroides fragilis and Clostridium enzymes can also utilize NADP+.
REFERENCE   1  [PMID:786279]
  AUTHORS   Haslewood ES, Haslewood GA.
  TITLE     The specificity of a 7 alpha-hydroxy steroid dehydrogenase from
            Escherichia coli.
  JOURNAL   Biochem. J. 157 (1976) 207-10.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:6945134]
  AUTHORS   MacDonald IA, Roach PD.
  TITLE     Bile induction of 7 alpha- and 7 beta-hydroxysteroid dehydrogenases
            in Clostridium absonum.
  JOURNAL   Biochim. Biophys. Acta. 665 (1981) 262-9.
  ORGANISM  Clostridium absonum
REFERENCE   3  [PMID:4581498]
  AUTHORS   Macdonald IA, Williams CN, Mahony DE.
  TITLE     7Alpha-hydroxysteroid dehydrogenase from Escherichia coli B:
            preliminary studies.
  JOURNAL   Biochim. Biophys. Acta. 309 (1973) 243-53.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:236764]
  AUTHORS   Macdonald IA, Williams CN, Mahony DE, Christie WM.
  TITLE     NAD- and NADP-dependent 7alpha-hydroxysteroid dehydrogenases from
            bacteroides fragilis.
  JOURNAL   Biochim. Biophys. Acta. 384 (1975) 12-24.
  ORGANISM  Bacteroides fragilis
ORTHOLOGY   KO: K00076  7-alpha-hydroxysteroid dehydrogenase
GENES       AFM: AFUA_1G06280 AFUA_5G01040 AFUA_5G14000
            TET: TTHERM_00637450
            ECO: b1619(hdhA)
            ECJ: JW1611(hdhA)
            ECE: Z2624(hdhA)
            ECS: ECs2327
            ECC: c2011(hdhA)
            ECI: UTI89_C1807(hdhA)
            ECP: ECP_1563
            ECV: APECO1_702(hdhA)
            SFL: SF1644(hdhA)
            SSN: SSON_1541(hdhA)
            SBO: SBO_1517(hdhA)
            SDY: SDY_1838(hdhA)
            PCR: Pcryo_2061
            PHA: PSHAa2129(hdhA)
            REH: H16_B0648
            BXE: Bxe_C0288
            NET: Neut_1072
            HPY: HP1014
            HPA: HPAG1_0432
            HHE: HH1627
            HAC: Hac_1118(hdhA)
            WSU: WS2222
            NIS: NIS_0698
            SUN: SUN_0808
            BME: BMEI0405 BMEI0406
            BMF: BAB1_1634
            BMS: BR1618
            BMB: BruAb1_1604 BruAb1_1605
            BOV: BOV_1561
            CPF: CPF_1154
            CPR: CPR_0991
            MTC: MT0954
            MBO: Mb0950c
            MPA: MAP0871c
            NFA: nfa24670
            CHU: CHU_1091(hdhA)
STRUCTURES  PDB: 1AHH  1AHI  1FMC  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.159
            ExPASy - ENZYME nomenclature database: 1.1.1.159
            ExplorEnz - The Enzyme Database: 1.1.1.159
            ERGO genome analysis and discovery system: 1.1.1.159
            BRENDA, the Enzyme Database: 1.1.1.159
            CAS: 39361-64-3
///
ENTRY       EC 1.1.1.160                Enzyme
NAME        dihydrobunolol dehydrogenase;
            bunolol reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (+/-)-5-[(tert-butylamino)-2'-hydroxypropoxy]-1,2,3,4-tetrahydro-1-n
            aphthol:NADP+ oxidoreductase
REACTION    (+/-)-5-[(tert-butylamino)-2'-hydroxypropoxy]-1,2,3,4-tetrahydro-1-
            naphthol + NADP+ =
            (+/-)-5-[(tert-butylamino)-2'-hydroxypropoxy]-3,4-dihydro-1(2H)-
            naphthalenone + NADPH + H+ [RN:R04623]
ALL_REAC    R04623
SUBSTRATE   (+/-)-5-[(tert-butylamino)-2'-hydroxypropoxy]-1,2,3,4-tetrahydro-1-
            naphthol [CPD:C04875];
            NADP+ [CPD:C00006]
PRODUCT     (+/-)-5-[(tert-butylamino)-2'-hydroxypropoxy]-3,4-dihydro-1(2H)-
            naphthalenone [CPD:C04883];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts, more slowly, with NAD+.
REFERENCE   1  [PMID:4560367]
  AUTHORS   Leinweber FJ, Greenough RC, Schwender CF, Kaplan HR, Di Carlo FJ.
  TITLE     Bunolol metabolism by cell-free preparations of human liver:
            biosynthesis of dihydrobunolol.
  JOURNAL   Xenobiotica. 2 (1972) 191-202.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:4560367]
  AUTHORS   Leinweber FJ, Greenough RC, Schwender CF, Kaplan HR, Di Carlo FJ.
  TITLE     Bunolol metabolism by cell-free preparations of human liver:
            biosynthesis of dihydrobunolol.
  JOURNAL   Xenobiotica. 2 (1972) 191-202.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.160
            ExPASy - ENZYME nomenclature database: 1.1.1.160
            ExplorEnz - The Enzyme Database: 1.1.1.160
            ERGO genome analysis and discovery system: 1.1.1.160
            BRENDA, the Enzyme Database: 1.1.1.160
            CAS: 62213-61-0
///
ENTRY       EC 1.1.1.161                Enzyme
NAME        cholestanetetraol 26-dehydrogenase;
            cholestanetetrol 26-dehydrogenase;
            5beta-cholestane-3alpha,7alpha,12alpha,26-tetrol dehydrogenase;
            TEHC-NAD oxidoreductase;
            5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol:NAD+
            26-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol:NAD+
            26-oxidoreductase
REACTION    (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + NAD+ =
            (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + NADH
            + H+ [RN:R03507]
ALL_REAC    R03507
SUBSTRATE   (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol;
            NAD+ [CPD:C00003]
PRODUCT     (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al;
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:5914340]
  AUTHORS   Masui T, Herman R, Staple E.
  TITLE     The oxidation of 5-beta-cholestane-3-alpha, 7-alpha, 12-alpha,
            26-tetraol to 5-beta-cholestane-3-alpha, 7-alpha,
            12-alpha-triol-26-oic acid via 5-beta-cholestane-3-alpha, 7-alpha,
            12-alpha-triol-26-al by rat liver.
  JOURNAL   Biochim. Biophys. Acta. 117 (1966) 266-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00120  Bile acid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.161
            ExPASy - ENZYME nomenclature database: 1.1.1.161
            ExplorEnz - The Enzyme Database: 1.1.1.161
            ERGO genome analysis and discovery system: 1.1.1.161
            BRENDA, the Enzyme Database: 1.1.1.161
            CAS: 62213-60-9
///
ENTRY       EC 1.1.1.162                Enzyme
NAME        erythrulose reductase;
            D-erythrulose reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     erythritol:NADP+ oxidoreductase
REACTION    erythritol + NADP+ = D-erythrulose + NADPH + H+ [RN:R02431]
ALL_REAC    R02431
SUBSTRATE   erythritol [CPD:C00503];
            NADP+ [CPD:C00006]
PRODUCT     D-erythrulose [CPD:C02022];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     NAD+ is also utilized, more slowly.
REFERENCE   1  [PMID:4152124]
  AUTHORS   Uehara K, Tanimoto T, Sato H.
  TITLE     Studies on D-tetrose metabolism. IV. Purification and some
            properties of D-erythrulose reductase from beef liver.
  JOURNAL   J. Biochem. (Tokyo). 75 (1974) 333-45.
  ORGANISM  cow [GN:bta]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.162
            ExPASy - ENZYME nomenclature database: 1.1.1.162
            ExplorEnz - The Enzyme Database: 1.1.1.162
            ERGO genome analysis and discovery system: 1.1.1.162
            BRENDA, the Enzyme Database: 1.1.1.162
            CAS: 52064-49-0
///
ENTRY       EC 1.1.1.163                Enzyme
NAME        cyclopentanol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     cyclopentanol:NAD+ oxidoreductase
REACTION    cyclopentanol + NAD+ = cyclopentanone + NADH + H+ [RN:R02553]
ALL_REAC    R02553
SUBSTRATE   cyclopentanol [CPD:C02020];
            NAD+ [CPD:C00003]
PRODUCT     cyclopentanone [CPD:C00557];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     4-Methylcyclohexanol and cyclohexanol can also act as substrates.
REFERENCE   1  [PMID:4349113]
  AUTHORS   Griffin M, Trudgill PW.
  TITLE     The metabolism of cyclopentanol by Pseudomonas N.C.I.B. 9872.
  JOURNAL   Biochem. J. 129 (1972) 595-603.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:12406764]
  AUTHORS   Iwaki H, Hasegawa Y, Wang S, Kayser MM, Lau PC.
  TITLE     Cloning and characterization of a gene cluster involved in
            cyclopentanol metabolism in Comamonas sp. strain NCIMB 9872 and
            biotransformations effected by Escherichia coli-expressed
            cyclopentanone 1,2-monooxygenase.
  JOURNAL   Appl. Environ. Microbiol. 68 (2002) 5671-84.
  ORGANISM  Comamonas sp.
GENES       MSM: MSMEG_6709
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.163
            ExPASy - ENZYME nomenclature database: 1.1.1.163
            ExplorEnz - The Enzyme Database: 1.1.1.163
            ERGO genome analysis and discovery system: 1.1.1.163
            BRENDA, the Enzyme Database: 1.1.1.163
            CAS: 37364-12-8
///
ENTRY       EC 1.1.1.164                Enzyme
NAME        hexadecanol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     hexadecanol:NAD+ oxidoreductase
REACTION    hexadecanol + NAD+ = hexadecanal + NADH + H+ [RN:R02462]
ALL_REAC    R02462
SUBSTRATE   hexadecanol [CPD:C00823];
            NAD+ [CPD:C00003]
PRODUCT     hexadecanal [CPD:C00517];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The liver enzyme acts on long-chain alcohols from C8 to C16. The
            Euglena enzyme also oxidizes the corresponding aldehydes to fatty
            acids.
REFERENCE   1  [PMID:4313936]
  AUTHORS   Kolattukudy PE.
  TITLE     Reduction of fatty acids to alcohols by cell-free preparations of
            Euglena gracilis.
  JOURNAL   Biochemistry. 9 (1970) 1095-102.
  ORGANISM  Euglena gracilis
REFERENCE   2  [PMID:5432753]
  AUTHORS   Stoffel W, LeKim D, Heyn G.
  TITLE     Metabolism of sphingosine bases. XIV. Sphinganine
            (dihydrosphingosine), an effective donor of the alk-1-enyl chain of
            plasmalogens.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 351 (1970) 875-83.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.164
            ExPASy - ENZYME nomenclature database: 1.1.1.164
            ExplorEnz - The Enzyme Database: 1.1.1.164
            ERGO genome analysis and discovery system: 1.1.1.164
            BRENDA, the Enzyme Database: 1.1.1.164
            CAS: 62213-59-6
///
ENTRY       EC 1.1.1.165                Enzyme
NAME        2-alkyn-1-ol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-butyne-1,4-diol:NAD+ 1-oxidoreductase
REACTION    2-butyne-1,4-diol + NAD+ = 4-hydroxy-2-butynal + NADH + H+
            [RN:R03963]
ALL_REAC    R03963
SUBSTRATE   2-butyne-1,4-diol [CPD:C02497];
            NAD+ [CPD:C00003]
PRODUCT     4-hydroxy-2-butynal [CPD:C02648];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Acts on a variety of 2-alkyn-1-ols, and also on 1,4-butanediol.
            NADP+ also acts as acceptor, but more slowly.
REFERENCE   1
  AUTHORS   Miyoshi, T., Sato, H. and Harada, T.
  TITLE     Purification and characterization of 2-alkyne-1-ol dehydrogenase
            induced by 2-butene-1,4-diol in Fusarium merismoides B11.
  JOURNAL   Biochim. Biophys. Acta 358 (1974) 231-239.
  ORGANISM  Fusarium merismoides
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.165
            ExPASy - ENZYME nomenclature database: 1.1.1.165
            ExplorEnz - The Enzyme Database: 1.1.1.165
            ERGO genome analysis and discovery system: 1.1.1.165
            BRENDA, the Enzyme Database: 1.1.1.165
            CAS: 54576-94-2
///
ENTRY       EC 1.1.1.166                Enzyme
NAME        hydroxycyclohexanecarboxylate dehydrogenase;
            dihydroxycyclohexanecarboxylate dehydrogenase;
            (-)t-3,t-4-dihydroxycyclohexane-c-1-carboxylate-NAD+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate:NAD+
            3-oxidoreductase
REACTION    (1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate + NAD+ =
            (1S,4S)-4-hydroxy-3-oxocyclohexane-1-carboxylate + NADH + H+
            [RN:R05315]
ALL_REAC    R05315
SUBSTRATE   (1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate [CPD:C04687];
            NAD+ [CPD:C00003]
PRODUCT     (1S,4S)-4-hydroxy-3-oxocyclohexane-1-carboxylate [CPD:C04670];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Acts on hydroxycyclohexanecarboxylates that have an equatorial
            carboxy group at C-1, an axial hydroxy group at C-3 and an
            equatorial hydroxy or carbonyl group at C-4, including (-)-quinate
            and (-)-shikimate.
REFERENCE   1  [PMID:4375976]
  AUTHORS   Whiting GC, Coggins RA.
  TITLE     A new nicotinamide-adenine dinucleotide-dependent hydroaromatic
            dehydrogenase of Lactobacillus plantarum and its role in formation
            of (minus)t-3,t-4-dihydroxycyclohexane-c-1-carboxylate.
  JOURNAL   Biochem. J. 141 (1974) 35-42.
  ORGANISM  Lactobacillus plantarum [GN:lpl]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.166
            ExPASy - ENZYME nomenclature database: 1.1.1.166
            ExplorEnz - The Enzyme Database: 1.1.1.166
            ERGO genome analysis and discovery system: 1.1.1.166
            BRENDA, the Enzyme Database: 1.1.1.166
            CAS: 55467-53-3
///
ENTRY       EC 1.1.1.167                Enzyme
NAME        hydroxymalonate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     hydroxymalonate:NAD+ oxidoreductase
REACTION    hydroxymalonate + NAD+ = oxomalonate + NADH + H+ [RN:R02969]
ALL_REAC    R02969
SUBSTRATE   hydroxymalonate [CPD:C02287];
            NAD+ [CPD:C00003]
PRODUCT     oxomalonate [CPD:C00830];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Jukova, N.I., Klunova, S.M. and Philippovich, Y.B.
  TITLE     Biochemistry of Insects, issue 17.
  JOURNAL   V.I. Lenin State Pedagogical Institute, Moscow, 1971, p. 56.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.167
            ExPASy - ENZYME nomenclature database: 1.1.1.167
            ExplorEnz - The Enzyme Database: 1.1.1.167
            ERGO genome analysis and discovery system: 1.1.1.167
            BRENDA, the Enzyme Database: 1.1.1.167
            CAS: 58693-60-0
///
ENTRY       EC 1.1.1.168                Enzyme
NAME        2-dehydropantolactone reductase (A-specific);
            2-oxopantoyl lactone reductase;
            ketopantoyl lactone reductase;
            2-ketopantoyl lactone reductase;
            2-dehydropantoyl-lactone reductase (A-specific)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-pantolactone:NADP+ oxidoreductase (A-specific)
REACTION    (R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
            [RN:R03155]
ALL_REAC    R03155
SUBSTRATE   (R)-pantolactone [CPD:C01012];
            NADP+ [CPD:C00006]
PRODUCT     2-dehydropantolactone [CPD:C01125];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The yeast enzyme differs from that from Escherichia coli [EC
            1.1.1.214 2-dehydropantolactone reductase (B-specific)], which is
            specific for the B-face of NADP+, and in receptor requirements from
            EC 1.1.99.26 3-hydroxycyclohexanone dehydrogenase.
REFERENCE   1
  AUTHORS   King, H.L., Jr. and Wilken, D.R.
  TITLE     Ketopantoyl lactone and ketopantoic acid reductases.
            Characterization of the reactions and purification of two forms of
            ketopantoyl lactone reductase.
  JOURNAL   J. Biol. Chem. 247 (1972) 4689-4695.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:234966]
  AUTHORS   Wilken DR, King HL Jr, Dyar RE.
  TITLE     Ketopantoic acid and ketopantoyl lactone reductases.
            Stereospecificity of transfer of hydrogen from reduced nicotinamide
            adenine dinucleotide phosphate.
  JOURNAL   J. Biol. Chem. 250 (1975) 2311-4.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.168
            ExPASy - ENZYME nomenclature database: 1.1.1.168
            ExplorEnz - The Enzyme Database: 1.1.1.168
            ERGO genome analysis and discovery system: 1.1.1.168
            BRENDA, the Enzyme Database: 1.1.1.168
            CAS: 37211-75-9
///
ENTRY       EC 1.1.1.169                Enzyme
NAME        2-dehydropantoate 2-reductase;
            2-oxopantoate reductase;
            2-ketopantoate reductase;
            2-ketopantoic acid reductase;
            ketopantoate reductase;
            ketopantoic acid reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-pantoate:NADP+ 2-oxidoreductase
REACTION    (R)-pantoate + NADP+ = 2-dehydropantoate + NADPH + H+ [RN:R02472]
ALL_REAC    R02472
SUBSTRATE   (R)-pantoate [CPD:C00522];
            NADP+ [CPD:C00006]
PRODUCT     2-dehydropantoate [CPD:C00966];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   King, H.L., Jr. and Wilken, D.R.
  TITLE     Ketopantoyl lactone and ketopantoic acid reductases.
            Characterization of the reactions and purification of two forms of
            ketopantoyl lactone reductase.
  JOURNAL   J. Biol. Chem. 247 (1972) 4689-4695.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], Escherichia coli [GN:eco]
PATHWAY     PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K00077  2-dehydropantoate 2-reductase
GENES       SCE: YHR063C(PAN5)
            AGO: AGOS_AAL044C
            PIC: PICST_54699(PAN5)
            CGR: CAGL0L10538g
            SPO: SPBPB2B2.09c
            AFM: AFUA_3G06390 AFUA_3G13550 AFUA_4G13960
            AOR: AO090009000600 AO090138000010 AO090138000046
            UMA: UM00283.1 UM00740.1
            ECO: b0425(apbA)
            ECJ: JW0415(panE)
            ECE: Z0528(apbA)
            ECS: ECs0479
            ECC: c0536(apbA)
            ECI: UTI89_C0448(apbA)
            ECP: ECP_0485
            ECV: APECO1_1586(apbA)
            ECW: EcE24377A_0457(panE)
            ECX: EcHS_A0497
            STY: STY0473(apbA) STY2819
            STT: t0284 t2430(apbA)
            SPT: SPA0292 SPA2289(apbA)
            SEC: SC0475(apbA) SC2568(panE)
            STM: STM0434(apbA) STM2573
            YPE: YPO3171(apbA)
            YPK: y1014(apbA)
            YPM: YP_0760(apbA)
            YPA: YPA_2665
            YPN: YPN_0917
            YPP: YPDSF_2806
            YPS: YPTB0945(panE)
            YPI: YpsIP31758_3106(panE)
            SFL: SF0362(apbA)
            SFX: S0370(apbA)
            SFV: SFV_0390(apbA)
            SSN: SSON_0402(apbA)
            SBO: SBO_0319(apbA)
            SDY: SDY_0305(apbA)
            ECA: ECA1136(panE) ECA1579
            PLU: plu3882(apbA)
            WBR: WGLp146(apbA)
            SGL: SG0661
            ENT: Ent638_0892 Ent638_2289
            SPE: Spro_1083 Spro_3174
            XCC: XCC3980(apbA)
            XCB: XC_4070
            XCV: XCV4154
            XAC: XAC4068(apbA)
            XOO: XOO0377(apbA)
            XOM: XOO_0340(XOO0340)
            VCH: VC2307
            VCO: VC0395_A1894(panE)
            VVU: VV1_1810
            VVY: VV2602
            VPA: VP2363
            VFI: VF0718 VF2526
            PPR: PBPRA0812(apbA)
            PAE: PA1752 PA4397
            PAU: PA14_41900(panE) PA14_57160(apbA)
            PAP: PSPA7_3556(panE2) PSPA7_4968(panE1)
            PPU: PP_1351 PP_2325 PP_2998
            PPF: Pput_2695 Pput_3445 Pput_4373
            PST: PSPTO_2276(panE-1) PSPTO_4394(panE-2)
            PSB: Psyr_2074 Psyr_4088
            PSP: PSPPH_2045(panE1)
            PFL: PFL_3476(panE) PFL_4271(panE) PFL_4776(panE)
            PFO: Pfl_4006 Pfl_4422
            PEN: PSEEN1893 PSEEN4470(panE)
            PMY: Pmen_0937 Pmen_2549
            SON: SO_3817(panE)
            SDN: Sden_0768 Sden_1081
            SFR: Sfri_0730 Sfri_0800
            SAZ: Sama_2559
            SBL: Sbal_0708
            SBM: Shew185_3603
            SLO: Shew_2895
            SPC: Sputcn32_0816
            SSE: Ssed_3445
            SPL: Spea_3116
            SHE: Shewmr4_3158
            SHM: Shewmr7_0809
            SHN: Shewana3_0780
            SHW: Sputw3181_3357
            ILO: IL1868(apbA)
            CPS: CPS_1095(panE)
            PHA: PSHAa2279
            PAT: Patl_1362 Patl_1772
            PIN: Ping_2262
            MAQ: Maqu_0958
            MCA: MCA2523(panE)
            HCH: HCH_00495(panE1) HCH_01927(panE2)
            CSA: Csal_2147
            ABO: ABO_0629 ABO_0967
            MMW: Mmwyl1_1818 Mmwyl1_2032
            AHA: AHA_1128(panE)
            BCI: BCI_0272(panE)
            REU: Reut_B4671 Reut_B4737 Reut_B4967
            REH: H16_A1715(apbA1) H16_B1719(apbA2) H16_B1769(apbA3)
            RME: Rmet_4356 Rmet_5770
            BMA: BMA0348(panE-1) BMA1471(panE-2) BMA2264(panE-3)
            BMV: BMASAVP1_A0561(panE-3) BMASAVP1_A0647(panE-1)
                 BMASAVP1_A1964(panE-2)
            BML: BMA10299_A2482(panE-1) BMA10299_A3341(panE-2)
            BMN: BMA10247_0095(panE-1) BMA10247_1238(panE-2)
                 BMA10247_2141(panE-3)
            BXE: Bxe_B0743 Bxe_B2259
            BVI: Bcep1808_1859 Bcep1808_4756 Bcep1808_5310 Bcep1808_5923
            BUR: Bcep18194_A5228 Bcep18194_A5870 Bcep18194_A5912
                 Bcep18194_B0882
            BCN: Bcen_1927 Bcen_1970 Bcen_3545 Bcen_5528 Bcen_5585 Bcen_6152
            BCH: Bcen2424_1927 Bcen2424_2539 Bcen2424_2581 Bcen2424_4822
                 Bcen2424_5892 Bcen2424_5949
            BAM: Bamb_1915 Bamb_2587 Bamb_2629 Bamb_4203 Bamb_5729 Bamb_6421
                 Bamb_6528
            BPS: BPSL0844 BPSL0885 BPSL1399
            BPM: BURPS1710b_1051(panE) BURPS1710b_1092(panE)
                 BURPS1710b_2487(panE)
            BPL: BURPS1106A_0892(panE) BURPS1106A_0940(panE)
                 BURPS1106A_2371(panE)
            BPD: BURPS668_0889(panE) BURPS668_0936(panE) BURPS668_2330(panE)
            BTE: BTH_I0707(panE-1) BTH_I0749(panE-2) BTH_I2115(panE-3)
            PNU: Pnuc_0191 Pnuc_1541
            BPE: BP1360
            BPA: BPP4389
            BBR: BB2814 BB4975
            POL: Bpro_0197 Bpro_0535 Bpro_2793 Bpro_2929 Bpro_4507 Bpro_5181
            PNA: Pnap_0135 Pnap_1551 Pnap_4016
            AAV: Aave_0260 Aave_1400 Aave_4737
            AJS: Ajs_3139
            VEI: Veis_3557 Veis_4655
            MPT: Mpe_A1361 Mpe_A2226
            HAR: HEAR0346
            MMS: mma_0393
            EBA: ebA232(apbA)
            AZO: azo0192(apbA1) azo1994(apbA2) azo2471(panE1) azo2607(panE2)
            DAR: Daro_1913
            ABU: Abu_2142
            NIS: NIS_0534
            GSU: GSU2683(panE)
            GME: Gmet_2643
            GUR: Gura_2230
            PPD: Ppro_2669
            DPS: DP0071
            ADE: Adeh_2159 Adeh_2270
            AFW: Anae109_2380
            MXA: MXAN_3121(panE)
            SAT: SYN_01709
            SFU: Sfum_1736 Sfum_2753
            MLO: mll6982
            RET: RHE_CH01710(ypch00569)
            RLE: RL1813
            BJA: bll3147 bll6396 blr0117 blr0589
            BRA: BRADO0328(panE)
            BBT: BBta_0313(panE)
            RPA: RPA0020(panE1) RPA1943(panE) RPA4562(apbA)
            RPB: RPB_0018 RPB_0218 RPB_3431 RPB_3888
            RPC: RPC_0016 RPC_1850
            RPD: RPD_0603 RPD_0729 RPD_2023
            RPE: RPE_0019 RPE_1954
            NWI: Nwi_0163
            NHA: Nham_0186
            XAU: Xaut_0480
            CCR: CC_0261
            SIL: SPO0966(panE-1) SPO1601(panE-2)
            RSP: RSP_1558
            RSH: Rsph17029_0211
            RSQ: Rsph17025_3040
            RDE: RD1_2198(panE)
            PDE: Pden_4530
            NAR: Saro_1677
            SWI: Swit_4927
            GBE: GbCGDNIH1_0789 GbCGDNIH1_1478
            ACR: Acry_0191 Acry_2462
            RRU: Rru_A3518
            MAG: amb1986
            MGM: Mmc1_0552
            SUS: Acid_0666
            BSU: BG13369(ylbQ)
            BHA: BH1763 BH2579(apbA)
            BAN: BA1884 BA4059
            BAR: GBAA1884 GBAA4059
            BAA: BA_2386(apbA) BA_4530(apbA)
            BAT: BAS1746 BAS3771
            BCE: BC1806 BC3920
            BCA: BCE_1964 BCE_3966
            BCZ: BCZK1696(panE) BCZK3679(panE)
            BCY: Bcer98_2570
            BTK: BT9727_1723(panE) BT9727_3662(panE)
            BTL: BALH_1660(panE)
            BLI: BL05158(panE)
            BLD: BLi01728(ylbQ)
            BCL: ABC2368
            BAY: RBAM_014180(ykpB)
            BPU: BPUM_1404(ylbQ)
            OIH: OB3273
            GKA: GK0614 GK1108
            SAU: SA2232 SA2393
            SAV: SAV2443 SAV2600
            SAM: MW2367 MW2519
            SAR: SAR2533 SAR2678
            SAS: SAS2335 SAS2485
            SAC: SACOL2448 SACOL2616
            SAB: SAB2325c SAB2473
            SAA: SAUSA300_2388(panE) SAUSA300_2535(panE)
            SAO: SAOUHSC_02739 SAOUHSC_02920
            SAJ: SaurJH9_2470 SaurJH9_2622
            SAH: SaurJH1_2518 SaurJH1_2676
            SEP: SE2009 SE2142
            SER: SERP2022 SERP2153
            SHA: SH0180 SH0615
            SSP: SSP0153 SSP0246
            LMO: lmo2046
            LMF: LMOf2365_2077(panE)
            LIN: lin2152
            LWE: lwe2060(panE)
            LLA: L157055(panE)
            LLC: LACR_1445
            LLM: llmg_1131(panE)
            SPY: SPy_0852(apbA)
            SPZ: M5005_Spy_0659(apbA)
            SPM: spyM18_0911(apbA)
            SPG: SpyM3_0577(apbA)
            SPS: SPs1277
            SPH: MGAS10270_Spy0718(apbA)
            SPI: MGAS10750_Spy0750(apbA)
            SPJ: MGAS2096_Spy0729(apbA)
            SPK: MGAS9429_Spy0714(apbA)
            SPF: SpyM51149
            SPA: M6_Spy0678
            SPB: M28_Spy0640(apbA)
            SAG: SAG1351
            SAN: gbs1421
            SAK: SAK_1382(panE)
            STC: str0092(panE)
            STL: stu0092(panE)
            LPL: lp_2532(panE1) lp_2788(panE2)
            LSA: LSA0041(panE)
            LSL: LSL_1365(apbA)
            LBR: LVIS_2138
            LCA: LSEI_1442
            LRE: Lreu_0349 Lreu_1867
            EFA: EF0517 EF1655 EF2445
            CAC: CAC2937
            CPE: CPE0786(apbA)
            CPF: CPF_0788(panE)
            CPR: CPR_0771(panE)
            CNO: NT01CX_0955(panE)
            CBO: CBO1170(panE)
            CBA: CLB_1201(panE)
            CBH: CLC_1213(panE)
            CBF: CLI_1252(panE)
            CBE: Cbei_1233 Cbei_1960
            CKL: CKL_2208
            DSY: DSY0361 DSY2000 DSY3549 DSY4724
            DRM: Dred_1323
            MTU: Rv2573
            MTC: MT2649
            MBO: Mb2603
            MPA: MAP1062c MAP4016c
            MAV: MAV_4625(panE)
            MSM: MSMEG_0153(panE) MSMEG_6374(panE)
            MMC: Mmcs_1695 Mmcs_2307
            MKM: Mkms_2354
            CGL: NCgl1044(cgl1089)
            CGB: cg1239
            CEF: CE1145
            RHA: RHA1_ro00838
            SCO: SCO0462(SCF76.02c) SCO6562(SC4B5.12c)
            SMA: SAV1833
            LXX: Lxx07200(panE)
            CMI: CMM_0370(panE) CMM_2145(apbA)
            ART: Arth_1893
            AAU: AAur_0936(panE)
            PAC: PPA0985
            FRA: Francci3_1861
            KRA: Krad_4304
            SEN: SACE_1860
            RXY: Rxyl_0382 Rxyl_2991
            RBA: RB12638(apbA) RB3312
            LIL: LA2190(panE1) LA3613(panE2)
            LIC: LIC10594(panE2) LIC11735(apbA)
            CYA: CYA_0405(panE-1) CYA_2356(panE-2)
            CYB: CYB_0856(panE-1) CYB_2432(panE-2)
            ANA: all1319
            AVA: Ava_2981
            GFO: GFO_3033(panE)
            FPS: FP1582(panE)
            RRS: RoseRS_0328 RoseRS_4344
            RCA: Rcas_0698 Rcas_0858
            AAE: aq_1727
            MMP: MMP0672
            MMZ: MmarC7_1698
            MVN: Mevan_1519
            MEM: Memar_0791 Memar_2382
            MBN: Mboo_1115
            MST: Msp_0966
            MSI: Msm_0033
            AFU: AF1695(apbA)
            HAL: VNG0730C
            HMA: rrnAC3068(panE)
            NPH: NP0942A(apbA)
            PHO: PH1390
            PAB: PAB0512(apbA)
            PFU: PF1396
            TKO: TK1968
            RCI: RCIX2330(apbA)
            APE: APE_0677.1
            SMR: Smar_1382
            PAI: PAE3409
            PIS: Pisl_1363
            PCL: Pcal_0383
            PAS: Pars_2003
STRUCTURES  PDB: 1KS9  1YJQ  1YON  2EW2  2OFP  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.169
            ExPASy - ENZYME nomenclature database: 1.1.1.169
            ExplorEnz - The Enzyme Database: 1.1.1.169
            ERGO genome analysis and discovery system: 1.1.1.169
            BRENDA, the Enzyme Database: 1.1.1.169
            CAS: 37211-74-8
///
ENTRY       EC 1.1.1.170                Enzyme
NAME        sterol-4alpha-carboxylate 3-dehydrogenase (decarboxylating);
            3beta-hydroxy-4beta-methylcholestenecarboxylate 3-dehydrogenase
            (decarboxylating);
            3beta-hydroxy-4beta-methylcholestenoate dehydrogenase;
            3beta-hydroxy-4beta-methylcholestenoate dehydrogenase;
            sterol 4alpha-carboxylic decarboxylase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate:N
            AD(P)+ 3-oxidoreductase (decarboxylating)
REACTION    3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate +
            NAD(P)+ = 4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NAD(P)H
            [RN:R04483 R07149]
ALL_REAC    R04483 R07149;
            (other) R04328 R07494
SUBSTRATE   3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate
            [CPD:C04840];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     4alpha-methyl-5alpha-cholest-7-en-3-one [CPD:C04453];
            CO2 [CPD:C00011];
            NADH [CPD:C00004];
            NADPH [CPD:C00005]
COMMENT     Also acts on 3beta-hydroxy-5alpha-cholest-7-ene-4alpha-carboxylate.
REFERENCE   1  [PMID:7430141]
  AUTHORS   Brady DR, Crowder RD, Hayes WJ.
  TITLE     Mixed function oxidases in sterol metabolism. Source of reducing
            equivalents.
  JOURNAL   J. Biol. Chem. 255 (1980) 10624-9.
REFERENCE   2  [PMID:4401584]
  AUTHORS   Rahimtula AD, Gaylor JL.
  TITLE     Partial purification of a microsomal sterol 4 -carboxylic acid
            decarboxylase.
  JOURNAL   J. Biol. Chem. 247 (1972) 9-15.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K07748  sterol-4alpha-carboxylate 3-dehydrogenase
                        (decarboxylating)
GENES       HSA: 50814(NSDHL)
            MMU: 18194(Nsdhl)
            RNO: 309262(Nsdhl)
            CFA: 481079(NSDHL)
            GGA: 422302(NSDHL)
            XLA: 496236(LOC496236)
            SPU: 577670(LOC577670)
            CME: CMP217C
            SCE: YGL001C(ERG26)
            AGO: AGOS_AFR001W
            PIC: PICST_71224(ERG26)
            SPO: SPBC3F6.02c
            ANI: AN7575.2
            AFM: AFUA_2G15030 AFUA_2G17400
            AOR: AO090120000187
            CNE: CNJ00460
            DDI: DDB_0233059
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.170
            ExPASy - ENZYME nomenclature database: 1.1.1.170
            ExplorEnz - The Enzyme Database: 1.1.1.170
            ERGO genome analysis and discovery system: 1.1.1.170
            BRENDA, the Enzyme Database: 1.1.1.170
            CAS: 71822-23-6
///
ENTRY       EC 1.1.1.171      Obsolete  Enzyme
NAME        Transferred to 1.5.1.20
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Transferred entry: now EC 1.5.1.20, methylenetetrahydrofolate
            reductase [NAD(P)H] (EC 1.1.1.171 created 1978, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.171
            ExPASy - ENZYME nomenclature database: 1.1.1.171
            ExplorEnz - The Enzyme Database: 1.1.1.171
            ERGO genome analysis and discovery system: 1.1.1.171
            BRENDA, the Enzyme Database: 1.1.1.171
///
ENTRY       EC 1.1.1.172                Enzyme
NAME        2-oxoadipate reductase;
            2-ketoadipate reductase;
            alpha-ketoadipate reductase;
            2-ketoadipate reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-hydroxyadipate:NAD+ 2-oxidoreductase
REACTION    2-hydroxyadipate + NAD+ = 2-oxoadipate + NADH + H+ [RN:R01932]
ALL_REAC    R01932
SUBSTRATE   2-hydroxyadipate [CPD:C02360];
            NAD+ [CPD:C00003]
PRODUCT     2-oxoadipate [CPD:C00322];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:185965]
  AUTHORS   Suda T, Robinson JC, Fjellstedt TA.
  TITLE     Purification and properties of alpha-ketoadipate reductase, a newly
            discovered enzyme from human placenta.
  JOURNAL   Arch. Biochem. Biophys. 176 (1976) 610-20.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.172
            ExPASy - ENZYME nomenclature database: 1.1.1.172
            ExplorEnz - The Enzyme Database: 1.1.1.172
            ERGO genome analysis and discovery system: 1.1.1.172
            BRENDA, the Enzyme Database: 1.1.1.172
            CAS: 61116-21-0
///
ENTRY       EC 1.1.1.173                Enzyme
NAME        L-rhamnose 1-dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-rhamnofuranose:NAD+ 1-oxidoreductase
REACTION    L-rhamnofuranose + NAD+ = L-rhamno-1,4-lactone + NADH + H+
            [RN:R03942]
ALL_REAC    R03942
SUBSTRATE   L-rhamnofuranose [CPD:C02431];
            NAD+ [CPD:C00003]
PRODUCT     L-rhamno-1,4-lactone [CPD:C02991];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Rigo, L.U., Marechal, L.R., Vieira, M.M. and Veiga, L.A.
  TITLE     Oxidative pathway for L-rhamnose degradation in Pallularia
            pullulans.
  JOURNAL   Can. J. Microbiol. 31 (1985) 817-822.
  ORGANISM  Pullularia pullulans
REFERENCE   2  [PMID:8142]
  AUTHORS   Rigo LU, Nakano M, Veiga LA, Feingold DS.
  TITLE     L-Rhamnose dehydrogenase of pullularia pullulans.
  JOURNAL   Biochim. Biophys. Acta. 445 (1976) 286-93.
  ORGANISM  Pullularia pullulans
PATHWAY     PATH: map00051  Fructose and mannose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.173
            ExPASy - ENZYME nomenclature database: 1.1.1.173
            ExplorEnz - The Enzyme Database: 1.1.1.173
            ERGO genome analysis and discovery system: 1.1.1.173
            BRENDA, the Enzyme Database: 1.1.1.173
            CAS: 52227-67-5
///
ENTRY       EC 1.1.1.174                Enzyme
NAME        cyclohexane-1,2-diol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     trans-cyclohexane-1,2-diol:NAD+ 1-oxidoreductase
REACTION    trans-cyclohexane-1,2-diol + NAD+ = 2-hydroxycyclohexan-1-one + NADH
            + H+ [RN:R03279]
ALL_REAC    R03279;
            (other) R03278 R06621
SUBSTRATE   trans-cyclohexane-1,2-diol [CPD:C03739];
            NAD+ [CPD:C00003]
PRODUCT     2-hydroxycyclohexan-1-one [CPD:C01147];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also oxidizes, more slowly, the cis isomer and
            2-hydroxycyclohexanone.
REFERENCE   1  [PMID:856571]
  AUTHORS   Davey JF, Trudgill PW.
  TITLE     The metabolism of trans-cyclohexan-1,2-diol by an Acinetobacter
            species.
  JOURNAL   Eur. J. Biochem. 74 (1977) 115-27.
  ORGANISM  Acinetobacter sp.
PATHWAY     PATH: map00930  Caprolactam degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.174
            ExPASy - ENZYME nomenclature database: 1.1.1.174
            ExplorEnz - The Enzyme Database: 1.1.1.174
            ERGO genome analysis and discovery system: 1.1.1.174
            BRENDA, the Enzyme Database: 1.1.1.174
            CAS: 62628-27-7
///
ENTRY       EC 1.1.1.175                Enzyme
NAME        D-xylose 1-dehydrogenase;
            NAD+-D-xylose dehydrogenase;
            D-xylose dehydrogenase;
            (NAD+)-linked D-xylose dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-xylose:NAD+ 1-oxidoreductase
REACTION    D-xylose + NAD+ = D-xylonolactone + NADH + H+ [RN:R01429]
ALL_REAC    R01429
SUBSTRATE   D-xylose [CPD:C00181];
            NAD+ [CPD:C00003]
PRODUCT     D-xylonolactone [CPD:C02266];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Yamanaka, K., Gino, M. and Kaneda, R.
  TITLE     A specific NAD-D-xylose dehydrogenase from Arthrobacter sp.
  JOURNAL   Agric. Biol. Chem. 41 (1977) 1493-1499.
  ORGANISM  Arthrobacter sp.
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.175
            ExPASy - ENZYME nomenclature database: 1.1.1.175
            ExplorEnz - The Enzyme Database: 1.1.1.175
            ERGO genome analysis and discovery system: 1.1.1.175
            BRENDA, the Enzyme Database: 1.1.1.175
            CAS: 62931-20-8
///
ENTRY       EC 1.1.1.176                Enzyme
NAME        12alpha-hydroxysteroid dehydrogenase;
            12alpha-hydroxy steroid dehydrogenase;
            12alpha-hydroxy steroid dehydrogenase;
            NAD+-dependent 12alpha-hydroxysteroid dehydrogenase;
            NADP+-12alpha-hydroxysteroid dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     12alpha-hydroxysteroid:NADP+ 12-oxidoreductase
REACTION    3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + NADP+ =
            3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate + NADPH + H+
            [RN:R02793]
ALL_REAC    R02793
SUBSTRATE   3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate [CPD:C00695];
            NADP+ [CPD:C00006]
PRODUCT     3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate [CPD:C01292];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Catalyses the oxidation of the 12alpha-hydroxy group of bile acids,
            both in their free and conjugated form. Also acts on bile alcohols.
REFERENCE   1  [PMID:201289]
  AUTHORS   MacDonald IA, Mahony DE, Jellet JF, Meier CE.
  TITLE     NAD-dependent 3alpha- and 12alpha-hydroxysteroid dehydrogenase
            activities from Eubacterium lentum ATCC no. 25559.
  JOURNAL   Biochim. Biophys. Acta. 489 (1977) 466-76.
  ORGANISM  Eubacterium lentum
REFERENCE   2  [PMID:921266]
  AUTHORS   Mahony DE, Meier CE, Macdonald IA, Holdeman LV.
  TITLE     Bile salt degradation by nonfermentative clostridia.
  JOURNAL   Appl. Environ. Microbiol. 34 (1977) 419-23.
  ORGANISM  Clostridium sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.176
            ExPASy - ENZYME nomenclature database: 1.1.1.176
            ExplorEnz - The Enzyme Database: 1.1.1.176
            ERGO genome analysis and discovery system: 1.1.1.176
            BRENDA, the Enzyme Database: 1.1.1.176
            CAS: 61642-40-8
///
ENTRY       EC 1.1.1.177                Enzyme
NAME        glycerol-3-phosphate 1-dehydrogenase (NADP+);
            glycerol phosphate (nicotinamide adenine dinucleotide phosphate)
            dehydrogenase;
            L-glycerol 3-phosphate:NADP+ oxidoreductase;
            glycerin-3-phosphate dehydrogenase;
            NADPH-dependent glycerin-3-phosphate dehydrogenase;
            glycerol-3-phosphate 1-dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     sn-glycerol-3-phosphate:NADP+ 1-oxidoreductase
REACTION    sn-glycerol 3-phosphate + NADP+ = D-glyceraldehyde 3-phosphate +
            NADPH + H+ [RN:R00845]
ALL_REAC    R00845
SUBSTRATE   sn-glycerol 3-phosphate [CPD:C00093];
            NADP+ [CPD:C00006]
PRODUCT     D-glyceraldehyde 3-phosphate [CPD:C00118];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Glushankov, P.E., Epifanova, V.E. and Kolotilova, A.I.
  TITLE     Pentose phosphate pathway of carbohydrate metabolism and
            NADP-dependent glycerol 3-phosphate dehydrogenase activity in some
            white rat tissues.
  JOURNAL   Biokhimiya 41 (1976) 1788-1790.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4152128]
  AUTHORS   Wood T.
  TITLE     Catalysis of pentose phosphate pathway reactions by cytoplasmic
            fractions from muscle, uterus and liver of the rat, and the presence
            of a reduced nicotinamide-adenine dinucleotide phosphate-triose
            phosphate oxidoreductase in rat muscle.
  JOURNAL   Biochem. J. 138 (1974) 71-6.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.177
            ExPASy - ENZYME nomenclature database: 1.1.1.177
            ExplorEnz - The Enzyme Database: 1.1.1.177
            ERGO genome analysis and discovery system: 1.1.1.177
            BRENDA, the Enzyme Database: 1.1.1.177
            CAS: 37213-46-0
///
ENTRY       EC 1.1.1.178                Enzyme
NAME        3-hydroxy-2-methylbutyryl-CoA dehydrogenase;
            2-methyl-3-hydroxybutyryl coenzyme A dehydrogenase;
            2-methyl-3-hydroxybutyryl coenzyme A dehydrogenase;
            2-methyl-3-hydroxy-butyryl CoA dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA:NAD+ oxidoreductase
REACTION    (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ =
            2-methylacetoacetyl-CoA + NADH + H+ [RN:R04203]
ALL_REAC    R04203
SUBSTRATE   (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA [CPD:C04405];
            NAD+ [CPD:C00003]
PRODUCT     2-methylacetoacetyl-CoA [CPD:C03344];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts, more slowly, on (2S,3S)-2-hydroxy-3-methylpentanoyl-CoA.
REFERENCE   1  [PMID:4150713]
  AUTHORS   Conrad RS, Massey LK, Sokatch JR.
  TITLE     D- and L-isoleucine metabolism and regulation of their pathways in
            Pseudomonas putida.
  JOURNAL   J. Bacteriol. 118 (1974) 103-11.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
ORTHOLOGY   KO: K08683  3-hydroxy-2-methylbutyryl-CoA dehydrogenase
GENES       HSA: 3028(HSD17B10)
            PTR: 465649(HSD17B10)
            MMU: 15108(Hsd17b10)
            RNO: 63864(Hadh2)
            CFA: 480930(HSD17B10)
            BTA: 281809(HADH2)
            XLA: 446903(hadh2)
            XTR: 549265(hadh2)
            DRE: 450078(hsd17b10)
            SPU: 579135(LOC579135)
            FTA: FTA_1353
            MAV: MAV_1812 MAV_2552 MAV_3936
            MSM: MSMEG_2279 MSMEG_4871
STRUCTURES  PDB: 2O23  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.178
            ExPASy - ENZYME nomenclature database: 1.1.1.178
            ExplorEnz - The Enzyme Database: 1.1.1.178
            ERGO genome analysis and discovery system: 1.1.1.178
            BRENDA, the Enzyme Database: 1.1.1.178
            CAS: 52227-66-4
///
ENTRY       EC 1.1.1.179                Enzyme
NAME        D-xylose 1-dehydrogenase (NADP+);
            D-xylose (nicotinamide adenine dinucleotide phosphate)
            dehydrogenase;
            D-xylose-NADP+ dehydrogenase;
            D-xylose:NADP+ oxidoreductase;
            D-xylose 1-dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-xylose:NADP+ 1-oxidoreductase
REACTION    D-xylose + NADP+ = D-xylono-1,5-lactone + NADPH + H+ [RN:R01430]
ALL_REAC    R01430
SUBSTRATE   D-xylose [CPD:C00181];
            NADP+ [CPD:C00006]
PRODUCT     D-xylono-1,5-lactone [CPD:C02266];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts, more slowly, on L-arabinose and D-ribose.
REFERENCE   1
  AUTHORS   Wissler, J.H.
  TITLE     D-Xylose:NADP oxidoreductase of arterial vessels and eye lens: a new
            enzyme and a final link in ATP-independent cycling of reducing
            eqivalents in aldose-polyol-ketose interconversion.
  JOURNAL   Hoppe-Seyler's Z. Physiol. Chem. 358 (1977) 1300-1301.
REFERENCE   2
  AUTHORS   Wissler, J.H.
  TITLE     Direct spectrophotometric and specific quantitative determination of
            free and bound D-xylose by analytical application of a new enzyme,
            D-xylose:NADP-oxidoreductase.
  JOURNAL   Fresenius' Z. Anal. Chem. 290 (1978) 179-180.
ORTHOLOGY   KO: K00078  D-xylose 1-dehydrogenase (NADP)
GENES       BME: BMEI2003
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.179
            ExPASy - ENZYME nomenclature database: 1.1.1.179
            ExplorEnz - The Enzyme Database: 1.1.1.179
            ERGO genome analysis and discovery system: 1.1.1.179
            BRENDA, the Enzyme Database: 1.1.1.179
            CAS: 83534-37-6
///
ENTRY       EC 1.1.1.180      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: mannonate dehydrogenase (NAD(P)+). Now included with
            EC 1.1.1.131 mannuronate reductase] (EC 1.1.1.180 created 1983,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.180
            ExPASy - ENZYME nomenclature database: 1.1.1.180
            ExplorEnz - The Enzyme Database: 1.1.1.180
            ERGO genome analysis and discovery system: 1.1.1.180
            BRENDA, the Enzyme Database: 1.1.1.180
///
ENTRY       EC 1.1.1.181                Enzyme
NAME        cholest-5-ene-3beta,7alpha-diol 3beta-dehydrogenase;
            3beta-hydroxy-Delta5-C27-steroid oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     cholest-5-ene-3beta,7alpha-diol:NAD+ 3-oxidoreductase
REACTION    cholest-5-ene-3beta,7alpha-diol + NAD+ =
            7alpha-hydroxycholest-4-en-3-one + NADH + H+ [RN:R04263]
ALL_REAC    R04263;
            (other) R04264
SUBSTRATE   cholest-5-ene-3beta,7alpha-diol [CPD:C03594];
            NAD+ [CPD:C00003]
PRODUCT     7alpha-hydroxycholest-4-en-3-one [CPD:C05455];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Highly specific for 3beta-hydroxy-C27-steroids with Delta5-double
            bond.
REFERENCE   1  [PMID:6937465]
  AUTHORS   Wikvall K.
  TITLE     Purification and properties of a 3 beta-hydroxy-delta 5-C27-steroid
            oxidoreductase from rabbit liver microsomes.
  JOURNAL   J. Biol. Chem. 256 (1981) 3376-80.
  ORGANISM  rabbit
PATHWAY     PATH: map00120  Bile acid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.181
            ExPASy - ENZYME nomenclature database: 1.1.1.181
            ExplorEnz - The Enzyme Database: 1.1.1.181
            ERGO genome analysis and discovery system: 1.1.1.181
            BRENDA, the Enzyme Database: 1.1.1.181
            CAS: 56626-16-5
///
ENTRY       EC 1.1.1.182      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: fenchol dehydrogenase. Now included with EC 1.1.1.198
            (+)-borneol dehydrogenase, EC 1.1.1.227 (-)-borneol dehydrogenase
            and EC 1.1.1.228 (+)-sabinol dehydrogenase (EC 1.1.1.182 created
            1983, deleted 1990)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.182
            ExPASy - ENZYME nomenclature database: 1.1.1.182
            ExplorEnz - The Enzyme Database: 1.1.1.182
            ERGO genome analysis and discovery system: 1.1.1.182
            BRENDA, the Enzyme Database: 1.1.1.182
///
ENTRY       EC 1.1.1.183                Enzyme
NAME        geraniol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     geraniol:NADP+ oxidoreductase
REACTION    geraniol + NADP+ = geranial + NADPH + H+ [RN:R03581]
ALL_REAC    R03581
SUBSTRATE   geraniol [CPD:C01500];
            NADP+ [CPD:C00006]
PRODUCT     geranial [CPD:C01499];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts, more slowly, on nerol, farnesol and citronellol.
REFERENCE   1
  AUTHORS   Potty, V.H. and Bruemmer, J.H.
  TITLE     Oxidation of geraniol by an enzyme system from orange.
  JOURNAL   Phytochemistry 9 (1970) 1001-1007.
  ORGANISM  orange
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.183
            ExPASy - ENZYME nomenclature database: 1.1.1.183
            ExplorEnz - The Enzyme Database: 1.1.1.183
            ERGO genome analysis and discovery system: 1.1.1.183
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.183
            BRENDA, the Enzyme Database: 1.1.1.183
            CAS: 56802-96-1
///
ENTRY       EC 1.1.1.184                Enzyme
NAME        carbonyl reductase (NADPH);
            aldehyde reductase 1;
            prostaglandin 9-ketoreductase;
            xenobiotic ketone reductase;
            NADPH-dependent carbonyl reductase;
            ALR3;
            carbonyl reductase;
            nonspecific NADPH-dependent carbonyl reductase;
            aldehyde reductase 1;
            carbonyl reductase (NADPH)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     secondary-alcohol:NADP+ oxidoreductase
REACTION    R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+ [RN:R03557]
ALL_REAC    R03557 > R02581
SUBSTRATE   R-CHOH-R' [CPD:C01612];
            NADP+ [CPD:C00006]
PRODUCT     R-CO-R' [CPD:C01450];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Acts on a wide range of carbonyl compounds, including quinones,
            aromatic aldehydes, ketoaldehydes, daunorubicin and prostaglandins E
            and F, reducing them to the corresponding alcohol. B-specific with
            respect to NADPH [cf. EC 1.1.1.2 alcohol dehydrogenase (NADP+)].
REFERENCE   1  [PMID:31888]
  AUTHORS   Ahmed NK, Felsted RL, Bachur NR.
  TITLE     Heterogeneity of anthracycline antibiotic carbonyl reductases in
            mammalian livers.
  JOURNAL   Biochem. Pharmacol. 27 (1978) 2713-9.
  ORGANISM  human [GN:hsa], rabbit, rat [GN:rno], mouse [GN:mmu]
REFERENCE   2  [PMID:666816]
  AUTHORS   Lin YM, Jarabak J.
  TITLE     Isolation of two proteins with 9-ketoprostaglandin reductase and
            NADP-linked 15-hydroxyprostaglandin dehydrogenase activities and
            studies on their inhibition.
  JOURNAL   Biochem. Biophys. Res. Commun. 81 (1978) 1227-34.
  ORGANISM  rabbit
REFERENCE   3  [PMID:7005231]
  AUTHORS   Wermuth B.
  TITLE     Purification and properties of an NADPH-dependent carbonyl reductase
            from human brain. Relationship to prostaglandin 9-ketoreductase and
            xenobiotic ketone reductase.
  JOURNAL   J. Biol. Chem. 256 (1981) 1206-13.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00590  Arachidonic acid metabolism
ORTHOLOGY   KO: K00079  carbonyl reductase (NADPH)
GENES       HSA: 10901(DHRS4) 873(CBR1) 874(CBR3)
            PTR: 452804(DHRS4)
            MMU: 109857(Cbr3) 12408(Cbr1) 12409(Cbr2) 28200(Dhrs4)
            RNO: 266686(Dhrs4) 29224(Cbr1)
            CFA: 487748(CBR3)
            BTA: 281360(NDRD)
            SSC: 396780(CR) 397082(DHRS4) 397143(CBR1)
            GGA: 426247(DHRS2)
            XLA: 444771(MGC81922)
            DRE: 393539(zgc:65987)
            SPU: 578300(LOC578300)
            DME: Dmel_CG10672 Dmel_CG10964(sni) Dmel_CG1386(antdh)
            CEL: F36H9.3(dhs-13) R11D1.11(dhs-21)
            ATH: AT4G05530
            OSA: 4346459
            PIC: PICST_38255(SOU1) PICST_65696(ARD2) PICST_86346(SOU2)
            TET: TTHERM_00011540
            RSO: RS05193(RSp0230)
            BUR: Bcep18194_A3706 Bcep18194_A6271 Bcep18194_B0709
                 Bcep18194_B0889 Bcep18194_B1491 Bcep18194_B3037
                 Bcep18194_C6897
            BPM: BURPS1710b_A0944
            RET: RHE_PA00027 RHE_PE00179
            RLE: RL0917
            BME: BMEII0062
            BRA: BRADO0986 BRADO2145(fixR1) BRADO2932
            BBT: BBta_2462(fixR1) BBta_5938 BBta_7068
            NWI: Nwi_2662
            RDE: RD1_2866
            RRU: Rru_A1945
            LLM: llmg_0154(cbr)
            MSM: MSMEG_1740 MSMEG_5383
            AVA: Ava_0980 Ava_2801
            CCH: Cag_1642
STRUCTURES  PDB: 1CYD  1WMA  2HRB  2PFG  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.184
            ExPASy - ENZYME nomenclature database: 1.1.1.184
            ExplorEnz - The Enzyme Database: 1.1.1.184
            ERGO genome analysis and discovery system: 1.1.1.184
            BRENDA, the Enzyme Database: 1.1.1.184
            CAS: 89700-36-7
///
ENTRY       EC 1.1.1.185                Enzyme
NAME        L-glycol dehydrogenase;
            glycol (nicotinamide adenine dinucleotide (phosphate))
            dehydrogenase;
            L-(+)-glycol:NAD(P)+ oxidoreductase;
            L-glycol:NAD(P)+ dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-glycol:NAD(P)+ oxidoreductase
REACTION    an L-glycol + NAD(P)+ = a 2-hydroxycarbonyl compound + NAD(P)H + H+
            [RN:R03584 R03585]
ALL_REAC    R03584 R03585
SUBSTRATE   L-glycol [CPD:C01506];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     2-hydroxycarbonyl compound [CPD:C03667];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The 2-hydroxycarbonyl compound formed can be further oxidized to a
            vicinal dicarbonyl compound. In the reverse direction, vicinal
            diketones, glyceraldehyde, glyoxal, methylglyoxal,
            2-oxo-hydroxyketones and 2-ketoacid esters can be reduced.
REFERENCE   1  [PMID:7018582]
  AUTHORS   Bernardo A, Burgos J, Martin R.
  TITLE     Purification and some properties of L-glycol dehydrogenase from
            hen's muscle.
  JOURNAL   Biochim. Biophys. Acta. 659 (1981) 189-98.
  ORGANISM  chicken [GN:gga]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.185
            ExPASy - ENZYME nomenclature database: 1.1.1.185
            ExplorEnz - The Enzyme Database: 1.1.1.185
            ERGO genome analysis and discovery system: 1.1.1.185
            BRENDA, the Enzyme Database: 1.1.1.185
            CAS: 77967-75-0
///
ENTRY       EC 1.1.1.186                Enzyme
NAME        dTDP-galactose 6-dehydrogenase;
            thymidine-diphosphate-galactose dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     dTDP-D-galactose:NADP+ 6-oxidoreductase
REACTION    dTDP-D-galactose + 2 NADP+ + H2O = dTDP-D-galacturonate + 2 NADPH +
            2 H+ [RN:R07150]
ALL_REAC    R07150;
            (other) R03826
SUBSTRATE   dTDP-D-galactose [CPD:C02097];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     dTDP-D-galacturonate [CPD:C03034];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4381717]
  AUTHORS   Katan R, Avigad G.
  TITLE     NADP dependent oxidation of TDP-glucose by an enzyme system from
            sugar beets.
  JOURNAL   Biochem. Biophys. Res. Commun. 24 (1966) 18-24.
  ORGANISM  Beta vulgaris
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.186
            ExPASy - ENZYME nomenclature database: 1.1.1.186
            ExplorEnz - The Enzyme Database: 1.1.1.186
            ERGO genome analysis and discovery system: 1.1.1.186
            BRENDA, the Enzyme Database: 1.1.1.186
///
ENTRY       EC 1.1.1.187                Enzyme
NAME        GDP-4-dehydro-D-rhamnose reductase;
            GDP-4-keto-6-deoxy-D-mannose reductase;
            GDP-4-keto-D-rhamnose reductase;
            guanosine diphosphate-4-keto-D-rhamnose reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     GDP-6-deoxy-D-mannose:NAD(P)+ 4-oxidoreductase
REACTION    GDP-6-deoxy-D-mannose + NAD(P)+ = GDP-4-dehydro-6-deoxy-D-mannose +
            NAD(P)H + H+ [RN:R03397 R03399]
ALL_REAC    R03397 R03399
SUBSTRATE   GDP-6-deoxy-D-mannose [CPD:C03117];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     GDP-4-dehydro-6-deoxy-D-mannose [CPD:C01222];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     In the reverse reaction, a mixture of GDP-D-rhamnose and its C-4
            epimer is formed.
REFERENCE   1  [PMID:4386238]
  AUTHORS   Barber GA.
  TITLE     The synthesis of guanosine 5'-diphosphate D-rhamnose by enzymes of a
            higher plant.
  JOURNAL   Biochim. Biophys. Acta. 165 (1968) 68-75.
  ORGANISM  Leucaena glauca
REFERENCE   2  [PMID:4398966]
  AUTHORS   Winkler NW, Markovitz A.
  TITLE     Guanosine diphosphate-4-keto-D-rhamnose reductase. A
            non-stereoselective enzyme.
  JOURNAL   J. Biol. Chem. 246 (1971) 5868-76.
  ORGANISM  soil bacterium GS
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K00080  GDP-4-dehydro-D-rhamnose reductase
GENES       FPS: FP1641(rmd)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.187
            ExPASy - ENZYME nomenclature database: 1.1.1.187
            ExplorEnz - The Enzyme Database: 1.1.1.187
            ERGO genome analysis and discovery system: 1.1.1.187
            BRENDA, the Enzyme Database: 1.1.1.187
            CAS: 9075-56-3
///
ENTRY       EC 1.1.1.188                Enzyme
NAME        prostaglandin-F synthase;
            prostaglandin-D2 11-reductase;
            reductase, 15-hydroxy-11-oxoprostaglandin;
            PGD2 11-ketoreductase;
            PGF2alpha synthetase;
            prostaglandin 11-ketoreductase;
            prostaglandin D2-ketoreductase;
            prostaglandin F synthase;
            prostaglandin F synthetase;
            synthetase, prostaglandin F2alpha;
            prostaglandin-D2 11-reductase;
            PGF synthetase;
            NADPH-dependent prostaglandin D2 11-keto reductase;
            prostaglandin 11-keto reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate:NADP
            + 11-oxidoreductase
REACTION    (5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate +
            NADP+ =
            (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate +
            NADPH + H+ [RN:R02684]
ALL_REAC    R02684;
            (other) R02799
SUBSTRATE   (5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate
            [CPD:C00639];
            NADP+ [CPD:C00006]
PRODUCT     (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
            [CPD:C00696];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Reduces prostaglandin D2 and prostaglandin H2 to prostaglandin F2;
            prostaglandin D2 is not an intermediate in the reduction of
            prostaglandin H2. Also catalyses the reduction of a number of
            carbonyl compounds, such as 9,10-phenanthroquinone and
            4-nitroacetophenone.
REFERENCE   1  [PMID:7248318]
  AUTHORS   Reingold DF, Kawasaki A, Needleman P.
  TITLE     A novel prostaglandin 11-keto reductase found in rabbit liver.
  JOURNAL   Biochim. Biophys. Acta. 659 (1981) 179-88.
  ORGANISM  rabbit
REFERENCE   2
  AUTHORS   Watanabe, K., Shimizu, T. and Hayaishi, O.
  TITLE     Enzymatic conversion of prostaglandin-D2 to prostaglandin-F2alpha in
            the rat lung.
  JOURNAL   Biochem. Int. 2 (1981) 603-610.
REFERENCE   3  [PMID:3858278]
  AUTHORS   Watanabe K, Yoshida R, Shimizu T, Hayaishi O.
  TITLE     Enzymatic formation of prostaglandin F2 alpha from prostaglandin H2
            and D2. Purification and properties of prostaglandin F synthetase
            from bovine lung.
  JOURNAL   J. Biol. Chem. 260 (1985) 7035-41.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:7248317]
  AUTHORS   Wong PY.
  TITLE     Purification and partial characterization of prostaglandin D2
            11-keto reductase in rabbit liver.
  JOURNAL   Biochim. Biophys. Acta. 659 (1981) 169-78.
  ORGANISM  rabbit
REFERENCE   5  [PMID:7132748]
  AUTHORS   Wong PY.
  TITLE     Purification of PGD2 11-ketoreductase from rabbit liver.
  JOURNAL   Methods. Enzymol. 86 (1982) 117-25.
  ORGANISM  rabbit
PATHWAY     PATH: map00590  Arachidonic acid metabolism
ORTHOLOGY   KO: K04119  prostaglandin-F synthase
GENES       HSA: 8644(AKR1C3)
STRUCTURES  PDB: 1RY0  1RY8  1VBJ  1XF0  1ZQ5  2F38  2FGB  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.188
            ExPASy - ENZYME nomenclature database: 1.1.1.188
            ExplorEnz - The Enzyme Database: 1.1.1.188
            ERGO genome analysis and discovery system: 1.1.1.188
            BRENDA, the Enzyme Database: 1.1.1.188
            CAS: 55976-95-9
///
ENTRY       EC 1.1.1.189                Enzyme
NAME        prostaglandin-E2 9-reductase;
            PGE2-9-OR;
            reductase, 15-hydroxy-9-oxoprostaglandin;
            9-keto-prostaglandin E2 reductase;
            9-ketoprostaglandin reductase;
            PGE-9-ketoreductase;
            PGE2 9-oxoreductase;
            PGE2-9-ketoreductase;
            prostaglandin 9-ketoreductase;
            prostaglandin E 9-ketoreductase;
            prostaglandin E2-9-oxoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate:NADP
            + 9-oxidoreductase
REACTION    (5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate +
            NADP+ =
            (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate +
            NADPH + H+ [RN:R02581]
ALL_REAC    R02581
SUBSTRATE   (5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate
            [CPD:C00639];
            NADP+ [CPD:C00006]
PRODUCT     (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate
            [CPD:C00584];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Reduces prostaglandin E2 to prostaglandin F2alpha. A number of other
            9-oxo- and 15-oxo-prostaglandin derivatives can also be reduced to
            the corresponding hydroxy compounds. May be identical with EC
            1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+).
REFERENCE   1  [PMID:166995]
  AUTHORS   Lee SC, Levine L.
  TITLE     Purification and regulatory properties of chicken heart
            prostaglandin E 9-ketoreductase.
  JOURNAL   J. Biol. Chem. 250 (1975) 4549-55.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:6586494]
  AUTHORS   Schlegel W, Kruger S, Korte K.
  TITLE     Purification of prostaglandin E2-9-oxoreductase from human decidua
            vera.
  JOURNAL   FEBS. Lett. 171 (1984) 141-4.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:7132747]
  AUTHORS   Tai HH, Yuan B.
  TITLE     Purification and assay of 9-hydroxyprostaglandin dehydrogenase from
            rat kidney.
  JOURNAL   Methods. Enzymol. 86 (1982) 113-7.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:3901124]
  AUTHORS   Watkins JD, Jarabak J.
  TITLE     The effect of NaCl intake on 9-ketoprostaglandin reductase activity
            in the rabbit kidney.
  JOURNAL   Prostaglandins. 30 (1985) 335-49.
  ORGANISM  rabbit
PATHWAY     PATH: map00590  Arachidonic acid metabolism
ORTHOLOGY   KO: K00081  prostaglandin-E2 9-reductase
GENES       HSA: 873(CBR1)
            SSC: 397143(CBR1)
            TET: TTHERM_00107090 TTHERM_00107100 TTHERM_00927240
                 TTHERM_00927250 TTHERM_01085680
STRUCTURES  PDB: 1Q13  1Q5M  2PFG  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.189
            ExPASy - ENZYME nomenclature database: 1.1.1.189
            ExplorEnz - The Enzyme Database: 1.1.1.189
            ERGO genome analysis and discovery system: 1.1.1.189
            BRENDA, the Enzyme Database: 1.1.1.189
            CAS: 42613-35-4
///
ENTRY       EC 1.1.1.190                Enzyme
NAME        indole-3-acetaldehyde reductase (NADH);
            indoleacetaldehyde reductase;
            indole-3-acetaldehyde reductase (NADH);
            indole-3-ethanol:NAD+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (indol-3-yl)ethanol:NAD+ oxidoreductase
REACTION    (indol-3-yl)ethanol + NAD+ = (indol-3-yl)acetaldehyde + NADH + H+
            [RN:R02679]
ALL_REAC    R02679
SUBSTRATE   (indol-3-yl)ethanol;
            NAD+ [CPD:C00003]
PRODUCT     (indol-3-yl)acetaldehyde;
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:2607]
  AUTHORS   Brown HM, Purves WK.
  TITLE     Isolation and characterization of indole-3-acetaldehyde reductases
            from Cucumis sativus.
  JOURNAL   J. Biol. Chem. 251 (1976) 907-13.
  ORGANISM  Cucumis sativus
PATHWAY     PATH: map00380  Tryptophan metabolism
GENES       PMB: A9601_14521(adhC) A9601_14641
            PMC: P9515_14261
            PMF: P9303_19231
            PMG: P9301_14501
            PME: NATL1_16841
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.190
            ExPASy - ENZYME nomenclature database: 1.1.1.190
            ExplorEnz - The Enzyme Database: 1.1.1.190
            ERGO genome analysis and discovery system: 1.1.1.190
            BRENDA, the Enzyme Database: 1.1.1.190
            CAS: 58875-06-2
///
ENTRY       EC 1.1.1.191                Enzyme
NAME        indole-3-acetaldehyde reductase (NADPH);
            indoleacetaldehyde (reduced nicotinamide adenine dinucleotide
            phosphate) reductase;
            indole-3-acetaldehyde reductase (NADPH);
            indole-3-ethanol:NADP+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (indol-3-yl)ethanol:NADP+ oxidoreductase
REACTION    (indol-3-yl)ethanol + NADP+ = (indol-3-yl)acetaldehyde + NADPH + H+
            [RN:R02680]
ALL_REAC    R02680
SUBSTRATE   (indol-3-yl)ethanol;
            NADP+ [CPD:C00006]
PRODUCT     (indol-3-yl)acetaldehyde;
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:2607]
  AUTHORS   Brown HM, Purves WK.
  TITLE     Isolation and characterization of indole-3-acetaldehyde reductases
            from Cucumis sativus.
  JOURNAL   J. Biol. Chem. 251 (1976) 907-13.
  ORGANISM  Cucumis sativus
PATHWAY     PATH: map00380  Tryptophan metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.191
            ExPASy - ENZYME nomenclature database: 1.1.1.191
            ExplorEnz - The Enzyme Database: 1.1.1.191
            ERGO genome analysis and discovery system: 1.1.1.191
            BRENDA, the Enzyme Database: 1.1.1.191
            CAS: 58875-05-1
///
ENTRY       EC 1.1.1.192                Enzyme
NAME        long-chain-alcohol dehydrogenase;
            long-chain alcohol dehydrogenase;
            fatty alcohol oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     long-chain-alcohol:NAD+ oxidoreductase
REACTION    a long-chain alcohol + 2 NAD+ + H2O = a long-chain carboxylate + 2
            NADH + 2 H+ [RN:R01998]
ALL_REAC    R01998;
            (other) R02462
SUBSTRATE   long-chain alcohol [CPD:C00339];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     long-chain carboxylate [CPD:C00347];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Hexadecanol is a good substrate.
REFERENCE   1  [PMID:34610]
  AUTHORS   Lee T.
  TITLE     Characterization of fatty alcohol:NAD+ oxidoreductase from rat
            liver.
  JOURNAL   J. Biol. Chem. 254 (1979) 2892-6.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00071  Fatty acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.192
            ExPASy - ENZYME nomenclature database: 1.1.1.192
            ExplorEnz - The Enzyme Database: 1.1.1.192
            ERGO genome analysis and discovery system: 1.1.1.192
            BRENDA, the Enzyme Database: 1.1.1.192
            CAS: 76774-36-2
///
ENTRY       EC 1.1.1.193                Enzyme
NAME        5-amino-6-(5-phosphoribosylamino)uracil reductase;
            aminodioxyphosphoribosylaminopyrimidine reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     5-amino-6-(5-phosphoribitylamino)uracil:NADP+ 1'-oxidoreductase
REACTION    5-amino-6-(5-phosphoribitylamino)uracil + NADP+ =
            5-amino-6-(5-phosphoribosylamino)uracil + NADPH + H+ [RN:R03458]
ALL_REAC    R03458
SUBSTRATE   5-amino-6-(5-phosphoribitylamino)uracil [CPD:C04454];
            NADP+ [CPD:C00006]
PRODUCT     5-amino-6-(5-phosphoribosylamino)uracil [CPD:C01268];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:30756]
  AUTHORS   Burrows RB, Brown GM.
  TITLE     Presence of Escherichia coli of a deaminase and a reductase involved
            in biosynthesis of riboflavin.
  JOURNAL   J. Bacteriol. 136 (1978) 657-67.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00740  Riboflavin metabolism
ORTHOLOGY   KO: K00082  5-amino-6-(5-phosphoribosylamino)uracil reductase
GENES       ATH: AT3G47390 AT4G20960
            OSA: 4329349 4331409 4335087
            CME: CMQ053C CMS352C
            SCE: YBR153W(RIB7)
            AGO: AGOS_AER037C
            PIC: PICST_53707
            CGR: CAGL0F05203g
            SPO: SPBC21C3.10c
            ANI: AN6979.2
            AFM: AFUA_4G04730
            AOR: AO090206000013
            ECO: b0414(ribD)
            ECJ: JW0404(ribD)
            ECE: Z0515(ribD)
            ECS: ECs0467
            ECC: c0524(ribD)
            ECI: UTI89_C0436(ribD)
            ECP: ECP_0473
            ECV: APECO1_1596(ribD)
            ECW: EcE24377A_0445(ribD)
            ECX: EcHS_A0485(ribD)
            STY: STY0455(ribD)
            STT: t2447(ribD)
            SPT: SPA2307(ribD)
            SEC: SC0457(ribD)
            STM: STM0416(ribD)
            YPE: YPO3183(ribD)
            YPK: y1000(ribD)
            YPM: YP_0748(ribD)
            YPA: YPA_2677
            YPN: YPN_0905
            YPP: YPDSF_2818
            YPS: YPTB0934(ribD)
            YPI: YpsIP31758_3117(ribD)
            SFL: SF0351(ribD)
            SFX: S0359(ribD)
            SFV: SFV_0379(ribD)
            SSN: SSON_0391(ribD)
            SDY: SDY_0320(ribD)
            ECA: ECA1126(ribD)
            PLU: plu3899(ribD)
            BUC: BU462(ribD2)
            BAS: BUsg446(ribD2)
            BAB: bbp408(ribD)
            WBR: WGLp462(ribD)
            SGL: SG0651
            ENT: Ent638_0882
            SPE: Spro_1072
            BFL: Bfl234(ribD)
            BPN: BPEN_240(ribD)
            HIN: HI0944(ribD)
            HIT: NTHI1115(ribD)
            HDU: HD1161(ribD)
            HSO: HS_1050(ribD)
            PMU: PM0749(ribD)
            MSU: MS1374(ribD)
            APL: APL_0382(ribD)
            ASU: Asuc_1368
            XFA: XF0950
            XFT: PD1747(ribD)
            XCC: XCC0693(ribD)
            XCB: XC_3541
            XCV: XCV0798(ribD)
            XAC: XAC0746(ribD)
            XOO: XOO3856(ribD)
            XOM: XOO_3635(XOO3635)
            VCH: VC2271
            VCO: VC0395_A1861(ribD)
            VVU: VV1_0323
            VVY: VV0861
            VPA: VP0679
            VFI: VF0700
            PPR: PBPRA0797
            PAE: PA4056(ribD)
            PAP: PSPA7_1045(ribD)
            PPU: PP_0514(ribD)
            PPF: Pput_0549
            PST: PSPTO_0690(ribD)
            PSB: Psyr_4462
            PSP: PSPPH_3758 PSPPH_4507(ribD)
            PFL: PFL_1032(ribD) PFL_5522(ribD)
            PFO: Pfl_5019(ribD)
            PEN: PSEEN0588(ribD)
            PMY: Pmen_3857
            PAR: Psyc_2141(ribD)
            PCR: Pcryo_2470
            PRW: PsycPRwf_2385
            ACI: ACIAD0247(ribD)
            SON: SO_3469(ribD)
            SDN: Sden_1144
            SFR: Sfri_1035
            SAZ: Sama_1016
            SBL: Sbal_3160
            SBM: Shew185_3159
            SLO: Shew_1187
            SPC: Sputcn32_2778
            SSE: Ssed_1273
            SPL: Spea_1162
            SHE: Shewmr4_1096
            SHM: Shewmr7_1162
            SHN: Shewana3_1096
            SHW: Sputw3181_1234
            ILO: IL1870(ribD)
            CPS: CPS_0730(ribD)
            PHA: PSHAa2374(ribD)
            PAT: Patl_1311
            SDE: Sde_3458
            PIN: Ping_1440
            MAQ: Maqu_0843
            CBU: CBU_0643(ribD)
            CBD: COXBU7E912_0655(ribD)
            LPN: lpg1177(ribD)
            LPF: lpl1186(ribD)
            LPP: lpp1180(ribD)
            MCA: MCA1658(ribD)
            FTU: FTT1671(ribD)
            FTF: FTF1671(ribD)
            FTW: FTW_1946(ribD)
            FTL: FTL_0078
            FTH: FTH_0074(ribD)
            FTA: FTA_0086(ribD)
            FTN: FTN_0114(ribD)
            TCX: Tcr_1400
            NOC: Noc_1079 Noc_2025
            AEH: Mlg_0375
            HHA: Hhal_0900
            HCH: HCH_05957(ribD)
            CSA: Csal_2585
            ABO: ABO_2174(ribD)
            AHA: AHA_3333(ribD)
            DNO: DNO_0474(ribD)
            BCI: BCI_0601(ribD)
            RMA: Rmag_0800
            VOK: COSY_0726(ribD)
            NME: NMB1817
            NMA: NMA0644(ribD)
            NMC: NMC0403(ribD)
            NGO: NGO0089
            CVI: CV_1290(ribD)
            RSO: RSc0715(ribD)
            REU: Reut_A0776
            REH: H16_A2848(ribD)
            RME: Rmet_2688
            BMA: BMA2143(ribD)
            BMV: BMASAVP1_A0767(ribD)
            BML: BMA10299_A2600(ribD)
            BMN: BMA10247_2013(ribD)
            BXE: Bxe_A0895
            BVI: Bcep1808_0877
            BUR: Bcep18194_A4064
            BCN: Bcen_0481
            BCH: Bcen2424_0960
            BAM: Bamb_0821
            BPS: BPSL2624(ribD) BPSS1125
            BPM: BURPS1710b_3100(ribD) BURPS1710b_A0085(ribD)
            BPL: BURPS1106A_3065(ribD) BURPS1106A_A1505(ribD)
            BPD: BURPS668_3012(ribD) BURPS668_A1588(ribD)
            BTE: BTH_I1542(ribD-1) BTH_II1281(ribD-2)
            PNU: Pnuc_0270
            BPE: BP2948
            BPA: BPP3871
            BBR: BB4344
            RFR: Rfer_2666
            POL: Bpro_2883
            PNA: Pnap_2915
            AAV: Aave_3555
            AJS: Ajs_3190
            VEI: Veis_2821
            MPT: Mpe_A2945
            HAR: HEAR2372(ribD)
            MMS: mma_2434(ribD)
            NEU: NE0793(ribD)
            NET: Neut_1091
            NMU: Nmul_A0006
            DAR: Daro_0605
            TBD: Tbd_2168
            MFA: Mfla_1915
            HPY: HP1505(ribG)
            HPJ: jhp1398(ribD)
            HPA: HPAG1_1407
            HHE: HH0838(ribD)
            HAC: Hac_0079(ribD)
            WSU: WS2019(ribD)
            TDN: Tmden_0679
            CJE: Cj1622(ribD)
            CJR: CJE1794
            CJJ: CJJ81176_1613(ribD)
            CJU: C8J_1524(ribD)
            CFF: CFF8240_1488(ribD)
            CCV: CCV52592_0359(ribD)
            CHA: CHAB381_0131(ribD)
            CCO: CCC13826_1500(ribD)
            ABU: Abu_2046(ribD)
            NIS: NIS_0424
            SUN: SUN_1968
            GSU: GSU1688(ribD)
            GME: Gmet_1624(ribD)
            PCA: Pcar_1445(ribD)
            PPD: Ppro_1596
            DVU: DVU1201(ribD)
            DDE: Dde_2434
            LIP: LI0157(ribD)
            BBA: Bd3542(ribD)
            DPS: DP2785(ribD)
            ADE: Adeh_2742
            AFW: Anae109_2731
            MXA: MXAN_4764(ribD)
            SAT: SYN_00578
            SFU: Sfum_1378
            WOL: WD0710(ribD)
            WBM: Wbm0026
            AMA: AM015(ribD)
            APH: APH_0037(ribD)
            ERU: Erum1140(ribD)
            ERW: ERWE_CDS_01110(ribD)
            ERG: ERGA_CDS_01070(ribD)
            ECN: Ecaj_0112
            ECH: ECH_0169(ribD)
            NSE: NSE_0499(ribD)
            PUB: SAR11_1046(ribD)
            MLO: mlr8405
            MES: Meso_1136
            PLA: Plav_2910
            SME: SMc01772(ribD)
            ATU: Atu1167(ribD*) Atu1168(ribD*)
            ATC: AGR_C_2159
            RET: RHE_CH01510(ribD) RHE_PD00036(ypd00011)
            RLE: RL1621(ribD) pRL110171
            BME: BMEI1189
            BMF: BAB1_0789(ribD)
            BMS: BR0767(ribD)
            BMB: BruAb1_0783(ribD)
            BOV: BOV_0760(ribD)
            BJA: bll5031(ribD)
            BRA: BRADO2375 BRADO4428(ribD)
            BBT: BBta_2727 BBta_4647(ribD)
            RPA: RPA2726(ribD)
            RPB: RPB_2636
            RPC: RPC_2661
            RPD: RPD_2673
            RPE: RPE_2810
            NWI: Nwi_1725
            NHA: Nham_1816
            BHE: BH07560(ribD)
            BQU: BQ05410(ribD)
            BBK: BARBAKC583_0631(ribD)
            CCR: CC_0885(ribD)
            SIL: SPO1754(ribD)
            SIT: TM1040_2135
            RSP: RSP_0393
            RSQ: Rsph17025_0844
            JAN: Jann_3421
            RDE: RD1_1799(ribD)
            ZMO: ZMO0476(ribD)
            NAR: Saro_2857
            SAL: Sala_2991
            ELI: ELI_00150
            GOX: GOX0978(ribD)
            RRU: Rru_A1825
            MAG: amb2341
            MGM: Mmc1_0168
            ABA: Acid345_3337
            SUS: Acid_4222
            BSU: BG10518(ribG)
            BHA: BH1554(ribG)
            BAN: BA4331(ribD)
            BAR: GBAA4331(ribD)
            BAA: BA_4789
            BAT: BAS4018(ribD)
            BCE: BC3387 BC4109
            BCA: BCE_4179(ribD)
            BCZ: BCZK3096(ribD) BCZK3865(ribD)
            BCY: Bcer98_2808
            BTK: BT9727_3851(ribD)
            BLI: BL01891(ribD)
            BLD: BLi02475(ribD)
            BCL: ABC3987(ribG)
            BPU: BPUM_0703(ribD2) BPUM_3532(ribD1)
            OIH: OB0423
            GKA: GK2297
            SAU: SA1589(ribD)
            SAV: SAV1771(ribD)
            SAM: MW1711(ribD)
            SAR: SAR1853(ribD)
            SAS: SAS1694
            SAC: SACOL1820(ribD)
            SAB: SAB1628c(ribD)
            SAA: SAUSA300_1715(ribD)
            SAO: SAOUHSC_01889
            SEP: SE1441
            SER: SERP1328(ribD)
            SHA: SH1153(ribD)
            SSP: SSP0995
            LLA: L0163(ribG)
            LLM: llmg_1532(ribD)
            SPN: SP_0178
            SPR: spr0164(ribD)
            SPD: SPD_0169(ribD)
            SAG: SAG0746(ribD)
            SAN: gbs0767
            SAK: SAK_0872(ribD)
            LBR: LVIS_1653
            CAC: CAC0590(ribD)
            CPE: CPE0566(ribB)
            CPF: CPF_0546(ribD)
            CPR: CPR_0530(ribD)
            CTC: CTC00671
            CTH: Cthe_0104
            CDF: CD1700(ribD)
            CBO: CBO2866(ribD)
            CBA: CLB_2832(ribD)
            CBH: CLC_2765(ribD)
            CBF: CLI_2922(ribD)
            CHY: CHY_1475(ribD)
            DSY: DSY1662(ribD)
            DRM: Dred_2093
            SWO: Swol_1222
            MTA: Moth_0915
            MTU: Rv1409(ribG) Rv2671(ribD)
            MTC: MT1453(ribD) MT2745
            MBO: Mb1444(ribG) Mb2690(ribD)
            MBB: BCG_1470(ribG) BCG_2684(ribD)
            MLE: ML0555(ribG) ML1340
            MPA: MAP1136(ribG) MAP2791(ribD)
            MAV: MAV_3368(ribD)
            MSM: MSMEG_3067(ribD)
            MVA: Mvan_2690
            MGI: Mflv_3727
            MMC: Mmcs_2386
            MKM: Mkms_2433
            MJL: Mjls_2427
            CGL: NCgl1535(cgl1597)
            CGB: cg1800(ribG)
            CEF: CE1716(ribD)
            CDI: DIP1319(ribD)
            CJK: jk1010(ribD)
            NFA: nfa33100 nfa37320 nfa780
            RHA: RHA1_ro06865 RHA1_ro07168(ribD)
            SCO: SCO2688(ribD) SCO4106(SCD17.10) SCO6058(SC9B1.05)
            SMA: SAP1p36 SAV2208 SAV4119(ribG)
            TWH: TWT392(ribD) TWT687(ribG)
            TWS: TW706(ribD)
            LXX: Lxx04370(ribD)
            CMI: CMM_0963(ribD)
            PAC: PPA1752
            NCA: Noca_2447
            TFU: Tfu_0876
            FRA: Francci3_1181
            FAL: FRAAL1884 FRAAL2113(ribD)
            ACE: Acel_1274
            KRA: Krad_0126
            SEN: SACE_1871(ribD) SACE_2121(ribG) SACE_2887(ribD)
            STP: Strop_1874
            RXY: Rxyl_1364 Rxyl_2578
            FNU: FN1506
            RBA: RB6126(ribD)
            CTR: CT730(ribD)
            CTA: CTA_0792(ribD)
            CMU: TC0103
            CPN: CPn0871(ribD)
            CPA: CP0998
            CPJ: CPj0871(ribD)
            CPT: CpB0900
            CCA: CCA00896(ribD)
            CAB: CAB864(ribD)
            CFE: CF0118(ribD)
            PCU: pc1042(ribD)
            LIL: LA1144(ribD1) LA4019(ribD2)
            LIC: LIC12536(ribD)
            LBJ: LBJ_2152(ribD)
            LBL: LBL_2146(ribD)
            SYN: slr0066(ribD)
            SYW: SYNW1590(ribD) SYNW2200
            SYC: syc0364_c(ribG) syc1308_d(ribD)
            SYF: Synpcc7942_0203 Synpcc7942_1186
            SYD: Syncc9605_0922 Syncc9605_2343
            SYE: Syncc9902_0348 Syncc9902_1486
            SYG: sync_0821(ribD) sync_2555
            SYR: SynRCC307_1751(ribD)
            SYX: SynWH7803_1692(ribD)
            CYA: CYA_0386(ribD) CYA_1389
            CYB: CYB_1847(ribD) CYB_2564
            TEL: tlr2152(ribD)
            GVI: gll1250(ribD) glr3534
            ANA: all0082(ribD) all4103(ribG)
            AVA: Ava_0803 Ava_1457
            PMA: Pro0126(ribD) Pro1339(ribD)
            PMM: PMM0105(ribG) PMM1265(ribD)
            PMT: PMT0165(ribG) PMT0375(ribD)
            PMN: PMN2A_0831 PMN2A_1474
            PMI: PMT9312_0109 PMT9312_1359
            PMB: A9601_01221 A9601_14641
            PMC: P9515_01181 P9515_14261
            PMF: P9303_02071 P9303_19231
            PMG: P9301_01211 P9301_14501
            PMH: P9215_14901(ribD)
            PME: NATL1_01771 NATL1_16841
            TER: Tery_1661
            BTH: BT_3728(ribD)
            BFR: BF0507(ribD)
            BFS: BF0452
            PGI: PG0155(ribD)
            SRU: SRU_2302(ribD)
            CHU: CHU_0203(ribD)
            FPS: FP2025(ribD)
            CTE: CT0747(ribD)
            CCH: Cag_0623
            CPH: Cpha266_0944
            PVI: Cvib_1105
            PLT: Plut_0727
            DET: DET1190(ribD)
            DEH: cbdb_A1105(ribD)
            DEB: DehaBAV1_1001
            DRA: DR_0153
            DGE: Dgeo_0300
            TTH: TTC0699(ribD)
            TTJ: TTHA1064
            AAE: aq_138(ribD1) aq_436(ribD2)
            TMA: TM1828
            MJA: MJ0671
            MMQ: MmarC5_0230
            MMZ: MmarC7_0593
            MAE: Maeo_0660
            MVN: Mevan_0659
            MAC: MA4092(ribD) MA4367(ribD)
            MBA: Mbar_A0489 Mbar_A1048
            MMA: MM_0826 MM_1058
            MBU: Mbur_2352
            MTP: Mthe_0604
            MHU: Mhun_0807 Mhun_2575
            MEM: Memar_1398 Memar_2026
            MBN: Mboo_0804 Mboo_0908
            MTH: MTH235
            MST: Msp_1185
            MSI: Msm_0065
            MKA: MK0098(ribD)
            AFU: AF2007(ribG)
            HAL: VNG1256G(ribG)
            HMA: rrnAC1131(ribG)
            HWA: HQ2510A(ribG)
            NPH: NP2672A(ribG)
            PFU: PF0062
            TKO: TK0424(ribD)
            RCI: LRC156(ribD)
            APE: APE_1279.1
            SMR: Smar_0461
            STO: ST0285
            SAI: Saci_2164(rib7)
            PAI: PAE2985
            PIS: Pisl_0385
            PCL: Pcal_1122
            PAS: Pars_1352
STRUCTURES  PDB: 2AZN  2B3Z  2D5N  2G6V  2HXV  2O7P  2OBC  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.193
            ExPASy - ENZYME nomenclature database: 1.1.1.193
            ExplorEnz - The Enzyme Database: 1.1.1.193
            ERGO genome analysis and discovery system: 1.1.1.193
            BRENDA, the Enzyme Database: 1.1.1.193
            CAS: 69020-28-6
///
ENTRY       EC 1.1.1.194                Enzyme
NAME        coniferyl-alcohol dehydrogenase;
            CAD
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     coniferyl-alcohol:NADP+ oxidoreductase
REACTION    coniferyl alcohol + NADP+ = coniferyl aldehyde + NADPH + H+
            [RN:R02593]
ALL_REAC    R02593
SUBSTRATE   coniferyl alcohol [CPD:C00590];
            NADP+ [CPD:C00006]
PRODUCT     coniferyl aldehyde [CPD:C02666];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Specific for coniferyl alcohol; does not act on cinnamyl alcohol,
            4-coumaryl alcohol or sinapyl alcohol.
REFERENCE   1
  AUTHORS   Mansell, R.L., Babbel, G.R. and Zenk, M.H.
  TITLE     Multiple forms and specificity of coniferyl alcohol dehydrogenase
            from cambial regions of higher plants.
  JOURNAL   Phytochemistry 15 (1976) 1849-1853.
  ORGANISM  Metasequoia glyptostroboides, Pinus palustris, Zea mays [GN:ezma],
            Acer rubrum, Prunus padus, Salix purpurea, Schinus terebinthifolius
REFERENCE   2  [PMID:1250]
  AUTHORS   Wyrambik D, Grisebach H.
  TITLE     Purification and properties of isoenzymes of cinnamyl-alcohol
            dehydrogenase from soybean-cell-suspension cultures.
  JOURNAL   Eur. J. Biochem. 59 (1975) 9-15.
  ORGANISM  Glycine max [GN:egma]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.194
            ExPASy - ENZYME nomenclature database: 1.1.1.194
            ExplorEnz - The Enzyme Database: 1.1.1.194
            ERGO genome analysis and discovery system: 1.1.1.194
            BRENDA, the Enzyme Database: 1.1.1.194
            CAS: 37250-27-4
///
ENTRY       EC 1.1.1.195                Enzyme
NAME        cinnamyl-alcohol dehydrogenase;
            cinnamyl alcohol dehydrogenase;
            CAD
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     cinnamyl-alcohol:NADP+ oxidoreductase
REACTION    cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+ [RN:R03054]
ALL_REAC    R03054;
            (other) R02593 R03918 R06570 R06571 R07437
SUBSTRATE   cinnamyl alcohol [CPD:C02394];
            NADP+ [CPD:C00006]
PRODUCT     cinnamaldehyde [CPD:C00903];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and
            cinnamyl alcohol (cf. EC 1.1.1.194 coniferyl-alcohol dehydrogenase).
REFERENCE   1  [PMID:6365550]
  AUTHORS   Sarni F, Grand C, Boudet AM.
  TITLE     Purification and properties of cinnamoyl-CoA reductase and cinnamyl
            alcohol dehydrogenase from poplar stems (Populus X euramericana).
  JOURNAL   Eur. J. Biochem. 139 (1984) 259-65.
  ORGANISM  Populus euramericana
REFERENCE   2  [PMID:1250]
  AUTHORS   Wyrambik D, Grisebach H.
  TITLE     Purification and properties of isoenzymes of cinnamyl-alcohol
            dehydrogenase from soybean-cell-suspension cultures.
  JOURNAL   Eur. J. Biochem. 59 (1975) 9-15.
  ORGANISM  Glycine max [GN:egma]
REFERENCE   3  [PMID:572771]
  AUTHORS   Wyrambik D, Grisebach H.
  TITLE     Enzymic synthesis of lignin precursors. Further studies on
            cinnamyl-alcohol dehydrogenase from soybean-cell-suspension
            cultures.
  JOURNAL   Eur. J. Biochem. 97 (1979) 503-9.
  ORGANISM  Glycine max [GN:egma]
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
ORTHOLOGY   KO: K00083  cinnamyl-alcohol dehydrogenase
GENES       ATH: AT3G19450(CAD4)
            OSA: 4328552
            PIC: PICST_32463(GRP3.1) PICST_34974(GRP2.2) PICST_36555(GRP1)
                 PICST_39216(GRP2.3) PICST_42452(GRP2.1) PICST_49223(GRP3.4)
                 PICST_56762(GRP3.2) PICST_72153(GRE2) PICST_80185(CAD2)
            CGR: CAGL0E05170g
            AFM: AFUA_2G17850
            CPV: cgd5_1140
            CHO: Chro.50271
            PSP: PSPPH_2773
            BUR: Bcep18194_A4359
STRUCTURES  PDB: 1YQD  1YQX  2CF5  2CF6  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.195
            ExPASy - ENZYME nomenclature database: 1.1.1.195
            ExplorEnz - The Enzyme Database: 1.1.1.195
            ERGO genome analysis and discovery system: 1.1.1.195
            BRENDA, the Enzyme Database: 1.1.1.195
            CAS: 55467-36-2
///
ENTRY       EC 1.1.1.196                Enzyme
NAME        15-hydroxyprostaglandin-D dehydrogenase (NADP+);
            prostaglandin-D 15-dehydrogenase (NADP+);
            dehydrogenase, prostaglandin D2;
            NADP+-PGD2 dehydrogenase;
            dehydrogenase, 15-hydroxyprostaglandin (nicotinamide adenine
            dinucleotide phosphate);
            15-hydroxy PGD2 dehydrogenase;
            15-hydroxyprostaglandin dehydrogenase (NADP+);
            NADP+-dependent 15-hydroxyprostaglandin dehydrogenase;
            prostaglandin D2 dehydrogenase;
            NADP+-linked 15-hydroxyprostaglandin dehydrogenase;
            NADP+-specific 15-hydroxyprostaglandin dehydrogenase;
            NADP+-linked prostaglandin D2 dehydrogenase;
            15-hydroxyprostaglandin-D dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate:NADP+
            15-oxidoreductase
REACTION    (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate +
            NADP+ = (5Z,13E)-9alpha-hydroxy-11,15-dioxoprosta-5,13-dienoate +
            NADPH + H+ [RN:R02800]
ALL_REAC    R02800;
            (other) R02683
SUBSTRATE   (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
            [CPD:C00696];
            NADP+ [CPD:C00006]
PRODUCT     (5Z,13E)-9alpha-hydroxy-11,15-dioxoprosta-5,13-dienoate
            [CPD:C04758];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Specific for prostaglandins D [cf. EC 1.1.1.141
            15-hydroxyprostaglandin dehydrogenase (NAD+) and EC 1.1.1.197
            15-hydroxyprostaglandin dehydrogenase (NADP+)].
REFERENCE   1  [PMID:7354056]
  AUTHORS   Watanabe K, Shimizu T, Iguchi S, Wakatsuka H, Hayashi M, Hayaishi O.
  TITLE     An NADP-linked prostaglandin D dehydrogenase in swine brain.
  JOURNAL   J. Biol. Chem. 255 (1980) 1779-82.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00590  Arachidonic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.196
            ExPASy - ENZYME nomenclature database: 1.1.1.196
            ExplorEnz - The Enzyme Database: 1.1.1.196
            ERGO genome analysis and discovery system: 1.1.1.196
            BRENDA, the Enzyme Database: 1.1.1.196
            CAS: 84399-95-1
///
ENTRY       EC 1.1.1.197                Enzyme
NAME        15-hydroxyprostaglandin dehydrogenase (NADP+);
            NADP+-dependent 15-hydroxyprostaglandin dehydrogenase;
            NADP+-linked 15-hydroxyprostaglandin dehydrogenase;
            NADP+-specific 15-hydroxyprostaglandin dehydrogenase;
            type II 15-hydroxyprostaglandin dehydrogenase;
            15-hydroxyprostaglandin dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate:NADP+
            15-oxidoreductase
REACTION    (13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NADP+ =
            (13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate + NADPH + H+
            [RN:R04552]
ALL_REAC    R04552
SUBSTRATE   (13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate [CPD:C04741];
            NADP+ [CPD:C00006]
PRODUCT     (13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate [CPD:C04654];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Acts on prostaglandins E2, F2alpha and B1, but not on prostaglandin
            D2 [cf. EC 1.1.1.141 15-hydroxyprostaglandin dehydrogenase (NAD+)
            and EC 1.1.1.196 15-hydroxyprostaglandin-D dehydrogenase (NADP+)].
            May be identical with EC 1.1.1.189 prostaglandin-E2 9-reductase.
REFERENCE   1  [PMID:234431]
  AUTHORS   Lee SC, Levine L.
  TITLE     Prostaglandin metabolism. II. Identification of two
            15-hydroxyprostaglandin dehydrogenase types.
  JOURNAL   J. Biol. Chem. 250 (1975) 548-52.
  ORGANISM  monkey, chicken [GN:gga], dog [GN:cfa], human [GN:hsa]
REFERENCE   2  [PMID:803247]
  AUTHORS   Lee SC, Pong SS, Katzen D, Wu KY, Levine L.
  TITLE     Distribution of prostaglandin E 9-KETOREDUCTASE AND TYPES I and II
            15-hydroxyprostaglandin dehydrogenase in swine kidney medulla and
            cortex.
  JOURNAL   Biochemistry. 14 (1975) 142-5.
  ORGANISM  pig [GN:ssc]
ORTHOLOGY   KO: K00084  15-hydroxyprostaglandin dehydrogenase (NADP)
GENES       HSA: 873(CBR1)
            SSC: 397143(CBR1)
STRUCTURES  PDB: 2PFG  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.197
            ExPASy - ENZYME nomenclature database: 1.1.1.197
            ExplorEnz - The Enzyme Database: 1.1.1.197
            ERGO genome analysis and discovery system: 1.1.1.197
            BRENDA, the Enzyme Database: 1.1.1.197
            CAS: 54989-39-8
///
ENTRY       EC 1.1.1.198                Enzyme
NAME        (+)-borneol dehydrogenase;
            bicyclic monoterpenol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (+)-borneol:NAD+ oxidoreductase
REACTION    (+)-borneol + NAD+ = (+)-camphor + NADH + H+ [RN:R02944]
ALL_REAC    R02944
SUBSTRATE   (+)-borneol [CPD:C01765];
            NAD+ [CPD:C00003]
PRODUCT     (+)-camphor [CPD:C00808];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     NADP+ can also act, but more slowly.
REFERENCE   1  [PMID:677891]
  AUTHORS   Croteau R, Hooper CL, Felton M.
  TITLE     Biosynthesis of monoterpenes. Partial purfication and
            characterization of a bicyclic monoterpenol dehydrogenase from sage
            (Salvia officinalis).
  JOURNAL   Arch. Biochem. Biophys. 188 (1978) 182-93.
  ORGANISM  sage
REFERENCE   2  [PMID:3310901]
  AUTHORS   Dehal SS, Croteau R.
  TITLE     Metabolism of monoterpenes: specificity of the dehydrogenases
            responsible for the biosynthesis of camphor, 3-thujone, and
            3-isothujone.
  JOURNAL   Arch. Biochem. Biophys. 258 (1987) 287-91.
  ORGANISM  sage
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.198
            ExPASy - ENZYME nomenclature database: 1.1.1.198
            ExplorEnz - The Enzyme Database: 1.1.1.198
            ERGO genome analysis and discovery system: 1.1.1.198
            BRENDA, the Enzyme Database: 1.1.1.198
            CAS: 67185-75-5
///
ENTRY       EC 1.1.1.199                Enzyme
NAME        (S)-usnate reductase;
            L-usnic acid dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     reduced-(S)-usnate:NAD+ oxidoreductase (ether-bond-forming)
REACTION    (6R)-2-acetyl-6-(3-acetyl-2,4,6-trihydroxy-5-methylphenyl)-3-
            hydroxy-6 methyl-2,4-cyclohexadien-1-one + NAD+ = (S)-usnate + NADH
            + H+ [RN:R07345]
ALL_REAC    R07345
SUBSTRATE   (6R)-2-acetyl-6-(3-acetyl-2,4,6-trihydroxy-5-methylphenyl)-3-
            hydroxy-6 methyl-2,4-cyclohexadien-1-one;
            NAD+ [CPD:C00003]
PRODUCT     (S)-usnate [CPD:C10101];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:16454408]
  AUTHORS   Barbini N, Gorini G, Ferrucci L, Biggeri A.
  TITLE     [Analysis of arterial hypertension and work in the epidemiologic
            study &quot;Aging, Health and Work&quot;]
  JOURNAL   Epidemiol. Prev. 29 (2005) 160-5.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.199
            ExPASy - ENZYME nomenclature database: 1.1.1.199
            ExplorEnz - The Enzyme Database: 1.1.1.199
            ERGO genome analysis and discovery system: 1.1.1.199
            BRENDA, the Enzyme Database: 1.1.1.199
            CAS: 77237-99-1
///
ENTRY       EC 1.1.1.200                Enzyme
NAME        aldose-6-phosphate reductase (NADPH);
            aldose 6-phosphate reductase;
            NADP+-dependent aldose 6-phosphate reductase;
            A6PR;
            aldose-6-P reductase;
            aldose-6-phosphate reductase;
            alditol 6-phosphate:NADP+ 1-oxidoreductase;
            aldose-6-phosphate reductase (NADPH)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-aldose-6-phosphate:NADP+ 1-oxidoreductase
REACTION    D-sorbitol 6-phosphate + NADP+ = D-glucose 6-phosphate + NADPH + H+
            [RN:R00834]
ALL_REAC    R00834
SUBSTRATE   D-sorbitol 6-phosphate [CPD:C01096];
            NADP+ [CPD:C00006]
PRODUCT     D-glucose 6-phosphate [CPD:C00092];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     In the reverse reaction, acts also on D-galactose 6-phosphate and,
            more slowly, on D-mannose 6-phosphate and 2-deoxy-D-glucose
            6-phosphate.
REFERENCE   1
  AUTHORS   Negm, F.B. and Loescher, W.H.
  TITLE     Characterization and partial-purification of aldose-6-phosphate
            reductase (alditol-6-phosphate-NADP 1-oxidoreductase) from apple
            leaves.
  JOURNAL   Plant Physiol. 67 (1981) 139-142.
  ORGANISM  Malus domestica, Prunus persica, Pyrus communis, Prunus armeniaca
ORTHOLOGY   KO: K00085  aldose-6-phosphate reductase (NADPH2)
GENES       ATH: AT2G21260
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.200
            ExPASy - ENZYME nomenclature database: 1.1.1.200
            ExplorEnz - The Enzyme Database: 1.1.1.200
            ERGO genome analysis and discovery system: 1.1.1.200
            BRENDA, the Enzyme Database: 1.1.1.200
            CAS: 76901-04-7
///
ENTRY       EC 1.1.1.201                Enzyme
NAME        7beta-hydroxysteroid dehydrogenase (NADP+);
            NADP+-dependent 7beta-hydroxysteroid dehydrogenase;
            7beta-hydroxysteroid dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     7beta-hydroxysteroid:NADP+ 7-oxidoreductase
REACTION    a 7beta-hydroxysteroid + NADP+ = a 7-oxosteroid + NADPH + H+
            [RN:R03753]
ALL_REAC    R03753
SUBSTRATE   7beta-hydroxysteroid [CPD:C02956];
            NADP+ [CPD:C00006]
PRODUCT     7-oxosteroid [CPD:C01881];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Catalyses the oxidation of the 7beta-hydroxy group of bile acids
            such as ursodeoxycholate.
REFERENCE   1  [PMID:6954878]
  AUTHORS   Hirano S, Masuda N.
  TITLE     Characterization of NADP-dependent 7 beta-hydroxysteroid
            dehydrogenases from Peptostreptococcus productus and Eubacterium
            aerofaciens.
  JOURNAL   Appl. Environ. Microbiol. 43 (1982) 1057-63.
  ORGANISM  Peptostreptococcus productus, Eubacterium aerofaciens
REFERENCE   2  [PMID:6945134]
  AUTHORS   MacDonald IA, Roach PD.
  TITLE     Bile induction of 7 alpha- and 7 beta-hydroxysteroid dehydrogenases
            in Clostridium absonum.
  JOURNAL   Biochim. Biophys. Acta. 665 (1981) 262-9.
  ORGANISM  Clostridium absonum
REFERENCE   3  [PMID:6758698]
  AUTHORS   MacDonald IA, Rochon YP, Hutchison DM, Holdeman LV.
  TITLE     Formation of ursodeoxycholic acid from chenodeoxycholic acid by a 7
            beta-hydroxysteroid dehydrogenase-elaborating Eubacterium
            aerofaciens strain cocultured with 7 alpha-hydroxysteroid
            dehydrogenase-elaborating organisms.
  JOURNAL   Appl. Environ. Microbiol. 44 (1982) 1187-95.
  ORGANISM  Eubacterium aerofaciens
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.201
            ExPASy - ENZYME nomenclature database: 1.1.1.201
            ExplorEnz - The Enzyme Database: 1.1.1.201
            ERGO genome analysis and discovery system: 1.1.1.201
            BRENDA, the Enzyme Database: 1.1.1.201
            CAS: 79393-83-2
///
ENTRY       EC 1.1.1.202                Enzyme
NAME        1,3-propanediol dehydrogenase;
            3-hydroxypropionaldehyde reductase;
            1,3-PD:NAD+ oxidoreductase;
            1,3-propanediol:NAD+ oxidoreductase;
            1,3-propanediol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     propane-1,3-diol:NAD+ 1-oxidoreductase
REACTION    propane-1,3-diol + NAD+ = 3-hydroxypropanal + NADH + H+ [RN:R03119]
ALL_REAC    R03119;
            (other) R02377
SUBSTRATE   propane-1,3-diol [CPD:C02457];
            NAD+ [CPD:C00003]
PRODUCT     3-hydroxypropanal [CPD:C00969];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13791444]
  AUTHORS   ABELES RH, BROWNSTEIN AM, RANDLES CH.
  TITLE     beta-Hydroxypropionaldehyde, an intermediate in the formation of
            1,3-propanediol by Aerobacter aerogenes.
  JOURNAL   Biochim. Biophys. Acta. 41 (1960) 530-1.
  ORGANISM  Aerobacter melanogaster
REFERENCE   2  [PMID:7035429]
  AUTHORS   Forage RG, Foster MA.
  TITLE     Glycerol fermentation in Klebsiella pneumoniae: functions of the
            coenzyme B12-dependent glycerol and diol dehydratases.
  JOURNAL   J. Bacteriol. 149 (1982) 413-9.
  ORGANISM  Klebsiella pneumoniae
PATHWAY     PATH: map00561  Glycerolipid metabolism
ORTHOLOGY   KO: K00086  1,3-propanediol dehydrogenase
GENES       GME: Gmet_1053
            PCA: Pcar_0257 Pcar_2510
            BCE: BC2176
            BCL: ABC0042 ABC0327
            BPU: BPUM_2350
            GKA: GK0727
            LPL: lp_3051(dhaT)
            LSA: LSA0122(dhaT)
            LBR: LVIS_2191
            OOE: OEOE_1336
            CPE: CPE0936
            CPF: CPF_1180(dhaT)
            CPR: CPR_1011(dhaT)
            CTC: CTC00506
            CNO: NT01CX_1219
            CDF: CD0274(dhaT)
            CKL: CKL_2405(dhaT1) CKL_3436(dhaT2)
            MSM: MSMEG_6239
            RHA: RHA1_ro06057 RHA1_ro06060
            SEN: SACE_2379 SACE_2386
            LIL: LA2996(dhaT)
            AAE: aq_1145(dhaT)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.202
            ExPASy - ENZYME nomenclature database: 1.1.1.202
            ExplorEnz - The Enzyme Database: 1.1.1.202
            ERGO genome analysis and discovery system: 1.1.1.202
            BRENDA, the Enzyme Database: 1.1.1.202
            CAS: 81611-70-3
///
ENTRY       EC 1.1.1.203                Enzyme
NAME        uronate dehydrogenase;
            uronate: NAD-oxidoreductase;
            uronic acid dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     uronate:NAD+ 1-oxidoreductase
REACTION    D-galacturonate + NAD+ + H2O = D-galactarate + NADH + H+ [RN:R01981]
ALL_REAC    R01981
SUBSTRATE   D-galacturonate [CPD:C00333];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     D-galactarate [CPD:C00879];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts on D-glucuronate.
REFERENCE   1  [PMID:13657147]
  AUTHORS   KILGORE WW, STARR MP.
  TITLE     Uronate oxidation by phytopathogenic pseudomonads.
  JOURNAL   Nature. 183 (1959) 1412-3.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.203
            ExPASy - ENZYME nomenclature database: 1.1.1.203
            ExplorEnz - The Enzyme Database: 1.1.1.203
            ERGO genome analysis and discovery system: 1.1.1.203
            BRENDA, the Enzyme Database: 1.1.1.203
            CAS: 37250-98-9
///
ENTRY       EC 1.1.1.204      Obsolete  Enzyme
NAME        Transferred to 1.17.1.4
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Transferred entry: now EC 1.17.1.4 xanthine dehydrogenase. The
            enzyme was incorrectly classified as acting on a CH-OH group (EC
            1.1.1.204 created 1972 as EC 1.2.1.37, transferred 1984 to EC
            1.1.1.204, modified 1989, deleted 2004)
STRUCTURES  PDB: 1FO4  1JRO  1JRP  1N5X  1V97  1VDV  1WYG  2CKJ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.204
            ExPASy - ENZYME nomenclature database: 1.1.1.204
            ExplorEnz - The Enzyme Database: 1.1.1.204
            ERGO genome analysis and discovery system: 1.1.1.204
            BRENDA, the Enzyme Database: 1.1.1.204
///
ENTRY       EC 1.1.1.205                Enzyme
NAME        IMP dehydrogenase;
            inosine-5'-phosphate dehydrogenase;
            inosinic acid dehydrogenase;
            inosinate dehydrogenase;
            inosine 5'-monophosphate dehydrogenase;
            inosine monophosphate dehydrogenase;
            IMP oxidoreductase;
            inosine monophosphate oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     IMP:NAD+ oxidoreductase
REACTION    inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH +
            H+ [RN:R01130]
ALL_REAC    R01130
SUBSTRATE   inosine 5'-phosphate [CPD:C00130];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     xanthosine 5'-phosphate [CPD:C00655];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The enzyme acts on the hydroxy group of the hydrated derivative of
            the substrate.
REFERENCE   1  [PMID:13428767]
  AUTHORS   MAGASANIK B, MOYED HS, GEHRING LB.
  TITLE     Enzymes essential for the biosynthesis of nucleic acid guanine;
            inosine 5'-phosphate dehydrogenase of Aerobacter aerogenes.
  JOURNAL   J. Biol. Chem. 226 (1957) 339-50.
  ORGANISM  Aerobacter aerogenes
REFERENCE   2
  AUTHORS   Turner, J.F. and King, J.E.
  TITLE     Inosine 5-phosphate dehydrogenase of pea seeds.
  JOURNAL   Biochem. J. 79 (1961) 147.
  ORGANISM  Pisum sativum
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K00088  IMP dehydrogenase
GENES       HSA: 3614(IMPDH1) 3615(IMPDH2)
            MMU: 23917(Impdh1) 23918(Impdh2)
            RNO: 301005(Impdh2) 362329(Impdh1_predicted)
            CFA: 476630(IMPDH2) 608783(IMPDH1)
            BTA: 504305(IMPDH1) 511969(IMPDH2)
            GGA: 416058(RCJMB04_1j11)
            XLA: 380485(impdh1) 398453(MGC53627) 399236(impdh2)
            XTR: 493428(impdh2) 550037(impdh1)
            DRE: 317745(impdh2)
            SPU: 581195(LOC581195)
            DME: Dmel_CG1799(ras)
            ATH: AT1G16350
            OSA: 4334308
            CME: CML243C
            SCE: YHR216W(IMD2) YLR432W(IMD3) YML056C(IMD4)
            AGO: AGOS_AER117W
            PIC: PICST_65804
            SPO: SPBC2F12.14c
            AFM: AFUA_2G03610
            AOR: AO090120000224
            CNE: CNA04240
            UMA: UM02566.1
            DDI: DDB_0230098(guaB)
            PFA: PFI1020c
            CPV: cgd6_20
            TAN: TA03405
            TPV: TP03_0220
            TET: TTHERM_00486810
            TBR: Tb10.61.0150 Tb927.5.2080
            TCR: 506519.130 508909.20 511301.110
            LMA: LmjF17.0725 LmjF19.1560
            ECO: b2508(guaB)
            ECJ: JW5401(guaB)
            ECE: Z3772(guaB)
            ECS: ECs3370
            ECC: c3027(guaB)
            ECI: UTI89_C0656(ybeX) UTI89_C2826(guaB) UTI89_C3070(gutQ)
            ECP: ECP_2510
            ECV: APECO1_4018(guaB)
            ECW: EcE24377A_2792(guaB)
            ECX: EcHS_A2659(guaB)
            STY: STY2752(guaB)
            STT: t0346(guaB)
            SPT: SPA0356(guaB)
            SEC: SC2509(imdH)
            STM: STM2511(guaB)
            YPE: YPO2871(guaB)
            YPK: y1362(guaB)
            YPM: YP_2737(guaB)
            YPA: YPA_2312
            YPN: YPN_1267
            YPP: YPDSF_2216
            YPS: YPTB2833(guaB)
            YPI: YpsIP31758_1194(guaB)
            SFX: S2726(guaB)
            SFV: SFV_2555(guaB)
            SSN: SSON_2590(guaB)
            SBO: SBO_2532(guaB)
            SDY: SDY_2704(guaB)
            ECA: ECA3209(guaB)
            PLU: plu2713(guaB)
            WBR: WGLp605(guaB)
            SGL: SG1749
            ENT: Ent638_2999
            KPN: KPN_02834(guaB)
            BFL: Bfl528(guaB)
            BPN: BPEN_547(guaB)
            HIT: NTHI0324(guaB)
            HIP: CGSHiEE_01970
            HDU: HD1503(guaB)
            HSO: HS_0420(guaB)
            PMU: PM0295(guaB)
            MSU: MS0774(guaB)
            APL: APL_0593(guaB)
            XFA: XF2430
            XFT: PD1448(guaB)
            XCC: XCC2184(guaB)
            XCB: XC_1934
            XCV: XCV2486(guaB)
            XAC: XAC2288(guaB)
            XOO: XOO2194(guaB)
            XOM: XOO_2062(XOO2062)
            VCH: VC0767
            VCO: VC0395_A0296(guaB)
            VVU: VV1_0419
            VVY: VV0775
            VPA: VP0616
            VFI: VF0637
            PPR: PBPRA0780
            PAE: PA3770(guaB)
            PAU: PA14_15310(guaB)
            PAP: PSPA7_1346(guaB)
            PPU: PP_1031(guaB)
            PST: PSPTO_1449(guaB)
            PSB: Psyr_1261
            PSP: PSPPH_1333(guaB)
            PFL: PFL_4940(guaB)
            PFO: Pfl_4588
            PEN: PSEEN4393(guaB)
            PAR: Psyc_1360(guaB)
            PCR: Pcryo_1005
            ACI: ACIAD3503(guaB)
            SON: SO_3293(guaB)
            SDN: Sden_1269
            SFR: Sfri_1137
            SAZ: Sama_2359
            SBL: Sbal_2984
            SLO: Shew_1297
            SPC: Sputcn32_2646
            SHE: Shewmr4_1234
            SHM: Shewmr7_1305
            SHN: Shewana3_1235
            SHW: Sputw3181_1361
            ILO: IL0578(guaB)
            CPS: CPS_4242(guaB)
            PHA: PSHAa0648(guaB)
            PAT: Patl_3120
            SDE: Sde_1459
            PIN: Ping_2950
            MAQ: Maqu_1728
            CBU: CBU_1342(guaB)
            CBD: COXBU7E912_1431(guaB)
            LPN: lpg1723(guaB) lpg2843
            LPF: lpl1687(guaB) lpl2755
            LPP: lpp1688(guaB) lpp2902
            MCA: MCA0291(guaB)
            FTU: FTT1317c(guaB)
            FTF: FTF1317c(guaB)
            FTW: FTW_1483(guaB)
            FTL: FTL_1478
            FTH: FTH_1432(guaB)
            FTA: FTA_1563(guaB)
            FTN: FTN_0661(guaB)
            TCX: Tcr_1616
            NOC: Noc_0613
            AEH: Mlg_1014
            HHA: Hhal_1682
            HCH: HCH_04943(guaB)
            CSA: Csal_0730
            ABO: ABO_1851(guaB)
            AHA: AHA_1989(guaB)
            DNO: DNO_0376(guaB)
            BCI: BCI_0651(guaB)
            RMA: Rmag_0462
            VOK: COSY_0427(guaB)
            NME: NMB1201
            NMA: NMA1372(guaB)
            NMC: NMC1103(guaB)
            NGO: NGO0799
            CVI: CV_1303(guaB)
            RSO: RSc1429(guaB)
            REU: Reut_A1856
            REH: H16_A2030(guaB)
            RME: Rmet_1461
            BMA: BMA1524(guaB)
            BMV: BMASAVP1_A2024(guaB)
            BML: BMA10299_A3287(guaB)
            BMN: BMA10247_1295(guaB)
            BXE: Bxe_A1706
            BVI: Bcep1808_1897
            BUR: Bcep18194_A5301
            BCN: Bcen_6086
            BCH: Bcen2424_1991
            BAM: Bamb_2024
            BPS: BPSL2129(guaB)
            BPM: BURPS1710b_2549(guaB) BURPS1710b_A1360 BURPS1710b_A2480
            BPL: BURPS1106A_2457(guaB)
            BPD: BURPS668_2405(guaB)
            BTE: BTH_I2056(guaB)
            PNU: Pnuc_1423
            BPE: BP2625(guaB)
            BPA: BPP1258(guaB)
            BBR: BB2326(guaB)
            RFR: Rfer_2288
            POL: Bpro_2440
            PNA: Pnap_2001
            AAV: Aave_3370
            AJS: Ajs_2548
            VEI: Veis_1246
            MPT: Mpe_A1620
            HAR: HEAR1359(guaB)
            MMS: mma_2034(guaB)
            NEU: NE0095(guaB) NE0524
            NET: Neut_2250
            NMU: Nmul_A1200
            EBA: ebA6647(guaB)
            AZO: azo1580(guaB)
            DAR: Daro_2338
            TBD: Tbd_1752
            MFA: Mfla_1141
            HPY: HP0829
            HPA: HPAG1_0815 HPAG1_1423
            HHE: HH0702(guaB)
            HAC: Hac_1197(guaB)
            WSU: WS1895(guaB)
            TDN: Tmden_0770
            CJE: Cj1058c(guaB)
            CJR: CJE1201(guaB)
            CJJ: CJJ81176_1078(guaB)
            CJU: C8J_0999(guaB)
            CJD: JJD26997_0664(guaB)
            CFF: CFF8240_0612(guaB)
            CCV: CCV52592_0979(guaB)
            CHA: CHAB381_0908(guaB)
            CCO: CCC13826_0276(guaB)
            ABU: Abu_1023(guaB)
            NIS: NIS_1280(guaB)
            SUN: SUN_1794(guaB)
            GSU: GSU2195(guaB)
            GME: Gmet_2293
            PCA: Pcar_1217
            PPD: Ppro_2011
            DVU: DVU1044(guaB)
            DVL: Dvul_1949
            DDE: Dde_1471
            LIP: LI0591(guaB)
            BBA: Bd0921 Bd1779(guaB) Bd2081(guaB)
            DPS: DP0902
            ADE: Adeh_2349 Adeh_3135
            MXA: MXAN_3777(guaB)
            SAT: SYN_00897
            SFU: Sfum_2122
            WOL: WD0089(guaB)
            WBM: Wbm0527(guaB)
            AMA: AM105(guaB)
            APH: APH_0088(guaB)
            ERU: Erum7500(guaB)
            ERW: ERWE_CDS_07900(guaB)
            ERG: ERGA_CDS_07810(guaB)
            ECN: Ecaj_0784
            ECH: ECH_0224(guaB)
            NSE: NSE_0525(guaB)
            PUB: SAR11_0649(guaB)
            MLO: mlr8350
            MES: Meso_0467
            SME: SMc00815(guaB)
            ATU: Atu0624(guaB)
            ATC: AGR_C_1108(guaB)
            RET: RHE_CH00794(guaB)
            RLE: RL0847(guaB)
            BME: BMEII0896
            BMF: BAB2_0851
            BMS: BRA0352(guaB)
            BMB: BruAb2_0830(guaB)
            BOV: BOV_A0319(guaB)
            BJA: blr3972(guaB)
            BRA: BRADO3165(guaB)
            BBT: BBta_3610(guaB)
            RPA: RPA2200(guaB)
            RPB: RPB_3193
            RPC: RPC_3071
            RPD: RPD_2264
            RPE: RPE_3268
            NWI: Nwi_2146
            NHA: Nham_2546
            BHE: BH01800(guaB)
            BQU: BQ01690(guaB)
            BBK: BARBAKC583_0341(guaB)
            CCR: CC_1617
            SIL: SPO2039(guaB)
            SIT: TM1040_1224
            RSP: RSP_2868
            RSH: Rsph17029_1514
            JAN: Jann_1982
            RDE: RD1_2713(guaB)
            PDE: Pden_0592
            MMR: Mmar10_1175
            HNE: HNE_1804(guaB)
            ZMO: ZMO1321(guaB)
            NAR: Saro_1752
            SAL: Sala_1027
            ELI: ELI_07095
            GOX: GOX2265
            GBE: GbCGDNIH1_1147
            RRU: Rru_A0244
            MAG: amb3781
            MGM: Mmc1_3015
            ABA: Acid345_1260
            SUS: Acid_6691
            BSU: BG10073(guaB) BG11600(yhcV)
            BHA: BH0020(guaB)
            BAN: BA0008(guaB)
            BAR: GBAA0008(guaB)
            BAA: BA_0603
            BAT: BAS0011
            BCE: BC0013
            BCA: BCE_0009(guaB)
            BCZ: BCZK0009(guaB)
            BTK: BT9727_0009(guaB)
            BTL: BALH_0009(guaB)
            BLI: BL02350(guaB)
            BLD: BLi00014(guaB) BLi00986(yhcV)
            BCL: ABC0011(guaB)
            BAY: RBAM_000120(guaB)
            BPU: BPUM_0504(guaB)
            OIH: OB0010
            GKA: GK0009
            SAU: SA0375(guaB)
            SAV: SAV0390(guaB)
            SAM: MW0366(guaB)
            SAR: SAR0408(guaB)
            SAS: SAS0366
            SAC: SACOL0460(guaB)
            SAB: SAB0340(guaB)
            SAA: SAUSA300_0388(guaB)
            SAO: SAOUHSC_00374
            SEP: SE2348
            SER: SERP0069(guaB)
            SHA: SH2583(guaB)
            SSP: SSP2323
            LMO: lmo0132 lmo2758(guaB)
            LMF: LMOf2365_0150 LMOf2365_2746(guaB)
            LIN: lin0179 lin2901(guaB)
            LWE: lwe0114 lwe2705(guaB)
            LLA: L21264(guaB)
            LLC: LACR_0225
            LLM: llmg_0230(guaB)
            SPY: SPy_2206(guaB)
            SPZ: M5005_Spy_1857(guaB)
            SPM: spyM18_2244(impd)
            SPG: SpyM3_1857(guaB)
            SPS: SPs1853
            SPH: MGAS10270_Spy1977(guaB)
            SPI: MGAS10750_Spy1970(guaB)
            SPJ: MGAS2096_Spy1888(guaB)
            SPK: MGAS9429_Spy1868(guaB)
            SPF: SpyM51830(guaB)
            SPA: M6_Spy1875
            SPB: M28_Spy1890(guaB)
            SPN: SP_2228
            SPR: spr2033(imdH)
            SPD: SPD_2055(guaB)
            SAG: SAG2159(guaB)
            SAN: gbs2118
            SAK: SAK_2117(guaB)
            SMU: SMU.2157(guaB)
            STC: str2016(guaB)
            STL: stu2016(guaB)
            SSA: SSA_2374(guaB)
            SGO: SGO_0008 SGO_1625
            LJO: LJ0043
            LAC: LBA0199
            LSA: LSA0276(guaB)
            LSL: LSL_1452(guaB)
            LDB: Ldb0297(guaB)
            LBU: LBUL_0251
            LBR: LVIS_2058
            LCA: LSEI_0217
            LGA: LGAS_0041
            PPE: PEPE_1719
            EFA: EF3293(guaB)
            OOE: OEOE_1127
            STH: STH2916
            CAC: CAC2701(guaB)
            CPE: CPE2276
            CPF: CPF_2558(guaB)
            CPR: CPR_2261(guaB)
            CTC: CTC02410
            CNO: NT01CX_0460(guaB)
            CDF: CD2335(guaB)
            CBO: CBO3296(guaB)
            CBA: CLB_3352(guaB)
            CBH: CLC_3238(guaB)
            CBF: CLI_3466(guaB)
            CBE: Cbei_2114
            CKL: CKL_0465(guaB)
            CHY: CHY_1176(guaB)
            DSY: DSY2052
            DRM: Dred_1906
            SWO: Swol_0916
            TTE: TTE0582(guaB)
            MTA: Moth_1108
            MPE: MYPE3150(guaB)
            MFL: Mfl343
            MTU: Rv1843c(guaB1) Rv3410c(guaB3) Rv3411c(guaB2)
            MTC: MT1891(guaB-1) MT3518 MT3519(guaB-2)
            MBO: Mb1874c(guaB1) Mb3444c(guaB3) Mb3445c(guaB2)
            MBB: BCG_1879c(guaB1) BCG_3480c(guaB3) BCG_3481c(guaB2)
            MLE: ML0387(guaB2) ML0388(guaB3) ML2066(guaB1)
            MPA: MAP1556c(guaB1) MAP4278(guaB2) MAP4279(guaB3)
            MAV: MAV_4356(guaB)
            MSM: MSMEG_1602(guaB) MSMEG_1603 MSMEG_3634
            MVA: Mvan_1511 Mvan_3090
            MGI: Mflv_3360 Mflv_4909
            MMC: Mmcs_1167 Mmcs_1168 Mmcs_2813
            MKM: Mkms_1184 Mkms_2857
            MJL: Mjls_1194 Mjls_2840
            CGL: NCgl0578(cgl0603) NCgl0579(cgl0604) NCgl2586(cgl2679)
            CGB: cg0699(guaB2) cg0700(guaB3) cg2964(guaB1)
            CEF: CE0608(guaB) CE0609 CE2530
            CDI: DIP0580(guaB) DIP0581
            CJK: jk1722(guaB2) jk1723(guaB1)
            NFA: nfa25140(guaB2) nfa8950(guaB) nfa8960
            RHA: RHA1_ro06199(guaB1) RHA1_ro06200 RHA1_ro07243(guaB2)
            SCO: SCO1461(guaB2) SCO4770(guaB) SCO4771(SCD63.03)
            SMA: SAV5000(guaB1) SAV5001(guaB2) SAV6884(guaB3)
            TWH: TWT075(guaB1) TWT076(guaB2)
            TWS: TW085(guaB1) TW086(guaB2)
            LXX: Lxx19150(guaB) Lxx19840(guaB) Lxx19860(guaB)
            CMI: CMM_2559(guaB1) CMM_2561(guaB2)
            ART: Arth_2879
            AAU: AAur_2867(guaB)
            PAC: PPA0708 PPA1767 PPA1768
            NCA: Noca_2608 Noca_3645
            TFU: Tfu_2440 Tfu_2595 Tfu_2596
            FRA: Francci3_0636 Francci3_0637
            FAL: FRAAL1139(guaB) FRAAL1140
            ACE: Acel_0366 Acel_0367
            SEN: SACE_0914(guaB2) SACE_6707(guaB3) SACE_6708(guaB-2)
            BLO: BL1500 BL1722(guaB)
            BAD: BAD_0450(guaB) BAD_0777
            RXY: Rxyl_0815
            FNU: FN1231
            RBA: RB11822(guaB)
            CMU: TC0443
            CPN: CPn0172(guaB_1)
            CPJ: CPj0172(guaB)
            CPT: CpB0174
            CCA: CCA00574
            CFE: CF0427(imdH)
            BBU: BBB17(guaB)
            BAF: BAPKO_5016(guaB)
            TDE: TDE2665(guaB)
            LIL: LA1986
            LIC: LIC11919(guaB)
            LBJ: LBJ_1530(imdH)
            LBL: LBL_1754(imdH)
            SYN: slr1722(guaB)
            SYW: SYNW0725(guaB)
            SYC: syc2263_d(guaB)
            SYF: Synpcc7942_1831
            SYD: Syncc9605_1944
            SYE: Syncc9902_0721
            SYG: sync_0971
            SYR: SynRCC307_0739(guaB)
            SYX: SynWH7803_1591(guaB)
            CYA: CYA_1409
            CYB: CYB_1616
            TEL: tll2190
            GVI: glr1603
            ANA: alr0051
            AVA: Ava_2653
            PMA: Pro1138(guaB)
            PMM: PMM1062(guaB)
            PMT: PMT1126(guaB)
            PMN: PMN2A_0690
            PMI: PMT9312_1073
            PMB: A9601_11671(guaB)
            PMC: P9515_11521(guaB)
            PMF: P9303_09131(guaB)
            PMG: P9301_11681(guaB)
            PME: NATL1_15241(guaB)
            BTH: BT_3845
            BFR: BF3536 BF4075
            BFS: BF3343(impDH) BF3891(guaB)
            PGI: PG0523(guaB)
            SRU: SRU_1496(guaB)
            CHU: CHU_0196(guaB)
            GFO: GFO_2510(guaB)
            FPS: FP1820(guaB)
            CTE: CT1293(guaB)
            CCH: Cag_0489
            CPH: Cpha266_1628
            PVI: Cvib_1056
            PLT: Plut_0788
            DET: DET0384
            DEH: cbdb_A329
            DRA: DR_1878
            DGE: Dgeo_0548
            TTH: TTC0064
            TTJ: TTHA0432
            AAE: aq_2023(guaB)
            TMA: TM1347
            MJA: MJ0188
            MMP: MMP0133(guaB) MMP0287
            MMQ: MmarC5_1545
            MHU: Mhun_2618 Mhun_2632
            MEM: Memar_1568
            MBN: Mboo_1716
            MTH: MTH1282
            MST: Msp_0431(guaB)
            MSI: Msm_1102 Msm_1629
            MKA: MK1600(guaB)
            AFU: AF0847(guaB-1) AF1259 AF2118(guaB-2)
            HAL: VNG0651G(imd1) VNG1001G(guaB)
            HMA: pNG7153(guaB1) rrnAC0267(imd1) rrnAC0748(guaB3)
                 rrnAC1274(guaB2) rrnAC2139(imd3) rrnAC2699 rrnB0175(imd2)
            HWA: HQ1650A HQ2382A(guaB)
            NPH: NP2318A NP3080A(guaB_2) NP3384A(guaB_1)
            TAC: Ta0219
            TVO: TVN1375
            PTO: PTO0470 PTO0540 PTO0859
            PAB: PAB1250
            PFU: PF0285
            TKO: TK0194
            RCI: RCIX2672(guaB-2) RCIX683(guaB-1)
            APE: APE_1507.1
STRUCTURES  PDB: 1AK5  1B3O  1EEP  1JCN  1JR1  1LRT  1ME7  1ME8  1ME9  1MEH  
                 1MEI  1MEW  1NF7  1NFB  1PVN  1VRD  1ZFJ  2CU0  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.205
            ExPASy - ENZYME nomenclature database: 1.1.1.205
            ExplorEnz - The Enzyme Database: 1.1.1.205
            ERGO genome analysis and discovery system: 1.1.1.205
            BRENDA, the Enzyme Database: 1.1.1.205
            CAS: 9028-93-7
///
ENTRY       EC 1.1.1.206                Enzyme
NAME        tropinone reductase I;
            tropine dehydrogenase;
            tropinone reductase (ambiguous);
            TR-I
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     tropine:NADP+ 3alpha-oxidoreductase
REACTION    tropine + NADP+ = tropinone + NADPH + H+ [RN:R02832]
ALL_REAC    R02832
SUBSTRATE   tropine [CPD:C00729];
            NADP+ [CPD:C00006]
PRODUCT     tropinone [CPD:C00783];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also oxidizes other tropan-3alpha-ols, but not the corresponding
            beta-derivatives [1]. This enzyme along with EC 1.1.1.236, tropinone
            reductase II, represents a branch point in tropane alkaloid
            metabolism [4]. Tropine (the product of EC 1.1.1.206) is
            incorporated into hyoscyamine and scopolamine whereas pseudotropine
            (the product of EC 1.1.1.236) is the first specific metabolite on
            the pathway to the calystegines [4]. Both enzymes are always found
            together in any given tropane-alkaloid-producing species, have a
            common substrate, tropinone, and are strictly stereospecific [3].
REFERENCE   1
  AUTHORS   Koelen, K.J. and Gross, G.G.
  TITLE     Partial purification and properties of tropine dehydrogenase from
            root cultures of Datura stramonium.
  JOURNAL   Planta Med. 44 (1982) 227-230.
  ORGANISM  Datura stramonium
REFERENCE   2
  AUTHORS   Couladis, M.M, Friesen, J.B., Landgrebe, M.E. and Leete, E.
  TITLE     Enzymes catalysing the reduction of tropinone to tropine and
            &psi;-tropine isolated from the roots of Datura innoxia.
  JOURNAL   Pytochemistry 30 (1991) 801-805.
REFERENCE   3  [PMID:8415746]
  AUTHORS   Nakajima K, Hashimoto T, Yamada Y.
  TITLE     Two tropinone reductases with different stereospecificities are
            short-chain dehydrogenases evolved from a common ancestor.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 9591-5.
REFERENCE   4  [PMID:16426652]
  AUTHORS   Drager B.
  TITLE     Tropinone reductases, enzymes at the branch point of tropane
            alkaloid metabolism.
  JOURNAL   Phytochemistry. 67 (2006) 327-37.
PATHWAY     PATH: map00960  Alkaloid biosynthesis II
ORTHOLOGY   KO: K08081  tropine dehydrogenase
GENES       ATH: AT1G07450 AT2G29150 AT2G29260 AT2G29290 AT2G29300 AT2G29310
                 AT2G29320 AT2G29330 AT2G29340 AT2G29360 AT2G29370 AT2G30670
                 AT5G06060
            OSA: 4332375 4332377
            XFA: XF0913
            XFT: PD1772
            XCC: XCC3760(trn2)
            XCB: XC_3830
            XCV: XCV3936(trn2)
            XAC: XAC3811(trn2)
            XOO: XOO0575(trn2)
            XOM: XOO_0536(XOO0536)
            ANA: alr4456
            AVA: Ava_3338
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.206
            ExPASy - ENZYME nomenclature database: 1.1.1.206
            ExplorEnz - The Enzyme Database: 1.1.1.206
            ERGO genome analysis and discovery system: 1.1.1.206
            BRENDA, the Enzyme Database: 1.1.1.206
            CAS: 118390-87-7
///
ENTRY       EC 1.1.1.207                Enzyme
NAME        (-)-menthol dehydrogenase;
            monoterpenoid dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (-)-menthol:NADP+ oxidoreductase
REACTION    (-)-menthol + NADP+ = (-)-menthone + NADPH + H+ [RN:R02177]
ALL_REAC    R02177
SUBSTRATE   (-)-menthol [CPD:C00400];
            NADP+ [CPD:C00006]
PRODUCT     (-)-menthone [CPD:C00843];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Not identical with EC 1.1.1.208 (+)-neomenthol dehydrogenase. Acts
            also on a number of other cyclohexanols and cyclohexenols.
REFERENCE   1
  AUTHORS   Kjonaas, R., Martinkus-Taylor, C. and Croteau, R.
  TITLE     Metabolism of monoterpenes: conversion of l-menthone to l-menthol
            and d-neomenthol by stereospecific dehydrogenases from peppermint
            (Mentha piperita) leaves.
  JOURNAL   Plant Physiol. 69 (1982) 1013-1017.
  ORGANISM  Mentha piperita
PATHWAY     PATH: map00902  Monoterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.207
            ExPASy - ENZYME nomenclature database: 1.1.1.207
            ExplorEnz - The Enzyme Database: 1.1.1.207
            ERGO genome analysis and discovery system: 1.1.1.207
            BRENDA, the Enzyme Database: 1.1.1.207
            CAS: 81811-46-3
///
ENTRY       EC 1.1.1.208                Enzyme
NAME        (+)-neomenthol dehydrogenase;
            monoterpenoid dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (+)-neomenthol:NADP+ oxidoreductase
REACTION    (+)-neomenthol + NADP+ = (-)-menthone + NADPH + H+ [RN:R02548]
ALL_REAC    R02548
SUBSTRATE   (+)-neomenthol [CPD:C00553];
            NADP+ [CPD:C00006]
PRODUCT     (-)-menthone [CPD:C00843];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Not identical with EC 1.1.1.207 (-)-menthol dehydrogenase. Acts also
            on a number of other cyclohexanols and cyclohexenols.
REFERENCE   1
  AUTHORS   Kjonaas, R., Martinkus-Taylor, C. and Croteau, R.
  TITLE     Metabolism of monoterpenes: conversion of l-menthone to l-menthol
            and d-neomenthol by stereospecific dehydrogenases from peppermint
            (Mentha piperita) leaves.
  JOURNAL   Plant Physiol. 69 (1982) 1013-1017.
  ORGANISM  Mentha piperita
PATHWAY     PATH: map00902  Monoterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.208
            ExPASy - ENZYME nomenclature database: 1.1.1.208
            ExplorEnz - The Enzyme Database: 1.1.1.208
            ERGO genome analysis and discovery system: 1.1.1.208
            BRENDA, the Enzyme Database: 1.1.1.208
            CAS: 81811-47-4
///
ENTRY       EC 1.1.1.209                Enzyme
NAME        3(or 17)alpha-hydroxysteroid dehydrogenase;
            3(17)alpha-hydroxysteroid dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3(or 17)alpha-hydroxysteroid:NAD(P)+ oxidoreductase
REACTION    androsterone + NAD(P)+ = 5alpha-androstane-3,17-dione + NAD(P)H + H+
            [RN:R02476 R02477]
ALL_REAC    R02476 R02477
SUBSTRATE   androsterone [CPD:C00523];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     5alpha-androstane-3,17-dione [CPD:C00674];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Acts on the 3alpha-hydroxy group of androgens of the
            5alpha-androstane series; and also, more slowly, on the
            17alpha-hydroxy group of both androgenic and estrogenic substrates
            (cf. EC 1.1.1.51 3(or 17)beta-hydroxysteroid dehydrogenase).
REFERENCE   1  [PMID:6955302]
  AUTHORS   Lau PC, Layne DS, Williamson DG.
  TITLE     A 3(17) alpha-hydroxysteroid dehydrogenase of female rabbit kidney
            cytosol. Purification and characterization of multiple forms of the
            enzyme.
  JOURNAL   J. Biol. Chem. 257 (1982) 9444-9.
  ORGANISM  rabbit
REFERENCE   2  [PMID:6955303]
  AUTHORS   Lau PC, Layne DS, Williamson DG.
  TITLE     Comparison of the multiple forms of the soluble 3(17)
            alpha-hydroxysteroid dehydrogenases of female rabbit kidney and
            liver.
  JOURNAL   J. Biol. Chem. 257 (1982) 9450-6.
  ORGANISM  rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.209
            ExPASy - ENZYME nomenclature database: 1.1.1.209
            ExplorEnz - The Enzyme Database: 1.1.1.209
            ERGO genome analysis and discovery system: 1.1.1.209
            BRENDA, the Enzyme Database: 1.1.1.209
            CAS: 83294-77-3
///
ENTRY       EC 1.1.1.210                Enzyme
NAME        3beta(or 20alpha)-hydroxysteroid dehydrogenase;
            progesterone reductase;
            dehydrogenase, 3beta,20alpha-hydroxy steroid;
            3beta,20alpha-hydroxysteroid oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3beta(or 20alpha)-hydroxysteroid:NADP+ oxidoreductase
REACTION    5alpha-androstan-3beta,17beta-diol + NADP+ =
            17beta-hydroxy-5alpha-androstan-3-one + NADPH + H+ [RN:R04344]
ALL_REAC    R04344
SUBSTRATE   5alpha-androstan-3beta,17beta-diol [CPD:C12525];
            NADP+ [CPD:C00006]
PRODUCT     17beta-hydroxy-5alpha-androstan-3-one [CPD:C03917];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on 20alpha-hydroxysteroids.
REFERENCE   1  [PMID:6958329]
  AUTHORS   Sharaf MA, Sweet F.
  TITLE     Dual activity at an enzyme active site: 3 beta,20
            alpha-hydroxysteroid oxidoreductase from fetal blood.
  JOURNAL   Biochemistry. 21 (1982) 4615-20.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K05883  
GENES       BTK: BT9727_3001
            BTL: BALH_2884
            SSA: SSA_2349(galE1)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.210
            ExPASy - ENZYME nomenclature database: 1.1.1.210
            ExplorEnz - The Enzyme Database: 1.1.1.210
            ERGO genome analysis and discovery system: 1.1.1.210
            BRENDA, the Enzyme Database: 1.1.1.210
            CAS: 82869-26-9
///
ENTRY       EC 1.1.1.211                Enzyme
NAME        long-chain-3-hydroxyacyl-CoA dehydrogenase;
            beta-hydroxyacyl-CoA dehydrogenase;
            long-chain 3-hydroxyacyl coenzyme A dehydrogenase;
            3-hydroxyacyl-CoA dehydrogenase;
            LCHAD
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     long-chain-(S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase
REACTION    (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+ [RN:R01778]
ALL_REAC    R01778 > R01975 R04737 R04739 R04741 R04743 R04745 R04748 R07890
            R07894 R07898 R07936 R07952
SUBSTRATE   (S)-3-hydroxyacyl-CoA [CPD:C00640];
            NAD+ [CPD:C00003]
PRODUCT     3-oxoacyl-CoA [CPD:C00264];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Acts most rapidly on derivatives with chain-length 8 or 10 (cf. EC
            1.1.1.35 3-hydroxyacyl-CoA dehydrogenase).
REFERENCE   1  [PMID:7150615]
  AUTHORS   El-Fakhri M, Middleton B.
  TITLE     The existence of an inner-membrane-bound, long acyl-chain-specific
            3-hydroxyacyl-CoA dehydrogenase in mammalian mitochondria.
  JOURNAL   Biochim. Biophys. Acta. 713 (1982) 270-9.
  ORGANISM  rat [GN:rno], rabbit
PATHWAY     PATH: map00062  Fatty acid elongation in mitochondria
            PATH: map00071  Fatty acid metabolism
            PATH: map00592  alpha-Linolenic acid metabolism
            PATH: map01040  Polyunsaturated fatty acid biosynthesis
ORTHOLOGY   KO: K07510  long-chain 3-hydroxyacyl-CoA dehydrogenase
            KO: K10527  enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase
GENES       HSA: 3030(HADHA)
            MMU: 97212(Hadha)
            RNO: 170670(Hadha)
            CFA: 475687(HADHA)
            BTA: 281810(HADHA)
            SSC: 397012(HADHA)
            GGA: 395929(HADHA)
            XLA: 444044(MGC82638)
            XTR: 394832(hadha)
            SPU: 585357(LOC585357)
            ATH: AT3G06860(MFP2) AT4G29010(AIM1)
            OSA: 4326503 4328997
            AZO: azo1933(abmB)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.211
            ExPASy - ENZYME nomenclature database: 1.1.1.211
            ExplorEnz - The Enzyme Database: 1.1.1.211
            ERGO genome analysis and discovery system: 1.1.1.211
            BRENDA, the Enzyme Database: 1.1.1.211
            CAS: 84177-52-6
///
ENTRY       EC 1.1.1.212                Enzyme
NAME        3-oxoacyl-[acyl-carrier-protein] reductase (NADH);
            3-oxoacyl-[acyl carrier protein] (reduced nicotinamide adenine
            dinucleotide) reductase;
            3-oxoacyl-[acyl-carrier-protein] reductase (NADH)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NAD+ oxidoreductase
REACTION    (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NAD+ =
            3-oxoacyl-[acyl-carrier-protein] + NADH + H+ [RN:R02766]
ALL_REAC    R02766
SUBSTRATE   (3R)-3-hydroxyacyl-[acyl-carrier-protein];
            NAD+ [CPD:C00003]
PRODUCT     3-oxoacyl-[acyl-carrier-protein];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Forms part of the fatty acid synthase system in plants. Can be
            separated from EC 1.1.1.100, 3-oxoacyl-[acyl-carrier-protein]
            reductase.
REFERENCE   1  [PMID:7075600]
  AUTHORS   Caughey I, Kekwick RG.
  TITLE     The characteristics of some components of the fatty acid synthetase
            system in the plastids from the mesocarp of avocado (Persea
            americana) fruit.
  JOURNAL   Eur. J. Biochem. 123 (1982) 553-61.
  ORGANISM  Persea americana
GENES       BPU: BPUM_1285
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.212
            ExPASy - ENZYME nomenclature database: 1.1.1.212
            ExplorEnz - The Enzyme Database: 1.1.1.212
            ERGO genome analysis and discovery system: 1.1.1.212
            BRENDA, the Enzyme Database: 1.1.1.212
            CAS: 82047-86-7
///
ENTRY       EC 1.1.1.213                Enzyme
NAME        3alpha-hydroxysteroid dehydrogenase (A-specific)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3alpha-hydroxysteroid:NAD(P)+ oxidoreductase (A-specific)
REACTION    androsterone + NAD(P)+ = 5alpha-androstane-3,17-dione + NAD(P)H + H+
            [RN:R02476 R02477]
ALL_REAC    R02476 R02477
SUBSTRATE   androsterone [CPD:C00523];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     5alpha-androstane-3,17-dione [CPD:C00674];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on other 3alpha-hydroxysteroids. A-specific with respect
            to NAD+ or NADP+ (cf. EC 1.1.1.50), 3alpha-hydroxysteroid
            dehydrogenase (B-specific)].
REFERENCE   1  [PMID:4392180]
  AUTHORS   Bjorkhem I, Danielsson H.
  TITLE     Stereochemistry of hydrogen transfer from pyridine nucleotides
            catalyzed by delta-4-3-oxosteroid 5-beta-reductase and
            3-alpha-hydroxysteroid dehydrogenase from rat liver.
  JOURNAL   Eur. J. Biochem. 12 (1970) 80-4.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Tomkins, G.M.
  TITLE     A mammalian 3alpha-hydroxysteroid dehydrogenase.
  JOURNAL   J. Biol. Chem. 218 (1956) 437-447.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K00089  3alpha-hydroxysteroid dehydrogenase (A-specific)
GENES       HSA: 1109(AKR1C4) 1645(AKR1C1) 1646(AKR1C2) 8644(AKR1C3)
STRUCTURES  PDB: 1J96  1LWI  1S1P  1S1R  1S2A  1S2C  1XJB  2F38  2FGB  2HDJ  
                 2IPJ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.213
            ExPASy - ENZYME nomenclature database: 1.1.1.213
            ExplorEnz - The Enzyme Database: 1.1.1.213
            ERGO genome analysis and discovery system: 1.1.1.213
            BRENDA, the Enzyme Database: 1.1.1.213
///
ENTRY       EC 1.1.1.214                Enzyme
NAME        2-dehydropantolactone reductase (B-specific);
            2-oxopantoyl lactone reductase;
            2-ketopantoyl lactone reductase;
            ketopantoyl lactone reductase;
            2-dehydropantoyl-lactone reductase (B-specific)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-pantolactone:NADP+ oxidoreductase (B-specific)
REACTION    (R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
            [RN:R03155]
ALL_REAC    R03155
SUBSTRATE   (R)-pantolactone [CPD:C01012];
            NADP+ [CPD:C00006]
PRODUCT     2-dehydropantolactone [CPD:C01125];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The Escherichia coli enzyme differs from that from yeast [EC
            1.1.1.168 2-dehydropantolactone reductase (A-specific)], which is
            specific for the A-face of NADP+, and in receptor requirements from
            EC 1.1.99.26 3-hydroxycyclohexanone dehydrogenase.
REFERENCE   1  [PMID:234966]
  AUTHORS   Wilken DR, King HL Jr, Dyar RE.
  TITLE     Ketopantoic acid and ketopantoyl lactone reductases.
            Stereospecificity of transfer of hydrogen from reduced nicotinamide
            adenine dinucleotide phosphate.
  JOURNAL   J. Biol. Chem. 250 (1975) 2311-4.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.214
            ExPASy - ENZYME nomenclature database: 1.1.1.214
            ExplorEnz - The Enzyme Database: 1.1.1.214
            ERGO genome analysis and discovery system: 1.1.1.214
            BRENDA, the Enzyme Database: 1.1.1.214
            CAS: 37211-75-9
///
ENTRY       EC 1.1.1.215                Enzyme
NAME        gluconate 2-dehydrogenase;
            2-keto-D-gluconate reductase;
            2-ketogluconate reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-gluconate:NADP+ oxidoreductase
REACTION    D-gluconate + NADP+ = 2-dehydro-D-gluconate + NADPH + H+ [RN:R01739]
ALL_REAC    R01739
SUBSTRATE   D-gluconate [CPD:C00257];
            NADP+ [CPD:C00006]
PRODUCT     2-dehydro-D-gluconate [CPD:C00629];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on L-idonate, D-galactonate and D-xylonate.
REFERENCE   1
  AUTHORS   Adachi, O., Chiyonobu, T., Shinagawa, E., Matsushita, K. and
            Ameyama, M.
  TITLE     Crystalline 2-ketogluconate reductase from Acetobacter ascendens,
            the second instance of crystalline enzyme in genus Acetobacter.
  JOURNAL   Agric. Biol. Chem. 42 (1978) 2057.
  ORGANISM  Acetobacter ascendens
REFERENCE   2
  AUTHORS   Chiyonobu, T., Shinagawa, E., Adachi, O. and Ameyama, M.
  TITLE     Purification, crystallization and properties of 2-ketogluconate
            reductase from Acetobacter rancens.
  JOURNAL   Agric. Biol. Chem. 40 (1976) 175-184.
  ORGANISM  Acetobacter rancens
ORTHOLOGY   KO: K00090  gluconate 2-dehydrogenase
GENES       PIC: PICST_31562(MDH97) PICST_37336(MDH98) PICST_43416(MDH99)
            DDI: DDB_0231445
            ECO: b3553(tkrA)
            ECE: Z4978(yiaE)
            ECS: ECs4438
            ECC: c4372(yiaE)
            ECI: UTI89_C4093(yiaE)
            ECP: ECP_3656
            ECV: APECO1_2895(tkrA)
            ECW: EcE24377A_4049(tkrA)
            ECX: EcHS_A3754(tkrA)
            STY: STY4156(yiaE)
            STT: t3873(yiaE)
            SPT: SPA3498(yiaE)
            SEC: SC3578(yiaE)
            STM: STM3646(yiaE)
            YPE: YPO4078
            YPK: y4096
            YPM: YP_3988(ldhA3)
            YPA: YPA_3006
            YPN: YPN_3723
            YPS: YPTB3910
            YPI: YpsIP31758_4137(tkrA)
            SFL: SF3587(yiaE)
            SFX: S4182(yiaE)
            SFV: SFV_3534(yiaE)
            SSN: SSON_3835(yiaE)
            SBO: SBO_3555(yiaE)
            SDY: SDY_4350(yiaE)
            ECA: ECA0078(tkrA)
            XCC: XCC2550
            XCB: XC_1568
            XCV: XCV2876
            XAC: XAC2724
            XOO: XOO3260
            XOM: XOO_3088(XOO3088)
            PAE: PA2263 PA3896
            PAU: PA14_13500
            PPU: PP_1261 PP_3376(kguD)
            PPF: Pput_2382
            PST: PSPTO_1215
            PSB: Psyr_1043
            PSP: PSPPH_1099
            PFL: PFL_1001 PFL_2717
            PFO: Pfl_0936 Pfl_2771 Pfl_2904
            PEN: PSEEN4562
            ACI: ACIAD1327(tkrA)
            CSA: Csal_0273
            RSO: RS05388(RSp0945)
            REU: Reut_A2281
            RME: Rmet_2446
            BXE: Bxe_A1982
            BVI: Bcep1808_1675
            BUR: Bcep18194_A5027
            BCN: Bcen_6348
            BCH: Bcen2424_1731
            BAM: Bamb_1652
            BPS: BPSL1577(tkrA)
            BPM: BURPS1710b_2286(tkrA)
            BPL: BURPS1106A_2151(tkrA)
            BPD: BURPS668_2094(tkrA)
            BTE: BTH_I2298(tkrA)
            RFR: Rfer_2144
            POL: Bpro_1736 Bpro_3078
            MPT: Mpe_A1511
            MMS: mma_0721 mma_3043
            RLE: RL4144
            BME: BMEI1952 BMEII0313
            BMF: BAB1_2178
            BJA: blr7063
            RSP: RSP_3366
            RDE: RD1_0689
            ZMO: ZMO0787
            BSU: BG12409(yvcT)
            BAN: BA5135
            BAR: GBAA5135
            BAA: BA_0009
            BAT: BAS4773
            BCE: BC4903
            BCA: BCE_5042
            BCZ: BCZK4635
            BTK: BT9727_4613
            BLI: BL03603(yvcT)
            BLD: BLi03716(yvcT)
            BCL: ABC0092
            BAY: RBAM_031930(yvcT)
            BPU: BPUM_3108
            OIH: OB2848
            DSY: DSY3442
            ANA: all8087
            PMF: P9303_11271
            PMG: P9301_12531
            PTO: PTO1438
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.215
            ExPASy - ENZYME nomenclature database: 1.1.1.215
            ExplorEnz - The Enzyme Database: 1.1.1.215
            ERGO genome analysis and discovery system: 1.1.1.215
            BRENDA, the Enzyme Database: 1.1.1.215
            CAS: 68417-42-5
///
ENTRY       EC 1.1.1.216                Enzyme
NAME        farnesol dehydrogenase;
            NADP+-farnesol dehydrogenase;
            farnesol (nicotinamide adenine dinucleotide phosphate) dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-trans,6-trans-farnesol:NADP+ 1-oxidoreductase
REACTION    2-trans,6-trans-farnesol + NADP+ = 2-trans,6-trans-farnesal + NADPH
            + H+ [RN:R03264]
ALL_REAC    R03264
SUBSTRATE   2-trans,6-trans-farnesol [CPD:C01126];
            NADP+ [CPD:C00006]
PRODUCT     2-trans,6-trans-farnesal [CPD:C03461];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts, more slowly, on 2-cis,6-trans-farnesol, geraniol,
            citronerol and nerol.
REFERENCE   1
  AUTHORS   Inoue, H., Tsuji, H. and Uritani, I.
  TITLE     Characterization and activity change of farnesol dehydrogenase in
            black rot fungus-infected sweet-potato.
  JOURNAL   Agric. Biol. Chem. 48 (1984) 733-738.
  ORGANISM  Ipomoea batatas
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.216
            ExPASy - ENZYME nomenclature database: 1.1.1.216
            ExplorEnz - The Enzyme Database: 1.1.1.216
            ERGO genome analysis and discovery system: 1.1.1.216
            BRENDA, the Enzyme Database: 1.1.1.216
            CAS: 90804-55-0
///
ENTRY       EC 1.1.1.217                Enzyme
NAME        benzyl-2-methyl-hydroxybutyrate dehydrogenase;
            benzyl 2-methyl-3-hydroxybutyrate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     benzyl-(2R,3S)-2-methyl-3-hydroxybutanoate:NADP+ 3-oxidoreductase
REACTION    benzyl (2R,3S)-2-methyl-3-hydroxybutanoate + NADP+ = benzyl
            2-methyl-3-oxobutanoate + NADPH + H+ [RN:R04370]
ALL_REAC    R04370
SUBSTRATE   benzyl (2R,3S)-2-methyl-3-hydroxybutanoate [CPD:C04561];
            NADP+ [CPD:C00006]
PRODUCT     benzyl 2-methyl-3-oxobutanoate [CPD:C04000];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on benzyl (2S,3S)-2-methyl-3-hydroxybutanoate; otherwise
            highly specific.
REFERENCE   1
  AUTHORS   Furuichi, A., Akita, H., Matsukura, H., Oishi, T. and Horikoshi, K.
  TITLE     Purification and properties of an asymmetric reduction enzyme of
            2-methyl-3-oxobutyrate in baker's yeast.
  JOURNAL   Agric. Biol. Chem. 49 (1985) 2563-2570.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.217
            ExPASy - ENZYME nomenclature database: 1.1.1.217
            ExplorEnz - The Enzyme Database: 1.1.1.217
            ERGO genome analysis and discovery system: 1.1.1.217
            BRENDA, the Enzyme Database: 1.1.1.217
            CAS: 99332-62-4
///
ENTRY       EC 1.1.1.218                Enzyme
NAME        morphine 6-dehydrogenase;
            naloxone reductase;
            reductase, naloxone
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     morphine:NAD(P)+ 6-oxidoreductase
REACTION    morphine + NAD(P)+ = morphinone + NAD(P)H + H+ [RN:R03591 R03592]
ALL_REAC    R03591 R03592
SUBSTRATE   morphine [CPD:C01516];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     morphinone [CPD:C01735];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
EFFECTOR    Mercaptoethanol [CPD:C00928]
COMMENT     Also acts on some other alkaloids, including codeine, normorphine
            and ethylmorphine, but only very slowly on 7,8-saturated derivatives
            such as dihydromorphine and dihydrocodeine. In the reverse
            direction, also reduces naloxone to the 6alpha-hydroxy analogue.
            Activated by 2-mercaptoethanol.
REFERENCE   1  [PMID:2580834]
  AUTHORS   Yamano S, Kageura E, Ishida T, Toki S.
  TITLE     Purification and characterization of guinea pig liver morphine
            6-dehydrogenase.
  JOURNAL   J. Biol. Chem. 260 (1985) 5259-64.
  ORGANISM  guinea pig
REFERENCE   2  [PMID:3539118]
  AUTHORS   Yamano S, Nishida F, Toki S.
  TITLE     Guinea-pig liver morphine 6-dehydrogenase as a naloxone reductase.
  JOURNAL   Biochem. Pharmacol. 35 (1986) 4321-6.
  ORGANISM  guinea pig
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
ORTHOLOGY   KO: K03378  morphine 6-dehydrogenase
GENES       ECW: EcE24377A_2005
            SAA: SAUSA300_2159
            LMF: LMOf2365_2565(morA)
            LWE: lwe2542
            MAV: MAV_1085 MAV_3815
            MSM: MSMEG_2407
            CGL: NCgl1003(cgl1048) NCgl1302(cgl1356)
            SEN: SACE_4695
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.218
            ExPASy - ENZYME nomenclature database: 1.1.1.218
            ExplorEnz - The Enzyme Database: 1.1.1.218
            ERGO genome analysis and discovery system: 1.1.1.218
            BRENDA, the Enzyme Database: 1.1.1.218
            CAS: 97002-71-6
///
ENTRY       EC 1.1.1.219                Enzyme
NAME        dihydrokaempferol 4-reductase;
            dihydroflavanol 4-reductase;
            dihydromyricetin reductase;
            NADPH-dihydromyricetin reductase;
            dihydroquercetin reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     cis-3,4-leucopelargonidin:NADP+ 4-oxidoreductase
REACTION    cis-3,4-leucopelargonidin + NADP+ = (+)-dihydrokaempferol + NADPH +
            H+ [RN:R03123]
ALL_REAC    R03123;
            (other) R03636 R04901 R05038 R06610
SUBSTRATE   cis-3,4-leucopelargonidin [CPD:C03648];
            NADP+ [CPD:C00006]
PRODUCT     (+)-dihydrokaempferol [CPD:C00974];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts, in the reverse direction, on (+)-dihydroquercetin and
            (+)-dihydromyricetin; each dihydroflavonol is reduced to the
            corresponding cis-flavan-3,4-diol. NAD+ can act instead of NADP+,
            but more slowly. Involved in the biosynthesis of anthocyanidins in
            plants.
REFERENCE   1
  AUTHORS   Heller, W., Forkmann, G., Britsch, L. and Grisebach, H.
  TITLE     Enzymatic reduction of (+)-dihydroflavonols to flavan-3,4-cis- diols
            with flower extracts from Matthiola incana and its role in
            anthocyanin biosynthesis.
  JOURNAL   Planta 165 (1985) 284-287.
  ORGANISM  Matthiola incana
REFERENCE   2
  AUTHORS   Stafford, H.A. and Lester, H.H.
  TITLE     Flavan-3-ol biosynthesis the conversion of (+)- dihydromyricetin to
            its flavan-3,4-diol (leucodelphinidin) and to (+)-gallocatechin by
            reductases extracted from tissue-cultures of Ginkgo biloba and
            Pseudotsuga-menziesii.
  JOURNAL   Plant Physiol. 78 (1985) 791-794.
  ORGANISM  Ginkgo biloba, Pseudotsuga menziesii
PATHWAY     PATH: map00941  Flavonoid biosynthesis
ORTHOLOGY   KO: K00091  dihydroflavonol-4-reductase
GENES       ATH: AT5G42800(DFR)
            OSA: 4323945
            PIC: PICST_58065(GRP3.3)
            AFM: AFUA_2G10280 AFUA_3G02250
            AOR: AO090010000230 AO090010000424 AO090103000435
            UMA: UM06374.1
            TET: TTHERM_00008630 TTHERM_00666390
            PAU: PA14_61280
            MCA: MCA1017
            NOC: Noc_0999
            HCH: HCH_04893
            CVI: CV_0690(hpnA)
            REU: Reut_B4897
            RME: Rmet_4170
            BMA: BMAA1958
            BXE: Bxe_B0022
            BUR: Bcep18194_B0109
            BCN: Bcen_5311 Bcen_5668
            BCH: Bcen2424_5549 Bcen2424_6032
            BAM: Bamb_5780
            BPS: BPSS2165
            BPM: BURPS1710b_A1280(hpnA)
            BTE: BTH_II2241
            NEU: NE1170(dfrA)
            NMU: Nmul_A2281
            GSU: GSU0687
            GME: Gmet_2821
            BBA: Bd0142(dfrA)
            RLE: RL0304
            BJA: bll5833 blr6564
            BRA: BRADO5042
            BBT: BBta_5514
            JAN: Jann_0529
            ZMO: ZMO0867
            GOX: GOX2253
            RRU: Rru_A0058
            MAG: amb1364
            ABA: Acid345_1741
            SSA: SSA_0314(wcaG)
            LSA: LSA1053
            MTC: MT0147
            MPA: MAP3556
            MSM: MSMEG_6563
            MMC: Mmcs_0039
            FAL: FRAAL1978
            SYN: slr1706(dfrA)
            TEL: tlr1370
            GVI: glr1747
            ANA: alr4268
            AVA: Ava_0206 Ava_1218 Ava_2547
            PMM: PMM1377
            PMC: P9515_15511
            CHU: CHU_2413
            CTE: CT1931
            CCH: Cag_0004 Cag_0240 Cag_0793
            PLT: Plut_0274
            DEH: cbdb_A1667
STRUCTURES  PDB: 2C29  2IOD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.219
            ExPASy - ENZYME nomenclature database: 1.1.1.219
            ExplorEnz - The Enzyme Database: 1.1.1.219
            ERGO genome analysis and discovery system: 1.1.1.219
            BRENDA, the Enzyme Database: 1.1.1.219
            CAS: 98668-58-7
///
ENTRY       EC 1.1.1.220                Enzyme
NAME        6-pyruvoyltetrahydropterin 2'-reductase;
            6-pyruvoyltetrahydropterin reductase;
            6PPH4(2'-oxo) reductase;
            6-pyruvoyl tetrahydropterin (2'-oxo)reductase;
            6-pyruvoyl-tetrahydropterin 2'-reductase;
            pyruvoyl-tetrahydropterin reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     6-lactoyl-5,6,7,8-tetrahydropterin:NADP+ 2'-oxidoreductase
REACTION    6-lactoyl-5,6,7,8-tetrahydropterin + NADP+ =
            6-pyruvoyltetrahydropterin + NADPH + H+ [RN:R04285]
ALL_REAC    R04285
SUBSTRATE   6-lactoyl-5,6,7,8-tetrahydropterin [CPD:C04244];
            NADP+ [CPD:C00006]
PRODUCT     6-pyruvoyltetrahydropterin [CPD:C03684];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Not identical with EC 1.1.1.153 sepiapterin reductase.
REFERENCE   1  [PMID:4004850]
  AUTHORS   Milstien S, Kaufman S.
  TITLE     Biosynthesis of tetrahydrobiopterin: conversion of dihydroneopterin
            triphosphate to tetrahydropterin intermediates.
  JOURNAL   Biochem. Biophys. Res. Commun. 128 (1985) 1099-107.
  ORGANISM  rat [GN:rno], cow [GN:bta]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K04071  6-pyruvoyltetrahydropterin 2'-reductase
GENES       HPA: HPAG1_0914
            PTO: PTO1063
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.220
            ExPASy - ENZYME nomenclature database: 1.1.1.220
            ExplorEnz - The Enzyme Database: 1.1.1.220
            ERGO genome analysis and discovery system: 1.1.1.220
            BRENDA, the Enzyme Database: 1.1.1.220
            CAS: 97089-79-7
///
ENTRY       EC 1.1.1.221                Enzyme
NAME        vomifoliol dehydrogenase;
            vomifoliol 4'-dehydrogenase;
            vomifoliol:NAD+ 4'-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     vomifoliol:NAD+ oxidoreductase
REACTION    (6S,9R)-6-hydroxy-3-oxo-alpha-ionol + NAD+ =
            (6R)-6-hydroxy-3-oxo-alpha-ionone + NADH + H+ [RN:R04412]
ALL_REAC    R04412
SUBSTRATE   (6S,9R)-6-hydroxy-3-oxo-alpha-ionol;
            NAD+ [CPD:C00003]
PRODUCT     (6R)-6-hydroxy-3-oxo-alpha-ionone;
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Oxidizes vomifoliol to dehydrovomifoliol; involved in the metabolism
            of abscisic acid in Corynebacterium sp.
REFERENCE   1
  AUTHORS   Hasegawa, S., Poling, S.M., Maier, V.P. and Bennett, R.D.
  TITLE     Metabolism of abscisic-acid bacterial conversion to
            dehydrovomifoliol and vomifoliol dehydrogenase-activity.
  JOURNAL   Phytochemistry 23 (1984) 2769-2771.
  ORGANISM  Corynebacterium
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.221
            ExPASy - ENZYME nomenclature database: 1.1.1.221
            ExplorEnz - The Enzyme Database: 1.1.1.221
            ERGO genome analysis and discovery system: 1.1.1.221
            BRENDA, the Enzyme Database: 1.1.1.221
            CAS: 94949-18-5
///
ENTRY       EC 1.1.1.222                Enzyme
NAME        (R)-4-hydroxyphenyllactate dehydrogenase;
            (R)-aromatic lactate dehydrogenase;
            D-hydrogenase, D-aryllactate
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-3-(4-hydroxyphenyl)lactate:NAD(P)+ 2-oxidoreductase
REACTION    (R)-3-(4-hydroxyphenyl)lactate + NAD(P)+ =
            3-(4-hydroxyphenyl)pyruvate + NAD(P)H + H+ [RN:R03337 R03339]
ALL_REAC    R03337 R03339;
            (other) R01370 R01371 R03336 R03338
SUBSTRATE   (R)-3-(4-hydroxyphenyl)lactate [CPD:C03964];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     3-(4-hydroxyphenyl)pyruvate [CPD:C01179];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts, more slowly, on (R)-3-phenyllactate,
            (R)-3-(indol-3-yl)lactate and (R)-lactate.
REFERENCE   1
  AUTHORS   Bode, R., Lippoldt, A. and Birnbaum, D.
  TITLE     Purification and properties of D-aromatic lactate dehydrogenase an
            enzyme involved in the catabolism of the aromatic amino acids of
            Candida maltosa.
  JOURNAL   Biochem. Physiol. Pflanzen 181 (1986) 189-198.
  ORGANISM  Candida maltosa
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.222
            ExPASy - ENZYME nomenclature database: 1.1.1.222
            ExplorEnz - The Enzyme Database: 1.1.1.222
            ERGO genome analysis and discovery system: 1.1.1.222
            BRENDA, the Enzyme Database: 1.1.1.222
            CAS: 101754-02-3
///
ENTRY       EC 1.1.1.223                Enzyme
NAME        isopiperitenol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (-)-trans-isopiperitenol:NAD+ oxidoreductase
REACTION    (-)-trans-isopiperitenol + NAD+ = (-)-isopiperitenone + NADH + H+
            [RN:R03261]
ALL_REAC    R03261
SUBSTRATE   (-)-trans-isopiperitenol [CPD:C01123];
            NAD+ [CPD:C00003]
PRODUCT     (-)-isopiperitenone [CPD:C02485];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Acts on (-)-trans-isopiperitenol, (+)-trans-piperitenol and
            (+)-trans-pulegol. Involved in the biosynthesis of menthol and
            related monoterpenes in peppermint (Mentha piperita) leaves.
REFERENCE   1  [PMID:3885858]
  AUTHORS   Kjonaas RB, Venkatachalam KV, Croteau R.
  TITLE     Metabolism of monoterpenes: oxidation of isopiperitenol to
            isopiperitenone, and subsequent isomerization to piperitenone by
            soluble enzyme preparations from peppermint (Mentha piperita)
            leaves.
  JOURNAL   Arch. Biochem. Biophys. 238 (1985) 49-60.
  ORGANISM  Mentha piperita
PATHWAY     PATH: map00902  Monoterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.223
            ExPASy - ENZYME nomenclature database: 1.1.1.223
            ExplorEnz - The Enzyme Database: 1.1.1.223
            ERGO genome analysis and discovery system: 1.1.1.223
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.223
            BRENDA, the Enzyme Database: 1.1.1.223
            CAS: 96595-05-0
///
ENTRY       EC 1.1.1.224                Enzyme
NAME        mannose-6-phosphate 6-reductase;
            NADPH-dependent mannose 6-phosphate reductase;
            mannose-6-phosphate reductase;
            6-phosphomannose reductase;
            NADP+-dependent mannose-6-P:mannitol-1-P oxidoreductase;
            NADPH-dependent M6P reductase;
            NADPH-mannose-6-P reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-mannitol-1-phosphate:NADP+ 6-oxidoreductase
REACTION    D-mannitol 1-phosphate + NADP+ = D-mannose 6-phosphate + NADPH + H+
            [RN:R01817]
ALL_REAC    R01817
SUBSTRATE   D-mannitol 1-phosphate [CPD:C00644];
            NADP+ [CPD:C00006]
PRODUCT     D-mannose 6-phosphate [CPD:C00275];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Involved in the biosynthesis of mannitol in celery (Apium
            graveolens) leaves.
REFERENCE   1
  AUTHORS   Rumpho, M.E., Edwards, G.E. and Loescher, W.H.
  TITLE     A pathway for photosynthetic carbon flow to mannitol in celery
            leaves Activity and localization of key enzymes.
  JOURNAL   Plant Physiol. 73 (1983) 869-873.
  ORGANISM  celery
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.224
            ExPASy - ENZYME nomenclature database: 1.1.1.224
            ExplorEnz - The Enzyme Database: 1.1.1.224
            ERGO genome analysis and discovery system: 1.1.1.224
            BRENDA, the Enzyme Database: 1.1.1.224
            CAS: 88747-79-9
///
ENTRY       EC 1.1.1.225                Enzyme
NAME        chlordecone reductase;
            CDR
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     chlordecone-alcohol:NADP+ 2-oxidoreductase
REACTION    chlordecone alcohol + NADP+ = chlordecone + NADPH + H+ [RN:R03716]
ALL_REAC    R03716
SUBSTRATE   chlordecone alcohol [CPD:C02817];
            NADP+ [CPD:C00006]
PRODUCT     chlordecone [CPD:C01792];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Chlordecone is an organochlorine pesticide.
REFERENCE   1  [PMID:2427522]
  AUTHORS   Molowa DT, Shayne AG, Guzelian PS.
  TITLE     Purification and characterization of chlordecone reductase from
            human liver.
  JOURNAL   J. Biol. Chem. 261 (1986) 12624-7.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K00092  chlordecone reductase
GENES       HSA: 1109(AKR1C4)
STRUCTURES  PDB: 2FVL  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.225
            ExPASy - ENZYME nomenclature database: 1.1.1.225
            ExplorEnz - The Enzyme Database: 1.1.1.225
            ERGO genome analysis and discovery system: 1.1.1.225
            BRENDA, the Enzyme Database: 1.1.1.225
            CAS: 102484-73-1
///
ENTRY       EC 1.1.1.226                Enzyme
NAME        4-hydroxycyclohexanecarboxylate dehydrogenase;
            trans-4-hydroxycyclohexanecarboxylate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     trans-4-hydroxycyclohexanecarboxylate:NAD+ 4-oxidoreductase
REACTION    trans-4-hydroxycyclohexanecarboxylate + NAD+ =
            4-oxocyclohexanecarboxylate + NADH + H+ [RN:R04307]
ALL_REAC    R04307
SUBSTRATE   trans-4-hydroxycyclohexanecarboxylate [CPD:C04404];
            NAD+ [CPD:C00003]
PRODUCT     4-oxocyclohexanecarboxylate [CPD:C03767];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The enzyme from Corynebacterium cyclohexanicum is highly specific
            for the trans-4-hydroxy derivative.
REFERENCE   1  [PMID:3292236]
  AUTHORS   Obata H, Uebayasi M, Kaneda T.
  TITLE     Purification and properties of 4-hydroxycyclohexanecarboxylate
            dehydrogenase from Corynebacterium cyclohexanicum.
  JOURNAL   Eur. J. Biochem. 174 (1988) 451-8.
  ORGANISM  Corynebacterium cyclohexanicum
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.226
            ExPASy - ENZYME nomenclature database: 1.1.1.226
            ExplorEnz - The Enzyme Database: 1.1.1.226
            ERGO genome analysis and discovery system: 1.1.1.226
            BRENDA, the Enzyme Database: 1.1.1.226
            CAS: 67272-36-0
///
ENTRY       EC 1.1.1.227                Enzyme
NAME        (-)-borneol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (-)-borneol:NAD+ oxidoreductase
REACTION    (-)-borneol + NAD+ = (-)-camphor + NADH + H+ [RN:R02945]
ALL_REAC    R02945
SUBSTRATE   (-)-borneol [CPD:C01766];
            NAD+ [CPD:C00003]
PRODUCT     (-)-camphor [CPD:C00809];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     NADP+ can also act, but more slowly.
REFERENCE   1  [PMID:3310901]
  AUTHORS   Dehal SS, Croteau R.
  TITLE     Metabolism of monoterpenes: specificity of the dehydrogenases
            responsible for the biosynthesis of camphor, 3-thujone, and
            3-isothujone.
  JOURNAL   Arch. Biochem. Biophys. 258 (1987) 287-91.
  ORGANISM  tansy
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.227
            ExPASy - ENZYME nomenclature database: 1.1.1.227
            ExplorEnz - The Enzyme Database: 1.1.1.227
            ERGO genome analysis and discovery system: 1.1.1.227
            BRENDA, the Enzyme Database: 1.1.1.227
            CAS: 111940-48-8
///
ENTRY       EC 1.1.1.228                Enzyme
NAME        (+)-sabinol dehydrogenase;
            (+)-cis-sabinol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (+)-cis-sabinol:NAD+ oxidoreductase
REACTION    (+)-cis-sabinol + NAD+ = (+)-sabinone + NADH + H+ [RN:R03745]
ALL_REAC    R03745
SUBSTRATE   (+)-cis-sabinol [CPD:C02213];
            NAD+ [CPD:C00003]
PRODUCT     (+)-sabinone [CPD:C01868];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     NADP+ can also act, but more slowly. Involved in the biosynthesis of
            (+)-3-thujone and (-)-3-isothujone.
REFERENCE   1  [PMID:3310901]
  AUTHORS   Dehal SS, Croteau R.
  TITLE     Metabolism of monoterpenes: specificity of the dehydrogenases
            responsible for the biosynthesis of camphor, 3-thujone, and
            3-isothujone.
  JOURNAL   Arch. Biochem. Biophys. 258 (1987) 287-91.
  ORGANISM  sage , tansy
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.228
            ExPASy - ENZYME nomenclature database: 1.1.1.228
            ExplorEnz - The Enzyme Database: 1.1.1.228
            ERGO genome analysis and discovery system: 1.1.1.228
            BRENDA, the Enzyme Database: 1.1.1.228
            CAS: 111940-50-2
///
ENTRY       EC 1.1.1.229                Enzyme
NAME        diethyl 2-methyl-3-oxosuccinate reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     diethyl-(2R,3R)-2-methyl-3-hydroxysuccinate:NADP+ 3-oxidoreductase
REACTION    diethyl (2R,3R)-2-methyl-3-hydroxysuccinate + NADP+ = diethyl
            2-methyl-3-oxosuccinate + NADPH + H+ [RN:R04387]
ALL_REAC    R04387
SUBSTRATE   diethyl (2R,3R)-2-methyl-3-hydroxysuccinate [CPD:C04586];
            NADP+ [CPD:C00006]
PRODUCT     diethyl 2-methyl-3-oxosuccinate [CPD:C04067];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on diethyl (2S,3R)-2-methyl-3-hydroxysuccinate; and on the
            corresponding dimethyl esters.
REFERENCE   1
  AUTHORS   Furuichi, A., Akita, H., Matsukura, H., Oishi, T. and Horikoshi, K.
  TITLE     Purification and properties of an asymmetric reduction of diethyl
            2-methyl-3-oxosuccinate in Saccharomyces fermentati.
  JOURNAL   Agric. Biol. Chem. 51 (1987) 293-299.
  ORGANISM  Saccharomyces fermentati
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.229
            ExPASy - ENZYME nomenclature database: 1.1.1.229
            ExplorEnz - The Enzyme Database: 1.1.1.229
            ERGO genome analysis and discovery system: 1.1.1.229
            BRENDA, the Enzyme Database: 1.1.1.229
            CAS: 110369-21-6
///
ENTRY       EC 1.1.1.230                Enzyme
NAME        3alpha-hydroxyglycyrrhetinate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3alpha-hydroxyglycyrrhetinate:NADP+ 3-oxidoreductase
REACTION    3alpha-hydroxyglycyrrhetinate + NADP+ = 3-oxoglycyrrhetinate + NADPH
            + H+ [RN:R04099]
ALL_REAC    R04099
SUBSTRATE   3alpha-hydroxyglycyrrhetinate [CPD:C03930];
            NADP+ [CPD:C00006]
PRODUCT     3-oxoglycyrrhetinate [CPD:C02943];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Highly specific to 3alpha-hydroxy derivatives of glycyrrhetinate and
            its analogues. Not identical to EC 1.1.1.50 3alpha-hydroxysteroid
            dehydrogenase (B-specific).
REFERENCE   1  [PMID:3164718]
  AUTHORS   Akao T, Akao T, Hattori M, Namba T, Kobashi K.
  TITLE     Purification and properties of 3 alpha-hydroxyglycyrrhetinate
            dehydrogenase of Clostridium innocuum from human intestine.
  JOURNAL   J. Biochem. (Tokyo). 103 (1988) 504-7.
  ORGANISM  Clostridium innocuum
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.230
            ExPASy - ENZYME nomenclature database: 1.1.1.230
            ExplorEnz - The Enzyme Database: 1.1.1.230
            ERGO genome analysis and discovery system: 1.1.1.230
            BRENDA, the Enzyme Database: 1.1.1.230
            CAS: 114308-07-5
///
ENTRY       EC 1.1.1.231                Enzyme
NAME        15-hydroxyprostaglandin-I dehydrogenase (NADP+);
            prostacyclin dehydrogenase;
            PG I2 dehydrogenase;
            prostacyclin dehydrogenase;
            NADP+-linked 15-hydroxyprostaglandin (prostacyclin) dehydrogenase;
            NADP+-dependent PGI2-specific 15-hydroxyprostaglandin dehydrogenase;
            15-hydroxyprostaglandin-I dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoa
            te:NADP+ 15-oxidoreductase
REACTION    (5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-
            dienoate + NADP+ =
            (5Z,13E)-6,9alpha-epoxy-11alpha-hydroxy-15-oxoprosta-5,13-dienoate +
            NADPH + H+ [RN:R03520]
ALL_REAC    R03520
SUBSTRATE   (5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-
            dienoate [CPD:C01312];
            NADP+ [CPD:C00006]
PRODUCT     (5Z,13E)-6,9alpha-epoxy-11alpha-hydroxy-15-oxoprosta-5,13-dienoate
            [CPD:C04835];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Specific for prostaglandin I2.
REFERENCE   1  [PMID:6182444]
  AUTHORS   Korff JM, Jarabak J.
  TITLE     Isolation and properties of an NADP+-dependent PGI2-specific
            15-hydroxyprostaglandin dehydrogenase from rabbit kidney.
  JOURNAL   Methods. Enzymol. 86 (1982) 152-5.
  ORGANISM  rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.231
            ExPASy - ENZYME nomenclature database: 1.1.1.231
            ExplorEnz - The Enzyme Database: 1.1.1.231
            ERGO genome analysis and discovery system: 1.1.1.231
            BRENDA, the Enzyme Database: 1.1.1.231
            CAS: 79468-49-8
///
ENTRY       EC 1.1.1.232                Enzyme
NAME        15-hydroxyicosatetraenoate dehydrogenase;
            15-hydroxyeicosatetraenoate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (15S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate:NAD(P)+
            15-oxidoreductase
REACTION    (15S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)+ =
            15-oxo-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)H + H+
            [RN:R04517 R04518]
ALL_REAC    R04517 R04518
SUBSTRATE   (15S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate [CPD:C04742];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     15-oxo-5,8,11-cis-13-trans-icosatetraenoate [CPD:C04577];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:3052453]
  AUTHORS   Sok DE, Kang JB, Shin HD.
  TITLE     15-Hydroxyeicosatetraenoic acid dehydrogenase activity in microsomal
            fraction of mouse liver homogenate.
  JOURNAL   Biochem. Biophys. Res. Commun. 156 (1988) 524-9.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map00590  Arachidonic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.232
            ExPASy - ENZYME nomenclature database: 1.1.1.232
            ExplorEnz - The Enzyme Database: 1.1.1.232
            ERGO genome analysis and discovery system: 1.1.1.232
            BRENDA, the Enzyme Database: 1.1.1.232
            CAS: 117910-46-0
///
ENTRY       EC 1.1.1.233                Enzyme
NAME        N-acylmannosamine 1-dehydrogenase;
            N-acylmannosamine dehydrogenase;
            N-acetyl-D-mannosamine dehydrogenase;
            N-acyl-D-mannosamine dehydrogenase;
            N-acylmannosamine dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N-acyl-D-mannosamine:NAD+ 1-oxidoreductase
REACTION    N-acyl-D-mannosamine + NAD+ = N-acyl-D-mannosaminolactone + NADH +
            H+ [RN:R02651]
ALL_REAC    R02651
SUBSTRATE   N-acyl-D-mannosamine [CPD:C00625];
            NAD+ [CPD:C00003]
PRODUCT     N-acyl-D-mannosaminolactone [CPD:C03792];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Acts on acetyl-D-mannosamine and glycolyl-D-mannosamine. Highly
            specific.
REFERENCE   1  [PMID:3240988]
  AUTHORS   Horiuchi T, Kurokawa T.
  TITLE     Purification and properties of N-acyl-D-mannosamine dehydrogenase
            from Flavobacterium sp. 141-8.
  JOURNAL   J. Biochem. (Tokyo). 104 (1988) 466-71.
  ORGANISM  Flavobacterium sp.
GENES       SAA: SAUSA300_0166(cap5O)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.233
            ExPASy - ENZYME nomenclature database: 1.1.1.233
            ExplorEnz - The Enzyme Database: 1.1.1.233
            ERGO genome analysis and discovery system: 1.1.1.233
            BRENDA, the Enzyme Database: 1.1.1.233
            CAS: 117698-08-5
///
ENTRY       EC 1.1.1.234                Enzyme
NAME        flavanone 4-reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (2S)-flavan-4-ol:NADP+ 4-oxidoreductase
REACTION    (2S)-flavan-4-ol + NADP+ = (2S)-flavanone + NADPH + H+ [RN:R03827]
ALL_REAC    R03827;
            (other) R04901 R06610
SUBSTRATE   (2S)-flavan-4-ol [CPD:C02345];
            NADP+ [CPD:C00006]
PRODUCT     (2S)-flavanone [CPD:C02099];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Involved in the biosynthesis of 3-deoxyanthocyanidins from
            flavanones such as naringenin or eriodictyol.
REFERENCE   1
  AUTHORS   Stich, K. and Forkmann, G.
  TITLE     Biosynthesis of 3-deoxyanthocyanins with flower extracts from
            Sinningia cardinalis.
  JOURNAL   Phytochemistry 27 (1988) 785-789.
  ORGANISM  Sinningia cardinalis
PATHWAY     PATH: map00941  Flavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.234
            ExPASy - ENZYME nomenclature database: 1.1.1.234
            ExplorEnz - The Enzyme Database: 1.1.1.234
            ERGO genome analysis and discovery system: 1.1.1.234
            BRENDA, the Enzyme Database: 1.1.1.234
            CAS: 115232-53-6
///
ENTRY       EC 1.1.1.235                Enzyme
NAME        8-oxocoformycin reductase;
            8-ketodeoxycoformycin reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     coformycin:NADP+ 8-oxidoreductase
REACTION    coformycin + NADP+ = 8-oxocoformycin + NADPH + H+ [RN:R03667]
ALL_REAC    R03667
SUBSTRATE   coformycin [CPD:C01677];
            NADP+ [CPD:C00006]
PRODUCT     8-oxocoformycin [CPD:C02243];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     B-specific with respect to NADPH. Also reduces 8-oxodeoxy-coformycin
            to the nucleoside antibiotic deoxycoformycin.
REFERENCE   1  [PMID:3052586]
  AUTHORS   Hanvey JC, Hawkins ES, Baker DC, Suhadolnik RJ.
  TITLE     8-Ketodeoxycoformycin and 8-ketocoformycin as intermediates in the
            biosynthesis of 2'-deoxycoformycin and coformycin.
  JOURNAL   Biochemistry. 27 (1988) 5790-5.
  ORGANISM  Streptomyces antibioticus
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.235
            ExPASy - ENZYME nomenclature database: 1.1.1.235
            ExplorEnz - The Enzyme Database: 1.1.1.235
            ERGO genome analysis and discovery system: 1.1.1.235
            BRENDA, the Enzyme Database: 1.1.1.235
            CAS: 114995-16-3
///
ENTRY       EC 1.1.1.236                Enzyme
NAME        tropinone reductase II;
            tropinone (psi-tropine-forming) reductase;
            pseudotropine forming tropinone reductase;
            tropinone reductase (ambiguous);
            TR-II
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     pseudotropine:NADP+ 3-oxidoreductase
REACTION    pseudotropine + NADP+ = tropinone + NADPH + H+ [RN:R06734]
ALL_REAC    R06734;
            (other) R02832
SUBSTRATE   pseudotropine [CPD:C02066];
            NADP+ [CPD:C00006]
PRODUCT     tropinone [CPD:C00783];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     This enzyme along with EC 1.1.1.206, tropine dehydrogenase,
            represents a branch point in tropane alkaloid metabolism [3].
            Tropine (the product of EC 1.1.1.206) is incorporated into
            hyoscyamine and scopolamine whereas pseudotropine (the product of EC
            1.1.1.236) is the first specific metabolite on the pathway to the
            calystegines [3]. Both enzymes are always found together in any
            given tropane-alkaloid-producing species, have a common substrate,
            tropinone, and are strictly stereospecific [2].
REFERENCE   1
  AUTHORS   Drager, B., Hashimoto, T. and Yamada, Y.
  TITLE     Purification and characterization of pseudotropine forming tropinone
            reductase from Hyoscyamus niger root cultures.
  JOURNAL   Agric. Biol. Chem. 52 (1988) 2663-2667.
  ORGANISM  Hyoscyamus niger
REFERENCE   2
  AUTHORS   Couladis, M.M, Friesen, J.B., Landgrebe, M.E. and Leete, E.
  TITLE     Enzymes catalysing the reduction of tropinone to tropine and
            &psi;-tropine isolated from the roots of Datura innoxia.
  JOURNAL   Pytochemistry 30 (1991) 801-805.
REFERENCE   3  [PMID:8415746]
  AUTHORS   Nakajima K, Hashimoto T, Yamada Y.
  TITLE     Two tropinone reductases with different stereospecificities are
            short-chain dehydrogenases evolved from a common ancestor.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 9591-5.
REFERENCE   4  [PMID:16426652]
  AUTHORS   Drager B.
  TITLE     Tropinone reductases, enzymes at the branch point of tropane
            alkaloid metabolism.
  JOURNAL   Phytochemistry. 67 (2006) 327-37.
PATHWAY     PATH: map00960  Alkaloid biosynthesis II
ORTHOLOGY   KO: K05354  tropinone reductase
STRUCTURES  PDB: 1AE1  1IPE  1IPF  1XHL  2AE1  2AE2  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.236
            ExPASy - ENZYME nomenclature database: 1.1.1.236
            ExplorEnz - The Enzyme Database: 1.1.1.236
            ERGO genome analysis and discovery system: 1.1.1.236
            BRENDA, the Enzyme Database: 1.1.1.236
            CAS: 136111-61-0
///
ENTRY       EC 1.1.1.237                Enzyme
NAME        hydroxyphenylpyruvate reductase;
            HPRP
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4-hydroxyphenyllactate:NAD+ oxidoreductase
REACTION    3-(4-hydroxyphenyl)lactate + NAD+ = 3-(4-hydroxyphenyl)pyruvate +
            NADH + H+ [RN:R03336]
ALL_REAC    R03336;
            (other) R01370 R01371 R03338 R03373
SUBSTRATE   3-(4-hydroxyphenyl)lactate [CPD:C03672];
            NAD+ [CPD:C00003]
PRODUCT     3-(4-hydroxyphenyl)pyruvate [CPD:C01179];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts on 3-(3,4-dihydroxyphenyl)lactate. Involved with EC
            2.3.1.140 rosmarinate synthase in the biosynthesis of rosmarinic
            acid.
REFERENCE   1
  AUTHORS   Petersen, M. and Alfermann, A.W.
  TITLE     Two new enzymes of rosmarinic acid biosynthesis from cell cultures
            of Coleus blumei: hydroxyphenylpyruvate reductase and rosmarinic
            acid synthase.
  JOURNAL   Z. Naturforsch. C: Biosci. 43 (1988) 501-504.
  ORGANISM  Coleus blumei
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.237
            ExPASy - ENZYME nomenclature database: 1.1.1.237
            ExplorEnz - The Enzyme Database: 1.1.1.237
            ERGO genome analysis and discovery system: 1.1.1.237
            BRENDA, the Enzyme Database: 1.1.1.237
            CAS: 117590-77-9
///
ENTRY       EC 1.1.1.238                Enzyme
NAME        12beta-hydroxysteroid dehydrogenase;
            12beta-hydroxy steroid (nicotinamide adenine dinucleotide phosphate)
            dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     12beta-hydroxysteroid:NADP+ 12-oxidoreductase
REACTION    3alpha,7alpha,12beta-trihydroxy-5beta-cholanate + NADP+ =
            3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate + NADPH + H+
            [RN:R03495]
ALL_REAC    R03495
SUBSTRATE   3alpha,7alpha,12beta-trihydroxy-5beta-cholanate [CPD:C04661];
            NADP+ [CPD:C00006]
PRODUCT     3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate [CPD:C01292];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Acts on a number of bile acids, both in their free and conjugated
            forms.
REFERENCE   1  [PMID:3167086]
  AUTHORS   Edenharder R, Pfutzner A.
  TITLE     Characterization of NADP-dependent 12 beta-hydroxysteroid
            dehydrogenase from Clostridium paraputrificum.
  JOURNAL   Biochim. Biophys. Acta. 962 (1988) 362-70.
  ORGANISM  Clostridium pasteurianum
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.238
            ExPASy - ENZYME nomenclature database: 1.1.1.238
            ExplorEnz - The Enzyme Database: 1.1.1.238
            ERGO genome analysis and discovery system: 1.1.1.238
            BRENDA, the Enzyme Database: 1.1.1.238
            CAS: 118390-62-8
///
ENTRY       EC 1.1.1.239                Enzyme
NAME        3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+);
            3alpha,17beta-hydroxy steroid dehydrogenase;
            3alpha(17beta)-HSD;
            3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3alpha(or 17beta)-hydroxysteroid:NAD+ oxidoreductase
REACTION    testosterone + NAD+ = androst-4-ene-3,17-dione + NADH + H+
            [RN:R01836]
ALL_REAC    R01836
SUBSTRATE   testosterone [CPD:C00535];
            NAD+ [CPD:C00003]
PRODUCT     androst-4-ene-3,17-dione [CPD:C00280];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts on other 17beta-hydroxysteroids, on the 3alpha-hydroxy
            group of pregnanes and bile acids, and on benzene dihydrodiol.
            Different from EC 1.1.1.50 3alpha-hydroxysteroid dehydrogenase
            (B-specific) or EC 1.1.1.213 3alpha-hydroxysteroid dehydrogenase
            (A-specific).
REFERENCE   1  [PMID:2317205]
  AUTHORS   Ohmura M, Hara A, Nakagawa M, Sawada H.
  TITLE     Demonstration of 3 alpha(17 beta)-hydroxysteroid dehydrogenase
            distinct from 3 alpha-hydroxysteroid dehydrogenase in hamster liver.
  JOURNAL   Biochem. J. 266 (1990) 583-9.
  ORGANISM  hamster
PATHWAY     PATH: map00150  Androgen and estrogen metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.239
            ExPASy - ENZYME nomenclature database: 1.1.1.239
            ExplorEnz - The Enzyme Database: 1.1.1.239
            ERGO genome analysis and discovery system: 1.1.1.239
            BRENDA, the Enzyme Database: 1.1.1.239
            CAS: 126469-82-7
///
ENTRY       EC 1.1.1.240                Enzyme
NAME        N-acetylhexosamine 1-dehydrogenase;
            N-acetylhexosamine dehydrogenase;
            N-acetyl-D-hexosamine dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N-acetyl-D-hexosamine:NAD+ 1-oxidoreductase
REACTION    N-acetyl-D-glucosamine + NAD+ = N-acetyl-D-glucosaminate + NADH + H+
            [RN:R01202]
ALL_REAC    R01202
SUBSTRATE   N-acetyl-D-glucosamine [CPD:C00140];
            NAD+ [CPD:C00003]
PRODUCT     N-acetyl-D-glucosaminate [CPD:C01133];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts on N-acetylgalactosamine and, more slowly, on
            N-acetylmannosamine.
REFERENCE   1
  AUTHORS   Horiuchi, T. and Kurokawa, T.
  TITLE     Purification and characterization of N-acetyl-D-hexosamine
            dehydrogenase from Pseudomonas sp no 53.
  JOURNAL   Agric. Biol. Chem. 53 (1989) 1919-1925.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.240
            ExPASy - ENZYME nomenclature database: 1.1.1.240
            ExplorEnz - The Enzyme Database: 1.1.1.240
            ERGO genome analysis and discovery system: 1.1.1.240
            BRENDA, the Enzyme Database: 1.1.1.240
            CAS: 122785-18-6
///
ENTRY       EC 1.1.1.241                Enzyme
NAME        6-endo-hydroxycineole dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     6-endo-hydroxycineole:NAD+ 6-oxidoreductase
REACTION    6-endo-hydroxycineole + NAD+ = 6-oxocineole + NADH + H+ [RN:R02994]
ALL_REAC    R02994
SUBSTRATE   6-endo-hydroxycineole [CPD:C03092];
            NAD+ [CPD:C00003]
PRODUCT     6-oxocineole [CPD:C00848];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Williams, D.R., Trudgill, P.W. and Taylor, D.G.
  TITLE     Metabolism of 1,8-cineole by Rhodococcus species: ring cleavage
            reactions.
  JOURNAL   J. Gen. Microbiol. 135 (1989) 1957-1967.
  ORGANISM  Rhodococcus sp.
PATHWAY     PATH: map00900  Terpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.241
            ExPASy - ENZYME nomenclature database: 1.1.1.241
            ExplorEnz - The Enzyme Database: 1.1.1.241
            ERGO genome analysis and discovery system: 1.1.1.241
            BRENDA, the Enzyme Database: 1.1.1.241
            CAS: 122933-68-0
///
ENTRY       EC 1.1.1.242      Obsolete  Enzyme
NAME        Transferred to 1.3.1.69
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Transferred entry: now EC 1.3.1.69 zeatin reductase (EC 1.1.1.242
            created 1992, deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.242
            ExPASy - ENZYME nomenclature database: 1.1.1.242
            ExplorEnz - The Enzyme Database: 1.1.1.242
            ERGO genome analysis and discovery system: 1.1.1.242
            BRENDA, the Enzyme Database: 1.1.1.242
///
ENTRY       EC 1.1.1.243                Enzyme
NAME        carveol dehydrogenase;
            (-)-trans-carveol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (-)-trans-carveol:NADP+ oxidoreductase
REACTION    (-)-trans-carveol + NADP+ = (-)-carvone + NADPH + H+ [RN:R03114]
ALL_REAC    R03114
SUBSTRATE   (-)-trans-carveol [CPD:C00964];
            NADP+ [CPD:C00006]
PRODUCT     (-)-carvone [CPD:C01767];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Gershenzon, J., Maffei, M. and Croteau, R.
  TITLE     Biochemical and histochemical-localization of monoterpene
            biosynthesis in the glandular trichomes of spearmint (Mentha
            spicata).
  JOURNAL   Plant Physiol. 89 (1989) 1351-1357.
  ORGANISM  Mentha spicata
PATHWAY     PATH: map00902  Monoterpenoid biosynthesis
            PATH: map00903  Limonene and pinene degradation
GENES       RHA: RHA1_ro00234 RHA1_ro00374 RHA1_ro00391 RHA1_ro02918
                 RHA1_ro10227
            FAL: FRAAL1387
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.243
            ExPASy - ENZYME nomenclature database: 1.1.1.243
            ExplorEnz - The Enzyme Database: 1.1.1.243
            ERGO genome analysis and discovery system: 1.1.1.243
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.243
            BRENDA, the Enzyme Database: 1.1.1.243
            CAS: 122653-66-1
///
ENTRY       EC 1.1.1.244                Enzyme
NAME        methanol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     methanol:NAD+ oxidoreductase
REACTION    methanol + NAD+ = formaldehyde + NADH + H+ [RN:R00605]
ALL_REAC    R00605
SUBSTRATE   methanol [CPD:C00132];
            NAD+ [CPD:C00003]
PRODUCT     formaldehyde [CPD:C00067];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:2673121]
  AUTHORS   Arfman N, Watling EM, Clement W, van Oosterwijk RJ, de Vries GE,
            Harder W, Attwood MM, Dijkhuizen L.
  TITLE     Methanol metabolism in thermotolerant methylotrophic Bacillus
            strains involving a novel catabolic NAD-dependent methanol
            dehydrogenase as a key enzyme.
  JOURNAL   Arch. Microbiol. 152 (1989) 280-8.
  ORGANISM  Bacillus sp.
PATHWAY     PATH: map00680  Methane metabolism
ORTHOLOGY   KO: K00093  methanol dehydrogenase
GENES       YPE: YPO0327
            YPK: y0584
            YPM: YP_0482(eutG)
            YPA: YPA_3955
            YPN: YPN_3343
            YPS: YPTB0382
            AHA: AHA_1506
            AZO: azo2862(moxR2)
            AAU: AAur_0652
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.244
            ExPASy - ENZYME nomenclature database: 1.1.1.244
            ExplorEnz - The Enzyme Database: 1.1.1.244
            ERGO genome analysis and discovery system: 1.1.1.244
            BRENDA, the Enzyme Database: 1.1.1.244
            CAS: 74506-37-9
///
ENTRY       EC 1.1.1.245                Enzyme
NAME        cyclohexanol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     cyclohexanol:NAD+ oxidoreductase
REACTION    cyclohexanol + NAD+ = cyclohexanone + NADH + H+ [RN:R02229]
ALL_REAC    R02229
SUBSTRATE   cyclohexanol [CPD:C00854];
            NAD+ [CPD:C00003]
PRODUCT     cyclohexanone [CPD:C00414];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also oxidizes some other alicyclic alcohols and diols.
REFERENCE   1
  AUTHORS   Dangel, W., Tschech, A. and Fuchs, G.
  TITLE     Enzyme-reactions involved in anaerobic cyclohexanol metabolism by a
            denitrifying Pseudomonas species.
  JOURNAL   Arch. Microbiol. 152 (1989) 273-279.
  ORGANISM  Pseudomonas species
REFERENCE   2  [PMID:1261]
  AUTHORS   Donoghue NA, Trudgill PW.
  TITLE     The metabolism of cyclohexanol by Acinetobacter NCIB 9871.
  JOURNAL   Eur. J. Biochem. 60 (1975) 1-7.
  ORGANISM  Acinetobacter sp.
REFERENCE   3  [PMID:16346796]
  AUTHORS   Trower MK, Buckland RM, Higgins R, Griffin M.
  TITLE     Isolation and Characterization of a Cyclohexane-Metabolizing
            Xanthobacter sp.
  JOURNAL   Appl. Environ. Microbiol. 49 (1985) 1282-1289.
  ORGANISM  Xanthobacter sp.
PATHWAY     PATH: map00930  Caprolactam degradation
GENES       REH: H16_B0601
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.245
            ExPASy - ENZYME nomenclature database: 1.1.1.245
            ExplorEnz - The Enzyme Database: 1.1.1.245
            ERGO genome analysis and discovery system: 1.1.1.245
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.245
            BRENDA, the Enzyme Database: 1.1.1.245
            CAS: 63951-98-4
///
ENTRY       EC 1.1.1.246                Enzyme
NAME        pterocarpin synthase;
            pterocarpan synthase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     medicarpin:NADP+ 2'-oxidoreductase
REACTION    medicarpin + NADP+ + H2O = vestitone + NADPH + H+ [RN:R02915]
ALL_REAC    R02915;
            (other) R07728 R07748 R07752
SUBSTRATE   medicarpin;
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     vestitone [CPD:C00786];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Catalyses the final step in the biosynthesis of the pterocarpin
            phytoalexins medicarpin and maackiain.
REFERENCE   1
  AUTHORS   Bless, W. and Barz, W.
  TITLE     Isolation of pterocarpan synthase, the terminal enzyme of
            pterocarpan phytoalexin biosynthesis in cell-suspension cultures of
            Cicer arietinum.
  JOURNAL   FEBS Lett. 235 (1988) 47-50.
  ORGANISM  Cicer arietinum
PATHWAY     PATH: map00943  Isoflavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.246
            ExPASy - ENZYME nomenclature database: 1.1.1.246
            ExplorEnz - The Enzyme Database: 1.1.1.246
            ERGO genome analysis and discovery system: 1.1.1.246
            BRENDA, the Enzyme Database: 1.1.1.246
            CAS: 118477-70-6
///
ENTRY       EC 1.1.1.247                Enzyme
NAME        codeinone reductase (NADPH)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     codeine:NADP+ oxidoreductase
REACTION    codeine + NADP+ = codeinone + NADPH + H+ [RN:R05124]
ALL_REAC    R05124
SUBSTRATE   codeine [CPD:C06174];
            NADP+ [CPD:C00006]
PRODUCT     codeinone [CPD:C06171];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Catalyses the reversible reduction of codeinone to codeine, which is
            a direct precursor of morphine in the opium poppy plant, Papaver
            somniferum.
REFERENCE   1
  AUTHORS   Lenz, R. and Zenk, M.H.
  TITLE     Stereoselective reduction of codeinone, the penultimate step during
            morphine biosynthesis in Papaver somniferum.
  JOURNAL   Tetrahedron Lett. 36 (1995) 2449-2452.
REFERENCE   2  [PMID:7588736]
  AUTHORS   Lenz R, Zenk MH.
  TITLE     Purification and properties of codeinone reductase (NADPH) from
            Papaver somniferum cell cultures and differentiated plants.
  JOURNAL   Eur. J. Biochem. 233 (1995) 132-9.
  ORGANISM  Papaver somniferum
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.247
            ExPASy - ENZYME nomenclature database: 1.1.1.247
            ExplorEnz - The Enzyme Database: 1.1.1.247
            ERGO genome analysis and discovery system: 1.1.1.247
            BRENDA, the Enzyme Database: 1.1.1.247
            CAS: 153302-41-1
///
ENTRY       EC 1.1.1.248                Enzyme
NAME        salutaridine reductase (NADPH)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     salutaridinol:NADP+ 7-oxidoreductase
REACTION    salutaridinol + NADP+ = salutaridine + NADPH + H+ [RN:R04697]
ALL_REAC    R04697
SUBSTRATE   salutaridinol [CPD:C05220];
            NADP+ [CPD:C00006]
PRODUCT     salutaridine [CPD:C05179];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Catalyses the reversible reduction of salutaridine to salutaridinol,
            which is a direct precursor of morphinan alkaloids in the poppy
            plant.
REFERENCE   1
  AUTHORS   Gerady, R. and Zenk, M.H.
  TITLE     Purification and characterization of salutaridine:NADPH
            7-oxidoreductase from Papaver somniferum.
  JOURNAL   Phytochemistry 34 (1993) 125-132.
  ORGANISM  Papaver somniferum, Papaver bracteatum
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.248
            ExPASy - ENZYME nomenclature database: 1.1.1.248
            ExplorEnz - The Enzyme Database: 1.1.1.248
            ERGO genome analysis and discovery system: 1.1.1.248
            BRENDA, the Enzyme Database: 1.1.1.248
            CAS: 152743-95-8
///
ENTRY       EC 1.1.1.249      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: Provisional entry deleted. Revised and reinstated as
            EC 2.5.1.46 deoxyhypusine synthase. (EC 1.1.1.249 provisional
            version created 1999, deleted 1999 (reinstated 2001 as EC 2.5.1.46))
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.249
            ExPASy - ENZYME nomenclature database: 1.1.1.249
            ExplorEnz - The Enzyme Database: 1.1.1.249
            ERGO genome analysis and discovery system: 1.1.1.249
            BRENDA, the Enzyme Database: 1.1.1.249
///
ENTRY       EC 1.1.1.250                Enzyme
NAME        D-arabinitol 2-dehydrogenase;
            D-arabinitol 2-dehydrogenase (ribulose-forming)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-arabinitol:NAD+ 2-oxidoreductase (D-ribulose-forming)
REACTION    D-arabinitol + NAD+ = D-ribulose + NADH + H+ [RN:R07134]
ALL_REAC    R07134
SUBSTRATE   D-arabinitol [CPD:C01904];
            NAD+ [CPD:C00003]
PRODUCT     D-ribulose [CPD:C00309];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:8407803]
  AUTHORS   Wong B, Murray JS, Castellanos M, Croen KD.
  TITLE     D-arabitol metabolism in Candida albicans: studies of the
            biosynthetic pathway and the gene that encodes NAD-dependent
            D-arabitol dehydrogenase.
  JOURNAL   J. Bacteriol. 175 (1993) 6314-20.
  ORGANISM  Candida albicans [GN:cal]
REFERENCE   2  [PMID:8250887]
  AUTHORS   Quong MW, Miyada CG, Switchenko AC, Goodman TC.
  TITLE     Identification, purification, and characterization of a
            D-arabinitol-specific dehydrogenase from Candida tropicalis.
  JOURNAL   Biochem. Biophys. Res. Commun. 196 (1993) 1323-9.
GENES       CAL: CaO19.6322(ard1)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.250
            ExPASy - ENZYME nomenclature database: 1.1.1.250
            ExplorEnz - The Enzyme Database: 1.1.1.250
            ERGO genome analysis and discovery system: 1.1.1.250
            BRENDA, the Enzyme Database: 1.1.1.250
            CAS: 336883-93-3
///
ENTRY       EC 1.1.1.251                Enzyme
NAME        galactitol-1-phosphate 5-dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     galactitol-1-phosphate:NAD+ oxidoreductase
REACTION    galactitol-1-phosphate + NAD+ = L-tagatose 6-phosphate + NADH + H+
            [RN:R05147]
ALL_REAC    R05147;
            (other) R05571
SUBSTRATE   galactitol-1-phosphate;
            NAD+ [CPD:C00003]
PRODUCT     L-tagatose 6-phosphate [CPD:C06312];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COFACTOR    Zinc [CPD:C00038]
COMMENT     Contains zinc.
REFERENCE   1  [PMID:7772602]
  AUTHORS   Nobelmann B, Lengeler JW.
  TITLE     Sequence of the gat operon for galactitol utilization from a
            wild-type strain EC3132 of Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 1262 (1995) 69-72.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00052  Galactose metabolism
ORTHOLOGY   KO: K00094  galactitol-1-phosphate 5-dehydrogenase
GENES       ECO: b2091(gatD)
            ECJ: JW2075(gatD)
            ECE: Z3254(gatD)
            ECS: ECs2894
            ECC: c2616(gatD)
            ECI: UTI89_C2364(gatD)
            ECP: ECP_2129
            ECV: APECO1_4454(gatD)
            ECW: EcE24377A_2379(gatD)
            ECX: EcHS_A2227(gatD)
            STY: STY3444(gatD)
            STT: t3181(gatD)
            SPT: SPA3130(gatD)
            SEC: SC3202(gadD)
            STM: STM3261
            SFL: SF2151(gatD)
            SFX: S2277(gatD)
            SSN: SSON_2138(gatD)
            SBO: SBO_0912(gatD)
            SDY: SDY_2263(gatD)
            HSO: HS_1141(gatD)
            BCL: ABC3569
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.251
            ExPASy - ENZYME nomenclature database: 1.1.1.251
            ExplorEnz - The Enzyme Database: 1.1.1.251
            ERGO genome analysis and discovery system: 1.1.1.251
            BRENDA, the Enzyme Database: 1.1.1.251
            CAS: 167618-25-9
///
ENTRY       EC 1.1.1.252                Enzyme
NAME        tetrahydroxynaphthalene reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     scytalone:NADP+ Delta5-oxidoreductase
REACTION    scytalone + NADP+ = 1,3,6,8-tetrahydroxynaphthalene + NADPH + H+
            [RN:R02906]
ALL_REAC    R02906;
            (other) R03322
SUBSTRATE   scytalone [CPD:C00779];
            NADP+ [CPD:C00006]
PRODUCT     1,3,6,8-tetrahydroxynaphthalene [CPD:C04033];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Reduces 1,3,6,8-tetrahydroxynaphthalene to scytalone and also
            reduces 1,3,8-trihydroxynaphthalene to vermelone. Involved with EC
            4.2.1.94 scytalone dehydratase in the biosynthesis of melanin in
            pathogenic fungi.
REFERENCE   1
  AUTHORS   Wheeler, M.H. and Greenblatt, G.A.
  TITLE     The inhibition of melanin biosynthetic reactions in Pyricularia
            oryzae by compounds that prevent rice blast disease.
  JOURNAL   Exp. Mycol. 12 (1988) 151-160.
  ORGANISM  Pyricularia oryzae
REFERENCE   2  [PMID:8112349]
  AUTHORS   Vidal-Cros A, Viviani F, Labesse G, Boccara M, Gaudry M.
  TITLE     Polyhydroxynaphthalene reductase involved in melanin biosynthesis in
            Magnaporthe grisea. Purification, cDNA cloning and sequencing.
  JOURNAL   Eur. J. Biochem. 219 (1994) 985-92.
  ORGANISM  Magnaporthe grisea [GN:dmgr]
REFERENCE   3  [PMID:9048570]
  AUTHORS   Thompson JE, Basarab GS, Andersson A, Lindqvist Y, Jordan DB.
  TITLE     Trihydroxynaphthalene reductase from Magnaporthe grisea: realization
            of an active center inhibitor and elucidation of the kinetic
            mechanism.
  JOURNAL   Biochemistry. 36 (1997) 1852-60.
  ORGANISM  Magnaporthe grisea [GN:dmgr]
GENES       BUR: Bcep18194_A5816
STRUCTURES  PDB: 1DOH  1G0N  1G0O  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.252
            ExPASy - ENZYME nomenclature database: 1.1.1.252
            ExplorEnz - The Enzyme Database: 1.1.1.252
            ERGO genome analysis and discovery system: 1.1.1.252
            BRENDA, the Enzyme Database: 1.1.1.252
            CAS: 153702-05-7
///
ENTRY       EC 1.1.1.253      Obsolete  Enzyme
NAME        Transferred to 1.5.1.33
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Transferred entry: now EC 1.5.1.33 pteridine reductase. (EC
            1.1.1.253 created 1999, deleted 2003)
STRUCTURES  PDB: 1E7W  1E92  1P33  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.253
            ExPASy - ENZYME nomenclature database: 1.1.1.253
            ExplorEnz - The Enzyme Database: 1.1.1.253
            ERGO genome analysis and discovery system: 1.1.1.253
            BRENDA, the Enzyme Database: 1.1.1.253
///
ENTRY       EC 1.1.1.254                Enzyme
NAME        (S)-carnitine 3-dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-carnitine:NAD+ oxidoreductase
REACTION    (S)-carnitine + NAD+ = 3-dehydrocarnitine + NADH + H+ [RN:R01921]
ALL_REAC    R01921
SUBSTRATE   (S)-carnitine [CPD:C15025];
            NAD+ [CPD:C00003]
PRODUCT     3-dehydrocarnitine [CPD:C02636];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Specific for the (S)-enantiomer of carnitine, i.e., the enantiomer
            of the substrate of EC 1.1.1.108 carnitine 3-dehydrogenase
REFERENCE   1  [PMID:9214773]
  AUTHORS   Setyahadi S, Ueyama T, Arimoto T, Mori N, Kitamoto Y.
  TITLE     Purification and properties of a new enzyme, D-carnitine
            dehydrogenase, from Agrobacterium sp. 525a.
  JOURNAL   Biosci. Biotechnol. Biochem. 61 (1997) 1055-8.
  ORGANISM  Agrobacterium sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.254
            ExPASy - ENZYME nomenclature database: 1.1.1.254
            ExplorEnz - The Enzyme Database: 1.1.1.254
            ERGO genome analysis and discovery system: 1.1.1.254
            BRENDA, the Enzyme Database: 1.1.1.254
            CAS: 169277-49-0
///
ENTRY       EC 1.1.1.255                Enzyme
NAME        mannitol dehydrogenase;
            MTD;
            NAD+-dependent mannitol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     mannitol:NAD+ 1-oxidoreductase
REACTION    D-mannitol + NAD+ = D-mannose + NADH + H+ [RN:R07135]
ALL_REAC    R07135
SUBSTRATE   D-mannitol [CPD:C00392];
            NAD+ [CPD:C00003]
PRODUCT     D-mannose [CPD:C00159];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The enzyme from Apium graveolens (celery) oxidizes alditols with a
            minimum requirement of 2R chirality at the carbon adjacent to the
            primary carbon undergoing the oxidation. The enzyme is specific for
            NAD+ and does not use NADP+.
REFERENCE   1  [PMID:1416989]
  AUTHORS   Stoop JM, Pharr DM.
  TITLE     Partial purification and characterization of mannitol: mannose
            1-oxidoreductase from celeriac (Apium graveolens var. rapaceum)
            roots.
  JOURNAL   Arch. Biochem. Biophys. 298 (1992) 612-9.
  ORGANISM  celery
REFERENCE   2  [PMID:7630943]
  AUTHORS   Stoop JM, Williamson JD, Conkling MA, Pharr DM.
  TITLE     Purification of NAD-dependent mannitol dehydrogenase from celery
            suspension cultures.
  JOURNAL   Plant. Physiol. 108 (1995) 1219-25.
  ORGANISM  celery
REFERENCE   3  [PMID:7638158]
  AUTHORS   Williamson JD, Stoop JM, Massel MO, Conkling MA, Pharr DM.
  TITLE     Sequence analysis of a mannitol dehydrogenase cDNA from plants
            reveals a function for the pathogenesis-related protein ELI3.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 7148-52.
  ORGANISM  celery
REFERENCE   4
  AUTHORS   Stoop, J.M.H., Chilton, W.S. and Pharr, D.M.
  TITLE     Substrate specificity of the NAD-dependent mannitol dehydrogenase
            from celery.
  JOURNAL   Phytochemistry 43 (1996) 1145-1150.
  ORGANISM  celery
ORTHOLOGY   KO: K00095  mannitol dehydrogenase
GENES       ATH: AT2G21890 AT4G37970
            OSA: 4346989
            CNE: CNA04970
            PHA: PSHAa2208(mtd)
            BUR: Bcep18194_A6455
            HAR: HEAR1610
            ABU: Abu_0783
            RRU: Rru_A1503
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.255
            ExPASy - ENZYME nomenclature database: 1.1.1.255
            ExplorEnz - The Enzyme Database: 1.1.1.255
            ERGO genome analysis and discovery system: 1.1.1.255
            BRENDA, the Enzyme Database: 1.1.1.255
            CAS: 144941-29-7
///
ENTRY       EC 1.1.1.256                Enzyme
NAME        fluoren-9-ol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     fluoren-9-ol:NAD(P)+ oxidoreductase
REACTION    fluoren-9-ol + 2 NAD(P)+ = fluoren-9-one + 2 NAD(P)H + 2 H+
            [RN:R05349 R05350]
ALL_REAC    R05349 R05350
SUBSTRATE   fluoren-9-ol [CPD:C06711];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     fluoren-9-one [CPD:C06712];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Involved in the pathway for fluorene metabolism in Arthrobacter sp.
REFERENCE   1  [PMID:9055403]
  AUTHORS   Casellas M, Grifoll M, Bayona JM, Solanas AM.
  TITLE     New metabolites in the degradation of fluorene by Arthrobacter sp.
            strain F101.
  JOURNAL   Appl. Environ. Microbiol. 63 (1997) 819-26.
  ORGANISM  Arthrobacter sp.
REFERENCE   2  [PMID:1444405]
  AUTHORS   Grifoll M, Casellas M, Bayona JM, Solanas AM.
  TITLE     Isolation and characterization of a fluorene-degrading bacterium:
            identification of ring oxidation and ring fission products.
  JOURNAL   Appl. Environ. Microbiol. 58 (1992) 2910-7.
  ORGANISM  Arthrobacter sp.
PATHWAY     PATH: map00628  Fluorene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.256
            ExPASy - ENZYME nomenclature database: 1.1.1.256
            ExplorEnz - The Enzyme Database: 1.1.1.256
            ERGO genome analysis and discovery system: 1.1.1.256
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.256
            BRENDA, the Enzyme Database: 1.1.1.256
            CAS: 154215-16-4
///
ENTRY       EC 1.1.1.257                Enzyme
NAME        4-(hydroxymethyl)benzenesulfonate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4-(hydroxymethyl)benzenesulfonate:NAD+ oxidoreductase
REACTION    4-(hydroxymethyl)benzenesulfonate + NAD+ = 4-formylbenzenesulfonate
            + NADH + H+ [RN:R05271]
ALL_REAC    R05271
SUBSTRATE   4-(hydroxymethyl)benzenesulfonate [CPD:C06678];
            NAD+ [CPD:C00003]
PRODUCT     4-formylbenzenesulfonate [CPD:C06679];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Involved in the toluene-4-sulfonate degradation pathway in Comamonas
            testosteroni.
REFERENCE   1  [PMID:8828208]
  AUTHORS   Junker F, Saller E, Schlafli Oppenberg HR, Kroneck PM, Leisinger T,
            Cook AM.
  TITLE     Degradative pathways for p-toluenecarboxylate and p-toluenesulfonate
            and their multicomponent oxygenases in Comamonas testosteroni
            strains PSB-4 and T-2.
  JOURNAL   Microbiology. 142 ( Pt 9) (1996) 2419-27.
  ORGANISM  Comamonas testosteroni
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.257
            ExPASy - ENZYME nomenclature database: 1.1.1.257
            ExplorEnz - The Enzyme Database: 1.1.1.257
            ERGO genome analysis and discovery system: 1.1.1.257
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.257
            BRENDA, the Enzyme Database: 1.1.1.257
            CAS: 167973-64-0
///
ENTRY       EC 1.1.1.258                Enzyme
NAME        6-hydroxyhexanoate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     6-hydroxyhexanoate:NAD+ oxidoreductase
REACTION    6-hydroxyhexanoate + NAD+ = 6-oxohexanoate + NADH + H+ [RN:R05283]
ALL_REAC    R05283
SUBSTRATE   6-hydroxyhexanoate [CPD:C06103];
            NAD+ [CPD:C00003]
PRODUCT     6-oxohexanoate [CPD:C06102];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Involved in the cyclohexanol degradation pathway in Acinetobacter
            NCIB 9871.
REFERENCE   1  [PMID:1261]
  AUTHORS   Donoghue NA, Trudgill PW.
  TITLE     The metabolism of cyclohexanol by Acinetobacter NCIB 9871.
  JOURNAL   Eur. J. Biochem. 60 (1975) 1-7.
  ORGANISM  Acinetobacter sp.
REFERENCE   2  [PMID:6722936]
  AUTHORS   Hecker LI, Tondeur Y, Farrelly JG.
  TITLE     Formation of epsilon-hydroxycaproate and epsilon-aminocaproate from
            N-nitrosohexamethyleneimine: evidence that microsomal
            alpha-hydroxylation of cyclic nitrosamines may not always involve
            the insertion of molecular oxygen into the substrate.
  JOURNAL   Chem. Biol. Interact. 49 (1984) 235-48.
PATHWAY     PATH: map00930  Caprolactam degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.258
            ExPASy - ENZYME nomenclature database: 1.1.1.258
            ExplorEnz - The Enzyme Database: 1.1.1.258
            ERGO genome analysis and discovery system: 1.1.1.258
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.258
            BRENDA, the Enzyme Database: 1.1.1.258
            CAS: 77000-03-4
///
ENTRY       EC 1.1.1.259                Enzyme
NAME        3-hydroxypimeloyl-CoA dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-hydroxypimeloyl-CoA:NAD+ oxidoreductase
REACTION    3-hydroxypimeloyl-CoA + NAD+ = 3-oxopimeloyl-CoA + NADH + H+
            [RN:R05305]
ALL_REAC    R05305
SUBSTRATE   3-hydroxypimeloyl-CoA [CPD:C06714];
            NAD+ [CPD:C00003]
PRODUCT     3-oxopimeloyl-CoA [CPD:C06715];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Involved in the anaerobic pathway of benzoate degradation in
            bacteria.
REFERENCE   1  [PMID:8990279]
  AUTHORS   Harwood CS, Gibson J.
  TITLE     Shedding light on anaerobic benzene ring degradation: a process
            unique to prokaryotes?
  JOURNAL   J. Bacteriol. 179 (1997) 301-9.
  ORGANISM  Rhodopseudomonas palustris, Thauera aromatica, Azoarcus evansii
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.259
            ExPASy - ENZYME nomenclature database: 1.1.1.259
            ExplorEnz - The Enzyme Database: 1.1.1.259
            ERGO genome analysis and discovery system: 1.1.1.259
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.259
            BRENDA, the Enzyme Database: 1.1.1.259
///
ENTRY       EC 1.1.1.260                Enzyme
NAME        sulcatone reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     sulcatol:NAD+ oxidoreductase
REACTION    sulcatol + NAD+ = sulcatone + NADH + H+ [RN:R05678]
ALL_REAC    R05678
SUBSTRATE   sulcatol [CPD:C07288];
            NAD+ [CPD:C00003]
PRODUCT     sulcatone [CPD:C07287];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Studies on the effects of growth-stage and nutrient supply on the
            stereochemistry of sulcatone reduction in Clostridia pasteurianum,
            C. tyrobutyricum and Lactobacillus brevis suggest that there may be
            at least two sulcatone reductases with different
            stereospecificities.
REFERENCE   1
  AUTHORS   Belan, A., Botle, J., Fauve, A., Gourcy, J.G. and Veschambre, H.
  TITLE     Use of biological systems for the preparation of chiral molecules.
            3. An application in pheromone synthesis: Preparation of sulcatol
            enantiomers.
  JOURNAL   J. Org. Chem. 52 (1987) 256-260.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2
  AUTHORS   Tidswell, E.C., Salter, G.J., Kell, D.B. and Morris, J.G.
  TITLE     Enantioselectivity of sulcatone reduction by some anaerobic
            bacteria.
  JOURNAL   Enzyme Microb. Technol. 21 (1997) 143-147.
  ORGANISM  Clostridium pasteurianum, Clostridium tyrobutyricum, Lactobacillus
            brevis [GN:lbr]
REFERENCE   3
  AUTHORS   Tidswell, E.C., Thompson, A.N. and Morris, J.G.
  TITLE     Selection in chemostat culture of a mutant strain of Clostridium
            tryobutyricum improved in its reduction of ketones.
  JOURNAL   J. Appl. Microbiol. Biotechnol. 35 (1991) 317-322.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.260
            ExPASy - ENZYME nomenclature database: 1.1.1.260
            ExplorEnz - The Enzyme Database: 1.1.1.260
            ERGO genome analysis and discovery system: 1.1.1.260
            BRENDA, the Enzyme Database: 1.1.1.260
            CAS: 196522-54-0
///
ENTRY       EC 1.1.1.261                Enzyme
NAME        glycerol-1-phosphate dehydrogenase [NAD(P)+];
            glycerol-1-phosphate dehydrogenase [NAD(P)+]
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     sn-glycerol-1-phosphate:NAD(P)+ 2-oxidoreductase
REACTION    sn-glycerol-1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H +
            H+ [RN:R05679 R05680]
ALL_REAC    R05679 R05680
SUBSTRATE   sn-glycerol-1-phosphate;
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     glycerone phosphate [CPD:C00111];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     This enzyme is responsible for the formation of Archaea-specific
            glycerophosphate and is stereospecifically different from EC
            1.1.1.94, sn-glycerol-3-phosphate dehydrogenase.
REFERENCE   1  [PMID:9419225]
  AUTHORS   Koga Y, Kyuragi T, Nishihara M, Sone N.
  TITLE     Did archaeal and bacterial cells arise independently from
            noncellular precursors? A hypothesis stating that the advent of
            membrane phospholipid with enantiomeric glycerophosphate backbones
            caused the separation of the two lines of descent.
  JOURNAL   J. Mol. Evol. 46 (1998) 54-63.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
ORTHOLOGY   KO: K00096  glycerol-1-phosphate dehydrogenase [NAD(P)]
GENES       DVU: DVUA0098
            DVL: Dvul_3015
            RET: RHE_PA00022(ypa00004)
            RDE: RD1_3615
            CBE: Cbei_2364 Cbei_2501
            CHY: CHY_2583
            SCO: SCO6754(SC6A5.03)
            SMA: SAV1659(gldA)
            TFU: Tfu_2533
            STP: Strop_4488
            TPT: Tpet_0627
            MJA: MJ0712
            MMP: MMP0225(gldA)
            MMQ: MmarC5_1469
            MAC: MA3686(gldA)
            MBA: Mbar_A0291
            MMA: MM_0590
            MBU: Mbur_1032
            MTH: MTH610
            MKA: MK1230(gldA)
            AFU: AF1674(gldA)
            HAL: VNG0406C
            HMA: rrnAC0175(gldA)
            HWA: HQ1560A(gldA)
            NPH: NP4492A(gldA)
            TAC: Ta1158
            TVO: TVN1227
            PTO: PTO0850
            PHO: PH1475
            PAB: PAB1907
            PFU: PF1382
            TKO: TK0789
            RCI: RCIX1388(gldA)
            APE: APE_0519.1
            SSO: SSO0760(gldA)
            STO: ST0344
            SAI: Saci_0640
            PAI: PAE1685(gldA)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.261
            ExPASy - ENZYME nomenclature database: 1.1.1.261
            ExplorEnz - The Enzyme Database: 1.1.1.261
            ERGO genome analysis and discovery system: 1.1.1.261
            BRENDA, the Enzyme Database: 1.1.1.261
            CAS: 204594-18-3
///
ENTRY       EC 1.1.1.262                Enzyme
NAME        4-hydroxythreonine-4-phosphate dehydrogenase;
            NAD+-dependent threonine 4-phosphate dehydrogenase;
            L-threonine 4-phosphate dehydrogenase;
            4-(phosphohydroxy)-L-threonine dehydrogenase;
            PdxA;
            4-(phosphonooxy)-L-threonine:NAD+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4-phosphonooxy-L-threonine:NAD+ oxidoreductase
REACTION    4-phosphonooxy-L-threonine + NAD+ =
            (2S)-2-amino-3-oxo-4-phosphonooxybutanoate + NADH + H+ [RN:R05681]
ALL_REAC    R05681
SUBSTRATE   4-phosphonooxy-L-threonine;
            NAD+ [CPD:C00003]
PRODUCT     (2S)-2-amino-3-oxo-4-phosphonooxybutanoate [CPD:C07335];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The product of the reaction undergoes decarboxylation to give
            3-amino-2-oxopropyl phosphate. In Escherichia coli, the coenzyme
            pyridoxal 5'-phosphate is synthesized de novo by a pathway that
            involves EC 1.2.1.72 (erythrose-4-phosphate dehydrogenase), EC
            1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52
            (phosphoserine transaminase), EC 1.1.1.262
            (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2
            (pyridoxine 5'-phosphate synthase) and EC 1.4.3.5 (with pyridoxine
            5'-phosphate as substrate).
REFERENCE   1
  AUTHORS   Cane, D.E., Hsiung, Y., Cornish, J.A., Robinson, J.K and Spenser,
            I.D.
  TITLE     Biosynthesis of vitamine B6: The oxidation of L-threonine
            4-phosphate by PdxA.
  JOURNAL   J. Am. Chem. Soc. 120 (1998) 1936-1937.
REFERENCE   2  [PMID:10225425]
  AUTHORS   Laber B, Maurer W, Scharf S, Stepusin K, Schmidt FS.
  TITLE     Vitamin B6 biosynthesis: formation of pyridoxine 5'-phosphate from
            4-(phosphohydroxy)-L-threonine and 1-deoxy-D-xylulose-5-phosphate by
            PdxA and PdxJ protein.
  JOURNAL   FEBS. Lett. 449 (1999) 45-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:12896974]
  AUTHORS   Sivaraman J, Li Y, Banks J, Cane DE, Matte A, Cygler M.
  TITLE     Crystal structure of Escherichia coli PdxA, an enzyme involved in
            the pyridoxal phosphate biosynthesis pathway.
  JOURNAL   J. Biol. Chem. 278 (2003) 43682-90.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00750  Vitamin B6 metabolism
ORTHOLOGY   KO: K00097  4-hydroxythreonine-4-phosphate dehydrogenase
GENES       ECO: b0052(pdxA)
            ECJ: JW0051(pdxA)
            ECE: Z0061(pdxA)
            ECS: ECs0057
            ECC: c0065(pdxA) c0764
            ECI: UTI89_C0059(pdxA) UTI89_C0682
            ECP: ECP_0054 ECP_0698
            ECV: APECO1_1386(pdxA) APECO1_1930(pdxA)
            ECW: EcE24377A_0056(pdxA)
            ECX: EcHS_A0058
            STY: STY0106(pdxA) STY0185(pdxA)
            STT: t0094(pdxA) t0168
            SPT: SPA0092(pdxA) SPA0166
            SEC: SC0086(pdxA) SC0163(pdxA)
            STM: STM0091(pdxA) STM0163
            YPE: YPO0493(pdxA)
            YPK: y3682(pdxA)
            YPM: YP_3686(pdxA)
            YPA: YPA_4087
            YPN: YPN_0367
            YPP: YPDSF_3141
            YPS: YPTB0634(pdxA)
            YPI: YpsIP31758_3443(pdxA)
            SFL: SF0049(pdxA)
            SFX: S0051(pdxA)
            SFV: SFV_0046(pdxA)
            SSN: SSON_0060(pdxA)
            SBO: SBO_0041(pdxA)
            SDY: SDY_0077(pdxA)
            ECA: ECA3760 ECA3858(pdxA)
            PLU: plu0610(pdxA)
            WBR: WGLp019(pdxA)
            SGL: SG0425
            ENT: Ent638_0601
            SPE: Spro_0725
            BFL: Bfl127(pdxA)
            BPN: BPEN_131(pdxA)
            HSO: HS_0925(pdxA)
            PMU: PM1650
            MSU: MS0066(pdxA) MS0381(pdxA)
            ASU: Asuc_1587 Asuc_1599 Asuc_1953
            XFA: XF0839
            XFT: PD1834(pdxA)
            XCC: XCC0792(pdxA)
            XCB: XC_3439
            XCV: XCV0901(pdxA)
            XAC: XAC0864(pdxA)
            XOO: XOO3747(pdxA)
            XOM: XOO_3537(XOO3537)
            VCH: VC0444(pdxA)
            VVU: VV1_0662
            VVY: VV0479
            VPA: VP0337(pdxA)
            VFI: VF0287
            PPR: PBPRA0403
            PAE: PA0593(pdxA) PA2212
            PAU: PA14_07740(pdxA) PA14_36100
            PAP: PSPA7_0737(pdxA2) PSPA7_3077(pdxA1)
            PPU: PP_0402(pdxA)
            PPF: Pput_0436
            PST: PSPTO_0552(pdxA)
            PSB: Psyr_4626(pdxA)
            PSP: PSPPH_0634(pdxA1) PSPPH_3435(pdxA2)
            PFL: PFL_5648(pdxA)
            PFO: Pfl_5134(pdxA)
            PEN: PSEEN0429(pdxA)
            PMY: Pmen_4012
            PAR: Psyc_0960(pdxA)
            PCR: Pcryo_1458
            PRW: PsycPRwf_0906
            ACI: ACIAD3010(pdxA)
            SON: SO_3638(pdxA)
            SDN: Sden_2887
            SFR: Sfri_3078
            SAZ: Sama_2818
            SBL: Sbal_0978
            SBM: Shew185_1047
            SLO: Shew_0880
            SPC: Sputcn32_0990
            SSE: Ssed_0965
            SPL: Spea_0863
            SHE: Shewmr4_0906
            SHM: Shewmr7_3114
            SHN: Shewana3_3208
            SHW: Sputw3181_3177
            ILO: IL2231(pdxA)
            CPS: CPS_4525(pdxA)
            PHA: PSHAa2634(pdxA)
            PAT: Patl_3420
            SDE: Sde_0738
            PIN: Ping_1048
            MAQ: Maqu_3508
            CBU: CBU_1981(pdxA)
            CBD: COXBU7E912_2078(pdxA)
            LPN: lpg0299(pdxA)
            LPF: lpl0352(pdxA)
            LPP: lpp0377(pdxA)
            MCA: MCA0603(pdxA)
            TCX: Tcr_1656
            NOC: Noc_1722
            AEH: Mlg_0201
            HHA: Hhal_1022
            HCH: HCH_06104(pdxA)
            CSA: Csal_0919 Csal_3194
            ABO: ABO_2047(pdxA)
            MMW: Mmwyl1_1052
            AHA: AHA_0943(pdxA)
            BCI: BCI_0564(pdxA)
            RMA: Rmag_0546
            VOK: COSY_0501(pdxA)
            NME: NMB0195(pdxA)
            NMA: NMA0072(pdxA)
            NGO: NGO1786(pdxA)
            CVI: CV_4231(pdxA)
            RSO: RSc0517(pdxA)
            REU: Reut_A0499(pdxA)
            REH: H16_A0513(pdxA1) H16_B0216(pdxA2) H16_B0319(pdxA3)
            RME: Rmet_0438 Rmet_2590
            BMA: BMA0210(pdxA)
            BMV: BMASAVP1_A2735(pdxA)
            BML: BMA10299_A2343(pdxA)
            BMN: BMA10247_2423(pdxA)
            BXE: Bxe_A4022 Bxe_B2750
            BVI: Bcep1808_2810
            BUR: Bcep18194_A6036(pdxA) Bcep18194_B3055
            BCN: Bcen_1534 Bcen_2097 Bcen_5054
            BCH: Bcen2424_2709 Bcen2424_5806 Bcen2424_6295
            BAM: Bamb_2761 Bamb_5072
            BPS: BPSL0660(pdxA)
            BPM: BURPS1710b_0873(pdxA)
            BPL: BURPS1106A_0708(pdxA)
            BPD: BURPS668_0694(pdxA)
            BTE: BTH_I0577(pdxA)
            PNU: Pnuc_1868
            BPE: BP1813(pdxA) BP2789
            BPA: BPP2474
            BBR: BB1921 BB3214(pdxA)
            RFR: Rfer_2962 Rfer_3565
            POL: Bpro_0819 Bpro_2835
            PNA: Pnap_0711
            AAV: Aave_3698
            AJS: Ajs_0787
            VEI: Veis_2710 Veis_3936
            MPT: Mpe_A0846
            HAR: HEAR0368(pdxA)
            MMS: mma_0419
            NEU: NE0883(pdxA)
            NET: Neut_1218
            NMU: Nmul_A0519
            EBA: ebA1139(pdxA)
            AZO: azo2885(pdxA)
            DAR: Daro_3657(pdxA)
            TBD: Tbd_2339
            MFA: Mfla_2151
            HPY: HP1583(pdxA)
            HPJ: jhp1490(pdxA)
            HPA: HPAG1_1531
            HHE: HH0861(pdxA)
            HAC: Hac_0032(pdxA)
            WSU: WS0106(pdxA)
            TDN: Tmden_0895
            CJE: Cj1239(pdxA)
            CJR: CJE1374(pdxA)
            CJJ: CJJ81176_1253(pdxA)
            CJU: C8J_1182(pdxA)
            CJD: JJD26997_0486(pdxA)
            CFF: CFF8240_0681(pdxA)
            CHA: CHAB381_1715(pdxA)
            ABU: Abu_0649(pdxA)
            NIS: NIS_1087(pdxA)
            SUN: SUN_1688(pdxA)
            GSU: GSU0115(pdxA)
            GME: Gmet_3404
            GUR: Gura_4268
            PCA: Pcar_0088(pdxA)
            PPD: Ppro_3229
            DVU: DVU2241(pdxA)
            DVL: Dvul_1001
            DDE: Dde_0127 Dde_2283
            BBA: Bd0015(pdxA)
            DPS: DP2808(pdxA)
            ADE: Adeh_4336
            AFW: Anae109_4482
            MXA: MXAN_0467(pdxA)
            SFU: Sfum_1601
            PUB: SAR11_0711(pdxA)
            MLO: mll7861(pdxA)
            MES: Meso_1761
            PLA: Plav_1763 Plav_3342
            SME: SMb20146(pdxA2) SMb20772(pdxA2) SMc00580(pdxA1)
            SMD: Smed_0761 Smed_3983 Smed_4223
            ATU: Atu1104(pdxA) Atu5073(pdxA)
            ATC: AGR_C_2043(pdxA) AGR_pAT_104(pdxA)
            RET: RHE_CH01450(pdxAch) RHE_PB00028(pdxAb)
            RLE: RL1565(pdxA) pRL90097(pdxA) pRL90106
            BME: BMEI1266(pdxA)
            BMF: BAB1_0705(pdxA)
            BMS: BR0683(pdxA)
            BMB: BruAb1_0702(pdxA)
            BOV: BOV_0675(pdxA)
            OAN: Oant_2605 Oant_3097
            BJA: bll4103(pdxA) blr3887(pdxA) blr4374(pdxA)
            BRA: BRADO3323(pdxA)
            BBT: BBta_3827(pdxA)
            RPA: RPA3065(pdxA)
            RPB: RPB_2476
            RPC: RPC_2309 RPC_4426
            RPD: RPD_2970
            RPE: RPE_3296
            NWI: Nwi_1681
            NHA: Nham_2344
            BHE: BH05410(pdxA)
            BQU: BQ04590(pdxA)
            BBK: BARBAKC583_0504(pdxA)
            XAU: Xaut_2834
            CCR: CC_1686(pdxA)
            SIL: SPO2457(pdxA-1) SPOA0246(pdxA-2)
            SIT: TM1040_0945
            RSP: RSP_2904(pdxA1) RSP_3406(pdxA)
            RSH: Rsph17029_1548 Rsph17029_3051
            RSQ: Rsph17025_1117
            JAN: Jann_1810
            RDE: RD1_3123(pdxA)
            PDE: Pden_0898
            MMR: Mmar10_1222
            HNE: HNE_2151(pdxA)
            ZMO: ZMO1313
            NAR: Saro_0887
            SAL: Sala_1477
            SWI: Swit_0409
            ELI: ELI_08895
            GOX: GOX2240(pdxA)
            GBE: GbCGDNIH1_2065
            ACR: Acry_1142 Acry_2630
            RRU: Rru_A0432
            MAG: amb3717
            MGM: Mmc1_2326
            SUS: Acid_0390
            BHA: BH0804(pdxA)
            BLI: BL03434
            BLD: BLi03699
            BCL: ABC0306(pdxA) ABC0660(pdxA)
            BPU: BPUM_2972
            OIH: OB1013
            STH: STH2235 STH2236 STH2300
            CNO: NT01CX_0635(pdxA)
            CTH: Cthe_0928
            CBA: CLB_2147(pdxA)
            CBF: CLI_2255(pdxA)
            AMT: Amet_0228
            CHY: CHY_1259(pdxA)
            DSY: DSY3455
            MTA: Moth_0727
            RHA: RHA1_ro08178(tpaC) RHA1_ro10197(tpaC)
            ART: Arth_1035
            PAC: PPA0296
            KRA: Krad_4366
            SEN: SACE_3460(pdxA) SACE_4548(pdxA3) SACE_4549
            RXY: Rxyl_2988
            FNU: FN0226(pdxA)
            RBA: RB7885(pdxA)
            LIL: LA0800(pdxA)
            LIC: LIC12820(pdxA)
            LBJ: LBJ_0753(pdxA)
            LBL: LBL_2325(pdxA)
            SYN: sll0660(pdxA)
            SYW: SYNW0035(pdxA)
            SYC: syc0734_c(pdxA)
            SYF: Synpcc7942_0804
            SYD: Syncc9605_0035
            SYE: Syncc9902_0031
            SYG: sync_0034(pdxA)
            SYR: SynRCC307_0033(pdxA)
            SYX: SynWH7803_0034(pdxA)
            CYA: CYA_2324(pdxA)
            CYB: CYB_1766(pdxA)
            TEL: tll2045(pdxA)
            GVI: glr0970
            ANA: alr4755(pdxA)
            AVA: Ava_1918
            PMA: Pro0028(pdxA)
            PMM: PMM0028(pdxA)
            PMT: PMT0033(pdxA)
            PMN: PMN2A_1355
            PMI: PMT9312_0028
            PMB: A9601_00271(pdxA)
            PMC: P9515_00271(pdxA)
            PMF: P9303_00321(pdxA)
            PMG: P9301_00271(pdxA)
            PMH: P9215_00271
            PME: NATL1_00271(pdxA)
            TER: Tery_3161
            BTH: BT_4374
            BFR: BF1080
            BFS: BF0997
            PGI: PG2067(pdxA)
            SRU: SRU_1006(pdxA)
            CHU: CHU_1627(pdxA)
            GFO: GFO_3339(pdxA)
            FJO: Fjoh_0649
            FPS: FP2382(pdxA)
            CTE: CT0591(pdxA)
            CCH: Cag_1208(pdxA)
            CPH: Cpha266_1780
            PVI: Cvib_1197
            PLT: Plut_0579(pdxA)
            AAE: aq_852(pdxA)
STRUCTURES  PDB: 1PS6  1PS7  1PTM  1R8K  1YXO  2HI1  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.262
            ExPASy - ENZYME nomenclature database: 1.1.1.262
            ExplorEnz - The Enzyme Database: 1.1.1.262
            ERGO genome analysis and discovery system: 1.1.1.262
            BRENDA, the Enzyme Database: 1.1.1.262
///
ENTRY       EC 1.1.1.263                Enzyme
NAME        1,5-anhydro-D-fructose reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     1,5-anhydro-D-glucitol:NADP+ oxidoreductase
REACTION    1,5-anhydro-D-glucitol + NADP+ = 1,5-anhydro-D-fructose + NADPH + H+
            [RN:R05682]
ALL_REAC    R05682
SUBSTRATE   1,5-anhydro-D-glucitol [CPD:C07326];
            NADP+ [CPD:C00006]
PRODUCT     1,5-anhydro-D-fructose [CPD:C06485];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also reduces pyridine-3-aldehyde and 2,3-butanedione. Acetaldehyde,
            2-dehydroglucose (glucosone) and glucuronate are poor substrates,
            but there is no detectable action on glucose, mannose and fructose.
REFERENCE   1
  AUTHORS   Sakuma, M., Kametani, S. and Akanuma, H.
  TITLE     Purification and some properties of a hepatic NADPH-dependent
            reductase that specifically acts on 1,5-anhydro-D-fructose.
  JOURNAL   J. Biochem. (Tokyo) 123 (1998) 189-193.
STRUCTURES  PDB: 2GLX  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.263
            ExPASy - ENZYME nomenclature database: 1.1.1.263
            ExplorEnz - The Enzyme Database: 1.1.1.263
            ERGO genome analysis and discovery system: 1.1.1.263
            BRENDA, the Enzyme Database: 1.1.1.263
///
ENTRY       EC 1.1.1.264                Enzyme
NAME        L-idonate 5-dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-idonate:NAD(P)+ oxidoreductase
REACTION    L-idonate + NAD(P)+ = 5-dehydrogluconate + NAD(P)H + H+ [RN:R05683
            R05684]
ALL_REAC    R05683 R05684
SUBSTRATE   L-idonate [CPD:C00770];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     5-dehydrogluconate [CPD:C01062];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The enzyme from Escherichia coli cannot oxidize D-gluconate to form
            5-dehydrogluconate, a reaction that is catalysed by EC 1.1.1.69,
            gluconate 5-dehydrogenase.
REFERENCE   1  [PMID:9658018]
  AUTHORS   Bausch C, Peekhaus N, Utz C, Blais T, Murray E, Lowary T, Conway T.
  TITLE     Sequence analysis of the GntII (subsidiary) system for gluconate
            metabolism reveals a novel pathway for L-idonic acid catabolism in
            Escherichia coli.
  JOURNAL   J. Bacteriol. 180 (1998) 3704-10.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K00098  L-idonate 5-dehydrogenase
GENES       ECO: b4267(idnD)
            ECJ: JW4224(idnD)
            ECC: c5368(idnD)
            ECI: UTI89_C4874(idnD)
            ECV: APECO1_2127(idnD)
            ECX: EcHS_A4523
            SPT: SPA4284(idnD)
            SEC: SC4340(idnD)
            STM: STM4484(idnD)
            SSN: SSON_4452(idnD)
            MSU: MS0956(tdh)
            RSO: RSp0948(idnD)
            BCH: Bcen2424_0642
            POL: Bpro_3523
            SME: SMa0512(idnD)
            ATU: Atu1408(gutB) Atu4087
            ATC: AGR_C_2601 AGR_L_1538
            RET: RHE_PC00142(idnD) RHE_PF00071
            RLE: pRL100389(idnD) pRL120403
            BJA: blr5278(idnD)
            BRA: BRADO1804(idnD)
            BBT: BBta_2124(idnD)
            SIL: SPO2424(idnD)
            RDE: RD1_1048(idnD) RD1_1108(idnD)
            MSM: MSMEG_2914
            SCO: SCO1682(SCI30A.03)
            SMA: SAV6626(idnD)
            SEN: SACE_4395(idnD) SACE_4939(idnD)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.264
            ExPASy - ENZYME nomenclature database: 1.1.1.264
            ExplorEnz - The Enzyme Database: 1.1.1.264
            ERGO genome analysis and discovery system: 1.1.1.264
            BRENDA, the Enzyme Database: 1.1.1.264
///
ENTRY       EC 1.1.1.265                Enzyme
NAME        3-methylbutanal reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-methylbutanol:NAD(P)+ oxidoreductase
REACTION    3-methylbutanol + NAD(P)+ = 3-methylbutanal + NAD(P)H + H+
            [RN:R05685 R05686]
ALL_REAC    R05685 R05686
SUBSTRATE   3-methylbutanol [CPD:C07328];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     3-methylbutanal [CPD:C07329];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The enzyme purified from Saccharomyces cerevisiae catalyses the
            reduction of a number of straight-chain and branched aldehydes, as
            well as some aromatic aldehydes.
REFERENCE   1  [PMID:9327572]
  AUTHORS   van Iersel MF, Eppink MH, van Berkel WJ, Rombouts FM, Abee T.
  TITLE     Purification and characterization of a novel NADP-dependent
            branched-chain alcohol dehydrogenase from Saccharomyces cerevisiae.
  JOURNAL   Appl. Environ. Microbiol. 63 (1997) 4079-82.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:16502707]
  AUTHORS   Bertaglia E, Shah D.
  TITLE     Typical atrial flutter ablation and the risk of postablation atrial
            fibrillation.
  JOURNAL   Ital. Heart. J. 6 (2005) 946-9.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.265
            ExPASy - ENZYME nomenclature database: 1.1.1.265
            ExplorEnz - The Enzyme Database: 1.1.1.265
            ERGO genome analysis and discovery system: 1.1.1.265
            BRENDA, the Enzyme Database: 1.1.1.265
///
ENTRY       EC 1.1.1.266                Enzyme
NAME        dTDP-4-dehydro-6-deoxyglucose reductase;
            dTDP-4-keto-6-deoxyglucose reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     dTDP-D-fucose:NADP+ oxidoreductase
REACTION    dTDP-D-fucose + NADP+ = dTDP-4-dehydro-6-deoxy-D-glucose + NADPH +
            H+ [RN:R05687]
ALL_REAC    R05687
SUBSTRATE   dTDP-D-fucose [CPD:C07277];
            NADP+ [CPD:C00006]
PRODUCT     dTDP-4-dehydro-6-deoxy-D-glucose [CPD:C11907];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The enzyme from the Gram-negative bacterium Actinobacillus
            actinomycetemcomitans forms activated fucose for incorporation into
            capsular polysaccharide.
REFERENCE   1  [PMID:10358040]
  AUTHORS   Yoshida Y, Nakano Y, Nezu T, Yamashita Y, Koga T.
  TITLE     A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the
            synthesis of thymidine diphosphate-D-fucose.
  JOURNAL   J. Biol. Chem. 274 (1999) 16933-9.
  ORGANISM  Actinobacillus actinomycetemcomitans
PATHWAY     PATH: map00523  Polyketide sugar unit biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.266
            ExPASy - ENZYME nomenclature database: 1.1.1.266
            ExplorEnz - The Enzyme Database: 1.1.1.266
            ERGO genome analysis and discovery system: 1.1.1.266
            BRENDA, the Enzyme Database: 1.1.1.266
///
ENTRY       EC 1.1.1.267                Enzyme
NAME        1-deoxy-D-xylulose-5-phosphate reductoisomerase;
            DXP-reductoisomerase;
            1-deoxy-D-xylulose-5-phosphate isomeroreductase;
            2-C-methyl-D-erythritol 4-phosphate (MEP) synthase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-C-methyl-D-erythritol-4-phosphate:NADP+ oxidoreductase
            (isomerizing)
REACTION    2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose
            5-phosphate + NADPH + H+ [RN:R05688]
ALL_REAC    R05688
SUBSTRATE   2-C-methyl-D-erythritol 4-phosphate [CPD:C11434];
            NADP+ [CPD:C00006]
PRODUCT     1-deoxy-D-xylulose 5-phosphate [CPD:C11437];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:9707569]
  AUTHORS   Takahashi S, Kuzuyama T, Watanabe H, Seto H.
  TITLE     A 1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzing the
            formation of 2-C-methyl-D-erythritol 4-phosphate in an alternative
            nonmevalonate pathway for terpenoid biosynthesis.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 9879-84.
  ORGANISM  Esherichia coli
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K00099  1-deoxy-D-xylulose-5-phosphate reductoisomerase
GENES       ATH: AT5G62790(DXR)
            OSA: 4326153
            CME: CMG148C
            PFA: PF14_0641
            TAN: TA14290
            TPV: TP02_0073
            ECO: b0173(ispC)
            ECJ: JW0168(dxr)
            ECE: Z0184(yaeM)
            ECS: ECs0175
            ECI: UTI89_C0188(dxr)
            ECP: ECP_0181
            ECV: APECO1_1814(dxr)
            ECW: EcE24377A_0177(dxr)
            STY: STY0243(dxr)
            STT: t0221(dxr)
            SPT: SPA0227(dxr)
            SEC: SC0220(dxr)
            STM: STM0220(dxr)
            YPE: YPO1048(dxr)
            YPK: y3131
            YPM: YP_2802(dxr)
            YPA: YPA_0524
            YPN: YPN_2952
            YPP: YPDSF_1664
            YPS: YPTB2999(dxr)
            YPI: YpsIP31758_1017(dxr)
            SFL: SF0163(dxr)
            SFX: S0166(yaeM)
            SFV: SFV_0156(yaeM)
            SSN: SSON_0185(yaeM)
            SBO: SBO_0161(yaeM)
            SDY: SDY_0189(yaeM)
            ECA: ECA1035(dxr)
            PLU: plu0676(dxr)
            BUC: BU235(dxr)
            BAS: BUsg229(dxr)
            WBR: WGLp388(yaeM)
            SGL: SG1939
            ENT: Ent638_0711
            SPE: Spro_3786
            BFL: Bfl275(dxr)
            BPN: BPEN_283(dxr)
            HIN: HI0807(dxr)
            HIT: NTHI0971(dxr)
            HIP: CGSHiEE_08040
            HIQ: CGSHiGG_07530
            HDU: HD1186(dxr)
            HSO: HS_0985(dxr)
            PMU: PM1988(dxr)
            MSU: MS1928(dxr)
            APL: APL_0406(dxr)
            ASU: Asuc_0657
            XFA: XF1048
            XFT: PD0328(dxr)
            XCC: XCC1367(dxr)
            XCB: XC_2871
            XCV: XCV1472(dxr)
            XAC: XAC1415(dxr)
            XOO: XOO1970(dxr)
            XOM: XOO_1860(XOO1860)
            VCH: VC2254
            VVU: VV1_1866
            VVY: VV2551
            VPA: VP2312
            VFI: VF1956
            PPR: PBPRA2962
            PAE: PA3650(dxr)
            PAU: PA14_17130(dxr)
            PAP: PSPA7_1489(dxr)
            PPU: PP_1597(dxr)
            PPF: Pput_4180
            PST: PSPTO_1540(dxr)
            PSB: Psyr_1349
            PSP: PSPPH_3834(dxr)
            PFL: PFL_1182(dxr)
            PFO: Pfl_1107
            PEN: PSEEN4214(dxr)
            PMY: Pmen_3047
            PAR: Psyc_1531(dxr)
            PCR: Pcryo_1710
            PRW: PsycPRwf_1798
            ACI: ACIAD1376(dxr)
            SON: SO_1635(dxr)
            SDN: Sden_1560
            SFR: Sfri_1276
            SAZ: Sama_1145
            SBL: Sbal_1456
            SBM: Shew185_1451
            SLO: Shew_2629
            SPC: Sputcn32_1354
            SSE: Ssed_3155
            SPL: Spea_2879
            SHE: Shewmr4_2635
            SHM: Shewmr7_2702
            SHN: Shewana3_2809
            SHW: Sputw3181_2749
            ILO: IL0839
            CPS: CPS_1559(dxr)
            PHA: PSHAa2030(dxr)
            PAT: Patl_1255
            SDE: Sde_2591
            PIN: Ping_2970
            MAQ: Maqu_2542
            MCA: MCA0573(dxr)
            FTU: FTT1574c(dxr)
            FTF: FTF1574c(dxr)
            FTW: FTW_0352(dxr)
            FTL: FTL_0534
            FTH: FTH_0536(dxr)
            FTA: FTA_0567(dxr)
            FTN: FTN_1483(dxr)
            NOC: Noc_0814
            AEH: Mlg_1857
            HHA: Hhal_1460
            HCH: HCH_05246(dxr)
            CSA: Csal_0569
            ABO: ABO_1149(dxr)
            MMW: Mmwyl1_1278
            AHA: AHA_1179(dxr)
            BCI: BCI_0531(dxr)
            RMA: Rmag_0025
            VOK: COSY_0025(dxr)
            NME: NMB0184
            NMA: NMA0083(dxr)
            NGO: NGO1799
            CVI: CV_2202(dxr)
            RSO: RSc1410(dxr)
            REU: Reut_A1875
            REH: H16_A2049(dxp)
            RME: Rmet_1441
            BMA: BMA1549(dxr)
            BMV: BMASAVP1_A2050(dxr)
            BML: BMA10299_A3261(dxr)
            BMN: BMA10247_1322(dxr)
            BXE: Bxe_A1688
            BVI: Bcep1808_1919
            BUR: Bcep18194_A5323
            BCN: Bcen_6064
            BCH: Bcen2424_2013
            BAM: Bamb_2046
            BPS: BPSL2153(dxr)
            BPM: BURPS1710b_2577(dxr)
            BPL: BURPS1106A_2487(dxr)
            BPD: BURPS668_2431(dxr)
            BTE: BTH_I2033(dxr)
            PNU: Pnuc_1445
            BPE: BP1425(dxr)
            BBR: BB2611(dxr)
            RFR: Rfer_1994
            POL: Bpro_2689
            PNA: Pnap_1764
            AAV: Aave_1829
            AJS: Ajs_2579
            VEI: Veis_1444
            MPT: Mpe_A1973
            HAR: HEAR1341(dxr)
            MMS: mma_2052
            NEU: NE1712(dxr)
            NET: Neut_2029
            NMU: Nmul_A0663
            EBA: ebA5994(dxr)
            AZO: azo1903(dxr)
            DAR: Daro_1748
            TBD: Tbd_0791
            MFA: Mfla_1524
            HPY: HP0216(dxr)
            HPJ: jhp0202
            HPA: HPAG1_0217
            HHE: HH0524(dxr)
            HAC: Hac_1502(dxr_fragment_2) Hac_1503(dxr_fragment_1)
            WSU: WS0812
            TDN: Tmden_0126
            CJE: Cj1346c(dxr)
            CJR: CJE1535(dxr)
            CJU: C8J_1262(dxr)
            CFF: CFF8240_0210(dxr)
            CCV: CCV52592_0594(dxr)
            CHA: CHAB381_0121(dxr)
            CCO: CCC13826_0420(dxr)
            ABU: Abu_0161(dxr)
            NIS: NIS_1666(ispC)
            SUN: SUN_0144
            GSU: GSU1915(dxr)
            GME: Gmet_1256
            GUR: Gura_3727
            PCA: Pcar_1915
            PPD: Ppro_2050
            DVU: DVU0866(dxr)
            DVL: Dvul_2116
            DDE: Dde_1123
            LIP: LI0386(dxr)
            DPS: DP1160
            ADE: Adeh_3583
            AFW: Anae109_3704
            SAT: SYN_00916
            SFU: Sfum_1784
            WOL: WD0992(dxr)
            WBM: Wbm0179
            AMA: AM743(dxr)
            APH: APH_0440(dxr)
            ERU: Erum4750(dxr)
            ERW: ERWE_CDS_04970(dxr)
            ERG: ERGA_CDS_04870(dxr)
            ECN: Ecaj_0473
            ECH: ECH_0557(dxr)
            NSE: NSE_0443(dxr)
            PUB: SAR11_0912(yaeM)
            PLA: Plav_3190
            SME: SMc03105(dxr)
            SMD: Smed_2879
            ATU: Atu2612(dxr)
            ATC: AGR_C_4736
            RET: RHE_CH03839(dxr)
            RLE: RL4372(dxr)
            BJA: bll4855(dxr)
            BRA: BRADO4134(dxr)
            BBT: BBta_4511(dxr)
            RPA: RPA2916(dxr)
            RPB: RPB_2822
            RPC: RPC_2442
            RPD: RPD_2851
            RPE: RPE_2559
            NWI: Nwi_1853
            NHA: Nham_1700
            XAU: Xaut_4433
            CCR: CC_1917
            SIL: SPO1667(dxr)
            SIT: TM1040_1410
            RSP: RSP_2709(dxr)
            RSH: Rsph17029_1366
            RSQ: Rsph17025_2149
            JAN: Jann_2455
            RDE: RD1_2590(dxr)
            PDE: Pden_3997
            MMR: Mmar10_1386
            HNE: HNE_1774(dxr)
            ZMO: ZMO1150(dxr)
            NAR: Saro_1375
            SAL: Sala_1954
            SWI: Swit_0466
            ELI: ELI_03805
            GOX: GOX1816
            GBE: GbCGDNIH1_0938
            ACR: Acry_2557
            RRU: Rru_A1592
            MAG: amb2492
            MGM: Mmc1_1846
            ABA: Acid345_1419
            SUS: Acid_7136
            BSU: BG13409(dxr)
            BHA: BH2421
            BAN: BA3409(dxr-1) BA3959(dxr-2)
            BAR: GBAA3409(dxr-1) GBAA3959(dxr-2)
            BAA: BA_4429
            BAT: BAS3160 BAS3672
            BCE: BC3341 BC3819
            BCA: BCE_3862(dxr)
            BCZ: BCZK3054(dxr) BCZK3580(dxr)
            BCY: Bcer98_2128 Bcer98_2473
            BTK: BT9727_3144(dxr) BT9727_3562(dxr)
            BLI: BL01237(dxr)
            BLD: BLi01876(dxr)
            BCL: ABC2236(dxr)
            BPU: BPUM_1554
            GKA: GK1255
            LMO: lmo1317
            LMF: LMOf2365_1334(dxr)
            LIN: lin1354
            LWE: lwe1332(dxr)
            STH: STH1499(dxr)
            CAC: CAC1795
            CPE: CPE1694
            CPF: CPF_1948(dxr)
            CPR: CPR_1666(dxr)
            CTC: CTC01268
            CNO: NT01CX_2143
            CTH: Cthe_0999
            CDF: CD2130(dxr)
            CBA: CLB_2290(dxr)
            CBH: CLC_2273(dxr)
            CBF: CLI_2482(dxr)
            CBE: Cbei_1195
            CKL: CKL_1423(dxr)
            AMT: Amet_2682
            CHY: CHY_1778(dxr)
            DSY: DSY2539
            DRM: Dred_1970
            SWO: Swol_0889
            CSC: Csac_2353
            TTE: TTE1402(dxr)
            MTA: Moth_1041
            MPE: MYPE1470
            MGA: MGA_0787(dxr)
            MTU: Rv2870c(dxr)
            MTC: MT2938(dxr)
            MBO: Mb2895c(dxr)
            MLE: ML1583
            MPA: MAP2940c
            MAV: MAV_3727(dxr)
            MSM: MSMEG_2578(dxr)
            MVA: Mvan_2260
            MGI: Mflv_4083
            MMC: Mmcs_2042
            MKM: Mkms_2088
            MJL: Mjls_2025
            CGL: NCgl1940(cgl2016)
            CGB: cg2208(dxr)
            CEF: CE1905
            CDI: DIP1500(dxr)
            CJK: jk1167(ispC)
            NFA: nfa41200(dxr)
            RHA: RHA1_ro06588(dxr)
            SCO: SCO5694(dxr)
            SMA: SAV2563(dxr)
            TWH: TWT089(dxr)
            TWS: TW099(dxr)
            LXX: Lxx12180(dxr)
            CMI: CMM_2160(dxrA)
            ART: Arth_1399
            AAU: AAur_1543(dxr)
            PAC: PPA1510
            NCA: Noca_3204
            TFU: Tfu_0747
            FRA: Francci3_3575
            FAL: FRAAL5774(dxr)
            ACE: Acel_1524
            KRA: Krad_1427 Krad_4655
            SEN: SACE_5994(dxr)
            STP: Strop_1350
            BLO: BL0097(ispC)
            BAD: BAD_1158(ispC)
            RXY: Rxyl_1404
            FNU: FN1324
            RBA: RB5568(dxr)
            CTR: CT071(yaeM)
            CTA: CTA_0076(dxr)
            CMU: TC0343
            CPN: CPn0345(yaeM)
            CPA: CP0415
            CPJ: CPj0344(yaeM)
            CPT: CpB0352
            CCA: CCA00441(dxr)
            CAB: CAB427(dxr)
            CFE: CF0566(yaeM)
            PCU: pc0260(dxr)
            TPA: TP0601
            TDE: TDE2342(dxr)
            LIL: LA3292(dxr)
            LIC: LIC10856(dxr)
            LBJ: LBJ_0910(dxr)
            LBL: LBL_0925(dxr)
            SYN: sll0019(dxr)
            SYW: SYNW0698(dxr)
            SYC: syc2498_d(dxr)
            SYF: Synpcc7942_1513
            SYD: Syncc9605_1970
            SYE: Syncc9902_0689
            SYG: sync_0920(dxr)
            SYR: SynRCC307_1674(dxr)
            SYX: SynWH7803_1622(dxr)
            CYA: CYA_0193(dxr)
            CYB: CYB_1233(dxr)
            TEL: tlr1040
            GVI: gll2252
            ANA: alr4351
            AVA: Ava_1300
            PMA: Pro1236(dxr)
            PMM: PMM1142(dxr)
            PMT: PMT1161(dxr)
            PMN: PMN2A_0751
            PMI: PMT9312_1238
            PMB: A9601_13171(dxr)
            PMC: P9515_13061(dxr)
            PMF: P9303_08651(dxr)
            PMG: P9301_13311(dxr)
            PMH: P9215_13461
            PME: NATL1_15911(dxr)
            TER: Tery_0416
            BTH: BT_2002
            BFR: BF3699
            BFS: BF3492
            PGI: PG1364(dxr)
            SRU: SRU_1849(dxr)
            CHU: CHU_2996(dxr)
            CTE: CT0125(dxr)
            CCH: Cag_0008
            CPH: Cpha266_2680
            PVI: Cvib_0138
            PLT: Plut_0077
            DET: DET0371(dxr)
            DEH: cbdb_A314(dxr)
            DEB: DehaBAV1_0353
            DRA: DR_1508
            DGE: Dgeo_1044
            TTH: TTC0504
            TTJ: TTHA0856
            AAE: aq_404
            TMA: TM0889
            TPT: Tpet_0038
            TME: Tmel_0037
            FNO: Fnod_0950
STRUCTURES  PDB: 1JVS  1ONN  1ONO  1ONP  1Q0H  1Q0L  1Q0Q  1R0K  1R0L  1T1R  
                 1T1S  2C82  2EGH  2JCV  2JCX  2JCY  2JCZ  2JD0  2JD1  2JD2  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.267
            ExPASy - ENZYME nomenclature database: 1.1.1.267
            ExplorEnz - The Enzyme Database: 1.1.1.267
            ERGO genome analysis and discovery system: 1.1.1.267
            BRENDA, the Enzyme Database: 1.1.1.267
///
ENTRY       EC 1.1.1.268                Enzyme
NAME        2-(R)-hydroxypropyl-CoM dehydrogenase;
            2-(2-(R)-hydroxypropylthio)ethanesulfonate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-[2-(R)-hydroxypropylthio]ethanesulfonate:NAD+ oxidoreductase
REACTION    2-(R)-hydroxypropyl-CoM + NAD+ = 2-oxopropyl-CoM + NADH + H+
            [RN:R05689]
ALL_REAC    R05689
SUBSTRATE   2-(R)-hydroxypropyl-CoM [CPD:C11496];
            NAD+ [CPD:C00003]
PRODUCT     2-oxopropyl-CoM [CPD:C11497];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The enzyme is highly specific for (R)-2-hydroxyalkyl thioethers of
            CoM, in contrast to EC 1.1.1.269, 2-(S)-hydroxypropyl-CoM
            dehydrogenase, which is highly specific for the (S)-enantiomer. This
            enzyme forms component III of a four-component enzyme system
            {comprising EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC
            1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II],
            EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III]
            and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component
            IV]} that is involved in epoxyalkane carboxylation in Xanthobacter
            sp. strain Py2.
REFERENCE   1  [PMID:10411892]
  AUTHORS   Allen JR, Clark DD, Krum JG, Ensign SA.
  TITLE     A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial
            pathway of aliphatic epoxide carboxylation.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 8432-7.
  ORGANISM  Xanthobacter sp.
STRUCTURES  PDB: 2CFC  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.268
            ExPASy - ENZYME nomenclature database: 1.1.1.268
            ExplorEnz - The Enzyme Database: 1.1.1.268
            ERGO genome analysis and discovery system: 1.1.1.268
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.268
            BRENDA, the Enzyme Database: 1.1.1.268
///
ENTRY       EC 1.1.1.269                Enzyme
NAME        2-(S)-hydroxypropyl-CoM dehydrogenase;
            2-(2-(S)-hydroxypropylthio)ethanesulfonate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-[2-(S)-hydroxypropylthio]ethanesulfonate:NAD+ oxidoreductase
REACTION    2-(S)-hydroxypropyl-CoM + NAD+ = 2-oxopropyl-CoM + NADH + H+
            [RN:R05690]
ALL_REAC    R05690
SUBSTRATE   2-(S)-hydroxypropyl-CoM [CPD:C11498];
            NAD+ [CPD:C00003]
PRODUCT     2-oxopropyl-CoM [CPD:C11497];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The enzyme is highly specific for (S)-2-hydroxyalkyl thioethers of
            CoM, in contrast to EC 1.1.1.268, 2-(R)-hydroxypropyl-CoM
            dehydrogenase, which is highly specific for the (R)-enantiomer. This
            enzyme forms component IV of a four-component enzyme system
            {comprising EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC
            1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II],
            EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III]
            and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component
            IV]} that is involved in epoxyalkane carboxylation in Xanthobacter
            sp. strain Py2.
REFERENCE   1  [PMID:10411892]
  AUTHORS   Allen JR, Clark DD, Krum JG, Ensign SA.
  TITLE     A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial
            pathway of aliphatic epoxide carboxylation.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 8432-7.
  ORGANISM  Xanthobacter sp.
GENES       BPM: BURPS1710b_3485
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.269
            ExPASy - ENZYME nomenclature database: 1.1.1.269
            ExplorEnz - The Enzyme Database: 1.1.1.269
            ERGO genome analysis and discovery system: 1.1.1.269
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.269
            BRENDA, the Enzyme Database: 1.1.1.269
///
ENTRY       EC 1.1.1.270                Enzyme
NAME        3-keto-steroid reductase;
            3-KSR
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3beta-hydroxy-steroid:NADP+ 3-oxidoreductase
REACTION    4alpha-methyl-5alpha-cholest-7-en-3beta-ol + NADP+ =
            4alpha-methyl-5alpha-cholest-7-en-3-one + NADPH + H+ [RN:R05691]
ALL_REAC    R05691;
            (other) R04328 R07495
SUBSTRATE   4alpha-methyl-5alpha-cholest-7-en-3beta-ol [CPD:C08825];
            NADP+ [CPD:C00006]
PRODUCT     4alpha-methyl-5alpha-cholest-7-en-3-one [CPD:C04453];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on 5alpha-cholest-7-en-3-one.
REFERENCE   1  [PMID:6946726]
  AUTHORS   Billheimer JT, Alcorn M, Gaylor JL.
  TITLE     Solubilization and partial purification of a microsomal
            3-ketosteroid reductase of cholesterol biosynthesis.
  JOURNAL   Arch. Biochem. Biophys. 211 (1981) 430-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4387005]
  AUTHORS   Swindell AC, Gaylor JL.
  TITLE     Investigation of the component reactions of oxidative sterol
            demethylation. Formation and metabolism of 3-ketosteroid
            intermediates.
  JOURNAL   J. Biol. Chem. 243 (1968) 5546-55.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K09827  3-keto steroid reductase
GENES       HSA: 51478(HSD17B7)
            PTR: 466046(LOC466046)
            MMU: 15490(Hsd17b7)
            RNO: 29540(Hsd17b7)
            CFA: 609364(HSD17B7)
            GGA: 424367(HSD17B7)
            XTR: 548963(hsd17b7)
            SPU: 588363(LOC588363)
            SCE: YLR100W(ERG27)
            AGO: AGOS_AGR068W
            PIC: PICST_61325(ERG27)
            CAL: CaO19_10750(CaO19.10750) CaO19_3240(CaO19.3240)
            CGR: CAGL0M11506g
            SPO: SPBC1709.07
            ANI: AN5585.2
            AFM: AFUA_4G11500
            AOR: AO090003001070
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.270
            ExPASy - ENZYME nomenclature database: 1.1.1.270
            ExplorEnz - The Enzyme Database: 1.1.1.270
            ERGO genome analysis and discovery system: 1.1.1.270
            BRENDA, the Enzyme Database: 1.1.1.270
            CAS: 42616-29-5
///
ENTRY       EC 1.1.1.271                Enzyme
NAME        GDP-L-fucose synthase;
            GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     GDP-L-fucose:NADP+ 4-oxidoreductase (3,5-epimerizing)
REACTION    GDP-L-fucose + NADP+ = GDP-4-dehydro-6-deoxy-D-mannose + NADPH + H+
            [RN:R05692]
ALL_REAC    R05692;
            (other) R07059 R07060
SUBSTRATE   GDP-L-fucose [CPD:C00325];
            NADP+ [CPD:C00006]
PRODUCT     GDP-4-dehydro-6-deoxy-D-mannose [CPD:C01222];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Both human and Escherichia coli enzymes can use NADH in place of
            NADPH to a slight extent.
REFERENCE   1  [PMID:3338988]
  AUTHORS   Chang S, Duerr B, Serif G.
  TITLE     An epimerase-reductase in L-fucose synthesis.
  JOURNAL   J. Biol. Chem. 263 (1988) 1693-7.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:11030750]
  AUTHORS   Mattila P, Rabina J, Hortling S, Helin J, Renkonen R.
  TITLE     Functional expression of Escherichia coli enzymes synthesizing
            GDP-L-fucose from inherent GDP-D-mannose in Saccharomyces
            cerevisiae.
  JOURNAL   Glycobiology. 10 (2000) 1041-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:10480878]
  AUTHORS   Menon S, Stahl M, Kumar R, Xu GY, Sullivan F.
  TITLE     Stereochemical course and steady state mechanism of the reaction
            catalyzed by the GDP-fucose synthetase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 274 (1999) 26743-50.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:9862812]
  AUTHORS   Somers WS, Stahl ML, Sullivan FX.
  TITLE     GDP-fucose synthetase from Escherichia coli: structure of a unique
            member of the short-chain dehydrogenase/reductase family that
            catalyzes two distinct reactions at the same active site.
  JOURNAL   Structure. 6 (1998) 1601-12.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K02377  GDP-L-fucose synthase
GENES       HSA: 7264(TSTA3)
            PTR: 464445(TSTA3)
            MMU: 22122(Tsta3)
            CFA: 475116(TSTA3)
            GGA: 420292(TSTA3)
            SPU: 585407(LOC585407)
            DME: Dmel_CG3495(Gmer)
            CEL: R01H2.5(ger-1)
            ATH: AT1G17890(GER2) AT1G73250(ATFX/GER1)
            OSA: 4341699
            DDI: DDBDRAFT_0190865
            PFA: PF10_0137
            TBR: Tb11.01.5560
            TCR: 511727.300
            ECO: b2052(wcaG)
            ECJ: JW2037(fcl)
            ECE: Z3197(fcI) Z3216(wcaG)
            ECS: ECs2838 ECs2857
            ECC: c2578(wcaG)
            ECI: UTI89_C2326(wcaG)
            ECP: ECP_2092
            ECV: APECO1_1142(wcaG)
            ECW: EcE24377A_2345(fcl)
            STY: STY2320(fcl)
            STT: t0765(fcl)
            SPT: SPA0758(fcl)
            SEC: SC2109(wcaG)
            STM: STM2108(wcaG)
            YPK: y1080(wcaG)
            YPM: YP_0826(wcaG2)
            YPA: YPA_2595
            YPI: YpsIP31758_3040(fcl)
            SFL: SF2115(wcaG)
            SFX: S2238(wcaG)
            SFV: SFV_2109(wcaG)
            SSN: SSON_2105(wcaG)
            SBO: SBO_0879(wcaG)
            SGL: SG0330
            VVY: VV0350
            CPS: CPS_4200
            CBU: CBU_0688(wcaG)
            CBD: COXBU7E912_0702(wcaG)
            MCA: MCA1147(fcl)
            NOC: Noc_1234
            RME: Rmet_5859
            BXE: Bxe_A3862 Bxe_C1084
            BAM: Bamb_0747
            RFR: Rfer_1235
            POL: Bpro_4000
            MPT: Mpe_A2730
            AZO: azo3586(fcl1) azo3599(fcl2)
            TBD: Tbd_1775
            HPY: HP0045(nolK)
            HPJ: jhp0039
            HPA: HPAG1_0042
            HHE: HH0173
            HAC: Hac_0057(wbcJ)
            CJE: Cj1428c(fcl)
            CJR: CJE1612(fcl)
            GSU: GSU0627
            GME: Gmet_1312
            DVU: DVU0090(wcaG)
            DDE: Dde_0425 Dde_2900
            LIP: LIC080
            DPS: DP0023
            SAT: SYN_00585
            PUB: SAR11_0571(wcaG)
            MLO: mlr8749
            ATU: Atu4790(fcl)
            ATC: AGR_L_185
            RET: RHE_CH00763(nolK) RHE_CH03468(sqdB)
            RLE: RL0826(fcl) RL3975(sqdB) pRL90132(fcl)
            BME: BMEII0849 BMEII0850
            BMF: BAB2_0803
            BMS: BRA0418
            BJA: bll1630(nolK) bll5464(fcl)
            BRA: BRADO2184(fcl) BRADO5259(fcl)
            BBT: BBta_5711(fcl)
            RPB: RPB_1526 RPB_1528
            NWI: Nwi_2384
            SIT: TM1040_1481
            RSP: RSP_2569(sqdB) RSP_4108(wcaG)
            ELI: ELI_13460
            RRU: Rru_A0254
            MAG: amb0161
            MGM: Mmc1_3315
            ABA: Acid345_3813
            CAC: CAC2179
            SWO: Swol_0619
            MTU: Rv1512
            MTC: MT1562(wcaG)
            MPA: MAP1232(epiA)
            RHA: RHA1_ro05445
            AAU: AAur_4112
            ACE: Acel_0450
            RBA: RB2521
            LIL: LA1577
            LIC: LIC12205(fcl)
            LBJ: LBJ_1111
            LBL: LBL_1165
            SYN: sll1213
            SYW: SYNW0423
            SYC: syc2390_d(wcaG)
            SYF: Synpcc7942_1700
            SYG: sync_0145(wcaG-2)
            SYR: SynRCC307_0218(wcaG)
            SYX: SynWH7803_0113(wcaG)
            CYA: CYA_1879
            CYB: CYB_1556
            TEL: tll0633
            GVI: glr3792
            ANA: all4826
            AVA: Ava_2096
            PMA: Pro0064(wcaG)
            PMM: PMM1207
            PMI: PMT9312_1315
            PMB: A9601_14001
            PMC: P9515_13691 P9515_14001
            PMG: P9301_14451
            PMH: P9215_14311(wcaG)
            TER: Tery_0491
            BTH: BT_1225
            BFR: BF1822
            BFS: BF1887(fcl)
            PGI: PG1289(fcl)
            CHU: CHU_0060(wcaG)
            GFO: GFO_0556(wcaG)
            CCH: Cag_0651
            PLT: Plut_1864
            DGE: Dgeo_2648
            MBA: Mbar_A0035
            MMA: MM_0658
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.271
            ExPASy - ENZYME nomenclature database: 1.1.1.271
            ExplorEnz - The Enzyme Database: 1.1.1.271
            ERGO genome analysis and discovery system: 1.1.1.271
            BRENDA, the Enzyme Database: 1.1.1.271
///
ENTRY       EC 1.1.1.272                Enzyme
NAME        (R)-2-hydroxyacid dehydrogenase;
            (R)-sulfolactate:NAD(P)+ oxidoreductase;
            L-sulfolactate dehydrogenase;
            ComC;
            (R)-sulfolactate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-2-hydroxyacid:NAD(P)+ oxidoreductase
REACTION    (2R)-3-sulfolactate + NAD(P)+ = 3-sulfopyruvate + NAD(P)H + H+
            [RN:R07136 R07137]
ALL_REAC    R07136 R07137;
            (other) R05693 R05694
SUBSTRATE   (2R)-3-sulfolactate [CPD:C11537];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     3-sulfopyruvate [CPD:C05528];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     This dehydrogenase also acts on (S)-malate and
            (S)-2-hydroxyglutarate i.e. with the same configuration as
            (R)-sulfolactate.
REFERENCE   1  [PMID:10850983]
  AUTHORS   Graupner M, Xu H, White RH.
  TITLE     Identification of an archaeal 2-hydroxy acid dehydrogenase
            catalyzing reactions involved in coenzyme biosynthesis in
            methanoarchaea.
  JOURNAL   J. Bacteriol. 182 (2000) 3688-92.
  ORGANISM  Methanococcus jannaschii [GN:mja], Methanothermus fervidus
REFERENCE   2  [PMID:11451450]
  AUTHORS   Graupner M, White RH.
  TITLE     The first examples of (S)-2-hydroxyacid dehydrogenases catalyzing
            the transfer of the pro-4S hydrogen of NADH are found in the
            archaea.
  JOURNAL   Biochim. Biophys. Acta. 1548 (2001) 169-73.
  ORGANISM  Methanococcus jannaschii [GN:mja], Methanothermus fervidus
REFERENCE   3  [PMID:12013276]
  AUTHORS   Graham DE, White RH.
  TITLE     Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy
            to genomics.
  JOURNAL   Nat. Prod. Rep. 19 (2002) 133-47.
  ORGANISM  Methanococcus jannaschii [GN:mja]
ORTHOLOGY   KO: K05884  (R)-2-hydroxyacid dehydrogenase
GENES       REU: Reut_B3531
            BCN: Bcen_3719
            BCH: Bcen2424_4649
            HAR: HEAR3341
            PUB: SAR11_0804(comC)
            RPC: RPC_0106
            PDE: Pden_0241
            MJA: MJ1425(mdh)
            MMP: MMP1133(comC)
            MMQ: MmarC5_0451
            MAE: Maeo_1015
STRUCTURES  PDB: 1RFM  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.272
            ExPASy - ENZYME nomenclature database: 1.1.1.272
            ExplorEnz - The Enzyme Database: 1.1.1.272
            ERGO genome analysis and discovery system: 1.1.1.272
            BRENDA, the Enzyme Database: 1.1.1.272
///
ENTRY       EC 1.1.1.273                Enzyme
NAME        vellosimine dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     10-deoxysarpagine:NADP+ oxidoreductase
REACTION    10-deoxysarpagine + NADP+ = vellosimine + NADPH + H+ [RN:R05827]
ALL_REAC    R05827
SUBSTRATE   10-deoxysarpagine [CPD:C11635];
            NADP+ [CPD:C00006]
PRODUCT     vellosimine [CPD:C11634];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on related alkaloids with an endo-aldehyde group as
            vellosimine (same stereochemistry at C-16) but only slight activity
            with exo-aldehydes. Detected in many cell suspension cultures of
            plants from the family Apocynaceae.
REFERENCE   1
  AUTHORS   Pfitzner, A., Krausch, B. and Stockigt, J.
  TITLE     Characteristics of vellosimine reductase, a specific enzyme involved
            in the biosynthesis of the Rauwolfia alkaloid sarpagine.
  JOURNAL   Tetrahedron 40 (1984) 1691-1699.
  ORGANISM  Rauwolfia
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.273
            ExPASy - ENZYME nomenclature database: 1.1.1.273
            ExplorEnz - The Enzyme Database: 1.1.1.273
            ERGO genome analysis and discovery system: 1.1.1.273
            BRENDA, the Enzyme Database: 1.1.1.273
            CAS: 86777-26-6
///
ENTRY       EC 1.1.1.274                Enzyme
NAME        2,5-didehydrogluconate reductase;
            2,5-diketo-D-gluconate reductase;
            YqhE reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-dehydro-D-gluconate:NADP+ 2-oxidoreductase
REACTION    2-dehydro-D-gluconate + NADP+ = 2,5-didehydro-D-gluconate + NADPH +
            H+ [RN:R05823]
ALL_REAC    R05823
SUBSTRATE   2-dehydro-D-gluconate [CPD:C00629];
            NADP+ [CPD:C00006]
PRODUCT     2,5-didehydro-D-gluconate [CPD:C02780];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     This is a key enzyme in the microbial production of ascorbate. Can
            also reduce ethyl 2-methylacetoacetate stereoselectively to ethyl
            (2R)-methyl-(3S)-hydroxybutanoate and can also accept some other
            beta-keto esters. The identification of a bacterial beta-keto ester
            reductase as a 2,5-didehydrogluconate reductase links two previously
            separate areas of biocatalysis, i.e., asymmetric carbonyl reduction
            and microbial vitamin C production.
REFERENCE   1  [PMID:10427017]
  AUTHORS   Yum DY, Lee BY, Pan JG.
  TITLE     Identification of the yqhE and yafB genes encoding two 2,
            5-diketo-D-gluconate reductases in Escherichia coli.
  JOURNAL   Appl. Environ. Microbiol. 65 (1999) 3341-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:9811658]
  AUTHORS   Yum DY, Lee BY, Hahm DH, Pan JG.
  TITLE     The yiaE gene, located at 80.1 minutes on the Escherichia coli
            chromosome, encodes a 2-ketoaldonate reductase.
  JOURNAL   J. Bacteriol. 180 (1998) 5984-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:11934293]
  AUTHORS   Habrych M, Rodriguez S, Stewart JD.
  TITLE     Purification and identification of an Escherichia coli beta-keto
            ester reductase as 2,5-diketo-D-gluconate reductase YqhE.
  JOURNAL   Biotechnol. Prog. 18 (2002) 257-61.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K05885  2,5-diketo-D-gluconate reductase
            KO: K06221  2,5-diketo-D-gluconate reductase A
            KO: K06222  2,5-diketo-D-gluconate reductase B
GENES       ECO: b0207(dkgB) b3012(dkgA)
            ECJ: JW0197(dkgB) JW5499(dkgA)
            ECE: Z0229(yafB) Z4365(yqhE)
            ECS: ECs0203 ECs3896
            ECC: c0244(yafB) c3746
            ECI: UTI89_C0226(dkgB) UTI89_C3432(dkgA)
            ECP: ECP_0213 ECP_3095
            ECV: APECO1_1783(yafB) APECO1_3413(dkgA)
            ECW: EcE24377A_0213(dkgB) EcE24377A_3480(dkgA)
            ECX: EcHS_A0211 EcHS_A3190
            STY: STY0276(yafB)
            STT: t2610(yafB)
            SPT: SPA2514(yafB) SPA3033(yqhE)
            SEC: SC0251(yafB) SC3109(yqhE)
            STM: STM0255(yafB) STM3165(yqhE)
            YPE: YPO0676 YPO1075
            YPK: y3501
            YPM: YP_2991(aRA14)
            YPA: YPA_0553 YPA_3115
            YPN: YPN_0534 YPN_1035
            YPP: YPDSF_0460 YPDSF_2695
            YPS: YPTB3388
            YPI: YpsIP31758_0586(dkgA) YpsIP31758_1048(dkgB)
            SFL: SF0192(yafB) SF3057(yqhE)
            SFX: S0200(yafB) S3260(yqhE)
            SFV: SFV_0190(yafB) SFV_3062(yqhE)
            SSN: SSON_0221(yafB) SSON_3155(yqhE)
            SBO: SBO_3006(yqhE)
            SDY: SDY_3061(yqhE)
            ECA: ECA0349(dkgA)
            PLU: plu1527(dkgB) plu3946(dkgA)
            SGL: SG0278
            ENT: Ent638_3423
            SPE: Spro_4216
            ASU: Asuc_0062
            XCC: XCC0269
            XCB: XC_0279
            XOM: XOO_4264(XOO4264)
            PFL: PFL_4075
            PEN: PSEEN3411(dkgB)
            ACI: ACIAD3281(dkg)
            SHN: Shewana3_3599
            AHA: AHA_1644
            REU: Reut_B5116
            BVI: Bcep1808_3606
            BUR: Bcep18194_A4726 Bcep18194_A5863 Bcep18194_B0240
                 Bcep18194_C7134
            BCN: Bcen_5450
            BCH: Bcen2424_5412
            BAM: Bamb_4753
            BPD: BURPS668_A0422
            BTE: BTH_II2153
            AAV: Aave_0287
            HAR: HEAR3312
            AZO: azo3631(yafB)
            GUR: Gura_4373
            ADE: Adeh_2028
            RLE: RL0474 RL4557(dkgA) pRL120107
            OAN: Oant_3013
            BRA: BRADO2128(dkgB) BRADO4561 BRADO5951
            BBT: BBta_1823 BBta_2445(dkgB) BBta_4789
            RPC: RPC_3339
            RPD: RPD_3073
            RPE: RPE_3420
            NHA: Nham_2432
            RSH: Rsph17029_0988
            RSQ: Rsph17025_1615
            RDE: RD1_0511(dkgB)
            ZMO: ZMO1344(dkg)
            GBE: GbCGDNIH1_0786
            RRU: Rru_A0288 Rru_A3551
            BCY: Bcer98_0196 Bcer98_2796
            BCL: ABC3477
            BAY: RBAM_002430(kdgR1)
            SAJ: SaurJH9_0727 SaurJH9_1839
            SAH: SaurJH1_0743 SaurJH1_1875
            SPH: MGAS10270_Spy1506
            LSA: LSA0030
            LSL: LSL_0147 LSL_0320 LSL_1681
            LDB: Ldb1901
            LBR: LVIS_1975
            LCA: LSEI_0758
            LRE: Lreu_0064 Lreu_0942 Lreu_1898
            CBO: CBO0984(dkgA)
            CBE: Cbei_3512 Cbei_3724
            MAV: MAV_3816 MAV_4483
            MSM: MSMEG_2408
            MVA: Mvan_1769 Mvan_2161
            MGI: Mflv_4205 Mflv_4697
            MMC: Mmcs_1360 Mmcs_1938
            MKM: Mkms_1378 Mkms_1984 Mkms_1985
            MJL: Mjls_1394 Mjls_1918 Mjls_1919
            RHA: RHA1_ro00567 RHA1_ro01851 RHA1_ro04589
            ART: Arth_0262 Arth_0685 Arth_2252
            AAU: AAur_0228 AAur_3779
            TFU: Tfu_1687
            FRA: Francci3_1172
            FAL: FRAAL1875(dkgA)
            KRA: Krad_1600 Krad_2708 Krad_4349
            SEN: SACE_3115(yqhE)
            AVA: Ava_0644 Ava_0681 Ava_1414 Ava_3061 Ava_3100 Ava_C0138
            CCH: Cag_1232
            RCA: Rcas_1051
            TPT: Tpet_1742
STRUCTURES  PDB: 1VP5  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.274
            ExPASy - ENZYME nomenclature database: 1.1.1.274
            ExplorEnz - The Enzyme Database: 1.1.1.274
            ERGO genome analysis and discovery system: 1.1.1.274
            BRENDA, the Enzyme Database: 1.1.1.274
            CAS: 95725-95-4
///
ENTRY       EC 1.1.1.275                Enzyme
NAME        (+)-trans-carveol dehydrogenase;
            carveol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (+)-trans-carveol:NAD+ oxidoreductase
REACTION    (+)-trans-carveol + NAD+ = (+)-(S)-carvone + NADH + H+ [RN:R06117]
ALL_REAC    R06117
SUBSTRATE   (+)-trans-carveol [CPD:C11409];
            NAD+ [CPD:C00003]
PRODUCT     (+)-(S)-carvone [CPD:C11383];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     NADP+ cannot replace NAD+. Forms part of the monoterpenoid
            biosynthesis pathway in Carum carvi (caraway) seeds.
REFERENCE   1  [PMID:9662532]
  AUTHORS   Bouwmeester HJ, Gershenzon J, Konings MC, Croteau R.
  TITLE     Biosynthesis of the monoterpenes limonene and carvone in the fruit
            of caraway. I. Demonstration Of enzyme activities and their changes
            with development
  JOURNAL   Plant. Physiol. 117 (1998) 901-12.
  ORGANISM  Carum carvi
PATHWAY     PATH: map00902  Monoterpenoid biosynthesis
            PATH: map00903  Limonene and pinene degradation
GENES       MAV: MAV_0479 MAV_0846 MAV_0896 MAV_1393 MAV_1570 MAV_1810
                 MAV_1881 MAV_1913 MAV_1921 MAV_2550 MAV_2598 MAV_2623 MAV_2636
                 MAV_2645 MAV_2946 MAV_2983 MAV_3017 MAV_3019 MAV_3098 MAV_3550
                 MAV_3551 MAV_3596 MAV_3641 MAV_3823
            RHA: RHA1_ro05789 RHA1_ro08632(limC2)
            FAL: FRAAL0316 FRAAL3298 FRAAL3338 FRAAL3551
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.275
            ExPASy - ENZYME nomenclature database: 1.1.1.275
            ExplorEnz - The Enzyme Database: 1.1.1.275
            ERGO genome analysis and discovery system: 1.1.1.275
            BRENDA, the Enzyme Database: 1.1.1.275
///
ENTRY       EC 1.1.1.276                Enzyme
NAME        serine 3-dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-serine:NADP+ 3-oxidoreductase
REACTION    L-serine + NADP+ = 2-ammoniomalonate semialdehyde + NADPH + H+
            [RN:R06126]
ALL_REAC    R06126
SUBSTRATE   L-serine [CPD:C00065];
            NADP+ [CPD:C00006]
PRODUCT     2-ammoniomalonate semialdehyde [CPD:C11822];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The product 2-ammoniomalonate semialdehyde is spontaneously
            converted into 2-aminoacetaldehyde and CO2. NAD+ cannot replace
            NADP+.
REFERENCE   1  [PMID:12092831]
  AUTHORS   Fujisawa H, Nagata S, Chowdhury EK, Matsumoto M, Misono H.
  TITLE     Cloning and sequencing of the serine dehydrogenase gene from
            Agrobacterium tumefaciens.
  JOURNAL   Biosci. Biotechnol. Biochem. 66 (2002) 1137-9.
  ORGANISM  Agrobacterium tumefaciens
REFERENCE   2  [PMID:9028042]
  AUTHORS   Chowdhury EK, Higuchi K, Nagata S, Misono H.
  TITLE     A novel NADP(+)-dependent serine dehydrogenase from Agrobacterium
            tumefaciens.
  JOURNAL   Biosci. Biotechnol. Biochem. 61 (1997) 152-7.
  ORGANISM  Agrobacterium tumefaciens
ORTHOLOGY   KO: K05886  serine 3-dehydrogenase
GENES       PSP: PSPPH_0597
            PFL: PFL_0603
            BUR: Bcep18194_A3894
            HAR: HEAR2402
            CCV: CCV52592_1706
            DDE: Dde_1841
            ATU: Atu4110(sdh)
            ATC: AGR_L_1487
            ZMO: ZMO0226(sdh)
            RRU: Rru_A2127
            MSM: MSMEG_0930
            SEN: SACE_2257
            AVA: Ava_2888
            CCH: Cag_0924
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.276
            ExPASy - ENZYME nomenclature database: 1.1.1.276
            ExplorEnz - The Enzyme Database: 1.1.1.276
            ERGO genome analysis and discovery system: 1.1.1.276
            BRENDA, the Enzyme Database: 1.1.1.276
            CAS: 9038-55-5
///
ENTRY       EC 1.1.1.277                Enzyme
NAME        3beta-hydroxy-5beta-steroid dehydrogenase;
            3beta-hydroxysteroid 5beta-oxidoreductase;
            3beta-hydroxysteroid 5beta-progesterone oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3beta-hydroxy-5beta-steroid:NADP+ 3-oxidoreductase
REACTION    3beta-hydroxy-5beta-pregnane-20-one + NADP+ =
            5beta-pregnan-3,20-dione + NADPH + H+ [RN:R06166]
ALL_REAC    R06166
SUBSTRATE   3beta-hydroxy-5beta-pregnane-20-one [CPD:C11825];
            NADP+ [CPD:C00006]
PRODUCT     5beta-pregnan-3,20-dione;
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Stuhlemmer, U. and Kreis, W.
  TITLE     Cardenolide formation and activity of pregnane-modifying enzymes in
            cell suspension cultures, shoot cultures and leaves of Digitalis
            lanata.
  JOURNAL   Plant Physiol. 34 (1996) 85-91.
REFERENCE   2
  AUTHORS   Seitz, H.U. and Gaertner, D.E.
  TITLE     Enzymes in cardenolide-accumulating shoot cultures of Digitalis
            purpurea.
  JOURNAL   Plant Cell 38 (1994) 337-344.
REFERENCE   3
  AUTHORS   Lindemann, P. and Luckner, M.
  TITLE     Biosynthesis of pregnane derivatives in somatic embryos of Digitalis
            lanata.
  JOURNAL   Phytochemistry 46 (1997) 507-513.
  ORGANISM  Digitalis lanata
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.277
            ExPASy - ENZYME nomenclature database: 1.1.1.277
            ExplorEnz - The Enzyme Database: 1.1.1.277
            ERGO genome analysis and discovery system: 1.1.1.277
            BRENDA, the Enzyme Database: 1.1.1.277
///
ENTRY       EC 1.1.1.278                Enzyme
NAME        3beta-hydroxy-5alpha-steroid dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3beta-hydroxy-5alpha-steroid:NADP+ 3-oxidoreductase
REACTION    3beta-hydroxy-5alpha-pregnane-20-one + NADP+ =
            5alpha-pregnan-3,20-dione + NADPH + H+ [RN:R07138]
ALL_REAC    R07138
SUBSTRATE   3beta-hydroxy-5alpha-pregnane-20-one [CPD:C15484];
            NADP+ [CPD:C00006]
PRODUCT     5alpha-pregnan-3,20-dione;
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Lindemann, P. and Luckner, M.
  TITLE     Biosynthesis of pregnane derivatives in somatic embryos of Digitalis
            lanata.
  JOURNAL   Phytochemistry 46 (1997) 507-513.
  ORGANISM  Digitalis lanata
REFERENCE   2  [PMID:2291772]
  AUTHORS   Warneck HM, Seitz HU.
  TITLE     3 beta-hydroxysteroid oxidoreductase in suspension cultures of
            Digitalis lanata EHRH.
  JOURNAL   Z. Naturforsch. [C]. 45 (1990) 963-72.
  ORGANISM  Digitalis lanata
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.278
            ExPASy - ENZYME nomenclature database: 1.1.1.278
            ExplorEnz - The Enzyme Database: 1.1.1.278
            ERGO genome analysis and discovery system: 1.1.1.278
            BRENDA, the Enzyme Database: 1.1.1.278
///
ENTRY       EC 1.1.1.279                Enzyme
NAME        (R)-3-hydroxyacid-ester dehydrogenase;
            3-oxo ester (R)-reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     ethyl-(R)-3-hydroxyhexanoate:NADP+ 3-oxidoreductase
REACTION    ethyl (R)-3-hydroxyhexanoate + NADP+ = ethyl 3-oxohexanoate + NADPH
            + H+ [RN:R04105]
ALL_REAC    R04105
SUBSTRATE   ethyl (R)-3-hydroxyhexanoate [CPD:C03864];
            NADP+ [CPD:C00006]
PRODUCT     ethyl 3-oxohexanoate [CPD:C02975];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on ethyl (R)-3-oxobutanoate and some other (R)-3-hydroxy
            acid esters. The (R)- symbol is allotted on the assumption that no
            substituents change the order of priority from O-3 > C-2 > C-4. A
            subunit of yeast fatty acid synthase EC 2.3.1.86 fatty-acyl-CoA
            synthase). cf. EC 1.1.1.280 (S)-3-hydroxyacid ester dehydrogenase.
REFERENCE   1  [PMID:3280313]
  AUTHORS   Heidlas J, Engel KH, Tressl R.
  TITLE     Purification and characterization of two oxidoreductases involved in
            the enantioselective reduction of 3-oxo, 4-oxo and 5-oxo esters in
            baker's yeast.
  JOURNAL   Eur. J. Biochem. 172 (1988) 633-9.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.279
            ExPASy - ENZYME nomenclature database: 1.1.1.279
            ExplorEnz - The Enzyme Database: 1.1.1.279
            ERGO genome analysis and discovery system: 1.1.1.279
            BRENDA, the Enzyme Database: 1.1.1.279
            CAS: 114705-02-1
///
ENTRY       EC 1.1.1.280                Enzyme
NAME        (S)-3-hydroxyacid-ester dehydrogenase;
            3-oxo ester (S)-reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     ethyl-(S)-3-hydroxyhexanoate:NADP+ 3-oxidoreductase
REACTION    ethyl (S)-3-hydroxyhexanoate + NADP+ = ethyl 3-oxohexanoate + NADPH
            + H+ [RN:R04106]
ALL_REAC    R04106
SUBSTRATE   ethyl (S)-3-hydroxyhexanoate [CPD:C03865];
            NADP+ [CPD:C00006]
PRODUCT     ethyl 3-oxohexanoate [CPD:C02975];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on 4-oxo- and 5-oxo-fatty acids and their esters. cf. EC
            1.1.1.279 (R)-3-hydroxyacid-ester dehydrogenase.
REFERENCE   1  [PMID:3280313]
  AUTHORS   Heidlas J, Engel KH, Tressl R.
  TITLE     Purification and characterization of two oxidoreductases involved in
            the enantioselective reduction of 3-oxo, 4-oxo and 5-oxo esters in
            baker's yeast.
  JOURNAL   Eur. J. Biochem. 172 (1988) 633-9.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.280
            ExPASy - ENZYME nomenclature database: 1.1.1.280
            ExplorEnz - The Enzyme Database: 1.1.1.280
            ERGO genome analysis and discovery system: 1.1.1.280
            BRENDA, the Enzyme Database: 1.1.1.280
            CAS: 114705-03-2
///
ENTRY       EC 1.1.1.281                Enzyme
NAME        GDP-4-dehydro-6-deoxy-D-mannose reductase;
            GDP-4-keto-6-deoxy-D-mannose reductase [ambiguous];
            GDP-6-deoxy-D-lyxo-4-hexulose reductase;
            Rmd
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     GDP-6-deoxy-D-mannose:NAD(P)+ 4-oxidoreductase (D-rhamnose-forming)
REACTION    GDP-6-deoxy-D-mannose + NAD(P)+ = GDP-4-dehydro-6-deoxy-D-mannose +
            NAD(P)H + H+ [RN:R03397 R03399]
ALL_REAC    R03397 R03399
SUBSTRATE   GDP-6-deoxy-D-mannose [CPD:C03117];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     GDP-4-dehydro-6-deoxy-D-mannose [CPD:C01222];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     This enzyme differs from EC 1.1.1.187, GDP-4-dehydro-D-rhamnose
            reductase, in that the only product formed is GDP-D-rhamnose
            (GDP-6-deoxy-D-mannose). D-Rhamnose is a constituent of
            lipopolysaccharides of Gram-negative plant and human pathogenic
            bacteria.
REFERENCE   1  [PMID:11096116]
  AUTHORS   Kneidinger B, Graninger M, Adam G, Puchberger M, Kosma P, Zayni S,
            Messner P.
  TITLE     Identification of two GDP-6-deoxy-D-lyxo-4-hexulose reductases
            synthesizing GDP-D-rhamnose in Aneurinibacillus thermoaerophilus
            L420-91T.
  JOURNAL   J. Biol. Chem. 276 (2001) 5577-83.
  ORGANISM  Aneurinibacillus thermoaerophilus
REFERENCE   2  [PMID:11856318]
  AUTHORS   Maki M, Jarvinen N, Rabina J, Roos C, Maaheimo H, Renkonen R.
  TITLE     Functional expression of Pseudomonas aeruginosa
            GDP-4-keto-6-deoxy-D-mannose reductase which synthesizes
            GDP-rhamnose.
  JOURNAL   Eur. J. Biochem. 269 (2002) 593-601.
  ORGANISM  Pseudomonas aeruginosa
PATHWAY     PATH: map00051  Fructose and mannose metabolism
GENES       MXA: MXAN_5328(rmd)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.281
            ExPASy - ENZYME nomenclature database: 1.1.1.281
            ExplorEnz - The Enzyme Database: 1.1.1.281
            ERGO genome analysis and discovery system: 1.1.1.281
            BRENDA, the Enzyme Database: 1.1.1.281
///
ENTRY       EC 1.1.1.282                Enzyme
NAME        quinate/shikimate dehydrogenase;
            YdiB
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-quinate:NAD(P)+ 3-oxidoreductase
REACTION    (1) L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+ [RN:R01872
            R06846];
            (2) shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
            [RN:R02413 R06847]
ALL_REAC    R01872 R02413 R06846 R06847
SUBSTRATE   L-quinate [CPD:C00296];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            shikimate [CPD:C00493]
PRODUCT     3-dehydroquinate [CPD:C00944];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            3-dehydroshikimate [CPD:C02637]
COMMENT     This is the second shikimate dehydrogenase enzyme found in
            Escherichia coli and differs from EC 1.1.1.25, shikimate
            dehydrogenase, in that it can use both quinate and shikimate as
            substrate and either NAD+ or NADP+ as acceptor.
REFERENCE   1  [PMID:12637497]
  AUTHORS   Michel G, Roszak AW, Sauve V, Maclean J, Matte A, Coggins JR, Cygler
            M, Lapthorn AJ.
  TITLE     Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A
            common structural framework for different activities.
  JOURNAL   J. Biol. Chem. 278 (2003) 19463-72.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:12624088]
  AUTHORS   Benach J, Lee I, Edstrom W, Kuzin AP, Chiang Y, Acton TB, Montelione
            GT, Hunt JF.
  TITLE     The 2.3-A crystal structure of the shikimate 5-dehydrogenase
            orthologue YdiB from Escherichia coli suggests a novel catalytic
            environment for an NAD-dependent dehydrogenase.
  JOURNAL   J. Biol. Chem. 278 (2003) 19176-82.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K05887  quinate/shikimate dehydrogenase
GENES       ECO: b1692(ydiB)
            ECJ: JW1682(ydiB)
            ECE: Z2720(ydiB)
            ECS: ECs2399
            ECC: c2087(ydiB)
            ECI: UTI89_C1884(ydiB)
            SEC: SC1378(ydiB)
            STM: STM1359(ydiB)
            SFL: SF1722(ydiB)
            SFX: S1854(ydiB)
            SFV: SFV_1718(ydiB)
            SSN: SSON_1462(ydiB)
            SDY: SDY_1475(ydiB)
            PMB: A9601_19151(aroE)
            PMC: P9515_18961(aroE)
            PMF: P9303_30051(aroE)
            PMG: P9301_18961(aroE)
            PMH: P9215_19781
            PME: NATL1_21871(aroE)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.282
            ExPASy - ENZYME nomenclature database: 1.1.1.282
            ExplorEnz - The Enzyme Database: 1.1.1.282
            ERGO genome analysis and discovery system: 1.1.1.282
            BRENDA, the Enzyme Database: 1.1.1.282
///
ENTRY       EC 1.1.1.283                Enzyme
NAME        methylglyoxal reductase (NADPH-dependent);
            lactaldehyde dehydrogenase (NADP+);
            Gre2
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     lactaldehyde:NADP+ oxidoreductase
REACTION    lactaldehyde + NADP+ = methylglyoxal + NADPH + H+ [RN:R07139]
ALL_REAC    R07139
SUBSTRATE   lactaldehyde [CPD:C05999];
            NADP+ [CPD:C00006]
PRODUCT     methylglyoxal [CPD:C00546];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The enzyme from the yeast Saccharomyces cerevisiae catalyses the
            conversion of methylglyoxal into lactaldehyde; the reverse reaction
            has not been demonstrated. It differs in coenzyme requirement from
            EC 1.1.1.78, methylglyoxal reductase (NADH-dependent), which is
            found in mammals. It also acts on phenylglyoxal and glyoxal.
REFERENCE   1  [PMID:3896793]
  AUTHORS   Murata K, Fukuda Y, Simosaka M, Watanabe K, Saikusa T, Kimura A.
  TITLE     Metabolism of 2-oxoaldehyde in yeasts. Purification and
            characterization of NADPH-dependent methylglyoxal-reducing enzyme
            from Saccharomyces cerevisiae.
  JOURNAL   Eur. J. Biochem. 151 (1985) 631-6.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:12722185]
  AUTHORS   Chen CN, Porubleva L, Shearer G, Svrakic M, Holden LG, Dover JL,
            Johnston M, Chitnis PR, Kohl DH.
  TITLE     Associating protein activities with their genes: rapid
            identification of a gene encoding a methylglyoxal reductase in the
            yeast Saccharomyces cerevisiae.
  JOURNAL   Yeast. 20 (2003) 545-54.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.283
            ExPASy - ENZYME nomenclature database: 1.1.1.283
            ExplorEnz - The Enzyme Database: 1.1.1.283
            ERGO genome analysis and discovery system: 1.1.1.283
            BRENDA, the Enzyme Database: 1.1.1.283
///
ENTRY       EC 1.1.1.284                Enzyme
NAME        S-(hydroxymethyl)glutathione dehydrogenase;
            NAD-linked formaldehyde dehydrogenase (incorrect);
            formaldehyde dehydrogenase (incorrect);
            formic dehydrogenase (incorrect);
            class III alcohol dehydrogenase;
            ADH3;
            &chi;
            -ADH;
            FDH (incorrect);
            formaldehyde dehydrogenase (glutathione) (incorrect);
            GS-FDH (incorrect);
            glutathione-dependent formaldehyde dehydrogenase (incorrect);
            NAD-dependent formaldehyde dehydrogenase;
            GD-FALDH;
            NAD- and glutathione-dependent formaldehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     S-(hydroxymethyl)glutathione:NAD+ oxidoreductase
REACTION    S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione +
            NAD(P)H + H+ [RN:R06983 R07140]
ALL_REAC    R06983 R07140
SUBSTRATE   S-(hydroxymethyl)glutathione [CPD:C14180];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     S-formylglutathione [CPD:C01031];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The substrate, S-(hydroxymethyl)glutathione, forms spontaneously
            from glutathione and formaldehyde; its rate of formation is
            increased in some bacteria by the presence of EC 4.4.1.22,
            S-(hydroxymethyl)glutathione synthase. This enzyme forms part of the
            pathway that detoxifies formaldehyde, since the product is
            hydrolysed by EC 3.1.2.12, S-formylglutathione hydrolase. The human
            enzyme belongs to the family of zinc-dependent alcohol
            dehydrogenases. Also specifically reduces S-nitrosylglutathione.
REFERENCE   1
  AUTHORS   Jakoby, W.B.
  TITLE     Aldehyde dehydrogenases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
REFERENCE   2
  AUTHORS   Rose, Z.B. and Racker, E.
  TITLE     Formaldehyde dehydrogenase.
  JOURNAL   Methods Enzymol. 9 (1966) 357-360.
REFERENCE   3  [PMID:11260719]
  AUTHORS   Liu L, Hausladen A, Zeng M, Que L, Heitman J, Stamler JS.
  TITLE     A metabolic enzyme for S-nitrosothiol conserved from bacteria to
            humans.
  JOURNAL   Nature. 410 (2001) 490-4.
REFERENCE   4  [PMID:10978156]
  AUTHORS   Sanghani PC, Stone CL, Ray BD, Pindel EV, Hurley TD, Bosron WF.
  TITLE     Kinetic mechanism of human glutathione-dependent formaldehyde
            dehydrogenase.
  JOURNAL   Biochemistry. 39 (2000) 10720-9.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:16525953]
  AUTHORS   Hildebrand F, van Griensven M, Giannoudis P, Schreiber T, Frink M,
            Probst C, Grotz M, Krettek C, Pape HC.
  TITLE     Impact of hypothermia on the immunologic response after trauma and
            elective surgery.
  JOURNAL   Surg. Technol. Int. 14 (2005) 41-50.
REFERENCE   6  [PMID:7798140]
  AUTHORS   Ras J, Van Ophem PW, Reijnders WN, Van Spanning RJ, Duine JA,
            Stouthamer AH, Harms N.
  TITLE     Isolation, sequencing, and mutagenesis of the gene encoding NAD- and
            glutathione-dependent formaldehyde dehydrogenase (GD-FALDH) from
            Paracoccus denitrificans, in which GD-FALDH is essential for
            methylotrophic growth.
  JOURNAL   J. Bacteriol. 177 (1995) 247-51.
  ORGANISM  Paracoccus denitrificans [GN:pde]
REFERENCE   7  [PMID:8631716]
  AUTHORS   Barber RD, Rott MA, Donohue TJ.
  TITLE     Characterization of a glutathione-dependent formaldehyde
            dehydrogenase from Rhodobacter sphaeroides.
  JOURNAL   J. Bacteriol. 178 (1996) 1386-93.
  ORGANISM  Rhodobacter sphaeroides
PATHWAY     PATH: map00680  Methane metabolism
ORTHOLOGY   KO: K00121  S-(hydroxymethyl)glutathione dehydrogenase
GENES       HSA: 128(ADH5)
            MMU: 11532(Adh5)
            CFA: 474946(LOC474946) 609781(LOC609781)
            GGA: 422705(RCJMB04_12i19)
            XLA: 432021(MGC82221)
            XTR: 497007(LOC497007)
            DRE: 116517(adh5)
            SPU: 579220(LOC579220)
            DME: Dmel_CG6598(Fdh)
            ATH: AT1G22430 AT1G22440 AT5G42250 AT5G43940(ADH2)
            OSA: 4331130
            CME: CMS125C
            SCE: YDL168W(SFA1)
            AGO: AGOS_ACL148C
            PIC: PICST_29252(FDH1)
            CGR: CAGL0L01111g
            SPO: SPBC1539.07c
            ANI: AN7632.2
            AFM: AFUA_2G00170 AFUA_2G01040
            AOR: AO090701000373
            CNE: CNM01690
            UMA: UM06244.1
            DDI: DDBDRAFT_0204255
            TET: TTHERM_00295700
            ECO: b0356(frmA)
            ECJ: JW0347(frmA)
            ECE: Z0456(adhC)
            ECS: ECs0411
            ECC: c0465(adhC)
            ECI: UTI89_C0376(adhC)
            ECP: ECP_0421
            ECV: APECO1_1645(adhC)
            ECW: EcE24377A_0630
            ECX: EcHS_A0421
            SEC: SC1622(adh3)
            STM: STM1627
            YPE: YPO1502
            YPK: y2667(adhC)
            YPM: YP_1392(adhC)
            YPA: YPA_0797
            YPN: YPN_2477
            YPS: YPTB1517
            YPI: YpsIP31758_2473
            SSN: SSON_0335(adhC)
            PLU: plu4332(adhC)
            HIN: HI0185(adhC)
            MSU: MS1386(adhC)
            APL: APL_1208(adhC)
            XCC: XCC3389 XCC3475(adhC)
            XCB: XC_0686 XC_0775
            XCV: XCV0713 XCV0788
            XAC: XAC0652(adhC) XAC0734
            XOO: XOO3867
            XOM: XOO_3647(XOO3647)
            VVU: VV1_0344
            VVY: VV0841
            VPA: VPA0071
            VFI: VF0645 VF0648
            PPR: PBPRA0784 PBPRA1480
            PAE: PA3629(adhC)
            PAP: PSPA7_1510
            PPU: PP_1616
            PST: PSPTO_1558(adhC) PSPTO_1875(fdH)
            PSB: Psyr_1367 Psyr_2956
            PSP: PSPPH_3816(adhC)
            PFL: PFL_1200
            PFO: Pfl_1125
            PEN: PSEEN2613(adhC-1) PSEEN4196(adhC-2)
            PAR: Psyc_1671(adhC)
            PCR: Pcryo_1939
            ACI: ACIAD1879(adhC)
            SON: SO_2054(adhC) SO_A0161
            SDN: Sden_3767
            SFR: Sfri_4059
            SHE: Shewmr4_1786
            SHM: Shewmr7_2191
            SHN: Shewana3_1837
            ILO: IL1773(adhC)
            CPS: CPS_0817
            PHA: PSHAa1386(adhC) PSHAa2213(adhC)
            PAT: Patl_1438
            FTU: FTT0883
            FTA: FTA_0409
            HCH: HCH_01446(adhC)
            NME: NMB1304
            NMA: NMA1518(adhC)
            CVI: CV_0740(adhC) CV_3945
            RSO: RSc0605(adhC2) RSp0069(adhC1)
            REU: Reut_B4000 Reut_B4833 Reut_B5201
            REH: H16_B1195(adhC)
            RME: Rmet_0545 Rmet_4784
            BMA: BMA0324
            BMV: BMASAVP1_A0622
            BML: BMA10299_A2456
            BMN: BMA10247_0070
            BPS: BPSL0820(flhA) BPSS2235
            BPM: BURPS1710b_A1366
            BPL: BURPS1106A_0866
            BPD: BURPS668_0862 BURPS668_A2916
            BTE: BTH_I0686
            BPE: BP3751(adhI)
            BPA: BPP4251(adhI)
            BBR: BB4838(adhI)
            RFR: Rfer_0121
            POL: Bpro_3129
            HAR: HEAR1070 HEAR2039
            MMS: mma_0221 mma_1172
            NEU: NE0907(adhC1)
            NET: Neut_1385
            EBA: ebA1699(fdh) ebA5713(fdhG)
            AZO: azo3623(adhC)
            BBA: Bd0898(adhC)
            MXA: MXAN_7094
            MLO: mlr0872
            MES: Meso_2671 Meso_3683
            SME: SMb20170(fdh) SMc01270(adhC1)
            ATU: Atu1670(adhC)
            ATC: AGR_C_3072
            RET: RHE_CH02227(adhCch)
            RLE: pRL120524(adhI)
            BJA: bll7898 blr6215(adhC)
            BRA: BRADO0921(adh) BRADO1941(fdh) BRADO5486(adhC)
            BBT: BBta_2247(fdh) BBta_5970(adhC) BBta_7131(adh)
            RPA: RPA1955
            RPB: RPB_3418
            RPD: RPD_2034
            RPE: RPE_4678
            NWI: Nwi_1739
            CCR: CC_2516 CC_3029
            SIL: SPO3850 SPOA0272
            RSP: RSP_2576(adhI) RSP_3104(fdh)
            RDE: RD1_0887(flhA) RD1_3806(flhA)
            HNE: HNE_0560
            ZMO: ZMO1722(adhC)
            GOX: GOX2018
            BSU: BG11902(adhB)
            BHA: BH1829(adhB)
            BAN: BA3131(adhB)
            BAR: GBAA3131(adhB)
            BAA: BA_3633
            BAT: BAS2912
            BCE: BC3092
            BCA: BCE_3145(adhB)
            BCZ: BCZK2838(adhB)
            BTK: BT9727_2881(adhB)
            BLI: BL02473(adhB)
            BLD: BLi03831(adhB)
            BCL: ABC3413 ABC3428(adhB)
            BPU: BPUM_0237
            GKA: GK0938 GK2774
            SSP: SSP1623
            SMU: SMU.119(adh)
            CAC: CAC3375
            DSY: DSY3044
            MTU: Rv0761c(adhB)
            MTC: MT0786
            MBO: Mb0784c(adhB)
            MPA: MAP0595c(adhB)
            MAV: MAV_4101
            MSM: MSMEG_0671 MSMEG_3388 MSMEG_6616
            NFA: nfa12770 nfa16040 nfa20970
            RHA: RHA1_ro02832
            TFU: Tfu_1270
            FRA: Francci3_1449
            FAL: FRAAL3376(adhC) FRAAL5467 FRAAL6444(fdh)
            RBA: RB10733(fdh)
            SYN: sll0990
            SYC: syc1059_d
            SYF: Synpcc7942_0459
            SYX: SynWH7803_0877(adhC)
            GVI: gll0735 glr4425
            ANA: all2810 alr0897
            AVA: Ava_1089 Ava_4500
            PMB: A9601_14521(adhC)
            TER: Tery_2840
            SSO: SSO0472(adh-1)
            STO: ST2056
            SAI: Saci_2145(adh)
STRUCTURES  PDB: 2FZE  2FZW  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.284
            ExPASy - ENZYME nomenclature database: 1.1.1.284
            ExplorEnz - The Enzyme Database: 1.1.1.284
            ERGO genome analysis and discovery system: 1.1.1.284
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.284
            BRENDA, the Enzyme Database: 1.1.1.284
///
ENTRY       EC 1.1.1.285                Enzyme
NAME        3"-deamino-3"-oxonicotianamine reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2'-deoxymugineic acid:NAD(P)+ 3''-oxidoreductase
REACTION    2'-deoxymugineic acid + NAD(P)+ = 3"-deamino-3"-oxonicotianamine +
            NAD(P)H + H+ [RN:R07141 R07142]
ALL_REAC    R07141 R07142
SUBSTRATE   2'-deoxymugineic acid [CPD:C15485];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     3''-deamino-3''-oxonicotianamine [CPD:C15486];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Shojima, S., Nishizawa, N.-K., Fushiya, S., Nozoe, S., Irifune, T.
            and Mori, S.
  TITLE     In vitro biosynthesis of 2'-deoxymugineic acid from L-methionine and
            nicotianamine.
  JOURNAL   Plant Physiol. 93 (1990) 1497-1503.
  ORGANISM  Hordeum vulgare [GN:ehvu]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.285
            ExPASy - ENZYME nomenclature database: 1.1.1.285
            ExplorEnz - The Enzyme Database: 1.1.1.285
            ERGO genome analysis and discovery system: 1.1.1.285
            BRENDA, the Enzyme Database: 1.1.1.285
///
ENTRY       EC 1.1.1.286                Enzyme
NAME        isocitrate---homoisocitrate dehydrogenase;
            homoisocitrate---isocitrate dehydrogenase;
            PH1722
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     isocitrate(homoisocitrate):NAD+ oxidoreductase (decarboxylating)
REACTION    (1) isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH [RN:R00709];
            (2) (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ =
            2-oxoadipate + CO2 + NADH + H+ [RN:R01934]
ALL_REAC    R00709 R01934
SUBSTRATE   isocitrate [CPD:C00311];
            NAD+ [CPD:C00003];
            (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate [CPD:C05662]
PRODUCT     2-oxoglutarate [CPD:C00026];
            CO2 [CPD:C00011];
            NADH [CPD:C00004];
            2-oxoadipate [CPD:C00322];
            H+ [CPD:C00080]
COMMENT     Requres Mn2+ and K+ or NH4+ for activity. Unlike EC 1.1.1.41,
            isocitrate dehydrogenase (NAD+) and EC 1.1.1.87, homoisocitrate
            dehydrogenase, this enzyme, from Pyrococcus horikoshii, can use both
            isocitrate and homoisocitrate as substrates. The enzyme may play a
            role in both the lysine and glutamate biosynthesis pathways.
REFERENCE   1  [PMID:15845397]
  AUTHORS   Miyazaki K.
  TITLE     Bifunctional isocitrate-homoisocitrate dehydrogenase: a missing link
            in the evolution of beta-decarboxylating dehydrogenase.
  JOURNAL   Biochem. Biophys. Res. Commun. 331 (2005) 341-6.
  ORGANISM  Pyrococcus horikoshii [GN:pho]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.286
            ExPASy - ENZYME nomenclature database: 1.1.1.286
            ExplorEnz - The Enzyme Database: 1.1.1.286
            ERGO genome analysis and discovery system: 1.1.1.286
            BRENDA, the Enzyme Database: 1.1.1.286
///
ENTRY       EC 1.1.1.287                Enzyme
NAME        D-arabinitol dehydrogenase (NADP+);
            NADP+-dependent D-arabitol dehydrogenase;
            ARD1p;
            D-arabitol dehydrogenase 1
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-arabinitol:NADP+ oxidoreductase
REACTION    (1) D-arabinitol + NADP+ = D-xylulose + NADPH + H+ [RN:R07143];
            (2) D-arabinitol + NADP+ = D-ribulose + NADPH + H+ [RN:R07144]
ALL_REAC    R07143 R07144
SUBSTRATE   D-arabinitol [CPD:C01904];
            NADP+ [CPD:C00006]
PRODUCT     D-xylulose [CPD:C00310];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            D-ribulose [CPD:C00309]
COMMENT     The enzyme from the rust fungus Uromyces fabae can use D-arabinitol
            and D-mannitol as substrates in the forward direction and
            D-xylulose, D-ribulose and, to a lesser extent, D-fructose as
            substrates in the reverse direction. This enzyme carries out the
            reactions of both EC 1.1.1.11, D-arabinitol 4-dehydrogenase and EC
            1.1.1.250, D-arabinitol 2-dehydrogenase, but unlike them, uses NADP+
            rather than NAD+ as cofactor. D-Arabinitol is capable of quenching
            reactive oxygen species involved in defense reactions of the host
            plant.
REFERENCE   1  [PMID:15796718]
  AUTHORS   Link T, Lohaus G, Heiser I, Mendgen K, Hahn M, Voegele RT.
  TITLE     Characterization of a novel NADP(+)-dependent D-arabitol
            dehydrogenase from the plant pathogen Uromyces fabae.
  JOURNAL   Biochem. J. 389 (2005) 289-95.
  ORGANISM  Uromyces fabae
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.287
            ExPASy - ENZYME nomenclature database: 1.1.1.287
            ExplorEnz - The Enzyme Database: 1.1.1.287
            ERGO genome analysis and discovery system: 1.1.1.287
            BRENDA, the Enzyme Database: 1.1.1.287
///
ENTRY       EC 1.1.1.288                Enzyme
NAME        xanthoxin dehydrogenase;
            xanthoxin oxidase;
            ABA2
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     xanthoxin:NAD+ oxidoreductase
REACTION    xanthoxin + NAD+ = abscisic aldehyde + NADH + H+
ALL_REAC    (other) R06954
SUBSTRATE   xanthoxin [CPD:C13453];
            NAD+ [CPD:C00003]
PRODUCT     abscisic aldehyde [CPD:C13455];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Requires a molybdenum cofactor for activity. NADP+ cannot replace
            NAD+ and short-chain alcohols such as ethanol, isopropanol, butanol
            and cyclohexanol cannot replace xanthoxin as substrate [3]. Involved
            in the abscisic-acid biosynthesis pathway in plants, along with EC
            1.2.3.14 (abscisic-aldehyde oxidase), EC 1.13.11.51
            (9-cis-epoxycarotenoid dioxygenase) and EC 1.14.13.93 [(+)-abscisic
            acid 8'-hydroxylase]. Abscisic acid is a sesquiterpenoid plant
            hormone that is involved in the control of a wide range of essential
            physiological processes, including seed development, germination and
            responses to stress [3].
REFERENCE   1
  AUTHORS   Sindhu, R.K. and Walton, D.C.
  TITLE     Xanthoxin metabolism in cell-free preparations from wild type and
            wilty mutants of tomato.
  JOURNAL   Plant Physiol. 88 (1988) 178-182.
REFERENCE   2  [PMID:9159947]
  AUTHORS   Schwartz SH, Leon-Kloosterziel KM, Koornneef M, Zeevaart JA.
  TITLE     Biochemical characterization of the aba2 and aba3 mutants in
            Arabidopsis thaliana.
  JOURNAL   Plant. Physiol. 114 (1997) 161-6.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   3  [PMID:12172025]
  AUTHORS   Gonzalez-Guzman M, Apostolova N, Belles JM, Barrero JM, Piqueras P,
            Ponce MR, Micol JL, Serrano R, Rodriguez PL.
  TITLE     The short-chain alcohol dehydrogenase ABA2 catalyzes the conversion
            of xanthoxin to abscisic aldehyde.
  JOURNAL   Plant. Cell. 14 (2002) 1833-46.
PATHWAY     PATH: map00906  Carotenoid biosynthesis - General
ORTHOLOGY   KO: K09841  xanthoxin dehydrogenase
GENES       ATH: AT1G52340(ABA2)
            OSA: 4334535
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.288
            ExPASy - ENZYME nomenclature database: 1.1.1.288
            ExplorEnz - The Enzyme Database: 1.1.1.288
            ERGO genome analysis and discovery system: 1.1.1.288
            BRENDA, the Enzyme Database: 1.1.1.288
///
ENTRY       EC 1.1.1.289                Enzyme
NAME        sorbose reductase;
            Sou1p
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-glucitol:NADP+ oxidoreductase
REACTION    D-glucitol + NADP+ = L-sorbose + NADPH + H+ [RN:R07346]
ALL_REAC    R07346
SUBSTRATE   D-glucitol [CPD:C00794];
            NADP+ [CPD:C00006]
PRODUCT     L-sorbose [CPD:C00247];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The reaction occurs predominantly in the reverse direction. This
            enzyme can also convert D-fructose into D-mannitol, but more slowly.
            Belongs in the short-chain dehydrogenase family.
REFERENCE   1  [PMID:16134116]
  AUTHORS   Greenberg JR, Price NP, Oliver RP, Sherman F, Rustchenko E.
  TITLE     Candida albicans SOU1 encodes a sorbose reductase required for
            L-sorbose utilization.
  JOURNAL   Yeast. 22 (2005) 957-69.
  ORGANISM  Candida albicans [GN:cal]
REFERENCE   2
  AUTHORS   Greenberg, J.R., Price, N.P., Oliver, R.P., Sherman, F. and
            Rustchenko, E.
  TITLE     Erratum report: Candida albicans SOU1 encodes a sorbose reductase
            required for L-sorbose utilization.
  JOURNAL   Yeast 22 (2005) 1171.
REFERENCE   3
  AUTHORS   Sugisawa, T., Hoshino, T. and Fujiwara, A.
  TITLE     Purification and properties of NADPH-linked L-sorbose reductase from
            Gluconobacter melanogenus N44-1.
  JOURNAL   Agric. Biol. Chem. 55 (1991) 2043-2049.
  ORGANISM  Gluconobacter melanogenus
REFERENCE   4  [PMID:11790761]
  AUTHORS   Shinjoh M, Tazoe M, Hoshino T.
  TITLE     NADPH-dependent L-sorbose reductase is responsible for L-sorbose
            assimilation in Gluconobacter suboxydans IFO 3291.
  JOURNAL   J. Bacteriol. 184 (2002) 861-3.
  ORGANISM  Gluconobacter suboxydans
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.289
            ExPASy - ENZYME nomenclature database: 1.1.1.289
            ExplorEnz - The Enzyme Database: 1.1.1.289
            ERGO genome analysis and discovery system: 1.1.1.289
            BRENDA, the Enzyme Database: 1.1.1.289
///
ENTRY       EC 1.1.1.290                Enzyme
NAME        4-phosphoerythronate dehydogenase;
            PdxB;
            PdxB 4PE dehydrogenase;
            4-O-phosphoerythronate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4-phospho-D-erythronate:NAD+ 2-oxidoreductase
REACTION    4-phospho-D-erythronate + NAD+ =
            (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH + H+ [RN:R04210]
ALL_REAC    R04210
SUBSTRATE   4-phospho-D-erythronate [CPD:C03393];
            NAD+ [CPD:C00003]
PRODUCT     (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate [CPD:C06054];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     This enzyme catalyses the second step in the biosynthesis of the
            coenzyme pyridoxal 5'-phosphate in Escherichia coli. The reaction
            occurs predominantly in the reverse direction [3]. Other enzymes
            involved in this pathway are EC 1.2.1.72 (erythrose-4-phosphate
            dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC
            1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC
            2.6.99.2 (pyridoxine 5'-phosphate synthase) and EC 1.4.3.5
            (pyridoxamine-phosphate oxidase).
REFERENCE   1  [PMID:2121717]
  AUTHORS   Lam HM, Winkler ME.
  TITLE     Metabolic relationships between pyridoxine (vitamin B6) and serine
            biosynthesis in Escherichia coli K-12.
  JOURNAL   J. Bacteriol. 172 (1990) 6518-28.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:11844765]
  AUTHORS   Pease AJ, Roa BR, Luo W, Winkler ME.
  TITLE     Positive growth rate-dependent regulation of the pdxA, ksgA, and
            pdxB genes of Escherichia coli K-12.
  JOURNAL   J. Bacteriol. 184 (2002) 1359-69.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:8550422]
  AUTHORS   Zhao G, Winkler ME.
  TITLE     A novel alpha-ketoglutarate reductase activity of the serA-encoded
            3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its
            possible implications for human 2-hydroxyglutaric aciduria.
  JOURNAL   J. Bacteriol. 178 (1996) 232-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:2692566]
  AUTHORS   Grant GA.
  TITLE     A new family of 2-hydroxyacid dehydrogenases.
  JOURNAL   Biochem. Biophys. Res. Commun. 165 (1989) 1371-4.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:2681152]
  AUTHORS   Schoenlein PV, Roa BB, Winkler ME.
  TITLE     Divergent transcription of pdxB and homology between the pdxB and
            serA gene products in Escherichia coli K-12.
  JOURNAL   J. Bacteriol. 171 (1989) 6084-92.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00750  Vitamin B6 metabolism
ORTHOLOGY   KO: K03473  erythronate-4-phosphate dehydrogenase
GENES       ECO: b2320(pdxB)
            ECJ: JW2317(pdxB)
            ECE: Z3582(pdxB)
            ECS: ECs3204
            ECC: c2865(pdxB)
            ECI: UTI89_C2605(pdxB)
            ECP: ECP_2359
            ECV: APECO1_4244(pdxB)
            STY: STY2601(pdxB)
            STT: t0494(pdxB)
            SPT: SPA0494(pdxB)
            SEC: SC2372(pdxB)
            STM: STM2370(pdxB)
            YPE: YPO2763(pdxB)
            YPK: y1597(pdxB)
            YPM: YP_2400(pdxB)
            YPA: YPA_2080
            YPN: YPN_2183
            YPP: YPDSF_1997
            YPS: YPTB2620(pdxB)
            YEN: YE1307(pdxB)
            SFL: SF2396(pdxB)
            SFX: S2531(pdxB)
            SFV: SFV_2389(pdxB)
            SSN: SSON_2378(pdxB)
            SBO: SBO_2357(pdxB)
            SDY: SDY_2519(pdxB)
            ECA: ECA3060(pdxB)
            PLU: plu3175(pdxB)
            WBR: WGLp308(pdxB)
            SGL: SG1621
            BFL: Bfl497(pdxB)
            BPN: BPEN_513(pdxB)
            VCH: VC2108
            VVU: VV1_1988
            VVY: VV2428
            VPA: VP2193
            VFI: VF1699
            PPR: PBPRA2656
            PAE: PA1375(pdxB)
            PAU: PA14_46470(pdxB)
            PPU: PP_2117(pdxB)
            PST: PSPTO_2019(pdxB)
            PSB: Psyr_1828
            PSP: PSPPH_1788
            PFL: PFL_1933(serA)
            PFO: Pfl_3886
            PEN: PSEEN3753(pdxB)
            PAR: Psyc_0272
            PCR: Pcryo_0298
            ACI: ACIAD2667(pdxB)
            ACB: A1S_2637
            SON: SO_3071(pdxB)
            SDN: Sden_1483
            SFR: Sfri_1392
            SAZ: Sama_2153
            SBL: Sbal_2745
            SLO: Shew_2309
            SHE: Shewmr4_1423
            SHM: Shewmr7_1488
            SHN: Shewana3_1476
            SHW: Sputw3181_1564
            ILO: IL1020(pdxB)
            CPS: CPS_3806(pdxB)
            PHA: PSHAa2079(pdxB)
            PAT: Patl_3364
            SDE: Sde_1159
            PIN: Ping_1994
            MAQ: Maqu_1775
            CBU: CBU_1812
            CBD: COXBU7E912_0041(pdxB)
            LPN: lpg0918
            LPF: lpl0949(pdxB)
            LPP: lpp0979(pdxB)
            TCX: Tcr_0451
            HCH: HCH_02292
            CSA: Csal_1346
            ABO: ABO_1177(pdxB)
            AHA: AHA_2683
            BCI: BCI_0363(pdxB)
            RMA: Rmag_0684
            BTH: BT_3361
            BFR: BF0222
            BFS: BF0181(pdxB)
            PGI: PG1220
            SRU: SRU_2082(pdxB)
STRUCTURES  PDB: 2O4C  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.290
            ExPASy - ENZYME nomenclature database: 1.1.1.290
            ExplorEnz - The Enzyme Database: 1.1.1.290
            ERGO genome analysis and discovery system: 1.1.1.290
            BRENDA, the Enzyme Database: 1.1.1.290
///
ENTRY       EC 1.1.1.291                Enzyme
NAME        2-hydroxymethylglutarate dehydrogenase;
            HgD
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-2-hydroxymethylglutarate:NAD+ oxidoreductase
REACTION    (S)-2-hydroxymethylglutarate + NAD+ = 2-formylglutarate + NADH + H+
            [RN:R07985]
ALL_REAC    R07985
SUBSTRATE   (S)-2-hydroxymethylglutarate;
            NAD+ [CPD:C00003]
PRODUCT     2-formylglutarate [CPD:C16159];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     NADP+ cannot replace NAD+. Forms part of the nicotinate-fermentation
            catabolism pathway in Eubacterium barkeri. Other enzymes involved in
            this pathway are EC 1.17.1.5 (nicotinate dehydrogenase), EC 1.3.7.1
            (6-hydroxynicotinate reductase), EC 3.5.2.18 (enamidase), EC
            5.4.99.4 (2-methyleneglutarate mutase), EC 5.3.3.6 (methylitaconate
            Delta-isomerase), EC 4.2.1.85 (dimethylmaleate hydratase) and EC
            4.1.3.32 (2,3-dimethylmalate lyase).
REFERENCE   1  [PMID:16894175]
  AUTHORS   Alhapel A, Darley DJ, Wagener N, Eckel E, Elsner N, Pierik AJ.
  TITLE     Molecular and functional analysis of nicotinate catabolism in
            Eubacterium barkeri.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 12341-6.
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.291
            ExPASy - ENZYME nomenclature database: 1.1.1.291
            ExplorEnz - The Enzyme Database: 1.1.1.291
            ERGO genome analysis and discovery system: 1.1.1.291
            BRENDA, the Enzyme Database: 1.1.1.291
///
ENTRY       EC 1.1.1.292                Enzyme
NAME        1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming);
            1,5-anhydro-D-fructose reductase (ambiguous);
            AFR
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     1,5-anhydro-D-mannitol:NADP+ oxidoreductase
REACTION    1,5-anhydro-D-mannitol + NADP+ = 1,5-anhydro-D-fructose + NADPH + H+
SUBSTRATE   1,5-anhydro-D-mannitol;
            NADP+ [CPD:C00006]
PRODUCT     1,5-anhydro-D-fructose [CPD:C06485];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     This enzyme is present in some but not all Rhizobium species and
            belongs in the GFO/IDH/MocA protein family [2]. This enzyme differs
            from hepatic 1,5-anhydro-D-fructose reductase, which yields
            1,5-anhydro-D-glucitol as the product (see EC 1.1.1.263). In
            Sinorhizobium morelense, the product of the reaction,
            1,5-anhydro-D-mannitol, can be further metabolized to D-mannose [1].
            The enzyme also reduces 1,5-anhydro-D-erythro-hexo-2,3-diulose and
            2-ketoaldoses (called osones), such as D-glucosone
            (D-arabino-hexos-2-ulose) and 6-deoxy-D-glucosone. It does not
            reduce common aldoses and ketoses, or non-sugar aldehydes and
            ketones [1].
REFERENCE   1  [PMID:16461673]
  AUTHORS   Kuhn A, Yu S, Giffhorn F.
  TITLE     Catabolism of 1,5-anhydro-D-fructose in Sinorhizobium morelense
            S-30.7.5: discovery, characterization, and overexpression of a new
            1,5-anhydro-D-fructose reductase and its application in sugar
            analysis and rare sugar synthesis.
  JOURNAL   Appl. Environ. Microbiol. 72 (2006) 1248-57.
REFERENCE   2  [PMID:16906761]
  AUTHORS   Dambe TR, Kuhn AM, Brossette T, Giffhorn F, Scheidig AJ.
  TITLE     Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose
            reductase from Sinorhizobium morelense at 2.2 A resolution:
            construction of a NADH-accepting mutant and its application in rare
            sugar synthesis.
  JOURNAL   Biochemistry. 45 (2006) 10030-42.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.292
            ExPASy - ENZYME nomenclature database: 1.1.1.292
            ExplorEnz - The Enzyme Database: 1.1.1.292
            ERGO genome analysis and discovery system: 1.1.1.292
            BRENDA, the Enzyme Database: 1.1.1.292
///
ENTRY       EC 1.1.1.293      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: tropinone reductase I. This enzyme was already in the
            Enzyme List as EC 1.1.1.206, tropine dehydrogenase so EC 1.1.1.293
            has been withdrawn at the public-review stage. (EC 1.1.1.293 created
            2007, withdrawn while undergoing public review)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.1.293
            ExPASy - ENZYME nomenclature database: 1.1.1.293
            ExplorEnz - The Enzyme Database: 1.1.1.293
            ERGO genome analysis and discovery system: 1.1.1.293
            BRENDA, the Enzyme Database: 1.1.1.293
///
ENTRY       EC 1.1.1.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With NAD+ or NADP+ as acceptor
REACTION    (1) UDP-D-galactose + 2 NAD+ + H2O <=> UDP-D-galacturonate + 2 NADH
            + 2 H+ [RN:R00501];
            (2) Methylglyoxal + NADPH <=> Hydroxyacetone + NADP+ [RN:R02528];
            (3) dTDP-glucose + 2 NADP+ + H2O <=> dTDP-D-glucuronate + 2 NADPH +
            2 H+ [RN:R02983];
            (4) beta-D-Galactose + NADPH <=> 3-Keto-beta-D-galactose + NADP+
            [RN:R03113];
            (5) Sorbitol 6-phosphate + NADP+ <=> Sorbose 1-phosphate + NADPH
            [RN:R03234];
            (6) UDP-N-acetyl-D-mannosamine + 2 NAD+ + H2O <=>
            UDP-N-acetyl-D-mannosaminouronate + 2 NADH + 2 H+ [RN:R03317];
            (7) Butanal + NADH <=> 1-Butanol + NAD+ [RN:R03544];
            (8) Butanal + NADPH + H+ <=> 1-Butanol + NADP+ [RN:R03545];
            (9) (S)-Mandelate + NAD+ <=> alpha-Oxo-benzeneacetic acid + NADH
            [RN:R03792];
            (10) 5-Acetamidopentanoate + NADH + H+ + CO2 <=>
            6-Acetamido-2-oxohexanoate + NAD+ + H2O [RN:R04142];
            (11) 2-Dehydro-3-deoxy-D-xylonate + NAD+ <=>
            (4S)-5-Hydroxy-2,4-dioxopentanoate + NADH [RN:R04375];
            (12) 3alpha,7alpha,24-Trihydroxy-5beta-cholestanoyl-CoA + NAD+ <=>
            3alpha,7alpha-Dihydroxy-5beta-24-oxocholestanoyl-CoA + NADH
            [RN:R04810];
            (13) 3alpha,7alpha,12alpha,24-Tetrahydroxy-5beta-cholestanoyl-CoA +
            NAD+ <=>
            3alpha,7alpha,12alpha-Trihydroxy-5beta-24-oxocholestanoyl-CoA + NADH
            [RN:R04812];
            (14) Ethylene oxide + CoA + NAD+ <=> Acetyl-CoA + NADH + H+
            [RN:R05351];
            (15) 6-Hydroxycyclohex-1-enecarbonyl-CoA + NAD+ <=>
            6-Ketoxycyclohex-1-ene-1-carboxyl-CoA + NADH + H+ [RN:R05581];
            (16) 2-Hydroxycyclohexane-1-carboxyl-CoA + NAD+ <=>
            2-Ketocyclohexane-1-carboxyl-CoA + NADH + H+ [RN:R05582];
            (17) 1-(4'-Hydroxyphenyl)ethanol + NAD+ <=> 4'-Hydroxyacetophenone +
            NADH + H+ [RN:R06891];
            (18) UDP-N-acetyl-D-galactosamine + 2 NAD+ + H2O <=>
            UDP-N-acetyl-D-galactosaminuronic acid + 2 NADH + 2 H+ [RN:R06894];
            (19) UDP-glucuronate + NAD+ <=> UDP-L-Ara4O + CO2 + NADH + H+
            [RN:R07658];
            (20) L-Galactonate + NADP+ <=> D-Galacturonate + NADPH + H+
            [RN:R07676];
            (21) 3-Oxostearoyl-CoA + NADPH + H+ <=> 3-Hydroxyoctadecanoyl-CoA +
            NADP+ [RN:R07759]
SUBSTRATE   UDP-D-galactose [CPD:C00052];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001];
            Methylglyoxal [CPD:C00546];
            NADPH [CPD:C00005];
            dTDP-glucose [CPD:C00842];
            NADP+ [CPD:C00006];
            beta-D-Galactose [CPD:C00962];
            Sorbitol 6-phosphate [CPD:C01096];
            UDP-N-acetyl-D-mannosamine [CPD:C01170];
            Butanal [CPD:C01412];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            (S)-Mandelate [CPD:C01984];
            5-Acetamidopentanoate [CPD:C03087];
            CO2 [CPD:C00011];
            2-Dehydro-3-deoxy-D-xylonate [CPD:C03826];
            3alpha,7alpha,24-Trihydroxy-5beta-cholestanoyl-CoA [CPD:C05448];
            3alpha,7alpha,12alpha,24-Tetrahydroxy-5beta-cholestanoyl-CoA
            [CPD:C05450];
            Ethylene oxide [CPD:C06548];
            CoA [CPD:C00010];
            6-Hydroxycyclohex-1-enecarbonyl-CoA [CPD:C06749];
            2-Hydroxycyclohexane-1-carboxyl-CoA [CPD:C09812];
            1-(4'-Hydroxyphenyl)ethanol [CPD:C13638];
            UDP-N-acetyl-D-galactosamine [CPD:C00203]
PRODUCT     UDP-D-galacturonate [CPD:C00617];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            Hydroxyacetone [CPD:C05235];
            NADP+ [CPD:C00006];
            dTDP-D-glucuronate [CPD:C06017];
            NADPH [CPD:C00005];
            3-Keto-beta-D-galactose [CPD:C05394];
            Sorbose 1-phosphate [CPD:C02888];
            UDP-N-acetyl-D-mannosaminouronate [CPD:C06240];
            1-Butanol [CPD:C06142];
            NAD+ [CPD:C00003];
            alpha-Oxo-benzeneacetic acid [CPD:C02137];
            6-Acetamido-2-oxohexanoate [CPD:C05548];
            H2O [CPD:C00001];
            (4S)-5-Hydroxy-2,4-dioxopentanoate [CPD:C05406];
            3alpha,7alpha-Dihydroxy-5beta-24-oxocholestanoyl-CoA [CPD:C05449];
            3alpha,7alpha,12alpha-Trihydroxy-5beta-24-oxocholestanoyl-CoA
            [CPD:C05467];
            Acetyl-CoA [CPD:C00024];
            6-Ketoxycyclohex-1-ene-1-carboxyl-CoA [CPD:C09821];
            2-Ketocyclohexane-1-carboxyl-CoA [CPD:C09813];
            4'-Hydroxyacetophenone [CPD:C10700];
            UDP-N-acetyl-D-galactosaminuronic acid [CPD:C13952]
///
ENTRY       EC 1.1.2.1        Obsolete  Enzyme
NAME        Transferred to 1.1.99.5
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With a cytochrome as acceptor
COMMENT     Transferred entry: now EC 1.1.99.5 glycerol-3-phosphate
            dehydrogenase (EC 1.1.2.1 created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.2.1
            ExPASy - ENZYME nomenclature database: 1.1.2.1
            ExplorEnz - The Enzyme Database: 1.1.2.1
            ERGO genome analysis and discovery system: 1.1.2.1
            BRENDA, the Enzyme Database: 1.1.2.1
///
ENTRY       EC 1.1.2.2                  Enzyme
NAME        mannitol dehydrogenase (cytochrome);
            polyol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With a cytochrome as acceptor
SYSNAME     D-mannitol:ferricytochrome-c 2-oxidoreductase
REACTION    D-mannitol + ferricytochrome c = D-fructose + ferrocytochrome c
            [RN:R00865]
ALL_REAC    R00865;
            (other) R01892
SUBSTRATE   D-mannitol [CPD:C00392];
            ferricytochrome c [CPD:C00125]
PRODUCT     D-fructose [CPD:C00095];
            ferrocytochrome c [CPD:C00126]
COMMENT     Acts on polyols with a D-lyxo configuration, such as D-mannitol and
            D-sorbitol.
REFERENCE   1  [PMID:13373782]
  AUTHORS   ARCUS AC, EDSON NL.
  TITLE     Polyol dehydrogenases.  2.  The polyol dehydrogenases of Acetobacter
            suboxydans and Candida utilis.
  JOURNAL   Biochem. J. 64 (1956) 385-94.
  ORGANISM  Acetobacter suboxydans, Candida utilis
REFERENCE   2
  AUTHORS   Cho, N.C., Kim, K. and Jhon, D.Y.
  TITLE     Purification and characterization of polyol dehydrogenase from
            Gluconobacter melanogenus.
  JOURNAL   Han'guk Saenghwa Hakhaochi 23 (1990) 172-178.
  ORGANISM  Gluconobacter melanogenus
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00051  Fructose and mannose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.2.2
            ExPASy - ENZYME nomenclature database: 1.1.2.2
            ExplorEnz - The Enzyme Database: 1.1.2.2
            ERGO genome analysis and discovery system: 1.1.2.2
            BRENDA, the Enzyme Database: 1.1.2.2
            CAS: 37250-78-5
///
ENTRY       EC 1.1.2.3                  Enzyme
NAME        L-lactate dehydrogenase (cytochrome);
            lactic acid dehydrogenase;
            cytochrome b2 (flavin-free derivative of flavocytochrome b2);
            flavocytochrome b2;
            L-lactate cytochrome c reductase;
            L(+)-lactate:cytochrome c oxidoreductase;
            dehydrogenase, lactate (cytochrome);
            L-lactate cytochrome c oxidoreductase;
            lactate dehydrogenase (cytochrome);
            lactic cytochrome c reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With a cytochrome as acceptor
SYSNAME     (S)-lactate:ferricytochrome-c 2-oxidoreductase
REACTION    (S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c +
            2 H+ [RN:R00196]
ALL_REAC    R00196
SUBSTRATE   (S)-lactate [CPD:C00186];
            ferricytochrome c [CPD:C00125]
PRODUCT     pyruvate [CPD:C00022];
            ferrocytochrome c [CPD:C00126];
            H+ [CPD:C00080]
COFACTOR    Heme [CPD:C00032];
            FMN [CPD:C00061]
COMMENT     Identical with cytochrome b2; a flavohemoprotein (FMN).
REFERENCE   1  [PMID:13638255]
  AUTHORS   APPLEBY CA, MORTON RK.
  TITLE     Lactic dehydrogenase and cytochrome b2 of baker's yeast;
            purification and crystallization.
  JOURNAL   Biochem. J. 71 (1959) 492-9.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:13793977]
  AUTHORS   APPLEBY CA, MORTON RK.
  TITLE     Lactic dehydrogenase and cytochrome b2 of baker's yeast. Enzymic and
            chemical properties of the crystalline enzyme.
  JOURNAL   Biochem. J. 73 (1959) 539-50.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:16747991]
  AUTHORS   Bach SJ, Dixon M, Zerfas LG.
  TITLE     Yeast lactic dehydrogenase and cytochrome b(2).
  JOURNAL   Biochem. J. 40 (1946) 229-39.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4
  AUTHORS   Nygaard, A.P.
  TITLE     Lactate dehydrogenases of yeast.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 557-565.
PATHWAY     PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K00101  L-lactate dehydrogenase (cytochrome)
GENES       XLA: 444538(MGC82107)
            SCE: YML054C(CYB2)
            PIC: PICST_53263(CYB3)
            SPO: SPAPB1A11.03
            ANI: AN3901.2 AN4424.2
            AFM: AFUA_1G07200 AFUA_4G03120 AFUA_4G07020
            AOR: AO090011000188 AO090102000252
            CNE: CNH01230 CNL04570
            UMA: UM04746.1
            ECO: b3605(lldD)
            ECJ: JW3580(lldD)
            ECE: Z5032(lldD)
            ECS: ECs4483
            ECC: c4427(lldD)
            ECI: UTI89_C4146(lldD)
            ECP: ECP_3706
            ECV: APECO1_2850(lldD)
            ECW: EcE24377A_4109(lldD)
            ECX: EcHS_A3817(lldD)
            STY: STY4102(lctD)
            STT: t3825(lctD)
            SPT: SPA3546(lctD)
            SEC: SC3618(lldD)
            STM: STM3694(lldD)
            YPE: YPO1569(lldD)
            YPK: y2596(lldD)
            YPM: YP_1457(lldD)
            YPA: YPA_0864
            YPN: YPN_2411
            YPP: YPDSF_1407
            YPS: YPTB1578(lldD)
            YPI: YpsIP31758_2409(lldD)
            SFL: SF3644(lldD)
            SFX: S4124(lldD)
            SFV: SFV_3926(lldD)
            SSN: SSON_3800(lldD)
            SBO: SBO_3610(lldD)
            SDY: SDY_4038(lldD)
            ECA: ECA0119(lctD)
            PLU: plu1106
            HIN: HI1739.1(lctD)
            HIT: NTHI2049(lldD)
            HIP: CGSHiEE_03365(lldD)
            HIQ: CGSHiGG_02435(lldD)
            HDU: HD0084(lldD)
            PMU: PM0288(lldD)
            APL: APL_1849(lldD)
            XCC: XCC0106(lctD)
            XCB: XC_0110
            XCV: XCV0110(lctD)
            XAC: XAC0133(lctD)
            XOO: XOO0022(lctD)
            XOM: XOO_0022(XOO0022)
            VCH: VCA0984
            VCO: VC0395_0254(lldD)
            VPA: VPA1499
            PAE: PA2382(lldA) PA4771(lldD)
            PAU: PA14_33860(lldA) PA14_63090(lldD)
            PPU: PP_4736(lldD)
            PSB: Psyr_0908
            PEN: PSEEN0767(lldD)
            PAR: Psyc_1654(lldA)
            PCR: Pcryo_1889
            ACI: ACIAD0108(lldD)
            CPS: CPS_2083
            FTU: FTT0303c(lldD)
            FTF: FTF0303c(lldD1)
            FTW: FTW_1032 FTW_1782(lldD)
            FTL: FTL_0214 FTL_0970
            FTH: FTH_0209(lldD) FTH_0948(lldA)
            FTN: FTN_0217 FTN_0991(lldD)
            MMW: Mmwyl1_1831
            NME: NMB1377
            NMA: NMA1592(lldA)
            NMC: NMC1312(lldA)
            NGO: NGO0639
            REU: Reut_A1661 Reut_C6258
            REH: H16_B0460(lldA) H16_B1817(lldD)
            BMA: BMAA0374(lldD) BMAA1565
            BMV: BMASAVP1_1563(lldD)
            BML: BMA10299_1750(lldD)
            BMN: BMA10247_A0415(lldD)
            BXE: Bxe_A2428 Bxe_A3368 Bxe_B0136 Bxe_C0228
            BPS: BPSS1560(mdlB) BPSS2125(lldA)
            BPM: BURPS1710b_A0604(mdlB) BURPS1710b_A1229(lldA)
            BPL: BURPS1106A_A2872
            BPD: BURPS668_A2580(lldD) BURPS668_A2990
            BTE: BTH_II0813
            PNU: Pnuc_1371
            BPE: BP0484(lldD) BP1293(lldD) BP1669(lldA)
            BPA: BPP2925(lldD) BPP4394(lldD)
            BBR: BB1109(lldD) BB2895(lldD) BB4980(lldD)
            RFR: Rfer_2351
            POL: Bpro_3678
            PNA: Pnap_3154
            AAV: Aave_1959
            VEI: Veis_3178
            MPT: Mpe_A0360 Mpe_A2829
            HAR: HEAR1710(lldD)
            MMS: mma_1588(lldD)
            AZO: azo1016(lldA) azo2470(lldD)
            CCV: CCV52592_0468
            PUB: SAR11_0280(ildD)
            MLO: mll6909
            PLA: Plav_0762
            SME: SMb20850(lldD3) SMc01712(lldD2) SMc01740(lldD1)
            SMD: Smed_4493 Smed_5475
            ATU: Atu2318(lldA) Atu3871(lldA)
            ATC: AGR_C_4216 AGR_L_1949
            RET: RHE_CH00425(lldD1) RHE_CH01847(lldD2) RHE_CH03131(lldD3)
            RLE: RL0444(lldD) RL2067(lldD) RL3578(lldD)
            BME: BMEII0377
            BMF: BAB2_0315(lldD)
            BMS: BRA0920(lldD)
            BMB: BruAb2_0313(lldD)
            BOV: BOV_A0862(lldD)
            BJA: bll6401 blr7409
            BRA: BRADO5958
            BBT: BBta_1816
            RPA: RPA4320(lldA)
            RPB: RPB_1305
            RPC: RPC_4115
            RPD: RPD_3916
            RPE: RPE_4170
            NHA: Nham_1112
            BHE: BH02710(lldD)
            BQU: BQ02590(lldD)
            CCR: CC_1151
            SIL: SPO0598 SPO0813 SPO1172
            SIT: TM1040_0219 TM1040_2026
            RSP: RSP_0829(lctB)
            RSH: Rsph17029_2487
            RSQ: Rsph17025_0350
            JAN: Jann_3598
            RDE: RD1_3375(lldD) RD1_3814(lldD) RD1_3896
            PDE: Pden_4075 Pden_4877 Pden_5062
            HNE: HNE_1192(lldD)
            NAR: Saro_1050
            SWI: Swit_4230
            MAG: amb4454
            LAC: LBA1598(lldD)
            MTU: Rv0694(lldD1) Rv1872c(lldD2)
            MTC: MT0721 MT1921(lldD)
            MBO: Mb0713(lldD1) Mb1903c(lldD2)
            MBB: BCG_0743(lldD1) BCG_1908c(lldD2)
            MLE: ML2046(lldD2)
            MPA: MAP1585c(lldD2) MAP4154(lldD1)
            CGL: NCgl2817(cgl2918)
            CGB: cg3227(lldA)
            CEF: CE2762
            CJK: jk1705(lldD)
            NFA: nfa22320 nfa32080 nfa32960(lldD)
            RHA: RHA1_ro02988 RHA1_ro10281
            ART: Arth_3343
            AAU: AAur_3324(lldD)
            FRA: Francci3_2407
            FAL: FRAAL4104
            KRA: Krad_1384
            SEN: SACE_2390(lldD1) SACE_4311(lldD2) SACE_5887(lldD2)
            PMA: Pro1754(lldD)
            PME: NATL1_20471(lldD)
            TER: Tery_2488
STRUCTURES  PDB: 1FCB  1KBI  1KBJ  1LCO  1LDC  1LTD  1QCW  1SZE  1SZF  1SZG  
                 2OZ0  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.2.3
            ExPASy - ENZYME nomenclature database: 1.1.2.3
            ExplorEnz - The Enzyme Database: 1.1.2.3
            ERGO genome analysis and discovery system: 1.1.2.3
            BRENDA, the Enzyme Database: 1.1.2.3
            CAS: 9078-32-4
///
ENTRY       EC 1.1.2.4                  Enzyme
NAME        D-lactate dehydrogenase (cytochrome);
            lactic acid dehydrogenase;
            D-lactate (cytochrome) dehydrogenase;
            cytochrome-dependent D-(-)-lactate dehydrogenase;
            D-lactate-cytochrome c reductase;
            D-(-)-lactic cytochrome c reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With a cytochrome as acceptor
SYSNAME     (R)-lactate:ferricytochrome-c 2-oxidoreductase
REACTION    (R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c
            [RN:R00197]
ALL_REAC    R00197
SUBSTRATE   (R)-lactate [CPD:C00256];
            ferricytochrome c [CPD:C00125]
PRODUCT     pyruvate [CPD:C00022];
            ferrocytochrome c [CPD:C00126]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:13950255]
  AUTHORS   GREGOLIN C, SINGER TP.
  TITLE     The lactic dehydrogenase of yeast. III. D(-)Lactic cytochrome c
            reductase, a zinc-flavoprotein from aerobic yeast.
  JOURNAL   Biochim. Biophys. Acta. 67 (1963) 201-18.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:13901630]
  AUTHORS   GREGOLIN C, SINGER TP, KEARNEY EB, BOERI E.
  TITLE     The formation and enzymatic properties of the various lactic
            dehydrogenases of yeast.
  JOURNAL   Ann. N. Y. Acad. Sci. 94 (1961) 780-97.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Nygaard, A.P.
  TITLE     D(-)-Lactate cytochrome c reductase, a flavoprotein from yeast.
  JOURNAL   J. Biol. Chem. 236 (1961) 920-925.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4
  AUTHORS   Nygaard, A.P.
  TITLE     Lactate dehydrogenases of yeast.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 557-565.
PATHWAY     PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K00102  D-lactate dehydrogenase (cytochrome)
GENES       SCE: YDL174C(DLD1)
            AGO: AGOS_AER321W
            PIC: PICST_31583(DLD3) PICST_52647(DLD4) PICST_86747(DLD1)
                 PICST_89565(DLD2)
            CGR: CAGL0I05148g CAGL0J06314g
            ANI: AN9066.2
            AFM: AFUA_1G00510 AFUA_1G17520 AFUA_3G06820 AFUA_7G02560
            AOR: AO090038000632
            ECI: UTI89_C1879(ydiJ)
            PPF: Pput_4603
            PFL: PFL_3836
            PCR: Pcryo_1885
            PRW: PsycPRwf_2348
            SSE: Ssed_1872
            NOC: Noc_1924
            MMW: Mmwyl1_0072
            RSO: RSc2664(dld)
            REU: Reut_A2787
            REH: H16_A3091(dld)
            RME: Rmet_2924
            BMA: BMA2415 BMAA0959
            BXE: Bxe_A3977
            BUR: Bcep18194_A3301 Bcep18194_A3819 Bcep18194_A3820
                 Bcep18194_A3821 Bcep18194_A4598 Bcep18194_B0032
                 Bcep18194_B0033 Bcep18194_B3025 Bcep18194_C7432
                 Bcep18194_C7704
            BAM: Bamb_0625 Bamb_6129
            BPS: BPSL2842 BPSS1318
            BPM: BURPS1710b_1859 BURPS1710b_3341 BURPS1710b_A0337
            BTE: BTH_I1292
            PNU: Pnuc_1781
            BPE: BP2906
            BPA: BPP2490
            BBR: BB1937
            RFR: Rfer_1477
            POL: Bpro_0111 Bpro_2755
            VEI: Veis_4691
            MPT: Mpe_A3774
            HAR: HEAR1203 HEAR2733
            EBA: ebA3803(dldH)
            AZO: azo3432(dld)
            DAR: Daro_0268
            HPY: HP1222(dld)
            HPA: HPAG1_1164
            HAC: Hac_1598(dld)
            DVL: Dvul_2154 Dvul_2544 Dvul_2725
            DDE: Dde_0182
            ADE: Adeh_2867
            AFW: Anae109_2921
            MLO: mll1488
            PLA: Plav_2439
            SMD: Smed_0394 Smed_2031
            RET: RHE_CH02804(dld)
            RLE: RL0959 RL3261 pRL120180
            BME: BMEI0599
            BMF: BAB1_1429
            BMS: BR1410
            BMB: BruAb1_1405
            OAN: Oant_3010
            BJA: bll2678 bll6558
            BRA: BRADO2057 BRADO5280 BRADO5609
            BBT: BBta_2386 BBta_5731 BBta_6133
            RPA: RPA3503
            RPB: RPB_2026
            RPD: RPD_4137
            RPE: RPE_2140 RPE_4381
            XAU: Xaut_1422
            SIL: SPO0634
            SIT: TM1040_0483 TM1040_2502
            RSP: RSP_0177 RSP_2120
            RSH: Rsph17029_0795
            JAN: Jann_1163 Jann_1937
            RDE: RD1_2145 RD1_3435
            PDE: Pden_2187
            NAR: Saro_0816
            SWI: Swit_0991
            ACR: Acry_1462
            RRU: Rru_A0442 Rru_A1124 Rru_A1299 Rru_A1410
            MAG: amb2985
            BAN: BA3575
            BAR: GBAA3575
            BAA: BA_4067
            BAT: BAS3315
            BCE: BC3504
            BCA: BCE_3530
            BCZ: BCZK3230(glcD)
            BTK: BT9727_3278
            OIH: OB1259 OB1357
            GKA: GK3215
            AMT: Amet_0764
            MMC: Mmcs_3961
            MKM: Mkms_4035
            MJL: Mjls_3975
            RHA: RHA1_ro03236 RHA1_ro08314
            NCA: Noca_2155
            FRA: Francci3_0962 Francci3_1983 Francci3_2007
            SEN: SACE_3640 SACE_3788 SACE_6365
            RXY: Rxyl_2833
            AVA: Ava_2520 Ava_4556
            TER: Tery_4091
            FJO: Fjoh_2129 Fjoh_4811
            CCH: Cag_0799 Cag_1163
            PVI: Cvib_1206
            PLT: Plut_0570
            RRS: RoseRS_1612 RoseRS_3360
            RCA: Rcas_3429 Rcas_4146
            DRA: DR_1026
            DGE: Dgeo_2410
            MBU: Mbur_1773
            MSE: Msed_0436 Msed_1118
            PIS: Pisl_1344 Pisl_1837
            PCL: Pcal_1218
            PAS: Pars_0490 Pars_2089
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.2.4
            ExPASy - ENZYME nomenclature database: 1.1.2.4
            ExplorEnz - The Enzyme Database: 1.1.2.4
            ERGO genome analysis and discovery system: 1.1.2.4
            BRENDA, the Enzyme Database: 1.1.2.4
            CAS: 37250-79-6
///
ENTRY       EC 1.1.2.5                  Enzyme
NAME        D-lactate dehydrogenase (cytochrome c-553)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With a cytochrome as acceptor
SYSNAME     (R)-lactate:ferricytochrome-c-553 2-oxidoreductase
REACTION    (R)-lactate + 2 ferricytochrome c-553 = pyruvate + 2 ferrocytochrome
            c-553 [RN:R00198]
ALL_REAC    R00198
SUBSTRATE   (R)-lactate [CPD:C00256];
            ferricytochrome c-553 [CPD:C01070]
PRODUCT     pyruvate [CPD:C00022];
            ferrocytochrome c-553 [CPD:C01071]
COMMENT     From Desulfovibrio vulgaris.
REFERENCE   1
  AUTHORS   Ogata, M., Arihara, K. and Yagi, T.
  TITLE     D-Lactate dehydrogenase of Desulfovibrio vulgaris.
  JOURNAL   J. Biochem. (Tokyo) 89 (1981) 1423-1431.
PATHWAY     PATH: map00620  Pyruvate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.2.5
            ExPASy - ENZYME nomenclature database: 1.1.2.5
            ExplorEnz - The Enzyme Database: 1.1.2.5
            ERGO genome analysis and discovery system: 1.1.2.5
            BRENDA, the Enzyme Database: 1.1.2.5
            CAS: 37250-79-6
///
ENTRY       EC 1.1.2.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With a cytochrome as acceptor
REACTION    (1) 2-Hydroxyethanesulfonate + 2 Ferricytochrome c <=>
            Sulfoacetaldehyde + 2 Ferrocytochrome c [RN:R06981];
            (2) (S)-Mandelate + FMN <=> alpha-Oxo-benzeneacetic acid + Reduced
            FMN [RN:R07664]
SUBSTRATE   2-Hydroxyethanesulfonate [CPD:C05123];
            Ferricytochrome c [CPD:C00125]
PRODUCT     Sulfoacetaldehyde [CPD:C00593];
            Ferrocytochrome c [CPD:C00126]
///
ENTRY       EC 1.1.3.1        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
COMMENT     Deleted entry: glycolate oxidase. Now included with EC 1.1.3.15
            (S)-2-hydroxy-acid oxidase (EC 1.1.3.1 created 1961, deleted 1984)
STRUCTURES  PDB: 1GOX  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.1
            ExPASy - ENZYME nomenclature database: 1.1.3.1
            ExplorEnz - The Enzyme Database: 1.1.3.1
            ERGO genome analysis and discovery system: 1.1.3.1
            BRENDA, the Enzyme Database: 1.1.3.1
///
ENTRY       EC 1.1.3.2        Obsolete  Enzyme
NAME        Transferred to 1.13.12.4
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now EC 1.13.12.4 lactate 2-monooxygenase (EC
            1.1.3.2 created 1961, deleted 1972)
STRUCTURES  PDB: 2J6X  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.2
            ExPASy - ENZYME nomenclature database: 1.1.3.2
            ExplorEnz - The Enzyme Database: 1.1.3.2
            ERGO genome analysis and discovery system: 1.1.3.2
            BRENDA, the Enzyme Database: 1.1.3.2
///
ENTRY       EC 1.1.3.3                  Enzyme
NAME        malate oxidase;
            FAD-dependent malate oxidase;
            malic oxidase;
            malic dehydrogenase II
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     (S)-malate:oxygen oxidoreductase
REACTION    (S)-malate + O2 = oxaloacetate + H2O2 [RN:R00360]
ALL_REAC    R00360
SUBSTRATE   (S)-malate [CPD:C00149];
            O2 [CPD:C00007]
PRODUCT     oxaloacetate [CPD:C00036];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:13563491]
  AUTHORS   COHN DV.
  TITLE     The enzymatic formation of oxalacetic acid by nonpyridine nucleotide
            malic dehydrogenase of Micrococcus lysodeikticus.
  JOURNAL   J. Biol. Chem. 233 (1958) 299-304.
  ORGANISM  Micrococcus lysodeikticus
REFERENCE   2  [PMID:368072]
  AUTHORS   Narindrasorasak S, Goldie AH, Sanwal BD.
  TITLE     Characteristics and regulation of a phospholipid-activated malate
            oxidase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 254 (1979) 1540-5.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00620  Pyruvate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.3
            ExPASy - ENZYME nomenclature database: 1.1.3.3
            ExplorEnz - The Enzyme Database: 1.1.3.3
            ERGO genome analysis and discovery system: 1.1.3.3
            BRENDA, the Enzyme Database: 1.1.3.3
            CAS: 9028-73-3
///
ENTRY       EC 1.1.3.4                  Enzyme
NAME        glucose oxidase;
            glucose oxyhydrase;
            corylophyline;
            penatin;
            glucose aerodehydrogenase;
            microcid;
            beta-D-glucose oxidase;
            D-glucose oxidase;
            D-glucose-1-oxidase;
            beta-D-glucose:quinone oxidoreductase;
            glucose oxyhydrase;
            deoxin-1;
            GOD
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     beta-D-glucose:oxygen 1-oxidoreductase
REACTION    beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2 [RN:R01522]
ALL_REAC    R01522
SUBSTRATE   beta-D-glucose [CPD:C00221];
            O2 [CPD:C00007]
PRODUCT     D-glucono-1,5-lactone [CPD:C00198];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1
  AUTHORS   Bentley, R.
  TITLE     Glucose oxidase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 567-586.
REFERENCE   2
  AUTHORS   Coulthard, C.E., Michaelis, R., Short, W.F., Sykes, G., Skrimshire,
            G.E.H., Standfast, A.F.B., Birkinshaw, J.H. and Raistick, H.
  TITLE     Notatin: an anti-bacterial glucose-aerodehydrogenase from
            Penicillium notatum Westling and Penicillium resticulosum sp. nov.
  JOURNAL   Biochem. J. 39 (1945) 24-36.
  ORGANISM  Penicillium notatum, Penicillium resticulosum, Aspergillus niger
REFERENCE   3
  AUTHORS   Keilin, D. and Hartree, E.F.
  TITLE     Properties of glucose oxidase (notatin).
  JOURNAL   Biochem. J. 42 (1948) 221-229.
  ORGANISM  Aspergillus niger, Penicillium glaucum
REFERENCE   4  [PMID:14915954]
  AUTHORS   KEILIN D, HARTREE EF.
  TITLE     Specificity of glucose oxidase (notatin).
  JOURNAL   Biochem. J. 50 (1952) 331-41.
  ORGANISM  Penicillium notatum
PATHWAY     PATH: map00030  Pentose phosphate pathway
GENES       ANG: An01g14740(goxC)
STRUCTURES  PDB: 1CF3  1GAL  1GPE  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.4
            ExPASy - ENZYME nomenclature database: 1.1.3.4
            ExplorEnz - The Enzyme Database: 1.1.3.4
            ERGO genome analysis and discovery system: 1.1.3.4
            BRENDA, the Enzyme Database: 1.1.3.4
            CAS: 9001-37-0
///
ENTRY       EC 1.1.3.5                  Enzyme
NAME        hexose oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     D-hexose:oxygen 1-oxidoreductase
REACTION    D-glucose + O2 = D-glucono-1,5-lactone + H2O2 [RN:R01522]
ALL_REAC    R01522
SUBSTRATE   D-glucose [CPD:C00031];
            O2 [CPD:C00007]
PRODUCT     D-glucono-1,5-lactone [CPD:C00198];
            H2O2 [CPD:C00027]
COFACTOR    Copper [CPD:C00070]
COMMENT     A copper glycoprotein. Also oxidizes D-galactose, D-mannose,
            maltose, lactose and cellobiose.
REFERENCE   1  [PMID:13278350]
  AUTHORS   BEAN RC, HASSID WZ.
  TITLE     Carbohydrate oxidase from A red alga, Iridophycus flaccidum.
  JOURNAL   J. Biol. Chem. 218 (1956) 425-36.
  ORGANISM  Iridophycus flaccidum
REFERENCE   2  [PMID:13688220]
  AUTHORS   BEAN RC, PORTER GG, STEINBERG BM.
  TITLE     Carbohydrate metabolism of citrus fruits. II. Oxidation of sugars by
            an aerodehydrogenase from young orange fruits.
  JOURNAL   J. Biol. Chem. 236 (1961) 1235-40.
  ORGANISM  Citrus sinensis [GN:ecsi]
REFERENCE   3  [PMID:4708670]
  AUTHORS   Sullivan JD Jr, Ikawa M.
  TITLE     Purification and characterization of hexose oxidase from the red
            alga Chondrus crispus.
  JOURNAL   Biochim. Biophys. Acta. 309 (1973) 11-22.
  ORGANISM  Chondrus crispus
PATHWAY     PATH: map00030  Pentose phosphate pathway
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.5
            ExPASy - ENZYME nomenclature database: 1.1.3.5
            ExplorEnz - The Enzyme Database: 1.1.3.5
            ERGO genome analysis and discovery system: 1.1.3.5
            BRENDA, the Enzyme Database: 1.1.3.5
            CAS: 9028-75-5
///
ENTRY       EC 1.1.3.6                  Enzyme
NAME        cholesterol oxidase;
            cholesterol- O2 oxidoreductase;
            3beta-hydroxy steroid oxidoreductase;
            3beta-hydroxysteroid:oxygen oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     cholesterol:oxygen oxidoreductase
REACTION    cholesterol + O2 = cholest-4-en-3-one + H2O2 [RN:R01459]
ALL_REAC    R01459
SUBSTRATE   cholesterol [CPD:C00187];
            O2 [CPD:C00007]
PRODUCT     cholest-4-en-3-one [CPD:C00599];
            H2O2 [CPD:C00027]
REFERENCE   1  [PMID:4757363]
  AUTHORS   Richmond W.
  TITLE     Preparation and properties of a cholesterol oxidase from Nocardia
            sp. and its application to the enzymatic assay of total cholesterol
            in serum.
  JOURNAL   Clin. Chem. 19 (1973) 1350-6.
  ORGANISM  Nocardia sp.
REFERENCE   2  [PMID:13143010]
  AUTHORS   STADTMAN TC, CHERKES A, ANFINSEN CB.
  TITLE     Studies on the microbiological degradation of cholesterol.
  JOURNAL   J. Biol. Chem. 206 (1954) 511-23.
  ORGANISM  Mycobacterium sp.
PATHWAY     PATH: map00120  Bile acid biosynthesis
ORTHOLOGY   KO: K03333  cholesterol oxidase
GENES       PIC: PICST_90828(FAO1)
            PRW: PsycPRwf_0069
            ABO: ABO_1259
            BBA: Bd0736(choA) Bd2646(choD)
            MTU: Rv3409c(choD)
            MBO: Mb3443c(choD)
            MBB: BCG_3479c(choD)
            CJK: jk0629(choE)
            RHA: RHA1_ro03863 RHA1_ro04305(choD) RHA1_ro06201(choD)
            FRA: Francci3_4446
            FAL: FRAAL6768(choA)
            SEN: SACE_6705(choD)
            STP: Strop_2611
            LIL: LA3998 LA3999(choB) LA4009(choA)
            LIC: LIC13194(choB) LIC13195
            SYD: Syncc9605_0826
STRUCTURES  PDB: 1B4V  1B8S  1CBO  1CC2  1COY  1I19  1IJH  1MXT  1N1P  1N4U  
                 1N4V  1N4W  2GEW  3COX  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.6
            ExPASy - ENZYME nomenclature database: 1.1.3.6
            ExplorEnz - The Enzyme Database: 1.1.3.6
            ERGO genome analysis and discovery system: 1.1.3.6
            BRENDA, the Enzyme Database: 1.1.3.6
            CAS: 9028-76-6
///
ENTRY       EC 1.1.3.7                  Enzyme
NAME        aryl-alcohol oxidase;
            aryl alcohol oxidase;
            veratryl alcohol oxidase;
            arom. alcohol oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     aryl-alcohol:oxygen oxidoreductase
REACTION    an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
            [RN:R01491]
ALL_REAC    R01491
SUBSTRATE   aromatic primary alcohol [CPD:C03485];
            O2 [CPD:C00007]
PRODUCT     aromatic aldehyde [CPD:C00193];
            H2O2 [CPD:C00027]
COMMENT     Oxidizes many primary alcohols containing an aromatic ring; best
            substrates are (2-naphthyl)methanol and 3-methoxybenzyl alcohol.
REFERENCE   1  [PMID:13821599]
  AUTHORS   FARMER VC, HENDERSON ME, RUSSELL JD.
  TITLE     Aromatic-alcohol-oxidase activity in the growth medium of
            Polystictus versicolor.
  JOURNAL   Biochem. J. 74 (1960) 257-62.
  ORGANISM  Polystictus versicolor
STRUCTURES  PDB: 1E8F  1E8H  1QLT  1QLU  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.7
            ExPASy - ENZYME nomenclature database: 1.1.3.7
            ExplorEnz - The Enzyme Database: 1.1.3.7
            ERGO genome analysis and discovery system: 1.1.3.7
            BRENDA, the Enzyme Database: 1.1.3.7
            CAS: 9028-77-7
///
ENTRY       EC 1.1.3.8                  Enzyme
NAME        L-gulonolactone oxidase;
            L-gulono-gamma-lactone: O2 oxidoreductase;
            L-gulono-gamma-lactone oxidase;
            L-gulono-gamma-lactone:oxidoreductase;
            GLO
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     L-gulono-1,4-lactone:oxygen 3-oxidoreductase
REACTION    (1) L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone +
            H2O2 [RN:R03184];
            (2) L-xylo-hex-2-ulono-1,4-lactone = L-ascorbate (spontaneous)
            [RN:R00647]
ALL_REAC    R00647 R03184
SUBSTRATE   L-gulono-1,4-lactone [CPD:C01040];
            O2 [CPD:C00007];
            L-xylo-hex-2-ulono-1,4-lactone
PRODUCT     L-xylo-hex-2-ulono-1,4-lactone;
            H2O2 [CPD:C00027];
            L-ascorbate [CPD:C00072]
COFACTOR    FAD [CPD:C00016]
COMMENT     A microsomal flavoprotein (FAD). The product spontaneously
            isomerizes to L-ascorbate. While most higher animals can synthesize
            asborbic acid, primates and guinea pigs cannot [3].
REFERENCE   1  [PMID:14405898]
  AUTHORS   ISHERWOOD FA, MAPSON LW, CHEN YT.
  TITLE     Synthesis of L-ascorbic acid in rat-liver homogenates. Conversion of
            L-gulono- and L-galactono-gamma-lactone and the respective acids
            into L-ascorbic acid.
  JOURNAL   Biochem. J. 76 (1960) 157-71.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:7138847]
  AUTHORS   Kiuchi K, Nishikimi M, Yagi K.
  TITLE     Purification and characterization of L-gulonolactone oxidase from
            chicken kidney microsomes.
  JOURNAL   Biochemistry. 21 (1982) 5076-82.
  ORGANISM  chicken [GN:gga]
REFERENCE   3  [PMID:8175804]
  AUTHORS   Nishikimi M, Fukuyama R, Minoshima S, Shimizu N, Yagi K.
  TITLE     Cloning and chromosomal mapping of the human nonfunctional gene for
            L-gulono-gamma-lactone oxidase, the enzyme for L-ascorbic acid
            biosynthesis missing in man.
  JOURNAL   J. Biol. Chem. 269 (1994) 13685-8.
REFERENCE   4
  AUTHORS   Chatterjee, I.B., Chatterjee, G.C., Ghosh, N.C. and Guha, B.C.
  TITLE     Identification of 2-keto-L-gulonolactone as an intermediate in the
            biosynthesis of L-ascorbic acid.
  JOURNAL   Naturwissenschaften 46 (1959) 475.
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K00103  L-gulonolactone oxidase
GENES       MMU: 268756(Gulo)
            RNO: 60671(Gulo)
            CFA: 486100(LOC486100)
            BTA: 286812(GULO)
            GGA: 770996(LOC770996)
            XLA: 495407(LOC495407)
            TET: TTHERM_00122050
            LPN: lpg2324
            BUR: Bcep18194_B2756 Bcep18194_B3008
            PLA: Plav_1740 Plav_2981
            SMD: Smed_0322
            BME: BMEII0438
            BMF: BAB2_0382
            GBE: GbCGDNIH1_2280
            BCY: Bcer98_0570
            OIH: OB1711
            CGB: cg0238
            FRA: Francci3_0346
            SEN: SACE_0063
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.8
            ExPASy - ENZYME nomenclature database: 1.1.3.8
            ExplorEnz - The Enzyme Database: 1.1.3.8
            ERGO genome analysis and discovery system: 1.1.3.8
            BRENDA, the Enzyme Database: 1.1.3.8
            CAS: 9028-78-8
///
ENTRY       EC 1.1.3.9                  Enzyme
NAME        galactose oxidase;
            D-galactose oxidase;
            beta-galactose oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     D-galactose:oxygen 6-oxidoreductase
REACTION    D-galactose + O2 = D-galacto-hexodialdose + H2O2 [RN:R01099]
ALL_REAC    R01099;
            (other) R01098
SUBSTRATE   D-galactose [CPD:C00124];
            O2 [CPD:C00007]
PRODUCT     D-galacto-hexodialdose [CPD:C03269];
            H2O2 [CPD:C00027]
COFACTOR    Copper [CPD:C00070]
COMMENT     A copper protein.
REFERENCE   1  [PMID:13863403]
  AUTHORS   AVIGAD G, AMARAL D, ASENSIO C, HORECKER BL.
  TITLE     The D-galactose oxidase of Polyporus circinatus.
  JOURNAL   J. Biol. Chem. 237 (1962) 2736-43.
  ORGANISM  Polyporus circinatus
PATHWAY     PATH: map00052  Galactose metabolism
GENES       AFM: AFUA_7G06820
            BPM: BURPS1710b_1758
            FAL: FRAAL1593
STRUCTURES  PDB: 1GOF  1GOG  1GOH  1K3I  1T2X  2EIB  2EIC  2EID  2EIE  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.9
            ExPASy - ENZYME nomenclature database: 1.1.3.9
            ExplorEnz - The Enzyme Database: 1.1.3.9
            ERGO genome analysis and discovery system: 1.1.3.9
            BRENDA, the Enzyme Database: 1.1.3.9
            CAS: 9028-79-9
///
ENTRY       EC 1.1.3.10                 Enzyme
NAME        pyranose oxidase;
            glucose 2-oxidase;
            pyranose-2-oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     pyranose:oxygen 2-oxidoreductase
REACTION    D-glucose + O2 = 2-dehydro-D-glucose + H2O2 [RN:R00302]
ALL_REAC    R00302
SUBSTRATE   D-glucose [CPD:C00031];
            O2 [CPD:C00007]
PRODUCT     2-dehydro-D-glucose [CPD:C02779];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Also oxidizes D-xylose, L-sorbose and
            D-glucono-1,5-lactone, which have the same ring conformation and
            configuration at C-2, C-3 and C-4.
REFERENCE   1  [PMID:5722278]
  AUTHORS   Janssen FW, Ruelius HW.
  TITLE     Carbohydrate oxidase, a novel enzyme from Polyporus obtusus. II.
            Specificity and characterization of reaction products.
  JOURNAL   Biochim. Biophys. Acta. 167 (1968) 501-10.
  ORGANISM  Polyporus obtusu
REFERENCE   2
  AUTHORS   Machida, Y. and Nakanishi, T.
  TITLE     Purification and properties of pyranose oxidase from Coriolus
            versicolor.
  JOURNAL   Agric. Biol. Chem. 48 (1984) 2463-2470.
  ORGANISM  Coriolus versicolor
REFERENCE   3
  AUTHORS   Neidleman, S.L., Amon, W.F., Jr. and Geigert, J.
  TITLE     Process for the production of fructose.
  JOURNAL   Chem. Abstr. 94 (1981) 20737.
REFERENCE   4  [PMID:5725162]
  AUTHORS   Ruelius HW, Kerwin RM, Janssen FW.
  TITLE     Carbohydrate oxidase, a novel enzyme from Polyporus obtusus. I.
            Isolation and purification.
  JOURNAL   Biochim. Biophys. Acta. 167 (1968) 493-500.
  ORGANISM  Coriolus versicolor
PATHWAY     PATH: map00030  Pentose phosphate pathway
GENES       FAL: FRAAL4641
STRUCTURES  PDB: 1TT0  1TZL  2F5V  2F6C  2IGK  2IGM  2IGN  2IGO  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.10
            ExPASy - ENZYME nomenclature database: 1.1.3.10
            ExplorEnz - The Enzyme Database: 1.1.3.10
            ERGO genome analysis and discovery system: 1.1.3.10
            BRENDA, the Enzyme Database: 1.1.3.10
            CAS: 37250-80-9
///
ENTRY       EC 1.1.3.11                 Enzyme
NAME        L-sorbose oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     L-sorbose:oxygen 5-oxidoreductase
REACTION    L-sorbose + O2 = 5-dehydro-D-fructose + H2O2 [RN:R01695]
ALL_REAC    R01695
SUBSTRATE   L-sorbose [CPD:C00247];
            O2 [CPD:C00007]
PRODUCT     5-dehydro-D-fructose [CPD:C00273];
            H2O2 [CPD:C00027]
COMMENT     Also acts on D-glucose, D-galactose and D-xylose, but not on
            D-fructose. 2,6-Dichloroindophenol can act as acceptor.
REFERENCE   1  [PMID:5586487]
  AUTHORS   Yamada Y, Lizuka K, Aida K, Uemura T.
  TITLE     Enzymatic studies on the oxidation of sugar and sugar alcohol. 3.
            Purification and properties of L-sorbose oxidase from Trametes
            sanguinea.
  JOURNAL   J. Biochem. (Tokyo). 62 (1967) 223-9.
  ORGANISM  Trametes sanguinea
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.11
            ExPASy - ENZYME nomenclature database: 1.1.3.11
            ExplorEnz - The Enzyme Database: 1.1.3.11
            ERGO genome analysis and discovery system: 1.1.3.11
            BRENDA, the Enzyme Database: 1.1.3.11
            CAS: 37250-81-0
///
ENTRY       EC 1.1.3.12                 Enzyme
NAME        pyridoxine 4-oxidase;
            pyridoxin 4-oxidase;
            pyridoxol 4-oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     pyridoxine:oxygen 4-oxidoreductase
REACTION    pyridoxine + O2 = pyridoxal + H2O2 [RN:R01711]
ALL_REAC    R01711
SUBSTRATE   pyridoxine [CPD:C00314];
            O2 [CPD:C00007]
PRODUCT     pyridoxal [CPD:C00250];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein. Can also use 2,6-dichloroindophenol as an acceptor.
REFERENCE   1  [PMID:5769992]
  AUTHORS   Sundaram TK, Snell EE.
  TITLE     The bacterial oxidation of vitamin B6. V. The enzymatic formation of
            pyridoxal and isopyridoxal from pyridoxine.
  JOURNAL   J. Biol. Chem. 244 (1969) 2577-84.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00750  Vitamin B6 metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.12
            ExPASy - ENZYME nomenclature database: 1.1.3.12
            ExplorEnz - The Enzyme Database: 1.1.3.12
            ERGO genome analysis and discovery system: 1.1.3.12
            BRENDA, the Enzyme Database: 1.1.3.12
            CAS: 37250-82-1
///
ENTRY       EC 1.1.3.13                 Enzyme
NAME        alcohol oxidase;
            ethanol oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     alcohol:oxygen oxidoreductase
REACTION    a primary alcohol + O2 = an aldehyde + H2O2 [RN:R00637]
ALL_REAC    R00637 > R00608
SUBSTRATE   primary alcohol [CPD:C00226];
            O2 [CPD:C00007]
PRODUCT     aldehyde [CPD:C00071];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD); acts on lower primary alcohols and unsaturated
            alcohols but branched-chain and secondary alcohols are not attacked.
REFERENCE   1  [PMID:5636370]
  AUTHORS   Janssen FW, Ruelius HW.
  TITLE     Alcohol oxidase, a flavoprotein from several Basidiomycetes species.
            Crystallization by fractional precipitation with polyethylene
            glycol.
  JOURNAL   Biochim. Biophys. Acta. 151 (1968) 330-42.
  ORGANISM  Basidiomycetes sp.
REFERENCE   2
  AUTHORS   Nishida, A., Ishihara, T. and Hiroi, T.
  TITLE     Studies on enzymes related to lignan biodegradation.
  JOURNAL   Baiomasu Henkan Keikaku Kenkyu Hokoku (1987) 38-59.
REFERENCE   3  [PMID:9142745]
  AUTHORS   Suye S.
  TITLE     Purification and properties of alcohol oxidase from Candida
            methanosorbosa M-2003.
  JOURNAL   Curr. Microbiol. 34 (1997) 374-7.
  ORGANISM  Candida methanosorbosa
PATHWAY     PATH: map00680  Methane metabolism
STRUCTURES  PDB: 1AHU  1AHV  1AHZ  1VAO  1W1J  1W1K  1W1L  1W1M  2VAO  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.13
            ExPASy - ENZYME nomenclature database: 1.1.3.13
            ExplorEnz - The Enzyme Database: 1.1.3.13
            ERGO genome analysis and discovery system: 1.1.3.13
            BRENDA, the Enzyme Database: 1.1.3.13
            CAS: 9073-63-6
///
ENTRY       EC 1.1.3.14                 Enzyme
NAME        catechol oxidase (dimerizing)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     catechol:oxygen oxidoreductase (dimerizing)
REACTION    4 catechol + 3 O2 = 2 dibenzo[1,4]dioxin-2,3-dione + 6 H2O
            [RN:R00080]
ALL_REAC    R00080
SUBSTRATE   catechol [CPD:C00090];
            O2 [CPD:C00007]
PRODUCT     dibenzo[1,4]dioxin-2,3-dione [CPD:C03861];
            H2O [CPD:C00001]
REFERENCE   1
  AUTHORS   Nair, P.M. and Vining, L.C.
  TITLE     Enzymic oxidation of catechol to diphenylenedioxide-2,3-quinone.
  JOURNAL   Arch. Biochem. Biophys. 106 (1964) 422-427.
  ORGANISM  spinach
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.14
            ExPASy - ENZYME nomenclature database: 1.1.3.14
            ExplorEnz - The Enzyme Database: 1.1.3.14
            ERGO genome analysis and discovery system: 1.1.3.14
            BRENDA, the Enzyme Database: 1.1.3.14
            CAS: 37250-83-2
///
ENTRY       EC 1.1.3.15                 Enzyme
NAME        (S)-2-hydroxy-acid oxidase;
            glycolate oxidase;
            hydroxy-acid oxidase A;
            hydroxy-acid oxidase B;
            glycolate oxidase;
            oxidase, L-2-hydroxy acid;
            hydroxyacid oxidase A;
            L-alpha-hydroxy acid oxidase;
            L-2-hydroxy acid oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     (S)-2-hydroxy-acid:oxygen 2-oxidoreductase
REACTION    (S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2 [RN:R01341]
ALL_REAC    R01341 > R00475
SUBSTRATE   (S)-2-hydroxy acid [CPD:C02613];
            O2 [CPD:C00007]
PRODUCT     2-oxo acid [CPD:C00161];
            H2O2 [CPD:C00027]
COFACTOR    FMN [CPD:C00061]
COMMENT     A flavoprotein (FMN). Exists as two major isoenzymes; the A form
            preferentially oxidizes short-chain aliphatic hydroxy acids, and was
            previously listed as EC 1.1.3.1, glycolate oxidase; the B form
            preferentially oxidizes long-chain and aromatic hydroxy acids. The
            rat isoenzyme B also acts as EC 1.4.3.2, L-amino-acid oxidase.
REFERENCE   1
  AUTHORS   Blanchard, M., Green, D.E., Nocito-Carroll, V. and Ratner, S.
  TITLE     l-Hydroxy acid oxidase.
  JOURNAL   J. Biol. Chem. 163 (1946) 137-144.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:13538955]
  AUTHORS   FRIGERIO NA, HARBURY HA.
  TITLE     Preparation and some properties of crystalline glycolic acid oxidase
            of spinach.
  JOURNAL   J. Biol. Chem. 231 (1958) 135-57.
  ORGANISM  spinach
REFERENCE   3  [PMID:13201588]
  AUTHORS   KUN E, DECHARY JM, PITOT HC.
  TITLE     The oxidation of glycolic acid by a liver enzyme.
  JOURNAL   J. Biol. Chem. 210 (1954) 269-80.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:5946631]
  AUTHORS   Nakano M, Danowski TS.
  TITLE     Crystalline mammalian L-amino acid oxidase from rat kidney
            mitochondria.
  JOURNAL   J. Biol. Chem. 241 (1966) 2075-83.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:5686300]
  AUTHORS   Nakano M, Ushijima Y, Saga M, Tsutsumi Y, Asami H.
  TITLE     Aliphatic L-alpha-hydroxyacid oxidase from rat livers: purification
            and properties.
  JOURNAL   Biochim. Biophys. Acta. 167 (1968) 9-22.
  ORGANISM  rat [GN:rno]
REFERENCE   6  [PMID:1268224]
  AUTHORS   Phillips DR, Duley JA, Fennell DJ, Holmes RS.
  TITLE     The self-association of L-alpha hydroxyacid oxidase.
  JOURNAL   Biochim. Biophys. Acta. 427 (1976) 679-87.
  ORGANISM  rat [GN:rno]
REFERENCE   7  [PMID:5569122]
  AUTHORS   Schuman M, Massey V.
  TITLE     Purification and characterization of glycolic acid oxidase from pig
            liver.
  JOURNAL   Biochim. Biophys. Acta. 227 (1971) 500-20.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K00104  (S)-2-hydroxy-acid oxidase
GENES       HSA: 51179(HAO2) 54363(HAO1)
            MMU: 15112(Hao1) 56185(Hao3)
            RNO: 84029(Hao2)
            CFA: 475814(HAO2) 485774(HAO1)
            GGA: 416728(HAO1)
            DRE: 393455(zgc:63690)
            SPU: 594782(LOC594782)
            CEL: F41E6.5
            ATH: AT3G14415 AT4G18360
            OSA: 4334349 4337048 4342420
            CME: CMQ436C
            CNE: CND02080
            DDI: DDBDRAFT_0184082
            TET: TTHERM_00290670
            ECJ: JW2946(glcD)
            ECC: c3709(glcD)
            ECI: UTI89_C3394(glcD)
            ECP: ECP_3057
            ECV: APECO1_3448(glcD)
            PAE: PA5355(glcD)
            PAU: PA14_70690(glcD)
            PPU: PP_3745(glcD)
            PST: PSPTO_3555(glcD)
            PSB: Psyr_3331(glcD)
            PSP: PSPPH_3252(glcD)
            PFL: PFL_2269(glcD)
            PFO: Pfl_2219(glcD)
            PEN: PSEEN3186(glcD)
            PAR: Psyc_1650(glcD)
            PAT: Patl_2274
            MCA: MCA1501(glcD)
            NOC: Noc_0495 Noc_0844
            HCH: HCH_01681 HCH_05806
            CSA: Csal_1075 Csal_2687
            VOK: COSY_0294(glcD) COSY_0296(glcF)
            CVI: CV_4235
            RSO: RSc2666(glcD) RSc2667(glcE) RSc2668(glcF)
            REU: Reut_A2790 Reut_B3845
            REH: H16_A1307(glcD2) H16_A1387(glcD3) H16_A3094(glcD1)
                 H16_A3096(glcE) H16_A3097(glcF)
            RME: Rmet_0839 Rmet_2926 Rmet_2928 Rmet_2929
            BMA: BMA2412(glcF) BMA2413(glcE) BMA2414(glcD)
            BXE: Bxe_A2219 Bxe_A2781 Bxe_A3978 Bxe_A3979 Bxe_A3980
            BUR: Bcep18194_A3818
            BCN: Bcen_3333
            BCH: Bcen2424_5034
            BPS: BPSL2843(glcD) BPSL2844(glcE) BPSL2845(glcF)
            BPM: BURPS1710b_2738 BURPS1710b_3342(glcD) BURPS1710b_3343(glcE)
                 BURPS1710b_3345(glcF)
            BPL: BURPS1106A_3332(glcF) BURPS1106A_A1566(glcF)
                 BURPS1106A_A1567(glcE)
            BPD: BURPS668_3298(glcF) BURPS668_A1647(glcF) BURPS668_A1648(glcE)
            BTE: BTH_I1290(glcE) BTH_I1291(glcD)
            BPE: BP2905(glcD)
            BPA: BPP2491(glcD)
            BBR: BB1938(glcD)
            RFR: Rfer_0480 Rfer_0481 Rfer_0606
            POL: Bpro_0187 Bpro_0188 Bpro_0433 Bpro_3049
            AJS: Ajs_0513 Ajs_3298
            MPT: Mpe_A0959 Mpe_A0960 Mpe_A0961 Mpe_A3638 Mpe_A3639 Mpe_A3640
            MMS: mma_0335(glcD1) mma_0336(glcE) mma_0337(glcF) mma_3114
            NEU: NE0674(glcE) NE0675(glcD) NE0741 NE2126 NE2237
            NET: Neut_1882 Neut_1883
            NMU: Nmul_A0173 Nmul_A0174
            EBA: ebA310 ebA4490(glcD) ebA4491(glcE) ebA5380
            AZO: azo0609(gox)
            DAR: Daro_3314 Daro_3315
            TBD: Tbd_0046 Tbd_0047(glcD)
            HPY: HP0509(glcD)
            HPJ: jhp0459(glcD)
            HPA: HPAG1_0137 HPAG1_0483
            HHE: HH0869(glcD)
            HAC: Hac_0898(glcD)
            WSU: WS0267(glcD)
            TDN: Tmden_0372
            CJE: Cj1213c(glcD)
            CJR: CJE1347(glcD)
            CJU: C8J_1156(glcD)
            ABU: Abu_1840(glcD)
            NIS: NIS_0341(glcD)
            SUN: SUN_2130(glcD)
            GSU: GSU1623 GSU3296
            GME: Gmet_3245
            PCA: Pcar_2765
            DVU: DVU0827 DVU3027(glcD)
            DDE: Dde_1087 Dde_3239(glcD)
            DPS: DP0059(glcD) DP1022(glcD)
            MXA: MXAN_2956
            SAT: SYN_00316 SYN_01167
            SFU: Sfum_0392 Sfum_0534
            PUB: SAR11_0276(glcF) SAR11_0277(glcE) SAR11_0278(glcD)
            MLO: mll4732 mlr6916(glcD)
            MES: Meso_0364
            SME: SMc00832(glcD)
            ATU: Atu0665(glcD)
            ATC: AGR_C_1189(glcD)
            RET: RHE_CH00808(glcD) RHE_CH00809(glcE) RHE_CH00810(glcF)
            RLE: RL0864(glcD) RL0865(glcE) RL0866(glcF)
            BME: BMEII1061 BMEII1062 BMEII1064
            BMF: BAB2_0174
            BMS: BRA0180(glcD)
            BMB: BruAb2_0175(glcD)
            BJA: bll7543(glcD)
            BRA: BRADO4114 BRADO6122(glcF) BRADO6123(glcE) BRADO6131(glcD)
            BBT: BBta_1662(glcD) BBta_1663(glcE) BBta_1664(glcF) BBta_4489
            RPA: RPA1130(glcD)
            RPB: RPB_1827
            RPC: RPC_4736
            RPE: RPE_4692 RPE_4693 RPE_4694
            NWI: Nwi_0702 Nwi_2581
            SIL: SPO3478(glcD)
            RSP: RSP_1020(glcD)
            RDE: RD1_0625(glcD) RD1_0626(glcE) RD1_0627(glcF)
            PDE: Pden_5045
            MMR: Mmar10_2117
            HNE: HNE_2118
            SAL: Sala_1846
            GBE: GbCGDNIH1_0886 GbCGDNIH1_1229 GbCGDNIH1_1230
            RRU: Rru_A0777
            BSU: BG12320(ysfC)
            BHA: BH2134 BH2730
            BAN: BA1309(glcD)
            BAR: GBAA1309(glcD)
            BAA: BA_1835
            BAT: BAS1210(glcD)
            BCE: BC1296 BC1297
            BCA: BCE_1410(glcD)
            BCZ: BCZK1189(glcF) BCZK1190(glcD) BCZK1196 BCZK2958
            BTK: BT9727_1188(glcD)
            BTL: BALH_1158(glcF) BALH_1159(glcD)
            BLI: BL01799
            BLD: BLi00330(ysfC)
            BCL: ABC1223(glcD) ABC2175 ABC2176 ABC2177 ABC3247 ABC3248 ABC4036
                 ABC4037
            BPU: BPUM_1672(yvfV) BPUM_1792(glcD) BPUM_1793(glcF)
            OIH: OB2831
            GKA: GK1530 GK1531 GK1532 GK2014
            STH: STH993
            CAC: CAC2542
            CPE: CPE0313
            CPF: CPF_0310
            CPR: CPR_0305
            CTC: CTC00976
            CHY: CHY_0432 CHY_1297(glcD)
            DSY: DSY3357
            TTE: TTE0224(glcD)
            MTA: Moth_2308
            MTU: Rv1257c
            MTC: MT1296
            MLE: ML1103
            MPA: MAP2517
            MVA: Mvan_1297
            MGI: Mflv_5059
            MMC: Mmcs_1002
            MKM: Mkms_1019
            MJL: Mjls_1029
            CGB: cg2543(glcD)
            NFA: nfa10070
            RHA: RHA1_ro01589 RHA1_ro06073
            SCO: SCO2925(SCE19A.25c) SCO3228(SCE63.05)
            SMA: SAV1386(glcD1) SAV5151(glcD2)
            LXX: Lxx08950
            NCA: Noca_0280
            TFU: Tfu_2980
            FRA: Francci3_2414 Francci3_2463
            FAL: FRAAL3579 FRAAL5480
            SEN: SACE_3870(glcD2) SACE_4261(glcD) SACE_6366(glcD)
            RXY: Rxyl_3151
            FNU: FN1536
            RBA: RB12039(glcD)
            SYN: sll0404(glcD)
            SYW: SYNW0161(glcE) SYNW1808
            SYC: syc1237_d(glcD)
            SYF: Synpcc7942_0276
            SYD: Syncc9605_0660
            SYE: Syncc9902_1700
            SYG: sync_0210 sync_0213 sync_2057
            SYR: SynRCC307_0146(glcE) SynRCC307_1647(glcD)
            SYX: SynWH7803_0214(glcE) SynWH7803_1820(glcD)
            TEL: tll1625(glcD)
            GVI: glr3069(glcD)
            ANA: all0170 alr5269(glcD)
            AVA: Ava_1430
            PMT: PMT1295(glcD) PMT1939(glcE)
            PMN: PMN2A_1172
            PMF: P9303_06971 P9303_25781 P9303_25811(glcE)
            FPS: FP0574(glcD)
            DRA: DR_1031 DR_1731(glcD)
            DGE: Dgeo_0624 Dgeo_2057
            TTH: TTC0127(glcF) TTC0128(glcE) TTC0129 TTC0443 TTC1966
            TTJ: TTHA0505
            MAC: MA4631
            MBA: Mbar_A0951
            MMA: MM_1291
            TAC: Ta0542
            TVO: TVN0596
            PTO: PTO0146 PTO0147 PTO1045
            RCI: RCIX1754(glcD-1) RCIX2225(glcD-2)
            APE: APE_0487
            SSO: SSO3163(glcD)
            STO: ST0649(glcD) ST2295
            SAI: Saci_0206(glcD) Saci_0299(dld)
            PAI: PAE1286(glcD)
STRUCTURES  PDB: 1AL7  1AL8  1GYL  1TB3  2NZL  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.15
            ExPASy - ENZYME nomenclature database: 1.1.3.15
            ExplorEnz - The Enzyme Database: 1.1.3.15
            ERGO genome analysis and discovery system: 1.1.3.15
            BRENDA, the Enzyme Database: 1.1.3.15
            CAS: 9037-63-2
///
ENTRY       EC 1.1.3.16                 Enzyme
NAME        ecdysone oxidase;
            beta-ecdysone oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     ecdysone:oxygen 3-oxidoreductase
REACTION    ecdysone + O2 = 3-dehydroecdysone + H2O2 [RN:R02373]
ALL_REAC    R02373
SUBSTRATE   ecdysone [CPD:C00477];
            O2 [CPD:C00007]
PRODUCT     3-dehydroecdysone [CPD:C02513];
            H2O2 [CPD:C00027]
COMMENT     2,6-Dichloroindophenol can act as an acceptor.
REFERENCE   1  [PMID:297]
  AUTHORS   Koolman J, Karlson P.
  TITLE     Ecdysone Oxidase, an enzyme from the blowfly Calliphora
            erythrocephala (Meigen).
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 356 (1975) 1131-8.
  ORGANISM  Calliphora erythrocephala
GENES       DME: Dmel_CG9504(Eo)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.16
            ExPASy - ENZYME nomenclature database: 1.1.3.16
            ExplorEnz - The Enzyme Database: 1.1.3.16
            ERGO genome analysis and discovery system: 1.1.3.16
            BRENDA, the Enzyme Database: 1.1.3.16
            CAS: 56803-12-4
///
ENTRY       EC 1.1.3.17                 Enzyme
NAME        choline oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     choline:oxygen 1-oxidoreductase
REACTION    choline + O2 = betaine aldehyde + H2O2 [RN:R01022]
ALL_REAC    R01022;
            (other) R00040
SUBSTRATE   choline [CPD:C00114];
            O2 [CPD:C00007]
PRODUCT     betaine aldehyde [CPD:C00576];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Also oxidizes betaine aldehyde to betaine. In
            many bacteria, plants and animals, betaine is synthesized in two
            steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to
            betaine. Different enzymes are involved in the first reaction. In
            plants, this reaction is catalysed by EC 1.14.15.7, choline
            monooxygenase, whereas in animals and many bacteria, it is catalysed
            by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or
            soluble choline oxidase (EC 1.1.3.17) [6]. The enzyme involved in
            the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears
            to be the same in plants, animals and bacteria. In some bacteria,
            betaine is synthesized from glycine through the actions of EC
            2.1.1.156, glycine/sarcosine N-methyltransferase and EC 2.1.1.157,
            sarcosine/dimethylglycine N-methyltransferase.
REFERENCE   1  [PMID:599154]
  AUTHORS   Ikuta S, Imamura S, Misaki H, Horiuti Y.
  TITLE     Purification and characterization of choline oxidase from
            Arthrobacter globiformis.
  JOURNAL   J. Biochem. (Tokyo). 82 (1977) 1741-9.
  ORGANISM  Arthrobacter globiformis
REFERENCE   2  [PMID:1987142]
  AUTHORS   Rozwadowski KL, Khachatourians GG, Selvaraj G.
  TITLE     Choline oxidase, a catabolic enzyme in Arthrobacter pascens,
            facilitates adaptation to osmotic stress in Escherichia coli.
  JOURNAL   J. Bacteriol. 173 (1991) 472-8.
  ORGANISM  Arthrobacter pascens
REFERENCE   3  [PMID:12795615]
  AUTHORS   Rand T, Halkier T, Hansen OC.
  TITLE     Structural characterization and mapping of the covalently linked FAD
            cofactor in choline oxidase from Arthrobacter globiformis.
  JOURNAL   Biochemistry. 42 (2003) 7188-94.
  ORGANISM  Arthrobacter globiformis
REFERENCE   4  [PMID:15369826]
  AUTHORS   Gadda G, Powell NL, Menon P.
  TITLE     The trimethylammonium headgroup of choline is a major determinant
            for substrate binding and specificity in choline oxidase.
  JOURNAL   Arch. Biochem. Biophys. 430 (2004) 264-73.
  ORGANISM  Arthrobacter globiformis
REFERENCE   5  [PMID:15713082]
  AUTHORS   Fan F, Gadda G.
  TITLE     On the catalytic mechanism of choline oxidase.
  JOURNAL   J. Am. Chem. Soc. 127 (2005) 2067-74.
  ORGANISM  Arthrobacter globiformis
REFERENCE   6  [PMID:12466265]
  AUTHORS   Waditee R, Tanaka Y, Aoki K, Hibino T, Jikuya H, Takano J, Takabe T,
            Takabe T.
  TITLE     Isolation and functional characterization of N-methyltransferases
            that catalyze betaine synthesis from glycine in a halotolerant
            photosynthetic organism Aphanothece halophytica.
  JOURNAL   J. Biol. Chem. 278 (2003) 4932-42.
  ORGANISM  Aphanothece halophytica
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
GENES       AFM: AFUA_8G04090
            AAU: AAur_0512
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.17
            ExPASy - ENZYME nomenclature database: 1.1.3.17
            ExplorEnz - The Enzyme Database: 1.1.3.17
            ERGO genome analysis and discovery system: 1.1.3.17
            BRENDA, the Enzyme Database: 1.1.3.17
            CAS: 9028-67-5
///
ENTRY       EC 1.1.3.18                 Enzyme
NAME        secondary-alcohol oxidase;
            polyvinyl alcohol oxidase;
            secondary alcohol oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     secondary-alcohol:oxygen oxidoreductase
REACTION    a secondary alcohol + O2 = a ketone + H2O2 [RN:R02277]
ALL_REAC    R02277
SUBSTRATE   secondary alcohol [CPD:C00432];
            O2 [CPD:C00007]
PRODUCT     ketone [CPD:C00709];
            H2O2 [CPD:C00027]
COMMENT     Acts on secondary alcohols with five or more carbons, and polyvinyl
            alcohols with molecular mass over 300 Da. The Pseudomonas enzyme
            contains one atom of non-heme iron per molecule.
REFERENCE   1
  AUTHORS   Morita, M., Hamada, N., Sakai, K. and Watanabe, Y.
  TITLE     Purification and properties of secondary alcohol oxidase from a
            strain of Pseudomonas.
  JOURNAL   Agric. Biol. Chem. 43 (1979) 1225-1235.
  ORGANISM  Pseudomonas sp.
REFERENCE   2
  AUTHORS   Sakai, K., Hamada, N. and Watanabe, Y.
  TITLE     Separation of secondary alcohol oxidase and oxidized poly(vinyl
            alcohol) hydrolase by hydrophobic and dye-ligand chromatographies.
  JOURNAL   Agric. Biol. Chem. 47 (1983) 153-155.
REFERENCE   3
  AUTHORS   Suzuki, T.
  TITLE     Purification and some properties of polyvinyl alcohol-degrading
            enzyme produced by Pseudomonas O-3.
  JOURNAL   Agric. Biol. Chem. 40 (1976) 497-504.
  ORGANISM  Pseudomonas sp.
REFERENCE   4
  AUTHORS   Suzuki, T.
  TITLE     Oxidation of secondary alcohols by polyvinyl alcohol-degrading
            enzyme produced by Pseudomonas O-3.
  JOURNAL   Agric. Biol. Chem. 42 (1977) 1187-1194.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.18
            ExPASy - ENZYME nomenclature database: 1.1.3.18
            ExplorEnz - The Enzyme Database: 1.1.3.18
            ERGO genome analysis and discovery system: 1.1.3.18
            BRENDA, the Enzyme Database: 1.1.3.18
            CAS: 71245-08-4
///
ENTRY       EC 1.1.3.19                 Enzyme
NAME        4-hydroxymandelate oxidase;
            L-4-hydroxymandelate oxidase (decarboxylating)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate:oxygen 1-oxidoreductase
REACTION    (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O2 =
            4-hydroxybenzaldehyde + CO2 + H2O2 [RN:R02673]
ALL_REAC    R02673
SUBSTRATE   (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate [CPD:C03198];
            O2 [CPD:C00007]
PRODUCT     4-hydroxybenzaldehyde [CPD:C00633];
            CO2 [CPD:C00011];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016];
            Manganese [CPD:C00034]
COMMENT     A flavoprotein (FAD); requires Mn2+.
REFERENCE   1  [PMID:976259]
  AUTHORS   Bhat SG, Vaidyanathan CS.
  TITLE     Purification and properties of L-4-hydroxymandelate oxidase from
            Pseudomonas convexa.
  JOURNAL   Eur. J. Biochem. 68 (1976) 323-31.
  ORGANISM  Pseudomonas convexa
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.19
            ExPASy - ENZYME nomenclature database: 1.1.3.19
            ExplorEnz - The Enzyme Database: 1.1.3.19
            ERGO genome analysis and discovery system: 1.1.3.19
            BRENDA, the Enzyme Database: 1.1.3.19
            CAS: 60976-30-9
///
ENTRY       EC 1.1.3.20                 Enzyme
NAME        long-chain-alcohol oxidase;
            long-chain fatty alcohol oxidase;
            fatty alcohol oxidase;
            fatty alcohol:oxygen oxidoreductase;
            long-chain fatty acid oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     long-chain-alcohol:oxygen oxidoreductase
REACTION    2 long-chain alcohol + O2 = 2 long-chain aldehyde + 2 H2O
            [RN:R00041]
ALL_REAC    R00041
SUBSTRATE   long-chain alcohol [CPD:C00339];
            O2 [CPD:C00007]
PRODUCT     long-chain aldehyde [CPD:C00609];
            H2O [CPD:C00001]
COMMENT     Oxidizes long-chain fatty alcohols; best substrate is dodecyl
            alcohol.
REFERENCE   1  [PMID:36040]
  AUTHORS   Moreau RA, Huang AH.
  TITLE     Oxidation of fatty alcohol in the cotyledons of jojoba seedlings.
  JOURNAL   Arch. Biochem. Biophys. 194 (1979) 422-30.
  ORGANISM  Simmondsia chinensis
REFERENCE   2
  AUTHORS   Moreau, R.A. and Huang, A.H.C.
  TITLE     Enzymes of wax ester catabolism in jojoba.
  JOURNAL   Methods Enzymol. 71 (1981) 804-813.
  ORGANISM  Simmondsia chinensis
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.20
            ExPASy - ENZYME nomenclature database: 1.1.3.20
            ExplorEnz - The Enzyme Database: 1.1.3.20
            ERGO genome analysis and discovery system: 1.1.3.20
            BRENDA, the Enzyme Database: 1.1.3.20
            CAS: 129430-50-8
///
ENTRY       EC 1.1.3.21                 Enzyme
NAME        glycerol-3-phosphate oxidase;
            glycerol phosphate oxidase;
            glycerol-1-phosphate oxidase;
            glycerol phosphate oxidase;
            L-alpha-glycerophosphate oxidase;
            alpha-glycerophosphate oxidase;
            L-alpha-glycerol-3-phosphate oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     sn-glycerol-3-phosphate:oxygen 2-oxidoreductase
REACTION    sn-glycerol 3-phosphate + O2 = glycerone phosphate + H2O2
            [RN:R00846]
ALL_REAC    R00846
SUBSTRATE   sn-glycerol 3-phosphate [CPD:C00093];
            O2 [CPD:C00007]
PRODUCT     glycerone phosphate [CPD:C00111];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:5667352]
  AUTHORS   Gancedo C, Gancedo JM, Sols A.
  TITLE     Glycerol metabolism in yeasts. Pathways of utilization and
            production.
  JOURNAL   Eur. J. Biochem. 5 (1968) 165-72.
  ORGANISM  Candida utilis, Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:5788698]
  AUTHORS   Koditschek LK, Umbreit WW.
  TITLE     Alpha-glycerophosphate oxidase in Streptococcus faecium F 24.
  JOURNAL   J. Bacteriol. 98 (1969) 1063-8.
  ORGANISM  Streptococcus faecium
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00105  alpha-glycerophosphate oxidase
GENES       PHA: PSHAb0547(glpD)
            PAT: Patl_3682
            NOC: Noc_2699
            BUR: Bcep18194_A6005 Bcep18194_B2081
            HAR: HEAR3388(glpD)
            LLA: L0013(glpD)
            SPY: SPy_1683(glpO)
            SPM: spyM18_1695(glpA)
            SPG: SpyM3_1467(glpO)
            SPS: SPs0399
            SPH: MGAS10270_Spy1498(glpO)
            SPI: MGAS10750_Spy1491(glpO)
            SPJ: MGAS2096_Spy1403(glpO)
            SPK: MGAS9429_Spy1378(glpO)
            SPF: SpyM50410(glpO)
            SPA: M6_Spy1428
            SPN: SP_2185
            SPR: spr1989 spr1990
            SPD: SPD_2012(glpO)
            SAG: SAG0274
            SAN: gbs0264(glpD)
            SAK: SAK_0346(glpO)
            SSA: SSA_1827(glp)
            SGO: SGO_0631
            LPL: lp_0371(glpD)
            LSL: LSL_0111(glpO)
            EFA: EF1928
            MMY: MSC_0259(glpO)
            FAL: FRAAL1569
            SYD: Syncc9605_0499
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.21
            ExPASy - ENZYME nomenclature database: 1.1.3.21
            ExplorEnz - The Enzyme Database: 1.1.3.21
            ERGO genome analysis and discovery system: 1.1.3.21
            BRENDA, the Enzyme Database: 1.1.3.21
            CAS: 9046-28-0
///
ENTRY       EC 1.1.3.22       Obsolete  Enzyme
NAME        Transferred to 1.17.3.2
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now EC 1.17.3.2 xanthine oxidase. The enzyme was
            incorrectly classified as acting on a CH-OH group (EC 1.1.3.22
            created 1961 as EC 1.2.3.2, transferred 1984 to EC 1.1.3.22,
            modified 1989, deleted 2004)
STRUCTURES  PDB: 1FIQ  1WYG  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.22
            ExPASy - ENZYME nomenclature database: 1.1.3.22
            ExplorEnz - The Enzyme Database: 1.1.3.22
            ERGO genome analysis and discovery system: 1.1.3.22
            BRENDA, the Enzyme Database: 1.1.3.22
///
ENTRY       EC 1.1.3.23                 Enzyme
NAME        thiamine oxidase;
            thiamin dehydrogenase;
            thiamine dehydrogenase;
            thiamin:oxygen 5-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     thiamine:oxygen 5-oxidoreductase
REACTION    thiamine + 2 O2 + H2O = thiamine acetic acid + 2 H2O2 [RN:R02132]
ALL_REAC    R02132;
            (other) R00033 R00072
SUBSTRATE   thiamine [CPD:C00378];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     thiamine acetic acid [CPD:C02892];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). The product differs from thiamine in
            replacement of -CH2.CH2.OH by -CH2.COOH; the two-step oxidation
            proceeds without the release of the intermediate aldehyde from the
            enzyme.
REFERENCE   1  [PMID:8076]
  AUTHORS   Edmondson DE, Kenney WC, Singer TP.
  TITLE     Structural elucidation and properties of
            8alpha-(N1-histidyl)riboflavin: the flavin component of thiamine
            dehydrogenase and beta-cyclopiazonate oxidocyclase.
  JOURNAL   Biochemistry. 15 (1976) 2937-45.
REFERENCE   2  [PMID:2988447]
  AUTHORS   Gomez-Moreno C, Edmondson DE.
  TITLE     Evidence for an aldehyde intermediate in the catalytic mechanism of
            thiamine oxidase.
  JOURNAL   Arch. Biochem. Biophys. 239 (1985) 46-52.
REFERENCE   3  [PMID:4987737]
  AUTHORS   Neal RA.
  TITLE     Bacterial metabolism of thiamine. 3. Metabolism of thiamine to
            3-(2'-methyl-4'-amino-5'-pyrimidylmethyl)-4-methyl-thiazole-5-acetic
            acid (thiamine acetic acid) by a flavoprotein isolated from a soil
            microorganism.
  JOURNAL   J. Biol. Chem. 245 (1970) 2599-604.
PATHWAY     PATH: map00730  Thiamine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.23
            ExPASy - ENZYME nomenclature database: 1.1.3.23
            ExplorEnz - The Enzyme Database: 1.1.3.23
            ERGO genome analysis and discovery system: 1.1.3.23
            BRENDA, the Enzyme Database: 1.1.3.23
            CAS: 96779-44-1
///
ENTRY       EC 1.1.3.24       Obsolete  Enzyme
NAME        Transferred to 1.3.3.12
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
COMMENT     Transferred entry: L-galactonolactone oxidase. Now EC 1.3.3.12,
            L-galactonolactone oxidase. The enzyme had been incorrectly
            classified as acting upon a CH-OH donor rather than a CH-CH donor.
            (EC 1.1.3.24 created 1984, deleted 2006)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.24
            ExPASy - ENZYME nomenclature database: 1.1.3.24
            ExplorEnz - The Enzyme Database: 1.1.3.24
            ERGO genome analysis and discovery system: 1.1.3.24
            BRENDA, the Enzyme Database: 1.1.3.24
///
ENTRY       EC 1.1.3.25       Obsolete  Enzyme
NAME        Transferred to 1.1.99.18
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now included with EC 1.1.99.18, cellobiose
            dehydrogenase (acceptor) (EC 1.1.3.25 created 1986, deleted 2005)
STRUCTURES  PDB: 1D7B  1D7C  1D7D  1KDG  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.25
            ExPASy - ENZYME nomenclature database: 1.1.3.25
            ExplorEnz - The Enzyme Database: 1.1.3.25
            ERGO genome analysis and discovery system: 1.1.3.25
            BRENDA, the Enzyme Database: 1.1.3.25
///
ENTRY       EC 1.1.3.26       Obsolete  Enzyme
NAME        Transferred to 1.21.3.2
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now EC 1.21.3.2 columbamine oxidase (EC 1.1.3.26
            created 1989, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.26
            ExPASy - ENZYME nomenclature database: 1.1.3.26
            ExplorEnz - The Enzyme Database: 1.1.3.26
            ERGO genome analysis and discovery system: 1.1.3.26
            BRENDA, the Enzyme Database: 1.1.3.26
///
ENTRY       EC 1.1.3.27                 Enzyme
NAME        hydroxyphytanate oxidase;
            L-2-hydroxyphytanate:oxygen 2-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     L-2-hydroxyphytanate:oxygen 2-oxidoreductase
REACTION    L-2-hydroxyphytanate + O2 = 2-oxophytanate + H2O2 [RN:R07151]
ALL_REAC    R07151
SUBSTRATE   L-2-hydroxyphytanate [CPD:C02982];
            O2 [CPD:C00007]
PRODUCT     2-oxophytanate [CPD:C02117];
            H2O2 [CPD:C00027]
REFERENCE   1  [PMID:3288289]
  AUTHORS   Vamecq J, Draye JP.
  TITLE     The enzymatic and mass spectrometric identification of 2-oxophytanic
            acid, a product of the peroxisomal oxidation of l-2-hydroxyphytanic
            acid.
  JOURNAL   Biomed. Environ. Mass. Spectrom. 15 (1988) 345-51.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.27
            ExPASy - ENZYME nomenclature database: 1.1.3.27
            ExplorEnz - The Enzyme Database: 1.1.3.27
            ERGO genome analysis and discovery system: 1.1.3.27
            BRENDA, the Enzyme Database: 1.1.3.27
            CAS: 114454-12-5
///
ENTRY       EC 1.1.3.28                 Enzyme
NAME        nucleoside oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     nucleoside:oxygen 5'-oxidoreductase
REACTION    (1) inosine + O2 = 9-riburonosylhypoxanthine + 2 H2O [RN:R05821];
            (2) (1a) 2 inosine + O2 = 2 5'-dehydroinosine + 2 H2O;
            (3) (1b) 2 5'-dehydroinosine + O2 = 2 9-riburonosylhypoxanthine + 2
            H2O
ALL_REAC    R05821;
            (other) R00055 R05822
SUBSTRATE   inosine [CPD:C00294];
            O2 [CPD:C00007];
            5'-dehydroinosine [CPD:C01993]
PRODUCT     9-riburonosylhypoxanthine [CPD:C11631];
            H2O [CPD:C00001];
            5'-dehydroinosine [CPD:C01993]
COMMENT     Other purine and pyrimidine nucleosides (as well as
            2'-deoxynucleosides) are substrates, but ribose and nucleotides are
            not substrates. The overall reaction takes place in two separate
            steps, with the 5'-dehydro nucleoside being released from the enzyme
            to serve as substrate for the second reaction. This enzyme differs
            from EC 1.1.3.39, nucleoside oxidase (H2O2-forming), as it produces
            water rather than hydrogen peroxide.
REFERENCE   1
  AUTHORS   Isono, Y., Sudo, T. and Hoshino, M.
  TITLE     Purification and reaction of a new enzyme, nucleoside oxidase.
  JOURNAL   Agric. Biol. Chem. 53 (1989) 1663-1669.
  ORGANISM  Pseudomonas maltophilia
REFERENCE   2
  AUTHORS   Isono, Y., Sudo, T. and Hoshino, M.
  TITLE     Properties of a new enzyme, nucleoside oxidase, from Pseudomonas
            maltophilia LB-86.
  JOURNAL   Agric. Biol. Chem. 53 (1989) 1671-1677.
  ORGANISM  Pseudomonas maltophilia
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.28
            ExPASy - ENZYME nomenclature database: 1.1.3.28
            ExplorEnz - The Enzyme Database: 1.1.3.28
            ERGO genome analysis and discovery system: 1.1.3.28
            BRENDA, the Enzyme Database: 1.1.3.28
            CAS: 82599-71-1
///
ENTRY       EC 1.1.3.29                 Enzyme
NAME        N-acylhexosamine oxidase;
            N-acyl-D-hexosamine oxidase;
            N-acyl-beta-D-hexosamine:oxygen 1-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     N-acyl-D-hexosamine:oxygen 1-oxidoreductase
REACTION    N-acetyl-D-glucosamine + O2 = N-acetyl-D-glucosaminate + H2O2
            [RN:R01203]
ALL_REAC    R01203
SUBSTRATE   N-acetyl-D-glucosamine [CPD:C00140];
            O2 [CPD:C00007]
PRODUCT     N-acetyl-D-glucosaminate [CPD:C01133];
            H2O2 [CPD:C00027]
COMMENT     Also acts on N-glycolylglucosamine, N-acetylgalactosamine and, more
            slowly, on N-acetylmannosamine.
REFERENCE   1
  AUTHORS   Horiuchi, T.
  TITLE     Purification and properties of N-acyl-D-hexosamine oxidase from
            Pseudomonas sp 15-1.
  JOURNAL   Agric. Biol. Chem. 53 (1989) 361-368.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.29
            ExPASy - ENZYME nomenclature database: 1.1.3.29
            ExplorEnz - The Enzyme Database: 1.1.3.29
            ERGO genome analysis and discovery system: 1.1.3.29
            BRENDA, the Enzyme Database: 1.1.3.29
            CAS: 121479-58-1
///
ENTRY       EC 1.1.3.30                 Enzyme
NAME        polyvinyl-alcohol oxidase;
            dehydrogenase, polyvinyl alcohol;
            PVA oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     polyvinyl-alcohol:oxygen oxidoreductase
REACTION    polyvinyl alcohol + O2 = oxidized polyvinyl alcohol + H2O2
            [RN:R03135]
ALL_REAC    R03135
SUBSTRATE   polyvinyl alcohol [CPD:C00980];
            O2 [CPD:C00007]
PRODUCT     oxidized polyvinyl alcohol [CPD:C01166];
            H2O2 [CPD:C00027]
REFERENCE   1  [PMID:16346711]
  AUTHORS   Shimao M, Nishimura Y, Kato N, Sakazawa C.
  TITLE     Localization of Polyvinyl Alcohol Oxidase Produced by a Bacterial
            Symbiont, Pseudomonas sp. Strain VM15C.
  JOURNAL   Appl. Environ. Microbiol. 49 (1985) 8-10.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:16347841]
  AUTHORS   Shimao M, Onishi S, Kato N, Sakazawa C.
  TITLE     Pyrroloquinoline Quinone-Dependent Cytochrome Reduction in Polyvinyl
            Alcohol-Degrading Pseudomonas sp. Strain VM15C.
  JOURNAL   Appl. Environ. Microbiol. 55 (1989) 275-278.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.30
            ExPASy - ENZYME nomenclature database: 1.1.3.30
            ExplorEnz - The Enzyme Database: 1.1.3.30
            ERGO genome analysis and discovery system: 1.1.3.30
            BRENDA, the Enzyme Database: 1.1.3.30
            CAS: 119940-13-5
///
ENTRY       EC 1.1.3.31       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
COMMENT     Deleted entry: methanol oxidase. Cannot be distinguished from EC
            1.1.3.13, alcohol oxidase. (EC 1.1.3.31 created 1992, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.31
            ExPASy - ENZYME nomenclature database: 1.1.3.31
            ExplorEnz - The Enzyme Database: 1.1.3.31
            ERGO genome analysis and discovery system: 1.1.3.31
            BRENDA, the Enzyme Database: 1.1.3.31
///
ENTRY       EC 1.1.3.32       Obsolete  Enzyme
NAME        Transferred to 1.14.21.1
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now EC 1.14.21.1, (S)-stylopine synthase (EC
            1.1.3.32 created 1999, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.32
            ExPASy - ENZYME nomenclature database: 1.1.3.32
            ExplorEnz - The Enzyme Database: 1.1.3.32
            ERGO genome analysis and discovery system: 1.1.3.32
            BRENDA, the Enzyme Database: 1.1.3.32
///
ENTRY       EC 1.1.3.33       Obsolete  Enzyme
NAME        Transferred to 1.14.21.2
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now EC 1.14.21.2, (S)-cheilanthifoline synthase
            (EC 1.1.3.33 created 1999, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.33
            ExPASy - ENZYME nomenclature database: 1.1.3.33
            ExplorEnz - The Enzyme Database: 1.1.3.33
            ERGO genome analysis and discovery system: 1.1.3.33
            BRENDA, the Enzyme Database: 1.1.3.33
///
ENTRY       EC 1.1.3.34       Obsolete  Enzyme
NAME        Transferred to 1.14.21.3
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now EC 1.14.21.3 berbamunine synthase (EC
            1.1.3.34 created 1999, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.34
            ExPASy - ENZYME nomenclature database: 1.1.3.34
            ExplorEnz - The Enzyme Database: 1.1.3.34
            ERGO genome analysis and discovery system: 1.1.3.34
            BRENDA, the Enzyme Database: 1.1.3.34
///
ENTRY       EC 1.1.3.35       Obsolete  Enzyme
NAME        Transferred to 1.14.21.4
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now EC 1.14.21.4 salutaridine synthase (EC
            1.1.3.35 created 1999, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.35
            ExPASy - ENZYME nomenclature database: 1.1.3.35
            ExplorEnz - The Enzyme Database: 1.1.3.35
            ERGO genome analysis and discovery system: 1.1.3.35
            BRENDA, the Enzyme Database: 1.1.3.35
///
ENTRY       EC 1.1.3.36       Obsolete  Enzyme
NAME        Transferred to 1.14.21.5
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now EC 1.14.21.5, (S)-canadine synthase (EC
            1.1.3.36 created 1999, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.36
            ExPASy - ENZYME nomenclature database: 1.1.3.36
            ExplorEnz - The Enzyme Database: 1.1.3.36
            ERGO genome analysis and discovery system: 1.1.3.36
            BRENDA, the Enzyme Database: 1.1.3.36
///
ENTRY       EC 1.1.3.37                 Enzyme
NAME        D-arabinono-1,4-lactone oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     D-arabinono-1,4-lactone:oxygen oxidoreductase
REACTION    D-arabinono-1,4-lactone + O2 = D-erythro-ascorbate + H2O2
            [RN:R02715]
ALL_REAC    R02715
SUBSTRATE   D-arabinono-1,4-lactone [CPD:C00652];
            O2 [CPD:C00007]
PRODUCT     D-erythro-ascorbate [CPD:C06316];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:7957197]
  AUTHORS   Huh WK, Kim ST, Yang KS, Seok YJ, Hah YC, Kang SO.
  TITLE     Characterisation of D-arabinono-1,4-lactone oxidase from Candida
            albicans ATCC 10231.
  JOURNAL   Eur. J. Biochem. 225 (1994) 1073-9.
  ORGANISM  Candida albicans [GN:cal]
ORTHOLOGY   KO: K00107  D-arabinono-1,4-lactone oxidase
GENES       SCE: YML086C(ALO1)
            AGO: AGOS_AFR440C
            PIC: PICST_88335(ALO1)
            CAL: CaO19_7551(CaO19.7551)
            CGR: CAGL0H04125g
            ANI: AN0836.2
            AOR: AO090005001234
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.37
            ExPASy - ENZYME nomenclature database: 1.1.3.37
            ExplorEnz - The Enzyme Database: 1.1.3.37
            ERGO genome analysis and discovery system: 1.1.3.37
            BRENDA, the Enzyme Database: 1.1.3.37
            CAS: 182372-12-9
///
ENTRY       EC 1.1.3.38                 Enzyme
NAME        vanillyl-alcohol oxidase;
            4-hydroxy-2-methoxybenzyl alcohol oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     vanillyl alcohol:oxygen oxidoreductase
REACTION    vanillyl alcohol + O2 = vanillin + H2O2 [RN:R02877]
ALL_REAC    R02877
SUBSTRATE   vanillyl alcohol [CPD:C06317];
            O2 [CPD:C00007]
PRODUCT     vanillin [CPD:C00755];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     Vanillyl-alcohol oxidase from Penicillium simplicissimum contains
            covalently bound FAD. It converts a wide range of 4-hydroxybenzyl
            alcohols and 4-hydroxybenzylamines into the corresponding aldehydes.
            The allyl group of 4-allylphenols is also converted into the
            -CH=CH-CH2OH group.
REFERENCE   1  [PMID:1396672]
  AUTHORS   de Jong E, van Berkel WJ, van der Zwan RP, de Bont JA.
  TITLE     Purification and characterization of vanillyl-alcohol oxidase from
            Penicillium simplicissimum. A novel aromatic alcohol oxidase
            containing covalently bound FAD.
  JOURNAL   Eur. J. Biochem. 208 (1992) 651-7.
  ORGANISM  Penicillium simplicissimum
REFERENCE   2  [PMID:8529652]
  AUTHORS   Fraaije MW, Veeger C, van Berkel WJ.
  TITLE     Substrate specificity of flavin-dependent vanillyl-alcohol oxidase
            from Penicillium simplicissimum. Evidence for the production of
            4-hydroxycinnamyl alcohols from 4-allylphenols.
  JOURNAL   Eur. J. Biochem. 234 (1995) 271-7.
  ORGANISM  Penicillium simplicissimum
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
GENES       NAR: Saro_1492
            RHA: RHA1_ro03282
STRUCTURES  PDB: 1DZN  1E0Y  1E8G  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.38
            ExPASy - ENZYME nomenclature database: 1.1.3.38
            ExplorEnz - The Enzyme Database: 1.1.3.38
            ERGO genome analysis and discovery system: 1.1.3.38
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.3.38
            BRENDA, the Enzyme Database: 1.1.3.38
            CAS: 143929-24-2
///
ENTRY       EC 1.1.3.39                 Enzyme
NAME        nucleoside oxidase (H2O2-forming)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     nucleoside:oxygen 5'-oxidoreductase (H2O2-forming)
REACTION    (1) adenosine + 2 O2 = 9-riburonosyladenine + 2 H2O2 [RN:R05695];
            (2) (1a) adenosine + O2 = 5'-dehydroadenosine + H2O2;
            (3) (1b) 5'-dehydroadenosine + O2 = 9-riburonosyladenine + H2O2
ALL_REAC    R05695;
            (other) R05696 R05697
SUBSTRATE   adenosine [CPD:C00212];
            O2 [CPD:C00007];
            5'-dehydroadenosine [CPD:C11500]
PRODUCT     9-riburonosyladenine [CPD:C11501];
            H2O2 [CPD:C00027];
            5'-dehydroadenosine [CPD:C11500]
COMMENT     A heme-containing flavoprotein (FAD). Other purine and pyrimidine
            nucleosides (as well as 2'-deoxynucleosides and arabinosides) are
            substrates, but ribose and nucleotides are not substrates. The
            overall reaction takes place in two separate steps, with the
            5'-dehydro nucleoside being released from the enzyme to serve as
            substrate for the second reaction. This enzyme differs from EC
            1.1.3.28, nucleoside oxidase, as it produces hydrogen peroxide
            rather than water.
REFERENCE   1
  AUTHORS   Koga, S., Ogawa, J., Cheng, L.Y., Choi, Y.M., Yamada, H. and
            Shimizu, S.
  TITLE     Nucleoside oxidase, a hydrogen peroxide-forming oxidase, from
            Flavobacterium meningosepticum.
  JOURNAL   Appl. Environ. Microbiol. 63 (1997) 4282-4286.
  ORGANISM  Flavobacterium meningosepticum
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.39
            ExPASy - ENZYME nomenclature database: 1.1.3.39
            ExplorEnz - The Enzyme Database: 1.1.3.39
            ERGO genome analysis and discovery system: 1.1.3.39
            BRENDA, the Enzyme Database: 1.1.3.39
///
ENTRY       EC 1.1.3.40                 Enzyme
NAME        D-mannitol oxidase;
            mannitol oxidase;
            D-arabitol oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     mannitol:oxygen oxidoreductase (cyclizing)
REACTION    mannitol + O2 = mannose + H2O2 [RN:R05698]
ALL_REAC    R05698
SUBSTRATE   mannitol [CPD:C00392];
            O2 [CPD:C00007]
PRODUCT     mannose [CPD:C00159];
            H2O2 [CPD:C00027]
COMMENT     Also catalyses the oxidation of D-arabinitol and, to a lesser
            extent, D-glucitol (sorbitol), whereas L-arabinitol is not a good
            substrate. The enzyme from the snails Helix aspersa and Arion ater
            is found in a specialised tubular organelle that has been termed the
            mannosome.
REFERENCE   1  [PMID:3519307]
  AUTHORS   Vorhaben JE, Smith DD Jr, Campbell JW.
  TITLE     Mannitol oxidase: partial purification and characterization of the
            membrane-bound enzyme from the snail Helix aspersa.
  JOURNAL   Int. J. Biochem. 18 (1986) 337-44.
  ORGANISM  Helix aspersa
REFERENCE   2
  AUTHORS   Large, A.T., Jones, C.J.P. and Connock, M.J.
  TITLE     The association of mannitol oxidase with a distinct organelle in the
            digestive gland of the terrestrial slug Arion ater.
  JOURNAL   Protoplasma 175 (1993) 93-101.
  ORGANISM  Arion ater
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.40
            ExPASy - ENZYME nomenclature database: 1.1.3.40
            ExplorEnz - The Enzyme Database: 1.1.3.40
            ERGO genome analysis and discovery system: 1.1.3.40
            BRENDA, the Enzyme Database: 1.1.3.40
///
ENTRY       EC 1.1.3.41                 Enzyme
NAME        xylitol oxidase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
SYSNAME     xylitol:oxygen oxidoreductase
REACTION    xylitol + O2 = xylose + H2O2 [RN:R07152]
ALL_REAC    R07152
SUBSTRATE   xylitol [CPD:C00379];
            O2 [CPD:C00007]
PRODUCT     xylose [CPD:C01394];
            H2O2 [CPD:C00027]
COMMENT     The enzyme from Streptomyces sp. IKD472 is a monomeric oxidase
            containing one molecule of FAD per molecule of protein. The enzyme
            also oxidizes D-sorbitol.
REFERENCE   1  [PMID:16232758]
  AUTHORS   Yamashita M, Omura H, Okamoto E, Furuya Y, Yabuuchi M, Fukahi K,
            Murooka Y.
  TITLE     Isolation, characterization, and molecular cloning of a thermostable
            xylitol oxidase from Streptomyces sp. IKD472.
  JOURNAL   J. Biosci. Bioeng. 89 (2000) 350-60.
  ORGANISM  Streptomyces sp.
ORTHOLOGY   KO: K00594  xylitol oxidase
GENES       SCO: SCO6147(SC1A9.11c)
            SMA: SAV2090
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.3.41
            ExPASy - ENZYME nomenclature database: 1.1.3.41
            ExplorEnz - The Enzyme Database: 1.1.3.41
            ERGO genome analysis and discovery system: 1.1.3.41
            BRENDA, the Enzyme Database: 1.1.3.41
            CAS: 177322-52-0
///
ENTRY       EC 1.1.3.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With oxygen as acceptor
REACTION    (1) 2-Dehydro-D-glucose + Oxygen <=> 2-Dehydro-D-glucono-1,5-lactone
            + H2O2 [RN:R04048];
            (2) 2 5,6-Dihydroxyindole + Oxygen <=> 2 Indole-5,6-quinone + 2 H2O
            [RN:R04884];
            (3) 2-Hydroxypropylphosphonate + Oxygen <=> Phosphonomycin + H2O2
            [RN:R05200];
            (4) 2,2-Bis(4-hydroxyphenyl)-1-propanol + Oxygen <=>
            2,2-Bis(4-hydroxyphenyl)-propanoic acid + H2O [RN:R06887]
SUBSTRATE   2-Dehydro-D-glucose [CPD:C02779];
            Oxygen [CPD:C00007];
            5,6-Dihydroxyindole [CPD:C05578];
            2-Hydroxypropylphosphonate [CPD:C06452];
            2,2-Bis(4-hydroxyphenyl)-1-propanol [CPD:C13631]
PRODUCT     2-Dehydro-D-glucono-1,5-lactone [CPD:C06440];
            H2O2 [CPD:C00027];
            Indole-5,6-quinone [CPD:C05579];
            H2O [CPD:C00001];
            Phosphonomycin [CPD:C06454];
            2,2-Bis(4-hydroxyphenyl)-propanoic acid [CPD:C13633]
///
ENTRY       EC 1.1.4.1                  Enzyme
NAME        vitamin-K-epoxide reductase (warfarin-sensitive)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With a disulfide as acceptor
SYSNAME     2-methyl-3-phytyl-1,4-naphthoquinone:oxidized-dithiothreitol
            oxidoreductase
REACTION    2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol =
            2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone +
            1,4-dithiothreitol [RN:R03511]
ALL_REAC    R03511;
            (other) R03645
SUBSTRATE   2-methyl-3-phytyl-1,4-naphthoquinone [CPD:C02059];
            oxidized dithiothreitol [CPD:C01119]
PRODUCT     2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone
            [CPD:C05849];
            1,4-dithiothreitol [CPD:C00265]
INHIBITOR   Warfarin [CPD:C01541]
COMMENT     In the reverse reaction, vitamin K 2,3-epoxide is reduced to vitamin
            K and possibly to vitamin K hydroquinone by 1,4-dithiothreitol,
            which is oxidized to a disulfide; some other dithiols and
            4-butanethiol can also act. Inhibited strongly by warfarin [cf. EC
            1.1.4.2 vitamin-K-epoxide reductase (warfarin-insensitive)].
REFERENCE   1  [PMID:6733086]
  AUTHORS   Lee JJ, Fasco MJ.
  TITLE     Metabolism of vitamin K and vitamin K 2,3-epoxide via interaction
            with a common disulfide.
  JOURNAL   Biochemistry. 23 (1984) 2246-52.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:3857611]
  AUTHORS   Mukharji I, Silverman RB.
  TITLE     Purification of a vitamin K epoxide reductase that catalyzes
            conversion of vitamin K 2,3-epoxide to
            3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 2713-7.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:646989]
  AUTHORS   Whitlon DS, Sadowski JA, Suttie JW.
  TITLE     Mechanism of coumarin action: significance of vitamin K epoxide
            reductase inhibition.
  JOURNAL   Biochemistry. 17 (1978) 1371-7.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K05357  vitamin-K-epoxide reductase (warfarin-sensitive)
GENES       HSA: 79001(VKORC1)
            MMU: 27973(Vkorc1)
            RNO: 309004(Vkorc1)
            CFA: 479775(VKORC1)
            BTA: 445422(VKORC1)
            GGA: 404205(VKORC1)
            DME: Dmel_CG33544(Vkor)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.4.1
            ExPASy - ENZYME nomenclature database: 1.1.4.1
            ExplorEnz - The Enzyme Database: 1.1.4.1
            ERGO genome analysis and discovery system: 1.1.4.1
            BRENDA, the Enzyme Database: 1.1.4.1
            CAS: 55963-40-1
///
ENTRY       EC 1.1.4.2                  Enzyme
NAME        vitamin-K-epoxide reductase (warfarin-insensitive)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With a disulfide as acceptor
SYSNAME     3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone:oxidized-dithi
            othreitol oxidoreductase
REACTION    3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized
            dithiothreitol =
            2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone +
            1,4-dithiothreitol [RN:R03512]
ALL_REAC    R03512;
            (other) R05830
SUBSTRATE   3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone [CPD:C02785];
            oxidized dithiothreitol [CPD:C01119]
PRODUCT     2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone
            [CPD:C05849];
            1,4-dithiothreitol [CPD:C00265]
COMMENT     In the reverse reaction, vitamin K 2,3-epoxide is reduced to
            3-hydroxy- (and 2-hydroxy-) vitamin K by 1,4-dithiothreitol, which
            is oxidized to a disulfide. Not inhibited by warfarin [cf. EC
            1.1.4.1 vitamin-K-epoxide reductase (warfarin-sensitive)].
REFERENCE   1  [PMID:3857611]
  AUTHORS   Mukharji I, Silverman RB.
  TITLE     Purification of a vitamin K epoxide reductase that catalyzes
            conversion of vitamin K 2,3-epoxide to
            3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 2713-7.
  ORGANISM  cow [GN:bta]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.4.2
            ExPASy - ENZYME nomenclature database: 1.1.4.2
            ExplorEnz - The Enzyme Database: 1.1.4.2
            ERGO genome analysis and discovery system: 1.1.4.2
            BRENDA, the Enzyme Database: 1.1.4.2
            CAS: 97089-80-0
///
ENTRY       EC 1.1.5.1        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With a quinone or similar compound as acceptor
COMMENT     Deleted entry: cellobiose dehydrogenase (quinone). Now known to be
            proteolytic product of EC 1.1.99.18, cellobiose dehydrogenase
            (acceptor). (EC 1.1.5.1 created 1983, deleted 2002)
STRUCTURES  PDB: 1KDG  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.5.1
            ExPASy - ENZYME nomenclature database: 1.1.5.1
            ExplorEnz - The Enzyme Database: 1.1.5.1
            ERGO genome analysis and discovery system: 1.1.5.1
            BRENDA, the Enzyme Database: 1.1.5.1
///
ENTRY       EC 1.1.5.2                  Enzyme
NAME        quinoprotein glucose dehydrogenase;
            D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase;
            glucose dehydrogenase (PQQ-dependent);
            glucose dehydrogenase (pyrroloquinoline-quinone);
            quinoprotein D-glucose dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With a quinone or similar compound as acceptor
SYSNAME     D-glucose:ubiquinone oxidoreductase
REACTION    D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
            [RN:R06620]
ALL_REAC    R06620
SUBSTRATE   D-glucose [CPD:C00031];
            ubiquinone [CPD:C00399]
PRODUCT     D-glucono-1,5-lactone [CPD:C00198];
            ubiquinol [CPD:C00390]
COFACTOR    PQQ [CPD:C00113]
COMMENT     Requires Mg2+ or Ca2+ for maximal activity. This is a PQQ-containing
            quinoprotein that catalyses a direct oxidation of D-glucose to
            D-gluconate in the periplasm of some bacteria and concomitantly
            transfers electrons to ubiquinol oxidase through ubiquinone in the
            respiratory chain.
REFERENCE   1
  AUTHORS   Ameyama, M., Nonobe, M., Hayashi, M., Shinagawa, E., Matsushita, K.
            and Adachi, O.
  TITLE     Mode of binding of pyrroloquinoline quinone to apo-glucose
            dehydrogenase.
  JOURNAL   Agric. Biol. Chem. 49 (1985) 1227-1231.
  ORGANISM  Pseudomonas fluorescens, Gluconobacter suboxydans, Escherichia coli
            [GN:eco]
REFERENCE   2  [PMID:520586]
  AUTHORS   Duine JA, Frank J, van Zeeland JK.
  TITLE     Glucose dehydrogenase from Acinetobacter calcoaceticus: a
            'quinoprotein'.
  JOURNAL   FEBS. Lett. 108 (1979) 443-6.
  ORGANISM  Acinetobacter calcoaceticus
REFERENCE   3  [PMID:8509415]
  AUTHORS   Yamada M, Sumi K, Matsushita K, Adachi O, Yamada Y.
  TITLE     Topological analysis of quinoprotein glucose dehydrogenase in
            Escherichia coli and its ubiquinone-binding site.
  JOURNAL   J. Biol. Chem. 268 (1993) 12812-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:9578566]
  AUTHORS   Dewanti AR, Duine JA.
  TITLE     Reconstitution of membrane-integrated quinoprotein glucose
            dehydrogenase apoenzyme with PQQ and the holoenzyme's mechanism of
            action.
  JOURNAL   Biochemistry. 37 (1998) 6810-8.
  ORGANISM  Acinetobacter calcoaceticus
REFERENCE   5  [PMID:10518528]
  AUTHORS   Oubrie A, Rozeboom HJ, Dijkstra BW.
  TITLE     Active-site structure of the soluble quinoprotein glucose
            dehydrogenase complexed with methylhydrazine: a covalent
            cofactor-inhibitor complex.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 11787-91.
  ORGANISM  Acinetobacter calcoaceticus
REFERENCE   6  [PMID:11604400]
  AUTHORS   Elias M, Tanaka M, Sakai M, Toyama H, Matsushita K, Adachi O, Yamada
            M.
  TITLE     C-terminal periplasmic domain of Escherichia coli quinoprotein
            glucose dehydrogenase transfers electrons to ubiquinone.
  JOURNAL   J. Biol. Chem. 276 (2001) 48356-61.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00030  Pentose phosphate pathway
ORTHOLOGY   KO: K00117  quinoprotein glucose dehydrogenase
GENES       ECO: b0124(gcd)
            ECJ: JW0120(gcd)
            ECE: Z0134(gcd)
            ECS: ECs0128
            ECC: c0153(gcd)
            ECI: UTI89_C0137(gcd)
            ECP: ECP_0132
            ECW: EcE24377A_0126(gcd) EcE24377A_0909(yliI)
            ECX: EcHS_A0128(gcd)
            STY: STY0191(gcd)
            STT: t0174(gcd)
            SPT: SPA0172(gcd)
            SEC: SC0169(gcd)
            STM: STM0169(gcd)
            SFL: SF0121(gcd)
            SFX: S0123(gcd)
            SFV: SFV_0115(gcd)
            SSN: SSON_0132(gcd)
            SBO: SBO_0113(gcd)
            ENT: Ent638_0672
            SPE: Spro_3100
            XCC: XCC1575(gcd) XCC3083(gcd)
            XCB: XC_1075 XC_2659
            XCV: XCV1673(gcd1) XCV3337(gcd2)
            XAC: XAC1633(gcd) XAC3212(gcd)
            PAE: PA2290(gcd)
            PAU: PA14_34970(gcd)
            PAP: PSPA7_3111
            PPU: PP_1444(gcd) PP_3569
            PST: PSPTO_2568(gcd-1) PSPTO_4196(gcd)
            PSB: Psyr_2574 Psyr_3930
            PSP: PSPPH_3927(gcd)
            PFL: PFL_4916 PFL_5668
            PFO: Pfl_2712 Pfl_4577
            PEN: PSEEN1170
            PAR: Psyc_1237
            ACI: ACIAD2983(gcd)
            ILO: IL0790(gcd)
            PAT: Patl_2112
            CSA: Csal_2831
            BXE: Bxe_A1505 Bxe_C0173
            MPT: Mpe_A1594
            HAR: HEAR0054
            PUB: SAR11_0305(yliI)
            MLO: mll1500
            PLA: Plav_2593
            SME: SMc00110(gcd)
            SMD: Smed_0595
            ATU: Atu3354 Atu4135(gcd)
            ATC: AGR_L_1436 AGR_L_2936
            RET: RHE_CH01222(gcd) RHE_CH03394(ypch01196)
            RLE: RL1354(gcd) RL3446 RL3832(gcd)
            BRA: BRADO0601(gcd)
            BBT: BBta_7581(gcd)
            RPB: RPB_3211
            RSP: RSP_2673
            RSH: Rsph17029_1330 Rsph17029_3539
            RSQ: Rsph17025_1211
            RDE: RD1_2633
            SWI: Swit_1054 Swit_1900
            GOX: GOX0265 GOX0516 GOX0854(sldA) GOX1441 GOX1857
            SUS: Acid_1044 Acid_1183 Acid_1639 Acid_1932 Acid_2289 Acid_2557
                 Acid_3097 Acid_3236 Acid_4075 Acid_4918
            SEN: SACE_0825
            RBA: RB10127 RB1988(gdhP)
            SYN: slr1608(gdhB)
            GFO: GFO_0814(gdhB)
            TTH: TTC0202
            HMA: pNG7073(qgd)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.5.2
            ExPASy - ENZYME nomenclature database: 1.1.5.2
            ExplorEnz - The Enzyme Database: 1.1.5.2
            ERGO genome analysis and discovery system: 1.1.5.2
            BRENDA, the Enzyme Database: 1.1.5.2
            CAS: 81669-60-5
///
ENTRY       EC 1.1.99.1                 Enzyme
NAME        choline dehydrogenase;
            choline oxidase;
            choline-cytochrome c reductase;
            choline:(acceptor) oxidoreductase;
            choline:(acceptor) 1-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     choline:acceptor 1-oxidoreductase
REACTION    choline + acceptor = betaine aldehyde + reduced acceptor [RN:R01025]
ALL_REAC    R01025;
            (other) R02567
SUBSTRATE   choline [CPD:C00114];
            acceptor [CPD:C00028]
PRODUCT     betaine aldehyde [CPD:C00576];
            reduced acceptor [CPD:C00030]
COFACTOR    PQQ [CPD:C00113]
COMMENT     A quinoprotein. In many bacteria, plants and animals, the
            osmoprotectant betaine is synthesized using different enzymes to
            catalyse the conversion of (1) choline into betaine aldehyde and (2)
            betaine aldehyde into betaine. In plants, the first reaction is
            catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals
            and many bacteria, it is catalysed by either membrane-bound choline
            dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17)
            [4]. The enzyme involved in the second step, EC 1.2.1.8,
            betaine-aldehyde dehydrogenase, appears to be the same in plants,
            animals and bacteria.
REFERENCE   1
  AUTHORS   Ameyama, M., Shinagawa, E., Matsuchita, K., Takimoto, K., Nakashima,
            K. and Adachi, O.
  TITLE     Mammalian choline dehydrogenase is a quinoprotein.
  JOURNAL   Agric. Biol. Chem. 49 (1985) 3623-3626.
  ORGANISM  dog [GN:cfa]
REFERENCE   2  [PMID:13249959]
  AUTHORS   EBISUZAKI K, WILLIAMS JN Jr.
  TITLE     Preparation and partial purification of soluble choline
            dehydrogenase from liver mitochondria.
  JOURNAL   Biochem. J. 60 (1955) 644-6.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:12676692]
  AUTHORS   Gadda G, McAllister-Wilkins EE.
  TITLE     Cloning, expression, and purification of choline dehydrogenase from
            the moderate halophile Halomonas elongata.
  JOURNAL   Appl. Environ. Microbiol. 69 (2003) 2126-32.
  ORGANISM  Halomonas elongata
REFERENCE   4  [PMID:12466265]
  AUTHORS   Waditee R, Tanaka Y, Aoki K, Hibino T, Jikuya H, Takano J, Takabe T,
            Takabe T.
  TITLE     Isolation and functional characterization of N-methyltransferases
            that catalyze betaine synthesis from glycine in a halotolerant
            photosynthetic organism Aphanothece halophytica.
  JOURNAL   J. Biol. Chem. 278 (2003) 4932-42.
  ORGANISM  Aphanothece halophytica
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K00108  choline dehydrogenase
GENES       HSA: 55349(CHDH)
            MMU: 218865(Chdh)
            RNO: 290551(Chdh)
            CFA: 484723(CHDH)
            GGA: 415993(CHDH)
            SPU: 587688(LOC587688) 589191(LOC589191) 591798(LOC591798)
                 591835(LOC591835)
            CEL: C34C6.4
            ANI: AN7832.2 AN7998.2
            AFM: AFUA_1G11370 AFUA_2G01770 AFUA_2G15020 AFUA_3G08070
                 AFUA_5G00630
            AOR: AO090120000309
            UMA: UM01872.1 UM03551.1
            TBR: Tb10.70.7840
            ECO: b0311(betA)
            ECJ: JW0303(betA)
            ECE: Z0398(betA)
            ECS: ECs0357
            ECC: c0431(betA)
            ECI: UTI89_C0340(betA)
            ECP: ECP_0386
            ECV: APECO1_1679(betA)
            ECW: EcE24377A_0326(betA)
            ECX: EcHS_A0370(betA)
            YPE: YPO1165(betA)
            YPM: YP_0994(betA)
            YPA: YPA_1073
            YPN: YPN_2836
            YPP: YPDSF_2532
            YPS: YPTB1195(betA)
            YPI: YpsIP31758_2831(betA)
            SFV: SFV_0322(betA)
            ECA: ECA1746(betA)
            XCC: XCC3404(betA)
            XCB: XC_0760
            XCV: XCV0774(betA) XCV2149
            XAC: XAC0718(betA)
            VVU: VV2_1688
            VVY: VVA0508
            VPA: VPA1112
            PPR: PBPRB1745
            PAE: PA5372(betA)
            PAU: PA14_70940(betA)
            PAP: PSPA7_6157(betA)
            PPU: PP_5064(betA)
            PST: PSPTO_0443(betA)
            PSB: Psyr_4732
            PSP: PSPPH_4766(betA)
            PFL: PFL_5768(betA)
            PFO: Pfl_5244
            PEN: PSEEN0291 PSEEN0372(betA) PSEEN2583
            PAR: Psyc_0728(betA)
            PCR: Pcryo_0874
            ACI: ACIAD1008(betA)
            SDN: Sden_0715
            SFR: Sfri_1946
            SBL: Sbal_1325
            SSE: Ssed_1119
            SPL: Spea_1007
            CPS: CPS_1334(betA1) CPS_4010(betA2)
            PHA: PSHAb0261(betC) PSHAb0418(betA)
            PAT: Patl_2587
            PIN: Ping_2072
            MAQ: Maqu_3840
            NOC: Noc_1796
            HCH: HCH_00851(betA)
            CSA: Csal_1514 Csal_2458
            MMW: Mmwyl1_3136
            RSO: RSc3345(betA)
            REU: Reut_A3372 Reut_B5834 Reut_C6373
            REH: H16_A0233(betA2) H16_A1655(betA3) H16_A3663(betA4) H16_A3737
                 H16_B2131(betA1)
            RME: Rmet_3521
            BMA: BMA2933 BMAA0914(betA)
            BMV: BMASAVP1_0468(betA)
            BML: BMA10299_0179(betA)
            BMN: BMA10247_A1428(betA)
            BXE: Bxe_A0016 Bxe_A3525 Bxe_B0698 Bxe_B1592
            BUR: Bcep18194_A3263 Bcep18194_A4369 Bcep18194_A4914
                 Bcep18194_A6419 Bcep18194_B0530 Bcep18194_B0553
                 Bcep18194_B1169 Bcep18194_B2005 Bcep18194_B2513
                 Bcep18194_B2838 Bcep18194_B3063 Bcep18194_B3144
                 Bcep18194_B3158 Bcep18194_C6778 Bcep18194_C6848
                 Bcep18194_C7343 Bcep18194_C7484
            BCN: Bcen_3268
            BCH: Bcen2424_0082 Bcen2424_5100
            BAM: Bamb_0073 Bamb_4512
            BPS: BPSL3419 BPSS1355(betA)
            BPM: BURPS1710b_0201(betA) BURPS1710b_A0377(betA)
            BPL: BURPS1106A_A1837(betA)
            BPD: BURPS668_A1925(betA)
            BTE: BTH_I3332 BTH_II0331 BTH_II1072(betA) BTH_II2161
            PNU: Pnuc_0353
            BPA: BPP0111 BPP3848
            BBR: BB0111 BB4316
            RFR: Rfer_3918
            POL: Bpro_0229
            VEI: Veis_3226
            MPT: Mpe_A3803
            HAR: HEAR3420(betA)
            MMS: mma_2811 mma_3641(betA)
            MLO: mll7609
            SME: SMc00093(betA)
            SMD: Smed_3164
            ATU: Atu0830(betA)
            ATC: AGR_C_1517
            RET: RHE_CH01136(betA) RHE_PB00070
            RLE: RL1270(betA) pRL110491 pRL120289 pRL120764
            BME: BMEI1380 BMEI1381
            BMF: BAB1_0577
            BMS: BR0553(betA)
            BOV: BOV_0554(betA)
            OAN: Oant_0877
            BJA: blr2397
            BRA: BRADO1398 BRADO1873(betA) BRADO5760
            BBT: BBta_2190(betA) BBta_6015(betA) BBta_6272 BBta_6705
            RPA: RPA2619
            RPC: RPC_2481
            RPE: RPE_2605 RPE_3915
            CCR: CC_2642
            SIL: SPO1088(betA) SPO2359
            SIT: TM1040_1882 TM1040_3389
            RSP: RSP_2184(betA)
            RSH: Rsph17029_0856
            JAN: Jann_1492
            RDE: RD1_0512(betA) RD1_2024(betA) RD1_4099
            HNE: HNE_2666(betA)
            GBE: GbCGDNIH1_1607
            SAU: SA2405(betA)
            SAV: SAV2612(betA)
            SAM: MW2531(betA)
            SAR: SAR2690(cudB)
            SAS: SAS2497
            SAC: SACOL2627(betA)
            SAB: SAB2486c(cudB)
            SAA: SAUSA300_2545(betA)
            SAO: SAOUHSC_02932
            SEP: SE2165
            SER: SERP2176(betA)
            SHA: SH0429(betA)
            SSP: SSP0196
            MAV: MAV_4980
            MSM: MSMEG_0281 MSMEG_3431 MSMEG_3432 MSMEG_3444 MSMEG_5305
            MMC: Mmcs_2628
            CDI: DIP2202(betA)
            CJK: jk1189(betA)
            RHA: RHA1_ro01725 RHA1_ro01805 RHA1_ro01877 RHA1_ro06079
            SCO: SCO4829(SC2A6.14)
            SMA: SAV3433 SAV6946
            ART: Arth_3726
            AAU: AAur_3606(betA)
            SEN: SACE_2592 SACE_2760 SACE_4202 SACE_4210 SACE_5444
            STP: Strop_1639
            AVA: Ava_C0102
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.1
            ExPASy - ENZYME nomenclature database: 1.1.99.1
            ExplorEnz - The Enzyme Database: 1.1.99.1
            ERGO genome analysis and discovery system: 1.1.99.1
            BRENDA, the Enzyme Database: 1.1.99.1
            CAS: 9028-67-5
///
ENTRY       EC 1.1.99.2                 Enzyme
NAME        2-hydroxyglutarate dehydrogenase;
            alpha-ketoglutarate reductase;
            alpha-hydroxyglutarate dehydrogenase;
            L-alpha-hydroxyglutarate dehydrogenase;
            hydroxyglutaric dehydrogenase;
            alpha-hydroxyglutarate oxidoreductase;
            L-alpha-hydroxyglutarate:NAD+ 2-oxidoreductase;
            alpha-hydroxyglutarate dehydrogenase (NAD+ specific);
            (S)-2-hydroxyglutarate:(acceptor) 2-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     (S)-2-hydroxyglutarate:acceptor 2-oxidoreductase
REACTION    (S)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced
            acceptor [RN:R00298]
ALL_REAC    R00298 > R03534
SUBSTRATE   (S)-2-hydroxyglutarate [CPD:C03196];
            acceptor [CPD:C00028]
PRODUCT     2-oxoglutarate [CPD:C00026];
            reduced acceptor [CPD:C00030]
REFERENCE   1
  AUTHORS   Weil-Malherbe, H.
  TITLE     The oxidation of l(-)alpha-hydroxyglutaric acid in animal tissues.
  JOURNAL   Biochem. J. 31 (1937) 2080-2094.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K00109  2-hydroxyglutarate dehydrogenase
GENES       HSA: 79944(L2HGDH)
            MMU: 217666(L2hgdh)
            CFA: 480316(L2HGDH)
            GGA: 423573(L2HGDH)
            DME: Dmel_CG10639
            CEL: Y45G12B.3
            DDI: DDBDRAFT_0189439
            FRA: Francci3_1888
            FNU: FN0487
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.2
            ExPASy - ENZYME nomenclature database: 1.1.99.2
            ExplorEnz - The Enzyme Database: 1.1.99.2
            ERGO genome analysis and discovery system: 1.1.99.2
            BRENDA, the Enzyme Database: 1.1.99.2
            CAS: 9028-80-2
///
ENTRY       EC 1.1.99.3                 Enzyme
NAME        gluconate 2-dehydrogenase (acceptor);
            gluconate oxidase;
            gluconate dehydrogenase;
            gluconic dehydrogenase;
            D-gluconate dehydrogenase;
            gluconic acid dehydrogenase;
            2-ketogluconate reductase;
            D-gluconate dehydrogenase, 2-keto-D-gluconate-yielding;
            D-gluconate:(acceptor) 2-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     D-gluconate:acceptor 2-oxidoreductase
REACTION    D-gluconate + acceptor = 2-dehydro-D-gluconate + reduced acceptor
            [RN:R01742]
ALL_REAC    R01742 > R01741
SUBSTRATE   D-gluconate [CPD:C00257];
            acceptor [CPD:C00028]
PRODUCT     2-dehydro-D-gluconate [CPD:C00629];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:6815420]
  AUTHORS   Matsushita K, Shinagawa E, Ameyama M.
  TITLE     D-Gluconate dehydrogenase from bacteria,
            2-keto-D-gluconate-yielding, membrane-bound.
  JOURNAL   Methods. Enzymol. 89 Pt D (1982) 187-93.
REFERENCE   2
  AUTHORS   Ramakrishnan, T. and Campbell, J.J.R.
  TITLE     Gluconic dehydrogenase of Pseudomonas aeruginosa.
  JOURNAL   Biochim. Biophys. Acta 17 (1955) 122-127.
  ORGANISM  Pseudomonas aeruginosa
PATHWAY     PATH: map00030  Pentose phosphate pathway
ORTHOLOGY   KO: K06150  gluconate 2-dehydrogenase
            KO: K06151  gluconate 2-dehydrogenase alpha chain
            KO: K06152  gluconate 2-dehydrogenase gamma chain
GENES       SPE: Spro_1807 Spro_2014 Spro_2015 Spro_2016 Spro_2085 Spro_2136
                 Spro_2137 Spro_2138 Spro_2321 Spro_2335 Spro_2490 Spro_3640
                 Spro_4016
            PAE: PA2264 PA2265
            PPU: PP_3383 PP_3384
            PPF: Pput_1632 Pput_2110 Pput_2375 Pput_2376 Pput_2377
            PFL: PFL_0053 PFL_0054
            PFO: Pfl_0085 Pfl_0086
            PRW: PsycPRwf_2356
            SBM: Shew185_0966
            SPL: Spea_0957
            RME: Rmet_2503 Rmet_2504
            BXE: Bxe_A4094 Bxe_A4095 Bxe_C0230
            BUR: Bcep18194_B1793 Bcep18194_B1794
            BCN: Bcen_4142
            BPA: BPP2079 BPP2080
            BBR: BB1475 BB1476
            CJE: Cj0414 Cj0415
            CJR: CJE0463 CJE0464
            CJU: C8J_0390
            SMD: Smed_0591
            RLE: RL1347(cycG)
            OAN: Oant_0689 Oant_2696 Oant_3607 Oant_3608
            XAU: Xaut_1071 Xaut_1761
            RSQ: Rsph17025_1042
            GOX: GOX1231 GOX1232
            ACR: Acry_0043
            SUS: Acid_5751
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.3
            ExPASy - ENZYME nomenclature database: 1.1.99.3
            ExplorEnz - The Enzyme Database: 1.1.99.3
            ERGO genome analysis and discovery system: 1.1.99.3
            BRENDA, the Enzyme Database: 1.1.99.3
            CAS: 9028-81-3
///
ENTRY       EC 1.1.99.4                 Enzyme
NAME        dehydrogluconate dehydrogenase;
            ketogluconate dehydrogenase;
            alpha-ketogluconate dehydrogenase;
            2-keto-D-gluconate dehydrogenase;
            2-oxogluconate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     2-dehydro-D-gluconate:acceptor 2-oxidoreductase
REACTION    2-dehydro-D-gluconate + acceptor = 2,5-didehydro-D-gluconate +
            reduced acceptor [RN:R07153]
ALL_REAC    R07153;
            (other) R00849
SUBSTRATE   2-dehydro-D-gluconate [CPD:C00629];
            acceptor [CPD:C00028]
PRODUCT     2,5-didehydro-D-gluconate [CPD:C02780];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016];
            Flavoprotein [CPD:C06411]
COMMENT     A flavoprotein.
REFERENCE   1  [PMID:13395514]
  AUTHORS   DATTA AG, KATZNELSON H.
  TITLE     The oxidation of 2-ketogluconate by a partially purified enzyme from
            Acetobactor melanogenum.
  JOURNAL   Arch. Biochem. Biophys. 65 (1956) 576-8.
  ORGANISM  Acetobacter melanogenum
REFERENCE   2
  AUTHORS   Shinagawa, E. and Ameyama, M.
  TITLE     2-Keto-D-gluconate dehydrogenase from Gluconobacter melanogenus,
            membrane-bound.
  JOURNAL   Methods Enzymol. 89 (1982) 194-198.
  ORGANISM  Gluconobacter melanogenus
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.4
            ExPASy - ENZYME nomenclature database: 1.1.99.4
            ExplorEnz - The Enzyme Database: 1.1.99.4
            ERGO genome analysis and discovery system: 1.1.99.4
            BRENDA, the Enzyme Database: 1.1.99.4
            CAS: 9028-82-4
///
ENTRY       EC 1.1.99.5                 Enzyme
NAME        glycerol-3-phosphate dehydrogenase;
            sn-glycerol-3-phosphate dehydrogenase;
            L-glycerol-3-phosphate dehydrogenase;
            alpha-glycerophosphate dehydrogenase;
            L-3-glycerophosphate-ubiquinone oxidoreductase;
            sn-glycerol 3-phosphate oxidase;
            dehydrogenase, glycerol phosphate (acceptor);
            glycerophosphate dehydrogenase;
            glycerol phosphate dehydrogenase;
            NAD+-independent glycerol phosphate dehydrogenase;
            glycerol 3-phosphate cytochrome c reductase;
            flavoprotein-linked L-glycerol 3-phosphate dehydrogenase;
            alpha-glycerophosphate dehydrogenase (acceptor);
            FAD-dependent glycerol-3-phosphate dehydrogenase;
            FAD-linked glycerol 3-phosphate dehydrogenase;
            glycerol phosphate dehydrogenase (FAD);
            glycerol phosphate dehydrogenase (acceptor);
            FAD-dependent sn-glycerol-3-phosphate dehydrogenase;
            L-glycerophosphate dehydrogenase;
            glycerol-3-phosphate dehydrogenase (flavin-linked);
            flavin-linked glycerol-3-phosphate dehydrogenase;
            pyridine nucleotide-independent L-glycerol 3-phosphate
            dehydrogenase;
            DL-glycerol 3-phosphate oxidase;
            FAD-linked L-glycerol-3-phosphate dehydrogenase;
            sn-glycerol-3-phosphate:(acceptor) 2-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     sn-glycerol-3-phosphate:acceptor 2-oxidoreductase
REACTION    sn-glycerol 3-phosphate + acceptor = glycerone phosphate + reduced
            acceptor [RN:R00849]
ALL_REAC    R00849 > R00848
SUBSTRATE   sn-glycerol 3-phosphate [CPD:C00093];
            acceptor [CPD:C00028]
PRODUCT     glycerone phosphate [CPD:C00111];
            reduced acceptor [CPD:C00030]
REFERENCE   1
  AUTHORS   Ringler, R.L.
  TITLE     Studies on the mitochondrial alpha-glycerophosphate dehydrogenase.
            II. Extraction and partial purification of the dehydrogenase from
            pig brain.
  JOURNAL   J. Biol. Chem. 236 (1961) 1192-1198.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00110  glycerol-3-phosphate dehydrogenase
            KO: K00111  glycerol-3-phosphate dehydrogenase
            KO: K00112  glycerol-3-phosphate dehydrogenase subunit B
            KO: K00113  glycerol-3-phosphate dehydrogenase subunit C
GENES       HSA: 2820(GPD2)
            MMU: 14571(Gpd2)
            RNO: 25062(Gpd2)
            GGA: 424321(GPD2)
            XLA: 444438(MGC83596)
            SPU: 576660(LOC576660)
            DME: Dmel_CG2137 Dmel_CG5526(Dhc36C) Dmel_CG7311
                 Dmel_CG8256(l(2)k05713)
            CEL: T25G3.4
            ATH: AT3G10370
            OSA: 4335210
            CME: CML209C
            SCE: YIL155C(GUT2)
            AGO: AGOS_AFR295W
            PIC: PICST_68764(GUT2)
            CGR: CAGL0H06699g
            SPO: SPCC1223.03c(gut2)
            ANI: AN1396.2
            AFM: AFUA_1G08810
            AOR: AO090005001646
            CNE: CNC04310 CNC04320
            UMA: UM01619.1
            ECU: ECU10_0870
            DDI: DDBDRAFT_0185769
            PFA: MAL3P2.24
            TAN: TA17925
            TPV: TP03_0730
            TET: TTHERM_00426250
            TBR: Tb11.02.5280 Tb927.1.1130
            TCR: 507949.130 511151.90 511423.70
            LMA: LmjF20.0430 LmjF28.0240
            EHI: 285.t00008 328.t00011
            ECO: b2241(glpA) b2242(glpB) b2243(glpC) b3426(glpD)
            ECJ: JW2235(glpA) JW2236(glpB) JW2237(glpC) JW3389(glpD)
            ECE: Z3499(glpA) Z3500(glpB) Z3501(glpC) Z4786(glpD)
            ECS: ECs3126 ECs3127 ECs3128 ECs4269
            ECC: c2782(glpA) c2783(glpB) c2784(glpC) c4203(glpD)
            ECI: UTI89_C2521(glpA) UTI89_C2522(glpB) UTI89_C2523(glpC)
                 UTI89_C3926(glpD)
            ECP: ECP_2283 ECP_2284 ECP_2285 ECP_3511
            ECV: APECO1_3041(glpD) APECO1_4318(glpC) APECO1_4319(glpB)
                 APECO1_4320(glpA)
            ECW: EcE24377A_2539(glpA) EcE24377A_2540(glpB)
                 EcE24377A_3902(glpD)
            ECX: EcHS_A2382(glpA) EcHS_A2383(glpB) EcHS_A2384(glpC)
                 EcHS_A3623(glpD)
            STY: STY2513(glpA) STY2514(glpB) STY2515(glpC) STY4277(glpD)
            STT: t0578(glpC) t0579(glpB) t0580(glpA) t3987(glpD)
            SPT: SPA0578(glpC) SPA0579(glpB) SPA0580(glpA) SPA3384(glpD)
            SEC: SC2287(glpA) SC2288(glpB) SC2289(glpC) SC3457(glpD)
            STM: STM2284(glpA) STM2285(glpB) STM2286(glpC) STM3526(glpD)
            YPE: YPO3824(glpC) YPO3825(glpB) YPO3826(glpA) YPO3937(glpD)
            YPK: y0404(glpA) y0405(glpB) y0406(glpC) y3891(glpD)
            YPM: YP_3222(glpA) YP_3223(glpB) YP_3224(glpC) YP_3299(glpD)
            YPA: YPA_0196 YPA_0197 YPA_0198 YPA_3766
            YPN: YPN_0138 YPN_0139 YPN_0140 YPN_3585
            YPP: YPDSF_3442
            YPS: YPTB0209(glpA) YPTB0210(glpB) YPTB0211(glpC) YPTB3782(glpD)
            YPI: YpsIP31758_0227(glpA) YpsIP31758_0228(glpB)
                 YpsIP31758_0229(glpC) YpsIP31758_4000(glpD)
            SFL: SF2323(glpA) SF2324(glpB) SF2325(glpC) SF3448(glpD)
            SFX: S2456(glpA) S2457(glpB) S2458(glpC) S4316(glpD)
            SFV: SFV_2313(glpA) SFV_2314(glpB) SFV_2315(glpC) SFV_3433(glpD)
            SSN: SSON_2302(glpA) SSON_2303(glpB) SSON_2304(glpC)
                 SSON_3663(glpD)
            SBO: SBO_2051(glpC) SBO_2052(glpB) SBO_2053(glpA) SBO_3414(glpD)
            SDY: SDY_2436(glpA) SDY_2437(glpB) SDY_2438(glpC) SDY_3649(glpD)
            ECA: ECA4141(glpD) ECA4163(glpC) ECA4164(glpB) ECA4165(glpA)
            PLU: plu0194(glpD)
            SGL: SG2329
            ENT: Ent638_2806
            SPE: Spro_0201
            HIN: HI0683(glpC) HI0684(glpB) HI0685(glpA)
            HIT: NTHI0805(glpC) NTHI0806(glpB) NTHI0808(glpA)
            HIP: CGSHiEE_08755(glpA) CGSHiEE_08760
            HIQ: CGSHiGG_06720 CGSHiGG_06730(glpA)
            HDU: HD1157(glpA) HD1158(glpB) HD1160(glpC)
            HSO: HS_0512(glpA) HS_0513(glpB) HS_0514(glpC)
            PMU: PM1440(glpC) PM1441(glpB) PM1442(glpA)
            MSU: MS1993(glpA) MS1994(glpB) MS1995(glpC)
            APL: APL_0379(glpA) APL_0380(glpB) APL_0381(glpC)
            ASU: Asuc_0204
            XFA: XF2266
            XFT: PD1302(glpD)
            XCC: XCC0360(glpD)
            XCB: XC_0372
            XCV: XCV0374(glpD)
            XAC: XAC0360(glpD)
            VCH: VCA0657 VCA0747 VCA0748 VCA0749
            VCO: VC0395_0601(glpD) VC0395_0686(glpA) VC0395_0687(glpB)
            VVU: VV1_1785 VV2_0010 VV2_0011 VV2_0012
            VVY: VV2626 VVA0519 VVA0520 VVA0521
            VPA: VP2388
            VFI: VFA0239 VFA0248 VFA0249 VFA0250
            PPR: PBPRA0160(glpD) PBPRA1370(glpC) PBPRA1371 PBPRA1372
            PAE: PA3025 PA3584(glpD)
            PAU: PA14_17930(glpD) PA14_24950(glpD2)
            PPU: PP_1073(glpD)
            PST: PSPTO_4170(glpD)
            PSB: Psyr_3907
            PSP: PSPPH_3901(glpD)
            PFL: PFL_2768 PFL_4870
            PFO: Pfl_4534
            PEN: PSEEN1195(glpD)
            PCR: Pcryo_0014
            ACI: ACIAD2844(glpD)
            SON: SO_0978
            SDN: Sden_0369
            SHE: Shewmr4_0816
            SHM: Shewmr7_3207
            SHN: Shewana3_3310
            PHA: PSHAa0189(glpD)
            SDE: Sde_1482
            CBU: CBU_0931(glpD)
            CBD: COXBU7E912_1143(glpD)
            LPN: lpg1413(glpD)
            LPF: lpl1364(glpD)
            LPP: lpp1368(glpD)
            FTU: FTT0132(glpA)
            FTF: FTF0132(glpA)
            FTL: FTL_1756
            FTH: FTH_1696(glpA)
            FTN: FTN_1584(glpD)
            HCH: HCH_04624(glpD) HCH_06964
            CSA: Csal_2106
            ABO: ABO_1408(glpD)
            AHA: AHA_1652 AHA_2460 AHA_2461 AHA_2462(glpC)
            CVI: CV_0254(glpD)
            RSO: RSc3045(glpD)
            REU: Reut_A2214
            REH: H16_A2508 H16_B1198
            RME: Rmet_2239 Rmet_5444
            BMA: BMA0241(glpD)
            BMV: BMASAVP1_A2705(glpD)
            BML: BMA10299_A2372(glpD)
            BMN: BMA10247_2453(glpD)
            BXE: Bxe_A0639
            BPS: BPSL0688(glpD)
            BPM: BURPS1710b_0907(glpD)
            BPL: BURPS1106A_0740(glpD)
            BPD: BURPS668_0726(glpD)
            BTE: BTH_I0600
            BPE: BP2644
            BPA: BPP3097
            BBR: BB3060
            RFR: Rfer_2333 Rfer_3670
            POL: Bpro_0484
            MPT: Mpe_A3664
            MMS: mma_3609(glpD)
            NEU: NE0370(eryB)
            NET: Neut_1770
            EBA: ebA4463
            AZO: azo2750(glpA)
            DAR: Daro_1921
            NIS: NIS_0367
            SUN: SUN_2092
            GSU: GSU2761
            GME: Gmet_1677
            PCA: Pcar_0048
            DVU: DVU1939 DVU1940 DVU3132
            DVL: Dvul_1229
            DDE: Dde_0408 Dde_3733
            LIP: LI1084 LI1085 LI1086(glpA)
            BBA: Bd0208(glpD)
            ADE: Adeh_2531 Adeh_2532
            MXA: MXAN_7329(glpD)
            SAT: SYN_02446
            SFU: Sfum_3498 Sfum_3499
            PUB: SAR11_0400(glpC)
            MLO: mll0710 mlr7270
            MES: Meso_1591
            SME: SMb20499 SMc01620(eryB) SMc02520(glpD)
            ATU: Atu3578(glpD) Atu3876(glpD) Atu3897(glpD)
            ATC: AGR_L_1902(glpD) AGR_L_1938 AGR_L_2503
            RET: RHE_PB00019(glpD) RHE_PB00073
            RLE: pRL120197 pRL120205(eryB) pRL120761 pRL90074(glpD)
            BME: BMEI1749 BMEII0429
            BMF: BAB1_0200(glpD) BAB2_0371
            BMS: BR0200(glpD) BRA0865(eryB)
            BMB: BruAb1_0195(glpD) BruAb2_0367(eryB)
            BOV: BOV_0192(glpD) BOV_A0812(eryB)
            BJA: bll7106(glpD) blr2436(glpD)
            BRA: BRADO1214(glpD) BRADO1908(glpD) BRADO4792(glpD)
            BBT: BBta_2221(glpD) BBta_3233(glpD) BBta_6839(glpD)
            RPA: RPA4410(glpD)
            RPB: RPB_4217
            RPC: RPC_1361
            RPD: RPD_1035 RPD_4069
            RPE: RPE_1378
            NWI: Nwi_2990
            NHA: Nham_1090
            BHE: BH08080(glpD)
            SIL: SPO0732(glpD)
            SIT: TM1040_1192 TM1040_2206
            RSP: RSP_2670(glpD)
            RDE: RD1_2884(glpD) RD1_3631(glpD)
            SAL: Sala_0189
            ELI: ELI_03510
            GOX: GOX2088 GOX2215
            RRU: Rru_A1508
            MGM: Mmc1_2531
            ABA: Acid345_3314 Acid345_3694
            SUS: Acid_5520
            BSU: BG10188(glpD)
            BHA: BH1095(glpD)
            BAN: BA1027(glpD)
            BAR: GBAA1027(glpD)
            BAA: BA_1587
            BAT: BAS0961
            BCE: BC1036
            BCA: BCE_1126(glpD)
            BCZ: BCZK0939(glpD)
            BTK: BT9727_0948(glpD)
            BLI: BL02902(glpD)
            BLD: BLi00996(glpD)
            BCL: ABC1257(glpD) ABC1498
            BAY: RBAM_009560(glpD)
            BPU: BPUM_0884(glpD)
            OIH: OB2471
            GKA: GK2153
            SAU: SA1142(glpD)
            SAV: SAV1302(glpD)
            SAM: MW1184(glpD)
            SAR: SAR1276(glpD)
            SAS: SAS1234
            SAC: SACOL1321(glpD)
            SAB: SAB1162(glpD) SAB1336c(gpsA)
            SAA: SAUSA300_1193(glpD)
            SAO: SAOUHSC_01278
            SEP: SE0979
            SER: SERP0868(glpD)
            SHA: SH1608(glpD)
            SSP: SSP1459
            LMO: lmo1293(glpD)
            LMF: LMOf2365_1310(glpD)
            LIN: lin1331(glpD)
            LWE: lwe1308(glpD)
            LLC: LACR_1486
            LLM: llmg_1098(glpD)
            SPZ: M5005_Spy_1380(glpO)
            SPB: M28_Spy1423(glpO)
            LSA: LSA0650(glpD)
            LCA: LSEI_0661
            STH: STH1984 STH1985 STH427
            CAC: CAC1322(glpA)
            CPE: CPE2551(glpA)
            CTC: CTC01808 CTC02436
            CNO: NT01CX_0612
            CBO: CBO1068(glpA)
            CKL: CKL_1357(gpsA)
            CHY: CHY_1836(glpC) CHY_1837(glpB) CHY_1838(glpA)
            DRM: Dred_2843
            TTE: TTE2001
            MGE: MG_039
            MPN: MPN051(glpD)
            MPU: MYPU_2640(glpD)
            MPE: MYPE6370(glpA)
            MGA: MGA_0646
            MMO: MMOB2950(glpD)
            MHY: mhp606(glpD)
            MHJ: MHJ_0588(glpD)
            MHP: MHP7448_0588(glpD)
            MCP: MCAP_0219
            MTU: Rv2249c(glpD1) Rv3302c(glpD2)
            MTC: MT2309(glpD-1) MT3401(glpD-2)
            MBO: Mb2273c(glpD1) Mb3330c(glpD2)
            MBB: BCG_2267c(glpD1) BCG_3331c(glpD2_1) BCG_3367c(glpD2_2)
            MLE: ML0713(glpD)
            MPA: MAP2002c(glpD1) MAP3423c(glpD2)
            MAV: MAV_2188 MAV_4278
            MSM: MSMEG_1736 MSMEG_4332 MSMEG_6761
            MMC: Mmcs_1250 Mmcs_3372
            CGL: NCgl1584(cgl1646)
            CGB: cg1853(glpD)
            CDI: DIP2237(glpD)
            NFA: nfa13430(glpD2) nfa9720(glpD)
            RHA: RHA1_ro06265(glpA) RHA1_ro06762
            SCO: SCO0670(glpD) SCO1661(SCI52.03) SCO4774(SCD63.06)
                 SCO7005(SC8F11.31)
            SMA: SAV5003(glpD) SAV6663(gpd)
            LXX: Lxx19830(glpD)
            CMI: CMM_1823(glpD)
            AAU: AAur_2249(glpD)
            PAC: PPA2248 PPA2249 PPA2250
            TFU: Tfu_2593
            FRA: Francci3_0938 Francci3_0941
            FAL: FRAAL1573(glpA)
            ACE: Acel_0029
            SEN: SACE_0658(glpD) SACE_3958(glpD) SACE_6515(glpD-2)
            FNU: FN0183
            RBA: RB3763(glpA)
            BBU: BB0243(glpA)
            BGA: BG0245(glpA)
            BAF: BAPKO_0252(glpA)
            TDE: TDE0134 TDE2643
            LIL: LA2236 LA2261(glpD)
            LIC: LIC11675 LIC11699(glpD)
            LBJ: LBJ_1380(glpA-1)
            LBL: LBL_1605(glpA-1)
            SYN: sll1085(glpD)
            SYW: SYNW1954
            SYG: sync_0568(glpA)
            SYR: SynRCC307_1381
            SYX: SynWH7803_0546
            SRU: SRU_1463(glpA) SRU_2437(glpA)
            CHU: CHU_1004(glpD)
            FJO: Fjoh_4885
            RRS: RoseRS_3300
            RCA: Rcas_4112
            DRA: DR_1019
            DGE: Dgeo_2521
            TTJ: TTHB143
            TMA: TM1432
            MBU: Mbur_0470
            AFU: AF1328(glpA)
            HAL: VNG1070Gm(gpdA1) VNG1969G(gpdA2) VNG1971G(gpdB)
                 VNG1972G(gpdC)
            HMA: rrnAC0554(gpdA) rrnAC0555(gpdB) rrnAC0556(gpdC)
                 rrnAC1955(glpA)
            HWA: HQ1734A(gpdA) HQ1735A(gpdB) HQ1736A(gpdC) HQ2675A(gpdA)
            TAC: Ta0633
            TVO: TVN0840
            PTO: PTO1486
            PAB: PAB0183(glpA)
            PFU: PF2005
            TKO: TK1393
            APE: APE_0309.1
            SSO: SSO2526(glpA) SSO2643(glpC)
            STO: ST2369
            SAI: Saci_1118 Saci_2032 Saci_2273
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.5
            ExPASy - ENZYME nomenclature database: 1.1.99.5
            ExplorEnz - The Enzyme Database: 1.1.99.5
            ERGO genome analysis and discovery system: 1.1.99.5
            BRENDA, the Enzyme Database: 1.1.99.5
            CAS: 9001-49-4
///
ENTRY       EC 1.1.99.6                 Enzyme
NAME        D-2-hydroxy-acid dehydrogenase;
            D-2-hydroxy acid dehydrogenase;
            (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     (R)-2-hydroxy-acid:acceptor 2-oxidoreductase
REACTION    (R)-lactate + acceptor = pyruvate + reduced acceptor [RN:R00297]
ALL_REAC    R00297
SUBSTRATE   (R)-lactate [CPD:C00256];
            acceptor [CPD:C00028]
PRODUCT     pyruvate [CPD:C00022];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016];
            Zinc [CPD:C00038]
COMMENT     A zinc flavoprotein (FAD). Acts on a variety of (R)-2-hydroxy acids.
REFERENCE   1  [PMID:13901630]
  AUTHORS   GREGOLIN C, SINGER TP, KEARNEY EB, BOERI E.
  TITLE     The formation and enzymatic properties of the various lactic
            dehydrogenases of yeast.
  JOURNAL   Ann. N. Y. Acad. Sci. 94 (1961) 780-97.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2
  AUTHORS   Nygaard, A.P.
  TITLE     D(-)-Lactate cytochrome c reductase, a flavoprotein from yeast.
  JOURNAL   J. Biol. Chem. 236 (1961) 920-925.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Tubbs, P.K. and Greville, G.D.
  TITLE     Dehydrogenation of D-lactate by a soluble enzyme from kidney
            mitochondria.
  JOURNAL   Biochim. Biophys. Acta 34 (1959) 290-291.
  ORGANISM  rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.6
            ExPASy - ENZYME nomenclature database: 1.1.99.6
            ExplorEnz - The Enzyme Database: 1.1.99.6
            ERGO genome analysis and discovery system: 1.1.99.6
            BRENDA, the Enzyme Database: 1.1.99.6
            CAS: 9028-83-5
///
ENTRY       EC 1.1.99.7                 Enzyme
NAME        lactate---malate transhydrogenase;
            malate-lactate transhydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     (S)-lactate:oxaloacetate oxidoreductase
REACTION    (S)-lactate + oxaloacetate = pyruvate + malate [RN:R01447]
ALL_REAC    R01447
SUBSTRATE   (S)-lactate [CPD:C00186];
            oxaloacetate [CPD:C00036]
PRODUCT     pyruvate [CPD:C00022];
            malate [CPD:C00711]
COFACTOR    Nicotinamide D-ribonucleotide [CPD:C00455]
COMMENT     Catalyses hydrogen transfer from C3 or C4 (S)-2-hydroxy acids to
            2-oxo acids. It contains tightly bound nicotinamide nucleotide in
            its active centre. This prosthetic group cannot be removed without
            denaturation of the protein.
REFERENCE   1  [PMID:4289051]
  AUTHORS   Allen SH.
  TITLE     The isolation and characterization of malate-lactate
            transhydrogenase from Micrococcus lactilyticus.
  JOURNAL   J. Biol. Chem. 241 (1966) 5266-75.
  ORGANISM  Micrococcus lactilyticus
REFERENCE   2  [PMID:4333516]
  AUTHORS   Allen SH, Patil JR.
  TITLE     Studies on the structure and mechanism of action of the
            malate-lactate transhydrogenase.
  JOURNAL   J. Biol. Chem. 247 (1972) 909-16.
  ORGANISM  Micrococcus lactilyticus, Veillonella alcalescens
PATHWAY     PATH: map00620  Pyruvate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.7
            ExPASy - ENZYME nomenclature database: 1.1.99.7
            ExplorEnz - The Enzyme Database: 1.1.99.7
            ERGO genome analysis and discovery system: 1.1.99.7
            BRENDA, the Enzyme Database: 1.1.99.7
            CAS: 9077-15-0
///
ENTRY       EC 1.1.99.8                 Enzyme
NAME        alcohol dehydrogenase (acceptor);
            primary alcohol dehydrogenase;
            MDH;
            quinohemoprotein alcohol dehydrogenase;
            quinoprotein alcohol dehydrogenase;
            quinoprotein ethanol dehydrogenase;
            alcohol:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     alcohol:acceptor oxidoreductase
REACTION    a primary alcohol + acceptor = an aldehyde + reduced acceptor
            [RN:R00639]
ALL_REAC    R00639 > R01146 R05062 R05121 R05198 R05285;
            (other) R02479
SUBSTRATE   primary alcohol [CPD:C00226];
            acceptor [CPD:C00028]
PRODUCT     aldehyde [CPD:C00071];
            reduced acceptor [CPD:C00030]
COFACTOR    PQQ [CPD:C00113]
COMMENT     A quinoprotein. Acts on a wide range of primary alcohols, including
            methanol [cf. EC 1.1.99.20 alkan-1-ol dehydrogenase (acceptor)].
REFERENCE   1
  AUTHORS   Ameyama, M. and Adachi, O.
  TITLE     Alcohol dehydrogenase from acetic acid bacteria, membrane-bound.
  JOURNAL   Methods Enzymol. 89 (1982) 450-457.
  ORGANISM  Acetobacter aceti, Gluconobacter oxydans subsp. suboxydans
REFERENCE   2  [PMID:6058112]
  AUTHORS   Anthony C, Zatman LJ.
  TITLE     The microbial oxidation of methanol. Purification and properties of
            the alcohol dehydrogenase of Pseudomonas sp. M27.
  JOURNAL   Biochem. J. 104 (1967) 953-9.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:520586]
  AUTHORS   Duine JA, Frank J, van Zeeland JK.
  TITLE     Glucose dehydrogenase from Acinetobacter calcoaceticus: a
            'quinoprotein'.
  JOURNAL   FEBS. Lett. 108 (1979) 443-6.
  ORGANISM  Acinetobacter calcoaceticus
REFERENCE   4  [PMID:6250827]
  AUTHORS   Duine JA, Frank J, Verwiel PE.
  TITLE     Structure and activity of the prosthetic group of methanol
            dehydrogenase.
  JOURNAL   Eur. J. Biochem. 108 (1980) 187-92.
  ORGANISM  Acinetobacter calcoaceticus
REFERENCE   5  [PMID:471057]
  AUTHORS   Salisbury SA, Forrest HS, Cruse WB, Kennard O.
  TITLE     A novel coenzyme from bacterial primary alcohol dehydrogenases.
  JOURNAL   Nature. 280 (1979) 843-4.
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00631  1,2-Dichloroethane degradation
            PATH: map00640  Propanoate metabolism
            PATH: map00650  Butanoate metabolism
            PATH: map00680  Methane metabolism
ORTHOLOGY   KO: K00114  alcohol dehydrogenase (acceptor)
GENES       APL: APL_1859
            XCC: XCC3479(mxaF)
            XCB: XC_0682
            XCV: XCV0708(mxaF) XCV0709(mxaF)
            PAE: PA1982(exaA)
            PPU: PP_2674(qedH)
            PFL: PFL_2216(exaA) PFL_2221(exaA)
            MCA: MCA0299 MCA0779(mxaF) MCA0782(mxaI)
            REU: Reut_A1784 Reut_B4160
            BXE: Bxe_B2427
            MPT: Mpe_A0341 Mpe_A0476 Mpe_A0877 Mpe_A1591 Mpe_A1595 Mpe_A3393
                 Mpe_A3660
            AZO: azo2844(exaA1) azo2972(exaA2) azo2975(exaA3) azo3022(exaA4)
                 azo3865(exaA5)
            DAR: Daro_1023
            MFA: Mfla_0344 Mfla_1717 Mfla_2041
            SME: SMb20173
            BJA: bll7639 blr6207(exaA) blr6213(mxaF')
            BRA: BRADO0123 BRADO1707 BRADO3897 BRADO5480 BRADO5484(mxaF')
            BBT: BBta_2017 BBta_2326 BBta_3937 BBta_5964 BBta_5968(mxaF')
            RPC: RPC_1907
            RPE: RPE_0851 RPE_3136 RPE_3139 RPE_3525
            SIL: SPO1508
            RSP: RSP_2578(xoxF)
            RDE: RD1_0890(moxF)
            HNE: HNE_0129(adhA)
            GOX: GOX1068
            GBE: GbCGDNIH1_0122 GbCGDNIH1_0344 GbCGDNIH1_0347 GbCGDNIH1_0651
                 GbCGDNIH1_1922
            MSM: MSMEG_3726
            SEN: SACE_4449(exaA)
            RBA: RB12562(adh)
STRUCTURES  PDB: 1G72  1H4I  1H4J  1LRW  1W6S  2AD6  2AD7  2AD8  2D0V  4AAH  
                 8ADH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.8
            ExPASy - ENZYME nomenclature database: 1.1.99.8
            ExplorEnz - The Enzyme Database: 1.1.99.8
            ERGO genome analysis and discovery system: 1.1.99.8
            UM-BBD (Biocatalysis/Biodegradation Database): 1.1.99.8
            BRENDA, the Enzyme Database: 1.1.99.8
            CAS: 37205-43-9
///
ENTRY       EC 1.1.99.9                 Enzyme
NAME        pyridoxine 5-dehydrogenase;
            pyridoxal-5-dehydrogenase;
            pyridoxol 5-dehydrogenase;
            pyridoxin 5-dehydrogenase;
            pyridoxine dehydrogenase;
            pyridoxine 5'-dehydrogenase;
            pyridoxine:(acceptor) 5-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     pyridoxine:acceptor 5-oxidoreductase
REACTION    pyridoxine + acceptor = isopyridoxal + reduced acceptor [RN:R07154]
ALL_REAC    R07154 > R01910;
            (other) R00639
SUBSTRATE   pyridoxine [CPD:C00314];
            acceptor [CPD:C00028]
PRODUCT     isopyridoxal [CPD:C06051];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016];
            PQQ [CPD:C00113]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:5769992]
  AUTHORS   Sundaram TK, Snell EE.
  TITLE     The bacterial oxidation of vitamin B6. V. The enzymatic formation of
            pyridoxal and isopyridoxal from pyridoxine.
  JOURNAL   J. Biol. Chem. 244 (1969) 2577-84.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00750  Vitamin B6 metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.9
            ExPASy - ENZYME nomenclature database: 1.1.99.9
            ExplorEnz - The Enzyme Database: 1.1.99.9
            ERGO genome analysis and discovery system: 1.1.99.9
            BRENDA, the Enzyme Database: 1.1.99.9
            CAS: 9023-39-6
///
ENTRY       EC 1.1.99.10                Enzyme
NAME        glucose dehydrogenase (acceptor);
            glucose dehydrogenase (Aspergillus);
            glucose dehydrogenase (decarboxylating);
            D-glucose:(acceptor) 1-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     D-glucose:acceptor 1-oxidoreductase
REACTION    D-glucose + acceptor = D-glucono-1,5-lactone + reduced acceptor
            [RN:R00305]
ALL_REAC    R00305
SUBSTRATE   D-glucose [CPD:C00031];
            acceptor [CPD:C00028]
PRODUCT     D-glucono-1,5-lactone [CPD:C00198];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016]
COMMENT     A glycoprotein containing one mole of FAD per mole of enzyme.
            2,6-Dichloroindophenol can act as acceptor
REFERENCE   1  [PMID:6034674]
  AUTHORS   Bak TG.
  TITLE     Studies on glucose dehydrogenase of Aspergillus oryzae. II.
            Purification and physical and chemical properties.
  JOURNAL   Biochim. Biophys. Acta. 139 (1967) 277-93.
  ORGANISM  Aspergillus oryzae [GN:aor]
PATHWAY     PATH: map00030  Pentose phosphate pathway
ORTHOLOGY   KO: K00115  glucose dehydrogenase (acceptor)
GENES       DME: Dmel_CG1152(Gld)
            BXE: Bxe_B1504 Bxe_C0846
            BJA: blr0367
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.10
            ExPASy - ENZYME nomenclature database: 1.1.99.10
            ExplorEnz - The Enzyme Database: 1.1.99.10
            ERGO genome analysis and discovery system: 1.1.99.10
            BRENDA, the Enzyme Database: 1.1.99.10
            CAS: 37250-84-3
///
ENTRY       EC 1.1.99.11                Enzyme
NAME        fructose 5-dehydrogenase;
            fructose 5-dehydrogenase (acceptor);
            D-fructose dehydrogenase;
            D-fructose:(acceptor) 5-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     D-fructose:acceptor 5-oxidoreductase
REACTION    D-fructose + acceptor = 5-dehydro-D-fructose + reduced acceptor
            [RN:R00873]
ALL_REAC    R00873
SUBSTRATE   D-fructose [CPD:C00095];
            acceptor [CPD:C00028]
PRODUCT     5-dehydro-D-fructose [CPD:C00273];
            reduced acceptor [CPD:C00030]
COMMENT     2,6-Dichloroindophenol can act as acceptor.
REFERENCE   1
  AUTHORS   Ameyama, M. and Adachi, O.
  TITLE     D-Fructose dehydrogenase from Gluconobacter industrius,
            membrane-bound.
  JOURNAL   Methods Enzymol. 89 (1982) 154-159.
  ORGANISM  Gluconobacter industrius
REFERENCE   2  [PMID:6059959]
  AUTHORS   Yamada Y, Aida K, Uemura T.
  TITLE     Enzymatic studies on the oxidation of sugar and sugar alcohol. I.
            Purification and properties of particle-bound fructose
            dehydrogenase.
  JOURNAL   J. Biochem. (Tokyo). 61 (1967) 636-46.
  ORGANISM  Gluconobacter cerinus
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.11
            ExPASy - ENZYME nomenclature database: 1.1.99.11
            ExplorEnz - The Enzyme Database: 1.1.99.11
            ERGO genome analysis and discovery system: 1.1.99.11
            BRENDA, the Enzyme Database: 1.1.99.11
            CAS: 37250-85-4
///
ENTRY       EC 1.1.99.12                Enzyme
NAME        sorbose dehydrogenase;
            L-sorbose:(acceptor) 5-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     L-sorbose:acceptor 5-oxidoreductase
REACTION    L-sorbose + acceptor = 5-dehydro-D-fructose + reduced acceptor
            [RN:R01696]
ALL_REAC    R01696
SUBSTRATE   L-sorbose [CPD:C00247];
            acceptor [CPD:C00028]
PRODUCT     5-dehydro-D-fructose [CPD:C00273];
            reduced acceptor [CPD:C00030]
COMMENT     2,6-Dichloroindophenol can act as acceptor.
REFERENCE   1  [PMID:5354025]
  AUTHORS   Sato K, Yamada Y, Aida K, Uemura T.
  TITLE     Enzymatic studies on the oxidation of sugar and sugar alcohol. 8.
            Particle-bound L-sorbose dehydrogenase from Gluconobacter
            suboxydans.
  JOURNAL   J. Biochem. (Tokyo). 66 (1969) 521-7.
  ORGANISM  Gluconobacter suboxydans
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.12
            ExPASy - ENZYME nomenclature database: 1.1.99.12
            ExplorEnz - The Enzyme Database: 1.1.99.12
            ERGO genome analysis and discovery system: 1.1.99.12
            BRENDA, the Enzyme Database: 1.1.99.12
            CAS: 37250-86-5
///
ENTRY       EC 1.1.99.13                Enzyme
NAME        glucoside 3-dehydrogenase;
            D-glucoside 3-dehydrogenase;
            D-aldohexopyranoside dehydrogenase;
            D-aldohexoside:cytochrome c oxidoreductase;
            D-glucoside 3-dehydrogenase;
            hexopyranoside-cytochrome c oxidoreductase;
            D-aldohexoside:(acceptor) 3-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     D-aldohexoside:acceptor 3-oxidoreductase
REACTION    sucrose + acceptor =
            3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside + reduced
            acceptor [RN:R00808]
ALL_REAC    R00808 > R00807 R06233(G);
            (other) R01680 R06219(G)
SUBSTRATE   sucrose [CPD:C00089];
            acceptor [CPD:C00028]
PRODUCT     3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside [CPD:C05731];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). The enzyme acts on D-glucose, D-galactose,
            D-glucosides and D-galactosides, but D-glucosides react more rapidly
            than D-galactosides.
REFERENCE   1
  AUTHORS   Hayano, K. and Fukui, S.
  TITLE     Purification and properties of 3-ketosucrose-forming enzyme from the
            cells of Agrobacterium tumefaciens.
  JOURNAL   J. Biol. Chem. 242 (1967) 3665-3672.
  ORGANISM  Agrobacterium tumefaciens
PATHWAY     PATH: map00052  Galactose metabolism
            PATH: map00500  Starch and sucrose metabolism
GENES       GFO: GFO_1027
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.13
            ExPASy - ENZYME nomenclature database: 1.1.99.13
            ExplorEnz - The Enzyme Database: 1.1.99.13
            ERGO genome analysis and discovery system: 1.1.99.13
            BRENDA, the Enzyme Database: 1.1.99.13
            CAS: 9031-74-7
///
ENTRY       EC 1.1.99.14                Enzyme
NAME        glycolate dehydrogenase;
            glycolate oxidoreductase;
            glycolic acid dehydrogenase;
            glycolate:(acceptor) 2-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     glycolate:acceptor 2-oxidoreductase
REACTION    glycolate + acceptor = glyoxylate + reduced acceptor [RN:R00476]
ALL_REAC    R00476
SUBSTRATE   glycolate [CPD:C00160];
            acceptor [CPD:C00028]
PRODUCT     glyoxylate [CPD:C00048];
            reduced acceptor [CPD:C00030]
COMMENT     Also acts on (R)-lactate. 2,6-Dichloroindophenol and phenazine
            methosulfate can act as acceptors.
REFERENCE   1  [PMID:4557653]
  AUTHORS   Lord JM.
  TITLE     Glycolate oxidoreductase in Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 267 (1972) 227-37.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
GENES       ECW: EcE24377A_3437(glcF) EcE24377A_3438(glcE)
            ECX: EcHS_A3150(glcF) EcHS_A3151(glcE) EcHS_A3152(glcD)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.14
            ExPASy - ENZYME nomenclature database: 1.1.99.14
            ExplorEnz - The Enzyme Database: 1.1.99.14
            ERGO genome analysis and discovery system: 1.1.99.14
            BRENDA, the Enzyme Database: 1.1.99.14
            CAS: 37368-32-4
///
ENTRY       EC 1.1.99.15      Obsolete  Enzyme
NAME        Transferred to 1.5.1.20
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
COMMENT     Transferred entry: now EC 1.5.1.20, methylenetetrahydrofolate
            reductase [NAD(P)H] (EC 1.1.99.15 created 1978, deleted 1980)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.15
            ExPASy - ENZYME nomenclature database: 1.1.99.15
            ExplorEnz - The Enzyme Database: 1.1.99.15
            ERGO genome analysis and discovery system: 1.1.99.15
            BRENDA, the Enzyme Database: 1.1.99.15
///
ENTRY       EC 1.1.99.16                Enzyme
NAME        malate dehydrogenase (acceptor);
            FAD-dependent malate-vitamin K reductase;
            malate-vitamin K reductase;
            (S)-malate:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     (S)-malate:acceptor oxidoreductase
REACTION    (S)-malate + acceptor = oxaloacetate + reduced acceptor [RN:R00361]
ALL_REAC    R00361 > R01257
SUBSTRATE   (S)-malate [CPD:C00149];
            acceptor [CPD:C00028]
PRODUCT     oxaloacetate [CPD:C00036];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1
  AUTHORS   Imai, D. and Brodie, A.F.
  TITLE     A phospholipid-requiring enzyme, malate-vitamin K reductase.
  JOURNAL   J. Biol. Chem. 248 (1973) 7487-7494.
  ORGANISM  Mycobacterium phlei
REFERENCE   2  [PMID:629992]
  AUTHORS   Imai T.
  TITLE     FAD-dependent malate dehydrogenase, a phospholipid-requiring enzyme
            from Mycobacterium sp. strain Takeo. Purification and some
            properties.
  JOURNAL   Biochim. Biophys. Acta. 523 (1978) 37-46.
  ORGANISM  Mycobacterium sp.
REFERENCE   3  [PMID:234747]
  AUTHORS   Prasada Reddy TL, Suryanarayana Murthy P, Venkitasubramanian TA.
  TITLE     Variations in the pathways of malate oxidation and phosphorylation
            in different species of Mycobacteria.
  JOURNAL   Biochim. Biophys. Acta. 376 (1975) 210-8.
  ORGANISM  Mycobacterium tuberculosis, Mycobacterium smegmatis [GN:msm],
            Mycobacterium phlei
PATHWAY     PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K00116  malate dehydrogenase (acceptor)
GENES       PFA: PFF0815w
            CHO: Chro.80050
            TAN: TA18100 TA21455
            TPV: TP03_0758
            ECO: b2210(mqo)
            ECJ: JW2198(mqo)
            ECE: Z3468(yojH)
            ECS: ECs3099
            ECC: c2751(yojH)
            ECI: UTI89_C2490(mqo)
            ECP: ECP_2252
            ECV: APECO1_4349(mqo)
            ECW: EcE24377A_2509(mqo)
            ECX: EcHS_A2349
            SSN: SSON_2268(yojH)
            SBO: SBO_2097(yojH)
            SDY: SDY_0866(yojH)
            ECA: ECA3082(mqo)
            WBR: WGLp604(yojH)
            SGL: SG1751
            ENT: Ent638_2788
            SPE: Spro_1524
            BFL: Bfl529(mqo)
            BPN: BPEN_548(mqo)
            HDU: HD0165(mqo)
            APL: APL_1414(mqo)
            XFA: XF0942
            XFT: PD1752(yojH)
            PAE: PA3452(mqoA) PA4640(mqoB)
            PAU: PA14_19470(mqoA) PA14_61400(mqoB)
            PAP: PSPA7_1675(mqo2) PSPA7_5289(mqo1)
            PPU: PP_0751(mqo-1) PP_1251(mqo-2) PP_2925(mqo-3)
            PPF: Pput_0779 Pput_1279 Pput_2767
            PST: PSPTO_1136(mqo)
            PSB: Psyr_0976 Psyr_2387
            PSP: PSPPH_1025(mqo1) PSPPH_2545(mqo2)
            PFL: PFL_2427(mqo) PFL_5134(mqo)
            PFO: Pfl_2102 Pfl_4724
            PEN: PSEEN0893(mqo-1) PSEEN2357(mqo-3) PSEEN3748(mqo-4)
                 PSEEN4056(mqo-2)
            PMY: Pmen_3093 Pmen_3677
            ACI: ACIAD1007(mqo)
            MAQ: Maqu_0370 Maqu_1383 Maqu_3398
            TCX: Tcr_1873
            HCH: HCH_04006(mqo)
            CSA: Csal_2579
            MMW: Mmwyl1_3994
            BCI: BCI_0001(mqo)
            CRP: CRP_107
            NME: NMB2096
            NMA: NMA0333(mqo)
            NMC: NMC2076(mqo)
            NGO: NGO1980
            RSO: RSp0814(mqo)
            RME: Rmet_4340
            BUR: Bcep18194_B2950
            BCN: Bcen_4992
            BCH: Bcen2424_3168
            BAM: Bamb_5100
            PNU: Pnuc_1616
            AAV: Aave_1166
            MMS: mma_1695
            MFA: Mfla_0011
            HPY: HP0086
            HPJ: jhp0079
            HPA: HPAG1_0087
            HHE: HH1720
            HAC: Hac_1519
            WSU: WS0776
            TDN: Tmden_1506
            CJE: Cj0393c
            CJR: CJE0442
            CJU: C8J_0368
            CFF: CFF8240_0628
            CCV: CCV52592_1243
            CHA: CHAB381_1634
            CCO: CCC13826_0986
            ABU: Abu_0518(mqo)
            SUN: SUN_0432(mqo)
            ATU: Atu0811(mqo)
            ATC: AGR_C_1485
            BJA: bll0284(mqo)
            RPA: RPA1331(mqoB)
            GOX: GOX2070
            GBE: GbCGDNIH1_1044
            BHA: BH3960
            BAN: BA2974(mqo)
            BAR: GBAA2974(mqo)
            BAA: BA_3480
            BAT: BAS2762
            BCE: BC2959
            BCA: BCE_3011(mqo)
            BCZ: BCZK2692(mqo)
            BCY: Bcer98_2135
            BTK: BT9727_2712(mqo)
            OIH: OB0946
            GKA: GK1396
            SAU: SA2155 SA2400(mqo2)
            SAV: SAV2365 SAV2607(mqo2)
            SAM: MW2286 MW2526(mqo2)
            SAR: SAR2454(mqo1) SAR2685(mqo2)
            SAS: SAS2256 SAS2492
            SAC: SACOL2362(mqo1) SACOL2623(mqo2)
            SAB: SAB2244c(mqo) SAB2480c(mqo)
            SAA: SAUSA300_2312(mqo) SAUSA300_2541(mqo)
            SAO: SAOUHSC_02647 SAOUHSC_02927
            SAJ: SaurJH9_2389 SaurJH9_2629
            SAH: SaurJH1_2435 SaurJH1_2683
            SEP: SE0157 SE0266 SE1943 SE2158
            SER: SERP1955(mqo-1) SERP2168(mqo-2) SERP2312(mqo-3)
                 SERP2412(mqo-4)
            SHA: SH0443(mqo) SH0693
            SSP: SSP0081 SSP0539
            MTU: Rv2852c(mqo)
            MTC: MT2918(yojH)
            MBO: Mb2877c(mqo)
            MBB: BCG_2872c(mqo)
            MPA: MAP2921c
            MAV: MAV_3708(mqo)
            MSM: MSMEG_2613(mqo)
            MVA: Mvan_2300
            MGI: Mflv_4052
            MMC: Mmcs_2069
            MKM: Mkms_2115
            MJL: Mjls_2052
            CGL: NCgl1926(cgl2001)
            CGB: cg2192(mqo)
            CEF: CE1894(mqo)
            CDI: DIP1492(mqo)
            CJK: jk1151(mqo)
            NFA: nfa40850
            RHA: RHA1_ro06612
            LXX: Lxx03470(mqoA)
            CMI: CMM_0904(mqoA)
            ART: Arth_2549 Arth_4255
            AAU: AAur_2520(mqo)
            KRA: Krad_3714
            SEN: SACE_1951
            SYW: SYNW1686(mqo)
            SYD: Syncc9605_0797
            SYE: Syncc9902_1584
            SYG: sync_0648(mqo)
            SYR: SynRCC307_0549(mqoA)
            SYX: SynWH7803_0602(mqoA)
            AVA: Ava_1107
            PMA: Pro0418(mqoA)
            PMM: PMM0419(mqo)
            PMT: PMT0255(mqo)
            PMN: PMN2A_1753
            PMI: PMT9312_0415
            PMB: A9601_04701(mqo)
            PMC: P9515_04801(mqo)
            PMF: P9303_20971(mqo)
            PMG: P9301_04391(mqo)
            PMH: P9215_04961
            PME: NATL1_04721(mqo)
            FJO: Fjoh_2529
            FPS: FP1752(mqo)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.16
            ExPASy - ENZYME nomenclature database: 1.1.99.16
            ExplorEnz - The Enzyme Database: 1.1.99.16
            ERGO genome analysis and discovery system: 1.1.99.16
            BRENDA, the Enzyme Database: 1.1.99.16
            CAS: 71822-24-7
///
ENTRY       EC 1.1.99.17      Obsolete  Enzyme
NAME        Transferred to 1.1.5.2
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
COMMENT     Transferred entry: now EC 1.1.5.2 quinoprotein glucose dehydrogenase
            (EC 1.1.99.17 created 1982, deleted 2003)
STRUCTURES  PDB: 1C9U  1CQ1  1CRU  1QBI  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.17
            ExPASy - ENZYME nomenclature database: 1.1.99.17
            ExplorEnz - The Enzyme Database: 1.1.99.17
            ERGO genome analysis and discovery system: 1.1.99.17
            BRENDA, the Enzyme Database: 1.1.99.17
///
ENTRY       EC 1.1.99.18                Enzyme
NAME        cellobiose dehydrogenase (acceptor);
            cellobiose dehydrogenase;
            cellobiose oxidoreductase;
            Phanerochaete chrysosporium cellobiose oxidoreductase;
            CBOR;
            cellobiose oxidase;
            cellobiose:oxygen 1-oxidoreductase;
            CDH;
            cellobiose:(acceptor) 1-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     cellobiose:acceptor 1-oxidoreductase
REACTION    cellobiose + acceptor = cellobiono-1,5-lactone + reduced acceptor
            [RN:R01443 R06246]
ALL_REAC    R01443 R06246(G) > R01442 R06244(G);
            (other) R02365 R06247(G)
SUBSTRATE   cellobiose [CPD:C00185];
            acceptor [CPD:C00028]
PRODUCT     cellobiono-1,5-lactone [CPD:C01093];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016]
COMMENT     2,6-Dichloroindophenol can act as acceptor. Also acts, more slowly,
            on cello-oligosaccharides, lactose and
            D-glucosyl-1,4-beta-D-mannose. Includes EC 1.1.5.1, cellobiose
            dehydrogenase (quinone), which is now known to be a proteolytic
            product of this enzyme. The enzyme from the white rot fungus
            Phanerochaete chrysosporium is unusual in having two redoxin
            domains, one containing a flavin and the other a protoheme group. It
            transfers reducing equivalents from cellobiose to two types of redox
            acceptor: two-electron oxidants, including redox dyes, benzoquinones
            and molecular oxygen and one-electron oxidants, including
            semiquinone species, iron(II) complexes and the model acceptor
            cytochrome c [9].
REFERENCE   1  [PMID:7103940]
  AUTHORS   Coudray MR, Canevascini G, Meier H.
  TITLE     Characterization of a cellobiose dehydrogenase in the cellulolytic
            fungus Sporotrichum (Chrysosporium) thermophile.
  JOURNAL   Biochem. J. 203 (1982) 277-84.
  ORGANISM  Sporotrichum thermophile
REFERENCE   2
  AUTHORS   Dekker, R.F.H.
  TITLE     Induction and characterization of a cellobiose dehydrogenase
            produced by a species of Monilia.
  JOURNAL   J. Gen. Microbiol. 120 (1980) 309-316.
  ORGANISM  Monilia sp.
REFERENCE   3
  AUTHORS   Dekker, R.F.H.
  TITLE     Cellobiose dehydrogenase produced by Monilia sp.
  JOURNAL   Methods Enzymol. 160 (1988) 454-463.
  ORGANISM  Monilia sp.
REFERENCE   4  [PMID:8392950]
  AUTHORS   Habu N, Samejima M, Dean JF, Eriksson KE.
  TITLE     Release of the FAD domain from cellobiose oxidase by proteases from
            cellulolytic cultures of Phanerochaete chrysosporium.
  JOURNAL   FEBS. Lett. 327 (1993) 161-4.
  ORGANISM  Phanerochaete chrysosporium
REFERENCE   5  [PMID:11282631]
  AUTHORS   Baminger U, Subramaniam SS, Renganathan V, Haltrich D.
  TITLE     Purification and characterization of cellobiose dehydrogenase from
            the plant pathogen Sclerotium (Athelia) rolfsii.
  JOURNAL   Appl. Environ. Microbiol. 67 (2001) 1766-74.
  ORGANISM  Sclerotium rolfsii
REFERENCE   6  [PMID:11786022]
  AUTHORS   Hallberg BM, Henriksson G, Pettersson G, Divne C.
  TITLE     Crystal structure of the flavoprotein domain of the extracellular
            flavocytochrome cellobiose dehydrogenase.
  JOURNAL   J. Mol. Biol. 315 (2002) 421-34.
  ORGANISM  Phanerochaete chrysosporium
REFERENCE   7  [PMID:710416]
  AUTHORS   Ayers AR, Ayers SB, Eriksson KE.
  TITLE     Cellobiose oxidase, purification and partial characterization of a
            hemoprotein from Sporotrichum pulverulentum.
  JOURNAL   Eur. J. Biochem. 90 (1978) 171-81.
  ORGANISM  Sporotrichum pulverulentum
REFERENCE   8  [PMID:7144569]
  AUTHORS   Ayers AR, Eriksson KE.
  TITLE     Cellobiose oxidase from Sporotrichum pulverulentum.
  JOURNAL   Methods. Enzymol. 89 Pt D (1982) 129-35.
  ORGANISM  Sporotrichum pulverulentum
REFERENCE   9  [PMID:12686420]
  AUTHORS   Mason MG, Nicholls P, Divne C, Hallberg BM, Henriksson G, Wilson MT.
  TITLE     The heme domain of cellobiose oxidoreductase: a one-electron
            reducing system.
  JOURNAL   Biochim. Biophys. Acta. 1604 (2003) 47-54.
  ORGANISM  Phanerochaete chrysosporium
STRUCTURES  PDB: 1NAA  1PL3  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.18
            ExPASy - ENZYME nomenclature database: 1.1.99.18
            ExplorEnz - The Enzyme Database: 1.1.99.18
            ERGO genome analysis and discovery system: 1.1.99.18
            BRENDA, the Enzyme Database: 1.1.99.18
            CAS: 54576-85-1
///
ENTRY       EC 1.1.99.19      Obsolete  Enzyme
NAME        Transferred to 1.17.99.4
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
COMMENT     Transferred entry: uracil dehydrogenase. Now EC 1.17.99.4,
            uracil/thymine dehydrogenase (EC 1.1.99.19 created 1961 as EC
            1.2.99.1, transferred 1984 to EC 1.1.99.19, deleted 2006)
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.19
            ExPASy - ENZYME nomenclature database: 1.1.99.19
            ExplorEnz - The Enzyme Database: 1.1.99.19
            ERGO genome analysis and discovery system: 1.1.99.19
            BRENDA, the Enzyme Database: 1.1.99.19
///
ENTRY       EC 1.1.99.20                Enzyme
NAME        alkan-1-ol dehydrogenase (acceptor);
            polyethylene glycol dehydrogenase;
            alkan-1-ol:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     alkan-1-ol:acceptor oxidoreductase
REACTION    primary alcohol + acceptor = aldehyde + reduced acceptor [RN:R00639]
ALL_REAC    R00639
SUBSTRATE   primary alcohol [CPD:C00226];
            acceptor [CPD:C00028]
PRODUCT     aldehyde [CPD:C00071];
            reduced acceptor [CPD:C00030]
COFACTOR    PQQ [CPD:C00113]
COMMENT     A quinoprotein. Acts on C3-C16 linear-chain saturated primary
            alcohols, C4-C7 aldehydes and on non-ionic surfactants containing
            polyethylene glycol residues, such as Tween 40 and 60, but not on
            methanol and only very slowly on ethanol. 2,6-Dichloroindophenol can
            act as acceptor. cf. EC 1.1.99.8 alcohol dehydrogenase (acceptor).
REFERENCE   1
  AUTHORS   Kawai, F., Kimura, T., Tani, Y., Yamada, H., Ueno, T. and Fukami, H.
  TITLE     Identification of reaction-products of polyethylene-glycol
            dehydrogenase.
  JOURNAL   Agric. Biol. Chem. 47 (1983) 1669-1671.
  ORGANISM  Pseudomonas sp., Flavobacterium sp.
REFERENCE   2
  AUTHORS   Kawai, F., Yamanaka, H., Ameyama, M., Shinagawa, E., Matsushita, K.
            and Adachi, O.
  TITLE     Identification of the prosthetic group and further characterization
            of a novel enzyme, polyethylene-glycol dehydrogenase.
  JOURNAL   Agric. Biol. Chem. 49 (1985) 1071-1076.
  ORGANISM  Pseudomonas sp., Flavobacterium sp.
PATHWAY     PATH: map00071  Fatty acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.20
            ExPASy - ENZYME nomenclature database: 1.1.99.20
            ExplorEnz - The Enzyme Database: 1.1.99.20
            ERGO genome analysis and discovery system: 1.1.99.20
            BRENDA, the Enzyme Database: 1.1.99.20
            CAS: 75496-55-8
///
ENTRY       EC 1.1.99.21                Enzyme
NAME        D-sorbitol dehydrogenase (acceptor);
            D-sorbitol:(acceptor) 1-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     D-sorbitol:acceptor 1-oxidoreductase
REACTION    D-sorbitol + acceptor = L-sorbose + reduced acceptor [RN:R01697]
ALL_REAC    R01697 > R02925
SUBSTRATE   D-sorbitol [CPD:C00794];
            acceptor [CPD:C00028]
PRODUCT     L-sorbose [CPD:C00247];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1
  AUTHORS   Shinagawa, E. and Ameyama, M.
  TITLE     Purification and characterization of D-sorbitol dehydrogenase from
            membrane of Gluconobacter suboxydans var-alpha.
  JOURNAL   Agric. Biol. Chem. 46 (1982) 135-141.
  ORGANISM  Gluconobacter suboxydans
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K08261  D-sorbitol dehydrogenase (acceptor)
GENES       BPM: BURPS1710b_A2589 BURPS1710b_A2590
            RET: RHE_PF00443
            ZMO: ZMO0788(sldC) ZMO1284(sldC) ZMO1285(sldL) ZMO1286(sldS)
            GOX: GOX2095 GOX2096 GOX2097
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.21
            ExPASy - ENZYME nomenclature database: 1.1.99.21
            ExplorEnz - The Enzyme Database: 1.1.99.21
            ERGO genome analysis and discovery system: 1.1.99.21
            BRENDA, the Enzyme Database: 1.1.99.21
            CAS: 9028-22-2
///
ENTRY       EC 1.1.99.22                Enzyme
NAME        glycerol dehydrogenase (acceptor);
            glycerol:(acceptor) 1-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     glycerol:acceptor 1-oxidoreductase
REACTION    glycerol + acceptor = glycerone + reduced acceptor [RN:R01045]
ALL_REAC    R01045
SUBSTRATE   glycerol [CPD:C00116];
            acceptor [CPD:C00028]
PRODUCT     glycerone [CPD:C00184];
            reduced acceptor [CPD:C00030]
COFACTOR    PQQ [CPD:C00113]
COMMENT     A quinoprotein. Also acts, more slowly, on a number of other polyols
            including D-sorbitol, D-arabitol, meso-erythritol, adonitol and
            propylene glycol.
REFERENCE   1
  AUTHORS   Ameyama, M., Shinagawa, E., Matsushita, K. and Adachi, O.
  TITLE     Solubilization, purification and properties of membrane-bound
            glycerol dehydrogenase from Gluconobacter industrius.
  JOURNAL   Agric. Biol. Chem. 49 (1985) 1001-1010.
  ORGANISM  Gluconobacter industrius
GENES       SWI: Swit_2024
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.22
            ExPASy - ENZYME nomenclature database: 1.1.99.22
            ExplorEnz - The Enzyme Database: 1.1.99.22
            ERGO genome analysis and discovery system: 1.1.99.22
            BRENDA, the Enzyme Database: 1.1.99.22
            CAS: 249285-11-8
///
ENTRY       EC 1.1.99.23                Enzyme
NAME        polyvinyl-alcohol dehydrogenase (acceptor);
            PVA dehydrogenase;
            polyvinyl-alcohol:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     polyvinyl-alcohol:acceptor oxidoreductase
REACTION    polyvinyl alcohol + acceptor = oxidized polyvinyl alcohol + reduced
            acceptor [RN:R03136]
ALL_REAC    R03136
SUBSTRATE   polyvinyl alcohol [CPD:C00980];
            acceptor [CPD:C00028]
PRODUCT     oxidized polyvinyl alcohol [CPD:C01166];
            reduced acceptor [CPD:C00030]
COFACTOR    PQQ [CPD:C00113]
COMMENT     A quinoprotein. Phenazine methosulfate and 2,6-dichloroindophenol
            can act as acceptors. Also acts, more slowly, on 2-hexanol and some
            other secondary alcohols. cf. EC 1.1.99.8 alcohol dehydrogenase
            (acceptor) and EC 1.1.99.20 alkan-1-ol dehydrogenase (acceptor).
REFERENCE   1  [PMID:3513704]
  AUTHORS   Shimao M, Ninomiya K, Kuno O, Kato N, Sakazawa C.
  TITLE     Existence of a novel enzyme, pyrroloquinoline quinone-dependent
            polyvinyl alcohol dehydrogenase, in a bacterial symbiont,
            Pseudomonas sp. strain VM15C.
  JOURNAL   Appl. Environ. Microbiol. 51 (1986) 268-75.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:16347841]
  AUTHORS   Shimao M, Onishi S, Kato N, Sakazawa C.
  TITLE     Pyrroloquinoline Quinone-Dependent Cytochrome Reduction in Polyvinyl
            Alcohol-Degrading Pseudomonas sp. Strain VM15C.
  JOURNAL   Appl. Environ. Microbiol. 55 (1989) 275-278.
  ORGANISM  Pseudomonas sp.
ORTHOLOGY   KO: K05889  
GENES       XFA: XF2259
            XFT: PD1299
            XCC: XCC4080
            XCB: XC_4171
            XCV: XCV4300
            XAC: XAC4199
            XOO: XOO0329
            XOM: XOO_0301(XOO0301)
            EBA: p2A321(pvaA)
            BJA: bll5504
            SUS: Acid_5713
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.23
            ExPASy - ENZYME nomenclature database: 1.1.99.23
            ExplorEnz - The Enzyme Database: 1.1.99.23
            ERGO genome analysis and discovery system: 1.1.99.23
            BRENDA, the Enzyme Database: 1.1.99.23
            CAS: 119940-13-5
///
ENTRY       EC 1.1.99.24                Enzyme
NAME        hydroxyacid-oxoacid transhydrogenase;
            transhydrogenase, hydroxy acid-oxo acid
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     (S)-3-hydroxybutanoate:2-oxoglutarate oxidoreductase
REACTION    (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate +
            (R)-2-hydroxyglutarate [RN:R03225]
ALL_REAC    R03225
SUBSTRATE   (S)-3-hydroxybutanoate [CPD:C03197];
            2-oxoglutarate [CPD:C00026]
PRODUCT     acetoacetate [CPD:C00164];
            (R)-2-hydroxyglutarate [CPD:C01087]
COMMENT     4-Hydroxybutanoate and (R)-2-hydroxyglutarate can also act as
            donors; 4-oxobutanoate can also act as acceptor.
REFERENCE   1  [PMID:3182820]
  AUTHORS   Kaufman EE, Nelson T, Fales HM, Levin DM.
  TITLE     Isolation and characterization of a hydroxyacid-oxoacid
            transhydrogenase from rat kidney mitochondria.
  JOURNAL   J. Biol. Chem. 263 (1988) 16872-9.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.24
            ExPASy - ENZYME nomenclature database: 1.1.99.24
            ExplorEnz - The Enzyme Database: 1.1.99.24
            ERGO genome analysis and discovery system: 1.1.99.24
            BRENDA, the Enzyme Database: 1.1.99.24
            CAS: 117698-31-4
///
ENTRY       EC 1.1.99.25                Enzyme
NAME        quinate dehydrogenase (pyrroloquinoline-quinone);
            NAD(P)+-independent quinate dehydrogenase;
            quinate:pyrroloquinoline-quinone 5-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     quinate:pyrroloquinoline-quinone 3-oxidoreductase
REACTION    quinate + pyrroloquinoline-quinone = 3-dehydroquinate + reduced
            pyrroloquinoline-quinone [RN:R01873]
ALL_REAC    R01873;
            (other) R02415
SUBSTRATE   quinate [CPD:C00296];
            pyrroloquinoline-quinone [CPD:C00113]
PRODUCT     3-dehydroquinate [CPD:C00944];
            reduced pyrroloquinoline-quinone [CPD:C01359]
REFERENCE   1  [PMID:3044290]
  AUTHORS   van Kleef MA, Duine JA.
  TITLE     Bacterial NAD(P)-independent quinate dehydrogenase is a
            quinoprotein.
  JOURNAL   Arch. Microbiol. 150 (1988) 32-6.
  ORGANISM  Acinetobacter calcoaceticus
REFERENCE   2  [PMID:14586099]
  AUTHORS   Adachi O, Tanasupawat S, Yoshihara N, Toyama H, Matsushita K.
  TITLE     3-dehydroquinate production by oxidative fermentation and further
            conversion of 3-dehydroquinate to the intermediates in the shikimate
            pathway.
  JOURNAL   Biosci. Biotechnol. Biochem. 67 (2003) 2124-31.
  ORGANISM  Gluconobacter oxydans [GN:gox]
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K05358  quinate dehydrogenase (pyrroloquinoline-quinone)
GENES       ENT: Ent638_1963
            PSP: PSPPH_2927(quiA)
            PEN: PSEEN2918(quiA)
            ACI: ACIAD1716(quiA)
            REH: H16_B1047(quiA)
            GBE: GbCGDNIH1_1597
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.25
            ExPASy - ENZYME nomenclature database: 1.1.99.25
            ExplorEnz - The Enzyme Database: 1.1.99.25
            ERGO genome analysis and discovery system: 1.1.99.25
            BRENDA, the Enzyme Database: 1.1.99.25
            CAS: 115299-99-5
///
ENTRY       EC 1.1.99.26                Enzyme
NAME        3-hydroxycyclohexanone dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     3-hydroxycyclohexanone:acceptor 1-oxidoreductase
REACTION    3-hydroxycyclohexanone + acceptor = cyclohexane-1,3-dione + reduced
            acceptor [RN:R03212]
ALL_REAC    R03212
SUBSTRATE   3-hydroxycyclohexanone [CPD:C03228];
            acceptor [CPD:C00028]
PRODUCT     cyclohexane-1,3-dione [CPD:C01066];
            reduced acceptor [CPD:C00030]
COMMENT     2,6-Dichloroindophenol and methylene blue can act as acceptors.
REFERENCE   1
  AUTHORS   Dangel, W., Tschech, A. and Fuchs, G.
  TITLE     Enzyme-reactions involved in anaerobic cyclohexanol metabolism by a
            denitrifying Pseudomonas species.
  JOURNAL   Arch. Microbiol. 152 (1989) 273-279.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.26
            ExPASy - ENZYME nomenclature database: 1.1.99.26
            ExplorEnz - The Enzyme Database: 1.1.99.26
            ERGO genome analysis and discovery system: 1.1.99.26
            BRENDA, the Enzyme Database: 1.1.99.26
            CAS: 123516-44-9
///
ENTRY       EC 1.1.99.27                Enzyme
NAME        (R)-pantolactone dehydrogenase (flavin);
            2-dehydropantolactone reductase (flavin);
            2-dehydropantoyl-lactone reductase (flavin);
            (R)-pantoyllactone dehydrogenase (flavin)
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     (R)-pantolactone:acceptor oxidoreductase (flavin-containing)
REACTION    (R)-pantolactone + acceptor = 2-dehydropantolactone + reduced
            acceptor [RN:R03156]
ALL_REAC    R03156
SUBSTRATE   (R)-pantolactone [CPD:C01012];
            acceptor [CPD:C00028]
PRODUCT     2-dehydropantolactone [CPD:C01125];
            reduced acceptor [CPD:C00030]
COMMENT     High specificity for (R)-pantolactone. Phenazine methosulfate (PMS)
            can act as acceptor. The enzyme has been studied in the bacterium
            Nocardia asteroides and shown to be membrane-bound and induced by
            1,2-propanediol. The FMN cofactor is non-covalently bound.
REFERENCE   1  [PMID:1541293]
  AUTHORS   Kataoka M, Shimizu S, Yamada H.
  TITLE     Purification and characterization of a novel FMN-dependent enzyme.
            Membrane-bound L-(+)-pantoyl lactone dehydrogenase from Nocardia
            asteroides.
  JOURNAL   Eur. J. Biochem. 204 (1992) 799-806.
  ORGANISM  Nocardia asteroides
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.27
            ExPASy - ENZYME nomenclature database: 1.1.99.27
            ExplorEnz - The Enzyme Database: 1.1.99.27
            ERGO genome analysis and discovery system: 1.1.99.27
            BRENDA, the Enzyme Database: 1.1.99.27
            CAS: 140879-14-7
///
ENTRY       EC 1.1.99.28                Enzyme
NAME        glucose-fructose oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     D-glucose:D-fructose oxidoreductase
REACTION    D-glucose + D-fructose = D-gluconolactone + D-glucitol [RN:R00874]
ALL_REAC    R00874
SUBSTRATE   D-glucose [CPD:C00031];
            D-fructose [CPD:C00095]
PRODUCT     D-gluconolactone [CPD:C00198];
            D-glucitol [CPD:C00794]
COMMENT     D-mannose, D-xylose, D-galactose, 2-deoxy-D-glucose and L-arabinose
            will function as aldose substrates, but with low affinities. The
            ketose substrate must be in the open-chain form. The apparent
            affinity for fructose is low, because little of the fructose
            substrate is in the open-chain form. Xylulose and glycerone
            (dihydroxyacetone) will replace fructose, but they are poor
            substrates. The enzyme from Zymomonas mobilis contains tightly bound
            NADP+.
REFERENCE   1
  AUTHORS   Zachariou, M. and Scopes, R.K.
  TITLE     Glucose-fructose oxidoreductase: a new enzyme isolated from
            Zymomonas mobilis that is responsible for sorbitol production.
  JOURNAL   J. Bacteriol. 167 (1986) 863-869.
  ORGANISM  Zymomonas mobilis [GN:zmo]
REFERENCE   2  [PMID:3356190]
  AUTHORS   Hardman MJ, Scopes RK.
  TITLE     The kinetics of glucose-fructose oxidoreductase from Zymomonas
            mobilis.
  JOURNAL   Eur. J. Biochem. 173 (1988) 203-9.
REFERENCE   3  [PMID:1537789]
  AUTHORS   Kanagasundaram V, Scopes RK.
  TITLE     Cloning, sequence analysis, and expression of the structural gene
            encoding glucose-fructose oxidoreductase from Zymomonas mobilis.
  JOURNAL   J. Bacteriol. 174 (1992) 1439-47.
  ORGANISM  Zymomonas mobilis [GN:zmo]
ORTHOLOGY   KO: K00118  glucose-fructose oxidoreductase
GENES       AFM: AFUA_2G16380
            XCC: XCC0815(gfo)
            XCB: XC_3415
            XCV: XCV0923(gfo)
            XAC: XAC0888(gfo)
            XOO: XOO3722(gfo)
            XOM: XOO_3515(XOO3515)
            RSO: RS02580(RSp1076)
            RLE: RL4170
            BME: BMEI0020
            BMF: BAB1_2049
            CCR: CC_1225
            ZMO: ZMO0689(gfo)
            RHA: RHA1_ro02475
            RBA: RB3265(gfo)
            GFO: GFO_2195(gfo)
            HWA: HQ3202A(gfoR)
STRUCTURES  PDB: 1H6A  1H6B  1H6C  1H6D  1OFG  1RYD  1RYE  
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.28
            ExPASy - ENZYME nomenclature database: 1.1.99.28
            ExplorEnz - The Enzyme Database: 1.1.99.28
            ERGO genome analysis and discovery system: 1.1.99.28
            BRENDA, the Enzyme Database: 1.1.99.28
            CAS: 94949-35-6
///
ENTRY       EC 1.1.99.29                Enzyme
NAME        pyranose dehydrogenase (acceptor);
            pyranose dehydrogenase;
            pyranose-quinone oxidoreductase;
            quinone-dependent pyranose dehydrogenase;
            PDH
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     pyranose:acceptor oxidoreductase
REACTION    (1) pyranose + acceptor = 2-dehydropyranose (or 3-dehydropyranose or
            2,3-didehydropyranose) + reduced acceptor [RN:R07347];
            (2) a pyranoside + acceptor = a 3-dehydropyranoside (or
            3,4-didehydropyranoside) + reduced acceptor [RN:R07348]
ALL_REAC    R07347 R07348
SUBSTRATE   pyranose [CPD:C15592];
            acceptor [CPD:C00028];
            pyranoside [CPD:C15594]
PRODUCT     2-dehydropyranose [CPD:C15593];
            3-dehydropyranose;
            2,3-didehydropyranose;
            reduced acceptor [CPD:C00030];
            3-dehydropyranoside [CPD:C15595];
            3,4-didehydropyranoside
COMMENT     Requires FAD. A number of aldoses and ketoses in pyranose form, as
            well as glycosides, gluco-oligosaccharides, sucrose and lactose can
            act as a donor. 1,4-Benzoquinone or ferricenium ion (ferrocene
            oxidized by removal of one electron) can serve as acceptor. Unlike
            EC 1.1.3.10, pyranose oxidase, this fungal enzyme does not interact
            with O2 and exhibits extremely broad substrate tolerance with
            variable regioselectivity (C-3, C-2 or C-3 + C-2 or C-3 + C-4) for
            (di)oxidation of different sugars. D-Glucose is exclusively or
            preferentially oxidized at C-3 (depending on the enzyme source), but
            can also be oxidized at C-2 + C-3. The enzyme also acts on
            1->4-alpha- and 1->4-beta-gluco-oligosaccharides, non-reducing
            gluco-oligosaccharides and L-arabinose, which are not substrates of
            EC 1.1.3.10. Sugars are oxidized in their pyranose but not in their
            furanose form.
REFERENCE   1  [PMID:9042751]
  AUTHORS   Volc J, Kubatova E, Wood DA, Daniel G.
  TITLE     Pyranose 2-dehydrogenase, a novel sugar oxidoreductase from the
            basidiomycete fungus Agaricus bisporus
  JOURNAL   Arch. Microbiol. 167 (1997) 119-25.
  ORGANISM  Agaricus bisporus
REFERENCE   2
  AUTHORS   Volc, J., Sedmera, P., Halada, P., Poikyrlova, V. and Daniel, G.
  TITLE     C-2 and C-3 oxidation of D-Glc, and C-2 oxidation of D-Gal by
            pyranose dehydrogenase from Agaricus bisporus.
  JOURNAL   Carbohydr. Res. 310 (1998) 151-156.
  ORGANISM  Agaricus bisporus
REFERENCE   3  [PMID:11086703]
  AUTHORS   Volc J, Sedmera P, Halada P, Prikrylova V, Haltrich D.
  TITLE     Double oxidation of D-xylose to D-glycero -pentos-2,3-diulose
            (2,3-diketo-D-xylose) by pyranose dehydrogenase from the mushroom
            Agaricus bisporus.
  JOURNAL   Carbohydr. Res. 329 (2000) 219-25.
  ORGANISM  Agaricus bisporus
REFERENCE   4  [PMID:11511865]
  AUTHORS   Volc J, Kubatova E, Daniel G, Sedmera P, Haltrich D.
  TITLE     Screening of basidiomycete fungi for the quinone-dependent sugar
            C-2/C-3 oxidoreductase, pyranose dehydrogenase, and properties of
            the enzyme from Macrolepiota rhacodes.
  JOURNAL   Arch. Microbiol. 176 (2001) 178-86.
  ORGANISM  Macrolepiota rhacodes
REFERENCE   5
  AUTHORS   Volc, J., Sedmera, P., Halada, P., Daniel, G., Poikyrlova, V. and
            Haltrich, D.
  TITLE     C-3 oxidation of non-reducing sugars by a fungal pyranose
            dehydrogenase: spectral characterization.
  JOURNAL   J. Mol. Catal., B Enzym. 17 (2002) 91-100.
  ORGANISM  Agaricus meleagris
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.29
            ExPASy - ENZYME nomenclature database: 1.1.99.29
            ExplorEnz - The Enzyme Database: 1.1.99.29
            ERGO genome analysis and discovery system: 1.1.99.29
            BRENDA, the Enzyme Database: 1.1.99.29
///
ENTRY       EC 1.1.99.30                Enzyme
NAME        2-oxo-acid reductase;
            (2R)-hydroxycarboxylate-viologen-oxidoreductase;
            HVOR;
            2-oxoacid reductase
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     (2R)-hydroxy-carboxylate:acceptor oxidoreductase
REACTION    a (2R)-hydroxy-carboxylate + acceptor = a 2-oxo-carboxylate +
            reduced acceptor [RN:R07155]
ALL_REAC    R07155
SUBSTRATE   (2R)-hydroxy-carboxylate [CPD:C15487];
            acceptor [CPD:C00028]
PRODUCT     2-oxo-carboxylate;
            reduced acceptor [CPD:C00030]
COMMENT     Contains [4Fe-4S] and a mononucleotide molybdenum (pyranopterin)
            cofactor. Has broad substrate specificity, with
            2-oxo-monocarboxylates and 2-oxo-dicarboxylates acting as
            substrates. Branching in a substrate at the C-3 position results in
            loss of activity. The enzyme from Proteus sp. is inactivated by
            oxygen.
REFERENCE   1  [PMID:8026480]
  AUTHORS   Trautwein T, Krauss F, Lottspeich F, Simon H.
  TITLE     The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus
            vulgaris is a molybdenum-containing iron-sulphur protein.
  JOURNAL   Eur. J. Biochem. 222 (1994) 1025-32.
  ORGANISM  Proteus vulgaris
REFERENCE   2
  AUTHORS   Neumann, S. and Simon, H.
  TITLE     On a non-pyridine nucleotide-dependent 2-oxoacid reductase of broad
            specificity from two Proteus species.
  JOURNAL   FEBS Lett. 167 (1985) 29-32.
  ORGANISM  Proteus sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.30
            ExPASy - ENZYME nomenclature database: 1.1.99.30
            ExplorEnz - The Enzyme Database: 1.1.99.30
            ERGO genome analysis and discovery system: 1.1.99.30
            BRENDA, the Enzyme Database: 1.1.99.30
            CAS: 115299-99-5
///
ENTRY       EC 1.1.99.31                Enzyme
NAME        (S)-mandelate dehydrogenase;
            MDH
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
SYSNAME     (S)-2-hydroxy-2-phenylacetate:acceptor 2-oxidoreductase
REACTION    (S)-2-hydroxy-2-phenylacetate + acceptor = 2-oxo-2-phenylacetate +
            reduced acceptor [RN:R03793]
ALL_REAC    R03793
SUBSTRATE   (S)-2-hydroxy-2-phenylacetate [CPD:C01984];
            acceptor [CPD:C00028]
PRODUCT     2-oxo-2-phenylacetate [CPD:C02137];
            reduced acceptor [CPD:C00030]
COMMENT     This enzyme is a member of the FMN-dependent alpha-hydroxy-acid
            oxidase/dehydrogenase family [1]. While all enzymes of this family
            oxidize the (S)-enantiomer of an alpha-hydroxy acid to an alpha-oxo
            acid, the ultimate oxidant (oxygen, intramolecular heme or some
            other acceptor) depends on the particular enzyme. This enzyme
            transfers the electron pair from FMNH2 to a component of the
            electron transport chain, most probably ubiquinone [1,2]. It is part
            of a metabolic pathway in Pseudomonads that allows these organisms
            to utilize mandelic acid, derivatized from the common soil
            metabolite amygdalin, as the sole source of carbon and energy [2].
            The enzyme has a large active-site pocket and preferentially binds
            substrates with longer sidechains, e.g. 2-hydroxyoctanoate rather
            than 2-hydroxybutyrate [1]. It also prefers substrates that, like
            (S)-mandelate, have beta unsaturation, e.g. (indol-3-yl)glycolate
            compared with (indol-3-yl)lactate [1]. Esters of mandelate, such as
            methyl (S)-mandelate, are also substrates [3].
REFERENCE   1  [PMID:10231535]
  AUTHORS   Lehoux IE, Mitra B.
  TITLE     (S)-Mandelate dehydrogenase from Pseudomonas putida: mechanistic
            studies with alternate substrates and pH and kinetic isotope
            effects.
  JOURNAL   Biochemistry. 38 (1999) 5836-48.
REFERENCE   2  [PMID:15311930]
  AUTHORS   Dewanti AR, Xu Y, Mitra B.
  TITLE     Role of glycine 81 in (S)-mandelate dehydrogenase from Pseudomonas
            putida in substrate specificity and oxidase activity.
  JOURNAL   Biochemistry. 43 (2004) 10692-700.
REFERENCE   3  [PMID:14967029]
  AUTHORS   Dewanti AR, Xu Y, Mitra B.
  TITLE     Esters of mandelic acid as substrates for (S)-mandelate
            dehydrogenase from Pseudomonas putida: implications for the reaction
            mechanism.
  JOURNAL   Biochemistry. 43 (2004) 1883-90.
DBLINKS     IUBMB Enzyme Nomenclature: 1.1.99.31
            ExPASy - ENZYME nomenclature database: 1.1.99.31
            ExplorEnz - The Enzyme Database: 1.1.99.31
            ERGO genome analysis and discovery system: 1.1.99.31
            BRENDA, the Enzyme Database: 1.1.99.31
///
ENTRY       EC 1.1.99.-                 Enzyme
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors;
            With other acceptors
REACTION    (1) (S)-4-Hydroxymandelate + Acceptor <=> 4-Hydroxyphenylglyoxylate
            + Reduced acceptor [RN:R04160];
            (2) (2-Aminoethyl)phosphonate <=> 1-Hydroxy-2-aminoethylphosphonate
            [RN:R04249];
            (3) Limonene-1,2-diol <=> (1S,4R)-1-Hydroxy-2-oxolimonene
            [RN:R06399]
SUBSTRATE   (S)-Mandelate [CPD:C01984];
            Acceptor [CPD:C00028];
            (S)-4-Hydroxymandelate [CPD:C03198];
            (2-Aminoethyl)phosphonate [CPD:C03557];
            trans-3-Chloro-2-propene-1-ol [CPD:C06611];
            cis-3-Chloro-2-propene-1-ol [CPD:C06612];
            Limonene-1,2-diol [CPD:C07276]
PRODUCT     alpha-Oxo-benzeneacetic acid [CPD:C02137];
            Reduced acceptor [CPD:C00030];
            4-Hydroxyphenylglyoxylate [CPD:C03590];
            1-Hydroxy-2-aminoethylphosphonate [CPD:C05678];
            3-Chloroallyl aldehyde [CPD:C06613];
            H+ [CPD:C00080];
            cis-3-Chloroallyl aldehyde [CPD:C16348];
            (1S,4R)-1-Hydroxy-2-oxolimonene [CPD:C11937]
///
ENTRY       EC 1.1.-.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on the CH-OH group of donors
REACTION    (1) 1-Phenylethanol <=> (S)-1-Phenylethanol + 2 e- + 2 H+
            [RN:R05352];
            (2) 2,6-Dihydroxycyclohexane-1-carboxyl-CoA + Acceptor <=>
            6-Oxo-2-hydroxycyclohexane-1-carboxyl-CoA + Reduced acceptor
            [RN:R05583];
            (3) 2-Hydroxy-4-isopropenylcyclohexane-1-carboxyl-CoA + Acceptor <=>
            4-Isopropenyl-2-oxy-cyclohexanecarboxyl-CoA + Reduced acceptor
            [RN:R06370];
            (4) Myrtenol + Oxygen + Acceptor <=> Myrtenal + 2 H2O + Reduced
            acceptor [RN:R06402];
            (5) Pinocarveol <=> Pinocarvone + H+ [RN:R06405];
            (6) 3-Hydroxy-2,6-dimethyl-5-methylene-heptanoyl-CoA + NAD+ <=>
            2,6-Dimethyl-5-methylene-3-oxo-heptanoyl-CoA + NADH + H+
            [RN:R06413];
            (7) Benzene-1,2,4-triol <=> 2-Hydroxy-1,4-benzoquinone [RN:R06853];
            (8) 2-Hydroxy-1,4-benzoquinone <=> p-Benzoquinone + H2O [RN:R06854];
            (9) 1,2-Bis(4-hydroxyphenyl)-2-propanol <=>
            4,4'-Dihydroxy-alpha-methylstilbene + H2O [RN:R06885];
            (10) Naphthyl-2-hydroxymethyl-succinyl CoA <=>
            Naphthyl-2-oxomethyl-succinyl-CoA + 2 H+ [RN:R06907];
            (11) cis-1,2-Dihydroxy-1,2-dihydro-8-carboxynaphthalene <=>
            1,2-Dihydroxy-8-carboxynaphthalene [RN:R06920];
            (12) Anthracene-9,10-dihydrodiol <=> 9,10-Dihydroxyanthracene + 4 H+
            [RN:R07688]
SUBSTRATE   1-Phenylethanol [CPD:C07112];
            2,6-Dihydroxycyclohexane-1-carboxyl-CoA [CPD:C09824];
            Acceptor [CPD:C00028];
            2-Hydroxy-4-isopropenylcyclohexane-1-carboxyl-CoA [CPD:C11934];
            Myrtenol [CPD:C11938];
            Oxygen [CPD:C00007];
            Pinocarveol [CPD:C11941];
            3-Hydroxy-2,6-dimethyl-5-methylene-heptanoyl-CoA [CPD:C11947];
            NAD+ [CPD:C00003];
            Benzene-1,2,4-triol [CPD:C02814];
            2-Hydroxy-1,4-benzoquinone [CPD:C07103];
            1,2-Bis(4-hydroxyphenyl)-2-propanol [CPD:C13629];
            Naphthyl-2-hydroxymethyl-succinyl CoA [CPD:C14118];
            cis-1,2-Dihydroxy-1,2-dihydro-8-carboxynaphthalene [CPD:C14092]
PRODUCT     (S)-1-Phenylethanol [CPD:C11348];
            e- [CPD:C05359];
            H+ [CPD:C00080];
            6-Oxo-2-hydroxycyclohexane-1-carboxyl-CoA [CPD:C09825];
            Reduced acceptor [CPD:C00030];
            4-Isopropenyl-2-oxy-cyclohexanecarboxyl-CoA [CPD:C11935];
            Myrtenal [CPD:C11939];
            H2O [CPD:C00001];
            Pinocarvone [CPD:C09884];
            2,6-Dimethyl-5-methylene-3-oxo-heptanoyl-CoA [CPD:C11948];
            NADH [CPD:C00004];
            2-Hydroxy-1,4-benzoquinone [CPD:C07103];
            p-Benzoquinone [CPD:C00472];
            4,4'-Dihydroxy-alpha-methylstilbene [CPD:C13632];
            Naphthyl-2-oxomethyl-succinyl-CoA [CPD:C14119];
            1,2-Dihydroxy-8-carboxynaphthalene [CPD:C14093]
///
ENTRY       EC 1.2.1.1        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: glutathione-dependent formaldehyde dehydrogenase.
            This enzyme was classified on the basis of an incorrect reaction. It
            has been replaced by two enzymes, EC 1.1.1.284,
            S-(hydroxymethyl)glutathione dehydrogenase and EC 4.4.1.22,
            S-(hydroxymethyl)glutathione synthase (EC 1.2.1.1 created 1961,
            modified 1982, modified 2002, deleted 2005)
GENES       SPO: SPCC13B11.04c
            BUR: Bcep18194_A5935
            BPM: BURPS1710b_1025(flhA)
            RET: RHE_PF00402(adhCf)
            RRU: Rru_A3405
            AVA: Ava_4498
STRUCTURES  PDB: 1M6H  1M6W  1MA0  1MC5  1MP0  1TEH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.1
            ExPASy - ENZYME nomenclature database: 1.2.1.1
            ExplorEnz - The Enzyme Database: 1.2.1.1
            ERGO genome analysis and discovery system: 1.2.1.1
            BRENDA, the Enzyme Database: 1.2.1.1
///
ENTRY       EC 1.2.1.2                  Enzyme
NAME        formate dehydrogenase;
            formate-NAD+ oxidoreductase;
            FDH I;
            FDH II;
            N-FDH;
            formic hydrogen-lyase;
            formate hydrogenlyase;
            hydrogenlyase;
            NAD+-linked formate dehydrogenase;
            NAD+-dependent formate dehydrogenase;
            formate dehydrogenase (NAD+);
            NAD+-formate dehydrogenase;
            formate benzyl-viologen oxidoreductase;
            formic acid dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     formate:NAD+ oxidoreductase
REACTION    formate + NAD+ = CO2 + NADH [RN:R00519]
ALL_REAC    R00519
SUBSTRATE   formate [CPD:C00058];
            NAD+ [CPD:C00003]
PRODUCT     CO2 [CPD:C00011];
            NADH [CPD:C00004]
COMMENT     The enzyme from most aerobic organisms is devoid of redox-active
            centres but that from the proteobacterium Methylosinus trichosporium
            contains iron-sulfur centres, flavin and a molybdenum centre [3].
            Together with EC 1.12.1.2 hydrogen dehydrogenase, forms a system
            previously known as formate hydrogenlyase.
REFERENCE   1  [PMID:14886318]
  AUTHORS   DAVISON DC.
  TITLE     Studies on plant formic dehydrogenase.
  JOURNAL   Biochem. J. 49 (1951) 520-6.
  ORGANISM  Phaseolus vulgaris
REFERENCE   2
  AUTHORS   Quayle, J.R.
  TITLE     Formate dehydrogenase.
  JOURNAL   Methods Enzymol. 9 (1966) 360-364.
  ORGANISM  Pseudomonas oxalaticus
REFERENCE   3  [PMID:1657982]
  AUTHORS   Jollie DR, Lipscomb JD.
  TITLE     Formate dehydrogenase from Methylosinus trichosporium OB3b.
            Purification and spectroscopic characterization of the cofactors.
  JOURNAL   J. Biol. Chem. 266 (1991) 21853-63.
  ORGANISM  Methylosinus trichosporium
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
            PATH: map00680  Methane metabolism
            PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K00122  formate dehydrogenase
            KO: K00123  formate dehydrogenase, alpha subunit
            KO: K00124  formate dehydrogenase, beta subunit
            KO: K00125  formate dehydrogenase, beta subunit
            KO: K00126  formate dehydrogenase, delta subunit
            KO: K00127  formate dehydrogenase, gamma subunit
            KO: K08348  formate dehydrogenase-N, alpha subunit
            KO: K08349  formate dehydrogenase-N, beta subunit
            KO: K08350  formate dehydrogenase-N, gamma subunit
GENES       ATH: AT5G14780(FDH)
            OSA: 4341069 4341070
            SCE: YOR388C(FDH1)
            PIC: PICST_33765(FDH1.2) PICST_43416(MDH99) PICST_47526(FOC1)
                 PICST_91526(FDH1.1)
            ANI: AN6525.2
            AFM: AFUA_6G04920
            AOR: AO090010000579 AO090701000046
            CNE: CNF03470
            ECO: b1474(fdnG) b1475(fdnH) b1476(fdnI) b3892(fdoI) b3893(fdoH)
                 b3894(fdoG) b4079(fdhF)
            ECJ: JW1470(fdnG) JW1471(fdnH) JW1472(fdnI) JW3863(fdoI)
                 JW3864(fdoH) JW3865(fdoG) JW4040(fdhF)
            ECE: Z2234(fdnI) Z2235(fdnH) Z2236(fdnG) Z5434(fdoI) Z5435(fdoH)
                 Z5436(fdoG) Z5678(fdhF)
            ECS: ECs2078 ECs2079 ECs2080 ECs4818 ECs4819 ECs4820 ECs5061
            ECC: c1906(fdnH) c1907(fdnI) c4842(fdoI) c4843(fdoH) c5623(fdnG)
                 c5624(fdoG) c5625(fdhF)
            ECI: UTI89_C1042(hyaC) UTI89_C1689(fdnG) UTI89_C1691(fdnH)
                 UTI89_C1692(fdnI) UTI89_C4115(ysaA) UTI89_C4479(fdoI)
                 UTI89_C4482(fdhD)
            ECP: ECP_1474 ECP_1475 ECP_1476 ECP_1477 ECP_4104 ECP_4105
            ECV: APECO1_2372(fdhF) APECO1_23722(fdhF) APECO1_2571(fdoG)
                 APECO1_25712(fdoG) APECO1_2572(fdoH) APECO1_2573(fdoI)
                 APECO1_609(fdnG) APECO1_611(fdnI)
            ECW: EcE24377A_1655(fdnG) EcE24377A_1657(fdnH)
                 EcE24377A_1658(fdnI) EcE24377A_4421(fdoI) EcE24377A_4422(fdoH)
                 EcE24377A_4635(fdhF)
            ECX: EcHS_A1557(fdnG) EcHS_A1558(fdnH) EcHS_A1559(fdnI)
                 EcHS_A4120(fdoI) EcHS_A4121(fdoH) EcHS_A4122(fdoG)
                 EcHS_A4324(fdhF)
            STY: STY3839(fdoG) STY3841(fdoH) STY3842(fdoI) STY4484(fdhF)
            STT: t3583(fdoG) t3584(fdoH) t3585(fdoI) t4192(fdhF)
            SPT: SPA1298(fdnG) SPA1299(fdnH) SPA1300(fdnI) SPA3877(fdoI)
                 SPA3878(fdoH) SPA4103(fdhF)
            SEC: SC1569(fdnI) SC1570(fdnH) SC3925(fdoI) SC3926(fdoH)
            STM: STM1568(fdnI) STM1569(fdnH) STM1570(fdnG) STM4035(fdoI)
                 STM4036(fdoH) STM4037(fdoG) STM4285(fdhF)
            YPE: YPO0344(fdhF) YPO4056(fdoI) YPO4057(fdoH)
            YPK: y0601(fdhF) y4076(fdoI) y4077(fdoH)
            YPM: YP_0498(fdhF) YP_3968(fdoI) YP_3969(fdoH)
            YPA: YPA_3026 YPA_3027 YPA_3029 YPA_3938
            YPN: YPN_3326 YPN_3703 YPN_3704 YPN_3705 YPN_3706
            YPP: YPDSF_0034
            YPS: YPTB0398(fdhF) YPTB3927(fdoG) YPTB3928(fdoH) YPTB3929(fdoI)
            YPI: YpsIP31758_3682(fdhF) YpsIP31758_4117(fdoI)
                 YpsIP31758_4119(fdoG)
            YEN: YE4135(fdoG)
            SFL: SF1749(fdnI) SF1750(fdnH) SF1751(fdnG) SF3968(fdoI)
                 SF3969(fdoH) SF3970(fdoG)
            SFX: S1882(fdnI) S1883(fdnH) S1884(fdnG) S3778(fdoG) S3779(fdoH)
                 S3780(fdoI)
            SFV: SFV_1745(fdnI) SFV_1746(fdnH) SFV_1747(fdnG) SFV_3601(fdoG)
                 SFV_3602(fdoH) SFV_3603(fdoI)
            SSN: SSON_1648(fdnI) SSON_1649(fdnH) SSON_1650(fdnG)
                 SSON_4061(fdoI) SSON_4062(fdoH) SSON_4063(fdoG)
            SBO: SBO_1581(fdnI) SBO_1582(fdnH) SBO_1583(fdnG) SBO_3906(fdoI)
                 SBO_3908(fdoG)
            SDY: SDY_1605(fdnH) SDY_1606(fdnI) SDY_3849(fdoG) SDY_3851(fdoI)
            ECA: ECA1250(fdhF) ECA1406(fdnI) ECA1407(fdnH) ECA1408(fdnG)
                 ECA1507
            PLU: plu4888(fdoH) plu4889(fdoI)
            ENT: Ent638_1750 Ent638_2054 Ent638_2055 Ent638_2347 Ent638_4084
                 Ent638_4085
            SPE: Spro_0084
            HIN: HI0007(fdxH) HI0008(fdxI)
            HIT: NTHI0007(fdxG) NTHI0010(fdxH) NTHI0011(fdxI)
            HDU: HD1111(fdnI)
            PMU: PM0406(fdxI) PM0407(fdxH) PM0408(fdxG_1) PM0409(fdxG_2)
            MSU: MS0732 MS0889(fdnI) MS0890(hybA) MS0891(bisC) MS0892(bisC)
                 MS1028(fdnI) MS1030(bisC)
            APL: APL_0892(fdxG) APL_0893(fdxG) APL_0895(fdnI)
            ASU: Asuc_1264 Asuc_1265
            XCC: XCC2354 XCC2664
            XCB: XC_1452 XC_1762
            XCV: XCV2664
            XAC: XAC2486
            XOO: XOO2789
            XOM: XOO_2630(XOO2630)
            VCH: VC1511 VC1512
            VVU: VV1_2590 VV1_2591 VV1_2592
            VVY: VV1698 VV1699 VV1700
            VPA: VP1513 VP1514 VP1515
            PPR: PBPRA1860 PBPRA1861 PBPRA1862 PBPRB1370
            PAE: PA4810(fdnI) PA4811(fdnH)
            PAU: PA14_63570(fdnI) PA14_63580(fdnH) PA14_63605(fdnG)
            PAP: PSPA7_5529 PSPA7_5530(fdxH) PSPA7_5531 PSPA7_5532
            PPU: PP_0490 PP_0491 PP_2183 PP_2184 PP_2185 PP_2186
            PPF: Pput_0523
            PSP: PSPPH_3292 PSPPH_4690
            PFL: PFL_0328 PFL_0329 PFL_0330 PFL_0331 PFL_4861
            PFO: Pfl_2698 Pfl_2699 Pfl_2700
            PEN: PSEEN0240 PSEEN0563(fdoG) PSEEN0564(fdnG) PSEEN0565(fdnH)
                 PSEEN0566(fdnI) PSEEN1826 PSEEN1827 PSEEN1828 PSEEN1829
                 PSEEN2409 PSEEN4042
            PCR: Pcryo_1602
            ACI: ACIAD1916(fdhD)
            SON: SO_0101(fdnG) SO_0102(fdnH) SO_0103(fdnI) SO_4509
                 SO_4510(fdhB-1) SO_4511 SO_4513 SO_4514(fdhB-2) SO_4515
            SFR: Sfri_0059
            SPL: Spea_0438
            SHE: Shewmr4_0101 Shewmr4_0102 Shewmr4_0103 Shewmr4_0104
                 Shewmr4_3722 Shewmr4_3726
            SHM: Shewmr7_0096 Shewmr7_0097 Shewmr7_0098 Shewmr7_0099
                 Shewmr7_3793 Shewmr7_3797
            SHN: Shewana3_0103 Shewana3_0104 Shewana3_0875 Shewana3_1872
                 Shewana3_2056 Shewana3_2089 Shewana3_2090 Shewana3_2091
                 Shewana3_3916 Shewana3_3917 Shewana3_3918 Shewana3_3920
                 Shewana3_3921 Shewana3_3922
            CPS: CPS_2056(fdhG1) CPS_2057(fdhB1) CPS_2058(fdhA1) CPS_2060
                 CPS_4022(fdhG2) CPS_4023(fdhB2) CPS_4024(fdhA2) CPS_4026
            PAT: Patl_2236 Patl_2844
            MAQ: Maqu_0643
            LPN: lpg0283
            LPF: lpl0335
            LPP: lpp0359
            MCA: MCA1208 MCA1209 MCA1210 MCA1389 MCA1391 MCA1392 MCA1393
                 MCA2576
            FTU: FTT1698c(fdh)
            FTF: FTF1698c(fdh)
            FTL: FTL_0127
            FTH: FTH_0119
            FTA: FTA_0136 FTA_0137 FTA_1993
            FTN: FTN_1719
            AEH: Mlg_0635 Mlg_2513
            HHA: Hhal_0353 Hhal_1166
            CSA: Csal_0997 Csal_1917 Csal_2691 Csal_2727
            AHA: AHA_2495(fdhA) AHA_3061 AHA_3062 AHA_3063
            CVI: CV_1622 CV_1624(fdhD) CV_3839(fdnG) CV_3840(fdoH)
                 CV_3841(fdoI)
            RSO: RS02045(RSp0070) RS02385(RSp1048) RSc2370(RS01176)
                 RSc2372(RS01174) RSc2373(RS01173)
            REU: Reut_A0619 Reut_A0621 Reut_A0682 Reut_A0683 Reut_A0685
                 Reut_B4091 Reut_B4651
            REH: H16_A0640(fdsG) H16_A0641(fdsB) H16_A0642(fdsA)
                 H16_A0644(fdsD) H16_A2932(fdhD1) H16_A2934(fdhC)
                 H16_A2936(fdhB1) H16_A2937(fdhA1) H16_A3292 H16_B1383(cbbB)
                 H16_B1452(fdoG) H16_B1453(fdoH) H16_B1454(fdoI)
                 H16_B1470(fdhD2) H16_B1471(fdhA2) H16_B1700(fdwA)
                 H16_B1701(fdwB)
            RME: Rmet_0553 Rmet_0555 Rmet_0557 Rmet_1124 Rmet_2758 Rmet_2761
            BMA: BMA0448 BMA0449 BMA0450(fdhF) BMA0451 BMAA1681(fdoI)
                 BMAA1682(fdoH)
            BMV: BMASAVP1_1691 BMASAVP1_1692 BMASAVP1_1693(fdoH)
                 BMASAVP1_1694(fdoI) BMASAVP1_A2593 BMASAVP1_A2594
                 BMASAVP1_A2595(fdhF) BMASAVP1_A2596
            BML: BMA10299_1897 BMA10299_1898 BMA10299_1900(fdoH)
                 BMA10299_1901(fdoI) BMA10299_A0965 BMA10299_A0966
                 BMA10299_A0967(fdhF)
            BMN: BMA10247_0180(fdhF) BMA10247_0181 BMA10247_0182
                 BMA10247_A0569 BMA10247_A0570 BMA10247_A0572(fdoH)
                 BMA10247_A0573(fdoI)
            BXE: Bxe_A0963(fdhD) Bxe_A0964(fdhA) Bxe_A0965(fdhB)
                 Bxe_A0966(fdhC) Bxe_A1486 Bxe_A4034 Bxe_B1304 Bxe_B2551
                 Bxe_B2552 Bxe_B2553 Bxe_B2554
            BVI: Bcep1808_3758 Bcep1808_4486 Bcep1808_5104
            BUR: Bcep18194_A3632 Bcep18194_A4143 Bcep18194_A4144
                 Bcep18194_B1265 Bcep18194_B1346 Bcep18194_B2001
                 Bcep18194_B2098 Bcep18194_B2100 Bcep18194_B2101
                 Bcep18194_C6997 Bcep18194_C7007
            BCN: Bcen_0552 Bcen_1398 Bcen_3789 Bcen_4380 Bcen_4381 Bcen_4382
            BCH: Bcen2424_1031 Bcen2424_3984 Bcen2424_3985 Bcen2424_3986
                 Bcen2424_4579 Bcen2424_6422 Bcen2424_6431
            BAM: Bamb_0894 Bamb_0895 Bamb_3376 Bamb_3377 Bamb_3378 Bamb_3379
                 Bamb_4006
            BPS: BPSL2528(fdsG) BPSL2529(fdsB) BPSL2530(fdsA) BPSL2531(fdsD)
                 BPSS1665(fdoI) BPSS1666(fdoH) BPSS1667(fdoG)
            BPM: BURPS1710b_3010(fdsG) BURPS1710b_3011(fdsB)
                 BURPS1710b_3012(fdsA) BURPS1710b_3013(fdsD) BURPS1710b_A0728
                 BURPS1710b_A0729 BURPS1710b_A0730 BURPS1710b_A0732(fdoG)
                 BURPS1710b_A2579
            BPL: BURPS1106A_2962 BURPS1106A_2963 BURPS1106A_2964(fdhA)
                 BURPS1106A_2965 BURPS1106A_A2257(fdoI) BURPS1106A_A2258(fdoH)
                 BURPS1106A_A2259 BURPS1106A_A2260
            BPD: BURPS668_2900 BURPS668_2901 BURPS668_2902(fdhA) BURPS668_2903
                 BURPS668_A2394(fdoI) BURPS668_A2395(fdoH) BURPS668_A2396
                 BURPS668_A2397
            BTE: BTH_I1622 BTH_I1623 BTH_I1624 BTH_II0707 BTH_II0708(fdxH)
                 BTH_II0709 BTH_II1422
            BPE: BP1472(fdhA) BP1475(fdhC) BP1513
            BPA: BPP1103(fdsD) BPP1105(fdsA) BPP1106(fdsB) BPP1107(fdsG)
                 BPP1186 BPP1933(fdhA) BPP1934(fdhB) BPP1936(fdhC)
            BBR: BB1319(fdsD) BB1321(fdsA) BB1322(fdsB) BB1323(fdsG) BB1402
                 BB2121(fdhA) BB2122(fdhB) BB2124(fdhC)
            RFR: Rfer_3258 Rfer_3260 Rfer_3261 Rfer_3269
            POL: Bpro_0937 Bpro_0940 Bpro_2805
            VEI: Veis_4915
            MPT: Mpe_A0337 Mpe_A1170 Mpe_A1171 Mpe_A1173 Mpe_A3708 Mpe_A3709
                 Mpe_A3710 Mpe_A3712
            HAR: HEAR0358 HEAR0433 HEAR1412 HEAR3342 HEAR3432 HEAR3442
            MMS: mma_0132 mma_0402(fdhB1) mma_0403(fdhA1) mma_1967(fdhC)
                 mma_1969(fdhB2) mma_1970(fdhA2) mma_3652(fdsA) mma_3654(fdnI)
                 mma_3661(fdh)
            EBA: ebA2749(fdhA) ebA2933(fdhC) ebA2935(fdhB) ebA2936(fdhA)
            AZO: azo3038(fdhA1) azo3482(fdhA2)
            DAR: Daro_1816 Daro_1817 Daro_1818
            MFA: Mfla_0338 Mfla_0718 Mfla_0720 Mfla_0722
            HPA: HPAG1_0616
            HHE: HH0058(hyaC) HH0226(fdhC) HH0227(fdhB) HH0228
            HAC: Hac_0746(hyaC)
            WSU: WS0027(fdhC) WS0028(fdhB) WS0029(fdhA) WS0126(flpF)
                 WS0733(fdhA) WS0735(fdhB) WS0736(fdhC) WS1146(fdhA)
                 WS1147(fdhB) WS1148(fdhC)
            TDN: Tmden_0819 Tmden_0820 Tmden_0821 Tmden_1902
            CJE: Cj1509c(fdhC) Cj1510c(fdhB) Cj1511c(fdhA)
            CJR: CJE1682(fdhC) CJE1683(fdhB) CJE1684(fdhA)
            CJJ: CJJ81176_1501(fdhC) CJJ81176_1502(fdhB) CJJ81176_1503(fdhA)
            CJU: C8J_1412(fdhC) C8J_1413(fdhB)
            CJD: JJD26997_1861(fdhC) JJD26997_1862(fdhB)
            ABU: Abu_1497(fdhB1) Abu_1498 Abu_1510(fdhB2) Abu_1511(fdhA2)
            NIS: NIS_1552(fdhF)
            SUN: SUN_0228
            GSU: GSU0777(fdnG) GSU0778(fdnH)
            GME: Gmet_1059 Gmet_1060
            GUR: Gura_1285
            DVU: DVU0587(fdnG-1) DVU2482(fdnG-2) DVU2811 DVU2812(fdnG-3)
            DVL: Dvul_2365
            DDE: Dde_0473 Dde_0680 Dde_0716 Dde_0717 Dde_0812 Dde_0813
                 Dde_3512 Dde_3513 Dde_3514
            DPS: DP0481 DP0682 DP1767 DP1768 DP1769 DP2986 DP2987 DP2988
            ADE: Adeh_0824 Adeh_1170 Adeh_2088 Adeh_2089 Adeh_3754 Adeh_3756
            AFW: Anae109_2008 Anae109_3043
            SAT: SYN_00634 SYN_00635
            SFU: Sfum_0035 Sfum_0036 Sfum_0037 Sfum_0822 Sfum_1274 Sfum_2706
                 Sfum_2742 Sfum_3509 Sfum_3510
            PUB: SAR11_0679(fdhF) SAR11_0680(fdsB) SAR11_0681(fdhD)
            MLO: mll5393 mll5396 mll5397 mll5398 mll9633
            MES: Meso_2427 Meso_2451
            SME: SMa0002(fdoG) SMa0005(fdoH) SMa0007(fdoI) SMa0478
                 SMc02524(fdsG) SMc02525(fdsB) SMc03086(fdsD) SMc04444(fdsA)
            ATU: Atu4706(nuoE) Atu4707(nuoF) Atu4708(fdhF) Atu4709(fdsD)
            ATC: AGR_L_346 AGR_L_347 AGR_L_349 AGR_L_350
            RET: RHE_CH03855(fdsD) RHE_CH03857(fdsA) RHE_CH03858(fdsB)
                 RHE_CH03859(fdsG) RHE_PF00416
            RLE: RL4389 RL4391(fdsA) RL4392(fdsB) RL4393(fdsG) pRL120509
            OAN: Oant_2863
            BJA: bll0280(fdhF) bll3136(fdhF) bll3137(nuoF) bll3138(nuoE)
                 bll5475 bll5476 bll5478 blr2317 bsl3134
            BRA: BRADO4975(fdsG) BRADO4976(fdsB) BRADO4977(fdsA)
                 BRADO4979(fdsD)
            BBT: BBta_3087(fdsD) BBta_3089(fdsA) BBta_3090(fdsB)
                 BBta_3091(fdsG) BBta_3664 BBta_6354
            RPA: RPA0380 RPA0732(fdsG) RPA0733(fdsB) RPA0734(fdsA)
                 RPA0735(fdsC) RPA0736(fdsD)
            RPB: RPB_0204 RPB_0443 RPB_0722 RPB_0724 RPB_0726
            RPC: RPC_1201 RPC_4578 RPC_4643 RPC_4645
            RPD: RPD_0346 RPD_0621 RPD_0623 RPD_0624 RPD_0625
            RPE: RPE_3650 RPE_4645 RPE_4647 RPE_4649
            NHA: Nham_3128
            XAU: Xaut_0662
            SIL: SPO0833 SPO0834 SPO1555 SPO1556 SPO1794 SPO1795 SPO1796
            SIT: TM1040_0402 TM1040_0403 TM1040_3190
            RSP: RSP_1078(fdsG) RSP_1079(fdsB) RSP_1080(fdsA) RSP_1082(fdsD)
                 RSP_1821
            RSH: Rsph17029_0469
            JAN: Jann_2558
            RDE: RD1_2895(fdhI) RD1_2896(fdhB) RD1_2897(fdhA) RD1_3410(fdhD)
                 RD1_4233(fdhB) RD1_4234(fdhA)
            PDE: Pden_1161 Pden_2829 Pden_4009
            MMR: Mmar10_2684
            NAR: Saro_0735 Saro_0736
            SAL: Sala_0186
            SWI: Swit_4198
            GBE: GbCGDNIH1_0813 GbCGDNIH1_1932 GbCGDNIH1_1933 GbCGDNIH1_1934
                 GbCGDNIH1_1936
            RRU: Rru_A0324 Rru_A2119
            MAG: amb0170 amb2671 amb2672 amb2674
            ABA: Acid345_0454 Acid345_0869 Acid345_0870 Acid345_2291
            SUS: Acid_0837 Acid_0838
            BSU: BG12294(yrhE) BG13190(yjgC) BG13476(yoaE)
            BHA: BH2530 BH2853
            BAN: BA0589 BA3631
            BAR: GBAA0589
            BAA: BA_4120
            BAT: BAS0557 BAS3367
            BCE: BC0589 BC3573
            BCA: BCE_0655 BCE_3588
            BCZ: BCZK0500(fdhD) BCZK0501(fdhF) BCZK3281(fdhF) BCZK3485(fdhC)
            BTK: BT9727_0499(fdhF) BT9727_3331(fdhF)
            BTL: BALH_0528(fdhD) BALH_0529(fdhF) BALH_3209(fdhD)
            BLI: BL01398 BL02109(yrhE) BL04035 BL05207
            BLD: BLi02222(yjgC) BLi02766(yrhE) BLi03918
            BCL: ABC0900
            BAY: RBAM_012270(yjgC)
            OIH: OB0770
            GKA: GK0459
            SAU: SA0171(fdh) SA2102
            SAV: SAV0177(fdh) SAV2309
            SAM: MW0151(fdh) MW2229
            SAR: SAR0178 SAR2393
            SAS: SAS0152 SAS2201
            SAC: SACOL0162 SACOL2301
            SAB: SAB0117 SAB2186c
            SAA: SAUSA300_0179 SAUSA300_2258
            SAO: SAOUHSC_00142 SAOUHSC_02582
            SHA: SH0748
            SSP: SSP0601 SSP2393
            LMO: lmo2586
            LMF: LMOf2365_2558
            LIN: lin2731
            LWE: lwe2536
            EFA: EF1390(fdhA)
            STH: STH112 STH2600 STH2601 STH2602 STH3099 STH3295
            CDF: CD3317(fdhF)
            CHY: CHY_0733(fdhA) CHY_0793(fdoG) CHY_0794(fdoH) CHY_0795(fdoI)
            DSY: DSY3099(fdoI) DSY3100(fdnH) DSY3101(fdnG) DSY3968(fdhF)
                 DSY4711
            DRM: Dred_1113 Dred_1114 Dred_1330
            SWO: Swol_0786 Swol_0797 Swol_0799 Swol_1823 Swol_1824 Swol_1825
            MTA: Moth_0450 Moth_0452 Moth_1243 Moth_2193 Moth_2312
            MMO: MMOB2210(focA)
            MTU: Rv2900c(fdhF)
            MBO: Mb2924c(fdhF)
            MBB: BCG_2921c(fdhF)
            MPA: MAP0367 MAP0368 MAP0369 MAP3680c
            MAV: MAV_0422 MAV_4930
            MSM: MSMEG_0159 MSMEG_0160 MSMEG_0161 MSMEG_0162 MSMEG_3521
                 MSMEG_4668
            MVA: Mvan_3010 Mvan_4032
            MGI: Mflv_2249 Mflv_2594 Mflv_3288
            MMC: Mmcs_2009 Mmcs_2721 Mmcs_3942 Mmcs_5220
            MKM: Mkms_2055 Mkms_2765 Mkms_4016 Mkms_5308
            MJL: Mjls_2751 Mjls_3956 Mjls_5600
            CGL: NCgl0507(cgl0529)
            CGB: cg0616(fdhD) cg0618(fdhF)
            RHA: RHA1_ro00413 RHA1_ro02585
            SCO: SCO6561(SC4B5.11c)
            SMA: SAV1834(fdnG) SAV1941(fdh)
            ART: Arth_0908
            NCA: Noca_2934
            TFU: Tfu_1737
            FAL: FRAAL2445 FRAAL2446(fdhD)
            ACE: Acel_0610
            KRA: Krad_1602
            SEN: SACE_1383 SACE_3562 SACE_4509
            RXY: Rxyl_0146 Rxyl_2724
            RBA: RB8598(fdhF)
            AVA: Ava_3783 Ava_4544
            CCH: Cag_0620 Cag_0954 Cag_1031
            CPH: Cpha266_0120 Cpha266_2562
            DET: DET0112 DET0187
            DEH: cbdb_A131 cbdb_A195(fdnG)
            DEB: DehaBAV1_0165
            RRS: RoseRS_1793
            DGE: Dgeo_0402 Dgeo_2746
            TTJ: TTHB197
            AAE: aq_1039(fdoG) aq_1046(fdoH) aq_1049(fdoI)
            MJA: MJ0005 MJ0006 MJ0155 MJ1353m(fdhF)
            MMP: MMP0138(fdhA) MMP0139(fdhB) MMP0979 MMP1297(fdhB)
                 MMP1298(fdhA)
            MMQ: MmarC5_0295 MmarC5_1538
            MBA: Mbar_A1561 Mbar_A1562
            MHU: Mhun_1814 Mhun_1833 Mhun_2020 Mhun_2021
            MTH: MTH1139 MTH1140 MTH1552 MTH1714 MTH1736 MTH1737
            MST: Msp_0639(fdhB) Msp_0640(fdhA)
            MSI: Msm_1404 Msm_1462 Msm_1463
            MKA: MK0321 MK0322 MK0725(hycB)
            HMA: pNG7151(fdhA) pNG7318(fdhG) rrnAC1332(fdhF) rrnAC1333(fdoH)
            HWA: HQ1129A(fdhAI) HQ1130A(fdhAII) HQ1132A(fdhA)
            NPH: NP3710A(fdhA_2a) NP3714A(fdhA_2b) NP4944A(fdhC)
                 NP4946A(fdhB_1) NP4960A(fdhB_2) NP4962A(fdhA_1)
            TAC: Ta0045m Ta0425
            TVO: TVN0002 TVN0243
            PTO: PTO1039
            PHO: PH0893 PH1353
            PAB: PAB1389 PAB1390 PAB2442(fdhA-like)
            PFU: PF1521
            TKO: TK0214 TK2076 TK2077
            RCI: RCIX1628(fdhA-1) RCIX1630(fdhB-1) RCIX1643(fdhD-2)
                 RCIX2372(fdhB-2) RCIX2373(fdhA-2) RCIX2376(fdhB-3)
                 RCIX2378(fdhA-3) RCIX572(fdhD-1) RRC251(fdhA-4) RRC252(fdhB-4)
            APE: APE_2556.1
            SSO: SSO1029(fdhF-1) SSO2824(fdhF-2)
            STO: ST0081
            SAI: Saci_0320(fdhF)
            PAI: PAE2660 PAE2661 PAE2662
            PCL: Pcal_0396
            TPE: Tpen_1408 Tpen_1631
STRUCTURES  PDB: 1AA6  1FDI  1FDO  1KQF  1KQG  2FSS  2GO1  2GUG  2IV2  2J6I  
                 2NAC  2NAD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.2
            ExPASy - ENZYME nomenclature database: 1.2.1.2
            ExplorEnz - The Enzyme Database: 1.2.1.2
            ERGO genome analysis and discovery system: 1.2.1.2
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.2
            BRENDA, the Enzyme Database: 1.2.1.2
            CAS: 9028-85-7
///
ENTRY       EC 1.2.1.3                  Enzyme
NAME        aldehyde dehydrogenase (NAD+);
            CoA-independent aldehyde dehydrogenase;
            m-methylbenzaldehyde dehydrogenase;
            NAD-aldehyde dehydrogenase;
            NAD-dependent 4-hydroxynonenal dehydrogenase;
            NAD-dependent aldehyde dehydrogenase;
            NAD-linked aldehyde dehydrogenase;
            propionaldehyde dehydrogenase;
            aldehyde dehydrogenase (NAD)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     aldehyde:NAD+ oxidoreductase
REACTION    an aldehyde + NAD+ + H2O = an acid + NADH + H+ [RN:R00632]
ALL_REAC    R00632 > R00538 R00631 R00710 R00904 R01752 R02549 R02678 R02940
            R03283 R03869 R04065 R04506 R04903 R05050 R05119 R05286 R06366;
            (other) R00711 R01986 R02957 R05237 R05238
SUBSTRATE   aldehyde [CPD:C00071];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     acid [CPD:C00174];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Wide specificity, including oxidation of D-glucuronolactone to
            D-glucarate.
REFERENCE   1
  AUTHORS   Jakoby, W.B.
  TITLE     Aldehyde dehydrogenases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
REFERENCE   2
  AUTHORS   Racker, E.
  TITLE     Aldehyde dehydrogenase, a diphosphopyridine nucleotide-linked
            enzyme.
  JOURNAL   J. Biol. Chem. 177 (1949) 883-892.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00053  Ascorbate and aldarate metabolism
            PATH: map00071  Fatty acid metabolism
            PATH: map00120  Bile acid biosynthesis
            PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00310  Lysine degradation
            PATH: map00340  Histidine metabolism
            PATH: map00380  Tryptophan metabolism
            PATH: map00410  beta-Alanine metabolism
            PATH: map00561  Glycerolipid metabolism
            PATH: map00620  Pyruvate metabolism
            PATH: map00631  1,2-Dichloroethane degradation
            PATH: map00640  Propanoate metabolism
            PATH: map00641  3-Chloroacrylic acid degradation
            PATH: map00650  Butanoate metabolism
            PATH: map00903  Limonene and pinene degradation
ORTHOLOGY   KO: K00128  aldehyde dehydrogenase (NAD+)
GENES       HSA: 217(ALDH2) 218(ALDH3A1) 219(ALDH1B1) 220(ALDH1A3)
                 223(ALDH9A1) 224(ALDH3A2) 501(ALDH7A1)
            PTR: 462033(ALDH7A1) 464931(ALDH1B1)
            MMU: 110695(Aldh7a1) 11669(Aldh2) 11671(Aldh3a2) 56752(Aldh9a1)
                 72535(Aldh1b1)
            RNO: 29539(Aldh2) 29651(Aldh1a7) 64040(Aldh9a1) 65183(Aldh3a2)
            CFA: 479518(ALDH3A2) 481486(ALDH7A1) 481620(ALDH1B1) 610941(ALDH2)
            GGA: 416880(ALDH2) 417615(ALDH3A2) 426812(ALDH7A1)
            XLA: 446857(MGC80785) 447522(MGC83352)
            XTR: 448267(aldh2)
            DRE: 323653(aldh3a2) 334197(aldh7a1) 393462(aldh2a)
            SPU: 581754(LOC581754) 588376(LOC588376)
            DME: Dmel_CG31075 Dmel_CG3752(Aldh) Dmel_CG9629
            CEL: F01F1.6(alh-9) F54D8.3(alh-1) K04F1.15(alh-2)
            ATH: AT1G23800(ALDH2B7) AT3G48000(ALDH2B4)
            OSA: 4330612 4340725 4347172
            CME: CMO345C
            SCE: YER073W(ALD5) YOR374W(ALD4) YPL061W(ALD6)
            AGO: AGOS_ACL044W AGOS_ADR417W
            PIC: PICST_28221(ALD7) PICST_29563(ALD5) PICST_40468(UGA2)
                 PICST_44169(ALD4) PICST_55391(PUT2) PICST_57266(UGA22)
                 PICST_60847(ALD3) PICST_63844(ALD2) PICST_90594(MSC7)
            CGR: CAGL0D06688g CAGL0H05137g CAGL0J03212g
            SPO: SPAC9E9.09c
            ANI: AN0554.2
            AFM: AFUA_2G00720 AFUA_4G08600 AFUA_6G11430 AFUA_7G01000
            AOR: AO090001000162 AO090023000467
            ANG: An08g07290(aldA)
            CNE: CNA07130 CND02060 CNF03900 CNL05070 CNM00220 CNM00290
            UMA: UM02508.1 UM03402.1 UM03665.1
            DDI: DDB_0231474 DDB_0231504
            TET: TTHERM_00405530 TTHERM_00530250 TTHERM_00678220
            TBR: Tb927.6.3050 Tb927.6.4210
            TCR: 507023.120 511751.120
            LMA: LmjF25.1120
            EHI: 11.t00020
            YPS: YPTB2197
            PLU: plu0142
            MSU: MS2132(putA)
            XCC: XCC0101(aldA) XCC0809(badH) XCC1791 XCC2410
            XCB: XC_0104 XC_1702 XC_2445 XC_3421
            XCV: XCV0105 XCV0917 XCV1838 XCV2743 XCV4345
            XAC: XAC0129(aldA) XAC0882(badH) XAC1808 XAC2546 XAC4238(alkH)
            XOO: XOO2240 XOO3136 XOO3729(badH)
            XOM: XOO_2105(XOO2105) XOO_2978(XOO2978) XOO_3521(XOO3521)
            VCH: VC0819 VC1819
            VCO: VC0395_0175 VC0395_A0344(aldA-1) VC0395_A1414(aldA-2)
            VVU: VV2_0869
            VVY: VVA1341
            VPA: VP1703 VP1776 VP1777
            PPR: PBPRB0309(aldA)
            PAE: PA0219 PA1027 PA1984 PA4022 PA4073 PA4189 PA4899
            PAU: PA14_51050(pcd) PA14_64740(pchA)
            PAP: PSPA7_1085
            PPU: PP_0545 PP_2589 PP_2680 PP_2694 PP_3463 PP_5258
            PPF: Pput_2306
            PST: PSPTO_0728 PSPTO_1891(pcD) PSPTO_3064 PSPTO_3644
            PSB: Psyr_0629 Psyr_3402 Psyr_3514 Psyr_3524
            PSP: PSPPH_3324 PSPPH_3456(pcd) PSPPH_3466 PSPPH_4666
            PFL: PFL_0596 PFL_0801 PFL_2222 PFL_2342 PFL_3475 PFL_3523
                 PFL_3648 PFL_4130 PFL_5469
            PFO: Pfl_0550 Pfl_0828 Pfl_2123 Pfl_2261 Pfl_4933 Pfl_4989
            PEN: PSEEN0634(aldB) PSEEN2586 PSEEN2886 PSEEN2956 PSEEN2978
                 PSEEN5402
            PAR: Psyc_1350 Psyc_1612
            PCR: Pcryo_0895 Pcryo_1015 Pcryo_1216 Pcryo_1815 Pcryo_1844
            ACI: ACIAD0131 ACIAD1577 ACIAD2018(ald1) ACIAD2542
            SON: SO_4480(aldA)
            SDN: Sden_2339
            SFR: Sfri_0883
            SAZ: Sama_2648 Sama_3435
            SBL: Sbal_0248 Sbal_1093
            SLO: Shew_0967 Shew_3574
            SPC: Sputcn32_0364 Sputcn32_1085
            SHE: Shewmr4_0249
            SHM: Shewmr7_3772
            SHN: Shewana3_0250
            SHW: Sputw3181_0214 Sputw3181_3079
            ILO: IL1993
            CPS: CPS_1451(aldH) CPS_1885 CPS_3862 CPS_4669
            PHA: PSHAb0219(aldB)
            PAT: Patl_1874
            PIN: Ping_2539
            MAQ: Maqu_3410
            LPN: lpg1351
            LPF: lpl1304
            LPP: lpp1305
            FTU: FTT0552
            FTF: FTF0552
            FTL: FTL_1009
            FTN: FTN_0963
            NOC: Noc_1710 Noc_2605 Noc_2916
            AEH: Mlg_2726
            HCH: HCH_01490 HCH_01852 HCH_03162
            CSA: Csal_0142 Csal_0348 Csal_2460 Csal_2913
            ABO: ABO_0087(aldH) ABO_0962(aldh1) ABO_2709(alkH)
            AHA: AHA_1248 AHA_3818
            CVI: CV_0393(aldB) CV_1222 CV_2491
            RSO: RS02148(RSp1591) RSc0161(RS01031) RSc2350(RS01196)
                 RSc3128(exaC)
            REU: Reut_A1459 Reut_A1478 Reut_A1903 Reut_A2614 Reut_A3050
                 Reut_B3678 Reut_B3763 Reut_B3858 Reut_B4074 Reut_B4159
                 Reut_B4750 Reut_B5279 Reut_C5935
            REH: H16_A0232 H16_A0745 H16_A1114 H16_A1495 H16_B0212 H16_B0421
                 H16_B0737 H16_B0833 H16_B1534 H16_B1735 H16_B1751 H16_B1835
                 H16_B1960(exaC) H16_B2444
            RME: Rmet_0677 Rmet_1898 Rmet_3207 Rmet_3632 Rmet_4856 Rmet_5017
                 Rmet_5128
            BMA: BMA0735 BMA1306(aldA) BMA2986 BMAA0779 BMAA1451
            BMV: BMASAVP1_0311 BMASAVP1_A1793(aldA)
            BML: BMA10299_0587 BMA10299_2162 BMA10299_A0102(aldA)
            BMN: BMA10247_1063(aldA) BMA10247_A0846 BMA10247_A0980
            BXE: Bxe_A0172 Bxe_A1826 Bxe_A2720 Bxe_A3401 Bxe_A3562 Bxe_A3599
                 Bxe_B0975 Bxe_B1006 Bxe_B1400 Bxe_B1418 Bxe_B1492 Bxe_B2149
                 Bxe_B2260 Bxe_B2718 Bxe_C0773 Bxe_C1164 Bxe_C1274 Bxe_C1357
            BVI: Bcep1808_0140 Bcep1808_2504 Bcep1808_3076
            BUR: Bcep18194_A3314 Bcep18194_A3630 Bcep18194_A5745
                 Bcep18194_A6492 Bcep18194_B0380 Bcep18194_B0607
                 Bcep18194_B1988 Bcep18194_B2311 Bcep18194_B2693
                 Bcep18194_C6645 Bcep18194_C6749 Bcep18194_C6756
                 Bcep18194_C7306 Bcep18194_C7342
            BCN: Bcen_1806 Bcen_2528 Bcen_2921 Bcen_3097 Bcen_3311 Bcen_4580
                 Bcen_5539
            BCH: Bcen2424_0134 Bcen2424_2418 Bcen2424_3141 Bcen2424_3783
                 Bcen2424_5056 Bcen2424_5270 Bcen2424_5904
            BAM: Bamb_0124 Bamb_2463 Bamb_3193 Bamb_6411
            BPS: BPSL1020 BPSL1550 BPSL3369(acoD) BPSS0307 BPSS1466
            BPM: BURPS1710b_0138(acoD) BURPS1710b_1235 BURPS1710b_2213(dhaS)
                 BURPS1710b_2317(aldA) BURPS1710b_A0495 BURPS1710b_A1857
                 BURPS1710b_A2502
            BTE: BTH_I0877 BTH_I2271 BTH_I3247 BTH_II0898 BTH_II2092
            BPE: BP0207 BP0360 BP0465 BP1858(aldH) BP2157(acoD)
            BPA: BPP0670 BPP1323(acoD) BPP2166 BPP2426 BPP4173 BPP4379
            BBR: BB0651 BB0677 BB0744 BB1563 BB1875 BB2388(acoD) BB4643 BB4965
            RFR: Rfer_0452 Rfer_0880 Rfer_1025 Rfer_2866 Rfer_3228
            POL: Bpro_2290 Bpro_3422 Bpro_3952 Bpro_4570 Bpro_5303
            PNA: Pnap_3013
            AAV: Aave_2664 Aave_3230
            AJS: Ajs_1756 Ajs_1890
            VEI: Veis_2689 Veis_3004 Veis_3514
            MPT: Mpe_A0599 Mpe_A1909 Mpe_A2577
            EBA: ebA2242(dhaL) ebA3161(pchA) ebA4625(aldB) ebA6190
            AZO: azo0215(aldH) azo2852(cddD) azo2939(aldA) azo3054
            DAR: Daro_1008
            ABU: Abu_0378(ald)
            PCA: Pcar_1496
            DDE: Dde_3121
            BBA: Bd2266(aldH)
            DPS: DP2332
            MXA: MXAN_0625 MXAN_0626 MXAN_5040
            SAT: SYN_00265
            SFU: Sfum_1309
            PUB: SAR11_0756(aldA) SAR11_0796(aldH) SAR11_1328
            MLO: mll1015 mll2219 mll2319 mll2867 mll4783 mll6639 mll7045
                 mlr3049 mlr5236 mlr6969
            MES: Meso_0313 Meso_1958 Meso_2524 Meso_3627 Meso_4607
            SME: SMA2213 SMa0796 SMa1844 SMb20891 SMb21301 SMc01971 SMc04385
            ATU: Atu3401 Atu3950 Atu4153 Atu4241(dhaS) Atu4849 Atu5228(dhaS)
            ATC: AGR_L_1241 AGR_L_1402 AGR_L_1806 AGR_L_2842 AGR_L_75
                 AGR_pAT_320
            RET: RHE_CH03161(ypch01101) RHE_CH03723(ypch01337)
                 RHE_CH04055(ypch01434) RHE_PC00026(dhaS) RHE_PF00196(ypf00094)
                 RHE_PF00338(ypf00170) RHE_PF00359(ypf00186)
            RLE: RL2745 RL3613 RL4267(acoD) RL4585(pcd) pRL100246 pRL110154
                 pRL110175 pRL120630
            BME: BMEI1740 BMEI1747 BMEII0124 BMEII0125 BMEII0141 BMEII0142
                 BMEII0242 BMEII0282 BMEII0608
            BMF: BAB1_0211 BAB2_0566 BAB2_0976
            BMS: BR0202 BR0210 BRA0673 BRA1014
            BMB: BruAb1_0205 BruAb2_0555 BruAb2_0954
            BJA: bll4784 bll6322 bll7607 blr2816 blr3776(betB) blr5873
            BRA: BRADO1563 BRADO2102 BRADO2593 BRADO5849
            BBT: BBta_1249 BBta_1974 BBta_2411 BBta_2939 BBta_6489 BBta_7827
            RPA: RPA0467 RPA1206 RPA2153
            RPB: RPB_0573 RPB_3249
            RPC: RPC_0573 RPC_1964 RPC_3193
            RPE: RPE_0105 RPE_2260 RPE_4234
            NWI: Nwi_2515
            NHA: Nham_3110
            BHE: BH03830(aldA)
            BQU: BQ02840(aldA)
            CCR: CC_0419 CC_0822 CC_1216
            SIL: SPO0235 SPO3191 SPO3368 SPO3382 SPOA0353
            SIT: TM1040_0074 TM1040_0096 TM1040_0515 TM1040_2655 TM1040_3321
                 TM1040_3381 TM1040_3621
            RSP: RSP_1292 RSP_1507 RSP_2372 RSP_3740 RSP_4003(dhaL)
            JAN: Jann_0786 Jann_3747 Jann_3789 Jann_4025 Jann_4156
            RDE: RD1_0633(ald) RD1_0660(ald) RD1_0840(cpnE)
            PDE: Pden_1051 Pden_1054 Pden_2366 Pden_3898
            NAR: Saro_1197 Saro_2503 Saro_2869
            SAL: Sala_0154 Sala_0871 Sala_1810 Sala_2454
            SWI: Swit_0732 Swit_4806
            GOX: GOX2110
            GBE: GbCGDNIH1_1022
            RRU: Rru_A0285 Rru_A0931
            ABA: Acid345_1381 Acid345_1459
            SUS: Acid_1786 Acid_6729
            BSU: BG10604(ywdH) BG11159(ycbD) BG11355(aldX) BG11903(aldY)
                 BG12582(dhaS)
            BHA: BH0539(dhaS) BH0681(aldA) BH0865 BH1005 BH2010
            BAN: BA1296(ywdH) BA2831(aldA) BA3609(dhaS)
            BAR: GBAA1296(ywdH) GBAA2831(aldA) GBAA3609(dhaS)
            BAA: BA_1823 BA_3352 BA_4101
            BAT: BAS1198 BAS2640 BAS3348
            BCE: BC1285 BC2832 BC3555
            BCA: BCE_1397(ywdH) BCE_2860(aldA) BCE_3569(dhaS)
            BCZ: BCZK2556(aldA) BCZK3263(dhaS)
            BCY: Bcer98_2229
            BTK: BT9727_2591(aldA) BT9727_3313(dhaS)
            BLI: BL00585(dhaS) BL01646 BL03952(ywdH)
            BLD: BLi00285(ycbD) BLi00757(yfmT) BLi02249(dhaS) BLi04011(ywdH)
            BCL: ABC0047(dhaS) ABC0470 ABC1114 ABC1279 ABC1818 ABC3014 ABC3810
            BAY: RBAM_026600(ywdH) RBAM_036890
            BPU: BPUM_1857
            OIH: OB0222 OB0484 OB0861 OB1857 OB2534 OB2840
            GKA: GK0199 GK0374 GK0730 GK1966 GK2772 GK3198
            SAU: SA0162(aldA) SA1736(aldH) SA1924
            SAV: SAV0167(aldA) SAV1920(aldH) SAV2122
            SAM: MW0142(aldA) MW1861(aldH) MW2046
            SAR: SAR0169 SAR2013 SAR2210
            SAS: SAS0142 SAS1844 SAS2025
            SAC: SACOL0154(aldA1) SACOL1984(aldA2) SACOL2114
            SAB: SAB0108(aldA) SAB1857
            SAA: SAUSA300_0170 SAUSA300_1901(aldA2) SAUSA300_2076
            SAO: SAOUHSC_00132 SAOUHSC_02142
            SEP: SE1603 SE1720 SE2071
            SER: SERP1456(aldA-1) SERP1729 SERP2084(aldA-2)
            SHA: SH0547(aldA) SH0913 SH1033(aldH)
            SSP: SSP0762 SSP0871
            LPL: lp_0047(aldH)
            CPE: CPE2310(aldH)
            CTC: CTC02523(ywdH)
            CDF: CD2206(aldH)
            CBO: CBO1099(aldH)
            CKL: CKL_2209
            DSY: DSY1102
            MPE: MYPE3920(dhaS)
            MGA: MGA_0590(putA)
            MTU: Rv0458 Rv0768(aldA) Rv2858c(aldC)
            MTC: MT0155 MT0233 MT0474 MT0792 MT3392
            MBO: Mb0152 Mb0228c Mb0467 Mb0791(aldA) Mb2883c(aldC) Mb3321(pcd)
            MBB: BCG_0498 BCG_2880c(aldC)
            MLE: ML2639
            MPA: MAP0602(aldA_1) MAP1658 MAP2084 MAP3413(aldB) MAP3513 MAP3566
                 MAP3662c MAP3952
            MAV: MAV_1922 MAV_4691 MAV_5095 MAV_5147
            MSM: MSMEG_0455 MSMEG_0900 MSMEG_1158 MSMEG_1461 MSMEG_1543
                 MSMEG_2597 MSMEG_5859 MSMEG_6687
            MVA: Mvan_0486 Mvan_1328 Mvan_1468
            MGI: Mflv_0569 Mflv_0667 Mflv_4952
            MMC: Mmcs_0090 Mmcs_0627 Mmcs_1270 Mmcs_1637 Mmcs_4395 Mmcs_4578
            MKM: Mkms_0640 Mkms_1663 Mkms_5624
            MJL: Mjls_0620 Mjls_1610 Mjls_2239
            CGL: NCgl0523(cgl0546) NCgl2578(cgl2668) NCgl2698(cgl2796)
            CGB: cg2713(dhaS) cg3096
            CEF: CE0079 CE0555 CE2625
            CDI: DIP2115
            CJK: jk0202(aldA)
            NFA: nfa12040 nfa12210 nfa29950 nfa46630 nfa54770 nfa9820
            RHA: RHA1_ro00340 RHA1_ro00395 RHA1_ro00646 RHA1_ro02498
                 RHA1_ro03066 RHA1_ro03790 RHA1_ro03974 RHA1_ro04375
                 RHA1_ro04663 RHA1_ro05244 RHA1_ro06111 RHA1_ro06275
                 RHA1_ro06678 RHA1_ro07077 RHA1_ro08090(aldH1) RHA1_ro08151
                 RHA1_ro08917(thcA) RHA1_ro10302 RHA1_ro11056(aldH2)
            SCO: SCO1174(SCG11A.05) SCO1706(SCI30A.27c) SCO3420(SCE9.27c)
                 SCO4913(SCK13.05c) SCO5679(SC5H4.03)
            SMA: SAV1187(aldH) SAV2579 SAV3347 SAV4650 SAV6595 SAV7177(thcA)
            LXX: Lxx22600(aldA)
            ART: Arth_1723 Arth_1856 Arth_3088 Arth_3511
            AAU: AAur_0581 AAur_0746 AAur_3070 AAur_4011 AAur_pTC20196
                 AAur_pTC20215
            NCA: Noca_0846 Noca_1053 Noca_2092 Noca_4004
            TFU: Tfu_0744 Tfu_2590(gabD2)
            FRA: Francci3_2784 Francci3_2872 Francci3_2944
            FAL: FRAAL0200 FRAAL0315 FRAAL1665 FRAAL2632 FRAAL2896 FRAAL3121
                 FRAAL3375(aldH) FRAAL3552 FRAAL4413(aldH) FRAAL4757 FRAAL6082
            SEN: SACE_0343 SACE_1341(aldA) SACE_2377(thcA) SACE_2783
                 SACE_2915(thcA) SACE_3880(aldH) SACE_6014 SACE_6249 SACE_6565
                 SACE_6566
            STP: Strop_0827
            BLO: BL1124(aldH)
            RXY: Rxyl_0544 Rxyl_2925
            RBA: RB10172 RB11945 RB683 RB8941
            TDE: TDE2512
            LIL: LA0869
            LIC: LIC12761(alkH)
            LBJ: LBJ_0465
            LBL: LBL_2614
            SYN: slr0091
            SYW: SYNW1956
            SYC: syc1030_d
            SYF: Synpcc7942_0489
            SYD: Syncc9605_0497
            SYE: Syncc9902_1838
            SYG: sync_0566 sync_2080
            SYR: SynRCC307_0455
            SYX: SynWH7803_0544
            GVI: glr3848
            ANA: alr3672 alr3771
            AVA: Ava_1554 Ava_2258
            PMA: Pro0374
            PMM: PMM0331
            PMT: PMT0191
            PMN: PMN2A_1709
            PMB: A9601_03571
            PMC: P9515_03631
            PMF: P9303_21711
            PMG: P9301_03581
            PME: NATL1_04241
            TER: Tery_2599
            SRU: SRU_1228 SRU_1456 SRU_1782
            CHU: CHU_0053(dhaL)
            GFO: GFO_3401
            FPS: FP0888(aldH)
            CTE: CT1886(aldA)
            RRS: RoseRS_0265
            RCA: Rcas_0272
            DRA: DR_A0126 DR_A0348
            TTH: TTC0513
            TTJ: TTHA0865
            AAE: aq_186(aldH1)
            MAC: MA2860(aldH)
            MBA: Mbar_A2387
            MMA: MM_0048
            HAL: VNG0771G(aldY2) VNG2513G(aldY1)
            HMA: pNG7352(aldA) rrnAC0201(aldY2) rrnAC1973(aldY4)
                 rrnAC2473(aldY2) rrnAC2631(aldY1) rrnAC3036(aldY3)
                 rrnB0092(aldY7) rrnB0095(aldY6) rrnB0246(aldY5)
            NPH: NP3020A(aldH_2)
            TAC: Ta0439
            TVO: TVN1054
            PTO: PTO0225
            SSO: SSO3117(aldhT)
            SAI: Saci_1700 Saci_1857 Saci_1938
            PAI: PAE2480
STRUCTURES  PDB: 1A4Z  1AG8  1BXS  1CW3  1NZW  1NZX  1NZZ  1O00  1O01  1O02  
                 1O04  1O05  1O9J  1OF7  1OM2  1ZUM  2J6L  2ONM  2ONN  2ONO  
                 2ONP  2V1S  2V1T  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.3
            ExPASy - ENZYME nomenclature database: 1.2.1.3
            ExplorEnz - The Enzyme Database: 1.2.1.3
            ERGO genome analysis and discovery system: 1.2.1.3
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.3
            BRENDA, the Enzyme Database: 1.2.1.3
            CAS: 9028-86-8
///
ENTRY       EC 1.2.1.4                  Enzyme
NAME        aldehyde dehydrogenase (NADP+);
            NADP+-acetaldehyde dehydrogenase;
            NADP+-dependent aldehyde dehydrogenase;
            aldehyde dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     aldehyde:NADP+ oxidoreductase
REACTION    an aldehyde + NADP+ + H2O = an acid + NADPH + H+ [RN:R00634]
ALL_REAC    R00634 > R05099
SUBSTRATE   aldehyde [CPD:C00071];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     acid [CPD:C00174];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Adachi, O., Matsushita, K., Shinagawa, E. and Ameyama, M.
  TITLE     Crystallization and properties of NADP-dependent aldehyde
            dehydrogenase from Gluconobacter melanogenus.
  JOURNAL   Agric. Biol. Chem. 44 (1980) 155-164.
  ORGANISM  Gluconobacter melanogenus
REFERENCE   2
  AUTHORS   Jakoby, W.B.
  TITLE     Aldehyde dehydrogenases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
REFERENCE   3
  AUTHORS   Nakayama, T.
  TITLE     Acetic acid bacteria. II. Intracellular distribution of enzymes
            related to acetic acid fermentation, and some properties of a highly
            purified triphosphopyridine nucleotide (TPN)-dependent aldehyde
            dehydrogenase.
  JOURNAL   J. Biochem. (Tokyo) 48 (1960) 812-830.
  ORGANISM  Acetobacter sp.
REFERENCE   4  [PMID:13061400]
  AUTHORS   SEEGMILLER JE.
  TITLE     Triphosphopyridine nucleotide-linked aldehyde dehydrogenase from
            yeast.
  JOURNAL   J. Biol. Chem. 201 (1953) 629-37.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00930  Caprolactam degradation
GENES       VPA: VP1329
            BUR: Bcep18194_B0328 Bcep18194_B1897
            AAU: AAur_3317(aldH)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.4
            ExPASy - ENZYME nomenclature database: 1.2.1.4
            ExplorEnz - The Enzyme Database: 1.2.1.4
            ERGO genome analysis and discovery system: 1.2.1.4
            BRENDA, the Enzyme Database: 1.2.1.4
            CAS: 9028-87-9
///
ENTRY       EC 1.2.1.5                  Enzyme
NAME        aldehyde dehydrogenase [NAD(P)+];
            aldehyde dehydrogenase [NAD(P)+];
            ALDH
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     aldehyde:NAD(P)+ oxidoreductase
REACTION    an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+ [RN:R00632
            R00634]
ALL_REAC    R00632 > R00710 R02536 R02695 R03300 R04882 R04888 R04891 R04996;
            R00634 > R00711 R02537 R02697 R03302 R04883 R04889 R04892;
            (other) R07104
SUBSTRATE   aldehyde [CPD:C00071];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     acid [CPD:C00174];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Black, S.
  TITLE     Yeast aldehyde dehydrogenase.
  JOURNAL   Arch. Biochem. Biophys. 34 (1951) 86-97.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2
  AUTHORS   Jakoby, W.B.
  TITLE     Aldehyde dehydrogenases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
REFERENCE   3  [PMID:13319337]
  AUTHORS   KING TE, CHELDELIN VH.
  TITLE     Oxidation of acetaldehyde by Acetobacter suboxydans.
  JOURNAL   J. Biol. Chem. 220 (1956) 177-91.
  ORGANISM  Aerobacter suboxydans
REFERENCE   4  [PMID:4293780]
  AUTHORS   Steinman CR, Jakoby WB.
  TITLE     Yeast aldehyde dehydrogenase. I. Purification and crystallization.
  JOURNAL   J. Biol. Chem. 242 (1967) 5019-23.
  ORGANISM  Acetobacter peroxidans
REFERENCE   5
  AUTHORS   Tanenbaum, S.W.
  TITLE     The metabolism of Acetobacter peroxidans. I. Oxidative enzymes.
  JOURNAL   Biochim. Biophys. Acta 21 (1956) 335-342.
  ORGANISM  Acetobacter peroxidans
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00340  Histidine metabolism
            PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
            PATH: map00980  Metabolism of xenobiotics by cytochrome P450
ORTHOLOGY   KO: K00129  aldehyde dehydrogenase (NAD(P)+)
GENES       HSA: 218(ALDH3A1) 220(ALDH1A3) 221(ALDH3B1) 222(ALDH3B2)
            MMU: 11670(Aldh3a1) 56847(Aldh1a3) 67689(Aldh3b1)
            RNO: 25375(Aldh3a1) 266603(Aldh1a3)
            CFA: 476003(ALDH3B1)
            BTA: 281617(ALDH3)
            GGA: 428813(ALDH3B1)
            DME: Dmel_CG11140(Aldh-III)
            CEL: T08B1.3(alh-5)
            SCE: YMR169C(ALD3) YMR170C(ALD2)
            PIC: PICST_63844(ALD2)
            SPO: SPAC922.07c
            AFM: AFUA_4G13500
            ADE: Adeh_1143
            BCZ: BCZK1178
            BTK: BT9727_1176
            CPR: CPR_2296
            RHA: RHA1_ro01724
            AVA: Ava_3615
            CCH: Cag_1754
STRUCTURES  PDB: 1AD3  1EYY  1EZ0  2AMF  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.5
            ExPASy - ENZYME nomenclature database: 1.2.1.5
            ExplorEnz - The Enzyme Database: 1.2.1.5
            ERGO genome analysis and discovery system: 1.2.1.5
            BRENDA, the Enzyme Database: 1.2.1.5
            CAS: 9028-88-0
///
ENTRY       EC 1.2.1.6        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: benzaldehyde dehydrogenase (EC 1.2.1.6 created 1961,
            deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.6
            ExPASy - ENZYME nomenclature database: 1.2.1.6
            ExplorEnz - The Enzyme Database: 1.2.1.6
            ERGO genome analysis and discovery system: 1.2.1.6
            BRENDA, the Enzyme Database: 1.2.1.6
///
ENTRY       EC 1.2.1.7                  Enzyme
NAME        benzaldehyde dehydrogenase (NADP+);
            NADP+-linked benzaldehyde dehydrogenase;
            benzaldehyde dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     benzaldehyde:NADP+ oxidoreductase
REACTION    benzaldehyde + NADP+ + H2O = benzoate + NADPH + 2 H+ [RN:R01420]
ALL_REAC    R01420;
            (other) R01294 R05289 R05663 R05664 R07666
SUBSTRATE   benzaldehyde [CPD:C00261];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     benzoate [CPD:C00180];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13108854]
  AUTHORS   GUNSALUS CF, STANIER RY, GUNSALUS IC.
  TITLE     The enzymatic conversion of mandelic acid to benzoic acid. III.
            Fractionation and properties of the soluble enzymes.
  JOURNAL   J. Bacteriol. 66 (1953) 548-53.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   2  [PMID:4383635]
  AUTHORS   Stachow CS, Stevenson IL, Day D.
  TITLE     Purification and properties of nicotinamide adenine dinucleotide
            phosphate-specific benzaldehyde dehydrogenase from Pseudomonas.
  JOURNAL   J. Biol. Chem. 242 (1967) 5294-300.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00622  Toluene and xylene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.7
            ExPASy - ENZYME nomenclature database: 1.2.1.7
            ExplorEnz - The Enzyme Database: 1.2.1.7
            ERGO genome analysis and discovery system: 1.2.1.7
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.7
            BRENDA, the Enzyme Database: 1.2.1.7
            CAS: 9028-89-1
///
ENTRY       EC 1.2.1.8                  Enzyme
NAME        betaine-aldehyde dehydrogenase;
            betaine aldehyde oxidase;
            BADH;
            betaine aldehyde dehydrogenase;
            BetB
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     betaine-aldehyde:NAD+ oxidoreductase
REACTION    betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+ [RN:R02565]
ALL_REAC    R02565;
            (other) R02566
SUBSTRATE   betaine aldehyde [CPD:C00576];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     betaine [CPD:C00719];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     In many bacteria, plants and animals, the osmoprotectant betaine is
            synthesized in two steps: (1) choline to betaine aldehyde and (2)
            betaine aldehyde to betaine. This enzyme is involved in the second
            step and appears to be the same in plants, animals and bacteria. In
            contrast, different enzymes are involved in the first reaction. In
            plants, this reaction is catalysed by EC 1.14.15.7, choline
            monooxygenase, whereas in animals and many bacteria, it is catalysed
            by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or
            soluble choline oxidase (EC 1.1.3.17) [5]. In some bacteria, betaine
            is synthesized from glycine through the actions of EC 2.1.1.156,
            glycine/sarcosine N-methyltransferase and EC 2.1.1.157,
            sarcosine/dimethylglycine N-methyltransferase.
REFERENCE   1  [PMID:13192104]
  AUTHORS   ROTHSCHILD HA, BARRON ES.
  TITLE     The oxidation of betaine aldehyde by betaine aldehyde dehydrogenase.
  JOURNAL   J. Biol. Chem. 209 (1954) 511-23.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:12736784]
  AUTHORS   Livingstone JR, Maruo T, Yoshida I, Tarui Y, Hirooka K, Yamamoto Y,
            Tsutui N, Hirasawa E.
  TITLE     Purification and properties of betaine aldehyde dehydrogenase from
            Avena sativa.
  JOURNAL   J. Plant. Res. 116 (2003) 133-40.
  ORGANISM  Avena sativa
REFERENCE   3  [PMID:12604197]
  AUTHORS   Munoz-Clares RA, Gonzalez-Segura L, Mujica-Jimenez C, Contreras-Diaz
            L.
  TITLE     Ligand-induced conformational changes of betaine aldehyde
            dehydrogenase from Pseudomonas aeruginosa and Amaranthus
            hypochondriacus L. leaves affecting the reactivity of the catalytic
            thiol.
  JOURNAL   Chem. Biol. Interact. 143-144 (2003) 129-37.
  ORGANISM  Pseudomonas aeruginosa, Amaranthus hypochondriacus
REFERENCE   4  [PMID:9792097]
  AUTHORS   Johansson K, El-Ahmad M, Ramaswamy S, Hjelmqvist L, Jornvall H,
            Eklund H.
  TITLE     Structure of betaine aldehyde dehydrogenase at 2.1 A resolution.
  JOURNAL   Protein. Sci. 7 (1998) 2106-17.
  ORGANISM  rat [GN:rno], cow [GN:bta]
REFERENCE   5  [PMID:12466265]
  AUTHORS   Waditee R, Tanaka Y, Aoki K, Hibino T, Jikuya H, Takano J, Takabe T,
            Takabe T.
  TITLE     Isolation and functional characterization of N-methyltransferases
            that catalyze betaine synthesis from glycine in a halotolerant
            photosynthetic organism Aphanothece halophytica.
  JOURNAL   J. Biol. Chem. 278 (2003) 4932-42.
  ORGANISM  Aphanothece halophytica
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K00130  betaine-aldehyde dehydrogenase
GENES       ATH: AT1G74920(ALDH10A8) AT3G48170(ALDH10A9)
            OSA: 4336081 4345606
            SPO: SPCC550.10
            ANI: AN1430.2
            AFM: AFUA_1G00470 AFUA_8G04080
            AOR: AO090103000021
            ECO: b0312(betB)
            ECJ: JW0304(betB)
            ECE: Z0399(betB)
            ECS: ECs0358
            ECC: c0432(betB)
            ECI: UTI89_C0341(betB)
            ECP: ECP_0387
            ECV: APECO1_1678(betB)
            ECW: EcE24377A_0327(betB)
            ECX: EcHS_A0371(betB)
            YPE: YPO1166(betB)
            YPM: YP_0993(betB)
            YPA: YPA_1074
            YPN: YPN_2688 YPN_2835
            YPP: YPDSF_2406
            YPS: YPTB1196(betB)
            YPI: YpsIP31758_2830(betB)
            SFV: SFV_0323(betB)
            ECA: ECA1745(betB)
            PLU: plu2349
            XCC: XCC3403(betB)
            XCB: XC_0761
            XCV: XCV0775(betB)
            XAC: XAC0719(betB)
            VVU: VV2_1687
            VVY: VVA0507
            VPA: VPA1113
            PPR: PBPRB1746
            PAE: PA3504 PA5373(betB)
            PAU: PA14_70950(betB)
            PAP: PSPA7_3182 PSPA7_6158(betB)
            PPU: PP_1481 PP_5063(betB)
            PPF: Pput_4936
            PST: PSPTO_0441(badH)
            PSB: Psyr_4733
            PSP: PSPPH_4767(betB)
            PFL: PFL_5767(betB)
            PFO: Pfl_1044 Pfl_1049 Pfl_4470 Pfl_5243
            PEN: PSEEN0373(betB) PSEEN0848
            PAR: Psyc_0729(betB)
            PCR: Pcryo_0873
            ACI: ACIAD1009(betB)
            SDN: Sden_0714
            SFR: Sfri_1947
            SBL: Sbal_1324
            SBM: Shew185_1314
            CPS: CPS_1333(betB1) CPS_4011(betB2)
            PHA: PSHAb0419(betB)
            PAT: Patl_0153 Patl_2553 Patl_2588 Patl_3760 Patl_3895
            SDE: Sde_2645
            PIN: Ping_2071
            LPN: lpg0238(gbsA)
            LPF: lpl0292
            LPP: lpp0308
            HCH: HCH_00850(betB)
            CSA: Csal_1515 Csal_1706 Csal_2844
            RSO: RSc1456(betB)
            REU: Reut_A1842 Reut_A1905 Reut_B3577 Reut_B5689 Reut_B5835
                 Reut_C6374
            REH: H16_B2130(betB)
            BMA: BMAA0915(betB)
            BMV: BMASAVP1_0467(betB)
            BML: BMA10299_0180(betB)
            BMN: BMA10247_A1427(betB)
            BXE: Bxe_A1944 Bxe_A3526 Bxe_B0183 Bxe_B1591 Bxe_C1004
            BVI: Bcep1808_1698 Bcep1808_4306 Bcep1808_4803 Bcep1808_6409
                 Bcep1808_6589 Bcep1808_7602
            BUR: Bcep18194_A4372 Bcep18194_A5054 Bcep18194_B0535
                 Bcep18194_B0554 Bcep18194_B0933 Bcep18194_B1113
                 Bcep18194_B1170 Bcep18194_B1371 Bcep18194_B1781
                 Bcep18194_B2738 Bcep18194_B2788 Bcep18194_B2835
                 Bcep18194_B2962 Bcep18194_B3062 Bcep18194_B3159
                 Bcep18194_C6720 Bcep18194_C6748 Bcep18194_C6785
                 Bcep18194_C7156 Bcep18194_C7278 Bcep18194_C7305
                 Bcep18194_C7485 Bcep18194_C7546 Bcep18194_C7647
                 Bcep18194_C7675 Bcep18194_C7700
            BCN: Bcen_3269 Bcen_3586 Bcen_3666 Bcen_3713 Bcen_4133
            BCH: Bcen2424_1758 Bcen2424_3431 Bcen2424_4233 Bcen2424_4655
                 Bcen2424_4701 Bcen2424_4781 Bcen2424_5099
            BAM: Bamb_1682 Bamb_3655 Bamb_4095 Bamb_4164 Bamb_5214 Bamb_5756
                 Bamb_5845 Bamb_6073 Bamb_6096 Bamb_6363
            BPS: BPSL1647 BPSS1354(betB)
            BPM: BURPS1710b_A0376(betB)
            BPL: BURPS1106A_A1836(betB)
            BPD: BURPS668_A1924(betB)
            BTE: BTH_II1073(betB)
            RFR: Rfer_0986 Rfer_3585
            POL: Bpro_0055 Bpro_0091 Bpro_2450 Bpro_3685
            AJS: Ajs_0220
            VEI: Veis_2088 Veis_2787 Veis_3304 Veis_3572 Veis_3876
            EBA: ebA4621(betB)
            PCA: Pcar_1701
            PUB: SAR11_1343(dhaS)
            MLO: mll7608 mlr5385
            SME: SMa1731(betB2) SMc00094(betB) SMc01656
            ATU: Atu0829(betB)
            ATC: AGR_C_1515(badH)
            RET: RHE_CH01137(betB) RHE_CH01722(ypch00579)
                 RHE_CH03664(ypch01305)
            RLE: RL1271(betB) RL1823 RL4194
            BME: BMEI1382
            BMF: BAB1_0576
            BMS: BR0552(betB)
            BMB: BruAb1_0574(betB)
            BOV: BOV_0553(betB)
            BRA: BRADO2486
            BBT: BBta_2831
            RPB: RPB_0137
            SIL: SPO0084(betB)
            SIT: TM1040_0847 TM1040_1883 TM1040_3468
            RSP: RSP_2183(betB)
            RSH: Rsph17029_0855 Rsph17029_3176 Rsph17029_3472
            JAN: Jann_0776 Jann_1493 Jann_3937
            RDE: RD1_2023(betB)
            PDE: Pden_1710 Pden_1897 Pden_4941
            NAR: Saro_2610
            SAL: Sala_0902
            GBE: GbCGDNIH1_1608
            MAG: amb2593
            ABA: Acid345_0685 Acid345_1535
            BSU: BG11940(gbsA)
            BHA: BH0203(gbsA)
            BCY: Bcer98_1476
            BLI: BL02564(gbsA)
            BLD: BLi03270(gbsA)
            BCL: ABC0980(gbsA)
            BPU: BPUM_2735(gbsA)
            GKA: GK2000 GK2037
            SAU: SA2406(gbsA)
            SAV: SAV2613(gbsA)
            SAM: MW2532(gbsA)
            SAR: SAR2691(cudA)
            SAS: SAS2498
            SAC: SACOL2628(betB)
            SAB: SAB2487c(cudA)
            SAA: SAUSA300_2546(betB)
            SAO: SAOUHSC_02933
            SEP: SE2166
            SER: SERP2177(betB)
            SHA: SH0428(gbsA)
            SSP: SSP0195
            MSM: MSMEG_2881 MSMEG_5815
            MVA: Mvan_0014 Mvan_0240 Mvan_1572 Mvan_2280 Mvan_2878
            MGI: Mflv_0428 Mflv_3083 Mflv_4063 Mflv_4860
            MMC: Mmcs_0307 Mmcs_1220 Mmcs_2059 Mmcs_2273 Mmcs_2462 Mmcs_4650
            MKM: Mkms_0317 Mkms_1237 Mkms_2105 Mkms_2507 Mkms_2657 Mkms_4738
            MJL: Mjls_0298 Mjls_1247 Mjls_2042 Mjls_2499 Mjls_2642 Mjls_4040
                 Mjls_5033
            CGB: cg0637(betB)
            CDI: DIP2200(gbsA)
            CJK: jk1187(gbsA)
            NFA: nfa12730
            RHA: RHA1_ro00373 RHA1_ro00383 RHA1_ro01771 RHA1_ro01807
                 RHA1_ro01879 RHA1_ro02831 RHA1_ro03079 RHA1_ro05182
                 RHA1_ro05290 RHA1_ro08207
            SCO: SCO4828(gbsA) SCO5657(SC6A9.10c) SCO5666(SC6A9.01c)
            SMA: SAV1622(gbsA1) SAV2592 SAV2610 SAV3434(gbsA2) SAV6948(gbsA3)
                 SAV789
            LXX: Lxx12000 Lxx12010
            CMI: CMM_1951
            ART: Arth_1894 Arth_3522 Arth_3725
            AAU: AAur_0513(betB)
            NCA: Noca_1115 Noca_2160 Noca_2586 Noca_3529
            TFU: Tfu_0279 Tfu_1287 Tfu_1471 Tfu_1776
            FRA: Francci3_3777
            FAL: FRAAL6022
            ACE: Acel_1100 Acel_1850
            SEN: SACE_2895 SACE_3776 SACE_3969 SACE_4203(gbsA) SACE_4926
                 SACE_5371(gbsA) SACE_5668 SACE_6016
            RXY: Rxyl_1035 Rxyl_1561 Rxyl_2380 Rxyl_2917 Rxyl_3194
            TDE: TDE0080(gbsA)
            CYA: CYA_0364
            CYB: CYB_0715
            DGE: Dgeo_2416
            MTP: Mthe_0395
            MEM: Memar_1201
            MBN: Mboo_1307
            TVO: TVN0397
            SAI: Saci_1099
STRUCTURES  PDB: 1A4S  1BPW  1WNB  1WND  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.8
            ExPASy - ENZYME nomenclature database: 1.2.1.8
            ExplorEnz - The Enzyme Database: 1.2.1.8
            ERGO genome analysis and discovery system: 1.2.1.8
            BRENDA, the Enzyme Database: 1.2.1.8
            CAS: 9028-90-4
///
ENTRY       EC 1.2.1.9                  Enzyme
NAME        glyceraldehyde-3-phosphate dehydrogenase (NADP+);
            triosephosphate dehydrogenase;
            dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine
            dinucleotide phosphate);
            glyceraldehyde phosphate dehydrogenase (NADP+);
            glyceraldehyde 3-phosphate dehydrogenase (NADP+);
            NADP+-glyceraldehyde phosphate dehydrogenase;
            NADP+-glyceraldehyde-3-phosphate dehydrogenase;
            glyceraldehyde-3-phosphate:NADP+ reductase;
            nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase;
            glyceraldehyde-3-phosphate dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-glyceraldehyde-3-phosphate:NADP+ oxidoreductase
REACTION    D-glyceraldehyde 3-phosphate + NADP+ + H2O = 3-phospho-D-glycerate +
            NADPH + 2 H+ [RN:R01058]
ALL_REAC    R01058
SUBSTRATE   D-glyceraldehyde 3-phosphate [CPD:C00118];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     3-phospho-D-glycerate [CPD:C00197];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13271400]
  AUTHORS   ROSENBERG LL, ARNON DI.
  TITLE     The preparation and properties of a new glyceraldehyde-3-phosphate
            dehydrogenase from photosynthetic tissues.
  JOURNAL   J. Biol. Chem. 217 (1955) 361-71.
  ORGANISM  spinach
ORTHOLOGY   KO: K00131  glyceraldehyde-3-phosphate dehydrogenase (NADP)
GENES       OSA: 4345685
            CME: CMT034C
            PIC: PICST_29563(ALD5) PICST_40468(UGA2) PICST_44169(ALD4)
                 PICST_57266(UGA22) PICST_60847(ALD3) PICST_63844(ALD2)
                 PICST_90594(MSC7)
            PAE: PA2323
            PPU: PP_0665 PP_3443
            PFL: PFL_3718 PFL_3808
            PFO: Pfl_2492
            ACI: ACIAD0546
            DAR: Daro_2068
            GSU: GSU0818
            GME: Gmet_0789
            SFU: Sfum_1087
            RET: RHE_PD00091(gabDd) RHE_PF00201(ypf00097) RHE_PF00340(gabDf1)
            RLE: pRL80070
            BHA: BH1738 BH2237(gapN)
            BAN: BA0849(gapN)
            BAR: GBAA0849(gapN)
            BAA: BA_1431
            BAT: BAS0808
            BCE: BC0868
            BCA: BCE_0940(gapN) BCE_4521
            BCZ: BCZK0750(gapN)
            BTK: BT9727_0757(gapN)
            BCL: ABC0024
            SPY: SPy_1371(gapN)
            SPZ: M5005_Spy_1119(gapN)
            SPM: spyM18_1383(gapN)
            SPG: SpyM3_1045(gapN)
            SPH: MGAS10270_Spy1189(gapN)
            SPI: MGAS10750_Spy1221(gapN)
            SPJ: MGAS2096_Spy1184(gapN)
            SPK: MGAS9429_Spy1166(gapN)
            SPF: SpyM50741(gapN)
            SPA: M6_Spy1093
            SPB: M28_Spy1112(gapN)
            SPN: SP_1119
            SPR: spr1028(gapN)
            SPD: SPD_1004(gapN)
            SAG: SAG0823(gapN)
            SAN: gbs0841
            SAK: SAK_0947(gapN)
            SMU: SMU.676(gapN)
            STC: str1263(gapN)
            STL: stu1263(gapN)
            SSA: SSA_0774(gapN)
            LDB: Ldb1179(gapN)
            LBU: LBUL_1096
            CAC: CAC3657
            CPE: CPE2438(gapN)
            CPF: CPF_2748(gapN)
            CPR: CPR_2434
            CDF: CD0580(gapN)
            CBO: CBO1253(gapN)
            CBF: CLI_2350(gapN)
            MPE: MYPE4710(gap)
            MGA: MGA_0860(putA)
            MMY: MSC_0509(gapN)
            MCP: MCAP_0461
            UUR: UU362(gapN)
            MFL: Mfl259
            FRA: Francci3_3825
            CHU: CHU_0301(gapN)
            GFO: GFO_0735(gapN)
            MMP: MMP1487(gapN)
            MKA: MK1108
            HAL: VNG0937G(gap)
            PFU: PF0755
            TKO: TK0705
            APE: APE_1786.1
            SSO: SSO1629(gapN-1) SSO1842(gapN-2) SSO3194(gapN-3)
            STO: ST0064 ST2477
            SAI: Saci_0227 Saci_1738
STRUCTURES  PDB: 1EUH  1KY8  1QI1  1QI6  1UXN  1UXP  1UXQ  1UXR  1UXT  1UXU  
                 1UXV  2ESD  2EUH  2ID2  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.9
            ExPASy - ENZYME nomenclature database: 1.2.1.9
            ExplorEnz - The Enzyme Database: 1.2.1.9
            ERGO genome analysis and discovery system: 1.2.1.9
            BRENDA, the Enzyme Database: 1.2.1.9
            CAS: 9028-92-6
///
ENTRY       EC 1.2.1.10                 Enzyme
NAME        acetaldehyde dehydrogenase (acetylating);
            aldehyde dehydrogenase (acylating);
            ADA;
            acylating acetaldehyde dehyrogenase;
            DmpF
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     acetaldehyde:NAD+ oxidoreductase (CoA-acetylating)
REACTION    acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+ [RN:R00228]
ALL_REAC    R00228;
            (other) R01172
SUBSTRATE   acetaldehyde [CPD:C00084];
            CoA [CPD:C00010];
            NAD+ [CPD:C00003]
PRODUCT     acetyl-CoA [CPD:C00024];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts, more slowly, on glycolaldehyde, propanal and butanal. In
            Pseudomonas species, this enzyme forms part of a bifunctional enzyme
            with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. It is the final
            enzyme in the meta-cleavage pathway for the degradation of phenols,
            cresols and catechol, converting the acetaldehyde produced by EC
            4.1.3.39 into acetyl-CoA [3]. NADP+ can replace NAD+ but the rate of
            reaction is much slower [3].
REFERENCE   1  [PMID:13061511]
  AUTHORS   BURTON RM, STADTMAN ER.
  TITLE     The oxidation of acetaldehyde to acetyl coenzyme A.
  JOURNAL   J. Biol. Chem. 202 (1953) 873-90.
  ORGANISM  Clostridium kluyveri
REFERENCE   2  [PMID:7458347]
  AUTHORS   Smith LT, Kaplan NO.
  TITLE     Purification, properties, and kinetic mechanism of coenzyme A-linked
            aldehyde dehydrogenase from Clostridium kluyveri.
  JOURNAL   Arch. Biochem. Biophys. 203 (1980) 663-75.
  ORGANISM  Clostridium kluyveri
REFERENCE   3  [PMID:8419288]
  AUTHORS   Powlowski J, Sahlman L, Shingler V.
  TITLE     Purification and properties of the physically associated
            meta-cleavage pathway enzymes 4-hydroxy-2-ketovalerate aldolase and
            aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain
            CF600.
  JOURNAL   J. Bacteriol. 175 (1993) 377-85.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00620  Pyruvate metabolism
            PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K00132  acetaldehyde dehydrogenase
            KO: K04072  acetaldehyde dehydrogenase
            KO: K04073  acetaldehyde dehydrogenase
GENES       CPV: cgd8_1720
            CHO: Chro.80199
            ECO: b0351(mhpF) b1241(adhE)
            ECJ: JW0342(mhpF) JW1228(adhE)
            ECE: Z0450(mhpF) Z2016(adhE)
            ECS: ECs0406 ECs1741
            ECC: c1705(adhE)
            ECI: UTI89_C1438(adhE)
            ECP: ECP_1287
            ECV: APECO1_355(adhE)
            ECW: EcE24377A_0375(mhpF) EcE24377A_1389(adhE)
            ECX: EcHS_A0415 EcHS_A1350
            STY: STY1302(adh)
            STT: t1660(adh)
            SPT: SPA1129(adh)
            SEC: SC1744(adhE)
            STM: STM1749(adhE)
            YPE: YPO2180(adhE)
            YPK: y2023(adhE)
            YPM: YP_1976(adhE)
            YPA: YPA_1537
            YPN: YPN_1646
            YPS: YPTB2103(adhE)
            YPI: YpsIP31758_1963(adhE)
            SFL: SF1240(adhE)
            SFX: S1326(adhE)
            SFV: SFV_1253(adhE)
            SSN: SSON_0330(mhpF) SSON_1939(adhE)
            SBO: SBO_1828(adhE)
            SDY: SDY_1295(adhE)
            ECA: ECA1428(nahO) ECA2326(adhE)
            PLU: plu2496(adhE)
            SGL: SG1372
            PMU: PM1453(adh2)
            MSU: MS2190(eutG)
            APL: APL_1011(adh2)
            VCH: VC2033
            VVU: VV1_3111
            VVY: VV1175
            VPA: VP2121
            VFI: VF0918
            PPR: PBPRA1103(adhE)
            SON: SO_2136(adhE)
            SDN: Sden_2000
            SFR: Sfri_1898
            SHN: Shewana3_1788
            PHA: PSHAa2142(mhpF)
            AHA: AHA_1333(eutE) AHA_2616
            CVI: CV_1137(adhE)
            RSO: RS01665(RSp0894)
            REU: Reut_A0867 Reut_B5824
            REH: H16_A1806 H16_A2747 H16_B0551(mhpF) H16_B0596
            RME: Rmet_1320 Rmet_5208
            BXE: Bxe_A1151(amnH) Bxe_A3547 Bxe_B0701 Bxe_B2326 Bxe_C1188(bphJ)
            BUR: Bcep18194_B1187 Bcep18194_B1458 Bcep18194_B2960
                 Bcep18194_C7645
            BPS: BPSS1808(mhpF)
            BPM: BURPS1710b_A0891(mhpF)
            BPL: BURPS1106A_4008(eutE)
            BPD: BURPS668_3936(eutE)
            BTE: BTH_II0569(mhpF)
            RFR: Rfer_0455
            POL: Bpro_5135
            MPT: Mpe_A2267 Mpe_A3322 Mpe_B0500
            AZO: azo1856(lapF) azo1973(mhpF) azo2432(nahO)
            DAR: Daro_0906 Daro_1355 Daro_3239 Daro_3783 Daro_3807
            PCA: Pcar_2758 Pcar_2851
            PPD: Ppro_0756
            DDE: Dde_3279 Dde_3283
            RPE: RPE_3692
            RDE: RD1_2918(adhE)
            RRU: Rru_A0914
            BAN: BA4599
            BAR: GBAA4599
            BAA: BA_5039
            BAT: BAS4267
            BCE: BC4365
            BCA: BCE_2156 BCE_4453
            BCZ: BCZK4115
            BTK: BT9727_4104
            BTL: BALH_3956
            BLI: BL00199
            BLD: BLi04290
            SAU: SA0143(adhE)
            SAV: SAV0148(adhE)
            SAM: MW0123(adhE)
            SAR: SAR0150(adhE)
            SAS: SAS0123
            SAC: SACOL0135
            SAA: SAUSA300_0151(adhE)
            SAO: SAOUHSC_00113
            SEP: SE0506
            SER: SERP0389
            LMO: lmo1634
            LMF: LMOf2365_1656(adhE)
            LIN: lin1675
            LWE: lwe1650
            LLA: L13145(adhE)
            LLC: LACR_2457
            LLM: llmg_2432(adhE)
            SPZ: M5005_Spy_0039(adh2)
            SPM: spyM18_0043(adhE)
            SPG: SpyM3_0036(adh2)
            SPS: SPs0037
            SPH: MGAS10270_Spy0042
            SPI: MGAS10750_Spy0041
            SPJ: MGAS2096_Spy0041
            SPK: MGAS9429_Spy0040(adh2)
            SPF: SpyM50039(adhE)
            SPA: M6_Spy0088
            SPB: M28_Spy0039
            SPN: SP_2026
            SPR: spr1837(adhE)
            SAG: SAG0053(adhE)
            SAN: gbs0053
            SAK: SAK_0086
            SMU: SMU.148(adhE)
            STC: str1879 str1881 str1882 str1884
            STL: stu1879 stu1880 stu1881 stu1882 stu1883 stu1884
            SSA: SSA_0523
            LPL: lp_0329(acdH) lp_3662(adhE)
            LJO: LJ1766
            LAC: LBA0461(adhE)
            LSA: LSA0379(adhE)
            LSL: LSL_1901
            LDB: Ldb1707
            LBU: LBUL_1581
            LBR: LVIS_0119
            LCA: LSEI_0775
            EFA: EF0900(adhE)
            OOE: OEOE_1248
            CAC: CA_P0035(adhE) CA_P0162(adhE1)
            CPE: CPE2531(adhE)
            CPF: CPF_2855(adhE)
            CPR: CPR_2540
            CTC: CTC01366 CTC02172(eutE)
            CDF: CD0334(adhE)
            CBO: CBO0345(aad)
            CBA: CLB_0388(adhE) CLB_2045(eutE)
            CBH: CLC_0403(adhE) CLC_2050(eutE)
            CBF: CLI_0416(adhE) CLI_2151(eutE)
            CHY: CHY_1279(mhpF)
            DSY: DSY0244 DSY5007
            MTA: Moth_1776
            MTU: Rv3535c
            MTC: MT3639(mhpF)
            MBO: Mb3565c
            MBB: BCG_3599c
            MPA: MAP0532
            MSM: MSMEG_0276 MSMEG_4149 MSMEG_5939
            MMC: Mmcs_5437
            NFA: nfa30500 nfa33190 nfa4660
            RHA: RHA1_ro00516 RHA1_ro03866 RHA1_ro04534(hsaG) RHA1_ro05800
                 RHA1_ro08084(bphG3) RHA1_ro09018(bphG1) RHA1_ro10116(bphG4)
            NCA: Noca_4031
            BLO: BL1575(adh2)
            BAD: BAD_0319
            CYA: CYA_0473(adhE)
            CYB: CYB_0241
            TEL: tlr0227
            PGI: PG0687(sucD)
            TTJ: TTHB247
STRUCTURES  PDB: 1NVM  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.10
            ExPASy - ENZYME nomenclature database: 1.2.1.10
            ExplorEnz - The Enzyme Database: 1.2.1.10
            ERGO genome analysis and discovery system: 1.2.1.10
            BRENDA, the Enzyme Database: 1.2.1.10
            CAS: 9028-91-5
///
ENTRY       EC 1.2.1.11                 Enzyme
NAME        aspartate-semialdehyde dehydrogenase;
            aspartate semialdehyde dehydrogenase;
            aspartic semialdehyde dehydrogenase;
            L-aspartate-beta-semialdehyde:NADP+ oxidoreductase
            (phosphorylating);
            aspartic beta-semialdehyde dehydrogenase;
            ASA dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-aspartate-4-semialdehyde:NADP+ oxidoreductase (phosphorylating)
REACTION    L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl
            phosphate + NADPH + H+ [RN:R02291]
ALL_REAC    R02291
SUBSTRATE   L-aspartate 4-semialdehyde [CPD:C00441];
            phosphate [CPD:C00009];
            NADP+ [CPD:C00006]
PRODUCT     L-4-aspartyl phosphate [CPD:C03082];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:14353904]
  AUTHORS   BLACK S, WRIGHT NG.
  TITLE     Aspartic beta-semialdehyde dehydrogenase and aspartic
            beta-semialdehyde.
  JOURNAL   J. Biol. Chem. 213 (1955) 39-50.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2
  AUTHORS   Jakoby, W.B.
  TITLE     Aldehyde dehydrogenases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K00133  aspartate-semialdehyde dehydrogenase
GENES       OSA: 4334188
            CME: CMG123C
            SCE: YDR158W(HOM2)
            AGO: AGOS_AGL175W
            PIC: PICST_89195(HOM2)
            CGR: CAGL0E01133g
            SPO: SPCC1827.06c
            ANI: AN4793.2
            AFM: AFUA_3G06830
            AOR: AO090020000314
            CNE: CNA02450
            ECO: b3433(asd)
            ECJ: JW3396(asd)
            ECE: Z4797(asd)
            ECS: ECs4278
            ECC: c4220(asd)
            ECI: UTI89_C2604(usg) UTI89_C3942(asd)
            ECP: ECP_3527
            ECV: APECO1_3024(asd)
            ECW: EcE24377A_3912(asd)
            ECX: EcHS_A3633
            STY: STY4271(asd)
            STT: t3981(asd)
            SPT: SPA3390(asd)
            SEC: SC3469(asd)
            STM: STM3539(asd)
            YPE: YPO3949(asd)
            YPK: y1598(usg) y3880(asd)
            YPM: YP_2399(asd1) YP_3311(asd2)
            YPA: YPA_2079 YPA_3777
            YPN: YPN_2182 YPN_3597
            YPP: YPDSF_1996 YPDSF_3313
            YPS: YPTB3790(asd)
            YPI: YpsIP31758_4013(asd)
            SFL: SF3456(asd)
            SFX: S4307(asd)
            SFV: SFV_3442(asd)
            SSN: SSON_3673(asd)
            SBO: SBO_3431(asd)
            SDY: SDY_3579(asd)
            ECA: ECA3059 ECA4155(asd)
            PLU: plu0007(asd)
            BUC: BU448(asd)
            BAS: BUsg433(asd)
            BAB: bbp398(asd)
            BCC: BCc_277(asd)
            WBR: WGLp443(asd)
            SGL: SG1620 SG2330
            ENT: Ent638_2868 Ent638_3841
            SPE: Spro_3335 Spro_4648
            BFL: Bfl574(asd)
            BPN: BPEN_594(asd)
            HIT: NTHI0765(asd)
            HIP: CGSHiEE_04565 CGSHiEE_04760 CGSHiEE_09005
            HIQ: CGSHiGG_01045 CGSHiGG_06530
            HDU: HD0847(asd)
            HSO: HS_1552(asd)
            PMU: PM1632(asd)
            MSU: MS0006(asd)
            APL: APL_0005(asd)
            ASU: Asuc_0278
            XFA: XF1371
            XFT: PD0608(asd)
            XCC: XCC2549(asd)
            XCB: XC_1569
            XCV: XCV2875(asd)
            XAC: XAC2723(asd)
            XOO: XOO3259(asd)
            XOM: XOO_3087(XOO3087)
            VCH: VC2036 VC2107
            VCO: VC0395_A1621(asd)
            VVU: VV1_1989 VV1_3115
            VVY: VV1171 VV2427
            VPA: VP2124 VP2192
            VFI: VF1645 VF1698
            PPR: PBPRA2579 PBPRA2655
            PAE: PA3116 PA3117(asd)
            PAU: PA14_23800(asd) PA14_23810
            PAP: PSPA7_2016(asd)
            PPU: PP_1989(asd) PP_1992
            PPF: Pput_3769 Pput_3770
            PST: PSPTO_2176(asd-1) PSPTO_3819(asd-2)
            PSB: Psyr_1660 Psyr_1986
            PSP: PSPPH_1654 PSPPH_1955(asd)
            PFL: PFL_2067(asd) PFL_2068
            PFO: Pfl_1893 Pfl_1894
            PEN: PSEEN1653(asd) PSEEN1687
            PMY: Pmen_2719 Pmen_2720
            PAR: Psyc_1523(asd)
            PCR: Pcryo_1701
            PRW: PsycPRwf_1791
            ACI: ACIAD0479(asd)
            SON: SO_3070(asd)
            SDN: Sden_1484
            SFR: Sfri_1393
            SAZ: Sama_2152
            SBL: Sbal_2744
            SBM: Shew185_2761
            SLO: Shew_2308
            SPC: Sputcn32_2443
            SSE: Ssed_1650
            SPL: Spea_1613
            SHE: Shewmr4_1424
            SHM: Shewmr7_1489
            SHN: Shewana3_1477
            SHW: Sputw3181_1565
            ILO: IL1019(asd)
            CPS: CPS_3805(asd)
            PHA: PSHAa2078(asd) PSHAb0528(asd)
            PAT: Patl_3363
            SDE: Sde_2083
            PIN: Ping_1993 Ping_3206
            MAQ: Maqu_1562
            CBU: CBU_0875(asd)
            CBD: COXBU7E912_0940(asd)
            LPN: lpg2302(asd)
            LPF: lpl2221(asd)
            LPP: lpp2250(asd)
            MCA: MCA2062(asd)
            FTU: FTT0425c(asd)
            FTF: FTF0425c(asd)
            FTW: FTW_1649(asd)
            FTL: FTL_0494
            FTA: FTA_0520(asd)
            FTN: FTN_0524(asd)
            TCX: Tcr_0800
            NOC: Noc_1016
            AEH: Mlg_1231
            HHA: Hhal_1808
            HCH: HCH_02431(asd)
            CSA: Csal_2450
            ABO: ABO_1465(asd-1) ABO_1466(asd-2)
            MMW: Mmwyl1_2094
            AHA: AHA_1945(asd-1) AHA_2682(asd-2)
            DNO: DNO_1053(asd)
            CRP: CRP_083
            RMA: Rmag_0951
            VOK: COSY_0851(asd)
            NME: NMB2079
            NMA: NMA0351
            NMC: NMC2058
            NGO: NGO1997
            CVI: CV_2767(usg) CV_2768(asd)
            RSO: RSc1987(asd)
            REU: Reut_A2310
            REH: H16_A2618(asd)
            RME: Rmet_2471
            BMA: BMAA1725(asd)
            BMV: BMASAVP1_1645(asd)
            BML: BMA10299_1854(asd)
            BMN: BMA10247_A0525(asd)
            BXE: Bxe_B2885
            BVI: Bcep1808_4458
            BUR: Bcep18194_B2130
            BCN: Bcen_4414
            BCH: Bcen2424_3953
            BAM: Bamb_3344
            BPS: BPSS1704(asd)
            BPM: BURPS1710b_A0773(asd)
            BPL: BURPS1106A_A2311(asd)
            BPD: BURPS668_A2449(asd)
            BTE: BTH_II0675(asd)
            PNU: Pnuc_0768
            BPE: BP1484(asd)
            BPA: BPP1945(asd)
            BBR: BB2133(asd)
            RFR: Rfer_1792
            POL: Bpro_3612
            PNA: Pnap_3042
            AAV: Aave_1219
            AJS: Ajs_3235
            VEI: Veis_4872
            MPT: Mpe_A2161
            HAR: HEAR1218(asd)
            MMS: mma_2168
            NEU: NE0689(asd)
            NET: Neut_1148
            NMU: Nmul_A1917
            EBA: ebA4761(asd)
            AZO: azo1042(asd)
            DAR: Daro_0865
            TBD: Tbd_1919
            MFA: Mfla_1702
            HPY: HP1189(asd)
            HPJ: jhp1114(asd)
            HPA: HPAG1_1130
            HHE: HH1874(asd)
            HAC: Hac_1565(asd)
            WSU: WS0368
            TDN: Tmden_0636
            CJE: Cj1023c(asd)
            CJR: CJE1167(asd)
            CJJ: CJJ81176_1042(asd)
            CJU: C8J_0960(asd)
            CJD: JJD26997_0765(asd)
            CFF: CFF8240_1458(asd)
            CCV: CCV52592_1463(asd)
            CHA: CHAB381_1243(asd)
            ABU: Abu_1788(asd)
            NIS: NIS_0488
            SUN: SUN_1615
            GSU: GSU2878
            GME: Gmet_0603 Gmet_0604
            GUR: Gura_1046 Gura_1047
            PCA: Pcar_1903
            PPD: Ppro_0046 Ppro_0047
            DVU: DVU3048(asd)
            DVL: Dvul_0328
            DDE: Dde_0254
            LIP: LI0951(asd)
            BBA: Bd0484(asd)
            DPS: DP2767
            ADE: Adeh_0382 Adeh_3578
            AFW: Anae109_4190
            MXA: MXAN_2560 MXAN_3050(asd)
            SAT: SYN_00911
            SFU: Sfum_2990
            RPR: RP316
            RTY: RT0306(asd)
            RCO: RC0430(asd)
            RFE: RF_0512(asd)
            RBE: RBE_0820(asd)
            RAK: A1C_02350
            RBO: A1I_05230
            RRI: A1G_02440
            OTS: OTBS_1798(asd)
            WOL: WD0954(asd)
            WBM: Wbm0042
            AMA: AM1277(asd)
            APH: APH_1346
            ERU: Erum0060(asd) Erum8540
            ERW: ERWE_CDS_09510(asd)
            ERG: ERGA_CDS_09430(asd)
            ECN: Ecaj_0944
            ECH: ECH_0016(asd)
            NSE: NSE_0260(asd)
            PUB: SAR11_0245(asd)
            MLO: mll4392
            MES: Meso_3384
            SME: SMc04410(asd)
            SMD: Smed_3182
            ATU: Atu2490(asd)
            ATC: AGR_C_4523
            RET: RHE_CH04100(asd)
            RLE: RL4715(asd)
            BME: BMEII0407
            BMF: BAB2_0349
            BMS: BRA0887(asd)
            BMB: BruAb2_0345(asd)
            BOV: BOV_A0831(asd)
            OAN: Oant_3290
            BJA: bll0501(asd) blr4687(asd)
            BRA: BRADO0358(asd) BRADO3992(asd)
            BBT: BBta_0344(asd) BBta_4365(asd)
            RPA: RPA0230(asdB)
            RPB: RPB_0338
            RPC: RPC_0237
            RPD: RPD_0493
            RPE: RPE_0484
            NWI: Nwi_2793
            NHA: Nham_3593
            BHE: BH12890(asd)
            BQU: BQ10170(asd)
            BBK: BARBAKC583_1101(asd)
            XAU: Xaut_2214
            CCR: CC_0253 CC_3485
            SIL: SPO3712(asd)
            SIT: TM1040_3459
            RSP: RSP_1376(asd)
            JAN: Jann_0114
            RDE: RD1_0306(asd)
            PDE: Pden_2775
            MMR: Mmar10_2876
            HNE: HNE_0061(asd)
            ZMO: ZMO1407(asd)
            NAR: Saro_1410
            SAL: Sala_2718
            ELI: ELI_07430
            GOX: GOX0878
            GBE: GbCGDNIH1_2081
            ACR: Acry_1717
            RRU: Rru_A1196
            MAG: amb0587
            MGM: Mmc1_1782
            ABA: Acid345_2358 Acid345_2490
            SUS: Acid_1719 Acid_6983
            BSU: BG10783(asd)
            BHA: BH2401(asd)
            BAN: BA2436(asd-1) BA3937(asd-2)
            BAR: GBAA2436(asd-1) GBAA3937(asd-2)
            BAA: BA_2932 BA_4409
            BAT: BAS2268 BAS3652
            BCE: BC2363 BC3799
            BCA: BCE_2465(asd) BCE_3838(asd)
            BCZ: BCZK2185(asd) BCZK3560(asd)
            BTK: BT9727_2228(asd) BT9727_3542(asd)
            BLI: BL01210(asd)
            BLD: BLi01900(asd)
            BCL: ABC2216(asd)
            BAY: RBAM_016590
            BPU: BPUM_1579
            OIH: OB1610(asd)
            GKA: GK1275
            SAU: SA1226(asd)
            SAV: SAV1394(asd)
            SAM: MW1282(asd)
            SAR: SAR1406(asd)
            SAS: SAS1335
            SAC: SACOL1429(asd)
            SAB: SAB1249(asd)
            SAA: SAUSA300_1287(asd)
            SAO: SAOUHSC_01395
            SAJ: SaurJH9_1455
            SAH: SaurJH1_1484
            SEP: SE1074
            SER: SERP0964(asd)
            SHA: SH1517(asd)
            SSP: SSP1356
            LMO: lmo1437
            LMF: LMOf2365_1456(asd)
            LIN: lin1476
            LWE: lwe1454(asd)
            LLA: L66199(asd)
            LLC: LACR_1731
            LLM: llmg_0871(asd)
            SPN: SP_1013
            SPR: spr0918(asd)
            SPD: SPD_0900(asd)
            SAG: SAG1051(asd)
            SAN: gbs1086
            SAK: SAK_1141(asd)
            SMU: SMU.989(asd)
            STC: str1298(asd)
            STL: stu1298(asd)
            SSA: SSA_1194(asd)
            SGO: SGO_1206(asd)
            LPL: lp_1346(asd1) lp_2570(asd2)
            LAC: LBA0857
            LSL: LSL_0313(asd)
            LDB: Ldb1348(asd)
            LBU: LBUL_1257
            LCA: LSEI_0101
            LRE: Lreu_0618
            EFA: EF1183(asd)
            OOE: OEOE_0776
            STH: STH1547
            CAC: CAC0022(asd) CAC0568(asd)
            CPE: CPE1904(asd)
            CPF: CPF_2160(asd)
            CPR: CPR_1871(asd)
            CTC: CTC02293
            CNO: NT01CX_1747
            CTH: Cthe_0961
            CDF: CD3224(asd)
            CBO: CBO3151(asd)
            CBA: CLB_3186(asd)
            CBH: CLC_3061(asd)
            CBF: CLI_3216(asd)
            CBE: Cbei_0518 Cbei_1797
            CKL: CKL_3207(asd)
            CHY: CHY_1154(asd)
            DSY: DSY2500
            DRM: Dred_1941
            SWO: Swol_1270
            TTE: TTE0833(asd)
            MTA: Moth_1066
            MTU: Rv3708c(asd)
            MTC: MT3811(asd)
            MBO: Mb3735c(asd)
            MBB: BCG_3768c(asd)
            MLE: ML2322(asd)
            MPA: MAP0310c(asd)
            MAV: MAV_0394(asd)
            MSM: MSMEG_6256(asd)
            MVA: Mvan_5503
            MGI: Mflv_1305
            MMC: Mmcs_4888
            MKM: Mkms_4977
            MJL: Mjls_5256
            CGL: NCgl0248(cgl0252)
            CGB: cg0307(asd)
            CEF: CE0221(asd)
            CDI: DIP0279(asd)
            CJK: jk1997(asd)
            NFA: nfa3190
            RHA: RHA1_ro04292(asd)
            SCO: SCO2640(asd1) SCO3614(asd2)
            SMA: SAV4560(asd1) SAV5397(asd2)
            TWH: TWT707(asd)
            TWS: TW724(asd)
            LXX: Lxx03460(asd)
            ART: Arth_3021
            AAU: AAur_2995(asd)
            PAC: PPA0318
            NCA: Noca_0322
            TFU: Tfu_0042
            FRA: Francci3_0261
            FAL: FRAAL0604(asd) FRAAL2412(asd-like)
            ACE: Acel_2011
            KRA: Krad_0462
            SEN: SACE_0283
            STP: Strop_0227 Strop_3567
            BLO: BL0492(asd)
            BAD: BAD_0141(asd)
            RXY: Rxyl_1092
            RBA: RB9795(asd)
            CTR: CT363(asd)
            CTA: CTA_0395(asd)
            CMU: TC0642
            CPN: CPn1048(asd)
            CPA: CP0804
            CPJ: CPj1048(asd)
            CPT: CpB1089
            CCA: CCA00714(asd)
            CAB: CAB679(asd)
            CFE: CF0304(asd)
            PCU: pc1102(asd)
            LIL: LB355(asd)
            LIC: LIC20266(asd)
            LBJ: LBJ_4255(asd)
            LBL: LBL_4269(asd)
            SYN: slr0549(asd)
            SYW: SYNW0066(asd)
            SYC: syc2246_d(asd)
            SYF: Synpcc7942_1848
            SYD: Syncc9605_0067
            SYE: Syncc9902_0064
            SYG: sync_0067(asd)
            SYR: SynRCC307_0068(asd)
            SYX: SynWH7803_0072(asd)
            CYA: CYA_1867(asd)
            CYB: CYB_1568(asd)
            TEL: tlr0069(asd)
            GVI: glr1017
            ANA: all3680
            AVA: Ava_3606
            PMA: Pro1814(asd)
            PMM: PMM1654(asd)
            PMT: PMT0064(asd)
            PMN: PMN2A_1252
            PMI: PMT9312_1746
            PMB: A9601_18631(asd)
            PMC: P9515_18441(asd)
            PMF: P9303_00711(asd)
            PMG: P9301_18441(asd)
            PME: NATL1_21221(asd)
            TER: Tery_0587
            BTH: BT_3636
            BFR: BF0444
            BFS: BF0384(asd)
            PGI: PG0571(asd)
            SRU: SRU_1838(asd)
            CHU: CHU_0139(asd)
            GFO: GFO_3351(asd)
            FPS: FP0524(asd)
            CTE: CT1928(asd)
            CCH: Cag_0282
            CPH: Cpha266_2287
            PLT: Plut_0277
            DET: DET0972(asd)
            DEH: cbdb_A934(asd)
            DEB: DehaBAV1_0863
            RRS: RoseRS_3078
            RCA: Rcas_3188
            DRA: DR_2008
            DGE: Dgeo_1782
            TTH: TTC0177
            TTJ: TTHA0545
            AAE: aq_1866(asd)
            TMA: TM1523
            TME: Tmel_1873
            FNO: Fnod_0070
            MMP: MMP1391(asd)
            MMZ: MmarC7_0636
            MAE: Maeo_1369
            MVN: Mevan_0702
            MAC: MA0430(asd)
            MBA: Mbar_A0760
            MMA: MM_1618
            MBU: Mbur_0379
            MHU: Mhun_1495
            MST: Msp_0110(asd)
            MSI: Msm_0829
            MKA: MK1389(asd)
            HAL: VNG1435G(asd)
            HMA: rrnAC0365(asd)
            HWA: HQ2908A(asd)
            NPH: NP1988A(asd)
            TAC: Ta0363
            PTO: PTO1367
            PHO: PH1088
            PAB: PAB1678(asd)
            PFU: PF1056
            TKO: TK1443
            RCI: RCIX722(asd)
            APE: APE_1143
            SSO: SSO0874(asd-1) SSO2178(asd-2)
            STO: ST1242 ST2171
            SAI: Saci_1411(asd) Saci_2147 Saci_2370
            MSE: Msed_0709
            PAI: PAE2876(asd)
            PIS: Pisl_0272
            PCL: Pcal_0378
            PAS: Pars_0957
STRUCTURES  PDB: 1BRM  1GL3  1MB4  1MC4  1NWC  1NWH  1NX6  1OZA  1PQP  1PQU  
                 1PR3  1PS8  1PU2  1Q2X  1T4B  1T4D  1TA4  1TB4  1YS4  2EP5  
                 2GYY  2GZ1  2GZ2  2GZ3  2YV3  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.11
            ExPASy - ENZYME nomenclature database: 1.2.1.11
            ExplorEnz - The Enzyme Database: 1.2.1.11
            ERGO genome analysis and discovery system: 1.2.1.11
            BRENDA, the Enzyme Database: 1.2.1.11
            CAS: 9000-98-0
///
ENTRY       EC 1.2.1.12                 Enzyme
NAME        glyceraldehyde-3-phosphate dehydrogenase (phosphorylating);
            triosephosphate dehydrogenase;
            dehydrogenase, glyceraldehyde phosphate;
            phosphoglyceraldehyde dehydrogenase;
            3-phosphoglyceraldehyde dehydrogenase;
            NAD+-dependent glyceraldehyde phosphate dehydrogenase;
            glyceraldehyde phosphate dehydrogenase (NAD+);
            glyceraldehyde-3-phosphate dehydrogenase (NAD+);
            NADH-glyceraldehyde phosphate dehydrogenase;
            glyceraldehyde-3-P-dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating)
REACTION    D-glyceraldehyde 3-phosphate + phosphate + NAD+ =
            3-phospho-D-glyceroyl phosphate + NADH + H+ [RN:R01061]
ALL_REAC    R01061;
            (other) R01063 R04201
SUBSTRATE   D-glyceraldehyde 3-phosphate [CPD:C00118];
            phosphate [CPD:C00009];
            NAD+ [CPD:C00003]
PRODUCT     3-phospho-D-glyceroyl phosphate [CPD:C00236];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts very slowly on D-glyceraldehyde and some other aldehydes;
            thiols can replace phosphate.
REFERENCE   1
  AUTHORS   Caputto, R. and Dixon, M.
  TITLE     Crystallization and identity of the triose and triosephosphate
            dehydrogenase of muscle.
  JOURNAL   Nature (Lond.) 156 (1945) 630-631.
REFERENCE   2
  AUTHORS   Cori, G.T., Slein, M.W. and Cori, C.F.
  TITLE     Crystalline D-glyceraldehyde-3-phosphate dehydrogenase from rabbit
            muscle.
  JOURNAL   J. Biol. Chem. 173 (1948) 605-618.
  ORGANISM  rabbit
REFERENCE   3
  AUTHORS   Hageman, R.H. and Arnon, D.I.
  TITLE     The isolation of triosephosphate dehydrogenase from pea seeds.
  JOURNAL   Arch. Biochem. Biophys. 55 (1955) 162-168.
  ORGANISM  Pisum sativum
REFERENCE   4
  AUTHORS   Velick, S.F. and Furfine, C.
  TITLE     Glyceraldehyde 3-phosphate dehydrogenase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 243-273.
REFERENCE   5
  AUTHORS   Velick, S.F. and Furfine, C.
  TITLE     Glyceraldehyde 3-phosphate dehydrogenase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 243-273.
REFERENCE   6
  AUTHORS   Warburg, O. and Christian, W.
  TITLE     Isolierung und Krystallisation des Proteins des oxydierenden
            Garungsferments.
  JOURNAL   Biochem. Z. 303 (1939) 40-68.
REFERENCE   7
  AUTHORS   Warburg, O. and Christian, W.
  TITLE     Isolierung und Krystallisation des Proteins des oxydierenden
            Garungsferments.
  JOURNAL   Biochem. Z. 303 (1939) 40-68.
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
ORTHOLOGY   KO: K00134  glyceraldehyde 3-phosphate dehydrogenase
GENES       HSA: 2597(GAPDH) 26330(GAPDHS)
            MMU: 14433(Gapdh) 14447(Gapdhs)
            RNO: 24383(Gapdh) 66020(Gapdhs)
            CFA: 403755(GAPDH) 476483(GAPDHS) 476969(LOC476969)
                 481027(LOC481027) 482889(LOC482889) 487478(LOC487478)
                 488591(LOC488591) 489985(LOC489985) 491880(LOC491880)
                 610978(LOC610978) 611353(LOC611353)
            BTA: 281181(GAPD)
            GGA: 374193(GAPDH)
            XLA: 380259(gapd) 380461(mg:bb02e05)
            XTR: 448356(gapdh)
            DRE: 406367(zgc:76908)
            SPU: 578260(LOC578260)
            DME: Dmel_CG12055(Gapdh1) Dmel_CG7769(DDB1) Dmel_CG8893(Gapdh2)
                 Dmel_CG9010
            CEL: F33H1.2(gpd-4) K10B3.7(gpd-3) K10B3.8(gpd-2) T09F3.3(gpd-1)
            ATH: AT1G12900(GAPA-2) AT1G13440(GAPC-2) AT1G16300(GAPCP-2)
                 AT1G42970(GAPB) AT1G79530(GAPCP-1) AT3G04120(GAPC)
            OSA: 4328446 4329892 4336044 4336216 4341782
            CME: CMJ250C CMM167C
            SCE: YGR192C(TDH3) YJL052W(TDH1) YJR009C(TDH2)
            AGO: AGOS_AER031C
            PIC: PICST_76518(TDH3) PICST_87252(TDH1)
            CGR: CAGL0G09383g
            SPO: SPBC32F12.11(gpd1) SPBC354.12
            ANI: AN2583.2 AN8041.2
            AFM: AFUA_5G01030 AFUA_5G01970 AFUA_8G02560
            AOR: AO090003001322 AO090011000414 AO090020000265
            ANG: An16g01830(gpdA)
            CNE: CNF03160
            ECU: ECU07_0800
            DDI: DDB_0185087(gpdA)
            PFA: PF14_0598
            CPV: cgd6_3790
            CHO: Chro.60434
            TAN: TA08145 TA15530
            TPV: TP02_0858 TP04_0383
            TET: TTHERM_00551160 TTHERM_00554190
            TBR: Tb10.6k15.3850 Tb927.6.4280 Tb927.6.4300
            TCR: 506943.50 506943.60 508537.10 509065.60 509065.70 509717.80
                 510105.230 510187.60 511235.20
            LMA: LmjF30.2970 LmjF30.2980 LmjF36.2350
            EHI: 12.t00040 224.t00017 360.t00004 55.t00032
            ECO: b1779(gapA)
            ECJ: JW1413(gapC) JW1768(gapA)
            ECE: Z2304(gapC) Z2818(gapA)
            ECS: ECs2022 ECs2488
            ECC: c1843 c2184(gapA)
            ECI: UTI89_C1638 UTI89_C1975(gapA)
            ECP: ECP_1421 ECP_1727
            ECV: APECO1_567 APECO1_847(gapA)
            ECW: EcE24377A_1597(gapC) EcE24377A_2003(gapA)
            ECX: EcHS_A1499(gapC) EcHS_A1864(gapA)
            STY: STY1825(gapA)
            STT: t1169(gapA)
            SPT: SPA1554(gapA)
            SEC: SC1303(gapA)
            STM: STM1290(gapA)
            YPE: YPO2157(gapA)
            YPK: y2165(gapA)
            YPM: YP_1957(gapA)
            YPA: YPA_1514
            YPN: YPN_1623
            YPP: YPDSF_0591
            YPS: YPTB2083(gapA)
            YPI: YpsIP31758_1987(gapA)
            SFL: SF1444(gapA) SF1795(gapC) SF1796(gapC_2)
            SFX: S1559(gapA)
            SFV: SFV_1436(gapA) SFV_1790(gapC)
            SSN: SSON_1384(gapA) SSON_1725(gapC)
            SBO: SBO_1316(gapA) SBO_1671(gapC)
            SDY: SDY_1488(gapA)
            ECA: ECA2344(gapA)
            PLU: plu2558(gapA)
            BUC: BU298(gapA)
            BAS: BUsg287(gapA)
            BAB: bbp276(gapA)
            BCC: BCc_181(gapA)
            WBR: WGLp108(gapA)
            SGL: SG1347
            ENT: Ent638_1675 Ent638_1955 Ent638_3340
            SPE: Spro_2728 Spro_3119 Spro_3946
            BFL: Bfl437(gapA)
            BPN: BPEN_451(gapA)
            HIT: NTHI0001(gapA)
            HDU: HD1291(gapA)
            HSO: HS_1466(gapA)
            PMU: PM0924(gapdH)
            MSU: MS1739(gapA)
            APL: APL_0434(gapA)
            XFA: XF0457
            XFT: PD1626(gapA)
            XCC: XCC3192(gapA)
            XCB: XC_0972
            XCV: XCV3469(gapA)
            XAC: XAC3352(gapA)
            XOO: XOO1203(gapA)
            XOM: XOO_1097(XOO1097)
            VCH: VC1069 VC2000
            VCO: VC0395_0393(gapA-2) VC0395_A0587(gap) VC0395_A1586(gapA-1)
            VVU: VV1_1141 VV1_3140
            VVY: VV0100 VV1147
            VPA: VP2157 VP2970
            VFI: VF0913 VF2360
            PPR: PBPRA2208 PBPRA2602
            PAE: PA3001 PA3195(ga)
            PAU: PA14_22890(gapA) PA14_25250(gapA)
            PPU: PP_1009(gap-1) PP_2149(gap-2)
            PPF: Pput_1047 Pput_3593 Pput_4837
            PST: PSPTO_1287(gap-1) PSPTO_2102(gap-2)
            PSB: Psyr_1108 Psyr_1897
            PSP: PSPPH_1176(gap1) PSPPH_1852(gap2)
            PFL: PFL_1955(gap) PFL_4623(gap)
            PFO: Pfl_3865 Pfl_4376
            PEN: PSEEN3714(gap-2) PSEEN4418(gap-1)
            PMY: Pmen_0459 Pmen_1311 Pmen_1451 Pmen_1522 Pmen_1594
            PAR: Psyc_1505(gapA) Psyc_1610(gpdH)
            PCR: Pcryo_1684 Pcryo_1842
            PRW: PsycPRwf_1559 PsycPRwf_1602
            ACI: ACIAD1255(gap) ACIAD2565(gap)
            SON: SO_0538(gapA-1) SO_2345(gapA-2) SO_2347(gapA-3)
            SDN: Sden_1084 Sden_1791 Sden_1793 Sden_3551
            SFR: Sfri_0648 Sfri_1940 Sfri_1942 Sfri_4002
            SAZ: Sama_0494 Sama_1806 Sama_1808 Sama_2758
            SBL: Sbal_0494 Sbal_0828 Sbal_2216 Sbal_2218
            SBM: Shew185_2153 Shew185_2155 Shew185_3539 Shew185_3830
            SLO: Shew_0419 Shew_0753 Shew_2000 Shew_2002
            SPC: Sputcn32_0873 Sputcn32_1223 Sputcn32_1889 Sputcn32_1891
                 Sputcn32_3815
            SSE: Ssed_0576 Ssed_0875 Ssed_2226 Ssed_2228
            SPL: Spea_0789 Spea_2104 Spea_2106 Spea_3736
            SHE: Shewmr4_0536 Shewmr4_0774 Shewmr4_2021 Shewmr4_2023
            SHM: Shewmr7_1952 Shewmr7_1954 Shewmr7_3249 Shewmr7_3495
            SHN: Shewana3_0534 Shewana3_2122 Shewana3_2124 Shewana3_2330
                 Shewana3_3352
            SHW: Sputw3181_2117 Sputw3181_2119 Sputw3181_2923 Sputw3181_3300
            ILO: IL2126
            CPS: CPS_2340(gap1) CPS_2344(gap2) CPS_3355(gap3)
            PHA: PSHAa1368(epd) PSHAa1900(gapA) PSHAb0182(gapB)
            PAT: Patl_1634 Patl_1640 Patl_2596
            SDE: Sde_1379
            PIN: Ping_1771 Ping_2004 Ping_3636
            MAQ: Maqu_1932 Maqu_3039 Maqu_3637
            CBU: CBU_1783(gap)
            LPN: lpg0138(gap)
            LPF: lpl0138(gap)
            LPP: lpp0153(gap)
            MCA: MCA2598(gap)
            FTU: FTT1368c(gapA)
            FTF: FTF1368c(gapA)
            FTL: FTL_1146
            FTH: FTH_1121(gapA)
            TCX: Tcr_0245 Tcr_1867 Tcr_1868
            NOC: Noc_2807
            AEH: Mlg_1514 Mlg_2260 Mlg_2840
            HHA: Hhal_0918
            HCH: HCH_02684(gap3)
            CSA: Csal_0372 Csal_0937 Csal_1482 Csal_1568
            ABO: ABO_1031(gapA) ABO_1776(gap) ABO_2614(gap)
            MMW: Mmwyl1_1079 Mmwyl1_1850 Mmwyl1_3958 Mmwyl1_4318
            AHA: AHA_3361(gap-1) AHA_3618(gap-2)
            DNO: DNO_0092(gap)
            BCI: BCI_0443(gapA)
            VOK: COSY_0071(gapA)
            NME: NMB0207 NMB2159
            NMA: NMA0062(gapA) NMA0246
            NMC: NMC0199(gapA) NMC2137
            NGO: NGO1776 NGO1931
            CVI: CV_0190 CV_0560(gapA)
            RSO: RSc2749(gapA)
            REU: Reut_A2840
            REH: H16_A3146(gapA) H16_B1386(cbbG2)
            RME: Rmet_1515 Rmet_2979
            BMA: BMA2468(gap)
            BXE: Bxe_A0566
            BVI: Bcep1808_0612
            BUR: Bcep18194_A3723
            BCN: Bcen_0156
            BCH: Bcen2424_0639
            BAM: Bamb_0539
            BPS: BPSL2952(gapA)
            BPM: BURPS1710b_3466(gap)
            BTE: BTH_I1196(gap)
            PNU: Pnuc_0228
            BPE: BP1000(gap)
            BPA: BPP1165(gap)
            BBR: BB1381(gap)
            RFR: Rfer_0919 Rfer_4111
            POL: Bpro_4826
            AAV: Aave_4588
            AJS: Ajs_3960
            VEI: Veis_0191
            MPT: Mpe_A0260(gapA) Mpe_A1586(gapA) Mpe_A2791(cbbG)
            HAR: HEAR0850(gap)
            MMS: mma_0833(gapA)
            NEU: NE0327(cbbG)
            NET: Neut_0333 Neut_1578
            NMU: Nmul_A0387
            EBA: ebA1102(gapA)
            AZO: azo2837(gapA)
            DAR: Daro_3592 Daro_3625
            TBD: Tbd_0160(cbbG)
            MFA: Mfla_2248
            HPY: HP0921(gap) HP1346
            HPA: HPAG1_0902 HPAG1_1293
            HHE: HH0492(gap_2) HH1157(gap_1)
            HAC: Hac_0275(gap) Hac_0698(gapA)
            WSU: WS0345(gapA) WS1026(gap_2)
            TDN: Tmden_1754
            CJE: Cj1403c(gapA)
            CJR: CJE1590(gapA)
            CJJ: CJJ81176_1402(gapA)
            CJU: C8J_1317(gapA)
            CJD: JJD26997_1737(gapA)
            ABU: Abu_0140(gapB) Abu_2132(gapA)
            NIS: NIS_0921 NIS_1492
            SUN: SUN_0253 SUN_1212 SUN_2204
            GSU: GSU1629(gap)
            GME: Gmet_1211 Gmet_1946
            GUR: Gura_1570 Gura_2061 Gura_2659 Gura_4250
            PCA: Pcar_1331 Pcar_2254 Pcar_2624
            PPD: Ppro_0343 Ppro_1714
            DVU: DVU0565(gap-1) DVU2144(gap-2)
            DVL: Dvul_1088 Dvul_2386
            DDE: Dde_2342 Dde_3736
            LIP: LI0764(gapA) LI1119(gapB)
            BBA: Bd1049(gapdh)
            DPS: DP0103 DP0822
            ADE: Adeh_1530
            AFW: Anae109_2282
            MXA: MXAN_2815(gapA)
            SAT: SYN_01810
            SFU: Sfum_1468 Sfum_2061 Sfum_2062
            OTS: OTBS_0952(gap)
            WOL: WD0451(gap)
            WBM: Wbm0298(gapA)
            AMA: AM1283(gapB)
            NSE: NSE_0434(gap)
            PUB: SAR11_0586(gap)
            MLO: mlr3750
            MES: Meso_3439
            PLA: Plav_2107
            SME: SMc03979(gap)
            SMD: Smed_2651
            ATU: Atu3737(gapA)
            ATC: AGR_L_2195
            RET: RHE_CH03496(gap)
            RLE: RL4007(gap)
            BME: BMEI0310
            BMF: BAB1_1741(gap)
            BMS: BR1728(gap)
            BMB: BruAb1_1713(gap)
            OAN: Oant_1189
            BJA: bll1523(gapA)
            BRA: BRADO1124(cbbG)
            BBT: BBta_0448(cbbG) BBta_6925(cbbG)
            RPA: RPA0944(cbbG)
            RPB: RPB_1642 RPB_4467
            RPC: RPC_4767
            RPD: RPD_4313
            RPE: RPE_4728
            NWI: Nwi_2735
            NHA: Nham_3532
            BHE: BH15080(gap)
            BQU: BQ12000(gap)
            XAU: Xaut_3075 Xaut_3960
            CCR: CC_3248
            SIL: SPO0701(gap-1) SPO3878(gap-4)
            SIT: TM1040_0417 TM1040_0525 TM1040_1111 TM1040_2394
            RSP: RSP_2959(gapB) RSP_3269(gapB) RSP_4211(gapA-1)
            RSH: Rsph17029_1604 Rsph17029_4002
            RSQ: Rsph17025_1387 Rsph17025_1411
            JAN: Jann_1695 Jann_1698 Jann_3828
            RDE: RD1_2398(gap) RD1_2880(gap) RD1_2984(gap)
            PDE: Pden_1060 Pden_4465
            MMR: Mmar10_2597
            HNE: HNE_3179(gap)
            ZMO: ZMO0177(gap)
            NAR: Saro_1967
            SAL: Sala_1319
            SWI: Swit_2602
            ELI: ELI_05210
            GOX: GOX0508
            GBE: GbCGDNIH1_0311
            ACR: Acry_1221
            RRU: Rru_A0222
            MAG: amb0512
            MGM: Mmc1_0446 Mmc1_2399 Mmc1_2970
            ABA: Acid345_2541
            SUS: Acid_7375
            BSU: BG10827(gapA) BG12592(gapB)
            BHA: BH3149(gapB) BH3560(gap)
            BAN: BA4827(gap-1) BA5369(gap-2)
            BAR: GBAA4827(gap-1) GBAA5369(gap-2)
            BAA: BA_0227 BA_5251
            BAT: BAS4478 BAS4989
            BCE: BC5140
            BCA: BCE_4714(gap) BCE_5242(gap)
            BCZ: BCZK4324(gap) BCZK4828(gap)
            BCY: Bcer98_3682
            BTK: BT9727_4818(gap)
            BTL: BALH_4631(gap)
            BLI: BL00390(gapB) BL03464(gapA)
            BLD: BLi03052(gapB) BLi03665(gapA)
            BCL: ABC2705(gapB) ABC3021(gapA)
            BAY: RBAM_026060(gapB) RBAM_031300(gapA)
            BPU: BPUM_3057(gapA)
            OIH: OB2160(gap) OB2438(gapA)
            GKA: GK2726 GK3058
            SAU: SA0727(gap) SA1510(gapB)
            SAV: SAV0772(gap) SAV1687(gapB)
            SAM: MW0734(gap) MW1630(gapB)
            SAR: SAR0828(gap1) SAR1766(gap2)
            SAS: SAS0738 SAS1615
            SAC: SACOL0838(gapA1) SACOL1734(gapA2)
            SAB: SAB0728(gap)
            SAA: SAUSA300_1633(gap)
            SAO: SAOUHSC_00795 SAOUHSC_01794
            SAJ: SaurJH9_0797 SaurJH9_1744
            SAH: SaurJH1_0813 SaurJH1_1778
            SEP: SE0557 SE1361
            SER: SERP0442(gapA-1) SERP1250(gapA-2)
            SHA: SH1238(gapB) SH2113(gap)
            SSP: SSP1078 SSP1916
            LMO: lmo2459(gap)
            LMF: LMOf2365_2432(gap)
            LIN: lin2553(gap)
            LWE: lwe2408(gap)
            LLA: L0004(gapA) L0005(gapB)
            LLC: LACR_0580 LACR_2555
            LLM: llmg_0530(gapA) llmg_2539(gapB)
            SPY: SPy_0274(plr)
            SPZ: M5005_Spy_0233(plr)
            SPM: spyM18_0261(gapA)
            SPG: SpyM3_0201(plr)
            SPS: SPs0207
            SPH: MGAS10270_Spy0233(plr)
            SPI: MGAS10750_Spy0228(plr)
            SPJ: MGAS2096_Spy0252(plr)
            SPK: MGAS9429_Spy0235(plr)
            SPF: SpyM50212(gapA)
            SPA: M6_Spy0265
            SPB: M28_Spy0227(plr)
            SPN: SP_2012
            SPR: spr1825(gapA)
            SAG: SAG1768(gap)
            SAN: gbs1811
            SAK: SAK_1790(gap)
            SMU: SMU.360(gapC)
            STC: str1788(gapA1)
            STL: stu1788(gapA1)
            SSA: SSA_2108(gapA)
            LPL: lp_0789(gapB)
            LJO: LJ0872
            LAC: LBA0698
            LSA: LSA0604(gap)
            LSL: LSL_1166(gapA)
            LDB: Ldb0635(gap)
            LBU: LBUL_0567
            LBR: LVIS_0661
            LCA: LSEI_0967
            EFA: EF1526(gap-1) EF1964(gap-2)
            OOE: OEOE_0404
            STH: STH1645 STH2164
            CAC: CAC0709(gapC)
            CPE: CPE1304(gapC)
            CPF: CPF_1511(gap)
            CPR: CPR_1301(gap)
            CTC: CTC00378
            CNO: NT01CX_1404
            CTH: Cthe_0137
            CDF: CD1767(gapA) CD3174(gapB)
            CBO: CBO0226(gap1) CBO1095(gap2)
            CBE: Cbei_0597
            CKL: CKL_1457(gap)
            AMT: Amet_3580 Amet_3679
            CHY: CHY_0280(gap)
            DSY: DSY1507 DSY1609(gapA) DSY1634
            DRM: Dred_0132 Dred_2991
            SWO: Swol_0272
            CSC: Csac_1953
            TTE: TTE1762(gapA)
            MTA: Moth_0262
            MPN: MPN430(gap)
            MPU: MYPU_0460(gap)
            MPE: MYPE8170(gap)
            MGA: MGA_0330 MGA_1186
            MMY: MSC_0679(gap)
            MMO: MMOB1870(gapA)
            MHY: mhp036(gap)
            MHJ: MHJ_0031(gap)
            MHP: MHP7448_0035(gap)
            MSY: MS53_0200(gap) MS53_0270(gapA)
            MCP: MCAP_0632(gap)
            POY: PAM175(gapA)
            AYW: AYWB_545(gapA)
            MFL: Mfl578
            MTU: Rv1436(gap)
            MTC: MT1480(gap)
            MBO: Mb1471(gap)
            MBB: BCG_1497(gap)
            MLE: ML0570(gap)
            MPA: MAP1164(gap)
            MSM: MSMEG_3084(gap)
            MVA: Mvan_2703
            MGI: Mflv_3710
            MMC: Mmcs_2404
            MKM: Mkms_2450
            MJL: Mjls_2444
            CGL: NCgl0900(cgl0937) NCgl1526(cgl1588)
            CGB: cg1069(gapX) cg1791(gap)
            CEF: CE1008 CE1706(gap)
            CDI: DIP1310(gap)
            CJK: jk0882(gapX) jk1001(gapA)
            NFA: nfa35890(gap)
            RHA: RHA1_ro03427(gap1) RHA1_ro07177(gap2)
            SCO: SCO1947(gap1) SCO7511(gap2)
            SMA: SAV2990(gap1) SAV6296(gap2)
            TWH: TWT300(gap)
            TWS: TW472(gap)
            LXX: Lxx11520(gap)
            CMI: CMM_1744(gapA)
            ART: Arth_2438
            AAU: AAur_2411(gap)
            PAC: PPA0816
            NCA: Noca_2530 Noca_4872
            TFU: Tfu_2017
            FRA: Francci3_1637 Francci3_4022
            FAL: FRAAL4588(gapA)
            ACE: Acel_1114
            KRA: Krad_2931
            SEN: SACE_2143(gap)
            STP: Strop_3098
            BLO: BL1363(gap)
            BAD: BAD_1079(gap)
            RXY: Rxyl_2005
            FNU: FN0652
            RBA: RB2627
            CTR: CT505(gapA)
            CTA: CTA_0554(gapA)
            CMU: TC0792
            CPN: CPn0624(gapA)
            CPA: CP0123
            CPJ: CPj0624(gapA)
            CPT: CpB0650
            CCA: CCA00116(gap)
            CAB: CAB115(gapA)
            CFE: CF0890(gapA)
            PCU: pc0435(gapA)
            BBU: BB0057(gap)
            BGA: BG0056(gap)
            BAF: BAPKO_0057(gap)
            TPA: TP0844
            TDE: TDE1488(gap)
            LIL: LA1704(gapL)
            LIC: LIC12090(gapA)
            LBJ: LBJ_1220(gapA)
            LBL: LBL_1271(gapA)
            SYN: slr0884(gap1)
            SYW: SYNW0799(gap3)
            SYC: syc1268_d(gap1) syc2155_c(gap1)
            SYF: Synpcc7942_0245 Synpcc7942_1939
            SYD: Syncc9605_0030 Syncc9605_1846
            SYE: Syncc9902_0026 Syncc9902_1815
            SYG: sync_0029(gap-1) sync_0872(gap-2)
            SYR: SynRCC307_0428(gap3)
            SYX: SynWH7803_0789(gapA) SynWH7803_1460(gap3)
            CYA: CYA_0020(gap-1) CYA_2179(gap-3)
            CYB: CYB_1429(gap-1) CYB_2306(gap-3)
            TEL: tll0043(gap1) tll1466(gap2)
            GVI: gll3325(gap1)
            ANA: all2566(gap1) all5062(gap2) alr1095(gap3)
            AVA: Ava_0495 Ava_2318 Ava_3715
            PMA: Pro1577(gap3)
            PMM: PMM0713(gap1)
            PMT: PMT1000
            PMN: PMN2A_0445 PMN2A_1350
            PMI: PMT9312_0023 PMT9312_0725
            PMB: A9601_00221(gap2)
            PMC: P9515_00221(gap2)
            PMF: P9303_00271(gap2) P9303_11051(gap3)
            PMG: P9301_00221(gap2) P9301_12361(gap3)
            PMH: P9215_00221(gap2)
            PME: NATL1_00221(gap2) NATL1_11571(gap3)
            TER: Tery_2881 Tery_3274
            BTH: BT_4263
            BFR: BF0967
            BFS: BF0885(gap)
            PGI: PG2124(gapA)
            SRU: SRU_1200(gap)
            CHU: CHU_0251(gap) CHU_2987(gapA)
            GFO: GFO_0622(gap) GFO_2130(gapA) GFO_2704(gap)
            FJO: Fjoh_0020 Fjoh_0228 Fjoh_4590
            FPS: FP1217(gapA2) FP1470(gapA1) FP1613(gapA3)
            CTE: CT1480(gapA)
            CCH: Cag_1420
            CPH: Cpha266_1870
            PVI: Cvib_1310
            PLT: Plut_1485
            DEB: DehaBAV1_0565
            RRS: RoseRS_0387 RoseRS_1226 RoseRS_1851
            RCA: Rcas_1157 Rcas_2314 Rcas_3283
            DRA: DR_1343
            DGE: Dgeo_1133
            TTH: TTC0549
            TTJ: TTHA0905
            AAE: aq_1065(gap)
            TMA: TM0688
            TPT: Tpet_0243
            TME: Tmel_1266
            FNO: Fnod_0740
            MBN: Mboo_1283
            HMA: rrnAC2363(gapA)
            IHO: Igni_1001
            TPE: Tpen_0757
STRUCTURES  PDB: 1A7K  1B7G  1CER  1CF2  1CRW  1DBV  1DC3  1DC4  1DC5  1DC6  
                 1DSS  1GAD  1GAE  1GD1  1GGA  1GPD  1GYP  1GYQ  1HDG  1I32  
                 1I33  1IHX  1IHY  1J0X  1K3T  1ML3  1NPT  1NQ5  1NQA  1NQO  
                 1OBF  1QXS  1S7C  1SZJ  1U8F  1VC2  1YWG  1ZNQ  2B4R  2B4T  
                 2DBV  2EP7  2G82  2GD1  2I5P  3DBV  3GPD  4DBV  4GPD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.12
            ExPASy - ENZYME nomenclature database: 1.2.1.12
            ExplorEnz - The Enzyme Database: 1.2.1.12
            ERGO genome analysis and discovery system: 1.2.1.12
            BRENDA, the Enzyme Database: 1.2.1.12
            CAS: 9001-50-7
///
ENTRY       EC 1.2.1.13                 Enzyme
NAME        glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating);
            triosephosphate dehydrogenase (NADP+);
            dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine
            dinucleotide phosphate) (phosphorylating);
            glyceraldehyde phosphate dehydrogenase (nicotinamide adenine
            dinucleotide phosphate) (phosphorylating);
            NADP+-glyceraldehyde-3-phosphate dehydrogenase;
            NADP+-glyceraldehyde phosphate dehydrogenase;
            NADP+-dependent glyceraldehyde phosphate dehydrogenase;
            NADP+-triose phosphate dehydrogenase;
            glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating);
            GAPDH
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-glyceraldehyde-3-phosphate:NADP+ oxidoreductase (phosphorylating)
REACTION    D-glyceraldehyde 3-phosphate + phosphate + NADP+ =
            3-phospho-D-glyceroyl phosphate + NADPH + H+ [RN:R01063]
ALL_REAC    R01063;
            (other) R01061
SUBSTRATE   D-glyceraldehyde 3-phosphate [CPD:C00118];
            phosphate [CPD:C00009];
            NADP+ [CPD:C00006]
PRODUCT     3-phospho-D-glyceroyl phosphate [CPD:C00236];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13804190]
  AUTHORS   BRENNEMAN FN, VOLK WA.
  TITLE     Glyceraldehyde phosphate dehydrogenase activity with
            triphosphopyridine nucleotide and with diphosphopyridine nucleotide.
  JOURNAL   J. Biol. Chem. 234 (1959) 2443-7.
  ORGANISM  Alcaligenes faecalis
REFERENCE   2
  AUTHORS   Gibbs, M.
  TITLE     TPN triosephosphate dehydrogenase from plant tissue.
  JOURNAL   Methods Enzymol. 1 (1955) 411-415.
  ORGANISM  Pisum sativum
REFERENCE   3  [PMID:13271400]
  AUTHORS   ROSENBERG LL, ARNON DI.
  TITLE     The preparation and properties of a new glyceraldehyde-3-phosphate
            dehydrogenase from photosynthetic tissues.
  JOURNAL   J. Biol. Chem. 217 (1955) 361-71.
  ORGANISM  spinach
PATHWAY     PATH: map00710  Carbon fixation
ORTHOLOGY   KO: K05298  glyceraldehyde-3-phosphate dehydrogenase (NADP+)
                        (phosphorylating)
GENES       ATH: AT3G26650(GAPA)
            CME: CMJ042C
            PMA: Pro0023(gap2)
            PMM: PMM0023(gap2)
            PMT: PMT0028(gap2)
            PMB: A9601_00221(gap2)
            PMC: P9515_00221(gap2)
            PMF: P9303_00271(gap2)
            PMG: P9301_00221(gap2)
            PME: NATL1_00221(gap2)
STRUCTURES  PDB: 1JN0  1NBO  1RM3  1RM4  1RM5  2D2I  2DUU  2HKI  2PKQ  2PKR  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.13
            ExPASy - ENZYME nomenclature database: 1.2.1.13
            ExplorEnz - The Enzyme Database: 1.2.1.13
            ERGO genome analysis and discovery system: 1.2.1.13
            BRENDA, the Enzyme Database: 1.2.1.13
            CAS: 37250-87-6
///
ENTRY       EC 1.2.1.14       Obsolete  Enzyme
NAME        Transferred to 1.1.1.205
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Transferred entry: now EC 1.1.1.205 IMP dehydrogenase (EC 1.2.1.14
            created 1961, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.14
            ExPASy - ENZYME nomenclature database: 1.2.1.14
            ExplorEnz - The Enzyme Database: 1.2.1.14
            ERGO genome analysis and discovery system: 1.2.1.14
            BRENDA, the Enzyme Database: 1.2.1.14
///
ENTRY       EC 1.2.1.15                 Enzyme
NAME        malonate-semialdehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-oxopropanoate:NAD(P)+ oxidoreductase
REACTION    3-oxopropanoate + NAD(P)+ + H2O = malonate + NAD(P)H + 2 H+
            [RN:R01604 R01607]
ALL_REAC    R01604 R01607
SUBSTRATE   3-oxopropanoate [CPD:C00222];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     malonate [CPD:C00383];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Nakamura, K. and Bernheim, F.
  TITLE     Studies on malonic semialdehyde dehydrogenase from Pseudomonas
            aeruginosa.
  JOURNAL   Biochim. Biophys. Acta 50 (1961) 147-152.
  ORGANISM  Pseudomonas aeruginosa
PATHWAY     PATH: map00410  beta-Alanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.15
            ExPASy - ENZYME nomenclature database: 1.2.1.15
            ExplorEnz - The Enzyme Database: 1.2.1.15
            ERGO genome analysis and discovery system: 1.2.1.15
            BRENDA, the Enzyme Database: 1.2.1.15
            CAS: 9028-94-8
///
ENTRY       EC 1.2.1.16                 Enzyme
NAME        succinate-semialdehyde dehydrogenase [NAD(P)+];
            succinate semialdehyde dehydrogenase (nicotinamide adenine
            dinucleotide (phosphate));
            succinate-semialdehyde dehydrogenase [NAD(P)+]
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     succinate-semialdehyde:NAD(P)+ oxidoreductase
REACTION    succinate semialdehyde + NAD(P)+ + H2O = succinate + NAD(P)H + 2 H+
            [RN:R00713 R00714]
ALL_REAC    R00713 R00714
SUBSTRATE   succinate semialdehyde [CPD:C00232];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     succinate [CPD:C00042];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Jakoby, W.B.
  TITLE     Aldehyde dehydrogenases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
REFERENCE   2  [PMID:13654295]
  AUTHORS   JAKOBY WB, SCOTT EM.
  TITLE     Aldehyde oxidation. III. Succinic semialdehyde dehydrogenase.
  JOURNAL   J. Biol. Chem. 234 (1959) 937-40.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   3
  AUTHORS   Nirenberg, M.W. and Jakoby, W.B.
  TITLE     Enzymatic utilization of gamma-hydroxybutyric acid.
  JOURNAL   J. Biol. Chem. 235 (1960) 954-960.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00350  Tyrosine metabolism
            PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K00135  succinate-semialdehyde dehydrogenase (NADP+)
GENES       ATH: AT1G79440(ALDH5F1)
            OSA: 4328459
            CME: CMR066C
            SCE: YBR006W(UGA2)
            AGO: AGOS_AER007W
            PIC: PICST_40468(UGA2) PICST_44169(ALD4) PICST_57266(UGA22)
                 PICST_60847(ALD3)
            SPO: SPAC1002.12c SPAC139.05
            ANI: AN7315.2
            AFM: AFUA_8G02160
            CNE: CND01570 CNI00900
            UMA: UM05610.1
            TET: TTHERM_00809400 TTHERM_00857780 TTHERM_01106130
            TCR: 507641.60
            LMA: LmjF36.1760
            ECO: b2661(gabD)
            ECJ: JW2636(gabD)
            ECE: Z3959(gabD)
            ECS: ECs3522
            ECC: c3209(gabD)
            ECI: UTI89_C3016(gabD)
            ECP: ECP_2624
            ECV: APECO1_3859(gabD)
            ECW: EcE24377A_2941(gabD)
            ECX: EcHS_A2796(gabD)
            STY: STY2911(gabD)
            STT: t2686(gabD)
            SPT: SPA2648(gabD) SPA4340
            SEC: SC2723(gabD)
            STM: STM2791(gabD) STM4519
            YPE: YPO1290
            YPK: y0176(gabD) y2894(gabD)
            YPM: YP_1301(gabD1)
            YPA: YPA_1008 YPA_3700
            YPN: YPN_3485
            YPS: YPTB1322 YPTB3545
            YPI: YpsIP31758_0422(gabD)
            YEN: YE3793(gabD)
            SSN: SSON_2805(gabD)
            ECA: ECA0280 ECA2054(gabD)
            PLU: plu0984(gabD)
            SGL: SG0164
            ENT: Ent638_3676
            HSO: HS_0407(attK) HS_1682(attK)
            PMU: PM1536(attK)
            XCC: XCC2336(gabD)
            XCB: XC_1780
            XCV: XCV2647
            XAC: XAC2469(gabD)
            XOO: XOO2774(gabD)
            XOM: XOO_2614(XOO2614)
            VCH: VC1745
            VCO: VC0395_A1344(gabD)
            VVU: VV2_1266
            VVY: VV1589 VVA0093
            VPA: VP1772 VP2630
            PPR: PBPRB0638
            PAE: PA0265(gabD)
            PAU: PA14_03430(gabD)
            PAP: PSPA7_4381
            PPU: PP_0213(gabD) PP_2488 PP_4422
            PST: PSPTO_0257(gabD-1) PSPTO_0300(gabD-2)
            PSB: Psyr_0091 Psyr_0149
            PSP: PSPPH_0096(gabD1) PSPPH_2572(gabD2)
            PFL: PFL_0185(gabD)
            PFO: Pfl_0187
            PEN: PSEEN0189(gabD)
            PAR: Psyc_0808
            PCR: Pcryo_0818
            ACI: ACIAD0960 ACIAD2539(gabD) ACIAD3445(gabD)
            SON: SO_1275(gabD)
            SDN: Sden_0909
            SFR: Sfri_2032 Sfri_3004
            SAZ: Sama_2637
            SBL: Sbal_1113
            SLO: Shew_3173
            SPC: Sputcn32_1099
            SHE: Shewmr4_2913
            SHM: Shewmr7_2995
            SHN: Shewana3_3092
            SHW: Sputw3181_3065
            ILO: IL1992
            CPS: CPS_2023(gabD1) CPS_4665(gabD2)
            PHA: PSHAa1590 PSHAa2402(gabD) PSHAa2665(gabD)
            PAT: Patl_0896
            SDE: Sde_2257
            PIN: Ping_1888 Ping_2783
            MAQ: Maqu_3647
            CBU: CBU_1204
            LPN: lpg1583
            LPF: lpl1442
            LPP: lpp1541
            MCA: MCA1756(gabD)
            FTA: FTA_0019 FTA_0021
            FTN: FTN_0127(gabD)
            TCX: Tcr_0222 Tcr_1887
            NOC: Noc_0391
            AEH: Mlg_0875
            CSA: Csal_0646 Csal_1290 Csal_2291 Csal_3191
            ABO: ABO_0511(gabD) ABO_1134
            AHA: AHA_3001
            NME: NMB1488
            NMA: NMA1696(gabD)
            NMC: NMC1423(gabD)
            NGO: NGO1061
            CVI: CV_3927(gabD)
            RSO: RSc0028(gabD1) RSp1611(gabD2)
            REU: Reut_B4208 Reut_B4277 Reut_B5660 Reut_C5901 Reut_C6272
            REH: H16_B0982(gabD1) H16_B1179(gabD2) H16_B1537(gabD3)
                 H16_B2057(gabD4)
            RME: Rmet_3961 Rmet_4942
            BMA: BMAA1481(gabD)
            BML: BMA10299_2125(gabD)
            BMN: BMA10247_A0808(gabD)
            BXE: Bxe_A2060 Bxe_B0833 Bxe_B1485 Bxe_B1976 Bxe_B2363 Bxe_B2498
                 Bxe_C0060 Bxe_C0300 Bxe_C0523 Bxe_C0666 Bxe_C0768
            BVI: Bcep1808_3590 Bcep1808_4941 Bcep1808_4963 Bcep1808_5459
                 Bcep1808_6431
            BUR: Bcep18194_B0279 Bcep18194_B0353 Bcep18194_B1600
                 Bcep18194_B2827 Bcep18194_C6772
            BCN: Bcen_3004 Bcen_3958 Bcen_5800 Bcen_6452
            BCH: Bcen2424_4409 Bcen2424_5362 Bcen2424_6164 Bcen2424_6687
            BAM: Bamb_3830 Bamb_4712 Bamb_6023 Bamb_6346
            BPS: BPSL1654(gabD) BPSS0280(gabD)
            BPM: BURPS1710b_2207(gabD) BURPS1710b_A1820(gabD)
            BPD: BURPS668_A0492
            BTE: BTH_II2120
            PNU: Pnuc_0263
            BPE: BP0757(gabD) BP0919(gabD) BP1976(gabD)
            BPA: BPP0319(gabD) BPP1286(gabG) BPP2356(gabD) BPP2812(gabD)
                 BPP3160(gabD)
            BBR: BB0322(gabD) BB1806(gabD) BB2351(gabG) BB3133(gabD)
                 BB3561(gabD)
            RFR: Rfer_0598
            POL: Bpro_0062 Bpro_0086 Bpro_2917 Bpro_5115
            PNA: Pnap_2636
            AAV: Aave_1365 Aave_2192
            AJS: Ajs_1978
            VEI: Veis_2146 Veis_3197 Veis_4041 Veis_4280 Veis_4520
            MPT: Mpe_A2324
            HAR: HEAR2670(gabD)
            MMS: mma_2905(gabD)
            NEU: NE2000(gabD)
            NET: Neut_0700
            NMU: Nmul_A2448
            EBA: ebA2996(gabD)
            AZO: azo0222(gabD1) azo1920(gabD2) azo2250(thmS1) azo3021(thmS2)
            DAR: Daro_3748
            CFF: CFF8240_0917
            CHA: CHAB381_1497
            ABU: Abu_2148
            GME: Gmet_3395
            PCA: Pcar_1074
            PPD: Ppro_2886
            BBA: Bd1926(gabD)
            ADE: Adeh_3025
            RCO: RC0621(gabD)
            RFE: RF_0684(gabD)
            RBE: RBE_0336(gabD)
            PUB: SAR11_0766(gabD)
            MLO: mll1168 mll5719 mll5809 mll7043 mll7128
            MES: Meso_1323
            SME: SMa0260(gabD3) SMa0805(gabD4) SMa1848(gabD5) SMb20424
                 SMb21185(gabD2) SMc02780(gabD1)
            ATU: Atu3403(attK2) Atu4247(attK) Atu4762(gabD) Atu5137(attK)
            ATC: AGR_L_1228 AGR_L_241(ssdH) AGR_L_2838 AGR_pAT_197(attK)
            RET: RHE_CH00092(gabDch) RHE_CH02147 RHE_PC00032(gabDc)
                 RHE_PF00201(ypf00097) RHE_PF00340(gabDf1) RHE_PF00364(gabDf2)
            RLE: RL0101(gabD) pRL100134(gabD) pRL100252(gabD) pRL110161
                 pRL120044(gabD) pRL120603(gabD) pRL120628(gabD)
            BME: BMEI0386
            BMF: BAB1_1655(gabD)
            BMS: BR1640(gabD)
            BMB: BruAb1_1628(gabD)
            BOV: BOV_1588(gabD)
            BJA: bll3998 blr0807
            BRA: BRADO0028(gabD)
            BBT: BBta_0032(gabD) BBta_1602 BBta_3039
            RPA: RPA0461(gabD1) RPA2324(gabD2)
            RPB: RPB_0577 RPB_3136
            RPC: RPC_0104 RPC_0454 RPC_3493
            RPD: RPD_0255
            RPE: RPE_0222 RPE_3204
            NHA: Nham_1844
            CCR: CC_3140
            SIL: SPO1137(gabD-1) SPO3328(gabD-2) SPOA0275(gabD-3)
            SIT: TM1040_1597 TM1040_2493 TM1040_2692 TM1040_3263
            RSP: RSP_1012(gabD4) RSP_4032
            RSH: Rsph17029_2672
            JAN: Jann_3829
            RDE: RD1_0927(gabD)
            PDE: Pden_0223 Pden_0243 Pden_0289 Pden_1013 Pden_2257 Pden_4969
            MMR: Mmar10_0971
            HNE: HNE_2325(gabD)
            ZMO: ZMO1754(ssdA)
            NAR: Saro_0797 Saro_2603 Saro_2936
            SAL: Sala_2116
            ELI: ELI_12665(gabD2)
            GOX: GOX0499 GOX1122
            GBE: GbCGDNIH1_1537
            RRU: Rru_A0134 Rru_A0462
            MAG: amb0814 amb1321
            ABA: Acid345_0377 Acid345_1443
            SUS: Acid_3101
            BSU: BG12044(gabD)
            BHA: BH0995 BH3316(gabD)
            BAN: BA0327(gabD)
            BAR: GBAA0327(gabD)
            BAA: BA_0897
            BAT: BAS0312
            BCE: BC0357 BC2241
            BCA: BCE_0356(gabD)
            BCZ: BCZK0299(gadD) BCZK2069(gabD)
            BTK: BT9727_0295(gadD) BT9727_2073(gabD)
            BTL: BALH_0319(gadD)
            BLI: BL01765(gabD)
            BLD: BLi00476(gabD)
            BCL: ABC0331 ABC1452(gabD)
            BPU: BPUM_0364(gabD)
            OIH: OB2247 OB2863
            SAO: SAOUHSC_02363
            SHA: SH0214
            SSP: SSP0188
            LMO: lmo0913
            LMF: LMOf2365_0935(gabD)
            LIN: lin0913
            LWE: lwe0897(gabD)
            SPY: SPy_1067(gabD)
            SPZ: M5005_Spy_0790(gabD)
            SPM: spyM18_1041
            SPG: SpyM3_0748
            SPS: SPs0949
            SPH: MGAS10270_Spy0903(gabD)
            SPI: MGAS10750_Spy0938(gabD)
            SPJ: MGAS2096_Spy0861(gabD)
            SPK: MGAS9429_Spy0904(gabD)
            SPA: M6_Spy0807
            SPB: M28_Spy0764(gabD)
            SAG: SAG1124
            SAN: gbs1192
            SAK: SAK_1211
            SMU: SMU.2127
            LPL: lp_3092(gabD)
            LAC: LBA1632(ssdH)
            LSL: LSL_1298
            LBR: LVIS_0323
            LCA: LSEI_2278
            STH: STH722
            CDF: CD2342(sucD)
            CKL: CKL_3015(sucD)
            DSY: DSY1502
            MTU: Rv0234c(gabD1) Rv1731(gabD2)
            MTC: MT0245(gabD-1) MT1772(gabD-2)
            MBO: Mb0239c(gabD1) Mb1760(gabD2)
            MBB: BCG_0271c(gabD1) BCG_1770(gabD2)
            MLE: ML2573(gabD)
            MPA: MAP3673c(gabD2)
            MAV: MAV_4936
            MSM: MSMEG_0582 MSMEG_2488 MSMEG_5538 MSMEG_5912 MSMEG_6452
                 MSMEG_6702
            MVA: Mvan_4876
            MGI: Mflv_1858
            MMC: Mmcs_4333
            MKM: Mkms_4419
            MJL: Mjls_4713
            CGL: NCgl0049(cgl0051) NCgl0463(cgl0480)
            CGB: cg0067(gabD3) cg0567(gabD2) cg3004(gabD1)
            CEF: CE1587
            CDI: DIP0833 DIP2331
            CJK: jk0450 jk1473
            NFA: nfa26820 nfa27730(gabD) nfa34350 nfa45120 nfa46640 nfa49970
            RHA: RHA1_ro00587 RHA1_ro00658(gabD1) RHA1_ro00822(gabD2)
                 RHA1_ro01994 RHA1_ro02683 RHA1_ro03944 RHA1_ro04543(gabD3)
                 RHA1_ro05568(gabD4) RHA1_ro05596(gabD5) RHA1_ro08792(gabD6)
            SCO: SCO1204(2SCG58.04) SCO4780(SCD63.12) SCO7035(gabD)
            SMA: SAV5016(gabD1) SAV7134(gabD2) SAV7159(gabD3)
            CMI: CMM_0933(gabD)
            ART: Arth_1207 Arth_1755 Arth_1786
            PAC: PPA0079
            NCA: Noca_0646 Noca_0692 Noca_1116 Noca_4473 Noca_4598
            TFU: Tfu_2949
            FAL: FRAAL6362(gabD) FRAAL6372
            SEN: SACE_3767(gabD3)
            RXY: Rxyl_1760 Rxyl_2905 Rxyl_3175
            RBA: RB10968(gabD)
            SYN: slr0370(gabD)
            SYG: sync_1835
            CYB: CYB_1893
            TEL: tlr0221
            GVI: gll2805
            ANA: all3556
            AVA: Ava_3534
            PMB: A9601_03571
            PMC: P9515_03631
            PMF: P9303_21711
            PMG: P9301_03581
            PME: NATL1_04241
            GFO: GFO_2167(gabD)
            CCH: Cag_0330
            PLT: Plut_0352
            DRA: DR_A0003 DR_A0343
            DGE: Dgeo_1120
            TTH: TTC0634
            TTJ: TTHA0996
            MAC: MA0705 MA1355
            MBA: Mbar_A0503 Mbar_A1620 Mbar_A2542
            MMA: MM_0838 MM_2341
            MBU: Mbur_0175
            MHU: Mhun_1783
            HAL: VNG0808G(gabD)
            HMA: rrnB0219(gabD)
            PTO: PTO0332
            RCI: RCIX91(gabD)
            PIS: Pisl_0249
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.16
            ExPASy - ENZYME nomenclature database: 1.2.1.16
            ExplorEnz - The Enzyme Database: 1.2.1.16
            ERGO genome analysis and discovery system: 1.2.1.16
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.16
            BRENDA, the Enzyme Database: 1.2.1.16
            CAS: 37250-88-7
///
ENTRY       EC 1.2.1.17                 Enzyme
NAME        glyoxylate dehydrogenase (acylating)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     glyoxylate:NADP+ oxidoreductase (CoA-oxalylating)
REACTION    glyoxylate + CoA + NADP+ = oxalyl-CoA + NADPH + H+ [RN:R00468]
ALL_REAC    R00468
SUBSTRATE   glyoxylate [CPD:C00048];
            CoA [CPD:C00010];
            NADP+ [CPD:C00006]
PRODUCT     oxalyl-CoA [CPD:C00313];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Quayle, J.R. and Taylor, G.A.
  TITLE     Carbon assimilation by Pseudomonas oxalaticus (OX1). 5. Purification
            and properties of glyoxylic dehydrogenase.
  JOURNAL   Biochem. J. 78 (1961) 611-615.
  ORGANISM  Pseudomonas oxalaticus
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.17
            ExPASy - ENZYME nomenclature database: 1.2.1.17
            ExplorEnz - The Enzyme Database: 1.2.1.17
            ERGO genome analysis and discovery system: 1.2.1.17
            BRENDA, the Enzyme Database: 1.2.1.17
            CAS: 9028-96-0
///
ENTRY       EC 1.2.1.18                 Enzyme
NAME        malonate-semialdehyde dehydrogenase (acetylating);
            malonic semialdehyde oxidative decarboxylase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-oxopropanoate:NAD(P)+ oxidoreductase (decarboxylating,
            CoA-acetylating)
REACTION    3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H
            [RN:R00705 R00706]
ALL_REAC    R00705 R00706;
            (other) R00740 R03381
SUBSTRATE   3-oxopropanoate [CPD:C00222];
            CoA [CPD:C00010];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     acetyl-CoA [CPD:C00024];
            CO2 [CPD:C00011];
            NADH [CPD:C00004];
            NADPH [CPD:C00005]
REFERENCE   1  [PMID:13712439]
  AUTHORS   HAYAISHI O, NISHIZUKA Y, TATIBANA M, TAKESHITA M, KUNO S.
  TITLE     Enzymatic studies on the metabolism of beta-alanine.
  JOURNAL   J. Biol. Chem. 236 (1961) 781-90.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   2
  AUTHORS   Jakoby, W.B.
  TITLE     Aldehyde dehydrogenases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
REFERENCE   3
  AUTHORS   Yamada, E.W. and Jakoby, W.B.
  TITLE     Aldehyde oxidation. V. Direct conversion of malonic semialdehyde to
            acetyl-coenzyme A.
  JOURNAL   J. Biol. Chem. 235 (1960) 589-594.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00031  Inositol metabolism
            PATH: map00252  Alanine and aspartate metabolism
            PATH: map00410  beta-Alanine metabolism
            PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K00136  malonate-semialdehyde dehydrogenase (acetylating)
GENES       BME: BMEI0219
            BJA: blr2174(iolD)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.18
            ExPASy - ENZYME nomenclature database: 1.2.1.18
            ExplorEnz - The Enzyme Database: 1.2.1.18
            ERGO genome analysis and discovery system: 1.2.1.18
            BRENDA, the Enzyme Database: 1.2.1.18
            CAS: 9028-97-1
///
ENTRY       EC 1.2.1.19                 Enzyme
NAME        aminobutyraldehyde dehydrogenase;
            gamma-guanidinobutyraldehyde dehydrogenase (ambiguous);
            ABAL dehydrogenase;
            4-aminobutyraldehyde dehydrogenase;
            4-aminobutanal dehydrogenase;
            gamma-aminobutyraldehyde dehydroganase;
            1-pyrroline dehydrogenase;
            ABALDH;
            YdcW
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4-aminobutanal:NAD+ 1-oxidoreductase
REACTION    4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH + 2 H+
            [RN:R02549]
ALL_REAC    R02549
SUBSTRATE   4-aminobutanal [CPD:C00555];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     4-aminobutanoate [CPD:C00334];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The enzyme from some species exhibits broad substrate specificity
            and has a marked preference for straight-chain aldehydes (up to 7
            carbon atoms) as substrates [9]. The plant enzyme also acts on
            4-guanidinobutanal (cf. EC 1.2.1.54 gamma-guanidinobutyraldehyde
            dehydrogenase). As 1-pyrroline and 4-aminobutanal are in equilibrium
            and can be interconverted spontaneously, 1-pyrroline may act as the
            starting substrate. The enzyme forms part of the arginine-catabolism
            pathway [8] and belongs in the aldehyde dehydrogenase superfamily
            [9].
REFERENCE   1  [PMID:4817964]
  AUTHORS   Callewaert DM, Rosemblatt MS, Tchen TT.
  TITLE     Purification and properties of 4-aminobutanal dehydrogenase from a
            Pseudomonas species.
  JOURNAL   J. Biol. Chem. 249 (1974) 1737-41.
  ORGANISM  Pseudomonas sp.
REFERENCE   2
  AUTHORS   Jakoby, W.B.
  TITLE     Aldehyde dehydrogenases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
REFERENCE   3  [PMID:13673029]
  AUTHORS   JAKOBY WB, FREDERICKS J.
  TITLE     Pyrrolidine and putrescine metabolism: gamma-aminobutyraldehyde
            dehydrogenase.
  JOURNAL   J. Biol. Chem. 234 (1959) 2145-50.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   4  [PMID:16663901]
  AUTHORS   Matsuda H, Suzuki Y.
  TITLE     gamma-Guanidinobutyraldehyde Dehydrogenase of Vicia faba Leaves.
  JOURNAL   Plant. Physiol. 76 (1984) 654-657.
  ORGANISM  Vicia faba
REFERENCE   5
  AUTHORS   Yorifuji, T., Koike, K., Sakurai, T. and Yokoyama, K.
  TITLE     4-Aminobutyraldehyde and 4-guanidinobutyraldehyde dehydrogenases for
            arginine degradation in Pseudomonas putida.
  JOURNAL   Agric. Biol. Chem. 50 (1986) 2009-2016.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   6  [PMID:3510672]
  AUTHORS   Prieto-Santos MI, Martin-Checa J, Balana-Fouce R, Garrido-Pertierra
            A.
  TITLE     A pathway for putrescine catabolism in Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 880 (1986) 242-4.
REFERENCE   7  [PMID:3129020]
  AUTHORS   Prieto MI, Martin J, Balana-Fouce R, Garrido-Pertierra A.
  TITLE     Properties of gamma-aminobutyraldehyde dehydrogenase from
            Escherichia coli.
  JOURNAL   Biochimie. 69 (1987) 1161-8.
REFERENCE   8  [PMID:16023116]
  AUTHORS   Samsonova NN, Smirnov SV, Novikova AE, Ptitsyn LR.
  TITLE     Identification of Escherichia coli K12 YdcW protein as a
            gamma-aminobutyraldehyde dehydrogenase.
  JOURNAL   FEBS. Lett. 579 (2005) 4107-12.
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00410  beta-Alanine metabolism
ORTHOLOGY   KO: K00137  aminobutyraldehyde dehydrogenase
GENES       HSA: 223(ALDH9A1)
            RNO: 64040(Aldh9a1)
            PIC: PICST_41267(GPH2)
            ECO: b1444(ydcW)
            ECJ: JW1439(ydcW)
            ECE: Z2275
            ECS: ECs2048
            ECC: c1869(ydcW)
            ECI: UTI89_C1663(ydcW)
            ECP: ECP_1446
            ECV: APECO1_586(ydcW)
            ECW: EcE24377A_1510(puuC)
            ECX: EcHS_A1415
            STY: STY1467
            STT: t1506
            SPT: SPA1271(ydcW)
            SEC: SC1594(ydcW)
            STM: STM1597(ydcW)
            SFL: SF1774(ydcW)
            SFX: S1905
            SFV: SFV_1770
            SSN: SSON_1693
            SDY: SDY_1730
            ECA: ECA1542
            ENT: Ent638_2124
            KPN: KPN_01924(ydcW)
            BPM: BURPS1710b_0434
            RLE: pRL90166
            BME: BMEII0291
            PMB: A9601_14181
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.19
            ExPASy - ENZYME nomenclature database: 1.2.1.19
            ExplorEnz - The Enzyme Database: 1.2.1.19
            ERGO genome analysis and discovery system: 1.2.1.19
            BRENDA, the Enzyme Database: 1.2.1.19
            CAS: 9028-98-2
///
ENTRY       EC 1.2.1.20                 Enzyme
NAME        glutarate-semialdehyde dehydrogenase;
            glutarate semialdehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     glutarate-semialdehyde:NAD+ oxidoreductase
REACTION    glutarate semialdehyde + NAD+ + H2O = glutarate + NADH + 2 H+
            [RN:R02401]
ALL_REAC    R02401
SUBSTRATE   glutarate semialdehyde [CPD:C03273];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     glutarate [CPD:C00489];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Ichihara, A. and Ichihara, E.A.
  TITLE     Metabolism of L-lysine by bacterial enzymes. V. Glutaric
            semialdehyde dehydrogenase.
  JOURNAL   J. Biochem. (Tokyo) 49 (1961) 154-157.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.20
            ExPASy - ENZYME nomenclature database: 1.2.1.20
            ExplorEnz - The Enzyme Database: 1.2.1.20
            ERGO genome analysis and discovery system: 1.2.1.20
            BRENDA, the Enzyme Database: 1.2.1.20
            CAS: 9028-99-3
///
ENTRY       EC 1.2.1.21                 Enzyme
NAME        glycolaldehyde dehydrogenase;
            glycol aldehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     glycolaldehyde:NAD+ oxidoreductase
REACTION    glycolaldehyde + NAD+ + H2O = glycolate + NADH + 2 H+ [RN:R01333]
ALL_REAC    R01333
SUBSTRATE   glycolaldehyde [CPD:C00266];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     glycolate [CPD:C00160];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Davies, D.D.
  TITLE     The purification and properties of glycolaldehyde dehydrogenase.
  JOURNAL   J. Exp. Bot. 11 (1960) 289-295.
  ORGANISM  Pisum sativum
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K07248  glycolaldehyde dehydrogenase
GENES       ECO: b1415(aldA)
            ECJ: JW1412(aldA)
            ECE: Z2306(aldA)
            ECS: ECs2021
            ECC: c1842(aldA)
            ECI: UTI89_C1637(aldA) UTI89_C4480(fdoH)
            ECP: ECP_1420
            ECV: APECO1_566(aldA)
            ECW: EcE24377A_1596(aldA)
            ECX: EcHS_A1498
            YPA: YPA_3028
            SFL: SF1797(aldA)
            SFX: S1475(aldA)
            SFV: SFV_1791(aldA)
            SBO: SBO_1672(aldA) SBO_3907(fdoH)
            SDY: SDY_3850(fdoH)
            ECA: ECA0118(aldA)
            NME: NMB1968
            NMA: NMA0480(aldA)
            RME: Rmet_2760
            POL: Bpro_0938
            CJR: CJE0539(aldA)
            CFF: CFF8240_0070
            LCA: LSEI_2424
            OOE: OEOE_0324
STRUCTURES  PDB: 2HG2  2ILU  2IMP  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.21
            ExPASy - ENZYME nomenclature database: 1.2.1.21
            ExplorEnz - The Enzyme Database: 1.2.1.21
            ERGO genome analysis and discovery system: 1.2.1.21
            BRENDA, the Enzyme Database: 1.2.1.21
            CAS: 37250-89-8
///
ENTRY       EC 1.2.1.22                 Enzyme
NAME        lactaldehyde dehydrogenase;
            L-lactaldehyde:NAD+ oxidoreductase;
            nicotinamide adenine dinucleotide (NAD+)-linked dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-lactaldehyde:NAD+ oxidoreductase
REACTION    (S)-lactaldehyde + NAD+ + H2O = (S)-lactate + NADH + 2 H+
            [RN:R01446]
ALL_REAC    R01446;
            (other) R00203
SUBSTRATE   (S)-lactaldehyde [CPD:C00424];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     (S)-lactate [CPD:C00186];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:5821022]
  AUTHORS   Rembold H, Simmersbach F.
  TITLE     Catabolism of pteridine cofactors. II. A specific pterin deaminase
            in rat liver.
  JOURNAL   Biochim. Biophys. Acta. 184 (1969) 589-96.
REFERENCE   2  [PMID:4310089]
  AUTHORS   Sridhara S, Wu TT.
  TITLE     Purification and properties of lactaldehyde dehydrogenase from
            Escherichia coli.
  JOURNAL   J. Biol. Chem. 244 (1969) 5233-8.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K00138  lactaldehyde dehydrogenase
GENES       ECO: b1415(aldA) b3588(aldB)
            ECJ: JW1412(aldA) JW3561(aldB)
            ECE: Z2306(aldA) Z5008(aldB)
            ECS: ECs2021 ECs4464
            ECC: c1842(aldA) c4408(aldB)
            ECI: UTI89_C1637(aldA) UTI89_C4129(aldB)
            ECP: ECP_1420
            ECV: APECO1_2866(aldB) APECO1_566(aldA)
            ECW: EcE24377A_1596(aldA)
            ECX: EcHS_A1498
            STY: STY4116(aldB)
            STT: t3839(aldB)
            SPT: SPA3531(aldB)
            SEC: SC3604(aldB)
            STM: STM3680(aldB)
            SFL: SF1797(aldA) SF3626(aldB)
            SFX: S1475(aldA) S4142(aldB)
            SFV: SFV_1791(aldA) SFV_3945(aldB)
            SBO: SBO_1672(aldA) SBO_3588(aldB)
            ECA: ECA0094(aldB) ECA0118(aldA)
            ENT: Ent638_0143 Ent638_1953
            NME: NMB1968
            NMA: NMA0480(aldA)
            NMC: NMC1942(aldA)
            REH: H16_A1919
            BXE: Bxe_B1123 Bxe_C1106
            VEI: Veis_4949
            MPT: Mpe_A0361
            MFA: Mfla_1995
            CJR: CJE0539(aldA)
            CJD: JJD26997_1445(aldA)
            CFF: CFF8240_0070
            BME: BMEII0140
            CCR: CC_3580
            SUS: Acid_0037
            LCA: LSEI_2424
            OOE: OEOE_0324
            MSY: MS53_0078(aldA)
            SCO: SCO3486(SCE65.22)
            FNU: FN0454
            ANA: all5022
            TAC: Ta0809
            TVO: TVN1021
STRUCTURES  PDB: 2HG2  2ILU  2IMP  2OPX  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.22
            ExPASy - ENZYME nomenclature database: 1.2.1.22
            ExplorEnz - The Enzyme Database: 1.2.1.22
            ERGO genome analysis and discovery system: 1.2.1.22
            BRENDA, the Enzyme Database: 1.2.1.22
            CAS: 37250-90-1
///
ENTRY       EC 1.2.1.23                 Enzyme
NAME        2-oxoaldehyde dehydrogenase (NAD+);
            alpha-ketoaldehyde dehydrogenase;
            methylglyoxal dehydrogenase;
            NAD+-linked alpha-ketoaldehyde dehydrogenase;
            2-ketoaldehyde dehydrogenase;
            NAD+-dependent alpha-ketoaldehyde dehydrogenase;
            2-oxoaldehyde dehydrogenase (NAD+)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-oxoaldehyde:NAD+ 2-oxidoreductase
REACTION    a 2-oxoaldehyde + NAD+ + H2O = a 2-oxo acid + NADH + H+ [RN:R01337]
ALL_REAC    R01337 > R00203;
            (other) R01735
SUBSTRATE   2-oxoaldehyde [CPD:C00538];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     2-oxo acid [CPD:C00161];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Not identical with EC 1.2.1.49 2-oxoaldehyde dehydrogenase (NADP+).
REFERENCE   1  [PMID:4383524]
  AUTHORS   Monder C.
  TITLE     Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the
            enzymic oxidation of methylglyoxal to pyruvate.
  JOURNAL   J. Biol. Chem. 242 (1967) 4603-9.
  ORGANISM  sheep
REFERENCE   2  [PMID:7107626]
  AUTHORS   Ray M, Ray S.
  TITLE     On the interaction of nucleotides and glycolytic intermediates with
            NAD-linked alpha-ketoaldehyde dehydrogenase.
  JOURNAL   J. Biol. Chem. 257 (1982) 10571-4.
  ORGANISM  goat
REFERENCE   3  [PMID:7107625]
  AUTHORS   Ray S, Ray M.
  TITLE     Purification and characterization of NAD and NADP-linked
            alpha-ketoaldehyde dehydrogenases involved in catalyzing the
            oxidation of methylglyoxal to pyruvate.
  JOURNAL   J. Biol. Chem. 257 (1982) 10566-70.
  ORGANISM  goat
PATHWAY     PATH: map00620  Pyruvate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.23
            ExPASy - ENZYME nomenclature database: 1.2.1.23
            ExplorEnz - The Enzyme Database: 1.2.1.23
            ERGO genome analysis and discovery system: 1.2.1.23
            BRENDA, the Enzyme Database: 1.2.1.23
            CAS: 37250-91-2
///
ENTRY       EC 1.2.1.24                 Enzyme
NAME        succinate-semialdehyde dehydrogenase;
            succinate semialdehyde dehydrogenase;
            succinic semialdehyde dehydrogenase;
            succinyl semialdehyde dehydrogenase;
            succinate semialdehyde:NAD+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     succinate-semialdehyde:NAD+ oxidoreductase
REACTION    succinate semialdehyde + NAD+ + H2O = succinate + NADH + 2 H+
            [RN:R00713]
ALL_REAC    R00713
SUBSTRATE   succinate semialdehyde [CPD:C00232];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     succinate [CPD:C00042];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13860092]
  AUTHORS   ALBERS RW, KOVAL GJ.
  TITLE     Succinic semialdehyde dehydrogenase: purification and properties of
            the enzyme from monkey brain.
  JOURNAL   Biochim. Biophys. Acta. 52 (1961) 29-35.
  ORGANISM  monkey
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K00139  succinate-semialdehyde dehydrogenase
GENES       HSA: 7915(ALDH5A1)
            MMU: 214579(Aldh5a1)
            RNO: 291133(Aldh5a1)
            CFA: 488246(ALDH5A1)
            GGA: 420818(ALDH5A1)
            SPU: 584281(LOC584281)
            DME: Dmel_CG4685
            CEL: F45H10.1(alh-7)
            PIC: PICST_40468(UGA2)
            AFM: AFUA_3G07150 AFUA_4G08170
            SFL: SF1480
            BAY: RBAM_004160(gabD)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.24
            ExPASy - ENZYME nomenclature database: 1.2.1.24
            ExplorEnz - The Enzyme Database: 1.2.1.24
            ERGO genome analysis and discovery system: 1.2.1.24
            BRENDA, the Enzyme Database: 1.2.1.24
            CAS: 9028-95-9
///
ENTRY       EC 1.2.1.25                 Enzyme
NAME        2-oxoisovalerate dehydrogenase (acylating);
            2-oxoisovalerate dehydrogenase;
            alpha-ketoisovalerate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-methyl-2-oxobutanoate:NAD+ 2-oxidoreductase
            (CoA-methyl-propanoylating)
REACTION    3-methyl-2-oxobutanoate + CoA + NAD+ = 2-methylpropanoyl-CoA + CO2 +
            NADH [RN:R01210]
ALL_REAC    R01210;
            (other) R01651 R03171
SUBSTRATE   3-methyl-2-oxobutanoate [CPD:C00141];
            CoA [CPD:C00010];
            NAD+ [CPD:C00003]
PRODUCT     2-methylpropanoyl-CoA [CPD:C00630];
            CO2 [CPD:C00011];
            NADH [CPD:C00004]
COMMENT     Also acts on (S)-3-methyl-2-oxopentanoate and
            4-methyl-2-oxopentanoate.
REFERENCE   1  [PMID:4308861]
  AUTHORS   Namba Y, Yoshizawa K, Ejima A, Hayashi T, Kaneda T.
  TITLE     Coenzyme A- and nicotinamide adenine dinucleotide-dependent branched
            chain alpha-keto acid dehydrogenase. I. Purification and properties
            of the enzyme from Bacillus subtilis.
  JOURNAL   J. Biol. Chem. 244 (1969) 4437-47.
  ORGANISM  Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.25
            ExPASy - ENZYME nomenclature database: 1.2.1.25
            ExplorEnz - The Enzyme Database: 1.2.1.25
            ERGO genome analysis and discovery system: 1.2.1.25
            BRENDA, the Enzyme Database: 1.2.1.25
            CAS: 37211-61-3
///
ENTRY       EC 1.2.1.26                 Enzyme
NAME        2,5-dioxovalerate dehydrogenase;
            2-oxoglutarate semialdehyde dehydrogenase;
            alpha-ketoglutaric semialdehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2,5-dioxopentanoate:NADP+ 5-oxidoreductase
REACTION    2,5-dioxopentanoate + NADP+ + H2O = 2-oxoglutarate + NADPH + 2 H+
            [RN:R00264]
ALL_REAC    R00264
SUBSTRATE   2,5-dioxopentanoate [CPD:C00433];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     2-oxoglutarate [CPD:C00026];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Adams, E. and Rosso, G.
  TITLE     alpha-Ketoglutaric semialdehyde dehydrogenase of Pseudomonas.
            Properties of the purified enzyme induced by hydroxyproline and of
            the glucarate-induced and constitutive enzymes.
  JOURNAL   J. Biol. Chem. 242 (1967) 1803-1814.
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
GENES       REH: H16_B0130
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.26
            ExPASy - ENZYME nomenclature database: 1.2.1.26
            ExplorEnz - The Enzyme Database: 1.2.1.26
            ERGO genome analysis and discovery system: 1.2.1.26
            BRENDA, the Enzyme Database: 1.2.1.26
            CAS: 37250-92-3
///
ENTRY       EC 1.2.1.27                 Enzyme
NAME        methylmalonate-semialdehyde dehydrogenase (acylating);
            MSDH;
            MMSA dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-methyl-3-oxopropanoate:NAD+ 3-oxidoreductase (CoA-propanoylating)
REACTION    2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3-
            + NADH [RN:R00922]
ALL_REAC    R00922 > R00935;
            (other) R00705
SUBSTRATE   2-methyl-3-oxopropanoate [CPD:C00349];
            CoA [CPD:C00010];
            H2O [CPD:C00001];
            NAD+ [CPD:C00003]
PRODUCT     propanoyl-CoA [CPD:C00100];
            HCO3- [CPD:C00288];
            NADH [CPD:C00004]
COMMENT     Also converts 3-oxopropanoate into acetyl-CoA [3]. The reaction
            occurs in two steps with the decarboxylation process preceding
            CoA-binding [3]. Bicarbonate rather than CO2 is released as a final
            product [3].
REFERENCE   1  [PMID:4297649]
  AUTHORS   Sokatch JR, Sanders LE, Marshall VP.
  TITLE     Oxidation of methylmalonate semialdehyde to propionyl coenzyme A in
            Pseudomonas aeruginosa grown on valine.
  JOURNAL   J. Biol. Chem. 243 (1968) 2500-6.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   2  [PMID:15272169]
  AUTHORS   Dubourg H, Stines-Chaumeil C, Didierjean C, Talfournier F,
            Rahuel-Clermont S, Branlant G, Aubry A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 60 (2004) 1435-7.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   3  [PMID:16332250]
  AUTHORS   Stines-Chaumeil C, Talfournier F, Branlant G.
  TITLE     Mechanistic characterization of the MSDH (methylmalonate
            semialdehyde dehydrogenase) from Bacillus subtilis.
  JOURNAL   Biochem. J. 395 (2006) 107-15.
  ORGANISM  Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00031  Inositol metabolism
            PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K00140  methylmalonate-semialdehyde dehydrogenase
GENES       HSA: 4329(ALDH6A1)
            PTR: 467506(ALDH6A1)
            MMU: 104776(Aldh6a1)
            RNO: 81708(Aldh6a1)
            CFA: 490779(ALDH6A1)
            BTA: 327692(ALDH6A1)
            GGA: 423345(ALDH6A1)
            DRE: 436647(zgc:92082)
            SPU: 578337(LOC578337)
            DME: Dmel_CG17896
            CEL: F13D12.4(alh-8)
            ATH: AT2G14170(ALDH6B2)
            OSA: 4342610
            PIC: PICST_80168(ALD6)
            ANI: AN3591.2
            AFM: AFUA_4G12870
            AOR: AO090009000314
            CNE: CND02030 CNI01990
            UMA: UM00214.1
            DDI: DDB_0231483
            TET: TTHERM_00299840
            STM: STM4421
            YPE: YPO2577
            YPK: y1146
            YPM: YP_1137(putA1)
            YPA: YPA_2524
            YPN: YPN_1061
            YPS: YPTB1071
            YPI: YpsIP31758_2977(mmsA)
            ECA: ECA1456
            PLU: plu1806
            XCC: XCC1260(mmsA)
            XCB: XC_2981
            XCV: XCV1363
            XAC: XAC1312(mmsA)
            XOO: XOO1842(mmsA)
            XOM: XOO_1738(XOO1738)
            VVU: VV2_0493
            VVY: VVA1042
            VPA: VPA0621 VPA1122
            PPR: PBPRB0478 PBPRB1111
            PAE: PA0130 PA0747 PA3570(mmsA)
            PAU: PA14_01600(mmsA) PA14_18120(mmsA) PA14_54620
            PAP: PSPA7_0206(mmsA3) PSPA7_1574(mmsA) PSPA7_4773(mmsA1)
            PPU: PP_0597(mmsA-1) PP_4667(mmsA-2)
            PST: PSPTO_0775(mmsA-1) PSPTO_0782(mmsA-2) PSPTO_3497(mmsA-3)
            PSB: Psyr_0679 Psyr_0689 Psyr_3271
            PSP: PSPPH_3191(mmsA1) PSPPH_4618(mmsA2)
            PFL: PFL_0734(mmsA) PFL_0747(mmsA)
            PFO: Pfl_0686 Pfl_0695
            PEN: PSEEN0682(mmsA-1) PSEEN0699(mmsA-2)
            PAR: Psyc_0900(mmsA)
            PCR: Pcryo_1517
            ACI: ACIAD1604(mmsA)
            SON: SO_1678(mmsA)
            SDN: Sden_1942
            SFR: Sfri_1339 Sfri_3023
            SHE: Shewmr4_2596 Shewmr4_2928
            SHM: Shewmr7_2663 Shewmr7_3010
            SHN: Shewana3_2770 Shewana3_3107
            ILO: IL0870(mmsA)
            CPS: CPS_0098(mmsA1) CPS_1432(mmsA2) CPS_3423(mmsA3)
                 CPS_4060(mmsA4)
            PHA: PSHAa1455
            PAT: Patl_0948
            CBU: CBU_0927(mmsA)
            CBD: COXBU7E912_1147(mmsA)
            LPN: lpg0129(mmsA)
            LPF: lpl0128
            LPP: lpp0143
            HCH: HCH_00642(mmsA1) HCH_01157(mmsA2)
            CSA: Csal_1126 Csal_2380
            ABO: ABO_0020(mmsA)
            AHA: AHA_0246(mmsA-1) AHA_2079(mmsA-2)
            CVI: CV_1437(mmsA2) CV_2085(mmsA1)
            RSO: RS02392(RSp1055) RSp0650(mmsA)
            REU: Reut_A0249 Reut_B4258 Reut_B5828 Reut_C5960
            REH: H16_A0273(mmsA1) H16_A3664(mmsA2) H16_B1191(mmsA3)
            RME: Rmet_0206
            BMA: BMA2931(mmsA-1) BMAA1379(mmsA-2)
            BMV: BMASAVP1_0493(mmsA-2) BMASAVP1_A3379(mmsA)
            BML: BMA10299_0157(mmsA-2) BMA10299_A1611(mmsA)
            BMN: BMA10247_2990(mmsA) BMA10247_A1453(mmsA-2)
            BXE: Bxe_A0015 Bxe_A3576 Bxe_B1086 Bxe_B2023 Bxe_C0244
            BUR: Bcep18194_A4576 Bcep18194_B0716 Bcep18194_B1697
                 Bcep18194_B2033
            BCN: Bcen_0950 Bcen_3406 Bcen_4052 Bcen_4319
            BCH: Bcen2424_1432 Bcen2424_4047 Bcen2424_4314 Bcen2424_4961
            BAM: Bamb_1312 Bamb_3442 Bamb_4383
            BPS: BPSL3420(msdA) BPSS0619(mmsA) BPSS0743
            BPM: BURPS1710b_0202(mmsA) BURPS1710b_A2180(mmsA)
                 BURPS1710b_A2319(mmsA)
            BPL: BURPS1106A_4070(mmsA) BURPS1106A_A0828(mmsA)
                 BURPS1106A_A1010(mmsA)
            BPD: BURPS668_3996(mmsA) BURPS668_A0920(mmsA) BURPS668_A1097(mmsA)
            BTE: BTH_I3333(mmsA-1) BTH_II1657(mmsA-2) BTH_II1801(mmsA-3)
            BPE: BP1615 BP2417 BP3158(mmsA)
            BPA: BPP0783(mmsA) BPP2970 BPP3281
            BBR: BB0868(mmsA) BB2936 BB3732
            RFR: Rfer_0372
            POL: Bpro_4547
            AAV: Aave_4746
            AJS: Ajs_4104
            VEI: Veis_4438
            HAR: HEAR3421(mmsA)
            MMS: mma_3642
            PCA: Pcar_2505
            BBA: Bd1534(mmsA)
            DPS: DP1915
            ADE: Adeh_2245
            MXA: MXAN_0121(mmsA)
            PUB: SAR11_0241(mmsA)
            MLO: mll3987
            MES: Meso_3319
            SME: SMc00781(iolA)
            ATU: Atu0205(mmsA)
            ATC: AGR_C_351
            RET: RHE_CH00731(iolA)
            BME: BMEI0219
            BMF: BAB1_1840(mmsA)
            BMS: BR1832(mmsA)
            BMB: BruAb1_1811(mmsA)
            BOV: BOV_1765(mmsA)
            BJA: blr3954
            BRA: BRADO3137
            BBT: BBta_3578
            RPA: RPA3450
            RPB: RPB_2117
            RPC: RPC_3095
            RPD: RPD_3302
            RPE: RPE_2382
            NWI: Nwi_2159
            NHA: Nham_2559
            CCR: CC_1302 CC_2274
            SIL: SPO2203(mmsA)
            SIT: TM1040_1106
            RSP: RSP_2962
            JAN: Jann_1913
            RDE: RD1_2990(mmsA)
            MMR: Mmar10_2838
            HNE: HNE_1828(mmsA1) HNE_2176(mmsA2)
            NAR: Saro_0855
            SAL: Sala_3049
            ELI: ELI_09995
            RRU: Rru_A1542 Rru_A2071
            ABA: Acid345_1533
            BSU: BG11117(iolA)
            BHA: BH2312
            BAN: BA2354(mmsA-1) BA2513(mmsA-2)
            BAR: GBAA2354(mmsA-1) GBAA2513(mmsA-2)
            BAA: BA_2848 BA_3004
            BAT: BAS2193 BAS2334
            BCE: BC2290
            BCA: BCE_2382(mmsA)
            BCZ: BCZK2116(mmsA) BCZK2253(iolA) pE33L466_0301(iolA)
            BTK: BT9727_2130(mmsA) BT9727_2297(iolA)
            BLI: BL00246(iolA) BL00293(iolAB)
            BLD: BLi02104(mmsA) BLi04251
            BCL: ABC0422(iolA) ABC1809
            BAY: RBAM_036780
            BPU: BPUM_1749
            OIH: OB0816 OB2736
            GKA: GK1426 GK1887(iolA) GK1951
            LMO: lmo0383
            LMF: LMOf2365_0395(mmsA)
            LIN: lin0401
            MHY: mhp153(mmsA)
            MHJ: MHJ_0219
            MHP: MHP7448_0225
            MTU: Rv0753c(mmsA)
            MTC: MT0777(mmsA)
            MBO: Mb0775c(mmsA)
            MBB: BCG_0804c(mmsA)
            MPA: MAP4215c(mmsA)
            MAV: MAV_2521(mmsA) MAV_4417(mmsA)
            MSM: MSMEG_1498(mmsA) MSMEG_2449(mmsA)
            MMC: Mmcs_0348 Mmcs_1064
            CGL: NCgl0157(cgl0160) NCgl0521(cgl0544)
            CGB: cg0199(msmA) cg0635
            NFA: nfa10370
            RHA: RHA1_ro01357(mmsA1) RHA1_ro01542(mmsA2) RHA1_ro04468(mmsA3)
                 RHA1_ro10225
            SCO: SCO2726(msdA)
            SMA: SAV5342(iolA)
            AAU: AAur_0499(mmsA) AAur_1941(mmsA) AAur_1980(mmsA)
            PAC: PPA0461
            TFU: Tfu_0687
            FAL: FRAAL1417(mmsA)
            SEN: SACE_1456(mmsA2) SACE_4672(mmsA1) SACE_5185(mmsA3)
            RXY: Rxyl_1716
            SSO: SSO1218
            STO: ST1116
            PAS: Pars_0509
STRUCTURES  PDB: 1T90  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.27
            ExPASy - ENZYME nomenclature database: 1.2.1.27
            ExplorEnz - The Enzyme Database: 1.2.1.27
            ERGO genome analysis and discovery system: 1.2.1.27
            BRENDA, the Enzyme Database: 1.2.1.27
            CAS: 37205-49-5
///
ENTRY       EC 1.2.1.28                 Enzyme
NAME        benzaldehyde dehydrogenase (NAD+);
            benzaldehyde (NAD+) dehydrogenase;
            benzaldehyde dehydrogenase (NAD+)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     benzaldehyde:NAD+ oxidoreductase
REACTION    benzaldehyde + NAD+ + H2O = benzoate + NADH + 2 H+ [RN:R01419]
ALL_REAC    R01419;
            (other) R01293 R07667
SUBSTRATE   benzaldehyde [CPD:C00261];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     benzoate [CPD:C00180];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13108854]
  AUTHORS   GUNSALUS CF, STANIER RY, GUNSALUS IC.
  TITLE     The enzymatic conversion of mandelic acid to benzoic acid. III.
            Fractionation and properties of the soluble enzymes.
  JOURNAL   J. Bacteriol. 66 (1953) 548-53.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00622  Toluene and xylene degradation
ORTHOLOGY   KO: K00141  benzaldehyde dehydrogenase (NAD)
GENES       PIC: PICST_60847(ALD3)
            XCC: XCC0354(xylC)
            XCB: XC_0366
            XCV: XCV0367
            XAC: XAC0354(xylC)
            PST: PSPTO_2950(xylcC)
            PSB: Psyr_2734
            PSP: PSPPH_2427(xylC)
            PFO: Pfl_2977
            ACI: ACIAD1430(areC) ACIAD1725(hcaB)
            RSO: RS05194(RSp0229)
            REH: H16_A1772
            BXE: Bxe_C0302
            BUR: Bcep18194_A4913
            BCN: Bcen_1311
            BCH: Bcen2424_6518
            BAM: Bamb_5579
            BPM: BURPS1710b_1049(vdh) BURPS1710b_A2362(vdh)
            POL: Bpro_0128 Bpro_4519
            EBA: ebA5642(ald)
            AZO: azo2473(xylC)
            BBT: BBta_6645(xylC)
            CCR: CC_2397
            MSM: MSMEG_4165
            CGB: cg2953(xylC)
            RHA: RHA1_ro02797(mdlD) RHA1_ro02986
            SCO: SCO7436(SC6D11.32c)
            SEN: SACE_3144(mdlD)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.28
            ExPASy - ENZYME nomenclature database: 1.2.1.28
            ExplorEnz - The Enzyme Database: 1.2.1.28
            ERGO genome analysis and discovery system: 1.2.1.28
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.28
            BRENDA, the Enzyme Database: 1.2.1.28
            CAS: 37250-93-4
///
ENTRY       EC 1.2.1.29                 Enzyme
NAME        aryl-aldehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     aryl-aldehyde:NAD+ oxidoreductase
REACTION    an aromatic aldehyde + NAD+ + H2O = an aromatic acid + NADH + H+
            [RN:R01486]
ALL_REAC    R01486 > R02655 R02695 R03300 R05235;
            (other) R02657
SUBSTRATE   aromatic aldehyde [CPD:C00193];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     aromatic acid [CPD:C00539];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Oxidizes a number of aromatic aldehydes, but not aliphatic
            aldehydes.
REFERENCE   1  [PMID:4289834]
  AUTHORS   Raison JK, Henson G, Rienits KG.
  TITLE     The oxidation of gentisaldehyde by nicotinamide-adenine
            dinucleotide-specific, aromatic aldehyde dehydrogenase from rabbit
            liver.
  JOURNAL   Biochim. Biophys. Acta. 118 (1966) 285-98.
  ORGANISM  rabbit
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00621  Biphenyl degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.29
            ExPASy - ENZYME nomenclature database: 1.2.1.29
            ExplorEnz - The Enzyme Database: 1.2.1.29
            ERGO genome analysis and discovery system: 1.2.1.29
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.29
            BRENDA, the Enzyme Database: 1.2.1.29
            CAS: 37250-94-5
///
ENTRY       EC 1.2.1.30                 Enzyme
NAME        aryl-aldehyde dehydrogenase (NADP+);
            aromatic acid reductase;
            aryl-aldehyde dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     aryl-aldehyde:NADP+ oxidoreductase (ATP-forming)
REACTION    an aromatic aldehyde + NADP+ + AMP + diphosphate + H2O = an aromatic
            acid + NADPH + H+ + ATP [RN:R01490]
ALL_REAC    R01490
SUBSTRATE   aromatic aldehyde [CPD:C00193];
            NADP+ [CPD:C00006];
            AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            H2O [CPD:C00001]
PRODUCT     aromatic acid [CPD:C00539];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            ATP [CPD:C00002]
REFERENCE   1  [PMID:4405494]
  AUTHORS   Gross GG.
  TITLE     Formation and reduction of intermediate acyladenylate by
            aryl-aldehyde. NADP oxidoreductase from Neurospora crassa.
  JOURNAL   Eur. J. Biochem. 31 (1972) 585-92.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2  [PMID:4389863]
  AUTHORS   Gross GG, Zenk MH.
  TITLE     [Reduction of aromatic acids to aldehydes and alcohols in the
            cell-free system. 1. Purification and properties of aryl-aldehyde:
            NADP-oxidoreductase from Neurospora crassa]
  JOURNAL   Eur. J. Biochem. 8 (1969) 413-9.
  ORGANISM  Neurospora crassa [GN:dncr]
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.30
            ExPASy - ENZYME nomenclature database: 1.2.1.30
            ExplorEnz - The Enzyme Database: 1.2.1.30
            ERGO genome analysis and discovery system: 1.2.1.30
            BRENDA, the Enzyme Database: 1.2.1.30
            CAS: 9074-94-6
///
ENTRY       EC 1.2.1.31                 Enzyme
NAME        L-aminoadipate-semialdehyde dehydrogenase;
            aminoadipate semialdehyde dehydrogenase;
            2-aminoadipate semialdehyde dehydrogenase;
            alpha-aminoadipate-semialdehyde dehydrogenase;
            alpha-aminoadipate reductase;
            2-aminoadipic semialdehyde dehydrogenase;
            L-alpha-aminoadipate delta-semialdehyde oxidoreductase;
            L-alpha-aminoadipate delta-semialdehyde:NAD+ oxidoreductase;
            L-alpha-aminoadipate delta-semialdehyde:nicotinamide adenine
            dinucleotide oxidoreductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-2-aminoadipate-6-semialdehyde:NAD(P)+ 6-oxidoreductase
REACTION    L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate +
            NAD(P)H + H+ [RN:R03102 R03103]
ALL_REAC    R03102 R03103;
            (other) R03098 R04390 R04863
SUBSTRATE   L-2-aminoadipate 6-semialdehyde [CPD:C04076];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     L-2-aminoadipate [CPD:C00956];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4285660]
  AUTHORS   Calvert AF, Rodwell VW.
  TITLE     Metabolism of pipecolic acid in a Pseudomonas species. 3.
            L-alpha-aminoadipate delta-semialdehyde:nicotinamide adenine
            dinucleotide oxidoreductase.
  JOURNAL   J. Biol. Chem. 241 (1966) 409-14.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00300  Lysine biosynthesis
            PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K00142  aminoadipate-semialdehyde dehydrogenase
            KO: K00143  aminoadipate-semialdehyde dehydrogenase large subunit
            KO: K00144  aminoadipate-semialdehyde dehydrogenase small subunit
GENES       HSA: 60496(AASDHPPT)
            MMU: 231326(A230062G08Rik)
            SCE: YBR115C(LYS2) YGL154C(LYS5)
            AGO: AGOS_ADL346W AGOS_AGR382W
            PIC: PICST_68020(LYS2)
            CAL: CaO19_2970(CaO19.2970)
            CGR: CAGL0E05104g CAGL0K07788g
            SPO: SPAP7G5.04c(lys1)
            ANI: AN5610.2
            AFM: AFUA_4G11240
            AOR: AO090003001097
            CNE: CNG00170
            BPM: BURPS1710b_2274
            BBT: BBta_1087 BBta_3701 BBta_4110
            AVA: Ava_2595
STRUCTURES  PDB: 2BYD  2C43  2CG5  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.31
            ExPASy - ENZYME nomenclature database: 1.2.1.31
            ExplorEnz - The Enzyme Database: 1.2.1.31
            ERGO genome analysis and discovery system: 1.2.1.31
            BRENDA, the Enzyme Database: 1.2.1.31
            CAS: 9067-87-2
///
ENTRY       EC 1.2.1.32                 Enzyme
NAME        aminomuconate-semialdehyde dehydrogenase;
            2-aminomuconate semialdehyde dehydrogenase;
            2-hydroxymuconic acid semialdehyde dehydrogenase;
            2-hydroxymuconate semialdehyde dehydrogenase;
            alpha-aminomuconic epsilon-semialdehyde dehydrogenase;
            alpha-hydroxymuconic epsilon-semialdehyde dehydrogenase;
            2-hydroxymuconic semialdehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-aminomuconate-6-semialdehyde:NAD+ 6-oxidoreductase
REACTION    2-aminomuconate 6-semialdehyde + NAD+ + H2O = 2-aminomuconate + NADH
            + 2 H+ [RN:R03889]
ALL_REAC    R03889;
            (other) R02762 R05353
SUBSTRATE   2-aminomuconate 6-semialdehyde [CPD:C03824];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     2-aminomuconate [CPD:C02220];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts on 2-hydroxymuconate semialdehyde.
REFERENCE   1  [PMID:14275130]
  AUTHORS   ICHIYAMA A, NAKAMURA S, KAWAI H, HONJO T, NISHIZUKA Y, HAYAISHI O,
            SENOH S.
  TITLE     STUDIES ON THE METABOLISM OF THE BENZENE RING OF TRYPTOPHAN IN
            MAMMALIAN TISSUES. II. ENZYMIC FORMATION OF ALPHA-AMINOMUCONIC ACID
            FROM 3-HYDROXYANTHRANILIC ACID.
  JOURNAL   J. Biol. Chem. 240 (1965) 740-9.
  ORGANISM  cat
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00380  Tryptophan metabolism
            PATH: map00622  Toluene and xylene degradation
ORTHOLOGY   KO: K10217  aminomuconate-semialdehyde dehydrogenase
GENES       REH: H16_B0547
            RHA: RHA1_ro03868
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.32
            ExPASy - ENZYME nomenclature database: 1.2.1.32
            ExplorEnz - The Enzyme Database: 1.2.1.32
            ERGO genome analysis and discovery system: 1.2.1.32
            BRENDA, the Enzyme Database: 1.2.1.32
            CAS: 37250-95-6
///
ENTRY       EC 1.2.1.33                 Enzyme
NAME        (R)-dehydropantoate dehydrogenase;
            D-aldopantoate dehydrogenase;
            D-2-hydroxy-3,3-dimethyl-3-formylpropionate:diphosphopyridine
            nucleotide (DPN+) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-4-dehydropantoate:NAD+ 4-oxidoreductase
REACTION    (R)-4-dehydropantoate + NAD+ + H2O = (R)-3,3-dimethylmalate + NADH +
            2 H+ [RN:R03198]
ALL_REAC    R03198
SUBSTRATE   (R)-4-dehydropantoate [CPD:C01053];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     (R)-3,3-dimethylmalate [CPD:C01088];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4287371]
  AUTHORS   Magee PT, Snell EE.
  TITLE     The bacterial degradation of pantothenic acid. IV. Enzymatic
            conversion of aldopantoate to alpha-ketoisovalerate.
  JOURNAL   Biochemistry. 5 (1966) 409-16.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00770  Pantothenate and CoA biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.33
            ExPASy - ENZYME nomenclature database: 1.2.1.33
            ExplorEnz - The Enzyme Database: 1.2.1.33
            ERGO genome analysis and discovery system: 1.2.1.33
            BRENDA, the Enzyme Database: 1.2.1.33
            CAS: 37250-96-7
///
ENTRY       EC 1.2.1.34       Obsolete  Enzyme
NAME        Transferred to 1.1.1.131
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Transferred entry: now EC 1.1.1.131 mannuronate reductase (EC
            1.2.1.34 created 1972, deleted 1983 [transferred to EC 1.1.1.180,
            deleted 1984])
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.34
            ExPASy - ENZYME nomenclature database: 1.2.1.34
            ExplorEnz - The Enzyme Database: 1.2.1.34
            ERGO genome analysis and discovery system: 1.2.1.34
            BRENDA, the Enzyme Database: 1.2.1.34
///
ENTRY       EC 1.2.1.35       Obsolete  Enzyme
NAME        Transferred to 1.1.1.203
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Transferred entry: now EC 1.1.1.203 uronate dehydrogenase (EC
            1.2.1.35 created 1972, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.35
            ExPASy - ENZYME nomenclature database: 1.2.1.35
            ExplorEnz - The Enzyme Database: 1.2.1.35
            ERGO genome analysis and discovery system: 1.2.1.35
            BRENDA, the Enzyme Database: 1.2.1.35
///
ENTRY       EC 1.2.1.36                 Enzyme
NAME        retinal dehydrogenase;
            cytosolic retinal dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     retinal:NAD+ oxidoreductase
REACTION    retinal + NAD+ + H2O = retinoate + NADH + 2 H+ [RN:R02123]
ALL_REAC    R02123
SUBSTRATE   retinal [CPD:C00376];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     retinoate [CPD:C00777];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016];
            Metal [CPD:C00050]
COMMENT     A metalloflavoprotein (FAD). Acts on both the 11-trans- and
            13-cis-forms of retinal.
REFERENCE   1  [PMID:4312676]
  AUTHORS   Moffa DJ, Lotspeich FJ, Krause RF.
  TITLE     Preparation and properties of retinal-oxidizing enzyme from rat
            intestinal mucosa.
  JOURNAL   J. Biol. Chem. 245 (1970) 439-47.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00830  Retinol metabolism
ORTHOLOGY   KO: K07249  retinal dehydrogenase
GENES       HSA: 216(ALDH1A1) 8854(ALDH1A2)
            PTR: 464529(ALDH1A1)
            MMU: 11668(Aldh1a1) 19378(Aldh1a2) 26358(Aldh1a7)
            RNO: 116676(Aldh1a2) 24188(Aldh1a1)
            CFA: 476323(ALDH1A1) 478319(ALDH1A2)
            GGA: 395264(ALDH1A1) 395844(ALDH1A2)
            XLA: 394296(aldh1-A) 397728(LOC397728)
            DRE: 116713(aldh1a2)
            DDI: DDB_0201650(hydA)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.36
            ExPASy - ENZYME nomenclature database: 1.2.1.36
            ExplorEnz - The Enzyme Database: 1.2.1.36
            ERGO genome analysis and discovery system: 1.2.1.36
            BRENDA, the Enzyme Database: 1.2.1.36
            CAS: 37250-99-0
///
ENTRY       EC 1.2.1.37       Obsolete  Enzyme
NAME        Transferred to 1.17.1.4
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Transferred entry: now EC 1.17.1.4, xanthine dehydrogenase (EC
            1.2.1.37 created 1972, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.37
            ExPASy - ENZYME nomenclature database: 1.2.1.37
            ExplorEnz - The Enzyme Database: 1.2.1.37
            ERGO genome analysis and discovery system: 1.2.1.37
            BRENDA, the Enzyme Database: 1.2.1.37
///
ENTRY       EC 1.2.1.38                 Enzyme
NAME        N-acetyl-gamma-glutamyl-phosphate reductase;
            reductase, acetyl-gamma-glutamyl phosphate;
            N-acetylglutamate 5-semialdehyde dehydrogenase;
            N-acetylglutamic gamma-semialdehyde dehydrogenase;
            N-acetyl-L-glutamate gamma-semialdehyde:NADP+ oxidoreductase
            (phosphorylating)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N-acetyl-L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase
            (phosphorylating)
REACTION    N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate =
            N-acetyl-L-glutamyl 5-phosphate + NADPH + H+ [RN:R03443]
ALL_REAC    R03443
SUBSTRATE   N-acetyl-L-glutamate 5-semialdehyde [CPD:C01250];
            NADP+ [CPD:C00006];
            phosphate [CPD:C00009]
PRODUCT     N-acetyl-L-glutamyl 5-phosphate [CPD:C04133];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13863980]
  AUTHORS   BAICH A, VOGEL HJ.
  TITLE     N-Acetyl-gamma-Ilutamokinase and N-acetylglutamic gamma-semialdehyde
            dehydrogenase: repressible enzymes of arginine synthesis in
            Escherichia coli.
  JOURNAL   Biochem. Biophys. Res. Commun. 7 (1962) 491-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Glansdorff, N. and Sand, G.
  TITLE     Coordination of enzyme synthesis in the arginine pathway of
            Escherichia coli K-12.
  JOURNAL   Biochim. Biophys. Acta 108 (1965) 308-311.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K00145  N-acetyl-gamma-glutamyl-phosphate reductase
GENES       OSA: 4333458
            CME: CMN048C
            SCE: YER069W(ARG5,6)
            AGO: AGOS_ADL062W
            PIC: PICST_55623
            CGR: CAGL0J03124g
            SPO: SPAC4G9.09c(arg11)
            AFM: AFUA_6G02910
            CNE: CNF02250
            DDI: DDB_0231462(argC)
            ECO: b3958(argC)
            ECJ: JW3930(argC)
            ECE: Z5516(argC)
            ECS: ECs4887
            ECC: c4917(argC)
            ECI: UTI89_C4549(argC)
            ECP: ECP_4171
            ECV: APECO1_2509(argC)
            ECW: EcE24377A_4497(argC)
            ECX: EcHS_A4192
            STY: STY3752(argC)
            STT: t3503(argC)
            SPT: SPA3959(argC)
            SEC: SC4011(argC)
            STM: STM4121(argC)
            YPE: YPO3927(argC)
            YPK: y0310(argC)
            YPM: YP_3123(argC)
            YPA: YPA_0097
            YPN: YPN_0042
            YPP: YPDSF_3537
            YPS: YPTB0110(argC)
            YPI: YpsIP31758_0127(argC)
            YEN: YE0119(argC)
            SFL: SF4035(argC)
            SFX: S3711(argC)
            SFV: SFV_4027(argC)
            SSN: SSON_4131(argC)
            SBO: SBO_3977(argC)
            SDY: SDY_3793(argC)
            ECA: ECA0192(argC)
            PLU: plu4744(argC)
            BUC: BU048(argC)
            BAS: BUsg045(argC)
            ENT: Ent638_4028
            SPE: Spro_4781
            HDU: HD0890(argC)
            PMU: PM1118(argC)
            MSU: MS0235(argC)
            APL: APL_0242(argC)
            ASU: Asuc_0255
            XFA: XF1002
            XFT: PD0294(argC)
            XCC: XCC2243(argC)
            XCB: XC_1875
            XCV: XCV2545(argC)
            XAC: XAC2346(argC)
            XOO: XOO2670(argC)
            XOM: XOO_2516(XOO2516)
            VCH: VC2644
            VCO: VC0395_A2220(argC)
            VVU: VV1_1371
            VVY: VV3002
            VPA: VP2759
            VFI: VF2306
            PPR: PBPRA0266
            PAE: PA0662(argC)
            PAU: PA14_08480(argC)
            PAP: PSPA7_0803(argC)
            PPU: PP_0432 PP_3633(argC)
            PPF: Pput_0465 Pput_2100
            PST: PSPTO_0604(argC)
            PSB: Psyr_4569
            PSP: PSPPH_0684(argC)
            PFL: PFL_5611(argC)
            PFO: Pfl_5102
            PEN: PSEEN0460(argC) PSEEN1929
            PMY: Pmen_3933
            PAR: Psyc_1501(argC)
            PCR: Pcryo_1680
            PRW: PsycPRwf_1598
            ACI: ACIAD1360(argC)
            SON: SO_0275(argC)
            SDN: Sden_0250
            SFR: Sfri_0191
            SAZ: Sama_0256
            SBL: Sbal_4124
            SBM: Shew185_4095
            SLO: Shew_0202
            SPC: Sputcn32_3717
            SSE: Ssed_4276
            SPL: Spea_0227
            SHE: Shewmr4_3709
            SHM: Shewmr7_0236
            SHN: Shewana3_3905
            SHW: Sputw3181_3860
            ILO: IL0612(argC)
            CPS: CPS_0460(argC)
            PHA: PSHAa2291(argC)
            PAT: Patl_0982
            SDE: Sde_0833
            PIN: Ping_0228
            MAQ: Maqu_0691
            MCA: MCA0700(argC)
            TCX: Tcr_0348
            NOC: Noc_1047
            AEH: Mlg_0434
            HHA: Hhal_0880
            HCH: HCH_06245(argC)
            CSA: Csal_2714
            ABO: ABO_0359(argC)
            MMW: Mmwyl1_1483
            AHA: AHA_0593(argC)
            RMA: Rmag_1061
            VOK: COSY_0960(argC)
            NME: NMB1787
            NMA: NMA0676(argC)
            NMC: NMC0434(argC)
            NGO: NGO0118
            CVI: CV_3695(argC)
            RSO: RSc0142(argC)
            REU: Reut_A0193(argC) Reut_B4603
            REH: H16_A0220(argC1) H16_B0337(argC2)
            RME: Rmet_0148 Rmet_1768
            BMA: BMA2590(argC)
            BMV: BMASAVP1_A3128(argC-1) BMASAVP1_A3528(argC-2)
            BML: BMA10299_A1965(argC)
            BMN: BMA10247_3519(argC)
            BXE: Bxe_A0277
            BVI: Bcep1808_0296 Bcep1808_3782
            BUR: Bcep18194_A3413(argC) Bcep18194_B3171
            BCN: Bcen_2792 Bcen_5150
            BCH: Bcen2424_0314 Bcen2424_5709
            BAM: Bamb_0233 Bamb_4978
            BPS: BPSL3246(argC)
            BPM: BURPS1710b_0023(argC)
            BPL: BURPS1106A_3855(argC)
            BPD: BURPS668_3793(argC)
            BTE: BTH_I3114(argC)
            PNU: Pnuc_1884
            BPE: BP2960(argC)
            BPA: BPP3882(argC)
            BBR: BB4355(argC)
            RFR: Rfer_3946
            POL: Bpro_4683
            PNA: Pnap_3954
            AAV: Aave_4685
            AJS: Ajs_4048
            VEI: Veis_1060 Veis_2731
            MPT: Mpe_A0073
            HAR: HEAR0242 HEAR0657
            MMS: mma_0296
            NEU: NE1482(argC)
            NET: Neut_0764
            NMU: Nmul_A0559
            EBA: ebA935(argC)
            AZO: azo3916(argC)
            DAR: Daro_1863
            TBD: Tbd_0455
            MFA: Mfla_0057
            HHE: HH0669(argC)
            WSU: WS2086(argC)
            TDN: Tmden_1533
            CJE: Cj0224(argC)
            CJR: CJE0275(argC)
            CJJ: CJJ81176_0249(argC)
            CJU: C8J_0202(argC)
            CJD: JJD26997_0222(argC)
            CFF: CFF8240_0328(argC)
            CCV: CCV52592_1654(argC)
            CHA: CHAB381_1309(argC)
            ABU: Abu_0986(argC)
            NIS: NIS_1312(argC)
            SUN: SUN_1304(argC)
            GSU: GSU2874(argC)
            GME: Gmet_0608
            GUR: Gura_1051
            PCA: Pcar_1898
            PPD: Ppro_3080
            DVU: DVU0492(argC)
            DVL: Dvul_2449
            DDE: Dde_3455
            LIP: LI0099(argC)
            DPS: DP1325
            ADE: Adeh_0171 Adeh_0588
            AFW: Anae109_0180 Anae109_0633
            MXA: MXAN_5110(argC)
            SAT: SYN_00234
            SFU: Sfum_1667
            ERU: Erum7830(argC)
            ERW: ERWE_CDS_08280(argC)
            ERG: ERGA_CDS_08180(argC)
            ECN: Ecaj_0820
            ECH: ECH_1017(argC)
            PUB: SAR11_1027(argC)
            MLO: mll8452
            MES: Meso_1161
            PLA: Plav_2939
            SME: SMc01801(argC)
            SMD: Smed_0859
            ATU: Atu1244(argC)
            ATC: AGR_C_2293
            RET: RHE_CH01567(argC)
            RLE: RL1668(argC)
            BME: BMEI1171
            BMF: BAB1_0808(argC)
            BMS: BR0788(argC)
            BMB: BruAb1_0802(argC)
            BOV: BOV_0783(argC)
            OAN: Oant_2500
            BJA: blr4385
            BRA: BRADO3558(argC) BRADO6484(argC)
            BBT: BBta_1151(argC) BBta_3983(argC)
            RPA: RPA2491(argC)
            RPB: RPB_2972
            RPC: RPC_2823
            RPD: RPD_2488
            RPE: RPE_2944
            NWI: Nwi_1651
            NHA: Nham_2314
            BHE: BH07530(argC)
            BQU: BQ05380(argC)
            BBK: BARBAKC583_0628(argC)
            XAU: Xaut_4756
            CCR: CC_1378
            SIL: SPO0964(argC-1) SPO1876(argC-2)
            SIT: TM1040_1123
            RSP: RSP_2946(argC)
            RSH: Rsph17029_1592
            RSQ: Rsph17025_0898
            JAN: Jann_2336
            RDE: RD1_3227(argC)
            PDE: Pden_1656
            MMR: Mmar10_0366
            HNE: HNE_2314(argC)
            ZMO: ZMO0804(argC)
            NAR: Saro_1114
            SAL: Sala_0711
            SWI: Swit_0095
            ELI: ELI_01670
            GOX: GOX1444
            GBE: GbCGDNIH1_0967
            ACR: Acry_1789
            RRU: Rru_A2421
            MAG: amb1793
            MGM: Mmc1_0248
            ABA: Acid345_4161
            SUS: Acid_0723
            BSU: BG10191(argC)
            BHA: BH2900(argC)
            BAN: BA4355(argC)
            BAR: GBAA4355(argC)
            BAA: BA_4812
            BAT: BAS4040
            BCA: BCE_4203(argC)
            BCZ: BCZK3887(argC)
            BCY: Bcer98_2829
            BTK: BT9727_3879(argC)
            BTL: BALH_3747
            BLI: BL03241(argC)
            BLD: BLi01206(argC)
            BCL: ABC2558(argC)
            BAY: RBAM_011190
            BPU: BPUM_1042
            OIH: OB1075(argC)
            GKA: GK0790
            SAU: SA0178(argC)
            SAV: SAV0184(argC)
            SAM: MW0158(argC)
            SAR: SAR0185(argC)
            SAS: SAS0159
            SAC: SACOL0169(argC1)
            SAB: SAB0124c SAB2006c
            SAA: SAUSA300_0186(argC)
            SAO: SAOUHSC_00149
            SAJ: SaurJH9_0169
            SAH: SaurJH1_0174
            SEP: SE1212
            SER: SERP1092(argC)
            SSP: SSP0221
            LMO: lmo1591(argC)
            LMF: LMOf2365_1613(argC)
            LIN: lin1633(argC)
            LWE: lwe1604(argC)
            LLA: L0104(argC)
            LLC: LACR_0856
            LLM: llmg_1758(argC)
            SMU: SMU.663(argC)
            STC: str0464(argC)
            STL: stu0464(argC)
            SSA: SSA_0757(argC)
            SGO: SGO_1569(argC)
            LPL: lp_0487(argC1) lp_0528(argC2)
            STH: STH2892
            CAC: CAC2390(argC)
            CNO: NT01CX_2379(argC)
            CTH: Cthe_1863
            CDF: CD2034(argC)
            CBE: Cbei_4517
            CKL: CKL_1553(argC)
            AMT: Amet_3383
            CHY: CHY_2265(argC)
            DSY: DSY0760
            DRM: Dred_0271
            SWO: Swol_2291
            CSC: Csac_1531
            TTE: TTE2498(argC)
            MTA: Moth_2290
            MTU: Rv1652(argC)
            MTC: MT1690(argC)
            MBO: Mb1680(argC)
            MBB: BCG_1691(argC)
            MLE: ML1406(argC)
            MPA: MAP1361(argC)
            MAV: MAV_3118(argC)
            MSM: MSMEG_3776(argC)
            MVA: Mvan_3314
            MGI: Mflv_3530
            MMC: Mmcs_2972
            MKM: Mkms_3016
            MJL: Mjls_2987
            CGL: NCgl1340(cgl1394)
            CGB: cg1580(argC)
            CEF: CE1526(argC)
            CDI: DIP1167(argC)
            CJK: jk0841(argC)
            NFA: nfa19360(argC)
            RHA: RHA1_ro00956(argC)
            SCO: SCO1580(argC)
            SMA: SAV6763(argC)
            LXX: Lxx06030(argC)
            CMI: CMM_2001(argC)
            ART: Arth_1496
            AAU: AAur_1631(argC)
            PAC: PPA1350
            NCA: Noca_2468
            TFU: Tfu_2057
            FRA: Francci3_3175
            FAL: FRAAL5208(argC)
            ACE: Acel_1263
            KRA: Krad_3161
            SEN: SACE_5263
            STP: Strop_1888
            BLO: BL1064(argC)
            BAD: BAD_0925(argC)
            RXY: Rxyl_2885
            RBA: RB2552(argC)
            LIL: LA2178(argC)
            LIC: LIC11746(argC)
            LBJ: LBJ_1343(argC)
            LBL: LBL_1568(argC)
            SYN: sll0080(argC)
            SYW: SYNW1262(argC)
            SYC: syc0123_c(argC)
            SYF: Synpcc7942_1433
            SYD: Syncc9605_1389
            SYE: Syncc9902_1099
            SYG: sync_1382(argC)
            SYR: SynRCC307_1353(argC)
            SYX: SynWH7803_1253(argC)
            CYA: CYA_0652(argC)
            CYB: CYB_0289(argC)
            TEL: tll2219(argC)
            GVI: glr4010(argC)
            ANA: all2498(argC) alr3537(hisH)
            AVA: Ava_0430 Ava_3516
            PMA: Pro0944(argC)
            PMM: PMM0892(argC)
            PMT: PMT0709(hisH)
            PMN: PMN2A_0318
            PMI: PMT9312_0908
            PMB: A9601_09691(argC)
            PMC: P9515_09741(argC)
            PMF: P9303_15121(argC)
            PMG: P9301_09671(argC)
            PMH: P9215_10001
            PME: NATL1_09911(argC)
            TER: Tery_2788
            BTH: BT_3759
            BFR: BF0532
            BFS: BF0480(argC)
            SRU: SRU_2216(argC)
            CHU: CHU_3081(argC)
            GFO: GFO_2106(argC)
            FJO: Fjoh_3434
            CTE: CT1109(argC)
            CCH: Cag_0772
            CPH: Cpha266_1320
            PVI: Cvib_0877
            PLT: Plut_1049
            DET: DET1626(argC)
            DEH: cbdb_A1722(argC)
            DEB: DehaBAV1_1371
            RRS: RoseRS_1060 RoseRS_4052
            RCA: Rcas_3362 Rcas_3468
            DRA: DR_0078
            DGE: Dgeo_1604
            TTH: TTC0836
            TTJ: TTHA1197
            AAE: aq_1879(argC)
            TMA: TM1782
            TPT: Tpet_1069
            MJA: MJ1096
            MMP: MMP0116(argC)
            MMQ: MmarC5_1562
            MMZ: MmarC7_1115
            MAE: Maeo_1314
            MVN: Mevan_1121
            MAC: MA3566(argC)
            MBA: Mbar_A2001
            MMA: MM_0476
            MBU: Mbur_1342
            MTP: Mthe_0489
            MHU: Mhun_3227
            MLA: Mlab_0715
            MEM: Memar_0151
            MBN: Mboo_0068
            MST: Msp_0552(argC)
            MSI: Msm_0860
            MKA: MK1077(argC)
            HMA: rrnAC2678(argC)
            HWA: HQ3715A(argC)
            NPH: NP5260A(argC)
            PTO: PTO1472
            PHO: PH1720
            PAB: PAB0291(argC)
            PFU: PF1683
            TKO: TK0277
            RCI: LRC63(argC) RCIX1777(argC)
            APE: APE_1462
            SSO: SSO0155(argC)
            STO: ST0195
            SAI: Saci_0750(argC)
            MSE: Msed_0164
            PAI: PAE2881(argC)
            PIS: Pisl_0276
            PCL: Pcal_0373
            PAS: Pars_0966
STRUCTURES  PDB: 1VKN  2CVO  2G17  2I3A  2I3G  2NQT  2OZP  2Q49  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.38
            ExPASy - ENZYME nomenclature database: 1.2.1.38
            ExplorEnz - The Enzyme Database: 1.2.1.38
            ERGO genome analysis and discovery system: 1.2.1.38
            BRENDA, the Enzyme Database: 1.2.1.38
            CAS: 37251-00-6
///
ENTRY       EC 1.2.1.39                 Enzyme
NAME        phenylacetaldehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     phenylacetaldehyde:NAD+ oxidoreductase
REACTION    phenylacetaldehyde + NAD+ + H2O = phenylacetate + NADH + 2 H+
            [RN:R02536]
ALL_REAC    R02536
SUBSTRATE   phenylacetaldehyde [CPD:C00601];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     phenylacetate [CPD:C07086];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Fujioka, M., Morino, Y. and Wada, H.
  TITLE     Metabolism of phenylalanine (Achromobacter eurydice). III.
            Phenylacetaldehyde dehydrogenase.
  JOURNAL   Methods Enzymol. 17A (1970) 593-596.
  ORGANISM  Achromobacter eurydice
PATHWAY     PATH: map00360  Phenylalanine metabolism
            PATH: map00643  Styrene degradation
ORTHOLOGY   KO: K00146  phenylacetaldehyde dehydrogenase
GENES       PIC: PICST_90594(MSC7)
            ECO: b1385(feaB)
            ECJ: JW1380(feaB)
            ECW: EcE24377A_1570(feaB)
            ECX: EcHS_A1472(feaB)
            STY: STY3298
            STT: t3051
            SPT: SPA2997
            SEC: SC3069(feaB)
            STM: STM3129
            PLU: plu4285(feaB)
            SPE: Spro_0985
            PFL: PFL_3217(styD)
            PEN: PSEEN3107
            REH: H16_B1358(paaK2) H16_B1939(feaB)
            BMA: BMA2663 BMAA1365
            BMV: BMASAVP1_0348 BMASAVP1_A3290
            BML: BMA10299_0628 BMA10299_A1837
            BMN: BMA10247_2715 BMA10247_A0943
            BXE: Bxe_B0108 Bxe_B1805
            BAM: Bamb_4998
            BPS: BPSL0051 BPSS0868(feaB)
            BPM: BURPS1710b_0272 BURPS1710b_A2466(feaB)
            BPL: BURPS1106A_A1201(ubiC)
            BPD: BURPS668_A1274
            BTE: BTH_I0050 BTH_II0330(pad) BTH_II1537
            BPA: BPP2085
            BBR: BB1481
            SIL: SPOA0112(feaB)
            MTC: MT2926
            MPA: MAP2929c(aldC)
            CGL: NCgl2619(gabD2)
            CGB: cg3004(gabD1)
            CEF: CE0603
            CJK: jk1473
            SCO: SCO1612(SCI35.34c)
            SMA: SAV6726(feaB)
            AAU: AAur_3626(maoB) AAur_pTC10061(maoB) AAur_pTC20096(maoB)
            SEN: SACE_5353(aldC)
            PMB: A9601_03571
            PMC: P9515_03631
            PMF: P9303_21711
            PMG: P9301_03581
            PME: NATL1_04241
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.39
            ExPASy - ENZYME nomenclature database: 1.2.1.39
            ExplorEnz - The Enzyme Database: 1.2.1.39
            ERGO genome analysis and discovery system: 1.2.1.39
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.39
            BRENDA, the Enzyme Database: 1.2.1.39
            CAS: 58943-37-6
///
ENTRY       EC 1.2.1.40                 Enzyme
NAME        3alpha,7alpha,12alpha-trihydroxycholestan-26-al 26-oxidoreductase;
            cholestanetriol-26-al 26-dehydrogenase;
            3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al
            dehydrogenase;
            trihydroxydeoxycoprostanal dehydrogenase;
            THAL-NAD oxidoreductase;
            3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al:NAD+
            26-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al:NAD+
            26-oxidoreductase
REACTION    (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + NAD+
            + H2O =
            (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate +
            NADH + 2 H+ [RN:R03506]
ALL_REAC    R03506
SUBSTRATE   (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al;
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate;
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:5914340]
  AUTHORS   Masui T, Herman R, Staple E.
  TITLE     The oxidation of 5-beta-cholestane-3-alpha, 7-alpha, 12-alpha,
            26-tetraol to 5-beta-cholestane-3-alpha, 7-alpha,
            12-alpha-triol-26-oic acid via 5-beta-cholestane-3-alpha, 7-alpha,
            12-alpha-triol-26-al by rat liver.
  JOURNAL   Biochim. Biophys. Acta. 117 (1966) 266-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00120  Bile acid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.40
            ExPASy - ENZYME nomenclature database: 1.2.1.40
            ExplorEnz - The Enzyme Database: 1.2.1.40
            ERGO genome analysis and discovery system: 1.2.1.40
            BRENDA, the Enzyme Database: 1.2.1.40
            CAS: 62213-58-5
///
ENTRY       EC 1.2.1.41                 Enzyme
NAME        glutamate-5-semialdehyde dehydrogenase;
            beta-glutamylphosphate reductase;
            gamma-glutamyl phosphate reductase;
            beta-glutamylphosphate reductase;
            glutamate semialdehyde dehydrogenase;
            glutamate-gamma-semialdehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating)
REACTION    L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl
            5-phosphate + NADPH + H+ [RN:R03313]
ALL_REAC    R03313;
            (other) R04295
SUBSTRATE   L-glutamate 5-semialdehyde [CPD:C01165];
            phosphate [CPD:C00009];
            NADP+ [CPD:C00006]
PRODUCT     L-glutamyl 5-phosphate [CPD:C03287];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4399189]
  AUTHORS   Baich A.
  TITLE     The biosynthesis of proline in Escherichia coli: phosphate-dependent
            glutamate  -semialdehyde dehydrogenase (NADP), the second enzyme in
            the pathway.
  JOURNAL   Biochim. Biophys. Acta. 244 (1971) 129-34.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K00147  glutamate-5-semialdehyde dehydrogenase
GENES       HSA: 5832(ALDH18A1)
            MMU: 56454(Aldh18a1)
            CFA: 477781(ALDH18A1)
            XLA: 444469(MGC81784)
            CEL: T22H6.2
            ATH: AT3G55610(P5CS2)
            OSA: 4324853 4338979
            CME: CMQ024C
            SCE: YOR323C(PRO2)
            AGO: AGOS_ADR351C
            CGR: CAGL0F00693g
            SPO: SPAC821.11
            ANI: AN5799.2
            AFM: AFUA_2G07350
            AOR: AO090011000955
            CNE: CNL06240
            UMA: UM05919.1
            CPV: cgd7_4940
            CHO: Chro.70551
            TCR: 509067.70 511023.10
            LMA: LmjF32.3140
            ECO: b0243(proA)
            ECJ: JW0233(proA)
            ECE: Z0304(proA)
            ECS: ECs0270
            ECC: c0390(proA)
            ECI: UTI89_C0284(proA)
            ECP: ECP_0272
            ECV: APECO1_1726(proA)
            ECW: EcE24377A_0275(proA)
            ECX: EcHS_A0270
            STY: STY0367(proA)
            STT: t2528(proA)
            SPT: SPA2433(proA)
            SEC: SC0323(proA)
            STM: STM0322(proA)
            YPE: YPO3221(proA)
            YPK: y0967(proA)
            YPM: YP_0712(proA)
            YPA: YPA_2713
            YPN: YPN_0872
            YPP: YPDSF_2850
            YPS: YPTB0905(proA)
            YPI: YpsIP31758_3149(proA)
            SFL: SF0293(proA)
            SFX: S0314(proA)
            SFV: SFV_0285(proA)
            SSN: SSON_0285(proA)
            SBO: SBO_0249(proA)
            SDY: SDY_0473(proA)
            ECA: ECA3462(proA)
            PLU: plu1244(proA)
            SGL: SG0601
            SPE: Spro_0968
            HIT: NTHI1926(proA)
            HIP: CGSHiEE_03950(proA)
            HIQ: CGSHiGG_01830(proA)
            HSO: HS_0408(proA)
            PMU: PM0936(proA)
            MSU: MS1604(proA)
            APL: APL_1951(proA)
            ASU: Asuc_0931
            XFA: XF1005
            XFT: PD0297(proA)
            XCC: XCC2238(proA)
            XCB: XC_1880
            XCV: XCV2541(proA)
            XAC: XAC2342(proA)
            XOO: XOO2665(proA)
            XOM: XOO_2511(XOO2511)
            VCH: VC2273
            VCO: VC0395_A1863(proA)
            VVU: VV1_0325
            VVY: VV0859
            VPA: VP0677
            VFI: VF0741
            PPR: PBPRA0840
            PAE: PA4007(proA)
            PPU: PP_4811(proA)
            PST: PSPTO_4829(proA)
            PSB: Psyr_4369
            PSP: PSPPH_4411(proA)
            PFL: PFL_5456(proA)
            PFO: Pfl_3372 Pfl_4974
            PEN: PSEEN4830(proA)
            PAR: Psyc_0293(proA)
            PCR: Pcryo_0322
            PRW: PsycPRwf_2079
            ACI: ACIAD0547(proA)
            SON: SO_1122(proA)
            SDN: Sden_0151
            SFR: Sfri_0762 Sfri_0967
            SAZ: Sama_2515
            SPC: Sputcn32_0081
            SPL: Spea_3084
            SHE: Shewmr4_0953 Shewmr4_3849
            SHM: Shewmr7_0991 Shewmr7_3942
            SHN: Shewana3_0955 Shewana3_4057
            SHW: Sputw3181_3996
            ILO: IL1986(proA)
            CPS: CPS_4833(proA)
            PHA: PSHAa0280(proA)
            PAT: Patl_4145 Patl_4268
            SDE: Sde_3345
            PIN: Ping_2952
            MAQ: Maqu_2417
            LPN: lpg1609
            LPF: lpl1415(proA)
            LPP: lpp1574(proA)
            MCA: MCA1880(proA)
            TCX: Tcr_0482
            NOC: Noc_2662
            AEH: Mlg_0403
            HHA: Hhal_2142
            HCH: HCH_05847
            CSA: Csal_1541
            ABO: ABO_1951(proA)
            MMW: Mmwyl1_2852
            AHA: AHA_3420(proA)
            RMA: Rmag_0133
            VOK: COSY_0135(proA)
            NME: NMB1068
            NMA: NMA1267(proA)
            NMC: NMC1032(proA)
            NGO: NGO0850
            CVI: CV_4289(proA)
            RSO: RSc2741(proA)
            REU: Reut_A2831
            REH: H16_A3136(proA)
            RME: Rmet_2970
            BMA: BMA2450(proA)
            BMV: BMASAVP1_A0367(proA)
            BML: BMA10299_A1226(proA)
            BMN: BMA10247_2637(proA)
            BXE: Bxe_A0579
            BUR: Bcep18194_A3743
            BCN: Bcen_0174
            BCH: Bcen2424_0657
            BAM: Bamb_0552
            BPS: BPSL2935(proA)
            BPM: BURPS1710b_3447(proA)
            BPL: BURPS1106A_3447(proA)
            BPD: BURPS668_3412(proA)
            BTE: BTH_I1214(proA)
            PNU: Pnuc_0235
            BPE: BP2041(proA)
            BPA: BPP1728(proA)
            BBR: BB3380(proA)
            RFR: Rfer_0761
            POL: Bpro_4584
            PNA: Pnap_3751
            AAV: Aave_4545
            AJS: Ajs_3913
            MPT: Mpe_A0269
            HAR: HEAR2664(proA)
            MMS: mma_2899
            NEU: NE2158(proA)
            NET: Neut_2104
            NMU: Nmul_A0514
            EBA: ebA4380(proA)
            AZO: azo3218(proA)
            DAR: Daro_0540
            TBD: Tbd_2442
            MFA: Mfla_2158
            HHE: HH0806(proA)
            WSU: WS1300(proA)
            TDN: Tmden_0792
            CJE: Cj0558c(proA)
            CJR: CJE0662(proA)
            CJJ: CJJ81176_0583(proA)
            CJU: C8J_0519(proA)
            CFF: CFF8240_0634(proA)
            CCV: CCV52592_0754(proA)
            CHA: CHAB381_1319(proA)
            CCO: CCC13826_1479
            ABU: Abu_1757(proA)
            NIS: NIS_0861(proA)
            SUN: SUN_1760(proA)
            GSU: GSU3211(proA)
            GME: Gmet_3199
            GUR: Gura_4131
            PCA: Pcar_2579
            DVU: DVU1953(proA)
            DDE: Dde_1633
            DPS: DP2588
            ADE: Adeh_0212
            AFW: Anae109_0227
            SAT: SYN_02002
            SFU: Sfum_3644
            PUB: SAR11_0224(proA)
            MLO: mll4009
            MES: Meso_3456
            PLA: Plav_1478
            SME: SMc03777(proA)
            SMD: Smed_3011
            ATU: Atu2779(proA)
            ATC: AGR_C_5042
            RET: RHE_CH04069(proA)
            RLE: RL4683(proA)
            BME: BMEI0208
            BMF: BAB1_1851(proA)
            BMS: BR1843(proA)
            BMB: BruAb1_1822(proA)
            BOV: BOV_1776(proA)
            OAN: Oant_1056
            BJA: blr0429(proA)
            BRA: BRADO0430(proA)
            BBT: BBta_0419(proA)
            RPA: RPA0164(proA)
            RPB: RPB_0253
            RPC: RPC_0161
            RPD: RPD_0571
            RPE: RPE_0266
            NWI: Nwi_0444
            NHA: Nham_0520
            BHE: BH01580(proA)
            BQU: BQ01480(proA)
            BBK: BARBAKC583_0319(proA)
            XAU: Xaut_2058
            CCR: CC_3430
            SIL: SPO1984(proA)
            SIT: TM1040_1205
            RSP: RSP_3824(proA)
            RSH: Rsph17029_3516
            JAN: Jann_2285
            RDE: RD1_2658(proA)
            MMR: Mmar10_2669
            HNE: HNE_3429(proA)
            ZMO: ZMO1661(proA)
            NAR: Saro_0060
            SAL: Sala_0581
            SWI: Swit_2337
            ELI: ELI_07240
            GOX: GOX1147
            GBE: GbCGDNIH1_1708
            RRU: Rru_A1238
            MAG: amb4082
            MGM: Mmc1_3348
            ABA: Acid345_1268
            BSU: BG10964(proA)
            BHA: BH1504
            BAN: BA2992(proA)
            BAR: GBAA2992(proA)
            BAA: BA_3499
            BAT: BAS2781
            BCA: BCE_3028(proA)
            BCZ: BCZK2711(proA)
            BTK: BT9727_2730(proA)
            BLI: BL01984(proAA) BL03751(proA)
            BLD: BLi01413(proA) BLi02148
            BCL: ABC1766(proA)
            BAY: RBAM_012940
            BPU: BPUM_1208 BPUM_1822
            OIH: OB1053(proA)
            GKA: GK2049
            LMO: lmo1259(proA)
            LMF: LMOf2365_1276(proA)
            LIN: lin1227(proA)
            LWE: lwe1278(proA)
            LLA: L0116(proA)
            LLC: LACR_1716
            LLM: llmg_0886(proA)
            SPY: SPy_1670(proA)
            SPZ: M5005_Spy_1370(proA)
            SPM: spyM18_1679(proA)
            SPG: SpyM3_1406(proA)
            SPS: SPs0458
            SPH: MGAS10270_Spy1488(proA)
            SPI: MGAS10750_Spy1480(proA)
            SPJ: MGAS2096_Spy1393(proA)
            SPK: MGAS9429_Spy1368(proA)
            SPF: SpyM50421(proA)
            SPA: M6_Spy1418
            SPB: M28_Spy1413(proA)
            SPN: SP_0932
            SPR: spr0833(proA)
            SPD: SPD_0823(proA)
            SAG: SAG0284(proA)
            SAN: gbs0274(proA)
            SAK: SAK_0356(proA)
            SMU: SMU.450(proA)
            STC: str1710(proA)
            STL: stu1710(proA)
            SSA: SSA_1073(proA)
            SGO: SGO_1098(proA)
            LPL: lp_0017(proA)
            LSL: LSL_1611(proA)
            LCA: LSEI_2357
            LRE: Lreu_0345
            EFA: EF0037(proA)
            OOE: OEOE_0948
            STH: STH2539
            CAC: CAC3254(proA)
            CPE: CPE2578(proA)
            CPF: CPF_2903(proA)
            CPR: CPR_2582(proA)
            CTC: CTC01042
            CNO: NT01CX_0901(proA)
            CKL: CKL_2735(proA)
            CHY: CHY_0383(proA)
            DSY: DSY1387
            DRM: Dred_1169
            SWO: Swol_1607
            CSC: Csac_1708
            TTE: TTE1278(proA)
            MTA: Moth_0563
            MTU: Rv2427c(proA)
            MTC: MT2500(proA)
            MBO: Mb2451c(proA)
            MBB: BCG_2444c(proA)
            MLE: ML1458(proA)
            MPA: MAP2247c(proA)
            MAV: MAV_1747(proA)
            MSM: MSMEG_4584(proA)
            MVA: Mvan_3934
            MGI: Mflv_2644
            MMC: Mmcs_3538
            MKM: Mkms_3611
            MJL: Mjls_3543
            CGL: NCgl2272(proA)
            CGB: cg2586(proA)
            CEF: CE2260(proA)
            CDI: DIP1776(proA)
            CJK: jk0565(proA)
            NFA: nfa13710(proA)
            RHA: RHA1_ro01300(proA)
            SCO: SCO2585(proA)
            SMA: SAV5473(proA)
            LXX: Lxx08080(proA)
            ART: Arth_2387
            AAU: AAur_2363(proA)
            PAC: PPA0835
            TFU: Tfu_2175
            FRA: Francci3_1227
            FAL: FRAAL1931(proA)
            ACE: Acel_0761
            KRA: Krad_3452
            SEN: SACE_1424(proA)
            STP: Strop_0385 Strop_0676
            BLO: BL1034(proA)
            BAD: BAD_0901(proA)
            RBA: RB7359(proA)
            TPA: TP0350
            LIL: LA0854(proA)
            LIC: LIC12771(proA)
            LBJ: LBJ_2490(proA)
            LBL: LBL_0619(proA)
            SYN: sll0373(proA) sll0461(proA)
            SYW: SYNW1486(proA)
            SYC: syc1833_c(proA) syc1855_d(proA)
            SYF: Synpcc7942_2243 Synpcc7942_2265
            SYD: Syncc9605_1026
            SYE: Syncc9902_0927
            SYG: sync_1878(proA)
            SYR: SynRCC307_0926(proA)
            SYX: SynWH7803_0764(proA) SynWH7803_1325(proA)
                 SynWH7803_1326(proA)
            CYA: CYA_0496 CYA_2820(proA)
            CYB: CYB_0553 CYB_0823(proA)
            TEL: tlr0764(proA) tlr1710
            GVI: gll3923(proA)
            ANA: all2166 alr3995
            AVA: Ava_0057 Ava_1702
            PMA: Pro1071(proA)
            PMM: PMM0590(proA)
            PMT: PMT0436(proA)
            PMN: PMN2A_0026
            PMI: PMT9312_0590
            PMB: A9601_06461(proA)
            PMC: P9515_06551(proA)
            PMF: P9303_18451(proA)
            PMG: P9301_06161(proA)
            PMH: P9215_06721
            PME: NATL1_06461(proA)
            TER: Tery_2275
            BTH: BT_3718
            BFR: BF0498
            BFS: BF0443(proA)
            SRU: SRU_1253(proA)
            GFO: GFO_1963(proA)
            FJO: Fjoh_3432
            CTE: CT1473(proA)
            CCH: Cag_1102
            CPH: Cpha266_1865
            PVI: Cvib_1295
            PLT: Plut_1479
            DET: DET1288(proA)
            DEH: cbdb_A1224(proA)
            DEB: DehaBAV1_1099
            RRS: RoseRS_0763
            RCA: Rcas_4447
            DRA: DR_1826
            DGE: Dgeo_0993
            TTH: TTC1564
            TTJ: TTHA1928
            AAE: aq_1071(proA)
            TMA: TM0293
            TPT: Tpet_0619
            MAC: MA4100(proA)
            MBA: Mbar_A0482
            MMA: MM_0819
            MBU: Mbur_2416
            HWA: HQ1844A(proA)
            NPH: NP3978A(proA)
STRUCTURES  PDB: 1O20  1VLU  2H5G  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.41
            ExPASy - ENZYME nomenclature database: 1.2.1.41
            ExplorEnz - The Enzyme Database: 1.2.1.41
            ERGO genome analysis and discovery system: 1.2.1.41
            BRENDA, the Enzyme Database: 1.2.1.41
            CAS: 54596-29-1
///
ENTRY       EC 1.2.1.42                 Enzyme
NAME        hexadecanal dehydrogenase (acylating);
            fatty acyl-CoA reductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     hexadecanal:NAD+ oxidoreductase (CoA-acylating)
REACTION    hexadecanal + CoA + NAD+ = hexadecanoyl-CoA + NADH + H+ [RN:R01277]
ALL_REAC    R01277
SUBSTRATE   hexadecanal [CPD:C00517];
            CoA [CPD:C00010];
            NAD+ [CPD:C00003]
PRODUCT     hexadecanoyl-CoA [CPD:C00154];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts, more slowly, on octadecanoyl-CoA.
REFERENCE   1  [PMID:4343165]
  AUTHORS   Johnson RC, Gilbertson JR.
  TITLE     Isolation, characterization, and partial purification of a fatty
            acyl coenzyme A reductase from bovine cardiac muscle.
  JOURNAL   J. Biol. Chem. 247 (1972) 6991-8.
  ORGANISM  cow [GN:bta]
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.42
            ExPASy - ENZYME nomenclature database: 1.2.1.42
            ExplorEnz - The Enzyme Database: 1.2.1.42
            ERGO genome analysis and discovery system: 1.2.1.42
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.42
            BRENDA, the Enzyme Database: 1.2.1.42
            CAS: 72561-01-4
///
ENTRY       EC 1.2.1.43                 Enzyme
NAME        formate dehydrogenase (NADP+);
            NADP+-dependent formate dehydrogenase;
            formate dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     formate:NADP+ oxidoreductase
REACTION    formate + NADP+ = CO2 + NADPH [RN:R00134]
ALL_REAC    R00134
SUBSTRATE   formate [CPD:C00058];
            NADP+ [CPD:C00006]
PRODUCT     CO2 [CPD:C00011];
            NADPH [CPD:C00005]
COFACTOR    Iron [CPD:C00023];
            Tungsten [CPD:C00753];
            Selenium [CPD:C01529]
COMMENT     A tungsten-selenium-iron protein.
REFERENCE   1  [PMID:4154039]
  AUTHORS   Andreesen JR, Ljungdahl LG.
  TITLE     Nicotinamide adenine dinucleotide phosphate-dependent formate
            dehydrogenase from Clostridium thermoaceticum: purification and
            properties.
  JOURNAL   J. Bacteriol. 120 (1974) 6-14.
  ORGANISM  Clostridium thermoaceticum
REFERENCE   2  [PMID:6822536]
  AUTHORS   Yamamoto I, Saiki T, Liu SM, Ljungdahl LG.
  TITLE     Purification and properties of NADP-dependent formate dehydrogenase
            from Clostridium thermoaceticum, a tungsten-selenium-iron protein.
  JOURNAL   J. Biol. Chem. 258 (1983) 1826-32.
  ORGANISM  Clostridium thermoaceticum
PATHWAY     PATH: map00680  Methane metabolism
ORTHOLOGY   KO: K05299  formate dehydrogenase (NADP+)
GENES       VFI: VFA0251 VFA0252
            WSU: WS0477(fdhB)
STRUCTURES  PDB: 2GSD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.43
            ExPASy - ENZYME nomenclature database: 1.2.1.43
            ExplorEnz - The Enzyme Database: 1.2.1.43
            ERGO genome analysis and discovery system: 1.2.1.43
            BRENDA, the Enzyme Database: 1.2.1.43
            CAS: 51377-43-6
///
ENTRY       EC 1.2.1.44                 Enzyme
NAME        cinnamoyl-CoA reductase;
            feruloyl-CoA reductase;
            cinnamoyl-coenzyme A reductase;
            ferulyl-CoA reductase;
            feruloyl coenzyme A reductase;
            p-hydroxycinnamoyl coenzyme A reductase;
            cinnamoyl-CoA:NADPH reductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     cinnamaldehyde:NADP+ oxidoreductase (CoA-cinnamoylating)
REACTION    cinnamaldehyde + CoA + NADP+ = cinnamoyl-CoA + NADPH + H+
            [RN:R02506]
ALL_REAC    R02506;
            (other) R01615 R01941 R02193 R02220 R06569
SUBSTRATE   cinnamaldehyde [CPD:C00903];
            CoA [CPD:C00010];
            NADP+ [CPD:C00006]
PRODUCT     cinnamoyl-CoA [CPD:C00540];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Acts also on a number of substituted cinnamoyl esters of coenzyme A.
REFERENCE   1  [PMID:236926]
  AUTHORS   Gross GG, Kreiten W.
  TITLE     Reduction of coenzyme A thioesters of cinnamic acids with an enzyme
            preparation from lignifying tissue of Forsythia.
  JOURNAL   FEBS. Lett. 54 (1975) 259-62.
  ORGANISM  Forsythia suspensa
REFERENCE   2  [PMID:6365550]
  AUTHORS   Sarni F, Grand C, Boudet AM.
  TITLE     Purification and properties of cinnamoyl-CoA reductase and cinnamyl
            alcohol dehydrogenase from poplar stems (Populus X euramericana).
  JOURNAL   Eur. J. Biochem. 139 (1984) 259-65.
  ORGANISM  Populus euramericana
REFERENCE   3  [PMID:7454]
  AUTHORS   Wengenmayer H, Ebel J, Grisebach H.
  TITLE     Enzymic synthesis of lignin precursors. Purification and properties
            of a cinnamoyl-CoA: NADPH reductase from cell suspension cultures of
            soybean (Glycinemax).
  JOURNAL   Eur. J. Biochem. 65 (1976) 529-36.
  ORGANISM  Glycine max [GN:egma]
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
ORTHOLOGY   KO: K05347  cinnamoyl-CoA reductase
            KO: K09753  cinnamoyl-CoA reductase
GENES       ATH: AT1G15950(CCR1) AT1G80820(CCR2)
            SPO: SPBC1773.04
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.44
            ExPASy - ENZYME nomenclature database: 1.2.1.44
            ExplorEnz - The Enzyme Database: 1.2.1.44
            ERGO genome analysis and discovery system: 1.2.1.44
            BRENDA, the Enzyme Database: 1.2.1.44
            CAS: 59929-39-4
///
ENTRY       EC 1.2.1.45                 Enzyme
NAME        4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase;
            2-hydroxy-4-carboxymuconate 6-semialdehyde dehydrogenase;
            2-hydroxy-4-carboxymuconate 6-semialdehyde dehydrogenase;
            4-carboxy-2-hydroxy-cis,cis-muconate-6-semialdehyde:NADP+
            oxidoreductase;
            alpha-hydroxy-gamma-carboxymuconic epsilon-semialdehyde
            dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4-carboxy-2-hydroxy-cis,cis-muconate-6-semialdehyde:NADP+
            6-oxidoreductase
REACTION    4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+ + H2O =
            4-carboxy-2-hydroxy-cis,cis-muconate + NADPH + 2 H+ [RN:R04453]
ALL_REAC    R04453;
            (other) R04278 R04279 R04418 R04419
SUBSTRATE   4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde [CPD:C04484];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     4-carboxy-2-hydroxy-cis,cis-muconate [CPD:C04324];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The enzyme does not act on unsubstituted aliphatic or aromatic
            aldehydes or glucose; NAD+ can replace NADP+, but with lower
            affinity.
REFERENCE   1  [PMID:26671]
  AUTHORS   Maruyama K, Ariga N, Tsuda M, Deguchi K.
  TITLE     Purification and properties of alpha-hydroxy-gamma-carboxymuconic
            epsilon-semialdehyde dehydrogenase.
  JOURNAL   J. Biochem. (Tokyo). 83 (1978) 1125-34.
  ORGANISM  Pseudomonas ochraceae
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00362  Benzoate degradation via hydroxylation
ORTHOLOGY   KO: K10219  4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase
GENES       PAT: Patl_3884
            RFR: Rfer_0329
            PNA: Pnap_2026
            VEI: Veis_0171
            AZO: azo2536(ligC)
            BRA: BRADO2343(ligC)
            BBT: BBta_2703(ligC)
            RPA: RPA4703(ligC)
            RPB: RPB_0871
            RPD: RPD_0981
            RPE: RPE_0752
            NAR: Saro_2811
            MAG: amb0255
            ART: Arth_4372
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.45
            ExPASy - ENZYME nomenclature database: 1.2.1.45
            ExplorEnz - The Enzyme Database: 1.2.1.45
            ERGO genome analysis and discovery system: 1.2.1.45
            BRENDA, the Enzyme Database: 1.2.1.45
            CAS: 67272-39-3
///
ENTRY       EC 1.2.1.46                 Enzyme
NAME        formaldehyde dehydrogenase;
            NAD+-linked formaldehyde dehydrogenase;
            NAD+-dependent formaldehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     formaldehyde:NAD+ oxidoreductase
REACTION    formaldehyde + NAD+ + H2O = formate + NADH + 2 H+ [RN:R00604]
ALL_REAC    R00604
SUBSTRATE   formaldehyde [CPD:C00067];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     formate [CPD:C00058];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:7461603]
  AUTHORS   Hohnloser W, Osswald B, Lingens F.
  TITLE     Enzymological aspects of caffeine demethylation and formaldehyde
            oxidation by Pseudomonas putida C1.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 361 (1980) 1763-6.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00680  Methane metabolism
ORTHOLOGY   KO: K00148  glutathione-independent formaldehyde dehydrogenase
GENES       PAU: PA14_71560(fdhA)
            PAP: PSPA7_6209(fdhA)
            PSB: Psyr_4718
            PSP: PSPPH_2569(fdhA1) PSPPH_4756(fdhA2)
            PFL: PFL_5723(fdhA)
            PFO: Pfl_5202
            PEN: PSEEN5156(fdhA)
            CPS: CPS_4039
            RSO: RSp0053(fdhA)
            REU: Reut_B4824
            BMA: BMAA0468(fdhA)
            BMV: BMASAVP1_0712(fdhA)
            BML: BMA10299_1008(fdhA)
            BMN: BMA10247_A1981(fdhA)
            BXE: Bxe_B1589(fdsA)
            BUR: Bcep18194_B0564
            BCH: Bcen2424_5090
            BPS: BPSS0545(fdhA)
            BPM: BURPS1710b_A2104(fdhA)
            BPL: BURPS1106A_A0738(fdhA)
            BPD: BURPS668_A0826(fdhA)
            BTE: BTH_II1870
            HAR: HEAR2048(fdhA)
            RET: RHE_PC00119
            RLE: pRL100370(fdhA)
            AAU: AAur_0480(fdhA) AAur_1867(fdhA)
            MMA: MM_0749
            HWA: HQ3187A(fdh)
            RCI: RCIX2285(fdh)
STRUCTURES  PDB: 1KOL  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.46
            ExPASy - ENZYME nomenclature database: 1.2.1.46
            ExplorEnz - The Enzyme Database: 1.2.1.46
            ERGO genome analysis and discovery system: 1.2.1.46
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.46
            BRENDA, the Enzyme Database: 1.2.1.46
            CAS: 9028-84-6
///
ENTRY       EC 1.2.1.47                 Enzyme
NAME        4-trimethylammoniobutyraldehyde dehydrogenase;
            4-trimethylaminobutyraldehyde dehydrogenase;
            4-N-trimethylaminobutyraldehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4-trimethylammoniobutanal:NAD+ 1-oxidoreductase
REACTION    4-trimethylammoniobutanal + NAD+ + H2O = 4-trimethylammoniobutanoate
            + NADH + 2 H+ [RN:R03283]
ALL_REAC    R03283
SUBSTRATE   4-trimethylammoniobutanal [CPD:C01149];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     4-trimethylammoniobutanoate [CPD:C01181];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:6770910]
  AUTHORS   Rebouche CJ, Engel AG.
  TITLE     Tissue distribution of carnitine biosynthetic enzymes in man.
  JOURNAL   Biochim. Biophys. Acta. 630 (1980) 22-9.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K00149  4-trimethylammoniobutyraldehyde dehydrogenase
GENES       HSA: 223(ALDH9A1)
            MMU: 56752(Aldh9a1)
            SPU: 580956(LOC580956)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.47
            ExPASy - ENZYME nomenclature database: 1.2.1.47
            ExplorEnz - The Enzyme Database: 1.2.1.47
            ERGO genome analysis and discovery system: 1.2.1.47
            BRENDA, the Enzyme Database: 1.2.1.47
            CAS: 73361-01-0
///
ENTRY       EC 1.2.1.48                 Enzyme
NAME        long-chain-aldehyde dehydrogenase;
            long-chain aliphatic aldehyde dehydrogenase;
            long-chain fatty aldehyde dehydrogenase;
            fatty aldehyde:NAD+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     long-chain-aldehyde:NAD+ oxidoreductase
REACTION    a long-chain aldehyde + NAD+ + H2O = a long-chain carboxylate + NADH
            + 2 H+ [RN:R02039]
ALL_REAC    R02039 > R01704
SUBSTRATE   long-chain aldehyde [CPD:C00609];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     long-chain carboxylate [CPD:C00347];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The best substrate is dodecylaldehyde.
REFERENCE   1  [PMID:5499619]
  AUTHORS   Lebeault JM, Roche B, Duvnjak Z, Azoulay E.
  TITLE     [Alcohol and aldehyde dehydrogenases of Candida tropicalis
            cultivated on hydrocarbons]
  JOURNAL   Biochim. Biophys. Acta. 220 (1970) 373-85.
  ORGANISM  Candida tropicalis
REFERENCE   2  [PMID:36040]
  AUTHORS   Moreau RA, Huang AH.
  TITLE     Oxidation of fatty alcohol in the cotyledons of jojoba seedlings.
  JOURNAL   Arch. Biochem. Biophys. 194 (1979) 422-30.
  ORGANISM  Simmondsia chinensis
REFERENCE   3
  AUTHORS   Moreau, R.A. and Huang, A.H.C.
  TITLE     Enzymes of wax ester catabolism in jojoba.
  JOURNAL   Methods Enzymol. 71 (1981) 804-813.
PATHWAY     PATH: map00071  Fatty acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.48
            ExPASy - ENZYME nomenclature database: 1.2.1.48
            ExplorEnz - The Enzyme Database: 1.2.1.48
            ERGO genome analysis and discovery system: 1.2.1.48
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.48
            BRENDA, the Enzyme Database: 1.2.1.48
            CAS: 59298-89-4
///
ENTRY       EC 1.2.1.49                 Enzyme
NAME        2-oxoaldehyde dehydrogenase (NADP+);
            alpha-ketoaldehyde dehydrogenase;
            methylglyoxal dehydrogenase;
            NADP+-linked alpha-ketoaldehyde dehydrogenase;
            2-ketoaldehyde dehydrogenase;
            NADP+-dependent alpha-ketoaldehyde dehydrogenase;
            2-oxoaldehyde dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-oxoaldehyde:NADP+ 2-oxidoreductase
REACTION    a 2-oxoaldehyde + NADP+ + H2O = a 2-oxo acid + NADPH + H+
            [RN:R01338]
ALL_REAC    R01338 > R00205;
            (other) R02260
SUBSTRATE   2-oxoaldehyde [CPD:C00538];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     2-oxo acid [CPD:C00161];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Not identical with EC 1.2.1.23 2-oxoaldehyde dehydrogenase (NAD+).
REFERENCE   1  [PMID:7107626]
  AUTHORS   Ray M, Ray S.
  TITLE     On the interaction of nucleotides and glycolytic intermediates with
            NAD-linked alpha-ketoaldehyde dehydrogenase.
  JOURNAL   J. Biol. Chem. 257 (1982) 10571-4.
  ORGANISM  goat
REFERENCE   2  [PMID:7107625]
  AUTHORS   Ray S, Ray M.
  TITLE     Purification and characterization of NAD and NADP-linked
            alpha-ketoaldehyde dehydrogenases involved in catalyzing the
            oxidation of methylglyoxal to pyruvate.
  JOURNAL   J. Biol. Chem. 257 (1982) 10566-70.
  ORGANISM  goat
PATHWAY     PATH: map00620  Pyruvate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.49
            ExPASy - ENZYME nomenclature database: 1.2.1.49
            ExplorEnz - The Enzyme Database: 1.2.1.49
            ERGO genome analysis and discovery system: 1.2.1.49
            BRENDA, the Enzyme Database: 1.2.1.49
            CAS: 83588-97-0
///
ENTRY       EC 1.2.1.50                 Enzyme
NAME        long-chain-fatty-acyl-CoA reductase;
            acyl-CoA reductase;
            acyl coenzyme A reductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming)
REACTION    a long-chain aldehyde + CoA + NADP+ = a long-chain acyl-CoA + NADPH
            + H+ [RN:R02620]
ALL_REAC    R02620
SUBSTRATE   long-chain aldehyde [CPD:C00609];
            CoA [CPD:C00010];
            NADP+ [CPD:C00006]
PRODUCT     long-chain acyl-CoA [CPD:C02843];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Together with EC 6.2.1.19
            long-chain-fatty-acid---luciferin-component ligase, forms a fatty
            acid reductase system that produces the substrate of EC 1.14.14.3
            alkanal monooxygenase (FMN-linked), thus being part of the bacterial
            luciferase system.
REFERENCE   1  [PMID:7085612]
  AUTHORS   Riendeau D, Rodriguez A, Meighen E.
  TITLE     Resolution of the fatty acid reductase from Photobacterium
            phosphoreum into acyl protein synthetase and acyl-CoA reductase
            activities. Evidence for an enzyme complex.
  JOURNAL   J. Biol. Chem. 257 (1982) 6908-15.
  ORGANISM  Photobacterium phosphoreum
REFERENCE   2
  AUTHORS   Wall, L. and Meighen, E.A.
  TITLE     Subunit structure of the fatty-acid reductase complex from
            Photobacterium phosphoreum.
  JOURNAL   Biochemistry 25 (1986) 4315-4321.
  ORGANISM  Photobacterium phosphoreum
GENES       PLU: plu2079(luxC)
            VFI: VFA0923
            CKL: CKL_3024
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.50
            ExPASy - ENZYME nomenclature database: 1.2.1.50
            ExplorEnz - The Enzyme Database: 1.2.1.50
            ERGO genome analysis and discovery system: 1.2.1.50
            BRENDA, the Enzyme Database: 1.2.1.50
            CAS: 50936-56-6
///
ENTRY       EC 1.2.1.51                 Enzyme
NAME        pyruvate dehydrogenase (NADP+);
            pyruvate dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     pyruvate:NADP+ 2-oxidoreductase (CoA-acetylating)
REACTION    pyruvate + CoA + NADP+ = acetyl-CoA + CO2 + NADPH [RN:R00210]
ALL_REAC    R00210
SUBSTRATE   pyruvate [CPD:C00022];
            CoA [CPD:C00010];
            NADP+ [CPD:C00006]
PRODUCT     acetyl-CoA [CPD:C00024];
            CO2 [CPD:C00011];
            NADPH [CPD:C00005]
INHIBITOR   Oxygen [CPD:C00007]
COMMENT     The Euglena enzyme can also use FAD or methyl viologen as acceptor,
            more slowly. The enzyme is inhibited by oxygen.
REFERENCE   1  [PMID:6438078]
  AUTHORS   Inui H, Miyatake K, Nakano Y, Kitaoka S.
  TITLE     Occurrence of oxygen-sensitive, NADP+-dependent pyruvate
            dehydrogenase in mitochondria of Euglena gracilis.
  JOURNAL   J. Biochem. (Tokyo). 96 (1984) 931-4.
  ORGANISM  Euglena gracilis
REFERENCE   2  [PMID:3110154]
  AUTHORS   Inui H, Ono K, Miyatake K, Nakano Y, Kitaoka S.
  TITLE     Purification and characterization of pyruvate:NADP+ oxidoreductase
            in Euglena gracilis.
  JOURNAL   J. Biol. Chem. 262 (1987) 9130-5.
  ORGANISM  Euglena gracilis
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00252  Alanine and aspartate metabolism
            PATH: map00620  Pyruvate metabolism
GENES       CPV: cgd4_690
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.51
            ExPASy - ENZYME nomenclature database: 1.2.1.51
            ExplorEnz - The Enzyme Database: 1.2.1.51
            ERGO genome analysis and discovery system: 1.2.1.51
            BRENDA, the Enzyme Database: 1.2.1.51
            CAS: 93389-35-6
///
ENTRY       EC 1.2.1.52                 Enzyme
NAME        oxoglutarate dehydrogenase (NADP+);
            oxoglutarate dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-oxoglutarate:NADP+ 2-oxidoreductase (CoA-succinylating)
REACTION    2-oxoglutarate + CoA + NADP+ = succinyl-CoA + CO2 + NADPH
            [RN:R00265]
ALL_REAC    R00265
SUBSTRATE   2-oxoglutarate [CPD:C00026];
            CoA [CPD:C00010];
            NADP+ [CPD:C00006]
PRODUCT     succinyl-CoA [CPD:C00091];
            CO2 [CPD:C00011];
            NADPH [CPD:C00005]
COMMENT     The Euglena enzyme can also use NAD+ as acceptor, but more slowly.
REFERENCE   1  [PMID:6438078]
  AUTHORS   Inui H, Miyatake K, Nakano Y, Kitaoka S.
  TITLE     Occurrence of oxygen-sensitive, NADP+-dependent pyruvate
            dehydrogenase in mitochondria of Euglena gracilis.
  JOURNAL   J. Biochem. (Tokyo). 96 (1984) 931-4.
  ORGANISM  Euglena gracilis
ORTHOLOGY   KO: K05890  
GENES       EBA: ebA4587(korC) p2A11(korC1)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.52
            ExPASy - ENZYME nomenclature database: 1.2.1.52
            ExplorEnz - The Enzyme Database: 1.2.1.52
            ERGO genome analysis and discovery system: 1.2.1.52
            BRENDA, the Enzyme Database: 1.2.1.52
            CAS: 126469-85-0
///
ENTRY       EC 1.2.1.53                 Enzyme
NAME        4-hydroxyphenylacetaldehyde dehydrogenase;
            4-HPAL dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4-hydroxyphenylacetaldehyde:NAD+ oxidoreductase
REACTION    4-hydroxyphenylacetaldehyde + NAD+ + H2O = 4-hydroxyphenylacetate +
            NADH + 2 H+ [RN:R02695]
ALL_REAC    R02695
SUBSTRATE   4-hydroxyphenylacetaldehyde [CPD:C03765];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     4-hydroxyphenylacetate [CPD:C00642];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     With EC 4.2.1.87 octopamine dehydratase, brings about the metabolism
            of octopamine in Pseudomonas.
REFERENCE   1  [PMID:3034855]
  AUTHORS   Cuskey SM, Peccoraro V, Olsen RH.
  TITLE     Initial catabolism of aromatic biogenic amines by Pseudomonas
            aeruginosa PAO: pathway description, mapping of mutations, and
            cloning of essential genes.
  JOURNAL   J. Bacteriol. 169 (1987) 2398-404.
  ORGANISM  Pseudomonas aeruginosa
PATHWAY     PATH: map00350  Tyrosine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.53
            ExPASy - ENZYME nomenclature database: 1.2.1.53
            ExplorEnz - The Enzyme Database: 1.2.1.53
            ERGO genome analysis and discovery system: 1.2.1.53
            BRENDA, the Enzyme Database: 1.2.1.53
            CAS: 109456-56-6
///
ENTRY       EC 1.2.1.54                 Enzyme
NAME        gamma-guanidinobutyraldehyde dehydrogenase;
            alpha-guanidinobutyraldehyde dehydrogenase;
            4-guanidinobutyraldehyde dehydrogenase;
            GBAL dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4-guanidinobutanal:NAD+ 1-oxidoreductase
REACTION    4-guanidinobutanal + NAD+ + H2O = 4-guanidinobutanoate + NADH + 2 H+
            [RN:R03177]
ALL_REAC    R03177
SUBSTRATE   4-guanidinobutanal [CPD:C02647];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     4-guanidinobutanoate [CPD:C01035];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Involved in the degradation of arginine in Pseudomonas putida (cf.
            EC 1.2.1.19 aminobutyraldehyde dehydrogenase).
REFERENCE   1
  AUTHORS   Yorifuji, T., Koike, K., Sakurai, T. and Yokoyama, K.
  TITLE     4-Aminobutyraldehyde and 4-guanidinobutyraldehyde dehydrogenases for
            arginine degradation in Pseudomonas putida.
  JOURNAL   Agric. Biol. Chem. 50 (1986) 2009-2016.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.54
            ExPASy - ENZYME nomenclature database: 1.2.1.54
            ExplorEnz - The Enzyme Database: 1.2.1.54
            ERGO genome analysis and discovery system: 1.2.1.54
            BRENDA, the Enzyme Database: 1.2.1.54
            CAS: 56831-75-5
///
ENTRY       EC 1.2.1.55       Obsolete  Enzyme
NAME        Transferred to 1.1.1.279
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Transferred entry: now EC 1.1.1.279 (R)-3-hydroxyacid-ester
            dehydrogenase (EC 1.2.1.55 created 1990, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.55
            ExPASy - ENZYME nomenclature database: 1.2.1.55
            ExplorEnz - The Enzyme Database: 1.2.1.55
            ERGO genome analysis and discovery system: 1.2.1.55
            BRENDA, the Enzyme Database: 1.2.1.55
///
ENTRY       EC 1.2.1.56       Obsolete  Enzyme
NAME        Transferred to 1.1.1.280
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Transferred entry: now EC 1.1.1.280, (S)-3-hydroxyacid-ester
            dehydrogenase (EC 1.2.1.56 created 1990, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.56
            ExPASy - ENZYME nomenclature database: 1.2.1.56
            ExplorEnz - The Enzyme Database: 1.2.1.56
            ERGO genome analysis and discovery system: 1.2.1.56
            BRENDA, the Enzyme Database: 1.2.1.56
///
ENTRY       EC 1.2.1.57                 Enzyme
NAME        butanal dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     butanal:NAD(P)+ oxidoreductase (CoA-acylating)
REACTION    butanal + CoA + NAD(P)+ = butanoyl-CoA + NAD(P)H + H+ [RN:R01172
            R01173]
ALL_REAC    R01172 R01173
SUBSTRATE   butanal [CPD:C01412];
            CoA [CPD:C00010];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     butanoyl-CoA [CPD:C00136];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on acetaldehyde, but more slowly.
REFERENCE   1  [PMID:3384801]
  AUTHORS   Palosaari NR, Rogers P.
  TITLE     Purification and properties of the inducible coenzyme A-linked
            butyraldehyde dehydrogenase from Clostridium acetobutylicum.
  JOURNAL   J. Bacteriol. 170 (1988) 2971-6.
  ORGANISM  Clostridium acetobutylicum [GN:cac]
PATHWAY     PATH: map00650  Butanoate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.57
            ExPASy - ENZYME nomenclature database: 1.2.1.57
            ExplorEnz - The Enzyme Database: 1.2.1.57
            ERGO genome analysis and discovery system: 1.2.1.57
            BRENDA, the Enzyme Database: 1.2.1.57
            CAS: 116412-25-0
///
ENTRY       EC 1.2.1.58                 Enzyme
NAME        phenylglyoxylate dehydrogenase (acylating)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     phenylglyoxylate:NAD+ oxidoreductase
REACTION    phenylglyoxylate + NAD+ + CoA-SH = benzoyl-S-CoA + CO2 + NADH
            [RN:R02450]
ALL_REAC    R02450
SUBSTRATE   phenylglyoxylate [CPD:C02137];
            NAD+ [CPD:C00003];
            CoA-SH [CPD:C00010]
PRODUCT     benzoyl-S-CoA;
            CO2 [CPD:C00011];
            NADH [CPD:C00004]
COFACTOR    FAD [CPD:C00016];
            Thiamin diphosphate [CPD:C00068];
            Iron-sulfur [CPD:C00824]
COMMENT     Requires thiamine diphosphate as cofactor. The enzyme from the
            denitrifying bacterium Azoarcus evansii is specific for
            phenylglyoxylate. 2-Oxoisovalerate is oxidized at 15% of the rate
            for phenylglyoxylate. Also reduces viologen dyes. Contains
            iron-sulfur centres and FAD.
REFERENCE   1  [PMID:9490067]
  AUTHORS   Hirsch W, Schagger H, Fuchs G.
  TITLE     Phenylglyoxylate:NAD+ oxidoreductase (CoA benzoylating), a new
            enzyme of anaerobic phenylalanine metabolism in the denitrifying
            bacterium Azoarcus evansii.
  JOURNAL   Eur. J. Biochem. 251 (1998) 907-15.
  ORGANISM  Azoarcus evansii
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.58
            ExPASy - ENZYME nomenclature database: 1.2.1.58
            ExplorEnz - The Enzyme Database: 1.2.1.58
            ERGO genome analysis and discovery system: 1.2.1.58
            BRENDA, the Enzyme Database: 1.2.1.58
            CAS: 205510-78-7
///
ENTRY       EC 1.2.1.59                 Enzyme
NAME        glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+)
            (phosphorylating);
            triosephosphate dehydrogenase (NAD(P));
            glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-glyceraldehyde 3-phosphate:NAD(P)+ oxidoreductase
            (phosphorylating)
REACTION    D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ =
            3-phospho-D-glyceroyl phosphate + NAD(P)H + H+ [RN:R01061 R01063]
ALL_REAC    R01061 R01063
SUBSTRATE   D-glyceraldehyde 3-phosphate [CPD:C00118];
            phosphate [CPD:C00009];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     3-phospho-D-glyceroyl phosphate [CPD:C00236];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     NAD+ and NADP+ can be used as cofactors with similar efficiency,
            unlike EC 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase
            (phosphorylating) and EC 1.2.1.13 glyceraldehyde-3-phosphate
            dehydrogenase (NADP+) (phosphorylating), which are NAD+- and
            NADP+-dependent, respectively.
REFERENCE   1
  AUTHORS   Valverde, F., Losada, M. and Serrano, A.
  TITLE     Cloning by functional complementation in E. coli of the gap2 gene of
            Synechocystis PCC 6803 supports an amphibolic role for
            cyanobacterial NAD(P)-dependent glyceraldehyde-3-phosphate
            dehydrogenase.
  JOURNAL   In: P. Mathis (Ed.), Photosynthesis: From Light to Biosphere, vol.
            1, Kluwer Academic Publishers, 1995, p. 959-962.
REFERENCE   2  [PMID:9226260]
  AUTHORS   Valverde F, Losada M, Serrano A.
  TITLE     Functional complementation of an Escherichia coli gap mutant
            supports an amphibolic role for NAD(P)-dependent
            glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain
            PCC 6803.
  JOURNAL   J. Bacteriol. 179 (1997) 4513-22.
  ORGANISM  Synechocystis sp.
ORTHOLOGY   KO: K00150  glyceraldehyde-3-phosphate dehydrogenase (NAD(P))
                        (phosphorylating)
GENES       FTU: FTT1368c(gapA)
            FTF: FTF1368c(gapA)
            AJS: Ajs_2165 Ajs_2680
            CCO: CCC13826_1508
            ERU: Erum0010(gapB)
            ERW: ERWE_CDS_09460(gap)
            ERG: ERGA_CDS_09370(gap)
            ECN: Ecaj_0939
            BCE: BC4583
            BTK: BT9727_4313(gap)
            BTL: BALH_4166(gap)
            BPU: BPUM_2547(gapB)
            SAB: SAB1546c(gap)
            SYN: sll1342(gap2)
            SYW: SYNW0030(gap2)
            SYC: syc2349_c(gap2)
            SYF: Synpcc7942_1742
            SYR: SynRCC307_0028(gap1)
            SYX: SynWH7803_0029(gap1)
            TER: Tery_4030
            MJA: MJ1146
            MMP: MMP0325
            MMQ: MmarC5_1348
            MMZ: MmarC7_1327
            MAE: Maeo_0627
            MVN: Mevan_1336
            MAC: MA1018(gap) MA3345(gap)
            MBA: Mbar_A2189 Mbar_A3564
            MMA: MM_2782
            MBU: Mbur_0851
            MHU: Mhun_2462
            MEM: Memar_2497
            MBN: Mboo_2454
            MTH: MTH1009
            MST: Msp_1346(gap)
            MKA: MK0618(gapA)
            AFU: AF1732(gap)
            HAL: VNG0095G(gapB)
            HMA: rrnAC2262(gapB)
            HWA: HQ1360A(gapB) HQ1394A(gapB) HQ2025A(gapB)
            NPH: NP0012A(gapB)
            TAC: Ta1103
            TVO: TVN0458
            PTO: PTO0742
            PHO: PH1830
            PAB: PAB0257(gap)
            PFU: PF1874
            TKO: TK0765
            RCI: RCIX551(gap)
            APE: APE_0171.1
            SMR: Smar_0241
            HBU: Hbut_0939
            SSO: SSO0528(gap)
            STO: ST1356
            SAI: Saci_1356
            MSE: Msed_1652
            PAI: PAE1740
            PIS: Pisl_1710
            PCL: Pcal_0632
            PAS: Pars_0743
            TPE: Tpen_1765
STRUCTURES  PDB: 2CZC  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.59
            ExPASy - ENZYME nomenclature database: 1.2.1.59
            ExplorEnz - The Enzyme Database: 1.2.1.59
            ERGO genome analysis and discovery system: 1.2.1.59
            BRENDA, the Enzyme Database: 1.2.1.59
            CAS: 39369-25-0
///
ENTRY       EC 1.2.1.60                 Enzyme
NAME        5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase;
            carboxymethylhydroxymuconic semialdehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     5-carboxymethyl-2-hydroxymuconic-semialdehyde:NAD+ oxidoreductase
REACTION    5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+ =
            5-carboxymethyl-2-hydroxymuconate + NADH + 2 H+ [RN:R04418]
ALL_REAC    R04418
SUBSTRATE   5-carboxymethyl-2-hydroxymuconate semialdehyde [CPD:C04642];
            H2O [CPD:C00001];
            NAD+ [CPD:C00003]
PRODUCT     5-carboxymethyl-2-hydroxymuconate [CPD:C04186];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Involved in the tyrosine degradation pathway in Arthrobacter sp.
REFERENCE   1  [PMID:20216]
  AUTHORS   Blakley ER.
  TITLE     The catabolism of L-tyrosine by an Arthrobacter sp.
  JOURNAL   Can. J. Microbiol. 23 (1977) 1128-39.
  ORGANISM  Arthrobacter sp.
REFERENCE   2  [PMID:6756482]
  AUTHORS   Alonso JM, Garrido-Pertierra A.
  TITLE     Carboxymethylhydroxymuconic semialdehyde dehydrogenase in the
            4-hydroxyphenylacetate catabolic pathway of Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 719 (1982) 165-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:6995433]
  AUTHORS   Cooper RA, Skinner MA.
  TITLE     Catabolism of 3- and 4-hydroxyphenylacetate by the
            3,4-dihydroxyphenylacetate pathway in Escherichia coli.
  JOURNAL   J. Bacteriol. 143 (1980) 302-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4
  AUTHORS   Garrido-Pertierra, A. and Cooper, R.A.
  TITLE     Identification and purification of distinct isomerase and
            decarboxylase enzymes involved in the 4-hydroxyphenylacetate pathway
            of Escherichia coli.
  JOURNAL   Eur. J. Biochem. 117 (1981) 581-584.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00350  Tyrosine metabolism
ORTHOLOGY   KO: K00151  5-carboxymethyl-2-hydroxymuconic-semialdehyde
                        dehydrogenase
GENES       ECX: EcHS_A4583(hpaE)
            SPT: SPA1748(hpaE)
            SEC: SC1052(hpaE)
            STM: STM1102(hpaE)
            YPE: YPO1763(hpaE)
            YPK: y2546(hpaE)
            YPM: YP_1630(hpaE)
            YPA: YPA_1135
            YPN: YPN_2360
            YPS: YPTB1639(hpaE)
            YPI: YpsIP31758_2363(hpaE)
            SFL: SF4383(hpaE)
            SFX: S4653(hpaE)
            SFV: SFV_4383(hpaE)
            SSN: SSON_4498(hpaE)
            SBO: SBO_4411(hpaE)
            PLU: plu0988(hpcC)
            PMU: PM1530(hpaE)
            VVY: VV1585
            PAE: PA4123(hpcC)
            PAU: PA14_10630(hpcC)
            PAP: PSPA7_0969(hpaE)
            PFL: PFL_3372(hpaE)
            PEN: PSEEN3094(hpaE)
            RSO: RSp0890(hpaE)
            REU: Reut_B5498
            RME: Rmet_5206
            BMA: BMAA1138(hpcE)
            BML: BMA10299_0102(hpaE)
            BMN: BMA10247_A1511(hpaE)
            BXE: Bxe_A1147(amnC) Bxe_B2030
            BPS: BPSS0694(hpcC)
            BPM: BURPS1710b_A2265(hpaE)
            BPL: BURPS1106A_A0940(hpaE)
            BPD: BURPS668_A1025(hpaE)
            BTE: BTH_II1733(hpaE)
            POL: Bpro_5132
            MPT: Mpe_A2275 Mpe_A3326 Mpe_A3328
            AZO: azo1852(lapC)
            DAR: Daro_2775 Daro_3787
            MES: Meso_2507
            BME: BMEII0135
            BMF: BAB2_1119
            BMS: BRA1161
            BMB: BruAb2_1097
            BOV: BOV_A1064(hpaE)
            BJA: bll2968(attK)
            RPA: RPA3760(hpcC)
            RPB: RPB_1706
            RPD: RPD_3591
            SIL: SPOA0027(hpcC)
            JAN: Jann_3503
            BLI: BL03906
            BLD: BLi03994
            OIH: OB2869
            GKA: GK3028
            MMC: Mmcs_2613
            NFA: nfa27770
            AAU: AAur_3915(hpaE) AAur_pTC20091(hpaE)
            DRA: DR_A0220
            TTH: TTC0593
            TTJ: TTHA0959 TTHB240
STRUCTURES  PDB: 2D4E  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.60
            ExPASy - ENZYME nomenclature database: 1.2.1.60
            ExplorEnz - The Enzyme Database: 1.2.1.60
            ERGO genome analysis and discovery system: 1.2.1.60
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.60
            BRENDA, the Enzyme Database: 1.2.1.60
///
ENTRY       EC 1.2.1.61                 Enzyme
NAME        4-hydroxymuconic-semialdehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4-hydroxymuconic-semialdehyde:NAD+ oxidoreductase
REACTION    4-hydroxymuconic semialdehyde + NAD+ + H2O = maleylacetate + NADH +
            2 H+ [RN:R05236]
ALL_REAC    R05236
SUBSTRATE   4-hydroxymuconic semialdehyde [CPD:C06603];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     maleylacetate [CPD:C02222];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Involved in the 4-nitrophenol degradation pathway.
REFERENCE   1  [PMID:16348446]
  AUTHORS   Spain JC, Gibson DT.
  TITLE     Pathway for Biodegradation of p-Nitrophenol in a Moraxella sp.
  JOURNAL   Appl. Environ. Microbiol. 57 (1991) 812-819.
  ORGANISM  Moraxella sp.
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.61
            ExPASy - ENZYME nomenclature database: 1.2.1.61
            ExplorEnz - The Enzyme Database: 1.2.1.61
            ERGO genome analysis and discovery system: 1.2.1.61
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.61
            BRENDA, the Enzyme Database: 1.2.1.61
///
ENTRY       EC 1.2.1.62                 Enzyme
NAME        4-formylbenzenesulfonate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4-formylbenzenesulfonate:NAD+ oxidoreductase
REACTION    4-formylbenzenesulfonate + NAD+ + H2O = 4-sulfobenzoate + NADH + 2
            H+ [RN:R05272]
ALL_REAC    R05272
SUBSTRATE   4-formylbenzenesulfonate [CPD:C06679];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     4-sulfobenzoate [CPD:C02236];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Involved in the toluene-4-sulfonate degradation pathway.
REFERENCE   1  [PMID:8828208]
  AUTHORS   Junker F, Saller E, Schlafli Oppenberg HR, Kroneck PM, Leisinger T,
            Cook AM.
  TITLE     Degradative pathways for p-toluenecarboxylate and p-toluenesulfonate
            and their multicomponent oxygenases in Comamonas testosteroni
            strains PSB-4 and T-2.
  JOURNAL   Microbiology. 142 ( Pt 9) (1996) 2419-27.
  ORGANISM  Comamonas testosteroni
REFERENCE   2  [PMID:9006050]
  AUTHORS   Junker F, Kiewitz R, Cook AM.
  TITLE     Characterization of the p-toluenesulfonate operon tsaMBCD and tsaR
            in Comamonas testosteroni T-2.
  JOURNAL   J. Bacteriol. 179 (1997) 919-27.
  ORGANISM  Comamonas testosteroni
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.62
            ExPASy - ENZYME nomenclature database: 1.2.1.62
            ExplorEnz - The Enzyme Database: 1.2.1.62
            ERGO genome analysis and discovery system: 1.2.1.62
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.62
            BRENDA, the Enzyme Database: 1.2.1.62
///
ENTRY       EC 1.2.1.63                 Enzyme
NAME        6-oxohexanoate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     6-oxohexanoate:NADP+ oxidoreductase
REACTION    6-oxohexanoate + NADP+ + H2O = adipate + NADPH + 2 H+ [RN:R05099]
ALL_REAC    R05099
SUBSTRATE   6-oxohexanoate [CPD:C06102];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     adipate [CPD:C06104];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Last step in the cyclohexanol degradation pathway in Acinetobacter
            sp.
REFERENCE   1  [PMID:856571]
  AUTHORS   Davey JF, Trudgill PW.
  TITLE     The metabolism of trans-cyclohexan-1,2-diol by an Acinetobacter
            species.
  JOURNAL   Eur. J. Biochem. 74 (1977) 115-27.
  ORGANISM  Acinetobacter sp.
REFERENCE   2  [PMID:1261]
  AUTHORS   Donoghue NA, Trudgill PW.
  TITLE     The metabolism of cyclohexanol by Acinetobacter NCIB 9871.
  JOURNAL   Eur. J. Biochem. 60 (1975) 1-7.
  ORGANISM  Nocardia globerula
PATHWAY     PATH: map00930  Caprolactam degradation
GENES       RHA: RHA1_ro10127(chnE)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.63
            ExPASy - ENZYME nomenclature database: 1.2.1.63
            ExplorEnz - The Enzyme Database: 1.2.1.63
            ERGO genome analysis and discovery system: 1.2.1.63
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.63
            BRENDA, the Enzyme Database: 1.2.1.63
///
ENTRY       EC 1.2.1.64                 Enzyme
NAME        4-hydroxybenzaldehyde dehydrogenase;
            p-hydroxybenzaldehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-hydroxybenzaldehyde:NAD+ oxidoreductase
REACTION    4-hydroxybenzaldehyde + NAD+ + H2O = 4-hydroxybenzoate + NADH + 2 H+
            [RN:R01293]
ALL_REAC    R01293;
            (other) R07667
SUBSTRATE   4-hydroxybenzaldehyde [CPD:C00633];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     4-hydroxybenzoate [CPD:C00156];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Involved in the toluene degradation pathway in Pseudomonas
            mendocina.
REFERENCE   1  [PMID:2722739]
  AUTHORS   Bossert ID, Whited G, Gibson DT, Young LY.
  TITLE     Anaerobic oxidation of p-cresol mediated by a partially purified
            methylhydroxylase from a denitrifying bacterium.
  JOURNAL   J. Bacteriol. 171 (1989) 2956-62.
REFERENCE   2  [PMID:2019564]
  AUTHORS   Whited GM, Gibson DT.
  TITLE     Separation and partial characterization of the enzymes of the
            toluene-4-monooxygenase catabolic pathway in Pseudomonas mendocina
            KR1.
  JOURNAL   J. Bacteriol. 173 (1991) 3017-20.
  ORGANISM  Pseudomonas mendocina
PATHWAY     PATH: map00622  Toluene and xylene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.64
            ExPASy - ENZYME nomenclature database: 1.2.1.64
            ExplorEnz - The Enzyme Database: 1.2.1.64
            ERGO genome analysis and discovery system: 1.2.1.64
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.64
            BRENDA, the Enzyme Database: 1.2.1.64
///
ENTRY       EC 1.2.1.65                 Enzyme
NAME        salicylaldehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     salicylaldehyde:NAD+ oxidoreductase
REACTION    salicylaldehyde + NAD+ + H2O = salicylate + NADH + 2 H+ [RN:R02941]
ALL_REAC    R02941
SUBSTRATE   salicylaldehyde [CPD:C06202];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     salicylate [CPD:C00805];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Involved in the naphthalene degradation pathway in some bacteria.
REFERENCE   1  [PMID:1447127]
  AUTHORS   Eaton RW, Chapman PJ.
  TITLE     Bacterial metabolism of naphthalene: construction and use of
            recombinant bacteria to study ring cleavage of
            1,2-dihydroxynaphthalene and subsequent reactions.
  JOURNAL   J. Bacteriol. 174 (1992) 7542-54.
  ORGANISM  Pseudomonas aeruginosa
PATHWAY     PATH: map00626  Naphthalene and anthracene degradation
ORTHOLOGY   KO: K00152  salicylaldehyde dehydrogenase
GENES       BUR: Bcep18194_A5913 Bcep18194_B0051
            BPL: BURPS1106A_A1068(vdh)
            RLE: pRL120487
            BME: BMEI1559 BMEI1560
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.65
            ExPASy - ENZYME nomenclature database: 1.2.1.65
            ExplorEnz - The Enzyme Database: 1.2.1.65
            ERGO genome analysis and discovery system: 1.2.1.65
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.65
            BRENDA, the Enzyme Database: 1.2.1.65
///
ENTRY       EC 1.2.1.66                 Enzyme
NAME        mycothiol-dependent formaldehyde dehydrogenase;
            NAD/factor-dependent formaldehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     formaldehyde:NAD+ oxidoreductase (mycothiol-formylating)
REACTION    formaldehyde + mycothiol + NAD+ = S-formylmycothiol + NADH + 2 H+
            [RN:R05307]
ALL_REAC    R05307
SUBSTRATE   formaldehyde [CPD:C00067];
            mycothiol [CPD:C06717];
            NAD+ [CPD:C00003]
PRODUCT     S-formylmycothiol [CPD:C06718];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The S-formylmycothiol formed hydrolyses to mycothiol and formate.
REFERENCE   1  [PMID:9202149]
  AUTHORS   Misset-Smits M, van Ophem PW, Sakuda S, Duine JA.
  TITLE     Mycothiol,
            1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)
            -D- myo-inositol, is the factor of NAD/factor-dependent formaldehyde
            dehydrogenase.
  JOURNAL   FEBS. Lett. 409 (1997) 221-2.
  ORGANISM  Amycolatopsis methanolica, Rhodococcus erythropolis
REFERENCE   2  [PMID:9346279]
  AUTHORS   Norin A, Van Ophem PW, Piersma SR, Persson B, Duine JA, Jornvall H.
  TITLE     Mycothiol-dependent formaldehyde dehydrogenase, a prokaryotic
            medium-chain dehydrogenase/reductase, phylogenetically links
            different eukaroytic alcohol dehydrogenases--primary structure,
            conformational modelling and functional correlations.
  JOURNAL   Eur. J. Biochem. 248 (1997) 282-9.
  ORGANISM  Amycolatopsis methanolica, Rhodococcus erythropolis
ORTHOLOGY   KO: K00153  NAD/factor-dependent formaldehyde dehydrogenase
GENES       RDE: RD1_3937
            MTU: Rv2259(adhE2)
            MTC: MT2320
            MBO: Mb2283(adhE2)
            MLE: ML1784(adhE2)
            MPA: MAP2008(adhE2)
            MSM: MSMEG_4340
            CGL: NCgl0313(cgl0319)
            CEF: CE0330
            NFA: nfa12230
            RHA: RHA1_ro02587
            SCO: SCO0741(3SC5B7.19c)
            SMA: SAV6953(adhA10)
            AAU: AAur_2317(adhE2)
            FAL: FRAAL2245
            SEN: SACE_3147 SACE_4443 SACE_4490 SACE_4513
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.66
            ExPASy - ENZYME nomenclature database: 1.2.1.66
            ExplorEnz - The Enzyme Database: 1.2.1.66
            ERGO genome analysis and discovery system: 1.2.1.66
            BRENDA, the Enzyme Database: 1.2.1.66
///
ENTRY       EC 1.2.1.67                 Enzyme
NAME        vanillin dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     vanillin:NAD+ oxidoreductase
REACTION    vanillin + NAD+ + H2O = vanillate + NADH + 2 H+ [RN:R05699]
ALL_REAC    R05699
SUBSTRATE   vanillin [CPD:C00755];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     vanillate [CPD:C06672];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:6870241]
  AUTHORS   Pometto AL 3rd, Crawford DL.
  TITLE     Whole-cell bioconversion of vanillin to vanillic acid by
            Streptomyces viridosporus.
  JOURNAL   Appl. Environ. Microbiol. 45 (1983) 1582-5.
  ORGANISM  Streptomyces viridosporus
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.67
            ExPASy - ENZYME nomenclature database: 1.2.1.67
            ExplorEnz - The Enzyme Database: 1.2.1.67
            ERGO genome analysis and discovery system: 1.2.1.67
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.1.67
            BRENDA, the Enzyme Database: 1.2.1.67
///
ENTRY       EC 1.2.1.68                 Enzyme
NAME        coniferyl-aldehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     coniferyl aldehyde:NAD(P)+ oxidoreductase
REACTION    coniferyl aldehyde + H2O + NAD(P)+ = ferulate + NAD(P)H + 2 H+
            [RN:R05700 R05701]
ALL_REAC    R05700 R05701
SUBSTRATE   coniferyl aldehyde [CPD:C02666];
            H2O [CPD:C00001];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     ferulate [CPD:C01494];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also oxidizes other aromatic aldehydes, but not aliphatic aldehydes.
REFERENCE   1  [PMID:9721273]
  AUTHORS   Achterholt S, Priefert H, Steinbuchel A.
  TITLE     Purification and characterization of the coniferyl aldehyde
            dehydrogenase from Pseudomonas sp. Strain HR199 and molecular
            characterization of the gene.
  JOURNAL   J. Bacteriol. 180 (1998) 4387-91.
  ORGANISM  Pseudomonas sp.
ORTHOLOGY   KO: K00154  coniferyl-aldehyde dehydrogenase
GENES       TET: TTHERM_01206390
            ECA: ECA3562(calB)
            VCH: VCA1067
            VVU: VV1_2147 VV2_0051
            VVY: VV2296 VVA0559
            VPA: VPA0761
            VFI: VF1681
            PPR: PBPRA0132
            PAE: PA0366
            PAU: PA14_04810
            PPU: PP_5120
            PST: PSPTO_0418
            PSB: Psyr_2579
            PSP: PSPPH_2732(calB)
            PFL: PFL_5865(calB)
            PFO: Pfl_5345
            PEN: PSEEN0293
            PAR: Psyc_1294
            PCR: Pcryo_1085
            ACI: ACIAD0503(calB)
            SON: SO_3683
            SDN: Sden_0975
            SFR: Sfri_0937
            SHN: Shewana3_3251
            CPS: CPS_0988 CPS_3428
            PHA: PSHAa2139 PSHAb0365
            LPN: lpg1381
            LPP: lpp1336
            HCH: HCH_01011
            AHA: AHA_1509
            REU: Reut_B4636
            RME: Rmet_5413
            BMA: BMA3273
            BUR: Bcep18194_A6421 Bcep18194_C6847 Bcep18194_C7472
            BCN: Bcen_2458
            BCH: Bcen2424_3072 Bcen2424_6041
            BAM: Bamb_3118
            BPS: BPSL0222(calB)
            BPM: BURPS1710b_0409(calB)
            BTE: BTH_I0192
            RFR: Rfer_0048
            MLO: mlr4051
            RLE: pRL120507(calB)
            BMF: BAB2_1019
            BMB: BruAb2_0998
            BJA: blr7884(calB)
            BRA: BRADO6419
            BBT: BBta_1214 BBta_6016(calB)
            RPA: RPA1687
            RPB: RPB_3846
            RPC: RPC_3791
            RPD: RPD_1503
            RPE: RPE_3914
            CCR: CC_1849
            MMR: Mmar10_1636
            HNE: HNE_2803(calB)
            GOX: GOX2376
            MSM: MSMEG_2242
            MMC: Mmcs_1784
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.68
            ExPASy - ENZYME nomenclature database: 1.2.1.68
            ExplorEnz - The Enzyme Database: 1.2.1.68
            ERGO genome analysis and discovery system: 1.2.1.68
            BRENDA, the Enzyme Database: 1.2.1.68
///
ENTRY       EC 1.2.1.69                 Enzyme
NAME        fluoroacetaldehyde dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     fluoroacetaldehyde:NAD+ oxidoreductase
REACTION    fluoroacetaldehyde + NAD+ + H2O = fluoroacetate + NADH + 2 H+
            [RN:R07156]
ALL_REAC    R07156
SUBSTRATE   fluoroacetaldehyde [CPD:C15488];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     fluoroacetate [CPD:C06108];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The enzyme from Streptomyces cattleya has a high affinity for
            fluoroacetate and glycolaldehyde but not for acetaldehyde.
REFERENCE   1  [PMID:11571203]
  AUTHORS   Murphy CD, Moss SJ, O'Hagan D.
  TITLE     Isolation of an aldehyde dehydrogenase involved in the oxidation of
            fluoroacetaldehyde to fluoroacetate in Streptomyces cattleya.
  JOURNAL   Appl. Environ. Microbiol. 67 (2001) 4919-21.
  ORGANISM  Streptomyces cattleya
REFERENCE   2  [PMID:12738270]
  AUTHORS   Murphy CD, Schaffrath C, O'Hagan D.
  TITLE     Fluorinated natural products: the biosynthesis of fluoroacetate and
            4-fluorothreonine in Streptomyces cattleya.
  JOURNAL   Chemosphere. 52 (2003) 455-61.
  ORGANISM  Streptomyces cattleya
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.69
            ExPASy - ENZYME nomenclature database: 1.2.1.69
            ExplorEnz - The Enzyme Database: 1.2.1.69
            ERGO genome analysis and discovery system: 1.2.1.69
            BRENDA, the Enzyme Database: 1.2.1.69
///
ENTRY       EC 1.2.1.70                 Enzyme
NAME        glutamyl-tRNA reductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-glutamate-semialdehyde: NADP+ oxidoreductase
            (L-glutamyl-tRNAGlu-forming)
REACTION    L-glutamate 1-semialdehyde + NADP+ + tRNAGlu = L-glutamyl-tRNAGlu +
            NADPH + H+ [RN:R04109]
ALL_REAC    R04109
SUBSTRATE   L-glutamate 1-semialdehyde [CPD:C03741];
            NADP+ [CPD:C00006];
            tRNA(Glu) [CPD:C01641]
PRODUCT     L-glutamyl-tRNA(Glu) [CPD:C02987];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     This enzyme forms part of the pathway for the biosynthesis of
            5-aminolevulinate from glutamate, known as the C5 pathway. The route
            shown in the diagram is used in most eubacteria, and in all
            archaebacteria, algae and plants. However, in the
            alpha-proteobacteria, EC 2.3.1.37, 5-aminolevulinate synthase, is
            used in an alternative route to produce the product
            5-aminolevulinate from succinyl-CoA and glycine. This route is found
            in the mitochondria of fungi and animals, organelles that are
            considered to be derived from an endosymbiotic
            alpha-proteobacterium. Although higher plants do not possess EC
            2.3.1.37, the protistan Euglena gracilis possesses both the C5
            pathway and EC 2.3.1.37.
REFERENCE   1  [PMID:12242396]
  AUTHORS   Von Wettstein D, Gough S, Kannangara CG.
  TITLE     Chlorophyll Biosynthesis.
  JOURNAL   Plant. Cell. 7 (1995) 1039-1057.
  ORGANISM  Escherichia coli [GN:eco], Salmonella typhinurium, Bacillus subtilis
            [GN:bsu], Synechocystis sp., Arabidopsis sp., Clostridium josni,
            Hordeum vulgare [GN:ehvu]
REFERENCE   2  [PMID:7957167]
  AUTHORS   Pontoppidan B, Kannangara CG.
  TITLE     Purification and partial characterisation of barley
            glutamyl-tRNA(Glu) reductase, the enzyme that directs glutamate to
            chlorophyll biosynthesis.
  JOURNAL   Eur. J. Biochem. 225 (1994) 529-37.
  ORGANISM  Escherichia coli [GN:eco], Synechocystis sp., Hordeum vulgare
            [GN:ehvu], Chlamydomonas reinhardtii
REFERENCE   3  [PMID:12370189]
  AUTHORS   Schauer S, Chaturvedi S, Randau L, Moser J, Kitabatake M, Lorenz S,
            Verkamp E, Schubert WD, Nakayashiki T, Murai M, Wall K, Thomann HU,
            Heinz DW, Inokuchi H, Soll D, Jahn D.
  TITLE     Escherichia coli glutamyl-tRNA reductase. Trapping the thioester
            intermediate.
  JOURNAL   J. Biol. Chem. 277 (2002) 48657-63.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K02492  glutamyl-tRNA reductase
GENES       ATH: AT1G09940(HEMA2) AT1G58290(HEMA1) AT2G31250(HEMA3)
            OSA: 4349044
            CME: CMJ054C
            ECO: b1210(hemA)
            ECJ: JW1201(hemA)
            ECE: Z1981(hemA)
            ECS: ECs1715
            ECC: c1668(hemA)
            ECI: UTI89_C1404(hemA)
            ECP: ECP_1258
            ECV: APECO1_327(hemA)
            ECX: EcHS_A1315(hemA)
            STY: STY1902(hemA)
            STT: t1099(hemA)
            SPT: SPA1096(hemA)
            SEC: SC1771(hemA)
            STM: STM1777(hemA)
            YPE: YPO2016(hemA)
            YPK: y2291(hemA)
            YPM: YP_1864(hemA)
            YPA: YPA_1400
            YPN: YPN_1498
            YPP: YPDSF_1102
            YPS: YPTB2004(hemA)
            YPI: YpsIP31758_2067(hemA)
            SFL: SF1213(hemA)
            SFX: S1297(hemA)
            SFV: SFV_1224(hemA)
            SSN: SSON_1968(hemA)
            SBO: SBO_1857(hemA)
            SDY: SDY_1259(hemA)
            ECA: ECA2189(hemA)
            PLU: plu2069(hemA)
            WBR: WGLp346(hemA)
            SGL: SG1877
            SPE: Spro_1989
            HSO: HS_0810(hemA)
            PMU: PM0684(gltX_1)
            MSU: MS1324(hemA)
            APL: APL_0404(hemA)
            ASU: Asuc_1116
            XFA: XF2648
            XFT: PD2021(hemA)
            XCC: XCC0868(hemA)
            XCB: XC_3362
            XCV: XCV0976(hemA)
            XAC: XAC0945(hemA)
            XOO: XOO3607(hemA)
            XOM: XOO_3409(XOO3409)
            VCH: VC2180
            VVU: VV1_0254
            VVY: VV0930
            VPA: VP0742
            VFI: VF0767
            PPR: PBPRA2846
            PAE: PA4666(hemA)
            PAU: PA14_61710(hemA)
            PAP: PSPA7_5315(hemA)
            PPU: PP_0732(hemA)
            PPF: Pput_0760
            PST: PSPTO_1108(hemA)
            PSB: Psyr_0948
            PSP: PSPPH_0996(hemA)
            PFL: PFL_5160(hemA)
            PFO: Pfl_4749
            PEN: PSEEN0875(hemA)
            PMY: Pmen_1059
            PAR: Psyc_0176(hemA)
            PCR: Pcryo_0189
            PRW: PsycPRwf_0311
            ACI: ACIAD2900(hemA)
            SON: SO_3834(hemA)
            SDN: Sden_0919
            SFR: Sfri_0722
            SAZ: Sama_2567
            SBL: Sbal_0695
            SBM: Shew185_3615
            SLO: Shew_2913
            SSE: Ssed_3460
            SPL: Spea_3127
            SHE: Shewmr4_3170
            SHM: Shewmr7_0796
            SHN: Shewana3_0768
            SHW: Sputw3181_3375
            ILO: IL0926(hemA)
            CPS: CPS_3554(hemA)
            PHA: PSHAa1057(hemA)
            PAT: Patl_2564
            SDE: Sde_3252
            PIN: Ping_1606
            MAQ: Maqu_2361
            CBU: CBU_1966(hemA)
            CBD: COXBU7E912_2065(hemA)
            LPN: lpg2335(hemA)
            LPF: lpl2256(hemA)
            LPP: lpp2283(hemA)
            MCA: MCA1052(hemA)
            FTU: FTT0167(hemA)
            FTF: FTF0167(hemA)
            FTW: FTW_0258(hemA)
            FTL: FTL_1722
            FTH: FTH_1661(hemA)
            FTN: FTN_1546(hemA)
            TCX: Tcr_0390
            NOC: Noc_0510
            AEH: Mlg_0279
            HHA: Hhal_0993
            HCH: HCH_01731(hemA)
            CSA: Csal_1528
            ABO: ABO_0522(hemA)
            MMW: Mmwyl1_3600
            AHA: AHA_3150(hemA)
            DNO: DNO_0069(hemA)
            VOK: COSY_0675(hemA)
            NME: NMB0576
            NMA: NMA0760(hemA)
            NMC: NMC0518(hemA)
            NGO: NGO1403(hemA)
            CVI: CV_0079(hemA)
            RSO: RSc2900(hemA)
            REU: Reut_A3043
            REH: H16_A3339(hemA)
            RME: Rmet_3200
            BMA: BMAA0505(hemA)
            BMV: BMASAVP1_0675(hemA)
            BML: BMA10299_0971(hemA)
            BMN: BMA10247_A1942(hemA)
            BXE: Bxe_A0437
            BUR: Bcep18194_A3598(hemA)
            BCN: Bcen_2593
            BCH: Bcen2424_0511
            BAM: Bamb_0415
            BPS: BPSL3072(hemA)
            BPM: BURPS1710b_3600(hemA)
            BPL: BURPS1106A_3613(hemA)
            BPD: BURPS668_3589(hemA)
            BTE: BTH_I2929(hemA)
            PNU: Pnuc_0137
            BPE: BP0677(hemA)
            BPA: BPP0381(hemA)
            BBR: BB0383(hemA)
            RFR: Rfer_1281
            POL: Bpro_0851
            PNA: Pnap_0776
            AAV: Aave_3663
            AJS: Ajs_0852
            VEI: Veis_1553
            MPT: Mpe_A0524
            HAR: HEAR0186(hemA)
            NEU: NE1914(hemA)
            NET: Neut_0826
            NMU: Nmul_A2642
            EBA: ebA1179(hemA)
            DAR: Daro_3689
            TBD: Tbd_2492
            MFA: Mfla_2473
            HPY: HP0239(hemA)
            HPJ: jhp0224(hemA)
            HPA: HPAG1_0242
            HHE: HH1725(hemA)
            HAC: Hac_1379(hemA)
            WSU: WS1581(hemA)
            TDN: Tmden_0859
            CJE: Cj0542(hemA)
            CJR: CJE0646(hemA)
            CJU: C8J_0503(hemA)
            CFF: CFF8240_0688(hemA)
            CCV: CCV52592_0764(hemA) CCV52592_1591
            CHA: CHAB381_0896(hemA)
            CCO: CCC13826_1051(hemA)
            NIS: NIS_1024(hemA)
            SUN: SUN_0638(hemA)
            GSU: GSU3284(hemA)
            GME: Gmet_3233
            GUR: Gura_0360
            PCA: Pcar_3064
            DVU: DVU1461(hemA)
            DDE: Dde_2025
            LIP: LI0322(hemA)
            BBA: Bd3446(hemA)
            DPS: DP3079
            ADE: Adeh_2493
            AFW: Anae109_1374 Anae109_1845
            MXA: MXAN_2655(hemA)
            SAT: SYN_02274
            SFU: Sfum_1590
            RRU: Rru_A0749
            MAG: amb1617
            MGM: Mmc1_3644
            BSU: BG10340(hemA)
            BHA: BH3048(hemA)
            BAN: BA4698(hemA)
            BAR: GBAA4698(hemA)
            BAA: BA_5137(glutR)
            BAT: BAS4363
            BCE: BC4473
            BCA: BCE_4557(hemA)
            BCZ: BCZK4210(hemA)
            BCY: Bcer98_3182
            BTK: BT9727_4199(hemA)
            BTL: BALH_4059(hemA)
            BLI: BL00623(hemA)
            BLD: BLi02947(hemA)
            BCL: ABC2632(hemA)
            BPU: BPUM_2458(hemA)
            OIH: OB2070(hemA)
            GKA: GK2647
            SAU: SA1496(hemA)
            SAV: SAV1672(hemA)
            SAM: MW1616(hemA)
            SAR: SAR1752(hemA)
            SAS: SAS1601
            SAC: SACOL1719(hemA)
            SAB: SAB1532c(hemA)
            SAO: SAOUHSC_01776
            SAJ: SaurJH9_1730
            SAH: SaurJH1_1764
            SEP: SE1347
            SER: SERP1236(hemA)
            SHA: SH1255(hemA)
            SSP: SSP1092
            LMO: lmo1557(hemA)
            LMF: LMOf2365_1578(hemA)
            LIN: lin1592(hemA)
            LWE: lwe1570(hemA)
            SSA: SSA_0484
            LRE: Lreu_1703
            CAC: CAC0095(hemA)
            CPE: CPE1437(hemA)
            CPF: CPF_1690(hemA)
            CPR: CPR_1424(hemA)
            CTC: CTC00725
            CNO: NT01CX_0264(hemA)
            CBE: Cbei_1283
            CKL: CKL_0657(hemA)
            AMT: Amet_0058
            CHY: CHY_1207(hemA)
            DSY: DSY2226
            CSC: Csac_1649
            MTA: Moth_1250
            MTU: Rv0509(hemA)
            MTC: MT0530(hemA)
            MBO: Mb0521(hemA)
            MLE: ML2422(hemA)
            MPA: MAP4002(hemA)
            MAV: MAV_4640(hemA)
            MSM: MSMEG_0952(hemA)
            MMC: Mmcs_0676
            CGL: NCgl0402(cgl0417)
            CGB: cg0497(hemA)
            CEF: CE0435
            CDI: DIP0400
            CJK: jk1902(hemA)
            NFA: nfa51700(hemA)
            RHA: RHA1_ro02053
            SCO: SCO3319(SCE68.17c)
            SMA: SAV4739(hemA)
            TWH: TWT736(hemA)
            TWS: TW750(hemA)
            LXX: Lxx01050(hemA)
            PAC: PPA0307
            TFU: Tfu_2733
            FRA: Francci3_0485
            FAL: FRAAL0983(hemA)
            ACE: Acel_0238
            KRA: Krad_0617
            SEN: SACE_6946(hemA)
            STP: Strop_0356
            FNU: FN0646
            RBA: RB9848(hemA)
            CTR: CT662(hemA)
            CTA: CTA_0719(hemA)
            CMU: TC0033
            CPN: CPn0714(hemA)
            CPA: CP0032
            CPJ: CPj0714(hemA)
            CPT: CpB0741
            CCA: CCA00028
            CAB: CAB028
            CFE: CF0977(hemA)
            PCU: pc0347(hemA)
            LIL: LB010(hemA)
            LIC: LIC20008(hemA)
            LBJ: LBJ_4008(hemA)
            LBL: LBL_4008(hemA)
            SYN: slr1808(hemA)
            SYW: SYNW1117(hemA)
            SYC: syc1016_d(hemA)
            SYF: Synpcc7942_0504
            SYD: Syncc9605_1254
            SYE: Syncc9902_1228
            SYG: sync_1686(hemA)
            SYR: SynRCC307_1254(hemA)
            SYX: SynWH7803_1299(hemA)
            CYA: CYA_0543(hemA)
            CYB: CYB_2258(hemA)
            TEL: tll1738(hemA)
            GVI: glr1218(hemA)
            ANA: alr1042(hemA)
            AVA: Ava_3699
            PMA: Pro0841(hemA)
            PMM: PMM0768(hemA)
            PMT: PMT0567(hemA)
            PMN: PMN2A_0174
            PMB: A9601_08301(hemA)
            PMC: P9515_08151(hemA)
            PMF: P9303_16841(hemA)
            PMG: P9301_08281(hemA)
            PMH: P9215_08621(hemA)
            PME: NATL1_08061(hemA)
            TER: Tery_0949
            SRU: SRU_1555(hemA)
            CHU: CHU_0333(hemA)
            FJO: Fjoh_0942 Fjoh_3752
            FPS: FP0044(hemA)
            CTE: CT1426(hemA)
            CCH: Cag_1516
            PLT: Plut_1426
            RRS: RoseRS_1746
            RCA: Rcas_2026
            DRA: DR_2547
            DGE: Dgeo_2128
            TTH: TTC1142
            TTJ: TTHA1506
            AAE: aq_1279(hemA)
            TME: Tmel_0706
            MJA: MJ0143(hemA)
            MMP: MMP0088(gtrA)
            MMZ: MmarC7_1087
            MAE: Maeo_0052
            MVN: Mevan_1100
            MAC: MA0577(hemA)
            MBA: Mbar_A1462
            MMA: MM_1741
            MBU: Mbur_1229
            MHU: Mhun_2562
            MTH: MTH1012(hemA)
            MSI: Msm_0967
            MKA: MK0200(hemA)
            AFU: AF1975(hemA)
            HAL: VNG1774G(hemA)
            HMA: rrnAC1708(hemA)
            HWA: HQ3336A(hemA)
            NPH: NP4502A(hemA)
            TAC: Ta0536
            TVO: TVN0590
            PTO: PTO0918
            RCI: RCIX911(hemA)
            APE: APE_2296
            IHO: Igni_0512
            SSO: SSO0180
            STO: ST0212
            SAI: Saci_0777(gluTR)
            MSE: Msed_0214
            PAI: PAE0601(hemA)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.70
            ExPASy - ENZYME nomenclature database: 1.2.1.70
            ExplorEnz - The Enzyme Database: 1.2.1.70
            ERGO genome analysis and discovery system: 1.2.1.70
            BRENDA, the Enzyme Database: 1.2.1.70
///
ENTRY       EC 1.2.1.71                 Enzyme
NAME        succinylglutamate-semialdehyde dehydrogenase;
            succinylglutamic semialdehyde dehydrogenase;
            N-succinylglutamate 5-semialdehyde dehydrogenase;
            SGSD;
            AruD;
            AstD
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N-succinyl-L-glutamate 5-semialdehyde:NAD+ oxidoreductase
REACTION    N-succinyl-L-glutamate 5-semialdehyde + NAD+ + H2O =
            N-succinyl-L-glutamate + NADH + 2 H+ [RN:R05049]
ALL_REAC    R05049
SUBSTRATE   N-succinyl-L-glutamate 5-semialdehyde [CPD:C05932];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     N-succinyl-L-glutamate [CPD:C05931];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     This is the fourth enzyme in the arginine succinyltransferase (AST)
            pathway for the catabolism of arginine [1]. This pathway converts
            the carbon skeleton of arginine into glutamate, with the concomitant
            production of ammonia and conversion of succinyl-CoA into succinate
            and CoA. The five enzymes involved in this pathway are EC 2.3.1.109
            (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine
            dihydrolase), EC 2.6.1.11 (acetylornithine transaminase), EC
            1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC
            3.5.1.96 (succinylglutamate desuccinylase) [3,6].
REFERENCE   1  [PMID:3144259]
  AUTHORS   Vander Wauven C, Jann A, Haas D, Leisinger T, Stalon V.
  TITLE     N2-succinylornithine in ornithine catabolism of Pseudomonas
            aeruginosa.
  JOURNAL   Arch. Microbiol. 150 (1988) 400-4.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   2  [PMID:2865249]
  AUTHORS   Vander Wauven C, Stalon V.
  TITLE     Occurrence of succinyl derivatives in the catabolism of arginine in
            Pseudomonas cepacia.
  JOURNAL   J. Bacteriol. 164 (1985) 882-6.
  ORGANISM  Pseudomonas cepacia
REFERENCE   3  [PMID:7523119]
  AUTHORS   Tricot C, Vander Wauven C, Wattiez R, Falmagne P, Stalon V.
  TITLE     Purification and properties of a succinyltransferase from
            Pseudomonas aeruginosa specific for both arginine and ornithine.
  JOURNAL   Eur. J. Biochem. 224 (1994) 853-61.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   4  [PMID:9393691]
  AUTHORS   Itoh Y.
  TITLE     Cloning and characterization of the aru genes encoding enzymes of
            the catabolic arginine succinyltransferase pathway in Pseudomonas
            aeruginosa.
  JOURNAL   J. Bacteriol. 179 (1997) 7280-90.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   5  [PMID:9696779]
  AUTHORS   Schneider BL, Kiupakis AK, Reitzer LJ.
  TITLE     Arginine catabolism and the arginine succinyltransferase pathway in
            Escherichia coli.
  JOURNAL   J. Bacteriol. 180 (1998) 4278-86.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:3534538]
  AUTHORS   Cunin R, Glansdorff N, Pierard A, Stalon V.
  TITLE     Biosynthesis and metabolism of arginine in bacteria.
  JOURNAL   Microbiol. Rev. 50 (1986) 314-52.
  ORGANISM  Pseudomonas cepacia
REFERENCE   7
  AUTHORS   Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V.
  TITLE     Erratum report: Biosynthesis and metabolism of arginine in bacteria.
  JOURNAL   Microbiol. Rev. 51 (1987) 178.
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K06447  succinylglutamic semialdehyde dehydrogenase
GENES       ECO: b1746(astD)
            ECJ: JW5282(astD)
            ECE: Z2778
            ECS: ECs2452
            ECC: c2146
            ECI: UTI89_C1941
            ECP: ECP_1692
            ECV: APECO1_815(thrL)
            ECW: EcE24377A_1968(astD)
            ECX: EcHS_A1829
            STY: STY1809(astD)
            STT: t1184(astD)
            SPT: SPA1539(astD)
            STM: STM1305(astD)
            YPE: YPO1964(astD)
            YPK: y2347
            YPM: YP_1709(astD)
            YPA: YPA_1346
            YPS: YPTB1961(astD)
            SFX: S1597
            SFV: SFV_1474
            SBO: SBO_1344
            SDY: SDY_1531
            PLU: plu3108(astD)
            VCH: VC2616
            VVU: VV1_1315
            VVY: VV3052
            VPA: VP2795
            VFI: VF2282
            PPR: PBPRA0291(astD)
            PAE: PA0898(aruD)
            PAU: PA14_52670(aruD)
            PAP: PSPA7_4617(astD)
            PPU: PP_4478(aruD)
            PST: PSPTO_1835(astD)
            PSB: Psyr_3562
            PSP: PSPPH_3518(astD)
            PFL: PFL_4512(astD)
            PFO: Pfl_4282
            PEN: PSEEN3879(aruD)
            ACI: ACIAD1287(astD)
            SON: SO_0619(astD)
            SDN: Sden_1056 Sden_3191
            SHN: Shewana3_0612
            ILO: IL2316
            CPS: CPS_0634(astD)
            PHA: PSHAa0196(astD) PSHAb0426
            PAT: Patl_0649
            LPN: lpg1707(aruD)
            LPF: lpl1666(astD)
            LPP: lpp1672(astD)
            HCH: HCH_01950(aruD)
            CSA: Csal_2805
            AHA: AHA_3178
            CVI: CV_1499(aruD)
            BMA: BMA0594(astD)
            BUR: Bcep18194_A4294
            BAM: Bamb_1064
            BPS: BPSL2387(astD)
            BPM: BURPS1710b_2843(astD)
            BPL: BURPS1106A_2782(astD)
            BTE: BTH_I1778
            BBA: Bd0131(astD)
            CCR: CC_0582
            ZMO: ZMO1272(astD)
            NAR: Saro_0939
            SAL: Sala_0773
            ELI: ELI_02870
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.71
            ExPASy - ENZYME nomenclature database: 1.2.1.71
            ExplorEnz - The Enzyme Database: 1.2.1.71
            ERGO genome analysis and discovery system: 1.2.1.71
            BRENDA, the Enzyme Database: 1.2.1.71
///
ENTRY       EC 1.2.1.72                 Enzyme
NAME        erythrose-4-phosphate dehydrogenase;
            erythrose 4-phosphate dehydrogenase;
            E4PDH;
            GapB;
            Epd dehydrogenase;
            E4P dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     D-erythrose 4-phosphate:NAD+ oxidoreductase
REACTION    D-erythrose 4-phosphate + NAD+ + H2O = 4-phosphoerythronat + NADH +
            2 H+ [RN:R01825]
ALL_REAC    R01825
SUBSTRATE   D-erythrose 4-phosphate [CPD:C00279];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     4-phosphoerythronat;
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     This enzyme was originally thought to be a
            glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12), but this has
            since been disproved, as glyceraldehyde 3-phosphate is not a
            substrate [1,2]. Forms part of the pyridoxal-5'-phosphate coenzyme
            biosynthesis pathway in Escherichia coli, along with EC 1.1.1.290
            (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine
            transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate
            dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and
            EC 1.4.3.5 (pyridoxamine-phosphate oxidase).
REFERENCE   1  [PMID:7751290]
  AUTHORS   Zhao G, Pease AJ, Bharani N, Winkler ME.
  TITLE     Biochemical characterization of gapB-encoded erythrose 4-phosphate
            dehydrogenase of Escherichia coli K-12 and its possible role in
            pyridoxal 5'-phosphate biosynthesis.
  JOURNAL   J. Bacteriol. 177 (1995) 2804-12.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:9182530]
  AUTHORS   Boschi-Muller S, Azza S, Pollastro D, Corbier C, Branlant G.
  TITLE     Comparative enzymatic properties of GapB-encoded
            erythrose-4-phosphate dehydrogenase of Escherichia coli and
            phosphorylating glyceraldehyde-3-phosphate dehydrogenase.
  JOURNAL   J. Biol. Chem. 272 (1997) 15106-12.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:9696782]
  AUTHORS   Yang Y, Zhao G, Man TK, Winkler ME.
  TITLE     Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in
            pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli
            K-12.
  JOURNAL   J. Bacteriol. 180 (1998) 4294-9.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00750  Vitamin B6 metabolism
ORTHOLOGY   KO: K03472  D-erythrose 4-phosphate dehydrogenase
GENES       ECO: b2927(epd)
            ECJ: JW2894(epd)
            ECE: Z4266(epd)
            ECS: ECs3798
            ECC: c3505(epd)
            ECI: UTI89_C3310(epd)
            ECP: ECP_2916
            ECV: APECO1_3606(epd)
            STY: STY3228(epd)
            STT: t2989(epd)
            SPT: SPA2941(epd)
            SEC: SC3012(epd)
            STM: STM3070(epd)
            YPE: YPO0922(epd)
            YPK: y3309(epd)
            YPM: YP_3518(epd)
            YPA: YPA_0342
            YPN: YPN_3121
            YPS: YPTB3197(epd)
            SFL: SF2912(epd)
            SFX: S3112(epd)
            SFV: SFV_2973(epd)
            SSN: SSON_3079(epd)
            SBO: SBO_3066(epd)
            SDY: SDY_3155(epd)
            ECA: ECA3913(epd)
            PLU: plu0955(epd)
            VCH: VC0476
            VVU: VV1_1539
            VVY: VV2859
            VPA: VP2601
            VFI: VF0441
            PPR: PBPRA3132
            PAE: PA0551(epd)
            PAU: PA14_07170(epd)
            PPU: PP_4964(epd)
            PST: PSPTO_0386(epd)
            PSB: Psyr_4791
            PSP: PSPPH_4820(epd)
            PFL: PFL_5785(epd)
            PFO: Pfl_5266
            PEN: PSEEN5023(epd)
            SON: SO_0931(epd)
            ILO: IL2213(epd)
            CPS: CPS_3873(epd)
            PHA: PSHAa0594(epd)
            PAT: Patl_3329
            AHA: AHA_0780(epd)
            EBA: ebA6546(epd)
            DAR: Daro_3593
            DPS: DP1972
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.1.72
            ExPASy - ENZYME nomenclature database: 1.2.1.72
            ExplorEnz - The Enzyme Database: 1.2.1.72
            ERGO genome analysis and discovery system: 1.2.1.72
            BRENDA, the Enzyme Database: 1.2.1.72
///
ENTRY       EC 1.2.1.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With NAD+ or NADP+ as acceptor
REACTION    (1) Salicylaldehyde + NAD+ + H2O <=> Salicylate + NADH + H+
            [RN:R02941];
            (2) (R)-Mandelate + NAD+ <=> alpha-Oxo-benzeneacetic acid + NADH +
            H+ [RN:R03790];
            (3) 5-(2'-Formylethyl)-4,6-dihydroxypicolinate + NAD+ + H2O <=>
            5-(2'-Carboxyethyl)-4,6-dihydroxypicolinate + NADH + H+ [RN:R04916];
            (4) 5-(2'-Formylethyl)-4,6-dihydroxypicolinate + NADP+ + H2O <=>
            5-(2'-Carboxyethyl)-4,6-dihydroxypicolinate + NADPH + H+
            [RN:R04917];
            (5) 2-Carboxybenzaldehyde + NAD+ + H2O <=> Phthalate + NADH + H+
            [RN:R05643];
            (6) 1-Hydroxy-2-naphthaldehyde + NAD+ + H2O <=>
            1-Hydroxy-2-naphthoate + NADH + H+ [RN:R05649];
            (7) Coniferyl aldehyde + H2O + NAD+ <=> Ferulate + NADH + H+
            [RN:R05700];
            (8) Coniferyl aldehyde + H2O + NADP+ <=> Ferulate + NADPH + H+
            [RN:R05701];
            (9) (Z)-2-Methyl-5-isopropylhexa-2,5-dienal + NAD+ + H2O <=>
            cis-2-Methyl-5-isopropylhexa-2,5-dienoic acid + NADH + H+
            [RN:R06407];
            (10) trans-2-Methyl-5-isopropylhexa-2,5-dienal + NAD+ + H2O <=>
            trans-2-Methyl-5-isopropylhexa-2,5-dienoic acid + NADH + H+
            [RN:R06408];
            (11) N2-Acetyl-L-aminoadipyl-delta-phosphate + NADPH + H+ <=>
            N2-Acetyl-L-aminoadipate semialdehyde + NADP+ + Orthophosphate
            [RN:R06843];
            (12) 3-Methylsalicylaldehyde + NAD+ + H2O <=> 3-Methylsalicylate +
            NADH + H+ [RN:R06914];
            (13) 1-Naphthaldehyde + NAD+ + H2O <=> 1-Naphthoic acid + NADH + H+
            [RN:R06918];
            (14) 2-Naphthaldehyde + NAD+ + H2O <=> 2-Naphthoic acid + NADH + H+
            [RN:R06928];
            (15) 4-Hydroxymethylsalicylaldehyde + NAD+ + H2O <=>
            4-Hydroxymethylsalicylate + NADH + H+ [RN:R06935];
            (16) Sulfoacetaldehyde + NAD+ + H2O <=> Sulfoacetate + NADH + H+
            [RN:R06980];
            (17) gamma-Glutamyl-gamma-aminobutyraldehyde + NAD+ + H2O <=>
            gamma-Glutamyl-gamma-aminobutyraye + NADH + H+ [RN:R07417];
            (18) gamma-Glutamyl-gamma-aminobutyraldehyde + NADP+ + H2O <=>
            gamma-Glutamyl-gamma-aminobutyraye + NADPH + H+ [RN:R07418];
            (19) Sinapoyl aldehyde + NAD+ + H2O <=> Sinapate + NADH + H+
            [RN:R07441];
            (20) Sinapoyl aldehyde + NADP+ + H2O <=> Sinapate + NADPH + H+
            [RN:R07442]
SUBSTRATE   Salicylaldehyde [CPD:C06202];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001];
            (R)-Mandelate [CPD:C01983];
            5-(2'-Formylethyl)-4,6-dihydroxypicolinate [CPD:C05654];
            NADP+ [CPD:C00006];
            2-Carboxybenzaldehyde [CPD:C03057];
            1-Hydroxy-2-naphthaldehyde [CPD:C11427];
            (Z)-2-Methyl-5-isopropylhexa-2,5-dienal [CPD:C04435];
            trans-2-Methyl-5-isopropylhexa-2,5-dienal [CPD:C11942];
            N2-Acetyl-L-aminoadipyl-delta-phosphate [CPD:C12987];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            3-Methylsalicylaldehyde [CPD:C14087];
            1-Naphthaldehyde [CPD:C14090];
            2-Naphthaldehyde [CPD:C14099];
            4-Hydroxymethylsalicylaldehyde [CPD:C14108];
            Sulfoacetaldehyde [CPD:C00593];
            gamma-Glutamyl-gamma-aminobutyraldehyde [CPD:C15700]
PRODUCT     Salicylate [CPD:C00805];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            alpha-Oxo-benzeneacetic acid [CPD:C02137];
            5-(2'-Carboxyethyl)-4,6-dihydroxypicolinate [CPD:C05655];
            NADPH [CPD:C00005];
            Phthalate [CPD:C01606];
            1-Hydroxy-2-naphthoate [CPD:C03203];
            cis-2-Methyl-5-isopropylhexa-2,5-dienoic acid [CPD:C11944];
            trans-2-Methyl-5-isopropylhexa-2,5-dienoic acid [CPD:C11943];
            N2-Acetyl-L-aminoadipate semialdehyde [CPD:C12988];
            NADP+ [CPD:C00006];
            Orthophosphate [CPD:C00009];
            3-Methylsalicylate [CPD:C14088];
            1-Naphthoic acid [CPD:C14091];
            2-Naphthoic acid [CPD:C14101];
            4-Hydroxymethylsalicylate [CPD:C14109];
            Sulfoacetate [CPD:C14179];
            gamma-Glutamyl-gamma-aminobutyraye [CPD:C15767]
///
ENTRY       EC 1.2.2.1                  Enzyme
NAME        formate dehydrogenase (cytochrome);
            formate dehydrogenase;
            formate:cytochrome b1 oxidoreductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With a cytochrome as acceptor
SYSNAME     formate:ferricytochrome-b1 oxidoreductase
REACTION    formate + 2 ferricytochrome b1 = CO2 + 2 ferrocytochrome b1 + 2 H+
            [RN:R03146]
ALL_REAC    R03146
SUBSTRATE   formate [CPD:C00058];
            ferricytochrome b1 [CPD:C00995]
PRODUCT     CO2 [CPD:C00011];
            ferrocytochrome b1 [CPD:C00998];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Gale, E.F.
  TITLE     Formic dehydrogenase of Bacterium coli: its inactivation by oxygen
            and its protection in the bacterial cell.
  JOURNAL   Biochem. J. 33 (1939) 1012-1027.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K04509  formate dehydrogenase (cytochrome)
GENES       VFI: VF1357 VF1358 VF1359 VF1360
            SAT: SYN_00602 SYN_00603 SYN_00604 SYN_00605 SYN_00632 SYN_00633
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.2.1
            ExPASy - ENZYME nomenclature database: 1.2.2.1
            ExplorEnz - The Enzyme Database: 1.2.2.1
            ERGO genome analysis and discovery system: 1.2.2.1
            BRENDA, the Enzyme Database: 1.2.2.1
///
ENTRY       EC 1.2.2.2                  Enzyme
NAME        pyruvate dehydrogenase (cytochrome);
            pyruvate dehydrogenase;
            pyruvic dehydrogenase;
            pyruvic (cytochrome b1) dehydrogenase;
            pyruvate:ubiquinone-8-oxidoreductase;
            pyruvate oxidase (ambiguous)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With a cytochrome as acceptor
SYSNAME     pyruvate:ferricytochrome-b1 oxidoreductase
REACTION    pyruvate + ferricytochrome b1 + H2O = acetate + CO2 +
            ferrocytochrome b1 [RN:R03145]
ALL_REAC    R03145
SUBSTRATE   pyruvate [CPD:C00022];
            ferricytochrome b1 [CPD:C00995];
            H2O [CPD:C00001]
PRODUCT     acetate [CPD:C00033];
            CO2 [CPD:C00011];
            ferrocytochrome b1 [CPD:C00998]
COFACTOR    FAD [CPD:C00016];
            Thiamin diphosphate [CPD:C00068]
COMMENT     A flavoprotein requiring thiamine diphosphate.
REFERENCE   1
  AUTHORS   Williams, F.R. and Hager, L.P.
  TITLE     A crystalline flavin pyruvate oxidase.
  JOURNAL   J. Biol. Chem. 236 (1961) PC36-PC37.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:7042705]
  AUTHORS   Koland JG, Gennis RB.
  TITLE     Identification of an active site cysteine residue in Escherichia
            coli pyruvate oxidase.
  JOURNAL   J. Biol. Chem. 257 (1982) 6023-7.
PATHWAY     PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K00156  pyruvate dehydrogenase (cytochrome)
GENES       ECO: b0871(poxB)
            ECJ: JW0855(poxB)
            ECE: Z1105(poxB)
            ECS: ECs0957
            ECC: c1004(poxB)
            ECI: UTI89_C0874(poxB)
            ECP: ECP_0886
            ECV: APECO1_1223(poxB)
            ECW: EcE24377A_0944(poxB)
            ECX: EcHS_A0975
            STY: STY0931(poxB)
            STT: t1998(poxB)
            SPT: SPA1864(poxB)
            SEC: SC0890(poxB)
            STM: STM0935(poxB)
            YPE: YPO1358(poxB)
            YPK: y2821(poxB)
            YPM: YP_1237(poxB)
            YPA: YPA_0647
            YPN: YPN_2623
            YPS: YPTB1384(poxB)
            YPI: YpsIP31758_2619(poxB)
            SFL: SF0826(poxB)
            SFX: S0867(poxB)
            SFV: SFV_0859(poxB)
            SSN: SSON_0857(poxB)
            SBO: SBO_0804(poxB)
            SDY: SDY_2392(poxB)
            XCC: XCC0206(poxB)
            XCB: XC_0216
            XCV: XCV0230(poxB)
            XAC: XAC0224(poxB)
            XOO: XOO4200(poxB)
            XOM: XOO_3969(XOO3969)
            PAE: PA5297(poxB)
            PAU: PA14_69925(poxB)
            PST: PSPTO_2510(poxB)
            PSB: Psyr_2314
            PSP: PSPPH_2857(poxB)
            PFL: PFL_3603(poxB)
            ACI: ACIAD3381(poxB)
            CBD: COXBU7E912_0736(poxB)
            REH: H16_A3123
            RME: Rmet_1899
            BMA: BMAA1650(poxB)
            BMV: BMASAVP1_1728(poxB)
            BML: BMA10299_1935(poxB)
            BMN: BMA10247_A0611(poxB)
            BXE: Bxe_B2374
            BUR: Bcep18194_B2858
            BPS: BPSS1636(poxB)
            BPM: BURPS1710b_0946(poxB) BURPS1710b_A0699(poxB)
            BPL: BURPS1106A_A2219
            BPD: BURPS668_A2302(poxB)
            MXA: MXAN_3654(poxB) MXAN_3857(poxB)
            BJA: bll7286(poxB)
            BRA: BRADO6642(poxB)
            BBT: BBta_0892(poxB)
            RPB: RPB_0203
            MSM: MSMEG_2280 MSMEG_3964
            CGL: NCgl2521(cgl2610)
            CGB: cg2891(poxB)
            CDI: DIP1952
            CJK: jk0715(poxB)
            RHA: RHA1_ro01066
            SCO: SCO6155(SC1A9.19)
            SMA: SAV2079(poxB2)
            CMI: CMM_2128(poxB)
            PAC: PPA1468
            FAL: FRAAL1802
            SEN: SACE_1218(poxB) SACE_5551(poxB)
            BTH: BT_1820 BT_1822
            BFR: BF3389
            BFS: BF3217(poxB)
            CHU: CHU_2249(poxB)
            TAC: Ta0816
            PTO: PTO1502
            SSO: SSO1012(ilvB-3) SSO2962(ilvB-5)
            SAI: Saci_1935(pox)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.2.2
            ExPASy - ENZYME nomenclature database: 1.2.2.2
            ExplorEnz - The Enzyme Database: 1.2.2.2
            ERGO genome analysis and discovery system: 1.2.2.2
            BRENDA, the Enzyme Database: 1.2.2.2
            CAS: 9079-84-9
///
ENTRY       EC 1.2.2.3                  Enzyme
NAME        formate dehydrogenase (cytochrome-c-553)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With a cytochrome as acceptor
SYSNAME     formate:ferricytochrome-c-553 oxidoreductase
REACTION    formate + ferricytochrome c-553 = CO2 + ferrocytochrome c-553
            [RN:R03215]
ALL_REAC    R03215
SUBSTRATE   formate [CPD:C00058];
            ferricytochrome c-553 [CPD:C01070]
PRODUCT     CO2 [CPD:C00011];
            ferrocytochrome c-553 [CPD:C01071]
COMMENT     Yeast cytochrome c, ferricyanide and phenazine methosulfate can act
            as acceptor.
REFERENCE   1  [PMID:4982127]
  AUTHORS   Yagi T.
  TITLE     Formate: cytochrome oxidoreductase of Desulfovibrio vulgaris.
  JOURNAL   J. Biochem. (Tokyo). 66 (1969) 473-8.
  ORGANISM  Desulfovibrio vulgaris
REFERENCE   2  [PMID:226135]
  AUTHORS   Yagi T.
  TITLE     Purification and properties of cytochrome c-553, an electron
            acceptor for formate dehydrogenase of Desulfovibrio vulgaris,
            Miyazaki.
  JOURNAL   Biochim. Biophys. Acta. 548 (1979) 96-105.
  ORGANISM  Desulfovibrio vulgaris
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.2.3
            ExPASy - ENZYME nomenclature database: 1.2.2.3
            ExplorEnz - The Enzyme Database: 1.2.2.3
            ERGO genome analysis and discovery system: 1.2.2.3
            BRENDA, the Enzyme Database: 1.2.2.3
///
ENTRY       EC 1.2.2.4                  Enzyme
NAME        carbon-monoxide dehydrogenase (cytochrome b-561);
            carbon monoxide oxidase;
            carbon monoxide oxygenase (cytochrome b-561);
            carbon monoxide:methylene blue oxidoreductase;
            CO dehydrogenase;
            carbon-monoxide dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With a cytochrome as acceptor
SYSNAME     carbon monoxide,water:cytochrome b-561 oxidoreductase
REACTION    CO + H2O + 2 ferricytochrome b-561 = CO2 + 2 H+ + 2 ferrocytochrome
            b-561 [RN:R04698]
ALL_REAC    R04698;
            (other) R00276
SUBSTRATE   CO [CPD:C00237];
            H2O [CPD:C00001];
            ferricytochrome b-561 [CPD:C05305]
PRODUCT     CO2 [CPD:C00011];
            H+ [CPD:C00080];
            ferrocytochrome b-561 [CPD:C05183]
COMMENT     Contains molybdopterin cytosine dinucleotide, FAD and
            [2Fe-2S]-clusters. Oxygen, methylene blue and iodonitrotetrazolium
            chloride can act as nonphysiological electron acceptors.
REFERENCE   1
  AUTHORS   Meyer, O., Jacobitz, S. and Kruger, B.
  TITLE     Biochemistry and physiology of aerobic carbon monoxide-utilizing
            bacteria.
  JOURNAL   FEMS Microbiol. Rev. 39 (1986) 161-179.
  ORGANISM  Pseudomonas carboxydovorans, Pseudomonas carboxydohydrogena,
            Pseudomonas carboxydoflava, Pseudomonas thermocarboxydovorans,
            Bacillus schlegelii
REFERENCE   2  [PMID:2808305]
  AUTHORS   Jacobitz S, Meyer O.
  TITLE     Removal of CO dehydrogenase from Pseudomonas carboxydovorans
            cytoplasmic membranes, rebinding of CO dehydrogenase to depleted
            membranes, and restoration of respiratory activities.
  JOURNAL   J. Bacteriol. 171 (1989) 6294-9.
  ORGANISM  Pseudomonas carboxydovorans
REFERENCE   3  [PMID:7354006]
  AUTHORS   Meyer O, Schlegel HG.
  TITLE     Carbon monoxide:methylene blue oxidoreductase from Pseudomonas
            carboxydovorans.
  JOURNAL   J. Bacteriol. 141 (1980) 74-80.
  ORGANISM  Pseudomonas carboxydovorans
REFERENCE   4  [PMID:10430865]
  AUTHORS   Dobbek H, Gremer L, Meyer O, Huber R.
  TITLE     Crystal structure and mechanism of CO dehydrogenase, a molybdo
            iron-sulfur flavoprotein containing S-selanylcysteine.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 8884-9.
  ORGANISM  Oligotropha carboxidovorans
REFERENCE   5  [PMID:10966817]
  AUTHORS   Hanzelmann P, Dobbek H, Gremer L, Huber R, Meyer O.
  TITLE     The effect of intracellular molybdenum in Hydrogenophaga pseudoflava
            on the crystallographic structure of the seleno-molybdo-iron-sulfur
            flavoenzyme carbon monoxide dehydrogenase.
  JOURNAL   J. Mol. Biol. 301 (2000) 1221-35.
  ORGANISM  Hydrogenophaga pseudoflava
ORTHOLOGY   KO: K05891  carbon-monoxide dehydrogenase (cytochrome b-561)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.2.4
            ExPASy - ENZYME nomenclature database: 1.2.2.4
            ExplorEnz - The Enzyme Database: 1.2.2.4
            ERGO genome analysis and discovery system: 1.2.2.4
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.2.4
            BRENDA, the Enzyme Database: 1.2.2.4
            CAS: 64972-88-9
///
ENTRY       EC 1.2.3.1                  Enzyme
NAME        aldehyde oxidase;
            quinoline oxidase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With oxygen as acceptor
SYSNAME     aldehyde:oxygen oxidoreductase
REACTION    an aldehyde + H2O + O2 = a carboxylic acid + H2O2 [RN:R00635]
ALL_REAC    R00635 > R02657 R04904;
            (other) R01709 R02655 R03871 R04085
SUBSTRATE   aldehyde [CPD:C00071];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     carboxylic acid [CPD:C00060];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016];
            Heme [CPD:C00032];
            Molybdenum [CPD:C00150];
            Iron-sulfur [CPD:C00824]
COMMENT     Contains molybdenum, [2Fe-2S] centres and FAD. Also oxidizes
            quinoline and pyridine derivatives. May be identical with EC
            1.2.3.11, retinal oxidase.
REFERENCE   1
  AUTHORS   Gordon, A.H., Green, D.E. and Subrahmanyan, V.
  TITLE     Liver aldehyde oxidase.
  JOURNAL   Biochem. J. 34 (1940) 764-774.
  ORGANISM  pig [GN:ssc]
REFERENCE   2
  AUTHORS   Knox, W.E.
  TITLE     The quinine-oxidizing enzyme and liver aldehyde oxidase.
  JOURNAL   J. Biol. Chem. 163 (1946) 699-711.
  ORGANISM  rabbit
REFERENCE   3  [PMID:13201608]
  AUTHORS   MAHLER HR, MACKLER B, GREEN DE.
  TITLE     Studies on metalloflavoproteins. III. Aldehyde oxidase: a
            molybdoflavoprotein.
  JOURNAL   J. Biol. Chem. 210 (1954) 465-80.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:10190983]
  AUTHORS   Huang DY, Furukawa A, Ichikawa Y.
  TITLE     Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from
            rabbit and mouse livers and functional expression of recombinant
            mouse retinal oxidase cDNA in Escherichia coli.
  JOURNAL   Arch. Biochem. Biophys. 364 (1999) 264-72.
  ORGANISM  rabbit, mouse [GN:mmu]
REFERENCE   5  [PMID:14659539]
  AUTHORS   Uchida H, Kondo D, Yamashita A, Nagaosa Y, Sakurai T, Fujii Y,
            Fujishiro K, Aisaka K, Uwajima T.
  TITLE     Purification and characterization of an aldehyde oxidase from
            Pseudomonas sp. KY 4690.
  JOURNAL   FEMS. Microbiol. Lett. 229 (2003) 31-6.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00350  Tyrosine metabolism
            PATH: map00380  Tryptophan metabolism
            PATH: map00750  Vitamin B6 metabolism
            PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K00157  aldehyde oxidase
GENES       HSA: 316(AOX1)
            RNO: 54349(Aox1)
            CFA: 608849(AOH3)
            BTA: 338074(AOX1)
            GGA: 424071(AOX1)
            XLA: 444490(MGC81880)
            BUR: Bcep18194_A3924
            BRA: BRADO5140
            BBT: BBta_5607
            RDE: RD1_1533(mop)
STRUCTURES  PDB: 1SIJ  1VLB  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.3.1
            ExPASy - ENZYME nomenclature database: 1.2.3.1
            ExplorEnz - The Enzyme Database: 1.2.3.1
            ERGO genome analysis and discovery system: 1.2.3.1
            BRENDA, the Enzyme Database: 1.2.3.1
            CAS: 9029-07-6
///
ENTRY       EC 1.2.3.2        Obsolete  Enzyme
NAME        Transferred to 1.17.3.2
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now EC 1.17.3.2, xanthine oxidase (EC 1.2.3.2
            created 1961, deleted 1984)
STRUCTURES  PDB: 2CKJ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.3.2
            ExPASy - ENZYME nomenclature database: 1.2.3.2
            ExplorEnz - The Enzyme Database: 1.2.3.2
            ERGO genome analysis and discovery system: 1.2.3.2
            BRENDA, the Enzyme Database: 1.2.3.2
///
ENTRY       EC 1.2.3.3                  Enzyme
NAME        pyruvate oxidase;
            pyruvic oxidase;
            phosphate-dependent pyruvate oxidase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With oxygen as acceptor
SYSNAME     pyruvate:oxygen 2-oxidoreductase (phosphorylating)
REACTION    pyruvate + phosphate + O2 = acetyl phosphate + CO2 + H2O2
            [RN:R00207]
ALL_REAC    R00207
SUBSTRATE   pyruvate [CPD:C00022];
            phosphate [CPD:C00009];
            O2 [CPD:C00007]
PRODUCT     acetyl phosphate [CPD:C00227];
            CO2 [CPD:C00011];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016];
            Thiamin diphosphate [CPD:C00068]
COMMENT     A flavoprotein (FAD) requiring thiamine diphosphate. Two reducing
            equivalents are transferred from the resonant carbanion/enamine
            forms of 2-hydroxyethyl-thiamine-diphosphate to the adjacent flavin
            cofactor, yielding 2-acetyl-thiamine diphosphate (AcThDP) and
            reduced flavin. FADH2 is reoxidized by O2 to yield H2O2 and FAD and
            AcThDP is cleaved phosphorolytically to acetyl phosphate and
            thiamine diphosphate [2].
REFERENCE   1  [PMID:5336022]
  AUTHORS   Williams FR, Hager LP.
  TITLE     Crystalline flavin pyruvate oxidase from Escherichia coli. I.
            Isolation and properties of the flavoprotein.
  JOURNAL   Arch. Biochem. Biophys. 116 (1966) 168-76.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:16201755]
  AUTHORS   Tittmann K, Wille G, Golbik R, Weidner A, Ghisla S, Hubner G.
  TITLE     Radical phosphate transfer mechanism for the thiamin diphosphate-
            and FAD-dependent pyruvate oxidase from Lactobacillus plantarum.
            Kinetic coupling of intercofactor electron transfer with phosphate
            transfer to acetyl-thiamin diphosphate via a transient FAD
            semiquinone/hydroxyethyl-ThDP radical pair.
  JOURNAL   Biochemistry. 44 (2005) 13291-303.
  ORGANISM  Lactobacillus plantarum [GN:lpl]
PATHWAY     PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K00158  pyruvate oxidase
GENES       GBE: GbCGDNIH1_2349
            BSU: BG12063(ydaP)
            BCE: BC2328
            BCA: BCE_2426
            BCZ: BCZK2152
            BLI: BL00146(ydaP)
            BLD: BLi00520(ydaP)
            BPU: BPUM_0407(ydaP)
            OIH: OB3409
            SAU: SA2327
            SAV: SAV2539
            SAM: MW2460
            SAR: SAR2619
            SAS: SAS2425
            SAC: SACOL2553
            SAB: SAB2413c
            SAA: SAUSA300_2477(cidC)
            SAO: SAOUHSC_02849
            SEP: SE2103
            SER: SERP2115
            SHA: SH0519
            SSP: SSP0333
            LMO: lmo0722
            LMF: LMOf2365_0758
            LIN: lin0730
            LWE: lwe0691
            LLA: L0199(poxL)
            LLM: llmg_2321(poxL)
            SPN: SP_0730
            SPR: spr0642(spxB)
            SPD: SPD_0636(spxB)
            SSA: SSA_0391(spxB)
            SGO: SGO_0292(spxB)
            LPL: lp_0849(pox1) lp_0852(pox2) lp_2629(pox3) lp_3587(pox4)
                 lp_3589(pox5)
            LJO: LJ1853
            LAC: LBA1974(poxB)
            LSA: LSA1188(pox1) LSA1830(pox2)
            LSL: LSL_0014 LSL_1372
            LDB: Ldb2213(pox1)
            LBU: LBUL_2034
            LBR: LVIS_0313
            LCA: LSEI_0433 LSEI_1784 LSEI_2143
            OOE: OEOE_0936
STRUCTURES  PDB: 1POW  1POX  1V5E  1V5F  1V5G  1Y9D  2DJI  2EZ4  2EZ8  2EZ9  
                 2EZT  2EZU  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.3.3
            ExPASy - ENZYME nomenclature database: 1.2.3.3
            ExplorEnz - The Enzyme Database: 1.2.3.3
            ERGO genome analysis and discovery system: 1.2.3.3
            BRENDA, the Enzyme Database: 1.2.3.3
            CAS: 9001-96-1
///
ENTRY       EC 1.2.3.4                  Enzyme
NAME        oxalate oxidase;
            aero-oxalo dehydrogenase;
            oxalic acid oxidase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With oxygen as acceptor
SYSNAME     oxalate:oxygen oxidoreductase
REACTION    oxalate + O2 + 2 H+ = 2 CO2 + H2O2 [RN:R00273]
ALL_REAC    R00273
SUBSTRATE   oxalate [CPD:C00209];
            O2 [CPD:C00007];
            H+ [CPD:C00080]
PRODUCT     CO2 [CPD:C00011];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016];
            Manganese [CPD:C00034]
COMMENT     Contains Mn2+ as a cofactor. The enzyme is not a flavoprotein as had
            been thought [3].
REFERENCE   1  [PMID:13250021]
  AUTHORS   DATTA PK, MEEUSE BJ.
  TITLE     Moss oxalic acid oxidase-a flavoprotein.
  JOURNAL   Biochim. Biophys. Acta. 17 (1955) 602-3.
  ORGANISM  Hylocomium loreum, Hylocomium splendens, Rhytidiadelphus squarrosus
REFERENCE   2  [PMID:9143327]
  AUTHORS   Kotsira VP, Clonis YD.
  TITLE     Oxalate oxidase from barley roots: purification to homogeneity and
            study of some molecular, catalytic, and binding properties.
  JOURNAL   Arch. Biochem. Biophys. 340 (1997) 239-49.
  ORGANISM  Hordeum vulgare [GN:ehvu]
REFERENCE   3  [PMID:10493928]
  AUTHORS   Requena L, Bornemann S.
  TITLE     Barley (Hordeum vulgare) oxalate oxidase is a manganese-containing
            enzyme.
  JOURNAL   Biochem. J. 343 Pt 1 (1999) 185-90.
  ORGANISM  Hordeum vulgare [GN:ehvu]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
GENES       TBR: Tb927.5.300 Tb927.7.7500
            TCR: 508409.160 510141.10
STRUCTURES  PDB: 1FI2  2ET1  2ET7  2ETE  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.3.4
            ExPASy - ENZYME nomenclature database: 1.2.3.4
            ExplorEnz - The Enzyme Database: 1.2.3.4
            ERGO genome analysis and discovery system: 1.2.3.4
            BRENDA, the Enzyme Database: 1.2.3.4
            CAS: 9031-79-2
///
ENTRY       EC 1.2.3.5                  Enzyme
NAME        glyoxylate oxidase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With oxygen as acceptor
SYSNAME     glyoxylate:oxygen oxidoreductase
REACTION    glyoxylate + H2O + O2 = oxalate + H2O2 [RN:R00466]
ALL_REAC    R00466
SUBSTRATE   glyoxylate [CPD:C00048];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     oxalate [CPD:C00209];
            H2O2 [CPD:C00027]
REFERENCE   1
  AUTHORS   Kasai, T., Suzuki, I. and Asai, T.
  TITLE     [Glyoxylic oxidase system in Acetobacter.].
  JOURNAL   Koso Kagaku Shimpojiumu 17 (1962) 77-81.
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.3.5
            ExPASy - ENZYME nomenclature database: 1.2.3.5
            ExplorEnz - The Enzyme Database: 1.2.3.5
            ERGO genome analysis and discovery system: 1.2.3.5
            BRENDA, the Enzyme Database: 1.2.3.5
            CAS: 37251-03-9
///
ENTRY       EC 1.2.3.6                  Enzyme
NAME        pyruvate oxidase (CoA-acetylating)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With oxygen as acceptor
SYSNAME     pyruvate:oxygen 2-oxidoreductase (CoA-acetylating)
REACTION    pyruvate + CoA + O2 = acetyl-CoA + CO2 + H2O2 [RN:R00211]
ALL_REAC    R00211
SUBSTRATE   pyruvate [CPD:C00022];
            CoA [CPD:C00010];
            O2 [CPD:C00007]
PRODUCT     acetyl-CoA [CPD:C00024];
            CO2 [CPD:C00011];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). May be identical with EC 1.2.7.1 pyruvate
            synthase.
REFERENCE   1  [PMID:13076]
  AUTHORS   Reeves RE, Warren LG, Susskind B, Lo HS.
  TITLE     An energy-conserving pyruvate-to-acetate pathway in Entamoeba
            histolytica. Pyruvate synthase and a new acetate thiokinase.
  JOURNAL   J. Biol. Chem. 252 (1977) 726-31.
  ORGANISM  Entamoeba histolytica [GN:ehi]
REFERENCE   2  [PMID:167776]
  AUTHORS   Takeuchi T, Weinbach EC, Diamond LS.
  TITLE     Pyruvate oxidase (CoA acetylating) in Entamoeba histolytica.
  JOURNAL   Biochem. Biophys. Res. Commun. 65 (1975) 591-6.
  ORGANISM  Entamoeba histolytica [GN:ehi]
PATHWAY     PATH: map00620  Pyruvate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.3.6
            ExPASy - ENZYME nomenclature database: 1.2.3.6
            ExplorEnz - The Enzyme Database: 1.2.3.6
            ERGO genome analysis and discovery system: 1.2.3.6
            BRENDA, the Enzyme Database: 1.2.3.6
            CAS: 62213-57-4
///
ENTRY       EC 1.2.3.7                  Enzyme
NAME        indole-3-acetaldehyde oxidase;
            indoleacetaldehyde oxidase;
            IAAld oxidase;
            AO1;
            indole-3-acetaldehyde:oxygen oxidoreductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With oxygen as acceptor
SYSNAME     (indol-3-yl)acetaldehyde:oxygen oxidoreductase
REACTION    (indol-3-yl)acetaldehyde + H2O + O2 = (indol-3-yl)acetate + H2O2
            [RN:R02681]
ALL_REAC    R02681
SUBSTRATE   (indol-3-yl)acetaldehyde;
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     (indol-3-yl)acetate [CPD:C00954];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016];
            Heme [CPD:C00032];
            Molybdenum [CPD:C00150]
COMMENT     A hemoprotein. This enzyme is an isoform of aldehyde oxidase (EC
            1.2.3.1). It has a preference for aldehydes having an indole-ring
            structure as substrate [6,7]. It may play a role in plant hormone
            biosynthesis as its activity is higher in the auxin-overproducing
            mutant, super-root1, than in wild-type Arabidopsis thaliana [7].
            While (indol-3-yl)acetaldehyde is the preferred substrate, it also
            oxidizes indole-3-carbaldehyde and acetaldehyde, but more slowly.
            The enzyme from maize contains FAD, iron and molybdenum [4].
REFERENCE   1
  AUTHORS   Bower, P.J., Brown, H.M. and Purves, W.K.
  TITLE     Cucumber seedling indoleacetaldehyde oxidase.
  JOURNAL   Plant Physiol. 61 (1978) 107-110.
  ORGANISM  Cucumis sativus
REFERENCE   2
  AUTHORS   Miyata, S., Suzuki, Y., Kamisaka, S. and Masuda, Y.
  TITLE     Indole-3-acetaldehyde oxidase of pea-seedlings.
  JOURNAL   Physiol. Plant. 51 (1981) 402-406.
  ORGANISM  Pisum satiyum
REFERENCE   3
  AUTHORS   Rajagopal, R.
  TITLE     Metabolism of indole-3-acetaldehyde. III. Some characteristics of
            the aldehyde oxidase of Avena coleoptiles.
  JOURNAL   Physiol. Plant. 24 (1971) 272-281.
  ORGANISM  Avena coleoptiles
REFERENCE   4  [PMID:12226218]
  AUTHORS   Koshiba T, Saito E, Ono N, Yamamoto N, Sato M.
  TITLE     Purification and Properties of Flavin- and Molybdenum-Containing
            Aldehyde Oxidase from Coleoptiles of Maize.
  JOURNAL   Plant. Physiol. 110 (1996) 781-789.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   5  [PMID:12231908]
  AUTHORS   Koshiba T, Matsuyama H.
  TITLE     An in Vitro System of Indole-3-Acetic Acid Formation from Tryptophan
            in Maize (Zea mays) Coleoptile Extracts.
  JOURNAL   Plant. Physiol. 102 (1993) 1319-1324.
REFERENCE   6  [PMID:9615466]
  AUTHORS   Sekimoto H, Seo M, Kawakami N, Komano T, Desloire S, Liotenberg S,
            Marion-Poll A, Caboche M, Kamiya Y, Koshiba T.
  TITLE     Molecular cloning and characterization of aldehyde oxidases in
            Arabidopsis thaliana.
  JOURNAL   Plant. Cell. Physiol. 39 (1998) 433-42.
REFERENCE   7  [PMID:9489015]
  AUTHORS   Seo M, Akaba S, Oritani T, Delarue M, Bellini C, Caboche M, Koshiba
            T.
  TITLE     Higher activity of an aldehyde oxidase in the auxin-overproducing
            superroot1 mutant of Arabidopsis thaliana.
  JOURNAL   Plant. Physiol. 116 (1998) 687-93.
PATHWAY     PATH: map00380  Tryptophan metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.3.7
            ExPASy - ENZYME nomenclature database: 1.2.3.7
            ExplorEnz - The Enzyme Database: 1.2.3.7
            ERGO genome analysis and discovery system: 1.2.3.7
            BRENDA, the Enzyme Database: 1.2.3.7
            CAS: 66082-22-2
///
ENTRY       EC 1.2.3.8                  Enzyme
NAME        pyridoxal oxidase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With oxygen as acceptor
SYSNAME     pyridoxal:oxygen 4-oxidoreductase
REACTION    pyridoxal + H2O + O2 = 4-pyridoxate + (?) [RN:R01709]
ALL_REAC    R01709
SUBSTRATE   pyridoxal [CPD:C00250];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     4-pyridoxate [CPD:C00847]
COFACTOR    Molybdenum [CPD:C00150]
COMMENT     A molybdenum protein.
REFERENCE   1
  AUTHORS   Hanly, E.W.
  TITLE     Preliminary characterization and physical properties of pyridoxal
            oxidase activity from Drosophila melanogaster.
  JOURNAL   Mol. Gen. Genet. 180 (1980) 455-462.
  ORGANISM  Drosophila melanogaster [GN:dme]
REFERENCE   2
  AUTHORS   Warner, C.K., Watts, D.T. and Finnerty, V.
  TITLE     Molybdenum hydroxylases in Drosophila. I. Preliminary studies of
            pyridoxal oxidase.
  JOURNAL   Mol. Gen. Genet. 180 (1980) 449-453.
  ORGANISM  Drosophila melanogaster [GN:dme]
PATHWAY     PATH: map00750  Vitamin B6 metabolism
ORTHOLOGY   KO: K00159  pyridoxal oxidase
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.3.8
            ExPASy - ENZYME nomenclature database: 1.2.3.8
            ExplorEnz - The Enzyme Database: 1.2.3.8
            ERGO genome analysis and discovery system: 1.2.3.8
            BRENDA, the Enzyme Database: 1.2.3.8
            CAS: 76415-81-1
///
ENTRY       EC 1.2.3.9                  Enzyme
NAME        aryl-aldehyde oxidase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With oxygen as acceptor
SYSNAME     aryl-aldehyde:oxygen oxidoreductase
REACTION    an aromatic aldehyde + O2 + H2O = an aromatic carboxylic acid + H2O2
            [RN:R01489]
ALL_REAC    R01489;
            (other) R05273
SUBSTRATE   aromatic aldehyde [CPD:C00193];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     aromatic carboxylic acid [CPD:C00539];
            H2O2 [CPD:C00027]
COMMENT     Acts on benzaldehyde, vanillin and a number of other aromatic
            aldehydes, but not on aliphatic aldehydes or sugars.
REFERENCE   1
  AUTHORS   Crawford, D.L., Sutherland, J.B., Pometto, A.L., III and Miller,
            J.M.
  TITLE     Production of an aromatic aldehyde oxidase by Streptomyces
            viridosporus.
  JOURNAL   Arch. Microbiol. 131 (1982) 351-355.
  ORGANISM  Streptomyces viridosporus
GENES       AFM: AFUA_8G05520
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.3.9
            ExPASy - ENZYME nomenclature database: 1.2.3.9
            ExplorEnz - The Enzyme Database: 1.2.3.9
            ERGO genome analysis and discovery system: 1.2.3.9
            BRENDA, the Enzyme Database: 1.2.3.9
            CAS: 82657-93-0
///
ENTRY       EC 1.2.3.10       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With oxygen as acceptor
COMMENT     Deleted entry: carbon-monoxide oxidase. Activity due to EC 1.2.2.4
            carbon-monoxide dehydrogenase (cytochrome b-561) (EC 1.2.3.10
            created 1990, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.3.10
            ExPASy - ENZYME nomenclature database: 1.2.3.10
            ExplorEnz - The Enzyme Database: 1.2.3.10
            ERGO genome analysis and discovery system: 1.2.3.10
            BRENDA, the Enzyme Database: 1.2.3.10
///
ENTRY       EC 1.2.3.11                 Enzyme
NAME        retinal oxidase;
            retinene oxidase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With oxygen as acceptor
SYSNAME     retinal:oxygen oxidoreductase
REACTION    retinal + O2 + H2O = retinoate + H2O2 [RN:R02125]
ALL_REAC    R02125
SUBSTRATE   retinal [CPD:C00376];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     retinoate [CPD:C00777];
            H2O2 [CPD:C00027]
COMMENT     May be the same as EC 1.2.3.1, aldehyde oxidase.
REFERENCE   1  [PMID:3452601]
  AUTHORS   Mandal SK, Datta Chaudhuri B.
  TITLE     Enzymic oxidation of vitamin A aldehyde to vitamin A acid by rat
            livers of experimental thyroid disorders.
  JOURNAL   Indian. J. Exp. Biol. 25 (1987) 796-7.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:10190983]
  AUTHORS   Huang DY, Furukawa A, Ichikawa Y.
  TITLE     Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from
            rabbit and mouse livers and functional expression of recombinant
            mouse retinal oxidase cDNA in Escherichia coli.
  JOURNAL   Arch. Biochem. Biophys. 364 (1999) 264-72.
  ORGANISM  mouse [GN:mmu], rabbit
PATHWAY     PATH: map00830  Retinol metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.3.11
            ExPASy - ENZYME nomenclature database: 1.2.3.11
            ExplorEnz - The Enzyme Database: 1.2.3.11
            ERGO genome analysis and discovery system: 1.2.3.11
            BRENDA, the Enzyme Database: 1.2.3.11
            CAS: 9033-52-7
///
ENTRY       EC 1.2.3.12       Obsolete  Enzyme
NAME        Transferred to 1.14.13.82
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now EC 1.14.13.82 vanillate monooxygenase (EC
            1.2.3.12 created 2000, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.3.12
            ExPASy - ENZYME nomenclature database: 1.2.3.12
            ExplorEnz - The Enzyme Database: 1.2.3.12
            ERGO genome analysis and discovery system: 1.2.3.12
            BRENDA, the Enzyme Database: 1.2.3.12
///
ENTRY       EC 1.2.3.13                 Enzyme
NAME        4-hydroxyphenylpyruvate oxidase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With oxygen as acceptor
SYSNAME     4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating)
REACTION    4-hydroxyphenylpyruvate + 1/2 O2 = 4-hydroxyphenylacetate + CO2
            [RN:R00042]
ALL_REAC    R00042
SUBSTRATE   4-hydroxyphenylpyruvate [CPD:C01179];
            O2 [CPD:C00007]
PRODUCT     4-hydroxyphenylacetate [CPD:C00642];
            CO2 [CPD:C00011]
COMMENT     Involved in tyrosine degradation pathway in Arthrobacter sp.
REFERENCE   1  [PMID:20216]
  AUTHORS   Blakley ER.
  TITLE     The catabolism of L-tyrosine by an Arthrobacter sp.
  JOURNAL   Can. J. Microbiol. 23 (1977) 1128-39.
  ORGANISM  Arthrobacter sp.
PATHWAY     PATH: map00350  Tyrosine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.3.13
            ExPASy - ENZYME nomenclature database: 1.2.3.13
            ExplorEnz - The Enzyme Database: 1.2.3.13
            ERGO genome analysis and discovery system: 1.2.3.13
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.3.13
            BRENDA, the Enzyme Database: 1.2.3.13
///
ENTRY       EC 1.2.3.14                 Enzyme
NAME        abscisic-aldehyde oxidase;
            abscisic aldehyde oxidase;
            AAO3;
            AOd;
            AOdelta
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With oxygen as acceptor
SYSNAME     abscisic-aldehyde:oxygen oxidoreductase
REACTION    abscisic aldehyde + H2O + O2 = abscisate + H2O2 [RN:R06957]
ALL_REAC    R06957
SUBSTRATE   abscisic aldehyde [CPD:C13455];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     abscisate [CPD:C06082];
            H2O2 [CPD:C00027]
COMMENT     Acts on both (+)- and (-)-abscisic aldehyde. Involved in the
            abscisic-acid biosynthesis pathway in plants, along with EC
            1.1.1.288, (xanthoxin dehydrogenase), EC 1.13.11.51
            (9-cis-epoxycarotenoid dioxygenase) and EC 1.14.13.93 [(+)-abscisic
            acid 8'-hydroxylase]. While abscisic aldehyde is the best substrate,
            the enzyme also acts with indole-3-aldehyde, 1-naphthaldehyde and
            benzaldehyde as substrates, but more slowly [3].
REFERENCE   1  [PMID:10364409]
  AUTHORS   Sagi M, Fluhr R, Lips SH.
  TITLE     Aldehyde oxidase and xanthine dehydrogenase in a flacca tomato
            mutant with deficient abscisic acid and wilty phenotype
  JOURNAL   Plant. Physiol. 120 (1999) 571-8.
  ORGANISM  Lycopersicon esculentum [GN:eles]
REFERENCE   2  [PMID:11050171]
  AUTHORS   Seo M, Peeters AJ, Koiwai H, Oritani T, Marion-Poll A, Zeevaart JA,
            Koornneef M, Kamiya Y, Koshiba T.
  TITLE     The Arabidopsis aldehyde oxidase 3 (AAO3) gene product catalyzes the
            final step in abscisic acid biosynthesis in leaves.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 12908-13.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   3  [PMID:10972874]
  AUTHORS   Seo M, Koiwai H, Akaba S, Komano T, Oritani T, Kamiya Y, Koshiba T.
  TITLE     Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana.
  JOURNAL   Plant. J. 23 (2000) 481-8.
  ORGANISM  Arabidopsis thaliana [GN:ath]
PATHWAY     PATH: map00906  Carotenoid biosynthesis - General
ORTHOLOGY   KO: K09842  abscisic-aldehyde oxidase
GENES       ATH: AT2G27150(AAO3)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.3.14
            ExPASy - ENZYME nomenclature database: 1.2.3.14
            ExplorEnz - The Enzyme Database: 1.2.3.14
            ERGO genome analysis and discovery system: 1.2.3.14
            BRENDA, the Enzyme Database: 1.2.3.14
///
ENTRY       EC 1.2.3.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With oxygen as acceptor
REACTION    (1) 2 3-(4-Hydroxyphenyl)pyruvate + Oxygen <=> 2
            4-Hydroxyphenylacetate + 2 CO2 [RN:R00042];
            (2) 3-Formylsalicylic acid + Oxygen + H2O <=> 2-Hydroxyisophthalic
            acid + H2O2 [RN:R06924];
            (3) Vanillate + Cob(I)alamin <=> 3,4-Dihydroxybenzoate +
            Methylcobalamin [RN:R07668]
SUBSTRATE   3-(4-Hydroxyphenyl)pyruvate [CPD:C01179];
            Oxygen [CPD:C00007];
            3-Formylsalicylic acid [CPD:C14096];
            H2O [CPD:C00001]
PRODUCT     4-Hydroxyphenylacetate [CPD:C00642];
            CO2 [CPD:C00011];
            2-Hydroxyisophthalic acid [CPD:C14097];
            H2O2 [CPD:C00027]
///
ENTRY       EC 1.2.4.1                  Enzyme
NAME        pyruvate dehydrogenase (acetyl-transferring);
            MtPDC (mitochondrial pyruvate dehydogenase complex);
            pyruvate decarboxylase;
            pyruvate dehydrogenase;
            pyruvate dehydrogenase (lipoamide);
            pyruvate dehydrogenase complex;
            pyruvate:lipoamide 2-oxidoreductase (decarboxylating and
            acceptor-acetylating);
            pyruvic acid dehydrogenase;
            pyruvic dehydrogenase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With a disulfide as acceptor
SYSNAME     pyruvate:[dihydrolipoyllysine-residue
            acetyltransferase]-lipoyllysine 2-oxidoreductase (decarboxylating,
            acceptor-acetylating)
REACTION    pyruvate + [dihydrolipoyllysine-residue acetyltransferase]
            lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase]
            S-acetyldihydrolipoyllysine + CO2 [RN:R01699]
ALL_REAC    R01699;
            (other) R00014 R00209 R03270
SUBSTRATE   pyruvate [CPD:C00022];
            [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine
PRODUCT     [dihydrolipoyllysine-residue acetyltransferase]
            S-acetyldihydrolipoyllysine [CPD:C16255];
            CO2 [CPD:C00011]
COFACTOR    Thiamin diphosphate [CPD:C00068]
COMMENT     Contains thiamine diphosphate. It is a component (in multiple
            copies) of the multienzyme pyruvate dehydrogenase complex in which
            it is bound to a core of molecules of EC 2.3.1.12,
            dihydrolipoyllysine-residue acetyltransferase, which also binds
            multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does
            not act on free lipoamide or lipoyllysine, but only on the
            lipoyllysine residue in EC 2.3.1.12.
REFERENCE   1  [PMID:13158180]
  AUTHORS   OCHOA S.
  TITLE     Enzymic mechanisms in the citric acid cycle.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 15 (1954) 183-270.
REFERENCE   2
  AUTHORS   Scriba, P. and Holzer, H.
  TITLE     Gewinnung von alphaHydroxyathyl-2-thiaminpyrophosphat mit
            Pyruvatoxydase aus Schweineherzmuskel.
  JOURNAL   Biochem. Z. 334 (1961) 473-486.
REFERENCE   3  [PMID:10966480]
  AUTHORS   Perham RN.
  TITLE     Swinging arms and swinging domains in multifunctional enzymes:
            catalytic machines for multistep reactions.
  JOURNAL   Annu. Rev. Biochem. 69 (2000) 961-1004.
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00252  Alanine and aspartate metabolism
            PATH: map00290  Valine, leucine and isoleucine biosynthesis
            PATH: map00620  Pyruvate metabolism
            PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K00160  pyruvate dehydrogenase
            KO: K00161  pyruvate dehydrogenase E1 component, alpha subunit
            KO: K00162  pyruvate dehydrogenase E1 component, beta subunit
            KO: K00163  pyruvate dehydrogenase E1 component
GENES       HSA: 5160(PDHA1) 5161(PDHA2) 5162(PDHB)
            PTR: 465525(PDHA1) 470832(PDHB) 471255(PDHA2)
            MMU: 18597(Pdha1) 18598(Pdha2) 68263(Pdhb)
            RNO: 117098(Pdha2) 289950(Pdhb)
            CFA: 480858(PDHA1)
            BTA: 407109(PDHA)
            GGA: 416066(PDHB) 418610(PDHA1)
            XLA: 398064(PdhE1beta-2) 446473(pdha1-a) 447434(pdha1-b)
            DRE: 406428(pdhb) 436672(zgc:92705)
            SPU: 580083(LOC580083) 752050(LOC752050)
            DME: Dmel_CG7010(l(1)G0334) Dmel_CG7024
            CEL: C04C3.3 T05H10.6
            ATH: AT5G50850
            OSA: 4330673 4334968 4340640 4346159 4347531 4352803
            CME: CMS327C CMT256C
            SCE: YBR221C(PDB1) YER178W(PDA1)
            AGO: AGOS_AAR167C AGOS_AGR103W
            PIC: PICST_68238(PDB1) PICST_80322(PDA1)
            CGR: CAGL0K06831g CAGL0L12078g
            SPO: SPAC26F1.03 SPBC30D10.13c(pdb1)
            ANI: AN5162.2 AN9403.2
            AFM: AFUA_1G06960 AFUA_3G04170
            AOR: AO090003000290 AO090012000948 AO090124000079
            CNE: CNF04450 CNL05600
            UMA: UM03854.1 UM06105.1
            ECU: ECU09_1040
            DDI: DDB_0229442(pdhB) DDB_0230185(bkdB) DDB_0230193(pdhA)
            PFA: PF11_0256 PF14_0441
            TET: TTHERM_00193230 TTHERM_00784570 TTHERM_00979780
            TBR: Tb10.389.0890 Tb10.70.2900 Tb927.3.1790
            TCR: 506295.160 507831.70 510091.80 510421.320 511261.160
                 511469.100
            LMA: LmjF18.1380 LmjF25.1710 LmjF35.0050
            ECO: b0114(aceE)
            ECJ: JW0110(aceE)
            ECE: Z0124(aceE)
            ECS: ECs0118
            ECC: c0142(aceE)
            ECI: UTI89_C0127(aceE) UTI89_C3373(neuD)
            ECP: ECP_0121
            ECV: APECO1_1871(aceE)
            ECW: EcE24377A_0116(aceE)
            ECX: EcHS_A0118
            STY: STY0175(aceE)
            STT: t0158(aceE)
            SPT: SPA0156(aceE)
            SEC: SC0151(aceE)
            STM: STM0152(aceE)
            YPE: YPO3419(aceE)
            YPK: y0767(aceE)
            YPM: YP_0265(aceE)
            YPA: YPA_2921
            YPN: YPN_0669
            YPP: YPDSF_2935
            YPS: YPTB0713(aceE)
            YPI: YpsIP31758_3363(aceE)
            YEN: YE0699(aceE)
            SFL: SF0111(aceE)
            SFX: S0113(aceE)
            SFV: SFV_0105(aceE)
            SSN: SSON_0122(aceE)
            SBO: SBO_0103(aceE)
            SDY: SDY_0144(aceE)
            ECA: ECA3789(aceE)
            PLU: plu3623(aceE)
            BUC: BU205(aceE)
            BAS: BUsg199(aceE)
            BAB: bbp189(aceE)
            BCC: BCc_131(aceE)
            WBR: WGLp323(aceE)
            SGL: SG0467
            SPE: Spro_4011
            BFL: Bfl153(aceE)
            BPN: BPEN_158(aceE)
            HIN: HI1233(aceE)
            HIT: NTHI1933(aceE)
            HDU: HD1625(aceE)
            HSO: HS_1095(aceE)
            PMU: PM0895(aceE)
            MSU: MS1336(aceE)
            APL: APL_0773(aceE)
            XFA: XF0669
            XFT: PD1505(aceE)
            XCC: XCC0429(pdhB) XCC0430(pdhA) XCC3625(aceE)
            XCB: XC_0443 XC_0444 XC_0588
            XCV: XCV0475 XCV0476 XCV0611(aceE)
            XAC: XAC0445(pdhB) XAC0446(pdhA) XAC0576(aceE)
            XOO: XOO4077(pdhA) XOO4078(pdhB) XOO4081(pdhB) XOO4248(aceE)
            XOM: XOO_3852(XOO3852) XOO_3853(XOO3853) XOO_3855(XOO3855)
                 XOO_4010(XOO4010)
            VCH: VC2414
            VCO: VC0395_A1990(aceE)
            VVU: VV1_1630 VV2_0469 VV2_0470
            VVY: VV2773 VVA1021 VVA1022
            VPA: VP2519 VPA0646 VPA0647
            VFI: VF2180 VF2181
            PPR: PBPRA3196 PBPRB1094 PBPRB1095
            PAE: PA3416 PA3417 PA4150 PA4151(acoB) PA5015(aceE)
            PAU: PA14_10250(acoB) PA14_10260(acoA) PA14_19900 PA14_19910(pdhB)
                 PA14_66290(aceA)
            PAP: PSPA7_1709(pdhA) PSPA7_5751(aceE)
            PPU: PP_0339(aceE) PP_0554(acoB) PP_0555(acoA)
            PPF: Pput_0364 Pput_0594
            PST: PSPTO_3860(aceE-1) PSPTO_5005(aceE-2)
            PSB: Psyr_0518 Psyr_1625
            PSP: PSPPH_0508(aceE1)
            PFL: PFL_0509(aceE) PFL_2170(acoA) PFL_2171(acoB) PFL_3977(aceE)
            PFO: Pfl_0463
            PEN: PSEEN4514(mdeB) PSEEN5145(aceE)
            PMY: Pmen_0576 Pmen_3247
            PAR: Psyc_1328(aceE-2)
            PCR: Pcryo_1050
            PRW: PsycPRwf_1404
            ACI: ACIAD1017(acoA) ACIAD1018(acoB) ACIAD3507(aceE)
            SON: SO_0424(aceE)
            SDN: Sden_3383
            SFR: Sfri_0318 Sfri_0319 Sfri_3777
            SAZ: Sama_0375
            SBL: Sbal_3913
            SBM: Shew185_3934
            SLO: Shew_3431
            SPC: Sputcn32_3417
            SSE: Ssed_0431 Ssed_2175
            SHE: Shewmr4_0428
            SHM: Shewmr7_3599
            SHN: Shewana3_0426
            SHW: Sputw3181_0526
            ILO: IL0458(aceE)
            CPS: CPS_3051(acoB) CPS_3052(acoA) CPS_4808(aceE)
            PHA: PSHAa0391(aceE)
            PAT: Patl_1115 Patl_3350
            SDE: Sde_2573
            PIN: Ping_3601
            MAQ: Maqu_3328
            CBU: CBU_0461(pdhA) CBU_0639 CBU_0640 CBU_0692 CBU_0693
            CBD: COXBU7E912_0650(pdhB) COXBU7E912_0651(pdhA)
                 COXBU7E912_0700(pdhAB) COXBU7E912_1614(aceE)
            LPN: lpg1504(aceE) lpg1558 lpg1559
            LPF: lpl1467 lpl1468 lpl1522(aceE)
            LPP: lpp1461(aceE) lpp1515 lpp1516
            MCA: MCA3000(aceE)
            FTU: FTT1485c(aceE)
            FTF: FTF1485c(aceE)
            FTW: FTW_0808(aceE)
            FTL: FTL_0309
            FTH: FTH_0310(aceE)
            FTA: FTA_0328
            FTN: FTN_1494(aceE)
            TCX: Tcr_1001
            NOC: Noc_1254 Noc_1434 Noc_1435 Noc_2110 Noc_2111
            AEH: Mlg_0269
            HHA: Hhal_1037
            HCH: HCH_01272(aceE) HCH_03687 HCH_06123
            CSA: Csal_0855
            ABO: ABO_0622(aceE)
            MMW: Mmwyl1_2307
            AHA: AHA_2866 AHA_2867 AHA_3863
            DNO: DNO_0544(aceE)
            BCI: BCI_0512(aceE)
            VOK: COSY_0425(aceE)
            NME: NMB1341
            NMA: NMA1554(aceE)
            NMC: NMC1278(aceE)
            NGO: NGO0565
            CVI: CV_0526(aceE)
            RSO: RSc1600(aceE) RSc1797(RS04198) RSc1798(RS04199)
            REU: Reut_A1303 Reut_B4683 Reut_B4976 Reut_B4977 Reut_B5550
                 Reut_B5551
            REH: H16_A1374(pdhA1) H16_A1753(pdhA2) H16_B0145(acoB)
                 H16_B1300(aceE) H16_B2234(bkdA2)
            RME: Rmet_1196 Rmet_4133 Rmet_4134 Rmet_4263
            BMA: BMA1721(aceE) BMAA1737
            BMV: BMASAVP1_1035 BMASAVP1_A2230(aceE)
            BML: BMA10299_1321 BMA10299_A3090(aceE)
            BMN: BMA10247_1502(pdhA) BMA10247_A2301
            BXE: Bxe_A1541 Bxe_A4472 Bxe_B0313 Bxe_B0314 Bxe_C0856 Bxe_C0857
                 Bxe_C1063
            BVI: Bcep1808_1766 Bcep1808_2217
            BUR: Bcep18194_A5139 Bcep18194_A5140 Bcep18194_A5443
                 Bcep18194_B1007 Bcep18194_B1009
            BCN: Bcen_5940 Bcen_6240
            BCH: Bcen2424_1839 Bcen2424_2137 Bcen2424_3245
            BAM: Bamb_1776 Bamb_1777 Bamb_2174
            BPS: BPSL2301(pdhA) BPSS1711(aceE)
            BPM: BURPS1710b_2746(aceE) BURPS1710b_A0783(aceE)
                 BURPS1710b_A1410(bkdA2)
            BPL: BURPS1106A_2667(pdhA)
            BPD: BURPS668_2612(pdhA)
            BTE: BTH_I1864 BTH_II0237 BTH_II0238 BTH_II0670 BTH_II0928
                 BTH_II0929
            PNU: Pnuc_0734
            BPE: BP0628 BP0629(pdhA) BP0993(aceE) BP1121(aceE)
            BPA: BPP1462(aceE) BPP3220(aceE)
            BBR: BB2536(aceE) BB3672(aceE) BB4704A BB4705(pdhA)
            RFR: Rfer_0386 Rfer_0387 Rfer_2212 Rfer_3650 Rfer_3965 Rfer_3966
            POL: Bpro_0762 Bpro_0763 Bpro_2672 Bpro_3831
            PNA: Pnap_1781
            VEI: Veis_1919 Veis_2230
            MPT: Mpe_A0874 Mpe_A1601 Mpe_A1602 Mpe_A2128
            HAR: HEAR0746(aceE)
            MMS: mma_0673 mma_1883
            NEU: NE0361(aceE)
            NET: Neut_1608
            NMU: Nmul_A0358
            EBA: ebA133(aceE) ebA2186 ebA2187
            AZO: azo1373(pdhA)
            DAR: Daro_0442 Daro_3700 Daro_3701
            TBD: Tbd_0654 Tbd_0655
            MFA: Mfla_2074
            ABU: Abu_1472(aceE)
            GSU: GSU2436 GSU2443 GSU2654(pdhA) GSU2655(pdhB)
            GME: Gmet_2509 Gmet_2510 Gmet_2753 Gmet_2760
            GUR: Gura_1266 Gura_1609 Gura_2900
            PCA: Pcar_0343 Pcar_0344
            PPD: Ppro_1024 Ppro_1027
            BBA: Bd0394(ace)
            DPS: DP2095(phdB) DP2096(phdB) DPPB38 DPPB39
            ADE: Adeh_2130 Adeh_2441
            AFW: Anae109_4128
            MXA: MXAN_2666(pdhA) MXAN_2667(pdhB)
            SFU: Sfum_0448 Sfum_2647 Sfum_2648
            RPR: RP261(pdhA) RP262(pdhB)
            RTY: RT0252(pdhA) RT0253(pdhB)
            RCO: RC0347(pdhA) RC0348(pdhB)
            RFE: RF_1019(pdhB) RF_1020(pdhA)
            RBE: RBE_0259(pdhA) RBE_0260(pdhB)
            RAK: A1C_01890
            RBO: A1I_06500
            RCM: A1E_01525
            RRI: A1G_01990
            WOL: WD0416(pdhA) WD0473
            WBM: Wbm0207 Wbm0666
            AMA: AM101(pdhA) AM1351(pdhB)
            APH: APH_0082(pdhA) APH_1308
            ERU: Erum0980(pdhB) Erum7520(pdhA)
            ERW: ERWE_CDS_00950(pdhB) ERWE_CDS_07920(pdhA)
            ERG: ERGA_CDS_00910(pdhB) ERGA_CDS_07830(pdhA)
            ECN: Ecaj_0098 Ecaj_0786
            ECH: ECH_0149 ECH_0220(pdhA)
            NSE: NSE_0746 NSE_0802(pdhA)
            PUB: SAR11_0429(aceE)
            MLO: mll3628 mll3629 mlr0383 mlr0384 mlr9539
            MES: Meso_1629 Meso_1630
            PLA: Plav_3141
            SME: SMc01030(pdhAa) SMc01031(pdhAb)
            ATU: Atu1429(pdhA) Atu1430(pdhB)
            ATC: AGR_C_2636 AGR_C_2638
            RET: RHE_CH01933(pdhA1) RHE_CH01934(pdhA2)
            RLE: RL2241(pdhA) RL2242(pdhB)
            BME: BMEI0854 BMEI0855
            BMF: BAB1_1151 BAB1_1152
            BMS: BR1128(pdhB) BR1129(pdhA)
            BMB: BruAb1_1134(pdhB) BruAb1_1135(pdhA)
            BOV: BOV_1086(pdhB) BOV_1087(pdhA)
            OAN: Oant_4117
            BJA: bll4782(pdhB) bll4783(pdhA) blr2815 blr3720
            BRA: BRADO4086(pdhB) BRADO4087(pdhA)
            BBT: BBta_4462(pdhB) BBta_4463(pdhA)
            RPA: RPA2866 RPA2867 RPA3922 RPA3923
            RPB: RPB_2770 RPB_2771 RPB_3251 RPB_3807 RPB_3808
            RPC: RPC_2489 RPC_2490
            RPD: RPD_2214 RPD_2811 RPD_2812
            RPE: RPE_2612 RPE_2614
            NWI: Nwi_1817 Nwi_1818
            NHA: Nham_1749 Nham_3109
            BHE: BH05750(pdhA) BH05760(pdhB)
            BQU: BQ04910(pdhA) BQ04920(pdhB)
            BBK: BARBAKC583_0534(pdhA) BARBAKC583_0535(pdhB)
            XAU: Xaut_0214 Xaut_3888 Xaut_4045
            CCR: CC_1205 CC_1726 CC_1727
            SIL: SPO2240(pdhA) SPO2241(pdhB) SPO3791(acoB) SPO3792(acoA)
                 SPOA0319
            SIT: TM1040_1078 TM1040_1079 TM1040_2736
            RSP: RSP_3974 RSP_4047(pdhAa) RSP_4049(pdhAb)
            RSH: Rsph17029_1149
            RSQ: Rsph17025_1094
            JAN: Jann_1691
            RDE: RD1_3011(pdhA) RD1_3013(pdhB)
            PDE: Pden_3892 Pden_4985
            MMR: Mmar10_1415
            HNE: HNE_1976(pdhB) HNE_1977(pdhA) HNE_2995
            ZMO: ZMO1605(pdhB) ZMO1606(pdhA)
            NAR: Saro_1908 Saro_1909
            SAL: Sala_0525 Sala_0526
            SWI: Swit_0346 Swit_0839 Swit_1057 Swit_1224 Swit_2270 Swit_5154
            ELI: ELI_06400 ELI_06405
            GOX: GOX2289 GOX2290
            GBE: GbCGDNIH1_1183 GbCGDNIH1_1184
            ACR: Acry_2013 Acry_2819
            RRU: Rru_A1880 Rru_A1881
            MAG: amb2316 amb2317
            ABA: Acid345_2792
            SUS: Acid_0352 Acid_2937
            BSU: BG10207(pdhA) BG10208(pdhB) BG12558(acoA) BG12559(acoB)
            BHA: BH0213 BH0214 BH0776 BH0777 BH1822(acoA) BH1823(acoB)
                 BH2654(pdhB) BH2655(pdhA)
            BAN: BA2775(acoB) BA2776(acoA) BA4183(pdhB) BA4184(pdhA)
            BAR: GBAA2775(acoB) GBAA2776(acoA) GBAA4183(pdhB) GBAA4184(pdhA)
            BAA: BA_3299 BA_3300 BA_4649 BA_4650
            BAT: BAS2587 BAS2588 BAS3882 BAS3883
            BCE: BC2778 BC2779 BC3972 BC3973
            BCA: BCE_2803(acoB) BCE_2804(acoA) BCE_4020(pdhB) BCE_4021(pdhA)
            BCZ: BCZK2504(acoB) BCZK2505(acoA) BCZK3730(pdhB) BCZK3731(pdhA)
                 BCZK4414(acuC)
            BCY: Bcer98_2674
            BTK: BT9727_2538(acoB) BT9727_2539(acoA) BT9727_3714(pdhB)
                 BT9727_3715(pdhA) BT9727_4397(acuC)
            BLI: BL01616(pdhA) BL01617(pdhB) BL03012(acoA) BL03013(acoB)
            BLD: BLi00849(acoA) BLi00850(acoB) BLi01674(pdhA) BLi01675(pdhB)
            BCL: ABC2419(pdhB) ABC2420(pdhA) ABC2785(acoB)
            BAY: RBAM_014420 RBAM_014430
            BPU: BPUM_1171 BPUM_1172 BPUM_1355 BPUM_1356
            OIH: OB1412(pdhA) OB1413(pdhB) OB2876 OB2877
            GKA: GK0710 GK0711 GK1058 GK1059 GK2024 GK2027 GK3216 GK3217
            SAU: SA0943-1(pdhA) SA0944(phdB)
            SAV: SAV1093(pdhA) SAV1094(phdB)
            SAM: MW0976 MW0977(phdB)
            SAR: SAR1067(pdhA) SAR1068(pdhB)
            SAS: SAS1028 SAS1029
            SAC: SACOL1102(pdhA) SACOL1103(pdhB) SACOL1561 SACOL1562
            SAB: SAB0959(pdhA) SAB0960(pdhB)
            SAA: SAUSA300_0993(pdhA) SAUSA300_0994(pdhB) SAUSA300_1465
                 SAUSA300_1466
            SAO: SAOUHSC_01040 SAOUHSC_01041 SAOUHSC_01612
            SAJ: SaurJH9_1153
            SAH: SaurJH1_1175
            SEP: SE0254 SE0255 SE0791 SE0792
            SER: SERP0680(pdhA) SERP0681(pdhB) SERP1077 SERP1078
            SHA: SH0224 SH0225 SH1858(phdB) SH1859
            SSP: SSP1695 SSP1696
            LMO: lmo1052(pdhA) lmo1053(PdhB)
            LMF: LMOf2365_1073(pdhA) LMOf2365_1074(pdhB) LMOf2365_1390
            LIN: lin1044(pdhA) lin1045(PdhB)
            LWE: lwe1028(pdhA) lwe1029(pdhB)
            LLA: L0033(pdhA) L0034(pdhB)
            LLC: LACR_0050 LACR_0051
            LLM: llmg_0073(pdhB) llmg_0074(pdhA)
            SPY: SPy_1026(acoA) SPy_1028(acoB)
            SPZ: M5005_Spy_0751(acoA) M5005_Spy_0752(acoB)
            SPM: spyM18_1009(acoA) spyM18_1010(acoB)
            SPG: SpyM3_0661(acoA) SpyM3_0662(acoB)
            SPS: SPs1191 SPs1192
            SPH: MGAS10270_Spy0869(acoA) MGAS10270_Spy0870(acoB)
            SPI: MGAS10750_Spy0903(acoA) MGAS10750_Spy0904(acoB)
            SPJ: MGAS2096_Spy0824(acoA) MGAS2096_Spy0825(acoB)
            SPK: MGAS9429_Spy0865(acoA) MGAS9429_Spy0866(acoB)
            SPF: SpyM51007(pdhB) SpyM51008(pdhA)
            SPA: M6_Spy0776 M6_Spy0777
            SPB: M28_Spy0730(acoA) M28_Spy0731(acoB)
            SPN: SP_1163 SP_1164
            SPR: spr1050(acoB) spr1051(acoA)
            SAG: SAG0878 SAG0879
            SAN: gbs0895 gbs0896
            SAK: SAK_1001 SAK_1002
            SMU: SMU.127(adhA) SMU.128(adhB) SMU.1422(pdhB) SMU.1423(pdhA)
            STC: str1050(acoB) str1051(acoA)
            STL: stu1050(acoB) stu1051(acoA)
            SSA: SSA_1138(pdhA) SSA_1139(pdhB) SSA_1176(acoB) SSA_1178(acoA)
            LPL: lp_2153(pdhB) lp_2154(pdhA)
            LSA: LSA1084(pdhB) LSA1085(pdhA)
            LSL: LSL_0153(acoA) LSL_0154(acoB)
            LBR: LVIS_1409 LVIS_1410
            LCA: LSEI_1305 LSEI_1306
            LRE: Lreu_0631
            EFA: EF1353(pdhA) EF1354(pdhB)
            OOE: OEOE_0328 OEOE_0329
            STH: STH411 STH412
            CKL: CKL_2270(pdhB) CKL_2271(pdhA)
            AMT: Amet_1251
            TTE: TTE0186(acoA) TTE0187(acoB) TTE0688(acoA2) TTE0689(acoB2)
            MGE: MG_273(pdhB) MG_274(pdhA)
            MPN: MPN392(pdhB) MPN393(pdhA)
            MPU: MYPU_7630(pdhB) MYPU_7640(pdhA)
            MPE: MYPE5080(pdhA) MYPE5090(pdhB)
            MGA: MGA_0164(acoB) MGA_0165(acoA)
            MMY: MSC_0265(pdhA) MSC_0266(pdhB)
            MMO: MMOB5830(pdhB) MMOB5840(pdhA)
            MHY: mhp264(pdhB) mhp265(pdhA)
            MHJ: MHJ_0111(pdhA) MHJ_0112(pdhB)
            MHP: MHP7448_0115(pdhA) MHP7448_0116(pdhB)
            MSY: MS53_0272(pdhA) MS53_0273(pdhB)
            MCP: MCAP_0225(pdhA) MCAP_0226(pdhB)
            POY: PAM600(acoA) PAM601(acoB)
            AYW: AYWB_136(acoA) AYWB_137(acoB)
            MFL: Mfl039 Mfl040
            MTU: Rv0843 Rv2241(aceE) Rv2496c(pdhB) Rv2497c(pdhA)
            MTC: MT0865 MT2301(aceE) MT2571 MT2572
            MBO: Mb0866 Mb2265(aceE) Mb2524c(pdhB) Mb2525c(pdhA)
            MBB: BCG_2258(aceE) BCG_2516c(pdhB) BCG_2517c(pdhA)
            MLE: ML1651(aceE)
            MPA: MAP0688 MAP1487c MAP1488c MAP1994(aceE) MAP2308c(pdhB)
                 MAP2309c(pdhA)
            MAV: MAV_1675 MAV_1676 MAV_2196
            MSM: MSMEG_4323 MSMEG_4711 MSMEG_4712
            MVA: Mvan_0911 Mvan_1408 Mvan_4086
            MMC: Mmcs_1091 Mmcs_1092 Mmcs_3362 Mmcs_3625 Mmcs_3626
            MKM: Mkms_1108 Mkms_3699
            MJL: Mjls_1119 Mjls_3631
            CGL: NCgl2167(aceE)
            CGB: cg2466(aceE)
            CEF: CE2143
            CDI: DIP1687(aceE)
            CJK: jk0661(aceE)
            NFA: nfa10210 nfa10220 nfa16130(aceE)
            RHA: RHA1_ro00542 RHA1_ro01197(aceE1) RHA1_ro01576(pdhA1)
                 RHA1_ro01577 RHA1_ro02566(aceE2) RHA1_ro03301 RHA1_ro03305
                 RHA1_ro03320(pdhB1) RHA1_ro03321(pdhA2) RHA1_ro03379(pdhB2)
                 RHA1_ro03380(pdhA3) RHA1_ro08623 RHA1_ro08624 RHA1_ro11030
                 RHA1_ro11031
            SCO: SCO1269(2SCG18.16c) SCO1270(2SCG18.17c) SCO2183(aceE1)
                 SCO2371(aceE2) SCO3816(bkdB1) SCO3817(bkdA1) SCO3830(bkdB2)
                 SCO3831(bkdA2) SCO7124(aceE3)
            SMA: SAV4362(bkdA) SAV4363(bkdB) SAV4376(bkdF) SAV4377(bkdG)
                 SAV5800(aceE1) SAV6020(aceE2)
            TWH: TWT255(aceE) TWT789(pdhB) TWT790(pdhA)
            TWS: TW515(aceE) TW798(pdhB)
            LXX: Lxx12700(aceE) Lxx25060(pdhB) Lxx25070(pdhA)
            CMI: CMM_1621(aceE)
            ART: Arth_0510 Arth_1381 Arth_2564 Arth_3193 Arth_4028
            AAU: AAur_1521 AAur_1912(aceE) AAur_2539 AAur_3391 AAur_3892
            PAC: PPA0989 PPA2093 PPA2094
            NCA: Noca_3769 Noca_4509 Noca_4858
            TFU: Tfu_0180 Tfu_0181 Tfu_3049 Tfu_3050
            FRA: Francci3_0057 Francci3_0058 Francci3_1895 Francci3_2487
                 Francci3_2488 Francci3_2785 Francci3_3057
            FAL: FRAAL0070 FRAAL0071 FRAAL3039(pdhA) FRAAL3040(pdhB) FRAAL3227
                 FRAAL3228 FRAAL4280 FRAAL5051(aceE)
            ACE: Acel_0032 Acel_0033 Acel_0589 Acel_0590 Acel_1046
            KRA: Krad_4288
            SEN: SACE_1532(aceE) SACE_2406(phdB) SACE_2407(phdB) SACE_3884
                 SACE_3952(pdhA2) SACE_3953(pdhB1) SACE_4754(acoA)
                 SACE_4755(acoB) SACE_5542(bkdA) SACE_5543(pdhB1) SACE_5675
                 SACE_5676 SACE_7294 SACE_7295(pdhB2)
            STP: Strop_0109 Strop_2097 Strop_3373
            RXY: Rxyl_0348 Rxyl_2324 Rxyl_2325 Rxyl_2403 Rxyl_2404 Rxyl_3050
            RBA: RB3424
            CTR: CT245(pdhA) CT246(pdhB)
            CTA: CTA_0267(pdhA_1) CTA_0268(pdhB)
            CMU: TC0516 TC0517
            CPN: CPn0304(pdhA) CPn0305(pdhB)
            CPA: CP0453 CP0454
            CPJ: CPj0304(pdhA) CPj0305(pdhB)
            CPT: CpB0313 CpB0314
            CCA: CCA00477(pdhB) CCA00478(pdhA)
            CAB: CAB463(pdhB) CAB464(pdhA)
            CFE: CF0529(pdhA) CF0530(pdhB)
            PCU: pc1732(pdhB) pc1733(pdhA)
            LIL: LA2009(aceE1) LA2010(aceE2)
            LIC: LIC11897(acoA) LIC11898(acoB)
            LBJ: LBJ_1966(acoA) LBJ_1967(acoB)
            LBL: LBL_1317(acoB) LBL_1318(acoA)
            SYN: sll1721(pdhB) slr1934
            SYW: SYNW1055(pdhB) SYNW1620(pdhA)
            SYC: syc1362_d(pdhB) syc2150_c(pdhA)
            SYF: Synpcc7942_0143 Synpcc7942_1944
            SYD: Syncc9605_0880 Syncc9605_1190
            SYE: Syncc9902_1280 Syncc9902_1519
            SYG: sync_0764(pdhA) sync_1590(pdhB)
            SYR: SynRCC307_1312(pdhB) SynRCC307_1706(pdhA)
            SYX: SynWH7803_1363(pdhB) SynWH7803_1734(pdhA)
            CYA: CYA_0519 CYA_2326
            CYB: CYB_0299 CYB_1765
            TEL: tll0204 tlr1169
            GVI: glr1529 glr1530 glr2844 glr2846
            ANA: all0122 alr2708
            AVA: Ava_1491 Ava_4276
            PMA: Pro0766(acoB) Pro1362(acoA)
            PMM: PMM0930(pdhB) PMM1229 PMM1288(pdhA)
            PMT: PMT0347(pdhA) PMT0618(pdhB)
            PMN: PMN2A_0855
            PMI: PMT9312_1302 PMT9312_1303 PMT9312_1384
            PMB: A9601_09301(pdhB) A9601_14871(acoA)
            PMC: P9515_10131(pdhB) P9515_14491(acoA)
            PMF: P9303_01031 P9303_01041 P9303_16211(pdhB) P9303_19591(acoA)
            PMG: P9301_09281(pdhB) P9301_14731(acoA)
            PME: NATL1_09511(pdhB) NATL1_17081(acoA)
            TER: Tery_5066 Tery_5078
            SRU: SRU_1970 SRU_1971
            CHU: CHU_2680(adhB) CHU_3718(acoA)
            GFO: GFO_0294(pdhB) GFO_1681(aceE) GFO_2889(pdhA)
            FJO: Fjoh_1553
            FPS: FP0337(pdhB) FP1385(pdhA)
            RRS: RoseRS_1728 RoseRS_2415
            RCA: Rcas_2013 Rcas_3063
            DRA: DR_0257
            DGE: Dgeo_1561 Dgeo_1562 Dgeo_1887 Dgeo_2338
            TTH: TTC0568 TTC0569 TTC1801
            TTJ: TTHA0185 TTHA0938 TTHA0939
            HAL: VNG1926G(pdhA1) VNG2217G(pdhA2) VNG2218G(pdhB)
            HMA: rrnAC0149(pdhA1) rrnAC2956(pdhB1) rrnAC2957(pdhA3)
                 rrnB0199(pdhB2) rrnB0200(pdhA2)
            NPH: NP0558A(oxdhB) NP0560A(oxdhA_1)
            TAC: Ta1437 Ta1438
            TVO: TVN0101 TVN0102
            PTO: PTO0548 PTO0549
            RCI: RRC126(pdhB) RRC128(pdhA)
            APE: APE_1674 APE_1677.1
            SSO: SSO1369(pdhA-1) SSO1370(pdhB-1) SSO1525(pdhA-2)
                 SSO1526(pdhB-2)
            MSE: Msed_1213
            PAI: PAE2644 PAE2646
            PCL: Pcal_1405
            PAS: Pars_1189
STRUCTURES  PDB: 1L8A  1NI4  1RP7  1W85  1W88  2G25  2G28  2G67  2IEA  2OZL  
                 2QTA  2QTC  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.4.1
            ExPASy - ENZYME nomenclature database: 1.2.4.1
            ExplorEnz - The Enzyme Database: 1.2.4.1
            ERGO genome analysis and discovery system: 1.2.4.1
            BRENDA, the Enzyme Database: 1.2.4.1
            CAS: 9014-20-4
///
ENTRY       EC 1.2.4.2                  Enzyme
NAME        oxoglutarate dehydrogenase (succinyl-transferring);
            2-ketoglutarate dehydrogenase;
            2-oxoglutarate dehydrogenase;
            2-oxoglutarate: lipoate oxidoreductase;
            2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and
            acceptor-succinylating);
            alpha-ketoglutarate dehydrogenase;
            alphaketoglutaric acid dehydrogenase;
            alpha-ketoglutaric dehydrogenase;
            alpha-oxoglutarate dehydrogenase;
            AKGDH;
            OGDC;
            ketoglutaric dehydrogenase;
            oxoglutarate decarboxylase;
            oxoglutarate dehydrogenase;
            oxoglutarate dehydrogenase (lipoamide)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With a disulfide as acceptor
SYSNAME     2-oxoglutarate:[dihydrolipoyllysine-residue
            succinyltransferase]-lipoyllysine 2-oxidoreductase (decarboxylating,
            acceptor-succinylating)
REACTION    2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase]
            lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase]
            S-succinyldihydrolipoyllysine + CO2 [RN:R01700]
ALL_REAC    R01700;
            (other) R00621 R01933 R01940 R03316
SUBSTRATE   2-oxoglutarate [CPD:C00026];
            [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
PRODUCT     [dihydrolipoyllysine-residue succinyltransferase]
            S-succinyldihydrolipoyllysine [CPD:C16254];
            CO2 [CPD:C00011]
COFACTOR    Thiamin diphosphate [CPD:C00068]
COMMENT     Contains thiamine diphosphate. It is a component of the multienzyme
            2-oxoglutarate dehydrogenase complex in which multiple copies of it
            are bound to a core of molecules of EC 2.3.1.61,
            dihydrolipoyllysine-residue succinyltransferase, which also binds
            multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does
            not act on free lipoamide or lipoyllysine, but only on the
            lipoyllysine residue in EC 2.3.1.61.
REFERENCE   1
  AUTHORS   Massey, V.
  TITLE     The composition of the ketoglutarate dehydrogenase complex.
  JOURNAL   Biochim. Biophys. Acta 38 (1960) 447-460.
  ORGANISM  pig [GN:ssc], Escherichia coli [GN:eco]
REFERENCE   2  [PMID:13158180]
  AUTHORS   OCHOA S.
  TITLE     Enzymic mechanisms in the citric acid cycle.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 15 (1954) 183-270.
REFERENCE   3  [PMID:12981117]
  AUTHORS   SANADI DR, LITTLEFIELD JW, BOCK RM.
  TITLE     Studies on alpha-ketoglutaric oxidase.  II.  Purification and
            properties.
  JOURNAL   J. Biol. Chem. 197 (1952) 851-62.
  ORGANISM  pigeon, pig [GN:ssc]
REFERENCE   4  [PMID:10966480]
  AUTHORS   Perham RN.
  TITLE     Swinging arms and swinging domains in multifunctional enzymes:
            catalytic machines for multistep reactions.
  JOURNAL   Annu. Rev. Biochem. 69 (2000) 961-1004.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00310  Lysine degradation
            PATH: map00380  Tryptophan metabolism
ORTHOLOGY   KO: K00164  2-oxoglutarate dehydrogenase E1 component
GENES       HSA: 4967(OGDH) 55753(OGDHL)
            MMU: 18293(Ogdh) 239017(Ogdhl)
            RNO: 290566(Ogdhl_predicted)
            CFA: 477748(OGDHL)
            GGA: 423618(OGDHL) 426429(RCJMB04_19j12)
            XLA: 399021(MGC68800) 444121(MGC80496)
            SPU: 587800(LOC587800)
            DME: Dmel_CG11661(Nc73EF)
            CEL: T22B11.5 ZK836.2
            ATH: AT3G55410 AT5G65750
            OSA: 4335673
            CME: CMF068C
            SCE: YIL125W(KGD1)
            AGO: AGOS_AER374C
            PIC: PICST_79721(KGD1)
            CGR: CAGL0G08712g
            SPO: SPBC3H7.03c
            ANI: AN5571.2
            AFM: AFUA_4G11650
            AOR: AO090003001055
            CNE: CNB01730
            UMA: UM04452.1
            DDI: DDBDRAFT_0219311
            PFA: PF08_0045 PF13_0070
            TAN: TA05275
            TPV: TP03_0124
            TET: TTHERM_00193640 TTHERM_00268070 TTHERM_00954380
            TBR: Tb11.01.1740
            TCR: 506337.70 510717.30
            LMA: LmjF36.3470
            ECO: b0726(sucA)
            ECJ: JW0715(sucA)
            ECE: Z0880(sucA)
            ECS: ECs0751
            ECC: c0803(sucA) c5032
            ECI: UTI89_C0721(sucA) UTI89_C4630
            ECP: ECP_0737 ECP_4274
            ECV: APECO1_2410
            ECW: EcE24377A_0752(sucA)
            ECX: EcHS_A0773(sucA)
            STY: STY0779(sucA)
            STT: t2140(sucA)
            SPT: SPA2007(sucA)
            SEC: SC0740(sucA)
            STM: STM0736(sucA)
            YPE: YPO1113(sucA)
            YPK: y3067(sucA)
            YPM: YP_1043(sucA)
            YPA: YPA_0591
            YPN: YPN_2885
            YPP: YPDSF_2584
            YPS: YPTB1147(sucA)
            YPI: YpsIP31758_2881(sucA)
            SFL: SF0571(sucA)
            SFX: S0584(sucA)
            SFV: SFV_0610(sucA)
            SSN: SSON_0677(sucA)
            SBO: SBO_0584(sucA)
            SDY: SDY_0664(sucA)
            ECA: ECA1361(sucA)
            PLU: plu1430(sucA)
            BUC: BU302(sucA)
            BAS: BUsg292(sucA)
            BAB: bbp280(sucA)
            BCC: BCc_184(sucA)
            WBR: WGLp419(sucA)
            SGL: SG0876
            ENT: Ent638_1226
            SPE: Spro_1267
            BFL: Bfl331(sucA)
            BPN: BPEN_341(sucA)
            HIT: NTHI1964(sucA)
            HIP: CGSHiEE_03745(kgd)
            HIQ: CGSHiGG_02060(kgd)
            HDU: HD1336(sucA)
            HSO: HS_0959(sucA)
            PMU: PM0277(sucA)
            MSU: MS1355(sucA)
            APL: APL_0455(sucA)
            XFA: XF1550
            XFT: PD0760(odhA)
            XCC: XCC1487(odhA)
            XCB: XC_2749
            XCV: XCV1578(sucA)
            XAC: XAC1535(odhA)
            XOO: XOO2044(odhA)
            XOM: XOO_1925(XOO1925)
            VCH: VC2087
            VCO: VC0395_A1673(sucA)
            VVU: VV1_0157
            VVY: VV1032
            VPA: VP0847
            VFI: VF0823
            PPR: PBPRA1048
            PAE: PA1585(sucA)
            PAU: PA14_44010(sucA)
            PAP: PSPA7_3689(sucA)
            PPU: PP_4189(kgdA)
            PPF: Pput_1665
            PST: PSPTO_2199(sucA)
            PSB: Psyr_2009
            PSP: PSPPH_1980(sucA)
            PFL: PFL_1718(sucA)
            PFO: Pfl_1614
            PEN: PSEEN3640(sucA)
            PAR: Psyc_0102(sucA)
            PCR: Pcryo_0111
            PRW: PsycPRwf_0266
            ACI: ACIAD2876(sucA)
            ACB: A1S_2715
            SON: SO_1930(sucA)
            SDN: Sden_2183
            SFR: Sfri_2343
            SAZ: Sama_1427
            SLO: Shew_1655
            SPC: Sputcn32_2269
            SSE: Ssed_2814
            SPL: Spea_1788
            SHE: Shewmr4_1635
            SHM: Shewmr7_1710
            SHN: Shewana3_1710 Shewana3_2472
            SHW: Sputw3181_1739
            ILO: IL1503(sucA)
            CPS: CPS_2219(sucA)
            PHA: PSHAa1647(sucA)
            PAT: Patl_1799
            SDE: Sde_2106
            PIN: Ping_2252
            MAQ: Maqu_1154
            CBU: CBU_1399(sucA)
            CBD: COXBU7E912_0594(sucA)
            LPN: lpg0532(sucA)
            LPF: lpl0578(sucA)
            LPP: lpp0597(sucA)
            MCA: MCA1952(sucA)
            FTU: FTT0076(sucA)
            FTF: FTF0076(sucA)
            FTW: FTW_0152(sucA1)
            FTL: FTL_1784
            FTH: FTH_1720(sucA)
            FTA: FTA_1890(sucA)
            FTN: FTN_1635(sucA)
            NOC: Noc_0111
            AEH: Mlg_2609
            HHA: Hhal_1086
            HCH: HCH_04745(sucA)
            CSA: Csal_1217
            ABO: ABO_1496(sucA)
            AHA: AHA_1927(sucA)
            DNO: DNO_0329(sucA)
            NME: NMB0955
            NMA: NMA1149(sucA)
            NMC: NMC0931(sucA)
            NGO: NGO0917
            CVI: CV_1071(sucA)
            RSO: RSc1269(odhA) RSp1364(sucA)
            REU: Reut_A2047 Reut_B4481
            REH: H16_A2325(odhA)
            RME: Rmet_2050
            BMA: BMA1052(sucA)
            BMV: BMASAVP1_A1498(sucA)
            BML: BMA10299_A0166(sucA)
            BMN: BMA10247_1000(sucA)
            BXE: Bxe_A2812
            BVI: Bcep1808_1474
            BUR: Bcep18194_A4649
            BCN: Bcen_1028
            BCH: Bcen2424_1508
            BAM: Bamb_1390
            BPS: BPSL1909(sucA)
            BPM: BURPS1710b_1924(sucA)
            BPL: BURPS1106A_1772(sucA) BURPS1106A_A3107
            BPD: BURPS668_1750(sucA) BURPS668_A3222
            BTE: BTH_I2556(sucA)
            PNU: Pnuc_0840
            BPE: BP1124(odhA)
            BPA: BPP3217(odhA)
            BBR: BB3669(odhA)
            RFR: Rfer_2321
            POL: Bpro_2624
            PNA: Pnap_1856
            AAV: Aave_3248
            AJS: Ajs_1822
            VEI: Veis_3979
            MPT: Mpe_A2013
            HAR: HEAR1772(sucA)
            MMS: mma_1512(sucA)
            NEU: NE2374(odhA)
            NET: Neut_0860
            NMU: Nmul_A0857
            EBA: ebA6685(sucA)
            AZO: azo1555(odhA)
            DAR: Daro_2859
            TBD: Tbd_1188
            GSU: GSU2449(sucA)
            GME: Gmet_2769
            GUR: Gura_1260
            PCA: Pcar_2940
            BBA: Bd2728(sucA)
            ADE: Adeh_0781
            MXA: MXAN_6035(sucA)
            SFU: Sfum_3547
            RPR: RP180
            RTY: RT0171(sucA)
            RCO: RC0227(sucA)
            RFE: RF_1092(sucA)
            RBE: RBE_1099(sucA)
            RAK: A1C_01300(kgd)
            RBO: A1I_01830(kgd)
            RCM: A1E_00930(kgd)
            RRI: A1G_01295(kgd)
            OTS: OTBS_1490(sucA)
            WOL: WD1309(sucA)
            WBM: Wbm0395
            AMA: AM405(sucA)
            APH: APH_0863(sucA)
            ERU: Erum2650(sucA)
            ERW: ERWE_CDS_02690(sucA)
            ERG: ERGA_CDS_02650(sucA)
            ECN: Ecaj_0255
            ECH: ECH_0832(sucA)
            NSE: NSE_0578(sucA)
            PUB: SAR11_0237(sucA)
            MLO: mll4301
            MES: Meso_3398
            SME: SMc02482(sucA)
            SMD: Smed_2941
            ATU: Atu2636(sucA)
            ATC: AGR_C_4776
            RET: RHE_CH03888(sucA)
            RLE: RL4435(odhA)
            BME: BMEI0140
            BMF: BAB1_1923(sucA)
            BMS: BR1923(sucA)
            BMB: BruAb1_1899(sucA)
            BOV: BOV_1852(sucA)
            OAN: Oant_0933
            BJA: bll0452(sucA)
            BRA: BRADO0406(sucA)
            BBT: BBta_0395(sucA)
            RPA: RPA0189(sucA)
            RPB: RPB_0278
            RPC: RPC_0191
            RPD: RPD_0544
            RPE: RPE_0297
            NWI: Nwi_0422
            NHA: Nham_0542
            BHE: BH16540(sucA)
            BQU: BQ13420(sucA)
            BBK: BARBAKC583_0025(sucA)
            XAU: Xaut_0156
            CCR: CC_0339
            SIL: SPO0344(sucA)
            SIT: TM1040_3511
            RSP: RSP_0965(sucA)
            RSH: Rsph17029_2625
            RSQ: Rsph17025_0077
            JAN: Jann_0831
            RDE: RD1_0974 RD1_1609(sucA)
            PDE: Pden_0555
            MMR: Mmar10_2817
            HNE: HNE_0312(sucA)
            NAR: Saro_1180
            SAL: Sala_2228
            SWI: Swit_1298
            ELI: ELI_08000
            GOX: GOX0882
            GBE: GbCGDNIH1_2068
            ACR: Acry_1623
            RRU: Rru_A1213
            MAG: amb3961
            MGM: Mmc1_2395
            ABA: Acid345_3507
            BSU: BG10272(odhA)
            BHA: BH2206
            BAN: BA1270(odhA)
            BAR: GBAA1270(odhA)
            BAA: BA_1802
            BAT: BAS1177
            BCE: BC1252
            BCA: BCE_1380(odhA)
            BCZ: BCZK1152(odhA)
            BCY: Bcer98_0961
            BTK: BT9727_1158(odhA)
            BLI: BL01452(odhA)
            BLD: BLi02260(odhA)
            BCL: ABC2114(odhA)
            BAY: RBAM_019130
            BPU: BPUM_1862
            OIH: OB1089
            GKA: GK1023
            SAU: SA1245(odhA)
            SAV: SAV1413(odhA)
            SAM: MW1303(odhA)
            SAR: SAR1425(odhA)
            SAS: SAS1356
            SAC: SACOL1449(sucA)
            SAB: SAB0910 SAB1269c(odhA)
            SAA: SAUSA300_1306(sucA)
            SAO: SAOUHSC_01418
            SAJ: SaurJH9_1474
            SAH: SaurJH1_1503
            SEP: SE1097
            SER: SERP0986(sucA)
            SHA: SH1492(odhA)
            SSP: SSP1325
            MTU: Rv1248c(kgd)
            MTC: MT1286(sucA)
            MBO: Mb1280c(kgd)
            MLE: ML1095(odhA)
            MPA: MAP2536(sucA)
            MSM: MSMEG_5049(sucA)
            MMC: Mmcs_3973
            CGL: NCgl1084(kgd)
            CGB: cg1280(kgd)
            CEF: CE1190(kgd)
            CDI: DIP1002(kgd)
            CJK: jk1373(sucA)
            NFA: nfa46950(sucA)
            RHA: RHA1_ro06012(odhA)
            SCO: SCO5281(SCCB12.05c)
            SMA: SAV2972(sucA)
            LXX: Lxx19140(sucA)
            CMI: CMM_1322(sucA)
            AAU: AAur_2635(sucA)
            PAC: PPA1261
            TFU: Tfu_0566
            FRA: Francci3_3748
            FAL: FRAAL5981(sucA)
            ACE: Acel_0586
            SEN: SACE_6385(sucA)
            RXY: Rxyl_2535
            RBA: RB9078(kdgA)
            CTR: CT054(sucA)
            CTA: CTA_0058(sucA)
            CMU: TC0324
            CPN: CPn0378(sucA)
            CPA: CP0378
            CPJ: CPj0378(sucA)
            CPT: CpB0390
            CCA: CCA00420(sucA)
            CAB: CAB406(sucA)
            CFE: CF0587(sucA)
            PCU: pc1090(sucA)
            LIL: LA1224(sucA)
            LIC: LIC12474(odhA)
            LBJ: LBJ_2123(sucA)
            LBL: LBL_2120(sucA)
            SRU: SRU_1173(sucA)
            CHU: CHU_3362(sucA)
            GFO: GFO_3083(sucA)
            FJO: Fjoh_1256
            FPS: FP2408(sucA)
            RRS: RoseRS_3396
            RCA: Rcas_1532
            DRA: DR_0287
            DGE: Dgeo_0140
            TTH: TTC1698
            TTJ: TTHA0289
STRUCTURES  PDB: 2JGD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.4.2
            ExPASy - ENZYME nomenclature database: 1.2.4.2
            ExplorEnz - The Enzyme Database: 1.2.4.2
            ERGO genome analysis and discovery system: 1.2.4.2
            BRENDA, the Enzyme Database: 1.2.4.2
            CAS: 9031-02-1
///
ENTRY       EC 1.2.4.3        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With a disulfide as acceptor
COMMENT     Deleted entry: 2-oxoisocaproate dehydrogenase. Now included with EC
            1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase
            (2-methylpropanoyl-transferring) (EC 1.2.4.3 created 1972, deleted
            1978)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.4.3
            ExPASy - ENZYME nomenclature database: 1.2.4.3
            ExplorEnz - The Enzyme Database: 1.2.4.3
            ERGO genome analysis and discovery system: 1.2.4.3
            BRENDA, the Enzyme Database: 1.2.4.3
///
ENTRY       EC 1.2.4.4                  Enzyme
NAME        3-methyl-2-oxobutanoate dehydrogenase
            (2-methylpropanoyl-transferring);
            2-oxoisocaproate dehydrogenase;
            2-oxoisovalerate (lipoate) dehydrogenase;
            3-methyl-2-oxobutanoate dehydrogenase (lipoamide);
            3-methyl-2-oxobutanoate:lipoamide oxidoreductase (decarboxylating
            and acceptor-2-methylpropanoylating);
            alpha-keto-alpha-methylvalerate dehydrogenase;
            alpha-ketoisocaproate dehydrogenase;
            alpha-ketoisocaproic dehydrogenase;
            alpha-ketoisocaproic-alpha-keto-alpha-methylvaleric dehydrogenase;
            alpha-ketoisovalerate dehydrogenase;
            alpha-oxoisocaproate dehydrogenase;
            BCKDH;
            BCOAD;
            branched chain keto acid dehydrogenase;
            branched-chain (-2-oxoacid) dehydrogenase (BCD);
            branched-chain 2-keto acid dehydrogenase;
            branched-chain 2-oxo acid dehydrogenase;
            branched-chain alpha-keto acid dehydrogenase;
            branched-chain alpha-oxo acid dehydrogenase;
            branched-chain keto acid dehydrogenase;
            branched-chain ketoacid dehydrogenase;
            dehydrogenase, 2-oxoisovalerate (lipoate);
            dehydrogenase, branched chain alpha-keto acid
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With a disulfide as acceptor
SYSNAME     3-methyl-2-oxobutanoate:[dihydrolipoyllysine-residue
            (2-methylpropanoyl)transferase]-lipoyllysine 2-oxidoreductase
            (decarboxylating, acceptor-2-methylpropanoylating)
REACTION    3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue
            (2-methylpropanoyl)transferase] lipoyllysine =
            [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]
            S-(2-methylpropanoyl)dihydrolipoyllysine + CO2 [RN:R01701]
ALL_REAC    R01701;
            (other) R01702 R04225 R07599 R07600 R07601 R07602 R07603 R07604
SUBSTRATE   3-methyl-2-oxobutanoate [CPD:C00141];
            [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]
            lipoyllysine
PRODUCT     [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]
            S-(2-methylpropanoyl)dihydrolipoyllysine [CPD:C15977];
            CO2 [CPD:C00011]
COFACTOR    Thiamin diphosphate [CPD:C00068]
COMMENT     Contains thiamine diphosphate. It acts not only on
            3-methyl-2-oxobutanaoate, but also on 4-methyl-2-oxopentanoate and
            (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids
            that derive from the action of transaminases on valine, leucine and
            isoleucine. It is a component of the multienzyme
            3-methyl-2-oxobutanoate dehydrogenase complex in which multiple
            copies of it are bound to a core of molecules of EC 2.3.1.168,
            dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, which
            also binds multiple copies of EC 1.8.1.4, dihydrolipoyl
            dehydrogenase. It does not act on free lipoamide or lipoyllysine,
            but only on the lipoyllysine residue in EC 2.3.1.168.
REFERENCE   1  [PMID:5656388]
  AUTHORS   Bowden JA, Connelly JL.
  TITLE     Branched chain alpha-keto acid metabolism. II. Evidence for the
            common identity of alpha-ketoisocaproic acid and
            alpha-keto-beta-methyl-valeric acid dehydrogenases.
  JOURNAL   J. Biol. Chem. 243 (1968) 3526-31.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:5689906]
  AUTHORS   Connelly JL, Danner DJ, Bowden JA.
  TITLE     Branched chain alpha-keto acid metabolism. I. Isolation,
            purification, and partial characterization of bovine liver
            alpha-ketoisocaproic:alpha-keto-beta-methylvaleric acid
            dehydrogenase.
  JOURNAL   J. Biol. Chem. 243 (1968) 1198-203.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:447664]
  AUTHORS   Danner DJ, Lemmon SK, Besharse JC, Elsas LJ 2nd.
  TITLE     Purification and characterization of branched chain alpha-ketoacid
            dehydrogenase from bovine liver mitochondria.
  JOURNAL   J. Biol. Chem. 254 (1979) 5522-6.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:283398]
  AUTHORS   Pettit FH, Yeaman SJ, Reed LJ.
  TITLE     Purification and characterization of branched chain alpha-keto acid
            dehydrogenase complex of bovine kidney.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 75 (1978) 4881-5.
  ORGANISM  cow [GN:bta]
REFERENCE   5  [PMID:10966480]
  AUTHORS   Perham RN.
  TITLE     Swinging arms and swinging domains in multifunctional enzymes:
            catalytic machines for multistep reactions.
  JOURNAL   Annu. Rev. Biochem. 69 (2000) 961-1004.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
ORTHOLOGY   KO: K00165  2-oxoisovalerate dehydrogenase
            KO: K00166  2-oxoisovalerate dehydrogenase alpha subunit
            KO: K00167  2-oxoisovalerate dehydrogenase beta subunit
GENES       HSA: 593(BCKDHA) 594(BCKDHB)
            PTR: 462845(BCKDHB) 468889(BCKDHA)
            MMU: 12039(Bckdha) 12040(Bckdhb)
            RNO: 25244(Bckdha) 29711(Bckdhb)
            CFA: 474978(BCKDHB) 484488(BCKDHA)
            BTA: 282149(BCKDHA) 282150(BCKDHB)
            GGA: 395375(BCKDHB)
            SPU: 583728(LOC583728)
            DME: Dmel_CG8199
            CEL: F27D4.5(tag-173) Y39E4A.3(Transketolase)
            OSA: 4342508
            CME: CMH008C CML168C
            ANI: AN1726.2
            AFM: AFUA_6G08830
            AOR: AO090001000555 AO090023000349
            CNE: CNA03850 CNE02620
            DDI: DDB_0230190(bkdA)
            PFA: PFE0225w
            TAN: TA06600 TA10340
            TPV: TP01_0956 TP04_0719
            TET: TTHERM_00325580 TTHERM_00704010
            TBR: Tb10.70.7550
            TCR: 506853.50 508781.110
            LMA: LmjF21.1430
            PLU: plu1883
            PAE: PA2247(bkdA1) PA2248(bkdA2)
            PAU: PA14_35520(bkdA2) PA14_35530(bkdA1)
            PPU: PP_4401(bkdA1) PP_4402(bkdA2)
            PPF: Pput_1453
            PFL: PFL_2533 PFL_2534
            PFO: Pfl_3463 Pfl_3464
            PEN: PSEEN3853(bkdA1) PSEEN3854(bkdA2)
            SON: SO_2339 SO_2340
            SDN: Sden_1786 Sden_1787
            SFR: Sfri_1935
            SAZ: Sama_1709
            SBL: Sbal_2222
            SBM: Shew185_2149
            SLO: Shew_1925
            SPC: Sputcn32_1885
            SSE: Ssed_2329
            SPL: Spea_2246
            SHE: Shewmr4_2028
            SHM: Shewmr7_1947
            SHN: Shewana3_2130 Shewana3_2131
            SHW: Sputw3181_2123
            ILO: IL0177(acoA) IL1679 IL1680
            CPS: CPS_1582 CPS_1583
            PHA: PSHAa1631(bkdA2) PSHAa1632(BckdhA)
            PAT: Patl_2036 Patl_2037
            MAQ: Maqu_1382
            LPN: lpg2581
            LPF: lpl2503
            LPP: lpp2633
            HCH: HCH_03686
            REH: H16_B2233(bkdA1)
            BMA: BMAA2012 BMAA2013
            BMV: BMASAVP1_1036
            BML: BMA10299_1322
            BMN: BMA10247_A2302
            BUR: Bcep18194_A4360 Bcep18194_A4361
            BCN: Bcen_0762
            BCH: Bcen2424_1243 Bcen2424_1244
            BAM: Bamb_1123 Bamb_1124
            BPS: BPSS2272(bkdA2) BPSS2273(bkdA1)
            BPM: BURPS1710b_A1410(bkdA2) BURPS1710b_A1411(bkdA1)
            BPL: BURPS1106A_A3066 BURPS1106A_A3067
            BPD: BURPS668_A3192 BURPS668_A3193
            BTE: BTH_II2303 BTH_II2304
            RFR: Rfer_3553 Rfer_3554
            POL: Bpro_0273 Bpro_0274
            BBA: Bd0972 Bd0974
            ADE: Adeh_1826 Adeh_1827
            AFW: Anae109_1993
            MXA: MXAN_4564 MXAN_4565
            MLO: mll4472 mll4473
            SME: SMb20020(pdh) SMc03201(bkdAa) SMc03202(bkdAb)
            SMD: Smed_2826
            ATU: Atu3472(bkdA2) Atu3473(bkdA1)
            ATC: AGR_L_2716 AGR_L_2718
            RET: RHE_PC00070(bkdA1) RHE_PC00071(bkdA2)
            RLE: pRL100303 pRL100304
            BME: BMEII0061 BMEII0216 BMEII0747 BMEII0748
            BMF: BAB2_0031 BAB2_0714 BAB2_0715 BAB2_1044
            BMS: BRA0032 BRA0524 BRA0525
            BMB: BruAb2_0032 BruAb2_0699 BruAb2_0700 BruAb2_1025
            BOV: BOV_A0455 BOV_A0456 BOV_A0457
            OAN: Oant_3551
            BJA: blr6331(bkdA1) blr6332(bkdA2)
            SIL: SPO0585
            SIT: TM1040_2777 TM1040_2778
            RSP: RSP_1294
            RDE: RD1_2926(pdhB)
            PDE: Pden_4757
            MMR: Mmar10_0704
            NAR: Saro_1975 Saro_1976
            SAL: Sala_1330 Sala_1331
            SWI: Swit_0782 Swit_2145
            ELI: ELI_05155 ELI_05160
            ABA: Acid345_1786
            BSU: BG10306(bkdA2) BG10307(bkdA1)
            BHA: BH2762(bfmBAB) BH2763(bfmBAA)
            BAN: BA4383(bfmbAb) BA4384(bfmbAa)
            BAR: GBAA4383(bfmbAb) GBAA4384(bfmbAa)
            BAA: BA_4838 BA_4839
            BAT: BAS4066 BAS4067
            BCE: BC4158 BC4159
            BCA: BCE_4233(bfmbAb) BCE_4234(bfmbAa)
            BCZ: BCZK3913(bfmbAb) BCZK3914(bfmbAa)
            BCY: Bcer98_2856
            BTK: BT9727_3904(bfmbAb) BT9727_3905(bfmbAa)
            BTL: BALH_3772(bfmbAa)
            BLI: BL01504(bkdAA) BL01505(bkdAB)
            BLD: BLi02581(bkdAB) BLi02582(bkdAA)
            BCL: ABC2450(bkdA2) ABC2451(bkdA1)
            BAY: RBAM_022320(bkdAB) RBAM_022330(bkdAA)
            BPU: BPUM_2143(bfmBAB) BPUM_2144(bfmBAA)
            OIH: OB1865 OB1866
            GKA: GK2377 GK2378
            SAU: SA1347(bfmBAB) SA1348(bfmBAA)
            SAV: SAV1516(bfmBAB) SAV1517(bfmBAA)
            SAM: MW1469(bfmBAB) MW1470(bfmBAA)
            SAR: SAR1594(bfmBAB) SAR1595(bfmBAA)
            SAS: SAS1455 SAS1456
            SAB: SAB1389c SAB1390c
            SAO: SAOUHSC_01613
            SAJ: SaurJH9_1576
            SAH: SaurJH1_1609
            SEP: SE1197 SE1198
            SHA: SH1398(bfmBAA) SH1399(bfmBAB)
            SSP: SSP1238 SSP1239
            LMO: lmo1372 lmo1373
            LMF: LMOf2365_1389
            LIN: lin1409 lin1410(BfmBAB)
            LWE: lwe1387 lwe1388
            SPD: SPD_1027
            LCA: LSEI_1444 LSEI_1445
            EFA: EF1659(bkdB) EF1660(bkdA)
            STH: STH2161 STH2162 STH583
            TWS: TW799(pdhA)
            RXY: Rxyl_2479 Rxyl_2480
            CTR: CT340(pdhA)
            CTA: CTA_0369(pdhA_2)
            CMU: TC0618
            CPN: CPn0033(pdhA)
            CPA: CP0743
            CPJ: CPj0033(pdhA_pdhB)
            CPT: CpB0037
            CCA: CCA00324(pdhA)
            CAB: CAB319
            CFE: CF0679(pdhAB)
            GVI: gll1094
            BTH: BT_0312
            BFR: BF1622
            BFS: BF1636
            SRU: SRU_0576
            CHU: CHU_3183(dxs)
            GFO: GFO_1616
            FPS: FP1028(bfmBA)
            DRA: DR_0029 DR_0030
            DGE: Dgeo_2339
            TTH: TTC1756 TTC1757
            TTJ: TTHA0229 TTHA0230
            HMA: rrnAC0149(pdhA1) rrnAC2957(pdhA3)
STRUCTURES  PDB: 1DTW  1OLS  1OLU  1OLX  1U5B  1UM9  1UMB  1UMC  1UMD  1V11  
                 1V16  1V1M  1V1R  1WCI  1X7W  1X7X  1X7Y  1X7Z  1X80  2BEU  
                 2BEV  2BEW  2BFB  2BFC  2BFD  2BFE  2BFF  2BP7  2J9F  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.4.4
            ExPASy - ENZYME nomenclature database: 1.2.4.4
            ExplorEnz - The Enzyme Database: 1.2.4.4
            ERGO genome analysis and discovery system: 1.2.4.4
            BRENDA, the Enzyme Database: 1.2.4.4
            CAS: 9082-72-8
///
ENTRY       EC 1.2.7.1                  Enzyme
NAME        pyruvate synthase;
            pyruvate oxidoreductase;
            pyruvate synthetase;
            pyruvate:ferredoxin oxidoreductase;
            pyruvic-ferredoxin oxidoreductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With an iron-sulfur protein as acceptor
SYSNAME     pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating)
REACTION    pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO2 + 2
            reduced ferredoxin + 2 H+ [RN:R01196]
ALL_REAC    R01196;
            (other) R01199
SUBSTRATE   pyruvate [CPD:C00022];
            CoA [CPD:C00010];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     acetyl-CoA [CPD:C00024];
            CO2 [CPD:C00011];
            reduced ferredoxin [CPD:C00138];
            H+ [CPD:C00080]
COMMENT     Contains thiamine diphosphate and [4Fe-4S] clusters. This enzyme is
            one of four2-oxoacid oxidoreductases that are differentiated by
            their abilities to oxidatively decarboxylatedifferent 2-oxoacids and
            form their CoA derivatives [see also EC 1.2.7.3, 2-oxoglutarate
            synthase, EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase
            (ferredoxin) and EC 1.2.7.8, indolepyruvate ferredoxin
            oxidoreductase]
REFERENCE   1  [PMID:5217644]
  AUTHORS   Evans MC, Buchanan BB.
  TITLE     Photoreduction of ferredoxin and its use in carbon dioxide fixation
            by a subcellular system from a photosynthetic bacterium.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 53 (1965) 1420-5.
  ORGANISM  Chromatium sp., Chlorobium thiosulfatophilum
REFERENCE   2  [PMID:4628267]
  AUTHORS   Gehring U, Arnon DI.
  TITLE     Purification and properties of  -ketoglutarate synthase from a
            photosynthetic bacterium.
  JOURNAL   J. Biol. Chem. 247 (1972) 6963-9.
  ORGANISM  Chromatium sp., Chlorobium thiosulfatophilum
REFERENCE   3  [PMID:5574389]
  AUTHORS   Uyeda K, Rabinowitz JC.
  TITLE     Pyruvate-ferredoxin oxidoreductase. 3. Purification and properties
            of the enzyme.
  JOURNAL   J. Biol. Chem. 246 (1971) 3111-9.
  ORGANISM  Clostridium acidi-urici
REFERENCE   4  [PMID:4324891]
  AUTHORS   Uyeda K, Rabinowitz JC.
  TITLE     Pyruvate-ferredoxin oxidoreductase. IV. Studies on the reaction
            mechanism.
  JOURNAL   J. Biol. Chem. 246 (1971) 3120-5.
  ORGANISM  Clostridium acidi-urici
REFERENCE   5  [PMID:10607667]
  AUTHORS   Charon MH, Volbeda A, Chabriere E, Pieulle L, Fontecilla-Camps JC.
  TITLE     Structure and electron transfer mechanism of pyruvate:ferredoxin
            oxidoreductase.
  JOURNAL   Curr. Opin. Struct. Biol. 9 (1999) 663-9.
  ORGANISM  Clostridium thermoaceticum
PATHWAY     PATH: map00620  Pyruvate metabolism
            PATH: map00640  Propanoate metabolism
            PATH: map00650  Butanoate metabolism
            PATH: map00720  Reductive carboxylate cycle (CO2 fixation)
ORTHOLOGY   KO: K00168  pyruvate ferredoxin oxidoreductase
            KO: K00169  pyruvate ferredoxin oxidoreductase, alpha subunit
            KO: K00170  pyruvate ferredoxin oxidoreductase, beta subunit
            KO: K00171  pyruvate ferredoxin oxidoreductase, delta subunit
            KO: K00172  pyruvate ferredoxin oxidoreductase, gamma subunit
GENES       ECI: UTI89_C1055(yccM)
            YPI: YpsIP31758_1803
            RFR: Rfer_2185 Rfer_2186 Rfer_2187
            EBA: ebA5397(padE) ebA5399(padG) ebA5401(padI) ebB191(padF)
            HPY: HP1108 HP1109 HP1110 HP1111
            HPJ: jhp1035(porG) jhp1036(porD) jhp1037(porA) jhp1038(porB)
            HPA: HPAG1_1047 HPAG1_1048 HPAG1_1049 HPAG1_1050
            HHE: HH0546(porB) HH0547(porA) HH0548(porD) HH0549(porG)
            HAC: Hac_0430(porB) Hac_0431(porA) Hac_0432(porD) Hac_0433(porG)
            WSU: WS2128 WS2130 WS2131 WS2132
            TDN: Tmden_0096 Tmden_0097 Tmden_0098 Tmden_0099
            CFF: CFF8240_0392(nifJ)
            CCV: CCV52592_0916(nifJ)
            CHA: CHAB381_1601(nifJ)
            CCO: CCC13826_1933(nifJ)
            NIS: NIS_1602 NIS_1603 NIS_1604 NIS_1605
            SUN: SUN_0198(porC) SUN_0199(porD) SUN_0200(porA) SUN_0201(porB)
            PCA: Pcar_1239(porA) Pcar_1240(porB)
            DVU: DVU1569(porA) DVU1570(porB)
            DPS: DP1200(porA) DP1201(porB)
            SAT: SYN_00154 SYN_00155 SYN_00156 SYN_00157 SYN_00691 SYN_00692
                 SYN_00693 SYN_00694
            SFU: Sfum_0114 Sfum_0543 Sfum_0544 Sfum_2792 Sfum_2793 Sfum_2794
                 Sfum_2795
            RPD: RPD_1510 RPD_1511 RPD_1512 RPD_1514
            MAG: amb1676 amb1677 amb1678 amb1680
            SAB: SAB1151 SAB1152
            CTC: CTC02525(porB) CTC02526(porA) CTC02527(porD) CTC02528(porC)
            CNO: NT01CX_0144(porB) NT01CX_0145 NT01CX_0146(porD)
                 NT01CX_0147(porG) NT01CX_1854(nifJ)
            CTH: Cthe_2390
            CDF: CD0116 CD0118
            CBO: CBO3421 CBO3423
            CBA: CLB_1223 CLB_2701
            CBH: CLC_1235 CLC_2634
            CBF: CLI_1276 CLI_2810
            CKL: CKL_2138 CKL_2996(porB) CKL_2997(porA) CKL_2998(porD)
                 CKL_2999(porC) CKL_3337
            SWO: Swol_1374 Swol_1375 Swol_1376 Swol_1377 Swol_2234 Swol_2235
                 Swol_2236 Swol_2237
            MTA: Moth_0378 Moth_0379 Moth_1591 Moth_1592
            ACE: Acel_0700 Acel_0701 Acel_0702
            DET: DET0724(porG) DET0725(porD) DET0726(porA) DET0727(porB)
            DEH: cbdb_A680(porD) cbdb_A681(porA) cbdb_A682(porB)
                 cbdb_B16(porG)
            DEB: DehaBAV1_0656
            AAE: aq_1167(forA2) aq_1168(forB2) aq_1169(forG2) aq_1195(forA1)
                 aq_1196(forB1) aq_1200(forG1)
            TMA: TM0015 TM0016 TM0017 TM0018
            MJA: MJ0266(porB) MJ0267(porA) MJ0268(porD) MJ0269(porG)
            MMP: MMP1504(porB) MMP1505(porA) MMP1506(porD) MMP1507(porC)
            MMQ: MmarC5_0070
            MMZ: MmarC7_0751
            MVN: Mevan_0816
            MAC: MA0031(porB) MA0032(porA) MA0033(porD) MA0034(porG)
                 MA2407(porB)
            MBA: Mbar_A0999 Mbar_A1000 Mbar_A1001 Mbar_A1002 Mbar_A3180
            MMA: MM_1339 MM_1340 MM_1341 MM_1342
            MBU: Mbur_2155 Mbur_2156 Mbur_2157 Mbur_2158
            MTP: Mthe_1648
            MHU: Mhun_0450 Mhun_0451 Mhun_0452 Mhun_0453
            MEM: Memar_0707
            MBN: Mboo_0675
            MTH: MTH1738 MTH1739 MTH1740
            MST: Msp_0334(porC) Msp_0335(porD) Msp_0336(porA) Msp_0337(porB)
            MSI: Msm_0557 Msm_0558 Msm_0559 Msm_0560
            MKA: MK0080(porG_1) MK0081(porD) MK0082(porA_1) MK0083(porB_1)
            AFU: AF1699(porG) AF1700(porD) AF1701(porA) AF1702(porB)
            HMA: rrnAC0718(porA) rrnAC0719(porB) rrnAC1267(korA)
                 rrnAC1268(korB)
            HWA: HQ3355A(porB) HQ3356A(porA)
            NPH: NP4044A(porB) NP4046A(porA)
            TAC: Ta0626m Ta0627 Ta0628m Ta0629
            TVO: TVN0833 TVN0834 TVN0835 TVN0836
            PTO: PTO1360 PTO1361
            PHO: PH0678 PH0679 PH0682 PH0684 PH0685
            PAB: PAB1470 PAB1474 PAB1475(POR) PAB1476(POR)
            PFU: PF0965 PF0966 PF0967 PF0970 PF0971
            TKO: TK1978 TK1979 TK1980 TK1982 TK1983 TK1984
            RCI: RCIX486(porC-1) RCIX488(porD-1) RCIX489(porA-1)
                 RCIX490(porB-1) RRC106(porB-2) RRC107(porA-2) RRC109(porC-2)
                 RRC110(porD-2)
            HBU: Hbut_0668 Hbut_0669 Hbut_0670 Hbut_0729
            SSO: SSO11071(porD-2) SSO1206(porB-1) SSO1207(porA-1)
                 SSO1208(porG-1) SSO2128(porD-like) SSO2129(porA-like)
                 SSO2130(porB-like) SSO2756(porB-2) SSO2757(porA-2)
                 SSO2758(porG-2) SSO7412(porD-1)
            STO: ST1531 ST1532 ST1533 ST1787 ST1788
            SAI: Saci_1088 Saci_2250(porC) Saci_2251(porD) Saci_2252(porA)
                 Saci_2253(porB)
            PAI: PAE1040(porG) PAE1041(porD) PAE1042(porA) PAE1043(porB)
                 PAE3274 PAE3275 PAE3276 PAE3279
            PAS: Pars_0193
STRUCTURES  PDB: 1B0P  1KEK  2C3M  2C3O  2C3P  2C3U  2C3Y  2C42  2PDA  2RAA  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.7.1
            ExPASy - ENZYME nomenclature database: 1.2.7.1
            ExplorEnz - The Enzyme Database: 1.2.7.1
            ERGO genome analysis and discovery system: 1.2.7.1
            BRENDA, the Enzyme Database: 1.2.7.1
            CAS: 9082-51-3
///
ENTRY       EC 1.2.7.2                  Enzyme
NAME        2-oxobutyrate synthase;
            alpha-ketobutyrate-ferredoxin oxidoreductase;
            2-ketobutyrate synthase;
            alpha-ketobutyrate synthase;
            2-oxobutyrate-ferredoxin oxidoreductase;
            2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propionylating)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With an iron-sulfur protein as acceptor
SYSNAME     2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propanoylating)
REACTION    2-oxobutanoate + CoA + oxidized ferredoxin = propanoyl-CoA + CO2 +
            reduced ferredoxin [RN:R01199]
ALL_REAC    R01199
SUBSTRATE   2-oxobutanoate [CPD:C00109];
            CoA [CPD:C00010];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     propanoyl-CoA [CPD:C00100];
            CO2 [CPD:C00011];
            reduced ferredoxin [CPD:C00138]
REFERENCE   1  [PMID:5800441]
  AUTHORS   Buchanan BB.
  TITLE     Role of ferredoxin in the synthesis of alpha-ketobutyrate from
            propionyl coenzyme A and carbon dioxide by enzymes from
            photosynthetic and nonphotosynthetic bacteria.
  JOURNAL   J. Biol. Chem. 244 (1969) 4218-23.
  ORGANISM  Chromatium sp., Clostridium pasteurianum, Desulfovibrio
            desulfuricans [GN:dde]
PATHWAY     PATH: map00640  Propanoate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.7.2
            ExPASy - ENZYME nomenclature database: 1.2.7.2
            ExplorEnz - The Enzyme Database: 1.2.7.2
            ERGO genome analysis and discovery system: 1.2.7.2
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.7.2
            BRENDA, the Enzyme Database: 1.2.7.2
            CAS: 37251-04-0
///
ENTRY       EC 1.2.7.3                  Enzyme
NAME        2-oxoglutarate synthase;
            2-ketoglutarate ferredoxin oxidoreductase;
            2-oxoglutarate:ferredoxin oxidoreductase;
            KGOR;
            2-oxoglutarate ferredoxin oxidoreductase;
            2-oxoglutarate:ferredoxin 2-oxidoreductase (CoA-succinylating)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With an iron-sulfur protein as acceptor
SYSNAME     2-oxoglutarate:ferredoxin oxidoreductase (decarboxylating)
REACTION    2-oxoglutarate + CoA + 2 oxidized ferredoxin = succinyl-CoA + CO2 +
            2 reduced ferredoxin [RN:R01197]
ALL_REAC    R01197
SUBSTRATE   2-oxoglutarate [CPD:C00026];
            CoA [CPD:C00010];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     succinyl-CoA [CPD:C00091];
            CO2 [CPD:C00011];
            reduced ferredoxin [CPD:C00138]
COMMENT     This enzyme is one of four 2-oxoacid oxidoreductases that are
            differentiated by their abilities to oxidatively decarboxylate
            different 2-oxoacids and form their CoA derivatives (see also EC
            1.2.7.1, pyruvate synthase, EC 1.2.7.7, 3-methyl-2-oxobutanoate
            dehydrogenase (ferredoxin) and EC 1.2.7.8, indolepyruvate ferredoxin
            oxidoreductase) [3]. Contains thiamine diphosphate and 2 [4Fe-4S]
            clusters. Highly specific for 2-oxoglutarate.
REFERENCE   1  [PMID:4286833]
  AUTHORS   Buchanan BB, Evans MC.
  TITLE     The synthesis of alpha-ketoglutarate from succinate and carbon
            dioxide by a subcellular preparation of a photosynthetic bacterium.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 54 (1965) 1212-8.
  ORGANISM  Chlorobium thiosulfatophilum
REFERENCE   2  [PMID:4628267]
  AUTHORS   Gehring U, Arnon DI.
  TITLE     Purification and properties of  -ketoglutarate synthase from a
            photosynthetic bacterium.
  JOURNAL   J. Biol. Chem. 247 (1972) 6963-9.
  ORGANISM  Chlorobium thiosulfatophilum
REFERENCE   3  [PMID:12081970]
  AUTHORS   Dorner E, Boll M.
  TITLE     Properties of 2-oxoglutarate:ferredoxin oxidoreductase from Thauera
            aromatica and its role in enzymatic reduction of the aromatic ring.
  JOURNAL   J. Bacteriol. 184 (2002) 3975-83.
  ORGANISM  Thauera aromatica
REFERENCE   4  [PMID:8830683]
  AUTHORS   Mai X, Adams MW.
  TITLE     Characterization of a fourth type of 2-keto acid-oxidizing enzyme
            from a hyperthermophilic archaeon: 2-ketoglutarate ferredoxin
            oxidoreductase from Thermococcus litoralis.
  JOURNAL   J. Bacteriol. 178 (1996) 5890-6.
  ORGANISM  Thermococcus litoralis
REFERENCE   5  [PMID:11265457]
  AUTHORS   Schut GJ, Menon AL, Adams MW.
  TITLE     2-keto acid oxidoreductases from Pyrococcus furiosus and
            Thermococcus litoralis.
  JOURNAL   Methods. Enzymol. 331 (2001) 144-58.
  ORGANISM  Thermococcus litoralis, Pyrococcus furiosus [GN:pfu]
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00720  Reductive carboxylate cycle (CO2 fixation)
ORTHOLOGY   KO: K00173  2-oxoglutarate ferredoxin oxidoreductase
            KO: K00174  2-oxoglutarate ferredoxin oxidoreductase, alpha subunit
            KO: K00175  2-oxoglutarate ferredoxin oxidoreductase, beta subunit
            KO: K00176  2-oxoglutarate ferredoxin oxidoreductase, delta subunit
            KO: K00177  2-oxoglutarate ferredoxin oxidoreductase, gamma subunit
GENES       LPN: lpg0947 lpg0948(korB)
            LPF: lpl0976 lpl0977
            LPP: lpp1009 lpp1010
            TCX: Tcr_1709 Tcr_1710
            RFR: Rfer_2798 Rfer_2799
            EBA: ebA3149(korA2) ebA3150(korB2) ebA4588(korA) ebA4589(korB)
                 p2A13(korA1) p2A16(korB1)
            HPY: HP0588 HP0589 HP0590 HP0591
            HPJ: jhp0536(oorD) jhp0537(oorA) jhp0538(oorB) jhp0539(oorC)
            HPA: HPAG1_0568 HPAG1_0569 HPAG1_0570 HPAG1_0571
            HHE: HH1567(oorC) HH1568(oorB) HH1569(oorA) HH1570(oorD)
            HAC: Hac_1420(oorC) Hac_1421(oorB) Hac_1422(oorA) Hac_1423(oorD)
            WSU: WS1067 WS1068 WS1069 WS1070
            TDN: Tmden_1052 Tmden_1053 Tmden_1054 Tmden_1055
            CJE: Cj0535(oorD) Cj0536(oorA) Cj0537(oorB) Cj0538(oorC)
            CJR: CJE0639(oorD) CJE0640(oorA) CJE0641(oorB) CJE0642(oorC)
            CJJ: CJJ81176_0560(oorD) CJJ81176_0561(oorA) CJJ81176_0562(oorB)
                 CJJ81176_0563(oorC)
            CJU: C8J_0496(oorD) C8J_0497(oorA) C8J_0498(oorB) C8J_0499(oorC)
            CJD: JJD26997_1392(oorC) JJD26997_1393(oorB) JJD26997_1394(oorA)
                 JJD26997_1395(oorD)
            ABU: Abu_0854(oorD) Abu_0855(oorA) Abu_0856(oorB) Abu_0857(oorC)
            NIS: NIS_0841 NIS_0842 NIS_0843 NIS_0844
            SUN: SUN_0578 SUN_0579 SUN_0580 SUN_0581
            GSU: GSU1468 GSU1469 GSU1470 GSU1860 GSU1861 GSU1862
            GME: Gmet_1306 Gmet_1308 Gmet_1309 Gmet_1362 Gmet_1363 Gmet_1364
            PCA: Pcar_1028 Pcar_1029 Pcar_1030 Pcar_1031 Pcar_1547
            DVU: DVU1944 DVU1945 DVU1946 DVU1947 DVU3347 DVU3348 DVU3349
            DVL: Dvul_1563
            DDE: Dde_0044 Dde_0045 Dde_0046 Dde_1637 Dde_1638 Dde_1639
                 Dde_1792 Dde_1793
            LIP: LI0790(vorB) LI0791(porB) LI0792(porB)
            DPS: DP2102(oforB) DP2103(oforA) DP2319 DP2320 DP2321 DP2322
            ADE: Adeh_1957 Adeh_1958 Adeh_1959 Adeh_1960 Adeh_1961 Adeh_1962
                 Adeh_3012 Adeh_3013
            SAT: SYN_02498 SYN_02499 SYN_03162 SYN_03163
            SFU: Sfum_0015 Sfum_0016 Sfum_0017 Sfum_0018 Sfum_0299 Sfum_0300
                 Sfum_0301 Sfum_0302 Sfum_1165 Sfum_1166 Sfum_1167 Sfum_1168
                 Sfum_3137 Sfum_3138 Sfum_3139
            BJA: blr6743 blr6744
            BRA: BRADO5801 BRADO5802
            BBT: BBta_6308 BBta_6309
            RPA: RPA1226 RPA1227(oorB) RPA1228
            RPB: RPB_1234 RPB_1235 RPB_1236
            RPC: RPC_0695 RPC_0696 RPC_0697
            RPD: RPD_1531 RPD_1532 RPD_4009 RPD_4010 RPD_4011
            RPE: RPE_0601 RPE_0602 RPE_0982 RPE_0983 RPE_0984
            NAR: Saro_1757 Saro_1758
            SAL: Sala_1547 Sala_1548
            ELI: ELI_07065 ELI_07070
            RRU: Rru_A2721 Rru_A2722
            MAG: amb2145 amb2146
            MGM: Mmc1_1749 Mmc1_1750
            ABA: Acid345_0598 Acid345_0599
            BHA: BH2373 BH2374
            BAN: BA3909 BA3910
            BAR: GBAA3909 GBAA3910
            BAA: BA_4379 BA_4380
            BAT: BAS3622 BAS3623
            BCE: BC3773(porB) BC3774
            BCA: BCE_3808 BCE_3809
            BCZ: BCZK3532(porB) BCZK3533(porA)
            BTK: BT9727_3514(porB) BT9727_3515(porA)
            GKA: GK1301 GK1302
            SAU: SA1131 SA1132
            SAV: SAV1289 SAV1290
            SAM: MW1172 MW1173
            SAR: SAR1265 SAR1266
            SAS: SAS1223 SAS1224
            SAC: SACOL1308 SACOL1309
            SAA: SAUSA300_1182 SAUSA300_1183
            SAO: SAOUHSC_01266 SAOUHSC_01267
            SEP: SE0967 SE0968
            SER: SERP0856 SERP0857
            SHA: SH1623 SH1624
            SSP: SSP1475 SSP1476
            STH: STH1316 STH1317 STH221 STH222 STH223 STH224
            CAC: CAC2458 CAC2459
            CBE: Cbei_4041
            AMT: Amet_2632
            CHY: CHY_0043 CHY_0044 CHY_0046 CHY_0575 CHY_1970 CHY_1971
            SWO: Swol_0036 Swol_0037 Swol_1398 Swol_1399
            TTE: TTE0960(porB) TTE0961(porA2) TTE1209(porA3) TTE1211(porG)
                 TTE1340(porA4) TTE1341(porB3) TTE1342(porG2)
            MTA: Moth_0033 Moth_0034 Moth_1984
            MTU: Rv2454c Rv2455c
            MTC: MT2529 MT2530
            MBO: Mb2481c Mb2482c
            MPA: MAP2276c MAP2277c
            MSM: MSMEG_4645(orb) MSMEG_4646
            NFA: nfa36600 nfa36610
            RHA: RHA1_ro02389 RHA1_ro02390
            SCO: SCO4594(SCD20.12c) SCO4595(SCD20.13c) SCO6269(SCAH10.34c)
                 SCO6270(SCAH10.35c)
            SMA: SAV4876(korB) SAV4877(korA)
            PAC: PPA1904 PPA1905
            TFU: Tfu_2674 Tfu_2675
            FRA: Francci3_0554 Francci3_0555 Francci3_4473 Francci3_4474
            FAL: FRAAL1050 FRAAL1051 FRAAL6798 FRAAL6799
            ACE: Acel_0283 Acel_0284
            SEN: SACE_3926 SACE_3927(korA)
            RBA: RB6933(korB) RB6935(korA)
            BTH: BT_0333 BT_2836(korA) BT_2837(korB)
            BFR: BF1648(vorB) BF1649 BF4440(korA) BF4441(korB)
            BFS: BF4239(porA) BF4240(porB)
            PGI: PG0429 PG0430 PG1809 PG1810 PG1812 PG1813
            SRU: SRU_0423 SRU_0424
            CTE: CT0162 CT0163
            CCH: Cag_0365 Cag_0366
            PLT: Plut_1072 Plut_1073 Plut_1954 Plut_1955
            TTH: TTC1591 TTC1592
            TTJ: TTHA1955 TTHA1956
            TMA: TM0405 TM0406 TM0878 TM1164 TM1165
            FNO: Fnod_0056
            MJA: MJ0146 MJ0276(korA) MJ0536(korG) MJ0537(korB)
            MMP: MMP0003(korA) MMP0305 MMP0306 MMP1315(korG) MMP1316(korB)
                 MMP1687(korD)
            MAC: MA3075 MA3076
            MBA: Mbar_A2214 Mbar_A2215
            MMA: MM_0419 MM_0420
            MBU: Mbur_0889 Mbur_0890
            MHU: Mhun_0092 Mhun_0093 Mhun_0094 Mhun_2992 Mhun_2993
            MTH: MTH1032 MTH1033 MTH1034 MTH1035 MTH536 MTH537
            MST: Msp_1387(korC) Msp_1388(korB) Msp_1389(korA) Msp_1390(korD)
            MSI: Msm_0331 Msm_0925 Msm_0926 Msm_0927 Msm_0928
            MKA: MK0727 MK0728(porA_2) MK0729(porB_2) MK0730(porG_2)
            AFU: AF0468(korB) AF0469(korA) AF0470(korD) AF0471(korG)
                 AF0749(orA) AF0750(orB)
            HAL: VNG0473G(porB) VNG0474G(porA) VNG1125G(korB) VNG1128G(korA)
            HMA: rrnAC0718(porA) rrnAC0719(porB) rrnAC1267(korA)
                 rrnAC1268(korB)
            HWA: HQ1535A(korB) HQ1536A(korA)
            NPH: NP1232A(korA) NP1234A(korB)
            TAC: Ta0259m Ta0260 Ta0772m Ta0773
            TVO: TVN0846 TVN0847 TVN1334 TVN1335
            PTO: PTO0999 PTO1000
            PHO: PH1660 PH1661 PH1662 PH1663 PH1665 PH1666
            PAB: PAB0341(korD) PAB0344(korB-1) PAB0345(korG-1) PAB0346(korA-2)
                 PAB0347(korB-2) PAB0348(korG-2) PAB2359(korA-1)
            PFU: PF0753 PF0754 PF1767 PF1768 PF1769 PF1770 PF1771 PF1772
                 PF1773
            TKO: TK0816 TK0817 TK1123 TK1124 TK1125 TK1126 TK1129 TK1130
                 TK1131
            APE: APE_1472 APE_1473.1 APE_2126.1 APE_2128
            SSO: SSO2815 SSO2816
            STO: ST2298 ST2300 ST2433 ST2435
            SAI: Saci_0208(korB) Saci_0209(korA) Saci_2306 Saci_2307(korB)
            PAI: PAE0938 PAE0939 PAE1558 PAE1559 PAE2736 PAE2737
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.7.3
            ExPASy - ENZYME nomenclature database: 1.2.7.3
            ExplorEnz - The Enzyme Database: 1.2.7.3
            ERGO genome analysis and discovery system: 1.2.7.3
            BRENDA, the Enzyme Database: 1.2.7.3
            CAS: 37251-05-1
///
ENTRY       EC 1.2.7.4                  Enzyme
NAME        carbon-monoxide dehydrogenase (ferredoxin)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With an iron-sulfur protein as acceptor
SYSNAME     carbon-monoxide,water:ferredoxin oxidoreductase
REACTION    CO + H2O + oxidized ferredoxin = CO2 + reduced ferredoxin
            [RN:R07157]
ALL_REAC    R07157
SUBSTRATE   CO [CPD:C00237];
            H2O [CPD:C00001];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     CO2 [CPD:C00011];
            reduced ferredoxin [CPD:C00138]
COMMENT     Contains nickel, zinc and non-heme iron. Methyl viologen can act as
            acceptor. The enzyme from Moorella thermoacetica exists as a complex
            with EC 2.3.1.169, CO-methylating acetyl CoA synthase, which
            catalyses the overall reaction:methylcorrinoid protein + CoA + CO2 +
            reduced ferredoxin = acetyl-CoA + corrinoid protein + H2O + oxidized
            ferredoxin.
REFERENCE   1  [PMID:7354006]
  AUTHORS   Meyer O, Schlegel HG.
  TITLE     Carbon monoxide:methylene blue oxidoreductase from Pseudomonas
            carboxydovorans.
  JOURNAL   J. Bacteriol. 141 (1980) 74-80.
  ORGANISM  Pseudomonas carboxydovorans
REFERENCE   2  [PMID:6687389]
  AUTHORS   Ragsdale SW, Clark JE, Ljungdahl LG, Lundie LL, Drake HL.
  TITLE     Properties of purified carbon monoxide dehydrogenase from
            Clostridium thermoaceticum, a nickel, iron-sulfur protein.
  JOURNAL   J. Biol. Chem. 258 (1983) 2364-9.
  ORGANISM  Moorella thermoacetica [GN:mta]
REFERENCE   3  [PMID:12386327]
  AUTHORS   Doukov TI, Iverson TM, Seravalli J, Ragsdale SW, Drennan CL.
  TITLE     A Ni-Fe-Cu center in a bifunctional carbon monoxide
            dehydrogenase/acetyl-CoA synthase.
  JOURNAL   Science. 298 (2002) 567-72.
  ORGANISM  Moorella thermoacetica [GN:mta]
GENES       CDF: CD0716(cooS)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.7.4
            ExPASy - ENZYME nomenclature database: 1.2.7.4
            ExplorEnz - The Enzyme Database: 1.2.7.4
            ERGO genome analysis and discovery system: 1.2.7.4
            BRENDA, the Enzyme Database: 1.2.7.4
///
ENTRY       EC 1.2.7.5                  Enzyme
NAME        aldehyde ferredoxin oxidoreductase;
            AOR
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With an iron-sulfur protein as acceptor
SYSNAME     aldehyde:ferredoxin oxidoreductase
REACTION    an aldehyde + H2O + 2 oxidized ferredoxin = an acid + 2 H+ + 2
            reduced ferredoxin [RN:R07158]
ALL_REAC    R07158
SUBSTRATE   aldehyde [CPD:C00071];
            H2O [CPD:C00001];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     acid [CPD:C00174];
            H+ [CPD:C00080];
            reduced ferredoxin [CPD:C00138]
COMMENT     This is an oxygen-sensitive enzyme that contains
            tungsten-molybdopterin and iron-sulfur clusters. Catalyses the
            oxidation of aldehydes (including crotonaldehyde, acetaldehyde,
            formaldehyde and glyceraldehyde) to their corresponding acids.
            However, it does not oxidize glyceraldehyde 3-phosphate [see EC
            1.2.7.6, glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)]. Can
            use ferredoxin or methyl viologen but not NAD(P)+ as electron
            acceptor.
REFERENCE   1  [PMID:1907273]
  AUTHORS   Mukund S, Adams MW.
  TITLE     The novel tungsten-iron-sulfur protein of the hyperthermophilic
            archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin
            oxidoreductase. Evidence for its participation in a unique
            glycolytic pathway.
  JOURNAL   J. Biol. Chem. 266 (1991) 14208-16.
  ORGANISM  Pyrococcus furiosus [GN:pfu]
REFERENCE   2  [PMID:8444863]
  AUTHORS   Johnson JL, Rajagopalan KV, Mukund S, Adams MW.
  TITLE     Identification of molybdopterin as the organic component of the
            tungsten cofactor in four enzymes from hyperthermophilic Archaea.
  JOURNAL   J. Biol. Chem. 268 (1993) 4848-52.
  ORGANISM  Pyrococcus furiosus [GN:pfu]
REFERENCE   3  [PMID:7878465]
  AUTHORS   Chan MK, Mukund S, Kletzin A, Adams MW, Rees DC.
  TITLE     Structure of a hyperthermophilic tungstopterin enzyme, aldehyde
            ferredoxin oxidoreductase.
  JOURNAL   Science. 267 (1995) 1463-9.
  ORGANISM  Pyrococcus furiosus [GN:pfu]
REFERENCE   4  [PMID:11265456]
  AUTHORS   Roy R, Menon AL, Adams MW.
  TITLE     Aldehyde oxidoreductases from Pyrococcus furiosus.
  JOURNAL   Methods. Enzymol. 331 (2001) 132-44.
  ORGANISM  Pyrococcus furiosus [GN:pfu]
ORTHOLOGY   KO: K03738  aldehyde:ferredoxin oxidoreductase
GENES       SBL: Sbal_3096
            SBM: Shew185_3106
            SPC: Sputcn32_1189
            SSE: Ssed_2568
            SPL: Spea_0261
            SHW: Sputw3181_2975
            AEH: Mlg_1297
            RFR: Rfer_2850
            PNA: Pnap_0049
            AJS: Ajs_3944
            AZO: azo2930(aorA)
            WSU: WS1844
            GME: Gmet_1045
            GUR: Gura_1195 Gura_2421 Gura_3269 Gura_3550
            PCA: Pcar_0254
            PPD: Ppro_0465 Ppro_0580 Ppro_0888
            DVU: DVU0687
            DVL: Dvul_1877 Dvul_2276
            DDE: Dde_2460 Dde_2943
            DPS: DP2476
            SAT: SYN_00261 SYN_01640 SYN_02419
            SFU: Sfum_1080 Sfum_1479 Sfum_2287
            RRU: Rru_A0313
            STH: STH2886
            CAC: CAC2018
            CBA: CLB_1874(aor)
            CBH: CLC_1881(aor)
            CBF: CLI_2002(aor)
            AMT: Amet_0699 Amet_3157 Amet_4643
            CHY: CHY_1747(aor4)
            DRM: Dred_1830 Dred_2273
            SWO: Swol_1703 Swol_1835
            CSC: Csac_0969
            MTA: Moth_0154 Moth_0722 Moth_2300
            RRS: RoseRS_4359
            RCA: Rcas_0715 Rcas_1863
            TTJ: TTHA0152
            MJA: MJ1185(aor)
            MMP: MMP0945
            MAC: MA1714 MA2962 MA3989(aor)
            MBA: Mbar_A0696
            MMA: MM_0921 MM_2645 MM_3326
            MTP: Mthe_0900
            MHU: Mhun_1005
            MLA: Mlab_0396
            MEM: Memar_0339
            AFU: AF0023(aor-1) AF0077(aor-2) AF0340(aor-3) AF2281(aor-4)
            HMA: rrnAC1318(aor2) rrnAC2064(aor1)
            NPH: NP1432A(aor_2) NP4964A(aor_1) NP5016A(aor_4) NP6186A(aor_3)
            TAC: Ta0810 Ta0834
            TVO: TVN0795 TVN1239
            PHO: PH0028 PH0457 PH0892 PH1019
            PAB: PAB0647(aor-2) PAB1315 PAB2085(aor-1) PAB2330(aor-3)
            PFU: PF0346 PF0464 PF1203 PF1961
            TKO: TK0844 TK1066 TK2163
            RCI: RCIX2090(aor-1) RRC230(aor-2)
            APE: APE_0266.1
            SMR: Smar_0668 Smar_1199
            IHO: Igni_0025 Igni_1032
            HBU: Hbut_1001
            PAI: PAE0622(aor) PAE1029(aor) PAE2052(aor) PAE3427(aor)
            PIS: Pisl_0738 Pisl_0970
            PCL: Pcal_0077 Pcal_0204 Pcal_1040 Pcal_2057
            PAS: Pars_1164 Pars_1880 Pars_2092 Pars_2285
            TPE: Tpen_0094 Tpen_0176 Tpen_1413 Tpen_1817
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.7.5
            ExPASy - ENZYME nomenclature database: 1.2.7.5
            ExplorEnz - The Enzyme Database: 1.2.7.5
            ERGO genome analysis and discovery system: 1.2.7.5
            BRENDA, the Enzyme Database: 1.2.7.5
            CAS: 138066-90-7
///
ENTRY       EC 1.2.7.6                  Enzyme
NAME        glyceraldehyde-3-phosphate dehydrogenase (ferredoxin);
            GAPOR;
            glyceraldehyde-3-phosphate Fd oxidoreductase;
            glyceraldehyde-3-phosphate ferredoxin reductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With an iron-sulfur protein as acceptor
SYSNAME     D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase
REACTION    D-glyceraldehyde-3-phosphate + H2O + 2 oxidized ferredoxin =
            3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin [RN:R07159]
ALL_REAC    R07159
SUBSTRATE   D-glyceraldehyde-3-phosphate;
            H2O [CPD:C00001];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     3-phospho-D-glycerate [CPD:C00197];
            H+ [CPD:C00080];
            reduced ferredoxin [CPD:C00138]
COMMENT     Contains tungsten-molybdopterin and iron-sulfur clusters. This
            enzyme is thought to function in place of glyceralde-3-phosphate
            dehydrogenase and possibly phosphoglycerate kinase in the novel
            Embden-Meyerhof-type glycolytic pathway found in Pyrococcus furiosus
            [1]. It is specific for glyceraldehyde-3-phosphate.
REFERENCE   1  [PMID:7721730]
  AUTHORS   Mukund S, Adams MW.
  TITLE     Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel
            tungsten-containing enzyme with a potential glycolytic role in the
            hyperthermophilic archaeon Pyrococcus furiosus.
  JOURNAL   J. Biol. Chem. 270 (1995) 8389-92.
  ORGANISM  Pyrococcus furiosus [GN:pfu]
REFERENCE   2  [PMID:11265456]
  AUTHORS   Roy R, Menon AL, Adams MW.
  TITLE     Aldehyde oxidoreductases from Pyrococcus furiosus.
  JOURNAL   Methods. Enzymol. 331 (2001) 132-44.
  ORGANISM  Pyrococcus furiosus [GN:pfu]
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.7.6
            ExPASy - ENZYME nomenclature database: 1.2.7.6
            ExplorEnz - The Enzyme Database: 1.2.7.6
            ERGO genome analysis and discovery system: 1.2.7.6
            BRENDA, the Enzyme Database: 1.2.7.6
///
ENTRY       EC 1.2.7.7                  Enzyme
NAME        3-methyl-2-oxobutanoate dehydrogenase (ferredoxin);
            2-ketoisovalerate ferredoxin reductase;
            3-methyl-2-oxobutanoate synthase (ferredoxin);
            VOR;
            branched-chain ketoacid ferredoxin reductase;
            branched-chain oxo acid ferredoxin reductase;
            keto-valine-ferredoxin oxidoreductase;
            ketoisovalerate ferredoxin reductase;
            2-oxoisovalerate ferredoxin reductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With an iron-sulfur protein as acceptor
REACTION    3-methyl-2-oxobutanoate + CoA + oxidized ferredoxin =
            S-(2-methylpropanoyl)-CoA + CO2 + reduced ferredoxin [RN:R07160]
ALL_REAC    R07160
SUBSTRATE   3-methyl-2-oxobutanoate [CPD:C00141];
            CoA [CPD:C00010];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     S-(2-methylpropanoyl)-CoA;
            CO2 [CPD:C00011];
            reduced ferredoxin [CPD:C00138]
COMMENT     This enzyme is one of four 2-oxoacid oxidoreductases that are
            differentiated by their abilities to oxidatively decarboxylate
            different 2-oxoacids and form their CoA derivatives (see also EC
            1.2.7.1, pyruvate synthase; EC 1.2.7.3, 2-oxoglutarate synthase and
            EC 1.2.7.8, indolepyruvate ferredoxin oxidoreductase). It is
            CoA-dependent and contains thiamine diphosphate and iron-sulfur
            clusters. Preferentially utilizes 2-oxo-acid derivatives of branched
            chain amino acids, e.g. 3-methyl-2-oxopentanoate,
            4-methyl-2-oxo-pentanoate, 2-oxobutyrate and
            3-methylthiopropanamine.
REFERENCE   1  [PMID:8550513]
  AUTHORS   Heider J, Mai X, Adams MW.
  TITLE     Characterization of 2-ketoisovalerate ferredoxin oxidoreductase, a
            new and reversible coenzyme A-dependent enzyme involved in peptide
            fermentation by hyperthermophilic archaea.
  JOURNAL   J. Bacteriol. 178 (1996) 780-7.
  ORGANISM  Thermococcus litoralis, Thermococcus sp. , Pyrococcus furiosus
            [GN:pfu], Pyrococcus sp.
REFERENCE   2  [PMID:9108258]
  AUTHORS   Tersteegen A, Linder D, Thauer RK, Hedderich R.
  TITLE     Structures and functions of four anabolic 2-oxoacid oxidoreductases
            in Methanobacterium thermoautotrophicum.
  JOURNAL   Eur. J. Biochem. 244 (1997) 862-8.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
REFERENCE   3  [PMID:11265457]
  AUTHORS   Schut GJ, Menon AL, Adams MW.
  TITLE     2-keto acid oxidoreductases from Pyrococcus furiosus and
            Thermococcus litoralis.
  JOURNAL   Methods. Enzymol. 331 (2001) 144-58.
  ORGANISM  Thermococcus litoralis, Pyrococcus furiosus [GN:pfu]
ORTHOLOGY   KO: K00186  2-oxoisovalerate ferredoxin oxidoreductase, alpha
                        subunit
            KO: K00187  2-oxoisovalerate ferredoxin oxidoreductase, beta subunit
            KO: K00188  2-oxoisovalerate ferredoxin oxidoreductase, delta
                        subunit
            KO: K00189  2-oxoisovalerate ferredoxin oxidoreductase, gamma
                        subunit
            KO: K04089  2-oxoisovalerate ferredoxin oxidoreductase
GENES       ECI: UTI89_C2486(napF)
            GME: Gmet_1307
            DVU: DVU3350
            DDE: Dde_0043
            SFU: Sfum_0115
            CTH: Cthe_0865
            CHY: CHY_0577 CHY_0578 CHY_1972 CHY_1973
            SWO: Swol_1400
            TTE: TTE2198(porA6) TTE2199
            BTH: BT_0329(vorA) BT_0330(vorA) BT_0331(vorB)
            TMA: TM1758 TM1759
            MMP: MMP1271(vorA) MMP1272(vorB) MMP1273(vorC)
            MAC: MA2909(vorA) MA2910(vorB) MA2911(vorC)
            MBA: Mbar_A2173 Mbar_A2174 Mbar_A2175
            MMA: MM_3181(vorC) MM_3182(vorB) MM_3183(vorA)
            MBU: Mbur_0605 Mbur_0606 Mbur_0607
            MTH: MTH703 MTH704 MTH705
            MSI: Msm_0332 Msm_0333
            AFU: AF2052(vorB) AF2053(vorA) AF2054(vorD) AF2055(vorG)
            PHO: PH0680 PH0681
            PAB: PAB1471(VOR) PAB1472(VOR) PAB1473(vor)
            PFU: PF0968 PF0969
            TKO: TK1981
            HBU: Hbut_0730
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.7.7
            ExPASy - ENZYME nomenclature database: 1.2.7.7
            ExplorEnz - The Enzyme Database: 1.2.7.7
            ERGO genome analysis and discovery system: 1.2.7.7
            BRENDA, the Enzyme Database: 1.2.7.7
///
ENTRY       EC 1.2.7.8                  Enzyme
NAME        indolepyruvate ferredoxin oxidoreductase;
            3-(indol-3-yl)pyruvate synthase (ferredoxin);
            IOR
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With an iron-sulfur protein as acceptor
SYSNAME     3-(indol-3-yl)pyruvate:ferredoxin oxidoreductase (decarboxylating,
            CoA-indole-acetylating)
REACTION    (indol-3-yl)pyruvate + CoA + oxidized ferredoxin =
            S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin [RN:R07161]
ALL_REAC    R07161
SUBSTRATE   (indol-3-yl)pyruvate [CPD:C00331];
            CoA [CPD:C00010];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     S-2-(indol-3-yl)acetyl-CoA [CPD:C15489];
            CO2 [CPD:C00011];
            reduced ferredoxin [CPD:C00138]
COMMENT     This enzyme, which is found in archaea, is one of four 2-oxoacid
            oxidoreductases that are differentiated by their abilities to
            oxidatively decarboxylate different 2-oxoacids and form their CoA
            derivatives (see also EC 1.2.7.1, pyruvate synthase, EC 1.2.7.3,
            2-oxoglutarate synthase and EC 1.2.7.7, 2-oxoisovalerate ferredoxin
            reductase) [4]. Contains thiamine diphosphate and [4Fe-4S] clusters.
            Preferentially utilizes the transaminated forms of aromatic amino
            acids and can use phenylpyruvate and p-hydroxyphenylpyruvate as
            substrates.
REFERENCE   1  [PMID:8206994]
  AUTHORS   Mai X, Adams MW.
  TITLE     Indolepyruvate ferredoxin oxidoreductase from the hyperthermophilic
            archaeon Pyrococcus furiosus. A new enzyme involved in peptide
            fermentation.
  JOURNAL   J. Biol. Chem. 269 (1994) 16726-32.
  ORGANISM  Pyrococcus furiosus [GN:pfu]
REFERENCE   2  [PMID:9180697]
  AUTHORS   Siddiqui MA, Fujiwara S, Imanaka T.
  TITLE     Indolepyruvate ferredoxin oxidoreductase from Pyrococcus sp. KOD1
            possesses a mosaic structure showing features of various
            oxidoreductases.
  JOURNAL   Mol. Gen. Genet. 254 (1997) 433-9.
  ORGANISM  Pyrococcus sp.
REFERENCE   3  [PMID:9108258]
  AUTHORS   Tersteegen A, Linder D, Thauer RK, Hedderich R.
  TITLE     Structures and functions of four anabolic 2-oxoacid oxidoreductases
            in Methanobacterium thermoautotrophicum.
  JOURNAL   Eur. J. Biochem. 244 (1997) 862-8.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
REFERENCE   4  [PMID:11265457]
  AUTHORS   Schut GJ, Menon AL, Adams MW.
  TITLE     2-keto acid oxidoreductases from Pyrococcus furiosus and
            Thermococcus litoralis.
  JOURNAL   Methods. Enzymol. 331 (2001) 144-58.
  ORGANISM  Pyrococcus furiosus [GN:pfu], Thermococcus litoralis
ORTHOLOGY   KO: K00179  indolepyruvate ferredoxin oxidoreductase, alpha subunit
            KO: K00180  indolepyruvate ferredoxin oxidoreductase, beta subunit
            KO: K04090  indolepyruvate ferredoxin oxidoreductase
GENES       HHA: Hhal_0068
            RSO: RSc1828(RS04259) RSc1829(RS04261)
            REU: Reut_B5840
            BMA: BMA2584
            BXE: Bxe_A4290
            BUR: Bcep18194_A3418 Bcep18194_A6292
            BCN: Bcen_2326
            BCH: Bcen2424_2940
            BAM: Bamb_0238 Bamb_2988
            BPS: BPSL0356 BPSL3241
            BPM: BURPS1710b_0563(iorA)
            BTE: BTH_I0328 BTH_I3108
            BPA: BPP3902
            BBR: BB4375
            POL: Bpro_4734 Bpro_4735
            VEI: Veis_1965
            EBA: ebA121(iorB) ebA122(iorA)
            AZO: azo1981
            DAR: Daro_0446 Daro_0447
            WSU: WS0713 WS0714
            GSU: GSU1738 GSU1739 GSU2052 GSU2053
            GME: Gmet_0948 Gmet_0949 Gmet_1826 Gmet_1827
            GUR: Gura_2134
            PCA: Pcar_1567 Pcar_1568 Pcar_2116 Pcar_2117
            PPD: Ppro_1667
            DVU: DVU0374 DVU1950 DVU1951
            DVL: Dvul_1217 Dvul_1218
            DDE: Dde_0467
            DPS: DP1264 DP1265
            ADE: Adeh_0039 Adeh_0040
            SAT: SYN_01197 SYN_01198
            SFU: Sfum_0386 Sfum_0387 Sfum_4075 Sfum_4076
            MLO: mlr5448 mlr5450
            RLE: pRL120179
            OAN: Oant_4013
            BJA: bll3410(iorB) bll3411(iorA) blr7589
            BRA: BRADO4317
            BBT: BBta_3242(iorA) BBta_5013
            RPA: RPA1224(iorA)
            RPB: RPB_1232
            RPC: RPC_0693 RPC_0694
            RPD: RPD_4013
            RPE: RPE_0985 RPE_0986 RPE_3529
            SIL: SPO1459 SPO1460 SPOA0110 SPOA0111
            SIT: TM1040_3680
            JAN: Jann_1332 Jann_1333
            RDE: RD1_3230
            SWI: Swit_1880
            RRU: Rru_A1977 Rru_A1978 Rru_A2185
            MAG: amb0179 amb0180 amb3233 amb3234
            CAC: CAC2000(iorB) CAC2001(iorA)
            CDF: CD2380(iorB) CD2381(iorA)
            AMT: Amet_1661 Amet_3333
            CHY: CHY_0121(iorA) CHY_0122(iorB)
            DRM: Dred_3188 Dred_3189
            SWO: Swol_1195
            CSC: Csac_2052
            TTE: TTE2193(porG3) TTE2194(porA5)
            MTA: Moth_0934 Moth_0935 Moth_2276
            NFA: nfa12360
            RHA: RHA1_ro00724 RHA1_ro01629
            SEN: SACE_4073
            BTH: BT_0429(iorB) BT_0430(iorA)
            BFR: BF1694(iorB) BF1695(iorA)
            BFS: BF1701 BF1702
            PGI: PG0674(iorB) PG0675(iorA)
            CTE: CT0113 CT0114
            CPH: Cpha266_1966 Cpha266_1967
            PLT: Plut_0067 Plut_0068
            DET: DET0947(iorA) DET0948(iorB)
            DEH: cbdb_A902(iorA) cbdb_A903(iorB)
            DEB: DehaBAV1_0832
            FNO: Fnod_0053
            MMP: MMP0315(iorB1) MMP0316(iorA1) MMP0713(iorA2) MMP0714(iorB2)
            MVN: Mevan_1326
            MAC: MA1022 MA1023 MA1726(iorB) MA1727(iorA) MA1982(ior)
            MBA: Mbar_A0057 Mbar_A0058 Mbar_A2300 Mbar_A2987 Mbar_A2988
            MMA: MM_2093(iorA) MM_2094(iorB) MM_2634 MM_2635 MM_2788
            MBU: Mbur_0537 Mbur_0761 Mbur_0762 Mbur_1132 Mbur_1133
            MTP: Mthe_0402 Mthe_1171
            MHU: Mhun_2358 Mhun_2359
            MEM: Memar_0807
            MBN: Mboo_0504
            MTH: MTH1852 MTH1853
            MST: Msp_1042(iorB) Msp_1043(iorA)
            MSI: Msm_0391 Msm_0392
            AFU: AF1489(iorA) AF2030(iorB)
            TAC: Ta1012 Ta1013
            TVO: TVN0576 TVN0577
            PHO: PH0229 PH0764 PH0765 PH1138
            PAB: PAB0143(iorB-2) PAB0718(iorA-2) PAB0855(iorA-1)
                 PAB0857(iorB-1)
            PFU: PF0139 PF0533 PF0534 PF0845
            TKO: TK0135 TK0136 TK1643 TK2244
            RCI: RCIX2649(iorA-2) RRC396(iorB) RRC398(iorA-1)
            HBU: Hbut_1625
            SSO: SSO2067(iorA) SSO2069(iorB)
            STO: ST0732 ST0734
            SAI: Saci_2228(iorB) Saci_2229(iorA)
            PAI: PAE3475 PAE3477 PAE3478
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.7.8
            ExPASy - ENZYME nomenclature database: 1.2.7.8
            ExplorEnz - The Enzyme Database: 1.2.7.8
            ERGO genome analysis and discovery system: 1.2.7.8
            BRENDA, the Enzyme Database: 1.2.7.8
///
ENTRY       EC 1.2.7.9        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With an iron-sulfur protein as acceptor
COMMENT     Deleted entry: This enzyme is identical to EC 1.2.7.3,
            2-oxoglutarate synthase (EC 1.2.7.9 created 2003, deleted 2005)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.7.9
            ExPASy - ENZYME nomenclature database: 1.2.7.9
            ExplorEnz - The Enzyme Database: 1.2.7.9
            ERGO genome analysis and discovery system: 1.2.7.9
            BRENDA, the Enzyme Database: 1.2.7.9
///
ENTRY       EC 1.2.99.1       Obsolete  Enzyme
NAME        Transferred to 1.17.99.4
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With other acceptors
COMMENT     Transferred entry: now EC 1.17.99.4, uracil/thymine dehydrogenase
            (EC 1.2.99.1 created 1961, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.99.1
            ExPASy - ENZYME nomenclature database: 1.2.99.1
            ExplorEnz - The Enzyme Database: 1.2.99.1
            ERGO genome analysis and discovery system: 1.2.99.1
            BRENDA, the Enzyme Database: 1.2.99.1
///
ENTRY       EC 1.2.99.2                 Enzyme
NAME        carbon-monoxide dehydrogenase (acceptor);
            anaerobic carbon monoxide dehydrogenase;
            carbon monoxide oxygenase;
            carbon-monoxide dehydrogenase;
            carbon-monoxide:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With other acceptors
SYSNAME     carbon-monoxide:acceptor oxidoreductase
REACTION    CO + H2O + A = CO2 + AH2 [RN:R00296]
ALL_REAC    R00296;
            (other) R05073
SUBSTRATE   CO [CPD:C00237];
            H2O [CPD:C00001];
            A [CPD:C00028]
PRODUCT     CO2 [CPD:C00011];
            AH2 [CPD:C00030]
COFACTOR    Iron [CPD:C00023];
            Zinc [CPD:C00038];
            Nickel [CPD:C00291];
            Iron-sulfur [CPD:C00824]
COMMENT     Contains a [Ni3Fe-4S] cluster and [4Fe-4S] clusters. It uses many
            electron acceptors, including ferredoxin, methyl viologen and benzyl
            viologen and flavins, but not pyridine nucleotides. Forms part of a
            membrane-bound multienzyme complex with EC 1.12.99.6, hydrogenase
            (acceptor), which catalyses the overall reaction: CO + H2O = CO2 +
            H2.
REFERENCE   1  [PMID:3029096]
  AUTHORS   Bonam D, Ludden PW.
  TITLE     Purification and characterization of carbon monoxide dehydrogenase,
            a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum.
  JOURNAL   J. Biol. Chem. 262 (1987) 2980-7.
  ORGANISM  Rhodospirillum rubrum [GN:rru]
REFERENCE   2  [PMID:6687458]
  AUTHORS   Diekert G, Ritter M.
  TITLE     Purification of the nickel protein carbon monoxide dehydrogenase of
            Clostridium thermoaceticum.
  JOURNAL   FEBS. Lett. 151 (1983) 41-4.
  ORGANISM  Clostridium thermoaceticum
REFERENCE   3  [PMID:11593006]
  AUTHORS   Drennan CL, Heo J, Sintchak MD, Schreiter E, Ludden PW.
  TITLE     Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum
            Ni-Fe-S carbon monoxide dehydrogenase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 11973-8.
  ORGANISM  Rhodospirillum rubrum [GN:rru]
REFERENCE   4  [PMID:11509720]
  AUTHORS   Dobbek H, Svetlitchnyi V, Gremer L, Huber R, Meyer O.
  TITLE     Crystal structure of a carbon monoxide dehydrogenase reveals a
            [Ni-4Fe-5S] cluster.
  JOURNAL   Science. 293 (2001) 1281-5.
  ORGANISM  Carboxydothermus hydrogenoformans [GN:chy]
PATHWAY     PATH: map00680  Methane metabolism
ORTHOLOGY   KO: K00190  carbon-monoxide dehydrogenase
            KO: K00191  carbon-monoxide dehydrogenase alpha subunit
            KO: K00192  carbon-monoxide dehydrogenase alpha subunit
            KO: K00193  carbon-monoxide dehydrogenase beta subunit
            KO: K00194  carbon-monoxide dehydrogenase delta subunit
            KO: K00195  carbon-monoxide dehydrogenase epsiolon subunit
            KO: K00196  carbon-monoxide dehydrogenase iron sulfur subunit
            KO: K00197  carbon-monoxide dehydrogenase gamma subunit
            KO: K00198  carbon-monoxide dehydrogenase catalytic subunit
            KO: K03518  carbon-monoxide dehydrogenase small subunit
            KO: K03519  carbon-monoxide dehydrogenase medium subunit
            KO: K03520  carbon-monoxide dehydrogenase large subunit
GENES       ECI: UTI89_C3253
            AHA: AHA_2179
            RSO: RSc1467(RS03840) RSc1468(RS03839) RSc1469(RS03838)
            REU: Reut_A0423 Reut_A0424 Reut_A0425 Reut_B3596 Reut_B3790
                 Reut_B3791 Reut_C5888 Reut_C5889 Reut_C5890
            REH: H16_A0437(coxM1) H16_A0438(coxL1) H16_A0701(coxL2) H16_B0816
                 H16_B1377(coxL6)
            RME: Rmet_0363 Rmet_0364 Rmet_0365
            BXE: Bxe_A2073 Bxe_A2074 Bxe_A2075 Bxe_A2144 Bxe_A2145
                 Bxe_A2146(coxL2) Bxe_A4351 Bxe_A4352(coxL1) Bxe_A4353
                 Bxe_B0074 Bxe_B0075 Bxe_B0076 Bxe_B1053 Bxe_B1054 Bxe_B1055
                 Bxe_B2530 Bxe_B2532 Bxe_B2533 Bxe_C0029 Bxe_C0030
                 Bxe_C0031(coxL)
            BPE: BP0590 BP0591 BP0684A BP0685
            BPA: BPP0278 BPP0279 BPP0388 BPP0389
            BBR: BB0281 BB0282 BB0390 BB0391 BB0392
            POL: Bpro_0576 Bpro_0577 Bpro_0578 Bpro_3394
            VEI: Veis_4542 Veis_4543
            MMS: mma_0774(cutL) mma_0775(cutM) mma_0776
            CCV: CCV52592_1131(cooS)
            CCO: CCC13826_0236(cooS) CCC13826_1945
            GSU: GSU2098(cooS)
            GUR: Gura_0618
            PCA: Pcar_0888
            DVU: DVU2098(cooS)
            DVL: Dvul_1133
            DDE: Dde_3028
            DPS: DP1726
            SAT: SYN_00351
            SFU: Sfum_2564 Sfum_2565 Sfum_2566 Sfum_2567 Sfum_2875
            MLO: mll1127 mll1128 mll1129 mlr7702
            MES: Meso_0058 Meso_0059 Meso_0060 Meso_0907
            SME: SMc03101 SMc03102 SMc03103
            SMD: Smed_2881
            RLE: pRL120302(yagT) pRL80021(coxG) pRL80023(coxL) pRL80024(coxS)
            BJA: bll3968 bll5664(cooxM) bll5665(cooxS) bll5914 bll6237(cutL)
                 bll6239(cutM) bll7271 blr0335 blr0336 blr0337 blr3350(cutL)
                 blr3351(cutM) blr3352 blr3533(cutL) blr3534(cutM) blr3535
            BRA: BRADO2857 BRADO2858 BRADO2882 BRADO3149 BRADO4584 BRADO4585
                 BRADO4586 BRADO6029(coxL) BRADO6030(coxS) BRADO6031(coxM)
                 BRADO6663 BRADO6957 BRADO6958 BRADO6959
            BBT: BBta_0572 BBta_0573 BBta_0574 BBta_0872 BBta_1747(coxM)
                 BBta_1748(coxS) BBta_1749(coxL) BBta_1909 BBta_1910 BBta_1911
                 BBta_2633(coxS) BBta_2634(coxL) BBta_2635(coxM) BBta_3595
                 BBta_3730 BBta_3731 BBta_3732 BBta_5317 BBta_5318
            RPA: RPA1572 RPA2194 RPA3802 RPA3803 RPA3974 RPA4666(coxS)
                 RPA4667(coxL) RPA4668(coxM)
            RPB: RPB_0911 RPB_0912 RPB_0913 RPB_1613 RPB_3094 RPB_3095
                 RPB_3096 RPB_3102 RPB_3103 RPB_3104 RPB_3111 RPB_3112 RPB_3198
                 RPB_3677 RPB_3678 RPB_3957
            RPC: RPC_0848 RPC_0849 RPC_0850 RPC_1439 RPC_1632 RPC_3083
                 RPC_4498 RPC_4528 RPC_4529 RPC_4530
            RPD: RPD_1022 RPD_1023 RPD_1024 RPD_1624 RPD_1782 RPD_1783
                 RPD_2257 RPD_3715
            RPE: RPE_1460 RPE_1655 RPE_1656 RPE_4323 RPE_4568 RPE_4569
                 RPE_4570
            NWI: Nwi_1079 Nwi_2204 Nwi_2205
            NHA: Nham_1307 Nham_1453 Nham_1454 Nham_1455 Nham_2606 Nham_2607
            SIL: SPO1518(coxS-1) SPO1519(coxL-1) SPO1520 SPO2397(coxL-2)
                 SPO2398(coxS-2) SPO2399(coxM) SPO2881 SPO3019
            SIT: TM1040_1705 TM1040_1764 TM1040_1765 TM1040_1766
            RSP: RSP_2876 RSP_2877(coxL) RSP_2878(coxS)
            RSH: Rsph17029_1523
            JAN: Jann_1765 Jann_1766 Jann_2095 Jann_2949
            RDE: RD1_1758 RD1_2972(coxM) RD1_2973(coxL) RD1_2974(coxS)
            ACR: Acry_0077 Acry_1968 Acry_2211
            RRU: Rru_A0965 Rru_A0966 Rru_A0967 Rru_A1427
            MAG: amb2881 amb2882 amb3707
            SUS: Acid_2226
            GKA: GKP18 GKP19 GKP21
            CAC: CAC0116 CAC2498
            CTC: CTC01156
            CNO: NT01CX_0669(cooS)
            CTH: Cthe_2801
            CDF: CD0716(cooS) CD2088(cutS)
            CBA: CLB_1359 CLB_2157
            CBH: CLC_1369
            CBF: CLI_1426 CLI_2267
            CBE: Cbei_3020 Cbei_5054
            AMT: Amet_1177 Amet_2016 Amet_3764
            CHY: CHY_0034(cooSV) CHY_0085(cooSII) CHY_0690(coxM)
                 CHY_0736(cooSIV) CHY_1222(acsB) CHY_1223(acsC) CHY_1226(acsD)
                 CHY_1824(cooSI)
            DSY: DSY0864 DSY1648 DSY1651 DSY1652 DSY1653 DSY2630 DSY4173
                 DSY4442
            DRM: Dred_0652
            CSC: Csac_0400
            TTE: TTE1708
            MTA: Moth_1198 Moth_1201 Moth_1202 Moth_1203 Moth_1972
            MTU: Rv0373c Rv0374c Rv0375c
            MTC: MT0388 MT0389 MT0390
            MBO: Mb0380c Mb0381c Mb0382c
            MBB: BCG_0411c BCG_0412c BCG_0413c
            MSM: MSMEG_0744 MSMEG_0745 MSMEG_0746 MSMEG_5880 MSMEG_5882
            MVA: Mvan_5183 Mvan_5185
            MGI: Mflv_1571 Mflv_1573
            MMC: Mmcs_0489 Mmcs_0490 Mmcs_0491 Mmcs_4600 Mmcs_4602 Mmcs_4603
            MKM: Mkms_0500 Mkms_4688 Mkms_4690
            MJL: Mjls_4983 Mjls_4985
            RHA: RHA1_ro03489 RHA1_ro03490 RHA1_ro04975 RHA1_ro04976
                 RHA1_ro04977 RHA1_ro05230 RHA1_ro05231 RHA1_ro05232
            NCA: Noca_0230 Noca_0596 Noca_1489 Noca_1491 Noca_3969
            TFU: Tfu_2586 Tfu_2587
            FAL: FRAAL6162
            ACE: Acel_1638
            SEN: SACE_0536 SACE_0537 SACE_0538 SACE_1160 SACE_1161 SACE_1162
                 SACE_4017 SACE_4018 SACE_4019 SACE_4873 SACE_4874 SACE_5140
            RXY: Rxyl_1872 Rxyl_1874
            AVA: Ava_3188 Ava_C0128
            CPH: Cpha266_0149
            DET: DET0665(acsC-1) DET0666 DET0667(acsD-1) DET0699(acsC-2)
                 DET0700 DET0701(acsD-2)
            DEH: cbdb_A651(acsC) cbdb_A652(codH) cbdb_A654(acsD)
            DGE: Dgeo_1946 Dgeo_1947
            MJA: MJ0112(cdhE) MJ0113(cdhD) MJ0152 MJ0153(cdhA) MJ0154(cdhB)
                 MJ0156(cdhC) MJ0264 MJ0265(cooF2) MJ0728(cooS)
            MMP: MMP0980(cdh) MMP0981(cdhD) MMP0983(cdhB) MMP0984(cdh)
                 MMP0985(cdhA)
            MMQ: MmarC5_0805
            MMZ: MmarC7_0227
            MAE: Maeo_0475 Maeo_1174
            MVN: Mevan_0311
            MAC: MA1011(cdhE) MA1012(cdhD) MA1014(cdhC) MA1015(cdhB)
                 MA1016(cdhA) MA1309(cooS) MA3282(cooS) MA3860(cdhA)
                 MA3861(cdhB) MA3862(cdhC) MA3864(cdhD) MA3865(cdhE)
                 MA4399(cdhA)
            MBA: Mbar_A0199 Mbar_A0200 Mbar_A0202 Mbar_A0203 Mbar_A0204
                 Mbar_A0429 Mbar_A0430 Mbar_A0432 Mbar_A0433 Mbar_A0434
                 Mbar_A3525 Mbar_A3717
            MMA: MM_0121 MM_0684 MM_0685 MM_0686 MM_0688 MM_0689 MM_2084
                 MM_2085 MM_2087 MM_2088 MM_2089 MM_2301
            MBU: Mbur_0858 Mbur_0859 Mbur_0862 Mbur_0863
            MTP: Mthe_0291 Mthe_0292 Mthe_1216 Mthe_1341
            MHU: Mhun_0686 Mhun_0687 Mhun_0689 Mhun_0690 Mhun_1272
            MBN: Mboo_0884 Mboo_1373
            MTH: MTH1708 MTH1709 MTH1710 MTH1712 MTH1713
            MSI: Msm_0561
            MKA: MK0536 MK0717(cdhA_1) MK0718(cdhB) MK0719(cdhA_1)
                 MK0720(cdhC) MK0722(cdhD) MK0723(cdhE)
            AFU: AF0376(cdhE) AF0377(cdhD) AF0379(cdhC) AF0950(cooF)
                 AF1100(cdhA-1) AF1101(cdhB-1) AF1849(cooS) AF2397(cdhA-2)
                 AF2398(cdhB-2)
            HMA: pNG7247(cutC)
            HWA: HQ1942A(coxM) HQ1943A(coxS) HQ1944A(coxL)
            PTO: PTO1119 PTO1120 PTO1121
            RCI: LRC456(cdhA) LRC458(cdhB) LRC459(cdhC) LRC461(cdhD)
                 LRC463(cdhE)
            APE: APE_2213 APE_2216.1 APE_2219
            SSO: SSO2433(cutC-1) SSO2434(cutB-1) SSO2636(cutB-2)
                 SSO2637(cutC-2) SSO2639(cutA-4)
            STO: ST0561 ST0562 ST1781 ST1783
            SAI: Saci_0916 Saci_0917 Saci_2269(cutB) Saci_2270(cutC)
                 Saci_2271(cutA)
            MSE: Msed_0297
            PAI: PAE1935 PAE1936 PAE1939
STRUCTURES  PDB: 1JQK  1MJG  1N5W  1N60  1N61  1N62  1N63  1OAO  1SU6  1SU7  
                 1SU8  1SUF  1ZXI  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.99.2
            ExPASy - ENZYME nomenclature database: 1.2.99.2
            ExplorEnz - The Enzyme Database: 1.2.99.2
            ERGO genome analysis and discovery system: 1.2.99.2
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.99.2
            BRENDA, the Enzyme Database: 1.2.99.2
            CAS: 64972-88-9
///
ENTRY       EC 1.2.99.3                 Enzyme
NAME        aldehyde dehydrogenase (pyrroloquinoline-quinone);
            aldehyde dehydrogenase (acceptor)
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With other acceptors
SYSNAME     aldehyde:(pyrroloquinoline-quinone) oxidoreductase
REACTION    an aldehyde + acceptor + H2O = a carboxylate + reduced acceptor
            [RN:R00544]
ALL_REAC    R00544 > R00638 R01019 R03535 R05120
SUBSTRATE   aldehyde [CPD:C00071];
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
PRODUCT     carboxylate [CPD:C00060];
            reduced acceptor [CPD:C00030]
COFACTOR    PQQ [CPD:C00113]
COMMENT     A quinoprotein. Wide specificity; acts on straight-chain aldehydes
            up to C10, aromatic aldehydes, glyoxylate and glyceraldehyde.
REFERENCE   1
  AUTHORS   Ameyama, M. and Adachi, O.
  TITLE     Aldehyde dehydrogenase from acetic acid bacteria, membrane-bound.
  JOURNAL   Methods Enzymol. 89 (1982) 491-497.
  ORGANISM  Gluconobacter oxydans subsp. suboxydans, Acetobacter aceti
REFERENCE   2
  AUTHORS   Ameyama, M., Osada, K., Shinagawa, E., Matsushita, K. and Adachi, O.
  TITLE     Purification and characterization of aldehyde dehydrogenase of
            Acetobacter aceti.
  JOURNAL   Agric. Biol. Chem. 45 (1981) 1189-1890.
  ORGANISM  Acetobacter aceti
REFERENCE   3  [PMID:6779711]
  AUTHORS   Patel RN, Hou CT, Derelanko P, Felix A.
  TITLE     Purification and properties of a heme-containing aldehyde
            dehydrogenase from Methylosinus trichosporium.
  JOURNAL   Arch. Biochem. Biophys. 203 (1980) 654-62.
  ORGANISM  Methylosinus trichosporium
PATHWAY     PATH: map00071  Fatty acid metabolism
            PATH: map00620  Pyruvate metabolism
            PATH: map00640  Propanoate metabolism
            PATH: map00650  Butanoate metabolism
GENES       BUR: Bcep18194_A4471
            RPB: RPB_1669
            NHA: Nham_1181
            GOX: GOX0587
            GBE: GbCGDNIH1_0793 GbCGDNIH1_0794 GbCGDNIH1_0795
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.99.3
            ExPASy - ENZYME nomenclature database: 1.2.99.3
            ExplorEnz - The Enzyme Database: 1.2.99.3
            ERGO genome analysis and discovery system: 1.2.99.3
            BRENDA, the Enzyme Database: 1.2.99.3
            CAS: 75536-77-5
///
ENTRY       EC 1.2.99.4                 Enzyme
NAME        formaldehyde dismutase;
            aldehyde dismutase;
            cannizzanase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With other acceptors
SYSNAME     formaldehyde:formaldehyde oxidoreductase
REACTION    2 formaldehyde = formate + methanol [RN:R00614]
ALL_REAC    R00614
SUBSTRATE   formaldehyde [CPD:C00067]
PRODUCT     formate [CPD:C00058];
            methanol [CPD:C00132]
COMMENT     Formaldehyde and acetaldehyde can act as donors; formaldehyde,
            acetaldehyde and propanal can act as acceptors.
REFERENCE   1
  AUTHORS   Kato, N., Shirakawa, K., Kobayashi, H. and Sakazawa, C.
  TITLE     The dismutation of aldehydes by a bacterial enzyme.
  JOURNAL   Agric. Biol. Chem. 47 (1983) 39-46.
  ORGANISM  Pseudomonas putida [GN:ppu]
STRUCTURES  PDB: 2DPH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.99.4
            ExPASy - ENZYME nomenclature database: 1.2.99.4
            ExplorEnz - The Enzyme Database: 1.2.99.4
            ERGO genome analysis and discovery system: 1.2.99.4
            BRENDA, the Enzyme Database: 1.2.99.4
            CAS: 85204-94-0
///
ENTRY       EC 1.2.99.5                 Enzyme
NAME        formylmethanofuran dehydrogenase;
            formylmethanofuran:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With other acceptors
SYSNAME     formylmethanofuran:acceptor oxidoreductase
REACTION    formylmethanofuran + H2O + acceptor = CO2 + methanofuran + reduced
            acceptor [RN:R03015]
ALL_REAC    R03015
SUBSTRATE   formylmethanofuran [CPD:C01001];
            H2O [CPD:C00001];
            acceptor [CPD:C00028]
PRODUCT     CO2 [CPD:C00011];
            methanofuran [CPD:C00862];
            reduced acceptor [CPD:C00030]
COFACTOR    Molybdenum [CPD:C00150];
            Pterin [CPD:C00715]
COMMENT     A molybdoprotein containing a pterin cofactor. Methyl viologen can
            act as acceptor. Also oxidizes N-furfurylformamide.
REFERENCE   1  [PMID:2125267]
  AUTHORS   Karrasch M, Borner G, Enssle M, Thauer RK.
  TITLE     The molybdoenzyme formylmethanofuran dehydrogenase from
            Methanosarcina barkeri contains a pterin cofactor.
  JOURNAL   Eur. J. Biochem. 194 (1990) 367-72.
  ORGANISM  Methanosarcina barkeri [GN:mba]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K00199  formylmethanofuran dehydrogenase
            KO: K00200  formylmethanofuran dehydrogenase subunit A
            KO: K00201  formylmethanofuran dehydrogenase subunit B
            KO: K00202  formylmethanofuran dehydrogenase subunit C
            KO: K00203  formylmethanofuran dehydrogenase subunit D
            KO: K00204  formylmethanofuran dehydrogenase subunit E
            KO: K00205  formylmethanofuran dehydrogenase subunit F
GENES       ECI: UTI89_C1866(ydhY)
            ACI: ACIAD2526
            MCA: MCA2859 MCA2860
            NOC: Noc_0022 Noc_0024 Noc_0025
            BXE: Bxe_B2461(fhcB) Bxe_B2462(fhcA) Bxe_B2464(fhcC)
            MPT: Mpe_A2623 Mpe_A2624
            MFA: Mfla_1662 Mfla_1663 Mfla_1665
            SAT: SYN_00638
            RET: RHE_PE00420(glxC)
            RLE: pRL110556(glxC)
            BRA: BRADO5884
            BBT: BBta_1943
            RDE: RD1_4252
            GBE: GbCGDNIH1_0778 GbCGDNIH1_0779 GbCGDNIH1_0781
            RHA: RHA1_ro02818
            RBA: RB9834(fwdA) RB9836(fwdC)
            MJA: MJ0658 MJ1165(fwdE) MJ1166(fwdF) MJ1167(fwdG) MJ1168(fwdD)
                 MJ1169(fwdA) MJ1171(fwdC) MJ1194m(fwdB)
            MMP: MMP0070 MMP0200(fmdE) MMP0508(fmdE) MMP0509(fmdA)
                 MMP0510(fmdC) MMP0511(fmdB) MMP0512(fmdB) MMP1244(fwdH)
                 MMP1245(fwdF) MMP1246(fwdG) MMP1247(fwdD) MMP1248(fwdA)
                 MMP1249(fwdC) MMP1691(fwdB)
            MMQ: MmarC5_0342 MmarC5_1450
            MMZ: MmarC7_0495 MmarC7_1531
            MAE: Maeo_0084 Maeo_1442
            MVN: Mevan_0563 Mevan_1663
            MAC: MA0304(fmdE) MA0305(fmdF) MA0306(fmdA) MA0307(fmdC)
                 MA0308(fmdD) MA0309(fmdB) MA0671(fwdG) MA0832(fwdC)
                 MA0833(fwdA) MA0834(fwdB) MA0835(fwuD) MA1241(fmdB) MA2867
                 MA2877(fwdG) MA2878(fwdB) MA2879(fwdD) MA4174(fmdF)
                 MA4175(fmdA) MA4176(fmdC) MA4177(fmdD) MA4178(fmdB)
            MBA: Mbar_A1287 Mbar_A1288 Mbar_A1289 Mbar_A1290 Mbar_A1291
                 Mbar_A1292 Mbar_A1560 Mbar_A1763 Mbar_A2588 Mbar_A2921
                 Mbar_A2922 Mbar_A2923
            MMA: MM_0055 MM_0058 MM_0059 MM_0060 MM_1564 MM_1565(fmdF)
                 MM_1566(fmdA) MM_1567(fmdC) MM_1568(fmdD) MM_1569(fmdB)
                 MM_1824 MM_1978 MM_1979 MM_1980 MM_1981
            MBU: Mbur_0281 Mbur_0282 Mbur_0283 Mbur_0284 Mbur_0285 Mbur_0286
                 Mbur_0335 Mbur_0336 Mbur_0337 Mbur_0553 Mbur_1478
            MTP: Mthe_1098
            MHU: Mhun_1981 Mhun_1982 Mhun_1983 Mhun_1984 Mhun_1985 Mhun_1988
                 Mhun_1989 Mhun_1990 Mhun_2112
            MEM: Memar_0370 Memar_0618
            MBN: Mboo_0875 Mboo_1473
            MTH: MTH1553 MTH1554 MTH1555 MTH1556 MTH1557 MTH1558 MTH1559
                 MTH238 MTH918 MTH919 MTH926
            MST: Msp_0241(fwdG) Msp_0242(fwdD) Msp_0243(fwdB) Msp_0244(fwdA)
                 Msp_0245(fwdC)
            MSI: Msm_1408 Msm_1409 Msm_1410 Msm_1411 Msm_1412 Msm_1413
                 Msm_1414
            MKA: MK0259(fwdB_1) MK0307(fwdF_1) MK0323(fwd_F2) MK1525(fwdG)
                 MK1526(fwdD) MK1527(fwdB_2) MK1529(fwdA) MK1530(fwdC)
            AFU: AF1644(fwdF) AF1649(fwdG) AF1650(fwdB-1) AF1651(fwdD-1)
                 AF1928(fwdD-2) AF1929(fwdB-2) AF1930(fwdA) AF1931(fwdC)
            RCI: RCIA24(fwdG-1) RCIX1392(fwdE) RCIX1639(fmdE) RCIX1641(fmdB)
                 RCIX1642(fmdD) RCIX598(fwdD-1) RCIX599(fwdB-1) RCIX600(fwdA-1)
                 RCIX601(fwdC-1) RRC253(fwdG-2) RRC254(fwdF-2) RRC260(fwdD-2)
                 RRC261(fwdB-2) RRC262(fwdA-2) RRC263(fwdC-2)
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.99.5
            ExPASy - ENZYME nomenclature database: 1.2.99.5
            ExplorEnz - The Enzyme Database: 1.2.99.5
            ERGO genome analysis and discovery system: 1.2.99.5
            UM-BBD (Biocatalysis/Biodegradation Database): 1.2.99.5
            BRENDA, the Enzyme Database: 1.2.99.5
            CAS: 119940-12-4
///
ENTRY       EC 1.2.99.6                 Enzyme
NAME        carboxylate reductase;
            aldehyde:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With other acceptors
SYSNAME     aldehyde:acceptor oxidoreductase
REACTION    an aldehyde + acceptor + H2O = a carboxylate + reduced acceptor
            [RN:R00544]
ALL_REAC    R00544 > R00326
SUBSTRATE   aldehyde [CPD:C00071];
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
PRODUCT     carboxylate [CPD:C00060];
            reduced acceptor [CPD:C00030]
COFACTOR    Tungsten [CPD:C00753]
COMMENT     A tungsten protein. Methyl viologen can act as acceptor. In the
            reverse direction, non-activated acids are reduced by reduced
            viologens to aldehydes, but not to the corresponding alcohols.
REFERENCE   1  [PMID:2550230]
  AUTHORS   White H, Strobl G, Feicht R, Simon H.
  TITLE     Carboxylic acid reductase: a new tungsten enzyme catalyses the
            reduction of non-activated carboxylic acids to aldehydes.
  JOURNAL   Eur. J. Biochem. 184 (1989) 89-96.
  ORGANISM  Clostridium thermoaceticum
PATHWAY     PATH: map00620  Pyruvate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.99.6
            ExPASy - ENZYME nomenclature database: 1.2.99.6
            ExplorEnz - The Enzyme Database: 1.2.99.6
            ERGO genome analysis and discovery system: 1.2.99.6
            BRENDA, the Enzyme Database: 1.2.99.6
            CAS: 125008-36-8
///
ENTRY       EC 1.2.99.7                 Enzyme
NAME        aldehyde dehydrogenase (FAD-independent);
            aldehyde oxidase;
            aldehyde oxidoreductase;
            Mop;
            AORDd
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With other acceptors
SYSNAME     aldehyde:acceptor oxidoreductase (FAD-independent)
REACTION    an aldehyde + H2O + acceptor = a carboxylate + reduced acceptor
            [RN:R00544]
ALL_REAC    R00544
SUBSTRATE   aldehyde [CPD:C00071];
            H2O [CPD:C00001];
            acceptor [CPD:C00028]
PRODUCT     carboxylate [CPD:C00060];
            reduced acceptor [CPD:C00030]
COMMENT     Belongs to the xanthine oxidase family of enzymes. The enzyme from
            Desulfovibrio sp. contains a molybdenum-molybdopterin-cytosine
            dinucleotide (MCD) complex and two types of [2Fe-2S] cluster per
            monomer, but does not contain FAD.
REFERENCE   1  [PMID:14659539]
  AUTHORS   Uchida H, Kondo D, Yamashita A, Nagaosa Y, Sakurai T, Fujii Y,
            Fujishiro K, Aisaka K, Uwajima T.
  TITLE     Purification and characterization of an aldehyde oxidase from
            Pseudomonas sp. KY 4690.
  JOURNAL   FEMS. Microbiol. Lett. 229 (2003) 31-6.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:10679276]
  AUTHORS   Duarte RO, Archer M, Dias JM, Bursakov S, Huber R, Moura I, Romao
            MJ, Moura JJ.
  TITLE     Biochemical/spectroscopic characterization and preliminary X-ray
            analysis of a new aldehyde oxidoreductase isolated from
            Desulfovibrio desulfuricans ATCC 27774.
  JOURNAL   Biochem. Biophys. Res. Commun. 268 (2000) 745-9.
  ORGANISM  Desulfovibrio desulfuricans [GN:dde]
REFERENCE   3  [PMID:10727945]
  AUTHORS   Andrade SL, Brondino CD, Feio MJ, Moura I, Moura JJ.
  TITLE     Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB
            13491 EPR assignment of the proximal [2Fe-2S] cluster to the Mo
            site.
  JOURNAL   Eur. J. Biochem. 267 (2000) 2054-61.
  ORGANISM  Desulfovibrio alaskensis
REFERENCE   4  [PMID:7502041]
  AUTHORS   Romao MJ, Archer M, Moura I, Moura JJ, LeGall J, Engh R, Schneider
            M, Hof P, Huber R.
  TITLE     Crystal structure of the xanthine oxidase-related aldehyde
            oxido-reductase from D. gigas.
  JOURNAL   Science. 270 (1995) 1170-6.
  ORGANISM  Desulfovibrio gigas
GENES       DVU: DVU1559(mop)
            DDE: Dde_3539
            DPS: DP0270
STRUCTURES  PDB: 1ZCS  
DBLINKS     IUBMB Enzyme Nomenclature: 1.2.99.7
            ExPASy - ENZYME nomenclature database: 1.2.99.7
            ExplorEnz - The Enzyme Database: 1.2.99.7
            ERGO genome analysis and discovery system: 1.2.99.7
            BRENDA, the Enzyme Database: 1.2.99.7
///
ENTRY       EC 1.2.99.-                 Enzyme
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors;
            With other acceptors
SUBSTRATE   3-Chloroallyl aldehyde [CPD:C06613];
            H2O [CPD:C00001];
            cis-3-Chloroallyl aldehyde [CPD:C16348]
PRODUCT     trans-3-Chloroacrylic acid [CPD:C06614];
            H+ [CPD:C00080];
            cis-3-Chloroacrylic acid [CPD:C06615]
///
ENTRY       EC 1.2.-.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on the aldehyde or oxo group of donors
REACTION    (1) 4-Chlorobenzoate <=> 4-Chlorobenzaldehyde + H2O [RN:R05252];
            (2) Myrtenal + H2O + Acceptor <=> Myrtenic acid + Reduced acceptor
            [RN:R06403]
SUBSTRATE   4-Chlorobenzoate [CPD:C02370];
            Myrtenal [CPD:C11939];
            H2O [CPD:C00001];
            Acceptor [CPD:C00028]
PRODUCT     4-Chlorobenzaldehyde [CPD:C06648];
            H2O [CPD:C00001];
            Myrtenic acid [CPD:C11940];
            Reduced acceptor [CPD:C00030]
///
ENTRY       EC 1.3.1.1                  Enzyme
NAME        dihydrouracil dehydrogenase (NAD+);
            dehydrogenase, dihydrouracil;
            dihydropyrimidine dehydrogenase;
            dihydrothymine dehydrogenase;
            pyrimidine reductase;
            thymine reductase;
            uracil reductase;
            dihydrouracil dehydrogenase (NAD+)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     5,6-dihydrouracil:NAD+ oxidoreductase
REACTION    5,6-dihydrouracil + NAD+ = uracil + NADH + H+ [RN:R00977]
ALL_REAC    R00977;
            (other) R01414
SUBSTRATE   5,6-dihydrouracil [CPD:C00429];
            NAD+ [CPD:C00003]
PRODUCT     uracil [CPD:C00106];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13462991]
  AUTHORS   CAMPBELL LL Jr.
  TITLE     Reductive degradation of pyrimidines. III. Purification and
            properties of dihydrouracil dehydrogenase.
  JOURNAL   J. Biol. Chem. 227 (1957) 693-700.
  ORGANISM  Clostridium uracilicum
PATHWAY     PATH: map00240  Pyrimidine metabolism
            PATH: map00410  beta-Alanine metabolism
            PATH: map00770  Pantothenate and CoA biosynthesis
GENES       SYR: SynRCC307_2353(pyrD)
            SYX: SynWH7803_2368(pyrD)
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.1
            ExPASy - ENZYME nomenclature database: 1.3.1.1
            ExplorEnz - The Enzyme Database: 1.3.1.1
            ERGO genome analysis and discovery system: 1.3.1.1
            BRENDA, the Enzyme Database: 1.3.1.1
            CAS: 9026-89-5
///
ENTRY       EC 1.3.1.2                  Enzyme
NAME        dihydropyrimidine dehydrogenase (NADP+);
            dihydrothymine dehydrogenase;
            dihydrouracil dehydrogenase (NADP+);
            4,5-dihydrothymine: oxidoreductase;
            DPD;
            DHPDH;
            dehydrogenase, dihydrouracil (nicotinamide adenine dinucleotide
            phosphate);
            dihydrouracil dehydrogenase (NADP+);
            DHU dehydrogenase;
            hydropyrimidine dehydrogenase;
            dihydropyrimidine dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     5,6-dihydrouracil:NADP+ 5-oxidoreductase
REACTION    5,6-dihydrouracil + NADP+ = uracil + NADPH + H+ [RN:R00978]
ALL_REAC    R00978;
            (other) R01415
SUBSTRATE   5,6-dihydrouracil [CPD:C00429];
            NADP+ [CPD:C00006]
PRODUCT     uracil [CPD:C00106];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts on dihydrothymine.
REFERENCE   1  [PMID:13825299]
  AUTHORS   FRITZSON P.
  TITLE     Properties and assay of dihydrouracil dehydrogenase of rat liver.
  JOURNAL   J. Biol. Chem. 235 (1960) 719-25.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:7451435]
  AUTHORS   Shiotani T, Weber G.
  TITLE     Purification and properties of dihydrothymine dehydrogenase from rat
            liver.
  JOURNAL   J. Biol. Chem. 256 (1981) 219-24.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00240  Pyrimidine metabolism
            PATH: map00410  beta-Alanine metabolism
            PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K00207  dihydropyrimidine dehydrogenase (NADP+)
GENES       HSA: 1806(DPYD)
            MMU: 99586(Dpyd)
            RNO: 81656(Dpyd)
            CFA: 479935(DPYD)
            BTA: 281124(DPYD)
            SSC: 397109(DPYD)
            GGA: 429083(DPYD)
            XLA: 447312(MGC81821)
            DRE: 405829(dpyd)
            SPU: 575768(LOC575768) 758949(LOC758949)
            DME: Dmel_CG2194(Reg-3)
            CEL: C25F6.3
            OSA: 4330657
            DDI: DDB_0231100(pyd1)
            TET: TTHERM_01250100
            EHI: 14.t00017
            PAE: PA0439
            PAU: PA14_05740(pydA)
            PPU: PP_4038
            PFL: PFL_2546
            PFO: Pfl_3443
            PEN: PSEEN3251
            BXE: Bxe_A1429
            BVI: Bcep1808_5511
            BUR: Bcep18194_C6656
            BCN: Bcen_1595
            BCH: Bcen2424_6236
            BAM: Bamb_5965
            PNA: Pnap_4020
            AAV: Aave_0967
            VEI: Veis_4151
            MLO: mll1643
            MES: Meso_2055
            SME: SMc01815
            RLE: RL3708(pydA)
            BME: BMEI1639
            BMF: BAB1_0313
            BMS: BR0282
            SIL: SPO1777
            SIT: TM1040_1500
            RSP: RSP_0187
            RSH: Rsph17029_1820
            RSQ: Rsph17025_1458
            JAN: Jann_2712
            RDE: RD1_3103
            SUS: Acid_7660
            BCL: ABC3782
            GKA: GK1422
            LRE: Lreu_1309
            CBE: Cbei_1943
            HMA: rrnAC0052(dpd)
STRUCTURES  PDB: 1GT8  1GTE  1GTH  1H7W  1H7X  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.2
            ExPASy - ENZYME nomenclature database: 1.3.1.2
            ExplorEnz - The Enzyme Database: 1.3.1.2
            ERGO genome analysis and discovery system: 1.3.1.2
            BRENDA, the Enzyme Database: 1.3.1.2
            CAS: 9029-01-0
///
ENTRY       EC 1.3.1.3                  Enzyme
NAME        Delta4-3-oxosteroid 5beta-reductase;
            3-oxo-Delta4-steroid 5beta-reductase;
            5beta-reductase;
            androstenedione 5beta-reductase;
            cholestenone 5beta-reductase;
            cortisone 5beta-reductase;
            cortisone beta-reductase;
            cortisone Delta4-5beta-reductase;
            steroid 5beta-reductase;
            testosterone 5beta-reductase;
            Delta4-3-ketosteroid 5beta-reductase;
            Delta4-5beta-reductase;
            Delta4-hydrogenase;
            4,5beta-dihydrocortisone:NADP+ Delta4-oxidoreductase;
            3-oxo-5beta-steroid:NADP+ Delta4-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     5beta-cholestan-3-one:NADP+ 4,5-oxidoreductase
REACTION    (1) 5beta-cholestan-3-one + NADP+ = cholest-4-en-3-one + NADPH + H+
            [RN:R02609];
            (2) 17,21-dihydroxy-5beta-pregnane-3,11,20-trione + NADP+ =
            cortisone + NADPH + H+ [RN:R02893]
ALL_REAC    R02609 R02893;
            (other) R02219 R02841 R03713 R04817 R04823
SUBSTRATE   5beta-cholestan-3-one [CPD:C03091];
            NADP+ [CPD:C00006];
            17,21-dihydroxy-5beta-pregnane-3,11,20-trione
PRODUCT     cholest-4-en-3-one [CPD:C00599];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            cortisone [CPD:C00762]
COMMENT     The enzyme from human efficiently catalyses the reduction of
            progesterone, androstenedione, 17alpha-hydroxyprogesterone and
            testosterone to 5beta-reduced metabolites; it can also act on
            aldosterone, corticosterone and cortisol, but to a lesser extent
            [8]. The bile acid intermediates
            7alpha,12alpha-dihydroxy-4-cholesten-3-one and
            7alpha-hydroxy-4-cholesten-3-one can also act as substrates [9].
REFERENCE   1  [PMID:13376613]
  AUTHORS   DORFMAN RI, FORCHIELLI E.
  TITLE     Separation of delta 4-5 alpha-hydrogenases from rat liver
            homogenates.
  JOURNAL   J. Biol. Chem. 223 (1956) 443-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:13805063]
  AUTHORS   BROWN-GRANT K, FORCHIELLI E, DORFMAN RI.
  TITLE     The delta4-hydrogenases of guinea pig adrenal gland.
  JOURNAL   J. Biol. Chem. 235 (1960) 1317-20.
  ORGANISM  guinea pig
REFERENCE   3
  AUTHORS   Levy, H.R. and Talalay, P.
  TITLE     Enzymatic introduction of double bonds into steroid ring A.
  JOURNAL   J. Am. Chem. Soc. 79 (1957) 2658-2659.
  ORGANISM  Pseudomonas testosteroni
REFERENCE   4  [PMID:13416214]
  AUTHORS   TOMKINS GM.
  TITLE     The enzymatic reduction of delta 4-3-ketosteroids.
  JOURNAL   J. Biol. Chem. 225 (1957) 13-24.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:2278855]
  AUTHORS   Sugimoto Y, Yoshida M, Tamaoki B.
  TITLE     Purification of 5 beta-reductase from hepatic cytosol fraction of
            chicken.
  JOURNAL   J. Steroid. Biochem. Mol. Biol. 37 (1990) 717-24.
  ORGANISM  chicken [GN:gga]
REFERENCE   6  [PMID:3828348]
  AUTHORS   Furuebisu M, Deguchi S, Okuda K.
  TITLE     Identification of cortisone 5 beta-reductase as delta
            4-3-ketosteroid 5 beta-reductase.
  JOURNAL   Biochim. Biophys. Acta. 912 (1987) 110-4.
  ORGANISM  rat [GN:rno]
REFERENCE   7  [PMID:6736016]
  AUTHORS   Okuda A, Okuda K.
  TITLE     Purification and characterization of delta 4-3-ketosteroid 5
            beta-reductase.
  JOURNAL   J. Biol. Chem. 259 (1984) 7519-24.
  ORGANISM  rat [GN:rno]
REFERENCE   8  [PMID:11342103]
  AUTHORS   Charbonneau A, The VL.
  TITLE     Genomic organization of a human 5beta-reductase and its pseudogene
            and substrate selectivity of the expressed enzyme.
  JOURNAL   Biochim. Biophys. Acta. 1517 (2001) 228-35.
  ORGANISM  rat [GN:rno]
REFERENCE   9  [PMID:7508385]
  AUTHORS   Kondo KH, Kai MH, Setoguchi Y, Eggertsen G, Sjoblom P, Setoguchi T,
            Okuda KI, Bjorkhem I.
  TITLE     Cloning and expression of cDNA of human delta 4-3-oxosteroid 5
            beta-reductase and substrate specificity of the expressed enzyme.
  JOURNAL   Eur. J. Biochem. 219 (1994) 357-63.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00120  Bile acid biosynthesis
            PATH: map00140  C21-Steroid hormone metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.3
            ExPASy - ENZYME nomenclature database: 1.3.1.3
            ExplorEnz - The Enzyme Database: 1.3.1.3
            ERGO genome analysis and discovery system: 1.3.1.3
            BRENDA, the Enzyme Database: 1.3.1.3
            CAS: 9029-08-7
///
ENTRY       EC 1.3.1.4                  Enzyme
NAME        cortisone alpha-reductase;
            cortisone Delta4-5alpha-reductase;
            microsomal steroid reductase (5alpha);
            Delta4-3-ketosteroid reductase (5alpha);
            Delta4-3-oxosteroid-5alpha-reductase;
            NADPH:Delta4-3-oxosteroid-5alpha-oxidoreductase;
            Delta4-5alpha-reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4,5alpha-dihydrocortisone:NADP+ Delta4-oxidoreductase
REACTION    4,5alpha-dihydrocortisone + NADP+ = cortisone + NADPH + H+
            [RN:R02892]
ALL_REAC    R02892
SUBSTRATE   4,5alpha-dihydrocortisone [CPD:C03588];
            NADP+ [CPD:C00006]
PRODUCT     cortisone [CPD:C00762];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   McGuire, J.S., Hollis, V.W. and Tomkins, G.M.
  TITLE     Some characteristics of the microsomal steroid reductases (5alpha)
            of rat liver.
  JOURNAL   J. Biol. Chem. 235 (1960) 3112-3117.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.4
            ExPASy - ENZYME nomenclature database: 1.3.1.4
            ExplorEnz - The Enzyme Database: 1.3.1.4
            ERGO genome analysis and discovery system: 1.3.1.4
            BRENDA, the Enzyme Database: 1.3.1.4
            CAS: 9029-09-8
///
ENTRY       EC 1.3.1.5                  Enzyme
NAME        cucurbitacin Delta23-reductase;
            NAD(P)H: cucurbitacin B Delta23-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     23,24-dihydrocucurbitacin:NAD(P)+ Delta23-oxidoreductase
REACTION    23,24-dihydrocucurbitacin + NAD(P)+ = cucurbitacin + NAD(P)H + H+
            [RN:R03763 R03764]
ALL_REAC    R03763 R03764
SUBSTRATE   23,24-dihydrocucurbitacin [CPD:C03578];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     cucurbitacin [CPD:C01901];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    Manganese [CPD:C00034]
COMMENT     Requires Mn2+. Fe2+ or Zn2+ can replace Mn2+ to some extent.
REFERENCE   1  [PMID:4384331]
  AUTHORS   Schabort JC, Potgieter DJ.
  TITLE     Cucurbitacin B delta 23-reductase from Cucurbita maxima. II.
            Cofactor requirements, enzyme kinetics, substrate specificity and
            other characteristics.
  JOURNAL   Biochim. Biophys. Acta. 151 (1968) 47-53.
  ORGANISM  Cucurbita maxima
REFERENCE   2  [PMID:5640163]
  AUTHORS   Schabort JC, Potgieter DJ, de Villiers V.
  TITLE     Cucurbitacin B delta 23-reductase from Cucurbita maxima. I. Assay
            methods, isolation and purification.
  JOURNAL   Biochim. Biophys. Acta. 151 (1968) 33-46.
  ORGANISM  Cucurbita maxima
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.5
            ExPASy - ENZYME nomenclature database: 1.3.1.5
            ExplorEnz - The Enzyme Database: 1.3.1.5
            ERGO genome analysis and discovery system: 1.3.1.5
            BRENDA, the Enzyme Database: 1.3.1.5
            CAS: 37256-38-5
///
ENTRY       EC 1.3.1.6                  Enzyme
NAME        fumarate reductase (NADH);
            NADH-fumarate reductase;
            NADH-dependent fumarate reductase;
            fumarate reductase (NADH)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     succinate:NAD+ oxidoreductase
REACTION    succinate + NAD+ = fumarate + NADH + H+ [RN:R00402]
ALL_REAC    R00402
SUBSTRATE   succinate [CPD:C00042];
            NAD+ [CPD:C00003]
PRODUCT     fumarate [CPD:C00122];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Hopgood, M.F. and Walker, D.J.
  TITLE     Succinic acid production by rumen bacteria. III. Enzymic studies on
            the formation of succinate by Ruminococcus flavefaciens.
  JOURNAL   Aust. J. Biol. Sci. 22 (1969) 1413-1424.
  ORGANISM  Ruminococcus flavefaciens
GENES       TBR: Tb927.5.930
            CVI: CV_3366(frdD) CV_3367(frdC) CV_3368(frdB) CV_3369(frdA)
            LDB: Ldb1095 Ldb1112
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.6
            ExPASy - ENZYME nomenclature database: 1.3.1.6
            ExplorEnz - The Enzyme Database: 1.3.1.6
            ERGO genome analysis and discovery system: 1.3.1.6
            BRENDA, the Enzyme Database: 1.3.1.6
            CAS: 9076-99-7
///
ENTRY       EC 1.3.1.7                  Enzyme
NAME        meso-tartrate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     meso-tartrate:NAD+ oxidoreductase
REACTION    meso-tartrate + NAD+ = dihydroxyfumarate + NADH + H+ [RN:R02544]
ALL_REAC    R02544
SUBSTRATE   meso-tartrate [CPD:C00552];
            NAD+ [CPD:C00003]
PRODUCT     dihydroxyfumarate [CPD:C00975];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Kohn, L.D. and Jakoby, W.B.
  TITLE     L- and mesotartaric acid dehydrogenase (crystalline).
  JOURNAL   Methods Enzymol. 9 (1966) 236-240.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.7
            ExPASy - ENZYME nomenclature database: 1.3.1.7
            ExplorEnz - The Enzyme Database: 1.3.1.7
            ERGO genome analysis and discovery system: 1.3.1.7
            BRENDA, the Enzyme Database: 1.3.1.7
            CAS: 37251-06-2
///
ENTRY       EC 1.3.1.8                  Enzyme
NAME        acyl-CoA dehydrogenase (NADP+);
            2-enoyl-CoA reductase;
            dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide
            phosphate);
            enoyl coenzyme A reductase;
            crotonyl coenzyme A reductase;
            crotonyl-CoA reductase;
            acyl-CoA dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     acyl-CoA:NADP+ 2-oxidoreductase
REACTION    acyl-CoA + NADP+ = 2,3-dehydroacyl-CoA + NADPH + H+ [RN:R00385]
ALL_REAC    R00385
SUBSTRATE   acyl-CoA [CPD:C00040];
            NADP+ [CPD:C00006]
PRODUCT     2,3-dehydroacyl-CoA [CPD:C00605];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The liver enzyme acts on enoyl-CoA derivatives of carbon chain
            length 4 to 16, with optimum activity on 2-hexenoyl-CoA. In
            Escherichia coli, cis-specific and trans-specific enzymes exist [EC
            1.3.1.37 cis-2-enoyl-CoA reductase (NADPH) and EC 1.3.1.38
            trans-2-enoyl-CoA reductase (NADPH)].
REFERENCE   1  [PMID:6749495]
  AUTHORS   Dommes V, Luster W, Cvetanovic M, Kunau WH.
  TITLE     Purification by affinity chromatography of 2,4-dienoyl-CoA
            reductases from bovine liver and Escherichia coli.
  JOURNAL   Eur. J. Biochem. 125 (1982) 335-41.
  ORGANISM  cow [GN:bta], Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4387390]
  AUTHORS   Seubert W, Lamberts I, Kramer R, Ohly B.
  TITLE     On the mechanism of malonyl-CoA-independent fatty acid synthesis. I.
            The mechanism of elongation of long-chain fatty acids by acetyl-CoA.
  JOURNAL   Biochim. Biophys. Acta. 164 (1968) 498-517.
  ORGANISM  cow [GN:bta]
GENES       BPU: BPUM_0635 BPUM_3370 BPUM_3371
STRUCTURES  PDB: 1YXM  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.8
            ExPASy - ENZYME nomenclature database: 1.3.1.8
            ExplorEnz - The Enzyme Database: 1.3.1.8
            ERGO genome analysis and discovery system: 1.3.1.8
            BRENDA, the Enzyme Database: 1.3.1.8
            CAS: 37251-07-3
///
ENTRY       EC 1.3.1.9                  Enzyme
NAME        enoyl-[acyl-carrier-protein] reductase (NADH);
            enoyl-[acyl carrier protein] reductase;
            enoyl-ACP reductase;
            NADH-enoyl acyl carrier protein reductase;
            NADH-specific enoyl-ACP reductase;
            enoyl-[acyl-carrier-protein] reductase (NADH)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     acyl-[acyl-carrier-protein]:NAD+ oxidoreductase
REACTION    acyl-[acyl-carrier-protein] + NAD+ =
            trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH + H+ [RN:R01403]
ALL_REAC    R01403 > R04724 R04955 R04958 R04961 R04966 R04969;
            (other) R04429
SUBSTRATE   acyl-[acyl-carrier-protein];
            NAD+ [CPD:C00003]
PRODUCT     trans-2,3-dehydroacyl-[acyl-carrier-protein];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Catalyses the reduction of enoyl-acyl-[acyl-carrier-protein]
            derivatives of carbon chain length from 4 to 16.
REFERENCE   1  [PMID:6756317]
  AUTHORS   Shimakata T, Stumpf PK.
  TITLE     Purification and characterizations of
            beta-Ketoacyl-[acyl-carrier-protein] reductase,
            beta-hydroxyacyl-[acylcarrier-protein] dehydrase, and
            enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea
            leaves.
  JOURNAL   Arch. Biochem. Biophys. 218 (1982) 77-91.
  ORGANISM  spinach
REFERENCE   2  [PMID:4384650]
  AUTHORS   Weeks G, Wakil SJ.
  TITLE     Studies on the mechanism of fatty acid synthesis. 18. Preparation
            and general properties of the enoyl acyl carrier protein reductases
            from Escherichia coli.
  JOURNAL   J. Biol. Chem. 243 (1968) 1180-9.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00061  Fatty acid biosynthesis
ORTHOLOGY   KO: K00208  enoyl-[acyl-carrier protein] reductase (NADH)
GENES       OSA: 4345286
            CME: CMT381C
            SCE: YKL182W(FAS1)
            AGO: AGOS_AER085C
            CGR: CAGL0D00528g
            SPO: SPAC926.09c(fas1)
            AFM: AFUA_5G09600
            CNE: CNE04370
            PFA: PFF0730c
            ECO: b1288(fabI)
            ECJ: JW1281(fabI)
            ECE: Z2512(fabI)
            ECS: ECs1861
            ECC: c1759(fabI)
            ECI: UTI89_C1561(fabI)
            ECP: ECP_1342
            ECV: APECO1_447(fabI)
            ECW: EcE24377A_1494(fabI)
            ECX: EcHS_A1401(fabI)
            STY: STY1352(fabI)
            STT: t1613(fabI)
            SPT: SPA1177(fabI)
            SEC: SC1694(fabI)
            STM: STM1700(fabI)
            SFL: SF1293(fabI)
            SFX: S1375(fabI)
            SFV: SFV_1302(fabI)
            SSN: SSON_1852(fabI)
            SBO: SBO_1774(fabI)
            SDY: SDY_1368(fabI)
            ECA: ECA1972(fabI)
            PLU: plu2592(fabI)
            BUC: BU265(fabI)
            BAS: BUsg255(fabI)
            BAB: bbp246(fabI)
            BCC: BCc_167(fabI)
            WBR: WGLp362(fabI)
            SGL: SG1513
            ENT: Ent638_2178
            KPN: KPN_01284(fabI)
            BFL: Bfl424(fabI)
            BPN: BPEN_436(fabI)
            HIN: HI1734(fabI)
            HIT: NTHI2042(fabI)
            HDU: HD1266(fabI)
            HSO: HS_0662(fabI)
            PMU: PM0182(fabI)
            MSU: MS1467(fabI)
            APL: APL_0755(fabI)
            PAE: PA1806(fabI)
            PAU: PA14_41170(fabI)
            PAP: PSPA7_3490
            PST: PSPTO_3721(fabI)
            PSB: Psyr_1754
            PSP: PSPPH_1703(fabI)
            PFL: PFL_3306(fabI) PFL_3411(fabK)
            PFO: Pfl_2177
            PMY: Pmen_2056
            PAR: Psyc_1045(fabI)
            PCR: Pcryo_1424
            ACI: ACIAD3116(fabI)
            ACB: A1S_0534
            MAQ: Maqu_1542
            LPN: lpg1854(fabI)
            LPF: lpl1820(fabI)
            LPP: lpp1821(fabI)
            MCA: MCA1263(fabI)
            FTU: FTT0782(fabI)
            FTF: FTF0782(fabI)
            FTW: FTW_0579(fabI)
            FTL: FTL_1442
            FTH: FTH_1403(fabI)
            FTA: FTA_1529
            FTN: FTN_1228(fabL)
            TCX: Tcr_1181
            NOC: Noc_1769
            AEH: Mlg_2277 Mlg_2379
            HHA: Hhal_0598
            HCH: HCH_02517
            ABO: ABO_1215(fabI)
            DNO: DNO_0074
            BCI: BCI_0296(fabI)
            VOK: COSY_0600(fabI)
            NME: NMB0336
            NMA: NMA2152(fabI)
            NMC: NMC1834(fabI)
            NGO: NGO1666
            CVI: CV_1583(fabI) CV_3743
            RSO: RSc1172(fabI)
            REU: Reut_A0628 Reut_A2130
            REH: H16_A2410(fabI1) H16_B1629(fabI2)
            RME: Rmet_0565 Rmet_2147
            BMA: BMA1608(fabI) BMAA1403
            BMV: BMASAVP1_0520 BMASAVP1_A2111(fabI)
            BML: BMA10299_0128 BMA10299_A3203(fabI)
            BMN: BMA10247_1384(fabI) BMA10247_A1486
            BXE: Bxe_A1635 Bxe_B0355 Bxe_C0050
            BUR: Bcep18194_B2636
            BCN: Bcen_3497
            BCH: Bcen2424_4869
            BPS: BPSL2204(fabI) BPSS0721
            BPM: BURPS1710b_2636(fabI) BURPS1710b_A2297(fabI-1)
            BPL: BURPS1106A_2548(fabI)
            BPD: BURPS668_2494(fabI)
            BTE: BTH_I1977 BTH_II1698
            PNU: Pnuc_1238
            BPE: BP1002(fabI) BP3215(fabI)
            BPA: BPP1167(fabI) BPP3838(fabI)
            BBR: BB1383(fabI) BB4282(fabI)
            RFR: Rfer_2127
            POL: Bpro_2419
            PNA: Pnap_2018
            AAV: Aave_3255
            AJS: Ajs_1809
            VEI: Veis_3815
            MPT: Mpe_A1924
            HAR: HEAR2327(fabI)
            MMS: mma_1203(fabI)
            NEU: NE2205
            NET: Neut_0663
            NMU: Nmul_A2335
            EBA: ebA6664(fabI)
            AZO: azo1569(fabI1) azo2130(fabI2)
            DAR: Daro_0978 Daro_1935
            TBD: Tbd_1672
            HPY: HP0195
            HPJ: jhp0181(fabI)
            HPA: HPAG1_0189
            HHE: HH1313
            HAC: Hac_0380(fabI)
            WSU: WS0423(fabI)
            TDN: Tmden_1751
            CJE: Cj1400c(fabI)
            CJR: CJE1587(fabI)
            CJJ: CJJ81176_1399(fabI)
            CJU: C8J_1314(fabI)
            CJD: JJD26997_1734(fabI)
            CFF: CFF8240_1426
            CHA: CHAB381_0780
            ABU: Abu_2135(fabI)
            NIS: NIS_1489(fabI)
            SUN: SUN_0717(fabI)
            GSU: GSU1008(fabI)
            GME: Gmet_2558
            PCA: Pcar_2044
            DVU: DVU0794(fabI)
            DDE: Dde_1006
            LIP: LI0350(fabI)
            DPS: DP1027
            MXA: MXAN_6034
            RPR: RP365
            RTY: RT0353(fabI)
            RCO: RC0494(fabI)
            RFE: RF_0575(fabI)
            RBE: RBE_1255(fabI)
            OTS: OTBS_0706(fabI)
            WOL: WD0085(fabI) WD1170(fabK)
            WBM: Wbm0470 Wbm0753(fabK)
            AMA: AM428(fabI)
            APH: APH_0473(fabI) APH_1048(fabK)
            ERU: Erum1560 Erum2860(fabI)
            ERW: ERWE_CDS_01520 ERWE_CDS_02920(fabI)
            ERG: ERGA_CDS_01480 ERGA_CDS_02870(fabI)
            ECN: Ecaj_0152 Ecaj_0269
            ECH: ECH_0811(fabI) ECH_0974(fabK)
            NSE: NSE_0043(fabI) NSE_0544(fabK)
            PUB: SAR11_0395(fabI)
            MLO: mll5565 mlr7458
            MES: Meso_0727 Meso_3937
            SME: SMc00005(fabI1) SMc00326(fabI2)
            ATU: Atu0149(fabI) Atu0757(fabI)
            ATC: AGR_C_1374 AGR_C_242
            RET: RHE_CH00109(fabI1) RHE_CH00938(fabI2)
            RLE: RL0118(fabI) RL1011(fabI)
            BME: BMEI1512 BMEI1958
            BMF: BAB1_0447(fabI-1) BAB1_2172(fabI-2)
            BMS: BR0420(fabI-1) BR2171(fabI-2)
            BMB: BruAb1_0443(fabI-1) BruAb1_2144(fabI-2)
            BOV: BOV_0428(fabI-1) BOV_2083(fabI-2)
            BJA: blr0771(fabI) blr2629(fabI) blr3459(fabI)
            BRA: BRADO0061(fabI) BRADO2151(fabI) BRADO6363(fabI)
            BBT: BBta_0066(fabI) BBta_2468(fabI) BBta_2653(fabI)
            RPA: RPA0427 RPA1199 RPA4568
            RPB: RPB_0611 RPB_1025 RPB_1211
            RPC: RPC_0347 RPC_1140 RPC_1999
            RPD: RPD_0222 RPD_1126 RPD_1312
            RPE: RPE_0255 RPE_3164 RPE_4591
            NWI: Nwi_0032
            NHA: Nham_0040 Nham_0866
            BHE: BH01270(fabI1) BH04310(fabI2)
            BQU: BQ01200(fabI1) BQ03500(fabI2)
            CCR: CC_3717
            SIL: SPO0113(fabI-1) SPO2142(fabI-2) SPOA0439(fabI-3)
            SIT: TM1040_0180 TM1040_1147
            RSP: RSP_1256 RSP_2344(fabI1) RSP_3176(fabI)
            JAN: Jann_1657 Jann_2476
            RDE: RD1_3199(fabI-2) RD1_3925(fabI)
            MMR: Mmar10_3058
            HNE: HNE_2786 HNE_3287(fabK) HNE_3436
            ZMO: ZMO1692(fabI)
            NAR: Saro_0051
            ELI: ELI_06735
            GOX: GOX0036 GOX1990
            GBE: GbCGDNIH1_0225 GbCGDNIH1_0601
            RRU: Rru_A2624 Rru_A3226
            MAG: amb1591 amb4226
            MGM: Mmc1_3620
            ABA: Acid345_3279
            BSU: BG13152(fabI)
            BHA: BH2843
            BAN: BA1232(fabI)
            BAR: GBAA1232(fabI)
            BAA: BA_1767
            BAT: BAS1139
            BCE: BC1216
            BCA: BCE_1339(fabI)
            BCZ: BCZK1113(fabI)
            BTK: BT9727_1119(fabI)
            BLI: BL05113(fabI)
            BLD: BLi01266(fabI)
            BCL: ABC1313(fabL) ABC2517(fabI)
            BAY: RBAM_008740(fabL) RBAM_011730(fabI)
            BPU: BPUM_0812(fabL) BPUM_1101(fabI)
            OIH: OB0223
            GKA: GK0834
            SAU: SA0869(fabI)
            SAV: SAV1011(fabI)
            SAM: MW0892(fabI)
            SAR: SAR0978(fabI)
            SAS: SAS0880
            SAC: SACOL1016(fabI)
            SAB: SAB0877(fabI)
            SAA: SAUSA300_0912
            SAO: SAOUHSC_00947
            SEP: SE0712
            SER: SERP0601(fabI)
            SHA: SH1947(fabI)
            SSP: SSP1774
            LMO: lmo0970
            LMF: LMOf2365_0990(fabI)
            LIN: lin0969
            LWE: lwe0952
            LLA: L161132(fabI)
            LLC: LACR_0587
            LLM: llmg_0539(fabI)
            SPZ: M5005_Spy_1492(fabK)
            SPH: MGAS10270_Spy1560(fabK)
            SPI: MGAS10750_Spy1551(fabK) MGAS10750_Spy1552
            SPJ: MGAS2096_Spy1520(fabK)
            SPK: MGAS9429_Spy1494(fabK)
            SPF: SpyM50353(fabK)
            SPA: M6_Spy1486
            SPB: M28_Spy1481(fabK)
            SAK: SAK_0420(fabK)
            SSA: SSA_1938(fabK)
            LPL: lp_1681(fabI)
            LSA: LSA0823(fabI)
            LSL: LSL_0461(fabI)
            LDB: Ldb0910(fabI)
            LBU: LBUL_0828
            LBR: LVIS_0925
            EFA: EF0282(fabI)
            STH: STH2927
            CTC: CTC00128
            CKL: CKL_0104(fabI)
            CHY: CHY_1449(fabK)
            MTU: Rv1484(inhA)
            MTC: MT1531(inhA)
            MBO: Mb1520(inhA)
            MBB: BCG_1546(inhA)
            MLE: ML1806(inhA)
            MPA: MAP1210(inhA)
            MAV: MAV_3294
            MSM: MSMEG_3151
            MVA: Mvan_2753
            MGI: Mflv_3657
            MMC: Mmcs_2457
            MKM: Mkms_2502
            MJL: Mjls_2494
            NFA: nfa34760(inhA)
            RHA: RHA1_ro07214
            SCO: SCO1814(inhA)
            SMA: SAV2295(fabI2) SAV6463(fabI1)
            PAC: PPA1532
            TFU: Tfu_1842
            FRA: Francci3_1894
            FAL: FRAAL4522
            SEN: SACE_3786(inhA)
            RXY: Rxyl_0853
            FNU: FN0174
            RBA: RB10790(fabI) RB8125(fabI)
            CTR: CT104(fabI)
            CTA: CTA_0110(fabI)
            CMU: TC0380
            CPN: CPn0406(fabI)
            CPA: CP0349
            CPJ: CPj0406(fabI)
            CPT: CpB0421
            CCA: CCA00388(fabI)
            CAB: CAB375
            CFE: CF0620(fabI)
            PCU: pc1152(fabI)
            SYN: slr1051(envM)
            SYW: SYNW0225(fabI)
            SYC: syc1378_d(envM)
            SYF: Synpcc7942_0126
            SYD: Syncc9605_0219
            SYE: Syncc9902_0246
            SYG: sync_0258
            SYR: SynRCC307_2289(fabI)
            SYX: SynWH7803_0268(fabI)
            CYA: CYA_1682
            CYB: CYB_1160
            TEL: tll1693
            GVI: glr4188
            ANA: all4391
            AVA: Ava_3284
            PMA: Pro0314(fabI)
            PMM: PMM0282(fabI)
            PMT: PMT1881(fabI)
            PMN: PMN2A_1648
            PMI: PMT9312_0284
            PMB: A9601_03051(fabI)
            PMC: P9515_03151(fabI)
            PMF: P9303_25131(fabI)
            PMG: P9301_03061(fabI)
            PME: NATL1_03621(fabI)
            TER: Tery_2024
            BTH: BT_4188
            BFR: BF0972
            BFS: BF0894
            SRU: SRU_0532(fabI)
            CHU: CHU_3011(fabI)
            GFO: GFO_0653(fabI) GFO_1609(fabI)
            CTE: CT0350(fabI)
            CCH: Cag_1411
            PVI: Cvib_0506
            PLT: Plut_0458
            DET: DET1272
            DEH: cbdb_A1199(fabI)
            DEB: DehaBAV1_1083
            DRA: DR_1967
            DGE: Dgeo_0260
            TTH: TTC1678(fabL)
            TTJ: TTHA0304
            AAE: aq_1552(fabI)
STRUCTURES  PDB: 1BVR  1C14  1CWU  1D7O  1D8A  1DFG  1DFH  1DFI  1ENO  1ENP  
                 1I2Z  1I30  1LX6  1LXC  1MFP  1NHG  1NHW  1NNU  1P44  1P45  
                 1QG6  1QSG  1UH5  1V35  1VRW  1ZID  1ZSN  1ZW1  1ZXB  1ZXL  
                 2AQ8  2AQH  2AQI  2AQK  2B35  2B36  2B37  2FHS  2FOI  2H7I  
                 2H7L  2H7M  2H7N  2H7P  2H9I  2IDZ  2IE0  2IEB  2IED  2NSD  
                 2NTJ  2NV6  2O2S  2O2Y  2O50  2OL4  2OOS  2OP0  2OP1  2P91  
                 2PD3  2PD4  2PFF  2PTG  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.9
            ExPASy - ENZYME nomenclature database: 1.3.1.9
            ExplorEnz - The Enzyme Database: 1.3.1.9
            ERGO genome analysis and discovery system: 1.3.1.9
            BRENDA, the Enzyme Database: 1.3.1.9
            CAS: 37251-08-4
///
ENTRY       EC 1.3.1.10                 Enzyme
NAME        enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific);
            acyl-ACP dehydrogenase;
            reductase, enoyl-[acyl carrier protein] (reduced nicotinamide
            adenine dinucleotide phosphate);
            NADPH 2-enoyl Co A reductase;
            enoyl acyl-carrier-protein reductase;
            enoyl-ACP reductase;
            enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (B-specific)
REACTION    acyl-[acyl-carrier-protein] + NADP+ =
            trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH + H+
            [RN:R01404]
ALL_REAC    R01404 > R04725 R04956 R04959 R04962 R04967 R04970;
            (other) R04430
SUBSTRATE   acyl-[acyl-carrier-protein];
            NADP+ [CPD:C00006]
PRODUCT     trans-2,3-dehydroacyl-[acyl-carrier-protein];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Catalyses the reduction of enoyl-acyl-[acyl-carrier-protein]
            derivatives of carbon chain length from 4 to 16. The yeast and
            Escherichia coli enzymes are B-specific with respect to NADP+ (cf.
            EC 1.3.1.19 cis-1,2-dihydrobenzene-1,2-diol dehydrogenase).
REFERENCE   1  [PMID:6990992]
  AUTHORS   Saito K, Kawaguchi A, Okuda S, Seyama Y, Yamakawa T.
  TITLE     Incorporation of hydrogen atoms from deuterated water and
            stereospecifically deuterium-labeled nicotin amide nucleotides into
            fatty acids with the Escherichia coli fatty acid synthetase system.
  JOURNAL   Biochim. Biophys. Acta. 618 (1980) 202-13.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:338601]
  AUTHORS   Seyama Y, Kasama T, Yamakawa T, Kawaguchi A, Saito K.
  TITLE     Origin of hydrogen atoms in the fatty acids synthesized with yeast
            fatty acid synthetase.
  JOURNAL   J. Biochem. (Tokyo). 82 (1977) 1325-9.
  ORGANISM  Brevibacterium ammoniagenes, Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:4384650]
  AUTHORS   Weeks G, Wakil SJ.
  TITLE     Studies on the mechanism of fatty acid synthesis. 18. Preparation
            and general properties of the enoyl acyl carrier protein reductases
            from Escherichia coli.
  JOURNAL   J. Biol. Chem. 243 (1968) 1180-9.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00061  Fatty acid biosynthesis
ORTHOLOGY   KO: K00209  enoyl-[acyl-carrier-protein] reductase (NADPH2,
                        B-specific)
GENES       HSA: 2194(FASN)
            MMU: 14104(Fasn)
            RNO: 50671(Fasn)
            BTA: 281152(FASN)
            GGA: 396061(FASN)
            CEL: F32H2.5(fasn-1)
            SCE: YBR026C(ETR1)
            RAK: A1C_02720
            RBO: A1I_01015
            RRI: A1G_02800
            CGB: cg0957(fas-IB) cg2743(fas-IA)
            FAL: FRAAL4071
            PMB: A9601_03051(fabI)
            PMC: P9515_03151(fabI)
            PMF: P9303_25131(fabI)
            PMG: P9301_03061(fabI)
            PMH: P9215_03071(fabI)
            PME: NATL1_03621(fabI)
STRUCTURES  PDB: 1ULU  2YW9  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.10
            ExPASy - ENZYME nomenclature database: 1.3.1.10
            ExplorEnz - The Enzyme Database: 1.3.1.10
            ERGO genome analysis and discovery system: 1.3.1.10
            BRENDA, the Enzyme Database: 1.3.1.10
            CAS: 37251-09-5
///
ENTRY       EC 1.3.1.11                 Enzyme
NAME        2-coumarate reductase;
            melilotate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-(2-hydroxyphenyl)propanoate:NAD+ oxidoreductase
REACTION    3-(2-hydroxyphenyl)propanoate + NAD+ = 2-coumarate + NADH + H+
            [RN:R03709]
ALL_REAC    R03709
SUBSTRATE   3-(2-hydroxyphenyl)propanoate [CPD:C01198];
            NAD+ [CPD:C00003]
PRODUCT     2-coumarate [CPD:C03549];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Levy, C.C. and Weinstein, G.D.
  TITLE     The metabolism of coumarin by a microorganism. II. The reduction of
            o-coumaric acid to melilotic acid.
  JOURNAL   Biochemistry 3 (1964) 1944-1947.
  ORGANISM  Arthrobacter sp.
PATHWAY     PATH: map00360  Phenylalanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.11
            ExPASy - ENZYME nomenclature database: 1.3.1.11
            ExplorEnz - The Enzyme Database: 1.3.1.11
            ERGO genome analysis and discovery system: 1.3.1.11
            BRENDA, the Enzyme Database: 1.3.1.11
            CAS: 37251-10-8
///
ENTRY       EC 1.3.1.12                 Enzyme
NAME        prephenate dehydrogenase;
            hydroxyphenylpyruvate synthase;
            chorismate mutase---prephenate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     prephenate:NAD+ oxidoreductase (decarboxylating)
REACTION    prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH [RN:R01728]
ALL_REAC    R01728
SUBSTRATE   prephenate [CPD:C00254];
            NAD+ [CPD:C00003]
PRODUCT     4-hydroxyphenylpyruvate [CPD:C01179];
            CO2 [CPD:C00011];
            NADH [CPD:C00004]
COMMENT     This enzyme in the enteric bacteria also possesses chorismate mutase
            activity (EC 5.4.99.5 chorismate mutase) and converts chorismate
            into prephenate.
REFERENCE   1  [PMID:5456988]
  AUTHORS   Koch GL, Shaw DC, Gibson F.
  TITLE     Tyrosine biosynthesis in Aerobacter aerogenes. Purification and
            properties of chorismate mutase-prephenate dehydrogenase.
  JOURNAL   Biochim. Biophys. Acta. 212 (1970) 375-86.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
            PATH: map00401  Novobiocin biosynthesis
ORTHOLOGY   KO: K00210  prephenate dehydrogenase
            KO: K04517  prephenate dehydrogenase
GENES       ECO: b2600(tyrA)
            ECJ: JW2581(tyrA)
            ECE: Z3892(tyrA)
            ECS: ECs3463
            ECC: c3121(tyrA)
            ECI: UTI89_C2933(tyrA)
            ECP: ECP_2601
            ECV: APECO1_3933(pheA)
            ECW: EcE24377A_2884(tyrA)
            ECX: EcHS_A2757(tyrA)
            STY: STY2856(tyrA)
            STT: t2624(tyrA)
            SPT: SPA2528(tyrA)
            SEC: SC2671(tyrA)
            STM: STM2669(tyrA)
            YPE: YPO3285(tyrA)
            YPK: y0904(tyrA)
            YPM: YP_0399(tyrA)
            YPA: YPA_2860
            YPN: YPN_0814
            YPS: YPTB0842(tyrA)
            YPI: YpsIP31758_3219(tyrA)
            SFL: SF2660(tyrA)
            SFX: S2837(tyrA)
            SFV: SFV_2871(tyrA)
            SSN: SSON_2751(tyrA)
            SBO: SBO_2638(tyrA)
            SDY: SDY_2766(tyrA)
            ECA: ECA3351(tyrA)
            PLU: plu1263(tyrA)
            SGL: SG0579
            BFL: Bfl178(tyrA)
            BPN: BPEN_184(tyrA)
            HIN: HI1290(tyrA)
            HIT: NTHI1833(tyrA)
            HIP: CGSHiEE_04195(tyrA)
            HIQ: CGSHiGG_01505(tyrA)
            HSO: HS_0671(tyrA)
            PMU: PM0664(tyrA)
            MSU: MS1102(tyrA)
            APL: APL_0184(tyrA)
            XFA: XF2338
            XFT: PD1368(tyrA)
            XCC: XCC1477(tyrA)
            XCB: XC_2760
            XCV: XCV1567
            XAC: XAC1525(tyrA)
            XOO: XOO2034(tyrA)
            XOM: XOO_1916(XOO1916)
            VCH: VC0696
            VVU: VV1_0494
            VVY: VV0702
            VPA: VP0547
            VFI: VF0554
            PPR: PBPRA3025
            PAE: PA3164
            PPU: PP_1770
            PST: PSPTO_1748
            PSB: Psyr_3644
            PSP: PSPPH_3664
            PFL: PFL_4310
            PFO: Pfl_4074
            PEN: PSEEN1490
            PAR: Psyc_1184
            PCR: Pcryo_1206
            ACI: ACIAD2222
            SON: SO_1362(tyrA)
            SDN: Sden_2749
            SFR: Sfri_2915
            SHE: Shewmr4_2833
            SHM: Shewmr7_2915
            SHN: Shewana3_3012
            ILO: IL1721(tyrA)
            CPS: CPS_3953(tyrA)
            PHA: PSHAa0949(tyrA)
            PAT: Patl_1588
            MAQ: Maqu_1025
            CBD: COXBU7E912_1063
            MCA: MCA1416(tyrA)
            FTL: FTL_0048
            FTH: FTH_0048(tyrA)
            FTA: FTA_0055
            FTN: FTN_0055(tyrA)
            TCX: Tcr_1195
            NOC: Noc_0176
            AEH: Mlg_0928
            HHA: Hhal_0566
            CSA: Csal_2165
            ABO: ABO_1747(tyrA)
            MMW: Mmwyl1_2857
            AHA: AHA_1655(tyrA)
            RMA: Rmag_0624
            VOK: COSY_0577
            NME: NMB0440
            NMA: NMA2045
            NGO: NGO1515
            CVI: CV_3407
            RSO: RSc0906(tyrA)
            REU: Reut_A2573
            REH: H16_A0794(tyrA)
            RME: Rmet_0718
            BMA: BMA0430
            BMV: BMASAVP1_A2574
            BML: BMA10299_A0949
            BMN: BMA10247_0199
            BXE: Bxe_A0979
            BVI: Bcep1808_0965
            BUR: Bcep18194_A4157
            BCN: Bcen_0565
            BCH: Bcen2424_1044
            BAM: Bamb_0920
            BPS: BPSL2517(aroA)
            BPM: BURPS1710b_2996(aroA)
            BPL: BURPS1106A_2947(aroA)
            BPD: BURPS668_2884(aroA)
            BTE: BTH_I1636
            PNU: Pnuc_0497
            BPE: BP0947(tyrA)
            BPA: BPP3131(tyrA)
            BBR: BB3470(tyrA)
            RFR: Rfer_1568
            POL: Bpro_1791
            AAV: Aave_3283
            VEI: Veis_3122
            MPT: Mpe_A2242
            HAR: HEAR2577
            MMS: mma_2671(tyrA)
            NEU: NE0337(tyrA)
            NET: Neut_1568
            NMU: Nmul_A2195
            EBA: ebA905(tyrA)
            AZO: azo1070(tyrA)
            DAR: Daro_1234
            TBD: Tbd_0953
            MFA: Mfla_0930 Mfla_1074
            HPY: HP1380
            HPA: HPAG1_1326
            HHE: HH0993(tyrA)
            HAC: Hac_0058(tyrA)
            WSU: WS0348(tyrA)
            TDN: Tmden_0659
            CJE: Cj0130(tyrA)
            CJR: CJE0125(tyrA)
            CJJ: CJJ81176_0165(tyrA)
            CJU: C8J_0123(tyrA)
            CJD: JJD26997_0143(tyrA)
            CFF: CFF8240_1500
            CCV: CCV52592_2225
            CHA: CHAB381_1685
            CCO: CCC13826_0943
            ABU: Abu_1210(tyrA)
            NIS: NIS_0406
            SUN: SUN_1998
            GSU: GSU2607
            GME: Gmet_0863
            GUR: Gura_1463
            PCA: Pcar_1886
            PPD: Ppro_1346
            DVU: DVU0464
            DDE: Dde_3485
            ADE: Adeh_0183
            MXA: MXAN_5840
            SAT: SYN_01933
            PUB: SAR11_0215(tyrA)
            MLO: mll3535
            MES: Meso_3085
            PLA: Plav_1584
            SME: SMc00711(tyrC)
            SMD: Smed_2549
            ATU: Atu3611(tyrC)
            ATC: AGR_L_2429(tyrC)
            RET: RHE_CH03809(tyrC)
            RLE: RL4337(tyrC)
            BME: BMEI0079
            BMF: BAB1_1989
            BMS: BR1988(tyrC)
            BMB: BruAb1_1964(tyrC)
            BOV: BOV_1914(tyrC)
            OAN: Oant_0992
            BJA: bll1396(tyrC)
            BRA: BRADO6464(tyrC)
            BBT: BBta_1182(tyrC)
            RPA: RPA4440(tyrC)
            RPB: RPB_4255
            RPC: RPC_4284
            RPD: RPD_4102
            RPE: RPE_4343
            NWI: Nwi_0582
            NHA: Nham_0673
            BHE: BH16210(tyrC)
            BQU: BQ13130(tyrC)
            CCR: CC_2224
            SIL: SPO3176
            SIT: TM1040_2100
            RSP: RSP_6215
            RSH: Rsph17029_0960
            RSQ: Rsph17025_2212
            JAN: Jann_1035 Jann_3543
            RDE: RD1_3387(tyrC)
            PDE: Pden_1408
            MMR: Mmar10_0997
            HNE: HNE_3400
            NAR: Saro_0696
            SAL: Sala_2888
            SWI: Swit_3007
            ELI: ELI_11420
            GOX: GOX2251
            GBE: GbCGDNIH1_0139
            ACR: Acry_0440
            RRU: Rru_A0972 Rru_A3263
            MGM: Mmc1_0175
            ABA: Acid345_1162
            BSU: BG10293(tyrA)
            BHA: BH1666(tyrA)
            BAN: BA2954(tyrA)
            BAR: GBAA2954(tyrA)
            BAA: BA_3463
            BAT: BAS2745
            BCE: BC2939
            BCA: BCE_2995(tyrA)
            BCZ: BCZK2674(tyrA)
            BTK: BT9727_2695(tyrA)
            BLI: BL02768(tyrA)
            BLD: BLi02396(tyrA)
            BCL: ABC1902(tyrA)
            BAY: RBAM_020770(tyrA)
            BPU: BPUM_1992(tyrA)
            OIH: OB1781
            GKA: GK2197(tyrA)
            SAU: SA1197(tyrA)
            SAV: SAV1365(tyrA)
            SAM: MW1252(tyrA)
            SAR: SAR1378
            SAS: SAS1305
            SAC: SACOL1401(tyrA)
            SAB: SAB1220c
            SAA: SAUSA300_1260
            SAO: SAOUHSC_01364
            SEP: SE1047
            SER: SERP0936(tyrA)
            SHA: SH1544(tyrA)
            SSP: SSP1387
            LMO: lmo1924(tyrA)
            LMF: LMOf2365_1953(tyrA)
            LIN: lin2038(tyrA)
            LWE: lwe1950(tyrA)
            LLA: L0058(tyrA)
            LLC: LACR_1908
            LLM: llmg_1927(tyrA)
            SPN: SP_1373
            SPR: spr1231(tyrA)
            SPD: SPD_1207(tyrA)
            SMU: SMU.781
            STC: str0642(tyrA)
            STL: stu0642(tyrA)
            SSA: SSA_1466(tyrA)
            SGO: SGO_1371
            LPL: lp_2034(tyrA)
            EFA: EF1565
            STH: STH1418
            CAC: CAC0893
            CNO: NT01CX_0626
            CKL: CKL_0785(tyrA)
            AMT: Amet_0646
            CHY: CHY_0474(tyrA)
            DSY: DSY2263
            SWO: Swol_1349
            TTE: TTE1014(tyrA)
            MTA: Moth_1333
            MTU: Rv3754(tyrA)
            MTC: MT3861(tyrA)
            MBO: Mb3780(tyrA)
            MBB: BCG_3813(tyrA)
            MLE: ML2472
            MPA: MAP0277c(tyrA)
            MAV: MAV_0321
            MSM: MSMEG_6330
            MMC: Mmcs_4962
            CGL: NCgl0223(cgl0226)
            CGB: cg0279(tyrA)
            CEF: CE0195
            CDI: DIP0245
            CJK: jk2025(tyrA)
            NFA: nfa2360
            RHA: RHA1_ro04152(tyrA) RHA1_ro06105(tryA)
            SCO: SCO1761(2SCI34.14c) SCO3221(SCE8.14c)
            SMA: SAV6521(tyrA)
            TWH: TWT050(tyrA)
            TWS: TW060
            LXX: Lxx05720(tyrA)
            PAC: PPA1208
            TFU: Tfu_1208
            FRA: Francci3_1455 Francci3_2453
            FAL: FRAAL2252
            SEN: SACE_0231(tyrA)
            BLO: BL1382(tyrA)
            BAD: BAD_1066(tyrA)
            RBA: RB5392(tyrA)
            LIL: LA1257(tyrA)
            LIC: LIC12450(tyrA)
            LBJ: LBJ_0933(tyrA)
            LBL: LBL_2100(tyrA)
            SYN: slr2081(tyrA)
            SYW: SYNW2058
            SYC: syc0868_c(tyrA)
            SYF: Synpcc7942_0660
            SYD: Syncc9605_0385
            SYE: Syncc9902_1945
            SYG: sync_0447(tyrA)
            SYR: SynRCC307_2107(tyrA)
            SYX: SynWH7803_0443(tyrA)
            CYA: CYA_2300(tyrA)
            CYB: CYB_0624(tyrA)
            TEL: tll2435(tyrA)
            GVI: glr0406(tyrA)
            ANA: all0418 all1141
            AVA: Ava_4397
            PMA: Pro1719(tyrA)
            PMM: PMM1565
            PMT: PMT1724
            PMN: PMN2A_1136
            PMI: PMT9312_1657
            PMB: A9601_17721(tyrA)
            PMC: P9515_17521(tyrA)
            PMF: P9303_22941(tyrA)
            PMG: P9301_17561(tyrA)
            PME: NATL1_20101(tyrA)
            TER: Tery_2701
            BTH: BT_3933(tyrA)
            BFR: BF3945
            BFS: BF3718
            SRU: SRU_1616(tyrA)
            CHU: CHU_1274(pdh)
            GFO: GFO_0342(tyrA)
            CTE: CT0084(tyrA)
            CCH: Cag_0018
            PLT: Plut_2049
            DET: DET0460
            DEH: cbdb_A423
            DRA: DR_1122
            DGE: Dgeo_1040
            TTJ: TTHA0799
            AAE: aq_1755(tyrA)
            TMA: TM0344
            MJA: MJ0612
            MMP: MMP1514(tyrA)
            MAC: MA4595
            MBA: Mbar_A0924
            MMA: MM_1275
            MBU: Mbur_1997
            MHU: Mhun_1033
            MEM: Memar_1300
            MTH: MTH1640
            MST: Msp_1083
            MSI: Msm_0641
            MKA: MK0798(tyrA_2)
            HMA: rrnAC0512(tyrA)
            HWA: HQ3352A(tyrA)
            NPH: NP3358A(tyrA)
            PTO: PTO0836
            PFU: PF1703
            TKO: TK0259
            RCI: RCIX1314(tyrA)
STRUCTURES  PDB: 2G5C  2PV7  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.12
            ExPASy - ENZYME nomenclature database: 1.3.1.12
            ExplorEnz - The Enzyme Database: 1.3.1.12
            ERGO genome analysis and discovery system: 1.3.1.12
            BRENDA, the Enzyme Database: 1.3.1.12
            CAS: 9044-92-2
///
ENTRY       EC 1.3.1.13                 Enzyme
NAME        prephenate dehydrogenase (NADP+);
            prephenate dehydrogenase;
            prephenate (nicotinamide adenine dinucleotide phosphate)
            dehydrogenase;
            prephenate dehydrogenase (NADP)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     prephenate:NADP+ oxidoreductase (decarboxylating)
REACTION    prephenate + NADP+ = 4-hydroxyphenylpyruvate + CO2 + NADPH
            [RN:R01730]
ALL_REAC    R01730
SUBSTRATE   prephenate [CPD:C00254];
            NADP+ [CPD:C00006]
PRODUCT     4-hydroxyphenylpyruvate [CPD:C01179];
            CO2 [CPD:C00011];
            NADPH [CPD:C00005]
REFERENCE   1  [PMID:4379953]
  AUTHORS   Gamborg OL, Keeley FW.
  TITLE     Aromatic metabolism in plants. I. A study of the prephenate
            dehydrogenase from bean plants.
  JOURNAL   Biochim. Biophys. Acta. 115 (1966) 65-72.
  ORGANISM  Phaseolus vulgaris, Vicia faba, Phaseolus coccineus, Phaseolus
            aureus
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K00211  prephenate dehydrogenase (NADP+)
GENES       SCE: YBR166C(TYR1)
            AGO: AGOS_AGR219W
            PIC: PICST_52223(TYR1)
            CGR: CAGL0M06017g
            SPO: SPCC1494.04c
            ANI: AN5959.2
            AFM: AFUA_2G10450
            AOR: AO090011000595
            CNE: CNK03330
            UMA: UM04182.1
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.13
            ExPASy - ENZYME nomenclature database: 1.3.1.13
            ExplorEnz - The Enzyme Database: 1.3.1.13
            ERGO genome analysis and discovery system: 1.3.1.13
            BRENDA, the Enzyme Database: 1.3.1.13
            CAS: 37251-11-9
///
ENTRY       EC 1.3.1.14                 Enzyme
NAME        orotate reductase (NADH);
            orotate reductase (NADH)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-dihydroorotate:NAD+ oxidoreductase
REACTION    (S)-dihydroorotate + NAD+ = orotate + NADH + H+ [RN:R01869]
ALL_REAC    R01869
SUBSTRATE   (S)-dihydroorotate [CPD:C00337];
            NAD+ [CPD:C00003]
PRODUCT     orotate [CPD:C00295];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016];
            FMN [CPD:C00061]
COMMENT     A flavoprotein (FAD, FMN).
REFERENCE   1  [PMID:13610849]
  AUTHORS   FRIEDMANN HC, VENNESLAND B.
  TITLE     Purification and properties of dihydro-orotic dehydrogenase.
  JOURNAL   J. Biol. Chem. 233 (1958) 1398-406.
  ORGANISM  Zymobacterium oroticum
REFERENCE   2  [PMID:13825167]
  AUTHORS   FRIEDMANN HC, VENNESLAND B.
  TITLE     Crystalline dihydroorotic dehydrogenase.
  JOURNAL   J. Biol. Chem. 235 (1960) 1526-32.
  ORGANISM  Zymobacterium oroticum
REFERENCE   3  [PMID:13115431]
  AUTHORS   LIEBERMAN I, KORNBERG A.
  TITLE     Enzymic synthesis and breakdown of a pyrimidine, orotic acid. I.
            Dihydro-orotic dehydrogenase.
  JOURNAL   Biochim. Biophys. Acta. 12 (1953) 223-34.
  ORGANISM  Zymobacterium oroticum
PATHWAY     PATH: map00240  Pyrimidine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.14
            ExPASy - ENZYME nomenclature database: 1.3.1.14
            ExplorEnz - The Enzyme Database: 1.3.1.14
            ERGO genome analysis and discovery system: 1.3.1.14
            BRENDA, the Enzyme Database: 1.3.1.14
            CAS: 37255-26-8
///
ENTRY       EC 1.3.1.15                 Enzyme
NAME        orotate reductase (NADPH);
            orotate reductase;
            dihydroorotate dehydrogenase;
            dihydro-orotic dehydrogenase;
            L-5,6-dihydro-orotate:NAD+ oxidoreductase;
            orotate reductase (NADPH)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-dihydroorotate:NADP+ oxidoreductase
REACTION    (S)-dihydroorotate + NADP+ = orotate + NADPH + H+ [RN:R01866]
ALL_REAC    R01866
SUBSTRATE   (S)-dihydroorotate [CPD:C00337];
            NADP+ [CPD:C00006]
PRODUCT     orotate [CPD:C00295];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016];
            Flavoprotein [CPD:C06411]
COMMENT     A flavoprotein.
REFERENCE   1  [PMID:4380263]
  AUTHORS   Taylor WH, Taylor ML, Eames DF.
  TITLE     Two functionally different dihydroorotic dehydrogenases in bacteria.
  JOURNAL   J. Bacteriol. 91 (1966) 2251-6.
  ORGANISM  Pseudomonas sp.
REFERENCE   2
  AUTHORS   Ukada, S. and Vennesland, B.
  TITLE     Properties of triphosphopyridine nucleotide-linked dihydroorotic
            dehydrogenase.
  JOURNAL   J. Biol. Chem. 237 (1962) 2018-2024.
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.15
            ExPASy - ENZYME nomenclature database: 1.3.1.15
            ExplorEnz - The Enzyme Database: 1.3.1.15
            ERGO genome analysis and discovery system: 1.3.1.15
            BRENDA, the Enzyme Database: 1.3.1.15
            CAS: 37255-27-9
///
ENTRY       EC 1.3.1.16                 Enzyme
NAME        beta-nitroacrylate reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-nitropropanoate:NADP+ oxidoreductase
REACTION    3-nitropropanoate + NADP+ = 3-nitroacrylate + NADPH + H+ [RN:R03900]
ALL_REAC    R03900
SUBSTRATE   3-nitropropanoate [CPD:C02516];
            NADP+ [CPD:C00006]
PRODUCT     3-nitroacrylate [CPD:C02231];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Shaw, P.D.
  TITLE     Biosynthesis of nitro compounds. III. The enzymatic reduction of
            beta-nitroacrylic acid to beta-nitropropionic acid.
  JOURNAL   Biochemistry 6 (1967) 2253-2260.
  ORGANISM  Penicillium atrovenetum
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.16
            ExPASy - ENZYME nomenclature database: 1.3.1.16
            ExplorEnz - The Enzyme Database: 1.3.1.16
            ERGO genome analysis and discovery system: 1.3.1.16
            BRENDA, the Enzyme Database: 1.3.1.16
            CAS: 37255-28-0
///
ENTRY       EC 1.3.1.17                 Enzyme
NAME        3-methyleneoxindole reductase;
            3-methyloxindole:NADP+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-methyl-1,3-dihydroindol-2-one:NADP+ oxidoreductase
REACTION    3-methyl-1,3-dihydroindol-2-one + NADP+ =
            3-methylene-1,3-dihydro-2H-indol-2-one + NADPH + H+ [RN:R03930]
ALL_REAC    R03930
SUBSTRATE   3-methyl-1,3-dihydroindol-2-one;
            NADP+ [CPD:C00006]
PRODUCT     3-methylene-1,3-dihydro-2H-indol-2-one;
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:6021071]
  AUTHORS   Moyed HS, Williamson V.
  TITLE     Multiple 3-methyleneoxindole reductases of peas, differential
            inhibition by synthetic auxins.
  JOURNAL   J. Biol. Chem. 242 (1967) 1075-7.
  ORGANISM  Pisum sativum
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.17
            ExPASy - ENZYME nomenclature database: 1.3.1.17
            ExplorEnz - The Enzyme Database: 1.3.1.17
            ERGO genome analysis and discovery system: 1.3.1.17
            BRENDA, the Enzyme Database: 1.3.1.17
            CAS: 37255-29-1
///
ENTRY       EC 1.3.1.18                 Enzyme
NAME        kynurenate-7,8-dihydrodiol dehydrogenase;
            7,8-dihydro-7,8-dihydroxykynurenate dehydrogenase;
            7,8-dihydroxykynurenic acid 7,8-diol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     7,8-dihydro-7,8-dihydroxykynurenate:NAD+ oxidoreductase
REACTION    7,8-dihydro-7,8-dihydroxykynurenate + NAD+ = 7,8-dihydroxykynurenate
            + NADH + H+ [RN:R03251]
ALL_REAC    R03251
SUBSTRATE   7,8-dihydro-7,8-dihydroxykynurenate [CPD:C01249];
            NAD+ [CPD:C00003]
PRODUCT     7,8-dihydroxykynurenate [CPD:C01111];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Taniuchi, H. and Hayaishi, O.
  TITLE     Studies on the metabolism of kynurenic acid. III. Enzymatic
            formation of 7,8-dihydroxykynurenic acid from kynurenic acid.
  JOURNAL   J. Biol. Chem. 238 (1963) 283-293.
  ORGANISM  Pyrococcus fluorescens
PATHWAY     PATH: map00380  Tryptophan metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.18
            ExPASy - ENZYME nomenclature database: 1.3.1.18
            ExplorEnz - The Enzyme Database: 1.3.1.18
            ERGO genome analysis and discovery system: 1.3.1.18
            BRENDA, the Enzyme Database: 1.3.1.18
            CAS: 37255-30-4
///
ENTRY       EC 1.3.1.19                 Enzyme
NAME        cis-1,2-dihydrobenzene-1,2-diol dehydrogenase;
            cis-benzene glycol dehydrogenase;
            cis-1,2-dihydrocyclohexa-3,5-diene (nicotinamide adenine
            dinucleotide) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     cis-1,2-dihydrobenzene-1,2-diol:NAD+ oxidoreductase
REACTION    cis-1,2-dihydrobenzene-1,2-diol + NAD+ = catechol + NADH + H+
            [RN:R00812]
ALL_REAC    R00812;
            (other) R04088 R05354 R06832 R06857 R07703
SUBSTRATE   cis-1,2-dihydrobenzene-1,2-diol [CPD:C04091];
            NAD+ [CPD:C00003]
PRODUCT     catechol [CPD:C00090];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4362337]
  AUTHORS   Axcell BC, Geary PJ.
  TITLE     The metabolism of benzene by bacteria. Purification and some
            properties of the enzyme cis-1,2-dihydroxycyclohexa-3,5-diene
            (nicotinamide adenine dinucleotide) oxidoreductase (cis-benzene
            glycol dehydrogenase).
  JOURNAL   Biochem. J. 136 (1973) 927-34.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:4298226]
  AUTHORS   Gibson DT, Koch JR, Kallio RE.
  TITLE     Oxidative degradation of aromatic hydrocarbons by microorganisms. I.
            Enzymatic formation of catechol from benzene.
  JOURNAL   Biochemistry. 7 (1968) 2653-62.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
            PATH: map00622  Toluene and xylene degradation
            PATH: map00626  Naphthalene and anthracene degradation
            PATH: map00643  Styrene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.19
            ExPASy - ENZYME nomenclature database: 1.3.1.19
            ExplorEnz - The Enzyme Database: 1.3.1.19
            ERGO genome analysis and discovery system: 1.3.1.19
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.19
            BRENDA, the Enzyme Database: 1.3.1.19
            CAS: 51923-03-6
///
ENTRY       EC 1.3.1.20                 Enzyme
NAME        trans-1,2-dihydrobenzene-1,2-diol dehydrogenase;
            dihydrodiol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     trans-1,2-dihydrobenzene-1,2-diol:NADP+ oxidoreductase
REACTION    trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
            [RN:R00814]
ALL_REAC    R00814;
            (other) R07015
SUBSTRATE   trans-1,2-dihydrobenzene-1,2-diol [CPD:C04221];
            NADP+ [CPD:C00006]
PRODUCT     catechol [CPD:C00090];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13651190]
  AUTHORS   AYENGAR PK, HAYAISHI O, NAKAJIMA M, TOMIDA I.
  TITLE     Enzymic aromatization of 3,5-cyclohexadiene-1,2-diol.
  JOURNAL   Biochim. Biophys. Acta. 33 (1959) 111-9.
  ORGANISM  rabbit
PATHWAY     PATH: map00980  Metabolism of xenobiotics by cytochrome P450
ORTHOLOGY   KO: K00212  trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
GENES       HSA: 1109(AKR1C4) 1645(AKR1C1) 1646(AKR1C2) 27294(DHDH)
                 8644(AKR1C3)
            PTR: 456194(DHDH)
            MMU: 71755(Dhdh)
            CFA: 403786(DHDH)
            BTA: 617564(MGC139501)
            SSC: 397337(SUS2DD)
            SPU: 581125(LOC581125)
            RLE: RL2323
            BME: BMEI2003 BMEII1125
            BMF: BAB2_0108
STRUCTURES  PDB: 1RY0  1RY8  1S1P  1S1R  1S2A  1S2C  1XF0  1ZQ5  2F38  2HDJ  
                 2IPJ  2O48  2O4U  2POQ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.20
            ExPASy - ENZYME nomenclature database: 1.3.1.20
            ExplorEnz - The Enzyme Database: 1.3.1.20
            ERGO genome analysis and discovery system: 1.3.1.20
            BRENDA, the Enzyme Database: 1.3.1.20
            CAS: 37255-32-6
///
ENTRY       EC 1.3.1.21                 Enzyme
NAME        7-dehydrocholesterol reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     cholesterol:NADP+ Delta7-oxidoreductase
REACTION    cholesterol + NADP+ = cholesta-5,7-dien-3beta-ol + NADPH + H+
            [RN:R01456]
ALL_REAC    R01456;
            (other) R01451
SUBSTRATE   cholesterol [CPD:C00187];
            NADP+ [CPD:C00006]
PRODUCT     cholesta-5,7-dien-3beta-ol [CPD:C01164];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:14189869]
  AUTHORS   DEMPSEY ME, SEATON JD, SCHROEPFER GJ Jr, TROCKMAN RW.
  TITLE     THE INTERMEDIARY ROLE OF DELTA-5,7-CHOLESTADIEN-3-BETA-OL IN
            CHOLESTEROL BIOSYNTHESIS.
  JOURNAL   J. Biol. Chem. 239 (1964) 1381-7.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K00213  7-dehydrocholesterol reductase
GENES       HSA: 1717(DHCR7)
            PTR: 451393(DHCR7)
            MMU: 13360(Dhcr7)
            RNO: 64191(Dhcr7)
            CFA: 483675(DHCR7)
            BTA: 514745(DHCR7)
            GGA: 422982(DHCR7)
            XLA: 379273(xdhcr7)
            XTR: 394844(dhcr7)
            DRE: 378446(dhcr7)
            ATH: AT1G50430(DWF5)
            OSA: 4329318
            AOR: AO090003000792
            PCU: pc1220(dhcR7)
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.21
            ExPASy - ENZYME nomenclature database: 1.3.1.21
            ExplorEnz - The Enzyme Database: 1.3.1.21
            ERGO genome analysis and discovery system: 1.3.1.21
            BRENDA, the Enzyme Database: 1.3.1.21
            CAS: 9080-21-1
///
ENTRY       EC 1.3.1.22                 Enzyme
NAME        cholestenone 5alpha-reductase;
            testosterone Delta4-5alpha-reductase;
            steroid 5alpha-reductase;
            3-oxosteroid Delta4-dehydrogenase;
            5alpha-reductase;
            steroid 5alpha-hydrogenase;
            3-oxosteroid 5alpha-reductase;
            testosterone Delta4-hydrogenase;
            4-ene-3-oxosteroid 5alpha-reductase;
            reduced nicotinamide adenine dinucleotide
            phosphate:Delta4-3-ketosteroid 5alpha-oxidoreductase;
            4-ene-5alpha-reductase;
            Delta4-3-ketosteroid 5alpha-oxidoreductase;
            cholest-4-en-3-one 5alpha-reductase;
            testosterone 5alpha-reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-oxo-5alpha-steroid:NADP+ Delta4-oxidoreductase
REACTION    5alpha-cholestan-3-one + NADP+ = cholest-4-en-3-one + NADPH + H+
            [RN:R02610]
ALL_REAC    R02610
SUBSTRATE   5alpha-cholestan-3-one [CPD:C03238];
            NADP+ [CPD:C00006]
PRODUCT     cholest-4-en-3-one [CPD:C00599];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:5907469]
  AUTHORS   Shefer S, Hauser S, Mosbach EH.
  TITLE     Studies on the biosynthesis of 5-alpha-cholestan-3-beta-ol. I.
            Cholestenone 5-alpha-reductase of rat liver.
  JOURNAL   J. Biol. Chem. 241 (1966) 946-52.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.22
            ExPASy - ENZYME nomenclature database: 1.3.1.22
            ExplorEnz - The Enzyme Database: 1.3.1.22
            ERGO genome analysis and discovery system: 1.3.1.22
            BRENDA, the Enzyme Database: 1.3.1.22
            CAS: 37255-34-8
///
ENTRY       EC 1.3.1.23       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: cholestenone beta-reductase. The enzyme is identical
            to EC 1.3.1.3, Delta4-3-oxosteroid 5beta-reductase. (EC 1.3.1.23
            created 1972, deleted 2005)
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.23
            ExPASy - ENZYME nomenclature database: 1.3.1.23
            ExplorEnz - The Enzyme Database: 1.3.1.23
            ERGO genome analysis and discovery system: 1.3.1.23
            BRENDA, the Enzyme Database: 1.3.1.23
///
ENTRY       EC 1.3.1.24                 Enzyme
NAME        biliverdin reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     bilirubin:NAD(P)+ oxidoreductase
REACTION    bilirubin + NAD(P)+ = biliverdin + NAD(P)H + H+ [RN:R02391 R02393]
ALL_REAC    R02391 R02393
SUBSTRATE   bilirubin [CPD:C00486];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     biliverdin [CPD:C00500];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4378982]
  AUTHORS   Singleton JW, Laster L.
  TITLE     Biliverdin reductase of guinea pig liver.
  JOURNAL   J. Biol. Chem. 240 (1965) 4780-9.
  ORGANISM  guinea pig
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K00214  biliverdin reductase
GENES       HSA: 644(BLVRA) 645(BLVRB)
            PTR: 463366(BLVRA)
            MMU: 109778(Blvra) 233016(Blvrb)
            RNO: 116599(Blvra)
            CFA: 475867(BLVRA)
            BTA: 281650(BLVRB)
            GGA: 420776(BLVRA)
            XTR: 448743(blvra)
            SYN: slr1784(bvdR)
            GVI: glr0850(bvdR)
            ANA: alr4149(bvdR)
            AVA: Ava_0755
STRUCTURES  PDB: 1GCU  1HDO  1HE2  1HE3  1HE4  1HE5  1LC0  1LC3  2H63  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.24
            ExPASy - ENZYME nomenclature database: 1.3.1.24
            ExplorEnz - The Enzyme Database: 1.3.1.24
            ERGO genome analysis and discovery system: 1.3.1.24
            BRENDA, the Enzyme Database: 1.3.1.24
            CAS: 9074-10-6
///
ENTRY       EC 1.3.1.25                 Enzyme
NAME        1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase;
            3,5-cyclohexadiene-1,2-diol-1-carboxylate dehydrogenase;
            3,5-cyclohexadiene-1,2-diol-1-carboxylic acid dehydrogenase;
            dihydrodihydroxybenzoate dehydrogenase;
            DHBDH;
            cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase;
            2-hydro-1,2-dihydroxybenzoate dehydrogenase;
            cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate:NAD+
            oxidoreductase;
            dihydrodihydroxybenzoate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate:NAD+
            oxidoreductase (decarboxylating)
REACTION    (1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+ =
            catechol + CO2 + NADH + H+ [RN:R00813]
ALL_REAC    R00813;
            (other) R00820
SUBSTRATE   (1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate;
            NAD+ [CPD:C00003]
PRODUCT     catechol [CPD:C00090];
            CO2 [CPD:C00011];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4341530]
  AUTHORS   Reiner AM.
  TITLE     Metabolism of aromatic compounds in bacteria. Purification and
            properties of the catechol-forming enzyme,
            3,5-cyclohexadiene-1,2-diol-1-carboxylic acid (NAD + )
            oxidoreductase (decarboxylating).
  JOURNAL   J. Biol. Chem. 247 (1972) 4960-5.
  ORGANISM  Alcaligenes eutrophus
REFERENCE   2  [PMID:1740120]
  AUTHORS   Neidle E, Hartnett C, Ornston LN, Bairoch A, Rekik M, Harayama S.
  TITLE     cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene
            and the Acinetobacter calcoaceticus chromosomal benD gene are
            members of the short-chain alcohol dehydrogenase superfamily.
  JOURNAL   Eur. J. Biochem. 204 (1992) 113-20.
  ORGANISM  Pseudomonas putida [GN:ppu], Acinetobacter calcoaceticus
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00632  Benzoate degradation via CoA ligation
ORTHOLOGY   KO: K05783  1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate
                        dehydrogenase
GENES       PAE: PA2515(xylL)
            PAU: PA14_32130(xylL)
            PPU: PP_3164(benD)
            PFL: PFL_3855(xylL)
            PFO: Pfl_2324 Pfl_2965
            PEN: PSEEN3140(benD)
            PCR: Pcryo_1264
            ACI: ACIAD1439(benD)
            REU: Reut_B4406
            REH: H16_A1960(benD)
            RME: Rmet_4885
            BMA: BMAA0184
            BMV: BMASAVP1_1357(benD)
            BML: BMA10299_1553(benD)
            BMN: BMA10247_A0212(benD)
            BXE: Bxe_B0912(benD)
            BCH: Bcen2424_6527
            BAM: Bamb_6581
            BPS: BPSS1906(benD)
            BPM: BURPS1710b_A1002(benD)
            BPL: BURPS1106A_A2584(benD)
            BPD: BURPS668_A2728(benD)
            BTE: BTH_II0470
            PNA: Pnap_2109
            DAR: Daro_2781
            CGL: NCgl2323(cgl2407)
            CGB: cg2640(benD)
            CEF: CE2308
            RHA: RHA1_ro02387(benD)
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.25
            ExPASy - ENZYME nomenclature database: 1.3.1.25
            ExplorEnz - The Enzyme Database: 1.3.1.25
            ERGO genome analysis and discovery system: 1.3.1.25
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.25
            BRENDA, the Enzyme Database: 1.3.1.25
            CAS: 60496-16-4
///
ENTRY       EC 1.3.1.26                 Enzyme
NAME        dihydrodipicolinate reductase;
            dihydrodipicolinic acid reductase;
            2,3,4,5-tetrahydrodipicolinate:NAD(P)+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate:NAD(P)+
            oxidoreductase
REACTION    (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ =
            2,3-dihydrodipicolinate + NAD(P)H + H+ [RN:R04198 R04199]
ALL_REAC    R04198 R04199
SUBSTRATE   (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate [CPD:C03972];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     2,3-dihydrodipicolinate [CPD:C03340];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4378965]
  AUTHORS   Farkas W, Gilvarg C.
  TITLE     The reduction step in diaminopimelic acid biosynthesis.
  JOURNAL   J. Biol. Chem. 240 (1965) 4717-22.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Tamir, H.
  TITLE     Dihydrodipicolinic acid reductase (Escherichia coli).
  JOURNAL   Methods Enzymol. 17B (1971) 134-139.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K00215  dihydrodipicolinate reductase
GENES       ATH: AT5G52100
            OSA: 4331417 4332231
            CME: CMN258C
            ECO: b0031(dapB)
            ECJ: JW0029(dapB)
            ECE: Z0036(dapB)
            ECS: ECs0034
            ECC: c0037(dapB)
            ECI: UTI89_C0034(dapB)
            ECP: ECP_0029
            ECV: APECO1_1951(dapB)
            ECW: EcE24377A_0031(dapB)
            ECX: EcHS_A0033
            STY: STY0073(dapB)
            STT: t0066(dapB)
            SPT: SPA0065(dapB)
            SEC: SC0058(dapB)
            STM: STM0064(dapB)
            YPE: YPO0480(dapB)
            YPK: y3694(dapB)
            YPM: YP_3699(dapB)
            YPA: YPA_4073
            YPN: YPN_0353
            YPP: YPDSF_3153
            YPS: YPTB0622(dapB)
            YPI: YpsIP31758_3455(dapB)
            SFL: SF0028(dapB)
            SFX: S0030(dapB)
            SFV: SFV_0025(dapB)
            SSN: SSON_0036(dapB)
            SBO: SBO_0030(dapB)
            SDY: SDY_0053(dapB)
            ECA: ECA3872
            PLU: plu0602(dapB)
            BUC: BU146(dapB)
            BAS: BUsg139(dapB)
            BAB: bbp136(dapB)
            BCC: BCc_092(dapB)
            WBR: WGLp025(dapB)
            SGL: SG0418
            ENT: Ent638_0590
            SPE: Spro_0712
            BFL: Bfl121(dapB)
            BPN: BPEN_125(dapB)
            HIT: NTHI1621(dapB)
            HIP: CGSHiEE_05150
            HIQ: CGSHiGG_01435
            HDU: HD1398(dapB)
            HSO: HS_0835(dapB)
            PMU: PM0726(dapB)
            MSU: MS0971(dapB)
            APL: APL_0684(dapB)
            ASU: Asuc_1483
            XFA: XF1105
            XFT: PD0397(dapB)
            XCC: XCC1840(dapB)
            XCB: XC_2349
            XCV: XCV1906(dapB)
            XAC: XAC1860(dapB)
            XOM: XOO_2741(XOO2741)
            VCH: VC2391
            VCO: VC0395_A1970(dapB)
            VVU: VV1_0567
            VVY: VV0623
            VPA: VP0469
            VFI: VF0471
            PPR: PBPRA0595
            PAE: PA4759(dapB)
            PAU: PA14_62940(dapB)
            PAP: PSPA7_5479(dapB)
            PPU: PP_4725(dapB)
            PPF: Pput_4591
            PST: PSPTO_4503(dapB)
            PSB: Psyr_4193(dapB)
            PSP: PSPPH_4204(dapB)
            PFL: PFL_0829(dapB)
            PFO: Pfl_0765
            PEN: PSEEN0780(dapB)
            PMY: Pmen_3622
            PAR: Psyc_0028(dapB)
            PCR: Pcryo_0035
            PRW: PsycPRwf_0041
            ACI: ACIAD3619(dapB)
            SON: SO_1140(dapB)
            SDN: Sden_0994
            SFR: Sfri_0974
            SAZ: Sama_2505
            SBL: Sbal_3306
            SBM: Shew185_3402
            SLO: Shew_2840
            SPC: Sputcn32_2941
            SSE: Ssed_3405
            SPL: Spea_3076
            SHE: Shewmr4_0964
            SHM: Shewmr7_1002
            SHN: Shewana3_0966
            SHW: Sputw3181_1001
            ILO: IL0982(dapB)
            CPS: CPS_3460(dapB)
            PHA: PSHAa1227(dapB)
            PAT: Patl_2216
            SDE: Sde_2730
            PIN: Ping_3648
            MAQ: Maqu_3360
            CBU: CBU_1709(dapB)
            CBD: COXBU7E912_0297(dapB)
            LPN: lpg0131(dapB)
            LPF: lpl0131(dapB)
            LPP: lpp0146(dapB)
            MCA: MCA1854(dapB)
            FTN: FTN_1729(dapB)
            TCX: Tcr_0872
            NOC: Noc_2809
            AEH: Mlg_1898
            HHA: Hhal_1474
            HCH: HCH_01226(dapB)
            CSA: Csal_3087
            ABO: ABO_0316(dapB)
            MMW: Mmwyl1_1150
            AHA: AHA_2725(dapB)
            DNO: DNO_0561(dapB)
            CRP: CRP_064
            RMA: Rmag_0828
            VOK: COSY_0754(dapB)
            NME: NMB0203
            NMA: NMA0066(dapB)
            NMC: NMC0195(dapB)
            NGO: NGO1781
            CVI: CV_1795(dapB)
            RSO: RSc2745(dapB)
            REU: Reut_A2835 Reut_A3053
            REH: H16_A3141(dapB) H16_A3348
            RME: Rmet_2974 Rmet_3210
            BMA: BMA2456(dapB)
            BMV: BMASAVP1_A0373(dapB)
            BML: BMA10299_A1232(dapB)
            BMN: BMA10247_2643(dapB)
            BXE: Bxe_A0573
            BVI: Bcep1808_0619
            BUR: Bcep18194_A3737
            BCN: Bcen_0168
            BCH: Bcen2424_0651
            BAM: Bamb_0546
            BPS: BPSL2941(dapB)
            BPM: BURPS1710b_3455(dapB)
            BPL: BURPS1106A_3453(dapB)
            BPD: BURPS668_3418(dapB)
            BTE: BTH_I1208(dapB)
            PNU: Pnuc_0231
            BPE: BP2509(dapB)
            BPA: BPP3496(dapB)
            BBR: BB3944(dapB)
            RFR: Rfer_0755
            POL: Bpro_4608
            PNA: Pnap_3789
            AAV: Aave_4553
            AJS: Ajs_3922
            VEI: Veis_1070
            MPT: Mpe_A0221
            HAR: HEAR2657(dapB)
            MMS: mma_2892
            NEU: NE0614
            NET: Neut_1940
            NMU: Nmul_A0477
            EBA: ebA4812(dapB)
            AZO: azo2576(dapB)
            DAR: Daro_0936
            TBD: Tbd_1125
            MFA: Mfla_0777
            HPY: HP0510(dapB)
            HPJ: jhp0460(dapB)
            HPA: HPAG1_0484
            HHE: HH0487(dapB)
            HAC: Hac_0897(dapB)
            WSU: WS0455(dapB)
            TDN: Tmden_1870
            CJE: Cj0197c(dapB)
            CJR: CJE0190(dapB)
            CJJ: CJJ81176_0228(dapB)
            CJU: C8J_0186(dapB)
            CJD: JJD26997_0207(dapB)
            CFF: CFF8240_0298(dapB)
            CCV: CCV52592_0841(dapB)
            CHA: CHAB381_1358(dapB)
            CCO: CCC13826_1138(dapB) CCC13826_1377
            ABU: Abu_2089(dapB)
            NIS: NIS_1548(dapB)
            SUN: SUN_0235(dapB)
            GSU: GSU0160(dapB)
            GME: Gmet_0212
            GUR: Gura_0235
            PCA: Pcar_2422
            PPD: Ppro_3062 Ppro_3262
            DVU: DVU1609(dapB)
            DVL: Dvul_1525
            DDE: Dde_2092
            LIP: LI0243(dapB)
            BBA: Bd0047(dapB)
            DPS: DP0431
            ADE: Adeh_4068
            AFW: Anae109_0355
            MXA: MXAN_5927(dapB)
            SAT: SYN_02162
            SFU: Sfum_0055
            RPR: RP148
            RTY: RT0137(dapB)
            RCO: RC0190(dapB)
            RFE: RF_1133(dapB)
            RBE: RBE_1138(dapB)
            RAK: A1C_01055
            RBO: A1I_01615
            RCM: A1E_00765
            RRI: A1G_01080
            OTS: OTBS_0446(dapB)
            WOL: WD0370(dapB)
            WBM: Wbm0177
            AMA: AM873(dapB)
            ERU: Erum5770(dapB)
            ERW: ERWE_CDS_06060(dapB)
            ERG: ERGA_CDS_05970(dapB)
            ECN: Ecaj_0579
            ECH: ECH_0443(dapB)
            PUB: SAR11_0366(dapB)
            MLO: mlr4642 mlr7948
            MES: Meso_3592
            PLA: Plav_3571
            SME: SMc02837(dapB)
            SMD: Smed_3371
            ATU: Atu0183(dapB)
            ATC: AGR_C_307(dhpR)
            RET: RHE_CH00170(dapB1) RHE_CH02593(dapB2)
            RLE: RL0180(dapB) RL3002(dapB)
            BME: BMEII0249
            BMF: BAB2_1012(dapB)
            BMS: BRA1051(dapB)
            BMB: BruAb2_0991(dapB)
            BOV: BOV_A0989(dapB)
            OAN: Oant_1330
            BJA: blr0685(dapB)
            BRA: BRADO0158(dapB)
            BBT: BBta_0197(dapB)
            RPA: RPA0339(dapB)
            RPB: RPB_0435
            RPC: RPC_0335
            RPD: RPD_0385
            RPE: RPE_0343
            NWI: Nwi_0201
            NHA: Nham_0158
            BHE: BH12440(dapB)
            BQU: BQ09810
            BBK: BARBAKC583_1051(dapB)
            XAU: Xaut_0359
            CCR: CC_3550
            SIL: SPO3834(dapB)
            SIT: TM1040_0087
            RSP: RSP_1105(dapB)
            RSH: Rsph17029_2767
            RSQ: Rsph17025_2925
            JAN: Jann_4037
            RDE: RD1_0650(dapB)
            PDE: Pden_2798
            MMR: Mmar10_2997
            HNE: HNE_0437(dapB)
            ZMO: ZMO0707(dapB)
            NAR: Saro_0004
            SAL: Sala_2747
            SWI: Swit_0204
            ELI: ELI_10585
            GOX: GOX0864
            GBE: GbCGDNIH1_2408
            ACR: Acry_1055
            RRU: Rru_A0154
            MGM: Mmc1_0512
            ABA: Acid345_2492
            SUS: Acid_6981
            BSU: BG11207(dapB)
            BHA: BH1680(dapB)
            BAN: BA1555(dapB)
            BAR: GBAA1555(dapB)
            BAA: BA_2073(dapB)
            BAT: BAS1442
            BCE: BC1532
            BCA: BCE_1661(dapB)
            BCZ: BCZK1415(dapB)
            BCY: Bcer98_1256
            BTK: BT9727_1414(dapB)
            BLI: BL02758(dapB)
            BLD: BLi02384(dapB)
            BCL: ABC1916(dapB)
            BAY: RBAM_020640
            BPU: BPUM_1980
            OIH: OB1768(dapB)
            GKA: GK2185
            SAU: SA1228(dapB)
            SAV: SAV1396(dapB)
            SAM: MW1284(dapB)
            SAR: SAR1408(dapB)
            SAS: SAS1337
            SAC: SACOL1431(dapB)
            SAB: SAB1251(dapB)
            SAA: SAUSA300_1289(dapB)
            SAO: SAOUHSC_01397
            SAJ: SaurJH9_1457
            SAH: SaurJH1_1486
            SEP: SE1076
            SER: SERP0966(dapB)
            SHA: SH1515(dapB)
            SSP: SSP1354
            LMO: lmo1907(dapB)
            LMF: LMOf2365_1936(dapB)
            LIN: lin2021(dapB)
            LWE: lwe1926(dapB)
            LLA: L0094(dapB)
            LLC: LACR_1655
            LLM: llmg_0940(dapB)
            SPN: SP_1555
            SPR: spr1414(dapB)
            SPD: SPD_1387(dapB)
            SMU: SMU.900(dapB)
            STC: str0424(dapB)
            STL: stu0424(dapB)
            SSA: SSA_1085(dapB)
            SGO: SGO_1116(dapB)
            LPL: lp_1874(dapB)
            LAC: LBA0855(dapB)
            LSL: LSL_0705(dapB)
            LCA: LSEI_0094
            LRE: Lreu_0616
            EFA: EF1557(dapB)
            OOE: OEOE_0775
            STH: STH1544
            CAC: CAC2379(dapB)
            CPE: CPE1906(dapB)
            CPF: CPF_2162(dapB)
            CPR: CPR_1873(dapB)
            CTC: CTC02295
            CNO: NT01CX_1745(dapB)
            CTH: Cthe_0963 Cthe_1170
            CDF: CD3226(dapB1) CD3229(dapB2)
            CBO: CBO0791(dapB) CBO3153(dapB)
            CBA: CLB_0833(dapB-1) CLB_3188(dapB-2)
            CBH: CLC_0847(dapB-1) CLC_3063(dapB-2)
            CBF: CLI_0877(dapB-1) CLI_3218(dapB-2)
            CBE: Cbei_1795 Cbei_2934
            CKL: CKL_2799(dapB1) CKL_3205(dapB2)
            AMT: Amet_3196
            CHY: CHY_1151(dapB)
            DSY: DSY2503 DSY3805
            DRM: Dred_1944
            SWO: Swol_1273
            CSC: Csac_1582
            TTE: TTE0831(dapB)
            MTA: Moth_1063
            MTU: Rv2773c(dapB)
            MTC: MT2843(dapB)
            MBO: Mb2795c(dapB)
            MBB: BCG_2790c(dapB)
            MPA: MAP2878c(dapB)
            MAV: MAV_0371(dapB) MAV_1045(dapB) MAV_1757(dapB) MAV_1830(dapB)
                 MAV_2176(dapB) MAV_3662(dapB) MAV_3665(dapB) MAV_4999(dapB)
            MSM: MSMEG_0560(dapB) MSMEG_0733(dapB) MSMEG_2664(dapB)
                 MSMEG_3317(dapB) MSMEG_4350(dapB) MSMEG_5286(dapB)
            MVA: Mvan_2374
            MGI: Mflv_4013
            MMC: Mmcs_2107 Mmcs_3388 Mmcs_3522 Mmcs_3568
            MKM: Mkms_2153
            MJL: Mjls_2090
            CGL: NCgl1898(cgl1973)
            CGB: cg2163(dapB)
            CEF: CE1866(dapB)
            CDI: DIP1466(dapB)
            CJK: jk1131(dapB)
            NFA: nfa38810(dapB)
            RHA: RHA1_ro06739(dapB)
            SCO: SCO5739(dapB)
            SMA: SAV2521(dapB)
            LXX: Lxx16160(dapB)
            ART: Arth_1448
            AAU: AAur_1582(dapB)
            PAC: PPA1470 PPA2276
            NCA: Noca_3167
            TFU: Tfu_0786
            FRA: Francci3_3553
            FAL: FRAAL5751(dapB)
            ACE: Acel_1506
            KRA: Krad_1468
            SEN: SACE_5912(dapB)
            STP: Strop_1383
            BLO: BL1194(dapB)
            BAD: BAD_1303(dapB)
            RXY: Rxyl_0096
            RBA: RB11959(dapB)
            CTR: CT364(dapB)
            CTA: CTA_0396(dapB)
            CMU: TC0643
            CPN: CPn1047(dapB)
            CPA: CP0805
            CPJ: CPj1047(dapB)
            CPT: CpB1088
            CCA: CCA00715(dapB)
            CAB: CAB680(dapB)
            CFE: CF0303(dapB)
            PCU: pc0687(dapB)
            LIL: LA3305(dapB)
            LIC: LIC10843(dapB)
            LBJ: LBJ_0897(dapB)
            LBL: LBL_0912(dapB)
            SYN: sll1058(dapB)
            SYW: SYNW0819(dapB)
            SYC: syc1956_d(dapB)
            SYF: Synpcc7942_2136
            SYD: Syncc9605_1829
            SYE: Syncc9902_0826
            SYG: sync_1221(dapB)
            SYR: SynRCC307_0971(dapB)
            SYX: SynWH7803_1439(dapB)
            CYA: CYA_1305(dapB)
            CYB: CYB_0924(dapB)
            TEL: tll1987(dapB)
            GVI: gll1206(dapB)
            ANA: alr2542
            AVA: Ava_0474
            PMA: Pro0904(dapB)
            PMM: PMM0832(dapB)
            PMT: PMT0814(dapB)
            PMN: PMN2A_0379
            PMI: PMT9312_0968
            PMB: A9601_10381(dapB)
            PMC: P9515_09071(dapB)
            PMF: P9303_13941(dapB)
            PMG: P9301_10381(dapB)
            PMH: P9215_10701
            PME: NATL1_10611(dapB)
            TER: Tery_3623
            BTH: BT_3320
            BFR: BF0182
            BFS: BF0147
            PGI: PG2002(dapB)
            SRU: SRU_1081(dapB)
            CHU: CHU_2563(dapB)
            GFO: GFO_0803(dapB)
            FJO: Fjoh_0205 Fjoh_3327
            FPS: FP1128(dapB)
            CTE: CT1850(dapB)
            CCH: Cag_1805
            CPH: Cpha266_2095
            PVI: Cvib_0390
            PLT: Plut_0324
            DET: DET0971(dapB)
            DEH: cbdb_A933(dapB)
            DEB: DehaBAV1_0862
            AAE: aq_916(dapB)
            TMA: TM1520
            TPT: Tpet_1272
            TME: Tmel_1876
            FNO: Fnod_0073
            MMP: MMP0923(dapB)
            MMQ: MmarC5_0730
            MMZ: MmarC7_0170
            MAE: Maeo_0670
            MVN: Mevan_0216
            MAC: MA4474(dapB)
            MBA: Mbar_A1151
            MMA: MM_1202
            MBU: Mbur_0148
            MTP: Mthe_0825
            MHU: Mhun_1493
            MEM: Memar_1457
            MBN: Mboo_1397
            MST: Msp_0109(dapB)
            MSI: Msm_0830
            MKA: MK1422(dapB)
            HMA: rrnAC0206(dapB)
            HWA: HQ1508A(dapB)
            NPH: NP1492A(dapB)
            RCI: RCIX734(dapB)
STRUCTURES  PDB: 1ARZ  1C3V  1DIH  1DRU  1DRV  1DRW  1P9L  1VM6  1YL5  1YL6  
                 1YL7  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.26
            ExPASy - ENZYME nomenclature database: 1.3.1.26
            ExplorEnz - The Enzyme Database: 1.3.1.26
            ERGO genome analysis and discovery system: 1.3.1.26
            BRENDA, the Enzyme Database: 1.3.1.26
            CAS: 9055-46-3
///
ENTRY       EC 1.3.1.27                 Enzyme
NAME        2-hexadecenal reductase;
            2-alkenal reductase;
            hexadecanal: NADP+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     hexadecanal:NADP+ Delta2-oxidoreductase
REACTION    hexadecanal + NADP+ = 2-trans-hexadecenal + NADPH + H+ [RN:R02463]
ALL_REAC    R02463
SUBSTRATE   hexadecanal [CPD:C00517];
            NADP+ [CPD:C00006]
PRODUCT     2-trans-hexadecenal [CPD:C02788];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Specific for long chain 2-trans- and 2-cis-alkenals, with chain
            length optimum around 14 to 16 carbon atoms.
REFERENCE   1  [PMID:4154890]
  AUTHORS   Stoffel W, Darr W.
  TITLE     2-alkenal reductase isolation, properties and specificities.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 355 (1974) 54-60.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.27
            ExPASy - ENZYME nomenclature database: 1.3.1.27
            ExplorEnz - The Enzyme Database: 1.3.1.27
            ERGO genome analysis and discovery system: 1.3.1.27
            BRENDA, the Enzyme Database: 1.3.1.27
            CAS: 52227-95-9
///
ENTRY       EC 1.3.1.28                 Enzyme
NAME        2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase;
            2,3-DHB dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2,3-dihydro-2,3-dihydroxybenzoate:NAD+ oxidoreductase
REACTION    2,3-dihydro-2,3-dihydroxybenzoate + NAD+ = 2,3-dihydroxybenzoate +
            NADH + H+ [RN:R01505]
ALL_REAC    R01505
SUBSTRATE   2,3-dihydro-2,3-dihydroxybenzoate [CPD:C04171];
            NAD+ [CPD:C00003]
PRODUCT     2,3-dihydroxybenzoate [CPD:C00196];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4306838]
  AUTHORS   Young IG, Gibson F.
  TITLE     Regulation of the enzymes involved in the biosynthesis of
            2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia
            coli.
  JOURNAL   Biochim. Biophys. Acta. 177 (1969) 401-11.
  ORGANISM  Aerobacter aerogenes, Escherichia coli [GN:eco]
PATHWAY     PATH: map01053  Biosynthesis of siderophore group nonribosomal
                            peptides
ORTHOLOGY   KO: K00216  2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
GENES       CME: CML083C
            ECO: b0596(entA)
            ECJ: JW0588(entA)
            ECE: Z0738(entA)
            ECS: ECs0635
            ECC: c0683(entA)
            ECI: UTI89_C0598(entA)
            ECP: ECP_0628
            ECV: APECO1_1453(entA)
            ECW: EcE24377A_0616(entA)
            ECX: EcHS_A0647(entA)
            STY: STY0642(entA)
            STT: t2270(entA)
            SPT: SPA2136(entA)
            SEC: SC0629(entA)
            STM: STM0598(entA)
            SFL: SF0510(entA)
            SFX: S0516(entA)
            SFV: SFV_0544(entA)
            SSN: SSON_0547(entA)
            SBO: SBO_0457(entA)
            SDY: SDY_0527(entA)
            ECA: ECA0481(entA)
            PLU: plu2727(entA)
            VCH: VC0774
            VVU: VV2_0834
            VVY: VVA1299
            PPR: PBPRB1820
            ACI: ACIAD2774(entA)
            SDE: Sde_3393
            HCH: HCH_06575
            AHA: AHA_2475
            CVI: CV_1482(entA)
            BAM: Bamb_1685
            MXA: MXAN_3647
            BME: BMEII0080
            BMF: BAB2_0012
            BMS: BRA0013(entA)
            BMB: BruAb2_0013(entA)
            BOV: BOV_A0010(entA)
            BSU: BG11019(dhbA)
            BAN: BA2368(entA)
            BAR: GBAA2368(entA)
            BAA: BA_2862
            BAT: BAS2204
            BCE: BC2302
            BCA: BCE_2398(entA)
            BCZ: BCZK2127(entA)
            BTK: BT9727_2143(entA)
            BLI: BL04020(dhbA)
            BLD: BLi03902(dhbA)
            BAY: RBAM_029050
            OIH: OB0954(dhbA)
            CJK: jk1819(entA)
            RHA: RHA1_ro04794(dhbA)
            TFU: Tfu_1873
            SEN: SACE_3855(dhbA)
            AVA: Ava_3970
STRUCTURES  PDB: 2FWM  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.28
            ExPASy - ENZYME nomenclature database: 1.3.1.28
            ExplorEnz - The Enzyme Database: 1.3.1.28
            ERGO genome analysis and discovery system: 1.3.1.28
            BRENDA, the Enzyme Database: 1.3.1.28
            CAS: 37250-40-1
///
ENTRY       EC 1.3.1.29                 Enzyme
NAME        cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase;
            (+)-cis-naphthalene dihydrodiol dehydrogenase;
            naphthalene dihydrodiol dehydrogenase;
            cis-dihydrodiol naphthalene dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     cis-1,2-dihydronaphthalene-1,2-diol:NAD+ 1,2-oxidoreductase
REACTION    cis-1,2-dihydronaphthalene-1,2-diol + NAD+ = naphthalene-1,2-diol +
            NADH + H+ [RN:R04115]
ALL_REAC    R04115;
            (other) R06910 R06931 R07705
SUBSTRATE   cis-1,2-dihydronaphthalene-1,2-diol [CPD:C04314];
            NAD+ [CPD:C00003]
PRODUCT     naphthalene-1,2-diol [CPD:C03012];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts, at half the rate, on cis-anthracene dihydrodiol and
            cis-phenanthrene dihydrodiol.
REFERENCE   1  [PMID:4369091]
  AUTHORS   Patel TR, Gibson DT.
  TITLE     Purification and propeties of (plus)-cis-naphthalene dihydrodiol
            dehydrogenase of Pseudomonas putida.
  JOURNAL   J. Bacteriol. 119 (1974) 879-88.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00624  1- and 2-Methylnaphthalene degradation
            PATH: map00626  Naphthalene and anthracene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.29
            ExPASy - ENZYME nomenclature database: 1.3.1.29
            ExplorEnz - The Enzyme Database: 1.3.1.29
            ERGO genome analysis and discovery system: 1.3.1.29
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.29
            BRENDA, the Enzyme Database: 1.3.1.29
            CAS: 53986-49-5
///
ENTRY       EC 1.3.1.30                 Enzyme
NAME        progesterone 5alpha-reductase;
            steroid 5-alpha-reductase;
            Delta4-steroid 5alpha-reductase (progesterone)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     5alpha-pregnan-3,20-dione:NADP+ 5-oxidoreductase
REACTION    5alpha-pregnan-3,20-dione + NADP+ = progesterone + NADPH + H+
            [RN:R02208]
ALL_REAC    R02208
SUBSTRATE   5alpha-pregnan-3,20-dione;
            NADP+ [CPD:C00006]
PRODUCT     progesterone [CPD:C00410];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Testosterone and 20alpha-hydroxy-4-pregn-3-one can act in place of
            progesterone.
REFERENCE   1  [PMID:240847]
  AUTHORS   Cheng YJ, Karavolas HJ.
  TITLE     Subcellular distribution and properties of progesterone
            (delta4-steroid) 5alpha-reductase in rat medial basal hypothalamus.
  JOURNAL   J. Biol. Chem. 250 (1975) 7997-8003.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:1166484]
  AUTHORS   Cheng YJ, Karavolas HJ.
  TITLE     Properties and subcellular distribution of delta4-steroid
            (progesterone) 5alpha-reductase in rat anterior pituitary.
  JOURNAL   Steroids. 26 (1975) 57-71.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00140  C21-Steroid hormone metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.30
            ExPASy - ENZYME nomenclature database: 1.3.1.30
            ExplorEnz - The Enzyme Database: 1.3.1.30
            ERGO genome analysis and discovery system: 1.3.1.30
            BRENDA, the Enzyme Database: 1.3.1.30
            CAS: 72412-84-1
///
ENTRY       EC 1.3.1.31                 Enzyme
NAME        2-enoate reductase;
            enoate reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     butanoate:NAD+ Delta2-oxidoreductase
REACTION    butanoate + NAD+ = 2-butenoate + NADH + H+ [RN:R01689]
ALL_REAC    R01689;
            (other) R02252
SUBSTRATE   butanoate [CPD:C00246];
            NAD+ [CPD:C00003]
PRODUCT     2-butenoate [CPD:C01771];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023];
            Sulfur [CPD:C00087];
            Iron-sulfur [CPD:C00824]
COMMENT     An iron-sulfur-flavoprotein (FAD). Acts (in the reverse direction)
            on a wide range of alkyl and aryl alphabeta-unsaturated carboxylate
            ions; 2-butenoate was the best substrate tested.
REFERENCE   1  [PMID:477658]
  AUTHORS   Tischer W, Bader J, Simon H.
  TITLE     Purification and some properties of a hitherto-unknown enzyme
            reducing the carbon-carbon double bond of alpha, beta-unsaturated
            carboxylate anions.
  JOURNAL   Eur. J. Biochem. 97 (1979) 103-12.
  ORGANISM  Clostridium kluyveri, Clostridium sp.
PATHWAY     PATH: map00360  Phenylalanine metabolism
GENES       CBO: CBO2166(fldZ)
            CBA: CLB_2105(enr)
            CBH: CLC_2109(enr)
            CBF: CLI_2212(enr)
            CKL: CKL_0591 CKL_0743 CKL_0746 CKL_0925 CKL_1009 CKL_1015
                 CKL_1689 CKL_2573 CKL_3437
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.31
            ExPASy - ENZYME nomenclature database: 1.3.1.31
            ExplorEnz - The Enzyme Database: 1.3.1.31
            ERGO genome analysis and discovery system: 1.3.1.31
            BRENDA, the Enzyme Database: 1.3.1.31
            CAS: 70712-51-5
///
ENTRY       EC 1.3.1.32                 Enzyme
NAME        maleylacetate reductase;
            maleolylacetate reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-oxoadipate:NAD(P)+ oxidoreductase
REACTION    3-oxoadipate + NAD(P)+ = 2-maleylacetate + NAD(P)H + H+ [RN:R02988
            R02989]
ALL_REAC    R02988 R02989;
            (other) R05355 R06848 R07781
SUBSTRATE   3-oxoadipate [CPD:C00846];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     2-maleylacetate [CPD:C02222];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:7387635]
  AUTHORS   Gaal AB, Neujahr HY.
  TITLE     Maleylacetate reductase from Trichosporon cutaneum.
  JOURNAL   Biochem. J. 185 (1980) 783-6.
  ORGANISM  Trichosporon cutaneum
REFERENCE   2
  AUTHORS   Gaal, A.B. and Neujahr, H.Y.
  TITLE     Induction of phenol-metabolizing enzymes in Trichosporon cutaneum.
  JOURNAL   Arch. Microbiol. 130 (1981) 54-58.
  ORGANISM  Trichosporon cutaneum
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
            PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00627  1,4-Dichlorobenzene degradation
ORTHOLOGY   KO: K00217  maleylacetate reductase
GENES       PAP: PSPA7_3908
            REH: H16_A1786 H16_B0970(pcpE)
            RME: Rmet_5063
            BXE: Bxe_A1126(clcE)
            BUR: Bcep18194_A4484 Bcep18194_B2737
            BAM: Bamb_3335
            RLE: pRL120100(tftE) pRL120215(tftE)
            BJA: bll0995
            BRA: BRADO2265
            RPE: RPE_4908
            MSM: MSMEG_6712
            CGB: cg1310(tfdF) cg3386(tcbF)
            RHA: RHA1_ro01858 RHA1_ro02996 RHA1_ro08510 RHA1_ro11309(macA)
            SSO: SSO2490(clcE)
            STO: ST1638
            SAI: Saci_1087
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.32
            ExPASy - ENZYME nomenclature database: 1.3.1.32
            ExplorEnz - The Enzyme Database: 1.3.1.32
            ERGO genome analysis and discovery system: 1.3.1.32
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.32
            BRENDA, the Enzyme Database: 1.3.1.32
            CAS: 69669-65-4
///
ENTRY       EC 1.3.1.33                 Enzyme
NAME        protochlorophyllide reductase;
            NADPH2-protochlorophyllide oxidoreductase;
            NADPH-protochlorophyllide oxidoreductase;
            NADPH-protochlorophyllide reductase;
            protochlorophyllide oxidoreductase;
            protochlorophyllide photooxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     chlorophyllide-a:NADP+ 7,8-oxidoreductase
REACTION    chlorophyllide a + NADP+ = protochlorophyllide + NADPH + H+
            [RN:R03845]
ALL_REAC    R03845;
            (other) R06286
SUBSTRATE   chlorophyllide a [CPD:C02139];
            NADP+ [CPD:C00006]
PRODUCT     protochlorophyllide [CPD:C02880];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The enzyme catalyses a light-dependent trans-reduction of the D-ring
            of protochlorophyllide; the product has the (7S,8S)-configuration.
REFERENCE   1  [PMID:7439188]
  AUTHORS   Apel K, Santel HJ, Redlinger TE, Falk H.
  TITLE     The protochlorophyllide holochrome of barley (Hordeum vulgare L.).
            Isolation and characterization of the NADPH:protochlorophyllide
            oxidoreductase.
  JOURNAL   Eur. J. Biochem. 111 (1980) 251-8.
  ORGANISM  Hordeum vulgare [GN:ehvu]
REFERENCE   2  [PMID:31865]
  AUTHORS   Griffiths WT.
  TITLE     Reconstitution of chlorophyllide formation by isolated etioplast
            membranes.
  JOURNAL   Biochem. J. 174 (1978) 681-92.
  ORGANISM  Hordeum vulgare [GN:ehvu]
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K00218  protochlorophyllide reductase
GENES       OSA: 4337415
            CME: CMD190C CMG217C CMN338C
            PIC: PICST_81469(RDH2)
            CGR: CAGL0J05852g
            EHI: 242.t00015
            BUR: Bcep18194_B0618 Bcep18194_C7081
            BPM: BURPS1710b_A2134
            BTE: BTH_II1842
            RLE: RL1421
            BRA: BRADO1620(bchZ)
            BBT: BBta_6435(bchZ)
            RPA: RPA1524(bchZ)
            SEN: SACE_1606 SACE_1627
            SYN: slr0506(por)
            SYW: SYNW1129(pcr) SYNW1726(pcr) SYNW2400
            SYC: syc1603_d(por)
            SYF: Synpcc7942_2503
            SYD: Syncc9605_0740 Syncc9605_1268 Syncc9605_2564
            SYE: Syncc9902_1216 Syncc9902_1623 Syncc9902_2219
            SYG: sync_1162 sync_1976
            SYR: SynRCC307_1572(por)
            SYX: SynWH7803_0669(por) SynWH7803_0868(por)
            CYA: CYA_2383
            CYB: CYB_1015
            TEL: tlr0575(por)
            GVI: glr2486(por)
            ANA: all1743(por)
            AVA: Ava_0294
            PMA: Pro0543(por) Pro0791(por) Pro1537(por)
            PMM: PMM0542(por) PMM0634(por) PMM1361
            PMT: PMT0480 PMT0871(F21B7.35) PMT1218(pcr)
            PMN: PMN2A_0074 PMN2A_0729 PMN2A_1871
            PMI: PMT9312_0542 PMT9312_0634
            PMB: A9601_05981 A9601_06901 A9601_15641
            PMC: P9515_06061 P9515_07001 P9515_15241
            PMF: P9303_07921 P9303_13231 P9303_17961
            PMG: P9301_05681 P9301_06611 P9301_15491
            PME: NATL1_05961 NATL1_06971 NATL1_15671
            TER: Tery_0109
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.33
            ExPASy - ENZYME nomenclature database: 1.3.1.33
            ExplorEnz - The Enzyme Database: 1.3.1.33
            ERGO genome analysis and discovery system: 1.3.1.33
            BRENDA, the Enzyme Database: 1.3.1.33
            CAS: 68518-04-7
///
ENTRY       EC 1.3.1.34                 Enzyme
NAME        2,4-dienoyl-CoA reductase (NADPH);
            4-enoyl-CoA reductase (NADPH);
            4-enoyl coenzyme A (reduced nicotinamide adenine dinucleotide
            phosphate) reductase;
            4-enoyl-CoA reductase;
            2,4-dienoyl-CoA reductase (NADPH)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     trans-2,3-didehydroacyl-CoA:NADP+ 4-oxidoreductase
REACTION    trans-2,3-didehydroacyl-CoA + NADP+ =
            trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH + H+ [RN:R04319]
ALL_REAC    R04319
SUBSTRATE   trans-2,3-didehydroacyl-CoA [CPD:C00658];
            NADP+ [CPD:C00006]
PRODUCT     trans,trans-2,3,4,5-tetradehydroacyl-CoA [CPD:C04512];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Best substrates for reduction contain a 2,4-diene structure with a
            chain-length of 8 or 10
REFERENCE   1  [PMID:6749495]
  AUTHORS   Dommes V, Luster W, Cvetanovic M, Kunau WH.
  TITLE     Purification by affinity chromatography of 2,4-dienoyl-CoA
            reductases from bovine liver and Escherichia coli.
  JOURNAL   Eur. J. Biochem. 125 (1982) 335-41.
  ORGANISM  cow [GN:bta], Escherichia coli [GN:eco]
REFERENCE   2  [PMID:729581]
  AUTHORS   Kunau WH, Dommes P.
  TITLE     Degradation of unsaturated fatty acids. Identification of
            intermediates in the degradation of cis-4-decenoly-CoA by extracts
            of beef-liver mitochondria.
  JOURNAL   Eur. J. Biochem. 91 (1978) 533-44.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K00219  2,4-dienoyl-CoA reductase (NADPH2)
GENES       HSA: 1666(DECR1) 26063(DECR2)
            MMU: 26378(Decr2) 67460(Decr1)
            RNO: 117543(Decr1) 64461(Decr2)
            CFA: 477938(DECR1)
            GGA: 420218(DECR1)
            XLA: 443792(MGC82265)
            DRE: 406623(decr2)
            ATH: AT3G12800
            SCE: YNL202W(SPS19)
            CNE: CNI03790
            TCR: 509941.100
            LMA: LmjF33.0830
            ECO: b3081(fadH)
            ECJ: JW3052(fadH)
            ECE: Z4434(ygjL)
            ECS: ECs3963
            ECC: c3839(ygjL)
            ECI: UTI89_C3521(ygjL)
            ECP: ECP_3172
            ECW: EcE24377A_3548(fadH)
            ECX: EcHS_A3263(fadH)
            SPT: SPA3087(fadH)
            SEC: SC3166(fadH)
            STM: STM3219(fadH)
            YPE: YPO0589(fadH)
            YPK: y3589
            YPM: YP_2909(fadH)
            YPA: YPA_3199
            YPN: YPN_0458
            YPS: YPTB3469(fadH)
            YPI: YpsIP31758_0501(fadH)
            SFL: SF3121(ygjL)
            SFX: S3328(ygjL)
            SFV: SFV_3122(ygjL)
            SSN: SSON_3124(ygjL)
            SBO: SBO_2942(ygjL)
            SDY: SDY_3265(ygjL)
            ECA: ECA0655(fadF)
            PLU: plu3990(fadH)
            XCC: XCC0933(fadH)
            XCB: XC_3302
            XCV: XCV1039(fadH)
            XAC: XAC1010(fadH)
            XOO: XOO3698(fadH)
            XOM: XOO_3492(XOO3492)
            VCH: VC1993
            VCO: VC0395_A1578(fadH)
            VVU: VV1_3132
            VVY: VV1153
            VPA: VP2151
            VFI: VF1642
            PPR: PBPRA2594
            PAE: PA3092(fadH1) PA4814(fadH2)
            PAU: PA14_24170(fadH1) PA14_63640(fadH2)
            PPU: PP_2008(fadH)
            PST: PSPTO_3803(fadH)
            PSB: Psyr_1675
            PSP: PSPPH_1672(fadH)
            PFL: PFL_3969(noxB-1)
            PFO: Pfl_3687
            PEN: PSEEN1703(fadH)
            PAR: Psyc_0181(fadH2)
            ACI: ACIAD1155(fadH) ACIAD1654(fadH)
            SON: SO_2419
            SDN: Sden_1900
            SFR: Sfri_2144
            SHE: Shewmr4_1910
            SHM: Shewmr7_2068
            SHN: Shewana3_1965
            ILO: IL1748
            CPS: CPS_0925(fadH1) CPS_2449(fadH2)
            PHA: PSHAa0892 PSHAa1410(fadH)
            PAT: Patl_1371 Patl_2400
            MAQ: Maqu_2074
            LPN: lpg2347(fadH)
            LPF: lpl2269(fadH)
            LPP: lpp2296(fadH)
            NOC: Noc_1799
            HCH: HCH_04596
            ABO: ABO_1705(fadH)
            AHA: AHA_3357
            CVI: CV_0169(fadH) CV_3946(fadH)
            REU: Reut_C6110
            BMA: BMAA0192(fadH)
            BML: BMA10299_1562(fadH)
            BXE: Bxe_A1452
            BUR: Bcep18194_A3253 Bcep18194_A4477 Bcep18194_B0574
                 Bcep18194_B1624 Bcep18194_B2335 Bcep18194_B2709
                 Bcep18194_C7286
            BCN: Bcen_0863
            BCH: Bcen2424_1344 Bcen2424_3764
            BPS: BPSS1133(fadH) BPSS1898(fadH)
            BPM: BURPS1710b_A0094(fadH) BURPS1710b_A0995(fadH)
            BPL: BURPS1106A_A1515
            BPD: BURPS668_A1598
            BTE: BTH_II0478 BTH_II1273
            BBR: BB4756(fadH)
            RFR: Rfer_1891
            POL: Bpro_5274
            EBA: ebA5836(fadH)
            RLE: RL2502 pRL110496
            SIL: SPO3586(fadH)
            SIT: TM1040_2458
            RDE: RD1_0957(fadH)
            RRU: Rru_A0144
            MAG: amb3454
            BCL: ABC1993
            BAY: RBAM_013850(ykuF)
            DSY: DSY3373
            MTU: Rv1175c(fadH)
            MTC: MT1212(fadH)
            MBO: Mb1208c(fadH)
            MBB: BCG_1238c(fadH)
            MSM: MSMEG_5124
            CJK: jk0075(fadH)
            NFA: nfa12900
            RHA: RHA1_ro01415 RHA1_ro04769 RHA1_ro06074 RHA1_ro06076
            SCO: SCO7066(fadH)
            SMA: SAV1292(fadH)
            SEN: SACE_2757 SACE_4167(fadH) SACE_4354
            LIL: LA2197(fadH)
            LIC: LIC11729(fadH)
            LBJ: LBJ_1360(fadH)
            LBL: LBL_1585(fadH)
            AVA: Ava_C0148
            NPH: NP5226A
STRUCTURES  PDB: 1PS9  1W6U  1W73  1W8D  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.34
            ExPASy - ENZYME nomenclature database: 1.3.1.34
            ExplorEnz - The Enzyme Database: 1.3.1.34
            ERGO genome analysis and discovery system: 1.3.1.34
            BRENDA, the Enzyme Database: 1.3.1.34
            CAS: 82869-38-3
///
ENTRY       EC 1.3.1.35                 Enzyme
NAME        phosphatidylcholine desaturase;
            oleate desaturase;
            linoleate synthase;
            oleoyl-CoA desaturase;
            oleoylphosphatidylcholine desaturase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     1-acyl-2-oleoyl-sn-glycero-3-phosphocholine:NAD+
            Delta12-oxidoreductase
REACTION    1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + NAD+ =
            1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + NADH + H+
            [RN:R03475]
ALL_REAC    R03475
SUBSTRATE   1-acyl-2-oleoyl-sn-glycero-3-phosphocholine [CPD:C01282];
            NAD+ [CPD:C00003]
PRODUCT     1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine [CPD:C04636];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also desaturates phosphatidylcholine containing the oleoyl group on
            O-2 of the glycerol residue.
REFERENCE   1  [PMID:166662]
  AUTHORS   Pugh EL, Kates M.
  TITLE     Characterization of a membrane-bound phospholipid desaturase system
            of candida lipolytica.
  JOURNAL   Biochim. Biophys. Acta. 380 (1975) 442-53.
  ORGANISM  Candida lipolytica
REFERENCE   2  [PMID:475773]
  AUTHORS   Slack CR, Roughan PG, Browse J.
  TITLE     Evidence for an oleoyl phosphatidylcholine desaturase in microsomal
            preparations from cotyledons of safflower (Carthamus tinctorius)
            seed.
  JOURNAL   Biochem. J. 179 (1979) 649-56.
  ORGANISM  Carthamus tinctorius
REFERENCE   3  [PMID:710426]
  AUTHORS   Stymne S, Appelqvist LA.
  TITLE     The biosynthesis of linoleate from oleoyl-CoA via
            oleoyl-phosphatidylcholine in microsomes of developing safflower
            seeds.
  JOURNAL   Eur. J. Biochem. 90 (1978) 223-9.
  ORGANISM  Carthamus tinctorius
ORTHOLOGY   KO: K05893  
GENES       PSP: PSPPH_4310
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.35
            ExPASy - ENZYME nomenclature database: 1.3.1.35
            ExplorEnz - The Enzyme Database: 1.3.1.35
            ERGO genome analysis and discovery system: 1.3.1.35
            BRENDA, the Enzyme Database: 1.3.1.35
            CAS: 59929-36-1
///
ENTRY       EC 1.3.1.36                 Enzyme
NAME        geissoschizine dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     geissoschizine:NADP+ 4,21-oxidoreductase
REACTION    geissoschizine + NADP+ = 4,21-didehydrogeissoschizine + NADPH
            [RN:R03860]
ALL_REAC    R03860
SUBSTRATE   geissoschizine [CPD:C02151];
            NADP+ [CPD:C00006]
PRODUCT     4,21-didehydrogeissoschizine;
            NADPH [CPD:C00005]
COMMENT     Involved in the interconversion of heteroyohimbine alkaloids in
            Catharanthus roseus.
REFERENCE   1
  AUTHORS   Pfitzner, A. and Stockigt, J.
  TITLE     Partial-purification and characterization of geissoschizine
            dehydrogenase from suspension-cultures of Catharanthus roseus.
  JOURNAL   Phytochemistry 21 (1982) 1585-1588.
  ORGANISM  Catharanthus roseus
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.36
            ExPASy - ENZYME nomenclature database: 1.3.1.36
            ExplorEnz - The Enzyme Database: 1.3.1.36
            ERGO genome analysis and discovery system: 1.3.1.36
            BRENDA, the Enzyme Database: 1.3.1.36
            CAS: 84399-94-0
///
ENTRY       EC 1.3.1.37                 Enzyme
NAME        cis-2-enoyl-CoA reductase (NADPH);
            NADPH-dependent cis-enoyl-CoA reductase;
            reductase, cis-2-enoyl coenzyme A;
            cis-2-enoyl-coenzyme A reductase;
            cis-2-enoyl-CoA reductase (NADPH)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     acyl-CoA:NADP+ cis-2-oxidoreductase
REACTION    acyl-CoA + NADP+ = cis-2,3-dehydroacyl-CoA + NADPH + H+ [RN:R00387]
ALL_REAC    R00387
SUBSTRATE   acyl-CoA [CPD:C00040];
            NADP+ [CPD:C00006]
PRODUCT     cis-2,3-dehydroacyl-CoA [CPD:C01122];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Not identical with EC 1.3.1.38 trans-2-enoyl-CoA reductase (NADPH)
            [cf. EC 1.3.1.8 acyl-CoA dehydrogenase (NADP+)].
REFERENCE   1  [PMID:6759504]
  AUTHORS   Mizugaki M, Nishimaki T, Shiraishi T, Kawaguchi A, Okuda S, Yamanaka
            H.
  TITLE     Studies on the metabolism of unsaturated fatty acids. IX.
            Stereochemical studies of the reaction catalyzed by
            trans-2-enoyl-coenzyme A reductase of Escherichia coli.
  JOURNAL   J. Biochem. (Tokyo). 92 (1982) 1649-54.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.37
            ExPASy - ENZYME nomenclature database: 1.3.1.37
            ExplorEnz - The Enzyme Database: 1.3.1.37
            ERGO genome analysis and discovery system: 1.3.1.37
            BRENDA, the Enzyme Database: 1.3.1.37
            CAS: 72841-00-0
///
ENTRY       EC 1.3.1.38                 Enzyme
NAME        trans-2-enoyl-CoA reductase (NADPH);
            NADPH-dependent trans-2-enoyl-CoA reductase;
            reductase, trans-enoyl coenzyme A;
            trans-2-enoyl-CoA reductase (NADPH)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     acyl-CoA:NADP+ trans-2-oxidoreductase
REACTION    acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+
            [RN:R07162]
ALL_REAC    R07162 > R01278 R03776 R03856 R03989 R04753 R06985 R07761
SUBSTRATE   acyl-CoA [CPD:C00040];
            NADP+ [CPD:C00006]
PRODUCT     trans-2,3-dehydroacyl-CoA [CPD:C00658];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Not identical with EC 1.3.1.37 cis-2-enoyl-CoA reductase (NADPH)
            [cf. EC 1.3.1.8 acyl-CoA dehydrogenase (NADP+)].
REFERENCE   1  [PMID:6759504]
  AUTHORS   Mizugaki M, Nishimaki T, Shiraishi T, Kawaguchi A, Okuda S, Yamanaka
            H.
  TITLE     Studies on the metabolism of unsaturated fatty acids. IX.
            Stereochemical studies of the reaction catalyzed by
            trans-2-enoyl-coenzyme A reductase of Escherichia coli.
  JOURNAL   J. Biochem. (Tokyo). 92 (1982) 1649-54.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00062  Fatty acid elongation in mitochondria
            PATH: map01040  Polyunsaturated fatty acid biosynthesis
ORTHOLOGY   KO: K07512  mitochondrial trans-2-enoyl-CoA reductase
            KO: K07753  peroxisomal trans-2-enoyl-CoA reductase
GENES       HSA: 51102(MECR) 55825(PECR)
            PTR: 456690(MECR) 459929(PECR)
            MMU: 111175(Pecr) 26922(Mecr)
            RNO: 113956(Pecr) 29470(Mecr)
            CFA: 475082(PECR) 478159(MECR)
            BTA: 353301(NRBF1)
            GGA: 424224(PECR)
            XLA: 446674(pecr)
            XTR: 549125(mecr)
            DRE: 550550(mecr)
            SPU: 574708(LOC574708) 753057(LOC753057)
            CEL: W09H1.5 Y48A6B.9
            ATH: AT3G45770
            OSA: 4351241
            SCE: YBR026C(ETR1) YDL015C(TSC13)
            AGO: AGOS_AEL081W
            PIC: PICST_34892(ETR2)
            CGR: CAGL0B04323g
            SPO: SPAC26F1.04c
            DDI: DDBDRAFT_0204417
            TET: TTHERM_00384890
            MSM: MSMEG_4074
STRUCTURES  PDB: 1ZSY  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.38
            ExPASy - ENZYME nomenclature database: 1.3.1.38
            ExplorEnz - The Enzyme Database: 1.3.1.38
            ERGO genome analysis and discovery system: 1.3.1.38
            BRENDA, the Enzyme Database: 1.3.1.38
            CAS: 77649-64-0
///
ENTRY       EC 1.3.1.39                 Enzyme
NAME        enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific);
            acyl-ACP dehydrogenase;
            enoyl-[acyl carrier protein] (reduced nicotinamide adenine
            dinucleotide phosphate) reductase;
            NADPH 2-enoyl Co A reductase;
            enoyl-ACp reductase;
            enoyl-[acyl-carrier-protein] reductase (NADPH2, A-specific)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (A-specific)
REACTION    acyl-[acyl-carrier-protein] + NADP+ =
            trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH + H+
            [RN:R01404]
ALL_REAC    R01404
SUBSTRATE   acyl-[acyl-carrier-protein];
            NADP+ [CPD:C00006]
PRODUCT     trans-2,3-dehydroacyl-[acyl-carrier-protein];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The liver enzyme is A-specific with respect to NADP+ [cf. EC
            1.3.1.10 enoyl-[acyl-carrier-protein] reductase (NADPH,
            B-specific)].
REFERENCE   1  [PMID:4394955]
  AUTHORS   Dugan RE, Slakey LL, Porter JW.
  TITLE     Stereospecificity of the transfer of hydrogen from reduced
            nicotinamide adenine dinucleotide phosphate to the acyl chain in the
            dehydrogenase-catalyzed reactions of fatty acid synthesis.
  JOURNAL   J. Biol. Chem. 245 (1970) 6312-6.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.39
            ExPASy - ENZYME nomenclature database: 1.3.1.39
            ExplorEnz - The Enzyme Database: 1.3.1.39
            ERGO genome analysis and discovery system: 1.3.1.39
            BRENDA, the Enzyme Database: 1.3.1.39
///
ENTRY       EC 1.3.1.40                 Enzyme
NAME        2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate reductase;
            2-hydroxy-6-oxo-phenylhexa-2,4-dienoate (reduced nicotinamide
            adenine dinucleotide phosphate) reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2,6-dioxo-6-phenylhexanoate:NADP+ Delta2-oxidoreductase
REACTION    2,6-dioxo-6-phenylhexanoate + NADP+ =
            2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + NADPH + H+ [RN:R03463]
ALL_REAC    R03463
SUBSTRATE   2,6-dioxo-6-phenylhexanoate [CPD:C03750];
            NADP+ [CPD:C00006]
PRODUCT     2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate [CPD:C01273];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Broad specificity; reduces a number of compounds produced by
            Pseudomonas from aromatic hydrocarbons by ring fission.
REFERENCE   1
  AUTHORS   Omori, T., Ishigooka, H. and Minoda, Y.
  TITLE     Purification and some properties of
            2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid(HOPDA) reducing enzyme
            from Pseudomonas cruciviae S93B1 involved in the degradation of
            biphenyl.
  JOURNAL   Agric. Biol. Chem. 50 (1986) 1513-1518.
  ORGANISM  Pseudomonas cruciviae
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.40
            ExPASy - ENZYME nomenclature database: 1.3.1.40
            ExplorEnz - The Enzyme Database: 1.3.1.40
            ERGO genome analysis and discovery system: 1.3.1.40
            BRENDA, the Enzyme Database: 1.3.1.40
            CAS: 104645-83-2
///
ENTRY       EC 1.3.1.41                 Enzyme
NAME        xanthommatin reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     5,12-dihydroxanthommatin:NAD+ oxidoreductase
REACTION    5,12-dihydroxanthommatin + NAD+ = xanthommatin + NADH + H+
            [RN:R03787]
ALL_REAC    R03787
SUBSTRATE   5,12-dihydroxanthommatin [CPD:C03476];
            NAD+ [CPD:C00003]
PRODUCT     xanthommatin [CPD:C01969];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     From Drosophila melanogaster.
REFERENCE   1
  AUTHORS   Santoro, P. and Parisi, G.
  TITLE     A new enzyme from Drosophila melanogaster - in vitro conversion of
            xanthommatin into its dihydroform by means of xanthommatin
            reductase.
  JOURNAL   J. Exp. Zool. 239 (1986) 169-173.
  ORGANISM  Drosophila melanogaster [GN:dme]
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.41
            ExPASy - ENZYME nomenclature database: 1.3.1.41
            ExplorEnz - The Enzyme Database: 1.3.1.41
            ERGO genome analysis and discovery system: 1.3.1.41
            BRENDA, the Enzyme Database: 1.3.1.41
            CAS: 62972-27-4
///
ENTRY       EC 1.3.1.42                 Enzyme
NAME        12-oxophytodienoate reductase;
            12-oxo-phytodienoic acid reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     8-[(1R,2R)-3-oxo-2-{(Z)-pent-2-enyl}cyclopentyl]octanoate:NADP+
            4-oxidoreductase
REACTION    8-[(1R,2R)-3-oxo-2-{(Z)-pent-2-enyl}cyclopentyl]octanoate + NADP+ =
            (15Z)-12-oxophyto-10,15-dienoate + NADPH + H+ [RN:R03401]
ALL_REAC    R03401
SUBSTRATE   8-[(1R,2R)-3-oxo-2-{(Z)-pent-2-enyl}cyclopentyl]octanoate
            [CPD:C04780];
            NADP+ [CPD:C00006]
PRODUCT     (15Z)-12-oxophyto-10,15-dienoate [CPD:C01226];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Involved in the conversion of linolenate into jasmonate in Zea mays.
REFERENCE   1
  AUTHORS   Vick, B.A. and Zimmerman, D.C.
  TITLE     Characterization of 12-oxo-phytodienoic acid reductase in corn - the
            jasmonic acid pathway.
  JOURNAL   Plant Physiol. 80 (1986) 202-205.
  ORGANISM  Zea mays [GN:ezma]
PATHWAY     PATH: map00592  alpha-Linolenic acid metabolism
ORTHOLOGY   KO: K05894  12-oxophytodienoic acid reductase
GENES       ATH: AT1G76680(OPR1) AT1G76690(OPR2) AT2G06050(OPR3)
            OSA: 4340485 4345762
            PIC: PICST_35725(OYE3.1)
            CAL: CaO19.125
STRUCTURES  PDB: 1ICP  1ICQ  1ICS  1Q45  2G5W  2HS6  2HS8  2HSA  2Q3O  2Q3R  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.42
            ExPASy - ENZYME nomenclature database: 1.3.1.42
            ExplorEnz - The Enzyme Database: 1.3.1.42
            ERGO genome analysis and discovery system: 1.3.1.42
            BRENDA, the Enzyme Database: 1.3.1.42
            CAS: 101150-03-2
///
ENTRY       EC 1.3.1.43                 Enzyme
NAME        arogenate dehydrogenase;
            arogenic dehydrogenase (ambiguous);
            cyclohexadienyl dehydrogenase;
            pretyrosine dehydrogenase (ambiguous);
            L-arogenate:NAD+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-arogenate:NAD+ oxidoreductase (decarboxylating)
REACTION    L-arogenate + NAD+ = L-tyrosine + NADH + CO2 [RN:R00732]
ALL_REAC    R00732;
            (other) R00733 R01728 R01730
SUBSTRATE   L-arogenate [CPD:C00826];
            NAD+ [CPD:C00003]
PRODUCT     L-tyrosine [CPD:C00082];
            NADH [CPD:C00004];
            CO2 [CPD:C00011]
COMMENT     See also EC 1.3.1.12 (prephenate dehydrogenase), EC 1.3.1.78
            [arogenate dehydrogenase (NADP+)] and EC 1.3.1.79 (arogenate
            dehydrogenase [NAD(P)+]).
REFERENCE   1  [PMID:4206476]
  AUTHORS   Stenmark SL, Pierson DL, Jensen RA, Glover GI.
  TITLE     Blue-green bacteria synthesise L-tyrosine by the pretyrosine
            pathway.
  JOURNAL   Nature. 247 (1974) 290-2.
REFERENCE   2
  AUTHORS   Byng, G., Whitaker, R., Flick, C. and Jensen, R.A.
  TITLE     Enzymology of L-tyrosine biosynthesis in corn (Zea mays).
  JOURNAL   Phytochemistry 20 (1981) 1289-1292.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   3  [PMID:3967752]
  AUTHORS   Mayer E, Waldner-Sander S, Keller B, Keller E, Lingens F.
  TITLE     Purification of arogenate dehydrogenase from Phenylobacterium
            immobile.
  JOURNAL   FEBS. Lett. 179 (1985) 208-12.
  ORGANISM  Phenylobacterium immobile
REFERENCE   4
  AUTHORS   Lingens, F., Keller, E. and Keller, B.
  TITLE     Arogenate dehydrogenase from Phenylobacterium immobile.
  JOURNAL   Methods Enzymol. 142 (1987) 513-518.
  ORGANISM  Phenylobacterium immobile
REFERENCE   5  [PMID:2972718]
  AUTHORS   Zamir LO, Tiberio R, Devor KA, Sauriol F, Ahmad S, Jensen RA.
  TITLE     Structure of D-prephenyllactate. A carboxycyclohexadienyl metabolite
            from Neurospora crassa.
  JOURNAL   J. Biol. Chem. 263 (1988) 17284-90.
  ORGANISM  Klebsiella pneumoniae
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
            PATH: map00401  Novobiocin biosynthesis
ORTHOLOGY   KO: K00220  cyclohexadienyl dehydrogenase
GENES       ACI: ACIAD2222
            MLO: mll3535
            MES: Meso_3085
            SME: SMc00711(tyrC)
            ATU: Atu3611(tyrC)
            ATC: AGR_L_2429(tyrC)
            RLE: RL4337(tyrC)
            BME: BMEI0079
            BMF: BAB1_1989
            BMS: BR1988(tyrC)
            BMB: BruAb1_1964(tyrC)
            BRA: BRADO6464(tyrC)
            BBT: BBta_1182(tyrC)
            BHE: BH16210(tyrC)
            BQU: BQ13130(tyrC)
            XAU: Xaut_0393
            CCR: CC_2224
            SIL: SPO3176
            ZMO: ZMO0420(tyrC)
            GOX: GOX2251
            CDF: CD1839(tyrC)
STRUCTURES  PDB: 2F1K  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.43
            ExPASy - ENZYME nomenclature database: 1.3.1.43
            ExplorEnz - The Enzyme Database: 1.3.1.43
            ERGO genome analysis and discovery system: 1.3.1.43
            BRENDA, the Enzyme Database: 1.3.1.43
            CAS: 64295-75-6
///
ENTRY       EC 1.3.1.44                 Enzyme
NAME        trans-2-enoyl-CoA reductase (NAD+);
            trans-2-enoyl-CoA reductase (NAD+)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     acyl-CoA:NAD+ trans-2-oxidoreductase
REACTION    acyl-CoA + NAD+ = trans-didehydroacyl-CoA + NADH + H+ [RN:R00384]
ALL_REAC    R00384 > R01171
SUBSTRATE   acyl-CoA [CPD:C00040];
            NAD+ [CPD:C00003]
PRODUCT     trans-didehydroacyl-CoA [CPD:C00658];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The enzyme from Euglena gracilis acts on crotonoyl-CoA and, more
            slowly, on trans-hex-2-enoyl-CoA and trans-oct-2-enoyl-CoA.
REFERENCE   1  [PMID:3102464]
  AUTHORS   Inui H, Miyatake K, Nakano Y, Kitaoka S.
  TITLE     Purification and some properties of short chain-length specific
            trans-2-enoyl-CoA reductase in mitochondria of Euglena gracilis.
  JOURNAL   J. Biochem. (Tokyo). 100 (1986) 995-1000.
  ORGANISM  Euglena gracilis
PATHWAY     PATH: map00650  Butanoate metabolism
GENES       SPE: Spro_1949
            PPF: Pput_4497
            SBM: Shew185_1599
            SSE: Ssed_1547 Ssed_3538
            SPL: Spea_2676
            MMW: Mmwyl1_2865
            CBE: Cbei_2086
            FJO: Fjoh_3464
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.44
            ExPASy - ENZYME nomenclature database: 1.3.1.44
            ExplorEnz - The Enzyme Database: 1.3.1.44
            ERGO genome analysis and discovery system: 1.3.1.44
            BRENDA, the Enzyme Database: 1.3.1.44
            CAS: 77649-64-0
///
ENTRY       EC 1.3.1.45                 Enzyme
NAME        2'-hydroxyisoflavone reductase;
            NADPH:2'-hydroxyisoflavone oxidoreductase;
            isoflavone reductase;
            2',7-dihydroxy-4',5'-methylenedioxyisoflavone reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     vestitone:NADP+ oxidoreductase
REACTION    vestitone + NADP+ = 2'-hydroxyformononetin + NADPH + H+ [RN:R06562]
ALL_REAC    R06562;
            (other) R06563 R07747 R07751
SUBSTRATE   vestitone [CPD:C00786];
            NADP+ [CPD:C00006]
PRODUCT     2'-hydroxyformononetin [CPD:C02920];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     In the reverse reaction, a 2'-hydroxyisoflavone is reduced to an
            isoflavanone; 2'-hydroxypseudobaptigenin also acts. Involved in the
            biosynthesis of the pterocarpin phytoalexins medicarpin and
            maackiain.
REFERENCE   1
  AUTHORS   Tiemann, K., Hinderer, W. and Barz, W.
  TITLE     Isolation of NADPH:isoflavone oxidoreductase, a new enzyme of
            pterocarpan biosynthesis in cell suspensions of Cicer arietinum.
  JOURNAL   FEBS Lett. 213 (1987) 324-328.
  ORGANISM  Cicer arietinum
ORTHOLOGY   KO: K05281  2'-hydroxyisoflavone reductase
GENES       RLE: RL3032
            BCZ: BCZK2770
            FRA: Francci3_2035
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.45
            ExPASy - ENZYME nomenclature database: 1.3.1.45
            ExplorEnz - The Enzyme Database: 1.3.1.45
            ERGO genome analysis and discovery system: 1.3.1.45
            BRENDA, the Enzyme Database: 1.3.1.45
            CAS: 128449-69-4
///
ENTRY       EC 1.3.1.46                 Enzyme
NAME        biochanin-A reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     dihydrobiochanin-A:NADP+ Delta2-oxidoreductase
REACTION    dihydrobiochanin A + NADP+ = biochanin A + NADPH + H+ [RN:R02954]
ALL_REAC    R02954
SUBSTRATE   dihydrobiochanin A [CPD:C02675];
            NADP+ [CPD:C00006]
PRODUCT     biochanin A [CPD:C00814];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Some other isoflavones are reduced to the corresponding
            isoflavanones.
REFERENCE   1
  AUTHORS   Tiemann, K., Hinderer, W. and Barz, W.
  TITLE     Isolation of NADPH:isoflavone oxidoreductase, a new enzyme of
            pterocarpan biosynthesis in cell suspensions of Cicer arietinum.
  JOURNAL   FEBS Lett. 213 (1987) 324-328.
  ORGANISM  Fusarium javanicum
PATHWAY     PATH: map00943  Isoflavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.46
            ExPASy - ENZYME nomenclature database: 1.3.1.46
            ExplorEnz - The Enzyme Database: 1.3.1.46
            ERGO genome analysis and discovery system: 1.3.1.46
            BRENDA, the Enzyme Database: 1.3.1.46
            CAS: 112198-90-0
///
ENTRY       EC 1.3.1.47                 Enzyme
NAME        alpha-santonin 1,2-reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     1,2-dihydrosantonin:NAD(P)+ 1,2-oxidoreductase
REACTION    1,2-dihydrosantonin + NAD(P)+ = alpha-santonin + NAD(P)H + H+
            [RN:R03882 R03883]
ALL_REAC    R03882 R03883
SUBSTRATE   1,2-dihydrosantonin [CPD:C02771];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     alpha-santonin [CPD:C02206];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:3690421]
  AUTHORS   Naik U, Mavuinkurve S.
  TITLE     alpha-Santonin 1,2-reductase and its role in the formation of
            dihydrosantonin and lumisantonin by Pseudomonas cichorii S.
  JOURNAL   Can. J. Microbiol. 33 (1987) 658-62.
  ORGANISM  Pseudomonas cichorii S
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.47
            ExPASy - ENZYME nomenclature database: 1.3.1.47
            ExplorEnz - The Enzyme Database: 1.3.1.47
            ERGO genome analysis and discovery system: 1.3.1.47
            BRENDA, the Enzyme Database: 1.3.1.47
            CAS: 111070-23-6
///
ENTRY       EC 1.3.1.48                 Enzyme
NAME        15-oxoprostaglandin 13-oxidase;
            15-oxo-Delta13-prostaglandin reductase;
            Delta13-15-ketoprostaglandin reductase;
            15-ketoprostaglandin Delta13-reductase;
            prostaglandin Delta13-reductase;
            prostaglandin 13-reductase;
            15-ketoprostaglandin Delta13-reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (5Z)-(15S)-11alpha-hydroxy-9,15-dioxoprostanoate:NAD(P)+
            Delta13-oxidoreductase
REACTION    (5Z)-(15S)-11alpha-hydroxy-9,15-dioxoprostanoate + NAD(P)+ =
            (5Z)-(15S)-11alpha-hydroxy-9,15-dioxoprosta-13-enoate + NAD(P)H + H+
            [RN:R04556 R04557]
ALL_REAC    R04556 R04557
SUBSTRATE   (5Z)-(15S)-11alpha-hydroxy-9,15-dioxoprostanoate [CPD:C04671];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     (5Z)-(15S)-11alpha-hydroxy-9,15-dioxoprosta-13-enoate [CPD:C04707];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Reduces 15-oxoprostaglandins to 13,14-dihydro derivatives. The
            enzyme from placenta is specific for NAD+.
REFERENCE   1  [PMID:6290839]
  AUTHORS   Hansen HS.
  TITLE     Purification and assay of 15-ketoprostaglandin delta 13-reductase
            from bovine lung.
  JOURNAL   Methods. Enzymol. 86 (1982) 156-63.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:7132753]
  AUTHORS   Jarabak J.
  TITLE     Isolation and properties of a 15-ketoprostaglandin delta
            13-reductase from human placenta.
  JOURNAL   Methods. Enzymol. 86 (1982) 163-7.
  ORGANISM  human [GN:hsa]
STRUCTURES  PDB: 1V3T  1V3U  1V3V  2DM6  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.48
            ExPASy - ENZYME nomenclature database: 1.3.1.48
            ExplorEnz - The Enzyme Database: 1.3.1.48
            ERGO genome analysis and discovery system: 1.3.1.48
            BRENDA, the Enzyme Database: 1.3.1.48
            CAS: 57406-74-3
///
ENTRY       EC 1.3.1.49                 Enzyme
NAME        cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (+)-cis-3,4-dihydrophenanthrene-3,4-diol:NAD+ 3,4-oxidoreductase
REACTION    (+)-cis-3,4-dihydrophenanthrene-3,4-diol + NAD+ =
            phenanthrene-3,4-diol + NADH + H+ [RN:R04151]
ALL_REAC    R04151
SUBSTRATE   (+)-cis-3,4-dihydrophenanthrene-3,4-diol [CPD:C04468];
            NAD+ [CPD:C00003]
PRODUCT     phenanthrene-3,4-diol [CPD:C03164];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Nagao, K., Takizawa, N. and Kiyahara, H.
  TITLE     Purification and properties of cis-phenanthrene dihydrodiol
            dehydrogenase in Alcaligenes faecalis AFK2.
  JOURNAL   Agric. Biol. Chem. 52 (1988) 2621-2623.
  ORGANISM  Alcaligenes faecalis
PATHWAY     PATH: map00626  Naphthalene and anthracene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.49
            ExPASy - ENZYME nomenclature database: 1.3.1.49
            ExplorEnz - The Enzyme Database: 1.3.1.49
            ERGO genome analysis and discovery system: 1.3.1.49
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.49
            BRENDA, the Enzyme Database: 1.3.1.49
            CAS: 118390-61-7
///
ENTRY       EC 1.3.1.50       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: tetrahydroxynaphthalene reductase. Now EC 1.1.1.252
            tetrahydroxynaphthalene reductase (EC 1.3.1.50 created 1992, deleted
            1999)
STRUCTURES  PDB: 1YBV  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.50
            ExPASy - ENZYME nomenclature database: 1.3.1.50
            ExplorEnz - The Enzyme Database: 1.3.1.50
            ERGO genome analysis and discovery system: 1.3.1.50
            BRENDA, the Enzyme Database: 1.3.1.50
///
ENTRY       EC 1.3.1.51                 Enzyme
NAME        2'-hydroxydaidzein reductase;
            NADPH:2'-hydroxydaidzein oxidoreductase;
            HDR;
            2'-hydroxydihydrodaidzein:NADP+ 2'-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2'-hydroxy-2,3-dihydrodaidzein:NADP+ 2'-oxidoreductase
REACTION    2'-hydroxy-2,3-dihydrodaidzein + NADP+ = 2'-hydroxydaidzein + NADPH
            + H+ [RN:R03962]
ALL_REAC    R03962
SUBSTRATE   2'-hydroxy-2,3-dihydrodaidzein [CPD:C03567];
            NADP+ [CPD:C00006]
PRODUCT     2'-hydroxydaidzein [CPD:C02495];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     In the reverse reaction, the 2'-hydroxyisoflavone
            (2'-hydroxydaidzein) is reduced to an isoflavanone. Also acts on
            2'-hydroxyformononetin and to a small extent on 2'-hydroxygenistein.
            Involved in the biosynthesis of the phytoalexin glyceollin. The
            isoflavones biochanin A, daidzein and genestein as well as the
            flavonoids apigenin, kaempferol and quercetin do not act as
            substrates.
REFERENCE   1  [PMID:2306102]
  AUTHORS   Fischer D, Ebenau-Jehle C, Grisebach H.
  TITLE     Phytoalexin synthesis in soybean: purification and characterization
            of NADPH:2'-hydroxydaidzein oxidoreductase from elicitor-challenged
            soybean cell cultures.
  JOURNAL   Arch. Biochem. Biophys. 276 (1990) 390-5.
  ORGANISM  Glycine max [GN:egma]
PATHWAY     PATH: map00943  Isoflavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.51
            ExPASy - ENZYME nomenclature database: 1.3.1.51
            ExplorEnz - The Enzyme Database: 1.3.1.51
            ERGO genome analysis and discovery system: 1.3.1.51
            BRENDA, the Enzyme Database: 1.3.1.51
            CAS: 126125-01-7
///
ENTRY       EC 1.3.1.52                 Enzyme
NAME        2-methyl-branched-chain-enoyl-CoA reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-methyl-branched-chain-acyl-CoA:NAD+ 2-oxidoreductase
REACTION    2-methylbutanoyl-CoA + NAD+ = 2-methylcrotonoyl-CoA + NADH + H+
            [RN:R03169]
ALL_REAC    R03169;
            (other) R01728
SUBSTRATE   2-methylbutanoyl-CoA [CPD:C01033];
            NAD+ [CPD:C00003]
PRODUCT     2-methylcrotonoyl-CoA;
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD) from Ascaris suum. The reaction proceeds only
            in the presence of another flavoprotein ('electron-transferring
            flavoprotein').
REFERENCE   1  [PMID:3988734]
  AUTHORS   Komuniecki R, Fekete S, Thissen-Parra J.
  TITLE     Purification and characterization of the 2-methyl branched-chain
            Acyl-CoA dehydrogenase, an enzyme involved in NADH-dependent
            enoyl-CoA reduction in anaerobic mitochondria of the nematode,
            Ascaris suum.
  JOURNAL   J. Biol. Chem. 260 (1985) 4770-7.
  ORGANISM  Ascaris suum
REFERENCE   2  [PMID:2736251]
  AUTHORS   Komuniecki R, McCrury J, Thissen J, Rubin N.
  TITLE     Electron-transfer flavoprotein from anaerobic Ascaris suum
            mitochondria and its role in NADH-dependent 2-methyl branched-chain
            enoyl-CoA reduction.
  JOURNAL   Biochim. Biophys. Acta. 975 (1989) 127-31.
  ORGANISM  Ascaris suum
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.52
            ExPASy - ENZYME nomenclature database: 1.3.1.52
            ExplorEnz - The Enzyme Database: 1.3.1.52
            ERGO genome analysis and discovery system: 1.3.1.52
            BRENDA, the Enzyme Database: 1.3.1.52
            CAS: 122320-06-3
///
ENTRY       EC 1.3.1.53                 Enzyme
NAME        (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate
            dehydrogenase;
            (1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate:NAD+
            oxidoreductase
REACTION    (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate + NAD+ =
            3,4-dihydroxybenzoate + CO2 + NADH [RN:R01633]
ALL_REAC    R01633
SUBSTRATE   (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate
            [CPD:C06318];
            NAD+ [CPD:C00003]
PRODUCT     3,4-dihydroxybenzoate [CPD:C00230];
            CO2 [CPD:C00011];
            NADH [CPD:C00004]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires FeII.
REFERENCE   1
  AUTHORS   Saller, E., Laue, H.R., Schlafli Oppenberg, H.R. and Cook, A.M.
  TITLE     Purification and some properties of
            (1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase
            from Comamonas testosteroni T-2.
  JOURNAL   FEMS Microbiol. Lett. 130 (1996) 97-102.
  ORGANISM  Comamonas testosteroni
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.53
            ExPASy - ENZYME nomenclature database: 1.3.1.53
            ExplorEnz - The Enzyme Database: 1.3.1.53
            ERGO genome analysis and discovery system: 1.3.1.53
            BRENDA, the Enzyme Database: 1.3.1.53
            CAS: 162032-77-1
///
ENTRY       EC 1.3.1.54                 Enzyme
NAME        precorrin-6A reductase;
            precorrin-6X reductase;
            precorrin-6Y:NADP+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     precorrin-6B:NADP+ oxidoreductase
REACTION    precorrin-6B + NADP+ = precorrin-6A + NADPH + H+ [RN:R05150]
ALL_REAC    R05150;
            (other) R05812
SUBSTRATE   precorrin 6B [CPD:C06319];
            NADP+ [CPD:C00006]
PRODUCT     precorrin 6A [CPD:C06320];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:1732193]
  AUTHORS   Blanche F, Thibaut D, Famechon A, Debussche L, Cameron B, Crouzet J.
  TITLE     Precorrin-6x reductase from Pseudomonas denitrificans: purification
            and characterization of the enzyme and identification of the
            structural gene.
  JOURNAL   J. Bacteriol. 174 (1992) 1036-42.
  ORGANISM  Pseudomonas denitrificans
REFERENCE   2  [PMID:12195810]
  AUTHORS   Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
  TITLE     The biosynthesis of adenosylcobalamin (vitamin B12).
  JOURNAL   Nat. Prod. Rep. 19 (2002) 390-412.
  ORGANISM  Propionibacterium freundenreichii
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K05895  precorrin-6X reductase
GENES       STY: STY2231(cbiJ)
            STT: t0848(cbiJ)
            SPT: SPA0845(cbiJ)
            SEC: SC2034(cbiJ)
            STM: STM2026(cbiJ)
            YEN: YE2717(cbiJ)
            PLU: plu2990(cbiJ)
            PAE: PA2909
            PAU: PA14_26460(cobK)
            PAP: PSPA7_2245
            PPU: PP_4832(cobK)
            PPF: Pput_4710
            PST: PSPTO_4880
            PSB: Psyr_4420
            PSP: PSPPH_4463
            PFL: PFL_0654
            PFO: Pfl_0601
            PEN: PSEEN4874(cobK)
            PMY: Pmen_4569
            HHA: Hhal_1927
            HCH: HCH_06470(cobK)
            MMW: Mmwyl1_3377
            CVI: CV_1562(cbiJ)
            RSO: RSp0618(cbiJH)
            BMA: BMA1158(cobK)
            BMV: BMASAVP1_A1599(cobK)
            BML: BMA10299_A0260(cobK)
            BMN: BMA10247_0900(cobK)
            BXE: Bxe_B1248
            BVI: Bcep1808_1613
            BUR: Bcep18194_A4828
            BCN: Bcen_1197
            BCH: Bcen2424_1677
            BAM: Bamb_1577
            BPS: BPSL1756(cobK)
            BPM: BURPS1710b_2116(cobK)
            BPL: BURPS1106A_1971(cobK)
            BPD: BURPS668_1954(cobK)
            BTE: BTH_I2395(cobK)
            PCA: Pcar_0470
            MLO: mll1382
            SME: SMc03189(cobK)
            SMD: Smed_2814
            ATU: Atu2799(cobK)
            ATC: AGR_C_5078
            RET: RHE_PE00451(cobK)
            RLE: pRL110627(cobK)
            BME: BMEI0702
            BMF: BAB1_1319(cobK)
            BMS: BR1299(cobK)
            BMB: BruAb1_1300(cobK)
            BOV: BOV_1263(cobK)
            OAN: Oant_1886
            BJA: bll3268(cobK)
            BRA: BRADO4902(cobK)
            BBT: BBta_3149(cobK)
            RPA: RPA2087(cobK)
            RPB: RPB_3181
            RPC: RPC_1885
            RPD: RPD_2317
            RPE: RPE_2222
            XAU: Xaut_3281
            SIL: SPO2868(cobK)
            SIT: TM1040_2215
            RSP: RSP_2825(cobK)
            RSH: Rsph17029_1472
            RSQ: Rsph17025_1522
            JAN: Jann_2926
            RDE: RD1_3177(cobK) RD1_3822(cobK)
            PDE: Pden_2537
            NAR: Saro_0337
            RRU: Rru_A2988
            MAG: amb2641
            GKA: GK1803
            LMO: lmo1200
            LMF: LMOf2365_1209(cobK)
            LIN: lin1163
            LWE: lwe1157(cbiJ)
            SSA: SSA_0473
            CAC: CAC1381(cbiJ)
            CPE: CPE1219(cbiJ)
            CPF: CPF_1427(cobK)
            CPR: CPR_1233(cobK)
            CTC: CTC00740
            CNO: NT01CX_0574(cobK)
            CBO: CBO0950(cbiJ)
            CBA: CLB_0992(cobK)
            CBH: CLC_1006(cobK)
            CBF: CLI_1039(cobK)
            CKL: CKL_0729(cbiJ)
            CHY: CHY_0765(cobK)
            DSY: DSY4065(cobK)
            MTA: Moth_1095
            MTU: Rv2070c(cobK)
            MTC: MT2130(cobK)
            MBO: Mb2096c(cobK)
            MBB: BCG_2089c(cobK)
            MPA: MAP1815c(cobK)
            MAV: MAV_2427(cobK)
            MSM: MSMEG_3875(cobK)
            MVA: Mvan_0378
            MGI: Mflv_0359
            MMC: Mmcs_2485
            MKM: Mkms_2530
            MJL: Mjls_2522
            CDI: DIP1234(cobK)
            NFA: nfa31540(cobK)
            RHA: RHA1_ro00826(cobK)
            SCO: SCO3283(SCE39.33c)
            SMA: SAV1601(cobK)
            PAC: PPA0440
            NCA: Noca_2881
            TFU: Tfu_0310
            FRA: Francci3_1522
            FAL: FRAAL2334(cobK)
            SEN: SACE_5950(cobK)
            FNU: FN0950
            TDE: TDE0624
            SYN: slr0252
            SYW: SYNW1776
            SYC: syc1476_d(cobK)
            SYF: Synpcc7942_0021
            SYD: Syncc9605_0688
            SYE: Syncc9902_1670
            SYG: sync_2025(cobK)
            SYR: SynRCC307_0882(cobK)
            SYX: SynWH7803_0618(cobK)
            CYA: CYA_2390(cobK)
            CYB: CYB_0118(cobK)
            TEL: tlr1056
            ANA: all1780
            AVA: Ava_0256
            PMA: Pro0503(cobK)
            PMM: PMM0503
            PMT: PMT1264
            PMN: PMN2A_1836
            PMI: PMT9312_0504
            PMB: A9601_05601(cobK)
            PMC: P9515_05671(cobK)
            PMF: P9303_07381(cobK)
            PMG: P9301_05301(cobK)
            PME: NATL1_05611(cobK)
            TER: Tery_2739
            MJA: MJ0552
            MMP: MMP0599(cbiJ)
            MTH: MTH1002
            MST: Msp_1205(cbiJ)
            MSI: Msm_0896
            PTO: PTO0039 PTO0112
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.54
            ExPASy - ENZYME nomenclature database: 1.3.1.54
            ExplorEnz - The Enzyme Database: 1.3.1.54
            ERGO genome analysis and discovery system: 1.3.1.54
            BRENDA, the Enzyme Database: 1.3.1.54
            CAS: 137672-84-5
///
ENTRY       EC 1.3.1.55       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate
            dehydrogenase. Enzyme is identical to EC 1.3.1.25,
            1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (EC
            1.3.1.55 created 1999, deleted 2004)
GENES       BUR: Bcep18194_C7049
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.55
            ExPASy - ENZYME nomenclature database: 1.3.1.55
            ExplorEnz - The Enzyme Database: 1.3.1.55
            ERGO genome analysis and discovery system: 1.3.1.55
            BRENDA, the Enzyme Database: 1.3.1.55
///
ENTRY       EC 1.3.1.56                 Enzyme
NAME        cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase;
            2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     cis-3-phenylcyclohexa-3,5-diene-1,2-diol:NAD+ oxidoreductase
REACTION    cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ = biphenyl-2,3-diol
            + NADH + H+ [RN:R05239]
ALL_REAC    R05239;
            (other) R05241
SUBSTRATE   cis-3-phenylcyclohexa-3,5-diene-1,2-diol [CPD:C06589];
            NAD+ [CPD:C00003]
PRODUCT     biphenyl-2,3-diol [CPD:C02526];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Catalyses the second step in the biphenyl degradation pathway in
            bacteria.
REFERENCE   1  [PMID:8702262]
  AUTHORS   Sylvestre M, Hurtubise Y, Barriault D, Bergeron J, Ahmad D.
  TITLE     Characterization of active recombinant
            2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase from Comamonas
            testosteroni B-356 and sequence of the encoding gene (bphB).
  JOURNAL   Appl. Environ. Microbiol. 62 (1996) 2710-5.
  ORGANISM  Comamonas testosteroni
REFERENCE   2  [PMID:8048958]
  AUTHORS   Fukuda M, Yasukochi Y, Kikuchi Y, Nagata Y, Kimbara K, Horiuchi H,
            Takagi M, Yano K.
  TITLE     Identification of the bphA and bphB genes of Pseudomonas sp. strains
            KKS102 involved in degradation of biphenyl and polychlorinated
            biphenyls.
  JOURNAL   Biochem. Biophys. Res. Commun. 202 (1994) 850-6.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:8344527]
  AUTHORS   Hofer B, Eltis LD, Dowling DN, Timmis KN.
  TITLE     Genetic analysis of a Pseudomonas locus encoding a pathway for
            biphenyl/polychlorinated biphenyl degradation.
  JOURNAL   Gene. 130 (1993) 47-55.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00621  Biphenyl degradation
ORTHOLOGY   KO: K08690  cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase
GENES       BXE: Bxe_C1192(bphB)
            RHA: RHA1_ro08054(bphB1) RHA1_ro10126(bphB2)
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.56
            ExPASy - ENZYME nomenclature database: 1.3.1.56
            ExplorEnz - The Enzyme Database: 1.3.1.56
            ERGO genome analysis and discovery system: 1.3.1.56
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.56
            BRENDA, the Enzyme Database: 1.3.1.56
///
ENTRY       EC 1.3.1.57                 Enzyme
NAME        phloroglucinol reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     dihydrophloroglucinol:NADP+ oxidoreductase
REACTION    dihydrophloroglucinol + NADP+ = phloroglucinol + NADPH + H+
            [RN:R05308]
ALL_REAC    R05308
SUBSTRATE   dihydrophloroglucinol [CPD:C06719];
            NADP+ [CPD:C00006]
PRODUCT     phloroglucinol [CPD:C02183];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Involved in the gallate anaerobic degradation pathway in bacteria.
REFERENCE   1  [PMID:2925649]
  AUTHORS   Haddock JD, Ferry JG.
  TITLE     Purification and properties of phloroglucinol reductase from
            Eubacterium oxidoreducens G-41.
  JOURNAL   J. Biol. Chem. 264 (1989) 4423-7.
  ORGANISM  Eubacterium oxidoreducens
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.57
            ExPASy - ENZYME nomenclature database: 1.3.1.57
            ExplorEnz - The Enzyme Database: 1.3.1.57
            ERGO genome analysis and discovery system: 1.3.1.57
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.57
            BRENDA, the Enzyme Database: 1.3.1.57
///
ENTRY       EC 1.3.1.58                 Enzyme
NAME        2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     cis-2,3-dihydroxy-2,3-dihydro-p-cumate:NAD+ oxidoreductase
REACTION    cis-5,6-dihydroxy-4-isopropylcyclohexa-1,3-dienecarboxylate + NAD+ =
            2,3-dihydroxy-p-cumate + NADH + H+ [RN:R05240]
ALL_REAC    R05240
SUBSTRATE   cis-5,6-dihydroxy-4-isopropylcyclohexa-1,3-dienecarboxylate
            [CPD:C06579];
            NAD+ [CPD:C00003]
PRODUCT     2,3-dihydroxy-p-cumate [CPD:C06580];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Involved in the p-cymene degradation pathway in Pseudomonas putida.
REFERENCE   1  [PMID:8631713]
  AUTHORS   Eaton RW.
  TITLE     p-Cumate catabolic pathway in Pseudomonas putida Fl: cloning and
            characterization of DNA carrying the cmt operon.
  JOURNAL   J. Bacteriol. 178 (1996) 1351-62.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00621  Biphenyl degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.58
            ExPASy - ENZYME nomenclature database: 1.3.1.58
            ExplorEnz - The Enzyme Database: 1.3.1.58
            ERGO genome analysis and discovery system: 1.3.1.58
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.58
            BRENDA, the Enzyme Database: 1.3.1.58
///
ENTRY       EC 1.3.1.59       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: 1,2-dihydroxy-3-methyl-1,2-dihydrobenzoate
            dehydrogenase. No evidence in the paper cited that the enzyme
            exists. (EC 1.3.1.59 created 2000, deleted 2006)
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.59
            ExPASy - ENZYME nomenclature database: 1.3.1.59
            ExplorEnz - The Enzyme Database: 1.3.1.59
            ERGO genome analysis and discovery system: 1.3.1.59
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.59
            BRENDA, the Enzyme Database: 1.3.1.59
///
ENTRY       EC 1.3.1.60                 Enzyme
NAME        dibenzothiophene dihydrodiol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene:NAD+ oxidoreductase
REACTION    cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene + NAD+ =
            1,2-dihydroxydibenzothiophene + NADH + H+ [RN:R05310]
ALL_REAC    R05310
SUBSTRATE   cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene [CPD:C06721];
            NAD+ [CPD:C00003]
PRODUCT     1,2-dihydroxydibenzothiophene [CPD:C06722];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Involved in the dibenzothiophene degradation pathway in bacteria.
REFERENCE   1  [PMID:596875]
  AUTHORS   Laborde AL, Gibson DT.
  TITLE     Metabolism of dibenzothiophene by a Beijerinckia species.
  JOURNAL   Appl. Environ. Microbiol. 34 (1977) 783-90.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2  [PMID:8226631]
  AUTHORS   Denome SA, Stanley DC, Olson ES, Young KD.
  TITLE     Metabolism of dibenzothiophene and naphthalene in Pseudomonas
            strains: complete DNA sequence of an upper naphthalene catabolic
            pathway.
  JOURNAL   J. Bacteriol. 175 (1993) 6890-901.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.60
            ExPASy - ENZYME nomenclature database: 1.3.1.60
            ExplorEnz - The Enzyme Database: 1.3.1.60
            ERGO genome analysis and discovery system: 1.3.1.60
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.60
            BRENDA, the Enzyme Database: 1.3.1.60
///
ENTRY       EC 1.3.1.61                 Enzyme
NAME        terephthalate 1,2-cis-dihydrodiol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate:NAD+
            oxidoreductase (decarboxylating)
REACTION    cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate + NAD+ =
            3,4-dihydroxybenzoate + CO2 + NADH [RN:R01633]
ALL_REAC    R01633
SUBSTRATE   cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate
            [CPD:C06318];
            NAD+ [CPD:C00003]
PRODUCT     3,4-dihydroxybenzoate [CPD:C00230];
            CO2 [CPD:C00011];
            NADH [CPD:C00004]
COMMENT     Involved in the terephthalate degradation pathway in bacteria.
REFERENCE   1  [PMID:8565920]
  AUTHORS   Wang YZ, Zhou Y, Zylstra GJ.
  TITLE     Molecular analysis of isophthalate and terephthalate degradation by
            Comamonas testosteroni YZW-D.
  JOURNAL   Environ. Health. Perspect. 103 Suppl 5 (1995) 9-12.
  ORGANISM  Comamonas testosteroni
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.61
            ExPASy - ENZYME nomenclature database: 1.3.1.61
            ExplorEnz - The Enzyme Database: 1.3.1.61
            ERGO genome analysis and discovery system: 1.3.1.61
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.61
            BRENDA, the Enzyme Database: 1.3.1.61
///
ENTRY       EC 1.3.1.62                 Enzyme
NAME        pimeloyl-CoA dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     pimeloyl-CoA:NAD+ oxidoreductase
REACTION    pimeloyl-CoA + NAD+ = 6-carboxyhex-2-enoyl-CoA + NADH + H+
            [RN:R05311]
ALL_REAC    R05311
SUBSTRATE   pimeloyl-CoA [CPD:C01063];
            NAD+ [CPD:C00003]
PRODUCT     6-carboxyhex-2-enoyl-CoA [CPD:C06723];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Involved in the benzoate degradation (anaerobic) pathway in
            bacteria.
REFERENCE   1  [PMID:8180704]
  AUTHORS   Gallus C, Schink B.
  TITLE     Anaerobic degradation of pimelate by newly isolated denitrifying
            bacteria.
  JOURNAL   Microbiology. 140 ( Pt 2) (1994) 409-16.
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
ORTHOLOGY   KO: K04118  pimeloyl-CoA dehydrogenase
GENES       REU: Reut_B4559
            REH: H16_B0371(pimC) H16_B0372(pimD)
            EBA: ebA5669(pimD)
            RPC: RPC_2229
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.62
            ExPASy - ENZYME nomenclature database: 1.3.1.62
            ExplorEnz - The Enzyme Database: 1.3.1.62
            ERGO genome analysis and discovery system: 1.3.1.62
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.62
            BRENDA, the Enzyme Database: 1.3.1.62
///
ENTRY       EC 1.3.1.63                 Enzyme
NAME        2,4-dichlorobenzoyl-CoA reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4-chlorobenzoyl-CoA:NADP+ oxidoreductase (halogenating)
REACTION    4-chlorobenzoyl-CoA + NADP+ + HCl = 2,4-dichlorobenzoyl-CoA + NADPH
            + H+ [RN:R05276]
ALL_REAC    R05276
SUBSTRATE   4-chlorobenzoyl-CoA [CPD:C06387];
            NADP+ [CPD:C00006];
            HCl [CPD:C01327]
PRODUCT     2,4-dichlorobenzoyl-CoA [CPD:C06671];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Acts in the reverse direction to form part of the
            2,4-dichlorobenzoate degradation pathway in bacteria.
REFERENCE   1  [PMID:8626335]
  AUTHORS   Romanov V, Hausinger RP.
  TITLE     NADPH-dependent reductive ortho dehalogenation of
            2,4-dichlorobenzoic acid in Corynebacterium sepedonicum KZ-4 and
            Coryneform bacterium strainNTB-1 via 2,4-dichlorobenzoyl coenzyme A.
  JOURNAL   J. Bacteriol. 178 (1996) 2656-61.
  ORGANISM  Corynebacterium sepedonicum , Coryneform bacterium
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.63
            ExPASy - ENZYME nomenclature database: 1.3.1.63
            ExplorEnz - The Enzyme Database: 1.3.1.63
            ERGO genome analysis and discovery system: 1.3.1.63
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.63
            BRENDA, the Enzyme Database: 1.3.1.63
///
ENTRY       EC 1.3.1.64                 Enzyme
NAME        phthalate 4,5-cis-dihydrodiol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate:NAD+
            oxidoreductase
REACTION    cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD+ =
            4,5-dihydroxyphthalate + NADH + H+ [RN:R05275]
ALL_REAC    R05275
SUBSTRATE   cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate
            [CPD:C04783];
            NAD+ [CPD:C00003]
PRODUCT     4,5-dihydroxyphthalate [CPD:C03233];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Involved in the phthalate degradation pathway in bacteria.
REFERENCE   1  [PMID:3805038]
  AUTHORS   Batie CJ, LaHaie E, Ballou DP.
  TITLE     Purification and characterization of phthalate oxygenase and
            phthalate oxygenase reductase from Pseudomonas cepacia.
  JOURNAL   J. Biol. Chem. 262 (1987) 1510-8.
  ORGANISM  Pseudomonas cepacia
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.64
            ExPASy - ENZYME nomenclature database: 1.3.1.64
            ExplorEnz - The Enzyme Database: 1.3.1.64
            ERGO genome analysis and discovery system: 1.3.1.64
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.64
            BRENDA, the Enzyme Database: 1.3.1.64
///
ENTRY       EC 1.3.1.65                 Enzyme
NAME        5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline
            dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline:NAD+
            oxidoreductase
REACTION    5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline + NAD+ =
            5,6-dihydroxy-3-methyl-2-oxo-1,2-dihydroquinoline + NADH + H+
            [RN:R05312]
ALL_REAC    R05312
SUBSTRATE   5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline
            [CPD:C06726];
            NAD+ [CPD:C00003]
PRODUCT     5,6-dihydroxy-3-methyl-2-oxo-1,2-dihydroquinoline [CPD:C06725];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Acts in the reverse direction to form part of the 3-methylquinoline
            degradation pathway in bacteria.
REFERENCE   1  [PMID:8489738]
  AUTHORS   Schach S, Schwarz G, Fetzner S, Lingens F.
  TITLE     Microbial metabolism of quinoline and related compounds. XVII.
            Degradation of 3-methylquinoline by Comamonas testosteroni 63.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 374 (1993) 175-81.
  ORGANISM  Comamonas testosteroni
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.65
            ExPASy - ENZYME nomenclature database: 1.3.1.65
            ExplorEnz - The Enzyme Database: 1.3.1.65
            ERGO genome analysis and discovery system: 1.3.1.65
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.65
            BRENDA, the Enzyme Database: 1.3.1.65
///
ENTRY       EC 1.3.1.66                 Enzyme
NAME        cis-dihydroethylcatechol dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     cis-1,2-dihydro-3-ethylcatechol:NAD+ oxidoreductase
REACTION    cis-1,2-dihydro-3-ethylcatechol + NAD+ = 3-ethylcatechol + NADH + H+
            [RN:R05313]
ALL_REAC    R05313
SUBSTRATE   cis-1,2-dihydro-3-ethylcatechol [CPD:C06727];
            NAD+ [CPD:C00003]
PRODUCT     3-ethylcatechol [CPD:C06728];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Involved in the ethylbenzene degradation pathway in bacteria.
REFERENCE   1  [PMID:4699984]
  AUTHORS   Gibson DT, Gschwendt B, Yeh WK, Kobal VM.
  TITLE     Initial reactions in the oxidation of ethylbenzene by Pseudomonas
            putida.
  JOURNAL   Biochemistry. 12 (1973) 1520-8.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00642  Ethylbenzene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.66
            ExPASy - ENZYME nomenclature database: 1.3.1.66
            ExplorEnz - The Enzyme Database: 1.3.1.66
            ERGO genome analysis and discovery system: 1.3.1.66
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.66
            BRENDA, the Enzyme Database: 1.3.1.66
///
ENTRY       EC 1.3.1.67                 Enzyme
NAME        cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate
            dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate:NAD(P)+
            oxidoreductase (decarboxylating)
REACTION    cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate +
            NAD(P)+ = 4-methylcatechol + NAD(P)H + CO2 [RN:R05292 R05293]
ALL_REAC    R05292 R05293
SUBSTRATE   cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate
            [CPD:C06729];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     4-methylcatechol [CPD:C06730];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            CO2 [CPD:C00011]
COMMENT     Involved in the p-xylene degradation pathway in bacteria.
REFERENCE   1  [PMID:3711022]
  AUTHORS   Whited GM, McCombie WR, Kwart LD, Gibson DT.
  TITLE     Identification of cis-diols as intermediates in the oxidation of
            aromatic acids by a strain of Pseudomonas putida that contains a TOL
            plasmid.
  JOURNAL   J. Bacteriol. 166 (1986) 1028-39.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00622  Toluene and xylene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.67
            ExPASy - ENZYME nomenclature database: 1.3.1.67
            ExplorEnz - The Enzyme Database: 1.3.1.67
            ERGO genome analysis and discovery system: 1.3.1.67
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.67
            BRENDA, the Enzyme Database: 1.3.1.67
///
ENTRY       EC 1.3.1.68                 Enzyme
NAME        1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate:NAD+
            oxidoreductase (decarboxylating)
REACTION    1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate + NAD+ =
            3-methylcatechol + NADH + CO2 [RN:R05314]
ALL_REAC    R05314
SUBSTRATE   1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate [CPD:C06731];
            NAD+ [CPD:C00003]
PRODUCT     3-methylcatechol [CPD:C02923];
            NADH [CPD:C00004];
            CO2 [CPD:C00011]
COMMENT     Involved in the o-xylene degradation pathway in bacteria.
REFERENCE   1  [PMID:1371658]
  AUTHORS   Higson FK, Focht DD.
  TITLE     Degradation of 2-methylbenzoic acid by Pseudomonas cepacia MB2.
  JOURNAL   Appl. Environ. Microbiol. 58 (1992) 194-200.
  ORGANISM  Pseudomonas cepacia
PATHWAY     PATH: map00622  Toluene and xylene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.68
            ExPASy - ENZYME nomenclature database: 1.3.1.68
            ExplorEnz - The Enzyme Database: 1.3.1.68
            ERGO genome analysis and discovery system: 1.3.1.68
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.1.68
            BRENDA, the Enzyme Database: 1.3.1.68
///
ENTRY       EC 1.3.1.69                 Enzyme
NAME        zeatin reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     dihydrozeatin:NADP+ oxidoreductase
REACTION    dihydrozeatin + NADP+ = zeatin + NADPH + H+ [RN:R05702]
ALL_REAC    R05702
SUBSTRATE   dihydrozeatin [CPD:C02029];
            NADP+ [CPD:C00006]
PRODUCT     zeatin [CPD:C00371];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Previously classified erroneously as EC 1.1.1.242.
REFERENCE   1  [PMID:16666974]
  AUTHORS   Martin RC, Mok MC, Shaw G, Mok DW.
  TITLE     An Enzyme Mediating the Conversion of Zeatin to Dihydrozeatin in
            Phaseolus Embryos.
  JOURNAL   Plant. Physiol. 90 (1989) 1630-1635.
  ORGANISM  Phaseolus vulgaris
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.69
            ExPASy - ENZYME nomenclature database: 1.3.1.69
            ExplorEnz - The Enzyme Database: 1.3.1.69
            ERGO genome analysis and discovery system: 1.3.1.69
            BRENDA, the Enzyme Database: 1.3.1.69
            CAS: 123644-82-6
///
ENTRY       EC 1.3.1.70                 Enzyme
NAME        Delta14-sterol reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol:NADP+
            Delta14-oxidoreductase
REACTION    4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP+ =
            4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + NADPH + H+
            [RN:R05639]
ALL_REAC    R05639;
            (other) R07483
SUBSTRATE   4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol [CPD:C05108];
            NADP+ [CPD:C00006]
PRODUCT     4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol [CPD:C11455];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     This enzyme acts on a range of steroids with a 14(15)-double bond.
REFERENCE   1  [PMID:32908]
  AUTHORS   Bottema CK, Parks LW.
  TITLE     Delta14-sterol reductase in Saccharomyces cerevisiae.
  JOURNAL   Biochim. Biophys. Acta. 531 (1978) 301-7.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:6444198]
  AUTHORS   Paik YK, Trzaskos JM, Shafiee A, Gaylor JL.
  TITLE     Microsomal enzymes of cholesterol biosynthesis from lanosterol.
            Characterization, solubilization, and partial purification of
            NADPH-dependent delta 8,14-steroid 14-reductase.
  JOURNAL   J. Biol. Chem. 259 (1984) 13413-23.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K00222  delta14-sterol reductase
GENES       HSA: 7108(TM7SF2)
            MMU: 73166(Tm7sf2)
            RNO: 293688(Tm7sf2)
            CFA: 476027(TM7SF2)
            BTA: 282384(TM7SF2)
            XLA: 379527(MGC68849)
            ATH: AT3G52940(FK)
            OSA: 4326276
            SCE: YNL280C(ERG24)
            AGO: AGOS_AFR346W
            PIC: PICST_36016
            CGR: CAGL0I02970g
            SPO: SPBC16G5.18(erg24)
            ANI: AN4094.2
            AFM: AFUA_1G03150
            AOR: AO090009000362 AO090023000728
            CNE: CNA01070
            DDI: DDB_0191312 DDB_0232079
            TET: TTHERM_00394500
            TBR: Tb11.01.7170
            TCR: 507969.60
            LMA: LmjF32.2320
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.70
            ExPASy - ENZYME nomenclature database: 1.3.1.70
            ExplorEnz - The Enzyme Database: 1.3.1.70
            ERGO genome analysis and discovery system: 1.3.1.70
            BRENDA, the Enzyme Database: 1.3.1.70
///
ENTRY       EC 1.3.1.71                 Enzyme
NAME        Delta24(241)-sterol reductase;
            sterol Delta24(28)-methylene reductase;
            sterol Delta24(28)-reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     ergosterol:NADP+ Delta24(241)-oxidoreductase
REACTION    ergosterol + NADP+ = ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH
            + H+ [RN:R05641]
ALL_REAC    R05641;
            (other) R03676
SUBSTRATE   ergosterol [CPD:C01694];
            NADP+ [CPD:C00006]
PRODUCT     ergosta-5,7,22,24(241)-tetraen-3beta-ol;
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Acts on a range of steroids with a 24(241)-double bond.
REFERENCE   1  [PMID:14922]
  AUTHORS   Neal WD, Parks LW.
  TITLE     Sterol 24(28) methylene reductase in Saccharomyces cerevisiae.
  JOURNAL   J. Bacteriol. 129 (1977) 1375-8.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:10722850]
  AUTHORS   Zweytick D, Hrastnik C, Kohlwein SD, Daum G.
  TITLE     Biochemical characterization and subcellular localization of the
            sterol C-24(28) reductase, erg4p, from the yeast saccharomyces
            cerevisiae.
  JOURNAL   FEBS. Lett. 470 (2000) 83-7.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K00223  delta24(24(1))-sterol reductase
GENES       SCE: YGL012W(ERG4)
            AGO: AGOS_AGL087C
            PIC: PICST_29811
            CAL: CaO19_12834(CaO19.12834) CaO19_5379(CaO19.5379)
            CGR: CAGL0A00429g
            SPO: SPAC20G4.07c(sts1)
            ANI: AN5184.2
            AOR: AO090012000966
            CNE: CNC04470
            UMA: UM01498.1
            TCR: 506577.120 507709.90
            LMA: LmjF33.0680
            CBU: CBU_1206
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.71
            ExPASy - ENZYME nomenclature database: 1.3.1.71
            ExplorEnz - The Enzyme Database: 1.3.1.71
            ERGO genome analysis and discovery system: 1.3.1.71
            BRENDA, the Enzyme Database: 1.3.1.71
///
ENTRY       EC 1.3.1.72                 Enzyme
NAME        Delta24-sterol reductase;
            lanosterol Delta24-reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     sterol:NADP+ Delta24-oxidoreductase
REACTION    5alpha-cholest-7-en-3beta-ol + NADP+ =
            5alpha-cholesta-7,24-dien-3beta-ol + NADPH + H+ [RN:R05703]
ALL_REAC    R05703;
            (other) R01457 R07488 R07493 R07498 R07507
SUBSTRATE   5alpha-cholest-7-en-3beta-ol [CPD:C01189];
            NADP+ [CPD:C00006]
PRODUCT     5alpha-cholesta-7,24-dien-3beta-ol [CPD:C05439];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Acts on a range of steroids with a 24(25)-double bond, including
            lanosterol, desmosterol and zymosterol.
REFERENCE   1  [PMID:9291139]
  AUTHORS   Bae SH, Paik YK.
  TITLE     Cholesterol biosynthesis from lanosterol: development of a novel
            assay method and characterization of rat liver microsomal lanosterol
            delta 24-reductase.
  JOURNAL   Biochem. J. 326 ( Pt 2) (1997) 609-16.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K09828  delta24-sterol reductase
GENES       HSA: 1718(DHCR24)
            PTR: 456879(DHCR24)
            MMU: 74754(Dhcr24)
            RNO: 298298(Dhcr24)
            CFA: 489573(DHCR24)
            GGA: 424661(RCJMB04_27e12)
            XLA: 444688(MGC84360)
            XTR: 549554(dhcr24)
            DRE: 494102(dhcr24)
            SPU: 587262(LOC587262)
            ATH: AT3G19820(DWF1)
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.72
            ExPASy - ENZYME nomenclature database: 1.3.1.72
            ExplorEnz - The Enzyme Database: 1.3.1.72
            ERGO genome analysis and discovery system: 1.3.1.72
            BRENDA, the Enzyme Database: 1.3.1.72
///
ENTRY       EC 1.3.1.73                 Enzyme
NAME        1,2-dihydrovomilenine reductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     17-O-acetylnorajmaline:NADP+ oxidoreductase
REACTION    17-O-acetylnorajmaline + NADP+ = 1,2-dihydrovomilenine + NADPH + H+
            [RN:R05879]
ALL_REAC    R05879
SUBSTRATE   17-O-acetylnorajmaline [CPD:C11809];
            NADP+ [CPD:C00006]
PRODUCT     1,2-dihydrovomilenine [CPD:C11808];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Forms part of the ajmaline biosynthesis pathway.
REFERENCE   1  [PMID:12391554]
  AUTHORS   Gao S, von Schumann G, Stockigt J.
  TITLE     A newly-detected reductase from Rauvolfia closes a gap in the
            biosynthesis of the antiarrhythmic alkaloid ajmaline.
  JOURNAL   Planta. Med. 68 (2002) 906-11.
  ORGANISM  Rauvolfia serpentina, Rauvolfia msnnii, Rauvolfia mombasiana
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.73
            ExPASy - ENZYME nomenclature database: 1.3.1.73
            ExplorEnz - The Enzyme Database: 1.3.1.73
            ERGO genome analysis and discovery system: 1.3.1.73
            BRENDA, the Enzyme Database: 1.3.1.73
///
ENTRY       EC 1.3.1.74                 Enzyme
NAME        2-alkenal reductase;
            NAD(P)H-dependent alkenal/one oxidoreductase;
            NADPH:2-alkenal alpha,beta-hydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     n-alkanal:NAD(P)+ 2-oxidoreductase
REACTION    n-alkanal + NAD(P)+ = alk-2-enal + NAD(P)H + H+ [RN:R07349 R07350]
ALL_REAC    R07349 R07350
SUBSTRATE   n-alkanal [CPD:C15596];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     alk-2-enal [CPD:C15597];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Highly specific for 4-hydroxynon-2-enal and non-2-enal. 2-Alkenals
            of shorter chain have lower affinities. Exhibits high activities
            also for 2-alkenones such as but-3-en-2-one and pent-3-en-2-one.
            Inactive with cyclohex-2-en-1-one and 12-oxophytodienoic acid.
            Involved in the detoxication of alpha,beta-unsaturated aldehydes and
            ketones.
REFERENCE   1  [PMID:12514241]
  AUTHORS   Mano J, Torii Y, Hayashi S, Takimoto K, Matsui K, Nakamura K, Inze
            D, Babiychuk E, Kushnir S, Asada K.
  TITLE     The NADPH:quinone oxidoreductase P1-zeta-crystallin in Arabidopsis
            catalyzes the alpha,beta-hydrogenation of 2-alkenals: detoxication
            of the lipid peroxide-derived reactive aldehydes.
  JOURNAL   Plant. Cell. Physiol. 43 (2002) 1445-55.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   2  [PMID:11524419]
  AUTHORS   Dick RA, Kwak MK, Sutter TR, Kensler TW.
  TITLE     Antioxidative function and substrate specificity of
            NAD(P)H-dependent alkenal/one oxidoreductase. A new role for
            leukotriene B4 12-hydroxydehydrogenase/15-oxoprostaglandin
            13-reductase.
  JOURNAL   J. Biol. Chem. 276 (2001) 40803-10.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K08070  2-alkenal reductase
GENES       HSA: 22949(LTB4DH)
            PTR: 467369(LOC467369)
            MMU: 67103(Ltb4dh)
            RNO: 192227(Ltb4dh)
            SSC: 397678(LTB4DH)
            DRE: 494108(ltb4dh)
            ATH: AT1G26320 AT1G65560 AT3G03080 AT3G59845 AT5G16960
                 AT5G16970(AT-AER) AT5G16980 AT5G16990 AT5G17000 AT5G37940
                 AT5G37980 AT5G38000
            SPE: Spro_0692 Spro_0710 Spro_0789 Spro_1160 Spro_1220 Spro_3623
                 Spro_3914 Spro_4230 Spro_4352 Spro_4353 Spro_4664
            ASU: Asuc_0405 Asuc_0496 Asuc_0868 Asuc_1092 Asuc_1160 Asuc_1952
            PPF: Pput_0876 Pput_1025 Pput_1228 Pput_4291 Pput_4424 Pput_4593
                 Pput_5099
            PMY: Pmen_0888 Pmen_1345 Pmen_1471 Pmen_1713 Pmen_3507 Pmen_3624
                 Pmen_3779
            PRW: PsycPRwf_0128 PsycPRwf_1580 PsycPRwf_1633 PsycPRwf_1725
                 PsycPRwf_1803 PsycPRwf_1875 PsycPRwf_2371
            SBM: Shew185_0517 Shew185_0699 Shew185_0700 Shew185_2382
                 Shew185_3303 Shew185_3411 Shew185_3675
            SSE: Ssed_0743 Ssed_0744 Ssed_2867 Ssed_3409 Ssed_3471 Ssed_3673
            SPL: Spea_1492 Spea_3080 Spea_3137 Spea_3301 Spea_3598 Spea_3599
            MMW: Mmwyl1_1102 Mmwyl1_1393 Mmwyl1_2285 Mmwyl1_2404 Mmwyl1_2909
                 Mmwyl1_3964
            AHA: AHA_3611
            BUR: Bcep18194_B1551 Bcep18194_B1574 Bcep18194_B1605
                 Bcep18194_B2291
            GUR: Gura_0211 Gura_0716 Gura_0879 Gura_1490 Gura_2824 Gura_3127
                 Gura_4295
            AFW: Anae109_0073 Anae109_0094 Anae109_0641 Anae109_1154
                 Anae109_1272 Anae109_1518 Anae109_1523 Anae109_2022
                 Anae109_2046 Anae109_2233 Anae109_2264 Anae109_2683
                 Anae109_4474
            PLA: Plav_0943 Plav_1414 Plav_2461 Plav_2762 Plav_3574 Plav_3617
            SMD: Smed_0040 Smed_0637 Smed_1014 Smed_1182 Smed_2014 Smed_3389
            OAN: Oant_0758 Oant_0790 Oant_0926 Oant_1797 Oant_1982 Oant_2667
                 Oant_3627 Oant_3862
            XAU: Xaut_0350 Xaut_0824 Xaut_0826 Xaut_1661 Xaut_1810 Xaut_3516
                 Xaut_4475 Xaut_4771
            RSQ: Rsph17025_0887 Rsph17025_2297 Rsph17025_2507 Rsph17025_2766
                 Rsph17025_3870
            SWI: Swit_1250 Swit_2354 Swit_2387 Swit_5274
            ACR: Acry_0051 Acry_0468 Acry_1317 Acry_1324 Acry_1353 Acry_1646
                 Acry_2497
            RRU: Rru_A0474
            BCY: Bcer98_2249 Bcer98_2424 Bcer98_3036 Bcer98_3040 Bcer98_4001
            SAJ: SaurJH9_1352 SaurJH9_1634 SaurJH9_1638 SaurJH9_1783
            SAH: SaurJH1_1378 SaurJH1_1668 SaurJH1_1672 SaurJH1_1818
            LRE: Lreu_0479 Lreu_0706
            CBE: Cbei_0109 Cbei_0379 Cbei_0830 Cbei_1214 Cbei_2555 Cbei_4545
            AMT: Amet_0285 Amet_2545 Amet_2660 Amet_3044 Amet_3048 Amet_4751
            CSC: Csac_1752 Csac_1847 Csac_2001 Csac_2048 Csac_2141 Csac_2307
            KRA: Krad_1014 Krad_1484 Krad_1499 Krad_3090 Krad_3493 Krad_4061
                 Krad_4233
            STP: Strop_2377
            FJO: Fjoh_0019 Fjoh_0445 Fjoh_1850 Fjoh_2631 Fjoh_4942 Fjoh_5039
            DEB: DehaBAV1_0919 DehaBAV1_1096 DehaBAV1_1195 DehaBAV1_1208
            RRS: RoseRS_0531 RoseRS_1881 RoseRS_2119 RoseRS_3025 RoseRS_3246
                 RoseRS_3460 RoseRS_3714
            RCA: Rcas_1284 Rcas_1750 Rcas_2149 Rcas_3236 Rcas_3537 Rcas_3734
                 Rcas_4392
            TPT: Tpet_0097 Tpet_0278 Tpet_0347 Tpet_0544 Tpet_0935
            TME: Tmel_0071 Tmel_0674 Tmel_1128 Tmel_1797
            FNO: Fnod_0454 Fnod_0969 Fnod_1007 Fnod_1209
            MMZ: MmarC7_1410
            MVN: Mevan_0093 Mevan_1400
            IHO: Igni_1419
            MSE: Msed_0657
STRUCTURES  PDB: 2DM6  2J3J  2J3K  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.74
            ExPASy - ENZYME nomenclature database: 1.3.1.74
            ExplorEnz - The Enzyme Database: 1.3.1.74
            ERGO genome analysis and discovery system: 1.3.1.74
            BRENDA, the Enzyme Database: 1.3.1.74
            CAS: 9032-20-6
///
ENTRY       EC 1.3.1.75                 Enzyme
NAME        divinyl chlorophyllide a 8-vinyl-reductase;
            [4-vinyl]chlorophyllide a reductase;
            4VCR
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     chlorophyllide-a:NADP+ oxidoreductase
REACTION    chlorophyllide a + NADP+ = divinyl chlorophyllide a + NADPH + H+
            [RN:R06272]
ALL_REAC    R06272;
            (other) R06896
SUBSTRATE   chlorophyllide a [CPD:C02139];
            NADP+ [CPD:C00006]
PRODUCT     divinyl chlorophyllide a [CPD:C11832];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also reduces divinyl protochlorophyllide to protochlorophyllide in
            some species, providing an alternative pathway.
REFERENCE   1
  AUTHORS   Tripathy, B.C. and Rebeiz, C.A.
  TITLE     Chloroplast biogenesis 60. Conversion of divinyl protochlorophyllide
            to monovinyl protochlorophyllide in green(ing) barley, a dark
            monovinyl/light divinyl plant species.
  JOURNAL   Plant Physiol. 87 (1988) 89-94.
  ORGANISM  Hordeum vulgare [GN:ehvu], Cucumis sativus
REFERENCE   2  [PMID:1390630]
  AUTHORS   Parham R, Rebeiz CA.
  TITLE     Chloroplast biogenesis: [4-vinyl] chlorophyllide a reductase is a
            divinyl chlorophyllide a-specific, NADPH-dependent enzyme.
  JOURNAL   Biochemistry. 31 (1992) 8460-4.
  ORGANISM  Cucumis sativus
REFERENCE   3  [PMID:8678296]
  AUTHORS   Parham R, Rebeiz CA.
  TITLE     Chloroplast biogenesis 72: a [4-vinyl]chlorophyllide a reductase
            assay using divinyl chlorophyllide a as an exogenous substrate.
  JOURNAL   Anal. Biochem. 231 (1995) 164-9.
  ORGANISM  Hordeum vulgare [GN:ehvu], Cucumis sativus, Zea mays [GN:ezma]
REFERENCE   4  [PMID:11488624]
  AUTHORS   Kolossov VL, Rebeiz CA.
  TITLE     Chloroplast biogenesis 84: solubilization and partial purification
            of membrane-bound [4-vinyl]chlorophyllide a reductase from etiolated
            barley leaves.
  JOURNAL   Anal. Biochem. 295 (2001) 214-9.
  ORGANISM  Hordeum vulgare [GN:ehvu], Cucumis sativus
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.75
            ExPASy - ENZYME nomenclature database: 1.3.1.75
            ExplorEnz - The Enzyme Database: 1.3.1.75
            ERGO genome analysis and discovery system: 1.3.1.75
            BRENDA, the Enzyme Database: 1.3.1.75
///
ENTRY       EC 1.3.1.76                 Enzyme
NAME        precorrin-2 dehydrogenase;
            Met8p;
            SirC;
            CysG
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     precorrin-2:NAD+ oxidoreductase
REACTION    precorrin-2 + NAD+ = sirohydrochlorin + NADH + H+ [RN:R03947]
ALL_REAC    R03947
SUBSTRATE   precorrin 2 [CPD:C02463];
            NAD+ [CPD:C00003]
PRODUCT     sirohydrochlorin [CPD:C05778];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     This enzyme catalyses the second of three steps leading to the
            formation of siroheme from uroporphyrinogen III. The first step
            involves the donation of two S-adenosyl-L-methionine-derived methyl
            groups to carbons 2 and 7 of uroporphyrinogen III to form
            precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and
            the third step involves the chelation of ferrous iron to
            sirohydrochlorin to form siroheme (EC 4.99.1.4, sirohydrochlorin
            ferrochelatase). In Saccharomyces cerevisiae, the last two steps are
            carried out by a single bifunctional enzyme, Met8p. In some
            bacteria, steps 1-3 are catalysed by a single multifunctional
            protein called CysG, whereas in Bacillus megaterium, three separate
            enzymes carry out each of the steps, with SirC being responsible for
            the above reaction.
REFERENCE   1  [PMID:11980703]
  AUTHORS   Schubert HL, Raux E, Brindley AA, Leech HK, Wilson KS, Hill CP,
            Warren MJ.
  TITLE     The structure of Saccharomyces cerevisiae Met8p, a bifunctional
            dehydrogenase and ferrochelatase.
  JOURNAL   EMBO. J. 21 (2002) 2068-75.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:12195810]
  AUTHORS   Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
  TITLE     The biosynthesis of adenosylcobalamin (vitamin B12).
  JOURNAL   Nat. Prod. Rep. 19 (2002) 390-412.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], Salmonella enterica
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K02303  precorrin-2 dehydrogenase
GENES       CME: CMB055C
            SCE: YBR213W(MET8)
            AGO: AGOS_AAR152W
            CAL: CaO19_6780(CaO19.6780)
            CGR: CAGL0K06677g
            SPO: SPAC4D7.06c
            ANI: AN6710.2
            AFM: AFUA_7G05680
            AOR: AO090005000430
            CNE: CNF00750
            UMA: UM00458.1
            ECO: b3368(cysG)
            ECJ: JW3331(cysG)
            ECE: Z4729(cysG)
            ECS: ECs4219
            ECC: c4144(cysG)
            ECI: UTI89_C3872(cysG)
            ECP: ECP_3459
            ECV: APECO1_3088(cysG)
            ECW: EcE24377A_3838(cysG)
            ECX: EcHS_A3564(cysG)
            STY: STY4319(cysG)
            STT: t4028(cysG)
            SPT: SPA3343(cysG)
            SEC: SC3411(cysG)
            STM: STM3477(cysG)
            YPE: YPO0158(cysG) YPO3367(cysG)
            YPK: y3941(cysG)
            YPM: YP_0160(cysG1)
            YPA: YPA_2776 YPA_3311
            YPN: YPN_0726 YPN_3907
            YPS: YPTB0764(cysG) YPTB3743(cysG)
            YPI: YpsIP31758_3305(cysG2) YpsIP31758_3959(cysG1)
            SFL: SF3387(cysG)
            SFX: S4376(cysG)
            SFV: SFV_3374(cysG)
            SSN: SSON_3499(cysG)
            SBO: SBO_3350(cysG)
            SDY: SDY_3530(cysG)
            ECA: ECA3544(cysG1) ECA4081(cysG2)
            PLU: plu0708(cysG)
            BUC: BU425(cysG)
            SGL: SG0520
            BFL: Bfl161(cysG)
            BPN: BPEN_166(cysG)
            MSU: MS1254(cysG)
            XFA: XF0832
            XFT: PD1840(cysG)
            XCC: XCC2003(cysG) XCC3181(cysG)
            XCB: XC_0983 XC_2181
            XCV: XCV2089 XCV3458(cysG)
            XAC: XAC2159(cysG) XAC3340(cysG)
            XOO: XOO3102(cysG) XOO3408(cysG)
            XOM: XOO_2947(XOO2947) XOO_3208(XOO3208)
            VCH: VC1363
            VVU: VV1_2702
            VVY: VV1558
            VPA: VP1619
            VFI: VF1531
            PPR: PBPRA1425 PBPRA2524 PBPRA3312 PBPRB0870(cobA2)
            PAE: PA2611(cysG)
            PPU: PP_3999(cobA-2)
            PST: PSPTO_3344(cysG)
            PSB: Psyr_3174
            PSP: PSPPH_3088(cysG)
            PFL: PFL_3875
            PFO: Pfl_3581
            PEN: PSEEN2217(cysG)
            PAR: Psyc_1065(cysG)
            ACI: ACIAD2934(cysG)
            SON: SO_3108
            SDN: Sden_3717
            SHN: Shewana3_1441
            PHA: PSHAa0213(cysG)
            PAT: Patl_0417
            MCA: MCA2089(cysG)
            TCX: Tcr_1160
            NOC: Noc_0863
            AEH: Mlg_1679
            HCH: HCH_02450(cysG)
            ABO: ABO_1295(cysG)
            AHA: AHA_2578 AHA_3568 AHA_4121
            BCI: BCI_0215(cysG)
            VOK: COSY_0254(cysG)
            NME: NMB1156 NMB1194
            NMA: NMA1367(cysG)
            CVI: CV_0813(cobA2)
            BPE: BP1055(cysG)
            BPA: BPP1151(cysG)
            BBR: BB1367(cysG)
            POL: Bpro_2765
            NEU: NE0532(cysG)
            NET: Neut_1002
            NMU: Nmul_A2313
            TBD: Tbd_2471
            MFA: Mfla_0652
            WSU: WS1003(cysG)
            DVU: DVU1463
            DDE: Dde_2023
            LIP: LI0320(cysG)
            ADE: Adeh_3154
            SAT: SYN_02276
            SFU: Sfum_1588
            MLO: mll3232
            MES: Meso_3989
            SME: SMc01053(cysG)
            ATU: Atu1454(cysG) Atu3899(cysG)
            ATC: AGR_C_2683 AGR_L_1897
            RET: RHE_CH01958(cysG)
            RLE: RL2288(cysG2)
            BME: BMEI1768
            BMF: BAB1_0179(cysG)
            BMS: BR0179(cysG)
            BMB: BruAb1_0175(cysG)
            BJA: blr1477
            BRA: BRADO1065(cysG)
            BBT: BBta_6982(cysG)
            RPA: RPA4215(cysG)
            RPB: RPB_1399
            RPC: RPC_4015
            RPD: RPD_1379
            RPE: RPE_1763
            NWI: Nwi_2762
            CCR: CC_0024
            RDE: RD1_2964(cysG) RD1_4164(cysG)
            MMR: Mmar10_0347
            HNE: HNE_0322(cysG)
            GOX: GOX2065
            GBE: GbCGDNIH1_0735
            RRU: Rru_A1933
            BSU: BG13382(ylnF)
            BHA: BH1497
            BAN: BA1447 BA2142
            BAR: GBAA1447 GBAA2142
            BAA: BA_1968 BA_2638
            BAT: BAS1337 BAS1993
            BCE: BC1428 BC2132
            BCA: BCE_1551
            BCZ: BCZK1311(cysG) BCZK1945
            BTK: BT9727_1310(cysG) BT9727_1966
            BLI: BL02289(sirA)
            BLD: BLi01784(ylnF)
            BPU: BPUM_1462
            OIH: OB1657
            GKA: GK0404
            SAU: SA2412
            SAV: SAV2619
            SAM: MW2539
            SAR: SAR2697
            SAS: SAS2505
            SAC: SACOL2638
            SAB: SAB2493c
            SAA: SAUSA300_2553
            SAO: SAOUHSC_02945
            SAJ: SaurJH9_2642
            SAH: SaurJH1_2697
            SEP: SE2177
            SER: SERP2188
            SHA: SH0417
            SSP: SSP2404
            LMO: lmo1141
            LMF: LMOf2365_1148
            LIN: lin1105
            LWE: lwe1099
            SSA: SSA_0483
            CAC: CAC0096(hemW)
            CPE: CPE1436
            CPR: CPR_1423
            CTC: CTC00726
            CKL: CKL_2909(sirC)
            DSY: DSY2227(cysG)
            MTU: Rv2847c(cysG)
            MTC: MT2913(cysG)
            MBO: Mb2872c(cysG)
            MPA: MAP2916c(cysG2)
            MMC: Mmcs_2074
            NFA: nfa40770(cysG)
            SCO: SCO1553(SCL11.09c)
            SMA: SAV6796(cysG)
            TFU: Tfu_2221
            FAL: FRAAL1357(cysG)
            FNU: FN0539
            LIL: LA4217
            LIC: LIC13368(cysG)
            LBJ: LBJ_2838(cysG)
            LBL: LBL_0233(cysG)
            CTE: CT2239
            CCH: Cag_1943
            PLT: Plut_0049
            TTH: TTC0311
            TTJ: TTHA0670
            AAE: aq_1237(cysG)
            MJA: MJ0140
            MMP: MMP0089
            MAC: MA0576(cysG)
            MBA: Mbar_A1461
            MMA: MM_1740
            MBU: Mbur_1230
            MTH: MTH1013
            MSI: Msm_0968
            MKA: MK1495(cysG_1)
            AFU: AF1592
            HAL: VNG1775C
            HMA: rrnAC1709(hemX)
            HWA: HQ3335A(cysG)
            NPH: NP4500A(cysG1)
            TAC: Ta0652
            TVO: TVN0924
            APE: APE_1491.1
            STO: ST0211
            SAI: Saci_0776
            PAI: PAE0585
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.76
            ExPASy - ENZYME nomenclature database: 1.3.1.76
            ExplorEnz - The Enzyme Database: 1.3.1.76
            ERGO genome analysis and discovery system: 1.3.1.76
            BRENDA, the Enzyme Database: 1.3.1.76
///
ENTRY       EC 1.3.1.77                 Enzyme
NAME        anthocyanidin reductase;
            AtANR;
            MtANR
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     flavan-3-ol:NAD(P)+ oxidoreductase
REACTION    a flavan-3-ol + 2 NAD(P)+ = an anthocyanidin + 2 NAD(P)H + H+
            [RN:R07351 R07352]
ALL_REAC    R07352 > R06541 R06542 R06543;
            R07351
SUBSTRATE   flavan-3-ol;
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     anthocyanidin [CPD:C02003];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Forms 2,3-cis-flavan-3-ols. The isomeric 2,3-trans-flavan-3-ols are
            formed from flavan-3,4-diols by EC 1.17.1.3 leucoanthocyanidin
            reductase. While the enzyme from the legume Medicago truncatula
            (MtANR) uses both NADPH and NADH as reductant, that from the
            crucifer Arabidopsis thaliana (AtANR) uses only NADPH. Also, while
            the substrate preference of MtANR is
            cyanidin>pelargonidin>delphinidin, the reverse preference is found
            with AtANR.
REFERENCE   1  [PMID:12532018]
  AUTHORS   Xie DY, Sharma SB, Paiva NL, Ferreira D, Dixon RA.
  TITLE     Role of anthocyanidin reductase, encoded by BANYULS in plant
            flavonoid biosynthesis.
  JOURNAL   Science. 299 (2003) 396-9.
  ORGANISM  Arabidopsis thaliana [GN:ath], Medicago truncatula [GN:emtr]
REFERENCE   2  [PMID:14725861]
  AUTHORS   Xie DY, Sharma SB, Dixon RA.
  TITLE     Anthocyanidin reductases from Medicago truncatula and Arabidopsis
            thaliana.
  JOURNAL   Arch. Biochem. Biophys. 422 (2004) 91-102.
  ORGANISM  Arabidopsis thaliana [GN:ath], Medicago truncatula [GN:emtr]
PATHWAY     PATH: map00941  Flavonoid biosynthesis
ORTHOLOGY   KO: K08695  anthocyanidin reductase
GENES       ATH: AT1G61720(BAN)
            OSA: 4337100
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.77
            ExPASy - ENZYME nomenclature database: 1.3.1.77
            ExplorEnz - The Enzyme Database: 1.3.1.77
            ERGO genome analysis and discovery system: 1.3.1.77
            BRENDA, the Enzyme Database: 1.3.1.77
            CAS: 93389-48-1
///
ENTRY       EC 1.3.1.78                 Enzyme
NAME        arogenate dehydrogenase (NADP+);
            arogenic dehydrogenase (ambiguous);
            pretyrosine dehydrogenase (ambiguous);
            TyrAAT1;
            TyrAAT2;
            TyrAa
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-arogenate:NADP+ oxidoreductase (decarboxylating)
REACTION    L-arogenate + NADP+ = L-tyrosine + NADPH + CO2 [RN:R00733]
ALL_REAC    R00733
SUBSTRATE   L-arogenate [CPD:C00826];
            NADP+ [CPD:C00006]
PRODUCT     L-tyrosine [CPD:C00082];
            NADPH [CPD:C00005];
            CO2 [CPD:C00011]
COMMENT     Unlike EC 1.3.1.43 (arogenate dehydrogenase) and EC 1.3.1.79
            [arogenate dehydrogenase (NAD(P)+)], this enzyme has a strict
            requirement for NADP+. The enzyme from Synechocystis sp. PCC 6803
            and the isoform TyrAAT1 cannot use prephenate as a substrate, while
            the isoform TyrAAT2 can use it only very poorly [3,4].
REFERENCE   1
  AUTHORS   Byng, G., Whitaker, R., Flick, C. and Jensen, R.A.
  TITLE     Enzymology of L-tyrosine biosynthesis in corn (Zea mays).
  JOURNAL   Phytochemistry 20 (1981) 1289-1292.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   2
  AUTHORS   Gaines, C.G., Byng, G.S., Whitaker, R.J. and Jensen, R.A.
  TITLE     L-Tyrosine regulation and biosynthesis via arogenate dehydrogenase
            in suspension-cultured cells of Nicotiana silvestris Speg. et Comes.
  JOURNAL   Planta 156 (1982) 233-240.
  ORGANISM  Nicotiana silvestris
REFERENCE   3  [PMID:12354100]
  AUTHORS   Ishikawa T, Hirayama J, Kobayashi Y, Todo T.
  TITLE     Zebrafish CRY represses transcription mediated by CLOCK-BMAL
            heterodimer without inhibiting its binding to DNA.
  JOURNAL   Genes. Cells. 7 (2002) 1073-86.
REFERENCE   4  [PMID:15171683]
  AUTHORS   Bonner CA, Jensen RA, Gander JE, Keyhani NO.
  TITLE     A core catalytic domain of the TyrA protein family: arogenate
            dehydrogenase from Synechocystis.
  JOURNAL   Biochem. J. 382 (2004) 279-91.
  ORGANISM  Synechocystis sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.78
            ExPASy - ENZYME nomenclature database: 1.3.1.78
            ExplorEnz - The Enzyme Database: 1.3.1.78
            ERGO genome analysis and discovery system: 1.3.1.78
            BRENDA, the Enzyme Database: 1.3.1.78
            CAS: 64295-75-6
///
ENTRY       EC 1.3.1.79                 Enzyme
NAME        arogenate dehydrogenase [NAD(P)+];
            arogenic dehydrogenase (ambiguous);
            cyclohexadienyl dehydrogenase;
            pretyrosine dehydrogenase (ambiguous)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-arogenate:NAD(P)+ oxidoreductase (decarboxylating)
REACTION    L-arogenate + NAD(P)+ = L-tyrosine + NAD(P)H + CO2 [RN:R00732
            R00733]
ALL_REAC    R00732 R00733
SUBSTRATE   L-arogenate [CPD:C00826];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     L-tyrosine [CPD:C00082];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            CO2 [CPD:C00011]
COMMENT     See also EC 1.3.1.12 (prephenate dehydrogenase), EC 1.3.1.43
            (arogenate dehydrogenase), and EC 1.3.1.78 [arogenate dehydrogenase
            (NADP+)].
REFERENCE   1  [PMID:2939643]
  AUTHORS   Connelly JA, Conn EE.
  TITLE     Tyrosine biosynthesis in Sorghum bicolor: isolation and regulatory
            properties of arogenate dehydrogenase.
  JOURNAL   Z. Naturforsch. [C]. 41 (1986) 69-78.
  ORGANISM  Sorghum bicolor [GN:esbi]
REFERENCE   2  [PMID:3600376]
  AUTHORS   Bonner C, Jensen R.
  TITLE     Arogenate dehydrogenase.
  JOURNAL   Methods. Enzymol. 142 (1987) 488-94.
  ORGANISM  Sorghum bicolor [GN:esbi], Nicotiana silvestris , Phenylobacterium
            immobile , Streptomyces phaeochromogenes , Zea mays [GN:ezma],
            Euglena gracilis , Vigna radiata , Corynebacterium glutamicum ,
            Brevibacterium flavum
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.1.79
            ExPASy - ENZYME nomenclature database: 1.3.1.79
            ExplorEnz - The Enzyme Database: 1.3.1.79
            ERGO genome analysis and discovery system: 1.3.1.79
            BRENDA, the Enzyme Database: 1.3.1.79
            CAS: 64295-75-6
///
ENTRY       EC 1.3.1.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With NAD+ or NADP+ as acceptor
REACTION    (1) Propanoyl-CoA + NADP+ <=> Propenoyl-CoA + NADPH [RN:R00919];
            (2) 5-(3'-Carboxy-3'-oxopropenyl)-4,6-dihydroxypicolinate + NADPH
            <=> 5-(3'-Carboxy-3'-oxopropyl)-4,6-dihydroxypicolinate + NADP+
            [RN:R04910];
            (3) 2,5-Dichloro-2,5-cyclohexadiene-1,4-diol + NAD+ <=>
            2,5-Dichlorohydroquinone + NADH [RN:R05243];
            (4) cis-2,3-Dihydrodiol
            1,1,1-Trichloro-2,2-bis(4'-chlorophenyl)ethane + NAD+ <=>
            2,3-Dihydroxy 1,1,1-Trichloro-2,2-bis(4'-chlorophenyl)ethane + NADH
            + H+ [RN:R05395];
            (5) cis-2,3-Dihydrodiol
            1,1,1-Trichloro-2,2-bis(4'-chlorophenyl)ethane + NADP+ <=>
            2,3-Dihydroxy 1,1,1-Trichloro-2,2-bis(4'-chlorophenyl)ethane + NADPH
            + H+ [RN:R05396];
            (6) 3,6-Dichloro-cis-1,2-dihydroxycyclohexa-3,5-diene + NAD+ <=>
            3,6-Dichlorocatechol + NADH + H+ [RN:R05397];
            (7) p-Coumaroyl-CoA <=> Isoliquiritigenin [RN:R06568];
            (8) cis-3-(Carboxy-ethyl)-3,5-cyclo-hexadiene-1,2-diol + NAD+ <=>
            3-(2,3-Dihydroxyphenyl)propanoate + NADH + H+ [RN:R06784];
            (9) cis-3-(3-Carboxyethenyl)-3,5-cyclohexadiene-1,2-diol + NAD+ <=>
            trans-2,3-Dihydroxycinnamate + NADH + H+ [RN:R06785];
            (10) (2E)-Octadecenoyl-[acp] + NADH + H+ <=> Stearoyl-[acyl-carrier
            protein] + NAD+ [RN:R07765];
            (11) (+)-(3S,4R)-cis-3,4-Dihydroxy-3,4-dihydrofluorene <=>
            3,4-Dihydroxyfluorene + 2 H+ [RN:R07804]
SUBSTRATE   Propanoyl-CoA [CPD:C00100];
            NADP+ [CPD:C00006];
            5-(3'-Carboxy-3'-oxopropenyl)-4,6-dihydroxypicolinate [CPD:C05641];
            NADPH [CPD:C00005];
            2,5-Dichloro-2,5-cyclohexadiene-1,4-diol [CPD:C06599];
            NAD+ [CPD:C00003];
            cis-2,3-Dihydrodiol 1,1,1-Trichloro-2,2-bis(4'-chlorophenyl)ethane
            [CPD:C06649];
            3,6-Dichloro-cis-1,2-dihydroxycyclohexa-3,5-diene [CPD:C07093];
            p-Coumaroyl-CoA [CPD:C00223];
            cis-3-(Carboxy-ethyl)-3,5-cyclo-hexadiene-1,2-diol [CPD:C11588];
            cis-3-(3-Carboxyethenyl)-3,5-cyclohexadiene-1,2-diol [CPD:C12622]
PRODUCT     Propenoyl-CoA [CPD:C00894];
            NADPH [CPD:C00005];
            5-(3'-Carboxy-3'-oxopropyl)-4,6-dihydroxypicolinate [CPD:C05656];
            NADP+ [CPD:C00006];
            2,5-Dichlorohydroquinone [CPD:C06600];
            NADH [CPD:C00004];
            2,3-Dihydroxy 1,1,1-Trichloro-2,2-bis(4'-chlorophenyl)ethane
            [CPD:C06650];
            H+ [CPD:C00080];
            3,6-Dichlorocatechol [CPD:C07094];
            Isoliquiritigenin [CPD:C08650];
            3-(2,3-Dihydroxyphenyl)propanoate [CPD:C04044];
            trans-2,3-Dihydroxycinnamate [CPD:C12623]
///
ENTRY       EC 1.3.2.1        Obsolete  Enzyme
NAME        Transferred to 1.3.99.2
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With a cytochrome as acceptor
COMMENT     Transferred entry: now EC 1.3.99.2 butyryl-CoA dehydrogenase (EC
            1.3.2.1 created 1961, deleted 1964)
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.2.1
            ExPASy - ENZYME nomenclature database: 1.3.2.1
            ExplorEnz - The Enzyme Database: 1.3.2.1
            ERGO genome analysis and discovery system: 1.3.2.1
            BRENDA, the Enzyme Database: 1.3.2.1
///
ENTRY       EC 1.3.2.2        Obsolete  Enzyme
NAME        Transferred to 1.3.99.3
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With a cytochrome as acceptor
COMMENT     Transferred entry: now EC 1.3.99.3 acyl-CoA dehydrogenase (EC
            1.3.2.2 created 1961, deleted 1964)
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.2.2
            ExPASy - ENZYME nomenclature database: 1.3.2.2
            ExplorEnz - The Enzyme Database: 1.3.2.2
            ERGO genome analysis and discovery system: 1.3.2.2
            BRENDA, the Enzyme Database: 1.3.2.2
///
ENTRY       EC 1.3.2.3                  Enzyme
NAME        L-galactonolactone dehydrogenase;
            galactonolactone dehydrogenase;
            L-galactono-gamma-lactone dehydrogenase;
            L-galactono-gamma-lactone:ferricytochrome-c oxidoreductase;
            GLDHase;
            GLDase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With a cytochrome as acceptor
SYSNAME     L-galactono-1,4-lactone:ferricytochrome-c oxidoreductase
REACTION    (1) L-galactono-1,4-lactone + 2 ferricytochrome c = L-ascorbate + 2
            ferrocytochrome c + 2 H+ [RN:R00640];
            (2) L-ascorbate + 2 ferricytochrome c = L-dehydroascorbate + 2
            ferrocytochrome c + 2 H+ (spontaneous) [RN:R07679]
ALL_REAC    R00640 R07679
SUBSTRATE   L-galactono-1,4-lactone [CPD:C01115];
            ferricytochrome c [CPD:C00125];
            L-ascorbate [CPD:C00072]
PRODUCT     L-ascorbate [CPD:C00072];
            ferrocytochrome c [CPD:C00126];
            H+ [CPD:C00080];
            L-dehydroascorbate [CPD:C05422]
COMMENT     This enzyme catalyses the final step in the biosynthesis of
            L-ascorbic acid in higher plants and in nearly all higher animals
            with the exception of primates and some birds [5]. The enzyme is
            very specific for its substrate L-galactono-1,4-lactone as
            D-galactono-gamma-lactone, D-gulono-gamma-lactone,
            L-gulono-gamma-lactone, D-erythronic-gamma-lactone,
            D-xylonic-gamma-lactone, L-mannono-gamma-lactone, D-galactonate,
            D-glucuronate and D-gluconate are not substrates [5]. FAD, NAD+,
            NADP+ and O2 (cf. EC 1.3.3.12, L-galactonolactone oxidase) cannot
            act as electron acceptor [5].
REFERENCE   1
  AUTHORS   Mapson, L.W. and Breslow, E.
  TITLE     Properties of partially purified L-galactono-gamma-lactone
            dehydrogenase.
  JOURNAL   Biochem. J. 65 (1957) 29.
REFERENCE   2  [PMID:13126087]
  AUTHORS   MAPSON LW, ISHERWOOD FA, CHEN YT.
  TITLE     Biological synthesis of L-ascorbic acid: the conversion of
            L-galactono-gamma-lactone into L-ascorbic acid by plant
            mitochondria.
  JOURNAL   Biochem. J. 56 (1954) 21-8.
  ORGANISM  Pisum sativum
REFERENCE   3  [PMID:13126085]
  AUTHORS   ISHERWOOD FA, CHEN YT, MAPSON LW.
  TITLE     Synthesis of L-ascorbic acid in plants and animals.
  JOURNAL   Biochem. J. 56 (1954) 1-15.
REFERENCE   4  [PMID:7775377]
  AUTHORS   Oba K, Ishikawa S, Nishikawa M, Mizuno H, Yamamoto T.
  TITLE     Purification and properties of L-galactono-gamma-lactone
            dehydrogenase, a key enzyme for ascorbic acid biosynthesis, from
            sweet potato roots.
  JOURNAL   J. Biochem. (Tokyo). 117 (1995) 120-4.
REFERENCE   5  [PMID:9374475]
  AUTHORS   Ostergaard J, Persiau G, Davey MW, Bauw G, Van Montagu M.
  TITLE     Isolation of a cDNA coding for L-galactono-gamma-lactone
            dehydrogenase, an enzyme involved in the biosynthesis of ascorbic
            acid in plants. Purification, characterization, cDNA cloning, and
            expression in yeast.
  JOURNAL   J. Biol. Chem. 272 (1997) 30009-16.
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K00225  L-galactono-1,4-lactone dehydorogenase
GENES       ATH: AT3G47930(ATGLDH)
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.2.3
            ExPASy - ENZYME nomenclature database: 1.3.2.3
            ExplorEnz - The Enzyme Database: 1.3.2.3
            ERGO genome analysis and discovery system: 1.3.2.3
            BRENDA, the Enzyme Database: 1.3.2.3
            CAS: 9029-02-1
///
ENTRY       EC 1.3.3.1                  Enzyme
NAME        dihydroorotate oxidase;
            DHOdehase;
            dihydroorotate dehydrogenase;
            dihydoorotic acid dehydrogenase;
            (DHO) dehydrogenase;
            4,5-L-dihydroorotate:oxygen oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With oxygen as acceptor
SYSNAME     (S)-dihydroorotate:oxygen oxidoreductase
REACTION    (S)-dihydroorotate + O2 = orotate + H2O2 [RN:R01867]
ALL_REAC    R01867
SUBSTRATE   (S)-dihydroorotate [CPD:C00337];
            O2 [CPD:C00007]
PRODUCT     orotate [CPD:C00295];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016];
            FMN [CPD:C00061]
COMMENT     A flavoprotein (FAD, FMN). Ferricyanide can act as acceptor.
REFERENCE   1  [PMID:13825167]
  AUTHORS   FRIEDMANN HC, VENNESLAND B.
  TITLE     Crystalline dihydroorotic dehydrogenase.
  JOURNAL   J. Biol. Chem. 235 (1960) 1526-32.
  ORGANISM  Zymobacterium oroticum
REFERENCE   2  [PMID:4380263]
  AUTHORS   Taylor WH, Taylor ML, Eames DF.
  TITLE     Two functionally different dihydroorotic dehydrogenases in bacteria.
  JOURNAL   J. Bacteriol. 91 (1966) 2251-6.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K00226  dihydroorotate oxidase
GENES       HSA: 1723(DHODH)
            MMU: 56749(Dhodh)
            RNO: 65156(Dhodh)
            CFA: 610755(DHODH)
            XLA: 432093(LOC432093)
            SPU: 589543(LOC589543)
            DME: Dmel_CG9741(Dhod)
            CEL: W02D3.2
            ATH: AT5G23300(PYRD)
            OSA: 4337396
            CME: CMC027C
            SCE: YKL216W(URA1)
            AGO: AGOS_ACL035C
            PIC: PICST_55711(URA1)
            CGR: CAGL0M12881g
            SPO: SPAC57A10.12c(ura3)
            ANI: AN5909.2
            AOR: AO090026000542
            UMA: UM03215.1
            PFA: PFF0160c
            TAN: TA11695
            TPV: TP02_0171
            TBR: Tb927.5.3830
            TCR: 507091.40 508375.50 511643.20 511923.120
            LMA: LmjF16.0530
            ECO: b0945(pyrD)
            ECJ: JW0928(pyrD)
            ECE: Z1294(pyrD)
            ECS: ECs1029
            ECC: c1081(pyrD)
            ECI: UTI89_C1010(pyrD)
            ECP: ECP_0950
            ECV: APECO1_50(pyrD)
            ECW: EcE24377A_1060(pyrD)
            ECX: EcHS_A1054
            STY: STY1079(pyrD)
            STT: t1862(pyrD)
            SPT: SPA1792(pyrD)
            SEC: SC1011(pyrD)
            STM: STM1058(pyrD)
            YPE: YPO1415(pyrD)
            YPK: y2755(pyrD)
            YPM: YP_1178(pyrD)
            YPA: YPA_0710
            YPN: YPN_2562
            YPP: YPDSF_2280
            YPS: YPTB1439(pyrD)
            YPI: YpsIP31758_2555(pyrD)
            SFL: SF0946(pyrD)
            SFX: S1011(pyrD)
            SFV: SFV_0954(pyrD)
            SSN: SSON_0949(pyrD)
            SBO: SBO_2286(pyrD)
            SDY: SDY_0918(pyrD)
            ECA: ECA2538(pyrD)
            PLU: plu1758(pyrD) plu3917
            BUC: BU362(pyrD)
            BAS: BUsg350(pyrD)
            WBR: WGLp131(pyrD)
            SGL: SG1018
            ENT: Ent638_1457
            SPE: Spro_1740
            HIN: HI1401(pyrD)
            HIT: NTHI1745(pyrD)
            HIP: CGSHiEE_04690
            HIQ: CGSHiGG_00985
            HDU: HD1626(pyrD)
            PMU: PM0617(pyrD)
            MSU: MS1035(pyrD)
            APL: APL_0774(pyrD)
            ASU: Asuc_1385
            XFA: XF2571
            XFT: PD1952(pyrD)
            XCC: XCC1788(pyrD)
            XCB: XC_2448
            XCV: XCV1835(pyrD)
            XAC: XAC1805(pyrD)
            XOO: XOO2237(pyrD)
            XOM: XOO_2102(XOO2102)
            VCH: VC1491
            VCO: VC0395_A1098(pyrD)
            VVU: VV1_2637
            VVY: VV1654
            VPA: VP1601
            VFI: VF1285
            PPR: PBPRA1767
            PAE: PA3050(pyrD)
            PAU: PA14_24640(pyrD)
            PAP: PSPA7_2087(pyrD)
            PPU: PP_2095(pyrD)
            PPF: Pput_3645
            PST: PSPTO_2309(pyrD)
            PSB: Psyr_2106
            PSP: PSPPH_2077(pyrD)
            PFL: PFL_1877(pyrD)
            PFO: Pfl_1786
            PEN: PSEEN1755(pyrD)
            PMY: Pmen_3011
            PAR: Psyc_1284(pyrD)
            PCR: Pcryo_1101
            PRW: PsycPRwf_0934
            ACI: ACIAD1321(pyrD)
            SON: SO_2592(pyrD)
            SDN: Sden_1730
            SFR: Sfri_2220
            SAZ: Sama_1593
            SBL: Sbal_2439
            SBM: Shew185_2432
            SLO: Shew_1810
            SPC: Sputcn32_2194
            SSE: Ssed_2475
            SPL: Spea_1943
            SHE: Shewmr4_1681
            SHM: Shewmr7_1756
            SHN: Shewana3_1786
            SHW: Sputw3181_1815
            ILO: IL1280(pyrD)
            CPS: CPS_2800(pyrD)
            PHA: PSHAa1669(pyrD)
            PAT: Patl_2003
            SDE: Sde_1750
            PIN: Ping_2299
            MAQ: Maqu_1037
            CBU: CBU_0971(pyrD)
            CBD: COXBU7E912_1077(pyrD)
            LPN: lpg1821(pyrD)
            LPF: lpl1785(pyrD)
            LPP: lpp1784(pyrD)
            MCA: MCA1242(pyrD)
            FTU: FTT1647c(pyrD)
            FTF: FTF1647c(pyrD)
            FTL: FTL_0046
            FTH: FTH_0046(pyrD)
            FTN: FTN_0036(pyrD)
            TCX: Tcr_1950
            NOC: Noc_2822
            AEH: Mlg_1463
            HHA: Hhal_0211
            HCH: HCH_04965(pyrD)
            CSA: Csal_1342
            ABO: ABO_1003(pyrD)
            MMW: Mmwyl1_1738
            AHA: AHA_2287(pyrD)
            DNO: DNO_0669(pyrD)
            BCI: BCI_0409(pyrD)
            VOK: COSY_0006(pyrD)
            NME: NMB0221
            NMA: NMA0042(pyrD)
            NMC: NMC0218(pyrD)
            NGO: NGO1761
            CVI: CV_1812(pyrD) CV_3551(pydA)
            RSO: RSc1619(pyrD)
            REU: Reut_A1317
            REH: H16_A1401(pyrD)
            RME: Rmet_1213
            BMA: BMA1253(pyrD)
            BMV: BMASAVP1_A1736(pyrD)
            BML: BMA10299_A0394(pyrD)
            BMN: BMA10247_0768(pyrD)
            BXE: Bxe_A2507
            BVI: Bcep1808_1518
            BUR: Bcep18194_A4696
            BCN: Bcen_1074
            BCH: Bcen2424_1554
            BAM: Bamb_1455
            BPS: BPSL1866(pyrD)
            BPM: BURPS1710b_1978(pyrD)
            BPL: BURPS1106A_1825(pyrD)
            BPD: BURPS668_1809(pyrD)
            BTE: BTH_I2511(pyrD)
            PNU: Pnuc_0741
            BPE: BP3442(pyrD)
            BPA: BPP3540(pyrD)
            BBR: BB3975(pyrD)
            RFR: Rfer_2205
            POL: Bpro_2858
            PNA: Pnap_2617
            AAV: Aave_2455
            AJS: Ajs_2132
            VEI: Veis_1935
            MPT: Mpe_A2138
            HAR: HEAR2444(pyrD)
            MMS: mma_2513
            NEU: NE2221(pyrD)
            NET: Neut_0646
            NMU: Nmul_A2706
            EBA: ebA4888(pyrD)
            AZO: azo2210(pyrD)
            DAR: Daro_1164
            TBD: Tbd_0645
            MFA: Mfla_0506
            HPY: HP1011(pyrD)
            HPJ: jhp0412(pyrD)
            HPA: HPAG1_0435
            HHE: HH1624(pyrD)
            HAC: Hac_1115(pyrD)
            WSU: WS2219(pyrD)
            TDN: Tmden_1224
            CJE: Cj0804(pyrD)
            CJR: CJE0895(pyrD)
            CJJ: CJJ81176_0825(pyrD)
            CJU: C8J_0755(pyrD)
            CJD: JJD26997_1206(pyrD)
            CFF: CFF8240_0786(pyrD)
            CCV: CCV52592_1140(pyrD)
            CHA: CHAB381_0581(pyrD)
            CCO: CCC13826_0118(pyrD) CCC13826_1143
            ABU: Abu_0876(pyrD)
            NIS: NIS_0701(pyrD)
            SUN: SUN_0811(pyrD)
            GSU: GSU1755(pyrD)
            GME: Gmet_1841
            PCA: Pcar_1296
            DVU: DVU3316(pyrD)
            DDE: Dde_0056
            LIP: LI0712(pyrD)
            BBA: Bd0715(pyrD)
            DPS: DP3015
            ADE: Adeh_1294
            AFW: Anae109_2471
            MXA: MXAN_3028(pyrD)
            SAT: SYN_02848 SYN_02850
            SFU: Sfum_2850
            WOL: WD1239(pyrD)
            WBM: Wbm0098
            AMA: AM273(pyrD)
            APH: APH_1013(pyrD)
            ERU: Erum1810(pyrD)
            ERW: ERWE_CDS_01800(dhoD)
            ERG: ERGA_CDS_01750(dhoD)
            ECN: Ecaj_0178
            ECH: ECH_0940(pyrD)
            NSE: NSE_0179(pyrD)
            PUB: SAR11_0209(pyrD)
            MLO: mll5681
            MES: Meso_0094
            SME: SMc02245(pyrD)
            SMD: Smed_0161
            ATU: Atu0486(pyrD)
            ATC: AGR_C_861(dhoD)
            RET: RHE_CH00540(pyrD) RHE_CH03278(ypch01135)
            RLE: RL0572
            BME: BMEI1611
            BMF: BAB1_0341(pyrD)
            BMS: BR0311(pyrD)
            BMB: BruAb1_0337(pyrD)
            BOV: BOV_0325(pyrD)
            OAN: Oant_0404
            BJA: blr1140(pyrD)
            BRA: BRADO6742(pyrD)
            BBT: BBta_0793(pyrD)
            RPA: RPA0797(uraI)
            RPB: RPB_3115 RPB_4622
            RPC: RPC_0755
            RPD: RPD_0788
            RPE: RPE_0721
            NWI: Nwi_0464
            NHA: Nham_0555
            BHE: BH03870(pyrD)
            BQU: BQ02890(pyrD)
            BBK: BARBAKC583_0293(pyrD)
            XAU: Xaut_0056
            CCR: CC_0528
            SIL: SPO2907(pyrD)
            SIT: TM1040_1550
            RSP: RSP_0957(pyrD)
            RSH: Rsph17029_2617
            RSQ: Rsph17025_3012
            JAN: Jann_2963
            RDE: RD1_3961
            MMR: Mmar10_0518
            HNE: HNE_3488(pyrD)
            NAR: Saro_0193
            SAL: Sala_0680
            SWI: Swit_2920
            ELI: ELI_12815
            GBE: GbCGDNIH1_1881
            ACR: Acry_1961
            RRU: Rru_A0514
            MAG: amb3890
            MGM: Mmc1_3426
            ABA: Acid345_0389 Acid345_0729
            BSU: BG10718(pyrDI)
            BHA: BH2534(pyrD)
            BAN: BA4023(pyrD)
            BAR: GBAA4023(pyrD)
            BAA: BA_4494
            BAT: BAS3735
            BCE: BC3884 BC3885
            BCA: BCE_3929(pyrD)
            BCZ: BCZK3643(pyrD) BCZK3644(pyrK)
            BTK: BT9727_3626(pyrD) BT9727_3627(pyrK)
            BLI: BL02278(pyrD)
            BLD: BLi01774(pyrD)
            BCL: ABC2331(pyrDI) ABC2332(pyrDII)
            BAY: RBAM_015370
            BPU: BPUM_1452 BPUM_1453
            OIH: OB1493(pyrD)
            GKA: GK1154(pyrD)
            SAU: SA2375
            SAV: SAV2589
            SAM: MW2509
            SAR: SAR2669
            SAS: SAS2475
            SAC: SACOL2606(pyrD)
            SAB: SAB2464
            SAA: SAUSA300_2526(pyrD)
            SAO: SAOUHSC_02909
            SAJ: SaurJH9_2611
            SAH: SaurJH1_2665
            SEP: SE2132
            SER: SERP2144(pyrD)
            SHA: SH0471
            SSP: SSP0278
            LMO: lmo1833(pyrD)
            LMF: LMOf2365_1861(pyrD)
            LIN: lin1947(pyrD)
            LWE: lwe1852(pyrD) lwe1853(pyrDII)
            LLA: L182555(pydB) L192589(pydA)
            LLC: LACR_1469 LACR_1644
            LLM: llmg_0952(pyrDA) llmg_1105(pyrK) llmg_1106(pyrDB)
            SPY: SPy_1432(pyrD)
            SPZ: M5005_Spy_1165(pyrD)
            SPM: spyM18_1441
            SPG: SpyM3_1091(pyrD)
            SPS: SPs0774
            SPH: MGAS10270_Spy1236(pyrD)
            SPI: MGAS10750_Spy1273(pyrD)
            SPJ: MGAS2096_Spy1237(pyrD)
            SPK: MGAS9429_Spy1214(pyrD)
            SPF: SpyM50695(pyrD)
            SPA: M6_Spy1191
            SPB: M28_Spy1159(pyrD)
            SPN: SP_0764 SP_0964
            SPR: spr0672(pyrDA) spr0866(pyrD)
            SPD: SPD_0665(pyrDa) SPD_0852(pyrDb)
            SAG: SAG0507(pyrDA)
            SAN: gbs0553
            SAK: SAK_0657(pyrD)
            SMU: SMU.1223(pyrDB) SMU.595(pyrD)
            STC: str0955(pyrDb) str1207(pyrDa)
            STL: stu0955(pyrDb) stu1207(pyrDa)
            SSA: SSA_0373(pyrDA) SSA_1242(pyrD)
            SGO: SGO_0277(pyrA) SGO_1255(pyrD) SGO_1256
            LPL: lp_2699(pyrD)
            LJO: LJ1281
            LAC: LBA1384(pyrD)
            LSA: LSA0446 LSA0956(pyrDA) LSA0957(pyrDB)
            LSL: LSL_0194(pyrD)
            LDB: Ldb1530(pyrD2) Ldb2114(pyrD1)
            LBU: LBUL_1421 LBUL_1955
            LCA: LSEI_1451 LSEI_1732
            EFA: EF0285(pyrD-1) EF1714(pyrD-2)
            OOE: OEOE_0264
            STH: STH1260
            CAC: CAC2650(pyrD)
            CPE: CPE1178(pyrD)
            CPF: CPF_1382(pyrD)
            CPR: CPR_1197(pyrD)
            CTC: CTC00930 CTC02379
            CNO: NT01CX_0391 NT01CX_0392 NT01CX_0467
            CDF: CD0186(pyrD) CD2077(pyrD)
            CBO: CBO3236(pyrD)
            CBA: CLB_3273(pyrD)
            CBH: CLC_3147(pyrD)
            CBF: CLI_3375(pyrD)
            CKL: CKL_2399(pyrD1) CKL_3356(pyrD2)
            CHY: CHY_1497(pyrD)
            DSY: DSY2857
            SWO: Swol_1279
            TTE: TTE1530(pyrD)
            MTA: Moth_2127
            MPE: MYPE7860(pyrD)
            MTU: Rv2139(pyrD)
            MTC: MT2197(pyrD)
            MBO: Mb2163(pyrD)
            MBB: BCG_2156(pyrD)
            MLE: ML1293(pyrD)
            MPA: MAP1883(pyrD)
            MAV: MAV_2353(pyrD)
            MSM: MSMEG_4198(pyrD)
            MVA: Mvan_3487
            MGI: Mflv_3039
            MMC: Mmcs_3162
            CGL: NCgl1461(cgl1518)
            CGB: cg1713(pyrD)
            CEF: CE1643(pyrD)
            CDI: DIP1264(pyrD)
            CJK: jk0365(pyrD2) jk0959(pyrD1)
            NFA: nfa29160(pyrD)
            RHA: RHA1_ro00890
            SCO: SCO1482(pyrD)
            SMA: SAV6868(pyrD)
            TWH: TWT238(pyrD)
            TWS: TW532(pyrD)
            LXX: Lxx15100(pyrD)
            CMI: CMM_1846(pyrD)
            ART: Arth_2221
            AAU: AAur_2219(pyrD)
            PAC: PPA0161 PPA1002
            NCA: Noca_2432
            TFU: Tfu_0927 Tfu_1059
            FRA: Francci3_1185
            FAL: FRAAL1902
            KRA: Krad_3268
            SEN: SACE_2136(pyrD)
            STP: Strop_1857
            BLO: BL0789(pyrD) BL1213
            BAD: BAD_0764(pyrD) BAD_1334
            FNU: FN0424
            RBA: RB4752(pyrD) RB8748(pyrD) RB9748
            LIL: LA4290(pyrD)
            LIC: LIC13433(pyrD)
            LBJ: LBJ_2928(pyrD)
            LBL: LBL_0135(pyrD)
            SYN: slr1418(pyrD)
            SYW: SYNW2337(pyrD)
            SYC: syc1222_c(pyrD)
            SYF: Synpcc7942_0290
            SYD: Syncc9605_2465
            SYE: Syncc9902_2150
            SYG: sync_2721(pyrD)
            CYA: CYA_2620(pyrD)
            CYB: CYB_2280(pyrD)
            TEL: tll0579(pyrD)
            GVI: gll3080(pyrD)
            ANA: all4272
            AVA: Ava_1222 Ava_3045
            PMA: Pro0225(pyrD)
            PMM: PMM0199(pyrD)
            PMT: PMT2094(pyrD)
            PMN: PMN2A_1566
            PMB: A9601_02171(pyrD)
            PMC: P9515_02281(pyrD)
            PMF: P9303_27841(pyrD)
            PMG: P9301_02191(pyrD)
            PMH: P9215_02171
            PME: NATL1_02751(pyrD)
            TER: Tery_2007
            BTH: BT_0892 BT_1009
            BFR: BF2161 BF2400
            BFS: BF2218(pyrD2) BF2483(pyrD1)
            PGI: PG1065(pyrD)
            SRU: SRU_2381(pyrD)
            CHU: CHU_2701(pyrD)
            GFO: GFO_2519(pyrD)
            FJO: Fjoh_2210
            FPS: FP1822(pyrD)
            CTE: CT1597(pyrDI)
            CCH: Cag_1783
            PLT: Plut_1596
            DET: DET1372(pyrD)
            DEH: cbdb_A1324(pyrD)
            RRS: RoseRS_2860
            RCA: Rcas_2437
            DRA: DR_0501
            DGE: Dgeo_0500
            TTH: TTC0424 TTC0616
            TTJ: TTHA0779
            AAE: aq_046(pyrD)
            TMA: TM0333
            MJA: MJ0654(pyrD)
            MMP: MMP0439(pyrD)
            MMQ: MmarC5_1198
            MMZ: MmarC7_1436
            MAE: Maeo_0912
            MAC: MA0583(pyrD)
            MBA: Mbar_A1466
            MMA: MM_1745
            MBU: Mbur_1225
            MHU: Mhun_1154
            MST: Msp_1421(pyrD)
            MSI: Msm_1044
            MKA: MK0563(pyrD)
            AFU: AF0745(pyrD)
            HAL: VNG2507G(pyrD)
            HMA: rrnAC2969(pyrD)
            HWA: HQ1052A(pyrD)
            NPH: NP0428A(pyrD)
            TAC: Ta0404
            TVO: TVN1170
            PTO: PTO0175 PTO0807
            PHO: PH1516
            PAB: PAB1936(pyrD)
            PFU: PF1539
            TKO: TK2260
            RCI: LRC390(pyrD)
            APE: APE_0260.1
            HBU: Hbut_0261
            SSO: SSO0610(pyrD)
            STO: ST1477
            SAI: Saci_1592(pyrD)
            PAI: PAE3263(pyrD)
STRUCTURES  PDB: 1D3G  1D3H  1DOR  1EP1  1EP2  1EP3  1F76  1JQV  1JQX  1JRB  
                 1JRC  1JUB  1JUE  1OVD  1TV5  2B0M  2BX7  2BXV  2DJL  2DJX  
                 2DOR  2FPT  2FPV  2FPY  2FQI  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.3.1
            ExPASy - ENZYME nomenclature database: 1.3.3.1
            ExplorEnz - The Enzyme Database: 1.3.3.1
            ERGO genome analysis and discovery system: 1.3.3.1
            BRENDA, the Enzyme Database: 1.3.3.1
            CAS: 9029-03-2
///
ENTRY       EC 1.3.3.2        Obsolete  Enzyme
NAME        Transferred to 1.14.21.6
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now EC 1.14.21.6, lathosterol oxidase. NAD(P)H
            had not been included previously, so enzyme had to be reclassified.
            (EC 1.3.3.2 created 1972, deleted 2005)
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.3.2
            ExPASy - ENZYME nomenclature database: 1.3.3.2
            ExplorEnz - The Enzyme Database: 1.3.3.2
            ERGO genome analysis and discovery system: 1.3.3.2
            BRENDA, the Enzyme Database: 1.3.3.2
///
ENTRY       EC 1.3.3.3                  Enzyme
NAME        coproporphyrinogen oxidase;
            coproporphyrinogen III oxidase;
            coproporphyrinogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With oxygen as acceptor
SYSNAME     coproporphyrinogen:oxygen oxidoreductase (decarboxylating)
REACTION    coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 +
            2 H2O [RN:R03220]
ALL_REAC    R03220
SUBSTRATE   coproporphyrinogen III [CPD:C03263];
            O2 [CPD:C00007];
            H+ [CPD:C00080]
PRODUCT     protoporphyrinogen IX [CPD:C01079];
            CO2 [CPD:C00011];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:5881662]
  AUTHORS   del Batlle AM, Benson A, Rimington C.
  TITLE     Purification and properties of coproporphyrinogenase.
  JOURNAL   Biochem. J. 97 (1965) 731-40.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:8955072]
  AUTHORS   Medlock AE, Dailey HA.
  TITLE     Human coproporphyrinogen oxidase is not a metalloprotein.
  JOURNAL   J. Biol. Chem. 271 (1996) 32507-10.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:8407975]
  AUTHORS   Kohno H, Furukawa T, Yoshinaga T, Tokunaga R, Taketani S.
  TITLE     Coproporphyrinogen oxidase. Purification, molecular cloning, and
            induction of mRNA during erythroid differentiation.
  JOURNAL   J. Biol. Chem. 268 (1993) 21359-63.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K00228  coproporphyrinogen III oxidase
GENES       HSA: 1371(CPOX)
            PTR: 460544(CPOX)
            MMU: 12892(Cpox)
            RNO: 304024(Cpox)
            CFA: 487948(LOC487948)
            GGA: 418377(CPOX)
            SPU: 580851(LOC580851)
            DME: Dmel_CG3433(Coprox)
            ATH: AT1G03475(LIN2)
            OSA: 4336951
            CME: CMO136C
            SCE: YDR044W(HEM13)
            AGO: AGOS_AGR030C
            PIC: PICST_64368(HEM13)
            CGR: CAGL0K12100g
            SPO: SPAC222.11
            ANI: AN5130.2
            AFM: AFUA_1G07480
            AOR: AO090012000998
            CNE: CNE00980
            UMA: UM02317.1
            DDI: DDB_0231414(hemF)
            TET: TTHERM_00716050
            LMA: LmjF06.1270
            ECO: b2436(hemF)
            ECJ: JW2429(hemF)
            ECE: Z3701(hemF)
            ECS: ECs3307
            ECC: c2970(hemF)
            ECI: UTI89_C2769(hemF)
            ECP: ECP_2457
            ECV: APECO1_4112(hemF)
            ECW: EcE24377A_2722(hemF)
            ECX: EcHS_A2573(hemF)
            STY: STY2688(hemF)
            STT: t0407(hemF)
            SPT: SPA0415(hemF)
            SEC: SC2450(hemF)
            STM: STM2451(hemF)
            YPE: YPO3032(hemF)
            YPK: y1451(hemF)
            YPM: YP_2655(hemF)
            YPA: YPA_2220
            YPN: YPN_1353
            YPP: YPDSF_2137
            YPS: YPTB2754(hemF)
            YPI: YpsIP31758_1280(hemF)
            YEN: YE1168(hemF)
            SFL: SF2489(hemF)
            SFV: SFV_2488(hemF)
            SSN: SSON_2525(hemF)
            SBO: SBO_2461(hemF)
            SDY: SDY_2634(hemF)
            ECA: ECA0874(hemF)
            PLU: plu1383(hemF)
            WBR: WGLp584(hemF)
            SGL: SG1712
            ENT: Ent638_2957
            KPN: KPN_02779(hemF)
            SPE: Spro_3464
            XFA: XF0017
            XFT: PD0015(hemF)
            XCC: XCC4019(hemF)
            XCB: XC_4108
            XCV: XCV4198(hemF)
            XAC: XAC4109(hemF)
            XOO: XOO4239(hemF)
            XOM: XOO_4002(XOO4002)
            VCH: VC0055
            VCO: VC0395_A2465(hemF)
            VVU: VV1_1056
            VVY: VV3216
            VPA: VP3034
            VFI: VFA0558
            PPR: PBPRA3572
            PAE: PA0024(hemF)
            PAU: PA14_00280(hemF)
            PPU: PP_0073(hemF)
            PPF: Pput_0089
            PST: PSPTO_0170(hemF)
            PSB: Psyr_0024
            PSP: PSPPH_0026(hemF)
            PFL: PFL_0027(hemF)
            PFO: Pfl_0022
            PEN: PSEEN0030(hemF)
            PMY: Pmen_0060
            PAR: Psyc_0219(hemF) Psyc_2126(hemN)
            PCR: Pcryo_0243 Pcryo_2449
            PRW: PsycPRwf_0409
            ACI: ACIAD3250(hemF)
            SON: SO_0038(hemF)
            SDN: Sden_0030
            SFR: Sfri_0030
            SAZ: Sama_0050
            SBL: Sbal_0038
            SBM: Shew185_0033
            SLO: Shew_3729
            SPC: Sputcn32_0030
            SSE: Ssed_0042
            SPL: Spea_0038
            SHE: Shewmr4_0035
            SHM: Shewmr7_0033
            SHN: Shewana3_0041
            SHW: Sputw3181_0030
            ILO: IL0023(hemF)
            CPS: CPS_3996(hemF)
            PHA: PSHAa0029(hemF)
            PAT: Patl_0029
            SDE: Sde_0025
            MAQ: Maqu_0047
            CBU: CBU_1729(hemF)
            CBD: COXBU7E912_0273(hemF)
            LPN: lpg1215(hemF)
            LPF: lpl1223(hemF)
            LPP: lpp1223(hemF)
            MCA: MCA2791(hemF)
            FTU: FTT1063(hemF)
            FTF: FTF1063(hemF)
            FTW: FTW_0975(hemF)
            FTL: FTL_1022
            FTH: FTH_0997(hemF)
            FTA: FTA_1078(hemF)
            FTN: FTN_0953(hemF)
            TCX: Tcr_0017
            NOC: Noc_2824
            AEH: Mlg_2634
            HHA: Hhal_2320
            HCH: HCH_00036(hemF)
            CSA: Csal_2863
            ABO: ABO_0135 ABO_1342(hemF) ABO_2580
            MMW: Mmwyl1_0061
            AHA: AHA_0265(hemF)
            RMA: Rmag_0496
            VOK: COSY_0456(hemF)
            CVI: CV_0757(hemF)
            RSO: RSc2192(hemF)
            REU: Reut_A2524
            REH: H16_A0914(hemF)
            RME: Rmet_0783
            BMA: BMA1886(hemF)
            BMV: BMASAVP1_A1073(hemF)
            BML: BMA10299_A0794(hemF)
            BMN: BMA10247_0356(hemF)
            BXE: Bxe_A0855 Bxe_A0901 Bxe_A3261
            BVI: Bcep1808_2381
            BUR: Bcep18194_A5623
            BCN: Bcen_1684
            BCH: Bcen2424_2296
            BAM: Bamb_2334
            BPS: BPSL1163(hemF)
            BPM: BURPS1710b_1383(hemF)
            BPL: BURPS1106A_1238(hemF)
            BPD: BURPS668_1229(hemF)
            BTE: BTH_I1013(hemF)
            PNU: Pnuc_0616
            BPE: BP2310(hemF)
            BPA: BPP2420(hemF)
            BBR: BB1869(hemF)
            RFR: Rfer_2077
            POL: Bpro_1970
            PNA: Pnap_1730
            AAV: Aave_3201
            AJS: Ajs_1900
            VEI: Veis_4240
            MPT: Mpe_A1339
            HAR: HEAR0556(hemF)
            MMS: mma_0542(hemF) mma_1334(hemN1) mma_1627(hemN2)
            NEU: NE1876(hemF)
            NET: Neut_1956
            NMU: Nmul_A0135
            EBA: ebA1156(hemF)
            AZO: azo1352(hemN) azo2896(hemF) azo3965
            DAR: Daro_3669
            TBD: Tbd_2461
            MFA: Mfla_0346
            ADE: Adeh_2014
            AFW: Anae109_1703
            MXA: MXAN_6762(hemF)
            RPR: RP882(hemF)
            RTY: RT0874(hemF)
            RCO: RC1369(hemF)
            RFE: RF_1396(hemF)
            RBE: RBE_1380(hemF)
            RAK: A1C_06860
            RBO: A1I_07665
            RCM: A1E_05665
            RRI: A1G_07495
            OTS: OTBS_0188(hemF)
            WOL: WD1214
            WBM: Wbm0709
            AMA: AM762(hemF)
            APH: APH_0423(hemF)
            ERU: Erum4550(hemF)
            ERW: ERWE_CDS_04770(hemF)
            ERG: ERGA_CDS_04670(hemF)
            ECN: Ecaj_0446
            ECH: ECH_0591(hemF)
            NSE: NSE_0454(hemF)
            PUB: SAR11_0102(hemF)
            MLO: mlr2722
            MES: Meso_2169
            PLA: Plav_2240
            SME: SMc00180(hemF)
            SMD: Smed_1549
            ATU: Atu2247(hemF)
            ATC: AGR_C_4089(hemF)
            RET: RHE_CH03046(hemF) RHE_PD00262(hemNd2) RHE_PD00300(hemNd1)
                 RHE_PF00519(hemNf)
            RLE: RL3494(hemF)
            BME: BMEI0467
            BMF: BAB1_1566(hemF)
            BMS: BR1550(hemF)
            BMB: BruAb1_1539(hemF)
            BOV: BOV_1498(hemF)
            OAN: Oant_1616
            BJA: bll2481(hemF)
            BRA: BRADO1972(hemF)
            BBT: BBta_2296(hemF)
            RPA: RPA1514(hemF)
            RPB: RPB_4009
            RPC: RPC_1263
            RPD: RPD_3764
            RPE: RPE_1317
            NWI: Nwi_2621
            NHA: Nham_3246
            XAU: Xaut_2954
            CCR: CC_0506
            SIL: SPO3653(hemF)
            SIT: TM1040_2531
            RSP: RSP_0682(hemF) RSP_3816
            RSH: Rsph17029_2337
            RSQ: Rsph17025_0548
            JAN: Jann_3848
            RDE: RD1_1282(hemF)
            PDE: Pden_1752
            MMR: Mmar10_0734
            HNE: HNE_0349(hemF)
            ZMO: ZMO0951(hemF)
            NAR: Saro_2536
            SAL: Sala_1347
            SWI: Swit_1398
            ELI: ELI_09420
            GOX: GOX1896
            GBE: GbCGDNIH1_1722
            ACR: Acry_2944
            BTL: BALH_0789(hemN) BALH_3907(hemN)
            BAY: RBAM_023800(hemN)
            BPU: BPUM_0930(hemZ)
            LLM: llmg_1418(hemN)
            CMI: CMM_1561(hemN)
            PCU: pc1975(hemF)
            LIL: LB017(hemF)
            LIC: LIC20015(hemN)
            LBJ: LBJ_4015(hemN)
            LBL: LBL_4015(hemN)
            SYN: sll1185(hemF)
            SYW: SYNW2040(hemF)
            SYC: syc0855_c(hemF)
            SYF: Synpcc7942_0674
            SYD: Syncc9605_0403
            SYE: Syncc9902_1926
            SYG: sync_0467(hemF)
            SYR: SynRCC307_2083(hemF)
            SYX: SynWH7803_0461(hemF)
            CYA: CYA_0869(hemF)
            CYB: CYB_2837(hemF)
            TEL: tll0684(hemF)
            GVI: gll3876(hemF)
            ANA: all0650(hemF1) all1357(hemF2)
            AVA: Ava_4581 Ava_4996
            PMA: Pro1737(hemF)
            PMM: PMM1582(hemF)
            PMT: PMT1706(hemF)
            PMN: PMN2A_1154
            PMI: PMT9312_1674
            PMB: A9601_15101(hemN) A9601_17891(hemF)
            PMC: P9515_14721(hemN) P9515_17691(hemF)
            PMF: P9303_19991(hemN) P9303_22671(hemF)
            PMG: P9301_14971(hemN) P9301_17731(hemF)
            PMH: P9215_18541(hemF)
            PME: NATL1_17311(hemN) NATL1_20281(hemF)
            TER: Tery_1166
            SRU: SRU_1742(hemF)
            CHU: CHU_1918(hemF)
            GFO: GFO_1414(hemN) GFO_3228(hemF)
            FJO: Fjoh_0950
            FPS: FP0037(hemF) FP0208 FP1163(hemN)
STRUCTURES  PDB: 1TK1  1TKL  1TLB  1TXN  1VJU  2AEX  2QT8  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.3.3
            ExPASy - ENZYME nomenclature database: 1.3.3.3
            ExplorEnz - The Enzyme Database: 1.3.3.3
            ERGO genome analysis and discovery system: 1.3.3.3
            BRENDA, the Enzyme Database: 1.3.3.3
            CAS: 9076-84-0
///
ENTRY       EC 1.3.3.4                  Enzyme
NAME        protoporphyrinogen oxidase;
            protoporphyrinogen IX oxidase;
            protoporphyrinogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With oxygen as acceptor
SYSNAME     protoporphyrinogen-IX:oxygen oxidoreductase
REACTION    protoporphyrinogen IX + 1.5 O2 = protoporphyrin IX + 3 H2O
            [RN:R03222]
ALL_REAC    R03222
SUBSTRATE   protoporphyrinogen IX [CPD:C01079];
            O2 [CPD:C00007]
PRODUCT     protoporphyrin IX [CPD:C02191];
            H2O [CPD:C00001]
COMMENT     Also slowly oxidizes mesoporphyrinogen IX.
REFERENCE   1  [PMID:6461]
  AUTHORS   Poulson R.
  TITLE     The enzymic conversion of protoporphyrinogen IX to protoporphyrin IX
            in mammalian mitochondria.
  JOURNAL   J. Biol. Chem. 251 (1976) 3730-3.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:234450]
  AUTHORS   Poulson R, Polglase WJ.
  TITLE     The enzymic conversion of protoporphyrinogen IX to protoporphyrin
            IX. Protoporphyrinogen oxidase activity in mitochondrial extracts of
            Saccharomyces cerevisiae.
  JOURNAL   J. Biol. Chem. 250 (1975) 1269-74.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:8621504]
  AUTHORS   Dailey HA, Dailey TA.
  TITLE     Protoporphyrinogen oxidase of Myxococcus xanthus. Expression,
            purification, and characterization of the cloned enzyme.
  JOURNAL   J. Biol. Chem. 271 (1996) 8714-8.
  ORGANISM  Myxococcus xanthus [GN:mxa]
REFERENCE   4  [PMID:11506917]
  AUTHORS   Wang KF, Dailey TA, Dailey HA.
  TITLE     Expression and characterization of the terminal heme synthetic
            enzymes from the hyperthermophile Aquifex aeolicus.
  JOURNAL   FEMS. Microbiol. Lett. 202 (2001) 115-9.
  ORGANISM  Aquifex aeolicus [GN:aae]
REFERENCE   5  [PMID:9784236]
  AUTHORS   Corrigall AV, Siziba KB, Maneli MH, Shephard EG, Ziman M, Dailey TA,
            Dailey HA, Kirsch RE, Meissner PN.
  TITLE     Purification of and kinetic studies on a cloned protoporphyrinogen
            oxidase from the aerobic bacterium Bacillus subtilis.
  JOURNAL   Arch. Biochem. Biophys. 358 (1998) 251-6.
  ORGANISM  Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K00229  protoporphyrinogen oxidase
            KO: K00230  protoporphyrinogen oxidase
            KO: K00231  protoporphyrinogen oxidase
GENES       HSA: 5498(PPOX)
            MMU: 19044(Ppox)
            CFA: 478980(PPOX)
            XLA: 446722(ppox)
            SPU: 592844(LOC592844)
            DME: Dmel_CG5796(Ppox)
            ATH: AT4G01690(PPOX) AT5G14220(HEMG2/MEE61)
            OSA: 4327918
            CME: CMB025C
            SCE: YER014W(HEM14)
            AGO: AGOS_AAR021W
            PIC: PICST_55152(HEM14)
            CAL: CaO19_4747(CaO19.4747)
            CGR: CAGL0H09504g
            SPO: SPAC1F5.07c
            ANI: AN3920.2
            AFM: AFUA_6G08440
            AOR: AO090001000500
            CNE: CNG03820
            UMA: UM04236.1
            DDI: DDB_0231419(hemG)
            PFA: PF10_0275
            TET: TTHERM_00157800
            LMA: LmjF06.1280
            ECO: b3850(hemG)
            ECJ: JW3827(hemG)
            ECE: Z5372(hemG)
            ECS: ECs4778
            ECC: c4797(hemG)
            ECI: UTI89_C4435(hemG)
            ECP: ECP_4063
            ECV: APECO1_2607(hemG)
            ECW: EcE24377A_4369(hemG)
            ECX: EcHS_A4073(hemG)
            STY: STY3573(hemG)
            STT: t3311(hemG)
            SPT: SPA3827(hemG)
            SEC: SC3883(hemG)
            STM: STM3987(hemG)
            YPE: YPO3761(hemG)
            YPK: y0469(hemG)
            YPM: YP_3286(hemG)
            YPA: YPA_3430
            YPN: YPN_0204
            YPP: YPDSF_3382
            YPS: YPTB0271(hemG)
            YPI: YpsIP31758_0287(hemG)
            SFL: SF3926(hemG)
            SFX: S3826(hemG)
            SFV: SFV_3650(hemG)
            SSN: SSON_4023(hemG)
            SBO: SBO_3862(hemG)
            SDY: SDY_3895(hemG)
            ECA: ECA0212(hemG)
            PLU: plu4398(hemG)
            WBR: WGLp123(hemG)
            SGL: SG0121
            ENT: Ent638_3945
            SPE: Spro_0266
            HSO: HS_1569
            PMU: PM1499
            MSU: MS0176(fldA)
            ASU: Asuc_0513
            VCH: VC2755
            VCO: VC0395_A2537(hemG)
            VVU: VV1_0978
            VVY: VV0033
            VPA: VP0033
            VFI: VF0028
            PPR: PBPRA0067
            SON: SO_0025 SO_0027 SO_3720
            SDN: Sden_0019
            SFR: Sfri_0017 Sfri_0019 Sfri_0813
            SAZ: Sama_0036 Sama_0038 Sama_2882
            SBL: Sbal_0025 Sbal_0027
            SBM: Shew185_0020 Shew185_0022 Shew185_0939
            SLO: Shew_0023 Shew_0025
            SPC: Sputcn32_0017 Sputcn32_0019 Sputcn32_3038
            SSE: Ssed_0027 Ssed_0029
            SPL: Spea_0022 Spea_0026 Spea_0673
            SHE: Shewmr4_0022 Shewmr4_0024 Shewmr4_3066
            SHM: Shewmr7_0020 Shewmr7_0022 Shewmr7_0906
            SHN: Shewana3_0028 Shewana3_0030 Shewana3_0871 Shewana3_3300
            SHW: Sputw3181_0017 Sputw3181_0019 Sputw3181_0907
            PIN: Ping_0198
            CSA: Csal_0796
            MMW: Mmwyl1_1487
            AHA: AHA_0144
            CVI: CV_1653(hemG)
            REH: H16_A2891 H16_B2453
            BXE: Bxe_B1116 Bxe_C1113
            RFR: Rfer_4072
            GSU: GSU0012(hemG)
            GME: Gmet_2953 Gmet_3551
            GUR: Gura_0144
            PCA: Pcar_0772
            PPD: Ppro_0014
            BBA: Bd2899(hemG) Bd3455(hemG)
            DPS: DP0277
            MXA: MXAN_1293(hemG)
            MLO: mlr4722
            JAN: Jann_0852
            MGM: Mmc1_0027
            ABA: Acid345_0695
            SUS: Acid_5204
            BSU: BG10431(hemY)
            BHA: BH1204(hemY)
            BAN: BA1072(hemY-1) BA2418(hemY-2)
            BAR: GBAA1072(hemY-1) GBAA2418(hemY-2)
            BAA: BA_1624 BA_2917
            BAT: BAS1001 BAS2253
            BCE: BC1070 BC2354
            BCA: BCE_1169(hemY) BCE_2450(hemY)
            BCZ: BCZK0988(hemY) BCZK2172(hemY)
            BCY: Bcer98_0826 Bcer98_1774
            BTK: BT9727_0986(hemY) BT9727_2212(hemY)
            BLI: BL01074(hemY)
            BLD: BLi01094(hemY)
            BCL: ABC1540(hemY)
            BAY: RBAM_010370(hemY)
            BPU: BPUM_0960(hemY)
            OIH: OB1169(hemY)
            GKA: GK0663
            SAU: SA1650(hemY)
            SAV: SAV1832(hemY)
            SAM: MW1772(hemY)
            SAR: SAR1923(hemY)
            SAS: SAS1753
            SAC: SACOL1887(hemG)
            SAB: SAB1763c(hemY)
            SAA: SAUSA300_1781(hemG)
            SAO: SAOUHSC_01960
            SEP: SE1511
            SER: SERP1366(hemG)
            SHA: SH1130(hemY)
            SSP: SSP0967
            LMO: lmo0884
            LMF: LMOf2365_0903(hemG)
            LIN: lin0883
            LWE: lwe0866(hemG)
            SGO: SGO_1153
            CHY: CHY_0481(hemG)
            MMO: MMOB1890(hemK)
            MHY: mhp242(hemK)
            MTU: Rv2677c(hemY)
            MTC: MT2751(hemG)
            MBO: Mb2696c(hemY)
            MBB: BCG_2690c(hemY)
            MLE: ML1044(hemY)
            MPA: MAP2798c(hemY')
            MSM: MSMEG_2781(hemG)
            MVA: Mvan_2482
            MGI: Mflv_3918
            MMC: Mmcs_2213
            MKM: Mkms_2259
            MJL: Mjls_2202
            CGL: NCgl0421(cgl0436)
            CGB: cg0517(hemY)
            CEF: CE0459
            CDI: DIP0408(hemG)
            CJK: jk1074(hemG)
            NFA: nfa37370
            RHA: RHA1_ro06859
            SCO: SCO6041(SC1B5.01)
            LXX: Lxx01060(hemG)
            ART: Arth_1632
            AAU: AAur_2754(hemG)
            PAC: PPA0305 PPA2095
            NCA: Noca_1429 Noca_3672
            TFU: Tfu_1897 Tfu_3023
            FRA: Francci3_1335
            FAL: FRAAL2102(hemG)
            ACE: Acel_1381
            KRA: Krad_1586
            SEN: SACE_0182 SACE_1837(hemG)
            STP: Strop_1533 Strop_2186
            RBA: RB10459(hemY) RB4887(hemG)
            CTR: CT745(hemG)
            CTA: CTA_0811(hemG)
            CMU: TC0121
            CPN: CPn0888(hemG)
            CPA: CP0978
            CPJ: CPj0888(hemG)
            CPT: CpB0918
            CCA: CCA00880
            CAB: CAB846
            CFE: CF0136(hemY)
            PCU: pc1512(hemG)
            LIL: LB020(hemG)
            LIC: LIC20017(hemG)
            LBJ: LBJ_4017(hemY)
            LBL: LBL_4017(hemY)
            SYW: SYNW1976(hemK)
            SYR: SynRCC307_0424(hemK)
            SYX: SynWH7803_0524(hemK)
            CYA: CYA_1101(hemG)
            CYB: CYB_1424(hemG)
            TEL: tlr0374
            GVI: glr0943(hemG)
            PMA: Pro0359(hemK)
            PMM: PMM0318(hemK)
            PMT: PMT1660(hemK)
            PMB: A9601_03421(hemK)
            PMC: P9515_03501(hemK) P9515_09631(hemG)
            PMF: P9303_22051(hemK)
            PMG: P9301_03431(hemK)
            PMH: P9215_10111(hemG)
            PME: NATL1_04091(hemK)
            TER: Tery_2218
            BFR: BF1913
            BFS: BF1983
            PGI: PG2159
            SRU: SRU_1215(hemG)
            CHU: CHU_0202(hemG) CHU_1574
            RRS: RoseRS_1744
            RCA: Rcas_2024
            DRA: DR_1130
            TTH: TTC0230
            TTJ: TTHA0599
            AAE: aq_2015(hemG)
            MAC: MA2078
            MMA: MM_3140
            HWA: HQ3321A(hemY)
            NPH: NP4520A(hemY)
            RCI: RCIX1909(hemG)
STRUCTURES  PDB: 1SEZ  2IVD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.3.4
            ExPASy - ENZYME nomenclature database: 1.3.3.4
            ExplorEnz - The Enzyme Database: 1.3.3.4
            ERGO genome analysis and discovery system: 1.3.3.4
            BRENDA, the Enzyme Database: 1.3.3.4
            CAS: 53986-32-6
///
ENTRY       EC 1.3.3.5                  Enzyme
NAME        bilirubin oxidase;
            bilirubin oxidase M-1
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With oxygen as acceptor
SYSNAME     bilirubin:oxygen oxidoreductase
REACTION    2 bilirubin + O2 = 2 biliverdin + 2 H2O [RN:R02394]
ALL_REAC    R02394
SUBSTRATE   bilirubin [CPD:C00486];
            O2 [CPD:C00007]
PRODUCT     biliverdin [CPD:C00500];
            H2O [CPD:C00001]
REFERENCE   1
  AUTHORS   Murao, S. and Tanaka, N.
  TITLE     A new enzyme bilirubin oxidase produced by Myrothecium verrucaria
            MT-1.
  JOURNAL   Agric. Biol. Chem. 45 (1981) 2383-2384.
  ORGANISM  Myrothecium verrucaria
REFERENCE   2
  AUTHORS   Tanaka, N. and Murao, S.
  TITLE     Reaction of bilirubin oxidase produced by Myrothecium verrucaria
            MT-1. Agr.
  JOURNAL   Biol. Chem. 49 (1985) 843-844.
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K08100  bilirubin oxidase
GENES       TCX: Tcr_1576 Tcr_2113
            RMA: Rmag_0708
            VOK: COSY_0659
            BMA: BMA0487
            BUR: Bcep18194_A5853
            BAM: Bamb_2569
            BPS: BPSL0897
            BPM: BURPS1710b_1110
            BTE: BTH_I0760
            PNA: Pnap_4517
            NET: Neut_1052
            NMU: Nmul_A1679
            AFW: Anae109_0501 Anae109_3891
            RLE: RL1604(cumA)
            XAU: Xaut_2270 Xaut_2898 Xaut_4880
            RDE: RD1_2306
            MJL: Mjls_1438 Mjls_1440
            STP: Strop_2658
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.3.5
            ExPASy - ENZYME nomenclature database: 1.3.3.5
            ExplorEnz - The Enzyme Database: 1.3.3.5
            ERGO genome analysis and discovery system: 1.3.3.5
            BRENDA, the Enzyme Database: 1.3.3.5
            CAS: 80619-01-8
///
ENTRY       EC 1.3.3.6                  Enzyme
NAME        acyl-CoA oxidase;
            fatty acyl-CoA oxidase;
            acyl coenzyme A oxidase;
            fatty acyl-coenzyme A oxidase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With oxygen as acceptor
SYSNAME     acyl-CoA:oxygen 2-oxidoreductase
REACTION    acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2 [RN:R00388]
ALL_REAC    R00388;
            (other) R01175 R01279 R03777 R03857 R03990 R04751 R04754 R07888
            R07892 R07896 R07934 R07950
SUBSTRATE   acyl-CoA [CPD:C00040];
            O2 [CPD:C00007]
PRODUCT     trans-2,3-dehydroacyl-CoA [CPD:C00658];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Acts on CoA derivatives of fatty acids with
            chain lengths from 8 to 18.
REFERENCE   1  [PMID:7462191]
  AUTHORS   Kawaguchi A, Tsubotani S, Seyama Y, Yamakawa T, Osumi T, Hashimoto
            T, Kikuchi T, Ando M, Okuda S.
  TITLE     Stereochemistry of dehydrogenation catalyzed by Acyl-CoA oxidase.
  JOURNAL   J. Biochem. (Tokyo). 88 (1980) 1481-6.
  ORGANISM  rat [GN:rno], Candida lipolytica
REFERENCE   2  [PMID:7400120]
  AUTHORS   Osumi T, Hashimoto T, Ui N.
  TITLE     Purification and properties of acyl-CoA oxidase from rat liver.
  JOURNAL   J. Biochem. (Tokyo). 87 (1980) 1735-46.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00071  Fatty acid metabolism
            PATH: map00592  alpha-Linolenic acid metabolism
            PATH: map01040  Polyunsaturated fatty acid biosynthesis
            PATH: map03320  PPAR signaling pathway
ORTHOLOGY   KO: K00232  acyl-CoA oxidase
GENES       HSA: 51(ACOX1) 8310(ACOX3)
            PTR: 454895(ACOX1) 461115(ACOX3)
            MMU: 11430(Acox1) 80911(Acox3)
            RNO: 50681(Acox1) 83522(Acox3)
            CFA: 483322(ACOX1) 488790(ACOX3)
            BTA: 513996(ACOX1)
            GGA: 417366(ACOX1) 422869(ACOX3)
            XLA: 403357(MGC68531)
            XTR: 548479(MGC108278)
            DRE: 406421(acox3)
            SPU: 578168(LOC578168) 580036(LOC580036) 580903(LOC580903)
            DME: Dmel_CG9707(Acox57D-p) Dmel_CG9709(Acox57D-d)
            CEL: C48B4.1 F08A8.2 F08A8.3 F08A8.4 F25C8.1 F58F9.7 F59F4.1
            ATH: AT1G06290(ACX3) AT1G06310(ACX6) AT2G35690(ACX5)
                 AT3G51840(ACX4) AT4G16760(ACX1) AT5G65110(ACX2)
            OSA: 4324062 4339846 4340986 4350881
            CME: CMK115C
            SCE: YGL205W(POX1)
            AGO: AGOS_AER358C
            PIC: PICST_75424(POX1)
            CGR: CAGL0A03740g
            YLI: YALI0C23859g(POX5) YALI0D24750g(POX3) YALI0F10857g(POX2)
            ANI: AN6752.2
            AFM: AFUA_7G06090 AFUA_7G06100
            AOR: AO090005000479 AO090010000014
            CNE: CNG00320
            UMA: UM04324.1
            DDI: DDBDRAFT_0188674 DDBDRAFT_0216722
            TET: TTHERM_00242260 TTHERM_00370760 TTHERM_00586710
            MPA: MAP2101
            MSM: MSMEG_4474
            NFA: nfa24790
            RHA: RHA1_ro02047
            CMI: CMM_0813
            TFU: Tfu_2239
            SEN: SACE_5537 SACE_7372
            SRU: SRU_1701
STRUCTURES  PDB: 1IS2  1W07  2DDH  2FON  2IX5  2IX6  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.3.6
            ExPASy - ENZYME nomenclature database: 1.3.3.6
            ExplorEnz - The Enzyme Database: 1.3.3.6
            ERGO genome analysis and discovery system: 1.3.3.6
            BRENDA, the Enzyme Database: 1.3.3.6
            CAS: 61116-22-1
///
ENTRY       EC 1.3.3.7                  Enzyme
NAME        dihydrouracil oxidase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With oxygen as acceptor
SYSNAME     5,6-dihydrouracil:oxygen oxidoreductase
REACTION    5,6-dihydrouracil + O2 = uracil + H2O2 [RN:R00975]
ALL_REAC    R00975
SUBSTRATE   5,6-dihydrouracil [CPD:C00429];
            O2 [CPD:C00007]
PRODUCT     uracil [CPD:C00106];
            H2O2 [CPD:C00027]
COFACTOR    FMN [CPD:C00061]
COMMENT     Also oxidizes dihydrothymine to thymine. A flavoprotein (FMN).
REFERENCE   1
  AUTHORS   Owaki, J., Uzura, K., Minami, Z. and Kusai, K.
  TITLE     Partial-purification and characterization of dihydrouracil oxidase,
            a flavoprotein from Rhodotorula glutinis.
  JOURNAL   J. Ferment. Technol. 64 (1986) 205-210.
  ORGANISM  Rhodotorula glutinis
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.3.7
            ExPASy - ENZYME nomenclature database: 1.3.3.7
            ExplorEnz - The Enzyme Database: 1.3.3.7
            ERGO genome analysis and discovery system: 1.3.3.7
            BRENDA, the Enzyme Database: 1.3.3.7
            CAS: 104327-11-9
///
ENTRY       EC 1.3.3.8                  Enzyme
NAME        tetrahydroberberine oxidase;
            (S)-THB oxidase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With oxygen as acceptor
SYSNAME     (S)-tetrahydroberberine:oxygen oxidoreductase
REACTION    (S)-tetrahydroberberine + 2 O2 = berberine + 2 H2O2 [RN:R02880]
ALL_REAC    R02880;
            (other) R03722
SUBSTRATE   (S)-tetrahydroberberine [CPD:C03329];
            O2 [CPD:C00007]
PRODUCT     berberine [CPD:C00757];
            H2O2 [CPD:C00027]
COMMENT     The enzyme from Berberis sp. is a flavoprotein; that from Coptis
            japonica is not. (R)-Tetrahydroberberines are not oxidized.
REFERENCE   1
  AUTHORS   Amann, M., Nagakura, N. and Zenk, M.H.
  TITLE     (S)-Tetrahydroprotoberberine oxidase the final enzyme in
            protoberberine biosynthesis.
  JOURNAL   Tetrahedron Lett. 25 (1984) 953-954.
  ORGANISM  Berberis wilsoniae , Papaver somniferum
REFERENCE   2
  AUTHORS   Okada, N., Shinmyo, A., Okada, H. and Yamada, Y.
  TITLE     Purification and characterization of (S)-tetrahydroberberine oxidase
            from cultured Coptis japonica cells.
  JOURNAL   Phytochemistry 27 (1988) 979-982.
  ORGANISM  Coptis japonica
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.3.8
            ExPASy - ENZYME nomenclature database: 1.3.3.8
            ExplorEnz - The Enzyme Database: 1.3.3.8
            ERGO genome analysis and discovery system: 1.3.3.8
            BRENDA, the Enzyme Database: 1.3.3.8
            CAS: 114705-00-9
///
ENTRY       EC 1.3.3.9                  Enzyme
NAME        secologanin synthase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With oxygen as acceptor
SYSNAME     loganin:oxygen oxidoreductase (ring-cleaving)
REACTION    loganin + NADPH + H+ + O2 = secologanin + NADP+ + 2 H2O [RN:R03555]
ALL_REAC    R03555;
            (other) R05833
SUBSTRATE   loganin [CPD:C01433];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     secologanin [CPD:C01852];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450). Secologanin is the precursor of the
            monoterpenoid indole alkaloids and ipecac alkaloids.
REFERENCE   1  [PMID:10656401]
  AUTHORS   Yamamoto H, Katano N, Ooi A, Inoue K.
  TITLE     Secologanin synthase which catalyzes the oxidative cleavage of
            loganin into secologanin is a cytochrome P450.
  JOURNAL   Phytochemistry. 53 (2000) 7-12.
  ORGANISM  Lonicera japonica
REFERENCE   2  [PMID:11135113]
  AUTHORS   Irmler S, Schroder G, St-Pierre B, Crouch NP, Hotze M, Schmidt J,
            Strack D, Matern U, Schroder J.
  TITLE     Indole alkaloid biosynthesis in Catharanthus roseus: new enzyme
            activities and identification of cytochrome P450 CYP72A1 as
            secologanin synthase.
  JOURNAL   Plant. J. 24 (2000) 797-804.
  ORGANISM  Catharanthus roseus
REFERENCE   3
  AUTHORS   Yamamoto, H., Katano, N., Ooi, Y. and Inoue, K.
  TITLE     Transformation of loganin and 7-deoxyloganin into secologanin by
            Lonicera japonica cell suspension cultures.
  JOURNAL   Phytochemistry 50 (1999) 417-422.
  ORGANISM  Lonicera japonica
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.3.9
            ExPASy - ENZYME nomenclature database: 1.3.3.9
            ExplorEnz - The Enzyme Database: 1.3.3.9
            ERGO genome analysis and discovery system: 1.3.3.9
            BRENDA, the Enzyme Database: 1.3.3.9
            CAS: 258339-71-8
///
ENTRY       EC 1.3.3.10                 Enzyme
NAME        tryptophan alpha,beta-oxidase;
            L-tryptophan 2',3'-oxidase;
            L-tryptophan alpha,beta-dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With oxygen as acceptor
SYSNAME     L-tryptophan:oxygen alpha,beta-oxidoreductase
REACTION    L-tryptophan + O2 = alpha,beta-didehydrotryptophan + H2O2
            [RN:R05317]
ALL_REAC    R05317
SUBSTRATE   L-tryptophan [CPD:C00078];
            O2 [CPD:C00007]
PRODUCT     alpha,beta-didehydrotryptophan [CPD:C06732];
            H2O2 [CPD:C00027]
COFACTOR    Heme [CPD:C00032]
COMMENT     Requires heme. The enzyme from Chromobacterium violaceum is specific
            for tryptophan derivatives possessing its carboxyl group free or as
            an amide or ester, and an unsubstituted indole ring. Also catalyses
            the alpha,beta dehydrogenation of L-tryptophan side chains in
            peptides. The product of the reaction can hydrolyse spontaneously to
            form indolepyruvate.
REFERENCE   1  [PMID:8027079]
  AUTHORS   Genet R, Denoyelle C, Menez A.
  TITLE     Purification and partial characterization of an amino acid
            alpha,beta- dehydrogenase, L-tryptophan 2',3'-oxidase from
            Chromobacterium violaceum.
  JOURNAL   J. Biol. Chem. 269 (1994) 18177-84.
  ORGANISM  Chromobacterium violaceum [GN:cvi]
REFERENCE   2  [PMID:7559518]
  AUTHORS   Genet R, Benetti PH, Hammadi A, Menez A.
  TITLE     L-tryptophan 2',3'-oxidase from Chromobacterium violaceum. Substrate
            specificity and mechanistic implications.
  JOURNAL   J. Biol. Chem. 270 (1995) 23540-5.
  ORGANISM  Chromobacterium violaceum [GN:cvi]
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.3.10
            ExPASy - ENZYME nomenclature database: 1.3.3.10
            ExplorEnz - The Enzyme Database: 1.3.3.10
            ERGO genome analysis and discovery system: 1.3.3.10
            BRENDA, the Enzyme Database: 1.3.3.10
            CAS: 156859-19-7
///
ENTRY       EC 1.3.3.11                 Enzyme
NAME        pyrroloquinoline-quinone synthase;
            PqqC
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With oxygen as acceptor
SYSNAME     6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-octahydroquinol
            ine-2,4-dicarboxylate:oxygen oxidoreductase (cyclizing)
REACTION    6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-
            octahydroquinoline-2,4-dicarboxylate + 3 O2 =
            4,5-dioxo-3a,4,5,6,7,8,9,9b-octahydro-1H-pyrrolo[2,3-f]quinoline-
            2,7,9-tricarboxylate + 2 H2O2 + 2 H2O
ALL_REAC    (other) R07353
SUBSTRATE   6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-
            octahydroquinoline-2,4-dicarboxylate;
            O2 [CPD:C00007]
PRODUCT     4,5-dioxo-3a,4,5,6,7,8,9,9b-octahydro-1H-pyrrolo[2,3-f]quinoline-
            2,7,9-tricarboxylate;
            H2O2 [CPD:C00027];
            H2O [CPD:C00001]
COMMENT     So far only a single turnover of the enzyme has been observed, and
            the pyrroloquinoline quinone remains bound to it. It is not yet
            known what releases the product in the bacterium.
REFERENCE   1  [PMID:15113189]
  AUTHORS   Magnusson OT, Toyama H, Saeki M, Schwarzenbacher R, Klinman JP.
  TITLE     The structure of a biosynthetic intermediate of pyrroloquinoline
            quinone (PQQ) and elucidation of the final step of PQQ biosynthesis.
  JOURNAL   J. Am. Chem. Soc. 126 (2004) 5342-3.
  ORGANISM  Klebsiella pneumoniae, Methylobacterium extorquens
REFERENCE   2  [PMID:15148379]
  AUTHORS   Magnusson OT, Toyama H, Saeki M, Rojas A, Reed JC, Liddington RC,
            Klinman JP, Schwarzenbacher R.
  TITLE     Quinone biogenesis: Structure and mechanism of PqqC, the final
            catalyst in the production of pyrroloquinoline quinone.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 7913-8.
  ORGANISM  Klebsiella pneumoniae, Methylobacterium extorquens
REFERENCE   3  [PMID:9043136]
  AUTHORS   Toyama H, Chistoserdova L, Lidstrom ME.
  TITLE     Sequence analysis of pqq genes required for biosynthesis of
            pyrroloquinoline quinone in Methylobacterium extorquens AM1 and the
            purification of a biosynthetic intermediate.
  JOURNAL   Microbiology. 143 ( Pt 2) (1997) 595-602.
  ORGANISM  Klebsiella pneumoniae, Methylobacterium extorquens
REFERENCE   4  [PMID:1243798]
  AUTHORS   Yasunaga K.
  TITLE     [Concept of thrombocytopathy and problems involved in its diagnosis
            (author's transl)]
  JOURNAL   Nippon. Ketsueki. Gakkai. Zasshi. 38 (1975) 734-40.
REFERENCE   5  [PMID:15211525]
  AUTHORS   Schwarzenbacher R, Stenner-Liewen F, Liewen H, Reed JC, Liddington
            RC.
  TITLE     Crystal structure of PqqC from Klebsiella pneumoniae at 2.1 A
            resolution.
  JOURNAL   Proteins. 56 (2004) 401-3.
  ORGANISM  Klebsiella pneumoniae
ORTHOLOGY   KO: K06137  pyrroloquinoline-quinone synthase
GENES       PPF: Pput_0403
            PMY: Pmen_1967
            SMD: Smed_3917
            XAU: Xaut_1801
            RSQ: Rsph17025_0388
            ACR: Acry_0079 Acry_0323
            MSM: MSMEG_3722
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.3.11
            ExPASy - ENZYME nomenclature database: 1.3.3.11
            ExplorEnz - The Enzyme Database: 1.3.3.11
            ERGO genome analysis and discovery system: 1.3.3.11
            BRENDA, the Enzyme Database: 1.3.3.11
///
ENTRY       EC 1.3.3.12                 Enzyme
NAME        L-galactonolactone oxidase;
            L-galactono-1,4-lactone oxidase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With oxygen as acceptor
SYSNAME     L-galactono-1,4-lactone:oxygen 3-oxidoreductase
REACTION    L-galactono-1,4-lactone + O2 = L-ascorbate + H2O2 [RN:R00643]
ALL_REAC    R00643
SUBSTRATE   L-galactono-1,4-lactone [CPD:C01115];
            O2 [CPD:C00007]
PRODUCT     L-ascorbate [CPD:C00072];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein. Acts on the 1,4-lactones of L-galactonic,
            D-altronic, L-fuconic, D-arabinic and D-threonic acids; not
            identical with EC 1.1.3.8 L-gulonolactone oxidase. (cf. EC 1.3.2.3
            galactonolactone dehydrogenase).
REFERENCE   1  [PMID:6754380]
  AUTHORS   Bleeg HS, Christensen F.
  TITLE     Biosynthesis of ascorbate in yeast. Purification of
            L-galactono-1,4-lactone oxidase with properties different from
            mammalian L-gulonolactone oxidase.
  JOURNAL   Eur. J. Biochem. 127 (1982) 391-6.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K05276  L-galactonolactone oxidase
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.3.12
            ExPASy - ENZYME nomenclature database: 1.3.3.12
            ExplorEnz - The Enzyme Database: 1.3.3.12
            ERGO genome analysis and discovery system: 1.3.3.12
            BRENDA, the Enzyme Database: 1.3.3.12
            CAS: 69403-13-0
///
ENTRY       EC 1.3.5.1                  Enzyme
NAME        succinate dehydrogenase (ubiquinone);
            succinic dehydrogenase;
            complex II;
            menaquinol: fumarate oxidoreductase;
            fumarate reductase complex (i.e. FRD, involved in anaerobic
            respiration, repressed in aerobic respiration);
            succinate dehydrogenase complex (i. e. SDH, involved in aerobic
            respiration, repressed in anaerobic respiration)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With a quinone or related compound as acceptor
SYSNAME     succinate:ubiquinone oxidoreductase
REACTION    succinate + ubiquinone = fumarate + ubiquinol [RN:R02164]
ALL_REAC    R02164
SUBSTRATE   succinate [CPD:C00042];
            ubiquinone [CPD:C00399]
PRODUCT     fumarate [CPD:C00122];
            ubiquinol [CPD:C00390]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023];
            Sulfur [CPD:C00087];
            Iron-sulfur [CPD:C00824]
COMMENT     A flavoprotein (FAD) containing iron-sulfur centres. The complex,
            present in mitochondria, can be degraded to form EC 1.3.99.1
            succinate dehydrogenase, which no longer reacts with ubiquinone.
REFERENCE   1
  AUTHORS   Hatefi, Y., Ragan, C.I. and Galante, Y.M.
  TITLE     The enzymes and the enzyme complexes of the mitochondrial oxidative
            phosphorylation system.
  JOURNAL   In: Martonosi, A. (Ed.), The Enzymes of Biological Membranes, 2nd
            ed., vol. 4, Plenum Press, New York, 1985, p. 1-70.
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00190  Oxidative phosphorylation
ORTHOLOGY   KO: K00233  succinate dehydrogenase (ubiquinone)
            KO: K00234  succinate dehydrogenase (ubiquinone) flavoprotein
                        subunit precursor
            KO: K00235  succinate dehydrogenase (ubiquinone) iron-sulfur protein
                        precursor
            KO: K00236  succinate dehydrogenase (ubiquinone) cytochrome b
                        subunit precursor
            KO: K00237  succinate dehydrogenase (ubiquinone) membrane anchor
                        subunit
GENES       HSA: 6389(SDHA) 6390(SDHB) 6391(SDHC) 6392(SDHD)
            PTR: 451547(SDHD)
            MMU: 66052(Sdhc) 66925(Sdhd) 66945(Sdha) 67680(Sdhb)
            RNO: 157074(Sdha) 289217(Sdhc) 298596(Sdhb_predicted) 363061(Sdhd)
            CFA: 478634(SDHA) 479438(LOC479438) 608210(SDHB)
            BTA: 281480(SDHA) 281481(SDHD) 286840(SDHB) 327696(SDHC)
            GGA: 395758(SDHA) 419793(SDHD) 770063(SDHB)
            XLA: 379939(sdhb) 380463(sdha) 398946(MGC68518) 496372(LOC496372)
            XTR: 394986(MGC75661)
            DRE: 393884(sdha)
            SPU: 580610(LOC580610) 588082(LOC588082) 589263(LOC589263)
            DME: Dmel_CG10219 Dmel_CG17246(Scs-fp) Dmel_CG3283(SdhB)
                 Dmel_CG6629 Dmel_CG7349
            CEL: C03G5.1(sdha-1) C34B2.7(flavoprotein) F33A8.5(sdhd-1)
                 F42A8.2(sdhb-1) T07C4.7(mev-1)
            ATH: AT2G18450(SDH1-2) AT3G27380(SDH2-1) AT5G40650(SDH2-2)
                 AT5G65165(SDH2-3) AT5G66760(SDH1-1)
            OSA: 4342350 4344541 4346890
            CME: CMT582C
            SCE: YDR178W(SDH4) YJL045W YKL141W(SDH3) YKL148C(SDH1)
                 YLL041C(SDH2) YLR164W YMR118C
            AGO: AGOS_ACL065C AGOS_ACR052W AGOS_AFR207C AGOS_AGL137W
            PIC: PICST_35527(SDH6) PICST_50416(SDH2) PICST_66251(SDH1)
                 PICST_90476(SDH4)
            CAL: CaO19.4468(sdh4) CaO19_2871(CaO19.2871)
            CGR: CAGL0C03223g CAGL0D01958g CAGL0E03850g CAGL0F05863g
                 CAGL0J00847g
            SPO: SPAC140.01(sdh2) SPAC1556.02c SPBP23A10.16 SPCC330.12c
            ANI: AN0896.2 AN2332.2 AN2916.2
            AFM: AFUA_1G15590 AFUA_3G07810 AFUA_5G09680 AFUA_5G10370
            AOR: AO090010000505 AO090020000415 AO090020000596
            CNE: CNB00800 CNG03480 CNI03270
            UMA: UM00844.1 UM01172.1 UM03845.1
            DDI: DDB_0214886(sdhA) DDB_0231383(sdhB) DDB_0231385(sdhC)
                 DDB_0231386(sdhD)
            PFA: PF10_0334 PFL0630w
            TAN: TA03455 TA19430
            TPV: TP01_0210 TP03_0230
            TET: TTHERM_00047080 TTHERM_00241700
            TBR: Tb927.8.6580
            TCR: 511909.40
            LMA: LmjF24.1630
            YPA: YPA_3924
            YPN: YPN_3312
            YPP: YPDSF_2585 YPDSF_3615
            ENT: Ent638_0342 Ent638_1225
            PMY: Pmen_2504
            PRW: PsycPRwf_0264
            SFR: Sfri_0458 Sfri_0678
            SAZ: Sama_1426 Sama_3219
            SBL: Sbal_2516 Sbal_3934
            SLO: Shew_0335 Shew_1654
            SPC: Sputcn32_0353 Sputcn32_2270 Sputcn32_3438
            SSE: Ssed_2815
            SHE: Shewmr4_0405
            SHM: Shewmr7_3620
            SHN: Shewana3_0404 Shewana3_2473
            SHW: Sputw3181_0203 Sputw3181_0501 Sputw3181_1738
            PHA: PSHAa1648(sdhB)
            SDE: Sde_2107
            PIN: Ping_2253(sucA) Ping_3279
            MAQ: Maqu_1153
            FTW: FTW_0148(sdhC)
            TCX: Tcr_2028
            NOC: Noc_2470
            HHA: Hhal_0043 Hhal_1449
            REU: Reut_A2322
            RME: Rmet_2483
            BVI: Bcep1808_4413 Bcep1808_5821
            BUR: Bcep18194_B2149
            BCN: Bcen_4430
            BCH: Bcen2424_3937 Bcen2424_6506
            BAM: Bamb_3314
            BPM: BURPS1710b_A0792(sdhD)
            PNU: Pnuc_0761
            RFR: Rfer_1798
            POL: Bpro_3603
            PNA: Pnap_3035
            AAV: Aave_2201
            AJS: Ajs_2796
            VEI: Veis_4351
            HAR: HEAR1775(sdhB) HEAR3327(frdB)
            NET: Neut_0863
            NMU: Nmul_A0860
            EBA: ebB235(sdhD)
            TDN: Tmden_1029
            RAK: A1C_00955(sdhA)
            RBO: A1I_01460(sdhA)
            RCM: A1E_00665(sdhA)
            RRI: A1G_00980(sdhA)
            AMA: AM168(sdhA) AM169(sdhB)
            PLA: Plav_1435 Plav_1436
            SMD: Smed_2956 Smed_2957
            OAN: Oant_0953 Oant_0954
            NWI: Nwi_2801(sdhB)
            XAU: Xaut_1964 Xaut_1965
            RSH: Rsph17029_2639 Rsph17029_3887
            RSQ: Rsph17025_0088 Rsph17025_0091
            JAN: Jann_0804 Jann_3966
            PDE: Pden_0572 Pden_3022
            NAR: Saro_2322
            SAL: Sala_2234
            SWI: Swit_1304 Swit_1310
            ACR: Acry_1881 Acry_1882
            MGM: Mmc1_0429
            MVA: Mvan_1586
            MGI: Mflv_4847
            MKM: Mkms_1244
            MJL: Mjls_1253
            ART: Arth_1128
            AVA: Ava_0523
            CCH: Cag_0128
            CPH: Cpha266_0176
            PVI: Cvib_1637
            PLT: Plut_1994
            IHO: Igni_0276 Igni_0445
            PIS: Pisl_0670
            PCL: Pcal_2128
            PAS: Pars_2359
            TPE: Tpen_1126
STRUCTURES  PDB: 1NEK  1NEN  1YQ3  1YQ4  1ZOY  1ZP0  2FBW  2H88  2H89  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.5.1
            ExPASy - ENZYME nomenclature database: 1.3.5.1
            ExplorEnz - The Enzyme Database: 1.3.5.1
            ERGO genome analysis and discovery system: 1.3.5.1
            BRENDA, the Enzyme Database: 1.3.5.1
            CAS: 9028-11-9
///
ENTRY       EC 1.3.7.1                  Enzyme
NAME        6-hydroxynicotinate reductase;
            6-oxotetrahydronicotinate dehydrogenase;
            6-hydroxynicotinic reductase;
            HNA reductase;
            1,4,5,6-tetrahydro-6-oxonicotinate:ferredoxin oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With an iron-sulfur protein as acceptor
SYSNAME     6-oxo-1,4,5,6-tetrahydronicotinate:ferredoxin oxidoreductase
REACTION    6-oxo-1,4,5,6-tetrahydronicotinate + oxidized ferredoxin =
            6-hydroxynicotinate + reduced ferredoxin [RN:R03164]
ALL_REAC    R03164
SUBSTRATE   6-oxo-1,4,5,6-tetrahydronicotinate [CPD:C04226];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     6-hydroxynicotinate [CPD:C01020];
            reduced ferredoxin [CPD:C00138]
REFERENCE   1  [PMID:5767303]
  AUTHORS   Holcenberg JS, Tsai L.
  TITLE     Nicotinic acid metabolism. IV. Ferredoxin-dependent reduction of
            6-hydroxynicotinic acid to 6-oxo-1,4,5,6-tetrahydronicotinic acid.
  JOURNAL   J. Biol. Chem. 244 (1969) 1204-11.
  ORGANISM  Clostridium sp.
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.7.1
            ExPASy - ENZYME nomenclature database: 1.3.7.1
            ExplorEnz - The Enzyme Database: 1.3.7.1
            ERGO genome analysis and discovery system: 1.3.7.1
            BRENDA, the Enzyme Database: 1.3.7.1
            CAS: 9030-84-6
///
ENTRY       EC 1.3.7.2                  Enzyme
NAME        15,16-dihydrobiliverdin:ferredoxin oxidoreductase;
            PebA
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With an iron-sulfur protein as acceptor
SYSNAME     15,16-dihydrobiliverdin:ferredoxin oxidoreductase
REACTION    15,16-dihydrobiliverdin + oxidized ferredoxin = biliverdin IXalpha +
            reduced ferredoxin [RN:R05818]
ALL_REAC    R05818
SUBSTRATE   15,16-dihydrobiliverdin [CPD:C11630];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     biliverdin IXalpha [CPD:C00500];
            reduced ferredoxin [CPD:C00138]
COMMENT     Catalyses the two-electron reduction of biliverdin IXalpha at the
            C15 methine bridge. It has been proposed that this enzyme and EC
            1.3.7.3, phycoerythrobilin:ferredoxin oxidoreductase, function as a
            dual enzyme complex in the conversion of biliverdin IXalpha into
            phycoerythrobilin.
REFERENCE   1  [PMID:11283349]
  AUTHORS   Frankenberg N, Mukougawa K, Kohchi T, Lagarias JC.
  TITLE     Functional genomic analysis of the HY2 family of
            ferredoxin-dependent bilin reductases from oxygenic photosynthetic
            organisms.
  JOURNAL   Plant. Cell. 13 (2001) 965-78.
  ORGANISM  Synechococcus sp., Nostoc punctiforme, Prochlorococcus sp.
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K05369  15,16-dihydrobiliverdin:ferredoxin oxidoreductase
GENES       SYW: SYNW2020(pebA)
            SYD: Syncc9605_0423
            SYE: Syncc9902_1906
            SYG: sync_0491
            SYR: SynRCC307_2061(pebA)
            SYX: SynWH7803_0482(pebA)
            GVI: glr1260(pebA)
            PMA: Pro1749(pebA)
            PMM: PMM1593(pebA)
            PMT: PMT1686(pebA)
            PMN: PMN2A_1168
            PMB: A9601_18021(pebA)
            PMC: P9515_17801(pebA)
            PMF: P9303_22431(pebA)
            PMG: P9301_17851(pebA)
            PME: NATL1_20431(pebA)
            TER: Tery_5051
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.7.2
            ExPASy - ENZYME nomenclature database: 1.3.7.2
            ExplorEnz - The Enzyme Database: 1.3.7.2
            ERGO genome analysis and discovery system: 1.3.7.2
            BRENDA, the Enzyme Database: 1.3.7.2
            CAS: 347401-20-1
///
ENTRY       EC 1.3.7.3                  Enzyme
NAME        phycoerythrobilin:ferredoxin oxidoreductase;
            PebB
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With an iron-sulfur protein as acceptor
SYSNAME     (3Z)-phycoerythrobilin:ferredoxin oxidoreductase
REACTION    (3Z)-phycoerythrobilin + oxidized ferredoxin =
            15,16-dihydrobiliverdin + reduced ferredoxin [RN:R05819]
ALL_REAC    R05819
SUBSTRATE   (3Z)-phycoerythrobilin [CPD:C05912];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     15,16-dihydrobiliverdin [CPD:C11630];
            reduced ferredoxin [CPD:C00138]
COMMENT     Catalyses the two-electron reduction of the C2 and C31 diene system
            of 15,16-dihydrobiliverdin. Specific for 15,16-dihydrobiliverdin. It
            has been proposed that this enzyme and EC 1.3.7.2,
            15,16-dihydrobiliverdin:ferredoxin oxidoreductase, function as a
            dual enzyme complex in the conversion of biliverdin IXalpha to
            phycoerythrobilin.
REFERENCE   1  [PMID:11283349]
  AUTHORS   Frankenberg N, Mukougawa K, Kohchi T, Lagarias JC.
  TITLE     Functional genomic analysis of the HY2 family of
            ferredoxin-dependent bilin reductases from oxygenic photosynthetic
            organisms.
  JOURNAL   Plant. Cell. 13 (2001) 965-78.
  ORGANISM  Synechococcus sp., Nostoc punctiforme, Prochlorococcus sp.
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K05370  phycoerythrobilin:ferredoxin oxidoreductase
GENES       SYW: SYNW2021(pebB)
            SYD: Syncc9605_0422
            SYE: Syncc9902_1907
            SYG: sync_0490(pebB)
            SYR: SynRCC307_2062(pebB)
            SYX: SynWH7803_0481(pebB)
            GVI: glr1261(pebB)
            PMA: Pro1748(pebB)
            PMM: PMM1592(pebB)
            PMT: PMT1687(pebB)
            PMN: PMN2A_1167(pebB)
            PMB: A9601_18011(pebB)
            PMC: P9515_17791(pebB)
            PMF: P9303_22441(pebB)
            PMG: P9301_17841(pebB)
            PME: NATL1_20421(pebB)
            TER: Tery_5050
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.7.3
            ExPASy - ENZYME nomenclature database: 1.3.7.3
            ExplorEnz - The Enzyme Database: 1.3.7.3
            ERGO genome analysis and discovery system: 1.3.7.3
            BRENDA, the Enzyme Database: 1.3.7.3
            CAS: 347401-21-2
///
ENTRY       EC 1.3.7.4                  Enzyme
NAME        phytochromobilin:ferredoxin oxidoreductase;
            HY2;
            PPhiB synthase;
            phytochromobilin synthase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With an iron-sulfur protein as acceptor
SYSNAME     (3Z)-phytochromobilin:ferredoxin oxidoreductase
REACTION    (3Z)-phytochromobilin + oxidized ferredoxin = biliverdin IXalpha +
            reduced ferredoxin [RN:R03678]
ALL_REAC    R03678
SUBSTRATE   (3Z)-phytochromobilin [CPD:C05913];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     biliverdin IXalpha [CPD:C00500];
            reduced ferredoxin [CPD:C00138]
COMMENT     Catalyses the two-electron reduction of biliverdin IXalpha. Can use
            2Fe-2S ferredoxins from a number of sources as acceptor but not the
            4Fe-4S ferredoxin from Clostridium pasteurianum. The isomerization
            of (3Z)-phytochromobilin to (3E)-phytochromobilin is thought to
            occur prior to covalent attachment to apophytochrome in the plant
            cell cytoplasm. Flavodoxins can be used instead of ferredoxin.
REFERENCE   1  [PMID:11283349]
  AUTHORS   Frankenberg N, Mukougawa K, Kohchi T, Lagarias JC.
  TITLE     Functional genomic analysis of the HY2 family of
            ferredoxin-dependent bilin reductases from oxygenic photosynthetic
            organisms.
  JOURNAL   Plant. Cell. 13 (2001) 965-78.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   2  [PMID:11500553]
  AUTHORS   McDowell MT, Lagarias JC.
  TITLE     Purification and biochemical properties of phytochromobilin synthase
            from etiolated oat seedlings.
  JOURNAL   Plant. Physiol. 126 (2001) 1546-54.
  ORGANISM  Avena sativa
REFERENCE   3  [PMID:8215388]
  AUTHORS   Terry MJ, Wahleithner JA, Lagarias JC.
  TITLE     Biosynthesis of the plant photoreceptor phytochrome.
  JOURNAL   Arch. Biochem. Biophys. 306 (1993) 1-15.
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K08101  phytochromobilin:ferredoxin oxidoreductase
GENES       ATH: AT3G09150(HY2)
            OSA: 4325761
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.7.4
            ExPASy - ENZYME nomenclature database: 1.3.7.4
            ExplorEnz - The Enzyme Database: 1.3.7.4
            ERGO genome analysis and discovery system: 1.3.7.4
            BRENDA, the Enzyme Database: 1.3.7.4
            CAS: 138263-99-7
///
ENTRY       EC 1.3.7.5                  Enzyme
NAME        phycocyanobilin:ferredoxin oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With an iron-sulfur protein as acceptor
SYSNAME     (3Z)-phycocyanobilin:ferredoxin oxidoreductase
REACTION    (3Z)-phycocyanobilin + oxidized ferredoxin = biliverdin IXalpha +
            reduced ferredoxin [RN:R05817]
ALL_REAC    R05817
SUBSTRATE   (3Z)-phycocyanobilin [CPD:C05786];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     biliverdin IXalpha [CPD:C00500];
            reduced ferredoxin [CPD:C00138]
COMMENT     Catalyses the four-electron reduction of biliverdin IXalpha
            (2-electron reduction at both the A and D rings). Reaction proceeds
            via an isolatable 2-electron intermediate,
            181,182-dihydrobiliverdin. Flavodoxins can be used instead of
            ferredoxin.The direct conversion of biliverdin IXalpha (BV) to
            (3Z)-phycocyanolbilin (PCB) in the cyanobacteria Synechocystis sp
            PCC 6803, Anabaena sp PCC7120 and Nostoc punctiforme is in contrast
            to the proposed pathways of PCB biosynthesis in the red alga
            Cyanidium caldarium, which involves (3Z)-phycoerythrobilin (PEB) as
            an intermediate [2] and in the green alga Mesotaenium caldariorum,
            in which PCB is an isolable intermediate.
REFERENCE   1  [PMID:11283349]
  AUTHORS   Frankenberg N, Mukougawa K, Kohchi T, Lagarias JC.
  TITLE     Functional genomic analysis of the HY2 family of
            ferredoxin-dependent bilin reductases from oxygenic photosynthetic
            organisms.
  JOURNAL   Plant. Cell. 13 (2001) 965-78.
  ORGANISM  Synechocystis sp. , Anabaena sp., Nostoc punctiforme
REFERENCE   2
  AUTHORS   Beale, S.I.
  TITLE     Biosynthesis of phycobilins.
  JOURNAL   Chem. Rev. 93 (1993) 785-802.
  ORGANISM  Cyanldlum caldarlum
REFERENCE   3  [PMID:9325294]
  AUTHORS   Wu SH, McDowell MT, Lagarias JC.
  TITLE     Phycocyanobilin is the natural precursor of the phytochrome
            chromophore in the green alga Mesotaenium caldariorum.
  JOURNAL   J. Biol. Chem. 272 (1997) 25700-5.
  ORGANISM  Mesotaenium caldariorum
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K05371  phycocyanobilin:ferredoxin oxidoreductase
GENES       BRA: BRADO1265
            SYN: slr0116(pcyA)
            SYW: SYNW1084(pcyA)
            SYC: syc0325_d
            SYF: Synpcc7942_1225
            SYD: Syncc9605_1216
            SYE: Syncc9902_1253
            SYG: sync_1656(pcyA)
            SYR: SynRCC307_1284(pcyA)
            SYX: SynWH7803_1335(pcyA)
            CYA: CYA_2492(pcyA)
            CYB: CYB_0698(pcyA)
            TEL: tll2308(pcyA)
            GVI: glr2589(pcyA)
            ANA: alr3707(pcyA)
            AVA: Ava_3585
            PMA: Pro0819(pcyA)
            PMM: PMM0747(pcyA)
            PMT: PMT0590(pcyA)
            PMN: PMN2A_0151
            PMI: PMT9312_0755
            PMB: A9601_08081(pcyA)
            PMC: P9515_08371(pcyA)
            PMF: P9303_16581(pcyA)
            PMG: P9301_08071(pcyA)
            PME: NATL1_07831(pcyA)
            TER: Tery_4156
STRUCTURES  PDB: 2D1E  2DKE  2G18  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.7.5
            ExPASy - ENZYME nomenclature database: 1.3.7.5
            ExplorEnz - The Enzyme Database: 1.3.7.5
            ERGO genome analysis and discovery system: 1.3.7.5
            BRENDA, the Enzyme Database: 1.3.7.5
            CAS: 347401-12-1
///
ENTRY       EC 1.3.99.1                 Enzyme
NAME        succinate dehydrogenase;
            succinic dehydrogenase;
            fumarate reductase;
            fumaric hydrogenase;
            succinodehydrogenase;
            succinic acid dehydrogenase;
            succinate oxidoreductase;
            succinyl dehydrogenase;
            succinate:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     succinate:acceptor oxidoreductase
REACTION    succinate + acceptor = fumarate + reduced acceptor [RN:R00412]
ALL_REAC    R00412 > R00408
SUBSTRATE   succinate [CPD:C00042];
            acceptor [CPD:C00028]
PRODUCT     fumarate [CPD:C00122];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023];
            Sulfur [CPD:C00087]
COMMENT     A flavoprotein (FAD) containing iron-sulfur centres. A component of
            EC 1.3.5.1 succinate dehydrogenase (ubiquinone).
REFERENCE   1
  AUTHORS   Hatefi, Y., Ragan, C.I. and Galante, Y.M.
  TITLE     The enzymes and the enzyme complexes of the mitochondrial oxidative
            phosphorylation system.
  JOURNAL   In: Martonosi, A. (Ed.), The Enzymes of Biological Membranes, 2nd
            ed., vol. 4, Plenum Press, New York, 1985, p. 1-70.
REFERENCE   2
  AUTHORS   Singer, T.P. and Kearney, E.B.
  TITLE     Succinate dehydrogenase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 383-445.
REFERENCE   3
  AUTHORS   Singer, T.P., Kearney, E.B. and Bernath, P.
  TITLE     Studies of succinic dehydrogenase. II. Isolation and properties of
            the dehydrogenase from beef heart.
  JOURNAL   J. Biol. Chem. 223 (1956) 599-613.
  ORGANISM  cow [GN:bta]
REFERENCE   4
  AUTHORS   Warringa, M.G.P.J. and Giuditta, A.
  TITLE     Studies on succinic dehydrogenase. IX. Characterization of the
            enzyme from Micrococcus lactilyticus.
  JOURNAL   J. Biol. Chem. 230 (1958) 111-123.
  ORGANISM  Micrococcus lactilyticus
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00190  Oxidative phosphorylation
            PATH: map00632  Benzoate degradation via CoA ligation
            PATH: map00650  Butanoate metabolism
            PATH: map00720  Reductive carboxylate cycle (CO2 fixation)
            PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K00238  succinate dehydrogenase
            KO: K00239  succinate dehydrogenase flavoprotein subunit
            KO: K00240  succinate dehydrogenase iron-sulfur protein
            KO: K00241  succinate dehydrogenase cytochrome b-556 subunit
            KO: K00242  succinate dehydrogenase hydrophobic membrane anchor
                        protein
            KO: K00244  fumarate reductase flavoprotein subunit
            KO: K00245  fumarate reductase iron-sulfur protein
            KO: K00246  fumarate reductase subunit C
            KO: K00247  fumarate reductase subunit D
GENES       PIC: PICST_35330(SDH5) PICST_45689(OSM1)
            AFM: AFUA_4G14850 AFUA_7G05070 AFUA_8G05530
            TAN: TA19430
            TCR: 504949.30
            ECO: b0721(sdhC) b0722(sdhD) b0723(sdhA) b0724(sdhB) b4151(frdD)
                 b4152(frdC) b4153(frdB) b4154(frdA)
            ECJ: JW0711(sdhC) JW0712(sdhD) JW0713(sdhA) JW0714(sdhB)
                 JW4112(frdD) JW4113(frdC) JW4114(frdB) JW4115(frdA)
            ECE: Z0875(sdhC) Z0876(sdhD) Z0877(sdhA) Z0878(sdhB) Z5758(frdD)
                 Z5759(frdC) Z5760(frdB) Z5762(frdA)
            ECS: ECs0746 ECs0747 ECs0748 ECs0749 ECs5132 ECs5133 ECs5134
                 ECs5135
            ECC: c0798(sdhC) c0800(sdhD) c0801(sdhA) c0802(sdhB) c5239(frdD)
                 c5240(frdC) c5241(frdB) c5242(frdA)
            ECI: UTI89_C0120(aroP) UTI89_C0717(sdhC) UTI89_C0718(sdhD)
                 UTI89_C0719(sdhA) UTI89_C0720(sdhB) UTI89_C4751(frdD)
                 UTI89_C4752(frdC) UTI89_C4753(frdB) UTI89_C4754(frdA)
            ECP: ECP_0733 ECP_0734 ECP_0735 ECP_0736 ECP_4397 ECP_4398
                 ECP_4399 ECP_4400
            ECV: APECO1_1354(sdhB) APECO1_1355(sdhA) APECO1_1356(sdhD)
                 APECO1_1357(sdhC) APECO1_2235(frdA) APECO1_2236(frdB)
                 APECO1_2237(frdC) APECO1_2238(frdD)
            ECW: EcE24377A_0751(sdhB) EcE24377A_4712(frdB)
                 EcE24377A_4713(frdA)
            ECX: EcHS_A0772(sdhB) EcHS_A4397(frdB) EcHS_A4398(frdA)
            STY: STY0775(sdhC) STY0776(sdhD) STY0777(sdhA) STY0778(sdhB)
                 STY4700(frdD) STY4701(frdC) STY4702(frdB) STY4703(frdA)
            STT: t2141(sdhB) t2142(sdhA) t2143(sdhD) t2144(sdhC) t4392(frdD)
                 t4393(frdC) t4394(frdB) t4395(frdA)
            SPT: SPA2008(sdhB) SPA2009(sdhA) SPA2010(sdhD) SPA2011(sdhC)
                 SPA4157(frdD) SPA4158(frdC) SPA4159(frdB) SPA4160(frdA)
            SEC: SC0737(sdhC) SC0738(sdhA) SC0739(sdhB) SC4219(frdD)
                 SC4220(frdC) SC4221(frdB) SC4222(frdA)
            STM: STM0732(sdhC) STM0733(sdhD) STM0734(sdhA) STM0735(sdhB)
                 STM4340(frdD) STM4341(frdC) STM4342(frdB) STM4343(frdA)
            YPE: YPO0357(frdD) YPO0358(frdC) YPO0359(frdB) YPO0360(frdA)
                 YPO1109(sdhC) YPO1110(sdhD) YPO1111(sdhA) YPO1112(sdhB)
            YPK: y0614(frdD) y0615(frdC) y0616(frdB) y0617(frdA) y3068(sdhB)
                 y3069(sdhA) y3070(sdhD) y3071(sdhC)
            YPM: YP_0512(frdD) YP_0513(frdC) YP_0514(frdB) YP_0515(frdA)
                 YP_1044(sdhB) YP_1045(sdhA) YP_1046(sdhD) YP_1047(sdhC)
            YPA: YPA_0587 YPA_0588 YPA_0589 YPA_0590 YPA_3923 YPA_3925
                 YPA_3926
            YPN: YPN_2886 YPN_2887 YPN_2888 YPN_2889 YPN_3311 YPN_3313
                 YPN_3314
            YPP: YPDSF_2586 YPDSF_3614
            YPS: YPTB0410(frdD) YPTB0411(frdC) YPTB0412(frdB) YPTB0413(frdA)
                 YPTB1143(sdhC) YPTB1144(sdhD) YPTB1145(sdhA) YPTB1146(sdhB)
            YPI: YpsIP31758_2882(sdhB) YpsIP31758_2883(sdhA)
                 YpsIP31758_3667(frdA) YpsIP31758_3668(frdB)
            SFL: SF0573(sdhB) SF0574(sdhA) SF0575(sdhD) SF0576(sdhC)
                 SF4309(frdD) SF4310(frdC) SF4311(frdB) SF4312(frdA)
            SFX: S0586(sdhB) S0587(sdhA) S0588(sdhD) S0589(sdhC) S4574(frdD)
                 S4575(frdC) S4576(frdB) S4577(frdA)
            SFV: SFV_0611(sdhB) SFV_0612(sdhA) SFV_0613(sdhD) SFV_0614(sdhC)
                 SFV_4310(frdD) SFV_4311(frdC) SFV_4312(frdB) SFV_4313(frdA)
            SSN: SSON_0672(sdhC) SSON_0673(sdhD) SSON_0674(sdhA)
                 SSON_0675(sdhB) SSON_4337(frdD) SSON_4338(frdC)
                 SSON_4339(frdB) SSON_4340(frdA)
            SBO: SBO_0579(sdhC) SBO_0580(sdhD) SBO_0581(sdhA) SBO_0582(sdhB)
                 SBO_4302(frdA) SBO_4303(frdB) SBO_4304(frdC) SBO_4305(frdD)
            SDY: SDY_0659(sdhC) SDY_0660(sdhD) SDY_0661(sdhA) SDY_0662(sdhB)
                 SDY_4395(frdD) SDY_4396(frdC) SDY_4397(frdB) SDY_4398(frdA)
            ECA: ECA1357(sdhC) ECA1358(sdhD) ECA1359(sdhA) ECA1360(sdhB)
                 ECA3969(frdA) ECA3970(frdB) ECA3971(frdC) ECA3972(frdD)
            PLU: plu1426(sdhC) plu1427(sdhD) plu1428(sdhA) plu1429(sdhB)
                 plu4124(frdA) plu4125(frdB) plu4126(frdC) plu4127(frdD)
            WBR: WGLp420(sdhB) WGLp421(sdhA) WGLp422(sdhD) WGLp423(sdhC)
            SGL: SG0872 SG0873 SG0874 SG0875 SG1547 SG1548
            ENT: Ent638_0343 Ent638_1224
            KPN: KPN_00730(sdhA)
            SPE: Spro_0418 Spro_0419 Spro_1265 Spro_1266
            BFL: Bfl327(sdhC) Bfl328(sdhD) Bfl329(sdhA) Bfl330(sdhB)
            BPN: BPEN_337(sdhC) BPEN_338(sdhD) BPEN_339(sdhA) BPEN_340(sdhB)
            HIN: HI0832(frdD) HI0833(frdC) HI0834(frdB) HI0835(frdA)
            HIT: NTHI0998(frdD) NTHI0999(frdC) NTHI1000(frdB) NTHI1002(frdA)
            HIP: CGSHiEE_07885 CGSHiEE_07890
            HIQ: CGSHiGG_07675
            HDU: HD0030(frdA) HD0032(frdB) HD0033(frdC) HD0034(frdD)
            HSO: HS_1277(frdA) HS_1278(frdB) HS_1279(frdC) HS_1280(frdD)
            PMU: PM0198(frdD) PM0199(frdC) PM0200(frdB) PM0201(frdA)
            MSU: MS1652(sdhA) MS1653(frdB) MS1654(frdC) MS1655(frdD)
            APL: APL_1526(frdD) APL_1527(frdC) APL_1528(frdB) APL_1529(frdA)
            ASU: Asuc_1813 Asuc_1814
            XFA: XF1070 XF1071 XF1072 XF1073
            XFT: PD0350 PD0351(sdhD) PD0352(sdhA) PD0353(sdhB)
            XCC: XCC2129(sdhB) XCC2130(sdhA) XCC2131(sdhD) XCC2132(sdhC)
            XCB: XC_1981 XC_1982 XC_1983 XC_1985
            XCV: XCV2241 XCV2242 XCV2243(sdhA) XCV2245
            XAC: XAC2075(sdhC) XAC2076(sdhD) XAC2077(sdhA) XAC2078(sdhB)
            XOO: XOO2307(sdhB) XOO2308(sdhA) XOO2309(sdhD) XOO2310(sdhC)
            XOM: XOO_2185(XOO2185) XOO_2186(XOO2186) XOO_2187(XOO2187)
                 XOO_2188(XOO2188)
            VCH: VC2088 VC2089 VC2090 VC2091 VC2656 VC2657 VC2658 VC2659
            VCO: VC0395_A1674(sdhB) VC0395_A1675(sdhA) VC0395_A2230(frdA)
                 VC0395_A2231(frdB)
            VVU: VV1_0158 VV1_0159 VV1_0160 VV1_0161 VV1_1266 VV1_1267
                 VV1_1268 VV1_1269
            VVY: VV1028 VV1029 VV1030 VV1031 VV3097 VV3098 VV3099 VV3100
            VPA: VP0843 VP0844 VP0845 VP0846 VP2840 VP2841 VP2842 VP2843
            VFI: VF0819 VF0820 VF0821 VF0822 VF2334 VF2335 VF2336 VF2337
            PPR: PBPRA1044 PBPRA1045 PBPRA1046 PBPRA1047 PBPRA3378 PBPRA3379
                 PBPRA3380(frdC) PBPRA3381
            PAE: PA1581(sdhC) PA1582(sdhD) PA1583(sdhA) PA1584(sdhB)
            PAU: PA14_44020(sdhB) PA14_44030(sdhA) PA14_44050(sdhD)
                 PA14_44060(sdhC)
            PPU: PP_4190(sdhB) PP_4191(sdhA) PP_4192(sdhD) PP_4193(sdhC)
            PPF: Pput_1663 Pput_1664
            PST: PSPTO_2195(sdhC) PSPTO_2196 PSPTO_2197(sdhA) PSPTO_2198(sdhB)
            PSB: Psyr_2005 Psyr_2006 Psyr_2007 Psyr_2008
            PSP: PSPPH_1976(sdhC) PSPPH_1977(sdhD) PSPPH_1978(sdhA)
                 PSPPH_1979(sdhB)
            PFL: PFL_1714(sdhC) PFL_1715(sdhD) PFL_1716(sdhA) PFL_1717(sdhB)
            PFO: Pfl_1610 Pfl_1611 Pfl_1612
            PEN: PSEEN0175 PSEEN3641(sdhB) PSEEN3642(sdhA) PSEEN3643(sdhD)
                 PSEEN3644(sdhC)
            PMY: Pmen_2505
            PAR: Psyc_0098(sdhC) Psyc_0099(sdhD) Psyc_0100(sdhA)
                 Psyc_0101(sdhB)
            PCR: Pcryo_0107 Pcryo_0108 Pcryo_0109 Pcryo_0110
            PRW: PsycPRwf_0263
            ACI: ACIAD2879(sdhB) ACIAD2880(sdhA) ACIAD2881(sdhD)
                 ACIAD2882(sdhC)
            SON: SO_0396(frdC) SO_0397(fdrC) SO_0398(frdA) SO_0399(frdB)
                 SO_0970 SO_1421(ifcA-1) SO_1927(sdhC) SO_1927.1 SO_1928(sdhA)
                 SO_1929(sdhB) SO_4620(ifcA-2)
            SDN: Sden_2184 Sden_2185 Sden_2186 Sden_2187
            SFR: Sfri_0457 Sfri_0679 Sfri_0680 Sfri_2344 Sfri_2345 Sfri_2346
                 Sfri_2347 Sfri_3690
            SAZ: Sama_1425 Sama_3220
            SBL: Sbal_2517 Sbal_3750 Sbal_3935
            SBM: Shew185_0615 Shew185_2509 Shew185_2510 Shew185_3959
                 Shew185_3960
            SLO: Shew_0334 Shew_1653 Shew_3112
            SPC: Sputcn32_0354 Sputcn32_2271 Sputcn32_2272 Sputcn32_3439
            SSE: Ssed_2816 Ssed_3877 Ssed_4113 Ssed_4114
            SPL: Spea_0394 Spea_0395 Spea_0722 Spea_1786 Spea_1787 Spea_3368
            SHE: Shewmr4_0402 Shewmr4_0403 Shewmr4_0404 Shewmr4_1631
                 Shewmr4_1632 Shewmr4_1633 Shewmr4_1634
            SHM: Shewmr7_1706 Shewmr7_1707 Shewmr7_1708 Shewmr7_1709
                 Shewmr7_3621 Shewmr7_3622 Shewmr7_3623
            SHN: Shewana3_0401 Shewana3_0402 Shewana3_0403 Shewana3_1706
                 Shewana3_1707 Shewana3_1708 Shewana3_1709 Shewana3_3318
                 Shewana3_4004
            SHW: Sputw3181_0204 Sputw3181_0500 Sputw3181_1736 Sputw3181_1737
            ILO: IL1504(sdhB) IL1505(sdhA) IL1506(sdhD) IL1507(sdhC)
            CPS: CPS_2215(sdhC) CPS_2216(sdhD) CPS_2217(sdhA) CPS_2218(sdhB)
            PHA: PSHAa1649(sdhA) PSHAa1650(sdhD) PSHAa1651(sdhC)
            PAT: Patl_1795 Patl_1796 Patl_1797 Patl_1798
            SDE: Sde_2108 Sde_2109 Sde_2110
            PIN: Ping_2254 Ping_3278
            MAQ: Maqu_1152
            CBU: CBU_1400(sdhB) CBU_1401(sdhA) CBU_1402(sdhD) CBU_1403(sdhC)
            CBD: COXBU7E912_0590(sdhC) COXBU7E912_0591(sdhD)
                 COXBU7E912_0592(sdhA) COXBU7E912_0593(sdhB)
            LPN: lpg0528(sdhC) lpg0529(sdhD) lpg0530(sdhA) lpg0531(sdhB)
            LPF: lpl0574(sdhC) lpl0575(sdhD) lpl0576(sdhA) lpl0577(sdhB)
            LPP: lpp0593(sdhC) lpp0594(sdhD) lpp0595(sdhA) lpp0596(sdhB)
            MCA: MCA1542(sdhB) MCA1548 MCA1549 MCA1550(sdhA)
            FTU: FTT0072(sdhC) FTT0073(sdhD) FTT0074(sdhA) FTT0075(sdhB)
            FTF: FTF0072(sdhC) FTF0073(sdhD) FTF0074(sdhA) FTF0075(sdhB)
            FTW: FTW_0149(sdhD) FTW_0150(sdhA) FTW_0151(sdhB)
            FTL: FTL_1785 FTL_1786 FTL_1787 FTL_1788
            FTH: FTH_1721(sdhB) FTH_1722(sdhA) FTH_1723(sdhD) FTH_1724(sdhC)
            FTN: FTN_1636(sdhB) FTN_1637(sdhA) FTN_1638(sdhD) FTN_1639(sdhC)
            TCX: Tcr_2029
            NOC: Noc_2471
            AEH: Mlg_1332 Mlg_1334 Mlg_1335
            HHA: Hhal_0044 Hhal_1450
            HCH: HCH_04746(sdhB) HCH_04747(sdhA) HCH_04748(sdhD)
                 HCH_04749(sdhC)
            CSA: Csal_1213 Csal_1214 Csal_1215 Csal_1216
            ABO: ABO_1497(sdhB) ABO_1498(sdhA) ABO_1499(sdhD) ABO_1500(sdhC)
            MMW: Mmwyl1_2801 Mmwyl1_2802
            AHA: AHA_1923(sdhC) AHA_1924 AHA_1925(sdhA) AHA_1926
                 AHA_3208(frdA) AHA_3209 AHA_3210 AHA_3211
            DNO: DNO_1026(frdA) DNO_1027(frdB) DNO_1028(frdC) DNO_1029
            NME: NMB0948 NMB0949 NMB0950 NMB0951
            NMA: NMA1143(sdhC) NMA1144(sdhD) NMA1145(sdhA) NMA1146(sdhB)
            NMC: NMC0927(sdhA) NMC0928(sdhB)
            NGO: NGO0920 NGO0921 NGO0922 NGO0923
            CVI: CV_1065(sdhC) CV_1066(sdhD) CV_1067(sdhA) CV_1068(sdhB)
            RSO: RSc1993(sdhB) RSc1994(sdhA) RSc1995(sdhD) RSc1996(sdhC)
            REU: Reut_A2323 Reut_A2324 Reut_A2325
            REH: H16_A2629(sdhB) H16_A2630(sdhA) H16_A2631(sdhD)
                 H16_A2632(sdhC) H16_B0204
            RME: Rmet_2484 Rmet_2485 Rmet_2486
            BMA: BMAA1746(sdhB-1) BMAA1747(sdhA) BMAA1748(sdhD) BMAA1749(sdhC)
                 BMAA1998(sdhB-2)
            BMV: BMASAVP1_1019(sdhB-2) BMASAVP1_1623(sdhA) BMASAVP1_1624(sdhB)
            BML: BMA10299_1307(sdhB-2) BMA10299_1831(sdhA) BMA10299_1832(sdhB)
            BMN: BMA10247_A0501(sdhA) BMA10247_A0502(sdhB)
                 BMA10247_A2285(sdhB-2)
            BXE: Bxe_B2892 Bxe_B2893 Bxe_B2894 Bxe_B2895
            BVI: Bcep1808_4412
            BUR: Bcep18194_A5287 Bcep18194_B1518 Bcep18194_B2150
            BCN: Bcen_1323 Bcen_4431
            BCH: Bcen2424_3936
            BAM: Bamb_3311 Bamb_3312 Bamb_3313
            BPS: BPSS1717(sdhB) BPSS1718(sdhA) BPSS1719 BPSS1720
                 BPSS2262(sdhB)
            BPM: BURPS1710b_A0790(sdhB-1) BURPS1710b_A0791(sdhA)
                 BURPS1710b_A0793(sdhC) BURPS1710b_A1395(sdhB-2)
            BPL: BURPS1106A_A2331(sdhB) BURPS1106A_A2333(sdhD)
                 BURPS1106A_A2334(sdhC)
            BPD: BURPS668_A2469(sdhB) BURPS668_A2471(sdhD)
                 BURPS668_A2472(sdhC)
            BTE: BTH_II0660 BTH_II0661 BTH_II0662(sdhA) BTH_II0663
            PNU: Pnuc_0760
            BPE: BP2360(sdhB) BP2361(sdhA) BP2362(sdhD) BP2363(sdhC)
            BPA: BPP1131 BPP3227(sdhB) BPP3228(sdhA) BPP3229(sdhD)
                 BPP3230(sdhC)
            BBR: BB1347 BB3679(sdhB) BB3680(sdhA) BB3681(sdhD) BB3682(sdhC)
            RFR: Rfer_1799 Rfer_1800 Rfer_1801
            POL: Bpro_3600 Bpro_3601 Bpro_3602
            PNA: Pnap_3034
            AAV: Aave_2202
            AJS: Ajs_2795
            VEI: Veis_2512 Veis_4352
            MPT: Mpe_A2167 Mpe_A2168 Mpe_A2169 Mpe_A2170
            HAR: HEAR1776(sdhA) HEAR3327(frdB) HEAR3333
            MMS: mma_1506(sdhC) mma_1507(sdhD) mma_1508(sdhA) mma_1509(sdhB)
            NEU: NE1046 NE1047(sdhD) NE1048(sdhA) NE2371(sdhB)
            NET: Neut_2484 Neut_2485 Neut_2486
            NMU: Nmul_A0861 Nmul_A0862 Nmul_A0863
            EBA: ebA4576(sdhD) ebA4578(sdhB) ebA6689(sdhB) ebA6690(sdhA)
                 ebB154(sdhC) ebD20(sdhC)
            AZO: azo1549(sdhC) azo1551(sdhA)
            DAR: Daro_1776 Daro_1777 Daro_1778 Daro_2862 Daro_2863 Daro_2864
                 Daro_2865
            TBD: Tbd_1182 Tbd_1183 Tbd_1184 Tbd_1185
            HPY: HP0191(frdB) HP0192(frdA) HP0193(frdC)
            HPJ: jhp0177(frdB) jhp0178(frdA) jhp0179(frdC)
            HPA: HPAG1_0185 HPAG1_0186 HPAG1_0187 HPAG1_0651
            HHE: HH0685(frdC) HH0686(frdA) HH0687(frdB)
            HAC: Hac_0376(frdB) Hac_0377(frdA) Hac_0378(frdC)
            WSU: WS0829(frdC2) WS0830(frdB) WS0831(frdA) WS0832(frdC)
                 WS1399(frdA) WS1920(sdhA) WS1921(sdhB) WS1922(sdhC)
            TDN: Tmden_0037 Tmden_1028 Tmden_1030
            CJE: Cj0408(frdC) Cj0409(frdA) Cj0410(frdB) Cj0437(sdhA)
                 Cj0438(sdhB) Cj0439(sdhC)
            CJR: CJE0457(frdC) CJE0458(frdA) CJE0459(frdB) CJE0488(sdhA)
                 CJE0489(sdhB) CJE0490(sdhC)
            CJJ: CJJ81176_0433(frdA) CJJ81176_0434(frdB) CJJ81176_0463(sdhA)
                 CJJ81176_0464(sdhB) CJJ81176_0465(sdhC)
            CJU: C8J_0383(frdC) C8J_0384(frdA) C8J_0385(frdB) C8J_0412(sdhA)
                 C8J_0413(sdhB) C8J_0414(sdhC)
            CJD: JJD26997_1547(frdB) JJD26997_1548(frdA)
            CFF: CFF8240_0137 CFF8240_0414 CFF8240_0415
            CCV: CCV52592_1873 CCV52592_2205
            CHA: CHAB381_0857 CHAB381_0858
            CCO: CCC13826_0977 CCC13826_0978(frdC) CCC13826_1283
            ABU: Abu_0299(frdB) Abu_0300(frdA)
            NIS: NIS_0006 NIS_0010 NIS_0688 NIS_0689 NIS_0690
            SUN: SUN_0151 SUN_0152 SUN_0412 SUN_0413 SUN_0414 SUN_1200
                 SUN_1201 SUN_1202
            GSU: GSU1176 GSU1177(frdA) GSU1178(frdB)
            GME: Gmet_0310 Gmet_2395 Gmet_2396 Gmet_2397
            GUR: Gura_3256
            PCA: Pcar_0444 Pcar_0445 Pcar_0446
            PPD: Ppro_2482
            DVU: DVU2674 DVU3261(frdC) DVU3262(fdrA) DVU3263(frdB)
            DVL: Dvul_0127
            DDE: Dde_1256 Dde_1257 Dde_1258
            BBA: Bd0024(sdhC) Bd0025(sdhA) Bd0026(sdhB)
            DPS: DP2135 DP2136 DP2137
            ADE: Adeh_2636 Adeh_2637 Adeh_2638 Adeh_2932 Adeh_2933 Adeh_2934
            AFW: Anae109_2603
            MXA: MXAN_1072(sdhC) MXAN_3539(sdhA) MXAN_3540(sdhB)
                 MXAN_5222(frdB) MXAN_5224(frdA) MXAN_5225(frdC)
            SFU: Sfum_0174 Sfum_1445 Sfum_1998 Sfum_1999 Sfum_2000 Sfum_2103
                 Sfum_2104
            RPR: RP044(sdhB) RP126(sdhC) RP127(sdhD) RP128(sdhA)
            RTY: RT0086(sdhB) RT0115(sdhC) RT0116(sdhD) RT0117(sdhA)
            RCO: RC0069(sdhB) RC0168(sdhC) RC0169(sdhD) RC0170(sdhA)
            RFE: RF_0136(sdhB) RF_1159(sdhA) RF_1161(sdhD) RF_1163(sdhC)
            RBE: RBE_1164(sdhA) RBE_1167(sdhD) RBE_1168(sdhC) RBE_1390(sdhB)
            RAK: A1C_00370(sdhB)
            RBO: A1I_07725(sdhB)
            RCM: A1E_00215(sdhB)
            RRI: A1G_00440(sdhB)
            OTS: OTBS_1696(sdhC) OTBS_1697(sdhD) OTBS_1698(sdhA)
                 OTBS_1699(sdhB)
            WOL: WD0437(sdhA) WD0727(sdhB) WD1221(sdhC) WD1222
            WBM: Wbm0448(sdhA) Wbm0485 Wbm0486(sdhC) Wbm0600(sdhB)
            AMA: AM168(sdhA) AM169(sdhB) AM290(sdhC) AM292(sdhD)
            APH: APH_0158(sdhA-1) APH_0159(sdhB-1) APH_0161(sdhA-2)
                 APH_0162(sdhB-2) APH_0998(sdhD) APH_0999(sdhC)
            ERU: Erum1890(sdhC) Erum1891(sdhD) Erum6800(sdhB) Erum6810(sdhA)
            ERW: ERWE_CDS_01890(sdhC) ERWE_CDS_01900(sdhD)
                 ERWE_CDS_07150(sdhB) ERWE_CDS_07160(sdhA)
            ERG: ERGA_CDS_01840(sdhC) ERGA_CDS_01850(sdhD)
                 ERGA_CDS_07070(sdhB) ERGA_CDS_07080(sdhA)
            ECN: Ecaj_0189 Ecaj_0190 Ecaj_0687 Ecaj_0688
            ECH: ECH_0315(sdhA) ECH_0316 ECH_0917 ECH_0918(sdhC)
            NSE: NSE_0047(sdhC) NSE_0048 NSE_0376(sdhA) NSE_0534
            PUB: SAR11_0242(sdhB) SAR11_0243(sdhA) SAR11_0244 SAR11_1721(sdhC)
            MLO: mll4260 mll4263 mll4265 mll4266
            MES: Meso_3243 Meso_3244 Meso_3245 Meso_3246
            SME: SMc02463(sdhC) SMc02464(sdhD) SMc02465(sdhA) SMc02466(sdhB)
            ATU: Atu2642(sdhB) Atu2643(sdhA) Atu2644(sdhD) Atu2645(sdhC)
            ATC: AGR_C_4790 AGR_C_4792 AGR_C_4793 AGR_C_4794
            RET: RHE_CH03894(sdhB) RHE_CH03895(sdhA) RHE_CH03896(sdhD)
                 RHE_CH03897(sdhC)
            RLE: RL1830 RL4443(sdhB) RL4444(sdhA) RL4445(sdhD) RL4446(sdhC)
            BME: BMEI0159 BMEI0160 BMEI0161 BMEI0162
            BMF: BAB1_1900 BAB1_1901 BAB1_1902 BAB1_1903(sdhC)
            BMS: BR1901(sdhB) BR1902(sdhA) BR1903 BR1904(sdhC)
            BMB: BruAb1_1877(sdhB) BruAb1_1878(sdhA) BruAb1_1879
                 BruAb1_1880(sdhC)
            BOV: BOV_1829(sdhB)
            BJA: blr0512(sdhC) blr0513(sdhD) blr0514(sdhA) blr0515(sdhB)
            BRA: BRADO0232(sdhC) BRADO0233(sdhD) BRADO0234(sdhA)
                 BRADO0235(sdhB) BRADO3505 BRADO4455 BRADO5504
            BBT: BBta_0228(sdhC) BBta_0229(sdhD) BBta_0230(sdhA)
                 BBta_0231(sdhB) BBta_2527 BBta_4211 BBta_4675 BBta_4872
                 BBta_4884 BBta_5986
            RPA: RPA0216(sdhB) RPA0217(sdhA) RPA0218(sdhD) RPA0219(sdhC)
            RPB: RPB_0324 RPB_0325 RPB_0326 RPB_0327
            RPC: RPC_0068 RPC_0070 RPC_0071 RPC_0072
            RPD: RPD_0478 RPD_0479 RPD_0480 RPD_0481
            RPE: RPE_0510 RPE_0511 RPE_0512 RPE_0514
            NWI: Nwi_2798 Nwi_2799 Nwi_2800
            NHA: Nham_3616 Nham_3617 Nham_3618 Nham_3619
            BHE: BH15770(sdhB) BH15780(sdhA) BH15790(sdhD) BH15800(sdhC)
            BQU: BQ12690(sdhB) BQ12700(sdhA) BQ12710(sdhD) BQ12720(sdhC)
            BBK: BARBAKC583_0091(sdhB)
            CCR: CC_3526 CC_3527 CC_3528 CC_3529
            SIL: SPO0358(sdhC) SPO0359(sdhD) SPO0360(sdhA) SPO0361(sdhB)
                 SPO1469
            SIT: TM1040_3525 TM1040_3526 TM1040_3527 TM1040_3530
            RSP: RSP_0974 RSP_0975 RSP_0976(sdhA) RSP_0979(sdhB)
                 RSP_3147(sdhA) RSP_3148 RSP_3149 RSP_3150(frdB)
            RSH: Rsph17029_2636
            JAN: Jann_0809 Jann_3768
            RDE: RD1_1626(sdhC) RD1_1627(sdhD) RD1_1628(sdhA) RD1_1630(sdhB)
            PDE: Pden_0569
            MMR: Mmar10_2844 Mmar10_2846 Mmar10_2847 Mmar10_2848
            HNE: HNE_3243(sdhC) HNE_3244(sdhD) HNE_3245(sdhA) HNE_3247(sdhB)
            ZMO: ZMO0569(sdhC)
            NAR: Saro_1744 Saro_1745 Saro_1746
            SAL: Sala_3030 Sala_3031 Sala_3032
            ELI: ELI_07155 ELI_07160 ELI_07165
            GBE: GbCGDNIH1_0072 GbCGDNIH1_2077 GbCGDNIH1_2078 GbCGDNIH1_2079
                 GbCGDNIH1_2080
            RRU: Rru_A1204 Rru_A1205 Rru_A2986
            MAG: amb3950 amb3951 amb3952 amb3953
            MGM: Mmc1_0430
            ABA: Acid345_1384 Acid345_1385 Acid345_2570 Acid345_2571
                 Acid345_2572
            SUS: Acid_7402
            BSU: BG10351(sdhC) BG10352(sdhA) BG10353(sdhB)
            BHA: BH3091(sdhB) BH3092(sdhA) BH3093(sdhC)
            BAN: BA4753(sdhB) BA4754(sdhA) BA4755(sdhC)
            BAR: GBAA4753(sdhB) GBAA4754(sdhA) GBAA4755(sdhC)
            BAA: BA_5183 BA_5184 BA_5185
            BAT: BAS4412 BAS4413 BAS4414
            BCE: BC4516 BC4517 BC4518
            BCA: BCE_4643(sdhB) BCE_4644(sdhA) BCE_4645(sdhC)
            BCZ: BCZK4263(sdhB) BCZK4264 BCZK4265(sdhC)
            BCY: Bcer98_3216
            BTK: BT9727_4251(sdhB) BT9727_4252 BT9727_4253(sdhC)
            BTL: BALH_4100(sdhB) BALH_4101(sdhA) BALH_4102(sdhC)
            BLI: BL00320(sdhB) BL00321(sdhAA) BL00322(sdhAB) BL00323(sdhC)
            BLD: BLi02992(sdhB) BLi02993(sdhA) BLi02994(sdhC)
            BCL: ABC2662(sdhB) ABC2663(sdhA) ABC2664(sdhC)
            BAY: RBAM_025500(sdhB) RBAM_025510(sdhA) RBAM_025520(sdhC)
            BPU: BPUM_2501(sdhB) BPUM_2502(sdhA) BPUM_2503(sdhC)
            OIH: OB2112(sdhB) OB2113(sdhA) OB2114(sdhC)
            GKA: GK2671(sdhB) GK2672(sdhA) GK2673(sdhC)
            SAU: SA0994(sdhC) SA0995(sdhA) SA0996(sdhB)
            SAV: SAV1147(sdhC) SAV1148(sdhA) SAV1149(sdhB)
            SAM: MW1030(sdhC) MW1031(sdhA) MW1032(sdhB)
            SAR: SAR1120(sdhC) SAR1121(sdhA) SAR1122(sdhB)
            SAS: SAS1081 SAS1082 SAS1083
            SAC: SACOL1158(sdhC) SACOL1159(sdhA) SACOL1160(sdhB)
            SAB: SAB1011(sdhC) SAB1012(sdhA) SAB1013(sdhB)
            SAA: SAUSA300_1046(sdhC) SAUSA300_1047(sdhA) SAUSA300_1048(sdhB)
            SAO: SAOUHSC_01103 SAOUHSC_01104 SAOUHSC_01105
            SAJ: SaurJH9_1207
            SAH: SaurJH1_1229
            SEP: SE0840 SE0841 SE0842
            SER: SERP0730(sdhC) SERP0731 SERP0732
            SHA: SH1812(sdhB) SH1813(sdhA) SH1814(sdhC)
            SSP: SSP1646 SSP1647 SSP1648
            LMO: lmo0355
            LMF: LMOf2365_0376
            LIN: lin0374
            LWE: lwe0312(frdC)
            LLA: L137630(frdC)
            LLC: LACR_1226
            LLM: llmg_1441(frdC)
            SMU: SMU.180
            LPL: lp_0055 lp_0952 lp_1113 lp_1425 lp_3125 lp_3491
            LJO: LJ1404
            LAC: LBA0064 LBA0908 LBA1411
            LSL: LSL_1326(frdA) LSL_1794(sdhA)
            LDB: Ldb0795
            LBU: LBUL_0726
            LCA: LSEI_0322
            LRE: Lreu_1530
            EFA: EF2556
            STH: STH2637 STH2638 STH2639 STH2640
            CTC: CTC00811 CTC01488 CTC01522 CTC01847
            AMT: Amet_1348 Amet_3000
            CHY: CHY_0063(frdA) CHY_0064(frdB1) CHY_1370(frdB2)
            DSY: DSY0735(frdC) DSY0736(frdA) DSY0737(frdB) DSY0972 DSY3139
                 DSY3697
            DRM: Dred_1869
            MTU: Rv0247c Rv0248c Rv1552(frdA) Rv1553(FrdB) Rv1554(frdC)
                 Rv1555(frdD) Rv3316(sdhC) Rv3317(sdhD) Rv3318(sdhA)
                 Rv3319(sdhB)
            MTC: MT0261 MT0262 MT1603(frdA) MT1604(frdB) MT1605(frdC)
                 MT1606(frdD) MT3417(sdhC) MT3418(sdhD) MT3419(sdhA)
                 MT3420(sdhB)
            MBO: Mb0253c Mb0254c Mb1578(frdA) Mb1579(frdBC) Mb1580(frdD)
                 Mb3345(sdhC) Mb3346(sdhD) Mb3347(sdhA) Mb3348(sdhB)
            MBB: BCG_0285c BCG_0286c BCG_1604(frdA) BCG_1605(frdBC)
                 BCG_1606(frdD) BCG_3382(sdhC) BCG_3383(sdhD) BCG_3384(sdhA)
                 BCG_3385(sdhB)
            MLE: ML0696(sdhB) ML0697(sdhA) ML0698(sdhD) ML0699(sdhC)
            MPA: MAP3441(sdhC) MAP3442(sdhD) MAP3443(sdhA) MAP3444(sdhB)
                 MAP3697c MAP3698c
            MSM: MSMEG_0417 MSMEG_0418 MSMEG_1669(sdhB) MSMEG_1670(sdhA)
                 MSMEG_1671 MSMEG_1672(sdhC) MSMEG_1693
            MVA: Mvan_0284 Mvan_1587
            MGI: Mflv_0394 Mflv_4846
            MMC: Mmcs_0252 Mmcs_0253 Mmcs_1227 Mmcs_1228 Mmcs_1229 Mmcs_1230
            MKM: Mkms_0263 Mkms_1245
            MJL: Mjls_0243 Mjls_1254
            CGL: NCgl0359(cgl0370) NCgl0360(cgl0371) NCgl0361(cgl0372)
            CGB: cg0445(sdhCD) cg0446(sdhA)
            CEF: CE0386 CE0387 CE0388
            CDI: DIP0370 DIP0371 DIP0372
            CJK: jk1927(sdhB) jk1928(sdhA) jk1929(sdhC)
            NFA: nfa56020 nfa56030 nfa9460(sdhB) nfa9470(sdhA) nfa9480(sdhD)
                 nfa9490(sdhC)
            RHA: RHA1_ro01048(sdhB1) RHA1_ro01049(sdhA1) RHA1_ro06245(sdhB2)
                 RHA1_ro06246(sdhA2) RHA1_ro06247 RHA1_ro06851
                 RHA1_ro08826(sdhC) RHA1_ro08827 RHA1_ro08828(sdhB3)
            SCO: SCO0922(SCM10.10c) SCO0923(SCM10.11c) SCO0924(SCM10.12c)
                 SCO4855(dhsB) SCO4856(dhsA) SCO4857(SC5G8.25c)
                 SCO4858(SC5G8.26c) SCO5106(SCBAC31E11.02c)
                 SCO5107(SCBAC31E11.02c) SCO7109(SC4B10.10c)
            SMA: SAV3181(sdhA2) SAV3182(sdhB2) SAV3395(sdhC) SAV3396(sdhD)
                 SAV3397(sdhA1) SAV3398(sdhB1) SAV7307(qcrB2) SAV7308(sdhA3)
                 SAV7309(sdhB3)
            LXX: Lxx04510(sdhB) Lxx04520(sdhA) Lxx04530(sdhD) Lxx04540(sdhC)
            CMI: CMM_0969(sdhB) CMM_0970 CMM_0971(sdhD) CMM_0972(sdhC)
            ART: Arth_1129
            AAU: AAur_1244(sdhB) AAur_1245(sdhA)
            PAC: PPA0950 PPA0951 PPA0952 PPA1437 PPA1438 PPA1439
            NCA: Noca_3548 Noca_3552
            TFU: Tfu_2451 Tfu_2452 Tfu_2453
            FRA: Francci3_0678 Francci3_0679 Francci3_0680 Francci3_0681
                 Francci3_3465 Francci3_3466 Francci3_3467
            FAL: FRAAL1187(sdhB) FRAAL1188(sdhA) FRAAL1189(sdhD)
                 FRAAL1190(sdhC) FRAAL5653(sdhC) FRAAL5654(sdhA)
                 FRAAL5655(sdhB)
            ACE: Acel_1865
            KRA: Krad_3954 Krad_3955
            SEN: SACE_1170(sdhA1) SACE_1171(sdhB1) SACE_6582(sdhC)
                 SACE_6584(sdhA) SACE_6585(sdhB)
            STP: Strop_1709 Strop_3768
            BLO: BL0938(sdhA) BL0939
            BAD: BAD_0592 BAD_0593(sdhA)
            RXY: Rxyl_0011 Rxyl_0012 Rxyl_0355
            FNU: FN0050
            RBA: RB10553(sdhC) RB10554(sdhA) RB10555(sdhB)
            CTR: CT591(sdhB) CT592(sdhA) CT593(sdhC) CT593.1
            CTA: CTA_0641(sdhB) CTA_0642(sdhA) CTA_0643(sdhC) CTA_0644
            CMU: TC0880 TC0881 TC0882
            CPN: CPn0788(sdhC) CPn0789(sdhA) CPn0790(sdhB)
            CPA: CP1082 CP1083 CP1084
            CPJ: CPj0788(sdhC) CPj0789(sdhA) CPj0790(sdhB)
            CPT: CpB0816 CpB0817 CpB0818(sdhB)
            CCA: CCA00967(sdhB) CCA00968(sdhA) CCA00969
            CAB: CAB936(sdhB) CAB937(sdhA) CAB938(sdhC)
            CFE: CF0044(sdhC) CF0045(sdhA) CF0046(sdhB)
            PCU: pc1841(sdhB) pc1842(sdhA) pc1843(sdhC)
            LIL: LA1896(sdhB) LA1897(sdhA) LA1898
            LIC: LIC12001(sdhC) LIC12002(sdhA) LIC12003(sdhB)
            LBJ: LBJ_1503 LBJ_1504(sdhA) LBJ_1505(sdhB)
            LBL: LBL_1727 LBL_1728(sdhA) LBL_1729(sdhB)
            SYN: sll0823(sdhB) sll1625(sdhB) slr1233(frdA)
            SYW: SYNW0590 SYNW0591(sdhA) SYNW0592
            SYC: syc0884_d(sdhA) syc1199_d syc2519_d(sdhB)
            SYF: Synpcc7942_0314 Synpcc7942_0641 Synpcc7942_1533
            SYD: Syncc9605_2086 Syncc9605_2087 Syncc9605_2088
            SYE: Syncc9902_0584 Syncc9902_0585 Syncc9902_0586
            CYA: CYA_0688
            CYB: CYB_2127 CYB_2507
            TEL: tlr1377 tlr1754
            GVI: glr2944 glr2988
            ANA: all0945 all2970
            AVA: Ava_0936 Ava_4067
            PMA: Pro0698 Pro0699(sdhA) Pro0700(sdhB)
            PMT: PMT0131 PMT0132(sdhA) PMT0133(sdhB)
            PMI: PMT9312_1354
            PMB: A9601_12591(sdhA)
            PMF: P9303_01681 P9303_01691(sdhA) P9303_01701(sdhB)
            PMG: P9301_12651(sdhA)
            PMH: P9215_12721(sdhA)
            TER: Tery_2474 Tery_3726
            BTH: BT_3053 BT_3054 BT_3055
            BFR: BF4551 BF4552 BF4553
            BFS: BF4339 BF4340 BF4341
            PGI: PG1614(frdB) PG1615(frdA) PG1616
            SRU: SRU_0484(sdhB) SRU_0485(sdhA) SRU_0486 SRU_0487 SRU_2444
            CHU: CHU_2473(sdhA) CHU_2474(frdB)
            GFO: GFO_3149(sdhA) GFO_3150(sdhB)
            FJO: Fjoh_0676 Fjoh_3325
            FPS: FP0092(sdhC) FP0093(sdhA) FP0095(sdhB)
            CTE: CT1245 CT2040 CT2041 CT2042 CT2266(sdhB) CT2267(sdhA) CT2268
            CCH: Cag_0127 Cag_0129 Cag_1028 Cag_1585 Cag_1933 Cag_1934
                 Cag_1935
            CPH: Cpha266_0101 Cpha266_0177
            PVI: Cvib_1638 Cvib_1722
            PLT: Plut_1108 Plut_1993 Plut_1995 Plut_2080 Plut_2081 Plut_2082
            RRS: RoseRS_2399
            RCA: Rcas_3080
            DRA: DR_0951 DR_0952 DR_0953 DR_0954
            DGE: Dgeo_0886 Dgeo_0887 Dgeo_0888 Dgeo_0889
            TTH: TTC1089 TTC1090 TTC1091 TTC1092
            TTJ: TTHA1453 TTHA1454 TTHA1455 TTHA1456
            AAE: aq_553(frdB1) aq_594(frdA) aq_655(frdB2)
            TMA: TM0427
            MJA: MJ0033 MJ0092
            MMP: MMP1067 MMP1277(frdA)
            MMQ: MmarC5_0315
            MMZ: MmarC7_0522
            MAE: Maeo_0245
            MVN: Mevan_0588
            MHU: Mhun_3052 Mhun_3053
            MLA: Mlab_0436
            MBN: Mboo_0086
            MTH: MTH1502 MTH1850
            MST: Msp_0180(tfrA) Msp_1044(tfrB)
            MSI: Msm_0393 Msm_1258
            MKA: MK0132(frdB) MK0828(sdhA)
            AFU: AF0681(sdhA) AF0682(sdhB) AF0683(sdhC) AF0684(sdhD)
                 AF1463(fdrA)
            HAL: VNG1306G(sdhA) VNG1308G(sdhB) VNG1309G(sdhD) VNG1310G(sdhC)
            HMA: rrnAC0141(sdhA2) rrnAC1091(sdhC) rrnAC1092 rrnAC1093(sdhB)
                 rrnAC1097(sdhA1)
            HWA: HQ2441A(sdhA) HQ2994A(sdhA) HQ2995A(sdhB) HQ2996A(sdhD)
                 HQ2997A(sdhC)
            NPH: NP4264A(sdhA) NP4266A(sdhB) NP4268A(sdhD) NP4270A(sdhC)
            TAC: Ta1001 Ta1002 Ta1003 Ta1004
            TVO: TVN0744 TVN0745 TVN0746 TVN0747
            PTO: PTO0995 PTO0996 PTO0997 PTO0998
            APE: APE_0946 APE_0947 APE_0948.1 APE_0950.1
            HBU: Hbut_0157
            SSO: SSO2356(sdhA) SSO2357(sdhB) SSO2358(sdhC)
            STO: ST0497 ST0498 ST0499
            SAI: Saci_0980(sdhC) Saci_0981(sdhB) Saci_0982(sdhA)
            MSE: Msed_0676 Msed_0677 Msed_1114
            PAI: PAE0716(sdhA) PAE0717(sdhB) PAE0718(sdhC) PAE2690
            PIS: Pisl_0247 Pisl_0671
            PCL: Pcal_1388 Pcal_2127
            PAS: Pars_2358
STRUCTURES  PDB: 1D4C  1D4D  1D4E  1E7P  1JRX  1JRY  1JRZ  1KF6  1KFY  1KSS  
                 1KSU  1L0V  1LJ1  1M64  1NEK  1NEN  1P2E  1P2H  1Q9I  1QLB  
                 1QO8  1Y0P  2ACZ  2B76  2B7R  2B7S  2BS2  2BS3  2BS4  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.1
            ExPASy - ENZYME nomenclature database: 1.3.99.1
            ExplorEnz - The Enzyme Database: 1.3.99.1
            ERGO genome analysis and discovery system: 1.3.99.1
            BRENDA, the Enzyme Database: 1.3.99.1
            CAS: 9002-02-2
///
ENTRY       EC 1.3.99.2                 Enzyme
NAME        butyryl-CoA dehydrogenase;
            butyryl dehydrogenase;
            unsaturated acyl-CoA reductase;
            ethylene reductase;
            enoyl-coenzyme A reductase;
            unsaturated acyl coenzyme A reductase;
            butyryl coenzyme A dehydrogenase;
            short-chain acyl CoA dehydrogenase;
            short-chain acyl-coenzyme A dehydrogenase;
            3-hydroxyacyl CoA reductase;
            butanoyl-CoA:(acceptor) 2,3-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     butanoyl-CoA:acceptor 2,3-oxidoreductase
REACTION    butanoyl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor
            [RN:R01178]
ALL_REAC    R01178 > R01175;
            (other) R01171 R02660 R03170 R04751
SUBSTRATE   butanoyl-CoA [CPD:C00136];
            acceptor [CPD:C00028]
PRODUCT     2-butenoyl-CoA [CPD:C00877];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein; forms, with another flavoprotein
            ('electron-transferring flavoproteins') and EC 1.5.5.1
            electron-transferring-flavoprotein dehydrogenase, a system reducing
            ubiquinone and other acceptors.
REFERENCE   1
  AUTHORS   Beinert, H.
  TITLE     Acyl coenzyme A dehydrogenase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 447-466.
REFERENCE   2  [PMID:13201608]
  AUTHORS   MAHLER HR, MACKLER B, GREEN DE.
  TITLE     Studies on metalloflavoproteins. III. Aldehyde oxidase: a
            molybdoflavoprotein.
  JOURNAL   J. Biol. Chem. 210 (1954) 465-80.
REFERENCE   3  [PMID:13319294]
  AUTHORS   HAUGE JG, CRANE FL, BEINERT H.
  TITLE     On the mechanism of dehydrogenation of fatty acyl derivatives of
            coenzyme A.  III.  Palmityl coA dehydrogenase.
  JOURNAL   J. Biol. Chem. 219 (1956) 727-33.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:13130522]
  AUTHORS   MAHLER HR.
  TITLE     Studies on the fatty acid oxidizing system of animal tissues. IV.
            The prosthetic group of butyryl coenzyme A dehydrogenase.
  JOURNAL   J. Biol. Chem. 206 (1954) 13-26.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00071  Fatty acid metabolism
            PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K00248  butyryl-CoA dehydrogenase
GENES       HSA: 35(ACADS)
            MMU: 11409(Acads)
            RNO: 64304(Acads)
            CFA: 477517(ACADS)
            SSC: 396932(ACADS)
            GGA: 416969(ACADS)
            PAE: PA5020
            PPU: PP_4948
            PST: PSPTO_5020
            PSB: Psyr_0505
            PSP: PSPPH_0495 PSPPH_3615
            PFL: PFL_0494
            PFO: Pfl_0451
            PEN: PSEEN5004
            PCR: Pcryo_0861 Pcryo_1516
            ACI: ACIAD1412
            SDN: Sden_1941
            SFR: Sfri_1340
            SAZ: Sama_1377
            SBL: Sbal_1497
            SLO: Shew_1669
            PHA: PSHAa0907 PSHAa1456 PSHAa1920(fadE)
            PAT: Patl_0949 Patl_2141
            MAQ: Maqu_2132
            LPN: lpg0868
            LPF: lpl0900
            LPP: lpp0931
            NOC: Noc_1555
            ABO: ABO_0833 ABO_1103(acdS) ABO_1918(acdS)
            RSO: RSc1762(RS02949)
            REU: Reut_A1408 Reut_B3825 Reut_B3882 Reut_B4150 Reut_B4257
                 Reut_C6425
            REH: H16_A0172 H16_B0014 H16_B0485 H16_B0638 H16_B0752 H16_B0850
                 H16_B1371 H16_B2555
            RME: Rmet_1852
            BUR: Bcep18194_A4177 Bcep18194_A6048 Bcep18194_B0714
                 Bcep18194_B1438 Bcep18194_B1754 Bcep18194_B2643
                 Bcep18194_C6872 Bcep18194_C7290 Bcep18194_C7492
            RFR: Rfer_2384 Rfer_4169 Rfer_4181
            POL: Bpro_2570
            VEI: Veis_3538
            MPT: Mpe_A1777
            HAR: HEAR0621 HEAR2838(acdB)
            GME: Gmet_1715
            BBA: Bd1973 Bd2174
            ADE: Adeh_0360 Adeh_1647 Adeh_1664 Adeh_1665
            SAT: SYN_00480 SYN_02587
            SFU: Sfum_1371
            BME: BMEI0689 BMEII0213 BMEII0818 BMEII1023
            BMF: BAB1_1333
            BMB: BruAb1_1314
            BJA: bll3855 bll5455 blr3437 blr3448 blr3955
            BRA: BRADO2179 BRADO2575 BRADO3035
            BBT: BBta_2498 BBta_2922 BBta_3103 BBta_5105
            RPE: RPE_3222
            NWI: Nwi_2158
            NHA: Nham_2558
            SIT: TM1040_2796
            RSP: RSP_0156
            JAN: Jann_1909
            RDE: RD1_1713 RD1_3681(acdA)
            PDE: Pden_0198 Pden_0714
            NAR: Saro_0858
            RRU: Rru_A1308 Rru_A1835
            ABA: Acid345_1131 Acid345_2471
            SUS: Acid_5310
            BCZ: BCZK5042(mmgC)
            BTK: BT9727_5025 BT9727_5026(mmgC)
            BTL: BALH_4840(acdA) BALH_4841(acd)
            BCL: ABC1506
            OIH: OB1695
            LBR: LVIS_1909
            CAC: CAC2711(bcd)
            CPE: CPE2300(bcd)
            CPF: CPF_0092 CPF_2584(bcd)
            CPR: CPR_2286(bcd)
            CTC: CTC01387
            CNO: NT01CX_0473
            CDF: CD1054(bcd2)
            CBO: CBO2196(acdB) CBO2843 CBO3199(bcd)
            CBA: CLB_3235(bcd)
            CBH: CLC_3109(bcd)
            CBF: CLI_3338(bcd)
            CKL: CKL_0455(bcd)
            CHY: CHY_1323(bcd1) CHY_1350(bcd2) CHY_1602(bcd3)
            DSY: DSY1568
            DRM: Dred_1490 Dred_1782
            SWO: Swol_0268 Swol_0488 Swol_0788 Swol_1483 Swol_1841
            TTE: TTE0545(caiA)
            MVA: Mvan_0221 Mvan_1977
            MGI: Mflv_0446 Mflv_4367 Mflv_4743
            MMC: Mmcs_0182
            MKM: Mkms_0191
            MJL: Mjls_0171
            NFA: nfa24470(fadE24)
            RHA: RHA1_ro02521 RHA1_ro03348 RHA1_ro03612 RHA1_ro03878
                 RHA1_ro05203 RHA1_ro06400
            TFU: Tfu_1281
            FRA: Francci3_1549 Francci3_2167 Francci3_2247 Francci3_2419
            FAL: FRAAL2792(acd) FRAAL3384 FRAAL6072
            RXY: Rxyl_1707
            FNU: FN1424 FN1535
            CHU: CHU_3827(bcd)
            DRA: DR_A0250
            DGE: Dgeo_2405
            TTH: TTC0238 TTC1575
            TTJ: TTHA1938 TTHB022
            PTO: PTO1025 PTO1396
            PIS: Pisl_1436
            PCL: Pcal_0838
            PAS: Pars_0456
STRUCTURES  PDB: 1BUC  1JQI  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.2
            ExPASy - ENZYME nomenclature database: 1.3.99.2
            ExplorEnz - The Enzyme Database: 1.3.99.2
            ERGO genome analysis and discovery system: 1.3.99.2
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.99.2
            BRENDA, the Enzyme Database: 1.3.99.2
            CAS: 9027-88-7
///
ENTRY       EC 1.3.99.3                 Enzyme
NAME        acyl-CoA dehydrogenase;
            acyl dehydrogenase;
            fatty acyl coenzyme A dehydrogenase;
            acyl coenzyme A dehydrogenase;
            fatty-acyl-CoA dehydrogenase;
            acyl CoA dehydrogenase;
            general acyl CoA dehydrogenase;
            medium-chain acyl-coenzyme A dehydrogenase;
            medium-chain acyl-CoA dehydrogenase;
            long-chain acyl coenzyme A dehydrogenase;
            long-chain acyl-CoA dehydrogenase;
            acyl-CoA:(acceptor) 2,3-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     acyl-CoA:acceptor 2,3-oxidoreductase
REACTION    acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor
            [RN:R00392]
ALL_REAC    R00392 > R00924 R01175 R01279 R02661 R03172 R03777 R03857 R03990
            R04095 R04432 R04751 R04754
SUBSTRATE   acyl-CoA [CPD:C00040];
            acceptor [CPD:C00028]
PRODUCT     2,3-dehydroacyl-CoA [CPD:C00605];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein; forms, with another flavoprotein
            ('electron-transferring flavoprotein') and EC 1.5.5.1
            electron-transferring-flavoprotein dehydrogenase, a system reducing
            ubiquinone and other acceptors.
REFERENCE   1
  AUTHORS   Beinert, H.
  TITLE     Acyl coenzyme A dehydrogenase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 447-466.
REFERENCE   2  [PMID:13295224]
  AUTHORS   CRANE FL, MII S, HAUGE JG, GREEN DE, BEINERT H.
  TITLE     On the mechanism of dehydrogenation of fatty acyl derivatives of
            coenzyme A.  I.  The general fatty acyl coenzyme A dehydrogenase.
  JOURNAL   J. Biol. Chem. 218 (1956) 701-6.
REFERENCE   3  [PMID:13319294]
  AUTHORS   HAUGE JG, CRANE FL, BEINERT H.
  TITLE     On the mechanism of dehydrogenation of fatty acyl derivatives of
            coenzyme A.  III.  Palmityl coA dehydrogenase.
  JOURNAL   J. Biol. Chem. 219 (1956) 727-33.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00071  Fatty acid metabolism
            PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00410  beta-Alanine metabolism
            PATH: map00640  Propanoate metabolism
            PATH: map03320  PPAR signaling pathway
ORTHOLOGY   KO: K00249  acyl-CoA dehydrogenase
GENES       HSA: 34(ACADM)
            MMU: 11364(Acadm)
            RNO: 24158(Acadm)
            CFA: 490207(ACADM)
            SSC: 397104(ACADM)
            XLA: 446467(acadm) 447486(MGC81873)
            DRE: 393147(acad11) 406283(acadm)
            SPU: 591118(LOC591118)
            DME: Dmel_CG12262 Dmel_CG4703 Dmel_CG4860
            CEL: K05F1.3 K09H11.1 T25G12.5
            ATH: AT3G06810
            CME: CML080C
            AGO: AGOS_AFL213W
            PIC: PICST_33103(ACD99)
            ANI: AN6761.2
            AFM: AFUA_5G06500 AFUA_7G06510
            AOR: AO090005000494 AO090009000596
            CNE: CNJ01190 CNK00550
            UMA: UM01049.1 UM06400.1
            TBR: Tb11.01.3640
            TCR: 509153.120 510303.290
            LMA: LmjF06.0880 LmjF28.2510
            SEC: SC0851(acdC)
            STM: STM0857
            PAE: PA0879 PA1187 PA1535 PA2550 PA2889 PA4435 PA4994
            PAU: PA14_26700 PA14_31580 PA14_35970 PA14_44590 PA14_51120
                 PA14_52900
            PPU: PP_2437 PP_2793
            PST: PSPTO_2745
            PSB: Psyr_2176 Psyr_2474
            PSP: PSPPH_2632 PSPPH_4712 PSPPH_4715
            PFL: PFL_1908(fadE13) PFL_2648(acd-6) PFL_3931(fadE1)
                 PFL_4197(fadE13) PFL_5084(fadE20)
            PFO: Pfl_1809 Pfl_3651 Pfl_3948 Pfl_4696
            PEN: PSEEN3343
            ACI: ACIAD0452 ACIAD1566
            SFR: Sfri_2069
            PAT: Patl_0315 Patl_1812 Patl_3783
            CBD: COXBU7E912_0283 COXBU7E912_1074
            FTU: FTT1529(fadE)
            FTF: FTF1529(fadE)
            FTH: FTH_0585(fadE)
            HCH: HCH_01061 HCH_02846 HCH_05750 HCH_05789
            ABO: ABO_0185(fadE-1) ABO_0186(fadE-2) ABO_0571 ABO_0957 ABO_0988
                 ABO_1264 ABO_1701(acdA) ABO_1702 ABO_2098(fadE) ABO_2533
                 ABO_2662
            CVI: CV_1785 CV_2084(caiA) CV_2723 CV_3816 CV_4136(aidB)
            RSO: RS02011(RSp0036) RSc2020(RS03588)
            REU: Reut_A1002 Reut_A2181 Reut_B3500 Reut_B3515 Reut_B3542
                 Reut_B3552 Reut_B3857 Reut_B4154 Reut_B4166 Reut_B4462
                 Reut_B4519 Reut_B4628 Reut_B4753 Reut_B5206 Reut_B5285
                 Reut_B5288 Reut_B5361 Reut_C6366
            REH: H16_A0101 H16_A0234(aidB) H16_A0460(acaD) H16_A0816 H16_A0843
                 H16_A0863 H16_A1067 H16_A1068 H16_A1530 H16_A2596 H16_B0087
                 H16_B0356 H16_B0360 H16_B0379 H16_B0383 H16_B0384 H16_B0395
                 H16_B0396 H16_B0400 H16_B0580 H16_B0660 H16_B0661 H16_B0664
                 H16_B0665 H16_B0676 H16_B0683 H16_B0703 H16_B0704 H16_B0721
                 H16_B0722 H16_B0751 H16_B0849 H16_B0909 H16_B0913 H16_B0938
                 H16_B0975 H16_B1192 H16_B1332 H16_B1367 H16_B1481 H16_B1694
                 H16_B1826 H16_B2157 H16_B2158
            RME: Rmet_0845 Rmet_0968 Rmet_1722 Rmet_1814 Rmet_2199 Rmet_3412
                 Rmet_3727 Rmet_3899 Rmet_4410 Rmet_4458 Rmet_4574 Rmet_4575
                 Rmet_4613 Rmet_5024 Rmet_5133 Rmet_5152 Rmet_5357 Rmet_5358
                 Rmet_5437 Rmet_5837
            BMA: BMA0042 BMA1755 BMA1806 BMA3156
            BXE: Bxe_A2526 Bxe_A2768 Bxe_A3188 Bxe_B0278 Bxe_B2584 Bxe_B2724
                 Bxe_B2741 Bxe_C0279 Bxe_C0426 Bxe_C0602 Bxe_C0604 Bxe_C0617
                 Bxe_C0655 Bxe_C0702 Bxe_C0852
            BUR: Bcep18194_B1442 Bcep18194_B1805 Bcep18194_B3035
                 Bcep18194_C7329 Bcep18194_C7425
            BCN: Bcen_4153 Bcen_5016 Bcen_5651 Bcen_5810
            BCH: Bcen2424_4213 Bcen2424_5844 Bcen2424_6016 Bcen2424_6174
            BPS: BPSL0061 BPSL0483 BPSL0614 BPSL1234 BPSL2329 BPSS2029
                 BPSS2032
            BPM: BURPS1710b_0285 BURPS1710b_0705 BURPS1710b_0818
                 BURPS1710b_1459 BURPS1710b_2781 BURPS1710b_2975
                 BURPS1710b_A1147 BURPS1710b_A1150
            BTE: BTH_I0060 BTH_I0531 BTH_I1083 BTH_I1655 BTH_I1833 BTH_II0292
            BPE: BP0310 BP0625 BP0640
            BPA: BPP0575 BPP0585 BPP0613 BPP2810 BPP3941
            BBR: BB0581 BB0591 BB0619 BB3131 BB4414 BB4702 BB4716
            RFR: Rfer_0062 Rfer_0994 Rfer_1019 Rfer_2752 Rfer_2817 Rfer_3328
                 Rfer_3506 Rfer_3689
            POL: Bpro_0583 Bpro_0590 Bpro_2961 Bpro_3014 Bpro_5265 Bpro_5275
                 Bpro_5284
            PNA: Pnap_2129
            MPT: Mpe_A1953
            MMS: mma_2331
            NEU: NE2348(fadE1)
            NMU: Nmul_A0967
            EBA: ebA5321 ebA5641 ebA736 p2A380
            AZO: azo0463(fadE) azo1702 azo1931(abmD) azo2299(aidB1)
                 azo2494(aidB2)
            SAT: SYN_02586
            PUB: SAR11_0249(mmgC)
            MLO: mll3094 mlr5042 mlr5626
            MES: Meso_0023 Meso_0723 Meso_3278 Meso_3279 Meso_3281
            SME: SMc01639
            ATU: Atu2572(acd)
            ATC: AGR_C_4660
            RET: RHE_CH04044(acd2) RHE_PC00127
            RLE: RL0591 RL0965 RL4513 RL4596 pRL100145 pRL100376
            BME: BMEI1521 BMEII0495 BMEII0671
            BMF: BAB1_0440 BAB2_0442 BAB2_0642
            BMS: BR0412
            BMB: BruAb1_0435 BruAb2_0437
            BJA: bll2940 bll6283(acd) bll6363 bll6377 bll6791 blr0119 blr0120
                 blr0981 blr0982 blr2947 blr2989 blr3304 blr7270
            BRA: BRADO3126 BRADO6906 BRADO7111
            BBT: BBta_3566 BBta_4293 BBta_7841
            RPA: RPA0480 RPA0481 RPA0589 RPA0740 RPA0780 RPA0816 RPA0995
                 RPA1236 RPA1612 RPA1699 RPA1708 RPA1709 RPA1710 RPA1762
                 RPA2137 RPA2138 RPA3289 RPA4002 RPA4553 RPA4598 RPA4798
                 RPA4799
            RPB: RPB_0216 RPB_0992 RPB_1146 RPB_1238 RPB_3266 RPB_3267
                 RPB_4074 RPB_4606 RPB_4641
            RPC: RPC_0737 RPC_2051 RPC_2197 RPC_3206 RPC_4699
            RPD: RPD_0612 RPD_0767 RPD_0804 RPD_1095 RPD_1248 RPD_2198
                 RPD_2199
            RPE: RPE_0073 RPE_0119 RPE_0120 RPE_0532 RPE_0534 RPE_0672
                 RPE_0889 RPE_2248 RPE_2249 RPE_3619 RPE_3822 RPE_3823 RPE_4126
                 RPE_4308
            CCR: CC_0079 CC_0690 CC_1110 CC_2328 CC_3087 CC_3454
            SIL: SPO0693 SPO0879 SPO2538 SPO2698 SPOA0288(acdA-3) SPOA0403
            SIT: TM1040_2239
            RSP: RSP_1679
            JAN: Jann_0530 Jann_1327 Jann_2811 Jann_2970 Jann_3822
            RDE: RD1_0611(acdA) RD1_1372(ibd2) RD1_2065 RD1_3969
            PDE: Pden_2840
            MMR: Mmar10_0539 Mmar10_1651 Mmar10_1653 Mmar10_1654 Mmar10_2691
            HNE: HNE_0278 HNE_0516 HNE_0669 HNE_0809 HNE_1134 HNE_2441
                 HNE_2442 HNE_2690(mmgC) HNE_2770 HNE_2772 HNE_2795
            SAL: Sala_3053
            MAG: amb0308 amb2588
            BCZ: BCZK2285(bcd) BCZK2818(acdA) BCZK4732(acdA) BCZK5041
            BTK: BT9727_2128(mmgC) BT9727_2327(acdA) BT9727_4717(acdA)
            BTL: BALH_2096(mmgC) BALH_2288(bcd) BALH_2769(acdA)
                 BALH_4545(acdA)
            BPU: BPUM_2341(ydbM) BPUM_2940
            OIH: OB0670 OB0674 OB2667 OB3010(acdA) OB3011
            GKA: GK1028 GK1316 GK1654 GK2780 GK3393
            SAB: SAB0172c(fadD)
            DSY: DSY1716
            MTU: Rv3140(fadE23)
            MTC: MT0139 MT0163 MT0241 MT1003 MT1719 MT2796 MT3227
            MBO: Mb0159c(fadE2) Mb0236(fadE4) Mb1000c(fadE13) Mb2743c(fadE20)
                 Mb3164(fadE23)
            MLE: ML0660(fadE23)
            MPA: MAP0723(fadE12_1) MAP0913c(fadE13) MAP1713(fadE20_1)
                 MAP3189(fadE23) MAP3539c(fadE1_3) MAP3570c(fadE2)
                 MAP3669(fadE4) MAP3877c(fadE20_3)
            MAV: MAV_1877
            MSM: MSMEG_0102 MSMEG_4826 MSMEG_4832 MSMEG_5491
            MMC: Mmcs_0098 Mmcs_0212 Mmcs_0213 Mmcs_1603 Mmcs_3185 Mmcs_3735
                 Mmcs_3740
            CJK: jk0229(fadE2) jk0296(fadE4) jk1462(fadE6) jk1479(fadE7)
            NFA: nfa21770(fadE19) nfa22680(fadE21) nfa24990(fadE26)
                 nfa25560(fadE27) nfa25620 nfa34080(fadE31) nfa35440(fadE33)
                 nfa38250(fadE35) nfa40720 nfa4420(fadE1) nfa44930(fadE38)
                 nfa53310(fadE45)
            RHA: RHA1_ro01875 RHA1_ro01932 RHA1_ro02214 RHA1_ro02297
                 RHA1_ro02341 RHA1_ro02696 RHA1_ro03059 RHA1_ro03093
                 RHA1_ro03965 RHA1_ro04596 RHA1_ro04636 RHA1_ro04692(fadE27)
                 RHA1_ro04693(fadE26) RHA1_ro04748 RHA1_ro04754 RHA1_ro05247
                 RHA1_ro05713 RHA1_ro05756 RHA1_ro05827 RHA1_ro05896
                 RHA1_ro06399 RHA1_ro06629 RHA1_ro06682 RHA1_ro07119
                 RHA1_ro08438 RHA1_ro09029 RHA1_ro10128 RHA1_ro10306
                 RHA1_ro10307 RHA1_ro10357
            SCO: SCO1690(SCI30A.11) SCO2774(acdH2) SCO6787(acdH3)
            SMA: SAV1381(fadE15) SAV5280(fadE7) SAV6614(fadE17)
            TFU: Tfu_1282 Tfu_1512 Tfu_1647 Tfu_1999 Tfu_2485
            FRA: Francci3_0940 Francci3_1193 Francci3_3276
            FAL: FRAAL1585 FRAAL2829 FRAAL3513 FRAAL3514 FRAAL4769
            SEN: SACE_2745(fadE21) SACE_2758 SACE_2850(acdA-3)
                 SACE_3126(fadE13) SACE_3565 SACE_4125(fadE1) SACE_5017(acdA)
                 SACE_5380(fadE31) SACE_5699
            RXY: Rxyl_2278 Rxyl_2418 Rxyl_2735
            LIL: LA0438 LA0560 LA1130(fadE1) LA1930 LA3143 LA3363 LA3627
                 LA3676 LA3928(fadE2) LA4117
            LIC: LIC10382 LIC10583 LIC11350 LIC11976 LIC12551(acd3) LIC13009
                 LIC13281
            LBJ: LBJ_1583(caiA-2) LBJ_2860
            LBL: LBL_0211 LBL_1801(caiA-2)
            DRA: DR_1318 DR_A0196
            DGE: Dgeo_0736 Dgeo_2399
            TTH: TT_P0074(aidB)
            TTJ: TTHB015 TTHB116
            HMA: rrnAC1983(acdI) rrnB0264(acdH)
            HWA: HQ2389A(acd)
            NPH: NP1596A(acd_5) NP1754A(acd_11) NP1870A(acd_9) NP2620A(acd_1)
                 NP2628A(acd_2) NP2934A(acd_7) NP3004A(acd_6) NP3460A(acd_3)
                 NP4050A(acd_10) NP4214A(acd_12) NP4254A(acd_4) NP6180A(acd_8)
            TAC: Ta0295m Ta0398
            TVO: TVN1175 TVN1305
            PTO: PTO0830 PTO1024 PTO1459
            APE: APE_0385.1 APE_0739 APE_1681.1 APE_2158.1 APE_2354
            PAI: PAE2070
STRUCTURES  PDB: 1EGC  1EGD  1EGE  1T9G  1UDY  1UKW  2A1T  2CX9  2PG0  3MDD  
                 3MDE  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.3
            ExPASy - ENZYME nomenclature database: 1.3.99.3
            ExplorEnz - The Enzyme Database: 1.3.99.3
            ERGO genome analysis and discovery system: 1.3.99.3
            BRENDA, the Enzyme Database: 1.3.99.3
            CAS: 9027-65-0
///
ENTRY       EC 1.3.99.4                 Enzyme
NAME        3-oxosteroid 1-dehydrogenase;
            3-oxosteroid Delta1-dehydrogenase;
            Delta1-dehydrogenase;
            3-ketosteroid-1-en-dehydrogenase;
            3-ketosteroid-Delta1-dehydrogenase;
            1-ene-dehydrogenase;
            3-oxosteroid:(2,6-dichlorphenolindophenol) Delta1-oxidoreductase;
            4-en-3-oxosteroid:(acceptor)-1-en-oxido-reductase;
            Delta1-steroid reductase;
            3-oxosteroid:(acceptor) Delta1-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     3-oxosteroid:acceptor Delta1-oxidoreductase
REACTION    a 3-oxosteroid + acceptor = a 3-oxo-Delta1-steroid + reduced
            acceptor [RN:R03748]
ALL_REAC    R03748
SUBSTRATE   3-oxosteroid [CPD:C01876];
            acceptor [CPD:C00028]
PRODUCT     3-oxo-Delta1-steroid [CPD:C02941];
            reduced acceptor [CPD:C00030]
REFERENCE   1  [PMID:13673006]
  AUTHORS   LEVY HR, TALALAY P.
  TITLE     Bacterial oxidation of steroids. II. Studies on the enzymatic
            mechanism of ring A dehydrogenation.
  JOURNAL   J. Biol. Chem. 234 (1959) 2014-21.
  ORGANISM  Pseudomonas testosteroni
ORTHOLOGY   KO: K05898  
GENES       PHA: PSHAa2133(tesH)
            REH: H16_B0639 H16_B0641
            BUR: Bcep18194_B1414
            PLA: Plav_1792
            BJA: blr3669
            BBT: BBta_4671
            SWI: Swit_1839
            CGB: cg2916(ksdD)
            RHA: RHA1_ro02483 RHA1_ro05813 RHA1_ro09040(kstD)
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.4
            ExPASy - ENZYME nomenclature database: 1.3.99.4
            ExplorEnz - The Enzyme Database: 1.3.99.4
            ERGO genome analysis and discovery system: 1.3.99.4
            BRENDA, the Enzyme Database: 1.3.99.4
            CAS: 9029-04-3
///
ENTRY       EC 1.3.99.5                 Enzyme
NAME        3-oxo-5alpha-steroid 4-dehydrogenase;
            steroid 5alpha-reductase;
            3-oxosteroid Delta4-dehydrogenase;
            3-oxo-5alpha-steroid Delta4-dehydrogenase;
            steroid Delta4-5alpha-reductase;
            Delta4-3-keto steroid 5alpha-reductase;
            Delta4-3-oxo steroid reductase;
            Delta4-3-ketosteroid5alpha-oxidoreductase;
            Delta4-3-oxosteroid-5alpha-reductase;
            3-keto-Delta4-steroid-5alpha-reductase;
            5alpha-reductase;
            testosterone 5alpha-reductase;
            4-ene-3-ketosteroid-5alpha-oxidoreductase;
            Delta4-5alpha-dehydrogenase;
            3-oxo-5alpha-steroid:(acceptor) Delta4-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     3-oxo-5alpha-steroid:acceptor Delta4-oxidoreductase
REACTION    a 3-oxo-5alpha-steroid + acceptor = a 3-oxo-Delta4-steroid + reduced
            acceptor [RN:R02643]
ALL_REAC    R02643 > R01834 R02497 R04827
SUBSTRATE   3-oxo-5alpha-steroid [CPD:C02940];
            acceptor [CPD:C00028]
PRODUCT     3-oxo-Delta4-steroid [CPD:C00619];
            reduced acceptor [CPD:C00030]
REFERENCE   1  [PMID:13673006]
  AUTHORS   LEVY HR, TALALAY P.
  TITLE     Bacterial oxidation of steroids. II. Studies on the enzymatic
            mechanism of ring A dehydrogenation.
  JOURNAL   J. Biol. Chem. 234 (1959) 2014-21.
  ORGANISM  Pseudomonas testosteroni
PATHWAY     PATH: map00120  Bile acid biosynthesis
            PATH: map00150  Androgen and estrogen metabolism
            PATH: map05215  Prostate cancer
ORTHOLOGY   KO: K00250  3-oxo-5alpha-steroid 4-dehydrogenase
GENES       HSA: 6715(SRD5A1) 6716(SRD5A2)
            PTR: 743740(SRD5A1)
            MMU: 78925(Srd5a1) 94224(Srd5a2)
            RNO: 24950(Srd5a1) 64677(Srd5a2)
            CFA: 403715(SRD5A2) 403716(SRD5A1)
            BTA: 527024(LOC527024) 614612(MGC143201)
            SSC: 397048(ST5AR2)
            GGA: 772291(SRD5A2)
            XTR: 448586(srd5a1) 549867(srd5a2)
            DRE: 767715(srd5a1)
            DME: Dmel_CG7840
            CEL: F19H6.4 F42F12.3
            PIC: PICST_31592(DFG10)
            AFM: AFUA_4G07350
            TET: TTHERM_01001550
            TBR: Tb927.8.2480
            TCR: 504427.70 509331.70
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.5
            ExPASy - ENZYME nomenclature database: 1.3.99.5
            ExplorEnz - The Enzyme Database: 1.3.99.5
            ERGO genome analysis and discovery system: 1.3.99.5
            BRENDA, the Enzyme Database: 1.3.99.5
            CAS: 9036-43-5
///
ENTRY       EC 1.3.99.6                 Enzyme
NAME        3-oxo-5beta-steroid 4-dehydrogenase;
            3-oxo-5beta-steroid:(acceptor) Delta4-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     3-oxo-5beta-steroid:acceptor Delta4-oxidoreductase
REACTION    a 3-oxo-5beta-steroid + acceptor = a 3-oxo-Delta4-steroid + reduced
            acceptor [RN:R02642]
ALL_REAC    R02642 > R01835 R02215 R02498 R03714 R03850 R04817 R04823 R04841;
            (other) R02219
SUBSTRATE   3-oxo-5beta-steroid [CPD:C02797];
            acceptor [CPD:C00028]
PRODUCT     3-oxo-Delta4-steroid [CPD:C00619];
            reduced acceptor [CPD:C00030]
REFERENCE   1  [PMID:5907467]
  AUTHORS   Davidson SJ, Talalay P.
  TITLE     Purification and mechanism of action of a steroid
            delta-4-5-beta-dehydrogenase.
  JOURNAL   J. Biol. Chem. 241 (1966) 906-15.
  ORGANISM  Pseudomonas testosteroni
PATHWAY     PATH: map00120  Bile acid biosynthesis
            PATH: map00140  C21-Steroid hormone metabolism
            PATH: map00150  Androgen and estrogen metabolism
ORTHOLOGY   KO: K00251  3-oxo-5beta-steroid 4-dehydrogenase
GENES       HSA: 6718(AKR1D1)
            PTR: 472607(AKR1D1)
            MMU: 208665(Akr1d1)
            RNO: 192242(Akr1d1)
            CFA: 482711(AKR1D1)
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.6
            ExPASy - ENZYME nomenclature database: 1.3.99.6
            ExplorEnz - The Enzyme Database: 1.3.99.6
            ERGO genome analysis and discovery system: 1.3.99.6
            BRENDA, the Enzyme Database: 1.3.99.6
            CAS: 9067-97-4
///
ENTRY       EC 1.3.99.7                 Enzyme
NAME        glutaryl-CoA dehydrogenase;
            glutaryl coenzyme A dehydrogenase;
            glutaryl-CoA:(acceptor) 2,3-oxidoreductase (decarboxylating)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     glutaryl-CoA:acceptor 2,3-oxidoreductase (decarboxylating)
REACTION    glutaryl-CoA + acceptor = crotonoyl-CoA + CO2 + reduced acceptor
            [RN:R02488]
ALL_REAC    R02488 > R02487;
            (other) R05579
SUBSTRATE   glutaryl-CoA [CPD:C00527];
            acceptor [CPD:C00028]
PRODUCT     crotonoyl-CoA [CPD:C00877];
            CO2 [CPD:C00011];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein.
REFERENCE   1  [PMID:4304226]
  AUTHORS   Besrat A, Polan CE, Henderson LM.
  TITLE     Mammalian metabolism of glutaric acid.
  JOURNAL   J. Biol. Chem. 244 (1969) 1461-7.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00071  Fatty acid metabolism
            PATH: map00310  Lysine degradation
            PATH: map00380  Tryptophan metabolism
            PATH: map00632  Benzoate degradation via CoA ligation
ORTHOLOGY   KO: K00252  glutaryl-CoA dehydrogenase
GENES       HSA: 2639(GCDH)
            MMU: 270076(Gcdh)
            CFA: 476696(GCDH)
            XLA: 446458(gcdh)
            DRE: 393860(gcdh)
            SPU: 580832(LOC580832)
            DME: Dmel_CG9547
            CEL: F54D5.7
            OSA: 4337904
            ANI: AN2762.2
            AFM: AFUA_3G06040
            AOR: AO090020000074
            CNE: CNG03020
            UMA: UM01335.1
            DDI: DDBDRAFT_0167901 DDBDRAFT_0185491
            TET: TTHERM_00079730 TTHERM_00138150 TTHERM_00313080
            TCR: 508951.40 510121.40
            XCC: XCC1429(gcdH)
            XCB: XC_2809
            XCV: XCV1529
            XAC: XAC1472(gcdH)
            XOO: XOO1517(gcdH)
            XOM: XOO_1408(XOO1408)
            PAE: PA0447(gcdH)
            PAU: PA14_05840(gcdH)
            PPU: PP_0158(gcdH)
            PST: PSPTO_5461
            PSB: Psyr_5014
            PFL: PFL_0117(gcdH)
            PFO: Pfl_0117
            PEN: PSEEN0120(gcdH)
            PAR: Psyc_0805(gcdH)
            PCR: Pcryo_0815
            ACI: ACIAD1660(gcdH)
            SDN: Sden_3018
            ILO: IL0178
            CPS: CPS_4667(gcdH)
            PAT: Patl_3993
            LPN: lpg2580(gcdH)
            LPF: lpl2502(gcdH)
            LPP: lpp2632(gcdH)
            HCH: HCH_06122
            ABO: ABO_0984(gcdH)
            AHA: AHA_1250
            CVI: CV_3918
            RSO: RSc0756(gcdH)
            REU: Reut_A0805
            REH: H16_A2818(gcdH)
            RME: Rmet_2653
            BMA: BMA2064(gcdH)
            BMV: BMASAVP1_A0845(gcdH)
            BML: BMA10299_A2678(gcdH)
            BXE: Bxe_A3904
            BUR: Bcep18194_A3906 Bcep18194_B1396
            BCN: Bcen_0330
            BCH: Bcen2424_0813
            BAM: Bamb_0694
            BPS: BPSL2747
            BPM: BURPS1710b_3237
            BTE: BTH_I1390
            BPE: BP1537(gcdH)
            BPA: BPP0656(gcdH) BPP1209(gcdH)
            BBR: BB0663(gcdH) BB1426(gcdH)
            RFR: Rfer_4070
            POL: Bpro_1671
            MPT: Mpe_A3170
            EBA: ebA2993(gcdH)
            AZO: azo1924(gcdH1) azo1930(gcdH2)
            DAR: Daro_0539
            GME: Gmet_2075
            MLO: mll2878
            MES: Meso_2481
            SME: SMb21181
            ATU: Atu4418(gcdH)
            ATC: AGR_L_896
            RET: RHE_PE00272(gcdH)
            RLE: pRL110386
            BME: BMEI0897
            BMF: BAB1_1109
            BMS: BR1085
            BMB: BruAb1_1091
            BJA: blr2616(gcdH)
            BRA: BRADO2134(gcdH)
            BBT: BBta_2451(gcdH)
            RPA: RPA1094
            RPB: RPB_1162
            RPC: RPC_1037 RPC_4297
            RPD: RPD_1264
            RPE: RPE_4356
            NWI: Nwi_0608
            NHA: Nham_0753
            SIL: SPO1955(gcdH)
            SIT: TM1040_1255
            RSP: RSP_1295
            JAN: Jann_2813 Jann_3069
            RDE: RD1_3956(gcdH)
            MMR: Mmar10_1661
            SAL: Sala_2879
            RRU: Rru_A2005
            MAG: amb3231
            ABA: Acid345_0610
            SAU: SA0225
            SAV: SAV0233
            SAM: MW0209
            SAR: SAR0225(fadD)
            SAS: SAS0209
            SAC: SACOL0213
            SAA: SAUSA300_0227(fadD)
            SAO: SAOUHSC_00197
            SSP: SSP2425
            MTC: MT0410
            MBO: Mb0406c(fadE7)
            MPA: MAP3878c(fadE7)
            MSM: MSMEG_2466 MSMEG_5267 MSMEG_6686
            MMC: Mmcs_4147
            CGL: NCgl0283(cgl0288)
            CGB: cg0346(fadE)
            CEF: CE0324 CE0723 CE0729 CE2777
            CJK: jk0194(fadE1)
            NFA: nfa48280(fadE41)
            RHA: RHA1_ro02304
            SCO: SCO1750(2SCI34.03c)
            SMA: SAV1347(gcdH2) SAV6542(fadE12) SAV719(gcdH1)
            TFU: Tfu_1068
            SEN: SACE_1911(fadE7) SACE_5409(gcdH2)
            RXY: Rxyl_2061
            SRU: SRU_0115(gcdH) SRU_1116
            CHU: CHU_1408(caiA)
            FPS: FP0347(gcdH)
            DRA: DR_0551 DR_A0337
            DGE: Dgeo_1221 Dgeo_2761
            TTH: TTC0435
            TTJ: TTHA0789
            HAL: VNG2499G(gcdH)
            HMA: rrnAC1972(gcdH)
STRUCTURES  PDB: 1SIQ  1SIR  2EBA  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.7
            ExPASy - ENZYME nomenclature database: 1.3.99.7
            ExplorEnz - The Enzyme Database: 1.3.99.7
            ERGO genome analysis and discovery system: 1.3.99.7
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.99.7
            BRENDA, the Enzyme Database: 1.3.99.7
            CAS: 37255-38-2
///
ENTRY       EC 1.3.99.8                 Enzyme
NAME        2-furoyl-CoA dehydrogenase;
            furoyl-CoA hydroxylase;
            2-furoyl coenzyme A hydroxylase;
            2-furoyl coenzyme A dehydrogenase;
            2-furoyl-CoA:(acceptor) 5-oxidoreductase (hydroxylating)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     2-furoyl-CoA:acceptor 5-oxidoreductase (hydroxylating)
REACTION    2-furoyl-CoA + H2O + acceptor = S-(5-hydroxy-2-furoyl)-CoA + reduced
            acceptor [RN:R02987]
ALL_REAC    R02987
SUBSTRATE   2-furoyl-CoA [CPD:C00845];
            H2O [CPD:C00001];
            acceptor [CPD:C00028]
PRODUCT     S-(5-hydroxy-2-furoyl)-CoA [CPD:C03724];
            reduced acceptor [CPD:C00030]
COFACTOR    Copper [CPD:C00070]
COMMENT     A copper protein. The oxygen atom of the -OH produced is derived
            from water, not O2; the actual oxidative step is probably
            dehydrogenation of a hydrated form -CHOH-CH2- to -C(OH)=CH-, which
            tautomerizes non-enzymically to -CO-CH2-, giving
            (5-oxo-4,5-dihydro-2-furoyl)-CoA. Methylene blue, nitro blue,
            tetrazolium and a membrane fraction from Pseudomonas putida can act
            as acceptors.
REFERENCE   1  [PMID:4655411]
  AUTHORS   Kitcher JP, Trudgill PW, Rees JS.
  TITLE     Purification and properties of 2-furoyl-coenzyme A hydroxylase from
            Pseudomonas putida F2.
  JOURNAL   Biochem. J. 130 (1972) 121-32.
  ORGANISM  Pseudomonas putida [GN:ppu]
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.8
            ExPASy - ENZYME nomenclature database: 1.3.99.8
            ExplorEnz - The Enzyme Database: 1.3.99.8
            ERGO genome analysis and discovery system: 1.3.99.8
            BRENDA, the Enzyme Database: 1.3.99.8
            CAS: 9068-18-2
///
ENTRY       EC 1.3.99.9       Obsolete  Enzyme
NAME        Transferred to 1.21.99.1
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
COMMENT     Transferred entry: now EC 1.21.99.1 beta-cyclopiazonate
            dehydrogenase (EC 1.3.99.9 created 1976, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.9
            ExPASy - ENZYME nomenclature database: 1.3.99.9
            ExplorEnz - The Enzyme Database: 1.3.99.9
            ERGO genome analysis and discovery system: 1.3.99.9
            BRENDA, the Enzyme Database: 1.3.99.9
///
ENTRY       EC 1.3.99.10                Enzyme
NAME        isovaleryl-CoA dehydrogenase;
            isovaleryl-coenzyme A dehydrogenase;
            isovaleroyl-coenzyme A dehydrogenase;
            3-methylbutanoyl-CoA:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     3-methylbutanoyl-CoA:acceptor oxidoreductase
REACTION    3-methylbutanoyl-CoA + acceptor = 3-methylbut-2-enoyl-CoA + reduced
            acceptor [RN:R04096]
ALL_REAC    R04096 > R04095
SUBSTRATE   3-methylbutanoyl-CoA [CPD:C02939];
            acceptor [CPD:C00028]
PRODUCT     3-methylbut-2-enoyl-CoA [CPD:C03069];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein; forms with electron-transferring flavoprotein and EC
            1.5.5.1 electron-transferring-flavoprotein dehydrogenase, a system
            reducing ubiquinone. n-Pentanoate can act as donor. Not identical
            with EC 1.3.99.2 (butyryl-CoA dehydrogenase), EC 1.3.99.3 (acyl-CoA
            dehydrogenase) or EC 1.3.99.12 (2-methylacyl-CoA dehydrogenase).
REFERENCE   1  [PMID:13319276]
  AUTHORS   BACHHAWAT BK, ROBINSON WG, COON MJ.
  TITLE     Enzymatic carboxylation of beta-hydroxyisovaleryl coenzyme A.
  JOURNAL   J. Biol. Chem. 219 (1956) 539-50.
  ORGANISM  rat [GN:rno], pig [GN:ssc]
REFERENCE   2  [PMID:6401713]
  AUTHORS   Ikeda Y, Tanaka K.
  TITLE     Purification and characterization of isovaleryl coenzyme A
            dehydrogenase from rat liver mitochondria.
  JOURNAL   J. Biol. Chem. 258 (1983) 1077-85.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:5229850]
  AUTHORS   Tanaka K, Budd MA, Efron ML, Isselbacher KJ.
  TITLE     Isovaleric acidemia: a new genetic defect of leucine metabolism.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 56 (1966) 236-42.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
ORTHOLOGY   KO: K00253  isovaleryl-CoA dehydrogenase
GENES       HSA: 3712(IVD)
            MMU: 56357(Ivd)
            RNO: 24513(Ivd)
            CFA: 478259(IVD)
            GGA: 423011(IVD)
            XTR: 496848(LOC496848)
            DRE: 368775(ivd)
            SPU: 591888(LOC591888)
            DME: Dmel_CG6638
            CEL: C02B10.1 C02D5.1
            ATH: AT3G45300(IVD)
            OSA: 4337676
            CME: CMT072C
            ANI: AN4688.2
            AFM: AFUA_5G08930
            AOR: AO090020000493
            CNE: CNA04330
            UMA: UM04833.1
            DDI: DDB_0230189(ivdA)
            TET: TTHERM_01019590
            TBR: Tb11.55.0026
            LMA: LmjF27.0930
            XCC: XCC0246(acdA)
            XCB: XC_0256
            XAC: XAC0265(acdA)
            XOO: XOO4379(acdA)
            XOM: XOO_4123(XOO4123)
            VVU: VV2_0496
            VVY: VVA1046
            VPA: VPA0618 VPA1125
            PPR: PBPRB1114
            PAE: PA2015
            PAU: PA14_38440(gnyD)
            PPU: PP_4064(ivd)
            PST: PSPTO_2739
            PSB: Psyr_2470
            PFL: PFL_3936(ivd)
            PFO: Pfl_3656
            PEN: PSEEN3386(ivd)
            PAR: Psyc_0313(acd)
            PCR: Pcryo_0344
            SON: SO_1897(ivd)
            SDN: Sden_2245
            SFR: Sfri_2727
            SAZ: Sama_1362
            SBL: Sbal_2828
            SLO: Shew_2570
            SHE: Shewmr4_2322
            SHM: Shewmr7_2394
            SHN: Shewana3_1672
            SHW: Sputw3181_2306
            ILO: IL0874
            CPS: CPS_1603(ivd)
            PHA: PSHAa0906 PSHAa1452
            PAT: Patl_2925
            MAQ: Maqu_2121
            CBU: CBU_0973
            LPN: lpg1824
            LPF: lpl1788
            LPP: lpp1787
            NOC: Noc_1735
            HCH: HCH_03943
            ABO: ABO_1240(ivd)
            AHA: AHA_2078
            CVI: CV_1766
            RSO: RSc0279(RS03246)
            REU: Reut_A0135 Reut_A1466
            REH: H16_A0167(ivd1) H16_A1291 H16_A1972(ivd2)
            RME: Rmet_0103
            BMA: BMAA0802(ivd)
            BMV: BMASAVP1_0542(ivd)
            BML: BMA10299_0654(ivd)
            BMN: BMA10247_A1608(ivd)
            BXE: Bxe_B0960
            BUR: Bcep18194_A3297 Bcep18194_A4473 Bcep18194_A4816
                 Bcep18194_A5469 Bcep18194_A5559 Bcep18194_A5560
                 Bcep18194_A6219 Bcep18194_A6220 Bcep18194_B0423
                 Bcep18194_B1437 Bcep18194_B1441 Bcep18194_B2484
                 Bcep18194_C7127 Bcep18194_C7145 Bcep18194_C7146
                 Bcep18194_C7297 Bcep18194_C7499 Bcep18194_C7558
                 Bcep18194_C7712
            BCN: Bcen_3127
            BCH: Bcen2424_5240
            BAM: Bamb_2269 Bamb_2270 Bamb_2932 Bamb_2933 Bamb_4588
            BPS: BPSS1448
            BPM: BURPS1710b_A0471
            BTE: BTH_II0288 BTH_II0947
            BPE: BP0440 BP0444
            BPA: BPP4359(ivd)
            BBR: BB4945(ivd)
            RFR: Rfer_3842
            POL: Bpro_4190
            VEI: Veis_2500
            MPT: Mpe_A3360
            HAR: HEAR1044
            EBA: ebA4656(acd)
            AZO: azo3081
            DAR: Daro_0100
            GME: Gmet_3289
            BBA: Bd1201
            SFU: Sfum_1260
            MLO: mll7732
            MES: Meso_0931
            SME: SMb21121(ivdH)
            ATU: Atu3477(acd)
            ATC: AGR_L_2707
            RET: RHE_PC00064(ivdH)
            RLE: pRL100296(ivdH)
            BME: BMEI1923
            BMS: BR0020(ivd)
            BMB: BruAb1_0020(ivd)
            BOV: BOV_0017(ivd)
            BJA: blr4419(acd)
            BRA: BRADO0920 BRADO1442 BRADO1447(ivd2) BRADO3035
            BBT: BBta_5105 BBta_6658(ivd2) BBta_6663 BBta_7132
            RPA: RPA1614(ivd2)
            RPB: RPB_3933
            RPC: RPC_4263
            RPD: RPD_0356 RPD_3693
            RPE: RPE_4310
            NWI: Nwi_2006 Nwi_2995 Nwi_3018
            NHA: Nham_3387
            CCR: CC_2172
            SIL: SPO2793(ivD)
            SIT: TM1040_0732 TM1040_2444
            RSP: RSP_2506(ivdH)
            RSH: Rsph17029_0312
            JAN: Jann_1142
            RDE: RD1_3301(ivd)
            MMR: Mmar10_1739
            HNE: HNE_1272(ivd2)
            RRU: Rru_A1948 Rru_A3064
            MAG: amb0677
            MJL: Mjls_4228
            RHA: RHA1_ro11032
            FAL: FRAAL2513 FRAAL3418 FRAAL4873 FRAAL6459
            SEN: SACE_0015
            LIL: LA0414
            LIC: LIC10363(ivd)
            LBJ: LBJ_2429(ivd)
            LBL: LBL_0682(ivd)
            AVA: Ava_1648
            TAC: Ta0230
            TVO: TVN1269
            PTO: PTO1189
STRUCTURES  PDB: 1IVH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.10
            ExPASy - ENZYME nomenclature database: 1.3.99.10
            ExplorEnz - The Enzyme Database: 1.3.99.10
            ERGO genome analysis and discovery system: 1.3.99.10
            BRENDA, the Enzyme Database: 1.3.99.10
            CAS: 37274-61-6
///
ENTRY       EC 1.3.99.11                Enzyme
NAME        dihydroorotate dehydrogenase;
            dihydroorotate:ubiquinone oxidoreductase;
            (S)-dihydroorotate:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     (S)-dihydroorotate:acceptor oxidoreductase
REACTION    (S)-dihydroorotate + acceptor = orotate + reduced acceptor
            [RN:R01868]
ALL_REAC    R01868;
            (other) R01867 R01869
SUBSTRATE   (S)-dihydroorotate [CPD:C00337];
            acceptor [CPD:C00028]
PRODUCT     orotate [CPD:C00295];
            reduced acceptor [CPD:C00030]
COFACTOR    Iron [CPD:C00023];
            Zinc [CPD:C00038]
COMMENT     An iron-zinc protein. Oxygen can act as acceptor, but much more
            slowly than 2,6-dichloroindophenol or 1,10-phenanthroline.
REFERENCE   1  [PMID:216313]
  AUTHORS   Forman HJ, Kennedy J.
  TITLE     Mammalian dihydroorotate dehydrogenase: physical and catalytic
            properties of the primary enzyme.
  JOURNAL   Arch. Biochem. Biophys. 191 (1978) 23-31.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K00254  dihydroorotate dehydrogenase
STRUCTURES  PDB: 1TV5  1UUM  1UUO  2B4G  2BSL  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.11
            ExPASy - ENZYME nomenclature database: 1.3.99.11
            ExplorEnz - The Enzyme Database: 1.3.99.11
            ERGO genome analysis and discovery system: 1.3.99.11
            BRENDA, the Enzyme Database: 1.3.99.11
            CAS: 9029-03-2
///
ENTRY       EC 1.3.99.12                Enzyme
NAME        2-methylacyl-CoA dehydrogenase;
            branched-chain acyl-CoA dehydrogenase;
            2-methyl branched chain acyl-CoA dehydrogenase;
            2-methylbutanoyl-CoA:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     2-methylbutanoyl-CoA:acceptor oxidoreductase
REACTION    2-methylbutanoyl-CoA + acceptor = 2-methylbut-2-enoyl-CoA + reduced
            acceptor [RN:R03173]
ALL_REAC    R03173 > R03172;
            (other) R02661
SUBSTRATE   2-methylbutanoyl-CoA [CPD:C01033];
            acceptor [CPD:C00028]
PRODUCT     2-methylbut-2-enoyl-CoA [CPD:C03345];
            reduced acceptor [CPD:C00030]
COMMENT     Also oxidizes 2-methylpropanoyl-CoA. Not identical with EC 1.3.99.2
            (butyryl-CoA dehydrogenase), EC 1.3.99.3 (acyl-CoA dehydrogenase),
            EC 1.3.99.10 (isovaleryl-CoA dehydrogenase) or EC 1.3.99.13
            (long-chain-acyl-CoA dehydrogenase).
REFERENCE   1  [PMID:6401712]
  AUTHORS   Ikeda Y, Dabrowski C, Tanaka K.
  TITLE     Separation and properties of five distinct acyl-CoA dehydrogenases
            from rat liver mitochondria. Identification of a new 2-methyl
            branched chain acyl-CoA dehydrogenase.
  JOURNAL   J. Biol. Chem. 258 (1983) 1066-76.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.12
            ExPASy - ENZYME nomenclature database: 1.3.99.12
            ExplorEnz - The Enzyme Database: 1.3.99.12
            ERGO genome analysis and discovery system: 1.3.99.12
            BRENDA, the Enzyme Database: 1.3.99.12
            CAS: 85130-32-1
///
ENTRY       EC 1.3.99.13                Enzyme
NAME        long-chain-acyl-CoA dehydrogenase;
            palmitoyl-CoA dehydrogenase;
            palmitoyl-coenzyme A dehydrogenase;
            long-chain acyl-coenzyme A dehydrogenase;
            long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     long-chain-acyl-CoA:acceptor 2,3-oxidoreductase
REACTION    acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor
            [RN:R00392]
ALL_REAC    R00392 > R01279 R03777 R03857 R03990 R04751 R04754
SUBSTRATE   acyl-CoA [CPD:C00040];
            acceptor [CPD:C00028]
PRODUCT     2,3-dehydroacyl-CoA [CPD:C00605];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD); forms with another flavoprotein
            ('electron-transferring flavoprotein') and EC 1.5.5.1 a system
            reducing ubiquinone and other acceptors. Not identical with EC
            1.3.99.2 (butyryl-CoA dehydrogenase), EC 1.3.99.3 (acyl-CoA
            dehydrogenase), EC 1.3.99.10 (isovaleryl-CoA dehydrogenase) or EC
            1.3.99.12 (2-methylacyl-CoA dehydrogenase).
REFERENCE   1  [PMID:1015826]
  AUTHORS   Hall CL, Heijkenskjold L, Bartfai T, Ernster L, Kamin H.
  TITLE     Acyl coenzyme A dehydrogenases and electron-transferring
            flavoprotein from beef hart mitochondria.
  JOURNAL   Arch. Biochem. Biophys. 177 (1976) 402-14.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:13319294]
  AUTHORS   HAUGE JG, CRANE FL, BEINERT H.
  TITLE     On the mechanism of dehydrogenation of fatty acyl derivatives of
            coenzyme A.  III.  Palmityl coA dehydrogenase.
  JOURNAL   J. Biol. Chem. 219 (1956) 727-33.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:3968063]
  AUTHORS   Ikeda Y, Okamura-Ikeda K, Tanaka K.
  TITLE     Purification and characterization of short-chain, medium-chain, and
            long-chain acyl-CoA dehydrogenases from rat liver mitochondria.
            Isolation of the holo- and apoenzymes and conversion of the
            apoenzyme to the holoenzyme.
  JOURNAL   J. Biol. Chem. 260 (1985) 1311-25.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00071  Fatty acid metabolism
            PATH: map03320  PPAR signaling pathway
ORTHOLOGY   KO: K00255  long-chain-acyl-CoA dehydrogenase
GENES       HSA: 33(ACADL)
            MMU: 11363(Acadl)
            RNO: 25287(Acadl)
            CFA: 478895(ACADL)
            BTA: 614508(MGC151674)
            SSC: 396931(ACADL)
            GGA: 424005(ACADL)
            XLA: 446669(acadl)
            DRE: 394156(acadl)
            SPU: 577166(LOC577166)
            PAP: PSPA7_4192
            ACI: ACIAD1723(hcaD) ACIAD2226 ACIAD3191(fadE)
            BMV: BMASAVP1_A3482
            BMN: BMA10247_2728
            BUR: Bcep18194_C6743 Bcep18194_C6744 Bcep18194_C7184
            SAT: SYN_02128
            SIL: SPO2380
            SIT: TM1040_1559
            RDE: RD1_3970(fadE)
            NAR: Saro_0132
            MAV: MAV_1822 MAV_2561 MAV_3616 MAV_4768
            MSM: MSMEG_5197
            MVA: Mvan_2439
            RHA: RHA1_ro00550 RHA1_ro02345 RHA1_ro02627 RHA1_ro02715
                 RHA1_ro02754 RHA1_ro03954 RHA1_ro05132 RHA1_ro06787
                 RHA1_ro08138
            FAL: FRAAL0412 FRAAL2362 FRAAL2625 FRAAL3144 FRAAL4870
            SEN: SACE_3993 SACE_6369
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.13
            ExPASy - ENZYME nomenclature database: 1.3.99.13
            ExplorEnz - The Enzyme Database: 1.3.99.13
            ERGO genome analysis and discovery system: 1.3.99.13
            BRENDA, the Enzyme Database: 1.3.99.13
            CAS: 59536-74-2
///
ENTRY       EC 1.3.99.14                Enzyme
NAME        cyclohexanone dehydrogenase;
            cyclohexanone:(acceptor) 2-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     cyclohexanone:acceptor 2-oxidoreductase
REACTION    cyclohexanone + acceptor = cyclohex-2-enone + reduced acceptor
            [RN:R02234]
ALL_REAC    R02234
SUBSTRATE   cyclohexanone [CPD:C00414];
            acceptor [CPD:C00028]
PRODUCT     cyclohex-2-enone [CPD:C02395];
            reduced acceptor [CPD:C00030]
COMMENT     2,6-Dichloroindophenol can act as acceptor. The corresponding
            ketones of cyclopentane and cycloheptane cannot act as donors.
REFERENCE   1
  AUTHORS   Dangel, W., Tschech, A. and Fuchs, G.
  TITLE     Enzyme-reactions involved in anaerobic cyclohexanol metabolism by a
            denitrifying Pseudomonas species.
  JOURNAL   Arch. Microbiol. 152 (1989) 273-279.
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.14
            ExPASy - ENZYME nomenclature database: 1.3.99.14
            ExplorEnz - The Enzyme Database: 1.3.99.14
            ERGO genome analysis and discovery system: 1.3.99.14
            BRENDA, the Enzyme Database: 1.3.99.14
            CAS: 123516-43-8
///
ENTRY       EC 1.3.99.15                Enzyme
NAME        benzoyl-CoA reductase;
            benzoyl-CoA reductase (dearomatizing)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     cyclohexa-1,5-diene-1-carbonyl-CoA:acceptor oxidoreductase
            (aromatizing, ATP-forming)
REACTION    benzoyl-CoA + reduced acceptor + 2 ATP + 2 H2O =
            cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + 2 ADP + 2 phosphate
            [RN:R02451]
ALL_REAC    R02451;
            (other) R00283
SUBSTRATE   benzoyl-CoA [CPD:C00512];
            reduced acceptor [CPD:C00030];
            ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     cyclohexa-1,5-diene-1-carbonyl-CoA [CPD:C06322];
            acceptor [CPD:C00028];
            ADP [CPD:C00008];
            phosphate [CPD:C00009]
COFACTOR    Manganese [CPD:C00034];
            Magnesium [CPD:C00305]
COMMENT     An iron-sulfur protein. Requires Mg2+ or Mn2+. Reduced methyl
            viologen can act as electron donor. Inactive towards aromatic acids
            that are not CoA esters but will also catalyse the reaction: ammonia
            + acceptor + 2 ADP + 2 phosphate + H2O = hydroxylamine + reduced
            acceptor + 2 ATP. In the presence of reduced acceptor, but in the
            absence of oxidizable substrate, the enzyme catalyses the hydrolysis
            of ATP to ADP plus phosphate.
REFERENCE   1  [PMID:8575453]
  AUTHORS   Boll M, Fuchs G.
  TITLE     Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of
            anaerobic aromatic metabolism. ATP dependence of the reaction,
            purification and some properties of the enzyme from Thauera
            aromatica strain K172.
  JOURNAL   Eur. J. Biochem. 234 (1995) 921-33.
  ORGANISM  Thauera aromatica
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
ORTHOLOGY   KO: K04111  benzoyl-CoA reductase
            KO: K04112  benzoyl-CoA reductase subunit
            KO: K04113  benzoyl-CoA reductase subunit
            KO: K04114  benzoyl-CoA reductase subunit
            KO: K04115  benzoyl-CoA reductase subunit
GENES       RPA: RPA0657(badD) RPA0658(badE) RPA0659(badF) RPA0660(badG)
            RPC: RPC_1026 RPC_1027 RPC_1028 RPC_1029
            RPD: RPD_1535 RPD_1536 RPD_1537 RPD_1538
            RPE: RPE_0605 RPE_0606 RPE_0607 RPE_0608
            MAG: amb2138 amb2139 amb2140 amb2141
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.15
            ExPASy - ENZYME nomenclature database: 1.3.99.15
            ExplorEnz - The Enzyme Database: 1.3.99.15
            ERGO genome analysis and discovery system: 1.3.99.15
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.99.15
            BRENDA, the Enzyme Database: 1.3.99.15
            CAS: 176591-18-7
///
ENTRY       EC 1.3.99.16                Enzyme
NAME        isoquinoline 1-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     isoquinoline:acceptor 1-oxidoreductase (hydroxylating)
REACTION    isoquinoline + acceptor + H2O = isoquinolin-1(2H)-one + reduced
            acceptor [RN:R05151]
ALL_REAC    R05151
SUBSTRATE   isoquinoline [CPD:C06323];
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
PRODUCT     isoquinolin-1(2H)-one [CPD:C06324];
            reduced acceptor [CPD:C00030]
COMMENT     The enzyme from Pseudomonas diminuta is specific towards
            N-containing N-heterocyclic substrates, including isoquinoline,
            isoquinolin-5-ol, phthalazine and quinazoline. Electron acceptors
            include 1,2-benzoquinone, cytochrome c, ferricyanide,
            iodonitrotetrazolium chloride, nitroblue tetrazolium, Meldola blue
            and phenazine methosulfate.
REFERENCE   1  [PMID:8157655]
  AUTHORS   Lehmann M, Tshisuaka B, Fetzner S, Roger P, Lingens F.
  TITLE     Purification and characterization of isoquinoline 1-oxidoreductase
            from Pseudomonas diminuta 7, a novel molybdenum-containing
            hydroxylase.
  JOURNAL   J. Biol. Chem. 269 (1994) 11254-60.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:7782304]
  AUTHORS   Lehmann M, Tshisuaka B, Fetzner S, Lingens F.
  TITLE     Molecular cloning of the isoquinoline 1-oxidoreductase genes from
            Pseudomonas diminuta 7, structural analysis of iorA and iorB, and
            sequence comparisons with other molybdenum-containing hydroxylases.
  JOURNAL   J. Biol. Chem. 270 (1995) 14420-9.
  ORGANISM  Pseudomonas sp.
ORTHOLOGY   KO: K00256  isoquinoline 1-oxidoreductase
            KO: K07302  isoquinoline 1-oxidoreductase, alpha subunit
            KO: K07303  isoquinoline 1-oxidoreductase, beta subunit
GENES       PAE: PA1880 PA1881 PA2378 PA2379
            PPU: PP_2477 PP_2478 PP_3621 PP_3622
            PFL: PFL_1783 PFL_1784
            PFO: Pfl_2173 Pfl_2174 Pfl_2472 Pfl_2473 Pfl_3425 Pfl_3426
                 Pfl_4169 Pfl_4170
            PEN: PSEEN2171 PSEEN2172
            SON: SO_3048 SO_3049
            SDN: Sden_2223 Sden_2224
            SFR: Sfri_0200
            SHE: Shewmr4_1440
            SHN: Shewana3_1496 Shewana3_1497
            CPS: CPS_0277(iorB) CPS_0278(iorA)
            PAT: Patl_2510 Patl_2511 Patl_2601 Patl_2602
            SDE: Sde_2853
            MAQ: Maqu_0906
            TCX: Tcr_0231 Tcr_0232
            HCH: HCH_01589(coxS) HCH_01590(coxL) HCH_05037
            CVI: CV_1673 CV_1674
            RSO: RS05441(RSp0325) RS05442(RSp0324) RSc0626(RS01528)
                 RSc0627(RS01529) RSc1889(iorB2) RSc1890(iorA2)
            REU: Reut_A1743 Reut_A1744 Reut_A2509 Reut_A2661 Reut_A2662
            REH: H16_A1652(iorB1) H16_A1653(iorA1) H16_B1523(iorB2)
                 H16_B1524(iorA2)
            RME: Rmet_0594 Rmet_0595
            BMA: BMAA1154(iorA) BMAA1154.1(iorB)
            BML: BMA10299_0085(iorB) BMA10299_0086(iorA)
            BMN: BMA10247_A1530(iorA) BMA10247_A1531(iorB)
            BXE: Bxe_B1690 Bxe_B1691 Bxe_B2506 Bxe_B2616 Bxe_B2617
            BUR: Bcep18194_A4470 Bcep18194_A4956 Bcep18194_A4957
                 Bcep18194_B0641 Bcep18194_B0642 Bcep18194_B0806
                 Bcep18194_B0807 Bcep18194_B0862 Bcep18194_B0863
                 Bcep18194_B1602 Bcep18194_B1603
            BCN: Bcen_3174 Bcen_3960
            BCH: Bcen2424_4407 Bcen2424_5194
            BAM: Bamb_1231
            BPS: BPSS0679 BPSS0680
            BPM: BURPS1710b_A2249(iorB) BURPS1710b_A2250(iorA)
            BTE: BTH_II1746 BTH_II1747
            BPE: BP2126 BP2127
            BPA: BPP0703 BPP0704 BPP1351
            BBR: BB0710 BB0711 BB2417 BB2418
            POL: Bpro_3556 Bpro_3557 Bpro_4058 Bpro_4227 Bpro_4228
            AAV: Aave_3932
            MPT: Mpe_A2930 Mpe_A3626 Mpe_A3627
            HAR: HEAR1179(iorA) HEAR1180(iorB)
            MMS: mma_0765
            AZO: azo0021(iorA)
            DAR: Daro_1891 Daro_1892
            MFA: Mfla_2619 Mfla_2620
            GSU: GSU0200(iorA) GSU0201(iorB)
            GME: Gmet_0837 Gmet_0838 Gmet_3490
            ADE: Adeh_3102 Adeh_3103
            MXA: MXAN_1751(iorA) MXAN_1752(iorB) MXAN_4829(iorB)
                 MXAN_4830(iorA)
            MLO: mll3836 mll3837
            SME: SMa1488 SMa1491 SMb20342 SMb20343
            RLE: RL2499(iorA) RL2500(iorB)
            BJA: bll1530 bll1531 bll2736 bll2737 blr6218 blr6219
            BRA: BRADO0449(iorA) BRADO0450 BRADO1711 BRADO1712 BRADO2114
                 BRADO2115 BRADO2413 BRADO2414 BRADO5488(iorA) BRADO5489(iorB)
                 BRADO7136
            BBT: BBta_2023 BBta_2287(iorA) BBta_2288 BBta_2423 BBta_2424
                 BBta_2766 BBta_2767 BBta_3260(iorA) BBta_3261 BBta_5972(iorA)
                 BBta_5973(iorB) BBta_7867
            RPB: RPB_2280 RPB_2281
            RPC: RPC_3465
            RPE: RPE_3603 RPE_3604
            CCR: CC_0021 CC_0022 CC_2269 CC_2270
            SIL: SPO2826(iorA) SPO2827
            SIT: TM1040_3146 TM1040_3147 TM1040_3229 TM1040_3230
            RSP: RSP_3163 RSP_3164
            RDE: RD1_0246(iorA) RD1_0247(iorB) RD1_A0087 RD1_A0088(iorA)
            HNE: HNE_2200 HNE_2202 HNE_2482 HNE_2483
            SWI: Swit_4597
            ELI: ELI_11225 ELI_11230
            GOX: GOX0586
            MAG: amb4196
            ABA: Acid345_1932 Acid345_3112
            SMA: SAV515 SAV516
            SEN: SACE_2974(iorA) SACE_2975(iorB)
            AAE: aq_227(aldH2)
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.16
            ExPASy - ENZYME nomenclature database: 1.3.99.16
            ExplorEnz - The Enzyme Database: 1.3.99.16
            ERGO genome analysis and discovery system: 1.3.99.16
            BRENDA, the Enzyme Database: 1.3.99.16
            CAS: 155948-73-5
///
ENTRY       EC 1.3.99.17                Enzyme
NAME        quinoline 2-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     quinoline:acceptor 2-oxidoreductase (hydroxylating)
REACTION    quinoline + acceptor + H2O = isoquinolin-1(2H)-one + reduced
            acceptor [RN:R05152]
ALL_REAC    R05152
SUBSTRATE   quinoline [CPD:C06413];
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
PRODUCT     isoquinolin-1(2H)-one [CPD:C06324];
            reduced acceptor [CPD:C00030]
COMMENT     Quinolin-2-ol, quinolin-7-ol, quinolin-8-ol, 3-, 4- and
            8-methylquinolines and 8-chloroquinoline are substrates.
            Iodonitrotetrazolium chloride can act as an electron acceptor.
REFERENCE   1  [PMID:2090161]
  AUTHORS   Bauder R, Tshisuaka B, Lingens F.
  TITLE     Microbial metabolism of quinoline and related compounds. VII.
            Quinoline oxidoreductase from Pseudomonas putida: a
            molybdenum-containing enzyme.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 371 (1990) 1137-44.
REFERENCE   2  [PMID:8251516]
  AUTHORS   Tshisuaka B, Kappl R, Huttermann J, Lingens F.
  TITLE     Quinoline oxidoreductase from Pseudomonas putida 86: an improved
            purification procedure and electron paramagnetic resonance
            spectroscopy.
  JOURNAL   Biochemistry. 32 (1993) 12928-34.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   3  [PMID:1789933]
  AUTHORS   Peschke B, Lingens F.
  TITLE     Microbial metabolism of quinoline and related compounds. XII.
            Isolation and characterization of the quinoline oxidoreductase from
            Rhodococcus spec. B1 compared with the quinoline oxidoreductase from
            Pseudomonas putida 86.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 372 (1991) 1081-8.
  ORGANISM  Pseudomonas putida [GN:ppu], Rhodococcus sp.
REFERENCE   4  [PMID:7556204]
  AUTHORS   Schach S, Tshisuaka B, Fetzner S, Lingens F.
  TITLE     Quinoline 2-oxidoreductase and 2-oxo-1,2-dihydroquinoline
            5,6-dioxygenase from Comamonas testosteroni 63. The first two
            enzymes in quinoline and 3-methylquinoline degradation.
  JOURNAL   Eur. J. Biochem. 232 (1995) 536-44.
  ORGANISM  Comamonas testosteroni
STRUCTURES  PDB: 1T3Q  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.17
            ExPASy - ENZYME nomenclature database: 1.3.99.17
            ExplorEnz - The Enzyme Database: 1.3.99.17
            ERGO genome analysis and discovery system: 1.3.99.17
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.99.17
            BRENDA, the Enzyme Database: 1.3.99.17
            CAS: 132264-32-5
///
ENTRY       EC 1.3.99.18                Enzyme
NAME        quinaldate 4-oxidoreductase;
            quinaldic acid 4-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     quinoline-2-carboxylate:acceptor 4-oxidoreductase (hydroxylating)
REACTION    quinaldate + acceptor + H2O = kynurenate + reduced acceptor
            [RN:R03687]
ALL_REAC    R03687
SUBSTRATE   quinaldate [CPD:C06325];
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
PRODUCT     kynurenate [CPD:C01717];
            reduced acceptor [CPD:C00030]
COMMENT     The enzyme from Pseudomonas sp. AK2 also acts on
            quinoline-8-carboxylate, whereas that from Serratia marcescens 2CC-1
            will oxidize nicotinate; quinaldate is a substrate for both of these
            enzymes. 2,4,6-Trinitrobenzene sulfonate, 1,4-benzoquinone,
            1,2-naphthoquinone, nitroblue tetrazolium, thionine and menadione
            will serve as an electron acceptor for the former enzyme and
            ferricyanide for the latter; Meldola blue, iodonitrotetrazolium
            chloride, phenazine methosulfate, 2,6-dichlorophenolindophenol and
            cytochrome c will act as electron acceptors for both.
REFERENCE   1  [PMID:8292263]
  AUTHORS   Sauter M, Tshisuaka B, Fetzner S, Lingens F.
  TITLE     Microbial metabolism of quinoline and related compounds. XX.
            Quinaldic acid 4-oxidoreductase from Pseudomonas sp. AK-2 compared
            to other procaryotic molybdenum-containing hydroxylases.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 374 (1993) 1037-46.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:8357532]
  AUTHORS   Fetzner S, Lingens F.
  TITLE     Microbial metabolism of quinoline and related compounds. XVIII.
            Purification and some properties of the molybdenum- and
            iron-containing quinaldic acid 4-oxidoreductase from Serratia
            marcescens 2CC-1.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 374 (1993) 363-76.
  ORGANISM  Serratia marcecens
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.18
            ExPASy - ENZYME nomenclature database: 1.3.99.18
            ExplorEnz - The Enzyme Database: 1.3.99.18
            ERGO genome analysis and discovery system: 1.3.99.18
            BRENDA, the Enzyme Database: 1.3.99.18
            CAS: 149885-77-8
///
ENTRY       EC 1.3.99.19                Enzyme
NAME        quinoline-4-carboxylate 2-oxidoreductase;
            quinaldic acid 4-oxidoreductase;
            quinoline-4-carboxylate:acceptor 2-oxidoreductase (hydroxylating)
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     quinoline-4-carboxylate:acceptor 2-oxidoreductase (hydroxylating)
REACTION    quinoline-4-carboxylate + acceptor + H2O =
            2-oxo-1,2-dihydroquinoline-4-carboxylate + reduced acceptor
            [RN:R05183]
ALL_REAC    R05183
SUBSTRATE   quinoline-4-carboxylate [CPD:C06414];
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
PRODUCT     2-oxo-1,2-dihydroquinoline-4-carboxylate;
            reduced acceptor [CPD:C00030]
COMMENT     A molybdenum---iron---sulfur flavoprotein with molybdopterin
            cytosine dinucleotide as the molybdenum cofactor. Quinoline,
            4-methylquinoline and 4-chloroquinoline can also serve as substrates
            for the enzyme from Agrobacterium sp. 1B. Iodonitrotetrazolium
            chloride, thionine, menadione and 2,6-dichlorophenolindophenol can
            act as electron acceptors.
REFERENCE   1  [PMID:1418685]
  AUTHORS   Bauer G, Lingens F.
  TITLE     Microbial metabolism of quinoline and related compounds. XV.
            Quinoline-4-carboxylic acid oxidoreductase from Agrobacterium
            spec.1B: a molybdenum-containing enzyme.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 373 (1992) 699-705.
  ORGANISM  Agrobacterium sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.19
            ExPASy - ENZYME nomenclature database: 1.3.99.19
            ExplorEnz - The Enzyme Database: 1.3.99.19
            ERGO genome analysis and discovery system: 1.3.99.19
            BRENDA, the Enzyme Database: 1.3.99.19
            CAS: 175780-18-4
///
ENTRY       EC 1.3.99.20                Enzyme
NAME        4-hydroxybenzoyl-CoA reductase;
            4-hydroxybenzoyl-CoA reductase (dehydroxylating);
            4-hydroxybenzoyl-CoA:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     benzoyl-CoA:acceptor oxidoreductase
REACTION    benzoyl-CoA + acceptor + H2O = 4-hydroxybenzoyl-CoA + reduced
            acceptor [RN:R05316]
ALL_REAC    R05316
SUBSTRATE   benzoyl-CoA [CPD:C00512];
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
PRODUCT     4-hydroxybenzoyl-CoA [CPD:C02949];
            reduced acceptor [CPD:C00030]
COMMENT     A molybdenum-flavin-iron-sulfur protein that is involved in the
            anaerobic pathway of phenol metabolism in bacteria. A ferredoxin
            with two [4Fe-4S] clusters functions as the natural electron donor
            [3]
REFERENCE   1  [PMID:2753161]
  AUTHORS   Glockler R, Tschech A, Fuchs G.
  TITLE     Reductive dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA in
            a denitrifying, phenol-degrading Pseudomonas species.
  JOURNAL   FEBS. Lett. 251 (1989) 237-40.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:9683649]
  AUTHORS   Heider J, Boll M, Breese K, Breinig S, Ebenau-Jehle C, Feil U,
            Gad'on N, Laempe D, Leuthner B, Mohamed ME, Schneider S, Burchhardt
            G, Fuchs G.
  TITLE     Differential induction of enzymes involved in anaerobic metabolism
            of aromatic compounds in the denitrifying bacterium Thauera
            aromatica.
  JOURNAL   Arch. Microbiol. 170 (1998) 120-31.
  ORGANISM  Thauera aromatica
REFERENCE   3  [PMID:9490068]
  AUTHORS   Breese K, Fuchs G.
  TITLE     4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from the
            denitrifying bacterium Thauera aromatica--prosthetic groups,
            electron donor, and genes of a member of the
            molybdenum-flavin-iron-sulfur proteins.
  JOURNAL   Eur. J. Biochem. 251 (1998) 916-23.
  ORGANISM  Thauera aromatica
REFERENCE   4  [PMID:8477729]
  AUTHORS   Brackmann R, Fuchs G.
  TITLE     Enzymes of anaerobic metabolism of phenolic compounds.
            4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from a denitrifying
            Pseudomonas species.
  JOURNAL   Eur. J. Biochem. 213 (1993) 563-71.
  ORGANISM  Pseudomonas sp.
REFERENCE   5  [PMID:9057820]
  AUTHORS   Heider J, Fuchs G.
  TITLE     Anaerobic metabolism of aromatic compounds.
  JOURNAL   Eur. J. Biochem. 243 (1997) 577-96.
  ORGANISM  Thauera aromatica, Azoarcus evansii, Rhodopseudonmonas palustris
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
ORTHOLOGY   KO: K04106  4-hydroxybenzoyl-CoA reductase
            KO: K04107  4-hydroxybenzoyl-CoA reductase subunit 1
            KO: K04108  4-hydroxybenzoyl-CoA reductase subunit 2
            KO: K04109  4-hydroxybenzoyl-CoA reductase subunit 3
GENES       REH: H16_B0743(hcrA) H16_B0744(hcrB) H16_B0745(hcrC)
            BUR: Bcep18194_B1542
            EBA: ebA3603(hcrA) ebA3604(hcrC)
            RPA: RPA0670(hbaB) RPA0671(hbaC) RPA0672(hbaD)
            RPC: RPC_1013 RPC_1014
            RPD: RPD_1523 RPD_1524 RPD_1525
            RPE: RPE_0589 RPE_0590 RPE_0591
            MAG: amb2019 amb2020 amb2021
            RHA: RHA1_ro05013
            SEN: SACE_4619
            AVA: Ava_C0127
STRUCTURES  PDB: 1RM6  1SB3  
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.20
            ExPASy - ENZYME nomenclature database: 1.3.99.20
            ExplorEnz - The Enzyme Database: 1.3.99.20
            ERGO genome analysis and discovery system: 1.3.99.20
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.99.20
            BRENDA, the Enzyme Database: 1.3.99.20
///
ENTRY       EC 1.3.99.21                Enzyme
NAME        (R)-benzylsuccinyl-CoA dehydrogenase;
            BbsG;
            (R)-benzylsuccinyl-CoA:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     (R)-benzylsuccinyl-CoA:acceptor oxidoreductase
REACTION    (R)-2-benzylsuccinyl-CoA + 2 electron-transferring flavoprotein =
            (E)-2-benzylidenesuccinyl-CoA + 2 reduced electron-transferring
            flavoprotein [RN:R05584]
ALL_REAC    R05584
SUBSTRATE   (R)-2-benzylsuccinyl-CoA [CPD:C09817];
            electron-transferring flavoprotein [CPD:C04253]
PRODUCT     (E)-2-benzylidenesuccinyl-CoA [CPD:C09818];
            reduced electron-transferring flavoprotein [CPD:C04570]
COMMENT     Requires FAD as cofactor. The enzyme is highly specific for
            (R)-benzylsuccinyl-CoA and is inhibited by (S)-benzylsuccinyl-CoA.
            Forms the third step in the anaerobic toluene metabolic pathway in
            Thauera aromatica. Uses the ferricenium ion as the preferred
            artificial electron acceptor. Unlike other acyl-CoA dehydrogenases,
            this enzyme exhibits high substrate- and enantiomer specificity.
REFERENCE   1  [PMID:12420174]
  AUTHORS   Leutwein C, Heider J.
  TITLE     (R)-Benzylsuccinyl-CoA dehydrogenase of Thauera aromatica, an enzyme
            of the anaerobic toluene catabolic pathway.
  JOURNAL   Arch. Microbiol. 178 (2002) 517-24.
  ORGANISM  Thauera aromatica
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
ORTHOLOGY   KO: K07545  (R)-benzylsuccinyl-CoA dehydro genase
GENES       BUR: Bcep18194_B0146
            EBA: c2A310(bbsG)
            FAL: FRAAL3561
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.21
            ExPASy - ENZYME nomenclature database: 1.3.99.21
            ExplorEnz - The Enzyme Database: 1.3.99.21
            ERGO genome analysis and discovery system: 1.3.99.21
            UM-BBD (Biocatalysis/Biodegradation Database): 1.3.99.21
            BRENDA, the Enzyme Database: 1.3.99.21
///
ENTRY       EC 1.3.99.22                Enzyme
NAME        coproporphyrinogen dehydrogenase;
            oxygen-independent coproporphyrinogen-III oxidase;
            HemN;
            radical SAM enzyme;
            coproporphyrinogen III oxidase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     coproporphyrinogen-III:S-adenosyl-L-methionine oxidoreductase
            (decarboxylating)
REACTION    coproporphyrinogen III + 2 S-adenosyl-L-methionine =
            protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
            [RN:R06895]
ALL_REAC    R06895
SUBSTRATE   coproporphyrinogen III [CPD:C03263];
            S-adenosyl-L-methionine [CPD:C00019]
PRODUCT     protoporphyrinogen IX [CPD:C01079];
            CO2 [CPD:C00011];
            L-methionine [CPD:C00073];
            5'-deoxyadenosine [CPD:C05198]
COMMENT     This enzyme differs from EC 1.3.3.3, coproporphyrinogen oxidase, by
            using S-adenosyl-L-methionine (AdoMet) instead of oxygen as oxidant.
            It occurs mainly in bacteria, whereas eukaryotes use the
            oxygen-dependent oxidase. The reaction starts by using an electron
            from the reduced form of the enzyme's [4Fe-4S] cluster to split
            AdoMet into methionine and the radical 5'-deoxyadenosin-5'-yl. This
            radical initiates attack on the 2-carboxyethyl groups, leading to
            their conversion into vinyl groups. This conversion, ---.CH-CH2-COO-
            -> ---CH=CH2 + CO2 + e- replaces the electron initially used.
REFERENCE   1  [PMID:12114526]
  AUTHORS   Layer G, Verfurth K, Mahlitz E, Jahn D.
  TITLE     Oxygen-independent coproporphyrinogen-III oxidase HemN from
            Escherichia coli.
  JOURNAL   J. Biol. Chem. 277 (2002) 34136-42.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:14633981]
  AUTHORS   Layer G, Moser J, Heinz DW, Jahn D, Schubert WD.
  TITLE     Crystal structure of coproporphyrinogen III oxidase reveals cofactor
            geometry of Radical SAM enzymes.
  JOURNAL   EMBO. J. 22 (2003) 6214-24.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K02495  oxygen-independent coproporphyrinogen III oxidase
GENES       ATH: AT5G63290
            OSA: 4351951
            CME: CMR445C
            DDI: DDBDRAFT_0205185
            TET: TTHERM_00112720
            ECO: b2955(yggW) b3867(hemN)
            ECJ: JW2922(yggW) JW3838(hemN)
            ECE: Z4300(yggW) Z4914(chuW) Z5403(hemN)
            ECS: ECs3831 ECs4383 ECs4789
            ECC: c3541(yggW) c4314(chuW) c4816(hemN)
            ECI: UTI89_C3344(yggW) UTI89_C4034(chuW) UTI89_C4456(hemN)
            ECP: ECP_2949 ECP_3601 ECP_4077
            ECV: APECO1_2595(hemN) APECO1_3566(yggW)
            ECW: EcE24377A_4386(hemN)
            ECX: EcHS_A4092(hemN)
            STY: STY3257 STY3877(hemN)
            STT: t3016 t3617(hemN)
            SPT: SPA2967(yggW) SPA3845(hemN)
            SEC: SC3044(yggW) SC3896(hemN)
            STM: STM3104(yggW) STM4004(hemN)
            YPE: YPO0021(hemN) YPO0286 YPO0946
            YPK: y0547 y3332 y3807(hemN)
            YPM: YP_0022(hemN1) YP_3496(hemN2)
            YPA: YPA_0319 YPA_3521 YPA_3995
            YPN: YPN_0248 YPN_3143 YPN_3380
            YPP: YPDSF_0569
            YPS: YPTB0021(hemN) YPTB0344 YPTB3218
            YPI: YpsIP31758_0024(hemN)
            SFL: SF2946(yggW) SF3937(hemN)
            SFX: S3150(yggW) S3809(hemN)
            SFV: SFV_3634(hemN)
            SSN: SSON_3109(yggW) SSON_4039(hemN)
            SBO: SBO_3035(yggW) SBO_3879(hemN)
            SDY: SDY_3117(yggW) SDY_3876(hemN)
            ECA: ECA0026(hemN) ECA3009 ECA3632
            PLU: plu0230(hemN) plu1176
            BUC: BU550(yggW)
            BAS: BUsg532(yggW)
            BAB: bbp498(yggW)
            BCC: BCc_361(yggW)
            SGL: SG2032
            ENT: Ent638_3361
            KPN: KPN_03389(yggW)
            SPE: Spro_4035 Spro_4884
            HIN: HI0463
            HIT: NTHI0594
            HDU: HD0037(chuW) HD1668
            HSO: HS_0124 HS_0472(hemN)
            PMU: PM1669 PM1833(hemN)
            MSU: MS0228(hemN) MS1746(hemN)
            APL: APL_0847 APL_0963(hemN) APL_1523(chuW)
            ASU: Asuc_0382 Asuc_1871
            XFA: XF1507
            XFT: PD0724(hemN)
            XCC: XCC2092 XCC3254
            XCB: XC_0963 XC_2090
            XCV: XCV3517
            XAC: XAC3400
            XOO: XOO1140
            XOM: XOO_1037(XOO1037)
            VCH: VC0116 VC0455 VCA0909
            VVU: VV1_0894 VV1_1519 VV2_1615
            VVY: VV0193 VV2880 VVA0425
            VPA: VP0115 VP2622 VPA0427(phuW)
            VFI: VF0080 VF0424 VF1226
            PPR: PBPRA2102 PBPRA3149 PBPRA3497
            PAE: PA0386 PA1546(hemN)
            PAU: PA14_05040 PA14_44470(hemN)
            PAP: PSPA7_3786(hemN)
            PPU: PP_4264(hemN) PP_5101
            PPF: Pput_1604 Pput_4974
            PST: PSPTO_1993(hemN) PSPTO_5052
            PSB: Psyr_0471 Psyr_3423(hemN)
            PSP: PSPPH_0462 PSPPH_3349(hemN)
            PFL: PFL_1912(hemN) PFL_5846
            PFO: Pfl_1813(hemN) Pfl_5327
            PEN: PSEEN0311 PSEEN1793(hemN)
            PMY: Pmen_2613 Pmen_4159
            PAR: Psyc_1224(hemN_rel)
            PCR: Pcryo_1168
            PRW: PsycPRwf_1655 PsycPRwf_2361
            ACI: ACIAD0432
            SON: SO_3359 SO_4730(hemN)
            SDN: Sden_2687 Sden_3626
            SFR: Sfri_0042 Sfri_2866
            SAZ: Sama_2483
            SBL: Sbal_3031
            SBM: Shew185_3046 Shew185_4118 Shew185_4351
            SLO: Shew_1131
            SPC: Sputcn32_2693
            SSE: Ssed_0090 Ssed_1226 Ssed_4414
            SPL: Spea_0096 Spea_1121 Spea_2394 Spea_3339 Spea_4126
            SHE: Shewmr4_1187 Shewmr4_3911
            SHM: Shewmr7_1258 Shewmr7_4003
            SHN: Shewana3_1188 Shewana3_4116
            SHW: Sputw3181_1318
            ILO: IL0190(hemN) IL1980
            CPS: CPS_3668 CPS_4823(hemN)
            PHA: PSHAa2609(yggW) PSHAa2749(hemN)
            PAT: Patl_1104 Patl_3288
            SDE: Sde_2483 Sde_3651
            PIN: Ping_3046
            CBU: CBU_0597
            LPN: lpg2354
            LPF: lpl2276(hemN)
            LPP: lpp2303(hemN)
            MCA: MCA0115(hemN) MCA3079
            FTU: FTT0084c(hemN)
            FTF: FTF0084c(hemN)
            FTW: FTW_0161
            FTL: FTL_1775
            FTH: FTH_1711(hemN)
            FTA: FTA_1882
            FTN: FTN_1626(hemN)
            TCX: Tcr_0117 Tcr_0501
            NOC: Noc_2444
            AEH: Mlg_1372 Mlg_2448
            HCH: HCH_02266(hemN2) HCH_06363
            CSA: Csal_3308
            MMW: Mmwyl1_2234 Mmwyl1_4335
            AHA: AHA_0272(hemN) AHA_0845
            DNO: DNO_0087(hemN-1) DNO_0131(hemN-2)
            BCI: BCI_0479
            VOK: COSY_0222(hemN)
            NME: NMB0379 NMB0665
            NMA: NMA0864 NMA2108(hemN)
            NGO: NGO0234 NGO1580(hemN)
            CVI: CV_0927 CV_3648(hemN)
            RSO: RSc2161(RS01441) RSc3284(hemN)
            REU: Reut_A2479 Reut_A3323(hemN)
            RME: Rmet_0850 Rmet_3474
            BMA: BMA0618(hemN-1) BMA2100 BMA2171(hemN-2)
            BUR: Bcep18194_A4018(hemN) Bcep18194_A4103
            BCN: Bcen_0435 Bcen_0516
            BCH: Bcen2424_0914 Bcen2424_0995
            BAM: Bamb_0791 Bamb_0855
            BPS: BPSL2366 BPSL2567 BPSL2646(hemN)
            BPM: BURPS1710b_2818(hemN) BURPS1710b_3053 BURPS1710b_3122(hemN)
            BTE: BTH_I1509(hemN-1) BTH_I1582 BTH_I1800(hemN-2) BTH_II0299
            PNU: Pnuc_1082
            BPE: BP1595
            BPA: BPP1960(hemN) BPP2989
            BBR: BB2147(hemN) BB2955
            RFR: Rfer_1631 Rfer_1938
            POL: Bpro_1208 Bpro_1341
            PNA: Pnap_0816
            MPT: Mpe_A2470 Mpe_A2703
            HAR: HEAR1650(hemNB) HEAR1651(hemNA)
            NEU: NE0278
            NET: Neut_0310
            NMU: Nmul_A0068
            EBA: c1A39(hemN) ebA5151(hemN)
            DAR: Daro_1048(hemN) Daro_3853
            TBD: Tbd_0479 Tbd_0635(hemN)
            MFA: Mfla_0040
            HPY: HP0665(hemN) HP1226(hemN)
            HPJ: jhp0610(hemN_1) jhp1147(hemN_2)
            HPA: HPAG1_0650 HPAG1_1168
            HHE: HH0615(hemN_2) HH0975(hemN_1)
            HAC: Hac_0850(hemN) Hac_1649(hemN)
            WSU: WS1722(hemN) WS1751(hemN)
            TDN: Tmden_0606
            CJE: Cj0992c(hemN)
            CJR: CJE1072(hemN)
            CJU: C8J_0929(hemN)
            CFF: CFF8240_1118 CFF8240_1571(hemN)
            CCV: CCV52592_0159(hemN) CCV52592_1573
            CHA: CHAB381_0997 CHAB381_1695(hemN)
            CCO: CCC13826_0887(hemN)
            ABU: Abu_1197(hemN1) Abu_1245(hemN2)
            NIS: NIS_0364(hemN) NIS_1142
            SUN: SUN_0454 SUN_2091(hemN)
            GSU: GSU0030
            GME: Gmet_3535
            GUR: Gura_0208
            PCA: Pcar_0110
            DVU: DVU3057
            DDE: Dde_0536
            LIP: LI0817(hemN)
            BBA: Bd3454(hemN) Bd3870(hemN)
            DPS: DP0716
            ADE: Adeh_1089
            AFW: Anae109_0263 Anae109_1129
            MXA: MXAN_1143
            SAT: SYN_02186
            SFU: Sfum_1360
            RPR: RP175(hemN)
            RTY: RT0166(hemN)
            RCO: RC0219(hemN)
            RFE: RF_1100(hemN)
            RBE: RBE_1145(hemN)
            MLO: mll5815 mll6408 mlr4627(hemN) mlr6390 mlr6633
            MES: Meso_4013 Meso_4298
            PLA: Plav_3582
            SME: SMa1266(hemN) SMc01147
            SMD: Smed_0007 Smed_6285
            ATU: Atu0325(hemN) Atu1601(hemN)
            ATC: AGR_C_2945 AGR_C_568(hemN)
            RET: RHE_CH00360(hemNch)
            RLE: RL0377(hemN) pRL90023(hemN)
            BME: BMEI1293 BMEI1771 BMEII0096
            BMF: BAB1_0176 BAB1_0675 BAB2_1161(hemN-2)
            BMS: BR0176 BR0655(hemN-1) BRA1199(hemN-2)
            BMB: BruAb1_0172 BruAb1_0672(hemN-1) BruAb2_1135(hemN-2)
            BOV: BOV_0648(hemN-2) BOV_A1101(hemN-1)
            OAN: Oant_0185 Oant_2633
            BJA: bll0672(hemN) bll2007(hemN1) bll7086(hemN)
            BRA: BRADO0175 BRADO1229(hemN)
            BBT: BBta_0184 BBta_6824(hemN)
            RPA: RPA0327(hemN2) RPA1666(hemN1) RPA2122
            RPB: RPB_0164 RPB_0423 RPB_3865
            RPC: RPC_0323 RPC_1971 RPC_3814
            RPD: RPD_0397 RPD_1485 RPD_2352
            RPE: RPE_0355 RPE_3151 RPE_3937
            NWI: Nwi_0191
            NHA: Nham_0149
            BHE: BH00530(hemN)
            BQU: BQ00470(hemN)
            XAU: Xaut_1747 Xaut_2537
            CCR: CC_0145 CC_1411
            SIL: SPO0006 SPO3532(hemN)
            SIT: TM1040_2548 TM1040_2870
            RSP: RSP_0317(hemN) RSP_0699(hemZ) RSP_1224(hemN)
            RSQ: Rsph17025_0531 Rsph17025_0977 Rsph17025_2661
            JAN: Jann_0204 Jann_3244 Jann_3859
            RDE: RD1_0428(hemN) RD1_1267(hemN) RD1_1696(hemN)
            MMR: Mmar10_2643 Mmar10_3011
            HNE: HNE_0554(hemN) HNE_3309
            ZMO: ZMO0012(hemN) ZMO1364(hemN)
            NAR: Saro_2063 Saro_2569
            SAL: Sala_0258 Sala_1668
            SWI: Swit_0569
            ELI: ELI_06000
            GOX: GOX1594
            GBE: GbCGDNIH1_0028
            ACR: Acry_1560 Acry_1693
            RRU: Rru_A2504 Rru_A3639
            MAG: amb2698 amb4500
            MGM: Mmc1_0026 Mmc1_0052
            ABA: Acid345_2366
            BSU: BG11395(hemN) BG12999(hemZ)
            BHA: BH1152 BH1343(hemN)
            BAN: BA0875 BA4542(hemN)
            BAR: GBAA0875 GBAA4542(hemN)
            BAA: BA_1457 BA_4989
            BAT: BAS0831 BAS4216
            BCE: BC0889 BC4315
            BCA: BCE_0964 BCE_4398(hemN)
            BCZ: BCZK0778(hemN) BCZK4064(hemN)
            BCY: Bcer98_0706 Bcer98_3043
            BTK: BT9727_0777(hemN) BT9727_4054(hemN)
            BLI: BL02093(hemN) BL02869(hemZ)
            BLD: BLi02742(hemN)
            BCL: ABC0501 ABC1656(hemN)
            BPU: BPUM_2283(hemN)
            OIH: OB1971(hemN)
            GKA: GK2507
            SAU: SA1412(hemN)
            SAV: SAV1583(hemN)
            SAM: MW1535(hemN)
            SAR: SAR1660
            SAS: SAS1521
            SAC: SACOL1640
            SAB: SAB1455c
            SAA: SAUSA300_1543
            SAO: SAOUHSC_01686
            SAJ: SaurJH9_1641
            SAH: SaurJH1_1675
            SEP: SE1270
            SER: SERP1151
            SHA: SH1333(hemN)
            SSP: SSP1174
            LMO: lmo1476(hemN)
            LMF: LMOf2365_1495
            LIN: lin1513(hemN)
            LWE: lwe1491(hemN)
            LLA: L0193(hemN)
            LLC: LACR_1249
            SPY: SPy_1040(hemN)
            SPZ: M5005_Spy_0765(hemN)
            SPM: spyM18_1022(hemN)
            SPG: SpyM3_0673(hemN)
            SPS: SPs1180
            SPI: MGAS10750_Spy0917(hemN)
            SPJ: MGAS2096_Spy0839(hemN)
            SPK: MGAS9429_Spy0880(hemN)
            SPA: M6_Spy0790
            SPB: M28_Spy0744(hemN)
            SPN: SP_1409
            SPR: spr1266(hemN)
            SPD: SPD_1240
            SAG: SAG0890
            SAN: gbs0907
            SAK: SAK_1013
            SMU: SMU.1418(hemN)
            STC: str1236(hemN)
            STL: stu1236(hemN)
            SSA: SSA_1075(hemN)
            LSA: LSA1240
            LCA: LSEI_1568
            EFA: EF1305
            STH: STH2425 STH483
            CAC: CAC1279(hemN) CAC2271
            CPE: CPE1935(hemZ) CPE2036(hemN)
            CPF: CPF_2293
            CPR: CPR_2008
            CTC: CTC02034 CTC02195
            CNO: NT01CX_0060 NT01CX_1847
            CBO: CBO2962(hemN)
            CBA: CLB_2926
            CBH: CLC_2858
            CBF: CLI_3015
            CBE: Cbei_0827 Cbei_1543
            AMT: Amet_2357 Amet_3051
            CHY: CHY_0411
            DSY: DSY3136
            SWO: Swol_1582
            CSC: Csac_1004 Csac_1749
            TTE: TTE0952(hemN)
            MTA: Moth_0582
            MPE: MYPE5010(hemN)
            MGA: MGA_0916(hemN)
            UUR: UU274(hemN)
            MTU: Rv2388c(hemN)
            MTC: MT2457
            MBO: Mb2409c(hemN)
            MPA: MAP2207c(hemN)
            MAV: MAV_1789
            MSM: MSMEG_4525
            MMC: Mmcs_3473
            CGL: NCgl2212(cgl2292)
            CGB: cg2517(hemN)
            CEF: CE2191
            CDI: DIP1722(hemN)
            CJK: jk0599(hemN)
            NFA: nfa14210
            RHA: RHA1_ro01249
            SCO: SCO2559(SCC77.26c)
            SMA: SAV5566(hemN)
            LXX: Lxx14670(hemN)
            PAC: PPA0911
            TFU: Tfu_0835
            FRA: Francci3_1263
            FAL: FRAAL2005
            ACE: Acel_0781
            KRA: Krad_3411
            SEN: SACE_1477
            STP: Strop_3458
            BLO: BL0847(hemN)
            BAD: BAD_0747(hemN)
            FNU: FN0560 FN1612
            RBA: RB6485(hemN) RB9876(hemN)
            CTR: CT052(hemN_1) CT746(hemN_2)
            CTA: CTA_0056(hemN_1) CTA_0812(hemN_2)
            CMU: TC0122 TC0322
            CPN: CPn0380(hemN_1) CPn0889(hemN_2)
            CPA: CP0376 CP0977
            CPJ: CPj0380(hemN_1) CPj0889(hemN_2)
            CPT: CpB0392 CpB0920
            CCA: CCA00418 CCA00879(hemN)
            CAB: CAB404 CAB845
            CFE: CF0137(hemN1) CF0589(hemN2)
            PCU: pc1096(hemN)
            SYN: sll1876(hemN1) sll1917(hemN2)
            SYW: SYNW1646(hemN)
            SYC: syc1723_d(hemN)
            SYF: Synpcc7942_2382
            SYD: Syncc9605_0843
            SYE: Syncc9902_1546
            SYG: sync_0729
            SYR: SynRCC307_0598(hemN)
            SYX: SynWH7803_1761(hemN)
            CYA: CYA_0785
            CYB: CYB_0890
            TEL: tll1192(hemN2) tll1720(hemN1)
            GVI: gll3085(hemN)
            ANA: all4956(hemN) alr3126
            AVA: Ava_2223 Ava_3828 Ava_4393
            PMA: Pro1385(hemN)
            PMM: PMM1311
            PMT: PMT0317
            PMN: PMN2A_0877
            PMB: A9601_15101(hemN)
            PMC: P9515_14721(hemN)
            PMF: P9303_19991(hemN)
            PMG: P9301_14971(hemN)
            PME: NATL1_17311(hemN)
            TER: Tery_1194
            BTH: BT_2168
            BFR: BF1914 BF3869
            BFS: BF1984(hemN) BF3638
            PGI: PG0475
            SRU: SRU_0746(hemN) SRU_1392
            CHU: CHU_0165(hemN)
            FJO: Fjoh_1376 Fjoh_2542
            CTE: CT0372(hemN) CT2010
            CCH: Cag_0285 Cag_1806
            PLT: Plut_0222 Plut_1579
            DET: DET0858
            DEH: cbdb_A840
            DEB: DehaBAV1_0776
            RRS: RoseRS_3875
            RCA: Rcas_3306
            DRA: DR_0130
            DGE: Dgeo_2324
            TTH: TTC0123
            TTJ: TTHA0497
            AAE: aq_1424(hemF) aq_2124(hemN)
            TMA: TM1166
            TPT: Tpet_1583
            TME: Tmel_0944
            FNO: Fnod_1224
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.22
            ExPASy - ENZYME nomenclature database: 1.3.99.22
            ExplorEnz - The Enzyme Database: 1.3.99.22
            ERGO genome analysis and discovery system: 1.3.99.22
            BRENDA, the Enzyme Database: 1.3.99.22
///
ENTRY       EC 1.3.99.23                Enzyme
NAME        all-trans-retinol 13,14-reductase;
            retinol saturase;
            RetSat;
            (13,14)-all-trans-retinol saturase;
            all-trans-retinol:all-trans-13,14-dihydroretinol saturase
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
SYSNAME     all-trans-13,14-dihydroretinol:acceptor 13,14-oxidoreductase
REACTION    all-trans-13,14-dihydroretinol + acceptor = all-trans-retinol +
            reduced acceptor [RN:R07163]
ALL_REAC    R07163
SUBSTRATE   all-trans-13,14-dihydroretinol [CPD:C15492];
            acceptor [CPD:C00028]
PRODUCT     all-trans-retinol [CPD:C00473];
            reduced acceptor [CPD:C00030]
COMMENT     The reaction is only known to occur in the opposite direction to
            that given above, with the enzyme being specific for
            all-trans-retinol as substrate. Neither all-trans-retinoic acid nor
            9-cis, 11-cis or 13-cis-retinol isomers are substrates. May play a
            role in the metabolism of vitamin A.
REFERENCE   1  [PMID:15358783]
  AUTHORS   Moise AR, Kuksa V, Imanishi Y, Palczewski K.
  TITLE     Identification of all-trans-retinol:all-trans-13,14-dihydroretinol
            saturase.
  JOURNAL   J. Biol. Chem. 279 (2004) 50230-42.
  ORGANISM  mouse [GN:mmu]
ORTHOLOGY   KO: K09516  all-trans-retinol 13,14-reductase
GENES       HSA: 54884(RETSAT)
            PTR: 470420(RETSAT)
            MMU: 67442(Retsat)
            RNO: 246298(Retsat)
            DRE: 325922(retsat)
            SPU: 581285(LOC581285)
            FJO: Fjoh_1077
DBLINKS     IUBMB Enzyme Nomenclature: 1.3.99.23
            ExPASy - ENZYME nomenclature database: 1.3.99.23
            ExplorEnz - The Enzyme Database: 1.3.99.23
            ERGO genome analysis and discovery system: 1.3.99.23
            BRENDA, the Enzyme Database: 1.3.99.23
            CAS: 418767-56-3
///
ENTRY       EC 1.3.99.-                 Enzyme
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors;
            With other acceptors
REACTION    (1) Butanoyl-CoA + FAD <=> FADH2 + Crotonoyl-CoA [RN:R01175];
            (2) Palmitoyl-CoA + FAD <=> trans-Hexadec-2-enoyl-CoA + FADH2
            [RN:R01279];
            (3) Sphinganine + FAD <=> FADH2 + Sphingosine [RN:R02979];
            (4) Octanoyl-CoA + FAD <=> trans-Oct-2-enoyl-CoA + FADH2
            [RN:R03777];
            (5) Lauroyl-CoA + FAD <=> 2-trans-Dodecenoyl-CoA + FADH2
            [RN:R03857];
            (6) Tetradecanoyl-CoA + FAD <=> trans-Tetradec-2-enoyl-CoA + FADH2
            [RN:R03990];
            (7) 3alpha,7alpha-Dihydroxy-5beta-cholestanoyl-CoA + FAD <=>
            3alpha,7alpha-Dihydroxy-5beta-cholest-24-enoyl-CoA + FADH2
            [RN:R04547];
            (8) 3alpha,7alpha,12alpha-Trihydroxy-5beta-cholestanoyl-CoA + FAD
            <=> 3alpha,7alpha,12alpha-Trihydroxy-5beta-cholest-24-enoyl-CoA +
            FADH2 [RN:R04592];
            (9) Hexanoyl-CoA + FAD <=> trans-Hex-2-enoyl-CoA + FADH2
            [RN:R04751];
            (10) Decanoyl-CoA + FAD <=> trans-Dec-2-enoyl-CoA + FADH2
            [RN:R04754];
            (11) Naphthyl-2-methyl-succinyl-CoA <=>
            Naphthyl-2-methylene-succinyl-CoA + 2 H+ [RN:R06905];
            (12) Adipyl-CoA + FAD <=> 5-Carboxy-2-pentenoyl-CoA + FADH2
            [RN:R06943];
            (13) Campest-4-en-3-one + NADPH <=> 5alpha-Campestan-3-one + NADP+
            [RN:R07429];
            (14) 22alpha-Hydroxy-campest-4-en-3-one + NADPH <=>
            22alpha-Hydroxy-5alpha-campestan-3-one + NADP+ [RN:R07447]
SUBSTRATE   Butanoyl-CoA [CPD:C00136];
            FAD [CPD:C00016];
            Palmitoyl-CoA [CPD:C00154];
            Sphinganine [CPD:C00836];
            Octanoyl-CoA [CPD:C01944];
            Lauroyl-CoA [CPD:C01832];
            Tetradecanoyl-CoA [CPD:C02593];
            3alpha,7alpha-Dihydroxy-5beta-cholestanoyl-CoA [CPD:C04644];
            3alpha,7alpha,12alpha-Trihydroxy-5beta-cholestanoyl-CoA
            [CPD:C04760];
            Hexanoyl-CoA [CPD:C05270];
            Decanoyl-CoA [CPD:C05274];
            Phytoene [CPD:C05413];
            Phytofluene [CPD:C05414];
            Naphthyl-2-methyl-succinyl-CoA [CPD:C14116];
            Adipyl-CoA [CPD:C14143]
PRODUCT     FADH2 [CPD:C01352];
            Crotonoyl-CoA [CPD:C00877];
            trans-Hexadec-2-enoyl-CoA [CPD:C05272];
            Sphingosine [CPD:C00319];
            trans-Oct-2-enoyl-CoA [CPD:C05276];
            2-trans-Dodecenoyl-CoA [CPD:C03221];
            trans-Tetradec-2-enoyl-CoA [CPD:C05273];
            3alpha,7alpha-Dihydroxy-5beta-cholest-24-enoyl-CoA [CPD:C05447];
            3alpha,7alpha,12alpha-Trihydroxy-5beta-cholest-24-enoyl-CoA
            [CPD:C05460];
            trans-Hex-2-enoyl-CoA [CPD:C05271];
            trans-Dec-2-enoyl-CoA [CPD:C05275];
            Phytofluene [CPD:C05414];
            Hydrogen [CPD:C00282];
            zeta-Carotene [CPD:C05430];
            Naphthyl-2-methylene-succinyl-CoA [CPD:C14117];
            H+ [CPD:C00080];
            5-Carboxy-2-pentenoyl-CoA [CPD:C14144]
///
ENTRY       EC 1.3.-.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on the CH-CH group of donors
REACTION    (1) 1-Chloro-2,2-bis(4'-chlorophenyl)ethylene + 2 H+ + 2 e- <=>
            1-Chloro-2,2-bis(4'-chlorophenyl)ethane [RN:R05398];
            (2) Cyclohexane-1-carboxyl-CoA + Acceptor <=>
            Cyclohex-1-ene-1-carboxyl-CoA + Reduced acceptor [RN:R05619];
            (3) (+)-(S)-Carvone + H+ <=> (1R,4S)-Iso-dihydrocarvone [RN:R06372];
            (4) (-)-Carvone + Reduced acceptor <=> (1R,4R)-Dihydrocarvone +
            Acceptor [RN:R06373];
            (5) 1-Hydro-1,1a-dihydroxy-9-fluorenone + H2O <=>
            2,3-Dihydroxy-2'-carboxybiphenyl + 2 H+ [RN:R07800]
SUBSTRATE   1-Chloro-2,2-bis(4'-chlorophenyl)ethylene [CPD:C06637];
            H+ [CPD:C00080];
            e- [CPD:C05359];
            Cyclohexane-1-carboxyl-CoA [CPD:C09823];
            Acceptor [CPD:C00028];
            (+)-(S)-Carvone [CPD:C11383];
            (-)-Carvone [CPD:C01767];
            Reduced acceptor [CPD:C00030]
PRODUCT     1-Chloro-2,2-bis(4'-chlorophenyl)ethane [CPD:C06638];
            Cyclohex-1-ene-1-carboxyl-CoA [CPD:C09811];
            Reduced acceptor [CPD:C00030];
            (1R,4S)-Iso-dihydrocarvone [CPD:C11412];
            (1R,4R)-Dihydrocarvone [CPD:C11398];
            Acceptor [CPD:C00028]
///
ENTRY       EC 1.4.1.1                  Enzyme
NAME        alanine dehydrogenase;
            AlaDH;
            L-alanine dehydrogenase;
            NAD+-linked alanine dehydrogenase;
            alpha-alanine dehydrogenase;
            NAD+-dependent alanine dehydrogenase;
            alanine oxidoreductase;
            NADH-dependent alanine dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-alanine:NAD+ oxidoreductase (deaminating)
REACTION    L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH + H+ [RN:R00396]
ALL_REAC    R00396;
            (other) R00145 R00146
SUBSTRATE   L-alanine [CPD:C00041];
            H2O [CPD:C00001];
            NAD+ [CPD:C00003]
PRODUCT     pyruvate [CPD:C00022];
            NH3 [CPD:C00014];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   O'Connor, R.J. and Halvorson, H.
  TITLE     The substrate specificity of L-alanine dehydrogenase.
  JOURNAL   Biochim. Biophys. Acta 48 (1961) 47-55.
  ORGANISM  Bacillus subtilis [GN:bsu], Bacillus cereus
REFERENCE   2
  AUTHORS   Pierard, A. and Wiame, J.M.
  TITLE     Proprietes de la L(+)-alanine-deshydrogenase.
  JOURNAL   Biochim. Biophys. Acta 37 (1960) 490-502.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   3
  AUTHORS   Yoshida, A. and Freese, E.
  TITLE     Enzymic properties of alanine dehydrogenase of Bacillus subtilis.
  JOURNAL   Biochim. Biophys. Acta 96 (1965) 248-262.
  ORGANISM  Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00430  Taurine and hypotaurine metabolism
            PATH: map00720  Reductive carboxylate cycle (CO2 fixation)
ORTHOLOGY   KO: K00259  alanine dehydrogenase
GENES       VCH: VC1905
            VCO: VC0395_A1495(ald)
            VVU: VV1_2952
            VVY: VV1320
            VPA: VP1103
            VFI: VF0903
            PPR: PBPRA1160 PBPRA2201
            SDN: Sden_1741
            SFR: Sfri_1793
            SHE: Shewmr4_1961
            SHM: Shewmr7_2015
            SHN: Shewana3_2048
            ILO: IL0669(pntA)
            CPS: CPS_2761(ald)
            PHA: PSHAa1718
            PAT: Patl_2462
            CBU: CBU_1116(ald)
            CBD: COXBU7E912_1216(ald)
            LPN: lpg0924(ald)
            LPF: lpl0955(ald)
            LPP: lpp0986(ald)
            MCA: MCA0563(ald)
            NOC: Noc_0346
            HCH: HCH_00974(ald)
            CSA: Csal_2966
            AHA: AHA_0248(ald)
            CVI: CV_2022(ald)
            REU: Reut_A1168 Reut_B5878
            REH: H16_A2009(ald)
            BUR: Bcep18194_B1797
            BCN: Bcen_4146
            BCH: Bcen2424_4220
            BPS: BPSS1090(ald)
            BPM: BURPS1710b_A0039(ald)
            BPL: BURPS1106A_A1449(ald)
            BPD: BURPS668_A1536(ald)
            BTE: BTH_II0922(ald)
            RFR: Rfer_4054
            POL: Bpro_3222
            NEU: NE0022
            NET: Neut_0212
            NMU: Nmul_A1155
            EBA: ebA3623(ald)
            DAR: Daro_2145
            TBD: Tbd_0644
            HPY: HP1398(ald)
            HPA: HPAG1_1472
            HAC: Hac_1765(ald)
            GSU: GSU2292(ald)
            GME: Gmet_1099
            PCA: Pcar_0416
            DVU: DVU0571(ald)
            DDE: Dde_1553
            BBA: Bd2478(alaDH)
            DPS: DP0540 DP0544
            ADE: Adeh_2109
            MXA: MXAN_4146(ald)
            SAT: SYN_00979
            SFU: Sfum_3106
            PUB: SAR11_0809(ald)
            MLO: mll0362 mll9089
            MES: Meso_1428
            SME: SMc01169(ald)
            RET: RHE_CH01770(aldA)
            RLE: RL1966(ald)
            BJA: blr1738(aldA) blr3179
            CCR: CC_3574
            SIL: SPO0222(ald)
            SIT: TM1040_3628
            RSP: RSP_0723(ald)
            JAN: Jann_0458
            RDE: RD1_1033(ald)
            MMR: Mmar10_1058
            HNE: HNE_0971(ald)
            NAR: Saro_1682
            SAL: Sala_0558
            ELI: ELI_11875
            RRU: Rru_A3686
            MAG: amb4487
            MGM: Mmc1_0055
            SUS: Acid_5426
            BSU: BG10468(ald)
            BHA: BH2329(ald) BH3180
            BAN: BA0592(ald-1) BA4873(ald-2)
            BAR: GBAA0592(ald-1) GBAA4873(ald-2)
            BAA: BA_1174 BA_5294
            BAT: BAS0561 BAS4521
            BCE: BC0592 BC4623
            BCA: BCE_0659(ald) BCE_4758(ald)
            BCZ: BCZK0505(ald) BCZK4368(ald)
            BCY: Bcer98_0509 Bcer98_3299
            BTK: BT9727_0503(ald) BT9727_4357(ald)
            BTL: BALH_0532(ald) BALH_4204(ald)
            BLI: BL00190(aldA) BL03009(ald)
            BLD: BLi03382(ald) BLi04275
            BCL: ABC0767(ald)
            BAY: RBAM_028980
            BPU: BPUM_2862
            OIH: OB2188 OB3225
            GKA: GK2752 GK3448
            GTN: GTNG_2677
            SAU: SA1272 SA1531(ald)
            SAV: SAV1439 SAV1709(ald)
            SAM: MW1328 MW1652(ald)
            SAR: SAR1451(ald2) SAR1787(ald1)
            SAS: SAS1382 SAS1636
            SAC: SACOL1478(ald1) SACOL1758(ald2)
            SAB: SAB1304c(ald) SAB1568c(ald)
            SAA: SAUSA300_1331(ald) SAUSA300_1655(ald)
            SAO: SAOUHSC_01452 SAOUHSC_01818
            SAJ: SaurJH9_1765
            SAH: SaurJH1_1800
            SEP: SE1384
            SER: SERP1272(ald)
            SHA: SH1216(ald)
            SSP: SSP1057
            LMO: lmo1579
            LMF: LMOf2365_1601(ald)
            LIN: lin1614
            LWE: lwe1592(ald)
            LLM: llmg_1237(ceo)
            SPR: spr0852 spr0853 spr0854
            STC: str0555 str0556
            STL: stu0555 stu0556
            SSA: SSA_1615
            SGO: SGO_0708(ald)
            LSL: LSL_1768(ald)
            LBR: LVIS_1053
            LCA: LSEI_2182
            STH: STH1822
            CKL: CKL_0660(ald)
            CHY: CHY_0666(ald)
            DSY: DSY0985
            TTE: TTE0161(ald)
            MMY: MSC_0064(ald)
            MMO: MMOB1000(ald)
            MTU: Rv2780(ald)
            MTC: MT2850(ald)
            MBO: Mb2802(aldA) Mb2803(aldB)
            MBB: BCG_2797(ald_a) BCG_2798(aldB)
            MLE: ML1532(ald)
            MPA: MAP2888(ald)
            MAV: MAV_3674(ald)
            MSM: MSMEG_2659(ald)
            MVA: Mvan_2355
            MGI: Mflv_4017
            MMC: Mmcs_2104
            NFA: nfa16250
            RHA: RHA1_ro03547(ald1) RHA1_ro04466(ald2)
            SCO: SCO1773(SCI51.13c)
            SMA: SAV6507(ald)
            LXX: Lxx12100(ald)
            CMI: CMM_2898(aldA)
            ART: Arth_1744 Arth_4012
            AAU: AAur_3870(ald) AAur_pTC10072(ald) AAur_pTC20204(ald)
            PAC: PPA2268 PPA2274
            TFU: Tfu_0961
            KRA: Krad_4085
            SEN: SACE_6380(ald)
            STP: Strop_1923
            RXY: Rxyl_2908
            RBA: RB1363(ald)
            PCU: pc1486(ald)
            SYN: sll1682
            SYW: SYNW0501(ald)
            SYC: syc2332_c(ald)
            SYF: Synpcc7942_1760
            SYD: Syncc9605_2181
            SYG: sync_2295(ald)
            SYR: SynRCC307_1871(ald)
            SYX: SynWH7803_2010(ald)
            CYA: CYA_1112(ald)
            CYB: CYB_1358(ald)
            TEL: tlr2107
            GVI: glr3969
            ANA: alr2355
            AVA: Ava_0176
            PMA: Pro1600(ald)
            PMT: PMT1462(ald)
            PMF: P9303_04881(ald)
            TER: Tery_3174
            BTH: BT_1554
            BFR: BF1475
            BFS: BF1406(ald)
            SRU: SRU_0902(ald)
            CHU: CHU_1995(alaDH) CHU_2439(pntA)
            GFO: GFO_1781(ald)
            FJO: Fjoh_0022 Fjoh_4205
            FPS: FP1068(ald)
            CTE: CT0650 CT0706(ald)
            CCH: Cag_1878
            CPH: Cpha266_0906
            PLT: Plut_0627 Plut_0663
            DRA: DR_1895
            DGE: Dgeo_0771
            TTH: TTC1082 TTC1770
            TTJ: TTHA0216 TTHA1447
            MMP: MMP1513(ald)
STRUCTURES  PDB: 1OMO  1PJB  1PJC  1SAY  1VLL  2EEZ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.1
            ExPASy - ENZYME nomenclature database: 1.4.1.1
            ExplorEnz - The Enzyme Database: 1.4.1.1
            ERGO genome analysis and discovery system: 1.4.1.1
            BRENDA, the Enzyme Database: 1.4.1.1
            CAS: 9029-06-5
///
ENTRY       EC 1.4.1.2                  Enzyme
NAME        glutamate dehydrogenase;
            glutamic dehydrogenase;
            glutamate dehydrogenase (NAD+);
            glutamate oxidoreductase;
            glutamic acid dehydrogenase;
            L-glutamate dehydrogenase;
            NAD+-dependent glutamate dehydrogenase;
            NAD+-dependent glutamic dehydrogenase;
            NAD+-glutamate dehydrogenase;
            NAD+-linked glutamate dehydrogenase;
            NAD+-linked glutamic dehydrogenase;
            NAD+-specific glutamic dehydrogenase;
            NAD+-specific glutamate dehydrogenase;
            NAD+:glutamate oxidoreductase;
            NADH-linked glutamate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-glutamate:NAD+ oxidoreductase (deaminating)
REACTION    L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+
            [RN:R00243]
ALL_REAC    R00243;
            (other) R00145 R00146
SUBSTRATE   L-glutamate [CPD:C00025];
            H2O [CPD:C00001];
            NAD+ [CPD:C00003]
PRODUCT     2-oxoglutarate [CPD:C00026];
            NH3 [CPD:C00014];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Frieden, C.
  TITLE     L-Glutamate dehydrogenase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 3-24.
REFERENCE   2  [PMID:13140081]
  AUTHORS   NISMAN B.
  TITLE     The Stickland reaction.
  JOURNAL   Bacteriol. Rev. 18 (1954) 16-42.
  ORGANISM  Clostridium sporogenes, Clostridium saccharobutyricum
REFERENCE   3  [PMID:4324282]
  AUTHORS   Pahlich E, Joy KW.
  TITLE     Glutamate dehydrogenase from pea roots: purification and properties
            of the enzyme.
  JOURNAL   Can. J. Biochem. 49 (1971) 127-38.
  ORGANISM  Pisum sativum
REFERENCE   4
  AUTHORS   Smith, E.L., Austen, B.M., Blumenthal, K.M. and Nyc, J.F.
  TITLE     Glutamate dehydrogenases.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 11, Academic
            Press, New York, 1975, p. 293-367.
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00260  glutamate dehydrogenase
GENES       SCE: YDL215C(GDH2)
            AGO: AGOS_AGL040C
            PIC: PICST_78004(GDH2)
            CGR: CAGL0G05698g
            SPO: SPCC132.04c
            ANI: AN7451.2
            AFM: AFUA_2G06000
            AOR: AO090001000717
            CNE: CND00180
            UMA: UM05984.1
            DDI: DDBDRAFT_0206512
            PFA: PF08_0132
            TAN: TA11105
            TPV: TP04_0883
            TBR: Tb09.160.4310
            LMA: LmjF15.1010
            XFA: XF2091
            XFT: PD0785(gdhA)
            XCC: XCC2365
            XCB: XC_1751
            XCV: XCV2674
            XAC: XAC2496
            XOO: XOO2802
            XOM: XOO_2642(XOO2642)
            PSP: PSPPH_3560
            PEN: PSEEN1740(gdhB)
            PAR: Psyc_1062(gdhA2)
            PHA: PSHAa1670
            MCA: MCA1030(gluD)
            ABO: ABO_1595
            NME: NMB1476
            NMA: NMA1687
            NMC: NMC1413
            CVI: CV_3084(gdhA)
            REH: H16_A1356(gudB)
            BBA: Bd0717
            ECN: Ecaj_0306
            RET: RHE_CH04105
            RLE: RL4720(gdhB)
            BME: BMEI0231
            BMF: BAB1_1827
            BSU: BG10621(rocG) BG11435(ypcA)
            BHA: BH1622 BH2718 BH3942
            BAN: BA1511(gdhA)
            BAR: GBAA1511(gdhA)
            BAA: BA_2033
            BAT: BAS1401
            BCE: BC1491
            BLI: BL02226(gudB)
            BLD: BLi02435(gudB)
            BCL: ABC1862(gudB)
            BAY: RBAM_021110(gudB)
            BPU: BPUM_2029(gudB)
            OIH: OB1810(gudB)
            GKA: GK0189 GK2235
            SAU: SA0819(gudB)
            SAV: SAV0958(gudB)
            SAM: MW0840(gudB)
            SAR: SAR0920
            SAS: SAS0828
            SAC: SACOL0961(gluD)
            SAB: SAB0825
            SAA: SAUSA300_0861(gudB)
            SAO: SAOUHSC_00895
            SEP: SE0654
            SER: SERP0546(gluD)
            STH: STH1196
            CTC: CTC01295
            CDF: CD0179(gluD)
            CBO: CBO1811(gluD)
            CBA: CLB_1746(gluD)
            CBH: CLC_1753(gluD)
            CBF: CLI_1806(gluD)
            TTE: TTE1205(gdhA) TTE1344(gdhA2)
            MTU: Rv2476c(gdh)
            MBO: Mb2503c(gdh)
            MBB: BCG_2496c(gdh)
            MSM: MSMEG_4699
            FAL: FRAAL0156
            SEN: SACE_1325(gudB) SACE_4093(gudB)
            FNU: FN0488
            BFS: BF3409(gdhB2) BF3437(gdhB)
            HMA: rrnAC0884
            NPH: NP6184A(gdhA_3)
STRUCTURES  PDB: 1AUP  1BGV  1EUZ  1HRD  1K89  1V9L  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.2
            ExPASy - ENZYME nomenclature database: 1.4.1.2
            ExplorEnz - The Enzyme Database: 1.4.1.2
            ERGO genome analysis and discovery system: 1.4.1.2
            BRENDA, the Enzyme Database: 1.4.1.2
            CAS: 9001-46-1
///
ENTRY       EC 1.4.1.3                  Enzyme
NAME        glutamate dehydrogenase [NAD(P)+];
            glutamic dehydrogenase;
            glutamate dehydrogenase [NAD(P)+]
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-glutamate:NAD(P)+ oxidoreductase (deaminating)
REACTION    L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H + H+
            [RN:R00243 R00248]
ALL_REAC    R00243 R00248;
            (other) R00145 R00146
SUBSTRATE   L-glutamate [CPD:C00025];
            H2O [CPD:C00001];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     2-oxoglutarate [CPD:C00026];
            NH3 [CPD:C00014];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:12981035]
  AUTHORS   OLSON JA, ANFINSEN CB.
  TITLE     The crystallization and characterization of L-glutamic acid
            dehydrogenase.
  JOURNAL   J. Biol. Chem. 197 (1952) 67-79.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   Smith, E.L., Austen, B.M., Blumenthal, K.M. and Nyc, J.F.
  TITLE     Glutamate dehydrogenases.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 11, Academic
            Press, New York, 1975, p. 293-367.
REFERENCE   3
  AUTHORS   Strecker, H.J.
  TITLE     Glutamic dehydrogenase.
  JOURNAL   Arch. Biochem. Biophys. 46 (1953) 128-140.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00330  Arginine and proline metabolism
            PATH: map00471  D-Glutamine and D-glutamate metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00261  glutamate dehydrogenase (NAD(P)+)
GENES       HSA: 2746(GLUD1) 2747(GLUD2)
            MMU: 14661(Glud1)
            RNO: 24399(Glud1)
            CFA: 483859(GLUD1)
            BTA: 281785(GLUD1)
            GGA: 423612(GLUD1)
            XLA: 446858(glud1)
            XTR: 496554(glud1)
            DRE: 317737(glud1a)
            SPU: 584300(LOC584300)
            DME: Dmel_CG5320(Gdh)
            CEL: ZK829.4
            ATH: AT3G03910 AT5G07440(GDH2) AT5G18170(GDH1)
            OSA: 4330164 4334405 4336554
            CME: CML049C
            TET: TTHERM_00787250 TTHERM_01048110 TTHERM_01049200
            ECI: UTI89_C1957(gdhA)
            STY: STY1922(gdhA)
            STT: t1082(gdhA)
            SEC: SC1788(gdh)
            STM: STM1795
            SGL: SG0175
            ACI: ACIAD2680(gdh)
            TCX: Tcr_1836
            NOC: Noc_2054
            RSO: RSc0480(gdhA)
            REU: Reut_A0456
            REH: H16_A0471(gdhA1)
            RME: Rmet_0398
            BMA: BMA2439(gdhA)
            BMV: BMASAVP1_A0353(gdhA)
            BML: BMA10299_A1212(gdhA)
            BMN: BMA10247_2623(gdhA)
            BXE: Bxe_A0596
            BUR: Bcep18194_A3754
            BCN: Bcen_0185
            BAM: Bamb_0563
            BPS: BPSL2925
            BPM: BURPS1710b_3435(gdhA)
            BTE: BTH_I1224
            BPE: BP1857(gdhA)
            BPA: BPP1568(gdhA)
            BBR: BB2646(gdhA)
            POL: Bpro_3239
            MPT: Mpe_A3745
            MMS: mma_0278(gdhA1)
            DAR: Daro_2721
            CCV: CCV52592_0886
            CHA: CHAB381_0345
            PCA: Pcar_1237
            DPS: DP1198
            ADE: Adeh_1766
            MXA: MXAN_5873(gdhA)
            SAT: SYN_01242 SYN_02382
            SFU: Sfum_3244 Sfum_3265
            PUB: SAR11_1187(gdhA)
            RLE: pRL100054
            BRA: BRADO2494(gdh)
            BBT: BBta_2839(gdh)
            NWI: Nwi_2286
            NHA: Nham_2702
            SIL: SPO1743
            SIT: TM1040_2150
            RSP: RSP_0398
            JAN: Jann_3440
            RDE: RD1_1787(gilL)
            ABA: Acid345_4115
            BHA: BH0824
            BCA: BCE_1617(gdhA)
            SSP: SSP1817
            SSA: SSA_0371(gdhA)
            LPL: lp_1169(gdh)
            SWO: Swol_2170
            CEF: CE1577
            RHA: RHA1_ro00339(gdhA1) RHA1_ro00573(dghA) RHA1_ro03043(gdhA2)
                 RHA1_ro03288 RHA1_ro08786(gdhA3)
            SMA: SAV1636(rocG)
            FRA: Francci3_4390
            FAL: FRAAL6693(gdhA)
            SEN: SACE_3873(dghA) SACE_3882(gdhA1)
            RBA: RB6930(gdhA)
            TDE: TDE0997(gdhA)
            AVA: Ava_1204 Ava_4115
            SRU: SRU_0505(gdhA)
            GFO: GFO_0726(gdhA) GFO_3186(gdhA)
            CTE: CT2023(gdhA)
            DRA: DR_0980
            DGE: Dgeo_0494 Dgeo_0495
            TTH: TTC1211 TTC1212
            TTJ: TTHA1576 TTHA1577
            TMA: TM1015
            MAC: MA3169(gdhA)
            MBA: Mbar_A2938
            MMA: MM_0357 MM_3297
            MBU: Mbur_1973
            HAL: VNG0161G(gdhB) VNG0628G(gdhA1) VNG1204G(gdhA2)
            HMA: pNG7157(gudB) rrnAC0384(gdhA1) rrnAC0775(gdhA2)
            NPH: NP1806A(gdhA_1) NP6184A(gdhA_3)
            TAC: Ta0635 Ta0776
            TVO: TVN0759 TVN0760
            PTO: PTO1315
            PHO: PH1593
            PAB: PAB0391(gdh)
            PFU: PF1602
            TKO: TK1431
            RCI: LRC421(gdh-1) LRC422(gdh-2)
            APE: APE_1386.1
            HBU: Hbut_0861
            SSO: SSO1457(gdhA-1) SSO1907(gdhA-2) SSO1930(gdhA-3)
                 SSO2044(gdhA-4)
            STO: ST2241
            SAI: Saci_0155(gdhA)
            PAI: PAE1996 PAE3438
            NEQ: NEQ077
STRUCTURES  PDB: 1B26  1B3B  1BVU  1GTM  1HWX  1HWY  1HWZ  1L1F  1NQT  1NR1  
                 1NR7  2TMG  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.3
            ExPASy - ENZYME nomenclature database: 1.4.1.3
            ExplorEnz - The Enzyme Database: 1.4.1.3
            ERGO genome analysis and discovery system: 1.4.1.3
            BRENDA, the Enzyme Database: 1.4.1.3
            CAS: 9029-12-3
///
ENTRY       EC 1.4.1.4                  Enzyme
NAME        glutamate dehydrogenase (NADP+);
            glutamic dehydrogenase;
            dehydrogenase, glutamate (nicotinamide adenine dinucleotide
            (phosphate));
            glutamic acid dehydrogenase;
            L-glutamate dehydrogenase;
            L-glutamic acid dehydrogenase;
            NAD(P)+-glutamate dehydrogenase;
            NAD(P)H-dependent glutamate dehydrogenase;
            glutamate dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-glutamate:NADP+ oxidoreductase (deaminating)
REACTION    L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH + H+
            [RN:R00248]
ALL_REAC    R00248;
            (other) R00145 R00146 R00243
SUBSTRATE   L-glutamate [CPD:C00025];
            H2O [CPD:C00001];
            NADP+ [CPD:C00006]
PRODUCT     2-oxoglutarate [CPD:C00026];
            NH3 [CPD:C00014];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4144743]
  AUTHORS   Coulton JW, Kapoor M.
  TITLE     Purification and some properties of the glutamate dehydrogenase of
            Salmonella typhimurium.
  JOURNAL   Can. J. Microbiol. 19 (1973) 427-38.
  ORGANISM  Salmonella typhimurium
REFERENCE   2
  AUTHORS   Grisolia, S., Quijada, C.L. and Fernandez, M.
  TITLE     Glutamate dehydrogenase from yeast and from animal tissues.
  JOURNAL   Biochim. Biophys. Acta 81 (1964) 61-70.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:4394939]
  AUTHORS   Shiio I, Ozaki H.
  TITLE     Regulation of nicotinamide adenine dinucleotide phosphate-specific
            glutamate dehydrogenase from Brevibacterium flavum, a
            glutamate-producing bacterium.
  JOURNAL   J. Biochem. (Tokyo). 68 (1970) 633-47.
  ORGANISM  Brevibacterium flavum
REFERENCE   4
  AUTHORS   Smith, E.L., Austen, B.M., Blumenthal, K.M. and Nyc, J.F.
  TITLE     Glutamate dehydrogenases.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 11, Academic
            Press, New York, 1975, p. 293-367.
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00262  glutamate dehydrogenase (NADP+)
GENES       ATH: AT1G51720
            OSA: 4324672
            CME: CMM119C
            SCE: YAL062W(GDH3) YOR375C(GDH1)
            PIC: PICST_82969(GDH3)
            CGR: CAGL0D00176g
            SPO: SPCC622.12c
            ANI: AN4376.2
            AFM: AFUA_4G06620
            AOR: AO090023000923
            ANG: An04g00990(gdhA)
            CNE: CNC00920
            UMA: UM02801.1
            DDI: DDB_0231438
            PFA: PF14_0164 PF14_0286
            TCR: 507875.20 508111.30
            LMA: LmjF28.2910
            ECO: b1761(gdhA)
            ECJ: JW1750(gdhA)
            ECE: Z2793(gdhA)
            ECS: ECs2467
            ECC: c2162(gdhA)
            ECP: ECP_1707
            ECV: APECO1_831(gdhA)
            STY: STY1815(gdhA)
            STT: t1178(gdhA)
            SPT: SPA1545(gdhA)
            SEC: SC1321(gdhA)
            STM: STM1299(gdhA)
            YPE: YPO3971(gdhA)
            YPK: y3858(gdhA)
            YPM: YP_3334(gdhA)
            YPA: YPA_3799
            YPN: YPN_3620
            YPP: YPDSF_3336
            YPS: YPTB3813(gdhA)
            YPI: YpsIP31758_4036(gdhA)
            SFL: SF1462(gdhA)
            SFV: SFV_1457(gdhA)
            SSN: SSON_1395(gdhA)
            SBO: SBO_1328(gdhA)
            SDY: SDY_1514(gdhA)
            ECA: ECA0051(gdhA)
            PLU: plu0122(gdhA)
            ENT: Ent638_1685
            SPE: Spro_4692
            HIT: NTHI0283(gdhA)
            HSO: HS_1339(gdhA)
            PMU: PM0043(gdhA)
            MSU: MS0196(gdhA)
            APL: APL_0427(gdhA)
            ASU: Asuc_0375
            PAE: PA4588(gdhA)
            PAU: PA14_60710(gdhA)
            PPU: PP_0675(gdhA)
            PFL: PFL_5343(gdhA)
            PFO: Pfl_4874
            PEN: PSEEN0812(gdhA)
            PMY: Pmen_1771
            PAR: Psyc_1670(dhe4)
            PCR: Pcryo_1935
            PRW: PsycPRwf_1144
            ACI: ACIAD1110(gdhA)
            SPL: Spea_0527
            ILO: IL2338(gdhA)
            PHA: PSHAa1392(gdhA)
            PAT: Patl_0286
            LPP: lpp2344(gdhA)
            FTU: FTT0380c(gdh)
            FTF: FTF0380c(gdh)
            FTL: FTL_0269
            FTH: FTH_0268
            FTN: FTN_1532(gdhA)
            NOC: Noc_0864
            AEH: Mlg_2123
            HHA: Hhal_0060
            ABO: ABO_2099(gdhA) ABO_2100(gdhA)
            MMW: Mmwyl1_1895
            AHA: AHA_1626
            NME: NMB1710
            NMA: NMA1964(gdhA)
            NMC: NMC1625(gdhA)
            NGO: NGO1358
            REU: Reut_B3724
            REH: H16_B1945(gdhA2)
            RME: Rmet_5114
            BPE: BP0368(gdhA)
            BPA: BPP4062(gdhA)
            BBR: BB4535(gdhA)
            AJS: Ajs_0977
            HAR: HEAR0384(gdhA)
            MMS: mma_1454(gdhA2)
            NEU: NE1616(gdhA)
            NET: Neut_0501
            NMU: Nmul_A2447
            EBA: ebA5425(gdhA)
            MFA: Mfla_1286
            HPY: HP0380
            HPJ: jhp1001(gdhA)
            HPA: HPAG1_1012
            HHE: HH1241(gdhA)
            HAC: Hac_0475(gdhA)
            WSU: WS1924(gdhA)
            TDN: Tmden_1510
            CCO: CCC13826_2140(gdhA)
            ABU: Abu_0287(gdhA)
            SUN: SUN_1928(gdhA)
            GSU: GSU1305
            GME: Gmet_1186
            GUR: Gura_2800
            PPD: Ppro_3497
            DPS: DP2840
            ADE: Adeh_3019
            AFW: Anae109_3000
            SME: SMa0228(gdhA)
            BME: BMEI1723
            BMF: BAB1_0228
            BMS: BR0227
            BMB: BruAb1_0222
            NHA: Nham_0996
            RDE: RD1_2450(gdhA)
            PDE: Pden_3872
            NAR: Saro_1272
            SAL: Sala_2771
            SWI: Swit_0418 Swit_5321
            ELI: ELI_03570
            ABA: Acid345_0942
            BHA: BH2101(gdhA)
            BCZ: BCZK1372(gdhA)
            BTK: BT9727_1373(gdhA)
            BTL: BALH_1347(gdhA)
            BLI: BL00756(rocG)
            BLD: BLi02964(rocG)
            BCL: ABC3392
            BPU: BPUM_3511(gdhA)
            SHA: SH1992(gudB)
            SSP: SSP2174
            LMO: lmo0560
            LMF: LMOf2365_0589(gdhA)
            LIN: lin0569
            LWE: lwe0526(gdhA)
            SPN: SP_1306
            SPR: spr1181(gdhA)
            SPD: SPD_1158(gdhA)
            SAG: SAG1335(gdhA)
            SAN: gbs1405
            SAK: SAK_1366(gdhA)
            SMU: SMU.913
            STC: str0430(gdhA)
            STL: stu0430(gdhA)
            SSA: SSA_0369 SSA_0371(gdhA)
            SGO: SGO_0276(gdhA)
            LSL: LSL_1297(gdhA)
            EFA: EF1415(gdhA)
            CAC: CAC0737
            CPE: CPE1518(gdhA)
            CPF: CPF_1770(gdhA)
            CPR: CPR_1499
            CNO: NT01CX_0097
            CTH: Cthe_0374
            CKL: CKL_3050(gdh)
            DSY: DSY4953
            MSM: MSMEG_5442
            MVA: Mvan_4804
            MMC: Mmcs_4267
            MKM: Mkms_4353
            MJL: Mjls_4646
            CGL: NCgl1999(cgl2079)
            CGB: cg2280(gdh)
            CEF: CE1982(gdh)
            CDI: DIP1547(gdh)
            CJK: jk1192(gdh)
            NFA: nfa45920
            RHA: RHA1_ro01405(gdh)
            SCO: SCO4683(gdhA)
            LXX: Lxx11950(gdhA)
            ART: Arth_3505
            AAU: AAur_3325(gdhA)
            PAC: PPA1513
            NCA: Noca_1658
            TFU: Tfu_1371
            SEN: SACE_5979(gdh)
            BLO: BL0630(gdhA)
            BAD: BAD_0008(gdhA)
            SYN: slr0710(gdhA)
            GVI: gll1133(gdhA)
            ANA: alr4255
            PMT: PMT0623(gdhA)
            PMF: P9303_16151(gdhA)
            TER: Tery_4311
            BTH: BT_1970 BT_1973
            BFR: BF3607 BF3635
            PGI: PG1232(gdh)
            FJO: Fjoh_0708
            FPS: FP0271(gdhA)
            DRA: DR_1718
            MVN: Mevan_1556
            MST: Msp_1416(gdhA)
            MSI: Msm_0888
            HWA: HQ1880A(gdhA)
            NPH: NP1582A(gdhA_2) NP6184A(gdhA_3)
STRUCTURES  PDB: 2BMA  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.4
            ExPASy - ENZYME nomenclature database: 1.4.1.4
            ExplorEnz - The Enzyme Database: 1.4.1.4
            ERGO genome analysis and discovery system: 1.4.1.4
            BRENDA, the Enzyme Database: 1.4.1.4
            CAS: 9029-11-2
///
ENTRY       EC 1.4.1.5                  Enzyme
NAME        L-amino-acid dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-amino-acid:NAD+ oxidoreductase (deaminating)
REACTION    an L-amino acid + H2O + NAD+ = a 2-oxo acid + NH3 + NADH + H+
            [RN:R01258]
ALL_REAC    R01258;
            (other) R00145 R00146
SUBSTRATE   L-amino acid [CPD:C00151];
            H2O [CPD:C00001];
            NAD+ [CPD:C00003]
PRODUCT     2-oxo acid [CPD:C00161];
            NH3 [CPD:C00014];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Acts on aliphatic amino acids.
REFERENCE   1
  AUTHORS   Nisman, B. and Mager, J.
  TITLE     Diphosphopyridine nucleotide and phosphate requirement for oxidation
            of amino-acids by cell-free extracts of obligate anaerobes.
  JOURNAL   Nature (Lond.) 169 (1952) 243-244.
  ORGANISM  Clostridia sporogenes, Clostridia saccharobutyricum
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.5
            ExPASy - ENZYME nomenclature database: 1.4.1.5
            ExplorEnz - The Enzyme Database: 1.4.1.5
            ERGO genome analysis and discovery system: 1.4.1.5
            BRENDA, the Enzyme Database: 1.4.1.5
            CAS: 9029-13-4
///
ENTRY       EC 1.4.1.6        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: now included with EC 1.21.4.1 D-proline reductase
            (dithiol) (EC 1.4.1.6 created 1961, deleted 1982)
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.6
            ExPASy - ENZYME nomenclature database: 1.4.1.6
            ExplorEnz - The Enzyme Database: 1.4.1.6
            ERGO genome analysis and discovery system: 1.4.1.6
            BRENDA, the Enzyme Database: 1.4.1.6
///
ENTRY       EC 1.4.1.7                  Enzyme
NAME        serine 2-dehydrogenase;
            L-serine:NAD+ oxidoreductase (deaminating);
            serine dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-serine:NAD+ 2-oxidoreductase (deaminating)
REACTION    L-serine + H2O + NAD+ = 3-hydroxypyruvate + NH3 + NADH + H+
            [RN:R00581]
ALL_REAC    R00581;
            (other) R00145 R00146
SUBSTRATE   L-serine [CPD:C00065];
            H2O [CPD:C00001];
            NAD+ [CPD:C00003]
PRODUCT     3-hydroxypyruvate [CPD:C00168];
            NH3 [CPD:C00014];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:5972761]
  AUTHORS   Kretovich VL, Stepanovich KM.
  TITLE     [The enzyme catalyzing the reductive amination of oxypyruvate]
  JOURNAL   Izv. Akad. Nauk. SSSR. Biol. 2 (1966) 295-300.
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.7
            ExPASy - ENZYME nomenclature database: 1.4.1.7
            ExplorEnz - The Enzyme Database: 1.4.1.7
            ERGO genome analysis and discovery system: 1.4.1.7
            BRENDA, the Enzyme Database: 1.4.1.7
///
ENTRY       EC 1.4.1.8                  Enzyme
NAME        valine dehydrogenase (NADP+);
            valine dehydrogenase (nicotinanide adenine dinucleotide phosphate);
            valine dehydrogenase (NADP+)
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-valine:NADP+ oxidoreductase (deaminating)
REACTION    L-valine + H2O + NADP+ = 3-methyl-2-oxobutanoate + NH3 + NADPH + H+
            [RN:R01212]
ALL_REAC    R01212;
            (other) R00145 R00146
SUBSTRATE   L-valine [CPD:C00183];
            H2O [CPD:C00001];
            NADP+ [CPD:C00006]
PRODUCT     3-methyl-2-oxobutanoate [CPD:C00141];
            NH3 [CPD:C00014];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:6005410]
  AUTHORS   Kagan ZS, Kretovich WL, Polyakov WA.
  TITLE     Biosynthesis of valine by reductive amination of its keto analogue
            in plants.
  JOURNAL   Enzymologia. 30 (1966) 343-66.
REFERENCE   2  [PMID:4385962]
  AUTHORS   Kagan ZS, Poliakov VA, Kretovich VL.
  TITLE     [Soluble valine dehydrogenase from roots of plant seedings]
  JOURNAL   Biokhimiia. 33 (1968) 89-96.
REFERENCE   3  [PMID:4389825]
  AUTHORS   Kagan ZS, Poliakov VA, Kretovich VL.
  TITLE     [Purification and properties of valine dehydrogenase]
  JOURNAL   Biokhimiia. 34 (1969) 59-65.
REFERENCE   4  [PMID:3182727]
  AUTHORS   Vancurova I, Vancura A, Volc J, Neuzil J, Flieger M, Basarova G,
            Behal V.
  TITLE     Isolation and characterization of valine dehydrogenase from
            Streptomyces aureofaciens.
  JOURNAL   J. Bacteriol. 170 (1988) 5192-6.
  ORGANISM  Streptomyces aureofaciens
GENES       FPS: FP0533(vdh)
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.8
            ExPASy - ENZYME nomenclature database: 1.4.1.8
            ExplorEnz - The Enzyme Database: 1.4.1.8
            ERGO genome analysis and discovery system: 1.4.1.8
            BRENDA, the Enzyme Database: 1.4.1.8
            CAS: 37255-39-3
///
ENTRY       EC 1.4.1.9                  Enzyme
NAME        leucine dehydrogenase;
            L-leucine dehydrogenase;
            L-leucine:NAD+ oxidoreductase, deaminating;
            LeuDH
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-leucine:NAD+ oxidoreductase (deaminating)
REACTION    L-leucine + H2O + NAD+ = 4-methyl-2-oxopentanoate + NH3 + NADH + H+
            [RN:R01088]
ALL_REAC    R01088;
            (other) R00145 R00146 R01434 R02196 R03960
SUBSTRATE   L-leucine [CPD:C00123];
            H2O [CPD:C00001];
            NAD+ [CPD:C00003]
PRODUCT     4-methyl-2-oxopentanoate [CPD:C00233];
            NH3 [CPD:C00014];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts on isoleucine, valine, norvaline and norleucine.
REFERENCE   1
  AUTHORS   Sanwal, B.D. and Zink, M.W.
  TITLE     L-Leucine dehydrogenase of Bacillus cereus.
  JOURNAL   Arch. Biochem. Biophys. 94 (1961) 430-435.
  ORGANISM  Bacillus cereus
REFERENCE   2
  AUTHORS   Zink, M.W. and Sanwal, B.D.
  TITLE     The distribution and substrate specificity of L-leucine
            dehydrogenase.
  JOURNAL   Arch. Biochem. Biophys. 99 (1962) 72-77.
  ORGANISM  Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00290  Valine, leucine and isoleucine biosynthesis
ORTHOLOGY   KO: K00263  leucine dehydrogenase
GENES       XCC: XCC1299(leu)
            XCB: XC_2941
            XCV: XCV1403(ldh)
            XAC: XAC1350(leu)
            XOO: XOO1883(leu)
            XOM: XOO_1780(XOO1780)
            PAE: PA3418(ldh)
            PAU: PA14_19870(ldh)
            PPU: PP_4617
            PFL: PFL_0973(ldh)
            PFO: Pfl_0915
            PEN: PSEEN4606
            SON: SO_2638(ldh)
            SDN: Sden_1823
            SFR: Sfri_2265
            SHE: Shewmr4_1598
            SHM: Shewmr7_1673
            SHN: Shewana3_1742
            ILO: IL1314
            CPS: CPS_2904
            PHA: PSHAa1167(bcd)
            PAT: Patl_2995
            CBU: CBU_0641
            LPN: lpg2276
            LPF: lpl2202
            LPP: lpp2230
            NOC: Noc_1436
            HCH: HCH_00319
            REU: Reut_B5816 Reut_C6219
            REH: H16_B0449
            BXE: Bxe_A2689
            BBA: Bd2028
            MXA: MXAN_1074
            MES: Meso_3241
            CCR: CC_2082
            SIL: SPO0390
            SIT: TM1040_2779
            MMR: Mmar10_0963
            HNE: HNE_1615(ldh1) HNE_2735(ldh2)
            SAL: Sala_1521 Sala_1973
            ELI: ELI_03850
            RRU: Rru_A1040
            BSU: BG11723(bcd)
            BHA: BH2765
            BAN: BA4387
            BAR: GBAA4387
            BAA: BA_4842
            BAT: BAS4070
            BCE: BC4162
            BCA: BCE_4237
            BCZ: BCZK3917(dhlE)
            BTK: BT9727_3908(dhlE)
            BTL: BALH_3775(dhlE)
            BLI: BL01501(bcd)
            BLD: BLi02585(bcd)
            BCL: ABC2453(bcd)
            BAY: RBAM_022360(bcd)
            BPU: BPUM_2147(bcd)
            OIH: OB1869
            GKA: GK2381
            GTN: GTNG_2310
            STH: STH1827 STH1830
            CHY: CHY_0579(ldh)
            TTE: TTE2202(gdhA3) TTE2203(gdhA4)
            RHA: RHA1_ro01628
            SMA: SAV4132(vdh)
            FRA: Francci3_0097
            FAL: FRAAL0132(vdh)
            RXY: Rxyl_2467
            CTR: CT773(ldh)
            CTA: CTA_0843(ldh)
            CMU: TC0154
            CPN: CPn0919(ldh)
            CPA: CP0947
            CPJ: CPj0919(ldh)
            CPT: CpB0951
            CCA: CCA00850
            CAB: CAB815
            CFE: CF0166(gdhA)
            SYD: Syncc9605_0225
            SYE: Syncc9902_0253
            SYG: sync_0270
            ANA: all0426
            GFO: GFO_2528(ldh)
            DRA: DR_0158
            DGE: Dgeo_0203
STRUCTURES  PDB: 1LEH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.9
            ExPASy - ENZYME nomenclature database: 1.4.1.9
            ExplorEnz - The Enzyme Database: 1.4.1.9
            ERGO genome analysis and discovery system: 1.4.1.9
            BRENDA, the Enzyme Database: 1.4.1.9
            CAS: 9082-71-7
///
ENTRY       EC 1.4.1.10                 Enzyme
NAME        glycine dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     glycine:NAD+ oxidoreductase (deaminating)
REACTION    glycine + H2O + NAD+ = glyoxylate + NH3 + NADH + H+ [RN:R00365]
ALL_REAC    R00365;
            (other) R00145 R00146
SUBSTRATE   glycine [CPD:C00037];
            H2O [CPD:C00001];
            NAD+ [CPD:C00003]
PRODUCT     glyoxylate [CPD:C00048];
            NH3 [CPD:C00014];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13948749]
  AUTHORS   GOLDMAN DS, WAGNER MJ.
  TITLE     Enzyme systems in the mycobacteria. XIII. Glycine dehydrogenase and
            the glyoxylic acid cycle.
  JOURNAL   Biochim. Biophys. Acta. 65 (1962) 297-306.
  ORGANISM  Mycobacterium tuberculosis
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.10
            ExPASy - ENZYME nomenclature database: 1.4.1.10
            ExplorEnz - The Enzyme Database: 1.4.1.10
            ERGO genome analysis and discovery system: 1.4.1.10
            BRENDA, the Enzyme Database: 1.4.1.10
            CAS: 37255-40-6
///
ENTRY       EC 1.4.1.11                 Enzyme
NAME        L-erythro-3,5-diaminohexanoate dehydrogenase;
            L-3,5-diaminohexanoate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-erythro-3,5-diaminohexanoate:NAD+ oxidoreductase (deaminating)
REACTION    L-erythro-3,5-diaminohexanoate + H2O + NAD+ =
            (S)-5-amino-3-oxohexanoate + NH3 + NADH + H+ [RN:R03349]
ALL_REAC    R03349
SUBSTRATE   L-erythro-3,5-diaminohexanoate [CPD:C01186];
            H2O [CPD:C00001];
            NAD+ [CPD:C00003]
PRODUCT     (S)-5-amino-3-oxohexanoate [CPD:C03656];
            NH3 [CPD:C00014];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4344229]
  AUTHORS   Baker JJ, Jeng I, Barker HA.
  TITLE     Purification and properties of L-erythro-3,5-diaminohexanoate
            dehydrogenase from a lysine-fermenting Clostridium.
  JOURNAL   J. Biol. Chem. 247 (1972) 7724-34.
  ORGANISM  Clostridium sp.
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.11
            ExPASy - ENZYME nomenclature database: 1.4.1.11
            ExplorEnz - The Enzyme Database: 1.4.1.11
            ERGO genome analysis and discovery system: 1.4.1.11
            BRENDA, the Enzyme Database: 1.4.1.11
            CAS: 37377-90-5
///
ENTRY       EC 1.4.1.12                 Enzyme
NAME        2,4-diaminopentanoate dehydrogenase;
            2,4-diaminopentanoic acid C4 dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2,4-diaminopentanoate:NAD(P)+ oxidoreductase (deaminating)
REACTION    2,4-diaminopentanoate + H2O + NAD(P)+ = 2-amino-4-oxopentanoate +
            NH3 + NAD(P)H + H+ [RN:R04200 R04201]
ALL_REAC    R04200 R04201;
            (other) R00145 R00146 R02825 R04687 R04688
SUBSTRATE   2,4-diaminopentanoate [CPD:C03943];
            H2O [CPD:C00001];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     2-amino-4-oxopentanoate [CPD:C03341];
            NH3 [CPD:C00014];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts, more slowly, on 2,5-diaminohexanoate forming
            2-amino-5-oxohexanoate, which then cyclizes non-enzymically to
            1-pyrroline-2-methyl-5-carboxylate.
REFERENCE   1  [PMID:4684685]
  AUTHORS   Somack R, Costilow RN.
  TITLE     2,4-diaminopentanoic acid C 4  dehydrogenase. Purification and
            properties of the protein.
  JOURNAL   J. Biol. Chem. 248 (1973) 385-8.
  ORGANISM  Clostridium sticklandii
REFERENCE   2
  AUTHORS   Stadtman, T.C.
  TITLE     Lysine metabolism by clostridia. XIIB 2,4-Diaminohexanoate
            dehydrogenase (2,4-diaminopentanoate dehydrogenase).
  JOURNAL   Adv. Enzymol. Relat. Areas Mol. Biol. 38 (1973) 441-445.
  ORGANISM  Clostridium sticklandii
REFERENCE   3  [PMID:4394942]
  AUTHORS   Tsuda Y, Friedmann HC.
  TITLE     Ornithine metabolism by Clostridium sticklandii. Oxidation of
            ornithine to 2-amino-4-ketopentanoic acid via 2,4-diaminopentanoic
            acid; participation of B12 coenzyme, pyridoxal phosphate, and
            pyridine nucleotide.
  JOURNAL   J. Biol. Chem. 245 (1970) 5914-26.
  ORGANISM  Clostridium sticklandii
PATHWAY     PATH: map00310  Lysine degradation
            PATH: map00330  Arginine and proline metabolism
            PATH: map00472  D-Arginine and D-ornithine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.12
            ExPASy - ENZYME nomenclature database: 1.4.1.12
            ExplorEnz - The Enzyme Database: 1.4.1.12
            ERGO genome analysis and discovery system: 1.4.1.12
            BRENDA, the Enzyme Database: 1.4.1.12
            CAS: 39346-26-4
///
ENTRY       EC 1.4.1.13                 Enzyme
NAME        glutamate synthase (NADPH);
            glutamate (reduced nicotinamide adenine dinucleotide phosphate)
            synthase;
            L-glutamate synthase;
            L-glutamate synthetase;
            glutamate synthetase (NADP);
            NADPH-dependent glutamate synthase;
            glutamine-ketoglutaric aminotransferase;
            NADPH-glutamate synthase;
            NADPH-linked glutamate synthase;
            glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase,
            NADP);
            L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing;
            glutamate synthase (NADPH)
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-glutamate:NADP+ oxidoreductase (transaminating)
REACTION    2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+
            [RN:R00114]
ALL_REAC    R00114
SUBSTRATE   L-glutamate [CPD:C00025];
            NADP+ [CPD:C00006]
PRODUCT     L-glutamine [CPD:C00064];
            2-oxoglutarate [CPD:C00026];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023];
            FMN [CPD:C00061];
            Sulfur [CPD:C00087];
            Iron-sulfur [CPD:C00824]
COMMENT     An iron-sulfur flavoprotein. In the reverse reaction, ammonia can
            act instead of glutamine, but more slowly.
REFERENCE   1  [PMID:4565085]
  AUTHORS   Miller RE, Stadtman ER.
  TITLE     Glutamate synthase from Escherichia coli. An iron-sulfide
            flavoprotein.
  JOURNAL   J. Biol. Chem. 247 (1972) 7407-19.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:5420057]
  AUTHORS   Tempest DW, Meers JL, Brown CM.
  TITLE     Synthesis of glutamate in Aerobacter aerogenes by a hitherto unknown
            route.
  JOURNAL   Biochem. J. 117 (1970) 405-7.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00264  glutamate synthase (NADPH)
            KO: K00265  glutamate synthase (NADPH) large chain
            KO: K00266  glutamate synthase (NADPH) small chain
GENES       CEL: W07E11.1
            ATH: AT5G53460(GLT1)
            SCE: YDL171C(GLT1)
            AGO: AGOS_ADR290W
            PIC: PICST_87428(GLT1)
            CGR: CAGL0L01089g
            SPO: SPAPB1E7.07
            ANI: AN5134.2
            AFM: AFUA_1G07380
            AOR: AO090012000988
            CNE: CNJ02910
            UMA: UM03850.1
            PFA: PF14_0334
            TET: TTHERM_01126420
            EHI: 3.t00052 5.t00071 78.t00007
            ECO: b3212(gltB) b3213(gltD)
            ECJ: JW3179(gltB) JW3180(gltD)
            ECE: Z4576(gltB) Z4577(gltD)
            ECS: ECs4091 ECs4092
            ECC: c3973(gltB) c3974(gltD)
            ECI: UTI89_C2419(yeiT) UTI89_C2794(aegA) UTI89_C3649(gltB)
                 UTI89_C3650(gltD)
            ECP: ECP_3302
            ECV: APECO1_3223(gltD) APECO1_32232(gltB)
            ECW: EcE24377A_3700(gltB) EcE24377A_3701(gltD)
            ECX: EcHS_A3405(gltB) EcHS_A3406(gltD)
            STY: STY3510(gltB) STY3511(gltD)
            STT: t3247(gltB) t3248(gltD)
            SPT: SPA3198(gltB) SPA3199(gltD)
            SEC: SC3268(gltB) SC3269(gltD)
            STM: STM3330(gltB) STM3331(gltD)
            YPE: YPO3557(gltB) YPO3558(gltD)
            YPK: y0128(gltB) y0129(gltD)
            YPM: YP_3811(gltB) YP_3812(gltD2)
            YPA: YPA_3745 YPA_3746
            YPN: YPN_3439 YPN_3440
            YPS: YPTB3502(gltB) YPTB3503(gltD)
            YPI: YpsIP31758_0465(gltD) YpsIP31758_0466(gltB)
            SFL: SF3252(gltB) SF3253(gltD)
            SFX: S3470(gltB) S3471(gltD)
            SFV: SFV_3242(gltB) SFV_3243(gltD)
            SSN: SSON_3360(gltB) SSON_3361(gltD)
            SBO: SBO_3169(gltD) SBO_3170(gltB)
            SDY: SDY_3393(gltB) SDY_3394(gltD)
            ECA: ECA0311(gltD) ECA0312(gltB)
            PLU: plu4009(gltB) plu4010(gltD)
            XFA: XF2709 XF2710
            XFT: PD2062(gltD) PD2063(gltB)
            XCC: XCC0031(gltD) XCC0032(gltB)
            XCB: XC_0031 XC_0032
            XCV: XCV0036(gltD) XCV0037(gltB)
            XAC: XAC0032(gltD) XAC0033(gltB)
            XOO: XOO0177(gltB) XOO0178(gltD)
            XOM: XOO_0157(XOO0157) XOO_0158(XOO0158)
            VCH: VC2373 VC2374 VC2376 VC2377
            VCO: VC0395_A1953(gltD-1) VC0395_A1954(gltB-2)
                 VC0395_A1955(gltD-2)
            VVU: VV1_0553 VV1_0554 VV1_0555 VV1_0556
            VVY: VV0638 VV0639 VV0640 VV0641
            VPA: VP0481 VP0482 VP0483 VP0484
            VFI: VF2124 VF2125
            PPR: PBPRA0539 PBPRA0540 PBPRA0541 PBPRA0542
            PAE: PA0440 PA3602 PA5035(gltD) PA5036(gltB)
            PAU: PA14_17690 PA14_66560(gltD) PA14_66570(gltB)
            PPU: PP_4037 PP_5075(gltD) PP_5076(gltB)
            PPF: Pput_0285 Pput_1101
            PST: PSPTO_5121(gltD) PSPTO_5123(gltB)
            PSB: Psyr_0411 Psyr_0412
            PSP: PSPPH_0398(gltB) PSPPH_0400(gltD)
            PFL: PFL_0453 PFL_0454 PFL_2547(gltD-2) PFL_4900(gltB)
            PFO: Pfl_0413 Pfl_0414 Pfl_3442 Pfl_4559
            PEN: PSEEN0337(gltB) PSEEN0338(gltD) PSEEN1180 PSEEN3252
            PMY: Pmen_1544
            PAR: Psyc_1873(gltD) Psyc_1874(gltB)
            PCR: Pcryo_0813 Pcryo_2164
            ACI: ACIAD2525 ACIAD3349(gltD) ACIAD3350(gltB)
            SON: SO_1324(gltD) SO_1325(gltB)
            SDN: Sden_2791
            SFR: Sfri_2952
            SHE: Shewmr4_2873
            SHM: Shewmr7_2955
            SHN: Shewana3_3051 Shewana3_3523
            ILO: IL1074(gltD) IL1075(gltB)
            CPS: CPS_0761 CPS_0762 CPS_4501(gltB) CPS_4502(gltD)
            PHA: PSHAa2923 PSHAb0127(gltB)
            PAT: Patl_1434 Patl_3749
            SDE: Sde_2682 Sde_2683
            PIN: Ping_2312
            CBU: CBU_1203
            LPN: lpg0074
            LPF: lpl0076
            LPP: lpp0088
            MCA: MCA2039(gltB) MCA2040(gltD)
            FTL: FTL_0665
            FTH: FTH_0667(gltB)
            FTN: FTN_1360(gltB)
            TCX: Tcr_1344 Tcr_1957 Tcr_1958
            NOC: Noc_0101 Noc_1603 Noc_1604 Noc_2957
            AEH: Mlg_0235 Mlg_2764
            HCH: HCH_05964 HCH_05965
            CSA: Csal_0616
            ABO: ABO_2228(gltD) ABO_2229(gltB)
            AHA: AHA_2703 AHA_2704
            VOK: COSY_0796(gltD) COSY_0919(gltB)
            CVI: CV_4037(gltD) CV_4038(gltB)
            RSO: RSc2964(gltD) RSc2965(gltB)
            REU: Reut_A3125
            REH: H16_A3430(gltD) H16_A3431(gltB1) H16_B2192(glxB)
                 H16_B2193(glxC) H16_B2194(gltB2)
            RME: Rmet_3262 Rmet_3263
            BMA: BMA2363 BMA2735(gltD) BMA2736(gltB)
            BMV: BMASAVP1_A0277 BMASAVP1_A3216(gltB) BMASAVP1_A3217(gltD)
            BML: BMA10299_A1139 BMA10299_A1767(gltB) BMA10299_A1768(gltD)
            BMN: BMA10247_2543 BMA10247_2786(gltD) BMA10247_2787(gltB)
            BXE: Bxe_A0365 Bxe_A0366 Bxe_A1428 Bxe_A4011
            BVI: Bcep1808_0662
            BUR: Bcep18194_A3500 Bcep18194_A3783 Bcep18194_C6655
            BCN: Bcen_0213
            BCH: Bcen2424_0403 Bcen2424_0697 Bcen2424_6235
            BAM: Bamb_0322 Bamb_0590
            BPS: BPSL2890 BPSL3158(glt2) BPSL3159(glt1)
            BPM: BURPS1710b_3397 BURPS1710b_3716 BURPS1710b_3718(gltB)
            BPL: BURPS1106A_3390 BURPS1106A_3746(gltD) BURPS1106A_3747(gltB)
            BPD: BURPS668_3355 BURPS668_3689(gltD) BURPS668_3690(gltB)
            BTE: BTH_I1256 BTH_I3013 BTH_I3014
            PNU: Pnuc_1210
            BPE: BP3753(gltB) BP3754
            BPA: BPP4253(gltB) BPP4254
            BBR: BB4840(gltB) BB4841
            RFR: Rfer_2934 Rfer_3208
            POL: Bpro_0792
            MPT: Mpe_A3102 Mpe_A3103
            HAR: HEAR0324 HEAR3081(gltD) HEAR3082(gltB)
            MMS: mma_3300(gltD) mma_3301(gltB)
            EBA: ebA2251(gltD) ebA2252(gls1)
            AZO: azo3641(gltD)
            DAR: Daro_0217 Daro_0218
            TBD: Tbd_2767 Tbd_2768
            MFA: Mfla_2734
            WSU: WS1201(gltD) WS1202
            TDN: Tmden_1131 Tmden_1175 Tmden_1824
            CJE: Cj0007(gltB) Cj0009(gltD)
            CJR: CJE0007(gltB) CJE0008(gltD)
            CJJ: CJJ81176_0033(gltB) CJJ81176_0035(gltD)
            CJU: C8J_0007(gltB) C8J_0008(gltD)
            CJD: JJD26997_0007 JJD26997_0009(gltD)
            CFF: CFF8240_1486(gltD) CFF8240_1487(gltB)
            ABU: Abu_1826(gltD) Abu_1827(gltB)
            NIS: NIS_1200(gltD) NIS_1201(gltB)
            SUN: SUN_0907(gltB)
            GSU: GSU1239 GSU3057(gltA) GSU3450
            GME: Gmet_0147 Gmet_1756
            GUR: Gura_2494
            PCA: Pcar_0752 Pcar_1482 Pcar_1483 Pcar_2295 Pcar_2944
            DVU: DVU0671 DVU1613 DVU1823 DVU2476(gltA)
            DVL: Dvul_1337
            DDE: Dde_1218 Dde_1250 Dde_1814 Dde_1815 Dde_2086 Dde_3635
            LIP: LI0325(gltD)
            BBA: Bd2241(glt)
            DPS: DP0508 DP0632
            MXA: MXAN_3918
            SAT: SYN_00363 SYN_00606 SYN_01629 SYN_01630 SYN_01631 SYN_02385
            SFU: Sfum_2150
            PUB: SAR11_0141 SAR11_0433(gltD) SAR11_0434(gltB) SAR11_1308
                 SAR11_1315(glxD)
            MLO: mll1646 mll3029 mll3030
            MES: Meso_2057 Meso_2743 Meso_2744
            SME: SMc01814 SMc04026(gltD) SMc04028(gltB)
            ATU: Atu3783(gltD) Atu3784(gltB)
            ATC: AGR_L_2101 AGR_L_2104
            RET: RHE_CH03277 RHE_CH03565(gltD) RHE_CH03566(gltB)
                 RHE_PE00419(glxD)
            RLE: RL3707(gltB) RL4084(gltB) RL4085(gltA) pRL110555(gltB)
            BME: BMEI1638 BMEII0039 BMEII0040
            BMF: BAB1_0314 BAB2_0053(gltB) BAB2_0054(gltD)
            BMS: BR0283 BRA0054(gltB) BRA0055(gltD)
            BMB: BruAb1_0309 BruAb2_0054(gltB) BruAb2_0055(gltD)
            BJA: blr7743(gltB) blr7744(gltD)
            BRA: BRADO0693 BRADO5800 BRADO5883 BRADO6238(gltB) BRADO6240(gltD)
            BBT: BBta_1370(gltD) BBta_1371(gltB) BBta_1944 BBta_6307
            RPA: RPA0473 RPA0891(gltB) RPA0892(gltD) RPA4722
            RPB: RPB_0566 RPB_0850 RPB_4530
            RPC: RPC_0567 RPC_0703 RPC_0760
            RPD: RPD_0262 RPD_0875 RPD_0876 RPD_0958
            RPE: RPE_0111 RPE_0682 RPE_0767
            NWI: Nwi_2954
            NHA: Nham_1137
            CCR: CC_3606 CC_3607
            SIL: SPO1776 SPO3768(gltB) SPO3770(gltD)
            SIT: TM1040_1501 TM1040_2822
            RSP: RSP_0189 RSP_1146(gltB) RSP_1149(gltD)
            JAN: Jann_0248
            RDE: RD1_0060(gltB) RD1_0063(gltD) RD1_0083 RD1_3104 RD1_4251
            MMR: Mmar10_0301
            HNE: HNE_0092(gltD) HNE_0093(gltB)
            ZMO: ZMO1116(gltD) ZMO1117(gltB)
            NAR: Saro_3175
            SAL: Sala_2138
            SWI: Swit_4784
            ELI: ELI_12125 ELI_12130
            GOX: GOX1851 GOX1852
            GBE: GbCGDNIH1_0703 GbCGDNIH1_0704 GbCGDNIH1_2111
            RRU: Rru_A0018 Rru_A0019
            MAG: amb0521 amb0522 amb2331 amb2332
            MGM: Mmc1_0707
            ABA: Acid345_2796 Acid345_3679
            BSU: BG10811(gltA) BG12594(gltB) BG12832(yerD)
            BHA: BH1728(gltA) BH1729(gltB)
            BAN: BA0530
            BAA: BA_1100
            BAT: BAS0498
            BCE: BC0511
            BCA: BCE_0585
            BCZ: BCZK0437(gltB) pE33L466_0262(gltB)
            BTK: BT9727_0441(gltB)
            BTL: BALH_0463(gltB)
            BLI: BL01971(gltA) BL01973(gltB)
            BLD: BLi02161(gltB) BLi02162(gltA)
            BCL: ABC2034(gltB) ABC2035(gltA) ABC3781
            BAY: RBAM_018610(gltB) RBAM_018620(gltA)
            BPU: BPUM_1813(gltB) BPUM_1814(gltA)
            OIH: OB3098 OB3099
            GKA: GK1421 GK1431 GK1432
            SAU: SA0430(gltB) SA0431(gltD) SA2248
            SAV: SAV0472(gltB) SAV2459
            SAM: MW0426(gltB) MW0427(gltD) MW2383
            SAR: SAR0471(gltA) SAR2547
            SAS: SAS0429 SAS0430 SAS2351
            SAC: SACOL0514(gltB) SACOL0515(gltD) SACOL2469
            SAB: SAB0421(gltA) SAB2343c
            SAA: SAUSA300_0445(gltB) SAUSA300_0446(gltD) SAUSA300_2404
            SAO: SAOUHSC_00435 SAOUHSC_00436 SAOUHSC_02760
            SEP: SE2028 SE2311 SE2312
            SER: SERP0109(gltD) SERP2041
            SHA: SH0594 SH2539(gltD) SH2540(gltB)
            SSP: SSP0439 SSP2283 SSP2284
            LMO: lmo1733 lmo1734
            LMF: LMOf2365_1757(gltD) LMOf2365_1758(gltB)
            LIN: lin1844 lin1845
            LWE: lwe1750(gltD) lwe1751(gltB)
            LLA: L0119(gltB) L114827(gltD)
            LLC: LACR_1406 LACR_1407
            LLM: llmg_1183(gltB) llmg_1184(gltD)
            SMU: SMU.365(gltA) SMU.366(gltB)
            LCA: LSEI_2555 LSEI_2556
            EFA: EF2560(gltA)
            STH: STH230
            CAC: CAC0764 CAC1673(gltA) CAC1674(gltB)
            CPE: CPE1254(gltB) CPE2461
            CPF: CPF_1463(gltA) CPF_2776
            CPR: CPR_1263(gltA) CPR_2463
            CTC: CTC02420
            CNO: NT01CX_0466(gltA)
            CTH: Cthe_0198
            CDF: CD1537(aspB)
            CBO: CBO1645(aspB)
            CBA: CLB_1662(gltA-1) CLB_3360(gltA-2)
            CBH: CLC_1671(gltA-1) CLC_3246(gltA-2)
            CBF: CLI_1722(gltA-1) CLI_3474(gltA-2)
            CKL: CKL_1619(gltD) CKL_1620(gltB)
            CHY: CHY_0707 CHY_1991(gltA)
            DSY: DSY2361 DSY3190 DSY4385
            CSC: Csac_0544 Csac_0578
            TTE: TTE0567(gltD) TTE0693(gltD2) TTE0819(gltB2)
            MTA: Moth_1292 Moth_1517
            MTU: Rv3858c(gltD) Rv3859c(gltB)
            MTC: MT3973(gltD) MT3974(gltB)
            MBO: Mb3888c(gltD) Mb3889c(gltB)
            MBB: BCG_3921c(gltD) BCG_3922c(gltB)
            MLE: ML0061(gltB) ML0062(gltD)
            MPA: MAP0172(gltB) MAP0173(gltD)
            MAV: MAV_0167(gltD)
            MSM: MSMEG_3226 MSMEG_6263 MSMEG_6458
            MMC: Mmcs_3043 Mmcs_5065
            CGL: NCgl0181(cgl0184) NCgl0182(cgl0185)
            CGB: cg0229(gltB) cg0230(gltD)
            CEF: CE0158(gltB) CE0159(gltD)
            CJK: jk0076(gltB) jk0077(gltD)
            NFA: nfa960(gltB) nfa970(gltD)
            RHA: RHA1_ro01008 RHA1_ro01009 RHA1_ro01796 RHA1_ro01871
                 RHA1_ro02817 RHA1_ro03717 RHA1_ro03718 RHA1_ro08307
            SCO: SCO1977(SC3C9.12) SCO2025(gltD) SCO2026(gltB)
            SMA: SAV6189(gltB) SAV6190(gltD1) SAV6258(gltD2)
            LXX: Lxx11320(gltB) Lxx11330(gltD)
            CMI: CMM_1759(gltD) CMM_1760(gltB)
            AAU: AAur_1842(gltB)
            PAC: PPA1134 PPA1135
            TFU: Tfu_1173 Tfu_1174
            FRA: Francci3_2913 Francci3_3012
            FAL: FRAAL1890(glxD) FRAAL2367 FRAAL4964(gltD) FRAAL4965(gltB)
            SEN: SACE_3997 SACE_3998(gltB) SACE_5741 SACE_5742(gltB)
            BLO: BL0833(gltD) BL0834(gltB)
            BAD: BAD_0748(gltB) BAD_0749(gltD)
            RXY: Rxyl_0342 Rxyl_2499
            RBA: RB5653(gltD) RB5654(gltB)
            TPA: TP0735
            TDE: TDE0407(gltA)
            LIL: LA0956(gltB1)
            LIC: LIC12694
            LBJ: LBJ_0741(gltB)
            LBL: LBL_2337(gltB)
            PMB: A9601_17161(gltB)
            PMC: P9515_16921(gltB)
            PMF: P9303_23581(gltB)
            PMG: P9301_17041(gltB)
            PMH: P9215_17801(gltB)
            PME: NATL1_19531(gltB)
            TER: Tery_0466
            BTH: BT_0552 BT_0553 BT_4310
            BFR: BF1005
            BFS: BF0926
            PGI: PG2033(gltD)
            SRU: SRU_1169(gltB) SRU_1170(gltD)
            CHU: CHU_3469(gltB) CHU_3776(gltB) CHU_3777(gltD)
            GFO: GFO_2908(gltB) GFO_2909(gltD)
            CTE: CT0282 CT0401(gltB) CT0402(gltD-2) CT0473(gltD-1)
            CCH: Cag_0185 Cag_0537 Cag_0580 Cag_1954
            CPH: Cpha266_1570
            PLT: Plut_0503 Plut_1693
            DET: DET0038(gltA) DET1128
            DEH: cbdb_A1055 cbdb_A46(gltA)
            DEB: DehaBAV1_0957
            DRA: DR_0182 DR_0183
            DGE: Dgeo_2627
            TTH: TTC1104
            TTJ: TTHA1468
            AAE: aq_1565(gltB) aq_2064(gltD)
            TMA: TM0397 TM1217 TM1640
            TPT: Tpet_0523
            MJA: MJ1351(gltB)
            MMP: MMP0080 MMP0081(gltB) MMP0082 MMP0496
            MMQ: MmarC5_1597
            MMZ: MmarC7_1079
            MAE: Maeo_1301
            MVN: Mevan_1093
            MAC: MA3787(gltD) MA4218
            MBA: Mbar_A0227 Mbar_A0664
            MMA: MM_0664 MM_0967
            MBU: Mbur_0092 Mbur_1328
            MTP: Mthe_0212
            MHU: Mhun_0781 Mhun_1117
            MEM: Memar_0333 Memar_2137
            MBN: Mboo_1691
            MTH: MTH105 MTH1666 MTH194
            MST: Msp_0667 Msp_0669 Msp_0670
            MSI: Msm_0027 Msm_0368
            MKA: MK0550(gltB_1)
            AFU: AF0953(gltB)
            HWA: HQ1714A(gltB)
            TAC: Ta0414
            TVO: TVN1157
            PTO: PTO1462 PTO1463
            PHO: PH0876 PH1873
            PAB: PAB1214 PAB1738
            PFU: PF0205 PF1327 PF1852 PF1910
            TKO: TK0672 TK1325 TK1684 TK2074
            RCI: RCIX52(gltB3) RCIX54(gltB2) RCIX56(gltB1) RRC282(gltD)
            APE: APE_0935
            SSO: SSO0684(gltB)
            STO: ST2198
            SAI: Saci_2320
            MSE: Msed_1884
            PAI: PAE3227(gltD) PAE3444
            PIS: Pisl_1811
            PCL: Pcal_1608
            PAS: Pars_1101
STRUCTURES  PDB: 1EA0  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.13
            ExPASy - ENZYME nomenclature database: 1.4.1.13
            ExplorEnz - The Enzyme Database: 1.4.1.13
            ERGO genome analysis and discovery system: 1.4.1.13
            BRENDA, the Enzyme Database: 1.4.1.13
            CAS: 37213-53-9
///
ENTRY       EC 1.4.1.14                 Enzyme
NAME        glutamate synthase (NADH);
            glutamate (reduced nicotinamide adenine dinucleotide) synthase;
            NADH: GOGAT;
            L-glutamate synthase (NADH);
            L-glutamate synthetase;
            NADH-glutamate synthase;
            NADH-dependent glutamate synthase;
            glutamate synthase (NADH)
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-glutamate:NAD+ oxidoreductase (transaminating)
REACTION    2 L-glutamate + NAD+ = L-glutamine + 2-oxoglutarate + NADH + H+
            [RN:R00093]
ALL_REAC    R00093
SUBSTRATE   L-glutamate [CPD:C00025];
            NAD+ [CPD:C00003]
PRODUCT     L-glutamine [CPD:C00064];
            2-oxoglutarate [CPD:C00026];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COFACTOR    FMN [CPD:C00061]
COMMENT     A flavoprotein (FMN).
REFERENCE   1  [PMID:21790]
  AUTHORS   Boland MJ, Benny AG.
  TITLE     Enzymes of nitrogen metabolism in legume nodules. Purification and
            properties of NADH-dependent glutamate synthase from lupin nodules.
  JOURNAL   Eur. J. Biochem. 79 (1977) 355-62.
  ORGANISM  Lupinus angustifolius
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00267  glutamate synthase (NADH)
            KO: K00268  glutamate synthase (NADH) large chain
            KO: K00269  glutamate synthase (NADH) small chain
GENES       OSA: 4339561
            PHA: PSHAb0128(gltD)
            ADE: Adeh_0818
            SAV: SAV0473(gltD)
            SAR: SAR0472(gltB)
            DSY: DSY4384
            FAL: FRAAL4964(gltD)
            SYN: sll1027(gltD) sll1502(gltB)
            HMA: rrnAC0169(gltB)
            NPH: NP1794A(gltB)
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.14
            ExPASy - ENZYME nomenclature database: 1.4.1.14
            ExplorEnz - The Enzyme Database: 1.4.1.14
            ERGO genome analysis and discovery system: 1.4.1.14
            BRENDA, the Enzyme Database: 1.4.1.14
            CAS: 65589-88-0
///
ENTRY       EC 1.4.1.15                 Enzyme
NAME        lysine dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-lysine:NAD+ oxidoreductase (deaminating, cyclizing)
REACTION    L-lysine + NAD+ = 1,2-didehydropiperidine-2-carboxylate + NH3 + NADH
            + H+ [RN:R00445]
ALL_REAC    R00445;
            (other) R00145 R00146
SUBSTRATE   L-lysine [CPD:C00047];
            NAD+ [CPD:C00003]
PRODUCT     1,2-didehydropiperidine-2-carboxylate [CPD:C01258];
            NH3 [CPD:C00014];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4291003]
  AUTHORS   Burgi W, Richterich R, Colombo JP.
  TITLE     L-Lysine dehydrogenase deficiency in a patient with congenital
            lysine intolerance.
  JOURNAL   Nature. 211 (1966) 854-5.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.15
            ExPASy - ENZYME nomenclature database: 1.4.1.15
            ExplorEnz - The Enzyme Database: 1.4.1.15
            ERGO genome analysis and discovery system: 1.4.1.15
            BRENDA, the Enzyme Database: 1.4.1.15
            CAS: 68073-29-0
///
ENTRY       EC 1.4.1.16                 Enzyme
NAME        diaminopimelate dehydrogenase;
            meso-alpha,epsilon-diaminopimelate dehydrogenase;
            meso-diaminopimelate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     meso-2,6-diaminoheptanedioate:NADP+ oxidoreductase (deaminating)
REACTION    meso-2,6-diaminoheptanedioate + H2O + NADP+ =
            L-2-amino-6-oxoheptanedioate + NH3 + NADPH + H+ [RN:R02755]
ALL_REAC    R02755
SUBSTRATE   meso-2,6-diaminoheptanedioate [CPD:C00680];
            H2O [CPD:C00001];
            NADP+ [CPD:C00006]
PRODUCT     L-2-amino-6-oxoheptanedioate [CPD:C03871];
            NH3 [CPD:C00014];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:10904]
  AUTHORS   Misono H, Togawa H, Yamamoto T, Soda K.
  TITLE     Occurrence of meso-alpha, epsilon-diaminopimelate dehydrogenase in
            Bacillus sphaericus.
  JOURNAL   Biochem. Biophys. Res. Commun. 72 (1976) 89-93.
  ORGANISM  Bacillus sphaericus
REFERENCE   2  [PMID:762012]
  AUTHORS   Misono H, Togawa H, Yamamoto T, Soda K.
  TITLE     Meso-alpha,epsilon-diaminopimelate D-dehydrogenase: distribution and
            the reaction product.
  JOURNAL   J. Bacteriol. 137 (1979) 22-7.
  ORGANISM  Bacillus sphaericus, Brevibacterium sp., Corynebacterium glutamicum,
            Proteus vulgaris
PATHWAY     PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K03340  diaminopimelate dehydrogenase
GENES       PRW: PsycPRwf_0683
            AJS: Ajs_2757
            HAR: HEAR2481
            CCO: CCC13826_1251
            PCA: Pcar_2787
            STH: STH1425
            CTC: CTC02532
            CNO: NT01CX_0433
            CTH: Cthe_0922
            DSY: DSY0242
            SWO: Swol_0940
            CGL: NCgl2528(cgl2617)
            CGB: cg2900(ddh)
            CEF: CE2498(ddh)
            BTH: BT_1979
            BFR: BF3690
            BFS: BF3481
            PGI: PG0806
            MVN: Mevan_0344
STRUCTURES  PDB: 1DAP  1F06  2DAP  3DAP  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.16
            ExPASy - ENZYME nomenclature database: 1.4.1.16
            ExplorEnz - The Enzyme Database: 1.4.1.16
            ERGO genome analysis and discovery system: 1.4.1.16
            BRENDA, the Enzyme Database: 1.4.1.16
            CAS: 60894-21-5
///
ENTRY       EC 1.4.1.17                 Enzyme
NAME        N-methylalanine dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N-methyl-L-alanine:NADP+ oxidoreductase (demethylating, deaminating)
REACTION    N-methyl-L-alanine + H2O + NADP+ = pyruvate + methylamine + NADPH +
            H+ [RN:R01584]
ALL_REAC    R01584
SUBSTRATE   N-methyl-L-alanine [CPD:C02721];
            H2O [CPD:C00001];
            NADP+ [CPD:C00006]
PRODUCT     pyruvate [CPD:C00022];
            methylamine [CPD:C00218];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:236301]
  AUTHORS   Lin MC, Wagner C.
  TITLE     Purification and characterization of N-methylalanine dehydrogenase.
  JOURNAL   J. Biol. Chem. 250 (1975) 3746-51.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.17
            ExPASy - ENZYME nomenclature database: 1.4.1.17
            ExplorEnz - The Enzyme Database: 1.4.1.17
            ERGO genome analysis and discovery system: 1.4.1.17
            BRENDA, the Enzyme Database: 1.4.1.17
            CAS: 56379-51-2
///
ENTRY       EC 1.4.1.18                 Enzyme
NAME        lysine 6-dehydrogenase;
            L-lysine epsilon-dehydrogenase;
            L-lysine 6-dehydrogenase;
            LysDH
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-lysine:NAD+ 6-oxidoreductase (deaminating)
REACTION    (1) (1a) L-lysine + NAD+ + H2O = (S)-2-amino-6-oxohexanoate + NADH +
            H+ + NH3 [RN:R00446];
            (2) (1b) (S)-2-amino-6-oxohexanoate =
            (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O (spontaneous)
ALL_REAC    R00446
SUBSTRATE   L-lysine [CPD:C00047];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001];
            (S)-2-amino-6-oxohexanoate
PRODUCT     (S)-2-amino-6-oxohexanoate;
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            NH3 [CPD:C00014];
            (S)-2,3,4,5-tetrahydropyridine-2-carboxylate;
            H2O [CPD:C00001]
COMMENT     The enzyme is highly specific for L-lysine as substrate, although
            (S)-(beta-aminoethyl)-L-cysteine can act as a substrate, but more
            slowly. While the enzyme from Agrobacterium tumefaciens can use only
            NAD+, that from the thermophilic bacterium Geobacillus
            stearothermophilus can also use NADP+, but more slowly [1,4].
REFERENCE   1  [PMID:6801024]
  AUTHORS   Misono H, Nagasaki S.
  TITLE     Occurrence of L-lysine epsilon-dehydrogenase in Agrobacterium
            tumefaciens.
  JOURNAL   J. Bacteriol. 150 (1982) 398-401.
REFERENCE   2
  AUTHORS   Misono, H., Uehigashi, H., Morimoto, E. and Nagasaki, S.
  TITLE     Purification and properties of L-lysine epsilon-dehydrogenase from
            Agrobacterium tumefaciens.
  JOURNAL   Agric. Biol. Chem. 49 (1985) 2253-2255.
  ORGANISM  Agrobacterium tumefaciens
REFERENCE   3  [PMID:2768207]
  AUTHORS   Misono H, Hashimoto H, Uehigashi H, Nagata S, Nagasaki S.
  TITLE     Properties of L-lysine epsilon-dehydrogenase from Agrobacterium
            tumefaciens.
  JOURNAL   J. Biochem. (Tokyo). 105 (1989) 1002-8.
REFERENCE   4  [PMID:14766574]
  AUTHORS   Heydari M, Ohshima T, Nunoura-Kominato N, Sakuraba H.
  TITLE     Highly stable L-lysine 6-dehydrogenase from the thermophile
            Geobacillus stearothermophilus isolated from a Japanese hot spring:
            characterization, gene cloning and sequencing, and expression.
  JOURNAL   Appl. Environ. Microbiol. 70 (2004) 937-42.
GENES       APE: APE_0193.1
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.18
            ExPASy - ENZYME nomenclature database: 1.4.1.18
            ExplorEnz - The Enzyme Database: 1.4.1.18
            ERGO genome analysis and discovery system: 1.4.1.18
            BRENDA, the Enzyme Database: 1.4.1.18
            CAS: 89400-30-6
///
ENTRY       EC 1.4.1.19                 Enzyme
NAME        tryptophan dehydrogenase;
            NAD(P)+-L-tryptophan dehydrogenase;
            L-tryptophan dehydrogenase;
            L-Trp-dehydrogenase;
            TDH
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-tryptophan:NAD(P)+ oxidoreductase (deaminating)
REACTION    L-tryptophan + NAD(P)+ + H2O = (indol-3-yl)pyruvate + NH3 + NAD(P)H
            + H+ [RN:R00675 R00676]
ALL_REAC    R00675 R00676;
            (other) R00145 R00146
SUBSTRATE   L-tryptophan [CPD:C00078];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     (indol-3-yl)pyruvate [CPD:C00331];
            NH3 [CPD:C00014];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
EFFECTOR    Calcium [CPD:C00076]
COMMENT     Activated by Ca2+.
REFERENCE   1
  AUTHORS   Vackova, K., Mehta, A. and Kutacek, M.
  TITLE     Tryptophan aminotransferase and tryptophan dehydrogenase -
            activities in some cell compartments of spinach leaves - the effect
            of calcium-ions on tryptophan dehydrogenase.
  JOURNAL   Biol. Plant. 27 (1985) 154-158.
  ORGANISM  spinach
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.19
            ExPASy - ENZYME nomenclature database: 1.4.1.19
            ExplorEnz - The Enzyme Database: 1.4.1.19
            ERGO genome analysis and discovery system: 1.4.1.19
            BRENDA, the Enzyme Database: 1.4.1.19
            CAS: 94047-13-9
///
ENTRY       EC 1.4.1.20                 Enzyme
NAME        phenylalanine dehydrogenase;
            L-phenylalanine dehydrogenase;
            PHD
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-phenylalanine:NAD+ oxidoreductase (deaminating)
REACTION    L-phenylalanine + H2O + NAD+ = phenylpyruvate + NH3 + NADH + H+
            [RN:R00688]
ALL_REAC    R00688;
            (other) R00145 R00146
SUBSTRATE   L-phenylalanine [CPD:C00079];
            H2O [CPD:C00001];
            NAD+ [CPD:C00003]
PRODUCT     phenylpyruvate [CPD:C00166];
            NH3 [CPD:C00014];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The enzymes from Bacillus badius and Sporosarcina ureae are highly
            specific for L-phenylalanine; that from Bacillus sphaericus also
            acts on L-tyrosine.
REFERENCE   1  [PMID:3112142]
  AUTHORS   Asano Y, Nakazawa A, Endo K.
  TITLE     Novel phenylalanine dehydrogenases from Sporosarcina ureae and
            Bacillus sphaericus. Purification and characterization.
  JOURNAL   J. Biol. Chem. 262 (1987) 10346-54.
  ORGANISM  Sporosarcina ureae, Bacillus sphaericus
REFERENCE   2  [PMID:3311741]
  AUTHORS   Asano Y, Nakazawa A, Endo K, Hibino Y, Ohmori M, Numao N, Kondo K.
  TITLE     Phenylalanine dehydrogenase of Bacillus badius. Purification,
            characterization and gene cloning.
  JOURNAL   Eur. J. Biochem. 168 (1987) 153-9.
  ORGANISM  Bacillus badius
PATHWAY     PATH: map00360  Phenylalanine metabolism
            PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K00270  phenylalanine dehydrogenase
GENES       OIH: OB2878
            GKA: GK2031(pdh)
            RHA: RHA1_ro01628
STRUCTURES  PDB: 1BW9  1BXG  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.20
            ExPASy - ENZYME nomenclature database: 1.4.1.20
            ExplorEnz - The Enzyme Database: 1.4.1.20
            ERGO genome analysis and discovery system: 1.4.1.20
            BRENDA, the Enzyme Database: 1.4.1.20
            CAS: 69403-12-9
///
ENTRY       EC 1.4.1.21                 Enzyme
NAME        aspartate dehydrogenase;
            NAD-dependent aspartate dehydrogenase;
            NADH2-dependent aspartate dehydrogenase;
            NADP+-dependent aspartate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-aspartate:NAD(P)+ oxidoreductase (deaminating)
REACTION    L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H + H+
            [RN:R07164 R07165]
ALL_REAC    R07164 R07165;
            (other) R07407 R07410
SUBSTRATE   L-aspartate [CPD:C00049];
            H2O [CPD:C00001];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     oxaloacetate [CPD:C00036];
            NH3 [CPD:C00014];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The enzyme is strictly specific for L-aspartate as substrate.
            Catalyses the first step in NAD biosynthesis from aspartate. The
            enzyme has a higher affinity for NAD+ than NADP+ [1].
REFERENCE   1  [PMID:12496312]
  AUTHORS   Yang Z, Savchenko A, Yakunin A, Zhang R, Edwards A, Arrowsmith C,
            Tong L.
  TITLE     Aspartate dehydrogenase, a novel enzyme identified from structural
            and functional studies of TM1643.
  JOURNAL   J. Biol. Chem. 278 (2003) 8804-8.
  ORGANISM  Thermotoga maritima [GN:tma]
REFERENCE   2  [PMID:9819709]
  AUTHORS   Okamura T, Noda H, Fukuda S, Ohsugi M.
  TITLE     Aspartate dehydrogenase in vitamin B12-producing Klebsiella
            pneumoniae IFO 13541.
  JOURNAL   J. Nutr. Sci. Vitaminol. (Tokyo). 44 (1998) 483-90.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   3
  AUTHORS   Kretovich, W.L., Kariakina, T.I., Weinova, M.K., Sidelnikova, L.I.
            and Kazakova, O.W.
  TITLE     The synthesis of aspartic acid in Rhizobium lupini bacteroids.
  JOURNAL   Plant Soil 61 (1981) 145-156.
  ORGANISM  Rhizobium lupini
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K06989  aspartate dehydrogenase
GENES       DRE: 447919(zgc:103722)
            SPE: Spro_3958
            PAE: PA3505
            PCR: Pcryo_1256
            ACI: ACIAD0997
            PHA: PSHAb0019
            CSA: Csal_0141
            RSO: RS01727(RSp0722)
            REU: Reut_B3576
            BMA: BMAA1329
            BXE: Bxe_B0182
            BUR: Bcep18194_B1112
            BCN: Bcen_3665
            BCH: Bcen2424_4702
            BPS: BPSS0903
            BPM: BURPS1710b_A2501
            BTE: BTH_II1494
            BPE: BP1922
            BPA: BPP2295
            BBR: BB1747 BB4781
            POL: Bpro_3686
            MES: Meso_0824
            OAN: Oant_4396
            BJA: bll6567
            RPB: RPB_0147 RPB_3108
            SIL: SPO2880
            SIT: TM1040_1595
            JAN: Jann_1451
            RDE: RD1_3642
            TMA: TM1643
            TPT: Tpet_1148
            TME: Tmel_1582
            MJA: MJ0915
            MMP: MMP0737
            MMZ: MmarC7_1758
            MAE: Maeo_0848
            MVN: Mevan_1607
            MAC: MA0958
            MBA: Mbar_A1866
            MMA: MM_2072
            MBU: Mbur_1681
            MHU: Mhun_2354
            MTH: MTH973
            MST: Msp_1148
            MSI: Msm_0464
            MKA: MK0094
            AFU: AF1838
            IHO: Igni_1349
STRUCTURES  PDB: 2DC1  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.21
            ExPASy - ENZYME nomenclature database: 1.4.1.21
            ExplorEnz - The Enzyme Database: 1.4.1.21
            ERGO genome analysis and discovery system: 1.4.1.21
            BRENDA, the Enzyme Database: 1.4.1.21
            CAS: 37278-97-0
///
ENTRY       EC 1.4.1.22       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: ornithine cyclodeaminase. It was pointed out during
            the public-review process that there is no overall consumption of
            NAD+ during the reaction. As a result, transfer of the enzyme from
            EC 4.3.1.12 was not necessary and EC 1.4.1.22 was withdrawn before
            being made official. (EC 1.4.1.22 created 2006, deleted 2006)
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.1.22
            ExPASy - ENZYME nomenclature database: 1.4.1.22
            ExplorEnz - The Enzyme Database: 1.4.1.22
            ERGO genome analysis and discovery system: 1.4.1.22
            BRENDA, the Enzyme Database: 1.4.1.22
///
ENTRY       EC 1.4.1.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With NAD+ or NADP+ as acceptor
REACTION    3-Sulfino-L-alanine + NAD+ + H2O <=> 3-Sulfinylpyruvate + NH3 + NADH
            + H+ [RN:R02618]
SUBSTRATE   3-Sulfino-L-alanine [CPD:C00606];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     3-Sulfinylpyruvate [CPD:C05527];
            NH3 [CPD:C00014];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
///
ENTRY       EC 1.4.2.1                  Enzyme
NAME        glycine dehydrogenase (cytochrome);
            glycine---cytochrome c reductase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With a cytochrome as acceptor
SYSNAME     glycine:ferricytochrome-c oxidoreductase (deaminating)
REACTION    glycine + H2O + 2 ferricytochrome c = glyoxylate + NH3 + 2
            ferrocytochrome c + 2 H+ [RN:R00364]
ALL_REAC    R00364
SUBSTRATE   glycine [CPD:C00037];
            H2O [CPD:C00001];
            ferricytochrome c [CPD:C00125]
PRODUCT     glyoxylate [CPD:C00048];
            NH3 [CPD:C00014];
            ferrocytochrome c [CPD:C00126];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:5016640]
  AUTHORS   Sanders HK, Becker GE, Nason A.
  TITLE     Glycine-cytochrome c reductase from Nitrobacter agilis.
  JOURNAL   J. Biol. Chem. 247 (1972) 2015-25.
  ORGANISM  Nitrobacter agilis
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.2.1
            ExPASy - ENZYME nomenclature database: 1.4.2.1
            ExplorEnz - The Enzyme Database: 1.4.2.1
            ERGO genome analysis and discovery system: 1.4.2.1
            BRENDA, the Enzyme Database: 1.4.2.1
            CAS: 9075-55-2
///
ENTRY       EC 1.4.2.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With a cytochrome as acceptor
REACTION    Taurine + H2O + 2 Ferricytochrome c <=> Sulfoacetaldehyde + NH3 + 2
            Ferrocytochrome c [RN:R01685]
SUBSTRATE   Taurine [CPD:C00245];
            H2O [CPD:C00001];
            Ferricytochrome c [CPD:C00125]
PRODUCT     Sulfoacetaldehyde [CPD:C00593];
            NH3 [CPD:C00014];
            Ferrocytochrome c [CPD:C00126]
///
ENTRY       EC 1.4.3.1                  Enzyme
NAME        D-aspartate oxidase;
            aspartic oxidase;
            D-aspartic oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     D-aspartate:oxygen oxidoreductase (deaminating)
REACTION    D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2 [RN:R00359]
ALL_REAC    R00359;
            (other) R06124
SUBSTRATE   D-aspartate [CPD:C00402];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     oxaloacetate [CPD:C00036];
            NH3 [CPD:C00014];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:6060479]
  AUTHORS   Dixon M, Kenworthy P.
  TITLE     D-aspartate oxidase of kidney.
  JOURNAL   Biochim. Biophys. Acta. 146 (1967) 54-76.
  ORGANISM  rabbit
REFERENCE   2
  AUTHORS   Still, J.L., Buell, M.V., Knox, W.E. and Green, D.E.
  TITLE     Studies on the cyclophorase system. VII. D-Aspartic oxidase.
  JOURNAL   J. Biol. Chem. 179 (1949) 831-837.
  ORGANISM  rabbit
REFERENCE   3
  AUTHORS   Still, J.L. and Sperling, E.
  TITLE     On the prosthetic group of the D-aspartic oxidase.
  JOURNAL   J. Biol. Chem. 182 (1950) 585-589.
  ORGANISM  rabbit
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
ORTHOLOGY   KO: K00272  D-aspartate oxidase
GENES       HSA: 8528(DDO)
            MMU: 70503(Ddo)
            CFA: 475026(DDO)
            BTA: 280763(DDO)
            SSC: 100037287(DDO)
            GGA: 770953(DDO)
            SPU: 582896(LOC582896)
            PIC: PICST_33517(IFG3) PICST_57912(DAO1)
            AOR: AO090023000258
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.1
            ExPASy - ENZYME nomenclature database: 1.4.3.1
            ExplorEnz - The Enzyme Database: 1.4.3.1
            ERGO genome analysis and discovery system: 1.4.3.1
            BRENDA, the Enzyme Database: 1.4.3.1
            CAS: 9029-20-3
///
ENTRY       EC 1.4.3.2                  Enzyme
NAME        L-amino-acid oxidase;
            ophio-amino-acid oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     L-amino-acid:oxygen oxidoreductase (deaminating)
REACTION    an L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2 [RN:R01259]
ALL_REAC    R01259 > R00357 R00648 R00677 R00689 R00729 R02197;
            (other) R06124
SUBSTRATE   L-amino acid [CPD:C00151];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     2-oxo acid [CPD:C00161];
            NH3 [CPD:C00014];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1
  AUTHORS   Meister, A. and Wellner, D.
  TITLE     Flavoprotein amino acid oxidase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 609-648.
REFERENCE   2
  AUTHORS   Wellner, D. and Meister, A.
  TITLE     Crystalline L-amino acid oxidase of Crotalus adamanteus.
  JOURNAL   J. Biol. Chem. 235 (1960) 2013-2018.
  ORGANISM  Crotalus adamanteus
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
            PATH: map00271  Methionine metabolism
            PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
            PATH: map00380  Tryptophan metabolism
            PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
            PATH: map00950  Alkaloid biosynthesis I
ORTHOLOGY   KO: K03334  L-amino-acid oxidase
GENES       AFM: AFUA_7G06810
            PCR: Pcryo_1780
            PRW: PsycPRwf_2357
            REH: H16_A0845(lao1) H16_A0856(lao2)
            RHA: RHA1_ro02017
            KRA: Krad_0085
            SEN: SACE_2785(lao2) SACE_4150(lao2) SACE_6018(lao2)
            LIL: LA4200
STRUCTURES  PDB: 1F8R  1F8S  1REO  1TDK  1TDN  1TDO  2IID  2JAE  2JB1  2JB2  
                 2JB3  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.2
            ExPASy - ENZYME nomenclature database: 1.4.3.2
            ExplorEnz - The Enzyme Database: 1.4.3.2
            ERGO genome analysis and discovery system: 1.4.3.2
            BRENDA, the Enzyme Database: 1.4.3.2
            CAS: 9000-89-9
///
ENTRY       EC 1.4.3.3                  Enzyme
NAME        D-amino-acid oxidase;
            ophio-amino-acid oxidase;
            L-amino acid:O2 oxidoreductase;
            new yellow enzyme
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     D-amino-acid:oxygen oxidoreductase (deaminating)
REACTION    a D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2 [RN:R01340]
ALL_REAC    R01340 > R02457 R02894 R02923 R05861 R07400;
            (other) R00366 R04221 R06124
SUBSTRATE   D-amino acid [CPD:C00405];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     2-oxo acid [CPD:C00161];
            NH3 [CPD:C00014];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Wide specificity for D-amino acids. Also acts
            on glycine.
REFERENCE   1  [PMID:14314378]
  AUTHORS   DIXON M, KLEPPE K.
  TITLE     D-AMINO ACID OXIDASE. I. DISSOCIATION AND RECOMBINATION OF THE
            HOLOENZYME.
  JOURNAL   Biochim. Biophys. Acta. 96 (1965) 357-67.
  ORGANISM  pig [GN:ssc]
REFERENCE   2
  AUTHORS   Dixon, M. and Kleppe, K.
  TITLE     D-Amino acid oxidase. II. Specificity, competitive inhibition and
            reaction sequence.
  JOURNAL   Biochim. Biophys. Acta 96 (1965) 368-382.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:14314379]
  AUTHORS   DIXON M, KLEPPE K.
  TITLE     D-AMINO ACID OXIDASE. 3. EFFECT OF PH.
  JOURNAL   Biochim. Biophys. Acta. 96 (1965) 383-9.
  ORGANISM  pig [GN:ssc]
REFERENCE   4
  AUTHORS   Massey, V., Palmer, G. and Bennett, R.
  TITLE     The purification and some properties of D-amino acid oxidase.
  JOURNAL   Biochim. Biophys. Acta 48 (1961) 1-9.
  ORGANISM  pig [GN:ssc]
REFERENCE   5
  AUTHORS   Meister, A. and Wellner, D.
  TITLE     Flavoprotein amino acid oxidase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 609-648.
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00311  Penicillin and cephalosporin biosynthesis
            PATH: map00330  Arginine and proline metabolism
            PATH: map00472  D-Arginine and D-ornithine metabolism
ORTHOLOGY   KO: K00273  D-amino-acid oxidase
GENES       HSA: 1610(DAO)
            MMU: 13142(Dao1)
            RNO: 114027(Dao1)
            CFA: 486317(DAO)
            SSC: 397134(DAO1)
            GGA: 416894(DAO)
            CEL: C47A10.5 F18E3.7
            AFM: AFUA_5G11290 AFUA_5G13940 AFUA_6G10230
            UMA: UM05703.1
            TET: TTHERM_00633280 TTHERM_00787140
            PAR: Psyc_1346
            AZO: azo1482(yfcK) azo1919
            PUB: SAR11_0547
            RLE: RL3590
            MTU: Rv1905c(aao)
            MTC: MT1956
            MBO: Mb1940c(aao)
            MBB: BCG_1944c(aao)
            NCA: Noca_1780
            RXY: Rxyl_0526
            PMB: A9601_19131
            PMC: P9515_18941
            PMF: P9303_30031
            PMG: P9301_18941
            PME: NATL1_21851
STRUCTURES  PDB: 1AN9  1C0I  1C0K  1C0P  1DAO  1DDO  1EVI  1KIF  1VE9  2DU8  
                 2E48  2E49  2E4A  2E82  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.3
            ExPASy - ENZYME nomenclature database: 1.4.3.3
            ExplorEnz - The Enzyme Database: 1.4.3.3
            ERGO genome analysis and discovery system: 1.4.3.3
            BRENDA, the Enzyme Database: 1.4.3.3
            CAS: 9000-88-8
///
ENTRY       EC 1.4.3.4                  Enzyme
NAME        amine oxidase (flavin-containing);
            monoamine oxidase;
            tyramine oxidase;
            tyraminase;
            amine oxidase;
            adrenalin oxidase;
            epinephrine oxidase;
            MAO;
            polyamine oxidase;
            serotonin deaminase;
            adrenaline oxidase;
            spermidine oxidase;
            spermine oxidase;
            monoamine:O2 oxidoreductase (deaminating)
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     amine:oxygen oxidoreductase (deaminating) (flavin-containing)
REACTION    RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 [RN:R01853]
ALL_REAC    R01853 > R02173 R02382 R02529 R02532 R02613 R02908 R04025 R04300
            R04674 R04890 R04893;
            (other) R02919 R04894 R04907 R04908 R06133
SUBSTRATE   RCH2NH2 [CPD:C00375];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     RCHO [CPD:C00071];
            NH3 [CPD:C00014];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Acts on primary amines, and usually also on
            some secondary and tertiary amines.
REFERENCE   1
  AUTHORS   Blaschko, H.
  TITLE     Amine oxidase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 8, Academic Press, New York, 1963, p. 337-351.
REFERENCE   2  [PMID:6061707]
  AUTHORS   Erwin VG, Hellerman L.
  TITLE     Mitochondrial monoamine oxidase. I. Purification and
            characterization of the bovine kidney enzyme.
  JOURNAL   J. Biol. Chem. 242 (1967) 4230-8.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:5657868]
  AUTHORS   Tipton KF.
  TITLE     The prosthetic groups of pig brain mitochondrial monoamine oxidase.
  JOURNAL   Biochim. Biophys. Acta. 159 (1968) 451-9.
  ORGANISM  pig [GN:ssc]
REFERENCE   4
  AUTHORS   Weaver, R.H. and Herbst, E.J.
  TITLE     The oxidation of polyamines by Neisseria perflava.
  JOURNAL   J. Biol. Chem. 231 (1958) 647-655.
  ORGANISM  Neisseria perflava
REFERENCE   5
  AUTHORS   Yamada, H. and Yasunobu, K.T.
  TITLE     Monoamine oxidase. I. Purification, crystallization, and properties
            of plasma monoamine oxidase.
  JOURNAL   J. Biol. Chem. 237 (1962) 1511-1516.
  ORGANISM  cow [GN:bta]
REFERENCE   6
  AUTHORS   Yamada, H. and Yasunobu, K.T.
  TITLE     Monoamine oxidase. II. Copper, one of the prosthetic groups of
            plasma monoamine oxidase.
  JOURNAL   J. Biol. Chem. 237 (1962) 3077-3082.
REFERENCE   7
  AUTHORS   Zeller, E.A.
  TITLE     Diamine oxidases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 8, Academic Press, New York, 1963, p. 313-335.
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00340  Histidine metabolism
            PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
            PATH: map00380  Tryptophan metabolism
ORTHOLOGY   KO: K00274  monoamine oxidase
GENES       HSA: 4128(MAOA) 4129(MAOB)
            MMU: 109731(Maob) 17161(Maoa)
            RNO: 25750(Maob)
            CFA: 403450(MAOA) 403451(MAOB)
            BTA: 281293(MAOA) 338445(MAOB)
            SSC: 414424(MAOA) 414909(MAOB)
            GGA: 418561(MAOB)
            XLA: 495197(LOC495197)
            DRE: 404730(mao)
            SPU: 583484(LOC583484) 590198(LOC590198) 760963(LOC760963)
            ANI: AN3291.2
            AFM: AFUA_3G00100
            AOR: AO090023000744 AO090103000118 AO090113000186
            ANG: An12g03290(maoN)
            CNE: CNL05890
            DDI: DDB_0231707(maoA)
            TET: TTHERM_00264690 TTHERM_00424660
            XCC: XCC3278
            XCB: XC_0886
            XCV: XCV3541
            XAC: XAC3426
            XOM: XOO_1119(XOO1119)
            PAU: PA14_05480
            PFO: Pfl_2742
            PEN: PSEEN5045
            PAR: Psyc_1152
            PCR: Pcryo_1131
            PAT: Patl_1720
            REU: Reut_C6401
            REH: H16_A0831(maoB)
            BXE: Bxe_B1535
            BUR: Bcep18194_C6829 Bcep18194_C6833
            BCN: Bcen_5037 Bcen_5048
            BCH: Bcen2424_5812 Bcen2424_5823
            AZO: azo2784
            BBA: Bd2540
            MLO: mll3668
            SME: SMb21110
            RET: RHE_PE00403
            RLE: pRL110538 pRL120187
            BRA: BRADO1842 BRADO2376
            BBT: BBta_2164 BBta_2728
            RPE: RPE_0041
            NWI: Nwi_0489
            RDE: RD1_0535
            MMR: Mmar10_0141
            SWI: Swit_4155
            BAN: BA1924 BA2018
            BAR: GBAA1924 GBAA2018
            BAA: BA_2428 BA_2522
            BAT: BAS1785 BAS1876
            BCE: BC1925 BC2016
            BCA: BCE_2008 BCE_2098
            BCZ: BCZK1742 BCZK1830
            BTK: BT9727_1764 BT9727_1846
            MTU: Rv3170(aofH)
            MTC: MT3259
            MBO: Mb3195(aofH)
            MBB: BCG_3194(aofH)
            MPA: MAP3228
            MSM: MSMEG_2035
            MVA: Mvan_5578
            MGI: Mflv_1230
            MMC: Mmcs_1556
            MKM: Mkms_1580
            MJL: Mjls_1526
            NFA: nfa26430 nfa30780
            RHA: RHA1_ro01769 RHA1_ro05707
            NCA: Noca_4000
            SEN: SACE_4116(aofH) SACE_4854
            SYF: Synpcc7942_0369
            SYD: Syncc9605_0745 Syncc9605_1906
            TER: Tery_1366
            SRU: SRU_0427
            CHU: CHU_0994(maoC)
            GFO: GFO_1974
            DGE: Dgeo_1827
STRUCTURES  PDB: 1DYU  1GOS  1JRQ  1O5W  1OJ9  1OJA  1OJB  1OJC  1OJD  1QAF  
                 1QAK  1QAL  1S2Q  1S2Y  1S3B  1S3E  2BK3  2BK4  2BK5  2BXR  
                 2BXS  2BYB  2C64  2C65  2C66  2C67  2C70  2C72  2C73  2C75  
                 2C76  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.4
            ExPASy - ENZYME nomenclature database: 1.4.3.4
            ExplorEnz - The Enzyme Database: 1.4.3.4
            ERGO genome analysis and discovery system: 1.4.3.4
            BRENDA, the Enzyme Database: 1.4.3.4
            CAS: 9001-66-5
///
ENTRY       EC 1.4.3.5                  Enzyme
NAME        pyridoxal 5'-phosphate synthase;
            pyridoxamine 5'-phosphate oxidase;
            pyridoxamine phosphate oxidase;
            pyridoxine (pyridoxamine)phosphate oxidase;
            pyridoxine (pyridoxamine) 5'-phosphate oxidase;
            pyridoxaminephosphate oxidase (EC 1.4.3.5: deaminating);
            PMP oxidase;
            pyridoxol-5'-phosphate:oxygen oxidoreductase (deaminating)
            (incorrect);
            pyridoxamine-phosphate oxidase;
            PdxH
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     pyridoxamine-5'-phosphate:oxygen oxidoreductase (deaminating)
REACTION    (1) pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate +
            NH3 + H2O2 [RN:R00277];
            (2) pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2
            [RN:R00278]
ALL_REAC    R00277 R00278;
            (other) R01710 R01711 R06133
SUBSTRATE   pyridoxamine 5'-phosphate [CPD:C00647];
            H2O [CPD:C00001];
            O2 [CPD:C00007];
            pyridoxine 5'-phosphate [CPD:C00627]
PRODUCT     pyridoxal 5'-phosphate [CPD:C00018];
            NH3 [CPD:C00014];
            H2O2 [CPD:C00027]
COFACTOR    FMN [CPD:C00061]
COMMENT     A flavoprotein (FMN). In Escherichia coli, the coenzyme pyridoxal
            5'-phosphate is synthesized de novo by a pathway that involves EC
            1.2.1.72 (erythrose-4-phosphate dehydrogenase), EC 1.1.1.290
            (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine
            transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate
            dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and
            EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate).
            N4'-Substituted pyridoxamine derivatives are also oxidized in
            reaction (1) to form pyridoxal 5'-phosphate and the corresponding
            primary amine.
REFERENCE   1  [PMID:6822512]
  AUTHORS   Choi JD, Bowers-Komro M, Davis MD, Edmondson DE, McCormick DB.
  TITLE     Kinetic properties of pyridoxamine (pyridoxine)-5'-phosphate oxidase
            from rabbit liver.
  JOURNAL   J. Biol. Chem. 258 (1983) 840-5.
  ORGANISM  rabbit
REFERENCE   2  [PMID:13782387]
  AUTHORS   WADA H, SNELL EE.
  TITLE     The enzymatic oxidation of pyridoxine and pyridoxamine phosphates.
  JOURNAL   J. Biol. Chem. 236 (1961) 2089-95.
  ORGANISM  rabbit
REFERENCE   3  [PMID:7696318]
  AUTHORS   Notheis C, Drewke C, Leistner E.
  TITLE     Purification and characterization of the
            pyridoxol-5'-phosphate:oxygen oxidoreductase (deaminating) from
            Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 1247 (1995) 265-71.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:10225425]
  AUTHORS   Laber B, Maurer W, Scharf S, Stepusin K, Schmidt FS.
  TITLE     Vitamin B6 biosynthesis: formation of pyridoxine 5'-phosphate from
            4-(phosphohydroxy)-L-threonine and 1-deoxy-D-xylulose-5-phosphate by
            PdxA and PdxJ protein.
  JOURNAL   FEBS. Lett. 449 (1999) 45-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:12824491]
  AUTHORS   Musayev FN, Di Salvo ML, Ko TP, Schirch V, Safo MK.
  TITLE     Structure and properties of recombinant human pyridoxine
            5'-phosphate oxidase.
  JOURNAL   Protein. Sci. 12 (2003) 1455-63.
  ORGANISM  human [GN:hsa]
REFERENCE   6  [PMID:15858270]
  AUTHORS   Safo MK, Musayev FN, Schirch V.
  TITLE     Structure of Escherichia coli pyridoxine 5'-phosphate oxidase in a
            tetragonal crystal form: insights into the mechanistic pathway of
            the enzyme.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 61 (2005) 599-604.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00750  Vitamin B6 metabolism
ORTHOLOGY   KO: K00275  pyridoxamine 5'-phosphate oxidase
GENES       HSA: 55163(PNPO)
            MMU: 103711(Pnpo)
            RNO: 64533(Pnpo)
            CFA: 480540(PNPO)
            XLA: 444757(MGC84800)
            SPU: 579975(LOC579975)
            CEL: F57B9.1
            SCE: YBR035C(PDX3)
            AGO: AGOS_AAR186W
            PIC: PICST_50793(PDX3)
            CGR: CAGL0I04708g
            SPO: SPAC1093.02
            AFM: AFUA_5G10650
            AOR: AO090010000473 AO090023000033
            DDI: DDB_0231657
            ECO: b1638(pdxH)
            ECJ: JW1630(pdxH)
            ECE: Z2652(pdxH)
            ECS: ECs2347
            ECC: c2030(pdxH)
            ECI: UTI89_C1829(pdxH)
            ECP: ECP_1584
            ECV: APECO1_721(pdxH)
            ECW: EcE24377A_1848(pdxH)
            ECX: EcHS_A1714
            STY: STY1674(pdxH)
            STT: t1316(pdxH)
            SPT: SPA1405(pdxH)
            SEC: SC1466(pdxH)
            STM: STM1448(pdxH)
            YPE: YPO2370(pdxH)
            YPK: y1965(pdxH)
            YPM: YP_2156(pdxH)
            YPA: YPA_1716
            YPN: YPN_1827
            YPP: YPDSF_0776
            YPS: YPTB2284(pdxH)
            YPI: YpsIP31758_1772(pdxH)
            SFL: SF1663(pdxH)
            SFX: S1795(pdxH)
            SFV: SFV_1655(pdxH)
            SSN: SSON_1518(pdxH)
            SBO: SBO_1496(pdxH)
            SDY: SDY_1861(pdxH)
            ECA: ECA1935(pdxH)
            PLU: plu2597(pdxH)
            WBR: WGLp337(pdxH)
            SGL: SG1447
            ENT: Ent638_1810
            SPE: Spro_2218
            BFL: Bfl370(pdxH)
            BPN: BPEN_381(pdxH)
            HIT: NTHI1032(pdxH)
            HIP: CGSHiEE_07725
            HDU: HD0214(pdxH)
            MSU: MS2064(pdxH)
            APL: APL_2009(pdxH)
            ASU: Asuc_0247
            XFA: XF1337
            XFT: PD0583(pdxH)
            XCC: XCC2840(pdxH)
            XCB: XC_1267 XC_1270
            XCV: XCV3159(pdxH)
            XAC: XAC3009(pdxH)
            XOO: XOO1245(pdxH)
            XOM: XOO_1145(XOO1145)
            VCH: VCA1079
            VCO: VC0395_0163(pdxH)
            VVU: VV2_1122
            VVY: VVA1648
            VPA: VPA1730
            VFI: VFA1161
            PPR: PBPRB2015(pdxH)
            PAE: PA1049(pdxH)
            PAU: PA14_50800(pdxH)
            PAP: PSPA7_4331(pdxH)
            PPU: PP_1129(pdxH)
            PPF: Pput_1165
            PST: PSPTO_4116(pdxH)
            PSB: Psyr_3853
            PSP: PSPPH_1409(pdxH)
            PFL: PFL_1283(pdxH)
            PFO: Pfl_1229
            PEN: PSEEN1277
            PMY: Pmen_1436
            PAR: Psyc_1358(pdxH)
            PCR: Pcryo_1007
            PRW: PsycPRwf_1259
            ACI: ACIAD3501(pdxH)
            SON: SO_2895(pdxH)
            SDN: Sden_1170 Sden_2277
            SFR: Sfri_1702
            SAZ: Sama_1961
            SBL: Sbal_1770
            SBM: Shew185_1763
            SLO: Shew_1622
            SPC: Sputcn32_1649
            SSE: Ssed_2606
            SPL: Spea_2477
            SHE: Shewmr4_1559
            SHM: Shewmr7_1634
            SHN: Shewana3_1626
            SHW: Sputw3181_2377
            ILO: IL1209(pdxH)
            CPS: CPS_1053(pdxH)
            PHA: PSHAa0658(pdxH)
            PAT: Patl_3147
            SDE: Sde_2258
            PIN: Ping_1481
            MAQ: Maqu_0155
            CBU: CBU_0928(pdxH)
            CBD: COXBU7E912_1146(pdxH)
            LPN: lpg0536(pdxH) lpg2139
            LPF: lpl0582(pdxH) lpl2068
            LPP: lpp0601(pdxH) lpp2078
            TCX: Tcr_0363 Tcr_1992
            AEH: Mlg_1988
            HHA: Hhal_1782
            HCH: HCH_04530(pdxH)
            CSA: Csal_1900
            ABO: ABO_0302(pdxH)
            MMW: Mmwyl1_2993
            AHA: AHA_1408(pdxH)
            DNO: DNO_1023(pdxH)
            BCI: BCI_0082(pdxH)
            RMA: Rmag_0434
            VOK: COSY_0404(pdxH)
            NME: NMB1360
            NMA: NMA1572(pdxH)
            NMC: NMC1295(pdxH)
            NGO: NGO0658
            CVI: CV_0059(pdxH)
            RSO: RSc0767(pdxH1) RSp0678(pdxH2)
            REU: Reut_A0815
            REH: H16_A2802(pdxH)
            RME: Rmet_2642
            BMA: BMA0359(pdxH)
            BMV: BMASAVP1_A0659(pdxH)
            BML: BMA10299_A2494(pdxH)
            BMN: BMA10247_0107(pdxH)
            BXE: Bxe_A0741
            BVI: Bcep1808_2662
            BUR: Bcep18194_A5900 Bcep18194_B1572
            BCN: Bcen_1957
            BCH: Bcen2424_2568
            BAM: Bamb_2616
            BPS: BPSL0854(pdxH)
            BPM: BURPS1710b_1061(pdxH)
            BPL: BURPS1106A_0904(pdxH)
            BPD: BURPS668_0901(pdxH)
            BTE: BTH_I0717(pdxH)
            PNU: Pnuc_0663
            BPE: BP3251(pdxH)
            BPA: BPP3607(pdxH)
            BBR: BB4042(pdxH)
            RFR: Rfer_2059
            POL: Bpro_3559
            PNA: Pnap_2989
            AAV: Aave_2803
            AJS: Ajs_2058
            VEI: Veis_2564
            MPT: Mpe_A2931
            HAR: HEAR2598(pdxH)
            MMS: mma_2836
            ABU: Abu_1541(pdxH)
            BBA: Bd2568(pdxH)
            ADE: Adeh_1455
            AFW: Anae109_1699
            MXA: MXAN_1295(pdxH)
            WOL: WD1159(pdxH)
            AMA: AM281(pdxH)
            APH: APH_1008(pdxH)
            ERU: Erum1850(pdxH)
            ERW: ERWE_CDS_01840(pdxH)
            ERG: ERGA_CDS_01790(pdxH)
            ECN: Ecaj_0183
            ECH: ECH_0931(pdxH)
            NSE: NSE_0371
            PUB: SAR11_0613(pdxH)
            MLO: mll7454
            MES: Meso_0724
            PLA: Plav_0790
            SME: SMc00069(pdxH)
            SMD: Smed_0509
            ATU: Atu0760(pdxH)
            ATC: AGR_C_1381
            RET: RHE_CH00941(pdxH)
            RLE: RL1014(pdxH)
            BME: BMEI1517
            BMF: BAB1_0444(pdxH)
            BMS: BR0416(pdxH)
            BMB: BruAb1_0439(pdxH)
            BOV: BOV_0424(pdxH)
            OAN: Oant_0531
            BJA: bll2624(pdxH)
            BRA: BRADO2146(pdxH)
            BBT: BBta_2463(pdxH)
            RPA: RPA1196(pdxH)
            RPB: RPB_1205
            RPC: RPC_1136
            RPD: RPD_1307
            RPE: RPE_4594
            NWI: Nwi_0622
            NHA: Nham_0765
            BHE: BH04290(pdxH)
            BQU: BQ03480(pdxH)
            BBK: BARBAKC583_0394(pdxH)
            XAU: Xaut_2478
            CCR: CC_0918
            SIL: SPO2141
            SIT: TM1040_1148
            RSP: RSP_2345(pdxH)
            RSH: Rsph17029_1020
            RSQ: Rsph17025_1052
            JAN: Jann_2475
            RDE: RD1_3198(pdxH)
            PDE: Pden_0858 Pden_4662
            MMR: Mmar10_0857
            HNE: HNE_0824(pdxH)
            ZMO: ZMO0851(pdxH)
            NAR: Saro_0048
            SAL: Sala_0654
            SWI: Swit_4754
            ELI: ELI_13435
            GOX: GOX1988
            GBE: GbCGDNIH1_0226
            ACR: Acry_0829
            RRU: Rru_A2627
            MAG: amb0886
            MTU: Rv2607(pdxH)
            MTC: MT2682(pdxH)
            MBO: Mb2639(pdxH)
            MBB: BCG_2632(pdxH)
            MLE: ML2131(pdxH)
            MPA: MAP0828(pdxH)
            MAV: MAV_1017(pdxH)
            MSM: MSMEG_5675(pdxH)
            MVA: Mvan_5024
            MGI: Mflv_1727
            MMC: Mmcs_4458
            MKM: Mkms_4545
            MJL: Mjls_4840
            NFA: nfa6600
            RHA: RHA1_ro04994(pdxH) RHA1_ro05689
            SCO: SCO4387(SCD10.19c)
            SMA: SAV3858(pdxH1)
            CMI: CMM_2909
            NCA: Noca_0734
            TFU: Tfu_0248
            FRA: Francci3_0079
            FAL: FRAAL0106(pdxH)
            ACE: Acel_0116
            KRA: Krad_3597
            SEN: SACE_0641(pdxH)
            STP: Strop_0424
            RXY: Rxyl_2372
            RBA: RB10006(pdxH)
            LIL: LA1166(pdxH)
            LIC: LIC12520(pdxH)
            LBJ: LBJ_2141(pdxH)
            LBL: LBL_2135(pdxH)
            SYN: sll1440(pdxH)
            SYR: SynRCC307_1504
            SYX: SynWH7803_0817
            TEL: tll0331(pdxH)
            ANA: all1248
            AVA: Ava_0557
            PMT: PMT2199(pdxH)
            PMF: P9303_29241(pdxH)
            BTH: BT_1577
            BFR: BF1453
            BFS: BF1385(pdxH)
            PGI: PG1714(pdxH)
            SRU: SRU_0544(pdxH)
            CHU: CHU_1775(pdxH)
            GFO: GFO_1835(pdxH)
            FJO: Fjoh_4542
            FPS: FP1704(pdxH)
            RRS: RoseRS_0423
            RCA: Rcas_1067
            DRA: DR_0495
            DGE: Dgeo_0443
STRUCTURES  PDB: 1CI0  1DNL  1G76  1G77  1G78  1G79  1JNW  1WV4  2A2J  2HHZ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.5
            ExPASy - ENZYME nomenclature database: 1.4.3.5
            ExplorEnz - The Enzyme Database: 1.4.3.5
            ERGO genome analysis and discovery system: 1.4.3.5
            BRENDA, the Enzyme Database: 1.4.3.5
            CAS: 9029-21-4
///
ENTRY       EC 1.4.3.6                  Enzyme
NAME        amine oxidase (copper-containing);
            diamine oxidase;
            diamino oxhydrase;
            histaminase;
            amine oxidase;
            monoamine oxidase;
            amine oxidase (pyridoxal containing);
            benzylamine oxidase;
            histamine deaminase;
            histamine oxidase;
            Cu-amine oxidase;
            amine oxygen oxidoreductase;
            diamine:O2 oxidoreductase (deaminating);
            semicarbazide-sensitive amine oxidase;
            SSAO
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     amine:oxygen oxidoreductase (deaminating) (copper-containing)
REACTION    RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 [RN:R01853]
ALL_REAC    R01853 > R01151 R02150 R02173 R02382 R02529 R02613 R03139 R04300
            R05334 R06154 R06740;
            (other) R04027 R06133
SUBSTRATE   RCH2NH2 [CPD:C00375];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     RCHO [CPD:C00071];
            NH3 [CPD:C00014];
            H2O2 [CPD:C00027]
COFACTOR    Copper [CPD:C00070];
            PQQ [CPD:C00113]
COMMENT     A group of enzymes including those oxidizing primary monoamines,
            diamines and histamine. They are copper quinoproteins. One form of
            EC 1.3.1.15 orotate reductase (NADPH) from rat kidney also catalyses
            this reaction.
REFERENCE   1
  AUTHORS   Ameyama, M., Hayashi, M., Matsushita, K., Shinagawa, E. and Adachi,
            O.
  TITLE     Microbial-production of pyrroloquinoline quinone.
  JOURNAL   Agric. Biol. Chem. 48 (1984) 561-565.
  ORGANISM  pig [GN:ssc], cow [GN:bta], Aspergillus niger
REFERENCE   2  [PMID:13638253]
  AUTHORS   AUGUSTINSSON KB, OLSSON B.
  TITLE     Esterases in the milk and blood plasma of swine. I. Substrate
            specificity and electrophoresis studies.
  JOURNAL   Biochem. J. 71 (1959) 477-84.
  ORGANISM  pig [GN:ssc]
REFERENCE   3
  AUTHORS   Blaschko, H.
  TITLE     Amine oxidase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 8, Academic Press, New York, 1963, p. 337-351.
REFERENCE   4  [PMID:14224405]
  AUTHORS   BUFFONI F, BLASCHKO H.
  TITLE     BENZYLAMINE OXIDASE AND HISTAMINASE: PURIFICATION AND
            CRYSTALLIZATION OF AN ENZYME FROM PIG PLASMA.
  JOURNAL   Proc. R. Soc. Lond. B. Biol. Sci. 161 (1964) 153-67.
REFERENCE   5  [PMID:7337701]
  AUTHORS   Haywood GW, Large PJ.
  TITLE     Microbial oxidation of amines. Distribution, purification and
            properties of two primary-amine oxidases from the yeast Candida
            boidinii grown on amines as sole nitrogen source.
  JOURNAL   Biochem. J. 199 (1981) 187-201.
  ORGANISM  Candida boidinii
REFERENCE   6  [PMID:5888801]
  AUTHORS   McEwen CM Jr.
  TITLE     Human plasma monoamine oxidase. 1. Purification and identification.
  JOURNAL   J. Biol. Chem. 240 (1965) 2003-10.
  ORGANISM  human [GN:hsa]
REFERENCE   7  [PMID:4964016]
  AUTHORS   Mondovi B, Costa MT, Agro AF, Rotilio G.
  TITLE     Pyridoxal phosphate as a prosthetic group of pig kidney diamine
            oxidase.
  JOURNAL   Arch. Biochem. Biophys. 119 (1967) 373-81.
  ORGANISM  pig [GN:ssc]
REFERENCE   8
  AUTHORS   Yamada, H., Adachi, O. and Ogata, K.
  TITLE     Amine oxidases of microorganisms. Part II. Purification and
            crystallisation of amine oxidase of Aspergillus niger.
  JOURNAL   Agric. Biol. Chem. 29 (1965) 649-654.
  ORGANISM  Aspergillus niger
REFERENCE   9
  AUTHORS   Yamada, H., Adachi, O. and Ogata, K.
  TITLE     Amine oxidases of microorganisms. Part III. Properties of amine
            oxidase of Aspergillus niger.
  JOURNAL   Agric. Biol. Chem. 29 (1965) 864-869.
  ORGANISM  Aspergillus niger
REFERENCE   10
  AUTHORS   Yamada, H., Adachi, O. and Ogata, K.
  TITLE     Amine oxidases of microorganisms. Part IV. Further properties of
            amine oxidase of Aspergillus niger.
  JOURNAL   Agric. Biol. Chem. 29 (1965) 912-917.
  ORGANISM  Aspergillus niger
REFERENCE   11
  AUTHORS   Zeller, E.A.
  TITLE     Diamine oxidases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 8, Academic Press, New York, 1963, p. 313-335.
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00340  Histidine metabolism
            PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
            PATH: map00380  Tryptophan metabolism
            PATH: map00410  beta-Alanine metabolism
            PATH: map00960  Alkaloid biosynthesis II
ORTHOLOGY   KO: K00276  copper amine oxidase
GENES       HSA: 26(ABP1) 314(AOC2) 8639(AOC3)
            PTR: 454702(AOC3) 463895(ABP1)
            MMU: 11754(Aoc3) 237940(Aoc2) 76507(Abp1)
            RNO: 65029(Abp1)
            CFA: 475536(ABP1) 480511(LOC480511) 490957(AOC2)
            BTA: 281002(AOC3)
            ATH: AT2G42490 AT3G43670 AT4G14940(ATAO1)
            OSA: 4336153
            CME: CMI002C CMS002C CMT003C
            AGO: AGOS_AGL073W
            PIC: PICST_55523(AMO1) PICST_83878(AMO2)
            SPO: SPAC2E1P3.04 SPBC1289.16c SPBC8E4.06
            ANI: AN1586.2 AN6092.2 AN7641.2 AN8454.2
            AFM: AFUA_1G13440 AFUA_3G00680 AFUA_3G14590 AFUA_5G01470
                 AFUA_5G07360 AFUA_7G04180 AFUA_7G08470
            AOR: AO090003000356 AO090011000229 AO090103000401 AO090138000079
                 AO090701000307 AO090701000490
            ANG: An09g01550(AO-I)
            CNE: CNG01110
            UMA: UM03524.1
            ECO: b1386(tynA)
            ECJ: JW1381(tynA)
            ECW: EcE24377A_1571(tynA)
            ECX: EcHS_A1473(tynA)
            LPN: lpg2910(tynA)
            LPP: lpp2979
            MLO: mll6250
            RLE: RL3036
            BRA: BRADO6525
            BBT: BBta_1115
            RPB: RPB_1133
            SUS: Acid_0916
            MSM: MSMEG_2526 MSMEG_3847
            MVA: Mvan_2218 Mvan_3407
            MGI: Mflv_3126 Mflv_4125
            MMC: Mmcs_2000
            MKM: Mkms_2046
            MJL: Mjls_1981
            NFA: nfa27860
            RHA: RHA1_ro02608 RHA1_ro02834 RHA1_ro05597 RHA1_ro08476(maoA)
            ART: Arth_3502
            AAU: AAur_0579 AAur_1378(maoII) AAur_pTC20082 AAur_pTC20192
            CYA: CYA_1346
            CYB: CYB_2794
            ANA: alr3431
            AVA: Ava_3451
            TER: Tery_1383
            DRA: DR_B0101
            SSO: SSO1692(tynA)
            SAI: Saci_2182(tynA)
STRUCTURES  PDB: 1A2V  1AV4  1AVK  1AVL  1D6U  1D6Y  1D6Z  1EKM  1IQX  1IQY  
                 1IU7  1IVU  1IVV  1IVW  1IVX  1KSI  1LVN  1OAC  1PU4  1RJO  
                 1SIH  1SII  1SPU  1TU5  1UI7  1UI8  1US1  1W2Z  1W4N  1W5Z  
                 1W6C  1W6G  1WMN  1WMO  1WMP  2BT3  2C10  2C11  2CFD  2CFG  
                 2CFK  2CFL  2CFW  2CG0  2CG1  2CWT  2CWU  2CWV  2D1W  2OOV  
                 2OQE  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.6
            ExPASy - ENZYME nomenclature database: 1.4.3.6
            ExplorEnz - The Enzyme Database: 1.4.3.6
            ERGO genome analysis and discovery system: 1.4.3.6
            BRENDA, the Enzyme Database: 1.4.3.6
            CAS: 9001-53-0
///
ENTRY       EC 1.4.3.7                  Enzyme
NAME        D-glutamate oxidase;
            D-glutamic oxidase;
            D-glutamic acid oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     D-glutamate:oxygen oxidoreductase (deaminating)
REACTION    D-glutamate + H2O + O2 = 2-oxoglutarate + NH3 + H2O2 [RN:R00279]
ALL_REAC    R00279;
            (other) R06124
SUBSTRATE   D-glutamate [CPD:C00217];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     2-oxoglutarate [CPD:C00026];
            NH3 [CPD:C00014];
            H2O2 [CPD:C00027]
REFERENCE   1  [PMID:13583997]
  AUTHORS   ROCCA E, GHIRETTI F.
  TITLE     Purification and properties of D-glutamic acid oxidase from Octopus
            vulgaris Lam.
  JOURNAL   Arch. Biochem. Biophys. 77 (1958) 336-49.
  ORGANISM  Octopus vulgaris
REFERENCE   2  [PMID:4387700]
  AUTHORS   Urich K.
  TITLE     [D-Glutamate oxidase from the antennal gland of the crayfish
            Oronectes limosus: purification and characterization]
  JOURNAL   Z. Naturforsch. B. 23 (1968) 1508-11.
  ORGANISM  Orconectes limosus
PATHWAY     PATH: map00471  D-Glutamine and D-glutamate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.7
            ExPASy - ENZYME nomenclature database: 1.4.3.7
            ExplorEnz - The Enzyme Database: 1.4.3.7
            ERGO genome analysis and discovery system: 1.4.3.7
            BRENDA, the Enzyme Database: 1.4.3.7
            CAS: 37255-41-7
///
ENTRY       EC 1.4.3.8                  Enzyme
NAME        ethanolamine oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     ethanolamine:oxygen oxidoreductase (deaminating)
REACTION    ethanolamine + H2O + O2 = glycolaldehyde + NH3 + H2O2 [RN:R01469]
ALL_REAC    R01469;
            (other) R06133
SUBSTRATE   ethanolamine [CPD:C00189];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     glycolaldehyde [CPD:C00266];
            NH3 [CPD:C00014];
            H2O2 [CPD:C00027]
COFACTOR    Cobalt [CPD:C00175];
            Cobamide [CPD:C00210]
COMMENT     A cobamide-protein.
REFERENCE   1
  AUTHORS   Narrod, S.A. and Jakoby, W.B.
  TITLE     Metabolism of ethanolamine. An ethanolamine oxidase.
  JOURNAL   J. Biol. Chem. 239 (1964) 2189-2193.
  ORGANISM  Arthrobacter sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.8
            ExPASy - ENZYME nomenclature database: 1.4.3.8
            ExplorEnz - The Enzyme Database: 1.4.3.8
            ERGO genome analysis and discovery system: 1.4.3.8
            BRENDA, the Enzyme Database: 1.4.3.8
            CAS: 9013-00-7
///
ENTRY       EC 1.4.3.9        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
COMMENT     Deleted entry: tyramine oxidase. Now included with EC 1.4.3.4 amine
            oxidase (flavin-containing) (EC 1.4.3.9 created 1972, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.9
            ExPASy - ENZYME nomenclature database: 1.4.3.9
            ExplorEnz - The Enzyme Database: 1.4.3.9
            ERGO genome analysis and discovery system: 1.4.3.9
            BRENDA, the Enzyme Database: 1.4.3.9
///
ENTRY       EC 1.4.3.10                 Enzyme
NAME        putrescine oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     putrescine:oxygen oxidoreductase (deaminating)
REACTION    putrescine + O2 + H2O = 4-aminobutanal + NH3 + H2O2 [RN:R01151]
ALL_REAC    R01151;
            (other) R06133
SUBSTRATE   putrescine [CPD:C00134];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     4-aminobutanal [CPD:C00555];
            NH3 [CPD:C00014];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). 4-Aminobutanal condenses non-enzymically to
            1-pyrroline.
REFERENCE   1  [PMID:4341347]
  AUTHORS   DeSa RJ.
  TITLE     Putrescine oxidase from Micrococcus rubens. Purification and
            properties of the enzyme.
  JOURNAL   J. Biol. Chem. 247 (1972) 5527-34.
  ORGANISM  Micrococcus rubens
REFERENCE   2
  AUTHORS   Yamada, H.
  TITLE     Putrescine oxidase (Micrococcus rubens).
  JOURNAL   Methods Enzymol. 17B (1971) 726-730.
  ORGANISM  Micrococcus rubens
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K03343  putrescine oxidase
GENES       CGL: NCgl0220(cgl0223)
            RHA: RHA1_ro05606
            ART: Arth_0040
            AAU: AAur_0043(puo)
            KRA: Krad_0838
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.10
            ExPASy - ENZYME nomenclature database: 1.4.3.10
            ExplorEnz - The Enzyme Database: 1.4.3.10
            ERGO genome analysis and discovery system: 1.4.3.10
            BRENDA, the Enzyme Database: 1.4.3.10
            CAS: 9076-87-3
///
ENTRY       EC 1.4.3.11                 Enzyme
NAME        L-glutamate oxidase;
            glutamate (acceptor) dehydrogenase;
            glutamate oxidase;
            glutamic acid oxidase;
            glutamic dehydrogenase (acceptor);
            L-glutamic acid oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     L-glutamate:oxygen oxidoreductase (deaminating)
REACTION    L-glutamate + O2 + H2O = 2-oxoglutarate + NH3 + H2O2 [RN:R00250]
ALL_REAC    R00250;
            (other) R06124
SUBSTRATE   L-glutamate [CPD:C00025];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     2-oxoglutarate [CPD:C00026];
            NH3 [CPD:C00014];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).The enzyme from Azotobacter previously listed
            under this number, which did not produce H2O2, was a crude cell-free
            extract that probably contained catalase.
REFERENCE   1
  AUTHORS   Kusakabe, H., Midorikawa, Y., Fujishima, T., Kuninaka, A. and
            Yoshino, H.
  TITLE     Purification and properties of a new enzyme, L-glutamate oxidase,
            from Streptomyces sp X-119-6 grown on wheat bran.
  JOURNAL   Agric. Biol. Chem. 47 (1983) 1323-1328.
  ORGANISM  Streptomyces sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.11
            ExPASy - ENZYME nomenclature database: 1.4.3.11
            ExplorEnz - The Enzyme Database: 1.4.3.11
            ERGO genome analysis and discovery system: 1.4.3.11
            BRENDA, the Enzyme Database: 1.4.3.11
            CAS: 39346-34-4
///
ENTRY       EC 1.4.3.12                 Enzyme
NAME        cyclohexylamine oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     cyclohexylamine:oxygen oxidoreductase (deaminating)
REACTION    cyclohexylamine + O2 + H2O = cyclohexanone + NH3 + H2O2 [RN:R02233]
ALL_REAC    R02233;
            (other) R06133
SUBSTRATE   cyclohexylamine [CPD:C00571];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     cyclohexanone [CPD:C00414];
            NH3 [CPD:C00014];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Some other cyclic amines can act instead of
            cyclohexylamine, but not simple aliphatic and aromatic amides.
REFERENCE   1  [PMID:18451]
  AUTHORS   Tokieda T, Niimura T, Takamura F, Yamaha T.
  TITLE     Purification and some properties of cyclohexylamine oxidase from a
            Pseudomonas sp.
  JOURNAL   J. Biochem. (Tokyo). 81 (1977) 851-8.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00930  Caprolactam degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.12
            ExPASy - ENZYME nomenclature database: 1.4.3.12
            ExplorEnz - The Enzyme Database: 1.4.3.12
            ERGO genome analysis and discovery system: 1.4.3.12
            UM-BBD (Biocatalysis/Biodegradation Database): 1.4.3.12
            BRENDA, the Enzyme Database: 1.4.3.12
            CAS: 63116-97-2
///
ENTRY       EC 1.4.3.13                 Enzyme
NAME        protein-lysine 6-oxidase;
            lysyl oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     protein-L-lysine:oxygen 6-oxidoreductase (deaminating)
REACTION    peptidyl-L-lysyl-peptide + O2 + H2O = peptidyl-allysyl-peptide + NH3
            + H2O2 [RN:R04239]
ALL_REAC    R04239
SUBSTRATE   peptidyl-L-lysyl-peptide [CPD:C03530];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     peptidyl-allysyl-peptide [CPD:C03531];
            NH3 [CPD:C00014];
            H2O2 [CPD:C00027]
COMMENT     Also acts on protein 5-hydroxylysine. This enzyme catalyses the
            final known enzymic step required for collagen and elastin
            cross-linking in the biosynthesis of normal mature extracellular
            matrices [4]. These reactions play an important role for the
            development, elasticity and extensibility of connective tissue. The
            enzyme is also active on free amines, such as cadaverine or
            benzylamine [4,5].
REFERENCE   1  [PMID:4838158]
  AUTHORS   Harris ED, Gonnerman WA, Savage JE, O'Dell BL.
  TITLE     Connective tissue amine oxidase. II. Purification and partial
            characterization of lysyl oxidase from chick aorta.
  JOURNAL   Biochim. Biophys. Acta. 341 (1974) 332-44.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:33171]
  AUTHORS   Rayton JK, Harris ED.
  TITLE     Induction of lysyl oxidase with copper. Properties of an in vitro
            system.
  JOURNAL   J. Biol. Chem. 254 (1979) 621-6.
  ORGANISM  chicken [GN:gga]
REFERENCE   3  [PMID:7318]
  AUTHORS   Stassen FL.
  TITLE     Properties of highly purified lysyl oxidase from embryonic chick
            cartilage.
  JOURNAL   Biochim. Biophys. Acta. 438 (1976) 49-60.
  ORGANISM  chicken [GN:gga]
REFERENCE   4  [PMID:11779117]
  AUTHORS   Palamakumbura AH, Trackman PC.
  TITLE     A fluorometric assay for detection of lysyl oxidase enzyme activity
            in biological samples.
  JOURNAL   Anal. Biochem. 300 (2002) 245-51.
  ORGANISM  cow [GN:bta]
REFERENCE   5  [PMID:6147351]
  AUTHORS   Kagan HM, Williams MA, Williamson PR, Anderson JM.
  TITLE     Influence of sequence and charge on the specificity of lysyl oxidase
            toward protein and synthetic peptide substrates.
  JOURNAL   J. Biol. Chem. 259 (1984) 11203-7.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K00277  protein-lysine 6-oxidase
GENES       HSA: 4015(LOX)
            PTR: 471614(LOX)
            MMU: 16948(Lox)
            RNO: 24914(Lox)
            CFA: 481478(LOX)
            BTA: 280841(LOX)
            GGA: 396474(LOX)
            DRE: 404621(lox)
            DME: Dmel_CG11335(lox) Dmel_CG4402(lox2)
STRUCTURES  PDB: 1N9E  1RKY  1W7C  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.13
            ExPASy - ENZYME nomenclature database: 1.4.3.13
            ExplorEnz - The Enzyme Database: 1.4.3.13
            ERGO genome analysis and discovery system: 1.4.3.13
            BRENDA, the Enzyme Database: 1.4.3.13
            CAS: 99676-44-5
///
ENTRY       EC 1.4.3.14                 Enzyme
NAME        L-lysine oxidase;
            L-lysine alpha-oxidase;
            L-lysyl-alpha-oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     L-lysine:oxygen 2-oxidoreductase (deaminating)
REACTION    L-lysine + O2 + H2O = 6-amino-2-oxohexanoate + NH3 + H2O2
            [RN:R00447]
ALL_REAC    R00447
SUBSTRATE   L-lysine [CPD:C00047];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     6-amino-2-oxohexanoate [CPD:C03239];
            NH3 [CPD:C00014];
            H2O2 [CPD:C00027]
COMMENT     Also acts, more slowly, on L-ornithine, L-phenylalanine, L-arginine
            and L-histidine.
REFERENCE   1  [PMID:6101334]
  AUTHORS   Kusakabe H, Kodama K, Kuninaka A, Yoshino H, Misono H, Soda K.
  TITLE     A new antitumor enzyme, L-lysine alpha-oxidase from Trichoderma
            viride. Purification and enzymological properties.
  JOURNAL   J. Biol. Chem. 255 (1980) 976-81.
  ORGANISM  Trichoderma viride
REFERENCE   2  [PMID:12460113]
  AUTHORS   Lukasheva EV, Berezov TT.
  TITLE     L-Lysine alpha-oxidase: physicochemical and biological properties.
  JOURNAL   Biochemistry. (Mosc). 67 (2002) 1152-8.
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.14
            ExPASy - ENZYME nomenclature database: 1.4.3.14
            ExplorEnz - The Enzyme Database: 1.4.3.14
            ERGO genome analysis and discovery system: 1.4.3.14
            BRENDA, the Enzyme Database: 1.4.3.14
            CAS: 70132-14-8
///
ENTRY       EC 1.4.3.15                 Enzyme
NAME        D-glutamate(D-aspartate) oxidase;
            D-glutamic-aspartic oxidase;
            D-monoaminodicarboxylic acid oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     D-glutamate(D-aspartate):oxygen oxidoreductase (deaminating)
REACTION    D-glutamate + H2O + O2 = 2-oxoglutarate + NH3 + H2O2 [RN:R00279]
ALL_REAC    R00279;
            (other) R00359
SUBSTRATE   D-glutamate [CPD:C00217];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     2-oxoglutarate [CPD:C00026];
            NH3 [CPD:C00014];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). D-Glutamate and D-aspartate are oxidized at
            the same rate. Other D-monoaminodicarboxylates, and other D- and
            L-amino acids, are not oxidized.
REFERENCE   1
  AUTHORS   Mizushima, S.
  TITLE     Purified D-glutamic-aspartic oxidase of Aspergillus ustus.
  JOURNAL   J. Gen. Appl. Microbiol. 3 (1957) 233-239.
  ORGANISM  Aspergillus ustus
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.15
            ExPASy - ENZYME nomenclature database: 1.4.3.15
            ExplorEnz - The Enzyme Database: 1.4.3.15
            ERGO genome analysis and discovery system: 1.4.3.15
            BRENDA, the Enzyme Database: 1.4.3.15
///
ENTRY       EC 1.4.3.16                 Enzyme
NAME        L-aspartate oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     L-aspartate:oxygen oxidoreductase (deaminating)
REACTION    L-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2 [RN:R00357]
ALL_REAC    R00357;
            (other) R00481
SUBSTRATE   L-aspartate [CPD:C00049];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     oxaloacetate [CPD:C00036];
            NH3 [CPD:C00014];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). A component of the bacterial quinolinate
            synthase system.
REFERENCE   1  [PMID:7033218]
  AUTHORS   Nasu S, Wicks FD, Gholson RK.
  TITLE     L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli,
            is the B protein of quinolinate synthetase.
  JOURNAL   J. Biol. Chem. 257 (1982) 626-32.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
            PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K00278  L-aspartate oxidase
GENES       ATH: AT5G14760(AO)
            OSA: 4328220
            ECO: b2574(nadB)
            ECJ: JW2558(nadB)
            ECE: Z3856(nadB)
            ECS: ECs3440
            ECC: c3098(nadB)
            ECI: UTI89_C0747(nadA) UTI89_C2896(nadB)
            ECP: ECP_2576
            ECV: APECO1_3957(nadB)
            ECW: EcE24377A_2862(nadB)
            ECX: EcHS_A2730
            STY: STY2834(nadB)
            STT: t0269(nadB)
            SPT: SPA0277(nadB)
            SEC: SC2646(nadB)
            STM: STM2641(nadB)
            YPE: YPO2710(nadB)
            YPK: y1289(nadB)
            YPM: YP_2514(nadB)
            YPA: YPA_2444
            YPN: YPN_1198
            YPP: YPDSF_1561
            YPS: YPTB2898(nadB)
            YPI: YpsIP31758_1128(nadB)
            YEN: YE1009(nadB)
            SDY: SDY_2815(nadB)
            ECA: ECA3285(nadB)
            PLU: plu3347(nadB)
            SGL: SG1794
            ENT: Ent638_3061
            KPN: KPN_02899(nadB)
            SPE: Spro_3677
            XFA: XF1924
            XFT: PD0868(nadB)
            VCH: VC2469
            VCO: VC0395_A2046(nadB)
            VVU: VV1_1558
            VVY: VV2839
            VPA: VP2580
            VFI: VF2094
            PPR: PBPRA3097(nadB)
            PAE: PA0761(nadB)
            PAU: PA14_54450(nadB)
            PAP: PSPA7_4759(nadB)
            PPU: PP_1426(nadB)
            PPF: Pput_4295
            PST: PSPTO_4225(nadB)
            PSB: Psyr_3959
            PSP: PSPPH_3956(nadB)
            PFL: PFL_1447(nadB)
            PFO: Pfl_1360
            PEN: PSEEN4297(nadB)
            PMY: Pmen_1466
            PAR: Psyc_0631(nadB)
            PCR: Pcryo_0599
            PRW: PsycPRwf_1965
            ACI: ACIAD2587(nadB)
            SON: SO_1341(nadB)
            SDN: Sden_2773
            SFR: Sfri_2936
            SAZ: Sama_0873
            SBL: Sbal_1194
            SBM: Shew185_1238
            SLO: Shew_1047
            SPC: Sputcn32_1152
            SSE: Ssed_1141
            SPL: Spea_1030
            SHE: Shewmr4_2855
            SHM: Shewmr7_2937
            SHN: Shewana3_3033
            SHW: Sputw3181_3012
            ILO: IL0817(nadB)
            CPS: CPS_4130(nadB)
            PHA: PSHAa0725(nadB)
            PAT: Patl_3156
            SDE: Sde_2252
            PIN: Ping_0064
            MAQ: Maqu_2264
            CBU: CBU_0101(nadB)
            CBD: COXBU7E912_2006(nadB)
            LPN: lpg0800(nadB1)
            LPF: lpl0833(nadB)
            LPP: lpp0862(nadB)
            MCA: MCA1472(nadB)
            FTU: FTT1467c(nadB)
            FTF: FTF1467c(nadB)
            FTW: FTW_0631(nadB)
            FTL: FTL_1388
            FTH: FTH_1350(nadB)
            FTA: FTA_1475(nadB)
            FTN: FTN_0694(nadB)
            TCX: Tcr_0729
            NOC: Noc_2467
            AEH: Mlg_1338
            HHA: Hhal_0041
            HCH: HCH_01789(nadB)
            ABO: ABO_1641(nadB)
            MMW: Mmwyl1_1097
            AHA: AHA_0793(nadB)
            BCI: BCI_0614(nadB)
            RMA: Rmag_0966
            VOK: COSY_0867(nadB)
            NME: NMB0392
            NMA: NMA2092(nadB)
            NMC: NMC1773(nadB)
            NGO: NGO1568
            CVI: CV_3930(nadB)
            RSO: RSc2447(nadB1) RSp1263(nadB2)
            REU: Reut_A2735 Reut_B4589
            REH: H16_A3036(nadB)
            RME: Rmet_2872
            BMA: BMA2233(nadB)
            BMV: BMASAVP1_A2649(nadB)
            BML: BMA10299_A1024(nadB)
            BMN: BMA10247_2103(nadB)
            BXE: Bxe_A0815
            BVI: Bcep1808_2582
            BUR: Bcep18194_A5836
            BCN: Bcen_1893
            BCH: Bcen2424_2504
            BAM: Bamb_2551
            BPS: BPSL0914(nadB)
            BPM: BURPS1710b_1134(nadB)
            BPL: BURPS1106A_0980(nadB)
            BPD: BURPS668_0976(nadB)
            BTE: BTH_I0778(nadB)
            PNU: Pnuc_1106
            RFR: Rfer_3031
            POL: Bpro_0905
            PNA: Pnap_0956
            AAV: Aave_3840
            AJS: Ajs_3493
            VEI: Veis_1080
            MPT: Mpe_A1551
            HAR: HEAR1385(nadB)
            MMS: mma_1997
            NEU: NE1892(nadB1)
            NET: Neut_2004
            NMU: Nmul_A1743
            EBA: ebA5461(nadB)
            AZO: azo1629(nadB)
            DAR: Daro_2021
            TBD: Tbd_2096
            MFA: Mfla_0855 Mfla_0999
            HPA: HPAG1_1303
            HHE: HH0017
            WSU: WS1604
            TDN: Tmden_0420
            ABU: Abu_0922(nadB)
            NIS: NIS_1341
            SUN: SUN_1899
            GSU: GSU1827(nadB)
            GME: Gmet_1954
            GUR: Gura_2487
            PCA: Pcar_1322
            PPD: Ppro_1736
            DVU: DVU1809(nadB)
            DVL: Dvul_1351
            DDE: Dde_1829
            LIP: LI0362(nadB)
            BBA: Bd3127(nadB)
            DPS: DP0711(nadB)
            ADE: Adeh_3566
            AFW: Anae109_3159 Anae109_3687
            MXA: MXAN_4629(nadB)
            SAT: SYN_00424 SYN_00729
            SFU: Sfum_0605
            MLO: mll5834 mll9103
            MES: Meso_2556
            PLA: Plav_0733
            SME: SMc02599(nadB)
            SMD: Smed_0700
            ATU: Atu4097(nadB)
            ATC: AGR_L_1513
            RET: RHE_PE00440(nadB)
            RLE: pRL110616(nadB)
            OAN: Oant_0430
            BJA: bll2541(nadB)
            BRA: BRADO2036(nadB) BRADO4283 BRADO4530(nadB)
            BBT: BBta_2362(nadB) BBta_3287 BBta_4756(nadB) BBta_4872
            RPA: RPA1054(nadB)
            RPB: RPB_1106
            RPC: RPC_4339
            RPD: RPD_1228
            RPE: RPE_4401
            NWI: Nwi_2425
            NHA: Nham_2820
            XAU: Xaut_1182 Xaut_3933
            CCR: CC_2913
            SIL: SPO3244
            SIT: TM1040_2249
            RSH: Rsph17029_3884
            RSQ: Rsph17025_1547
            JAN: Jann_3969
            PDE: Pden_4431
            MMR: Mmar10_0790
            HNE: HNE_0690(nadB)
            ZMO: ZMO0144(nadB)
            NAR: Saro_0410
            SAL: Sala_2315
            SWI: Swit_1927
            ELI: ELI_11660
            GBE: GbCGDNIH1_0641
            ACR: Acry_1542
            RRU: Rru_A1433
            MAG: amb3884
            MGM: Mmc1_1746 Mmc1_1770
            ABA: Acid345_2250
            SUS: Acid_7341
            BSU: BG10867(nadB)
            BHA: BH1218(nadB)
            BAN: BA4662(nadB)
            BAR: GBAA4662(nadB)
            BAA: BA_5101
            BAT: BAS4327
            BCE: BC4423
            BCA: BCE_4515(nadB)
            BCZ: BCZK4175(nadB)
            BCY: Bcer98_3145
            BTK: BT9727_4164(nadB)
            BTL: BALH_4011(nadB)
            BLI: BL01155(nadB)
            BLD: BLi02914(nadB)
            BCL: ABC1547(nadB) ABC1549(nadA)
            BAY: RBAM_024920
            BPU: BPUM_2427
            GKA: GK2601
            LMO: lmo2023(nadB)
            LMF: LMOf2365_2048(nadB)
            LIN: lin2131(nadB)
            CAC: CAC1024(nadB)
            CPE: CPE0395(nadB)
            CPF: CPF_0383(nadB)
            CPR: CPR_0377(nadB)
            CNO: NT01CX_0089
            CTH: Cthe_2355
            CDF: CD2371(nadB)
            CBO: CBO1447A(nadB)
            CBA: CLB_1473(nadB)
            CBH: CLC_1485(nadB)
            CBF: CLI_1532(nadB)
            CBE: Cbei_0793
            CKL: CKL_0749(nadB)
            AMT: Amet_0018
            CHY: CHY_2373(nadB)
            DSY: DSY0213(nadB)
            DRM: Dred_0164
            SWO: Swol_0105
            CSC: Csac_1778
            MTU: Rv1595(nadB)
            MTC: MT1631(nadB)
            MBO: Mb1621(nadB)
            MBB: BCG_1633(nadB)
            MLE: ML1226(nadB)
            MPA: MAP1290(nadB)
            MAV: MAV_3190(nadB)
            MSM: MSMEG_3200(nadB)
            MVA: Mvan_2799
            MGI: Mflv_3618
            MMC: Mmcs_3067
            MKM: Mkms_3127
            MJL: Mjls_3084
            CDI: DIP2258(nadB)
            NFA: nfa18380(nadB)
            RHA: RHA1_ro01037(nadB)
            SCO: SCO3382(nadB)
            SMA: SAV4688(nadB)
            ART: Arth_2559
            AAU: AAur_2533(nadB)
            NCA: Noca_0462
            TFU: Tfu_2883
            FRA: Francci3_4377
            FAL: FRAAL6672(nadB)
            ACE: Acel_0213
            KRA: Krad_3558
            SEN: SACE_5802(nadB)
            STP: Strop_4280
            BLO: BL1375(nadB)
            RXY: Rxyl_0107
            FNU: FN0009
            RBA: RB3824(nadB) RB7425(nadA)
            LIL: LA1511(nadB)
            LIC: LIC12251(nadB)
            LBJ: LBJ_1708(nadB)
            LBL: LBL_1927(nadB)
            SYN: sll0631(nadB)
            SYW: SYNW2192(nadB)
            SYC: syc2214_d(nadB)
            SYF: Synpcc7942_1881
            SYD: Syncc9605_2335
            SYE: Syncc9902_0355
            SYG: sync_2546(nadB)
            SYR: SynRCC307_0303(nadB)
            SYX: SynWH7803_2204(nadB)
            CYA: CYA_0948(nadB)
            CYB: CYB_2480(nadB)
            TEL: tll2407 tll2408(nadB)
            GVI: glr0846(nadB)
            ANA: alr1217
            AVA: Ava_0636 Ava_5000 Ava_5007
            PMA: Pro0119(nadB)
            PMM: PMM0100(nadB)
            PMT: PMT0177(nadB)
            PMN: PMN2A_1468
            PMI: PMT9312_0104
            PMB: A9601_01161(nadB)
            PMC: P9515_01121(nadB)
            PMF: P9303_02181(nadB)
            PMG: P9301_01151(nadB)
            PMH: P9215_01161
            PME: NATL1_01711(nadB)
            TER: Tery_2445
            BTH: BT_3184
            BFR: BF0022
            BFS: BF0021(nadB)
            PGI: PG1576(nadB)
            SRU: SRU_1914
            FJO: Fjoh_4056
            CTE: CT0561(nadB)
            CCH: Cag_1159
            CPH: Cpha266_0811
            PVI: Cvib_1210
            PLT: Plut_0565
            DEH: cbdb_A1338(nabD)
            DEB: DehaBAV1_1193
            RRS: RoseRS_0437
            RCA: Rcas_1003
            DGE: Dgeo_1162
            TTH: TTC0619
            TTJ: TTHA0983
            AAE: aq_777(nadB)
            MEM: Memar_0221
            HAL: VNG1883G(nadB)
            HMA: rrnAC3409(nadB)
            HWA: HQ3217A(nadB)
            NPH: NP2416A(nadB)
            PHO: PH0015
            PAB: PAB2343
            PFU: PF1976
            TKO: TK0297
            SSO: SSO0997(nadB)
            STO: ST1196
            SAI: Saci_0549(nadB)
STRUCTURES  PDB: 1J5P  1KNP  1KNR  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.16
            ExPASy - ENZYME nomenclature database: 1.4.3.16
            ExplorEnz - The Enzyme Database: 1.4.3.16
            ERGO genome analysis and discovery system: 1.4.3.16
            BRENDA, the Enzyme Database: 1.4.3.16
            CAS: 69106-47-4
///
ENTRY       EC 1.4.3.17       Obsolete  Enzyme
NAME        Transferred to 1.3.3.10
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now EC 1.3.3.10 tryptophan alpha,beta-oxidase.
            Enzyme was incorrectly classified as acting on a CH-NH bond rather
            than a CH-CH bond. (EC 1.4.3.17 created 2000, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.17
            ExPASy - ENZYME nomenclature database: 1.4.3.17
            ExplorEnz - The Enzyme Database: 1.4.3.17
            ERGO genome analysis and discovery system: 1.4.3.17
            BRENDA, the Enzyme Database: 1.4.3.17
///
ENTRY       EC 1.4.3.18       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
COMMENT     Deleted entry: Not approved as the enzyme was shown to be a
            dehydrogenase and not an oxidase (see EC 1.5.99.12 cytokinin
            dehydrogenase). (EC 1.4.3.18 proposed 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.18
            ExPASy - ENZYME nomenclature database: 1.4.3.18
            ExplorEnz - The Enzyme Database: 1.4.3.18
            ERGO genome analysis and discovery system: 1.4.3.18
            BRENDA, the Enzyme Database: 1.4.3.18
///
ENTRY       EC 1.4.3.19                 Enzyme
NAME        glycine oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     glycine:oxygen oxidoreductase (deaminating)
REACTION    (1) glycine + H2O + O2 = glyoxylate + NH3 + H2O2 [RN:R00366];
            (2) D-alanine + H2O + O2 = pyruvate + NH3 + H2O2 [RN:R05861];
            (3) sarcosine + H2O + O2 = glyoxylate + methylamine + H2O2
            [RN:R05862];
            (4) N-ethylglycine + H2O + O2 = glyoxylate + ethylamine + H2O2
            [RN:R05863]
ALL_REAC    R00366 R05861 R05862 R05863;
            (other) R07463
SUBSTRATE   glycine [CPD:C00037];
            H2O [CPD:C00001];
            O2 [CPD:C00007];
            D-alanine [CPD:C00133];
            sarcosine [CPD:C00213];
            N-ethylglycine [CPD:C11735]
PRODUCT     glyoxylate [CPD:C00048];
            NH3 [CPD:C00014];
            H2O2 [CPD:C00027];
            pyruvate [CPD:C00022];
            methylamine [CPD:C00218];
            ethylamine [CPD:C00797]
COMMENT     A flavoenzyme containing non-covalently bound FAD. The enzyme from
            Bacillus subtilis is active with glycine, sarcosine, N-ethylglycine,
            D-alanine, D-alpha-aminobutyrate, D-proline, D-pipecolate and
            N-methyl-D-alanine. It differs from EC 1.4.3.3, D-amino-acid
            oxidase, due to its activity on sarcosine and D-pipecolate.
REFERENCE   1  [PMID:11744710]
  AUTHORS   Job V, Marcone GL, Pilone MS, Pollegioni L.
  TITLE     Glycine oxidase from Bacillus subtilis. Characterization of a new
            flavoprotein.
  JOURNAL   J. Biol. Chem. 277 (2002) 6985-93.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   2  [PMID:9827558]
  AUTHORS   Nishiya Y, Imanaka T.
  TITLE     Purification and characterization of a novel glycine oxidase from
            Bacillus subtilis.
  JOURNAL   FEBS. Lett. 438 (1998) 263-6.
  ORGANISM  Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00730  Thiamine metabolism
ORTHOLOGY   KO: K03153  glycine oxidase
            KO: K05899  glycine oxidase
GENES       PAE: PA4548
            PAU: PA14_60270
            PAP: PSPA7_5188(thiO)
            PPU: PP_0612
            PST: PSPTO_0817
            PSB: Psyr_0721
            PSP: PSPPH_0732(thiO)
            PFL: PFL_5310(thiO)
            PFO: Pfl_4841
            PEN: PSEEN4683 PSEEN5520(hcnC)
            CBD: COXBU7E912_1748(thiO)
            NOC: Noc_2269
            HCH: HCH_00138(thiO)
            CSA: Csal_0494
            CVI: CV_1682(hcnC)
            RSO: RSc0112(RS00982)
            REU: Reut_A0206
            REH: H16_A0236(thiO)
            RME: Rmet_0163
            BMA: BMA2730
            BMV: BMASAVP1_A3224(thiO)
            BML: BMA10299_A1773(thiO)
            BMN: BMA10247_2780(thiO)
            BXE: Bxe_A0383
            BUR: Bcep18194_A3508 Bcep18194_B1496
            BCN: Bcen_2697
            BCH: Bcen2424_0410
            BAM: Bamb_0328
            BPS: BPSL3154(thiO)
            BPM: BURPS1710b_3710(thiO)
            BPL: BURPS1106A_3739(thiO)
            BPD: BURPS668_3681(thiO)
            BTE: BTH_I3008
            RFR: Rfer_2464
            POL: Bpro_0038
            TBD: Tbd_1866
            MFA: Mfla_0136
            ADE: Adeh_0139
            MXA: MXAN_4231(thiO)
            APH: APH_0325
            ECH: ECH_0452
            MES: Meso_2562
            SME: SMb20616(thiO)
            ATU: Atu2568(thiO)
            ATC: AGR_C_4654
            RET: RHE_PB00081(thiO)
            RLE: RL3589(goxB)
            BOV: BOV_0208(thiO)
            RPA: RPA3573(thiO)
            RPB: RPB_1958(thiO)
            RPD: RPD_3428
            RPE: RPE_2073
            NHA: Nham_2891
            CCR: CC_2329
            SIT: TM1040_3650
            RDE: RD1_0747(thiO) RD1_0969
            HNE: HNE_2691
            MGM: Mmc1_2933
            ABA: Acid345_1735
            BSU: BG13147(goxB)
            BHA: BH1434
            BAN: BA0730(goxB)
            BAR: GBAA0730(goxB)
            BAA: BA_1318
            BAT: BAS0696
            BCE: BC0747
            BCA: BCE_0800(goxB)
            BCZ: BCZK0640(goxB)
            BTK: BT9727_0640(goxB)
            BTL: BALH_0667(goxB)
            BLI: BL01590(goxB)
            BLD: BLi01261(goxB)
            BCL: ABC1736(goxB)
            BPU: BPUM_1096(goxB)
            GKA: GK0623
            SEP: SE2058
            SER: SERP2071
            SHA: SH0564
            SSP: SSPP135
            MTU: Rv0415(thiO)
            MTC: MT0428
            MBO: Mb0423(thiO)
            MLE: ML0299
            MPA: MAP3898
            MAV: MAV_4746(thiO)
            MSM: MSMEG_0791(thiO)
            MUL: MUL_2805(thiO)
            MMC: Mmcs_0545
            CGL: NCgl1962(cgl2039)
            CGB: cg2237(thiO)
            CEF: CE1934
            CDI: DIP0031(thiO)
            CJK: jk0852(thiO)
            NFA: nfa53390
            RHA: RHA1_ro02190
            SCO: SCO2107(SC2C1A.03)
            SMA: SAV6095(goxB)
            ART: Arth_2781
            AAU: AAur_2764(thiO)
            PAC: PPA0520
            TFU: Tfu_1044(thiO)
            ACE: Acel_0989
            RXY: Rxyl_0462
            SYW: SYNW2357(thiO)
            SYC: syc1699_c
            SYF: Synpcc7942_2406
            SYD: Syncc9605_2498
            SYE: Syncc9902_2170
            SYG: sync_2740(thiO)
            CYA: CYA_1058(thiO)
            CYB: CYB_2393(thiO)
            TEL: tlr2368
            GVI: gll2137
            AVA: Ava_3219(thiG)
            PMT: PMT2140(thiO)
            PMN: PMN2A_1380
            PMC: P9515_00541(dadA)
            PMF: P9303_28291(dadA)
            PME: NATL1_00611(dadA)
            TER: Tery_0284
            SRU: SRU_1233(thiO)
            DGE: Dgeo_1920
            AAE: aq_707
STRUCTURES  PDB: 1RYI  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.19
            ExPASy - ENZYME nomenclature database: 1.4.3.19
            ExplorEnz - The Enzyme Database: 1.4.3.19
            ERGO genome analysis and discovery system: 1.4.3.19
            BRENDA, the Enzyme Database: 1.4.3.19
            CAS: 39307-16-9
///
ENTRY       EC 1.4.3.20                 Enzyme
NAME        L-lysine 6-oxidase;
            L-lysine-epsilon-oxidase;
            Lod;
            LodA;
            marinocine
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
SYSNAME     L-lysine:oxygen 6-oxidoreductase (deaminating)
REACTION    L-lysine + O2 + H2O = 2-aminoadipate 6-semialdehyde + H2O2 + NH3
            [RN:R07598]
ALL_REAC    R07598
SUBSTRATE   L-lysine [CPD:C00047];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     2-aminoadipate 6-semialdehyde [CPD:C04076];
            H2O2 [CPD:C00027];
            NH3 [CPD:C00014]
COMMENT     Differs from EC 1.4.3.13, protein-lysine 6-oxidase, by using free
            L-lysine rather than the protein-bound form. N2-Acetyl-L-lysine is
            also a substrate, but N6-acetyl-L-lysine, which has an acetyl group
            at position 6, is not a substrate. Also acts on L-ornithine,
            D-lysine and 4-hydroxy-L-lysine, but more slowly. The amines
            cadaverine and putrescine are not substrates [2].
REFERENCE   1  [PMID:16547036]
  AUTHORS   Lucas-Elio P, Gomez D, Solano F, Sanchez-Amat A.
  TITLE     The antimicrobial activity of marinocine, synthesized by Marinomonas
            mediterranea, is due to hydrogen peroxide generated by its lysine
            oxidase activity.
  JOURNAL   J. Bacteriol. 188 (2006) 2493-501.
  ORGANISM  Marinomonas mediterranea
REFERENCE   2  [PMID:17030025]
  AUTHORS   Gomez D, Lucas-Elio P, Sanchez-Amat A, Solano F.
  TITLE     A novel type of lysine oxidase: L-lysine-epsilon-oxidase.
  JOURNAL   Biochim. Biophys. Acta. 1764 (2006) 1577-85.
  ORGANISM  Marinomonas mediterranea
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.3.20
            ExPASy - ENZYME nomenclature database: 1.4.3.20
            ExplorEnz - The Enzyme Database: 1.4.3.20
            ERGO genome analysis and discovery system: 1.4.3.20
            BRENDA, the Enzyme Database: 1.4.3.20
///
ENTRY       EC 1.4.3.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With oxygen as acceptor
REACTION    (1) L-Arginine + Oxygen + H2O <=> 2-Oxoarginine + H2O2 + NH3
            [RN:R00556];
            (2) gamma-L-Glutamylputrescine + H2O + Oxygen <=>
            gamma-Glutamyl-gamma-aminobutyraldehyde + NH3 + H2O2 [RN:R07415]
SUBSTRATE   L-Arginine [CPD:C00062];
            Oxygen [CPD:C00007];
            H2O [CPD:C00001];
            gamma-L-Glutamylputrescine [CPD:C15699]
PRODUCT     2-Oxoarginine [CPD:C05935];
            H2O2 [CPD:C00027];
            NH3 [CPD:C00014];
            gamma-Glutamyl-gamma-aminobutyraldehyde [CPD:C15700]
///
ENTRY       EC 1.4.4.1        Obsolete  Enzyme
NAME        Transferred to 1.21.4.1
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With a disulfide as acceptor
COMMENT     Transferred entry: now EC 1.21.4.1, D-proline reductase (dithiol)
            (EC 1.4.4.1 created 1972, modified 1982 (EC 1.4.1.6 created 1961,
            incorporated 1982), deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.4.1
            ExPASy - ENZYME nomenclature database: 1.4.4.1
            ExplorEnz - The Enzyme Database: 1.4.4.1
            ERGO genome analysis and discovery system: 1.4.4.1
            BRENDA, the Enzyme Database: 1.4.4.1
///
ENTRY       EC 1.4.4.2                  Enzyme
NAME        glycine dehydrogenase (decarboxylating);
            P-protein;
            glycine decarboxylase;
            glycine-cleavage complex;
            glycine:lipoylprotein oxidoreductase (decarboxylating and
            acceptor-aminomethylating);
            protein P1
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With a disulfide as acceptor
SYSNAME     glycine:H-protein-lipoyllysine oxidoreductase (decarboxylating,
            acceptor-amino-methylating)
REACTION    glycine + H-protein-lipoyllysine =
            H-protein-S-aminomethyldihydrolipoyllysine + CO2 [RN:R03425]
ALL_REAC    R03425
SUBSTRATE   glycine [CPD:C00037];
            H-protein-lipoyllysine [CPD:C02051]
PRODUCT     H-protein-S-aminomethyldihydrolipoyllysine [CPD:C01242];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. A component, with EC 2.1.2.10,
            aminomethyltransferase and EC 1.8.1.4, dihydrolipoyl dehydrogenanse,
            of the glycine cleavage system, previously known as glycine
            synthase. The glycine cleavage system is composed of four components
            that only loosely associate: the P protein (EC 1.4.4.2), the T
            protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the
            lipoyl-bearing H protein [3].
REFERENCE   1  [PMID:7440563]
  AUTHORS   Hiraga K, Kikuchi G.
  TITLE     The mitochondrial glycine cleavage system. Functional association of
            glycine decarboxylase and aminomethyl carrier protein.
  JOURNAL   J. Biol. Chem. 255 (1980) 11671-6.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:10966480]
  AUTHORS   Perham RN.
  TITLE     Swinging arms and swinging domains in multifunctional enzymes:
            catalytic machines for multistep reactions.
  JOURNAL   Annu. Rev. Biochem. 69 (2000) 961-1004.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   3  [PMID:15642479]
  AUTHORS   Nesbitt NM, Baleanu-Gogonea C, Cicchillo RM, Goodson K, Iwig DF,
            Broadwater JA, Haas JA, Fox BG, Booker SJ.
  TITLE     Expression, purification, and physical characterization of
            Escherichia coli lipoyl(octanoyl)transferase.
  JOURNAL   Protein. Expr. Purif. 39 (2005) 269-82.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K00281  glycine dehydrogenase
            KO: K00282  glycine dehydrogenase subunit 1
            KO: K00283  glycine dehydrogenase subunit 2
GENES       HSA: 2731(GLDC)
            MMU: 104174(Gldc)
            CFA: 481534(GLDC)
            GGA: 374222(GLDC)
            XLA: 379833(gldc)
            DRE: 321621(gldc)
            SPU: 578453(LOC578453)
            ATH: AT2G26080 AT4G33010
            OSA: 4325932 4341516
            CME: CMR282C
            SCE: YMR189W(GCV2)
            PIC: PICST_75631(GCV2)
            CGR: CAGL0L00429g
            SPO: SPAC13G6.06c
            ANI: AN7136.2
            AFM: AFUA_4G03760
            AOR: AO090011000351
            CNE: CNC01070
            UMA: UM04175.1
            DDI: DDB_0231130(gcvP)
            TET: TTHERM_00794020
            TBR: Tb927.7.1910
            TCR: 509161.10 509163.80 510911.50
            LMA: LmjF26.0030
            ECO: b2903(gcvP)
            ECJ: JW2871(gcvP)
            ECE: Z4240(gcvP)
            ECS: ECs3774
            ECC: c3483(gcvP)
            ECI: UTI89_C3288(gcvP)
            ECP: ECP_2896
            ECW: EcE24377A_3230(gcvP)
            ECX: EcHS_A3062(gcvP)
            STY: STY3209(gcvP)
            STT: t2971(gcvP)
            SPT: SPA2921(gcvP)
            SEC: SC2994(gcvP)
            STM: STM3053(gcvP)
            YPE: YPO0905(gcvP)
            YPK: y3292(gcvP)
            YPM: YP_3602(gcvP)
            YPA: YPA_0362
            YPN: YPN_3104
            YPP: YPDSF_0609
            YPS: YPTB3180(gcvP)
            SFL: SF2889(gcvP)
            SFX: S3088(gcvP)
            SFV: SFV_2951(gcvP)
            SSN: SSON_3056(gcvP)
            ECA: ECA0745(gcvP)
            PLU: plu3596(gcvP)
            SGL: SG2000
            ENT: Ent638_3322
            XFA: XF1385
            XFT: PD0620(gcvP)
            XCC: XCC1112(gcvP)
            XCB: XC_3135
            XCV: XCV1243(gcvP)
            XAC: XAC1214(gcvP)
            XOO: XOO3547(gcvP)
            XOM: XOO_3351(XOO3351)
            VVU: VV2_0186
            VVY: VVA0691
            VPA: VPA0801
            VFI: VFA0703
            PPR: PBPRB1324
            PAE: PA2445(gcvP2) PA5213(gcvP1)
            PAP: PSPA7_2805(gcvP2) PSPA7_5958(gcvP1)
            PPU: PP_0988(gcvP-1) PP_5192(gcvP-2)
            PST: PSPTO_1276(gcvP)
            PSB: Psyr_1096
            PSP: PSPPH_1162(gcvP)
            PFL: PFL_4641(gcvP) PFL_5959(gcvP)
            PFO: Pfl_4392 Pfl_5426
            PEN: PSEEN4436(gcvP-2) PSEEN5307(gcvP-1)
            PAR: Psyc_0796(gcvP)
            PCR: Pcryo_0803
            SON: SO_0781(gcvP)
            SDN: Sden_0835
            SFR: Sfri_3149
            SAZ: Sama_2719
            SBL: Sbal_0619
            SLO: Shew_3062
            SPC: Sputcn32_3209
            SHE: Shewmr4_3329
            SHM: Shewmr7_0624
            SHN: Shewana3_3499
            SHW: Sputw3181_0732
            ILO: IL2092(gcvP_1_2)
            CPS: CPS_1276(gcvP1) CPS_3846(gcvP2)
            PHA: PSHAa2473(gcvP)
            PAT: Patl_3590
            SDE: Sde_2476
            PIN: Ping_2729
            CBU: CBU_1713 CBU_1714
            CBD: COXBU7E912_0291(gcvPA) COXBU7E912_0293(gcvPB)
            LPN: lpg0114 lpg0116
            LPF: lpl0113(gcsB) lpl0115(gcsA)
            LPP: lpp0128(gcsB) lpp0130(gcsA)
            MCA: MCA0348 MCA0349
            FTU: FTT0409(gcvP1) FTT0410(gcvP2)
            FTF: FTF0409(gcvP1) FTF0410(gcvP2)
            FTW: FTW_1663(gcvP2) FTW_1664(gcvP1)
            FTL: FTL_0479 FTL_0480
            FTH: FTH_0477(gcvP1) FTH_0478(gcvP2)
            FTA: FTA_0505
            FTN: FTN_0507(gcvP1) FTN_0508(gcvP2)
            NOC: Noc_0908 Noc_2547
            AEH: Mlg_2578 Mlg_2580
            HHA: Hhal_1192 Hhal_1194
            HCH: HCH_03861(gcvP)
            CSA: Csal_1811
            ABO: ABO_2591(gcvP-1) ABO_2592(gcvP-2)
            AHA: AHA_1720(gcvP)
            DNO: DNO_1069(gcvP)
            RMA: Rmag_0821
            NMA: NMA1934(gcvP)
            NMC: NMC1594(gcvP)
            NGO: NGO1325(gcsP) NGO1404
            CVI: CV_3429(gcvP)
            RSO: RSc3295(gcvP)
            REU: Reut_A3331
            REH: H16_A3621(gcvP)
            RME: Rmet_3482
            BMA: BMA2993(gcvP)
            BMV: BMASAVP1_A3312(gcvP)
            BML: BMA10299_A1544(gcvP)
            BMN: BMA10247_3058(gcvP)
            BXE: Bxe_A0054
            BVI: Bcep1808_0149
            BUR: Bcep18194_A3323
            BCN: Bcen_2911
            BCH: Bcen2424_0144
            BAM: Bamb_0131
            BPS: BPSL3362(gcvP)
            BPM: BURPS1710b_0129(gcvP)
            BPL: BURPS1106A_4000(gcvP)
            BPD: BURPS668_3929(gcvP)
            BTE: BTH_I3253(gcvP)
            BPE: BP0197(gcvP)
            BPA: BPP0771(gcvP)
            BBR: BB0856(gcvP)
            RFR: Rfer_3021
            POL: Bpro_1866
            PNA: Pnap_2685
            AAV: Aave_3147
            AJS: Ajs_1936
            VEI: Veis_2458 Veis_2459 Veis_3959
            MPT: Mpe_A1431
            NEU: NE0609 NE0610
            NET: Neut_1952 Neut_1953
            NMU: Nmul_A0210 Nmul_A0212
            EBA: ebA6124(gcvP1)
            AZO: azo1285(gcvP)
            DAR: Daro_2465
            TBD: Tbd_0173 Tbd_0176
            GSU: GSU0377 GSU0378
            GME: Gmet_3152 Gmet_3153
            GUR: Gura_0336 Gura_0337
            PPD: Ppro_1592 Ppro_1593
            DVU: DVU1424(gcvPB) DVU1425(gcvPA)
            DVL: Dvul_1651 Dvul_1652
            DDE: Dde_1691 Dde_1692
            BBA: Bd0692
            DPS: DP0298 DP0299
            ADE: Adeh_1242 Adeh_1243
            AFW: Anae109_2524 Anae109_2525
            MXA: MXAN_3042(gcvP)
            PUB: SAR11_0668(gcvP)
            MLO: mlr0885
            MES: Meso_1016 Meso_4266
            PLA: Plav_0690
            SME: SMc02049(gcvP)
            ATU: Atu1462(gcvP)
            ATC: AGR_C_2699
            RET: RHE_CH02243(gcvP)
            RLE: RL2573(gcvP)
            BME: BMEII0561
            BMF: BAB2_0515(gcvP)
            BMS: BRA0725(gcvP)
            BMB: BruAb2_0506(gcvP)
            BOV: BOV_A0679(gcvP)
            BJA: blr5753(gcvP)
            BRA: BRADO4984(gcvP)
            BBT: BBta_5451(gcvP)
            RPA: RPA3850(gcvP)
            RPB: RPB_3740
            RPC: RPC_1568
            RPD: RPD_1731
            RPE: RPE_1595
            NWI: Nwi_1284
            NHA: Nham_1618
            BHE: BH12820(gcvP)
            BQU: BQ10110(gcvP)
            BBK: BARBAKC583_1094(gcvP)
            XAU: Xaut_2197 Xaut_2198
            CCR: CC_3352 CC_3353
            SIL: SPOA0059(gcvP)
            SIT: TM1040_2391
            RSP: RSP_2195(gcvP)
            RSH: Rsph17029_0870
            JAN: Jann_3622
            RDE: RD1_1225(gcvP)
            PDE: Pden_2346
            MMR: Mmar10_2208 Mmar10_2209
            HNE: HNE_2721 HNE_2722
            NAR: Saro_1852 Saro_1853
            SAL: Sala_1867 Sala_1868
            SWI: Swit_2696 Swit_2697
            ELI: ELI_10060 ELI_10065
            GOX: GOX1097
            RRU: Rru_A3048 Rru_A3049
            MAG: amb0768 amb0769
            MGM: Mmc1_1560 Mmc1_1561
            ABA: Acid345_2458 Acid345_2459
            SUS: Acid_0481 Acid_0482
            BSU: BG11510(gcvPA) BG11511(gcvPB)
            BHA: BH2814 BH2815
            BAN: BA4447(yqhK) BA4448(yqhJ)
            BAR: GBAA4447(yqhK) GBAA4448(yqhJ)
            BAA: BA_4901 BA_4902
            BAT: BAS4129 BAS4130
            BCE: BC4224 BC4225
            BCA: BCE_4303(yqhK) BCE_4304(yqhJ) BCE_5130(gcvH)
            BCZ: BCZK3979 BCZK3980
            BCY: Bcer98_2913 Bcer98_2914
            BTK: BT9727_3969 BT9727_3970
            BTL: BALH_3827(gcvPB) BALH_3828(gcvPA)
            BLI: BL01560(gcvPB) BL01561(gcvPA)
            BLD: BLi02629(gcvPB) BLi02630(gcvPA)
            BCL: ABC2493(gcvPB) ABC2494(gcvPA)
            BAY: RBAM_022870(gcvPB) RBAM_022880(gcvPA)
            BPU: BPUM_2187(gcvPB) BPUM_2188(gcvPA)
            OIH: OB1902 OB1903
            GKA: GK2423 GK2424
            SAU: SA1365 SA1366
            SAV: SAV1535 SAV1536
            SAM: MW1487 MW1488
            SAR: SAR1612 SAR1613
            SAS: SAS1473 SAS1474
            SAC: SACOL1593 SACOL1594
            SAB: SAB1407c SAB1408c
            SAA: SAUSA300_1496 SAUSA300_1497
            SAO: SAOUHSC_01632 SAOUHSC_01633
            SAJ: SaurJH9_1593 SaurJH9_1594
            SAH: SaurJH1_1626 SaurJH1_1627
            SEP: SE1220 SE1221
            SER: SERP1100 SERP1101
            SHA: SH1380 SH1381
            SSP: SSP1219 SSP1220
            LMO: lmo1349 lmo1350
            LMF: LMOf2365_1366(gcvP1) LMOf2365_1367(gcvP2)
            LIN: lin1386 lin1387
            LWE: lwe1364(gcvP1) lwe1365(gcvP2)
            STH: STH1919 STH1920
            CDF: CD1657 CD1658(gcvPB)
            CBO: CBO0698(gcvP) CBO0699(gcvP')
            CBA: CLB_0737(gcvPA) CLB_0738(gcvPB)
            CBH: CLC_0752(gcvPA) CLC_0753(gcvPB)
            CBF: CLI_0767(gcvPA) CLI_0768
            CKL: CKL_1771(gcvPB) CKL_1772(gcvPA)
            AMT: Amet_0015 Amet_0016 Amet_1356 Amet_1357
            CHY: CHY_0491(gcvPA) CHY_0492(gcvPB)
            DSY: DSY2877 DSY2878
            DRM: Dred_0722 Dred_0723
            SWO: Swol_1980 Swol_1981
            TTE: TTE0293(gcvP) TTE0294(gcvP2)
            MTA: Moth_1942 Moth_1943
            MTU: Rv1832(gcvB)
            MTC: MT1880(gcvP)
            MBO: Mb1863(gcvB)
            MBB: BCG_1867(gcvB)
            MLE: ML2072(gcvB)
            MPA: MAP1545(gcvB)
            MAV: MAV_2884(gcvP)
            MSM: MSMEG_3642(gcvP)
            MVA: Mvan_3131
            MGI: Mflv_3398
            MMC: Mmcs_2840
            MKM: Mkms_2884
            MJL: Mjls_2871
            CJK: jk0209(gcvP)
            NFA: nfa24900(gcvP)
            RHA: RHA1_ro00902(gcvP1) RHA1_ro02930(gcvP2) RHA1_ro08466(gcvPb)
                 RHA1_ro08467(gcvPa)
            SCO: SCO1378(SC10A9.20c)
            SMA: SAV6987(gcvB)
            TWH: TWT135(gcvB)
            TWS: TW144(gcvP)
            CMI: CMM_2195(gcvP)
            ART: Arth_0764
            AAU: AAur_0987(gcvP) AAur_4007(gcvP)
            PAC: PPA0742
            NCA: Noca_2709
            TFU: Tfu_1398
            FRA: Francci3_4065
            FAL: FRAAL6434(gcvP)
            ACE: Acel_1222
            SEN: SACE_3842(gcvP1)
            RXY: Rxyl_3185 Rxyl_3186
            RBA: RB7584(yqhK) RB7585(yqhJ)
            PCU: pc0283(gcvP1) pc0284(gcvP2)
            TDE: TDE1624(gcvP2) TDE1625(gcvP1)
            LIL: LA0360
            LIC: LIC10309(gcvP)
            LBJ: LBJ_2732(gcvP)
            LBL: LBL_0338(gcvP) LBL_0593(metG)
            SYN: slr0293(gcvP)
            SYW: SYNW2374(gcvP)
            SYC: syc2046_c(gcvP)
            SYF: Synpcc7942_2047
            SYD: Syncc9605_2538
            SYE: Syncc9902_2188
            SYG: sync_2788(gcvP)
            SYR: SynRCC307_2390(gcvP)
            SYX: SynWH7803_2412(gcvP)
            CYA: CYA_2098(gcvP)
            CYB: CYB_0137(gcvP)
            TEL: tll1603
            GVI: glr0246
            ANA: all4607
            AVA: Ava_2762
            PMA: Pro1829(gcvP)
            PMM: PMM1668(gcvP)
            PMT: PMT2169(gcvP)
            PMN: PMN2A_1267
            PMI: PMT9312_1760
            PMB: A9601_18771(gcvP) A9601_18781(gcvH)
            PMC: P9515_18581(gcvP) P9515_18591(gcvH)
            PMF: P9303_28901(gcvP) P9303_28911(gcvH)
            PMG: P9301_18581(gcvP) P9301_18591(gcvH)
            PMH: P9215_19411(gcvP)
            PME: NATL1_21381(gcvP) NATL1_21391(gcvH)
            TER: Tery_5031
            BTH: BT_1147
            BFR: BF2025
            BFS: BF2079
            PGI: PG1305(gcvP)
            SRU: SRU_1257(gcvP)
            CHU: CHU_1021(gcvP)
            GFO: GFO_2875(gcvP)
            FPS: FP1372(gcvP)
            CTE: CT1625(gcvP1) CT2123(gcvP2)
            CCH: Cag_1658 Cag_1733
            CPH: Cpha266_0574 Cpha266_2496
            PVI: Cvib_0194 Cvib_1404
            PLT: Plut_0127 Plut_1614
            RRS: RoseRS_1522 RoseRS_1524
            RCA: Rcas_2281 Rcas_2283
            DRA: DR_1809
            DGE: Dgeo_1907
            TTH: TTC0150 TTC0151
            TTJ: TTHA0525 TTHA0526
            AAE: aq_1109(gcsP2) aq_1903(gcsP1)
            TMA: TM0213 TM0214
            TPT: Tpet_0710 Tpet_0711
            TME: Tmel_1886 Tmel_1887
            FNO: Fnod_0974 Fnod_0975
            HAL: VNG1601G(gcvP2) VNG1603G(gcvP1)
            HMA: rrnAC1498(gcvP1)
            NPH: NP4594A(gcvP2) NP4596A(gcvP1)
            TAC: Ta1357 Ta1358
            TVO: TVN0297 TVN0298
            PTO: PTO1170 PTO1171
            PHO: PH1994 PH1995
            PAB: PAB1171 PAB1172
            PFU: PF1999 PF2000
            TKO: TK1379 TK1380
            APE: APE_2121.1 APE_2124.1
            SMR: Smar_1113 Smar_1114
            SSO: SSO0917 SSO0918
            STO: ST1207 ST1208
            SAI: Saci_1381(gcvP) Saci_1382
            MSE: Msed_1664 Msed_1665
STRUCTURES  PDB: 1HPC  1HTP  1WYT  1WYU  1WYV  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.4.2
            ExPASy - ENZYME nomenclature database: 1.4.4.2
            ExplorEnz - The Enzyme Database: 1.4.4.2
            ERGO genome analysis and discovery system: 1.4.4.2
            BRENDA, the Enzyme Database: 1.4.4.2
            CAS: 37259-67-9
///
ENTRY       EC 1.4.7.1                  Enzyme
NAME        glutamate synthase (ferredoxin);
            ferredoxin-dependent glutamate synthase;
            ferredoxin-glutamate synthase;
            glutamate synthase (ferredoxin-dependent)
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With an iron-sulfur protein as acceptor
SYSNAME     L-glutamate:ferredoxin oxidoreductase (transaminating)
REACTION    2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate
            + 2 reduced ferredoxin + 2 H+ [RN:R00021]
ALL_REAC    R00021
SUBSTRATE   L-glutamate [CPD:C00025];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     L-glutamine [CPD:C00064];
            2-oxoglutarate [CPD:C00026];
            reduced ferredoxin [CPD:C00138];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023];
            Sulfur [CPD:C00087];
            Iron-sulfur [CPD:C00824];
            Flavoprotein [CPD:C06411]
COMMENT     An iron-sulfur flavoprotein.
REFERENCE   1  [PMID:16522168]
  AUTHORS   Jang JE, Shaw K, Yu XJ, Petersen D, Pepper K, Lutzko C, Kohn DB.
  TITLE     Specific and stable gene transfer to human embryonic stem cells
            using pseudotyped lentiviral vectors.
  JOURNAL   Stem. Cells. Dev. 15 (2006) 109-17.
REFERENCE   2  [PMID:4423889]
  AUTHORS   Lea PJ, Miflin BJ.
  TITLE     Alternative route for nitrogen assimilation in higher plants.
  JOURNAL   Nature. 251 (1974) 614-6.
PATHWAY     PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00284  glutamate synthase (ferredoxin)
GENES       ATH: AT2G41220(GLU2)
            OSA: 4344164
            YPP: YPDSF_0340
            ENT: Ent638_3656
            SPE: Spro_4344
            PPF: Pput_4949
            PMY: Pmen_0550
            PCR: Pcryo_2165
            PRW: PsycPRwf_0403
            SDN: Sden_2790
            SFR: Sfri_2951
            SAZ: Sama_0857
            SBL: Sbal_1178
            SBM: Shew185_1222
            SLO: Shew_1032
            SPC: Sputcn32_1136
            SSE: Ssed_1126
            SPL: Spea_1013
            SHE: Shewmr4_2872
            SHM: Shewmr7_2954
            SHN: Shewana3_3050
            SHW: Sputw3181_3028
            PAT: Patl_3748
            PIN: Ping_1007
            MAQ: Maqu_0834
            AEH: Mlg_2763
            HHA: Hhal_1056 Hhal_1617
            CSA: Csal_0615
            MMW: Mmwyl1_4114
            RMA: Rmag_1018
            REU: Reut_A3126
            BVI: Bcep1808_0384
            BUR: Bcep18194_A3499
            BCN: Bcen_2705
            BCH: Bcen2424_0402
            BAM: Bamb_0321
            PNU: Pnuc_0094
            RFR: Rfer_2933
            POL: Bpro_0791
            PNA: Pnap_0683
            AAV: Aave_1008
            AJS: Ajs_0741
            VEI: Veis_2395
            MMS: mma_0368
            NEU: NE2123
            AZO: azo3642(gltB)
            TDN: Tmden_1176
            GUR: Gura_0393
            PPD: Ppro_0729
            ADE: Adeh_0817
            AFW: Anae109_0854
            PLA: Plav_1964
            SMD: Smed_2711
            OAN: Oant_4277
            RPB: RPB_4531
            RPC: RPC_0761
            RPE: RPE_0683
            NWI: Nwi_2953
            NHA: Nham_1138
            XAU: Xaut_0477
            SIT: TM1040_2823
            RSH: Rsph17029_2807
            RSQ: Rsph17025_2781
            JAN: Jann_0251
            PDE: Pden_0488
            MMR: Mmar10_0302
            NAR: Saro_3176
            SAL: Sala_2140
            SWI: Swit_0265 Swit_0657
            ACR: Acry_1666
            MGM: Mmc1_0706
            ABA: Acid345_3680
            SUS: Acid_3816
            BCE: BC3646
            BCZ: BCZK3348(gltB)
            BCY: Bcer98_0452
            BTK: BT9727_3397(gltB)
            BPU: BPUM_0621(yerD)
            OIH: OB3408
            SAJ: SaurJH9_0493
            SAH: SaurJH1_0506
            CBE: Cbei_4204
            AMT: Amet_3397
            DRM: Dred_2805
            MAV: MAV_0166
            MSM: MSMEG_3225 MSMEG_6459
            MVA: Mvan_2822 Mvan_5698
            MGI: Mflv_1114 Mflv_3593
            MMC: Mmcs_3044 Mmcs_5066
            MKM: Mkms_3103 Mkms_5154
            MJL: Mjls_3060 Mjls_5445
            ART: Arth_1691
            NCA: Noca_3022
            FRA: Francci3_3013
            FAL: FRAAL4965(gltB)
            ACE: Acel_1078
            KRA: Krad_2961
            RXY: Rxyl_0341
            LIL: LB286(gltB2)
            LIC: LIC20220(gltB)
            SYN: sll1499(glsF)
            SYW: SYNW2132(glsF)
            SYC: syc0650_c(glsF)
            SYF: Synpcc7942_0890
            SYD: Syncc9605_0326
            SYE: Syncc9902_2016
            SYG: sync_0387
            SYR: SynRCC307_2164(gltS)
            SYX: SynWH7803_0385(gltS)
            CYA: CYA_2704(gltS)
            CYB: CYB_1253(gltS)
            TEL: tll1368(glsF)
            GVI: glr1508(glsF)
            ANA: alr4344(glsF)
            AVA: Ava_1294
            PMA: Pro1668(glsF)
            PMM: PMM1512(glsF)
            PMT: PMT1777(glsF)
            PMN: PMN2A_1078
            PMI: PMT9312_1604
            PMB: A9601_17161(gltB)
            PMC: P9515_16921(gltB)
            PMF: P9303_23581(gltB)
            PMG: P9301_17041(gltB)
            PME: NATL1_19531(gltB)
            FJO: Fjoh_2161
            FPS: FP1025
            CCH: Cag_0186
            CPH: Cpha266_0628
            PVI: Cvib_0558
            PLT: Plut_0502
            RRS: RoseRS_2985
            RCA: Rcas_1903
            DGE: Dgeo_2626
STRUCTURES  PDB: 1LLW  1LLZ  1LM1  1OFD  1OFE  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.7.1
            ExPASy - ENZYME nomenclature database: 1.4.7.1
            ExplorEnz - The Enzyme Database: 1.4.7.1
            ERGO genome analysis and discovery system: 1.4.7.1
            BRENDA, the Enzyme Database: 1.4.7.1
            CAS: 62213-56-3
///
ENTRY       EC 1.4.99.1                 Enzyme
NAME        D-amino-acid dehydrogenase;
            D-amino-acid:(acceptor) oxidoreductase (deaminating)
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With other acceptors
SYSNAME     D-amino-acid:acceptor oxidoreductase (deaminating)
REACTION    a D-amino acid + H2O + acceptor = a 2-oxo acid + NH3 + reduced
            acceptor [RN:R07166]
ALL_REAC    R07166 > R01374;
            (other) R01342
SUBSTRATE   D-amino acid [CPD:C00405];
            H2O [CPD:C00001];
            acceptor [CPD:C00028]
PRODUCT     2-oxo acid [CPD:C00161];
            NH3 [CPD:C00014];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Acts to some extent on all D-amino acids,
            except D-aspartate and D-glutamate.
REFERENCE   1  [PMID:5925166]
  AUTHORS   Tsukada K.
  TITLE     D-amino acid dehydrogenases of Pseudomonas fluorescens.
  JOURNAL   J. Biol. Chem. 241 (1966) 4522-8.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00360  Phenylalanine metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00285  D-amino-acid dehydrogenase
GENES       PIC: PICST_70688(DAD1)
            UMA: UM05259.1
            ECO: b1189(dadA)
            ECJ: JW1178(dadA)
            ECE: Z1952(dadA)
            ECS: ECs1684
            ECC: c1638(dadA)
            ECI: UTI89_C1375(dadA)
            ECP: ECP_1232
            ECV: APECO1_301(dadA)
            ECW: EcE24377A_1334(dadA)
            ECX: EcHS_A1292
            STY: STY1931(dadA)
            STT: t1074(dadA)
            SPT: SPA1070(dadA)
            SEC: SC1796(dadA)
            STM: STM1803(dadA)
            YPE: YPO2147(dadA)
            YPK: y2174(dadA)
            YPM: YP_1948(dadA1)
            YPA: YPA_1505
            YPN: YPN_1614
            YPP: YPDSF_0986
            YPS: YPTB2074(dadA)
            YPI: YpsIP31758_1997(dadA)
            SFL: SF1178(dadA)
            SFX: S1266(dadA)
            SFV: SFV_1196(dadA)
            SSN: SSON_1181(dadA)
            SBO: SBO_1883(dadA)
            SDY: SDY_1226(dadA)
            ECA: ECA2351(dadA)
            PLU: plu2561(dadA)
            ENT: Ent638_2363
            SPE: Spro_2746
            XFA: XF0851
            XFT: PD1824(dadA)
            XCC: XCC2580(dadA) XCC3648(dadA)
            XCB: XC_1538 XC_3719
            XCV: XCV2904(dadA) XCV3809(dadA2)
            XAC: XAC2751(dadA) XAC3688(dadA)
            XOO: XOO0693(dadA) XOO3288(dadA)
            XOM: XOO_0630(XOO0630) XOO_3111(XOO3111)
            VCH: VC0786
            VCO: VC0395_A0313(dadA)
            VVU: VV1_0414
            VVY: VV0781
            VPA: VP0623 VP1331
            PPR: PBPRB1593
            PAE: PA5084 PA5304(dadA)
            PAU: PA14_67150 PA14_70040(dadA)
            PPU: PP_1255 PP_3596 PP_4311 PP_4434(dadA-1) PP_5270(dadA-2)
            PPF: Pput_1556 Pput_5180
            PST: PSPTO_0101(dadA)
            PSB: Psyr_0235
            PSP: PSPPH_0223(dadA)
            PFL: PFL_2195 PFL_3591 PFL_5808(dadA) PFL_6038(dadA)
            PFO: Pfl_2305 Pfl_5290 Pfl_5526
            PEN: PSEEN1658 PSEEN2664 PSEEN4053 PSEEN5416(dadA)
            PMY: Pmen_0245
            PAR: Psyc_0158(dadA)
            PCR: Pcryo_0168 Pcryo_1218
            ACI: ACIAD0115(dadA) ACIAD0922 ACIAD1998(dadA)
            SAZ: Sama_1533
            SLO: Shew_2360
            CPS: CPS_1447 CPS_2746
            PIN: Ping_2082
            MAQ: Maqu_2864
            AEH: Mlg_0415
            HHA: Hhal_1817
            HCH: HCH_00170 HCH_03166
            CSA: Csal_2708
            MMW: Mmwyl1_3630
            AHA: AHA_1961
            NME: NMB0176
            NMA: NMA0092(dadA)
            NMC: NMC0166(dadA)
            NGO: NGO1808
            CVI: CV_1914(dadA2) CV_2823(dadA1) CV_3692
            RSO: RSc0507(RS05000) RSc0926(dadA) RSc2262(RS01297)
            REU: Reut_A1655 Reut_A2547 Reut_A2589 Reut_B3726
            REH: H16_A0770(dadA2) H16_A0817(dadA1) H16_A0841(dadA3)
                 H16_A0857(dadA4) H16_A1505(dadA5) H16_B0508(dadA6)
                 H16_B1893(dadA7) H16_B2189(dadA8)
            RME: Rmet_0700 Rmet_0740 Rmet_1877 Rmet_4441 Rmet_5580
            BMA: BMA0408(dadA) BMA1447 BMAA1933
            BMV: BMASAVP1_0948 BMASAVP1_A2551(dadA)
            BML: BMA10299_1236 BMA10299_A0927(dadA)
            BMN: BMA10247_0222 BMA10247_A2211
            BXE: Bxe_A0369 Bxe_A1001 Bxe_A2285 Bxe_B1348 Bxe_B1416 Bxe_C0404
            BVI: Bcep1808_0985 Bcep1808_1847 Bcep1808_3377 Bcep1808_6420
                 Bcep1808_6673 Bcep1808_6677
            BUR: Bcep18194_A3504 Bcep18194_A3940 Bcep18194_A4178
                 Bcep18194_A5087 Bcep18194_A5216 Bcep18194_B0064
                 Bcep18194_B0629 Bcep18194_B1893
            BCN: Bcen_0367 Bcen_0585 Bcen_1434 Bcen_2701 Bcen_3334 Bcen_6164
            BCH: Bcen2424_0406 Bcen2424_0850 Bcen2424_1064 Bcen2424_1915
                 Bcen2424_5033 Bcen2424_6394 Bcen2424_6641
            BAM: Bamb_0725 Bamb_0940 Bamb_1903 Bamb_3394 Bamb_4442
            BPS: BPSL1415 BPSL2497(dadA) BPSS0154(dadA) BPSS0574
            BPM: BURPS1710b_2464(dadA) BURPS1710b_2974(dadA)
                 BURPS1710b_A1670(dadA) BURPS1710b_A2137(dadA)
            BPL: BURPS1106A_2925 BURPS1106A_A0215
            BPD: BURPS668_2864 BURPS668_A0305
            BTE: BTH_I1656 BTH_I2134 BTH_II0223 BTH_II1840
            BPE: BP1818(dadA) BP2210 BP2634(dadA) BP3009
            BPA: BPP1901(dadA) BPP2721(dadA3) BPP3086(dadA) BPP3738
            BBR: BB2777(dadA3) BB3049(dadA) BB3089 BB3209(dadA) BB4184
            RFR: Rfer_0240 Rfer_1987
            POL: Bpro_0148 Bpro_1385 Bpro_1999 Bpro_2697 Bpro_4194
            PNA: Pnap_0094 Pnap_1756
            AAV: Aave_0131 Aave_1822 Aave_1936 Aave_2554 Aave_4507
            AJS: Ajs_0071 Ajs_2587 Ajs_3886
            VEI: Veis_0793 Veis_2001 Veis_4473 Veis_4738 Veis_5009
            MPT: Mpe_A1981 Mpe_A3520
            HAR: HEAR0360 HEAR0740(dadA) HEAR1744
            MMS: mma_0406 mma_0667 mma_1540
            EBA: ebA1192(dadA)
            AZO: azo0967(dadA1) azo3924(dadA2)
            DAR: Daro_3842
            MFA: Mfla_0791
            HPY: HP0943(dadA)
            HPJ: jhp0878(dadA)
            HPA: HPAG1_0926
            HAC: Hac_1311(dadA)
            BBA: Bd0322(dadA)
            PUB: SAR11_1368(dadA)
            MLO: mll3980 mll3992 mll6285 mlr9201
            SME: SMb20267 SMc03265
            SMD: Smed_2093 Smed_3864
            ATU: Atu3293(dadA) Atu3364 Atu4682(dadA)
            ATC: AGR_L_2918 AGR_L_3050 AGR_L_400
            RET: RHE_CH00451 RHE_PF00436(dadA)
            RLE: RL0477(dadA) RL0784 RL2917(dadA) pRL120417(dadA)
            BME: BMEI0256 BMEII0373
            BMF: BAB1_1801 BAB2_0311 BAB2_0613
            BMS: BRA0630 BRA0924(dadA)
            BMB: BruAb1_1774 BruAb2_0309(dadA) BruAb2_0596
            BOV: BOV_A0866(dadA)
            OAN: Oant_1110
            BJA: bll6812 blr2222(dadA)
            BRA: BRADO3486 BRADO4568
            BBT: BBta_1259 BBta_4795
            RPB: RPB_1124 RPB_1503 RPB_3648
            RPC: RPC_1652
            RPD: RPD_1816
            RPE: RPE_1682
            NWI: Nwi_2282
            NHA: Nham_2698
            XAU: Xaut_2304
            SIL: SPO3666 SPOA0168 SPOA0262
            SIT: TM1040_0355 TM1040_2064 TM1040_3200
            RSP: RSP_2316(dadA) RSP_3113(dadA)
            RSH: Rsph17029_0990
            JAN: Jann_1410
            RDE: RD1_0238
            PDE: Pden_0183 Pden_0804 Pden_4628 Pden_4860
            MMR: Mmar10_2102
            HNE: HNE_2416(dadA)
            SWI: Swit_0808
            GOX: GOX0632
            GBE: GbCGDNIH1_0502
            RRU: Rru_A1546 Rru_A2064
            MAG: amb2799
            BAN: BA2715
            BAR: GBAA2715
            BAA: BA_3236
            BAT: BAS2529
            BCE: BC2723
            BCA: BCE_2742
            BCZ: BCZK2454(dadA) pE33L466_0322(dadA)
            BTK: BT9727_2489(dadA)
            BCL: ABC2595
            GKA: GK1399
            LWE: lwe1929
            MSM: MSMEG_6291
            MVA: Mvan_4780
            MGI: Mflv_0955
            MMC: Mmcs_5235
            MKM: Mkms_5323
            MJL: Mjls_5615
            CGL: NCgl2909(cgl3012)
            CGB: cg3340(dadA)
            CEF: CE2845
            RHA: RHA1_ro01324 RHA1_ro02152(dadA2)
            NCA: Noca_0647
            TFU: Tfu_2797
            FRA: Francci3_3470
            FAL: FRAAL5656
            SEN: SACE_4702(dadA2) SACE_5427(dadA2)
            RXY: Rxyl_1818
            RBA: RB5278(dadA)
            AVA: Ava_5037
            PMC: P9515_00541(dadA)
            PMF: P9303_28291(dadA)
            PME: NATL1_00611(dadA)
STRUCTURES  PDB: 1FE2  1IGX  1IGZ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.99.1
            ExPASy - ENZYME nomenclature database: 1.4.99.1
            ExplorEnz - The Enzyme Database: 1.4.99.1
            ERGO genome analysis and discovery system: 1.4.99.1
            BRENDA, the Enzyme Database: 1.4.99.1
            CAS: 37205-44-0
///
ENTRY       EC 1.4.99.2                 Enzyme
NAME        taurine dehydrogenase;
            taurine:(acceptor) oxidoreductase (deaminating)
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With other acceptors
SYSNAME     taurine:acceptor oxidoreductase (deaminating)
REACTION    taurine + H2O + acceptor = sulfoacetaldehyde + NH3 + reduced
            acceptor [RN:R07167]
ALL_REAC    R07167
SUBSTRATE   taurine [CPD:C00245];
            H2O [CPD:C00001];
            acceptor [CPD:C00028]
PRODUCT     sulfoacetaldehyde [CPD:C00593];
            NH3 [CPD:C00014];
            reduced acceptor [CPD:C00030]
REFERENCE   1  [PMID:4724302]
  AUTHORS   Kondo H, Kagotani K, Oshima M, Ishimoto M.
  TITLE     Purification and some properties of taurine dehydrogenase from a
            bacterium.
  JOURNAL   J. Biochem. (Tokyo). 73 (1973) 1269-78.
  ORGANISM  bacterium
PATHWAY     PATH: map00910  Nitrogen metabolism
GENES       RDE: RD1_0829(tauX)
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.99.2
            ExPASy - ENZYME nomenclature database: 1.4.99.2
            ExplorEnz - The Enzyme Database: 1.4.99.2
            ERGO genome analysis and discovery system: 1.4.99.2
            BRENDA, the Enzyme Database: 1.4.99.2
            CAS: 50812-14-1
///
ENTRY       EC 1.4.99.3                 Enzyme
NAME        amine dehydrogenase;
            methylamine dehydrogenase;
            primary-amine dehydrogenase;
            amine: (acceptor) oxidoreductase (deaminating);
            primary-amine:(acceptor) oxidoreductase (deaminating)
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With other acceptors
SYSNAME     primary-amine:acceptor oxidoreductase (deaminating)
REACTION    RCH2NH2 + H2O + acceptor = RCHO + NH3 + reduced acceptor [RN:R01854]
ALL_REAC    R01854 > R00606
SUBSTRATE   RCH2NH2 [CPD:C00375];
            H2O [CPD:C00001];
            acceptor [CPD:C00028]
PRODUCT     RCHO [CPD:C00071];
            NH3 [CPD:C00014];
            reduced acceptor [CPD:C00030]
COFACTOR    PQQ [CPD:C00113]
COMMENT     A quinoprotein.
REFERENCE   1  [PMID:6246962]
  AUTHORS   de Beer R, Duine JA, Frank J, Large PJ.
  TITLE     The prosthetic group of methylamine dehydrogenase from Pseudomonas
            AM1: evidence for a quinone structure.
  JOURNAL   Biochim. Biophys. Acta. 622 (1980) 370-4.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:4388687]
  AUTHORS   Eady RR, Large PJ.
  TITLE     Purification and properties of an amine dehydrogenase from
            Pseudomonas AM1 and its role in growth on methylamine.
  JOURNAL   Biochem. J. 106 (1968) 245-55.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:5124384]
  AUTHORS   Eady RR, Large PJ.
  TITLE     Microbial oxidation of amines. Spectral and kinetic properties of
            the primary amine dehydrogenase of Pseudomonas AM1.
  JOURNAL   Biochem. J. 123 (1971) 757-71.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00680  Methane metabolism
ORTHOLOGY   KO: K08685  amine dehydrogenase
GENES       PEN: PSEEN2552 PSEEN2555
            PAT: Patl_0157 Patl_0160
            REU: Reut_B4077 Reut_B4080
            BUR: Bcep18194_B0601 Bcep18194_B0604
            BCN: Bcen_3305 Bcen_3308
            BCH: Bcen2424_5059 Bcen2424_5062
            BAM: Bamb_4469 Bamb_4472
            AZO: azo1239(qhpA) azo2257(mauA) azo2260(mauB)
            MFA: Mfla_0548 Mfla_0551
            PDE: Pden_4730 Pden_4733
            NAR: Saro_1685 Saro_1688
            SWI: Swit_3251 Swit_3254 Swit_4365
STRUCTURES  PDB: 1MAE  1MAF  1MDA  1MG2  1MG3  1PBY  2BBK  2GC4  2GC7  2J55  
                 2J56  2J57  2MAD  2MTA  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.99.3
            ExPASy - ENZYME nomenclature database: 1.4.99.3
            ExplorEnz - The Enzyme Database: 1.4.99.3
            ERGO genome analysis and discovery system: 1.4.99.3
            UM-BBD (Biocatalysis/Biodegradation Database): 1.4.99.3
            BRENDA, the Enzyme Database: 1.4.99.3
            CAS: 60496-14-2
///
ENTRY       EC 1.4.99.4                 Enzyme
NAME        aralkylamine dehydrogenase;
            aromatic amine dehydrogenase;
            dehydrogenase, arylamine;
            tyramine dehydrogenase;
            aromatic amine dehydrogenase;
            aralkylamine:(acceptor) oxidoreductase (deaminating)
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With other acceptors
SYSNAME     aralkylamine:acceptor oxidoreductase (deaminating)
REACTION    RCH2NH2 + H2O + acceptor = RCHO + NH3 + reduced acceptor [RN:R01854]
ALL_REAC    R01854 > R02612;
            (other) R02382 R04300
SUBSTRATE   RCH2NH2 [CPD:C00375];
            H2O [CPD:C00001];
            acceptor [CPD:C00028]
PRODUCT     RCHO [CPD:C00071];
            NH3 [CPD:C00014];
            reduced acceptor [CPD:C00030]
COMMENT     Phenazine methosulfate can act as acceptor. Acts on aromatic amines
            and, more slowly, on some long-chain aliphatic amines, but not on
            methylamine or ethylamine (cf. EC 1.4.99.3 amine dehydrogenase).
REFERENCE   1  [PMID:6830237]
  AUTHORS   Iwaki M, Yagi T, Horiike K, Saeki Y, Ushijima T, Nozaki M.
  TITLE     Crystallization and properties of aromatic amine dehydrogenase from
            Pseudomonas sp.
  JOURNAL   Arch. Biochem. Biophys. 220 (1983) 253-62.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
STRUCTURES  PDB: 2AGL  2AGW  2AGX  2AGY  2AGZ  2AH0  2AH1  2H3X  2H47  2HXC  
                 2I0R  2I0S  2I0T  2IAA  2IUP  2IUQ  2IUR  2IUV  2OIZ  2OJY  
                 2OK4  2OK6  2Q7Q  
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.99.4
            ExPASy - ENZYME nomenclature database: 1.4.99.4
            ExplorEnz - The Enzyme Database: 1.4.99.4
            ERGO genome analysis and discovery system: 1.4.99.4
            BRENDA, the Enzyme Database: 1.4.99.4
            CAS: 85030-73-5
///
ENTRY       EC 1.4.99.5                 Enzyme
NAME        glycine dehydrogenase (cyanide-forming);
            hydrogen cyanide synthase;
            HCN synthase
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors;
            With other acceptors
SYSNAME     glycine:acceptor oxidoreductase (hydrogen-cyanide-forming)
REACTION    glycine + 2 A = hydrogen cyanide + CO2 + 2 AH2 [RN:R05704]
ALL_REAC    R05704
SUBSTRATE   glycine [CPD:C00037];
            A [CPD:C00028]
PRODUCT     hydrogen cyanide [CPD:C01326];
            CO2 [CPD:C00011];
            AH2 [CPD:C00030]
COMMENT     The enzyme from Pseudomonas sp. contains FAD. The enzyme is
            membrane-bound, and the 2-electron acceptor is a component of the
            respiratory chain. The enzyme can act with various artificial
            electron acceptors, including phenazine methosulfate.
REFERENCE   1  [PMID:234422]
  AUTHORS   Wissing F.
  TITLE     Cyanide production from glycine by a homogenate from a Pseudomonas
            species.
  JOURNAL   J. Bacteriol. 121 (1975) 695-9.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:233722]
  AUTHORS   Castric PA.
  TITLE     Glycine metabolism by Pseudomonas aeruginosa: hydrogen cyanide
            biosynthesis.
  JOURNAL   J. Bacteriol. 130 (1977) 826-31.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   3  [PMID:9620970]
  AUTHORS   Laville J, Blumer C, Von Schroetter C, Gaia V, Defago G, Keel C,
            Haas D.
  TITLE     Characterization of the hcnABC gene cluster encoding hydrogen
            cyanide synthase and anaerobic regulation by ANR in the strictly
            aerobic biocontrol agent Pseudomonas fluorescens CHA0.
  JOURNAL   J. Bacteriol. 180 (1998) 3187-96.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   4  [PMID:10763748]
  AUTHORS   Blumer C, Haas D.
  TITLE     Mechanism, regulation, and ecological role of bacterial cyanide
            biosynthesis.
  JOURNAL   Arch. Microbiol. 173 (2000) 170-7.
  ORGANISM  Pseudomonas aeruginosa, Pseudomonas fluorescens
GENES       PFL: PFL_2577(hcnA) PFL_2578(hcnB) PFL_2579(hcnC)
DBLINKS     IUBMB Enzyme Nomenclature: 1.4.99.5
            ExPASy - ENZYME nomenclature database: 1.4.99.5
            ExplorEnz - The Enzyme Database: 1.4.99.5
            ERGO genome analysis and discovery system: 1.4.99.5
            BRENDA, the Enzyme Database: 1.4.99.5
///
ENTRY       EC 1.4.-.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on the CH-NH2 group of donors
REACTION    (1) Anthranilyl-CoA + 2 H+ <=> S-Benzoate coenzyme A + NH3
            [RN:R05585];
            (2) 4-Hydroxyaniline + H2O <=> p-Benzoquinone + NH3 [RN:R06852];
            (3) o-Hydroxylaminobenzoate + 2 H+ <=> Anthranilate + H2O
            [RN:R07734]
SUBSTRATE   Anthranilyl-CoA [CPD:C02247];
            H+ [CPD:C00080];
            4-Hydroxyaniline [CPD:C02372];
            H2O [CPD:C00001]
PRODUCT     S-Benzoate coenzyme A [CPD:C00512];
            NH3 [CPD:C00014];
            p-Benzoquinone [CPD:C00472]
///
ENTRY       EC 1.5.1.1                  Enzyme
NAME        pyrroline-2-carboxylate reductase;
            Delta1-pyrroline-2-carboxylate reductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-proline:NAD(P)+ 2-oxidoreductase
REACTION    L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+
            [RN:R01246 R01249]
ALL_REAC    R01246 R01249;
            (other) R02201 R02203
SUBSTRATE   L-proline [CPD:C00148];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     1-pyrroline-2-carboxylate [CPD:C03564];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Reduces 1-pyrroline-2-carboxylate to L-proline and also
            1,2-didehydropiperidine-2-carboxylate to L-pipecolate.
REFERENCE   1
  AUTHORS   Meister, A., Radhakrishnan, A.N. and Buckley, S.D.
  TITLE     Enzymatic synthesis of L-pipecolic acid and L-proline.
  JOURNAL   J. Biol. Chem. 229 (1957) 789-800.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00310  Lysine degradation
            PATH: map00330  Arginine and proline metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.1
            ExPASy - ENZYME nomenclature database: 1.5.1.1
            ExplorEnz - The Enzyme Database: 1.5.1.1
            ERGO genome analysis and discovery system: 1.5.1.1
            BRENDA, the Enzyme Database: 1.5.1.1
            CAS: 9029-16-7
///
ENTRY       EC 1.5.1.2                  Enzyme
NAME        pyrroline-5-carboxylate reductase;
            proline oxidase;
            L-proline oxidase;
            1-pyrroline-5-carboxylate reductase;
            NADPH-L-Delta1-pyrroline carboxylic acid reductase;
            L-proline-NAD(P)+ 5-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-proline:NAD(P)+ 5-oxidoreductase
REACTION    L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H + H+
            [RN:R01248 R01251]
ALL_REAC    R01248 R01251;
            (other) R03291 R03293
SUBSTRATE   L-proline [CPD:C00148];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     1-pyrroline-5-carboxylate [CPD:C03912];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also reduces 1-pyrroline-3-hydroxy-5-carboxylate to
            L-hydroxyproline.
REFERENCE   1
  AUTHORS   Adams, E. and Goldstone, A.
  TITLE     Hydroxyproline metabolism. III. Enzymatic synthesis of
            hydroxyproline from Delta1-pyrroline-3-hydroxy-5-carboxylate.
  JOURNAL   J. Biol. Chem. 235 (1960) 3499-3503.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2
  AUTHORS   Meister, A., Radhakrishnan, A.N. and Buckley, S.D.
  TITLE     Enzymatic synthesis of L-pipecolic acid and L-proline.
  JOURNAL   J. Biol. Chem. 229 (1957) 789-800.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Smith, M.E. and Greenberg, D.M.
  TITLE     Characterization of an enzyme reducing pyrroline-5-carboxylate to
            proline.
  JOURNAL   Nature (Lond.) 177 (1956) 1130.
REFERENCE   4
  AUTHORS   Yura, T. and Vogel, H.J.
  TITLE     Pyrroline-5-carboxylate reductase of Neurospora crassa: partial
            purification and some properties.
  JOURNAL   J. Biol. Chem. 234 (1959) 335-338.
  ORGANISM  Neurospora crassa [GN:dncr]
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K00286  pyrroline-5-carboxylate reductase
GENES       HSA: 29920(PYCR2) 5831(PYCR1) 65263(PYCRL)
            PTR: 454977(PYCR1) 472886(PYCRL)
            MMU: 209027(Pycr1) 69051(Pycr2)
            RNO: 364064(Pycr2)
            CFA: 483372(PYCR1)
            GGA: 420293(PYCRL)
            XLA: 432159(MGC81282)
            DRE: 393799(zgc:73112) 560682(pycrl)
            SPU: 583853(LOC583853)
            DME: Dmel_CG6009(P5cr)
            CEL: F55G1.9 M153.1
            ATH: AT5G14800(P5CR)
            OSA: 4325755
            CME: CMH137C CMI158C
            SCE: YER023W(PRO3)
            AGO: AGOS_ABR168W
            PIC: PICST_35750(PRO3)
            CGR: CAGL0I08283g
            SPO: SPAPYUG7.05
            ANI: AN4355.2 AN6025.2 AN7387.2 AN9279.2
            AFM: AFUA_3G02310 AFUA_5G14770
            AOR: AO090005000035 AO090012000119 AO090120000046 AO090206000124
            CNE: CNF00740
            UMA: UM00547.1
            PFA: MAL13P1.284
            CPV: cgd6_3720
            CHO: Chro.60426
            TET: TTHERM_00107210
            TBR: Tb927.7.2440
            TCR: 506857.20 509207.90
            LMA: LmjF13.1680
            ECO: b0386(proC)
            ECJ: JW0377(proC)
            ECE: Z0482(proC)
            ECS: ECs0437
            ECC: c0493(proC)
            ECI: UTI89_C0405(proC)
            ECP: ECP_0445
            ECV: APECO1_1622(proC)
            ECW: EcE24377A_0413(proC)
            ECX: EcHS_A0454
            STY: STY0419(proC)
            STT: t2478(proC)
            SPT: SPA2337(proC)
            SEC: SC0427(proC)
            STM: STM0386(proC)
            YPE: YPO0942(proC)
            YPK: y3328(proC)
            YPM: YP_3500(proC)
            YPA: YPA_0323
            YPN: YPN_3139
            YPP: YPDSF_0573
            YPS: YPTB3214(proC)
            YPI: YpsIP31758_0829(proC)
            SFL: SF0322(proC)
            SFX: S0330(proC)
            SFV: SFV_0351(proC)
            SSN: SSON_0362(proC)
            SBO: SBO_0282(proC)
            SDY: SDY_0356(proC)
            ECA: ECA3628(proC)
            PLU: plu1179(proC)
            WBR: WGLp079(proC)
            SGL: SG2028
            ENT: Ent638_0857
            SPE: Spro_4031
            HIN: HI0307(proC)
            HIT: NTHI0426(proC)
            HIP: CGSHiEE_01515
            HSO: HS_1285(proC)
            PMU: PM0095(proC)
            MSU: MS1799(proC)
            APL: APL_0160(proC)
            ASU: Asuc_1764
            XFA: XF2712
            XFT: PD2064(proC)
            XCC: XCC2757(proC)
            XCB: XC_1356
            XCV: XCV3070(proC)
            XAC: XAC2926(proC)
            XOO: XOO1416(proC)
            XOM: XOO_1300(XOO1300)
            VCH: VC0460
            VCO: VC0395_A0012(proC)
            VVU: VV1_1524
            VVY: VV2875
            VPA: VP2617
            VFI: VF0429
            PPR: PBPRA3144
            PAE: PA0393(proC)
            PAU: PA14_05150(proC)
            PAP: PSPA7_0493(proC)
            PPU: PP_5095(proC-2)
            PPF: Pput_4968
            PST: PSPTO_5047(proC)
            PSB: Psyr_0476
            PSP: PSPPH_0467(proC)
            PFL: PFL_5839(proC)
            PFO: Pfl_5320
            PEN: PSEEN0317(proC)
            PMY: Pmen_4151
            PAR: Psyc_0165(proC)
            PCR: Pcryo_0177
            PRW: PsycPRwf_0337
            ACI: ACIAD3032(proC)
            ACB: A1S_0610
            SON: SO_3354(proC)
            SDN: Sden_2683
            SFR: Sfri_0761 Sfri_2861
            SAZ: Sama_2478
            SBL: Sbal_3026
            SBM: Shew185_3041
            SLO: Shew_1136 Shew_3016
            SPC: Sputcn32_2688
            SSE: Ssed_1231
            SPL: Spea_1126
            SHE: Shewmr4_1192
            SHM: Shewmr7_1263
            SHN: Shewana3_1193
            SHW: Sputw3181_1323
            ILO: IL1975(proC)
            CPS: CPS_3664(proC)
            PHA: PSHAa2605(proC)
            PAT: Patl_3719
            SDE: Sde_3642
            PIN: Ping_3041
            MAQ: Maqu_0535
            CBU: CBU_2090(proC)
            CBD: COXBU7E912_2189(proC)
            LPN: lpg2015(proC)
            LPF: lpl1992(proC)
            LPP: lpp1997(proC)
            MCA: MCA1535(proC)
            FTU: FTT1559c(proC)
            FTF: FTF1559c(proC)
            FTW: FTW_0368(proC)
            FTL: FTL_0549
            FTH: FTH_0551(proC)
            FTA: FTA_0582(proC)
            FTN: FTN_1467(proC)
            TCX: Tcr_1837
            NOC: Noc_3002
            AEH: Mlg_0340
            HHA: Hhal_0946
            HCH: HCH_06354(proC)
            CSA: Csal_3055
            ABO: ABO_2668(proC)
            MMW: Mmwyl1_0546
            AHA: AHA_3663(proC)
            DNO: DNO_0674(proC)
            RMA: Rmag_0116
            VOK: COSY_0121(proC)
            NME: NMB0055
            NMA: NMA0215(proC)
            NMC: NMC0039(proC)
            NGO: NGO1905
            CVI: CV_0177(proC)
            RSO: RSc2684(proC)
            REU: Reut_A2802
            REH: H16_A3106(proC)
            RME: Rmet_2938
            BMA: BMA2410(proC)
            BMV: BMASAVP1_A0327(proC)
            BML: BMA10299_A1188(proC)
            BMN: BMA10247_2597(proC)
            BXE: Bxe_A3982
            BVI: Bcep1808_0691
            BUR: Bcep18194_A3816
            BCN: Bcen_0246
            BCH: Bcen2424_0730
            BAM: Bamb_0620
            BPS: BPSL2847
            BPM: BURPS1710b_3347(proC)
            BPL: BURPS1106A_3334(proC)
            BPD: BURPS668_3300(proC)
            BTE: BTH_I1287(proC)
            PNU: Pnuc_1785
            BPE: BP1280(proC)
            BPA: BPP1311(proC) BPP2943(proC)
            BBR: BB2376(proC) BB2911(proC)
            RFR: Rfer_3679
            POL: Bpro_0475
            PNA: Pnap_0327
            AAV: Aave_0601
            AJS: Ajs_0381
            VEI: Veis_2325
            MPT: Mpe_A3746
            HAR: HEAR0291(proC)
            MMS: mma_0342
            NEU: NE0393(proC)
            NET: Neut_2148
            NMU: Nmul_A0581
            EBA: ebA1766(proC)
            AZO: azo3466(proC)
            DAR: Daro_3885
            TBD: Tbd_2417
            MFA: Mfla_2109
            HPY: HP1158
            HPA: HPAG1_1097
            HHE: HH0842(proC)
            HAC: Hac_1325(proC)
            WSU: WS1975(proC)
            TDN: Tmden_0791
            CJE: Cj1076(proC)
            CJR: CJE1219(proC)
            CJJ: CJJ81176_1094(proC)
            CJU: C8J_1017(proC)
            CJD: JJD26997_0647(proC)
            CFF: CFF8240_1569
            CCV: CCV52592_0752(proC) CCV52592_1603(proC)
            CHA: CHAB381_0551(proC)
            ABU: Abu_0590(proC)
            NIS: NIS_1350(proC)
            SUN: SUN_1761(proC)
            GSU: GSU2541(proC)
            GME: Gmet_0899
            GUR: Gura_0979
            PCA: Pcar_0397
            PPD: Ppro_2828
            DVU: DVU2332(proC)
            DVL: Dvul_0926
            DDE: Dde_1440
            LIP: LI1120(proC)
            BBA: Bd0465(proC)
            DPS: DP2233
            ADE: Adeh_2480
            AFW: Anae109_1387
            SAT: SYN_02197
            SFU: Sfum_0197
            ERU: Erum0030(proC)
            ERW: ERWE_CDS_09480(proC)
            ERG: ERGA_CDS_09400(proC)
            ECN: Ecaj_0941
            ECH: ECH_0013
            PUB: SAR11_1353
            MLO: mll6498
            MES: Meso_0151
            PLA: Plav_2265
            SME: SMc02677(proC)
            SMD: Smed_2249 Smed_5474
            ATU: Atu2209(proC)
            ATC: AGR_C_4015
            RET: RHE_CH03015(proC)
            RLE: RL3460(proC) pRL120421(proC)
            BME: BMEII0509
            BMF: BAB2_0456(proC)
            BMS: BRA0782(proC)
            BMB: BruAb2_0450(proC)
            BOV: BOV_A0732(proC)
            OAN: Oant_3963
            BJA: blr7454(proC)
            BRA: BRADO6035(proC)
            BBT: BBta_1743(proC)
            RPA: RPA4366(proC)
            RPB: RPB_4171
            RPC: RPC_1406
            RPD: RPD_3882
            RPE: RPE_1427
            NWI: Nwi_2514
            NHA: Nham_3106
            XAU: Xaut_2538
            CCR: CC_0494
            SIL: SPO0911(proC)
            SIT: TM1040_0623
            RSP: RSP_3364(proC)
            RSH: Rsph17029_3009
            RSQ: Rsph17025_1323
            JAN: Jann_3328
            RDE: RD1_2848 RD1_3497(proC)
            PDE: Pden_2198 Pden_4871
            MMR: Mmar10_0764 Mmar10_2668
            HNE: HNE_1387(proC)
            ZMO: ZMO0311(proC) ZMO1303(proC)
            NAR: Saro_1142
            SAL: Sala_0045
            SWI: Swit_4472
            ELI: ELI_01840
            GOX: GOX1131
            GBE: GbCGDNIH1_2307
            ACR: Acry_2704
            RRU: Rru_A3281
            MAG: amb0545
            MGM: Mmc1_3656
            ABA: Acid345_1478
            BSU: BG10841(proG) BG11049(proH) BG11744(yqjO)
            BHA: BH0887 BH1503
            BAN: BA0197 BA2995(proC-1) BA3143(proC-2) BA4359(proC-3)
            BAR: GBAA0197 GBAA2995(proC-1) GBAA3143(proC-2) GBAA4359(proC-3)
            BAA: BA_0778 BA_3501 BA_3644 BA_4817
            BAT: BAS0198 BAS2783 BAS2921 BAS4045
            BCE: BC0218 BC2977(proC) BC3109(proC) BC4134
            BCA: BCE_0217 BCE_3031(proC) BCE_4207(proC)
            BCZ: BCZK0188(proC) BCZK2713(proC) BCZK2850(proC) BCZK3891(proC)
            BCY: Bcer98_0197 Bcer98_2833 Bcer98_3054
            BTK: BT9727_0185(proC) BT9727_2732(proC) BT9727_2899(proC)
                 BT9727_3883(proC)
            BTL: BALH_0197(proC) BALH_2680(proC) BALH_2813(proC)
                 BALH_3751(proC) BALH_3916(comER)
            BLI: BL00796(proI) BL01982(proH) BL03773(proG)
            BLD: BLi01391(proG) BLi02150(proH) BLi02549(proI)
            BCL: ABC1247 ABC1765(proI)
            BAY: RBAM_018650 RBAM_021930
            BPU: BPUM_1824 BPUM_2109 BPUM_2294(comER)
            OIH: OB0013
            GKA: GK2331
            SAU: SA1334
            SAV: SAV1503
            SAM: MW1457
            SAR: SAR1579
            SAS: SAS1443
            SAC: SACOL1546(proC)
            SAB: SAB1364
            SAA: SAUSA300_1452(proC)
            SAO: SAOUHSC_01597
            SAJ: SaurJH9_1560
            SAH: SaurJH1_1591
            SEP: SE1186
            SER: SERP1065(proC)
            SHA: SH1413
            SSP: SSP1250
            LMO: lmo0396 lmo1387
            LMF: LMOf2365_0408(proC) LMOf2365_1406
            LIN: lin0414 lin1424
            LWE: lwe0344(proC) lwe1403
            LLA: L135991(proC)
            LLC: LACR_2080
            LLM: llmg_2077(proC)
            SPY: SPy_0112(proC)
            SPZ: M5005_Spy_0096(proC)
            SPM: spyM18_0113
            SPG: SpyM3_0088(proC)
            SPS: SPs0089
            SPH: MGAS10270_Spy0098(proC)
            SPI: MGAS10750_Spy0103(proC)
            SPJ: MGAS2096_Spy0099(proC)
            SPK: MGAS9429_Spy0097(proC)
            SPF: SpyM50094(proC)
            SPA: M6_Spy0144
            SPB: M28_Spy0094(proC)
            SPN: SP_0933
            SPR: spr0834(proC)
            SPD: SPD_0824(proC)
            SAG: SAG0173(proC)
            SAN: gbs0171
            SAK: SAK_0239(proC)
            SMU: SMU.1974(proC)
            STC: str1852(proC)
            STL: stu1852(proC)
            SSA: SSA_1074(proC)
            SGO: SGO_1099(proC)
            LPL: lp_0561(proC)
            LAC: LBA1116
            LSA: LSA1590(proC)
            LSL: LSL_1264(proC)
            LBR: LVIS_0538
            LCA: LSEI_1809
            LRE: Lreu_0033 Lreu_0344
            EFA: EF0961 EF2424
            OOE: OEOE_0946
            STH: STH1086
            CAC: CAC3252(proC)
            CPE: CPE2633(proC)
            CPF: CPF_2969(proC)
            CPR: CPR_2647(proC)
            CTC: CTC02431(proC)
            CNO: NT01CX_0903(proC)
            CTH: Cthe_0672
            CDF: CD1495(proC1) CD3281(proC2)
            CBO: CBO3182(proC)
            CBA: CLB_3218(proC)
            CBH: CLC_3092(proC)
            CBF: CLI_3321(proC)
            CBE: Cbei_5077
            CKL: CKL_0326(proC1) CKL_2737(proC2)
            AMT: Amet_2533
            CHY: CHY_2041(proC)
            DSY: DSY1385
            DRM: Dred_1168
            SWO: Swol_0955
            CSC: Csac_1902
            TTE: TTE1361(proC)
            MTA: Moth_0860
            MFL: Mfl045
            MTU: Rv0500(proC)
            MTC: MT0520(proC)
            MBO: Mb0511(proC)
            MBB: BCG_0542(proC)
            MLE: ML2430(proC)
            MPA: MAP3991(proC)
            MAV: MAV_4652(proC)
            MSM: MSMEG_0943(proC)
            MVA: Mvan_0837
            MGI: Mflv_0075
            MMC: Mmcs_0668
            MKM: Mkms_0681
            MJL: Mjls_0661
            CGL: NCgl0398(cgl0410)
            CGB: cg0490(proC)
            CEF: CE0430(proC)
            CDI: DIP0394(proC)
            CJK: jk1906(proC)
            NFA: nfa51770(proC)
            RHA: RHA1_ro02061
            SCO: SCO3337(proC)
            SMA: SAV4724(proC)
            TWH: TWT752(proC)
            TWS: TW764(proC)
            LXX: Lxx01720(proC)
            ART: Arth_3348
            AAU: AAur_3330(proC)
            PAC: PPA0319
            NCA: Noca_0481
            TFU: Tfu_2708
            FRA: Francci3_0476
            FAL: FRAAL0974(proC)
            ACE: Acel_0247
            KRA: Krad_0610
            SEN: SACE_6959(proC)
            STP: Strop_3266
            BLO: BL0927(proC)
            BAD: BAD_0608(proC)
            RXY: Rxyl_1485
            RBA: RB3891(proC)
            PCU: pc1132(proC)
            TPA: TP0797
            LIL: LA1481(proC)
            LIC: LIC12275(proC)
            LBJ: LBJ_0981(proC)
            LBL: LBL_2052(proC)
            SYN: slr0661(proC)
            SYW: SYNW0662(proC)
            SYC: syc2035_d(proC)
            SYF: Synpcc7942_2058
            SYD: Syncc9605_2023
            SYE: Syncc9902_0649
            SYG: sync_0601(proC)
            SYR: SynRCC307_0471(proC)
            SYX: SynWH7803_0573(proC)
            CYA: CYA_0863(proC)
            CYB: CYB_1749(proC)
            TEL: tlr1217(proC)
            GVI: glr0704
            ANA: alr0488
            AVA: Ava_1616 Ava_2901
            PMA: Pro0393(proC)
            PMM: PMM0396(proC)
            PMT: PMT0208(proC)
            PMN: PMN2A_1731
            PMI: PMT9312_0392
            PMB: A9601_04471(proC)
            PMC: P9515_04581(proC)
            PMF: P9303_21461(proC)
            PMG: P9301_04161(proC)
            PMH: P9215_04731
            PME: NATL1_04481(proC)
            TER: Tery_4908
            BTH: BT_1902 BT_3757
            BFR: BF0530
            BFS: BF0478
            SRU: SRU_1560(proC)
            CHU: CHU_0937(proC)
            GFO: GFO_1961(proC) GFO_2105
            FJO: Fjoh_0842
            FPS: FP0066(proC)
            CTE: CT0077(proC)
            CCH: Cag_1680
            CPH: Cpha266_2466
            PVI: Cvib_0217
            PLT: Plut_0150
            DET: DET0193(proC)
            DEH: cbdb_A200(proC)
            DEB: DehaBAV1_0160
            RRS: RoseRS_0390
            RCA: Rcas_1154
            DRA: DR_1522
            DGE: Dgeo_0841
            TTH: TTC0500
            TTJ: TTHA0852
            AAE: aq_166(proC)
            TMA: TM0578
            TPT: Tpet_0340
            MAC: MA4102(proC)
            MBA: Mbar_A0480
            MMA: MM_0817
            MBU: Mbur_2111
            MEM: Memar_1294
            MST: Msp_1314(proC)
            MSI: Msm_0089
            HWA: HQ1846A(proC)
            NPH: NP3974A(proC)
            TAC: Ta0139
            TVO: TVN1139
            PTO: PTO1416
            PFU: PF1715
            TKO: TK0272 TK0273
            APE: APE_0146.1
            HBU: Hbut_0328
            SSO: SSO0495(proC)
            STO: ST0646
            MSE: Msed_0977
            PAI: PAE1917
            TPE: Tpen_1839
STRUCTURES  PDB: 2AHR  2GER  2GR9  2GRA  2IZZ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.2
            ExPASy - ENZYME nomenclature database: 1.5.1.2
            ExplorEnz - The Enzyme Database: 1.5.1.2
            ERGO genome analysis and discovery system: 1.5.1.2
            BRENDA, the Enzyme Database: 1.5.1.2
            CAS: 9029-17-8
///
ENTRY       EC 1.5.1.3                  Enzyme
NAME        dihydrofolate reductase;
            tetrahydrofolate dehydrogenase;
            DHFR;
            pteridine reductase:dihydrofolate reductase;
            dihydrofolate reductase:thymidylate synthase;
            thymidylate synthetase-dihydrofolate reductase;
            folic acid reductase;
            folic reductase;
            dihydrofolic acid reductase;
            dihydrofolic reductase;
            7,8-dihydrofolate reductase;
            NADPH-dihydrofolate reductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     5,6,7,8-tetrahydrofolate:NADP+ oxidoreductase
REACTION    5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+
            [RN:R00939]
ALL_REAC    R00939;
            (other) R00936 R00937 R00940 R02235 R02236
SUBSTRATE   5,6,7,8-tetrahydrofolate [CPD:C00101];
            NADP+ [CPD:C00006]
PRODUCT     7,8-dihydrofolate [CPD:C00415];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
INHIBITOR   Methotrexate [CPD:C01937];
            Trimethoprim [CPD:C01965]
COMMENT     The enzyme from animals and some micro-organisms also slowly reduces
            folate to 5,6,7,8-tetrahydrofolate.
REFERENCE   1
  AUTHORS   Blakley, R.L. and MacDougall, B.M.
  TITLE     Dihydrofolic reductase from Streptococcus faecalis R.
  JOURNAL   J. Biol. Chem. 236 (1961) 1163.
  ORGANISM  Streptococcus faecalis
REFERENCE   2  [PMID:6815178]
  AUTHORS   Bolin JT, Filman DJ, Matthews DA, Hamlin RC, Kraut J.
  TITLE     Crystal structures of Escherichia coli and Lactobacillus casei
            dihydrofolate reductase refined at 1.7 A resolution. I. General
            features and binding of methotrexate.
  JOURNAL   J. Biol. Chem. 257 (1982) 13650-62.
  ORGANISM  Escherichia coli [GN:eco], Lactobacillus casei [GN:lca]
REFERENCE   3  [PMID:4379915]
  AUTHORS   Kaufman BT, Gardiner RC.
  TITLE     Studies on dihydrofolic reductase. I. Purification and properties of
            dihydrofolic reductase from chicken liver.
  JOURNAL   J. Biol. Chem. 241 (1966) 1319-28.
  ORGANISM  chicken [GN:gga]
REFERENCE   4  [PMID:4306838]
  AUTHORS   Young IG, Gibson F.
  TITLE     Regulation of the enzymes involved in the biosynthesis of
            2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia
            coli.
  JOURNAL   Biochim. Biophys. Acta. 177 (1969) 401-11.
PATHWAY     PATH: map00670  One carbon pool by folate
            PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K00287  dihydrofolate reductase
GENES       HSA: 1719(DHFR)
            MMU: 13361(Dhfr)
            RNO: 24312(Dhfr)
            CFA: 609048(DHFR)
            BTA: 508809(DHFR)
            GGA: 427317(DHFR)
            XLA: 495375(LOC495375)
            DRE: 81882(dhfr)
            SPU: 575335(LOC575335)
            DME: Dmel_CG14887(Dhfr)
            CEL: C36B1.7
            ATH: AT2G16370(THY-1)
            OSA: 4350527
            CME: CMS462C
            SCE: YOR236W(DFR1)
            AGO: AGOS_ACR124W
            PIC: PICST_38512(FSH1) PICST_60284(FSH3) PICST_82622(DFR1)
            CGR: CAGL0J00385g CAGL0J03894g CAGL0L11044g
            SPO: SPCC1223.08c(dfr1)
            AFM: AFUA_2G08890 AFUA_3G06620
            AOR: AO090020000337
            CNE: CNJ01940
            UMA: UM03183.1 UM06281.1
            ECU: ECU08_0080
            DDI: DDB_0230113
            PFA: PFD0805w
            CPV: cgd4_4460
            CHO: Chro.40506
            TAN: TA08775
            TPV: TP04_0504
            TET: TTHERM_00312120
            TBR: Tb927.7.5480
            TCR: 509153.90 510303.320
            LMA: LmjF06.0860
            ECO: b0048(folA) b1606(folM)
            ECJ: JW0047(folA)
            ECE: Z0055
            ECS: ECs0051
            ECC: c0058(folA)
            ECI: UTI89_C0054(folA)
            ECP: ECP_0048
            ECV: APECO1_1934(folA)
            ECW: EcE24377A_0052(folA)
            ECX: EcHS_A0054(folA)
            STY: HCM1.165c(dhfR) HCM2.0117c STY0102(folA)
            STT: t0090(folA)
            SPT: SPA0088(folA)
            SEC: SC0082(folA) SC030(tri)
            STM: STM0087(folA)
            YPE: YPO0486(folA)
            YPK: y3688(folA)
            YPM: YP_3693(folA)
            YPA: YPA_4079
            YPN: YPN_0359
            YPP: YPDSF_3147
            YPS: YPTB0628(folA)
            YPI: YpsIP31758_3449(folA)
            SFL: SF0045(folA)
            SFX: S0047(folA)
            SFV: SFV_0042(folA)
            SSN: SSON_0056(folA)
            SBO: SBO_0037(folA)
            SDY: SDY_0071(folA)
            ECA: ECA3864(folA)
            PLU: plu0606(folA)
            BUC: BU143(folA)
            BAS: BUsg136(folA)
            BAB: bbp133(folA)
            WBR: WGLp022(folA)
            SGL: SG0421
            ENT: Ent638_0597
            SPE: Spro_0720
            BFL: Bfl124(folA)
            BPN: BPEN_128(folA)
            HIN: HI0899(folA)
            HIT: NTHI1065(folA)
            HDU: HD1118(folA)
            HSO: HS_0189(folA)
            PMU: PM1893(folA)
            MSU: MS1858(folA)
            APL: APL_0883(folA)
            ASU: Asuc_0714
            XFA: XF2331
            XFT: PD1363(folA)
            XCC: XCC0788(folA)
            XCB: XC_3443
            XCV: XCV0897(folA)
            XAC: XAC0844(folA)
            XOO: XOO3751(folA)
            XOM: XOO_3541(XOO3541)
            VCH: VC0440
            VCO: VC0395_A2858(folA)
            VVU: VV1_0666
            VVY: VV0475
            VPA: VP0333
            VFI: VF0284
            PPR: PBPRA0399
            PAE: PA0350(folA)
            PAU: PA14_04580(folA)
            PPU: PP_5132(folA)
            PPF: Pput_5005
            PST: PSPTO_0437(folA)
            PSB: Psyr_4737
            PSP: PSPPH_4771(folA)
            PFL: PFL_5883(folA)
            PFO: Pfl_5361
            PEN: PSEEN0273(folA)
            PMY: Pmen_4209
            PAR: Psyc_2012(folA)
            PCR: Pcryo_2315
            PRW: PsycPRwf_2332
            ACI: ACIAD0514(folA)
            SON: SO_3646(folA)
            SDN: Sden_2922
            SFR: Sfri_3084
            SAZ: Sama_2824
            SBL: Sbal_0972
            SBM: Shew185_1041
            SLO: Shew_0874
            SPC: Sputcn32_0984
            SSE: Ssed_0959
            SPL: Spea_0857
            SHE: Shewmr4_0900
            SHM: Shewmr7_3120
            SHN: Shewana3_3214
            SHW: Sputw3181_3183
            ILO: IL0478(folA)
            CPS: CPS_4505(folA)
            PHA: PSHAa2653(folA)
            PAT: Patl_3735
            SDE: Sde_0351
            PIN: Ping_1045
            MAQ: Maqu_2431
            CBU: CBU_1993(folA)
            CBD: COXBU7E912_2090(folA)
            LPN: lpg0300
            LPF: lpl0353(folA)
            LPP: lpp0378(folA)
            MCA: MCA2729(folA)
            FTU: FTT0312c(folA)
            FTF: FTF0312c(folA)
            FTW: FTW_1770(folA)
            FTL: FTL_0223
            FTH: FTH_0218(folA)
            FTA: FTA_0239(folA)
            FTN: FTN_0226(folA)
            TCX: Tcr_0573
            NOC: Noc_0235
            AEH: Mlg_0423
            HHA: Hhal_2048
            HCH: HCH_05856
            CSA: Csal_2571
            ABO: ABO_2343(folA)
            MMW: Mmwyl1_3741
            AHA: AHA_3377(folA)
            DNO: DNO_0789(folA)
            BCI: BCI_0561(folA)
            RMA: Rmag_1019
            VOK: COSY_0920(folA)
            NME: NMB0308
            NMA: NMA2179(folA)
            NMC: NMC1873(folA)
            NGO: NGO1694
            CVI: CV_1028(folA)
            RSO: RSc0946(folA)
            REU: Reut_A0914
            REH: H16_A1840(folA1) H16_A2704(folA2)
            BMA: BMA0387(folA)
            BMV: BMASAVP1_A2530(folA)
            BML: BMA10299_A0903(folA)
            BMN: BMA10247_0244(folA)
            BXE: Bxe_A1020 Bxe_B1926
            BVI: Bcep1808_1002
            BUR: Bcep18194_A4196
            BCN: Bcen_0603
            BCH: Bcen2424_1082
            BAM: Bamb_0958
            BPS: BPSL2476
            BPM: BURPS1710b_2952(folA)
            BPL: BURPS1106A_2902(folA)
            BPD: BURPS668_2842(folA)
            BTE: BTH_I1674
            PNU: Pnuc_0380
            BPE: BP3155(folA)
            BPA: BPP0786(folA)
            BBR: BB0871(folA)
            RFR: Rfer_2985
            POL: Bpro_1822
            PNA: Pnap_2773
            AAV: Aave_1448
            AJS: Ajs_1195
            VEI: Veis_3173
            MPT: Mpe_A2052 Mpe_B0221
            HAR: HEAR1055(folA)
            MMS: mma_1192(folA)
            NEU: NE0567(dfrA)
            NET: Neut_1020
            NMU: Nmul_A1963
            EBA: ebA4414(dfrA)
            AZO: azo3198(folA)
            DAR: Daro_0579
            TBD: Tbd_2039
            MFA: Mfla_0914 Mfla_1058
            GSU: GSU0571(folA)
            GME: Gmet_2947
            GUR: Gura_0932
            PCA: Pcar_2754
            BBA: Bd3231(folA)
            DPS: DP0311
            MXA: MXAN_5943(folA)
            RCO: RC0034(folA)
            RFE: RF_0037 RF_0038
            RBE: RBE_0033(folA)
            WOL: WD0884(folA)
            MLO: mll1457
            MES: Meso_1750
            PLA: Plav_2449
            SME: SMc01442(folA)
            SMD: Smed_2019
            ATU: Atu2046(folA)
            ATC: AGR_C_3708
            RET: RHE_CH02798(folA)
            RLE: RL0585 RL3255(folA)
            BME: BMEI0609
            BMF: BAB1_1417(folA)
            BMS: BR1398(folA)
            BMB: BruAb1_1393(folA)
            BOV: BOV_1354(folA)
            OAN: Oant_1793
            BJA: bll6510(folA)
            BRA: BRADO5576(folA)
            BBT: BBta_6098(folA)
            RPA: RPA3492(dyr)
            RPB: RPB_2037
            RPC: RPC_3263
            RPD: RPD_3353
            RPE: RPE_2177
            NWI: Nwi_2350
            NHA: Nham_2729
            BHE: BH10970(folA)
            BQU: BQ08620(folA)
            BBK: BARBAKC583_0925(folA)
            XAU: Xaut_1420
            CCR: CC_2126
            SIT: TM1040_1728
            RSP: RSP_0389(folA)
            RSH: Rsph17029_2043
            RSQ: Rsph17025_0847
            RDE: RD1_1875(folA)
            MMR: Mmar10_2025
            HNE: HNE_0463(folA)
            ZMO: ZMO0321(dhfrIII)
            NAR: Saro_3262
            SAL: Sala_2360
            SWI: Swit_3786
            ELI: ELI_13570
            GBE: GbCGDNIH1_1342
            MAG: amb1326
            BSU: BG10795(dfrA)
            BHA: BH3450(dfrA)
            BAN: BA2237(dfrA)
            BAR: GBAA2237(dfrA)
            BAA: BA_2741
            BAT: BAS2083
            BCE: BC2192
            BCA: BCE_2267(dfrA)
            BCZ: BCZK2021(dfrA)
            BCY: Bcer98_1640
            BTK: BT9727_2021(dfrA)
            BTL: BALH_2001
            BLI: BL03300(dfrA)
            BLD: BLi02319(dfrA)
            BCL: ABC2954(dfrA)
            BAY: RBAM_019960
            BPU: BPUM_0485 BPUM_1915
            OIH: OB1739(dfrA)
            GKA: GK1775
            SAU: SA1259(dfrA)
            SAV: SAV1426(dfrA)
            SAM: MW1316(dfrA)
            SAR: SAR1439(dfrB)
            SAS: SAS1369
            SAC: SACOL1461(folA)
            SAB: SAB1281c(dfrB)
            SAA: SAUSA300_1319(folA)
            SAO: SAOUHSC_01434
            SAJ: SaurJH9_1486
            SAH: SaurJH1_1515
            SEP: SE1119
            SER: SERP1002(folA-1) SERP1581(folA-2)
            SHA: SH1480(dfrA)
            SSP: SSP1313
            LMO: lmo1873
            LMF: LMOf2365_1903(folA)
            LIN: lin1987
            LWE: lwe1893(dfrA)
            LLA: L162872(dfrA)
            LLC: LACR_1270
            LLM: llmg_1342(dfrA)
            SPY: SPy_0883(dyr)
            SPZ: M5005_Spy_0689(dyr)
            SPM: spyM18_0944(dfr)
            SPG: SpyM3_0602(dyr)
            SPS: SPs1251
            SPH: MGAS10270_Spy0747(dyr)
            SPI: MGAS10750_Spy0781(dyr)
            SPJ: MGAS2096_Spy0761(dyr)
            SPK: MGAS9429_Spy0745(dyr)
            SPF: SpyM51119(dfrB)
            SPA: M6_Spy0706
            SPB: M28_Spy0669(dyr)
            SPN: SP_1571
            SPR: spr1429(dfr)
            SPD: SPD_1401(folA)
            SAG: SAG1314(folA)
            SAN: gbs1384(dfrA)
            SAK: SAK_1345(folA)
            SMU: SMU.947(dfrA)
            STC: str0579(folA)
            STL: stu0579(folA)
            STE: STER_0623
            SSA: SSA_1092(dfrA)
            SGO: SGO_0348 SGO_1141(folA)
            LPL: lp_1869(dfrA)
            LJO: LJ1470
            LAC: LBA0902(dfrA)
            LSA: LSA1000(dfrA)
            LSL: LSL_0709(folA)
            LDB: Ldb0788(folA)
            LBU: LBUL_0721
            LBR: LVIS_0785
            LCA: LSEI_1388
            LRE: Lreu_0770
            PPE: PEPE_1069
            EFA: EF1577(folA)
            OOE: OEOE_1013
            STH: STH3116
            CAC: CAC3004(folA)
            CPE: CPE0044(folA)
            CPF: CPF_0051(folA)
            CPR: CPR_0054(folA)
            CTC: CTC01529
            CNO: NT01CX_1208(folA)
            CBE: Cbei_4953
            CKL: CKL_2200(dfrD)
            MGE: MG_228(dhfR)
            MPN: MPN321(dhfR)
            MPU: MYPU_5370(dhfr)
            MPE: MYPE6860(dhfR)
            MMO: MMOB0350(dhfR)
            MSY: MS53_0397(folA)
            UUR: UU114(folA)
            POY: PAM294(folA)
            AYW: AYWB_429(folA)
            MFL: Mfl383
            MTU: Rv2763c(dfrA)
            MTC: MT2833(folA)
            MBO: Mb2785c(dfrA)
            MBB: BCG_2780c(dfrA)
            MLE: ML1518(folA)
            MPA: MAP2868c(dfrA)
            MAV: MAV_3651(folA)
            MSM: MSMEG_2671(folA)
            MVA: Mvan_2381
            MGI: Mflv_4006
            MMC: Mmcs_2113
            MKM: Mkms_2159
            MJL: Mjls_2100
            CGL: NCgl0809(cgl0843)
            CGB: cg0965(folA)
            CEF: CE0918
            CDI: DIP0824
            CJK: jk0440(folA)
            NFA: nfa50230(dfrA)
            RHA: RHA1_ro02249
            LXX: Lxx09920(folA)
            ART: Arth_3019
            AAU: AAur_2993(folA)
            PAC: PPA1671
            NCA: Noca_2312
            KRA: Krad_4438
            BLO: BL1666(dfrA)
            BAD: BAD_0389(dfrA)
            FNU: FN0241
            RBA: RB12617(folA)
            CTR: CT612(folA)
            CTA: CTA_0665(folA)
            CMU: TC0902
            CPN: CPn0759(folA)
            CPA: CP1113
            CPJ: CPj0759(folA)
            CPT: CpB0787
            CCA: CCA00998(folA)
            CAB: CAB968(folA)
            CFE: CF0015(folA)
            GVI: glr2476
            BTH: BT_2048
            BFR: BF3735
            BFS: BF3524(dfrA)
            PGI: PG2061(folA)
            SRU: SRU_0412(folA)
            CHU: CHU_0402(folA) CHU_1297(dfr) CHU_1569(folA) CHU_1753(dfr)
                 CHU_2397(folA) CHU_2917(folA) CHU_3049(dfr)
            GFO: GFO_0279(dfrA)
            FJO: Fjoh_1468
            FPS: FP0328(dfrA)
            DRA: DR_2632
            TMA: TM1641
            HMA: pNG7359(folA2) rrnAC0859(folA1)
            HWA: HQ1842A(folA) HQ2455A(folA)
            NPH: NP2922A(folA)
STRUCTURES  PDB: 1AI9  1AO8  1AOE  1BOZ  1BZF  1CD2  1CZ3  1D1G  1DAJ  1DDR  
                 1DDS  1DF7  1DG5  1DG7  1DG8  1DHF  1DHI  1DHJ  1DIS  1DIU  
                 1DLR  1DLS  1DR1  1DR2  1DR3  1DR4  1DR5  1DR6  1DR7  1DRA  
                 1DRB  1DRE  1DRF  1DRH  1DYH  1DYI  1DYJ  1DYR  1E26  1HFP  
                 1HFQ  1HFR  1IA1  1IA2  1IA3  1IA4  1J3I  1J3J  1J3K  1JOL  
                 1JOM  1JUV  1KLK  1KMS  1KMV  1LUD  1LY3  1LY4  1M78  1M79  
                 1M7A  1MVS  1MVT  1OHJ  1OHK  1PD8  1PD9  1PDB  1QZF  1RA1  
                 1RA2  1RA3  1RA8  1RA9  1RB2  1RB3  1RC4  1RD7  1RE7  1RF7  
                 1RG7  1RH3  1RX1  1RX2  1RX3  1RX4  1RX5  1RX6  1RX7  1RX8  
                 1RX9  1S3U  1S3V  1S3W  1S3Y  1SEJ  1TDR  1U70  1U71  1U72  
                 1VDR  1VIE  1VIF  1VJ3  1YHO  1ZDR  2ANO  2ANQ  2BL9  2BLA  
                 2BLB  2BLC  2C2S  2C2T  2CD2  2CIG  2D0K  2DHF  2DRC  2FZH  
                 2FZI  2FZJ  2GQV  2HM9  2HQP  2INQ  2ITH  2OIP  2P4T  2QK8  
                 3CD2  3DFR  3DRC  4CD2  4DFR  5DFR  6DFR  7DFR  8DFR  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.3
            ExPASy - ENZYME nomenclature database: 1.5.1.3
            ExplorEnz - The Enzyme Database: 1.5.1.3
            ERGO genome analysis and discovery system: 1.5.1.3
            BRENDA, the Enzyme Database: 1.5.1.3
            CAS: 9002-03-3
///
ENTRY       EC 1.5.1.4        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: dihydrofolate dehydrogenase. Now included with EC
            1.5.1.3 dihydrofolate reductase (EC 1.5.1.4 created 1961, deleted
            1976)
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.4
            ExPASy - ENZYME nomenclature database: 1.5.1.4
            ExplorEnz - The Enzyme Database: 1.5.1.4
            ERGO genome analysis and discovery system: 1.5.1.4
            BRENDA, the Enzyme Database: 1.5.1.4
///
ENTRY       EC 1.5.1.5                  Enzyme
NAME        methylenetetrahydrofolate dehydrogenase (NADP+);
            N5,N10-methylenetetrahydrofolate dehydrogenase;
            5,10-methylenetetrahydrofolate:NADP oxidoreductase;
            5,10-methylenetetrahydrofolate dehydrogenase;
            methylenetetrahydrofolate dehydrogenase;
            methylenetetrahydrofolate dehydrogenase (NADP)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     5,10-methylenetetrahydrofolate:NADP+ oxidoreductase
REACTION    5,10-methylenetetrahydrofolate + NADP+ =
            5,10-methenyltetrahydrofolate + NADPH + H+ [RN:R01220]
ALL_REAC    R01220
SUBSTRATE   5,10-methylenetetrahydrofolate [CPD:C00143];
            NADP+ [CPD:C00006]
PRODUCT     5,10-methenyltetrahydrofolate [CPD:C00445];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     In eukaryotes, occurs as a trifunctional enzyme also having
            methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) and
            formate---tetrahydrofolate ligase (EC 6.3.4.3) activity. In some
            prokaryotes occurs as a bifunctional enzyme also having
            methenyltetrahydrofolate cyclohydrolase activity (EC 3.5.4.9).
REFERENCE   1  [PMID:13462986]
  AUTHORS   HATEFI Y, OSBORN MJ, KAY LD, HUENNEKENS FM.
  TITLE     Hydroxymethyl tetrahydrofolic dehydrogenase.
  JOURNAL   J. Biol. Chem. 227 (1957) 637-47.
  ORGANISM  pigeon, cow [GN:bta]
REFERENCE   2  [PMID:13499428]
  AUTHORS   OSBORN MJ, HUENNEKENS FM.
  TITLE     Participation of anhydroleucovorin in the hydroxymethyl
            tetrahydrofolic dehydrogenase system.
  JOURNAL   Biochim. Biophys. Acta. 26 (1957) 646-7.
  ORGANISM  chicken [GN:gga]
REFERENCE   3  [PMID:14490085]
  AUTHORS   RAMASASTRI BV, BLAKLEY RL.
  TITLE     5,10-Methylenetetrahydrofolic dehydrogenase from bakers' yeast. I.
            Partial purification and some properties.
  JOURNAL   J. Biol. Chem. 237 (1962) 1982-8.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4  [PMID:4379024]
  AUTHORS   Yeh YC, Greenberg DM.
  TITLE     Purification and properties of N5, N10-Methylenetetra-hydrofolate
            dehydrogenase of calf thymus.
  JOURNAL   Biochim. Biophys. Acta. 105 (1965) 279-91.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
            PATH: map00670  One carbon pool by folate
ORTHOLOGY   KO: K00288  methylenetetrahydrofolate dehydrogenase (NADP+)
GENES       HSA: 25902(MTHFD1L) 4522(MTHFD1)
            MMU: 108156(Mthfd1) 270685(Mthfd1l)
            RNO: 64300(Mthfd1)
            CFA: 476245(MTHFD1L)
            GGA: 423508(RCJMB04_29j22)
            XLA: 380266(mthfd1)
            XTR: 493369(TNeu036b14.1)
            DRE: 260441(mthfd1)
            DME: Dmel_CG18466(Nmdmc) Dmel_CG4067(pug)
            CEL: K07E3.3(dao-3)
            ATH: AT3G12290
            OSA: 4328117 4337829
            CME: CMR167C
            SCE: YBR084W(MIS1) YGR204W(ADE3)
            AGO: AGOS_ACL121C AGOS_AER178W
            PIC: PICST_80013(MIS1) PICST_88119(ADE3)
            CAL: CaO19_7534(CaO19.7534)
            CGR: CAGL0K00913g CAGL0M01694g
            SPO: SPBC2G2.08 SPBC839.16
            CNE: CNG00590
            UMA: UM03320.1
            DDI: DDB_0230115
            TET: TTHERM_00339820
            TBR: Tb927.7.1600
            TCR: 508207.240 509509.20 511517.60 511741.50
            LMA: LmjF26.0320 LmjF30.2600
            ECO: b0529(folD)
            ECJ: JW0518(folD)
            ECE: Z0684(folD)
            ECS: ECs0591
            ECC: c0645(folD)
            ECI: UTI89_C0559(folD)
            ECP: ECP_0590
            ECV: APECO1_1486(folD)
            ECW: EcE24377A_0570(folD)
            ECX: EcHS_A0603(folD)
            STY: STY0588(folD)
            STT: t2321(folD)
            SPT: SPA2183(folD)
            SEC: SC0581(folD)
            STM: STM0542(folD)
            YPE: YPO2824(folD)
            YPK: y1110(folD)
            YPM: YP_0855(folD)
            YPA: YPA_2565
            YPN: YPN_1020
            YPS: YPTB1037(folD)
            YPI: YpsIP31758_3012(folD)
            SFL: SF0460(folD)
            SFX: S0468(folD)
            SFV: SFV_0487(folD)
            SSN: SSON_0489(folD)
            SBO: SBO_0414(folD)
            SDY: SDY_0281(folD)
            ECA: ECA3149(folD)
            PLU: plu4317(folD)
            BUC: BU486(folD)
            BAS: BUsg470(folD)
            BAB: bbp430(folD)
            BCC: BCc_305(folD)
            WBR: WGLp242(folD)
            SGL: SG0706
            SPE: Spro_1168
            BFL: Bfl305(folD)
            BPN: BPEN_313(folD)
            HIN: HI0609(folD)
            HIT: NTHI0864(folD)
            HDU: HD1108(folD)
            HSO: HS_1221(folD)
            PMU: PM1933(folD)
            MSU: MS1851(folD) MS1852(folD)
            APL: APL_0897(folD)
            XFA: XF2431
            XFT: PD1449(folD)
            XCC: XCC2185(folD)
            XCB: XC_1933
            XCV: XCV2487(folD)
            XAC: XAC2289(folD)
            XOO: XOO2193(folD)
            XOM: XOO_2061(XOO2061)
            VCH: VC1942
            VVU: VV1_2022
            VVY: VV2391
            VPA: VP0879
            VFI: VF1770
            PPR: PBPRA2641
            PAE: PA1796(folD)
            PPU: PP_1945(folD-1) PP_2265(folD-2)
            PPF: Pput_3472
            PST: PSPTO_2453(folD-1) PSPTO_3733(folD-2)
            PSB: Psyr_1743 Psyr_2225
            PSP: PSPPH_1687(folD1) PSPPH_2961(folD2)
            PFL: PFL_3992
            PFO: Pfl_3699
            PEN: PSEEN1862(folD)
            PMY: Pmen_3471
            PAR: Psyc_0673(folD)
            ACI: ACIAD2553(folD) ACIAD2847(folD)
            SON: SO_1792(folD)
            SFR: Sfri_2598
            SAZ: Sama_1222
            SLO: Shew_2510
            SSE: Ssed_1539
            SPL: Spea_2683
            SHE: Shewmr4_2497
            SHM: Shewmr7_2565
            SHN: Shewana3_2663
            ILO: IL1008(folD)
            CPS: CPS_3133(folD1) CPS_3791(folD2)
            PHA: PSHAa2064(folD)
            PIN: Ping_1473
            MAQ: Maqu_1842
            CBU: CBU_0312(folD)
            LPN: lpg1297(folD)
            LPF: lpl1260(folD)
            LPP: lpp1261(folD)
            MCA: MCA0508
            FTU: FTT0892(folD)
            FTF: FTF0892(folD)
            FTL: FTL_0394
            FTH: FTH_0386
            FTA: FTA_0417
            FTN: FTN_0417(folD)
            TCX: Tcr_0723 Tcr_1343
            NOC: Noc_2248
            AEH: Mlg_0591
            HHA: Hhal_0610
            HCH: HCH_02155(folD)
            CSA: Csal_2048
            AHA: AHA_1854
            BCI: BCI_0122(folD)
            VOK: COSY_0765(folD)
            NMA: NMA0354(folD)
            NMC: NMC2056(folD)
            NGO: NGO1999(folD)
            CVI: CV_1925(folD)
            RSO: RSc1596(folD)
            REU: Reut_A1299
            REH: H16_A1370(folD)
            RME: Rmet_1192
            BMA: BMA1724(folD)
            BXE: Bxe_A1536
            BUR: Bcep18194_A5446
            BPS: BPSL2304(folD)
            BPM: BURPS1710b_2749(folD)
            BPL: BURPS1106A_2672(folD)
            BPD: BURPS668_2616(folD)
            BTE: BTH_I1861
            BPE: BP0990(folD) BP2522(folD)
            BPA: BPP1459(folD) BPP3509(folD)
            BBR: BB2533(folD)
            RFR: Rfer_2209
            POL: Bpro_2675
            MPT: Mpe_A2131 Mpe_A3259
            HAR: HEAR0745(folD)
            MMS: mma_0672(folD)
            NEU: NE0362(folD)
            NET: Neut_1607
            NMU: Nmul_A0357
            EBA: ebA118(folD)
            AZO: azo1377(folD)
            DAR: Daro_0448
            TBD: Tbd_0689
            HPY: HP0577(folD)
            HPA: HPAG1_0556
            HHE: HH1366(folD)
            HAC: Hac_1435(folD)
            WSU: WS1345(folD)
            TDN: Tmden_1113
            CJE: Cj0855(folD)
            CJR: CJE0942(folD)
            CJU: C8J_0802(folD)
            CFF: CFF8240_1174
            CCV: CCV52592_0799 CCV52592_2154
            CHA: CHAB381_1036
            ABU: Abu_0637(folD)
            NIS: NIS_0711(folD)
            SUN: SUN_0665(folD)
            GSU: GSU0215(folD-1) GSU0862(folD-2)
            GME: Gmet_0247 Gmet_1162
            GUR: Gura_1169
            PCA: Pcar_2461
            DVU: DVU0323(folD)
            DVL: Dvul_2658
            DDE: Dde_0296
            LIP: LI0875
            BBA: Bd3295(folD)
            DPS: DP1901
            ADE: Adeh_1247
            AFW: Anae109_2520
            MXA: MXAN_2226(folD) MXAN_3032(folD)
            SAT: SYN_02873
            SFU: Sfum_2686
            RPR: RP515(folD)
            RTY: RT0501(folD)
            RCO: RC0636(folD)
            RFE: RF_0699(folD)
            RBE: RBE_0983(folD)
            OTS: OTBS_1842(folD)
            WOL: WD0555(folD)
            WBM: Wbm0073
            AMA: AM179(folD)
            APH: APH_0175(folD)
            ERU: Erum6730(folD)
            ERW: ERWE_CDS_07060(folD)
            ERG: ERGA_CDS_06980(folD)
            ECN: Ecaj_0680
            ECH: ECH_0324(folD)
            NSE: NSE_0821(folD)
            PUB: SAR11_0307(folD)
            MLO: mll6921 mlr6508
            MES: Meso_0152
            SME: SMc02604(folD1) SMc03059(folD2)
            ATU: Atu0589(folD)
            ATC: AGR_C_1042(folD)
            RET: RHE_CH00694(folDch)
            RLE: RL0743
            BME: BMEII0510
            BMF: BAB2_0457(folD)
            BMS: BRA0781(folD)
            BMB: BruAb2_0451(folD)
            OAN: Oant_3959
            BJA: bll0549(folD)
            BRA: BRADO0277(folD)
            BBT: BBta_0269(folD)
            RPA: RPA0413
            RPB: RPB_0108
            RPC: RPC_0059
            RPD: RPD_0694
            RPE: RPE_0047
            NWI: Nwi_0480
            NHA: Nham_0609
            BHE: BH03940(folD)
            BQU: BQ02960(folD)
            BBK: BARBAKC583_0297(folD)
            CCR: CC_1217
            SIL: SPO1559 SPO1560(folD) SPO3101
            SIT: TM1040_2356
            RSP: RSP_0661
            RSH: Rsph17029_2314
            JAN: Jann_0983
            RDE: RD1_2105(folD) RD1_4236(folD) RD1_4237(folD)
            ZMO: ZMO0914(folD)
            NAR: Saro_3300
            SAL: Sala_3097
            ELI: ELI_11530
            GOX: GOX0792
            GBE: GbCGDNIH1_0050
            ACR: Acry_2656
            RRU: Rru_A0557
            MAG: amb4374
            BSU: BG11711(folD)
            BHA: BH2784(folD)
            BAN: BA4405(folD)
            BAR: GBAA4405(folD)
            BAA: BA_4857
            BAT: BAS4085
            BCE: BC4180
            BCA: BCE_4254(folD)
            BCZ: BCZK3934(folD)
            BTK: BT9727_3923(folD)
            BTL: BALH_3789(folD)
            BLI: BL01527(folD)
            BLD: BLi02602(folD)
            BCL: ABC3388(folD)
            BAY: RBAM_022640(folD)
            BPU: BPUM_2163(folD)
            OIH: OB1880(folD)
            GKA: GK2396
            SAU: SA0915(folD)
            SAV: SAV1063(folD)
            SAM: MW0946(folD)
            SAR: SAR1037(folD)
            SAS: SAS0999(folD)
            SAC: SACOL1072(folD)
            SAB: SAB0930c(folD)
            SAA: SAUSA300_0965(folD)
            SAO: SAOUHSC_01007
            SAJ: SaurJH9_1123
            SAH: SaurJH1_1145
            SEP: SE0761
            SER: SERP0648(folD)
            SHA: SH1894(folD)
            SSP: SSP1727
            LMO: lmo1360(folD)
            LMF: LMOf2365_1377(folD)
            LIN: lin1397(folD)
            LWE: lwe1375(folD)
            LLA: L76582(folD)
            LLC: LACR_0921
            SPY: SPy_1502(folD)
            SPZ: M5005_Spy_1234(folD)
            SPM: spyM18_1520(folD)
            SPG: SpyM3_1157(folD)
            SPS: SPs0705
            SPH: MGAS10270_Spy1250(folD)
            SPI: MGAS10750_Spy1341(folD)
            SPJ: MGAS2096_Spy1252(folD)
            SPK: MGAS9429_Spy1228(folD)
            SPF: SpyM50619(folD)
            SPA: M6_Spy1254
            SPB: M28_Spy1173(folD)
            SPN: SP_0825
            SPR: spr0729(folD)
            SPD: SPD_0721(folD)
            SAG: SAG0494(folD)
            SAN: gbs0540
            SAK: SAK_0595(folD)
            SMU: SMU.572(folD)
            STL: stu0611(folD)
            SSA: SSA_0671(folD)
            LPL: lp_1599(folD)
            LJO: LJ1215 LJ1550
            LAC: LBA1332(folD)
            LSA: LSA0676(folD)
            LSL: LSL_0533(folD)
            LDB: Ldb1425(folD)
            LBU: LBUL_1320
            LBR: LVIS_0978
            LCA: LSEI_1639
            LGA: LGAS_0751
            PPE: PEPE_0817
            EFA: EF0978(folD)
            OOE: OEOE_0943
            STH: STH1847
            CAC: CAC2083(folD)
            CPE: CPE1823(folD)
            CPF: CPF_2077(folD)
            CPR: CPR_1791(folD)
            CTC: CTC01579
            CDF: CD0720(folD)
            CBO: CBO1172
            CBA: CLB_1203(folD)
            CBH: CLC_1215(folD)
            CBF: CLI_1254(folD)
            CBE: Cbei_1702
            CKL: CKL_0442(folD)
            AMT: Amet_2020
            CHY: CHY_1878(folD)
            DSY: DSY0607 DSY2356
            DRM: Dred_1073
            SWO: Swol_1474
            CSC: Csac_2142
            TTE: TTE1293(folD)
            MTA: Moth_1516
            MPN: MPN017(mtd1)
            MPU: MYPU_2580(folD)
            MPE: MYPE6880(folD)
            MGA: MGA_0596(folD)
            MMY: MSC_0758(folD)
            MMO: MMOB1600(folD)
            MSY: MS53_0297(folD)
            MCP: MCAP_0706(folD)
            UUR: UU337(folD)
            MFL: Mfl167
            MTU: Rv3356c(folD)
            MTC: MT3464(folD)
            MBO: Mb3391c(folD)
            MBB: BCG_3428c(folD)
            MLE: ML0674(folD)
            MPA: MAP3463c(folD)
            MVA: Mvan_1550
            MGI: Mflv_4879
            MKM: Mkms_1221
            MJL: Mjls_1231
            CGL: NCgl0620(cgl0648)
            CGB: cg0750(folD)
            CEF: CE0659
            CDI: DIP0620(folD)
            CJK: jk1697
            NFA: nfa34300(folD)
            RHA: RHA1_ro01817 RHA1_ro06234(folD)
            SCO: SCO4824(folD)
            SMA: SAV3442(folD1) SAV543(folD2)
            TWH: TWT634(folD)
            TWS: TW653(folD)
            LXX: Lxx18630(folD)
            CMI: CMM_2521(folD)
            AAU: AAur_0482(folD)
            PAC: PPA1743
            NCA: Noca_3582
            TFU: Tfu_2571
            FRA: Francci3_1492 Francci3_2667
            FAL: FRAAL2298(folD) FRAAL4216(folD)
            ACE: Acel_0385
            SEN: SACE_4498(folD) SACE_6651(folD)
            BLO: BL0993(folD)
            BAD: BAD_0673(folD)
            RXY: Rxyl_1566 Rxyl_2517
            FNU: FN1488
            RBA: RB10295(mtdA) RB7468(folD)
            CTR: CT078(folD)
            CTA: CTA_0083(folD)
            CMU: TC0350
            CPN: CPn0335(folD)
            CPA: CP0423
            CPJ: CPj0335(folD)
            CPT: CpB0344
            CCA: CCA00448(folD)
            CAB: CAB434
            CFE: CF0559(folD)
            PCU: pc1701(folD)
            BBU: BB0026(folD)
            BGA: BG0026(folD)
            BAF: BAPKO_0025(folD)
            TPA: TP0732
            TDE: TDE0013(folD)
            LIL: LA1865(folD)
            LIC: LIC12026(folD)
            LBJ: LBJ_1651(folD)
            LBL: LBL_1870(folD)
            SYN: sll0753(folD)
            SYW: SYNW0740(folD)
            SYC: syc0759_d(folD)
            SYF: Synpcc7942_0777
            SYD: Syncc9605_1928
            SYE: Syncc9902_0737
            SYG: sync_0990
            SYR: SynRCC307_0749(folD)
            SYX: SynWH7803_1570(folD)
            CYA: CYA_1974(folD)
            CYB: CYB_0090(folD)
            TEL: tll0021(folD)
            GVI: gll1884
            ANA: alr0212
            AVA: Ava_2703 Ava_C0058
            PMA: Pro1130(folD)
            PMM: PMM1069(folD)
            PMT: PMT1110(folD)
            PMN: PMN2A_0682
            PMI: PMT9312_1080
            PMB: A9601_11741(folD)
            PMC: P9515_11591(folD)
            PMF: P9303_09321(folD)
            PMG: P9301_11751(folD)
            PMH: P9215_12041(folD)
            PME: NATL1_15161(folD)
            TER: Tery_4172
            BTH: BT_1607
            BFR: BF3219
            BFS: BF3058
            PGI: PG1116(folD)
            SRU: SRU_1839
            CHU: CHU_1706(clpP) CHU_1716(folD)
            GFO: GFO_2795(folD)
            FPS: FP1475(folD)
            CTE: CT0719(mtd)
            CCH: Cag_0779
            PLT: Plut_0927
            DET: DET0668(folD-1) DET0702(folD-2)
            DEH: cbdb_A656(folD)
            RRS: RoseRS_4392
            DRA: DR_0867
            DGE: Dgeo_0514 Dgeo_0699
            TTH: TTC0755
            TTJ: TTHA1120
            AAE: aq_1898(folD)
            TMA: TM1767
            MAC: MA3519(folD)
            MBA: Mbar_A2315
            MMA: MM_0441
            MBU: Mbur_1814
            HAL: VNG1416G(folD)
            HMA: pNG7328(folD2) rrnAC0996(folD1)
            HWA: HQ2790A(folD)
            NPH: NP2054A(folD)
            TAC: Ta0898
            TVO: TVN1018
            PTO: PTO1071
            PAI: PAE0220(folD)
STRUCTURES  PDB: 1A4I  1DIA  1DIB  1DIG  1LU9  1LUA  2C2X  2C2Y  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.5
            ExPASy - ENZYME nomenclature database: 1.5.1.5
            ExplorEnz - The Enzyme Database: 1.5.1.5
            ERGO genome analysis and discovery system: 1.5.1.5
            BRENDA, the Enzyme Database: 1.5.1.5
            CAS: 9029-14-5
///
ENTRY       EC 1.5.1.6                  Enzyme
NAME        formyltetrahydrofolate dehydrogenase;
            10-formyl tetrahydrofolate:NADP oxidoreductase;
            10-formyl-H2PtGlu:NADP oxidoreductase ;
            10-formyl-H4folate dehydrogenase;
            N10-formyltetrahydrofolate dehydrogenase ;
            10-formyltetrahydrofolate dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     10-formyltetrahydrofolate:NADP+ oxidoreductase
REACTION    10-formyltetrahydrofolate + NADP+ + H2O = tetrahydrofolate + CO2 +
            NADPH + H+ [RN:R00941]
ALL_REAC    R00941
SUBSTRATE   10-formyltetrahydrofolate [CPD:C00234];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     tetrahydrofolate [CPD:C00101];
            CO2 [CPD:C00011];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4384443]
  AUTHORS   Kutzbach C, Stokstad EL.
  TITLE     Partial purification of a 10-formyl-tetrahydrofolate: NADP
            oxidoreductase from mammalian liver.
  JOURNAL   Biochem. Biophys. Res. Commun. 30 (1968) 111-7.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00670  One carbon pool by folate
ORTHOLOGY   KO: K00289  formyltetrahydrofolate dehydrogenase
GENES       HSA: 10840(ALDH1L1)
            MMU: 107747(Aldh1l1)
            RNO: 64392(Fthfd)
            CFA: 476506(ALDH1L1)
            XLA: 444321(MGC81015)
            XTR: 496436(fthfd)
            DME: Dmel_CG8665
            CEL: F36H1.6(alh-3)
STRUCTURES  PDB: 1S3I  2BW0  2CFI  2CQ8  2O2P  2O2Q  2O2R  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.6
            ExPASy - ENZYME nomenclature database: 1.5.1.6
            ExplorEnz - The Enzyme Database: 1.5.1.6
            ERGO genome analysis and discovery system: 1.5.1.6
            BRENDA, the Enzyme Database: 1.5.1.6
            CAS: 37256-25-0
///
ENTRY       EC 1.5.1.7                  Enzyme
NAME        saccharopine dehydrogenase (NAD+, L-lysine-forming);
            lysine-2-oxoglutarate reductase;
            dehydrogenase, saccharopine (nicotinamide adenine dinucleotide,
            lysine forming);
            epsilon-N-(L-glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine
            forming);
            N6-(glutar-2-yl)-L-lysine:NAD oxidoreductase (L-lysine-forming);
            6-N-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase
            (L-lysine-forming)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase
            (L-lysine-forming)
REACTION    N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine +
            2-oxoglutarate + NADH + H+ [RN:R00715]
ALL_REAC    R00715
SUBSTRATE   N6-(L-1,3-dicarboxypropyl)-L-lysine [CPD:C00449];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     L-lysine [CPD:C00047];
            2-oxoglutarate [CPD:C00026];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4339117]
  AUTHORS   Fujioka M, Nakatani Y.
  TITLE     Saccharopine dehydrogenase. Interaction with substrate analogues.
  JOURNAL   Eur. J. Biochem. 25 (1972) 301-7.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:4287986]
  AUTHORS   Saunders PP, Broquist HP.
  TITLE     Saccharopine, an intermediate of the aminoadipic acid pathway of
            lysine biosynthesis. IV. Saccharopine dehydrogenase.
  JOURNAL   J. Biol. Chem. 241 (1966) 3435-40.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], Neurospora crassa [GN:dncr]
PATHWAY     PATH: map00300  Lysine biosynthesis
            PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K00290  saccharopine dehydrogenase (NAD+, L-lysine forming)
GENES       HSA: 10157(AASS)
            GGA: 417757(AASS)
            SCE: YIR034C(LYS1)
            AGO: AGOS_ACR167C
            PIC: PICST_86170(LYS1)
            CGR: CAGL0F06875g
            SPO: SPAC227.18(lys3)
            AFM: AFUA_3G11710
            AOR: AO090003000729
            CNE: CND06290
            UMA: UM04426.1
            PPR: PBPRB1102
            PFL: PFL_3539(lyS1)
            FTN: FTN_0964
            BXE: Bxe_A1992
            BAM: Bamb_1645
            BPM: BURPS1710b_2269
            BPL: BURPS1106A_2136(lys1)
            BPD: BURPS668_2080
            HPA: HPAG1_1405
            HAC: Hac_0077(lys1)
            CJR: CJE0165
            CJJ: CJJ81176_0208
            CJD: JJD26997_0186
            CFF: CFF8240_0285(lys)
            CCV: CCV52592_0415(lys1)
            CHA: CHAB381_0061(lys1)
            CCO: CCC13826_0747(lys1)
            ABU: Abu_1706
            NIS: NIS_1295
            SUN: SUN_1368
            GSU: GSU2539(LYS1)
            DVU: DVU0418(lys1)
            DDE: Dde_0572
            MXA: MXAN_0831(lys1)
            RLE: RL0376 pRL110083
            BBK: BARBAKC583_0028(lys1)
            SIL: SPO0601
            SIT: TM1040_0107
            RSQ: Rsph17025_2942
            JAN: Jann_4015
            RDE: RD1_0698
            HNE: HNE_0588(lys1)
            MGM: Mmc1_1081
            SPD: SPD_0812(lys1)
            DSY: DSY3821
            MAV: MAV_1723
            MSM: MSMEG_4632 MSMEG_6311(lys1)
            SEN: SACE_1566(lys1)
            SRU: SRU_1725(lys1) SRU_2554(lys1)
            CHU: CHU_2707(lys)
            HMA: rrnAC0132
STRUCTURES  PDB: 1FF9  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.7
            ExPASy - ENZYME nomenclature database: 1.5.1.7
            ExplorEnz - The Enzyme Database: 1.5.1.7
            ERGO genome analysis and discovery system: 1.5.1.7
            BRENDA, the Enzyme Database: 1.5.1.7
            CAS: 9073-96-5
///
ENTRY       EC 1.5.1.8                  Enzyme
NAME        saccharopine dehydrogenase (NADP+, L-lysine-forming);
            lysine-2-oxoglutarate reductase;
            lysine-ketoglutarate reductase;
            L-lysine-alpha-ketoglutarate reductase;
            lysine:alpha-ketoglutarate:TPNH oxidoreductase
            (epsilon-N-[gultaryl-2]-L-lysine forming);
            saccharopine (nicotinamide adenine dinucleotide phosphate,
            lysine-forming) dehydrogenase;
            6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase
            (L-lysine-forming)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase
            (L-lysine-forming)
REACTION    N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-lysine +
            2-oxoglutarate + NADPH + H+ [RN:R00716]
ALL_REAC    R00716
SUBSTRATE   N6-(L-1,3-dicarboxypropyl)-L-lysine [CPD:C00449];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     L-lysine [CPD:C00047];
            2-oxoglutarate [CPD:C00026];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4385118]
  AUTHORS   Hutzler J, Dancis J.
  TITLE     Conversion of lysine to saccharopine by human tissues.
  JOURNAL   Biochim. Biophys. Acta. 158 (1968) 62-9.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:6434529]
  AUTHORS   Markovitz PJ, Chuang DT, Cox RP.
  TITLE     Familial hyperlysinemias. Purification and characterization of the
            bifunctional aminoadipic semialdehyde synthase with
            lysine-ketoglutarate reductase and saccharopine dehydrogenase
            activities.
  JOURNAL   J. Biol. Chem. 259 (1984) 11643-6.
  ORGANISM  baboon, cow [GN:bta]
PATHWAY     PATH: map00300  Lysine biosynthesis
            PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K00291  saccharopine dehydrogenase (NADP+, L-lysine forming)
GENES       HSA: 10157(AASS)
            MMU: 30956(Aass)
            TET: TTHERM_00149450
            BCZ: BCZK1219(lys1)
            GFO: GFO_2567
            FJO: Fjoh_1364
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.8
            ExPASy - ENZYME nomenclature database: 1.5.1.8
            ExplorEnz - The Enzyme Database: 1.5.1.8
            ERGO genome analysis and discovery system: 1.5.1.8
            BRENDA, the Enzyme Database: 1.5.1.8
            CAS: 9031-19-0
///
ENTRY       EC 1.5.1.9                  Enzyme
NAME        saccharopine dehydrogenase (NAD+, L-glutamate-forming);
            dehydrogenase, saccharopine (nicotinamide adenine dinucleotide,
            glutamate-forming);
            saccharopin dehydrogenase;
            NAD+ oxidoreductase (L-2-aminoadipic-delta-semialdehyde and
            glutamate forming);
            aminoadipic semialdehyde synthase;
            saccharopine dehydrogenase (NAD+, L-glutamate-forming);
            6-N-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase
            (L-glutamate-forming)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase
            (L-glutamate-forming)
REACTION    N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-glutamate +
            2-aminoadipate 6-semialdehyde + NADH + H+ [RN:R02313]
ALL_REAC    R02313
SUBSTRATE   N6-(L-1,3-dicarboxypropyl)-L-lysine [CPD:C00449];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     L-glutamate [CPD:C00025];
            2-aminoadipate 6-semialdehyde [CPD:C04076];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4385118]
  AUTHORS   Hutzler J, Dancis J.
  TITLE     Conversion of lysine to saccharopine by human tissues.
  JOURNAL   Biochim. Biophys. Acta. 158 (1968) 62-9.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:6434529]
  AUTHORS   Markovitz PJ, Chuang DT, Cox RP.
  TITLE     Familial hyperlysinemias. Purification and characterization of the
            bifunctional aminoadipic semialdehyde synthase with
            lysine-ketoglutarate reductase and saccharopine dehydrogenase
            activities.
  JOURNAL   J. Biol. Chem. 259 (1984) 11643-6.
  ORGANISM  baboon, cow [GN:bta]
PATHWAY     PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K00292  saccharopine dehydrogenase (NAD+, L-glutamate forming)
GENES       HSA: 10157(AASS)
            MMU: 30956(Aass)
            PRW: PsycPRwf_2123
            STP: Strop_3396
            GFO: GFO_0103
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.9
            ExPASy - ENZYME nomenclature database: 1.5.1.9
            ExplorEnz - The Enzyme Database: 1.5.1.9
            ERGO genome analysis and discovery system: 1.5.1.9
            BRENDA, the Enzyme Database: 1.5.1.9
            CAS: 37256-26-1
///
ENTRY       EC 1.5.1.10                 Enzyme
NAME        saccharopine dehydrogenase (NADP+, L-glutamate-forming);
            saccharopine (nicotinamide adenine dinucleotide phosphate,
            glutamate-forming) dehydrogenase;
            aminoadipic semialdehyde-glutamic reductase;
            aminoadipate semialdehyde-glutamate reductase;
            aminoadipic semialdehyde-glutamate reductase;
            epsilon-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase
            (L-2-aminoadipate-semialdehyde forming);
            saccharopine reductase;
            6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase
            (L-glutamate-forming)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase
            (L-glutamate-forming)
REACTION    N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-glutamate +
            L-2-aminoadipate 6-semialdehyde + NADPH + H+ [RN:R02315]
ALL_REAC    R02315
SUBSTRATE   N6-(L-1,3-dicarboxypropyl)-L-lysine [CPD:C00449];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     L-glutamate [CPD:C00025];
            L-2-aminoadipate 6-semialdehyde [CPD:C04076];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4380448]
  AUTHORS   Jones EE, Broquist HP.
  TITLE     Saccharopine, an intermediate of the aminoadipic acid pathway of
            lysine biosynthesis. 3. Aminoadipic semialdehyde-glutamate
            reductase.
  JOURNAL   J. Biol. Chem. 241 (1966) 3430-4.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00300  Lysine biosynthesis
            PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K00293  saccharopine dehydrogenase (NADP+, L-glutamate forming)
GENES       SCE: YNR050C(LYS9)
            AGO: AGOS_ABR116C
            PIC: PICST_70210(LYS9)
            CGR: CAGL0C03443g
            SPO: SPBC3B8.03
            ANI: AN5601.2
            AFM: AFUA_4G11340
            AOR: AO090003001086
            DDI: DDBDRAFT_0186419
            SIT: TM1040_0106
            FRA: Francci3_3091
            HMA: rrnAC0132
STRUCTURES  PDB: 1E5L  1E5Q  2AXQ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.10
            ExPASy - ENZYME nomenclature database: 1.5.1.10
            ExplorEnz - The Enzyme Database: 1.5.1.10
            ERGO genome analysis and discovery system: 1.5.1.10
            BRENDA, the Enzyme Database: 1.5.1.10
            CAS: 9033-55-0
///
ENTRY       EC 1.5.1.11                 Enzyme
NAME        D-octopine dehydrogenase;
            D-octopine synthase;
            octopine dehydrogenase;
            octopine:NAD+ oxidoreductase;
            ODH;
            2-N-(D-1-carboxyethyl)-L-arginine:NAD+ oxidoreductase
            (L-arginine-forming)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N2-(D-1-carboxyethyl)-L-arginine:NAD+ oxidoreductase
            (L-arginine-forming)
REACTION    N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine +
            pyruvate + NADH + H+ [RN:R00562]
ALL_REAC    R00562
SUBSTRATE   N2-(D-1-carboxyethyl)-L-arginine [CPD:C04137];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     L-arginine [CPD:C00062];
            pyruvate [CPD:C00022];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     In the reverse direction, acts also on L-ornithine, L-lysine and
            L-histidine.
REFERENCE   1
  AUTHORS   Kemp, J.D., Hack, E., Sutton, D.W. and El-Wakil, M.
  TITLE     Unusual amino acids and their relationship to tumorigenesis.
  JOURNAL   Proc. Int. Conf. Plant Pathol. Bact. 4th (1979) 183-188.
REFERENCE   2  [PMID:4310628]
  AUTHORS   van Thoai N, Huc C, Pho DB, Olomucki A.
  TITLE     [Octopine dehydrogenase. Purification and catalytic properties]
  JOURNAL   Biochim. Biophys. Acta. 191 (1969) 46-57.
  ORGANISM  Pecten maximus
PATHWAY     PATH: map00330  Arginine and proline metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.11
            ExPASy - ENZYME nomenclature database: 1.5.1.11
            ExplorEnz - The Enzyme Database: 1.5.1.11
            ERGO genome analysis and discovery system: 1.5.1.11
            BRENDA, the Enzyme Database: 1.5.1.11
            CAS: 37256-27-2
///
ENTRY       EC 1.5.1.12                 Enzyme
NAME        1-pyrroline-5-carboxylate dehydrogenase;
            Delta1-pyrroline-5-carboxylate dehydrogenase;
            1-pyrroline dehydrogenase;
            pyrroline-5-carboxylate dehydrogenase;
            pyrroline-5-carboxylic acid dehydrogenase;
            L-pyrroline-5-carboxylate-NAD+ oxidoreductase;
            1-pyrroline-5-carboxylate:NAD+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (S)-1-pyrroline-5-carboxylate:NAD+ oxidoreductase
REACTION    (S)-1-pyrroline-5-carboxylate + NAD+ + 2 H2O = L-glutamate + NADH +
            H+ [RN:R00707]
ALL_REAC    R00707;
            (other) R00245 R00708 R03294 R04444 R04445 R05051
SUBSTRATE   (S)-1-pyrroline-5-carboxylate [CPD:C03912];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     L-glutamate [CPD:C00025];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Oxidizes other 1-pyrrolines, e.g.
            3-hydroxy-1-pyrroline-5-carboxylate forms 4-hydroxyglutamate. The
            enzyme also converts (R)-1-pyrroline-5-carboxylate into D-glutamate.
REFERENCE   1
  AUTHORS   Adams, E. and Goldstone, A.
  TITLE     Hydroxyproline metabolism. IV. Enzymatic synthesis of
            gamma-hydroxyglutamate from
            Delta1-pyrroline-3-hydroxy-5-carboxylate.
  JOURNAL   J. Biol. Chem. 235 (1960) 3504-3512.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Strecker, H.J.
  TITLE     The interconversion of glutamic acid and proline. III.
            Delta1-Pyrroline-5-carboxylic acid dehydrogenase.
  JOURNAL   J. Biol. Chem. 235 (1960) 3218-3223.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K00294  1-pyrroline-5-carboxylate dehydrogenase
GENES       HSA: 8659(ALDH4A1)
            MMU: 212647(Aldh4a1)
            CFA: 612452(ALDH4A1)
            GGA: 419467(ALDH4A1)
            DRE: 394133(zgc:63592)
            SPU: 576807(LOC576807)
            DME: Dmel_CG7145
            CME: CMG200C
            SCE: YHR037W(PUT2)
            AGO: AGOS_AAL071C
            PIC: PICST_55391(PUT2)
            CGR: CAGL0D03982g
            SPO: SPBC24C6.04
            ANI: AN1733.2
            AFM: AFUA_6G08750
            AOR: AO090001000549
            CNE: CNH02450
            UMA: UM01250.1
            DDI: DDB_0229934
            TET: TTHERM_00822160
            TBR: Tb10.70.4280
            TCR: 510943.50
            LMA: LmjF03.0200
            ECO: b1014(putA)
            ECJ: JW0999(putA)
            ECE: Z1513(putA)
            ECS: ECs1260
            ECC: c1151(putA)
            ECI: UTI89_C1077(putA)
            ECP: ECP_1013
            ECV: APECO1_105(putA)
            ECW: EcE24377A_1132(putA)
            ECX: EcHS_A1129
            STY: STY1159(putA)
            STT: t1797(putA)
            SPT: SPA1727(putA)
            SEC: SC1074(putA)
            STM: STM1124(putA)
            YPE: YPO1851(putA)
            YPK: y2455(putA)
            YPM: YP_1542(putA2)
            YPA: YPA_1229
            YPN: YPN_2272
            YPS: YPTB1723(putA)
            YPI: YpsIP31758_2268(putA)
            SSN: SSON_1034(putA)
            SBO: SBO_2043(putA)
            ECA: ECA4217(putA)
            PLU: plu1957(putA)
            WBR: WGLp434(putA)
            SGL: SG1243
            PMU: PM0589(putA)
            APL: APL_0106(putA)
            XCC: XCC3835(putA)
            XCB: XC_3907(putA)
            XCV: XCV4008(putA)
            XAC: XAC3890(putA)
            XOO: XOO4145(putA)
            XOM: XOO_3922(XOO3922)
            VVU: VV2_1118
            VVY: VVA1644
            VPA: VPA1726
            VFI: VFA0831 VFA0832
            PPR: PBPRB1999
            PAE: PA0782(putA)
            PPU: PP_4947(putA)
            PST: PSPTO_5017
            PSB: Psyr_0506
            PSP: PSPPH_0496(putA)
            PFL: PFL_0495(putA)
            PFO: Pfl_0452
            PEN: PSEEN4999(putA)
            PAR: Psyc_1249
            PCR: Pcryo_1138
            ACI: ACIAD1646(putA)
            SON: SO_3774
            SDN: Sden_0689
            SFR: Sfri_0568
            SHE: Shewmr4_3122
            SHM: Shewmr7_0850
            SHN: Shewana3_0819
            ILO: IL1961(putA)
            CPS: CPS_4410(putA)
            PHA: PSHAa2264(putA)
            CBU: CBU_0629(putA)
            CBD: COXBU7E912_0641(putA)
            LPN: lpg1696(putA)
            LPF: lpl1655(putA)
            LPP: lpp1661(putA)
            FTU: FTT1150c(putA)
            FTF: FTF1150c(putA)
            FTW: FTW_1189(putA)
            FTL: FTL_0805
            FTH: FTH_0799(putA)
            FTA: FTA_0851
            FTN: FTN_1131(putA)
            NOC: Noc_1705
            AEH: Mlg_2702
            HCH: HCH_01824(putA)
            AHA: AHA_0776
            NME: NMB0401
            NMA: NMA2084(putA)
            NMC: NMC1766(putA)
            CVI: CV_1538(putA)
            RSO: RSc3301(putA)
            REU: Reut_A3340
            REH: H16_A3631(putA)
            RME: Rmet_3489
            BMA: BMA2965(putA)
            BUR: Bcep18194_A3294
            BCN: Bcen_2942
            BCH: Bcen2424_0113
            BAM: Bamb_0103
            BPS: BPSL3389(putA)
            BPM: BURPS1710b_0166(putA)
            BPL: BURPS1106A_4032(putA)
            BPD: BURPS668_3958(putA)
            BTE: BTH_I3301
            BPE: BP0429 BP2749(putA)
            BPA: BPP2579(putA)
            BBR: BB2024(putA)
            RFR: Rfer_2811
            POL: Bpro_0406
            MPT: Mpe_A3747 Mpe_A3748
            MMS: mma_1319
            NET: Neut_1859
            NMU: Nmul_A1546
            EBA: ebA551(putA)
            AZO: azo3753(putA)
            HPY: HP0056
            HPJ: jhp0048(putA)
            HPA: HPAG1_0053
            HHE: HH0156
            HAC: Hac_1557(putA)
            TDN: Tmden_1327
            CJE: Cj1503c(putA)
            CJR: CJE1676
            CJU: C8J_1406
            GSU: GSU3395(putA)
            GME: Gmet_3512
            DVU: DVU3319(putA)
            DDE: Dde_0054
            BBA: Bd1251(putA)
            DPS: DP2491
            MXA: MXAN_5891(pruA)
            SFU: Sfum_0833 Sfum_2203
            WOL: WD0103(putA)
            WBM: Wbm0539
            AMA: AM583(putA)
            APH: APH_0669(putA)
            ERU: Erum3850(putA)
            ERW: ERWE_CDS_03970(putA)
            ERG: ERGA_CDS_03930(putA)
            ECN: Ecaj_0375
            MLO: mll1160
            MES: Meso_1325
            SME: SMc02181(putA)
            ATU: Atu4157(putA)
            ATC: AGR_L_1394
            RET: RHE_PF00384(putA)
            RLE: pRL120554(putA)
            BME: BMEII0564
            BMF: BAB2_0518
            BMB: BruAb2_0509
            BJA: blr7261(putA)
            BRA: BRADO6914(putA)
            BBT: BBta_6002(putA)
            RPA: RPA1580(putA)
            RPB: RPB_3946
            RPC: RPC_4274
            RPD: RPD_3707
            RPE: RPE_4317
            NWI: Nwi_3055
            CCR: CC_0804
            SIL: SPO3010(putA)
            SIT: TM1040_1695
            RSP: RSP_2166(putA)
            RDE: RD1_2509(putA)
            MMR: Mmar10_0398
            HNE: HNE_2333(pruA) HNE_2988
            GOX: GOX2117
            GBE: GbCGDNIH1_0110
            RRU: Rru_A0656
            MAG: amb2507
            ABA: Acid345_0400
            BSU: BG10622(rocA) BG12012(ycgN)
            BHA: BH2737 BH3940
            BAN: BA0309
            BAR: GBAA0309
            BAA: BA_0880 BA_0884
            BAT: BAS0295
            BCE: BC0344
            BCA: BCE_0338
            BCZ: BCZK0282(rocA)
            BTK: BT9727_0279(rocA)
            BTL: BALH_0301(rocA)
            BLI: BL01710
            BLD: BLi00374(ycgN)
            BCL: ABC0965
            BAY: RBAM_003450(ycgN) RBAM_034980(rocA)
            BPU: BPUM_0301(ycgN)
            OIH: OB1349(rocA)
            GKA: GK0187 GK2889
            SAU: SA2341(rocA)
            SAV: SAV2554(rocA)
            SAM: MW2475(rocA)
            SAR: SAR2634
            SAS: SAS2440
            SAC: SACOL2569
            SAB: SAB2428c
            SAA: SAUSA300_2491
            SAO: SAOUHSC_02869
            SEP: SE2116
            SER: SERP2128
            SHA: SH0500(rocA)
            SSP: SSP0311
            STH: STH2741 STH646
            MTU: Rv1187(rocA)
            MTC: MT1224(pruA)
            MBO: Mb1219(rocA)
            MBB: BCG_1249(rocA)
            MPA: MAP2593c(rocA)
            MAV: MAV_1331(pruA)
            MSM: MSMEG_5119(pruA)
            MMC: Mmcs_4026
            CGL: NCgl0098(cgl0099)
            CGB: cg0129(putA)
            CEF: CE0101
            CJK: jk0454(putA)
            NFA: nfa47480
            RHA: RHA1_ro00348(rocA1) RHA1_ro05951(rocA2)
            SCO: SCO5520(SC1C2.01)
            SMA: SAV2723(rocA)
            LXX: Lxx02530(poaA)
            PAC: PPA0620
            TFU: Tfu_0433
            FRA: Francci3_2822
            FAL: FRAAL4347(putA)
            SEN: SACE_1979
            RXY: Rxyl_2922
            RBA: RB8262(putA)
            PCU: pc0033(putA)
            SYN: sll1561(putA)
            CYB: CYB_0516
            TEL: tlr0416(putA)
            GVI: glr2755(putA)
            ANA: alr0540
            AVA: Ava_2942
            TER: Tery_3446
            BTH: BT_3115
            BFR: BF3796
            PGI: PG1269(pruA)
            SRU: SRU_1517(pruA)
            CHU: CHU_0703
            GFO: GFO_0395
            FPS: FP0415(pruA)
            DRA: DR_0813 DR_A0030
            DGE: Dgeo_0850 Dgeo_1174
            TTH: TTC1213
            TTJ: TTHA1578
            TAC: Ta0603
            TVO: TVN0653
            PTO: PTO1261
            APE: APE_0807.1
            SAI: Saci_0166
STRUCTURES  PDB: 2BHP  2BHQ  2BJA  2BJK  2EHQ  2EHU  2EII  2EIT  2EIW  2EJ6  
                 2EJD  2EJL  2IY6  2J40  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.12
            ExPASy - ENZYME nomenclature database: 1.5.1.12
            ExplorEnz - The Enzyme Database: 1.5.1.12
            ERGO genome analysis and discovery system: 1.5.1.12
            BRENDA, the Enzyme Database: 1.5.1.12
            CAS: 9054-82-4
///
ENTRY       EC 1.5.1.13       Obsolete  Enzyme
NAME        Transferred to 1.17.1.5
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Transferred entry: now EC 1.17.1.5, nicotinate dehydrogenase. The
            enzyme was incorrectly classified as acting on a CH-NH group. (EC
            1.5.1.13 created 1972, deleted 2004)
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.13
            ExPASy - ENZYME nomenclature database: 1.5.1.13
            ExplorEnz - The Enzyme Database: 1.5.1.13
            ERGO genome analysis and discovery system: 1.5.1.13
            BRENDA, the Enzyme Database: 1.5.1.13
///
ENTRY       EC 1.5.1.14       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: 1,2-didehydropipecolate reductase. Now included with
            EC 1.5.1.21 Delta1-piperideine-2-carboxylate reductase (EC 1.5.1.14
            created 1976, deleted 1989)
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.14
            ExPASy - ENZYME nomenclature database: 1.5.1.14
            ExplorEnz - The Enzyme Database: 1.5.1.14
            ERGO genome analysis and discovery system: 1.5.1.14
            BRENDA, the Enzyme Database: 1.5.1.14
///
ENTRY       EC 1.5.1.15                 Enzyme
NAME        methylenetetrahydrofolate dehydrogenase (NAD+);
            methylenetetrahydrofolate dehydrogenase (NAD+)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     5,10-methylenetetrahydrofolate:NAD+ oxidoreductase
REACTION    5,10-methylenetetrahydrofolate + NAD+ =
            5,10-methenyltetrahydrofolate + NADH + H+ [RN:R01218]
ALL_REAC    R01218
SUBSTRATE   5,10-methylenetetrahydrofolate [CPD:C00143];
            NAD+ [CPD:C00003]
PRODUCT     5,10-methenyltetrahydrofolate [CPD:C00445];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4153026]
  AUTHORS   Moore MR, O'Brien WE, Ljungdahl LG.
  TITLE     Purification and characterization of nicotinamide adenine
            dinucleotide-dependent methylenetetrahydrofolate dehydrogenase from
            Clostridium formicoaceticum.
  JOURNAL   J. Biol. Chem. 249 (1974) 5250-3.
  ORGANISM  Clostridium formicoaceticum
PATHWAY     PATH: map00670  One carbon pool by folate
ORTHOLOGY   KO: K00295  methylenetetrahydrofolate dehydrogenase (NAD+)
GENES       HSA: 10797(MTHFD2) 4522(MTHFD1)
            MMU: 17768(Mthfd2)
            RNO: 313410(RGD1564040_predicted)
            GGA: 426126(RCJMB04_12b8)
            XLA: 446641(mthfd2)
            SPU: 588966(LOC588966)
            SCE: YKR080W(MTD1)
            AGO: AGOS_ADR214W
            PIC: PICST_73792
            SPO: SPBC1711.04
            ANI: AN1524.2
            AFM: AFUA_8G05330
            AOR: AO090005000616
            CNE: CNF03710
            DDI: DDB_0230118(thfA)
            MMO: MMOB1600(folD)
STRUCTURES  PDB: 1EDZ  1EE9  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.15
            ExPASy - ENZYME nomenclature database: 1.5.1.15
            ExplorEnz - The Enzyme Database: 1.5.1.15
            ERGO genome analysis and discovery system: 1.5.1.15
            BRENDA, the Enzyme Database: 1.5.1.15
            CAS: 82062-90-6
///
ENTRY       EC 1.5.1.16                 Enzyme
NAME        D-lysopine dehydrogenase;
            D-lysopine synthase;
            lysopine dehydrogenase;
            D(+)-lysopine dehydrogenase;
            2-N-(D-1-carboxyethyl)-L-lysine:NADP+ oxidoreductase
            (L-lysine-forming)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N2-(D-1-carboxyethyl)-L-lysine:NADP+ oxidoreductase
            (L-lysine-forming)
REACTION    N2-(D-1-carboxyethyl)-L-lysine + NADP+ + H2O = L-lysine + pyruvate +
            NADPH + H+ [RN:R00452]
ALL_REAC    R00452
SUBSTRATE   N2-(D-1-carboxyethyl)-L-lysine [CPD:C04020];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     L-lysine [CPD:C00047];
            pyruvate [CPD:C00022];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     In the reverse reaction, a number of L-amino acids can act instead
            of L-lysine, and 2-oxobutanoate and, to a lesser extent, glyoxylate
            can act instead of pyruvate.
REFERENCE   1  [PMID:21695]
  AUTHORS   Otten LA, Vreugdenhil D, Schilperoort RA.
  TITLE     Properties of D(+)-lysopine dehydrogenase from crown gall tumour
            tissue.
  JOURNAL   Biochim. Biophys. Acta. 485 (1977) 268-77.
  ORGANISM  Nicotiana tabacum
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.16
            ExPASy - ENZYME nomenclature database: 1.5.1.16
            ExplorEnz - The Enzyme Database: 1.5.1.16
            ERGO genome analysis and discovery system: 1.5.1.16
            BRENDA, the Enzyme Database: 1.5.1.16
            CAS: 65187-41-9
///
ENTRY       EC 1.5.1.17                 Enzyme
NAME        alanopine dehydrogenase;
            ALPDH ;
            alanopine[meso-N-(1-carboxyethyl)-alanine]dehydrogenase;
            meso-N-(1-carboxyethyl)-alanine:NAD+ oxidoreductase;
            alanopine: NAD+ oxidoreductase;
            ADH;
            alanopine:NAD+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2,2'-iminodipropanoate:NAD+ oxidoreductase (L-alanine-forming)
REACTION    2,2'-iminodipropanoate + NAD+ + H2O = L-alanine + pyruvate + NADH +
            H+ [RN:R00398]
ALL_REAC    R00398
SUBSTRATE   2,2'-iminodipropanoate [CPD:C03210];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     L-alanine [CPD:C00041];
            pyruvate [CPD:C00022];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     In the reverse reaction, L-alanine can be replaced by L-cysteine,
            L-serine or L-threonine; glycine acts very slowly (cf. EC 1.5.1.22
            strombine dehydrogenase).
REFERENCE   1
  AUTHORS   Dando, P.R.
  TITLE     Strombine [N-(carboxymethyl)-D-alanine] dehydrogenase and alanopine
            [meso-N-(1-carboxyethyl)-alanine dehydrogenase from the mussel
            Mytilus edulis L.
  JOURNAL   Biochem. Soc. Trans. 9 (1981) 297-298.
  ORGANISM  Mytilus edulis
REFERENCE   2  [PMID:6156653]
  AUTHORS   Fields JH, Eng AK, Ramsden WD, Hochachka PW, Weinstein B.
  TITLE     Alanopine and strombine are novel imino acids produced by a
            dehydrogenase found in the adductor muscle of the oyster,
            Crassostrea gigas.
  JOURNAL   Arch. Biochem. Biophys. 201 (1980) 110-4.
  ORGANISM  Crassostrea gigas
REFERENCE   3  [PMID:7238503]
  AUTHORS   Fields JH, Hochachka PW.
  TITLE     Purification and properties of alanopine dehydrogenase from the
            adductor muscle of the oyster, Crassostrea gigas (Mollusca,
            Bivalvia).
  JOURNAL   Eur. J. Biochem. 114 (1981) 615-21.
  ORGANISM  Crassostrea gigas
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.17
            ExPASy - ENZYME nomenclature database: 1.5.1.17
            ExplorEnz - The Enzyme Database: 1.5.1.17
            ERGO genome analysis and discovery system: 1.5.1.17
            BRENDA, the Enzyme Database: 1.5.1.17
            CAS: 71343-07-2
///
ENTRY       EC 1.5.1.18                 Enzyme
NAME        ephedrine dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (-)-ephedrine:NAD+ 2-oxidoreductase
REACTION    (-)-ephedrine + NAD+ = (R)-2-methylimino-1-phenylpropan-1-ol + NADH
            + H+ [RN:R03614]
ALL_REAC    R03614
SUBSTRATE   (-)-ephedrine [CPD:C01575];
            NAD+ [CPD:C00003]
PRODUCT     (R)-2-methylimino-1-phenylpropan-1-ol [CPD:C04351];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     The product immediately hydrolyses to methylamine and
            1-hydroxy-1-phenylpropan-2-one. Acts on a number of related
            compounds including (-)-sympatol, (+)-pseudoephedrine and
            (+)-norephedrine.
REFERENCE   1  [PMID:7405363]
  AUTHORS   Klamann E, Lingens F.
  TITLE     Degradation of (-)-ephedrine by Pseudomonas putida. Detection of
            (-)-ephedrine: NAD+-oxidoreductase from Arthrobacter globiformis.
  JOURNAL   Z. Naturforsch. [C]. 35 (1980) 80-7.
  ORGANISM  Arthrobacter globiformis
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.18
            ExPASy - ENZYME nomenclature database: 1.5.1.18
            ExplorEnz - The Enzyme Database: 1.5.1.18
            ERGO genome analysis and discovery system: 1.5.1.18
            BRENDA, the Enzyme Database: 1.5.1.18
            CAS: 73508-06-2
///
ENTRY       EC 1.5.1.19                 Enzyme
NAME        D-nopaline dehydrogenase;
            D-nopaline synthase;
            nopaline dehydrogenase;
            nopaline synthase;
            NOS;
            2-N-(D-1,3-dicarboxypropyl)-L-arginine:NADP+ oxidoreductase
            (L-arginine-forming)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N2-(D-1,3-dicarboxypropyl)-L-arginine:NADP+ oxidoreductase
            (L-arginine-forming)
REACTION    N2-(D-1,3-dicarboxypropyl)-L-arginine + NADP+ + H2O = L-arginine +
            2-oxoglutarate + NADPH + H+ [RN:R00563]
ALL_REAC    R00563
SUBSTRATE   N2-(D-1,3-dicarboxypropyl)-L-arginine [CPD:C01682];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     L-arginine [CPD:C00062];
            2-oxoglutarate [CPD:C00026];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     In the reverse direction, forms D-nopaline from L-arginine and
            D-ornaline from L-ornithine.
REFERENCE   1  [PMID:476084]
  AUTHORS   Kemp JD, Sutton DW, Hack E.
  TITLE     Purification and characterization of the crown gall specific enzyme
            nopaline synthase.
  JOURNAL   Biochemistry. 18 (1979) 3755-60.
  ORGANISM  Helianthus annuus[GN:ehan], Agrobacterium tumefaciens
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K00296  D-nopaline dehydrogenase
GENES       BPL: BURPS1106A_A0476
            BPD: BURPS668_A0573
            ATU: Atu6015(nos)
            ATC: AGR_pTi_53(nos)
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.19
            ExPASy - ENZYME nomenclature database: 1.5.1.19
            ExplorEnz - The Enzyme Database: 1.5.1.19
            ERGO genome analysis and discovery system: 1.5.1.19
            BRENDA, the Enzyme Database: 1.5.1.19
            CAS: 64763-57-1
///
ENTRY       EC 1.5.1.20                 Enzyme
NAME        methylenetetrahydrofolate reductase [NAD(P)H];
            methylenetetrahydrofolate (reduced nicotinamide adenine dinucleotide
            phosphate) reductase;
            5,10-methylenetetrahydrofolate reductase (NADPH);
            5,10-methylenetetrahydrofolic acid reductase;
            5,10-CH2-H4folate reductase;
            methylenetetrahydrofolate reductase (NADPH2);
            5-methyltetrahydrofolate:NAD+ oxidoreductase;
            5-methyltetrahydrofolate:NAD+ oxidoreductase;
            methylenetetrahydrofolate (reduced riboflavin adenine dinucleotide)
            reductase;
            5,10-methylenetetrahydrofolate reductase;
            methylenetetrahydrofolate reductase;
            N5,10-methylenetetrahydrofolate reductase;
            5,10-methylenetetrahydropteroylglutamate reductase;
            N5,N10-methylenetetrahydrofolate reductase;
            methylenetetrahydrofolic acid reductase;
            5-methyltetrahydrofolate:(acceptor) oxidoreductase (incorrect);
            5,10-methylenetetrahydrofolate reductase (FADH2);
            MetF;
            methylenetetrahydrofolate reductase (NADPH);
            5-methyltetrahydrofolate:NADP+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     5-methyltetrahydrofolate:NAD(P)+ oxidoreductase
REACTION    5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate
            + NAD(P)H + H+ [RN:R01224 R07168]
ALL_REAC    R01224 R07168
SUBSTRATE   5-methyltetrahydrofolate [CPD:C00440];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     5,10-methylenetetrahydrofolate [CPD:C00143];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Menadione can also serve as an electron
            acceptor.
REFERENCE   1  [PMID:6975779]
  AUTHORS   Daubner SC, Matthews RG.
  TITLE     Purification and properties of methylenetetrahydrofolate reductase
            from pig liver.
  JOURNAL   J. Biol. Chem. 257 (1982) 140-5.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:4399897]
  AUTHORS   Kutzbach C, Stokstad EL.
  TITLE     Mammalian methylenetetrahydrofolate reductase. Partial purification,
            properties, and inhibition by S-adenosylmethionine.
  JOURNAL   Biochim. Biophys. Acta. 250 (1971) 459-77.
  ORGANISM  pig [GN:ssc], rat [GN:rno]
REFERENCE   3  [PMID:9922232]
  AUTHORS   Sheppard CA, Trimmer EE, Matthews RG.
  TITLE     Purification and properties of NADH-dependent 5,
            10-methylenetetrahydrofolate reductase (MetF) from Escherichia coli.
  JOURNAL   J. Bacteriol. 181 (1999) 718-25.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:10201405]
  AUTHORS   Guenther BD, Sheppard CA, Tran P, Rozen R, Matthews RG, Ludwig ML.
  TITLE     The structure and properties of methylenetetrahydrofolate reductase
            from Escherichia coli suggest how folate ameliorates human
            hyperhomocysteinemia.
  JOURNAL   Nat. Struct. Biol. 6 (1999) 359-65.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00670  One carbon pool by folate
            PATH: map00680  Methane metabolism
ORTHOLOGY   KO: K00297  methylenetetrahydrofolate reductase (NADPH)
GENES       HSA: 4524(MTHFR)
            MMU: 17769(Mthfr)
            CFA: 478230(MTHFR)
            BTA: 497032(MTHFR)
            GGA: 419489(MTHFR)
            XLA: 379784(mthfr)
            SPU: 589576(LOC589576)
            CEL: C06A8.1
            ATH: AT3G59970(MTHFR1)
            OSA: 4334554
            CME: CMT610C
            SCE: YGL125W(MET13)
            AGO: AGOS_AAR170W AGOS_AFR457W
            PIC: PICST_71674 PICST_83803
            CGR: CAGL0F07029g CAGL0J09504g
            SPO: SPAC343.10(mthfr2) SPAC56F8.10
            ANI: AN5883.2 AN8215.2
            AFM: AFUA_2G11300 AFUA_5G03480
            AOR: AO090026000520 AO090102000557
            CNE: CNA07390 CNL04820
            UMA: UM04612.1
            DDI: DDB_0230137
            LMA: LmjF36.6390
            ECO: b3941(metF)
            ECJ: JW3913(metF)
            ECE: Z5496(metF)
            ECS: ECs4870
            ECC: c4899(metF)
            ECI: UTI89_C4531(metF)
            ECP: ECP_4155
            ECV: APECO1_2525(metF)
            ECW: EcE24377A_4481(metF)
            ECX: EcHS_A4175
            STY: STY3761(metF)
            STT: t3511(metF)
            SPT: SPA3951(metF)
            SEC: SC3997(metF)
            STM: STM4105(metF)
            YPE: YPO0117(metF) YPO0287
            YPK: y0304(metF) y0548
            YPM: YP_0119(metF1) YP_0445(metF2)
            YPA: YPA_0266 YPA_3994
            YPN: YPN_3379 YPN_3737
            YPP: YPDSF_3790
            YPS: YPTB0107(metF) YPTB0345
            YPI: YpsIP31758_0123(metF)
            YEN: YE0114(metF)
            SFL: SF4019(metF)
            SFX: S3728(metF)
            SFV: SFV_4011(metF)
            SSN: SSON_4115(metF)
            SBO: SBO_3961(metF)
            SDY: SDY_3776(metF)
            ECA: ECA4244(metF)
            PLU: plu4754(metF)
            BUC: BU046(metF)
            BAS: BUsg043(metF)
            BAB: bbp047(metF)
            BCC: BCc_030(metF)
            SGL: SG2162
            SPE: Spro_4784
            BFL: Bfl597(metF)
            BPN: BPEN_619(metF)
            HIN: HI1444(metF)
            HIT: NTHI1686(metF)
            HIP: CGSHiEE_04820(metF)
            HIQ: CGSHiGG_01105(metF)
            HSO: HS_1130(metF)
            PMU: PM0235(metF)
            MSU: MS0787(metF)
            APL: APL_0854(metF)
            XFA: XF1121
            XFT: PD0413(metF)
            XCC: XCC0314(metF) XCC0739(metF)
            XCB: XC_0326 XC_3496
            XCV: XCV0340 XCV0842(metF)
            XAC: XAC0331(metF) XAC0791(metF)
            XOO: XOO3810(metF) XOO4338(metF)
            XOM: XOO_3591(XOO3591) XOO_4089(XOO4089)
            VCH: VC2685
            VCO: VC0395_A2258(metF)
            VVU: VV1_1366
            VVY: VV3006
            VPA: VP2763
            VFI: VF2309
            PPR: PBPRA0263
            PAE: PA0430(metF)
            PAU: PA14_05590(metF)
            PAP: PSPA7_0530(metF)
            PPU: PP_4977(metF)
            PST: PSPTO_5069(metF)
            PSB: Psyr_0459
            PSP: PSPPH_0450(metF)
            PFL: PFL_5799(metF)
            PFO: Pfl_5281
            PEN: PSEEN5038(metF)
            PAR: Psyc_0967(metF)
            PCR: Pcryo_1449
            ACI: ACIAD2283(metF)
            SON: SO_4054(metF)
            SDN: Sden_0642
            SFR: Sfri_3547
            SAZ: Sama_3169
            SBL: Sbal_3774
            SLO: Shew_0522
            SPC: Sputcn32_0618
            SSE: Ssed_4039
            SPL: Spea_0562
            SHE: Shewmr4_3437
            SHM: Shewmr7_0514
            SHN: Shewana3_3612
            SHW: Sputw3181_3552
            PAT: Patl_3955
            SDE: Sde_0468
            MAQ: Maqu_3044
            CBU: CBU_2047(metF)
            CBD: COXBU7E912_2143(metF)
            MCA: MCA0137(metF)
            TCX: Tcr_1822
            NOC: Noc_2680
            AEH: Mlg_2264
            HHA: Hhal_1674
            HCH: HCH_01531(metF)
            CSA: Csal_0396
            ABO: ABO_2619(metF)
            AHA: AHA_3949(metF)
            DNO: DNO_0863(metF)
            BCI: BCI_0162(metF)
            CRP: CRP_015
            RMA: Rmag_0851
            VOK: COSY_0776(metF)
            NME: NMB0943
            NMA: NMA1139(metF)
            NMC: NMC0921(metF)
            NGO: NGO0929
            CVI: CV_0966(metF)
            RSO: RSc0091(metF)
            REU: Reut_A0215
            REH: H16_A0246
            RME: Rmet_0172 Rmet_2988
            BMA: BMA2840(metF)
            BMV: BMASAVP1_A3415(metF)
            BML: BMA10299_A1703(metF)
            BMN: BMA10247_3136(metF)
            BXE: Bxe_A0180
            BUR: Bcep18194_A3377
            BCN: Bcen_2833
            BCH: Bcen2424_0274
            BAM: Bamb_0188
            BPS: BPSL3288(metF)
            BPM: BURPS1710b_0055(metF)
            BPD: BURPS668_3836(metF)
            BTE: BTH_I3163(metF)
            BPE: BP3066
            BPA: BPP0197
            BBR: BB0200
            RFR: Rfer_0654
            POL: Bpro_4130
            PNA: Pnap_0491
            AAV: Aave_4058
            AJS: Ajs_0620
            VEI: Veis_0654
            HAR: HEAR2948(metF)
            NEU: NE0661(metF)
            NET: Neut_1891
            NMU: Nmul_A2539
            EBA: ebA1875(metF)
            DAR: Daro_0183
            TBD: Tbd_2517
            MFA: Mfla_0191
            CJE: Cj1202(metF)
            CJR: CJE1336(metF)
            CJU: C8J_1146(metF)
            NIS: NIS_1309
            SUN: SUN_0641
            PCA: Pcar_1732
            PPD: Ppro_1089
            DVU: DVU0997(metF)
            DVL: Dvul_1992
            DDE: Dde_2525
            DPS: DP1612
            ADE: Adeh_2676
            MXA: MXAN_3039(metF)
            SAT: SYN_02872
            PUB: SAR11_1264(metF)
            MLO: mll1587
            MES: Meso_2028
            SME: SMa2143 SMc01843(metF)
            ATU: Atu1418(metF) Atu2123(metF)
            ATC: AGR_C_2619 AGR_C_3850
            RET: RHE_CH02871(metF)
            RLE: RL3331(metF) pRL90256
            BME: BMEI0559
            BMF: BAB1_1468(metF)
            BMS: BR1450(metF)
            BMB: BruAb1_1445(metF)
            BOV: BOV_1406(metF)
            BJA: bll1419(metF)
            BRA: BRADO0995(metF)
            BBT: BBta_7060(metF)
            RPA: RPA3701(metF)
            RPB: RPB_1765
            RPC: RPC_3734
            RPD: RPD_3540
            RPE: RPE_3772
            NWI: Nwi_0284
            NHA: Nham_0364
            CCR: CC_2140
            SIL: SPO1862 SPO3016(metF)
            SIT: TM1040_1185 TM1040_1700
            RSP: RSP_2172(metF) RSP_2769
            RSH: Rsph17029_0844
            JAN: Jann_1026 Jann_1978
            RDE: RD1_1762(metF) RD1_3056(metF)
            PDE: Pden_2319
            MMR: Mmar10_2438
            HNE: HNE_2103(metF)
            ZMO: ZMO1747(metF)
            NAR: Saro_2860 Saro_3208
            SAL: Sala_0035
            ELI: ELI_10095
            GOX: GOX0791 GOX2207
            GBE: GbCGDNIH1_0206
            RRU: Rru_A1530
            MGM: Mmc1_1506
            BCL: ABC1868
            BPU: BPUM_1027(yitJ)
            LLA: L0099(metF)
            SPN: SP_0586
            SPR: spr0515(metF)
            SPD: SPD_0511(metF)
            STC: str0786(metF)
            STL: stu0786(metF)
            SSA: SSA_0417(metF)
            LBU: LBUL_1231
            LCA: LSEI_0624
            CTH: Cthe_0099
            CBO: CBO1621(metF)
            CBA: CLB_1639(metF)
            CBH: CLC_1648(metF)
            CBF: CLI_1699(metF)
            SWO: Swol_0934
            CGL: NCgl2091(cgl2171)
            CGB: cg2383(metF)
            CEF: CE2066
            CDI: DIP1611
            CJK: jk0737(metF)
            NFA: nfa17400(metF)
            RHA: RHA1_ro01105
            SCO: SCO2103(metF)
            SMA: SAV6100(metF)
            ART: Arth_0063 Arth_2367
            NCA: Noca_3083
            TFU: Tfu_1050
            FRA: Francci3_1389
            FAL: FRAAL2163(metF)
            ACE: Acel_0991
            SEN: SACE_1715(metF) SACE_3895(metF) SACE_5618(metF)
            BLO: BL0797(metF)
            BAD: BAD_0757(metF)
            RXY: Rxyl_0765
            RBA: RB7546(metF)
            LIL: LB002(metF)
            LIC: LIC20002(metF)
            LBJ: LBJ_4004(metF)
            LBL: LBL_4004(metF)
            SYR: SynRCC307_0227(metF)
            SYX: SynWH7803_2283(metF)
            AVA: Ava_2992
            BTH: BT_3821
            BFR: BF4092
            BFS: BF3908
            SRU: SRU_2094(metF)
            CHU: CHU_1435(metF)
            GFO: GFO_0334(metF)
            CTE: CT1368(metF)
            CCH: Cag_1108
            CPH: Cpha266_1723
            PVI: Cvib_0706
            PLT: Plut_1347
            DGE: Dgeo_1337
            TTH: TTC1656
            TTJ: TTHA0327
            AAE: aq_1429(metF)
            HMA: pNG7363(metF)
            HWA: HQ1756A(metF)
STRUCTURES  PDB: 2FMN  2FMO  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.20
            ExPASy - ENZYME nomenclature database: 1.5.1.20
            ExplorEnz - The Enzyme Database: 1.5.1.20
            ERGO genome analysis and discovery system: 1.5.1.20
            BRENDA, the Enzyme Database: 1.5.1.20
            CAS: 71822-25-8
///
ENTRY       EC 1.5.1.21                 Enzyme
NAME        Delta1-piperideine-2-carboxylate reductase;
            1,2-didehydropipecolate reductase;
            P2C reductase;
            1,2-didehydropipecolic reductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-pipecolate:NADP+ 2-oxidoreductase
REACTION    L-pipecolate + NADP+ = Delta1-piperideine-2-carboxylate + NADPH + H+
            [RN:R02203]
ALL_REAC    R02203;
            (other) R02201
SUBSTRATE   L-pipecolate [CPD:C00408];
            NADP+ [CPD:C00006]
PRODUCT     Delta1-piperideine-2-carboxylate [CPD:C04092];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:6801013]
  AUTHORS   Payton CW, Chang YF.
  TITLE     delta1-piperideine-2-carboxylate reductase of Pseudomonas putida.
  JOURNAL   J. Bacteriol. 149 (1982) 864-71.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.21
            ExPASy - ENZYME nomenclature database: 1.5.1.21
            ExplorEnz - The Enzyme Database: 1.5.1.21
            ERGO genome analysis and discovery system: 1.5.1.21
            BRENDA, the Enzyme Database: 1.5.1.21
            CAS: 52037-88-4
///
ENTRY       EC 1.5.1.22                 Enzyme
NAME        strombine dehydrogenase;
            strombine[N-(carboxymethyl)-D-alanine]dehydrogenase;
            N-(carboxymethyl)-D-alanine: NAD+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N-(carboxymethyl)-D-alanine:NAD+ oxidoreductase (glycine-forming)
REACTION    N-(carboxymethyl)-D-alanine + NAD+ + H2O = glycine + pyruvate + NADH
            + H+ [RN:R00368]
ALL_REAC    R00368
SUBSTRATE   N-(carboxymethyl)-D-alanine [CPD:C03790];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     glycine [CPD:C00037];
            pyruvate [CPD:C00022];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also catalyses the reaction of EC 1.5.1.17 alanopine dehydrogenase,
            but more slowly. Does not act on L-strombine.
REFERENCE   1
  AUTHORS   Dando, P.R.
  TITLE     Strombine [N-(carboxymethyl)-D-alanine] dehydrogenase and alanopine
            [meso-N-(1-carboxyethyl)-alanine dehydrogenase from the mussel
            Mytilus edulis L.
  JOURNAL   Biochem. Soc. Trans. 9 (1981) 297-298.
  ORGANISM  Mytilus edulis
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.22
            ExPASy - ENZYME nomenclature database: 1.5.1.22
            ExplorEnz - The Enzyme Database: 1.5.1.22
            ERGO genome analysis and discovery system: 1.5.1.22
            BRENDA, the Enzyme Database: 1.5.1.22
            CAS: 79393-84-3
///
ENTRY       EC 1.5.1.23                 Enzyme
NAME        tauropine dehydrogenase;
            2-N-(D-1-carboxyethyl)taurine:NAD+ oxidoreductase (taurine-forming)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N2-(D-1-carboxyethyl)taurine:NAD+ oxidoreductase (taurine-forming)
REACTION    tauropine + NAD+ + H2O = taurine + pyruvate + NADH + H+ [RN:R01683]
ALL_REAC    R01683
SUBSTRATE   tauropine [CPD:C01616];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     taurine [CPD:C00245];
            pyruvate [CPD:C00022];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     In the reverse reaction, alanine can act instead of taurine, but
            more slowly, and 2-oxobutanoate and 2-oxopentanoate can act instead
            of pyruvate.
REFERENCE   1  [PMID:3769931]
  AUTHORS   Gade G.
  TITLE     Purification and properties of tauropine dehydrogenase from the
            shell adductor muscle of the ormer, Haliotis lamellosa.
  JOURNAL   Eur. J. Biochem. 160 (1986) 311-8.
  ORGANISM  Haliotis lamellosa
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.23
            ExPASy - ENZYME nomenclature database: 1.5.1.23
            ExplorEnz - The Enzyme Database: 1.5.1.23
            ERGO genome analysis and discovery system: 1.5.1.23
            BRENDA, the Enzyme Database: 1.5.1.23
            CAS: 104645-74-1
///
ENTRY       EC 1.5.1.24                 Enzyme
NAME        N5-(carboxyethyl)ornithine synthase;
            5-N-(L-1-carboxyethyl)-L-ornithine:NADP+ oxidoreductase
            (L-ornithine-forming)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N5-(L-1-carboxyethyl)-L-ornithine:NADP+ oxidoreductase
            (L-ornithine-forming)
REACTION    N5-(L-1-carboxyethyl)-L-ornithine + NADP+ + H2O = L-ornithine +
            pyruvate + NADPH + H+ [RN:R00666]
ALL_REAC    R00666
SUBSTRATE   N5-(L-1-carboxyethyl)-L-ornithine [CPD:C04210];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     L-ornithine [CPD:C00077];
            pyruvate [CPD:C00022];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     In the reverse direction, L-lysine can act instead of L-ornithine,
            but more slowly. Acts on the amino group. cf. EC 1.5.1.16,
            D-lysopine dehydrogenase.
REFERENCE   1  [PMID:2498334]
  AUTHORS   Thompson J.
  TITLE     N5-(L-1-carboxyethyl)-L-ornithine:NADP+ oxidoreductase from
            Streptococcus lactis. Purification and partial characterization.
  JOURNAL   J. Biol. Chem. 264 (1989) 9592-601.
  ORGANISM  Streptococcus lactis
ORTHOLOGY   KO: K00298  N5-(carboxyethyl)ornithine synthase
GENES       LLA: L64332(ceo)
            CTC: CTC00375
            CBO: CBO0515(ceo)
            CBA: CLB_0555(ceo)
            CBH: CLC_0588(ceo)
            CBF: CLI_0595(ceo)
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.24
            ExPASy - ENZYME nomenclature database: 1.5.1.24
            ExplorEnz - The Enzyme Database: 1.5.1.24
            ERGO genome analysis and discovery system: 1.5.1.24
            BRENDA, the Enzyme Database: 1.5.1.24
            CAS: 129070-70-8
///
ENTRY       EC 1.5.1.25                 Enzyme
NAME        thiomorpholine-carboxylate dehydrogenase;
            ketimine reductase;
            ketimine-reducing enzyme
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     thiomorpholine-3-carboxylate:NAD(P)+ 5,6-oxidoreductase
REACTION    thiomorpholine 3-carboxylate + NAD(P)+ =
            3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+ [RN:R04339
            R04340]
ALL_REAC    R04339 R04340
SUBSTRATE   thiomorpholine 3-carboxylate [CPD:C03901];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     3,4-dehydro-thiomorpholine-3-carboxylate;
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The product is the cyclic imine of the 2-oxoacid corresponding to
            S-(2-aminoethyl)cysteine. In the reverse direction, a number of
            other cyclic unsaturated compounds can act as substrates, but more
            slowly.
REFERENCE   1  [PMID:3371353]
  AUTHORS   Nardini M, Ricci G, Caccuri AM, Solinas SP, Vesci L, Cavallini D.
  TITLE     Purification and characterization of a ketimine-reducing enzyme.
  JOURNAL   Eur. J. Biochem. 173 (1988) 689-94.
  ORGANISM  pig [GN:ssc]
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.25
            ExPASy - ENZYME nomenclature database: 1.5.1.25
            ExplorEnz - The Enzyme Database: 1.5.1.25
            ERGO genome analysis and discovery system: 1.5.1.25
            BRENDA, the Enzyme Database: 1.5.1.25
            CAS: 115232-54-7
///
ENTRY       EC 1.5.1.26                 Enzyme
NAME        beta-alanopine dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N-(D-1-carboxyethyl)-beta-alanine:NAD+ oxidoreductase
            (beta-alanine-forming)
REACTION    beta-alanopine + NAD+ + H2O = beta-alanine + pyruvate + NADH + H+
            [RN:R00906]
ALL_REAC    R00906
SUBSTRATE   beta-alanopine [CPD:C02207];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     beta-alanine [CPD:C00099];
            pyruvate [CPD:C00022];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Sato, M., Takahara, M., Kanno, N., Sato, Y. and Ellington, W.R.
  TITLE     Isolation of a new opine, beta-alanopine, from the extracts of the
            muscle of the marine bivalve mollusc Scapharca broughtonii.
  JOURNAL   Comp. Biochem. Physiol. 88B (1987) 803-806.
  ORGANISM  Scapharca broughtonii
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.26
            ExPASy - ENZYME nomenclature database: 1.5.1.26
            ExplorEnz - The Enzyme Database: 1.5.1.26
            ERGO genome analysis and discovery system: 1.5.1.26
            BRENDA, the Enzyme Database: 1.5.1.26
            CAS: 113573-64-1
///
ENTRY       EC 1.5.1.27                 Enzyme
NAME        1,2-dehydroreticulinium reductase (NADPH);
            1,2-dehydroreticulinium ion reductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-reticuline:NADP+ oxidoreductase
REACTION    (R)-reticuline + NADP+ = 1,2-dehydroreticulinium + NADPH + H+
            [RN:R04695]
ALL_REAC    R04695
SUBSTRATE   (R)-reticuline [CPD:C05178];
            NADP+ [CPD:C00006]
PRODUCT     1,2-dehydroreticulinium [CPD:C06167];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Reduces the 1,2-dehydroreticulinium ion to (R)-reticuline, which is
            a direct precursor of morphinan alkaloids in the poppy plant. The
            enzyme does not catalyse the reverse reaction to any significant
            extent under physiological conditions.
REFERENCE   1
  AUTHORS   De-Eknamkul, W. and Zenk, M.H.
  TITLE     Purification and properties of 1,2-dehydroreticulinium reductase
            from Papaver somniferum seedlings.
  JOURNAL   Phytochemistry 31 (1992) 813-821.
  ORGANISM  Papaver somniferum
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.27
            ExPASy - ENZYME nomenclature database: 1.5.1.27
            ExplorEnz - The Enzyme Database: 1.5.1.27
            ERGO genome analysis and discovery system: 1.5.1.27
            BRENDA, the Enzyme Database: 1.5.1.27
            CAS: 130590-58-8
///
ENTRY       EC 1.5.1.28                 Enzyme
NAME        opine dehydrogenase;
            (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate dehydrogenase (NAD+,
            L-aminopentanoate-forming)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate:NAD+ oxidoreductase
            (L-aminopentanoate-forming)
REACTION    (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate + NAD+ + H2O =
            L-2-aminopentanoic acid + pyruvate + NADH + H+ [RN:R03732]
ALL_REAC    R03732
SUBSTRATE   (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate [CPD:C06326];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     L-2-aminopentanoic acid [CPD:C01826];
            pyruvate [CPD:C00022];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     In the forward direction, the enzyme from Arthrobacter sp. acts also
            on secondary amine dicarboxylates such as
            N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine.
            Dehydrogenation forms an imine, which dissociates to the amino acid
            and pyruvate. In the reverse direction, the enzyme acts also on
            neutral amino acids as an amino donor. They include L-amino acids
            such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic
            acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine,
            valine, phenylalanine, leucine and alanine. The amino acceptors
            include 2-oxoacids such as pyruvate, oxaloacetate, glyoxylate and
            2-oxobutyrate.
REFERENCE   1  [PMID:2753861]
  AUTHORS   Asano Y, Yamaguchi K, Kondo K.
  TITLE     A new NAD+-dependent opine dehydrogenase from Arthrobacter sp.
            strain 1C.
  JOURNAL   J. Bacteriol. 171 (1989) 4466-71.
  ORGANISM  Arthrobacter sp.
REFERENCE   2  [PMID:7487048]
  AUTHORS   Dairi T, Asano Y.
  TITLE     Cloning, nucleotide sequencing, and expression of an opine
            dehydrogenase gene from Arthrobacter sp. strain 1C.
  JOURNAL   Appl. Environ. Microbiol. 61 (1995) 3169-71.
  ORGANISM  Arthrobacter sp.
REFERENCE   3
  AUTHORS   Kato, Y., Yamada, H. and Asano, Y.
  TITLE     Stereoselective synthesis of opine-type secondary amine carboxylic
            acids by a new enzyme opine dehydrogenase. Use of recombinant
            enzymes.
  JOURNAL   J. Mol. Catal., B Enzym. 1 (1996) 151-160.
  ORGANISM  Arthrobacter sp.
GENES       BUR: Bcep18194_B2489
            VEI: Veis_1521
            SMD: Smed_3845
            BRA: BRADO2316
            BBT: BBta_2679
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.28
            ExPASy - ENZYME nomenclature database: 1.5.1.28
            ExplorEnz - The Enzyme Database: 1.5.1.28
            ERGO genome analysis and discovery system: 1.5.1.28
            BRENDA, the Enzyme Database: 1.5.1.28
            CAS: 108281-02-3
///
ENTRY       EC 1.5.1.29                 Enzyme
NAME        FMN reductase;
            NAD(P)H-FMN reductase;
            NAD(P)H-dependent FMN reductase;
            NAD(P)H:FMN oxidoreductase;
            NAD(P)H:flavin oxidoreductase;
            NAD(P)H2 dehydrogenase (FMN);
            NAD(P)H2:FMN oxidoreductase;
            SsuE ;
            riboflavin mononucleotide reductase;
            flavine mononucleotide reductase;
            riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide
            (phosphate)) reductase;
            flavin mononucleotide reductase;
            riboflavine mononucleotide reductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     FMNH2:NAD(P)+ oxidoreductase
REACTION    FMNH2 + NAD(P)+ = FMN + NAD(P)H + H+ [RN:R05705 R05706]
ALL_REAC    R05705 R05706
SUBSTRATE   FMNH2 [CPD:C01847];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     FMN [CPD:C00061];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The enzyme from luminescent bacteria and the SsuE enzyme from
            Escherichia coli also reduce riboflavin and FAD, but more slowly. In
            E. coli, this enzyme, in conjunction with EC 1.14.14.5,
            alkanesulfonate monooxygenase, forms a two-component alkanesulfonate
            monooxygenase, which allows for utilization of alkanesulfonates as
            sulfur sources under conditions of sulfate and cysteine starvation.
REFERENCE   1  [PMID:47604]
  AUTHORS   Duane W, Hastings JW.
  TITLE     Flavin mononucleotide reductase of luminous bacteria.
  JOURNAL   Mol. Cell. Biochem. 6 (1975) 53-64.
  ORGANISM  Photobacterium fischeri
REFERENCE   2  [PMID:3207]
  AUTHORS   Fisher J, Spencer R, Walsh C.
  TITLE     Enzyme-catalyzed redox reactions with the flavin analogues
            5-deazariboflavin, 5-deazariboflavin 5'-phosphte, and
            5-deazariboflavin 5'-diphosphate, 5' leads to 5'-adenosine ester.
  JOURNAL   Biochemistry. 15 (1976) 1054-64.
  ORGANISM  Vibrio harveyi
REFERENCE   3  [PMID:222213]
  AUTHORS   Tu SC, Becvar JE, Hastings JW.
  TITLE     Kinetic studies on the mechanism of bacterial NAD(P)H:flavin
            oxidoreductase.
  JOURNAL   Arch. Biochem. Biophys. 193 (1979) 110-6.
  ORGANISM  Photobacterium fischeri
REFERENCE   4  [PMID:8990272]
  AUTHORS   Liu M, Lei B, Ding Q, Lee JC, Tu SC.
  TITLE     Vibrio harveyi NADPH:FMN oxidoreductase: preparation and
            characterization of the apoenzyme and monomer-dimer equilibrium.
  JOURNAL   Arch. Biochem. Biophys. 337 (1997) 89-95.
  ORGANISM  Vibrio harveyi
REFERENCE   5  [PMID:9772191]
  AUTHORS   Lei B, Tu SC.
  TITLE     Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN
            oxidoreductase to luciferase.
  JOURNAL   Biochemistry. 37 (1998) 14623-9.
  ORGANISM  Vibrio harveyi
REFERENCE   6  [PMID:11469801]
  AUTHORS   Tang CK, Jeffers CE, Nichols JC, Tu SC.
  TITLE     Flavin specificity and subunit interaction of Vibrio fischeri
            general NAD(P)H-flavin oxidoreductase FRG/FRase I.
  JOURNAL   Arch. Biochem. Biophys. 392 (2001) 110-6.
  ORGANISM  Vibrio fischeri [GN:vfi]
REFERENCE   7  [PMID:10353815]
  AUTHORS   Ingelman M, Ramaswamy S, Niviere V, Fontecave M, Eklund H.
  TITLE     Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia
            coli.
  JOURNAL   Biochemistry. 38 (1999) 7040-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   8  [PMID:10480865]
  AUTHORS   Eichhorn E, van der Ploeg JR, Leisinger T.
  TITLE     Characterization of a two-component alkanesulfonate monooxygenase
            from Escherichia coli.
  JOURNAL   J. Biol. Chem. 274 (1999) 26639-46.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K00299  FMN reductase
            KO: K03180  NAD(P)H-flavin reductase
GENES       ECO: b0937(ssuE) b3844(fre)
            ECJ: JW0920(ssuE) JW3820(fre)
            ECE: Z1285(ycbP) Z5365(ubiB)
            ECS: ECs1020 ECs4772
            ECC: c1080(ycbP) c4791(ubiB)
            ECI: UTI89_C1009(ycbP) UTI89_C4429(fre)
            ECP: ECP_0949 ECP_4057
            ECV: APECO1_2613(fre) APECO1_49(ssuE)
            ECW: EcE24377A_4363(fre)
            ECX: EcHS_A4066(fre)
            STY: STY3580(ubiB)
            STT: t3318(ubiB)
            SPT: SPA3820(ubiB)
            SEC: SC3877(fre)
            STM: STM3979(ubiB)
            YPE: YPO3623(ssuE) YPO3768(fadI)
            YPK: y0246 y0462(ubiB)
            YPM: YP_3280(fadI) YP_3924(ssuE)
            YPA: YPA_3438 YPA_3636
            YPN: YPN_3547
            YPP: YPDSF_0230
            YPS: YPTB0265(fadI) YPTB3606(ssuE)
            SFL: SF0936(ycbP) SF3920(ubiB)
            SFX: S1001(ycbP) S3832(ubiB)
            SFV: SFV_0941(ycbP) SFV_3656(ubiB)
            SSN: SSON_0940(ycbP) SSON_4017(ubiB)
            SBO: SBO_2228(ycbP) SBO_3856(ubiB)
            SDY: SDY_2319(ycbP) SDY_3901(ubiB)
            ECA: ECA0206(fre)
            PLU: plu4404(fre)
            SGL: SG0117
            ENT: Ent638_1456
            SPE: Spro_1739
            XCC: XCC0316(sflA)
            XCB: XC_0328
            XCV: XCV0343
            XAC: XAC0334(sflA) XAC0851(slfA)
            XOO: XOO4335(sflA)
            XOM: XOO_4086(XOO4086)
            VCH: VC0312
            VVU: VV1_0933
            VVY: VV3177
            VPA: VP2995
            VFI: VF0062 VFA0918
            PPR: PBPRA3536(luxG)
            PAE: PA2357(msuE) PA3446
            PAU: PA14_19530(ssuE) PA14_34180(msuE)
            PPU: PP_0236(ssuE) PP_2764(msuE)
            PPF: Pput_0251 Pput_2990
            PST: PSPTO_3451(ssuE)
            PSB: Psyr_3233
            PFL: PFL_4155(msuE) PFL_5938(ssuE)
            PFO: Pfl_3915 Pfl_5415
            PEN: PSEEN0217(ssuE)
            PMY: Pmen_4324
            ACI: ACIAD3470(msuE)
            SON: SO_0504(fre)
            SDN: Sden_3058
            SFR: Sfri_3390
            SHE: Shewmr4_0505
            SHM: Shewmr7_3526
            SHN: Shewana3_0505
            ILO: IL2359(ubiB)
            CPS: CPS_0178
            PHA: PSHAa0104(fre)
            AHA: AHA_0102
            DNO: DNO_0091
            BCI: BCI_0060(ubiB)
            RSO: RSc1337(RS02859)
            REU: Reut_A2705
            RME: Rmet_4788 Rmet_5075
            BMA: BMAA0563
            BXE: Bxe_B1014
            BUR: Bcep18194_C7714
            BCN: Bcen_3190 Bcen_5790
            BCH: Bcen2424_5177 Bcen2424_6155
            BAM: Bamb_6034
            BPS: BPSS1427
            BPM: BURPS1710b_A0451
            BTE: BTH_II0965
            BPA: BPP0636
            BBR: BB0642
            RFR: Rfer_1780
            PNA: Pnap_0558
            MPT: Mpe_A2148
            MMS: mma_0738(ssuE)
            MFA: Mfla_1569
            MLO: mlr5227
            MES: Meso_1830
            SME: SMb20573
            ATU: Atu5527
            ATC: AGR_pAT_786
            RET: RHE_PC00012
            RLE: RL2888(arsH) pRL100232 pRL90304
            BRA: BRADO0161 BRADO3417 BRADO5570 BRADO5909
            BBT: BBta_0194 BBta_1869 BBta_4290 BBta_6091
            GBE: GbCGDNIH1_0381
            BHA: BH3321(ssuE)
            BCL: ABC0597 ABC3399
            BPU: BPUM_1955(yqiG) BPUM_3131
            OIH: OB0356 OB3079 OB3146
            SAU: SA0328
            SAV: SAV0340
            SAM: MW0316
            SAS: SAS0316
            SAC: SACOL0410
            SAB: SAB0289 SAB0511
            SAA: SAUSA300_0340 SAUSA300_0545
            SAO: SAOUHSC_00320
            SSP: SSP0226
            LMO: lmo2351
            LMF: LMOf2365_2321
            LIN: lin2445
            LSL: LSL_1504
            MHY: mhp322(baiH)
            MSM: MSMEG_2800
            MMC: Mmcs_3780 Mmcs_4899
            CGL: NCgl1582(cgl1644)
            CGB: cg1850
            CEF: CE1759
            CDI: DIP1437
            NFA: nfa23490
            RHA: RHA1_ro01755
            SCO: SCO3295(SCE15.12c)
            SMA: SAV1207 SAV4764
            LXX: Lxx03550(msuE) Lxx23200
            TFU: Tfu_1931
            FRA: Francci3_3454
            FAL: FRAAL0777 FRAAL5630(ssuE)
            SEN: SACE_0288 SACE_3968
            RXY: Rxyl_1783
            CYA: CYA_0352 CYA_1496
            CYB: CYB_1452 CYB_2096
            GVI: gll2765
            ANA: alr4777
            AVA: Ava_1214 Ava_2443
            TER: Tery_3252
            HMA: rrnAC0982(ssuE1) rrnAC2773(ssuE2)
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.29
            ExPASy - ENZYME nomenclature database: 1.5.1.29
            ExplorEnz - The Enzyme Database: 1.5.1.29
            ERGO genome analysis and discovery system: 1.5.1.29
            BRENDA, the Enzyme Database: 1.5.1.29
            CAS: 64295-83-6
///
ENTRY       EC 1.5.1.30                 Enzyme
NAME        flavin reductase;
            NADPH:flavin oxidoreductase;
            riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide
            phosphate) reductase;
            flavin mononucleotide reductase;
            flavine mononucleotide reductase;
            FMN reductase (NADPH);
            NADPH-dependent FMN reductase;
            NADPH-flavin reductase;
            NADPH-FMN reductase;
            NADPH-specific FMN reductase;
            riboflavin mononucleotide reductase;
            riboflavine mononucleotide reductase;
            NADPH2 dehydrogenase (flavin);
            NADPH2:riboflavin oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     reduced-riboflavin:NADP+ oxidoreductase
REACTION    reduced riboflavin + NADP+ = riboflavin + NADPH + H+ [RN:R05707]
ALL_REAC    R05707
SUBSTRATE   reduced riboflavin [CPD:C01007];
            NADP+ [CPD:C00006]
PRODUCT     riboflavin [CPD:C00255];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The enzyme from Entamoeba histolytica reduces riboflavin and
            galactoflavin, and, more slowly, FMN and FAD. NADH is oxidized more
            slowly than NADPH.
REFERENCE   1  [PMID:6258069]
  AUTHORS   Lo H, Reeves RE.
  TITLE     Purification and properties of NADPH:flavin oxidoreductase from
            Entamoeba histolytica.
  JOURNAL   Mol. Biochem. Parasitol. 2 (1980) 23-30.
  ORGANISM  Entamoeba histolytica [GN:ehi]
REFERENCE   2  [PMID:3453680]
  AUTHORS   Yubisui T, Tamura M, Takeshita M.
  TITLE     Characterization of a second form of NADPH-flavin reductase purified
            from human erythrocytes.
  JOURNAL   Biochem. Int. 15 (1987) 1-8.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K05901  flavin reductase
GENES       HSA: 645(BLVRB)
            MMU: 233016(Blvrb)
            BTA: 281650(BLVRB)
            LPN: lpg2932(ubiB)
            LPF: lpl2861
            LPP: lpp3000
            CVI: CV_3784(ubiB)
            REH: H16_A2352 H16_B0671
            BXE: Bxe_B2749
            BRA: BRADO0997
            BPU: BPUM_0624 BPUM_1731 BPUM_2112(yqjM) BPUM_3458
            RHA: RHA1_ro08916 RHA1_ro08996
            SEN: SACE_4772
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.30
            ExPASy - ENZYME nomenclature database: 1.5.1.30
            ExplorEnz - The Enzyme Database: 1.5.1.30
            ERGO genome analysis and discovery system: 1.5.1.30
            BRENDA, the Enzyme Database: 1.5.1.30
            CAS: 56626-29-0
///
ENTRY       EC 1.5.1.31                 Enzyme
NAME        berberine reductase;
            (R)-canadine synthase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (R)-tetrahydroberberine:NADP+ oxidoreductase
REACTION    (R)-canadine + 2 NADP+ = berberine + 2 NADPH + H+ [RN:R07169]
ALL_REAC    R07169
SUBSTRATE   (R)-canadine [CPD:C11818];
            NADP+ [CPD:C00006]
PRODUCT     berberine [CPD:C00757];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Involved in alkaloid biosynthesis in Corydalis cava to give
            (R)-canadine with the opposite configuration to the precursor of
            berberine (see EC 1.3.3.8 tetrahydroberberine oxidase). Also acts on
            7,8-dihydroberberine.
REFERENCE   1
  AUTHORS   Bauer, W. and Zenk, M.H.
  TITLE     Formation of (R)-configurated tetrahydroprotoberberine alkaloids in
            vivo and in vitro.
  JOURNAL   Tetrahedron Lett. 32 (1991) 487-490.
  ORGANISM  Corydalis cava
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.31
            ExPASy - ENZYME nomenclature database: 1.5.1.31
            ExplorEnz - The Enzyme Database: 1.5.1.31
            ERGO genome analysis and discovery system: 1.5.1.31
            BRENDA, the Enzyme Database: 1.5.1.31
///
ENTRY       EC 1.5.1.32                 Enzyme
NAME        vomilenine reductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     1,2-dihydrovomilenine:NADP+ oxidoreductase
REACTION    1,2-dihydrovomilenine + NADP+ = vomilenine + NADPH + H+ [RN:R05878]
ALL_REAC    R05878
SUBSTRATE   1,2-dihydrovomilenine [CPD:C11808];
            NADP+ [CPD:C00006]
PRODUCT     vomilenine [CPD:C01761];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Forms part of the ajmaline biosynthesis pathway.
REFERENCE   1  [PMID:11937349]
  AUTHORS   von Schumann G, Gao S, Stockigt J.
  TITLE     Vomilenine reductase--a novel enzyme catalyzing a crucial step in
            the biosynthesis of the therapeutically applied antiarrhythmic
            alkaloid ajmaline.
  JOURNAL   Bioorg. Med. Chem. 10 (2002) 1913-8.
  ORGANISM  Rauvolfia serpentina
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.32
            ExPASy - ENZYME nomenclature database: 1.5.1.32
            ExplorEnz - The Enzyme Database: 1.5.1.32
            ERGO genome analysis and discovery system: 1.5.1.32
            BRENDA, the Enzyme Database: 1.5.1.32
            CAS: 462127-03-3
///
ENTRY       EC 1.5.1.33                 Enzyme
NAME        pteridine reductase;
            PTR1;
            pteridine reductase 1
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     5,6,7,8-tetrahydrobiopterin:NADP+ oxidoreductase
REACTION    5,6,7,8-tetrahydrobiopterin + 2 NADP+ = biopterin + 2 NADPH + 2 H+
            [RN:R01812]
ALL_REAC    R01812
SUBSTRATE   5,6,7,8-tetrahydrobiopterin [CPD:C00272];
            NADP+ [CPD:C00006]
PRODUCT     biopterin [CPD:C06313];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The enzyme from Leishmania (both amastigote and promastigote forms)
            catalyses the reduction by NADPH of folate and a wide variety of
            unconjugated pterins, including biopterin, to their tetrahydro
            forms. It also catalyses the reduction of 7,8-dihydropterins and
            7,8-dihydrofolate to their tetrahydro forms. In contrast to EC
            1.5.1.3 (dihydrofolate reductase) and EC 1.5.1.34
            (6,7-dihydropteridine reductase), pteridine reductase will not
            catalyse the reduction of the quinonoid form of dihydrobiopterin.
            The enzyme is specific for NADPH; no activity has been detected with
            NADH. It also differs from EC 1.5.1.3 (dihydrofolate reductase) in
            being specific for the B side of NADPH.
REFERENCE   1  [PMID:9153248]
  AUTHORS   Nare B, Hardy LW, Beverley SM.
  TITLE     The roles of pteridine reductase 1 and dihydrofolate
            reductase-thymidylate synthase in pteridine metabolism in the
            protozoan parasite Leishmania major.
  JOURNAL   J. Biol. Chem. 272 (1997) 13883-91.
  ORGANISM  Leishmania major [GN:lma]
REFERENCE   2  [PMID:11373620]
  AUTHORS   Gourley DG, Schuttelkopf AW, Leonard GA, Luba J, Hardy LW, Beverley
            SM, Hunter WN.
  TITLE     Pteridine reductase mechanism correlates pterin metabolism with drug
            resistance in trypanosomatid parasites.
  JOURNAL   Nat. Struct. Biol. 8 (2001) 521-5.
  ORGANISM  Leishmania major [GN:lma]
REFERENCE   3  [PMID:10800597]
  AUTHORS   Fitzpatrick PF.
  TITLE     The aromatic amino acid hydroxylases.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 74 (2000) 235-94.
ORTHOLOGY   KO: K03793  pteridine reductase
GENES       TBR: Tb927.8.2210
            LMA: LmjF23.0270
            XFA: XF1457
            XFT: PD0677(ptr1)
            XCC: XCC3431(ptr1)
            XCB: XC_0733
            XCV: XCV0748
            XAC: XAC0688(ptr1)
            XOO: XOO3932(ptr1)
            XOM: XOO_3709(XOO3709)
            MCA: MCA2986
            CVI: CV_4132
            NEU: NE1165
            NMU: Nmul_A0336
            EBA: ebA3368
            TBD: Tbd_2701
            MFA: Mfla_0229
STRUCTURES  PDB: 1W0C  2BF7  2BFA  2BFM  2BFO  2BFP  2C7V  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.33
            ExPASy - ENZYME nomenclature database: 1.5.1.33
            ExplorEnz - The Enzyme Database: 1.5.1.33
            ERGO genome analysis and discovery system: 1.5.1.33
            BRENDA, the Enzyme Database: 1.5.1.33
            CAS: 131384-61-7
///
ENTRY       EC 1.5.1.34                 Enzyme
NAME        6,7-dihydropteridine reductase;
            6,7-dihydropteridine:NAD(P)H oxidoreductase;
            DHPR;
            NAD(P)H:6,7-dihydropteridine oxidoreductase;
            NADH-dihydropteridine reductase;
            NADPH-dihydropteridine reductase;
            NADPH-specific dihydropteridine reductase;
            dihydropteridine (reduced nicotinamide adenine dinucleotide)
            reductase;
            dihydropteridine reductase;
            dihydropteridine reductase (NADH);
            5,6,7,8-tetrahydropteridine:NAD(P)H+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     5,6,7,8-tetrahydropteridine:NAD(P)+ oxidoreductase
REACTION    a 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine +
            NAD(P)H + H+ [RN:R07354 R07355]
ALL_REAC    R07354 > R01793;
            R07355 > R01794
SUBSTRATE   5,6,7,8-tetrahydropteridine [CPD:C05650];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     6,7-dihydropteridine [CPD:C05649];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The substrate is the quinonoid form of dihydropteridine. Not
            identical with EC 1.5.1.3 dihydrofolate reductase.
REFERENCE   1
  AUTHORS   Harano, T.
  TITLE     New diaphorases from Bombyx silkworm eggs. NADH/NADPH cytochrome c
            reductase activity mediated with 6,7-dimethyltetrahydropterin.
  JOURNAL   Insect Biochem. 2 (1972) 385-399.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:191436]
  AUTHORS   Hasegawa H.
  TITLE     Dihydropteridine reductase from bovine liver. Purification,
            crystallization, and isolation of a binary complex with NADH.
  JOURNAL   J. Biochem. (Tokyo). 81 (1977) 169-77.
  ORGANISM  cow [GN:bta]
REFERENCE   3
  AUTHORS   Kaufman, S.
  TITLE     Phenylalanine hydroxylase.
  JOURNAL   Methods Enzymol. 5 (1962) 809-816.
REFERENCE   4  [PMID:4402916]
  AUTHORS   Lind KE.
  TITLE     Dihydropteridine reductase. Investigation of the specificity for
            quinoid dihydropteridine and the inhibition by
            2,4-diaminopteridines.
  JOURNAL   Eur. J. Biochem. 25 (1972) 560-2.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:16875]
  AUTHORS   Nakanishi N, Hasegawa H, Watabe S.
  TITLE     A new enzyme, NADPH-dihydropteridine reductase in bovine liver.
  JOURNAL   J. Biochem. (Tokyo). 81 (1977) 681-5.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K00357  dihydropteridine reductase
GENES       HSA: 5860(QDPR)
            MMU: 110391(Qdpr)
            RNO: 64192(Qdpr)
            CFA: 479082(QDPR)
            SSC: 397619(QDPR)
            GGA: 426335(QDPR)
            XTR: 496990(qdpr)
            SPU: 575893(LOC575893)
            DME: Dmel_CG4665(Dhpr)
            CEL: T03F6.1(qdpr-1)
            CAL: CaO19.3707(yhb1) CaO19_7637(CaO19.7637)
            DDI: DDBDRAFT_0168923
            TET: TTHERM_00220710
            TCR: 510689.20
            LMA: LmjF34.4330
            ECO: b0578(nfnB)
            ECJ: JW0567(nfnB)
            ECE: Z0717(nfnB)
            ECS: ECs0616
            ECC: c0664(nfnB)
            ECI: UTI89_C0578(nfnB)
            ECV: APECO1_1470(nfnB)
            ECW: EcE24377A_0596(nfnB)
            ECX: EcHS_A0625
            STY: STY0620(nfnB)
            STT: t2290(nfnB)
            SPT: SPA2156(nfnB)
            SEC: SC0609(nfnB)
            STM: STM0578(nfnB)
            SFX: S0493(nfnB)
            SFV: SFV_0518(nfnB)
            SSN: SSON_0529(nfnB)
            SBO: SBO_0439(nfnB)
            SDY: SDY_0491(nfnB)
            VCH: VCA0637
            VCO: VC0395_1093(hmpA)
            VVU: VV2_0966
            VVY: VVA1455
            VPA: VPA1591
            VFI: VF2316 VFA0691
            PPU: PP_2432
            PPF: Pput_3263
            PEN: PSEEN1322 PSEEN2307(nfsB)
            PMY: Pmen_2015
            ACI: ACIAD1923(nfnB) ACIAD3226
            SON: SO_3715
            SDN: Sden_2794
            SBM: Shew185_0943
            SSE: Ssed_3785
            SHN: Shewana3_0876
            CPS: CPS_4747
            PHA: PSHAa1234
            FTU: FTT0304c(nfnB)
            FTF: FTF0304c(nfnB)
            FTL: FTL_0215
            FTH: FTH_0210(nfnB)
            FTA: FTA_0231
            TCX: Tcr_1024
            CVI: CV_2244(nfnB)
            RME: Rmet_3717
            BUR: Bcep18194_A3823 Bcep18194_B2438 Bcep18194_C6878
            HAR: HEAR0672
            MMS: mma_0615(hmp)
            DAR: Daro_1868
            DDE: Dde_0086
            DPS: DP0728
            SAT: SYN_01293
            GOX: GOX0473 GOX0861
            GBE: GbCGDNIH1_1674
            CPR: CPR_0756
            MVA: Mvan_1541
            MGI: Mflv_4884
            CGB: cg3141(hmp)
            SCO: SCO7094(hmpA2)
            FAL: FRAAL5017(hmpA)
            FNU: FN1223 FN1254 FN1880
            TTH: TTC1718
STRUCTURES  PDB: 1YKI  1YLR  1YLU  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.34
            ExPASy - ENZYME nomenclature database: 1.5.1.34
            ExplorEnz - The Enzyme Database: 1.5.1.34
            ERGO genome analysis and discovery system: 1.5.1.34
            BRENDA, the Enzyme Database: 1.5.1.34
            CAS: 9074-11-7
///
ENTRY       EC 1.5.1.35       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: 1-pyrroline dehydrogenase. The enzyme is identical to
            EC 1.2.1.19, aminobutyraldehyde dehydrogenase, as the substrates
            1-pyrroline and 4-aminobutanal are interconvertible. (EC 1.5.1.35
            created 2006, deleted 2007)
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.1.35
            ExPASy - ENZYME nomenclature database: 1.5.1.35
            ExplorEnz - The Enzyme Database: 1.5.1.35
            ERGO genome analysis and discovery system: 1.5.1.35
            BRENDA, the Enzyme Database: 1.5.1.35
///
ENTRY       EC 1.5.1.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With NAD+ or NADP+ as acceptor
REACTION    (1) 2-Oxoadipate + NH3 + NAD+ <=> 2-Aminomuconate + NADH + H+ + H2O
            [RN:R01937];
            (2) 2-Oxoadipate + NH3 + NADP+ <=> 2-Aminomuconate + NADPH + H+ +
            H2O [RN:R01938]
SUBSTRATE   2-Oxoadipate [CPD:C00322];
            NH3 [CPD:C00014];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     2-Aminomuconate [CPD:C02220];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            H2O [CPD:C00001];
            NADPH [CPD:C00005]
///
ENTRY       EC 1.5.3.1                  Enzyme
NAME        sarcosine oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With oxygen as acceptor
SYSNAME     sarcosine:oxygen oxidoreductase (demethylating)
REACTION    sarcosine + H2O + O2 = glycine + formaldehyde + H2O2 [RN:R00610]
ALL_REAC    R00610
SUBSTRATE   sarcosine [CPD:C00213];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     glycine [CPD:C00037];
            formaldehyde [CPD:C00067];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). The flavin is both covalently and
            non-covalently bound in a molar ratio of 1:1.
REFERENCE   1  [PMID:6158947]
  AUTHORS   Hayashi S, Nakamura S, Suzuki M.
  TITLE     Corynebacterium sarcosine oxidase: a unique enzyme having
            covalently-bound and noncovalently-bound flavins.
  JOURNAL   Biochem. Biophys. Res. Commun. 96 (1980) 924-30.
  ORGANISM  Corynebacterium sp.
REFERENCE   2
  AUTHORS   Mori, N., Sano, M., Tani, Y. and Yamada, H.
  TITLE     Purification and propertie of sarcosine oxidase from Cylindrocarpon
            didymum M-1.
  JOURNAL   Agric. Biol. Chem. 44 (1980) 1391-1397.
  ORGANISM  Cylindrocarpon didymum
REFERENCE   3  [PMID:7240129]
  AUTHORS   Suzuki M.
  TITLE     Purification and some properties of sarcosine oxidase from
            Corynebacterium sp. U-96.
  JOURNAL   J. Biochem. (Tokyo). 89 (1981) 599-607.
  ORGANISM  Corynebacterium sp.
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K00301  sarcosine oxidase
            KO: K00302  sarcosine oxidase, subunit alpha
            KO: K00303  sarcosine oxidase, subunit beta
            KO: K00304  sarcosine oxidase, subunit delta
            KO: K00305  sarcosine oxidase, subunit gamma
GENES       HSA: 51268(PIPOX)
            MMU: 19193(Pipox)
            CFA: 491177(PIPOX)
            CEL: C15B12.1
            ATH: AT2G24580
            OSA: 4347470
            AFM: AFUA_2G16610 AFUA_3G01180
            AOR: AO090038000193
            CNE: CNC05930
            DDI: DDBDRAFT_0215209
            TET: TTHERM_00242470 TTHERM_00414420
            EHI: 173.t00005 328.t00012 360.t00007
            ECO: b1059(solA)
            ECJ: JW1046(solA)
            ECE: Z1696(solA)
            ECS: ECs1437
            ECC: c1326(solA)
            ECI: UTI89_C1184(solA)
            ECV: APECO1_141(solA)
            STY: STY1198(solA)
            STT: t1760(solA)
            SPT: SPA1691(solA)
            SEC: SC1108(solA)
            STM: STM1160(solA)
            YPE: YPO2448(solA)
            YPK: y1742(solA)
            YPM: YP_2268(solA)
            YPA: YPA_1945
            YPN: YPN_2045
            YPP: YPDSF_1863
            YPS: YPTB2485(solA)
            SFL: SF1066(solA)
            SFX: S1143(solA)
            SFV: SFV_1082(solA)
            SSN: SSON_1079(solA)
            SBO: SBO_2005(solA)
            SDY: SDY_2096(solA)
            ENT: Ent638_1573
            SPE: Spro_1892
            XCC: XCC2413(soxA)
            XCB: XC_1699
            XCV: XCV2746
            XOO: XOO3139(soxA)
            XOM: XOO_2981(XOO2981)
            PAE: PA5416(soxB) PA5417(soxD) PA5418(soxA) PA5419(soxG)
            PAU: PA14_71470(soxB) PA14_71490(soxD) PA14_71500(soxA)
                 PA14_71510(soxG)
            PPU: PP_0323(soxB) PP_0324(soxD) PP_0325(soxA) PP_0326(soxG)
                 PP_3775
            PST: PSPTO_0457(soxG-1) PSPTO_0458(soxA-1) PSPTO_0459(soxD-1)
                 PSPTO_0460(soxB-1) PSPTO_2449(soxG-2) PSPTO_2450(soxA-2)
                 PSPTO_2451(soxD-2) PSPTO_2452(soxB-2) PSPTO_2519
            PSB: Psyr_2221 Psyr_2222 Psyr_2223 Psyr_2224 Psyr_2330 Psyr_4713
                 Psyr_4714 Psyr_4715 Psyr_4716
            PSP: PSPPH_2838 PSPPH_2962 PSPPH_2963 PSPPH_2964 PSPPH_2965
                 PSPPH_3071 PSPPH_4751(soxB) PSPPH_4752(soxD) PSPPH_4753(soxA)
                 PSPPH_4754(soxG)
            PFL: PFL_2285 PFL_2333 PFL_5725(soxG) PFL_5726(soxA)
                 PFL_5727(soxD) PFL_5728(soxB)
            PFO: Pfl_2285 Pfl_5204 Pfl_5205 Pfl_5206 Pfl_5207
            PEN: PSEEN5158(soxG) PSEEN5159(soxA) PSEEN5160(soxD)
                 PSEEN5161(soxB)
            ACI: ACIAD2549 ACIAD2550(soxA) ACIAD2551(soxD) ACIAD2552(soxB)
            CPS: CPS_2478(soxB1) CPS_2479(soxD1) CPS_2480(soxA1)
                 CPS_2481(soxG1) CPS_4032(soxB2) CPS_4033(soxD2)
                 CPS_4034(soxA2) CPS_4035(soxG2)
            TCX: Tcr_1350 Tcr_1351
            CSA: Csal_0998 Csal_0999 Csal_1000 Csal_1001
            RSO: RSc1101(soxB2) RSc1102(soxD2) RSc1103(soxA2) RSc1104(soxG2)
                 RSp0046(soxB1) RSp0047(soxD1) RSp0048(soxA1) RSp0049(soxG1)
            REU: Reut_B4827 Reut_B4829 Reut_B4830
            BXE: Bxe_B0194 Bxe_B0746 Bxe_B1597 Bxe_B1598 Bxe_B1599 Bxe_B1600
                 Bxe_B2709
            BUR: Bcep18194_A6395 Bcep18194_A6498 Bcep18194_B0486
                 Bcep18194_B0489 Bcep18194_B1161 Bcep18194_B2677
                 Bcep18194_C6672 Bcep18194_C6842
            BCN: Bcen_3216 Bcen_3217 Bcen_3219
            BCH: Bcen2424_5148 Bcen2424_5150 Bcen2424_5151
            BPS: BPSS1366(soxG) BPSS1367(soxA) BPSS1368(soxD) BPSS1369(soxB)
            BPM: BURPS1710b_A0392(soxG) BURPS1710b_A0393(soxA)
                 BURPS1710b_A0394(soxD) BURPS1710b_A0395
            BPL: BURPS1106A_A1859(soxG) BURPS1106A_A1860(soxA)
                 BURPS1106A_A1861(soxD)
            BPD: BURPS668_A1953 BURPS668_A1954
            BTE: BTH_II0996 BTH_II0997 BTH_II0998 BTH_II0999
            BPE: BP2515(soxG) BP2516(soxA) BP2517(soxD) BP2518(soxB)
            BPA: BPP3502(soxG) BPP3503(soxA) BPP3504(soxD) BPP3505(soxB)
            RFR: Rfer_0884
            POL: Bpro_3942
            AZO: azo0209(agaE) azo3004(soxB)
            MFA: Mfla_0452 Mfla_0453
            PUB: SAR11_1064(soxB) SAR11_1065(soxD) SAR11_1066(soxA)
                 SAR11_1067(soxG) SAR11_1281(soxG2) SAR11_1282(soxA2)
                 SAR11_1283(soxD2) SAR11_1284(soxB2)
            MLO: mll3107 mll3108 mll3111 mll5230 mll5232 mll6237 mll6238
                 mll6240 mll7022 mll7303 mll7304 mll7306 mlr1273 mlr1275
                 mlr1276 mlr8469 msl3109 msl5231 msl6239 msl7305 msr1274
            MES: Meso_0591 Meso_0592 Meso_0593 Meso_0594
            SME: SMc01856 SMc02605(soxG) SMc02606(soxA1) SMc02607(soxD)
                 SMc02608(soxB) SMc03930(soxG2) SMc03931(soxA2) SMc03932(soxD2)
                 SMc03933(soxB2)
            ATU: Atu2110(solA) Atu2111(solA) Atu4066(soxB) Atu4068(soxD)
                 Atu4069(soxA) Atu4070(soxG) Atu4221 Atu4222(soxA)
                 Atu4223(soxD) Atu4224(soxB) Atu4310(soxB) Atu4311(soxD)
                 Atu4312(soxA) Atu4313(soxG)
            ATC: AGR_C_3826 AGR_C_3830 AGR_L_1101 AGR_L_1103 AGR_L_1105
                 AGR_L_1106 AGR_L_1275 AGR_L_1275gl AGR_L_1276 AGR_L_1279
                 AGR_L_1572 AGR_L_1574 AGR_L_1575 AGR_L_1577
            RET: RHE_CH02857 RHE_CH02858 RHE_CH03600(soxGch)
                 RHE_CH03601(soxAch) RHE_CH03602(soxDch) RHE_CH03603(soxBch)
                 RHE_CH04054 RHE_PE00424(soxBe) RHE_PE00426(soxAe) RHE_PF00356
            RLE: RL1363 RL3317 RL3318 RL4122(soxG) RL4123(soxA) RL4124(soxD)
                 RL4126(soxB) RL4586 pRL110560(soxB) pRL110561(soxD)
                 pRL110562(soxA) pRL110563(soxG) pRL120605 pRL120621
            BME: BMEI1719 BMEI1720 BMEI1721 BMEI1722 BMEII0391 BMEII0582
            BMF: BAB1_0230 BAB1_0231(soxD) BAB1_0235(soxG) BAB2_0330 BAB2_0537
            BMS: BR0229(soxB) BR0230(soxD) BR0231(soxA) BR0232(soxG)
            BMB: BruAb1_0225(soxD) BruAb1_0227(soxG)
            BOV: BOV_0220 BOV_0222(soxB) BOV_0223(soxD) BOV_0224
            BJA: bll7190(soxB)
            BRA: BRADO1552 BRADO2168 BRADO5878(soxB) BRADO5879(soxD)
                 BRADO5880(soxA) BRADO5881(soxG)
            BBT: BBta_1830 BBta_1832 BBta_1917 BBta_1927 BBta_1946(soxG)
                 BBta_1947(soxA) BBta_1948(soxD) BBta_1949(soxB) BBta_2484
                 BBta_6497
            RPB: RPB_1141 RPB_1142 RPB_1143 RPB_1144
            SIL: SPO1585 SPO1586 SPO1587 SPO1588 SPO1744 SPO1745 SPO1746
                 SPO1747 SPO2344 SPO2345 SPO2346 SPO2348
            SIT: TM1040_0970 TM1040_0972 TM1040_2144 TM1040_2145 TM1040_2146
                 TM1040_2147 TM1040_3375 TM1040_3376 TM1040_3377 TM1040_3378
            RSP: RSP_0638 RSP_2686 RSP_2688(soxD) RSP_2689(soxA) RSP_2690
            JAN: Jann_2183 Jann_2185 Jann_2186 Jann_2187 Jann_3445 Jann_3446
                 Jann_3447 Jann_3448
            RDE: RD1_0009(soxG) RD1_0010(soxA) RD1_0011(soxD) RD1_0012(soxB)
                 RD1_1701(soxB) RD1_1702(soxD) RD1_1704(soxA) RD1_1705(soxG)
                 RD1_1788(soxB) RD1_1789(soxD) RD1_1790(soxA) RD1_1791(soxG)
                 RD1_2063
            GBE: GbCGDNIH1_0079 GbCGDNIH1_0080 GbCGDNIH1_0081 GbCGDNIH1_0082
                 GbCGDNIH1_0173 GbCGDNIH1_0174 GbCGDNIH1_0175 GbCGDNIH1_0177
            RRU: Rru_A2070 Rru_A2648 Rru_A2874
            SUS: Acid_5898
            BAN: BA2835
            BAR: GBAA2835
            BAA: BA_3356 BA_3360
            BAT: BAS2644 BAS2647 BAS2648
            BCE: BC2836 BC2839 BC2840
            BCA: BCE_2864 BCE_3187
            BCZ: BCZK2560(soxB) BCZK2563(soxA) BCZK2564(soxA)
            BTK: BT9727_2595(soxB) BT9727_2598(soxA) BT9727_2599(soxA)
            BTL: BALH_2547
            BAY: RBAM_011680(goxB)
            OIH: OB2802
            CTC: CTC02435
            MGI: Mflv_3081
            MMC: Mmcs_2460
            MKM: Mkms_2505
            MJL: Mjls_2497
            CGL: NCgl1519(cgl1581)
            CGB: cg1783(soxA')
            CEF: CE1699
            RHA: RHA1_ro01821(soxB) RHA1_ro01822(soxD) RHA1_ro01823(soxA1)
                 RHA1_ro01824(soxG) RHA1_ro03302(soxA2)
            ART: Arth_0077
            AAU: AAur_1202(soxA) AAur_3826(soxB) AAur_3827 AAur_3828
                 AAur_3829(soxG)
            FAL: FRAAL1891 FRAAL4450
            SEN: SACE_2963(soxA2) SACE_4491(soxG) SACE_4492(soxA)
                 SACE_4493(soxD) SACE_4494(soxB) SACE_5611(soxG)
                 SACE_5612(soxA) SACE_5613(soxD) SACE_5614(soxB)
            RXY: Rxyl_0471 Rxyl_0768 Rxyl_1558 Rxyl_2495 Rxyl_2926
            FNU: FN0182
            SYW: SYNW0230(solA)
            SYD: Syncc9605_0224
            SYE: Syncc9902_0252
            SYG: sync_0269
            SYR: SynRCC307_2294(solA)
            SYX: SynWH7803_0274(solA)
            PMC: P9515_04101(solA)
            PMH: P9215_04081(solA)
            CHU: CHU_3234(thiO)
            RRS: RoseRS_2528
            RCA: Rcas_3393
            AFU: AF0273(soxA) AF0274(soxB)
            HAL: VNG0281G(soxB)
            HMA: pNG7366(gcvT3) pNG7370(gcvT1) rrnAC1865(soxB)
            PHO: PH1363 PH1364 PH1749 PH1751
            PAB: PAB0212(soxA) PAB0214(soxB) PAB1842 PAB1843(soxB)
            PFU: PF1245 PF1246 PF1795 PF1798
            TKO: TK0116 TK0117 TK0119 TK0122
            SSO: SSO0186(soxA-like) SSO0187(soxB-like)
            STO: ST0220 ST0221
STRUCTURES  PDB: 1EL5  1EL7  1EL8  1EL9  1ELI  1L9C  1L9D  1L9E  1VRQ  1X31  
                 1ZOV  2A89  2GB0  2GF3  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.3.1
            ExPASy - ENZYME nomenclature database: 1.5.3.1
            ExplorEnz - The Enzyme Database: 1.5.3.1
            ERGO genome analysis and discovery system: 1.5.3.1
            BRENDA, the Enzyme Database: 1.5.3.1
            CAS: 9029-22-5
///
ENTRY       EC 1.5.3.2                  Enzyme
NAME        N-methyl-L-amino-acid oxidase;
            N-methylamino acid oxidase;
            demethylase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With oxygen as acceptor
SYSNAME     N-methyl-L-amino-acid:oxygen oxidoreductase (demethylating)
REACTION    an N-methyl-L-amino acid + H2O + O2 = an L-amino acid + formaldehyde
            + H2O2 [RN:R01264]
ALL_REAC    R01264
SUBSTRATE   N-methyl-L-amino acid [CPD:C03148];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     L-amino acid [CPD:C00151];
            formaldehyde [CPD:C00067];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016];
            Flavoprotein [CPD:C06411]
COMMENT     A flavoprotein.
REFERENCE   1
  AUTHORS   Moritani, M.
  TITLE     Demethylase. IV. Kinetics and reaction mechanism.
  JOURNAL   Hukuoka Acta Med. 43 (1952) 651-658.
  ORGANISM  rabbit
REFERENCE   2
  AUTHORS   Moritani, M.
  TITLE     Demethylase. V. Specificity and its relation to amino acid oxidase.
  JOURNAL   Hukuoka Acta Med. 43 (1952) 731-735.
  ORGANISM  rabbit
REFERENCE   3  [PMID:13192101]
  AUTHORS   MORITANI M, TUNG TC, FUJII S, MITO H, IZUMIYA N, KENMOCHI K,
            HIROHATA R.
  TITLE     Specificity of rabbit kidney demethylase.
  JOURNAL   J. Biol. Chem. 209 (1954) 485-92.
  ORGANISM  rabbit
GENES       ECW: EcE24377A_1182(solA)
            ECX: EcHS_A1182(solA)
            YPI: YpsIP31758_1564(solA)
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.3.2
            ExPASy - ENZYME nomenclature database: 1.5.3.2
            ExplorEnz - The Enzyme Database: 1.5.3.2
            ERGO genome analysis and discovery system: 1.5.3.2
            BRENDA, the Enzyme Database: 1.5.3.2
            CAS: 9029-23-6
///
ENTRY       EC 1.5.3.3        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With oxygen as acceptor
COMMENT     Deleted entry: spermine oxidase (EC 1.5.3.3 created 1961, deleted
            1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.3.3
            ExPASy - ENZYME nomenclature database: 1.5.3.3
            ExplorEnz - The Enzyme Database: 1.5.3.3
            ERGO genome analysis and discovery system: 1.5.3.3
            BRENDA, the Enzyme Database: 1.5.3.3
///
ENTRY       EC 1.5.3.4                  Enzyme
NAME        N6-methyl-lysine oxidase;
            epsilon-alkyl-L-lysine:oxygen oxidoreductase ;
            N6-methyllysine oxidase;
            epsilon-N-methyllysine demethylase;
            epsilon-alkyllysinase;
            6-N-methyl-L-lysine:oxygen oxidoreductase (demethylating)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With oxygen as acceptor
SYSNAME     N6-methyl-L-lysine:oxygen oxidoreductase (demethylating)
REACTION    N6-methyl-L-lysine + H2O + O2 = L-lysine + formaldehyde + H2O2
            [RN:R00612]
ALL_REAC    R00612
SUBSTRATE   N6-methyl-L-lysine [CPD:C02728];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     L-lysine [CPD:C00047];
            formaldehyde [CPD:C00067];
            H2O2 [CPD:C00027]
REFERENCE   1
  AUTHORS   Kim, S., Benoiton, L. and Paik, W.K.
  TITLE     alpha-Alkyllysinase. Purification and properties of the enzyme.
  JOURNAL   J. Biol. Chem. 239 (1964) 3790-3796.
  ORGANISM  rat [GN:rno]
GENES       FAL: FRAAL6442(hesA2)
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.3.4
            ExPASy - ENZYME nomenclature database: 1.5.3.4
            ExplorEnz - The Enzyme Database: 1.5.3.4
            ERGO genome analysis and discovery system: 1.5.3.4
            BRENDA, the Enzyme Database: 1.5.3.4
            CAS: 37256-28-3
///
ENTRY       EC 1.5.3.5                  Enzyme
NAME        (S)-6-hydroxynicotine oxidase;
            L-6-hydroxynicotine oxidase;
            6-hydroxy-L-nicotine oxidase;
            6-hydroxy-L-nicotine:oxygen oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With oxygen as acceptor
SYSNAME     (S)-6-hydroxynicotine:oxygen oxidoreductase
REACTION    (S)-6-hydroxynicotine + H2O + O2 =
            1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
            [RN:R03202]
ALL_REAC    R03202
SUBSTRATE   (S)-6-hydroxynicotine [CPD:C01056];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one [CPD:C01297];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:5646150]
  AUTHORS   Dai VD, Decker K, Sund H.
  TITLE     Purification and properties of L-6-hydroxynicotine oxidase.
  JOURNAL   Eur. J. Biochem. 4 (1968) 95-102.
  ORGANISM  Arthrobacter oxidans
REFERENCE   2  [PMID:5849820]
  AUTHORS   Decker K, Bleeg H.
  TITLE     Induction and purification of stereospecific nicotine oxidizing
            enzymes from Arthrobacter oxidans.
  JOURNAL   Biochim. Biophys. Acta. 105 (1965) 313-24.
  ORGANISM  Arthrobacter oxidans
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.3.5
            ExPASy - ENZYME nomenclature database: 1.5.3.5
            ExplorEnz - The Enzyme Database: 1.5.3.5
            ERGO genome analysis and discovery system: 1.5.3.5
            UM-BBD (Biocatalysis/Biodegradation Database): 1.5.3.5
            BRENDA, the Enzyme Database: 1.5.3.5
            CAS: 37256-29-4
///
ENTRY       EC 1.5.3.6                  Enzyme
NAME        (R)-6-hydroxynicotine oxidase;
            D-6-hydroxynicotine oxidase;
            6-hydroxy-D-nicotine oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With oxygen as acceptor
SYSNAME     (R)-6-hydroxynicotine:oxygen oxidoreductase
REACTION    (R)-6-hydroxynicotine + H2O + O2 =
            1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
            [RN:R07170]
ALL_REAC    R07170
SUBSTRATE   (R)-6-hydroxynicotine [CPD:C03043];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one [CPD:C01297];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:4628374]
  AUTHORS   Bruhmuller M, Mohler H, Decker K.
  TITLE     Covalently bound flavin in D-6-hydroxynicotine oxidase from
            Arthrobacter oxidans. Purification and properties of
            D-6-hydroxynicotine oxidase.
  JOURNAL   Eur. J. Biochem. 29 (1972) 143-51.
  ORGANISM  Arthrobacter oxidans
REFERENCE   2  [PMID:5849820]
  AUTHORS   Decker K, Bleeg H.
  TITLE     Induction and purification of stereospecific nicotine oxidizing
            enzymes from Arthrobacter oxidans.
  JOURNAL   Biochim. Biophys. Acta. 105 (1965) 313-24.
  ORGANISM  Arthrobacter oxidans
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
GENES       REH: H16_B1606
STRUCTURES  PDB: 2BVF  2BVG  2BVH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.3.6
            ExPASy - ENZYME nomenclature database: 1.5.3.6
            ExplorEnz - The Enzyme Database: 1.5.3.6
            ERGO genome analysis and discovery system: 1.5.3.6
            UM-BBD (Biocatalysis/Biodegradation Database): 1.5.3.6
            BRENDA, the Enzyme Database: 1.5.3.6
            CAS: 37233-46-8
///
ENTRY       EC 1.5.3.7                  Enzyme
NAME        L-pipecolate oxidase;
            pipecolate oxidase;
            L-pipecolic acid oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With oxygen as acceptor
SYSNAME     L-pipecolate:oxygen 1,6-oxidoreductase
REACTION    L-pipecolate + O2 = 2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
            [RN:R02204]
ALL_REAC    R02204
SUBSTRATE   L-pipecolate [CPD:C00408];
            O2 [CPD:C00007]
PRODUCT     2,3,4,5-tetrahydropyridine-2-carboxylate [CPD:C00450];
            H2O2 [CPD:C00027]
COMMENT     The product reacts with water to form 2-aminoadipate 6-semialdehyde,
            i.e. 2-amino-6-oxohexanoate.
REFERENCE   1  [PMID:6051341]
  AUTHORS   Baginsky ML, Rodwell VW.
  TITLE     Metabolism of pipecolic acid in a Pseudomonas species. V. Pipecolate
            oxidase and dehydrogenase.
  JOURNAL   J. Bacteriol. 94 (1967) 1034-9.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:6809728]
  AUTHORS   Kinzel JJ, Bhattacharjee JK.
  TITLE     Lysine biosynthesis in Rhodotorula glutinis: properties of pipecolic
            acid oxidase.
  JOURNAL   J. Bacteriol. 151 (1982) 1073-7.
  ORGANISM  Rhodotorula glutinis
PATHWAY     PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K00306  L-pipecolate oxidase
GENES       HSA: 51268(PIPOX)
            MMU: 19193(Pipox)
            CFA: 491177(PIPOX)
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.3.7
            ExPASy - ENZYME nomenclature database: 1.5.3.7
            ExplorEnz - The Enzyme Database: 1.5.3.7
            ERGO genome analysis and discovery system: 1.5.3.7
            BRENDA, the Enzyme Database: 1.5.3.7
            CAS: 81669-65-0
///
ENTRY       EC 1.5.3.8        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With oxygen as acceptor
COMMENT     Deleted entry: now included with EC 1.3.3.8 tetrahydroberberine
            oxidase (EC 1.5.3.8 created 1989, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.3.8
            ExPASy - ENZYME nomenclature database: 1.5.3.8
            ExplorEnz - The Enzyme Database: 1.5.3.8
            ERGO genome analysis and discovery system: 1.5.3.8
            BRENDA, the Enzyme Database: 1.5.3.8
///
ENTRY       EC 1.5.3.9        Obsolete  Enzyme
NAME        Transferred to 1.21.3.3
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now EC 1.21.3.3 reticuline oxidase (EC 1.5.3.9
            created 1989, modified 1999, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.3.9
            ExPASy - ENZYME nomenclature database: 1.5.3.9
            ExplorEnz - The Enzyme Database: 1.5.3.9
            ERGO genome analysis and discovery system: 1.5.3.9
            BRENDA, the Enzyme Database: 1.5.3.9
///
ENTRY       EC 1.5.3.10                 Enzyme
NAME        dimethylglycine oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With oxygen as acceptor
SYSNAME     N,N-dimethylglycine:oxygen oxidoreductase (demethylating)
REACTION    N,N-dimethylglycine + H2O + O2 = sarcosine + formaldehyde + H2O2
            [RN:R01564]
ALL_REAC    R01564
SUBSTRATE   N,N-dimethylglycine [CPD:C01026];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     sarcosine [CPD:C00213];
            formaldehyde [CPD:C00067];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Does not oxidize sarcosine.
REFERENCE   1
  AUTHORS   Mori, N., Kawakami, B., Tani, Y. and Yamada, H.
  TITLE     Purification and properties of dimethylglycine oxidase from
            Cylindrocarpon didymum M-1.
  JOURNAL   Agric. Biol. Chem. 44 (1980) 1383-1389.
  ORGANISM  Cylindrocarpon didymum
STRUCTURES  PDB: 1PJ5  1PJ6  1PJ7  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.3.10
            ExPASy - ENZYME nomenclature database: 1.5.3.10
            ExplorEnz - The Enzyme Database: 1.5.3.10
            ERGO genome analysis and discovery system: 1.5.3.10
            BRENDA, the Enzyme Database: 1.5.3.10
            CAS: 74870-79-4
///
ENTRY       EC 1.5.3.11                 Enzyme
NAME        polyamine oxidase;
            1-N-acetylspermidine:oxygen oxidoreductase (deaminating)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With oxygen as acceptor
SYSNAME     N1-acetylspermidine:oxygen oxidoreductase (deaminating)
REACTION    N1-acetylspermine + O2 + H2O = N1-acetylspermidine + 3-aminopropanal
            + H2O2 [RN:R03899]
ALL_REAC    R03899
SUBSTRATE   N1-acetylspermine [CPD:C02567];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     N1-acetylspermidine [CPD:C00612];
            3-aminopropanal [CPD:C02229];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023]
COMMENT     A flavoprotein requiring Fe2+. Also acts on N1-acetylspermidine and
            N1,N12-diacetylspermine.
REFERENCE   1  [PMID:7215618]
  AUTHORS   Bolkenius FN, Seiler N.
  TITLE     Acetylderivatives as intermediates in polyamine catabolism.
  JOURNAL   Int. J. Biochem. 13 (1981) 287-92.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6621391]
  AUTHORS   Holtta E.
  TITLE     Polyamine oxidase (rat liver).
  JOURNAL   Methods. Enzymol. 94 (1983) 306-11.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K00308  polyamine oxidase
GENES       HSA: 196743(PAOX)
            MMU: 212503(Paox)
            ATH: AT5G13700(APAO/ATPAO1)
            OSA: 4346882
            PIC: PICST_28515(CPB2)
            ANI: AN6658.2
            AFM: AFUA_5G09720 AFUA_6G03510
            AOR: AO090010000340
            TET: TTHERM_00621520 TTHERM_00621530
STRUCTURES  PDB: 1B37  1H81  1H82  1H83  1H84  1H86  1RSG  1YY5  1Z6L  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.3.11
            ExPASy - ENZYME nomenclature database: 1.5.3.11
            ExplorEnz - The Enzyme Database: 1.5.3.11
            ERGO genome analysis and discovery system: 1.5.3.11
            BRENDA, the Enzyme Database: 1.5.3.11
            CAS: 294646-71-2
///
ENTRY       EC 1.5.3.12                 Enzyme
NAME        dihydrobenzophenanthridine oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With oxygen as acceptor
SYSNAME     dihydrobenzophenanthridine:oxygen oxidoreductase
REACTION    (1) dihydrosanguinarine + O2 = sanguinarine + H2O2 [RN:R04703];
            (2) dihydrochelirubine + O2 = chelirubine + H2O2 [RN:R04706];
            (3) dihydromacarpine + O2 = macarpine + H2O2 [RN:R04768]
ALL_REAC    R04703 R04706 R04768
SUBSTRATE   dihydrosanguinarine [CPD:C05191];
            O2 [CPD:C00007];
            dihydrochelirubine [CPD:C05194];
            dihydromacarpine [CPD:C05316]
PRODUCT     sanguinarine [CPD:C06162];
            H2O2 [CPD:C00027];
            chelirubine [CPD:C06327];
            macarpine [CPD:C06165]
COFACTOR    Copper [CPD:C00070]
COMMENT     A CuII enzyme found in higher plants that produces oxidized forms of
            the benzophenanthridine alkaloids
REFERENCE   1
  AUTHORS   Schumacher, H.-M. and Zenk, M.H.
  TITLE     Partial purification and characterization of
            dihydrobenzophenanthridine oxidase from Eschscholtzia tenuifolia
            cell suspension cultures.
  JOURNAL   Plant Cell Reports 7 (1988) 43-46.
  ORGANISM  Eschscholzia tenuifolia
REFERENCE   2  [PMID:1444440]
  AUTHORS   Arakawa H, Clark WG, Psenak M, Coscia CJ.
  TITLE     Purification and characterization of dihydrobenzophenanthridine
            oxidase from elicited Sanguinaria canadensis cell cultures.
  JOURNAL   Arch. Biochem. Biophys. 299 (1992) 1-7.
  ORGANISM  Sanguinaria canadensis
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.3.12
            ExPASy - ENZYME nomenclature database: 1.5.3.12
            ExplorEnz - The Enzyme Database: 1.5.3.12
            ERGO genome analysis and discovery system: 1.5.3.12
            BRENDA, the Enzyme Database: 1.5.3.12
            CAS: 114051-83-1
///
ENTRY       EC 1.5.4.1                  Enzyme
NAME        pyrimidodiazepine synthase;
            PDA synthase;
            pyrimidodiazepine:oxidized-glutathione oxidoreductase (ring-opening,
            cyclizing)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With a disulfide as acceptor
SYSNAME     pyrimidodiazepine:glutathione-disulfide oxidoreductase
            (ring-opening, cyclizing)
REACTION    a pyrimidodiazepine + glutathione disulfide + H2O =
            6-pyruvoyltetrahydropterin + 2 glutathione [RN:R03984]
ALL_REAC    R03984
SUBSTRATE   pyrimidodiazepine [CPD:C02587];
            glutathione disulfide [CPD:C00127];
            H2O [CPD:C00001]
PRODUCT     6-pyruvoyltetrahydropterin [CPD:C03684];
            glutathione [CPD:C00051]
COMMENT     In the reverse direction of reaction, the reduction of
            6-pyruvoyl-tetrahydropterin is accompanied by the opening of the
            6-membered pyrazine ring and the formation of the 7-membered
            diazepine ring. The pyrimidodiazepine involved is an acetyldihydro
            derivative. Involved in the formation of the eye pigment drosopterin
            in Drosophila melanogaster.
REFERENCE   1  [PMID:6438092]
  AUTHORS   Wiederrecht GJ, Brown GM.
  TITLE     Purification and properties of the enzymes from Drosophila
            melanogaster that catalyze the conversion of dihydroneopterin
            triphosphate to the pyrimidodiazepine precursor of the drosopterins.
  JOURNAL   J. Biol. Chem. 259 (1984) 14121-7.
  ORGANISM  Drosophila melanogaster [GN:dme]
PATHWAY     PATH: map00480  Glutathione metabolism
ORTHOLOGY   KO: K00310  pyrimidodiazepine synthase
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.4.1
            ExPASy - ENZYME nomenclature database: 1.5.4.1
            ExplorEnz - The Enzyme Database: 1.5.4.1
            ERGO genome analysis and discovery system: 1.5.4.1
            BRENDA, the Enzyme Database: 1.5.4.1
            CAS: 93586-06-2
///
ENTRY       EC 1.5.5.1                  Enzyme
NAME        electron-transferring-flavoprotein dehydrogenase;
            ETF-QO;
            ETF:ubiquinone oxidoreductase;
            electron transfer flavoprotein dehydrogenase;
            electron transfer flavoprotein Q oxidoreductase;
            electron transfer flavoprotein-ubiquinone oxidoreductase;
            electron transfer flavoprotein reductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With a quinone or similar compound as acceptor
SYSNAME     electron-transferring-flavoprotein:ubiquinone oxidoreductase
REACTION    reduced electron-transferring flavoprotein + ubiquinone =
            electron-transferring flavoprotein + ubiquinol [RN:R04433]
ALL_REAC    R04433
SUBSTRATE   reduced electron-transferring flavoprotein [CPD:C04570];
            ubiquinone [CPD:C00399]
PRODUCT     electron-transferring flavoprotein [CPD:C04253];
            ubiquinol [CPD:C00390]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023];
            Sulfur [CPD:C00087];
            Iron-sulfur [CPD:C00824]
COMMENT     An iron-sulfur flavoprotein, forming part of the mitochondrial
            electron-transfer system.
REFERENCE   1  [PMID:4052375]
  AUTHORS   Beckmann JD, Frerman FE.
  TITLE     Electron-transfer flavoprotein-ubiquinone oxidoreductase from pig
            liver: purification and molecular, redox, and catalytic properties.
  JOURNAL   Biochemistry. 24 (1985) 3913-21.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:925004]
  AUTHORS   Ruzicka FJ, Beinert H.
  TITLE     A new iron-sulfur flavoprotein of the respiratory chain. A component
            of the fatty acid beta oxidation pathway.
  JOURNAL   J. Biol. Chem. 252 (1977) 8440-5.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K00311  electron-transferring-flavoprotein dehydrogenase
GENES       HSA: 2110(ETFDH)
            PTR: 461573(ETFDH)
            MMU: 66841(Etfdh)
            RNO: 295143(Etfdh)
            CFA: 475480(ETFDH)
            GGA: 428724(RCJMB04_20k15)
            XLA: 447730(MGC81928)
            XTR: 448088(etfdh)
            SPU: 587199(LOC587199)
            DME: Dmel_CG12140
            CEL: C05D11.12(YAAS)
            ATH: AT2G43400(ETFQO)
            OSA: 4349116
            CME: CMT089C
            SCE: YOR356W
            AGO: AGOS_ADR387W
            PIC: PICST_49344(ETF4)
            CGR: CAGL0G06402g
            SPO: SPAC20G8.04c
            ANI: AN4977.2
            AFM: AFUA_3G10110
            AOR: AO090003000545
            CNE: CNA04420
            DDI: DDBDRAFT_0206234
            TET: TTHERM_00444850
            TBR: Tb927.8.1240
            TCR: 506401.220 508543.140
            LMA: LmjF07.0600
            SEC: SC0852(etfD)
            STM: STM0858
            XFA: XF1298
            XFT: PD0549(etfD)
            XCC: XCC0630(etf-QO)
            XCB: XC_3604
            XCV: XCV3700
            XAC: XAC3575(etf-QO)
            XOO: XOO0801(etf-QO)
            XOM: XOO_0729(XOO0729)
            VVU: VV2_0476
            VVY: VVA1026
            VPA: VPA0643 VPA1155
            PPR: PBPRB1099
            PAE: PA2953
            PAU: PA14_25840
            PPU: PP_4203
            PPF: Pput_1650
            PSB: Psyr_1994
            PSP: PSPPH_1963
            PFL: PFL_1818
            PFO: Pfl_4118
            PEN: PSEEN3660
            PMY: Pmen_2708
            PAR: Psyc_1956
            PCR: Pcryo_2251
            PRW: PsycPRwf_0282
            ACI: ACIAD1680(etfD) ACIAD3259(etfD)
            SON: SO_4453
            SDN: Sden_0100
            SFR: Sfri_0081
            SAZ: Sama_3523
            SBL: Sbal_0283
            SBM: Shew185_0276
            SLO: Shew_0086
            SPC: Sputcn32_0388
            SSE: Ssed_4403
            SPL: Spea_2172 Spea_4121
            SHE: Shewmr4_0272
            SHM: Shewmr7_3749
            SHN: Shewana3_0273
            SHW: Sputw3181_0242
            ILO: IL0881
            CPS: CPS_3686
            PHA: PSHAa1619(etfdH)
            PAT: Patl_2147
            SDE: Sde_1999
            MAQ: Maqu_1472
            CBU: CBU_1120
            CBD: COXBU7E912_1221
            LPN: lpg1276
            LPF: lpl1239
            LPP: lpp1239
            HHA: Hhal_1492
            HCH: HCH_03954
            CSA: Csal_1612
            ABO: ABO_1100(etf)
            MMW: Mmwyl1_2259
            AHA: AHA_1975
            NME: NMB0581
            NGO: NGO1396
            CVI: CV_3916
            RSO: RSc1567(etf)
            REU: Reut_A1262
            REH: H16_A1324(fixC)
            RME: Rmet_1146
            BMA: BMA1116
            BXE: Bxe_A1362 Bxe_B0378 Bxe_B2714
            BVI: Bcep1808_1426 Bcep1808_4577 Bcep1808_5643
            BUR: Bcep18194_A4606 Bcep18194_C6873
            BCN: Bcen_0979 Bcen_1554
            BCH: Bcen2424_1461 Bcen2424_6275
            BAM: Bamb_1346 Bamb_5772
            BPS: BPSL1961
            BPM: BURPS1710b_1869
            BPL: BURPS1106A_1715
            BTE: BTH_I2613
            PNU: Pnuc_0824
            BPE: BP2403
            BPA: BPP3268
            BBR: BB3719
            RFR: Rfer_2269 Rfer_3018 Rfer_4163
            POL: Bpro_1895 Bpro_5295
            PNA: Pnap_2315 Pnap_2679 Pnap_3283
            AAV: Aave_3139
            AJS: Ajs_1950
            VEI: Veis_3981
            MPT: Mpe_A1443
            HAR: HEAR1810
            MMS: mma_1478(etf)
            EBA: ebA6155
            AZO: azo2151(etf1) azo3008(etf2)
            DAR: Daro_0228 Daro_1936
            MFA: Mfla_0725
            BBA: Bd0945(etf-QO)
            AFW: Anae109_2898
            PUB: SAR11_1250
            MLO: mlr7709
            MES: Meso_0911
            PLA: Plav_0719
            SME: SMc02377(etf)
            SMD: Smed_0649
            ATU: Atu0994
            ATC: AGR_C_1825
            RET: RHE_CH01308(etf)
            RLE: RL1457
            BME: BMEI1320
            BMF: BAB1_0645
            BMS: BR0621
            BMB: BruAb1_0640
            OAN: Oant_2658
            BJA: blr2524
            BRA: BRADO2020 BRADO5384(fixC)
            BBT: BBta_2346 BBta_5870(fixC)
            RPA: RPA1037
            RPB: RPB_1084
            RPC: RPC_4358
            RPD: RPD_1211
            RPE: RPE_4421
            NWI: Nwi_2595
            NHA: Nham_3218
            BHE: BH12310
            BQU: BQ09690
            BBK: BARBAKC583_1039
            XAU: Xaut_0140 Xaut_2374
            CCR: CC_1334
            SIL: SPO0316
            SIT: TM1040_3745
            RSP: RSP_1777
            RSH: Rsph17029_0424
            RSQ: Rsph17025_2473
            JAN: Jann_0484
            RDE: RD1_3404
            PDE: Pden_0425
            MMR: Mmar10_2188
            HNE: HNE_1909
            ZMO: ZMO1184(yjcC)
            NAR: Saro_1781
            SAL: Sala_1185
            SWI: Swit_4100
            ELI: ELI_06930
            GOX: GOX0868
            GBE: GbCGDNIH1_0540
            ACR: Acry_1057
            RRU: Rru_A0265 Rru_A1317
            MAG: amb4437
            MGM: Mmc1_3687
            ABA: Acid345_3065
            CYA: CYA_1694
            CYB: CYB_1991
            GVI: gll3362
            CCH: Cag_1800
            PVI: Cvib_0385
            PLT: Plut_0319
            RRS: RoseRS_0958
            RCA: Rcas_3598
            HWA: HQ1520A HQ1534A HQ2910A(fixC) HQ3113A
            NPH: NP3024A NP4168A NP4564A
STRUCTURES  PDB: 2GMH  2GMJ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.5.1
            ExPASy - ENZYME nomenclature database: 1.5.5.1
            ExplorEnz - The Enzyme Database: 1.5.5.1
            ERGO genome analysis and discovery system: 1.5.5.1
            BRENDA, the Enzyme Database: 1.5.5.1
            CAS: 86551-03-3
///
ENTRY       EC 1.5.7.1                  Enzyme
NAME        methylenetetrahydrofolate reductase (ferredoxin);
            5,10-methylenetetrahydrofolate reductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With an iron-sulfur protein as acceptor
SYSNAME     5-methyltetrahydrofolate:ferredoxin oxidoreductase
REACTION    5-methyltetrahydrofolate + 2 oxidized ferredoxin =
            5,10-methylenetetrahydrofolate + 2 reduced ferredoxin + 2 H+
            [RN:R01217]
ALL_REAC    R01217
SUBSTRATE   5-methyltetrahydrofolate [CPD:C00440];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     5,10-methylenetetrahydrofolate [CPD:C00143];
            reduced ferredoxin [CPD:C00138];
            H+ [CPD:C00080]
COMMENT     An iron-sulfur flavoprotein that also contains zinc. The enzyme from
            Clostridium formicoaceticum catalyses the reduction of methylene
            blue, menadione, benzyl viologen, rubredoxin or FAD with
            5-methyltetrahydrofolate and the oxidation of reduced ferredoxin or
            FADH2 with 5,10-methylenetetrahydrofolate. However, unlike EC
            1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H], there is no
            activity with NAD(P)H.
REFERENCE   1  [PMID:6381490]
  AUTHORS   Clark JE, Ljungdahl LG.
  TITLE     Purification and properties of 5,10-methylenetetrahydrofolate
            reductase, an iron-sulfur flavoprotein from Clostridium
            formicoaceticum.
  JOURNAL   J. Biol. Chem. 259 (1984) 10845-9.
  ORGANISM  Clostridium formicoaceticum
PATHWAY     PATH: map00670  One carbon pool by folate
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.7.1
            ExPASy - ENZYME nomenclature database: 1.5.7.1
            ExplorEnz - The Enzyme Database: 1.5.7.1
            ERGO genome analysis and discovery system: 1.5.7.1
            BRENDA, the Enzyme Database: 1.5.7.1
///
ENTRY       EC 1.5.8.1                  Enzyme
NAME        dimethylamine dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With a flavin as acceptor
SYSNAME     dimethylamine:electron-transferring flavoprotein oxidoreductase
REACTION    dimethylamine + H2O + electron-transferring flavoprotein =
            methylamine + formaldehyde + reduced electron-transferring
            flavoprotein [RN:R01588]
ALL_REAC    R01588
SUBSTRATE   dimethylamine [CPD:C00543];
            H2O [CPD:C00001];
            electron-transferring flavoprotein [CPD:C04253]
PRODUCT     methylamine [CPD:C00218];
            formaldehyde [CPD:C00067];
            reduced electron-transferring flavoprotein [CPD:C04570]
COFACTOR    FMN [CPD:C00061]
COMMENT     Contains FAD and a [4Fe-4S] cluster.
REFERENCE   1  [PMID:7556160]
  AUTHORS   Yang CC, Packman LC, Scrutton NS.
  TITLE     The primary structure of Hyphomicrobium X dimethylamine
            dehydrogenase. Relationship to trimethylamine dehydrogenase and
            implications for substrate recognition.
  JOURNAL   Eur. J. Biochem. 232 (1995) 264-71.
  ORGANISM  Hyphomicrobium sp.
PATHWAY     PATH: map00680  Methane metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.8.1
            ExPASy - ENZYME nomenclature database: 1.5.8.1
            ExplorEnz - The Enzyme Database: 1.5.8.1
            ERGO genome analysis and discovery system: 1.5.8.1
            UM-BBD (Biocatalysis/Biodegradation Database): 1.5.8.1
            BRENDA, the Enzyme Database: 1.5.8.1
///
ENTRY       EC 1.5.8.2                  Enzyme
NAME        trimethylamine dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With a flavin as acceptor
SYSNAME     trimethylamine:electron-transferring flavoprotein oxidoreductase
            (demethylating)
REACTION    trimethylamine + H2O + electron-transferring flavoprotein =
            dimethylamine + formaldehyde + reduced electron-transferring
            flavoprotein [RN:R02511]
ALL_REAC    R02511
SUBSTRATE   trimethylamine [CPD:C00565];
            H2O [CPD:C00001];
            electron-transferring flavoprotein [CPD:C04253]
PRODUCT     dimethylamine [CPD:C00543];
            formaldehyde [CPD:C00067];
            reduced electron-transferring flavoprotein [CPD:C04570]
COMMENT     A number of alkyl-substituted derivatives of trimethylamine can also
            act as electron donors; phenazine methosulfate and
            2,6-dichloroindophenol can act as electron acceptors. Contains FAD
            and a [4Fe-4S] cluster.
REFERENCE   1
  AUTHORS   Colby, J. and Zatman, L.J.
  TITLE     The purification and properties of a bacterial trimethylamine
            dehydrogenase.
  JOURNAL   Biochem. J. 121 (1971) 9.
REFERENCE   2  [PMID:204297]
  AUTHORS   Steenkamp DJ, Singer TP.
  TITLE     Participation of the iron-sulphur cluster and of the covalently
            bound coenzyme of trimethylamine dehydrogenase in catalysis.
  JOURNAL   Biochem. J. 169 (1978) 361-9.
  ORGANISM  methylotrophic bacterium
REFERENCE   3  [PMID:7592591]
  AUTHORS   Huang L, Rohlfs RJ, Hille R.
  TITLE     The reaction of trimethylamine dehydrogenase with electron
            transferring flavoprotein.
  JOURNAL   J. Biol. Chem. 270 (1995) 23958-65.
  ORGANISM  Methylophilus methylotrophus
REFERENCE   4  [PMID:11756429]
  AUTHORS   Jones M, Talfournier F, Bobrov A, Grossmann JG, Vekshin N, Sutcliffe
            MJ, Scrutton NS.
  TITLE     Electron transfer and conformational change in complexes of
            trimethylamine dehydrogenase and electron transferring flavoprotein.
  JOURNAL   J. Biol. Chem. 277 (2002) 8457-65.
  ORGANISM  Methylophilus methylotrophus
REFERENCE   5  [PMID:11192721]
  AUTHORS   Scrutton NS, Sutcliffe MJ.
  TITLE     Trimethylamine dehydrogenase and electron transferring flavoprotein.
  JOURNAL   Subcell. Biochem. 35 (2000) 145-81.
PATHWAY     PATH: map00680  Methane metabolism
ORTHOLOGY   KO: K00317  trimethylamine dehydrogenase
GENES       CAL: CaO19.125
            MSU: MS2010(nemA)
            BUR: Bcep18194_C7137
            RDE: RD1_4141(tmd) RD1_4142(tmd)
            SAU: SA0311
            SAV: SAV0322
            SAM: MW0299
            SAR: SAR0319
            SAS: SAS0299
            SAC: SACOL0392
            SAB: SAB0272c
            SAA: SAUSA300_0322
            SAO: SAOUHSC_00302
            SHA: SH0268
            SPY: SPy_1219
            SPZ: M5005_Spy_0933
            SPM: spyM18_1171
            SPG: SpyM3_0859
            SPS: SPs1059
            SPJ: MGAS2096_Spy0992
            SPA: M6_Spy0922(yqiG)
            SPB: M28_Spy0905(yqiG)
            SAG: SAG1061
            SAN: gbs1095
            SAK: SAK_1150
            MPU: MYPU_7720(baiH)
            MMY: MSC_0526
            MCP: MCAP_0450
            AVA: Ava_4435
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.8.2
            ExPASy - ENZYME nomenclature database: 1.5.8.2
            ExplorEnz - The Enzyme Database: 1.5.8.2
            ERGO genome analysis and discovery system: 1.5.8.2
            UM-BBD (Biocatalysis/Biodegradation Database): 1.5.8.2
            BRENDA, the Enzyme Database: 1.5.8.2
            CAS: 39307-09-0
///
ENTRY       EC 1.5.99.1                 Enzyme
NAME        sarcosine dehydrogenase;
            sarcosine N-demethylase;
            monomethylglycine dehydrogenase;
            sarcosine:(acceptor) oxidoreductase (demethylating)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With other acceptors
SYSNAME     sarcosine:acceptor oxidoreductase (demethylating)
REACTION    sarcosine + acceptor + H2O = glycine + formaldehyde + reduced
            acceptor [RN:R00611]
ALL_REAC    R00611
SUBSTRATE   sarcosine [CPD:C00213];
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
PRODUCT     glycine [CPD:C00037];
            formaldehyde [CPD:C00067];
            reduced acceptor [CPD:C00030]
COFACTOR    FMN [CPD:C00061]
COMMENT     A flavoprotein (FMN).
REFERENCE   1  [PMID:13895406]
  AUTHORS   FRISELL WR, MACKENZIE CG.
  TITLE     Separation and purification of sarcosine dehydrogenase and
            dimethylglycine dehydrogenase.
  JOURNAL   J. Biol. Chem. 237 (1962) 94-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:13716069]
  AUTHORS   HOSKINS DD, MACKENZIE CG.
  TITLE     Solubilization and electron transfer flavoprtein requirement of
            mitochondrial sarcosine dehydrogenase and dimethylglycine
            dehydrogenase.
  JOURNAL   J. Biol. Chem. 236 (1961) 177-83.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K00314  sarcosine dehydrogenase
GENES       HSA: 1757(SARDH)
            PTR: 464828(SARDH)
            MMU: 192166(Sardh)
            RNO: 114123(Sardh)
            CFA: 491277(SARDH)
            GGA: 417146(SARDH)
            DME: Dmel_CG6385
            AFM: AFUA_4G01150
            PUB: SAR11_1221
            MLO: mll5369 mlr1213 mlr1283
            SME: SMc01662
            RET: RHE_CH00088 RHE_PE00084
            RLE: RL0097 pRL110236
            BME: BMEI0684
            SIL: SPO3396
            SIT: TM1040_0434
            RDE: RD1_4112
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.99.1
            ExPASy - ENZYME nomenclature database: 1.5.99.1
            ExplorEnz - The Enzyme Database: 1.5.99.1
            ERGO genome analysis and discovery system: 1.5.99.1
            BRENDA, the Enzyme Database: 1.5.99.1
            CAS: 37228-65-2
///
ENTRY       EC 1.5.99.2                 Enzyme
NAME        dimethylglycine dehydrogenase;
            N,N-dimethylglycine oxidase;
            N,N-dimethylglycine:(acceptor) oxidoreductase (demethylating)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With other acceptors
SYSNAME     N,N-dimethylglycine:acceptor oxidoreductase (demethylating)
REACTION    N,N-dimethylglycine + acceptor + H2O = sarcosine + formaldehyde +
            reduced acceptor [RN:R01565]
ALL_REAC    R01565
SUBSTRATE   N,N-dimethylglycine [CPD:C01026];
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
PRODUCT     sarcosine [CPD:C00213];
            formaldehyde [CPD:C00067];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein.
REFERENCE   1  [PMID:13895406]
  AUTHORS   FRISELL WR, MACKENZIE CG.
  TITLE     Separation and purification of sarcosine dehydrogenase and
            dimethylglycine dehydrogenase.
  JOURNAL   J. Biol. Chem. 237 (1962) 94-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:13716069]
  AUTHORS   HOSKINS DD, MACKENZIE CG.
  TITLE     Solubilization and electron transfer flavoprtein requirement of
            mitochondrial sarcosine dehydrogenase and dimethylglycine
            dehydrogenase.
  JOURNAL   J. Biol. Chem. 236 (1961) 177-83.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K00315  dimethylglycine dehydrogenase
GENES       HSA: 29958(DMGDH)
            PTR: 471505(DMGDH)
            MMU: 74129(Dmgdh)
            RNO: 245961(Dmgdh)
            CFA: 488935(DMGDH)
            XLA: 446949(LOC446949)
            SPU: 587447(LOC587447)
            REH: H16_B1955(gcvT3)
            PUB: SAR11_1253
            MLO: mll1517 mll1653 mll2449 mlr1280
            SME: SMa1483 SMc01663
            ATU: Atu1632
            ATC: AGR_C_3012
            SIL: SPO0207 SPO0544 SPO0564 SPO3400 SPOA0063
            SIT: TM1040_0486 TM1040_1426 TM1040_2063
            RSP: RSP_3566
            JAN: Jann_0919 Jann_1481 Jann_1596
            RDE: RD1_0017 RD1_0019 RD1_0607 RD1_1345 RD1_3093 RD1_3434
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.99.2
            ExPASy - ENZYME nomenclature database: 1.5.99.2
            ExplorEnz - The Enzyme Database: 1.5.99.2
            ERGO genome analysis and discovery system: 1.5.99.2
            BRENDA, the Enzyme Database: 1.5.99.2
            CAS: 37256-30-7
///
ENTRY       EC 1.5.99.3                 Enzyme
NAME        L-pipecolate dehydrogenase;
            L-pipecolate:(acceptor) 1,6-oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With other acceptors
SYSNAME     L-pipecolate:acceptor 1,6-oxidoreductase
REACTION    L-pipecolate + acceptor = 2,3,4,5-tetrahydropyridine-2-carboxylate +
            reduced acceptor [RN:R02206]
ALL_REAC    R02206 > R02205
SUBSTRATE   L-pipecolate [CPD:C00408];
            acceptor [CPD:C00028]
PRODUCT     2,3,4,5-tetrahydropyridine-2-carboxylate [CPD:C00450];
            reduced acceptor [CPD:C00030]
COMMENT     The product reacts with water to form 2-aminoadipate 6-semialdehyde,
            i.e. 2-amino-6-oxohexanoate.
REFERENCE   1  [PMID:6051341]
  AUTHORS   Baginsky ML, Rodwell VW.
  TITLE     Metabolism of pipecolic acid in a Pseudomonas species. V. Pipecolate
            oxidase and dehydrogenase.
  JOURNAL   J. Bacteriol. 94 (1967) 1034-9.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.99.3
            ExPASy - ENZYME nomenclature database: 1.5.99.3
            ExplorEnz - The Enzyme Database: 1.5.99.3
            ERGO genome analysis and discovery system: 1.5.99.3
            BRENDA, the Enzyme Database: 1.5.99.3
            CAS: 9076-63-5
///
ENTRY       EC 1.5.99.4                 Enzyme
NAME        nicotine dehydrogenase;
            nicotine oxidase;
            D-nicotine oxidase;
            nicotine:(acceptor) 6-oxidoreductase (hydroxylating);
            L-nicotine oxidase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With other acceptors
SYSNAME     nicotine:acceptor 6-oxidoreductase (hydroxylating)
REACTION    (S)-nicotine + acceptor + H2O = (S)-6-hydroxynicotine + reduced
            acceptor [RN:R02860]
ALL_REAC    R02860 > R07946
SUBSTRATE   (S)-nicotine;
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
PRODUCT     (S)-6-hydroxynicotine [CPD:C01056];
            reduced acceptor [CPD:C00030]
COFACTOR    Metal [CPD:C00050];
            FMN [CPD:C00061]
COMMENT     A metalloprotein (FMN). The enzyme can act on both the naturally
            found (S)-enantiomer and the synthetic (R)-enantiomer of nicotine,
            with retention of configuration in both cases [4].
REFERENCE   1  [PMID:13475371]
  AUTHORS   BEHRMAN EJ, STANIER RY.
  TITLE     The bacterial oxidation of nicotinic acid.
  JOURNAL   J. Biol. Chem. 228 (1957) 923-45.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   2  [PMID:5849820]
  AUTHORS   Decker K, Bleeg H.
  TITLE     Induction and purification of stereospecific nicotine oxidizing
            enzymes from Arthrobacter oxidans.
  JOURNAL   Biochim. Biophys. Acta. 105 (1965) 313-24.
  ORGANISM  Arthrobacter oxidans
REFERENCE   3  [PMID:4962139]
  AUTHORS   Hochstein LI, Dalton BP.
  TITLE     The purification and properties of nicotine oxidase.
  JOURNAL   Biochim. Biophys. Acta. 139 (1967) 56-68.
  ORGANISM  Arthrobacter oxidans
REFERENCE   4  [PMID:13610912]
  AUTHORS   HOCHSTEIN LI, RITTENBERG SC.
  TITLE     The bacterial oxidation of nicotine. II. The isolation of the first
            oxidative product and its identification as (1)-6-hydroxynicotine.
  JOURNAL   J. Biol. Chem. 234 (1959) 156-60.
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
GENES       FAL: FRAAL6160
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.99.4
            ExPASy - ENZYME nomenclature database: 1.5.99.4
            ExplorEnz - The Enzyme Database: 1.5.99.4
            ERGO genome analysis and discovery system: 1.5.99.4
            UM-BBD (Biocatalysis/Biodegradation Database): 1.5.99.4
            BRENDA, the Enzyme Database: 1.5.99.4
            CAS: 37256-31-8
///
ENTRY       EC 1.5.99.5                 Enzyme
NAME        methylglutamate dehydrogenase;
            N-methylglutamate dehydrogenase;
            N-methyl-L-glutamate:(acceptor) oxidoreductase (demethylating)
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With other acceptors
SYSNAME     N-methyl-L-glutamate:acceptor oxidoreductase (demethylating)
REACTION    N-methyl-L-glutamate + acceptor + H2O = L-glutamate + formaldehyde +
            reduced acceptor [RN:R00609]
ALL_REAC    R00609
SUBSTRATE   N-methyl-L-glutamate [CPD:C01046];
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
PRODUCT     L-glutamate [CPD:C00025];
            formaldehyde [CPD:C00067];
            reduced acceptor [CPD:C00030]
COMMENT     A number of N-methyl-substituted amino acids can act as donor;
            2,6-dichloroindophenol is the best acceptor.
REFERENCE   1  [PMID:5028076]
  AUTHORS   Hersh LB, Stark MJ, Worthen S, Fiero MK.
  TITLE     N-methylglutamate dehydrogenase: kinetic studies on the solubilized
            enzyme.
  JOURNAL   Arch. Biochem. Biophys. 150 (1972) 219-26.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00680  Methane metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.99.5
            ExPASy - ENZYME nomenclature database: 1.5.99.5
            ExplorEnz - The Enzyme Database: 1.5.99.5
            ERGO genome analysis and discovery system: 1.5.99.5
            BRENDA, the Enzyme Database: 1.5.99.5
            CAS: 37217-26-8
///
ENTRY       EC 1.5.99.6                 Enzyme
NAME        spermidine dehydrogenase;
            spermidine:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With other acceptors
SYSNAME     spermidine:acceptor oxidoreductase
REACTION    spermidine + acceptor + H2O = propane-1,3-diamine + 4-aminobutanal +
            reduced acceptor [RN:R01915]
ALL_REAC    R01915 > R01914
SUBSTRATE   spermidine [CPD:C00315];
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
PRODUCT     propane-1,3-diamine [CPD:C00986];
            4-aminobutanal [CPD:C00555];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016];
            Heme [CPD:C00032]
COMMENT     A flavohemoprotein (FAD). Ferricyanide, 2,6-dichloroindophenol and
            cytochrome c can act as acceptor. 4-Aminobutanal condenses
            non-enzymically to 1-pyrroline.
REFERENCE   1  [PMID:4918845]
  AUTHORS   Tabor CW, Kellogg PD.
  TITLE     Identification of flavin adenine dinucleotide and heme in a
            homogeneous spermidine dehydrogenase from Serratia marcescens.
  JOURNAL   J. Biol. Chem. 245 (1970) 5424-33.
  ORGANISM  Serratia marcescens
REFERENCE   2
  AUTHORS   Tabor, H. and Tabor, C.W.
  TITLE     Biosynthesis and metabolism of 1,4-diaminobutane, spermidine,
            spermine, and related amines. IIE2a Speridine dehydrogenase.
  JOURNAL   Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 225-226.
  ORGANISM  Serratia marcescens
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00410  beta-Alanine metabolism
ORTHOLOGY   KO: K00316  spermidine dehydrogenase
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.99.6
            ExPASy - ENZYME nomenclature database: 1.5.99.6
            ExplorEnz - The Enzyme Database: 1.5.99.6
            ERGO genome analysis and discovery system: 1.5.99.6
            BRENDA, the Enzyme Database: 1.5.99.6
            CAS: 9076-64-6
///
ENTRY       EC 1.5.99.7       Obsolete  Enzyme
NAME        Transferred to 1.5.8.2
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With other acceptors
COMMENT     Transferred entry: now EC 1.5.8.2 trimethylamine dehydrogenase (EC
            1.5.99.7 created 1976, deleted 2002)
STRUCTURES  PDB: 1DJN  1DJQ  1O94  1O95  2TMD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.99.7
            ExPASy - ENZYME nomenclature database: 1.5.99.7
            ExplorEnz - The Enzyme Database: 1.5.99.7
            ERGO genome analysis and discovery system: 1.5.99.7
            BRENDA, the Enzyme Database: 1.5.99.7
///
ENTRY       EC 1.5.99.8                 Enzyme
NAME        proline dehydrogenase;
            L-proline dehydrogenase;
            L-proline:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With other acceptors
SYSNAME     L-proline:acceptor oxidoreductase
REACTION    L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced
            acceptor [RN:R01253]
ALL_REAC    R01253;
            (other) R03295 R05051
SUBSTRATE   L-proline [CPD:C00148];
            acceptor [CPD:C00028]
PRODUCT     (S)-1-pyrroline-5-carboxylate [CPD:C03912];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:355248]
  AUTHORS   Scarpulla RC, Soffer RL.
  TITLE     Membrane-bound proline dehydrogenase from Escherichia coli.
            Solubilization, purification, and characterization.
  JOURNAL   J. Biol. Chem. 253 (1978) 5997-6001.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K00318  proline dehydrogenase
GENES       HSA: 5625(PRODH)
            MMU: 19125(Prodh)
            RNO: 680409(LOC680409)
            CFA: 477562(PRODH)
            BTA: 505094(PRODH)
            GGA: 770734(PRODH)
            SPU: 583929(LOC583929)
            DME: Dmel_CG1417(slgA)
            CEL: B0513.5
            SCE: YLR142W(PUT1)
            PIC: PICST_84147(PUT1)
            CGR: CAGL0M04499g
            ECO: b1014(putA)
            ECJ: JW0999(putA)
            ECE: Z1513(putA)
            ECS: ECs1260
            ECC: c1151(putA)
            ECI: UTI89_C1077(putA)
            ECP: ECP_1013
            ECV: APECO1_105(putA)
            ECW: EcE24377A_1132(putA)
            ECX: EcHS_A1129
            STY: STY1159(putA)
            STT: t1797(putA)
            SPT: SPA1727(putA)
            SEC: SC1074(putA)
            STM: STM1124(putA)
            YPE: YPO1851(putA)
            YPK: y2455(putA)
            YPM: YP_1542(putA2)
            YPA: YPA_1229
            YPN: YPN_2272
            YPS: YPTB1723(putA)
            YPI: YpsIP31758_2268(putA)
            SSN: SSON_1034(putA)
            SBO: SBO_2043(putA)
            ECA: ECA4217(putA)
            PLU: plu1957(putA)
            WBR: WGLp434(putA)
            SGL: SG1243
            PMU: PM0589(putA)
            APL: APL_0106(putA)
            XCC: XCC3835(putA)
            XCB: XC_3907(putA)
            XCV: XCV4008(putA)
            XAC: XAC3890(putA)
            XOO: XOO4145(putA)
            XOM: XOO_3922(XOO3922)
            VVU: VV2_1118
            VVY: VVA1644
            VPA: VPA1726
            VFI: VFA0831 VFA0832
            PPR: PBPRB1999
            PAE: PA0782(putA)
            PPU: PP_4947(putA)
            PST: PSPTO_5017
            PSB: Psyr_0506
            PSP: PSPPH_0496(putA)
            PFL: PFL_0495(putA)
            PFO: Pfl_0452
            PEN: PSEEN4999(putA)
            PAR: Psyc_1249
            PCR: Pcryo_1138
            ACI: ACIAD1646(putA)
            SON: SO_3774
            SDN: Sden_0689
            SFR: Sfri_0568
            SHE: Shewmr4_3122
            SHM: Shewmr7_0850
            SHN: Shewana3_0819
            ILO: IL1961(putA)
            CPS: CPS_4410(putA)
            PHA: PSHAa2264(putA)
            CBU: CBU_0629(putA)
            CBD: COXBU7E912_0641(putA)
            LPN: lpg1696(putA)
            LPF: lpl1655(putA)
            LPP: lpp1661(putA)
            FTU: FTT1150c(putA)
            FTF: FTF1150c(putA)
            FTW: FTW_1189(putA)
            FTL: FTL_0805
            FTH: FTH_0799(putA)
            FTA: FTA_0851
            FTN: FTN_1131(putA)
            NOC: Noc_1705
            AEH: Mlg_2702
            HCH: HCH_01824(putA)
            AHA: AHA_0776
            NME: NMB0401
            NMA: NMA2084(putA)
            NMC: NMC1766(putA)
            CVI: CV_1538(putA)
            RSO: RSc3301(putA)
            REU: Reut_A3340
            REH: H16_A3631(putA)
            RME: Rmet_3489
            BMA: BMA2965(putA)
            BXE: Bxe_A0049
            BUR: Bcep18194_A3294 Bcep18194_B1500
            BCN: Bcen_2942
            BCH: Bcen2424_0113
            BAM: Bamb_0103
            BPS: BPSL3389(putA)
            BPM: BURPS1710b_0166(putA)
            BPL: BURPS1106A_4032(putA)
            BPD: BURPS668_3958(putA)
            BTE: BTH_I3301
            BPE: BP2749(putA)
            BPA: BPP2579(putA)
            BBR: BB2024(putA)
            RFR: Rfer_2811
            POL: Bpro_0406
            HAR: HEAR2142(putA)
            MMS: mma_1319
            NET: Neut_1859
            NMU: Nmul_A1546
            EBA: ebA551(putA)
            HPY: HP0056
            HPJ: jhp0048(putA)
            HPA: HPAG1_0053
            HHE: HH0156
            HAC: Hac_1557(putA)
            TDN: Tmden_1327
            CJE: Cj1503c(putA)
            CJR: CJE1676
            CJU: C8J_1406
            GSU: GSU3395(putA)
            GME: Gmet_3512
            DVU: DVU3319(putA)
            DDE: Dde_0054
            BBA: Bd1251(putA)
            MXA: MXAN_7405
            SFU: Sfum_0833
            WOL: WD0103(putA)
            WBM: Wbm0539
            AMA: AM583(putA)
            APH: APH_0669(putA)
            ERU: Erum3850(putA)
            ERW: ERWE_CDS_03970(putA)
            ERG: ERGA_CDS_03930(putA)
            ECN: Ecaj_0375
            ECH: ECH_0667(putA)
            MLO: mll1160
            MES: Meso_1325
            SME: SMc02181(putA)
            ATU: Atu4157(putA)
            ATC: AGR_L_1394
            RLE: pRL120554(putA)
            BME: BMEII0564
            BMF: BAB2_0518
            BMB: BruAb2_0509
            BJA: blr7261(putA)
            BRA: BRADO6914(putA)
            BBT: BBta_6002(putA)
            RPA: RPA1580(putA)
            RPB: RPB_3946
            RPC: RPC_4274
            RPD: RPD_3707
            RPE: RPE_4317
            NWI: Nwi_3055
            CCR: CC_0804
            SIL: SPO3010(putA)
            SIT: TM1040_1695
            RSP: RSP_2166(putA)
            RDE: RD1_2509(putA)
            MMR: Mmar10_0398
            HNE: HNE_2988
            GOX: GOX2117
            GBE: GbCGDNIH1_0110
            RRU: Rru_A0656
            MAG: amb2507
            ABA: Acid345_1338
            BAN: BA5253
            BAR: GBAA5253
            BAA: BA_0116
            BAT: BAS4879
            BCE: BC5006
            BCA: BCE_5148
            BCZ: BCZK4736(putA)
            BTK: BT9727_4721(putA)
            BTL: BALH_2996(putA) BALH_4549(putA)
            BLI: BL01709
            BLD: BLi00373(ycgM)
            BCL: ABC0247 ABC0963
            BPU: BPUM_0300(ycgM)
            GKA: GK3010
            SAC: SACOL1816(putA)
            SAA: SAUSA300_1711(putA)
            SER: SERP1324(putA)
            SHA: SH1157
            STH: STH645
            MTU: Rv1188
            MBO: Mb1220
            MBB: BCG_1250
            MSM: MSMEG_5117
            MMC: Mmcs_4025
            CGL: NCgl0098(cgl0099)
            CGB: cg0129(putA)
            CEF: CE0101
            CJK: jk0454(putA)
            LXX: Lxx02530(poaA)
            CMI: CMM_0619(putA)
            PAC: PPA0620
            TFU: Tfu_0434
            FRA: Francci3_2823
            FAL: FRAAL4348
            ACE: Acel_0248
            SEN: SACE_1978
            RXY: Rxyl_2923
            RBA: RB8262(putA)
            PCU: pc0033(putA)
            SYN: sll1561(putA)
            CYB: CYB_0516
            TEL: tlr0416(putA)
            GVI: glr2755(putA)
            ANA: alr0540
            AVA: Ava_2942
            TER: Tery_3446
            BTH: BT_3115
            SRU: SRU_0546
            CHU: CHU_0720(pdh)
            GFO: GFO_1493
            DGE: Dgeo_0851
            TTJ: TTHA1579
            HMA: rrnAC2471(yusM)
STRUCTURES  PDB: 1K87  1TIW  1TJ0  1TJ1  1TJ2  1Y56  2FZM  2FZN  2G37  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.99.8
            ExPASy - ENZYME nomenclature database: 1.5.99.8
            ExplorEnz - The Enzyme Database: 1.5.99.8
            ERGO genome analysis and discovery system: 1.5.99.8
            BRENDA, the Enzyme Database: 1.5.99.8
            CAS: 9050-70-8
///
ENTRY       EC 1.5.99.9                 Enzyme
NAME        methylenetetrahydromethanopterin dehydrogenase;
            N5,N10-methylenetetrahydromethanopterin dehydrogenase;
            5,10-methylenetetrahydromethanopterin dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With other acceptors
SYSNAME     5,10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase
REACTION    5,10-methylenetetrahydromethanopterin + coenzyme F420 =
            5,10-methenyltetrahydromethanopterin + reduced coenzyme F420
            [RN:R04456]
ALL_REAC    R04456
SUBSTRATE   5,10-methylenetetrahydromethanopterin [CPD:C04377];
            coenzyme F420 [CPD:C00876]
PRODUCT     5,10-methenyltetrahydromethanopterin [CPD:C04330];
            reduced coenzyme F420 [CPD:C01080]
COMMENT     Coenzyme F420 is a 7,8-didemethyl-8-hydroxy-5-deazariboflavin
            derivative; methanopterin is a pterin analogue. The enzyme is
            involved in the formation of methane from CO2 in Methanobacterium
            thermoautotrophicum.
REFERENCE   1  [PMID:4084309]
  AUTHORS   Hartzell PL, Zvilius G, Escalante-Semerena JC, Donnelly MI.
  TITLE     Coenzyme F420 dependence of the methylenetetrahydromethanopterin
            dehydrogenase of Methanobacterium thermoautotrophicum.
  JOURNAL   Biochem. Biophys. Res. Commun. 133 (1985) 884-90.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
REFERENCE   2  [PMID:1911853]
  AUTHORS   te Brommelstroet BW, Geerts WJ, Keltjens JT, van der Drift C, Vogels
            GD.
  TITLE     Purification and properties of 5,10-methylenetetrahydromethanopterin
            dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase,
            two coenzyme F420-dependent enzymes, from Methanosarcina barkeri.
  JOURNAL   Biochim. Biophys. Acta. 1079 (1991) 293-302.
  ORGANISM  Methanosarcina barkeri [GN:mba]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K00319  methylenetetrahydromethanopterin dehydrogenase
GENES       MJA: MJ0715
            MMP: MMP0058(mer) MMP0372(mtd) MMP1716(hmdII)
            MMQ: MmarC5_1303
            MMZ: MmarC7_1368
            MAE: Maeo_1367
            MVN: Mevan_1360
            MAC: MA3733(mer) MA4430(mtd)
            MBA: Mbar_A0254 Mbar_A1095
            MMA: MM_0628 MM_1108
            MBU: Mbur_0929
            MTP: Mthe_0809
            MHU: Mhun_2255
            MEM: Memar_0562
            MBN: Mboo_0530
            MTH: MTH1464(mtd)
            MST: Msp_0163(mtd)
            MSI: Msm_0542 Msm_1204
            MKA: MK0011(mtd) MK0524(mer) MK1122(hmdIII) MK1365(hmdII)
            AFU: AF1066(mer-1) AF1196(mer-2)
            HMA: rrnAC2437(mer1)
            NPH: NP1056A
            RCI: RCIX2230(mtd)
STRUCTURES  PDB: 1QV9  1U6I  1U6J  1U6K  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.99.9
            ExPASy - ENZYME nomenclature database: 1.5.99.9
            ExplorEnz - The Enzyme Database: 1.5.99.9
            ERGO genome analysis and discovery system: 1.5.99.9
            UM-BBD (Biocatalysis/Biodegradation Database): 1.5.99.9
            BRENDA, the Enzyme Database: 1.5.99.9
            CAS: 100357-01-5
///
ENTRY       EC 1.5.99.10      Obsolete  Enzyme
NAME        Transferred to 1.5.8.1
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With other acceptors
COMMENT     Transferred entry: now EC 1.5.8.1 dimethylamine dehydrogenase (EC
            1.5.99.10 created 1999, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.99.10
            ExPASy - ENZYME nomenclature database: 1.5.99.10
            ExplorEnz - The Enzyme Database: 1.5.99.10
            ERGO genome analysis and discovery system: 1.5.99.10
            BRENDA, the Enzyme Database: 1.5.99.10
///
ENTRY       EC 1.5.99.11                Enzyme
NAME        5,10-methylenetetrahydromethanopterin reductase;
            5,10-methylenetetrahydromethanopterin cyclohydrolase;
            N5,N10-methylenetetrahydromethanopterin reductase;
            methylene-H4MPT reductase;
            coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin
            reductase;
            N5,N10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With other acceptors
SYSNAME     5-methyltetrahydromethanopterin:coenzyme-F420 oxidoreductase
REACTION    5-methyltetrahydromethanopterin + coenzyme F420 =
            5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
            [RN:R04464]
ALL_REAC    R04464
SUBSTRATE   5-methyltetrahydromethanopterin [CPD:C04488];
            coenzyme F420 [CPD:C00876]
PRODUCT     5,10-methylenetetrahydromethanopterin [CPD:C04377];
            reduced coenzyme F420 [CPD:C01080]
COMMENT     Catalyses an intermediate step in methanogenesis from CO2 and H2 in
            bacteria.
REFERENCE   1  [PMID:2379499]
  AUTHORS   Ma K, Thauer RK.
  TITLE     Purification and properties of N5,
            N10-methylenetetrahydromethanopterin reductase from Methanobacterium
            thermoautotrophicum (strain Marburg).
  JOURNAL   Eur. J. Biochem. 191 (1990) 187-93.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
REFERENCE   2  [PMID:1911853]
  AUTHORS   te Brommelstroet BW, Geerts WJ, Keltjens JT, van der Drift C, Vogels
            GD.
  TITLE     Purification and properties of 5,10-methylenetetrahydromethanopterin
            dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase,
            two coenzyme F420-dependent enzymes, from Methanosarcina barkeri.
  JOURNAL   Biochim. Biophys. Acta. 1079 (1991) 293-302.
  ORGANISM  Methanosarcina barkeri [GN:mba]
REFERENCE   3  [PMID:1696553]
  AUTHORS   Ma K, Thauer RK.
  TITLE     Single step purification of methylenetetrahydromethanopterin
            reductase from Methanobacterium thermoautotrophicum by specific
            binding to blue sepharose CL-6B.
  JOURNAL   FEBS. Lett. 268 (1990) 59-62.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
REFERENCE   4  [PMID:2298726]
  AUTHORS   te Brommelstroet BW, Hensgens CM, Keltjens JT, van der Drift C,
            Vogels GD.
  TITLE     Purification and properties of 5,10-methylenetetrahydromethanopterin
            reductase, a coenzyme F420-dependent enzyme, from Methanobacterium
            thermoautotrophicum strain delta H.
  JOURNAL   J. Biol. Chem. 265 (1990) 1852-7.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
REFERENCE   5  [PMID:2298699]
  AUTHORS   te Brommelstroet BW, Hensgens CM, Geerts WJ, Keltjens JT, van der
            Drift C, Vogels GD.
  TITLE     Purification and properties of 5,10-methenyltetrahydromethanopterin
            cyclohydrolase from Methanosarcina barkeri.
  JOURNAL   J. Bacteriol. 172 (1990) 564-71.
  ORGANISM  Methanosarcina barkeri [GN:mba]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K00320  coenzyme F420-dependent
                        N5,N10-methenyltetrahydromethanopterin reductase
GENES       ABO: ABO_1208(hmd)
            RPB: RPB_4431
            SWI: Swit_0724
            MAV: MAV_2543
            MSM: MSMEG_2103 MSMEG_2456 MSMEG_3445
            RHA: RHA1_ro00195 RHA1_ro00400 RHA1_ro01290 RHA1_ro01706
                 RHA1_ro02495 RHA1_ro02649 RHA1_ro04686
            NCA: Noca_1630
            FAL: FRAAL3374 FRAL5465
            SEN: SACE_2863
            MJA: MJ0784
            MMP: MMP0127(hmd)
            MMQ: MmarC5_1619
            MMZ: MmarC7_1055
            MAE: Maeo_0749
            MVN: Mevan_1073
            MBU: Mbur_2372
            MTP: Mthe_0205
            MHU: Mhun_2257
            MEM: Memar_0557
            MBN: Mboo_0528
            MTH: MTH1142(hmd)
            MST: Msp_1128(mer)
            MSI: Msm_0572
            MKA: MK0013(hmd)
            HWA: HQ3154A(mer)
            RCI: RCIX564(mer)
STRUCTURES  PDB: 1Z69  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.99.11
            ExPASy - ENZYME nomenclature database: 1.5.99.11
            ExplorEnz - The Enzyme Database: 1.5.99.11
            ERGO genome analysis and discovery system: 1.5.99.11
            UM-BBD (Biocatalysis/Biodegradation Database): 1.5.99.11
            BRENDA, the Enzyme Database: 1.5.99.11
///
ENTRY       EC 1.5.99.12                Enzyme
NAME        cytokinin dehydrogenase;
            N6-dimethylallyladenine:(acceptor) oxidoreductase;
            6-N-dimethylallyladenine:acceptor oxidoreductase;
            OsCKX2;
            CKX;
            cytokinin oxidase/dehydrogenase
CLASS       Oxidoreductases;
            Acting on the CH-NH group of donors;
            With other acceptors
SYSNAME     N6-dimethylallyladenine:acceptor oxidoreductase
REACTION    N6-dimethylallyladenine + acceptor + H2O = adenine +
            3-methylbut-2-enal + reduced acceptor [RN:R05708]
ALL_REAC    R05708
SUBSTRATE   N6-dimethylallyladenine [CPD:C04083];
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
PRODUCT     adenine [CPD:C00147];
            3-methylbut-2-enal [CPD:C07330];
            reduced acceptor [CPD:C00030]
COMMENT     A flavoprotein(FAD). Catalyses the oxidation of cytokinins, a family
            of N6-substituted adenine derivatives that are plant hormones, where
            the substituent is a dimethylallyl or other prenyl group. Although
            this activity was previously thought to be catalysed by a
            hydrogen-peroxide-forming oxidase, this enzyme does not require
            oxygen for activity and does not form hydrogen peroxide.
            2,6-Dichloroindophenol, methylene blue, nitroblue tetrazolium,
            phenazine methosulfate and Cu(II) in the presence of imidazole can
            act as acceptors. This enzyme plays a part in regulating rice-grain
            production, with lower levels of the enzyme resulting in enhanced
            grain production [2].
REFERENCE   1  [PMID:11168382]
  AUTHORS   Galuszka P, Frebort I, Sebela M, Sauer P, Jacobsen S, Pec P.
  TITLE     Cytokinin oxidase or dehydrogenase? Mechanism of cytokinin
            degradation in cereals.
  JOURNAL   Eur. J. Biochem. 268 (2001) 450-61.
  ORGANISM  Arabidopsis thaliana [GN:ath]
ORTHOLOGY   KO: K00279  cytokinin dehydrogenase
GENES       ATH: AT1G75450(CKX5) AT2G19500(CKX2) AT2G41510(ATCKX1/CKX1)
                 AT4G29740(CKX4) AT5G21482(CKX7) AT5G56970(CKX3)
            OSA: 4338605
            ANA: all0324
            AVA: Ava_4717
STRUCTURES  PDB: 1W1O  1W1Q  1W1R  1W1S  2EXR  2Q4W  
DBLINKS     IUBMB Enzyme Nomenclature: 1.5.99.12
            ExPASy - ENZYME nomenclature database: 1.5.99.12
            ExplorEnz - The Enzyme Database: 1.5.99.12
            ERGO genome analysis and discovery system: 1.5.99.12
            BRENDA, the Enzyme Database: 1.5.99.12
///
ENTRY       EC 1.6.1.1                  Enzyme
NAME        NAD(P)+ transhydrogenase (B-specific);
            pyridine nucleotide transhydrogenase;
            transhydrogenase;
            NAD(P)+ transhydrogenase;
            nicotinamide adenine dinucleotide (phosphate) transhydrogenase;
            NAD+ transhydrogenase;
            NADH transhydrogenase;
            nicotinamide nucleotide transhydrogenase;
            NADPH-NAD+ transhydrogenase;
            pyridine nucleotide transferase;
            NADPH-NAD+ oxidoreductase;
            NADH-NADP+-transhydrogenase;
            NADPH:NAD+ transhydrogenase;
            H+-Thase;
            non-energy-linked transhydrogenase;
            NAD(P)+ transhydrogenase (B-specific)
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With NAD+ or NADP+ as acceptor
SYSNAME     NADPH:NAD+ oxidoreductase (B-specific)
REACTION    NADPH + NAD+ = NADP+ + NADH [RN:R00112]
ALL_REAC    R00112
SUBSTRATE   NADPH [CPD:C00005];
            NAD+ [CPD:C00003]
PRODUCT     NADP+ [CPD:C00006];
            NADH [CPD:C00004]
COFACTOR    FAD [CPD:C00016]
COMMENT     The enzyme from Azotobacter vinelandii is a flavoprotein (FAD). It
            is B-specific with respect to both NAD+ and NADP+. Also acts on
            deamino coenzymes [cf. EC 1.6.1.2 NAD(P)+ transhydrogenase
            (AB-specific)].
REFERENCE   1  [PMID:13412660]
  AUTHORS   HUMPHREY GF.
  TITLE     The distribution and properties of transhydrogenase from animal
            tissues.
  JOURNAL   Biochem. J. 65 (1957) 546-50.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   2  [PMID:3157549]
  AUTHORS   You KS.
  TITLE     Stereospecificity for nicotinamide nucleotides in enzymatic and
            chemical hydride transfer reactions.
  JOURNAL   CRC. Crit. Rev. Biochem. 17 (1985) 313-451.
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K00322  NAD(P) transhydrogenase
GENES       AFM: AFUA_5G02780
            PFA: PF14_0508
            CPV: cgd8_2330
            CHO: Chro.80274
            TET: TTHERM_00314860
            ECO: b3962(udhA)
            ECJ: JW5551(sthA)
            ECE: Z5521(udhA)
            ECS: ECs4891
            ECC: c4923(udhA)
            ECI: UTI89_C4555(sthA)
            ECP: ECP_4177
            ECV: APECO1_2503(udhA)
            ECW: EcE24377A_1810(pntA) EcE24377A_4502(sthA)
            ECX: EcHS_A1677 EcHS_A4196(sthA)
            STY: STY3748(udhA)
            STT: t3499(udhA)
            SPT: SPA3964(udhA)
            SEC: SC4015(udhA)
            STM: STM4126(udhA)
            YPE: YPO3914(sthA)
            YPK: y0321(udhA)
            YPM: YP_3134(sthA)
            YPA: YPA_0108
            YPN: YPN_0053
            YPP: YPDSF_3526
            YPS: YPTB0121(sthA)
            YPI: YpsIP31758_0137(sthA) YpsIP31758_1830(pntA)
                 YpsIP31758_1831(pntB)
            YEN: YE0134(sth)
            SFL: SF4044(udhA)
            SFX: S3700(udhA)
            SFV: SFV_4035(udhA)
            SSN: SSON_4135(udhA)
            SBO: SBO_3981(udhA)
            SDY: SDY_3797(udhA)
            ECA: ECA4242(sthA)
            PLU: plu4739(sthA)
            SGL: SG2157
            KPN: KPN_04251(udhA)
            VCH: VC0151
            VCO: VC0395_0497(pntA) VC0395_0498(pntB)
            VVU: VV1_1168
            VVY: VV0126
            VPA: VP2942
            VFI: VF2439
            PPR: PBPRA3468(sthA)
            PAE: PA2991(sth)
            PAU: PA14_25390(sth)
            PPU: PP_2151(sthA)
            PST: PSPTO_2106(sthA)
            PSB: Psyr_1901
            PSP: PSPPH_1856(sthA) PSPPH_5098(pntAA) PSPPH_5099(pntAB)
                 PSPPH_5100(pntB)
            PFL: PFL_0113(pntB) PFL_0114(pntAB) PFL_0115(pntAA) PFL_1958(sthA)
            PFO: Pfl_3862
            PEN: PSEEN3711(sthA)
            PMY: Pmen_1603
            PAR: Psyc_1333(sthA)
            PCR: Pcryo_1036
            ACI: ACIAD2274(sthA)
            ACB: A1S_2328
            ILO: IL0322(udhA)
            CPS: CPS_0334(sthA)
            PHA: PSHAa2898(sthA)
            SDE: Sde_1805
            PIN: Ping_0118
            MAQ: Maqu_1923
            LPN: lpg0876(pntAa)
            FTU: FTT0684c(sthA)
            FTF: FTF0684c(sthA)
            FTW: FTW_1044(sthA)
            FTL: FTL_0960
            FTH: FTH_0938
            FTA: FTA_1011
            FTN: FTN_0999(udhA)
            AEH: Mlg_0914
            HCH: HCH_02051 HCH_02695 HCH_03045(pntA)
            CSA: Csal_1577
            ABO: ABO_1570(sth)
            NMC: NMC0958(pntB) NMC0960(pntA)
            CVI: CV_0099(pntB)
            RSO: RSc2733(pntB)
            BMV: BMASAVP1_A0280 BMASAVP1_A0281 BMASAVP1_A0282(pntB)
            BML: BMA10299_A1142 BMA10299_A1143 BMA10299_A1144(pntB)
            BMN: BMA10247_2546 BMA10247_2547 BMA10247_2548(pntB)
            BPM: BURPS1710b_3393(pntAB) BURPS1710b_3394(pntAA)
            NEU: NE0859(pntAa) NE0861(pntB)
            MXA: MXAN_2411(sthA)
            RTY: RT0058(pntB) RT0852(pntA)
            RCO: RC0104(pntB)
            RFE: RF_0059(pntB) RF_1361(pntA2) RF_1362(pntA1)
            RBE: RBE_0024(pntB) RBE_0044(pntA2) RBE_0045(pntA1)
            PUB: SAR11_0576(pntB)
            MLO: mlr8366
            SME: SMc00300
            ATU: Atu1661(sthA)
            ATC: AGR_C_3055
            RET: RHE_CH01846(ypch00610)
            RLE: RL2066(sthA)
            BME: BMEII0324
            BOV: BOV_A0911(pntB) BOV_A0912(pntAB) BOV_A0913(pntA)
            BJA: bll0896
            RPA: RPA4181(pntA) RPA4182(pntA)
            SIL: SPO3828(sthA)
            SIT: TM1040_3447
            GBE: GbCGDNIH1_1246
            ABA: Acid345_3223
            SUS: Acid_1071
            MTU: Rv2713(sthA)
            MTC: MT2786
            MBO: Mb2732(sthA)
            MBB: BCG_0193(pntB) BCG_2726(sthA)
            MPA: MAP2829
            MAV: MAV_3606
            MSM: MSMEG_2748(sthA)
            MVA: Mvan_2448
            FRA: Francci3_3883
            FAL: FRAAL6153(sthA)
            RBA: RB5717(sthA)
            PCU: pc0725(udhA)
            LIL: LA0334 LA0335(pntB)
            SYR: SynRCC307_0626
STRUCTURES  PDB: 1D4O  1DJL  1E3T  1F8G  1HZZ  1L7D  1L7E  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.1.1
            ExPASy - ENZYME nomenclature database: 1.6.1.1
            ExplorEnz - The Enzyme Database: 1.6.1.1
            ERGO genome analysis and discovery system: 1.6.1.1
            BRENDA, the Enzyme Database: 1.6.1.1
            CAS: 9014-18-0
///
ENTRY       EC 1.6.1.2                  Enzyme
NAME        NAD(P)+ transhydrogenase (AB-specific);
            pyridine nucleotide transhydrogenase;
            transhydrogenase;
            NAD(P)+ transhydrogenase;
            nicotinamide adenine dinucleotide (phosphate) transhydrogenase;
            NAD+ transhydrogenase;
            NADH transhydrogenase;
            nicotinamide nucleotide transhydrogenase;
            NADPH-NAD+ transhydrogenase;
            pyridine nucleotide transferase;
            NADPH-NAD+ oxidoreductase;
            NADH-NADP+-transhydrogenase;
            NADPH:NAD+ transhydrogenase;
            H+-Thase;
            energy-linked transhydrogenase;
            NAD(P)+ transhydrogenase (AB-specific)
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With NAD+ or NADP+ as acceptor
SYSNAME     NADPH:NAD+ oxidoreductase (AB-specific)
REACTION    NADPH + NAD+ = NADP+ + NADH [RN:R00112]
ALL_REAC    R00112
SUBSTRATE   NADPH [CPD:C00005];
            NAD+ [CPD:C00003]
PRODUCT     NADP+ [CPD:C00006];
            NADH [CPD:C00004]
COMMENT     The enzyme from heart mitochondria is A-specific with respect to
            NAD+ and B-specific with respect to NADP+ [cf. EC 1.6.1.1 NAD(P)+
            transhydrogenase (B-specific)].
REFERENCE   1
  AUTHORS   Fisher, R.R. and Earle, S.R.
  TITLE     Membrane-bound pyridine dinucleotide transhydrogenases.
  JOURNAL   In: Everse, J., Anderson, B. and You, K. (Eds.), The Pyridine
            Nucleotide Coenzymes, The Pyridine Nucleotide Coenzymes, New York,
            1982, p. 279-324.
REFERENCE   2  [PMID:3157549]
  AUTHORS   You KS.
  TITLE     Stereospecificity for nicotinamide nucleotides in enzymatic and
            chemical hydride transfer reactions.
  JOURNAL   CRC. Crit. Rev. Biochem. 17 (1985) 313-451.
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K00323  NAD(P) transhydrogenase
            KO: K00324  NAD(P) transhydrogenase subunit alpha
            KO: K00325  NAD(P) transhydrogenase subunit beta
GENES       HSA: 23530(NNT)
            PTR: 461888(NNT)
            MMU: 18115(Nnt)
            CFA: 479342(NNT)
            BTA: 280878(NNT)
            XLA: 447528(MGC83563)
            DRE: 406619(nnt)
            SPU: 373388(LOC373388)
            CEL: C15H9.1(nnt-1)
            AOR: AO090102000470 AO090102000471 AO090102000473
            DDI: DDB_0231372
            EHI: 490.t00007
            ECO: b1602(pntB) b1603(pntA)
            ECJ: JW1594(pntB) JW1595(pntA)
            ECE: Z2597(pntB) Z2600(pntA)
            ECS: ECs2308 ECs2309
            ECC: c1994(pntB) c1995(pntA)
            ECI: UTI89_C1790(pntB) UTI89_C1791(pntA)
            ECP: ECP_1546 ECP_1547
            ECV: APECO1_685 APECO1_686(pntA)
            STY: STY1588(pntB) STY1589(pntA)
            STT: t1399(pntA) t1400(pntB)
            SPT: SPA1375(pntB) SPA1376(pntA)
            SEC: SC1497(pntA) SC1498(pntB)
            STM: STM1479(pntA) STM1480(pntB)
            YPE: YPO2302(pntB) YPO2303(pntA)
            YPK: y2134(pntB) y2135(pntA)
            YPM: YP_2087(pntB) YP_2088(pntA)
            YPA: YPA_1651 YPA_1652
            YPN: YPN_1763 YPN_1764
            YPP: YPDSF_0840
            YPS: YPTB2224(pntB) YPTB2225(pntA)
            SFL: SF1623(pntB) SF1624(pntA)
            SFX: S1755(pntB) S1756(pntA)
            SFV: SFV_1617(pntB) SFV_1618(pntA)
            SSN: SSON_1557(pntA) SSON_1558(pntB)
            SBO: SBO_1533(pntA) SBO_1534(pntB)
            SDY: SDY_1550(pntA) SDY_1551(pntB)
            ECA: ECA2204(pntA) ECA2205(pntB)
            PLU: plu2167(pntA) plu2168(pntB)
            SGL: SG1487 SG1488
            ENT: Ent638_1849
            SPE: Spro_2584 Spro_2585
            HIN: HI1362(pntA) HI1363(pntB)
            HIT: NTHI1801(pntB) NTHI1802(pntA)
            HIP: CGSHiEE_04340(pntA) CGSHiEE_04355(pntB)
            HIQ: CGSHiGG_00465(pntA)
            HDU: HD1662(pntB) HD1663(pntA)
            HSO: HS_0232(pntA) HS_0233(pntB)
            PMU: PM0752(pntB) PM0753(pntA)
            MSU: MS1223(pntB) MS1224(pntA)
            APL: APL_0841(pntB) APL_0842(pntA)
            ASU: Asuc_1022
            XCV: XCV0951 XCV0955
            XAC: XAC0918(pntA) XAC0919(pntA) XAC0923(pntA) XAC0924(pntB)
            XOO: XOO3629(pntB) XOO3630(pntA) XOO3633(pntA)
            XOM: XOO_3430(XOO3430) XOO_3431(XOO3431) XOO_3435(XOO3435)
            VCH: VCA0563 VCA0564
            VVU: VV2_0315 VV2_0316 VV2_0317
            VVY: VVA0811 VVA0812
            VPA: VPA0921 VPA0922
            VFI: VFA0585 VFA0586
            PPR: PBPRB0902 PBPRB0903
            PAE: PA0196(pntB)
            PAP: PSPA7_0275 PSPA7_0276
            PPU: PP_0155(pntB)
            PPF: Pput_0173 Pput_0175
            PST: PSPTO_5464(pntB)
            PSB: Psyr_5016 Psyr_5017 Psyr_5018
            PFO: Pfl_0112 Pfl_0113 Pfl_0114
            PEN: PSEEN0114(pntB) PSEEN0115(pntAB) PSEEN0116(pntAA)
            PMY: Pmen_4431 Pmen_4433
            PAR: Psyc_0555 Psyc_0556(pntA) Psyc_0557(pntB)
            PCR: Pcryo_0543 Pcryo_0545
            PRW: PsycPRwf_0634
            ACI: ACIAD3078(pntB) ACIAD3079(pntA-2) ACIAD3080(pntA-1)
            SON: SO_3740(pntA) SO_3741(pntB)
            SDN: Sden_0930 Sden_0931
            SFR: Sfri_3194 Sfri_3195
            SAZ: Sama_2840
            SBM: Shew185_0917
            SSE: Ssed_1757
            SPL: Spea_0650
            SHE: Shewmr4_3081 Shewmr4_3082
            SHM: Shewmr7_0890 Shewmr7_0891
            SHN: Shewana3_0853 Shewana3_0854
            CPS: CPS_1783(pntA) CPS_1784(pntB1) CPS_4040(pntB2)
            PAT: Patl_3654 Patl_3655 Patl_3656
            SDE: Sde_0956 Sde_0957 Sde_0958 Sde_1274 Sde_1275 Sde_1276
            MAQ: Maqu_0369
            CBU: CBU_1955(pntAA) CBU_1956(pntAB) CBU_1957(pntB)
            CBD: COXBU7E912_0164(pntB) COXBU7E912_0165(pntAB)
                 COXBU7E912_0166(pntAA)
            LPN: lpg0874(pntB) lpg0875(pntAb2)
            LPF: lpl0907(pntB) lpl0908(pnaB)
            LPP: lpp0937(pntB) lpp0938(pnaB) lpp0939(pntA)
            MCA: MCA2767(pntB) MCA2768(pntA)
            NOC: Noc_0261 Noc_0262(pntA)
            AEH: Mlg_2769 Mlg_2770 Mlg_2771
            HCH: HCH_03044
            CSA: Csal_2491 Csal_2492
            ABO: ABO_1327(pntB) ABO_1329(pntA)
            MMW: Mmwyl1_1968 Mmwyl1_2278
            AHA: AHA_4079(pntB) AHA_4080(pntA)
            NME: NMB0978 NMB0980
            NMA: NMA1175(pntB) NMA1177(pntA)
            NGO: NGO1470 NGO1472
            CVI: CV_0100 CV_0101(pntA)
            RSO: RSc2730(pntAa) RSc2732(pntAb) RSp0949(pntAa2) RSp0950(pntAb2)
                 RSp0951(pntB2a) RSp0954(pntB2b)
            REU: Reut_A2823 Reut_A2825 Reut_A2826 Reut_B4666 Reut_B4667
                 Reut_B5290 Reut_B5291 Reut_B5292 Reut_B5720 Reut_B5721
                 Reut_B5722 Reut_C6058 Reut_C6059 Reut_C6060 Reut_C6083
                 Reut_C6084 Reut_C6085 Reut_C6362 Reut_C6363 Reut_C6364
                 Reut_C6407 Reut_C6408 Reut_C6409
            REH: H16_A0850(pntAa1) H16_A0851(pntAb1) H16_A0852(pntB1)
                 H16_A1264(pntAa2) H16_A1265(pntAb2) H16_A1266(pntB2)
                 H16_A3128(pntAa3) H16_A3130(pntAb3) H16_A3131(pntB3)
                 H16_B1714(pntB4) H16_B1715(pntA4)
            RME: Rmet_1531 Rmet_1532 Rmet_2963 Rmet_2964 Rmet_2965
            BMA: BMA2366 BMA2367 BMA2368(pntB)
            BXE: Bxe_A4006 Bxe_A4007 Bxe_A4008 Bxe_B2265 Bxe_C0524 Bxe_C0525
                 Bxe_C0526
            BUR: Bcep18194_A3786 Bcep18194_A3787 Bcep18194_A3788
                 Bcep18194_C7227 Bcep18194_C7228 Bcep18194_C7554
            BCN: Bcen_0218
            BCH: Bcen2424_0702
            BPS: BPSL2885(pntB) BPSL2886(pntAB) BPSL2887(pntAA)
            BPM: BURPS1710b_3392(pntB) BURPS1710b_3393(pntAB)
                 BURPS1710b_3394(pntAA)
            BTE: BTH_I1259 BTH_I1260 BTH_I1261
            BPE: BP2897(pntAA) BP2898(pntAB) BP2899(pntB)
            BPA: BPP2497(pntB) BPP2498(pntAB) BPP2499(pntaA)
            BBR: BB1944(pntB) BB1945(pntAB) BB1946(pntaA)
            RFR: Rfer_3753 Rfer_3754
            POL: Bpro_4544 Bpro_4545 Bpro_4546
            PNA: Pnap_3800
            AJS: Ajs_3954
            VEI: Veis_4748
            MPT: Mpe_A3568 Mpe_A3570 Mpe_A3571
            HAR: HEAR0329(pntA) HEAR0330(pntB)
            MMS: mma_0376 mma_0377
            NEU: NE0860(pntAb2)
            NET: Neut_1191 Neut_1192 Neut_1193
            NMU: Nmul_A1151 Nmul_A1153
            EBA: ebA4497(pntAA) ebA4498(pntA) ebA4500(pntB)
            AZO: azo1003(pntAA)
            DAR: Daro_1497 Daro_1498 Daro_1499 Daro_3122 Daro_3123 Daro_3124
            ADE: Adeh_3005 Adeh_3006 Adeh_3007
            AFW: Anae109_2971 Anae109_2973
            RPR: RP074(pntB) RP862(pntAB) RP863(pntAA)
            RTY: RT0851(pntAB)
            RCO: RC1333(pntAB) RC1334(pntAA)
            PUB: SAR11_0574(pntA) SAR11_0575(pntAB)
            MLO: mlr5181 mlr5183 mlr5184
            MES: Meso_2804 Meso_2805 Meso_2806
            PLA: Plav_2058 Plav_2060
            SME: SMc03938(pntB) SMc03939(pntAb) SMc03950(pntAa)
            SMD: Smed_2757
            ATU: Atu2493(pntA) Atu2494(pntB)
            ATC: AGR_C_4529 AGR_C_4531
            RET: RHE_CH03611(pntB) RHE_CH03612(pntA1) RHE_CH03613(pntA2)
            RLE: RL4134(pntB) RL4135(pntAB) RL4136(pntAA) pRL80042(pntA)
                 pRL80043(pntB)
            BME: BMEII0323 BMEII0325
            BMF: BAB2_0261(pntA) BAB2_0262(pntAB) BAB2_0263(pntB)
            BMS: BRA0971(pntB) BRA0972(pntAB) BRA0973(pntA)
            BMB: BruAb2_0260(pntA) BruAb2_0261(pntAB) BruAb2_0262(pntB)
            OAN: Oant_1386
            BJA: bll7124(pntB) bll7125(pntAB) bll7126(pntA)
            BRA: BRADO1196(pntA2) BRADO1197(pntA2) BRADO1198(pntB)
            BBT: BBta_6856(pntB) BBta_6857(pntA2) BBta_6858(pntA2)
            RPA: RPA4180(pntB)
            RPB: RPB_1435 RPB_1437
            RPC: RPC_3966 RPC_3968
            RPD: RPD_1415 RPD_1417
            RPE: RPE_4096 RPE_4097 RPE_4098
            NWI: Nwi_0995 Nwi_0996 Nwi_0997
            NHA: Nham_1227 Nham_1228 Nham_1229
            XAU: Xaut_1948 Xaut_1950
            CCR: CC_3303 CC_3304 CC_3305
            SIL: SPO2819(pntB) SPO2820(pntA)
            SIT: TM1040_0707 TM1040_0708
            RSP: RSP_0239(pntB) RSP_0240(pntA)
            RSQ: Rsph17025_1581
            JAN: Jann_3281 Jann_3282
            RDE: RD1_3318(pntB) RD1_3319(pntA)
            MMR: Mmar10_2548 Mmar10_2549
            HNE: HNE_1138(pntB) HNE_1139(pntAB) HNE_1140(pntAA)
            NAR: Saro_1843 Saro_1844 Saro_1845
            SAL: Sala_0971 Sala_1381 Sala_1382
            SWI: Swit_1181
            ELI: ELI_02335 ELI_02345 ELI_02350
            GOX: GOX0310 GOX0311 GOX0312
            ACR: Acry_2155
            RRU: Rru_A2181 Rru_A2182 Rru_A2183
            MAG: amb2823 amb2824
            MGM: Mmc1_2119 Mmc1_2120
            ABA: Acid345_4185 Acid345_4186 Acid345_4187
            OOE: OEOE_0369 OEOE_0371
            MTU: Rv0155(pntAa) Rv0156(pntAb) Rv0157(pntB)
            MTC: MT0165(pntB)
            MBO: Mb0160(pntAa) Mb0161(pntAb) Mb0162(pntB)
            MBB: BCG_0191(pntAa)
            MLE: ML2634(pntB) ML2635(pntAB) ML2636(pntAA)
            MPA: MAP3572(pntAA) MAP3573(pntAB) MAP3574(pntB)
            MSM: MSMEG_0109(pntB) MSMEG_0110(pntA) MSMEG_0150 MSMEG_0151
                 MSMEG_0152 MSMEG_4108(pntB) MSMEG_4109(pntA)
            MMC: Mmcs_0100 Mmcs_0101
            CJK: jk1276
            NFA: nfa10130(pntAa) nfa10140(pntAb) nfa10150(pntB)
            RHA: RHA1_ro01581(pntB1) RHA1_ro01582 RHA1_ro01583(pntA1)
                 RHA1_ro02719(pntB2) RHA1_ro02720(pntA2)
            SCO: SCO7622(pntB) SCO7623(pntA)
            SMA: SAV403(pntB) SAV404(pntA)
            LXX: Lxx22560(pntA) Lxx22570 Lxx22580(pntB)
            PAC: PPA0625 PPA0626
            FRA: Francci3_2946 Francci3_2947 Francci3_2948
            SEN: SACE_5818(pntAA) SACE_5819(pntAb) SACE_5820(pntB)
            BLO: BL0856(pntB) BL0857(pntA)
            BAD: BAD_0725(pntA) BAD_0726(pntB)
            RXY: Rxyl_2938 Rxyl_2940
            RBA: RB12290(pntB) RB12291 RB12292(pntA)
            TDE: TDE1188(pntB)
            LIL: LA0052(pntA)
            LIC: LIC10046(pntA)
            LBJ: LBJ_0040(pntA)
            LBL: LBL_2994(pntA)
            SYN: slr1239(pntA) slr1434(pntB)
            SYW: SYNW0692(pntA-1) SYNW0693(pntA-2) SYNW0694(pntB)
            SYC: syc0067_c(pntB) syc0068_c(pntA) syc0069_c(pntA)
            SYF: Synpcc7942_1610 Synpcc7942_1611 Synpcc7942_1612
            SYD: Syncc9605_1974 Syncc9605_1975 Syncc9605_1976
            SYE: Syncc9902_0684 Syncc9902_0685 Syncc9902_0686
            SYG: sync_0915 sync_0916 sync_0917(pntB)
            SYR: SynRCC307_0358(pntB) SynRCC307_0359(pntAB)
                 SynRCC307_0360(pntAA)
            SYX: SynWH7803_1627(pntB) SynWH7803_1628(pntAB)
                 SynWH7803_1629(pntAA)
            TEL: tlr0694(pntA) tlr0696(pntB) tsr0695
            ANA: all3408 all3410 asl3409
            AVA: Ava_3428 Ava_3429 Ava_3430
            PMA: Pro1239(pntB) Pro1240(pntA) Pro1241(pntA)
            PMM: PMM1145(pntB) PMM1146(pntA-2) PMM1147(pntA-1)
            PMT: PMT1164(pntB) PMT1165(pntA-2) PMT1166(pntA-1)
            PMN: PMN2A_0753 PMN2A_0754 PMN2A_0755
            PMI: PMT9312_1244
            PMB: A9601_13201(pntB) A9601_13211(pntA-2) A9601_13221(pntA)
            PMC: P9515_13101(pntB) P9515_13111(pntA-2) P9515_13121(pntA)
            PMF: P9303_08601(pntA) P9303_08611(pntA-2) P9303_08621(pntB)
            PMG: P9301_13351(pntB) P9301_13361(pntA-2) P9301_13371(pntA)
            PMH: P9215_13501
            PME: NATL1_15931(pntB) NATL1_15941(pntA-2) NATL1_15951(pntA)
            TER: Tery_4703 Tery_4704 Tery_4705
            PGI: PG1332(pntB)
            SRU: SRU_2204 SRU_2205 SRU_2206
            TTH: TTC1778 TTC1779 TTC1780
            TTJ: TTHA0206 TTHA0207 TTHA0208
            MBN: Mboo_1315
STRUCTURES  PDB: 1NM5  1PNO  1PNQ  1PT9  1PTJ  1U28  1U2D  1U2G  1U31  1X13  
                 1X14  1X15  1XLT  2BRU  2FR8  2FRD  2FSV  2OO5  2OOR  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.1.2
            ExPASy - ENZYME nomenclature database: 1.6.1.2
            ExplorEnz - The Enzyme Database: 1.6.1.2
            ERGO genome analysis and discovery system: 1.6.1.2
            BRENDA, the Enzyme Database: 1.6.1.2
            CAS: 9014-18-0
///
ENTRY       EC 1.6.2.1        Obsolete  Enzyme
NAME        Transferred to 1.6.99.3
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a heme protein as acceptor
COMMENT     Transferred entry: now EC 1.6.99.3 NADH dehydrogenase (EC 1.6.2.1
            created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.2.1
            ExPASy - ENZYME nomenclature database: 1.6.2.1
            ExplorEnz - The Enzyme Database: 1.6.2.1
            ERGO genome analysis and discovery system: 1.6.2.1
            BRENDA, the Enzyme Database: 1.6.2.1
///
ENTRY       EC 1.6.2.2                  Enzyme
NAME        cytochrome-b5 reductase;
            cytochrome b5 reductase;
            dihydronicotinamide adenine dinucleotide-cytochrome b5 reductase;
            reduced nicotinamide adeninedinucleotide-cytochrome b5 reductase;
            NADH-ferricytochrome b5 oxidoreductase;
            NADH-cytochrome b5 reductase;
            NADH 5alpha-reductase ;
            NADH-cytochrome-b5 reductase
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a heme protein as acceptor
SYSNAME     NADH:ferricytochrome-b5 oxidoreductase
REACTION    NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
            [RN:R00100]
ALL_REAC    R00100
SUBSTRATE   NADH [CPD:C00004];
            ferricytochrome b5 [CPD:C00996]
PRODUCT     NAD+ [CPD:C00003];
            H+ [CPD:C00080];
            ferrocytochrome b5 [CPD:C00999]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:13563476]
  AUTHORS   MAHLER HR, RAW I, MOLINARI R, DO AMARAL DF.
  TITLE     Studies of electron transport enzymes. II. Isolation and some
            properties of a cytochrome-specific reduced diphosphopyridine
            nucleotide dehydrogenase from pig liver.
  JOURNAL   J. Biol. Chem. 233 (1958) 230-9.
  ORGANISM  pig [GN:ssc]
REFERENCE   2
  AUTHORS   Strittmatter, P.
  TITLE     Microsomal cytochrome b5 and cytochrome b5 reductase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 8, Academic Press, New York, 1963, p. 113-145.
REFERENCE   3  [PMID:13475360]
  AUTHORS   STRITTMATTER P, VELICK SF.
  TITLE     The purification and properties of microsomal cytochrome reductase.
  JOURNAL   J. Biol. Chem. 228 (1957) 785-99.
  ORGANISM  rat [GN:rno], rabbit
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K00326  cytochrome-b5 reductase
GENES       HSA: 1727(CYB5R3) 51706(CYB5R1)
            MMU: 109754(Cyb5r3) 72017(Cyb5r1)
            RNO: 25035(Cyb5r3)
            CFA: 474479(CYB5R3)
            GGA: 418220(RCJMB04_4p8)
            XLA: 380169(dia1)
            DRE: 336553(dia1)
            CEL: T05H4.4 T05H4.5
            ATH: AT5G17770(ATCBR)
            OSA: 4327126 4327480 4339153
            CME: CMS286C
            SCE: YIL043C(CBR1) YKL150W(MCR1)
            AGO: AGOS_ACR054C AGOS_ADL087W
            PIC: PICST_44816(CBR2) PICST_45522(CBR3) PICST_68997(CBR1)
            CGR: CAGL0E06424g CAGL0L00847g
            SPO: SPAC17H9.12c SPCC970.03
            ANI: AN0432.2 AN8920.2
            AFM: AFUA_1G04540 AFUA_3G03970 AFUA_5G10060
            AOR: AO090001000630 AO090003000873 AO090011000149
            CNE: CNM00240
            DDI: DDBDRAFT_0218707
            PFA: PF13_0353
            TAN: TA13765
            TBR: Tb11.01.7190 Tb11.02.1230 Tb11.47.0018 Tb927.5.1470
                 Tb927.7.2700 Tb927.7.2710
            TCR: 511047.40 511817.40 511859.170
            LMA: LmjF13.1060 LmjF15.0050 LmjF22.0770 LmjF22.0780
            NOC: Noc_1586
            NPH: NP1230A
STRUCTURES  PDB: 1I7P  1IB0  1NDH  1QX4  1UMK  2EIX  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.2.2
            ExPASy - ENZYME nomenclature database: 1.6.2.2
            ExplorEnz - The Enzyme Database: 1.6.2.2
            ERGO genome analysis and discovery system: 1.6.2.2
            BRENDA, the Enzyme Database: 1.6.2.2
            CAS: 9032-25-1
///
ENTRY       EC 1.6.2.3        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a heme protein as acceptor
COMMENT     Deleted entry: cytochrome reductase (NADPH) (EC 1.6.2.3 created
            1972, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.2.3
            ExPASy - ENZYME nomenclature database: 1.6.2.3
            ExplorEnz - The Enzyme Database: 1.6.2.3
            ERGO genome analysis and discovery system: 1.6.2.3
            BRENDA, the Enzyme Database: 1.6.2.3
///
ENTRY       EC 1.6.2.4                  Enzyme
NAME        NADPH---hemoprotein reductase;
            CPR;
            FAD-cytochrome c reductase;
            NADP---cytochrome c reductase;
            NADP---cytochrome reductase;
            NADPH-dependent cytochrome c reductase;
            NADPH:P-450 reductase;
            NADPH:ferrihemoprotein oxidoreductase;
            NADPH---cytochrome P-450 oxidoreductase;
            NADPH---cytochrome c oxidoreductase;
            NADPH---cytochrome c reductase;
            NADPH---cytochrome p-450 reductase;
            NADPH---ferricytochrome c oxidoreductase;
            NADPH---ferrihemoprotein reductase;
            TPNH2 cytochrome c reductase;
            TPNH-cytochrome c reductase;
            aldehyde reductase (NADPH-dependent);
            cytochrome P-450 reductase;
            cytochrome c reductase (reduced nicotinamide adenine dinucleotide
            phosphate, NADPH, NADPH-dependent);
            dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome c
            reductase;
            ferrihemoprotein P-450 reductase;
            reduced nicotinamide adenine dinucleotide phosphate-cytochrome c
            reductase;
            reductase, cytochrome c (reduced nicotinamide adenine dinucleotide
            phosphate)
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a heme protein as acceptor
SYSNAME     NADPH:hemoprotein oxidoreductase
REACTION    NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
ALL_REAC    (other) R00106
SUBSTRATE   NADPH [CPD:C00005];
            H+ [CPD:C00080];
            oxidized hemoprotein
PRODUCT     NADP+ [CPD:C00006];
            reduced hemoprotein
COFACTOR    FAD [CPD:C00016];
            FMN [CPD:C00061]
COMMENT     A flavoprotein (FMN, FAD) containing both FMN and FAD. The number n
            in the equation is 1 if the hemoprotein undergoes a 2-electron
            reduction, and is 2 if it undergoes a 1-electron reduction. The
            enzyme catalyses the reduction of the heme-thiolate-dependent
            monooxygenases, such as EC 1.14.14.1, unspecific monooxygenase and
            reduction of EC 1.14.99.3, heme oxygenase (decyclizing). It is part
            of the microsomal hydroxylating system. It also reduces cytochrome
            b5 and cytochrome c.
REFERENCE   1
  AUTHORS   Haas, E., Horecker, B.L. and Hogness, T.R.
  TITLE     The enzymatic reduction of cytochrome c, cytochrome c reductase.
  JOURNAL   J. Biol. Chem. 136 (1940) 747-774.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2
  AUTHORS   Horecker, B.L.
  TITLE     Triphosphopyridine nucleotide-cytochrome c reductase in liver.
  JOURNAL   J. Biol. Chem. 183 (1950) 593-605.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:4389465]
  AUTHORS   Lu AY, Junk KW, Coon MJ.
  TITLE     Resolution of the cytochrome P-450-containing omega-hydroxylation
            system of liver microsomes into three components.
  JOURNAL   J. Biol. Chem. 244 (1969) 3714-21.
  ORGANISM  rabbit
REFERENCE   4  [PMID:14275154]
  AUTHORS   GIBSON QH, PALMER G, WHARTON DC.
  TITLE     STUDIES ON THE MECHANISM OF MICROSOMAL TRIPHOSPHOPYRIDINE
            NUCLEOTIDE-CYTOCHROME C REDUCTASE.
  JOURNAL   J. Biol. Chem. 240 (1965) 921-31.
  ORGANISM  pig [GN:ssc]
REFERENCE   5  [PMID:14007123]
  AUTHORS   WILLIAMS CH Jr, KAMIN H.
  TITLE     Microsomal triphosphopyridine nucleotide-cytochrome c reductase of
            liver.
  JOURNAL   J. Biol. Chem. 237 (1962) 587-95.
  ORGANISM  pig [GN:ssc]
REFERENCE   6  [PMID:4378860]
  AUTHORS   Masters BS, Bilimoria MH, Kamin H, Gibson QH.
  TITLE     The mechanism of 1- and 2-electron transfers catalyzed by reduced
            triphosphopyridine nucleotide-cytochrome c reductase.
  JOURNAL   J. Biol. Chem. 240 (1965) 4081-8.
  ORGANISM  pig [GN:ssc]
REFERENCE   7  [PMID:8589067]
  AUTHORS   Sevrioukova IF, Peterson JA.
  TITLE     NADPH-P-450 reductase: structural and functional comparisons of the
            eukaryotic and prokaryotic isoforms.
  JOURNAL   Biochimie. 77 (1995) 562-72.
  ORGANISM  human [GN:hsa]
REFERENCE   8  [PMID:9237990]
  AUTHORS   Wang M, Roberts DL, Paschke R, Shea TM, Masters BS, Kim JJ.
  TITLE     Three-dimensional structure of NADPH-cytochrome P450 reductase:
            prototype for FMN- and FAD-containing enzymes.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 8411-6.
  ORGANISM  rat [GN:rno]
REFERENCE   9  [PMID:11329262]
  AUTHORS   Munro AW, Noble MA, Robledo L, Daff SN, Chapman SK.
  TITLE     Determination of the redox properties of human NADPH-cytochrome P450
            reductase.
  JOURNAL   Biochemistry. 40 (2001) 1956-63.
  ORGANISM  human [GN:hsa], rabbit
REFERENCE   10 [PMID:11329262]
  AUTHORS   Munro AW, Noble MA, Robledo L, Daff SN, Chapman SK.
  TITLE     Determination of the redox properties of human NADPH-cytochrome P450
            reductase.
  JOURNAL   Biochemistry. 40 (2001) 1956-63.
  ORGANISM  human [GN:hsa], rabbit
REFERENCE   11 [PMID:12773143]
  AUTHORS   Gutierrez A, Grunau A, Paine M, Munro AW, Wolf CR, Roberts GC,
            Scrutton NS.
  TITLE     Electron transfer in human cytochrome P450 reductase.
  JOURNAL   Biochem. Soc. Trans. 31 (2003) 497-501.
  ORGANISM  human [GN:hsa]
REFERENCE   12 [PMID:12773143]
  AUTHORS   Gutierrez A, Grunau A, Paine M, Munro AW, Wolf CR, Roberts GC,
            Scrutton NS.
  TITLE     Electron transfer in human cytochrome P450 reductase.
  JOURNAL   Biochem. Soc. Trans. 31 (2003) 497-501.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K00327  NADPH-ferrihemoprotein reductase
GENES       HSA: 5447(POR)
            PTR: 463481(POR)
            MMU: 18984(Por)
            RNO: 29441(Por)
            CFA: 489816(LOC489816)
            GGA: 417520(LOC417520)
            XLA: 379707(npr)
            SPU: 594665(LOC594665)
            DME: Dmel_CG11567(Cpr) Dmel_CG13667
            CEL: K10D2.6(emb-8)
            ATH: AT4G24520(ATR1) AT4G30210(ATR2)
            OSA: 4347838
            SCE: YHR042W(NCP1)
            AGO: AGOS_AAL121C
            PIC: PICST_55602(TAH13) PICST_77786
            CAL: CaO19.4076
            CGR: CAGL0D04114g
            SPO: SPAC1296.06 SPBC29A10.01(ccr1)
            ANI: AN0595.2 AN6835.2
            AFM: AFUA_2G07940 AFUA_3G09220 AFUA_6G10990
            AOR: AO090001000445 AO090023000520
            ANG: An08g07840(cprA)
            CNE: CND01320
            UMA: UM06273.1
            DDI: DDBDRAFT_0190667
            PFA: PFI1140w
            CPV: cgd4_2700
            CHO: Chro.40304
            TAN: TA04090
            TPV: TP03_0092
            TET: TTHERM_01013300 TTHERM_01044750
            TBR: Tb09.211.4110 Tb11.01.0170 Tb11.02.5420 Tb927.4.1950
            TCR: 506585.70
            LMA: LmjF28.1240 LmjF34.2670
            REH: H16_B1009
            RME: Rmet_3467
            BUR: Bcep18194_C6803
            BJA: blr2882
            BRA: BRADO3794
            BBT: BBta_4136
            RPD: RPD_1820
            ELI: ELI_00100
            BSU: BG12299(yrhJ) BG12871(yetO)
            BAN: BA3221(cypD)
            BAR: GBAA3221(cypD)
            BAT: BAS2993
            BCE: BC3211
            BCA: BCE_3239(cypD)
            BCZ: BCZK2921
            BTK: BT9727_2981
            BLI: BL02398(cypE)
            BLD: BLi02848(yrhJ)
            BPU: BPUM_1680(yrhJ)
            RHA: RHA1_ro01798
            FAL: FRAAL5324(narB)
            SEN: SACE_4205(cypD)
            HMA: rrnAC0073(cyc) rrnAC3312(cyp1)
STRUCTURES  PDB: 1AMO  1B1C  1J9Z  1JA0  1JA1  1YQO  1YQP  2BF4  2BN4  2BPO  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.2.4
            ExPASy - ENZYME nomenclature database: 1.6.2.4
            ExplorEnz - The Enzyme Database: 1.6.2.4
            ERGO genome analysis and discovery system: 1.6.2.4
            BRENDA, the Enzyme Database: 1.6.2.4
            CAS: 9023-03-4
///
ENTRY       EC 1.6.2.5                  Enzyme
NAME        NADPH---cytochrome-c2 reductase;
            cytochrome c2 reductase (reduced nicotinamide adenine dinucleotide
            phosphate);
            cytochrome c2 reductase (reduced nicotinamide adinine dinucleotide
            phosphate, NADPH)
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a heme protein as acceptor
SYSNAME     NADPH:ferricytochrome-c2 oxidoreductase
REACTION    NADPH + 2 ferricytochrome c2 = NADP+ + H+ + 2 ferrocytochrome c2
            [RN:R00108]
ALL_REAC    R00108
SUBSTRATE   NADPH [CPD:C00005];
            ferricytochrome c2 [CPD:C00997]
PRODUCT     NADP+ [CPD:C00006];
            H+ [CPD:C00080];
            ferrocytochrome c2 [CPD:C01000]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:4385431]
  AUTHORS   Sabo DJ, Orlando JA.
  TITLE     Isolation, purification, and some properties of reduced nicotinamide
            adenine dinucleotide phosphate-cytochrome C2 reductase from
            Rhodopseudomonas spheroides.
  JOURNAL   J. Biol. Chem. 243 (1968) 3742-9.
  ORGANISM  Rhodopseudomonas spheroides
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.2.5
            ExPASy - ENZYME nomenclature database: 1.6.2.5
            ExplorEnz - The Enzyme Database: 1.6.2.5
            ERGO genome analysis and discovery system: 1.6.2.5
            BRENDA, the Enzyme Database: 1.6.2.5
            CAS: 37256-32-9
///
ENTRY       EC 1.6.2.6                  Enzyme
NAME        leghemoglobin reductase;
            ferric leghemoglobin reductase
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a heme protein as acceptor
SYSNAME     NAD(P)H:ferrileghemoglobin oxidoreductase
REACTION    NAD(P)H + H+ + 2 ferrileghemoglobin = NAD(P)+ + 2 ferroleghemoglobin
            [RN:R00101 R00109]
ALL_REAC    R00101 R00109
SUBSTRATE   NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            ferrileghemoglobin [CPD:C02683]
PRODUCT     NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            ferroleghemoglobin [CPD:C02685]
REFERENCE   1  [PMID:6539095]
  AUTHORS   Saari LL, Klucas RV.
  TITLE     Ferric leghemoglobin reductase from soybean root nodules.
  JOURNAL   Arch. Biochem. Biophys. 231 (1984) 102-13.
  ORGANISM  Glycine max [GN:egma]
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.2.6
            ExPASy - ENZYME nomenclature database: 1.6.2.6
            ExplorEnz - The Enzyme Database: 1.6.2.6
            ERGO genome analysis and discovery system: 1.6.2.6
            BRENDA, the Enzyme Database: 1.6.2.6
            CAS: 60440-35-9
///
ENTRY       EC 1.6.3.1                  Enzyme
NAME        NAD(P)H oxidase;
            THOX2;
            ThOX;
            dual oxidase;
            p138tox;
            thyroid NADPH oxidase;
            thyroid oxidase;
            thyroid oxidase 2;
            NADPH oxidase
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With oxygen as acceptor
SYSNAME     NAD(P)H:oxygen oxidoreductase
REACTION    NAD(P)H + H+ + O2 = NAD(P)+ + H2O2 [RN:R07171 R07172]
ALL_REAC    R07171 R07172
SUBSTRATE   NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O2 [CPD:C00027]
COMMENT     Requires FAD, heme and calcium. When calcium is present, this
            transmembrane glycoprotein generates H2O2 by transfering electrons
            from intracellular NAD(P)H to extracellular molecular oxygen. The
            electron bridge within the enzyme contains one molecule of FAD and
            probably two heme groups. This flavoprotein is expressed at the
            apical membrane of thyrocytes, and provides H2O2 for the thyroid
            peroxidase-catalysed biosynthesis of thyroid hormones.
REFERENCE   1  [PMID:12110737]
  AUTHORS   Moreno JC, Bikker H, Kempers MJ, van Trotsenburg AS, Baas F, de
            Vijlder JJ, Vulsma T, Ris-Stalpers C.
  TITLE     Inactivating mutations in the gene for thyroid oxidase 2 (THOX2) and
            congenital hypothyroidism.
  JOURNAL   N. Engl. J. Med. 347 (2002) 95-102.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:11822874]
  AUTHORS   De Deken X, Wang D, Dumont JE, Miot F.
  TITLE     Characterization of ThOX proteins as components of the thyroid
            H(2)O(2)-generating system.
  JOURNAL   Exp. Cell. Res. 273 (2002) 187-96.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:10806195]
  AUTHORS   De Deken X, Wang D, Many MC, Costagliola S, Libert F, Vassart G,
            Dumont JE, Miot F.
  TITLE     Cloning of two human thyroid cDNAs encoding new members of the NADPH
            oxidase family.
  JOURNAL   J. Biol. Chem. 275 (2000) 23227-33.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:10601291]
  AUTHORS   Dupuy C, Ohayon R, Valent A, Noel-Hudson MS, Deme D, Virion A.
  TITLE     Purification of a novel flavoprotein involved in the thyroid NADPH
            oxidase. Cloning of the porcine and human cdnas.
  JOURNAL   J. Biol. Chem. 274 (1999) 37265-9.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:10401672]
  AUTHORS   Leseney AM, Deme D, Legue O, Ohayon R, Chanson P, Sales JP, Pires de
            Carvalho D, Dupuy C, Virion A.
  TITLE     Biochemical characterization of a Ca2+/NAD(P)H-dependent H2O2
            generator in human thyroid tissue.
  JOURNAL   Biochimie. 81 (1999) 373-80.
  ORGANISM  human [GN:hsa]
REFERENCE   6  [PMID:1995628]
  AUTHORS   Dupuy C, Virion A, Ohayon R, Kaniewski J, Deme D, Pommier J.
  TITLE     Mechanism of hydrogen peroxide formation catalyzed by NADPH oxidase
            in thyroid plasma membrane.
  JOURNAL   J. Biol. Chem. 266 (1991) 3739-43.
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.3.1
            ExPASy - ENZYME nomenclature database: 1.6.3.1
            ExplorEnz - The Enzyme Database: 1.6.3.1
            ERGO genome analysis and discovery system: 1.6.3.1
            BRENDA, the Enzyme Database: 1.6.3.1
///
ENTRY       EC 1.6.4.1        Obsolete  Enzyme
NAME        Transferred to 1.8.1.6
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a disulfide as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.8.1.6 cystine reductase (EC 1.6.4.1
            created 1961, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.4.1
            ExPASy - ENZYME nomenclature database: 1.6.4.1
            ExplorEnz - The Enzyme Database: 1.6.4.1
            ERGO genome analysis and discovery system: 1.6.4.1
            BRENDA, the Enzyme Database: 1.6.4.1
///
ENTRY       EC 1.6.4.2        Obsolete  Enzyme
NAME        Transferred to 1.8.1.7
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a disulfide as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.8.1.7 glutathione-disulfide reductase
            (EC 1.6.4.2 created 1961, modified 1989, deleted 2002)
STRUCTURES  PDB: 1ALG  1BWC  1DNC  1GER  1GES  1GET  1GEU  1GRA  1GRB  1GRE  
                 1GRF  1GRG  1GRT  1GSN  1K4Q  1XAN  2GRT  3GRS  3GRT  4GR1  
                 4GRT  5GRT  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.4.2
            ExPASy - ENZYME nomenclature database: 1.6.4.2
            ExplorEnz - The Enzyme Database: 1.6.4.2
            ERGO genome analysis and discovery system: 1.6.4.2
            BRENDA, the Enzyme Database: 1.6.4.2
///
ENTRY       EC 1.6.4.3        Obsolete  Enzyme
NAME        Transferred to 1.8.1.4
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a disulfide as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.8.1.4, dihydrolipoyl dehydrogenase (EC
            1.6.4.3 created 1961, modified 1976, deleted 1983)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.4.3
            ExPASy - ENZYME nomenclature database: 1.6.4.3
            ExplorEnz - The Enzyme Database: 1.6.4.3
            ERGO genome analysis and discovery system: 1.6.4.3
            BRENDA, the Enzyme Database: 1.6.4.3
///
ENTRY       EC 1.6.4.4        Obsolete  Enzyme
NAME        Transferred to 1.8.1.8
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a disulfide as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.8.1.8 protein-disulfide reductase (EC
            1.6.4.4 created 1965, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.4.4
            ExPASy - ENZYME nomenclature database: 1.6.4.4
            ExplorEnz - The Enzyme Database: 1.6.4.4
            ERGO genome analysis and discovery system: 1.6.4.4
            BRENDA, the Enzyme Database: 1.6.4.4
///
ENTRY       EC 1.6.4.5        Obsolete  Enzyme
NAME        Transferred to 1.8.1.9
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a disulfide as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.8.1.9 thioredoxin-disulfide reductase
            (EC 1.6.4.5 created 1972, deleted 2002)
STRUCTURES  PDB: 1CL0  1F6M  1H6V  1TDE  1TDF  1TRB  1VDC  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.4.5
            ExPASy - ENZYME nomenclature database: 1.6.4.5
            ExplorEnz - The Enzyme Database: 1.6.4.5
            ERGO genome analysis and discovery system: 1.6.4.5
            BRENDA, the Enzyme Database: 1.6.4.5
///
ENTRY       EC 1.6.4.6        Obsolete  Enzyme
NAME        Transferred to 1.8.1.10
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a disulfide as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.8.1.10 CoA-glutathione reductase (EC
            1.6.4.6 created 1972, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.4.6
            ExPASy - ENZYME nomenclature database: 1.6.4.6
            ExplorEnz - The Enzyme Database: 1.6.4.6
            ERGO genome analysis and discovery system: 1.6.4.6
            BRENDA, the Enzyme Database: 1.6.4.6
///
ENTRY       EC 1.6.4.7        Obsolete  Enzyme
NAME        Transferred to 1.8.1.11
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a disulfide as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.8.1.11 asparagusate reductase (EC
            1.6.4.7 created 1978, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.4.7
            ExPASy - ENZYME nomenclature database: 1.6.4.7
            ExplorEnz - The Enzyme Database: 1.6.4.7
            ERGO genome analysis and discovery system: 1.6.4.7
            BRENDA, the Enzyme Database: 1.6.4.7
///
ENTRY       EC 1.6.4.8        Obsolete  Enzyme
NAME        Transferred to 1.8.1.12
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a disulfide as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.8.1.12 trypanothione-disulfide reductase
            (EC 1.6.4.8 created 1989, deleted 2002)
STRUCTURES  PDB: 1AOG  1BZL  1FEA  1FEB  1FEC  1GXF  1TYP  1TYT  2TPR  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.4.8
            ExPASy - ENZYME nomenclature database: 1.6.4.8
            ExplorEnz - The Enzyme Database: 1.6.4.8
            ERGO genome analysis and discovery system: 1.6.4.8
            BRENDA, the Enzyme Database: 1.6.4.8
///
ENTRY       EC 1.6.4.9        Obsolete  Enzyme
NAME        Transferred to 1.8.1.13
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a disulfide as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.8.1.13 bis-gamma-glutamylcystine
            reductase (EC 1.6.4.9 created 1992, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.4.9
            ExPASy - ENZYME nomenclature database: 1.6.4.9
            ExplorEnz - The Enzyme Database: 1.6.4.9
            ERGO genome analysis and discovery system: 1.6.4.9
            BRENDA, the Enzyme Database: 1.6.4.9
///
ENTRY       EC 1.6.4.10       Obsolete  Enzyme
NAME        Transferred to 1.8.1.14
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a disulfide as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.8.1.14 CoA-disulfide reductase (EC
            1.6.4.10 created 1992, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.4.10
            ExPASy - ENZYME nomenclature database: 1.6.4.10
            ExplorEnz - The Enzyme Database: 1.6.4.10
            ERGO genome analysis and discovery system: 1.6.4.10
            BRENDA, the Enzyme Database: 1.6.4.10
///
ENTRY       EC 1.6.5.1        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a quinone or similar compound as acceptor
COMMENT     Deleted entry: quinone reductase (EC 1.6.5.1 created 1961, deleted
            1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.5.1
            ExPASy - ENZYME nomenclature database: 1.6.5.1
            ExplorEnz - The Enzyme Database: 1.6.5.1
            ERGO genome analysis and discovery system: 1.6.5.1
            BRENDA, the Enzyme Database: 1.6.5.1
///
ENTRY       EC 1.6.5.2                  Enzyme
NAME        NAD(P)H dehydrogenase (quinone);
            menadione reductase;
            phylloquinone reductase;
            quinone reductase;
            dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate,
            quinone);
            DT-diaphorase;
            flavoprotein NAD(P)H-quinone reductase;
            menadione oxidoreductase;
            NAD(P)H dehydrogenase;
            NAD(P)H menadione reductase;
            NAD(P)H-quinone dehydrogenase;
            NAD(P)H-quinone oxidoreductase;
            NAD(P)H: (quinone-acceptor)oxidoreductase;
            NAD(P)H: menadione oxidoreductase;
            NADH-menadione reductase;
            naphthoquinone reductase;
            p-benzoquinone reductase;
            reduced NAD(P)H dehydrogenase;
            viologen accepting pyridine nucleotide oxidoreductase;
            vitamin K reductase;
            diaphorase;
            reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase;
            vitamin-K reductase;
            NAD(P)H2 dehydrogenase (quinone);
            NQO1;
            QR1;
            NAD(P)H:(quinone-acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a quinone or similar compound as acceptor
SYSNAME     NAD(P)H:quinone oxidoreductase
REACTION    NAD(P)H + H+ + a quinone = NAD(P)+ + a hydroquinone [RN:R07358
            R07359]
ALL_REAC    R07358 > R03643;
            R07359
SUBSTRATE   NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            quinone [CPD:C00472]
PRODUCT     NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            hydroquinone [CPD:C00530]
COFACTOR    FAD [CPD:C00016]
INHIBITOR   Dicumarol [CPD:C00796]
COMMENT     A flavoprotein. The enzyme catalyses a two-electron reduction and
            has a preference for short-chain acceptor quinones, such as
            ubiquinone, benzoquinone, juglone and duroquinone [6]. The animal,
            but not the plant, form of the enzyme is inhibited by dicoumarol.
REFERENCE   1  [PMID:4171422]
  AUTHORS   Di Prisco G, Casola L, Giuditta A.
  TITLE     Purification and properties of a soluble reduced
            nicotinamide-adenine dinucleotide (phosphate) dehydrogenase from the
            hepatopancreas of Octopus vulgaris.
  JOURNAL   Biochem. J. 105 (1967) 455-60.
  ORGANISM  Octopus vulgaris
REFERENCE   2  [PMID:13705804]
  AUTHORS   GIUDITTA A, STRECKER HJ.
  TITLE     Purification and some properties of a brain diaphorase.
  JOURNAL   Biochim. Biophys. Acta. 48 (1961) 10-9.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:13765127]
  AUTHORS   MAERKI F, MARTIUS C.
  TITLE     [Vitamin K reductase, preparation and properties.]
  JOURNAL   Biochem. Z. 333 (1960) 111-35.
REFERENCE   4
  AUTHORS   Misaka, E. and Nakanishi, K.
  TITLE     Studies on menadione reductase of bakers' yeast. I. Purification,
            crystallization and some properties.
  JOURNAL   J. Biochem. (Tokyo) 53 (1963) 465-471.
  ORGANISM  dog [GN:cfa], Mycobactirium phlei, Escherichia coli [GN:eco],
            Achromobacter fisheri, Streptococcus fatcalis, Saccharomyces
            cerevisiae [GN:sce]
REFERENCE   5  [PMID:13846011]
  AUTHORS   WOSILAIT WD.
  TITLE     The reduction of vitamin K1 by an enzyme from dog liver.
  JOURNAL   J. Biol. Chem. 235 (1960) 1196-201.
  ORGANISM  dog [GN:cfa]
REFERENCE   6  [PMID:12226388]
  AUTHORS   Sparla F, Tedeschi G, Trost P.
  TITLE     NAD(P)H:(Quinone-Acceptor) Oxidoreductase of Tobacco Leaves Is a
            Flavin Mononucleotide-Containing Flavoenzyme.
  JOURNAL   Plant. Physiol. 112 (1996) 249-258.
  ORGANISM  Nicotiana tabacum
REFERENCE   7  [PMID:9485311]
  AUTHORS   Braun M, Bungert S, Friedrich T.
  TITLE     Characterization of the overproduced NADH dehydrogenase fragment of
            the NADH:ubiquinone oxidoreductase (complex I) from Escherichia
            coli.
  JOURNAL   Biochemistry. 37 (1998) 1861-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   8  [PMID:10683249]
  AUTHORS   Jaiswal AK.
  TITLE     Characterization and partial purification of microsomal
            NAD(P)H:quinone oxidoreductases.
  JOURNAL   Arch. Biochem. Biophys. 375 (2000) 62-8.
  ORGANISM  rat [GN:rno]
REFERENCE   9  [PMID:7568029]
  AUTHORS   Li R, Bianchet MA, Talalay P, Amzel LM.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 8846-50.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K00355  NAD(P)H dehydrogenase (quinone)
GENES       HSA: 1728(NQO1)
            PTR: 468012(NQO1)
            MMU: 18104(Nqo1)
            RNO: 24314(Nqo1)
            CFA: 610935(NQO1)
            DRE: 322506(nqo1)
            ECW: EcE24377A_1122(wrbA)
            ECX: EcHS_A1117(wrbA)
            ECA: ECA0951
            HSO: HS_0336(kefF) HS_0573
            XCB: XC_0060
            XAC: XAC2229
            PAE: PA1224 PA1225 PA4975
            PAU: PA14_48440 PA14_65760
            PAP: PSPA7_4560(wrbA)
            PPU: PP_3720
            PSB: Psyr_0122 Psyr_3797
            PFL: PFL_2716 PFL_3429
            PFO: Pfl_3534
            PEN: PSEEN2157 PSEEN2559 PSEEN3245
            PMY: Pmen_3208
            CBD: COXBU7E912_0408(wrbA)
            CSA: Csal_0147
            CVI: CV_0290 CV_0530
            RSO: RSc3097(RS00550)
            REU: Reut_C6287
            REH: H16_A0616 H16_B2315
            RME: Rmet_4021
            BMA: BMAA1893
            BMV: BMASAVP1_0903
            BML: BMA10299_1191
            BMN: BMA10247_A2166
            BXE: Bxe_B2110
            BVI: Bcep1808_4156
            BUR: Bcep18194_B2332
            BCN: Bcen_4596
            BCH: Bcen2424_3767
            BAM: Bamb_5496
            BPS: BPSS0188
            BPM: BURPS1710b_A1711
            BPL: BURPS1106A_A0261
            BPD: BURPS668_A0353
            RFR: Rfer_2434
            MPT: Mpe_A3318
            MMS: mma_0890 mma_1556
            AZO: azo1477(drgA) azo1583(nqo1)
            HPA: HPAG1_0613
            PUB: SAR11_1255
            MLO: mll7814
            SME: SMc03185
            RLE: RL2909
            BOV: BOV_1014(wrbA)
            BRA: BRADO5589
            BBT: BBta_6111
            RPA: RPA4746
            RPB: RPB_0823
            RPC: RPC_0109
            RSP: RSP_3025
            RSH: Rsph17029_3569
            RRU: Rru_A1713 Rru_A3066
            BAN: BA1908 BA2239
            BAR: GBAA1908 GBAA2239
            BAA: BA_2412 BA_2744
            BAT: BAS1770 BAS2085
            BCE: BC1835 BC2194 BC4958
            BCA: BCE_2269
            BCZ: BCZK1728(azr) BCZK2023(yvaB) BCZK2056(azr) BCZK3002 BCZK3128
                 BCZK4683
            BTK: BT9727_1750(azr) BT9727_2025(yvaB) BT9727_4666
            BTL: BALH_1689(azr) BALH_2003(yvaB) BALH_2976 BALH_3075 BALH_4491
            BPU: BPUM_0365 BPUM_2597
            OIH: OB3182
            LLM: llmg_0123(acpD)
            SMU: SMU.1420
            SSA: SSA_0047 SSA_0903
            MAV: MAV_3849(wrbA)
            MSM: MSMEG_2375(wrbA) MSMEG_5564
            RHA: RHA1_ro06352
            FRA: Francci3_2561
            FAL: FRAAL6868
            MAC: MA0326
            MBA: Mbar_A1308
            MMA: MM_1581
STRUCTURES  PDB: 2F1O  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.5.2
            ExPASy - ENZYME nomenclature database: 1.6.5.2
            ExplorEnz - The Enzyme Database: 1.6.5.2
            ERGO genome analysis and discovery system: 1.6.5.2
            BRENDA, the Enzyme Database: 1.6.5.2
            CAS: 9032-20-6
///
ENTRY       EC 1.6.5.3                  Enzyme
NAME        NADH dehydrogenase (ubiquinone);
            ubiquinone reductase;
            type 1 dehydrogenase;
            complex 1 dehydrogenase;
            coenzyme Q reductase;
            complex I (electron transport chain);
            complex I (mitochondrial electron transport);
            complex I (NADH:Q1 oxidoreductase);
            dihydronicotinamide adenine dinucleotide-coenzyme Q reductase;
            DPNH-coenzyme Q reductase;
            DPNH-ubiquinone reductase;
            mitochondrial electron transport complex 1;
            mitochondrial electron transport complex I;
            NADH coenzyme Q1 reductase;
            NADH-coenzyme Q oxidoreductase;
            NADH-coenzyme Q reductase;
            NADH-CoQ oxidoreductase;
            NADH-CoQ reductase;
            NADH-ubiquinone reductase;
            NADH-ubiquinone oxidoreductase;
            NADH-ubiquinone-1 reductase;
            reduced nicotinamide adenine dinucleotide-coenzyme Q reductase;
            NADH:ubiquinone oxidoreductase complex;
            NADH-Q6 oxidoreductase;
            electron transfer complex I;
            NADH2 dehydrogenase (ubiquinone)
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a quinone or similar compound as acceptor
SYSNAME     NADH:ubiquinone oxidoreductase
REACTION    NADH + H+ + ubiquinone = NAD+ + ubiquinol [RN:R02163]
ALL_REAC    R02163;
            (other) R02166
SUBSTRATE   NADH [CPD:C00004];
            H+ [CPD:C00080];
            ubiquinone [CPD:C00399]
PRODUCT     NAD+ [CPD:C00003];
            ubiquinol [CPD:C00390]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023];
            Sulfur [CPD:C00087];
            Iron-sulfur [CPD:C00824]
COMMENT     A flavoprotein (FAD) containing iron-sulfur centres. The complex,
            present in mitochondria, can be degraded to form EC 1.6.99.3, NADH
            dehydrogenase.
REFERENCE   1
  AUTHORS   Hatefi, Y., Ragan, C.I. and Galante, Y.M.
  TITLE     The enzymes and the enzyme complexes of the mitochondrial oxidative
            phosphorylation system.
  JOURNAL   In: Martonosi, A. (Ed.), The Enzymes of Biological Membranes, 2nd
            ed., vol. 4, Plenum Press, New York, 1985, p. 1-70.
PATHWAY     PATH: map00130  Ubiquinone biosynthesis
            PATH: map00190  Oxidative phosphorylation
ORTHOLOGY   KO: K00329  NADH dehydrogenase
            KO: K00330  NADH dehydrogenase I chain A
            KO: K00331  NADH dehydrogenase I chain B
            KO: K00332  NADH dehydrogenase I chain C
            KO: K00333  NADH dehydrogenase I chain D
            KO: K00334  NADH dehydrogenase I chain E
            KO: K00335  NADH dehydrogenase I chain F
            KO: K00336  NADH dehydrogenase I chain G
            KO: K00337  NADH dehydrogenase I chain H
            KO: K00338  NADH dehydrogenase I chain I
            KO: K00339  NADH dehydrogenase I chain J
            KO: K00340  NADH dehydrogenase I chain K
            KO: K00341  NADH dehydrogenase I chain L
            KO: K00342  NADH dehydrogenase I chain M
            KO: K00343  NADH dehydrogenase I chain N
            KO: K03878  NADH dehydrogenase I subunit 1
            KO: K03879  NADH dehydrogenase I subunit 2
            KO: K03880  NADH dehydrogenase I subunit 3
            KO: K03881  NADH dehydrogenase I subunit 4
            KO: K03882  NADH dehydrogenase I subunit 4L
            KO: K03883  NADH dehydrogenase I subunit 5
            KO: K03884  NADH dehydrogenase I subunit 6
            KO: K03934  NADH dehydrogenase (ubiquinone) Fe-S protein 1
            KO: K03935  NADH dehydrogenase (ubiquinone) Fe-S protein 2
            KO: K03936  NADH dehydrogenase (ubiquinone) Fe-S protein 3
            KO: K03937  NADH dehydrogenase (ubiquinone) Fe-S protein 4
            KO: K03938  NADH dehydrogenase (ubiquinone) Fe-S protein 5
            KO: K03939  NADH dehydrogenase (ubiquinone) Fe-S protein 6
            KO: K03940  NADH dehydrogenase (ubiquinone) Fe-S protein 7
            KO: K03941  NADH dehydrogenase (ubiquinone) Fe-S protein 8
            KO: K03942  NADH dehydrogenase (ubiquinone) flavoprotein 1
            KO: K03943  NADH dehydrogenase (ubiquinone) flavoprotein 2
            KO: K03944  NADH dehydrogenase (ubiquinone) flavoprotein 3
            KO: K03945  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 1
            KO: K03946  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 2
            KO: K03947  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 3
            KO: K03948  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 4
            KO: K03949  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 5
            KO: K03950  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 6
            KO: K03951  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 7
            KO: K03952  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 8
            KO: K03953  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 9
            KO: K03954  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 10
            KO: K03955  NADH dehydrogenase (ubiquinone) 1 alpha/beta subcomplex
                        1
            KO: K03956  NADH-ubiquinone oxidoreductase subunit
            KO: K03957  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 1
            KO: K03958  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 2
            KO: K03959  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 3
            KO: K03960  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 4
            KO: K03961  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 5
            KO: K03962  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 6
            KO: K03963  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 7
            KO: K03964  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 8
            KO: K03965  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 9
            KO: K03966  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 10
            KO: K03967  NADH dehydrogenase (ubiquinone) 1 subcomplex unknown 1
            KO: K03968  NADH dehydrogenase (ubiquinone) 1 subcomplex unknown 2
            KO: K05572  NADH dehydrogenase I subunit 1
            KO: K05573  NADH dehydrogenase I subunit 2
            KO: K05574  NADH dehydrogenase I subunit 3
            KO: K05575  NADH dehydrogenase I subunit 4
            KO: K05576  NADH dehydrogenase I subunit 4L
            KO: K05577  NADH dehydrogenase I subunit 5
            KO: K05578  NADH dehydrogenase I subunit 6
            KO: K05579  NADH dehydrogenase I subunit 7
            KO: K05580  NADH dehydrogenase I subunit I
            KO: K05581  NADH dehydrogenase I subunit J
            KO: K05582  NADH dehydrogenase I subunit K
            KO: K05583  NADH dehydrogenase I subunit L
            KO: K05584  NADH dehydrogenase I subunit M
            KO: K05585  NADH dehydrogenase I subunit N
            KO: K05586  diaphorase subunit of the bidirectional hydrogenase
            KO: K05587  diaphorase subunit of the bidirectional hydrogenase
            KO: K05588  diaphorase subunit of the bidirectional hydrogenase
GENES       HSA: 126328(NDUFA11) 374291(NDUFS7) 4535(ND1) 4536(ND2) 4537(ND3)
                 4538(ND4) 4539(ND4L) 4540(ND5) 4541(ND6) 4694(NDUFA1)
                 4695(NDUFA2) 4696(NDUFA3) 4697(NDUFA4) 4698(NDUFA5)
                 4700(NDUFA6) 4701(NDUFA7) 4702(NDUFA8) 4704(NDUFA9)
                 4705(NDUFA10) 4706(NDUFAB1) 4707(NDUFB1) 4708(NDUFB2)
                 4709(NDUFB3) 4710(NDUFB4) 4711(NDUFB5) 4712(NDUFB6)
                 4713(NDUFB7) 4714(NDUFB8) 4715(NDUFB9) 4716(NDUFB10)
                 4717(NDUFC1) 4718(NDUFC2) 4719(NDUFS1) 4720(NDUFS2)
                 4722(NDUFS3) 4723(NDUFV1) 4724(NDUFS4) 4725(NDUFS5)
                 4726(NDUFS6) 4728(NDUFS8) 4729(NDUFV2) 4731(NDUFV3)
                 51079(NDUFA13) 54539(NDUFB11) 55967(NDUFA12) 56901(NDUFA4L2)
            PTR: 451175(NDUFS3) 451375(NDUFS8) 451766(NDUFA9) 453115(NDUFB1)
                 455295(NDUFV2) 459896(NDUFS1) 460612(NDUFB4) 461878(NDUFS4)
                 462119(NDUFA2) 463686(NDUFA5) 463780(NDUFB2) 464380(NDUFB9)
                 464897(NDUFA8) 468748(NDUFB7) 470696(NDUFA10) 471008(NDUFB5)
                 473588(NDUFB11) 807860(ND5) 807861(ND6) 807863(ND4)
                 807865(ND2) 807867(ND1) 807868(ND4L) 807870(ND3)
            MCC: 641333(NDUFA4) 693506(NDUFS5) 698706(LOC698706)
                 699693(LOC699693) 700718(NDUFAB1) 722578(LOC722578)
            MMU: 104130(Ndufb11) 17716(ND1) 17717(ND2) 17718(ND3) 17719(ND4)
                 17720(ND4L) 17721(ND5) 17722(ND6) 17991(Ndufa2) 17992(Ndufa4)
                 17993(Ndufs4) 17995(Ndufv1) 225887(Ndufs8) 226646(Ndufs2)
                 227197(Ndufs1) 230075(Ndufb6) 239760(EG239760) 407785(Ndufs6)
                 54405(Ndufa1) 66046(Ndufb5) 66091(Ndufa3) 66108(Ndufa9)
                 66218(Ndufb9) 66377(Ndufc1) 66414(Ndufa12) 66416(Ndufa7)
                 66495(Ndufb3) 66916(Ndufb7) 67130(Ndufa6) 67184(Ndufa13)
                 67264(Ndufb8) 67273(Ndufa10) 68194(Ndufb4) 68197(Ndufc2)
                 68198(Ndufb2) 68202(Ndufa5) 68342(Ndufb10) 68349(Ndufs3)
                 68375(Ndufa8) 69875(Ndufa11) 70316(Ndufab1) 72900(Ndufv2)
                 75406(Ndufs7)
            RNO: 25488(Ndufa5) 26193(ND1) 26194(ND2) 26199(ND3) 26200(ND4L)
                 26201(ND4) 26202(ND5) 26203(ND6) 288088(Ndufb4) 289218(Ndufs2)
                 291660(Ndufa2_predicted) 293130(Ndufc2)
                 293453(Ndufab1_predicted) 293652(Ndufs8_predicted)
                 293655(Ndufv1) 293991(Ndufb8_predicted) 29478(Ndufs6)
                 294964(Ndufb5_predicted) 295923(Ndufs3_predicted)
                 296658(Ndufa8) 297990(Ndufb6_predicted)
                 299643(Ndufa7_predicted) 299954(Ndufb9_predicted)
                 301123(Ndufa11) 301427(Ndufb3_predicted) 301458(Ndufs1)
                 314071(Ndufa10) 315167(Ndufa6_predicted) 316632(LOC316632)
                 361385(Ndufb7_predicted) 362344(Ndufb2_predicted)
                 362588(Ndufs5b) 362837(Ndufs7) 363441(Ndufa1_predicted)
                 366074(RGD1560451_predicted) 81728(Ndufv2)
            CFA: 474483(NDUFA6) 475094(NDUFB9) 475322(NDUFS5) 475428(NDUFA12)
                 475978(NDUFS3) 476004(NDUFV1) 476659(NDUFA13) 476686(NDUFB7)
                 476722(NDUFA7) 476735(NDUFA11) 476754(NDUFS7) 476794(NDUFC2)
                 477682(NDUFA4) 477718(NDUFA9) 477798(NDUFB8) 478032(NDUFA2)
                 478421(LOC478421) 478577(NDUFB4) 478639(LOC478639)
                 478869(NDUFB3) 478880(NDUFS1) 478981(NDUFS2) 479887(NDUFB10)
                 480204(NDUFV2) 480741(NDUFA8) 480894(NDUFB11)
                 481033(LOC481033) 485505(LOC485505) 488724(LOC488724)
                 607407(NDUFA4L2) 607943(NDUFC1) 608244(NDUFA10)
                 610413(LOC610413) 611480(NDUFA3) 804476(ND1) 804477(ND2)
                 804481(ND3) 804482(ND4L) 804483(ND4) 804484(ND5) 804485(ND6)
            BTA: 281742(DAP13) 282289(NDUFC1) 282290(NDUFV2) 282517(NDUFB8)
                 287014(NDUFV1) 287027(NDUFS8) 287327(NDUFS3) 288380(NDUFS1)
                 326346(b14.7) 327660(NDUFB9) 327665(NDUFB6) 327670(NDUFA6)
                 327673(NDUFA1) 327680(NDUFS4) 327690(NDUFB1) 327691(NDUFS6)
                 327697(NDUFS2) 327698(NDUFA2) 327701(NDUFB10) 327702(NDUFAB1)
                 327704(NDUFA4) 327706(NDUFB4) 327710(NDUFA8) 327713(NDUFB2)
                 327714(NDUFA5) 327717(NDUFV3) 3283877(ND1) 3283878(ND2)
                 3283884(ND3) 3283885(ND4L) 3283886(ND4) 3283887(ND5)
                 3283888(ND6) 338046(NDUFC2) 338057(NDUFS5) 338060(NDUFA10)
                 338061(NDUFB5) 338063(NDUFA7) 338064(NDUFA3) 338065(NDUFB7)
                 338073(NDUFB3) 338079(NDUFS7) 338084(GRIM19) 404161(ESSS)
                 404188(NDUFA9)
            SSC: 808501(ND1) 808502(ND2) 808508(ND3) 808509(ND4L) 808510(ND4)
                 808511(ND5) 808512(ND6)
            GGA: 404751(NDUFC2) 416391(NDUFB6) 416543(NDUFB10) 416571(NDUFAB1)
                 417112(NDUFA8) 417753(NDUFA5) 417907(NDUFA12) 418118(NDUFB2)
                 418541(NDUFV3) 419039(NDUFA9) 420060(NDUFA11) 420065(NDUFA7)
                 420337(NDUFB9) 420976(NDUFS6) 423179(NDUFS3) 423763(NDUFB8)
                 424032(RCJMB04_24e8) 424078(NDUFB3) 424102(NDUFS1)
                 424978(NDUFB5) 426488(NDUFV2) 427897(NDUFA6)
                 430210(RCJMB04_33n14) 768860(NDUFA2) 769492(NDUFS8)
                 769954(NDUFB4) 770724(LOC770724) 770879(LOC770879)
                 771510(NDUFS5) 772135(NDUFA4) 772150(NDUFA1) 807636(ND1)
                 807638(ND3) 807640(ND6) 807642(ND5) 807643(ND4) 807644(ND4L)
                 807645(ND2)
            XLA: 2642076(ND4L) 2642077(ND4) 2642078(ND5) 2642079(ND6)
                 2642085(ND3) 2642086(ND1) 2642087(ND2) 379572(MGC69110)
                 379900(ndufb5) 379907(ndufv1) 379950(ndufb2) 380000(ndufs1)
                 398665(MGC64316) 443927(MGC80253) 447095(MGC85267)
                 447154(MGC85457) 447172(MGC85528) 495159(LOC495159)
                 495365(LOC495365) 495975(LOC495975) 496233(LOC496233)
                 496303(LOC496303) 496350(LOC496350)
            XTR: 3283492(ND1) 3283493(ND2) 3283499(ND3) 3283500(ND4L)
                 3283501(ND4) 3283502(ND5) 3283503(ND6) 394690(ndufs3)
                 394993(MGC76312) 448707(MGC89694) 448777(TEgg077n03.1)
                 496917(ndufa9) 496988(ndufv1) 549920(LOC549920)
            DRE: 140531(ND1) 140532(ND2) 140533(ND3) 140534(ND4) 140535(ND5)
                 140536(ND6) 140538(ND4L) 321951(ndufa10) 338177(zgc:77225)
                 393497(zgc:66391) 393700(zgc:73139) 393703(ndufb10)
                 393720(zgc:73198) 393764(zgc:73329) 393781(zgc:73375)
                 393821(zgc:77820) 393829(ndufb8) 406306(ndufb4) 406413(ndufs8)
                 406726(ndufa4l) 445291(ndufv1) 493605(zgc:92209)
                 550451(ndufs3) 641476(zgc:123301)
            SPU: 2652716(ND1) 2652717(ND2) 2652719(ND4L) 2652723(ND3)
                 2652724(ND4) 2652725(ND5) 2652726(ND6) 577933(LOC577933)
                 578949(LOC578949) 581703(LOC581703) 581848(LOC581848)
                 582177(LOC582177) 582178(LOC582178) 583405(LOC583405)
                 585599(LOC585599) 586214(LOC586214) 587789(LOC587789)
                 587821(LOC587821) 591737(LOC591737) 591836(LOC591836)
                 752184(LOC752184) 756564(LOC756564) 758156(LOC758156)
            DME: Dmel_CG10320 Dmel_CG11455 Dmel_CG12079 Dmel_CG12203
                 Dmel_CG12400 Dmel_CG12859 Dmel_CG15434 Dmel_CG18624
                 Dmel_CG1970 Dmel_CG2014 Dmel_CG2286(ND75) Dmel_CG3192
                 Dmel_CG3621 Dmel_CG3683 Dmel_CG3944(ND23) Dmel_CG5548
                 Dmel_CG5703 Dmel_CG6020 Dmel_CG6343(ND42) Dmel_CG6463
                 Dmel_CG6914 Dmel_CG7712 Dmel_CG8680 Dmel_CG8844 Dmel_CG9140
                 Dmel_CG9172 Dmel_CG9306 Dmel_CG9350 Dmel_CG9762(l(3)neo18) ND1
                 ND2 ND3 ND4 ND4L ND5 ND6
            CEL: C09H10.3(nuo-1) C16A3.5 C18E9.4 C25A1.13 C25H3.9 C33A12.1
                 D2030.4 F16B4.6 F22D6.4 F37C12.3 F44G4.2 F45H10.3 F53F4.10
                 F59C6.5 K04G7.4(nuo-4) K09A9.5(gas-1) ND1 ND2 ND3 ND4 ND4L ND5
                 ND6 T10E9.7(nuo-2) T20H4.5 T26A5.3(tag-99) W01A8.4 W10D5.2
                 Y45G12B.1(nuo-5) Y53G8AL.2 Y54E10BL.5 Y54F10AM.5 Y56A3A.19
                 Y57G11C.12(nuo-3) Y63D3A.7 Y71H2AM.4 Y94H6A.8 ZK809.3
                 ZK973.10(lpd-5)
            ATH: AT1G16700(ATMLO14) AT1G49140 AT1G65290 AT1G79010 AT2G02050
                 AT2G07751 AT2G07785 AT2G20360 AT2G33220 AT2G44620(mtACP-1)
                 AT2G47690 AT3G03070 AT3G06310 AT3G08610 AT3G12260 AT3G18410
                 AT3G62790 AT4G02580 AT5G08530 AT5G11770 AT5G37510(EMB1467)
                 AT5G47890 AT5G52840 AT5G67590(FRO1) ArthCp025(ndhJ)
                 ArthCp026(ndhK) ArthCp027(ndhC) ArthCp068(ndhB)
                 ArthCp071(ndhF) ArthCp074(ndhD) ArthCp076(ndhE)
                 ArthCp077(ndhG) ArthCp078(ndhI) ArthCp079(ndhA)
                 ArthCp080(ndhH)
            OSA: 3131395(ndhA) 3131396(ndhB) 3131397(ndhB) 3131398(ndhD)
                 3131399(ndhE) 3131400(ndhF) 3131401(ndhG) 3131458(OrsajCp028)
                 3131459(OrsajCp029) 3131460(OrsajCp030) 3131488(OrsajCp092)
                 3131489(OrsajCp094) 4324703 4331143 4332639 4333901 4334276
                 4339127 4339271 4339427 4342058 4342743 4343746 4344058
                 4344095 4344724 4346289 4349513 nad1 nad2 nad3 nad4 nad4L nad5
                 nad6 nad7 nad9
            CME: CMA090C CMC091C CMC099C CMI095C CMI118C CMI200C CMI262C
                 CMJ185C CMJ211C CMK135C CMM030C CMM034C CMM267C CMN320C
                 CMO080C CMQ200C CMR188C CMR289C CMS223C CMS372C CMT198C
            SCE: YKL192C(ACP1)
            AGO: AGOS_AER103W
            PIC: PICST_31688(NUO51) PICST_44890(NUO17) PICST_46630(NUFM)
                 PICST_58506(NUO13) PICST_62206(NUO21.2) PICST_65836(NUO10)
                 PICST_68160(NUC1) PICST_71972(ACP1) PICST_72822(NUO21.3)
                 PICST_74163(NUO30) PICST_75097(NUO21.1) PICST_75518(NUO20)
                 PICST_76018(NUE1) PICST_76226 PICST_76559(NUO24) PICST_79236
                 PICST_80821(ACP2) PICST_82538 PICST_84570(NBM4)
                 PICST_85822(NUO78) PICST_88630(NUO1)
            CAL: CaO19.4495 CaO19_2091(CaO19.2091) CaO19_2821(CaO19.2821)
                 CaO19_4758(CaO19.4758) CaO19_5547(CaO19.5547)
                 CaO19_6035(CaO19.6035) CaalfMp02(NAD6) CaalfMp03(NAD1)
                 CaalfMp09(NAD2) CaalfMp10(NAD3) CaalfMp12(NAD4L)
                 CaalfMp13(NAD5) CaalfMp14(NAD4)
            CGR: CAGL0D03586g
            SPO: SPAC11E3.12 SPAC4H3.09 SPBC18E5.10
            ANI: AN1063.2 AN1728.2 AN2414.2 AN4288.2 AN4297.2 AN5629.2
                 AN5704.2 AN5971.2 AN6077.2 AN7497.2 AN8049.2
            AFM: AFUA_1G06610 AFUA_1G06620 AFUA_1G12290 AFUA_2G05500
                 AFUA_2G09130 AFUA_2G10600 AFUA_2G13710 AFUA_2G14905
                 AFUA_3G08770 AFUA_3G13910 AFUA_4G05860 AFUA_4G05910
                 AFUA_4G11050 AFUA_5G02080 AFUA_5G04370 AFUA_5G06540
                 AFUA_5G08980 AFUA_6G02960 AFUA_6G04620 AFUA_6G08810
                 AFUA_6G12790
            AOR: AO090001000300 AO090001000459 AO090001000553 AO090001000661
                 AO090003000400 AO090003001115 AO090003001313 AO090011000502
                 AO090011000578 AO090011000782 AO090026000229 AO090102000645
                 AO090103000199 AO090672000005
            ANG: An04g05640(nuo51)
            CNE: CNA02430 CNA05580 CNB01310 CNC07090 CND01070 CND04070
                 CND04410 CNE01150 CNE02800 CNE03960 CNF03360 CNH01030 CNH02730
                 CNL04280 CNL05770 CNM01400 CNM02270
            UMA: UM00381.1 UM00512.1 UM00633.1 UM00634.1 UM00718.1 UM00778.1
                 UM01681.1 UM02437.1 UM02893.1 UM03931.1 UM04822.1 UM04924.1
                 UM05598.1 UM05625.1 UM05902.1 UM06170.1 nad1 nad4 nad4L nad5
                 nad6
            DDI: DDBDRAFT_0184099 DDBDRAFT_0203708 DDBDRAFT_0206064
                 DDBDRAFT_0218264 DDB_0191420(qinA) DDB_0233205 DDB_0233206
                 DDB_0233208 DDB_0233209 DDB_0233240 DDB_0233241
                 DidioMp02(nad4) DidioMp03(nad2) DidioMp13(nad3)
                 DidioMp14(nad1) DidioMp15(nad6) DidioMp17(nad9)
                 DidioMp18(nad7) DidioMp38(nad5) DidioMp41(nad4L)
            TPV: TP03_0539
            TET: TTHERM_00193910 TTHERM_00194260 TTHERM_00294640
                 TTHERM_00335630 TTHERM_00557760 TTHERM_01161000
                 TepyoMp09(nad10) TepyoMp11(nad2) TepyoMp12(nad7)
                 TepyoMp17(nad1_b) TepyoMp26(nad3) TepyoMp29(nad9_1)
                 TepyoMp30(nad9_2) TepyoMp33(nad5) TepyoMp40(nad1_a)
                 TepyoMp44(nad4)
            TBR: Tb09.244.2620 Tb10.389.1140 Tb11.47.0017 Tb927.3.860
                 Tb927.5.450 Tb927.7.6350
            TCR: 503893.80 506513.190 507869.10 508399.10 508507.59 509809.10
                 511323.50 511867.140
            LMA: LmjF05.0980 LmjF17.0270 LmjF18.1480 LmjF27.0290 LmjF27.0740
            ECO: b2276(nuoN) b2277(nuoM) b2278(nuoL) b2279(nuoK) b2280(nuoJ)
                 b2281(nuoI) b2282(nuoH) b2283(nuoG) b2284(nuoF) b2285(nuoE)
                 b2286(nuoC) b2287(nuoB) b2288(nuoA)
            ECJ: JW2271(nuoN) JW2272(nuoM) JW2273(nuoL) JW2274(nuoK)
                 JW2275(nuoJ) JW2276(nuoI) JW2277(nuoH) JW2278(nuoG)
                 JW2279(nuoF) JW2280(nuoE) JW2283(nuoA) JW5375(nuoC)
                 JW5875(nuoB)
            ECE: Z3534(nuoN) Z3536(nuoM) Z3537(nuoL) Z3538(nuoK) Z3539(nuoJ)
                 Z3540(nuoI) Z3541(nuoH) Z3542(nuoG) Z3543(nuoF) Z3544(nuoE)
                 Z3545(nuoC) Z3546(nuoB) Z3547(nuoA)
            ECS: ECs3160 ECs3161 ECs3162 ECs3163 ECs3164 ECs3165 ECs3166
                 ECs3167 ECs3168 ECs3169 ECs3170 ECs3171 ECs3172
            ECC: c2817(nuoN) c2818(nuoM) c2819(nuoL) c2820(nuoK) c2821(nuoJ)
                 c2822(nuoI) c2823(nuoH) c2824(nuoG) c2825(nuoF) c2826(nuoE)
                 c2827(nuoC) c2828(nuoB) c2829(nuoA)
            ECI: UTI89_C1220(acpP) UTI89_C2556(nuoN) UTI89_C2557(nuoM)
                 UTI89_C2558(nuoL) UTI89_C2559(nuoK) UTI89_C2560(nuoJ)
                 UTI89_C2561(nuoI) UTI89_C2562(nuoH) UTI89_C2563(nuoG)
                 UTI89_C2564(nuoF) UTI89_C2565(nuoE) UTI89_C2566(nuoC)
                 UTI89_C2567 UTI89_C2568(nuoA)
            ECP: ECP_2315 ECP_2316 ECP_2317 ECP_2318 ECP_2319 ECP_2320
                 ECP_2321 ECP_2322 ECP_2323 ECP_2324 ECP_2325 ECP_2326 ECP_2327
            ECV: APECO1_4277(nuoA) APECO1_4278(nuoB) APECO1_4280(nuoE)
                 APECO1_4281(nuoF) APECO1_4282(nuoG) APECO1_4283(nuoH)
                 APECO1_4284(nuoI) APECO1_4285(nuoJ) APECO1_4286(nuoK)
                 APECO1_4287(nuoL) APECO1_4288(nuoM) APECO1_4289(nuoN)
            STY: STY2546(nuoN) STY2547(nuoM) STY2548(nuoL) STY2549(nuoK)
                 STY2550(nuoJ) STY2551(nuoI) STY2552(nuoH) STY2553(nuoG)
                 STY2554(nuoF) STY2555(nuoE) STY2556(nuoC) STY2557(nuoB)
                 STY2558(nuoA)
            STT: t0536(nuoA) t0537(nuoB) t0538(nuoC) t0539(nuoE) t0540(nuoF)
                 t0541(nuoG) t0542(nuoH) t0543(nuoI) t0544(nuoJ) t0545(nuoK)
                 t0546(nuoL) t0547(nuoM) t0548(nuoN)
            SPT: SPA0536(nuoA) SPA0537(nuoB) SPA0538(nuoC) SPA0539(nuoE)
                 SPA0540(nuoF) SPA0541(nuoG) SPA0542(nuoH) SPA0543(nuoI)
                 SPA0544(nuoJ) SPA0545(nuoK) SPA0546(nuoL) SPA0547(nuoM)
                 SPA0548(nuoN)
            SEC: SC2316(nuoN) SC2317(nuoM) SC2318(nuoL) SC2319(nuoK)
                 SC2320(nuoJ) SC2321(nuoI) SC2322(nuoH) SC2323(nuoG)
                 SC2324(nuoF) SC2325(nuoE) SC2326(nuoC) SC2327(nuoB)
                 SC2328(nuoA)
            STM: STM2316.S(nuoN) STM2317(nuoM) STM2318(nuoL) STM2319(nuoK)
                 STM2320(nuoJ) STM2321(nuoI) STM2322(nuoH) STM2323.S(nuoG)
                 STM2324(nuoF) STM2325(nuoE) STM2326(nuoC) STM2327(nuoB)
                 STM2328(nuoA)
            YPE: YPO2543(nuoN) YPO2544(nuoM) YPO2545(nuoL) YPO2546(nuoK)
                 YPO2547(nuoJ) YPO2548(nuoI) YPO2549(nuoH) YPO2550(nuoG)
                 YPO2551(nuoF) YPO2552(nuoE) YPO2553(nuoD) YPO2554(nuoB)
                 YPO2555(nuoA)
            YPK: y1630(nuoA) y1631(nuoB) y1632(nuoC) y1633(nuoE) y1634(nuoF)
                 y1635(nuoG) y1636(nuoH) y1637(nuoI) y1638(nuoJ) y1639(nuoK)
                 y1640(nuoL) y1641(nuoM) y1642(nuoN)
            YPM: YP_2354(nuoN) YP_2355(nuoM) YP_2356(nuoL) YP_2357(nuoK)
                 YP_2358(nuoJ) YP_2359(nuoI) YP_2360(nuoH) YP_2361(nuoG)
                 YP_2362(nuoF) YP_2363(nuoE) YP_2364(nuoD) YP_2365(nuoB)
                 YP_2366(nuoA)
            YPA: YPA_2041
            YPN: YPN_2144
            YPS: YPTB2575(nuoN) YPTB2576(nuoM) YPTB2577(nuoL) YPTB2578(nuoK)
                 YPTB2579(nuoJ) YPTB2580(nuoI) YPTB2581(nuoH) YPTB2582(nuoG)
                 YPTB2583(nuoF) YPTB2584(nuoE) YPTB2585(nuoD) YPTB2586(nuoB)
                 YPTB2587(nuoA)
            YEN: YE1349(nuoG)
            SFL: SF2352(nuoN) SF2353(nuoM) SF2354(nuoL) SF2355(nuoK)
                 SF2356(nuoJ) SF2357(nuoI) SF2358(nuoH) SF2359(nuoG)
                 SF2360(nuoF) SF2361(nuoE) SF2362(nuoC) SF2363(nuoB)
                 SF2364(nuoA)
            SFX: S2487(nuoN) S2488(nuoM) S2489(nuoL) S2490(nuoK) S2491(nuoJ)
                 S2492(nuoI) S2493(nuoH) S2494(nuoG) S2495(nuoF) S2496(nuoE)
                 S2497(nuoC) S2498(nuoB) S2499(nuoA)
            SFV: SFV_2343(nuoN) SFV_2344(nuoM) SFV_2345(nuoL) SFV_2346(nuoK)
                 SFV_2347(nuoJ) SFV_2348(nuoI) SFV_2349(nuoH) SFV_2350(nuoG)
                 SFV_2351(nuoF) SFV_2352(nuoE) SFV_2353(nuoC) SFV_2354(nuoB)
            SSN: SSON_2333(nuoN) SSON_2334(nuoM) SSON_2335(nuoL)
                 SSON_2336(nuoK) SSON_2337(nuoJ) SSON_2338(nuoI)
                 SSON_2339(nuoH) SSON_2340(nuoG) SSON_2341(nuoF)
                 SSON_2342(nuoE) SSON_2343(nuoC) SSON_2344(nuoB)
                 SSON_2345(nuoA)
            SBO: SBO_2309(nuoN) SBO_2310(nuoM) SBO_2311(nuoL) SBO_2312(nuoK)
                 SBO_2313(nuoJ) SBO_2314(nuoI) SBO_2315(nuoH) SBO_2316(nuoG)
                 SBO_2317(nuoF) SBO_2318(nuoE) SBO_2319(nuoC) SBO_2320(nuoB)
                 SBO_2321(nuoA)
            SDY: SDY_2472(nuoN) SDY_2473(nuoM) SDY_2474(nuoL) SDY_2475(nuoK)
                 SDY_2476(nuoJ) SDY_2477(nuoI) SDY_2478(nuoH) SDY_2479(nuoG)
                 SDY_2480(nuoF) SDY_2481(nuoE) SDY_2482(nuoC) SDY_2483(nuoB)
                 SDY_2484(nuoA)
            ECA: ECA3016(nuoN) ECA3017(nuoM) ECA3018(nuoL) ECA3019(nuoK)
                 ECA3020(nuoJ) ECA3021(nuoI) ECA3022(nuoH)
            PLU: plu3077(nuoN) plu3078(nuoM) plu3079(nuoL) plu3080(nuoK)
                 plu3081(nuoJ) plu3082(nuoI) plu3083(nuoH) plu3084(nuoG)
                 plu3085(nuoF) plu3086(nuoE) plu3087(nuoC) plu3088(nuoB)
                 plu3089(nuoA)
            BUC: BU154(nuoA) BU155(nuoB) BU156(nuoCD) BU157(nuoE) BU158(nuoF)
                 BU159(nuoG) BU160(nuoH) BU161(nuoI) BU162(nuoJ) BU163(nuoK)
                 BU164(nuoL) BU165(nuoM) BU166(nuoN)
            BAS: BUsg147(nuoA) BUsg148(nuoB) BUsg149(nuoCD) BUsg150(nuoE)
                 BUsg151(nuoF) BUsg152(nuoG) BUsg153(nuoH) BUsg154(nuoI)
                 BUsg155(nuoJ) BUsg156(nuoK) BUsg157(nuoL) BUsg158(nuoM)
                 BUsg159(nuoN)
            BAB: bbp143(nuoA) bbp144(nuoB) bbp145(nuoCD) bbp146(nuoE)
                 bbp147(nuoF) bbp148(nuoG) bbp149(nuoH) bbp150(nuoI)
                 bbp151(nuoJ) bbp152(nuoK) bbp153(nuoL) bbp154(nuoM)
                 bbp155(nuoN)
            BCC: BCc_097(nuoA) BCc_098(nuoB) BCc_099(nuoCD) BCc_100(nuoE)
                 BCc_101(nuoF) BCc_102(nuoG) BCc_103(nuoH) BCc_104(nuoI)
                 BCc_105(nuoJ) BCc_106(nuoK) BCc_107(nuoL) BCc_108(nuoM)
                 BCc_109(nuoN)
            SGL: SG1589 SG1590 SG1591 SG1592 SG1593 SG1594 SG1595 SG1596
                 SG1597 SG1598 SG1599 SG1600 SG1601
            BFL: Bfl481(nuoN) Bfl482(nuoM) Bfl483(nuoL) Bfl484(nuoK)
                 Bfl485(nuoJ) Bfl486(nuoI) Bfl487(nuoH) Bfl488(nuoG)
                 Bfl489(nuoF) Bfl490(nuoE) Bfl491(nuoCD) Bfl492(nuoB)
                 Bfl493(nuoA)
            BPN: BPEN_497(nuoN) BPEN_498(nuoM) BPEN_499(nuoL) BPEN_500(nuoK)
                 BPEN_501(nuoJ) BPEN_502(nuoI) BPEN_503(nuoH) BPEN_504(nuoG)
                 BPEN_505(nuoF) BPEN_506(nuoE) BPEN_507(nuoCD) BPEN_508(nuoB)
                 BPEN_509(nuoA)
            XFA: XF0305 XF0306 XF0307 XF0308 XF0309 XF0310 XF0311 XF0312
                 XF0313 XF0314 XF0315 XF0316 XF0317 XF0318
            XFT: PD0248(nuoA) PD0249(nuoB) PD0250(nuoC) PD0251(nuoD)
                 PD0252(nuoE) PD0253(nuoF) PD0254(nuoG) PD0255(nuoH)
                 PD0256(nuoI) PD0257(nuoJ) PD0258(nuoK) PD0259(nuoL)
                 PD0260(nuoM) PD0261(nuoN)
            XCC: XCC2515(nuoN) XCC2516(nuoM) XCC2517(nuoL) XCC2518(nuoK)
                 XCC2519(nuoJ) XCC2520(nuoI) XCC2521(nuoH) XCC2522(nuoG)
                 XCC2523(nuoF) XCC2524(nuoE) XCC2525(nuoD) XCC2526(nuoC)
                 XCC2527(nuoB) XCC2528(nuoA)
            XCB: XC_1589 XC_1590 XC_1591 XC_1592 XC_1593 XC_1594 XC_1595
                 XC_1596 XC_1597 XC_1598 XC_1599 XC_1600 XC_1601 XC_1602
            XCV: XCV2177 XCV2840(nuoN) XCV2841(nuoM) XCV2842(nuoL)
                 XCV2843(nuoK) XCV2844(nuoJ) XCV2845(nuoI) XCV2846(nuoH)
                 XCV2847(nuoG) XCV2848(nuoF) XCV2849(nuoE) XCV2850(nuoD)
                 XCV2851(nuoC) XCV2852(nuoB) XCV2853(nuoA)
            XAC: XAC2172 XAC2691(nuoN) XAC2692(nuoM) XAC2693(nuoL)
                 XAC2694(nuoK) XAC2695(nuoJ) XAC2696(nuoI) XAC2697(nuoH)
                 XAC2698(nuoG) XAC2699(nuoF) XAC2700(nuoE) XAC2701(nuoD)
                 XAC2702(nuoC) XAC2703(nuoB) XAC2704(nuoA)
            XOO: XOO2197 XOO3222(nuoN) XOO3223(nuoM) XOO3224(nuoL)
                 XOO3225(nuoK) XOO3226(nuoJ) XOO3227(nuoI) XOO3228(nuoH)
                 XOO3229(nuoG) XOO3230(nuoF) XOO3232(nuoE) XOO3233(nuoD)
                 XOO3234(nuoC) XOO3235(nuoB) XOO3236(nuoA)
            XOM: XOO_2065(XOO2065) XOO_3054(XOO3054) XOO_3055(XOO3055)
                 XOO_3056(XOO3056) XOO_3057(XOO3057) XOO_3058(XOO3058)
                 XOO_3059(XOO3059) XOO_3060(XOO3060) XOO_3061(XOO3061)
                 XOO_3062(XOO3062) XOO_3063(XOO3063) XOO_3064(XOO3064)
                 XOO_3065(XOO3065) XOO_3066(XOO3066) XOO_3067(XOO3067)
            VCH: VC1581
            PAE: PA1883 PA2637(nuoA) PA2638(nuoB) PA2639(nuoD) PA2640(nuoE)
                 PA2641(nuoF) PA2642(nuoG) PA2643(nuoH) PA2644(nuoI)
                 PA2645(nuoJ) PA2646(nuoK) PA2647(nuoL) PA2648(nuoM)
                 PA2649(nuoN)
            PAU: PA14_29850(nuoN) PA14_29860(nuoM) PA14_29880(nuoL)
                 PA14_29890(nuoK) PA14_29900(nuoJ) PA14_29920(nuoI)
                 PA14_29930(nuoH) PA14_29940(nuoG) PA14_29970(nuoF)
                 PA14_29980(nuoE) PA14_29990(nuoD) PA14_30010(nuoB)
                 PA14_40160(nuoA)
            PPU: PP_4119(nuoA) PP_4120(nuoB) PP_4121(nuoCD) PP_4122(nuoE)
                 PP_4123(nuoF) PP_4124(nuoG) PP_4125(nuoH) PP_4126(nuoI)
                 PP_4127(nuoJ) PP_4128(nouK) PP_4129(nuoL) PP_4130(nuoM)
                 PP_4131(nuoN)
            PST: PSPTO_3365(nuoA) PSPTO_3366(nuoB) PSPTO_3367(nuoCD)
                 PSPTO_3368(nuoE) PSPTO_3369(nuoF) PSPTO_3370(nuoG)
                 PSPTO_3371(nuoH) PSPTO_3372(nuoI) PSPTO_3373(nuoJ)
                 PSPTO_3374(nouK) PSPTO_3375(nuoL) PSPTO_3376(nuoM)
                 PSPTO_3377(nuoN)
            PSB: Psyr_3197 Psyr_3198 Psyr_3199 Psyr_3200 Psyr_3201 Psyr_3202
                 Psyr_3203 Psyr_3204 Psyr_3205 Psyr_3206 Psyr_3207 Psyr_3208
                 Psyr_3209
            PSP: PSPPH_3109(nuoA) PSPPH_3110(nuoB) PSPPH_3111(nuoCD)
                 PSPPH_3112(nuoE) PSPPH_3113(nuoF) PSPPH_3114(nuoG)
                 PSPPH_3115(nuoH) PSPPH_3116(nuoI) PSPPH_3117(nuoJ)
                 PSPPH_3118(nouK) PSPPH_3119(nuoL) PSPPH_3120(nuoM)
                 PSPPH_3121(nuoN)
            PFL: PFL_3899(nuoD) PFL_3903(nuoH) PFL_3904(nuoI) PFL_3905(nuoJ)
                 PFL_3906(nuoK) PFL_3907(nuoL) PFL_3908(nuoM) PFL_3909(nuoN)
            PFO: Pfl_3603 Pfl_3605 Pfl_3606 Pfl_3608 Pfl_3609 Pfl_3610
                 Pfl_3612 Pfl_3613 Pfl_3614 Pfl_3615
            PEN: PSEEN3484(nuoA) PSEEN3485(nuoB) PSEEN3486(nuoC)
                 PSEEN3487(nuoE) PSEEN3488(nuoF) PSEEN3489(nuoG)
                 PSEEN3490(nuoH) PSEEN3491(nuoI) PSEEN3492(nuoJ)
                 PSEEN3493(nuoK) PSEEN3494(nuoL) PSEEN3495(nuoM)
                 PSEEN3496(nuoN)
            PAR: Psyc_0584(nuoA) Psyc_0585(nuoB) Psyc_0586(nuoD)
                 Psyc_0587(nuoE) Psyc_0588(nuoF) Psyc_0589(nuoG)
                 Psyc_0590(nuoH) Psyc_0591(nuoI) Psyc_0592(nuoJ)
                 Psyc_0593(nouK) Psyc_0594(nuoL) Psyc_0595(nuoM)
                 Psyc_0596(nuoN)
            PCR: Pcryo_0573 Pcryo_0574 Pcryo_0575 Pcryo_0576 Pcryo_0577
                 Pcryo_0578 Pcryo_0579 Pcryo_0580 Pcryo_0581 Pcryo_0582
                 Pcryo_0583 Pcryo_0584 Pcryo_0585
            ACI: ACIAD0730(nuoA) ACIAD0731(nuoB) ACIAD0733(nuoCD)
                 ACIAD0734(nuoE) ACIAD0735(nuoF) ACIAD0736(nuoG)
                 ACIAD0737(nuoH) ACIAD0738(nuoI) ACIAD0739(nuoJ)
                 ACIAD0740(nuoK) ACIAD0741(nuoL) ACIAD0742(nuoM)
                 ACIAD0743(nuoN)
            ACB: A1S_0757
            SON: SO_1009(nuoN) SO_1010(nuoM) SO_1011(nuoL) SO_1012(nuoK)
                 SO_1013(nuoJ) SO_1014(nuoI) SO_1015(nuoH) SO_1016(nuoG)
                 SO_1017(nuoF) SO_1018(nuoE) SO_1019(nuoCD) SO_1020(nuoB)
                 SO_1021(nuoA)
            ILO: IL0524
            CBU: CBU_1435(nuoN) CBU_1436(nuoM) CBU_1437(nuoL) CBU_1438(nuoK)
                 CBU_1439(nuoJ) CBU_1440(nuoI) CBU_1441(nuoH) CBU_1442(nuoG)
                 CBU_1443(nuoF) CBU_1444(nuoE) CBU_1445(nuoD) CBU_1446(nuoC)
                 CBU_1447(nuoB) CBU_1448(nuoA)
            CBD: COXBU7E912_0545(nuoA) COXBU7E912_0546(nuoB)
                 COXBU7E912_0547(nuoC) COXBU7E912_0548(nuoD)
                 COXBU7E912_0549(nuoE) COXBU7E912_0550(nuoF)
                 COXBU7E912_0552(nuoG) COXBU7E912_0553(nuoH)
                 COXBU7E912_0554(nuoI) COXBU7E912_0555(nuoJ)
                 COXBU7E912_0556(nuoK) COXBU7E912_0557(nuoL)
                 COXBU7E912_0558(nuoM) COXBU7E912_0559(nuoN)
            LPN: lpg0222 lpg2776(nuoN) lpg2777(nuoM) lpg2778(nuoL)
                 lpg2779(nuoK) lpg2780(nuoJ) lpg2781(nuoI) lpg2782(nuoH)
                 lpg2783(nuoG) lpg2784(nuoF) lpg2785 lpg2786(nuoD)
                 lpg2787(nuoC) lpg2788(nuoB2) lpg2789(nuoA)
            LPF: lpl0276 lpl2692(nuoN) lpl2693(nuoM) lpl2694(nuoL)
                 lpl2695(nuoK) lpl2696(nuoJ) lpl2697(nuoI) lpl2698(nuoH)
                 lpl2699(nuoG) lpl2700(nuoF) lpl2701(nuoE) lpl2702(nuoD)
                 lpl2703(nuoC) lpl2704(nuoB) lpl2705(nuoA)
            LPP: lpp0281 lpp2823(nuoN) lpp2824(nuoM) lpp2825(nuoL)
                 lpp2826(nuoK) lpp2827(nuoJ) lpp2828(nuoI) lpp2829(nuoH)
                 lpp2830(nuoG) lpp2831(nuoF) lpp2832(nuoE) lpp2833(nuoD)
                 lpp2834(nuoC) lpp2835(nuoB) lpp2836(nuoA)
            MCA: MCA0511 MCA0514 MCA0515 MCA1347(nuoN) MCA1348(nuoM)
                 MCA1349(nuoL) MCA1350(nuoK) MCA1351(nuoJ) MCA1352(nuoI)
                 MCA1353(nuoH) MCA1354(nuoG) MCA1355(nuoF) MCA1356(nuoE)
                 MCA1357(nuoCD) MCA1358(nuoB) MCA1359(nuoA) MCA2577
            FTU: FTT0031(nuoA) FTT0032(nuoB) FTT0033(nuoC) FTT0034(nuoD)
                 FTT0035(nuoE) FTT0036(nuoF) FTT0037(nuoG) FTT0038(nuoH)
                 FTT0039(nuoI) FTT0040(nuoJ) FTT0041(nuoK) FTT0042(nuoL)
                 FTT0043(nuoM) FTT0044(nuoN)
            FTF: FTF0031(nuoA) FTF0032(nuoB) FTF0033(nuoC) FTF0034(nuoD)
                 FTF0035(nuoE) FTF0036(nuoF) FTF0037(nuoG) FTF0038(nuoH)
                 FTF0039(nuoI) FTF0040(nuoJ) FTF0041(nuoK) FTF0042(nuoL)
                 FTF0043(nuoM) FTF0044(nuoN)
            FTL: FTL_1817 FTL_1818 FTL_1819 FTL_1820 FTL_1821 FTL_1822
                 FTL_1823 FTL_1824 FTL_1825 FTL_1826 FTL_1827 FTL_1828 FTL_1829
                 FTL_1830
            FTH: FTH_1753(nuoN) FTH_1754(nuoM) FTH_1755(nuoL) FTH_1756(nuoK)
                 FTH_1757(nuoJ) FTH_1758(nuoI) FTH_1759(nuoH) FTH_1760(nuoG)
                 FTH_1761(nuoF) FTH_1762(nuoE) FTH_1763(nuoD) FTH_1764(nuoC)
                 FTH_1765(nuoB)
            FTN: FTN_1667(nuoN) FTN_1668(nuoM) FTN_1669(nuoL) FTN_1670(nuoK)
                 FTN_1671(nuoJ) FTN_1672(nuoI) FTN_1673(nuoH) FTN_1674(nuoG)
                 FTN_1675(nuoF) FTN_1676(nuoE) FTN_1677(nuoD) FTN_1678(nuoC)
                 FTN_1679(nuoB)
            TCX: Tcr_0239 Tcr_0817 Tcr_0818 Tcr_0819 Tcr_0820 Tcr_0821
                 Tcr_0822 Tcr_0823 Tcr_0824 Tcr_0826 Tcr_0827 Tcr_0853
            NOC: Noc_0107 Noc_0390 Noc_0477 Noc_1115 Noc_1116 Noc_1117
                 Noc_1118 Noc_1121 Noc_1122 Noc_1123 Noc_1124 Noc_1125 Noc_1127
                 Noc_2555 Noc_2558 Noc_2561 Noc_2565
            AEH: Mlg_0029 Mlg_1957 Mlg_1958 Mlg_1959 Mlg_1960 Mlg_1961
                 Mlg_1962 Mlg_1963 Mlg_1964 Mlg_1965 Mlg_1966 Mlg_1967 Mlg_1968
                 Mlg_1969 Mlg_1970 Mlg_2512
            HHA: Hhal_1758 Hhal_1759
            CSA: Csal_3130
            ABO: ABO_1612(rnfD)
            AHA: AHA_1770 AHA_1771 AHA_1772 AHA_1773 AHA_1774 AHA_1775
                 AHA_1776 AHA_1777 AHA_1778(nuoF) AHA_1779 AHA_1780 AHA_1781
                 AHA_1782
            BCI: BCI_0369(nuoN) BCI_0370(nuoM) BCI_0371(nuoL) BCI_0372(nuoK)
                 BCI_0373(nuoJ) BCI_0374(nuoI) BCI_0375(nuoH) BCI_0376(nuoG)
                 BCI_0377(nuoF) BCI_0378(nuoE) BCI_0379(nuoCD) BCI_0380(nuoB)
                 BCI_0381(nuoA)
            RMA: Rmag_0239 Rmag_0241 Rmag_0243 Rmag_0244
            VOK: COSY_0229(nuoA) COSY_0230(nuoB) COSY_0231(nuoC)
                 COSY_0232(nuoD) COSY_0233(nuoE) COSY_0234(nuoF)
                 COSY_0235(nuoG) COSY_0236(nuoH) COSY_0237(nuoI)
                 COSY_0238(nuoJ) COSY_0239(nuoK) COSY_0240(nuoL)
                 COSY_0241(nuoM) COSY_0242(nuoN)
            NME: NMB0241 NMB0242 NMB0243 NMB0244 NMB0245 NMB0246 NMB0249
                 NMB0250 NMB0251 NMB0253 NMB0254 NMB0257 NMB0258 NMB0259
            NMA: NMA0002(nuoL) NMA0005(nuoK) NMA0006(nuoJ) NMA0008(nuoI)
                 NMA0009(nuoH) NMA0010(nuoG) NMA0014(nuoF) NMA0015(nuoE)
                 NMA0016(nuoD) NMA0017(nuoC) NMA0018(nuoB) NMA0019(nuoA)
                 NMA2228(nuoN) NMA2229(nuoM)
            NMC: NMC0237(nuoA) NMC0238(nuoB) NMC0239(nuoC) NMC0240(nuoD)
                 NMC0241(nuoE) NMC0242(nuoF) NMC0244(nuoG) NMC0245(nuoH)
                 NMC0246(nuoI) NMC0247(nuoJ) NMC0248(nuoK) NMC0251(nuoL)
                 NMC0252(nuoM) NMC0253(nuoN) NMC0505(nqrF) NMC0509(nqrB)
                 NMC0510(nqrA)
            NGO: NGO1737(nuoN) NGO1738(nuoM) NGO1740(nuoL) NGO1741(nuoK)
                 NGO1742(nuoJ) NGO1743(nuoI) NGO1744(nuoH) NGO1745(nuoG)
                 NGO1746(nuoF) NGO1747(nuoE) NGO1748(nuoD) NGO1749(nuoC)
                 NGO1750(nuoB) NGO1751(nuoA)
            CVI: CV_0633(nuoA1) CV_0941(nuoA2) CV_0942(nuoB2) CV_0943(nuoC)
                 CV_0944(nuoD) CV_0945(nuoE) CV_0946(nuoF) CV_0947(nuoG)
                 CV_0948(nuoH) CV_0949(nuoI) CV_0950(nuoJ) CV_0951(nuoK)
                 CV_0952(nuoL) CV_0953(nuoM) CV_0954(nuoN) CV_2033
                 CV_2755(nuoB1) CV_3221
            RSO: RSc0087(RS02261) RSc2049(nuoN) RSc2050(nuoM) RSc2051(nuoL)
                 RSc2052(nuoK) RSc2053(nuoJ) RSc2054(nuoI) RSc2055(nuoH)
                 RSc2056(nuoG) RSc2057(nuoF) RSc2058(nuoE) RSc2059(nuoD)
                 RSc2060(nuoC) RSc2061(nuoB) RSc2062(nuoA)
            REU: Reut_A0220 Reut_A0617 Reut_A0961 Reut_A0965 Reut_A0967
                 Reut_A0968 Reut_A0971
            REH: H16_A1050(nuoA) H16_A1051(nuoB) H16_A1052(nuoC)
                 H16_A1053(nuoD) H16_A1054(nuoE) H16_A1055(nuoF)
                 H16_A1056(nuoG) H16_A1057(nuoH) H16_A1058(nuoI)
                 H16_A1059(nuoJ) H16_A1060(nuoK) H16_A1061(nuoL)
                 H16_A1062(nuoM) H16_A1063(nuoN)
            RME: Rmet_0177 Rmet_0927 Rmet_0928 Rmet_0929 Rmet_0930 Rmet_0931
                 Rmet_0932 Rmet_0933 Rmet_0934 Rmet_0935 Rmet_0936 Rmet_0937
                 Rmet_0938
            BMA: BMA1816(nuoN) BMA1817(nuoM) BMA1818(nuoL) BMA1819(nuoK)
                 BMA1820(nuoJ) BMA1821(nuoI) BMA1822(nuoH) BMA1823(nuoG)
                 BMA1824(nuoF) BMA1825(nuoE) BMA1826(nuoD) BMA1827(nuoC)
                 BMA1828(nuoB-1) BMA1829(nuoA) BMA3315 BMAA0517(nuoB-2)
            BMV: BMASAVP1_A1130(nuoA) BMASAVP1_A1132(nuoC)
                 BMASAVP1_A1133(nuoD) BMASAVP1_A1134(nuoE) BMASAVP1_A1135(nuoF)
                 BMASAVP1_A1136(nuoG) BMASAVP1_A1137(nuoH) BMASAVP1_A1138(nuoI)
                 BMASAVP1_A1139(nuoJ) BMASAVP1_A1140(nuoK) BMASAVP1_A1141(nuoL)
                 BMASAVP1_A1142(nuoM) BMASAVP1_A1143(nuoN)
            BML: BMA10299_A0724(nuoN) BMA10299_A0725(nuoM)
                 BMA10299_A0726(nuoL) BMA10299_A0727(nuoK) BMA10299_A0728(nuoJ)
                 BMA10299_A0729(nuoI) BMA10299_A0730(nuoH) BMA10299_A0731(nuoG)
                 BMA10299_A0732(nuoF) BMA10299_A0733(nuoE) BMA10299_A0734(nuoD)
                 BMA10299_A0735(nuoC) BMA10299_A0737(nuoA)
            BMN: BMA10247_0413(nuoA) BMA10247_0415(nuoC) BMA10247_0416(nuoD)
                 BMA10247_0417(nuoE) BMA10247_0418(nuoF) BMA10247_0419(nuoG)
                 BMA10247_0420(nuoH) BMA10247_0421(nuoI) BMA10247_0422(nuoJ)
                 BMA10247_0423(nuoK) BMA10247_0424(nuoL) BMA10247_0425(nuoM)
                 BMA10247_0426(nuoN)
            BXE: Bxe_A0199 Bxe_A3201 Bxe_A3202 Bxe_A3203 Bxe_A3204 Bxe_A3205
                 Bxe_A3206 Bxe_A3207 Bxe_A3208 Bxe_A3209 Bxe_A3210 Bxe_A3211
                 Bxe_A3212 Bxe_A3213 Bxe_A3214 Bxe_B1638 Bxe_C0528 Bxe_C0529
            BVI: Bcep1808_2328 Bcep1808_2331
            BUR: Bcep18194_A5567 Bcep18194_A5570 Bcep18194_A5574
                 Bcep18194_A5577 Bcep18194_A6380
            BCN: Bcen_1624 Bcen_1627 Bcen_1628 Bcen_1630 Bcen_1634 Bcen_1637
                 Bcen_6005
            BCH: Bcen2424_2072 Bcen2424_2236 Bcen2424_2237 Bcen2424_2238
                 Bcen2424_2239 Bcen2424_2240 Bcen2424_2241 Bcen2424_2242
                 Bcen2424_2243 Bcen2424_2244 Bcen2424_2245 Bcen2424_2246
                 Bcen2424_2247 Bcen2424_2248 Bcen2424_2249
            BAM: Bamb_2108 Bamb_2275 Bamb_2276 Bamb_2277 Bamb_2278 Bamb_2279
                 Bamb_2280 Bamb_2281 Bamb_2282 Bamb_2283 Bamb_2284 Bamb_2285
                 Bamb_2286 Bamb_2287 Bamb_3078
            BPS: BPSL0263 BPSL1211(nuoA) BPSL1212(nuoB) BPSL1213(nuoC)
                 BPSL1214(nuoD) BPSL1215 BPSL1216(nuoF) BPSL1217 BPSL1218(nuoH)
                 BPSL1219 BPSL1220(nuoJ) BPSL1221(nuoK) BPSL1222(nuoL)
                 BPSL1223(nuoM) BPSL1224(nuoN) BPSL3063
            BPM: BURPS1710b_0455 BURPS1710b_1435(nuoA) BURPS1710b_1436(nuoB)
                 BURPS1710b_1437(nuoC) BURPS1710b_1438(nuoD)
                 BURPS1710b_1439(nuoE) BURPS1710b_1440(nuoF) BURPS1710b_1441
                 BURPS1710b_1442(nuoH) BURPS1710b_1443(nuoI)
                 BURPS1710b_1444(nuoJ) BURPS1710b_1445(nuoK)
                 BURPS1710b_1446(nuoL) BURPS1710b_1448(nuoM)
                 BURPS1710b_1449(nuoN)
            BTE: BTH_I1061 BTH_I1062 BTH_I1063 BTH_I1064(nuoD) BTH_I1065
                 BTH_I1066(nuoF) BTH_I1067 BTH_I1068 BTH_I1069 BTH_I1070
                 BTH_I1071 BTH_I1072 BTH_I1073 BTH_I1074
            PNU: Pnuc_1045
            BPE: BP0841(nuoA) BP0842(nuoB) BP0843(nuoC) BP0844(nuoD)
                 BP0845(nuoE) BP0846(nuoF) BP0847(nuoG) BP0848(nuoH)
                 BP0849(nuoI) BP0850(nuoJ) BP0851(nuoK) BP0852(nuoL)
                 BP0853(nuoM) BP0854(nuoN) BP3419
            BPA: BPP3378(nuoN) BPP3379(nuoM) BPP3380(nuoL) BPP3381(nuoK)
                 BPP3382(nuoJ) BPP3383(nuoI) BPP3384(nuoH) BPP3385(nuoG)
                 BPP3386(nuoF) BPP3387(nuoE) BPP3388(nuoD) BPP3389(nuoC)
                 BPP3390(nuoB) BPP3391(nuoA) BPP3569
            BBR: BB3828(nuoN) BB3829(nuoM) BB3830(nuoL) BB3831(nuoK)
                 BB3832(nuoJ) BB3833(nuoI) BB3834(nuoH) BB3835(nuoG)
                 BB3836(nuoF) BB3837(nuoE) BB3838(nuoD) BB3839(nuoC)
                 BB3840(nuoB) BB3841(nuoA) BB4004
            RFR: Rfer_1493 Rfer_1495 Rfer_1497 Rfer_1499 Rfer_1500 Rfer_2690
            POL: Bpro_3249 Bpro_3250 Bpro_3252 Bpro_3256 Bpro_3910
            PNA: Pnap_1430
            AAV: Aave_1269
            AJS: Ajs_0963
            VEI: Veis_2807 Veis_2811 Veis_2812
            MPT: Mpe_A0338 Mpe_A1403 Mpe_A1404 Mpe_A1405 Mpe_A1406 Mpe_A1407
                 Mpe_A1408 Mpe_A1409 Mpe_A1410 Mpe_A1411 Mpe_A1412 Mpe_A1413
                 Mpe_A1414 Mpe_A1415 Mpe_A1416 Mpe_A3296
            HAR: HEAR1819(nuoH) HEAR1823(nuoD) HEAR1824 HEAR1826 HEAR3435
            MMS: mma_1462 mma_1463 mma_1464 mma_1465 mma_1466 mma_1467
                 mma_1468 mma_1469 mma_1470 mma_1471 mma_1472 mma_1473 mma_1474
                 mma_1475
            NEU: NE1764(nuoN) NE1765(nuoM) NE1766(nuoL) NE1767(nuoK)
                 NE1768(nuoJ) NE1769(nuoI) NE1770(nuoH) NE1771(nuoG)
                 NE1772(nuoF) NE1773(nuoE) NE1774(nuoD) NE1775(nuoC)
                 NE1776(nuoB) NE1777(nuoA)
            NET: Neut_0799 Neut_0922 Neut_0923 Neut_0924 Neut_0925 Neut_0926
                 Neut_0927 Neut_0928 Neut_0929 Neut_0930 Neut_0931 Neut_0932
                 Neut_0933 Neut_0934 Neut_0935
            NMU: Nmul_A1013 Nmul_A1014 Nmul_A1015 Nmul_A1016 Nmul_A1017
                 Nmul_A1018 Nmul_A1019 Nmul_A1020 Nmul_A1021 Nmul_A1022
                 Nmul_A1023 Nmul_A1024 Nmul_A1025 Nmul_A1091 Nmul_A1092
                 Nmul_A1093 Nmul_A1094 Nmul_A1095 Nmul_A1096 Nmul_A1097
                 Nmul_A1098 Nmul_A1099 Nmul_A2450
            EBA: ebA2750(fdhB) ebA3382 ebA4835(nuoB) ebA4836(nuoC)
                 ebA4837(nuoD) ebA4838(nuoE) ebA4840(nuoF) ebA4841(nuoG)
                 ebA4842(nuoH) ebA4843(nuoI) ebA4844(nuoJ) ebA4846(nuoL)
                 ebA4847(nuoM) ebA4848(nuoN) ebB168(nuoK) ebD11(nuoA)
            AZO: azo0495 azo0829(nuoB1) azo1396(nuoA) azo1401(nuoF)
                 azo1402(nuoG) azo1403(nuoH) azo1826
            DAR: Daro_0564 Daro_0568 Daro_0949 Daro_0950 Daro_0951 Daro_0952
                 Daro_0953 Daro_0954 Daro_0955 Daro_0956 Daro_0957 Daro_0958
                 Daro_0959 Daro_0960 Daro_0961 Daro_0962 Daro_4134
            TBD: Tbd_1142(nuoA) Tbd_1143(nuoB) Tbd_1144(nuoC) Tbd_1145(nuoD)
                 Tbd_1146(nuoE) Tbd_1147(nuoF) Tbd_1148(nuoG) Tbd_1149(nuoH)
                 Tbd_1150(nuoI) Tbd_1151(nuoJ) Tbd_1152(nuoK) Tbd_1153(nuoL)
                 Tbd_1154(nuoM) Tbd_1155(nuoN) Tbd_2361
            MFA: Mfla_2054 Mfla_2055 Mfla_2057 Mfla_2058 Mfla_2061 Mfla_2260
            HPY: HP1260(NQO7) HP1261(NQO6) HP1262(NQO5) HP1263 HP1264 HP1265
                 HP1266(NQO3) HP1267(NQO8) HP1268(NQO9) HP1269(NQO10) HP1270
                 HP1271(NQO12) HP1272(NQO13) HP1273(NQO14)
            HPJ: jhp1181(nuoA) jhp1182(nuoB) jhp1183(nuoC) jhp1184(nuoD)
                 jhp1185(nuoE) jhp1186(nuoF) jhp1187(nuoG) jhp1188(nuoH)
                 jhp1189(nuoI) jhp1190(nuoJ) jhp1191(nuoK) jhp1192(nuoL)
                 jhp1193(nuoM) jhp1194(nuoN)
            HPA: HPAG1_0035 HPAG1_1204 HPAG1_1205 HPAG1_1206 HPAG1_1207
                 HPAG1_1208 HPAG1_1209 HPAG1_1210 HPAG1_1211 HPAG1_1212
                 HPAG1_1213 HPAG1_1214 HPAG1_1215 HPAG1_1216 HPAG1_1217
            HHE: HH1590(nuoN) HH1591(nuoM) HH1592(nuoL) HH1593(nuoK)
                 HH1594(nuoJ) HH1595(nuoI) HH1596(nuoH) HH1597(nuoG) HH1598
                 HH1599 HH1600(nuoD) HH1601(nuoC) HH1602(nuoB) HH1603(nuoA)
            HAC: Hac_0211(nuoN) Hac_0212(nuoM) Hac_0213(nuoL) Hac_0214(nuoK)
                 Hac_0215(nuoJ) Hac_0216(nuoI) Hac_0217(nuoH) Hac_0218(nuoG)
                 Hac_0219(nuoF) Hac_0220(nuoE) Hac_0221(nuoD) Hac_0222(nuoC)
                 Hac_0223(nuoB) Hac_0224(nuoA)
            WSU: WS0472(nuoA) WS0473(nuoB) WS0474(nuoC) WS0475(nuoD)
                 WS0476(nuoE) WS0478 WS0479(nuoG) WS0481(nuoH) WS0482(nuoI)
                 WS0483(nuoJ) WS0484(nuoK) WS0485(nuoL) WS0487 WS0488
                 WS1839(nuoN)
            TDN: Tmden_1826
            CJE: Cj1566c(nuoN) Cj1567c(nuoM) Cj1568c(nuoL) Cj1569c(nuoK)
                 Cj1570c(nuoJ) Cj1571c(nuoI) Cj1572c(nuoH) Cj1573c(nuoG)
                 Cj1574c Cj1575c Cj1576c(nuoD) Cj1577c(nuoC) Cj1578c(nuoB)
                 Cj1579c(nuoA)
            CJU: C8J_1463(nuoN) C8J_1464(nuoM) C8J_1465(nuoL) C8J_1466(nuoK)
                 C8J_1467(nuoJ) C8J_1469(nuoH) C8J_1471 C8J_1472 C8J_1473(nuoD)
                 C8J_1474(nuoC) C8J_1475(nuoB)
            CFF: CFF8240_0164
            CHA: CHAB381_0181
            ABU: Abu_0302(nuoN) Abu_0303(nuoM) Abu_0304(nuoL) Abu_0305(nuoK)
                 Abu_0307(nuoI) Abu_0308(nuoH) Abu_0309(nuoG) Abu_0311(nuoF)
                 Abu_0312(nuoE) Abu_0313(nuoCD) Abu_0314(nuoB) Abu_0315(nuoA)
                 Abu_2232
            NIS: NIS_0288(nuoA) NIS_0289(nuoB) NIS_0290(nuoC) NIS_0291(nuoD)
                 NIS_0294 NIS_0295(nuoG) NIS_0296(nuoH) NIS_0297(nuoI)
                 NIS_0298(nuoJ) NIS_0299(nuoK) NIS_0300(nuoL) NIS_0301(nuoM)
                 NIS_0302(nuoN)
            SUN: SUN_0844 SUN_0845 SUN_0846 SUN_0847 SUN_0849 SUN_0850
                 SUN_0851 SUN_0852 SUN_0853 SUN_2218(nuoN) SUN_2219(nuoM)
                 SUN_2220(nuoL) SUN_2221(nuoK) SUN_2222(nuoJ) SUN_2223(nuoI)
                 SUN_2224(nuoH) SUN_2225 SUN_2226 SUN_2229(nuoD) SUN_2230(nuoC)
                 SUN_2231(nuoB) SUN_2232(nuoA)
            GSU: GSU0338(nuoA-1) GSU0339(nuoB) GSU0340(nuoC) GSU0341(nouD)
                 GSU0342(nuoE-1) GSU0343(nouF) GSU0344 GSU0345(nuoH-1)
                 GSU0346(nuoI-1) GSU0347(nouJ) GSU0348(nuoK) GSU0349(nuoL-1)
                 GSU0350(nuoM-1) GSU0351(nuoN-1) GSU0385 GSU2722
                 GSU3429(nuoN-2) GSU3430(nuoM-2) GSU3431(nuoL-2) GSU3432(nuoI)
                 GSU3433(nuoJ) GSU3434(nuoI-2) GSU3436(nuoH-2) GSU3439
                 GSU3441(nuoF) GSU3443(nuoE-2) GSU3444(nuoBCD) GSU3445(nuoA-2)
            GME: Gmet_0152 Gmet_0153 Gmet_0154 Gmet_0157 Gmet_0159 Gmet_0161
                 Gmet_0163 Gmet_0165 Gmet_0168 Gmet_0171 Gmet_0172 Gmet_1109
                 Gmet_3144 Gmet_3342 Gmet_3343 Gmet_3344 Gmet_3345 Gmet_3346
                 Gmet_3347 Gmet_3348 Gmet_3349 Gmet_3350 Gmet_3351 Gmet_3352
                 Gmet_3353 Gmet_3354 Gmet_3355
            PCA: Pcar_0020 Pcar_0205 Pcar_0206 Pcar_0207 Pcar_0208 Pcar_0209
                 Pcar_0210 Pcar_0211 Pcar_0212 Pcar_0213 Pcar_0214 Pcar_0215
                 Pcar_0216 Pcar_0833 Pcar_0834 Pcar_1602 Pcar_1604 Pcar_1605
                 Pcar_1636 Pcar_1846 Pcar_2708
            PPD: Ppro_0595 Ppro_0631 Ppro_1626 Ppro_3190 Ppro_3524
            DVL: Dvul_0964 Dvul_2505
            BBA: Bd3080(nuoI) Bd3081(nuoG) Bd3083(nuoF) Bd3084(nuoE)
                 Bd3085(nuoD) Bd3086(nuoB) Bd3886(nuoN) Bd3887(nuoM)
                 Bd3888(nuoL) Bd3889(nuoK) Bd3890(nuoJ) Bd3891(nuoH)
                 Bd3892(nuoA)
            DPS: DP0683 DP0684 DP1309 DP1310 DP1311 DP1314 DP1315 DP1316
                 DP1317 DP1318 DP1319 DP1320 DP1321 DP2208 DP2209 DP2210
            ADE: Adeh_2567 Adeh_2570 Adeh_2571 Adeh_2573 Adeh_2574 Adeh_2575
                 Adeh_2576 Adeh_2577 Adeh_2578
            MXA: MXAN_1080 MXAN_1081 MXAN_1082 MXAN_1083 MXAN_1084 MXAN_1085
                 MXAN_1086 MXAN_2726 MXAN_2727 MXAN_2728 MXAN_2729 MXAN_2730
                 MXAN_2733 MXAN_2734
            SAT: SYN_00152 SYN_00153 SYN_00631 SYN_01369 SYN_01370 SYN_01647
                 SYN_01648 SYN_02139 SYN_02425
            SFU: Sfum_0199 Sfum_0201 Sfum_0202 Sfum_0203 Sfum_0204 Sfum_0205
                 Sfum_0206 Sfum_1938 Sfum_1939 Sfum_1940 Sfum_1941 Sfum_1942
                 Sfum_1943 Sfum_1954 Sfum_1956 Sfum_2703 Sfum_2712 Sfum_2740
                 Sfum_2745
            RPR: RP115(nuoF) RP353(nuoE) RP354(nuoD) RP355(nuoC) RP356(nuoB)
                 RP357(nuoA) RP537(nuoN1) RP790(nuoJ) RP791(nuoK) RP792(nuoL1)
                 RP793(nuoM) RP795(nuoI) RP796(nuoH) RP797(nuoG)
            RTY: RT0021(nuoF) RT0342(nuoE) RT0343(nuoD) RT0344(nuoC)
                 RT0345(nuoB) RT0346(nuoA) RT0526(nuoN) RT0777(nuoJ)
                 RT0778(nuoK) RT0779(nuoL) RT0780(nuoM) RT0782(nuoI)
                 RT0783(nuoH) RT0784(nuoG)
            RCO: RC0155(nuoF) RC0481(nuoE) RC0482(nuoD) RC0483(nuoC)
                 RC0484(nuoB) RC0485(nuoA) RC0796(nuoN1) RC1224(nuoJ)
                 RC1225(nuoK) RC1226(nuoL1) RC1227(nuoM) RC1229(nuoI)
                 RC1230(nuoH) RC1231(nuoG)
            RFE: RF_0455(nuoL3) RF_0458(nuoL2) RF_0460(nuoN2) RF_0563(nuoE)
                 RF_0564(nuoD) RF_0565(nuoC) RF_0566(nuoB) RF_0567(nuoA)
                 RF_0854(nuoN1) RF_1178(nuoF) RF_1255(nuoJ) RF_1256(nuoK)
                 RF_1257(nuoL1) RF_1258(nuoM) RF_1260(nuoI) RF_1261(nuoH)
                 RF_1262(nuoG)
            RBE: RBE_0085(nuoJ) RBE_0086(nuoK) RBE_0087(nuoL1) RBE_0088(nuoM)
                 RBE_0101(nuoG) RBE_0102(nuoH) RBE_0103(nuoI) RBE_0392(nuoE)
                 RBE_0394(nuoD) RBE_0396(nuoC) RBE_0397(nuoB) RBE_0398(nuoA)
                 RBE_0781(nuoN1) RBE_0905(nuoL2) RBE_1010(nuoN2)
                 RBE_1022(nuoL3) RBE_1183(nuoF)
            RAK: A1C_02645 A1C_02650 A1C_02660 A1C_02670 A1C_02675 A1C_03460
                 A1C_03985 A1C_06105 A1C_06110 A1C_06120 A1C_06135 A1C_06140
                 A1C_06150
            RBO: A1I_05020 A1I_05765 A1I_05775 A1I_05780 A1I_05790 A1I_05800
                 A1I_07420 A1I_07425 A1I_07430 A1I_07495 A1I_07515 A1I_07520
            RCM: A1E_02335 A1E_05035 A1E_05040 A1E_05065 A1E_05070 A1E_05080
                 A1E_05090
            RRI: A1G_02735 A1G_02740 A1G_02745 A1G_02750 A1G_02755 A1G_04470
                 A1G_06705 A1G_06710 A1G_06720 A1G_06730 A1G_06735 A1G_06740
            OTS: OTBS_1425(nuoN2) OTBS_1426(nuoL2) OTBS_1627(nuoA)
                 OTBS_1628(nuoB) OTBS_1629(nuoC) OTBS_1630(nuoD)
                 OTBS_1631(nuoE) OTBS_1632(nuoF) OTBS_2159(nuoG)
                 OTBS_2160(nuoH) OTBS_2161(nuoI) OTBS_2162(nuoJ)
                 OTBS_2163(nuoK)
            WOL: WD0159 WD0160(nuoG) WD0560(nuoD) WD0734(nuoE) WD0965(nuoJ)
                 WD0966(nuoK) WD0967(nuoL) WD0968(nuoM) WD0969 WD0976
                 WD0980(nuoI) WD1122(nuoC) WD1123(nuoB) WD1124(nuoA) WD1129
            WBM: Wbm0125 Wbm0237 Wbm0241 Wbm0242 Wbm0243 Wbm0375 Wbm0376
                 Wbm0471 Wbm0474 Wbm0594 Wbm0621 Wbm0622 Wbm0623 Wbm0624
                 Wbm0625
            AMA: AM193(nuoL2) AM452(nuoC1) AM453(nuoB) AM454(nuoA) AM623(nuoD)
                 AM624(nuoE) AM640(nuoH) AM641(nuoG) AM707(nuoI) AM744(nuoN1)
                 AM745(nuoM) AM746(nuoL) AM747(nuoK) AM748(nuoJ) AM750(nuoF)
                 AM840(nuoL3)
            APH: APH_0044 APH_1299
            ERU: Erum0430
            ERW: ERWE_CDS_00330 ERWE_CDS_03120(nuoC) ERWE_CDS_03130(nuoC)
                 ERWE_CDS_03140(nuoB) ERWE_CDS_03150(nuoA) ERWE_CDS_03830(nuoI)
                 ERWE_CDS_04450(nuoG) ERWE_CDS_04460(nuoH) ERWE_CDS_04620(nuoD)
                 ERWE_CDS_04630(nuoE) ERWE_CDS_04980(nuoN) ERWE_CDS_04990(nuoM)
                 ERWE_CDS_05000(nuoL) ERWE_CDS_05010(nuoK) ERWE_CDS_05020(nuoJ)
                 ERWE_CDS_05030(nuoF)
            ERG: ERGA_CDS_00320 ERGA_CDS_03070(nuoC) ERGA_CDS_03080(nuoC)
                 ERGA_CDS_03090(nuoB) ERGA_CDS_03100(nuoA) ERGA_CDS_03790(nuoI)
                 ERGA_CDS_04400(nuoG) ERGA_CDS_04410(nuoH) ERGA_CDS_04530(nuoD)
                 ERGA_CDS_04540(nuoE) ERGA_CDS_04880(nuoN) ERGA_CDS_04890(nuoM)
                 ERGA_CDS_04900(nuoL) ERGA_CDS_04910(nuoK) ERGA_CDS_04920(nuoJ)
                 ERGA_CDS_04930(nuoF)
            ECN: Ecaj_0035 Ecaj_0287 Ecaj_0288 Ecaj_0289 Ecaj_0361 Ecaj_0421
                 Ecaj_0422 Ecaj_0426 Ecaj_0427 Ecaj_0474 Ecaj_0475 Ecaj_0476
                 Ecaj_0477 Ecaj_0478 Ecaj_0486 Ecaj_0552 Ecaj_0677
            ECH: ECH_0063 ECH_0179
            NSE: NSE_0386 NSE_0563 NSE_0820
            PUB: SAR11_0499 SAR11_0883(nuoA) SAR11_0884(nuoB) SAR11_0885(nuoC)
                 SAR11_0886(nuoD) SAR11_0887(nuoE) SAR11_0888(nuoF)
                 SAR11_0889(nuoG) SAR11_0890(nuoH) SAR11_0891(nuoI)
                 SAR11_0892(nuoJ) SAR11_0893(nuoK) SAR11_0894(nuoL)
                 SAR11_0896(nuoM) SAR11_0897(nuoN)
            MLO: mll1352 mll1354 mll1355 mll1357 mll1358 mll1359 mll1361
                 mll1362 mll1364 mll1365 mll1366 mll1367 mll1369 mll1371
                 mll1372 mll5193 mlr3004
            MES: Meso_1022 Meso_1023 Meso_1024 Meso_1025 Meso_1026 Meso_1027
                 Meso_1028 Meso_1029 Meso_1030 Meso_1031 Meso_1032 Meso_1033
                 Meso_1034 Meso_1035 Meso_2428
            SME: SMa1516(nuoH2) SMa1519 SMa1523(nuoG2) SMa1525(nuoF2)
                 SMa1526(nuoE2) SMa1529(nuoD2) SMa1531(nuoC2) SMa1532(nuoB2)
                 SMa1533(nuoA2) SMa1535(nuoN2) SMa1536(nuoM2) SMa1544(nuoK2)
                 SMa1545 SMc00410 SMc01912(nuoA1) SMc01913(nuoB1)
                 SMc01914(nuoC1) SMc01915(nuoD1) SMc01917(nuoE1)
                 SMc01918(nuoF1) SMc01919 SMc01920(nuoG1) SMc01921(nuoH)
                 SMc01922(nuoI) SMc01923(nuoJ) SMc01924(nuoK1) SMc01925(nuoL)
                 SMc01926(nuoM) SMc01927(nuoN)
            SMD: Smed_0890 Smed_3538
            ATU: Atu0296 Atu1268(nuoA) Atu1269(nuoB) Atu1270(nuoC)
                 Atu1272(nouD) Atu1274(nuoE) Atu1275(nuoF) Atu1276(nuoG)
                 Atu1277(nuoH) Atu1278(nuoI) Atu1279(nuoJ) Atu1280(nuoK)
                 Atu1281(nuoL) Atu1282(nuoM) Atu1283(nuoN)
            ATC: AGR_C_2340 AGR_C_2341 AGR_C_2342(nuoC1) AGR_C_2346 AGR_C_2348
                 AGR_C_2350 AGR_C_2353 AGR_C_2354 AGR_C_2355 AGR_C_2357
                 AGR_C_2359 AGR_C_2360 AGR_C_2362 AGR_C_2364 AGR_C_511
            RET: RHE_CH00312(ypch00117) RHE_CH01602(nuoA1) RHE_CH01603(nuoB1)
                 RHE_CH01604(nuoC1) RHE_CH01606(nuoD1) RHE_CH01608(nuoE1)
                 RHE_CH01610 RHE_CH01611(nuoG1) RHE_CH01612(nuoH1)
                 RHE_CH01613(nuoI) RHE_CH01614(nuoJ) RHE_CH01615(nuoK1)
                 RHE_CH01616(nuoL) RHE_CH01617(nuoM1) RHE_CH01618(nuoN1)
                 RHE_CH02557(nuoB2) RHE_CH03729 RHE_CH03730(nuoK2)
                 RHE_CH03734(nuoM3) RHE_CH03735(nuoN2) RHE_CH03736(nuoA2)
                 RHE_CH03737(nuoB3) RHE_CH03738(nuoC2) RHE_CH03739(nuoD2)
                 RHE_CH03740(nuoE2) RHE_CH03741(nuoF2) RHE_CH03742(nuoG2)
                 RHE_CH03744 RHE_CH03745(nuoH2)
            RLE: RL1700(nqo1) RL1701(nqo6) RL1702(nqo5) RL1703(nqo4)
                 RL1704(nqo2) RL1705(nqo1) RL1706 RL1707(nqo3) RL1708(nuoH)
                 RL1709(nuoI) RL1710(nqo10) RL1711(nuoK) RL1713(nuoM) RL3240
            BME: BMEI1145 BMEI1146 BMEI1147 BMEI1148 BMEI1149 BMEI1150
                 BMEI1151 BMEI1152 BMEI1153 BMEI1154 BMEI1155 BMEI1156 BMEI1157
                 BMEI1158 BMEI1231 BMEII0259
            BMF: BAB1_0822 BAB1_0823(nuoB) BAB1_0824(nuoC) BAB1_0825
                 BAB1_0826(nuoE) BAB1_0827 BAB1_0828(nuoG) BAB1_0829(nuoH)
                 BAB1_0830(nuoI) BAB1_0831(nuoJ) BAB1_0832(nuoK) BAB1_0833
                 BAB1_0834(nuoM) BAB1_0835 BAB2_1002
            BMS: BR0802(nuoA) BR0803(nuoB) BR0804(nuoC) BR0805(nuoD)
                 BR0806(nuoE) BR0807(nuoF) BR0808(nuoG) BR0809(nuoH)
                 BR0810(nuoI) BR0811(nuoJ) BR0812(nuoK) BR0813(nuoL)
                 BR0814(nuoM) BR0815(nuoN) BRA1041
            BMB: BruAb1_0816(nuoA) BruAb1_0817(nuoB) BruAb1_0818(nuoC)
                 BruAb1_0819(nuoD) BruAb1_0820(nuoE) BruAb1_0821(nuoF)
                 BruAb1_0822(nuoG) BruAb1_0823(nuoH) BruAb1_0824(nuoI)
                 BruAb1_0825(nuoJ) BruAb1_0826(nuoK) BruAb1_0827(nuoL)
                 BruAb1_0828(nuoM) BruAb1_0829(nuoN)
            BOV: BOV_0797(nuoA) BOV_0798(nuoB) BOV_0799(nuoC) BOV_0801(nuoE)
                 BOV_0804(nuoH) BOV_0805(nuoI) BOV_0806(nuoJ) BOV_0807(nuoK)
                 BOV_0808(nuoL) BOV_0809(nuoM) BOV_0810(nuoN)
            BJA: bll0717 bll4904(nuoN) bll4905(nuoM) bll4906(nuoL) bll4907
                 bll4908(nuoJ) bll4909(nuoI) bll4910(nuoH) bll4911(nuoG)
                 bll4912(nuoF) bll4914 bll4916(nouD) bll4917(nuoC)
                 bll4918(nuoB) bll4919(nuoA) blr2316
            BRA: BRADO3480 BRADO3676 BRADO4171(nuoN) BRADO4172(nuoM)
                 BRADO4173(nuoL) BRADO4174(nuoK) BRADO4175(nuoJ)
                 BRADO4176(nuoII) BRADO4177(nuoH) BRADO4178(nuoG)
                 BRADO4179(nuoF) BRADO4181(nuoE) BRADO4183(nuoD)
                 BRADO4184(nuoC) BRADO4185(nuoB) BRADO4186(nuoA)
            BBT: BBta_4044 BBta_4231 BBta_4548(nuoN) BBta_4549(nuoM)
                 BBta_4550(nuoL) BBta_4551(nuoK) BBta_4552(nuoJ)
                 BBta_4553(nuoII) BBta_4554(nuoH) BBta_4555(nuoG)
                 BBta_4556(nuoF) BBta_4558(nuoE) BBta_4560(nuoD)
                 BBta_4561(nuoC) BBta_4562(nuoB) BBta_4563(nuoA)
            RPA: RPA0045 RPA2537 RPA2937(nuoN1) RPA2938(nuoM1) RPA2939(nuoL1)
                 RPA2940(nuoK1) RPA2941(nuoJ1) RPA2942(nuoI1) RPA2943(nuoH1)
                 RPA2944(nuoG1) RPA2945(nuoF1) RPA2947(nuoE1) RPA2949(nuoD)
                 RPA2950(nuoC) RPA2951(nuoB1) RPA2952(nuoA1) RPA2995(nuoL3)
                 RPA4252(nuoN2) RPA4253(nuoM2) RPA4254(nuoL2) RPA4255(nuoK2)
                 RPA4256(nuoJ2) RPA4257(nuoI2) RPA4258(nuoH2) RPA4259(nuoG2)
                 RPA4260(nuoF2) RPA4261(nuoE2) RPA4262(nuoCD) RPA4263(nuoB2)
                 RPA4264(nuoA2)
            RPB: RPB_0660 RPB_1347 RPB_1348 RPB_1349 RPB_1350 RPB_1351
                 RPB_1352 RPB_1353 RPB_1354 RPB_1355 RPB_1356 RPB_1357 RPB_1358
                 RPB_1359 RPB_2572 RPB_2573 RPB_2574 RPB_2575 RPB_2577 RPB_2579
                 RPB_2580 RPB_2581 RPB_2582 RPB_2583 RPB_2584 RPB_2585 RPB_2586
                 RPB_2587
            RPC: RPC_0437 RPC_2399 RPC_2400 RPC_2402 RPC_2404 RPC_2406
                 RPC_2408 RPC_2410 RPC_2411 RPC_2412 RPC_2413 RPC_2414 RPC_2415
                 RPC_2416 RPC_2417 RPC_4059 RPC_4060 RPC_4061 RPC_4062 RPC_4063
                 RPC_4064 RPC_4065 RPC_4066 RPC_4067 RPC_4068 RPC_4069 RPC_4070
                 RPC_4071 RPC_4501
            RPD: RPD_0173 RPD_0653 RPD_1328 RPD_1331 RPD_2878 RPD_2879
                 RPD_2882 RPD_2884 RPD_2885 RPD_2887
            RPE: RPE_0505 RPE_1710 RPE_1711 RPE_1712 RPE_1713 RPE_1714
                 RPE_1715 RPE_1716 RPE_1717 RPE_1718 RPE_1719 RPE_1720 RPE_1721
                 RPE_1722 RPE_2519 RPE_2520 RPE_2521 RPE_2523 RPE_2525 RPE_2527
                 RPE_2529 RPE_2530 RPE_2531 RPE_2532 RPE_2533 RPE_2534 RPE_2535
                 RPE_2536
            NWI: Nwi_0166 Nwi_1880 Nwi_1885 Nwi_1886 Nwi_1888
            NHA: Nham_0183 Nham_1172 Nham_2210 Nham_2211 Nham_2212 Nham_2213
                 Nham_2214 Nham_2216 Nham_2218 Nham_2221 Nham_4321
            BHE: BH00320 BH08820(nuoN) BH08830(nuoM) BH08840(nuoL)
                 BH08850(nuoK) BH08860(nuoJ) BH08870(nuoI) BH08880(nuoH)
                 BH08890(nuoG) BH08900(nuoF) BH08910(nuoE) BH08920(nuoD)
                 BH08930(nuoC) BH08940(nuoB) BH08950(nuoA)
            BQU: BQ00300 BQ05640(nuoA) BQ05650(nuoB) BQ05660(nuoC)
                 BQ05670(nuoD) BQ05680(nuoE) BQ05690(nuoF) BQ05700(nuoG)
                 BQ05710(nuoH) BQ05720(nuoI) BQ05730(nuoJ) BQ05740(nuoK)
                 BQ05750(nuoL) BQ05760(nuoM) BQ05770(nuoN)
            XAU: Xaut_1691
            CCR: CC_1937 CC_1938 CC_1939 CC_1940 CC_1941 CC_1942 CC_1945
                 CC_1946 CC_1947 CC_1950 CC_1952 CC_1954 CC_1955 CC_1956
                 CC_3604
            SIL: SPO2763(nuoN) SPO2764(nuoM) SPO2765(nuoL) SPO2766(nuoK)
                 SPO2767(nuoJ) SPO2770(nuoI) SPO2772(nuoH) SPO2774(nuoG)
                 SPO2777(nuoF) SPO2780(nuoE) SPO2782(nuoD) SPO2784(nuoC)
                 SPO2785(nuoB) SPO2786(nuoA) SPO3772
            SIT: TM1040_0741 TM1040_0744 TM1040_0746 TM1040_0748 TM1040_0751
                 TM1040_0753 TM1040_0754 TM1040_0756 TM1040_0757 TM1040_0832
                 TM1040_3191
            RSP: RSP_0100(nuoA) RSP_0101(nuoB) RSP_0102(nuoCD) RSP_0103(nuoE)
                 RSP_0104(nuoF) RSP_0105(nuoG) RSP_0106(nuoH) RSP_0107(nuoI)
                 RSP_0108(nuoJ) RSP_0109(nuoK) RSP_0110(nuoL) RSP_0112(nuoN)
                 RSP_1151 RSP_2512(nuoA) RSP_2513(nuoB) RSP_2514(nuoC)
                 RSP_2515(nuoD) RSP_2516(nuoE) RSP_2518(nuoF) RSP_2521(nuoG)
                 RSP_2522(nuoH) RSP_2523(nuoI) RSP_2525(nuoJ) RSP_2526(nuoK)
                 RSP_2527(nuoL) RSP_2529(nuoM) RSP_2530(nuoN)
            RSH: Rsph17029_1175 Rsph17029_1176 Rsph17029_1177 Rsph17029_1178
                 Rsph17029_1737 Rsph17029_1741
            RSQ: Rsph17025_2005
            JAN: Jann_1154 Jann_1171 Jann_1173 Jann_1176 Jann_1179 Jann_1183
                 Jann_1185 Jann_1259
            RDE: RD1_0065 RD1_1255 RD1_2855 RD1_3268(nuoN) RD1_3269(nuoM)
                 RD1_3270(nuoL) RD1_3271(nuoK) RD1_3273(nuoJ) RD1_3275(nuoI)
                 RD1_3278(nuoG) RD1_3285(nuoE) RD1_3292(nuoA) RD1_4145(nuo)
            PDE: Pden_2246 Pden_2247 Pden_2248 Pden_2249
            MMR: Mmar10_0113 Mmar10_1355 Mmar10_1356 Mmar10_1357 Mmar10_1358
                 Mmar10_1359 Mmar10_1360 Mmar10_1361 Mmar10_1362 Mmar10_1363
                 Mmar10_1364 Mmar10_1365 Mmar10_1366 Mmar10_1367 Mmar10_1368
            HNE: HNE_1742(nuoA) HNE_1743(nuoB) HNE_1744(nuoC) HNE_1745(nuoD)
                 HNE_1748(nuoE) HNE_1749(nuoF) HNE_1751(nuoG) HNE_1752(nuoH)
                 HNE_1753(nuoI) HNE_1754(nuoJ) HNE_1755(nuoK) HNE_1756(nuoL)
                 HNE_1757(nuoM) HNE_1758(nuoN)
            ZMO: ZMO1949
            NAR: Saro_2293 Saro_2303 Saro_2476
            SAL: Sala_1299 Sala_1300 Sala_1302 Sala_1303 Sala_1309 Sala_1311
            ELI: ELI_06625 ELI_06630 ELI_06640 ELI_06650 ELI_06665 ELI_06675
                 ELI_06685 ELI_06690 ELI_06695
            GOX: GOX1849
            GBE: GbCGDNIH1_0702 GbCGDNIH1_0708 GbCGDNIH1_1289 GbCGDNIH1_1290
                 GbCGDNIH1_1291 GbCGDNIH1_1292 GbCGDNIH1_1293 GbCGDNIH1_1294
                 GbCGDNIH1_1295 GbCGDNIH1_1296 GbCGDNIH1_1297 GbCGDNIH1_1298
                 GbCGDNIH1_1299 GbCGDNIH1_1300 GbCGDNIH1_1301 GbCGDNIH1_1302
                 GbCGDNIH1_1736
            ACR: Acry_1668
            RRU: Rru_A0316 Rru_A0321 Rru_A1425 Rru_A1555 Rru_A1557 Rru_A1558
                 Rru_A1559 Rru_A1562
            MAG: amb0169 amb2774 amb2775 amb2776 amb2777 amb2778 amb2779
                 amb2780 amb2781 amb2782 amb2783 amb2784 amb2785 amb2786
                 amb2787 amb3931
            MGM: Mmc1_0977 Mmc1_2206 Mmc1_2208 Mmc1_2209 Mmc1_3623 Mmc1_3625
                 Mmc1_3626 Mmc1_3627 Mmc1_3628 Mmc1_3629 Mmc1_3632 Mmc1_3634
                 Mmc1_3635
            ABA: Acid345_1287 Acid345_1288 Acid345_1289 Acid345_1292
                 Acid345_1293 Acid345_1294 Acid345_1295 Acid345_1296
                 Acid345_1306 Acid345_1307 Acid345_1308 Acid345_1309
                 Acid345_1312 Acid345_1313 Acid345_1314 Acid345_1315
                 Acid345_1845 Acid345_2252 Acid345_3358
            SUS: Acid_5318 Acid_5684
            BSU: BG10949(ndhF)
            BAN: BA3183(ndhF) BA5532(nuoN) BA5533(nuoM) BA5534(nuoL)
                 BA5535(nuoK) BA5536(nuoJ) BA5537(nuoI) BA5538(nuoH)
                 BA5539(nuoD) BA5540 BA5541(nuoB) BA5542(nuoA)
            BAR: GBAA3183(ndhF) GBAA5532(nuoN) GBAA5533(nuoM) GBAA5534(nuoL)
                 GBAA5535(nuoK) GBAA5536(nuoJ) GBAA5537(nuoI) GBAA5538(nuoH)
                 GBAA5539(nuoD) GBAA5540 GBAA5541(nuoB) GBAA5542(nuoA)
            BAA: BA_0386 BA_0387 BA_0388 BA_0389 BA_0390 BA_0391 BA_0392
                 BA_0393 BA_0394 BA_0395 BA_0396 BA_3692
            BAT: BAS2959 BAS5140 BAS5141 BAS5142 BAS5143 BAS5144 BAS5145
                 BAS5146 BAS5147 BAS5148 BAS5149 BAS5150
            BCE: BC3142 BC5291 BC5292 BC5293 BC5294 BC5295 BC5296 BC5297
                 BC5298 BC5299 BC5300 BC5301
            BCA: BCE_3191(ndhF) BCE_5415(nuoN) BCE_5416(nuoM) BCE_5417(nuoL)
                 BCE_5418(nuoK) BCE_5419(nuoJ) BCE_5420(nuoI) BCE_5421(nuoH)
                 BCE_5422(nuoD) BCE_5423 BCE_5424(nuoB) BCE_5425(nuoA)
            BCZ: BCZK2874(ndhF) BCZK4990(nuoN) BCZK4991(nuoM) BCZK4992(nuoL)
                 BCZK4993(nuoK) BCZK4994(nuoJ) BCZK4995(nuoI) BCZK4996(nuoH)
                 BCZK4997(nuoD) BCZK4998(nuoC) BCZK4999(nuoB) BCZK5000(nuoA)
            BTK: BT9727_2938(ndhF) BT9727_4972(nuoN) BT9727_4973(nuoM)
                 BT9727_4974(nuoL) BT9727_4975(nuoK) BT9727_4976(nuoJ)
                 BT9727_4977(nuoI) BT9727_4978(nuoH) BT9727_4979(nuoD)
                 BT9727_4980(nuoC) BT9727_4981(nuoB) BT9727_4982(nuoA)
            BTL: BALH_4794(nuoN) BALH_4798(nuoJ) BALH_4801(nuoC)
                 BALH_4802(nuoB)
            BLI: BL00918(ndhF)
            BLD: BLi00846(ndhF) BLi01934
            GKA: GK0442 GK3345 GK3346 GK3347 GK3348 GK3349 GK3350 GK3352
                 GK3353 GK3354 GK3355 GK3356
            SAU: SA0411(ndhF)
            SAV: SAV0452(ndhF)
            SAM: MW0407(ndhF)
            SAR: SAR0452
            SAS: SAS0410
            SAC: SACOL0494(nuoF)
            SAB: SAB0402 SAB0573
            SAA: SAUSA300_0425
            SAO: SAOUHSC_00412
            SEP: SE2333
            SER: SERP0084(nuoF)
            SHA: SH2561(ndhF)
            SSP: SSP2380
            EFA: EF1388 EF1389
            STH: STH1586(nuoA1) STH1587(nuoB1) STH1588(nuoC1) STH1589(nuoD1)
                 STH1590(nuoE1) STH1591(nuoF1) STH1592(nuoG1) STH1593(nuoH1)
                 STH1594(nuoI1) STH1595(nuoJ1) STH1596(nuoK1) STH1597(nuoL1)
                 STH1598(nuoN1) STH2767(nuoN2) STH2768(nuoM2) STH2769(nuoL2)
                 STH2770(nuoK2) STH2771(nuoJ2) STH2773(nuoH2) STH2774(nuoD2)
                 STH2775(nuoC2) STH2776(nuoA2) STH2777(nuoB2) STH404
            CTH: Cthe_3020
            CHY: CHY_0731(hydC) CHY_0732(hydB) CHY_1415 CHY_1417 CHY_1421
                 CHY_1422 CHY_1424
            DSY: DSY2578(nuoN) DSY2579(nuoM) DSY2580(nuoL) DSY2581(nuoK)
                 DSY2582(nuoJ) DSY2583(nuoI) DSY2584(nuoH) DSY2585(nuoD)
                 DSY2586(nuoC) DSY2587(nuoB) DSY2588(nuoA) DSY3969(nuoG)
                 DSY3970(nuoF) DSY3971(nuoE)
            DRM: Dred_2043
            SWO: Swol_0657 Swol_0784 Swol_1701
            TTE: TTE0123(nuoL) TTE0124(nuoH) TTE0125(nuoB) TTE0127(nuoD)
                 TTE0128(nuoI) TTE0890(nuoE) TTE0893(nuoF) TTE0894(nuoG)
            MTA: Moth_0980 Moth_0981 Moth_0986 Moth_1717 Moth_1886 Moth_1887
            MTU: Rv3145(nuoA) Rv3146(nuoB) Rv3147(nuoC) Rv3148(nuoD)
                 Rv3149(nuoE) Rv3150(nuoF) Rv3151(nuoG) Rv3152(nuoH)
                 Rv3153(nuoI) Rv3154(nuoJ) Rv3155(nuoK) Rv3156(nuoL)
                 Rv3157(nuoM) Rv3158(nuoN)
            MTC: MT3233(nuoA) MT3234(nuoB) MT3235(nuoC) MT3236(nuoD)
                 MT3237(nuoE) MT3238(nuoF) MT3239(nuoG) MT3240(nuoH)
                 MT3241(nuoI) MT3242(nuoJ) MT3243(nuoK) MT3244(nuoL)
                 MT3245(nuoM) MT3246(nuoN)
            MBO: Mb3169(nuoA) Mb3170(nuoB) Mb3171(nuoC) Mb3172(nuoD)
                 Mb3173(nuoE) Mb3174(nuoF) Mb3175(nuoG) Mb3176(nuoH)
                 Mb3177(nuoI) Mb3178(nuoJ) Mb3179(nuoK) Mb3180(nuoL)
                 Mb3181(nuoM) Mb3182(nuoN)
            MBB: BCG_3168(nuoA) BCG_3169(nuoB) BCG_3170(nuoC) BCG_3171(nuoD)
                 BCG_3172(nuoE) BCG_3173(nuoF) BCG_3174(nuoG) BCG_3175(nuoH)
                 BCG_3176(nuoI) BCG_3177(nuoJ) BCG_3178(nuoK) BCG_3179(nuoL)
                 BCG_3180(nuoM) BCG_3181(nuoN)
            MPA: MAP0095c(nuoI_1) MAP3201(nuoA) MAP3202(nuoB) MAP3203(nuoC)
                 MAP3204(nuoD) MAP3205(nuoE) MAP3206(nuoF) MAP3207(nuoG)
                 MAP3208(nuoH) MAP3209(nuoI_2) MAP3210(nuoJ) MAP3211(nuoK)
                 MAP3212(nuoL) MAP3213(nuoM) MAP3214(nuoN)
            MSM: MSMEG_2050(nuoN) MSMEG_2051(nuoM) MSMEG_2052(nuoL)
                 MSMEG_2053(nuoK) MSMEG_2054 MSMEG_2055(nuoI) MSMEG_2056(nuoH)
                 MSMEG_2057(nuoG) MSMEG_2058(nuoF) MSMEG_2059 MSMEG_2060(nuoD)
                 MSMEG_2061 MSMEG_2062(nuoB) MSMEG_2063(nuoA)
            MVA: Mvan_1884
            MGI: Mflv_4482
            MMC: Mmcs_1564 Mmcs_1565 Mmcs_1566 Mmcs_1570 Mmcs_1571 Mmcs_1572
                 Mmcs_1573 Mmcs_1574 Mmcs_1576 Mmcs_1577 Mmcs_1578 Mmcs_1579
                 Mmcs_1580
            MJL: Mjls_1549
            CGB: cg0326(nuoL)
            CJK: jk1986(mnhB) jk1988(mnhD)
            NFA: nfa26550(nuoN) nfa26560(nuoM) nfa26570(nuoL) nfa26580(nuoK)
                 nfa26590(nuoJ) nfa26600(nuoH) nfa26610(nuoG) nfa26620(nuoF)
                 nfa26630(nuoE) nfa26640(nuoD) nfa26650(nuoC) nfa26660(nuoB)
                 nfa26670(nuoA)
            RHA: RHA1_ro05909 RHA1_ro05910 RHA1_ro05911 RHA1_ro05912
                 RHA1_ro05913 RHA1_ro05914 RHA1_ro05915 RHA1_ro05916
                 RHA1_ro05917 RHA1_ro05918 RHA1_ro05919 RHA1_ro05920
                 RHA1_ro05921 RHA1_ro05922
            SCO: SCO3392(nuoD2) SCO4562(nuoA) SCO4563(nuoB) SCO4564(nuoC)
                 SCO4565(nuoD) SCO4566(nuoE) SCO4567(nuoF) SCO4568(nuoG)
                 SCO4569(nuoH) SCO4570(nuoI) SCO4571(nuoJ) SCO4572(nuoK)
                 SCO4573(nuoL) SCO4574(nuoM) SCO4575(nuoN) SCO4599(nuoA2)
                 SCO4600(nuoB2) SCO4602(nuoH2) SCO4603(nuoI2) SCO4604(nuoJ2)
                 SCO4605(nuoK2) SCO4606(nuoL2) SCO4607(nuoM2) SCO4608(nuoN2)
                 SCO6560(SC4B5.10c)
            SMA: SAV1835(nuoF2) SAV4678(nuoD2) SAV4837(nuoA1) SAV4838(nuoB1)
                 SAV4839(nuoC) SAV4840(nuoD1) SAV4841(nuoE) SAV4842(nuoF1)
                 SAV4843(nuoG1) SAV4844(nuoH1) SAV4845(nuoI1) SAV4846(nuoJ1)
                 SAV4847(nuoK1) SAV4848(nuoL1) SAV4849(nuoM1) SAV4850(nuoN1)
                 SAV4881(nuoA2) SAV4882(nuoB2) SAV4884(nuoH2) SAV4885(nuoI2)
                 SAV4886(nuoJ2) SAV4887(nuoK2) SAV4888(nuoL2) SAV4889(nuoM2)
                 SAV4890(nuoN2)
            CMI: CMM_1087(mnhAB) CMM_1089(mnhD)
            PAC: PPA0276 PPA1922 PPA1923 PPA1924 PPA1925 PPA1926 PPA1928
                 PPA1929 PPA1930 PPA1931 PPA1932 PPA1933 PPA1934 PPA1935
                 PPA1936
            NCA: Noca_0521 Noca_0523
            TFU: Tfu_2685 Tfu_2686 Tfu_2687 Tfu_2688 Tfu_2689 Tfu_2691
                 Tfu_2693 Tfu_2695
            FAL: FRAAL1032(nuoA) FRAAL1033(nuoB) FRAAL1034(nuoC)
                 FRAAL1035(nuoD) FRAAL1036(nuoE) FRAAL1037(nuoF)
                 FRAAL1038(nuoG) FRAAL1039(nuoH) FRAAL1040(nuoI)
                 FRAAL1041(nuoJ) FRAAL1042(nuoK) FRAAL1043(nuoL)
                 FRAAL1044(nuoM) FRAAL1045(nuoN)
            ACE: Acel_0267 Acel_0268 Acel_0269 Acel_0271 Acel_0273 Acel_0274
                 Acel_0275 Acel_0276 Acel_0277
            SEN: SACE_2433 SACE_6889(nuoN) SACE_6890(nuoM) SACE_6891(nuoL)
                 SACE_6892(nuoK) SACE_6893(nuoJ) SACE_6894(nuoI)
                 SACE_6895(nuoH) SACE_6896(nuoG) SACE_6897(nuoF)
                 SACE_6898(nuoE) SACE_6899(nuoD) SACE_6900(nuoC)
                 SACE_6901(nuoB) SACE_6902(nuoA)
            RXY: Rxyl_1625 Rxyl_1627 Rxyl_1628 Rxyl_1629 Rxyl_1630 Rxyl_1631
                 Rxyl_1632 Rxyl_1633 Rxyl_1634
            RBA: RB10313(ndhF) RB1134(ndhF)
            PCU: pc0559(nuoA) pc0560(nuoB) pc0561(nuoC) pc0562(nuoD)
                 pc0563(nuoE) pc0564(nuoF) pc0565(nuoG) pc0566(nuoH)
                 pc0567(nuoI) pc0568(nuoJ) pc0569(nuoK) pc0570(nuoL)
                 pc0571(nuoM) pc0572(nuoN)
            LIL: LA0160(nuoG) LA0161(nuoI) LA0884(nuoN) LA0885(nuoM)
                 LA0886(nuoL) LA0887(nuoK) LA0888(nuoJ) LA0889(nuoH)
                 LA0890(nuoF) LA0891(nuoE) LA0892(nuoD) LA0893(nuoC)
                 LA0894(nuoB) LA0895(nuoA)
            LIC: LIC10141(nuoG) LIC10142(nuoI) LIC12741(nuoA) LIC12742(nuoB)
                 LIC12743(nuoC) LIC12744(nuoD2) LIC12745(nuoE) LIC12746(nuoF)
                 LIC12747(nuoH) LIC12748(nuoJ) LIC12749(nuoK) LIC12750(nuoL)
                 LIC12751(nuoM) LIC12752(nuoN)
            LBJ: LBJ_0137(nuoG) LBJ_0138(nuoI) LBJ_0501(nuoA) LBJ_0502(nuoB)
                 LBJ_0503(nuoC) LBJ_0504(nuoD) LBJ_0505(nuoE) LBJ_0506(nuoF)
                 LBJ_0507(nuoH) LBJ_0508(nuoJ) LBJ_0509(nuoK) LBJ_0510(nuoL)
                 LBJ_0511(nuoM) LBJ_0512(nuoN)
            LBL: LBL_2567(nuoN) LBL_2568(nuoM) LBL_2569(nuoL) LBL_2570(nuoK)
                 LBL_2571(nuoJ) LBL_2572(nuoH) LBL_2573(nuoF) LBL_2574(nuoE)
                 LBL_2575(nuoD) LBL_2576(nuoC) LBL_2577(nuoB) LBL_2578(nuoA)
                 LBL_2886 LBL_2945(nuoI) LBL_2946(nuoG)
            SYN: sll0026(ndhF4) sll0027(ndhD4) sll0223(ndhB) sll0519(ndhA)
                 sll0520(ndhI) sll0521(ndhG) sll0522(ndhE) sll1220(hoxE)
                 sll1221(hoxF) sll1223(hoxU) sll1262(ndhN) sll1732(ndhF3)
                 sll1733(ndhD3) slr0261(ndhH) slr0331(ndhD1) slr0844(ndhF1)
                 slr1279(ndhC) slr1280(ndhK) slr1281(ndhJ) slr1291(ndhD2)
                 slr1623(ndhM) ssr1386(ndhL)
            SYW: SYNW0207(ndhC) SYNW0208(ndhK) SYNW0209(ndhJ) SYNW1482(ndhD3)
                 SYNW1521 SYNW1710(ndhD2) SYNW1711(ndhF1) SYNW1873(ndhB)
                 SYNW2066 SYNW2258 SYNW2262(ndhF2) SYNW2263(ndhD1)
                 SYNW2271(ndhE) SYNW2272(ndhG) SYNW2273(ndhI) SYNW2274(ndhA)
                 SYNW2299(ndhH)
            SYC: syc0117_d(ndhD) syc0140_d(ndhB) syc0207_c(ndhE)
                 syc0208_c(ndhG) syc0209_c(ndhI) syc0210_c(ndhA)
                 syc0368_c(ndhJ) syc0369_c(ndhK) syc0370_c(ndhC)
                 syc0915_c(ndhD4) syc1104_d(ndhL) syc1204_d(ndhF4)
                 syc1234_c(hoxF) syc1235_c syc1553_d(hoxU) syc1864_c
                 syc2001_c(ndhD3) syc2002_c(ndhF3) syc2114_d syc2119_d(ndhF)
                 syc2120_d(ndhD) syc2348_c(ndhH)
            SYF: Synpcc7942_0309 Synpcc7942_0609 Synpcc7942_1180
                 Synpcc7942_1181 Synpcc7942_1182 Synpcc7942_1343
                 Synpcc7942_1344 Synpcc7942_1345 Synpcc7942_1346
                 Synpcc7942_1415 Synpcc7942_1439 Synpcc7942_1743
                 Synpcc7942_1976 Synpcc7942_1977 Synpcc7942_1982
                 Synpcc7942_2091 Synpcc7942_2234 Synpcc7942_2557
            SYD: Syncc9605_0203 Syncc9605_0204 Syncc9605_0205 Syncc9605_0377
                 Syncc9605_0759 Syncc9605_0760 Syncc9605_2396 Syncc9605_2409
                 Syncc9605_2410 Syncc9605_2411 Syncc9605_2412 Syncc9605_2432
            SYE: Syncc9902_0230 Syncc9902_0231 Syncc9902_0232 Syncc9902_0280
                 Syncc9902_0281 Syncc9902_0282 Syncc9902_0283 Syncc9902_0297
                 Syncc9902_1606 Syncc9902_1607 Syncc9902_1953 Syncc9902_2112
            SYG: sync_0242 sync_0243 sync_0244 sync_1870(ndhD) sync_1912(ndhL)
                 sync_1958 sync_1959 sync_2113 sync_2613 sync_2614 sync_2622
                 sync_2623 sync_2624(ndhI) sync_2625 sync_2648
            SYR: SynRCC307_0213(ndhC) SynRCC307_0214(ndhK)
                 SynRCC307_0215(ndhJ) SynRCC307_0231(ndhD) SynRCC307_0233(ndhF)
                 SynRCC307_0659(ndhB) SynRCC307_0827(ndhF) SynRCC307_0828(ndhD)
                 SynRCC307_0942(ndhD) SynRCC307_2257(ndhH) SynRCC307_2277(ndhA)
                 SynRCC307_2278(ndhI) SynRCC307_2279(ndhG) SynRCC307_2280(ndhE)
            SYX: SynWH7803_0685(ndhF) SynWH7803_0686(ndhD)
                 SynWH7803_1884(ndhB) SynWH7803_2278(ndhF) SynWH7803_2280(ndhD)
                 SynWH7803_2288(ndhE) SynWH7803_2289(ndhG) SynWH7803_2290(ndhI)
                 SynWH7803_2291(ndhA)
            CYA: CYA_0520 CYA_0639 CYA_0640 CYA_0744 CYA_0745 CYA_0747
                 CYA_1484 CYA_1593 CYA_1594 CYA_1630 CYA_1631 CYA_1755 CYA_1915
                 CYA_1994 CYA_1995 CYA_1996 CYA_2069 CYA_2391
            CYB: CYB_0115 CYB_0208 CYB_0298 CYB_0644 CYB_0869 CYB_0870
                 CYB_0872 CYB_1278 CYB_1279 CYB_1471 CYB_1811 CYB_1812 CYB_2004
                 CYB_2332 CYB_2333 CYB_2334 CYB_2875 CYB_2876
            TEL: tll0045(ndhB) tll0447 tll0719(ndhD1) tll0720(ndhF1)
                 tlr0667(ndhA) tlr0668(ndhI) tlr0669(ndhG) tlr0670(ndhE)
                 tlr0705(ndhK) tlr0904(ndhF3) tlr0905(ndhD3) tlr1130
                 tlr1288(ndhH) tlr1429(ndhC) tlr1430(ndhJ) tlr1819(ndhD2)
                 tlr2124(ndhF4) tlr2125(ndhD4) tsr0706(ndhL)
            GVI: gll0652(ndhE) gll0653(ndhG) gll0654(ndhI) gll1584(ndhA)
                 gll2082(ndhD4) gll2083(ndhF4) gll2383(ndhH) gll2536(ndhD)
                 gll3635 gll3770 glr0218(ndhF1) glr0219(ndhD1) glr0748(ndhC)
                 glr0749(ndhK) glr0750(ndhJ) glr1003(ndhF3) glr1004(ndhD3)
                 glr1522 glr2372(ndhH) glr2379(ndhK) glr2380(ndhJ)
                 glr2599(ndhF) glr3120(ndhB)
            ANA: all1732 all3840(ndhJ) all3841(ndhK) all3842(ndhC)
                 all4883(ndhB) alr0223(ndhA) alr0224(ndhI) alr0225(ndhG)
                 alr0226(ndhE) alr0348(ndhD2a) alr0751(hoxE) alr0752(hoxF)
                 alr0762(hoxU) alr0869(ndhF4) alr0870(ndhD4) alr3355(ndhH)
                 alr3956(ndhF1) alr3957(ndhD1) alr4156(ndhF3) alr4157(ndhD3)
                 alr4216 alr5050(ndhD2)
            AVA: Ava_0303 Ava_0690 Ava_1745 Ava_1858 Ava_1860 Ava_2714
                 Ava_2717 Ava_2796 Ava_3198 Ava_4473 Ava_4474
            PMA: Pro0168 Pro0172(ndhF) Pro0173(ndhD) Pro0181(ndhE)
                 Pro0182(ndhG) Pro0183(ndhI) Pro0184(ndhA) Pro0197(ndhH)
                 Pro0323(ndhJ) Pro0324(ndhK) Pro0325(ndhC) Pro0431(ndhB)
                 Pro1067(ndhD) Pro1713
            PMM: PMM0145 PMM0149(ndhF) PMM0150(ndhD) PMM0157(ndhE)
                 PMM0158(ndhG) PMM0159(ndhI) PMM0160(ndhA) PMM0172(ndhH)
                 PMM0292(ndhJ) PMM0293(ndhK) PMM0294(ndhC) PMM0435(ndhB)
                 PMM0570(ndhL) PMM0594(ndhD) PMM1559
            PMT: PMT0427(ndhD) PMT0848(ndhF) PMT1354(ndhB) PMT1731
                 PMT1891(ndhJ) PMT1892(ndhK) PMT1893(ndhC) PMT2005
                 PMT2009(ndhF) PMT2010(ndhD) PMT2017(ndhE) PMT2018(ndhG)
                 PMT2019(ndhI) PMT2020(ndhA) PMT2049(ndhH)
            PMN: PMN2A_1130 PMN2A_1511 PMN2A_1524 PMN2A_1525 PMN2A_1526
                 PMN2A_1527 PMN2A_1540 PMN2A_1658 PMN2A_1660
            PMI: PMT9312_0147 PMT9312_0151 PMT9312_0152 PMT9312_0159
                 PMT9312_0160 PMT9312_0161 PMT9312_0162 PMT9312_0174
                 PMT9312_0294 PMT9312_0295 PMT9312_0296 PMT9312_0570
                 PMT9312_1651
            PMB: A9601_01621 A9601_01661(ndhF) A9601_01671 A9601_01751(ndhE)
                 A9601_01761(ndhG) A9601_01771(ndhI) A9601_01781(ndhA)
                 A9601_01901(ndhH) A9601_03151(ndhJ) A9601_03161(ndhK)
                 A9601_03171(ndhC) A9601_04901(ndhB) A9601_06261 A9601_06501
                 A9601_17661
            PMC: P9515_01731 P9515_01771(ndhF) P9515_01781 P9515_01861(ndhE)
                 P9515_01871(ndhG) P9515_01881(ndhI) P9515_01891(ndhA)
                 P9515_02011(ndhH) P9515_03251(ndhJ) P9515_03261(ndhK)
                 P9515_03271(ndhC) P9515_04971(ndhB) P9515_06351(ndhL)
                 P9515_06591 P9515_17411
            PMF: P9303_06291(ndhB) P9303_13511 P9303_18141 P9303_18571
                 P9303_23011 P9303_25241(ndhJ) P9303_25251(ndhK)
                 P9303_25261(ndhC) P9303_26661 P9303_26701(ndhF) P9303_26711
                 P9303_26871(ndhE) P9303_26881(ndhG) P9303_26891(ndhI)
                 P9303_26911(ndhA) P9303_27241(ndhH)
            PMG: P9301_01641 P9301_01681(ndhF) P9301_01691 P9301_01771(ndhE)
                 P9301_01781(ndhG) P9301_01791(ndhI) P9301_01801(ndhA)
                 P9301_01921(ndhH) P9301_03161(ndhJ) P9301_03171(ndhK)
                 P9301_03181(ndhC) P9301_04591(ndhB) P9301_05961 P9301_06201
                 P9301_17501
            PMH: P9215_01661 P9215_01671 P9215_01751 P9215_01761 P9215_01781
                 P9215_03191 P9215_05141
            PME: NATL1_02171 NATL1_02211(ndhF) NATL1_02221 NATL1_02301(ndhE)
                 NATL1_02311(ndhG) NATL1_02321(ndhI) NATL1_02331(ndhA)
                 NATL1_02471(ndhH) NATL1_03721(ndhJ) NATL1_03731(ndhK)
                 NATL1_03741(ndhC) NATL1_06251 NATL1_06501 NATL1_20041
            TER: Tery_1576 Tery_1577 Tery_1578 Tery_1579 Tery_2883 Tery_3013
                 Tery_4815
            BTH: BT_0123 BT_0124 BT_0125 BT_4058 BT_4059 BT_4060 BT_4061
                 BT_4062 BT_4063 BT_4064 BT_4065 BT_4066 BT_4067
            BFR: BF0860 BF0861 BF0862 BF0863 BF0864 BF0865 BF0866 BF0867
                 BF0868 BF0869
            BFS: BF0783(nuoN) BF0784(nuoM) BF0785(nuoL) BF0786(nuoK)
                 BF0787(nuoJ) BF0788(nuoI) BF0789(nuoH)
            SRU: SRU_0393 SRU_0394 SRU_0396(nuoD) SRU_0397 SRU_0398
                 SRU_0400(nuoG) SRU_0496(nuoI) SRU_1445(nuoL) SRU_1446(nuoM)
                 SRU_2058
            CHU: CHU_0510(hycG) CHU_0511(nuoC) CHU_0512(nuoD) CHU_1369(nuoN)
                 CHU_1370(nuoM) CHU_1371(nuoL) CHU_1372(nuoK) CHU_1373(nuoJ)
                 CHU_1374(nuoI) CHU_1375(nuoH) CHU_1376(nuoG) CHU_1377(nuoF)
                 CHU_1378(nuoE) CHU_1379(nuoD) CHU_1380(nuoC) CHU_1381
                 CHU_1382(nuoA) CHU_2613(nuoN) CHU_2614(nuoM) CHU_2616(nuoL)
                 CHU_2619(hyfH) CHU_2620(hyfC)
            CTE: CT0766(ndhC) CT0767(ndhH) CT0768(ndhJ) CT0769(ndhK)
                 CT0770(ndhA) CT0771(ndhI) CT0772(ndhG) CT0773(ndhE)
                 CT0774(ndhF) CT0775(ndhD) CT0776(ndhB)
            CCH: Cag_0634 Cag_0637 Cag_0638 Cag_0640 Cag_0641
            CPH: Cpha266_0964
            PVI: Cvib_1090 Cvib_1092
            PLT: Plut_0743 Plut_0744 Plut_0746 Plut_0747 Plut_0749 Plut_0750
            DET: DET0145 DET0146 DET0147 DET0446 DET0728 DET0729 DET0923
                 DET0924 DET0925 DET0926 DET0927 DET0928 DET0929 DET0930
                 DET0931 DET0932 DET0933 DET1324
            DEH: cbdb_A1269 cbdb_A169(hymA) cbdb_A170(hymB) cbdb_A171(hymC)
                 cbdb_A403 cbdb_A683(hymA) cbdb_A684(hymB) cbdb_A845(hymA)
                 cbdb_A874 cbdb_A875(nuoB) cbdb_A876(nuoC) cbdb_A877(nuoD)
                 cbdb_A879(nuoH) cbdb_A880 cbdb_A881 cbdb_A882 cbdb_A883
                 cbdb_A884(nuoM) cbdb_A885(nuoN)
            DRA: DR_1492 DR_1493 DR_1494 DR_1495 DR_1496 DR_1497 DR_1498
                 DR_1499 DR_1500 DR_1501 DR_1503 DR_1504 DR_1505 DR_1506
                 DR_1980
            DGE: Dgeo_0898 Dgeo_0909 Dgeo_0910 Dgeo_0911 Dgeo_0912 Dgeo_0913
                 Dgeo_0915 Dgeo_0916 Dgeo_0917 Dgeo_0919 Dgeo_0921 Dgeo_0922
            TTH: TTC1907 TTC1908 TTC1909 TTC1910 TTC1911 TTC1912 TTC1913
                 TTC1914 TTC1915 TTC1916 TTC1917 TTC1918 TTC1919 TTC1920
                 TT_P0054
            TTJ: TTHA0084 TTHA0085 TTHA0086 TTHA0087 TTHA0088 TTHA0089
                 TTHA0090 TTHA0091 TTHA0092 TTHA0093 TTHA0094 TTHA0095 TTHA0096
                 TTHA0097 TTHB098
            AAE: aq_1310(nuoA2) aq_1312(nuoB) aq_1314(nuoD2) aq_1315(nuoH1)
                 aq_1317(nuoI1) aq_1318(nuoJ1) aq_1319(nuoK1) aq_1320(nuoL1)
                 aq_1321(nuoM1) aq_1322(nuoN1) aq_135(nueM) aq_1373(nuoH2)
                 aq_1374(nuoH3) aq_1375(nuoI2) aq_1377(nuoJ2) aq_1378(nuoK2)
                 aq_1379(nuoL3) aq_1382(nuoM2) aq_1383(nuoN2) aq_1385(nuoA1)
                 aq_437(nuoG) aq_551(nuoD1) aq_573(nuoF) aq_574(nuoE)
                 aq_866(nuoL2)
            TMA: TM0010 TM0011 TM0012 TM0201 TM0228 TM1211 TM1212 TM1213
                 TM1214 TM1215 TM1216 TM1424 TM1425 TM1426
            MJA: MJ0520
            MMP: MMP1153(ehbN) MMP1461(ehaN) MMP1462(ehaO) MMP1622(ehbM)
            MMQ: MmarC5_0116
            MMZ: MmarC7_0702
            MAE: Maeo_0366
            MVN: Mevan_0768
            MAC: MA1495(fpoA) MA1496(fpoB) MA1497(fpoC) MA1498(fpoD)
                 MA1499(fpoH) MA1500(fpoI) MA1501(fpoJ) MA1502(fpoJ)
                 MA1503(fpoK) MA1504(fpoL) MA1505(fpoM) MA1506(fpoN)
            MBA: Mbar_A3401 Mbar_A3402(fpoM) Mbar_A3403 Mbar_A3404(fpoK)
                 Mbar_A3405 Mbar_A3406(fpoJ) Mbar_A3407(fpoI) Mbar_A3408(fpoH)
                 Mbar_A3409(fpoD) Mbar_A3410(fpoC) Mbar_A3411(fpoB) Mbar_A3412
            MMA: MM_2480(fpoN) MM_2481(fpoM) MM_2482(fpoL) MM_2483(fpoK)
                 MM_2484(fpoJ) MM_2485(fpoJ) MM_2486(fpoI) MM_2487(fpoH)
                 MM_2488(fpoD) MM_2489(fpoC) MM_2490(fpoB) MM_2491(fpoA)
            MBU: Mbur_1292 Mbur_1293 Mbur_1294 Mbur_1295 Mbur_1297
            MTP: Mthe_1052
            MHU: Mhun_2590
            MEM: Memar_1184
            MBN: Mboo_0028
            MTH: MTH1237 MTH1246 MTH1548 MTH1549 MTH393
            MSI: Msm_0317 Msm_0783
            AFU: AF1823 AF1824 AF1825(nuoM) AF1826(nuoL) AF1827 AF1828 AF1829
                 AF1830(nuoD) AF1831 AF1832a
            HAL: VNG0635G(nolB) VNG0636G(ndhG1) VNG0637G(ndhG5)
                 VNG0639G(ndhG4) VNG0640G(nolD) VNG0641C VNG0643G(nolC)
                 VNG0646G(nuoL) VNG0647G(nuoM) VNG0648G(ndhG3) VNG1932G(nolA)
            HMA: pNG7189(ndhG1) pNG7319(nuoF) rrnAC1448(nuoB) rrnAC1449(ndHG5)
                 rrnAC1450(ndhG4) rrnAC1451(nolD) rrnAC1454(nolC)
                 rrnAC1455(nuoL2) rrnAC1456(ndhD) rrnAC1458(ndhG3)
                 rrnAC2023(nuoC) rrnAC3285(nolA)
            HWA: HQ1637A(nuoA) HQ1638A(nuoB) HQ1639A(nuoCD) HQ1640A(nuoH)
                 HQ1641A(nuoI) HQ1643A(nuoJ) HQ1644A(nuoJ2) HQ1645A(nuoK)
                 HQ1646A(nuoL) HQ1647A(nuoM) HQ1648A(nuoN) HQ2621A(nuoL)
                 HQ3146A(nolA)
            NPH: NP2292A(nuoA) NP2294A(nuoB) NP2296A(nuoCD) NP2298A(nuoH)
                 NP2300A(nuoI) NP2304A(nuoJ1) NP2308A(nuoK) NP2310A(nuoL)
                 NP2312A(nuoM) NP2406A(nolA_1) NP5056A(phaA)
            TAC: Ta0959 Ta0960 Ta0961 Ta0962 Ta0963 Ta0964 Ta0965 Ta0966
                 Ta0967m Ta0968 Ta0969m Ta0970m
            TVO: TVN1104 TVN1105 TVN1106 TVN1107 TVN1108 TVN1110 TVN1111
                 TVN1112 TVN1113 TVN1114 TVN1115 TVN1116
            PTO: PTO0929 PTO0930 PTO1028 PTO1029 PTO1400 PTO1401 PTO1402
                 PTO1403 PTO1404 PTO1405 PTO1406 PTO1407 PTO1408 PTO1409
            PHO: PH1446 PH1447 PH1448 PH1449 PH1450 PH1451 PH1452
            PAB: PAB0490(nuoM) PAB0492(nuoH) PAB0493(nuoB) PAB0494(nuoC)
                 PAB0495(nuoD) PAB0496(nuoI) PAB2416(nuoN)
            PFU: PF1441 PF1442 PF1443 PF1444 PF1445 PF1446 PF1447
            TKO: TK1214 TK1215 TK1216 TK1217 TK1218 TK1219 TK1220 TK1221
                 TK1613 TK1614
            APE: APE_1410.1 APE_1411.1 APE_1415 APE_1417.1 APE_1418.1
                 APE_1419.1 APE_1421.1 APE_1422 APE_1426 APE_1428.1 APE_1430.1
            SMR: Smar_0020
            HBU: Hbut_0186 Hbut_0187
            SSO: SSO0322(nuoA) SSO0323(nuoC) SSO0324(nuoD) SSO0325(nuoH)
                 SSO0326(nuoI) SSO0327(nuoJ) SSO0328(nuoL) SSO0329(nuoN)
                 SSO0665(nuoB)
            STO: ST1527 ST2216 ST2217 ST2218 ST2219 ST2220 ST2221 ST2222
                 ST2223 STS234
            SAI: Saci_1644 Saci_2338(nqo14) Saci_2339(nqo12) Saci_2340(ndhE)
                 Saci_2341 Saci_2342 Saci_2343(ndhA) Saci_2344 Saci_2345
                 Saci_2346(nou3)
            PAI: PAE1567 PAE1568 PAE1576 PAE1577 PAE1578 PAE1580 PAE1581
                 PAE1582 PAE2926 PAE2928 PAE3520
            PIS: Pisl_0331 Pisl_1634
            PCL: Pcal_0514 Pcal_2045
            PAS: Pars_2120 Pars_2272
            TPE: Tpen_1081
STRUCTURES  PDB: 1S3A  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.5.3
            ExPASy - ENZYME nomenclature database: 1.6.5.3
            ExplorEnz - The Enzyme Database: 1.6.5.3
            ERGO genome analysis and discovery system: 1.6.5.3
            BRENDA, the Enzyme Database: 1.6.5.3
            CAS: 9028-04-0
///
ENTRY       EC 1.6.5.4                  Enzyme
NAME        monodehydroascorbate reductase (NADH);
            NADH:semidehydroascorbic acid oxidoreductase;
            MDHA;
            semidehydroascorbate reductase;
            AFR;
            AFR-reductase;
            ascorbic free radical reductase;
            ascorbate free radical reductase;
            SOR;
            MDAsA reductase (NADPH) ;
            SDA reductase;
            NADH:ascorbate radical oxidoreductase;
            NADH-semidehydroascorbate oxidoreductase;
            ascorbate free-radical reductase ;
            NADH:AFR oxidoreductase;
            monodehydroascorbate reductase (NADH2)
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a quinone or similar compound as acceptor
SYSNAME     NADH:monodehydroascorbate oxidoreductase
REACTION    NADH + H+ + 2 monodehydroascorbate = NAD+ + 2 ascorbate [RN:R00095]
ALL_REAC    R00095
SUBSTRATE   NADH [CPD:C00004];
            H+ [CPD:C00080];
            monodehydroascorbate [CPD:C01041]
PRODUCT     NAD+ [CPD:C00003];
            ascorbate [CPD:C00072]
REFERENCE   1  [PMID:4405497]
  AUTHORS   Schulze HU, Schott HH, Staudinger H.
  TITLE     [The isolation and characterization of a NADH: semidehydroascorbic
            acid oxidoreductase from Neurospora crassa]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 353 (1972) 1931-42.
  ORGANISM  Neurospora crassa [GN:dncr]
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K08232  monodehydroascorbate reductase (NADH)
GENES       ATH: AT3G09940(MDHAR) AT3G27820(ATMDAR4) AT3G52880(ATMDAR1)
                 AT5G03630
            OSA: 4330469 4344670 4346299 4347885
            CME: CMT414C
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.5.4
            ExPASy - ENZYME nomenclature database: 1.6.5.4
            ExplorEnz - The Enzyme Database: 1.6.5.4
            ERGO genome analysis and discovery system: 1.6.5.4
            BRENDA, the Enzyme Database: 1.6.5.4
            CAS: 9029-26-9
///
ENTRY       EC 1.6.5.5                  Enzyme
NAME        NADPH:quinone reductase;
            NADPH2:quinone reductase
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a quinone or similar compound as acceptor
SYSNAME     NADPH:quinone oxidoreductase
REACTION    NADPH + H+ + quinone = NADP+ + semiquinone [RN:R02364]
ALL_REAC    R02364
SUBSTRATE   NADPH [CPD:C00005];
            H+ [CPD:C00080];
            quinone [CPD:C00472]
PRODUCT     NADP+ [CPD:C00006];
            semiquinone [CPD:C05309]
COMMENT     A zinc enzyme, specific for NADPH. Catalyses the one-electron
            reduction of certain quinones; orthoquinones are the best
            substrates. Dicoumarol [cf. EC 1.6.5.2 NAD(P)H dehydrogenase
            (quinone)] and nitrofurantoin are competitive inhibitors with
            respect to the quinone substrate. In some mammals the enzyme is
            abundant in the lens of the eye, where it is identified with the
            protein zeta-crystallin.
REFERENCE   1  [PMID:1370456]
  AUTHORS   Rao PV, Krishna CM, Zigler JS Jr.
  TITLE     Identification and characterization of the enzymatic activity of
            zeta-crystallin from guinea pig lens. A novel NADPH:quinone
            oxidoreductase.
  JOURNAL   J. Biol. Chem. 267 (1992) 96-102.
  ORGANISM  guinea pig
ORTHOLOGY   KO: K00344  NADPH2:quinone reductase
GENES       HSA: 1429(CRYZ)
            MMU: 12972(Cryz)
            RNO: 362061(Cryz)
            CFA: 476107(LOC476107)
            BTA: 281093(CRYZ)
            GGA: 772289(RCJMB04_33h20)
            CEL: F39B2.3
            ATH: AT3G56460
            OSA: 4331066 4331289 4338383
            SCE: YBR046C(ZTA1)
            AGO: AGOS_ABL090W
            PIC: PICST_44171(IFR1) PICST_53084(ETR1) PICST_74654(QOR1)
                 PICST_84928(ZTA1)
            CGR: CAGL0H09944g
            SPO: SPBC16A3.02c
            ANI: AN0158.2 AN8515.2 AN9075.2
            AFM: AFUA_1G02090 AFUA_3G13610 AFUA_5G10220 AFUA_5G11430
                 AFUA_7G02400 AFUA_8G01420
            AOR: AO090005000678 AO090011000128 AO090026000695 AO090038000620
            CNE: CNB01200
            UMA: UM00045.1 UM03068.1
            TET: TTHERM_00016280 TTHERM_00077600 TTHERM_00189520
                 TTHERM_00775980
            TBR: Tb09.160.5260 Tb10.6k15.0820 Tb927.3.4990 Tb927.7.7410
                 Tb927.8.3970
            TCR: 506485.80 508409.160 510141.10 510265.10 510311.90
            LMA: LmjF03.0570
            ECO: b4051(qor)
            ECJ: JW4011(qor)
            ECE: Z5649(qor)
            ECS: ECs5033
            ECC: c5020(qor)
            ECI: UTI89_C4619(qor)
            ECP: ECP_4267
            ECV: APECO1_2421(qor)
            ECW: EcE24377A_4603(qor)
            ECX: EcHS_A4291(qor)
            STY: STY4441(qor)
            STT: t4151(qor)
            SPT: SPA4062(qor)
            SEC: SC4124(qor)
            STM: STM4245(qor)
            YPE: YPO0319(qor)
            YPK: y0576(qor)
            YPM: YP_0474(qor1)
            YPA: YPA_3966
            YPN: YPN_3351
            YPS: YPTB0374(qor)
            YPI: YpsIP31758_3766
            SFL: SF4153(qor)
            SFX: S3576(qor)
            SFV: SFV_4162(qor)
            SSN: SSON_4231(qor)
            SBO: SBO_4066(qor)
            SDY: SDY_4523(qor)
            ECA: ECA3663(qor)
            PLU: plu4360(qor)
            XCC: XCC0934
            XCB: XC_3301
            XCV: XCV1041
            XAC: XAC1011
            XOO: XOO3697
            XOM: XOO_3491(XOO3491)
            VCH: VC0552
            VCO: VC0395_A0087
            VVU: VV1_1603
            VVY: VV2797
            VPA: VP2542
            VFI: VF0978
            PPR: PBPRB0221
            PAE: PA0023(qor) PA2680 PA5234
            PAU: PA14_00250(qor) PA14_29460(qor)
            PPU: PP_0072(qor-1) PP_3606(qor-2) PP_5210
            PPF: Pput_2719
            PST: PSPTO_0173(qor) PSPTO_5231
            PSB: Psyr_0023 Psyr_0313
            PSP: PSPPH_0025(qor1) PSPPH_0298(qor2)
            PFL: PFL_0026(qor) PFL_2346(qor) PFL_5977(fadB4)
            PFO: Pfl_0021 Pfl_2252 Pfl_5445
            PEN: PSEEN0029(qor) PSEEN2630 PSEEN2731 PSEEN2868 PSEEN5326
            PAR: Psyc_0081
            PCR: Pcryo_0087
            ACI: ACIAD1454 ACIAD2738
            SHE: Shewmr4_0407
            SHM: Shewmr7_3618
            SHN: Shewana3_3581
            CPS: CPS_0991
            PHA: PSHAa1308
            PAT: Patl_1357 Patl_1753 Patl_1814
            CBU: CBU_1023
            MCA: MCA2788
            NOC: Noc_2046 Noc_2551
            HCH: HCH_00322 HCH_04350
            CSA: Csal_1508
            ABO: ABO_0980(qor)
            CVI: CV_0213(qor) CV_2043
            RSO: RSc1203(RS02677) RSc2184(qor)
            REU: Reut_A1476 Reut_A1596 Reut_A1603 Reut_A1917 Reut_A2099
                 Reut_A2148 Reut_A2503 Reut_B3840 Reut_B4732 Reut_C6116
            REH: H16_A0618 H16_A0632 H16_A1262 H16_A2079 H16_A2377 H16_B0304
                 H16_B0332 H16_B0463 H16_B1003 H16_B1031 H16_B1340 H16_B2004
                 H16_B2520
            RME: Rmet_1716 Rmet_2119 Rmet_4852 Rmet_5285
            BMA: BMA1833 BMA1879(qor-1) BMAA1920 BMAA2042(qor-2)
            BMV: BMASAVP1_1065(qor-2) BMASAVP1_A1080(qor-1)
            BML: BMA10299_1350(qor-2) BMA10299_A0787(qor-1)
            BMN: BMA10247_0363(qor-1) BMA10247_A2332(qor-2)
            BXE: Bxe_A2354 Bxe_A3255 Bxe_B0289
            BUR: Bcep18194_A3580 Bcep18194_A3873 Bcep18194_A4474
                 Bcep18194_A4840 Bcep18194_A5075 Bcep18194_A5580
                 Bcep18194_A5617 Bcep18194_B0250 Bcep18194_B0501
                 Bcep18194_B1156 Bcep18194_B1199 Bcep18194_B1489
                 Bcep18194_B1771 Bcep18194_B1971 Bcep18194_B2465
                 Bcep18194_B2595 Bcep18194_B2916 Bcep18194_B3044
            BCN: Bcen_1678
            BCH: Bcen2424_1238 Bcen2424_2290 Bcen2424_4645 Bcen2424_4667
            BAM: Bamb_1234 Bamb_1585 Bamb_2290 Bamb_2328
            BPS: BPSL1169(qor) BPSL1208 BPSS0164 BPSS2293
            BPM: BURPS1710b_1391(qor) BURPS1710b_1431(qor) BURPS1710b_A0259
                 BURPS1710b_A1439(qor-2) BURPS1710b_A1683
            BTE: BTH_I1019 BTH_I1057 BTH_I1516 BTH_II0233
            BPE: BP2283(qor) BP3708
            BPA: BPP2445(qor)
            BBR: BB1893(qor) BB4304
            RFR: Rfer_1429 Rfer_2783
            POL: Bpro_3062 Bpro_3853
            MPT: Mpe_A0899 Mpe_A1251 Mpe_A3049
            HAR: HEAR0340 HEAR0568(qor)
            MMS: mma_0387(qor1) mma_0551(qor2)
            NMU: Nmul_A1959
            EBA: ebA4396(qor)
            AZO: azo3042 azo3209(qor)
            DAR: Daro_0548 Daro_3833
            GME: Gmet_0231
            DVU: DVU2754(qor)
            ADE: Adeh_3010
            MXA: MXAN_0845 MXAN_6107
            OTS: OTBS_0501(qor)
            WOL: WD0948
            WBM: Wbm0629
            AMA: AM928(qor)
            APH: APH_0257(qor)
            ERU: Erum6260(qor)
            ERW: ERWE_CDS_06570(qor)
            ERG: ERGA_CDS_06480(qor)
            ECN: Ecaj_0630
            ECH: ECH_0385(qor)
            NSE: NSE_0380(qor)
            PUB: SAR11_0143(qor)
            MLO: mll0505 mll2594
            MES: Meso_1694
            SME: SMa2383 SMb20388 SMb21290 SMc00246(qor)
            ATU: Atu5182(qor)
            ATC: AGR_pAT_254
            RET: RHE_CH01124 RHE_CH01141 RHE_CH02080(qor) RHE_PF00011
                 RHE_PF00156
            RLE: RL0861 RL1257(qor) RL1276 RL1462 RL2371(qor) RL2518 RL3511
                 pRL110134 pRL120366
            BME: BMEI0302 BMEII0696 BMEII0697 BMEII0876
            BMF: BAB1_1750 BAB2_0669(qor) BAB2_0831
            BMS: BRA0571(qor)
            BMB: BruAb2_0810
            BJA: bll3142 bll4583(qor) bll5605 bll6137(qor) blr0528 blr3079
                 blr5742 blr7675
            BRA: BRADO0250 BRADO1103 BRADO2914 BRADO3783(qor) BRADO4637
                 BRADO4966 BRADO5342(qor)
            BBT: BBta_0243 BBta_1153 BBta_3096 BBta_4146(qor) BBta_5040
                 BBta_5263 BBta_5834(qor) BBta_6946
            RPA: RPA0400 RPA1940 RPA2184 RPA2201 RPA2674 RPA2989
            RPB: RPB_0095 RPB_2841
            RPC: RPC_2619
            RPD: RPD_0707 RPD_2632
            RPE: RPE_0040 RPE_0668 RPE_2304 RPE_2800 RPE_3558
            NWI: Nwi_1504 Nwi_2750
            NHA: Nham_2044
            XAU: Xaut_2758
            CCR: CC_0096 CC_0770 CC_3759
            SIL: SPO0232 SPO0616 SPO1969 SPO2548 SPO2960
            SIT: TM1040_1910 TM1040_2230
            RSP: RSP_1891 RSP_3381
            JAN: Jann_0482
            RDE: RD1_1040 RD1_1041(qor) RD1_2290 RD1_3439 RD1_4096
            MMR: Mmar10_1647 Mmar10_2969
            HNE: HNE_2746
            GBE: GbCGDNIH1_0016 GbCGDNIH1_1057 GbCGDNIH1_1348
            RRU: Rru_A0088 Rru_A0384 Rru_A1056 Rru_A2962 Rru_A3063 Rru_A3371
                 Rru_A3620
            MAG: amb0752 amb4555
            ABA: Acid345_0192 Acid345_2350
            BHA: BH0363 BH0935
            BAN: BA2113(qor-1) BA3438 BA3544(qor-2)
            BAR: GBAA2113(qor-1) GBAA3438 GBAA3544(qor-2)
            BAA: BA_2608 BA_3936 BA_4036
            BAT: BAS1965 BAS3186 BAS3286
            BCE: BC2107 BC3380 BC3477
            BCA: BCE_2194(qor) BCE_3496(qor)
            BCZ: BCZK0911(qor) BCZK1920(qor) BCZK3087(qor) BCZK3175
                 BCZK3200(qor)
            BTK: BT9727_1944(qor) BT9727_3168(qor) BT9727_3256(qor)
            BPU: BPUM_0783
            OIH: OB2947
            GKA: GK1034
            SAB: SAB2068c
            LWE: lwe2524
            SSA: SSA_1279
            LSA: LSA1006 LSA1875
            LSL: LSL_0970(qor)
            LCA: LSEI_0148
            MTU: Rv1454c(qor) Rv3141(fadB4)
            MTC: MT0157 MT1501 MT1963 MT3228 MT3886
            MBO: Mb0154 Mb1489c(qor) Mb3165(fadB4)
            MBB: BCG_1515c(qor) BCG_3164(fadB4)
            MPA: MAP0263c MAP1180c(qor) MAP3190(fadB4)
            MAV: MAV_3325
            MSM: MSMEG_2033 MSMEG_3106 MSMEG_4146 MSMEG_4828
            MMC: Mmcs_0092 Mmcs_1554 Mmcs_2351 Mmcs_2427 Mmcs_3737
            CGL: NCgl1510(cgl1572)
            CGB: cg0251 cg1771(qor) cg3332
            CEF: CE1692
            NFA: nfa35710(qor) nfa41240 nfa50840
            RHA: RHA1_ro00434 RHA1_ro00633 RHA1_ro00783 RHA1_ro01058
                 RHA1_ro01498 RHA1_ro01510 RHA1_ro01618 RHA1_ro01951
                 RHA1_ro02339 RHA1_ro03100 RHA1_ro03786 RHA1_ro03949
                 RHA1_ro04118 RHA1_ro05955 RHA1_ro07188 RHA1_ro08046
                 RHA1_ro08437 RHA1_ro08445 RHA1_ro10219
            SCO: SCO1199(SCG11A.30c) SCO4266(SCD86A.03c) SCO5073(SCBAC20F6.16)
            SMA: SAV3956 SAV4018 SAV7139
            CMI: CMM_0652(qorA) CMM_1929
            TFU: Tfu_0360 Tfu_2228
            FRA: Francci3_4153
            FAL: FRAAL0182 FRAAL1956 FRAAL4847 FRAAL5913 FRAAL6309 FRAAL6600
            SEN: SACE_0203 SACE_0927(adh10) SACE_2164(qor) SACE_2564 SACE_3735
                 SACE_4163(adh1) SACE_4474(qor) SACE_4681 SACE_4992 SACE_5209
                 SACE_5389 SACE_6641
            RXY: Rxyl_2398
            RBA: RB11985 RB4399
            SYC: syc1296_d
            SYF: Synpcc7942_0216
            CYA: CYA_1334
            CYB: CYB_2656
            TEL: tlr0001
            ANA: alr2948
            AVA: Ava_0954 Ava_C0108
            TER: Tery_1832
            CHU: CHU_1033(qor)
            DRA: DR_1061 DR_A0251
            DGE: Dgeo_0529 Dgeo_0753 Dgeo_2406
            TTH: TTC0305 TTC1833
            TTJ: TTHA0153 TTHA0664
            HMA: pNG7022(adh1) pNG7032(adh10) pNG7289(adh6) pNG7351(adh13)
                 rrnAC0012(adh11) rrnAC0191(adh3) rrnAC1526(yfmJ2)
                 rrnAC3026(yfmJ1) rrnAC3506(adh2)
            HWA: HQ1939A(qor) HQ1987A(qor) HQ3024A(qor)
            NPH: NP3766A(qor_2) NP4816A(qor_1)
STRUCTURES  PDB: 1IYZ  1IZ0  1YB5  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.5.5
            ExPASy - ENZYME nomenclature database: 1.6.5.5
            ExplorEnz - The Enzyme Database: 1.6.5.5
            ERGO genome analysis and discovery system: 1.6.5.5
            BRENDA, the Enzyme Database: 1.6.5.5
            CAS: 9032-20-6
///
ENTRY       EC 1.6.5.6                  Enzyme
NAME        p-benzoquinone reductase (NADPH)
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a quinone or similar compound as acceptor
SYSNAME     NADPH:p-benzoquinone oxidoreductase
REACTION    NADPH + H+ + p-benzoquinone = NADP+ + hydroquinone [RN:R05244]
ALL_REAC    R05244
SUBSTRATE   NADPH [CPD:C00005];
            H+ [CPD:C00080];
            p-benzoquinone [CPD:C00472]
PRODUCT     NADP+ [CPD:C00006];
            hydroquinone [CPD:C00530]
COMMENT     Involved in the 4-nitrophenol degradation pathway in bacteria.
REFERENCE   1  [PMID:16348446]
  AUTHORS   Spain JC, Gibson DT.
  TITLE     Pathway for Biodegradation of p-Nitrophenol in a Moraxella sp.
  JOURNAL   Appl. Environ. Microbiol. 57 (1991) 812-819.
  ORGANISM  Moraxella sp.
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.5.6
            ExPASy - ENZYME nomenclature database: 1.6.5.6
            ExplorEnz - The Enzyme Database: 1.6.5.6
            ERGO genome analysis and discovery system: 1.6.5.6
            UM-BBD (Biocatalysis/Biodegradation Database): 1.6.5.6
            BRENDA, the Enzyme Database: 1.6.5.6
///
ENTRY       EC 1.6.5.7                  Enzyme
NAME        2-hydroxy-1,4-benzoquinone reductase;
            hydroxybenzoquinone reductase;
            1,2,4-trihydroxybenzene:NAD oxidoreductase;
            NADH:2-hydroxy-1,4-benzoquinone oxidoreductase
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a quinone or similar compound as acceptor
SYSNAME     2-hydroxy-1,4-benzoquinone:NADH oxidoreductase
REACTION    2-hydroxy-1,4-benzoquinone + NADH + H+ = 1,2,4-trihydroxybenzene +
            NAD+ [RN:R05399]
ALL_REAC    R05399
SUBSTRATE   2-hydroxy-1,4-benzoquinone [CPD:C07103];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
PRODUCT     1,2,4-trihydroxybenzene [CPD:C02814];
            NAD+ [CPD:C00003]
COMMENT     A flavoprotein (FMN) that differs in substrate specificity from
            other quinone reductases. The enzyme in Burkholderia cepacia is
            inducible by 2,4,5-trichlorophenoxyacetate.
REFERENCE   1  [PMID:9721310]
  AUTHORS   Zaborina O, Daubaras DL, Zago A, Xun L, Saido K, Klem T, Nikolic D,
            Chakrabarty AM.
  TITLE     Novel pathway for conversion of chlorohydroxyquinol to maleylacetate
            in Burkholderia cepacia AC1100.
  JOURNAL   J. Bacteriol. 180 (1998) 4667-75.
  ORGANISM  Burkholderia cepacia [GN:bam]
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
            PATH: map00627  1,4-Dichlorobenzene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.5.7
            ExPASy - ENZYME nomenclature database: 1.6.5.7
            ExplorEnz - The Enzyme Database: 1.6.5.7
            ERGO genome analysis and discovery system: 1.6.5.7
            UM-BBD (Biocatalysis/Biodegradation Database): 1.6.5.7
            BRENDA, the Enzyme Database: 1.6.5.7
///
ENTRY       EC 1.6.5.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a quinone or similar compound as acceptor
REACTION    (1) Menaquinone + 2 H+ <=> Menaquinol [RN:R02964];
            (2) Phylloquinone + 2 H+ <=> Phylloquinol [RN:R03816]
SUBSTRATE   Menaquinone [CPD:C00828];
            H+ [CPD:C00080];
            Phylloquinone [CPD:C02059]
PRODUCT     Menaquinol [CPD:C05819];
            Phylloquinol [CPD:C06245]
///
ENTRY       EC 1.6.6.1        Obsolete  Enzyme
NAME        Transferred to 1.7.1.1
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a nitrogenous group as acceptor
COMMENT     Transferred entry: now EC 1.7.1.1, nitrate reductase (NADH) (EC
            1.6.6.1 created 1961, deleted 2002)
STRUCTURES  PDB: 1CNE  1CNF  2CND  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.6.1
            ExPASy - ENZYME nomenclature database: 1.6.6.1
            ExplorEnz - The Enzyme Database: 1.6.6.1
            ERGO genome analysis and discovery system: 1.6.6.1
            BRENDA, the Enzyme Database: 1.6.6.1
///
ENTRY       EC 1.6.6.2        Obsolete  Enzyme
NAME        Transferred to 1.7.1.2
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a nitrogenous group as acceptor
COMMENT     Transferred entry: now EC 1.7.1.2, nitrate reductase [NAD(P)H] (EC
            1.6.6.2 created 1961, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.6.2
            ExPASy - ENZYME nomenclature database: 1.6.6.2
            ExplorEnz - The Enzyme Database: 1.6.6.2
            ERGO genome analysis and discovery system: 1.6.6.2
            BRENDA, the Enzyme Database: 1.6.6.2
///
ENTRY       EC 1.6.6.3        Obsolete  Enzyme
NAME        Transferred to 1.7.1.3
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a nitrogenous group as acceptor
COMMENT     Transferred entry: now EC 1.7.1.3, nitrate reductase (NADPH) (EC
            1.6.6.3 created 1961, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.6.3
            ExPASy - ENZYME nomenclature database: 1.6.6.3
            ExplorEnz - The Enzyme Database: 1.6.6.3
            ERGO genome analysis and discovery system: 1.6.6.3
            BRENDA, the Enzyme Database: 1.6.6.3
///
ENTRY       EC 1.6.6.4        Obsolete  Enzyme
NAME        Transferred to 1.7.1.4
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a nitrogenous group as acceptor
COMMENT     Transferred entry: now EC 1.7.1.4, nitrite reductase [NAD(P)H] (EC
            1.6.6.4 created 1961, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.6.4
            ExPASy - ENZYME nomenclature database: 1.6.6.4
            ExplorEnz - The Enzyme Database: 1.6.6.4
            ERGO genome analysis and discovery system: 1.6.6.4
            BRENDA, the Enzyme Database: 1.6.6.4
///
ENTRY       EC 1.6.6.5        Obsolete  Enzyme
NAME        Transferred to 1.7.2.1
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a nitrogenous group as acceptor
COMMENT     Transferred entry: now EC 1.7.2.1, nitrite reductase (NO-forming)
            (EC 1.6.6.5 created 1961, deleted 1964)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.6.5
            ExPASy - ENZYME nomenclature database: 1.6.6.5
            ExplorEnz - The Enzyme Database: 1.6.6.5
            ERGO genome analysis and discovery system: 1.6.6.5
            BRENDA, the Enzyme Database: 1.6.6.5
///
ENTRY       EC 1.6.6.6        Obsolete  Enzyme
NAME        Transferred to 1.7.1.5
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a nitrogenous group as acceptor
COMMENT     Transferred entry: now EC 1.7.1.5 hyponitrite reductase (EC 1.6.6.6
            created 1961, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.6.6
            ExPASy - ENZYME nomenclature database: 1.6.6.6
            ExplorEnz - The Enzyme Database: 1.6.6.6
            ERGO genome analysis and discovery system: 1.6.6.6
            BRENDA, the Enzyme Database: 1.6.6.6
///
ENTRY       EC 1.6.6.7        Obsolete  Enzyme
NAME        Transferred to 1.7.1.6
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a nitrogenous group as acceptor
COMMENT     Transferred entry: now EC 1.7.1.6 azobenzene reductase (EC 1.6.6.7
            created 1961, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.6.7
            ExPASy - ENZYME nomenclature database: 1.6.6.7
            ExplorEnz - The Enzyme Database: 1.6.6.7
            ERGO genome analysis and discovery system: 1.6.6.7
            BRENDA, the Enzyme Database: 1.6.6.7
///
ENTRY       EC 1.6.6.8        Obsolete  Enzyme
NAME        Transferred to 1.7.1.7
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a nitrogenous group as acceptor
COMMENT     Transferred entry: now EC 1.7.1.7 GMP reductase (EC 1.6.6.8 created
            1965, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.6.8
            ExPASy - ENZYME nomenclature database: 1.6.6.8
            ExplorEnz - The Enzyme Database: 1.6.6.8
            ERGO genome analysis and discovery system: 1.6.6.8
            BRENDA, the Enzyme Database: 1.6.6.8
///
ENTRY       EC 1.6.6.9                  Enzyme
NAME        trimethylamine-N-oxide reductase;
            trimethylamine N-oxide reductase;
            trimethylamine oxide reductase;
            TMAO reductase;
            TOR
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a nitrogenous group as acceptor
SYSNAME     NADH:trimethylamine-N-oxide oxidoreductase
REACTION    NADH + H+ + trimethylamine N-oxide = NAD+ + trimethylamine + H2O
            [RN:R02559]
ALL_REAC    R02559;
            (other) R02560
SUBSTRATE   NADH [CPD:C00004];
            H+ [CPD:C00080];
            trimethylamine N-oxide [CPD:C01104]
PRODUCT     NAD+ [CPD:C00003];
            trimethylamine [CPD:C00565];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:4286289]
  AUTHORS   Unemoto T, Hayashi M, Miyaki K, Hayashi M.
  TITLE     Intracellular localization and properties of trimethylamine-N-oxide
            reductase in Vibrio parahaemolyticus.
  JOURNAL   Biochim. Biophys. Acta. 110 (1965) 319-28.
  ORGANISM  Vibrio parahaemolyticus [GN:vpa]
PATHWAY     PATH: map00680  Methane metabolism
ORTHOLOGY   KO: K00352  trimethylamine-N-oxide reductase
GENES       VCO: VC0395_A1296(torA)
STRUCTURES  PDB: 1TMO  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.6.9
            ExPASy - ENZYME nomenclature database: 1.6.6.9
            ExplorEnz - The Enzyme Database: 1.6.6.9
            ERGO genome analysis and discovery system: 1.6.6.9
            BRENDA, the Enzyme Database: 1.6.6.9
            CAS: 37256-34-1
///
ENTRY       EC 1.6.6.10       Obsolete  Enzyme
NAME        Transferred to 1.7.1.9
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a nitrogenous group as acceptor
COMMENT     Transferred entry: now EC 1.7.1.9 nitroquinoline-N-oxide reductase
            (EC 1.6.6.10 created 1972, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.6.10
            ExPASy - ENZYME nomenclature database: 1.6.6.10
            ExplorEnz - The Enzyme Database: 1.6.6.10
            ERGO genome analysis and discovery system: 1.6.6.10
            BRENDA, the Enzyme Database: 1.6.6.10
///
ENTRY       EC 1.6.6.11       Obsolete  Enzyme
NAME        Transferred to 1.7.1.10
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a nitrogenous group as acceptor
COMMENT     Transferred entry: now EC 1.7.1.10, hydroxylamine reductase (NADH)
            (EC 1.6.6.11 created 1972, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.6.11
            ExPASy - ENZYME nomenclature database: 1.6.6.11
            ExplorEnz - The Enzyme Database: 1.6.6.11
            ERGO genome analysis and discovery system: 1.6.6.11
            BRENDA, the Enzyme Database: 1.6.6.11
///
ENTRY       EC 1.6.6.12       Obsolete  Enzyme
NAME        Transferred to 1.7.1.11
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a nitrogenous group as acceptor
COMMENT     Transferred entry: now EC 1.7.1.11,
            4-(dimethylamino)phenylazoxybenzene reductase (EC 1.6.6.12 created
            1989, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.6.12
            ExPASy - ENZYME nomenclature database: 1.6.6.12
            ExplorEnz - The Enzyme Database: 1.6.6.12
            ERGO genome analysis and discovery system: 1.6.6.12
            BRENDA, the Enzyme Database: 1.6.6.12
///
ENTRY       EC 1.6.6.13       Obsolete  Enzyme
NAME        Transferred to 1.7.1.12
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a nitrogenous group as acceptor
COMMENT     Transferred entry: now EC 1.7.1.12 N-hydroxy-2-acetamidofluorene
            reductase (EC 1.6.6.13 created 1989, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.6.13
            ExPASy - ENZYME nomenclature database: 1.6.6.13
            ExplorEnz - The Enzyme Database: 1.6.6.13
            ERGO genome analysis and discovery system: 1.6.6.13
            BRENDA, the Enzyme Database: 1.6.6.13
///
ENTRY       EC 1.6.6.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a nitrogenous group as acceptor
REACTION    (1) Nitrosobenzene + NADPH + H+ <=> N-Hydroxyarylamine + NADP+
            [RN:R05400];
            (2) Nitrobenzene + NADPH + H+ <=> Nitrosobenzene + NADP+ + H2O
            [RN:R05401]
SUBSTRATE   4-Aminobenzenesulfonate [CPD:C06335];
            4-Aminobenzoate [CPD:C00568];
            Nitrosobenzene [CPD:C06876];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            Nitrobenzene [CPD:C06813]
PRODUCT     4-Carboxy-4'-sulfoazobenzene [CPD:C06673];
            H+ [CPD:C00080];
            N-Hydroxyarylamine [CPD:C02720];
            NADP+ [CPD:C00006];
            Nitrosobenzene [CPD:C06876];
            H2O [CPD:C00001]
///
ENTRY       EC 1.6.7.1        Obsolete  Enzyme
NAME        Transferred to 1.18.1.2
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With an iron-sulfur protein as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.18.1.2 ferredoxin-NADP+ reductase (EC
            1.6.7.1 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.7.1
            ExPASy - ENZYME nomenclature database: 1.6.7.1
            ExplorEnz - The Enzyme Database: 1.6.7.1
            ERGO genome analysis and discovery system: 1.6.7.1
            BRENDA, the Enzyme Database: 1.6.7.1
///
ENTRY       EC 1.6.7.2        Obsolete  Enzyme
NAME        Transferred to 1.18.1.1
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With an iron-sulfur protein as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.18.1.1 rubredoxin-NAD+ reductase (EC
            1.6.7.2 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.7.2
            ExPASy - ENZYME nomenclature database: 1.6.7.2
            ExplorEnz - The Enzyme Database: 1.6.7.2
            ERGO genome analysis and discovery system: 1.6.7.2
            BRENDA, the Enzyme Database: 1.6.7.2
///
ENTRY       EC 1.6.7.3        Obsolete  Enzyme
NAME        Transferred to 1.18.1.3
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With an iron-sulfur protein as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.18.1.3, ferredoxin-NAD+ reductase (EC
            1.6.7.3 created 1978, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.7.3
            ExPASy - ENZYME nomenclature database: 1.6.7.3
            ExplorEnz - The Enzyme Database: 1.6.7.3
            ERGO genome analysis and discovery system: 1.6.7.3
            BRENDA, the Enzyme Database: 1.6.7.3
///
ENTRY       EC 1.6.8.1        Obsolete  Enzyme
NAME        Transferred to 1.5.1.29
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a flavin as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.5.1.29 FMN reductase (EC 1.6.8.1 created
            1981, deleted 2002)
STRUCTURES  PDB: 1BKJ  1VFR  2BKJ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.8.1
            ExPASy - ENZYME nomenclature database: 1.6.8.1
            ExplorEnz - The Enzyme Database: 1.6.8.1
            ERGO genome analysis and discovery system: 1.6.8.1
            BRENDA, the Enzyme Database: 1.6.8.1
///
ENTRY       EC 1.6.8.2        Obsolete  Enzyme
NAME        Transferred to 1.5.1.30
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With a flavin as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.5.1.30 flavin reductase (EC 1.6.8.2
            created 1982, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.8.2
            ExPASy - ENZYME nomenclature database: 1.6.8.2
            ExplorEnz - The Enzyme Database: 1.6.8.2
            ERGO genome analysis and discovery system: 1.6.8.2
            BRENDA, the Enzyme Database: 1.6.8.2
///
ENTRY       EC 1.6.99.1                 Enzyme
NAME        NADPH dehydrogenase;
            NADPH2 diaphorase;
            NADPH diaphorase;
            OYE;
            diaphorase;
            dihydronicotinamide adenine dinucleotide phosphate dehydrogenase;
            NADPH-dehydrogenase;
            NADPH-diaphorase;
            NADPH2-dehydrogenase;
            old yellow enzyme;
            reduced nicotinamide adenine dinucleotide phosphate dehydrogenase;
            TPNH dehydrogenase;
            TPNH-diaphorase;
            triphosphopyridine diaphorase;
            triphosphopyridine nucleotide diaphorase;
            NADPH2 dehydrogenase;
            NADPH:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With other acceptors
SYSNAME     NADPH:acceptor oxidoreductase
REACTION    NADPH + H+ + acceptor = NADP+ + reduced acceptor [RN:R00282]
ALL_REAC    R00282
SUBSTRATE   NADPH [CPD:C00005];
            H+ [CPD:C00080];
            acceptor [CPD:C00028]
PRODUCT     NADP+ [CPD:C00006];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016];
            FMN [CPD:C00061]
COMMENT     A flavoprotein (FMN in yeast, FAD in plants).
REFERENCE   1
  AUTHORS   Akesson, A., Ehrenberg, A. and Theorell, H.
  TITLE     Old yellow enzyme.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 477-494.
REFERENCE   2  [PMID:13471057]
  AUTHORS   AVRON M, JAGENDORF AT.
  TITLE     Some further investigations on chloroplast TPNH diaphorase.
  JOURNAL   Arch. Biochem. Biophys. 72 (1957) 17-24.
  ORGANISM  spinach
REFERENCE   3
  AUTHORS   Jagendorf, A.T.
  TITLE     Chloroplast TPNH diaphorase.
  JOURNAL   Methods Enzymol. 6 (1963) 430-434.
  ORGANISM  spinach
REFERENCE   4
  AUTHORS   Theorell, H.
  TITLE     Das gelbe Oxydationsferment.
  JOURNAL   Biochem. Z. 278 (1935) 263-290.
REFERENCE   5
  AUTHORS   Theorell, H. and Akesson, A.
  TITLE     Molecular weight and FMN content of crystalline "old yellow enzyme".
  JOURNAL   Arch. Biochem. Biophys. 65 (1956) 439-448.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K00354  NADPH2 dehydrogenase
GENES       SCE: YHR179W(OYE2) YPL171C(OYE3)
            AGO: AGOS_AGR329C
            PIC: PICST_31957(OYE2.9) PICST_31958(OYE2.4) PICST_43720(OYE2.2)
                 PICST_52325(OYE3.3) PICST_57042(OPR1) PICST_89722(OYE2.1)
            CAL: CaO19.125 CaO19_3443(CaO19.3443)
            CGR: CAGL0I02024g CAGL0I02574g CAGL0L09537g
            SPO: SPAC5H10.04 SPAC5H10.10
            AFM: AFUA_2G17960
            CNE: CNI02360
            TET: TTHERM_00024260 TTHERM_00038960 TTHERM_00038970
                 TTHERM_00094280 TTHERM_00160800 TTHERM_00160810
                 TTHERM_00160820 TTHERM_00694470 TTHERM_00784330
            PHA: PSHAa0880 PSHAa1863
            BUR: Bcep18194_A4953 Bcep18194_B0239 Bcep18194_B0492
                 Bcep18194_B0503 Bcep18194_B0951 Bcep18194_B1242
                 Bcep18194_B1736
            HAR: HEAR1430(nemA) HEAR2541
            CFF: CFF8240_0619
            CCV: CCV52592_1828
            BRA: BRADO0620(namA) BRADO2322
            BBT: BBta_2683 BBta_7562(namA)
            RRU: Rru_A0475
            AVA: Ava_4760
            NPH: NP5226A
STRUCTURES  PDB: 1BWK  1BWL  1HDO  1HE2  1HE3  1HE4  1HE5  1K02  1K03  1OYA  
                 1OYB  1OYC  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.99.1
            ExPASy - ENZYME nomenclature database: 1.6.99.1
            ExplorEnz - The Enzyme Database: 1.6.99.1
            ERGO genome analysis and discovery system: 1.6.99.1
            UM-BBD (Biocatalysis/Biodegradation Database): 1.6.99.1
            BRENDA, the Enzyme Database: 1.6.99.1
            CAS: 9001-68-7
///
ENTRY       EC 1.6.99.2       Obsolete  Enzyme
NAME        Transferred to 1.6.5.2
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With other acceptors
COMMENT     Transferred entry: now EC 1.6.5.2 NAD(P)H dehydrogenase (quinone).
            The enzyme was erroneously transferred from this sub-subclass in
            1965 (EC 1.6.99.2 created 1961 as EC 1.6.5.2, transferred 1965 to EC
            1.6.99.2, deleted 2005)
GENES       ECI: UTI89_C3455(mdaB)
            BXE: Bxe_A1917
            BCZ: BCZK0742
            BTK: BT9727_0747
STRUCTURES  PDB: 1D4A  1DXO  1DXQ  1GG5  1H66  1H69  1KBO  1KBQ  1QBG  1QR2  
                 1QRD  1SG0  2QR2  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.99.2
            ExPASy - ENZYME nomenclature database: 1.6.99.2
            ExplorEnz - The Enzyme Database: 1.6.99.2
            ERGO genome analysis and discovery system: 1.6.99.2
            BRENDA, the Enzyme Database: 1.6.99.2
///
ENTRY       EC 1.6.99.3                 Enzyme
NAME        NADH dehydrogenase;
            cytochrome c reductase;
            type 1 dehydrogenase;
            beta-NADH dehydrogenase dinucleotide;
            diaphorase;
            dihydrocodehydrogenase I dehydrogenase;
            dihydronicotinamide adenine dinucleotide dehydrogenase;
            diphosphopyridine diaphorase;
            DPNH diaphorase;
            NADH diaphorase;
            NADH hydrogenase;
            NADH oxidoreductase;
            NADH-menadione oxidoreductase;
            reduced diphosphopyridine nucleotide diaphorase;
            NADH:cytochrome c oxidoreductase;
            NADH2 dehydrogenase;
            NADH:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With other acceptors
SYSNAME     NADH:acceptor oxidoreductase
REACTION    NADH + H+ + acceptor = NAD+ + reduced acceptor [RN:R00281]
ALL_REAC    R00281
SUBSTRATE   NADH [CPD:C00004];
            H+ [CPD:C00080];
            acceptor [CPD:C00028]
PRODUCT     NAD+ [CPD:C00003];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023];
            Sulfur [CPD:C00087];
            Iron-sulfur [CPD:C00824];
            Flavoprotein [CPD:C06411]
COMMENT     A flavoprotein containing iron-sulfur centres. After preparations
            have been subjected to certain treatments, cytochrome c may act as
            an acceptor. Under normal conditions, two protons are extruded from
            the cytoplasm or the intramitochondrial or stromal compartment.
            Present in a mitochondrial complex as EC 1.6.5.3, NADH dehydrogenase
            (ubiquinone).
REFERENCE   1  [PMID:4402556]
  AUTHORS   Adachi K, Okuyama T.
  TITLE     Study on the reduced pyridine nucleotide dehydrogenase of bovine
            erythrocytes. I. Crystallization and properties of the reduced
            pyridine nucleotide dehydrogenase of bovine erythrocytes.
  JOURNAL   Biochim. Biophys. Acta. 268 (1972) 629-37.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   Hatefi, Y., Ragan, C.I. and Galante, Y.M.
  TITLE     The enzymes and the enzyme complexes of the mitochondrial oxidative
            phosphorylation system.
  JOURNAL   In: Martonosi, A. (Ed.), The Enzymes of Biological Membranes, 2nd
            ed., vol. 4, Plenum Press, New York, 1985, p. 1-70.
REFERENCE   3  [PMID:4144655]
  AUTHORS   Hochstein LI, Dalton BP.
  TITLE     Studies of a halophilic NADH dehydrogenase. I. Purification and
            properties of the enzyme.
  JOURNAL   Biochim. Biophys. Acta. 302 (1973) 216-28.
  ORGANISM  halophilic bacterium
REFERENCE   4  [PMID:14074130]
  AUTHORS   KANIUGA Z.
  TITLE     THE TRANSFORMATION OF MITOCHONDRIAL NADH DEHYDROGENASE INTO NADH:
            CYTOCHROME C OXIDOREDUCTASE.
  JOURNAL   Biochim. Biophys. Acta. 73 (1963) 550-64.
PATHWAY     PATH: map00190  Oxidative phosphorylation
ORTHOLOGY   KO: K00356  NADH dehydrogenase
            KO: K03885  NADH dehydrogenase
            KO: K03934  NADH dehydrogenase (ubiquinone) Fe-S protein 1
            KO: K03935  NADH dehydrogenase (ubiquinone) Fe-S protein 2
            KO: K03936  NADH dehydrogenase (ubiquinone) Fe-S protein 3
            KO: K03937  NADH dehydrogenase (ubiquinone) Fe-S protein 4
            KO: K03938  NADH dehydrogenase (ubiquinone) Fe-S protein 5
            KO: K03939  NADH dehydrogenase (ubiquinone) Fe-S protein 6
            KO: K03940  NADH dehydrogenase (ubiquinone) Fe-S protein 7
            KO: K03941  NADH dehydrogenase (ubiquinone) Fe-S protein 8
            KO: K03942  NADH dehydrogenase (ubiquinone) flavoprotein 1
            KO: K03943  NADH dehydrogenase (ubiquinone) flavoprotein 2
            KO: K03944  NADH dehydrogenase (ubiquinone) flavoprotein 3
            KO: K03945  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 1
            KO: K03946  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 2
            KO: K03947  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 3
            KO: K03948  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 4
            KO: K03949  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 5
            KO: K03950  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 6
            KO: K03951  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 7
            KO: K03952  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 8
            KO: K03953  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 9
            KO: K03954  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 10
            KO: K03955  NADH dehydrogenase (ubiquinone) 1 alpha/beta subcomplex
                        1
            KO: K03957  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 1
            KO: K03958  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 2
            KO: K03959  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 3
            KO: K03960  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 4
            KO: K03961  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 5
            KO: K03962  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 6
            KO: K03963  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 7
            KO: K03964  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 8
            KO: K03965  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 9
            KO: K03966  NADH dehydrogenase (ubiquinone) 1 beta subcomplex 10
            KO: K03967  NADH dehydrogenase (ubiquinone) 1 subcomplex unknown 1
            KO: K03968  NADH dehydrogenase (ubiquinone) 1 subcomplex unknown 2
GENES       HSA: 126328(NDUFA11) 374291(NDUFS7) 4694(NDUFA1) 4695(NDUFA2)
                 4696(NDUFA3) 4697(NDUFA4) 4698(NDUFA5) 4700(NDUFA6)
                 4701(NDUFA7) 4702(NDUFA8) 4704(NDUFA9) 4705(NDUFA10)
                 4706(NDUFAB1) 4707(NDUFB1) 4708(NDUFB2) 4709(NDUFB3)
                 4710(NDUFB4) 4711(NDUFB5) 4712(NDUFB6) 4713(NDUFB7)
                 4714(NDUFB8) 4715(NDUFB9) 4716(NDUFB10) 4717(NDUFC1)
                 4718(NDUFC2) 4719(NDUFS1) 4720(NDUFS2) 4722(NDUFS3)
                 4723(NDUFV1) 4724(NDUFS4) 4725(NDUFS5) 4726(NDUFS6)
                 4728(NDUFS8) 4729(NDUFV2) 4731(NDUFV3) 51079(NDUFA13)
                 54539(NDUFB11) 55967(NDUFA12) 56901(NDUFA4L2)
            PTR: 451175(NDUFS3) 451375(NDUFS8) 451766(NDUFA9) 453115(NDUFB1)
                 455295(NDUFV2) 459896(NDUFS1) 460612(NDUFB4) 461878(NDUFS4)
                 462119(NDUFA2) 463686(NDUFA5) 463780(NDUFB2) 464380(NDUFB9)
                 464897(NDUFA8) 468748(NDUFB7) 470696(NDUFA10) 471008(NDUFB5)
                 473588(NDUFB11)
            MCC: 641333(NDUFA4) 693506(NDUFS5) 698706(LOC698706)
                 699693(LOC699693) 700718(NDUFAB1)
            MMU: 104130(Ndufb11) 17991(Ndufa2) 17992(Ndufa4) 17993(Ndufs4)
                 17995(Ndufv1) 225887(Ndufs8) 226646(Ndufs2) 227197(Ndufs1)
                 230075(Ndufb6) 407785(Ndufs6) 54405(Ndufa1) 66046(Ndufb5)
                 66091(Ndufa3) 66108(Ndufa9) 66218(Ndufb9) 66377(Ndufc1)
                 66414(Ndufa12) 66416(Ndufa7) 66495(Ndufb3) 66916(Ndufb7)
                 67130(Ndufa6) 67184(Ndufa13) 67264(Ndufb8) 67273(Ndufa10)
                 68194(Ndufb4) 68197(Ndufc2) 68198(Ndufb2) 68202(Ndufa5)
                 68342(Ndufb10) 68349(Ndufs3) 68375(Ndufa8) 69875(Ndufa11)
                 70316(Ndufab1) 72900(Ndufv2) 75406(Ndufs7)
            RNO: 25488(Ndufa5) 288088(Ndufb4) 289218(Ndufs2)
                 291660(Ndufa2_predicted) 293130(Ndufc2)
                 293453(Ndufab1_predicted) 293652(Ndufs8_predicted)
                 293655(Ndufv1) 293991(Ndufb8_predicted) 29478(Ndufs6)
                 294964(Ndufb5_predicted) 295923(Ndufs3_predicted)
                 296658(Ndufa8) 297990(Ndufb6_predicted)
                 299643(Ndufa7_predicted) 299954(Ndufb9_predicted)
                 301427(Ndufb3_predicted) 301458(Ndufs1) 314071(Ndufa10)
                 315167(Ndufa6_predicted) 316632(LOC316632)
                 361385(Ndufb7_predicted) 362344(Ndufb2_predicted)
                 362588(Ndufs5b) 362837(Ndufs7) 363441(Ndufa1_predicted)
                 366074(RGD1560451_predicted) 81728(Ndufv2)
            CFA: 474483(NDUFA6) 475094(NDUFB9) 475322(NDUFS5) 475428(NDUFA12)
                 475978(NDUFS3) 476004(NDUFV1) 476659(NDUFA13) 476686(NDUFB7)
                 476722(NDUFA7) 476754(NDUFS7) 476794(NDUFC2) 477682(NDUFA4)
                 477718(NDUFA9) 477798(NDUFB8) 478032(NDUFA2) 478421(LOC478421)
                 478577(NDUFB4) 478639(LOC478639) 478869(NDUFB3) 478880(NDUFS1)
                 478981(NDUFS2) 479887(NDUFB10) 480204(NDUFV2) 480741(NDUFA8)
                 480894(NDUFB11) 481033(LOC481033) 485505(LOC485505)
                 488724(LOC488724) 607407(NDUFA4L2) 607943(NDUFC1)
                 608244(NDUFA10) 610413(LOC610413) 611480(NDUFA3)
            BTA: 281742(DAP13) 282289(NDUFC1) 282517(NDUFB8) 287014(NDUFV1)
                 287027(NDUFS8) 288380(NDUFS1) 326346(b14.7) 327660(NDUFB9)
                 327665(NDUFB6) 327670(NDUFA6) 327673(NDUFA1) 327680(NDUFS4)
                 327690(NDUFB1) 327691(NDUFS6) 327697(NDUFS2) 327698(NDUFA2)
                 327701(NDUFB10) 327702(NDUFAB1) 327704(NDUFA4) 327706(NDUFB4)
                 327710(NDUFA8) 327713(NDUFB2) 327714(NDUFA5) 327717(NDUFV3)
                 338046(NDUFC2) 338057(NDUFS5) 338060(NDUFA10) 338061(NDUFB5)
                 338063(NDUFA7) 338064(NDUFA3) 338065(NDUFB7) 338073(NDUFB3)
                 338079(NDUFS7) 338084(GRIM19) 404161(ESSS) 404188(NDUFA9)
            GGA: 404751(NDUFC2) 416391(NDUFB6) 416543(NDUFB10) 416571(NDUFAB1)
                 417112(NDUFA8) 417753(NDUFA5) 417907(NDUFA12) 418118(NDUFB2)
                 418541(NDUFV3) 419039(NDUFA9) 420065(NDUFA7) 420337(NDUFB9)
                 420976(NDUFS6) 423179(NDUFS3) 423763(NDUFB8)
                 424032(RCJMB04_24e8) 424078(NDUFB3) 424102(NDUFS1)
                 424978(NDUFB5) 426488(NDUFV2) 427897(NDUFA6)
                 430210(RCJMB04_33n14) 768860(NDUFA2) 769492(NDUFS8)
                 769954(NDUFB4) 770724(LOC770724) 770879(LOC770879)
                 771510(NDUFS5) 772135(NDUFA4) 772150(NDUFA1)
            XLA: 379572(MGC69110) 379900(ndufb5) 379907(ndufv1) 379950(ndufb2)
                 380000(ndufs1) 398665(MGC64316) 447095(MGC85267)
                 447172(MGC85528) 495159(LOC495159)
            XTR: 448707(MGC89694) 496917(ndufa9) 496988(ndufv1)
                 549920(LOC549920)
            DRE: 321951(ndufa10) 338177(zgc:77225) 393497(zgc:66391)
                 393700(zgc:73139) 393703(ndufb10) 393720(zgc:73198)
                 393764(zgc:73329) 393781(zgc:73375) 393821(zgc:77820)
                 393829(ndufb8) 406298(ndufa4) 406306(ndufb4) 406413(ndufs8)
                 406726(ndufa4l) 445291(ndufv1) 493605(zgc:92209)
                 550451(ndufs3) 641476(zgc:123301)
            SPU: 577933(LOC577933) 578949(LOC578949) 581703(LOC581703)
                 581848(LOC581848) 582177(LOC582177) 582178(LOC582178)
                 585599(LOC585599) 586214(LOC586214) 587789(LOC587789)
                 587821(LOC587821) 591737(LOC591737) 591836(LOC591836)
                 752184(LOC752184) 756564(LOC756564) 758156(LOC758156)
            DME: Dmel_CG10320 Dmel_CG11455 Dmel_CG12079 Dmel_CG12203
                 Dmel_CG12400 Dmel_CG12859 Dmel_CG13240(l(2)35Di) Dmel_CG15434
                 Dmel_CG18624 Dmel_CG1970 Dmel_CG2014 Dmel_CG2286(ND75)
                 Dmel_CG3192 Dmel_CG3621 Dmel_CG3683 Dmel_CG3944(ND23)
                 Dmel_CG5548 Dmel_CG5703 Dmel_CG6020 Dmel_CG6343(ND42)
                 Dmel_CG6463 Dmel_CG6914 Dmel_CG7712 Dmel_CG8680 Dmel_CG8844
                 Dmel_CG9140 Dmel_CG9160(mtacp1) Dmel_CG9172 Dmel_CG9306
                 Dmel_CG9350 Dmel_CG9762(l(3)neo18)
            CEL: C09H10.3(nuo-1) C16A3.5 C18E9.4 C25A1.13 C33A12.1 D2030.4
                 F16B4.6 F22D6.4 F37C12.3 F44G4.2 F45H10.3 F53F4.10 F59C6.5
                 K09A9.5(gas-1) T20H4.5 T26A5.3(tag-99) W01A8.4 W10D5.2
                 Y53G8AL.2 Y54E10BL.5 Y54F10AM.5 Y56A3A.19 Y57G11C.12(nuo-3)
                 Y63D3A.7 Y71H2AM.4 Y94H6A.8 ZK809.3 ZK973.10(lpd-5)
            ATH: AT1G16700(ATMLO14) AT1G49140 AT1G65290 AT1G79010 AT2G02050
                 AT2G20360 AT2G29990(NDA2) AT2G33220 AT2G44620(mtACP-1)
                 AT2G47690 AT3G03070 AT3G06310 AT3G08610 AT3G12260 AT3G18410
                 AT3G62790 AT4G02580 AT4G05020(NDB2) AT4G21490 AT4G28220(NDB1)
                 AT5G08530 AT5G11770 AT5G37510(EMB1467) AT5G47890 AT5G52840
                 AT5G67590(FRO1) ArthMp006(nad5) ArthMp007(nad9)
                 ArthMp024(nad6) ArthMp026(nad2) ArthMp043(nad7)
                 ArthMp051(nad4) ArthMp058(nad4L) ArthMp086
            OSA: 4324703 4331143 4332639 4333901 4334276 4338442 4339127
                 4339271 4339427 4340478 4341876 4342058 4342743 4343746
                 4344058 4344095 4344724 4346289 4349513 nad7 nad9
            CME: CMA090C CMC091C CMC099C CMF056C CMI095C CMI118C CMI200C
                 CMI262C CMJ185C CMJ211C CMK135C CMM030C CMM034C CMM178C
                 CMM267C CMN320C CMO080C CMQ200C CMQ432C CMR188C CMR289C
                 CMS223C CMS372C CMT198C
            SCE: YDL085W(NDE2) YKL192C(ACP1) YML120C(NDI1) YMR145C(NDE1)
            AGO: AGOS_ADR262C AGOS_AER103W AGOS_AFR447C
            PIC: PICST_31688(NUO51) PICST_46630(NUFM) PICST_58506(NUO13)
                 PICST_58800(NDI1) PICST_62206(NUO21.2) PICST_65836(NUO10)
                 PICST_66598(NDE1) PICST_68160(NUC1) PICST_69376(NBM8)
                 PICST_71972(ACP1) PICST_74163(NUO30) PICST_76018(NUE1)
                 PICST_76226 PICST_76559(NUO24) PICST_79236 PICST_80821(ACP2)
                 PICST_82538 PICST_84570(NBM4) PICST_85822(NUO78)
            CAL: CaO19.4495 CaO19_2091(CaO19.2091) CaO19_2821(CaO19.2821)
                 CaO19_339(CaO19.339) CaO19_4758(CaO19.4758)
                 CaO19_5547(CaO19.5547) CaO19_5713(CaO19.5713)
                 CaO19_6035(CaO19.6035)
            CGR: CAGL0B02431g CAGL0D03586g CAGL0I00748g
            YLI: YALI0F06050g(NUKM)
            SPO: SPAC11E3.12 SPAC3A11.07 SPAC4H3.09 SPBC18E5.10 SPBC947.15c
            ANI: AN1063.2 AN1094.2 AN1728.2 AN2414.2 AN4288.2 AN4297.2
                 AN5629.2 AN5704.2 AN5971.2 AN6077.2 AN7497.2 AN7500.2 AN8049.2
            AFM: AFUA_1G06610 AFUA_1G06620 AFUA_1G11960 AFUA_1G12290
                 AFUA_1G14520 AFUA_2G05450 AFUA_2G05500 AFUA_2G09130
                 AFUA_2G10600 AFUA_3G13910 AFUA_4G05860 AFUA_4G11050
                 AFUA_5G02080 AFUA_5G04370 AFUA_5G06540 AFUA_6G02960
                 AFUA_6G04620 AFUA_6G08810 AFUA_6G12790
            AOR: AO090001000300 AO090001000358 AO090001000459 AO090001000553
                 AO090001000657 AO090001000661 AO090003000400 AO090003001115
                 AO090003001313 AO090011000358 AO090011000502 AO090011000578
                 AO090011000782 AO090026000229 AO090102000645 AO090103000199
                 AO090672000005
            CNE: CNA02430 CNA05580 CNA07650 CNB01310 CNC07090 CND01070
                 CND04070 CND04410 CNE02800 CNE03960 CNF03360 CNG00750 CNH01030
                 CNH02730 CNL04280 CNL05770 CNM01400 CNM02270
            UMA: UM00381.1 UM00512.1 UM00633.1 UM00634.1 UM00718.1 UM00778.1
                 UM01681.1 UM02164.1 UM02437.1 UM03669.1 UM03931.1 UM04822.1
                 UM04924.1 UM05598.1 UM05625.1 UM05902.1 UM06170.1
            DDI: DDBDRAFT_0168392 DDBDRAFT_0184099 DDBDRAFT_0188774
                 DDBDRAFT_0190805 DDBDRAFT_0203708 DDBDRAFT_0206064
                 DDBDRAFT_0218264 DDB_0191420(qinA) DDB_0233205 DDB_0233206
                 DDB_0233208 DDB_0233209 DDB_0233240 DDB_0233241
            PFA: PFI0735c
            CPV: cgd7_1900
            CHO: Chro.70218
            TAN: TA05115
            TET: TTHERM_00193910 TTHERM_00194260 TTHERM_00294640
                 TTHERM_00335630 TTHERM_00557760 TTHERM_01161000
            TBR: Tb09.244.2620 Tb10.389.1140 Tb10.6k15.0960 Tb11.47.0017
                 Tb927.3.860 Tb927.5.450 Tb927.7.6350 Tb927.7.7230
            TCR: 503893.80 506513.190 506839.70 507869.10 508399.10 508507.59
                 508717.20 509809.10 511323.50 511867.140
            LMA: LmjF05.0980 LmjF17.0270 LmjF18.1480 LmjF27.0290 LmjF27.0740
                 LmjF36.5380
            ECO: b1109(ndh)
            ECJ: JW1095(ndh)
            ECE: Z1748(ndh)
            ECS: ECs1487
            ECC: c1382(ndh)
            ECI: UTI89_C1220(acpP) UTI89_C1237(ndh)
            ECP: ECP_1101
            ECV: APECO1_190(ndh)
            ECW: EcE24377A_1231(ndh)
            ECX: EcHS_A1232
            STY: STY1251(ndh)
            STT: t1709(ndh)
            SPT: SPA1640(ndh)
            SEC: SC1161(ndh)
            STM: STM1211(ndh)
            YPE: YPO1617(ndh)
            YPK: y1777(ndh)
            YPM: YP_2237(ndh)
            YPA: YPA_1905 YPA_2046
            YPN: YPN_2012 YPN_2149
            YPP: YPDSF_1964
            YPS: YPTB2447(ndh)
            YPI: YpsIP31758_1594(ndh)
            SFL: SF1113(ndh)
            SFX: S1193(ndh)
            SFV: SFV_1129(ndh)
            SSN: SSON_1129(ndh)
            SBO: SBO_1952(ndh)
            SDY: SDY_2041(ndh)
            ECA: ECA1815(ndh)
            PLU: plu2821(ndh)
            WBR: WGLp098(ndh)
            SGL: SG1073
            ENT: Ent638_2831
            HIN: HI0747(ndh)
            HIT: NTHI0903(ndhA)
            HDU: HD0874(ndh)
            MSU: MS0181(ndh)
            APL: APL_1271(ndh)
            XCC: XCC3769(ndh)
            XCB: XC_3841
            XCV: XCV3947
            XAC: XAC3822(ndh)
            XOO: XOO4294(ndh)
            XOM: XOO_4048(XOO4048)
            VCH: VC1890
            VCO: VC0395_A1480(ndh)
            VVU: VV1_2074 VV1_2075
            VVY: VV2368
            VPA: VP0971
            VFI: VF1143 VF2364
            PPR: PBPRA2396 PBPRB1564
            PAE: PA2691 PA4538(ndh)
            PAU: PA14_29320 PA14_58870(ndh)
            PPU: PP_0626(ndh)
            PST: PSPTO_0917(ndH)
            PSB: Psyr_0790
            PSP: PSPPH_0809(ndh)
            PFL: PFL_5296(ndh)
            PFO: Pfl_2451 Pfl_3604 Pfl_4831
            PEN: PSEEN2040 PSEEN2617 PSEEN4675(ndh)
            ACI: ACIAD3633(ndh)
            SON: SO_3517(ndh)
            SDN: Sden_2710
            SFR: Sfri_2878 Sfri_3431
            SAZ: Sama_0936
            SBL: Sbal_1070
            SLO: Shew_1161 Shew_2195
            SPC: Sputcn32_1072
            SPL: Spea_3414
            SHE: Shewmr4_2944
            SHM: Shewmr7_3026
            SHN: Shewana3_3123
            SHW: Sputw3181_3093
            ILO: IL1690(ndh)
            PHA: PSHAb0118(ndh)
            PAT: Patl_4266
            LPN: lpg0671(ndh)
            LPF: lpl0707
            LPP: lpp0727
            MCA: MCA1918(ndh)
            FTU: FTT1034c(ndh) FTT1425c(naoX)
            FTF: FTF1034c(ndh) FTF1425c(naoX)
            FTL: FTL_1051
            FTH: FTH_1030(ndh)
            FTN: FTN_0912(ndh)
            TCX: Tcr_0239 Tcr_0825
            NOC: Noc_0107 Noc_0390 Noc_1126 Noc_2557 Noc_2562 Noc_2564
            AEH: Mlg_0029
            HHA: Hhal_1757 Hhal_1762 Hhal_1763 Hhal_1764
            HCH: HCH_06629
            CSA: Csal_2325 Csal_3131
            ABO: ABO_0274(ndh)
            MMW: Mmwyl1_2257
            AHA: AHA_2584
            DNO: DNO_0618(ndh)
            RMA: Rmag_0238 Rmag_0240 Rmag_0245
            CVI: CV_0992(ndh) CV_2033
            RSO: RSc0087(RS02261) RSc2229(ndh)
            REU: Reut_A0874 Reut_A0962 Reut_A0964 Reut_A0969 Reut_B4838
            REH: H16_A1815(nrcN) H16_A2740(ndh)
            RME: Rmet_0177 Rmet_2623 Rmet_4310
            BMA: BMA3315 BMAA0320(ndh)
            BMV: BMASAVP1_1501(ndh)
            BML: BMA10299_1697(ndh)
            BMN: BMA10247_A0354(ndh)
            BXE: Bxe_A2958 Bxe_B2833 Bxe_C0262
            BVI: Bcep1808_2326 Bcep1808_2330 Bcep1808_2333 Bcep1808_3896
                 Bcep1808_4249
            BUR: Bcep18194_A5569 Bcep18194_A5573 Bcep18194_A5576
                 Bcep18194_B0999 Bcep18194_B2217 Bcep18194_B2936
                 Bcep18194_B2984
            BCN: Bcen_1629 Bcen_1633 Bcen_1636 Bcen_4492 Bcen_5003
            BCH: Bcen2424_3873 Bcen2424_5857
            BAM: Bamb_3078 Bamb_3244
            BPS: BPSL0263 BPSS1769(ndh)
            BPM: BURPS1710b_0319 BURPS1710b_0455 BURPS1710b_A0534
                 BURPS1710b_A0850(ndh) BURPS1710b_A2214(ftrA) BURPS1710b_A2293
            BPD: BURPS668_A2545(ndh)
            BTE: BTH_II0606
            PNU: Pnuc_0991 Pnuc_1043 Pnuc_1048 Pnuc_1050
            BPE: BP3419 BP3491(ndh)
            BPA: BPP0864(ndh) BPP3569
            BBR: BB0958(ndh) BB4004
            RFR: Rfer_1494 Rfer_1496 Rfer_1501 Rfer_2690
            POL: Bpro_3248 Bpro_3253 Bpro_3255 Bpro_3455 Bpro_3910
            PNA: Pnap_1280 Pnap_1425 Pnap_1427 Pnap_1432
            AAV: Aave_1264 Aave_1266 Aave_1271 Aave_3130
            AJS: Ajs_0958 Ajs_0960 Ajs_0961 Ajs_0965
            VEI: Veis_2805 Veis_2810
            MPT: Mpe_A0160 Mpe_A2216 Mpe_A2974
            HAR: HEAR1818(nuoI) HEAR1822(nuoE) HEAR1825 HEAR2035 HEAR2516(ndh)
            MMS: mma_1033 mma_2605
            NEU: NE2216
            NMU: Nmul_A2450
            EBA: ebA3382 ebA6958(ndh)
            AZO: azo0769(ahpC) azo0770(ahpF) azo1766(ndh1) azo1834(ndh2)
            DAR: Daro_4134
            TBD: Tbd_2220 Tbd_2361
            MFA: Mfla_2053 Mfla_2060 Mfla_2260 Mfla_2311
            HPA: HPAG1_1165
            HHE: HH1243(ndh)
            TDN: Tmden_1828
            ABU: Abu_2220(ndh)
            GSU: GSU0385
            GME: Gmet_3144
            PCA: Pcar_0020
            PPD: Ppro_0629 Ppro_1624 Ppro_3192
            DVL: Dvul_1888
            DDE: Dde_0642 Dde_2562
            BBA: Bd0332(ndh)
            ADE: Adeh_2153 Adeh_2569 Adeh_2572
            AFW: Anae109_1051
            MXA: MXAN_0385 MXAN_1442
            SFU: Sfum_0200
            WOL: WD1129
            WBM: Wbm0237
            APH: APH_0078 APH_1299
            ERU: Erum0430 Erum7570
            ERW: ERWE_CDS_00330 ERWE_CDS_07970
            ERG: ERGA_CDS_00320 ERGA_CDS_07880
            ECN: Ecaj_0035 Ecaj_0791
            ECH: ECH_0063 ECH_0213
            NSE: NSE_0386
            PUB: SAR11_0499 SAR11_1007(ndufs4)
            MLO: mll5193 mlr0365
            PLA: Plav_3218 Plav_3223 Plav_3224
            SME: SMb20861 SMc00410 SMc04452(ndh)
            SMD: Smed_0898
            ATU: Atu0296 Atu2023(ndh)
            ATC: AGR_C_3667 AGR_C_511
            RET: RHE_CH00312(ypch00117) RHE_CH02760(ndhch) RHE_PD00134(ndhd)
            RLE: RL3214 RL3709
            BME: BMEI1231 BMEII0259 BMEII0786
            BMF: BAB2_0758
            BMS: BRA1041
            BMB: BruAb2_0744
            OAN: Oant_2415 Oant_2422
            BJA: bll0717 bll1051(ndh) bll2792 blr2205 blr3727
            BRA: BRADO2302(ndh) BRADO3480 BRADO3676
            BBT: BBta_4044 BBta_4231
            RPA: RPA0045 RPA1104(ndh)
            RPB: RPB_0660 RPB_4267
            RPC: RPC_0437 RPC_2168
            RPD: RPD_0173 RPD_1327 RPD_2877 RPD_2886 RPD_4164
            RPE: RPE_0505 RPE_2075
            NWI: Nwi_0166 Nwi_1879 Nwi_1883 Nwi_1887
            NHA: Nham_0183 Nham_2219 Nham_2220
            BHE: BH00320
            BQU: BQ00300
            XAU: Xaut_4625 Xaut_4631
            CCR: CC_3604
            SIL: SPO3772
            SIT: TM1040_0742 TM1040_0743
            RSP: RSP_0195 RSP_1151 RSP_3707
            RSH: Rsph17029_1185
            RSQ: Rsph17025_1997 Rsph17025_2776
            JAN: Jann_0866 Jann_1170 Jann_1187
            RDE: RD1_0065 RD1_2501 RD1_2855
            PDE: Pden_2238
            MMR: Mmar10_0113
            ZMO: ZMO1113(ndh)
            NAR: Saro_2292 Saro_2296 Saro_2300 Saro_2301 Saro_2302
            SAL: Sala_1301 Sala_1306 Sala_1308 Sala_1310
            SWI: Swit_0661 Swit_2984 Swit_2985 Swit_2993
            GOX: GOX1675 GOX1849
            GBE: GbCGDNIH1_0702 GbCGDNIH1_1652
            ACR: Acry_0923 Acry_0924 Acry_0929
            RRU: Rru_A1422 Rru_A1556 Rru_A1563
            MAG: amb3931
            MGM: Mmc1_0977 Mmc1_3633
            ABA: Acid345_2526
            SUS: Acid_0111 Acid_3779 Acid_7576
            BSU: BG12390(yumB) BG13203(yjlD) BG14046(yutJ)
            BHA: BH3407 BH3415
            BAN: BA2038
            BAR: GBAA2038
            BAA: BA_2537
            BAT: BAS1891
            BCE: BC2023 BC4925 BC4938 BC5061
            BCA: BCE_2106
            BCZ: BCZK0670(ndh) BCZK1144 BCZK1148(noxC) BCZK1843
            BTK: BT9727_0684(ndh) BT9727_1150 BT9727_1853
            BTL: BALH_0703(ndh) BALH_1107 BALH_4464 BALH_4475 BALH_4602
            BLI: BL01996 BL03146(yumB)
            BLD: BLi02134(yjlD) BLi03392(yumB) BLi03402(yutJ)
            BCL: ABC1842 ABC2924 ABC2937
            BAY: RBAM_022120(yqjM) RBAM_036970
            BPU: BPUM_2106
            OIH: OB1365 OB2350 OB3117 OB3312
            GKA: GK2953 GK2959
            SAU: SA0799 SA0802
            SAV: SAV0938 SAV0941
            SAM: MW0820 MW0823
            SAC: SACOL0944
            SAB: SAB0804c SAB0807
            SAA: SAUSA300_0841 SAUSA300_0844 SAUSA300_2464
            SAO: SAOUHSC_00878
            SEP: SE0632 SE0635
            SER: SERP0524 SERP0527
            SHA: SH2010 SH2013
            SSP: SSP1834 SSP1837
            LMO: lmo2389 lmo2638
            LIN: lin2488 lin2787
            LWE: lwe2337 lwe2588
            LLA: L39857(noxA) L41335(noxB)
            LLC: LACR_0885 LACR_0886
            LLM: llmg_1734(noxB) llmg_1735(noxA)
            SPF: SpyM50918(nox) SpyM51727(ahpF)
            SPD: SPD_1298(nox)
            SAN: gbs1788
            SAK: SAK_1751
            SSA: SSA_1127(nox)
            LPL: lp_0313(ndh1) lp_1069(ndh2)
            LAC: LBA1619 LBA1620
            LSA: LSA0312 LSA0802(nox)
            LSL: LSL_1026(ndh)
            LBR: LVIS_0320
            LCA: LSEI_0186 LSEI_0285 LSEI_2297
            EFA: EF1586(nox)
            OOE: OEOE_1838
            STH: STH404 STH963
            CTC: CTC01178
            CDF: CD2540(nox)
            CKL: CKL_0362(ahpF)
            DRM: Dred_2045
            TTE: TTE2486(ndh)
            MTA: Moth_0978
            MGE: MG_275(nox)
            MPN: MPN394(nox)
            MPU: MYPU_0230(nox)
            MPE: MYPE1690(nox)
            MGA: MGA_0167(hcaD)
            MMY: MSC_0263(nox)
            MMO: MMOB6200(nox)
            MHY: mhp299(nox)
            MHJ: MHJ_0078(nox)
            MHP: MHP7448_0082(nox)
            MSY: MS53_0522(nox)
            MCP: MCAP_0223 MCAP_0858
            MFL: Mfl037
            MTU: Rv0392c(ndhA) Rv1812c Rv1854c(ndh)
            MTC: MT0403(ndh-1) MT1902(ndh-2)
            MBO: Mb0398c(ndhA) Mb1842c Mb1885c(ndh)
            MBB: BCG_0429c(ndhA) BCG_1890c(ndh)
            MLE: ML2061
            MPA: MAP1561c(ndh) MAP3874c
            MSM: MSMEG_3621(ndh) MSMEG_4433 MSMEG_5443
            MUL: MUL_3025(ndh)
            MVA: Mvan_1882
            MGI: Mflv_4484
            MMC: Mmcs_2801
            MKM: Mkms_1601 Mkms_2845
            MJL: Mjls_1547 Mjls_2828
            CGL: NCgl1409(cgl1465)
            CGB: cg1656(ndh)
            CEF: CE1593(ndh)
            CDI: DIP1217(ndh)
            CJK: jk0914(ndh)
            NFA: nfa24230 nfa25420
            RHA: RHA1_ro00125 RHA1_ro01358 RHA1_ro05564 RHA1_ro07103
                 RHA1_ro07256(ndh1) RHA1_ro07273(ndh2) RHA1_ro08842(ndh3)
            SCO: SCO4119(SCD72A.05) SCO6496(SC1E6.05)
            SMA: SAV1892(ndh1) SAV3529(ndh2) SAV4109(ndh3)
            TWH: TWT780(ndh)
            TWS: TW790
            LXX: Lxx17150
            CMI: CMM_2259
            AAU: AAur_0954
            PAC: PPA0152
            NCA: Noca_4289
            TFU: Tfu_0432 Tfu_0950 Tfu_2692 Tfu_2694
            FRA: Francci3_0975 Francci3_3918
            FAL: FRAAL1622(ndh) FRAAL2433 FRAAL6227
            ACE: Acel_0270
            SEN: SACE_0853 SACE_1119 SACE_2978
            BLO: BL1266(nox)
            RXY: Rxyl_1112
            RBA: RB5766(ndh) RB8937(noxA)
            PCU: pc1809(ndh)
            LIL: LB036(ndh)
            LIC: LIC20028(ndh)
            LBJ: LBJ_4031(ndh)
            LBL: LBL_4031(ndh)
            SYN: sll1484(ndbC) slr0851(ndbA) slr1743(ndbB)
            SYW: SYNW0297(ndh) SYNW2165
            SYC: syc1313_d(ndbC) syc1403_c(ndbA) syc1598_c(ndbB)
            SYF: Synpcc7942_0101 Synpcc7942_0198 Synpcc7942_2508
            SYD: Syncc9605_0293 Syncc9605_2310
            SYE: Syncc9902_0383 Syncc9902_2050
            SYG: sync_0344 sync_2511
            SYR: SynRCC307_0389(ndh) SynRCC307_2203(ndh)
            SYX: SynWH7803_0345(ndh)
            CYA: CYA_0862
            CYB: CYB_1748
            TEL: tlr1136(ndbB)
            GVI: gll0525 gll1171 gll3635 glr3503
            ANA: all1126 all1127 all1553 all2964 alr4094 alr5211
            AVA: Ava_0810 Ava_0942 Ava_1859 Ava_2770 Ava_3574 Ava_4035
                 Ava_4653 Ava_4690 Ava_4691 Ava_4759 Ava_4965 Ava_4994
            PMA: Pro0096(ndh)
            PMM: PMM0082
            PMT: PMT1625 PMT1806
            PMN: PMN2A_1446 PMN2A_1659
            PMI: PMT9312_0085
            PMB: A9601_00951
            PMC: P9515_00921
            PMF: P9303_02581 P9303_23921
            PMG: P9301_00941
            PMH: P9215_00951
            PME: NATL1_01471
            TER: Tery_2062 Tery_3500 Tery_3661
            BTH: BT_1537
            BFR: BF1599
            BFS: BF1612(ndh)
            SRU: SRU_2211(ndh)
            CHU: CHU_0250(ndh) CHU_2634(naoX)
            GFO: GFO_1013(ndh)
            FPS: FP1931(ndh)
            CTE: CT0369(ndh)
            CCH: Cag_0288 Cag_0635
            CPH: Cpha266_0962 Cpha266_1073
            PLT: Plut_1582
            DET: DET1324
            DEH: cbdb_A1269
            DRA: DR_0950 DR_1980
            DGE: Dgeo_0528 Dgeo_0898 Dgeo_1949
            TTH: TTC0057 TT_P0054
            TTJ: TTHB098
            AAE: aq_788
            MJA: MJ0649
            MMP: MMP1259
            MAC: MA4636(ndh)
            MBA: Mbar_A0960
            MMA: MM_1296
            MBU: Mbur_1296 Mbur_1767
            MTP: Mthe_1051
            MTH: MTH1354
            MST: Msp_1460
            MSI: Msm_0046 Msm_0783
            MKA: MK0881
            AFU: AF0400(noxA-3)
            HAL: VNG0891G(yjlD) VNG1932G(nolA)
            HMA: rrnAC1301(yjlD2) rrnAC1485(yjlD4) rrnAC3285(nolA)
            HWA: HQ1526A(ndh) HQ2648A(ndh) HQ3146A(nolA)
            NPH: NP2406A(nolA_1) NP3508A(ndh)
            PTO: PTO1177 PTO1479
            PHO: PH1509
            PAB: PAB1931(noxA-2)
            PFU: PF1532
            TKO: TK0304
            RCI: RCIX501(ndh)
            SMR: Smar_0018 Smar_0648
            SSO: SSO1010 SSO2960 SSO3148
            STO: ST2573
            SAI: Saci_1702 Saci_1934
            PIS: Pisl_0336
            PCL: Pcal_1957 Pcal_2046
            PAS: Pars_1001 Pars_2273
            TPE: Tpen_1079
STRUCTURES  PDB: 1NOX  1S3A  2B67  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.99.3
            ExPASy - ENZYME nomenclature database: 1.6.99.3
            ExplorEnz - The Enzyme Database: 1.6.99.3
            ERGO genome analysis and discovery system: 1.6.99.3
            BRENDA, the Enzyme Database: 1.6.99.3
            CAS: 9079-67-8
///
ENTRY       EC 1.6.99.4       Obsolete  Enzyme
NAME        Transferred to 1.18.1.2
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With other acceptors
COMMENT     Transferred entry: now EC 1.18.1.2 ferredoxin-NADP+ reductase (EC
            1.6.99.4 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.99.4
            ExPASy - ENZYME nomenclature database: 1.6.99.4
            ExplorEnz - The Enzyme Database: 1.6.99.4
            ERGO genome analysis and discovery system: 1.6.99.4
            BRENDA, the Enzyme Database: 1.6.99.4
///
ENTRY       EC 1.6.99.5                 Enzyme
NAME        NADH dehydrogenase (quinone);
            reduced nicotinamide adenine dinucleotide (quinone) dehydrogenase;
            NADH-quinone oxidoreductase;
            DPNH-menadione reductase;
            D-diaphorase;
            NADH2 dehydrogenase (quinone)
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With other acceptors
SYSNAME     NADH:(quinone-acceptor) oxidoreductase
REACTION    NADH + H+ + acceptor = NAD+ + reduced acceptor [RN:R00281]
ALL_REAC    R00281
SUBSTRATE   NADH [CPD:C00004];
            H+ [CPD:C00080];
            acceptor [CPD:C00028]
PRODUCT     NAD+ [CPD:C00003];
            reduced acceptor [CPD:C00030]
INHIBITOR   AMP [CPD:C00020];
            2,4-Dinitrophenol [CPD:C02496]
COMMENT     Menaquinone can act as acceptor. Inhibited by AMP and
            2,4-dinitrophenol but not by dicoumarol or folic acid derivatives.
REFERENCE   1  [PMID:4388793]
  AUTHORS   Koli AK, Yearby C, Scott W, Donaldson KO.
  TITLE     Purification and properties of three separate menadione reductases
            from hog liver.
  JOURNAL   J. Biol. Chem. 244 (1969) 621-9.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00190  Oxidative phosphorylation
ORTHOLOGY   KO: K05903  NADH dehydrogenase (quinone)
GENES       ECW: EcE24377A_2569(nuoN) EcE24377A_2570(nuoM)
                 EcE24377A_2571(nuoL) EcE24377A_2572(nuoK) EcE24377A_2573(nuoJ)
                 EcE24377A_2574(nuoI) EcE24377A_2575(nuoH) EcE24377A_2576(nuoG)
                 EcE24377A_2577(nuoF) EcE24377A_2578(nuoE) EcE24377A_2579(nuoC)
                 EcE24377A_2580(nuoB) EcE24377A_2581(nuoA)
            ECX: EcHS_A2425 EcHS_A2426 EcHS_A2427 EcHS_A2428 EcHS_A2429
                 EcHS_A2430 EcHS_A2431 EcHS_A2432 EcHS_A2433 EcHS_A2434
                 EcHS_A2435 EcHS_A2436 EcHS_A2437
            YPA: YPA_2035 YPA_2036 YPA_2037 YPA_2039 YPA_2043
            YPN: YPN_2138 YPN_2139 YPN_2140 YPN_2142 YPN_2146
            YPP: YPDSF_1953 YPDSF_1954 YPDSF_1955 YPDSF_1957 YPDSF_1961
            YPI: YpsIP31758_1454(nuoA) YpsIP31758_1455(nuoB)
                 YpsIP31758_1456(nuoCD) YpsIP31758_1458(nuoF)
                 YpsIP31758_1459(nuoG) YpsIP31758_1460(nuoH)
                 YpsIP31758_1461(nuoI) YpsIP31758_1462(nuoJ)
                 YpsIP31758_1463(nuoK) YpsIP31758_1464(nuoL)
                 YpsIP31758_1465(nuoM) YpsIP31758_1466(nuoN)
            ECA: ECA3023(nuoG) ECA3024(nuoF) ECA3025(nuoE) ECA3026(nuoC)
                 ECA3027(nuoB) ECA3028(nuoA)
            ENT: Ent638_2820 Ent638_2821 Ent638_2822 Ent638_2824 Ent638_2828
            SPE: Spro_2432 Spro_3296 Spro_3297 Spro_3298 Spro_3300 Spro_3302
                 Spro_3304 Spro_3307 Spro_3308
            PAP: PSPA7_2564(nuoG) PSPA7_2566(nuoF)
            PPF: Pput_1734 Pput_1735 Pput_1736 Pput_1740 Pput_1742 Pput_1745
                 Pput_3510 Pput_3553
            PFL: PFL_3898(nuoB) PFL_3900(nuoE) PFL_3901(nuoF) PFL_3902(nuoG)
            PFO: Pfl_3310
            PMY: Pmen_0388 Pmen_1431 Pmen_1433 Pmen_1441 Pmen_2019 Pmen_2413
                 Pmen_2416 Pmen_2418 Pmen_2422 Pmen_2423 Pmen_2424
            PRW: PsycPRwf_1687 PsycPRwf_1688 PsycPRwf_1689 PsycPRwf_1693
                 PsycPRwf_1695 PsycPRwf_1698
            SFR: Sfri_2286 Sfri_2288 Sfri_2290 Sfri_2741 Sfri_2742
            SSE: Ssed_1397 Ssed_1398 Ssed_3666 Ssed_3667 Ssed_3669
            SPL: Spea_3284 Spea_3285 Spea_3287
            PIN: Ping_1357 Ping_1359
            MAQ: Maqu_1368 Maqu_2849 Maqu_2851 Maqu_2855 Maqu_2858
            FTW: FTW_0114(nuoI)
            FTH: FTH_1766(nuoA)
            FTA: FTA_1936 FTA_1938
            TCX: Tcr_0061 Tcr_0062 Tcr_0063 Tcr_0828 Tcr_0829 Tcr_0830
            NOC: Noc_0478 Noc_0480 Noc_0481 Noc_1119 Noc_1120 Noc_1125
                 Noc_1248 Noc_1249 Noc_1250 Noc_1252 Noc_1280 Noc_1281 Noc_2552
                 Noc_2553 Noc_2554 Noc_2556 Noc_2559 Noc_2560 Noc_2563
            AEH: Mlg_0743 Mlg_0744 Mlg_2090 Mlg_2093
            HHA: Hhal_0812 Hhal_0813 Hhal_1752 Hhal_1753 Hhal_1754 Hhal_1760
                 Hhal_2032 Hhal_2035
            CSA: Csal_0901 Csal_0903 Csal_0996 Csal_3120 Csal_3121 Csal_3122
                 Csal_3124 Csal_3128
            MMW: Mmwyl1_2275 Mmwyl1_3982 Mmwyl1_3984
            RMA: Rmag_0242 Rmag_0248 Rmag_0249 Rmag_0250
            REU: Reut_A0618 Reut_A0963 Reut_A0966 Reut_A0970 Reut_A0972
                 Reut_A0973 Reut_A0974 Reut_A1678 Reut_B4588 Reut_B4652
            RME: Rmet_0939 Rmet_0940 Rmet_4300
            BMV: BMASAVP1_0658(nuoB-2) BMASAVP1_A1131(nuoB-1)
            BML: BMA10299_0954(nuoB-2) BMA10299_A0736(nuoB-1)
            BMN: BMA10247_0414(nuoB-1) BMA10247_A1924(nuoB-2)
            BVI: Bcep1808_0953 Bcep1808_1974 Bcep1808_2321 Bcep1808_2322
                 Bcep1808_2323 Bcep1808_2329 Bcep1808_2332
            BUR: Bcep18194_A4145 Bcep18194_A5377 Bcep18194_A5564
                 Bcep18194_A5565 Bcep18194_A5566 Bcep18194_A5568
                 Bcep18194_A5571 Bcep18194_A5572 Bcep18194_A5575
            BCN: Bcen_0553 Bcen_1625 Bcen_1626 Bcen_1631 Bcen_1632 Bcen_1635
            BCH: Bcen2424_1032
            BAM: Bamb_0896 Bamb_2274
            BPM: BURPS1710b_1436(nuoB) BURPS1710b_3588(nuoB-2)
            BPL: BURPS1106A_1299(nuoA) BURPS1106A_1300(nuoB)
                 BURPS1106A_1301(nuoC) BURPS1106A_1302(nuoD)
                 BURPS1106A_1303(nuoE) BURPS1106A_1304(nuoF)
                 BURPS1106A_1305(nuoG) BURPS1106A_1306(nuoH)
                 BURPS1106A_1307(nuoI) BURPS1106A_1308(nuoJ)
                 BURPS1106A_1309(nuoK) BURPS1106A_1310(nuoL)
                 BURPS1106A_1311(nuoM) BURPS1106A_1312(nuoN)
            BPD: BURPS668_1290(nuoA) BURPS668_1291(nuoB) BURPS668_1292(nuoC)
                 BURPS668_1293(nuoD) BURPS668_1294(nuoE) BURPS668_1295(nuoF)
                 BURPS668_1296(nuoG) BURPS668_1297(nuoH) BURPS668_1298(nuoI)
                 BURPS668_1299(nuoJ) BURPS668_1300(nuoK) BURPS668_1301(nuoL)
                 BURPS668_1302(nuoM) BURPS668_1303(nuoN)
            PNU: Pnuc_1038 Pnuc_1039 Pnuc_1040 Pnuc_1046 Pnuc_1049 Pnuc_1110
            RFR: Rfer_1498 Rfer_1504 Rfer_1505 Rfer_1506 Rfer_3270 Rfer_3276
                 Rfer_3289 Rfer_3292
            POL: Bpro_0916 Bpro_0919 Bpro_2804 Bpro_3243 Bpro_3244 Bpro_3245
                 Bpro_3251 Bpro_3254
            PNA: Pnap_0825 Pnap_1426 Pnap_1429 Pnap_1435 Pnap_1436 Pnap_1437
                 Pnap_1524
            AAV: Aave_1265 Aave_1268 Aave_1274 Aave_1275 Aave_1276 Aave_3289
            AJS: Ajs_0959 Ajs_0962 Ajs_0968 Ajs_0969 Ajs_0970 Ajs_2474
                 Ajs_3471
            VEI: Veis_2384 Veis_2800 Veis_2801 Veis_2802 Veis_2808 Veis_3909
            HAR: HEAR0357 HEAR1813(nuoN) HEAR1814(nuoM) HEAR1815(nuoL)
                 HEAR1816(nuoK) HEAR1817(nuoJ) HEAR1820(nuoG) HEAR1821(nuoF)
                 HEAR3433
            NET: Neut_1697
            NMU: Nmul_A0709 Nmul_A1102 Nmul_A1103 Nmul_A1104 Nmul_A1591
            TBD: Tbd_2655
            MFA: Mfla_0580 Mfla_0582 Mfla_0721 Mfla_2048 Mfla_2049 Mfla_2050
                 Mfla_2056 Mfla_2059
            TDN: Tmden_1815 Tmden_1816 Tmden_1817
            CJR: CJE1737(nuoN) CJE1738(nuoM) CJE1739(nuoL) CJE1740(nuoK)
                 CJE1741(nuoJ) CJE1742(nuoI) CJE1743(nuoH) CJE1744(nuoG)
                 CJE1745 CJE1746 CJE1747(nuoD) CJE1748(nuoC) CJE1749(nuoB)
                 CJE1750(nuoA)
            CJJ: CJJ81176_1551(nuoN) CJJ81176_1552(nuoM) CJJ81176_1553(nuoL)
                 CJJ81176_1554(nuoK) CJJ81176_1555(nuoJ) CJJ81176_1556(nuoI)
                 CJJ81176_1557(nuoH) CJJ81176_1558(nuoG) CJJ81176_1561(nuoD)
                 CJJ81176_1562(nuoC) CJJ81176_1563(nuoB) CJJ81176_1564(nuoA)
            CJU: C8J_1468(nuoI) C8J_1470(nuoG) C8J_1476(nuoA)
            CJD: JJD26997_1917(nuoN) JJD26997_1918(nuoM) JJD26997_1919(nuoL)
                 JJD26997_1920(nuoK) JJD26997_1921(nuoJ) JJD26997_1922(nuoI)
                 JJD26997_1923(nuoH) JJD26997_1924(nuoG) JJD26997_1927(nuoD)
                 JJD26997_1928(nuoC) JJD26997_1929(nuoB) JJD26997_1930(nuoA)
            CFF: CFF8240_0157(nuoA) CFF8240_0158 CFF8240_0159 CFF8240_0161
                 CFF8240_0162(nuoG) CFF8240_0165 CFF8240_0166(nuoK)
                 CFF8240_0167 CFF8240_0168
            CCV: CCV52592_1517 CCV52592_1518 CCV52592_1519 CCV52592_1521
                 CCV52592_1522 CCV52592_1526(nuoD)
            CHA: CHAB381_0184(nuoD) CHAB381_0188 CHAB381_0189
                 CHAB381_0190(nuoJ) CHAB381_0191(nuoK) CHAB381_0192
                 CHAB381_0193
            CCO: CCC13826_1664
            ABU: Abu_0306(nuoJ)
            GUR: Gura_0313 Gura_0314 Gura_0320 Gura_0325 Gura_0329 Gura_0803
                 Gura_0889 Gura_0892 Gura_2653 Gura_4066 Gura_4231 Gura_4232
                 Gura_4233 Gura_4237 Gura_4239 Gura_4241 Gura_4243
            PPD: Ppro_0070 Ppro_0336 Ppro_0339 Ppro_0587 Ppro_0588 Ppro_0589
                 Ppro_0633 Ppro_0639 Ppro_0640 Ppro_0641 Ppro_1489 Ppro_1628
                 Ppro_1634 Ppro_1635 Ppro_1636 Ppro_2787 Ppro_2795 Ppro_3180
                 Ppro_3181 Ppro_3182 Ppro_3188 Ppro_3218 Ppro_3221 Ppro_3516
                 Ppro_3530 Ppro_3531 Ppro_3532
            DVL: Dvul_0969 Dvul_2501
            ADE: Adeh_0413 Adeh_0414 Adeh_0415 Adeh_2564 Adeh_2566 Adeh_2568
                 Adeh_2579 Adeh_2580 Adeh_2581 Adeh_3654 Adeh_3655 Adeh_3658
                 Adeh_4197 Adeh_4198 Adeh_4199
            AFW: Anae109_1279 Anae109_1280 Anae109_1281 Anae109_1285
                 Anae109_1286 Anae109_1288 Anae109_1291 Anae109_1293
                 Anae109_1295 Anae109_3780 Anae109_3781 Anae109_3784
                 Anae109_4154 Anae109_4155 Anae109_4156 Anae109_4348
            SFU: Sfum_0207 Sfum_0208 Sfum_0209 Sfum_0845 Sfum_1935 Sfum_1936
                 Sfum_1937 Sfum_1955 Sfum_2704 Sfum_2713
            APH: APH_0434(nuoF) APH_0435(nuoJ) APH_0436(nuoK) APH_0437(nuoL)
                 APH_0438(nuoM) APH_0439(nuoN) APH_0519(nuoA) APH_0520(nuoB)
                 APH_0521(nuoC) APH_0711(nuoH) APH_0712(nuoG) APH_0731(nuoE)
                 APH_0732(nuoD) APH_0801(nuoI)
            ERU: Erum1240 Erum3070(nuoC) Erum3080 Erum3090(nuoB)
                 Erum3100(nuoA) Erum3710(nuoI) Erum4270(nuoG) Erum4280(nuoH)
                 Erum4290 Erum4300 Erum4420(nuoD) Erum4430(nuoE) Erum4760(nuoN)
                 Erum4770(nuoM) Erum4780(nuoL) Erum4790(nuoK) Erum4800(nuoJ)
                 Erum4810(nuoF) Erum5440 Erum6700
            ERW: ERWE_CDS_01200(nuoN)
            ERG: ERGA_CDS_01160(nuoN)
            ECN: Ecaj_0121
            ECH: ECH_0548(nuoF) ECH_0552(nuoJ) ECH_0553(nuoK) ECH_0554(nuoL)
                 ECH_0555(nuoM) ECH_0556(nuoN) ECH_0615(nuoE) ECH_0616(nuoD)
                 ECH_0617(nuoH) ECH_0618(nuoG) ECH_0691(nuoI) ECH_0786(nuoA)
                 ECH_0787(nuoB) ECH_0788(nuoC)
            NSE: NSE_0010(nuoJ) NSE_0012(nuoK) NSE_0014(nuoL) NSE_0053(nuoG)
                 NSE_0054(nuoH) NSE_0429(nuoA) NSE_0431(nuoB) NSE_0432(nuoC)
                 NSE_0566(nuoD) NSE_0636(nuoE) NSE_0691(nuoM) NSE_0692(nuoN)
                 NSE_0714(nuoF)
            PLA: Plav_2964 Plav_2966 Plav_2967 Plav_3214 Plav_3215 Plav_3219
                 Plav_3221 Plav_3222 Plav_3225
            SMD: Smed_0607 Smed_0610 Smed_0889 Smed_0891 Smed_0893 Smed_0894
                 Smed_0897 Smed_0901 Smed_0902 Smed_2806 Smed_2898 Smed_3614
                 Smed_3618 Smed_3620 Smed_3621 Smed_3622 Smed_3624 Smed_3625
                 Smed_3626 Smed_3628
            RLE: RL1712(nqo14) RL1714(nuoN) pRL110294(hyfF) pRL110297(hyfB)
            BOV: BOV_0800(nuoD) BOV_0802(nuoF) BOV_0803(nuoG)
            OAN: Oant_2411 Oant_2412 Oant_2416 Oant_2418 Oant_2419 Oant_2420
                 Oant_2423 Oant_3531
            BRA: BRADO4171(nuoN) BRADO4172(nuoM) BRADO4173(nuoL)
                 BRADO4174(nuoK) BRADO4175(nuoJ) BRADO4176(nuoII)
                 BRADO4177(nuoH) BRADO4178(nuoG) BRADO4179(nuoF)
                 BRADO4181(nuoE) BRADO4183(nuoD) BRADO4184(nuoC)
                 BRADO4185(nuoB) BRADO4186(nuoA)
            BBT: BBta_4548(nuoN) BBta_4549(nuoM) BBta_4550(nuoL)
                 BBta_4551(nuoK) BBta_4552(nuoJ) BBta_4553(nuoII)
                 BBta_4554(nuoH) BBta_4555(nuoG) BBta_4556(nuoF)
                 BBta_4558(nuoE) BBta_4560(nuoD) BBta_4561(nuoC)
                 BBta_4562(nuoB) BBta_4563(nuoA)
            RPB: RPB_0725 RPB_1260 RPB_1263
            RPC: RPC_0929 RPC_0932 RPC_3855 RPC_3857 RPC_4506 RPC_4571
                 RPC_4573 RPC_4575 RPC_4646
            RPD: RPD_0674 RPD_0676 RPD_1330 RPD_1336 RPD_1337 RPD_1338
                 RPD_2872 RPD_2873 RPD_2874 RPD_2876 RPD_2880 RPD_3852 RPD_3855
            RPE: RPE_0952 RPE_0955 RPE_3871 RPE_3873 RPE_4648
            NWI: Nwi_1874 Nwi_1875 Nwi_1876 Nwi_1878 Nwi_1881 Nwi_1882
                 Nwi_1992
            NHA: Nham_1010 Nham_2207 Nham_2208 Nham_2209 Nham_2215
            BBK: BARBAKC583_0778(nuoA) BARBAKC583_0779(nuoB)
                 BARBAKC583_0780(nuoC) BARBAKC583_0781(nuoD)
                 BARBAKC583_0782(nuoE) BARBAKC583_0783(nuoF)
                 BARBAKC583_0784(nuoG) BARBAKC583_0785(nuoH)
                 BARBAKC583_0786(nuoI) BARBAKC583_0787(nuoJ)
                 BARBAKC583_0788(nuoK) BARBAKC583_0789(nuoL)
                 BARBAKC583_0790(nuoM) BARBAKC583_0791(nuoN)
            XAU: Xaut_0166 Xaut_0169 Xaut_1582 Xaut_3480 Xaut_3932 Xaut_4621
                 Xaut_4622 Xaut_4626 Xaut_4628 Xaut_4629 Xaut_4630 Xaut_4632
            SIT: TM1040_0758 TM1040_0759 TM1040_0760 TM1040_1538 TM1040_1540
            RSH: Rsph17029_1180 Rsph17029_1187 Rsph17029_1189 Rsph17029_1190
                 Rsph17029_1191 Rsph17029_1740 Rsph17029_1746 Rsph17029_1747
                 Rsph17029_1748 Rsph17029_2652 Rsph17029_2654 Rsph17029_2740
                 Rsph17029_3449
            RSQ: Rsph17025_0230 Rsph17025_0232 Rsph17025_1690 Rsph17025_1693
                 Rsph17025_1695 Rsph17025_1699 Rsph17025_1700 Rsph17025_1701
                 Rsph17025_1992 Rsph17025_1993 Rsph17025_1998 Rsph17025_2001
                 Rsph17025_2003 Rsph17025_2004 Rsph17025_2006 Rsph17025_2854
            JAN: Jann_1190 Jann_1194 Jann_1195 Jann_1196 Jann_2559 Jann_3692
                 Jann_3695 Jann_3715 Jann_3717
            RDE: RD1_3276(nuoH) RD1_3282(nuoF) RD1_3287(nuoD) RD1_3290(nuoC)
                 RD1_3291(nuoB)
            PDE: Pden_0697 Pden_0699 Pden_1289 Pden_2231 Pden_2232 Pden_2233
                 Pden_2235 Pden_2243 Pden_2857
            MMR: Mmar10_0890 Mmar10_0891 Mmar10_0893 Mmar10_2683
            NAR: Saro_0733 Saro_2287 Saro_2288 Saro_2289 Saro_2295
            SAL: Sala_1296 Sala_1297 Sala_1298 Sala_1305
            SWI: Swit_1474 Swit_2983 Swit_2986 Swit_2988 Swit_2992 Swit_2996
                 Swit_2997 Swit_2998
            ELI: ELI_06605
            ACR: Acry_0605 Acry_0840 Acry_0922 Acry_0925 Acry_0926 Acry_0928
                 Acry_0932 Acry_0933 Acry_0934 Acry_1108 Acry_1109 Acry_1110
                 Acry_1114 Acry_1116 Acry_1119 Acry_1396 Acry_1399 Acry_2333
            RRU: Rru_A0314 Rru_A0315 Rru_A0318 Rru_A0320 Rru_A1420 Rru_A1560
                 Rru_A1561 Rru_A1564 Rru_A1566 Rru_A1567 Rru_A1568 Rru_A1632
                 Rru_A1634 Rru_A1635
            MGM: Mmc1_2210 Mmc1_3622 Mmc1_3624 Mmc1_3630
            ABA: Acid345_1303 Acid345_1304 Acid345_1305 Acid345_1311
            SUS: Acid_0113 Acid_0118 Acid_0119 Acid_0120 Acid_2320 Acid_5018
                 Acid_5688 Acid_5689 Acid_5690
            BCY: Bcer98_1106 Bcer98_3809 Bcer98_3810 Bcer98_3811 Bcer98_3815
                 Bcer98_3816 Bcer98_3818
            SAJ: SaurJH9_0474 SaurJH9_0645 SaurJH9_0648 SaurJH9_0949
                 SaurJH9_0952
            SAH: SaurJH1_0487 SaurJH1_0660 SaurJH1_0663 SaurJH1_0968
                 SaurJH1_0971
            CTH: Cthe_0341 Cthe_0429 Cthe_3024
            CBE: Cbei_2986 Cbei_2987 Cbei_2988 Cbei_2992 Cbei_2993 Cbei_2995
                 Cbei_4111
            AMT: Amet_0640 Amet_1149 Amet_3095 Amet_4100 Amet_4108 Amet_4150
                 Amet_4151 Amet_4152
            DRM: Dred_1652 Dred_1655 Dred_1857 Dred_2036 Dred_2037 Dred_2038
                 Dred_3291
            SWO: Swol_1018 Swol_1024 Swol_1828
            CSC: Csac_0620 Csac_1534 Csac_1863
            MTA: Moth_0985 Moth_0987 Moth_1718 Moth_2187 Moth_2188 Moth_2191
            MAV: MAV_4033(nuoA) MAV_4034 MAV_4035 MAV_4037 MAV_4040 MAV_4041
                 MAV_4043(nuoK) MAV_4044 MAV_4045 MAV_4047
            MVA: Mvan_0742 Mvan_0744 Mvan_1872 Mvan_1873 Mvan_1874 Mvan_1880
            MGI: Mflv_0162 Mflv_0164 Mflv_4486 Mflv_4492 Mflv_4493 Mflv_4494
            MMC: Mmcs_0584 Mmcs_0586 Mmcs_1575
            MKM: Mkms_0596 Mkms_0598 Mkms_1588 Mkms_1589 Mkms_1590 Mkms_1599
            MJL: Mjls_0574 Mjls_0576 Mjls_1534 Mjls_1535 Mjls_1536 Mjls_1545
                 Mjls_4493 Mjls_4494 Mjls_4495
            ART: Arth_3659 Arth_3871 Arth_3873 Arth_4496 Arth_4497 Arth_4498
            NCA: Noca_0525 Noca_0531 Noca_0532 Noca_0533 Noca_4466 Noca_4469
            TFU: Tfu_0348 Tfu_0350 Tfu_2682 Tfu_2683 Tfu_2684 Tfu_2690
            FRA: Francci3_0538 Francci3_0539 Francci3_0540 Francci3_0541
                 Francci3_0542 Francci3_0543 Francci3_0544 Francci3_0545
                 Francci3_0546 Francci3_0547 Francci3_0548 Francci3_0549
                 Francci3_0550 Francci3_0551
            ACE: Acel_0272 Acel_0278 Acel_0279 Acel_0280 Acel_0729
            KRA: Krad_0044 Krad_0046
            SEN: SACE_6542 SACE_6545
            STP: Strop_0390 Strop_0393 Strop_0403 Strop_0404 Strop_0405
                 Strop_0771 Strop_0772 Strop_0773 Strop_3231 Strop_4052
                 Strop_4053 Strop_4058 Strop_4060 Strop_4062 Strop_4064
                 Strop_4286
            RXY: Rxyl_0123 Rxyl_0124 Rxyl_0125 Rxyl_1626 Rxyl_1798 Rxyl_1800
                 Rxyl_3145 Rxyl_3148
            SYF: Synpcc7942_0279 Synpcc7942_2092
            SYD: Syncc9605_0596 Syncc9605_1030 Syncc9605_2400 Syncc9605_2401
            SYE: Syncc9902_0292 Syncc9902_0293 Syncc9902_0931 Syncc9902_1766
            AVA: Ava_0748 Ava_0749 Ava_1746 Ava_2153 Ava_2308 Ava_2715
                 Ava_4654 Ava_4787
            PMN: PMN2A_0030 PMN2A_1515 PMN2A_1516 PMN2A_1767
            PMI: PMT9312_0434 PMT9312_0594
            TER: Tery_0349 Tery_0659 Tery_0660 Tery_2529 Tery_3241 Tery_3853
            BFS: BF0790(nuoC) BF0791(nuoB) BF0792(nuoA)
            SRU: SRU_0395
            FJO: Fjoh_1233 Fjoh_1234 Fjoh_1235 Fjoh_1239 Fjoh_1241 Fjoh_1243
                 Fjoh_1245
            FPS: FP2218(nuoN) FP2219(nuoM) FP2220(nuoL) FP2221(nuoK)
                 FP2222(nuoJ) FP2223(nuoI) FP2224(nuoH) FP2225(nuoG)
                 FP2227(nuoF) FP2228(nuoE) FP2229(nuoD) FP2230(nuoC)
                 FP2231(nuoB) FP2232(nuoA)
            CCH: Cag_0636 Cag_0639 Cag_0642 Cag_0643 Cag_0644
            CPH: Cpha266_0969 Cpha266_0970 Cpha266_0971
            PVI: Cvib_1083 Cvib_1084 Cvib_1085 Cvib_1257 Cvib_1260
            PLT: Plut_0751 Plut_0752 Plut_0753
            DEB: DehaBAV1_0225 DehaBAV1_0661 DehaBAV1_0778 DehaBAV1_0782
                 DehaBAV1_0808 DehaBAV1_0810 DehaBAV1_0811 DehaBAV1_0815
                 DehaBAV1_0816 DehaBAV1_0817 DehaBAV1_1318 DehaBAV1_1321
            RRS: RoseRS_2099 RoseRS_2102 RoseRS_2230 RoseRS_2231 RoseRS_2232
                 RoseRS_2236 RoseRS_2238 RoseRS_2990 RoseRS_2992 RoseRS_2994
                 RoseRS_2997 RoseRS_2998 RoseRS_2999 RoseRS_3000 RoseRS_3542
                 RoseRS_3675 RoseRS_3676 RoseRS_3677 RoseRS_3854
            RCA: Rcas_0566 Rcas_1321 Rcas_1323 Rcas_1365 Rcas_1768 Rcas_1771
                 Rcas_2089 Rcas_2091 Rcas_2093 Rcas_2096 Rcas_2097 Rcas_2098
                 Rcas_2099 Rcas_3382 Rcas_3383 Rcas_3384 Rcas_3388 Rcas_3391
            DGE: Dgeo_0914 Dgeo_0920
            TPT: Tpet_0696 Tpet_0913 Tpet_1368
            TME: Tmel_0491 Tmel_1168 Tmel_1170 Tmel_1217 Tmel_1221
            FNO: Fnod_0226 Fnod_0991 Fnod_0993 Fnod_1737 Fnod_1741
            MMQ: MmarC5_1781
            MMZ: MmarC7_0707 MmarC7_0875
            MAE: Maeo_0306 Maeo_0940 Maeo_0943 Maeo_1353
            MVN: Mevan_0473 Mevan_0773 Mevan_0937
            MBU: Mbur_0132 Mbur_0135 Mbur_1287 Mbur_1288 Mbur_1289
            MTP: Mthe_1058 Mthe_1059 Mthe_1060
            MHU: Mhun_1274 Mhun_1741 Mhun_1819 Mhun_1822 Mhun_2586
            MEM: Memar_0364
            MBN: Mboo_0024 Mboo_1124 Mboo_1127
            HMA: pNG7037(ndhF)
            SMR: Smar_0028 Smar_0645 Smar_1071
            IHO: Igni_0545 Igni_0546 Igni_1144
            HBU: Hbut_0185 Hbut_0190 Hbut_0191 Hbut_0192
            MSE: Msed_1897 Msed_1898 Msed_1902 Msed_1903 Msed_2012
            PIS: Pisl_1628 Pisl_1629
            PCL: Pcal_0519 Pcal_0520
            PAS: Pars_0650 Pars_0651
            TPE: Tpen_0180 Tpen_0184 Tpen_0185 Tpen_0188 Tpen_1076 Tpen_1077
                 Tpen_1086 Tpen_1087 Tpen_1088
STRUCTURES  PDB: 2FUG  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.99.5
            ExPASy - ENZYME nomenclature database: 1.6.99.5
            ExplorEnz - The Enzyme Database: 1.6.99.5
            ERGO genome analysis and discovery system: 1.6.99.5
            BRENDA, the Enzyme Database: 1.6.99.5
            CAS: 37256-36-3
///
ENTRY       EC 1.6.99.6                 Enzyme
NAME        NADPH dehydrogenase (quinone);
            reduced nicotinamide adenine dinucleotide phosphate (quinone)
            dehydrogenase;
            NADPH oxidase;
            NADPH2 dehydrogenase (quinone)
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With other acceptors
SYSNAME     NADPH:(quinone-acceptor) oxidoreductase
REACTION    NADPH + H+ + acceptor = NADP+ + reduced acceptor [RN:R00282]
ALL_REAC    R00282
SUBSTRATE   NADPH [CPD:C00005];
            H+ [CPD:C00080];
            acceptor [CPD:C00028]
PRODUCT     NADP+ [CPD:C00006];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016];
            Flavoprotein [CPD:C06411]
INHIBITOR   Folate [CPD:C00504];
            Dicumarol [CPD:C00796]
COMMENT     A flavoprotein. Menaquinone can act as acceptor. Inhibited by
            dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.
REFERENCE   1  [PMID:4388793]
  AUTHORS   Koli AK, Yearby C, Scott W, Donaldson KO.
  TITLE     Purification and properties of three separate menadione reductases
            from hog liver.
  JOURNAL   J. Biol. Chem. 244 (1969) 621-9.
  ORGANISM  pig [GN:ssc]
GENES       PSP: PSPPH_0710(mdaB)
STRUCTURES  PDB: 1F5V  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.99.6
            ExPASy - ENZYME nomenclature database: 1.6.99.6
            ExplorEnz - The Enzyme Database: 1.6.99.6
            ERGO genome analysis and discovery system: 1.6.99.6
            BRENDA, the Enzyme Database: 1.6.99.6
            CAS: 37256-37-4
///
ENTRY       EC 1.6.99.7       Obsolete  Enzyme
NAME        Transferred to 1.5.1.34
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With other acceptors
COMMENT     Transferred entry: now EC 1.5.1.34, 6,7-dihydropteridine reductase
            (EC 1.6.99.7 created 1972, modified 1981 (EC 1.6.99.10 created 1978,
            incorporated 1981), deleted 2003)
STRUCTURES  PDB: 1DIR  1DS7  1GVH  1HDR  1ICR  1ICU  1ICV  1IDT  1OO5  1OO6  
                 1OOE  1OON  1OOQ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.99.7
            ExPASy - ENZYME nomenclature database: 1.6.99.7
            ExplorEnz - The Enzyme Database: 1.6.99.7
            ERGO genome analysis and discovery system: 1.6.99.7
            BRENDA, the Enzyme Database: 1.6.99.7
///
ENTRY       EC 1.6.99.8       Obsolete  Enzyme
NAME        Transferred to 1.16.1.3
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With other acceptors
COMMENT     Transferred entry: now EC 1.16.1.3 aquacobalamin reductase (EC
            1.6.99.8 created 1972, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.99.8
            ExPASy - ENZYME nomenclature database: 1.6.99.8
            ExplorEnz - The Enzyme Database: 1.6.99.8
            ERGO genome analysis and discovery system: 1.6.99.8
            BRENDA, the Enzyme Database: 1.6.99.8
///
ENTRY       EC 1.6.99.9       Obsolete  Enzyme
NAME        Transferred to 1.16.1.4
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With other acceptors
COMMENT     Transferred entry: now EC 1.16.1.4, cob(II)alamin reductase (EC
            1.6.99.9 created 1972, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.99.9
            ExPASy - ENZYME nomenclature database: 1.6.99.9
            ExplorEnz - The Enzyme Database: 1.6.99.9
            ERGO genome analysis and discovery system: 1.6.99.9
            BRENDA, the Enzyme Database: 1.6.99.9
///
ENTRY       EC 1.6.99.10      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With other acceptors
COMMENT     Deleted entry: Now included with EC 1.5.1.34, 6,7-dihydropteridine
            reductase (EC 1.6.99.10 created 1978, deleted 1981)
STRUCTURES  PDB: 1DHR  
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.99.10
            ExPASy - ENZYME nomenclature database: 1.6.99.10
            ExplorEnz - The Enzyme Database: 1.6.99.10
            ERGO genome analysis and discovery system: 1.6.99.10
            BRENDA, the Enzyme Database: 1.6.99.10
///
ENTRY       EC 1.6.99.11      Obsolete  Enzyme
NAME        Transferred to 1.16.1.5
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With other acceptors
COMMENT     Transferred entry: now EC 1.16.1.5, aquacobalamin reductase (NADPH)
            (EC 1.6.99.11 created 1989, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.99.11
            ExPASy - ENZYME nomenclature database: 1.6.99.11
            ExplorEnz - The Enzyme Database: 1.6.99.11
            ERGO genome analysis and discovery system: 1.6.99.11
            BRENDA, the Enzyme Database: 1.6.99.11
///
ENTRY       EC 1.6.99.12      Obsolete  Enzyme
NAME        Transferred to 1.16.1.6
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With other acceptors
COMMENT     Transferred entry: now EC 1.16.1.6, cyanocobalamin reductase
            (cyanide-eliminating) (EC 1.6.99.12 created 1989, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.99.12
            ExPASy - ENZYME nomenclature database: 1.6.99.12
            ExplorEnz - The Enzyme Database: 1.6.99.12
            ERGO genome analysis and discovery system: 1.6.99.12
            BRENDA, the Enzyme Database: 1.6.99.12
///
ENTRY       EC 1.6.99.13      Obsolete  Enzyme
NAME        Transferred to 1.16.1.7
CLASS       Oxidoreductases;
            Acting on NADH or NADPH;
            With other acceptors
COMMENT     Transferred entry: now EC 1.16.1.7 ferric-chelate reductase (EC
            1.6.99.13 created 1992, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.6.99.13
            ExPASy - ENZYME nomenclature database: 1.6.99.13
            ExplorEnz - The Enzyme Database: 1.6.99.13
            ERGO genome analysis and discovery system: 1.6.99.13
            BRENDA, the Enzyme Database: 1.6.99.13
///
ENTRY       EC 1.7.1.1                  Enzyme
NAME        nitrate reductase (NADH);
            assimilatory nitrate reductase;
            NADH-nitrate reductase;
            NADH-dependent nitrate reductase;
            assimilatory NADH: nitrate reductase;
            nitrate reductase (NADH2);
            NADH2:nitrate oxidoreductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     nitrite:NAD+ oxidoreductase
REACTION    nitrite + NAD+ + H2O = nitrate + NADH + H+ [RN:R00794]
ALL_REAC    R00794
SUBSTRATE   nitrite [CPD:C00088];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     nitrate [CPD:C00244];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016];
            FMN [CPD:C00061];
            Molybdenum [CPD:C00150]
COMMENT     An iron-sulfur molybdenum flavoprotein.
REFERENCE   1  [PMID:13699254]
  AUTHORS   FEWSON CA, NICHOLAS DJ.
  TITLE     Nitrate reductase from Pseudomonas aeruginosa.
  JOURNAL   Biochim. Biophys. Acta. 49 (1961) 335-49.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   2
  AUTHORS   Nason, A.
  TITLE     Nitrate reductases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 587-607.
REFERENCE   3
  AUTHORS   Nicholas, D.J.D. and Nason, A.
  TITLE     Diphosphopyridine nucleotide-nitrate reductase from Escherichia
            coli.
  JOURNAL   J. Bacteriol. 69 (1955) 580-583.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4
  AUTHORS   Spencer, D.
  TITLE     A reduced diphosphopyridine-specific nitrate reductase from
            germinating wheat.
  JOURNAL   Aust. J. Biol. Sci. 12 (1959) 181-189.
  ORGANISM  Triticum aestivum [GN:etae]
REFERENCE   5  [PMID:8534676]
  AUTHORS   Berks BC, Ferguson SJ, Moir JW, Richardson DJ.
  TITLE     Enzymes and associated electron transport systems that catalyse the
            respiratory reduction of nitrogen oxides and oxyanions.
  JOURNAL   Biochim. Biophys. Acta. 1232 (1995) 97-173.
  ORGANISM  Paracoccus denitrificans [GN:pde], Rhodobacter capsulatus,
            Rhodobacter sphaeroides, Escherichia coli [GN:eco]
PATHWAY     PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00360  nitrate reductase (NADH)
GENES       ATH: AT1G37130(NIA2) AT1G77760(NIA1)
            OSA: 4345795
            AFM: AFUA_2G14060 AFUA_5G10420 AFUA_6G04980
            TET: TTHERM_00196130
            TBR: Tb927.6.2040
            TCR: 507019.20
            LMA: LmjF30.0610
            ECI: UTI89_C2170(yedY) UTI89_C4929
            PSP: PSPPH_3291
            REH: H16_B0776
            HAR: HEAR1188(soxC)
            RLE: pRL80077
            NWI: Nwi_2988
            ART: Arth_3951
            SEN: SACE_1163
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.1.1
            ExPASy - ENZYME nomenclature database: 1.7.1.1
            ExplorEnz - The Enzyme Database: 1.7.1.1
            ERGO genome analysis and discovery system: 1.7.1.1
            BRENDA, the Enzyme Database: 1.7.1.1
            CAS: 9013-03-0
///
ENTRY       EC 1.7.1.2                  Enzyme
NAME        nitrate reductase [NAD(P)H];
            assimilatory nitrate reductase;
            assimilatory NAD(P)H-nitrate reductase;
            NAD(P)H bispecific nitrate reductase;
            nitrate reductase (reduced nicotinamide adenine dinucleotide
            (phosphate));
            nitrate reductase NAD(P)H;
            NAD(P)H-nitrate reductase;
            nitrate reductase [NAD(P)H2];
            NAD(P)H2:nitrate oxidoreductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     nitrite:NAD(P)+ oxidoreductase
REACTION    nitrite + NAD(P)+ + H2O = nitrate + NAD(P)H + H+ [RN:R00794 R00796]
ALL_REAC    R00794 R00796
SUBSTRATE   nitrite [CPD:C00088];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     nitrate [CPD:C00244];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016];
            FMN [CPD:C00061]
COMMENT     An iron-sulfur molybdenum flavoprotein.
REFERENCE   1
  AUTHORS   Nason, A.
  TITLE     Nitrate reductases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 587-607.
REFERENCE   2  [PMID:5864033]
  AUTHORS   Paneque A, Del Campo FF, Ramirez JM, Losada M.
  TITLE     Flavin nucleotide nitrate reductase from spinach.
  JOURNAL   Biochim. Biophys. Acta. 109 (1965) 79-85.
  ORGANISM  spinach
REFERENCE   3  [PMID:11289301]
  AUTHORS   Campbell WH.
  TITLE     Structure and function of eukaryotic NAD(P)H:nitrate reductase.
  JOURNAL   Cell. Mol. Life. Sci. 58 (2001) 194-204.
  ORGANISM  Pichia pastoris
REFERENCE   4  [PMID:8534676]
  AUTHORS   Berks BC, Ferguson SJ, Moir JW, Richardson DJ.
  TITLE     Enzymes and associated electron transport systems that catalyse the
            respiratory reduction of nitrogen oxides and oxyanions.
  JOURNAL   Biochim. Biophys. Acta. 1232 (1995) 97-173.
PATHWAY     PATH: map00910  Nitrogen metabolism
STRUCTURES  PDB: 2BIH  2BII  
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.1.2
            ExPASy - ENZYME nomenclature database: 1.7.1.2
            ExplorEnz - The Enzyme Database: 1.7.1.2
            ERGO genome analysis and discovery system: 1.7.1.2
            BRENDA, the Enzyme Database: 1.7.1.2
            CAS: 9029-27-0
///
ENTRY       EC 1.7.1.3                  Enzyme
NAME        nitrate reductase (NADPH);
            assimilatory nitrate reductase;
            assimilatory reduced nicotinamide adenine dinucleotide
            phosphate-nitrate reductase;
            NADPH-nitrate reductase;
            assimilatory NADPH-nitrate reductase;
            triphosphopyridine nucleotide-nitrate reductase;
            NADPH:nitrate reductase;
            nitrate reductase (NADPH2);
            NADPH2:nitrate oxidoreductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     nitrite:NADP+ oxidoreductase
REACTION    nitrite + NADP+ + H2O = nitrate + NADPH + H+ [RN:R00796]
ALL_REAC    R00796
SUBSTRATE   nitrite [CPD:C00088];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     nitrate [CPD:C00244];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016];
            Molybdenum [CPD:C00150]
COMMENT     An iron-sulfur molybdenum flavoprotein.
REFERENCE   1
  AUTHORS   Nason, A.
  TITLE     Nitrate reductases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 587-607.
REFERENCE   2  [PMID:13061490]
  AUTHORS   NASON A, EVANS HJ.
  TITLE     Triphosphopyridine nucleotide-nitrate reductase in Neurospora.
  JOURNAL   J. Biol. Chem. 202 (1953) 655-73.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   3
  AUTHORS   Nicholas, D.J.D. and Nason, A.
  TITLE     Molybdenum and nitrate reductase. II. Molybdenum as a constituent of
            nitrate reductase.
  JOURNAL   J. Biol. Chem. 207 (1954) 353-360.
  ORGANISM  Neurospora crassa [GN:dncr], Aspergillus niger
REFERENCE   4
  AUTHORS   Taniguchi, H., Mitsui, H., Nakamura, K. and Egami, F.
  TITLE     Ann. Acad. Sci. Fenn. Ser. A II 60 (1955) 200.
REFERENCE   5  [PMID:8534676]
  AUTHORS   Berks BC, Ferguson SJ, Moir JW, Richardson DJ.
  TITLE     Enzymes and associated electron transport systems that catalyse the
            respiratory reduction of nitrogen oxides and oxyanions.
  JOURNAL   Biochim. Biophys. Acta. 1232 (1995) 97-173.
  ORGANISM  Klebsiella pneumoniae, Bacillus subtilis [GN:bsu], Synechococcus sp.
PATHWAY     PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K10534  nitrate reductase (NADPH)
GENES       AFM: AFUA_1G12830
            ANG: An08g05610(niaD)
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.1.3
            ExPASy - ENZYME nomenclature database: 1.7.1.3
            ExplorEnz - The Enzyme Database: 1.7.1.3
            ERGO genome analysis and discovery system: 1.7.1.3
            BRENDA, the Enzyme Database: 1.7.1.3
            CAS: 9029-28-1
///
ENTRY       EC 1.7.1.4                  Enzyme
NAME        nitrite reductase [NAD(P)H];
            nitrite reductase (reduced nicotinamide adenine dinucleotide
            (phosphate));
            NADH-nitrite oxidoreductase;
            NADPH-nitrite reductase;
            assimilatory nitrite reductase;
            nitrite reductase [NAD(P)H2];
            NAD(P)H2:nitrite oxidoreductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     ammonium-hydroxide:NAD(P)+ oxidoreductase
REACTION    ammonium hydroxide + 3 NAD(P)+ + H2O = nitrite + 3 NAD(P)H + 3 H+
            [RN:R00787 R00789]
ALL_REAC    R00787 R00789
SUBSTRATE   ammonium hydroxide [CPD:C01358];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     nitrite [CPD:C00088];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023];
            Siroheme [CPD:C00748]
COMMENT     An iron-sulfur heme flavoprotein containing siroheme.
REFERENCE   1  [PMID:6297458]
  AUTHORS   Cammack R, Jackson RH, Cornish-Bowden A, Cole JA.
  TITLE     Electron-spin-resonance studies of the NADH-dependent nitrite
            reductase from Escherichia coli K12.
  JOURNAL   Biochem. J. 207 (1982) 333-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Lazzarini, R.A. and Atkinson, D.E.
  TITLE     A triphosphopyridine nucleotide-specific nitrite reductase from
            Escherichia coli.
  JOURNAL   J. Biol. Chem. 236 (1961) 3330-3335.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Nicholas, D.J.D., Medina, A. and Jones, O.T.G.
  TITLE     A nitrite reductase from Neurospora crassa.
  JOURNAL   Biochim. Biophys. Acta 37 (1960) 468.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   4
  AUTHORS   Taniguchi, H., Mitsui, H., Nakamura, K. and Egami, F.
  TITLE     Ann. Acad. Sci. Fenn. Ser. A II 60 (1955) 200.
REFERENCE   5  [PMID:8798648]
  AUTHORS   Colandene JD, Garrett RH.
  TITLE     Functional dissection and site-directed mutagenesis of the
            structural gene for NAD(P)H-nitrite reductase in Neurospora crassa.
  JOURNAL   J. Biol. Chem. 271 (1996) 24096-104.
  ORGANISM  Neurospora crassa [GN:dncr]
PATHWAY     PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00361  nitrite reductase (NAD(P)H)
            KO: K00362  nitrite reductase (NAD(P)H) large subunit
            KO: K00363  nitrite reductase (NAD(P)H) small subunit
GENES       ANI: AN1007.2
            AFM: AFUA_1G12840
            AOR: AO090012000624
            UMA: UM03848.1
            EHI: 24.t00053
            ECO: b3365(nirB) b3366(nirD)
            ECJ: JW3328(nirB) JW3329(nirD)
            ECE: Z4726(nirB) Z4727(nirD)
            ECS: ECs4216 ECs4217
            ECC: c4141(nirB) c4142(nirD)
            ECI: UTI89_C3869(nirB) UTI89_C3870(nirD)
            ECP: ECP_3456 ECP_3457
            ECV: APECO1_3090(nirD) APECO1_3091(nirB)
            ECW: EcE24377A_3835(nirB) EcE24377A_3836(nirD)
            ECX: EcHS_A3561 EcHS_A3562
            STY: STY4321(nirD) STY4322(nirB)
            STT: t4030(nirD) t4031(nirB)
            SPT: SPA3340(nirB) SPA3341(nirD)
            SEC: SC3408(nirB) SC3409(nirD)
            STM: STM3474(nirB) STM3475(nirD)
            YPE: YPO0160(nirD) YPO0161(nirB)
            YPK: y3944(nirD) y3945(nirB)
            YPM: YP_0162(nirD) YP_0163(nirB)
            YPA: YPA_3308 YPA_3309
            YPN: YPN_3903 YPN_3904
            YPP: YPDSF_0087
            YPS: YPTB3740(nirB) YPTB3741(nirD)
            YPI: YpsIP31758_3956(nirB) YpsIP31758_3957(nirD)
            SFL: SF3384(nirB) SF3385(nirD)
            SFX: S4378(nirD) S4379(nirB)
            SFV: SFV_3371(nirB) SFV_3372(nirD)
            SSN: SSON_3496(nirB) SSON_3497(nirD)
            SBO: SBO_3347(nirB) SBO_3348(nirD)
            SDY: SDY_3527(nirB) SDY_3528(nirD)
            ECA: ECA2991(nasB) ECA4079(nirB) ECA4080(nirD)
            ENT: Ent638_3794
            SPE: Spro_4596
            XCC: XCC2007(nasD) XCC2008(nasE)
            XCB: XC_2176 XC_2177
            XCV: XCV2093(nasB) XCV2094(nasE)
            VVU: VV2_0369 VV2_0370 VV2_0389 VV2_0390
            VVY: VVA0926 VVA0927 VVA0947 VVA0948
            VPA: VPA0986 VPA0987 VPA1054 VPA1055
            VFI: VF0775 VF0776
            PPR: PBPRA1427 PBPRA1428 PBPRA2522 PBPRA2523
            PAE: PA1780(nirD) PA1781(nirB)
            PAU: PA14_41530(nirB) PA14_41540(nirD)
            PPU: PP_1705(nirB) PP_1706(nirD)
            PST: PSPTO_2302 PSPTO_3262(nirB) PSPTO_3263(nirD)
            PSB: Psyr_2100 Psyr_3099 Psyr_3100
            PSP: PSPPH_2071 PSPPH_3012(nirD)
            PFO: Pfl_1780 Pfl_1781
            PEN: PSEEN1418(nirB) PSEEN1419
            PCR: Pcryo_1319
            ACI: ACIAD1910(nasD)
            SDN: Sden_3715 Sden_3716
            SFR: Sfri_1509 Sfri_1510
            CPS: CPS_4946(nirD) CPS_4947(nirB)
            PAT: Patl_2533 Patl_2534
            SDE: Sde_2354 Sde_2355
            MCA: MCA0591(nirD) MCA0592(nirB)
            TCX: Tcr_1156 Tcr_1157 Tcr_1158
            AEH: Mlg_1700 Mlg_1701
            HCH: HCH_05820 HCH_05822
            CSA: Csal_1117
            ABO: ABO_0855(nirB1) ABO_1086(nirB) ABO_1087(nirD) ABO_1088
            AHA: AHA_3407 AHA_3408(nirB-1) AHA_4118(nirB-2) AHA_4119(nirD)
            VOK: COSY_0638(nirB)
            RSO: RS03164(RSp1220) RSp1221(nirD) RSp1222(nirB)
            REU: Reut_B4860 Reut_B4861 Reut_B4862
            REH: H16_B0778(nasE) H16_B0779(nasD)
            RME: Rmet_4818 Rmet_4819 Rmet_4820
            BMA: BMA3130(nirB-1) BMA3131(nirD-1) BMAA1085(nirD-2)
                 BMAA1086(nirB-2)
            BMV: BMASAVP1_0081(nirD-2) BMASAVP1_0082(nirB-2)
                 BMASAVP1_A0099(nirB-1) BMASAVP1_A0100(nirD-1)
            BML: BMA10299_0338(nirB-2) BMA10299_0339(nirD-2)
                 BMA10299_A1489(nirD-1) BMA10299_A1490(nirB-1)
            BMN: BMA10247_2918(nirD-1) BMA10247_2919(nirB-1)
                 BMA10247_A1248(nirD-2) BMA10247_A1249(nirB-2)
            BXE: Bxe_A2213 Bxe_A2214
            BUR: Bcep18194_B1345
            BCH: Bcen2424_4505 Bcen2424_4506
            BPS: BPSL0511 BPSL0512 BPSS1242 BPSS1243(nirB)
            BPM: BURPS1710b_0740(nirD-1) BURPS1710b_0741(nirB)
                 BURPS1710b_A0242(nirD) BURPS1710b_A0243(nirB)
            BPL: BURPS1106A_0572(nirD) BURPS1106A_0573(nirB)
                 BURPS1106A_A1664(nirD) BURPS1106A_A1665(nirB)
            BPD: BURPS668_0557(nirD) BURPS668_0558(nirB) BURPS668_A1753(nirD)
                 BURPS668_A1754(nirB)
            BTE: BTH_I0463 BTH_I0464(nirB-1) BTH_II1170(nirB-2)
                 BTH_II1171(nirD)
            RFR: Rfer_2557 Rfer_2558
            POL: Bpro_3276 Bpro_3278
            MPT: Mpe_A2317 Mpe_A2318
            HAR: HEAR0431(nasD) HEAR0432(nasE)
            MMS: mma_0483 mma_0484
            EBA: ebA1215(nirD) ebA1216(nirB)
            AZO: azo1175(nirB) azo1616 azo2601
            DAR: Daro_0816 Daro_0817
            TBD: Tbd_2308 Tbd_2309
            MFA: Mfla_0319
            PCA: Pcar_2879
            ADE: Adeh_1967
            MLO: mlr2862 mlr2863
            MES: Meso_1451 Meso_1452
            SME: SMb20984(nirB) SMb20985(nirD)
            ATU: Atu3901(nirD) Atu3902(nirB)
            ATC: AGR_L_1891 AGR_L_1892
            RET: RHE_CH01781(nirD) RHE_CH01782(nirB)
            RLE: RL1990(nirD) RL1991(nasD)
            BJA: blr2808
            BRA: BRADO2475(nasD)
            BBT: BBta_2822(nasD)
            RPB: RPB_1755
            RPE: RPE_1261
            NWI: Nwi_0720
            NHA: Nham_2965
            CCR: CC_0615 CC_0616
            JAN: Jann_3043 Jann_3044
            RDE: RD1_4167(nirD) RD1_4168(nirB)
            HNE: HNE_2234(nirB) HNE_2235(nirD)
            NAR: Saro_2967 Saro_2968
            SAL: Sala_1266 Sala_1267
            GBE: GbCGDNIH1_1726 GbCGDNIH1_1727
            MAG: amb0532 amb0533
            BSU: BG11094(nasB) BG11096(nasD) BG11097(nasE)
            BHA: BH0613(nasD) BH0614(nasE)
            BAN: BA2145(nirD) BA2146(nirB)
            BAR: GBAA2145(nirD) GBAA2146(nirB)
            BAA: BA_2641 BA_2642
            BAT: BAS1996 BAS1997
            BCE: BC2135 BC2136
            BCA: BCE_1547(nirA)
            BCZ: BCZK1948(nasE) BCZK1949(nirB)
            BTK: BT9727_1969(nasE) BT9727_1970(nirB)
            BTL: BALH_1907(nirB)
            BLI: BL01767(nasB) BL01769(nasD) BL01770(nasE)
            BLD: BLi00482(nasB) BLi00484(nasD) BLi00485(nasE)
            BCL: ABC1621(nasD) ABC1622(nasE) ABC1623(nasB)
            BAY: RBAM_003500 RBAM_003510
            BPU: BPUM_1810 BPUM_1811
            GKA: GK1867 GK1868
            SAU: SA2187(nasE) SA2188(nasD)
            SAV: SAV2399(nasE) SAV2400(nasD)
            SAM: MW2321(nasE) MW2322(nasD)
            SAR: SAR2488(nasE) SAR2489(nasD)
            SAS: SAS2290 SAS2291
            SAC: SACOL2397(nirD) SACOL2398(nirB)
            SAB: SAB2279c(nasE) SAB2280c(nasD)
            SAA: SAUSA300_2345(nirD) SAUSA300_2346(nirB)
            SAO: SAOUHSC_02683 SAOUHSC_02684
            SEP: SE1977 SE1978
            SER: SERP1989(nirD) SERP1990(nirB)
            SHA: SH0651(nasD) SH0652(nasE)
            CBA: CLB_1361(noxA)
            CBH: CLC_1371(noxA)
            CBF: CLI_1428(noxA)
            CHY: CHY_2596
            MTU: Rv0252(nirB) Rv0253
            MTC: MT0266(nirB)
            MBO: Mb0258(nirB) Mb0259(nirD)
            MBB: BCG_0290(nirB) BCG_0291(nirD)
            MPA: MAP3702(nirB) MAP3703(nirD)
            MAV: MAV_4903(nirD) MAV_4904(nirB)
            MSM: MSMEG_0427(nirB) MSMEG_0428
            MMC: Mmcs_3231
            NFA: nfa45600(nirD) nfa45610(nirB)
            RHA: RHA1_ro00862(nasD) RHA1_ro00863(nasE) RHA1_ro06366
                 RHA1_ro06367
            SCO: SCO2487(nirB) SCO2488(nirC)
            SMA: SAV5660(nirD) SAV5661(nirB)
            AAU: AAur_1398(nirB) AAur_1399(nirD) AAur_3264 AAur_3265
            FRA: Francci3_0794(nirB) Francci3_0795(nirD) Francci3_0862
            FAL: FRAAL1355(nirB) FRAAL1356(nirD)
            SEN: SACE_3801(nirB) SACE_3802(nirB) SACE_3803(nirD)
                 SACE_4910(nirB) SACE_4911(nirB)
            RBA: RB1902(nirB) RB5336(nasE)
            CHU: CHU_1331(nirD) CHU_1332(nirB)
            DEH: cbdb_A1059
            DGE: Dgeo_2391 Dgeo_2392
            AAE: aq_206(nirB)
STRUCTURES  PDB: 2JO6  
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.1.4
            ExPASy - ENZYME nomenclature database: 1.7.1.4
            ExplorEnz - The Enzyme Database: 1.7.1.4
            ERGO genome analysis and discovery system: 1.7.1.4
            BRENDA, the Enzyme Database: 1.7.1.4
            CAS: 9029-29-2
///
ENTRY       EC 1.7.1.5                  Enzyme
NAME        hyponitrite reductase;
            NADH2:hyponitrite oxidoreductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     hydroxylamine:NAD+ oxidoreductase
REACTION    2 hydroxylamine + 2 NAD+ = hyponitrous acid + 2 NADH + 2 H+
            [RN:R00023]
ALL_REAC    R00023
SUBSTRATE   hydroxylamine [CPD:C00192];
            NAD+ [CPD:C00003]
PRODUCT     hyponitrous acid [CPD:C01818];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COFACTOR    Metal [CPD:C00050]
COMMENT     A metalloprotein.
REFERENCE   1
  AUTHORS   Medina, A. and Nicholas, D.J.D.
  TITLE     Hyponitrite reductase in Neurospora.
  JOURNAL   Nature (Lond.) 179 (1957) 533-534.
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.1.5
            ExPASy - ENZYME nomenclature database: 1.7.1.5
            ExplorEnz - The Enzyme Database: 1.7.1.5
            ERGO genome analysis and discovery system: 1.7.1.5
            BRENDA, the Enzyme Database: 1.7.1.5
            CAS: 9029-30-5
///
ENTRY       EC 1.7.1.6                  Enzyme
NAME        azobenzene reductase;
            new coccine (NC)-reductase;
            NC-reductase;
            azo-dye reductase;
            orange II azoreductase;
            NAD(P)H:1-(4'-sulfophenylazo)-2-naphthol oxidoreductase;
            orange I azoreductase;
            azo reductase;
            azoreductase;
            nicotinamide adenine dinucleotide (phosphate) azoreductase;
            NADPH2-dependent azoreductase;
            dimethylaminobenzene reductase;
            p-dimethylaminoazobenzene azoreductase;
            dibromopropylaminophenylazobenzoic azoreductase;
            N,N-dimethyl-4-phenylazoaniline azoreductase;
            p-aminoazobenzene reductase;
            methyl red azoreductase;
            NADPH2:4-(dimethylamino)azobenzene oxidoreductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     N,N-dimethyl-1,4-phenylenediamine, aniline:NADP+ oxidoreductase
REACTION    N,N-dimethyl-1,4-phenylenediamine + aniline + NADP+ =
            4-(dimethylamino)azobenzene + NADPH + H+ [RN:R05711]
ALL_REAC    R05711
SUBSTRATE   N,N-dimethyl-1,4-phenylenediamine [CPD:C04203];
            aniline [CPD:C00292];
            NADP+ [CPD:C00006]
PRODUCT     4-(dimethylamino)azobenzene [CPD:C03764];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The reaction occurs in the reverse direction to that shown above.
            Other azo dyes, such as Methyl Red, Rocceline, Solar Orange and
            Sumifix Black B can also be reduced [2].
REFERENCE   1
  AUTHORS   Mueller, G.C. and Miller, J.A.
  TITLE     The reductive cleavage of 4-dimethylaminoazobenzene by rat liver:
            the intracellular distribution of the enzyme system and its
            requirements for triphosphopyridine nucleotide.
  JOURNAL   J. Biol. Chem. 180 (1949) 1125-1136.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:11134015]
  AUTHORS   Suzuki Y, Yoda T, Ruhul A, Sugiura W.
  TITLE     Molecular cloning and characterization of the gene coding for
            azoreductase from Bacillus sp. OY1-2 isolated from soil.
  JOURNAL   J. Biol. Chem. 276 (2001) 9059-65.
  ORGANISM  Bacillus sp.
GENES       BCY: Bcer98_1668
STRUCTURES  PDB: 1NNI  1V4B  2D5I  
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.1.6
            ExPASy - ENZYME nomenclature database: 1.7.1.6
            ExplorEnz - The Enzyme Database: 1.7.1.6
            ERGO genome analysis and discovery system: 1.7.1.6
            UM-BBD (Biocatalysis/Biodegradation Database): 1.7.1.6
            BRENDA, the Enzyme Database: 1.7.1.6
            CAS: 9029-31-6
///
ENTRY       EC 1.7.1.7                  Enzyme
NAME        GMP reductase;
            guanosine 5'-monophosphate reductase;
            NADPH:GMP oxidoreductase (deaminating);
            guanosine monophosphate reductase;
            guanylate reductase;
            NADPH:guanosine-5'-phosphate oxidoreductase (deaminating);
            guanosine 5'-phosphate reductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     inosine-5'-phosphate:NADP+ oxidoreductase (aminating)
REACTION    inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH
            + H+ [RN:R01134]
ALL_REAC    R01134
SUBSTRATE   inosine 5'-phosphate [CPD:C00130];
            NH3 [CPD:C00014];
            NADP+ [CPD:C00006]
PRODUCT     guanosine 5'-phosphate [CPD:C00144];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4149840]
  AUTHORS   Mackenzie JJ, Sorensen LB.
  TITLE     Guanosine 5'-phosphate reductase of human erythrocytes.
  JOURNAL   Biochim. Biophys. Acta. 327 (1973) 282-94.
  ORGANISM  human [GN:hsa]
REFERENCE   2
  AUTHORS   Mager, J. and Magasanik, B.
  TITLE     Guanosine 5'-phosphate reductase and its role in the interconversion
            of purine nucleotides.
  JOURNAL   J. Biol. Chem. 235 (1960) 1474-1478.
  ORGANISM  Escherichia coli [GN:eco], Aerobacter aerogenes
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K00364  GMP reductase
GENES       HSA: 2766(GMPR) 51292(GMPR2)
            PTR: 462453(GMPR)
            MMU: 105446(Gmpr2) 66355(Gmpr)
            RNO: 117533(Gmpr)
            CFA: 488231(GMPR)
            GGA: 420842(RCJMB04_19j20)
            XLA: 444486(MGC81876)
            SPU: 591487(LOC591487) 756209(LOC756209)
            CEL: F32D1.5
            TAN: TA21065
            TPV: TP01_0363
            ECO: b0104(guaC)
            ECJ: JW0101(guaC)
            ECE: Z0114(guaC)
            ECS: ECs0108
            ECC: c0124(guaC)
            ECI: UTI89_C0112(guaC)
            ECP: ECP_0105
            ECV: APECO1_1884(guaC)
            ECW: EcE24377A_0106(guaC)
            ECX: EcHS_A0109(guaC)
            STY: STY0163(guaC)
            STT: t0147(guaC)
            SPT: SPA0145(guaC)
            SEC: SC0140(guaC)
            STM: STM0141(guaC)
            YPE: YPO3428(guaC)
            YPK: y0758(guaC)
            YPM: YP_0256(guaC)
            YPN: YPN_0660
            YPS: YPTB0703(guaC)
            YPI: YpsIP31758_3373(guaC)
            SFL: SF0101(guaC)
            SFX: S0103(guaC)
            SFV: SFV_0096(guaC)
            SSN: SSON_0112(guaC)
            SBO: SBO_0092(guaC)
            SDY: SDY_0134(guaC)
            ECA: ECA3801(guaC)
            BUC: BU204(guaC)
            BAS: BUsg198(guaC)
            BAB: bbp188(guaC)
            VCH: VCA0197
            VCO: VC0395_1030 VC0395_1080(guaC)
            VVU: VV2_0712
            VVY: VVA1179
            VPA: VPA1159
            VFI: VFA0695
            PPR: PBPRB1716
            AHA: AHA_3225(guaC)
            CVI: CV_2922
            RFR: Rfer_3037
            POL: Bpro_1718
            PNA: Pnap_1472
            AAV: Aave_1911
            AJS: Ajs_3326
            VEI: Veis_1695
            HAR: HEAR2601(guaC)
            MMS: mma_2838(guaC)
            HPY: HP0854(guaC)
            HPJ: jhp0790(guaC)
            HPA: HPAG1_0838
            RPA: RPA4561
            RPB: RPB_0217
            RPD: RPD_0604
            RPE: RPE_0636
            RRU: Rru_A1958
            BSU: BG12392(guaC)
            BAN: BA5705(guaC)
            BAR: GBAA5705(guaC)
            BAA: BA_0563
            BAT: BAS5309
            BCE: BC5452
            BCA: BCE_5594(guaC)
            BCZ: BCZK5151(guaC)
            BTK: BT9727_5137(guaC)
            BTL: BALH_4963(guaC)
            BLI: BL05105(guaC)
            BLD: BLi01200(guaC)
            BCL: ABC3216(guaC)
            BAY: RBAM_029180(guaC)
            OIH: OB1310
            SAU: SA1172
            SAV: SAV1337
            SAM: MW1224
            SAR: SAR1347
            SAS: SAS1277
            SAC: SACOL1371(guaC)
            SAB: SAB1195
            SAA: SAUSA300_1235(guaC)
            SAO: SAOUHSC_01330
            SEP: SE1019
            SER: SERP0906(guaC)
            SHA: SH1570
            SSP: SSP1420
            LLA: L158186(guaC)
            LLC: LACR_1256
            LLM: llmg_1412(guaC)
            SPY: SPy_1135
            SPZ: M5005_Spy_0857(guaC)
            SPM: spyM18_1095
            SPG: SpyM3_0793
            SPS: SPs0992
            SPH: MGAS10270_Spy0971(guaC)
            SPI: MGAS10750_Spy1006(guaC)
            SPJ: MGAS2096_Spy0931(guaC)
            SPK: MGAS9429_Spy0974(guaC)
            SPF: SpyM50933
            SPA: M6_Spy0853
            SPB: M28_Spy0831(guaC)
            SPN: SP_1249
            SPR: spr1128(guaC)
            SPD: SPD_1107(guaC)
            SAG: SAG1087(guaC)
            SAN: gbs1154
            SAK: SAK_1172(guaC)
            SSU: SSU05_0815
            SSV: SSU98_0815
            LPL: lp_3271(guaC)
            LJO: LJ0441
            LAC: LBA1893
            LSA: LSA0476(guaC)
            LSL: LSL_1139(guaC)
            LDB: Ldb0292(guaC)
            LBU: LBUL_0246
            LBR: LVIS_0226
            LCA: LSEI_0911
            LGA: LGAS_0389
            PPE: PEPE_0595
            EFA: EF2429(guaC)
            OOE: OEOE_0535
            CAC: CAC3471
            MMY: MSC_0050(guaC)
            MFL: Mfl170
            ART: Arth_2644
            FRA: Francci3_1752
            NPH: NP3080A(guaB_2)
            TPE: Tpen_1064
STRUCTURES  PDB: 1YPF  2A1Y  2A7R  2BLE  2BWG  2BZN  2C6Q  
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.1.7
            ExPASy - ENZYME nomenclature database: 1.7.1.7
            ExplorEnz - The Enzyme Database: 1.7.1.7
            ERGO genome analysis and discovery system: 1.7.1.7
            BRENDA, the Enzyme Database: 1.7.1.7
            CAS: 9029-32-7
///
ENTRY       EC 1.7.1.8        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: withdrawn in the light of further information on the
            acceptor (EC 1.7.1.8 created 2002, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.1.8
            ExPASy - ENZYME nomenclature database: 1.7.1.8
            ExplorEnz - The Enzyme Database: 1.7.1.8
            ERGO genome analysis and discovery system: 1.7.1.8
            BRENDA, the Enzyme Database: 1.7.1.8
///
ENTRY       EC 1.7.1.9                  Enzyme
NAME        nitroquinoline-N-oxide reductase;
            4-nitroquinoline 1-oxide reductase;
            4NQO reductase;
            NAD(P)H2:4-nitroquinoline-N-oxide oxidoreductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4-(hydroxyamino)quinoline N-oxide:NADP+ oxidoreductase
REACTION    4-(hydroxyamino)quinoline N-oxide + 2 NAD(P)+ + H2O =
            4-nitroquinoline N-oxide + 2 NAD(P)H + 2 H+ [RN:R04228 R04229]
ALL_REAC    R04228 R04229
SUBSTRATE   4-hydroxyaminoquinoline N-oxide [CPD:C04050];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     4-nitroquinoline N-oxide [CPD:C03474];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Toriyama, N.
  TITLE     [Metabolism of quinoline derivatives. On the reducing enzyme of
            4-nitroquinoline-N-oxide].
  JOURNAL   Nichidai Igaku Zasshi 24 (1965) 423-432.
REFERENCE   2  [PMID:1370076]
  AUTHORS   Stanley JS, York JL, Benson AM.
  TITLE     Nitroreductases and glutathione transferases that act on
            4-nitroquinoline 1-oxide and their differential induction by
            butylated hydroxyanisole in mice.
  JOURNAL   Cancer. Res. 52 (1992) 58-63.
  ORGANISM  mouse [GN:mmu]
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.1.9
            ExPASy - ENZYME nomenclature database: 1.7.1.9
            ExplorEnz - The Enzyme Database: 1.7.1.9
            ERGO genome analysis and discovery system: 1.7.1.9
            BRENDA, the Enzyme Database: 1.7.1.9
            CAS: 37256-35-2
///
ENTRY       EC 1.7.1.10                 Enzyme
NAME        hydroxylamine reductase (NADH);
            hydroxylamine reductase;
            ammonium dehydrogenase;
            NADH-hydroxylamine reductase;
            N-hydroxy amine reductase;
            hydroxylamine reductase (NADH2);
            NADH2:hydroxylamine oxidoreductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     ammonium:NAD+ oxidoreductase
REACTION    NH3 + NAD+ + H2O = hydroxylamine + NADH + H+ [RN:R00143]
ALL_REAC    R00143
SUBSTRATE   NH3 [CPD:C00014];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     hydroxylamine [CPD:C00192];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts on some hydroxamates.
REFERENCE   1  [PMID:4311180]
  AUTHORS   Bernheim ML.
  TITLE     The hydroxylamine reductase of mitochondria.
  JOURNAL   Arch. Biochem. Biophys. 134 (1969) 408-13.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4298499]
  AUTHORS   Bernheim ML, Hochstein P.
  TITLE     Reduction of hydroxylamine by rat liver mitochondria.
  JOURNAL   Arch. Biochem. Biophys. 124 (1968) 436-42.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Wang, R. and Nicholas, D.J.D.
  TITLE     Some properties of nitrite and hydroxylamine reductases from Derxia
            gummosa.
  JOURNAL   Phytochemistry 25 (1986) 2463-2469.
  ORGANISM  Derxia gummosa
PATHWAY     PATH: map00910  Nitrogen metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.1.10
            ExPASy - ENZYME nomenclature database: 1.7.1.10
            ExplorEnz - The Enzyme Database: 1.7.1.10
            ERGO genome analysis and discovery system: 1.7.1.10
            BRENDA, the Enzyme Database: 1.7.1.10
            CAS: 9032-06-8
///
ENTRY       EC 1.7.1.11                 Enzyme
NAME        4-(dimethylamino)phenylazoxybenzene reductase;
            N,N-dimethyl-p-aminoazobenzene oxide reductase;
            dimethylaminoazobenzene N-oxide reductase;
            NADPH-dependent DMAB N-oxide reductase;
            NADPH:4-(dimethylamino)phenylazoxybenzene oxidoreductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     4-(dimethylamino)phenylazobenzene:NADP+ oxidoreductase
REACTION    4-(dimethylamino)phenylazobenzene + NADP+ =
            4-(dimethylamino)phenylazoxybenzene + NADPH + H+ [RN:R04303]
ALL_REAC    R04303
SUBSTRATE   4-(dimethylamino)phenylazobenzene [CPD:C03764];
            NADP+ [CPD:C00006]
PRODUCT     4-(dimethylamino)phenylazoxybenzene [CPD:C04291];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:3152268]
  AUTHORS   Lashmet Johnson PR, Ziegler DM.
  TITLE     Properties of an N,N-dimethyl-p-aminoazobenzene oxide reductase
            purified from rat liver cytosol.
  JOURNAL   J. Biochem. Toxicol. 1 (1986) 15-27.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.1.11
            ExPASy - ENZYME nomenclature database: 1.7.1.11
            ExplorEnz - The Enzyme Database: 1.7.1.11
            ERGO genome analysis and discovery system: 1.7.1.11
            BRENDA, the Enzyme Database: 1.7.1.11
            CAS: 103843-39-6
///
ENTRY       EC 1.7.1.12                 Enzyme
NAME        N-hydroxy-2-acetamidofluorene reductase;
            N-hydroxy-2-acetylaminofluorene reductase;
            NAD(P)H:N-hydroxy-2-acetamidofluorene N-oxidoreductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-acetamidofluorene:NAD(P)+ oxidoreductase
REACTION    2-acetamidofluorene + NAD(P)+ + H2O = N-hydroxy-2-acetamidofluorene
            + NAD(P)H + H+ [RN:R04046 R04047]
ALL_REAC    R04046 R04047
SUBSTRATE   2-acetamidofluorene [CPD:C02778];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     N-hydroxy-2-acetamidofluorene [CPD:C03954];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Also acts, more slowly, on N-hydroxy-4-acetamidobiphenyl.
REFERENCE   1  [PMID:5780838]
  AUTHORS   Gutmann HR, Erickson RR.
  TITLE     The conversion of the carcinogen N-hydroxy-2-fluorenylacetamide to
            o-amidophenols by rat liver in vitro. An inducible enzymatic
            reaction.
  JOURNAL   J. Biol. Chem. 244 (1969) 1729-40.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4074379]
  AUTHORS   Kitamura S, Tatsumi K.
  TITLE     Purification of N-hydroxy-2-acetylaminofluorene reductase from
            rabbit liver cytosol.
  JOURNAL   Biochem. Biophys. Res. Commun. 133 (1985) 67-74.
  ORGANISM  rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.1.12
            ExPASy - ENZYME nomenclature database: 1.7.1.12
            ExplorEnz - The Enzyme Database: 1.7.1.12
            ERGO genome analysis and discovery system: 1.7.1.12
            BRENDA, the Enzyme Database: 1.7.1.12
            CAS: 99890-08-1
///
ENTRY       EC 1.7.1.13                 Enzyme
NAME        preQ1 synthase;
            YkvM;
            QueF;
            preQ0 reductase;
            preQ0 oxidoreductase;
            7-cyano-7-deazaguanine reductase;
            7-aminomethyl-7-carbaguanine:NADP+ oxidoreductase;
            queuine synthase (incorrect as queuine is not the product);
            queuine:NADP+ oxidoreductase (incorrect as queuine is not the
            product)
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     7-aminomethyl-7-carbaguanine:NADP+ oxidoreductase
REACTION    7-aminomethyl-7-carbaguanine + 2 NADP+ = 7-cyano-7-carbaguanine + 2
            NADPH + 2 H+ [RN:R07605]
ALL_REAC    R07605
SUBSTRATE   7-aminomethyl-7-carbaguanine;
            NADP+ [CPD:C00006]
PRODUCT     7-cyano-7-carbaguanine [CPD:C15996];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The reaction occurs in the reverse direction. This enzyme catalyses
            one of the early steps in the synthesis of queosine (Q-tRNA), and is
            followed by the action of EC 2.4.2.29, queuine
            tRNA-ribosyltransferase. Queosine is found in the wobble position of
            tRNAGUN in Eukarya and Bacteria [2] and is thought to be involved in
            translational modulation. The enzyme is not a GTP cyclohydrolase, as
            was thought previously based on sequence-homology studies.
REFERENCE   1  [PMID:15767583]
  AUTHORS   Van Lanen SG, Reader JS, Swairjo MA, de Crecy-Lagard V, Lee B,
            Iwata-Reuyl D.
  TITLE     From cyclohydrolase to oxidoreductase: discovery of nitrile
            reductase activity in a common fold.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 4264-9.
  ORGANISM  Bacillus subtilis [GN:bsu], Escherichia coli [GN:eco]
REFERENCE   2  [PMID:388227]
  AUTHORS   Yokoyama S, Miyazawa T, Iitaka Y, Yamaizumi Z, Kasai H, Nishimura S.
  TITLE     Three-dimensional structure of hyper-modified nucleoside Q located
            in the wobbling position of tRNA.
  JOURNAL   Nature. 282 (1979) 107-9.
REFERENCE   3  [PMID:1257053]
  AUTHORS   Kuchino Y, Kasai H, Nihei K, Nishimura S.
  TITLE     Biosynthesis of the modified nucleoside Q in transfer RNA.
  JOURNAL   Nucleic. Acids. Res. 3 (1976) 393-8.
  ORGANISM  Escherichia coli [GN:eco], Salmonella typhimurium
REFERENCE   4  [PMID:353740]
  AUTHORS   Okada N, Noguchi S, Nishimura S, Ohgi T, Goto T, Crain PF, McCloskey
            JA.
  TITLE     Structure determination of a nucleoside Q precursor isolated from E.
            coli tRNA: 7-(aminomethyl)-7-deazaguanosine.
  JOURNAL   Nucleic. Acids. Res. 5 (1978) 2289-96.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:364423]
  AUTHORS   Noguchi S, Yamaizumi Z, Ohgi T, Goto T, Nishimura Y, Hirota Y,
            Nishimura S.
  TITLE     Isolation of Q nucleoside precursor present in tRNA of an E. coli
            mutant and its characterization as 7-(cyano)-7-deazaguanosine.
  JOURNAL   Nucleic. Acids. Res. 5 (1978) 4215-23.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:16511203]
  AUTHORS   Swairjo MA, Reddy RR, Lee B, Van Lanen SG, Brown S, de Crecy-Lagard
            V, Iwata-Reuyl D, Schimmel P.
  TITLE     Crystallization and preliminary X-ray characterization of the
            nitrile reductase QueF: a queuosine-biosynthesis enzyme.
  JOURNAL   Acta. Crystallograph. Sect. F. Struct. Biol. Cryst. Commun. 61
            (2005) 945-8.
ORTHOLOGY   KO: K06879  7-cyano-7-deazaguanine reductase
GENES       ECO: b2794(yqcD)
            ECJ: JW2765(yqcD)
            ECE: Z4111(yqcD)
            ECS: ECs3654
            ECC: c3360(yqcD)
            ECI: UTI89_C3164(yqcD)
            ECP: ECP_2776
            ECV: APECO1_3737(yqcD)
            STY: STY3107
            STT: t2876
            SPT: SPA2832(yqcD)
            SEC: SC2907(yqcD)
            STM: STM2968(yqcD)
            YPE: YPO1034
            YPK: y3147
            YPM: YP_2817
            YPA: YPA_0508
            YPN: YPN_2968
            YPS: YPTB3012
            SFL: SF2807(yqcD)
            SFX: S3002(yqcD)
            SFV: SFV_2663(yqcD)
            SSN: SSON_2951(yqcD)
            SBO: SBO_2675(yqcD)
            SDY: SDY_3011(yqcD)
            ECA: ECA1020
            PLU: plu0662
            BAS: BUsg288(yqcD)
            SGL: SG1950
            HIN: HI1291
            HIT: NTHI1832
            HDU: HD1665
            HSO: HS_0851
            PMU: PM0476
            MSU: MS1069
            XFA: XF2383
            XFT: PD1401
            XCC: XCC3785
            XCB: XC_3857
            XCV: XCV3963
            XAC: XAC3846
            XOO: XOO4185
            XOM: XOO_3954(XOO3954)
            VCH: VC0902
            VVU: VV1_0297
            VVY: VV0887
            VPA: VP0701
            VFI: VF0598
            PPR: PBPRA2982
            PAE: PA2806
            PAP: PSPA7_2351(queF)
            PPU: PP_2160
            PST: PSPTO_2112
            PSB: Psyr_1907
            PSP: PSPPH_1862
            PFL: PFL_1967
            PFO: Pfl_3853
            PEN: PSEEN3702
            PAR: Psyc_0428
            PCR: Pcryo_0462
            ACI: ACIAD2261
            SON: SO_1608
            SDN: Sden_1513
            SFR: Sfri_1248
            SHE: Shewmr4_2661
            SHM: Shewmr7_2728
            SHN: Shewana3_2835
            ILO: IL0855
            CPS: CPS_3533
            PHA: PSHAa1980(queD)
            PAT: Patl_3193
            SDE: Sde_1172
            CBU: CBU_0151
            CBD: COXBU7E912_1955(queF)
            LPN: lpg0616
            LPF: lpl0654
            LPP: lpp0670
            MCA: MCA2441
            TCX: Tcr_2191
            NOC: Noc_1696
            AEH: Mlg_0678
            HCH: HCH_04489
            CSA: Csal_1353
            ABO: ABO_0880
            BCI: BCI_0525
            NME: NMB0317
            NMA: NMA2170
            NGO: NGO1684
            CVI: CV_3750
            RSO: RSc0448(RS04454)
            REU: Reut_A0412
            RME: Rmet_0353
            BMA: BMA0180
            BXE: Bxe_A4056
            BUR: Bcep18194_A6065
            BAM: Bamb_2788
            BPS: BPSL0632
            BPM: BURPS1710b_0839(queF)
            BTE: BTH_I0548
            BPE: BP2084
            BPA: BPP1768
            BBR: BB3340
            RFR: Rfer_2370
            POL: Bpro_3710
            NEU: NE2285
            NET: Neut_2123
            NMU: Nmul_A0644
            EBA: ebA1782
            DAR: Daro_2346
            TBD: Tbd_1227
            MFA: Mfla_1400
            HPY: HP1413
            HPJ: jhp1308
            HAC: Hac_0024
            TDN: Tmden_0004
            DVU: DVU0963
            LIP: LI0089(folE)
            BBA: Bd0087
            DPS: DP0168
            ADE: Adeh_4094
            MXA: MXAN_6316
            SAT: SYN_01967
            SFU: Sfum_1983
            RPR: RP072
            RTY: RT0060
            RCO: RC0102
            RFE: RF_0057
            RBE: RBE_1294
            MLO: mll8291
            MES: Meso_0442
            SME: SMc02723
            ATU: Atu2273
            ATC: AGR_C_4128
            RET: RHE_CH03071
            RLE: RL3517
            BME: BMEI0804
            BMF: BAB1_1206
            BMS: BR1183
            BMB: BruAb1_1189
            BJA: blr4796
            RPA: RPA2875
            RPB: RPB_2779
            RPC: RPC_2482
            RPD: RPD_2817
            RPE: RPE_2606
            NWI: Nwi_1828
            NHA: Nham_1742
            CCR: CC_2654
            SIL: SPO3753
            SIT: TM1040_2044
            ZMO: ZMO0326
            NAR: Saro_2551
            SAL: Sala_3063
            ELI: ELI_01920
            GOX: GOX0637
            GBE: GbCGDNIH1_0291
            MAG: amb0779
            MGM: Mmc1_3421
            ABA: Acid345_1832
            BSU: BG13315(ykvM)
            BHA: BH2241
            BAN: BA1362
            BAR: GBAA1362
            BAT: BAS1260
            BCE: BC1344
            BCA: BCE_1461
            BCZ: BCZK1235(folE)
            BTK: BT9727_1233(folE)
            BLI: BL03549(queF)
            BLD: BLi01530(ykvM)
            BCL: ABC2126
            BPU: BPUM_1266(queF)
            OIH: OB2210
            GKA: GK0978
            SAU: SA0683
            SAV: SAV0728
            SAM: MW0690
            SAR: SAR0782
            SAS: SAS0693
            SAC: SACOL0789
            SAB: SAB0678c
            SAA: SAUSA300_0713(folE)
            SAO: SAOUHSC_00739
            SEP: SE0510
            SER: SERP0394
            SHA: SH2165
            SSP: SSP1989
            SPN: SP_1777
            SPR: spr1603
            SMU: SMU.915c
            STC: str0828
            STL: stu0828
            STE: STER_0872
            TTE: TTE1563
            FRA: Francci3_3383
            RBA: RB2642
            LIL: LA2085
            LIC: LIC11832
            LBJ: LBJ_1924
            LBL: LBL_1360
            SYW: SYNW0463
            SYC: syc2250_d
            SYF: Synpcc7942_1844
            SYD: Syncc9605_2205
            SYE: Syncc9902_0471
            SYG: sync_2329
            TEL: tll0218
            ANA: all1162
            AVA: Ava_4416
            PMM: PMM1461
            PMT: PMT1478
            PMN: PMN2A_0991
            PMI: PMT9312_1554
            TER: Tery_2098
            BTH: BT_1564
            BFR: BF1466
            BFS: BF1397
            PGI: PG1347
            CTE: CT1638
            CCH: Cag_1759
            PLT: Plut_1627
            TMA: TM0791
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.1.13
            ExPASy - ENZYME nomenclature database: 1.7.1.13
            ExplorEnz - The Enzyme Database: 1.7.1.13
            ERGO genome analysis and discovery system: 1.7.1.13
            BRENDA, the Enzyme Database: 1.7.1.13
///
ENTRY       EC 1.7.2.1                  Enzyme
NAME        nitrite reductase (NO-forming);
            cd-cytochrome nitrite reductase;
            [nitrite reductase (cytochrome)] [misleading, see comments.];
            cytochrome c-551:O2, NO2+ oxidoreductase;
            cytochrome cd;
            cytochrome cd1;
            hydroxylamine (acceptor) reductase;
            methyl viologen-nitrite reductase;
            nitrite reductase (cytochrome;
            NO-forming)
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With a cytochrome as acceptor
SYSNAME     nitric-oxide:ferricytochrome-c oxidoreductase
REACTION    nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c
            + 2 H+ [RN:R00783]
ALL_REAC    R00783 > R00784;
            (other) R00082 R00280 R00785
SUBSTRATE   nitric oxide [CPD:C00533];
            H2O [CPD:C00001];
            ferricytochrome c [CPD:C00125]
PRODUCT     nitrite [CPD:C00088];
            ferrocytochrome c [CPD:C00126];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023];
            Copper [CPD:C00070]
COMMENT     The reaction is catalysed by two types of enzymes, found in the
            perimplasm of denitrifying bacteria. One type comprises proteins
            containing multiple copper centres, the other a heme protein,
            cytochrome cd1. Acceptors include c-type cytochromes such as
            cytochrome c-550 or cytochrome c-551 from Paracoccus denitrificans
            or Pseudomonas aeruginosa, and small blue copper proteins such as
            azurin and pseudoazurin. Cytochrome cd1 also has oxidase and
            hydroxylamine reductase activities. May also catalyse the reaction
            of hydroxylamine reductase (EC 1.7.99.1) since this is a well-known
            activity of cytochrome cd1.
REFERENCE   1  [PMID:5354021]
  AUTHORS   Miyata M, Mori T.
  TITLE     Studies on denitrification. X. The &quot;denitrifying enzyme&quot;
            as a nitrite reductase and the electron donating system for
            denitrification.
  JOURNAL   J. Biochem. (Tokyo). 66 (1969) 463-71.
  ORGANISM  Pseudomonas denitrificans
REFERENCE   2  [PMID:13295215]
  AUTHORS   CHUNG CW, NAJJAR VA.
  TITLE     Cofactor requirements for enzymatic denitrification.  I.  Nitrite
            reductase.
  JOURNAL   J. Biol. Chem. 218 (1956) 617-25.
  ORGANISM  Pseudomonas stutzeri
REFERENCE   3
  AUTHORS   Walker, G.C. and Nicholas, D.J.D.
  TITLE     Nitrite reductase from Pseudomonas aeruginosa.
  JOURNAL   Biochim. Biophys. Acta 49 (1961) 350-360.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   4
  AUTHORS   Singh, J.
  TITLE     Cytochrome oxidase from Pseudomonas aeruginosa. III. Reduction of
            hydroxylamine.
  JOURNAL   Biochim. Biophys. Acta 333 (1974) 28-36.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   5
  AUTHORS   Michalski, W.P. and Nicholas, D.J.D.
  TITLE     Molecular characterization of a copper-containing nitrite reductase
            from Rhodopseudomonas sphaeriodes forma sp. Denitrificans.
  JOURNAL   Biochim. Biophys. Acta 828 (1985) 130-137.
  ORGANISM  Rhodopseudomonas sphaeriodes
REFERENCE   6  [PMID:1862344]
  AUTHORS   Godden JW, Turley S, Teller DC, Adman ET, Liu MY, Payne WJ, LeGall
            J.
  TITLE     The 2.3 angstrom X-ray structure of nitrite reductase from
            Achromobacter cycloclastes.
  JOURNAL   Science. 253 (1991) 438-42.
  ORGANISM  Achromobacter cycloclastes
REFERENCE   7  [PMID:7583671]
  AUTHORS   Williams PA, Fulop V, Leung YC, Chan C, Moir JW, Howlett G, Ferguson
            SJ, Radford SE, Hajdu J.
  TITLE     Pseudospecific docking surfaces on electron transfer proteins as
            illustrated by pseudoazurin, cytochrome c550 and cytochrome cd1
            nitrite reductase.
  JOURNAL   Nat. Struct. Biol. 2 (1995) 975-82.
REFERENCE   8  [PMID:8639023]
  AUTHORS   Hole UH, Vollack KU, Zumft WG, Eisenmann E, Siddiqui RA, Friedrich
            B, Kroneck PM.
  TITLE     Characterization of the membranous denitrification enzymes nitrite
            reductase (cytochrome cd1) and copper-containing nitrous oxide
            reductase from Thiobacillus denitrificans.
  JOURNAL   Arch. Microbiol. 165 (1996) 55-61.
  ORGANISM  Thiobacillus denitrificans [GN:tbd]
REFERENCE   9  [PMID:9409151]
  AUTHORS   Zumft WG.
  TITLE     Cell biology and molecular basis of denitrification.
  JOURNAL   Microbiol. Mol. Biol. Rev. 61 (1997) 533-616.
  ORGANISM  Pseudomonas aeruginosa, Thiobacillus denitrificans [GN:tbd],
            Pseudomonas stutzeri, Paracoccus denitrificans [GN:pde], Ralstonia
            eutropha, Alcaligenes faecalis, Azospirillum brasilense,
            Magnetospirillum magnetotacticum, Halomonas halodenitrificans,
            Pseudomonas nautica, Roseobacter denitrificans [GN:rde]
REFERENCE   10 [PMID:9667932]
  AUTHORS   Ferguson SJ.
  TITLE     Nitrogen cycle enzymology.
  JOURNAL   Curr. Opin. Chem. Biol. 2 (1998) 182-93.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   11 [PMID:9308169]
  AUTHORS   Vijgenboom E, Busch JE, Canters GW.
  TITLE     In vivo studies disprove an obligatory role of azurin in
            denitrification in Pseudomonas aeruginosa and show that azu
            expression is under control of rpoS and ANR.
  JOURNAL   Microbiology. 143 ( Pt 9) (1997) 2853-63.
  ORGANISM  Pseudomonas aeruginosa
PATHWAY     PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00368  nitrite reductase (NO-forming)
GENES       OSA: 4324803
            ECI: UTI89_C3443(sufI)
            ASU: Asuc_0978
            PAE: PA0519(nirS)
            PFL: PFL_5501(nirK)
            PEN: PSEEN5226
            SDN: Sden_3482
            SAZ: Sama_2681
            SLO: Shew_3335
            CPS: CPS_4220(nirS)
            PHA: PSHAa1477
            NOC: Noc_0089
            HCH: HCH_04416
            NME: NMB1623
            NMA: NMA1887(aniA)
            NMC: NMC1549(aniA)
            NGO: NGO1276(aniA)
            CVI: CV_2007(aniA)
            RSO: RS03038(RSp1503)
            REU: Reut_B5010 Reut_B5018
            REH: H16_B2277(nirS)
            RME: Rmet_3172
            BMA: BMAA0755 BMAA0798
            BPS: BPSS1452 BPSS1487
            BPM: BURPS1710b_A0477(aniA) BURPS1710b_A0520
            BPL: BURPS1106A_A2012(nirK)
            BPD: BURPS668_A2107(nirK)
            BTE: BTH_II0881 BTH_II0944
            PNA: Pnap_1326
            AJS: Ajs_1912
            HAR: HEAR3245
            NMU: Nmul_A1998
            EBA: ebA888(nirS)
            DAR: Daro_3323
            TBD: Tbd_0077
            TDN: Tmden_1985
            NIS: NIS_1793 NIS_1794
            SUN: SUN_0245
            BBA: Bd2608
            PLA: Plav_1009
            SME: SMa1250(nirK)
            SMD: Smed_6278
            ATU: Atu4382(nirK)
            ATC: AGR_L_970
            RET: RHE_PF00525(nirK)
            BME: BMEII0988
            BMF: BAB2_0943
            BMS: BRA0260
            BMB: BruAb2_0919
            BOV: BOV_A0236(nirK)
            OAN: Oant_1108 Oant_4379
            BJA: blr7089(nirK)
            BRA: BRADO1227(nirK)
            BBT: BBta_6826(nirK)
            RPA: RPA3306(nirK1) RPA4145(nirK2)
            RPE: RPE_4071
            NWI: Nwi_2648
            SIL: SPOA0220(nirS)
            RSQ: Rsph17025_1595
            RDE: RD1_1565(nirS) RD1_1567(nirC) RD1_1568(nirF) RD1_1573(nirN)
            MAG: amb4165
            GKA: GK0767
            STH: STH741
            FJO: Fjoh_2418
            NPH: NP1598A(nirK)
STRUCTURES  PDB: 1RZP  1RZQ  1SJM  1SNR  1ZDQ  1ZDS  1ZV2  2A3T  2AVF  2B08  
                 2BW4  2BW5  2BWD  2BWI  2DV6  2DWS  2DWT  2DY2  2FJS  2JFC  
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.2.1
            ExPASy - ENZYME nomenclature database: 1.7.2.1
            ExplorEnz - The Enzyme Database: 1.7.2.1
            ERGO genome analysis and discovery system: 1.7.2.1
            BRENDA, the Enzyme Database: 1.7.2.1
            CAS: 37256-41-0
///
ENTRY       EC 1.7.2.2                  Enzyme
NAME        nitrite reductase (cytochrome; ammonia-forming);
            cytochrome c nitrite reductase;
            multiheme nitrite reductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With a cytochrome as acceptor
SYSNAME     ammonia:ferricytochrome-c oxidoreductase
REACTION    NH3 + 2 H2O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c +
            7 H+ [RN:R05712]
ALL_REAC    R05712
SUBSTRATE   NH3 [CPD:C00014];
            H2O [CPD:C00001];
            ferricytochrome c [CPD:C00125]
PRODUCT     nitrite [CPD:C00088];
            ferrocytochrome c [CPD:C00126];
            H+ [CPD:C00080]
COMMENT     Found as a multiheme cytochrome in many bacteria. The enzyme from
            Escherichia coli contains five hemes c and requires Ca2+. It also
            reduces nitric oxide and hydroxylamine to ammonia, and sulfite to
            sulfide.
REFERENCE   1  [PMID:10440380]
  AUTHORS   Einsle O, Messerschmidt A, Stach P, Bourenkov GP, Bartunik HD, Huber
            R, Kroneck PM.
  TITLE     Structure of cytochrome c nitrite reductase.
  JOURNAL   Nature. 400 (1999) 476-80.
  ORGANISM  Sulfurospirillum deleyianum
PATHWAY     PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K03385  formate-dependent nitrite reductase, periplasmic
                        cytochrome c552 subunit
            KO: K05904  
GENES       ECO: b4070(nrfA)
            ECJ: JW4031(nrfA)
            ECE: Z5669(nrfA)
            ECS: ECs5052
            ECC: c5066(nrfA)
            ECI: UTI89_C4660(nrfA)
            ECP: ECP_4303
            ECV: APECO1_2385(nrfA)
            ECW: EcE24377A_4626(nrfA) EcE24377A_4627(nrfB)
                 EcE24377A_4628(nrfC)
            ECX: EcHS_A4315 EcHS_A4316 EcHS_A4317
            STY: STY4475(nrfA)
            STT: t4183(nrfA)
            SPT: SPA4094(nrfA)
            SEC: SC4156(nrfA)
            STM: STM4277(nrfA)
            SFL: SF4130(nrfA)
            SFX: S3597(nrfA)
            SFV: SFV_4141(nrfA)
            SSN: SSON_4251(nrfA)
            SBO: SBO_4101(nrfA)
            ECA: ECA1875(nrfA)
            HIN: HI1069(nrfA)
            HIT: NTHI1230(nrfA)
            HIP: CGSHiEE_06735(nrfA)
            HIQ: CGSHiGG_08980(nrfA)
            HDU: HD0344(nrfA)
            PMU: PM0023(nrfA)
            MSU: MS1819(nrfA)
            APL: APL_0100(nrfA)
            ASU: Asuc_0704
            VVU: VV1_3035
            VVY: VV1250
            VPA: VP1929
            VFI: VF1554
            PPR: PBPRA1258
            SON: SO_3980
            SFR: Sfri_0622
            SAZ: Sama_0648
            SBL: Sbal_0794
            SBM: Shew185_3711
            SLO: Shew_0505 Shew_0844
            SPC: Sputcn32_0685 Sputcn32_3604
            SSE: Ssed_0688 Ssed_0931 Ssed_3653 Ssed_3744
            SPL: Spea_0831 Spea_1228 Spea_2812
            SHE: Shewmr4_0659
            SHM: Shewmr7_3363
            SHN: Shewana3_0658
            SHW: Sputw3181_3486 Sputw3181_3743
            HHA: Hhal_1374
            AHA: AHA_2464(nrfA)
            HHE: HH0217
            WSU: WS0969(nrfA)
            CJE: Cj1357c
            CJR: CJE1546(nrfA)
            CJJ: CJJ81176_1359(nrfA)
            CJU: C8J_1275(nrfA)
            CJD: JJD26997_0341(nrfA)
            CFF: CFF8240_1244(nrfA)
            CHA: CHAB381_0129(nrfA) CHAB381_0130(nrfH)
            ABU: Abu_0347(nrfA)
            GSU: GSU3154
            GME: Gmet_0294 Gmet_0296
            GUR: Gura_0665
            PCA: Pcar_2866
            PPD: Ppro_1200 Ppro_3705
            DVU: DVU0625
            DVL: Dvul_2333
            LIP: LI1002(nrfA)
            BBA: Bd2825(nrfA)
            DPS: DP0344
            ADE: Adeh_0910 Adeh_2902
            AFW: Anae109_0955 Anae109_0964
            MXA: MXAN_2209
            SAT: SYN_02616
            SFU: Sfum_2398
            STH: STH729
            AMT: Amet_2920
            CHY: CHY_0243(nrfA) CHY_0608
            DSY: DSY2472(nrfA) DSY3065(nrfA)
            DRM: Dred_0701
            SWO: Swol_1521
            RBA: RB11165(nrfA)
            BTH: BT_1417
            BFR: BF0420
            BFS: BF0361(nrfA)
            PGI: PG1820(nrfA)
STRUCTURES  PDB: 1OAH  2E80  2E81  
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.2.2
            ExPASy - ENZYME nomenclature database: 1.7.2.2
            ExplorEnz - The Enzyme Database: 1.7.2.2
            ERGO genome analysis and discovery system: 1.7.2.2
            BRENDA, the Enzyme Database: 1.7.2.2
///
ENTRY       EC 1.7.2.3                  Enzyme
NAME        trimethylamine-N-oxide reductase (cytochrome c);
            TMAO reductase;
            TOR
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With a cytochrome as acceptor
SYSNAME     trimethylamine:cytochrome c oxidoreductase
REACTION    trimethylamine + 2 (ferricytochrome c)-subunit + H2O =
            trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+
SUBSTRATE   trimethylamine [CPD:C00565];
            (ferricytochrome c)-subunit;
            H2O [CPD:C00001]
PRODUCT     trimethylamine N-oxide [CPD:C01104];
            (ferrocytochrome c)-subunit;
            H+ [CPD:C00080]
COMMENT     The cytochrome c involved in photosynthetic bacteria is a pentaheme
            protein. Contains bis(molybdopterin guanine dinucleotide)molybdenum
            cofactor. The reductant is a membrane-bound multiheme cytochrome c.
            Also reduces dimethyl sulfoxide to dimethyl sulfide.
REFERENCE   1  [PMID:1337081]
  AUTHORS   Arata H, Shimizu M, Takamiya K.
  TITLE     Purification and properties of trimethylamine N-oxide reductase from
            aerobic photosynthetic bacterium Roseobacter denitrificans.
  JOURNAL   J. Biochem. (Tokyo). 112 (1992) 470-5.
  ORGANISM  Roseobacter denitrificans [GN:rde]
REFERENCE   2  [PMID:9165084]
  AUTHORS   Knablein J, Dobbek H, Ehlert S, Schneider F.
  TITLE     Isolation, cloning, sequence analysis and X-ray structure of
            dimethyl sulfoxide/trimethylamine N-oxide reductase from Rhodobacter
            capsulatus.
  JOURNAL   Biol. Chem. 378 (1997) 293-302.
  ORGANISM  Rhodobacter capsulatus
REFERENCE   3  [PMID:9813128]
  AUTHORS   Czjzek M, Dos Santos JP, Pommier J, Giordano G, Mejean V, Haser R.
  TITLE     Crystal structure of oxidized trimethylamine N-oxide reductase from
            Shewanella massilia at 2.5 A resolution.
  JOURNAL   J. Mol. Biol. 284 (1998) 435-47.
  ORGANISM  Shewanella massilia
REFERENCE   4  [PMID:11056172]
  AUTHORS   Gon S, Giudici-Orticoni MT, Mejean V, Iobbi-Nivol C.
  TITLE     Electron transfer and binding of the c-type cytochrome TorC to the
            trimethylamine N-oxide reductase in Escherichia coli.
  JOURNAL   J. Biol. Chem. 276 (2001) 11545-51.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K07811  trimethylamine-N-oxide reductase (cytochrome c) 1
            KO: K07812  trimethylamine-N-oxide reductase (cytochrome c) 2
GENES       ECO: b0997(torA) b1872(torZ)
            ECJ: JW0982(torA) JW1861(torZ)
            ECE: Z1415(torA) Z2925(bisZ)
            ECS: ECs1152 ECs2582
            ECC: c1133(torA) c2286(bisZ)
            ECI: UTI89_C1061(torA) UTI89_C2076(bisZ)
            ECP: ECP_0995
            ECV: APECO1_90(torA) APECO1_922(bisZ)
            ECW: EcE24377A_1114(torA) EcE24377A_2103(torZ)
                 EcE24377A_2105(torY)
            ECX: EcHS_A1108(torA) EcHS_A1967(torZ) EcHS_A1968(torY)
            STY: STY3956(torA)
            STT: t3696(torA)
            SPT: SPA3672(torA)
            SEC: SC3740(torA)
            STM: STM3822(torA)
            SFL: SF1913(bisZ)
            SFX: S2003(bisZ)
            SFV: SFV_1007(torA)
            SSN: SSON_1248(bisZ)
            SDY: SDY_1171(bisZ)
            ENT: Ent638_0173
            SPE: Spro_3233 Spro_4218
            HIN: HI0643(bisC)
            HDU: HD1394(torZ)
            HSO: HS_0806(torZ) HS_1673(torA)
            PMU: PM1793(torA)
            MSU: MS0588(bisC)
            APL: APL_0688(torZ) APL_1798(torA)
            ASU: Asuc_1914 Asuc_1916
            VCH: VC1692 VC1950
            VVU: VV1_2895
            VVY: VV1375
            VPA: VP1162
            VFI: VFA0188 VFA0299 VFA0990
            PPR: PBPRA1467 PBPRA1495 PBPRA2363(torA)
            SON: SO_1232(torA)
            SFR: Sfri_1994
            SHE: Shewmr4_1051
            SHM: Shewmr7_1116
            SHN: Shewana3_1055
            CPS: CPS_1833(torA)
            VEI: Veis_3613
            HHE: HH0950(bisC)
            WSU: WS1849
            CJE: Cj0264c
            CFF: CFF8240_0429
            CCV: CCV52592_0114 CCV52592_0392 CCV52592_2044
            CHA: CHAB381_1514
            CCO: CCC13826_0958
            ABU: Abu_1143(bisC)
            RPB: RPB_1492 RPB_3139
            RPC: RPC_0658 RPC_0661 RPC_1751 RPC_1877
            RSH: Rsph17029_3775
            RDE: RD1_3664(dmsA)
            RRU: Rru_A1287
            MTA: Moth_1389
            RHA: RHA1_ro06861
            TFU: Tfu_0340
            CCH: Cag_0954
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.2.3
            ExPASy - ENZYME nomenclature database: 1.7.2.3
            ExplorEnz - The Enzyme Database: 1.7.2.3
            ERGO genome analysis and discovery system: 1.7.2.3
            BRENDA, the Enzyme Database: 1.7.2.3
            CAS: 37256-34-1
///
ENTRY       EC 1.7.3.1                  Enzyme
NAME        nitroalkane oxidase;
            nitroethane oxidase;
            NAO;
            nitroethane:oxygen oxidoreductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With oxygen as acceptor
SYSNAME     nitroalkane:oxygen oxidoreductase
REACTION    a nitroalkane + H2O + O2 = an aldehyde or ketone + nitrite + H2O2
            [RN:R00799]
ALL_REAC    R00799
SUBSTRATE   nitroalkane [CPD:C06058];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     aldehyde [CPD:C00071];
            ketone [CPD:C00709];
            nitrite [CPD:C00088];
            H2O2 [CPD:C00027]
COMMENT     Has an absolute requirement for FAD [4]. While nitroethane may be
            the physiological substrate [2], the enzyme also acts on several
            other nitroalkanes, including 1-nitropropane, 2-nitropropane,
            1-nitrobutane, 1-nitropentane, 1-nitrohexane, nitrocyclohexane and
            some nitroalkanols [4]. Differs from EC 1.13.11.32, 2-nitropropane
            dioxygenase, in that the preferred substrates are neutral
            nitroalkanes rather than anionic nitronates [4].
REFERENCE   1  [PMID:14907722]
  AUTHORS   LITTLE HN.
  TITLE     Oxidation of nitroethane by extracts from Neurospora.
  JOURNAL   J. Biol. Chem. 193 (1951) 347-58.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2  [PMID:22538]
  AUTHORS   Kido T, Hashizume K, Soda K.
  TITLE     Purification and properties of nitroalkane oxidase from Fusarium
            oxysporum.
  JOURNAL   J. Bacteriol. 133 (1978) 53-8.
REFERENCE   3  [PMID:11867731]
  AUTHORS   Daubner SC, Gadda G, Valley MP, Fitzpatrick PF.
  TITLE     Cloning of nitroalkane oxidase from Fusarium oxysporum identifies a
            new member of the acyl-CoA dehydrogenase superfamily.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 2702-7.
REFERENCE   4  [PMID:15581574]
  AUTHORS   Fitzpatrick PF, Orville AM, Nagpal A, Valley MP.
  TITLE     Nitroalkane oxidase, a carbanion-forming flavoprotein homologous to
            acyl-CoA dehydrogenase.
  JOURNAL   Arch. Biochem. Biophys. 433 (2005) 157-65.
REFERENCE   5  [PMID:15713081]
  AUTHORS   Valley MP, Tichy SE, Fitzpatrick PF.
  TITLE     Establishing the kinetic competency of the cationic imine
            intermediate in nitroalkane oxidase.
  JOURNAL   J. Am. Chem. Soc. 127 (2005) 2062-6.
PATHWAY     PATH: map00910  Nitrogen metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.3.1
            ExPASy - ENZYME nomenclature database: 1.7.3.1
            ExplorEnz - The Enzyme Database: 1.7.3.1
            ERGO genome analysis and discovery system: 1.7.3.1
            BRENDA, the Enzyme Database: 1.7.3.1
            CAS: 9029-36-1
///
ENTRY       EC 1.7.3.2                  Enzyme
NAME        acetylindoxyl oxidase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With oxygen as acceptor
SYSNAME     N-acetylindoxyl:oxygen oxidoreductase
REACTION    N-acetylindoxyl + O2 = N-acetylisatin + (?) [RN:R03873]
ALL_REAC    R03873
SUBSTRATE   N-acetylindoxyl [CPD:C02298];
            O2 [CPD:C00007]
PRODUCT     N-acetylisatin [CPD:C02172]
REFERENCE   1  [PMID:13159343]
  AUTHORS   BEEVERS H, FRENCH RC.
  TITLE     Oxidation of N-acetylindoxyl by an enzyme from plants.
  JOURNAL   Arch. Biochem. Biophys. 50 (1954) 427-39.
  ORGANISM  Zea mays [GN:ezma]
PATHWAY     PATH: map00380  Tryptophan metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.3.2
            ExPASy - ENZYME nomenclature database: 1.7.3.2
            ExplorEnz - The Enzyme Database: 1.7.3.2
            ERGO genome analysis and discovery system: 1.7.3.2
            BRENDA, the Enzyme Database: 1.7.3.2
            CAS: 9029-37-2
///
ENTRY       EC 1.7.3.3                  Enzyme
NAME        urate oxidase;
            uric acid oxidase;
            uricase;
            uricase II
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With oxygen as acceptor
SYSNAME     urate:oxygen oxidoreductase
REACTION    urate + O2 + H2O = 5-hydroxyisourate + H2O2 [RN:R02106]
ALL_REAC    R02106;
            (other) R07981
SUBSTRATE   urate [CPD:C00366];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     5-hydroxyisourate [CPD:C11821];
            H2O2 [CPD:C00027]
COFACTOR    Copper [CPD:C00070]
COMMENT     This enzyme was previously thought to be a copper protein, but it is
            now known that the enzymes from soy bean (Glycine max), the mould
            Aspergillus flavus and Bacillus subtilis contains no copper nor any
            other transition-metal ion. The 5-hydroxyisourate formed decomposes
            spontaneously to form allantoin and CO2, although there is an
            enzyme-catalysed pathway in which EC 3.5.2.17, hydroxyisourate
            hydrolase, catalyses the first step.
REFERENCE   1  [PMID:13363909]
  AUTHORS   HUDSON PB, LONDON M.
  TITLE     Purification and properties of solubilized uricase.
  JOURNAL   Biochim. Biophys. Acta. 21 (1956) 290-8.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:13271340]
  AUTHORS   MAHLER HR, HUBSCHER G, BAUM R.
  TITLE     Studies on uricase.  I.  Preparation, purification, and properties
            of a cuproprotein.
  JOURNAL   J. Biol. Chem. 216 (1955) 625-41.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:13252004]
  AUTHORS   ROBBINS KC, BARNETT EL, GRANT NH.
  TITLE     Partial pruficiation of procine liver uricase.
  JOURNAL   J. Biol. Chem. 216 (1955) 27-35.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:9709003]
  AUTHORS   Kahn K, Tipton PA.
  TITLE     Spectroscopic characterization of intermediates in the urate oxidase
            reaction.
  JOURNAL   Biochemistry. 37 (1998) 11651-9.
  ORGANISM  Glycine max [GN:egma]
REFERENCE   5  [PMID:9360612]
  AUTHORS   Colloc'h N, el Hajji M, Bachet B, L'Hermite G, Schiltz M, Prange T,
            Castro B, Mornon JP.
  TITLE     Crystal structure of the protein drug urate oxidase-inhibitor
            complex at 2.05 A resolution.
  JOURNAL   Nat. Struct. Biol. 4 (1997) 947-52.
  ORGANISM  human [GN:hsa]
REFERENCE   6  [PMID:12680763]
  AUTHORS   Imhoff RD, Power NP, Borrok MJ, Tipton PA.
  TITLE     General base catalysis in the urate oxidase reaction: evidence for a
            novel Thr-Lys catalytic diad.
  JOURNAL   Biochemistry. 42 (2003) 4094-100.
  ORGANISM  Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00232  Caffeine metabolism
ORTHOLOGY   KO: K00365  urate oxidase
GENES       MMU: 22262(Uox)
            RNO: 114768(Uox)
            CFA: 490189(UOX)
            SSC: 397510(UOX)
            GGA: 771293(LOC771293)
            XLA: 399031(MGC68684)
            XTR: 496896(uox)
            SPU: 588974(LOC588974)
            DME: Dmel_CG7171(Uro)
            OSA: 4324793
            PIC: PICST_40781(URO1)
            SPO: SPCC1223.09
            ANI: AN9470.2
            AFM: AFUA_2G10520
            AOR: AO090011000588
            CNE: CNI02420
            DDI: DDB_0231470
            SME: SMb21284
            RLE: RL3586
            RDE: RD1_4151
            GBE: GbCGDNIH1_1242 GbCGDNIH1_1243
            SUS: Acid_0359
            BSU: BG13986(pucL)
            BCL: ABC3735 ABC3736
            MSM: MSMEG_1296
            RHA: RHA1_ro01568 RHA1_ro04509
            ART: Arth_3427
            NCA: Noca_1142
            FRA: Francci3_1910
            FAL: FRAAL4508
            KRA: Krad_2071
            SEN: SACE_6736
            RXY: Rxyl_2843
            DGE: Dgeo_2601
STRUCTURES  PDB: 1J2G  1R4S  1R4U  1R51  1R56  1VAX  1VAY  1WRR  1WS2  1WS3  
                 1XT4  1XXJ  1XY3  2FUB  2FXL  2IBA  2IC0  2ICQ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.3.3
            ExPASy - ENZYME nomenclature database: 1.7.3.3
            ExplorEnz - The Enzyme Database: 1.7.3.3
            ERGO genome analysis and discovery system: 1.7.3.3
            UM-BBD (Biocatalysis/Biodegradation Database): 1.7.3.3
            BRENDA, the Enzyme Database: 1.7.3.3
            CAS: 9002-12-4
///
ENTRY       EC 1.7.3.4                  Enzyme
NAME        hydroxylamine oxidase;
            HAO;
            hydroxylamine oxidoreductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With oxygen as acceptor
SYSNAME     hydroxylamine:oxygen oxidoreductase
REACTION    hydroxylamine + O2 = nitrite + H2O [RN:R00793]
ALL_REAC    R00793
SUBSTRATE   hydroxylamine [CPD:C00192];
            O2 [CPD:C00007]
PRODUCT     nitrite [CPD:C00088];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A hemoprotein with seven c-type hemes and one P-460-type heme per
            subunit.
REFERENCE   1  [PMID:7117545]
  AUTHORS   Hooper AB, Balny C.
  TITLE     Reaction of oxygen with hydroxylamine oxidoreductase of
            Nitrosomonas: fast kinetics.
  JOURNAL   FEBS. Lett. 144 (1982) 299-303.
  ORGANISM  Nitrosomonas sp.
REFERENCE   2  [PMID:6289867]
  AUTHORS   Lipscomb JD, Hooper AB.
  TITLE     Resolution of multiple heme centers of hydroxylamine oxidoreductase
            from Nitrosomonas. 1. Electron paramagnetic resonance spectroscopy.
  JOURNAL   Biochemistry. 21 (1982) 3965-72.
  ORGANISM  Nitrosomonas europeae [GN:neu]
REFERENCE   3  [PMID:5758552]
  AUTHORS   Rees MK.
  TITLE     Studies of the hydroxylamine metabolism of Nitrosomonas europaea. I.
            Purification of hydroxylamine oxidase.
  JOURNAL   Biochemistry. 7 (1968) 353-66.
  ORGANISM  Nitrosomonas europeae [GN:neu]
PATHWAY     PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K10535  hydroxylamine oxidase
GENES       MCA: MCA0956
            NOC: Noc_0892
            NMU: Nmul_A0805 Nmul_A1082 Nmul_A2662
            AFW: Anae109_0953
            SIL: SPOA0201
            MBU: Mbur_0467
STRUCTURES  PDB: 1FGJ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.3.4
            ExPASy - ENZYME nomenclature database: 1.7.3.4
            ExplorEnz - The Enzyme Database: 1.7.3.4
            ERGO genome analysis and discovery system: 1.7.3.4
            BRENDA, the Enzyme Database: 1.7.3.4
            CAS: 9075-43-8
///
ENTRY       EC 1.7.3.5                  Enzyme
NAME        3-aci-nitropropanoate oxidase;
            propionate-3-nitronate oxidase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With oxygen as acceptor
SYSNAME     3-aci-nitropropanoate:oxygen oxidoreductase
REACTION    3-aci-nitropropanoate + O2 + H2O = 3-oxopropanoate + nitrite + H2O2
            [RN:R01609]
ALL_REAC    R01609
SUBSTRATE   3-aci-nitropropanoate [CPD:C03071];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     3-oxopropanoate [CPD:C00222];
            nitrite [CPD:C00088];
            H2O2 [CPD:C00027]
COFACTOR    FMN [CPD:C00061]
COMMENT     A flavoprotein (FMN). The primary products of the enzymic reaction
            are probably the nitropropanoate free radical and superoxide. Also
            acts, more slowly, on 4-aci-nitrobutanoate.
REFERENCE   1  [PMID:3667582]
  AUTHORS   Porter DJ, Bright HJ.
  TITLE     Propionate-3-nitronate oxidase from Penicillium atrovenetum is a
            flavoprotein which initiates the autoxidation of its substrate by
            O2.
  JOURNAL   J. Biol. Chem. 262 (1987) 14428-34.
  ORGANISM  Penicillium atrovenetum
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.3.5
            ExPASy - ENZYME nomenclature database: 1.7.3.5
            ExplorEnz - The Enzyme Database: 1.7.3.5
            ERGO genome analysis and discovery system: 1.7.3.5
            BRENDA, the Enzyme Database: 1.7.3.5
            CAS: 111940-52-4
///
ENTRY       EC 1.7.7.1                  Enzyme
NAME        ferredoxin---nitrite reductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With an iron-sulfur protein as acceptor
SYSNAME     ammonia:ferredoxin oxidoreductase
REACTION    NH3 + 2 H2O + 6 oxidized ferredoxin = nitrite + 6 reduced ferredoxin
            + 7 H+ [RN:R00790]
ALL_REAC    R00790
SUBSTRATE   NH3 [CPD:C00014];
            H2O [CPD:C00001];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     nitrite [CPD:C00088];
            reduced ferredoxin [CPD:C00138];
            H+ [CPD:C00080]
COFACTOR    Iron [CPD:C00023];
            Siroheme [CPD:C00748];
            Iron-sulfur [CPD:C00824]
COMMENT     An iron protein. Contains siroheme and [4Fe-4S] clusters.
REFERENCE   1  [PMID:4381617]
  AUTHORS   Joy KW, Hageman RH.
  TITLE     The purification and properties of nitrite reductase from higher
            plants, and its dependence on ferredoxin.
  JOURNAL   Biochem. J. 100 (1966) 263-73.
  ORGANISM  spinach, Zea mays [GN:ezma]
REFERENCE   2  [PMID:5954064]
  AUTHORS   Ramirez JM, Del Campo FF, Paneque A, Losada M.
  TITLE     Ferredoxin-nitrite reductase from spinach.
  JOURNAL   Biochim. Biophys. Acta. 118 (1966) 58-71.
  ORGANISM  spinach
REFERENCE   3  [PMID:4390523]
  AUTHORS   Zumft WG, Paneque A, Aparicio PJ, Losada M.
  TITLE     Mechanism of nitrate reduction in Chlorella.
  JOURNAL   Biochem. Biophys. Res. Commun. 36 (1969) 980-6.
  ORGANISM  Chlorella fusca
PATHWAY     PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00366  ferredoxin-nitrite reductase
GENES       ATH: AT2G15620(NIR1)
            OSA: 4330835
            PIC: PICST_67906(ECM17.1)
            BUR: Bcep18194_A5806 Bcep18194_B1354
            HAR: HEAR2392(cysI)
            TDN: Tmden_0159 Tmden_1241
            ABU: Abu_2013(nirA) Abu_2176(cysI)
            NIS: NIS_0952 NIS_1436
            SUN: SUN_0312 SUN_1492
            AFW: Anae109_4432
            RET: RHE_CH01960(cysI)
            BJA: bll4571
            BRA: BRADO1067 BRADO3793
            BBT: BBta_4137 BBta_6980
            RPA: RPA3710(nirA)
            RPB: RPB_1754
            RPE: RPE_1260
            XAU: Xaut_2499
            RRU: Rru_A1931
            ABA: Acid345_2373
            BAN: BA1443(nirA)
            BAR: GBAA1443(nirA)
            BAA: BA_1964
            BAT: BAS1333
            BCE: BC1424
            BCZ: BCZK1307(nirA)
            BCY: Bcer98_1146
            BTK: BT9727_1306(nirA)
            CAC: CAC0094
            CPE: CPE0547
            CPF: CPF_0526
            CPR: CPR_0512
            MTU: Rv2391(nirA)
            MTC: MT2461(nirA)
            MBO: Mb2412(nirA)
            MBB: BCG_2405(nirA)
            MPA: MAP2208(nirA_2)
            MVA: Mvan_3857
            MGI: Mflv_2686
            MMC: Mmcs_3474
            MKM: Mkms_3537
            MJL: Mjls_3487
            CGL: NCgl2718(cgl2817)
            CEF: CE2644
            CJK: jk0243(cysI)
            NFA: nfa14190(cysI)
            RHA: RHA1_ro00172 RHA1_ro00330(nirA) RHA1_ro01251
            SCO: SCO6102(SCBAC1A6.26c)
            SMA: SAV2127(nirA)
            ART: Arth_3125
            NCA: Noca_2351 Noca_3793
            TFU: Tfu_1888
            FRA: Francci3_0525
            FAL: FRAAL1017
            ACE: Acel_2055
            SEN: SACE_1476(nirA)
            RXY: Rxyl_0963
            RBA: RB379(nirA)
            SYN: slr0898(nirA)
            SYW: SYNW2477(nirA)
            SYC: syc0310_d(nirA)
            SYF: Synpcc7942_1240 Synpcc7942_1851
            SYD: Syncc9605_2656
            SYE: Syncc9902_2284
            SYG: sync_2898
            SYR: SynRCC307_2482(nirA)
            SYX: SynWH7803_2492(nirA)
            CYA: CYA_0612(nirA)
            CYB: CYB_0034(nirA)
            TEL: tlr1349(nirA)
            GVI: gll1557(nirA)
            ANA: alr0607(nirA)
            AVA: Ava_2866 Ava_4539
            PMT: PMT2239(nirA)
            PMN: PMN2A_1298
            PMF: P9303_29861(nirA)
            PME: NATL1_21711(nirA)
            TER: Tery_1068
            DRA: DR_A0013
            DGE: Dgeo_1407
            TTH: TTC0313
            HMA: rrnAC2625(nirA1) rrnAC2992(nirA2)
            HWA: HQ1116A(nirA) HQ2212A(nirA)
            NPH: NP1146A(nirA_2) NP4004A(nirA_3) NP4224A(nirA_1)
            PAI: PAE2577
STRUCTURES  PDB: 1ZJ8  1ZJ9  2AKJ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.7.1
            ExPASy - ENZYME nomenclature database: 1.7.7.1
            ExplorEnz - The Enzyme Database: 1.7.7.1
            ERGO genome analysis and discovery system: 1.7.7.1
            BRENDA, the Enzyme Database: 1.7.7.1
            CAS: 37256-44-3
///
ENTRY       EC 1.7.7.2                  Enzyme
NAME        ferredoxin---nitrate reductase;
            assimilatory nitrate reductase;
            nitrate (ferredoxin) reductase;
            assimilatory ferredoxin-nitrate reductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With an iron-sulfur protein as acceptor
SYSNAME     nitrite:ferredoxin oxidoreductase
REACTION    nitrite + H2O + 2 oxidized ferredoxin = nitrate + 2 reduced
            ferredoxin + 2 H+ [RN:R00791]
ALL_REAC    R00791
SUBSTRATE   nitrite [CPD:C00088];
            H2O [CPD:C00001];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     nitrate [CPD:C00244];
            reduced ferredoxin [CPD:C00138];
            H+ [CPD:C00080]
COFACTOR    Iron [CPD:C00023];
            Sulfur [CPD:C00087];
            Molybdenum [CPD:C00150];
            Iron-sulfur [CPD:C00824]
COMMENT     A molybdenum-iron-sulfur protein.
REFERENCE   1
  AUTHORS   Mikami, B. and Ida, S.
  TITLE     Purification and properties of ferrodoxin-nitrate reductase from the
            cyanobacterium Plectonema borganum.
  JOURNAL   Biochim. Biophys. Acta 791 (1984) 294-304.
  ORGANISM  Plectonema borganum
PATHWAY     PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00367  ferredoxin-nitrate reductase
GENES       SYN: sll1454(narB)
            SYW: SYNW2464(narB)
            SYC: syc0315_d(narB)
            SYF: Synpcc7942_1235
            SYD: Syncc9605_2643
            SYE: Syncc9902_2272
            SYR: SynRCC307_2489(narB)
            SYX: SynWH7803_2481(narB)
            CYA: CYA_0619(narB)
            CYB: CYB_0040(narB)
            TEL: tlr1355(narB)
            GVI: glr1571(narB)
            ANA: alr0612(narB)
STRUCTURES  PDB: 1PFD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.7.2
            ExPASy - ENZYME nomenclature database: 1.7.7.2
            ExplorEnz - The Enzyme Database: 1.7.7.2
            ERGO genome analysis and discovery system: 1.7.7.2
            BRENDA, the Enzyme Database: 1.7.7.2
            CAS: 60382-69-6
///
ENTRY       EC 1.7.7.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With an iron-sulfur protein as acceptor
SUBSTRATE   5,10-Methylenetetrahydrofolate [CPD:C00143];
            Reduced ferredoxin [CPD:C00138]
PRODUCT     5-Methyltetrahydrofolate [CPD:C00440];
            Oxidized ferredoxin [CPD:C00139]
///
ENTRY       EC 1.7.99.1                 Enzyme
NAME        hydroxylamine reductase;
            hydroxylamine (acceptor) reductase;
            ammonia:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With other acceptors
SYSNAME     ammonia:acceptor oxidoreductase
REACTION    NH3 + H2O + acceptor = hydroxylamine + reduced acceptor [RN:R00284]
ALL_REAC    R00284 > R00143
SUBSTRATE   NH3 [CPD:C00014];
            H2O [CPD:C00001];
            acceptor [CPD:C00028]
PRODUCT     hydroxylamine [CPD:C00192];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016];
            Flavoprotein [CPD:C06411]
COMMENT     A flavoprotein. Reduced pyocyanine, methylene blue and flavins act
            as donors for the reduction of hydroxylamine. May be identical to EC
            1.7.2.1, nitrite reductase (NO-forming).
REFERENCE   1
  AUTHORS   Taniguchi, H., Mitsui, H., Nakamura, K. and Egami, F.
  TITLE     Ann. Acad. Sci. Fenn. Ser. A II 60 (1955) 200.
REFERENCE   2
  AUTHORS   Walker, G.C. and Nicholas, D.J.D.
  TITLE     Hydroxylamine reductase from Pseudomonas aeruginosa.
  JOURNAL   Biochim. Biophys. Acta 49 (1961) 361-368.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   3  [PMID:11709555]
  AUTHORS   Richter CD, Allen JW, Higham CW, Koppenhofer A, Zajicek RS, Watmough
            NJ, Ferguson SJ.
  TITLE     Cytochrome cd1, reductive activation and kinetic analysis of a
            multifunctional respiratory enzyme.
  JOURNAL   J. Biol. Chem. 277 (2002) 3093-100.
  ORGANISM  Paracoccus pantotrophus
PATHWAY     PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K05601  hydroxylamine reductase
GENES       VFI: VFA0863
            PAE: PA0519(nirS)
            CPS: CPS_4220(nirS)
            MAQ: Maqu_3125 Maqu_3132
            HCH: HCH_04416
            REU: Reut_B5010
            REH: H16_B2277(nirS)
            RME: Rmet_3172
            EBA: ebA888(nirS)
            DAR: Daro_3323
            TBD: Tbd_0077
            SIL: SPOA0220(nirS)
            RDE: RD1_1565(nirS)
            PDE: Pden_2487
            MAG: amb4165
            MGM: Mmc1_1816
            BAN: BA3497
            BAR: GBAA3497
            BAA: BA_3996
            BAT: BAS3243
            BCE: BC3439
            BCZ: BCZK3153(hcp)
            BTK: BT9727_3216(hcp)
            RCA: Rcas_3430
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.99.1
            ExPASy - ENZYME nomenclature database: 1.7.99.1
            ExplorEnz - The Enzyme Database: 1.7.99.1
            ERGO genome analysis and discovery system: 1.7.99.1
            BRENDA, the Enzyme Database: 1.7.99.1
            CAS: 37256-42-1
///
ENTRY       EC 1.7.99.2       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With other acceptors
COMMENT     Deleted entry: nitric-oxide reductase. Reaction may have been due to
            the combined action of EC 1.7.99.6 nitrous-oxide reductase and EC
            1.7.99.7 nitric-oxide reductase (EC 1.7.99.2 created 1961, modified
            1976, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.99.2
            ExPASy - ENZYME nomenclature database: 1.7.99.2
            ExplorEnz - The Enzyme Database: 1.7.99.2
            ERGO genome analysis and discovery system: 1.7.99.2
            BRENDA, the Enzyme Database: 1.7.99.2
///
ENTRY       EC 1.7.99.3       Obsolete  Enzyme
NAME        Transferred to 1.7.2.1
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With other acceptors
COMMENT     Transferred entry: now included with EC 1.7.2.1, nitrite reductase
            (NO-forming) (EC 1.7.99.3 created 1961 as EC 1.6.6.5, transferred
            1964 to EC 1.7.99.3, modified 1976, deleted 2002)
STRUCTURES  PDB: 1AQ8  1AS6  1AS7  1AS8  1ET5  1ET7  1ET8  1GS6  1GS7  1GS8  
                 1HAU  1HAW  1J9Q  1J9R  1J9S  1J9T  1KCB  1L9O  1L9P  1L9Q  
                 1L9R  1L9S  1L9T  1MZY  1MZZ  1N70  1NDR  1NDS  1NDT  1NIA  
                 1NIB  1NIC  1NID  1NIE  1NIF  1NPJ  1NPN  1NTD  1WAE  2AFN  
                 2NRD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.99.3
            ExPASy - ENZYME nomenclature database: 1.7.99.3
            ExplorEnz - The Enzyme Database: 1.7.99.3
            ERGO genome analysis and discovery system: 1.7.99.3
            BRENDA, the Enzyme Database: 1.7.99.3
///
ENTRY       EC 1.7.99.4                 Enzyme
NAME        nitrate reductase;
            respiratory nitrate reductase;
            nitrate reductase (acceptor);
            nitrite:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With other acceptors
SYSNAME     nitrite:acceptor oxidoreductase
REACTION    nitrite + acceptor = nitrate + reduced acceptor [RN:R00798]
ALL_REAC    R00798;
            (other) R01106 R02165
SUBSTRATE   nitrite [CPD:C00088];
            acceptor [CPD:C00028]
PRODUCT     nitrate [CPD:C00244];
            reduced acceptor [CPD:C00030]
COFACTOR    Iron [CPD:C00023];
            Molybdenum [CPD:C00150];
            Cytochrome [CPD:C01679]
COMMENT     The Pseudomonas enzyme is a cytochrome, but the enzyme from
            Micrococcus halodenitrificans is an iron protein containing
            molybdenum. Reduced benzyl viologen and other dyes bring about the
            reduction of nitrate.
REFERENCE   1
  AUTHORS   Nason, A.
  TITLE     Nitrate reductases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 587-607.
REFERENCE   2  [PMID:4316095]
  AUTHORS   Radcliffe BC, Nicholas DJ.
  TITLE     Some properties of a nitrate reductase from Pseudomonas
            denitrificans.
  JOURNAL   Biochim. Biophys. Acta. 205 (1970) 273-87.
  ORGANISM  Pseudomonas denitrificans
REFERENCE   3  [PMID:4762405]
  AUTHORS   Rosso JP, Forget P, Pichinoty F.
  TITLE     [Bacterial nitrate reductases. Solubilization, purification and
            properties of the enzyme A of Micrococcus halodenitrificans
            (author's transl)]
  JOURNAL   Biochim. Biophys. Acta. 321 (1973) 443-55.
  ORGANISM  Micrococcus halodenitrificans
PATHWAY     PATH: map00910  Nitrogen metabolism
            PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K00369  nitrate reductase
            KO: K00370  nitrate reductase 1, alpha subunit
            KO: K00371  nitrate reductase 1, beta subunit
            KO: K00372  nitrate reductase catalytic subunit
            KO: K00373  nitrate reductase 1, delta subunit
            KO: K00374  nitrate reductase 1, gamma subunit
            KO: K02567  periplasmic nitrate reductase NapA
            KO: K08345  nitrate reductase 2, alpha subunit
            KO: K08346  nitrate reductase 2, beta subunit
            KO: K08347  nitrate reductase 2, gamma subunit
            KO: K08361  nitrate reductase 2, delta subunit
GENES       AFM: AFUA_3G15190
            ECO: b1224(narG) b1225(narH) b1226(narJ) b1227(narI) b1465(narV)
                 b1466(narW) b1467(narY) b1468(narZ) b2206(napA)
            ECJ: JW1215(narG) JW1216(narH) JW1217(narJ) JW1218(narI)
                 JW1460(narV) JW1461(narW) JW1462(narY) JW1463(narZ)
                 JW2194(napA)
            ECE: Z2001(narG) Z2002(narH) Z2003(narJ) Z2004(narI) Z2244(narZ)
                 Z2245(narY) Z2246(narW) Z2247(narV) Z3463(napA)
            ECS: ECs1729 ECs1730 ECs1731 ECs1732 ECs2068 ECs2069 ECs2070
                 ECs2071 ECs3095
            ECC: c1685(narG) c1686(narH) c1687(narJ) c1688(narI) c1897(narV)
                 c1898(narW) c1899(narY) c1900(narZ) c2745(napA)
            ECI: UTI89_C1421(narG) UTI89_C1422(narH) UTI89_C1423(narJ)
                 UTI89_C1424(narI) UTI89_C1683(narV) UTI89_C1684(narW)
                 UTI89_C1685(narY) UTI89_C1686(narZ) UTI89_C2480(napC)
                 UTI89_C2481(napB) UTI89_C2482(napH) UTI89_C2483(napG)
                 UTI89_C2484(napA) UTI89_C2485(napD)
            ECP: ECP_1274 ECP_1275 ECP_1276 ECP_1277 ECP_1467 ECP_1468
                 ECP_1469 ECP_1470 ECP_2247
            ECV: APECO1_341(narG) APECO1_342(narH) APECO1_343(narJ)
                 APECO1_344(narI) APECO1_4353(napA) APECO1_602(narV)
                 APECO1_603(narW) APECO1_604(narY) APECO1_605(narZ)
            ECW: EcE24377A_1375(narG) EcE24377A_1376(narH)
                 EcE24377A_1378(narI1) EcE24377A_1646(narI2)
                 EcE24377A_1648(narY) EcE24377A_1649(narZ) EcE24377A_2505(napA)
            ECX: EcHS_A1334 EcHS_A1335 EcHS_A1337 EcHS_A1549 EcHS_A1551
                 EcHS_A1552 EcHS_A2344
            STY: STY1288(narG) STY1289(narH) STY1290(narJ) STY1291(narI)
                 STY1485(narV) STY1486(narW) STY1487(narY) STY1488(narZ)
                 STY2485(napA)
            STT: t0605(napA) t1488(narZ) t1489(narY) t1670(narI) t1671(narJ)
                 t1672(narH) t1673(narG)
            SPT: SPA0605(napA) SPA1109(narG) SPA1110(narH) SPA1111(narJ)
                 SPA1112(narI) SPA1288(narV) SPA1290(narY) SPA1291(narZ)
            SEC: SC1577(narY) SC1578(narV) SC1755(narI) SC1756(narJ)
                 SC1757(narH) SC1758(narG) SC2264(napA)
            STM: STM1577(narZ) STM1578(narY) STM1579(narW) STM1580(narV)
                 STM1761(narI) STM1762(narJ) STM1763(narH) STM1764(narG)
                 STM2259(napA)
            YPE: YPO3038(napA)
            YPM: YP_2661(napA)
            YPA: YPA_2229
            YPN: YPN_1347
            YPS: YPTB2760(napA)
            YPI: YpsIP31758_1273(napA)
            SFL: SF1227(narG) SF1228(narH) SF1229(narJ) SF1230(narI)
                 SF2290(napA)
            SFX: S1311(narG) S1312(narH) S1313(narJ) S1314(narI) S2420(napA)
            SFV: SFV_1240(narG) SFV_1241(narH) SFV_1242(narJ) SFV_1243(narI)
                 SFV_1757(narZ) SFV_2282(napA)
            SSN: SSON_1657(narZ) SSON_1658(narY) SSON_1659(narW)
                 SSON_1660(narV) SSON_1949(narI) SSON_1950(narJ)
                 SSON_1951(narH) SSON_1952(narG) SSON_2264(napA)
            SBO: SBO_1839(narI) SBO_1840(narJ) SBO_1841(narH) SBO_1842(narG)
                 SBO_2101(napA)
            SDY: SDY_0872(napA) SDY_1279(narG) SDY_1280(narH) SDY_1281(narJ)
                 SDY_1282(narI) SDY_1651(narY) SDY_1652(narW) SDY_1653(narV)
            ECA: ECA1896(napA) ECA2031(narG) ECA2032(narH) ECA2033(narJ)
                 ECA2034(narI) ECA2990(nasA)
            SPE: Spro_2880
            HIN: HI0344(napA)
            HIT: NTHI0463(napA)
            HDU: HD0074(napA)
            HSO: HS_1508(napA)
            PMU: PM1594(napA)
            MSU: MS2281(bisC)
            APL: APL_1429(napA)
            XCC: XCC2009
            XCB: XC_2175
            XCV: XCV2095
            VCH: VCA0678
            VCO: VC0395_0617(napA)
            VVU: VV2_0398 VV2_0721
            VVY: VVA0958 VVA1192
            VPA: VPA1065 VPA1199
            VFI: VF1905
            PPR: PBPRA0853 PBPRA2030 PBPRA2525
            PAE: PA1174(napA) PA1779 PA3872(narI) PA3873(narJ) PA3874(narH)
                 PA3875(narG)
            PAU: PA14_13780(narG) PA14_13800(narH) PA14_13810(narJ)
                 PA14_13830(narI) PA14_49250(napA)
            PAP: PSPA7_1234 PSPA7_1235(narH) PSPA7_1237(narI) PSPA7_4205(napA)
            PST: PSPTO_2301(nasA)
            PSB: Psyr_2099
            PSP: PSPPH_2070 PSPPH_3893
            PFO: Pfl_1779
            PEN: PSEEN1417(narB)
            PAR: Psyc_0605(narG) Psyc_0606(narH) Psyc_0607(narJ)
                 Psyc_0608(narI)
            PRW: PsycPRwf_0669
            ACI: ACIAD1908(nasA)
            SON: SO_0848(napA)
            SDN: Sden_1497 Sden_3718
            SFR: Sfri_0553 Sfri_2553
            SSE: Ssed_1957
            SHE: Shewmr4_0704 Shewmr4_1842 Shewmr4_2226 Shewmr4_2227
                 Shewmr4_2228 Shewmr4_2229
            SHM: Shewmr7_2135 Shewmr7_2302 Shewmr7_2303 Shewmr7_2304
                 Shewmr7_2305 Shewmr7_3318
            SHN: Shewana3_1900 Shewana3_3430
            CPS: CPS_1056(napB) CPS_1057(napA) CPS_4945(nasA)
            SDE: Sde_0084 Sde_0764
            MAQ: Maqu_3085
            MCA: MCA0590(nasA)
            TCX: Tcr_1159
            AEH: Mlg_1000 Mlg_1001 Mlg_1002 Mlg_1003
            HCH: HCH_03364(napA) HCH_04008(narI) HCH_04009(narJ)
                 HCH_04010(narH) HCH_04011(narG) HCH_05823
            CSA: Csal_1119 Csal_1330 Csal_1331 Csal_1332 Csal_1333
            ABO: ABO_0543(narI) ABO_0544(narJ) ABO_0545(narH) ABO_0546(narG)
                 ABO_1089(narB)
            AHA: AHA_1586(napA) AHA_3414
            VOK: COSY_0646(narI) COSY_0647(narJ) COSY_0648(narH)
                 COSY_0649(narG)
            CVI: CV_2229(napA) CV_2540(narI) CV_2541(narJ) CV_2542(narH)
                 CV_2543(narG)
            RSO: RSp0974(narG) RSp0975(narH) RSp0976(narJ) RSp0977(narI)
                 RSp1219(nasA)
            REU: Reut_B4763 Reut_B4863 Reut_B5002 Reut_B5003 Reut_B5004
                 Reut_B5005
            REH: H16_B2265(narG2) H16_B2266(narH2) H16_B2267(narJ2)
                 H16_B2268(narI2)
            RME: Rmet_2074 Rmet_2075 Rmet_2077 Rmet_4063 Rmet_4821
            BMA: BMA1731(narG) BMA1732(narH) BMA1733(narJ) BMA1734(narI)
                 BMA3132 BMAA1084
            BMV: BMASAVP1_A2241(narG) BMASAVP1_A2242(narH)
                 BMASAVP1_A2243(narJ) BMASAVP1_A2244(narI)
            BML: BMA10299_A3074(narI) BMA10299_A3075(narJ)
                 BMA10299_A3076(narH) BMA10299_A3077(narG)
            BMN: BMA10247_1514(narG) BMA10247_1515(narH) BMA10247_1516(narJ)
                 BMA10247_1517(narI)
            BXE: Bxe_A2212 Bxe_C0367(napA)
            BUR: Bcep18194_B2099
            BPS: BPSL0510 BPSL2309(narG) BPSL2310(narH) BPSL2311 BPSL2312
                 BPSS1156(narI) BPSS1157(narJ) BPSS1158(narH) BPSS1159(narG)
                 BPSS1241
            BPM: BURPS1710b_0739(narA) BURPS1710b_2757 BURPS1710b_2758(narH)
                 BURPS1710b_2759(narJ) BURPS1710b_2761(narI)
                 BURPS1710b_A0119(narI) BURPS1710b_A0120(narJ)
                 BURPS1710b_A0121(narH) BURPS1710b_A0122 BURPS1710b_A0241(fdhF)
            BPL: BURPS1106A_0571(narB) BURPS1106A_2681(narG)
                 BURPS1106A_2682(narH) BURPS1106A_2684(narI)
                 BURPS1106A_A1542(narI) BURPS1106A_A1544(narH)
                 BURPS1106A_A1545(narG)
            BPD: BURPS668_0556(narB) BURPS668_2625(narG) BURPS668_2626(narH)
                 BURPS668_2628(narI) BURPS668_A1627(narI) BURPS668_A1629(narH)
                 BURPS668_A1630(narG)
            BTE: BTH_I0462 BTH_I1851(narI-1) BTH_I1852 BTH_I1853(narH-1)
                 BTH_I1854 BTH_II1172 BTH_II1249 BTH_II1250(narH-2) BTH_II1251
                 BTH_II1252(narI-2)
            BPA: BPP2702(napA)
            BBR: BB2800(napA)
            RFR: Rfer_2559 Rfer_2792 Rfer_2793 Rfer_2794 Rfer_2795
            POL: Bpro_3279 Bpro_4592 Bpro_4593 Bpro_4594 Bpro_4595
            AAV: Aave_0662
            AJS: Ajs_0437
            MPT: Mpe_A1705 Mpe_A1706 Mpe_A1707 Mpe_A1708 Mpe_A2319
            HAR: HEAR1660(narJ) HEAR1661(narH) HEAR3342
            MMS: mma_0485
            EBA: c1A65(ebdA) ebA1211(narA) ebA6282(narI) ebA6283(narJ)
                 ebA6285(narH) ebA6286(narG)
            AZO: azo0671(napA1) azo0947(nasA) azo3942(napA2)
            DAR: Daro_0814 Daro_2583 Daro_2584 Daro_3515
            TBD: Tbd_1403 Tbd_1404 Tbd_1405 Tbd_1406 Tbd_2310
            HHE: HH0158(napA) HH0161(napB)
            WSU: WS1178(napA)
            TDN: Tmden_1514
            CJE: Cj0780(napA)
            CJR: CJE0871(napA)
            CJJ: CJJ81176_0801(napA)
            CJU: C8J_0731(napA)
            CFF: CFF8240_1161(napA)
            CCV: CCV52592_0009(napB) CCV52592_1928(napA)
            CHA: CHAB381_1716(napA)
            CCO: CCC13826_0868(napA)
            ABU: Abu_0358(napA)
            NIS: NIS_1435 NIS_1802 NIS_1803 NIS_1804(napF) NIS_1805
                 NIS_1806(napH) NIS_1807(napG) NIS_1808(napA)
            SUN: SUN_0299(napA) SUN_0300(napG) SUN_0301(napH) SUN_0302(napB)
                 SUN_0303(napF) SUN_0305(napL) SUN_0306(napD) SUN_0669 SUN_1500
            GME: Gmet_0329 Gmet_0330 Gmet_0331 Gmet_0332 Gmet_1021 Gmet_1022
            GUR: Gura_2777
            DDE: Dde_2271
            ADE: Adeh_0908 Adeh_2170 Adeh_2171 Adeh_2172 Adeh_2173
            AFW: Anae109_3596
            MLO: mlr2864
            SME: SMa1236(napA) SMb20986(narB)
            SMD: Smed_0789
            ATU: Atu3900(nasA) Atu4408(napA)
            ATC: AGR_L_1895 AGR_L_917(napA)
            RET: RHE_CH01780(narB)
            RLE: RL1592 RL1989(nasA)
            BME: BMEII0949 BMEII0950 BMEII0951 BMEII0952 BMEII0953
            BMF: BAB2_0904(narG) BAB2_0905(narH) BAB2_0906(narJ) BAB2_0907
            BMS: BRA0296(narI) BRA0297(narJ) BRA0298(narH) BRA0299(narG)
            BMB: BruAb2_0882(narG) BruAb2_0883(narH) BruAb2_0884(narJ)
                 BruAb2_0885(narI)
            BOV: BOV_A0272(narI) BOV_A0274(narH) BOV_A0275
            OAN: Oant_2579 Oant_2894
            BJA: blr2809(nasA) blr7038(napA)
            BRA: BRADO2476(nasA) BRADO5916(napA)
            BBT: BBta_1862(napA) BBta_2823(nasA)
            RPC: RPC_0952
            RPE: RPE_1258
            NWI: Nwi_0776 Nwi_0778 Nwi_0965 Nwi_2068
            NHA: Nham_0951 Nham_3289 Nham_3445 Nham_3447
            CCR: CC_0617
            RSP: RSP_4116(napA)
            JAN: Jann_3045
            RDE: RD1_2442(narG) RD1_2443(narH) RD1_2444(narJ) RD1_2445(narI)
                 RD1_4166(nasA)
            MMR: Mmar10_2703 Mmar10_2704 Mmar10_2705 Mmar10_2706
            HNE: HNE_1560(narG) HNE_1561(narH) HNE_1564(narI)
            SAL: Sala_1268
            GBE: GbCGDNIH1_1725
            ACR: Acry_0345 Acry_1582 Acry_1584
            MAG: amb0531 amb2690
            MGM: Mmc1_1591
            BSU: BG11081(narG) BG11082(narH) BG11083(narJ) BG11084(narI)
                 BG11095(nasC)
            BHA: BH0615(nasC)
            BAN: BA2125(narG) BA2126(narH) BA2127(narJ) BA2128(narI)
            BAR: GBAA2125(narG) GBAA2126(narH) GBAA2127(narJ) GBAA2128(narI)
            BAA: BA_2621 BA_2622 BA_2623 BA_2624
            BAT: BAS1977 BAS1978 BAS1979 BAS1980
            BCE: BC2118 BC2119 BC2120 BC2121
            BCZ: BCZK1932(narG) BCZK1933(narH) BCZK1934(narJ) BCZK1935(narI)
            BCY: Bcer98_3399 Bcer98_3400 Bcer98_3402
            BTK: BT9727_1954(narG) BT9727_1955(narH) BT9727_1956(narJ)
                 BT9727_1957(narI)
            BLI: BL01172(narG) BL01173(narH) BL01174(narJ) BL01175(narI)
                 BL01768(nasC)
            BLD: BLi00483(nasC) BLi02071(narI) BLi02072(narJ) BLi02073(narH)
                 BLi02074(narG)
            BCL: ABC0715(narG) ABC0716(narH) ABC0717(narJ) ABC0718(narI)
                 ABC1624(nasC)
            BAY: RBAM_003520 RBAM_034400 RBAM_034410 RBAM_034430
            GKA: GK1827 GK1828 GK1866
            SAU: SA2182(narI) SA2183 SA2184(narH) SA2185(narG)
            SAV: SAV2394(narI) SAV2395 SAV2396(narH) SAV2397(narG)
            SAM: MW2316(narI) MW2317 MW2318(narH) MW2319(narG)
            SAR: SAR2483(narI) SAR2484(narJ) SAR2485(narH) SAR2486(narG)
            SAS: SAS2285 SAS2286 SAS2287 SAS2288
            SAC: SACOL2392(narI) SACOL2393(narJ) SACOL2394(narH)
                 SACOL2395(narG)
            SAB: SAB2273c(narI) SAB2274c(narJ) SAB2275c(narH) SAB2276c(narG)
            SAA: SAUSA300_2340(narI) SAUSA300_2341(narJ) SAUSA300_2342(narH)
                 SAUSA300_2343
            SAO: SAOUHSC_02678 SAOUHSC_02679 SAOUHSC_02680 SAOUHSC_02681
            SAJ: SaurJH9_2418 SaurJH9_2420
            SAH: SaurJH1_2466 SaurJH1_2468
            SEP: SE1972 SE1973 SE1974 SE1975
            SER: SERP1984(narI) SERP1985(narJ) SERP1986(narH) SERP1987(narG)
            SHA: SH0654(narG) SH0655(narH) SH0656 SH0657(narI)
            LPL: lp_1497(narG) lp_1498(narH) lp_1499(narJ) lp_1500(narI)
            STH: STH917(napA)
            CPE: CPE1797
            CPF: CPF_2052(narA)
            CPR: CPR_1767(narA)
            AMT: Amet_4646
            CHY: CHY_0601(napA)
            DSY: DSY0187(dmsB) DSY0188(dmsC) DSY0334(narG) DSY0335(narH)
                 DSY0336(narJ) DSY0337(narI) DSY0355(dmsC) DSY0356(dmsB)
                 DSY0597(dmsA) DSY0598(dmsB) DSY0599(dmsC) DSY1241(dmsB)
                 DSY1242(dmsC) DSY1246(dmsB) DSY1248(dmsC) DSY1249(dmsC)
                 DSY1250(dmsB) DSY1251(dmsA) DSY1449(dmsB) DSY1450(dmsC)
                 DSY2330(dmsC) DSY2331(dmsB) DSY2332(dmsA) DSY3408(dmsC)
                 DSY3409(dmsB) DSY3466(dmsA) DSY3467(dmsB) DSY3468(dmsC)
                 DSY3470(dmsA) DSY3471(dmsB) DSY3472(dmsC) DSY3750(dmsC)
                 DSY3751(dmsB) DSY3752(dmsA) DSY4078 DSY4084(dmsC)
                 DSY4085(dmsC) DSY4086(dmsB) DSY4087(dmsA) DSY4088(dmsC)
                 DSY4089(dmsB) DSY4090(dmsA) DSY4818(dmsC) DSY4819(dmsB)
                 DSY4820(dmsA) DSY4821(dmsA) DSY4822(dmsC) DSY4823(dmsB)
                 DSY4824(dmsA)
            CSC: Csac_1780
            MTU: Rv1161(narG) Rv1162(narH) Rv1163(narJ) Rv1164(narI)
                 Rv1736c(narX)
            MTC: MT0207 MT1198(narG) MT1199(narH) MT1200(narJ) MT1201(narI)
                 MT1778
            MBO: Mb0203 Mb1193(narG) Mb1194(narH) Mb1195(narJ) Mb1196(narI)
                 Mb1765c(narX)
            MBB: BCG_1223(narG) BCG_1224(narH) BCG_1225(narJ) BCG_1226(narI)
                 BCG_1775c(narX)
            MPA: MAP2617c(narI) MAP2618c(narJ) MAP2619c(narH) MAP2620c(narG)
                 MAP3636
            MAV: MAV_1303 MAV_1304(narH) MAV_1306(narI)
            MSM: MSMEG_5137(narI) MSMEG_5138(narJ) MSMEG_5139(narH) MSMEG_5140
            MMC: Mmcs_1262 Mmcs_1263
            MKM: Mkms_1279
            MJL: Mjls_1288
            CGL: NCgl1139(cgl1186) NCgl1140(cgl1187) NCgl1141(cgl1188)
                 NCgl1142(cgl1189)
            CGB: cg1341(narI) cg1342(narJ) cg1343(narH) cg1344(narG)
            CEF: CE1293 CE1294 CE1295 CE1296
            CDI: DIP0497(narI) DIP0498 DIP0499(narH) DIP0500(narG)
            NFA: nfa45490(narG) nfa45500(narH) nfa45510(narJ) nfa45520(narI)
            SCO: SCO0216(narG2) SCO0217(narH2) SCO0218(narJ2) SCO0219(narI2)
                 SCO2473(SC7A8.12) SCO4947(2SCK31.07) SCO4948(2SCK31.08)
                 SCO4949(2SCK31.09) SCO6532(narI) SCO6534(narH) SCO6535(narG)
            AAU: AAur_1407
            PAC: PPA0507 PPA0508 PPA0509 PPA0510
            NCA: Noca_1347
            FAL: FRAAL5324(narB)
            ACE: Acel_0506 Acel_0507 Acel_0508 Acel_0509 Acel_0510
            SEN: SACE_3800 SACE_4067(narI) SACE_4068(narJ) SACE_4069(narH)
                 SACE_4070(narG) SACE_4912
            STP: Strop_0178 Strop_0180
            RXY: Rxyl_1205 Rxyl_1206 Rxyl_1207 Rxyl_1208
            RBA: RB378(narB)
            SYG: sync_2888
            CHU: CHU_0561(soxC) CHU_1320(napA)
            RCA: Rcas_2173
            DGE: Dgeo_2390
            AAE: aq_217(narB)
            AFU: AF0501 AF0546(narI)
            HMA: rrnAC1199(narG) rrnAC1200(narH) rrnAC2627(narB)
            HWA: HQ2211A(narB) HQ2213A(narB)
            NPH: NP1244A(narB_2) NP2044A NP2584A NP2718A NP4226A(narB_1)
            APE: APE_1288.1 APE_1294.1 APE_1297 APE_1300.1
            PAI: PAE2614(narI) PAE3610(narJ) PAE3611(narG) PAE3612(narH)
            PCL: Pcal_1906
            PAS: Pars_0498
STRUCTURES  PDB: 1OGY  1Q16  1R27  1SIW  1Y4Z  1Y5I  1Y5L  1Y5N  2NYA  
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.99.4
            ExPASy - ENZYME nomenclature database: 1.7.99.4
            ExplorEnz - The Enzyme Database: 1.7.99.4
            ERGO genome analysis and discovery system: 1.7.99.4
            BRENDA, the Enzyme Database: 1.7.99.4
            CAS: 37256-45-4
///
ENTRY       EC 1.7.99.5       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With other acceptors
COMMENT     Deleted entry: 5,10-methylenetetrahydrofolate reductase (FADH2). Now
            included with EC 1.5.1.20, methylenetetrahydrofolate reductase
            [NAD(P)H]. Based on the reference, it had been thought that this was
            a separate enzyme from EC 1.5.1.20 but the reference upon which the
            entry was based has since been disproved. (EC 1.7.99.5 created 1965
            as EC 1.1.1.68, transferred 1978 to EC 1.1.99.15, transferred 1980
            to EC 1.7.99.5, deleted 2005)
STRUCTURES  PDB: 1B5T  1V93  1ZP3  1ZP4  1ZPT  1ZRQ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.99.5
            ExPASy - ENZYME nomenclature database: 1.7.99.5
            ExplorEnz - The Enzyme Database: 1.7.99.5
            ERGO genome analysis and discovery system: 1.7.99.5
            BRENDA, the Enzyme Database: 1.7.99.5
///
ENTRY       EC 1.7.99.6                 Enzyme
NAME        nitrous-oxide reductase;
            nitrous oxide reductase;
            N2O reductase;
            nitrogen:(acceptor) oxidoreductase (N2O-forming)
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With other acceptors
SYSNAME     nitrogen:acceptor oxidoreductase (N2O-forming)
REACTION    nitrogen + H2O + acceptor = nitrous oxide + reduced acceptor
            [RN:R02804]
ALL_REAC    R02804
SUBSTRATE   nitrogen [CPD:C00697];
            H2O [CPD:C00001];
            acceptor [CPD:C00028]
PRODUCT     nitrous oxide [CPD:C00887];
            reduced acceptor [CPD:C00030]
COFACTOR    Copper [CPD:C00070]
COMMENT     A copper protein. Reduced viologens or methylene blue act as donors
            for the reduction of nitrous oxide.
REFERENCE   1  [PMID:3000778]
  AUTHORS   Coyle CL, Zumft WG, Kroneck PM, Korner H, Jakob W.
  TITLE     Nitrous oxide reductase from denitrifying Pseudomonas
            perfectomarina. Purification and properties of a novel multicopper
            enzyme.
  JOURNAL   Eur. J. Biochem. 153 (1985) 459-67.
  ORGANISM  Pseudomonas perfectomarina
PATHWAY     PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00376  nitrous-oxide reductase
GENES       PPR: PBPRB0847(nosZ)
            PAE: PA3392(nosZ)
            PAU: PA14_20200(nosZ)
            SDN: Sden_2219
            SLO: Shew_3400
            CPS: CPS_4732(nosZ)
            PIN: Ping_1428
            MAQ: Maqu_3078
            AEH: Mlg_1074
            HCH: HCH_03388
            RSO: RSp1368(nosZ)
            RME: Rmet_4917
            BMA: BMA0995(nosZ)
            BPS: BPSL1607(nosZ)
            BPM: BURPS1710b_2255(nosZ)
            BPL: BURPS1106A_2115(nosZ)
            BPD: BURPS668_2060(nosZ)
            BTE: BTH_I2325
            RFR: Rfer_3199
            AJS: Ajs_1139
            EBA: ebA6272(nosZ)
            AZO: azo3113(nosZ)
            DAR: Daro_1571
            TBD: Tbd_1389
            TDN: Tmden_1298 Tmden_1770
            NIS: NIS_1789
            SUN: SUN_2179
            ADE: Adeh_2402
            AFW: Anae109_0244
            SME: SMa1182(nosZ)
            BME: BMEII0973 BMEII0974
            BMF: BAB2_0928(nosZ)
            BMS: BRA0275(nosZ)
            BMB: BruAb2_0905(nosZ)
            BOV: BOV_A0251(nosZ)
            OAN: Oant_4346
            BJA: blr0315(nosZ)
            BBT: BBta_6008(nosZ)
            RPA: RPA2061(nosZ)
            RPB: RPB_3142
            RPC: RPC_0428
            RPE: RPE_3095
            SIL: SPOA0050(nosZ)
            RDE: RD1_1547(nosZ)
            PDE: Pden_4219
            MAG: amb3086
            DSY: DSY0261
            SRU: SRU_0308(nosZ)
            GFO: GFO_1411(nosZ)
            HMA: rrnAC0390(nosZ)
            PCL: Pcal_1928
STRUCTURES  PDB: 1FWX  2IWF  2IWK  
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.99.6
            ExPASy - ENZYME nomenclature database: 1.7.99.6
            ExplorEnz - The Enzyme Database: 1.7.99.6
            ERGO genome analysis and discovery system: 1.7.99.6
            BRENDA, the Enzyme Database: 1.7.99.6
            CAS: 55576-44-8
///
ENTRY       EC 1.7.99.7                 Enzyme
NAME        nitric-oxide reductase;
            nitrogen oxide reductase;
            nitrous-oxide:(acceptor) oxidoreductase (NO-forming)
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With other acceptors
SYSNAME     nitrous-oxide:acceptor oxidoreductase (NO-forming)
REACTION    nitrous oxide + acceptor + H2O = 2 nitric oxide + reduced acceptor
            [RN:R00294]
ALL_REAC    R00294;
            (other) R02492
SUBSTRATE   nitrous oxide [CPD:C00887];
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
PRODUCT     nitric oxide [CPD:C00533];
            reduced acceptor [CPD:C00030]
COMMENT     A heterodimer of cytochromes b and c. Phenazine methosulfate can act
            as acceptor.
REFERENCE   1  [PMID:2542222]
  AUTHORS   Heiss B, Frunzke K, Zumft WG.
  TITLE     Formation of the N-N bond from nitric oxide by a membrane-bound
            cytochrome bc complex of nitrate-respiring (denitrifying)
            Pseudomonas stutzeri.
  JOURNAL   J. Bacteriol. 171 (1989) 3288-97.
  ORGANISM  Pseudomonas stutzeri
PATHWAY     PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00377  nitric-oxide reductase
            KO: K02164  nitric-oxide reductase NorE protein
            KO: K02305  nitric-oxide reductase, cytochrome c-containing subunit
                        II
            KO: K02448  nitric-oxide reductase NorD protein
            KO: K04561  nitric-oxide reductase, cytochrome b-containing subunit
                        I
            KO: K04747  nitric-oxide reductase NorF protein
            KO: K04748  nitric-oxide reductase NorQ protein
GENES       MSU: MS0294(norB)
            PPR: PBPRB1053 PBPRB1054 PBPRB1055(norD) PBPRB1057(nirQ)
            PAE: PA0520(nirQ) PA0521 PA0523(norC) PA0524(norB) PA0525
            PAU: PA14_06810(norC) PA14_06830(norB) PA14_06840(norD)
            SDN: Sden_1968 Sden_1978 Sden_1979 Sden_1980 Sden_1981
            SFR: Sfri_3253
            SHE: Shewmr4_3089
            SHM: Shewmr7_0883
            SHN: Shewana3_0846
            ILO: IL0186
            CPS: CPS_0600(norC) CPS_0601(norB) CPS_1918 CPS_2319(nirQ)
                 CPS_2320 CPS_2324
            PHA: PSHAa2417(nor)
            MAQ: Maqu_3114
            LPN: lpg2236
            LPF: lpl2162
            LPP: lpp2189
            MCA: MCA2400 MCA2746(cbbQ)
            TCX: Tcr_0429
            NOC: Noc_1847 Noc_1848 Noc_1849 Noc_1850
            AEH: Mlg_2116 Mlg_2117 Mlg_2118 Mlg_2838
            HCH: HCH_00713 HCH_04408(norD) HCH_04410(norB) HCH_04411 HCH_04414
            NME: NMB1622
            NMA: NMA1886(nor)
            NMC: NMC1548(nor)
            NGO: NGO1275(norB)
            CVI: CV_3494(norB)
            RSO: RSp1505(norB)
            REU: Reut_B5055
            REH: H16_B2323(norB2)
            RME: Rmet_1499 Rmet_3167
            BMA: BMA0633 BMAA0799(norB) BMAA1163
            BMV: BMASAVP1_0547(norB)
            BML: BMA10299_0658(norB)
            BMN: BMA10247_A1612(norB)
            BUR: Bcep18194_B1844
            BPS: BPSL2351 BPSS0673
            BPM: BURPS1710b_2802(norB) BURPS1710b_A0474(norB)
                 BURPS1710b_A0475(norB) BURPS1710b_A0476(norB)
                 BURPS1710b_A2238(norE)
            BTE: BTH_I1813 BTH_II0945
            RFR: Rfer_1886
            MPT: Mpe_A3615
            NEU: NE1919(cbbQ) NE2003 NE2004(norB) NE2005 NE2006(norD)
            NET: Neut_0518 Neut_0519 Neut_0520 Neut_0521 Neut_0815
            NMU: Nmul_A1253 Nmul_A1254 Nmul_A1255 Nmul_A1256
            EBA: ebA179(norB) ebA182(norE) ebA183(norQ) ebA188 ebB6(norC)
            AZO: azo3088(norC) azo3095(norQ)
            DAR: Daro_3190 Daro_3191 Daro_3192 Daro_3194 Daro_3197
            TBD: Tbd_0555 Tbd_0558(norQ) Tbd_0560 Tbd_0561 Tbd_0562 Tbd_0822
                 Tbd_0823 Tbd_0824(norQ) Tbd_0869(norQ) Tbd_2622(cbbQ1)
            TDN: Tmden_1984
            ABU: Abu_1354(norB)
            NIS: NIS_1795 NIS_1796
            SUN: SUN_0243 SUN_0244
            GME: Gmet_3493
            BBA: Bd2597(norD) Bd2598(norQ) Bd2599(norB) Bd2601(norC)
            ADE: Adeh_1403 Adeh_3720
            AFW: Anae109_2758
            SFU: Sfum_2932
            SME: SMa1269(norD) SMa1272(norQ) SMa1273(norB) SMa1276(norC)
                 SMa1279(norE)
            SMD: Smed_6288
            ATU: Atu4386(norD) Atu4387(norQ) Atu4388(norB) Atu4389(norC)
                 Atu4391(norE)
            ATC: AGR_L_949(norE) AGR_L_954 AGR_L_956 AGR_L_958(norQ) AGR_L_961
            RET: RHE_PF00515(norC) RHE_PF00516(norB) RHE_PF00517(norQ)
                 RHE_PF00518(norD)
            BME: BMEII0996 BMEII0997 BMEII0998 BMEII0999 BMEII1000 BMEII1001
            BMF: BAB2_0952 BAB2_0953 BAB2_0954 BAB2_0955 BAB2_0957
            BMS: BRA0246 BRA0247(norF) BRA0248(norC) BRA0249(norB) BRA0250
                 BRA0251(norD)
            BMB: BruAb2_0928(norD) BruAb2_0929 BruAb2_0930(norB)
                 BruAb2_0931(norC) BruAb2_0932(norF) BruAb2_0933
            BOV: BOV_A0224(norC)
            OAN: Oant_4387
            BJA: blr3212(norE) blr3214(norC) blr3215(norB) blr3216(norQ)
                 blr3217(norD)
            BRA: BRADO1774(norE) BRADO1776(norC) BRADO1777(norB)
            BBT: BBta_2086(norE) BBta_2088(norC) BBta_2089(norB)
            RPA: RPA1453(norE) RPA1455(norC) RPA1456(norB) RPA1457(norQ)
                 RPA1458(norD)
            RPD: RPD_1547
            RPE: RPE_0618 RPE_0620 RPE_0621 RPE_0622 RPE_0624
            NWI: Nwi_1976
            SIL: SPOA0213 SPOA0214(norD) SPOA0215(norQ) SPOA0216(norB)
                 SPOA0217(norC)
            RSP: RSP_0321(norD) RSP_0322(norQ) RSP_0323(norB) RSP_0324(norC)
            RSH: Rsph17029_1969
            RSQ: Rsph17025_0971
            RDE: RD1_1557(norF) RD1_1558(norE) RD1_1559(norD) RD1_1560(norQ)
                 RD1_1561(norB) RD1_1562(norC)
            PDE: Pden_2484
            MAG: amb2941 amb2942 amb2943 amb2944 amb2945
            MGM: Mmc1_0117 Mmc1_0119 Mmc1_0120 Mmc1_0121
            ABA: Acid345_0364
            BCZ: BCZK0535(norQ)
            BTK: BT9727_0535(norQ)
            BTL: BALH_0562(norQ)
            BLI: BL01473
            BLD: BLi02084
            GKA: GK0758
            SAR: SAR0261
            SAB: SAB1265c
            DSY: DSY1165 DSY1166
            MPA: MAP2653c(nirQ)
            MMC: Mmcs_1569
            CDI: DIP2249
            PAC: PPA1975
            SYN: sll0450(norB)
            MMA: MM_2988
            HMA: rrnAC2272(norB)
            SSO: SSO1571(norB-1)
            PAI: PAE3603
STRUCTURES  PDB: 1EHE  1F24  1F25  1F26  1JFB  1JFC  1ULW  1XQD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.99.7
            ExPASy - ENZYME nomenclature database: 1.7.99.7
            ExplorEnz - The Enzyme Database: 1.7.99.7
            ERGO genome analysis and discovery system: 1.7.99.7
            BRENDA, the Enzyme Database: 1.7.99.7
            CAS: 37256-43-2
///
ENTRY       EC 1.7.99.8                 Enzyme
NAME        hydroxylamine oxidoreductase
CLASS       Oxidoreductases;
            Acting on other nitrogenous compounds as donors;
            With other acceptors
SYSNAME     hydroxylamine:acceptor oxidoreductase
REACTION    (1) hydroxylamine + NH3 = hydrazine + H2O [RN:R07173];
            (2) hydrazine + acceptor = N2 + reduced acceptor [RN:R07174]
ALL_REAC    R07173 R07174
SUBSTRATE   hydroxylamine [CPD:C00192];
            NH3 [CPD:C00014];
            hydrazine [CPD:C05361];
            acceptor [CPD:C00028]
PRODUCT     hydrazine [CPD:C05361];
            H2O [CPD:C00001];
            N2 [CPD:C00697];
            reduced acceptor [CPD:C00030]
COMMENT     The enzyme from anammox bacteria is inhibited by phosphate, oxygen
            and high nitrite concentrations and is also capable of reducing NO
            to N2O. Ferricyanide, phenazine methosulfate and
            methylthiazolyltetrazolium bromide can act as acceptors in this
            4-electron transfer reaction.
REFERENCE   1  [PMID:10820012]
  AUTHORS   Schalk J, de Vries S, Kuenen JG, Jetten MS.
  TITLE     Involvement of a novel hydroxylamine oxidoreductase in anaerobic
            ammonium oxidation.
  JOURNAL   Biochemistry. 39 (2000) 5405-12.
  ORGANISM  Nitrosomonas europeae [GN:neu]
REFERENCE   2  [PMID:11404106]
  AUTHORS   Jetten MS, Wagner M, Fuerst J, van Loosdrecht M, Kuenen G, Strous M.
  TITLE     Microbiology and application of the anaerobic ammonium oxidation
            ('anammox') process.
  JOURNAL   Curr. Opin. Biotechnol. 12 (2001) 283-8.
  ORGANISM  Brocadia anammoxidans, Nitrosomonas europeae [GN:neu]
DBLINKS     IUBMB Enzyme Nomenclature: 1.7.99.8
            ExPASy - ENZYME nomenclature database: 1.7.99.8
            ExplorEnz - The Enzyme Database: 1.7.99.8
            ERGO genome analysis and discovery system: 1.7.99.8
            BRENDA, the Enzyme Database: 1.7.99.8
///
ENTRY       EC 1.8.1.1        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With NAD+ or NADP+ as acceptor
COMMENT     Deleted entry: cysteamine dehydrogenase (EC 1.8.1.1 created 1961,
            deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.1.1
            ExPASy - ENZYME nomenclature database: 1.8.1.1
            ExplorEnz - The Enzyme Database: 1.8.1.1
            ERGO genome analysis and discovery system: 1.8.1.1
            BRENDA, the Enzyme Database: 1.8.1.1
///
ENTRY       EC 1.8.1.2                  Enzyme
NAME        sulfite reductase (NADPH);
            sulfite (reduced nicotinamide adenine dinucleotide phosphate)
            reductase;
            NADPH-sulfite reductase;
            NADPH-dependent sulfite reductase;
            H2S-NADP oxidoreductase;
            sulfite reductase (NADPH2)
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     hydrogen-sulfide:NADP+ oxidoreductase
REACTION    hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+
            [RN:R00858]
ALL_REAC    R00858;
            (other) R03596
SUBSTRATE   hydrogen sulfide [CPD:C00283];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     sulfite [CPD:C00094];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023];
            Heme [CPD:C00032];
            FMN [CPD:C00061]
COMMENT     An iron flavoprotein (FAD and FMN).
REFERENCE   1  [PMID:14401842]
  AUTHORS   HILZ H, KITTLER M, KNAPE G.
  TITLE     [The reduction of sulfate in yeast.]
  JOURNAL   Biochem. Z. 332 (1959) 151-66.
REFERENCE   2  [PMID:4144254]
  AUTHORS   Siegel LM, Murphy MJ, Kamin H.
  TITLE     Reduced nicotinamide adenine dinucleotide phosphate-sulfite
            reductase of enterobacteria. I. The Escherichia coli
            hemoflavoprotein: molecular parameters and prosthetic groups.
  JOURNAL   J. Biol. Chem. 248 (1973) 251-64.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4384979]
  AUTHORS   Yoshimoto A, Sato R.
  TITLE     Studies on yeast sulfite reductase. I. Purification and
            characterization.
  JOURNAL   Biochim. Biophys. Acta. 153 (1968) 555-75.
  ORGANISM  Escherichia coli [GN:eco], Saccharomyces cerevisiae [GN:sce],
            Salmonella typhimurium, Aspergillus nidulans [GN:ani], Neurospora
            crassa [GN:dncr], Desulfovibrio desulfuricans [GN:dde],
            Desulfovibrio gigas, Clostridium nigrificans
PATHWAY     PATH: map00450  Selenoamino acid metabolism
            PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K00379  sulfite reductase (NADPH)
            KO: K00380  sulfite reductase (NADPH) flavoprotein alpha-component
            KO: K00381  sulfite reductase (NADPH) hemoprotein beta-component
GENES       SPU: 581212(LOC581212)
            CME: CMR440C
            SCE: YFR030W(MET10)
            AGO: AGOS_AGR237C
            PIC: PICST_67906(ECM17.1) PICST_83457
            CAL: CaO19.4076
            CGR: CAGL0D05280g
            SPO: SPCC584.01c
            ANI: AN1752.2
            AFM: AFUA_6G08920
            AOR: AO090001000571
            CNE: CNG03990
            UMA: UM03576.1
            DDI: DDB_0215407(redA)
            ECO: b2763(cysI) b2764(cysJ)
            ECJ: JW2733(cysI) JW2734(cysJ)
            ECE: Z4073(cysI) Z4074(cysJ)
            ECS: ECs3618 ECs3619
            ECC: c3322(cysI) c3323(cysJ)
            ECI: UTI89_C3127(cysI) UTI89_C3128(cysJ)
            ECP: ECP_2737 ECP_2738
            ECV: APECO1_3768 APECO1_3769(cysI)
            ECW: EcE24377A_3065(cysI) EcE24377A_3066(cysJ)
            ECX: EcHS_A2903(cysI) EcHS_A2904(cysJ)
            STY: STY3075(cysI) STY3076(cysJ)
            STT: t2848(cysI) t2849(cysJ)
            SPT: SPA2803(cysI) SPA2804(cysJ)
            SEC: SC2878(cysI) SC2879(cysJ)
            STM: STM2947(cysI) STM2948(cysJ)
            YPE: YPO3371(cysI) YPO3372(cysJ)
            YPK: y0818(cysJ) y0819(cysI)
            YPM: YP_0314(cysJ) YP_0315(cysI)
            YPA: YPA_2869 YPA_2870
            YPN: YPN_0720 YPN_0721
            YPP: YPDSF_2987
            YPS: YPTB0759(cysJ) YPTB0760(cysI)
            YPI: YpsIP31758_3310(cysI) YpsIP31758_3311
            YEN: YE0755(cysJ)
            SFL: SF2779(cysI) SF2780(cysJ)
            SFX: S2972(cysI) S2973(cysJ)
            SFV: SFV_2741(cysJ) SFV_2742(cysI)
            SSN: SSON_2916(cysI) SSON_2917(cysJ)
            SBO: SBO_2646(cysI) SBO_2647(cysJ)
            SDY: SDY_2965(cysI) SDY_2966(cysJ)
            ECA: ECA3546(cysI) ECA3547(cysJ)
            PLU: plu0703(cysJ) plu0704(cysI)
            BUC: BU427(cysI) BU428(cysJ)
            BAS: BUsg413(cysJ)
            SGL: SG0516 SG0517
            BFL: Bfl158(cysJ) Bfl159(cysI)
            BPN: BPEN_163(cysJ) BPEN_164(cysI)
            MSU: MS1249(cysI) MS1250(cysJ)
            APL: APL_1842(cysI) APL_1843(cysJ)
            XFA: XF1498 XF1499
            XFT: PD0715(cysI) PD0716(cysJ)
            XCC: XCC2779 XCC3173(cysJ) XCC3174(cysI) XCC3955(piuB)
            XCB: XC_0991 XC_0992 XC_1334 XC_4044
            XCV: XCV3092 XCV3447(cysJ) XCV3448(cysI) XCV4128
            XAC: XAC2948 XAC3330(cysJ) XAC3331(cysI) XAC4036(piuB)
            XOO: XOO0407(piuB) XOO3398(cysJ) XOO3400(cysI)
            XOM: XOO_0370(XOO0370) XOO_3199(XOO3199) XOO_3200(XOO3200)
            VCH: VC0384 VC0385
            VCO: VC0395_A2795(cysJ)
            VVU: VV1_1402 VV1_1403
            VVY: VV2966 VV2967
            VPA: VP2721 VP2722
            VFI: VF0310 VF0311
            PPR: PBPRA3320 PBPRA3321
            PAE: PA1838(cysI) PA4130 PA4513
            PAU: PA14_58560(piuB)
            PPU: PP_0860 PP_2371(cysI)
            PST: PSPTO_2730(cysI) PSPTO_4569
            PSB: Psyr_2462 Psyr_4243
            PSP: PSPPH_2618(cysI) PSPPH_4268
            PFL: PFL_0863 PFL_2835(cysI) PFL_3665(cysI)
            PFO: Pfl_0797 Pfl_2513 Pfl_3112
            PEN: PSEEN1028 PSEEN3407(cysI)
            PAR: Psyc_1068(cysI)
            PCR: Pcryo_1394
            ACI: ACIAD0799
            SON: SO_3737(cysI) SO_3738(cysJ)
            SDN: Sden_0932 Sden_0933
            SFR: Sfri_3192 Sfri_3193
            SAZ: Sama_2839
            SBL: Sbal_3416
            SLO: Shew_0665
            SHE: Shewmr4_3079 Shewmr4_3080
            SHM: Shewmr7_0892 Shewmr7_0893
            SHN: Shewana3_0855 Shewana3_0856
            SHW: Sputw3181_0881
            CPS: CPS_4759(cysJ) CPS_4760(cysI)
            PHA: PSHAa0154(cysJ) PSHAa0155(cysI)
            PAT: Patl_4038 Patl_4039
            SDE: Sde_2013
            PIN: Ping_3434
            MCA: MCA2059
            FTU: FTT0457c(yccK)
            FTF: FTF0457c(yccK)
            FTW: FTW_1613
            FTL: FTL_1607
            FTH: FTH_1553(dsrC)
            FTN: FTN_0548
            TCX: Tcr_1893
            NOC: Noc_1305 Noc_1306
            HCH: HCH_02538
            CSA: Csal_1891 Csal_2695 Csal_2696
            ABO: ABO_1188(cysI) ABO_2124(cysJ) ABO_2125(cysI-1) ABO_2126(cysI)
            AHA: AHA_3371 AHA_3372(cysI)
            BCI: BCI_0217(cysI) BCI_0218(cysJ)
            NME: NMB1151 NMB1152 NMB1189 NMB1190
            NMA: NMA1362(cysI) NMA1363(cysJ)
            NMC: NMC1091(cysI) NMC1092(cysJ)
            CVI: CV_3573(cysI)
            RSO: RSc1862(cysI2) RSc2425(cysI1)
            REU: Reut_A2696 Reut_B3940 Reut_B5165 Reut_B5211
            REH: H16_A2999(cysI1) H16_B2500
            RME: Rmet_2816 Rmet_5389 Rmet_5636
            BMA: BMA0663(cysI) BMA3052 BMAA1084
            BMV: BMASAVP1_A2348(cysI)
            BML: BMA10299_0676 BMA10299_A2937(cysI)
            BMN: BMA10247_1662(cysI)
            BXE: Bxe_A3664 Bxe_B0922
            BPS: BPSL0956(cysI) BPSL1319 BPSS1241 BPSS1464
            BPM: BURPS1710b_1166(cysI) BURPS1710b_1568(cysI)
                 BURPS1710b_A0241(fdhF) BURPS1710b_A0493
            BTE: BTH_I0814 BTH_II0900 BTH_II1172
            BPE: BP1209
            BPA: BPP1823
            BBR: BB3283
            RFR: Rfer_2456
            POL: Bpro_2339
            MPT: Mpe_A3726
            HAR: HEAR3398
            MMS: mma_2452(cysI)
            NEU: NE0852(yvgQ) NE0853(yvgR)
            NET: Neut_1184 Neut_1185
            EBA: ebA2619(cysI) ebA3193
            AZO: azo0432(cysI)
            DAR: Daro_2912
            MFA: Mfla_0428 Mfla_2733
            ABU: Abu_0730(cysJ)
            MXA: MXAN_2334(cysI) MXAN_2335(cysJ)
            MLO: mll3230
            MES: Meso_3991
            SME: SMc02124
            ATU: Atu0146(cysJ) Atu1456(cisI)
            ATC: AGR_C_238 AGR_C_2687
            RET: RHE_CH01960(cysI)
            RLE: RL2274 RL2290(cysI)
            BME: BMEI1766 BMEII1011
            BMF: BAB1_0181(cysI) BAB2_0225 BAB2_0226
            BMS: BR0181(cysI) BRA0233
            BMB: BruAb1_0177(cysI)
            BOV: BOV_0175(cysI)
            BJA: bll4570 blr1479
            RPA: RPA3711 RPA4213
            RPB: RPB_1401 RPB_1753
            RPC: RPC_4013
            RPD: RPD_1381
            RPE: RPE_1259 RPE_1765
            NWI: Nwi_0590 Nwi_0591
            NHA: Nham_0682 Nham_0683
            CCR: CC_1119 CC_3063
            SIL: SPO2634
            SIT: TM1040_1758
            RSP: RSP_1942
            RDE: RD1_2966(cysI)
            MMR: Mmar10_0345
            ZMO: ZMO0008(cysI) ZMO0009(cysJ)
            BSU: BG14099(yvgQ) BG14100(yvgR)
            BHA: BH0609 BH0610
            BCE: BC4751
            BCZ: BCZK4507(cysJ)
            BTK: BT9727_4489(cysJ)
            BTL: BALH_4332(cysJ)
            BLI: BL01949(cysI) BL01950(cysJ)
            BLD: BLi01302(yvgR) BLi01303(yvgQ)
            BCL: ABC0618(cysI) ABC0619(cysJ)
            BAY: RBAM_030610(yvgR)
            BPU: BPUM_1777(cysJ) BPUM_1778(cysI)
            OIH: OB1653 OB1654
            GKA: GK1409 GK1410
            SAU: SA2413
            SAV: SAV2620
            SAM: MW2540
            SAR: SAR2698(cysJ)
            SAS: SAS2506
            SAC: SACOL2639(cysJ)
            SAB: SAB2494c(cysJ)
            SAA: SAUSA300_2554
            SAO: SAOUHSC_02947
            SEP: SE2179 SE2180
            SER: SERP2190(cysI) SERP2191(cysJ)
            SHA: SH0414(cysJ) SH0415
            SSP: SSP2407 SSP2408 SSP2418
            CGB: cg3118(cysI) cg3119(cysJ)
            RHA: RHA1_ro01797(cysJ)
            RBA: RB380(cysJ)
            CTR: CT435(cysJ)
            CTA: CTA_0475(cysJ)
            CMU: TC0719
            CPN: CPn0548(cysJ)
            CPA: CP0204
            CPJ: CPj0548(cysJ)
            CPT: CpB0569
            CCA: CCA00194
            CAB: CAB190
            CFE: CF0813(cysJ)
            PCU: pc0226(yvgR)
            PMB: A9601_08201(sir)
            PMC: P9515_08251(sir)
            PMF: P9303_16711(sir)
            PMG: P9301_08181(sir)
            PMH: P9215_08521(sir)
            PME: NATL1_07941(sir)
            CHU: CHU_2637(cysI)
            SSO: SSO2909(cysI)
            STO: ST2566
            SAI: Saci_2201(sir)
STRUCTURES  PDB: 1AOP  1DDG  1DDI  1YKG  2AOP  2GEP  3AOP  3GEO  4AOP  4GEP  
                 5AOP  5GEP  6GEP  7GEP  8GEP  
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.1.2
            ExPASy - ENZYME nomenclature database: 1.8.1.2
            ExplorEnz - The Enzyme Database: 1.8.1.2
            ERGO genome analysis and discovery system: 1.8.1.2
            BRENDA, the Enzyme Database: 1.8.1.2
            CAS: 9029-35-0
///
ENTRY       EC 1.8.1.3                  Enzyme
NAME        hypotaurine dehydrogenase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     hypotaurine:NAD+ oxidoreductase
REACTION    hypotaurine + H2O + NAD+ = taurine + NADH + H+ [RN:R01681]
ALL_REAC    R01681
SUBSTRATE   hypotaurine [CPD:C00519];
            H2O [CPD:C00001];
            NAD+ [CPD:C00003]
PRODUCT     taurine [CPD:C00245];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COFACTOR    Heme [CPD:C00032];
            Molybdenum [CPD:C00150]
COMMENT     A molybdohemoprotein.
REFERENCE   1
  AUTHORS   Sumizu, K.
  TITLE     Oxidation of hypotaurine in rat liver.
  JOURNAL   Biochim. Biophys. Acta 63 (1962) 210-212.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00430  Taurine and hypotaurine metabolism
GENES       RHA: RHA1_ro08057(bphAd)
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.1.3
            ExPASy - ENZYME nomenclature database: 1.8.1.3
            ExplorEnz - The Enzyme Database: 1.8.1.3
            ERGO genome analysis and discovery system: 1.8.1.3
            BRENDA, the Enzyme Database: 1.8.1.3
            CAS: 37256-46-5
///
ENTRY       EC 1.8.1.4                  Enzyme
NAME        dihydrolipoyl dehydrogenase;
            LDP-Glc;
            LDP-Val;
            dehydrolipoate dehydrogenase;
            diaphorase;
            dihydrolipoamide dehydrogenase;
            dihydrolipoamide:NAD+ oxidoreductase;
            dihydrolipoic dehydrogenase;
            dihydrothioctic dehydrogenase;
            lipoamide dehydrogenase (NADH);
            lipoamide oxidoreductase (NADH);
            lipoamide reductase;
            lipoamide reductase (NADH);
            lipoate dehydrogenase;
            lipoic acid dehydrogenase;
            lipoyl dehydrogenase;
            protein-6-N-(dihydrolipoyl)lysine:NAD+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     protein-N6-(dihydrolipoyl)lysine:NAD+ oxidoreductase
REACTION    protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine
            + NADH + H+
ALL_REAC    (other) R00209 R01698 R03815 R07618
SUBSTRATE   protein N6-(dihydrolipoyl)lysine;
            NAD+ [CPD:C00003]
PRODUCT     protein N6-(lipoyl)lysine [CPD:C16237];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid
            dehydrogenase complexes. In the pyruvate dehydrogenase complex, it
            binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue
            acetyltransferase, and catalyses oxidation of its dihydrolipoyl
            groups. It plays a similar role in the oxoglutarate and
            3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate
            is the dihydrolipoyl group in the H-protein of the glycine-cleavage
            system (click here for diagram), in which it acts, together with EC
            1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10,
            aminomethyltransferase, to break down glycine. It can also use free
            dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as
            substrate. This enzyme was first shown to catalyse the oxidation of
            NADH by methylene blue; this activity was called diaphorase. The
            glycine cleavage system is composed of four components that only
            loosely associate: the P protein (EC 1.4.4.2), the T protein (EC
            2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H
            protein [6].
REFERENCE   1
  AUTHORS   Massey, V.
  TITLE     Lipoyl dehydrogenase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 275-306.
REFERENCE   2  [PMID:13767908]
  AUTHORS   MASSEY V, GIBSON QH, VEEGER C.
  TITLE     Intermediates in the catalytic action of lipoyl dehydrogenase
            (diaphorase).
  JOURNAL   Biochem. J. 77 (1960) 341-51.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:13471525]
  AUTHORS   SAVAGE N.
  TITLE     Preparation and properties of highly purified diaphorase.
  JOURNAL   Biochem. J. 67 (1957) 146-55.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:16746974]
  AUTHORS   Straub FB.
  TITLE     Isolation and properties of a flavoprotein from heart muscle tissue.
  JOURNAL   Biochem. J. 33 (1939) 787-92.
  ORGANISM  pig [GN:ssc]
REFERENCE   5  [PMID:10966480]
  AUTHORS   Perham RN.
  TITLE     Swinging arms and swinging domains in multifunctional enzymes:
            catalytic machines for multistep reactions.
  JOURNAL   Annu. Rev. Biochem. 69 (2000) 961-1004.
  ORGANISM  Pseudomonas putida [GN:ppu], Escherichia coli [GN:eco]
REFERENCE   6  [PMID:15642479]
  AUTHORS   Nesbitt NM, Baleanu-Gogonea C, Cicchillo RM, Goodson K, Iwig DF,
            Broadwater JA, Haas JA, Fox BG, Booker SJ.
  TITLE     Expression, purification, and physical characterization of
            Escherichia coli lipoyl(octanoyl)transferase.
  JOURNAL   Protein. Expr. Purif. 39 (2005) 269-82.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00252  Alanine and aspartate metabolism
            PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K00382  dihydrolipoamide dehydrogenase
GENES       HSA: 1738(DLD)
            PTR: 463861(DLD)
            MMU: 13382(Dld)
            CFA: 403978(DLD)
            SSC: 397129(DLD)
            GGA: 417699(RCJMB04_3f8)
            XLA: 380588(dld)
            DRE: 399479(dldh)
            SPU: 577103(LOC577103) 588124(LOC588124)
            DME: Dmel_CG7430
            CEL: LLC1.3
            OSA: 4326849 4326980 4337862
            CME: CMM299C CMQ234C
            SCE: YFL018C(LPD1) YPL017C(IRC15)
            AGO: AGOS_AFR512W
            PIC: PICST_36951(LPD1)
            CGR: CAGL0F01947g
            SPO: SPAC1002.09c(dld1)
            AFM: AFUA_2G02100
            AOR: AO090011000486
            CNE: CND05840
            DDI: DDB_0216232(lpd)
            PFA: PF08_0066 PFL1550w
            TAN: TA03445
            TPV: TP03_0227
            TET: TTHERM_00043870
            TBR: Tb11.01.8470 Tb927.3.4390 Tb927.4.5040 Tb927.8.7380
            TCR: 506701.10 507089.270 507757.70 508933.20 509379.10 511025.110
            LMA: LmjF29.1830 LmjF31.2650 LmjF32.3310
            ECO: b0116(lpd)
            ECJ: JW0112(lpd)
            ECE: Z0126(lpdA)
            ECS: ECs0120
            ECC: c0145(lpdA) c5035
            ECI: UTI89_C0129(lpdA) UTI89_C4633
            ECP: ECP_0123
            ECV: APECO1_1869(lpd)
            ECW: EcE24377A_0118(lpdA)
            ECX: EcHS_A0117 EcHS_A0120(lpdA)
            STY: STY0177(lpdA)
            STT: t0160(lpdA)
            SPT: SPA0158(lpdA)
            SEC: SC0153(lpdA)
            STM: STM0154(lpdA)
            YPE: YPO3417(lpdA) YPO3917
            YPK: y0318 y0769(lpdA)
            YPM: YP_0268(lpdA) YP_3131(lpd)
            YPA: YPA_0105 YPA_2919
            YPN: YPN_0050 YPN_0671
            YPP: YPDSF_2938
            YPS: YPTB0118 YPTB0715(lpdA)
            YPI: YpsIP31758_3360(lpdA)
            YEN: YE0702(lpd)
            SFL: SF0113(lpd)
            SFX: S0115(lpdA)
            SFV: SFV_0107(lpdA)
            SSN: SSON_0124(lpdA)
            SBO: SBO_0105(lpdA)
            SDY: SDY_0146(lpdA)
            ECA: ECA3787(lpdA)
            PLU: plu3621(lpdA)
            BUC: BU207(lpdA)
            BAS: BUsg201(lpdA)
            BAB: bbp191(lpdA)
            BCC: BCc_133(lpdA)
            WBR: WGLp321(lpdA)
            SGL: SG0469
            BFL: Bfl151(lpdA)
            BPN: BPEN_156(lpdA)
            HIN: HI1231(lpdA)
            HIT: NTHI1935(lpdA)
            HIP: CGSHiEE_03895
            HIQ: CGSHiGG_01850
            HDU: HD1623(lpdA)
            HSO: HS_1093(lpdA)
            PMU: PM0893(lpdA)
            MSU: MS1334(lpd)
            APL: APL_0771(lpdA)
            XFA: XF0868 XF1548
            XFT: PD0758(lpd) PD1810(lpdA)
            XCC: XCC0544(lpdA) XCC1485(ldp)
            XCB: XC_2751
            XCV: XCV1576(lpd) XCV2303 XCV3777(lpdA)
            XAC: XAC1533(ldp) XAC3659(lpdA)
            XOO: XOO0722(lpdA) XOO2042(ldp)
            XOM: XOO_0658(XOO0658) XOO_1923(XOO1923)
            VCH: VC2412 VC2638
            VCO: VC0395_A1988(lpdA)
            VVU: VV1_1632
            VVY: VV2771
            VPA: VP2517
            VFI: VF2178 VF2301
            PPR: PBPRA0271 PBPRA3194
            PAE: PA1587(lpdG) PA2250(lpdV) PA4829(lpd3)
            PAU: PA14_35490(lpdV) PA14_43970(lpdG) PA14_63850(lpd3)
            PAP: PSPA7_2991(lpdA2) PSPA7_3687(lpdA1) PSPA7_5548
            PPU: PP_4187(lpdG) PP_4404(lpdV) PP_5366(lpd3)
            PST: PSPTO_2201(lpdA)
            PSB: Psyr_2011
            PSP: PSPPH_1982(lpdA)
            PFL: PFL_0268(lpdA) PFL_1720(lpdA) PFL_2531
            PFO: Pfl_1616 Pfl_3466 Pfl_5671
            PEN: PSEEN3638(lpd) PSEEN3856(lpdV) PSEEN5519(lpd3)
            PAR: Psyc_0104(lpdG) Psyc_0768
            PCR: Pcryo_0113 Pcryo_0774
            ACI: ACIAD1020(acoD) ACIAD2874(lpd) ACIAD3145
            SON: SO_0426(lpdA)
            SDN: Sden_3381
            SFR: Sfri_3775
            SAZ: Sama_0377
            SBL: Sbal_3911
            SLO: Shew_3429
            SHE: Shewmr4_0430
            SHM: Shewmr7_3597
            SHN: Shewana3_0428
            SHW: Sputw3181_0528
            ILO: IL0460(lpd)
            CPS: CPS_0826 CPS_4805(lpdA)
            PHA: PSHAa0393(lpd) PSHAa0758
            PAT: Patl_3352
            SDE: Sde_2104
            PIN: Ping_2925
            MAQ: Maqu_1156
            CBU: CBU_0463(lpdA)
            CBD: COXBU7E912_1612(lpdA)
            LPN: lpg1502(lpdA)
            LPF: lpl1524(lpd)
            LPP: lpp1459(lpd)
            MCA: MCA3002(lpdA)
            FTU: FTT1483c(lpd)
            FTF: FTF1483c(lpd)
            FTW: FTW_0810(lpdA)
            FTL: FTL_0311
            FTH: FTH_0312(lpd)
            FTA: FTA_0330(lpdA)
            FTN: FTN_1492(lpdA)
            TCX: Tcr_1003 Tcr_1491
            NOC: Noc_0113 Noc_0965 Noc_1256 Noc_2109
            AEH: Mlg_0271 Mlg_2607
            HHA: Hhal_1084
            HCH: HCH_00152 HCH_00873(lpdA1) HCH_04743(lpdA2)
            CSA: Csal_1219
            ABO: ABO_1494(lpdG)
            AHA: AHA_3861(lpdA)
            DNO: DNO_1100(lpdA)
            BCI: BCI_0510(lpdA)
            VOK: COSY_0864(lpdA)
            NME: NMB0947 NMB0957 NMB1344
            NMA: NMA1142(lpdA2) NMA1151(lpdA3) NMA1556(lpdA)
            NMC: NMC0924(lpdA2) NMC0933(lpdA3) NMC1280(lpdA)
            NGO: NGO0562 NGO0915(dldH) NGO0925
            CVI: CV_0528(lpdA1) CV_1074(lpdA2) CV_2037
            RSO: RSc1271(RS02809) RSc1603(lpdA)
            REU: Reut_A1306 Reut_A2045 Reut_B4451
            REH: H16_A1377(pdhL) H16_A2323(odhL) H16_A3724(lpdaA) H16_B1098
            RME: Rmet_1199 Rmet_2048 Rmet_4216 Rmet_4888
            BMA: BMA1050 BMA1719(lpdA) BMAA2010
            BMV: BMASAVP1_1033 BMASAVP1_A1496 BMASAVP1_A2228(lpdA)
            BML: BMA10299_1319 BMA10299_A0164 BMA10299_A3092(lpdA)
            BMN: BMA10247_1002 BMA10247_1500(lpdA) BMA10247_A2299
            BXE: Bxe_A1543 Bxe_A2810 Bxe_B0582 Bxe_C0853
            BUR: Bcep18194_A4363 Bcep18194_A4651 Bcep18194_A5441
                 Bcep18194_B2463
            BCN: Bcen_0765 Bcen_1030 Bcen_5942
            BCH: Bcen2424_1246 Bcen2424_1510 Bcen2424_2135
            BAM: Bamb_1126 Bamb_1392 Bamb_1974 Bamb_2172 Bamb_6503
            BPS: BPSL1907(odhL) BPSL2299 BPSS2270(lpdV)
            BPM: BURPS1710b_1926(lpdA) BURPS1710b_2743(lpdA)
                 BURPS1710b_A1408(lpdA)
            BPL: BURPS1106A_1774(lpdA) BURPS1106A_2665(lpdA)
                 BURPS1106A_A3064(lpdA)
            BPD: BURPS668_1752(lpdA) BURPS668_2610(lpdA) BURPS668_A3190(lpdA)
            BTE: BTH_I1866 BTH_I2554(lpdA-1) BTH_II2301(lpdA-2)
            PNU: Pnuc_0736 Pnuc_0842
            BPE: BP0618(lpdA) BP0995(lpdA) BP1126(odhL) BP1729
            BPA: BPP1464(lpdA) BPP3047 BPP3215(odhL)
            BBR: BB2538(lpdA) BB3010 BB3667(odhL) BB4695(lpdA)
            RFR: Rfer_0181 Rfer_2214 Rfer_2319
            POL: Bpro_2622 Bpro_2669
            PNA: Pnap_1858
            AAV: Aave_3246
            AJS: Ajs_1824
            VEI: Veis_3977
            MPT: Mpe_A2010 Mpe_A2126 Mpe_A2524
            HAR: HEAR0748(lpd) HEAR1770(odhL) HEAR3352
            MMS: mma_0676(lpdA) mma_1514 mma_3575
            NEU: NE0774 NE2157 NE2319(lpdA3)
            NET: Neut_1632 Neut_1773 Neut_2103
            NMU: Nmul_A0515 Nmul_A0855 Nmul_A2075
            EBA: ebA136(lpd) ebA6683(ldp)
            AZO: azo1371(lpdA) azo1557(odhL)
            DAR: Daro_0440 Daro_2857
            MFA: Mfla_2076
            ABU: Abu_1474(lpdA)
            NIS: NIS_0931
            SUN: SUN_1208 SUN_1210
            GSU: GSU2446(lpdA-1) GSU2588(lpdA-2)
            GME: Gmet_1896 Gmet_2764
            PCA: Pcar_0347 Pcar_1486
            DVU: DVU1423(lpdA)
            DDE: Dde_1690
            BBA: Bd0778(pdhD) Bd2731(lpdA)
            DPS: DP0303(phdD)
            ADE: Adeh_1822
            MXA: MXAN_4219(lpdA)
            SFU: Sfum_2645 Sfum_3549
            RPR: RP460 RP805
            RTY: RT0447(pdhD1) RT0792(pdhD2)
            RCO: RC0693(pdhD) RC1239(pdhD)
            RFE: RF_0807(lpdA2) RF_1270(lpdA1)
            RBE: RBE_0091(lpdA1) RBE_0578(lpdA2)
            RAK: A1C_04135 A1C_06210
            RBO: A1I_03305 A1I_07480
            RCM: A1E_02510 A1E_05230
            RRI: A1G_04340 A1G_06780
            OTS: OTBS_0019(lpdA)
            WOL: WD0325(lpdA) WD0751(lpdA)
            WBM: Wbm0559 Wbm0561
            AMA: AM797(lpdA)
            APH: APH_0065(lpdA-1) APH_0393(lpdA-2) APH_1070(lpdA-3)
            ERU: Erum1420 Erum4941 Erum5130
            ERW: ERWE_CDS_01380(lpd) ERWE_CDS_05380(lpd)
            ERG: ERGA_CDS_01340(lpd) ERGA_CDS_05280(lpd)
            ECN: Ecaj_0138 Ecaj_0521
            ECH: ECH_0509(lpdA-1) ECH_0992(lpdA-2)
            NSE: NSE_0463(lpdA-1) NSE_0671(lpdA-2)
            PUB: SAR11_0235(pdhD)
            MLO: mll4296 mll4470 mlr0388
            MES: Meso_1626 Meso_3400
            SME: SMc01035(lpdA1) SMc02487(lpdA2) SMc03204(lpdA3)
            ATU: Atu1434(lpdA) Atu2632(lpdA)
            ATC: AGR_C_2644 AGR_C_4772
            RET: RHE_CH01938(lpdAch1) RHE_CH03882(lpdAch2) RHE_PC00073(lpdAc)
            RLE: RL2246 RL4429(lpdA) pRL100306(lpdV)
            BME: BMEI0145 BMEI0857 BMEII0744 BMEII0745
            BMF: BAB1_1149 BAB1_1918(lpdA-2) BAB2_0712(lpdA-3)
            BMS: BR1126(lpdA-1) BR1918(lpdA-2) BRA0527(lpdA-3)
            BMB: BruAb1_1132(lpdA-1) BruAb1_1894(lpdA-2) BruAb2_0697(lpdA-3)
            BOV: BOV_1084(lpdA-2) BOV_1847(lpdA-3) BOV_A0459(lpdA-1)
            BJA: bll0449(lpdA) bll4778 blr3722(lpd) blr6334(lpdA)
            BRA: BRADO0409(lpd) BRADO4083(lpd)
            BBT: BBta_0398(lpd) BBta_4459(lpd)
            RPA: RPA0185(dldH) RPA2863
            RPB: RPB_0274 RPB_2766
            RPC: RPC_0183 RPC_2493
            RPD: RPD_0550 RPD_2807
            RPE: RPE_0290 RPE_2618
            NWI: Nwi_0425 Nwi_1813
            NHA: Nham_0537 Nham_1752
            BHE: BH05780(pdhD1) BH16520(pdhD2)
            BQU: BQ04940(pdhD2) BQ13400(pdhD1)
            BBK: BARBAKC583_0027(lpdA1) BARBAKC583_0537(lpdA2)
            CCR: CC_0342 CC_1731
            SIL: SPO0340(lpdA) SPO2222
            SIT: TM1040_1096 TM1040_2775 TM1040_3504
            RSP: RSP_0962 RSP_2968
            JAN: Jann_0837 Jann_1720
            RDE: RD1_1603(lpdA) RD1_2995(lpdA) RD1_3670
            PDE: Pden_0551 Pden_4760
            MMR: Mmar10_0709 Mmar10_1425 Mmar10_2813
            HNE: HNE_1974(lpdA1) HNE_3262(lpdA2)
            ZMO: ZMO0512(lpd)
            NAR: Saro_1178 Saro_1945
            SAL: Sala_1237 Sala_2225
            ELI: ELI_06145 ELI_08010
            GOX: GOX2292
            GBE: GbCGDNIH1_1187 GbCGDNIH1_2066
            RRU: Rru_A1215 Rru_A1878
            MAG: amb2321 amb3963
            MGM: Mmc1_1453 Mmc1_2397 Mmc1_3245
            ABA: Acid345_2790 Acid345_4304
            BSU: BG10210(pdhD) BG11725(lpd) BG12561(acoL)
            BHA: BH0216 BH0779 BH1825(acoL) BH2652(pdhD) BH2764
            BAN: BA2773(acoL) BA4181(pdhD) BA4385(bfmbC)
            BAR: GBAA2773(acoL) GBAA4181(pdhD) GBAA4385(bfmbC)
            BAA: BA_3297 BA_4647 BA_4840
            BAT: BAS2585 BAS3880 BAS4068
            BCE: BC2776 BC3970 BC4160
            BCA: BCE_2801(acoL) BCE_4018(pdhD) BCE_4235(bfmbC)
            BCZ: BCZK2502(acoL) BCZK3728(pdhD) BCZK3915(bfmbC)
            BTK: BT9727_2536(acoL) BT9727_3712(pdhD) BT9727_3906(bfmbC)
            BTL: BALH_2491(acoL) BALH_3592(pdhD) BALH_3773(bfmbC)
            BLI: BL01503(bfmBC) BL01619(pdhD) BL03015(acoL)
            BLD: BLi00852(acoL) BLi01677(pdhD) BLi02583(lpdV)
            BCL: ABC2417(pdhD) ABC2452(lpd) ABC2787(acoL)
            BAY: RBAM_014450
            BPU: BPUM_0453 BPUM_0454 BPUM_1174 BPUM_1358 BPUM_2145(bfmBC)
            OIH: OB1415(pdhD) OB1867
            GKA: GK1061 GK2379
            SAU: SA0946(pdhD) SA1349
            SAV: SAV1096(pdhD) SAV1518
            SAM: MW0979(pdhD) MW1471
            SAR: SAR1070(pdhD) SAR1596(bfmBC)
            SAS: SAS1031 SAS1457
            SAC: SACOL1105(pdhD) SACOL1563(lpdA)
            SAB: SAB0962(pdhD) SAB1391c
            SAA: SAUSA300_0996(lpdA) SAUSA300_1467(lpdA)
            SAO: SAOUHSC_01043 SAOUHSC_01614
            SEP: SE0077 SE0253 SE0794 SE1199
            SER: SERP0683(pdhD) SERP1079(lpdA) SERP2327
            SHA: SH0223 SH1397 SH1856(pdhD)
            SSP: SSP1237 SSP1693
            LMO: lmo1055(PdhD) lmo1371
            LMF: LMOf2365_1076 LMOf2365_1388
            LIN: lin1047(PdhD) lin1408
            LWE: lwe1031(pdhD) lwe1386
            LLA: L0036(pdhD)
            LLC: LACR_0048
            LLM: llmg_0071(pdhD)
            SPY: SPy_1031(acoL)
            SPZ: M5005_Spy_0755(acoL)
            SPM: spyM18_1013(acoL)
            SPG: SpyM3_0664(acoL)
            SPS: SPs1189
            SPH: MGAS10270_Spy0873(acoL)
            SPI: MGAS10750_Spy0907(acoL)
            SPJ: MGAS2096_Spy0828(acoL)
            SPK: MGAS9429_Spy0869(acoL)
            SPF: SpyM51004(acoL)
            SPA: M6_Spy0779
            SPB: M28_Spy0734(acoL)
            SPN: SP_1161
            SPR: spr1048(acoL)
            SPD: SPD_1025(lpdA)
            SAG: SAG0881
            SAN: gbs0898
            SAK: SAK_1004
            SMU: SMU.130(adhD) SMU.1424(pdhD)
            STC: str1048(acoL)
            STL: stu1048(acoL)
            SSA: SSA_1137(pdhD) SSA_1174(acoL)
            SGO: SGO_1130
            LPL: lp_2151(pdhD)
            LSA: LSA1082(pdhD)
            LSL: LSL_0156(lpd)
            LBR: LVIS_1407
            LCA: LSEI_1308 LSEI_1446
            EFA: EF1356(lpdA) EF1661(bkdD)
            OOE: OEOE_0331
            STH: STH2163 STH414
            CTC: CTC02047
            CDF: CD0039(acoL)
            CBO: CBO0700(pdhD1) CBO1634(acoL)
            CBA: CLB_0739 CLB_1651(acoL)
            CBH: CLC_0754 CLC_1660(acoL)
            CBF: CLI_0769(lpdA) CLI_1711(acoL)
            CKL: CKL_1769(bfmBC) CKL_2268(lpdA)
            CHY: CHY_0713(lpdA)
            DSY: DSY2918 DSY4139 DSY4281
            TTE: TTE0088(lpd) TTE1674(lpd2)
            MTA: Moth_1763
            MGE: MG_271(pdhD)
            MPN: MPN390(pdhD)
            MPU: MYPU_0210(pdhD) MYPU_7610(pdhD)
            MPE: MYPE5110(pdhD)
            MGA: MGA_0161(lpd)
            MMY: MSC_0268(pdhD) MSC_0544(pdhD)
            MMO: MMOB1750(pdhD) MMOB5800(pdhD)
            MHY: mhp504(pdhD) mhp587(pdhD)
            MHJ: MHJ_0504(pdhD) MHJ_0572(pdhD-1)
            MHP: MHP7448_0507(pdhD) MHP7448_0571(pdhD-1)
            MSY: MS53_0275(pdhD)
            MCP: MCAP_0228(pdhD) MCAP_0427
            POY: PAM603(lpd)
            AYW: AYWB_139(lpd)
            MFL: Mfl042
            MTU: Rv0462(lpd) Rv3303c(lpdA)
            MTC: MT0478(lpdA-1) MT0817 MT3402(lpdA-2)
            MBO: Mb0471(lpd) Mb0819c Mb3331c(lpdA)
            MBB: BCG_0502(lpd) BCG_3368c(lpdA)
            MLE: ML2387(lpd)
            MPA: MAP3424c(lpdA) MAP3956
            MAV: MAV_4687(lpdA)
            MSM: MSMEG_0903(lpdA) MSMEG_1735
            MMC: Mmcs_0631 Mmcs_1249
            CGL: NCgl0355(cgl0366) NCgl0658(cgl0688)
            CGB: cg0441(lpd) cg0790(lpdA)
            CEF: CE0383(lpd) CE0708
            CDI: DIP0368(lpd) DIP0645(lpdA)
            CJK: jk1936(lpd)
            NFA: nfa50180 nfa52650 nfa9670
            RHA: RHA1_ro02140(dldH1) RHA1_ro02927(dldH2) RHA1_ro03318(dldH3)
                 RHA1_ro03377(dldH4) RHA1_ro05562(dldH5) RHA1_ro06262(dldH6)
                 RHA1_ro11024(lpdA)
            SCO: SCO0884(SCM1.17c) SCO2180(pdhL) SCO4919(SCK13.11)
            SMA: SAV3340 SAV6024(lpdA1) SAV7348(lpdB2)
            TWH: TWT019 TWT502(lpd) TWT629
            TWS: TW019 TW260(acoL) TW646(pdhD)
            LXX: Lxx04710(lpdA) Lxx10150
            CMI: CMM_0990(lpdA) CMM_1642(lpdB)
            ART: Arth_4300 Arth_4469
            AAU: AAur_1404(lpdA) AAur_1756(lpdA)
            PAC: PPA1227 PPA1721
            TFU: Tfu_0994 Tfu_2559
            FRA: Francci3_0696 Francci3_3134
            FAL: FRAAL1206 FRAAL3607(lpd) FRAAL5151(lpdA)
            ACE: Acel_0394 Acel_0936
            SEN: SACE_1639(dldH2) SACE_5677(pdhD) SACE_6526(lpdA)
            BLO: BL1074(pdhD)
            BAD: BAD_0945(pdhD)
            RXY: Rxyl_2549
            RBA: RB1231(lpd) RB2718(dldH)
            CTR: CT557(lpdA)
            CTA: CTA_0607(lpdA)
            CMU: TC0846
            CPN: CPn0833(lpdA)
            CPA: CP1037
            CPJ: CPj0833(lpdA)
            CPT: CpB0862
            CCA: CCA00933
            CAB: CAB902(pdhD)
            CFE: CF0081(lpdA)
            PCU: pc0151(lpdA) pc1088(dld1)
            TDE: TDE1629(lpdA)
            LIL: LA1223(lpdA1) LA2115(lpdA2) LA2886(lpdA3)
            LIC: LIC11159 LIC12475(lpdA)
            LBJ: LBJ_2037(lpdA-2) LBJ_2124(lpdA-1)
            LBL: LBL_1013(lpdA-2) LBL_2121(lpdA-1)
            SYN: slr1096(phdD)
            SYW: SYNW1630(lpdA)
            SYC: syc0352_d(phdD)
            SYF: Synpcc7942_1198
            SYD: Syncc9605_0869
            SYE: Syncc9902_1530
            SYG: sync_0750(lpdA)
            SYR: SynRCC307_0615(lpdA)
            SYX: SynWH7803_1744(lpdA)
            CYA: CYA_2059(lpdA)
            CYB: CYB_0749(lpdA)
            TEL: tll0868
            GVI: glr3029
            ANA: alr4745
            AVA: Ava_1765 Ava_1927 Ava_2431 Ava_3460
            PMA: Pro1372(lpd)
            PMM: PMM1298(lpdA)
            PMT: PMT0335(lpdA)
            PMN: PMN2A_0864
            PMB: A9601_14971(lpd)
            PMC: P9515_14591(lpd)
            PMF: P9303_19781(lpd)
            PMG: P9301_14831(lpd)
            PMH: P9215_15261(lpd)
            PME: NATL1_17171(lpd)
            TER: Tery_3171
            BTH: BT_0309 BT_3186
            BFR: BF0024 BF1618
            BFS: BF0023(pdhD) BF1631(lpd)
            PGI: PG0802(pdhD)
            SRU: SRU_1603(lpdA)
            CHU: CHU_1086(adhD) CHU_3360(lpdA)
            GFO: GFO_1202(lpd) GFO_1679(lpd) GFO_1865(lpd) GFO_2165(lpd)
            FPS: FP0706(lpdA2) FP1735(lpdA1)
            CTE: CT1298(lpd-1)
            CCH: Cag_1276
            PLT: Plut_0784
            DRA: DR_2370 DR_2526
            DGE: Dgeo_0353 Dgeo_2323
            TTH: TTC1700 TTC1753
            TTJ: TTHA0233 TTHA0287
            AAE: aq_736(lpdA)
            TMA: TM0381
            MJA: MJ0636
            MMP: MMP1332
            MAC: MA1652
            MBA: Mbar_A2696
            MMA: MM_3279
            MST: Msp_1077
            MSI: Msm_0637
            MKA: MK0849(lpd)
            HAL: VNG2220G(lpdA)
            HMA: rrnAC2953(lpdA2) rrnAC3381(lpdA1) rrnB0197(lpdA3)
            HWA: HQ1085A(lpdA)
            NPH: NP0104A(lpdA)
            TAC: Ta0208 Ta1435
            TVO: TVN0099 TVN1386
            PTO: PTO0546 PTO0887
            RCI: RCIX79(lpd) RRC122(pdhD)
            APE: APE_1669.1
            SSO: SSO1123(pdhD-1) SSO1524(pdhD-2) SSO1565(pdhD-3)
                 SSO2559(pdhD-4)
            STO: ST0687 ST1487 ST1865 ST1879
            SAI: Saci_0136(lpdV) Saci_0338(pdhD)
            PAI: PAE2649
STRUCTURES  PDB: 1DXL  1EBD  1GJX  1IVI  1JEH  1LPF  1LVL  1V59  1ZMC  1ZMD  
                 1ZY8  2A8X  2F5Z  2PDD  2PDE  3LAD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.1.4
            ExPASy - ENZYME nomenclature database: 1.8.1.4
            ExplorEnz - The Enzyme Database: 1.8.1.4
            ERGO genome analysis and discovery system: 1.8.1.4
            BRENDA, the Enzyme Database: 1.8.1.4
            CAS: 9001-18-7
///
ENTRY       EC 1.8.1.5                  Enzyme
NAME        2-oxopropyl-CoM reductase (carboxylating);
            NADPH:2-(2-ketopropylthio)ethanesulfonate
            oxidoreductase/carboxylase;
            NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     2-mercaptoethanesulfonate,acetoacetate:NADP+ oxidoreductase
            (decarboxylating)
REACTION    2-mercaptoethanesulfonate + acetoacetate + NADP+ =
            2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH [RN:R05713]
ALL_REAC    R05713
SUBSTRATE   2-mercaptoethanesulfonate [CPD:C03576];
            acetoacetate [CPD:C00164];
            NADP+ [CPD:C00006]
PRODUCT     2-(2-oxopropylthio)ethanesulfonate [CPD:C11497];
            CO2 [CPD:C00011];
            NADPH [CPD:C00005]
COMMENT     Also acts on thioethers longer in chain length on the oxo side, e.g.
            2-oxobutyl-CoM, but this portion must be attached to CoM
            (2-mercaptoethanesulfonate); no CoM analogs will substitute. This
            enzyme forms component II of a four-component enzyme system
            {comprising EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC
            1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II],
            EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III]
            and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component
            IV]} that is involved in epoxyalkane carboxylation in Xanthobacter
            sp. strain Py2.
REFERENCE   1  [PMID:10411892]
  AUTHORS   Allen JR, Clark DD, Krum JG, Ensign SA.
  TITLE     A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial
            pathway of aliphatic epoxide carboxylation.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 8432-7.
  ORGANISM  Xanthobacter sp.
REFERENCE   2  [PMID:10684609]
  AUTHORS   Clark DD, Allen JR, Ensign SA.
  TITLE     Characterization of five catalytic activities associated with the
            NADPH:2-ketopropyl-coenzyme M [2-(2-ketopropylthio)ethanesulfonate]
            oxidoreductase/carboxylase of the Xanthobacter strain Py2 epoxide
            carboxylase system.
  JOURNAL   Biochemistry. 39 (2000) 1294-304.
  ORGANISM  Xanthobacter sp.
GENES       XAU: Xaut_5075
STRUCTURES  PDB: 2C3C  2C3D  
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.1.5
            ExPASy - ENZYME nomenclature database: 1.8.1.5
            ExplorEnz - The Enzyme Database: 1.8.1.5
            ERGO genome analysis and discovery system: 1.8.1.5
            UM-BBD (Biocatalysis/Biodegradation Database): 1.8.1.5
            BRENDA, the Enzyme Database: 1.8.1.5
///
ENTRY       EC 1.8.1.6                  Enzyme
NAME        cystine reductase;
            cystine reductase (NADH);
            NADH-dependent cystine reductase;
            cystine reductase (NADH2);
            NADH2:L-cystine oxidoreductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     L-cysteine:NAD+ oxidoreductase
REACTION    2 L-cysteine + NAD+ = L-cystine + NADH + H+ [RN:R00892]
ALL_REAC    R00892
SUBSTRATE   L-cysteine [CPD:C00097];
            NAD+ [CPD:C00003]
PRODUCT     L-cystine [CPD:C00491];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13174550]
  AUTHORS   ROMANO AH, NICKERSON WJ.
  TITLE     Cystine reductase of pea seeds and yeasts.
  JOURNAL   J. Biol. Chem. 208 (1954) 409-16.
  ORGANISM  pig [GN:ssc], Candida albicans [GN:cal], Pisum sativum
REFERENCE   2  [PMID:5436160]
  AUTHORS   Carroll JE, Kosicki GW, Thibert RJ.
  TITLE     Alpha-substituted cystines as possible substrates for cystine
            reductase and L-amino acid oxidase.
  JOURNAL   Biochim. Biophys. Acta. 198 (1970) 601-3.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:211119]
  AUTHORS   Maresca B, Jacobson E, Medoff G, Kobayashi G.
  TITLE     Cystine reductase in the dimorphic fungus Histoplasma capsulatum.
  JOURNAL   J. Bacteriol. 135 (1978) 987-92.
  ORGANISM  Histoplasma capsulatum
PATHWAY     PATH: map00272  Cysteine metabolism
ORTHOLOGY   KO: K05395  cystine reductase
GENES       CVI: CV_0530
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.1.6
            ExPASy - ENZYME nomenclature database: 1.8.1.6
            ExplorEnz - The Enzyme Database: 1.8.1.6
            ERGO genome analysis and discovery system: 1.8.1.6
            BRENDA, the Enzyme Database: 1.8.1.6
            CAS: 9029-18-9
///
ENTRY       EC 1.8.1.7                  Enzyme
NAME        glutathione-disulfide reductase;
            glutathione reductase;
            glutathione reductase (NADPH);
            NADPH-glutathione reductase;
            GSH reductase;
            GSSG reductase;
            NADPH-GSSG reductase;
            glutathione S-reductase;
            NADPH:oxidized-glutathione oxidoreductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     glutathione:NADP+ oxidoreductase
REACTION    2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
            [RN:R00115]
ALL_REAC    R00115;
            (other) R00094
SUBSTRATE   glutathione [CPD:C00051];
            NADP+ [CPD:C00006]
PRODUCT     glutathione disulfide [CPD:C00127];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016]
COMMENT     A dimeric flavoprotein (FAD); activity is dependent on a
            redox-active disulfide in each of the active centres.
REFERENCE   1
  AUTHORS   Pai, E.F., Schirmer, R.H. and Schulz, G.E.
  TITLE     Structural studies on crystalline glutathione reductase from human
            erythrocytes.
  JOURNAL   In: Singer, T.P. and Ondarza, R.N. (Eds.), Mechanisms of Oxidizing
            Enzymes, Mechanisms of Oxidizing Enzymes, New York, 1978, p. 17-22.
REFERENCE   2  [PMID:330529]
  AUTHORS   Pigiet VP, Conley RR.
  TITLE     Purification of thioredoxin, thioredoxin reductase, and glutathione
            reductase by affinity chromatography.
  JOURNAL   J. Biol. Chem. 252 (1977) 6367-72.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:13271446]
  AUTHORS   RACKER E.
  TITLE     Glutathione reductase from bakers' yeast and beef liver.
  JOURNAL   J. Biol. Chem. 217 (1955) 855-65.
  ORGANISM  cow [GN:bta]
REFERENCE   4
  AUTHORS   van Heyningen, R. and Pirie, A.
  TITLE     Reduction of glutathione coupled with oxidative decarboxylation of
            malate in cattle lens.
  JOURNAL   Biochem. J. 53 (1953) 436-444.
REFERENCE   5  [PMID:9277]
  AUTHORS   Worthington DJ, Rosemeyer MA.
  TITLE     Glutathione reductase from human erythrocytes. Catalytic properties
            and aggregation.
  JOURNAL   Eur. J. Biochem. 67 (1976) 231-8.
  ORGANISM  human [GN:hsa]
REFERENCE   6  [PMID:10969088]
  AUTHORS   Bohme CC, Arscott LD, Becker K, Schirmer RH, Williams CH Jr.
  TITLE     Kinetic characterization of glutathione reductase from the malarial
            parasite Plasmodium falciparum. Comparison with the human enzyme.
  JOURNAL   J. Biol. Chem. 275 (2000) 37317-23.
  ORGANISM  human [GN:hsa]
REFERENCE   7  [PMID:1524433]
  AUTHORS   Libreros-Minotta CA, Pardo JP, Mendoza-Hernandez G, Rendon JL.
  TITLE     Purification and characterization of glutathione reductase from
            Rhodospirillum rubrum.
  JOURNAL   Arch. Biochem. Biophys. 298 (1992) 247-53.
  ORGANISM  Rhodospirillum rubrum [GN:rru]
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00480  Glutathione metabolism
ORTHOLOGY   KO: K00383  glutathione reductase (NADPH)
GENES       HSA: 2936(GSR)
            PTR: 464099(GSR)
            MMU: 14782(Gsr)
            RNO: 116686(Gsr)
            CFA: 475596(GSR)
            BTA: 282388(TXNRD1)
            XLA: 447610(MGC85342)
            SPU: 589396(LOC589396)
            CEL: ZK637.10(trxr-2)
            ATH: AT3G54660(GR)
            OSA: 4331112 4331719
            CME: CMC043C
            SCE: YPL091W(GLR1)
            AGO: AGOS_AGR196W
            PIC: PICST_40145(GLR2) PICST_42900(GLR1)
            CGR: CAGL0H05665g
            SPO: SPBC17A3.07
            ANI: AN0932.2
            AFM: AFUA_1G15960
            AOR: AO090005001092
            CNE: CNE01560
            DDI: DDB_0231410(gsr)
            PFA: PF14_0192
            TET: TTHERM_00047660 TTHERM_01222600
            ECO: b3500(gor)
            ECJ: JW3467(gor)
            ECE: Z4900(gor)
            ECS: ECs4372
            ECC: c4299(gor)
            ECI: UTI89_C4019(gor)
            ECP: ECP_3590
            ECV: APECO1_2953(gor)
            ECW: EcE24377A_3982(gor)
            ECX: EcHS_A3700(gor)
            STY: STY4205(gor)
            STT: t3918(gor)
            SPT: SPA3455(gor)
            SEC: SC3526(gor)
            STM: STM3597(gor)
            YPE: YPO3977(gor)
            YPK: y3852(gor)
            YPM: YP_3340(gor)
            YPA: YPA_3805
            YPN: YPN_3626
            YPP: YPDSF_3342
            YPS: YPTB3818(gor)
            YPI: YpsIP31758_4049(gor)
            SFL: SF3531(gor)
            SFX: S4237(gor)
            SFV: SFV_3512(gor)
            SSN: SSON_3735(gor)
            SBO: SBO_3498(gor)
            SDY: SDY_3562(gor)
            ECA: ECA0062(gor)
            PLU: plu0375(gor)
            SGL: SG0068
            ENT: Ent638_3913
            KPN: KPN_03866(gor)
            HIN: HI0161(gor)
            HIT: NTHI0251(gor)
            HIP: CGSHiEE_02475
            HDU: HD0354(gshR)
            HSO: HS_1106(gor)
            PMU: PM1235(gor)
            MSU: MS1985(lpd)
            APL: APL_1243(gor)
            XCC: XCC2579
            XCB: XC_1539
            XCV: XCV2903
            XAC: XAC2750
            XOM: XOO_3110(XOO3110)
            VCH: VC0186
            VCO: VC0395_A2568(gor)
            VVU: VV1_1105
            VVY: VV0065
            VPA: VP0068
            VFI: VF2489
            PPR: PBPRA3546
            PAE: PA2025(gor)
            PAU: PA14_38330(gor)
            PPU: PP_3819(gor)
            PST: PSPTO_3112(gor-1) PSPTO_4254(gor-2)
            PSB: Psyr_2979
            PSP: PSPPH_2261(gor)
            PFL: PFL_3398(gor)
            PFO: Pfl_2928
            PEN: PSEEN2295(gor)
            PAR: Psyc_1693(gor)
            PCR: Pcryo_1966
            SON: SO_4702(gor)
            SDN: Sden_3592
            SFR: Sfri_3877
            SAZ: Sama_3543
            SBL: Sbal_0121
            SLO: Shew_3660
            SPC: Sputcn32_0084
            SHE: Shewmr4_3845
            SHM: Shewmr7_3938
            SHN: Shewana3_4054
            SHW: Sputw3181_3981
            ILO: IL2329(gor)
            CPS: CPS_4984(gor)
            PHA: PSHAa0360(gor)
            PAT: Patl_4206
            PIN: Ping_0507
            LPN: lpg0578(gor)
            LPF: lpl0614(gor)
            LPP: lpp0630(gor)
            FTU: FTT0955c(gor)
            FTF: FTF0955c(gor)
            FTW: FTW_0853(gor)
            FTL: FTL_1248
            FTH: FTH_1225(gor)
            FTA: FTA_1321(gor)
            FTN: FTN_0834(gor)
            TCX: Tcr_0140
            NOC: Noc_1608
            AEH: Mlg_2534
            HCH: HCH_03925(gor)
            ABO: ABO_1423(gor)
            AHA: AHA_0019(gor)
            VOK: COSY_0276(gor)
            RSO: RSc0014(gor)
            REU: Reut_A1485 Reut_A3435
            RME: Rmet_3554
            BMA: BMA3362(gor)
            BMV: BMASAVP1_A3030(gor)
            BML: BMA10299_A2063(gor)
            BMN: BMA10247_2222(gor)
            BUR: Bcep18194_A6352
            BCN: Bcen_2392
            BCH: Bcen2424_3006
            BAM: Bamb_3050 Bamb_6438
            BPS: BPSL0297(gor)
            BPM: BURPS1710b_0498(gor)
            BPL: BURPS1106A_0317(gor)
            BPD: BURPS668_0303(gor)
            BTE: BTH_I0272(gor)
            BPE: BP2120(gor)
            BPA: BPP1358(gor)
            BBR: BB2424(gor)
            POL: Bpro_0643
            MPT: Mpe_A2124
            MMS: mma_0966(gor)
            AZO: azo0659(gor)
            MXA: MXAN_2318(gor)
            AMA: AM215(gor)
            MLO: mll0523
            MES: Meso_1461
            SME: SMc00154(gor)
            ATU: Atu1611(gor)
            ATC: AGR_C_2967
            RET: RHE_CH02377(gor)
            RLE: RL2694(gor)
            BME: BMEI0972
            BMF: BAB1_1030
            BMS: BR1012(gor)
            BMB: BruAb1_1017(gor)
            BOV: BOV_0978(gor)
            BJA: blr3757(gor)
            BRA: BRADO4712(gor)
            BBT: BBta_3485(gor)
            RPA: RPA1983(gor)
            RPB: RPB_3384
            RPC: RPC_2078
            RPD: RPD_2057
            RPE: RPE_1989
            NWI: Nwi_1223
            NHA: Nham_1482
            BHE: BH06430(gor)
            BQU: BQ06800(gor)
            BBK: BARBAKC583_0604(gor)
            CCR: CC_2302
            SIL: SPO1328(gor)
            SIT: TM1040_1957
            RSP: RSP_0358(gor)
            RDE: RD1_1919(gor)
            MMR: Mmar10_0973
            HNE: HNE_0707(gor)
            ZMO: ZMO1211(gor)
            GOX: GOX1764
            GBE: GbCGDNIH1_1427
            RRU: Rru_A0682
            MAG: amb1666
            SEP: SE0080 SE2184
            SER: SERP2195
            SHA: SH0217
            SSP: SSP1636
            LMO: lmo0906 lmo1433
            LMF: LMOf2365_0928(gor) LMOf2365_1452
            LIN: lin0906 lin1472
            LWE: lwe0891 lwe1450
            LLA: L0197(gshR)
            LLC: LACR_0912
            LLM: llmg_1702(gshR) llmg_2331
            SPY: SPy_0813(gor)
            SPZ: M5005_Spy_0627(gor)
            SPM: spyM18_0875(gshR)
            SPG: SpyM3_0546(gor)
            SPS: SPs1308
            SPH: MGAS10270_Spy0683(gor)
            SPI: MGAS10750_Spy0715(gor)
            SPJ: MGAS2096_Spy0692(gor)
            SPK: MGAS9429_Spy0682(gor)
            SPF: SpyM51180(gor)
            SPA: M6_Spy0644
            SPB: M28_Spy0607(gor)
            SPN: SP_0784
            SPR: spr0692(gor)
            SPD: SPD_0685(gor)
            SAG: SAG1375(gor)
            SAN: gbs1445
            SAK: SAK_1408(gor)
            SMU: SMU.140 SMU.838(gshR)
            STC: str0408(gor)
            STL: stu0408(gor)
            STE: STER_0447
            SSA: SSA_1533(gor)
            SGO: SGO_0749
            LPL: lp_0369(gshR1) lp_1253(gshR2) lp_1822(gshR3) lp_3267(gshR4)
            LJO: LJ0042
            LAC: LBA1107
            LSA: LSA1871(gshR)
            LSL: pSF118-44_42
            LBR: LVIS_0434 LVIS_2051
            LCA: LSEI_2187 LSEI_2627
            LGA: LGAS_0040
            EFA: EF3270(gor)
            OOE: OEOE_1191
            LME: LEUM_0947
            MTU: Rv2855(mtr)
            MTC: MT2922
            MBO: Mb2880(mtr)
            MPA: MAP2923(gorA)
            CGL: NCgl1928(cgl2003)
            CGB: cg2194(gor)
            CEF: CE1896
            CDI: DIP1494
            CJK: jk1153(gorA)
            RHA: RHA1_ro06610
            SMA: SAV2154(lpdA2)
            NCA: Noca_1648
            SEN: SACE_5978(mtr)
            RBA: RB4396
            SYW: SYNW1533(gshR)
            SYC: syc0698_d(gor)
            SYF: Synpcc7942_0842
            SYD: Syncc9605_0976
            SYE: Syncc9902_0889
            SYG: sync_1931
            SYR: SynRCC307_1202(gor)
            SYX: SynWH7803_0706(gor)
            TEL: tll1608
            GVI: gll4201
            ANA: all4968(gor)
            AVA: Ava_2244
            PMA: Pro0569(gor)
            PMM: PMM0567(gshR)
            PMT: PMT0470(gshR)
            PMN: PMN2A_0003
            PMB: A9601_06231(gor)
            PMC: P9515_06311(gor)
            PMF: P9303_18091(gor)
            PMG: P9301_05931(gor)
            PMH: P9215_06481(gor)
            PME: NATL1_06221(gor)
            GFO: GFO_1323(gor) GFO_3156(gor)
            MAC: MA1019 MA4013(gor)
            MBA: Mbar_A0570
            MMA: MM_0897
STRUCTURES  PDB: 1ONF  2AAQ  2GH5  2HQM  
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.1.7
            ExPASy - ENZYME nomenclature database: 1.8.1.7
            ExplorEnz - The Enzyme Database: 1.8.1.7
            ERGO genome analysis and discovery system: 1.8.1.7
            BRENDA, the Enzyme Database: 1.8.1.7
            CAS: 9001-48-3
///
ENTRY       EC 1.8.1.8                  Enzyme
NAME        protein-disulfide reductase;
            protein disulphide reductase;
            insulin-glutathione transhydrogenase;
            disulfide reductase;
            NAD(P)H2:protein-disulfide oxidoreductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     protein-dithiol:NAD(P)+ oxidoreductase
REACTION    protein dithiol + NAD(P)+ = protein disulfide + NAD(P)H + H+
            [RN:R03913 R03914]
ALL_REAC    R03913 R03914
SUBSTRATE   protein dithiol [CPD:C02315];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     protein disulfide [CPD:C02582];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:13712218]
  AUTHORS   HATCH MD, TURNER JF.
  TITLE     A protein disulphide reductase from pea seeds.
  JOURNAL   Biochem. J. 76 (1960) 556-62.
  ORGANISM  Pisum sativum
ORTHOLOGY   KO: K03672  thioredoxin 2
            KO: K04084  thiol:disulfide interchange protein DsbD
            KO: K05905  protein-disulfide reductase
GENES       ECO: b2582(trxC) b4136(dsbD)
            ECJ: JW2566(trxC) JW5734(dipZ)
            ECE: Z3867(trxC) Z5741(dsbD)
            ECS: ECs3448 ECs5117
            ECC: c3107(trxC) c5218(dsbD)
            ECI: UTI89_C2905(trxC) UTI89_C4733(dsbD)
            ECP: ECP_2584 ECP_4380
            ECV: APECO1_2252(dsbD) APECO1_3950(trxC)
            ECW: EcE24377A_4691(dsbD)
            ECX: EcHS_A4377
            STY: STY2842(yfiG) STY4682(dsbD)
            STT: t0261(yfiG) t4374(dsbD)
            SPT: SPA0268(yfiG) SPA4139(dsbD)
            SEC: SC2654(trxC) SC4201(dsbD)
            STM: STM2649(trxC) STM4323(dsbD)
            YPE: YPO0345(dsbD) YPO3270(trxC)
            YPK: y0603(dsbD) y0919(trxC)
            YPM: YP_0499(dsbD) YP_0661(trxC)
            YPA: YPA_2761 YPA_3937
            YPN: YPN_0826 YPN_3325
            YPP: YPDSF_3628
            YPS: YPTB0399(dsbD) YPTB0853(trxC)
            YPI: YpsIP31758_3681(dsbD)
            SFL: SF2644(trxC) SF4290(dsbD)
            SFX: S2817(trxC) S4557(dsbD)
            SFV: SFV_2645(trxC) SFV_4292(dsbD)
            SSN: SSON_2708(trxC) SSON_4319(dsbD)
            SBO: SBO_2614(trxC) SBO_4319(dsbD)
            SDY: SDY_2825(trxC) SDY_4441(dsbD)
            ECA: ECA0618(dsbD) ECA3517(trxC)
            PLU: plu4139(dsbD)
            SGL: SG0301 SG1909
            ENT: Ent638_0323
            SPE: Spro_0403
            HIN: HI0885(dsbD)
            HIT: NTHI1048(dsbD)
            HIP: CGSHiEE_07605(dipZ)
            HDU: HD0807(dsbD)
            HSO: HS_0712(dsbD)
            PMU: PM0221(dsbD_1)
            MSU: MS1299(trxA)
            APL: APL_1359(dsbD)
            ASU: Asuc_1145
            XFA: XF0620
            XFT: PD1535(dsbD)
            XCC: XCC0519(dsbD) XCC1180(trx)
            XCB: XC_0531 XC_3062
            XCV: XCV0567 XCV1327 XCV2308
            XAC: XAC0534(dsbD) XAC1277(trx)
            XOO: XOO0561(dsbD)
            XOM: XOO_0524(XOO0524)
            VCH: VC2701(dsbD) VCA0752
            VVU: VV1_1247 VV2_0350
            VVY: VV3120 VVA0907
            VPA: VP2865(dsbD) VPA0972
            VFI: VF0909 VF2356(dsbD)
            PPR: PBPRB1491 PBPRB1771
            PAE: PA2478 PA4845(dipZ)
            PAU: PA14_32590(dipZ2) PA14_64080(dipZ)
            PPU: PP_0561(dsbD-1) PP_4235(dsbD-2) PP_5069(trxC)
            PPF: Pput_0600 Pput_1629
            PST: PSPTO_4858(dsbD)
            PSB: Psyr_4398
            PSP: PSPPH_4441(dsbD)
            PFL: PFL_0482 PFL_4182
            PFO: Pfl_0443 Pfl_0621 Pfl_3936
            PEN: PSEEN0368 PSEEN1818(dsbD-2) PSEEN4854(dsbD-1)
            PMY: Pmen_0716
            PAR: Psyc_1789
            PCR: Pcryo_0259 Pcryo_2066
            ACI: ACIAD3140(thi3) ACIAD3532(dsbD)
            SON: SO_0452(trxC) SO_0696(dsbD)
            SDN: Sden_0416
            SFR: Sfri_0867 Sfri_3666
            SAZ: Sama_0538 Sama_0738
            SBL: Sbal_0428 Sbal_3726
            SBM: Shew185_0636
            SLO: Shew_3266
            SPC: Sputcn32_3247
            SSE: Ssed_4015
            SPL: Spea_0583
            SHE: Shewmr4_0456 Shewmr4_3406
            SHM: Shewmr7_0546 Shewmr7_3573
            SHN: Shewana3_0452 Shewana3_3576
            SHW: Sputw3181_0551 Sputw3181_0694
            ILO: IL0066(trxC) IL2283(dsbD)
            CPS: CPS_0953(dsbD) CPS_2236(trx2)
            PHA: PSHAa0263(dsbD)
            PAT: Patl_0084 Patl_0420
            SDE: Sde_0814 Sde_1181
            MAQ: Maqu_1778 Maqu_2977
            CBU: CBU_1723(dsbD)
            CBD: COXBU7E912_0281(dsbD)
            LPN: lpg0686(dsbD) lpg1680(dsbD)
            LPF: lpl0722(dsbD)
            LPP: lpp0741(dsbD) lpp1653
            MCA: MCA1041 MCA2134(trxA-2)
            TCX: Tcr_0102 Tcr_0446
            NOC: Noc_1055
            AEH: Mlg_0022
            HCH: HCH_02282(dsbD) HCH_06554(trxB2)
            CSA: Csal_2592
            ABO: ABO_2007(dsbD)
            AHA: AHA_0785(dsbD) AHA_2429
            DNO: DNO_0418(dsbD)
            RMA: Rmag_1057
            VOK: COSY_0956(dsbD)
            NME: NMB1519(dsbD)
            NMA: NMA1719
            NGO: NGO0978
            CVI: CV_2353(dsbD)
            RSO: RSc2990(dsbD)
            REU: Reut_A3151
            REH: H16_A3455(dsbD)
            RME: Rmet_2394 Rmet_3288
            BMA: BMA2602
            BXE: Bxe_A0343
            BVI: Bcep1808_0359 Bcep1808_7178
            BUR: Bcep18194_A3476
            BCN: Bcen_2730
            BCH: Bcen2424_0377
            BAM: Bamb_0296 Bamb_1975
            BPS: BPSL3184(dsbD)
            BPM: BURPS1710b_3747(dsbD)
            BTE: BTH_I3039 BTH_II0054
            PNU: Pnuc_0081
            BPE: BP3646
            BPA: BPP0061
            BBR: BB0061
            RFR: Rfer_1123
            POL: Bpro_3369 Bpro_3506
            MPT: Mpe_A3415
            HAR: HEAR3138(dsbD)
            NEU: NE2389(dsbD)
            NET: Neut_0846
            NMU: Nmul_A0053 Nmul_A2683
            EBA: ebA3571(cutA2) ebA4178(trxC)
            AZO: azo0193(trxC1)
            DAR: Daro_0928 Daro_4167
            TBD: Tbd_2401 Tbd_2559(dsbD) Tbd_2790(dsbD)
            MFA: Mfla_0028 Mfla_1161
            HPA: HPAG1_0810 HPAG1_1457
            TDN: Tmden_0898 Tmden_2099
            CJE: Cj0603c(dsbD)
            CJR: CJE0706(dsbD)
            CJJ: CJJ81176_0631(dsbD)
            CJU: C8J_0565(dsbD)
            CJD: JJD26997_1067(dsbD)
            CFF: CFF8240_1087
            CCV: CCV52592_1494
            CHA: CHAB381_0980
            ABU: Abu_0457 Abu_1880(trx1) Abu_2091(trx2) Abu_2187(dsbD)
            NIS: NIS_1116(dsbD)
            SUN: SUN_1858
            GSU: GSU3446
            DVU: DVU0999
            DDE: Dde_1301 Dde_3416
            LIP: LI0433(dsbD)
            BBA: Bd0175(trx) Bd3255(dsbD)
            ADE: Adeh_0591 Adeh_3508
            MXA: MXAN_4999(dbsD)
            SAT: SYN_01815
            SFU: Sfum_4096
            MLO: mll6589
            MES: Meso_2259
            BJA: blr5775
            RPA: RPA0373(trxC)
            RPB: RPB_0448
            RPD: RPD_2375 RPD_4244
            SIL: SPO0442
            HNE: HNE_2426 HNE_3155
            SAL: Sala_0405
            GBE: GbCGDNIH1_0148
            MGM: Mmc1_0456
            CBO: CBO3434(trxC)
            DSY: DSY4141
            CJK: jk2056(trxA)
            RHA: RHA1_ro06703
            SMA: SAV7242(trxA2)
            LIL: LA1321(dsbD)
            LIC: LIC12404(dsbD)
            LBJ: LBJ_1993(dsbD)
            LBL: LBL_1057(dsbD)
            SYG: sync_2327
            GFO: GFO_1278(dsbD) GFO_3022(dsbD)
            FPS: FP1627(dsbD)
            CTE: CT1075(dsbD)
            CCH: Cag_1683(dsbD)
            PVI: Cvib_0573
            PLT: Plut_0520 Plut_1568
            DRA: DR_A0164
            DGE: Dgeo_2518
            TTH: TTC1117
            TTJ: TTHA1481
STRUCTURES  PDB: 1UC7  1VRS  1Z5Y  2FWE  2FWF  2FWG  2FWH  2PPT  
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.1.8
            ExPASy - ENZYME nomenclature database: 1.8.1.8
            ExplorEnz - The Enzyme Database: 1.8.1.8
            ERGO genome analysis and discovery system: 1.8.1.8
            BRENDA, the Enzyme Database: 1.8.1.8
            CAS: 9029-19-0
///
ENTRY       EC 1.8.1.9                  Enzyme
NAME        thioredoxin-disulfide reductase;
            NADP-thioredoxin reductase;
            NADPH-thioredoxin reductase;
            thioredoxin reductase (NADPH);
            NADPH2:oxidized thioredoxin oxidoreductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     thioredoxin:NADP+ oxidoreductase
REACTION    thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+ [RN:R02016]
ALL_REAC    R02016
SUBSTRATE   thioredoxin [CPD:C00342];
            NADP+ [CPD:C00006]
PRODUCT     thioredoxin disulfide [CPD:C00343];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:14245401]
  AUTHORS   MOORE EC, REICHARD P, THELANDER L.
  TITLE     ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES.V. PURIFICATION AND
            PROPERTIES OF THIOREDOXIN REDUCTASE FROM ESCHERICHIA COLI B.
  JOURNAL   J. Biol. Chem. 239 (1964) 3445-52.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4149839]
  AUTHORS   Speranza ML, Ronchi S, Minchiotti L.
  TITLE     Purification and characterization of yeast thioredoxin reductase.
  JOURNAL   Biochim. Biophys. Acta. 327 (1973) 274-81.
  ORGANISM  Escherichia coli [GN:eco], Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:11012661]
  AUTHORS   Arner ES, Holmgren A.
  TITLE     Physiological functions of thioredoxin and thioredoxin reductase.
  JOURNAL   Eur. J. Biochem. 267 (2000) 6102-9.
  ORGANISM  Escherichia coli [GN:eco], human [GN:hsa]
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K00384  thioredoxin reductase (NADPH)
GENES       HSA: 10587(TXNRD2) 7296(TXNRD1)
            PTR: 467112(TXNRD1)
            MMU: 26462(Txnrd2) 50493(Txnrd1)
            RNO: 50551(Txnrd2) 58819(Txnrd1)
            CFA: 474536(TXNRD1) 608155(TXNRD2)
            BTA: 282389(TXNRD2)
            SSC: 397299(TXNRD1)
            GGA: 416782(TXNRD2)
            XLA: 379744(txnrd2)
            DRE: 352924(txnrd1)
            SPU: 593150(LOC593150)
            DME: Dmel_CG11401(Trxr-2) Dmel_CG2151(Trxr-1)
            CEL: C06G3.7(trxr-1)
            ATH: AT4G35460(NTR1)
            OSA: 4330505 4340912
            CME: CMI298C
            SCE: YDR353W(TRR1) YHR106W(TRR2)
            AGO: AGOS_ACL109C
            PIC: PICST_59792(TRR1)
            CAL: CaO19_4290(CaO19.4290) CaO19_7611(CaO19.7611)
            CGR: CAGL0A02530g CAGL0I01166g
            SPO: SPBC3F6.03
            ANI: AN3581.2
            AFM: AFUA_4G12990
            AOR: AO090009000289
            CNE: CNF01260
            ECU: ECU02_0940
            DDI: DDB_0231235(trrA)
            PFA: PFI1170c
            CPV: cgd2_4320
            CHO: Chro.20464
            TAN: TA04645
            TPV: TP03_0110
            EHI: 23.t00001 386.t00003
            ECO: b0888(trxB)
            ECJ: JW0871(trxB)
            ECE: Z1232(trxB)
            ECS: ECs0973
            ECC: c1025(trxB)
            ECI: UTI89_C0903(trxB)
            ECP: ECP_0902
            ECV: APECO1_1201(trxB)
            ECW: EcE24377A_0962(trxB)
            ECX: EcHS_A0992(trxB)
            STY: STY0956(trxB)
            STT: t1976(trxB)
            SPT: SPA1840(trxB)
            SEC: SC0912(trxB)
            STM: STM0958(trxB)
            YPE: YPO1374(trxB)
            YPK: y2802(trxB)
            YPM: YP_1219(trxB)
            YPA: YPA_0664
            YPN: YPN_2606
            YPP: YPDSF_2321
            YPS: YPTB1399(trxB)
            YPI: YpsIP31758_2598(trxB)
            YEN: YE1523(trxB)
            SFL: SF0847(trxB)
            SFX: S0888(trxB)
            SFV: SFV_0879(trxB)
            SSN: SSON_0889(trxB)
            SBO: SBO_0821(trxB)
            SDY: SDY_2373(trxB)
            ECA: ECA2649
            PLU: plu1599(trxB)
            BUC: BU314(trxB)
            BAS: BUsg304(trxB)
            BAB: bbp291(trxB)
            BCC: BCc_194(trxB) BCc_386(trxA)
            WBR: WGLp492(trxB)
            SGL: SG1106
            ENT: Ent638_1412
            KPN: KPN_00920(trxB)
            BFL: Bfl387(trxB)
            BPN: BPEN_398(trxB)
            HIN: HI1158(trxB)
            HIT: NTHI1327(trxB)
            HDU: HD0333(trxB)
            HSO: HS_1148(trxB)
            PMU: PM0573(trxB)
            MSU: MS0951(trxB)
            APL: APL_0084(trxB)
            XFA: XF1448
            XFT: PD0669(trxB)
            XCC: XCC1084(trxB) XCC1971(trxB)
            XCB: XC_2214 XC_3165
            XCV: XCV1208 XCV2055(trxB1) XCV2311(trxB2)
            XAC: XAC1182(trxB) XAC2005(trxB)
            XOO: XOO2547(trxB)
            XOM: XOO_2406(XOO2406)
            VCH: VC1182
            VCO: VC0395_A0803(trxB)
            VVU: VV1_2810
            VVY: VV1455
            VPA: VP1251
            VFI: VF0902
            PPR: PBPRA1159 PBPRB1551
            PAE: PA0849(trxB2) PA2616(trxB1)
            PAU: PA14_30280(trxB1) PA14_53290(trxB2)
            PAP: PSPA7_2591(trxB2) PSPA7_4671(trxB1)
            PPU: PP_0786(trxB)
            PST: PSPTO_1178(trxB)
            PSB: Psyr_1016
            PSP: PSPPH_1067(trxB)
            PFL: PFL_0945(trxB) PFL_3881(trxB)
            PFO: Pfl_0887
            PEN: PSEEN0924(trxB)
            PMY: Pmen_0978 Pmen_2389
            PAR: Psyc_0388(trxB)
            PCR: Pcryo_0429
            ACI: ACIAD0890(trxB)
            SON: SO_2303(trxB)
            SDN: Sden_1713
            SFR: Sfri_1932
            SAZ: Sama_1769
            SBL: Sbal_2152
            SLO: Shew_2028
            SPC: Sputcn32_2014
            SHE: Shewmr4_1959
            SHM: Shewmr7_2017
            SHN: Shewana3_2047 Shewana3_2096
            SHW: Sputw3181_1998
            ILO: IL0670(trxB)
            CPS: CPS_1923 CPS_2762(trxB)
            PHA: PSHAa1720(trxB)
            PAT: Patl_2370
            SDE: Sde_1692
            PIN: Ping_2209
            MAQ: Maqu_1753
            CBU: CBU_1193(trxB)
            CBD: COXBU7E912_1283(trxB)
            LPN: lpg1767(trxB1)
            LPF: lpl1731(trxB)
            LPP: lpp1731(trxB)
            MCA: MCA1694(trxB)
            FTU: FTT0489c(trxB)
            FTF: FTF0489c(trxB)
            FTW: FTW_1580(trxB)
            FTL: FTL_1571
            FTH: FTH_1519(trxB)
            FTA: FTA_1656(trxB)
            FTN: FTN_0580(trxB)
            TCX: Tcr_0763
            NOC: Noc_0345
            AEH: Mlg_0248
            HHA: Hhal_2289
            HCH: HCH_02344(trxB1)
            CSA: Csal_2959
            ABO: ABO_1289(trxB)
            MMW: Mmwyl1_3225
            AHA: AHA_1863(trxB)
            DNO: DNO_1099(trxB)
            BCI: BCI_0321(trxB)
            VOK: COSY_0047(trxB)
            NME: NMB1324
            NMA: NMA1538(trxB)
            NMC: NMC1261(trxB)
            NGO: NGO0580
            CVI: CV_1895 CV_2813(trxB)
            RSO: RSc1139(RS04614) RSc2342(trxB)
            REU: Reut_A2287 Reut_A2601 Reut_B4454
            REH: H16_A0753 H16_A1199(trxB1) H16_A1779 H16_A2592(trxB2)
                 H16_B1092 H16_B1422
            RME: Rmet_0684 Rmet_1063 Rmet_1922 Rmet_2452 Rmet_4894
            BMA: BMA2123(trxB)
            BMV: BMASAVP1_A0789(trxB)
            BML: BMA10299_A2621(trxB)
            BMN: BMA10247_1991(trxB)
            BXE: Bxe_A2024 Bxe_A3442 Bxe_B2987
            BVI: Bcep1808_6377
            BUR: Bcep18194_A4077 Bcep18194_A4965 Bcep18194_B1954
            BCN: Bcen_0495 Bcen_3172
            BCH: Bcen2424_0974 Bcen2424_5196
            BAM: Bamb_0834
            BPS: BPSL2605(trxB)
            BPM: BURPS1710b_3078(trxB)
            BPL: BURPS1106A_3045(trxB)
            BPD: BURPS668_2991(trxB)
            BTE: BTH_I1560(trxB) BTH_II1477
            PNU: Pnuc_0689
            BPE: BP2474(trxB)
            BPA: BPP3463(trxB) BPP4293(trxB)
            BBR: BB3912(trxB) BB4880(trxB)
            RFR: Rfer_2462 Rfer_3179
            POL: Bpro_2333 Bpro_3801
            PNA: Pnap_3213
            AAV: Aave_3427
            AJS: Ajs_1360 Ajs_3383
            VEI: Veis_1758
            MPT: Mpe_A1118 Mpe_A1496
            HAR: HEAR1017(trxB)
            MMS: mma_1153(trxB)
            NEU: NE1929(trxB)
            NET: Neut_0792
            NMU: Nmul_A0023 Nmul_A1516
            EBA: ebA7042(trxB)
            AZO: azo0452(trxB1) azo1030(trxA1) azo1363(trxB2) azo1635
                 azo2490(txn) azo2658(trxA2) azo3700(trxC2)
            DAR: Daro_1293
            TBD: Tbd_1001
            MFA: Mfla_1119
            HPY: HP0825(trxB) HP1164(trxB)
            HPJ: jhp0764(trxB_1) jhp1091(trxB_2)
            HPA: HPAG1_0811 HPAG1_1103
            HHE: HH0486(trxB_1) HH1153(trxB_2)
            HAC: Hac_0729(trxB) Hac_1331(trxB)
            WSU: WS0327(trxB_2) WS0454(trxB)
            TDN: Tmden_1869
            CJE: Cj0146c(trxB)
            CJR: CJE0142(trxB)
            CJJ: CJJ81176_0182(trxB)
            CJU: C8J_0143(trxB)
            CJD: JJD26997_0161(trxB)
            CFF: CFF8240_0296(trxB)
            CCV: CCV52592_0124 CCV52592_0838(trxB)
            CHA: CHAB381_0214(trxB)
            CCO: CCC13826_1140(trxB) CCC13826_1380
            ABU: Abu_0004 Abu_2090(trxB)
            NIS: NIS_1549(trxB) NIS_1734
            SUN: SUN_0234(trxB) SUN_0563
            GSU: GSU0488(trxB)
            GME: Gmet_3070
            GUR: Gura_4032
            PCA: Pcar_0114 Pcar_2943
            PPD: Ppro_3328
            DVU: DVU0283 DVU0377(trxB-1) DVU1457 DVU1838(trxB-2)
            DVL: Dvul_1324 Dvul_1622
            DDE: Dde_0210 Dde_0465 Dde_1203 Dde_2066 Dde_2151
            LIP: LI0366(trxB)
            BBA: Bd0373(trxB)
            DPS: DP0809
            ADE: Adeh_3951
            AFW: Anae109_0473 Anae109_3313 Anae109_3360
            MXA: MXAN_1954(trxB)
            SAT: SYN_01439
            SFU: Sfum_0698 Sfum_1709
            RPR: RP445(trxB1) RP514(trxB2)
            RTY: RT0432(trxB1) RT0500(trxB2)
            RCO: RC0618(trxB1) RC0637(trxB2)
            RFE: RF_0681(trxB1) RF_0700(trxB2)
            RBE: RBE_0445(trxB1) RBE_0982(trxB2)
            RCM: A1E_03100
            OTS: OTBS_0016(trxB1) OTBS_1841(trxB2)
            WOL: WD0755(trxB) WD0982
            WBM: Wbm0566 Wbm0685
            AMA: AM510(trxB) AM617(trxB2)
            APH: APH_0658(trxB) APH_0734
            ERU: Erum3470(trxB) Erum4020
            ERW: ERWE_CDS_03540(trxB) ERWE_CDS_04150(trxB2)
            ERG: ERGA_CDS_03500(trxB) ERGA_CDS_04100(trxB2)
            ECN: Ecaj_0331 Ecaj_0391
            ECH: ECH_0649 ECH_0735(trxB)
            NSE: NSE_0558(trxB) NSE_0779
            PUB: SAR11_0077(trxB) SAR11_0627(trxB2)
            MLO: mll0792 mll2552
            MES: Meso_2112
            SME: SMc01224(trxB)
            SMD: Smed_1248
            ATU: Atu2185(trxB)
            ATC: AGR_C_3970(trxR)
            RET: RHE_CH02975(trxBch) RHE_PF00137(trxBf)
            RLE: RL3428(trxB) pRL110062
            BME: BMEI0512 BMEI0958
            BMF: BAB1_1518(trxB)
            BMS: BR1499(trxB)
            BMB: BruAb1_1492(trxB)
            BOV: BOV_1450(trxB)
            BJA: bll5883 blr7381(trxB)
            BRA: BRADO1321(trxB) BRADO1584 BRADO5079 BRADO6640
            BBT: BBta_0894 BBta_5550 BBta_6803(trxB)
            RPA: RPA3954 RPA4075(trxB)
            RPB: RPB_1512 RPB_3841 RPB_4356
            RPC: RPC_1458 RPC_3838 RPC_4421
            RPD: RPD_1453 RPD_1645
            RPE: RPE_1478 RPE_3643 RPE_3964 RPE_4494
            NWI: Nwi_1089 Nwi_2453
            NHA: Nham_1321 Nham_2880
            BHE: BH11660(trxB)
            BQU: BQ09280(trxB)
            BBK: BARBAKC583_0981(trxB)
            CCR: CC_2871
            SIL: SPO0903(trxB)
            SIT: TM1040_0614
            RSP: RSP_1576(trxB)
            RSH: Rsph17029_0228
            JAN: Jann_2058 Jann_3338
            RDE: RD1_3505(trxB)
            MMR: Mmar10_2145
            HNE: HNE_0548(trxB)
            ZMO: ZMO1142(trxB)
            NAR: Saro_2343
            SAL: Sala_0145
            ELI: ELI_02155 ELI_04700
            GOX: GOX0131 GOX0631
            GBE: GbCGDNIH1_0720 GbCGDNIH1_2006
            ACR: Acry_2441
            RRU: Rru_A1417 Rru_A2898 Rru_A3439
            MAG: amb0663 amb3892
            MGM: Mmc1_0414
            ABA: Acid345_1337 Acid345_1748
            SUS: Acid_0437 Acid_1030
            BSU: BG12018(ycgT) BG12391(yumC) BG12398(trxB)
            BHA: BH3408 BH3571(trxB)
            BAN: BA0352 BA1515 BA5160 BA5387(trxB)
            BAR: GBAA0352 GBAA1515 GBAA5160 GBAA5387(trxB)
            BAA: BA_0033 BA_0245 BA_0924 BA_2037
            BAT: BAS0337 BAS1405 BAS4797 BAS5007
            BCE: BC0385 BC1495 BC4926 BC5159
            BCA: BCE_0452 BCE_1621 BCE_5065 BCE_5262(trxB)
            BCZ: BCZK0324(trxB) BCZK1376(trxB) BCZK4658(trxB) BCZK4851(trxB)
            BCY: Bcer98_3539
            BTK: BT9727_0321(trxB) BT9727_1377(trxB) BT9727_4639(trxB)
                 BT9727_4836(trxB)
            BTL: BALH_0343(trxB) BALH_1350(trxB) BALH_2487(trxB)
                 BALH_4465(trxB) BALH_4650(trxB)
            BLI: BL02042 BL03143(yumC) BL03415(trxB)
            BLD: BLi02810(ycgT) BLi03393(yumC) BLi03728(trxB)
            BCL: ABC0094 ABC2925 ABC3038(trxB)
            BAY: RBAM_032010(trxB)
            BPU: BPUM_0664 BPUM_0777(ycgT) BPUM_3117(trxB)
            OIH: OB0186 OB2351 OB2469
            GKA: GK2954 GK3068
            SAU: SA0719(trxB) SA2162
            SAV: SAV0764(trxB) SAV2372
            SAM: MW0726(trxB) MW2294
            SAR: SAR0818(trxB) SAR2461
            SAS: SAS0729 SAS2264
            SAC: SACOL0829(trxB) SACOL2369
            SAB: SAB0717(trxB) SAB1245c SAB2252c
            SAA: SAUSA300_0747(trxB) SAUSA300_1369 SAUSA300_2319
            SAO: SAOUHSC_00785 SAOUHSC_02654
            SEP: SE0547
            SER: SERP0432(trxB)
            SHA: SH0681 SH2125(trxB)
            SSP: SSP0530 SSP1953
            LMO: lmo1961 lmo2390 lmo2478(trxB)
            LMF: LMOf2365_1991 LMOf2365_2364 LMOf2365_2451(trxB)
            LIN: lin2075 lin2489 lin2621(trxB)
            LWE: lwe1188(trxA) lwe1987 lwe2338 lwe2426(trxB)
            LLA: L00196(trxB2) L0196(trxB1)
            LLC: LACR_1013 LACR_1811
            LLM: llmg_0776(trxB2) llmg_1588(trxB1)
            SPY: SPy_0850
            SPZ: M5005_Spy_0657(trxB) M5005_Spy_1360
            SPM: spyM18_0909(trxB) spyM18_1666(trxB)
            SPG: SpyM3_0575 SpyM3_1395(nox.2)
            SPS: SPs0467 SPs1279
            SPH: MGAS10270_Spy0716(trxB) MGAS10270_Spy1477
            SPI: MGAS10750_Spy0748(trxB) MGAS10750_Spy1469
            SPJ: MGAS2096_Spy0727(trxB) MGAS2096_Spy1382
            SPK: MGAS9429_Spy0712(trxB) MGAS9429_Spy1356
            SPA: M6_Spy0676 M6_Spy1406
            SPB: M28_Spy0638(trxB) M28_Spy1401
            SPN: SP_1458 SP_1563
            SPR: spr1312(trxB) spr1421(trxB)
            SPD: SPD_1287(trxB) SPD_1393
            SAG: SAG0294(trxB) SAG1353
            SAN: gbs0284 gbs1423
            SAK: SAK_0366(trxB) SAK_1384
            SMU: SMU.463(trxB) SMU.869(trxB2)
            STC: str1417(trxB2) str1650(trxB1)
            STL: stu1417(trxB2)
            SSA: SSA_0813 SSA_1865
            SSU: SSU05_1986
            SGO: SGO_0581(trxB) SGO_1284
            LPL: lp_0761(trxB1) lp_2585(trxB2)
            LJO: LJ0501 LJ0852
            LAC: LBA0439 LBA0679(trxB) LBA1898(trxR)
            LSA: LSA0403 LSA0435(trxB1) LSA0520(trxB2)
            LSL: LSL_0439(trxB) LSL_1722(trxB)
            LDB: Ldb0613(trxB1) Ldb1586(trxB2)
            LBU: LBUL_0548 LBUL_1466
            LBR: LVIS_0645 LVIS_1813
            LCA: LSEI_0826 LSEI_0948
            LGA: LGAS_0447
            EFA: EF1338(trxB) EF2738 EF2899
            OOE: OEOE_0566
            STH: STH1072 STH1762 STH2872 STH965
            CAC: CAC0869
            CPE: CPE0783 CPE2440
            CPF: CPF_2750(trxB)
            CPR: CPR_2349 CPR_2436(trxB)
            CTC: CTC00842 CTC02552
            CNO: NT01CX_1159(trxB) NT01CX_2374
            CTH: Cthe_1945
            CDF: CD1691(trxB1) CD2117(trxB2) CD2356(trxB3)
            CBO: CBO1254(trxB1) CBO1259(trxB2) CBO3433(trxB3)
            CBA: CLB_1287(trxB)
            CBH: CLC_1298(trxB)
            CBF: CLI_1344(trxB)
            CBE: Cbei_0778
            CKL: CKL_0311(trxR)
            CHY: CHY_0560 CHY_0906(trxB1) CHY_2389(trxB2)
            DSY: DSY0525 DSY1359 DSY4463 DSY4471
            DRM: Dred_1749
            SWO: Swol_1300 Swol_2471
            CSC: Csac_0533
            TTE: TTE1881(trxB) TTE2220(trxB2)
            MTA: Moth_2420
            MGE: MG_102(trxB)
            MPN: MPN240(trxB)
            MPU: MYPU_7130(trxB)
            MPE: MYPE1390(trxB) MYPE9330(trxB)
            MGA: MGA_0124(trxB) MGA_1221(trxB)
            MMY: MSC_0938(trxB)
            MMO: MMOB1840(trxB)
            MHY: mhp281(trxB)
            MHJ: MHJ_0095(trxB)
            MHP: MHP7448_0098(trxB)
            MSY: MS53_0596(trxB)
            MCP: MCAP_0779(trxB)
            UUR: UU074(trxB)
            MFL: Mfl064
            MTU: Rv3913(trxB2)
            MTC: MT4032(trxB)
            MBO: Mb3944(trxB2)
            MBB: BCG_0019(trxB2_2) BCG_3971(trxB2_1)
            MLE: ML2703(trxB)
            MPA: MAP4339(trxB2)
            MAV: MAV_5301(trxB)
            MSM: MSMEG_1516 MSMEG_6933(trxB)
            MVA: Mvan_1371
            MGI: Mflv_5003
            MMC: Mmcs_1070 Mmcs_3340 Mmcs_5402
            MKM: Mkms_1086
            MJL: Mjls_1097
            CGL: NCgl0663(cgl0693) NCgl2984(cgl3090)
            CGB: cg3422(trxB)
            CEF: CE2933
            CDI: DIP2373(trxB)
            CJK: jk2093(trxB)
            NFA: nfa56620
            RHA: RHA1_ro03650 RHA1_ro04004 RHA1_ro04104 RHA1_ro06701
                 RHA1_ro09062(trxB)
            SCO: SCO3890(SCH24.12c) SCO6834(trxB2)
            SMA: SAV4305(trxB1)
            LXX: Lxx25220(trxB)
            CMI: CMM_1109(trxB2) CMM_2967(trxB1) CMM_2968(trxA)
            AAU: AAur_3629(trxB) AAur_4198(trxB) AAur_pTC20059(trxB)
            PAC: PPA2309
            TFU: Tfu_3108
            FRA: Francci3_0530 Francci3_4536
            FAL: FRAAL1022 FRAAL1961 FRAAL6872(trxB)
            KRA: Krad_0457
            SEN: SACE_0284 SACE_0932(yumC) SACE_3636 SACE_6311 SACE_7076
                 SACE_7384(trxB) SACE_7385(trxB)
            BLO: BL0614 BL0649(trxB)
            BAD: BAD_1623(trxB)
            RXY: Rxyl_0229
            FNU: FN1163 FN1984
            RBA: RB1488(trxB) RB7223(trx)
            CTR: CT099(trxB)
            CTA: CTA_0105(trxB)
            CMU: TC0375
            CPN: CPn0314(trxB)
            CPA: CP0444
            CPJ: CPj0314(trxB)
            CPT: CpB0322
            CCA: CCA00468(trxB)
            CAB: CAB454(trxB)
            CFE: CF0539(trxB)
            PCU: pc1713(trxB)
            BBU: BB0515(trxB)
            BGA: BG0526(trxB)
            BAF: BAPKO_0542(trxB)
            TPA: TP0814
            TDE: TDE0743(trxB)
            LIL: LA2494
            LIC: LIC11470(trxB)
            LBJ: LBJ_1491(trxB)
            LBL: LBL_1715(trxB)
            SYN: slr0600
            SYW: SYNW0687
            SYC: syc0901_c(trxB)
            SYF: Synpcc7942_0623
            SYD: Syncc9605_1583 Syncc9605_1981
            SYE: Syncc9902_0680 Syncc9902_2006
            SYG: sync_0910(trxB) sync_1951
            SYR: SynRCC307_1683(trxB)
            SYX: SynWH7803_1634(trxB)
            CYA: CYA_1362(trxB)
            CYB: CYB_2806(trxB)
            TEL: tll1924
            GVI: gll2934 glr0719
            ANA: all0737 all4510 alr2204
            AVA: Ava_3376 Ava_4637
            PMA: Pro0239(trxB) Pro1245(trxB)
            PMM: PMM0211(trxB) PMM1150
            PMT: PMT1551
            PMN: PMN2A_0758 PMN2A_1578
            PMI: PMT9312_0213 PMT9312_1247
            PMB: A9601_02291 A9601_13251
            PMC: P9515_02401 P9515_13151
            PMF: P9303_03841
            PMG: P9301_02311 P9301_13401
            PME: NATL1_02881 NATL1_15981
            TER: Tery_1699
            BTH: BT_4336
            BFR: BF1035
            BFS: BF0952(trxB)
            PGI: PG1134(trxB)
            SRU: SRU_2658(trxB)
            CHU: CHU_1778(trxB)
            GFO: GFO_0125(trxB) GFO_0330(trxB) GFO_0987
            FPS: FP0615(trxB1) FP1670(trxB2)
            CTE: CT0842(trxB) CT1512
            CCH: Cag_0944 Cag_1151
            PVI: Cvib_1011
            PLT: Plut_1260 Plut_1516
            DET: DET0542(trxB)
            DEH: cbdb_A516(trxB)
            DRA: DR_1982 DR_2623
            DGE: Dgeo_1013 Dgeo_1576 Dgeo_2331 Dgeo_2772
            TTH: TTC0096 TTC0853 TTC1555
            TTJ: TTHA0465 TTHA1920
            AAE: aq_500(trxB)
            TMA: TM0869
            MJA: MJ1536(trxB)
            MMP: MMP0959(trxB)
            MAC: MA1368
            MBA: Mbar_A2898
            MMA: MM_2353
            MBU: Mbur_0101
            MTP: Mthe_1150
            MTH: MTH708
            MST: Msp_1413
            MSI: Msm_0340
            MKA: MK1561(trxB)
            AFU: AF1554(trxB)
            HAL: VNG1259G(trxB2) VNG6074G(trxB1_1) VNG6075G(trh_1)
                 VNG6451G(trh_2) VNG6452G(trxB1_2)
            HMA: pNG7078(trxB1) rrnAC1129(trxB3) rrnAC1470(trxB2)
            HWA: HQ1592A(trxB) HQ1652A(trxB)
            NPH: NP2680A(trxB_1)
            TAC: Ta0984
            TVO: TVN1129
            PTO: PTO0431 PTO0734
            PHO: PH1426
            PAB: PAB0500(trxB)
            PFU: PF1422
            TKO: TK2100
            RCI: RRC232(trxB-1) RRC321(trxB-2)
            APE: APE_1061.1
            HBU: Hbut_0180
            SSO: SSO2222(trxB-1) SSO2416(trxB-3) SSO2765(trxB-2)
            STO: ST0438 ST0546 ST2133
            SAI: Saci_0029(trxR) Saci_0931(trxR) Saci_1169(trxB) Saci_2144
            PAI: PAE1725(trxB) PAE2744(trxB)
            PIS: Pisl_1704
            PCL: Pcal_0626
            PAS: Pars_0776
            NEQ: NEQ491
STRUCTURES  PDB: 1NSW  1NW2  1V98  1ZDL  1ZKQ  2A87  2CFY  2J3N  2NVK  2Q0K  
                 2Q0L  
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.1.9
            ExPASy - ENZYME nomenclature database: 1.8.1.9
            ExplorEnz - The Enzyme Database: 1.8.1.9
            ERGO genome analysis and discovery system: 1.8.1.9
            BRENDA, the Enzyme Database: 1.8.1.9
            CAS: 9074-14-0
///
ENTRY       EC 1.8.1.10                 Enzyme
NAME        CoA-glutathione reductase;
            coenzyme A glutathione disulfide reductase;
            NADPH-dependent coenzyme A-SS-glutathione reductase;
            coenzyme A disulfide-glutathione reductase;
            NADPH:CoA-glutathione oxidoreductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     glutathione:NADP+ oxidoreductase (CoA-acylating)
REACTION    CoA + glutathione + NADP+ = CoA-glutathione + NADPH + H+ [RN:R05714]
ALL_REAC    R05714;
            (other) R00116 R00900
SUBSTRATE   CoA [CPD:C00010];
            glutathione [CPD:C00051];
            NADP+ [CPD:C00006]
PRODUCT     CoA-glutathione [CPD:C00920];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein. The substrate is a mixed disulfide. May be identical
            to EC 1.8.1.9, thioredoxin-disulfide reductase.
REFERENCE   1  [PMID:4390951]
  AUTHORS   Ondarza RN, Abney R, Lopez-Colome AM.
  TITLE     Characterization of a NADPH-dependent coenzyme A-SS-glutathione
            reductase from yeast.
  JOURNAL   Biochim. Biophys. Acta. 191 (1969) 239-48.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:4151341]
  AUTHORS   Ondarza RN, Escamilla E, Gutierrez J, De la Chica G.
  TITLE     CoAS-Sglutathione and GSSG reductases from rat liver. Two disulfide
            oxidoreductase activities in one protein entity.
  JOURNAL   Biochim. Biophys. Acta. 341 (1974) 162-71.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:334266]
  AUTHORS   Carlberg I, Mannervik B.
  TITLE     Purification by affinity chromatography of yeast glutathione
            reductase, the enzyme responsible for the NADPH-dependent reduction
            of the mixed disulfide of coenzyme A and glutathione.
  JOURNAL   Biochim. Biophys. Acta. 484 (1977) 268-74.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00272  Cysteine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.1.10
            ExPASy - ENZYME nomenclature database: 1.8.1.10
            ExplorEnz - The Enzyme Database: 1.8.1.10
            ERGO genome analysis and discovery system: 1.8.1.10
            BRENDA, the Enzyme Database: 1.8.1.10
            CAS: 37256-33-0
///
ENTRY       EC 1.8.1.11                 Enzyme
NAME        asparagusate reductase;
            asparagusate dehydrogenase;
            asparagusic dehydrogenase;
            asparagusate reductase (NADH2);
            NADH2:asparagusate oxidoreductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     3-mercapto-2-mercaptomethylpropanoate:NAD+ oxidoreductase
REACTION    3-mercapto-2-mercaptomethylpropanoate + NAD+ = asparagusate + NADH +
            H+ [RN:R03761]
ALL_REAC    R03761
SUBSTRATE   3-mercapto-2-mercaptomethylpropanoate [CPD:C04371];
            NAD+ [CPD:C00003]
PRODUCT     asparagusate [CPD:C01892];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Also acts on lipoate.
REFERENCE   1  [PMID:1125255]
  AUTHORS   Yanagawa H, Egami F.
  TITLE     Asparagusate dehydrogenases and lipoyl dehydrogenase from asparagus
            mitochondria.
  JOURNAL   Biochim. Biophys. Acta. 384 (1975) 342-52.
  ORGANISM  Asparagus officinalis
REFERENCE   2  [PMID:180003]
  AUTHORS   Yanagawa H, Egami F.
  TITLE     Asparagusate dehydrogenases and lipoyl dehydrogenase from asparagus
            mitochondria. Physical, chemical, and enzymatic properties.
  JOURNAL   J. Biol. Chem. 251 (1976) 3637-44.
  ORGANISM  Asparagus officinalis
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.1.11
            ExPASy - ENZYME nomenclature database: 1.8.1.11
            ExplorEnz - The Enzyme Database: 1.8.1.11
            ERGO genome analysis and discovery system: 1.8.1.11
            BRENDA, the Enzyme Database: 1.8.1.11
            CAS: 56126-52-4
///
ENTRY       EC 1.8.1.12                 Enzyme
NAME        trypanothione-disulfide reductase;
            trypanothione reductase;
            NADPH2:trypanothione oxidoreductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     trypanothione:NADP+ oxidoreductase
REACTION    trypanothione + NADP+ = trypanothione disulfide + NADPH + H+
            [RN:R03821]
ALL_REAC    R03821
SUBSTRATE   trypanothione [CPD:C02090];
            NADP+ [CPD:C00006]
PRODUCT     trypanothione disulfide [CPD:C03170];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016]
COMMENT     Trypanothione disulfide is the oxidized form of
            N1,N8-bis(glutathionyl)-spermidine from the insect-parasitic
            trypanosomatid Crithidia fasciculata. The enzyme from Crithidia
            fasciculata is a flavoprotein (FAD), whose activity is dependent on
            a redox-active cystine at the active centre. (cf. EC 1.8.1.7,
            glutathione-disulfide reductase)
REFERENCE   1  [PMID:3718941]
  AUTHORS   Shames SL, Fairlamb AH, Cerami A, Walsh CT.
  TITLE     Purification and characterization of trypanothione reductase from
            Crithidia fasciculata, a newly discovered member of the family of
            disulfide-containing flavoprotein reductases.
  JOURNAL   Biochemistry. 25 (1986) 3519-26.
  ORGANISM  Crithidia fasciculata
REFERENCE   2  [PMID:9057833]
  AUTHORS   Marsh IR, Bradley M.
  TITLE     Substrate specificity of trypanothione reductase.
  JOURNAL   Eur. J. Biochem. 243 (1997) 690-4.
  ORGANISM  Trypanosoma cruzi [GN:tcr]
REFERENCE   3  [PMID:7607216]
  AUTHORS   Cunningham ML, Fairlamb AH.
  TITLE     Trypanothione reductase from Leishmania donovani. Purification,
            characterisation and inhibition by trivalent antimonials.
  JOURNAL   Eur. J. Biochem. 230 (1995) 460-8.
  ORGANISM  Leishmania donovani
ORTHOLOGY   KO: K04283  trypanothione-disulfide reductase
GENES       TBR: Tb10.406.0520
            TCR: 484299.10 503555.30
            LMA: LmjF05.0350
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.1.12
            ExPASy - ENZYME nomenclature database: 1.8.1.12
            ExplorEnz - The Enzyme Database: 1.8.1.12
            ERGO genome analysis and discovery system: 1.8.1.12
            BRENDA, the Enzyme Database: 1.8.1.12
            CAS: 102210-35-5
///
ENTRY       EC 1.8.1.13                 Enzyme
NAME        bis-gamma-glutamylcystine reductase;
            NADPH2:bis-gamma-glutamylcysteine oxidoreductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     gamma-glutamylcysteine:NADP+ oxidoreductase
REACTION    2 gamma-glutamylcysteine + NADP+ = bis-gamma-glutamylcystine + NADPH
            + H+ [RN:R02742]
ALL_REAC    R02742
SUBSTRATE   gamma-glutamylcysteine [CPD:C00669];
            NADP+ [CPD:C00006]
PRODUCT     bis-gamma-glutamylcystine [CPD:C03646];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Highly specific. Not identical with EC 1.8.1.7
            (glutathione-disulfide reductase) or EC 1.8.1.14 (CoA-disulfide
            reductase).
REFERENCE   1  [PMID:3136140]
  AUTHORS   Sundquist AR, Fahey RC.
  TITLE     The novel disulfide reductase bis-gamma-glutamylcystine reductase
            and dihydrolipoamide dehydrogenase from Halobacterium halobium:
            purification by immobilized-metal-ion affinity chromatography and
            properties of the enzymes.
  JOURNAL   J. Bacteriol. 170 (1988) 3459-67.
  ORGANISM  Halobacterium halobium
REFERENCE   2  [PMID:2910862]
  AUTHORS   Sundquist AR, Fahey RC.
  TITLE     The function of gamma-glutamylcysteine and bis-gamma-glutamylcystine
            reductase in Halobacterium halobium.
  JOURNAL   J. Biol. Chem. 264 (1989) 719-25.
  ORGANISM  Halobacterium halobium
PATHWAY     PATH: map00480  Glutathione metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.1.13
            ExPASy - ENZYME nomenclature database: 1.8.1.13
            ExplorEnz - The Enzyme Database: 1.8.1.13
            ERGO genome analysis and discovery system: 1.8.1.13
            BRENDA, the Enzyme Database: 1.8.1.13
            CAS: 117056-54-9
///
ENTRY       EC 1.8.1.14                 Enzyme
NAME        CoA-disulfide reductase;
            CoA-disulfide reductase (NADH2);
            NADH2:CoA-disulfide oxidoreductase;
            CoA:NAD+ oxidoreductase;
            CoADR;
            coenzyme A disulfide reductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     CoA:NAD(P)+ oxidoreductase
REACTION    2 CoA + NAD(P)+ = CoA-disulfide + NAD(P)H + H+ [RN:R00091 R07175]
ALL_REAC    R00091 R07175
SUBSTRATE   CoA [CPD:C00010];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     CoA-disulfide [CPD:C02015];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     A flavoprotein. Not identical with EC 1.8.1.6 (cystine reductase),
            EC 1.8.1.7 (glutathione-disulfide reductase) or EC 1.8.1.13
            (bis-gamma-glutamylcystine reductase). While the enzyme from
            Staphylococcus aureus has a strong preference for NADPH [3], that
            from the thermophilic Archaea Pyrococcus horikoshii can use both
            NADH and NADPH efficiently [4].
REFERENCE   1  [PMID:410791]
  AUTHORS   Setlow B, Setlow P.
  TITLE     Levels of acetyl coenzyme A, reduced and oxidized coenzyme A, and
            coenzyme A in disulfide linkage to protein in dormant and germinated
            spores and growing and sporulating cells of Bacillus megaterium.
  JOURNAL   J. Bacteriol. 132 (1977) 444-52.
  ORGANISM  Bacillus megaterium
REFERENCE   2  [PMID:9488707]
  AUTHORS   delCardayre SB, Stock KP, Newton GL, Fahey RC, Davies JE.
  TITLE     Coenzyme A disulfide reductase, the primary low molecular weight
            disulfide reductase from Staphylococcus aureus. Purification and
            characterization of the native enzyme.
  JOURNAL   J. Biol. Chem. 273 (1998) 5744-51.
  ORGANISM  Staphylococcus aureus
REFERENCE   3  [PMID:10052943]
  AUTHORS   Luba J, Charrier V, Claiborne A.
  TITLE     Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence
            for asymmetric behavior on interaction with pyridine nucleotides.
  JOURNAL   Biochemistry. 38 (1999) 2725-37.
  ORGANISM  Staphylococcus aureus
REFERENCE   4  [PMID:15720393]
  AUTHORS   Harris DR, Ward DE, Feasel JM, Lancaster KM, Murphy RD, Mallet TC,
            Crane EJ 3rd.
  TITLE     Discovery and characterization of a Coenzyme A disulfide reductase
            from Pyrococcus horikoshii. Implications for this disulfide
            metabolism of anaerobic hyperthermophiles.
  JOURNAL   FEBS. J. 272 (2005) 1189-200.
  ORGANISM  Pyrococcus horikoshii [GN:pho]
ORTHOLOGY   KO: K08255  CoA-disulfide reductase
GENES       AHA: AHA_4075
            SAU: SA0831(cdr)
            SAV: SAV0970(cdr)
            SAM: MW0852(cdr)
            SAR: SAR0933
            SAS: SAS0840
            SAC: SACOL0975
            SAA: SAUSA300_0873(cdr)
            SAO: SAOUHSC_00908
            SEP: SE0669
            SER: SERP0560
            SHA: SH1979(cdr)
            SSP: SSP1804
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.1.14
            ExPASy - ENZYME nomenclature database: 1.8.1.14
            ExplorEnz - The Enzyme Database: 1.8.1.14
            ERGO genome analysis and discovery system: 1.8.1.14
            BRENDA, the Enzyme Database: 1.8.1.14
            CAS: 206770-55-0
///
ENTRY       EC 1.8.1.15                 Enzyme
NAME        mycothione reductase;
            mycothiol-disulfide reductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     mycothiol:NAD(P)+ oxidoreductase
REACTION    2 mycothiol + NAD(P)+ = mycothione + NAD(P)H + H+ [RN:R05715 R05716
            R06289 R06290]
ALL_REAC    R05715 R05716 R06289(G) R06290(G)
SUBSTRATE   mycothiol [CPD:C06717];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     mycothione [CPD:C11502];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Contains FAD. No activity with glutathione, trypanothione or
            coenzyme A as substrate.
REFERENCE   1  [PMID:10512639]
  AUTHORS   Patel MP, Blanchard JS.
  TITLE     Expression, purification, and characterization of Mycobacterium
            tuberculosis mycothione reductase.
  JOURNAL   Biochemistry. 38 (1999) 11827-33.
  ORGANISM  Mycobacterium tuberculosis
REFERENCE   2  [PMID:11318633]
  AUTHORS   Patel MP, Blanchard JS.
  TITLE     Mycobacterium tuberculosis mycothione reductase: pH dependence of
            the kinetic parameters and kinetic isotope effects.
  JOURNAL   Biochemistry. 40 (2001) 5119-26.
  ORGANISM  Mycobacterium tuberculosis
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.1.15
            ExPASy - ENZYME nomenclature database: 1.8.1.15
            ExplorEnz - The Enzyme Database: 1.8.1.15
            ERGO genome analysis and discovery system: 1.8.1.15
            BRENDA, the Enzyme Database: 1.8.1.15
///
ENTRY       EC 1.8.2.1                  Enzyme
NAME        sulfite dehydrogenase;
            sulfite cytochrome c reductase;
            sulfite-cytochrome c oxidoreductase;
            sulfite oxidase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a cytochrome as acceptor
SYSNAME     sulfite:ferricytochrome-c oxidoreductase
REACTION    sulfite + 2 ferricytochrome c + H2O = sulfate + 2 ferrocytochrome c
            + 2 H+ [RN:R00528]
ALL_REAC    R00528
SUBSTRATE   sulfite [CPD:C00094];
            ferricytochrome c [CPD:C00125];
            H2O [CPD:C00001]
PRODUCT     sulfate [CPD:C00059];
            ferrocytochrome c [CPD:C00126];
            H+ [CPD:C00080]
COMMENT     Associated with cytochrome c-551.
REFERENCE   1
  AUTHORS   Charles, A.M. and Suzuki, I.
  TITLE     Purification and properties of sulfite:cytochrome c oxidoreductase
            from Thiobacillus novellus.
  JOURNAL   Biochim. Biophys. Acta 128 (1966) 522-534.
  ORGANISM  Thiobacillus novellus
REFERENCE   2
  AUTHORS   Lu, W.-P. and Kelly, D.P.
  TITLE     Properties and role of sulphite:cytochrome c oxidoreductase purified
            from Thiobacillus versutus (A2).
  JOURNAL   J. Gen. Microbiol. 130 (1984) 1683-1692.
  ORGANISM  Thiobacillus versutus
PATHWAY     PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K05301  sulfite dehydrogenase
GENES       CVI: CV_0158(sorA) CV_0159(sorB)
            REH: H16_A1639(cysI2) H16_A3572(soxC) H16_B2222
            AZO: azo1141(soxF)
            RDE: RD1_1516(soxC)
            TTH: TTC1046(soxC)
            NPH: NP2044A NP2718A
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.2.1
            ExPASy - ENZYME nomenclature database: 1.8.2.1
            ExplorEnz - The Enzyme Database: 1.8.2.1
            ERGO genome analysis and discovery system: 1.8.2.1
            BRENDA, the Enzyme Database: 1.8.2.1
            CAS: 37256-47-6
///
ENTRY       EC 1.8.2.2                  Enzyme
NAME        thiosulfate dehydrogenase;
            tetrathionate synthase;
            thiosulfate oxidase;
            thiosulfate-oxidizing enzyme;
            thiosulfate-acceptor oxidoreductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a cytochrome as acceptor
SYSNAME     thiosulfate:ferricytochrome-c oxidoreductase
REACTION    2 thiosulfate + 2 ferricytochrome c = tetrathionate + 2
            ferrocytochrome c [RN:R00029]
ALL_REAC    R00029
SUBSTRATE   thiosulfate [CPD:C00320];
            ferricytochrome c [CPD:C00125]
PRODUCT     tetrathionate [CPD:C02084];
            ferrocytochrome c [CPD:C00126]
REFERENCE   1
  AUTHORS   Lu, W.-P. and Kelly, D.P.
  TITLE     Cellular location and partial purification of the
            'thiosulphate-oxidizing enzyme' and 'trithionate hydrolase' from
            Thiobacillus tepidarius.
  JOURNAL   J. Gen. Microbiol. 134 (1988) 877-885.
  ORGANISM  Thiobacillus tepidarius
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.2.2
            ExPASy - ENZYME nomenclature database: 1.8.2.2
            ExplorEnz - The Enzyme Database: 1.8.2.2
            ERGO genome analysis and discovery system: 1.8.2.2
            BRENDA, the Enzyme Database: 1.8.2.2
            CAS: 9076-88-4
///
ENTRY       EC 1.8.3.1                  Enzyme
NAME        sulfite oxidase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With oxygen as acceptor
SYSNAME     sulfite:oxygen oxidoreductase
REACTION    sulfite + O2 + H2O = sulfate + H2O2 [RN:R00533]
ALL_REAC    R00533
SUBSTRATE   sulfite [CPD:C00094];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     sulfate [CPD:C00059];
            H2O2 [CPD:C00027]
COFACTOR    Heme [CPD:C00032];
            Molybdenum [CPD:C00150]
COMMENT     A molybdohemoprotein.
REFERENCE   1
  AUTHORS   Kessel, D.L., Johnston, J.L., Cohen, H.J. and Rajagopalan, K.V.
  TITLE     Visualization of hepatic sulfite oxidase in crude tissue preparation
            by electron paramagnetic resonance spectroscopy.
  JOURNAL   Biochim. Biophys. Acta 334 (1974) 86-96.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   MacLeod, R.M., Farkas, W., Fridovitch, I. and Handler, P.
  TITLE     Purfication and properties of hepatic sulfite oxidase.
  JOURNAL   J. Biol. Chem. 236 (1961) 1841-1846.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Tager, J.M. and Rautanen, N.
  TITLE     Sulfite oxidation by a plant mitochondrial system. I. Preliminary
            observations.
  JOURNAL   Biochim. Biophys. Acta 18 (1955) 111-121.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K00387  sulfite oxidase
GENES       HSA: 6821(SUOX)
            PTR: 451978(SUOX)
            MMU: 211389(Suox)
            RNO: 81805(Suox)
            CFA: 481103(SUOX)
            SPU: 586173(LOC586173)
            DME: Dmel_CG7280
            OSA: 4346125
            CME: CMR126C
            ANI: AN8058.2
            AFM: AFUA_5G02190
            AOR: AO090020000232 AO090102000277
            UMA: UM02399.1
            DDI: DDBDRAFT_0206266
            REH: H16_B0860
            HAR: HEAR1188(soxC) HEAR2349(sorA)
            ABU: Abu_0565(soxC)
            SME: SMc04049
            RPA: RPA4464(soxC)
            NWI: Nwi_3022
            MBO: Mb1786
            MBB: BCG_1796
            RHA: RHA1_ro01563
            AVA: Ava_0958
STRUCTURES  PDB: 1MJ4  1OGP  1SOX  2A99  2A9A  2A9B  2A9C  2A9D  
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.3.1
            ExPASy - ENZYME nomenclature database: 1.8.3.1
            ExplorEnz - The Enzyme Database: 1.8.3.1
            ERGO genome analysis and discovery system: 1.8.3.1
            BRENDA, the Enzyme Database: 1.8.3.1
            CAS: 9029-38-3
///
ENTRY       EC 1.8.3.2                  Enzyme
NAME        thiol oxidase;
            sulfhydryl oxidase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With oxygen as acceptor
SYSNAME     thiol:oxygen oxidoreductase
REACTION    4 R'C(R)SH + O2 = 2 R'C(R)S-S(R)CR' + 2 H2O [RN:R00057]
ALL_REAC    R00057
SUBSTRATE   R'C(R)SH [CPD:C01525];
            O2 [CPD:C00007]
PRODUCT     R'C(R)S-S(R)CR' [CPD:C02318];
            H2O [CPD:C00001]
COMMENT     R may be =S or =O, or a variety of other groups. The enzyme is not
            specific for R'.
REFERENCE   1  [PMID:13863296]
  AUTHORS   AURBACH GD, JAKOBY WB.
  TITLE     The multiple functions of thiooxidase.
  JOURNAL   J. Biol. Chem. 237 (1962) 565-8.
  ORGANISM  Piricularia oryzae
REFERENCE   2  [PMID:13549489]
  AUTHORS   NEUFELD HA, GREEN LF, LATTERELL FM, WEINTRAUB RL.
  TITLE     Thioxidase, a new sulfhydryl-oxidizing enzyme from Piricularia
            oryzae and Polyporus versicolor.
  JOURNAL   J. Biol. Chem. 232 (1958) 1093-9.
  ORGANISM  Piricularia oryzae
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.3.2
            ExPASy - ENZYME nomenclature database: 1.8.3.2
            ExplorEnz - The Enzyme Database: 1.8.3.2
            ERGO genome analysis and discovery system: 1.8.3.2
            UM-BBD (Biocatalysis/Biodegradation Database): 1.8.3.2
            BRENDA, the Enzyme Database: 1.8.3.2
            CAS: 9029-39-4
///
ENTRY       EC 1.8.3.3                  Enzyme
NAME        glutathione oxidase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With oxygen as acceptor
SYSNAME     glutathione:oxygen oxidoreductase
REACTION    2 glutathione + O2 = glutathione disulfide + H2O2 [RN:R00120]
ALL_REAC    R00120
SUBSTRATE   glutathione [CPD:C00051];
            O2 [CPD:C00007]
PRODUCT     glutathione disulfide [CPD:C00127];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Also acts, more slowly, on L-cysteine and
            several other thiols.
REFERENCE   1
  AUTHORS   Kusakabe, H., Kuninaka, A. and Yoshino, H.
  TITLE     Purification and properties of a new enzyme, glutathione oxidase
            from Penicillium sp.K-6-5.
  JOURNAL   Agric. Biol. Chem. 46 (1982) 2057-2067.
  ORGANISM  Penicillium sp.
PATHWAY     PATH: map00480  Glutathione metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.3.3
            ExPASy - ENZYME nomenclature database: 1.8.3.3
            ExplorEnz - The Enzyme Database: 1.8.3.3
            ERGO genome analysis and discovery system: 1.8.3.3
            BRENDA, the Enzyme Database: 1.8.3.3
            CAS: 55467-56-6
///
ENTRY       EC 1.8.3.4                  Enzyme
NAME        methanethiol oxidase;
            methylmercaptan oxidase;
            methyl mercaptan oxidase;
            (MM)-oxidase;
            MT-oxidase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With oxygen as acceptor
SYSNAME     methanethiol:oxygen oxidoreductase
REACTION    methanethiol + O2 + H2O = formaldehyde + hydrogen sulfide + H2O2
            [RN:R01851]
ALL_REAC    R01851
SUBSTRATE   methanethiol [CPD:C00409];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     formaldehyde [CPD:C00067];
            hydrogen sulfide [CPD:C00283];
            H2O2 [CPD:C00027]
REFERENCE   1
  AUTHORS   Suylen, G.M.H., Large, P.J., van Dijken, J.P. and Kuenen, J.G.
  TITLE     Methylmercaptan oxidase, a key enzyme in the metabolism of
            methylated sulphur compounds by Hyphomicrobium EG.
  JOURNAL   J. Gen. Microbiol. 133 (1987) 2989-2997.
  ORGANISM  Hyphomicrobium sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.3.4
            ExPASy - ENZYME nomenclature database: 1.8.3.4
            ExplorEnz - The Enzyme Database: 1.8.3.4
            ERGO genome analysis and discovery system: 1.8.3.4
            UM-BBD (Biocatalysis/Biodegradation Database): 1.8.3.4
            BRENDA, the Enzyme Database: 1.8.3.4
            CAS: 112821-28-0
///
ENTRY       EC 1.8.3.5                  Enzyme
NAME        prenylcysteine oxidase;
            prenylcysteine lyase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With oxygen as acceptor
SYSNAME     S-prenyl-L-cysteine:oxygen oxidoreductase
REACTION    an S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2
            [RN:R07360]
ALL_REAC    R07360
SUBSTRATE   S-prenyl-L-cysteine [CPD:C06751];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     prenal [CPD:C15604];
            L-cysteine [CPD:C00097];
            H2O2 [CPD:C00027]
COMMENT     A flavoprotein (FAD). Cleaves the thioether bond of
            S-prenyl-L-cysteines, such as S-farnesylcysteine and
            S-geranylgeranylcysteine. N-Acetyl-prenylcysteine and
            prenylcysteinyl peptides are not substrates. May represent the final
            step in the degradation of prenylated proteins in mammalian tissues.
            Originally thought to be a simple lyase so it had been classified as
            EC 4.4.1.18.
REFERENCE   1  [PMID:9287348]
  AUTHORS   Zhang L, Tschantz WR, Casey PJ.
  TITLE     Isolation and characterization of a prenylcysteine lyase from bovine
            brain.
  JOURNAL   J. Biol. Chem. 272 (1997) 23354-9.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:11078725]
  AUTHORS   Tschantz WR, Digits JA, Pyun HJ, Coates RM, Casey PJ.
  TITLE     Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase.
  JOURNAL   J. Biol. Chem. 276 (2001) 2321-4.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K05906  prenylcysteine oxidase
GENES       HSA: 51449(PCYOX1)
            MMU: 66881(Pcyox1)
            RNO: 246302(Pcyox1)
            CFA: 481418(PCYOX1)
            GGA: 426297(PCYOX1)
            SPU: 582165(LOC582165)
            ATH: AT5G63910
            OSA: 4337518
            ANI: AN3057.2
            CNE: CNK01940
            UMA: UM04318.1
            DDI: DDBDRAFT_0218901
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.3.5
            ExPASy - ENZYME nomenclature database: 1.8.3.5
            ExplorEnz - The Enzyme Database: 1.8.3.5
            ERGO genome analysis and discovery system: 1.8.3.5
            BRENDA, the Enzyme Database: 1.8.3.5
///
ENTRY       EC 1.8.4.1                  Enzyme
NAME        glutathione---homocystine transhydrogenase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a disulfide as acceptor
SYSNAME     glutathione:homocystine oxidoreductase
REACTION    2 glutathione + homocystine = glutathione disulfide + 2 homocysteine
            [RN:R01110]
ALL_REAC    R01110 > R01292;
            (other) R00120
SUBSTRATE   glutathione [CPD:C00051];
            homocystine [CPD:C01817]
PRODUCT     glutathione disulfide [CPD:C00127];
            homocysteine [CPD:C05330]
COMMENT     The reactions catalysed by this enzyme and by others in this
            subclass may be similar to those catalysed by EC 2.5.1.18
            glutathione transferase.
REFERENCE   1
  AUTHORS   Racker, E.
  TITLE     Glutathione-homocystine transhydrogenase.
  JOURNAL   J. Biol. Chem. 217 (1955) 867-874.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00271  Methionine metabolism
            PATH: map00480  Glutathione metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.4.1
            ExPASy - ENZYME nomenclature database: 1.8.4.1
            ExplorEnz - The Enzyme Database: 1.8.4.1
            ERGO genome analysis and discovery system: 1.8.4.1
            BRENDA, the Enzyme Database: 1.8.4.1
            CAS: 9029-40-7
///
ENTRY       EC 1.8.4.2                  Enzyme
NAME        protein-disulfide reductase (glutathione);
            glutathione-insulin transhydrogenase;
            insulin reductase;
            reductase, protein disulfide (glutathione);
            protein disulfide transhydrogenase;
            glutathione-protein disulfide oxidoreductase;
            protein disulfide reductase (glutathione);
            GSH-insulin transhydrogenase;
            protein-disulfide interchange enzyme;
            protein-disulfide isomerase/oxidoreductase;
            thiol:protein-disulfide oxidoreductase;
            thiol-protein disulphide oxidoreductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a disulfide as acceptor
SYSNAME     glutathione:protein-disulfide oxidoreductase
REACTION    2 glutathione + protein-disulfide = glutathione disulfide +
            protein-dithiol [RN:R03915]
ALL_REAC    R03915;
            (other) R02824
SUBSTRATE   glutathione [CPD:C00051];
            protein disulfide [CPD:C02582]
PRODUCT     glutathione disulfide [CPD:C00127];
            protein dithiol [CPD:C02315]
COMMENT     Reduces insulin and some other proteins.
REFERENCE   1  [PMID:14031343]
  AUTHORS   KATZEN HM, TIETZE F, STETTEN D Jr.
  TITLE     Further studies on the properties of hepatic glutathione-insulin
            transhydro-genase.
  JOURNAL   J. Biol. Chem. 238 (1963) 1006-11.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   Kohnert, K.-D., Hahn, H.-J., Zuhlke, H., Schmidt, S. and Fiedler, H.
  TITLE     Breakdown of exogenous insulin by Langerhans islets of the pancreas
            in vitro.
  JOURNAL   Biochim. Biophys. Acta 338 (1974) 68-77.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00480  Glutathione metabolism
ORTHOLOGY   KO: K05360  protein-disulfide reductase (glutathione)
GENES       HSA: 51060(TXNDC12)
            MMU: 66073(Txndc12)
            RNO: 298370(Txndc12)
            CFA: 609843(TXNDC12)
            BTA: 506991(TLP19)
            GGA: 772208(TXNDC12)
            ECI: UTI89_C1371(dsbB)
            XCV: XCV1026(dsbB)
            CVI: CV_3193(dsbH)
            BAY: RBAM_021290(resA)
STRUCTURES  PDB: 2IJY  
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.4.2
            ExPASy - ENZYME nomenclature database: 1.8.4.2
            ExplorEnz - The Enzyme Database: 1.8.4.2
            ERGO genome analysis and discovery system: 1.8.4.2
            BRENDA, the Enzyme Database: 1.8.4.2
            CAS: 9082-53-5
///
ENTRY       EC 1.8.4.3                  Enzyme
NAME        glutathione---CoA-glutathione transhydrogenase;
            glutathione-coenzyme A glutathione disulfide transhydrogenase;
            glutathione-coenzyme A glutathione disulfide transhydrogenase;
            glutathione coenzyme A-glutathione transhydrogenase;
            glutathione:coenzyme A-glutathione transhydrogenase;
            coenzyme A:oxidized-glutathione oxidoreductase;
            coenzyme A:glutathione-disulfide oxidoreductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a disulfide as acceptor
SYSNAME     CoA:glutathione-disulfide oxidoreductase
REACTION    CoA + glutathione disulfide = CoA-glutathione + glutathione
            [RN:R01111]
ALL_REAC    R01111;
            (other) R02409 R04860
SUBSTRATE   CoA [CPD:C00010];
            glutathione disulfide [CPD:C00127]
PRODUCT     CoA-glutathione [CPD:C00920];
            glutathione [CPD:C00051]
REFERENCE   1  [PMID:5924646]
  AUTHORS   Chang SH, Wilken DR.
  TITLE     Participation of the unsymmetrical disulfide of coenzyme A and
            glutathione in an enzymatic sulfhydryl-disulfide interchange. I.
            Partial purification and properties of the bovine kidney enzyme.
  JOURNAL   J. Biol. Chem. 241 (1966) 4251-60.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00272  Cysteine metabolism
            PATH: map00480  Glutathione metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.4.3
            ExPASy - ENZYME nomenclature database: 1.8.4.3
            ExplorEnz - The Enzyme Database: 1.8.4.3
            ERGO genome analysis and discovery system: 1.8.4.3
            BRENDA, the Enzyme Database: 1.8.4.3
            CAS: 37256-48-7
///
ENTRY       EC 1.8.4.4                  Enzyme
NAME        glutathione---cystine transhydrogenase;
            GSH-cystine transhydrogenase;
            NADPH-dependent GSH-cystine transhydrogenase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a disulfide as acceptor
SYSNAME     glutathione:cystine oxidoreductase
REACTION    2 glutathione + cystine = glutathione disulfide + 2 cysteine
            [RN:R01109]
ALL_REAC    R01109 > R01113;
            (other) R00120
SUBSTRATE   glutathione [CPD:C00051];
            cystine [CPD:C01420]
PRODUCT     glutathione disulfide [CPD:C00127];
            cysteine [CPD:C00736]
REFERENCE   1  [PMID:5646485]
  AUTHORS   Nagai S, Black S.
  TITLE     A thiol-disulfide transhydrogenase from yeast.
  JOURNAL   J. Biol. Chem. 243 (1968) 1942-7.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00272  Cysteine metabolism
            PATH: map00480  Glutathione metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.4.4
            ExPASy - ENZYME nomenclature database: 1.8.4.4
            ExplorEnz - The Enzyme Database: 1.8.4.4
            ERGO genome analysis and discovery system: 1.8.4.4
            BRENDA, the Enzyme Database: 1.8.4.4
            CAS: 37256-49-8
///
ENTRY       EC 1.8.4.5        Obsolete  Enzyme
NAME        Transferred to 1.8.4.13 and 1.8.4.14
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a disulfide as acceptor
COMMENT     Transferred entry: methionine-S-oxide reductase. Now EC 1.8.4.13,
            L-methionine (S)-S-oxide reductase and EC 1.8.4.14, L-methionine
            (R)-S-oxide reductase. (EC 1.8.4.5 created 1984, deleted 2006)
GENES       REH: H16_A1517(pmsR)
STRUCTURES  PDB: 1L1D  
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.4.5
            ExPASy - ENZYME nomenclature database: 1.8.4.5
            ExplorEnz - The Enzyme Database: 1.8.4.5
            ERGO genome analysis and discovery system: 1.8.4.5
            BRENDA, the Enzyme Database: 1.8.4.5
///
ENTRY       EC 1.8.4.6        Obsolete  Enzyme
NAME        Transferred to 1.8.4.11
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a disulfide as acceptor
COMMENT     Transferred entry: protein-methionine-S-oxide reductase. Proved to
            be due to EC 1.8.4.11, peptide-methionine (S)-S-oxide reductase. (EC
            1.8.4.6 created 1984, deleted 2006)
GENES       NIS: NIS_0051 NIS_1118(msrA)
            SUN: SUN_0678 SUN_1691 SUN_2465
STRUCTURES  PDB: 1FVA  1FVG  1NWA  1XM0  2FY6  2GT3  2H30  2IEM  
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.4.6
            ExPASy - ENZYME nomenclature database: 1.8.4.6
            ExplorEnz - The Enzyme Database: 1.8.4.6
            ERGO genome analysis and discovery system: 1.8.4.6
            BRENDA, the Enzyme Database: 1.8.4.6
///
ENTRY       EC 1.8.4.7                  Enzyme
NAME        enzyme-thiol transhydrogenase (glutathione-disulfide);
            [xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase;
            enzyme-thiol transhydrogenase (oxidized-glutathione);
            glutathione-dependent thiol:disulfide oxidoreductase;
            thiol:disulphide oxidoreductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a disulfide as acceptor
SYSNAME     [xanthine-dehydrogenase]:glutathione-disulfide S-oxidoreductase
REACTION    [xanthine dehydrogenase] + glutathione disulfide = [xanthine
            oxidase] + 2 glutathione [RN:R04039]
ALL_REAC    R04039
SUBSTRATE   [xanthine dehydrogenase] [CPD:C03544];
            glutathione disulfide [CPD:C00127]
PRODUCT     [xanthine oxidase] [CPD:C02756];
            glutathione [CPD:C00051]
COMMENT     Converts EC 1.17.1.4 xanthine dehydrogenase into EC 1.17.3.2
            xanthine oxidase in the presence of glutathione disulfide; also
            reduces the disulfide bond of ricin. Not inhibited by Cu2+ or thiol
            reagents.
REFERENCE   1  [PMID:6960894]
  AUTHORS   Battelli MG, Lorenzoni E.
  TITLE     Purification and properties of a new glutathione-dependent
            thiol:disulphide oxidoreductase from rat liver.
  JOURNAL   Biochem. J. 207 (1982) 133-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00480  Glutathione metabolism
GENES       AZO: azo0102(helX)
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.4.7
            ExPASy - ENZYME nomenclature database: 1.8.4.7
            ExplorEnz - The Enzyme Database: 1.8.4.7
            ERGO genome analysis and discovery system: 1.8.4.7
            BRENDA, the Enzyme Database: 1.8.4.7
            CAS: 85030-79-1
///
ENTRY       EC 1.8.4.8                  Enzyme
NAME        phosphoadenylyl-sulfate reductase (thioredoxin);
            PAPS reductase, thioredoxin-dependent;
            PAPS reductase;
            thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase;
            3'-phosphoadenylylsulfate reductase;
            thioredoxin:3'-phospho-adenylylsulfate reductase;
            phosphoadenosine-phosphosulfate reductase;
            adenosine 3',5'-bisphosphate,sulfite:oxidized-thioredoxin
            oxidoreductase (3'-phosphoadenosine-5'-phosphosulfate-forming)
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a disulfide as acceptor
SYSNAME     adenosine 3',5'-bisphosphate,sulfite:thioredoxin-disulfide
            oxidoreductase (3'-phosphoadenosine-5'-phosphosulfate-forming)
REACTION    adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide =
            3'-phosphoadenylyl sulfate + thioredoxin [RN:R02021]
ALL_REAC    R02021
SUBSTRATE   adenosine 3',5'-bisphosphate [CPD:C00054];
            sulfite [CPD:C00094];
            thioredoxin disulfide [CPD:C00343]
PRODUCT     3'-phosphoadenylyl sulfate [CPD:C00053];
            thioredoxin [CPD:C00342]
COMMENT     Specific for PAPS. The enzyme from Escherichia coli will use
            thioredoxins from other species.
REFERENCE   1  [PMID:7588765]
  AUTHORS   Berendt U, Haverkamp T, Prior A, Schwenn JD.
  TITLE     Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate
            reductase investigated by site-directed mutagenesis.
  JOURNAL   Eur. J. Biochem. 233 (1995) 347-56.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K00390  phosphoadenosine phosphosulfate reductase
GENES       CME: CMT162C
            SCE: YPR167C(MET16)
            AGO: AGOS_AEL259W
            PIC: PICST_49723
            CGR: CAGL0I08503g
            SPO: SPAC13G7.06
            ANI: AN4770.2
            AOR: AO090020000347
            CNE: CNB03860
            UMA: UM02942.1
            ECO: b2762(cysH)
            ECJ: JW2732(cysH)
            ECE: Z4072(cysH)
            ECS: ECs3617
            ECC: c3321(cysH)
            ECI: UTI89_C3126(cysH)
            ECP: ECP_2736
            ECV: APECO1_3770(cysH)
            ECW: EcE24377A_3064(cysH)
            ECX: EcHS_A2902(cysH)
            STY: STY3074(cysH)
            STT: t2847(cysH)
            SPT: SPA2802(cysH)
            SEC: SC2877(cysH)
            STM: STM2946(cysH)
            YPE: YPO3370(cysH)
            YPA: YPA_2867
            YPN: YPN_0723
            YPP: YPDSF_2990
            YPS: YPTB0761(cysH)
            YPI: YpsIP31758_3309(cysH)
            YEN: YE0757(cysH)
            SFL: SF2778(cysH)
            SFX: S2971(cysH)
            SFV: SFV_2743(cysH)
            SSN: SSON_2915(cysH)
            SBO: SBO_2645(cysH)
            SDY: SDY_2964(cysH)
            ECA: ECA3545(cysH)
            PLU: plu0705(cysH)
            BUC: BU426(cysH)
            SGL: SG0518
            BFL: Bfl160(cysH)
            BPN: BPEN_165(cysH)
            MSU: MS1253(cysH)
            ASU: Asuc_1690
            XFA: XF1497
            XFT: PD0714(cysH)
            XCC: XCC3175(cysH)
            XCB: XC_0990
            XCV: XCV3449(cysH)
            XAC: XAC3332(cysH)
            XOO: XOO3401(cysH)
            XOM: XOO_3201(XOO3201)
            VCH: VC0386
            VCO: VC0395_A2797(cysH)
            VVU: VV1_1404
            VVY: VV2965
            VPA: VP2720
            VFI: VF0312
            PPR: PBPRA3319
            PAE: PA1756(cysH)
            PAU: PA14_41840(cysH)
            PPU: PP_2328(cysH)
            PST: PSPTO_2280(cysH)
            PSB: Psyr_2078
            PSP: PSPPH_2049
            PFL: PFL_1854
            PEN: PSEEN1896
            PAR: Psyc_1066
            PCR: Pcryo_1396
            ACI: ACIAD0833(cysH)
            SON: SO_3736(cysH)
            SDN: Sden_0934
            SFR: Sfri_3191
            SHE: Shewmr4_3078
            SHM: Shewmr7_0894
            SHN: Shewana3_0857
            CPS: CPS_4761(cysH)
            PHA: PSHAa0156(cysH)
            PAT: Patl_4037
            MCA: MCA2468(cysH)
            NOC: Noc_2290
            AEH: Mlg_1263 Mlg_2114
            HHA: Hhal_1777
            HCH: HCH_02658 HCH_04016
            CSA: Csal_2427
            ABO: ABO_1686(cysH)
            AHA: AHA_3373(cysH)
            BCI: BCI_0216(cysH)
            NME: NMB1155 NMB1193
            NMA: NMA1366(cysH)
            CVI: CV_3574(cysH)
            RSO: RSc2423(cysH)
            REU: Reut_A2694
            REH: H16_A2997(cysH)
            RME: Rmet_2814
            BMA: BMA0665
            BXE: Bxe_A3662
            BVI: Bcep1808_2556
            BUR: Bcep18194_A5804
            BCN: Bcen_1862
            BCH: Bcen2424_2473
            BAM: Bamb_2522
            BPS: BPSL0958(cysH)
            BPM: BURPS1710b_1168(cysH)
            BTE: BTH_I0816
            PNU: Pnuc_1481
            BPE: BP0970(cysH)
            BPA: BPP1659(cysH)
            BBR: BB3449(cysH)
            RFR: Rfer_2458
            POL: Bpro_2337
            PNA: Pnap_2429
            VEI: Veis_4333
            MPT: Mpe_A1501
            HAR: HEAR2394(cysH)
            MMS: mma_2454(cysH)
            NEU: NE0855(cysH)
            NET: Neut_1187
            NMU: Nmul_A1147
            EBA: ebA2623(cysH)
            AZO: azo0430(cysH)
            DAR: Daro_2914
            MFA: Mfla_1679
            WSU: WS1010(cysH)
            TDN: Tmden_0156
            ABU: Abu_2173(cysH)
            NIS: NIS_1681
            GSU: GSU1716
            GME: Gmet_2858
            GUR: Gura_3935
            PCA: Pcar_1770
            DDE: Dde_1789
            AFW: Anae109_1642
            MLO: mll3228
            MES: Meso_3992
            SME: SMc00092(cysH)
            SMD: Smed_0559
            ATU: Atu0818(cysH)
            ATC: AGR_C_1497
            RET: RHE_CH01132(cysH)
            RLE: RL1262
            BME: BMEI1765
            BMF: BAB1_0182(cysH)
            BMS: BR0182(cysH)
            BMB: BruAb1_0178(cysH)
            BOV: BOV_0176(cysH)
            BJA: blr1481(cysH)
            BRA: BRADO1069(cysH)
            BBT: BBta_6978(cysH)
            RPA: RPA0751(cysH)
            RPB: RPB_1044
            RPC: RPC_4011
            RPD: RPD_1155
            RPE: RPE_1767
            NWI: Nwi_2761
            NHA: Nham_3561
            CCR: CC_1121
            SIL: SPO2635(cysH)
            SIT: TM1040_1759
            RSP: RSP_1941(cysH)
            JAN: Jann_1772
            RDE: RD1_2967(cysH)
            HNE: HNE_0327(cysH)
            ZMO: ZMO0007(cysH)
            NAR: Saro_2560
            SAL: Sala_0768
            ELI: ELI_01870
            GOX: GOX0928
            GBE: GbCGDNIH1_0530
            RRU: Rru_A1929
            MAG: amb2210
            ABA: Acid345_0830
            SUS: Acid_7933
            BSU: BG11930(cysH) BG13107(yitB)
            BHA: BH1486(cysH)
            BAN: BA1440(cysH)
            BAR: GBAA1440(cysH)
            BAA: BA_1961
            BAT: BAS1330
            BCE: BC1421
            BCA: BCE_1544(cysH)
            BCZ: BCZK1304(cysH)
            BTK: BT9727_1303(cysH)
            BLI: BL01979(yitB) BL02282(cysH)
            BLD: BLi01778 BLi02154(yitB)
            BCL: ABC0611
            BPU: BPUM_1456(cysH)
            OIH: OB1652(cysH)
            GKA: GK0416
            SEP: SE2181
            SER: SERP2192(cysH)
            SHA: SH0413
            SSP: SSP2409
            STH: STH1142
            CTH: Cthe_2535
            DSY: DSY2953(cysH)
            MTU: Rv2392(cysH)
            MTC: MT2462(cysH)
            MBO: Mb2413(cysH)
            MBB: BCG_2406(cysH)
            MPA: MAP2036(cysH_1) MAP2209(cysH_2)
            MAV: MAV_1786 MAV_2153
            MSM: MSMEG_4528
            MMC: Mmcs_3475
            CGL: NCgl2717(cgl2816)
            CGB: cg3116(cysH)
            CEF: CE2642
            CJK: jk0245(cysH)
            NFA: nfa14180(cysH)
            RHA: RHA1_ro01252(cysH) RHA1_ro10068 RHA1_ro11012
            SCO: SCO6100(cysH)
            SMA: SAV2129(cysH)
            AAU: AAur_3092(cysH)
            NCA: Noca_3794
            TFU: Tfu_1889
            FRA: Francci3_0527
            FAL: FRAAL1019(cysH)
            ACE: Acel_2054
            SEN: SACE_1475(cysH)
            RXY: Rxyl_0962
            FNU: FN0444
            RBA: RB6993(cysH)
            LIL: LA4221(cysH)
            LIC: LIC13372(cysH)
            LBJ: LBJ_2842(cysH-1)
            LBL: LBL_0229(cysH-1)
            SYN: slr1791(cysH)
            SYW: SYNW2164(cysH)
            SYC: syc1600_d(cysH)
            SYF: Synpcc7942_2506
            SYD: Syncc9605_2309
            SYE: Syncc9902_0384
            SYG: sync_2510
            SYR: SynRCC307_0390(cysH)
            SYX: SynWH7803_2174(cysH)
            CYA: CYA_1123(cysH)
            CYB: CYB_0438(cysH)
            TEL: tll1035(cysH)
            GVI: glr1656
            ANA: all4464
            AVA: Ava_3330
            PMA: Pro0095(cysH)
            PMM: PMM0081(cysH)
            PMT: PMT1624(cysH)
            PMN: PMN2A_1445
            PMI: PMT9312_0084
            PMB: A9601_00941(cysH)
            PMC: P9515_00911(cysH)
            PMF: P9303_02591(cysH)
            PMG: P9301_00931(cysH)
            PMH: P9215_00941(cysH)
            PME: NATL1_01461(cysH)
            TER: Tery_2837
            SRU: SRU_0422(cysH)
            CHU: CHU_0957(cysH)
            GFO: GFO_0323(cysH)
            FJO: Fjoh_1501
            PLT: Plut_1561
            DRA: DR_A0015
            DGE: Dgeo_1409
            TTH: TTC0310
            TTJ: TTHA0669
            MAC: MA2894
            MBA: Mbar_A2943
            MMA: MM_3300
            HMA: pNG2036(papSR) rrnAC0653(cysH)
            RCI: RCIX1979(cysH-1) RRC23(cysH-2)
            SSO: SSO2911(cysH)
            STO: ST2567
            SAI: Saci_1925(cysH) Saci_2202
            MSE: Msed_0962
            PAI: PAE2575
STRUCTURES  PDB: 1ILO  1WMJ  2O8V  
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.4.8
            ExPASy - ENZYME nomenclature database: 1.8.4.8
            ExplorEnz - The Enzyme Database: 1.8.4.8
            ERGO genome analysis and discovery system: 1.8.4.8
            BRENDA, the Enzyme Database: 1.8.4.8
            CAS: 9068-63-7
///
ENTRY       EC 1.8.4.9                  Enzyme
NAME        adenylyl-sulfate reductase (glutathione);
            5'-adenylylsulfate reductase (also used for
            internal_xref(ec_num(1,8,99,2)));
            AMP,sulfite:oxidized-glutathione oxidoreductase
            (adenosine-5'-phosphosulfate-forming);
            plant-type 5'-adenylylsulfate reductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a disulfide as acceptor
SYSNAME     AMP,sulfite:glutathione-disulfide oxidoreductase
            (adenosine-5'-phosphosulfate-forming)
REACTION    AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2
            glutathione [RN:R05717]
ALL_REAC    R05717
SUBSTRATE   AMP [CPD:C00020];
            sulfite [CPD:C00094];
            glutathione disulfide [CPD:C00127]
PRODUCT     adenylyl sulfate [CPD:C00224];
            glutathione [CPD:C00051]
COMMENT     This enzyme differs from EC 1.8.99.2, adenylyl-sulfate reductase
            (acceptor), in using glutathione as the reductant. Glutathione can
            be replaced by gamma-glutamylcysteine or dithiothreitol, but not by
            thioredoxin, glutaredoxin or mercaptoethanol. The enzyme from the
            mouseear cress, Arabidopsis thaliana, contains a glutaredoxin-like
            domain. The enzyme is also found in other photosynthetic eukaryotes,
            e.g., the Madagascar periwinkle, Catharanthus roseus and the hollow
            green seaweed, Enteromorpha intestinalis.
REFERENCE   1  [PMID:8917599]
  AUTHORS   Gutierrez-Marcos JF, Roberts MA, Campbell EI, Wray JL.
  TITLE     Three members of a novel small gene-family from Arabidopsis thaliana
            able to complement functionally an Escherichia coli mutant defective
            in PAPS reductase activity encode proteins with a thioredoxin-like
            domain and &quot;APS reductase&quot; activity.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 13377-82.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   2  [PMID:8917600]
  AUTHORS   Setya A, Murillo M, Leustek T.
  TITLE     Sulfate reduction in higher plants: molecular evidence for a novel
            5'-adenylylsulfate reductase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 13383-8.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   3  [PMID:9653199]
  AUTHORS   Bick JA, Aslund F, Chen Y, Leustek T.
  TITLE     Glutaredoxin function for the carboxyl-terminal domain of the
            plant-type 5'-adenylylsulfate reductase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 8404-9.
  ORGANISM  Arabidopsis thaliana [GN:ath]
ORTHOLOGY   KO: K05907  adenylyl-sulfate reductase (glutathione)
GENES       ATH: AT1G62180(APR2) AT4G04610(APR1) AT4G21990(APR3)
            OSA: 4343348
            PPF: Pput_3442
            PFO: Pfl_1757
            SDE: Sde_1669
            MAQ: Maqu_1582
            MMW: Mmwyl1_2969
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.4.9
            ExPASy - ENZYME nomenclature database: 1.8.4.9
            ExplorEnz - The Enzyme Database: 1.8.4.9
            ERGO genome analysis and discovery system: 1.8.4.9
            BRENDA, the Enzyme Database: 1.8.4.9
///
ENTRY       EC 1.8.4.10                 Enzyme
NAME        adenylyl-sulfate reductase (thioredoxin);
            thioredoxin-dependent 5'-adenylylsulfate reductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a disulfide as acceptor
SYSNAME     AMP,sulfite:thioredoxin-disulfide oxidoreductase
            (adenosine-5'-phosphosulfate-forming)
REACTION    AMP + sulfite + thioredoxin disulfide = 5'-adenylyl sulfate +
            thioredoxin [RN:R07176]
ALL_REAC    R07176
SUBSTRATE   AMP [CPD:C00020];
            sulfite [CPD:C00094];
            thioredoxin disulfide [CPD:C00343]
PRODUCT     5'-adenylyl sulfate [CPD:C00224];
            thioredoxin [CPD:C00342]
COMMENT     Uses adenylyl sulfate, not phosphoadenylyl sulfate, distinguishing
            this enzyme from EC 1.8.4.8, phosphoadenylyl-sulfate reductase
            (thioredoxin). Uses thioredoxin as electron donor, not glutathione
            or other donors, distinguishing it from EC 1.8.4.9 [adenylyl-sulfate
            reductase (glutathione)] and EC 1.8.99.2 (adenylyl-sulfate
            reductase).
REFERENCE   1  [PMID:10613872]
  AUTHORS   Bick JA, Dennis JJ, Zylstra GJ, Nowack J, Leustek T.
  TITLE     Identification of a new class of 5'-adenylylsulfate (APS) reductases
            from sulfate-assimilating bacteria.
  JOURNAL   J. Bacteriol. 182 (2000) 135-42.
  ORGANISM  Burkholderia cepacia [GN:bam]
REFERENCE   2  [PMID:10464198]
  AUTHORS   Abola AP, Willits MG, Wang RC, Long SR.
  TITLE     Reduction of adenosine-5'-phosphosulfate instead of
            3'-phosphoadenosine-5'-phosphosulfate in cysteine biosynthesis by
            Rhizobium meliloti and other members of the family Rhizobiaceae.
  JOURNAL   J. Bacteriol. 181 (1999) 5280-7.
  ORGANISM  Rhizobium meliloti
REFERENCE   3  [PMID:12072441]
  AUTHORS   Williams SJ, Senaratne RH, Mougous JD, Riley LW, Bertozzi CR.
  TITLE     5'-adenosinephosphosulfate lies at a metabolic branch point in
            mycobacteria.
  JOURNAL   J. Biol. Chem. 277 (2002) 32606-15.
  ORGANISM  Mycobacterium tuberculosis, Mycobacterium smegmatis [GN:msm]
REFERENCE   4  [PMID:10939523]
  AUTHORS   Neumann S, Wynen A, Truper HG, Dahl C.
  TITLE     Characterization of the cys gene locus from Allochromatium vinosum
            indicates an unusual sulfate assimilation pathway.
  JOURNAL   Mol. Biol. Rep. 27 (2000) 27-33.
  ORGANISM  Allochromatium vinosum
GENES       BPL: BURPS1106A_1015
            BPD: BURPS668_1008
STRUCTURES  PDB: 2GOY  
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.4.10
            ExPASy - ENZYME nomenclature database: 1.8.4.10
            ExplorEnz - The Enzyme Database: 1.8.4.10
            ERGO genome analysis and discovery system: 1.8.4.10
            BRENDA, the Enzyme Database: 1.8.4.10
///
ENTRY       EC 1.8.4.11                 Enzyme
NAME        peptide-methionine (S)-S-oxide reductase;
            MsrA;
            methionine sulfoxide reductase (ambiguous);
            methionine sulphoxide reductase A;
            methionine S-oxide reductase (ambiguous);
            methionine S-oxide reductase (S-form oxidizing);
            methionine sulfoxide reductase A;
            peptide methionine sulfoxide reductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a disulfide as acceptor
SYSNAME     peptide-L-methionine:thioredoxin-disulfide S-oxidoreductase
            [L-methionine (S)-S-oxide-forming]
REACTION    (1) peptide-L-methionine + thioredoxin disulfide + H2O =
            peptide-L-methionine (S)-S-oxide + thioredoxin [RN:R04120];
            (2) L-methionine + thioredoxin disulfide + H2O = L-methionine
            (S)-S-oxide + thioredoxin [RN:R07606]
ALL_REAC    R04120 R07606
SUBSTRATE   peptide-L-methionine [CPD:C03023];
            thioredoxin disulfide [CPD:C00343];
            H2O [CPD:C00001];
            L-methionine [CPD:C00073]
PRODUCT     peptide-L-methionine (S)-S-oxide [CPD:C03895];
            thioredoxin [CPD:C00342];
            L-methionine (S)-S-oxide [CPD:C15999]
COMMENT     The reaction occurs in the reverse direction to that shown above.
            The enzyme exhibits high specificity for the reduction of the S-form
            of L-methionine S-oxide, acting faster on the residue in a peptide
            than on the free amino acid [9]. On the free amino acid, it can also
            reduce D-methionine (S)-S-oxide but more slowly [9]. The enzyme
            plays a role in preventing oxidative-stress damage caused by
            reactive oxygen species by reducing the oxidized form of methionine
            back to methionine and thereby reactivating peptides that had been
            damaged. In some species, e.g. Neisseria meningitidis, both this
            enzyme and EC 1.8.4.12, peptide-methionine (R)-S-oxide reductase,
            are found within the same protein whereas, in other species, they
            are separate proteins [1,4]. The reaction proceeds via a
            sulfenic-acid intermediate [5,10].
REFERENCE   1  [PMID:11779133]
  AUTHORS   Moskovitz J, Singh VK, Requena J, Wilkinson BJ, Jayaswal RK,
            Stadtman ER.
  TITLE     Purification and characterization of methionine sulfoxide reductases
            from mouse and Staphylococcus aureus and their substrate
            stereospecificity.
  JOURNAL   Biochem. Biophys. Res. Commun. 290 (2002) 62-5.
  ORGANISM  Staphylococcus aureus, mouse [GN:mmu]
REFERENCE   2  [PMID:12837786]
  AUTHORS   Taylor AB, Benglis DM Jr, Dhandayuthapani S, Hart PJ.
  TITLE     Structure of Mycobacterium tuberculosis methionine sulfoxide
            reductase A in complex with protein-bound methionine.
  JOURNAL   J. Bacteriol. 185 (2003) 4119-26.
  ORGANISM  Mycobacterium tuberculosis
REFERENCE   3  [PMID:14523107]
  AUTHORS   Singh VK, Moskovitz J.
  TITLE     Multiple methionine sulfoxide reductase genes in Staphylococcus
            aureus: expression of activity and roles in tolerance of oxidative
            stress.
  JOURNAL   Microbiology. 149 (2003) 2739-47.
  ORGANISM  Staphylococcus aureus
REFERENCE   4  [PMID:15680231]
  AUTHORS   Boschi-Muller S, Olry A, Antoine M, Branlant G.
  TITLE     The enzymology and biochemistry of methionine sulfoxide reductases.
  JOURNAL   Biochim. Biophys. Acta. 1703 (2005) 231-8.
  ORGANISM  Escherichia coli [GN:eco], Saccharomyces cerevisiae [GN:sce], ,
            Neisseria meningitidis
REFERENCE   5  [PMID:15680230]
  AUTHORS   Ezraty B, Aussel L, Barras F.
  TITLE     Methionine sulfoxide reductases in prokaryotes.
  JOURNAL   Biochim. Biophys. Acta. 1703 (2005) 221-9.
  ORGANISM  Staphylococcus aureus, Escherichia coli [GN:eco], Bacillus subtilis
            [GN:bsu]
REFERENCE   6  [PMID:15680228]
  AUTHORS   Weissbach H, Resnick L, Brot N.
  TITLE     Methionine sulfoxide reductases: history and cellular role in
            protecting against oxidative damage.
  JOURNAL   Biochim. Biophys. Acta. 1703 (2005) 203-12.
  ORGANISM  Mycobacterium tuberculosis, Escherichia coli [GN:eco], Neisseria
            meningitidis, cow [GN:bta], Helicobacteria pylori, Haemophilus
            influenzae, Streptococcus pneumoniae, Streptococcus gordonii
REFERENCE   7  [PMID:15680233]
  AUTHORS   Kauffmann B, Aubry A, Favier F.
  TITLE     The three-dimensional structures of peptide methionine sulfoxide
            reductases: current knowledge and open questions.
  JOURNAL   Biochim. Biophys. Acta. 1703 (2005) 249-60.
  ORGANISM  Mycobacterium tuberculosis, Escherichia coli [GN:eco], cow [GN:bta],
            Bacillus subtilis [GN:bsu], Deinococcus radiodurans [GN:dra]
REFERENCE   8  [PMID:12693988]
  AUTHORS   Vougier S, Mary J, Friguet B.
  TITLE     Subcellular localization of methionine sulphoxide reductase A
            (MsrA): evidence for mitochondrial and cytosolic isoforms in rat
            liver cells.
  JOURNAL   Biochem. J. 373 (2003) 531-7.
  ORGANISM  rat [GN:rno]
REFERENCE   9  [PMID:11812798]
  AUTHORS   Olry A, Boschi-Muller S, Marraud M, Sanglier-Cianferani S, Van
            Dorsselear A, Branlant G.
  TITLE     Characterization of the methionine sulfoxide reductase activities of
            PILB, a probable virulence factor from Neisseria meningitidis.
  JOURNAL   J. Biol. Chem. 277 (2002) 12016-22.
  ORGANISM  Staphylococcus aureus, Escherichia coli [GN:eco], Neisseria
            meningitidis, Streptococcus pneumoniae, Erwinia chrysanthemi,
            Mycoplasma genitalium [GN:mge], Neisseria gonorrhoeae [GN:ngo]
REFERENCE   10 [PMID:7017726]
  AUTHORS   Brot N, Weissbach L, Werth J, Weissbach H.
  TITLE     Enzymatic reduction of protein-bound methionine sulfoxide.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 78 (1981) 2155-8.
  ORGANISM  Escherichia coli [GN:eco], rat [GN:rno], Euglena gracilis,
            Tetrahymena pyriformis, spinach
ORTHOLOGY   KO: K07304  peptide-methionine (S)-S-oxide reductase
GENES       HSA: 4482(MSRA)
            MMU: 110265(Msra)
            RNO: 29447(Msra)
            CFA: 608103(MSRA)
            BTA: 281312(MSRA)
            GGA: 422027(MSRA)
            XLA: 379956(msra)
            DME: Dmel_CG7266(Eip71CD)
            ATH: AT4G25130
            OSA: 4336192 4349402
            SCE: YER042W(MXR1)
            AGO: AGOS_AFR239W
            PIC: PICST_87980
            CGR: CAGL0C02233g
            SPO: SPAC30.09c
            ANI: AN4514.2
            AFM: AFUA_2G03140
            AOR: AO090120000273
            CNE: CNG04210
            DDI: DDBDRAFT_0217823
            TET: TTHERM_00160750 TTHERM_00219050 TTHERM_00590190
                 TTHERM_01289140
            TBR: Tb927.8.550
            TCR: 509611.180 510855.10
            LMA: LmjF07.1140
            ECO: b4219(msrA)
            ECJ: JW4178(msrA)
            ECE: Z5830(msrA)
            ECS: ECs5197
            ECC: c5317(msrA)
            ECI: UTI89_C4827(msrA)
            ECP: ECP_4472
            ECV: APECO1_2169(msrA)
            ECW: EcE24377A_4789(msrA)
            STY: STY4767(msrA)
            STT: t4462(msrA)
            SPT: SPA4228(msrA)
            SEC: SC4283(msrA)
            STM: STM4408(msrA)
            YPE: YPO3525(msrA)
            YPK: y0658(msrA)
            YPM: YP_0558(msrA)
            YPA: YPA_0075
            YPN: YPN_3269
            YPP: YPDSF_3574
            YPS: YPTB0451(msrA)
            SFL: SF4268(msrA)
            SFX: S4532(msrA)
            SFV: SFV_4269(msrA)
            SSN: SSON_4404(msrA)
            SBO: SBO_4224(msrA)
            SDY: SDY_4456(msrA)
            ECA: ECA3597(msrA)
            PLU: plu4555(msrA)
            ENT: Ent638_0397 Ent638_1676
            SPE: Spro_0458 Spro_2727
            HIN: HI1455(msrA)
            HIT: NTHI1677(msaB)
            HSO: HS_1687(msrAB)
            PMU: PM0605
            XFA: XF1940
            XFT: PD0859(msrA)
            XCC: XCC0828(pms)
            XCB: XC_3402
            XCV: XCV0937(pms)
            XAC: XAC0900(pms)
            XOO: XOO3657(pms)
            XOM: XOO_3455(XOO3455)
            VCH: VC2549 VCA0615
            VCO: VC0395_0557 VC0395_A2127(msrA)
            VVU: VV1_0713 VV2_1038 VV2_1649
            VVY: VV0427 VVA0461 VVA1534
            VPA: VP0306 VPA0207 VPA0301
            VFI: VF0331 VFA0005
            PPR: PBPRA0378(msrA) PBPRB1251
            PAE: PA5018(msrA)
            PAU: PA14_66330(msrA)
            PAP: PSPA7_0128(msrA2) PSPA7_5755(msrA1)
            PPU: PP_0336(msrA)
            PPF: Pput_0361 Pput_3842
            PST: PSPTO_0405(msrA)
            PSB: Psyr_4771
            PSP: PSPPH_4802(msrA)
            PFL: PFL_0506 PFL_2555(msrA)
            PFO: Pfl_0459 Pfl_2296 Pfl_2778
            PEN: PSEEN5148(msrA)
            PMY: Pmen_0572 Pmen_2521
            PAR: Psyc_1043 Psyc_1950
            PCR: Pcryo_1088 Pcryo_1427 Pcryo_2243
            PRW: PsycPRwf_0289 PsycPRwf_0816 PsycPRwf_1374
            ACI: ACIAD0510(msrA)
            SON: SO_2337(msrA) SO_2588
            SDN: Sden_1784 Sden_2304
            SFR: Sfri_1402 Sfri_1488 Sfri_1933
            SAZ: Sama_1707
            SBL: Sbal_1857 Sbal_2224
            SBM: Shew185_2147
            SLO: Shew_1591 Shew_1923
            SPC: Sputcn32_1883
            SSE: Ssed_2331
            SPL: Spea_2248
            SHE: Shewmr4_2030 Shewmr4_2184
            SHM: Shewmr7_1945 Shewmr7_2261
            SHN: Shewana3_2133 Shewana3_2393 Shewana3_4324 Shewana3_4325
                 Shewana3_4335
            SHW: Sputw3181_2125 Sputw3181_2271
            ILO: IL1525 IL2039(msrA)
            CPS: CPS_2638(msrA1) CPS_3068(msrA) CPS_3069 CPS_3367(msrAB)
                 CPS_4817(msrA2)
            PHA: PSHAa1243(mrsAB) PSHAa1444(msrC) PSHAa1583(msrAA)
                 PSHAa2274(msrAB)
            PAT: Patl_0746 Patl_4063
            SDE: Sde_1862
            PIN: Ping_0217 Ping_1028 Ping_1447
            MAQ: Maqu_1009 Maqu_3401 Maqu_3402
            CBU: CBU_1306(msrA)
            CBD: COXBU7E912_1394(msrA)
            LPN: lpg0104 lpg2098 lpg2908(msrA)
            LPF: lpl0104 lpl2825
            LPP: lpp0118 lpp2977
            MCA: MCA2979(msrA)
            FTU: FTT1105c(msrA1) FTT1797c(msrA2)
            FTF: FTF1105c(msrA1) FTF1797c(msrA2)
            FTW: FTW_1414 FTW_2019(msrA)
            FTL: FTL_1093 FTL_1960
            FTH: FTH_1069(msrA1) FTH_1877(msrA2)
            FTA: FTA_2074(msrA)
            FTN: FTN_0769 FTN_1772
            TCX: Tcr_0783
            NOC: Noc_1776 Noc_2080
            AEH: Mlg_1308
            HHA: Hhal_1380 Hhal_1595
            HCH: HCH_02243(msrA)
            CSA: Csal_1295 Csal_1866
            ABO: ABO_1530(msrA) ABO_2703(msrA)
            MMW: Mmwyl1_1855 Mmwyl1_3869
            AHA: AHA_2568(msrA)
            RMA: Rmag_0196 Rmag_0636
            NME: NMB0044
            NMA: NMA0290(pilB)
            NMC: NMC0020(pilB)
            NGO: NGO2059
            CVI: CV_2325(msrA)
            RSO: RSc0764(msrA)
            REU: Reut_A0812 Reut_B4156
            REH: H16_A2806
            RME: Rmet_1169 Rmet_2645 Rmet_4557
            BMA: BMA0356(msrA)
            BML: BMA10299_A2491(msrA)
            BMN: BMA10247_0103(msrA)
            BXE: Bxe_A0738 Bxe_B0562 Bxe_B0817
            BVI: Bcep1808_1841 Bcep1808_2665 Bcep1808_5515 Bcep1808_5517
            BUR: Bcep18194_A5903 Bcep18194_C6663
            BCN: Bcen_1588 Bcen_1960
            BCH: Bcen2424_2571 Bcen2424_6243
            BAM: Bamb_2619 Bamb_5961
            BPS: BPSL0851
            BPM: BURPS1710b_1058
            BPL: BURPS1106A_0900(msrA)
            BPD: BURPS668_0897(msrA)
            BTE: BTH_I0714
            PNU: Pnuc_0662 Pnuc_0972
            BPE: BP3041
            BPA: BPP3768
            BBR: BB4214
            RFR: Rfer_2598
            POL: Bpro_1674 Bpro_2741
            PNA: Pnap_1135 Pnap_1835
            AAV: Aave_2814 Aave_2948
            AJS: Ajs_1676 Ajs_2030
            VEI: Veis_1801 Veis_3045
            MPT: Mpe_A1767 Mpe_A2934
            MMS: mma_0947 mma_0948 mma_1547 mma_2839
            NEU: NE1701(msrA)
            NET: Neut_0419
            NMU: Nmul_A0327 Nmul_A2452
            EBA: ebA4211(msrA) ebA872(msrA)
            AZO: azo2170(msrB) azo3320(msrA)
            DAR: Daro_3532
            TBD: Tbd_0847 Tbd_2632
            MFA: Mfla_2085
            HPY: HP0224(msrA)
            HPJ: jhp0210
            HPA: HPAG1_0226
            HHE: HH0739(msrA)
            HAC: Hac_1495(msrA)
            TDN: Tmden_0012
            CJE: Cj0637c(mrsA)
            CJR: CJE0740(msrA)
            CJJ: CJJ81176_0665(msrA)
            CFF: CFF8240_1279
            ABU: Abu_1631(msrA)
            GSU: GSU3161(msrA)
            GME: Gmet_0222 Gmet_0268
            GUR: Gura_1044 Gura_1749 Gura_4073
            PCA: Pcar_2611
            PPD: Ppro_2948
            DVU: DVU1984(msrA)
            DVL: Dvul_1188 Dvul_2376
            DDE: Dde_1002 Dde_2482
            LIP: LI0119(msrA)
            BBA: Bd1058(msrA)
            DPS: DP0315 DP1227
            ADE: Adeh_1892
            AFW: Anae109_1335 Anae109_2777 Anae109_3626 Anae109_3627
            MXA: MXAN_6864(msrBA) MXAN_7060(msrA)
            SAT: SYN_01261
            SFU: Sfum_2572
            PUB: SAR11_0188(msrB)
            MLO: mll1760 mll4530
            MES: Meso_3242 Meso_3981
            PLA: Plav_0845 Plav_1522 Plav_1523 Plav_2156
            SME: SMa1896 SMc02467(msrA2) SMc02885(msrA1)
            SMD: Smed_2955 Smed_3417 Smed_5350 Smed_5572 Smed_5573
            ATU: Atu0125(msrA)
            ATC: AGR_C_197
            RET: RHE_PB00110(msrAb) RHE_PE00011(msrAe)
            RLE: pRL110014 pRL90212
            BME: BMEII0230
            BMF: BAB2_1029
            BMS: BRA1069(msrA)
            BMB: BruAb2_1009(msrA)
            BOV: BOV_A1007(msrA)
            OAN: Oant_1312 Oant_3364
            BJA: bll6260 blr0834(msrA) blr7043(msrA)
            BRA: BRADO5066(msrB) BRADO5925(msrA) BRADO5926(msrB)
                 BRADO7141(msrA)
            BBT: BBta_1855(msrB) BBta_1856(msrA) BBta_5538(msrB)
                 BBta_7872(msrA)
            RPA: RPA4070(msrA1) RPA4834(msrA2)
            RPB: RPB_1517 RPB_4709
            RPC: RPC_3834 RPC_4941
            RPD: RPD_1458 RPD_4419
            RPE: RPE_3959 RPE_4918
            NWI: Nwi_0971
            NHA: Nham_1129 Nham_2938
            XAU: Xaut_2494 Xaut_2840 Xaut_2966 Xaut_2967
            CCR: CC_0994 CC_1039
            SIL: SPO0014(msrA-1) SPO3740(msrA-2)
            SIT: TM1040_2804 TM1040_2879
            RSP: RSP_0559(msrA)
            RSH: Rsph17029_1275 Rsph17029_2211
            RSQ: Rsph17025_1226 Rsph17025_1907
            JAN: Jann_0340 Jann_2142
            RDE: RD1_0419(msrA-1) RD1_0596(msrA)
            PDE: Pden_0621 Pden_1893
            MMR: Mmar10_0153
            HNE: HNE_3001(msrA1) HNE_3479(msrA2) HNE_3496(msrA3)
            ZMO: ZMO0998(msrA)
            NAR: Saro_0158 Saro_3095
            SAL: Sala_0126 Sala_0173 Sala_0240
            SWI: Swit_0074 Swit_2816 Swit_2900 Swit_3550
            ELI: ELI_11290 ELI_12530
            GOX: GOX2493
            GBE: GbCGDNIH1_2419
            ACR: Acry_0406
            RRU: Rru_A2362
            MAG: amb1953
            MGM: Mmc1_2294
            ABA: Acid345_2013 Acid345_3735 Acid345_3737
            SUS: Acid_4514 Acid_6211
            BSU: BG11627(msrA)
            BHA: BH1448 BH2249
            BAN: BA1846(msrA-1) BA5687(msrA-2)
            BAR: GBAA1846(msrA-1) GBAA5687(msrA-2)
            BAA: BA_0545 BA_2350
            BAT: BAS1711 BAS5290
            BCE: BC1774 BC5436
            BCA: BCE_1931(msrA) BCE_5569(msrA)
            BCZ: BCZK1663(msrB) BCZK5132(msrA)
            BCY: Bcer98_1443 Bcer98_3954
            BTK: BT9727_1688(msrB) BT9727_5115(msrA)
            BTL: BALH_4939(msrA)
            BLI: BL01421(msrA)
            BLD: BLi02303(msrA)
            BCL: ABC1748(msrA) ABC2140
            BPU: BPUM_1900 BPUM_1901
            OIH: OB0734 OB1734
            GKA: GK2710
            SAU: SA1194(msrA) SA1257 SA2453
            SAV: SAV1361(msrA) SAV1424 SAV2660
            SAM: MW1248(msrA) MW1314 MW2580
            SAR: SAR1373(msrA1) SAR1437(msrA2) SAR2741
            SAS: SAS1301 SAS1367 SAS2546
            SAC: SACOL1397(msrA) SACOL2683
            SAB: SAB1217c(msrA1) SAB1279c(msrA) SAB2535c
            SAA: SAUSA300_1256(msrA) SAUSA300_1317(msrA) SAUSA300_2594(msrA)
            SAO: SAOUHSC_01360 SAOUHSC_01432 SAOUHSC_02996
            SAJ: SaurJH9_1422 SaurJH9_1483 SaurJH9_1484
            SAH: SaurJH1_1450 SaurJH1_1512 SaurJH1_1513
            SEP: SE1042 SE1117 SE2240
            SER: SERP0931(msrA-1) SERP1000(msrA-2) SERP2272
            SHA: SH0343 SH1482 SH1548(msrA)
            SSP: SSP0129 SSP1315 SSP1391
            LMO: lmo1860
            LMF: LMOf2365_1888(msrA)
            LIN: lin1974
            LWE: lwe1879(msrA)
            LLA: L193644(pmsX) L67708(pmsR)
            LLC: LACR_1645 LACR_2288
            LLM: llmg_0201(msrB) llmg_0951(msrA) llmg_2281(pmsR)
            SPY: SPy_0466(msrA.2) SPy_1557(msrA)
            SPZ: M5005_Spy_0382(msrA.2) M5005_Spy_1282(msrA)
            SPM: spyM18_0509(msrA) spyM18_1571
            SPG: SpyM3_0329(msrA.2) SpyM3_1267(msrA.1)
            SPS: SPs0596 SPs1528
            SPH: MGAS10270_Spy0383(msrA2) MGAS10270_Spy1362(msrA)
            SPI: MGAS10750_Spy0381(msrA2) MGAS10750_Spy1389(msrA)
            SPJ: MGAS2096_Spy0400(msrA2) MGAS2096_Spy1301(msrA)
            SPK: MGAS9429_Spy0382(msrA2) MGAS9429_Spy1276(msrA)
            SPF: SpyM50570(msrAB) SpyM50988(csrA) SpyM51486(msrA)
            SPA: M6_Spy0407(msrA) M6_Spy1303
            SPB: M28_Spy0368(msrA.2) M28_Spy1286(msrA)
            SPN: SP_0660 SP_1359
            SPR: spr0577(msrA) spr1217(msrA)
            SPD: SPD_0573(msrAB2) SPD_1193(msrAB1)
            SAG: SAG1510(msrA)
            SAN: gbs1569
            SAK: SAK_1534(msrA)
            SMU: SMU.1622(pmsR)
            STC: str1343(msrA1) str1632(msrA2)
            STL: stu1343(msrA1) stu1632(msrA2)
            SSA: SSA_0374 SSA_1118
            SGO: SGO_0278(msrA) SGO_1176
            LPL: lp_1339(mrsA1) lp_1835(msrA2) lp_1979(msrA4)
            LJO: LJ1331
            LAC: LBA1208(msrA)
            LSA: LSA0866(msrA)
            LSL: LSL_0692(msrA)
            LDB: Ldb0673(msrA)
            LBU: LBUL_0605 LBUL_0965
            LBR: LVIS_0737 LVIS_0810
            LCA: LSEI_1202 LSEI_1393
            LRE: Lreu_0188 Lreu_1198
            EFA: EF1681(msrA)
            OOE: OEOE_0508 OEOE_1538
            STH: STH1761
            CAC: CAC0088
            CPE: CPE2588
            CPF: CPF_2913(msrA)
            CPR: CPR_2591(msrA)
            CTC: CTC00149
            CTH: Cthe_2990
            CBO: CBO1923(msrA)
            CBA: CLB_1861(msrA)
            CBH: CLC_1868(msrA)
            CBF: CLI_1988(msrA)
            CBE: Cbei_1306 Cbei_2461
            CKL: CKL_0343(msrA) CKL_2434(msrB)
            AMT: Amet_3384 Amet_3697
            DSY: DSY1514 DSY4697
            MGE: MG_408
            MPN: MPN607(pmsR)
            MPU: MYPU_7780(pmsR)
            MPE: MYPE5610(pmsR)
            MGA: MGA_0571(msrA)
            MMY: MSC_0774(msrA)
            MMO: MMOB4950(pmsR)
            MCP: MCAP_0722
            UUR: UU289(msrA)
            MFL: Mfl050
            MTU: Rv0137c(msrA)
            MTC: MT0145(msrA)
            MBO: Mb0142c(msrA)
            MLE: ML2647
            MPA: MAP3554c
            MAV: MAV_5159(msrA)
            MSM: MSMEG_2784(msrB) MSMEG_4417(msrA) MSMEG_6477(msrA)
            MVA: Mvan_2487 Mvan_5708 Mvan_5709
            MGI: Mflv_1105 Mflv_1106 Mflv_3916
            MMC: Mmcs_5092
            MKM: Mkms_2262 Mkms_5179 Mkms_5180
            MJL: Mjls_2205 Mjls_5470 Mjls_5471
            CGL: NCgl2825(cgl2926)
            CGB: cg3236(msrA)
            CEF: CE2764(msrA)
            CDI: DIP2260(msrA)
            CJK: jk0110(msrA)
            NFA: nfa32240(msrA)
            RHA: RHA1_ro04011
            SCO: SCO4956(2SCK31.16)
            SMA: SAV3307
            LXX: Lxx06570(msrA)
            CMI: CMM_1446(msrA)
            ART: Arth_2445
            AAU: AAur_1802(msrB) AAur_2415(msrA)
            PAC: PPA0556
            NCA: Noca_0974 Noca_3669
            TFU: Tfu_2678
            FRA: Francci3_3895
            FAL: FRAAL6201(msrA)
            ACE: Acel_1898
            KRA: Krad_1091 Krad_1589
            SEN: SACE_0107(msrA)
            STP: Strop_0918 Strop_1542
            BLO: BL0568(msrA)
            RXY: Rxyl_2864
            FNU: FN0188 FN0803(ccdA)
            RBA: RB11847(msrA) RB11878(msrA)
            PCU: pc0964(msrA)
            TPA: TP0633
            TDE: TDE0709(msrA)
            LIL: LA0600 LA3673
            LIC: LIC10545 LIC12978(msrA)
            LBJ: LBJ_2709(msrA)
            LBL: LBL_0365(msrA)
            SYN: sll1394(msrA) slr1795(msrA)
            SYW: SYNW0560(msrA) SYNW1021(msrA)
            SYC: syc1670_d(msrA) syc2157_d(msrA)
            SYF: Synpcc7942_1937 Synpcc7942_2436
            SYD: Syncc9605_1148 Syncc9605_2114
            SYE: Syncc9902_0559 Syncc9902_1311
            SYG: sync_1640(msrA) sync_2210
            SYR: SynRCC307_0016(msrB) SynRCC307_0339(msrB)
                 SynRCC307_1336(msrA) SynRCC307_1814(msrA)
            SYX: SynWH7803_0016(msrB) SynWH7803_1056(msrA)
                 SynWH7803_1954(msrA) SynWH7803_2126(msrB)
            CYA: CYA_0467(msrA)
            CYB: CYB_0235(msrA)
            TEL: tll0885
            GVI: gll1819 glr2516
            ANA: all1062 alr1675
            AVA: Ava_1180 Ava_3782
            PMA: Pro0740(msrA) Pro1414(msrA)
            PMM: PMM0955(msrA) PMM1333
            PMT: PMT0492(msrA) PMT1408
            PMN: PMN2A_0254 PMN2A_0904
            PMI: PMT9312_0844 PMT9312_1431
            PMB: A9601_00141 A9601_09051 A9601_15331
            PMC: P9515_00141 P9515_10381 P9515_14941
            PMF: P9303_03241 P9303_05541 P9303_17771
            PMG: P9301_00141 P9301_09031 P9301_15191
            PMH: P9215_00141
            PME: NATL1_00141 NATL1_09231 NATL1_17601
            TER: Tery_0394
            BTH: BT_2499
            BFR: BF3573
            BFS: BF3378
            PGI: PG2088(msrA)
            SRU: SRU_1074(msrA) SRU_1576(msrA) SRU_2776
            CHU: CHU_1649(msrA)
            GFO: GFO_1461(msrA) GFO_1585(msrA) GFO_1862(msrB) GFO_1863(msrB)
                 GFO_2710(msrA)
            FJO: Fjoh_0270 Fjoh_0271 Fjoh_2552 Fjoh_2794
            CTE: CT1278(msrA)
            CCH: Cag_0960
            CPH: Cpha266_1459
            PLT: Plut_0905
            DET: DET1241(msrA)
            DEH: cbdb_A1161(msrA)
            DEB: DehaBAV1_1055
            RRS: RoseRS_2424 RoseRS_3364
            RCA: Rcas_3054 Rcas_4142
            DRA: DR_1849
            DGE: Dgeo_0843
            TTH: TT_P0095
            TTJ: TTHB132
            FNO: Fnod_0746
            MMP: MMP0848
            MMQ: MmarC5_1107
            MMZ: MmarC7_0092
            MVN: Mevan_1612
            MAC: MA1431
            MBA: Mbar_A2815
            MMA: MM_2399
            MBU: Mbur_2328
            MHU: Mhun_0652
            MEM: Memar_1027 Memar_1080
            MBN: Mboo_0606 Mboo_1531 Mboo_2160
            MTH: MTH535
            MST: Msp_0737
            MSI: Msm_0582
            HAL: VNG1180G(msrA)
            HMA: rrnAC1491(msrA2) rrnAC2024(msrA1)
            HWA: HQ1843A(msrA)
            NPH: NP0038A(msrA)
            PTO: PTO0143
            TKO: TK0819
            SSO: SSO1503(msr)
            SAI: Saci_1170(msrA)
            MSE: Msed_0712
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.4.11
            ExPASy - ENZYME nomenclature database: 1.8.4.11
            ExplorEnz - The Enzyme Database: 1.8.4.11
            ERGO genome analysis and discovery system: 1.8.4.11
            BRENDA, the Enzyme Database: 1.8.4.11
///
ENTRY       EC 1.8.4.12                 Enzyme
NAME        peptide-methionine (R)-S-oxide reductase;
            MsrB;
            methionine sulfoxide reductase (ambiguous);
            pMSR;
            methionine S-oxide reductase (ambiguous);
            selenoprotein R;
            methionine S-oxide reductase (R-form oxidizing);
            methionine sulfoxide reductase B;
            SelR;
            SelX;
            PilB;
            pRMsr
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a disulfide as acceptor
SYSNAME     peptide-methionine:thioredoxin-disulfide S-oxidoreductase
            [methionine (R)-S-oxide-forming]
REACTION    peptide-L-methionine + thioredoxin disulfide + H2O =
            peptide-L-methionine (R)-S-oxide + thioredoxin [RN:R07607]
ALL_REAC    R07607
SUBSTRATE   peptide-L-methionine [CPD:C03023];
            thioredoxin disulfide [CPD:C00343];
            H2O [CPD:C00001]
PRODUCT     peptide-L-methionine (R)-S-oxide [CPD:C15653];
            thioredoxin [CPD:C00342]
COMMENT     The reaction occurs in the reverse direction to that shown above.
            The enzyme exhibits high specificity for reduction of the R-form of
            methionine S-oxide, with higher activity being observed with
            L-methionine S-oxide than with D-methionine S-oxide [9]. While both
            free and protein-bound methionine (R)-S-oxide act as substrates, the
            activity with the peptide-bound form is far greater [10]. The enzyme
            plays a role in preventing oxidative-stress damage caused by
            reactive oxygen species by reducing the oxidized form of methionine
            back to methionine and thereby reactivating peptides that had been
            damaged. In some species, e.g. Neisseria meningitidis, both this
            enzyme and EC 1.8.4.11, peptide-methionine (S)-S-oxide reductase,
            are found within the same protein whereas in other species, they are
            separate proteins [3,5]. The reaction proceeds via a sulfenic-acid
            intermediate [5,10]. For MsrB2 and MsrB3, thioredoxin is a poor
            reducing agent but thionein works well [11]. The enzyme from some
            species contains selenocysteine and Zn2+.
REFERENCE   1  [PMID:11779133]
  AUTHORS   Moskovitz J, Singh VK, Requena J, Wilkinson BJ, Jayaswal RK,
            Stadtman ER.
  TITLE     Purification and characterization of methionine sulfoxide reductases
            from mouse and Staphylococcus aureus and their substrate
            stereospecificity.
  JOURNAL   Biochem. Biophys. Res. Commun. 290 (2002) 62-5.
  ORGANISM  Staphylococcus aureus, mouse [GN:mmu]
REFERENCE   2  [PMID:12837786]
  AUTHORS   Taylor AB, Benglis DM Jr, Dhandayuthapani S, Hart PJ.
  TITLE     Structure of Mycobacterium tuberculosis methionine sulfoxide
            reductase A in complex with protein-bound methionine.
  JOURNAL   J. Bacteriol. 185 (2003) 4119-26.
  ORGANISM  Mycobacterium tuberculosis
REFERENCE   3  [PMID:14523107]
  AUTHORS   Singh VK, Moskovitz J.
  TITLE     Multiple methionine sulfoxide reductase genes in Staphylococcus
            aureus: expression of activity and roles in tolerance of oxidative
            stress.
  JOURNAL   Microbiology. 149 (2003) 2739-47.
  ORGANISM  Staphylococcus aureus
REFERENCE   4  [PMID:15680231]
  AUTHORS   Boschi-Muller S, Olry A, Antoine M, Branlant G.
  TITLE     The enzymology and biochemistry of methionine sulfoxide reductases.
  JOURNAL   Biochim. Biophys. Acta. 1703 (2005) 231-8.
  ORGANISM  Escherichia coli [GN:eco], Saccharomyces cerevisiae [GN:sce],
            Neisseria meningitidis
REFERENCE   5  [PMID:15680230]
  AUTHORS   Ezraty B, Aussel L, Barras F.
  TITLE     Methionine sulfoxide reductases in prokaryotes.
  JOURNAL   Biochim. Biophys. Acta. 1703 (2005) 221-9.
  ORGANISM  Staphylococcus aureus, Escherichia coli [GN:eco], Bacillus subtilis
            [GN:bsu]
REFERENCE   6  [PMID:15680228]
  AUTHORS   Weissbach H, Resnick L, Brot N.
  TITLE     Methionine sulfoxide reductases: history and cellular role in
            protecting against oxidative damage.
  JOURNAL   Biochim. Biophys. Acta. 1703 (2005) 203-12.
  ORGANISM  Mycobacterium tuberculosis, Escherichia coli [GN:eco], Neisseria
            meningitidis, cow [GN:bta], Helicobacteria pylori, Haemophilus
            influenzae, Streptococcus pneumoniae, Streptococcus gordonii
REFERENCE   7  [PMID:15680233]
  AUTHORS   Kauffmann B, Aubry A, Favier F.
  TITLE     The three-dimensional structures of peptide methionine sulfoxide
            reductases: current knowledge and open questions.
  JOURNAL   Biochim. Biophys. Acta. 1703 (2005) 249-60.
  ORGANISM  Mycobacterium tuberculosis, Escherichia coli [GN:eco], Bacillus
            subtilis [GN:bsu], cow [GN:bta], Deinococcus radiodurans [GN:dra]
REFERENCE   8  [PMID:12693988]
  AUTHORS   Vougier S, Mary J, Friguet B.
  TITLE     Subcellular localization of methionine sulphoxide reductase A
            (MsrA): evidence for mitochondrial and cytosolic isoforms in rat
            liver cells.
  JOURNAL   Biochem. J. 373 (2003) 531-7.
  ORGANISM  rat [GN:rno]
REFERENCE   9  [PMID:11812798]
  AUTHORS   Olry A, Boschi-Muller S, Marraud M, Sanglier-Cianferani S, Van
            Dorsselear A, Branlant G.
  TITLE     Characterization of the methionine sulfoxide reductase activities of
            PILB, a probable virulence factor from Neisseria meningitidis.
  JOURNAL   J. Biol. Chem. 277 (2002) 12016-22.
  ORGANISM  Staphylococcus aureus, Escherichia coli [GN:eco], Neisseria
            meningitidis, Streptococcus pneumoniae, Erwinia chrysanthemi,
            Mycoplasma genitalium [GN:mge], Neisseria gonorrhoeae [GN:ngo]
REFERENCE   10 [PMID:16735467]
  AUTHORS   Sagher D, Brunell D, Hejtmancik JF, Kantorow M, Brot N, Weissbach H.
  TITLE     Thionein can serve as a reducing agent for the methionine sulfoxide
            reductases.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 8656-61.
  ORGANISM  Escherichia coli [GN:eco], cow [GN:bta]
ORTHOLOGY   KO: K07305  peptide-methionine (R)-S-oxide reductase
GENES       ECO: b1778(yeaA)
            ECJ: JW1767(yeaA)
            ECE: Z2817(yeaA)
            ECS: ECs2487
            ECC: c2183(yeaA)
            ECI: UTI89_C1974(msrB)
            ECP: ECP_1726
            ECV: APECO1_846(yeaA)
            STY: STY1824
            STT: t1170
            SPT: SPA1553(yeaA)
            SEC: SC1304(yeaA)
            STM: STM1291(yeaA)
            YPE: YPO2158
            YPK: y2164
            YPM: YP_1958
            YPA: YPA_1515
            YPN: YPN_1624
            YPS: YPTB2084
            SFL: SF1445(yeaA)
            SFX: S1560(yeaA)
            SFV: SFV_1437(yeaA)
            SSN: SSON_1385(yeaA)
            SBO: SBO_1317(yeaA)
            SDY: SDY_1489(yeaA)
            ECA: ECA2343(msrB)
            PLU: plu2557(msrB)
            SGL: SG1348
            HIN: HI1455(msrA)
            HIT: NTHI1677(msaB)
            HDU: HD1290(msrB)
            HSO: HS_1687(msrAB)
            PMU: PM0923
            APL: APL_0433(msrB) APL_1024
            XFA: XF0849
            XFT: PD1825
            XCC: XCC3651
            XCB: XC_3722
            XCV: XCV3812(msrB)
            XAC: XAC3691
            XOO: XOO0690
            XOM: XOO_0627(XOO0627)
            VCH: VC1998 VCA0615
            VVU: VV1_3139 VV2_1649
            VVY: VV1148 VVA0461
            VPA: VP2156 VPA0207
            VFI: VF0914 VFA0005
            PPR: PBPRA2601(msrB)
            PAE: PA2827
            PPU: PP_1873
            PST: PSPTO_1780
            PSB: Psyr_3614
            PSP: PSPPH_3630(msrB)
            PFL: PFL_4246(msrB)
            PFO: Pfl_3982
            PEN: PSEEN1584(msrB)
            PAR: Psyc_0718 Psyc_1043
            PCR: Pcryo_0693 Pcryo_1088 Pcryo_1427
            ACI: ACIAD2086(msrB)
            SON: SO_2588
            SDN: Sden_2304
            SFR: Sfri_1488
            SBL: Sbal_1857
            SLO: Shew_1591
            SHE: Shewmr4_2184
            SHM: Shewmr7_2261
            SHN: Shewana3_2393 Shewana3_4326 Shewana3_4333
            SHW: Sputw3181_2271
            ILO: IL1264 IL1525
            CPS: CPS_2342(msrB1) CPS_3070(msrB2) CPS_3367(msrAB)
            PHA: PSHAa1087(msrB) PSHAa1444(msrC)
            PAT: Patl_1638
            SDE: Sde_1165 Sde_3185
            CBU: CBU_1306(msrA)
            LPN: lpg1105 lpg2099 lpg2111 lpg2908(msrA)
            LPF: lpl1104 lpl2825
            LPP: lpp1104 lpp2977
            MCA: MCA1955
            FTU: FTT0878c(msrB) FTT1105c(msrA1)
            FTF: FTF0878c(msrB) FTF1105c(msrA1)
            FTL: FTL_0379 FTL_1093
            FTH: FTH_0372(msrB) FTH_1069(msrA1)
            FTN: FTN_0404 FTN_0769
            TCX: Tcr_0783
            NOC: Noc_0985 Noc_2728
            AEH: Mlg_1780 Mlg_2039
            HCH: HCH_02302
            CSA: Csal_1350 Csal_2656
            ABO: ABO_1531(msrB) ABO_2703(msrA)
            AHA: AHA_3614(msrB)
            NME: NMB0044
            NMA: NMA0290(pilB)
            NGO: NGO2059
            CVI: CV_3212(trh1)
            RSO: RSc1747(RS02935)
            REU: Reut_A1395
            RME: Rmet_1172 Rmet_1865
            BMA: BMA1441(msrB)
            BXE: Bxe_A2277
            BUR: Bcep18194_A5210 Bcep18194_C6665
            BCN: Bcen_1586 Bcen_6170
            BCH: Bcen2424_1909 Bcen2424_6245
            BAM: Bamb_1897 Bamb_5959
            BPS: BPSL1421(msrB)
            BPM: BURPS1710b_2458(msrB)
            BTE: BTH_I2139(msrB)
            BPE: BP3564(msrB)
            BPA: BPP3349(msrB)
            BBR: BB3800(msrB)
            RFR: Rfer_2396
            POL: Bpro_2582 Bpro_2740
            NEU: NE1701(msrA)
            NET: Neut_0419
            NMU: Nmul_A0327 Nmul_A2110
            EBA: ebA5827(msrB) ebA875
            DAR: Daro_1889
            TBD: Tbd_1105 Tbd_2631
            MFA: Mfla_0013
            HPY: HP0224(msrA)
            HPJ: jhp0210
            HPA: HPAG1_0226
            HHE: HH1416
            HAC: Hac_1495(msrA)
            TDN: Tmden_0012
            CJE: Cj1112c
            CJR: CJE1255(msrB)
            CFF: CFF8240_1279
            GSU: GSU2451
            GME: Gmet_0222
            PCA: Pcar_2611
            PPD: Ppro_2948
            DVU: DVU0576(msrB)
            DDE: Dde_0704 Dde_1003
            BBA: Bd0757 Bd1365
            DPS: DP1227
            ADE: Adeh_0325
            MXA: MXAN_2350(msrB) MXAN_6864(msrBA)
            SAT: SYN_01261
            SFU: Sfum_2571
            PUB: SAR11_1365
            MLO: mll4820 mlr3964
            MES: Meso_0379 Meso_0863
            SME: SMa1894 SMc00117 SMc01724
            ATU: Atu0908
            ATC: AGR_C_1655
            RET: RHE_CH01247(msrB)
            RLE: RL1370(msrB) RL4265(msrB)
            BME: BMEII0819
            BMF: BAB2_0792
            BMS: BRA0446
            BMB: BruAb2_0776
            BJA: bll5855 blr7044
            RPA: RPA3937 RPA4069
            RPB: RPB_1518 RPB_3821
            RPC: RPC_1480 RPC_3833
            RPD: RPD_1459 RPD_1663
            RPE: RPE_1500 RPE_3958
            NWI: Nwi_2960
            NHA: Nham_1128 Nham_1330
            CCR: CC_2183
            SIL: SPO3741(msrB)
            SIT: TM1040_2803 TM1040_3781
            RSP: RSP_2617
            JAN: Jann_0834 Jann_2143
            RDE: RD1_0597(msrB)
            MMR: Mmar10_0879
            HNE: HNE_0120(msrB1)
            NAR: Saro_0221 Saro_3328
            SAL: Sala_0125 Sala_2864 Sala_2975
            ELI: ELI_11350 ELI_12450(selR)
            GOX: GOX0328
            GBE: GbCGDNIH1_2159
            RRU: Rru_A1907
            MAG: amb4119
            MGM: Mmc1_2336
            ABA: Acid345_2786 Acid345_3736
            SUS: Acid_0169
            BSU: BG11628(yppQ)
            BHA: BH1447
            BAN: BA5687(msrA-2)
            BAR: GBAA5687(msrA-2)
            BAA: BA_0545
            BAT: BAS5290
            BCE: BC5436
            BCA: BCE_5569(msrA)
            BCZ: BCZK5132(msrA)
            BTK: BT9727_5115(msrA)
            BTL: BALH_4939(msrA)
            BLI: BL01422(mrsB)
            BLD: BLi02302(yppQ)
            BCL: ABC1747
            OIH: OB1734
            SAU: SA1256
            SAV: SAV1423
            SAM: MW1313
            SAR: SAR1436
            SAS: SAS1366
            SAB: SAB1278c
            SAO: SAOUHSC_01431
            SEP: SE1116
            SER: SERP0999(msrB)
            SHA: SH1483(msrB)
            SSP: SSP1316(msrB)
            LMO: lmo1859
            LMF: LMOf2365_1887
            LIN: lin1973
            LWE: lwe1878(mrsB)
            LLA: L192996(ybjA)
            LLC: LACR_0195
            SPY: SPy_1055(csrA) SPy_1557(msrA)
            SPZ: M5005_Spy_0778(msrB) M5005_Spy_1282(msrA)
            SPM: spyM18_1032 spyM18_1571
            SPG: SpyM3_0739(csrA) SpyM3_1267(msrA.1)
            SPS: SPs0596 SPs0940
            SPH: MGAS10270_Spy0894(msrB) MGAS10270_Spy1362(msrA)
            SPI: MGAS10750_Spy0929(msrB) MGAS10750_Spy1389(msrA)
            SPJ: MGAS2096_Spy0852(msrB) MGAS2096_Spy1301(msrA)
            SPK: MGAS9429_Spy0895(msrB) MGAS9429_Spy1276(msrA)
            SPA: M6_Spy0798(msrB) M6_Spy1303
            SPB: M28_Spy0755(msrB) M28_Spy1286(msrA)
            SPN: SP_0660 SP_1359
            SPR: spr0577(msrA) spr1217(msrA)
            SPD: SPD_0573(msrAB2) SPD_1193(msrAB1)
            SAG: SAG0910
            SAN: gbs0921
            SAK: SAK_1026(msrB)
            STC: str1343(msrA1)
            STL: stu1343(msrA1)
            LPL: lp_1836(msrA3)
            LJO: LJ1389
            LAC: LBA1374(msrA)
            LSA: LSA0865
            LSL: LSL_0029
            LDB: Ldb1971(msrB)
            LBU: LBUL_1833
            LBR: LVIS_0809
            LCA: LSEI_1525
            EFA: EF3164
            OOE: OEOE_1554
            STH: STH1761
            CAC: CAC1550
            CPE: CPE1607
            DSY: DSY1514 DSY4697
            MGE: MG_448
            MPN: MPN662(pilB)
            MPU: MYPU_5060(pmsR)
            MGA: MGA_0149
            MMY: MSC_0774(msrA)
            MMO: MMOB2320(pmsR)
            MHY: mhp546(pmsR)
            MHJ: MHJ_0530(pmsR)
            MHP: MHP7448_0529(pmsR)
            MCP: MCAP_0722
            MTU: Rv2674
            MTC: MT2748
            MBO: Mb2693
            MPA: MAP2794
            MMC: Mmcs_2216 Mmcs_5091
            CGL: NCgl1823(cgl1898)
            CEF: CE1791
            CDI: DIP1393
            CJK: jk1072(msrB)
            NFA: nfa37350
            RHA: RHA1_ro06862
            SCO: SCO6061(SC9B1.08)
            SMA: SAV2204
            LXX: Lxx06560(msrB) Lxx18050
            ART: Arth_1661
            PAC: PPA1065
            TFU: Tfu_1893
            FRA: Francci3_2268
            FAL: FRAAL3773(msrB)
            ACE: Acel_1379
            SEN: SACE_1845(msrB)
            BLO: BL0568(msrA)
            RXY: Rxyl_0660
            FNU: FN0188 FN0803(ccdA)
            RBA: RB2268(msrB) RB7900(msrB)
            PCU: pc0964(msrA)
            TDE: TDE0709(msrA)
            LIL: LA0824
            LIC: LIC12800
            LBJ: LBJ_0547
            LBL: LBL_2533
            SYN: sll1680
            SYW: SYNW0016 SYNW0338
            SYC: syc1161_d syc1907_c
            SYF: Synpcc7942_0352 Synpcc7942_2190
            SYD: Syncc9605_0016 Syncc9605_2257
            SYE: Syncc9902_0016 Syncc9902_0423
            SYG: sync_0016(msrB-1) sync_2456(msrB-2)
            TEL: tlr1214
            GVI: gll4019 glr4339
            ANA: alr3901
            AVA: Ava_1796
            PMA: Pro0015
            PMM: PMM0015
            PMT: PMT0016 PMT1586
            PMN: PMN2A_1342
            PMI: PMT9312_0015
            TER: Tery_4070
            BTH: BT_2499
            BFR: BF3573
            BFS: BF3378
            PGI: PG2088(msrA)
            CHU: CHU_0754(msrB)
            CTE: CT0103 CT1278(msrA)
            CCH: Cag_0960
            CPH: Cpha266_0090 Cpha266_1459
            PLT: Plut_0905
            DEH: cbdb_A1163(msrB)
            DRA: DR_1378
            DGE: Dgeo_2072
            MAC: MA0449
            MBA: Mbar_A0743
            MMA: MM_1634
            MBU: Mbur_2329
            MHU: Mhun_2964
            MTH: MTH711
            MST: Msp_0737
            HAL: VNG1404G(trh1)
            HMA: rrnAC0109(msrB)
            HWA: HQ1930A(msrB) HQ2921A(msrB)
            NPH: NP0048A(msrB)
            TKO: TK0819
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.4.12
            ExPASy - ENZYME nomenclature database: 1.8.4.12
            ExplorEnz - The Enzyme Database: 1.8.4.12
            ERGO genome analysis and discovery system: 1.8.4.12
            BRENDA, the Enzyme Database: 1.8.4.12
///
ENTRY       EC 1.8.4.13                 Enzyme
NAME        L-methionine (S)-S-oxide reductase;
            fSMsr;
            methyl sulfoxide reductase I and II;
            acetylmethionine sulfoxide reductase;
            methionine sulfoxide reductase;
            L-methionine:oxidized-thioredoxin S-oxidoreductase;
            methionine-S-oxide reductase;
            free-methionine (S)-S-oxide reductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a disulfide as acceptor
SYSNAME     L-methionine:thioredoxin-disulfide S-oxidoreductase
REACTION    L-methionine + thioredoxin disulfide + H2O = L-methionine
            (S)-S-oxide + thioredoxin [RN:R07606]
ALL_REAC    R07606;
            (other) R02025
SUBSTRATE   L-methionine [CPD:C00073];
            thioredoxin disulfide [CPD:C00343];
            H2O [CPD:C00001]
PRODUCT     L-methionine (S)-S-oxide [CPD:C15999];
            thioredoxin [CPD:C00342]
COMMENT     Requires NADPH [2]. The reaction occurs in the opposite direction to
            that given above. Dithiothreitol can replace reduced thioredoxin.
            L-Methionine (R)-S-oxide is not a substrate [see EC 1.8.4.14,
            L-methionine (R)-S-oxide reductase].
REFERENCE   1
  AUTHORS   Black, S., Harte, E.M., Hudson, B. and Wartofsky, L.
  TITLE     A specific enzymatic reduction of L-(-)methionine sulfoxide and a
            related nonspecific reduction of diulfides.
  JOURNAL   J. Biol. Chem. 235 (1960) 2910-2916.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:37234]
  AUTHORS   Ejiri SI, Weissbach H, Brot N.
  TITLE     Reduction of methionine sulfoxide to methionine by Escherichia coli.
  JOURNAL   J. Bacteriol. 139 (1979) 161-4.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:6999943]
  AUTHORS   Ejiri SI, Weissbach H, Brot N.
  TITLE     The purification of methionine sulfoxide reductase from Escherichia
            coli.
  JOURNAL   Anal. Biochem. 102 (1980) 393-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:15680228]
  AUTHORS   Weissbach H, Resnick L, Brot N.
  TITLE     Methionine sulfoxide reductases: history and cellular role in
            protecting against oxidative damage.
  JOURNAL   Biochim. Biophys. Acta. 1703 (2005) 203-12.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K00388  methionine (S)-S-oxide reductase
GENES       BMV: BMASAVP1_A0655(msrA)
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.4.13
            ExPASy - ENZYME nomenclature database: 1.8.4.13
            ExplorEnz - The Enzyme Database: 1.8.4.13
            ERGO genome analysis and discovery system: 1.8.4.13
            BRENDA, the Enzyme Database: 1.8.4.13
///
ENTRY       EC 1.8.4.14                 Enzyme
NAME        L-methionine (R)-S-oxide reductase;
            fRMsr;
            FRMsr;
            free met-R-(o) reductase;
            free-methionine (R)-S-oxide reductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a disulfide as acceptor
SYSNAME     L-methionine:thioredoxin-disulfide S-oxidoreductase [L-methionine
            (R)-S-oxide-forming]
REACTION    L-methionine + thioredoxin disulfide + H2O = L-methionine
            (R)-S-oxide + thioredoxin [RN:R07608]
ALL_REAC    R07608;
            (other) R02025
SUBSTRATE   L-methionine [CPD:C00073];
            thioredoxin disulfide [CPD:C00343];
            H2O [CPD:C00001]
PRODUCT     L-methionine (R)-S-oxide [CPD:C15998];
            thioredoxin [CPD:C00342]
COMMENT     Requires NADPH. Unlike EC 1.8.4.12, peptide-methionine (R)-S-oxide
            reductase, this enzyme cannot use peptide-bound methionine
            (R)-S-oxide as a substrate [1]. Differs from EC 1.8.4.13,
            L-methionine (S)-S-oxide in that L-methionine (S)-S-oxide is not a
            substrate.
REFERENCE   1  [PMID:12504094]
  AUTHORS   Etienne F, Spector D, Brot N, Weissbach H.
  TITLE     A methionine sulfoxide reductase in Escherichia coli that reduces
            the R enantiomer of methionine sulfoxide.
  JOURNAL   Biochem. Biophys. Res. Commun. 300 (2003) 378-82.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K08968  methionine (R)-S-oxide reductase
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.4.14
            ExPASy - ENZYME nomenclature database: 1.8.4.14
            ExplorEnz - The Enzyme Database: 1.8.4.14
            ERGO genome analysis and discovery system: 1.8.4.14
            BRENDA, the Enzyme Database: 1.8.4.14
///
ENTRY       EC 1.8.4.-                  Enzyme
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a disulfide as acceptor
REACTION    2 Glutathione <=> Glutathione disulfide [RN:R00500]
SUBSTRATE   Glutathione [CPD:C00051]
PRODUCT     Glutathione disulfide [CPD:C00127]
///
ENTRY       EC 1.8.5.1                  Enzyme
NAME        glutathione dehydrogenase (ascorbate);
            dehydroascorbic reductase;
            dehydroascorbic acid reductase;
            glutathione dehydroascorbate reductase;
            DHA reductase ;
            dehydroascorbate reductase;
            GDOR;
            glutathione:dehydroascorbic acid oxidoreductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a quinone or similar compound as acceptor
SYSNAME     glutathione:dehydroascorbate oxidoreductase
REACTION    2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
            [RN:R01112]
ALL_REAC    R01112 > R01108
SUBSTRATE   glutathione [CPD:C00051];
            dehydroascorbate [CPD:C00425]
PRODUCT     glutathione disulfide [CPD:C00127];
            ascorbate [CPD:C00072]
REFERENCE   1
  AUTHORS   Crook, E.M.
  TITLE     The system dehydroascorbic acid-glutathione.
  JOURNAL   Biochem. J. 35 (1941) 226-236.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
            PATH: map00251  Glutamate metabolism
            PATH: map00480  Glutathione metabolism
STRUCTURES  PDB: 2HZE  2HZF  
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.5.1
            ExPASy - ENZYME nomenclature database: 1.8.5.1
            ExplorEnz - The Enzyme Database: 1.8.5.1
            ERGO genome analysis and discovery system: 1.8.5.1
            BRENDA, the Enzyme Database: 1.8.5.1
            CAS: 9026-38-4
///
ENTRY       EC 1.8.5.2                  Enzyme
NAME        thiosulfate dehydrogenase (quinone);
            thiosulfate:quinone oxidoreductase;
            thiosulphate:quinone oxidoreductase;
            thiosulfate oxidoreductase, tetrathionate-forming;
            TQO
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a quinone or similar compound as acceptor
SYSNAME     thiosulfate:6-decylubiquinone oxidoreductase
REACTION    2 thiosulfate + 2 6-decylubiquinone = tetrathionate + 2
            6-decylubiquinol [RN:R07177]
ALL_REAC    R07177
SUBSTRATE   thiosulfate [CPD:C00320];
            6-decylubiquinone [CPD:C15494]
PRODUCT     tetrathionate [CPD:C02084];
            6-decylubiquinol [CPD:C15495]
COMMENT     The reaction can also proceed with ferricyanide as the electron
            acceptor, but more slowly. Unlike EC 1.8.2.2, thiosulfate
            dehydrogenase, this enzyme cannot utilize cytochrome c as an
            acceptor.
REFERENCE   1  [PMID:15306018]
  AUTHORS   Muller FH, Bandeiras TM, Urich T, Teixeira M, Gomes CM, Kletzin A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase.
  JOURNAL   Mol. Microbiol. 53 (2004) 1147-60.
  ORGANISM  Acidianus ambivalens
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.5.2
            ExPASy - ENZYME nomenclature database: 1.8.5.2
            ExplorEnz - The Enzyme Database: 1.8.5.2
            ERGO genome analysis and discovery system: 1.8.5.2
            BRENDA, the Enzyme Database: 1.8.5.2
///
ENTRY       EC 1.8.6.1        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With a nitrogenous group as acceptor (deleted sub-subclass)
COMMENT     Deleted entry: Nitrate-ester reductase. Now included with EC
            2.5.1.18 glutathione transferase (EC 1.8.6.1 created 1961, deleted
            1976)
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.6.1
            ExPASy - ENZYME nomenclature database: 1.8.6.1
            ExplorEnz - The Enzyme Database: 1.8.6.1
            ERGO genome analysis and discovery system: 1.8.6.1
            BRENDA, the Enzyme Database: 1.8.6.1
///
ENTRY       EC 1.8.7.1                  Enzyme
NAME        sulfite reductase (ferredoxin);
            ferredoxin-sulfite reductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With an iron-sulfur protein as acceptor
SYSNAME     hydrogen-sulfide:ferredoxin oxidoreductase
REACTION    hydrogen sulfide + 6 oxidized ferredoxin + 3 H2O = sulfite + 6
            reduced ferredoxin + 6 H+ [RN:R00859]
ALL_REAC    R00859;
            (other) R03600
SUBSTRATE   hydrogen sulfide [CPD:C00283];
            oxidized ferredoxin [CPD:C00139];
            H2O [CPD:C00001]
PRODUCT     sulfite [CPD:C00094];
            reduced ferredoxin [CPD:C00138];
            H+ [CPD:C00080]
COFACTOR    Iron [CPD:C00023]
COMMENT     An iron protein.
REFERENCE   1  [PMID:4390248]
  AUTHORS   Schmidt A, Trebst A.
  TITLE     The mechanism of photosynthetic sulfate reduction by isolated
            chloroplasts.
  JOURNAL   Biochim. Biophys. Acta. 180 (1969) 529-35.
  ORGANISM  spinach
PATHWAY     PATH: map00450  Selenoamino acid metabolism
            PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K00392  sulfite reductase (ferredoxin)
GENES       ATH: AT5G04590(SIR)
            OSA: 4339248
            CME: CMG021C CMJ117C
            PIC: PICST_67906(ECM17.1)
            SPO: SPAC4C5.05c
            UMA: UM02922.1
            ENT: Ent638_3226
            PPF: Pput_3324
            PMY: Pmen_2147
            ACI: ACIAD2982(cysI)
            SAZ: Sama_2838
            MMW: Mmwyl1_2345 Mmwyl1_3156
            BPE: BP3432(cysI)
            BPA: BPP0395(cysI)
            BBR: BB0397(cysI)
            PLA: Plav_0889
            OAN: Oant_0190
            SWI: Swit_4058
            GOX: GOX1198
            GBE: GbCGDNIH1_0909
            CBE: Cbei_3024
            AMT: Amet_3499
            MAV: MAV_1787 MAV_2154
            MSM: MSMEG_4527
            RBA: RB7465(sir)
            LIL: LA4216(sirA)
            SYN: slr0963(sir)
            SYW: SYNW1095(sir)
            SYC: syc1478_c(sir)
            SYF: Synpcc7942_0019
            SYD: Syncc9605_1227
            SYE: Syncc9902_1242
            SYG: sync_1280
            SYR: SynRCC307_1269(sir)
            SYX: SynWH7803_1319(sir)
            CYA: CYA_0952(sir)
            CYB: CYB_0180(sir)
            TEL: tlr0339(sir)
            GVI: glr1848(sir)
            ANA: alr1348(sir)
            AVA: Ava_5043
            PMA: Pro0830(sir)
            PMM: PMM0758(sir)
            PMT: PMT0579(sir)
            PMB: A9601_08201(sir)
            PMC: P9515_08251(sir)
            PMF: P9303_16711(sir)
            PMG: P9301_08181(sir)
            PME: NATL1_07941(sir)
            GFO: GFO_0327(sir)
            FJO: Fjoh_1504
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.7.1
            ExPASy - ENZYME nomenclature database: 1.8.7.1
            ExplorEnz - The Enzyme Database: 1.8.7.1
            ERGO genome analysis and discovery system: 1.8.7.1
            BRENDA, the Enzyme Database: 1.8.7.1
            CAS: 37256-50-1
///
ENTRY       EC 1.8.98.1                 Enzyme
NAME        CoB---CoM heterodisulfide reductase;
            heterodisulfide reductase;
            soluble heterodisulfide reductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With other, known, acceptors
SYSNAME     coenzyme B:coenzyme M:methanophenazine oxidoreductase
REACTION    coenzyme B + coenzyme M + methanophenazine =
            N-{7-[(2-sulfoethyl)dithio]heptanoyl}-O3-phospho-L-threonine +
            dihydromethanophenazine [RN:R04540]
ALL_REAC    R04540
SUBSTRATE   coenzyme B [CPD:C04628];
            coenzyme M [CPD:C03576];
            methanophenazine [CPD:C11903]
PRODUCT     N-{7-[(2-sulfoethyl)dithio]heptanoyl}-O3-phospho-L-threonine;
            dihydromethanophenazine [CPD:C11904]
COMMENT     This enzyme is found in methanogenic archaea, particularly
            Methanosarcina species, and regenerates coenzyme M and coenzyme B
            after the action of EC 2.8.4.1, coenzyme-B
            sulfoethylthiotransferase. Contains (per heterodimeric unit) two
            distinct b-type hemes and two [4Fe-4S] clusters [3]. Highly specific
            for both coenzyme M and coenzyme B. Reacts with various phenazine
            derivatives, including 2-hydroxyphenazine and 2-bromophenazine.
REFERENCE   1  [PMID:2121478]
  AUTHORS   Hedderich R, Berkessel A, Thauer RK.
  TITLE     Purification and properties of heterodisulfide reductase from
            Methanobacterium thermoautotrophicum (strain Marburg).
  JOURNAL   Eur. J. Biochem. 193 (1990) 255-61.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
REFERENCE   2  [PMID:9555882]
  AUTHORS   Abken HJ, Tietze M, Brodersen J, Baumer S, Beifuss U, Deppenmeier U.
  TITLE     Isolation and characterization of methanophenazine and function of
            phenazines in membrane-bound electron transport of Methanosarcina
            mazei Go1.
  JOURNAL   J. Bacteriol. 180 (1998) 2027-32.
  ORGANISM  Methanosarcina mazei [GN:mma]
REFERENCE   3  [PMID:9665708]
  AUTHORS   Simianu M, Murakami E, Brewer JM, Ragsdale SW.
  TITLE     Purification and properties of the heme- and iron-sulfur-containing
            heterodisulfide reductase from Methanosarcina thermophila.
  JOURNAL   Biochemistry. 37 (1998) 10027-39.
  ORGANISM  Methanosarcina thermophila
REFERENCE   4  [PMID:11034998]
  AUTHORS   Murakami E, Deppenmeier U, Ragsdale SW.
  TITLE     Characterization of the intramolecular electron transfer pathway
            from 2-hydroxyphenazine to the heterodisulfide reductase from
            Methanosarcina thermophila.
  JOURNAL   J. Biol. Chem. 276 (2001) 2432-9.
  ORGANISM  Methanosarcina thermophila
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K03388  heterodisulfide reductase subunit A
            KO: K03389  heterodisulfide reductase subunit B
            KO: K03390  heterodisulfide reductase subunit C
            KO: K08263  heterodisulfide reductase
            KO: K08264  heterodisulfide reductase subunit D
            KO: K08265  heterodisulfide reductase subunit E
GENES       ECI: UTI89_C0330(ykgF)
            BUR: Bcep18194_A5437 Bcep18194_B0031 Bcep18194_B0575
            HAR: HEAR0286(glcF)
            TBD: Tbd_1645 Tbd_1646 Tbd_1648
            GSU: GSU0090 GSU0091 GSU0092
            GME: Gmet_2084 Gmet_3424 Gmet_3425 Gmet_3426
            GUR: Gura_0150 Gura_3582
            DVU: DVU0848 DVU0849 DVU2402(hdrA) DVU2403(hdrB) DVU2404(hdrC)
            DVL: Dvul_0827
            DDE: Dde_1111 Dde_1112 Dde_1207 Dde_1208 Dde_1209 Dde_3524
                 Dde_3525 Dde_3526
            DPS: DP1010 DP1106(hdrA)
            ADE: Adeh_4164
            SAT: SYN_00626
            SFU: Sfum_0819
            MAG: amb4130
            MGM: Mmc1_0428
            CHY: CHY_0927 CHY_0929 CHY_0930
            DRM: Dred_0357 Dred_0433 Dred_0634
            SWO: Swol_0395
            MTA: Moth_0439 Moth_0440 Moth_0810 Moth_0812 Moth_1195
            RHA: RHA1_ro03479
            SEN: SACE_3507
            SYN: slr0201(hdrB)
            ANA: all3341
            TER: Tery_0453
            CTE: CT0866(hdrA-1) CT1245 CT1246(hdrA-2)
            CCH: Cag_1028 Cag_1029 Cag_1584
            CPH: Cpha266_0175 Cpha266_1261
            PVI: Cvib_0844 Cvib_1636
            PLT: Plut_1108 Plut_1109
            AAE: aq_395(hdrA) aq_398(hdrC) aq_400(hdrB)
            MJA: MJ0743(hdrB1) MJ0744(hdrC) MJ0863(hdrB2) MJ0864(hdrC2)
                 MJ1190m(hdrA)
            MMP: MMP0825(hdrA) MMP1053(hdrB2) MMP1054(hdrC2) MMP1154(hdrC1)
                 MMP1155(hdrB1) MMP1697(hdrA)
            MMQ: MmarC5_0432 MmarC5_0433 MmarC5_0539 MmarC5_0540
            MMZ: MmarC7_0307 MmarC7_0308 MmarC7_0402 MmarC7_0403
            MAE: Maeo_0307 Maeo_0308
            MVN: Mevan_0376 Mevan_0377 Mevan_0474 Mevan_0475
            MAC: MA0687(hdrE) MA0688(hdrD) MA2868(hdrA) MA3126(hdrB)
                 MA3127(hdrC) MA3128(hdrA) MA4236(hdrC) MA4237(hdrB)
            MBA: Mbar_A0639 Mbar_A0640 Mbar_A1598 Mbar_A1599 Mbar_A1952(hdrA)
                 Mbar_A1953(hdrC) Mbar_A1954 Mbar_A2589
            MMA: MM_0056 MM_0387(hdrA) MM_0388(hdrC) MM_0389(hdrB) MM_0979
                 MM_0980 MM_1843(hdrE) MM_1844(hdrD)
            MBU: Mbur_0552 Mbur_0952 Mbur_1516 Mbur_1517 Mbur_1774 Mbur_2436
                 Mbur_2437
            MTP: Mthe_0980 Mthe_1573
            MHU: Mhun_1836 Mhun_1837 Mhun_1838
            MLA: Mlab_0344
            MEM: Memar_0624
            MBN: Mboo_0589
            MTH: MTH1381 MTH1878 MTH1879
            MST: Msp_0125(hdrC2) Msp_0126(hdrB2) Msp_0127(hdrA2)
                 Msp_1013(hdrB1) Msp_1014(hdrC1) Msp_1476(hdrA1)
            MSI: Msm_0795 Msm_0796 Msm_1336
            MKA: MK0249(hdrA_1) MK0265(hdrA_2) MK0572(hdrB) MK0573(hdrC)
            AFU: AF0661 AF0663(hdrA-1) AF1238 AF1375(hdrB) AF1376(hdrC)
                 AF1377(hdrA-2)
            RCI: LRC437(hdrA-1) LRC438(hdrB-1) LRC439(hdrC-1) RCIX594(hdrC-2)
                 RCIX595(hdrB-2) RCIX596(hdrA-2) RRC256(hdrC-3) RRC257(hdrB-3)
                 RRC258(hdrA-3)
            SSO: SSO1127(hdrC-1) SSO1131(hdrA) SSO1134(hdrC-2) SSO1135(hdrB-2)
            STO: ST1870 ST1871 ST1873 ST1874 ST1875
            SAI: Saci_0325(hdrB) Saci_0326 Saci_0328(hdrA) Saci_0329
                 Saci_0334(hdrC)
            MSE: Msed_0675 Msed_1542
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.98.1
            ExPASy - ENZYME nomenclature database: 1.8.98.1
            ExplorEnz - The Enzyme Database: 1.8.98.1
            ERGO genome analysis and discovery system: 1.8.98.1
            BRENDA, the Enzyme Database: 1.8.98.1
///
ENTRY       EC 1.8.98.2                 Enzyme
NAME        sulfiredoxin;
            Srx1;
            sulphiredoxin;
            peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With other, known, acceptors
SYSNAME     peroxiredoxin-(S-hydroxy-S-oxocysteine):thiol oxidoreductase
            [ATP-hydrolysing; peroxiredoxin-(S-hydroxycysteine)-forming]
REACTION    peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH =
            peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
SUBSTRATE   peroxiredoxin-(S-hydroxy-S-oxocysteine);
            ATP [CPD:C00002];
            RSH [CPD:C01336]
PRODUCT     peroxiredoxin-(S-hydroxycysteine);
            ADP [CPD:C00008];
            phosphate [CPD:C00009];
            R-S-S-R [CPD:C15496]
COMMENT     In the course of the reaction of EC 1.11.1.15, peroxiredoxin, its
            cysteine residue is alternately oxidized to the sulfenic acid,
            S-hydroxycysteine, and reduced back to cysteine. Occasionally the
            S-hydroxycysteine residue is further oxidized to the sulfinic acid
            S-hydroxy-S-oxocysteine, thereby inactivating the enzyme. The
            reductase provides a mechanism for regenerating the active form of
            peroxiredoxin, i.e. the peroxiredoxin-(S-hydroxycysteine) form.
            Apparently the reductase first catalyses the phosphorylation of the
            -S(O)-OH group by ATP to give -S(O)-O-P, which is attached to the
            peroxiredoxin by a cysteine residue, forming an -S(O)-S- link
            between the two enzymes. Attack by a thiol splits this bond, leaving
            the peroxiredoxin as the sulfenic acid and the reductase as the
            thiol.
REFERENCE   1  [PMID:14586471]
  AUTHORS   Biteau B, Labarre J, Toledano MB.
  TITLE     ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae
            sulphiredoxin.
  JOURNAL   Nature. 425 (2003) 980-4.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:15448164]
  AUTHORS   Chang TS, Jeong W, Woo HA, Lee SM, Park S, Rhee SG.
  TITLE     Characterization of mammalian sulfiredoxin and its reactivation of
            hyperoxidized peroxiredoxin through reduction of cysteine sulfinic
            acid in the active site to cysteine.
  JOURNAL   J. Biol. Chem. 279 (2004) 50994-1001.
  ORGANISM  human [GN:hsa], rat [GN:rno], mouse [GN:mmu]
REFERENCE   3  [PMID:15590625]
  AUTHORS   Woo HA, Jeong W, Chang TS, Park KJ, Park SJ, Yang JS, Rhee SG.
  TITLE     Reduction of cysteine sulfinic acid by sulfiredoxin is specific to
            2-cys peroxiredoxins.
  JOURNAL   J. Biol. Chem. 280 (2005) 3125-8.
  ORGANISM  human [GN:hsa], rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.98.2
            ExPASy - ENZYME nomenclature database: 1.8.98.2
            ExplorEnz - The Enzyme Database: 1.8.98.2
            ERGO genome analysis and discovery system: 1.8.98.2
            BRENDA, the Enzyme Database: 1.8.98.2
///
ENTRY       EC 1.8.99.1                 Enzyme
NAME        sulfite reductase;
            assimilatory sulfite reductase;
            assimilatory-type sulfite reductase;
            hydrogen-sulfide:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With other acceptors
SYSNAME     hydrogen-sulfide:acceptor oxidoreductase
REACTION    hydrogen sulfide + acceptor + 3 H2O = sulfite + reduced acceptor
            [RN:R00861]
ALL_REAC    R00861;
            (other) R03597
SUBSTRATE   hydrogen sulfide [CPD:C00283];
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
PRODUCT     sulfite [CPD:C00094];
            reduced acceptor [CPD:C00030]
COFACTOR    Iron [CPD:C00023]
COMMENT     An iron-protein. A stoichiometry of six molecules of reduced methyl
            viologen per molecule of sulfide formed was found.
REFERENCE   1  [PMID:6038492]
  AUTHORS   Asada K.
  TITLE     Purification and properties of a sulfite reductase from leaf tissue.
  JOURNAL   J. Biol. Chem. 242 (1967) 3646-54.
  ORGANISM  Escherichia coli [GN:eco], Desulfovibrio desulfuricans [GN:dde],
            Desulfovibrio gigas, Aspergillus nidulans [GN:ani], Neurospora
            crassa [GN:dncr], Salmonella typhimurium, Clostridium nigrificans,
            Allium odorum
REFERENCE   2  [PMID:5824566]
  AUTHORS   Asada K, Tamura G, Bandurski RS.
  TITLE     Methyl viologen-linked sulfite reductase from spinach leaves.
  JOURNAL   J. Biol. Chem. 244 (1969) 4904-15.
  ORGANISM  Escherichia coli [GN:eco], Aspergillus nidulans [GN:ani], Allium
            odorum, spinach
REFERENCE   3  [PMID:5589532]
  AUTHORS   Yoshimoto A, Nakamura T, Sato R.
  TITLE     Isolation from Aspergillus nidulans, of a protein catalyzing the
            reduction of sulfite by reduced viologen dyes.
  JOURNAL   J. Biochem. (Tokyo). 62 (1967) 756-66.
  ORGANISM  Aspergillus nidulans [GN:ani]
PATHWAY     PATH: map00450  Selenoamino acid metabolism
            PATH: map00920  Sulfur metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.99.1
            ExPASy - ENZYME nomenclature database: 1.8.99.1
            ExplorEnz - The Enzyme Database: 1.8.99.1
            ERGO genome analysis and discovery system: 1.8.99.1
            BRENDA, the Enzyme Database: 1.8.99.1
            CAS: 37256-51-2
///
ENTRY       EC 1.8.99.2                 Enzyme
NAME        adenylyl-sulfate reductase;
            adenosine phosphosulfate reductase;
            adenosine 5'-phosphosulfate reductase;
            APS-reductase;
            APS reductase;
            AMP, sulfite:(acceptor) oxidoreductase
            (adenosine-5'-phosphosulfate-forming)
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With other acceptors
SYSNAME     AMP,sulfite:acceptor oxidoreductase
            (adenosine-5'-phosphosulfate-forming)
REACTION    AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor
            [RN:R00860]
ALL_REAC    R00860;
            (other) R04927
SUBSTRATE   AMP [CPD:C00020];
            sulfite [CPD:C00094];
            acceptor [CPD:C00028]
PRODUCT     adenylyl sulfate [CPD:C00224];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023]
COMMENT     An iron flavoprotein (FAD). Methyl viologen can act as acceptor.
REFERENCE   1  [PMID:5421934]
  AUTHORS   Michaels GB, Davidson JT, Peck HD Jr.
  TITLE     A flavin-sulfite adduct as an intermediate in the reaction catalyzed
            by adenylyl sulfate reductase from Desulfovibrio vulgaris.
  JOURNAL   Biochem. Biophys. Res. Commun. 39 (1970) 321-8.
  ORGANISM  Desulfovibrio vulgaris
PATHWAY     PATH: map00450  Selenoamino acid metabolism
            PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K00393  adenylylsulfate reductase
            KO: K00394  adenylylsulfate reductase, subunit A
            KO: K00395  adenylylsulfate reductase, subunit B
GENES       VOK: COSY_0091(aprB) COSY_0092(aprA)
            TBD: Tbd_0872 Tbd_0873 Tbd_2282 Tbd_2283
            DVU: DVU0846(aprB) DVU0847(aprA)
            DDE: Dde_1109 Dde_1110
            DPS: DP1104(aprB) DP1105(aprA)
            SFU: Sfum_1047 Sfum_1048
            PUB: SAR11_0836(aprB) SAR11_0837(aprA)
            CAC: CAC0104
            CKL: CKL_1798(aprA)
            CHY: CHY_2690(aprB) CHY_2691
            CTE: CT0864(aspB) CT0865(apsA)
            CCH: Cag_1586
            AFU: AF1669(aprB) AF1670(aprA)
            PAI: PAE2561 PAE2562 PAE2563 PAE2564
STRUCTURES  PDB: 1JNR  1JNZ  2FJA  2FJB  2FJD  2FJE  
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.99.2
            ExPASy - ENZYME nomenclature database: 1.8.99.2
            ExplorEnz - The Enzyme Database: 1.8.99.2
            ERGO genome analysis and discovery system: 1.8.99.2
            BRENDA, the Enzyme Database: 1.8.99.2
            CAS: 9027-75-2
///
ENTRY       EC 1.8.99.3                 Enzyme
NAME        hydrogensulfite reductase;
            bisulfite reductase;
            dissimilatory sulfite reductase;
            desulfoviridin;
            desulforubidin;
            desulfofuscidin;
            dissimilatory-type sulfite reductase;
            trithionate:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With other acceptors
SYSNAME     trithionate:acceptor oxidoreductase
REACTION    trithionate + acceptor + 2 H2O + OH- = 3 bisulfite + reduced
            acceptor [RN:R00295]
ALL_REAC    R00295
SUBSTRATE   trithionate [CPD:C01861];
            acceptor [CPD:C00028];
            H2O [CPD:C00001];
            OH- [CPD:C01328]
PRODUCT     bisulfite [CPD:C11481];
            reduced acceptor [CPD:C00030]
COFACTOR    Iron [CPD:C00023];
            Sulfur [CPD:C00087];
            Siroheme [CPD:C00748];
            Iron-sulfur [CPD:C00824]
COMMENT     Methylviologen can act as acceptor. A group of sirohemoproteins
            containing iron-sulfur centres (P-582).
REFERENCE   1  [PMID:6826522]
  AUTHORS   Hatchikian EC, Zeikus JG.
  TITLE     Characterization of a new type of dissimilatory sulfite reductase
            present in Thermodesulfobacterium commune.
  JOURNAL   J. Bacteriol. 153 (1983) 1211-20.
  ORGANISM  Thermodesulfobacterium commune
REFERENCE   2  [PMID:4717523]
  AUTHORS   Lee JP, Yi CS, LeGall J, Peck HD Jr.
  TITLE     Isolation of a new pigment, desulforubidin, from Desulfovibrio
            desulfuricans (Norway strain) and its role in sulfite reduction.
  JOURNAL   J. Bacteriol. 115 (1973) 453-5.
  ORGANISM  Desulfovibrio desulfuricans [GN:dde]
REFERENCE   3  [PMID:5473884]
  AUTHORS   Trudinger PA.
  TITLE     Carbon monoxide-reacting pigment from Desulfotomaculum nigrificans
            and its possible relevance to sulfite reduction.
  JOURNAL   J. Bacteriol. 104 (1970) 158-70.
  ORGANISM  Desulfotomaculum nigrificans
ORTHOLOGY   KO: K00396  sulfite reductase
GENES       ECO: b0969(yccK)
            ECJ: JW0952(yccK)
            ECE: Z1321(yccK)
            ECS: ECs1053
            ECC: c1107(yccK)
            ECI: UTI89_C3418(hybA)
            ECP: ECP_0975
            ECV: APECO1_74(yccK)
            STY: STY1111
            STT: t1835
            SPT: SPA1766(yccK)
            SEC: SC1036(yccK)
            STM: STM1084(yccK)
            YPE: YPO1447
            YPK: y2723
            YPM: YP_1338(dsrC)
            YPA: YPA_0739
            YPN: YPN_2532
            YPS: YPTB1465
            SFL: SF0971(yccK)
            SFX: S1037(yccK)
            SFV: SFV_0978(yccK)
            SSN: SSON_0974(yccK)
            SBO: SBO_2262(yccK)
            SDY: SDY_0944(yccK)
            ECA: ECA1762
            PLU: plu1786
            BUC: BU467(yccK)
            BAS: BUsg451(yccK)
            BAB: bbp412(yccK)
            SGL: SG1037
            BFL: Bfl418(yccK)
            BPN: BPEN_430(yccK)
            HIN: HI1371
            HIT: NTHI1790
            HDU: HD1815
            HSO: HS_0329
            PMU: PM0401
            MSU: MS0846(dsrC)
            APL: APL_0273
            VCH: VC1356
            VVU: VV1_2710
            VVY: VV1551
            VPA: VP1626
            VFI: VF1501
            PPR: PBPRA2191
            PAE: PA2608
            PAU: PA14_30370
            PPU: PP_3996
            PST: PSPTO_3341
            PSB: Psyr_3171
            PSP: PSPPH_3085
            PFL: PFL_3872
            PFO: Pfl_3578
            PEN: PSEEN2220
            PAR: Psyc_1221
            PCR: Pcryo_1171
            ACI: ACIAD1895
            SON: SO_2379
            SDN: Sden_1805
            ILO: IL0662(dsrC)
            CPS: CPS_2346(dsrC)
            PHA: PSHAa1687
            PAT: Patl_2455
            MCA: MCA1334(dsrC)
            AEH: Mlg_1653 Mlg_1654
            HHA: Hhal_1951 Hhal_1952
            HCH: HCH_02545
            AHA: AHA_2676
            RMA: Rmag_0869 Rmag_0870
            VOK: COSY_0575(yccK)
            TBD: Tbd_1309 Tbd_1369 Tbd_2480 Tbd_2484 Tbd_2485
            DVU: DVU0402(dsvA) DVU0403(dvsB) DVU0404 DVU2776(dsvC)
            DVL: Dvul_2531 Dvul_2532
            DDE: Dde_0526 Dde_0527 Dde_0528 Dde_0762
            LIP: LI0901(dsr)
            DPS: DP0797(dsrA) DP0798(dsrB) DP0799 DP0997(dsrC)
            SFU: Sfum_4041 Sfum_4042 Sfum_4043 Sfum_4045
            MAG: amb1649 amb3367 amb3368 amb3372
            MGM: Mmc1_0048 Mmc1_2156 Mmc1_2157
            ABA: Acid345_0635
            CHY: CHY_2402(dsrC) CHY_2409(dsrB) CHY_2410(dsrA)
            DSY: DSY0309(dsrA) DSY0310(dsrB) DSY0317 DSY4469
            DRM: Dred_3186 Dred_3187
            MTA: Moth_1600 Moth_1601 Moth_1629 Moth_1630 Moth_1632
            CTE: CT0851(dsrC-1) CT0852(dsrA-1) CT0853(dsrB-1) CT2249(dsrA-2)
                 CT2250(dsrC-2)
            CCH: Cag_1955 Cag_1956 Cag_1957
            CPH: Cpha266_0128 Cpha266_0129
            PVI: Cvib_0039 Cvib_0040
            PLT: Plut_0035 Plut_0036 Plut_0037
            AFU: AF0425(dsrD)
            PAI: PAE2566 PAE2596 PAE2597
            PIS: Pisl_0170 Pisl_0171
            PCL: Pcal_1445 Pcal_1446 Pcal_1456 Pcal_1457
            PAS: Pars_0907 Pars_0908 Pars_1212 Pars_1213 Pars_1224
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.99.3
            ExPASy - ENZYME nomenclature database: 1.8.99.3
            ExplorEnz - The Enzyme Database: 1.8.99.3
            ERGO genome analysis and discovery system: 1.8.99.3
            UM-BBD (Biocatalysis/Biodegradation Database): 1.8.99.3
            BRENDA, the Enzyme Database: 1.8.99.3
            CAS: 9059-42-1
///
ENTRY       EC 1.8.99.4       Obsolete  Enzyme
NAME        Transferred to 1.8.4.8
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With other acceptors
COMMENT     Transferred entry: now EC 1.8.4.8, phosphoadenylyl-sulfate reductase
            (thioredoxin) (EC 1.8.99.4 created 1999, deleted 2000)
STRUCTURES  PDB: 1SUR  
DBLINKS     IUBMB Enzyme Nomenclature: 1.8.99.4
            ExPASy - ENZYME nomenclature database: 1.8.99.4
            ExplorEnz - The Enzyme Database: 1.8.99.4
            ERGO genome analysis and discovery system: 1.8.99.4
            BRENDA, the Enzyme Database: 1.8.99.4
///
ENTRY       EC 1.8.99.-                 Enzyme
CLASS       Oxidoreductases;
            Acting on a sulfur group of donors;
            With other acceptors
REACTION    (1) Tetrachlorohydroquinone + 2 Glutathione <=>
            2,3,6-Trichlorohydroquinone + Glutathione disulfide + HCl
            [RN:R05402];
            (2) 2,3,6-Trichlorohydroquinone + 2 Glutathione <=>
            2,6-Dichlorohydroquinone + Glutathione disulfide + HCl [RN:R05403]
SUBSTRATE   Tetrachlorohydroquinone [CPD:C03434];
            Glutathione [CPD:C00051];
            2,3,6-Trichlorohydroquinone [CPD:C07099]
PRODUCT     2,3,6-Trichlorohydroquinone [CPD:C07099];
            Glutathione disulfide [CPD:C00127];
            HCl [CPD:C01327];
            2,6-Dichlorohydroquinone [CPD:C07097]
///
ENTRY       EC 1.9.3.1                  Enzyme
NAME        cytochrome-c oxidase;
            cytochrome oxidase;
            cytochrome a3;
            cytochrome aa3;
            Warburg's respiratory enzyme;
            indophenol oxidase;
            indophenolase;
            complex IV (mitochondrial electron transport);
            ferrocytochrome c oxidase;
            NADH cytochrome c oxidase
CLASS       Oxidoreductases;
            Acting on a heme group of donors;
            With oxygen as acceptor
SYSNAME     ferrocytochrome-c:oxygen oxidoreductase
REACTION    4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
            [RN:R00081]
ALL_REAC    R00081
SUBSTRATE   ferrocytochrome c [CPD:C00126];
            O2 [CPD:C00007];
            H+ [CPD:C00080]
PRODUCT     ferricytochrome c [CPD:C00125];
            H2O [CPD:C00001]
COMMENT     A cytochrome of the a type containing copper. The reduction of O2 to
            water is accompanied by the extrusion of four protons from the
            intramitochondrial compartment. Several bacteria appear to contain
            analogous oxidases.
REFERENCE   1
  AUTHORS   Keilin, D. and Hartree, E.F.
  TITLE     Cytochrome oxidase.
  JOURNAL   Proc. R. Soc. Lond. B Biol. Sci. 125 (1938) 171-186.
  ORGANISM  pig [GN:ssc]
REFERENCE   2
  AUTHORS   Keilin, D. and Hartree, E.F.
  TITLE     Cytochrome and cytochrome oxidase.
  JOURNAL   Proc. R. Soc. Lond. B Biol. Sci. 127 (1939) 167-191.
  ORGANISM  horse
REFERENCE   3
  AUTHORS   Wainio, W.W., Eichel, B. and Gould, A.
  TITLE     Ion and pH optimum for the oxidation of ferrocytochrome c by
            cytochrome c oxidase in air.
  JOURNAL   J. Biol. Chem. 235 (1960) 1521-1525.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:13787372]
  AUTHORS   YONETANI T.
  TITLE     Studies on cytochrome oxidase. II. Steady state properties.
  JOURNAL   J. Biol. Chem. 235 (1960) 3138-43.
REFERENCE   5  [PMID:13787373]
  AUTHORS   YONETANI T.
  TITLE     Studies on cytochrome oxidase. III. Improved preparation and some
            properties.
  JOURNAL   J. Biol. Chem. 236 (1961) 1680-8.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00190  Oxidative phosphorylation
ORTHOLOGY   KO: K00403  cytochrome c oxidase
            KO: K00404  cb-type cytochrome c oxidase subunit I
            KO: K00405  cb-type cytochrome c oxidase subunit II
            KO: K00406  cb-type cytochrome c oxidase subunit III
            KO: K00407  cb-type cytochrome c oxidase subunit IV
            KO: K02256  cytochrome c oxidase subunit I
            KO: K02261  cytochrome c oxidase subunit II
            KO: K02262  cytochrome c oxidase subunit III
            KO: K02263  cytochrome c oxidase subunit IV
            KO: K02264  cytochrome c oxidase subunit Va
            KO: K02265  cytochrome c oxidase subunit Vb
            KO: K02266  cytochrome c oxidase subunit VIa
            KO: K02267  cytochrome c oxidase subunit VIb
            KO: K02268  cytochrome c oxidase subunit VIc
            KO: K02269  cytochrome c oxidase subunit VII
            KO: K02270  cytochrome c oxidase subunit VIIa
            KO: K02271  cytochrome c oxidase subunit VIIb
            KO: K02272  cytochrome c oxidase subunit VIIc
            KO: K02273  cytochrome c oxidase subunit VIII
            KO: K02274  cytochrome c oxidase subunit I
            KO: K02275  cytochrome c oxidase subunit II
            KO: K02276  cytochrome c oxidase subunit III
            KO: K02277  cytochrome c oxidase subunit IV
GENES       HSA: 125965(COX6B2) 1327(COX4I1) 1329(COX5B) 1337(COX6A1)
                 1339(COX6A2) 1340(COX6B1) 1345(COX6C) 1346(COX7A1)
                 1347(COX7A2) 1349(COX7B) 1350(COX7C) 1351(COX8A)
                 170712(COX7B2) 341947(COX8C) 4512(COX1) 4513(COX2) 4514(COX3)
                 84701(COX4I2) 9377(COX5A)
            PTR: 453750(LOC453750) 454391(LOC454391) 465727(LOC465727)
                 469913(LOC469913) 807864(COX2) 807866(COX1) 807869(COX3)
            MCC: 692062(COX6B) 701661(LOC701661)
            MMU: 110323(Cox6b1) 12857(Cox4i1) 12858(Cox5a) 12859(Cox5b)
                 12861(Cox6a1) 12862(Cox6a2) 12864(Cox6c) 12865(Cox7a1)
                 12866(Cox7a2) 12867(Cox7c) 12868(Cox8a) 12869(Cox8b)
                 17708(COX1) 17709(COX2) 17710(COX3) 20463(Cox7a2l)
                 333182(Cox6b2) 66142(Cox7b) 78174(Cox7b2) 84682(Cox4i2)
            RNO: 25250(Cox8h) 25278(Cox6a2) 252934(Cox5a) 26195(COX1)
                 26198(COX2) 26204(COX3) 286962(Cox6c1) 29445(Cox4i1)
                 29507(Cox7a2) 298762(Cox7a2l_predicted) 303393(Cox7b)
                 360229(LOC360229) 54322(Cox6c) 84683(Cox4i2) 94194(Cox5b)
            CFA: 474567(LOC474567) 475739(LOC475739) 476040(LOC476040)
                 477508(LOC477508) 477724(LOC477724) 478370(LOC478370)
                 479623(LOC479623) 479780(LOC479780) 485825(LOC485825)
                 606860(LOC606860) 610768(LOC610768) 611134(LOC611134)
                 612614(LOC612614) 612644(LOC612644) 804478(COX1) 804479(COX2)
                 804480(COX3)
            BTA: 281090(COX4) 281091(COX8) 282199(COX6A1) 282200(COX6A2)
                 287012(COX5B) 327674(COX7B) 327688(COX7A2) 327718(COX7C)
                 3283879(COX1) 3283880(COX2) 3283883(COX3) 338086(COX7A1)
                 338087(COX6B) 444878(COX5A) 503554(COX6B2)
            SSC: 399685(COX7A1) 492822(Cox5b) 808503(COX1) 808504(COX2)
                 808507(COX3)
            GGA: 415826(RCJMB04_15g7) 416978(COX6A1) 420243(COX6C)
                 431629(LOC431629) 769735(LOC769735) 771947(LOC771947)
                 772260(LOC772260) 775974(LOC775974) 807635(COX2) 807637(COX3)
                 807639(COX1)
            XLA: 2642081(COX2) 2642084(COX3) 2642088(COX1) 379593(MGC68573)
                 432126(MGC82295) 443818(MGC79007) 444031(MGC82595)
                 447180(MGC85571) 447187(MGC85582) 447278(MGC86432)
            XTR: 3283494(COX1) 3283495(COX2) 3283498(COX3)
                 448681(TGas029a19.1) 496600(cox6c)
            DRE: 140539(COX1) 140540(COX2) 140541(COX3) 326975(cox4i1)
                 335751(cox7a2l) 336118(cox7c) 393478(zgc:66195)
                 393776(zgc:73355)
            SPU: 2652715(COX3) 2652718(COX1) 2652720(COX2) 579345(LOC579345)
                 580629(LOC580629) 581274(LOC581274) 584872(LOC584872)
                 585298(LOC585298) 587578(LOC587578) 591899(LOC591899)
                 752987(LOC752987) 753740(LOC753740)
            DME: COX1 COX2 COX3 Dmel_CG10396 Dmel_CG10664 Dmel_CG11015
                 Dmel_CG11043 Dmel_CG14028(cype) Dmel_CG14077
                 Dmel_CG14724(CoVa) Dmel_CG17280 Dmel_CG18193 Dmel_CG2249
                 Dmel_CG30093 Dmel_CG31644 Dmel_CG9603
            CEL: COX1 COX2 COX3 F26E4.6 F26E4.9(cco-1) F29C4.2
                 F54D8.2(tag-174) W09C5.8 Y37D8A.14(cco-2) Y71H2AM.5
            ATH: AT1G22450(COX6B) AT1G32710 AT1G80230 AT2G07695 AT3G15640
                 AT4G28060 AT4G37830 AT5G57815 ArthMp015(cox2) ArthMp065(cox3)
                 ArthMp109(cox1)
            OSA: 4325317 4330974 4333018 4334266 4336292 4340088 cox1 cox2
                 cox3
            CME: CMJ036C CML098C CMR404C
            SCE: Q0045(COX1) Q0065(AI4) Q0070(AI5_ALPHA) Q0250(COX2)
                 Q0275(COX3) YDL067C(COX9) YGL187C(COX4) YGL191W(COX13)
                 YHR051W(COX6) YIL111W(COX5B) YLR038C(COX12) YLR395C(COX8)
                 YMR256C(COX7) YNL052W(COX5A)
            AGO: AGOS_ACL110W AGOS_ADL243W AGOS_ADR240C AGOS_AER062C
                 AGOS_AER063W AGOS_AFR193W AGOS_AFR196C AGOS_AGL216W
                 AGOS_AMI001W AGOS_AMI002W AGOS_AMI003W
            KLA: KllafMp05(COX1)
            PIC: PICST_67314(COX13) PICST_71543(COX12) PICST_77110(COX5a)
                 PICST_82299(COX6) PICST_85465(COX7) PICST_88762(COX4)
            CAL: CaO19_4759(CaO19.4759) CaalfMp01(COX2) CaalfMp04(COX3a)
                 CaalfMp15(COX3b)
            CGR: CAGL0A03542g CAGL0D00748g CAGL0I04136g CAGL0J00429g
                 CAGL0L06160g CAGL0L06204g CaglfMp04(cox1) CaglfMp11(cox2)
                 CaglfMp12(cox3)
            SPO: SPAC1296.02(cox4) SPAC1B2.04 SPAC24C9.16c SPCC1259.05c
                 SPCC1442.08c SPCC1739.09c SPCC338.10c
            ANI: AN2316.2 AN4525.2 AN6255.2 AN8118.2
            AFM: AFUA_2G13010 AFUA_3G14440 AFUA_5G02750 AFUA_5G10560
            AOR: AO090010000481 AO090026000651
            ANG: An14g04170(cox5)
            CNE: CNB03500 CNC04090 CNC05480 CNF01340 CNG02210 CNK03240
                 CNL04890 CNN01330
            UMA: UM01147.1 UM02643.1 UM04802.1 UM05465.1 cox1 cox2 cox3
            DDI: DDBDRAFT_0186146 DidioMp04(cox3) DidioMp06(cox1)
            PFA: PF14_0288 PFI1365w PFI1375w
            TAN: TA02790 TA12915 TA20025 q2ca38.01(Tap370b08.q2ca38.01)
                 q2ca38.02c(Tap370b08.q2ca38.02c)
            TPV: TP01_0093 TP01_0588 TP01_0683 TP02_0045
            TET: TepyoMp34(cox2) TepyoMp39(cox1)
            TBR: Tb10.100.0160
            YPP: YPDSF_2800
            ENT: Ent638_0898
            SPE: Spro_1089
            XCC: XCC3829(cox3) XCC3832(ctaD) XCC3833(ctaC)
            XCB: XC_3901 XC_3904 XC_3905
            XCV: XCV4002 XCV4005(ctaD) XCV4006(ctaC)
            XAC: XAC3884(cox3) XAC3887(ctaD) XAC3888(ctaC)
            XOO: XOO4137(cox3) XOO4140(ctaD) XOO4141(ctaC)
            XOM: XOO_3916(XOO3916) XOO_3919(XOO3919) XOO_3920(XOO3920)
            VCH: VC1439(ccoP) VC1440(ccoQ) VC1441(ccoO) VC1442(ccoN)
            VCO: VC0395_A1051(ccoQ) VC0395_A1052(ccoO) VC0395_A1053(ccoN)
            VVU: VV1_2617 VV1_2618 VV1_2619 VV1_2620 VV2_0565 VV2_0567
                 VV2_0568
            VVY: VV1671 VV1672 VV1673 VV1674(ccoP) VVA1113 VVA1115 VVA1116
            VPA: VP1541(ccoP) VP1542(ccoQ) VP1543(ccoO) VP1544(ccoN) VPA0536
                 VPA0537 VPA0539
            VFI: VF1299 VF1300 VF1301 VF1302
            PPR: PBPRA0167 PBPRA0168 PBPRA0170 PBPRA1831(ccoN) PBPRA1832
                 PBPRA1833(ccoQ) PBPRA1834(ccoP) PBPRB0386 PBPRB0387 PBPRB0388
                 PBPRB0389
            PAE: PA0105(coxB) PA0106(coxA) PA0108(coIII) PA1552 PA1553 PA1554
                 PA1555 PA1556 PA1557 PA1856 PA4133
            PAU: PA14_01290(coxB) PA14_01300(coxA) PA14_01320(coIII)
                 PA14_10500(ccoN) PA14_40510(ccoN-2) PA14_44340(ccoN)
                 PA14_44350(fixO) PA14_44360(fixP) PA14_44370(ccoN)
                 PA14_44380(ccoO) PA14_44390 PA14_44400(ccoP)
            PAP: PSPA7_0181(ctaD) PSPA7_0958(ccoN4) PSPA7_3436(ccoN3)
                 PSPA7_3773(ccoN2) PSPA7_3774(ccoO2) PSPA7_3775(ccoQ2)
                 PSPA7_3776(ccoP2) PSPA7_3777(ccoN1) PSPA7_3778(ccoO1)
                 PSPA7_3779(ccoQ1) PSPA7_3780(ccoP1)
            PPU: PP_0103 PP_0104 PP_0106 PP_4250(ccoN-1) PP_4251(ccoO-1)
                 PP_4252(ccoQ-1) PP_4253(ccoP-1) PP_4255(ccoN-2)
                 PP_4256(ccoO-2) PP_4257(ccoQ-2) PP_4258(ccoP-2)
            PPF: Pput_0120 Pput_0836 Pput_1613 Pput_1618
            PST: PSPTO_2001(ccoP) PSPTO_2002(ccoQ) PSPTO_2003(ccoO)
                 PSPTO_2004(ccoN)
            PSB: Psyr_3413 Psyr_3414 Psyr_3415 Psyr_3416
            PSP: PSPPH_3337(ccoN) PSPPH_3338(ccoO) PSPPH_3339(ccoQ)
                 PSPPH_3340(ccoP)
            PFL: PFL_0061 PFL_0062 PFL_0064 PFL_1918(ccoP) PFL_1919(ccoQ)
                 PFL_1920(ccoO) PFL_1921(ccoN) PFL_1922(ccoP) PFL_1923(ccoQ)
                 PFL_1924(ccoO) PFL_1925(ccoN) PFL_2834(ccoN)
            PFO: Pfl_0076 Pfl_0078 Pfl_0079 Pfl_1820 Pfl_1821 Pfl_1822
                 Pfl_1823 Pfl_1824 Pfl_1825 Pfl_1826 Pfl_1827 Pfl_2512 Pfl_4647
            PEN: PSEEN0056(coxB) PSEEN0057(coxA) PSEEN0059 PSEEN1799(ccoP-2)
                 PSEEN1800(ccoQ-2) PSEEN1801(ccoO-2) PSEEN1802(ccoN-2)
                 PSEEN1804(ccoP-1) PSEEN1805(ccoQ-1) PSEEN1806(ccoO-1)
                 PSEEN1807(ccoN-1)
            PMY: Pmen_0143 Pmen_2266 Pmen_2267 Pmen_2599 Pmen_2604
            PAR: Psyc_0775 Psyc_0776 Psyc_0777 Psyc_0778
            PCR: Pcryo_0781 Pcryo_0782 Pcryo_0783 Pcryo_0784
            PRW: PsycPRwf_1744
            SON: SO_2361(ccoP) SO_2362(ccoQ) SO_2363(ccoO) SO_2364(ccoN)
                 SO_4606 SO_4607 SO_4609
            SDN: Sden_1848 Sden_1849 Sden_1850 Sden_1851 Sden_3517 Sden_3518
                 Sden_3520
            SFR: Sfri_0255 Sfri_0257 Sfri_0258 Sfri_2010 Sfri_2011 Sfri_2012
                 Sfri_2013
            SAZ: Sama_3483 Sama_3484
            SBL: Sbal_0153 Sbal_0154
            SBM: Shew185_2170 Shew185_4180 Shew185_4219
            SLO: Shew_0124 Shew_0125 Shew_0367
            SPC: Sputcn32_3783 Sputcn32_3859
            SSE: Ssed_0197 Ssed_0198
            SPL: Spea_3999 Spea_4000
            SHE: Shewmr4_2006 Shewmr4_2007 Shewmr4_2008 Shewmr4_2009
                 Shewmr4_3791 Shewmr4_3792 Shewmr4_3794 Shewmr4_3824
            SHM: Shewmr7_1966 Shewmr7_1967 Shewmr7_1968 Shewmr7_1969
                 Shewmr7_3864 Shewmr7_3865 Shewmr7_3867 Shewmr7_3915
            SHN: Shewana3_2107 Shewana3_2108 Shewana3_2109 Shewana3_2110
                 Shewana3_3991 Shewana3_3992 Shewana3_3994 Shewana3_4032
            SHW: Sputw3181_0094 Sputw3181_0132 Sputw3181_0133
            ILO: IL0257(cyoC) IL0259(cyoB) IL0260(cyoA) IL1297(ccoN)
                 IL1298(ccoO) IL1299(ccoQ) IL1300(ccoP)
            CPS: CPS_0233 CPS_0235 CPS_0236 CPS_1992(ccoP) CPS_1993(ccoQ)
                 CPS_1994(ccoO) CPS_1995(ccoN)
            PHA: PSHAa1842 PSHAa1843 PSHAa1844 PSHAa1845(ccoP) PSHAa2869
                 PSHAa2871(ctaD) PSHAa2872
            PAT: Patl_2070 Patl_2071 Patl_2072 Patl_2073 Patl_4243 Patl_4245
                 Patl_4246
            SDE: Sde_0036 Sde_0037 Sde_0039 Sde_2419 Sde_2421 Sde_2422
            PIN: Ping_2716(cyoB) Ping_2717
            MAQ: Maqu_0062 Maqu_0063
            LPN: lpg2894 lpg2896 lpg2897
            LPF: lpl2808(coxC) lpl2810(coxA) lpl2811(coxB)
            LPP: lpp2959(coxC) lpp2961(coxA) lpp2962(coxB)
            MCA: MCA0879 MCA0880 MCA0883 MCA2396 MCA2397
            TCX: Tcr_1963 Tcr_1964 Tcr_1965
            NOC: Noc_1244 Noc_1245 Noc_1246 Noc_1766 Noc_1767 Noc_2970
                 Noc_2971 Noc_3044 Noc_3046 Noc_3047
            AEH: Mlg_0293 Mlg_0294 Mlg_0296 Mlg_1879 Mlg_1880 Mlg_1881
                 Mlg_1882
            HCH: HCH_00047(coxB) HCH_00048(coxA) HCH_00049(coxC)
                 HCH_02273(ccoP) HCH_02274(ccoQ) HCH_02275(ccoO)
                 HCH_02276(ccoN)
            ABO: ABO_1348 ABO_1349(ccoQ) ABO_1350(ccoO-1) ABO_1351(ccoN-1)
                 ABO_1897(coxC) ABO_1899(coxA) ABO_1900(coxB)
            MMW: Mmwyl1_0090
            AHA: AHA_2295(ccoN) AHA_2296(ccoO) AHA_2297(ccoQ) AHA_2298(ccoP)
            RMA: Rmag_0034 Rmag_0035
            VOK: COSY_0034(coxB) COSY_0035(coxA) COSY_0037(coxC)
                 COSY_0040(ccoN) COSY_0041(ccoO) COSY_0042(ccoQ)
                 COSY_0043(ccoP)
            NME: NMB1723 NMB1724 NMB1725
            NMA: NMA1977 NMA1978 NMA1979 NMA1980
            NMC: NMC1645
            NGO: NGO1371(ccoP) NGO1372 NGO1373(ccoO) NGO1374(ccoN)
            CVI: CV_0599(coxB) CV_0600(coxA) CV_0603(coxC) CV_1171 CV_1172
                 CV_1173 CV_1174 CV_4386(cyc)
            RSO: RS02212(RSp1653) RS02325(RSp0993) RSc0362(coxB) RSc0363(coxA)
                 RSc0367(coxC) RSc1276(RS02814) RSc1277(RS02815)
                 RSc1279(RS02792) RSp1564(coxM) RSp1565(coxN) RSp1566(coxO)
                 RSp1567(coxP)
            REU: Reut_A0314 Reut_A0315 Reut_A0318 Reut_A0983 Reut_A2038
                 Reut_A2039 Reut_A2040 Reut_A2041 Reut_B3632 Reut_B3633
                 Reut_B3634 Reut_B3635 Reut_B4253 Reut_B4435 Reut_B4436
                 Reut_B4437 Reut_B4578 Reut_B4891
            REH: H16_A0342(ctaC) H16_A0343(ctaD) H16_A0347(ctaE)
                 H16_A2316(ccoP) H16_A2317(ccoQ) H16_A2318(ccoO)
                 H16_A2319(ccoN) H16_B2060(coxO) H16_B2061(coxN)
                 H16_B2062(coxM)
            RME: Rmet_0261 Rmet_0262 Rmet_0265 Rmet_0599 Rmet_0949 Rmet_2041
                 Rmet_2042 Rmet_2043 Rmet_2044 Rmet_3955 Rmet_3956 Rmet_3957
                 Rmet_3958 Rmet_4322 Rmet_4323
            BMA: BMA1408 BMA3193(coxC) BMA3196(coxA) BMA3197(coxB)
            BMV: BMASAVP1_A0165(coxC) BMASAVP1_A0169(coxA)
                 BMASAVP1_A0170(coxB)
            BML: BMA10299_A1422(coxB) BMA10299_A1423(coxA)
                 BMA10299_A1427(coxC)
            BMN: BMA10247_2849(coxB) BMA10247_2850(coxA) BMA10247_2854(coxC)
            BXE: Bxe_A2183 Bxe_A2184 Bxe_A2185 Bxe_A4077 Bxe_A4078 Bxe_A4167
                 Bxe_A4170 Bxe_A4171 Bxe_C0079 Bxe_C0080 Bxe_C0081 Bxe_C0167
                 Bxe_C0168
            BVI: Bcep1808_1972 Bcep1808_2822 Bcep1808_2946
            BUR: Bcep18194_A5375 Bcep18194_A5376 Bcep18194_A6172
                 Bcep18194_A6175 Bcep18194_A6176 Bcep18194_B1402
                 Bcep18194_B1403 Bcep18194_C7359 Bcep18194_C7360
                 Bcep18194_C7361 Bcep18194_C7362
            BCN: Bcen_1292 Bcen_1293 Bcen_2228 Bcen_2232 Bcen_2233 Bcen_6007
            BCH: Bcen2424_2070 Bcen2424_2842 Bcen2424_2846 Bcen2424_2847
                 Bcen2424_6538 Bcen2424_6539
            BAM: Bamb_2106 Bamb_2898 Bamb_2901 Bamb_2902 Bamb_6210
            BPS: BPSL0453 BPSL0454(ctaD) BPSL0458 BPSL0722 BPSL0723 BPSL1259
                 BPSL1260 BPSL1454 BPSS0086
            BPM: BURPS1710b_0672(coxB) BURPS1710b_0673(ctaD) BURPS1710b_0677
                 BURPS1710b_0944 BURPS1710b_0945 BURPS1710b_1491(cbaB)
                 BURPS1710b_1492 BURPS1710b_2422(soxH) BURPS1710b_A1593(ctaD)
            BPL: BURPS1106A_0507 BURPS1106A_0508 BURPS1106A_0512
                 BURPS1106A_0783 BURPS1106A_1358 BURPS1106A_1359
                 BURPS1106A_A0112(ctaD) BURPS1106A_A0911
            BPD: BURPS668_0489 BURPS668_0490 BURPS668_0494 BURPS668_0770
                 BURPS668_0771 BURPS668_1352 BURPS668_1353 BURPS668_A0137(ctaD)
                 BURPS668_A0998
            BTE: BTH_I0426 BTH_I0427 BTH_I0430 BTH_I2874 BTH_I2875 BTH_II1618
                 BTH_II1619
            PNU: Pnuc_1939
            BPE: BP2169 BP2170 BP2171 BP2172 BP3740(coIII) BP3743(ctaD) BP3744
            BPA: BPP1779 BPP1780 BPP1780A BPP1781 BPP4204(ctaD) BPP4239(coIII)
                 BPP4242(ctaD) BPP4243
            BBR: BB3326 BB3327 BB3328 BB3329 BB4674(ctaD) BB4827(coIII)
                 BB4830(ctaD) BB4831
            RFR: Rfer_1680 Rfer_1681 Rfer_1684 Rfer_1930 Rfer_1931 Rfer_1932
                 Rfer_1933 Rfer_4126 Rfer_4127
            POL: Bpro_0726 Bpro_0727 Bpro_0728 Bpro_0729 Bpro_1245 Bpro_1246
                 Bpro_1249 Bpro_1266 Bpro_1267 Bpro_4302 Bpro_4303 Bpro_4304
                 Bpro_4305
            PNA: Pnap_0878 Pnap_0879
            AAV: Aave_2222 Aave_3557 Aave_3906 Aave_3907
            AJS: Ajs_2776 Ajs_3536 Ajs_3537
            VEI: Veis_1380 Veis_1381
            MPT: Mpe_A2475 Mpe_A2477 Mpe_A2478 Mpe_A3177 Mpe_A3180 Mpe_A3181
            HAR: HEAR1115 HEAR1116 HEAR1641 HEAR1643 HEAR1644 HEAR2701(cyoB)
                 HEAR2702(cyoA) HEAR2915(coxC) HEAR2918(coxA) HEAR2919(coxB)
            MMS: mma_1631(ccoN) mma_1632(ccoO) mma_1634(ccoP) mma_3149(coxC)
                 mma_3151(coxA)
            NEU: NE0683(coxA2) NE0684(coxB) NE0925 NE1013(coxC) NE1016(coxA)
                 NE1017(coxB)
            NET: Neut_1582 Neut_1583 Neut_1874 Neut_1875 Neut_2392 Neut_2394
                 Neut_2395
            NMU: Nmul_A0183 Nmul_A0184 Nmul_A0187 Nmul_A0458 Nmul_A0459
                 Nmul_A0460 Nmul_A1775 Nmul_A1776 Nmul_A1777 Nmul_A2666
                 Nmul_A2667
            EBA: ebA156(coxA) ebA158(coxB) ebA2880(ccoN) ebA2882(ccoO)
                 ebA3665(coxB2) ebA3666(coxA2) ebA4227(coxB) ebA4228(coxA)
                 ebA4231(coxC) ebA4542(coxC) ebA4544(coxA) ebA4547(coxB)
                 ebA5131(ccoN) ebA5132(ccoO) ebA5134(ccoP) ebA6329(norE)
                 ebC11(ccoQ)
            AZO: azo1341(ccoN) azo3299(coxC) azo3304(coxB)
            DAR: Daro_0713 Daro_0714 Daro_0715 Daro_0716 Daro_1065(norE)
                 Daro_1467 Daro_1470 Daro_1471
            TBD: Tbd_0325 Tbd_0326 Tbd_0330 Tbd_0338 Tbd_0339 Tbd_0341
                 Tbd_0640 Tbd_0641(ccoQ) Tbd_0642 Tbd_0643 Tbd_1970(norE)
            MFA: Mfla_0629 Mfla_0630 Mfla_0632 Mfla_1433 Mfla_1434 Mfla_1448
                 Mfla_1449
            HPY: HP0144(fixN) HP0145(fixO) HP0146(ccoQ) HP0147(fixP)
            HPJ: jhp0132(fixN) jhp0133(fixO) jhp0134(fixQ) jhp0135(fixP)
            HPA: HPAG1_0142 HPAG1_0143 HPAG1_0144 HPAG1_0145
            HHE: HH1256(fixN) HH1257(fixO) HH1258(fixQ) HH1259(fixP)
            HAC: Hac_0325(fixN) Hac_0326(fixO) Hac_0327(fixQ) Hac_0328(fixP)
            WSU: WS0178(fixN) WS0179(ccoO) WS0180 WS0181(ccoP)
            TDN: Tmden_0081 Tmden_0082 Tmden_0084 Tmden_0103 Tmden_0104
            CJE: Cj1487c(ccoP) Cj1488c(ccoQ) Cj1489c(ccoO) Cj1490c(ccoN)
            CJR: CJE1660(ccoP) CJE1661(ccoQ) CJE1662(ccoO) CJE1663(ccoN)
            CJJ: CJJ81176_1479(ccoP) CJJ81176_1480(ccoQ) CJJ81176_1481(ccoO)
                 CJJ81176_1482(ccoN)
            CJU: C8J_1392(ccoP) C8J_1393(ccoQ) C8J_1394(ccoO) C8J_1395(ccoN)
            CJD: JJD26997_1833(ccoP) JJD26997_1834(ccoQ) JJD26997_1835(ccoO)
                 JJD26997_1836(ccoN)
            CFF: CFF8240_0378(ccoN) CFF8240_0379(ccoO) CFF8240_0380
                 CFF8240_0381(ccoP)
            CCV: CCV52592_0902(ccoN) CCV52592_0903(ccoO) CCV52592_0904
                 CCV52592_0905(ccoP)
            CHA: CHAB381_1397 CHAB381_1398(ccoO) CHAB381_1399(ccoN)
            CCO: CCC13826_0725 CCC13826_0726(ccoP)
            ABU: Abu_2078(ccoP) Abu_2079(ccoQ) Abu_2080(ccoO) Abu_2081(ccoN)
            NIS: NIS_1615(ccoP) NIS_1616(ccoQ) NIS_1617(ccoO) NIS_1618(ccoN)
            SUN: SUN_0178 SUN_0179 SUN_0180 SUN_0181
            GSU: GSU0219 GSU0220 GSU0221 GSU0222
            GME: Gmet_0249 Gmet_0250 Gmet_0251 Gmet_0252
            GUR: Gura_0408
            PCA: Pcar_2526 Pcar_2527 Pcar_2528 Pcar_2529
            DVU: DVU1812 DVU1813 DVU1814 DVU1815
            DVL: Dvul_1345
            DDE: Dde_1823 Dde_1824 Dde_1825 Dde_1826
            BBA: Bd0286(ctaC) Bd0287(ctaD) Bd0288(ctaE) Bd2611(fixN)
                 Bd2613(fixP)
            ADE: Adeh_0803 Adeh_0804 Adeh_0805 Adeh_1171 Adeh_1172 Adeh_2273
                 Adeh_2274
            AFW: Anae109_0849 Anae109_2861
            MXA: MXAN_3867(coxC) MXAN_3868(ctaD) MXAN_3869(coxB)
                 MXAN_5539(ccoP) MXAN_5541(ccoNO) MXAN_6086(coxB)
                 MXAN_6087(ctaD) MXAN_6088(coxC)
            RPR: RP191(coxC) RP405(coxA) RP406(coxB)
            RCO: RC0240(coxC) RC0553(coxA) RC0555(coxB)
            RFE: RF_0627(coxA) RF_0629(coxB) RF_1076(coxC)
            RBE: RBE_0889(coxB) RBE_0891(coxA) RBE_1104(coxC)
            RCM: A1E_00865
            OTS: OTBS_0283(coxB) OTBS_1495(coxC) OTBS_1800(coxA)
            WOL: WD0141(coxC) WD0300(coxB) WD0301(coxA)
            WBM: Wbm0307 Wbm0308 Wbm0698
            AMA: AM1007(coxB) AM1008(coxA) AM1300(coxC)
            APH: APH_0019 APH_1084 APH_1085(ctaD)
            ERU: Erum0170(coxC) Erum7730(coxB) Erum7740(coxA)
            ERW: ERWE_CDS_00040(coxC) ERWE_CDS_08170(ctaC)
                 ERWE_CDS_08180(ctaD)
            ERG: ERGA_CDS_00040(coxC) ERGA_CDS_08070(ctaC)
                 ERGA_CDS_08080(ctaD)
            ECN: Ecaj_0009 Ecaj_0809 Ecaj_0810
            ECH: ECH_0029 ECH_1002 ECH_1003(ctaD)
            NSE: NSE_0621 NSE_0622(ctaD) NSE_0676
            PUB: SAR11_0130(coxC) SAR11_0133(ctaB) SAR11_0134(cox1)
                 SAR11_0135(coxB)
            MLO: mll6628 mll6629 mll6630 mll9630 mll9631 mlr1039 mlr1041
                 mlr1042 mlr1043 mlr6411 mlr6412 mlr6414 mlr7490 mlr7491
                 mlr7496 msl6627(fixQ) msr6413
            MES: Meso_0741 Meso_0742 Meso_0746 Meso_2250 Meso_2251 Meso_2252
                 Meso_2253 Meso_2474 Meso_2475 Meso_2476 Meso_2477 Meso_2791
                 Meso_2792
            PLA: Plav_0564 Plav_0669 Plav_0670 Plav_1532
            SME: SMa0612(fixN3) SMa0615(fixO3) SMa0616(fixQ3) SMa0617(fixP3)
                 SMa0765(fixN2) SMa0766(fixO2) SMa0767(fixQ2) SMa0769(fixP2)
                 SMa1213(fixP1) SMa1214(fixQ1) SMa1216(fixO1) SMa1220(fixN1)
                 SMb21368 SMb21370 SMc00009(ctaC) SMc00010(ctaD) SMc00013(ctaE)
                 SMc01982(coxM) SMc01983(coxN) SMc01984(coxO) SMc01985(coxP)
            SMD: Smed_0518 Smed_0519 Smed_2426 Smed_4371 Smed_4762 Smed_5926
                 Smed_5935 Smed_6268
            ATU: Atu0767(coxB) Atu0768(coxA) Atu0771(coxC) Atu1534(fixP)
                 Atu1535(fixQ) Atu1536(fixO) Atu1537(fixN)
            ATC: AGR_C_1397 AGR_C_1399 AGR_C_1407 AGR_C_2829 AGR_C_2832
                 AGR_C_2835
            RET: RHE_CH00952(ctaC) RHE_CH00953(ctaD) RHE_CH00956(ctaE)
                 RHE_CH00982 RHE_CH00983 RHE_CH02614(coxP) RHE_CH02615(coxO)
                 RHE_CH02616(coxN) RHE_CH02617(coxM) RHE_PB00064 RHE_PB00065
                 RHE_PF00504(fixPf) RHE_PF00506(fixOf) RHE_PF00507(fixNf)
            RLE: RL0533A(fixQ) RL0534(fixP) RL0535(fixO) RL0536(fixN)
                 RL1021(coxB) RL1022(coxA) RL1026(ctaE) RL1160 RL3042(ctaE2)
                 RL3043(ctaE1) RL3044(ctaD) RL3045(ctaC) pRL100205(fixN)
                 pRL100206(fixO) pRL100206A(fixQ) pRL100207(fixP)
                 pRL90016(fixP) pRL90017(fixO) pRL90018(fixN)
            BME: BMEI1462 BMEI1465 BMEI1466 BMEI1564 BMEI1565 BMEI1566
                 BMEII0322
            BMF: BAB1_0389 BAB1_0390(ccoQ) BAB1_0391(ccoO) BAB1_0392(ccoN)
                 BAB1_0492 BAB1_0493(coxA) BAB1_0497(coxC)
            BMS: BR0360(ccoP) BR0361(ccoQ) BR0362(ccoO) BR0363(ccoN)
                 BR0467(coxB) BR0468(coxA) BR0472(coxC)
            BMB: BruAb1_0386(ccoP) BruAb1_0387(ccoQ) BruAb1_0388(ccoO)
                 BruAb1_0389(ccoN) BruAb1_0489(coxB) BruAb1_0490(coxA)
                 BruAb1_0494(coxC)
            BOV: BOV_0376(ccoP) BOV_0377(ccoQ) BOV_0378(ccoO) BOV_0379(ccoN)
                 BOV_0474(ctaD)
            OAN: Oant_0049 Oant_0469 Oant_0581 Oant_0582
            BJA: bll3782(coxP) bll3783(coxO) bll3784(coxN) bll3785(coxM)
                 bll4480 bll4481 blr1170(coxB) blr1171(coxA) blr1175(coxC)
                 blr2763(fixN) blr2764(fixO) blr2766(fixP) bsr2765(fixQ)
            BRA: BRADO2259 BRADO2260 BRADO6702(coxC) BRADO6706(coxA)
                 BRADO6707(coxB)
            BBT: BBta_0828(coxB) BBta_0829(coxA) BBta_0833(coxC)
            RPA: RPA0016(ccoP) RPA0017(ccoQ) RPA0018(ccoO) RPA0019(ccoN)
                 RPA0831(coxB) RPA0832(coxA) RPA0836(coxC)
            RPB: RPB_0014 RPB_0015 RPB_0016 RPB_0017 RPB_0155 RPB_0156
                 RPB_4583 RPB_4587 RPB_4588
            RPC: RPC_0012 RPC_0013 RPC_0014 RPC_0015 RPC_3849 RPC_3850
                 RPC_4787 RPC_4788 RPC_4792
            RPD: RPD_0730 RPD_0731 RPD_0732 RPD_0733 RPD_0814 RPD_0815
                 RPD_0819
            RPE: RPE_0015 RPE_0016 RPE_0017 RPE_0018 RPE_3865 RPE_3866
                 RPE_4751 RPE_4752 RPE_4756
            NWI: Nwi_0223 Nwi_0224 Nwi_0228 Nwi_0761 Nwi_0762 Nwi_0766
                 Nwi_0770 Nwi_2313 Nwi_2314
            NHA: Nham_0255 Nham_0256 Nham_0260 Nham_2711 Nham_2712 Nham_3462
                 Nham_3463 Nham_3643 Nham_4178 Nham_4179 Nham_4180
            XAU: Xaut_0459 Xaut_4647 Xaut_4648
            CCR: CC_1401 CC_1402 CC_1403 CC_1404 CC_3402 CC_3406 CC_3407
            SIL: SPO1383(ctaD) SPO3073(ctaE) SPO3076(ctaC) SPO3523(ccoP-1)
                 SPO3524(ccoQ-1) SPO3525(ccoO-1) SPO3526(ccoN-1) SPOA0184
                 SPOA0185 SPOA0187(ccoP-2) SPOA0188(ccoQ-2) SPOA0189(ccoO-2)
                 SPOA0190(ccoN-2)
            SIT: TM1040_2291 TM1040_2332 TM1040_2336 TM1040_2542 TM1040_2543
                 TM1040_2544 TM1040_2545
            RSP: RSP_0117 RSP_0118 RSP_0693(ccoP) RSP_0694(ccoQ)
                 RSP_0695(ccoO) RSP_0696(ccoN) RSP_1826(coxII) RSP_1829(coxIII)
                 RSP_1877(coxI)
            RSH: Rsph17029_0474 Rsph17029_0527 Rsph17029_1753 Rsph17029_3824
            RSQ: Rsph17025_0534 Rsph17025_0614 Rsph17025_0664 Rsph17025_1704
                 Rsph17025_3668
            JAN: Jann_1250 Jann_3151 Jann_3155 Jann_3854 Jann_3855 Jann_3856
                 Jann_3857
            RDE: RD1_1270(ccoN) RD1_1271(ccoO) RD1_1272(ccoQ) RD1_1273(ccoP)
                 RD1_1967(ctaD) RD1_2135(ctaC) RD1_2138(ctaG) RD1_2139(ctaE)
                 RD1_3687
            PDE: Pden_1938 Pden_3028 Pden_4321 Pden_5107
            MMR: Mmar10_1149 Mmar10_1150 Mmar10_1152 Mmar10_2229 Mmar10_2233
                 Mmar10_2234
            HNE: HNE_1038(coxB) HNE_1039 HNE_1043 HNE_1229(ccoP)
                 HNE_1230(ccoQ) HNE_1231(ccoO) HNE_1232(ccoN)
            NAR: Saro_0913 Saro_0914 Saro_0918 Saro_2575 Saro_2577 Saro_2578
            SAL: Sala_1401 Sala_1404 Sala_1405 Sala_1673 Sala_1674 Sala_1675
                 Sala_1676
            SWI: Swit_1801 Swit_3875 Swit_3876
            ELI: ELI_02725 ELI_02730 ELI_02750
            GBE: GbCGDNIH1_2250 GbCGDNIH1_2258 GbCGDNIH1_2259
            ACR: Acry_1095 Acry_2166
            RRU: Rru_A3330 Rru_A3331 Rru_A3332
            MAG: amb2167 amb2169 amb2170 amb2221 amb2222 amb4363 amb4365
            MGM: Mmc1_2353 Mmc1_2354 Mmc1_2355
            ABA: Acid345_0437 Acid345_0438 Acid345_0439 Acid345_0440
                 Acid345_0884 Acid345_2994 Acid345_2995 Acid345_2996
            SUS: Acid_0498 Acid_5590 Acid_6908 Acid_7581
            BSU: BG10215(ctaC) BG10216(ctaD) BG10217(ctaE) BG10218(ctaF)
            BHA: BH0739 BH0740 BH2612(ctaF) BH2613(ctaE) BH2614(ctaD)
                 BH2615(ctaC)
            BAN: BA4151(ctaF) BA4152(ctaE) BA4153(ctaD) BA4154(ctaC)
            BAR: GBAA4151(ctaF) GBAA4152(ctaE) GBAA4153(ctaD) GBAA4154(ctaC)
            BAA: BA_4619 BA_4620 BA_4622 BA_4623
            BAT: BAS3853 BAS3854 BAS3855 BAS3856
            BCE: BC3941 BC3942 BC3943 BC3944
            BCA: BCE_3988(ctaF) BCE_3989(ctaE) BCE_3990(ctaD) BCE_3991(ctaC)
            BCZ: BCZK0611(qoxD) BCZK0612(qoxC) BCZK0613(qoxB) BCZK3701(ctaF)
                 BCZK3702(ctaE) BCZK3703(ctaD) BCZK3704(ctaC) BCZK3706(ctaA)
            BCY: Bcer98_0590 Bcer98_2645 Bcer98_2646
            BTK: BT9727_0610(qoxD) BT9727_0611(qoxC) BT9727_0612(qoxB)
                 BT9727_0613(qoxA) BT9727_3684(ctaF) BT9727_3685(ctaE)
                 BT9727_3686(ctaD) BT9727_3687(ctaC) BT9727_3689(ctaA)
            BLI: BL02980(ctaC) BL02981(ctaD) BL02982(ctaE) BL02983(ctaF)
            BLD: BLi01706(ctaC) BLi01707(ctaD) BLi01708(ctaE) BLi01709(ctaF)
            BCL: ABC2390(ctaF) ABC2391(ctaE) ABC2392(ctaD) ABC2393(ctaC)
            BAY: RBAM_014750(ctaC) RBAM_014760(ctaD) RBAM_014770(ctaE)
                 RBAM_014780(ctaF) RBAM_019900(ypmQ)
            BPU: BPUM_1381(ctaC) BPUM_1382(ctaD) BPUM_1383(ctaE)
                 BPUM_1384(ctaF)
            OIH: OB1437(ctaC) OB1438(ctaD) OB1439(ctaE) OB1440(ctaF) OB1745
                 OB1746
            GKA: GK1082(ctaC) GK1083(ctaD) GK1084(ctaE) GK1085(ctaF) GK1546
                 GK1547 GK1670 GK1671 GK3457(qoxC)
            SAJ: SaurJH9_1119
            SAH: SaurJH1_1142
            LWE: lwe2078(ctaA)
            STH: STH2096 STH2097 STH2098 STH3152 STH3153
            MTU: Rv2193(ctaE) Rv2200c(ctaC) Rv3043c(ctaD)
            MTC: MT2249(ctaE) MT2256(ctaC) MT3128(ctaD)
            MBO: Mb2216(ctaE) Mb2223c(ctaC) Mb3069c(ctaD)
            MBB: BCG_2209(ctaE) BCG_2216c(ctaC) BCG_3067c(ctaD)
            MLE: ML0875(ctaC) ML0882(ctaE) ML1728
            MPA: MAP1932(ctaE) MAP1940c(ctaC) MAP3091c(ctaD)
            MAV: MAV_2291 MAV_2292 MAV_2299 MAV_3908(ctaD)
            MSM: MSMEG_4260 MSMEG_4267 MSMEG_4268 MSMEG_4437(ctaD)
            MVA: Mvan_2082 Mvan_3704 Mvan_5610
            MGI: Mflv_1196 Mflv_2818 Mflv_4277 Mflv_5341 Mflv_5377
            MMC: Mmcs_1852 Mmcs_3291 Mmcs_3298 Mmcs_3438
            MKM: Mkms_1899 Mkms_3501 Mkms_5670
            MJL: Mjls_1833 Mjls_3449
            CGL: NCgl2112(cgl2192) NCgl2115(cgl2195) NCgl2437(cgl2523)
            CGB: cg2406(ctaE) cg2409(ctaC) cg2780(ctaD)
            CEF: CE2085 CE2087 CE2418(ctaD)
            CDI: DIP1627(ctaE) DIP1629 DIP1864(ctaD)
            CJK: jk0481(ctaD) jk0716(ctaC) jk0719(ctaE)
            NFA: nfa11940 nfa17080 nfa17260 nfa42940
            RHA: RHA1_ro01130 RHA1_ro01137 RHA1_ro04224 RHA1_ro06446
                 RHA1_ro08285
            SCO: SCO2151(cox3) SCO2155(cox1) SCO2156(cox) SCO7234(ctaD)
            SMA: SAV6047(ctaC) SAV6048(ctaD1) SAV6052(ctaE) SAV6537(ctaD2)
            TWH: TWT243(ctaC) TWT244(ctaD) TWT246(ctaE)
            TWS: TW524(ctaE) TW526(ctaD) TW527(ctaC)
            LXX: Lxx09850(ctaE) Lxx15040(ctaD) Lxx15050(ctaC)
            CMI: CMM_1834(ctaE) CMM_1841(ctaD) CMM_1842(ctaC)
            ART: Arth_2216
            AAU: AAur_2207 AAur_2214(ctaD) AAur_2215 AAur_pTC10179(ctaE)
            PAC: PPA0701 PPA0702 PPA0713
            NCA: Noca_3140 Noca_4865
            TFU: Tfu_0881 Tfu_1015 Tfu_1016 Tfu_1022 Tfu_1695
            FRA: Francci3_2009 Francci3_2493 Francci3_3108 Francci3_3116
                 Francci3_3117 Francci3_3821
            FAL: FRAAL4147(ctaD) FRAAL5112(ctaF) FRAAL5122(cyoB)
                 FRAAL5123(cyoA) FRAAL6078(cyoB)
            ACE: Acel_0490 Acel_0956 Acel_0957 Acel_0964
            KRA: Krad_3258
            SEN: SACE_1187(ctaD) SACE_1678(ctaC) SACE_1684(ctaE)
                 SACE_4988(ctaE) SACE_7041(ctaD)
            STP: Strop_1094 Strop_2143 Strop_3299
            RBA: RB12681(ctaC) RB12683(ctaD) RB12685(ctaE) RB12687(ctaF)
                 RB3953 RB4416 RB4417 RB4646(cox3) RB6350 RB6353
            PCU: pc1977(fixO) pc1978(fixN)
            LIL: LA0242(ctaC) LA0243(ctaD) LA0244(ctaE) LA3499 LA4027 LB343
            LIC: LIC10208(cyoA) LIC10209(cyoB) LIC10210(cyoC) LIC10688
                 LIC20261
            LBJ: LBJ_1474(ccoN) LBJ_1475(ccoO) LBJ_1477(cccA) LBJ_2793(cyoC)
                 LBJ_2794(cyoB) LBJ_2795(cyoA)
            LBL: LBL_0276(cyoA) LBL_0277(cyoB) LBL_0278(cyoC) LBL_1698(ccoN)
                 LBL_1699(ccoO) LBL_1701(cccA)
            SYN: sll0813(ctaC) slr1136(coxB) slr1137(coxA) slr1138(ctaEI)
                 slr2082(ctaD) slr2083(ctaE)
            SYW: SYNW1528(coxB) SYNW1529(coxA) SYNW1530(coxC) SYNW1861(coxB)
                 SYNW1862(coxA) SYNW1863(coxC)
            SYC: syc1309_d(ccoN) syc1506_c(ctaE) syc1507_c(ctaD)
                 syc1508_c(ctaC)
            SYF: Synpcc7942_0202 Synpcc7942_2602 Synpcc7942_2603
                 Synpcc7942_2604
            SYD: Syncc9605_0606 Syncc9605_0607 Syncc9605_0608 Syncc9605_0979
                 Syncc9605_0980 Syncc9605_0981
            SYE: Syncc9902_1754 Syncc9902_1755 Syncc9902_1756
            SYG: sync_1927 sync_1928 sync_1929 sync_2125 sync_2126
                 sync_2127(coxB)
            SYR: SynRCC307_0670(ctaE) SynRCC307_0671(ctaD)
                 SynRCC307_0672(ctaC) SynRCC307_1934(ctaE) SynRCC307_1935(ctaD)
                 SynRCC307_1937(ctaC)
            SYX: SynWH7803_0713(ctaE) SynWH7803_0714(ctaD)
                 SynWH7803_0715(ctaC) SynWH7803_1871(ctaC) SynWH7803_1872(ctaD)
                 SynWH7803_1873(ctaE)
            CYA: CYA_1512(ctaE) CYA_1513(ctaD) CYA_1514(ctaC)
            CYB: CYB_2697(coxB) CYB_2698(ctaD) CYB_2700(ctaE)
            TEL: tll2009(coxC) tll2010(coxA) tll2011(coxB)
            GVI: gll2162(coxC) gll2163(coxA) gll2164(coxB) glr0739(ctaC)
                 glr0740(ctaD)
            ANA: alr0950(coxB1) alr0951(coxA1) alr0952(coxC1) alr2514(coxB2)
                 alr2515(coxA2) alr2516(coxC2) alr2731(ctaC) alr2732(ctaD)
                 alr2734(ctaE)
            AVA: Ava_0446 Ava_0447 Ava_0448 Ava_0528 Ava_0529 Ava_0530
                 Ava_3575 Ava_3576 Ava_3577 Ava_4298 Ava_4299 Ava_4300
                 Ava_B0177 Ava_B0178 Ava_B0179
            PMA: Pro0440(cyoC) Pro0441(cyoB) Pro0442(cyoA)
            PMM: PMM0444(ctaE) PMM0445(ctaD) PMM0446(ctaC)
            PMT: PMT1341(ctaC) PMT1342(ctaD) PMT1343(ctaE)
            PMN: PMN2A_1775 PMN2A_1776 PMN2A_1777
            PMI: PMT9312_0443 PMT9312_0444 PMT9312_0445
            PMB: A9601_04991(ctaE) A9601_05001(cyoB) A9601_05011(ctaC)
            PMC: P9515_05061(cyoC) P9515_05071(cyoB) P9515_05081(cyoA)
                 P9515_12631 P9515_12641 P9515_12651(ctaE)
            PMF: P9303_06401(ctaE) P9303_06411(cyoB) P9303_06421(ctaC)
            PMG: P9301_04681(ctaE) P9301_04691(cyoB) P9301_04701(cyoA)
            PME: NATL1_04981(ctaE) NATL1_04991(cyoB) NATL1_05001(cyoA)
            TER: Tery_0276 Tery_0277 Tery_0278 Tery_1777 Tery_1778 Tery_1779
            SRU: SRU_0313(coxB2) SRU_0314(coxA2) SRU_0322 SRU_0323 SRU_2098
                 SRU_2099(coxA1) SRU_2100(coxB1)
            CHU: CHU_1138(cyo) CHU_2202(cox3) CHU_2203(coxO) CHU_2206(coxN)
                 CHU_2207(ctaC)
            GFO: GFO_0166(ctaC) GFO_0167(ctaD) GFO_0189(ctaE) GFO_1397
                 GFO_1398 GFO_1433(ccoN) GFO_1435(ccoP)
            FJO: Fjoh_1641
            FPS: FP0088 FP0378 FP0379 FP0919 FP0920 FP1156(ccoN) FP1158(ccoP)
                 FP2111
            CCH: Cag_1356 Cag_1357 Cag_1358
            RRS: RoseRS_2264
            RCA: Rcas_3557
            DRA: DR_2619(ctaC) DR_2620
            DGE: Dgeo_0016 Dgeo_0017 Dgeo_0406 Dgeo_0407
            TTH: TTC0768 TTC0769 TTC0770 TTC1671 TTC1672
            TTJ: TTHA0311 TTHA0312 TTHA1133 TTHA1134 TTHA1135
            AAE: aq_2188(coxC) aq_2190(coxB) aq_2191(coxA1) aq_2191a(coxB2)
                 aq_2192(coxA2)
            AFU: AF0142 AF0144(cbaB) AF0190
            HAL: VNG0657G(coxA2) VNG0662G(coxC) VNG0665G(coxB1)
                 VNG2193Gm(coxA1) VNG2195G(coxB2)
            HMA: rrnAC0043(coxB1) rrnAC0880(coxA4) rrnAC0882(coxC)
                 rrnAC1153(coxB2) rrnAC1154(coxA3) rrnAC1278(coxA1)
                 rrnAC1399(cyoC) rrnAC2310(coxB4) rrnAC2311(coxA2)
            HWA: HQ1578A(coxB) HQ1611A(coxA) HQ2352A(coxC)
            NPH: NP2448A(coxB_1) NP2450A(coxC) NP2456A(coxA_1) NP2962A(cbaA)
                 NP2964A(cbaB) NP2966A(cbaD) NP2968A(cbaE) NP4294A(coxB_3)
                 NP4296A(coxA_3)
            PTO: PTO1304 PTO1306
            APE: APE_0792.1 APE_0793.1 APE_1623 APE_1720
            STO: ST0611 ST0676 ST2053 ST2594 ST2595
            SAI: Saci_0097(cbaA)
            MSE: Msed_0290 Msed_0324 Msed_0570
            PAI: PAE1355 PAE1357
            PCL: Pcal_1943 Pcal_1949
STRUCTURES  PDB: 1AR1  1EHK  1HR8  1M56  1M57  1OCC  1OCO  1OCR  1OCZ  1QLE  
                 1V54  1V55  1W2L  1XME  2CUA  2DYR  2DYS  2EIJ  2EIK  2EIL  
                 2EIM  2EIN  2FWL  2GSM  2OCC  2ODX  
DBLINKS     IUBMB Enzyme Nomenclature: 1.9.3.1
            ExPASy - ENZYME nomenclature database: 1.9.3.1
            ExplorEnz - The Enzyme Database: 1.9.3.1
            ERGO genome analysis and discovery system: 1.9.3.1
            BRENDA, the Enzyme Database: 1.9.3.1
            CAS: 9001-16-5
///
ENTRY       EC 1.9.3.2        Obsolete  Enzyme
NAME        Transferred to 1.7.2.1
CLASS       Oxidoreductases;
            Acting on a heme group of donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now included with EC 1.7.2.1, nitrite reductase
            (NO-forming) (EC 1.9.3.2 created 1965, deleted 2002)
STRUCTURES  PDB: 1BL9  1DY7  1GJQ  1GQ1  1HZU  1HZV  1N15  1N50  1N90  1NIR  
                 1NNO  1XLN  1XLO  1XLP  1XLQ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.9.3.2
            ExPASy - ENZYME nomenclature database: 1.9.3.2
            ExplorEnz - The Enzyme Database: 1.9.3.2
            ERGO genome analysis and discovery system: 1.9.3.2
            BRENDA, the Enzyme Database: 1.9.3.2
///
ENTRY       EC 1.9.6.1                  Enzyme
NAME        nitrate reductase (cytochrome);
            respiratory nitrate reductase;
            benzyl viologen-nitrate reductase
CLASS       Oxidoreductases;
            Acting on a heme group of donors;
            With a nitrogenous group as acceptor
SYSNAME     ferrocytochrome:nitrate oxidoreductase
REACTION    2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite
            [RN:R03071]
ALL_REAC    R03071 > R00792
SUBSTRATE   ferrocytochrome [CPD:C00924];
            H+ [CPD:C00080];
            nitrate [CPD:C00244]
PRODUCT     ferricytochrome [CPD:C00923];
            nitrite [CPD:C00088]
REFERENCE   1  [PMID:13412117]
  AUTHORS   SADANA JC, MCELROY WD.
  TITLE     Nitrate reductase from Achromobacter fischeri; purification and
            properties:  function of flavines and cytochrome.
  JOURNAL   Arch. Biochem. Biophys. 67 (1957) 16-34.
  ORGANISM  Achromobacter fischeri
PATHWAY     PATH: map00910  Nitrogen metabolism
GENES       VFI: VF1903(napC) VF1904(napB)
DBLINKS     IUBMB Enzyme Nomenclature: 1.9.6.1
            ExPASy - ENZYME nomenclature database: 1.9.6.1
            ExplorEnz - The Enzyme Database: 1.9.6.1
            ERGO genome analysis and discovery system: 1.9.6.1
            BRENDA, the Enzyme Database: 1.9.6.1
            CAS: 9029-42-9
///
ENTRY       EC 1.9.99.1                 Enzyme
NAME        iron---cytochrome-c reductase;
            iron-cytochrome c reductase
CLASS       Oxidoreductases;
            Acting on a heme group of donors;
            With other acceptors
SYSNAME     ferrocytochrome-c:Fe3+ oxidoreductase
REACTION    ferrocytochrome c + Fe3+ = ferricytochrome c + Fe2+ [RN:R05318]
ALL_REAC    R05318
SUBSTRATE   ferrocytochrome c [CPD:C00126];
            Fe3+ [CPD:C14819]
PRODUCT     ferricytochrome c [CPD:C00125];
            Fe2+ [CPD:C14818]
COFACTOR    Iron [CPD:C00023]
COMMENT     An iron protein.
REFERENCE   1  [PMID:4288725]
  AUTHORS   Yates MG, Nason A.
  TITLE     Electron transport systems of the chemoautotroph Ferrobacillus
            ferrooxidans. II. Purification and properties of a heat-labile
            iron-cytochrome c reductase.
  JOURNAL   J. Biol. Chem. 241 (1966) 4872-80.
  ORGANISM  Ferrobacillus ferrooxidans
DBLINKS     IUBMB Enzyme Nomenclature: 1.9.99.1
            ExPASy - ENZYME nomenclature database: 1.9.99.1
            ExplorEnz - The Enzyme Database: 1.9.99.1
            ERGO genome analysis and discovery system: 1.9.99.1
            BRENDA, the Enzyme Database: 1.9.99.1
            CAS: 37256-52-3
///
ENTRY       EC 1.10.1.1                 Enzyme
NAME        trans-acenaphthene-1,2-diol dehydrogenase;
            trans-1,2-acenaphthenediol dehydrogenase
CLASS       Oxidoreductases;
            Acting on diphenols and related substances as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     (+/-)-trans-acenaphthene-1,2-diol:NADP+ oxidoreductase
REACTION    (+/-)-trans-acenaphthene-1,2-diol + 2 NADP+ = acenaphthenequinone +
            2 NADPH + 2 H+ [RN:R04059]
ALL_REAC    R04059
SUBSTRATE   (+/-)-trans-acenaphthene-1,2-diol [CPD:C04167];
            NADP+ [CPD:C00006]
PRODUCT     acenaphthenequinone [CPD:C02807];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Some preparations also utilize NAD+.
REFERENCE   1
  AUTHORS   Hopkins, R.P., Drummond, E.C. and Callaghan, P.
  TITLE     Dehydrogenation of trans-acenaphthene-1,2-diol by liver cytosol
            preparations.
  JOURNAL   Biochem. Soc. Trans. 1 (1973) 989-991.
DBLINKS     IUBMB Enzyme Nomenclature: 1.10.1.1
            ExPASy - ENZYME nomenclature database: 1.10.1.1
            ExplorEnz - The Enzyme Database: 1.10.1.1
            ERGO genome analysis and discovery system: 1.10.1.1
            BRENDA, the Enzyme Database: 1.10.1.1
            CAS: 51901-21-4
///
ENTRY       EC 1.10.2.1                 Enzyme
NAME        L-ascorbate---cytochrome-b5 reductase;
            ascorbate-cytochrome b5 reductase
CLASS       Oxidoreductases;
            Acting on diphenols and related substances as donors;
            With a cytochrome as acceptor
SYSNAME     L-ascorbate:ferricytochrome-b5 oxidoreductase
REACTION    L-ascorbate + ferricytochrome b5 = monodehydroascorbate +
            ferrocytochrome b5 + H+ [RN:R03147]
ALL_REAC    R03147
SUBSTRATE   L-ascorbate [CPD:C00072];
            ferricytochrome b5 [CPD:C00996]
PRODUCT     monodehydroascorbate [CPD:C01041];
            ferrocytochrome b5 [CPD:C00999];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:5363650]
  AUTHORS   Everling FB, Weis W, Staudinger H.
  TITLE     [Kinetic studies on an ascorbate: ferricytochrome b5 oxidoreductase
            (EC 1.1.2.?)]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 350 (1969) 1485-92.
DBLINKS     IUBMB Enzyme Nomenclature: 1.10.2.1
            ExPASy - ENZYME nomenclature database: 1.10.2.1
            ExplorEnz - The Enzyme Database: 1.10.2.1
            ERGO genome analysis and discovery system: 1.10.2.1
            BRENDA, the Enzyme Database: 1.10.2.1
            CAS: 37237-57-3
///
ENTRY       EC 1.10.2.2                 Enzyme
NAME        ubiquinol---cytochrome-c reductase;
            coenzyme Q-cytochrome c reductase;
            dihydrocoenzyme Q-cytochrome c reductase;
            reduced ubiquinone-cytochrome c reductase, complex III
            (mitochondrial electron transport);
            ubiquinone-cytochrome c reductase;
            ubiquinol-cytochrome c oxidoreductase;
            reduced coenzyme Q-cytochrome c reductase;
            ubiquinone-cytochrome c oxidoreductase;
            reduced ubiquinone-cytochrome c oxidoreductase;
            mitochondrial electron transport complex III;
            ubiquinol-cytochrome c-2 oxidoreductase;
            ubiquinone-cytochrome b-c1 oxidoreductase;
            ubiquinol-cytochrome c2 reductase;
            ubiquinol-cytochrome c1 oxidoreductase;
            CoQH2-cytochrome c oxidoreductase;
            ubihydroquinol:cytochrome c oxidoreductase;
            coenzyme QH2-cytochrome c reductase;
            QH2:cytochrome c oxidoreductase
CLASS       Oxidoreductases;
            Acting on diphenols and related substances as donors;
            With a cytochrome as acceptor
SYSNAME     ubiquinol:ferricytochrome-c oxidoreductase
REACTION    QH2 + 2 ferricytochrome c = Q + 2 ferrocytochrome c + 2 H+
            [RN:R02161]
ALL_REAC    R02161
SUBSTRATE   QH2 [CPD:C00390];
            ferricytochrome c [CPD:C00125]
PRODUCT     Q [CPD:C00399];
            ferrocytochrome c [CPD:C00126];
            H+ [CPD:C00080]
COFACTOR    Cytochrome c1 [CPD:C02021];
            Cytochrome b-562 [CPD:C02396];
            Cytochrome b-566 [CPD:C02397];
            2-Iron ferredoxin [CPD:C02503]
COMMENT     Contains cytochromes b-562, b-566 and c1, and a 2-iron ferredoxin.
            Depending on the organism and physiological conditions, either two
            or four protons are extruded from the cytoplasmic to the
            non-cytoplasmic compartment (cf. EC 1.6.99.3 NADH dehydrogenase).
REFERENCE   1  [PMID:597492]
  AUTHORS   Marres CM, Slater EC.
  TITLE     Polypeptide composition of purified QH2:cytochrome c oxidoreductase
            from beef-heart mitochondria.
  JOURNAL   Biochim. Biophys. Acta. 462 (1977) 531-48.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:788795]
  AUTHORS   Rieske JS.
  TITLE     Composition, structure, and function of complex III of the
            respiratory chain.
  JOURNAL   Biochim. Biophys. Acta. 456 (1976) 195-247.
  ORGANISM  cow [GN:bta], rat [GN:rno], Candida utilis, pigeon
REFERENCE   3  [PMID:6267990]
  AUTHORS   Wikstrom M, Krab K, Saraste M.
  TITLE     Proton-translocating cytochrome complexes.
  JOURNAL   Annu. Rev. Biochem. 50 (1981) 623-55.
PATHWAY     PATH: map00190  Oxidative phosphorylation
ORTHOLOGY   KO: K00410  ubiquinol-cytochrome c reductase
            KO: K00411  ubiquinol-cytochrome c reductase iron-sulfur subunit
            KO: K00412  ubiquinol-cytochrome c reductase cytochrome b subunit
            KO: K00413  ubiquinol-cytochrome c reductase cytochrome c1 subunit
            KO: K00414  ubiquinol-cytochrome c reductase core subunit 1
            KO: K00415  ubiquinol-cytochrome c reductase core subunit 2
            KO: K00416  ubiquinol-cytochrome c reductase subunit 6
            KO: K00417  ubiquinol-cytochrome c reductase subunit 7
            KO: K00418  ubiquinol-cytochrome c reductase subunit 8
            KO: K00419  ubiquinol-cytochrome c reductase subunit 9
            KO: K00420  ubiquinol-cytochrome c reductase subunit 10
GENES       HSA: 10975(UQCR) 1537(CYC1) 27089(UQCRQ) 29796(UCRC) 4519(CYTB)
                 7381(UQCRB) 7384(UQCRC1) 7385(UQCRC2) 7386(UQCRFS1)
                 7388(UQCRH)
            PTR: 460348(UQCRC1) 464294(LOC464294) 468094(UQCRC2) 472893(CYC1)
                 807858(CYTB)
            MCC: 708396(UQCR)
            MMU: 17711(CYTB) 22272(Uqcrq) 22273(Uqcrc1) 66152(1110020P15Rik)
                 66445(Cyc1) 66576(Uqcrh) 66594(Uqcr) 66694(Uqcrfs1)
                 67003(Uqcrc2) 67530(Uqcrb)
            RNO: 26192(CYTB) 291103(Uqcrfs1) 293448(Uqcrc2)
                 300047(Cyc1_predicted) 301011(Uqcrc1) 362897(Uqcrb_predicted)
                 366448(Uqcrh)
            CFA: 475121(LOC475121) 476503(LOC476503) 477944(LOC477944)
                 479815(LOC479815) 486347(LOC486347) 608455(LOC608455)
                 609744(LOC609744) 611791(LOC611791) 804486(CYTB)
            BTA: 281570(UQCR) 282393(UQCRC1) 282394(UQCRC2) 286885(QP-C)
                 287020(UQCRFS1) 3283889(CYTB)
            SSC: 808513(CYTB)
            GGA: 415752(UQCRFS1) 416013(LOC416013) 416336(LOC416336)
                 420236(LOC420236) 427009(LOC427009) 770135(LOC770135)
                 770937(LOC770937) 771939(LOC771939) 807641(CYTB)
            XLA: 2642080(CYTB) 379401(uqcrc1) 379942(uqcrfs1) 380071(cyc1)
                 380093(uqcrc2) 446522(uqcrc2) 447091(MGC85256)
            XTR: 3283504(CYTB) 394506(uqcrfs1) 394843(MGC75973)
            DRE: 140512(CYTB) 393793(zgc:73404) 406359(uqcrfs1)
            SPU: 2652727(CYTB) 580369(LOC580369) 584954(LOC584954)
                 586030(LOC586030) 586686(LOC586686) 590393(LOC590393)
                 594483(LOC594483) 754314(LOC754314)
            DME: CYTB Dmel_CG14482 Dmel_CG14508 Dmel_CG17856 Dmel_CG30354
                 Dmel_CG3560 Dmel_CG4769 Dmel_CG7361(RFeSP) Dmel_CG8764(ox)
            CEL: C54G4.8(cyc-1) CYTB F42G8.12(isp-1) F45H10.2 F57B10.14
                 R07E4.3 T02H6.11 T10B10.2(ucr-2.2) T24C4.1(ucr-2.3) T27E9.2
            ATH: AT1G15120 AT2G01090 AT3G27240 AT3G52730 AT4G32470 AT5G13430
                 AT5G13440 AT5G25450 AT5G40810
            OSA: 4326795 4329497 4334506 4335710 4338350 4338723 4342681
                 4349859 cob
            CME: CMD048C CMG215C CMK031C CMN203C CMP152C CMR178C
            SCE: Q0105(COB) YBL045C(COR1) YDR529C(QCR7) YEL024W(RIP1)
                 YFR033C(QCR6) YGR183C(QCR9) YHR001W-A(QCR10) YJL166W(QCR8)
                 YOR065W(CYT1) YPR191W(QCR2)
            AGO: AGOS_AAL145W AGOS_ABR146W AGOS_ACL199C AGOS_ADL124C
                 AGOS_ADR208W AGOS_AEL067W AGOS_AEL121W AGOS_AFR731W
                 AGOS_AGL059C AGOS_AMI008W
            KLA: KllafMp02(CYTB)
            PIC: PICST_39828(UCRI) PICST_52082(QCR10) PICST_73333(UCR7)
                 PICST_75355(QCR6) PICST_77955(QCR8) PICST_78316(UQC2)
                 PICST_81500(COR1) PICST_86147(CYT1)
            CAL: CaO19.3527 CaO19_4016(CaO19.4016)
            CGR: CAGL0D05192g CAGL0F04565g CAGL0G10131g CAGL0G10153g
                 CAGL0H09328g CAGL0I03190g CAGL0I06270g CAGL0K02893g
                 CAGL0L10406g CaglfMp03(cyb)
            SPO: SPAC1782.07(qcr8) SPBC16C6.08c SPBC16H5.06(rip1) SPBC29A3.18
                 SPBP4H10.08 SPCC613.10 SPCC737.02c SPCp015
            ANI: AN0357.2 AN2306.2 AN3922.2 AN4388.2 AN5597.2 AN8273.2
            AFM: AFUA_1G02070 AFUA_1G13480 AFUA_4G11390 AFUA_5G04210
                 AFUA_5G10610
            AOR: AO090001000498 AO090003001082 AO090005000888 AO090010000475
                 AO090102000625
            CNE: CND04430 CNE02310 CNF00630 CNH02740 CNL04470 CNL05510
            UMA: UM01478.1 UM03526.1 UM03825.1 UM03913.1 UM04237.1 cob
            DDI: DDBDRAFT_0184465 DDBDRAFT_0185618 DDBDRAFT_0186273
                 DidioMp12(cytB)
            PFA: PF14_0248 PF14_0373 PF14_0597 PFE1155c
            TAN: TA06055 TA07960 TA08150 TA10085
                 q2ca38.03c(Tap370b08.q2ca38.03c)
            TPV: TP01_0151 TP01_0860 TP02_0218 TP04_0347 TP04_0384 TP04_0913
            TET: TTHERM_00295080 TTHERM_00918500 TepyoMp32(cob)
            TBR: Tb09.211.4700 Tb10.70.2970 Tb927.4.4990 Tb927.5.1060
                 Tb927.8.1890
            TCR: 504575.15 506295.100 506999.90 508301.20 510759.120 511181.50
                 511391.160
            LMA: LmjF07.0060 LmjF35.0100 LmjF35.1380 LmjF35.1540
            XFA: XF0908 XF0909 XF0910
            XFT: PD1775(petC) PD1776(petB) PD1777(petA)
            XCC: XCC2322(petC) XCC2323(petB) XCC2324(petA)
            XCB: XC_1792 XC_1793 XC_1794
            XCV: XCV2632(petC) XCV2633(petB) XCV2634(petA)
            XAC: XAC2455(petC) XAC2456(petB) XAC2457(petA)
            XOO: XOO2760(petC) XOO2761(petB) XOO2762(petA)
            XOM: XOO_2600(XOO2600) XOO_2601(XOO2601) XOO_2602(XOO2602)
            VCH: VC0573 VC0574 VC0575
            VCO: VC0395_A0105(petA)
            VVU: VV1_0595 VV1_0596 VV1_0597
            VVY: VV0596 VV0597 VV0598
            VPA: VP0441 VP0442 VP0443
            VFI: VF2217 VF2218 VF2219 VF2220
            PPR: PBPRA3233 PBPRA3234 PBPRA3235
            PAE: PA4429 PA4430 PA4431
            PAU: PA14_57540 PA14_57560 PA14_57570
            PAP: PSPA7_5003(petA)
            PPU: PP_1317(petA) PP_1318(petB) PP_1319(petC)
            PPF: Pput_4407
            PFL: PFL_5078 PFL_5079(petB) PFL_5080(petA)
            PFO: Pfl_4690 Pfl_4691 Pfl_4692
            PEN: PSEEN4503(petC) PSEEN4504(petB) PSEEN4505(petA)
            PAR: Psyc_1420 Psyc_1421 Psyc_1422
            PCR: Pcryo_1583 Pcryo_1584 Pcryo_1585
            PRW: PsycPRwf_0796
            SON: SO_0608(petA) SO_0609(petB) SO_0610(petC)
            SDN: Sden_3199 Sden_3200 Sden_3201
            SFR: Sfri_3305 Sfri_3307
            SAZ: Sama_3021
            SBL: Sbal_0562
            SBM: Shew185_3763
            SPC: Sputcn32_3276
            SSE: Ssed_0801
            SPL: Spea_3536
            SHE: Shewmr4_0602 Shewmr4_0603 Shewmr4_0604
            SHM: Shewmr7_3426 Shewmr7_3427 Shewmr7_3428
            SHN: Shewana3_0601 Shewana3_0602 Shewana3_0603 Shewana3_3559
            SHW: Sputw3181_0665
            ILO: IL0416 IL0417 IL0418
            CPS: CPS_4438(petC) CPS_4439(petB) CPS_4440(petA)
            PHA: PSHAa2528 PSHAa2529 PSHAa2530
            PAT: Patl_3699 Patl_3700 Patl_3701
            SDE: Sde_3162
            MAQ: Maqu_2470
            LPN: lpg2703 lpg2704(petB) lpg2705(petA)
            LPF: lpl2631(petC) lpl2632(petB) lpl2633(petA)
            LPP: lpp2758(petC) lpp2759(petB) lpp2760(petA)
            MCA: MCA1960(petC) MCA1961(petB) MCA1962(petA)
            TCX: Tcr_0991 Tcr_0992 Tcr_0993
            NOC: Noc_0297 Noc_0298 Noc_0299
            AEH: Mlg_2209 Mlg_2210 Mlg_2211
            HHA: Hhal_0182
            HCH: HCH_05898 HCH_05899 HCH_05900(petA)
            ABO: ABO_0578(petA) ABO_0579(petB) ABO_0580(petC)
            AHA: AHA_3901 AHA_3902(petB) AHA_3903(petA)
            RMA: Rmag_0011
            VOK: COSY_0010(petC) COSY_0011(petB) COSY_0012(petA)
            NME: NMB2051 NMB2052 NMB2053
            NMA: NMA0383(petA) NMA0384(petB) NMA0385(petC)
            NMC: NMC2033(petB)
            NGO: NGO2029(petA) NGO2030(petB) NGO2031(petC)
            CVI: CV_4006(petC) CV_4007(petB) CV_4008(petA)
            RSO: RSc2927(petC) RSc2928(petB) RSc2929(petA)
            REU: Reut_A3091 Reut_A3092 Reut_A3093
            REH: H16_A3396(qcrC) H16_A3397(qcrB) H16_A3398(qcrA)
            RME: Rmet_3228 Rmet_3229 Rmet_3230
            BMA: BMA2696(petC) BMA2697(petB) BMA2698(petA)
            BMV: BMASAVP1_A3256(petA) BMASAVP1_A3257(petB)
                 BMASAVP1_A3258(petC)
            BML: BMA10299_A1805(petA) BMA10299_A1806(petB)
                 BMA10299_A1807(petC)
            BMN: BMA10247_2746(petC) BMA10247_2747(petB) BMA10247_2748(petA)
            BXE: Bxe_A0414 Bxe_A0415 Bxe_A0416
            BVI: Bcep1808_0420
            BUR: Bcep18194_A3539 Bcep18194_A3540 Bcep18194_A3541
            BCN: Bcen_2664 Bcen_2665 Bcen_2666
            BCH: Bcen2424_0441 Bcen2424_0442 Bcen2424_0443
            BAM: Bamb_0359 Bamb_0360 Bamb_0361
            BPS: BPSL3121(petC) BPSL3122(petB) BPSL3123(petA)
            BPM: BURPS1710b_3673(petC) BURPS1710b_3674(petB)
                 BURPS1710b_3676(petA)
            BPL: BURPS1106A_3705(petC) BURPS1106A_3706(petB)
                 BURPS1106A_3707(petA)
            BPD: BURPS668_3648(petC) BURPS668_3649(petB) BURPS668_3650(petA)
            BTE: BTH_I2975 BTH_I2976 BTH_I2977(petA)
            PNU: Pnuc_0125
            BPE: BP0275(petC) BP0276(petB) BP0277(petA)
            BPA: BPP4283(petA) BPP4284(petB) BPP4285(petC)
            BBR: BB4870(petA) BB4871(petB) BB4872(petC)
            RFR: Rfer_2964 Rfer_2965 Rfer_2966
            POL: Bpro_0821 Bpro_0822 Bpro_0823 Bpro_3500
            PNA: Pnap_0713
            AAV: Aave_3696
            AJS: Ajs_0145 Ajs_0789
            VEI: Veis_3935
            MPT: Mpe_A0849 Mpe_A0850 Mpe_A0851 Mpe_A1832
            MMS: mma_3269 mma_3270(cytB) mma_3271
            NEU: NE0809 NE0810 NE0811(petC)
            NET: Neut_1110 Neut_1111 Neut_1112
            NMU: Nmul_A1003 Nmul_A1004 Nmul_A1005
            EBA: ebA1196(petC) ebA1197(petB) ebA1198(petA)
            AZO: azo0960(petA1)
            DAR: Daro_0809 Daro_0810 Daro_0811
            TBD: Tbd_1831 Tbd_1832 Tbd_1833
            HPY: HP1539(fbcH) HP1540(fbcF)
            HPJ: jhp1459(petA) jhp1460(petB) jhp1461(petC)
            HPA: HPAG1_1487 HPAG1_1488 HPAG1_1489
            HHE: HH1005 HH1006 HH1007
            HAC: Hac_0300(fbcF) Hac_0301(fbcB) Hac_0302(fbcC)
            WSU: WS2152(petA) WS2153(cytB) WS2154(petC)
            TDN: Tmden_1919 Tmden_1920 Tmden_1921
            CJE: Cj1184c(petC) Cj1185c(petB) Cj1186c(petA)
            CJR: CJE1318(petC) CJE1319(petB) CJE1320(petA)
            CJJ: CJJ81176_1199(petC) CJJ81176_1200(petB) CJJ81176_1201(petA)
            CJU: C8J_1128(petC) C8J_1129(petB) C8J_1130(petA)
            CJD: JJD26997_0543(petA) JJD26997_0544(petB) JJD26997_0545(petC)
            CFF: CFF8240_1448(petA)
            CCV: CCV52592_1814(petA)
            CHA: CHAB381_1238(petA)
            CCO: CCC13826_1921(petA)
            ABU: Abu_2064(petC) Abu_2065(petB) Abu_2066(petA)
            NIS: NIS_1583 NIS_1584 NIS_1585
            SUN: SUN_0208 SUN_0209 SUN_0210
            GSU: GSU1649
            GME: Gmet_1923
            RPR: RP270(petA) RP271(petB) RP272(fbcH)
            RTY: RT0261(petA) RT0262(petB) RT0263(fbcH)
            RCO: RC0358(petA) RC0359(petB) RC0360(fbcH)
            RFE: RF_1007(fbcH) RF_1009(petB) RF_1010(petA)
            RBE: RBE_0828(petA) RBE_0829(petB) RBE_0830(fbcH)
            OTS: OTBS_0259(fbcH) OTBS_1396(petA) OTBS_1397(petB)
            WOL: WD1070(petC) WD1071(petB) WD1201(petA)
            WBM: Wbm0406 Wbm0774 Wbm0775
            AMA: AM781(petC) AM783(petB) AM784(petA)
            APH: APH_0401(petA) APH_0402(petB) APH_0403(petC)
            ERU: Erum5020(petC) Erum5030(petB) Erum5040(petA)
            ERW: ERWE_CDS_05260 ERWE_CDS_05270(petB) ERWE_CDS_05280(petA)
            ERG: ERGA_CDS_05160 ERGA_CDS_05170(petB) ERGA_CDS_05180(petA)
            ECN: Ecaj_0510 Ecaj_0511 Ecaj_0512
            ECH: ECH_0520(petA) ECH_0521(petB) ECH_0522(petC)
            NSE: NSE_0624(petA) NSE_0625(petB) NSE_0626(petC)
            PUB: SAR11_0098(fbcH) SAR11_0099(petB) SAR11_0100(petA)
            MLO: mll2705 mll2706 mll2707 mlr0970 mlr0971
            MES: Meso_2164 Meso_2165 Meso_2166
            PLA: Plav_2242
            SME: SMc00187(fbcF) SMc00188(fbcB) SMc00189(fbcC)
            SMD: Smed_1541
            ATU: Atu2237(fbcC) Atu2238(fbcB) Atu2239(fbcF)
            ATC: AGR_C_4072 AGR_C_4073 AGR_C_4074
            RET: RHE_CH03036(fbcC) RHE_CH03037(fbcB) RHE_CH03038(fbcF)
            RLE: RL3484(petC) RL3485(petB) RL3486(petA)
            BME: BMEI0473 BMEI0474 BMEI0475
            BMF: BAB1_1557 BAB1_1558(petB) BAB1_1559
            BMS: BR1541 BR1542(petB) BR1543
            BMB: BruAb1_1530 BruAb1_1531(petB) BruAb1_1532
            BOV: BOV_1491(petB) BOV_1492(petA)
            OAN: Oant_1623
            BJA: blr2485 blr2486
            BRA: BRADO1976
            BBT: BBta_2300 BBta_p0097(petA)
            RPA: RPA1016(petA) RPA1192 RPA1193
            RPB: RPB_1200 RPB_1201 RPB_4306
            RPC: RPC_0924 RPC_0925 RPC_1923 RPC_3226
            RPD: RPD_1302 RPD_1303 RPD_4204
            RPE: RPE_0948 RPE_0949 RPE_1207 RPE_3977
            NWI: Nwi_2616 Nwi_2617
            NHA: Nham_3241
            CCR: CC_0472 CC_0473 CC_0474
            SIL: SPO0271(petA) SPO0272(petB) SPO0273(petC)
            SIT: TM1040_2812 TM1040_2813 TM1040_2814
            RSP: RSP_1394(fbcC) RSP_1395(fbcB) RSP_1396(fbcF)
            RSH: Rsph17029_0063
            RSQ: Rsph17025_2803
            JAN: Jann_0325 Jann_0327
            RDE: RD1_0563(petA) RD1_0564(petB) RD1_0565(petC)
            MMR: Mmar10_0185 Mmar10_0736 Mmar10_0737 Mmar10_0738
            HNE: HNE_0350(petA) HNE_0351 HNE_0352
            ZMO: ZMO0956 ZMO0957 ZMO0958(petC)
            NAR: Saro_0676 Saro_0677 Saro_0678
            SAL: Sala_1343 Sala_1344 Sala_1345
            SWI: Swit_1396
            ELI: ELI_13635 ELI_13640(petB) ELI_13645
            GOX: GOX0565 GOX0566 GOX0567
            RRU: Rru_A0362 Rru_A0363 Rru_A0364 Rru_A1192
            MAG: amb4088
            MGM: Mmc1_0356 Mmc1_0357 Mmc1_0358
            CGB: cg2403(qcrB)
            TFU: Tfu_1019
            FRA: Francci3_2489
            SEN: SACE_1687(qcrB)
            CCH: Cag_0395
            PLT: Plut_1718
            DRA: DR_0435 DR_0436
            DGE: Dgeo_0319
            TTH: TTC1567
            TTJ: TTHA1930
            AAE: aq_042(cyc) aq_044(petB) aq_045(petA)
STRUCTURES  PDB: 1BCC  1BE3  1BGY  1EZV  1KB9  1KYO  1L0L  1L0N  1NTK  1NTM  
                 1NTZ  1NU1  1P84  1PP9  1PPJ  1QCR  1RIE  1SQB  1SQP  1SQQ  
                 1SQV  1SQX  1ZRT  2A06  2BCC  2FYN  2FYU  2IBZ  2NUK  2NUM  
                 2NVE  2NVF  2NVG  2NWF  3BCC  
DBLINKS     IUBMB Enzyme Nomenclature: 1.10.2.2
            ExPASy - ENZYME nomenclature database: 1.10.2.2
            ExplorEnz - The Enzyme Database: 1.10.2.2
            ERGO genome analysis and discovery system: 1.10.2.2
            BRENDA, the Enzyme Database: 1.10.2.2
            CAS: 9027-03-6
///
ENTRY       EC 1.10.3.1                 Enzyme
NAME        catechol oxidase;
            diphenol oxidase;
            o-diphenolase;
            phenolase;
            polyphenol oxidase;
            tyrosinase;
            pyrocatechol oxidase;
            Dopa oxidase;
            catecholase;
            o-diphenol:oxygen oxidoreductase;
            o-diphenol oxidoreductase
CLASS       Oxidoreductases;
            Acting on diphenols and related substances as donors;
            With oxygen as acceptor
SYSNAME     1,2-benzenediol:oxygen oxidoreductase
REACTION    2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O [RN:R00058]
ALL_REAC    R00058;
            (other) R00031 R00045
SUBSTRATE   catechol [CPD:C00090];
            O2 [CPD:C00007]
PRODUCT     1,2-benzoquinone [CPD:C02351];
            H2O [CPD:C00001]
COFACTOR    Copper [CPD:C00070]
COMMENT     A group of copper proteins that act also on a variety of substituted
            catechols, and many of which also catalyse the reaction listed under
            EC 1.14.18.1 monophenol monooxygenase; this is especially true for
            the classical tyrosinase.
REFERENCE   1
  AUTHORS   Brown, F.C. and Ward, D.N.
  TITLE     Preparation of a soluble mammalian tyrosinase.
  JOURNAL   J. Am. Chem. Soc. 79 (1957) 2647-2648.
  ORGANISM  mammalian
REFERENCE   2
  AUTHORS   Dawson, C.R. and Tarpley, W.B.
  TITLE     The copper oxidases.
  JOURNAL   In: Sumner, J.B. and Myrback, K. (Eds.), The Enzymes, 1st ed., vol.
            2, Academic Press, New York, 1951, p. 454-498.
REFERENCE   3
  AUTHORS   Gregory, R.P.F. and Bendall, D.S.
  TITLE     The purification and some properties of the polyphenol oxidse from
            tea (Camellia sinensis L.).
  JOURNAL   Biochem. J. 101 (1966) 569-581.
  ORGANISM  Camellia sinensis
REFERENCE   4
  AUTHORS   Mason, H.S.
  TITLE     Structures and functions of the phenolase complex.
  JOURNAL   Nature (Lond.) 177 (1956) 79-81.
REFERENCE   5
  AUTHORS   Mayer, A.M. and Harel, E.
  TITLE     Polyphenol oxidases in plants.
  JOURNAL   Phytochemistry 18 (1979) 193-215.
  ORGANISM  Agaricus bisporus, Neurospora crassa [GN:dncr]
REFERENCE   6  [PMID:5842066]
  AUTHORS   Patil SS, Zucker M.
  TITLE     Potato phenolases. Purification and properties.
  JOURNAL   J. Biol. Chem. 240 (1965) 3938-43.
  ORGANISM  Solanum tuberosum [GN:estu]
REFERENCE   7  [PMID:4965136]
  AUTHORS   Pomerantz SH, Warner MC.
  TITLE     3,4-dihydroxy-L-phenylalanine as the tyrosinase cofactor. Occurrence
            in melanoma and binding constant.
  JOURNAL   J. Biol. Chem. 242 (1967) 5308-14.
  ORGANISM  hamster
REFERENCE   8
  AUTHORS   Robb, D.A.
  TITLE     `Tyrosinase.
  JOURNAL   In: Lontie, R. (Ed.), Copper Proteins and Copper Enzymes, vol. 2,
            CRC Press, Boca Raton, FL, 1984, p. 207-240.
PATHWAY     PATH: map00350  Tyrosine metabolism
ORTHOLOGY   KO: K00422  polyphenol oxidase
STRUCTURES  PDB: 1BT1  1BT2  1BT3  1BUG  
DBLINKS     IUBMB Enzyme Nomenclature: 1.10.3.1
            ExPASy - ENZYME nomenclature database: 1.10.3.1
            ExplorEnz - The Enzyme Database: 1.10.3.1
            ERGO genome analysis and discovery system: 1.10.3.1
            BRENDA, the Enzyme Database: 1.10.3.1
            CAS: 9002-10-2
///
ENTRY       EC 1.10.3.2                 Enzyme
NAME        laccase;
            urishiol oxidase;
            urushiol oxidase;
            p-diphenol oxidase
CLASS       Oxidoreductases;
            Acting on diphenols and related substances as donors;
            With oxygen as acceptor
SYSNAME     benzenediol:oxygen oxidoreductase
REACTION    4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O [RN:R00083]
ALL_REAC    R00083
SUBSTRATE   benzenediol [CPD:C01785];
            O2 [CPD:C00007]
PRODUCT     benzosemiquinone [CPD:C02389];
            H2O [CPD:C00001]
COFACTOR    Copper [CPD:C00070]
COMMENT     A group of multi-copper proteins of low specificity acting on both
            o- and p-quinols, and often acting also on aminophenols and
            phenylenediamine. The semiquinone may react further either
            enzymically or non-enzymically.
REFERENCE   1
  AUTHORS   Dawson, C.R. and Tarpley, W.B.
  TITLE     The copper oxidases.
  JOURNAL   In: Sumner, J.B. and Myrback, K. (Eds.), The Enzymes, 1st ed., vol.
            2, Academic Press, New York, 1951, p. 454-498.
REFERENCE   2
  AUTHORS   Keilin, D. and Mann, T.
  TITLE     Laccase, a blue copper-protein oxidase from the latex of Rhus
            succedanea.
  JOURNAL   Nature (Lond.) 143 (1939) 23-24.
  ORGANISM  Rhus succedanea
REFERENCE   3
  AUTHORS   Malmstrom, B.G., Andreasson, L.-E. and Reinhammar, B.
  TITLE     Copper-containing oxidases and superoxide dismutase.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 12, Academic
            Press, New York, 1975, p. 507-579.
REFERENCE   4
  AUTHORS   Mayer, A.M. and Harel, E.
  TITLE     Polyphenol oxidases in plants.
  JOURNAL   Phytochemistry 18 (1979) 193-215.
  ORGANISM  Agaricus bisporus, Neurospora crassa [GN:dncr]
REFERENCE   5  [PMID:13584395]
  AUTHORS   NAKAMURA T.
  TITLE     Purification and physico-chemical properties of laccase.
  JOURNAL   Biochim. Biophys. Acta. 30 (1958) 44-52.
  ORGANISM  Rhus vernicifera
REFERENCE   6  [PMID:13618260]
  AUTHORS   NAKAMURA T.
  TITLE     Stoichiometric studies on the action of laccase.
  JOURNAL   Biochim. Biophys. Acta. 30 (1958) 538-42.
  ORGANISM  Rhus vernicifera
REFERENCE   7
  AUTHORS   Peisach, J. and Levine, W.G.
  TITLE     A comparison of the enzymic activities of pig ceruloplasmin and Rhus
            vernicifera laccase.
  JOURNAL   J. Biol. Chem. 240 (1965) 2284-2289.
  ORGANISM  pig [GN:ssc], Rhus vernicifera
REFERENCE   8
  AUTHORS   Reinhammar, B. and Malmstrom, B.G.
  TITLE     "Blue" copper-containing oxidases.
  JOURNAL   In: Spiro, T.G. (Ed.), Copper Proteins, Copper Proteins, New York,
            1981, p. 109-149.
ORTHOLOGY   KO: K05909  
GENES       PIC: PICST_79365(FET3)
            AFM: AFUA_1G15670 AFUA_4G14490 AFUA_5G03790
            CNE: CNG01240
            UMA: UM00105.1 UM05861.1
            TTH: TTC1370
STRUCTURES  PDB: 1A65  1GW0  1GYC  1HFU  1KYA  1V10  2H5U  2HRG  2HRH  2IH8  
                 2IH9  
DBLINKS     IUBMB Enzyme Nomenclature: 1.10.3.2
            ExPASy - ENZYME nomenclature database: 1.10.3.2
            ExplorEnz - The Enzyme Database: 1.10.3.2
            ERGO genome analysis and discovery system: 1.10.3.2
            UM-BBD (Biocatalysis/Biodegradation Database): 1.10.3.2
            BRENDA, the Enzyme Database: 1.10.3.2
            CAS: 80498-15-3
///
ENTRY       EC 1.10.3.3                 Enzyme
NAME        L-ascorbate oxidase;
            ascorbase;
            ascorbic acid oxidase;
            ascorbate oxidase;
            ascorbic oxidase;
            ascorbate dehydrogenase;
            L-ascorbic acid oxidase;
            AAO;
            L-ascorbate:O2 oxidoreductase ;
            AA oxidase
CLASS       Oxidoreductases;
            Acting on diphenols and related substances as donors;
            With oxygen as acceptor
SYSNAME     L-ascorbate:oxygen oxidoreductase
REACTION    2 L-ascorbate + O2 = 2 dehydroascorbate + 2 H2O [RN:R00035]
ALL_REAC    R00035 > R00068
SUBSTRATE   L-ascorbate [CPD:C00072];
            O2 [CPD:C00007]
PRODUCT     dehydroascorbate [CPD:C00425];
            H2O [CPD:C00001]
COFACTOR    Copper [CPD:C00070]
COMMENT     A multicopper protein.
REFERENCE   1
  AUTHORS   Stark, G.R. and Dawson, C.R.
  TITLE     Ascorbic acid oxidase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 8, Academic Press, New York, 1963, p. 297-311.
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K00423  L-ascorbate oxidase
GENES       ATH: AT1G55570(SKS12) AT5G21100
            XFA: XF2677
            XFT: PD2039
            MAQ: Maqu_0126
            RSO: RS04807(RSp1530)
            BXE: Bxe_C1337
            BUR: Bcep18194_B2764
            BPM: BURPS1710b_A2009(copA)
            RET: RHE_CH02519
            RLE: RL2434(copA)
            BRA: BRADO1520
            BBT: BBta_6519
            NAR: Saro_2929
STRUCTURES  PDB: 1AOZ  1ASO  1ASP  1ASQ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.10.3.3
            ExPASy - ENZYME nomenclature database: 1.10.3.3
            ExplorEnz - The Enzyme Database: 1.10.3.3
            ERGO genome analysis and discovery system: 1.10.3.3
            BRENDA, the Enzyme Database: 1.10.3.3
            CAS: 9029-44-1
///
ENTRY       EC 1.10.3.4                 Enzyme
NAME        o-aminophenol oxidase;
            isophenoxazine synthase;
            o-aminophenol:O2 oxidoreductase;
            2-aminophenol:O2 oxidoreductase;
            GriF
CLASS       Oxidoreductases;
            Acting on diphenols and related substances as donors;
            With oxygen as acceptor
SYSNAME     2-aminophenol:oxygen oxidoreductase
REACTION    (1) (1a) 2 2-aminophenol + O2 = 2 6-iminocyclohexa-2,4-dienone + 2
            H2O [RN:R00074];
            (2) (1b) 2 6-iminocyclohexa-2,4-dienone + oxidant =
            2-aminophenoxazin-3-one + reduced oxidant (spontaneous)
ALL_REAC    R00074
SUBSTRATE   2-aminophenol [CPD:C01987];
            O2 [CPD:C00007];
            6-iminocyclohexa-2,4-dienone;
            oxidant
PRODUCT     6-iminocyclohexa-2,4-dienone;
            H2O [CPD:C00001];
            2-aminophenoxazin-3-one;
            reduced oxidant (spontaneous)
COFACTOR    FAD [CPD:C00016];
            Manganese [CPD:C00034];
            Copper [CPD:C00070];
            Flavoprotein [CPD:C06411]
COMMENT     A flavoprotein. While the enzyme from the plant Tecoma stans is
            activated by Mn2+ [1], that from the bacterium Streptomyces griseus
            (GriF) requires Cu2+ for maximal activity. Two molecules of the
            product 6-iminocyclohexa-2,4-dienone (i.e. 1,2-benzoquinone
            monoimine) spontaneously condense with oxidation to yield
            2-aminophenoxazin-3-one [4]. 3-Amino-4-hydroxybenzaldehyde, which
            has a -CHO group at the para-position with respect to the hydroxy
            group of 2-aminophenol, was found to be the best substrate for GriF
            [4].
REFERENCE   1
  AUTHORS   Nair, P.M. and Vaidynathan, C.S.
  TITLE     Isophenoxazine synthase.
  JOURNAL   Biochim. Biophys. Acta 81 (1964) 507-516.
  ORGANISM  Tecoma stans
REFERENCE   2  [PMID:14298835]
  AUTHORS   NAIR PM, VINING LC.
  TITLE     ESOPHENOXAZINE SYNTHASE APOENZYME FROM PYCNOPORUS COCCINEUS.
  JOURNAL   Biochim. Biophys. Acta. 96 (1965) 318-27.
  ORGANISM  Pycnoporus coccineus
REFERENCE   3  [PMID:4166439]
  AUTHORS   Subba Rao PV, Vaidyanathan CS.
  TITLE     Studies on the metabolism of o-aminophenol. Purification and
            properties of isophenoxazine synthase from Bauhenia monandra.
  JOURNAL   Arch. Biochem. Biophys. 118 (1967) 388-94.
  ORGANISM  Bauhenia monandra
REFERENCE   4  [PMID:16282322]
  AUTHORS   Suzuki H, Furusho Y, Higashi T, Ohnishi Y, Horinouchi S.
  TITLE     A novel o-aminophenol oxidase responsible for formation of the
            phenoxazinone chromophore of grixazone.
  JOURNAL   J. Biol. Chem. 281 (2006) 824-33.
  ORGANISM  Streptomyces griseus
PATHWAY     PATH: map00380  Tryptophan metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.10.3.4
            ExPASy - ENZYME nomenclature database: 1.10.3.4
            ExplorEnz - The Enzyme Database: 1.10.3.4
            ERGO genome analysis and discovery system: 1.10.3.4
            BRENDA, the Enzyme Database: 1.10.3.4
            CAS: 9013-85-8
///
ENTRY       EC 1.10.3.5                 Enzyme
NAME        3-hydroxyanthranilate oxidase;
            3-hydroxyanthranilic acid oxidase
CLASS       Oxidoreductases;
            Acting on diphenols and related substances as donors;
            With oxygen as acceptor
SYSNAME     3-hydroxyanthranilate:oxygen oxidoreductase
REACTION    3-hydroxyanthranilate + O2 =
            6-imino-5-oxocyclohexa-1,3-dienecarboxylate + H2O2 [RN:R02666]
ALL_REAC    R02666
SUBSTRATE   3-hydroxyanthranilate [CPD:C00632];
            O2 [CPD:C00007]
PRODUCT     6-imino-5-oxocyclohexa-1,3-dienecarboxylate [CPD:C04584];
            H2O2 [CPD:C00027]
REFERENCE   1  [PMID:14347936]
  AUTHORS   MORGAN LR Jr, WEIMORTS DM, AUBERT CC.
  TITLE     OXIDATION OF 3-HYDROXYANTHRANILIC ACID BY A SOLUBLE LIVER FRACTION
            FROM POIKILOTHERMIC VERTEBRATES.
  JOURNAL   Biochim. Biophys. Acta. 100 (1965) 393-402.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.10.3.5
            ExPASy - ENZYME nomenclature database: 1.10.3.5
            ExplorEnz - The Enzyme Database: 1.10.3.5
            ERGO genome analysis and discovery system: 1.10.3.5
            BRENDA, the Enzyme Database: 1.10.3.5
            CAS: 37256-53-4
///
ENTRY       EC 1.10.3.6                 Enzyme
NAME        rifamycin-B oxidase;
            rifamycin B oxidase
CLASS       Oxidoreductases;
            Acting on diphenols and related substances as donors;
            With oxygen as acceptor
SYSNAME     rifamycin-B:oxygen oxidoreductase
REACTION    rifamycin B + O2 = rifamycin O + H2O2 [RN:R03736]
ALL_REAC    R03736
SUBSTRATE   rifamycin B [CPD:C01848];
            O2 [CPD:C00007]
PRODUCT     rifamycin O [CPD:C01849];
            H2O2 [CPD:C00027]
COMMENT     Acts also on benzene-1,4-diol and, more slowly, on some other
            p-quinols. Not identical with EC 1.10.3.1 (catechol oxidase), EC
            1.10.3.2 (laccase), EC 1.10.3.4 (o-aminophenol oxidase) or EC
            1.10.3.5 (3-hydroxyanthranilate oxidase).
REFERENCE   1  [PMID:6825839]
  AUTHORS   Han MH, Seong BL, Son HJ, Mheen TI.
  TITLE     Rifamycin B oxidase from Monocillium spp., a new type of diphenol
            oxidase.
  JOURNAL   FEBS. Lett. 151 (1983) 36-40.
  ORGANISM  Monocillium spp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.10.3.6
            ExPASy - ENZYME nomenclature database: 1.10.3.6
            ExplorEnz - The Enzyme Database: 1.10.3.6
            ERGO genome analysis and discovery system: 1.10.3.6
            BRENDA, the Enzyme Database: 1.10.3.6
            CAS: 84932-52-5
///
ENTRY       EC 1.10.3.7       Obsolete  Enzyme
NAME        Transferred to 1.21.3.4
CLASS       Oxidoreductases;
            Acting on diphenols and related substances as donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now EC 1.21.3.4, sulochrin oxidase
            [(+)-bisdechlorogeodin-forming] (EC 1.10.3.7 created 1986, deleted
            2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.10.3.7
            ExPASy - ENZYME nomenclature database: 1.10.3.7
            ExplorEnz - The Enzyme Database: 1.10.3.7
            ERGO genome analysis and discovery system: 1.10.3.7
            BRENDA, the Enzyme Database: 1.10.3.7
///
ENTRY       EC 1.10.3.8       Obsolete  Enzyme
NAME        Transferred to 1.21.3.5
CLASS       Oxidoreductases;
            Acting on diphenols and related substances as donors;
            With oxygen as acceptor
COMMENT     Transferred entry: now EC 1.21.3.5, sulochrin oxidase
            [(-)-bisdechlorogeodin-forming] (EC 1.10.3.8 created 1986, deleted
            2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.10.3.8
            ExPASy - ENZYME nomenclature database: 1.10.3.8
            ExplorEnz - The Enzyme Database: 1.10.3.8
            ERGO genome analysis and discovery system: 1.10.3.8
            BRENDA, the Enzyme Database: 1.10.3.8
///
ENTRY       EC 1.10.99.1                Enzyme
NAME        plastoquinol---plastocyanin reductase;
            plastoquinol/plastocyanin oxidoreductase;
            cytochrome b6/f complex;
            cytochrome b6/ complex
CLASS       Oxidoreductases;
            Acting on diphenols and related substances as donors;
            With other acceptors
SYSNAME     plastoquinol:oxidized-plastocyanin oxidoreductase
REACTION    plastoquinol-1 + 2 oxidized plastocyanin = plastoquinone + 2 reduced
            plastocyanin [RN:R03817]
ALL_REAC    R03817
SUBSTRATE   plastoquinol-1 [CPD:C02185];
            oxidized plastocyanin [CPD:C03162]
PRODUCT     plastoquinone [CPD:C02061];
            reduced plastocyanin [CPD:C03025]
COMMENT     A cytochrome f,b6 complex separated from chloroplasts. Also acts,
            more slowly, on plastoquinol-9 and ubiquinols. Cytochrome c-552 can
            act instead of plastocyanin, but more slowly.
REFERENCE   1  [PMID:6269845]
  AUTHORS   Hurt E, Hauska G.
  TITLE     A cytochrome f/b6 complex of five polypeptides with
            plastoquinol-plastocyanin-oxidoreductase activity from spinach
            chloroplasts.
  JOURNAL   Eur. J. Biochem. 117 (1981) 591-5.
  ORGANISM  spinach
PATHWAY     PATH: map00195  Photosynthesis
ORTHOLOGY   KO: K02636  cytochrome b6-f complex iron-sulfur subunit
GENES       ATH: AT4G03280(PETC)
            OSA: 4343570
            CME: CMI281C CMO066C CMQ165C
            RHA: RHA1_ro00654
            SYN: sll1182(petC3) sll1316(petC) slr1185(petC2)
            SYW: SYNW1841(petC)
            SYC: syc0318_d(petC)
            SYF: Synpcc7942_1232
            SYG: sync_0549(petB) sync_2149(petC)
            SYR: SynRCC307_0704(petC)
            SYX: SynWH7803_1850(petC)
            CYA: CYA_1403(petC)
            CYB: CYB_1622(petC)
            TEL: tlr0959(petC)
            GVI: glr3038(petC)
            ANA: all0606(petC) all1512(petC) all2453(petC) all4511(petC)
            AVA: Ava_0385 Ava_3377 Ava_4538
            PMA: Pro0460(petC)
            PMM: PMM0462(petC)
            PMT: PMT1322(petC)
            PMN: PMN2A_1794
            PMI: PMT9312_0462
            PMB: A9601_03501(petD) A9601_05181(petC)
            PMC: P9515_03581(petD) P9515_05261(petC)
            PMF: P9303_06651(petC) P9303_21841(petD)
            PMG: P9301_03521(petD) P9301_04871(petC)
            PME: NATL1_04181(petD) NATL1_05171(petC)
            CTE: CT0302(petC)
            CCH: Cag_0394
            CPH: Cpha266_0429
            PVI: Cvib_1501
            PLT: Plut_1719
STRUCTURES  PDB: 1B3I  1Q90  2B3I  2D2C  2E74  2E75  2E76  
DBLINKS     IUBMB Enzyme Nomenclature: 1.10.99.1
            ExPASy - ENZYME nomenclature database: 1.10.99.1
            ExplorEnz - The Enzyme Database: 1.10.99.1
            ERGO genome analysis and discovery system: 1.10.99.1
            BRENDA, the Enzyme Database: 1.10.99.1
            CAS: 79079-13-3
///
ENTRY       EC 1.10.99.2                Enzyme
NAME        ribosyldihydronicotinamide dehydrogenase (quinone);
            NRH:quinone oxidoreductase 2;
            NQO2;
            NQO2;
            NAD(P)H:quinone oxidoreductase-2 (misleading);
            QR2;
            quinone reductase 2;
            N-ribosyldihydronicotinamide dehydrogenase (quinone);
            NAD(P)H:quinone oxidoreductase2 (misleading)
CLASS       Oxidoreductases;
            Acting on diphenols and related substances as donors;
            With other acceptors
SYSNAME     1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide:quinone
            oxidoreductase
REACTION    1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone =
            1-(beta-D-ribofuranosyl)nicotinamide + a hydroquinone [RN:R07361]
ALL_REAC    R07361
SUBSTRATE   1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide [CPD:C15497];
            quinone [CPD:C00472]
PRODUCT     1-(beta-D-ribofuranosyl)nicotinamide [CPD:C03150];
            hydroquinone [CPD:C00530]
COMMENT     A flavoprotein. Unlike EC 1.6.5.2, NAD(P)H dehydrogenase (quinone),
            this quinone reductase cannot use NADH or NADPH; instead it uses
            N-ribosyl- and N-alkyldihydronicotinamides. Polycyclic aromatic
            hydrocarbons, such as benz[a]anthracene, and the oestrogens
            17beta-estradiol and diethylstilbestrol are potent inhibitors, but
            dicoumarol is only a very weak inhibitor [2]. This enzyme can
            catalyse both 2-electron and 4-electron reductions, but one-electron
            acceptors, such as potassium ferricyanide, cannot be reduced [3].
REFERENCE   1  [PMID:14465018]
  AUTHORS   LIAO S, DULANEY JT, WILLIAMS-ASHMAN HG.
  TITLE     Purification and properties of a flavoprotein catalyzing the
            oxidation of reduced ribosyl nicotinamide.
  JOURNAL   J. Biol. Chem. 237 (1962) 2981-7.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:9050836]
  AUTHORS   Zhao Q, Yang XL, Holtzclaw WD, Talalay P.
  TITLE     Unexpected genetic and structural relationships of a long-forgotten
            flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase)
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 1669-74.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:9367528]
  AUTHORS   Wu K, Knox R, Sun XZ, Joseph P, Jaiswal AK, Zhang D, Deng PS, Chen
            S.
  TITLE     Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a
            dihydronicotinamide riboside dependent oxidoreductase.
  JOURNAL   Arch. Biochem. Biophys. 347 (1997) 221-8.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:8182056]
  AUTHORS   Jaiswal AK.
  TITLE     Human NAD(P)H:quinone oxidoreductase2. Gene structure, activity, and
            tissue-specific expression.
  JOURNAL   J. Biol. Chem. 269 (1994) 14502-8.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K08071  ribosyldihydronicotinamide dehydrogenase (quinone)
GENES       HSA: 4835(NQO2)
            PTR: 462395(NQO2)
            MMU: 18105(Nqo2)
            RNO: 291084(Nqo2)
            CFA: 606932(NQO2)
            GGA: 420886(NQO2)
            SPE: Spro_2460
            PAP: PSPA7_5708
            PPF: Pput_2044
            MSM: MSMEG_0284
DBLINKS     IUBMB Enzyme Nomenclature: 1.10.99.2
            ExPASy - ENZYME nomenclature database: 1.10.99.2
            ExplorEnz - The Enzyme Database: 1.10.99.2
            ERGO genome analysis and discovery system: 1.10.99.2
            BRENDA, the Enzyme Database: 1.10.99.2
///
ENTRY       EC 1.10.99.3                Enzyme
NAME        violaxanthin de-epoxidase;
            VDE
CLASS       Oxidoreductases;
            Acting on diphenols and related substances as donors;
            With other acceptors
SYSNAME     violaxanthin:ascorbate oxidoreductase
REACTION    (1) violaxanthin + ascorbate = antheraxanthin + dehydroascorbate +
            H2O [RN:R07178];
            (2) antheraxanthin + ascorbate = zeaxanthin + dehydroascorbate + H2O
            [RN:R07179]
ALL_REAC    R07178 R07179
SUBSTRATE   violaxanthin [CPD:C08614];
            ascorbate [CPD:C00072];
            antheraxanthin [CPD:C08579]
PRODUCT     antheraxanthin [CPD:C08579];
            dehydroascorbate [CPD:C00425];
            H2O [CPD:C00001];
            zeaxanthin [CPD:C06098]
COMMENT     Along with EC 1.14.13.90, zeaxanthin epoxidase, this enzyme forms
            part of the xanthophyll (or violaxanthin) cycle for controlling the
            concentration of zeaxanthin in chloroplasts. It is activated by a
            low pH of the thylakoid lumen (produced by high light intensity).
            Zeaxanthin induces the dissipation of excitation energy in the
            chlorophyll of the light-harvesting protein complex of photosystem
            II. In higher plants the enzyme reacts with all-trans-diepoxides,
            such as violaxanthin, and all-trans-monoepoxides, but in the alga
            Mantoniella squamata, only the diepoxides are good substrates.
REFERENCE   1  [PMID:102251]
  AUTHORS   Yamamoto HY, Higashi RM.
  TITLE     Violaxanthin de-epoxidase. Lipid composition and substrate
            specificity.
  JOURNAL   Arch. Biochem. Biophys. 190 (1978) 514-22.
  ORGANISM  Lactuca sativa [GN:elsa]
REFERENCE   2  [PMID:8742341]
  AUTHORS   Rockholm DC, Yamamoto HY.
  TITLE     Violaxanthin de-epoxidase.
  JOURNAL   Plant. Physiol. 110 (1996) 697-703.
  ORGANISM  Lactuca sativa [GN:elsa]
REFERENCE   3  [PMID:9624110]
  AUTHORS   Bugos RC, Hieber AD, Yamamoto HY.
  TITLE     Xanthophyll cycle enzymes are members of the lipocalin family, the
            first identified from plants.
  JOURNAL   J. Biol. Chem. 273 (1998) 15321-4.
  ORGANISM  Nicotiana tabacum, Arabidopsis thaliana [GN:ath]
REFERENCE   4  [PMID:10635115]
  AUTHORS   Kuwabara T, Hasegawa M, Kawano M, Takaichi S.
  TITLE     Characterization of violaxanthin de-epoxidase purified in the
            presence of Tween 20: effects of dithiothreitol and pepstatin A.
  JOURNAL   Plant. Cell. Physiol. 40 (1999) 1119-26.
  ORGANISM  spinach
REFERENCE   5  [PMID:12230579]
  AUTHORS   Latowski D, Kruk J, Burda K, Skrzynecka-Jaskier M, Kostecka-Gugala
            A, Strzalka K.
  TITLE     Kinetics of violaxanthin de-epoxidation by violaxanthin
            de-epoxidase, a xanthophyll cycle enzyme, is regulated by membrane
            fluidity in model lipid bilayers.
  JOURNAL   Eur. J. Biochem. 269 (2002) 4656-65.
  ORGANISM  Lactuca sativa [GN:elsa], spinach
REFERENCE   6  [PMID:12748855]
  AUTHORS   Goss R.
  TITLE     Substrate specificity of the violaxanthin de-epoxidase of the
            primitive green alga Mantoniella squamata (Prasinophyceae).
  JOURNAL   Planta. 217 (2003) 801-12.
  ORGANISM  Mantoniella squamata
REFERENCE   7  [PMID:15078086]
  AUTHORS   Latowski D, Akerlund HE, Strzalka K.
  TITLE     Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires
            lipid inverted hexagonal structures for its activity.
  JOURNAL   Biochemistry. 43 (2004) 4417-20.
  ORGANISM  Triticum aestivum [GN:etae]
PATHWAY     PATH: map00906  Carotenoid biosynthesis - General
ORTHOLOGY   KO: K09839  violaxanthin de-epoxidase
GENES       ATH: AT1G08550(NPQ1)
            OSA: 4335625
DBLINKS     IUBMB Enzyme Nomenclature: 1.10.99.3
            ExPASy - ENZYME nomenclature database: 1.10.99.3
            ExplorEnz - The Enzyme Database: 1.10.99.3
            ERGO genome analysis and discovery system: 1.10.99.3
            BRENDA, the Enzyme Database: 1.10.99.3
///
ENTRY       EC 1.11.1.1                 Enzyme
NAME        NADH peroxidase;
            DPNH peroxidase;
            NAD peroxidase;
            diphosphopyridine nucleotide peroxidase;
            NADH-peroxidase;
            nicotinamide adenine dinucleotide peroxidase;
            NADH2 peroxidase
CLASS       Oxidoreductases;
            Acting on a peroxide as acceptor;
            Peroxidases
SYSNAME     NADH:hydrogen-peroxide oxidoreductase
REACTION    NADH + H+ + H2O2 = NAD+ + 2 H2O [RN:R00090]
ALL_REAC    R00090
SUBSTRATE   NADH [CPD:C00004];
            H+ [CPD:C00080];
            H2O2 [CPD:C00027]
PRODUCT     NAD+ [CPD:C00003];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Ferricyanide, quinones, etc., can replace
            H2O2.
REFERENCE   1
  AUTHORS   Domagk, G.F. and Horecker, B.L.
  TITLE     Fructose and erythrose metabolism in Alcaligenes faecalis.
  JOURNAL   Arch. Biochem. Biophys. 109 (1965) 342-349.
  ORGANISM  Alcaligenes faecalis
REFERENCE   2
  AUTHORS   Mizushima, S. and Kitahara, K.
  TITLE     Purification and properties of DPNH peroxidase in Lactobacillus
            casei.
  JOURNAL   J. Gen. Appl. Microbiol. 8 (1962) 56-62.
  ORGANISM  Lactobacillus casei [GN:lca]
REFERENCE   3  [PMID:4285876]
  AUTHORS   Walker GA, Kilgour GL.
  TITLE     Pyridine nucleotide oxidizing enzymes of Lactobacillus casei. II.
            Oxidase and peroxidase.
  JOURNAL   Arch. Biochem. Biophys. 111 (1965) 534-9.
  ORGANISM  Lactobacillus casei [GN:lca]
ORTHOLOGY   KO: K05910  NADH peroxidase
GENES       RRU: Rru_A2309
            BCL: ABC1389
            SPZ: M5005_Spy_1378
            SPH: MGAS10270_Spy1496
            SPI: MGAS10750_Spy1489
            SPJ: MGAS2096_Spy1401
            SPK: MGAS9429_Spy1376
            SPA: M6_Spy1426
            SPB: M28_Spy1421
            LPL: lp_1445(npr1) lp_2544(npr2)
            LAC: LBA1401
            LSA: LSA0575(npr)
            LSL: LSL_0137
            LBR: LVIS_B09
            LCA: LSEI_0397
            EFA: EF1211(npr)
STRUCTURES  PDB: 1F8W  1JOA  1NHP  1NHQ  1NHR  1NHS  1NPX  2NPX  
DBLINKS     IUBMB Enzyme Nomenclature: 1.11.1.1
            ExPASy - ENZYME nomenclature database: 1.11.1.1
            ExplorEnz - The Enzyme Database: 1.11.1.1
            ERGO genome analysis and discovery system: 1.11.1.1
            BRENDA, the Enzyme Database: 1.11.1.1
            CAS: 9032-24-0
///
ENTRY       EC 1.11.1.2                 Enzyme
NAME        NADPH peroxidase;
            TPNH peroxidase;
            NADP peroxidase;
            nicotinamide adenine dinucleotide phosphate peroxidase;
            TPN peroxidase;
            triphosphopyridine nucleotide peroxidase;
            NADPH2 peroxidase
CLASS       Oxidoreductases;
            Acting on a peroxide as acceptor;
            Peroxidases
SYSNAME     NADPH:hydrogen-peroxide oxidoreductase
REACTION    NADPH + H+ + H2O2 = NADP+ + 2 H2O [RN:R00113]
ALL_REAC    R00113
SUBSTRATE   NADPH [CPD:C00005];
            H+ [CPD:C00080];
            H2O2 [CPD:C00027]
PRODUCT     NADP+ [CPD:C00006];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:14927602]
  AUTHORS   CONN EE, KRAEMER LM, LIU PN, VENNESLAND B.
  TITLE     The aerobic oxidation of reduced triphosphopyridine nucleotide by a
            wheat germ enzyme system.
  JOURNAL   J. Biol. Chem. 194 (1952) 143-51.
  ORGANISM  horseradish
DBLINKS     IUBMB Enzyme Nomenclature: 1.11.1.2
            ExPASy - ENZYME nomenclature database: 1.11.1.2
            ExplorEnz - The Enzyme Database: 1.11.1.2
            ERGO genome analysis and discovery system: 1.11.1.2
            BRENDA, the Enzyme Database: 1.11.1.2
            CAS: 9029-51-0
///
ENTRY       EC 1.11.1.3                 Enzyme
NAME        fatty-acid peroxidase;
            long chain fatty acid peroxidase
CLASS       Oxidoreductases;
            Acting on a peroxide as acceptor;
            Peroxidases
SYSNAME     hexadecanoate:hydrogen-peroxide oxidoreductase
REACTION    palmitate + 2 H2O2 = pentadecanal + CO2 + 3 H2O [RN:R01703]
ALL_REAC    R01703
SUBSTRATE   palmitate [CPD:C00249];
            H2O2 [CPD:C00027]
PRODUCT     pentadecanal [CPD:C01948];
            CO2 [CPD:C00011];
            H2O [CPD:C00001]
COMMENT     Acts on long-chain fatty acids from dodecanoic to octadecanoic acid.
REFERENCE   1  [PMID:14421733]
  AUTHORS   MARTIN RO, STUMPF PK.
  TITLE     Fat metabolism in higher plants. XII. alpha-Oxidation of long chain
            fatty acids.
  JOURNAL   J. Biol. Chem. 234 (1959) 2548-54.
  ORGANISM  peanut
DBLINKS     IUBMB Enzyme Nomenclature: 1.11.1.3
            ExPASy - ENZYME nomenclature database: 1.11.1.3
            ExplorEnz - The Enzyme Database: 1.11.1.3
            ERGO genome analysis and discovery system: 1.11.1.3
            BRENDA, the Enzyme Database: 1.11.1.3
            CAS: 9029-52-1
///
ENTRY       EC 1.11.1.4       Obsolete  Enzyme
NAME        Transferred to 1.13.11.11
CLASS       Oxidoreductases;
            Acting on a peroxide as acceptor;
            Peroxidases
COMMENT     Transferred entry: now EC 1.13.11.11 tryptophan 2,3-dioxygenase (EC
            1.11.1.4 created 1961, deleted 1964, reinstated 1965 as EC
            1.13.1.12, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.11.1.4
            ExPASy - ENZYME nomenclature database: 1.11.1.4
            ExplorEnz - The Enzyme Database: 1.11.1.4
            ERGO genome analysis and discovery system: 1.11.1.4
            BRENDA, the Enzyme Database: 1.11.1.4
///
ENTRY       EC 1.11.1.5                 Enzyme
NAME        cytochrome-c peroxidase;
            cytochrome peroxidase;
            cytochrome c-551 peroxidase;
            apocytochrome c peroxidase;
            mesocytochrome c peroxidase azide;
            mesocytochrome c peroxidase cyanide;
            mesocytochrome c peroxidase cyanate;
            cytochrome c-H2O oxidoreductase;
            cytochrome c peroxidase
CLASS       Oxidoreductases;
            Acting on a peroxide as acceptor;
            Peroxidases
SYSNAME     ferrocytochrome-c:hydrogen-peroxide oxidoreductase
REACTION    2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O [RN:R00017]
ALL_REAC    R00017
SUBSTRATE   ferrocytochrome c [CPD:C00126];
            H2O2 [CPD:C00027]
PRODUCT     ferricytochrome c [CPD:C00125];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A hemoprotein.
REFERENCE   1
  AUTHORS   Altschul, A.M., Abrams, R. and Hogness, T.R.
  TITLE     Cytochrome c peroxidase.
  JOURNAL   J. Biol. Chem. 136 (1940) 777-794.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:5487887]
  AUTHORS   Yamanaka T, Okunuki K.
  TITLE     Isolation of a cytochrome peroxidase from Thiobacillus novellus.
  JOURNAL   Biochim. Biophys. Acta. 220 (1970) 354-6.
  ORGANISM  Thiobacillus novellus
REFERENCE   3  [PMID:4318313]
  AUTHORS   Yonetani T.
  TITLE     Cytochrome c peroxidase.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 33 (1970) 309-35.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K00428  cytochrome c peroxidase
GENES       SCE: YKR066C(CCP1)
            PIC: PICST_67176(CCP2) PICST_85478
            CAL: CaO19_238(CaO19.238)
            CGR: CAGL0K08184g
            ANI: AN1630.2
            AFM: AFUA_4G09110
            AOR: AO090023000654
            CNE: CND02630
            UMA: UM02377.1
            TET: TTHERM_00133500
            ECO: b3518(yhjA)
            ECJ: JW3486(yhjA)
            ECE: Z4931(yhjA)
            ECS: ECs4398
            ECC: c4329(yhjA)
            ECI: UTI89_C4050(yhjA)
            ECV: APECO1_2930(yhjA)
            STY: STY3958(yhjA)
            STT: t3698(yhjA)
            SPT: SPA3670(yhjA)
            SEC: SC3738(yhjA)
            STM: STM3820
            YPE: YPO3342(yhjA)
            YPK: y0848
            YPM: YP_0345(mauG)
            YPA: YPA_2801
            YPN: YPN_0751
            YPP: YPDSF_3018
            YPS: YPTB0790(yhjA)
            YPI: YpsIP31758_3278
            SFL: SF3593(yhjA)
            SFX: S4174(yhjA)
            SFV: SFV_3990(yhjA)
            SSN: SSON_3568(yhjA)
            SBO: SBO_3517(yhjA)
            SPE: Spro_1968
            PMU: PM0939
            MSU: MS0223(mauG)
            APL: APL_1379(ccp)
            ASU: Asuc_2054
            XCV: XCV2146
            XOO: XOO3031
            XOM: XOO_2883(XOO2883)
            VCH: VC0089
            VCO: VC0395_A2426(yhjA)
            VVU: VV2_0949
            VVY: VVA1438
            VPA: VP1718 VPA1101
            VFI: VF2055
            PAE: PA4587(ccpR)
            PAU: PA14_60700(ccpR)
            PPU: PP_2943
            PPF: Pput_2744
            PFL: PFL_3326(ccpA) PFL_5183(ccpA)
            PFO: Pfl_4553
            PRW: PsycPRwf_2378
            SON: SO_2178(ccpA)
            SDN: Sden_0005
            SBL: Sbal_2533
            SBM: Shew185_2526
            SPC: Sputcn32_2287
            SSE: Ssed_1107 Ssed_2684
            SPL: Spea_1877
            SHE: Shewmr4_2216
            SHM: Shewmr7_2292
            SHN: Shewana3_2425
            SHW: Sputw3181_1721
            CPS: CPS_1343 CPS_1860
            PHA: PSHAa2702
            SDE: Sde_1590
            MAQ: Maqu_0372
            MCA: MCA0345
            NOC: Noc_0114 Noc_1263 Noc_2697
            AEH: Mlg_2854
            HCH: HCH_02475
            ABO: ABO_2374(ccpR)
            MMW: Mmwyl1_0409
            AHA: AHA_3403
            NGO: NGO1769
            CVI: CV_0300
            RME: Rmet_4808 Rmet_4968
            BMA: BMA0887 BMAA0610
            BUR: Bcep18194_A4546 Bcep18194_B1675
            BCN: Bcen_0920 Bcen_4022
            BCH: Bcen2424_1402 Bcen2424_4344
            BAM: Bamb_1279
            BPS: BPSL2017
            BPM: BURPS1710b_1805 BURPS1710b_A2342
            BPL: BURPS1106A_1649
            BPD: BURPS668_1628
            BTE: BTH_I2670 BTH_II1637
            RFR: Rfer_3124
            POL: Bpro_4821
            NEU: NE1315(ccp)
            NET: Neut_1249 Neut_1521
            NMU: Nmul_A0448
            EBA: ebA3202(cpx)
            AZO: azo1279 azo1831(mauG) azo2562(ccp)
            MFA: Mfla_0552
            HPY: HP1461
            HPA: HPAG1_1454
            HHE: HH1316(yhjA)
            HAC: Hac_0123(ccpA)
            WSU: WS1491
            TDN: Tmden_0214 Tmden_1585
            CJE: Cj0020c Cj0358
            CJR: CJE0020(ccpA-1) CJE0407(ccpA-2)
            CJJ: CJJ81176_0047(ccpA-1) CJJ81176_0382(ccpA-2)
            CJU: C8J_0019 C8J_0335
            CFF: CFF8240_1539 CFF8240_1734
            CCV: CCV52592_1483
            CHA: CHAB381_0370
            CCO: CCC13826_0119 CCC13826_1108
            ABU: Abu_1742 Abu_2140
            NIS: NIS_0141 NIS_0547 NIS_1135 NIS_1638
            SUN: SUN_0270 SUN_1234 SUN_1627
            GSU: GSU0466(ccpA-1) GSU2813(ccpA-2)
            GME: Gmet_3091
            GUR: Gura_1316
            LIP: LIC102(yhjA)
            BBA: Bd0904(ccpA)
            AFW: Anae109_2766
            MXA: MXAN_5562
            MLO: mlr5805
            RLE: pRL110284
            BJA: blr2696
            BRA: BRADO0674 BRADO1062
            BBT: BBta_6985 BBta_7510
            RPB: RPB_4384
            RPC: RPC_1205
            RPE: RPE_4145
            NWI: Nwi_0943
            SIL: SPO0330(ccpA)
            SIT: TM1040_3135 TM1040_3354
            RSP: RSP_2395
            RSH: Rsph17029_1058
            RSQ: Rsph17025_1377
            JAN: Jann_3672
            PDE: Pden_0893
            ZMO: ZMO1136(cytC)
            SWI: Swit_1193
            GOX: GOX1889
            ACR: Acry_2827
            RRU: Rru_A1789
            MAG: amb1222 amb2822
            MGM: Mmc1_1488 Mmc1_2527 Mmc1_2947
            SUS: Acid_6510
            STH: STH2047
            RBA: RB304 RB3109(mauG)
            LIL: LA0666
            LIC: LIC12927
            LBL: LBL_0731(mauG-1)
            AVA: Ava_B0145
            BTH: BT_1606
            BFR: BF2268
            BFS: BF2362(ccp)
            CHU: CHU_0523(ccpA) CHU_2275(yhjA) CHU_3118(yhjA)
            FJO: Fjoh_0766 Fjoh_2477 Fjoh_3340 Fjoh_5007
            FPS: FP0568 FP0579
            CCH: Cag_1187
            CPH: Cpha266_1353
            PLT: Plut_0811
            RRS: RoseRS_3631
            RCA: Rcas_0505
            AAE: aq_136(cpx)
            MAC: MA2908
            HMA: rrnAC1372(ccpA)
            NPH: NP4384A(cpx)
STRUCTURES  PDB: 1A2F  1A2G  1AA4  1AC4  1AC8  1AEB  1AED  1AEE  1AEF  1AEG  
                 1AEH  1AEJ  1AEK  1AEM  1AEN  1AEO  1AEQ  1AES  1AET  1AEU  
                 1AEV  1BEJ  1BEK  1BEM  1BEP  1BEQ  1BES  1BJ9  1BVA  1CCA  
                 1CCB  1CCC  1CCE  1CCG  1CCI  1CCJ  1CCK  1CCL  1CCP  1CMP  
                 1CMQ  1CMT  1CMU  1CPD  1CPE  1CPF  1CPG  1CYF  1DCC  1DJ1  
                 1DJ5  1DS4  1DSE  1DSG  1DSO  1DSP  1EB7  1EBE  1JCI  1JDR  
                 1KOK  1KRJ  1KXM  1KXN  1MK8  1MKQ  1MKR  1ML2  1NML  1RYC  
                 1RZ5  1RZ6  1S6V  1S73  1SBM  1SDQ  1SOG  1STQ  1U74  1U75  
                 1Z53  1ZBY  1ZBZ  1ZZH  2ANZ  2AQD  2AS1  2AS2  2AS3  2AS4  
                 2AS6  2B0Z  2B10  2B11  2B12  2BCN  2C1U  2C1V  2CCP  2CEP  
                 2CYP  2EUN  2EUO  2EUP  2EUQ  2EUR  2EUS  2EUT  2EUU  2GB8  
                 2IA8  2ICV  3CCP  3CCX  4CCP  4CCX  5CCP  6CCP  7CCP  
DBLINKS     IUBMB Enzyme Nomenclature: 1.11.1.5
            ExPASy - ENZYME nomenclature database: 1.11.1.5
            ExplorEnz - The Enzyme Database: 1.11.1.5
            ERGO genome analysis and discovery system: 1.11.1.5
            BRENDA, the Enzyme Database: 1.11.1.5
            CAS: 9029-53-2
///
ENTRY       EC 1.11.1.6                 Enzyme
NAME        catalase;
            equilase;
            caperase;
            optidase;
            catalase-peroxidase;
            CAT
CLASS       Oxidoreductases;
            Acting on a peroxide as acceptor;
            Peroxidases
SYSNAME     hydrogen-peroxide:hydrogen-peroxide oxidoreductase
REACTION    2 H2O2 = O2 + 2 H2O [RN:R00009]
ALL_REAC    R00009;
            (other) R00602 R02670
SUBSTRATE   H2O2 [CPD:C00027]
PRODUCT     O2 [CPD:C00007];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032];
            Manganese [CPD:C00034]
COMMENT     A hemoprotein. This enzyme can also act as a peroxidase (EC 1.11.1.7
            peroxidase) for which several organic substances, especially
            ethanol, can act as a hydrogen donor. A manganese protein containing
            MnIII in the resting state, which also belongs here, is often called
            pseudocatalase. Enzymes from some microorganisms, such as
            Penicillium simplicissimum, which exhibit both catalase and
            peroxidase activity, have sometimes been referred to as
            catalase-peroxidase.
REFERENCE   1
  AUTHORS   Herbert, D. and Pinsent, J.
  TITLE     Crystalline bacterial catalase.
  JOURNAL   Biochem. J. 43 (1948) 193-202.
  ORGANISM  Micrococcus lysodeikticus
REFERENCE   2
  AUTHORS   Herbert, D. and Pinsent, J.
  TITLE     Crystalline human erythrocyte catalase.
  JOURNAL   Biochem. J. 43 (1948) 203-205.
  ORGANISM  human [GN:hsa]
REFERENCE   3
  AUTHORS   Keilin, D. and Hartree, E.F.
  TITLE     Coupled oxidation of alcohol.
  JOURNAL   Proc. R. Soc. Lond. B Biol. Sci. 119 (1936) 141-159.
REFERENCE   4  [PMID:6853475]
  AUTHORS   Kono Y, Fridovich I.
  TITLE     Isolation and characterization of the pseudocatalase of
            Lactobacillus plantarum.
  JOURNAL   J. Biol. Chem. 258 (1983) 6015-9.
  ORGANISM  Lactobacillus plantarum [GN:lpl]
REFERENCE   5
  AUTHORS   Nicholls, P. and Schonbaum, G.R.
  TITLE     Catalases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 8, Academic Press, New York, 1963, p. 147-225.
REFERENCE   6
  AUTHORS   Sumner, J.B. and Dounce, A.L.
  TITLE     Crystalline catalase.
  JOURNAL   J. Biol. Chem. 121 (1937) 417-424.
  ORGANISM  cow [GN:bta]
REFERENCE   7  [PMID:8631329]
  AUTHORS   Fraaije MW, Roubroeks HP, Hagen WR, Van Berkel WJ.
  TITLE     Purification and characterization of an intracellular
            catalase-peroxidase from Penicillium simplicissimum.
  JOURNAL   Eur. J. Biochem. 235 (1996) 192-8.
  ORGANISM  Penicillium simplicissimum
PATHWAY     PATH: map00380  Tryptophan metabolism
            PATH: map00680  Methane metabolism
            PATH: map05030  Amyotrophic lateral sclerosis (ALS)
ORTHOLOGY   KO: K00429  catalase
            KO: K03781  catalase
            KO: K03782  catalase/peroxidase
GENES       HSA: 847(CAT)
            MMU: 12359(Cat)
            RNO: 24248(Cat)
            CFA: 403474(CAT)
            SSC: 397568(CAT)
            GGA: 423600(RCJMB04_1j22) 769804(CAT)
            XLA: 380236(cat) 495840(LOC495840)
            XTR: 496897(cat)
            DRE: 30068(cat)
            SPU: 548621(LOC548621)
            DME: Dmel_CG6871(Cat) Dmel_CG9314
            CEL: Y54G11A.6(catalase)
            ATH: AT1G20620(CAT3) AT1G20630(CAT1)
            OSA: 4328073 4331509 4342124
            CME: CMI050C
            SCE: YDR256C(CTA1) YGR088W(CTT1)
            AGO: AGOS_AGL256W
            PIC: PICST_40324(CAT1)
            CAL: CaO19_6229(CaO19.6229)
            CGR: CAGL0K10868g
            SPO: SPCC757.07c
            ANI: AN5918.2 AN7388.2 AN8553.2 AN8637.2
            AFM: AFUA_2G00200 AFUA_2G18030 AFUA_3G02270 AFUA_6G03890
                 AFUA_8G01670
            AOR: AO090003000380 AO090010000722 AO090011000540 AO090020000389
                 AO090113000153 AO090701000158
            ANG: An01g01820(catR)
            CNE: CNH03740 CNL03740 CNL06020 CNL06340
            UMA: UM03399.1
            DDI: DDB_0185123(catA) DDB_0191496(catB)
            TET: TTHERM_01146030
            ECO: b1732(katE) b3942(katG)
            ECJ: JW1721(katE) JW3914(katG)
            ECE: Z2761(katE) Z5497(katG)
            ECS: ECs2438 ECs4871
            ECC: c2131(katE) c4900(katG)
            ECI: UTI89_C1925(katE) UTI89_C4532(katG)
            ECP: ECP_1678 ECP_4156
            ECV: APECO1_2524(katG) APECO1_801(katE)
            ECW: EcE24377A_1953(katE) EcE24377A_4482(katG)
            ECX: EcHS_A1813(katE) EcHS_A4176(katG)
            STY: STY1793(katE) STY3760(katG)
            STT: t1198(katE) t3510(katG)
            SPT: SPA1526(katE) SPA3952(katG)
            SEC: SC1339(katE) SC3998(katG)
            STM: STM1318(katE) STM4106(katG)
            YPE: YPO1207(katA) YPO3319(katY)
            YPK: y0870(katG) y2981(katE)
            YPM: YP_0367(katG) YP_0931(katA)
            YPA: YPA_0921 YPA_2825
            YPN: YPN_0774 YPN_2770
            YPP: YPDSF_2486 YPDSF_3041
            YPS: YPTB0811(katY) YPTB1246(katA)
            YPI: YpsIP31758_2776(katA) YpsIP31758_3254(katG)
            SFL: SF1496(katE) SF4020(katG)
            SFX: S1613(katE) S3727(katG)
            SFV: SFV_1488(katE) SFV_4012(katG)
            SSN: SSON_1426(katE) SSON_4116(katG)
            SBO: SBO_3962(katG)
            ECA: ECA1216(katA) ECA1909(katB)
            PLU: plu3068(katE)
            SGL: SG2101
            ENT: Ent638_1712 Ent638_3129 Ent638_4032
            SPE: Spro_0377 Spro_3278
            HIN: HI0928(hktE)
            HIT: NTHI1099(hktE)
            PMU: PM0032(hktE)
            APL: APL_0988(hktE)
            ASU: Asuc_0654
            XFA: XF2232
            XFT: PD1278(cpeB)
            XCC: XCC1109(katE) XCC1205(katG) XCC3905(srpA) XCC3949(catB)
            XCB: XC_3037 XC_3139 XC_3993 XC_4037
            XCV: XCV1240(katE) XCV1350(katG) XCV4083(srpA) XCV4122(catB)
            XAC: XAC1211(katE) XAC1301(katG) XAC3990(srpA) XAC4029(catB)
                 XAC4030(catB)
            XOO: XOO0417(catB) XOO0447(srpA) XOO3423(katE)
            XOM: XOO_0379(XOO0379) XOO_0410(XOO0410) XOO_3220(XOO3220)
            VCH: VC1560 VC1585
            VCO: VC0395_A1166(perA) VC0395_A1188(katB)
            VVU: VV1_2755 VV2_1473
            VVY: VV1506 VVA0294
            VPA: VPA0305 VPA0453 VPA0768 VPA1418
            VFI: VFA0009
            PPR: PBPRB0286
            PAE: PA2147(katE) PA4236(katA) PA4613(katB)
            PAU: PA14_36810(katE) PA14_61040(katB)
            PAP: PSPA7_5254
            PPU: PP_0115(katE) PP_0481(katA) PP_2887 PP_3668
            PPF: Pput_0132 Pput_0514
            PST: PSPTO_3582(katB) PSPTO_4530(katG) PSPTO_5263(katE)
            PSB: Psyr_0280 Psyr_3353 Psyr_4208 Psyr_4522
            PSP: PSPPH_0267(katE) PSPPH_3274(katB) PSPPH_4229(katG)
                 PSPPH_4565(katA)
            PFL: PFL_0074(katE) PFL_2690(katG) PFL_3946 PFL_5358(katB)
                 PFL_5556(katA)
            PFO: Pfl_0064 Pfl_2201 Pfl_2262 Pfl_3665 Pfl_4886 Pfl_5053
            PEN: PSEEN0517(katA) PSEEN2069 PSEEN2372(katG) PSEEN2810(katB)
            PMY: Pmen_2273
            PAR: Psyc_0570(katE)
            PCR: Pcryo_0560 Pcryo_1999
            PRW: PsycPRwf_0656 PsycPRwf_1836
            ACI: ACIAD0451(katA)
            ACB: A1S_1351 A1S_3382
            SON: SO_0725(katG-1) SO_1070(katB) SO_4405(katG-2)
            SDN: Sden_1384
            SFR: Sfri_0563 Sfri_1917 Sfri_3122
            SAZ: Sama_0745 Sama_2941 Sama_3270
            SBL: Sbal_0875 Sbal_0894
            SBM: Shew185_0250 Shew185_3468
            SLO: Shew_0709 Shew_3190
            SPC: Sputcn32_0415 Sputcn32_0590
            SSE: Ssed_3251 Ssed_3940
            SPL: Spea_0125 Spea_0638
            SHE: Shewmr4_0311 Shewmr4_3029 Shewmr4_3379
            SHM: Shewmr7_0574 Shewmr7_0945 Shewmr7_3713
            SHN: Shewana3_0306 Shewana3_0908 Shewana3_2683 Shewana3_3549
            SHW: Sputw3181_0269 Sputw3181_3582
            ILO: IL0108(katG) IL1414 IL2052(katE)
            CPS: CPS_1344(katG) CPS_2441
            PHA: PSHAa1737 PSHAb0205(katB)
            PAT: Patl_0481 Patl_0766 Patl_1107 Patl_1975
            SDE: Sde_0830 Sde_3888
            PIN: Ping_2142
            MAQ: Maqu_1056
            CBU: CBU_0281(katE)
            CBD: COXBU7E912_1812
            LPN: lpg0194 lpg2389
            LPF: lpl0250(katG) lpl2313(katB)
            LPP: lpp0252(katG) lpp2454(katB)
            FTU: FTT0721c(katG)
            FTF: FTF0721c(katG)
            FTW: FTW_1518(katG)
            FTL: FTL_1504
            FTH: FTH_1458(katG)
            FTA: FTA_1588(katG)
            FTN: FTN_0633(katG)
            NOC: Noc_1165
            AEH: Mlg_1522
            HHA: Hhal_0547
            HCH: HCH_03207(katG)
            CSA: Csal_0159 Csal_0803 Csal_1100
            ABO: ABO_1845(katA)
            AHA: AHA_3994
            NME: NMB0216
            NMA: NMA0050(katA)
            NMC: NMC0211(katA)
            NGO: NGO1767(katA)
            CVI: CV_3549(katE)
            RSO: RSc0775(katGb) RSc0776(katGa) RSp1581(katE)
            REU: Reut_A1635 Reut_A1741 Reut_B4409
            REH: H16_A2777(katG) H16_A3109(katE1) H16_B1428(katE2)
            RME: Rmet_5371 Rmet_5599
            BMA: BMA2391(katG) BMAA1223(katB)
            BMV: BMASAVP1_0190(katB) BMASAVP1_A0308(katG)
            BML: BMA10299_0466 BMA10299_A1169(katG)
            BMN: BMA10247_2578(katG) BMA10247_A1109
            BXE: Bxe_A0772 Bxe_A3986 Bxe_B1215 Bxe_B1668
            BVI: Bcep1808_0687 Bcep1808_5181 Bcep1808_5214 Bcep1808_5733
                 Bcep1808_5870
            BUR: Bcep18194_A3196 Bcep18194_A3814 Bcep18194_B2194
                 Bcep18194_C7513
            BCN: Bcen_0061 Bcen_0242 Bcen_1348 Bcen_1578 Bcen_3169 Bcen_4468
                 Bcen_4987
            BCH: Bcen2424_0010 Bcen2424_0726 Bcen2424_3173 Bcen2424_3898
                 Bcen2424_5199 Bcen2424_6253 Bcen2424_6481
            BAM: Bamb_0007 Bamb_0616 Bamb_5612 Bamb_5842
            BPS: BPSL0071 BPSL2865(katG) BPSS0993(katB) BPSS2214(katE)
            BPM: BURPS1710b_0295 BURPS1710b_3366(katG) BURPS1710b_A1340(katE)
                 BURPS1710b_A1348 BURPS1710b_A2604(katB)
            BPL: BURPS1106A_0085 BURPS1106A_3356(katG) BURPS1106A_A1374(katB)
                 BURPS1106A_A2991
            BPD: BURPS668_0085 BURPS668_3322(katG) BURPS668_A1461(katB)
                 BURPS668_A3115
            BTE: BTH_I0072 BTH_I1282(katG)
            PNU: Pnuc_2044
            BPE: BP3852(katA)
            BPA: BPP4406(katA)
            BBR: BB4994(katA)
            POL: Bpro_0678 Bpro_2453
            PNA: Pnap_1830 Pnap_1993 Pnap_2662
            AAV: Aave_3132 Aave_3137 Aave_3991
            AJS: Ajs_1958 Ajs_3310
            MPT: Mpe_A1580 Mpe_A3740
            HAR: HEAR1200(katA)
            MMS: mma_1554(katG) mma_2184(katE)
            NEU: NE1812 NE1813 NE1886(katA)
            NET: Neut_1969
            NMU: Nmul_A1515
            EBA: ebA2102(katA)
            AZO: azo1675 azo2989(katG) azo3768
            DAR: Daro_0523 Daro_3836
            TBD: Tbd_2311
            MFA: Mfla_1436 Mfla_2377 Mfla_2572
            HPY: HP0875(kata)
            HPJ: jhp0809(katA)
            HPA: HPAG1_0461 HPAG1_0858
            HHE: HH0043(katA)
            HAC: Hac_1240(katA)
            TDN: Tmden_1323
            CJE: Cj1385(katA)
            CJR: CJE1576(katA)
            CJJ: CJJ81176_1387(katA)
            CJU: C8J_1303(katA)
            CJD: JJD26997_0265(katA)
            CFF: CFF8240_1057
            ABU: Abu_1548(katG)
            SUN: SUN_0439
            GSU: GSU2100(katG)
            PCA: Pcar_1175
            PPD: Ppro_1387 Ppro_1932
            DVU: DVUA0091(katA)
            DVL: Dvul_3018
            LIP: LI0842(katE)
            BBA: Bd0798(catA) Bd1154(katA)
            DPS: DP3003
            AFW: Anae109_3162
            MXA: MXAN_4389(katB) MXAN_6188(katE)
            SAT: SYN_02396
            SFU: Sfum_1721
            MLO: mlr2101 mlr6940
            MES: Meso_0626
            SME: SMa2379 SMb20007(catC) SMc00819(katA)
            SMD: Smed_0383 Smed_3979 Smed_4123 Smed_6390
            ATU: Atu4642(katA) Atu5491(catE)
            ATC: AGR_L_481 AGR_pAT_722
            RET: RHE_PF00004(katG)
            RLE: RL2024(katE) pRL120362(katG)
            BME: BMEII0893
            BMF: BAB2_0848
            BMS: BRA0355(katA)
            BMB: BruAb2_0827(katA)
            BOV: BOV_A0322(katA)
            OAN: Oant_3054 Oant_4790
            BJA: bll0292 blr0778
            BRA: BRADO1380 BRADO1666(katG) BRADO2172(katN)
            BBT: BBta_2489(katN) BBta_6389(katG) BBta_6719
            RPA: RPA0429(katG) RPA3310(katE)
            RPB: RPB_0610 RPB_0721
            RPC: RPC_0361 RPC_3625
            RPD: RPD_0223 RPD_0617
            RPE: RPE_0253 RPE_3645
            NWI: Nwi_0030
            NHA: Nham_0037 Nham_0804 Nham_0843 Nham_0854
            XAU: Xaut_2321
            CCR: CC_3043
            SIL: SPOA0061(katG)
            SIT: TM1040_2791
            RSP: RSP_2380(catC) RSP_2779(catA)
            RSH: Rsph17029_1040 Rsph17029_1421
            RSQ: Rsph17025_0606 Rsph17025_1896 Rsph17025_3305
            JAN: Jann_1586
            RDE: RD1_2195(katG)
            PDE: Pden_2497 Pden_4611
            MMR: Mmar10_2686
            HNE: HNE_2115(katG) HNE_2467(katE)
            ZMO: ZMO0918(cat)
            NAR: Saro_2909
            SAL: Sala_2146
            SWI: Swit_0269 Swit_3730 Swit_5248
            ELI: ELI_10465
            GOX: GOX1138
            GBE: GbCGDNIH1_1598 GbCGDNIH1_1615 GbCGDNIH1_1677 GbCGDNIH1_1969
            ACR: Acry_1147
            RRU: Rru_A1356 Rru_A2489
            ABA: Acid345_1356 Acid345_1673
            SUS: Acid_1112 Acid_6914
            BSU: BG10849(katA) BG11102(katB) BG11945(katX)
            BHA: BH0906 BH1306(katX) BH1980(katB)
            BAN: BA0843 BA1159(katB) BA3030 BA3164
            BAR: GBAA0843 GBAA1159(katB) GBAA3030 GBAA3164
            BAA: BA_1426 BA_1704 BA_3539
            BAT: BAS0803 BAS1076 BAS2816 BAS2940
            BCE: BC0863 BC1155 BC3008
            BCA: BCE_1261(katB) BCE_3059
            BCZ: BCZK0747(katB) BCZK1055(katB) BCZK2747(katX) BCZK2865(kat)
            BCY: Bcer98_0874
            BTK: BT9727_0752(katB) BT9727_1057(katB) BT9727_2764(katX)
                 BT9727_2914(katA)
            BTL: BALH_1019 BALH_2710
            BLI: BL00939(katX) BL00951(katA) BL01943(katB) BL01944
            BLD: BLi04111(katX) BLi04113(katA) BLi04196(katE1) BLi04197(katE2)
            BCL: ABC1186 ABC1283 ABC2074 ABC3415 ABC3627 ABC3969(katX)
            BAY: RBAM_009090(katA) RBAM_035940(katX) RBAM_036170(katE)
            BPU: BPUM_0892(katX2) BPUM_3712(katX1)
            OIH: OB0435 OB0633 OB1666 OB1667 OB2659(katB) OB2782 OB3262
            GKA: GK1710 GK3036
            SAU: SA1170(katA)
            SAV: SAV1334(katA)
            SAM: MW1221(katA)
            SAR: SAR1344
            SAS: SAS1274
            SAC: SACOL1368(kataA)
            SAB: SAB1192
            SAA: SAUSA300_1232
            SAO: SAOUHSC_01327
            SAJ: SaurJH9_1395
            SAH: SaurJH1_1422
            SEP: SE1016
            SER: SERP0903(katA)
            SHA: SH1573(katA)
            SSP: SSP1432
            LMO: lmo2785(kat)
            LMF: LMOf2365_2776(kaT)
            LIN: lin2920(kat)
            LWE: lwe2731(katB)
            LPL: lp_3578(kat)
            LSA: LSA0171(katA)
            LBR: LVIS_0906
            EFA: EF1597(katA)
            STH: STH2416
            CBE: Cbei_4834
            CKL: CKL_0487
            AMT: Amet_0511 Amet_3282 Amet_3934
            DSY: DSY1012 DSY3709 DSY4294
            MTA: Moth_1016
            MTU: Rv1908c(katG)
            MTC: MT1959(katG)
            MBO: Mb1943c(katG)
            MBB: BCG_1947c(katG)
            MPA: MAP1668c(katG) MAP1725c MAP3236(catB) MAP3682
            MAV: MAV_2753(katG) MAV_3520 MAV_4069(katE) MAV_4926(katA)
                 MAV_4927(katA)
            MSM: MSMEG_3461(katG) MSMEG_3486(katA) MSMEG_3708 MSMEG_3729(katG)
                 MSMEG_6232(katA) MSMEG_6384(katG)
            MUL: MUL_2190(katG)
            MVA: Mvan_2984 Mvan_3201 Mvan_3208 Mvan_5493
            MGI: Mflv_1308 Mflv_3446 Mflv_3451
            MMC: Mmcs_2682 Mmcs_5060
            MKM: Mkms_2727 Mkms_5148
            MJL: Mjls_2713 Mjls_5439
            CGL: NCgl0251(cgl0255)
            CGB: cg0310(katA)
            CEF: CE0072 CE0224
            CDI: DIP0281(cat)
            CJK: jk1994(katA)
            NFA: nfa27070(katB) nfa29500(katG) nfa55390(katC)
            RHA: RHA1_ro00439(katA) RHA1_ro00603 RHA1_ro03419 RHA1_ro04309
                 RHA1_ro05275(katG) RHA1_ro05836 RHA1_ro05938 RHA1_ro08262
            SCO: SCO0379(katA) SCO0560(cpeB) SCO0666(catB) SCO6204(SC2G5.25c)
                 SCO7590(katA2)
            SMA: SAV2026(katA3) SAV3052(katA1) SAV3224(katA2) SAV348(katB)
            LXX: Lxx02780(katA)
            ART: Arth_1094 Arth_3078
            AAU: AAur_0634 AAur_1864 AAur_3059
            PAC: PPA0097
            NCA: Noca_0875
            TFU: Tfu_0886 Tfu_1649
            FRA: Francci3_1918 Francci3_2949
            FAL: FRAAL3167(katA) FRAAL3889(katB)
            ACE: Acel_2094
            KRA: Krad_0815 Krad_0865
            SEN: SACE_0302(katA) SACE_3046 SACE_3861(katE) SACE_4668(katG)
            STP: Strop_2054
            RXY: Rxyl_0681
            RBA: RB3010(perA) RB4376(katA)
            LIL: LA1859(catA)
            LIC: LIC12032(katE)
            LBJ: LBJ_1598(katE)
            LBL: LBL_1816(katE)
            SYN: sll1987(cpx)
            SYC: syc2431_d(cpx)
            SYF: Synpcc7942_1656 Synpcc7942_B2620
            SYD: Syncc9605_0181
            SYR: SynRCC307_1434(katG)
            SYX: SynWH7803_0792(katG)
            GVI: gll2771
            AVA: Ava_3821
            TER: Tery_1759
            BTH: BT_1971
            BFR: BF1245
            BFS: BF1195(katA)
            SRU: SRU_2405(katG)
            CHU: CHU_2836(katE)
            GFO: GFO_0850(cpeB) GFO_2653(kat)
            FJO: Fjoh_3140 Fjoh_3897
            FPS: FP1730(catG)
            CCH: Cag_0386
            CPH: Cpha266_0755
            DRA: DR_1998 DR_A0259
            DGE: Dgeo_2728
            TTH: TTC1872
            TTJ: TTHA0122
            MAC: MA0972
            MBA: Mbar_A0814
            MMA: MM_1950 MM_2557
            MBU: Mbur_0523
            MHU: Mhun_2433
            MEM: Memar_0875
            MBN: Mboo_0959
            AFU: AF2233(perA)
            HAL: VNG6294G(perA)
            HMA: rrnAC1171(katG2) rrnAC2018(katG1)
            NPH: NP2708A(perA)
            RCI: RCIX619(katE)
STRUCTURES  PDB: 1A4E  1CF9  1DGB  1DGF  1DGG  1DGH  1E93  1F4J  1GG9  1GGE  
                 1GGF  1GGH  1GGJ  1GGK  1GWE  1GWF  1GWH  1H6N  1H7K  1HBZ  
                 1IPH  1ITK  1JKU  1JKV  1M7S  1M85  1MQF  1MWV  1NM0  1O9I  
                 1P7Y  1P7Z  1P81  1QF7  1QQW  1QWL  1QWM  1QWS  1SI8  1SJ2  
                 1SY7  1TGU  1TH2  1TH3  1TH4  1U2J  1U2K  1U2L  1UB2  1X7U  
                 1YE9  2A9E  2B2O  2B2Q  2B2R  2B2S  2CAG  2CAH  2CCA  2CWL  
                 2FXG  2FXH  2FXJ  2IQF  2ISA  2IUF  2J2M  2V8T  2V8U  4BLC  
                 4CAT  7CAT  8CAT  
DBLINKS     IUBMB Enzyme Nomenclature: 1.11.1.6
            ExPASy - ENZYME nomenclature database: 1.11.1.6
            ExplorEnz - The Enzyme Database: 1.11.1.6
            ERGO genome analysis and discovery system: 1.11.1.6
            UM-BBD (Biocatalysis/Biodegradation Database): 1.11.1.6
            BRENDA, the Enzyme Database: 1.11.1.6
            CAS: 9001-05-2
///
ENTRY       EC 1.11.1.7                 Enzyme
NAME        peroxidase;
            myeloperoxidase;
            lactoperoxidase;
            verdoperoxidase;
            guaiacol peroxidase;
            thiocyanate peroxidase;
            eosinophil peroxidase;
            Japanese radish peroxidase;
            horseradish peroxidase (HRP);
            extensin peroxidase;
            heme peroxidase;
            MPO;
            oxyperoxidase;
            protoheme peroxidase;
            pyrocatechol peroxidase;
            scopoletin peroxidase
CLASS       Oxidoreductases;
            Acting on a peroxide as acceptor;
            Peroxidases
SYSNAME     donor:hydrogen-peroxide oxidoreductase
REACTION    donor + H2O2 = oxidized donor + 2 H2O [RN:R03532]
ALL_REAC    R03532 > R00602;
            (other) R00698 R02596 R03919 R04007 R07443
SUBSTRATE   donor [CPD:C01351];
            H2O2 [CPD:C00027]
PRODUCT     oxidized donor [CPD:C02177];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A hemoprotein.
REFERENCE   1  [PMID:13172193]
  AUTHORS   KENTEN RH, MANN PJ.
  TITLE     A simple method for the preparation of horseradish peroxidase.
  JOURNAL   Biochem. J. 57 (1954) 347-8.
  ORGANISM  horseradish
REFERENCE   2  [PMID:13475358]
  AUTHORS   MORRISON M, HAMILTON HB, STOTZ E.
  TITLE     The isolation and purification of lactoperoxidase by ion exchange
            chromatography.
  JOURNAL   J. Biol. Chem. 228 (1957) 767-76.
  ORGANISM  cow [GN:bta]
REFERENCE   3
  AUTHORS   Paul, K.G.
  TITLE     Peroxidases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 8, Academic Press, New York, 1963, p. 227-274.
REFERENCE   4
  AUTHORS   Tagawa, K., Shin, M. and Okunuki, K.
  TITLE     Peroxidases from wheat germ.
  JOURNAL   Nature (Lond.) 183 (1959) 111.
  ORGANISM  Triticum aestivum [GN:etae]
REFERENCE   5
  AUTHORS   Theorell, H.
  TITLE     Preparation and properties of crystalline horseradish peroxidase.
  JOURNAL   Ark. Kemi Mineral. Geol. 16A (1943) 11pp.
PATHWAY     PATH: map00360  Phenylalanine metabolism
            PATH: map00680  Methane metabolism
            PATH: map00940  Phenylpropanoid biosynthesis
ORTHOLOGY   KO: K00430  peroxidase
GENES       HSA: 4025(LPO) 4353(MPO) 7173(TPO) 8288(EPX) 9588(PRDX6)
            PTR: 468420(EPX) 469589(PRDX6)
            MMU: 11758(Prdx6) 13861(Epx) 17523(Mpo) 320769(Prdx6-rs1)
                 76113(Lpo)
            RNO: 94167(Prdx6)
            CFA: 480069(PRDX6) 491109(EPX) 491111(LPO) 609986(MPO)
            BTA: 280844(LPO) 282438(AOP2)
            SSC: 399538(PRDX6)
            GGA: 417467(MPO) 429062(RCJMB04_18k11) 776120(TPO)
            DME: Dmel_CG10211 Dmel_CG11765(Prx2540-2) Dmel_CG12002(Pxn)
                 Dmel_CG12199(kek5) Dmel_CG12405(Prx2540-1)
                 Dmel_CG1274(Jafrac2) Dmel_CG1804(kek6) Dmel_CG2019(disp)
                 Dmel_CG3083(Prx6005) Dmel_CG3131(Duox) Dmel_CG3477(Pxd)
                 Dmel_CG4977(kek2) Dmel_CG7660(pxt) Dmel_CG8913(Irc)
            CEL: F09F3.5 T06D8.10(peroxidase)
            ATH: AT1G05260(RCI3) AT1G14540 AT1G14550 AT1G24110 AT1G30870
                 AT1G34510 AT1G44970 AT1G49570 AT1G68850 AT1G71695 AT2G18140
                 AT2G18150 AT2G18980 AT2G22420 AT2G24800 AT2G34060 AT2G37130
                 AT2G38380 AT2G38390 AT2G39040 AT2G41480 AT2G43480 AT3G01190
                 AT3G03670 AT3G17070 AT3G21770 AT3G28200
                 AT3G49110(ATPCA/ATPRX33/PRX33/PRXCA)
                 AT3G49120(ATPCB/ATPERX34/PERX34/PRXCB) AT3G49960 AT4G08770
                 AT4G08780 AT4G11290 AT4G16270 AT4G17690 AT4G21960(PRXR1)
                 AT4G26010 AT4G30170 AT4G31760 AT4G33420 AT4G36430 AT4G37520
                 AT4G37530 AT5G05340 AT5G06720 AT5G06730 AT5G14130 AT5G15180
                 AT5G17820 AT5G19880 AT5G19890 AT5G22410 AT5G24070 AT5G40150
                 AT5G42180 AT5G47000 AT5G51890 AT5G58390 AT5G58400 AT5G64100
                 AT5G64110 AT5G64120 AT5G66390 AT5G67400
            OSA: 4325127 4326874 4332174 4332175 4335846 4338164 4340745
                 4341861 4342251 4343309 4345222 4347336 4349587
            CME: CMC039C
            AFM: AFUA_4G08580
            DDI: DDBDRAFT_0204808
            PFA: PF14_0368 PFL0595c PFL0725w
            ECI: UTI89_C4532(katG)
            HIP: CGSHiEE_01810(bcp)
            PPU: PP_0235(lsfA)
            PPF: Pput_0250
            PFL: PFL_5939
            PFO: Pfl_5416
            PEN: PSEEN0215(lsfA)
            PMY: Pmen_4325
            PCR: Pcryo_0667
            PRW: PsycPRwf_1436
            SFR: Sfri_1982
            PHA: PSHAa1122(bcp)
            MAQ: Maqu_0254 Maqu_0381 Maqu_1410
            NOC: Noc_0878 Noc_1307
            AEH: Mlg_0829
            CSA: Csal_0179
            CVI: CV_1938 CV_3739
            RSO: RSc0754(RS05099)
            REU: Reut_B4984
            REH: H16_B0946
            RME: Rmet_2654 Rmet_4131
            BMA: BMA2066
            BXE: Bxe_A3905 Bxe_B2802
            BVI: Bcep1808_0748
            BUR: Bcep18194_A3905 Bcep18194_B0181 Bcep18194_B1953
            BCN: Bcen_0329
            BCH: Bcen2424_0812
            BAM: Bamb_0693
            BPS: BPSL2748
            BPM: BURPS1710b_3239(lsfA)
            BTE: BTH_I1388
            POL: Bpro_2374 Bpro_4841
            VEI: Veis_0864
            HAR: HEAR3137
            MMS: mma_0861 mma_3379(lsfA)
            NMU: Nmul_A2312
            AZO: azo2548(dyp)
            MFA: Mfla_1551
            DVU: DVU2247
            AFW: Anae109_0482
            SMD: Smed_4963
            RET: RHE_CH01791
            RLE: RL1859 RL2003
            BRA: BRADO1666(katG)
            BBT: BBta_6389(katG)
            RPA: RPA2443
            RPB: RPB_3015
            RPC: RPC_1920
            RPD: RPD_2437
            RPE: RPE_3981
            NWI: Nwi_0891 Nwi_1738
            NHA: Nham_2167
            XAU: Xaut_2363
            SIT: TM1040_0075
            JAN: Jann_4026
            RDE: RD1_0634
            PDE: Pden_2756
            MMR: Mmar10_0498
            SWI: Swit_3162
            GBE: GbCGDNIH1_0908 GbCGDNIH1_1677
            ACR: Acry_2948
            RRU: Rru_A1418 Rru_A2897
            SUS: Acid_5901
            MVA: Mvan_1420
            FAL: FRAAL0302 FRAAL4492(ahpC)
            RBA: RB11131 RB4293 RB633
            SYF: Synpcc7942_2449
            AVA: Ava_1358 Ava_2024
            TER: Tery_5038
            FJO: Fjoh_5017
            FPS: FP1730(catG)
            CCH: Cag_0700
            PLT: Plut_0581
            MMQ: MmarC5_0413
            MBU: Mbur_0959
            MTP: Mthe_1416
            MHU: Mhun_2734
            MEM: Memar_0162
            NPH: NP2708A(perA)
            SMR: Smar_0058
            PIS: Pisl_1860
            PCL: Pcal_0184
            PAS: Pars_0481
            TPE: Tpen_1570
STRUCTURES  PDB: 1ARP  1ARU  1ARV  1ARW  1ARX  1ARY  1ATJ  1BGP  1C8I  1CK6  
                 1CXP  1D2V  1D5L  1D7W  1DNU  1DNW  1FHF  1GW2  1GWO  1GWT  
                 1GWU  1GX2  1GZA  1GZB  1H3J  1H55  1H57  1H58  1H5A  1H5C  
                 1H5D  1H5E  1H5F  1H5G  1H5H  1H5I  1H5J  1H5K  1H5L  1H5M  
                 1HCH  1HSR  1KZM  1LY8  1LY9  1LYC  1LYK  1MHL  1MNP  1MYP  
                 1PA2  1QO4  1SCH  1W4W  1W4Y  1XXU  2ATJ  2C0D  2E39  2E3A  
                 2E3B  2E9E  2EFB  2EHA  2GJ1  2GJM  2IKC  2IPS  2NQX  2O86  
                 2OJV  2PT3  2PUM  2QPK  2QQT  2QRB  2R5L  2Z5Z  3ATJ  4ATJ  
                 6ATJ  7ATJ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.11.1.7
            ExPASy - ENZYME nomenclature database: 1.11.1.7
            ExplorEnz - The Enzyme Database: 1.11.1.7
            ERGO genome analysis and discovery system: 1.11.1.7
            BRENDA, the Enzyme Database: 1.11.1.7
            CAS: 9003-99-0
///
ENTRY       EC 1.11.1.8                 Enzyme
NAME        iodide peroxidase;
            iodotyrosine deiodase;
            iodinase;
            iodoperoxidase (heme type);
            thyroid peroxidase;
            iodide peroxidase-tyrosine iodinase;
            iodotyrosine deiodinase;
            monoiodotyrosine deiodinase;
            thyroperoxidase;
            tyrosine iodinase;
            TPO
CLASS       Oxidoreductases;
            Acting on a peroxide as acceptor;
            Peroxidases
SYSNAME     iodide:hydrogen-peroxide oxidoreductase
REACTION    2 iodide + H2O2 + 2 H+ = diiodine + 2 H2O [RN:R02810]
ALL_REAC    R02810;
            (other) R03208 R03539 R03953 R03973
SUBSTRATE   iodide [CPD:C00708];
            H2O2 [CPD:C00027];
            H+ [CPD:C00080]
PRODUCT     diiodine;
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A hemoprotein.
REFERENCE   1  [PMID:12325367]
  AUTHORS   Coval ML, Taurog A.
  TITLE     Purification and iodinating activity of hog thyroid peroxidase.
  JOURNAL   J. Biol. Chem. 242 (1967) 5510-23.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:13718859]
  AUTHORS   CUNNINGHAM BA, KIRKWOOD S.
  TITLE     Enzyme systems concerned with the synthesis of monoiodotyrosine.
            III. Ion requirements of the soluble system.
  JOURNAL   J. Biol. Chem. 236 (1961) 485-9.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Hosoya, T., Kondo, Y. and Ui, N.
  TITLE     Peroxidase activity in thyroid gland and partial purification of the
            enzyme.
  JOURNAL   J. Biochem. (Tokyo) 52 (1962) 180-189.
  ORGANISM  pig [GN:ssc]
REFERENCE   4
  AUTHORS   Serif, G.S. and Kirkwood, S.
  TITLE     Enzyme systems concerned with the synthesis of monoiodotyrosine. II.
            Further properties of the soluble and mitochondrial systems.
  JOURNAL   J. Biol. Chem. 233 (1958) 109-115.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map04060  Cytokine-cytokine receptor interaction
            PATH: map04630  Jak-STAT signaling pathway
            PATH: map04640  Hematopoietic cell lineage
ORTHOLOGY   KO: K00431  thyroid peroxidase
GENES       HSA: 7173(TPO)
            MMU: 22018(Tpo)
            RNO: 54314(Tpo)
            CFA: 403521(TPO)
DBLINKS     IUBMB Enzyme Nomenclature: 1.11.1.8
            ExPASy - ENZYME nomenclature database: 1.11.1.8
            ExplorEnz - The Enzyme Database: 1.11.1.8
            ERGO genome analysis and discovery system: 1.11.1.8
            BRENDA, the Enzyme Database: 1.11.1.8
            CAS: 9031-28-1
///
ENTRY       EC 1.11.1.9                 Enzyme
NAME        glutathione peroxidase;
            GSH peroxidase;
            selenium-glutathione peroxidase;
            reduced glutathione peroxidase
CLASS       Oxidoreductases;
            Acting on a peroxide as acceptor;
            Peroxidases
SYSNAME     glutathione:hydrogen-peroxide oxidoreductase
REACTION    2 glutathione + H2O2 = glutathione disulfide + 2 H2O [RN:R00274]
ALL_REAC    R00274;
            (other) R07034 R07035
SUBSTRATE   glutathione [CPD:C00051];
            H2O2 [CPD:C00027]
PRODUCT     glutathione disulfide [CPD:C00127];
            H2O [CPD:C00001]
COFACTOR    Selenium [CPD:C01529]
COMMENT     A protein containing a selenocysteine residue. Steroid and lipid
            hydroperoxides, but not the product of reaction of EC 1.13.11.12
            lipoxygenase on phospholipids, can act as acceptor, but more slowly
            than H2O2 (cf. EC 1.11.1.12 phospholipid-hydroperoxide glutathione
            peroxidase).
REFERENCE   1  [PMID:6227287]
  AUTHORS   Chaudiere J, Tappel AL.
  TITLE     Purification and characterization of selenium-glutathione peroxidase
            from hamster liver.
  JOURNAL   Arch. Biochem. Biophys. 226 (1983) 448-57.
  ORGANISM  hamster
REFERENCE   2  [PMID:6413205]
  AUTHORS   Grossmann A, Wendel A.
  TITLE     Non-reactivity of the selenoenzyme glutathione peroxidase with
            enzymatically hydroperoxidized phospholipids.
  JOURNAL   Eur. J. Biochem. 135 (1983) 549-52.
  ORGANISM  cow [GN:bta]
REFERENCE   3
  AUTHORS   Nakamura, W., Hosoda, S. and Hayashi, K.
  TITLE     Purification and properties of rat liver glutathione peroxidase.
  JOURNAL   Biochim. Biophys. Acta 358 (1974) 251-261.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00480  Glutathione metabolism
            PATH: map00590  Arachidonic acid metabolism
ORTHOLOGY   KO: K00432  glutathione peroxidase
GENES       HSA: 257202(GPX6) 2876(GPX1) 2877(GPX2) 2878(GPX3) 2879(GPX4)
                 2880(GPX5) 2882(GPX7)
            PTR: 469325(GPX7)
            MMU: 14775(Gpx1) 14776(Gpx2) 14778(Gpx3) 14780(Gpx5) 67305(Gpx7)
                 75512(Gpx6)
            RNO: 24404(Gpx1) 259233(Gpx6) 29326(Gpx2) 29328(Gpx4) 64317(Gpx3)
            CFA: 442961(GPX1) 489179(LOC489179) 606843(LOC606843)
            BTA: 281209(GPX1) 281210(GPX3) 286809(GPX4)
            SSC: 396920(GPX5) 397403(GPX1) 399537(GPX4)
            GGA: 424643(GPX7)
            XLA: 432086(MGC78781) 494689(LOC494689) 495339(LOC495339)
                 496242(LOC496242) 496254(LOC496254)
            XTR: 394558(gpx3)
            DRE: 352926(gpx1a)
            SPU: 587759(LOC587759) 588243(LOC588243)
            DME: Dmel_CG12013 Dmel_CG4421(GstD8)
            CEL: C11E4.1 C11E4.2 F26E4.12 R03G5.5 R05H10.5
            ATH: AT1G63460 AT2G25080(ATGPX1) AT2G31570(ATGPX2)
                 AT2G48150(ATGPX4) AT3G63080(ATGPX5) AT4G11600(ATGPX6)
                 AT4G31870(ATGPX7)
            OSA: 4330235 4332876 4336627 4340341
            SCE: YBR244W(GPX2) YIR037W(HYR1) YKL026C(GPX1)
            PIC: PICST_52875(HYR1) PICST_78456(GPX2)
            CGR: CAGL0C01705g CAGL0I00264g
            SPO: SPBC32F12.03c
            ANI: AN2846.2
            AFM: AFUA_3G12270
            AOR: AO090005000739
            CNE: CNE00580
            UMA: UM01784.1
            ECU: ECU02_0440
            PFA: PFL0595c
            CPV: cgd3_460
            CHO: Chro.30063
            TET: TTHERM_00630010 TTHERM_00895650 TTHERM_00895660
            TBR: Tb11.01.7560 Tb927.7.1120 Tb927.7.1130 Tb927.7.1140
            TCR: 503899.110 503899.119 503899.130 507515.10 511019.99
                 511543.60
            LMA: LmjF26.0800 LmjF26.0810 LmjF26.0820 LmjF36.3010
            ECO: b1710(btuE)
            ECJ: JW1700(btuE)
            ECE: Z2739(btuE)
            ECS: ECs2417
            ECC: c2106(btuE)
            ECI: UTI89_C1903(btuE)
            ECP: ECP_1658
            ECV: APECO1_785(btuE)
            STY: STY1769(btuE)
            STT: t1222(btuE)
            SPT: SPA1502(btuE)
            SEC: SC1360(btuE)
            STM: STM1341(btuE)
            YPE: YPO2424(btuE)
            YPK: y1915(btuE)
            YPM: YP_2211(btuE)
            YPA: YPA_1768
            YPN: YPN_1878
            YPP: YPDSF_0726
            YPS: YPTB2332(btuE)
            YEN: YE2194(btuE)
            SFL: SF1521(btuE)
            SFX: S1638(btuE)
            SFV: SFV_1513(btuE)
            SSN: SSON_1448(btuE)
            SBO: SBO_1418(btuE)
            SDY: SDY_1805(btuE)
            ECA: ECA1833(btuE)
            ENT: Ent638_1732 Ent638_2699
            KPN: KPN_02167(btuE)
            SPE: Spro_2152 Spro_2171
            XFA: XF1604 XF1890
            XFT: PD0901(gpo) PD1169(btuE)
            XCC: XCC1413(gpo) XCC1501(btuE) XCC4213(btuE)
            XCB: XC_2735 XC_2825 XC_4302
            XCV: XCV1514(gpo) XCV1592 XCV4457(btuE)
            XAC: XAC1457(gpo) XAC1549(btuE) XAC4346(btuE)
            XOO: XOO2064(btuE) XOO2339(gpo)
            XOM: XOO_1944(XOO1944) XOO_2219(XOO2219) XOO_4312(XOO4312)
            PPR: PBPRB1182
            PAE: PA0838 PA1287 PA2826
            PAU: PA14_27520(gpo) PA14_47550 PA14_53420(btuE)
            PPU: PP_0777 PP_1686 PP_1874
            PPF: Pput_3841
            PST: PSPTO_1172 PSPTO_1719 PSPTO_1781
            PSB: Psyr_1010 Psyr_3613 Psyr_3670
            PSP: PSPPH_1059 PSPPH_3629 PSPPH_3690
            PFL: PFL_0941 PFL_4245 PFL_4419
            PFO: Pfl_0883 Pfl_1654 Pfl_3981
            PEN: PSEEN0919(gpo) PSEEN1392 PSEEN1585
            PMY: Pmen_3641
            PCR: Pcryo_0694
            ACI: ACIAD0193 ACIAD2085(gpo)
            ACB: A1S_0159 A1S_1470
            SON: SO_1563
            SDN: Sden_2552 Sden_2679
            SFR: Sfri_2764 Sfri_2853
            SAZ: Sama_1080
            SBL: Sbal_1384
            SBM: Shew185_1368
            SLO: Shew_2741
            SPC: Sputcn32_1300
            SSE: Ssed_3298
            SPL: Spea_2964
            SHE: Shewmr4_1196 Shewmr4_2705
            SHM: Shewmr7_1267 Shewmr7_2773
            SHN: Shewana3_1197 Shewana3_2875
            SHW: Sputw3181_2803
            CPS: CPS_2006
            PHA: PSHAa0062 PSHAa1253 PSHAa2487
            PAT: Patl_2176 Patl_2526
            SDE: Sde_2931
            MAQ: Maqu_1771
            MCA: MCA0841(bsaA)
            FTU: FTT0733
            FTF: FTF0733
            FTW: FTW_0638
            FTL: FTL_1383
            FTH: FTH_1345
            FTN: FTN_0698
            HCH: HCH_00110 HCH_00491 HCH_02304
            CSA: Csal_2825
            ABO: ABO_2638(GSHPx)
            MMW: Mmwyl1_2461
            AHA: AHA_0644
            NME: NMB1621
            NMA: NMA1820(gpxA)
            NMC: NMC1547(gpxA)
            CVI: CV_1107 CV_3555 CV_3787
            RSO: RSc0307(RS03274) RSc2674(RS00047)
            REU: Reut_A0042 Reut_A2798
            RME: Rmet_0018 Rmet_2934
            BMA: BMA1571(bsaA)
            BMV: BMASAVP1_A2074(bsaA)
            BML: BMA10299_A3238(bsaA)
            BMN: BMA10247_1346(bsaA)
            BXE: Bxe_A1665
            BVI: Bcep1808_1941
            BUR: Bcep18194_A5344 Bcep18194_C7246
            BCN: Bcen_6042
            BCH: Bcen2424_2035
            BAM: Bamb_2067
            BPS: BPSL2175(gpo)
            BPM: BURPS1710b_2599(gpo)
            BPL: BURPS1106A_2510(bsaA)
            BPD: BURPS668_2454(bsaA)
            BTE: BTH_I2011
            BPE: BP1301
            BPA: BPP2917
            BBR: BB2887
            RFR: Rfer_0484
            POL: Bpro_0190 Bpro_4659
            PNA: Pnap_0128
            AAV: Aave_0250
            AJS: Ajs_0173
            MPT: Mpe_A3685
            HAR: HEAR2926
            MMS: mma_0338(bsaA)
            NEU: NE1206
            NET: Neut_0992
            EBA: ebA6393(btuE)
            AZO: azo1277 azo3790
            DAR: Daro_0488 Daro_1090
            PPD: Ppro_0118 Ppro_0123
            BBA: Bd0326(btuE) Bd0522(bsaA) Bd1947(bsaA)
            DPS: DP0532
            MXA: MXAN_2389 MXAN_7090
            PUB: SAR11_1004(bsaA)
            RET: RHE_CH01597(btuE)
            RLE: RL1698
            BJA: bll4149 bll6732
            BRA: BRADO3371 BRADO5788(gpx)
            BBT: BBta_3880 BBta_6295(gpx)
            RPA: RPA3627
            RPB: RPB_1897
            RPC: RPC_3665
            RPD: RPD_3470
            RPE: RPE_2397 RPE_3703
            NWI: Nwi_2639
            NHA: Nham_3267
            XAU: Xaut_3507
            CCR: CC_1730
            SIL: SPO3742
            RSP: RSP_2389
            JAN: Jann_3273
            RDE: RD1_0599(gpo)
            HNE: HNE_3064
            NAR: Saro_0565 Saro_1769
            SAL: Sala_1178
            SWI: Swit_4077
            ELI: ELI_06990
            GOX: GOX1877
            GBE: GbCGDNIH1_1033 GbCGDNIH1_1961
            RRU: Rru_A0020 Rru_A1863
            MAG: amb3627
            ABA: Acid345_1872
            SUS: Acid_7250
            BSU: BG11530(bsaA)
            BHA: BH2830(bsaA)
            BAN: BA2119(bsaA)
            BAR: GBAA2119(bsaA)
            BAA: BA_2615
            BAT: BAS1971
            BCE: BC2114
            BCA: BCE_2202(bsaA)
            BCZ: BCZK1926(bsaA)
            BCY: Bcer98_1597
            BTK: BT9727_1950(bsaA)
            BTL: BALH_1881
            BLI: BL01369(bsaA)
            BLD: BLi02327(bsaA)
            BCL: ABC1266(bsaA)
            BAY: RBAM_020040(bsaA)
            BPU: BPUM_1925(bsaA)
            OIH: OB0263 OB0570
            GKA: GK1785
            SAU: SA1146(bsaA) SA2414
            SAV: SAV1306(bsaA) SAV2621
            SAM: MW1188(bsaA) MW2541
            SAR: SAR1280 SAR2699
            SAS: SAS1238 SAS2507
            SAC: SACOL1325(gpxA1) SACOL2641(gpxA2)
            SAB: SAB1168c SAB2495c
            SAA: SAUSA300_1197 SAUSA300_2555
            SAO: SAOUHSC_01282 SAOUHSC_02949
            SEP: SE0983 SE2183
            SER: SERP0872(gpxA-1) SERP2194(gpxA-2)
            SHA: SH1604(bsaA)
            SSP: SSP1455
            LMO: lmo0983
            LMF: LMOf2365_1004(bsaA)
            LIN: lin0982
            LWE: lwe0966(bsaA)
            LLA: L0198(gpo)
            LLC: LACR_1499
            LLM: llmg_1088(gpo)
            SPY: SPy_0605(bsaA)
            SPZ: M5005_Spy_0503
            SPM: spyM18_0672(bsaA)
            SPG: SpyM3_0428
            SPS: SPs1427
            SPH: MGAS10270_Spy0497
            SPI: MGAS10750_Spy0522
            SPJ: MGAS2096_Spy0514
            SPK: MGAS9429_Spy0493
            SPF: SpyM51360
            SPA: M6_Spy0524
            SPB: M28_Spy0482
            SPN: SP_0313
            SPR: spr0285(basA)
            SPD: SPD_0286
            SSA: SSA_1523(basA)
            SGO: SGO_0758
            LPL: lp_0220(gpo)
            LBR: LVIS_2003
            LCA: LSEI_0893
            OOE: OEOE_0888
            CAC: CAC1549(bsaA) CAC1570(bsaA) CAC1571
            CPE: CPE0911(bsaA) CPE0954(gpo)
            CPF: CPF_0904 CPF_1198
            CPR: CPR_0867 CPR_1026
            CNO: NT01CX_2376
            CBE: Cbei_0389 Cbei_0777
            MPE: MYPE5120
            UUR: UU291(bsaA)
            MAV: MAV_4129
            MSM: MSMEG_5837
            MVA: Mvan_5134
            MMC: Mmcs_4557
            MKM: Mkms_4645
            MJL: Mjls_4940
            CGL: NCgl2502(cgl2591)
            CGB: cg2867(gpx)
            CEF: CE2483
            CDI: DIP1925
            NFA: nfa46650
            RHA: RHA1_ro04823
            SCO: SCO4444(SCD6.22c)
            SMA: SAV3778(bsaA)
            LXX: Lxx17630(gpoA)
            ART: Arth_0559
            NCA: Noca_0137
            TFU: Tfu_2759
            FRA: Francci3_1059
            FAL: FRAAL1783(btuE)
            KRA: Krad_1247
            FNU: FN2007
            RBA: RB2244
            TDE: TDE1729
            LIL: LA1007 LA4299
            LIC: LIC12648(btuE) LIC13442(gpo)
            LBJ: LBJ_2622(btuE-2) LBJ_2958(btuE-1)
            LBL: LBL_0106(btuE-1) LBL_0500(btuE-2)
            SYN: slr1171(gpx1) slr1992(gpx2)
            SYW: SYNW0099
            SYC: syc0336_c(gpx1)
            SYF: Synpcc7942_1214
            SYD: Syncc9605_0091
            SYE: Syncc9902_0137
            SYG: sync_0096
            SYR: SynRCC307_0096
            SYX: SynWH7803_0151
            GVI: glr4043
            PMA: Pro1221(ctuE)
            PMM: PMM1006
            PMT: PMT0125
            PMN: PMN2A_1209
            PMI: PMT9312_1016
            PMB: A9601_10951(btuE)
            PMC: P9515_10911(btuE)
            PMF: P9303_01621(btuE)
            PMG: P9301_10951(btuE)
            PME: NATL1_20841(btuE)
            BTH: BT_3971
            BFR: BF3886
            BFS: BF3656
            CHU: CHU_1579(btuE)
            FPS: FP1417(bsaA)
            RRS: RoseRS_3106
            RCA: Rcas_2947
STRUCTURES  PDB: 1GP1  2F8A  2HE3  2I3Y  2P31  2R37  
DBLINKS     IUBMB Enzyme Nomenclature: 1.11.1.9
            ExPASy - ENZYME nomenclature database: 1.11.1.9
            ExplorEnz - The Enzyme Database: 1.11.1.9
            ERGO genome analysis and discovery system: 1.11.1.9
            BRENDA, the Enzyme Database: 1.11.1.9
            CAS: 9013-66-5
///
ENTRY       EC 1.11.1.10                Enzyme
NAME        chloride peroxidase;
            chloroperoxidase
CLASS       Oxidoreductases;
            Acting on a peroxide as acceptor;
            Peroxidases
SYSNAME     chloride:hydrogen-peroxide oxidoreductase
REACTION    2 RH + 2 Cl- + H2O2 = 2 RCl + 2 H2O [RN:R00052]
ALL_REAC    R00052
SUBSTRATE   RH [CPD:C01371];
            Cl- [CPD:C00698];
            H2O2 [CPD:C00027]
PRODUCT     RCl [CPD:C01334];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     Brings about the chlorination of a range of organic molecules,
            forming stable C-Cl bonds. Can also act on Br- and I-. Probably a
            heme-thiolate protein (P-450).
REFERENCE   1  [PMID:1056179]
  AUTHORS   Hager LP, Hollenberg PF, Rand-Meir T, Chiang R, Doubek D.
  TITLE     Chemistry of peroxidase intermediates.
  JOURNAL   Ann. N. Y. Acad. Sci. 244 (1975) 80-93.
REFERENCE   2  [PMID:5949836]
  AUTHORS   Morris DR, Hager LP.
  TITLE     Chloroperoxidase. I. Isolation and properties of the crystalline
            glycoprotein.
  JOURNAL   J. Biol. Chem. 241 (1966) 1763-8.
  ORGANISM  Caldariomyces fumago
REFERENCE   3
  AUTHORS   Theiler, R., Cook, J.C., Hager, L.P. and Siuda, J.F.
  TITLE     Halohydrocarbon synthesis by homoperoxidase.
  JOURNAL   Science 202 (1978) 1094-1096.
  ORGANISM  Bonnemaisonia hamifera
ORTHOLOGY   KO: K00433  chloride peroxidase
GENES       TET: TTHERM_00089170
            XCC: XCC2172(cpo)
            XCB: XC_1946
            XCV: XCV2196
            XAC: XAC2035(cpo)
            PAE: PA2717(cpo)
            PAU: PA14_29020(cpo)
            PPU: PP_4021(est)
            PSB: Psyr_4478
            PFL: PFL_3458
            PFO: Pfl_2172 Pfl_2461
            PEN: PSEEN2814(cpo) PSEEN5395
            SDN: Sden_2086
            HCH: HCH_03053
            REU: Reut_B5209
            REH: H16_B1410 H16_B1943
            RME: Rmet_5312
            BXE: Bxe_B1809 Bxe_B2381
            BUR: Bcep18194_A4969 Bcep18194_C6615 Bcep18194_C6846
                 Bcep18194_C6920 Bcep18194_C7311 Bcep18194_C7313
                 Bcep18194_C7479 Bcep18194_C7536
            BCN: Bcen_1465
            BCH: Bcen2424_6363
            BPS: BPSS0444(cpo)
            BPM: BURPS1710b_A1992(cpo)
            BPL: BURPS1106A_A0603(cpoF)
            BPD: BURPS668_A0694
            AZO: azo0490
            MLO: mll2689 mlr0978
            SME: SMa1809 SMb20054(cpo) SMc01944
            SMD: Smed_4084
            ATU: Atu3463(cpoF) Atu3493 Atu4778(cpo)
            ATC: AGR_L_210 AGR_L_2670 AGR_L_2734
            RET: RHE_CH01162 RHE_CH01902 RHE_CH02571(ypch00867)
            RLE: RL2208 RL2967(cpo) pRL110136(cpo) pRL120450(cpo)
            BME: BMEI0733
            BJA: blr1251
            BRA: BRADO1257 BRADO2692 BRADO4449(cpo)
            BBT: BBta_1889(cpo) BBta_2279 BBta_4668(cpo)
            RPA: RPA2105
            RPB: RPB_0185 RPB_0194 RPB_3239 RPB_3504
            RPC: RPC_4420
            RPE: RPE_2277 RPE_4490
            HNE: HNE_3365
            SAL: Sala_0477
            GOX: GOX0738 GOX1766
            ABA: Acid345_3102 Acid345_3745
            BAN: BA5030
            BAR: GBAA5030
            BAA: BA_5447
            BAT: BAS4670
            BCE: BC4774
            BCA: BCE_3158 BCE_4929
            BCZ: BCZK4530
            BTK: BT9727_4511
            BTL: BALH_4349
            BLD: BLi02236(yisY)
            LLM: llmg_1737(cpo)
            CTC: CTC01150
            CKL: CKL_0764
            MVA: Mvan_1567
            MMC: Mmcs_1286
            MKM: Mkms_1303
            RHA: RHA1_ro01401 RHA1_ro02074 RHA1_ro02101
            SCO: SCO0465(SCF76.05c)
            SMA: SAV974
            TFU: Tfu_1653
            FAL: FRAAL2804(cpo)
            KRA: Krad_0128
            SEN: SACE_3365(cpo)
            STP: Strop_4189
            RBA: RB2401(cpo) RB3694
            SYN: slr0314
            AVA: Ava_0013 Ava_3458 Ava_5030 Ava_C0107
            CCH: Cag_1627
            MAC: MA0993
STRUCTURES  PDB: 1A7U  1A88  1A8Q  1A8S  1A8U  1BRT  1CPO  1IDQ  1IDU  1QHB  
                 1QI9  1VNC  1VNE  1VNF  1VNG  1VNH  1VNI  1VNS  2CIV  2CIW  
                 2CIX  2CIY  2CIZ  2CJ0  2CJ1  2CJ2  2CPO  2J18  2J19  2J5M  
DBLINKS     IUBMB Enzyme Nomenclature: 1.11.1.10
            ExPASy - ENZYME nomenclature database: 1.11.1.10
            ExplorEnz - The Enzyme Database: 1.11.1.10
            ERGO genome analysis and discovery system: 1.11.1.10
            BRENDA, the Enzyme Database: 1.11.1.10
            CAS: 9055-20-3
///
ENTRY       EC 1.11.1.11                Enzyme
NAME        L-ascorbate peroxidase;
            L-ascorbic acid peroxidase;
            L-ascorbic acid-specific peroxidase;
            ascorbate peroxidase;
            ascorbic acid peroxidase
CLASS       Oxidoreductases;
            Acting on a peroxide as acceptor;
            Peroxidases
SYSNAME     L-ascorbate:hydrogen-peroxide oxidoreductase
REACTION    L-ascorbate + H2O2 = dehydroascorbate + 2 H2O [RN:R00642]
ALL_REAC    R00642 > R00644
SUBSTRATE   L-ascorbate [CPD:C00072];
            H2O2 [CPD:C00027]
PRODUCT     dehydroascorbate [CPD:C00425];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:6772104]
  AUTHORS   Shigeoka S, Nakano Y, Kitaoka S.
  TITLE     Purification and some properties of L-ascorbic-acid-specific
            peroxidase in Euglena gracilis Z.
  JOURNAL   Arch. Biochem. Biophys. 201 (1980) 121-7.
  ORGANISM  Euglena gracilis
REFERENCE   2  [PMID:6768357]
  AUTHORS   Shigeoka S, Nakano Y, Kitaoka S.
  TITLE     Metabolism of hydrogen peroxide in Euglena gracilis Z by L-ascorbic
            acid peroxidase.
  JOURNAL   Biochem. J. 186 (1980) 377-80.
  ORGANISM  Euglena gracilis
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K00434  L-ascorbate peroxidase
GENES       OSA: 4335202 4336886 4344397 4346247
            TCR: 503745.30 506193.60
            LMA: LmjF34.0070
STRUCTURES  PDB: 1APX  1IYN  1OAF  1OAG  1V0H  2CL4  2GGN  2GHC  2GHD  2GHE  
                 2GHH  2GHK  
DBLINKS     IUBMB Enzyme Nomenclature: 1.11.1.11
            ExPASy - ENZYME nomenclature database: 1.11.1.11
            ExplorEnz - The Enzyme Database: 1.11.1.11
            ERGO genome analysis and discovery system: 1.11.1.11
            BRENDA, the Enzyme Database: 1.11.1.11
            CAS: 72906-87-7
///
ENTRY       EC 1.11.1.12                Enzyme
NAME        phospholipid-hydroperoxide glutathione peroxidase;
            peroxidation-inhibiting protein;
            PHGPX;
            peroxidation-inhibiting protein: peroxidase, glutathione
            (phospholipid hydroperoxide-reducing);
            phospholipid hydroperoxide glutathione peroxidase;
            hydroperoxide glutathione peroxidase
CLASS       Oxidoreductases;
            Acting on a peroxide as acceptor;
            Peroxidases
SYSNAME     glutathione:lipid-hydroperoxide oxidoreductase
REACTION    2 glutathione + a lipid hydroperoxide = glutathione disulfide +
            lipid + 2 H2O [RN:R03167]
ALL_REAC    R03167
SUBSTRATE   glutathione [CPD:C00051];
            lipid hydroperoxide [CPD:C01025]
PRODUCT     glutathione disulfide [CPD:C00127];
            lipid [CPD:C01356];
            H2O [CPD:C00001]
COMMENT     A protein containing a selenocysteine residue. The products of
            action of EC 1.13.11.12 lipoxygenase on phospholipids can act as
            acceptor; H2O2 can also act, but much more slowly (cf. EC 1.11.1.9
            glutathione peroxidase).
REFERENCE   1  [PMID:3978121]
  AUTHORS   Ursini F, Maiorino M, Gregolin C.
  TITLE     The selenoenzyme phospholipid hydroperoxide glutathione peroxidase.
  JOURNAL   Biochim. Biophys. Acta. 839 (1985) 62-70.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00480  Glutathione metabolism
ORTHOLOGY   KO: K05361  phospholipid-hydroperoxide glutathione peroxidase
GENES       MMU: 625249(Gpx4)
            DRE: 352928(gpx4a) 352929(gpx4b)
            TET: TTHERM_00046090 TTHERM_00046110 TTHERM_00895630
                 TTHERM_00895640 TTHERM_01099010
STRUCTURES  PDB: 2GS3  2OBI  
DBLINKS     IUBMB Enzyme Nomenclature: 1.11.1.12
            ExPASy - ENZYME nomenclature database: 1.11.1.12
            ExplorEnz - The Enzyme Database: 1.11.1.12
            ERGO genome analysis and discovery system: 1.11.1.12
            BRENDA, the Enzyme Database: 1.11.1.12
            CAS: 97089-70-8
///
ENTRY       EC 1.11.1.13                Enzyme
NAME        manganese peroxidase;
            peroxidase-M2;
            Mn-dependent (NADH-oxidizing) peroxidase
CLASS       Oxidoreductases;
            Acting on a peroxide as acceptor;
            Peroxidases
SYSNAME     Mn(II):hydrogen-peroxide oxidoreductase
REACTION    2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O [RN:R00011]
ALL_REAC    R00011
SUBSTRATE   Mn(II) [CPD:C00034];
            H+ [CPD:C00080];
            H2O2 [CPD:C00027]
PRODUCT     Mn(III) [CPD:C00034];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A hemoprotein. Involved in the oxidative degradation of lignin in
            white rot basidiomycetes.
REFERENCE   1  [PMID:3800395]
  AUTHORS   Glenn JK, Akileswaran L, Gold MH.
  TITLE     Mn(II) oxidation is the principal function of the extracellular
            Mn-peroxidase from Phanerochaete chrysosporium.
  JOURNAL   Arch. Biochem. Biophys. 251 (1986) 688-96.
  ORGANISM  Phanerochaete chrysosporium
REFERENCE   2  [PMID:3080953]
  AUTHORS   Paszczynski A, Huynh VB, Crawford R.
  TITLE     Comparison of ligninase-I and peroxidase-M2 from the white-rot
            fungus Phanerochaete chrysosporium.
  JOURNAL   Arch. Biochem. Biophys. 244 (1986) 750-65.
  ORGANISM  Phanerochaete chrysosporium
REFERENCE   3
  AUTHORS   Wariishi, H., Akileswaran, L. and Gold, M.H.
  TITLE     Manganese peroxidase from the basidiomycete Phanerochaete
            chrysosporium: spectral characterization of the oxidized states and
            the catalytic cycle.
  JOURNAL   Biochemistry 27 (1988) 5365-5370.
  ORGANISM  Phanerochaete chrysosporium
STRUCTURES  PDB: 1MN1  1MN2  1YYD  1YYG  1YZP  1YZR  
DBLINKS     IUBMB Enzyme Nomenclature: 1.11.1.13
            ExPASy - ENZYME nomenclature database: 1.11.1.13
            ExplorEnz - The Enzyme Database: 1.11.1.13
            ERGO genome analysis and discovery system: 1.11.1.13
            BRENDA, the Enzyme Database: 1.11.1.13
            CAS: 114995-15-2
///
ENTRY       EC 1.11.1.14                Enzyme
NAME        lignin peroxidase;
            diarylpropane oxygenase;
            ligninase I;
            diarylpropane peroxidase;
            LiP;
            diarylpropane:oxygen,hydrogen-peroxide oxidoreductase
            (C-C-bond-cleaving)
CLASS       Oxidoreductases;
            Acting on a peroxide as acceptor;
            Peroxidases
SYSNAME     1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol:hydrogen-peroxide
            oxidoreductase
REACTION    1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H2O2 =
            3,4-dimethoxybenzaldehyde + 1-(3,4-dimethoxyphenyl)ethane-1,2-diol +
            H2O [RN:R04461]
ALL_REAC    R04461
SUBSTRATE   1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol [CPD:C04597];
            H2O2 [CPD:C00027]
PRODUCT     3,4-dimethoxybenzaldehyde [CPD:C02201];
            1-(3,4-dimethoxyphenyl)ethane-1,2-diol;
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A hemoprotein. Brings about the oxidative cleavage of C-C and ether
            (C-O-C) bonds in a number of lignin model compounds (of the
            diarylpropane and arylpropane-aryl ether type). The enzyme also
            oxidizes benzyl alcohols to aldehydes, via an aromatic cation
            radical [9]. Involved in the oxidative breakdown of lignin in white
            rot basidiomycetes. Molecular oxygen may be involved in the reaction
            of substrate radicals under aerobic conditions [3,8].
REFERENCE   1  [PMID:3080953]
  AUTHORS   Paszczynski A, Huynh VB, Crawford R.
  TITLE     Comparison of ligninase-I and peroxidase-M2 from the white-rot
            fungus Phanerochaete chrysosporium.
  JOURNAL   Arch. Biochem. Biophys. 244 (1986) 750-65.
  ORGANISM  Phanerochaete chrysosporium
REFERENCE   2  [PMID:4026322]
  AUTHORS   Renganathan V, Miki K, Gold MH.
  TITLE     Multiple molecular forms of diarylpropane oxygenase, an
            H2O2-requiring, lignin-degrading enzyme from Phanerochaete
            chrysosporium.
  JOURNAL   Arch. Biochem. Biophys. 241 (1985) 304-14.
  ORGANISM  Phanerochaete chrysosporium
REFERENCE   3
  AUTHORS   Tien, M. and Kirk, T.T.
  TITLE     Lignin-degrading enzyme from Phanerochaete chrysosporium;
            purification, characterization, and catalytic properties of a unique
            H2O2-requiring oxygenase.
  JOURNAL   Proc. Natl. Acad. Sci. USA 81 (1984) 2280-2284.
  ORGANISM  Phanerochaete chrysosporium
REFERENCE   4  [PMID:9790672]
  AUTHORS   Doyle WA, Blodig W, Veitch NC, Piontek K, Smith AT.
  TITLE     Two substrate interaction sites in lignin peroxidase revealed by
            site-directed mutagenesis.
  JOURNAL   Biochemistry. 37 (1998) 15097-105.
  ORGANISM  Phanerochaete chrysosporium
REFERENCE   5  [PMID:2162833]
  AUTHORS   Wariishi H, Marquez L, Dunford HB, Gold MH.
  TITLE     Lignin peroxidase compounds II and III. Spectral and kinetic
            characterization of reactions with peroxides.
  JOURNAL   J. Biol. Chem. 265 (1990) 11137-42.
  ORGANISM  Phanerochaete chrysosporium
REFERENCE   6  [PMID:2328240]
  AUTHORS   Cai DY, Tien M.
  TITLE     Characterization of the oxycomplex of lignin peroxidases from
            Phanerochaete chrysosporium: equilibrium and kinetics studies.
  JOURNAL   Biochemistry. 29 (1990) 2085-91.
  ORGANISM  Phanerochaete chrysosporium
REFERENCE   7  [PMID:3561490]
  AUTHORS   Tien M, Tu CP.
  TITLE     Cloning and sequencing of a cDNA for a ligninase from Phanerochaete
            chrysosporium.
  JOURNAL   Nature. 326 (1987) 520-3.
  ORGANISM  Phanerochaete chrysosporium
REFERENCE   8  [PMID:3754412]
  AUTHORS   Renganathan V, Miki K, Gold MH.
  TITLE     Role of molecular oxygen in lignin peroxidase reactions.
  JOURNAL   Arch. Biochem. Biophys. 246 (1986) 155-61.
  ORGANISM  Phanerochaete chrysosporium
REFERENCE   9  [PMID:2982828]
  AUTHORS   Kersten PJ, Tien M, Kalyanaraman B, Kirk TK.
  TITLE     The ligninase of Phanerochaete chrysosporium generates cation
            radicals from methoxybenzenes.
  JOURNAL   J. Biol. Chem. 260 (1985) 2609-12.
  ORGANISM  Phanerochaete chrysosporium
REFERENCE   10 [PMID:3318677]
  AUTHORS   Kirk TK, Farrell RL.
  TITLE     Enzymatic &quot;combustion&quot;: the microbial degradation of
            lignin.
  JOURNAL   Annu. Rev. Microbiol. 41 (1987) 465-505.
STRUCTURES  PDB: 1B80  1B82  1B85  
DBLINKS     IUBMB Enzyme Nomenclature: 1.11.1.14
            ExPASy - ENZYME nomenclature database: 1.11.1.14
            ExplorEnz - The Enzyme Database: 1.11.1.14
            ERGO genome analysis and discovery system: 1.11.1.14
            BRENDA, the Enzyme Database: 1.11.1.14
            CAS: 93792-13-3
///
ENTRY       EC 1.11.1.15                Enzyme
NAME        peroxiredoxin;
            thioredoxin peroxidase;
            tryparedoxin peroxidase;
            alkyl hydroperoxide reductase C22;
            AhpC;
            TrxPx;
            TXNPx;
            Prx;
            PRDX
CLASS       Oxidoreductases;
            Acting on a peroxide as acceptor;
            Peroxidases
SYSNAME     thiol-containing-reductant:hydroperoxide oxidoreductase
REACTION    2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH [RN:R07180]
ALL_REAC    R07180
SUBSTRATE   R'-SH;
            ROOH [CPD:C15498]
PRODUCT     R-S-S-R [CPD:C15496];
            H2O [CPD:C00001];
            ROH [CPD:C01335]
COMMENT     Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant
            proteins. They can be divided into three classes: typical 2-Cys,
            atypical 2-Cys and 1-Cys peroxiredoxins [1]. The peroxidase reaction
            comprises two steps centred around a redox-active cysteine called
            the peroxidatic cysteine. All three peroxiredoxin classes have the
            first step in common, in which the peroxidatic cysteine attacks the
            peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic
            acid) (see mechanism). The second step of the peroxidase reaction,
            the regeneration of cysteine from S-hydroxycysteine, distinguishes
            the three peroxiredoxin classes. For typical 2-Cys Prxs, in the
            second step, the peroxidatic S-hydroxycysteine from one subunit is
            attacked by the 'resolving' cysteine located in the C-terminus of
            the second subunit, to form an intersubunit disulfide bond, which is
            then reduced by one of several cell-specific thiol-containing
            reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD),
            completing the catalytic cycle. In the atypical 2-Cys Prxs, both the
            peroxidatic cysteine and its resolving cysteine are in the same
            polypeptide, so their reaction forms an intrachain disulfide bond
            [1]. To recycle the disulfide, known atypical 2-Cys Prxs appear to
            use thioredoxin as an electron donor [3]. The 1-Cys Prxs conserve
            only the peroxidatic cysteine, so that its oxidized form is directly
            reduced to cysteine by the reductant molecule [4].
REFERENCE   1  [PMID:12517450]
  AUTHORS   Wood ZA, Schroder E, Robin Harris J, Poole LB.
  TITLE     Structure, mechanism and regulation of peroxiredoxins.
  JOURNAL   Trends. Biochem. Sci. 28 (2003) 32-40.
  ORGANISM  rat [GN:rno], human [GN:hsa], Crithidia fasciculata, Salmonella
            typhimurium
REFERENCE   2  [PMID:12033427]
  AUTHORS   Hofmann B, Hecht HJ, Flohe L.
  TITLE     Peroxiredoxins.
  JOURNAL   Biol. Chem. 383 (2002) 347-64.
  ORGANISM  Crithidia fasciculata, Salmonella typhimurium
REFERENCE   3  [PMID:10751410]
  AUTHORS   Seo MS, Kang SW, Kim K, Baines IC, Lee TH, Rhee SG.
  TITLE     Identification of a new type of mammalian peroxiredoxin that forms
            an intramolecular disulfide as a reaction intermediate.
  JOURNAL   J. Biol. Chem. 275 (2000) 20346-54.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:9587003]
  AUTHORS   Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE.
  TITLE     Crystal structure of a novel human peroxidase enzyme at 2.0 A
            resolution.
  JOURNAL   Nat. Struct. Biol. 5 (1998) 400-6.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K03386  peroxiredoxin (alkyl hydroperoxide reductase subunit C)
GENES       HSA: 10549(PRDX4) 10935(PRDX3) 25824(PRDX5) 5052(PRDX1)
                 7001(PRDX2) 9588(PRDX6)
            PTR: 465865(LOC465865) 468740(PRDX2) 469589(PRDX6)
            MMU: 11757(Prdx3) 11758(Prdx6) 18477(Prdx1) 21672(Prdx2)
                 53381(Prdx4) 54683(Prdx5)
            RNO: 113898(Prdx5) 117254(Prdx1) 29338(Prdx2) 64371(Prdx3)
                 85274(Prdx4) 94167(Prdx6)
            CFA: 475375(PRDX1) 476032(PRDX5) 477839(LOC477839) 480069(PRDX6)
                 484926(PRDX2) 491776(PRDX4)
            BTA: 281997(PRDX1) 281998(PRDX3) 281999(PRDX4) 282438(AOP2)
                 282885(PRDX5) 286793(PRDX2)
            SSC: 397273(PRDX5) 399538(PRDX6)
            GGA: 418601(PRDX4) 424598(PRDX1) 428986(PRDX3)
                 429062(RCJMB04_18k11)
            XLA: 398641(MGC64582) 399434(prdx6) 432262(MGC83501)
                 443840(MGC83078) 443911(MGC80194) 444345(MGC82793)
                 444559(MGC83969) 496089(LOC496089)
            XTR: 394597(TTpA010e06.1) 394706(MGC76137) 448526(prdx4)
                 496551(prdx1)
            DRE: 393778(prdx6)
            SPU: 579239(LOC579239) 579284(LOC579284) 581408(LOC581408)
                 590165(LOC590165) 591742(LOC591742)
            DME: Dmel_CG1633(Jafrac1) Dmel_CG3083(Prx6005)
                 Dmel_CG5826(Prx5037)
            CEL: R07E5.2(prdx-3)
            ATH: AT1G48130(ATPER1) AT1G60740 AT3G11630
            OSA: 4344045
            SCE: YBL064C(PRX1) YDR453C(TSA2) YIL010W(DOT5) YLR109W(AHP1)
                 YML028W(TSA1)
            AGO: AGOS_AER312W AGOS_AGR368W
            PIC: PICST_70431(TSA1)
            CAL: CaO19_7417(CaO19.7417)
            CGR: CAGL0A04433g CAGL0G07271g CAGL0K06259g
            SPO: SPCC330.06c(pmp20)
            ANI: AN3973.2 AN4301.2
            AFM: AFUA_4G05915 AFUA_8G07130
            AOR: AO090020000634
            UMA: UM03177.1 UM06404.1
            DDI: DDB_0231647
            TAN: TA19270
            TPV: TP01_0177
            TET: TTHERM_00295170 TTHERM_00721530 TTHERM_00821930
                 TTHERM_00822060 TTHERM_01044760 TTHERM_01194830
            TBR: Tb09.160.4250 Tb927.8.1990
            TCR: 487507.10 504839.28 504839.44 505983.9 507259.10 509445.10
                 509499.14
            LMA: LmjF15.1040 LmjF15.1060 LmjF15.1080 LmjF15.1100 LmjF15.1120
                 LmjF15.1140 LmjF15.1160 LmjF23.0040
            EHI: 294.t00003 94.t00032 963.t00001
            ECO: b0605(ahpC) b2480(bcp)
            ECJ: JW0598(ahpC) JW2465(bcp)
            ECE: Z0749(ahpC) Z3739(bcp)
            ECS: ECs0644 ECs3342
            ECC: c0694(ahpC) c3008(bcp)
            ECI: UTI89_C0608(ahpC)
            ECP: ECP_0638
            ECV: APECO1_1444(ahpC)
            ECW: EcE24377A_0626(ahpC) EcE24377A_1664(osmC) EcE24377A_2762(bcp)
            ECX: EcHS_A0657 EcHS_A0658 EcHS_A1567 EcHS_A2612(bcp)
            STY: STY0440 STY0653(ahpC)
            STT: t2260(ahpC) t2461
            SPT: SPA2126(ahpC) SPA2321
            SEC: SC0444(tsaA) SC0639(ahpC)
            STM: STM0402 STM0608(ahpC)
            YPE: YPO3194(ahpC)
            YPK: y0988
            YPM: YP_0737(ahpC)
            YPA: YPA_2689
            YPN: YPN_0893
            YPS: YPTB0925(ahpC)
            YPI: YpsIP31758_0136 YpsIP31758_1245(bcp)
            SFL: SF0524(ahpC) SF2523(bcp)
            SFX: S0529(ahpC) S2673(bcp)
            SFV: SFV_0559(ahpC)
            SSN: SSON_0557(ahpC) SSON_2561(bcp)
            SBO: SBO_0470(ahpC)
            SDY: SDY_0540(ahpC)
            ECA: ECA1117 ECA3942(ahpC)
            PLU: plu3907(ahpC)
            BUC: BU182(ahpC)
            BAS: BUsg089(bcp) BUsg176(ahpC)
            BAB: bbp171(ahpC)
            BCC: BCc_117(ahpC)
            WBR: WGLp487(ahpC)
            SGL: SG0642
            SPE: Spro_3511 Spro_4776
            BFL: Bfl228(ahpC)
            BPN: BPEN_235(ahpC)
            HIN: HI0254(bcp) HI0572
            HIT: NTHI0212(tsaA) NTHI0705(pdgX)
            HSO: HS_0476(tsaA)
            PMU: PM0795(tsaA)
            MSU: MS1521(ahpC)
            ASU: Asuc_0390
            XFA: XF1530
            XFT: PD0745(ahpC)
            XCC: XCC0834(ahpC)
            XCB: XC_3396
            XCV: XCV0943(ahpC)
            XAC: XAC0907(ahpC)
            XOO: XOO3645(ahpC)
            XOM: XOO_3447(XOO3447)
            VCH: VC0731
            VVU: VV1_0453 VV2_0501
            VVY: VV0739 VVA1050
            VPA: VP0580 VPA1683
            VFI: VF1975
            PPR: PBPRA0735(ahpC) PBPRA2575
            PAE: PA0139(ahpC) PA0848 PA3529
            PAU: PA14_01710(ahpC) PA14_18690(ahpC)
            PAP: PSPA7_0216(ahpC)
            PPU: PP_1084 PP_2439(ahpC)
            PPF: Pput_0802
            PST: PSPTO_3108(ahpC)
            PSB: Psyr_2975
            PSP: PSPPH_2265(ahpC)
            PFL: PFL_3395(ahpC) PFL_4857
            PFO: Pfl_2925 Pfl_4521
            PEN: PSEEN1206 PSEEN2296(ahpC)
            PMY: Pmen_1323 Pmen_1909
            PAR: Psyc_1797(ahpC)
            PRW: PsycPRwf_2139
            ACI: ACIAD0436(ahpC)
            SON: SO_0958(ahpC)
            SDN: Sden_2091 Sden_3012
            SFR: Sfri_0522 Sfri_1455
            SHN: Shewana3_2541 Shewana3_3325
            ILO: IL1803(ahpC) IL2576
            CPS: CPS_3474 CPS_4717(ahpC)
            PHA: PSHAa0839(ahpCB) PSHAb0265(ahpC)
            PAT: Patl_1066 Patl_1398
            CBU: CBU_1477 CBU_1706
            CBD: COXBU7E912_1085 COXBU7E912_1367
            LPN: lpg2350 lpg2965
            LPF: lpl2272 lpl2895(ahpC)
            LPP: lpp2299 lpp3037(ahpC)
            MCA: MCA1023
            FTA: FTA_1070
            TCX: Tcr_0139 Tcr_1387
            HCH: HCH_04994
            ABO: ABO_2431(ahpC)
            MMW: Mmwyl1_3890
            AHA: AHA_0894 AHA_1732 AHA_2406
            DNO: DNO_0143(ahpC)
            CRP: CRP_112
            RSO: RSc1646(ahpC2) RSp0245(ahpC1)
            REU: Reut_A1365
            RME: Rmet_1950
            BMA: BMA1487 BMAA1786(ahpC)
            BMV: BMASAVP1_0779(ahpC)
            BML: BMA10299_1072(ahpC)
            BMN: BMA10247_A2046(ahpC)
            BXE: Bxe_A2911
            BUR: Bcep18194_A5251
            BAM: Bamb_1928
            BPS: BPSL2096 BPSS0492(ahpC)
            BPM: BURPS1710b_2509(ahpC) BURPS1710b_A2045(ahpC)
            BPL: BURPS1106A_1364 BURPS1106A_A0667(ahpC)
            BPD: BURPS668_1358
            BTE: BTH_I2092 BTH_II1926
            BPE: BP3552(ahpC)
            BPA: BPP3361(ahpC)
            BBR: BB3812(ahpC)
            RFR: Rfer_2234
            POL: Bpro_3044
            MPT: Mpe_A2095
            HAR: HEAR0029(ahpC) HEAR0287(hyr1)
            NEU: NE2465
            NET: Neut_2366
            NMU: Nmul_A2387
            EBA: ebA4399(ahpC)
            DAR: Daro_0563 Daro_3517
            MFA: Mfla_1197 Mfla_1689
            HPY: HP0136(bcp) HP1563(tsaA)
            HPJ: jhp0124(bcp) jhp1471(tsaA)
            HPA: HPAG1_1512
            HHE: HH1544(tsaA)
            HAC: Hac_1670(ahpC)
            WSU: WS1744(ahpC1) WS1995(ahpC)
            TDN: Tmden_1778
            CJE: Cj0334(ahpC)
            CJR: CJE0379
            CJU: C8J_0311(ahpC)
            CCV: CCV52592_0858
            CHA: CHAB381_1011
            CCO: CCC13826_0985 CCC13826_2112
            NIS: NIS_0392
            SUN: SUN_0752 SUN_1284
            DDE: Dde_2560
            BBA: Bd2517(ahpC)
            ADE: Adeh_0313
            MXA: MXAN_1564(ahpC)
            SAT: SYN_00591 SYN_03096 SYN_03642 SYN_03680
            RPR: RP327(tdpX1)
            RTY: RT0318(tdpX1)
            RCO: RC0451(tdpX1)
            RFE: RF_0532(tdpX1)
            OTS: OTBS_0544(bcp)
            WOL: WD0756
            WBM: Wbm0567
            AMA: AM511(tdpX1)
            APH: APH_0659
            ERU: Erum3480
            ERW: ERWE_CDS_03550(tsaA)
            ERG: ERGA_CDS_03510(tsaA)
            ECN: Ecaj_0332
            ECH: ECH_0734
            NSE: NSE_0559
            SMD: Smed_2381
            BME: BMEII0577
            BMF: BAB2_0531(ahpC)
            BMS: BRA0708(ahpC)
            BMB: BruAb2_0522(ahpC)
            BJA: bll1777(ahpC)
            BRA: BRADO3235 BRADO4472 BRADO5376 BRADO6585
            BBT: BBta_0951 BBta_4691 BBta_4916 BBta_5863
            RPB: RPB_4601
            RPC: RPC_4443
            RPE: RPE_4513
            BBK: BARBAKC583_0053
            XAU: Xaut_4220
            CCR: CC_2918
            MMR: Mmar10_2887
            HNE: HNE_2627(bcp) HNE_3035(ahpC)
            ZMO: ZMO1732(ahpC)
            NAR: Saro_1717
            SAL: Sala_0629
            SWI: Swit_3741 Swit_3743
            ELI: ELI_10450
            GOX: GOX0574 GOX1332
            GBE: GbCGDNIH1_0680 GbCGDNIH1_0841 GbCGDNIH1_0865 GbCGDNIH1_1878
            MAG: amb0664
            MGM: Mmc1_1679
            ABA: Acid345_4100
            BSU: BG11385(ahpC)
            BAN: BA0345(ahpC)
            BAR: GBAA0345(ahpC)
            BAA: BA_0916
            BAT: BAS0330
            BCE: BC0377
            BCA: BCE_0440(ahpC)
            BCZ: BCZK0317(ahpC)
            BCY: Bcer98_0315
            BTK: BT9727_0314(ahpC)
            BLI: BL00200(ahpC)
            BLD: BLi04291(ahpC)
            BAY: RBAM_036960
            BPU: BPUM_0826(ygaF) BPUM_1319(ykuU) BPUM_3690
            GKA: GK2575
            SAU: SA0366(ahpC)
            SAV: SAV0381(ahpC)
            SAM: MW0357(ahpC)
            SAR: SAR0399(ahpC)
            SAS: SAS0358
            SAC: SACOL0452(ahpC)
            SAB: SAB0331c(ahpC)
            SAO: SAOUHSC_00365
            SAJ: SaurJH9_0429 SaurJH9_1364 SaurJH9_2644
            SAH: SaurJH1_0440 SaurJH1_1390 SaurJH1_2699
            SEP: SE2357
            SER: SERP0060(ahpC)
            SHA: SH2592(ahpC)
            SSP: SSP2333
            LLA: L135351(ahpC)
            LLC: LACR_0383
            SPY: SPy_2079(ahpC)
            SPZ: M5005_Spy_1768(ahpC)
            SPM: spyM18_2137(ahpC)
            SPG: SpyM3_1770(ahpC)
            SPS: SPs1767
            SPH: MGAS10270_Spy1834(ahpC)
            SPI: MGAS10750_Spy1860(ahpC)
            SPJ: MGAS2096_Spy1801(ahpC)
            SPK: MGAS9429_Spy1778(ahpC)
            SPA: M6_Spy1765
            SPB: M28_Spy1752(ahpC)
            SAG: SAG1833(ahpC)
            SAN: gbs1874
            SAK: SAK_1853(ahpC)
            SMU: SMU.764(ahpC)
            LSL: LSL_1686
            LBR: LVIS_0086
            LCA: LSEI_2506
            LRE: Lreu_1072
            EFA: EF2739(ahpC)
            CPE: CPE0782
            CPF: CPF_0784(ahpC)
            CTC: CTC00894
            CBE: Cbei_2135
            CKL: CKL_0363(ahpC)
            DSY: DSY0524
            TTE: TTE0270(ahpC) TTE2186(ahpC2)
            MMO: MMOB5230(ahpC)
            MTU: Rv2238c(ahpE) Rv2428(ahpC)
            MTC: MT2298 MT2503(ahpC)
            MBO: Mb2262c(ahpE) Mb2454(ahpC)
            MLE: ML2042(ahpC)
            MPA: MAP1589c(ahpC) MAP1991c(ahpE)
            MAV: MAV_3178
            MSM: MSMEG_4320 MSMEG_4753 MSMEG_4891 MSMEG_6683
            CDI: DIP1420(dirA)
            CJK: jk0155(ahpC)
            NFA: nfa37890(ahpC)
            SCO: SCO5032(ahpC)
            SMA: SAV3232(ahpC)
            AAU: AAur_2517(bcp) AAur_3512(bcp)
            PAC: PPA1989
            SEN: SACE_1534(ahpE)
            BLO: BL0615(ahpC)
            FNU: FN1983
            CTR: CT603(ahpC)
            CTA: CTA_0654(ahpC)
            CMU: TC0892
            CPN: CPn0778(ahpC)
            CPA: CP1094
            CPJ: CPj0778(ahpC)
            CPT: CpB0806
            CCA: CCA00979
            CAB: CAB948
            CFE: CF0034(ahpC)
            PCU: pc0024(ahpC)
            TPA: TP0509
            TDE: TDE0011
            SYN: sll1621
            SYG: sync_2508(bcp-2)
            SYR: SynRCC307_0386
            PMB: A9601_10131(ahpC)
            PMC: P9515_09331(ahpC)
            PMF: P9303_14621(ahpC) P9303_19011
            PMG: P9301_10121(ahpC)
            PMH: P9215_10441
            PME: NATL1_10331(ahpC) NATL1_16391
            BTH: BT_2812
            BFR: BF1259 BF2266
            BFS: BF1210(ahpC) BF2360
            PGI: PG0618
            CHU: CHU_2724(ahpC) CHU_3760(ahpC)
            GFO: GFO_1783(bcp)
            FPS: FP0702 FP0914 FP1100 FP1729 FP1790
            CTE: CT1492 CT1747
            CCH: Cag_1980
            PLT: Plut_1493
            DET: DET1581
            DEH: cbdb_A1669(ahpC)
            DEB: DehaBAV1_1330
            AAE: aq_486(ahpC1) aq_858(ahpC2)
            TMA: TM0807
            TME: Tmel_1196
            FNO: Fnod_1445
            MJA: MJ0736
            MMP: MMP1174
            MAC: MA4103(ahpC)
            MBA: Mbar_A0479
            MMA: MM_0814
            MTH: MTH159
            AFU: AF0270
            TAC: Ta0473
            TVO: TVN1099
            PTO: PTO0377 PTO0727 PTO1522
            PHO: PH1217
            PAB: PAB1673
            PFU: PF0722 PF1033
            TKO: TK0537
            RCI: LRC46(prx1-2) RCIX1144(prx2-1) RCIX1399(prx1-1)
                 RCIX2514(prx2-2) RCIX2524(prx2-3)
            APE: APE_2278
            SSO: SSO2121(bcp-2)
            STO: ST0584 ST2442
            NEQ: NEQ191
STRUCTURES  PDB: 1X0R  1ZOF  1ZYE  2A4V  2BMX  2CX3  2CX4  2PN8  
DBLINKS     IUBMB Enzyme Nomenclature: 1.11.1.15
            ExPASy - ENZYME nomenclature database: 1.11.1.15
            ExplorEnz - The Enzyme Database: 1.11.1.15
            ERGO genome analysis and discovery system: 1.11.1.15
            BRENDA, the Enzyme Database: 1.11.1.15
///
ENTRY       EC 1.11.1.16                Enzyme
NAME        versatile peroxidase;
            VP;
            hybrid peroxidase;
            polyvalent peroxidase
CLASS       Oxidoreductases;
            Acting on a peroxide as acceptor;
            Peroxidases
SYSNAME     reactive-black-5:hydrogen-peroxide oxidoreductase
REACTION    (1) Reactive Black 5 + H2O2 = oxidized Reactive Black 5 + 2 H2O
            [RN:R07612];
            (2) donor + H2O2 = oxidized donor + 2 H2O [RN:R03532]
ALL_REAC    R03532 R07612
SUBSTRATE   Reactive Black 5 [CPD:C16001];
            H2O2 [CPD:C00027];
            donor [CPD:C01351]
PRODUCT     oxidized Reactive Black 5 [CPD:C16002];
            H2O [CPD:C00001];
            oxidized donor [CPD:C02177]
COMMENT     A hemoprotein. This ligninolytic peroxidase combines the
            substrate-specificity characteristics of the two other ligninolytic
            peroxidases, EC 1.11.1.13, manganese peroxidase and EC 1.11.1.14,
            lignin peroxidase. It is also able to oxidize phenols, hydroquinones
            and both low- and high-redox-potential dyes, due to a hybrid
            molecular architecture that involves multiple binding sites for
            substrates [2,4].
REFERENCE   1  [PMID:8647081]
  AUTHORS   Martinez MJ, Ruiz-Duenas FJ, Guillen F, Martinez AT.
  TITLE     Purification and catalytic properties of two manganese peroxidase
            isoenzymes from Pleurotus eryngii.
  JOURNAL   Eur. J. Biochem. 237 (1996) 424-32.
  ORGANISM  Pleurotus eryngii
REFERENCE   2  [PMID:9654123]
  AUTHORS   Heinfling A, Ruiz-Duenas FJ, Martinez MJ, Bergbauer M, Szewzyk U,
            Martinez AT.
  TITLE     A study on reducing substrates of manganese-oxidizing peroxidases
            from Pleurotus eryngii and Bjerkandera adusta.
  JOURNAL   FEBS. Lett. 428 (1998) 141-6.
  ORGANISM  Pleurotus eryngii, Bjerkandera adusta
REFERENCE   3  [PMID:9987124]
  AUTHORS   Ruiz-Duenas FJ, Martinez MJ, Martinez AT.
  TITLE     Molecular characterization of a novel peroxidase isolated from the
            ligninolytic fungus Pleurotus eryngii.
  JOURNAL   Mol. Microbiol. 31 (1999) 223-35.
  ORGANISM  Pleurotus eryngii
REFERENCE   4  [PMID:10187820]
  AUTHORS   Camarero S, Sarkar S, Ruiz-Duenas FJ, Martinez MJ, Martinez AT.
  TITLE     Description of a versatile peroxidase involved in the natural
            degradation of lignin that has both manganese peroxidase and lignin
            peroxidase substrate interaction sites.
  JOURNAL   J. Biol. Chem. 274 (1999) 10324-30.
  ORGANISM  Pleurotus eryngii, Phanerochaete chrysosporium
REFERENCE   5  [PMID:10508113]
  AUTHORS   Ruiz-Duenas FJ, Martinez MJ, Martinez AT.
  TITLE     Heterologous expression of Pleurotus eryngii peroxidase confirms its
            ability to oxidize Mn(2+) and different aromatic substrates.
  JOURNAL   Appl. Environ. Microbiol. 65 (1999) 4705-7.
  ORGANISM  Pleurotus eryngii
REFERENCE   6  [PMID:11004397]
  AUTHORS   Camarero S, Ruiz-Duenas FJ, Sarkar S, Martinez MJ, Martinez AT.
  TITLE     The cloning of a new peroxidase found in lignocellulose cultures of
            Pleurotus eryngii and sequence comparison with other fungal
            peroxidases.
  JOURNAL   FEMS. Microbiol. Lett. 191 (2000) 37-43.
  ORGANISM  Pleurotus eryngii
REFERENCE   7  [PMID:11356138]
  AUTHORS   Ruiz-Duenas FJ, Camarero S, Perez-Boada M, Martinez MJ, Martinez AT.
  TITLE     A new versatile peroxidase from Pleurotus.
  JOURNAL   Biochem. Soc. Trans. 29 (2001) 116-22.
  ORGANISM  Pleurotus eryngii, Bjerkandera adusta, Phanerochaete chrysosporium
REFERENCE   8  [PMID:12884090]
  AUTHORS   Banci L, Camarero S, Martinez AT, Martinez MJ, Perez-Boada M,
            Pierattelli R, Ruiz-Duenas FJ.
  TITLE     NMR study of manganese(II) binding by a new versatile peroxidase
            from the white-rot fungus Pleurotus eryngii.
  JOURNAL   J. Biol. Inorg. Chem. 8 (2003) 751-60.
  ORGANISM  Pleurotus eryngii
REFERENCE   9  [PMID:16246366]
  AUTHORS   Perez-Boada M, Ruiz-Duenas FJ, Pogni R, Basosi R, Choinowski T,
            Martinez MJ, Piontek K, Martinez AT.
  TITLE     Versatile peroxidase oxidation of high redox potential aromatic
            compounds: site-directed mutagenesis, spectroscopic and
            crystallographic investigation of three long-range electron transfer
            pathways.
  JOURNAL   J. Mol. Biol. 354 (2005) 385-402.
  ORGANISM  Pleurotus eryngii
REFERENCE   10 [PMID:10049842]
  AUTHORS   Caramelo L, Martinez MJ, Martinez AT.
  TITLE     A search for ligninolytic peroxidases in the fungus pleurotus
            eryngii involving alpha-keto-gamma-thiomethylbutyric acid and lignin
            model dimers
  JOURNAL   Appl. Environ. Microbiol. 65 (1999) 916-22.
DBLINKS     IUBMB Enzyme Nomenclature: 1.11.1.16
            ExPASy - ENZYME nomenclature database: 1.11.1.16
            ExplorEnz - The Enzyme Database: 1.11.1.16
            ERGO genome analysis and discovery system: 1.11.1.16
            BRENDA, the Enzyme Database: 1.11.1.16
///
ENTRY       EC 1.12.1.1       Obsolete  Enzyme
NAME        Transferred to 1.12.7.2
CLASS       Oxidoreductases;
            Acting on hydrogen as donor;
            With NAD+ or NADP+ as acceptor
COMMENT     Transferred entry: now EC 1.12.7.2, ferredoxin hydrogenase (EC
            1.12.1.1 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.12.1.1
            ExPASy - ENZYME nomenclature database: 1.12.1.1
            ExplorEnz - The Enzyme Database: 1.12.1.1
            ERGO genome analysis and discovery system: 1.12.1.1
            BRENDA, the Enzyme Database: 1.12.1.1
///
ENTRY       EC 1.12.1.2                 Enzyme
NAME        hydrogen dehydrogenase;
            H2:NAD+ oxidoreductase;
            NAD+-linked hydrogenase;
            bidirectional hydrogenase;
            hydrogenase
CLASS       Oxidoreductases;
            Acting on hydrogen as donor;
            With NAD+ or NADP+ as acceptor
SYSNAME     hydrogen:NAD+ oxidoreductase
REACTION    H2 + NAD+ = H+ + NADH [RN:R00700]
ALL_REAC    R00700;
            (other) R07181
SUBSTRATE   H2 [CPD:C00282];
            NAD+ [CPD:C00003]
PRODUCT     H+ [CPD:C00080];
            NADH [CPD:C00004]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023];
            FMN [CPD:C00061];
            Flavin [CPD:C00176];
            Nickel [CPD:C00291];
            Iron-sulfur [CPD:C00824]
COMMENT     An iron-sulfur flavoprotein (FMN or FAD). Some forms of this enzyme
            contain nickel.
REFERENCE   1  [PMID:13968752]
  AUTHORS   BONE DH, BERNSTEIN S, VISHNIAC W.
  TITLE     Purification and some properties of different forms of hydrogen
            dehydrogenase.
  JOURNAL   Biochim. Biophys. Acta. 67 (1963) 581-8.
  ORGANISM  Pseudomonas saccharophila, Hydrogemonas ruhlandii
REFERENCE   2  [PMID:186126]
  AUTHORS   Schneider K, Schlegel HG.
  TITLE     Purification and properties of soluble hydrogenase from Alcaligenes
            eutrophus H 16.
  JOURNAL   Biochim. Biophys. Acta. 452 (1976) 66-80.
  ORGANISM  Alcaligenes eutrophus
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
            PATH: map00680  Methane metabolism
ORTHOLOGY   KO: K00436  hydrogen dehydrogenase
GENES       PIN: Ping_1216 Ping_1217
            MCA: MCA0114 MCA2724 MCA2725
            BUR: Bcep18194_A4144 Bcep18194_A4146
            BAM: Bamb_0897
            HAR: HEAR0358 HEAR3432
            NMU: Nmul_A1670 Nmul_A1671 Nmul_A1672
            AZO: azo1412(hoxF)
            DAR: Daro_0980 Daro_0982
            GSU: GSU2718(hoxH) GSU2719(hoxY) GSU2720(hoxU) GSU2721(hoxF)
            SFU: Sfum_1791
            SUS: Acid_5017
            MVA: Mvan_4114 Mvan_4115 Mvan_4116
            AVA: Ava_4657 Ava_4659 Ava_4661
            PMB: A9601_00341(dhsS)
            PMC: P9515_00341(dhsS)
            PMF: P9303_00431(dhsS)
            PMG: P9301_00341(dhsS)
            PME: NATL1_00331(dhsS)
            CCH: Cag_0244 Cag_0245
            HWA: HQ1128A(hoxF)
DBLINKS     IUBMB Enzyme Nomenclature: 1.12.1.2
            ExPASy - ENZYME nomenclature database: 1.12.1.2
            ExplorEnz - The Enzyme Database: 1.12.1.2
            ERGO genome analysis and discovery system: 1.12.1.2
            BRENDA, the Enzyme Database: 1.12.1.2
            CAS: 9027-05-8
///
ENTRY       EC 1.12.1.3                 Enzyme
NAME        hydrogen dehydrogenase (NADP+);
            NADP+-linked hydrogenase;
            NADP+-reducing hydrogenase;
            hydrogen dehydrogenase (NADP+);
            hydrogenase [ambiguous]
CLASS       Oxidoreductases;
            Acting on hydrogen as donor;
            With NAD+ or NADP+ as acceptor
SYSNAME     hydrogen:NADP+ oxidoreductase
REACTION    H2 + NADP+ = H+ + NADPH
SUBSTRATE   H2 [CPD:C00282];
            NADP+ [CPD:C00006]
PRODUCT     H+ [CPD:C00080];
            NADPH [CPD:C00005]
COMMENT     An iron-sulfur flavoprotein.
REFERENCE   1  [PMID:9703971]
  AUTHORS   de Luca G, de Philip P, Rousset M, Belaich JP, Dermoun Z.
  TITLE     The NADP-reducing hydrogenase of Desulfovibrio fructosovorans:
            evidence for a native complex with hydrogen-dependent
            methyl-viologen-reducing activity.
  JOURNAL   Biochem. Biophys. Res. Commun. 248 (1998) 591-6.
  ORGANISM  Desulfovibrio fructosovorans
STRUCTURES  PDB: 2AUV  
DBLINKS     IUBMB Enzyme Nomenclature: 1.12.1.3
            ExPASy - ENZYME nomenclature database: 1.12.1.3
            ExplorEnz - The Enzyme Database: 1.12.1.3
            ERGO genome analysis and discovery system: 1.12.1.3
            BRENDA, the Enzyme Database: 1.12.1.3
            CAS: 9027-05-8
///
ENTRY       EC 1.12.2.1                 Enzyme
NAME        cytochrome-c3 hydrogenase;
            H2:ferricytochrome c3 oxidoreductase;
            cytochrome c3 reductase;
            cytochrome hydrogenase;
            hydrogenase [ambiguous]
CLASS       Oxidoreductases;
            Acting on hydrogen as donor;
            With a cytochrome as acceptor
SYSNAME     hydrogen:ferricytochrome-c3 oxidoreductase
REACTION    2 H2 + ferricytochrome c3 = 4 H+ + ferrocytochrome c3 [RN:R04015]
ALL_REAC    R04015
SUBSTRATE   H2 [CPD:C00282];
            ferricytochrome c3 [CPD:C02682]
PRODUCT     H+ [CPD:C00080];
            ferrocytochrome c3 [CPD:C02684]
COFACTOR    Iron [CPD:C00023];
            Nickel [CPD:C00291];
            Iron-sulfur [CPD:C00824]
COMMENT     An iron-sulfur protein. Some forms of the enzyme contain nickel
            ([NiFe]-hydrogenases) and, of these, some contain selenocysteine
            ([NiFeSe]-hydrogenases). Methylene blue and other acceptors can also
            be reduced.
REFERENCE   1
  AUTHORS   DerVartanian, D.V. and Le Gall, J.
  TITLE     A monomolecular electron transfer chain: structure and function of
            cytochrome c3.
  JOURNAL   Biochim. Biophys. Acta 346 (1974) 79-99.
  ORGANISM  Desulfovibrio vulgaris, Desulfovibrio desulfuricans [GN:dde],
            Desulfovibrio gigas
REFERENCE   2  [PMID:3546297]
  AUTHORS   Higuchi Y, Yasuoka N, Kakudo M, Katsube Y, Yagi T, Inokuchi H.
  TITLE     Single crystals of hydrogenase from Desulfovibrio vulgaris Miyazaki
            F.
  JOURNAL   J. Biol. Chem. 262 (1987) 2823-5.
  ORGANISM  Desulfovibrio vulgaris
REFERENCE   3
  AUTHORS   Rilkis, E. and Rittenberg, D.
  TITLE     Some observations on the enzyme, hydrogenase.
  JOURNAL   J. Biol. Chem. 236 (1961) 2526-2529.
  ORGANISM  Desulfovibrio desulfuricans [GN:dde]
REFERENCE   4
  AUTHORS   Sadana, J.C. and Morey, A.V.
  TITLE     Purification and properties of the hydrogenase of Desulfovibrio
            desulfuricans.
  JOURNAL   Biochim. Biophys. Acta 50 (1961) 153-163.
  ORGANISM  Desulfovibrio desulfuricans [GN:dde]
REFERENCE   5  [PMID:7854413]
  AUTHORS   Volbeda A, Charon MH, Piras C, Hatchikian EC, Frey M,
            Fontecilla-Camps JC.
  TITLE     Crystal structure of the nickel-iron hydrogenase from Desulfovibrio
            gigas.
  JOURNAL   Nature. 373 (1995) 580-7.
  ORGANISM  Desulfovibrio gigas
REFERENCE   6  [PMID:10378275]
  AUTHORS   Garcin E, Vernede X, Hatchikian EC, Volbeda A, Frey M,
            Fontecilla-Camps JC.
  TITLE     The crystal structure of a reduced [NiFeSe] hydrogenase provides an
            image of the activated catalytic center.
  JOURNAL   Structure. 7 (1999) 557-66.
  ORGANISM  Desulfovibrio gigas
ORTHOLOGY   KO: K00437  cytochrome-c3 hydrogenase
GENES       MCA: MCA2726
            DAR: Daro_0981
            ABU: Abu_1437(hupS)
            DVL: Dvul_0719 Dvul_1246
            CNO: NT01CX_0257
            PAB: PAB0638(hydB-2) PAB0640(hydD-2) PAB1784
STRUCTURES  PDB: 1FRV  1H2R  1UBH  1UBJ  1UBK  1UBL  1UBM  1UBO  1UBR  1UBT  
                 1UBU  1WUH  1WUI  1WUJ  1WUK  1WUL  1YQ9  1YQW  1YRQ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.12.2.1
            ExPASy - ENZYME nomenclature database: 1.12.2.1
            ExplorEnz - The Enzyme Database: 1.12.2.1
            ERGO genome analysis and discovery system: 1.12.2.1
            UM-BBD (Biocatalysis/Biodegradation Database): 1.12.2.1
            BRENDA, the Enzyme Database: 1.12.2.1
            CAS: 9027-05-8
///
ENTRY       EC 1.12.5.1                 Enzyme
NAME        hydrogen:quinone oxidoreductase;
            hydrogen-ubiquinone oxidoreductase;
            hydrogen:menaquinone oxidoreductase;
            membrane-bound hydrogenase;
            quinone-reactive Ni/Fe-hydrogenase
CLASS       Oxidoreductases;
            Acting on hydrogen as donor;
            With a quinone or similar compound as acceptor
SYSNAME     hydrogen:quinone oxidoreductase
REACTION    H2 + menaquinone = menaquinol [RN:R02965]
ALL_REAC    R02965
SUBSTRATE   H2 [CPD:C00282];
            menaquinone [CPD:C00828]
PRODUCT     menaquinol [CPD:C05819]
COMMENT     Contains nickel, iron-sulfur clusters and cytochrome b. Also
            catalyses the reduction of water-soluble quinones (e.g.
            2,3-dimethylnaphthoquinone) or viologen dyes (benzyl viologen or
            methyl viologen).
REFERENCE   1  [PMID:1587288]
  AUTHORS   Dross F, Geisler V, Lenger R, Theis F, Krafft T, Fahrenholz F, Kojro
            E, Duchene A, Tripier D, Juvenal K, et al.
  TITLE     The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes.
  JOURNAL   Eur. J. Biochem. 206 (1992) 93-102.
  ORGANISM  Wolinella succinogenes [GN:wsu]
REFERENCE   2  [PMID:8319698]
  AUTHORS   Dross F, Geisler V, Lenger R, Theis F, Krafft T, Fahrenholz F, Kojro
            E, Duchene A, Tripier D, Juvenal K, et al.
  TITLE     The quinone-reactive Ni/Fe-hydrogenase of Wolinella Succinogenes.
  JOURNAL   Eur. J. Biochem. 214 (1993) 949-50.
REFERENCE   3  [PMID:9822828]
  AUTHORS   Gross R, Simon J, Lancaster CR, Kroger A.
  TITLE     Identification of histidine residues in Wolinella succinogenes
            hydrogenase that are essential for menaquinone reduction by H2.
  JOURNAL   Mol. Microbiol. 30 (1998) 639-46.
  ORGANISM  Wolinella succinogenes [GN:wsu]
REFERENCE   4  [PMID:9310376]
  AUTHORS   Bernhard M, Benelli B, Hochkoeppler A, Zannoni D, Friedrich B.
  TITLE     Functional and structural role of the cytochrome b subunit of the
            membrane-bound hydrogenase complex of Alcaligenes eutrophus H16.
  JOURNAL   Eur. J. Biochem. 248 (1997) 179-86.
  ORGANISM  Alcaligenes eutrophus
REFERENCE   5  [PMID:8354459]
  AUTHORS   Ferber DM, Maier RJ.
  TITLE     Hydrogen-ubiquinone oxidoreductase activity by the Bradyrhizobium
            japonicum membrane-bound hydrogenase.
  JOURNAL   FEMS. Microbiol. Lett. 110 (1993) 257-64.
  ORGANISM  Bradyrhizobium japonicum [GN:bja]
REFERENCE   6
  AUTHORS   Ishii, M., Omori, T., Igarashi, Y., Adachi, O., Ameyama, M. and
            Kodama, T.
  TITLE     Methionaquinone is a direct natural electron-acceptor for the
            membrane-bound hydrogenase in Hydrogenobacter thermophilus strain
            TK-6.
  JOURNAL   Agric. Biol. Chem. 55 (1991) 3011-3016.
  ORGANISM  Hydrogenobacter thermophilus
ORTHOLOGY   KO: K05911  quinone-reactive Ni/Fe-hydrogenase
            KO: K05922  quinone-reactive Ni/Fe-hydrogenase large subunit
            KO: K05927  quinone-reactive Ni/Fe-hydrogenase small subunit
GENES       SON: SO_2098(hyaB) SO_2099(hoxK)
            SFR: Sfri_2103 Sfri_2104
            SAZ: Sama_1679
            SBL: Sbal_1889
            SBM: Shew185_1915
            SLO: Shew_1765
            SPC: Sputcn32_2088
            SSE: Ssed_1908
            SPL: Spea_2033
            SHE: Shewmr4_1821 Shewmr4_1822
            SHM: Shewmr7_2155 Shewmr7_2156
            SHN: Shewana3_1879 Shewana3_1880
            SHW: Sputw3181_1924
            RFR: Rfer_4121
            HPY: HP0631(hydA) HP0632(hydB)
            HPJ: jhp0574(hyaA) jhp0575(hyaB)
            HPA: HPAG1_0614 HPAG1_0615
            HHE: HH0056(hyaA) HH0057(hyaB) HH0198
            HAC: Hac_0744(hyaA) Hac_0745(hyaB)
            WSU: WS1686 WS1687(hydA)
            TDN: Tmden_1435 Tmden_1436
            CJE: Cj1266c(hydB) Cj1267c(hydA) Cj1399c(hydA2)
            CJR: CJE1402(hydB) CJE1403(hydA) CJE1586
            CJJ: CJJ81176_1281(hydC) CJJ81176_1282(hydB) CJJ81176_1283(hydA)
            CJU: C8J_1210(hydB) C8J_1211(hydA) C8J_1313(hydA2)
            CJD: JJD26997_0458(hydA) JJD26997_0459(hydB) JJD26997_0460(hydC)
            CFF: CFF8240_0939 CFF8240_0940
            CCV: CCV52592_1902
            CHA: CHAB381_0861 CHAB381_0862
            ABU: Abu_1427(hydB) Abu_1428(hydA) Abu_1434(hyaB) Abu_1435(hyaA)
            GSU: GSU0122 GSU0123
            GME: Gmet_3331 Gmet_3332
            BRA: BRADO1683(hupV)
            BBT: BBta_1995(hupV)
            RPE: RPE_1230
            RSH: Rsph17029_2144
            MAG: amb1114 amb1115
            SUS: Acid_6556
            MSM: MSMEG_2262(hybA) MSMEG_2263(hybC) MSMEG_2719
            MVA: Mvan_2366
            MMC: Mmcs_2143
            MKM: Mkms_2189
            MJL: Mjls_2130
            FRA: Francci3_1076 Francci3_1077(hydA)
            TER: Tery_3368
DBLINKS     IUBMB Enzyme Nomenclature: 1.12.5.1
            ExPASy - ENZYME nomenclature database: 1.12.5.1
            ExplorEnz - The Enzyme Database: 1.12.5.1
            ERGO genome analysis and discovery system: 1.12.5.1
            BRENDA, the Enzyme Database: 1.12.5.1
            CAS: 147097-29-8
///
ENTRY       EC 1.12.7.1       Obsolete  Enzyme
NAME        Transferred to 1.12.7.2
CLASS       Oxidoreductases;
            Acting on hydrogen as donor;
            With an iron-sulfur protein as acceptor
COMMENT     Transferred entry: now EC 1.12.7.2, ferredoxin hydrogenase (EC
            1.12.7.1 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 1.12.7.1
            ExPASy - ENZYME nomenclature database: 1.12.7.1
            ExplorEnz - The Enzyme Database: 1.12.7.1
            ERGO genome analysis and discovery system: 1.12.7.1
            BRENDA, the Enzyme Database: 1.12.7.1
///
ENTRY       EC 1.12.7.2                 Enzyme
NAME        ferredoxin hydrogenase;
            H2 oxidizing hydrogenase;
            H2 producing hydrogenase [ambiguous];
            bidirectional hydrogenase;
            hydrogen-lyase [ambiguous];
            hydrogenase (ferredoxin);
            hydrogenase I;
            hydrogenase II;
            hydrogenlyase [ambiguous];
            uptake hydrogenase [ambiguous]
CLASS       Oxidoreductases;
            Acting on hydrogen as donor;
            With an iron-sulfur protein as acceptor
SYSNAME     hydrogen:ferredoxin oxidoreductase
REACTION    H2 + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H+ [RN:R00019]
ALL_REAC    R00019
SUBSTRATE   H2 [CPD:C00282];
            oxidized ferredoxin [CPD:C00139]
PRODUCT     reduced ferredoxin [CPD:C00138];
            H+ [CPD:C00080]
COFACTOR    Iron [CPD:C00023];
            Sulfur [CPD:C00087];
            Nickel [CPD:C00291]
COMMENT     Contains iron-sulfur clusters. The enzymes from some sources
            contains nickel. Can use molecular hydrogen for the reduction of a
            variety of substances.
REFERENCE   1
  AUTHORS   Shug, A.L., Wilson, P.W., Green, D.E. and Mahler, H.R.
  TITLE     The role of molybdenum and flavin in hydrogenase.
  JOURNAL   J. Am. Chem. Soc. 76 (1954) 3355-3356.
  ORGANISM  Clostridium pasteurianum
REFERENCE   2
  AUTHORS   Tagawa, K. and Arnon, D.I.
  TITLE     Ferredoxin as electron carriers in photosynthesis and in the
            bioogical production and consumption of hydrogen gas.
  JOURNAL   Nature (Lond.) 195 (1962) 537-543.
REFERENCE   3
  AUTHORS   Valentine, R.C., Mortenson, L.E. and Carnahan, J.E.
  TITLE     The hydrogenase system of Clostridium pasteurianum.
  JOURNAL   J. Biol. Chem. 238 (1963) 1141-1144.
  ORGANISM  Clostridium pasteurianum
REFERENCE   4  [PMID:164247]
  AUTHORS   Zumft WG, Mortenson LE.
  TITLE     The nitrogen-fixing complex of bacteria.
  JOURNAL   Biochim. Biophys. Acta. 416 (1975) 1-52.
  ORGANISM  Clostridium pasteurianum
REFERENCE   5  [PMID:2173950]
  AUTHORS   Adams MW.
  TITLE     The structure and mechanism of iron-hydrogenases.
  JOURNAL   Biochim. Biophys. Acta. 1020 (1990) 115-45.
  ORGANISM  Clostridium pasteurianum, Megasphaera elsdenii, Desulfovibrio
            vulgaris
REFERENCE   6  [PMID:9836629]
  AUTHORS   Peters JW, Lanzilotta WN, Lemon BJ, Seefeldt LC.
  TITLE     X-ray crystal structure of the Fe-only hydrogenase (CpI) from
            Clostridium pasteurianum to 1.8 angstrom resolution.
  JOURNAL   Science. 282 (1998) 1853-8.
  ORGANISM  Clostridium pasteurianum
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
            PATH: map00680  Methane metabolism
ORTHOLOGY   KO: K00532  ferredoxin hydrogenase
            KO: K00533  ferredoxin hydrogenase large subunit
            KO: K00534  ferredoxin hydrogenase small subunit
            KO: K06441  ferredoxin hydrogenase gamma subunit
GENES       AFM: AFUA_4G11960
            TPV: TP03_0164
            TET: TTHERM_00198090
            EHI: 131.t00027
            ECI: UTI89_C3075(hydN)
            YEN: YE3606(hybC) YE3609(hyb0)
            SON: SO_3920(hydA) SO_3921(hydB)
            SHE: Shewmr4_3250
            SHN: Shewana3_0710 Shewana3_0711 Shewana3_3459
            RFR: Rfer_4120
            MPT: Mpe_A2807
            AZO: azo3786(hupS)
            DAR: Daro_3961(hupU)
            PCA: Pcar_2502
            DVU: DVU1769(hydA) DVU1770(hydB) DVU1771(hydC) DVU1917(hysB)
                 DVU1918(hysA) DVU1921(hynB-1) DVU2525(hynB-2) DVU2526(hynA-2)
            DVL: Dvul_1385 Dvul_1386
            DDE: Dde_0081 Dde_0082 Dde_0475 Dde_2280 Dde_2281 Dde_3755(hydA)
                 Dde_3756
            DPS: DP0159 DP0160 DP0479
            SFU: Sfum_0847 Sfum_0848
            BJA: bll6944(hupU)
            RPA: RPA0134(hydC) RPA0959(hupU)
            RPE: RPE_1229 RPE_3860
            RSP: RSP_0492(hupU)
            RRU: Rru_A0310
            CPR: CPR_0261 CPR_0938 CPR_2341(hydA)
            CTC: CTC02417
            CNO: NT01CX_0464 NT01CX_1006 NT01CX_1699 NT01CX_2259
            CTH: Cthe_3003
            CDF: CD3314(hydA)
            CBE: Cbei_0327 Cbei_3796 Cbei_4000
            CKL: CKL_2257
            CHY: CHY_1545
            SWO: Swol_1925
            MTA: Moth_1883
DBLINKS     IUBMB Enzyme Nomenclature: 1.12.7.2
            ExPASy - ENZYME nomenclature database: 1.12.7.2
            ExplorEnz - The Enzyme Database: 1.12.7.2
            ERGO genome analysis and discovery system: 1.12.7.2
            UM-BBD (Biocatalysis/Biodegradation Database): 1.12.7.2
            BRENDA, the Enzyme Database: 1.12.7.2
            CAS: 9080-02-8
///
ENTRY       EC 1.12.98.1                Enzyme
NAME        coenzyme F420 hydrogenase;
            8-hydroxy-5-deazaflavin-reducing hydrogenase;
            F420-reducing hydrogenase;
            coenzyme F420-dependent hydrogenase
CLASS       Oxidoreductases;
            Acting on hydrogen as donor;
            With other, known, acceptors
SYSNAME     hydrogen:coenzyme F420 oxidoreductase
REACTION    H2 + coenzyme F420 = reduced coenzyme F420 [RN:R03025]
ALL_REAC    R03025
SUBSTRATE   H2 [CPD:C00282];
            coenzyme F420 [CPD:C00876]
PRODUCT     reduced coenzyme F420 [CPD:C01080]
COFACTOR    Iron [CPD:C00023];
            Nickel [CPD:C00291];
            Deazaflavin [CPD:C01800]
COMMENT     An iron-sulfur flavoprotein (FAD) containing nickel. The enzyme from
            some sources contains selenocysteine. The enzyme also reduces the
            riboflavin analogue of F420, flavins and methylviologen, but to a
            lesser extent. The hydrogen acceptor coenzyme F420 is a deazaflavin
            derivative.
REFERENCE   1
  AUTHORS   Adams, M.W.W., Mortenson, L.E. and Chen, J.-S.
  TITLE     Hydrogenase.
  JOURNAL   Biochim. Biophys. Acta 594 (1981) 105-176.
  ORGANISM  Methanobacterium formicicum
REFERENCE   2  [PMID:6211447]
  AUTHORS   Yamazaki S.
  TITLE     A selenium-containing hydrogenase from Methanococcus vannielii.
            Identification of the selenium moiety as a selenocysteine residue.
  JOURNAL   J. Biol. Chem. 257 (1982) 7926-9.
  ORGANISM  Methanococcus vannielii
REFERENCE   3  [PMID:3663585]
  AUTHORS   Fox JA, Livingston DJ, Orme-Johnson WH, Walsh CT.
  TITLE     8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium
            thermoautotrophicum: 1. Purification and characterization.
  JOURNAL   Biochemistry. 26 (1987) 4219-27.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
REFERENCE   4  [PMID:3121317]
  AUTHORS   Muth E, Morschel E, Klein A.
  TITLE     Purification and characterization of an
            8-hydroxy-5-deazaflavin-reducing hydrogenase from the
            archaebacterium Methanococcus voltae.
  JOURNAL   Eur. J. Biochem. 169 (1987) 571-7.
  ORGANISM  Methanococcus voltae
REFERENCE   5  [PMID:2738024]
  AUTHORS   Baron SF, Ferry JG.
  TITLE     Purification and properties of the membrane-associated coenzyme
            F420-reducing hydrogenase from Methanobacterium formicicum.
  JOURNAL   J. Bacteriol. 171 (1989) 3846-53.
  ORGANISM  Methanobacterium formicicum
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K00439  coenzyme F420 hydrogenase
            KO: K00440  coenzyme F420 hydrogenase alpha subunit
            KO: K00441  coenzyme F420 hydrogenase beta subunit
            KO: K00442  coenzyme F420 hydrogenase delta subunit
            KO: K00443  coenzyme F420 hydrogenase gamma subunit
GENES       OSA: 4335472
            CME: CMJ076C
            DPS: DP1008
            RET: RHE_CH02742(yhch00827)
            RPA: RPA1501
            RPB: RPB_4023
            RPC: RPC_1245
            RPD: RPD_3777
            RPE: RPE_1300
            JAN: Jann_0300
            RDE: RD1_3988
            RRU: Rru_A0937
            SYN: slr1923(frhB)
            SYC: syc0195_d
            SYF: Synpcc7942_1359
            SYX: SynWH7803_1550(frhB)
            CYA: CYA_1215
            CYB: CYB_1261
            TEL: tll1845
            GVI: gll0878
            ANA: all1601
            AVA: Ava_4214
            TER: Tery_0742
            DET: DET0616
            DEH: cbdb_A598
            MJA: MJ0029 MJ0030(frhD) MJ0031(frhG) MJ0032(frhB) MJ0253 MJ0725
                 MJ0726 MJ0727 MJ1191(vhuG)
            MMP: MMP0817(frcB) MMP0818(frcG) MMP0819(frcD) MMP0820(frcA)
                 MMP1337 MMP1382(fruA) MMP1383(fruD) MMP1384(fruG)
                 MMP1385(fruB) MMP1694(vhuA) MMP1695(vhuG)
            MMQ: MmarC5_0194 MmarC5_0647
            MMZ: MmarC7_0629
            MAE: Maeo_1043
            MVN: Mevan_0075
            MAC: MA0975(frhA) MA0976(frhD) MA0977(frhG) MA0978(frhB) MA3439
            MBA: Mbar_A0449 Mbar_A0450 Mbar_A0451 Mbar_A0452 Mbar_A2287
                 Mbar_A2289 Mbar_A2290
            MMA: MM_3042 MM_3043 MM_3044 MM_3045 MM_3264
            MBU: Mbur_2261
            MTP: Mthe_0174
            MHU: Mhun_2329 Mhun_2330 Mhun_2331 Mhun_2332
            MEM: Memar_2176
            MBN: Mboo_0477 Mboo_0479
            MTH: MTH1297(frhB) MTH1298(frhG) MTH1299(frhD) MTH1300(frhA)
                 MTH193 MTH341
            MST: Msp_1302(frhA) Msp_1303(frhD) Msp_1304(frhG) Msp_1305(frhB)
                 Msp_1514
            MSI: Msm_1000 Msm_1121 Msm_1122 Msm_1123 Msm_1124
            MKA: MK0267 MK0538 MK0929 MK0930 MK0931 MK1624(hyaD_2)
            AFU: AF1372(vhuA)
            NPH: NP4006A
            RCI: RCIA172(frhD-1) RCIX1471(frhB-3) RCIX2136(frhB-2)
                 RCIX2137(frhG-2) RCIX2138(frhA-2) RCIX2388(frhA-1)
                 RCIX2390(frhG-1) RCIX2391(frhB-1) RCIX2759(frhB-4)
DBLINKS     IUBMB Enzyme Nomenclature: 1.12.98.1
            ExPASy - ENZYME nomenclature database: 1.12.98.1
            ExplorEnz - The Enzyme Database: 1.12.98.1
            ERGO genome analysis and discovery system: 1.12.98.1
            BRENDA, the Enzyme Database: 1.12.98.1
            CAS: 9027-05-8
///
ENTRY       EC 1.12.98.2                Enzyme
NAME        5,10-methenyltetrahydromethanopterin hydrogenase;
            H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase;
            nonmetal hydrogenase;
            N5,N10-methenyltetrahydromethanopterin hydrogenase;
            hydrogen:N5,N10-methenyltetrahydromethanopterin oxidoreductase
CLASS       Oxidoreductases;
            Acting on hydrogen as donor;
            With other, known, acceptors
SYSNAME     hydrogen:5,10-methenyltetrahydromethanopterin oxidoreductase
REACTION    H2 + 5,10-methenyltetrahydromethanopterin = H+ +
            5,10-methylenetetrahydromethanopterin [RN:R04455]
ALL_REAC    R04455
SUBSTRATE   H2 [CPD:C00282];
            5,10-methenyltetrahydromethanopterin [CPD:C04330]
PRODUCT     H+ [CPD:C00080];
            5,10-methylenetetrahydromethanopterin [CPD:C04377]
COMMENT     Does not catalyse the reduction of artificial dyes. Does not by
            itself catalyse a H2/H+ exchange reaction. Does not contain nickel
            or iron-sulfur clusters.
REFERENCE   1
  AUTHORS   Zirngibl, C., Hedderich, R. and Thauer, R.K.
  TITLE     N5,N10-Methylenetetrahydromethanopterin dehydrogenase from
            Methanobacterium thermoautotrophicum has hydrogenase activity.
  JOURNAL   FEBS Lett. 261 (1990) 112-116.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
REFERENCE   2  [PMID:7628605]
  AUTHORS   Klein AR, Fernandez VM, Thauer RK.
  TITLE     H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase:
            mechanism of H2 formation analyzed using hydrogen isotopes.
  JOURNAL   FEBS. Lett. 368 (1995) 203-6.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
GENES       MMQ: MmarC5_1551
            MMZ: MmarC7_1126
            MAE: Maeo_1025
            MVN: Mevan_1132
STRUCTURES  PDB: 2B0J  
DBLINKS     IUBMB Enzyme Nomenclature: 1.12.98.2
            ExPASy - ENZYME nomenclature database: 1.12.98.2
            ExplorEnz - The Enzyme Database: 1.12.98.2
            ERGO genome analysis and discovery system: 1.12.98.2
            BRENDA, the Enzyme Database: 1.12.98.2
            CAS: 100357-01-5
///
ENTRY       EC 1.12.98.3                Enzyme
NAME        Methanosarcina-phenazine hydrogenase;
            methanophenazine hydrogenase;
            methylviologen-reducing hydrogenase
CLASS       Oxidoreductases;
            Acting on hydrogen as donor;
            With other, known, acceptors
SYSNAME     hydrogen:2-(2,3-dihydropentaprenyloxy)phenazine oxidoreductase
REACTION    H2 + 2-(2,3-dihydropentaprenyloxy)phenazine =
            2-dihydropentaprenyloxyphenazine
SUBSTRATE   H2 [CPD:C00282];
            2-(2,3-dihydropentaprenyloxy)phenazine
PRODUCT     2-dihydropentaprenyloxyphenazine
COMMENT     Contains nickel, iron-sulfur clusters and cytochrome b. The enzyme
            from some sources contains selenocysteine.
REFERENCE   1  [PMID:9555882]
  AUTHORS   Abken HJ, Tietze M, Brodersen J, Baumer S, Beifuss U, Deppenmeier U.
  TITLE     Isolation and characterization of methanophenazine and function of
            phenazines in membrane-bound electron transport of Methanosarcina
            mazei Go1.
  JOURNAL   J. Bacteriol. 180 (1998) 2027-32.
  ORGANISM  Methanosarcina mazei [GN:mma]
REFERENCE   2  [PMID:10471795]
  AUTHORS   Deppenmeier U, Lienard T, Gottschalk G.
  TITLE     Novel reactions involved in energy conservation by methanogenic
            archaea.
  JOURNAL   FEBS. Lett. 457 (1999) 291-7.
REFERENCE   3  [PMID:10941105]
  AUTHORS   Beifuss U, Tietze M, Baumer S, Deppenmeier U.
  TITLE     Methanophenazine: Structure, Total Synthesis, and Function of a New
            Cofactor from Methanogenic Archaea This work was supported by the
            Deutsche Forschungsgemeinschaft (Sonderforschungsbereich 416; grants
            De 488/6-1 and De 488/4-2) and the Fonds der Chemischen Industrie.
            We are grateful to Drs. J. Paust and H. Jaedicke (BASF AG,
            Ludwigshafen) and Dr. R. K. Muller (Hoffmann-La Roche Ltd., Basel)
            for generously providing chemicals.
  JOURNAL   Angew. Chem. Int. Ed. Engl. 39 (2000) 2470-2472.
  ORGANISM  Methanosarcina mazei [GN:mma]
DBLINKS     IUBMB Enzyme Nomenclature: 1.12.98.3
            ExPASy - ENZYME nomenclature database: 1.12.98.3
            ExplorEnz - The Enzyme Database: 1.12.98.3
            ERGO genome analysis and discovery system: 1.12.98.3
            BRENDA, the Enzyme Database: 1.12.98.3
            CAS: 9027-05-8
///
ENTRY       EC 1.12.99.1      Obsolete  Enzyme
NAME        Transferred to 1.12.98.1
CLASS       Oxidoreductases;
            Acting on hydrogen as donor;
            With other acceptors
COMMENT     Transferred entry: now EC 1.12.98.1 coenzyme F420 hydrogenase (EC
            1.12.99.1 created 1989, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.12.99.1
            ExPASy - ENZYME nomenclature database: 1.12.99.1
            ExplorEnz - The Enzyme Database: 1.12.99.1
            ERGO genome analysis and discovery system: 1.12.99.1
            BRENDA, the Enzyme Database: 1.12.99.1
///
ENTRY       EC 1.12.99.2      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on hydrogen as donor;
            With other acceptors
COMMENT     Deleted entry:
            coenzyme-M-7-mercaptoheptanoylthreonine-phosphate-heterodisulfide
            hydrogenase. Now shown to be two enzymes, EC 1.12.98.3,
            Methanosarcina-phenazine hydrogenase and EC 1.8.98.1, CoB-CoM
            heterodisulfide reductase. (EC 1.12.99.2 created 1992, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.12.99.2
            ExPASy - ENZYME nomenclature database: 1.12.99.2
            ExplorEnz - The Enzyme Database: 1.12.99.2
            ERGO genome analysis and discovery system: 1.12.99.2
            BRENDA, the Enzyme Database: 1.12.99.2
///
ENTRY       EC 1.12.99.3      Obsolete  Enzyme
NAME        Transferred to 1.12.5.1
CLASS       Oxidoreductases;
            Acting on hydrogen as donor;
            With other acceptors
COMMENT     Transferred entry: now EC 1.12.5.1 hydrogen:quinone oxidoreductase
            (EC 1.12.99.3 created 1999, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.12.99.3
            ExPASy - ENZYME nomenclature database: 1.12.99.3
            ExplorEnz - The Enzyme Database: 1.12.99.3
            ERGO genome analysis and discovery system: 1.12.99.3
            BRENDA, the Enzyme Database: 1.12.99.3
///
ENTRY       EC 1.12.99.4      Obsolete  Enzyme
NAME        Transferred to 1.12.98.2
CLASS       Oxidoreductases;
            Acting on hydrogen as donor;
            With other acceptors
COMMENT     Transferred entry: now EC 1.12.98.2,
            5,10-methenyltetrahydromethanopterin hydrogenase (EC 1.12.99.4
            created 1999, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.12.99.4
            ExPASy - ENZYME nomenclature database: 1.12.99.4
            ExplorEnz - The Enzyme Database: 1.12.99.4
            ERGO genome analysis and discovery system: 1.12.99.4
            BRENDA, the Enzyme Database: 1.12.99.4
///
ENTRY       EC 1.12.99.5      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on hydrogen as donor;
            With other acceptors
COMMENT     Deleted entry: 3,4-dihydroxyquinoline 2,4-dioxygenase. Identical to
            EC 1.13.11.47, 3-hydroxy-4-oxoquinoline 2,4-dioxygenase. (EC
            1.12.99.5 created 1999, deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 1.12.99.5
            ExPASy - ENZYME nomenclature database: 1.12.99.5
            ExplorEnz - The Enzyme Database: 1.12.99.5
            ERGO genome analysis and discovery system: 1.12.99.5
            BRENDA, the Enzyme Database: 1.12.99.5
///
ENTRY       EC 1.12.99.6                Enzyme
NAME        hydrogenase (acceptor);
            H2 producing hydrogenase[ambiguous];
            hydrogen-lyase[ambiguous];
            hydrogenlyase[ambiguous];
            uptake hydrogenase[ambiguous];
            hydrogen:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on hydrogen as donor;
            With other acceptors
SYSNAME     hydrogen:acceptor oxidoreductase
REACTION    H2 + A = AH2 [RN:R07182]
ALL_REAC    R07182
SUBSTRATE   H2 [CPD:C00282];
            A [CPD:C00028]
PRODUCT     AH2 [CPD:C00030]
COMMENT     Uses molecular hydrogen for the reduction of a variety of
            substances. Contains iron-sulfur clusters. The enzyme from some
            sources contains nickel.
REFERENCE   1
  AUTHORS   Shug, A.L., Wilson, P.W., Green, D.E. and Mahler, H.R.
  TITLE     The role of molybdenum and flavin in hydrogenase.
  JOURNAL   J. Am. Chem. Soc. 76 (1954) 3355-3356.
  ORGANISM  Clostridium pasteurianum
REFERENCE   2
  AUTHORS   Adams, M.W.W., Mortenson, L.E. and Chen, J.-S.
  TITLE     Hydrogenase.
  JOURNAL   Biochim. Biophys. Acta 594 (1981) 105-176.
  ORGANISM  Methanobacterium formicicum
REFERENCE   3  [PMID:11524134]
  AUTHORS   Vignais PM, Billoud B, Meyer J.
  TITLE     Classification and phylogeny of hydrogenases.
  JOURNAL   FEMS. Microbiol. Rev. 25 (2001) 455-501.
  ORGANISM  Clostridium pasteurianum
ORTHOLOGY   KO: K06280  hydrogenase
            KO: K06281  hydrogenase large subunit
            KO: K06282  hydrogenase small subunit
GENES       ECO: b0972(hyaA) b0973(hyaB) b2994(hybC) b2997(hybO)
            ECJ: JW0954(hyaA) JW0955(hyaB) JW2962(hybC) JW2965(hybO)
            ECE: Z1389(hyaA) Z1390(hyaB) Z4348(hybC) Z4351
            ECS: ECs1128 ECs1129 ECs3879 ECs3882
            ECC: c1113(hyaA) c1114(hyaB) c3731(hybC) c3734
            ECI: UTI89_C1040(hyaA) UTI89_C1041(hyaB) UTI89_C3416(hybC)
                 UTI89_C3419
            ECP: ECP_0977 ECP_0978 ECP_3080 ECP_3083
            ECV: APECO1_3425(hybO) APECO1_3428(hybC) APECO1_76(hyaA)
                 APECO1_77(hyaB)
            ECW: EcE24377A_1087(hyaA) EcE24377A_3463(hybC)
                 EcE24377A_3466(hyb0)
            ECX: EcHS_A1080(hyaA) EcHS_A3174(hybC) EcHS_A3177(hyb0)
            STY: STY1523(hyaA2) STY1525(hyaB2) STY1914 STY3318(hybC)
                 STY3321(hyb0)
            STT: t1089 t1458(hyaA) t3068(hybC) t3071(hyb0)
            SPT: SPA1086(hyaB) SPA1317(hyaA2) SPA1318(hyaB2) SPA3015(hybC)
                 SPA3018(hyb0)
            SEC: SC1782(mbhS) SC3088(hybC) SC3091(hypO)
            STM: STM1538 STM1539 STM1786 STM1787 STM3147(hybC) STM3150(hypO)
            SFL: SF0973(hyaA) SF0974(hyaB) SF3041(hybC) SF3044(hybO)
            SFX: S1040(hyaA) S1041(hyaB) S3242(hybC) S3245
            SFV: SFV_0981(hyaA) SFV_0982(hyaB) SFV_3047(hybC) SFV_3050
            SSN: SSON_0978(hyaA) SSON_0979(hyaB) SSON_3139(hybC) SSON_3142
            SBO: SBO_2258(hyaB) SBO_2259(hyaA) SBO_2866 SBO_2869(hybC)
            SDY: SDY_0947(hyaA) SDY_0948(hyaB) SDY_3076 SDY_3079(hybC)
            ECA: ECA1225(hybO) ECA1228(hybC)
            MSU: MS2361(hyaB) MS2365(hyaA)
            APL: APL_1331(hyaA) APL_1334(hyaB)
            ASU: Asuc_1277
            MCA: MCA0165 MCA0166
            TCX: Tcr_2037 Tcr_2038
            AEH: Mlg_2028 Mlg_2029
            AHA: AHA_2523(hybC) AHA_2526
            RME: Rmet_1297 Rmet_1298
            BVI: Bcep1808_5931
            RFR: Rfer_4088 Rfer_4091
            PNA: Pnap_1975
            MPT: Mpe_A2826 Mpe_A2827
            DAR: Daro_3971 Daro_3974 Daro_3988 Daro_3989
            TBD: Tbd_1375 Tbd_1378
            ABU: Abu_1436(hupL)
            GSU: GSU0782 GSU0785
            GUR: Gura_0545 Gura_0872 Gura_1943
            DVU: DVU1922(hynA-1)
            DVL: Dvul_1249
            DDE: Dde_2134(hydA) Dde_2135 Dde_2137(hydA) Dde_2138
            LIP: LI0439(hyaA) LI0440(hyaB)
            DPS: DP0574(hynB) DP0575(hynA)
            ADE: Adeh_0478 Adeh_0481
            AFW: Anae109_0526 Anae109_3523
            SFU: Sfum_2953
            BJA: bll6941(hupL) bll6942(hupS) blr1720(hupS) blr1721(hupL)
            BRA: BRADO1682(hupU) BRADO1684(hupS) BRADO1685(hupL)
            BBT: BBta_0460(hupU) BBta_1994(hupU) BBta_1996(hupS)
                 BBta_1997(hupL) BBta_p0179(hupL) BBta_p0180(hupS)
            RPA: RPA0962(hupS) RPA0963(hupL)
            RPC: RPC_3771 RPC_3772
            RPD: RPD_1162 RPD_1163
            RPE: RPE_1231 RPE_1232
            XAU: Xaut_2173
            RSP: RSP_0495(hupS) RSP_0496(hupL)
            RSH: Rsph17029_2146
            PDE: Pden_3097
            ACR: Acry_0338
            RRU: Rru_A1161 Rru_A1162
            MAG: amb1647 amb1650
            MGM: Mmc1_2503 Mmc1_2506
            ABA: Acid345_4237 Acid345_4240
            SUS: Acid_6923
            CAC: CA_P0141(mbhS) CA_P0142(mbhL)
            CBE: Cbei_3013
            CHY: CHY_1546
            DSY: DSY0796 DSY1598 DSY1599 DSY2101 DSY2238 DSY2239
            MSM: MSMEG_2720
            CDI: DIP0672 DIP0673
            RHA: RHA1_ro04603 RHA1_ro04604
            SMA: SAV7366(hydA) SAV7367(hydB)
            FRA: Francci3_1941 Francci3_1942
            FAL: FRAAL1830(hupS2) FRAAL2392(hupS1) FRAAL2393(hupL1)
            SEN: SACE_3061 SACE_3062
            ANA: all0687(hupL) all0688
            AVA: Ava_4595 Ava_4596
            FJO: Fjoh_3906
            CTE: CT0777(hupL)
            CPH: Cpha266_0972
            PLT: Plut_1446 Plut_1447
            DEH: cbdb_A129(hupL) cbdb_A130(hupS)
            DEB: DehaBAV1_0257
            RRS: RoseRS_2319
            RCA: Rcas_3148
            AAE: aq_660(mbhS1) aq_662(mbhL1) aq_960(mbhL2) aq_965(mbhS2)
DBLINKS     IUBMB Enzyme Nomenclature: 1.12.99.6
            ExPASy - ENZYME nomenclature database: 1.12.99.6
            ExplorEnz - The Enzyme Database: 1.12.99.6
            ERGO genome analysis and discovery system: 1.12.99.6
            BRENDA, the Enzyme Database: 1.12.99.6
            CAS: 9027-05-8
///
ENTRY       EC 1.13.1.1       Obsolete  Enzyme
NAME        Transferred to 1.13.11.1
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2
COMMENT     Transferred entry: Now EC 1.13.11.1, catechol 1,2-dioxygenase (EC
            1.13.1.1 created 1961 as EC 1.99.2.2, transferred 1965 to EC
            1.13.1.1, deleted 1972)
STRUCTURES  PDB: 1E9P  1E9Q  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.1.1
            ExPASy - ENZYME nomenclature database: 1.13.1.1
            ExplorEnz - The Enzyme Database: 1.13.1.1
            ERGO genome analysis and discovery system: 1.13.1.1
            BRENDA, the Enzyme Database: 1.13.1.1
///
ENTRY       EC 1.13.1.2       Obsolete  Enzyme
NAME        Transferred to 1.13.11.2
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2
COMMENT     Transferred entry: Now EC 1.13.11.2, catechol 2,3-dioxygenase (EC
            1.13.1.2 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.1.2
            ExPASy - ENZYME nomenclature database: 1.13.1.2
            ExplorEnz - The Enzyme Database: 1.13.1.2
            ERGO genome analysis and discovery system: 1.13.1.2
            BRENDA, the Enzyme Database: 1.13.1.2
///
ENTRY       EC 1.13.1.3       Obsolete  Enzyme
NAME        Transferred to 1.13.11.3
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2
COMMENT     Transferred entry: Now EC 1.13.11.3, protocatechuate 3,4-dioxygenase
            (EC 1.13.1.3 created 1961 as EC 1.99.2.3, transferred 1965 to EC
            1.13.1.3, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.1.3
            ExPASy - ENZYME nomenclature database: 1.13.1.3
            ExplorEnz - The Enzyme Database: 1.13.1.3
            ERGO genome analysis and discovery system: 1.13.1.3
            BRENDA, the Enzyme Database: 1.13.1.3
///
ENTRY       EC 1.13.1.4       Obsolete  Enzyme
NAME        Transferred to 1.13.11.4
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2
COMMENT     Transferred entry: Now EC 1.13.11.4, gentisate 1,2-dioxygenase (EC
            1.13.1.4 created 1961 as EC 1.99.2.4, transferred 1965 to EC
            1.13.1.4, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.1.4
            ExPASy - ENZYME nomenclature database: 1.13.1.4
            ExplorEnz - The Enzyme Database: 1.13.1.4
            ERGO genome analysis and discovery system: 1.13.1.4
            BRENDA, the Enzyme Database: 1.13.1.4
///
ENTRY       EC 1.13.1.5       Obsolete  Enzyme
NAME        Transferred to 1.13.11.5
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2
COMMENT     Transferred entry: Now EC 1.13.11.5, homogentisate 1,2-dioxygenase
            (EC 1.13.1.5 created 1961 as EC 1.99.2.5, transferred 1965 to EC
            1.13.1.5, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.1.5
            ExPASy - ENZYME nomenclature database: 1.13.1.5
            ExplorEnz - The Enzyme Database: 1.13.1.5
            ERGO genome analysis and discovery system: 1.13.1.5
            BRENDA, the Enzyme Database: 1.13.1.5
///
ENTRY       EC 1.13.1.6       Obsolete  Enzyme
NAME        Transferred to 1.13.11.6
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2
COMMENT     Transferred entry: Now EC 1.13.11.6, 3-hydroxyanthranilate
            3,4-dioxygenase (EC 1.13.1.6 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.1.6
            ExPASy - ENZYME nomenclature database: 1.13.1.6
            ExplorEnz - The Enzyme Database: 1.13.1.6
            ERGO genome analysis and discovery system: 1.13.1.6
            BRENDA, the Enzyme Database: 1.13.1.6
///
ENTRY       EC 1.13.1.7       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2
COMMENT     Deleted entry: 3,4-dihydroxyphenylacetate 3,4-dioxygenase (EC
            1.13.1.7 created 1965, transferred 1972 to EC 1.13.11.7, deleted
            1980)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.1.7
            ExPASy - ENZYME nomenclature database: 1.13.1.7
            ExplorEnz - The Enzyme Database: 1.13.1.7
            ERGO genome analysis and discovery system: 1.13.1.7
            BRENDA, the Enzyme Database: 1.13.1.7
///
ENTRY       EC 1.13.1.8       Obsolete  Enzyme
NAME        Transferred to 1.13.11.8
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2
COMMENT     Transferred entry: Now EC 1.13.11.8, protocatechuate 4,5-dioxygenase
            (EC 1.13.1.8 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.1.8
            ExPASy - ENZYME nomenclature database: 1.13.1.8
            ExplorEnz - The Enzyme Database: 1.13.1.8
            ERGO genome analysis and discovery system: 1.13.1.8
            BRENDA, the Enzyme Database: 1.13.1.8
///
ENTRY       EC 1.13.1.9       Obsolete  Enzyme
NAME        Transferred to 1.13.11.9
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2
COMMENT     Transferred entry: Now EC 1.13.11.9, 2,5-dihydroxypyridine
            5,6-dioxygenase (EC 1.13.1.9 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.1.9
            ExPASy - ENZYME nomenclature database: 1.13.1.9
            ExplorEnz - The Enzyme Database: 1.13.1.9
            ERGO genome analysis and discovery system: 1.13.1.9
            BRENDA, the Enzyme Database: 1.13.1.9
///
ENTRY       EC 1.13.1.10      Obsolete  Enzyme
NAME        Transferred to 1.13.11.10
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2
COMMENT     Transferred entry: Now EC 1.13.11.10, 7,8-dihydroxykynurenate
            8,8a-dioxygenase (EC 1.13.1.10 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.1.10
            ExPASy - ENZYME nomenclature database: 1.13.1.10
            ExplorEnz - The Enzyme Database: 1.13.1.10
            ERGO genome analysis and discovery system: 1.13.1.10
            BRENDA, the Enzyme Database: 1.13.1.10
///
ENTRY       EC 1.13.1.11      Obsolete  Enzyme
NAME        Transferred to 1.13.99.1
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2
COMMENT     Transferred entry: Now EC 1.13.99.1, inositol oxygenase (EC
            1.13.1.11 created 1961 as EC 1.99.2.6, transferred 1965 to EC
            1.13.1.11, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.1.11
            ExPASy - ENZYME nomenclature database: 1.13.1.11
            ExplorEnz - The Enzyme Database: 1.13.1.11
            ERGO genome analysis and discovery system: 1.13.1.11
            BRENDA, the Enzyme Database: 1.13.1.11
///
ENTRY       EC 1.13.1.12      Obsolete  Enzyme
NAME        Transferred to 1.13.11.11
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2
COMMENT     Transferred entry: Now EC 1.13.11.11, tryptophan 2,3-dioxygenase (EC
            1.13.1.12 created 1961 as EC 1.11.1.4, deleted 1964, reinstated 1965
            as EC 1.13.1.12, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.1.12
            ExPASy - ENZYME nomenclature database: 1.13.1.12
            ExplorEnz - The Enzyme Database: 1.13.1.12
            ERGO genome analysis and discovery system: 1.13.1.12
            BRENDA, the Enzyme Database: 1.13.1.12
///
ENTRY       EC 1.13.1.13      Obsolete  Enzyme
NAME        Transferred to 1.13.11.12
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2
COMMENT     Transferred entry: Now EC 1.13.11.12, lipoxygenase (EC 1.13.1.13
            created 1961 as EC 1.99.2.1, transferred 1965 to EC 1.13.1.13,
            deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.1.13
            ExPASy - ENZYME nomenclature database: 1.13.1.13
            ExplorEnz - The Enzyme Database: 1.13.1.13
            ERGO genome analysis and discovery system: 1.13.1.13
            BRENDA, the Enzyme Database: 1.13.1.13
///
ENTRY       EC 1.13.11.1                Enzyme
NAME        catechol 1,2-dioxygenase;
            catechol-oxygen 1,2-oxidoreductase;
            1,2-pyrocatechase;
            catechase;
            catechol 1,2-oxygenase;
            catechol dioxygenase;
            pyrocatechase;
            pyrocatechol 1,2-dioxygenase;
            CD I;
            CD II
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     catechol:oxygen 1,2-oxidoreductase
REACTION    catechol + O2 = cis,cis-muconate [RN:R00817]
ALL_REAC    R00817;
            (other) R04258 R05299 R06833 R06839
SUBSTRATE   catechol [CPD:C00090];
            O2 [CPD:C00007]
PRODUCT     cis,cis-muconate [CPD:C02480]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe3+. Involved in the metabolism of nitro-aromatic
            compounds by a strain of Pseudomonas putida.
REFERENCE   1
  AUTHORS   Hayaishi, O.
  TITLE     Direct oxygenation by O2, oxygenases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 8, Academic Press, New York, 1963, p. 353-371.
REFERENCE   2  [PMID:13502352]
  AUTHORS   HAYAISHI O, KATAGIRI M, ROTHBERG S.
  TITLE     Studies on oxygenases; pyrocatechase.
  JOURNAL   J. Biol. Chem. 229 (1957) 905-20.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   3
  AUTHORS   Sistrom, W.R. and Stanier, R.Y.
  TITLE     The mechanism of formation of beta-ketoadipic acid by bacteria.
  JOURNAL   J. Biol. Chem. 210 (1954) 821-836.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   4  [PMID:3752997]
  AUTHORS   Zeyer J, Kocher HP, Timmis KN.
  TITLE     Influence of para-substituents on the oxidative metabolism of
            o-nitrophenols by Pseudomonas putida B2.
  JOURNAL   Appl. Environ. Microbiol. 52 (1986) 334-9.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
            PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00622  Toluene and xylene degradation
            PATH: map00627  1,4-Dichlorobenzene degradation
            PATH: map00629  Carbazole degradation
ORTHOLOGY   KO: K03381  catechol 1,2-dioxygenase
GENES       PAE: PA2507(catA)
            PAU: PA14_32240(catA)
            PAP: PSPA7_2732(catA)
            PPU: PP_3166 PP_3713(catA)
            PFL: PFL_3860(catA)
            PFO: Pfl_2327 Pfl_2961
            PEN: PSEEN3136(catA)
            PCR: Pcryo_1268
            ACI: ACIAD1442(catA)
            ACB: A1S_1845
            NOC: Noc_1128 Noc_2416
            REU: Reut_A1705 Reut_B4137 Reut_B4402 Reut_D6466 Reut_D6473
            REH: H16_A1964(catA)
            RME: Rmet_1781 Rmet_4881 Rmet_5062
            BMA: BMAA0199(catA)
            BMV: BMASAVP1_1374(catA)
            BML: BMA10299_1571(catA)
            BMN: BMA10247_A0230(catA)
            BXE: Bxe_A1130(clcA) Bxe_A2109(catA)
            BVI: Bcep1808_5824
            BUR: Bcep18194_A4486 Bcep18194_B2329 Bcep18194_C7045
            BCN: Bcen_1307 Bcen_4594
            BCH: Bcen2424_3769 Bcen2424_6523
            BAM: Bamb_3333 Bamb_6585
            BPS: BPSS1892(catA)
            BPM: BURPS1710b_A0987(catA)
            BPL: BURPS1106A_A2567(catA)
            BPD: BURPS668_A2711(catA)
            BTE: BTH_II0484
            POL: Bpro_2064
            AJS: Ajs_0142
            VEI: Veis_4613
            RET: RHE_CH02298(ypch00749)
            RLE: pRL120093 pRL120101 pRL120214
            BRA: BRADO0539 BRADO2264 BRADO2272 BRADO2470
            BBT: BBta_2816 BBta_7639
            RPC: RPC_3196
            RPD: RPD_2210
            PDE: Pden_1176
            MSM: MSMEG_1911(catA)
            MGI: Mflv_1358
            MMC: Mmcs_1376
            MKM: Mkms_1394
            MJL: Mjls_1410
            CGL: NCgl1113(cgl1160) NCgl2319(cgl2402)
            CGB: cg1311(catA2) cg2636(catA1) cg3385(catA3)
            RHA: RHA1_ro02373(catA1) RHA1_ro02515(catA2) RHA1_ro02997
                 RHA1_ro08069 RHA1_ro08511
            SEN: SACE_4382(catA1)
STRUCTURES  PDB: 1DLM  1DLQ  1DLT  1DMH  1S9A  2AZQ  2BOY  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.1
            ExPASy - ENZYME nomenclature database: 1.13.11.1
            ExplorEnz - The Enzyme Database: 1.13.11.1
            ERGO genome analysis and discovery system: 1.13.11.1
            UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.1
            BRENDA, the Enzyme Database: 1.13.11.1
            CAS: 9027-16-1
///
ENTRY       EC 1.13.11.2                Enzyme
NAME        catechol 2,3-dioxygenase;
            2,3-pyrocatechase;
            catechol 2,3-oxygenase;
            catechol oxygenase;
            metapyrocatechase;
            pyrocatechol 2,3-dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     catechol:oxygen 2,3-oxidoreductase (decyclizing)
REACTION    catechol + O2 = 2-hydroxymuconate semialdehyde [RN:R00816]
ALL_REAC    R00816;
            (other) R04089 R05295 R05404 R05406 R07795
SUBSTRATE   catechol [CPD:C00090];
            O2 [CPD:C00007]
PRODUCT     2-hydroxymuconate semialdehyde [CPD:C00682]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires FeII. The enzyme from Alcaligenes sp. strain O-1 has also
            been shown to catalyse the reaction: 2,3-dihydroxybenzenesulfonate +
            O2 + H2O = 2-hydroxymuconate + bisulfite and has been referred to as
            2,3-dihydroxybenzenesulfonate 2,3-dioxygenase. Further work will be
            necessary to show whether or not this is a distinct enzyme.
REFERENCE   1  [PMID:8002948]
  AUTHORS   Junker F, Field JA, Bangerter F, Ramsteiner K, Kohler HP, Joannou
            CL, Mason JR, Leisinger T, Cook AM.
  TITLE     Oxygenation and spontaneous deamination of 2-aminobenzenesulphonic
            acid in Alcaligenes sp. strain O-1 with subsequent meta ring
            cleavage and spontaneous desulphonation to 2-hydroxymuconic acid.
  JOURNAL   Biochem. J. 300 ( Pt 2) (1994) 429-36.
  ORGANISM  Alcaligenes sp.
REFERENCE   2  [PMID:8075807]
  AUTHORS   Junker F, Leisinger T, Cook AM.
  TITLE     3-Sulphocatechol 2,3-dioxygenase and other dioxygenases (EC
            1.13.11.2 and EC 1.14.12.-) in the degradative pathways of
            2-aminobenzenesulphonic, benzenesulphonic and 4-toluenesulphonic
            acids in Alcaligenes sp. strain O-1.
  JOURNAL   Microbiology. 140 ( Pt 7) (1994) 1713-22.
  ORGANISM  Alcaligenes sp.
REFERENCE   3
  AUTHORS   Hayaishi, O.
  TITLE     Direct oxygenation by O2, oxygenases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 8, Academic Press, New York, 1963, p. 353-371.
REFERENCE   4
  AUTHORS   Kojima, Y., Itada, N. and Hayaishi, O.
  TITLE     Metapyrocatechase: a new catechol-cleaving enzyme.
  JOURNAL   J. Biol. Chem. 236 (1961) 2223-2228.
  ORGANISM  Pseudomonas sp.
REFERENCE   5  [PMID:14087325]
  AUTHORS   NOZAKI M, KAGAMIYAMA H, HAYAISHI O.
  TITLE     METAPYROCATECHASE. I. PURIFICATION, CRYSTALLIZATION AND SOME
            PROPERTIES.
  JOURNAL   Biochem. Z. 338 (1963) 582-90.
  ORGANISM  Pseudomonas arvilla
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00622  Toluene and xylene degradation
            PATH: map00627  1,4-Dichlorobenzene degradation
            PATH: map00629  Carbazole degradation
            PATH: map00643  Styrene degradation
ORTHOLOGY   KO: K00446  catechol 2,3-dioxygenase
GENES       REU: Reut_A1133 Reut_B4677 Reut_B5687 Reut_C6234
            REH: H16_B0546
            RME: Rmet_1324
            BVI: Bcep1808_7600
            BUR: Bcep18194_B1114 Bcep18194_B1182 Bcep18194_B2964
                 Bcep18194_C7651
            AJS: Ajs_0214 Ajs_0218
            VEI: Veis_2789
            MPT: Mpe_A2277
            AZO: azo1844(lapB1) azo1858(xylE) azo2438(lapB2)
            DAR: Daro_3805
            RLE: RL2852
            BMB: BruAb2_1096
            BJA: bll2967 blr3819
            BRA: BRADO5115
            BBT: BBta_5584
            RPA: RPA3761
            RPB: RPB_1705
            RPD: RPD_3592
            SIT: TM1040_3467
            RSP: RSP_3021
            JAN: Jann_3502
            MAV: MAV_1947
            RHA: RHA1_ro03865 RHA1_ro08079
            ART: Arth_3523
            RXY: Rxyl_0199 Rxyl_2243
            RRS: RoseRS_2570
            RCA: Rcas_2413
            DGE: Dgeo_2419
            SSO: SSO1223 SSO2054
            STO: ST0724
            SAI: Saci_2295(xylE)
STRUCTURES  PDB: 1MPY  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.2
            ExPASy - ENZYME nomenclature database: 1.13.11.2
            ExplorEnz - The Enzyme Database: 1.13.11.2
            ERGO genome analysis and discovery system: 1.13.11.2
            UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.2
            BRENDA, the Enzyme Database: 1.13.11.2
            CAS: 9029-46-3
///
ENTRY       EC 1.13.11.3                Enzyme
NAME        protocatechuate 3,4-dioxygenase;
            protocatechuate oxygenase;
            protocatechuic acid oxidase;
            protocatechuic 3,4-dioxygenase;
            protocatechuic 3,4-oxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     protocatechuate:oxygen 3,4-oxidoreductase (decyclizing)
REACTION    3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate [RN:R01631]
ALL_REAC    R01631;
            (other) R03549
SUBSTRATE   3,4-dihydroxybenzoate [CPD:C00230];
            O2 [CPD:C00007]
PRODUCT     3-carboxy-cis,cis-muconate [CPD:C01163]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe3+.
REFERENCE   1  [PMID:4967959]
  AUTHORS   Fujisawa H, Hayaishi O.
  TITLE     Protocatechuate 3,4-dioxygenase. I. Crystallization and
            characterization.
  JOURNAL   J. Biol. Chem. 243 (1968) 2673-81.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   2  [PMID:13319299]
  AUTHORS   GROSS SR, GAFFORD RD, TATUM EL.
  TITLE     The metabolism of protocatechuic acid by Neurospora.
  JOURNAL   J. Biol. Chem. 219 (1956) 781-96.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   3
  AUTHORS   Stanier, R.Y. and Ingraham, J.L.
  TITLE     Protocatechuic acid oxidase.
  JOURNAL   J. Biol. Chem. 210 (1954) 799-820.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00623  2,4-Dichlorobenzoate degradation
ORTHOLOGY   KO: K00447  protocatechuate 3,4-dioxygenase
            KO: K00448  protocatechuate 3,4-dioxygenase, alpha subunit
            KO: K00449  protocatechuate 3,4-dioxygenase, beta subunit
GENES       SPE: Spro_2502
            XCC: XCC0367(pcaH) XCC0368(pcaG)
            XCB: XC_0379 XC_0380
            XCV: XCV0381(pcaH) XCV0382(pcaG)
            XAC: XAC0367(pcaH) XAC0368(pcaG)
            XOO: XOO0482(pcaH) XOO0483(pcaG)
            XOM: XOO_0448(XOO0448) XOO_0449(XOO0449)
            VPA: VPA0640
            PAE: PA0153(pcaH) PA0154(pcaG)
            PAU: PA14_01900(pcaH) PA14_01910(pcaG)
            PAP: PSPA7_0231(pcaH) PSPA7_0232(pcaG)
            PPU: PP_4655(pcaG) PP_4656(pcaH)
            PPF: Pput_4517
            PST: PSPTO_2338(pcaH) PSPTO_2339(pcaG)
            PSB: Psyr_2122 Psyr_2123
            PSP: PSPPH_2096(pcaH) PSPPH_2097(pcaG)
            PFL: PFL_1320(pcaH) PFL_1321(pcaG) PFL_5395(pcaG) PFL_5396(pcaH)
            PFO: Pfl_1270 Pfl_1271
            PEN: PSEEN4783(pcaG) PSEEN4784(pcaH)
            ACI: ACIAD1711(pcaH) ACIAD1712(pcaG)
            CSA: Csal_0311 Csal_0312
            RSO: RSc1441(pcaH) RSc1442(pcaG)
            REU: Reut_B5024 Reut_B5025
            REH: H16_B0795 H16_B1799 H16_B2290(pcaG) H16_B2291(pcaH1)
            RME: Rmet_4013 Rmet_4014
            BMA: BMAA0980(pcaG) BMAA0981(pcaH)
            BMV: BMASAVP1_0394(pcaH) BMASAVP1_0395(pcaG)
            BML: BMA10299_0244(pcaG) BMA10299_0245(pcaH)
            BMN: BMA10247_A1351(pcaH) BMA10247_A1352(pcaG)
            BXE: Bxe_B2775 Bxe_B2776
            BVI: Bcep1808_4739
            BUR: Bcep18194_B1859 Bcep18194_B1860
            BCN: Bcen_4195 Bcen_4196
            BCH: Bcen2424_4171 Bcen2424_4172
            BAM: Bamb_3578
            BPS: BPSS1300(pcaH) BPSS1301(pcaG)
            BPM: BURPS1710b_A0318(pcaH) BURPS1710b_A0319(pcaG)
            BPL: BURPS1106A_A1760(pcaH) BURPS1106A_A1761(pcaG)
            BPD: BURPS668_A1845(pcaH) BURPS668_A1846(pcaG)
            BTE: BTH_II1118 BTH_II1119
            POL: Bpro_0627 Bpro_0628
            RTY: RT0384(pcaH)
            RCO: RC0543
            RFE: RF_0617
            RBE: RBE_0329
            MLO: mlr7208 mlr7210
            MES: Meso_2050 Meso_2051
            SME: SMb20576(pcaG) SMb20577(pcaH)
            SMD: Smed_4209
            ATU: Atu4539(pcaG) Atu4540(pcaH)
            ATC: AGR_L_656 AGR_L_658
            RET: RHE_PE00056(pcaG) RHE_PE00057(pcaH)
            RLE: RL3016(pcaH) pRL110086(pcaG) pRL110087(pcaH)
            BME: BMEII0635 BMEII0636
            BMF: BAB2_0595(pcaG) BAB2_0596(pcaH)
            BMS: BRA0645(pcaH) BRA0646(pcaG)
            BMB: BruAb2_0580(pcaG) BruAb2_0581(pcaH)
            BOV: BOV_A0608(pcaG)
            OAN: Oant_3728
            BJA: blr0927(pcaH) blr0928(pcaG) blr2333(pcaH) blr2334(pcaG)
            XAU: Xaut_2689
            CCR: CC_2408 CC_2409
            SIL: SPOA0043(pcaG) SPOA0044(pcaH)
            SIT: TM1040_0557 TM1040_0558
            JAN: Jann_4163 Jann_4164
            RDE: RD1_3774(pcaH) RD1_3775(pcaG)
            PDE: Pden_3494
            SWI: Swit_1072
            SUS: Acid_0246
            MPA: MAP2730c(pcaG) MAP2731c(pcaH)
            MAV: MAV_3505(pcaG) MAV_3506(pcaH)
            MSM: MSMEG_2601(pcaH) MSMEG_2602(pcaG)
            MMC: Mmcs_1698 Mmcs_1699
            CGL: NCgl2314(cgl2397) NCgl2315(cgl2398)
            CGB: cg2630(pcaG) cg2631(pcaH)
            CEF: CE2300 CE2301
            RHA: RHA1_ro01335(pcaH) RHA1_ro01336(pcaG)
            SCO: SCO6699(pcaG) SCO6700(pcaH)
            SMA: SAV1703(pcaH) SAV1704(pcaG)
            AAU: AAur_4043(pcaG) AAur_4044(pcaH)
            SEN: SACE_3513(pcaG) SACE_3514(pcaH)
            RXY: Rxyl_1580 Rxyl_1581
            RBA: RB7678(pcxB)
            DGE: Dgeo_2386 Dgeo_2387
STRUCTURES  PDB: 1EO2  1EO9  1EOA  1EOB  1EOC  1YKK  1YKL  1YKM  1YKN  1YKO  
                 1YKP  2BUM  2BUQ  2BUR  2BUT  2BUU  2BUV  2BUW  2BUX  2BUY  
                 2BUZ  2BV0  2PCD  3PCA  3PCB  3PCC  3PCD  3PCE  3PCF  3PCG  
                 3PCH  3PCI  3PCJ  3PCK  3PCL  3PCM  3PCN  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.3
            ExPASy - ENZYME nomenclature database: 1.13.11.3
            ExplorEnz - The Enzyme Database: 1.13.11.3
            ERGO genome analysis and discovery system: 1.13.11.3
            UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.3
            BRENDA, the Enzyme Database: 1.13.11.3
            CAS: 9029-47-4
///
ENTRY       EC 1.13.11.4                Enzyme
NAME        gentisate 1,2-dioxygenase;
            gentisate oxygenase;
            2,5-dihydroxybenzoate dioxygenase;
            gentisate dioxygenase;
            gentisic acid oxidase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     gentisate:oxygen 1,2-oxidoreductase (decyclizing)
REACTION    2,5-dihydroxybenzoate + O2 = maleylpyruvate [RN:R02656]
ALL_REAC    R02656
SUBSTRATE   2,5-dihydroxybenzoate [CPD:C00628];
            O2 [CPD:C00007]
PRODUCT     maleylpyruvate [CPD:C02167]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+.
REFERENCE   1
  AUTHORS   Hayaishi, O.
  TITLE     Direct oxygenation by O2, oxygenases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 8, Academic Press, New York, 1963, p. 353-371.
REFERENCE   2
  AUTHORS   Sugiyama, S., Yano, K., Komagata, K. and Arima, K.
  TITLE     Metabolites of aromatic compounds by microbes. Part VII. Gentisic
            acid oxidase.
  JOURNAL   Bull. Agric. Chem. Soc. Jpn 24 (1960) 243-248.
  ORGANISM  Pseudomonas ovalis
REFERENCE   3
  AUTHORS   Sugiyama, S., Yano, K. and Arima, K.
  TITLE     Metabolites of aromatic compounds by microbes. Part VII. Further
            studies of gentisic acid oxidase.
  JOURNAL   Bull. Agric. Chem. Soc. Jpn 24 (1960) 249-254.
  ORGANISM  Pseudomonas ovalis
PATHWAY     PATH: map00350  Tyrosine metabolism
ORTHOLOGY   KO: K00450  gentisate 1,2-dioxygenase
GENES       AOR: AO090005000292
            ECW: EcE24377A_2433(gtdA)
            STY: STY2408
            STT: t0677
            SPT: SPA0673
            SEC: SC2195(gdo)
            STM: STM2178
            PAU: PA14_32690(gtdA)
            PAP: PSPA7_2768(gtdA)
            PEN: PSEEN2593(mhbD)
            RSO: RSc1087(nagI)
            REU: Reut_B5802 Reut_B5864
            REH: H16_B0873
            BXE: Bxe_A2627 Bxe_A4526
            BUR: Bcep18194_B1889
            BCN: Bcen_4221
            BCH: Bcen2424_4145
            POL: Bpro_2125
            EBA: ebA1373(nagI) ebA5613(nagI)
            AZO: azo2420(nagI)
            MES: Meso_0053
            BJA: blr0110 blr3412
            BRA: BRADO0683
            BBT: BBta_3243 BBta_7501
            SIL: SPO3690(gtdA-1) SPOA0115(gtdA-2)
            JAN: Jann_2910
            MMC: Mmcs_1628
            CGB: cg3351(nagI)
            RHA: RHA1_ro01866
            AAU: AAur_0331(gtdA)
STRUCTURES  PDB: 2D40  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.4
            ExPASy - ENZYME nomenclature database: 1.13.11.4
            ExplorEnz - The Enzyme Database: 1.13.11.4
            ERGO genome analysis and discovery system: 1.13.11.4
            BRENDA, the Enzyme Database: 1.13.11.4
            CAS: 9029-48-5
///
ENTRY       EC 1.13.11.5                Enzyme
NAME        homogentisate 1,2-dioxygenase;
            homogentisicase;
            homogentisate oxygenase;
            homogentisate dioxygenase;
            homogentisate oxidase;
            homogentisic acid oxidase;
            homogentisic acid oxygenase;
            homogentisic oxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     homogentisate:oxygen 1,2-oxidoreductase (decyclizing)
REACTION    homogentisate + O2 = 4-maleylacetoacetate [RN:R02519]
ALL_REAC    R02519
SUBSTRATE   homogentisate [CPD:C00544];
            O2 [CPD:C00007]
PRODUCT     4-maleylacetoacetate [CPD:C01036]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+.
REFERENCE   1  [PMID:5954067]
  AUTHORS   Adachi K, Iwayama Y, Tanioka H, Takeda Y.
  TITLE     Purification and properties of homogentisate oxygenase from
            Pseudomonas fluorescens.
  JOURNAL   Biochim. Biophys. Acta. 118 (1966) 88-97.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   2  [PMID:13174573]
  AUTHORS   CRANDALL DI, HALIKIS DN.
  TITLE     Homogentisic acid oxidase. I. Distribution in animal tissue and
            relation to tyrosine metabolism in rat kidney.
  JOURNAL   J. Biol. Chem. 208 (1954) 629-38.
  ORGANISM  rat [GN:rno], cow [GN:bta], pig [GN:ssc], gunea pig, rabbit
REFERENCE   3
  AUTHORS   Hayaishi, O.
  TITLE     Direct oxygenation by O2, oxygenases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 8, Academic Press, New York, 1963, p. 353-371.
REFERENCE   4  [PMID:14265758]
  AUTHORS   KITA H, KAMIMOTO M, SENOH S, ADACHI T, TAKEDA Y.
  TITLE     CRYSTALLIZATION AND SOME PROPERTIES OF
            3,4-DIHYDROXYPHENYLACETATE-2,3-OXYGENASE.
  JOURNAL   Biochem. Biophys. Res. Commun. 18 (1965) 66-70.
  ORGANISM  Pseudomonas ovalis
REFERENCE   5  [PMID:13271328]
  AUTHORS   KNOX WE, EDWARDS SW.
  TITLE     Homogentisate oxidase of liver.
  JOURNAL   J. Biol. Chem. 216 (1955) 479-87.
  ORGANISM  rat [GN:rno]
REFERENCE   6  [PMID:14832225]
  AUTHORS   RAVDIN RG, CRANDALL DI.
  TITLE     The enzymatic conversion of homogentisic acid to
            4-fumarylacetoacetic acid.
  JOURNAL   J. Biol. Chem. 189 (1951) 137-49.
  ORGANISM  Pseudomonas fluorescens, human [GN:hsa]
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00643  Styrene degradation
ORTHOLOGY   KO: K00451  homogentisate 1,2-dioxygenase
GENES       HSA: 3081(HGD)
            MMU: 15233(Hgd)
            RNO: 360719(Hgd)
            CFA: 478578(HGD)
            GGA: 418330(HGD)
            XLA: 447328(MGC82288)
            DRE: 259189(hgd)
            DME: Dmel_CG4779(hgo)
            CEL: W06D4.1(hgo-1)
            OSA: 4339844
            ANI: AN1897.2 AN6390.2
            AFM: AFUA_2G04220 AFUA_6G10810
            AOR: AO090003000210 AO090012000156
            UMA: UM01425.1
            DDI: DDB_0191461(hgd)
            TET: TTHERM_00446240
            XCC: XCC0438(hmgA)
            XCB: XC_0452
            XCV: XCV0484(hmgA)
            XAC: XAC0454(hmgA)
            XOO: XOO4070(hmgA)
            XOM: XOO_3845(XOO3845)
            PPR: PBPRB1165(hmgA)
            PAE: PA2009(hmgA)
            PAU: PA14_38510(hmgA)
            PAP: PSPA7_3280(hmgA)
            PPU: PP_4621(hmgA)
            PPF: Pput_4481
            PST: PSPTO_3551(hmgA)
            PSB: Psyr_3326
            PSP: PSPPH_3246(hmgA)
            PFL: PFL_0967(hmgA)
            PFO: Pfl_0910
            PEN: PSEEN4612(hmgA)
            SON: SO_1963
            SDN: Sden_2162
            SHE: Shewmr4_2291
            SHM: Shewmr7_2363
            SHN: Shewana3_2481
            PHA: PSHAb0338(hmgA)
            LPN: lpg1285
            LPF: lpl1248(hmgA)
            LPP: lpp1248(hmgA)
            NOC: Noc_1438
            HCH: HCH_00954(hmgA)
            MMW: Mmwyl1_2738
            AHA: AHA_2662(hmgA)
            CVI: CV_0970(hmgA)
            RSO: RSp0691(hmgA)
            REU: Reut_B3923
            REH: H16_B1671(hmgA)
            RME: Rmet_4374
            BMA: BMA2056(hmgA)
            BMV: BMASAVP1_A0856(hmgA)
            BML: BMA10299_A2688(hmgA)
            BMN: BMA10247_1921(hmgA)
            BXE: Bxe_A2725 Bxe_A3900 Bxe_C0994 Bxe_C1025
            BVI: Bcep1808_0757
            BUR: Bcep18194_A3913
            BCN: Bcen_0337
            BCH: Bcen2424_0820
            BAM: Bamb_0701
            BPS: BPSL2739(hmgA)
            BPM: BURPS1710b_3228(hmgA)
            BPL: BURPS1106A_3213(hmgA)
            BPD: BURPS668_3174(hmgA)
            BTE: BTH_I1397(hmgA)
            BPE: BP3134(hmgA)
            BPA: BPP0807(hmgA)
            BBR: BB0892(hmgA)
            POL: Bpro_2997
            MPT: Mpe_A0876
            BBA: Bd3185(hmgA)
            ADE: Adeh_3423
            MXA: MXAN_2787(hmgA)
            MLO: mlr8303
            MES: Meso_2456
            SME: SMc03208(hmgA)
            SMD: Smed_2833
            RET: RHE_CH01746(hmgA)
            RLE: RL1864(hmgA)
            BJA: bll0343
            BRA: BRADO6966(hmgA)
            BBT: BBta_0566(hmgA)
            RPA: RPA4672(hmgA)
            RPB: RPB_0907
            RPC: RPC_0891
            RPD: RPD_1018
            RPE: RPE_0912
            NHA: Nham_0921
            XAU: Xaut_3333
            CCR: CC_2532
            SIL: SPO0686(hmgA)
            SIT: TM1040_2621
            JAN: Jann_1439
            RDE: RD1_3651(hmgA)
            PDE: Pden_0913 Pden_3547
            SWI: Swit_1557 Swit_3864
            ABA: Acid345_2005
            SUS: Acid_6518
            BAN: BA0242
            BAR: GBAA0242
            BAA: BA_0810
            BAT: BAS0228
            BCE: BC0254
            BCA: BCE_0262
            BCZ: BCZK0217
            BTK: BT9727_0215
            BTL: BALH_0227(hmgA)
            MAV: MAV_4022(hmgA)
            MSM: MSMEG_2075(hmgA)
            MMC: Mmcs_1591
            NFA: nfa53040
            RHA: RHA1_ro02311(hmgA)
            SCO: SCO1715(hgd)
            SMA: SAV6587(hmgA)
            SEN: SACE_3944(hmgA)
            GFO: GFO_3171
            FPS: FP0225(hmgA)
            PTO: PTO1371
            SSO: SSO1533
STRUCTURES  PDB: 1EY2  1EYB  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.5
            ExPASy - ENZYME nomenclature database: 1.13.11.5
            ExplorEnz - The Enzyme Database: 1.13.11.5
            ERGO genome analysis and discovery system: 1.13.11.5
            UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.5
            BRENDA, the Enzyme Database: 1.13.11.5
            CAS: 9029-49-6
///
ENTRY       EC 1.13.11.6                Enzyme
NAME        3-hydroxyanthranilate 3,4-dioxygenase;
            3-hydroxyanthranilate oxygenase;
            3-hydroxyanthranilic acid oxygenase;
            3-hydroxyanthranilic oxygenase;
            3-hydroxyanthranilic acid oxidase;
            3HAO
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     3-hydroxyanthranilate:oxygen 3,4-oxidoreductase (decyclizing)
REACTION    3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde
            [RN:R02665]
ALL_REAC    R02665
SUBSTRATE   3-hydroxyanthranilate [CPD:C00632];
            O2 [CPD:C00007]
PRODUCT     2-amino-3-carboxymuconate semialdehyde [CPD:C04409]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+.
REFERENCE   1  [PMID:13884755]
  AUTHORS   DECKER RH, KANG HH, LEACH FR, HENDERSON LM.
  TITLE     Purification and properties of 3-hydroxyanthranilic acid oxidase.
  JOURNAL   J. Biol. Chem. 236 (1961) 3076-82.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   Hayaishi, O.
  TITLE     Direct oxygenation by O2, oxygenases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 8, Academic Press, New York, 1963, p. 353-371.
PATHWAY     PATH: map00380  Tryptophan metabolism
ORTHOLOGY   KO: K00452  3-hydroxyanthranilate 3,4-dioxygenase
GENES       HSA: 23498(HAAO)
            MMU: 107766(Haao)
            RNO: 56823(Haao)
            CFA: 611728(HAAO)
            GGA: 421396(HAAO)
            DRE: 492518(zgc:103585)
            SPU: 582154(LOC582154)
            CEL: K06A4.5
            CME: CMF152C
            SCE: YJR025C(BNA1)
            AGO: AGOS_ACL127W
            PIC: PICST_76205(BNA1)
            AFM: AFUA_2G17450 AFUA_8G04650
            AOR: AO090023000314 AO090102000066
            CNE: CNB05620
            UMA: UM05606.1
            DDI: DDB_0231359
            XCC: XCC1555(haaO)
            XCB: XC_2679
            XCV: XCV1645
            XAC: XAC1603(haaO)
            XOO: XOO2424(haaO)
            XOM: XOO_2302(XOO2302)
            REU: Reut_B5502
            RME: Rmet_5193
            BUR: Bcep18194_C7641
            POL: Bpro_5139
            MXA: MXAN_0919
            OAN: Oant_4402
            SIL: SPO1774
            SIT: TM1040_1592
            JAN: Jann_1447
            SWI: Swit_3523
            ABA: Acid345_0683
            BCA: BCE_2151
            BTL: BALH_1838
            STP: Strop_3522
            CHU: CHU_3382(nbaC)
            GFO: GFO_3400
            FJO: Fjoh_1221
            FPS: FP2235(haaO)
STRUCTURES  PDB: 1YFU  1YFW  1YFX  1YFY  1ZVF  2QNK  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.6
            ExPASy - ENZYME nomenclature database: 1.13.11.6
            ExplorEnz - The Enzyme Database: 1.13.11.6
            ERGO genome analysis and discovery system: 1.13.11.6
            UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.6
            BRENDA, the Enzyme Database: 1.13.11.6
            CAS: 9029-50-9
///
ENTRY       EC 1.13.11.7      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
COMMENT     Deleted entry: 3,4-dihydroxyphenylacetate 3,4-dioxygenase (EC
            1.13.11.7 created 1965 as EC 1.13.1.7, transferred 1972 to EC
            1.13.11.7, deleted 1980)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.7
            ExPASy - ENZYME nomenclature database: 1.13.11.7
            ExplorEnz - The Enzyme Database: 1.13.11.7
            ERGO genome analysis and discovery system: 1.13.11.7
            BRENDA, the Enzyme Database: 1.13.11.7
///
ENTRY       EC 1.13.11.8                Enzyme
NAME        protocatechuate 4,5-dioxygenase;
            protocatechuate 4,5-oxygenase;
            protocatechuic 4,5-dioxygenase;
            protocatechuic 4,5-oxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     protocatechuate:oxygen 4,5-oxidoreductase (decyclizing)
REACTION    protocatechuate + O2 = 4-carboxy-2-hydroxymuconate semialdehyde
            [RN:R01632]
ALL_REAC    R01632;
            (other) R03550 R04280
SUBSTRATE   protocatechuate [CPD:C00230];
            O2 [CPD:C00007]
PRODUCT     4-carboxy-2-hydroxymuconate semialdehyde [CPD:C04484]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+.
REFERENCE   1
  AUTHORS   Trippett, S., Dagley, S. and Stopher, D.A.
  TITLE     The bacterial oxidation of nicotinic acid.
  JOURNAL   Biochem. J. 76 (1960) 9.
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00623  2,4-Dichlorobenzoate degradation
ORTHOLOGY   KO: K04099  protocatechuate 4,5-dioxygenase
            KO: K04100  protocatechuate 4,5-dioxygenase, alpha chain
            KO: K04101  protocatechuate 4,5-dioxygenase, beta chain
GENES       SPE: Spro_2096
            XCC: XCC0804(pcaH) XCC0805(ligA)
            XCB: XC_3426 XC_3427
            XCV: XCV0913(ligB) XCV0914(ligA)
            XAC: XAC0878(pcaH) XAC0879(ligA)
            XOO: XOO3734(pcaH)
            XOM: XOO_3524(XOO3524) XOO_3525(XOO3525)
            PPU: PP_2518
            PPF: Pput_3200
            PAT: Patl_3885 Patl_3886
            CSA: Csal_0323 Csal_0324 Csal_0325
            MMW: Mmwyl1_0508 Mmwyl1_0509 Mmwyl1_3920 Mmwyl1_3938
            REU: Reut_B5775
            RME: Rmet_3709
            BUR: Bcep18194_C7572
            RFR: Rfer_0294 Rfer_0295 Rfer_0330 Rfer_0331
            PNA: Pnap_2027 Pnap_2028 Pnap_2733
            VEI: Veis_0170
            AZO: azo2523(ligA1) azo2538(ligA2) azo2868(ygiD)
            DAR: Daro_3248
            BRA: BRADO1853(ligB) BRADO2341(ligA) BRADO2342(ligB) BRADO2379
                 BRADO2380(mhpB)
            BBT: BBta_2174(ligB) BBta_2701(ligA) BBta_2702(ligB) BBta_2733
                 BBta_2734(mhpB)
            RPA: RPA1006 RPA1007(mhpB) RPA4701(ligA) RPA4702(ligB)
            RPB: RPB_0872 RPB_0873 RPB_1060 RPB_1061
            RPD: RPD_0982 RPD_0983
            RPE: RPE_0750 RPE_0751
            NAR: Saro_1233 Saro_1234 Saro_2812 Saro_2813
            MAG: amb0257 amb0258
            ART: Arth_4373
STRUCTURES  PDB: 1B4U  1BOU  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.8
            ExPASy - ENZYME nomenclature database: 1.13.11.8
            ExplorEnz - The Enzyme Database: 1.13.11.8
            ERGO genome analysis and discovery system: 1.13.11.8
            UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.8
            BRENDA, the Enzyme Database: 1.13.11.8
            CAS: 9029-56-5
///
ENTRY       EC 1.13.11.9                Enzyme
NAME        2,5-dihydroxypyridine 5,6-dioxygenase;
            2,5-dihydroxypyridine oxygenase;
            pyridine-2,5-diol dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     2,5-dihydroxypyridine:oxygen 5,6-oxidoreductase
REACTION    2,5-dihydroxypyridine + O2 + H2O = maleamate + formate [RN:R03204]
ALL_REAC    R03204
SUBSTRATE   2,5-dihydroxypyridine [CPD:C01059];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     maleamate [CPD:C01596];
            formate [CPD:C00058]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+.
REFERENCE   1  [PMID:13475371]
  AUTHORS   BEHRMAN EJ, STANIER RY.
  TITLE     The bacterial oxidation of nicotinic acid.
  JOURNAL   J. Biol. Chem. 228 (1957) 923-45.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   2  [PMID:5578917]
  AUTHORS   Gauthier JJ, Rittenberg SC.
  TITLE     The metabolism of nicotinic acid. I. Purification and properties of
            2,5-dihydroxypyridine oxygenase from Pseudomonas putida N-9.
  JOURNAL   J. Biol. Chem. 246 (1971) 3737-42.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   3  [PMID:5578918]
  AUTHORS   Gauthier JJ, Rittenberg SC.
  TITLE     The metabolism of nicotinic acid. II. 2,5-dihydroxypyridine
            oxidation, product formation, and oxygen 18 incorporation.
  JOURNAL   J. Biol. Chem. 246 (1971) 3743-8.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.9
            ExPASy - ENZYME nomenclature database: 1.13.11.9
            ExplorEnz - The Enzyme Database: 1.13.11.9
            ERGO genome analysis and discovery system: 1.13.11.9
            BRENDA, the Enzyme Database: 1.13.11.9
            CAS: 9029-57-6
///
ENTRY       EC 1.13.11.10               Enzyme
NAME        7,8-dihydroxykynurenate 8,8a-dioxygenase;
            7,8-dihydroxykynurenate oxygenase;
            7,8-dihydroxykynurenate 8,8alpha-dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     7,8-dihydroxykynurenate:oxygen 8,8a-oxidoreductase (decyclizing)
REACTION    7,8-dihydroxykynurenate + O2 =
            5-(3-carboxy-3-oxopropenyl)-4,6-dihydroxypyridine-2-carboxylate
            [RN:R03252]
ALL_REAC    R03252;
            (other) R03253
SUBSTRATE   7,8-dihydroxykynurenate [CPD:C01111];
            O2 [CPD:C00007]
PRODUCT     5-(3-carboxy-3-oxopropenyl)-4,6-dihydroxypyridine-2-carboxylate
            [CPD:C04826]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+.
REFERENCE   1
  AUTHORS   Kuno, S., Tashiro, M., Taniuchi, H., Horibata, K., Hayaishi, O.,
            Seno, S., Tokuyama, T. and Sakan, T.
  TITLE     Enzymatic degradation of kynurenic acid.
  JOURNAL   Fed. Proc. 20 (1961) 3.
PATHWAY     PATH: map00380  Tryptophan metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.10
            ExPASy - ENZYME nomenclature database: 1.13.11.10
            ExplorEnz - The Enzyme Database: 1.13.11.10
            ERGO genome analysis and discovery system: 1.13.11.10
            BRENDA, the Enzyme Database: 1.13.11.10
            CAS: 9029-58-7
///
ENTRY       EC 1.13.11.11               Enzyme
NAME        tryptophan 2,3-dioxygenase;
            tryptophan pyrrolase (ambiguous);
            tryptophanase;
            tryptophan oxygenase;
            tryptamine 2,3-dioxygenase;
            tryptophan peroxidase;
            indoleamine 2,3-dioxygenase (ambiguous);
            indolamine 2,3-dioxygenase (ambiguous);
            L-tryptophan pyrrolase;
            TDO;
            L-tryptophan 2,3-dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     L-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)
REACTION    L-tryptophan + O2 = N-formyl-L-kynurenine
ALL_REAC    (other) R00678
SUBSTRATE   L-tryptophan [CPD:C00078];
            O2 [CPD:C00007]
PRODUCT     N-formyl-L-kynurenine [CPD:C02700]
COFACTOR    Heme [CPD:C00032]
COMMENT     A protohemoprotein. In mammals, the enzyme appears to be located
            only in the liver. This enzyme, together with EC 1.13.11.52,
            indoleamine 2,3-dioxygenase, catalyses the first and rate-limiting
            step in the kynurenine pathway, the major pathway of tryptophan
            metabolism [5]. The enzyme is specific for tryptophan as substrate,
            but is far more active with L-tryptophan than with D-tryptophan [2].
REFERENCE   1  [PMID:6600455]
  AUTHORS   Uchida K, Shimizu T, Makino R, Sakaguchi K, Iizuka T, Ishimura Y,
            Nozawa T, Hatano M.
  TITLE     Magnetic and natural circular dichroism of L-tryptophan
            2,3-dioxygenases and indoleamine 2,3-dioxygenase. I. Spectra of
            ferric and ferrous high spin forms.
  JOURNAL   J. Biol. Chem. 258 (1983) 2519-25.
  ORGANISM  Pseudomonas acidovorans, rat [GN:rno]
REFERENCE   2  [PMID:8806758]
  AUTHORS   Ren S, Liu H, Licad E, Correia MA.
  TITLE     Expression of rat liver tryptophan 2,3-dioxygenase in Escherichia
            coli: structural and functional characterization of the purified
            enzyme.
  JOURNAL   Arch. Biochem. Biophys. 333 (1996) 96-102.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:8349662]
  AUTHORS   Leeds JM, Brown PJ, McGeehan GM, Brown FK, Wiseman JS.
  TITLE     Isotope effects and alternative substrate reactivities for
            tryptophan 2,3-dioxygenase.
  JOURNAL   J. Biol. Chem. 268 (1993) 17781-6.
  ORGANISM  Pseudomonas acidovorans, rat [GN:rno]
REFERENCE   4  [PMID:10719243]
  AUTHORS   Dang Y, Dale WE, Brown OR.
  TITLE     Comparative effects of oxygen on indoleamine 2,3-dioxygenase and
            tryptophan 2,3-dioxygenase of the kynurenine pathway.
  JOURNAL   Free. Radic. Biol. Med. 28 (2000) 615-24.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:12766158]
  AUTHORS   Littlejohn TK, Takikawa O, Truscott RJ, Walker MJ.
  TITLE     Asp274 and his346 are essential for heme binding and catalytic
            function of human indoleamine 2,3-dioxygenase.
  JOURNAL   J. Biol. Chem. 278 (2003) 29525-31.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00380  Tryptophan metabolism
ORTHOLOGY   KO: K00453  tryptophan 2,3-dioxygenase
GENES       HSA: 6999(TDO2)
            MMU: 56720(Tdo2)
            RNO: 64206(Tdo2)
            CFA: 475476(TDO2)
            GGA: 422409(TDO2)
            XLA: 495495(LOC495495)
            DRE: 334082(zgc:63488)
            SPU: 593764(LOC593764)
            DME: Dmel_CG2155(v)
            CME: CMT104C
            DDI: DDB_0231363(tdo)
            PLU: plu1434
            XCC: XCC0432 XCC1210
            XCB: XC_0446 XC_3032
            XCV: XCV0478
            XAC: XAC0448
            XOO: XOO4075
            XOM: XOO_3850(XOO3850)
            PAE: PA2579
            PAU: PA14_30750
            PAP: PSPA7_2637(kynA)
            PFL: PFL_0753
            PAT: Patl_0410
            RSO: RS01755(RSp0694)
            REU: Reut_A0807
            REH: H16_A2816(tdo1) H16_B1418(tdo2)
            RME: Rmet_2651
            BMA: BMA0351
            BMV: BMASAVP1_A0650(kynA)
            BML: BMA10299_A2485(kynA)
            BMN: BMA10247_0098(kynA)
            BXE: Bxe_A0733
            BUR: Bcep18194_A5910
            BCN: Bcen_1968
            BCH: Bcen2424_2579
            BAM: Bamb_2627
            BPS: BPSL0846
            BPM: BURPS1710b_1053
            BPL: BURPS1106A_0895(kynA)
            BPD: BURPS668_0892(kynA)
            BTE: BTH_I0709
            BPE: BP1233
            BPA: BPP1848
            BBR: BB3260
            POL: Bpro_3590
            BBA: Bd1810
            MXA: MXAN_7400
            MLO: mlr0620
            BJA: blr4158
            BRA: BRADO1529
            BBT: BBta_6511
            CCR: CC_2886
            SIL: SPOA0409
            SIT: TM1040_2226
            JAN: Jann_2084
            MMR: Mmar10_1469
            SAL: Sala_1391
            BAN: BA2751
            BAR: GBAA2751
            BAA: BA_3277
            BAT: BAS2565
            BCE: BC2757
            BCA: BCE_2785
            BCZ: BCZK2486
            BTK: BT9727_2521
            BCL: ABC0653
            OIH: OB0754
            RHA: RHA1_ro01801
            SCO: SCO3646(SCH10.24c)
            SMA: SAV4526(tdo)
            AAU: AAur_2058(kynA)
            TFU: Tfu_0921
            SEN: SACE_4055
            GVI: glr2058
            CHU: CHU_1409
            GFO: GFO_1393(tdo2) GFO_3168
            FPS: FP0228
            DRA: DR_A0339
            DGE: Dgeo_2857
STRUCTURES  PDB: 1YW0  2NOX  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.11
            ExPASy - ENZYME nomenclature database: 1.13.11.11
            ExplorEnz - The Enzyme Database: 1.13.11.11
            ERGO genome analysis and discovery system: 1.13.11.11
            BRENDA, the Enzyme Database: 1.13.11.11
            CAS: 9014-51-1
///
ENTRY       EC 1.13.11.12               Enzyme
NAME        lipoxygenase;
            lipoxidase;
            carotene oxidase;
            lipoperoxidase;
            fat oxidase;
            lipoxydase;
            lionoleate:O2 oxidoreductase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     linoleate:oxygen 13-oxidoreductase
REACTION    linoleate + O2 = (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
            [RN:R03626]
ALL_REAC    R03626;
            (other) R07864 R07869
SUBSTRATE   linoleate [CPD:C01595];
            O2 [CPD:C00007]
PRODUCT     (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate [CPD:C04717]
COFACTOR    Iron [CPD:C00023];
            PQQ [CPD:C00113]
COMMENT     An iron protein. Also oxidizes other methylene-interrupted
            polyunsaturated fatty acids.
REFERENCE   1
  AUTHORS   Christopher, J., Pistorius, E. and Axelrod, B.
  TITLE     Isolation of an enzyme of soybean lipoxidase.
  JOURNAL   Biochim. Biophys. Acta 198 (1970) 12-19.
  ORGANISM  Glycine max [GN:egma]
REFERENCE   2
  AUTHORS   Theorell, H., Holman, R.T. and Akesson, A.
  TITLE     Crystalline lipoxidase.
  JOURNAL   Acta Chem. Scand. 1 (1947) 571-576.
  ORGANISM  Glycine max [GN:egma]
REFERENCE   3  [PMID:5447012]
  AUTHORS   Zimmerman DC, Vick BA.
  TITLE     Specificity of flaxseed lipoxidase.
  JOURNAL   Lipids. 5 (1970) 392-7.
  ORGANISM  Glycine max [GN:egma], flaxseed
PATHWAY     PATH: map00591  Linoleic acid metabolism
            PATH: map00592  alpha-Linolenic acid metabolism
ORTHOLOGY   KO: K00454  lipoxygenase
GENES       DRE: 768204(zgc:152891)
            ATH: AT1G17420(LOX3) AT1G55020(LOX1) AT1G67560 AT1G72520 AT3G22400
                 AT3G45140(LOX2)
            OSA: 4328603 4331824 4333818 4333821 4333823 4334049 4335971
                 4338358 4345993 4345994 4350766 4352505 4352509
STRUCTURES  PDB: 1F8N  1FGM  1FGO  1FGQ  1FGR  1FGT  1HU9  1IK3  1JNQ  1N8Q  
                 1NO3  1ROV  1RRH  1RRL  1Y4K  1YGE  2IUK  2SBL  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.12
            ExPASy - ENZYME nomenclature database: 1.13.11.12
            ExplorEnz - The Enzyme Database: 1.13.11.12
            ERGO genome analysis and discovery system: 1.13.11.12
            BRENDA, the Enzyme Database: 1.13.11.12
            CAS: 9029-60-1
///
ENTRY       EC 1.13.11.13               Enzyme
NAME        ascorbate 2,3-dioxygenase;
            AAoxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     ascorbate:oxygen 2,3-oxidoreductase (bond-cleaving)
REACTION    ascorbate + O2 + H2O = oxalate + threonate [RN:R00646]
ALL_REAC    R00646
SUBSTRATE   ascorbate [CPD:C00072];
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     oxalate [CPD:C00209];
            threonate [CPD:C01620]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires iron(II).
REFERENCE   1  [PMID:5891457]
  AUTHORS   White GA, Krupka RM.
  TITLE     Ascorbic acid oxidase and ascorbic acid oxygenase of Myrothecium
            verrucaria.
  JOURNAL   Arch. Biochem. Biophys. 110 (1965) 448-61.
  ORGANISM  Myrothecium verrucaria
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.13
            ExPASy - ENZYME nomenclature database: 1.13.11.13
            ExplorEnz - The Enzyme Database: 1.13.11.13
            ERGO genome analysis and discovery system: 1.13.11.13
            BRENDA, the Enzyme Database: 1.13.11.13
            CAS: 37256-55-6
///
ENTRY       EC 1.13.11.14               Enzyme
NAME        2,3-dihydroxybenzoate 3,4-dioxygenase;
            o-pyrocatechuate oxygenase;
            2,3-dihydroxybenzoate 1,2-dioxygenase;
            2,3-dihydroxybenzoic oxygenase;
            2,3-dihydroxybenzoate oxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     2,3-dihydroxybenzoate:oxygen 3,4-oxidoreductase (decyclizing)
REACTION    2,3-dihydroxybenzoate + O2 = 3-carboxy-2-hydroxymuconate
            semialdehyde [RN:R01507]
ALL_REAC    R01507
SUBSTRATE   2,3-dihydroxybenzoate [CPD:C00196];
            O2 [CPD:C00007]
PRODUCT     3-carboxy-2-hydroxymuconate semialdehyde [CPD:C04480]
REFERENCE   1
  AUTHORS   Ribbons, D.W.
  TITLE     Bacterial oxidation of 2,3-dihydroxybenzoic acid - a new oxygenase.
  JOURNAL   Biochem. J. 99 (1966) 30.
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.14
            ExPASy - ENZYME nomenclature database: 1.13.11.14
            ExplorEnz - The Enzyme Database: 1.13.11.14
            ERGO genome analysis and discovery system: 1.13.11.14
            BRENDA, the Enzyme Database: 1.13.11.14
            CAS: 9032-31-9
///
ENTRY       EC 1.13.11.15               Enzyme
NAME        3,4-dihydroxyphenylacetate 2,3-dioxygenase;
            3,4-dihydroxyphenylacetic acid 2,3-dioxygenase;
            HPC dioxygenase;
            homoprotocatechuate 2,3-dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     3,4-dihydroxyphenylacetate:oxygen 2,3-oxidoreductase (decyclizing)
REACTION    3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate
            semialdehyde [RN:R03303]
ALL_REAC    R03303
SUBSTRATE   3,4-dihydroxyphenylacetate [CPD:C01161];
            O2 [CPD:C00007]
PRODUCT     2-hydroxy-5-carboxymethylmuconate semialdehyde [CPD:C04642]
COFACTOR    Iron [CPD:C00023]
COMMENT     An iron protein.
REFERENCE   1  [PMID:14263147]
  AUTHORS   ADACHI K, TAKEDA Y, SENOH S, KITA H.
  TITLE     METABOLISM OF P-HYDROXYPHENYLACETIC ACID IN PSEUDOMONAS OVALIS.
  JOURNAL   Biochim. Biophys. Acta. 93 (1964) 483-93.
  ORGANISM  Pseudomonas ovalis
REFERENCE   2  [PMID:6895079]
  AUTHORS   Barbour MG, Bayly RC.
  TITLE     Control of meta-cleavage degradation of 4-hydroxyphenylacetate in
            Pseudomonas putida.
  JOURNAL   J. Bacteriol. 147 (1981) 844-50.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   3  [PMID:588248]
  AUTHORS   Kutty RK, Devi NA, Veeraswamy M, Ramesh S, Rao PV.
  TITLE     Degradation of (+/-)-synephrine by Arthrobacter synephrinum.
            Oxidation of 3,4-dihydroxyphenylacetate to
            2-hydroxy-5-carboxymethyl-muconate semialdehyde.
  JOURNAL   Biochem. J. 167 (1977) 163-70.
  ORGANISM  Arthrobacter synephrinum
PATHWAY     PATH: map00350  Tyrosine metabolism
ORTHOLOGY   KO: K00455  3,4-dihydroxyphenylacetate 2,3-dioxygenase
GENES       ECX: EcHS_A4582(hpaD)
            STY: STY1137(hpcB)
            STT: t1816(hpcB)
            SPT: SPA1747(hpcB)
            SEC: SC1053(hpaD)
            STM: STM1103(hpaD)
            YPE: YPO1764(hpaD)
            YPK: y2545(hpaD)
            YPM: YP_1629(hpaD)
            YPA: YPA_1136
            YPN: YPN_2359
            YPP: YPDSF_1359
            YPS: YPTB1640(hpaD)
            YPI: YpsIP31758_2362(hpaD)
            SFL: SF4382(hpaD)
            SFX: S4652(hpaD)
            SFV: SFV_4382(hpaD)
            SSN: SSON_4497(hpaD)
            SBO: SBO_4410(hpaD)
            PLU: plu0987(hpcB)
            SPE: Spro_0628
            PMU: PM1531(hpaD)
            VVY: VV1588
            PAE: PA4124(hpcB)
            PAU: PA14_10620(hpcB)
            PAP: PSPA7_0968(hpaD)
            PFL: PFL_3373(hpaD)
            PEN: PSEEN3095(hpaD)
            MMW: Mmwyl1_3169
            REH: H16_A3520(paaA1)
            BMA: BMAA1137(hpcB)
            BML: BMA10299_0103(hpaD)
            BMN: BMA10247_A1510(hpaD)
            BXE: Bxe_A1145(amnB) Bxe_B2031
            BVI: Bcep1808_4804
            BUR: Bcep18194_B1780
            BCN: Bcen_4132
            BCH: Bcen2424_4234
            BAM: Bamb_3656
            BPS: BPSS0695(hpcB)
            BPM: BURPS1710b_A2267(hpaD)
            BPL: BURPS1106A_A0941(hpaD)
            BPD: BURPS668_A1026(hpaD)
            BTE: BTH_II1732(hpaD)
            BBR: BB0737(hpaD)
            BRA: BRADO4665(hpcB)
            BBT: BBta_3528(hpcB)
            RPA: RPA1663(hpaD)
            RPB: RPB_3868
            SIL: SPOA0026(hpcB)
            MAG: amb0804
            BLI: BL03909
            BLD: BLi03991
            OIH: OB2868
            GKA: GK3033
            GTN: GTNG_2991
            NFA: nfa27760
            SEN: SACE_3544(paaA1)
STRUCTURES  PDB: 1F1R  1F1U  1F1V  1F1X  1Q0C  1Q0O  2IG9  2IGA  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.15
            ExPASy - ENZYME nomenclature database: 1.13.11.15
            ExplorEnz - The Enzyme Database: 1.13.11.15
            ERGO genome analysis and discovery system: 1.13.11.15
            UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.15
            BRENDA, the Enzyme Database: 1.13.11.15
            CAS: 37256-56-7
///
ENTRY       EC 1.13.11.16               Enzyme
NAME        3-carboxyethylcatechol 2,3-dioxygenase;
            2,3-dihydroxy-beta-phenylpropionic dioxygenase;
            2,3-dihydroxy-beta-phenylpropionate oxygenase;
            3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase
            (decyclizing)
REACTION    3-(2,3-dihydroxyphenyl)propanoate + O2 =
            2-hydroxy-6-oxonona-2,4-diene-1,9-dioate [RN:R04376]
ALL_REAC    R04376;
            (other) R06788
SUBSTRATE   3-(2,3-dihydroxyphenyl)propanoate [CPD:C04044];
            O2 [CPD:C00007]
PRODUCT     2-hydroxy-6-oxonona-2,4-diene-1,9-dioate [CPD:C04479]
COFACTOR    Iron [CPD:C00023]
COMMENT     An iron protein.
REFERENCE   1  [PMID:5881653]
  AUTHORS   Dagley S, Chapman PJ, Gibson DT.
  TITLE     The metabolism of beta-phenylpropionic acid by an Achromobacter.
  JOURNAL   Biochem. J. 97 (1965) 643-50.
  ORGANISM  Achromobacter sp.
PATHWAY     PATH: map00360  Phenylalanine metabolism
ORTHOLOGY   KO: K05713  2,3-dihydroxyphenylpropionate 1,2-dioxygenase
GENES       ECO: b0348(mhpB)
            ECJ: JW0339(mhpB)
            ECE: Z0446(mhpB)
            ECS: ECs0403
            SSN: SSON_0295(mhpB)
            PLU: plu2208
            REU: Reut_A0271
            BPA: BPP3697
            BBR: BB4131
            DAR: Daro_1353
            MPA: MAP0695(mhpB)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.16
            ExPASy - ENZYME nomenclature database: 1.13.11.16
            ExplorEnz - The Enzyme Database: 1.13.11.16
            ERGO genome analysis and discovery system: 1.13.11.16
            BRENDA, the Enzyme Database: 1.13.11.16
            CAS: 105503-63-7
///
ENTRY       EC 1.13.11.17               Enzyme
NAME        indole 2,3-dioxygenase;
            indole oxidase;
            indoleamine 2,3-dioxygenase (ambiguous);
            indole:O2 oxidoreductase;
            indole-oxygen 2,3-oxidoreductase (decyclizing);
            IDO (ambiguous)
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     indole:oxygen 2,3-oxidoreductase (decyclizing)
REACTION    indole + O2 = 2-formylaminobenzaldehyde [RN:R02338]
ALL_REAC    R02338
SUBSTRATE   indole [CPD:C00463];
            O2 [CPD:C00007]
PRODUCT     2-formylaminobenzaldehyde [CPD:C03574]
COFACTOR    Copper [CPD:C00070];
            Flavin [CPD:C00176];
            Flavoprotein [CPD:C06411]
COMMENT     The enzyme from the plant Jasminum grandiflorum is a flavoprotein
            containing copper, and forms anthranilate as the final product. One
            enzyme from Tecoma stans is also a flavoprotein containing copper
            and uses three atoms of oxygen per molecule of indole, to form
            anthranil (3,4-benzoisoxazol). A second enzyme from Tecoma stans,
            which is not a flavoprotein, uses four atoms of oxygen and forms
            anthranilate as the final product.
REFERENCE   1
  AUTHORS   Divakar, N.G., Subramanian, V., Sugumaran, M. and Vaidyanathan, C.S.
  TITLE     Indole oxygenase from the leaves of Jasminum grandiflorum.
  JOURNAL   Plant Sci. Lett. 15 (1979) 177-181.
  ORGANISM  Jasminum grandiflorum
REFERENCE   2
  AUTHORS   Kunapuli, S.P. and Vaidyanathan, C.S.
  TITLE     Purification and characterization of a new indole oxygenase from the
            leaves of Tecoma stans L.
  JOURNAL   Plant Physiol. 71 (1983) 19-23.
  ORGANISM  Tecoma stans
REFERENCE   3
  AUTHORS   Nair, P.M. and Vaidyanathan, C.S.
  TITLE     An indole oxidase isolated from the leaves of Tecoma stans.
  JOURNAL   Biochim. Biophys. Acta 81 (1964) 496-506.
  ORGANISM  Tecoma stans
PATHWAY     PATH: map00380  Tryptophan metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.17
            ExPASy - ENZYME nomenclature database: 1.13.11.17
            ExplorEnz - The Enzyme Database: 1.13.11.17
            ERGO genome analysis and discovery system: 1.13.11.17
            BRENDA, the Enzyme Database: 1.13.11.17
            CAS: 37256-57-8
///
ENTRY       EC 1.13.11.18               Enzyme
NAME        sulfur dioxygenase;
            sulfur oxygenase;
            sulfur:oxygen oxidoreductase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     S-sulfanylglutathione:oxygen oxidoreductase
REACTION    (1) (1a) glutathione + sulfur = S-sulfanylglutathione (spontaneous)
            [RN:R00781];
            (2) (1b) S-sulfanylglutathione + O2 + H2O = glutathione + sulfite +
            2 H+
ALL_REAC    R00781
SUBSTRATE   glutathione [CPD:C00051];
            sulfur [CPD:C00087];
            S-sulfanylglutathione;
            O2 [CPD:C00007];
            H2O [CPD:C00001]
PRODUCT     S-sulfanylglutathione (spontaneous);
            glutathione [CPD:C00051];
            sulfite [CPD:C00094];
            H+ [CPD:C00080]
COFACTOR    Iron [CPD:C00023]
COMMENT     An iron protein. Glutathione (GSH) plays a catalytic role in
            elemental sulfur activation, but is not consumed during the enzymic
            reaction. GSH and elemental sulfur react non-enzymically to yield
            S-sulfanylglutathione and it is only in this form that the sulfur
            can be oxidized to yield sulfite. The sulfite can be further
            converted into sulfate, thiosulfate or S-sulfoglutathione (GSSO3-)
            non-enzymically [2].
REFERENCE   1  [PMID:5968172]
  AUTHORS   Suzuki I, Silver M.
  TITLE     The initial product and properties of the sulfur-oxidizing enzyme of
            thiobacilli.
  JOURNAL   Biochim. Biophys. Acta. 122 (1966) 22-33.
  ORGANISM  Thiobacillus thioparus, Thiobacillus thiooxidans
REFERENCE   2  [PMID:12855721]
  AUTHORS   Rohwerder T, Sand W.
  TITLE     The sulfane sulfur of persulfides is the actual substrate of the
            sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium
            spp.
  JOURNAL   Microbiology. 149 (2003) 1699-710.
  ORGANISM  Acidiphilium acidophilum, Acidithiobacillus thiooxidans,
            Acidithiobacillus ferrooxidans
PATHWAY     PATH: map00920  Sulfur metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.18
            ExPASy - ENZYME nomenclature database: 1.13.11.18
            ExplorEnz - The Enzyme Database: 1.13.11.18
            ERGO genome analysis and discovery system: 1.13.11.18
            BRENDA, the Enzyme Database: 1.13.11.18
            CAS: 37256-58-9
///
ENTRY       EC 1.13.11.19               Enzyme
NAME        cysteamine dioxygenase;
            persulfurase;
            cysteamine oxygenase;
            cysteamine:oxygen oxidoreductase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     2-aminoethanethiol:oxygen oxidoreductase
REACTION    2-aminoethanethiol + O2 = hypotaurine [RN:R02467]
ALL_REAC    R02467
SUBSTRATE   2-aminoethanethiol [CPD:C01678];
            O2 [CPD:C00007]
PRODUCT     hypotaurine [CPD:C00519]
COFACTOR    Iron [CPD:C00023]
COMMENT     A non-heme iron protein that is involved in the biosynthesis of
            taurine. Requires catalytic amounts of a cofactor-like compound,
            such as sulfur, sufide, selenium or methylene blue for maximal
            activity. 3-Aminopropanethiol (homocysteamine) and 2-mercaptoethanol
            can also act as substrates, but glutathione, cysteine, and cysteine
            ethyl- and methyl esters are not good substrates [1,3].
REFERENCE   1  [PMID:5912113]
  AUTHORS   Cavallini D, De Marco C, Scandurra R, Dupre S, Graziani MT.
  TITLE     The enzymatic oxidation of cysteamine to hypotaurine. Purification
            and properties of the enzyme.
  JOURNAL   J. Biol. Chem. 241 (1966) 3189-96.
  ORGANISM  horse
REFERENCE   2  [PMID:6052430]
  AUTHORS   Wood JL, Cavallini D.
  TITLE     Enzymic oxidation of cysteamine to hypotaurine in the absence of a
            cofactor.
  JOURNAL   Arch. Biochem. Biophys. 119 (1967) 368-72.
  ORGANISM  horse
REFERENCE   3  [PMID:1157952]
  AUTHORS   Cavallini D, Federici G, Ricci G, Dupre S, Antonucci A.
  TITLE     The specificity of cysteamine oxygenase.
  JOURNAL   FEBS. Lett. 56 (1975) 348-51.
REFERENCE   4  [PMID:3657558]
  AUTHORS   Richerson RB, Ziegler DM.
  TITLE     Cysteamine dioxygenase.
  JOURNAL   Methods. Enzymol. 143 (1987) 410-5.
  ORGANISM  horse
PATHWAY     PATH: map00430  Taurine and hypotaurine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.19
            ExPASy - ENZYME nomenclature database: 1.13.11.19
            ExplorEnz - The Enzyme Database: 1.13.11.19
            ERGO genome analysis and discovery system: 1.13.11.19
            BRENDA, the Enzyme Database: 1.13.11.19
            CAS: 9033-41-4
///
ENTRY       EC 1.13.11.20               Enzyme
NAME        cysteine dioxygenase;
            cysteine oxidase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     L-cysteine:oxygen oxidoreductase
REACTION    L-cysteine + O2 = 3-sulfinoalanine [RN:R00893]
ALL_REAC    R00893
SUBSTRATE   L-cysteine [CPD:C00097];
            O2 [CPD:C00007]
PRODUCT     3-sulfinoalanine [CPD:C00606]
COFACTOR    NADH [CPD:C00004];
            NADPH [CPD:C00005];
            Iron [CPD:C00023]
COMMENT     Requires Fe2+ and NAD(P)H.
REFERENCE   1  [PMID:5767301]
  AUTHORS   Lombardini JB, Singer TP, Boyer PD.
  TITLE     Cystein oxygenase. II. Studies on the mechanism of the reaction with
            18oxygen.
  JOURNAL   J. Biol. Chem. 244 (1969) 1172-5.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00272  Cysteine metabolism
            PATH: map00430  Taurine and hypotaurine metabolism
ORTHOLOGY   KO: K00456  cysteine dioxygenase
GENES       HSA: 1036(CDO1)
            PTR: 462010(CDO1)
            MMU: 12583(Cdo1)
            RNO: 81718(Cdo1)
            CFA: 474637(CDO1)
            GGA: 427391(CDO1)
            XLA: 398963(MGC68656) 443755(MGC81086)
            XTR: 394737(MGC75851)
            DRE: 393714(cdo1)
            SPU: 575999(LOC575999)
            DME: Dmel_CG5493
            CEL: F56F10.3
            PIC: PICST_43654(CDG1)
            ANI: AN4081.2
            AFM: AFUA_1G05570 AFUA_5G14410
            AOR: AO090011000009 AO090020000659
            DDI: DDB_0231093
            REH: H16_B1863(cdo)
STRUCTURES  PDB: 2ATF  2B5H  2GH2  2IC1  2Q4S  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.20
            ExPASy - ENZYME nomenclature database: 1.13.11.20
            ExplorEnz - The Enzyme Database: 1.13.11.20
            ERGO genome analysis and discovery system: 1.13.11.20
            BRENDA, the Enzyme Database: 1.13.11.20
            CAS: 37256-59-0
///
ENTRY       EC 1.13.11.21     Obsolete  Enzyme
NAME        Transferred to 1.14.99.36
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
COMMENT     Transferred entry: now EC 1.14.99.36 beta-carotene
            15,15'-monooxygenase (EC 1.13.11.21 created 1972, deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.21
            ExPASy - ENZYME nomenclature database: 1.13.11.21
            ExplorEnz - The Enzyme Database: 1.13.11.21
            ERGO genome analysis and discovery system: 1.13.11.21
            BRENDA, the Enzyme Database: 1.13.11.21
///
ENTRY       EC 1.13.11.22               Enzyme
NAME        caffeate 3,4-dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     3,4-dihydroxy-trans-cinnamate:oxygen 3,4-oxidoreductase
            (decyclizing)
REACTION    3,4-dihydroxy-trans-cinnamate + O2 =
            3-(2-carboxyethenyl)-cis,cis-muconate [RN:R03365]
ALL_REAC    R03365
SUBSTRATE   3,4-dihydroxy-trans-cinnamate [CPD:C01197];
            O2 [CPD:C00007]
PRODUCT     3-(2-carboxyethenyl)-cis,cis-muconate [CPD:C04366]
REFERENCE   1  [PMID:5776526]
  AUTHORS   Seidman MM, Toms A, Wood JM.
  TITLE     Influence of side-chain substituents on the position of cleavage of
            the benzene ring by Pseudomonas fluorescens.
  JOURNAL   J. Bacteriol. 97 (1969) 1192-7.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.22
            ExPASy - ENZYME nomenclature database: 1.13.11.22
            ExplorEnz - The Enzyme Database: 1.13.11.22
            ERGO genome analysis and discovery system: 1.13.11.22
            BRENDA, the Enzyme Database: 1.13.11.22
            CAS: 37256-61-4
///
ENTRY       EC 1.13.11.23               Enzyme
NAME        2,3-dihydroxyindole 2,3-dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     2,3-dihydroxyindole:oxygen 2,3-oxidoreductase (decyclizing)
REACTION    2,3-dihydroxyindole + O2 = anthranilate + CO2 [RN:R00983]
ALL_REAC    R00983
SUBSTRATE   2,3-dihydroxyindole [CPD:C02775];
            O2 [CPD:C00007]
PRODUCT     anthranilate [CPD:C00108];
            CO2 [CPD:C00011]
REFERENCE   1  [PMID:5652436]
  AUTHORS   Fujioka M, Wada H.
  TITLE     The bacterial oxidation of indole.
  JOURNAL   Biochim. Biophys. Acta. 158 (1968) 70-8.
PATHWAY     PATH: map00380  Tryptophan metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.23
            ExPASy - ENZYME nomenclature database: 1.13.11.23
            ExplorEnz - The Enzyme Database: 1.13.11.23
            ERGO genome analysis and discovery system: 1.13.11.23
            BRENDA, the Enzyme Database: 1.13.11.23
            CAS: 37256-62-5
///
ENTRY       EC 1.13.11.24               Enzyme
NAME        quercetin 2,3-dioxygenase;
            quercetinase;
            flavonol 2,4-oxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     quercetin:oxygen 2,3-oxidoreductase (decyclizing)
REACTION    quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate +
            CO + H+ [RN:R02156]
ALL_REAC    R02156
SUBSTRATE   quercetin [CPD:C00389];
            O2 [CPD:C00007]
PRODUCT     2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate [CPD:C04524];
            CO [CPD:C00237];
            H+ [CPD:C00080]
COFACTOR    Iron [CPD:C00023];
            Copper [CPD:C00070]
COMMENT     The enzyme from Aspergillus sp. is a copper protein whereas that
            from Bacillus subtilis contains iron. Quercetin is a flavonol
            (5,7,3',4'-tetrahydroxyflavonol).
REFERENCE   1  [PMID:5579942]
  AUTHORS   Oka T, Simpson FJ.
  TITLE     Quercetinase, a dioxygenase containing copper.
  JOURNAL   Biochem. Biophys. Res. Commun. 43 (1971) 1-5.
  ORGANISM  Aspergillus flavus
REFERENCE   2  [PMID:12486225]
  AUTHORS   Steiner RA, Kalk KH, Dijkstra BW.
  TITLE     Anaerobic enzyme.substrate structures provide insight into the
            reaction mechanism of the copper-dependent quercetin
            2,3-dioxygenase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 16625-30.
  ORGANISM  Aspergillus flavus
REFERENCE   3  [PMID:14741339]
  AUTHORS   Bowater L, Fairhurst SA, Just VJ, Bornemann S.
  TITLE     Bacillus subtilis YxaG is a novel Fe-containing quercetin
            2,3-dioxygenase.
  JOURNAL   FEBS. Lett. 557 (2004) 45-8.
  ORGANISM  Bacillus subtilis [GN:bsu]
ORTHOLOGY   KO: K07155  quercetin 2,3-dioxygenase
GENES       BSU: BG11109(yxaG)
STRUCTURES  PDB: 1GQG  1GQH  1H1I  1H1M  1JUH  2H0V  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.24
            ExPASy - ENZYME nomenclature database: 1.13.11.24
            ExplorEnz - The Enzyme Database: 1.13.11.24
            ERGO genome analysis and discovery system: 1.13.11.24
            UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.24
            BRENDA, the Enzyme Database: 1.13.11.24
            CAS: 9075-67-6
///
ENTRY       EC 1.13.11.25               Enzyme
NAME        3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione
            4,5-dioxygenase;
            steroid 4,5-dioxygenase;
            3-alkylcatechol 2,3-dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione:oxygen
            4,5-oxidoreductase (decyclizing)
REACTION    3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + O2 =
            3-hydroxy-5,9,17-trioxo-4,5:9,10-disecoandrosta-1(10),2-dien-4-oate
            [RN:R04597]
ALL_REAC    R04597
SUBSTRATE   3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione
            [CPD:C04793];
            O2 [CPD:C00007]
PRODUCT     3-hydroxy-5,9,17-trioxo-4,5:9,10-disecoandrosta-1(10),2-dien-4-oate
            [CPD:C04844]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+. Also acts on 3-isopropylcatechol and
            3-tert-butyl-5-methylcatechol.
REFERENCE   1  [PMID:5908121]
  AUTHORS   Gibson DT, Wang KC, Sih CJ, Whitlock H Jr.
  TITLE     Mechanisms of steroid oxidation by microorganisms. IX. On the
            mechanism of ring A cleavage in the degradation of 9,10-seco
            steroids by microorganisms.
  JOURNAL   J. Biol. Chem. 241 (1966) 551-9.
  ORGANISM  Nacardia restrictus
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.25
            ExPASy - ENZYME nomenclature database: 1.13.11.25
            ExplorEnz - The Enzyme Database: 1.13.11.25
            ERGO genome analysis and discovery system: 1.13.11.25
            UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.25
            BRENDA, the Enzyme Database: 1.13.11.25
            CAS: 37256-63-6
///
ENTRY       EC 1.13.11.26               Enzyme
NAME        peptide-tryptophan 2,3-dioxygenase;
            pyrrolooxygenase;
            peptidyltryptophan 2,3-dioxygenase;
            tryptophan pyrrolooxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     peptide-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)
REACTION    peptide tryptophan + O2 = peptide formylkynurenine [RN:R04032]
ALL_REAC    R04032
SUBSTRATE   peptide tryptophan [CPD:C02732];
            O2 [CPD:C00007]
PRODUCT     peptide formylkynurenine [CPD:C03529]
COMMENT     Also acts on tryptophan.
REFERENCE   1  [PMID:4403729]
  AUTHORS   Frydman RB, Tomaro ML, Frydman B.
  TITLE     Pyrrolooxygenase: its action on tryptophan-containing enzymes and
            peptides.
  JOURNAL   Biochim. Biophys. Acta. 284 (1972) 80-9.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.26
            ExPASy - ENZYME nomenclature database: 1.13.11.26
            ExplorEnz - The Enzyme Database: 1.13.11.26
            ERGO genome analysis and discovery system: 1.13.11.26
            BRENDA, the Enzyme Database: 1.13.11.26
            CAS: 37256-64-7
///
ENTRY       EC 1.13.11.27               Enzyme
NAME        4-hydroxyphenylpyruvate dioxygenase;
            p-hydroxyphenylpyruvic hydroxylase;
            p-hydroxyphenylpyruvate hydroxylase;
            p-hydroxyphenylpyruvate oxidase;
            p-hydroxyphenylpyruvic oxidase;
            p-hydroxyphenylpyruvate dioxygenase;
            p-hydroxyphenylpyruvic acid hydroxylase;
            4-hydroxyphenylpyruvic acid dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     4-hydroxyphenylpyruvate:oxygen oxidoreductase (hydroxylating,
            decarboxylating)
REACTION    4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 [RN:R02521]
ALL_REAC    R02521;
            (other) R01372
SUBSTRATE   4-hydroxyphenylpyruvate [CPD:C01179];
            O2 [CPD:C00007]
PRODUCT     homogentisate [CPD:C00544];
            CO2 [CPD:C00011]
COMMENT     The Pseudomonas enzyme contains one Fe3+ per mole of enzyme; the
            enzymes from other sources may contain essential iron or copper.
REFERENCE   1  [PMID:7118918]
  AUTHORS   Lindstedt S, Rundgren M.
  TITLE     Blue color, metal content, and substrate binding in
            4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P.
            J. 874.
  JOURNAL   J. Biol. Chem. 257 (1982) 11922-31.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:7103516]
  AUTHORS   Roche PA, Moorehead TJ, Hamilton GA.
  TITLE     Purification and properties of hog liver 4-hydroxyphenylpyruvate
            dioxygenase.
  JOURNAL   Arch. Biochem. Biophys. 216 (1982) 62-73.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
ORTHOLOGY   KO: K00457  4-hydroxyphenylpyruvate dioxygenase
GENES       HSA: 3242(HPD)
            PTR: 473296(HPD)
            MMU: 15445(Hpd)
            RNO: 29531(Hpd)
            CFA: 610778(HPD)
            SSC: 397443(HPD)
            GGA: 416852(HPD)
            XLA: 398893(MGC68535) 495029(LOC495029)
            DRE: 394142(zgc:56326)
            DME: Dmel_CG11796
            CEL: T21C12.2(hpd-1)
            ATH: AT1G06570(PDS1)
            OSA: 4328425
            CME: CMI063C
            PIC: PICST_46345(HPD1)
            ANI: AN1899.2
            AFM: AFUA_1G11560 AFUA_2G04200 AFUA_4G10620
            AOR: AO090003000208 AO090038000266
            TET: TTHERM_00678260
            XCC: XCC0436
            XCB: XC_0450
            XCV: XCV0482
            XAC: XAC0452
            XOO: XOO4071
            XOM: XOO_3846(XOO3846)
            VCH: VC1344
            VCO: VC0395_A0960(hppD)
            VVU: VV1_2768
            VVY: VV1495
            VPA: VP1349
            PPR: PBPRB1180
            PAE: PA0242 PA0865(hpd)
            PAU: PA14_03000 PA14_53070(hpd)
            PAP: PSPA7_4652(hppD)
            PPU: PP_2554 PP_3433(hpd)
            PPF: Pput_2329 Pput_3161
            PST: PSPTO_2346 PSPTO_3553(hppD)
            PSB: Psyr_2130 Psyr_3330
            PSP: PSPPH_2105 PSPPH_3250(hppD)
            PFL: PFL_3387(hppD) PFL_5385
            PFO: Pfl_2917 Pfl_4905
            PEN: PSEEN2014 PSEEN3054(hpd)
            PMY: Pmen_1696
            PCR: Pcryo_1555
            PRW: PsycPRwf_1040
            ACB: A1S_3418
            SON: SO_1962
            SDN: Sden_2163
            SFR: Sfri_2327
            SAZ: Sama_1568
            SBL: Sbal_2616
            SBM: Shew185_2654
            SLO: Shew_2155
            SPC: Sputcn32_1670
            SSE: Ssed_2687
            SPL: Spea_1873
            SHE: Shewmr4_2292
            SHM: Shewmr7_2364
            SHN: Shewana3_2482
            SHW: Sputw3181_2355
            ILO: IL0722
            CPS: CPS_3484(hppD)
            PHA: PSHAa2168(melA)
            PAT: Patl_1125 Patl_2997
            LPN: lpg2278(hpd)
            LPF: lpl2204(lly)
            LPP: lpp2232(lly)
            NOC: Noc_1437
            HCH: HCH_00955(hppD)
            CSA: Csal_0292
            MMW: Mmwyl1_2737
            AHA: AHA_2663(hppD)
            CVI: CV_0969(hpd)
            RSO: RS02058(RSp1400) RS04776(RSp1347) RS05661(RSp1316)
                 RSc3103(RS00556)
            REU: Reut_B4501 Reut_B5028 Reut_B5035
            REH: H16_B1083(hpd)
            RME: Rmet_4925
            BMA: BMA2582(hppD) BMAA0848
            BMV: BMASAVP1_1752 BMASAVP1_A0003(hppD-1) BMASAVP1_A3120(hppD-2)
            BML: BMA10299_2205 BMA10299_A1975(hppD)
            BMN: BMA10247_3528(hppD) BMA10247_A0891
            BXE: Bxe_A0286 Bxe_B0882 Bxe_B2773
            BVI: Bcep1808_0303 Bcep1808_3553 Bcep1808_4921
            BUR: Bcep18194_A3420 Bcep18194_B0343 Bcep18194_B1625
            BCN: Bcen_2785 Bcen_3062 Bcen_3972
            BCH: Bcen2424_0321 Bcen2424_4395 Bcen2424_5305
            BAM: Bamb_0240 Bamb_3806 Bamb_4666
            BPS: BPSL3239 BPSS0339
            BPM: BURPS1710b_0016(hppD) BURPS1710b_A1894
            BPL: BURPS1106A_3845(hppD) BURPS1106A_A0481(hppD)
            BPD: BURPS668_3784(hppD) BURPS668_A0577
            BTE: BTH_I3106(hppD) BTH_II1222 BTH_II2059
            BPE: BP3040(bllY)
            BPA: BPP3767(bllY)
            BBR: BB4213(bllY)
            POL: Bpro_4213 Bpro_4496
            PNA: Pnap_1120 Pnap_1560
            AAV: Aave_4191
            AJS: Ajs_0520
            VEI: Veis_2137
            MPT: Mpe_A0346
            AZO: azo1193(hppD)
            BBA: Bd3543
            ADE: Adeh_3422
            AFW: Anae109_3484
            MXA: MXAN_2786(hppD)
            MLO: mll8309
            MES: Meso_0782 Meso_2885
            SME: SMb20581 SMc03211
            SMD: Smed_2836
            ATU: Atu4529
            ATC: AGR_L_678
            RET: RHE_CH01745(ypch00593) RHE_PC00215(ypc00119)
            RLE: RL1863 RL2846 pRL110074
            OAN: Oant_4428
            BJA: bll0339 bll1053
            BRA: BRADO5592 BRADO6961(hpd)
            BBT: BBta_0570(hpd) BBta_6113
            RPA: RPA0005(hpd)
            CCR: CC_2533
            SIL: SPO1426(hppD)
            SIT: TM1040_0582
            JAN: Jann_3260
            RDE: RD1_1830(hppD)
            PDE: Pden_1664
            MMR: Mmar10_0336
            HNE: HNE_2900(hppD)
            NAR: Saro_0597 Saro_1586
            SAL: Sala_3119
            SWI: Swit_3865
            ELI: ELI_06415
            GOX: GOX0471
            ABA: Acid345_2004
            SUS: Acid_4167
            BAN: BA0240(hppD)
            BAR: GBAA0240(hppD)
            BAA: BA_0807
            BAT: BAS0226
            BCE: BC0252
            BCA: BCE_0260(hppD)
            BCZ: BCZK0215(hppD)
            BCY: Bcer98_0228
            BTK: BT9727_0213(hppD)
            BTL: BALH_0225(hppD)
            NFA: nfa50810
            RHA: RHA1_ro01367 RHA1_ro02040 RHA1_ro03041(hpd1)
                 RHA1_ro03170(hpd2) RHA1_ro05074(hpd3)
            SCO: SCO2927(SCE19A.27c)
            SMA: SAV1776 SAV5149(hpd)
            NCA: Noca_1295
            FRA: Francci3_2454
            SEN: SACE_0905(hpd3)
            STP: Strop_2490 Strop_2727 Strop_4250
            SYN: slr0090(ppd)
            CYA: CYA_0478
            CYB: CYB_0246
            GVI: glr3091
            ANA: all0771
            AVA: Ava_4666
            TER: Tery_4182
            SRU: SRU_1370(hppD)
            GFO: GFO_3170
            FJO: Fjoh_0729
            FPS: FP0226(hppD)
            DGE: Dgeo_2375
            PTO: PTO1369
STRUCTURES  PDB: 1CJX  1SP9  1SQD  1T47  1TFZ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.27
            ExPASy - ENZYME nomenclature database: 1.13.11.27
            ExplorEnz - The Enzyme Database: 1.13.11.27
            ERGO genome analysis and discovery system: 1.13.11.27
            UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.27
            BRENDA, the Enzyme Database: 1.13.11.27
            CAS: 9029-72-5
///
ENTRY       EC 1.13.11.28               Enzyme
NAME        2,3-dihydroxybenzoate 2,3-dioxygenase;
            2,3-dihydroxybenzoate 2,3-oxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     2,3-dihydroxybenzoate:oxygen 2,3-oxidoreductase (decyclizing)
REACTION    2,3-dihydroxybenzoate + O2 = 2-carboxy-cis,cis-muconate [RN:R01506]
ALL_REAC    R01506
SUBSTRATE   2,3-dihydroxybenzoate [CPD:C00196];
            O2 [CPD:C00007]
PRODUCT     2-carboxy-cis,cis-muconate [CPD:C03666]
COMMENT     Also acts, more slowly, with 2,3-dihydroxy-4-methylbenzoate and
            2,3-dihydroxy-4-isopropylbenzoate.
REFERENCE   1  [PMID:16525856]
  AUTHORS   Stein MB, Seedat S, Gelernter J.
  TITLE     Serotonin transporter gene promoter polymorphism predicts SSRI
            response in generalized social anxiety disorder.
  JOURNAL   Psychopharmacology. (Berl). 187 (2006) 68-72.
REFERENCE   2  [PMID:1175620]
  AUTHORS   Sharma HK, Vaidyanathan CS.
  TITLE     A new mode of ring cleavage of 2,3-dihydroxybenzoic acid in Tecoma
            stans (L.). Partial purification and properties of
            2,3-dihydroxybenzoate 2,3-oxygenase.
  JOURNAL   Eur. J. Biochem. 56 (1975) 163-71.
  ORGANISM  Tecoma stans
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.28
            ExPASy - ENZYME nomenclature database: 1.13.11.28
            ExplorEnz - The Enzyme Database: 1.13.11.28
            ERGO genome analysis and discovery system: 1.13.11.28
            BRENDA, the Enzyme Database: 1.13.11.28
            CAS: 56802-97-2
///
ENTRY       EC 1.13.11.29               Enzyme
NAME        stizolobate synthase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     3,4-dihydroxy-L-phenylalanine:oxygen 4,5-oxidoreductase
            (recyclizing)
REACTION    3,4-dihydroxy-L-phenylalanine + O2 =
            4-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde
            [RN:R02075]
ALL_REAC    R02075;
            (other) R04598 R04599
SUBSTRATE   3,4-dihydroxy-L-phenylalanine [CPD:C00355];
            O2 [CPD:C00007]
PRODUCT     4-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde
            [CPD:C04796]
COFACTOR    Zinc [CPD:C00038]
COMMENT     The intermediate product undergoes ring closure and oxidation, with
            NAD(P)+ as acceptor, to stizolobic acid. The enzyme requires Zn2+.
REFERENCE   1  [PMID:9285]
  AUTHORS   Saito K, Komamine A.
  TITLE     Biosynthesis of stizolobinic acid and stizolobic acid in higher
            plants. An enzyme system(s) catalyzing the conversion of
            dihydroxyphenylalanine into stizolobinic acid and stizolobic acid
            from etiolated seedlings of Stizolobium hassjoo.
  JOURNAL   Eur. J. Biochem. 68 (1976) 237-43.
  ORGANISM  Stizolobium hassjoo
REFERENCE   2  [PMID:624278]
  AUTHORS   Saito K, Komamine A.
  TITLE     Biosynthesis of stizolobinic acid and stizolobic acid in higher
            plants.
  JOURNAL   Eur. J. Biochem. 82 (1978) 385-92.
  ORGANISM  Stizolobium hassjoo
PATHWAY     PATH: map00350  Tyrosine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.29
            ExPASy - ENZYME nomenclature database: 1.13.11.29
            ExplorEnz - The Enzyme Database: 1.13.11.29
            ERGO genome analysis and discovery system: 1.13.11.29
            BRENDA, the Enzyme Database: 1.13.11.29
            CAS: 65979-39-7
///
ENTRY       EC 1.13.11.30               Enzyme
NAME        stizolobinate synthase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     3,4-dihydroxy-L-phenylalanine:oxygen 2,3-oxidoreductase
            (recyclizing)
REACTION    3,4-dihydroxy-L-phenylalanine + O2 =
            5-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde
            [RN:R02076]
ALL_REAC    R02076;
            (other) R04600 R04601
SUBSTRATE   3,4-dihydroxy-L-phenylalanine [CPD:C00355];
            O2 [CPD:C00007]
PRODUCT     5-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde
            [CPD:C04797]
COFACTOR    Zinc [CPD:C00038]
COMMENT     The intermediate product undergoes ring closure and oxidation, with
            NAD(P)+ as acceptor, to stizolobinic acid. The enzyme requires Zn2+.
REFERENCE   1  [PMID:9285]
  AUTHORS   Saito K, Komamine A.
  TITLE     Biosynthesis of stizolobinic acid and stizolobic acid in higher
            plants. An enzyme system(s) catalyzing the conversion of
            dihydroxyphenylalanine into stizolobinic acid and stizolobic acid
            from etiolated seedlings of Stizolobium hassjoo.
  JOURNAL   Eur. J. Biochem. 68 (1976) 237-43.
  ORGANISM  Stizolobium hassjoo
REFERENCE   2  [PMID:624278]
  AUTHORS   Saito K, Komamine A.
  TITLE     Biosynthesis of stizolobinic acid and stizolobic acid in higher
            plants.
  JOURNAL   Eur. J. Biochem. 82 (1978) 385-92.
  ORGANISM  Stizolobium hassjoo
PATHWAY     PATH: map00350  Tyrosine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.30
            ExPASy - ENZYME nomenclature database: 1.13.11.30
            ExplorEnz - The Enzyme Database: 1.13.11.30
            ERGO genome analysis and discovery system: 1.13.11.30
            BRENDA, the Enzyme Database: 1.13.11.30
            CAS: 65979-38-6
///
ENTRY       EC 1.13.11.31               Enzyme
NAME        arachidonate 12-lipoxygenase;
            Delta12-lipoxygenase;
            12-lipoxygenase;
            12Delta-lipoxygenase;
            C-12 lipoxygenase;
            12S-lipoxygenase;
            leukotriene A4 synthase;
            LTA4 synthase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     arachidonate:oxygen 12-oxidoreductase
REACTION    arachidonate + O2 =
            (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
            [RN:R01596]
ALL_REAC    R01596
SUBSTRATE   arachidonate [CPD:C00219];
            O2 [CPD:C00007]
PRODUCT     (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
            [CPD:C05965]
INHIBITOR   3-Methoxytropolone [CPD:C02639]
COMMENT     The product is rapidly reduced to the corresponding 12S-hydroxy
            compound.
REFERENCE   1  [PMID:4215079]
  AUTHORS   Hamberg M, Samuelsson B.
  TITLE     Prostaglandin endoperoxides. Novel transformations of arachidonic
            acid in human platelets.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 71 (1974) 3400-4.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:804329]
  AUTHORS   Nugteren DH.
  TITLE     Arachidonate lipoxygenase in blood platelets.
  JOURNAL   Biochim. Biophys. Acta. 380 (1975) 299-307.
  ORGANISM  horse, cow [GN:bta], pig [GN:ssc], sheep
REFERENCE   3  [PMID:6783111]
  AUTHORS   Wallach DP, Brown VR.
  TITLE     A novel preparation of human platelet lipoxygenase. Characteristics
            and inhibition by a variety of phenyl hydrazones and comparisons
            with other lipoxygenases.
  JOURNAL   Biochim. Biophys. Acta. 663 (1981) 361-72.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00590  Arachidonic acid metabolism
ORTHOLOGY   KO: K00458  arachidonate 12-lipoxygenase
GENES       HSA: 239(ALOX12)
            MMU: 11684(Alox12) 11685(Alox12e) 11687(Alox15)
            RNO: 81639(Alox15)
            CFA: 479476(ALOX12)
            BTA: 407169(LOC407169)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.31
            ExPASy - ENZYME nomenclature database: 1.13.11.31
            ExplorEnz - The Enzyme Database: 1.13.11.31
            ERGO genome analysis and discovery system: 1.13.11.31
            BRENDA, the Enzyme Database: 1.13.11.31
            CAS: 82391-43-3
///
ENTRY       EC 1.13.11.32               Enzyme
NAME        2-nitropropane dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     2-nitropropane:oxygen 2-oxidoreductase
REACTION    2 2-nitropropane + O2 = 2 acetone + 2 nitrite [RN:R00025]
ALL_REAC    R00025
SUBSTRATE   2-nitropropane [CPD:C02116];
            O2 [CPD:C00007]
PRODUCT     acetone [CPD:C00207];
            nitrite [CPD:C00088]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023];
            FMN [CPD:C00061]
COMMENT     While the enzyme from the fungus Neurospora crassa contains
            non-covalently bound FMN as the cofactor, that from the yeast
            Williopsis mrakii contains FAD [2]. This enzyme differs from EC
            1.7.3.1, nitroalkane oxidase, in that the preferred substrates are
            anionic nitronates rather than neutral nitroalkanes [2,3]. The
            enzyme has broad substrate specificity that is independent of
            substrate size [2,3]. Some other nitroalkanes, including
            nitroethane, 1-nitropropane and 3-nitropentan-2-ol, can act as
            donors, but more slowly.
REFERENCE   1  [PMID:11214]
  AUTHORS   Kido T, Soda K, Suzuki T, Asada K.
  TITLE     A new oxygenase, 2-nitropropane dioxygenase of Hansenula mrakii.
            Enzymologic and spectrophotometric properties.
  JOURNAL   J. Biol. Chem. 251 (1976) 6994-7000.
  ORGANISM  Hansenula mrakii
REFERENCE   2  [PMID:16682407]
  AUTHORS   Ha JY, Min JY, Lee SK, Kim HS, Kim do J, Kim KH, Lee HH, Kim HK,
            Yoon HJ, Suh SW.
  TITLE     Crystal structure of 2-nitropropane dioxygenase complexed with FMN
            and substrate. Identification of the catalytic base.
  JOURNAL   J. Biol. Chem. 281 (2006) 18660-7.
REFERENCE   3  [PMID:15582992]
  AUTHORS   Francis K, Russell B, Gadda G.
  TITLE     Involvement of a flavosemiquinone in the enzymatic oxidation of
            nitroalkanes catalyzed by 2-nitropropane dioxygenase.
  JOURNAL   J. Biol. Chem. 280 (2005) 5195-204.
PATHWAY     PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00459  2-nitropropane dioxygenase
GENES       ANI: AN8801.2
            XCC: XCC1197
            XCB: XC_3045
            XCV: XCV1339 XCV1340
            XAC: XAC1290
            XOO: XOO1323
            XOM: XOO_1217(XOO1217)
            PAU: PA14_08460
            PEN: PSEEN0458
            PCR: Pcryo_0024
            ACI: ACIAD1570
            PHA: PSHAa0904
            NME: NMB1452
            NMA: NMA1666
            NGO: NGO1024
            CVI: CV_4048
            RSO: RS05464(RSp0307) RSc0114(RS00984) RSc0255(RS00690)
            REU: Reut_A0268 Reut_B5061 Reut_B5128 Reut_C6053
            REH: H16_B0364 H16_B0401 H16_B1763 H16_B2331
            RME: Rmet_0222 Rmet_2083 Rmet_5434
            BMA: BMA0622 BMA1305 BMA2836
            BXE: Bxe_A1945 Bxe_A4276 Bxe_A4328 Bxe_B2734
            BUR: Bcep18194_A3380 Bcep18194_A4869 Bcep18194_A5053
                 Bcep18194_A6315 Bcep18194_B0781 Bcep18194_B1435
            BCN: Bcen_2351 Bcen_2830 Bcen_6322
            BCH: Bcen2424_0277 Bcen2424_1757 Bcen2424_2965 Bcen2424_4912
            BAM: Bamb_0191 Bamb_1606 Bamb_1681 Bamb_3013
            BPS: BPSL0328 BPSL1551 BPSL2363 BPSL3285
            BPM: BURPS1710b_0052(fabK) BURPS1710b_0536 BURPS1710b_2314
                 BURPS1710b_2815
            BTE: BTH_I0307 BTH_I1803 BTH_I2272 BTH_I3159
            BPA: BPP1043
            BBR: BB1259
            RFR: Rfer_1008
            POL: Bpro_3833 Bpro_4589
            AZO: azo0323(naoA) azo1158(ncd2) azo3821(ncd2)
            DAR: Daro_1554
            TBD: Tbd_2188
            HPA: HPAG1_0758
            ABU: Abu_0643(npd)
            NIS: NIS_0762
            SUN: SUN_1743
            BBA: Bd2156
            MXA: MXAN_2267
            RET: RHE_CH00505
            RLE: RL0537 RL2298
            BME: BMEII0460
            BMF: BAB2_0405
            BJA: blr2606
            BRA: BRADO4492 BRADO4493
            BBT: BBta_4714 BBta_4715 BBta_5146
            RPA: RPA1941
            RPE: RPE_3363
            NWI: Nwi_3001
            NHA: Nham_1075
            SIL: SPOA0325
            SIT: TM1040_2459
            GOX: GOX1587
            ABA: Acid345_3501 Acid345_4298
            BAN: BA1385
            BAR: GBAA1385
            BAA: BA_1911
            BAT: BAS1283
            BCE: BC1368
            BCA: BCE_1483
            BCZ: BCZK1257(fabK)
            BTK: BT9727_1255(fabK)
            BPU: BPUM_2794
            SGO: SGO_1695
            LPL: lp_0912
            MSM: MSMEG_0332 MSMEG_5182
            MMC: Mmcs_4067
            CGL: NCgl0899(cgl0936)
            CGB: cg1068
            RHA: RHA1_ro00808 RHA1_ro00812 RHA1_ro04649 RHA1_ro04690
                 RHA1_ro06117 RHA1_ro08143
            SEN: SACE_1450
            FNU: FN0664
            LIL: LA2727
            LIC: LIC11285
            GFO: GFO_2224
            TTH: TTC1901
            TTJ: TTHA0103
STRUCTURES  PDB: 2GJL  2GJN  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.32
            ExPASy - ENZYME nomenclature database: 1.13.11.32
            ExplorEnz - The Enzyme Database: 1.13.11.32
            ERGO genome analysis and discovery system: 1.13.11.32
            UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.32
            BRENDA, the Enzyme Database: 1.13.11.32
            CAS: 65802-82-6
///
ENTRY       EC 1.13.11.33               Enzyme
NAME        arachidonate 15-lipoxygenase;
            15-lipoxygenase;
            linoleic acid omega6-lipoxygenase;
            omega6 lipoxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     arachidonate:oxygen 15-oxidoreductase
REACTION    arachidonate + O2 =
            (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
            [RN:R01593]
ALL_REAC    R01593;
            (other) R03626
SUBSTRATE   arachidonate [CPD:C00219];
            O2 [CPD:C00007]
PRODUCT     (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
            [CPD:C05966]
COMMENT     The product is rapidly reduced to the corresponding 15S-hydroxy
            compound.
REFERENCE   1  [PMID:6804460]
  AUTHORS   Bryant RW, Bailey JM, Schewe T, Rapoport SM.
  TITLE     Positional specificity of a reticulocyte lipoxygenase. Conversion of
            arachidonic acid to 15-S-hydroperoxy-eicosatetraenoic acid.
  JOURNAL   J. Biol. Chem. 257 (1982) 6050-5.
  ORGANISM  Glycine max [GN:egma]
REFERENCE   2  [PMID:6813644]
  AUTHORS   Narumiya S, Salmon JA.
  TITLE     Arachidonic acid-15-lipoxygenase from rabbit peritoneal
            polymorphonuclear leukocytes.
  JOURNAL   Methods. Enzymol. 86 (1982) 45-8.
  ORGANISM  rabbit
REFERENCE   3  [PMID:2496760]
  AUTHORS   Oliw EH, Sprecher H.
  TITLE     Metabolism of polyunsaturated fatty acids by an (n - 6)-lipoxygenase
            associated with human ejaculates.
  JOURNAL   Biochim. Biophys. Acta. 1002 (1989) 283-91.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:3112136]
  AUTHORS   Shibata D, Steczko J, Dixon JE, Hermodson M, Yazdanparast R, Axelrod
            B.
  TITLE     Primary structure of soybean lipoxygenase-1.
  JOURNAL   J. Biol. Chem. 262 (1987) 10080-5.
  ORGANISM  Glycine max [GN:egma]
PATHWAY     PATH: map00590  Arachidonic acid metabolism
            PATH: map00591  Linoleic acid metabolism
ORTHOLOGY   KO: K00460  arachidonate 15-lipoxygenase
            KO: K08022  arachidonate 15-lipoxygenase (second type) /
                        8-lipoxygenase (S-type)
GENES       HSA: 246(ALOX15) 247(ALOX15B)
            MMU: 11688(Alox8)
            RNO: 266604(Alox15b)
            CFA: 489458(ALOX15)
            BTA: 282139(ALOX15) 286820(ALOX15B)
            SSC: 396971(ALOX15)
            GGA: 425997(ALOX15B)
            DRE: 322732(alox12)
            SDN: Sden_1680
            BTE: BTH_I2353
            NMU: Nmul_A0532
STRUCTURES  PDB: 1LOX  2P0M  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.33
            ExPASy - ENZYME nomenclature database: 1.13.11.33
            ExplorEnz - The Enzyme Database: 1.13.11.33
            ERGO genome analysis and discovery system: 1.13.11.33
            BRENDA, the Enzyme Database: 1.13.11.33
            CAS: 82249-77-2
///
ENTRY       EC 1.13.11.34               Enzyme
NAME        arachidonate 5-lipoxygenase;
            leukotriene-A4 synthase;
            Delta5-lipoxygenase;
            5Delta-lipoxygenase;
            arachidonic 5-lipoxygenase;
            arachidonic acid 5-lipoxygenase;
            C-5-lipoxygenase;
            LTA synthase;
            leukotriene A4 synthase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     arachidonate:oxygen 5-oxidoreductase
REACTION    arachidonate + O2 =
            (6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyicosa-6,8,11,14-tetraenoate
            [RN:R01595]
ALL_REAC    R01595;
            (other) R03058 R07057
SUBSTRATE   arachidonate [CPD:C00219];
            O2 [CPD:C00007]
PRODUCT     (6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
            [CPD:C05356]
INHIBITOR   AA861 [CPD:C01349];
            Caffeate [CPD:C01481];
            2-Heptyl-4-hydroxyquinoline-N-oxide [CPD:C04284]
COMMENT     The product shown above is further converted by the enzyme into
            (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate
            (leukotriene A4).
REFERENCE   1  [PMID:2829172]
  AUTHORS   Matsumoto T, Funk CD, Radmark O, Hoog JO, Jornvall H, Samuelsson B.
  TITLE     Molecular cloning and amino acid sequence of human 5-lipoxygenase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 26-30.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:3038871]
  AUTHORS   Ohishi N, Izumi T, Minami M, Kitamura S, Seyama Y, Ohkawa S, Terao
            S, Yotsumoto H, Takaku F, Shimizu T.
  TITLE     Leukotriene A4 hydrolase in the human lung. Inactivation of the
            enzyme with leukotriene A4 isomers.
  JOURNAL   J. Biol. Chem. 262 (1987) 10200-5.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:3012557]
  AUTHORS   Shimizu T, Izumi T, Seyama Y, Tadokoro K, Radmark O, Samuelsson B.
  TITLE     Characterization of leukotriene A4 synthase from murine mast cells:
            evidence for its identity to arachidonate 5-lipoxygenase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 4175-9.
  ORGANISM  mouse [GN:mmu]
REFERENCE   4  [PMID:6322165]
  AUTHORS   Shimizu T, Radmark O, Samuelsson B.
  TITLE     Enzyme with dual lipoxygenase activities catalyzes leukotriene A4
            synthesis from arachidonic acid.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 689-93.
  ORGANISM  Solanum tuberosum [GN:estu]
PATHWAY     PATH: map00590  Arachidonic acid metabolism
            PATH: map00591  Linoleic acid metabolism
ORTHOLOGY   KO: K00461  arachidonate 5-lipoxygenase
GENES       HSA: 240(ALOX5)
            PTR: 450428(ALOX5)
            RNO: 25290(Alox5)
            CFA: 477753(ALOX5)
            SPU: 584481(LOC584481)
            NEU: NE1239(ALOX5)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.34
            ExPASy - ENZYME nomenclature database: 1.13.11.34
            ExplorEnz - The Enzyme Database: 1.13.11.34
            ERGO genome analysis and discovery system: 1.13.11.34
            BRENDA, the Enzyme Database: 1.13.11.34
            CAS: 80619-02-9
///
ENTRY       EC 1.13.11.35               Enzyme
NAME        pyrogallol 1,2-oxygenase;
            pyrogallol 1,2-dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     1,2,3-trihydroxybenzene:oxygen 1,2-oxidoreductase (decyclizing)
REACTION    1,2,3-trihydroxybenzene + O2 = (Z)-5-oxohex-2-enedioate [RN:R03246]
ALL_REAC    R03246
SUBSTRATE   1,2,3-trihydroxybenzene [CPD:C01108];
            O2 [CPD:C00007]
PRODUCT     (Z)-5-oxohex-2-enedioate [CPD:C03453]
REFERENCE   1  [PMID:7217008]
  AUTHORS   Groseclose EE, Ribbons DW.
  TITLE     Metabolism of resorcinylic compounds by bacteria: new pathway for
            resorcinol catabolism in Azotobacter vinelandii.
  JOURNAL   J. Bacteriol. 146 (1981) 460-6.
  ORGANISM  Azotobacter vinelandii
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.35
            ExPASy - ENZYME nomenclature database: 1.13.11.35
            ExplorEnz - The Enzyme Database: 1.13.11.35
            ERGO genome analysis and discovery system: 1.13.11.35
            BRENDA, the Enzyme Database: 1.13.11.35
            CAS: 78310-68-6
///
ENTRY       EC 1.13.11.36               Enzyme
NAME        chloridazon-catechol dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone
            1,2-oxidoreductase (decyclizing)
REACTION    5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2 =
            5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
            [RN:R04602]
ALL_REAC    R04602
SUBSTRATE   5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone
            [CPD:C04798];
            O2 [CPD:C00007]
PRODUCT     5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
            [CPD:C05155]
COFACTOR    Iron [CPD:C00023]
COMMENT     An iron protein, requiring additional Fe2+. Not identical with EC
            1.13.11.1 (catechol 1,2-dioxygenase), EC 1.13.11.2 (catechol
            2,3-dioxygenase) or EC 1.13.11.5 (homogentisate 1,2-dioxygenase).
            Involved in the breakdown of the herbicide chloridazon.
REFERENCE   1  [PMID:19349]
  AUTHORS   Muller R, Haug S, Eberspacher J, Lingens F.
  TITLE     [Catechol 2,3-dioxygenase from pyrazon-degrading bacteria (author's
            transl)]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 358 (1977) 797-805.
REFERENCE   2  [PMID:6811270]
  AUTHORS   Muller R, Schmitt S, Lingens F.
  TITLE     A novel non-heme iron-containing dioxygenase. Chloridazon-catechol
            dioxygenase from Phenylobacterium immobilis DSM 1986.
  JOURNAL   Eur. J. Biochem. 125 (1982) 579-84.
  ORGANISM  Phenylobacterium immobilis
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.36
            ExPASy - ENZYME nomenclature database: 1.13.11.36
            ExplorEnz - The Enzyme Database: 1.13.11.36
            ERGO genome analysis and discovery system: 1.13.11.36
            BRENDA, the Enzyme Database: 1.13.11.36
            CAS: 82869-32-7
///
ENTRY       EC 1.13.11.37               Enzyme
NAME        hydroxyquinol 1,2-dioxygenase;
            hydroxyquinol dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     benzene-1,2,4-triol:oxygen 1,2-oxidoreductase (decyclizing)
REACTION    benzene-1,2,4-triol + O2 = 3-hydroxy-cis,cis-muconate [RN:R04061]
ALL_REAC    R04061;
            (other) R03891
SUBSTRATE   benzene-1,2,4-triol [CPD:C02814];
            O2 [CPD:C00007]
PRODUCT     3-hydroxy-cis,cis-muconate [CPD:C03676]
COFACTOR    Iron [CPD:C00023]
COMMENT     An iron protein. The product isomerizes to 2-maleylacetate
            (cis-hexenedioate). Highly specific; catechol and pyrogallol are
            acted on at less than 1% of the rate at which hydroxyquinol is
            oxidized.
REFERENCE   1  [PMID:6539772]
  AUTHORS   Sze IS, Dagley S.
  TITLE     Properties of salicylate hydroxylase and hydroxyquinol
            1,2-dioxygenase purified from Trichosporon cutaneum.
  JOURNAL   J. Bacteriol. 159 (1984) 353-9.
  ORGANISM  Trichosporon cutaneum
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00627  1,4-Dichlorobenzene degradation
ORTHOLOGY   KO: K04098  hydroxyquinol 1,2-dioxygenase
GENES       PIC: PICST_52208(HDQ2) PICST_62287(HQD1)
            PAP: PSPA7_3907
            RPA: RPA2149
            SWI: Swit_4890 Swit_5063
            MSM: MSMEG_4041 MSMEG_6713
            RHA: RHA1_ro11310
STRUCTURES  PDB: 1TMX  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.37
            ExPASy - ENZYME nomenclature database: 1.13.11.37
            ExplorEnz - The Enzyme Database: 1.13.11.37
            ERGO genome analysis and discovery system: 1.13.11.37
            UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.37
            BRENDA, the Enzyme Database: 1.13.11.37
            CAS: 91847-14-2
///
ENTRY       EC 1.13.11.38               Enzyme
NAME        1-hydroxy-2-naphthoate 1,2-dioxygenase;
            1-hydroxy-2-naphthoate dioxygenase;
            1-hydroxy-2-naphthoate-degrading enzyme;
            1-hydroxy-2-naphthoic acid dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     1-hydroxy-2-naphthoate:oxygen 1,2-oxidoreductase (decyclizing)
REACTION    1-hydroxy-2-naphthoate + O2 =
            (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate [RN:R07657]
ALL_REAC    R07657;
            (other) R03466
SUBSTRATE   1-hydroxy-2-naphthoate [CPD:C03203];
            O2 [CPD:C00007]
PRODUCT     (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate [CPD:C16149]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+. Involved, with EC 4.1.2.34
            4-(2-carboxyphenyl)-2-oxobut-3-enoate aldolase, in the metabolism of
            phenanthrene in bacteria.
REFERENCE   1  [PMID:6833175]
  AUTHORS   Barnsley EA.
  TITLE     Phthalate pathway of phenanthrene metabolism: formation of
            2'-carboxybenzalpyruvate.
  JOURNAL   J. Bacteriol. 154 (1983) 113-7.
  ORGANISM  gram-negative coccus
PATHWAY     PATH: map00626  Naphthalene and anthracene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.38
            ExPASy - ENZYME nomenclature database: 1.13.11.38
            ExplorEnz - The Enzyme Database: 1.13.11.38
            ERGO genome analysis and discovery system: 1.13.11.38
            UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.38
            BRENDA, the Enzyme Database: 1.13.11.38
            CAS: 85941-64-6
///
ENTRY       EC 1.13.11.39               Enzyme
NAME        biphenyl-2,3-diol 1,2-dioxygenase;
            2,3-dihydroxybiphenyl dioxygenase;
            biphenyl-2,3-diol dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     biphenyl-2,3-diol:oxygen 1,2-oxidoreductase (decyclizing)
REACTION    biphenyl-2,3-diol + O2 = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate +
            H2O [RN:R03462]
ALL_REAC    R03462;
            (other) R05245 R07827
SUBSTRATE   biphenyl-2,3-diol [CPD:C02526];
            O2 [CPD:C00007]
PRODUCT     2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate [CPD:C01273];
            H2O [CPD:C00001]
COMMENT     Also acts on 3-isopropylcatechol, forming
            7-methyl-2-hydroxy-6-oxoocta-2,4-dienoate. Not identical with EC
            1.13.11.2 catechol 2,3-dioxygenase.
REFERENCE   1
  AUTHORS   Utsumi, T. and Funatsu, G.
  TITLE     Induction of superoxide production in polymorphonuclear leukocytes
            by ricinus lectins and its dependency on lectin valency.
  JOURNAL   Agric. Biol. Chem. 50 (1986) 1047-1049.
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
            PATH: map00621  Biphenyl degradation
ORTHOLOGY   KO: K00462  biphenyl-2,3-diol 1,2-dioxygenase
GENES       PHA: PSHAa0900(tesB)
            AEH: Mlg_2458
            CVI: CV_0246
            REU: Reut_A1557
            REH: H16_B0654(bphC)
            BXE: Bxe_C0640 Bxe_C1191(bphC)
            BUR: Bcep18194_B1431
            DAR: Daro_1335
            RET: RHE_CH00346
            RLE: RL0363
            BME: BMEI1118 BMEII0295
            BMF: BAB2_0231
            BRA: BRADO6043
            SAA: SAUSA300_2461
            MTU: Rv3568c(bphC)
            MTC: MT3673
            MBO: Mb3599c(bphC)
            MBB: BCG_3633c(bphC)
            MPA: MAP0499
            MAV: MAV_3021
            MSM: MSMEG_2891 MSMEG_6036
            NFA: nfa4720
            RHA: RHA1_ro05803 RHA1_ro08055(bphC1) RHA1_ro09005
                 RHA1_ro10135(etbC)
            STP: Strop_2669
STRUCTURES  PDB: 1DHY  1EIL  1EIQ  1EIR  1HAN  1KMY  1KND  1KNF  1KW3  1KW6  
                 1KW8  1KW9  1KWB  1KWC  1LGT  1LKD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.39
            ExPASy - ENZYME nomenclature database: 1.13.11.39
            ExplorEnz - The Enzyme Database: 1.13.11.39
            ERGO genome analysis and discovery system: 1.13.11.39
            UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.39
            BRENDA, the Enzyme Database: 1.13.11.39
            CAS: 103679-58-9
///
ENTRY       EC 1.13.11.40               Enzyme
NAME        arachidonate 8-lipoxygenase;
            8-lipoxygenase;
            8(R)-lipoxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     arachidonate:oxygen 8-oxidoreductase
REACTION    arachidonate + O2 =
            (5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
            [RN:R01594]
ALL_REAC    R01594
SUBSTRATE   arachidonate [CPD:C00219];
            O2 [CPD:C00007]
PRODUCT     (5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
COMMENT     From the coral Pseudoplexaura porosa.
REFERENCE   1  [PMID:2867091]
  AUTHORS   Bundy GL, Nidy EG, Epps DE, Mizsak SA, Wnuk RJ.
  TITLE     Discovery of an arachidonic acid C-8 lipoxygenase in the gorgonian
            coral Pseudoplexaura porosa.
  JOURNAL   J. Biol. Chem. 261 (1986) 747-51.
  ORGANISM  Pseudoplexaura porosa
PATHWAY     PATH: map00590  Arachidonic acid metabolism
STRUCTURES  PDB: 2FNQ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.40
            ExPASy - ENZYME nomenclature database: 1.13.11.40
            ExplorEnz - The Enzyme Database: 1.13.11.40
            ERGO genome analysis and discovery system: 1.13.11.40
            BRENDA, the Enzyme Database: 1.13.11.40
            CAS: 100900-72-9
///
ENTRY       EC 1.13.11.41               Enzyme
NAME        2,4'-dihydroxyacetophenone dioxygenase;
            (4-hydroxybenzoyl)methanol oxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     2,4'-dihydroxyacetophenone oxidoreductase (C-C-bond-cleaving)
REACTION    2,4'-dihydroxyacetophenone + O2 = 4-hydroxybenzoate + formate
            [RN:R01305]
ALL_REAC    R01305
SUBSTRATE   2,4'-dihydroxyacetophenone [CPD:C13635];
            O2 [CPD:C00007]
PRODUCT     4-hydroxybenzoate [CPD:C00156];
            formate [CPD:C00058]
REFERENCE   1  [PMID:3814084]
  AUTHORS   Hopper DJ.
  TITLE     Oxygenase properties of the (4-hydroxybenzoyl)methanol-cleavage
            enzyme from an Alcaligenes sp.
  JOURNAL   Biochem. J. 239 (1986) 469-72.
  ORGANISM  Alcaligenes sp.
PATHWAY     PATH: map00363  Bisphenol A degradation
ORTHOLOGY   KO: K05913  2,4'-dihydroxyacetophenone dioxygenase
GENES       PAE: PA4095
            PAU: PA14_10920(dad)
            PST: PSPTO_3051
            PFL: PFL_3363(dad)
            BMA: BMAA1385
            BML: BMA10299_0151
            BPM: BURPS1710b_A2315
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.41
            ExPASy - ENZYME nomenclature database: 1.13.11.41
            ExplorEnz - The Enzyme Database: 1.13.11.41
            ERGO genome analysis and discovery system: 1.13.11.41
            UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.41
            BRENDA, the Enzyme Database: 1.13.11.41
            CAS: 105503-64-8
///
ENTRY       EC 1.13.11.42     Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
COMMENT     Deleted entry: indoleamine-pyrrole 2,3-dioxygenase (EC 1.13.11.42
            created 1992, deleted 2006)
STRUCTURES  PDB: 2D0T  2D0U  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.42
            ExPASy - ENZYME nomenclature database: 1.13.11.42
            ExplorEnz - The Enzyme Database: 1.13.11.42
            ERGO genome analysis and discovery system: 1.13.11.42
            BRENDA, the Enzyme Database: 1.13.11.42
///
ENTRY       EC 1.13.11.43               Enzyme
NAME        lignostilbene alphabeta-dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene:oxygen oxidoreductase
            (alphabeta-bond-cleaving)
REACTION    1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene + O2 = 2 vanillin
            [RN:R00043]
ALL_REAC    R00043
SUBSTRATE   1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene [CPD:C04547];
            O2 [CPD:C00007]
PRODUCT     vanillin [CPD:C00755]
COFACTOR    Iron [CPD:C00023]
COMMENT     An iron protein. The enzyme catalyses oxidative cleavage of the
            interphenyl double bond in the synthetic substrate and
            lignin-derived stilbenes. It is responsible for the degradation of a
            diarylpropane-type structure in lignin.
REFERENCE   1
  AUTHORS   Kamoda, S., Habu, N., Samejima, M. and Yoshimoto, T.
  TITLE     Purification and some properties of lignostilbene-alphabeta-
            dioxygenase responsible for the Calpha-Cbeta cleavage of a
            diarylpropane type lignin model-compound from Pseudomonas sp
            TMY1009.
  JOURNAL   Agric. Biol. Chem. 53 (1989) 2757-2761.
  ORGANISM  Pseudomonas sp.
ORTHOLOGY   KO: K00464  lignostilbene-alpha,beta-dioxygenase
GENES       XCV: XCV0111
            MPA: MAP1324
            MSM: MSMEG_1564
            SYN: sll1541
            SYW: SYNW0227
            SYC: syc1315_d
            SYD: Syncc9605_0221
            SYE: Syncc9902_0248
            CYA: CYA_1068
            CYB: CYB_0263
            TEL: tll0015
            GVI: gll3689
            ANA: all4284
            AVA: Ava_1236
            PMA: Pro0312
            PMM: PMM0280
            PMT: PMT1879
            PMN: PMN2A_1646
            PMB: A9601_03031
            PMC: P9515_03131
            PMF: P9303_25111
            PMG: P9301_03041
            PME: NATL1_03601
            TER: Tery_3212
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.43
            ExPASy - ENZYME nomenclature database: 1.13.11.43
            ExplorEnz - The Enzyme Database: 1.13.11.43
            ERGO genome analysis and discovery system: 1.13.11.43
            BRENDA, the Enzyme Database: 1.13.11.43
            CAS: 124834-28-2
///
ENTRY       EC 1.13.11.44               Enzyme
NAME        linoleate diol synthase;
            linoleate (8R)-dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     linoleate:oxygen 7S,8S-oxidoreductase
REACTION    linoleate + O2 = (9Z,12Z)-(7S,8S)-dihydroxyoctadeca-9,12-dienoate
            [RN:R07061 R07062]
ALL_REAC    R07061 R07062
SUBSTRATE   linoleate [CPD:C01595];
            O2 [CPD:C00007]
PRODUCT     (9Z,12Z)-(7S,8S)-dihydroxyoctadeca-9,12-dienoate [CPD:C07354]
COMMENT     Oleate and linolenate are also substrates, whereas stearate,
            elaidate, gamma-linolenate, arachidonate and icosapentaenate are
            not. This enzyme differs from lipoxygenase (EC 1.13.11.12) because
            it catalyses the formation of a hydroperoxide without affecting the
            double bonds of the substrate.
REFERENCE   1  [PMID:1634517]
  AUTHORS   Brodowsky ID, Hamberg M, Oliw EH.
  TITLE     A linoleic acid (8R)-dioxygenase and hydroperoxide isomerase of the
            fungus Gaeumannomyces graminis. Biosynthesis of (8R)-hydroxylinoleic
            acid and (7S,8S)-dihydroxylinoleic acid from
            (8R)-hydroperoxylinoleic acid.
  JOURNAL   J. Biol. Chem. 267 (1992) 14738-45.
  ORGANISM  Gaeumannomyces graminis
REFERENCE   2  [PMID:8117115]
  AUTHORS   Hamberg M, Zhang LY, Brodowsky ID, Oliw EH.
  TITLE     Sequential oxygenation of linoleic acid in the fungus Gaeumannomyces
            graminis: stereochemistry of dioxygenase and hydroperoxide isomerase
            reactions.
  JOURNAL   Arch. Biochem. Biophys. 309 (1994) 77-80.
  ORGANISM  Gaeumannomyces graminis
REFERENCE   3  [PMID:10497176]
  AUTHORS   Hornsten L, Su C, Osbourn AE, Garosi P, Hellman U, Wernstedt C, Oliw
            EH.
  TITLE     Cloning of linoleate diol synthase reveals homology with
            prostaglandin H synthases.
  JOURNAL   J. Biol. Chem. 274 (1999) 28219-24.
  ORGANISM  Gaeumannomyces graminis
REFERENCE   4  [PMID:9778131]
  AUTHORS   Oliw EH, Su C, Skogstrom T, Benthin G.
  TITLE     Analysis of novel hydroperoxides and other metabolites of oleic,
            linoleic, and linolenic acids by liquid chromatography-mass
            spectrometry with ion trap MSn.
  JOURNAL   Lipids. 33 (1998) 843-52.
  ORGANISM  Gaeumannomyces graminis
REFERENCE   5  [PMID:8662736]
  AUTHORS   Su C, Oliw EH.
  TITLE     Purification and characterization of linoleate 8-dioxygenase from
            the fungus Gaeumannomyces graminis as a novel hemoprotein.
  JOURNAL   J. Biol. Chem. 271 (1996) 14112-8.
  ORGANISM  Gaeumannomyces graminis
REFERENCE   6  [PMID:9694817]
  AUTHORS   Su C, Sahlin M, Oliw EH.
  TITLE     A protein radical and ferryl intermediates are generated by
            linoleate diol synthase, a ferric hemeprotein with dioxygenase and
            hydroperoxide isomerase activities.
  JOURNAL   J. Biol. Chem. 273 (1998) 20744-51.
  ORGANISM  Gaeumannomyces graminis
PATHWAY     PATH: map00591  Linoleic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.44
            ExPASy - ENZYME nomenclature database: 1.13.11.44
            ExplorEnz - The Enzyme Database: 1.13.11.44
            ERGO genome analysis and discovery system: 1.13.11.44
            BRENDA, the Enzyme Database: 1.13.11.44
///
ENTRY       EC 1.13.11.45               Enzyme
NAME        linoleate 11-lipoxygenase;
            linoleate dioxygenase, manganese lipoxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     linoleate:oxygen 11S-oxidoreductase
REACTION    linoleate + O2 = (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
            [RN:R05718]
ALL_REAC    R05718
SUBSTRATE   linoleate [CPD:C01595];
            O2 [CPD:C00007]
PRODUCT     (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate [CPD:C07338]
COMMENT     The product (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate, is
            converted, more slowly, into
            (9Z,11E)-(13R)-13-hydroperoxyoctadeca-9,11-dienoate. The enzyme from
            the fungus Gaeumannomyces graminis requires Mn2+. It also acts on
            alpha-linolenate, whereas gamma-linolenate is a poor substrate.
            Oleate and arachidonate are not substrates.
REFERENCE   1  [PMID:9582346]
  AUTHORS   Hamberg M, Su C, Oliw E.
  TITLE     Manganese lipoxygenase. Discovery of a bis-allylic hydroperoxide as
            product and intermediate in a lipoxygenase reaction.
  JOURNAL   J. Biol. Chem. 273 (1998) 13080-8.
  ORGANISM  Gaeumannomyces graminis
REFERENCE   2  [PMID:9778131]
  AUTHORS   Oliw EH, Su C, Skogstrom T, Benthin G.
  TITLE     Analysis of novel hydroperoxides and other metabolites of oleic,
            linoleic, and linolenic acids by liquid chromatography-mass
            spectrometry with ion trap MSn.
  JOURNAL   Lipids. 33 (1998) 843-52.
  ORGANISM  Gaeumannomyces graminis
REFERENCE   3  [PMID:9582345]
  AUTHORS   Su C, Oliw EH.
  TITLE     Manganese lipoxygenase. Purification and characterization.
  JOURNAL   J. Biol. Chem. 273 (1998) 13072-9.
  ORGANISM  Gaeumannomyces graminis
PATHWAY     PATH: map00591  Linoleic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.45
            ExPASy - ENZYME nomenclature database: 1.13.11.45
            ExplorEnz - The Enzyme Database: 1.13.11.45
            ERGO genome analysis and discovery system: 1.13.11.45
            BRENDA, the Enzyme Database: 1.13.11.45
///
ENTRY       EC 1.13.11.46               Enzyme
NAME        4-hydroxymandelate synthase;
            4-hydroxyphenylpyruvate dioxygenase II
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating)
REACTION    4-hydroxyphenylpyruvate + O2 = 4-hydroxymandelate + CO2 [RN:R05778]
ALL_REAC    R05778
SUBSTRATE   4-hydroxyphenylpyruvate [CPD:C01179];
            O2 [CPD:C00007]
PRODUCT     4-hydroxymandelate [CPD:C11527];
            CO2 [CPD:C00011]
COMMENT     Requires Fe2+. Involved in the biosynthesis of the vancomycin group
            of glycopeptide antibiotics.
REFERENCE   1
  AUTHORS   Choroba, O.W., Williams, D.H. and Spencer, J.B.
  TITLE     Biosynthesis of the vancomycin group of antibiotics: involvement of
            an unusual dioxygenase in the pathway to (S)-4-hydroxyphenylglycine.
  JOURNAL   J. Am. Chem. Soc. 122 (2000) 5389-5390.
  ORGANISM  Amycolatopsis orientalis
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.46
            ExPASy - ENZYME nomenclature database: 1.13.11.46
            ExplorEnz - The Enzyme Database: 1.13.11.46
            ERGO genome analysis and discovery system: 1.13.11.46
            BRENDA, the Enzyme Database: 1.13.11.46
///
ENTRY       EC 1.13.11.47               Enzyme
NAME        3-hydroxy-4-oxoquinoline 2,4-dioxygenase;
            (1H)-3-hydroxy-4-oxoquinoline 2,4-dioxygenase;
            3-hydroxy-4-oxo-1,4-dihydroquinoline 2,4-dioxygenase;
            3-hydroxy-4(1H)-one, 2,4-dioxygenase;
            quinoline-3,4-diol 2,4-dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     3-hydroxy-1H-quinolin-4-one 2,4-dioxygenase (CO-forming)
REACTION    3-hydroxy-1H-quinolin-4-one + O2 = N-formylanthranilate + CO
            [RN:R05719]
ALL_REAC    R05719;
            (other) R04915 R05155
SUBSTRATE   3-hydroxy-1H-quinolin-4-one [CPD:C11503];
            O2 [CPD:C00007]
PRODUCT     N-formylanthranilate [CPD:C05653];
            CO [CPD:C00237]
COMMENT     Does not contain a metal centre or organic cofactor. Fission of two
            C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of
            carbon monoxide. The enzyme from Pseudomonas putida is highly
            specific for this substrate.
REFERENCE   1
  AUTHORS   Bauer, I., De Beyer, A., Tsisuaka, B., Fetzner, S. and Lingens, F.
  TITLE     A novel type of oxygenolytic ring cleavage: 2,4-Oxygenation and
            decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and
            1H-3-hydroxy-4-oxoquinoline.
  JOURNAL   FEMS Microbiol. Lett. 117 (1994) 299-304.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2  [PMID:8856057]
  AUTHORS   Bauer I, Max N, Fetzner S, Lingens F.
  TITLE     2,4-dioxygenases catalyzing N-heterocyclic-ring cleavage and
            formation of carbon monoxide. Purification and some properties of
            1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp.
            Ru61a and comparison with 1H-3-hydroxy-4-oxoquinoline
            2,4-dioxygenase from Pseudomonas putida 33/1.
  JOURNAL   Eur. J. Biochem. 240 (1996) 576-83.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   3  [PMID:10482514]
  AUTHORS   Fischer F, Kunne S, Fetzner S.
  TITLE     Bacterial 2,4-dioxygenases: new members of the alpha/beta
            hydrolase-fold superfamily of enzymes functionally related to serine
            hydrolases.
  JOURNAL   J. Bacteriol. 181 (1999) 5725-33.
  ORGANISM  Pseudomonas putida [GN:ppu]
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.47
            ExPASy - ENZYME nomenclature database: 1.13.11.47
            ExplorEnz - The Enzyme Database: 1.13.11.47
            ERGO genome analysis and discovery system: 1.13.11.47
            BRENDA, the Enzyme Database: 1.13.11.47
///
ENTRY       EC 1.13.11.48               Enzyme
NAME        3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase;
            (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     3-hydroxy-2-methyl-1H-quinolin-4-one 2,4-dioxygenase (CO-forming)
REACTION    3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = N-acetylanthranilate +
            CO [RN:R05720]
ALL_REAC    R05720
SUBSTRATE   3-hydroxy-2-methyl-1H-quinolin-4-one [CPD:C11504];
            O2 [CPD:C00007]
PRODUCT     N-acetylanthranilate [CPD:C06332];
            CO [CPD:C00237]
COMMENT     Does not contain a metal centre or organic cofactor. Fission of two
            C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of
            carbon monoxide. The enzyme from Arthrobacter sp. can also act on
            3-hydroxy-4-oxoquinoline, forming N-formylanthranilate and CO (cf.
            EC 1.13.11.47, 3-hydroxy-4-oxoquinoline 2,4-dioxygenase), but more
            slowly.
REFERENCE   1
  AUTHORS   Bauer, I., De Beyer, A., Tsisuaka, B., Fetzner, S. and Lingens, F.
  TITLE     A novel type of oxygenolytic ring cleavage: 2,4-Oxygenation and
            decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and
            1H-3-hydroxy-4-oxoquinoline.
  JOURNAL   FEMS Microbiol. Lett. 117 (1994) 299-304.
  ORGANISM  Arthrobacter sp.
REFERENCE   2  [PMID:8856057]
  AUTHORS   Bauer I, Max N, Fetzner S, Lingens F.
  TITLE     2,4-dioxygenases catalyzing N-heterocyclic-ring cleavage and
            formation of carbon monoxide. Purification and some properties of
            1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp.
            Ru61a and comparison with 1H-3-hydroxy-4-oxoquinoline
            2,4-dioxygenase from Pseudomonas putida 33/1.
  JOURNAL   Eur. J. Biochem. 240 (1996) 576-83.
  ORGANISM  Arthrobacter sp.
REFERENCE   3  [PMID:10482514]
  AUTHORS   Fischer F, Kunne S, Fetzner S.
  TITLE     Bacterial 2,4-dioxygenases: new members of the alpha/beta
            hydrolase-fold superfamily of enzymes functionally related to serine
            hydrolases.
  JOURNAL   J. Bacteriol. 181 (1999) 5725-33.
  ORGANISM  Arthrobacter ilicis
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.48
            ExPASy - ENZYME nomenclature database: 1.13.11.48
            ExplorEnz - The Enzyme Database: 1.13.11.48
            ERGO genome analysis and discovery system: 1.13.11.48
            BRENDA, the Enzyme Database: 1.13.11.48
///
ENTRY       EC 1.13.11.49               Enzyme
NAME        chlorite O2-lyase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     chloride:oxygen oxidoreductase
REACTION    chloride + O2 = chlorite [RN:R05721]
ALL_REAC    R05721;
            (other) R07183
SUBSTRATE   chloride [CPD:C00115];
            O2 [CPD:C00007]
PRODUCT     chlorite [CPD:C01486]
COMMENT     Reaction occurs in the reverse direction in chlorate- and
            perchlorate-reducing bacteria. There is no activity when chlorite is
            replaced by hydrogen peroxide, perchlorate, chlorate or nitrite. The
            term 'chlorite dismutase' is misleading as the reaction does not
            involve dismutation/disproportionation. Contains iron and protoheme
            IX.
REFERENCE   1  [PMID:8929278]
  AUTHORS   van Ginkel CG, Rikken GB, Kroon AG, Kengen SW.
  TITLE     Purification and characterization of chlorite dismutase: a novel
            oxygen-generating enzyme.
  JOURNAL   Arch. Microbiol. 166 (1996) 321-6.
  ORGANISM  gram-negative bacterium
REFERENCE   2  [PMID:11472023]
  AUTHORS   Stenklo K, Thorell HD, Bergius H, Aasa R, Nilsson T.
  TITLE     Chlorite dismutase from Ideonella dechloratans.
  JOURNAL   J. Biol. Inorg. Chem. 6 (2001) 601-7.
  ORGANISM  Ideonella dechloratans
GENES       BPU: BPUM_3416(ywfI)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.49
            ExPASy - ENZYME nomenclature database: 1.13.11.49
            ExplorEnz - The Enzyme Database: 1.13.11.49
            ERGO genome analysis and discovery system: 1.13.11.49
            UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.49
            BRENDA, the Enzyme Database: 1.13.11.49
///
ENTRY       EC 1.13.11.50               Enzyme
NAME        acetylacetone-cleaving enzyme;
            Dke1;
            acetylacetone dioxygenase;
            diketone cleaving dioxygenase;
            diketone cleaving enzyme
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     acetylacetone:oxygen oxidoreductase
REACTION    pentane-2,4-dione + O2 = acetate + 2-oxopropanal
SUBSTRATE   pentane-2,4-dione [CPD:C15499];
            O2 [CPD:C00007]
PRODUCT     acetate [CPD:C00033];
            2-oxopropanal [CPD:C00546]
COMMENT     An Fe(II)-dependent enzyme. Forms the first step in the
            acetylacetone degradation pathway of Acinetobacter johnsonii. While
            acetylacetone is by far the best substrate, heptane-3,5-dione,
            octane-2,4-dione, 2-acetylcyclohexanone and ethyl acetoacetate can
            also act as substrates.
REFERENCE   1  [PMID:12379146]
  AUTHORS   Straganz GD, Glieder A, Brecker L, Ribbons DW, Steiner W.
  TITLE     Acetylacetone-cleaving enzyme Dke1: a novel C-C-bond-cleaving enzyme
            from Acinetobacter johnsonii.
  JOURNAL   Biochem. J. 369 (2003) 573-81.
  ORGANISM  Acinetobacter johnsonii
GENES       AAV: Aave_3966
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.50
            ExPASy - ENZYME nomenclature database: 1.13.11.50
            ExplorEnz - The Enzyme Database: 1.13.11.50
            ERGO genome analysis and discovery system: 1.13.11.50
            BRENDA, the Enzyme Database: 1.13.11.50
            CAS: 524047-53-8
///
ENTRY       EC 1.13.11.51               Enzyme
NAME        9-cis-epoxycarotenoid dioxygenase;
            nine-cis-epoxycarotenoid dioxygenase;
            NCED;
            AtNCED3;
            PvNCED1;
            VP14
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     9-cis-epoxycarotenoid 11,12-dioxygenase
REACTION    (1) a 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a
            12'-apo-carotenal;
            (2) 9-cis-violaxanthin + O2 = 2-cis,4-trans-xanthoxin +
            (3S,5R,6S)-5,6-epoxy-3-hydroxy-5,6-dihydro-12'-apo-beta-caroten-12'-
            al;
            (3) 9'-cis-neoxanthin + O2 = 2-cis,4-trans-xanthoxin +
            (3S,5R,6R)-5,6-dihydroxy-6,7-didehydro-5,6-dihydro-12'-apo-beta-
            caroten-12'-al
ALL_REAC    (other) R06952 R06953
SUBSTRATE   9-cis-epoxycarotenoid;
            O2 [CPD:C00007];
            9-cis-violaxanthin [CPD:C13433];
            9'-cis-neoxanthin [CPD:C13431]
PRODUCT     2-cis,4-trans-xanthoxin [CPD:C13453];
            12'-apo-carotenal;
            (3S,5R,6S)-5,6-epoxy-3-hydroxy-5,6-dihydro-12'-apo-beta-caroten-12'-
            al;
            (3S,5R,6R)-5,6-dihydroxy-6,7-didehydro-5,6-dihydro-12'-apo-beta-
            caroten-12'-al
COMMENT     Requires iron(II). Acts on 9-cis-violaxanthin and 9'-cis-neoxanthin
            but not on the all-trans isomers [2,3]. In vitro, it will cleave
            9-cis-zeaxanthin. Catalyses the first step of abscisic-acid
            biosynthesis from carotenoids in chloroplasts, in response to water
            stress. The other enzymes involved in the abscisic-acid biosynthesis
            pathway are EC 1.1.1.288 (xanthoxin dehydrogenase), EC 1.2.3.14
            (abscisic-aldehyde oxidase) and EC 1.14.13.93 [(+)-abscisic acid
            8'-hydroxylase].
REFERENCE   1  [PMID:9188535]
  AUTHORS   Schwartz SH, Tan BC, Gage DA, Zeevaart JA, McCarty DR.
  TITLE     Specific oxidative cleavage of carotenoids by VP14 of maize.
  JOURNAL   Science. 276 (1997) 1872-4.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   2  [PMID:9342392]
  AUTHORS   Tan BC, Schwartz SH, Zeevaart JA, McCarty DR.
  TITLE     Genetic control of abscisic acid biosynthesis in maize.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 12235-40.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   3  [PMID:10611388]
  AUTHORS   Qin X, Zeevaart JA.
  TITLE     The 9-cis-epoxycarotenoid cleavage reaction is the key regulatory
            step of abscisic acid biosynthesis in water-stressed bean.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 15354-61.
  ORGANISM  Phaseolus vulgaris
REFERENCE   4  [PMID:10929129]
  AUTHORS   Thompson AJ, Jackson AC, Symonds RC, Mulholland BJ, Dadswell AR,
            Blake PS, Burbidge A, Taylor IB.
  TITLE     Ectopic expression of a tomato 9-cis-epoxycarotenoid dioxygenase
            gene causes over-production of abscisic acid.
  JOURNAL   Plant. J. 23 (2000) 363-74.
  ORGANISM  Zea mays [GN:ezma], Lycopersicon esculentum [GN:eles], Arabidopsis
            thaliana [GN:ath]
REFERENCE   5  [PMID:11532178]
  AUTHORS   Iuchi S, Kobayashi M, Taji T, Naramoto M, Seki M, Kato T, Tabata S,
            Kakubari Y, Yamaguchi-Shinozaki K, Shinozaki K.
  TITLE     Regulation of drought tolerance by gene manipulation of
            9-cis-epoxycarotenoid dioxygenase, a key enzyme in abscisic acid
            biosynthesis in Arabidopsis.
  JOURNAL   Plant. J. 27 (2001) 325-33.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   6
  AUTHORS   Iuchi, S., Kobayashi, M., Taji, T., Naramoto, M., Seki, M., Kato,
            T., Tabata, S., Kakubari, Y., Yamaguchi-Shinozaki, K. and Shinozaki,
            K.
  TITLE     Regulation of drought tolerance by gene manipulation of
  JOURNAL    9-cis-epoxycarotenoid dioxygenase, a key enzyme in abscisic acid
REFERENCE    biosynthesis in Arabidopsis.
  AUTHORS   Plant J. 30 (2002) 611.
PATHWAY     PATH: map00906  Carotenoid biosynthesis - General
ORTHOLOGY   KO: K09840  9-cis-epoxycarotenoid dioxygenase
GENES       ATH: AT1G30100(NCED5) AT1G78390(NCED9) AT3G14440(NCED3)
                 AT3G24220(NCED6) AT4G18350(NCED2)
            OSA: 4333566
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.51
            ExPASy - ENZYME nomenclature database: 1.13.11.51
            ExplorEnz - The Enzyme Database: 1.13.11.51
            ERGO genome analysis and discovery system: 1.13.11.51
            BRENDA, the Enzyme Database: 1.13.11.51
///
ENTRY       EC 1.13.11.52               Enzyme
NAME        indoleamine 2,3-dioxygenase;
            IDO (ambiguous);
            tryptophan pyrrolase (ambiguous)
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     D-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)
REACTION    (1) D-tryptophan + O2 = N-formyl-D-kynurenine [RN:R07362];
            (2) L-tryptophan + O2 = N-formyl-L-kynurenine [RN:R00678]
ALL_REAC    R00678 R07362;
            (other) R02702 R02909 R03628
SUBSTRATE   D-tryptophan [CPD:C00525];
            O2 [CPD:C00007];
            L-tryptophan [CPD:C00078]
PRODUCT     N-formyl-D-kynurenine [CPD:C15605];
            N-formyl-L-kynurenine [CPD:C02700]
COMMENT     A protohemoprotein. Requires ascorbic acid and methylene blue for
            activity. This enzyme has broader substrate specificity than EC
            1.13.11.11, tryptophan 2,3-dioxygenase [1]. It is induced in
            response to pathological conditions and host-defense mechanisms and
            its distribution in mammals is not confined to the liver [2]. While
            the enzyme is more active with D-tryptophan than L-tryptophan, its
            only known function to date is in the metabolism of L-tryptophan
            [2,6]. Superoxide radicals can replace O2 as oxygen donor [4,7].
REFERENCE   1  [PMID:6065097]
  AUTHORS   Yamamoto S, Hayaishi O.
  TITLE     Tryptophan pyrrolase of rabbit intestine. D- and
            L-tryptophan-cleaving enzyme or enzymes.
  JOURNAL   J. Biol. Chem. 242 (1967) 5260-6.
  ORGANISM  rabbit
REFERENCE   2  [PMID:2428037]
  AUTHORS   Yasui H, Takai K, Yoshida R, Hayaishi O.
  TITLE     Interferon enhances tryptophan metabolism by inducing pulmonary
            indoleamine 2,3-dioxygenase: its possible occurrence in cancer
            patients.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 6622-6.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:2419335]
  AUTHORS   Takikawa O, Yoshida R, Kido R, Hayaishi O.
  TITLE     Tryptophan degradation in mice initiated by indoleamine
            2,3-dioxygenase.
  JOURNAL   J. Biol. Chem. 261 (1986) 3648-53.
  ORGANISM  mouse [GN:mmu]
REFERENCE   4  [PMID:194886]
  AUTHORS   Hirata F, Ohnishi T, Hayaishi O.
  TITLE     Indoleamine 2,3-dioxygenase. Characterization and properties of
            enzyme. O2- complex.
  JOURNAL   J. Biol. Chem. 252 (1977) 4637-42.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:10719243]
  AUTHORS   Dang Y, Dale WE, Brown OR.
  TITLE     Comparative effects of oxygen on indoleamine 2,3-dioxygenase and
            tryptophan 2,3-dioxygenase of the kynurenine pathway.
  JOURNAL   Free. Radic. Biol. Med. 28 (2000) 615-24.
  ORGANISM  human [GN:hsa], rat [GN:rno]
REFERENCE   6  [PMID:12766158]
  AUTHORS   Littlejohn TK, Takikawa O, Truscott RJ, Walker MJ.
  TITLE     Asp274 and his346 are essential for heme binding and catalytic
            function of human indoleamine 2,3-dioxygenase.
  JOURNAL   J. Biol. Chem. 278 (2003) 29525-31.
  ORGANISM  human [GN:hsa]
REFERENCE   7  [PMID:10731095]
  AUTHORS   Thomas SR, Stocker R.
  TITLE     Redox reactions related to indoleamine 2,3-dioxygenase and
            tryptophan metabolism along the kynurenine pathway.
  JOURNAL   Redox. Rep. 4 (1999) 199-220.
REFERENCE   8  [PMID:2334706]
  AUTHORS   Sono M.
  TITLE     Spectroscopic and equilibrium studies of ligand and organic
            substrate binding to indolamine 2,3-dioxygenase.
  JOURNAL   Biochemistry. 29 (1990) 1451-60.
  ORGANISM  rabbit
PATHWAY     PATH: map00380  Tryptophan metabolism
ORTHOLOGY   KO: K00463  indoleamine 2,3-dioxygenase
GENES       HSA: 3620(INDO)
            PTR: 464134(INDO)
            MMU: 15930(Indo)
            RNO: 66029(Indo)
            CFA: 475574(INDO) 482846(INDOL1)
            BTA: 506281(MGC179467)
            GGA: 426785(INDOL1)
            XTR: 448488(indo)
            SPU: 577419(LOC577419)
            SCE: YJR078W(BNA2)
            AGO: AGOS_ACR188C
            PIC: PICST_87443(BNA2)
            CAL: CaO19.583
            ANI: AN1858.2 AN2509.2
            AFM: AFUA_3G14250 AFUA_4G09830
            AOR: AO090003001248 AO090020000618 AO090038000578
            UMA: UM03728.1
            TET: TTHERM_00035520
            NOC: Noc_1709
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.52
            ExPASy - ENZYME nomenclature database: 1.13.11.52
            ExplorEnz - The Enzyme Database: 1.13.11.52
            ERGO genome analysis and discovery system: 1.13.11.52
            BRENDA, the Enzyme Database: 1.13.11.52
///
ENTRY       EC 1.13.11.53               Enzyme
NAME        acireductone dioxygenase (Ni2+-requiring);
            ARD;
            2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase (ambiguous);
            acireductone dioxygenase (ambiguous);
            E-2
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     1,2-dihydroxy-5-(methylthio)pent-1-en-3-one:oxygen oxidoreductase
            (formate- and CO-forming)
REACTION    1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 =
            3-(methylthio)propanoate + formate + CO [RN:R07363]
ALL_REAC    R07363
SUBSTRATE   1,2-dihydroxy-5-(methylthio)pent-1-en-3-one [CPD:C15606];
            O2 [CPD:C00007]
PRODUCT     3-(methylthio)propanoate;
            formate [CPD:C00058];
            CO [CPD:C00237]
COMMENT     Requires Ni2+. If iron(II) is bound instead of Ni2+, the reaction
            catalysed by EC 1.13.11.54, acireductone dioxygenase
            [iron(II)-requiring], occurs instead [1]. The enzyme from the
            bacterium Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC
            strain 8724 is involved in the methionine salvage pathway.
REFERENCE   1  [PMID:8407993]
  AUTHORS   Wray JW, Abeles RH.
  TITLE     A bacterial enzyme that catalyzes formation of carbon monoxide.
  JOURNAL   J. Biol. Chem. 268 (1993) 21466-9.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   2  [PMID:7852397]
  AUTHORS   Wray JW, Abeles RH.
  TITLE     The methionine salvage pathway in Klebsiella pneumoniae and rat
            liver. Identification and characterization of two novel
            dioxygenases.
  JOURNAL   J. Biol. Chem. 270 (1995) 3147-53.
  ORGANISM  Klebsiella pneumoniae, rat [GN:rno]
REFERENCE   3  [PMID:2838472]
  AUTHORS   Furfine ES, Abeles RH.
  TITLE     Intermediates in the conversion of 5'-S-methylthioadenosine to
            methionine in Klebsiella pneumoniae.
  JOURNAL   J. Biol. Chem. 263 (1988) 9598-606.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   4  [PMID:9880484]
  AUTHORS   Dai Y, Wensink PC, Abeles RH.
  TITLE     One protein, two enzymes.
  JOURNAL   J. Biol. Chem. 274 (1999) 1193-5.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   5  [PMID:10481280]
  AUTHORS   Mo H, Dai Y, Pochapsky SS, Pochapsky TC.
  TITLE     1H, 13C and 15N NMR assignments for a carbon monoxide generating
            metalloenzyme from Klebsiella pneumoniae.
  JOURNAL   J. Biomol. NMR. 14 (1999) 287-8.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   6  [PMID:11371200]
  AUTHORS   Dai Y, Pochapsky TC, Abeles RH.
  TITLE     Mechanistic studies of two dioxygenases in the methionine salvage
            pathway of Klebsiella pneumoniae.
  JOURNAL   Biochemistry. 40 (2001) 6379-87.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   7  [PMID:12022880]
  AUTHORS   Al-Mjeni F, Ju T, Pochapsky TC, Maroney MJ.
  TITLE     XAS investigation of the structure and function of Ni in
            acireductone dioxygenase.
  JOURNAL   Biochemistry. 41 (2002) 6761-9.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   8  [PMID:12402029]
  AUTHORS   Pochapsky TC, Pochapsky SS, Ju T, Mo H, Al-Mjeni F, Maroney MJ.
  TITLE     Modeling and experiment yields the structure of acireductone
            dioxygenase from Klebsiella pneumoniae.
  JOURNAL   Nat. Struct. Biol. 9 (2002) 966-72.
  ORGANISM  Klebsiella pneumoniae
PATHWAY     PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K08967  1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase
GENES       BSU: BG13285(mtnZ)
            BAN: BA4258
            BAR: GBAA4258
            BAA: BA_4717
            BAT: BAS3949
            BCE: BC4039
            BCA: BCE_4106
            BCZ: BCZK3796
            BTK: BT9727_3781
            BLI: BL03542(mtnZ)
            BLD: BLi01517(ykrZ)
            GKA: GK0956
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.53
            ExPASy - ENZYME nomenclature database: 1.13.11.53
            ExplorEnz - The Enzyme Database: 1.13.11.53
            ERGO genome analysis and discovery system: 1.13.11.53
            BRENDA, the Enzyme Database: 1.13.11.53
///
ENTRY       EC 1.13.11.54               Enzyme
NAME        acireductone dioxygenase [iron(II)-requiring];
            ARD';
            2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase (ambiguous);
            acireductone dioxygenase (ambiguous);
            E-2';
            E-3 dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     1,2-dihydroxy-5-(methylthio)pent-1-en-3-one:oxygen oxidoreductase
            (formate-forming)
REACTION    1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 =
            4-(methylthio)-2-oxobutanoate + formate [RN:R07364]
ALL_REAC    R07364
SUBSTRATE   1,2-dihydroxy-5-(methylthio)pent-1-en-3-one [CPD:C15606];
            O2 [CPD:C00007]
PRODUCT     4-methylthio-2-oxobutanoate [CPD:C01180];
            formate [CPD:C00058]
COMMENT     Requires iron(II). If Ni2+ is bound instead of iron(II), the
            reaction catalysed by EC 1.13.11.53, acireductone dioxygenase
            (Ni2+-requiring), occurs instead. The enzyme from the bacterium
            Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC strain 8724
            is involved in the methionine salvage pathway.
REFERENCE   1  [PMID:8407993]
  AUTHORS   Wray JW, Abeles RH.
  TITLE     A bacterial enzyme that catalyzes formation of carbon monoxide.
  JOURNAL   J. Biol. Chem. 268 (1993) 21466-9.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   2  [PMID:7852397]
  AUTHORS   Wray JW, Abeles RH.
  TITLE     The methionine salvage pathway in Klebsiella pneumoniae and rat
            liver. Identification and characterization of two novel
            dioxygenases.
  JOURNAL   J. Biol. Chem. 270 (1995) 3147-53.
  ORGANISM  Klebsiella pneumoniae, rat [GN:rno]
REFERENCE   3  [PMID:2838472]
  AUTHORS   Furfine ES, Abeles RH.
  TITLE     Intermediates in the conversion of 5'-S-methylthioadenosine to
            methionine in Klebsiella pneumoniae.
  JOURNAL   J. Biol. Chem. 263 (1988) 9598-606.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   4  [PMID:9880484]
  AUTHORS   Dai Y, Wensink PC, Abeles RH.
  TITLE     One protein, two enzymes.
  JOURNAL   J. Biol. Chem. 274 (1999) 1193-5.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   5  [PMID:10481280]
  AUTHORS   Mo H, Dai Y, Pochapsky SS, Pochapsky TC.
  TITLE     1H, 13C and 15N NMR assignments for a carbon monoxide generating
            metalloenzyme from Klebsiella pneumoniae.
  JOURNAL   J. Biomol. NMR. 14 (1999) 287-8.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   6  [PMID:11371200]
  AUTHORS   Dai Y, Pochapsky TC, Abeles RH.
  TITLE     Mechanistic studies of two dioxygenases in the methionine salvage
            pathway of Klebsiella pneumoniae.
  JOURNAL   Biochemistry. 40 (2001) 6379-87.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   7  [PMID:12022880]
  AUTHORS   Al-Mjeni F, Ju T, Pochapsky TC, Maroney MJ.
  TITLE     XAS investigation of the structure and function of Ni in
            acireductone dioxygenase.
  JOURNAL   Biochemistry. 41 (2002) 6761-9.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   8  [PMID:12402029]
  AUTHORS   Pochapsky TC, Pochapsky SS, Ju T, Mo H, Al-Mjeni F, Maroney MJ.
  TITLE     Modeling and experiment yields the structure of acireductone
            dioxygenase from Klebsiella pneumoniae.
  JOURNAL   Nat. Struct. Biol. 9 (2002) 966-72.
  ORGANISM  Klebsiella pneumoniae
PATHWAY     PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K08967  1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase
GENES       BSU: BG13285(mtnZ)
            BAN: BA4258
            BAR: GBAA4258
            BAA: BA_4717
            BAT: BAS3949
            BCE: BC4039
            BCA: BCE_4106
            BCZ: BCZK3796
            BTK: BT9727_3781
            BLI: BL03542(mtnZ)
            BLD: BLi01517(ykrZ)
            GKA: GK0956
STRUCTURES  PDB: 2HJI  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.54
            ExPASy - ENZYME nomenclature database: 1.13.11.54
            ExplorEnz - The Enzyme Database: 1.13.11.54
            ERGO genome analysis and discovery system: 1.13.11.54
            BRENDA, the Enzyme Database: 1.13.11.54
///
ENTRY       EC 1.13.11.55               Enzyme
NAME        sulfur oxygenase/reductase;
            SOR;
            sulfur oxygenase;
            sulfur oxygenase reductase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of two atoms of oxygen
SYSNAME     sulfur:oxygen oxidoreductase (hydrogen-sulfide- and sulfite-forming)
REACTION    4 sulfur + 4 H2O + O2 = 2 hydrogen sulfide + 2 bisulfite + 2 H+
            [RN:R07365]
ALL_REAC    R07365
SUBSTRATE   sulfur [CPD:C00087];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     hydrogen sulfide [CPD:C00283];
            bisulfite [CPD:C11481];
            H+ [CPD:C00080]
COMMENT     This enzyme, which is found in thermophilic microorganisms, contains
            one mononuclear none-heme iron centre per subunit. Elemental sulfur
            is both the electron donor and one of the two known acceptors, the
            other being oxygen. Another reaction product is thiosulfate, but
            this is probably formed non-enzymically at elevated temperature from
            sulfite and sulfur [1]. This enzyme differs from EC 1.13.11.18,
            sulfur dioxygenase and EC 1.97.1.3, sulfur reductase, in that both
            activities are found together.
REFERENCE   1  [PMID:2493451]
  AUTHORS   Kletzin A.
  TITLE     Coupled enzymatic production of sulfite, thiosulfate, and hydrogen
            sulfide from sulfur: purification and properties of a sulfur
            oxygenase reductase from the facultatively anaerobic archaebacterium
            Desulfurolobus ambivalens.
  JOURNAL   J. Bacteriol. 171 (1989) 1638-43.
  ORGANISM  Desulfurolobus ambivalens
REFERENCE   2  [PMID:1522063]
  AUTHORS   Kletzin A.
  TITLE     Molecular characterization of the sor gene, which encodes the sulfur
            oxygenase/reductase of the thermoacidophilic Archaeum Desulfurolobus
            ambivalens.
  JOURNAL   J. Bacteriol. 174 (1992) 5854-9.
  ORGANISM  Desulfurolobus ambivalens
REFERENCE   3  [PMID:12664265]
  AUTHORS   Sun CW, Chen ZW, He ZG, Zhou PJ, Liu SJ.
  TITLE     Purification and properties of the sulfur oxygenase/reductase from
            the acidothermophilic archaeon, Acidianus strain S5.
  JOURNAL   Extremophiles. 7 (2003) 131-4.
  ORGANISM  Acidianus sp.
REFERENCE   4  [PMID:15030315]
  AUTHORS   Urich T, Bandeiras TM, Leal SS, Rachel R, Albrecht T, Zimmermann P,
            Scholz C, Teixeira M, Gomes CM, Kletzin A.
  TITLE     The sulphur oxygenase reductase from Acidianus ambivalens is a
            multimeric protein containing a low-potential mononuclear non-haem
            iron centre.
  JOURNAL   Biochem. J. 381 (2004) 137-46.
  ORGANISM  Acidianus sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.11.55
            ExPASy - ENZYME nomenclature database: 1.13.11.55
            ExplorEnz - The Enzyme Database: 1.13.11.55
            ERGO genome analysis and discovery system: 1.13.11.55
            BRENDA, the Enzyme Database: 1.13.11.55
///
ENTRY       EC 1.13.11.-                Enzyme
CLASS       Oxidoreductases;
            Acting on single donors with incorporation of molecular oxygen
            (oxygenases);
            With incorporation of two atoms of oxygen
REACTION    (1) Oxaloacetate + 2-Oxoglutarate + NH3 <=>
            5-(2'-Carboxyethyl)-4,6-dihydroxypicolinate + 2 Oxygen [RN:R00356];
            (2) 3,4-Dihydroxybenzoate + Oxygen + NADH <=> Benzene-1,2,4-triol +
            CO2 + NAD+ + H2O [RN:R01629];
            (3) 3,4-Dihydroxybenzoate + Oxygen + NADPH <=> Benzene-1,2,4-triol +
            CO2 + NADP+ + H2O [RN:R01630];
            (4) Naphthalene-1,2-diol + Oxygen <=>
            2-Hydroxychromene-2-carboxylate [RN:R04117];
            (5) p-Benzenediol + Oxygen <=> cis,trans-4-Hydroxymuconic
            semialdehyde [RN:R05246];
            (6) p-Cumate + Oxygen + NADH <=>
            cis-2,3-Dihydroxy-2,3-dihydro-p-cumate + NAD+ [RN:R05247];
            (7) 2,3-Dihydroxy-p-cumate + Oxygen <=>
            2-Hydroxy-3-carboxy-6-oxo-7-methylocta-2,4-dienoate [RN:R05248];
            (8)
            1,1-Dichloro-2-(dihydroxy-4'-chlorophenyl)-2-(4'-
            chlorophenyl)ethylene + Oxygen <=>
            6-Oxo-2-hydroxy-7-(4'-chlorophenyl)-3,8,8-trichloroocta-2E,4E,7E-
            trienoate [RN:R05256];
            (9) 2,3-Dihydroxy 1,1,1-Trichloro-2,2-bis(4'-chlorophenyl)ethane +
            Oxygen <=>
            6-Oxo-2-hydroxy-7-(4'-chlorophenyl)-3,8,8,8-tetrachloroocta-2E,4E-
            dienoate [RN:R05257];
            (10) 4-Sulfocatechol + Oxygen <=> 3-Sulfomuconate [RN:R05278];
            (11) 2-Aminophenol + Oxygen <=> 2-Aminomuconate semialdehyde
            [RN:R05405];
            (12) 3,5-Dichlorocatechol + Oxygen <=> 2,4-Dichloro-cis,cis-muconate
            [RN:R05407];
            (13) 2,6-Dichlorohydroquinone + Oxygen + H2O <=>
            2-Chloromaleylacetate + HCl [RN:R05408];
            (14) 3,6-Dichlorocatechol + Oxygen <=> 2,5-Dichloro-cis,cis-muconate
            [RN:R05409];
            (15) 3,4-Dihydroxyfluorene + Oxygen <=>
            2-Hydroxy-4-(1-oxo-1,3-dihydro-2H-inden-2-ylidene)-but-2-enoic acid
            [RN:R05410];
            (16) 2,2',3-Trihydroxybiphenyl + Oxygen <=>
            2-Hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate [RN:R05411];
            (17) 1,2-Dihydroxyfluorene + Oxygen <=>
            2-Hydroxy-4-(2-oxo-1,3-dihydro-2H-inden-1-ylidene)but-2-enoic acid
            [RN:R05412];
            (18) 2,2',3-Trihydroxydiphenylether + Oxygen <=>
            2-Hydroxy-6-oxo-6-(2-hydroxyphenoxy)-hexa-2,4-dienoate [RN:R05413];
            (19) Carbazole + Oxygen + NADH + H+ <=> 2'-Aminobiphenyl-2,3-diol +
            NAD+ [RN:R05414];
            (20) 2'-Aminobiphenyl-2,3-diol + Oxygen <=>
            2-Hydroxy-6-oxo-(2'-aminophenyl)-hexa-2,4-dienoate [RN:R05415];
            (21) 3-Ethylcatechol + Oxygen <=> 2-Hydroxy-6-oxo-octa-2,4-dienoate
            + H+ [RN:R05416];
            (22) Styrene + Oxygen + NADH + H+ <=> Styrene cis-glycol + NAD+
            [RN:R05417];
            (23) Phenanthrene-3,4-diol + Oxygen <=>
            2-Hydroxy-2H-benzo[h]chromene-2-carboxylate [RN:R05650];
            (24) Phenanthracene + NADH + H+ + Oxygen <=>
            (+)-cis-3,4-Dihydrophenanthrene-3,4-diol + NAD+ [RN:R05843];
            (25) (5Z,8Z,11Z,14Z)-Icosatetraenoic acid + Oxygen <=> 12(R)-HPETE
            [RN:R07038];
            (26) (5Z,8Z,11Z,14Z)-Icosatetraenoic acid + Oxygen <=> 11(R)-HPETE
            [RN:R07047];
            (27) (5Z,8Z,11Z,14Z)-Icosatetraenoic acid + Oxygen <=> 9(S)-HPETE
            [RN:R07049];
            (28) (5Z,8Z,11Z,14Z)-Icosatetraenoic acid + Oxygen <=> 8(S)-HPETE
            [RN:R07053];
            (29) 1,2-Dihydroxynaphthalene-6-sulfonate + Oxygen <=>
            (Z)-4-(2-Hydroxy-5-sulfonatophenyl)-2-oxo-3-butenoate [RN:R07684];
            (30) 3-Hydroxy-2-naphthoate + Oxygen <=>
            3-[6-(Carboxymethylene)cyclohexa-2,4-dien-1-ylidene]-2-oxopropanate
            [RN:R07691];
            (31) 1,2-Anthracenediol + Oxygen <=>
            4-(3-Hydroxy-2-naphthyl)-2-oxobut-3-enoic acid [RN:R07701];
            (32) 1,2-Anthracenediol + Oxygen <=>
            3-(2-Carboxyvinyl)naphthalene-2-carboxylic acid [RN:R07702]
SUBSTRATE   Oxaloacetate [CPD:C00036];
            2-Oxoglutarate [CPD:C00026];
            NH3 [CPD:C00014];
            3,4-Dihydroxybenzoate [CPD:C00230];
            Oxygen [CPD:C00007];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            Naphthalene-1,2-diol [CPD:C03012];
            p-Benzenediol [CPD:C00530];
            p-Cumate [CPD:C06578];
            2,3-Dihydroxy-p-cumate [CPD:C06580];
            1,1-Dichloro-2-(dihydroxy-4'-chlorophenyl)-2-(4'-
            chlorophenyl)ethylene [CPD:C06644];
            2,3-Dihydroxy 1,1,1-Trichloro-2,2-bis(4'-chlorophenyl)ethane
            [CPD:C06650];
            4-Sulfocatechol [CPD:C06674];
            2-Aminophenol [CPD:C01987];
            3,5-Dichlorocatechol [CPD:C02933];
            2,6-Dichlorohydroquinone [CPD:C07097];
            H2O [CPD:C00001];
            3,6-Dichlorocatechol [CPD:C07094];
            3,4-Dihydroxyfluorene [CPD:C07717];
            2,2',3-Trihydroxybiphenyl [CPD:C03569];
            1,2-Dihydroxyfluorene [CPD:C07724];
            2,2',3-Trihydroxydiphenylether [CPD:C07733];
            Carbazole [CPD:C08060];
            H+ [CPD:C00080];
            2'-Aminobiphenyl-2,3-diol [CPD:C08061];
            3-Ethylcatechol [CPD:C06728];
            Styrene [CPD:C07083];
            Phenanthrene-3,4-diol [CPD:C03164];
            Phenanthracene [CPD:C11422];
            (5Z,8Z,11Z,14Z)-Icosatetraenoic acid [CPD:C00219]
PRODUCT     5-(2'-Carboxyethyl)-4,6-dihydroxypicolinate [CPD:C05655];
            Oxygen [CPD:C00007];
            Benzene-1,2,4-triol [CPD:C02814];
            CO2 [CPD:C00011];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001];
            NADP+ [CPD:C00006];
            2-Hydroxychromene-2-carboxylate [CPD:C06204];
            cis,trans-4-Hydroxymuconic semialdehyde [CPD:C06603];
            cis-2,3-Dihydroxy-2,3-dihydro-p-cumate [CPD:C06579];
            2-Hydroxy-3-carboxy-6-oxo-7-methylocta-2,4-dienoate [CPD:C06581];
            6-Oxo-2-hydroxy-7-(4'-chlorophenyl)-3,8,8-trichloroocta-2E,4E,7E-
            trienoate [CPD:C06645];
            6-Oxo-2-hydroxy-7-(4'-chlorophenyl)-3,8,8,8-tetrachloroocta-2E,4E-
            dienoate [CPD:C06651];
            3-Sulfomuconate [CPD:C06675];
            2-Aminomuconate semialdehyde [CPD:C03824];
            2,4-Dichloro-cis,cis-muconate [CPD:C03918];
            2-Chloromaleylacetate [CPD:C06329];
            HCl [CPD:C01327];
            2,5-Dichloro-cis,cis-muconate [CPD:C07095];
            2-Hydroxy-4-(1-oxo-1,3-dihydro-2H-inden-2-ylidene)-but-2-enoic acid
            [CPD:C07718];
            2-Hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate [CPD:C07731];
            2-Hydroxy-4-(2-oxo-1,3-dihydro-2H-inden-1-ylidene)but-2-enoic acid
            [CPD:C07725];
            2-Hydroxy-6-oxo-6-(2-hydroxyphenoxy)-hexa-2,4-dienoate [CPD:C07734];
            2'-Aminobiphenyl-2,3-diol [CPD:C08061];
            2-Hydroxy-6-oxo-(2'-aminophenyl)-hexa-2,4-dienoate [CPD:C08062];
            2-Hydroxy-6-oxo-octa-2,4-dienoate [CPD:C07123];
            H+ [CPD:C00080];
            Styrene cis-glycol [CPD:C07084];
            2-Hydroxy-2H-benzo[h]chromene-2-carboxylate [CPD:C11425];
            (+)-cis-3,4-Dihydrophenanthrene-3,4-diol [CPD:C04468];
            12(R)-HPETE [CPD:C14812];
            11(R)-HPETE [CPD:C14820];
            9(S)-HPETE [CPD:C14821];
            8(S)-HPETE [CPD:C14823]
///
ENTRY       EC 1.13.12.1                Enzyme
NAME        arginine 2-monooxygenase;
            arginine monooxygenase;
            arginine decarboxylase;
            arginine oxygenase (decarboxylating);
            arginine decarboxy-oxidase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of one atom of oxygen (internal monooxygenases or
            internal mixed-function oxidases)
SYSNAME     L-arginine:oxygen 2-oxidoreductase (decarboxylating)
REACTION    L-arginine + O2 = 4-guanidinobutanamide + CO2 + H2O [RN:R00559]
ALL_REAC    R00559
SUBSTRATE   L-arginine [CPD:C00062];
            O2 [CPD:C00007]
PRODUCT     4-guanidinobutanamide [CPD:C03078];
            CO2 [CPD:C00011];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016];
            Flavoprotein [CPD:C06411]
COMMENT     A flavoprotein. Also acts on canavanine and homoarginine.
REFERENCE   1  [PMID:4295160]
  AUTHORS   Olomucki A, Pho DB, Lebar R, Delcambe L, Thoai NV.
  TITLE     [Arginine oxygenase (decarboxylating). V. Purification and flavin
            nature]
  JOURNAL   Biochim. Biophys. Acta. 151 (1968) 353-66.
  ORGANISM  Streptomyces griseus
REFERENCE   2
  AUTHORS   Thoai, N.V. and Olomucki, A.
  TITLE     Arginine decarboxy-oxydase. I. Caracteres et nature de l'enzyme.
  JOURNAL   Biochim. Biophys. Acta 59 (1962) 533-544.
  ORGANISM  Streptomyces griseus
REFERENCE   3
  AUTHORS   Thoai, N.V. and Olomucki, A.
  TITLE     Arginine decarboxy-oxydase. II. Oxydation de la canavanine et de
            l'homoarginine en beta-guanidopropionamide et en
            delta-guanidovaleramide.
  JOURNAL   Biochim. Biophys. Acta 59 (1962) 545-552.
  ORGANISM  Streptomyces griseus
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.12.1
            ExPASy - ENZYME nomenclature database: 1.13.12.1
            ExplorEnz - The Enzyme Database: 1.13.12.1
            ERGO genome analysis and discovery system: 1.13.12.1
            BRENDA, the Enzyme Database: 1.13.12.1
            CAS: 9027-36-5
///
ENTRY       EC 1.13.12.2                Enzyme
NAME        lysine 2-monooxygenase;
            lysine oxygenase;
            lysine monooxygenase;
            L-lysine-2-monooxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of one atom of oxygen (internal monooxygenases or
            internal mixed-function oxidases)
SYSNAME     L-lysine:oxygen 2-oxidoreductase (decarboxylating)
REACTION    L-lysine + O2 = 5-aminopentanamide + CO2 + H2O [RN:R00449]
ALL_REAC    R00449
SUBSTRATE   L-lysine [CPD:C00047];
            O2 [CPD:C00007]
PRODUCT     5-aminopentanamide [CPD:C00990];
            CO2 [CPD:C00011];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Also acts on other diamino acids.
REFERENCE   1  [PMID:4624115]
  AUTHORS   Nakazawa T, Hori K, Hayaishi O.
  TITLE     Studies on monooxygenases. V. Manifestation of amino acid oxidase
            activity by L-lysine monooxygenase.
  JOURNAL   J. Biol. Chem. 247 (1972) 3439-44.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   2  [PMID:5911646]
  AUTHORS   Takeda H, Hayaishi O.
  TITLE     Crystalline L-lysine oxygenase.
  JOURNAL   J. Biol. Chem. 241 (1966) 2733-6.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   3  [PMID:5772467]
  AUTHORS   Takeda H, Yamamoto S, Kojima Y, Hayaishi O.
  TITLE     Studies on monooxygenases. I. General properties of crystalline
            L-lysine monooxygenase.
  JOURNAL   J. Biol. Chem. 244 (1969) 2935-41.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.12.2
            ExPASy - ENZYME nomenclature database: 1.13.12.2
            ExplorEnz - The Enzyme Database: 1.13.12.2
            ERGO genome analysis and discovery system: 1.13.12.2
            BRENDA, the Enzyme Database: 1.13.12.2
            CAS: 9031-22-5
///
ENTRY       EC 1.13.12.3                Enzyme
NAME        tryptophan 2-monooxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of one atom of oxygen (internal monooxygenases or
            internal mixed-function oxidases)
SYSNAME     L-tryptophan:oxygen 2-oxidoreductase (decarboxylating)
REACTION    L-tryptophan + O2 = (indol-3-yl)acetamide + CO2 + H2O [RN:R00679]
ALL_REAC    R00679
SUBSTRATE   L-tryptophan [CPD:C00078];
            O2 [CPD:C00007]
PRODUCT     (indol-3-yl)acetamide;
            CO2 [CPD:C00011];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:5916389]
  AUTHORS   Kosuge T, Heskett MG, Wilson EE.
  TITLE     Microbial synthesis and degradation of indole-3-acetic acid. I. The
            conversion of L-tryptophan to indole-3-acetamide by an enzyme system
            from Pseudomonas savastanoi.
  JOURNAL   J. Biol. Chem. 241 (1966) 3738-44.
  ORGANISM  Pseudomonas savastanoi
REFERENCE   2
  AUTHORS   Kuo, T.T. and Kosuge, T.
  TITLE     Factors influencing the production and further metabolism of
            indole-3-acetic acid by Pseudomonas savastanoi.
  JOURNAL   J. Gen. Appl. Microbiol. 15 (1969) 51-63.
  ORGANISM  Pseudomonas savastanoi
PATHWAY     PATH: map00380  Tryptophan metabolism
ORTHOLOGY   KO: K00466  tryptophan 2-monooxygenase
GENES       PAP: PSPA7_3191
            PFO: Pfl_5154
            RSO: RSc3151
            BXE: Bxe_C1245
            ATU: Atu6011(tms1)
            ATC: AGR_pTi_49(iaaM)
            RDE: RD1_1495
            RHA: RHA1_ro03531
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.12.3
            ExPASy - ENZYME nomenclature database: 1.13.12.3
            ExplorEnz - The Enzyme Database: 1.13.12.3
            ERGO genome analysis and discovery system: 1.13.12.3
            BRENDA, the Enzyme Database: 1.13.12.3
            CAS: 37256-65-8
///
ENTRY       EC 1.13.12.4                Enzyme
NAME        lactate 2-monooxygenase;
            lactate oxidative decarboxylase;
            lactate oxidase;
            lactic oxygenase;
            lactate oxygenase;
            lactic oxidase;
            L-lactate monooxygenase;
            lactate monooxygenase;
            L-lactate-2-monooxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of one atom of oxygen (internal monooxygenases or
            internal mixed-function oxidases)
SYSNAME     (S)-lactate:oxygen 2-oxidoreductase (decarboxylating)
REACTION    (S)-lactate + O2 = acetate + CO2 + H2O [RN:R00319]
ALL_REAC    R00319
SUBSTRATE   (S)-lactate [CPD:C00186];
            O2 [CPD:C00007]
PRODUCT     acetate [CPD:C00033];
            CO2 [CPD:C00011];
            H2O [CPD:C00001]
COFACTOR    FMN [CPD:C00061]
COMMENT     A flavoprotein (FMN).
REFERENCE   1
  AUTHORS   Hayaishi, O. and Sutton, W.B.
  TITLE     Enzymatic oxygen fixation into acetate concomitant with the
            enzymatic decarboxylation of L-lactate.
  JOURNAL   J. Am. Chem. Soc. 79 (1957) 4809-4810.
  ORGANISM  Mycobacterium phlei
REFERENCE   2  [PMID:13428772]
  AUTHORS   SUTTON WB.
  TITLE     Mechanism of action and crystallization of lactic oxidative
            decarboxylase from Mycobacterium phlei.
  JOURNAL   J. Biol. Chem. 226 (1957) 395-405.
  ORGANISM  Mycobacterium phlei
PATHWAY     PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K00467  lactate 2-monooxygenase
GENES       AFM: AFUA_4G07050
            CCR: CC_1396
            LSA: LSA0664(loxL1N) LSA0665(loxL1I) LSA0666(loxL1C)
                 LSA1399(loxL2)
            MAV: MAV_3747 MAV_4345
            MSM: MSMEG_2512 MSMEG_3962
            MMC: Mmcs_1989
            SEN: SACE_6523
            RXY: Rxyl_1052
            DGE: Dgeo_0626
            TTH: TTC1744
            PTO: PTO1012
STRUCTURES  PDB: 2DU2  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.12.4
            ExPASy - ENZYME nomenclature database: 1.13.12.4
            ExplorEnz - The Enzyme Database: 1.13.12.4
            ERGO genome analysis and discovery system: 1.13.12.4
            BRENDA, the Enzyme Database: 1.13.12.4
            CAS: 9028-72-2
///
ENTRY       EC 1.13.12.5                Enzyme
NAME        Renilla-luciferin 2-monooxygenase;
            Renilla-type luciferase;
            aequorin;
            luciferase (Renilla luciferin)
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of one atom of oxygen (internal monooxygenases or
            internal mixed-function oxidases)
SYSNAME     Renilla-luciferin:oxygen 2-oxidoreductase (decarboxylating)
REACTION    Renilla luciferin + O2 = oxidized Renilla luciferin + CO2 + hnu
            [RN:R03137]
ALL_REAC    R03137
SUBSTRATE   Renilla luciferin [CPD:C00982];
            O2 [CPD:C00007]
PRODUCT     oxidized Renilla luciferin [CPD:C03717];
            CO2 [CPD:C00011];
            hn [CPD:C00205]
COMMENT     From the soft coral coelenterate Renilla reniformis. The luciferin
            is bound to a luciferin-binding protein (BP-LH2). The bioluminescent
            reaction between the luciferin complex, luciferase and oxygen is
            triggered by calcium ions. In vivo, the excited state
            luciferin---luciferase complex undergoes the process of nonradiative
            energy transfer to an accessory protein, Renilla green fluorescent
            protein, which results in green bioluminescence. In vitro, Renilla
            luciferase emits blue light in the absence of any green fluorescent
            protein.
REFERENCE   1  [PMID:4154104]
  AUTHORS   Cormier MJ, Hori K, Anderson JM.
  TITLE     Bioluminescence in coelenterates.
  JOURNAL   Biochim. Biophys. Acta. 346 (1974) 137-64.
  ORGANISM  Renilla reniformis
REFERENCE   2  [PMID:237531]
  AUTHORS   Hori K, Anderson JM, Ward WW, Cormier MJ.
  TITLE     Renilla luciferin as the substrate for calcium induced photoprotein
            bioluminescence. Assignment of luciferin tautomers in aequorin and
            mnemiopsin.
  JOURNAL   Biochemistry. 14 (1975) 2371-6.
  ORGANISM  Renilla reniformis
REFERENCE   3  [PMID:236561]
  AUTHORS   Shimomura O, Johnson FH.
  TITLE     Chemical nature of bioluminescence systems in coelenterates.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 72 (1975) 1546-9.
  ORGANISM  Renilla reniformis
REFERENCE   4  [PMID:33174]
  AUTHORS   Charbonneau H, Cormier MJ.
  TITLE     Ca2+-induced bioluminescence in Renilla reniformis. Purification and
            characterization of a calcium-triggered luciferin-binding protein.
  JOURNAL   J. Biol. Chem. 254 (1979) 769-80.
  ORGANISM  Renilla reniformis
REFERENCE   5  [PMID:4149963]
  AUTHORS   Anderson JM, Charbonneau H, Cormier MJ.
  TITLE     Mechanism of calcium induction of Renilla bioluminescence.
            Involvement of a calcium-triggered luciferin binding protein.
  JOURNAL   Biochemistry. 13 (1974) 1195-200.
  ORGANISM  Renilla reniformis, Renilla muelleri
REFERENCE   6  [PMID:1674607]
  AUTHORS   Lorenz WW, McCann RO, Longiaru M, Cormier MJ.
  TITLE     Isolation and expression of a cDNA encoding Renilla reniformis
            luciferase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 4438-42.
  ORGANISM  Renilla reniformis
STRUCTURES  PDB: 1QV0  1QV1  2PSD  2PSE  2PSF  2PSH  2PSJ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.12.5
            ExPASy - ENZYME nomenclature database: 1.13.12.5
            ExplorEnz - The Enzyme Database: 1.13.12.5
            ERGO genome analysis and discovery system: 1.13.12.5
            BRENDA, the Enzyme Database: 1.13.12.5
            CAS: 61869-41-8
///
ENTRY       EC 1.13.12.6                Enzyme
NAME        Cypridina-luciferin 2-monooxygenase;
            Cypridina-type luciferase;
            luciferase (Cypridina luciferin);
            Cypridina luciferase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of one atom of oxygen (internal monooxygenases or
            internal mixed-function oxidases)
SYSNAME     Cypridina-luciferin:oxygen 2-oxidoreductase (decarboxylating)
REACTION    Cypridina luciferin + O2 = oxidized Cypridina luciferin + CO2 + hnu
            [RN:R04063]
ALL_REAC    R04063
SUBSTRATE   Cypridina luciferin [CPD:C02825];
            O2 [CPD:C00007]
PRODUCT     oxidized Cypridina luciferin [CPD:C03887];
            CO2 [CPD:C00011];
            hn [CPD:C00205]
COMMENT     Cypridina is a bioluminescent crustacea. The luciferins (and
            presumably the luciferases, since they cross-react) of some luminous
            fish (e.g. Apogon, Parapriacanthus, Porichthys) are apparently
            similar. The enzyme may be assayed by measurement of light emission.
REFERENCE   1  [PMID:5624784]
  AUTHORS   Cormier MJ, Crane JM Jr, Nakano Y.
  TITLE     Evidence for the identity of the luminescent systems of Porichthys
            porosissimus (fish) and Cypridina hilgendorfii (crustacean).
  JOURNAL   Biochem. Biophys. Res. Commun. 29 (1967) 747-52.
  ORGANISM  Porichthys porosissimus, Cypridina hilgendorfii
REFERENCE   2
  AUTHORS   Karpetsky, T.P. and White, E.H.
  TITLE     The synthesis of Cypridina etioluciferamine and the proof of the
            structure of Cypridina luciferin.
  JOURNAL   Tetrahedron 29 (1973) 3761-3773.
  ORGANISM  Cypridina sp.
REFERENCE   3
  AUTHORS   Kishi, Y., Goto, T., Hirata, Y., Shiromura, O. and Johnson, F.H.
  TITLE     Cypridina bioluminescence. I. Structure of Cypridina luciferin.
  JOURNAL   Tetrahedron Lett. (1966) 3427-3436.
  ORGANISM  Cypridina hilgendorfii
REFERENCE   4  [PMID:4433517]
  AUTHORS   Tsuji FI, Lynch RV 3rd, Stevens CL.
  TITLE     Some properties of luciferase from the bioluminescent crustacean,
            Cypridina hilgendorfii.
  JOURNAL   Biochemistry. 13 (1974) 5204-9.
  ORGANISM  Cypridina hilgendorfii
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.12.6
            ExPASy - ENZYME nomenclature database: 1.13.12.6
            ExplorEnz - The Enzyme Database: 1.13.12.6
            ERGO genome analysis and discovery system: 1.13.12.6
            BRENDA, the Enzyme Database: 1.13.12.6
            CAS: 61969-99-1
///
ENTRY       EC 1.13.12.7                Enzyme
NAME        Photinus-luciferin 4-monooxygenase (ATP-hydrolysing);
            firefly luciferase;
            luciferase (firefly luciferin);
            Photinus luciferin 4-monooxygenase (adenosine
            triphosphate-hydrolyzing);
            firefly luciferin luciferase;
            Photinus pyralis luciferase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of one atom of oxygen (internal monooxygenases or
            internal mixed-function oxidases)
SYSNAME     Photinus-luciferin:oxygen 4-oxidoreductase (decarboxylating,
            ATP-hydrolysing)
REACTION    Photinus luciferin + O2 + ATP = oxidized Photinus luciferin + CO2 +
            AMP + diphosphate + hnu [RN:R04036]
ALL_REAC    R04036
SUBSTRATE   Photinus luciferin [CPD:C02740];
            O2 [CPD:C00007];
            ATP [CPD:C00002]
PRODUCT     oxidized Photinus luciferin [CPD:C03797];
            CO2 [CPD:C00011];
            AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            hn [CPD:C00205]
COMMENT     Photinus (firefly) is a bioluminescent insect. The first step in the
            reaction is the formation of an acid anhydride between the
            carboxylic group and AMP, with the release of diphosphate. The
            enzyme may be assayed by measurement of light emission.
REFERENCE   1  [PMID:6064360]
  AUTHORS   Hopkins TA, Seliger HH, White EH, Cass MH.
  TITLE     The chemiluminescence of firefly luciferin. A model for the
            bioluminescent reaction and identification of the product excited
            state.
  JOURNAL   J. Am. Chem. Soc. 89 (1967) 7148-50.
  ORGANISM  Photinus pyralis
REFERENCE   2
  AUTHORS   White, E.H., McCapra, F., Field, G.F. and McElroy, W.D.
  TITLE     The structure and synthesis of firefly luciferin.
  JOURNAL   J. Am. Chem. Soc. 83 (1961) 2402-2403.
  ORGANISM  Photinus pyralis
REFERENCE   3  [PMID:5784183]
  AUTHORS   White EH, Rapaport E, Hopkins TA, Seliger HH.
  TITLE     Chemi- and bioluminescence of firefly luciferin.
  JOURNAL   J. Am. Chem. Soc. 91 (1969) 2178-80.
  ORGANISM  Photinus pyralis
ORTHOLOGY   KO: K05914  
GENES       AVA: Ava_C0002
STRUCTURES  PDB: 1BA3  1LCI  2D1Q  2D1R  2D1S  2D1T  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.12.7
            ExPASy - ENZYME nomenclature database: 1.13.12.7
            ExplorEnz - The Enzyme Database: 1.13.12.7
            ERGO genome analysis and discovery system: 1.13.12.7
            BRENDA, the Enzyme Database: 1.13.12.7
            CAS: 61970-00-1
///
ENTRY       EC 1.13.12.8                Enzyme
NAME        Watasenia-luciferin 2-monooxygenase;
            Watasenia-type luciferase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of one atom of oxygen (internal monooxygenases or
            internal mixed-function oxidases)
SYSNAME     Watasenia-luciferin:oxygen 2-oxidoreductase (decarboxylating)
REACTION    Watasenia luciferin + O2 = oxidized Watasenia luciferin + CO2 + hnu
            [RN:R04078]
ALL_REAC    R04078
SUBSTRATE   Watasenia luciferin [CPD:C02894];
            O2 [CPD:C00007]
PRODUCT     oxidized Watasenia luciferin [CPD:C03888];
            CO2 [CPD:C00011];
            hn [CPD:C00205]
COMMENT     The enzyme from the luminous squid Watasenia may be assayed by
            measurement of light emission.
REFERENCE   1
  AUTHORS   Inoue, S., Kakoi, H. and Goto, T.
  TITLE     Squid bioluminescence. III. Isolation and structure of Watasenia
            luciferin.
  JOURNAL   Tetrahedron Lett. (1976) 2971-2974.
  ORGANISM  Watasenia scintillans
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.12.8
            ExPASy - ENZYME nomenclature database: 1.13.12.8
            ExplorEnz - The Enzyme Database: 1.13.12.8
            ERGO genome analysis and discovery system: 1.13.12.8
            BRENDA, the Enzyme Database: 1.13.12.8
///
ENTRY       EC 1.13.12.9                Enzyme
NAME        phenylalanine 2-monooxygenase;
            L-phenylalanine oxidase (deaminating and decarboxylating);
            phenylalanine (deaminating, decarboxylating)oxidase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of one atom of oxygen (internal monooxygenases or
            internal mixed-function oxidases)
SYSNAME     L-phenylalanine:oxygen 2-oxidoreductase (decarboxylating)
REACTION    L-phenylalanine + O2 = 2-phenylacetamide + CO2 + H2O [RN:R00690]
ALL_REAC    R00690
SUBSTRATE   L-phenylalanine [CPD:C00079];
            O2 [CPD:C00007]
PRODUCT     2-phenylacetamide [CPD:C02505];
            CO2 [CPD:C00011];
            H2O [CPD:C00001]
COMMENT     The reaction shown above is about 80% of the reaction catalysed; the
            remaining 20% is: L-phenylalanine + O2 + H2O = 3-phenylpyruvic acid
            + ammonia + H2O2 a reaction similar to that of EC 1.4.3.2,
            L-amino-acid oxidase.
REFERENCE   1  [PMID:7174643]
  AUTHORS   Koyama H.
  TITLE     Purification and characterization of a novel L-phenylalanine oxidase
            (Deaminating and decarboxylating) from Pseudomonas sp. P-501.
  JOURNAL   J. Biochem. (Tokyo). 92 (1982) 1235-40.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:6501250]
  AUTHORS   Koyama H.
  TITLE     Oxidation and oxygenation of L-amino acids catalyzed by a
            L-phenylalanine oxidase (deaminating and decarboxylating) from
            Pseudomonas sp. P-501.
  JOURNAL   J. Biochem. (Tokyo). 96 (1984) 421-7.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:6692570]
  AUTHORS   Koyama H.
  TITLE     A simple and rapid enzymatic determination of L-phenylalanine with a
            novel L-phenylalanine oxidase (deaminating and decarboxylating) from
            Pseudomonas sp. P-501.
  JOURNAL   Clin. Chim. Acta. 136 (1984) 131-6.
  ORGANISM  Pseudomonas sp.
REFERENCE   4  [PMID:3818566]
  AUTHORS   Koyama H, Suzuki H.
  TITLE     Spectral and kinetic studies on Pseudomonas L-phenylalanine oxidase
            (deaminating and decarboxylating).
  JOURNAL   J. Biochem. (Tokyo). 100 (1986) 859-66.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00360  Phenylalanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.12.9
            ExPASy - ENZYME nomenclature database: 1.13.12.9
            ExplorEnz - The Enzyme Database: 1.13.12.9
            ERGO genome analysis and discovery system: 1.13.12.9
            BRENDA, the Enzyme Database: 1.13.12.9
            CAS: 84012-76-0;
///
ENTRY       EC 1.13.12.10     Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of one atom of oxygen (internal monooxygenases or
            internal mixed-function oxidases)
COMMENT     Deleted entry: lysine 6-monooxygenase. reaction covered by EC
            1.14.13.59, L-lysine 6-monooxygenase (NADPH) (EC 1.13.12.10 created
            1989, modified 1999, deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.12.10
            ExPASy - ENZYME nomenclature database: 1.13.12.10
            ExplorEnz - The Enzyme Database: 1.13.12.10
            ERGO genome analysis and discovery system: 1.13.12.10
            BRENDA, the Enzyme Database: 1.13.12.10
///
ENTRY       EC 1.13.12.11     Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of one atom of oxygen (internal monooxygenases or
            internal mixed-function oxidases)
COMMENT     Deleted entry: methylphenyltetrahydropyridine N-monooxygenase. The
            activity is due to EC 1.14.13.8, flavin-containing monooxygenase.
            (EC 1.13.12.11 created 1992, deleted 2006)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.12.11
            ExPASy - ENZYME nomenclature database: 1.13.12.11
            ExplorEnz - The Enzyme Database: 1.13.12.11
            ERGO genome analysis and discovery system: 1.13.12.11
            BRENDA, the Enzyme Database: 1.13.12.11
///
ENTRY       EC 1.13.12.12               Enzyme
NAME        apo-beta-carotenoid-14',13'-dioxygenase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of one atom of oxygen (internal monooxygenases or
            internal mixed-function oxidases)
SYSNAME     8'-apo-beta-carotenol:O2 oxidoreductase
REACTION    8'-apo-beta-carotenol + O2 = 14'-apo-beta-carotenal + H2O
            [RN:R05319]
ALL_REAC    R05319
SUBSTRATE   8'-apo-beta-carotenol [CPD:C06733];
            O2 [CPD:C00007]
PRODUCT     14'-apo-beta-carotenal [CPD:C06734];
            H2O [CPD:C00001]
COMMENT     A thiol-dependent enzyme. Unlike EC 1.14.99.36,
            beta-carotene-15,15'-monooxygenase, it is not active towards
            beta-carotene. Presumably 2-methyl-6-oxohepta-2,4-dienal is also
            formed in this reaction.
REFERENCE   1  [PMID:9331970]
  AUTHORS   Dmitrovskii AA, Gessler NN, Gomboeva SB, Ershov YuV, Bykhovsky VYa.
  TITLE     Enzymatic oxidation of beta-apo-8'-carotenol to
            beta-apo-14'-carotenal by an enzyme different from
            beta-carotene-15,15'-dioxygenase.
  JOURNAL   Biochemistry. (Mosc). 62 (1997) 787-92.
  ORGANISM  rat [GN:rno], rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.12.12
            ExPASy - ENZYME nomenclature database: 1.13.12.12
            ExplorEnz - The Enzyme Database: 1.13.12.12
            ERGO genome analysis and discovery system: 1.13.12.12
            BRENDA, the Enzyme Database: 1.13.12.12
///
ENTRY       EC 1.13.12.13               Enzyme
NAME        Oplophorus-luciferin 2-monooxygenase;
            Oplophorus luciferase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of one atom of oxygen (internal monooxygenases or
            internal mixed-function oxidases)
SYSNAME     Oplophorus-luciferin:oxygen 2-oxidoreductase (decarboxylating)
REACTION    Oplophorus luciferin + O2 = oxidized Oplophorus luciferin + CO2 +
            hnu [RN:R07128]
ALL_REAC    R07128
SUBSTRATE   Oplophorus luciferin [CPD:C15037];
            O2 [CPD:C00007]
PRODUCT     oxidized Oplophorus luciferin [CPD:C15038];
            CO2 [CPD:C00011];
            hn [CPD:C00205]
COMMENT     The luciferase from the deep sea shrimp Oplophorus gracilorostris is
            a complex composed of more than one protein. The enzyme's
            specificity is quite broad, with both coelenterazine and
            bisdeoxycoelenterazine being good substrates.
REFERENCE   1  [PMID:629957]
  AUTHORS   Shimomura O, Masugi T, Johnson FH, Haneda Y.
  TITLE     Properties and reaction mechanism of the bioluminescence system of
            the deep-sea shrimp Oplophorus gracilorostris.
  JOURNAL   Biochemistry. 17 (1978) 994-8.
  ORGANISM  Oplophorus gracilorostris
REFERENCE   2  [PMID:10984608]
  AUTHORS   Inouye S, Watanabe K, Nakamura H, Shimomura O.
  TITLE     Secretional luciferase of the luminous shrimp Oplophorus
            gracilirostris: cDNA cloning of a novel imidazopyrazinone
            luciferase(1).
  JOURNAL   FEBS. Lett. 481 (2000) 19-25.
  ORGANISM  Oplophorus gracilorostris
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.12.13
            ExPASy - ENZYME nomenclature database: 1.13.12.13
            ExplorEnz - The Enzyme Database: 1.13.12.13
            ERGO genome analysis and discovery system: 1.13.12.13
            BRENDA, the Enzyme Database: 1.13.12.13
///
ENTRY       EC 1.13.12.14               Enzyme
NAME        chlorophyllide-a oxygenase;
            chlorophyllide a oxygenase;
            cholorophyll-b synthase;
            CAO
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            With incorporation of one atom of oxygen (internal monooxygenases or
            internal mixed-function oxidases)
SYSNAME     chlorophyllide-a:oxygen 7-oxidoreductase
REACTION    (1) chlorophyllide a + O2 + NADPH + H+ = 7-hydroxychlorophyllide a +
            H2O + NADP+;
            (2) 7-hydroxychlorophyllide a + O2 + NADPH + H+ = chlorophyllide b +
            2 H2O + NADP+
SUBSTRATE   chlorophyllide a [CPD:C02139];
            O2 [CPD:C00007];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            7-hydroxychlorophyllide a
PRODUCT     7-hydroxychlorophyllide a;
            H2O [CPD:C00001];
            NADP+ [CPD:C00006];
            chlorophyllide b
COMMENT     Chlorophyll b is required for the assembly of stable
            light-harvesting complexes (LHCs) in the chloroplast of green algae,
            cyanobacteria and plants [2,3]. Contains a mononuclear iron centre
            [3]. The enzyme catalyses two successive hydroxylations at the
            7-methyl group of chlorophyllide a. The second step yields the
            aldehyde hydrate, which loses H2O spontaneously to form
            chlorophyllide b [2]. Chlorophyll a and protochlorophyllide a are
            not substrates [2].
REFERENCE   1  [PMID:10468639]
  AUTHORS   Espineda CE, Linford AS, Devine D, Brusslan JA.
  TITLE     The AtCAO gene, encoding chlorophyll a oxygenase, is required for
            chlorophyll b synthesis in Arabidopsis thaliana.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 10507-11.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   2  [PMID:10758481]
  AUTHORS   Oster U, Tanaka R, Tanaka A, Rudiger W.
  TITLE     Cloning and functional expression of the gene encoding the key
            enzyme for chlorophyll b biosynthesis (CAO) from Arabidopsis
            thaliana.
  JOURNAL   Plant. J. 21 (2000) 305-10.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   3  [PMID:15086960]
  AUTHORS   Eggink LL, LoBrutto R, Brune DC, Brusslan J, Yamasato A, Tanaka A,
            Hoober JK.
  TITLE     Synthesis of chlorophyll b: localization of chlorophyllide a
            oxygenase and discovery of a stable radical in the catalytic
            subunit.
  JOURNAL   BMC. Plant. Biol. 4 (2004) 5.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   4  [PMID:8307032]
  AUTHORS   Porra RJ, Schafer W, Cmiel E, Katheder I, Scheer H.
  TITLE     The derivation of the formyl-group oxygen of chlorophyll b in higher
            plants from molecular oxygen. Achievement of high enrichment of the
            7-formyl-group oxygen from 18O2 in greening maize leaves.
  JOURNAL   Eur. J. Biochem. 219 (1994) 671-9.
  ORGANISM  Zea mays [GN:ezma]
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.12.14
            ExPASy - ENZYME nomenclature database: 1.13.12.14
            ExplorEnz - The Enzyme Database: 1.13.12.14
            ERGO genome analysis and discovery system: 1.13.12.14
            BRENDA, the Enzyme Database: 1.13.12.14
///
ENTRY       EC 1.13.12.-                Enzyme
CLASS       Oxidoreductases;
            Acting on single donors with incorporation of molecular oxygen
            (oxygenases);
            With incorporation of one atom of oxygen (internal monooxygenases or
            internal mixed function oxidases)
REACTION    (1) NH3 + Oxygen <=> Hydroxylamine + H2O [RN:R00148];
            (2) Homogentisate + Oxygen <=> Gentisate aldehyde + CO2 + H2O
            [RN:R02520];
            (3) Caffeine + NADPH + Oxygen + H+ <=> 1,7-Dimethylxanthine + NADP+
            + Formaldehyde + H2O [RN:R07939];
            (4) Caffeine + NADH + H+ + Oxygen <=> 1,7-Dimethylxanthine + NAD+ +
            Formaldehyde + H2O [RN:R07954];
            (5) Caffeine + NADH + H+ + Oxygen <=> Theobromine + NAD+ +
            Formaldehyde + H2O [RN:R07955];
            (6) Caffeine + NADPH + H+ + Oxygen <=> Theobromine + NADP+ +
            Formaldehyde + H2O [RN:R07956];
            (7) 1,7-Dimethylxanthine + NADH + H+ + Oxygen <=> 7-Methylxanthine +
            NAD+ + Formaldehyde + H2O [RN:R07957];
            (8) 1,7-Dimethylxanthine + NADPH + H+ + Oxygen <=> 7-Methylxanthine
            + NADP+ + Formaldehyde + H2O [RN:R07958];
            (9) 1,7-Dimethylxanthine + NADH + H+ + Oxygen <=> 1-Methylxanthine +
            NAD+ + Formaldehyde + H2O [RN:R07959];
            (10) 1,7-Dimethylxanthine + NADPH + H+ + Oxygen <=> 1-Methylxanthine
            + NADP+ + Formaldehyde + H2O [RN:R07960];
            (11) Theobromine + NADH + H+ + Oxygen <=> 7-Methylxanthine + NAD+ +
            Formaldehyde + H2O [RN:R07961];
            (12) Theobromine + NADPH + H+ + Oxygen <=> 7-Methylxanthine + NADP+
            + Formaldehyde + H2O [RN:R07962];
            (13) Theobromine + NADH + H+ + Oxygen <=> 3-Methylxanthine + NAD+ +
            Formaldehyde + H2O [RN:R07963];
            (14) Theobromine + NADPH + H+ + Oxygen <=> 3-Methylxanthine + NADP+
            + Formaldehyde + H2O [RN:R07964];
            (15) 7-Methylxanthine + NADH + H+ + Oxygen <=> Xanthine + NAD+ +
            Formaldehyde + H2O [RN:R07965];
            (16) 7-Methylxanthine + NADPH + H+ + Oxygen <=> Xanthine + NADP+ +
            Formaldehyde + H2O [RN:R07966];
            (17) 3-Methylxanthine + NADH + H+ + Oxygen <=> Xanthine + NAD+ +
            Formaldehyde + H2O [RN:R07967];
            (18) 3-Methylxanthine + NADPH + H+ + Oxygen <=> Xanthine + NADP+ +
            Formaldehyde + H2O [RN:R07968];
            (19) 1-Methylxanthine + NADH + H+ + Oxygen <=> Xanthine + NAD+ +
            Formaldehyde + H2O [RN:R07969];
            (20) 1-Methylxanthine + NADPH + H+ + Oxygen <=> Xanthine + NADP+ +
            Formaldehyde + H2O [RN:R07970];
            (21) Caffeine + NADH + H+ + Oxygen <=> Theophylline + NAD+ +
            Formaldehyde + H2O [RN:R07971];
            (22) Caffeine + NADPH + H+ + Oxygen <=> Theophylline + NADP+ +
            Formaldehyde + H2O [RN:R07972];
            (23) Theophylline + NADH + H+ + Oxygen <=> 3-Methylxanthine + NAD+ +
            Formaldehyde + H2O [RN:R07973];
            (24) Theophylline + NADPH + H+ + Oxygen <=> 3-Methylxanthine + NADP+
            + Formaldehyde + H2O [RN:R07974];
            (25) Theophylline + NADH + H+ + Oxygen <=> 1-Methylxanthine + NAD+ +
            Formaldehyde + H2O [RN:R07975];
            (26) Theophylline + NADPH + H+ + Oxygen <=> 1-Methylxanthine + NADP+
            + Formaldehyde + H2O [RN:R07976]
SUBSTRATE   NH3 [CPD:C00014];
            Oxygen [CPD:C00007];
            Homogentisate [CPD:C00544]
PRODUCT     Hydroxylamine [CPD:C00192];
            H2O [CPD:C00001];
            Gentisate aldehyde [CPD:C05585];
            CO2 [CPD:C00011]
///
ENTRY       EC 1.13.99.1                Enzyme
NAME        inositol oxygenase;
            meso-inositol oxygenase;
            myo-inositol oxygenase;
            MOO
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            Miscellaneous
SYSNAME     myo-inositol:oxygen oxidoreductase
REACTION    myo-inositol + O2 = D-glucuronate + H2O [RN:R01184]
ALL_REAC    R01184
SUBSTRATE   myo-inositol [CPD:C00137];
            O2 [CPD:C00007]
PRODUCT     D-glucuronate [CPD:C00191];
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023]
COMMENT     An iron protein.
REFERENCE   1  [PMID:13630882]
  AUTHORS   CHARALAMPOUS FC.
  TITLE     Biochemical studies on inositol. V. Purification and properties of
            the enzyme that cleaves inositol to D-glucuronic acid.
  JOURNAL   J. Biol. Chem. 234 (1959) 220-7.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:7263666]
  AUTHORS   Reddy CC, Swan JS, Hamilton GA.
  TITLE     myo-Inositol oxygenase from hog kidney. I. Purification and
            characterization of the oxygenase and of an enzyme complex
            containing the oxygenase and D-glucuronate reductase.
  JOURNAL   J. Biol. Chem. 256 (1981) 8510-8.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:11716759]
  AUTHORS   Arner RJ, Prabhu KS, Thompson JT, Hildenbrandt GR, Liken AD, Reddy
            CC.
  TITLE     myo-Inositol oxygenase: molecular cloning and expression of a unique
            enzyme that oxidizes myo-inositol and D-chiro-inositol.
  JOURNAL   Biochem. J. 360 (2001) 313-20.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
            PATH: map00562  Inositol phosphate metabolism
ORTHOLOGY   KO: K00469  inositol oxygenase
GENES       HSA: 55586(MIOX)
            MMU: 56727(Miox)
            RNO: 252899(Miox)
            CFA: 481189(MIOX)
            SSC: 397189(MIOX)
            DRE: 571850(zgc:114168)
            SPU: 593425(LOC593425)
            ATH: AT1G14520(MIOX1) AT2G19800(MIOX2) AT4G26260(MIOX4)
                 AT5G56640(MIOX5)
            OSA: 4341305
            CNE: CNG03010 CNH03170
            DDI: DDBDRAFT_0188751
            SUS: Acid_4072
            FJO: Fjoh_3119
STRUCTURES  PDB: 2HUO  2IBN  
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.99.1
            ExPASy - ENZYME nomenclature database: 1.13.99.1
            ExplorEnz - The Enzyme Database: 1.13.99.1
            ERGO genome analysis and discovery system: 1.13.99.1
            BRENDA, the Enzyme Database: 1.13.99.1
            CAS: 9029-59-8
///
ENTRY       EC 1.13.99.2      Obsolete  Enzyme
NAME        Transferred to 1.14.12.10
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            Miscellaneous
COMMENT     Transferred entry: now EC 1.14.12.10 benzoate 1,2-dioxygenase (EC
            1.13.99.2 created 1972, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.99.2
            ExPASy - ENZYME nomenclature database: 1.13.99.2
            ExplorEnz - The Enzyme Database: 1.13.99.2
            ERGO genome analysis and discovery system: 1.13.99.2
            BRENDA, the Enzyme Database: 1.13.99.2
///
ENTRY       EC 1.13.99.3                Enzyme
NAME        tryptophan 2'-dioxygenase;
            indole-3-alkane alpha-hydroxylase;
            tryptophan side-chain alpha,beta-oxidase;
            tryptophan side chain oxidase II;
            tryptophan side-chain oxidase;
            TSO;
            indolyl-3-alkan alpha-hydroxylase;
            tryptophan side chain oxidase type I;
            TSO I ;
            TSO II;
            tryptophan side chain oxidase
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            Miscellaneous
SYSNAME     L-tryptophan:oxygen 2'-oxidoreductase (side-chain-cleaving)
REACTION    L-tryptophan + O2 = (indol-3-yl)glycolaldehyde + CO2 + NH3
            [RN:R00681]
ALL_REAC    R00681
SUBSTRATE   L-tryptophan [CPD:C00078];
            O2 [CPD:C00007]
PRODUCT     (indol-3-yl)glycolaldehyde;
            CO2 [CPD:C00011];
            NH3 [CPD:C00014]
COFACTOR    Heme [CPD:C00032]
COMMENT     A hemoprotein. Acts on a number of indole-3-alkane derivatives,
            oxidizing the 3-side-chain in the 2'-position. Best substrates were
            L-tryptophan and 5-hydroxy-L-tryptophan.
REFERENCE   1  [PMID:15994]
  AUTHORS   Roberts J, Rosenfeld HJ.
  TITLE     Isolation, crystallization, and properties of indolyl-3-alkane
            alpha-hydroxylase. A novel tryptophan-metabolizing enzyme.
  JOURNAL   J. Biol. Chem. 252 (1977) 2640-7.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:15995]
  AUTHORS   Takai K, Ushiro H, Noda Y, Narumiya S, Tokuyama T.
  TITLE     Crystalline hemoprotein from Pseudomonas that catalyzes oxidation of
            side chain of tryptophan and other indole derivatives.
  JOURNAL   J. Biol. Chem. 252 (1977) 2648-56.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00380  Tryptophan metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.99.3
            ExPASy - ENZYME nomenclature database: 1.13.99.3
            ExplorEnz - The Enzyme Database: 1.13.99.3
            ERGO genome analysis and discovery system: 1.13.99.3
            BRENDA, the Enzyme Database: 1.13.99.3
            CAS: 64295-81-4
///
ENTRY       EC 1.13.99.4      Obsolete  Enzyme
NAME        Transferred to 1.14.12.9
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            Miscellaneous
COMMENT     Transferred entry: now EC 1.14.12.9 4-chlorophenylacetate
            3,4-dioxygenase (EC 1.13.99.4 created 1989, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.99.4
            ExPASy - ENZYME nomenclature database: 1.13.99.4
            ExplorEnz - The Enzyme Database: 1.13.99.4
            ERGO genome analysis and discovery system: 1.13.99.4
            BRENDA, the Enzyme Database: 1.13.99.4
///
ENTRY       EC 1.13.99.5      Obsolete  Enzyme
NAME        Transferred to 1.13.11.47
CLASS       Oxidoreductases;
            Acting on single donors with O2 as oxidant and incorporation of
            oxygen into the substrate (oxygenases). The oxygen incorporated need
            not be derived from O2;
            Miscellaneous
COMMENT     Transferred entry: now EC 1.13.11.47, 3-hydroxy-4-oxoquinoline
            2,4-dioxygenase (EC 1.13.99.5 created 1999, deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 1.13.99.5
            ExPASy - ENZYME nomenclature database: 1.13.99.5
            ExplorEnz - The Enzyme Database: 1.13.99.5
            ERGO genome analysis and discovery system: 1.13.99.5
            BRENDA, the Enzyme Database: 1.13.99.5
///
ENTRY       EC 1.13.99.-                Enzyme
CLASS       Oxidoreductases;
            Acting on single donors with incorporation of molecular oxygen
            (oxygenases);
            Miscellaneous
REACTION    (1) Oxygen + H2O + 2 Sulfur <=> Hydrogen sulfide + Sulfite
            [RN:R00121];
            (2) 2 2,4,5-Trichlorophenoxyacetic acid + Oxygen <=> 2
            2,4,5-Trichlorophenol + 2 Glyoxylate [RN:R05418]
SUBSTRATE   Oxygen [CPD:C00007];
            H2O [CPD:C00001];
            Sulfur [CPD:C00087];
            2,4,5-Trichlorophenoxyacetic acid [CPD:C07100]
PRODUCT     Hydrogen sulfide [CPD:C00283];
            Sulfite [CPD:C00094];
            2,4,5-Trichlorophenol [CPD:C07101];
            Glyoxylate [CPD:C00048]
///
ENTRY       EC 1.13.-.-                 Enzyme
CLASS       Oxidoreductases;
            Acting on single donors with incorporation of molecular oxygen
            (oxygenases)
REACTION    (1) 4,4'-Dihydroxy-alpha-methylstilbene + Oxygen <=>
            4-Hydroxybenzaldehyde + 4'-Hydroxyacetophenone [RN:R06886];
            (2) 2,3-Bis(4-hydroxyphenyl)-1,2-propanediol + Oxygen <=>
            4-Hydroxyphenacyl alcohol + 4-Hydroxybenzoate [RN:R06889];
            (3) 1,2-Dihydroxy-8-methylnaphthalene + Oxygen <=>
            2-Hydroxy-8-methylchromene-2-carboxylate [RN:R06911];
            (4) 1,2-Dihydroxy-8-carboxynaphthalene + Oxygen <=>
            2-Carboxy-2-hydroxy-8-carboxychromene [RN:R06921];
            (5) 1,2-Dihydroxy-7-hydroxymethylnaphthalene + Oxygen <=>
            2-Hydroxy-7-hydroxymethylchromene-2-carboxylate [RN:R06932];
            (6) 2,3-Dihydroxy-2'-carboxybiphenyl + Oxygen <=>
            2-Hydroxy-6-oxo-6-(2-carboxyphenyl)-hexa-2,4-dienoate [RN:R07801]
SUBSTRATE   4,4'-Dihydroxy-alpha-methylstilbene [CPD:C13632];
            Oxygen [CPD:C00007];
            2,3-Bis(4-hydroxyphenyl)-1,2-propanediol [CPD:C13634];
            1,2-Dihydroxy-8-methylnaphthalene [CPD:C14084];
            1,2-Dihydroxy-8-carboxynaphthalene [CPD:C14093];
            1,2-Dihydroxy-7-hydroxymethylnaphthalene [CPD:C14105]
PRODUCT     4-Hydroxybenzaldehyde [CPD:C00633];
            4'-Hydroxyacetophenone [CPD:C10700];
            4-Hydroxyphenacyl alcohol [CPD:C13635];
            4-Hydroxybenzoate [CPD:C00156];
            2-Hydroxy-8-methylchromene-2-carboxylate [CPD:C14085];
            2-Carboxy-2-hydroxy-8-carboxychromene [CPD:C14094];
            2-Hydroxy-7-hydroxymethylchromene-2-carboxylate [CPD:C14106]
///
ENTRY       EC 1.14.1.1       Obsolete  Enzyme
NAME        Transferred to 1.14.14.1
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.14.14.1, unspecific monooxygenase (EC
            1.14.1.1 created 1961 as EC 1.99.1.1, transferred 1965 to EC
            1.14.14.1, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.1.1
            ExPASy - ENZYME nomenclature database: 1.14.1.1
            ExplorEnz - The Enzyme Database: 1.14.1.1
            ERGO genome analysis and discovery system: 1.14.1.1
            BRENDA, the Enzyme Database: 1.14.1.1
///
ENTRY       EC 1.14.1.2       Obsolete  Enzyme
NAME        Transferred to 1.14.13.9
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.14.13.9, kynurenine 3-monooxygenase (EC
            1.14.1.2 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.1.2
            ExPASy - ENZYME nomenclature database: 1.14.1.2
            ExplorEnz - The Enzyme Database: 1.14.1.2
            ERGO genome analysis and discovery system: 1.14.1.2
            BRENDA, the Enzyme Database: 1.14.1.2
///
ENTRY       EC 1.14.1.3       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor (deleted sub-subclass)
COMMENT     Deleted entry: squalene hydroxylase. Activity is covered by EC
            1.14.99.7, squalene monooxygenase and EC 5.4.99.7, lanosterol
            synthase (EC 1.14.1.3 created 1961 as EC 1.99.1.13, transferred 1965
            to EC 1.14.1.3, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.1.3
            ExPASy - ENZYME nomenclature database: 1.14.1.3
            ExplorEnz - The Enzyme Database: 1.14.1.3
            ERGO genome analysis and discovery system: 1.14.1.3
            BRENDA, the Enzyme Database: 1.14.1.3
///
ENTRY       EC 1.14.1.4       Obsolete  Enzyme
NAME        Transferred to 1.14.99.2
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.14.99.2, kynurenine 7,8-hydroxylase (EC
            1.14.1.4 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.1.4
            ExPASy - ENZYME nomenclature database: 1.14.1.4
            ExplorEnz - The Enzyme Database: 1.14.1.4
            ERGO genome analysis and discovery system: 1.14.1.4
            BRENDA, the Enzyme Database: 1.14.1.4
///
ENTRY       EC 1.14.1.5       Obsolete  Enzyme
NAME        Transferred to 1.14.13.5
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.14.13.5, imidazoleacetate
            4-monooxygenase (EC 1.14.1.5 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.1.5
            ExPASy - ENZYME nomenclature database: 1.14.1.5
            ExplorEnz - The Enzyme Database: 1.14.1.5
            ERGO genome analysis and discovery system: 1.14.1.5
            BRENDA, the Enzyme Database: 1.14.1.5
///
ENTRY       EC 1.14.1.6       Obsolete  Enzyme
NAME        Transferred to 1.14.15.4
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.14.15.4, steroid 11beta-monooxygenase
            (EC 1.14.1.6 created 1961 as EC 1.99.1.7, transferred 1965 to EC
            1.14.1.6, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.1.6
            ExPASy - ENZYME nomenclature database: 1.14.1.6
            ExplorEnz - The Enzyme Database: 1.14.1.6
            ERGO genome analysis and discovery system: 1.14.1.6
            BRENDA, the Enzyme Database: 1.14.1.6
///
ENTRY       EC 1.14.1.7       Obsolete  Enzyme
NAME        Transferred to 1.14.99.9
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.14.99.9, steroid 17alpha-monooxygenase
            (EC 1.14.1.7 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.1.7
            ExPASy - ENZYME nomenclature database: 1.14.1.7
            ExplorEnz - The Enzyme Database: 1.14.1.7
            ERGO genome analysis and discovery system: 1.14.1.7
            BRENDA, the Enzyme Database: 1.14.1.7
///
ENTRY       EC 1.14.1.8       Obsolete  Enzyme
NAME        Transferred to 1.14.99.10
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.14.99.10, steroid 21-monooxygenase (EC
            1.14.1.8 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.1.8
            ExPASy - ENZYME nomenclature database: 1.14.1.8
            ExplorEnz - The Enzyme Database: 1.14.1.8
            ERGO genome analysis and discovery system: 1.14.1.8
            BRENDA, the Enzyme Database: 1.14.1.8
///
ENTRY       EC 1.14.1.9       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor (deleted sub-subclass)
COMMENT     Deleted entry: cholesterol 20-hydroxylase (EC 1.14.1.9 created 1965,
            deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.1.9
            ExPASy - ENZYME nomenclature database: 1.14.1.9
            ExplorEnz - The Enzyme Database: 1.14.1.9
            ERGO genome analysis and discovery system: 1.14.1.9
            BRENDA, the Enzyme Database: 1.14.1.9
///
ENTRY       EC 1.14.1.10      Obsolete  Enzyme
NAME        Transferred to 1.14.99.11
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.14.99.11, estradiol 6beta-monooxygenase
            (EC 1.14.1.10 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.1.10
            ExPASy - ENZYME nomenclature database: 1.14.1.10
            ExplorEnz - The Enzyme Database: 1.14.1.10
            ERGO genome analysis and discovery system: 1.14.1.10
            BRENDA, the Enzyme Database: 1.14.1.10
///
ENTRY       EC 1.14.1.11      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor (deleted sub-subclass)
COMMENT     Deleted entry: oestriol 2-hydroxylase (EC 1.14.1.11 created 1965,
            deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.1.11
            ExPASy - ENZYME nomenclature database: 1.14.1.11
            ExplorEnz - The Enzyme Database: 1.14.1.11
            ERGO genome analysis and discovery system: 1.14.1.11
            BRENDA, the Enzyme Database: 1.14.1.11
///
ENTRY       EC 1.14.2.1       Obsolete  Enzyme
NAME        Transferred to 1.14.17.1
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With ascorbate as one donor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.14.17.1, dopamine beta-monooxygenase (EC
            1.14.2.1 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.2.1
            ExPASy - ENZYME nomenclature database: 1.14.2.1
            ExplorEnz - The Enzyme Database: 1.14.2.1
            ERGO genome analysis and discovery system: 1.14.2.1
            BRENDA, the Enzyme Database: 1.14.2.1
///
ENTRY       EC 1.14.2.2       Obsolete  Enzyme
NAME        Transferred to 1.13.11.27
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With ascorbate as one donor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.13.11.27, 4-hydroxyphenylpyruvate
            dioxygenase (EC 1.14.2.2 created 1961 as EC 1.99.1.14, transferred
            1965 to EC 1.14.2.2, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.2.2
            ExPASy - ENZYME nomenclature database: 1.14.2.2
            ExplorEnz - The Enzyme Database: 1.14.2.2
            ERGO genome analysis and discovery system: 1.14.2.2
            BRENDA, the Enzyme Database: 1.14.2.2
///
ENTRY       EC 1.14.3.1       Obsolete  Enzyme
NAME        Transferred to 1.14.16.1
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced pteridine as one donor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.14.16.1, phenylalanine 4-monooxygenase
            (EC 1.14.3.1 created 1961 as EC 1.99.1.2, transferred 1965 to EC
            1.14.3.1, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.3.1
            ExPASy - ENZYME nomenclature database: 1.14.3.1
            ExplorEnz - The Enzyme Database: 1.14.3.1
            ERGO genome analysis and discovery system: 1.14.3.1
            BRENDA, the Enzyme Database: 1.14.3.1
///
ENTRY       EC 1.14.11.1                Enzyme
NAME        gamma-butyrobetaine dioxygenase;
            alpha-butyrobetaine hydroxylase;
            gamma-butyrobetaine hydroxylase;
            butyrobetaine hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     4-trimethylammoniobutanoate,2-oxoglutarate:oxygen oxidoreductase
            (3-hydroxylating)
REACTION    4-trimethylammoniobutanoate + 2-oxoglutarate + O2 =
            3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2 [RN:R02397]
ALL_REAC    R02397;
            (other) R02399
SUBSTRATE   4-trimethylammoniobutanoate [CPD:C01181];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     3-hydroxy-4-trimethylammoniobutanoate [CPD:C00487];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COFACTOR    Iron [CPD:C00023];
            Ascorbate [CPD:C00072]
COMMENT     Requires Fe2+ and ascorbate.
REFERENCE   1  [PMID:4396068]
  AUTHORS   Lindstedt G, Lindstedt S.
  TITLE     Cofactor requirements of gamma-butyrobetaine hydroxylase from rat
            liver.
  JOURNAL   J. Biol. Chem. 245 (1970) 4178-86.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K00471  gamma-butyrobetaine dioxygenase
GENES       HSA: 8424(BBOX1)
            PTR: 466474(BBOX1)
            MMU: 170442(Bbox1)
            RNO: 64564(Bbox1)
            CFA: 476894(BBOX1)
            GGA: 426932(BBOX1)
            DME: Dmel_CG4335 Dmel_CG5321
            CEL: D2089.5(gbh-1) M05D6.7(gbh-2)
            PIC: PICST_33061(GBO1)
            PFL: PFL_5756
            PFO: Pfl_5234
            PMY: Pmen_0503
            SPL: Spea_2204
            CSA: Csal_0540 Csal_2770
            BVI: Bcep1808_3389
            BUR: Bcep18194_B0616
            BCN: Bcen_3320
            BCH: Bcen2424_5047
            BAM: Bamb_4455
            BPS: BPSS1110
            BPM: BURPS1710b_A0070 BURPS1710b_A1680(pvcB)
            BPL: BURPS1106A_A1481
            BPD: BURPS668_A1569
            MLO: mll1440
            SIL: SPO3380
            SIT: TM1040_0052 TM1040_0333 TM1040_2006
            TER: Tery_0693
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.1
            ExPASy - ENZYME nomenclature database: 1.14.11.1
            ExplorEnz - The Enzyme Database: 1.14.11.1
            ERGO genome analysis and discovery system: 1.14.11.1
            BRENDA, the Enzyme Database: 1.14.11.1
            CAS: 9045-31-2
///
ENTRY       EC 1.14.11.2                Enzyme
NAME        procollagen-proline dioxygenase;
            protocollagen hydroxylase;
            proline hydroxylase;
            proline,2-oxoglutarate 4-dioxygenase;
            collagen proline hydroxylase;
            hydroxylase, collagen proline;
            peptidyl proline hydroxylase;
            proline protocollagen hydroxylase;
            proline, 2-oxoglutarate dioxygenase;
            prolyl hydroxylase;
            prolylprotocollagen dioxygenase;
            prolylprotocollagen hydroxylase;
            protocollagen proline 4-hydroxylase;
            protocollagen proline dioxygenase;
            protocollagen proline hydroxylase;
            protocollagen prolyl hydroxylase;
            prolyl 4-hydroxylase;
            prolyl-glycyl-peptide, 2-oxoglutarate:oxygen oxidoreductase,
            4-hydroxylating;
            procollagen-proline 4-dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     procollagen-L-proline,2-oxoglutarate:oxygen oxidoreductase
            (4-hydroxylating)
REACTION    procollagen L-proline + 2-oxoglutarate + O2 = procollagen
            trans-4-hydroxy-L-proline + succinate + CO2 [RN:R03219]
ALL_REAC    R03219;
            (other) R01252
SUBSTRATE   procollagen L-proline [CPD:C01078];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     procollagen trans-4-hydroxy-L-proline [CPD:C04398];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COFACTOR    Iron [CPD:C00023];
            Ascorbate [CPD:C00072]
COMMENT     Requires Fe2+ and ascorbate.
REFERENCE   1  [PMID:4346946]
  AUTHORS   Berg RA, Prockop DJ.
  TITLE     Affinity column purification of protocollagen proline hydroxylase
            from chick embryos and further characterization of the enzyme.
  JOURNAL   J. Biol. Chem. 248 (1973) 1175-82.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Hutton, J.J., Jr., Tappel, A.L. and Udenfriend, S.
  TITLE     Cofactor and substrate requirements of collagen proline hydroxylase.
  JOURNAL   Arch. Biochem. Biophys. 118 (1967) 231-240.
  ORGANISM  rat [GN:rno], gunea pig
REFERENCE   3  [PMID:5046811]
  AUTHORS   Kivirikko KI, Kishida Y, Sakakibara S, Prockop DJ.
  TITLE     Hydroxylation of (X-Pro-Gly)n by protocollagen proline hydroxylase.
            Effect of chain length, helical conformation and amino acid sequence
            in the substrate.
  JOURNAL   Biochim. Biophys. Acta. 271 (1972) 347-56.
  ORGANISM  rat [GN:rno], chicken [GN:gga]
REFERENCE   4
  AUTHORS   Kivirikko, K.I. and Prockop, D.J.
  TITLE     Purification and partial characterization of the enzyme for the
            hydroxylation of proline in protocollogen.
  JOURNAL   Arch. Biochem. Biophys. 118 (1967) 611-618.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K00472  prolyl 4-hydroxylase
GENES       HSA: 283208(P4HA3) 5033(P4HA1) 8974(P4HA2)
            PTR: 450891(P4HA1)
            MMU: 18451(P4ha1) 18452(P4ha2) 320452(P4ha3)
            RNO: 361612(P4ha3) 64475(P4ha1)
            CFA: 474672(P4HA2) 479242(P4HA1)
            BTA: 414348(P4HA3)
            GGA: 416326(P4HA2) 423704(P4HA1)
            XLA: 447527(MGC83530)
            XTR: 493342(p4ha2)
            SPU: 592929(LOC592929)
            DME: Dmel_CG1546(PH4alphaSG2) Dmel_CG31014(PH4alphaSG1)
                 Dmel_CG31015(PH4alphaPV) Dmel_CG31017(PH4alphaNE3)
                 Dmel_CG31022(PH4alphaEFB) Dmel_CG9720(PH4alphaNE2)
                 Dmel_CG9726(PH4alphaMP) Dmel_CG9728(PH4alphaNE1)
            CEL: F35G2.4(phy-2) Y47D3B.10(dpy-18)
            ATH: AT3G28480
            ANI: AN2851.2
            AOR: AO090003000761
            DDI: DDBDRAFT_0202598
            TAN: TA04445
            PRW: PsycPRwf_1859
            REU: Reut_A2950
            REH: H16_A3244(phy)
            RME: Rmet_3098
            BXE: Bxe_B1199
            POL: Bpro_3712
            AZO: azo0608(ybiX)
            BRA: BRADO6316
            BBT: BBta_1313
            BAN: BA4459
            BAR: GBAA4459
            BAA: BA_4910
            BAT: BAS4138
            BCE: BC4233
            BCA: BCE_4314
            BCZ: BCZK3988
            BTK: BT9727_3978
            BTL: BALH_3835
STRUCTURES  PDB: 1TJC  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.2
            ExPASy - ENZYME nomenclature database: 1.14.11.2
            ExplorEnz - The Enzyme Database: 1.14.11.2
            ERGO genome analysis and discovery system: 1.14.11.2
            BRENDA, the Enzyme Database: 1.14.11.2
            CAS: 9028-06-2
///
ENTRY       EC 1.14.11.3                Enzyme
NAME        pyrimidine-deoxynucleoside 2'-dioxygenase;
            deoxyuridine 2'-dioxygenase;
            deoxyuridine 2'-hydroxylase;
            pyrimidine deoxyribonucleoside 2'-hydroxylase;
            thymidine 2'-dioxygenase;
            thymidine 2'-hydroxylase;
            thymidine 2-oxoglutarate dioxygenase;
            thymidine dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     2'-deoxyuridine,2-oxoglutarate:oxygen oxidoreductase
            (2'-hydroxylating)
REACTION    2'-deoxyuridine + 2-oxoglutarate + O2 = uridine + succinate + CO2
            [RN:R01879]
ALL_REAC    R01879
SUBSTRATE   2'-deoxyuridine [CPD:C00526];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     uridine [CPD:C00299];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COFACTOR    Iron [CPD:C00023];
            Ascorbate [CPD:C00072]
COMMENT     Requires Fe(II) and ascorbate. Also acts on thymidine. cf. EC
            1.14.11.10, pyrimidine-deoxynucleoside 1'-dioxygenase.
REFERENCE   1  [PMID:4265566]
  AUTHORS   Bankel L, Lindstedt G, Lindstedt S.
  TITLE     Thymidine 2'-hydroxylation in Neurospora crassa.
  JOURNAL   J. Biol. Chem. 247 (1972) 6128-34.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2  [PMID:4040518]
  AUTHORS   Stubbe J.
  TITLE     Identification of two alpha-ketoglutarate-dependent dioxygenases in
            extracts of Rhodotorula glutinis catalyzing deoxyuridine
            hydroxylation.
  JOURNAL   J. Biol. Chem. 260 (1985) 9972-5.
  ORGANISM  Rhodotorula glutinis
REFERENCE   3  [PMID:6684117]
  AUTHORS   Warn-Cramer BJ, Macrander LA, Abbott MT.
  TITLE     Markedly different ascorbate dependencies of the sequential
            alpha-ketoglutarate dioxygenase reactions catalyzed by an
            essentially homogeneous thymine 7-hydroxylase from Rhodotorula
            glutinis.
  JOURNAL   J. Biol. Chem. 258 (1983) 10551-7.
  ORGANISM  Rhodotorula glutinis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.3
            ExPASy - ENZYME nomenclature database: 1.14.11.3
            ExplorEnz - The Enzyme Database: 1.14.11.3
            ERGO genome analysis and discovery system: 1.14.11.3
            BRENDA, the Enzyme Database: 1.14.11.3
            CAS: 9076-89-5
///
ENTRY       EC 1.14.11.4                Enzyme
NAME        procollagen-lysine 5-dioxygenase;
            lysine hydroxylase;
            lysine,2-oxoglutarate 5-dioxygenase;
            protocollagen lysine dioxygenase;
            collagen lysine hydroxylase;
            lysine-2-oxoglutarate dioxygenase;
            lysyl hydroxylase;
            lysylprotocollagen dioxygenase;
            protocollagen lysyl hydroxylase;
            peptidyl-lysine, 2-oxoglutarate: oxygen oxidoreductase;
            peptidyllysine, 2-oxoglutarate:oxygen 5-oxidoreductase;
            protocollagen lysine hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     procollagen-L-lysine,2-oxoglutarate:oxygen oxidoreductase
            (5-hydroxylating)
REACTION    procollagen L-lysine + 2-oxoglutarate + O2 = procollagen
            5-hydroxy-L-lysine + succinate + CO2
ALL_REAC    (other) R03376
SUBSTRATE   procollagen L-lysine [CPD:C02188];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     procollagen 5-hydroxy-L-lysine [CPD:C01211];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COFACTOR    Iron [CPD:C00023];
            Ascorbate [CPD:C00072]
COMMENT     Requires Fe2+ and ascorbate.
REFERENCE   1  [PMID:6033801]
  AUTHORS   Hausmann E.
  TITLE     Cofactor requirements for the enzymatic hydroxylation of lysine in a
            polypeptide precursor of collagen.
  JOURNAL   Biochim. Biophys. Acta. 133 (1967) 591-3.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:5244754]
  AUTHORS   Rhoads RE, Udenfriend S.
  TITLE     Decarboxylation of alpha-ketoglutarate coupled to collagen proline
            hydroxylase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 60 (1968) 1473-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K00473  procollagen-lysine,2-oxoglutarate 5-dioxygenase
GENES       HSA: 5351(PLOD1) 5352(PLOD2) 8985(PLOD3)
            PTR: 463618(PLOD3)
            MMU: 18822(Plod1) 26432(Plod2) 26433(Plod3)
            RNO: 116552(Plod1) 288583(Plod3) 300901(Plod2)
            CFA: 479730(PLOD3) 485702(PLOD2) 487440(PLOD1)
            BTA: 281409(PLOD)
            GGA: 419485(PLOD1) 424882(PLOD2)
            XLA: 380138(plod) 495112(LOC495112)
            DRE: 100036767(plod2) 777635(zgc:152876)
            SPU: 576306(LOC576306)
            DME: Dmel_CG6199
            CEL: F52H3.1(let-268)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.4
            ExPASy - ENZYME nomenclature database: 1.14.11.4
            ExplorEnz - The Enzyme Database: 1.14.11.4
            ERGO genome analysis and discovery system: 1.14.11.4
            BRENDA, the Enzyme Database: 1.14.11.4
            CAS: 9059-25-0
///
ENTRY       EC 1.14.11.5      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
COMMENT     Deleted entry: 5-hydroxymethyluracil,2-oxoglutarate dioxygenase. Now
            included with EC 1.14.11.6 thymine dioxygenase (EC 1.14.11.5 created
            1972, deleted 1976)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.5
            ExPASy - ENZYME nomenclature database: 1.14.11.5
            ExplorEnz - The Enzyme Database: 1.14.11.5
            ERGO genome analysis and discovery system: 1.14.11.5
            BRENDA, the Enzyme Database: 1.14.11.5
///
ENTRY       EC 1.14.11.6                Enzyme
NAME        thymine dioxygenase;
            thymine 7-hydroxylase;
            5-hydroxy-methyluracil dioxygenase;
            5-hydroxymethyluracil oxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     thymine,2-oxoglutarate:oxygen oxidoreductase (7-hydroxylating)
REACTION    thymine + 2-oxoglutarate + O2 = 5-hydroxymethyluracil + succinate +
            CO2 [RN:R01412]
ALL_REAC    R01412
SUBSTRATE   thymine [CPD:C00178];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     5-hydroxymethyluracil [CPD:C03088];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COFACTOR    Iron [CPD:C00023];
            Ascorbate [CPD:C00072]
COMMENT     Requires Fe2+ and ascorbate. Also acts on 5-hydroxymethyluracil to
            oxidize its -CH2OH group first to -CHO and then to -COOH.
REFERENCE   1  [PMID:11946494]
  AUTHORS   Bankel L, Holme E, Lindstedt G, Lindstedt S.
  TITLE     Oxygenases involved in thymine and thymidine metabolism in
            Neurospora crassa.
  JOURNAL   FEBS. Lett. 21 (1972) 135-138.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2  [PMID:4274083]
  AUTHORS   Liu CK, Hsu CA, Abbott MT.
  TITLE     Catalysis of three sequential dioxygenase reactions by thymine
            7-hydroxylase.
  JOURNAL   Arch. Biochem. Biophys. 159 (1973) 180-7.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   3  [PMID:6684117]
  AUTHORS   Warn-Cramer BJ, Macrander LA, Abbott MT.
  TITLE     Markedly different ascorbate dependencies of the sequential
            alpha-ketoglutarate dioxygenase reactions catalyzed by an
            essentially homogeneous thymine 7-hydroxylase from Rhodotorula
            glutinis.
  JOURNAL   J. Biol. Chem. 258 (1983) 10551-7.
  ORGANISM  Rhodotorula glutinis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.6
            ExPASy - ENZYME nomenclature database: 1.14.11.6
            ExplorEnz - The Enzyme Database: 1.14.11.6
            ERGO genome analysis and discovery system: 1.14.11.6
            BRENDA, the Enzyme Database: 1.14.11.6
            CAS: 37256-67-0
///
ENTRY       EC 1.14.11.7                Enzyme
NAME        procollagen-proline 3-dioxygenase;
            proline,2-oxoglutarate 3-dioxygenase;
            prolyl 3-hydroxylase;
            protocollagen proline 3-hydroxylase;
            prolyl-4-hydroxyprolyl-glycyl-peptide, 2-oxoglutarate: oxygen
            oxidoreductase, 3-hydroxylating
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     procollagen-L-proline,2-oxoglutarate:oxygen oxidoreductase
            (3-hydroxylating)
REACTION    procollagen L-proline + 2-oxoglutarate + O2 = procollagen
            trans-3-hydroxy-L-proline + succinate + CO2 [RN:R03218]
ALL_REAC    R03218
SUBSTRATE   procollagen L-proline [CPD:C01078];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     procollagen trans-3-hydroxy-L-proline [CPD:C04397];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COFACTOR    Iron [CPD:C00023];
            Ascorbate [CPD:C00072]
COMMENT     Requires Fe2+ and ascorbate.
REFERENCE   1  [PMID:191255]
  AUTHORS   Risteli J, Tryggvason K, Kivirikko KI.
  TITLE     Prolyl 3-hydroxylase: partial characterization of the enzyme from
            rat kidney cortex.
  JOURNAL   Eur. J. Biochem. 73 (1977) 485-92.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:204218]
  AUTHORS   Risteli J, Tryggvason K, Kivirikko KI.
  TITLE     A rapid assay for prolyl 3-hydroxylase activity.
  JOURNAL   Anal. Biochem. 84 (1978) 423-31.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.7
            ExPASy - ENZYME nomenclature database: 1.14.11.7
            ExplorEnz - The Enzyme Database: 1.14.11.7
            ERGO genome analysis and discovery system: 1.14.11.7
            BRENDA, the Enzyme Database: 1.14.11.7
            CAS: 63551-75-7
///
ENTRY       EC 1.14.11.8                Enzyme
NAME        trimethyllysine dioxygenase;
            trimethyllysine alpha-ketoglutarate dioxygenase;
            TML-alpha-ketoglutarate dioxygenase;
            TML hydroxylase;
            6-N,6-N,6-N-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase
            (3-hydroxylating)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     N6,N6,N6-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase
            (3-hydroxylating)
REACTION    N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 =
            3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2 [RN:R03451]
ALL_REAC    R03451
SUBSTRATE   N6,N6,N6-trimethyl-L-lysine [CPD:C03793];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     3-hydroxy-N6,N6,N6-trimethyl-L-lysine [CPD:C01259];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COFACTOR    Iron [CPD:C00023];
            Ascorbate [CPD:C00072];
            Fe2+ [CPD:C14818]
COMMENT     Requires Fe2+ and ascorbate.
REFERENCE   1  [PMID:627563]
  AUTHORS   Hulse JD, Ellis SR, Henderson LM.
  TITLE     Carnitine biosynthesis. beta-Hydroxylation of trimethyllysine by an
            alpha-ketoglutarate-dependent mitochondrial dioxygenase.
  JOURNAL   J. Biol. Chem. 253 (1978) 1654-9.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K00474  trimethyllysine dioxygenase
GENES       HSA: 55217(TMLHE)
            PTR: 465953(TMLHE)
            MMU: 192289(Tmlhe)
            RNO: 170898(Tmlhe)
            CFA: 481090(TMLHE)
            GGA: 422296(TMLHE)
            AGO: AGOS_AEL035W
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.8
            ExPASy - ENZYME nomenclature database: 1.14.11.8
            ExplorEnz - The Enzyme Database: 1.14.11.8
            ERGO genome analysis and discovery system: 1.14.11.8
            BRENDA, the Enzyme Database: 1.14.11.8
            CAS: 74622-49-4
///
ENTRY       EC 1.14.11.9                Enzyme
NAME        flavanone 3-dioxygenase;
            naringenin 3-hydroxylase;
            flavanone 3-hydroxylase;
            flavanone 3beta-hydroxylase;
            flavanone synthase I;
            (2S)-flavanone 3-hydroxylase;
            naringenin,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     flavanone,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
REACTION    a flavanone + 2-oxoglutarate + O2 = a dihydroflavonol + succinate +
            CO2 [RN:R07329]
ALL_REAC    R07329 > R02444 R03640 R05039
SUBSTRATE   flavanone [CPD:C00766];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     dihydroflavonol [CPD:C15570];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COFACTOR    Iron [CPD:C00023];
            Ascorbate [CPD:C00072]
COMMENT     Requires Fe2+ and ascorbate.
REFERENCE   1
  AUTHORS   Forkmann, G., Heller, W. and Grisebach, H.
  TITLE     Anthocyanin biosynthesis in flowers of Matthiola incana flavanone 3-
            and flavonoid 3'-hydroxylases.
  JOURNAL   Z. Naturforsch. C: Biosci. 35 (1980) 691-695.
  ORGANISM  Matthiola incana
REFERENCE   2  [PMID:15013767]
  AUTHORS   Wellmann F, Matern U, Lukacin R.
  TITLE     Significance of C-terminal sequence elements for Petunia flavanone
            3beta-hydroxylase activity.
  JOURNAL   FEBS. Lett. 561 (2004) 149-54.
  ORGANISM  Petunia hybrida, Citrus unshiu
PATHWAY     PATH: map00941  Flavonoid biosynthesis
ORTHOLOGY   KO: K00475  naringenin 3-dioxygenase
GENES       ATH: AT3G51240(F3H)
            OSA: 4337296
            PIC: PICST_32280(NGD3)
            BBT: BBta_2508
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.9
            ExPASy - ENZYME nomenclature database: 1.14.11.9
            ExplorEnz - The Enzyme Database: 1.14.11.9
            ERGO genome analysis and discovery system: 1.14.11.9
            BRENDA, the Enzyme Database: 1.14.11.9
            CAS: 75991-43-4
///
ENTRY       EC 1.14.11.10               Enzyme
NAME        pyrimidine-deoxynucleoside 1'-dioxygenase;
            deoxyuridine-uridine 1'-dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     2'-deoxyuridine,2-oxoglutarate:oxygen oxidoreductase
            (1'-hydroxylating)
REACTION    2'-deoxyuridine + 2-oxoglutarate + O2 = uracil +
            2-deoxyribonolactone + succinate + CO2 [RN:R02486]
ALL_REAC    R02486
SUBSTRATE   2'-deoxyuridine [CPD:C00526];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     uracil [CPD:C00106];
            2-deoxyribonolactone [CPD:C02674];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COFACTOR    Iron [CPD:C00023];
            Ascorbate [CPD:C00072]
COMMENT     Requires Fe(II) and ascorbate. cf. EC 1.14.11.3,
            pyrimidine-deoxynucleoside 2'-dioxygenase.
REFERENCE   1  [PMID:4040518]
  AUTHORS   Stubbe J.
  TITLE     Identification of two alpha-ketoglutarate-dependent dioxygenases in
            extracts of Rhodotorula glutinis catalyzing deoxyuridine
            hydroxylation.
  JOURNAL   J. Biol. Chem. 260 (1985) 9972-5.
  ORGANISM  Rhodotorula glutinis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.10
            ExPASy - ENZYME nomenclature database: 1.14.11.10
            ExplorEnz - The Enzyme Database: 1.14.11.10
            ERGO genome analysis and discovery system: 1.14.11.10
            BRENDA, the Enzyme Database: 1.14.11.10
            CAS: 98865-52-2
///
ENTRY       EC 1.14.11.11               Enzyme
NAME        hyoscyamine (6S)-dioxygenase;
            hyoscyamine 6beta-hydroxylase;
            hyoscyamine 6beta-dioxygenase;
            hyoscyamine 6-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     L-hyoscyamine,2-oxoglutarate:oxygen oxidoreductase
            ((6S)-hydroxylating)
REACTION    L-hyoscyamine + 2-oxoglutarate + O2 = (6S)-hydroxyhyoscyamine +
            succinate + CO2 [RN:R03812]
ALL_REAC    R03812
SUBSTRATE   L-hyoscyamine [CPD:C02046];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     (6S)-hydroxyhyoscyamine [CPD:C03325];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COFACTOR    Iron [CPD:C00023];
            Ascorbate [CPD:C00072]
COMMENT     Requires Fe2+ and ascorbate.
REFERENCE   1
  AUTHORS   Hashimoto, T. and Yamada, Y.
  TITLE     Hyoscyamine 6beta-hydroxylase, a 2-oxoglutarate-dependent
            dioxygenase, in alkaloid-producing root cultures.
  JOURNAL   Plant Physiol. 81 (1986) 619-625.
  ORGANISM  Hyoscyamus niger, Duboisia leichhardtii, Datura fastuosa, Atropa
            belladonna, Hyoscyamus albus, Hyoscyamus gyorffi, Hyoscyamus
            pusillus, Hyoscyamus muticus
PATHWAY     PATH: map00960  Alkaloid biosynthesis II
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.11
            ExPASy - ENZYME nomenclature database: 1.14.11.11
            ExplorEnz - The Enzyme Database: 1.14.11.11
            ERGO genome analysis and discovery system: 1.14.11.11
            BRENDA, the Enzyme Database: 1.14.11.11
            CAS: 103865-33-4
///
ENTRY       EC 1.14.11.12               Enzyme
NAME        gibberellin-44 dioxygenase;
            oxygenase, gibberellin A44 oxidase;
            (gibberellin-44), 2-oxoglutarate:oxygen oxidoreductase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     (gibberellin-44),2-oxoglutarate:oxygen oxidoreductase
REACTION    gibberellin 44 + 2-oxoglutarate + O2 = gibberellin 19 + succinate +
            CO2 [RN:R07184]
ALL_REAC    R07184;
            (other) R03806 R03807 R05097 R06322 R06323 R06326
SUBSTRATE   gibberellin 44 [CPD:C12308];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     gibberellin 19 [CPD:C02034];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+.
REFERENCE   1
  AUTHORS   Gilmour, S.J., Bleecker, A.B. and Zeevaart, J.A.D.
  TITLE     Partial-purification of gibberellin oxidases from spinach leaves.
  JOURNAL   Plant Physiol. 85 (1987) 87-90.
  ORGANISM  spinach
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
ORTHOLOGY   KO: K05282  gibberellin 20-oxidase
GENES       ATH: AT4G25420(GA5) AT5G07200(YAP169) AT5G51810(ATGA20OX2/GA20OX2)
            OSA: 4334841
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.12
            ExPASy - ENZYME nomenclature database: 1.14.11.12
            ExplorEnz - The Enzyme Database: 1.14.11.12
            ERGO genome analysis and discovery system: 1.14.11.12
            BRENDA, the Enzyme Database: 1.14.11.12
            CAS: 112198-85-3
///
ENTRY       EC 1.14.11.13               Enzyme
NAME        gibberellin 2beta-dioxygenase;
            gibberellin 2beta-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     (gibberellin-1),2-oxoglutarate:oxygen oxidoreductase
            (2beta-hydroxylating)
REACTION    gibberellin 1 + 2-oxoglutarate + O2 = 2beta-hydroxygibberellin 1 +
            succinate + CO2 [RN:R03008]
ALL_REAC    R03008;
            (other) R03809 R06337 R06338 R06342 R06343 R06344 R06345
SUBSTRATE   gibberellin 1 [CPD:C00859];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     2beta-hydroxygibberellin 1 [CPD:C03579];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COMMENT     Also acts on a number of other gibberellins.
REFERENCE   1
  AUTHORS   Smith, V.A. and MacMillan, J.
  TITLE     The partial-purification and characterization of gibberellin
            2beta-hydroxylases from seeds of Pisum sativum.
  JOURNAL   Planta 167 (1986) 9-18.
  ORGANISM  Pisum sativum
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
ORTHOLOGY   KO: K04125  gibberellin 2-oxidase
GENES       ATH: AT1G78440(ATGA2OX1) AT2G34555(ATGA2OX3)
            PIC: PICST_51972(GBD1)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.13
            ExPASy - ENZYME nomenclature database: 1.14.11.13
            ExplorEnz - The Enzyme Database: 1.14.11.13
            ERGO genome analysis and discovery system: 1.14.11.13
            BRENDA, the Enzyme Database: 1.14.11.13
            CAS: 85713-20-8
///
ENTRY       EC 1.14.11.14               Enzyme
NAME        6beta-hydroxyhyoscyamine epoxidase;
            hydroxyhyoscyamine dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     (6S)-6-hydroxyhyoscyamine,2-oxoglutarate oxidoreductase
            (epoxide-forming)
REACTION    (6S)-6-hydroxyhyoscyamine + 2-oxoglutarate + O2 = scopolamine +
            succinate + CO2 + H2O [RN:R03737]
ALL_REAC    R03737
SUBSTRATE   (6S)-6-hydroxyhyoscyamine [CPD:C03325];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     scopolamine [CPD:C01851];
            succinate [CPD:C00042];
            CO2 [CPD:C00011];
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023];
            Ascorbate [CPD:C00072]
COMMENT     Requires Fe2+ and ascorbate.
REFERENCE   1
  AUTHORS   Hashimoto, T., Kohno, J. and Yamada, Y.
  TITLE     6beta-Hydroxyhyoscyamine epoxidase from cultured roots of Hyoscyamus
            niger.
  JOURNAL   Phytochemistry 28 (1989) 1077-1082.
  ORGANISM  Hyoscyamus niger
PATHWAY     PATH: map00960  Alkaloid biosynthesis II
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.14
            ExPASy - ENZYME nomenclature database: 1.14.11.14
            ExplorEnz - The Enzyme Database: 1.14.11.14
            ERGO genome analysis and discovery system: 1.14.11.14
            BRENDA, the Enzyme Database: 1.14.11.14
            CAS: 121479-53-6
///
ENTRY       EC 1.14.11.15               Enzyme
NAME        gibberellin 3beta-dioxygenase;
            gibberellin 3beta-hydroxylase;
            (gibberrellin-20),2-oxoglutarate: oxygen oxidoreductase
            (3beta-hydroxylating)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     (gibberellin-20),2-oxoglutarate:oxygen oxidoreductase
            (3beta-hydroxylating)
REACTION    gibberellin 20 + 2-oxoglutarate + O2 = gibberellin 1 + succinate +
            CO2 [RN:R03009]
ALL_REAC    R03009;
            (other) R06336
SUBSTRATE   gibberellin 20 [CPD:C02035];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     gibberellin 1 [CPD:C00859];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COFACTOR    Iron [CPD:C00023];
            Ascorbate [CPD:C00072]
COMMENT     Requires Fe2+ and ascorbate.
REFERENCE   1
  AUTHORS   Kwak, S.-S., Kamiya, Y., Sakurai, A., Takahishi, N. and Graebe, J.E.
  TITLE     Partial-purification and characterization of gibberellin
            3beta-hydroxylase from immature seeds of Phaseolus vulgaris L.
  JOURNAL   Plant Cell Physiol. 29 (1988) 935-943.
  ORGANISM  Phaseolus vulgaris
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
ORTHOLOGY   KO: K04124  gibberellin 3-beta-dioxygenase
GENES       ATH: AT1G15550(GA4) AT1G80340(GA4H)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.15
            ExPASy - ENZYME nomenclature database: 1.14.11.15
            ExplorEnz - The Enzyme Database: 1.14.11.15
            ERGO genome analysis and discovery system: 1.14.11.15
            BRENDA, the Enzyme Database: 1.14.11.15
            CAS: 116036-68-1
///
ENTRY       EC 1.14.11.16               Enzyme
NAME        peptide-aspartate beta-dioxygenase;
            aspartate beta-hydroxylase;
            aspartylpeptide beta-dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     peptide-L-aspartate,2-oxoglutarate:oxygen oxidoreductase
            (3-hydroxylating)
REACTION    peptide-L-aspartate + 2-oxoglutarate + O2 =
            peptide-3-hydroxy-L-aspartate + succinate + CO2 [RN:R04073]
ALL_REAC    R04073
SUBSTRATE   peptide-L-aspartate;
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     peptide-3-hydroxy-L-aspartate;
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+. Some vitamin K-dependent coagulation factors, as well
            as synthetic peptides based on the structure of the first epidermal
            growth factor domain of human coagulation factor IX or X, can act as
            acceptors.
REFERENCE   1  [PMID:2187868]
  AUTHORS   Gronke RS, Welsch DJ, VanDusen WJ, Garsky VM, Sardana MK, Stern AM,
            Friedman PA.
  TITLE     Partial purification and characterization of bovine liver aspartyl
            beta-hydroxylase.
  JOURNAL   J. Biol. Chem. 265 (1990) 8558-65.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K00476  aspartate beta-hydroxylase
GENES       HSA: 444(ASPH) 55662(HIF1AN)
            PTR: 464202(ASPH) 466183(HIF1AN)
            MMU: 319594(Hif1an)
            CFA: 609221(HIF1AN)
            GGA: 421142(ASPH) 428952(HIF1AN)
            XLA: 432095(MGC84481)
            XTR: 394511(hif1an)
            DRE: 373126(hif1an)
            DME: Dmel_CG8421(Asph)
            TET: TTHERM_01228990
            ECI: UTI89_C2652
            ECV: APECO1_4203
            XFA: XF2100
            XFT: PD0777(aspH)
            XCC: XCC0382(aspH)
            XCB: XC_0394
            XCV: XCV0397(aspH)
            XAC: XAC0382(aspH)
            XOO: XOO0232(aspH)
            XOM: XOO_0212(XOO0212)
            PEN: PSEEN2136 PSEEN4012
            LPN: lpg2463
            LPF: lpl2383
            LPP: lpp2530
            ABO: ABO_0732
            CVI: CV_0836
            REH: H16_A0967(aspH)
            RME: Rmet_0866
            BMA: BMAA0568 BMAA0571
            BML: BMA10299_0896
            BMN: BMA10247_A1863
            BXE: Bxe_A2054 Bxe_C0347
            BUR: Bcep18194_B0466
            BCN: Bcen_4278
            BCH: Bcen2424_4088 Bcen2424_5163
            BPS: BPSS1421 BPSS1422
            BPM: BURPS1710b_2148 BURPS1710b_A0445 BURPS1710b_A0446
            BPL: BURPS1106A_A1927 BURPS1106A_A1928
            BPD: BURPS668_A2019 BURPS668_A2021
            BTE: BTH_II0971
            HAR: HEAR3465
            BME: BMEI0465
            BRA: BRADO5215
            BBT: BBta_5679
            HNE: HNE_1807
STRUCTURES  PDB: 1YCI  2CGN  2CGO  2ILM  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.16
            ExPASy - ENZYME nomenclature database: 1.14.11.16
            ExplorEnz - The Enzyme Database: 1.14.11.16
            ERGO genome analysis and discovery system: 1.14.11.16
            BRENDA, the Enzyme Database: 1.14.11.16
            CAS: 122544-66-5
///
ENTRY       EC 1.14.11.17               Enzyme
NAME        taurine dioxygenase;
            2-aminoethanesulfonate dioxygenase;
            alpha-ketoglutarate-dependent taurine dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     taurine, 2-oxoglutarate:O2 oxidoreductase (sulfite-forming)
REACTION    taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde +
            succinate + CO2 [RN:R05320]
ALL_REAC    R05320
SUBSTRATE   taurine [CPD:C00245];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     sulfite [CPD:C00094];
            aminoacetaldehyde [CPD:C06735];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COFACTOR    Iron [CPD:C00023];
            Ascorbate [CPD:C00072];
            Fe2+ [CPD:C14818]
COMMENT     Requires FeII. The enzyme from Escherichia coli also acts on
            pentanesulfonate, 3-(N-morpholino)propanesulfonate and
            2-(1,3-dioxoisoindolin-2-yl)ethanesulfonate, but at lower rates.
REFERENCE   1  [PMID:9287300]
  AUTHORS   Eichhorn E, van der Ploeg JR, Kertesz MA, Leisinger T.
  TITLE     Characterization of alpha-ketoglutarate-dependent taurine
            dioxygenase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 272 (1997) 23031-6.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00430  Taurine and hypotaurine metabolism
ORTHOLOGY   KO: K03119  taurine dioxygenase
GENES       PIC: PICST_34605(TCD4) PICST_39554(IFH2)
            AFM: AFUA_3G07960 AFUA_4G00110 AFUA_6G10720 AFUA_7G06030
                 AFUA_8G02210
            AOR: AO090003000525
            TET: TTHERM_00823760
            ECO: b0368(tauD)
            ECJ: JW0360(tauD)
            ECE: Z0467(tauD)
            ECS: ECs0422
            ECC: c0476(tauD)
            ECI: UTI89_C0387(tauD)
            ECP: ECP_0431
            ECV: APECO1_1636(tauD)
            ECW: EcE24377A_0392(tauD)
            ECX: EcHS_A0432(tauD)
            YPE: YPO0185(tauD)
            YPK: y3966(tauD)
            YPM: YP_0184(tauD)
            YPA: YPA_3287
            YPN: YPN_3882
            YPP: YPDSF_0110
            YPS: YPTB3719(tauD)
            YPI: YpsIP31758_3935(tauD)
            SFL: SF0250(tauD)
            SFX: S0271(tauD)
            SFV: SFV_0332(tauD)
            SSN: SSON_0346(tauD)
            SBO: SBO_0262(tauD)
            SDY: SDY_0502(tauD)
            PLU: plu1004
            ENT: Ent638_0841
            SPE: Spro_4563
            XCC: XCC0775(tauD)
            XCB: XC_3456
            XCV: XCV0883(tauD)
            XAC: XAC0830(tauD)
            XOO: XOO3767(tauD)
            XOM: XOO_3556(XOO3556)
            VVU: VV2_1395
            VVY: VVA0231
            PAE: PA0193 PA2310 PA3935(tauD)
            PAU: PA14_02420(atsK) PA14_12970(tauD) PA14_34750(tauD)
            PPU: PP_0169 PP_0230(tauD)
            PPF: Pput_0190 Pput_0245 Pput_2676
            PST: PSPTO_5198
            PSB: Psyr_0337 Psyr_1795
            PSP: PSPPH_0320 PSPPH_1752
            PFL: PFL_0137 PFL_0210 PFL_0269(tauD)
            PFO: Pfl_0137 Pfl_0213 Pfl_0253 Pfl_2270
            PEN: PSEEN0146 PSEEN0183(atsK) PSEEN0210(tauD) PSEEN2720
            ACI: ACIAD1592 ACIAD1600
            PHA: PSHAa2147
            AHA: AHA_2939
            CVI: CV_0804 CV_2855(tauD)
            RSO: RSc0746(tauD)
            REU: Reut_A0021 Reut_A1602 Reut_A1665 Reut_A2147 Reut_B3847
                 Reut_B4158 Reut_B4542 Reut_B4751 Reut_B5054 Reut_B5293
                 Reut_C6361
            REH: H16_A0037 H16_A0038 H16_A1263 H16_B0422 H16_B1004 H16_B1034
                 H16_B1533 H16_B2220(tauD1) H16_B2227(tauD2) H16_B2521
            RME: Rmet_1717 Rmet_4136 Rmet_4409 Rmet_4633 Rmet_5119 Rmet_5292
                 Rmet_5823
            BMA: BMA1633 BMAA0690 BMAA2043(tauD)
            BMV: BMASAVP1_1066(tauD)
            BML: BMA10299_1351(tauD)
            BMN: BMA10247_A2333(tauD)
            BXE: Bxe_A2155 Bxe_A2169 Bxe_B2717 Bxe_C0112 Bxe_C0153 Bxe_C0930
            BVI: Bcep1808_4970
            BUR: Bcep18194_A4841 Bcep18194_B2065 Bcep18194_B2066
            BCN: Bcen_1245 Bcen_4348
            BCH: Bcen2424_4017 Bcen2424_4018 Bcen2424_6587
            BAM: Bamb_1586 Bamb_3417 Bamb_6536
            BPS: BPSL2227 BPSS0665 BPSS0824 BPSS1165 BPSS1575(tauD) BPSS2294
            BPM: BURPS1710b_2661(tauD) BURPS1710b_A0131 BURPS1710b_A0623(tauD)
                 BURPS1710b_A1440(tauD) BURPS1710b_A2229 BURPS1710b_A2415(tauD)
            BTE: BTH_I1958 BTH_II0799(tauD) BTH_II1242
            BPE: BP1135(tauD) BP3856
            BPA: BPP3209(tauD) BPP4410
            BBR: BB1053 BB3661(tauD) BB4998
            VEI: Veis_3809
            MMS: mma_2486(tauD)
            MLO: mll5998
            PLA: Plav_0828 Plav_0829 Plav_0838 Plav_0986 Plav_2004 Plav_2504
            RET: RHE_PE00352(ype00176)
            BJA: bll2125 blr0937
            BRA: BRADO1082 BRADO4030 BRADO4292
            BBT: BBta_1366 BBta_3279 BBta_4401
            XAU: Xaut_2770
            RSP: RSP_4012(tauD)
            RSQ: Rsph17025_0752
            HNE: HNE_0905
            NAR: Saro_1546 Saro_3087
            SWI: Swit_2086 Swit_3261
            ELI: ELI_04765
            MTU: Rv3406
            MTC: MT3514
            MBO: Mb3440
            MPA: MAP3729
            MAV: MAV_4353
            MSM: MSMEG_0181 MSMEG_3870
            MGI: Mflv_3107
            MMC: Mmcs_2491
            MKM: Mkms_2536
            MJL: Mjls_2528
            NFA: nfa19570(tauD) nfa32540
            RHA: RHA1_ro01729 RHA1_ro01730 RHA1_ro02083 RHA1_ro02477(tauD)
                 RHA1_ro03785
            SCO: SCO7507(SCBAC17A6.40c)
            SMA: SAV2995(ptlD) SAV5415
            ART: Arth_3036
            AAU: AAur_3009(tauD)
            FRA: Francci3_0252
            FAL: FRAAL0590 FRAAL3281 FRAAL4058 FRAAL4213
            SEN: SACE_3290 SACE_4651(tauD)
            GVI: gll2680
            AVA: Ava_2481 Ava_4329
            TER: Tery_3110
STRUCTURES  PDB: 1GQW  1GY9  1OS7  1OTJ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.17
            ExPASy - ENZYME nomenclature database: 1.14.11.17
            ExplorEnz - The Enzyme Database: 1.14.11.17
            ERGO genome analysis and discovery system: 1.14.11.17
            BRENDA, the Enzyme Database: 1.14.11.17
///
ENTRY       EC 1.14.11.18               Enzyme
NAME        phytanoyl-CoA dioxygenase;
            phytanoyl-CoA hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     phytanoyl-CoA, 2-oxoglutarate:oxygen oxidoreductase
            (2-hydroxylating)
REACTION    phytanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxyphytanoyl-CoA +
            succinate + CO2 [RN:R05722]
ALL_REAC    R05722
SUBSTRATE   phytanoyl-CoA [CPD:C02060];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     2-hydroxyphytanoyl-CoA [CPD:C07343];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COMMENT     Part of the peroxisomal phytanic acid alpha-oxidation pathway.
            Requires Fe2+ and ascorbate.
REFERENCE   1  [PMID:9565335]
  AUTHORS   Jansen GA, Mihalik SJ, Watkins PA, Jakobs C, Moser HW, Wanders RJ.
  TITLE     Characterization of phytanoyl-Coenzyme A hydroxylase in human liver
            and activity measurements in patients with peroxisomal disorders.
  JOURNAL   Clin. Chim. Acta. 271 (1998) 203-11.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:8954107]
  AUTHORS   Jansen GA, Mihalik SJ, Watkins PA, Moser HW, Jakobs C, Denis S,
            Wanders RJ.
  TITLE     Phytanoyl-CoA hydroxylase is present in human liver, located in
            peroxisomes, and deficient in Zellweger syndrome: direct,
            unequivocal evidence for the new, revised pathway of phytanic acid
            alpha-oxidation in humans.
  JOURNAL   Biochem. Biophys. Res. Commun. 229 (1996) 205-10.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:9326940]
  AUTHORS   Jansen GA, Ofman R, Ferdinandusse S, Ijlst L, Muijsers AO, Skjeldal
            OH, Stokke O, Jakobs C, Besley GT, Wraith JE, Wanders RJ.
  TITLE     Refsum disease is caused by mutations in the phytanoyl-CoA
            hydroxylase gene.
  JOURNAL   Nat. Genet. 17 (1997) 190-3.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:7556205]
  AUTHORS   Mihalik SJ, Rainville AM, Watkins PA.
  TITLE     Phytanic acid alpha-oxidation in rat liver peroxisomes. Production
            of alpha-hydroxyphytanoyl-CoA and formate is enhanced by dioxygenase
            cofactors.
  JOURNAL   Eur. J. Biochem. 232 (1995) 545-51.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:9326939]
  AUTHORS   Mihalik SJ, Morrell JC, Kim D, Sacksteder KA, Watkins PA, Gould SJ.
  TITLE     Identification of PAHX, a Refsum disease gene.
  JOURNAL   Nat. Genet. 17 (1997) 185-9.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K00477  phytanoyl-CoA hydroxylase
GENES       HSA: 5264(PHYH)
            PTR: 450310(PHYH)
            MMU: 16922(Phyh)
            RNO: 114209(Phyh)
            CFA: 478001(PHYH)
            BTA: 281400(PHYH)
            GGA: 426601(PHYH)
            XLA: 446332(phyh)
            SPU: 579037(LOC579037)
            CEL: ZK550.6
            ANI: AN1262.2
            AFM: AFUA_1G10170
            AOR: AO090038000507
            TET: TTHERM_00925630 TTHERM_00925650 TTHERM_00925660
            RME: Rmet_3627
            BMA: BMA3264
            BXE: Bxe_A4369
            BUR: Bcep18194_A6429
            BCN: Bcen_2465
            BCH: Bcen2424_3079
            BAM: Bamb_3127
            BPS: BPSL0213
            BPM: BURPS1710b_0397
            BTE: BTH_I0176
            HAR: HEAR3315
            MMS: mma_3549
            SUN: SUN_0232
            RLE: RL3145
            FAL: FRAAL0297
STRUCTURES  PDB: 2A1X  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.18
            ExPASy - ENZYME nomenclature database: 1.14.11.18
            ExplorEnz - The Enzyme Database: 1.14.11.18
            ERGO genome analysis and discovery system: 1.14.11.18
            BRENDA, the Enzyme Database: 1.14.11.18
///
ENTRY       EC 1.14.11.19               Enzyme
NAME        leucocyanidin oxygenase;
            anthocyanidin synthase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     leucocyanidin,2-oxoglutarate:oxygen oxidoreductase
REACTION    leucocyanidin + 2-oxoglutarate + O2 = cis- and
            trans-dihydroquercetins + succinate + CO2 + 2 H2O [RN:R05723 R07366]
ALL_REAC    R05723 R07366;
            (other) R04276 R05036 R05037 R06540
SUBSTRATE   leucocyanidin [CPD:C05906];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     cis-dihydroquercetin [CPD:C12316];
            trans-dihydroquercetin [CPD:C01617];
            succinate [CPD:C00042];
            CO2 [CPD:C00011];
            H2O [CPD:C00001]
COMMENT     The enzyme requires Fe(II) and ascorbate. It is involved in the
            pathway by which many flowering plants make anthocyanin
            (glycosylated anthocyandin) flower pigments. The intermediates are
            transformed into cis- and trans-dihydroquercetin [2], which the
            enzyme can also oxidize to quercetin. Acidification of the products
            gives anthocyanidin [1], which, however, may not be a natural
            precursor of the anthocyanins.
REFERENCE   1  [PMID:10074715]
  AUTHORS   Saito K, Kobayashi M, Gong Z, Tanaka Y, Yamazaki M.
  TITLE     Direct evidence for anthocyanidin synthase as a
            2-oxoglutarate-dependent oxygenase: molecular cloning and functional
            expression of cDNA from a red forma of Perilla frutescens.
  JOURNAL   Plant. J. 17 (1999) 181-9.
  ORGANISM  Perilla frutescens
REFERENCE   2
  AUTHORS   Turnbull, J.J., Sobey, W.J., Aplin, R.T., Hassan, A., Firmin, J.L.,
            Schofield, C.J. and Prescott, A.G.
  TITLE     Are anthocyanidins the immediate products of anthocyanidin
            synthase?.
  JOURNAL   Chem. Commun. (2000) 2473-2474.
  ORGANISM  Perilla frutescens
PATHWAY     PATH: map00941  Flavonoid biosynthesis
ORTHOLOGY   KO: K05277  leucoanthocyanidin dioxygenase
GENES       ATH: AT4G22870 AT4G22880(LDOX)
STRUCTURES  PDB: 2BRT  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.19
            ExPASy - ENZYME nomenclature database: 1.14.11.19
            ExplorEnz - The Enzyme Database: 1.14.11.19
            ERGO genome analysis and discovery system: 1.14.11.19
            BRENDA, the Enzyme Database: 1.14.11.19
            CAS: 180984-01-4
///
ENTRY       EC 1.14.11.20               Enzyme
NAME        deacetoxyvindoline 4-hydroxylase;
            desacetoxyvindoline 4-hydroxylase;
            desacetyoxyvindoline-17-hydroxylase;
            D17H;
            desacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase
            (4beta-hydroxylating)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     deacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase
            (4beta-hydroxylating)
REACTION    deacetoxyvindoline + 2-oxoglutarate + O2 = deacetylvindoline +
            succinate + CO2 [RN:R05857]
ALL_REAC    R05857
SUBSTRATE   deacetoxyvindoline [CPD:C02673];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     deacetylvindoline [CPD:C01091];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COMMENT     Requires Fe2+ and ascorbate. Also acts on
            3-hydroxy-16-methoxy-2,3-dihydrotabersonine and to a lesser extent
            on 16-methoxy-2,3-dihydrotabersonine.
REFERENCE   1  [PMID:16526094]
  AUTHORS   Foucher AL, McIntosh A, Douce G, Wastling J, Tait A, Turner CM.
  TITLE     A proteomic analysis of arsenical drug resistance in Trypanosoma
            brucei.
  JOURNAL   Proteomics. 6 (2006) 2726-32.
REFERENCE   2  [PMID:8449913]
  AUTHORS   De Carolis E, De Luca V.
  TITLE     Purification, characterization, and kinetic analysis of a
            2-oxoglutarate-dependent dioxygenase involved in vindoline
            biosynthesis from Catharanthus roseus.
  JOURNAL   J. Biol. Chem. 268 (1993) 5504-11.
  ORGANISM  Catharanthus roseus
REFERENCE   3  [PMID:9701591]
  AUTHORS   Vazquez-Flota FA, De Luca V.
  TITLE     Developmental and light regulation of desacetoxyvindoline
            4-hydroxylase in catharanthus roseus (L.) G. Don. . Evidence Of a
            multilevel regulatory mechanism
  JOURNAL   Plant. Physiol. 117 (1998) 1351-61.
  ORGANISM  Catharanthus roseus
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.20
            ExPASy - ENZYME nomenclature database: 1.14.11.20
            ExplorEnz - The Enzyme Database: 1.14.11.20
            ERGO genome analysis and discovery system: 1.14.11.20
            BRENDA, the Enzyme Database: 1.14.11.20
            CAS: 132084-83-4
///
ENTRY       EC 1.14.11.21               Enzyme
NAME        clavaminate synthase;
            clavaminate synthase 2;
            clavaminic acid synthase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     deoxyamidinoproclavaminate,2-oxoglutarate:oxygen oxidoreductase
            (3-hydroxylating)
REACTION    (1) deoxyamidinoproclavaminate + 2-oxoglutarate + O2 =
            amidinoproclavaminate + succinate + CO2 [RN:R05466];
            (2) proclavaminate + 2-oxoglutarate + O2 = dihydroclavaminate +
            succinate + CO2 + H2O [RN:R05468];
            (3) dihydroclavaminate + 2-oxoglutarate + O2 = clavaminate +
            succinate + CO2 + H2O [RN:R05469]
ALL_REAC    R05466 R05468 R05469
SUBSTRATE   deoxyamidinoproclavaminate [CPD:C06656];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007];
            proclavaminate [CPD:C06658];
            dihydroclavaminate [CPD:C06659]
PRODUCT     amidinoproclavaminate [CPD:C06657];
            succinate [CPD:C00042];
            CO2 [CPD:C00011];
            dihydroclavaminate [CPD:C06659];
            H2O [CPD:C00001];
            clavaminate [CPD:C06660]
COMMENT     Contains nonheme iron. Catalyses three separate oxidative reactions
            in the pathway for the biosythesis of the beta-lactamase inhibitor
            clavulanate in Streptomyces clavuligerus. The first step
            (hydroxylation) is separated from the latter two (oxidative
            cyclization and desaturation) by the action of EC 3.5.3.22,
            proclavaminate amidinohydrolase. The three reactions are all
            catalysed at the same nonheme iron site.
REFERENCE   1  [PMID:1998687]
  AUTHORS   Salowe SP, Krol WJ, Iwata-Reuyl D, Townsend CA.
  TITLE     Elucidation of the order of oxidations and identification of an
            intermediate in the multistep clavaminate synthase reaction.
  JOURNAL   Biochemistry. 30 (1991) 2281-92.
  ORGANISM  Streptomyces clavuligerus
REFERENCE   2
  AUTHORS   Zhou, J., Gunsior, M., Bachmann, B.O., Townsend, C.A. and Solomon,
            E.I.
  TITLE     Substrate binding to the alpha-ketoglutarate-dependent non-heme iron
            enzyme clavaminate synthase 2: Coupling mechanism of oxidative
            decarboxylation and hydroxylation.
  JOURNAL   J. Am. Chem. Soc. 120 (1998) 13539-13540.
REFERENCE   3  [PMID:10655615]
  AUTHORS   Zhang Z, Ren J, Stammers DK, Baldwin JE, Harlos K, Schofield CJ.
  TITLE     Structural origins of the selectivity of the trifunctional oxygenase
            clavaminic acid synthase.
  JOURNAL   Nat. Struct. Biol. 7 (2000) 127-33.
  ORGANISM  Streptomyces clavuligerus
REFERENCE   4  [PMID:11472170]
  AUTHORS   Zhou J, Kelly WL, Bachmann BO, Gunsior M, Townsend CA, Solomon EI.
  TITLE     Spectroscopic studies of substrate interactions with clavaminate
            synthase 2, a multifunctional alpha-KG-dependent non-heme iron
            enzyme: correlation with mechanisms and reactivities.
  JOURNAL   J. Am. Chem. Soc. 123 (2001) 7388-98.
  ORGANISM  Streptomyces clavuligerus
REFERENCE   5  [PMID:12413541]
  AUTHORS   Townsend CA.
  TITLE     New reactions in clavulanic acid biosynthesis.
  JOURNAL   Curr. Opin. Chem. Biol. 6 (2002) 583-9.
  ORGANISM  Streptomyces clavuligerus
PATHWAY     PATH: map00331  Clavulanic acid biosynthesis
GENES       CYB: CYB_1854
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.21
            ExPASy - ENZYME nomenclature database: 1.14.11.21
            ExplorEnz - The Enzyme Database: 1.14.11.21
            ERGO genome analysis and discovery system: 1.14.11.21
            BRENDA, the Enzyme Database: 1.14.11.21
///
ENTRY       EC 1.14.11.22               Enzyme
NAME        flavone synthase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     flavanone,2-oxoglutarate:oxygen oxidoreductase (dehydrating)
REACTION    a flavanone + 2-oxoglutarate + O2 = a flavone + succinate + CO2 +
            H2O [RN:R07367]
ALL_REAC    R07367 > R02445 R03590 R06551
SUBSTRATE   flavanone [CPD:C00766];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     flavone [CPD:C10043];
            succinate [CPD:C00042];
            CO2 [CPD:C00011];
            H2O [CPD:C00001]
COMMENT     Requires ascorbate for full activity and Fe2+.
REFERENCE   1  [PMID:11524111]
  AUTHORS   Martens S, Forkmann G, Matern U, Lukacin R.
  TITLE     Cloning of parsley flavone synthase I.
  JOURNAL   Phytochemistry. 58 (2001) 43-6.
  ORGANISM  Petroselinum crispum
REFERENCE   2  [PMID:11516175]
  AUTHORS   Lukacin R, Matern U, Junghanns KT, Heskamp ML, Britsch L, Forkmann
            G, Martens S.
  TITLE     Purification and antigenicity of flavone synthase I from irradiated
            parsley cells.
  JOURNAL   Arch. Biochem. Biophys. 393 (2001) 177-83.
  ORGANISM  Apiaceae sp.
REFERENCE   3  [PMID:12782296]
  AUTHORS   Martens S, Forkmann G, Britsch L, Wellmann F, Matern U, Lukacin R.
  TITLE     Divergent evolution of flavonoid 2-oxoglutarate-dependent
            dioxygenases in parsley.
  JOURNAL   FEBS. Lett. 544 (2003) 93-8.
  ORGANISM  Apiaceae sp.
PATHWAY     PATH: map00941  Flavonoid biosynthesis
            PATH: map00943  Isoflavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.22
            ExPASy - ENZYME nomenclature database: 1.14.11.22
            ExplorEnz - The Enzyme Database: 1.14.11.22
            ERGO genome analysis and discovery system: 1.14.11.22
            BRENDA, the Enzyme Database: 1.14.11.22
            CAS: 138263-98-6
///
ENTRY       EC 1.14.11.23               Enzyme
NAME        flavonol synthase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     dihydroflavonol,2-oxoglutarate:oxygen oxidoreductase
REACTION    a dihydroflavonol + 2-oxoglutarate + O2 = a flavonol + succinate +
            CO2 + H2O [RN:R07368]
ALL_REAC    R07368 > R02160 R03126 R06539
SUBSTRATE   dihydroflavonol [CPD:C15570];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     flavonol [CPD:C01495];
            succinate [CPD:C00042];
            CO2 [CPD:C00011];
            H2O [CPD:C00001]
COMMENT     In addition to the desaturation of (2R,3R)-dihydroflavonols to
            flavonols, the enzyme from the satsuma Citrus unshiu also has a
            non-specific activity that trans-hydroxylates the flavanones
            (2S)-naringenin and the unnatural (2R)-naringenin at C-3 to
            kaempferol and (2R,3R)-dihydrokaempferol, respectively [2]. Requires
            Fe2+.
REFERENCE   1  [PMID:12180990]
  AUTHORS   Wellmann F, Lukacin R, Moriguchi T, Britsch L, Schiltz E, Matern U.
  TITLE     Functional expression and mutational analysis of flavonol synthase
            from Citrus unshiu.
  JOURNAL   Eur. J. Biochem. 269 (2002) 4134-42.
  ORGANISM  Citrus unshiu
REFERENCE   2  [PMID:12620339]
  AUTHORS   Lukacin R, Wellmann F, Britsch L, Martens S, Matern U.
  TITLE     Flavonol synthase from Citrus unshiu is a bifunctional dioxygenase.
  JOURNAL   Phytochemistry. 62 (2003) 287-92.
  ORGANISM  Citrus unshiu
REFERENCE   3  [PMID:12782296]
  AUTHORS   Martens S, Forkmann G, Britsch L, Wellmann F, Matern U, Lukacin R.
  TITLE     Divergent evolution of flavonoid 2-oxoglutarate-dependent
            dioxygenases in parsley.
  JOURNAL   FEBS. Lett. 544 (2003) 93-8.
  ORGANISM  Citrus unshiu, Petunia hybrida, Solanum tuberosum [GN:estu], Eustoma
            grandiflorum
REFERENCE   4  [PMID:14570878]
  AUTHORS   Turnbull JJ, Nakajima J, Welford RW, Yamazaki M, Saito K, Schofield
            CJ.
  TITLE     Mechanistic studies on three 2-oxoglutarate-dependent oxygenases of
            flavonoid biosynthesis: anthocyanidin synthase, flavonol synthase,
            and flavanone 3beta-hydroxylase.
  JOURNAL   J. Biol. Chem. 279 (2004) 1206-16.
  ORGANISM  Arabidopsis thaliana [GN:ath]
PATHWAY     PATH: map00941  Flavonoid biosynthesis
ORTHOLOGY   KO: K05278  flavonol synthase
GENES       ATH: AT5G08640(FLS)
            OSA: 4330843
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.23
            ExPASy - ENZYME nomenclature database: 1.14.11.23
            ExplorEnz - The Enzyme Database: 1.14.11.23
            ERGO genome analysis and discovery system: 1.14.11.23
            BRENDA, the Enzyme Database: 1.14.11.23
            CAS: 146359-76-4
///
ENTRY       EC 1.14.11.24               Enzyme
NAME        2'-deoxymugineic-acid 2'-dioxygenase;
            IDS3
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     2'-deoxymugineic acid,2-oxoglutarate:oxygen oxidoreductase
            (2-hydroxylating)
REACTION    2'-deoxymugineic acid + 2-oxoglutarate + O2 = mugineic acid +
            succinate + CO2 [RN:R07185]
ALL_REAC    R07185
SUBSTRATE   2'-deoxymugineic acid [CPD:C15485];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     mugineic acid [CPD:C15500];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COMMENT     Requires iron(II). It is also likely that this enzyme can catalyse
            the hydroxylation of 3-epihydroxy-2'-deoxymugineic acid to form
            3-epihydroxymugineic acid.
REFERENCE   1  [PMID:11117263]
  AUTHORS   Nakanishi H, Yamaguchi H, Sasakuma T, Nishizawa NK, Mori S.
  TITLE     Two dioxygenase genes, Ids3 and Ids2, from Hordeum vulgare are
            involved in the biosynthesis of mugineic acid family
            phytosiderophores.
  JOURNAL   Plant. Mol. Biol. 44 (2000) 199-207.
  ORGANISM  Hordeum vulgare [GN:ehvu]
REFERENCE   2  [PMID:11346963]
  AUTHORS   Kobayashi T, Nakanishi H, Takahashi M, Kawasaki S, Nishizawa NK,
            Mori S.
  TITLE     In vivo evidence that Ids3 from Hordeum vulgare encodes a
            dioxygenase that converts 2'-deoxymugineic acid to mugineic acid in
            transgenic rice.
  JOURNAL   Planta. 212 (2001) 864-71.
  ORGANISM  Hordeum vulgare [GN:ehvu]
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.24
            ExPASy - ENZYME nomenclature database: 1.14.11.24
            ExplorEnz - The Enzyme Database: 1.14.11.24
            ERGO genome analysis and discovery system: 1.14.11.24
            BRENDA, the Enzyme Database: 1.14.11.24
///
ENTRY       EC 1.14.11.25               Enzyme
NAME        mugineic-acid 3-dioxygenase;
            IDS2
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     mugineic acid,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
REACTION    (1) mugineic acid + 2-oxoglutarate + O2 = 3-epihydroxymugineic acid
            + succinate + CO2 [RN:R07186];
            (2) 2'-deoxymugineic acid + 2-oxoglutarate + O2 =
            3-epihydroxy-2'-deoxymugineic acid + succinate + CO2 [RN:R07187]
ALL_REAC    R07186 R07187
SUBSTRATE   mugineic acid [CPD:C15500];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007];
            2'-deoxymugineic acid [CPD:C15485]
PRODUCT     3-epihydroxymugineic acid [CPD:C15501];
            succinate [CPD:C00042];
            CO2 [CPD:C00011];
            3-epihydroxy-2'-deoxymugineic acid [CPD:C15502]
COMMENT     Requires iron(II).
REFERENCE   1  [PMID:11117263]
  AUTHORS   Nakanishi H, Yamaguchi H, Sasakuma T, Nishizawa NK, Mori S.
  TITLE     Two dioxygenase genes, Ids3 and Ids2, from Hordeum vulgare are
            involved in the biosynthesis of mugineic acid family
            phytosiderophores.
  JOURNAL   Plant. Mol. Biol. 44 (2000) 199-207.
  ORGANISM  Hordeum vulgare [GN:ehvu]
REFERENCE   2  [PMID:8061321]
  AUTHORS   Okumura N, Nishizawa NK, Umehara Y, Ohata T, Nakanishi H, Yamaguchi
            T, Chino M, Mori S.
  TITLE     A dioxygenase gene (Ids2) expressed under iron deficiency conditions
            in the roots of Hordeum vulgare.
  JOURNAL   Plant. Mol. Biol. 25 (1994) 705-19.
  ORGANISM  Hordeum vulgare [GN:ehvu]
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.25
            ExPASy - ENZYME nomenclature database: 1.14.11.25
            ExplorEnz - The Enzyme Database: 1.14.11.25
            ERGO genome analysis and discovery system: 1.14.11.25
            BRENDA, the Enzyme Database: 1.14.11.25
///
ENTRY       EC 1.14.11.26               Enzyme
NAME        deacetoxycephalosporin-C hydroxylase;
            deacetylcephalosporin C synthase;
            3'-methylcephem hydroxylase;
            DACS;
            DAOC hydroxylase;
            deacetoxycephalosporin C hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     deacetoxycephalosporin-C,2-oxoglutarate:oxygen oxidoreductase
            (3-hydroxylating)
REACTION    deacetoxycephalosporin C + 2-oxoglutarate + O2 =
            deacetylcephalosporin C + succinate + CO2 [RN:R05229]
ALL_REAC    R05229
SUBSTRATE   deacetoxycephalosporin C [CPD:C06565];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     deacetylcephalosporin C [CPD:C03112];
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COMMENT     Requires iron(II). The enzyme can also use
            3-exomethylenecephalosporin C as a substrate to form
            deacetoxycephalosporin C, although more slowly [2]. In Acremonium
            chrysogenum, the enzyme forms part of a bifunctional protein along
            with EC 1.14.20.1, deactoxycephalosporin-C synthase. It is a
            separate enzyme in Streptomyces clavuligerus.
REFERENCE   1  [PMID:3558321]
  AUTHORS   Dotzlaf JE, Yeh WK.
  TITLE     Copurification and characterization of deacetoxycephalosporin C
            synthetase/hydroxylase from Cephalosporium acremonium.
  JOURNAL   J. Bacteriol. 169 (1987) 1611-8.
  ORGANISM  Cephalosporium acremonium
REFERENCE   2  [PMID:2002049]
  AUTHORS   Baker BJ, Dotzlaf JE, Yeh WK.
  TITLE     Deacetoxycephalosporin C hydroxylase of Streptomyces clavuligerus.
            Purification, characterization, bifunctionality, and evolutionary
            implication.
  JOURNAL   J. Biol. Chem. 266 (1991) 5087-93.
  ORGANISM  Streptomyces clavuligerus
REFERENCE   3  [PMID:8703431]
  AUTHORS   Coque JJ, Enguita FJ, Cardoza RE, Martin JF, Liras P.
  TITLE     Characterization of the cefF gene of Nocardia lactamdurans encoding
            a 3'-methylcephem hydroxylase different from the 7-cephem
            hydroxylase.
  JOURNAL   Appl. Microbiol. Biotechnol. 44 (1996) 605-9.
  ORGANISM  Nocardia lactamdurans
REFERENCE   4  [PMID:8865604]
  AUTHORS   Ghag SK, Brems DN, Hassell TC, Yeh WK.
  TITLE     Refolding and purification of Cephalosporium acremonium
            deacetoxycephalosporin C synthetase/hydroxylase from granules of
            recombinant Escherichia coli.
  JOURNAL   Biotechnol. Appl. Biochem. 24 ( Pt 2) (1996) 109-19.
  ORGANISM  Cephalosporium acremonium
REFERENCE   5  [PMID:14734549]
  AUTHORS   Lloyd MD, Lipscomb SJ, Hewitson KS, Hensgens CM, Baldwin JE,
            Schofield CJ.
  TITLE     Controlling the substrate selectivity of
            deacetoxycephalosporin/deacetylcephalosporin C synthase.
  JOURNAL   J. Biol. Chem. 279 (2004) 15420-6.
  ORGANISM  Cephalosporium acremonium
REFERENCE   6  [PMID:15869968]
  AUTHORS   Wu XB, Fan KQ, Wang QH, Yang KQ.
  TITLE     C-terminus mutations of Acremonium chrysogenum
            deacetoxy/deacetylcephalosporin C synthase with improved activity
            toward penicillin analogs.
  JOURNAL   FEMS. Microbiol. Lett. 246 (2005) 103-10.
  ORGANISM  Acremonium chrysogenum
REFERENCE   7  [PMID:7847890]
  AUTHORS   Martin JF, Gutierrez S, Fernandez FJ, Velasco J, Fierro F, Marcos
            AT, Kosalkova K.
  TITLE     Expression of genes and processing of enzymes for the biosynthesis
            of penicillins and cephalosporins.
  JOURNAL   Antonie. Van. Leeuwenhoek. 65 (1994) 227-43.
  ORGANISM  Acremonium chrysogenum
PATHWAY     PATH: map00311  Penicillin and cephalosporin biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.26
            ExPASy - ENZYME nomenclature database: 1.14.11.26
            ExplorEnz - The Enzyme Database: 1.14.11.26
            ERGO genome analysis and discovery system: 1.14.11.26
            BRENDA, the Enzyme Database: 1.14.11.26
///
ENTRY       EC 1.14.11.27               Enzyme
NAME        [histone-H3]-lysine-36 demethylase;
            JHDM1A;
            JmjC domain-containing histone demethylase 1A;
            H3-K36-specific demethylase;
            histone-lysine (H3-K36) demethylase;
            histone demethylase;
            protein-6-N,6-N-dimethyl-L-lysine,2-oxoglutarate:oxygen
            oxidoreductase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     protein-N6,N6-dimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase
REACTION    (1) protein N6,N6-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein
            N6-methyl-L-lysine + succinate + formaldehyde + CO2;
            (2) protein N6-methyl-L-lysine + 2-oxoglutarate + O2 = protein
            L-lysine + succinate + formaldehyde + CO2
SUBSTRATE   protein N6,N6-dimethyl-L-lysine [CPD:C05545];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007];
            protein N6-methyl-L-lysine [CPD:C05544]
PRODUCT     protein N6-methyl-L-lysine [CPD:C05544];
            succinate [CPD:C00042];
            formaldehyde [CPD:C00067];
            CO2 [CPD:C00011];
            protein L-lysine
COMMENT     Requires iron(II). Of the seven potential methylation sites in
            histones H3 (K4, K9, K27, K36, K79) and H4 (K20, R3) from HeLa
            cells, the enzyme is specific for Lys-36. Lysine residues exist in
            three methylation states (mono-, di- and trimethylated). The enzyme
            preferentially demethylates the dimethyl form of Lys-36 (K36me2),
            which is its natural substrate, to form the monomethyl and
            unmethylated forms of Lys-36. It can also demethylate the
            monomethyl- but not the trimethyl form of Lys-36.
REFERENCE   1  [PMID:16362057]
  AUTHORS   Tsukada Y, Fang J, Erdjument-Bromage H, Warren ME, Borchers CH,
            Tempst P, Zhang Y.
  TITLE     Histone demethylation by a family of JmjC domain-containing
            proteins.
  JOURNAL   Nature. 439 (2006) 811-6.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], human [GN:hsa]
ORTHOLOGY   KO: K10276  F-box and leucine-rich repeat protein 10
            KO: K10277  F-box and leucine-rich repeat protein 11
STRUCTURES  PDB: 2OQ7  2YU1  2YU2  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.27
            ExPASy - ENZYME nomenclature database: 1.14.11.27
            ExplorEnz - The Enzyme Database: 1.14.11.27
            ERGO genome analysis and discovery system: 1.14.11.27
            BRENDA, the Enzyme Database: 1.14.11.27
///
ENTRY       EC 1.14.11.28               Enzyme
NAME        proline 3-hydroxylase;
            P-3-H
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and incorporation of one atom of
            oxygen into each donor
SYSNAME     L-proline,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
REACTION    L-proline + 2-oxoglutarate + O2 = cis-3-hydroxy-L-proline +
            succinate + CO2
SUBSTRATE   L-proline [CPD:C00148];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     cis-3-hydroxy-L-proline;
            succinate [CPD:C00042];
            CO2 [CPD:C00011]
COMMENT     Requires iron(II) for activity. Unlike the proline hydroxylases
            involved in collagen biosynthesis [EC 1.14.11.2 (procollagen-proline
            dioxygenase) and EC 1.14.11.7 (procollagen-proline 3-dioxygenase)],
            this enzyme does not require ascorbate for activity although it does
            increase the activity of the enzyme [2]. The enzyme is specific for
            L-proline as D-proline, trans-4-hydroxy-L-proline,
            cis-4-hydroxy-L-proline and 3,4-dehydro-DL-proline are not
            substrates [2].
REFERENCE   1  [PMID:16535329]
  AUTHORS   Mori H, Shibasaki T, Uozaki Y, Ochiai K, Ozaki A.
  TITLE     Detection of Novel Proline 3-Hydroxylase Activities in Streptomyces
            and Bacillus spp. by Regio- and Stereospecific Hydroxylation of
            l-Proline.
  JOURNAL   Appl. Environ. Microbiol. 62 (1996) 1903-1907.
  ORGANISM  Streptomyces sp., Bacillus sp.
REFERENCE   2  [PMID:9294421]
  AUTHORS   Mori H, Shibasaki T, Yano K, Ozaki A.
  TITLE     Purification and cloning of a proline 3-hydroxylase, a novel enzyme
            which hydroxylates free L-proline to cis-3-hydroxy-L-proline.
  JOURNAL   J. Bacteriol. 179 (1997) 5677-83.
  ORGANISM  Streptomyces sp.
REFERENCE   3  [PMID:11737217]
  AUTHORS   Clifton IJ, Hsueh LC, Baldwin JE, Harlos K, Schofield CJ.
  TITLE     Structure of proline 3-hydroxylase. Evolution of the family of
            2-oxoglutarate dependent oxygenases.
  JOURNAL   Eur. J. Biochem. 268 (2001) 6625-36.
  ORGANISM  Streptomyces sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.11.28
            ExPASy - ENZYME nomenclature database: 1.14.11.28
            ExplorEnz - The Enzyme Database: 1.14.11.28
            ERGO genome analysis and discovery system: 1.14.11.28
            BRENDA, the Enzyme Database: 1.14.11.28
///
ENTRY       EC 1.14.11.-                Enzyme
CLASS       Oxidoreductases;
            Acting on paired donors with incorporation of molecular oxygen;
            With 2-oxoglutarate as one donor, and incorporation of one atom each
            of oxygen into both donors
REACTION    (1) Deacetylcephalosporin C + Succinate + CO2 <=>
            Deacetoxycephalosporin C + 2-Oxoglutarate + Oxygen [RN:R05229];
            (2) 2,4-Dichlorophenoxyacetate + 2-Oxoglutarate + Oxygen <=>
            2,4-Dichlorophenol + Glyoxylate + Succinate + CO2 + H2O [RN:R05419];
            (3) Gibberellin A20 <=> Gibberellin A5 [RN:R06346];
            (4) Gibberellin A5 <=> Gibberellin A3 [RN:R06347];
            (5) Gibberellin A9 <=> 2,3-Dehydro-gibberellin A9 [RN:R06349];
            (6) 2,3-Dehydro-gibberellin A9 <=> Gibberellin A7 [RN:R06350]
SUBSTRATE   Deacetylcephalosporin C [CPD:C03112];
            Succinate [CPD:C00042];
            CO2 [CPD:C00011];
            2,4-Dichlorophenoxyacetate [CPD:C03664];
            2-Oxoglutarate [CPD:C00026];
            Oxygen [CPD:C00007];
            Gibberellin A20 [CPD:C02035];
            Gibberellin A5 [CPD:C11871];
            Gibberellin A9 [CPD:C11863];
            2,3-Dehydro-gibberellin A9 [CPD:C11866]
PRODUCT     Deacetoxycephalosporin C [CPD:C06565];
            2-Oxoglutarate [CPD:C00026];
            Oxygen [CPD:C00007];
            2,4-Dichlorophenol [CPD:C02625];
            Glyoxylate [CPD:C00048];
            Succinate [CPD:C00042];
            CO2 [CPD:C00011];
            H2O [CPD:C00001];
            Gibberellin A5 [CPD:C11871];
            Gibberellin A3 [CPD:C01699];
            2,3-Dehydro-gibberellin A9 [CPD:C11866];
            Gibberellin A7 [CPD:C11867]
///
ENTRY       EC 1.14.12.1                Enzyme
NAME        anthranilate 1,2-dioxygenase (deaminating, decarboxylating);
            anthranilate hydroxylase;
            anthranilic hydroxylase;
            anthranilic acid hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     anthranilate,NAD(P)H:oxygen oxidoreductase (1,2-hydroxylating,
            deaminating, decarboxylating)
REACTION    anthranilate + NAD(P)H + 2 H+ + O2 = catechol + CO2 + NAD(P)+ + NH3
            [RN:R00823]
ALL_REAC    R00823;
            (other) R00825
SUBSTRATE   anthranilate [CPD:C00108];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     catechol [CPD:C00090];
            CO2 [CPD:C00011];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            NH3 [CPD:C00014]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+.
REFERENCE   1
  AUTHORS   Kobayashi, S. and Hayaishi, O.
  TITLE     Anthranilic acid conversion to catechol (Pseudomonas).
  JOURNAL   Methods Enzymol. 17A (1970) 505-510.
  ORGANISM  Pseudomonas sp.
REFERENCE   2
  AUTHORS   Taniguchi, H., Hatanaka, M., Kuno, S., Hayaishi, O., Nakajima, M.
            and Kurihara, N.
  TITLE     Enzymatic formation of catechol from anthranilic acid.
  JOURNAL   J. Biol. Chem. 239 (1964) 2204-2211.
  ORGANISM  Pseudomonas sp., Pseudomonas fluorescens
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00629  Carbazole degradation
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K05598  anthranilate 1,2-dioxygenase (deaminating,
                        decarboxylating)
            KO: K05599  anthranilate 1,2-dioxygenase (deaminating,
                        decarboxylating) large subunit
            KO: K05600  anthranilate 1,2-dioxygenase (deaminating,
                        decarboxylating) small subunit
GENES       PAE: PA2512(antA) PA2513(antB)
            PAU: PA14_32150(antB) PA14_32160(antA)
            PAP: PSPA7_2724(antB) PSPA7_2725(antA)
            PFL: PFL_0758
            ACI: ACIAD2669(antA) ACIAD2670(antB)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.1
            ExPASy - ENZYME nomenclature database: 1.14.12.1
            ExplorEnz - The Enzyme Database: 1.14.12.1
            ERGO genome analysis and discovery system: 1.14.12.1
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.12.1
            BRENDA, the Enzyme Database: 1.14.12.1
            CAS: 9059-17-0
///
ENTRY       EC 1.14.12.2      Obsolete  Enzyme
NAME        Transferred to 1.14.13.35
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
COMMENT     Transferred entry: now EC 1.14.13.35 anthranilate 3-monooxygenase
            (deaminating) (EC 1.14.12.2 created 1972, deleted 1990)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.2
            ExPASy - ENZYME nomenclature database: 1.14.12.2
            ExplorEnz - The Enzyme Database: 1.14.12.2
            ERGO genome analysis and discovery system: 1.14.12.2
            BRENDA, the Enzyme Database: 1.14.12.2
///
ENTRY       EC 1.14.12.3                Enzyme
NAME        benzene 1,2-dioxygenase;
            benzene hydroxylase;
            benzene dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     benzene,NADH:oxygen oxidoreductase (1,2-hydroxylating)
REACTION    benzene + NADH + H+ + O2 = cis-cyclohexa-3,5-diene-1,2-diol + NAD+
            [RN:R03543]
ALL_REAC    R03543
SUBSTRATE   benzene [CPD:C01407];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     cis-cyclohexa-3,5-diene-1,2-diol [CPD:C04091];
            NAD+ [CPD:C00003]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023];
            Sulfur [CPD:C00087];
            Iron-sulfur [CPD:C00824]
COMMENT     A system, containing a reductase which is an iron-sulfur
            flavoprotein (FAD), an iron-sulfur oxygenase and ferredoxin.
            Requires Fe2+.
REFERENCE   1  [PMID:4298226]
  AUTHORS   Gibson DT, Koch JR, Kallio RE.
  TITLE     Oxidative degradation of aromatic hydrocarbons by microorganisms. I.
            Enzymatic formation of catechol from benzene.
  JOURNAL   Biochemistry. 7 (1968) 2653-62.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00626  Naphthalene and anthracene degradation
ORTHOLOGY   KO: K03268  benzene 1,2-dioxygenase
GENES       BUR: Bcep18194_C7072
            BBR: BB0730
            PNA: Pnap_4151
            MVA: Mvan_4416
            LIL: LA3561
            LIC: LIC10633(bedB)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.3
            ExPASy - ENZYME nomenclature database: 1.14.12.3
            ExplorEnz - The Enzyme Database: 1.14.12.3
            ERGO genome analysis and discovery system: 1.14.12.3
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.12.3
            BRENDA, the Enzyme Database: 1.14.12.3
            CAS: 9075-66-5
///
ENTRY       EC 1.14.12.4                Enzyme
NAME        3-hydroxy-2-methylpyridinecarboxylate dioxygenase;
            methylhydroxypyridinecarboxylate oxidase;
            2-methyl-3-hydroxypyridine 5-carboxylic acid dioxygenase;
            methylhydroxypyridine carboxylate dioxygenase;
            3-hydroxy-3-methylpyridinecarboxylate dioxygenase [incorrect]
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     3-hydroxy-2-methylpyridine-5-carboxylate,NAD(P)H:oxygen
            oxidoreductase (decyclizing)
REACTION    3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 =
            2-(acetamidomethylene)succinate + NAD(P)+ [RN:R03385]
ALL_REAC    R03385;
            (other) R03386
SUBSTRATE   3-hydroxy-2-methylpyridine-5-carboxylate [CPD:C01270];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     2-(acetamidomethylene)succinate [CPD:C01215];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:4306031]
  AUTHORS   Sparrow LG, Ho PP, Sundaram TK, Zach D, Nyns EJ, Snell EE.
  TITLE     The bacterial oxidation of vitamin B6. VII. Purification,
            properties, and mechanism of action of an oxygenase which cleaves
            the 3-hydroxypyridine ring.
  JOURNAL   J. Biol. Chem. 244 (1969) 2590-600.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00750  Vitamin B6 metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.4
            ExPASy - ENZYME nomenclature database: 1.14.12.4
            ExplorEnz - The Enzyme Database: 1.14.12.4
            ERGO genome analysis and discovery system: 1.14.12.4
            BRENDA, the Enzyme Database: 1.14.12.4
            CAS: 37256-69-2
///
ENTRY       EC 1.14.12.5                Enzyme
NAME        5-pyridoxate dioxygenase;
            5-pyridoxate oxidase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     5-pyridoxate,NADPH:oxygen oxidoreductase (decyclizing)
REACTION    3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH +
            H+ + O2 = 2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+
            [RN:R04570]
ALL_REAC    R04570
SUBSTRATE   3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate
            [CPD:C04773];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     2-(acetamidomethylene)-3-(hydroxymethyl)succinate [CPD:C04690];
            NADP+ [CPD:C00006]
COFACTOR    FAD [CPD:C00016];
            Flavoprotein [CPD:C06411]
COMMENT     A flavoprotein.
REFERENCE   1  [PMID:4306031]
  AUTHORS   Sparrow LG, Ho PP, Sundaram TK, Zach D, Nyns EJ, Snell EE.
  TITLE     The bacterial oxidation of vitamin B6. VII. Purification,
            properties, and mechanism of action of an oxygenase which cleaves
            the 3-hydroxypyridine ring.
  JOURNAL   J. Biol. Chem. 244 (1969) 2590-600.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00750  Vitamin B6 metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.5
            ExPASy - ENZYME nomenclature database: 1.14.12.5
            ExplorEnz - The Enzyme Database: 1.14.12.5
            ERGO genome analysis and discovery system: 1.14.12.5
            BRENDA, the Enzyme Database: 1.14.12.5
            CAS: 37256-70-5
///
ENTRY       EC 1.14.12.6      Obsolete  Enzyme
NAME        Transferred to 1.14.13.66
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
COMMENT     Transferred entry: now EC 1.14.13.66 2-hydroxycyclohexanone
            2-monooxygenase (EC 1.14.12.6 created 1978, deleted 1999)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.6
            ExPASy - ENZYME nomenclature database: 1.14.12.6
            ExplorEnz - The Enzyme Database: 1.14.12.6
            ERGO genome analysis and discovery system: 1.14.12.6
            BRENDA, the Enzyme Database: 1.14.12.6
///
ENTRY       EC 1.14.12.7                Enzyme
NAME        phthalate 4,5-dioxygenase;
            PDO ;
            phthalate dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     phthalate,NADH:oxygen oxidoreductase (4,5-hydroxylating)
REACTION    phthalate + NADH + H+ + O2 =
            cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD+
            [RN:R03630]
ALL_REAC    R03630
SUBSTRATE   phthalate [CPD:C01606];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate
            [CPD:C04783];
            NAD+ [CPD:C00003]
COFACTOR    Iron [CPD:C00023];
            FMN [CPD:C00061];
            Iron-sulfur [CPD:C00824]
COMMENT     A system, containing a reductase which is an iron-sulfur
            flavoprotein (FMN), an iron-sulfur oxygenase, and no independent
            ferredoxin. Requires Fe2+.
REFERENCE   1  [PMID:3805038]
  AUTHORS   Batie CJ, LaHaie E, Ballou DP.
  TITLE     Purification and characterization of phthalate oxygenase and
            phthalate oxygenase reductase from Pseudomonas cepacia.
  JOURNAL   J. Biol. Chem. 262 (1987) 1510-8.
  ORGANISM  Pseudomonas cepacia
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
ORTHOLOGY   KO: K07519  phthalate 4,5-dioxygenase
GENES       REU: Reut_B4795 Reut_B5777 Reut_C6324
            BUR: Bcep18194_B0419 Bcep18194_B0531 Bcep18194_B0741
                 Bcep18194_B2494 Bcep18194_C6765 Bcep18194_C7074
                 Bcep18194_C7584 Bcep18194_C7699
            VEI: Veis_3584
            MMS: mma_0889
            BRA: BRADO1869
            BBT: BBta_2186
            XAU: Xaut_1044
            SWI: Swit_3062 Swit_4297
            RHA: RHA1_ro00369 RHA1_ro00470 RHA1_ro02824 RHA1_ro03672
                 RHA1_ro03984 RHA1_ro04256
            ART: Arth_1726
            SEN: SACE_2477 SACE_2819 SACE_3556
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.7
            ExPASy - ENZYME nomenclature database: 1.14.12.7
            ExplorEnz - The Enzyme Database: 1.14.12.7
            ERGO genome analysis and discovery system: 1.14.12.7
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.12.7
            BRENDA, the Enzyme Database: 1.14.12.7
            CAS: 63626-44-8
///
ENTRY       EC 1.14.12.8                Enzyme
NAME        4-sulfobenzoate 3,4-dioxygenase;
            4-sulfobenzoate dioxygenase;
            4-sulfobenzoate 3,4-dioxygenase system
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     4-sulfobenzoate,NADH:oxygen oxidoreductase (3,4-hydroxylating,
            sulfite-forming)
REACTION    4-sulfobenzoate + NADH + H+ + O2 = 3,4-dihydroxybenzoate + sulfite +
            NAD+ [RN:R01636]
ALL_REAC    R01636
SUBSTRATE   4-sulfobenzoate [CPD:C02236];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     3,4-dihydroxybenzoate [CPD:C00230];
            sulfite [CPD:C00094];
            NAD+ [CPD:C00003]
COFACTOR    Iron [CPD:C00023];
            FMN [CPD:C00061];
            Iron-sulfur [CPD:C00824]
COMMENT     A system, containing a reductase which is an iron-sulfur
            flavoprotein (FMN), an iron-sulfur oxygenase, and no independent
            ferredoxin. Requires Fe2+.
REFERENCE   1  [PMID:2012609]
  AUTHORS   Locher HH, Leisinger T, Cook AM.
  TITLE     4-Sulphobenzoate 3,4-dioxygenase. Purification and properties of a
            desulphonative two-component enzyme system from Comamonas
            testosteroni T-2.
  JOURNAL   Biochem. J. 274 ( Pt 3) (1991) 833-42.
  ORGANISM  Comamonas testosteroni
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.8
            ExPASy - ENZYME nomenclature database: 1.14.12.8
            ExplorEnz - The Enzyme Database: 1.14.12.8
            ERGO genome analysis and discovery system: 1.14.12.8
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.12.8
            BRENDA, the Enzyme Database: 1.14.12.8
            CAS: 122933-81-7
///
ENTRY       EC 1.14.12.9                Enzyme
NAME        4-chlorophenylacetate 3,4-dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     4-chlorophenylacetate,NADH:oxygen oxidoreductase (3,4-hydroxylating,
            dechlorinating)
REACTION    4-chlorophenylacetate + NADH + H+ + O2 = 3,4-dihydroxyphenylacetate
            + chloride + NAD+ [RN:R03306]
ALL_REAC    R03306
SUBSTRATE   4-chlorophenylacetate [CPD:C03077];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     3,4-dihydroxyphenylacetate [CPD:C01161];
            chloride [CPD:C00115];
            NAD+ [CPD:C00003]
COFACTOR    Iron [CPD:C00023]
COMMENT     A system, containing a reductase and an iron-sulfur oxygenase, and
            no independent ferredoxin. Requires Fe2+. Also acts on 4-bromophenyl
            acetate.
REFERENCE   1  [PMID:3745216]
  AUTHORS   Markus A, Krekel D, Lingens F.
  TITLE     Purification and some properties of component A of the
            4-chlorophenylacetate 3,4-dioxygenase from Pseudomonas species
            strain CBS.
  JOURNAL   J. Biol. Chem. 261 (1986) 12883-8.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.9
            ExPASy - ENZYME nomenclature database: 1.14.12.9
            ExplorEnz - The Enzyme Database: 1.14.12.9
            ERGO genome analysis and discovery system: 1.14.12.9
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.12.9
            BRENDA, the Enzyme Database: 1.14.12.9
            CAS: 105006-00-6
///
ENTRY       EC 1.14.12.10               Enzyme
NAME        benzoate 1,2-dioxygenase;
            benzoate hydroxylase;
            benzoate hydroxylase;
            benzoic hydroxylase;
            benzoate dioxygenase;
            benzoate,NADH:oxygen oxidoreductase (1,2-hydroxylating,
            decarboxylating) [incorrect]
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     benzoate,NADH:oxygen oxidoreductase (1,2-hydroxylating)
REACTION    benzoate + NADH + H+ + O2 =
            1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate + NAD+ [RN:R07188]
ALL_REAC    R07188 > R05621;
            (other) R00819 R05622
SUBSTRATE   benzoate [CPD:C00180];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate [CPD:C04634];
            NAD+ [CPD:C00003]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023];
            Sulfur [CPD:C00087]
COMMENT     A system, containing a reductase which is an iron-sulfur
            flavoprotein (FAD), and an iron-sulfur oxygenase. Requires Fe2+.
REFERENCE   1  [PMID:214433]
  AUTHORS   Yamaguchi M, Fujisawa H.
  TITLE     Characterization of NADH-cytochrome c reductase, a component of
            benzoate 1,2-dioxygenase system from Pseudomonas arvilla c-1.
  JOURNAL   J. Biol. Chem. 253 (1978) 8848-53.
  ORGANISM  Pseudomonas arvilla
REFERENCE   2  [PMID:7372624]
  AUTHORS   Yamaguchi M, Fujisawa H.
  TITLE     Purification and characterization of an oxygenase component in
            benzoate 1,2-dioxygenase system from Pseudomonas arvilla C-1.
  JOURNAL   J. Biol. Chem. 255 (1980) 5058-63.
  ORGANISM  Pseudomonas arvilla
REFERENCE   3  [PMID:7130163]
  AUTHORS   Yamaguchi M, Fujisawa H.
  TITLE     Subunit structure of oxygenase component in benzoate-1,2-dioxygenase
            system from Pseudomonas arvilla C-1.
  JOURNAL   J. Biol. Chem. 257 (1982) 12497-502.
  ORGANISM  Pseudomonas arvilla
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00632  Benzoate degradation via CoA ligation
ORTHOLOGY   KO: K00479  benzoate 1,2-dioxygenase
            KO: K05549  benzoate 1,2-dioxygenase alpha subunit
            KO: K05550  benzoate 1,2-dioxygenase beta subunit
GENES       PAE: PA2518(xylX)
            PAU: PA14_32080(xylX) PA14_32100(xylY)
            PAP: PSPA7_2719(benA) PSPA7_2720(benB)
            PPU: PP_3161(benA) PP_3162(benB)
            PPF: Pput_2553
            PFL: PFL_3857 PFL_3858
            PFO: Pfl_2321 Pfl_2322 Pfl_2967 Pfl_2968
            PEN: PSEEN3142(benB) PSEEN3143(benA)
            PCR: Pcryo_1266
            ACI: ACIAD1436(benA) ACIAD1437(benB)
            REU: Reut_B4403
            REH: H16_A1961(benC) H16_A1962(benB) H16_A1963(benA)
            RME: Rmet_4882 Rmet_4883
            BMA: BMAA0186(benB) BMAA0187(benA)
            BMV: BMASAVP1_1358(benC) BMASAVP1_1359(benB) BMASAVP1_1360(benA)
            BML: BMA10299_1554(benC) BMA10299_1555(benB) BMA10299_1556(benA)
            BMN: BMA10247_A0213(benC) BMA10247_A0214(benB)
                 BMA10247_A0215(benA)
            BXE: Bxe_A0093 Bxe_B0914(benB) Bxe_B0915(benA)
            BPS: BPSS1903(benA) BPSS1904(benB)
            BPM: BURPS1710b_A1000(benB) BURPS1710b_A2115
            BPL: BURPS1106A_A2581(benA) BURPS1106A_A2582(benB)
                 BURPS1106A_A2583(benC)
            BPD: BURPS668_A2725(benA) BURPS668_A2726(benB)
                 BURPS668_A2727(benC)
            BTE: BTH_II0472 BTH_II0473
            BPA: BPP3691 BPP3692
            BBR: BB4125 BB4126
            DAR: Daro_2778 Daro_2779
            RET: RHE_CH00901 RHE_PF00388
            RLE: RL0962 pRL120538
            BME: BMEI0549
            XAU: Xaut_1135
            MSM: MSMEG_1908
            CGL: NCgl2320(cgl2404) NCgl2321(cgl2405)
            CGB: cg2637(benA) cg2638(benB)
            CEF: CE2305 CE2306
            RHA: RHA1_ro02384(benA) RHA1_ro02385(benB)
            SEN: SACE_4378(benB) SACE_4379(benA)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.10
            ExPASy - ENZYME nomenclature database: 1.14.12.10
            ExplorEnz - The Enzyme Database: 1.14.12.10
            ERGO genome analysis and discovery system: 1.14.12.10
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.12.10
            BRENDA, the Enzyme Database: 1.14.12.10
            CAS: 9059-18-1
///
ENTRY       EC 1.14.12.11               Enzyme
NAME        toluene dioxygenase;
            toluene 2,3-dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     toluene,NADH:oxygen oxidoreductase (1,2-hydroxylating)
REACTION    toluene + NADH + H+ + O2 =
            (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+ [RN:R03559]
ALL_REAC    R03559
SUBSTRATE   toluene [CPD:C01455];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol [CPD:C04592];
            NAD+ [CPD:C00003]
COMMENT     A system, containing a reductase which is an iron-sulfur
            flavoprotein (FAD), an iron-sulfur oxygenase, and a ferredoxin. Some
            other aromatic compounds, including ethylbenzene, 4-xylene and some
            halogenated toluenes, are converted into the corresponding
            cis-dihydrodiols.
REFERENCE   1
  AUTHORS   Renganathan, V.
  TITLE     Possible involvement of toluene-2,3-dioxygenase in defluorination of
            3-fluoro-substituted benzenes by toluene-degrading Pseudomonas sp.
            strain T-12.
  JOURNAL   Appl. Exp. Microbiol. 55 (1989) 330-334.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:526270]
  AUTHORS   Subramanian V, Liu TN, Yeh WK, Gibson DT.
  TITLE     Toluene dioxygenase: purification of an iron-sulfur protein by
            affinity chromatography.
  JOURNAL   Biochem. Biophys. Res. Commun. 91 (1979) 1131-9.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00622  Toluene and xylene degradation
GENES       PPF: Pput_2880
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.11
            ExPASy - ENZYME nomenclature database: 1.14.12.11
            ExplorEnz - The Enzyme Database: 1.14.12.11
            ERGO genome analysis and discovery system: 1.14.12.11
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.12.11
            BRENDA, the Enzyme Database: 1.14.12.11
            CAS: 120038-36-0
///
ENTRY       EC 1.14.12.12               Enzyme
NAME        naphthalene 1,2-dioxygenase;
            naphthalene dioxygenase;
            naphthalene oxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     naphthalene,NADH:oxygen oxidoreductase (1,2-hydroxylating)
REACTION    naphthalene + NADH + H+ + O2 =
            (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+ [RN:R02968]
ALL_REAC    R02968;
            (other) R02967 R05422 R05423 R05424 R05425 R05426 R05427 R06909
            R06930 R06937 R07704
SUBSTRATE   naphthalene [CPD:C00829];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (1R,2S)-1,2-dihydronaphthalene-1,2-diol [CPD:C04314];
            NAD+ [CPD:C00003]
COFACTOR    Iron [CPD:C00023]
COMMENT     A system, containing a reductase which is an iron-sulfur
            flavoprotein (FAD), an iron-sulfur oxygenase, and ferredoxin.
            Requires Fe2+.
REFERENCE   1  [PMID:6874638]
  AUTHORS   Ensley BD, Gibson DT.
  TITLE     Naphthalene dioxygenase: purification and properties of a terminal
            oxygenase component.
  JOURNAL   J. Bacteriol. 155 (1983) 505-11.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:234247]
  AUTHORS   Jeffrey AM, Yeh HJ, Jerina DM, Patel TR, Davey JF, Gibson DT.
  TITLE     Initial reactions in the oxidation of naphthalene by Pseudomonas
            putida.
  JOURNAL   Biochemistry. 14 (1975) 575-84.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00624  1- and 2-Methylnaphthalene degradation
            PATH: map00626  Naphthalene and anthracene degradation
            PATH: map00628  Fluorene degradation
            PATH: map00642  Ethylbenzene degradation
GENES       BUR: Bcep18194_B0578 Bcep18194_C6764
            BPM: BURPS1710b_A2492(hcaA12)
            AZO: azo2517(nagAa)
STRUCTURES  PDB: 1EG9  1NDO  1O7G  1O7H  1O7M  1O7N  1O7P  1O7W  1UUV  1UUW  
                 2B1X  2B24  2HMJ  2HMK  2HML  2HMM  2HMN  2HMO  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.12
            ExPASy - ENZYME nomenclature database: 1.14.12.12
            ExplorEnz - The Enzyme Database: 1.14.12.12
            ERGO genome analysis and discovery system: 1.14.12.12
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.12.12
            BRENDA, the Enzyme Database: 1.14.12.12
            CAS: 9074-04-8
///
ENTRY       EC 1.14.12.13               Enzyme
NAME        2-chlorobenzoate 1,2-dioxygenase;
            2-halobenzoate 1,2-dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     2-chlorobenzoate,NADH:oxygen oxidoreductase (1,2-hydroxylating,
            dechlorinating, decarboxylating)
REACTION    2-chlorobenzoate + NADH + H+ + O2 = catechol + chloride + NAD+ + CO2
            [RN:R01033]
ALL_REAC    R01033
SUBSTRATE   2-chlorobenzoate [CPD:C02357];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     catechol [CPD:C00090];
            chloride [CPD:C00115];
            NAD+ [CPD:C00003];
            CO2 [CPD:C00011]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+.
REFERENCE   1  [PMID:2610934]
  AUTHORS   Fetzner S, Muller R, Lingens F.
  TITLE     Degradation of 2-chlorobenzoate by Pseudomonas cepacia 2CBS.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 370 (1989) 1173-82.
  ORGANISM  Pseudomonas cepacia
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
ORTHOLOGY   KO: K08686  2-chlorobenzoate 1,2-dioxygenase
GENES       REU: Reut_B4404
            BXE: Bxe_A1107(ohbB) Bxe_A1108(ohbA)
            BVI: Bcep1808_5826
            BUR: Bcep18194_C7046 Bcep18194_C7047 Bcep18194_C7073
            BCN: Bcen_1305
            BCH: Bcen2424_6525
            BAM: Bamb_6583
            PNA: Pnap_2111
            PDE: Pden_1178
            NAR: Saro_0539
            SWI: Swit_2635
            MSM: MSMEG_1907
            MGI: Mflv_1354
            MMC: Mmcs_1372
            MKM: Mkms_1390
            MJL: Mjls_1406
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.13
            ExPASy - ENZYME nomenclature database: 1.14.12.13
            ExplorEnz - The Enzyme Database: 1.14.12.13
            ERGO genome analysis and discovery system: 1.14.12.13
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.12.13
            BRENDA, the Enzyme Database: 1.14.12.13
            CAS: 125268-83-9
///
ENTRY       EC 1.14.12.14               Enzyme
NAME        2-aminobenzenesulfonate 2,3-dioxygenase;
            2-aminosulfobenzene 2,3-dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     2-aminobenzenesulfonate,NADH:oxygen oxidoreductase
            (2,3-hydroxylating, ammonia-forming)
REACTION    2-aminobenzenesulfonate + NADH + H+ + O2 =
            2,3-dihydroxybenzenesulfonate + NH3 + NAD+ [RN:R05156]
ALL_REAC    R05156
SUBSTRATE   2-aminobenzenesulfonate [CPD:C06333];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     2,3-dihydroxybenzenesulfonate [CPD:C06336];
            NH3 [CPD:C00014];
            NAD+ [CPD:C00003]
REFERENCE   1  [PMID:8002948]
  AUTHORS   Junker F, Field JA, Bangerter F, Ramsteiner K, Kohler HP, Joannou
            CL, Mason JR, Leisinger T, Cook AM.
  TITLE     Oxygenation and spontaneous deamination of 2-aminobenzenesulphonic
            acid in Alcaligenes sp. strain O-1 with subsequent meta ring
            cleavage and spontaneous desulphonation to 2-hydroxymuconic acid.
  JOURNAL   Biochem. J. 300 ( Pt 2) (1994) 429-36.
  ORGANISM  Alcaligenes sp.
REFERENCE   2  [PMID:8075807]
  AUTHORS   Junker F, Leisinger T, Cook AM.
  TITLE     3-Sulphocatechol 2,3-dioxygenase and other dioxygenases (EC
            1.13.11.2 and EC 1.14.12.-) in the degradative pathways of
            2-aminobenzenesulphonic, benzenesulphonic and 4-toluenesulphonic
            acids in Alcaligenes sp. strain O-1.
  JOURNAL   Microbiology. 140 ( Pt 7) (1994) 1713-22.
  ORGANISM  Alcaligenes sp.
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.14
            ExPASy - ENZYME nomenclature database: 1.14.12.14
            ExplorEnz - The Enzyme Database: 1.14.12.14
            ERGO genome analysis and discovery system: 1.14.12.14
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.12.14
            BRENDA, the Enzyme Database: 1.14.12.14
            CAS: 156621-16-8
///
ENTRY       EC 1.14.12.15               Enzyme
NAME        terephthalate 1,2-dioxygenase;
            benzene-1,4-dicarboxylate 1,2-dioxygenase;
            1,4-dicarboxybenzoate 1,2-dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     benzene-1,4-dicarboxylate,NADH:oxygen oxidoreductase
            (1,2-hydroxylating)
REACTION    terephthalate + NADH + H+ + O2 =
            (1R,6S)-dihydroxycyclohexa-2,4-diene-1,4-dicarboxylate + NAD+
            [RN:R05148]
ALL_REAC    R05148
SUBSTRATE   terephthalate [CPD:C06337];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (1R,6S)-dihydroxycyclohexa-2,4-diene-1,4-dicarboxylate [CPD:C06318];
            NAD+ [CPD:C00003]
COMMENT     Has been shown to contain a Rieske [2Fe-2S] cluster
REFERENCE   1  [PMID:7961417]
  AUTHORS   Schlafli HR, Weiss MA, Leisinger T, Cook AM.
  TITLE     Terephthalate 1,2-dioxygenase system from Comamonas testosteroni
            T-2: purification and some properties of the oxygenase component.
  JOURNAL   J. Bacteriol. 176 (1994) 6644-52.
  ORGANISM  Comamonas testosteroni
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.15
            ExPASy - ENZYME nomenclature database: 1.14.12.15
            ExplorEnz - The Enzyme Database: 1.14.12.15
            ERGO genome analysis and discovery system: 1.14.12.15
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.12.15
            BRENDA, the Enzyme Database: 1.14.12.15
            CAS: 162032-76-0
///
ENTRY       EC 1.14.12.16               Enzyme
NAME        2-hydroxyquinoline 5,6-dioxygenase;
            2-oxo-1,2-dihydroquinoline 5,6-dioxygenase;
            quinolin-2-ol 5,6-dioxygenase;
            quinolin-2(1H)-one 5,6-dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     quinolin-2-ol,NADH:oxygen oxidoreductase (5,6-hydroxylating)
REACTION    quinolin-2-ol + NADH + H+ + O2 =
            2,5,6-trihydroxy-5,6-dihydroquinoline + NAD+ [RN:R05157]
ALL_REAC    R05157
SUBSTRATE   quinolin-2-ol [CPD:C06338];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     2,5,6-trihydroxy-5,6-dihydroquinoline [CPD:C06339];
            NAD+ [CPD:C00003]
COMMENT     3-Methylquinolin-2-ol, quinolin-8-ol and quinolin-2,8-diol are also
            substrates. Quinolin-2-ols exist largely as their quinolin-2(1H)-one
            tautomers
REFERENCE   1  [PMID:7556204]
  AUTHORS   Schach S, Tshisuaka B, Fetzner S, Lingens F.
  TITLE     Quinoline 2-oxidoreductase and 2-oxo-1,2-dihydroquinoline
            5,6-dioxygenase from Comamonas testosteroni 63. The first two
            enzymes in quinoline and 3-methylquinoline degradation.
  JOURNAL   Eur. J. Biochem. 232 (1995) 536-44.
  ORGANISM  Comamonas testosteroni
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.16
            ExPASy - ENZYME nomenclature database: 1.14.12.16
            ExplorEnz - The Enzyme Database: 1.14.12.16
            ERGO genome analysis and discovery system: 1.14.12.16
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.12.16
            BRENDA, the Enzyme Database: 1.14.12.16
            CAS: 172399-50-7
///
ENTRY       EC 1.14.12.17               Enzyme
NAME        nitric oxide dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     nitric oxide,NAD(P)H:oxygen oxidoreductase
REACTION    2 nitric oxide + 2 O2 + NAD(P)H = 2 nitrate + NAD(P)+ + H+
            [RN:R05724 R05725]
ALL_REAC    R05724 R05725
SUBSTRATE   nitric oxide [CPD:C00533];
            O2 [CPD:C00007];
            NADH [CPD:C00004];
            NADPH [CPD:C00005]
PRODUCT     nitrate [CPD:C00244];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H+ [CPD:C00080]
COMMENT     A flavohemoglobin (FAD). It has been proposed that FAD functions as
            the electron carrier from NADPH to the ferric heme prosthetic group.
REFERENCE   1  [PMID:9756889]
  AUTHORS   Gardner PR, Costantino G, Salzman AL.
  TITLE     Constitutive and adaptive detoxification of nitric oxide in
            Escherichia coli. Role of nitric-oxide dioxygenase in the protection
            of aconitase.
  JOURNAL   J. Biol. Chem. 273 (1998) 26528-33.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:9724711]
  AUTHORS   Gardner PR, Gardner AM, Martin LA, Salzman AL.
  TITLE     Nitric oxide dioxygenase: an enzymic function for flavohemoglobin.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 10378-83.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K05916  nitric oxide dioxygenase
GENES       SCE: YGR234W(YHB1)
            PIC: PICST_88330(YHB1)
            CGR: CAGL0L06666g
            SPO: SPAC869.02c
            ANI: AN7169.2
            AFM: AFUA_4G03410
            AOR: AO090011000202
            CNE: CNC07160
            DDI: DDB_0191088(fhbB) DDB_0191099(fhbA)
            ECO: b2552(hmpA)
            ECJ: JW2536(hmp)
            ECE: Z3828(hmpA)
            ECS: ECs3418
            ECC: c3075(hmpA)
            ECI: UTI89_C2871(hmpA)
            ECV: APECO1_3979(hmpA)
            ECW: EcE24377A_2837(hmp)
            ECX: EcHS_A2705(hmp)
            STY: STY2803(hmpA)
            STT: t0300(hmpA)
            SPT: SPA0310(hmpA)
            SEC: SC2551(hmpA)
            STM: STM2556(hmpA)
            YPE: YPO2908(hmp)
            YPK: y1321(hmpA)
            YPM: YP_2547(hmp2)
            YPA: YPA_2348
            YPN: YPN_1231
            YPS: YPTB2870(hmp)
            YPI: YpsIP31758_1157(hmp)
            SFL: SF2599(hmp)
            SFX: S2771(hmpA)
            SFV: SFV_2600(hmpA)
            SSN: SSON_2635(hmpA)
            SBO: SBO_2580(hmpA)
            SDY: SDY_2742(hmpA)
            ECA: ECA3251(hmpX)
            PLU: plu3292(hmpA)
            XFA: XF0053
            XFT: PD0038(hmpA)
            VCH: VCA0183
            VVU: VV1_1301
            VVY: VV3064
            VPA: VP2809
            VFI: VF2316
            PPR: PBPRA3343
            PAE: PA2664(fhp)
            PPU: PP_0808(hmpA)
            PSP: PSPPH_1247(hmp)
            PFL: PFL_5040(hmp)
            PFO: Pfl_4652
            PEN: PSEEN0952(hmp)
            SHN: Shewana3_3174
            CPS: CPS_0848(hmpA)
            PHA: PSHAa2880(hmp)
            HCH: HCH_01369(hmp)
            AHA: AHA_0661
            CVI: CV_3488(hmpA)
            RSO: RSc3398(RS01706)
            REU: Reut_A3219
            REH: H16_A3533(hmp2)
            RME: Rmet_3382
            BMA: BMA2417(hmp)
            BMV: BMASAVP1_A0334(hmp)
            BML: BMA10299_A1195(hmp)
            BMN: BMA10247_2605(hmp)
            BXE: Bxe_B2333
            BPS: BPSL2840(hmpA)
            BPM: BURPS1710b_3338(hmpA)
            BPL: BURPS1106A_3326(hmp)
            BPD: BURPS668_3293(hmp)
            BTE: BTH_I1294
            BPE: BP2212(fhp)
            BPA: BPP1637(fhp)
            BBR: BB3091(fhp)
            POL: Bpro_3408
            HAR: HEAR0653
            TBD: Tbd_2329
            MFA: Mfla_0639
            SME: SMa1191
            BRA: BRADO2474
            BBT: BBta_2821
            RPE: RPE_1262
            NAR: Saro_0148
            SWI: Swit_1434 Swit_5203 Swit_5299
            GOX: GOX0861
            GBE: GbCGDNIH1_1674
            BSU: BG11418(hmp)
            BHA: BH1058(hmp)
            BAN: BA1467(hmp)
            BAR: GBAA1467(hmp)
            BAA: BA_1989
            BAT: BAS1357
            BCE: BC1448
            BCA: BCE_1571(hmp)
            BCZ: BCZK1330(hmp)
            BTK: BT9727_1331(hmp)
            BLI: BL02894(hmp)
            BLD: BLi01006(hmp)
            BCL: ABC0350(hmp)
            BAY: RBAM_026710(hmp) RBAM_028210(hmp1)
            BPU: BPUM_0894(hmp)
            OIH: OB0291
            GKA: GK1737
            SAU: SA0231
            SAV: SAV0240
            SAM: MW0216
            SAR: SAR0233
            SAS: SAS0216
            SAC: SACOL0220
            SAB: SAB0179c
            SAA: SAUSA300_0234
            SAO: SAOUHSC_00204
            SEP: SE0440
            SER: SERP0325
            SHA: SH1899
            SSP: SSP1728 SSP2410
            CPE: CPE0778
            CGL: NCgl2740(cgl2838)
            CEF: CE2658
            NFA: nfa36850
            RHA: RHA1_ro02265
            SCO: SCO7428(hmpA1)
            SMA: SAV5953(fhbB)
            TFU: Tfu_0423
            FAL: FRAAL5017(hmpA)
            RBA: RB12262(fhp)
            FPS: FP1857(hmp)
            DRA: DR_A0243
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.17
            ExPASy - ENZYME nomenclature database: 1.14.12.17
            ExplorEnz - The Enzyme Database: 1.14.12.17
            ERGO genome analysis and discovery system: 1.14.12.17
            BRENDA, the Enzyme Database: 1.14.12.17
///
ENTRY       EC 1.14.12.18               Enzyme
NAME        biphenyl 2,3-dioxygenase;
            biphenyl dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     biphenyl,NADH:oxygen oxidoreductase (2,3-hydroxylating)
REACTION    biphenyl + NADH + H+ + O2 =
            (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ [RN:R05263]
ALL_REAC    R05263;
            (other) R05261 R05262 R05264
SUBSTRATE   biphenyl [CPD:C06588];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol [CPD:C06589];
            NAD+ [CPD:C00003]
COMMENT     Requires Fe2+. The enzyme from Burkholderia fungorum LB400
            (previously Pseudomonas sp.) is part of a multicomponent system
            composed of an NADH:ferredoxin oxidoreductase (FAD cofactor), a
            [2Fe-2S] Rieske-type ferredoxin, and a terminal oxygenase that
            contains a [2Fe-2S] Rieske-type iron-sulfur cluster and a catalytic
            mononuclear nonheme iron centre. Chlorine-substituted biphenyls can
            also act as substrates. Similar to the three-component enzyme
            systems EC 1.14.12.3 (benzene 1,2-dioxygenase) and EC 1.14.12.11
            (toluene dioxygenase).
REFERENCE   1  [PMID:7592331]
  AUTHORS   Haddock JD, Gibson DT.
  TITLE     Purification and characterization of the oxygenase component of
            biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400.
  JOURNAL   J. Bacteriol. 177 (1995) 5834-9.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:9451832]
  AUTHORS   Haddock JD, Pelletier DA, Gibson DT.
  TITLE     Purification and properties of ferredoxinBPH, a component of
            biphenyl 2,3-dioxygenase of Pseudomonas sp strain LB400.
  JOURNAL   J. Ind. Microbiol. Biotechnol. 19 (1997) 355-9.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:9683647]
  AUTHORS   Broadus RM, Haddock JD.
  TITLE     Purification and characterization of the NADH:ferredoxinBPH
            oxidoreductase component of biphenyl 2,3-dioxygenase from
            Pseudomonas sp. strain LB400.
  JOURNAL   Arch. Microbiol. 170 (1998) 106-12.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00621  Biphenyl degradation
ORTHOLOGY   KO: K08689  biphenyl 2,3-dioxygenase
GENES       BXE: Bxe_C1196(bphA2) Bxe_C1197(bphA1)
            BUR: Bcep18194_B2325 Bcep18194_B2496
            RHA: RHA1_ro08058(bphAc) RHA1_ro08059(bphAb) RHA1_ro08060(bphAa)
                 RHA1_ro10133(etbAa1) RHA1_ro10134(etbAb1) RHA1_ro10143(etbAa2)
                 RHA1_ro10144(etbAb2) RHA1_ro10145(etbAc)
STRUCTURES  PDB: 1ULI  1ULJ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.18
            ExPASy - ENZYME nomenclature database: 1.14.12.18
            ExplorEnz - The Enzyme Database: 1.14.12.18
            ERGO genome analysis and discovery system: 1.14.12.18
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.12.18
            BRENDA, the Enzyme Database: 1.14.12.18
///
ENTRY       EC 1.14.12.19               Enzyme
NAME        3-phenylpropanoate dioxygenase;
            HcaA1A2CD;
            Hca dioxygenase;
            3-phenylpropionate dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into the other donor
SYSNAME     3-phenylpropanoate,NADH:oxygen oxidoreductase (2,3-hydroxylating)
REACTION    3-phenylpropanoate + NADH + H+ + O2 =
            3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD+
            [RN:R06782]
ALL_REAC    R06782;
            (other) R06783
SUBSTRATE   3-phenylpropanoate;
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate;
            NAD+ [CPD:C00003]
COMMENT     This enzyme catalyses the insertion of both atoms of molecular
            oxygen into positions 2 and 3 of the phenyl ring of
            3-phenylpropanoate. The product,
            3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate, is then
            converted into 3-(2,3-dihydroxyphenyl)propanoate, by a
            dehydrogenase, with the concomitant regeneration of NADH. The enzyme
            also acts on (2E)-3-phenylprop-2-enoate (cinnamate).
REFERENCE   1  [PMID:9603882]
  AUTHORS   Diaz E, Ferrandez A, Garcia JL.
  TITLE     Characterization of the hca cluster encoding the dioxygenolytic
            pathway for initial catabolism of 3-phenylpropionic acid in
            Escherichia coli K-12.
  JOURNAL   J. Bacteriol. 180 (1998) 2915-23.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:6345502]
  AUTHORS   Burlingame R, Chapman PJ.
  TITLE     Catabolism of phenylpropionic acid and its 3-hydroxy derivative by
            Escherichia coli.
  JOURNAL   J. Bacteriol. 155 (1983) 113-21.
  ORGANISM  Escherichia coli [GN:eco]
GENES       ECW: EcE24377A_2824(hcaF)
            ECX: EcHS_A2690(hcaE) EcHS_A2692(hcaC)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.12.19
            ExPASy - ENZYME nomenclature database: 1.14.12.19
            ExplorEnz - The Enzyme Database: 1.14.12.19
            ERGO genome analysis and discovery system: 1.14.12.19
            BRENDA, the Enzyme Database: 1.14.12.19
///
ENTRY       EC 1.14.12.-                Enzyme
CLASS       Oxidoreductases;
            Acting on paired donors with incorporation of molecular oxygen;
            With NADH or NADPH as one donor, and incorporation of two atoms of
            oxygen into one donor
REACTION    (1) 4-Aminobenzenesulfonate + Oxygen + 2 H+ <=> 4-Sulfocatechol +
            NH3 [RN:R05279];
            (2) 3,4-Dihydroxybenzoate + NH3 <=> 4-Aminobenzoate + Oxygen + 2 H+
            [RN:R05280];
            (3) Toluate + Oxygen + NADH + H+ <=>
            cis-1,2-Dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate + NAD+
            [RN:R05290];
            (4) Toluate + Oxygen + NADPH + H+ <=>
            cis-1,2-Dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate + NADP+
            [RN:R05291];
            (5) Toluene-4-sulfonate + Oxygen + NADH <=> 4-Methylcatechol + HSO3-
            + NAD+ [RN:R05294];
            (6) o-Toluate + Oxygen + NADH + H+ <=>
            1,2-Dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate + NAD+
            [RN:R05428];
            (7) 1,4-Dichlorobenzene + Oxygen + NADH + H+ <=>
            3,6-Dichloro-cis-1,2-dihydroxycyclohexa-3,5-diene + NAD+
            [RN:R05429];
            (8) 2 Indanone + Oxygen + 2 NADH + 2 H+ <=> 2 Dihydrocoumarin + 2
            NAD+ [RN:R05430];
            (9) 2 Indanone + Oxygen + 2 NADH + 2 H+ <=> 2 3-Hydroxy-1-indanone +
            2 NAD+ [RN:R05431];
            (10) 2 Indanone + Oxygen + 2 NADPH + 2 H+ <=> 2 Dihydrocoumarin + 2
            NADP+ [RN:R05432];
            (11) 2 Indanone + Oxygen + 2 NADPH + 2 H+ <=> 2 3-Hydroxy-1-indanone
            + 2 NADP+ [RN:R05433];
            (12) Dibenzofuran + Oxygen + NADH + H+ <=> 2,2',3-Trihydroxybiphenyl
            + NAD+ [RN:R05434];
            (13) Fluoren-9-one + Oxygen + 2 NADH <=>
            3,4-Dihydroxy-3,4-dihydro-9-fluorenone + 2 NAD+ [RN:R05435];
            (14) Fluoren-9-one + Oxygen + 2 NADPH <=>
            3,4-Dihydroxy-3,4-dihydro-9-fluorenone + 2 NADP+ [RN:R05436];
            (15) 2 2-Indanone + Oxygen + 2 NADH + 2 H+ <=> 2 3-Isochromanone + 2
            NAD+ [RN:R05437];
            (16) 2 2-Indanone + Oxygen + 2 NADPH + 2 H+ <=> 2 3-Isochromanone +
            2 NADP+ [RN:R05438];
            (17) Dibenzo-p-dioxin + Oxygen + NADH + H+ <=>
            2,2',3-Trihydroxydiphenylether + NAD+ [RN:R05439];
            (18) Ethylbenzene + Oxygen + NADH + H+ <=>
            cis-1,2-Dihydro-3-ethylcatechol + NAD+ [RN:R05440];
            (19) m-Methylbenzoate + NADH + Oxygen + H+ <=>
            1,6-Dihydroxy-5-methylcyclohexa-2,4-dienecarboxylate + NAD+
            [RN:R05665];
            (20) Phenylpropanoate + Oxygen + NADH + H+ <=>
            cis-3-(Carboxy-ethyl)-3,5-cyclo-hexadiene-1,2-diol + NAD+
            [RN:R06782];
            (21) trans-Cinnamate + Oxygen + NADH + H+ <=>
            cis-3-(3-Carboxyethenyl)-3,5-cyclohexadiene-1,2-diol + NAD+
            [RN:R06783];
            (22) 1,2,4-Trichlorobenzene + NADH + H+ + Oxygen <=>
            3,4,6-Trichloro-cis-1,2-dihydroxycyclohexa-3,5-diene + NAD+
            [RN:R06831];
            (23) Chlorobenzene + Oxygen + NADH + H+ <=>
            3-Chloro-cis-1,2-dihydroxycyclohexa-3,5-diene + NAD+ [RN:R06856];
            (24) 1-Naphthoic acid + Oxygen + NADH + H+ <=>
            cis-1,2-Dihydroxy-1,2-dihydro-8-carboxynaphthalene + NAD+
            [RN:R06919]
SUBSTRATE   4-Aminobenzenesulfonate [CPD:C06335];
            Oxygen [CPD:C00007];
            H+ [CPD:C00080];
            3,4-Dihydroxybenzoate [CPD:C00230];
            NH3 [CPD:C00014];
            Toluate [CPD:C01454];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            Toluene-4-sulfonate [CPD:C06677];
            o-Toluate [CPD:C07215];
            1,4-Dichlorobenzene [CPD:C07092];
            Indanone [CPD:C01504];
            Dibenzofuran [CPD:C07729];
            Fluoren-9-one [CPD:C06712];
            2-Indanone [CPD:C07727];
            Dibenzo-p-dioxin [CPD:C07732];
            Ethylbenzene [CPD:C07111];
            m-Methylbenzoate [CPD:C07211];
            Phenylpropanoate [CPD:C05629];
            trans-Cinnamate [CPD:C00423];
            1,2,4-Trichlorobenzene [CPD:C06594];
            Chlorobenzene [CPD:C06990];
            1-Naphthoic acid [CPD:C14091]
PRODUCT     4-Sulfocatechol [CPD:C06674];
            NH3 [CPD:C00014];
            4-Aminobenzoate [CPD:C00568];
            Oxygen [CPD:C00007];
            H+ [CPD:C00080];
            cis-1,2-Dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate
            [CPD:C06729];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            4-Methylcatechol [CPD:C06730];
            HSO3- [CPD:C11481];
            1,2-Dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate [CPD:C06731];
            3,6-Dichloro-cis-1,2-dihydroxycyclohexa-3,5-diene [CPD:C07093];
            Dihydrocoumarin [CPD:C02274];
            3-Hydroxy-1-indanone [CPD:C07720];
            2,2',3-Trihydroxybiphenyl [CPD:C03569];
            3,4-Dihydroxy-3,4-dihydro-9-fluorenone [CPD:C07722];
            3-Isochromanone [CPD:C07728];
            2,2',3-Trihydroxydiphenylether [CPD:C07733];
            cis-1,2-Dihydro-3-ethylcatechol [CPD:C06727];
            1,6-Dihydroxy-5-methylcyclohexa-2,4-dienecarboxylate [CPD:C06720];
            cis-3-(Carboxy-ethyl)-3,5-cyclo-hexadiene-1,2-diol [CPD:C11588];
            cis-3-(3-Carboxyethenyl)-3,5-cyclohexadiene-1,2-diol [CPD:C12622];
            3,4,6-Trichloro-cis-1,2-dihydroxycyclohexa-3,5-diene [CPD:C12832];
            3-Chloro-cis-1,2-dihydroxycyclohexa-3,5-diene [CPD:C12837];
            cis-1,2-Dihydroxy-1,2-dihydro-8-carboxynaphthalene [CPD:C14092]
///
ENTRY       EC 1.14.13.1                Enzyme
NAME        salicylate 1-monooxygenase;
            salicylate hydroxylase;
            salicylate 1-hydroxylase;
            salicylate monooxygenase;
            salicylate hydroxylase (decarboxylating)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     salicylate,NADH:oxygen oxidoreductase (1-hydroxylating,
            decarboxylating)
REACTION    salicylate + NADH + 2 H+ + O2 = catechol + NAD+ + H2O + CO2
            [RN:R00818]
ALL_REAC    R00818;
            (other) R05632 R06915 R06936 R06939
SUBSTRATE   salicylate [CPD:C00805];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     catechol [CPD:C00090];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001];
            CO2 [CPD:C00011]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1
  AUTHORS   Suzuki, K., Takemori, S. and Katagiri, M.
  TITLE     Mechanism of the salicylate hydroxylase reaction. IV. Fluorimetric
            analysis of the complex formation.
  JOURNAL   Biochim. Biophys. Acta 191 (1969) 77-85.
REFERENCE   2  [PMID:4898626]
  AUTHORS   Takemori S, Yasuda H, Mihara K, Suzuki K, Katagiri M.
  TITLE     Mechanism of the salicylate hydroxylase reaction. II. The
            enzyme-substrate complex.
  JOURNAL   Biochim. Biophys. Acta. 191 (1969) 58-68.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   3  [PMID:4309912]
  AUTHORS   Takemori S, Yasuda H, Mihara K, Suzuki K, Katagiri M.
  TITLE     Mechanism of the salicylate hydroxylase reaction. 3.
            Characterization and reactivity of chemically or photochemically
            reduced enzyme-flavin.
  JOURNAL   Biochim. Biophys. Acta. 191 (1969) 69-76.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   4
  AUTHORS   Yamamoto, S., Katagiri, M., Maeno, H. and Hayaishi, O.
  TITLE     Salicylate hydroxylase, a monooxygenase requiring flavin adenine
            dinucleotide.
  JOURNAL   J. Biol. Chem. 240 (1965) 3408-3413.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00624  1- and 2-Methylnaphthalene degradation
            PATH: map00626  Naphthalene and anthracene degradation
            PATH: map00628  Fluorene degradation
ORTHOLOGY   KO: K00480  salicylate hydroxylase
GENES       PIC: PICST_31033(NHG3) PICST_56402(NHG1.2)
            ANI: AN2114.2 AN3382.2 AN4576.2 AN7382.2 AN7902.2
            AFM: AFUA_1G02970 AFUA_1G12410 AFUA_1G17670 AFUA_2G00770
                 AFUA_2G01680 AFUA_2G01950 AFUA_2G04330 AFUA_2G05260
                 AFUA_3G01460 AFUA_3G01600 AFUA_4G01530 AFUA_6G07340
                 AFUA_6G13970 AFUA_6G14510 AFUA_7G00590 AFUA_8G02380
                 AFUA_8G06050 AFUA_8G07020
            AOR: AO090003000349 AO090010000109 AO090011000262 AO090011000462
                 AO090020000356
            CNE: CNA08200
            UMA: UM03408.1 UM05967.1
            ECE: Z3390
            ECS: ECs3027
            STY: STY2405
            STT: t0680
            SPT: SPA0676
            SEC: SC2192(nhg)
            STM: STM2175
            SGL: SG0076
            PPU: PP_3944(nahG)
            PEN: PSEEN2596(mhbM)
            ACI: ACIAD0984 ACIAD1424(salA)
            MMW: Mmwyl1_0991
            RSO: RS01683(RSp0911)
            REU: Reut_A2515 Reut_B3601 Reut_B5805 Reut_B5861
            REH: H16_A0578 H16_A0922 H16_A1785 H16_B0750
            BXE: Bxe_B2392 Bxe_B2526 Bxe_C0213 Bxe_C1022
            BUR: Bcep18194_A4962 Bcep18194_B0481 Bcep18194_B1231
                 Bcep18194_B1886 Bcep18194_C6859
            BCN: Bcen_4324
            BCH: Bcen2424_4042
            BAM: Bamb_1082 Bamb_4040
            BPE: BP1954
            BPA: BPP2327
            BBR: BB1778
            RFR: Rfer_3311
            POL: Bpro_2128 Bpro_3591
            AAV: Aave_3927
            EBA: ebA1378(s5h)
            AZO: azo2422(nahG)
            PUB: SAR11_0110(nah)
            MLO: mll8158
            MES: Meso_0052 Meso_1117
            SME: SMc02116
            ATU: Atu1574(nah)
            ATC: AGR_C_2901
            RET: RHE_CH01900(nah)
            RLE: RL2206
            BME: BMEI1017 BMEI1207
            BMF: BAB1_0770
            BMS: BR0746
            BMB: BruAb1_0763
            BJA: blr4977 blr5591(nah)
            BRA: BRADO2323 BRADO2935
            BBT: BBta_2684 BBta_5237
            RPA: RPA3433
            RPB: RPB_2131
            RPC: RPC_3149
            RPD: RPD_3292
            RPE: RPE_2307
            NWI: Nwi_2182
            NHA: Nham_2584
            BHE: BH09840
            BQU: BQ07610
            SIL: SPO2510(nahG) SPO3692
            SIT: TM1040_0896
            RSP: RSP_2656(nahG)
            RDE: RD1_2791
            CGL: NCgl2923(cgl3026)
            CGB: cg3354
            CEF: CE0117 CE2863
            RHA: RHA1_ro01869
            SCO: SCO3245(SCE29.14c)
            FRA: Francci3_2068 Francci3_4207
            SEN: SACE_1995
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.1
            ExPASy - ENZYME nomenclature database: 1.14.13.1
            ExplorEnz - The Enzyme Database: 1.14.13.1
            ERGO genome analysis and discovery system: 1.14.13.1
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.1
            BRENDA, the Enzyme Database: 1.14.13.1
            CAS: 9059-28-3
///
ENTRY       EC 1.14.13.2                Enzyme
NAME        4-hydroxybenzoate 3-monooxygenase;
            p-hydroxybenzoate hydrolyase;
            p-hydroxybenzoate hydroxylase;
            4-hydroxybenzoate 3-hydroxylase;
            4-hydroxybenzoate monooxygenase;
            4-hydroxybenzoic hydroxylase;
            p-hydroxybenzoate-3-hydroxylase;
            p-hydroxybenzoic acid hydrolase;
            p-hydroxybenzoic acid hydroxylase;
            p-hydroxybenzoic hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     4-hydroxybenzoate,NADPH:oxygen oxidoreductase (3-hydroxylating)
REACTION    4-hydroxybenzoate + NADPH + H+ + O2 = protocatechuate + NADP+ + H2O
            [RN:R01298]
ALL_REAC    R01298
SUBSTRATE   4-hydroxybenzoate [CPD:C00156];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     protocatechuate [CPD:C00230];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Most enzymes from Pseudomonas are highly
            specific for NADPH (cf. EC 1.14.13.33 4-hydroxybenzoate
            3-monooxygenase [NAD(P)H]).
REFERENCE   1  [PMID:4380381]
  AUTHORS   Hosokawa K, Stanier RY.
  TITLE     Crystallization and properties of p-hydroxybenzoate hydroxylase from
            Pseudomonas putida.
  JOURNAL   J. Biol. Chem. 241 (1966) 2453-60.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2  [PMID:4402514]
  AUTHORS   Howell LG, Spector T, Massey V.
  TITLE     Purification and properties of p-hydroxybenzoate hydroxylase from
            Pseudomonas fluorescens.
  JOURNAL   J. Biol. Chem. 247 (1972) 4340-50.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   3  [PMID:4402938]
  AUTHORS   Spector T, Massey V.
  TITLE     Studies on the effector specificity of p-hydroxybenzoate hydroxylase
            from Pseudomonas fluorescens.
  JOURNAL   J. Biol. Chem. 247 (1972) 4679-87.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   4  [PMID:4403446]
  AUTHORS   Spector T, Massey V.
  TITLE     p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Evidence
            for an oxygenated flavin intermediate.
  JOURNAL   J. Biol. Chem. 247 (1972) 5632-6.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   5  [PMID:4404745]
  AUTHORS   Spector T, Massey V.
  TITLE     p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens.
            Reactivity with oxygen.
  JOURNAL   J. Biol. Chem. 247 (1972) 7123-7.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   6  [PMID:8706756]
  AUTHORS   Seibold B, Matthes M, Eppink MH, Lingens F, Van Berkel WJ, Muller R.
  TITLE     4-Hydroxybenzoate hydroxylase from Pseudomonas sp. CBS3.
            Purification, characterization, gene cloning, sequence analysis and
            assignment of structural features determining the coenzyme
            specificity.
  JOURNAL   Eur. J. Biochem. 239 (1996) 469-78.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00623  2,4-Dichlorobenzoate degradation
ORTHOLOGY   KO: K00481  p-hydroxybenzoate 3-monooxygenase
GENES       SPE: Spro_2506
            XCC: XCC0356(pobA)
            XCB: XC_0368
            XCV: XCV0369(pobA)
            XAC: XAC0356(pobA)
            PAE: PA0247(pobA)
            PAU: PA14_03050(pobA)
            PAP: PSPA7_0332(pobA)
            PPU: PP_3537(pobA)
            PPF: Pput_2237
            PST: PSPTO_1907(pobA)
            PSB: Psyr_3500
            PSP: PSPPH_3432(pobA)
            PFL: PFL_5170(pobA)
            PFO: Pfl_4478
            PEN: PSEEN3048(pobA)
            ACI: ACIAD1719(pobA)
            PAT: Patl_3893
            CSA: Csal_0347
            MMW: Mmwyl1_0707
            RSO: RSc2242(pobB)
            REU: Reut_B4006 Reut_B5020
            REH: H16_B2286(pobA)
            RME: Rmet_4018 Rmet_5490
            BMV: BMASAVP1_1199(pobA)
            BML: BMA10299_1482(pobA)
            BMN: BMA10247_A0055(pobA)
            BXE: Bxe_A2040(pobB)
            BVI: Bcep1808_3744
            BUR: Bcep18194_B3130
            BCN: Bcen_5114
            BCH: Bcen2424_5745
            BAM: Bamb_5016
            BPS: BPSS0042(pobA)
            BPM: BURPS1710b_A1551(pobA)
            BPL: BURPS1106A_A0053(pobA)
            BPD: BURPS668_A0066(pobA)
            BTE: BTH_II0045
            RFR: Rfer_0339
            POL: Bpro_2992
            PNA: Pnap_1901
            VEI: Veis_2573
            AZO: azo2448(pobA)
            MLO: mlr7212
            MES: Meso_2573
            SME: SMb20583(pobA)
            SMD: Smed_4202
            ATU: Atu4544(pobA)
            ATC: AGR_L_646
            RET: RHE_CH03444(pobA)
            RLE: RL3905(pobA)
            BME: BMEII0640
            BMF: BAB2_0600(pobA) BAB2_0601
            BMS: BRA0641(pobA)
            BOV: BOV_A0603(pobA)
            OAN: Oant_3723
            BJA: bll7838(pobA) blr2337(pobA) blr6420(pobA)
            BRA: BRADO2352(phbH)
            BBT: BBta_2710(phbH)
            RPA: RPA1781(phbH)
            RPB: RPB_3583
            RPD: RPD_1884
            RPE: RPE_3808
            XAU: Xaut_2684
            CCR: CC_2404
            SIL: SPOA0046(pobA)
            SIT: TM1040_0561
            JAN: Jann_4161
            RDE: RD1_2336(pobA)
            PDE: Pden_3490
            NAR: Saro_2436
            ACR: Acry_1850
            MAG: amb0259
            SUS: Acid_0252
            BLI: BL03911
            BLD: BLi03989
            CGL: NCgl1032(cgl1077)
            CGB: cg1226(pobB)
            CEF: CE1133
            RHA: RHA1_ro02539
            SCO: SCO3084(pobA)
            SMA: SAV3517(pobA)
            ART: Arth_4043
            AAU: AAur_3979(pobA)
            SEN: SACE_0822(pobA) SACE_4035(pobA)
            RXY: Rxyl_1564
            DGE: Dgeo_2382
            HMA: rrnAC0359 rrnAC0657
STRUCTURES  PDB: 1BF3  1BGJ  1BGN  1BKW  1CC4  1CC6  1CJ2  1CJ3  1CJ4  1D7L  
                 1IUS  1IUT  1IUU  1IUV  1IUW  1IUX  1K0I  1K0J  1K0L  1PBB  
                 1PBC  1PBD  1PBE  1PBF  1PDH  1PHH  1PXA  1PXB  1PXC  1YKJ  
                 2PHH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.2
            ExPASy - ENZYME nomenclature database: 1.14.13.2
            ExplorEnz - The Enzyme Database: 1.14.13.2
            ERGO genome analysis and discovery system: 1.14.13.2
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.2
            BRENDA, the Enzyme Database: 1.14.13.2
            CAS: 9059-23-8
///
ENTRY       EC 1.14.13.3                Enzyme
NAME        4-hydroxyphenylacetate 3-monooxygenase;
            p-hydroxyphenylacetate 3-hydroxylase;
            4-hydroxyphenylacetic acid-3-hydroxylase;
            p-hydroxyphenylacetate hydroxylase;
            4 HPA 3-hydroxylase;
            p-hydroxyphenylacetate 3-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     4-hydroxyphenylacetate,NADH:oxygen oxidoreductase (3-hydroxylating)
REACTION    4-hydroxyphenylacetate + NADH + H+ + O2 = 3,4-dihydroxyphenylacetate
            + NAD+ + H2O [RN:R02698]
ALL_REAC    R02698;
            (other) R03299
SUBSTRATE   4-hydroxyphenylacetate [CPD:C00642];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     3,4-dihydroxyphenylacetate [CPD:C01161];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein.
REFERENCE   1  [PMID:14263147]
  AUTHORS   ADACHI K, TAKEDA Y, SENOH S, KITA H.
  TITLE     METABOLISM OF P-HYDROXYPHENYLACETIC ACID IN PSEUDOMONAS OVALIS.
  JOURNAL   Biochim. Biophys. Acta. 93 (1964) 483-93.
  ORGANISM  Pseudomonas ovalis
PATHWAY     PATH: map00350  Tyrosine metabolism
ORTHOLOGY   KO: K00482  4-hydroxyphenylacetate-3-hydroxylase
            KO: K00483  4-hydroxyphenylacetate-3-hydroxylase large chain
            KO: K00484  4-hydroxyphenylacetate-3-hydroxylase small chain
GENES       ECX: EcHS_A4575(hpaC) EcHS_A4576(hpaB)
            STY: STY1130(hpaC) STY1131(hpaB)
            STT: t1820(hpaB) t1821(hpaC)
            SPT: SPA1751(hpaB) SPA1752(hpaC)
            SEC: SC1048(hpaC) SC1049(hpaB)
            STM: STM1098(hpaC) STM1099(hpaB)
            YPE: YPO1769(hpaB) YPO1770(hpaC)
            YPK: y2538 y2539(hpaB)
            YPM: YP_1623(hpaC) YP_1624(hpaB)
            YPA: YPA_1141 YPA_1142
            YPN: YPN_2353 YPN_2354
            YPS: YPTB1645(hpaB) YPTB1646(hpaC)
            YPI: YpsIP31758_2356(hpaC) YpsIP31758_2357(hpaB)
            SFL: SF4373(hpaC) SF4374 SF4375
            SFX: S4643(hpaC)
            SFV: SFV_4374(hpaC)
            SSN: SSON_4488(hpaC) SSON_4489(hpaB)
            SBO: SBO_4403(hpaC) SBO_4404(hpaB)
            ECA: ECA2159(hpaC)
            PLU: plu0974(hpaC) plu0975(hpaB) plu4027 plu4258
            HDU: HD0987(hpaC)
            PMU: PM1522 PM1523
            APL: APL_1349(hpaC)
            VVY: VV1574
            PAE: PA2256(pvcC) PA4091(hpaA) PA4092(hpaC)
            PAU: PA14_10990(hpaC) PA14_11000(hpaA)
            PAP: PSPA7_1006(hpaC) PSPA7_1007(hpaB)
            PSB: Psyr_0995
            PSP: PSPPH_1044(hpaC)
            PFL: PFL_3356(hpaB) PFL_3357(hpaC)
            PFO: Pfl_0712
            PAR: Psyc_0847
            CPS: CPS_2047
            NME: NMB1842
            NMA: NMA0614
            NGO: NGO0059
            REU: Reut_A1584 Reut_A1585 Reut_B5770 Reut_C6314
            REH: H16_B0496
            BMA: BMAA0045(pobA) BMAA1922(pvcC)
            BXE: Bxe_B2309
            BUR: Bcep18194_B2506
            BCH: Bcen2424_3609
            BPS: BPSS0162
            BPM: BURPS1710b_A1403 BURPS1710b_A1681(pvcC)
            BTE: BTH_II0231(pvcC) BTH_II0316(hpaC)
            MPT: Mpe_A2516
            AZO: azo1943(hpaC)
            DAR: Daro_0903
            GME: Gmet_2215
            MLO: mlr0087
            MES: Meso_2465
            SME: SMc00514
            RET: RHE_CH02268
            RLE: pRL100364 pRL120218
            BME: BMEI0709
            BMS: BR1292
            BJA: blr3324 blr7290(hpaC)
            RPA: RPA2609
            RPE: RPE_3196
            NWI: Nwi_0686
            BHE: BH09670(nmoB)
            BQU: BQ07430(nmoB)
            RSP: RSP_3957
            BHA: BH3836
            BCA: BCE_2148 BCE_2601
            BCL: ABC0890
            OIH: OB2872
            GKA: GK2138 GK3034
            LPL: lp_0070
            CHY: CHY_1730
            DSY: DSY4732
            NFA: nfa20870 nfa28410 nfa30560
            RHA: RHA1_ro01782 RHA1_ro02514(pheA1) RHA1_ro03853 RHA1_ro03872
            FRA: Francci3_2770
            SEN: SACE_4928
            DRA: DR_A0223
            DGE: Dgeo_2418
            TTH: TTC0594
            TTJ: TTHA0960 TTHB249
            AFU: AF0333(hpaA-1) AF0885(hpaA-2) AF1027(hpaA-3)
            SSO: SSO2053(hpaA) SSO2738(abfD-2)
            STO: ST0726 ST1659
            SAI: Saci_2143(abfD) Saci_2294(hpaA)
            PAI: PAE2693
STRUCTURES  PDB: 2YYG  2YYI  2YYJ  2YYK  2YYL  2YYM  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.3
            ExPASy - ENZYME nomenclature database: 1.14.13.3
            ExplorEnz - The Enzyme Database: 1.14.13.3
            ERGO genome analysis and discovery system: 1.14.13.3
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.3
            BRENDA, the Enzyme Database: 1.14.13.3
            CAS: 37256-71-6
///
ENTRY       EC 1.14.13.4                Enzyme
NAME        melilotate 3-monooxygenase;
            2-hydroxyphenylpropionate hydroxylase;
            melilotate hydroxylase;
            2-hydroxyphenylpropionic hydroxylase;
            melilotic hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     3-(2-hydroxyphenyl)propanoate,NADH:oxygen oxidoreductase
            (3-hydroxylating)
REACTION    3-(2-hydroxyphenyl)propanoate + NADH + H+ + O2 =
            3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O [RN:R03369]
ALL_REAC    R03369
SUBSTRATE   3-(2-hydroxyphenyl)propanoate [CPD:C01198];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     3-(2,3-dihydroxyphenyl)propanoate [CPD:C04044];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:6017743]
  AUTHORS   Levy CC.
  TITLE     Melilotate hydroxylase. Purification of the enzyme and the nature of
            the prosthetic group.
  JOURNAL   J. Biol. Chem. 242 (1967) 747-53.
  ORGANISM  Arthrobacter sp.
REFERENCE   2  [PMID:4285850]
  AUTHORS   Levy CC, Frost P.
  TITLE     The metabolism of coumarin by a microorganism. V. Melilotate
            hydroxylase.
  JOURNAL   J. Biol. Chem. 241 (1966) 997-1003.
  ORGANISM  Arthrobacter sp.
REFERENCE   3  [PMID:4348920]
  AUTHORS   Strickland S, Massey V.
  TITLE     The purification and properties of the flavoprotein melilotate
            hydroxylase.
  JOURNAL   J. Biol. Chem. 248 (1973) 2944-52.
  ORGANISM  Pseudomonas sp.
REFERENCE   4  [PMID:4348921]
  AUTHORS   Strickland S, Massey V.
  TITLE     The mechanism of action of the flavoprotein melilotate hydroxylase.
  JOURNAL   J. Biol. Chem. 248 (1973) 2953-62.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00360  Phenylalanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.4
            ExPASy - ENZYME nomenclature database: 1.14.13.4
            ExplorEnz - The Enzyme Database: 1.14.13.4
            ERGO genome analysis and discovery system: 1.14.13.4
            BRENDA, the Enzyme Database: 1.14.13.4
            CAS: 37256-72-7
///
ENTRY       EC 1.14.13.5                Enzyme
NAME        imidazoleacetate 4-monooxygenase;
            imidazoleacetic hydroxylase;
            imidazoleacetate hydroxylase;
            imidazoleacetic monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     4-imidazoleacetate,NADH:oxygen oxidoreductase (5-hydroxylating)
REACTION    4-imidazoleacetate + NADH + H+ + O2 = 5-hydroxy-4-imidazoleacetate +
            NAD+ + H2O [RN:R04066]
ALL_REAC    R04066
SUBSTRATE   4-imidazoleacetate [CPD:C02835];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     5-hydroxy-4-imidazoleacetate [CPD:C05133];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:5772468]
  AUTHORS   Maki Y, Yamamoto S, Nozaki M, Hayaishi O.
  TITLE     Studies on monooxygenases. II. Crystallization and some properties
            of imidazole acetate monooxygenase.
  JOURNAL   J. Biol. Chem. 244 (1969) 2942-50.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00340  Histidine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.5
            ExPASy - ENZYME nomenclature database: 1.14.13.5
            ExplorEnz - The Enzyme Database: 1.14.13.5
            ERGO genome analysis and discovery system: 1.14.13.5
            BRENDA, the Enzyme Database: 1.14.13.5
            CAS: 9029-65-6
///
ENTRY       EC 1.14.13.6                Enzyme
NAME        orcinol 2-monooxygenase;
            orcinol hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     orcinol,NADH:oxygen oxidoreductase (2-hydroxylating)
REACTION    orcinol + NADH + H+ + O2 = 2,3,5-trihydroxytoluene + NAD+ + H2O
            [RN:R02830]
ALL_REAC    R02830
SUBSTRATE   orcinol [CPD:C00727];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     2,3,5-trihydroxytoluene [CPD:C03338];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:11945483]
  AUTHORS   Otha Y, Ribbons DW.
  TITLE     Crystallization of orcinol hydroxylase from Pseudomonas putida.
  JOURNAL   FEBS. Lett. 11 (1970) 189-192.
  ORGANISM  Pseudomonas putida [GN:ppu]
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.6
            ExPASy - ENZYME nomenclature database: 1.14.13.6
            ExplorEnz - The Enzyme Database: 1.14.13.6
            ERGO genome analysis and discovery system: 1.14.13.6
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.6
            BRENDA, the Enzyme Database: 1.14.13.6
            CAS: 37217-34-8
///
ENTRY       EC 1.14.13.7                Enzyme
NAME        phenol 2-monooxygenase;
            phenol hydroxylase;
            phenol o-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     phenol,NADPH:oxygen oxidoreductase (2-hydroxylating)
REACTION    phenol + NADPH + H+ + O2 = catechol + NADP+ + H2O [RN:R00815]
ALL_REAC    R00815;
            (other) R03560 R03562 R03566 R03568 R03608 R05249
SUBSTRATE   phenol [CPD:C00146];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     catechol [CPD:C00090];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Also active with resorcinol and o-cresol.
REFERENCE   1  [PMID:14478080]
  AUTHORS   NAKAGAWA H, TAKEDA Y.
  TITLE     Phenol hydroxylase.
  JOURNAL   Biochim. Biophys. Acta. 62 (1962) 423-6.
  ORGANISM  Brevibacterium fuscum
REFERENCE   2  [PMID:4146224]
  AUTHORS   Neujahr HY, Gaal A.
  TITLE     Phenol hydroxylase from yeast. Purification and properties of the
            enzyme from Trichosporon cutaneum.
  JOURNAL   Eur. J. Biochem. 35 (1973) 386-400.
  ORGANISM  Trichosporon cutaneum
REFERENCE   3  [PMID:810352]
  AUTHORS   Neujahr HY, Gaal A.
  TITLE     Phenol hydroxylase from yeast. Sulfhydryl groups in phenol
            hydroxylase from Trichosporon cutaneum.
  JOURNAL   Eur. J. Biochem. 58 (1975) 351-7.
  ORGANISM  Trichosporon cutaneum
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
            PATH: map00622  Toluene and xylene degradation
            PATH: map00626  Naphthalene and anthracene degradation
ORTHOLOGY   KO: K03380  phenol 2-monooxygenase
GENES       PIC: PICST_57166(PHH2)
            AFM: AFUA_1G13660 AFUA_3G02620
            XCC: XCC3977(poxF)
            XCB: XC_4067
            XCV: XCV4151
            XAC: XAC4066(poxF)
            XOO: XOO0382(poxF)
            XOM: XOO_0344(XOO0344)
            VFI: VF0061
            LPN: lpg0471(poxF)
            LPF: lpl0512
            LPP: lpp0536
            FTU: FTT0365(poxF)
            FTF: FTF0365(poxF)
            FTW: FTW_1699(poxF)
            FTL: FTL_1302
            FTH: FTH_1274(poxF)
            FTN: FTN_0279
            REH: H16_B0539(poxA) H16_B0540(poxB) H16_B0541(poxC)
                 H16_B0542(poxD) H16_B0543(poxE) H16_B0544(poxF)
            BUR: Bcep18194_B2966
            AZO: azo1222(dmpM) azo1845(lapK) azo1850(lapP) azo2439(poxF)
            BBA: Bd2437
            BJA: blr4222
            BBT: BBta_1594 BBta_1595 BBta_1596 BBta_1597
            ABA: Acid345_0992
            CGL: NCgl2588(cgl2681)
            NFA: nfa22280
            RHA: RHA1_ro02379 RHA1_ro02380 RHA1_ro08076 RHA1_ro08077
STRUCTURES  PDB: 1FOH  1HQI  1PN0  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.7
            ExPASy - ENZYME nomenclature database: 1.14.13.7
            ExplorEnz - The Enzyme Database: 1.14.13.7
            ERGO genome analysis and discovery system: 1.14.13.7
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.7
            BRENDA, the Enzyme Database: 1.14.13.7
            CAS: 37256-84-1
///
ENTRY       EC 1.14.13.8                Enzyme
NAME        flavin-containing monooxygenase;
            dimethylaniline oxidase;
            dimethylaniline N-oxidase;
            FAD-containing monooxygenase;
            N,N-dimethylaniline monooxygenase;
            DMA oxidase;
            flavin mixed function oxidase;
            Ziegler's enzyme;
            mixed-function amine oxidase;
            FMO;
            FMO-I;
            FMO-II;
            FMO1;
            FMO2;
            FMO3;
            FMO4;
            FMO5;
            flavin monooxygenase;
            methylphenyltetrahydropyridine N-monooxygenase;
            1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine:oxygen
            N-oxidoreductase;
            dimethylaniline monooxygenase (N-oxide-forming)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     N,N-dimethylaniline,NADPH:oxygen oxidoreductase (N-oxide-forming)
REACTION    N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide
            + NADP+ + H2O [RN:R03344]
ALL_REAC    R03344;
            (other) R04523
SUBSTRATE   N,N-dimethylaniline [CPD:C02846];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     N,N-dimethylaniline N-oxide [CPD:C01183];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016];
            Flavin [CPD:C00176]
COMMENT     A flavoprotein. A broad spectrum monooxygenase that accepts
            substrates as diverse as hydrazines, phosphines, boron-containing
            compounds, sulfides, selenides, iodide, as well as primary,
            secondary and tertiary amines [3,4]. This enzyme is distinct from
            other monooxygenases in that the enzyme forms a relatively stable
            hydroperoxy flavin intermediate [4,5]. This microsomal enzyme
            generally converts nucleophilic heteroatom-containing chemicals and
            drugs into harmless, readily excreted metabolites. For example,
            N-oxygenation is largely responsible for the detoxification of the
            dopaminergic neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
            (MPTP) [2,6]
REFERENCE   1  [PMID:4381353]
  AUTHORS   Ziegler DM, Pettit FH.
  TITLE     Microsomal oxidases. I. The isolation and dialkylarylamine oxygenase
            activity of pork liver microsomes.
  JOURNAL   Biochemistry. 5 (1966) 2932-8.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:3262153]
  AUTHORS   Chiba K, Kubota E, Miyakawa T, Kato Y, Ishizaki T.
  TITLE     Characterization of hepatic microsomal metabolism as an in vivo
            detoxication pathway of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
            in mice.
  JOURNAL   J. Pharmacol. Exp. Ther. 246 (1988) 1108-15.
REFERENCE   3
  AUTHORS   Cashman, J.R.
  TITLE     Structural and catalytic properties of the mammalian
            flavin-containing monooxygenase.
  JOURNAL   Chem. Res. Toxicol. 8 (1995) 165-181.
REFERENCE   4  [PMID:16402899]
  AUTHORS   Cashman JR, Zhang J.
  TITLE     Human flavin-containing monooxygenases.
  JOURNAL   Annu. Rev. Pharmacol. Toxicol. 46 (2006) 65-100.
REFERENCE   5  [PMID:3949735]
  AUTHORS   Jones KC, Ballou DP.
  TITLE     Reactions of the 4a-hydroperoxide of liver microsomal
            flavin-containing monooxygenase with nucleophilic and electrophilic
            substrates.
  JOURNAL   J. Biol. Chem. 261 (1986) 2553-9.
REFERENCE   6  [PMID:7672012]
  AUTHORS   Chiba K, Kobayashi K, Itoh K, Itoh S, Chiba T, Ishizaki T, Kamataki
            T.
  TITLE     N-oxygenation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine by the
            rat liver flavin-containing monooxygenase expressed in yeast cells.
  JOURNAL   Eur. J. Pharmacol. 293 (1995) 97-100.
ORTHOLOGY   KO: K00485  dimethylaniline monooxygenase (N-oxide forming)
GENES       HSA: 2326(FMO1) 2327(FMO2) 2328(FMO3) 2329(FMO4) 2330(FMO5)
            PTR: 449587(FMO2)
            MCC: 703639(FMO2)
            MMU: 14261(Fmo1) 14262(Fmo3) 14263(Fmo5) 226564(Fmo4) 55990(Fmo2)
            RNO: 246245(Fmo2) 246247(Fmo4) 246248(Fmo5) 25256(Fmo1)
                 84493(Fmo3)
            CFA: 403603(FMO3) 403604(FMO1) 475819(FMO5) 480076(FMO2)
                 490345(FMO4)
            BTA: 281167(FMO3)
            SSC: 397132(FMO1)
            GGA: 395267(FMO6) 770587(FMO4)
            XLA: 398813(MGC68633)
            DRE: 334666(fmo5)
            SPU: 580981(LOC580981)
            DME: Dmel_CG3006(Fmo-1) Dmel_CG3174(Fmo-2)
            CEL: H24K24.5(fmo-5) K08C7.2(fmo-1) K08C7.5(fmo-2)
                 Y39A1A.19(fmo-3)
            ATH: AT1G12200
            PIC: PICST_30092(FMO6) PICST_32260(FMO2) PICST_66263(FMO1)
            UMA: UM03429.1
            TET: TTHERM_00052340 TTHERM_00448990 TTHERM_01004950
            XCV: XCV2088(pedG)
            PMY: Pmen_2142 Pmen_3459
            PHA: PSHAa1699
            CSA: Csal_1416
            MMW: Mmwyl1_4167
            HAR: HEAR2456
            PLA: Plav_0443 Plav_0603
            RET: RHE_PE00411
            RLE: pRL110548
            BRA: BRADO5772
            BBT: BBta_6282
            RDE: RD1_0632
            NAR: Saro_1820
            SWI: Swit_3885
            GBE: GbCGDNIH1_1825
            MSM: MSMEG_2202
            MVA: Mvan_1971
            MGI: Mflv_4373 Mflv_5135
            MMC: Mmcs_1752
            MKM: Mkms_1799
            MJL: Mjls_1733
            CGB: cg1292
            RHA: RHA1_ro00740 RHA1_ro05696
            TER: Tery_3826
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.8
            ExPASy - ENZYME nomenclature database: 1.14.13.8
            ExplorEnz - The Enzyme Database: 1.14.13.8
            ERGO genome analysis and discovery system: 1.14.13.8
            BRENDA, the Enzyme Database: 1.14.13.8
            CAS: 37256-73-8
///
ENTRY       EC 1.14.13.9                Enzyme
NAME        kynurenine 3-monooxygenase;
            kynurenine 3-hydroxylase;
            kynurenine hydroxylase;
            L-kynurenine-3-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     L-kynurenine,NADPH:oxygen oxidoreductase (3-hydroxylating)
REACTION    L-kynurenine + NADPH + H+ + O2 = 3-hydroxy-L-kynurenine + NADP+ +
            H2O [RN:R01960]
ALL_REAC    R01960
SUBSTRATE   L-kynurenine [CPD:C00328];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     3-hydroxy-L-kynurenine [CPD:C03227];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:16526094]
  AUTHORS   Foucher AL, McIntosh A, Douce G, Wastling J, Tait A, Turner CM.
  TITLE     A proteomic analysis of arsenical drug resistance in Trypanosoma
            brucei.
  JOURNAL   Proteomics. 6 (2006) 2726-32.
REFERENCE   2  [PMID:6076241]
  AUTHORS   Okamoto H, Hayaishi O.
  TITLE     Flavin adenine dinucleotide requirement for kynurenine hydroxylase
            of rat liver mitochondria.
  JOURNAL   Biochem. Biophys. Res. Commun. 29 (1967) 394-9.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:13502353]
  AUTHORS   SAITO Y, HAYAISHI O, ROTHBERG S.
  TITLE     Studies on oxygenases; enzymatic formation of 3-hydroxy-L-kynurenine
            from L-kynurenine.
  JOURNAL   J. Biol. Chem. 229 (1957) 921-34.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00380  Tryptophan metabolism
ORTHOLOGY   KO: K00486  kynurenine 3-monooxygenase
GENES       HSA: 8564(KMO)
            PTR: 469730(KMO)
            MMU: 98256(Kmo)
            RNO: 59113(Kmo)
            CFA: 480093(KMO)
            SSC: 397148(KMO)
            GGA: 424041(KMO)
            XTR: 448312(kmo)
            SPU: 592365(LOC592365)
            DME: Dmel_CG1555(cn)
            CEL: R07B7.5(Monooxygenase)
            PIC: PICST_40545(BNA4)
            CAL: CaO19_5443(CaO19.5443)
            UMA: UM06333.1
            DDI: DDB_0231360(kmo)
            XCC: XCC1552
            XCB: XC_2682
            XCV: XCV1641
            XAC: XAC1600
            XOO: XOO2429
            XOM: XOO_2306(XOO2306)
            CPS: CPS_3582
            LPN: lpg0892
            LPF: lpl0923
            LPP: lpp0953
            MXA: MXAN_0916
            STP: Strop_3529 Strop_4419
            CHU: CHU_3380
            FJO: Fjoh_0495
            FPS: FP2212(kmo)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.9
            ExPASy - ENZYME nomenclature database: 1.14.13.9
            ExplorEnz - The Enzyme Database: 1.14.13.9
            ERGO genome analysis and discovery system: 1.14.13.9
            BRENDA, the Enzyme Database: 1.14.13.9
            CAS: 9029-61-2
///
ENTRY       EC 1.14.13.10               Enzyme
NAME        2,6-dihydroxypyridine 3-monooxygenase;
            2,6-dihydroxypyridine oxidase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     2,6-dihydroxypyridine,NADH:oxygen oxidoreductase (3-hydroxylating)
REACTION    2,6-dihydroxypyridine + NADH + H+ + O2 = 2,3,6-trihydroxypyridine +
            NAD+ + H2O [RN:R04130]
ALL_REAC    R04130
SUBSTRATE   2,6-dihydroxypyridine [CPD:C03056];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     2,3,6-trihydroxypyridine [CPD:C03458];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016];
            Flavoprotein [CPD:C06411]
COMMENT     A flavoprotein.
REFERENCE   1  [PMID:4344227]
  AUTHORS   Holmes PE, Rittenberg SC.
  TITLE     The bacterial oxidation of nicotine. VII. Partial purification and
            properties of 2,6-dihydroxypyridine oxidase.
  JOURNAL   J. Biol. Chem. 247 (1972) 7622-7.
  ORGANISM  Arthrobacter oxydans
REFERENCE   2  [PMID:4636328]
  AUTHORS   Holmes PE, Rittenberg SC, Knackmuss HJ.
  TITLE     The bacterial oxidation of nicotine. 8. Synthesis of
            2,3,6-trihydroxypyridine and accumulation and partial
            characterization of the product of 2,6-dihydroxypyridine oxidation.
  JOURNAL   J. Biol. Chem. 247 (1972) 7628-33.
  ORGANISM  Arthrobacter oxydans
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.10
            ExPASy - ENZYME nomenclature database: 1.14.13.10
            ExplorEnz - The Enzyme Database: 1.14.13.10
            ERGO genome analysis and discovery system: 1.14.13.10
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.10
            BRENDA, the Enzyme Database: 1.14.13.10
            CAS: 39279-38-4
///
ENTRY       EC 1.14.13.11               Enzyme
NAME        trans-cinnamate 4-monooxygenase;
            cinnamic acid 4-hydroxylase;
            oxygenase, cinnamate 4-mono-;
            CA4H ;
            cytochrome P450 cinnamate 4-hydroxylase;
            cinnamate 4-hydroxylase;
            cinnamate 4-monooxygenase;
            cinnamate hydroxylase;
            cinnamic 4-hydroxylase;
            cinnamic acid 4-monooxygenase;
            cinnamic acid p-hydroxylase;
            hydroxylase, cinnamate 4-;
            t-cinnamic acid hydroxylase;
            trans-cinnamate 4-hydroxylase;
            trans-cinnamic acid 4-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     trans-cinnamate,NADPH:oxygen oxidoreductase (4-hydroxylating)
REACTION    trans-cinnamate + NADPH + H+ + O2 = 4-hydroxycinnamate + NADP+ + H2O
            [RN:R02253]
ALL_REAC    R02253
SUBSTRATE   trans-cinnamate [CPD:C00423];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     4-hydroxycinnamate [CPD:C00811];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     NADH also acts, more slowly. Involves a heme-thiolate protein
            (P-450).
REFERENCE   1  [PMID:4153152]
  AUTHORS   Potts JR, Weklych R, Conn EE, Rowell J.
  TITLE     The 4-hydroxylation of cinnamic acid by sorghum microsomes and the
            requirement for cytochrome P-450.
  JOURNAL   J. Biol. Chem. 249 (1974) 5019-26.
  ORGANISM  Sorghum sp.
REFERENCE   2  [PMID:4383827]
  AUTHORS   Russell DW, Conn EE.
  TITLE     The cinnamic acid 4-hydroxylase of pea seedlings.
  JOURNAL   Arch. Biochem. Biophys. 122 (1967) 256-8.
  ORGANISM  Pisum sativum
PATHWAY     PATH: map00360  Phenylalanine metabolism
            PATH: map00940  Phenylpropanoid biosynthesis
ORTHOLOGY   KO: K00487  trans-cinnamate-4-hydroxylase
GENES       OSA: 4338409
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.11
            ExPASy - ENZYME nomenclature database: 1.14.13.11
            ExplorEnz - The Enzyme Database: 1.14.13.11
            ERGO genome analysis and discovery system: 1.14.13.11
            BRENDA, the Enzyme Database: 1.14.13.11
            CAS: 9077-75-2
///
ENTRY       EC 1.14.13.12               Enzyme
NAME        benzoate 4-monooxygenase;
            benzoic acid 4-hydroxylase;
            benzoate 4-hydroxylase;
            benzoic 4-hydroxylase;
            benzoate-p-hydroxylase;
            p-hydroxybenzoate hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     benzoate,NADPH:oxygen oxidoreductase (4-hydroxylating)
REACTION    benzoate + NADPH + H+ + O2 = 4-hydroxybenzoate + NADP+ + H2O
            [RN:R01295]
ALL_REAC    R01295
SUBSTRATE   benzoate [CPD:C00180];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     4-hydroxybenzoate [CPD:C00156];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023];
            Tetrahydrobiopterin [CPD:C00272];
            Tetrahydropteridine [CPD:C05650]
COMMENT     Requires Fe2+ and tetrahydropteridine.
REFERENCE   1  [PMID:236777]
  AUTHORS   Reddy CC, Vaidyanathan CS.
  TITLE     Purification, properties and induction of a specific
            benzoate-4-hydroxylase from Aspergillus niger (UBC 814).
  JOURNAL   Biochim. Biophys. Acta. 384 (1975) 46-57.
  ORGANISM  Aspergillus niger
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00632  Benzoate degradation via CoA ligation
ORTHOLOGY   KO: K07824  benzoate 4-monooxygenase
GENES       AFM: AFUA_2G15230
            ANG: An09g03500(bphA)
            BUR: Bcep18194_C7583
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.12
            ExPASy - ENZYME nomenclature database: 1.14.13.12
            ExplorEnz - The Enzyme Database: 1.14.13.12
            ERGO genome analysis and discovery system: 1.14.13.12
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.12
            BRENDA, the Enzyme Database: 1.14.13.12
            CAS: 39391-25-8
///
ENTRY       EC 1.14.13.13               Enzyme
NAME        calcidiol 1-monooxygenase;
            25-hydroxycholecalciferol 1-hydroxylase;
            25-hydroxycholecalciferol 1-monooxygenase;
            1-hydroxylase-25-hydroxyvitamin D3;
            25-hydroxy D3-1alpha-hydroxylase;
            25-hydroxycholecalciferol 1alpha-hydroxylase;
            25-hydroxyvitamin D3 1alpha-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     calcidiol,NADPH:oxygen oxidoreductase (1-hydroxylating)
REACTION    calcidiol + NADPH + H+ + O2 = calcitriol + NADP+ + H2O [RN:R03610]
ALL_REAC    R03610
SUBSTRATE   calcidiol [CPD:C01561];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     calcitriol [CPD:C01673];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:4404596]
  AUTHORS   Gray RW, Omdahl JL, Ghazarian JG, DeLuca HF.
  TITLE     25-Hydroxycholecalciferol-1-hydroxylase. Subcellular location and
            properties.
  JOURNAL   J. Biol. Chem. 247 (1972) 7528-32.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K07438  cytochrome P450, family 27, subfamily B
                        (25-hydroxyvitamin D3 1alpha-hydroxylase)
GENES       HSA: 1594(CYP27B1)
            MMU: 13115(Cyp27b1)
            RNO: 114700(Cyp27b1)
            CFA: 481133(LOC481133)
            SSC: 397055(CYP27B1)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.13
            ExPASy - ENZYME nomenclature database: 1.14.13.13
            ExplorEnz - The Enzyme Database: 1.14.13.13
            ERGO genome analysis and discovery system: 1.14.13.13
            BRENDA, the Enzyme Database: 1.14.13.13
            CAS: 9081-36-1
///
ENTRY       EC 1.14.13.14               Enzyme
NAME        trans-cinnamate 2-monooxygenase;
            cinnamic acid 2-hydroxylase;
            cinnamate 2-monooxygenase;
            cinnamic 2-hydroxylase;
            cinnamate 2-hydroxylase;
            trans-cinnamic acid 2-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     trans-cinnamate,NADPH:oxygen oxidoreductase (2-hydroxylating)
REACTION    trans-cinnamate + NADPH + H+ + O2 = 2-hydroxycinnamate + NADP+ + H2O
            [RN:R07189]
ALL_REAC    R07189 > R02254
SUBSTRATE   trans-cinnamate [CPD:C00423];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     2-hydroxycinnamate [CPD:C03549];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:4153528]
  AUTHORS   Gestetner B, Conn EE.
  TITLE     The 2-hydroxylation of trans-cinnamic acid by chloroplasts from
            Melilotus alba Desr.
  JOURNAL   Arch. Biochem. Biophys. 163 (1974) 617-24.
  ORGANISM  Melilotus alba Desr
PATHWAY     PATH: map00360  Phenylalanine metabolism
            PATH: map00940  Phenylpropanoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.14
            ExPASy - ENZYME nomenclature database: 1.14.13.14
            ExplorEnz - The Enzyme Database: 1.14.13.14
            ERGO genome analysis and discovery system: 1.14.13.14
            BRENDA, the Enzyme Database: 1.14.13.14
            CAS: 53126-56-0
///
ENTRY       EC 1.14.13.15               Enzyme
NAME        cholestanetriol 26-monooxygenase;
            5beta-cholestane-3alpha,7alpha,12alpha-triol 26-hydroxylase;
            5beta-cholestane-3alpha,7alpha,12alpha-triol hydroxylase;
            cholestanetriol 26-hydroxylase;
            sterol 27-hydroxylase;
            sterol 26-hydroxylase;
            cholesterol 27-hydroxylase;
            CYP27A;
            CYP27A1;
            cytochrome P450 27A1'
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     5beta-cholestane-3alpha,7alpha,12alpha-triol,NADPH:oxygen
            oxidoreductase (26-hydroxylating)
REACTION    5beta-cholestane-3alpha,7alpha,12alpha-triol + NADPH + H+ + O2 =
            (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + NADP+ +
            H2O [RN:R04807]
ALL_REAC    R04807;
            (other) R04806
SUBSTRATE   5beta-cholestane-3alpha,7alpha,12alpha-triol [CPD:C05454];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol;
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     Requires ferrodoxin. Acts on cholesterol,
            cholest-5-en-3beta,7alpha-diol, 7alpha-hydroxycholest-4-en-3-one,
            5beta-cholestane-3alpha,7alpha-diol as well as
            5beta-cholestane-3alpha,7alpha,12alpha-triol. With cholesterol as
            well as 26-hydroxycholesterol, 24-hydroxy- and 25-hydroxycholesterol
            are also formed. With prolonged treatment, 26-hydroxycholesterol is
            converted into the corresponding 27-aldehyde and 27-oic acid.
REFERENCE   1  [PMID:4388637]
  AUTHORS   Okuda K, Hoshita N.
  TITLE     Oxidation of 5-beta-cholestane-3 alpha, 7 alpha, 12 alpha-triol by
            rat-liver mitochondria.
  JOURNAL   Biochim. Biophys. Acta. 164 (1968) 381-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6423637]
  AUTHORS   Wikvall K.
  TITLE     Hydroxylations in biosynthesis of bile acids. Isolation of a
            cytochrome P-450 from rabbit liver mitochondria catalyzing
            26-hydroxylation of C27-steroids.
  JOURNAL   J. Biol. Chem. 259 (1984) 3800-4.
  ORGANISM  rabbit
REFERENCE   3  [PMID:2722778]
  AUTHORS   Andersson S, Davis DL, Dahlback H, Jornvall H, Russell DW.
  TITLE     Cloning, structure, and expression of the mitochondrial cytochrome
            P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme.
  JOURNAL   J. Biol. Chem. 264 (1989) 8222-9.
  ORGANISM  rabbit
REFERENCE   4  [PMID:2318307]
  AUTHORS   Usui E, Noshiro M, Okuda K.
  TITLE     Molecular cloning of cDNA for vitamin D3 25-hydroxylase from rat
            liver mitochondria.
  JOURNAL   FEBS. Lett. 262 (1990) 135-8.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:10512735]
  AUTHORS   Furster C, Bergman T, Wikvall K.
  TITLE     Biochemical characterization of a truncated form of CYP27A purified
            from rabbit liver mitochondria.
  JOURNAL   Biochem. Biophys. Res. Commun. 263 (1999) 663-6.
  ORGANISM  rabbit
REFERENCE   6  [PMID:8496170]
  AUTHORS   Holmberg-Betsholtz I, Lund E, Bjorkhem I, Wikvall K.
  TITLE     Sterol 27-hydroxylase in bile acid biosynthesis. Mechanism of
            oxidation of 5 beta-cholestane-3 alpha,7 alpha,12 alpha,27-tetrol
            into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid.
  JOURNAL   J. Biol. Chem. 268 (1993) 11079-85.
  ORGANISM  rabbit
REFERENCE   7  [PMID:11412116]
  AUTHORS   Pikuleva IA, Puchkaev A, Bjorkhem I.
  TITLE     Putative helix F contributes to regioselectivity of hydroxylation in
            mitochondrial cytochrome P450 27A1.
  JOURNAL   Biochemistry. 40 (2001) 7621-9.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00120  Bile acid biosynthesis
            PATH: map03320  PPAR signaling pathway
ORTHOLOGY   KO: K00488  cytochrome P450, family 27, subfamily A (cholestanetriol
                        26-monooxygenase)
GENES       HSA: 1593(CYP27A1)
            MMU: 104086(Cyp27a1)
            RNO: 301517(Cyp27a1)
            CFA: 610489(LOC610489)
            GGA: 431683(CYP27A1)
            XLA: 446987(cyp27a1)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.15
            ExPASy - ENZYME nomenclature database: 1.14.13.15
            ExplorEnz - The Enzyme Database: 1.14.13.15
            ERGO genome analysis and discovery system: 1.14.13.15
            BRENDA, the Enzyme Database: 1.14.13.15
            CAS: 52227-77-7
///
ENTRY       EC 1.14.13.16               Enzyme
NAME        cyclopentanone monooxygenase;
            cyclopentanone oxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     cyclopentanone,NADPH:oxygen oxidoreductase (5-hydroxylating,
            lactonizing)
REACTION    cyclopentanone + NADPH + H+ + O2 = 5-valerolactone + NADP+ + H2O
            [RN:R02554]
ALL_REAC    R02554
SUBSTRATE   cyclopentanone [CPD:C00557];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     5-valerolactone [CPD:C02240];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:4349113]
  AUTHORS   Griffin M, Trudgill PW.
  TITLE     The metabolism of cyclopentanol by Pseudomonas N.C.I.B. 9872.
  JOURNAL   Biochem. J. 129 (1972) 595-603.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:4313]
  AUTHORS   Griffin M, Trudgill PW.
  TITLE     Purification and properties of cyclopentanone oxygenase of
            Pseudomonas NCIB 9872.
  JOURNAL   Eur. J. Biochem. 63 (1976) 199-209.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.16
            ExPASy - ENZYME nomenclature database: 1.14.13.16
            ExplorEnz - The Enzyme Database: 1.14.13.16
            ERGO genome analysis and discovery system: 1.14.13.16
            BRENDA, the Enzyme Database: 1.14.13.16
            CAS: 37364-15-1
///
ENTRY       EC 1.14.13.17               Enzyme
NAME        cholesterol 7alpha-monooxygenase;
            cholesterol 7alpha-hydroxylase;
            CYP7A1
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     cholesterol,NADPH:oxygen oxidoreductase (7alpha-hydroxylating)
REACTION    cholesterol + NADPH + H+ + O2 = 7alpha-hydroxycholesterol + NADP+ +
            H2O [RN:R01463]
ALL_REAC    R01463
SUBSTRATE   cholesterol [CPD:C00187];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     7alpha-hydroxycholesterol [CPD:C03594];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A heme-thiolate protein (P-450).
REFERENCE   1  [PMID:4147676]
  AUTHORS   Boyd GS, Grimwade AM, Lawson ME.
  TITLE     Studies on rat-liver microsomal cholesterol 7alpha-hydroxylase.
  JOURNAL   Eur. J. Biochem. 37 (1973) 334-40.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4397276]
  AUTHORS   Mitton JR, Scholan NA, Boyd GS.
  TITLE     The oxidation of cholesterol in rat liver sub-cellular particles.
            The cholesterol-7-alpha-Hydroxylase enzyme system.
  JOURNAL   Eur. J. Biochem. 20 (1971) 569-79.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:3584134]
  AUTHORS   Ogishima T, Deguchi S, Okuda K.
  TITLE     Purification and characterization of cholesterol 7 alpha-hydroxylase
            from rat liver microsomes.
  JOURNAL   J. Biol. Chem. 262 (1987) 7646-50.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00120  Bile acid biosynthesis
            PATH: map03320  PPAR signaling pathway
ORTHOLOGY   KO: K00489  cytochrome P450, family 7, subfamily A (cholesterol
                        7alpha-monooxygenase)
GENES       HSA: 1581(CYP7A1)
            PTR: 464191(CYP7A1)
            MMU: 13122(Cyp7a1)
            RNO: 25428(Cyp7a1)
            CFA: 486962(LOC486962)
            BTA: 510507(LOC510507)
            SSC: 448985(CYP7)
            GGA: 414834(CYP7A1)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.17
            ExPASy - ENZYME nomenclature database: 1.14.13.17
            ExplorEnz - The Enzyme Database: 1.14.13.17
            ERGO genome analysis and discovery system: 1.14.13.17
            BRENDA, the Enzyme Database: 1.14.13.17
            CAS: 9037-53-0
///
ENTRY       EC 1.14.13.18               Enzyme
NAME        4-hydroxyphenylacetate 1-monooxygenase;
            4-hydroxyphenylacetate 1-hydroxylase;
            4-hydroxyphenylacetic 1-hydroxylase;
            4-HPA 1-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     4-hydroxyphenylacetate,NAD(P)H:oxygen oxidoreductase
            (1-hydroxylating)
REACTION    4-hydroxyphenylacetate + NAD(P)H + H+ + O2 = homogentisate + NAD(P)+
            + H2O [RN:R02514 R02516]
ALL_REAC    R02514 R02516
SUBSTRATE   4-hydroxyphenylacetate [CPD:C00642];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     homogentisate [CPD:C00544];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Also acts on 4-hydroxyhydratropate (forming
            2-methylhomogentisate) and on 4-hydroxyphenoxyacetate (forming
            hydroquinone and glycolate).
REFERENCE   1  [PMID:234937]
  AUTHORS   Hareland WA, Crawford RL, Chapman PJ, Dagley S.
  TITLE     Metabolic function and properties of 4-hydroxyphenylacetic acid
            1-hydroxylase from Pseudomonas acidovorans.
  JOURNAL   J. Bacteriol. 121 (1975) 272-85.
  ORGANISM  Pseudomonas acidovorans
PATHWAY     PATH: map00350  Tyrosine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.18
            ExPASy - ENZYME nomenclature database: 1.14.13.18
            ExplorEnz - The Enzyme Database: 1.14.13.18
            ERGO genome analysis and discovery system: 1.14.13.18
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.18
            BRENDA, the Enzyme Database: 1.14.13.18
            CAS: 55326-44-8
///
ENTRY       EC 1.14.13.19               Enzyme
NAME        taxifolin 8-monooxygenase;
            taxifolin hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     taxifolin,NAD(P)H:oxygen oxidoreductase (8-hydroxylating)
REACTION    taxifolin + NAD(P)H + H+ + O2 = 2,3-dihydrogossypetin + NAD(P)+ +
            H2O [RN:R03637 R03638]
ALL_REAC    R03637 R03638
SUBSTRATE   taxifolin [CPD:C01617];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     2,3-dihydrogossypetin [CPD:C03052];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016];
            Flavoprotein [CPD:C06411]
COMMENT     A flavoprotein, converting a flavanol into a flavanone. Also acts on
            fustin, but not on catechin, quercetin or mollisacidin.
REFERENCE   1  [PMID:4146277]
  AUTHORS   Jeffrey AM, Knight M, Evans WC.
  TITLE     The bacterial degradation of flavonoids. Hydroxylation of the A-ring
            of taxifolin by a soil pseudomonad.
  JOURNAL   Biochem. J. 130 (1972) 373-81.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.19
            ExPASy - ENZYME nomenclature database: 1.14.13.19
            ExplorEnz - The Enzyme Database: 1.14.13.19
            ERGO genome analysis and discovery system: 1.14.13.19
            BRENDA, the Enzyme Database: 1.14.13.19
            CAS: 39307-19-2
///
ENTRY       EC 1.14.13.20               Enzyme
NAME        2,4-dichlorophenol 6-monooxygenase;
            2,4-dichlorophenol hydroxylase;
            2,4-dichlorophenol monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     2,4-dichlorophenol,NADPH:oxygen oxidoreductase (6-hydroxylating)
REACTION    2,4-dichlorophenol + NADPH + H+ + O2 = 3,5-dichlorocatechol + NADP+
            + H2O [RN:R03997]
ALL_REAC    R03997;
            (other) R05441
SUBSTRATE   2,4-dichlorophenol [CPD:C02625];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     3,5-dichlorocatechol [CPD:C02933];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Also acts, more slowly, on 4-chlorophenol and
            4-chloro-2-methylphenol; NADH can act instead of NADPH, but more
            slowly.
REFERENCE   1  [PMID:7075592]
  AUTHORS   Beadle CA, Smith AR.
  TITLE     The purification and properties of 2,4-dichlorophenol hydroxylase
            from a strain of Acinetobacter species.
  JOURNAL   Eur. J. Biochem. 123 (1982) 323-32.
  ORGANISM  Acinetobacter sp.
PATHWAY     PATH: map00627  1,4-Dichlorobenzene degradation
GENES       TET: TTHERM_00637700
            REU: Reut_D6462 Reut_D6470
            BUR: Bcep18194_A3910 Bcep18194_A4483
            DAR: Daro_0899
            PLA: Plav_0131
            RLE: pRL120094(tfdB)
            BRA: BRADO2059 BRADO2271(tfdB)
            BBT: BBta_2389
            RHA: RHA1_ro00538 RHA1_ro03910 RHA1_ro10313
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.20
            ExPASy - ENZYME nomenclature database: 1.14.13.20
            ExplorEnz - The Enzyme Database: 1.14.13.20
            ERGO genome analysis and discovery system: 1.14.13.20
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.20
            BRENDA, the Enzyme Database: 1.14.13.20
            CAS: 92767-55-0
///
ENTRY       EC 1.14.13.21               Enzyme
NAME        flavonoid 3'-monooxygenase;
            flavonoid 3'-hydroxylase;
            flavonoid 3-hydroxylase (erroneous);
            NADPH:flavonoid-3'-hydroxylase;
            flavonoid 3-monooxygenase (erroneous)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     flavonoid,NADPH:oxygen oxidoreductase (3'-hydroxylating)
REACTION    a flavonoid + NADPH + H+ + O2 = a 3'-hydroxyflavonoid + NADP+ + H2O
            [RN:R03615]
ALL_REAC    R03615 > R02442 R03124 R06537 R06538
SUBSTRATE   flavonoid [CPD:C01579];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     3'-hydroxyflavonoid [CPD:C02790];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     Acts on a number of flavonoids, including naringenin and
            dihydrokaempferol. Does not act on 4-coumarate or 4-coumaroyl-CoA.
REFERENCE   1
  AUTHORS   Forkmann, G., Heller, W. and Grisebach, H.
  TITLE     Anthocyanin biosynthesis in flowers of Matthiola incana flavanone 3-
            and flavonoid 3'-hydroxylases.
  JOURNAL   Z. Naturforsch. C: Biosci. 35 (1980) 691-695.
  ORGANISM  Matthiola incana
PATHWAY     PATH: map00941  Flavonoid biosynthesis
ORTHOLOGY   KO: K05280  flavonoid 3'-monooxygenase
GENES       ATH: AT5G07990(TT7)
            OSA: 4348304
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.21
            ExPASy - ENZYME nomenclature database: 1.14.13.21
            ExplorEnz - The Enzyme Database: 1.14.13.21
            ERGO genome analysis and discovery system: 1.14.13.21
            BRENDA, the Enzyme Database: 1.14.13.21
            CAS: 85340-98-3
///
ENTRY       EC 1.14.13.22               Enzyme
NAME        cyclohexanone monooxygenase;
            cyclohexanone 1,2-monooxygenase;
            cyclohexanone oxygenase;
            cyclohexanone:NADPH:oxygen oxidoreductase (6-hydroxylating,
            1,2-lactonizing)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     cyclohexanone,NADPH:oxygen oxidoreductase (lactone-forming)
REACTION    cyclohexanone + NADPH + H+ + O2 = hexano-6-lactone + NADP+ + H2O
            [RN:R02231]
ALL_REAC    R02231;
            (other) R06622
SUBSTRATE   cyclohexanone [CPD:C00414];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     hexano-6-lactone [CPD:C01880];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). In the catalytic mechanism of this enzyme, the
            nucleophilic species that attacks the carbonyl group is a
            peroxyflavin intermediate that is generated by reaction of the
            enzyme-bound flavin cofactor with NAD(P)H and oxygen [2]. This
            enzyme is able to catalyse a wide range of oxidative reactions,
            including enantioselective Baeyer-Villiger reactions [3],
            sulfoxidations [4], amine oxidations [5] and epoxidations [6].
REFERENCE   1  [PMID:1261545]
  AUTHORS   Donoghue NA, Norris DB, Trudgill PW.
  TITLE     The purification and properties of cyclohexanone oxygenase from
            Nocardia globerula CL1 and Acinetobacter NCIB 9871.
  JOURNAL   Eur. J. Biochem. 63 (1976) 175-92.
  ORGANISM  Norcardia globerula, Acinetobacter sp.
REFERENCE   2  [PMID:11551214]
  AUTHORS   Sheng D, Ballou DP, Massey V.
  TITLE     Mechanistic studies of cyclohexanone monooxygenase: chemical
            properties of intermediates involved in catalysis.
  JOURNAL   Biochemistry. 40 (2001) 11156-67.
  ORGANISM  Norcardia globerula, Acinetobacter sp.
REFERENCE   3
  AUTHORS   Stewart, J.D.
  TITLE     Cyclohexanone monooxygenase: a useful reagent for asymmetric
            Baeyer-Villiger reactions.
  JOURNAL   Curr. Org. Chem. 2 (1998) 195-216.
REFERENCE   4
  AUTHORS   Chen, G., Kayser, M.M., Milhovilovic, M.D., Mrstik, M.E., Martinez,
            C.A. and Stewart, J.D.
  TITLE     Asymmetric oxidations at sulfur catalyzed by engineered strains that
            overexpress cyclohexanone monooxygenase.
  JOURNAL   New J. Chem. 23 (1999) 827-832.
  ORGANISM  Acinetobacter sp.
REFERENCE   5
  AUTHORS   Ottolina, G., Bianchi, S., Belloni, B., Carrea, G. and Danieli, B.
  TITLE     First asymmetric oxidation of tertiary amines by cyclohexanone
            monooxygenase.
  JOURNAL   Tetrahedron Lett. 40 (1999) 8483-8486.
  ORGANISM  Acinetobacter calcoaceticus
REFERENCE   6
  AUTHORS   Colonna, S., Gaggero, N., Carrea, G., Ottolina, G., Pasta, P. and
            Zambianchi, F.
  TITLE     First asymmetric epoxidation catalysed by cyclohexanone
            monooxygenase.
  JOURNAL   Tetrahedron Lett. 43 (2002) 1797-1799.
  ORGANISM  Acinetobacter calcoaceticus
PATHWAY     PATH: map00930  Caprolactam degradation
ORTHOLOGY   KO: K03379  cyclohexanone monooxygenase
GENES       PIC: PICST_52278(FMO3) PICST_57936(FMO5)
            UMA: UM03415.1
            PMY: Pmen_2620
            ACI: ACIAD2339 ACIAD3192
            MAQ: Maqu_3819 Maqu_3830
            REU: Reut_B4935
            REH: H16_B1746
            BXE: Bxe_A3588 Bxe_C0276
            BUR: Bcep18194_B1145 Bcep18194_B1220 Bcep18194_B2444
                 Bcep18194_B2514 Bcep18194_C6774 Bcep18194_C6776
                 Bcep18194_C6845 Bcep18194_C7122 Bcep18194_C7142
            AJS: Ajs_2102
            MPT: Mpe_A2915 Mpe_B0579 Mpe_B0607
            PLA: Plav_0813 Plav_1165 Plav_1623
            BJA: blr2938 blr3857 blr6984
            NAR: Saro_0510 Saro_1480 Saro_2452
            MBO: Mb1428c
            MBB: BCG_1454c
            MSM: MSMEG_2567 MSMEG_5625
            MVA: Mvan_0615 Mvan_2013 Mvan_2671 Mvan_2894 Mvan_3104
            MGI: Mflv_1789 Mflv_3736 Mflv_4332 Mflv_4506 Mflv_4607
            MMC: Mmcs_0511 Mmcs_2024 Mmcs_2374 Mmcs_3189 Mmcs_4405
            MKM: Mkms_2070 Mkms_2421 Mkms_3251 Mkms_4492
            MJL: Mjls_0301 Mjls_2007 Mjls_2415 Mjls_4786
            RHA: RHA1_ro01874 RHA1_ro02492 RHA1_ro03063 RHA1_ro03247
                 RHA1_ro03437 RHA1_ro03773 RHA1_ro06008 RHA1_ro06679
                 RHA1_ro06698 RHA1_ro08137 RHA1_ro09035 RHA1_ro09039
                 RHA1_ro10187
            FAL: FRAAL3387
            SEN: SACE_2596
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.22
            ExPASy - ENZYME nomenclature database: 1.14.13.22
            ExplorEnz - The Enzyme Database: 1.14.13.22
            ERGO genome analysis and discovery system: 1.14.13.22
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.22
            BRENDA, the Enzyme Database: 1.14.13.22
            CAS: 52037-90-8
///
ENTRY       EC 1.14.13.23               Enzyme
NAME        3-hydroxybenzoate 4-monooxygenase;
            3-hydroxybenzoate 4-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     3-hydroxybenzoate,NADPH:oxygen oxidoreductase (4-hydroxylating)
REACTION    3-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+
            + H2O [RN:R01628]
ALL_REAC    R01628
SUBSTRATE   3-hydroxybenzoate [CPD:C00587];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     3,4-dihydroxybenzoate [CPD:C00230];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Acts also on a number of analogues of
            3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions.
REFERENCE   1  [PMID:4148586]
  AUTHORS   Michalover JL, Ribbons DW, Hughes H.
  TITLE     3-Hydroxybenzoate 4-hydroxylase from Pseudomonas testosteroni.
  JOURNAL   Biochem. Biophys. Res. Commun. 55 (1973) 888-96.
  ORGANISM  Pseudomonas testosteroni
REFERENCE   2  [PMID:4390252]
  AUTHORS   Premkumar R, Rao PV, Sreeleela NS, Vaidyanathan CS.
  TITLE     m-Hydroxybenzoic acid 4-hydroxylase from Aspergillus niger.
  JOURNAL   Can. J. Biochem. 47 (1969) 825-7.
  ORGANISM  Aspergillus niger
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00623  2,4-Dichlorobenzoate degradation
STRUCTURES  PDB: 2DKH  2DKI  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.23
            ExPASy - ENZYME nomenclature database: 1.14.13.23
            ExplorEnz - The Enzyme Database: 1.14.13.23
            ERGO genome analysis and discovery system: 1.14.13.23
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.23
            BRENDA, the Enzyme Database: 1.14.13.23
            CAS: 37256-76-1
///
ENTRY       EC 1.14.13.24               Enzyme
NAME        3-hydroxybenzoate 6-monooxygenase;
            3-hydroxybenzoate 6-hydroxylase;
            m-hydroxybenzoate 6-hydroxylase;
            3-hydroxybenzoic acid-6-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     3-hydroxybenzoate,NADH:oxygen oxidoreductase (6-hydroxylating)
REACTION    3-hydroxybenzoate + NADH + H+ + O2 = 2,5-dihydroxybenzoate + NAD+ +
            H2O [RN:R02589]
ALL_REAC    R02589
SUBSTRATE   3-hydroxybenzoate [CPD:C00587];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     2,5-dihydroxybenzoate [CPD:C00628];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Acts also on a number of analogues of
            3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions; NADPH
            can act instead of NADH, but more slowly.
REFERENCE   1  [PMID:4357436]
  AUTHORS   Groseclose EE, Ribbons DW, Hughes H.
  TITLE     3-Hydroxybenzoate 6-hydroxylase from Pseudomonas aeruginosa.
  JOURNAL   Biochem. Biophys. Res. Commun. 55 (1973) 897-903.
  ORGANISM  Pseudomonas aeruginosa
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
GENES       REH: H16_B0876
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.24
            ExPASy - ENZYME nomenclature database: 1.14.13.24
            ExplorEnz - The Enzyme Database: 1.14.13.24
            ERGO genome analysis and discovery system: 1.14.13.24
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.24
            BRENDA, the Enzyme Database: 1.14.13.24
            CAS: 51570-26-4
///
ENTRY       EC 1.14.13.25               Enzyme
NAME        methane monooxygenase;
            methane hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     methane,NAD(P)H:oxygen oxidoreductase (hydroxylating)
REACTION    methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O [RN:R01142
            R01143]
ALL_REAC    R01142 R01143;
            (other) R02823
SUBSTRATE   methane [CPD:C01438];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     methanol [CPD:C00132];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023]
COMMENT     Broad specificity; many alkanes can be hydroxylated, and alkenes are
            converted into the corresponding epoxides; CO is oxidized to CO2,
            ammonia is oxidized to hydroxylamine, and some aromatic compounds
            and cyclic alkanes can also be hydroxylated, but more slowly.
REFERENCE   1  [PMID:411486]
  AUTHORS   Colby J, Stirling DI, Dalton H.
  TITLE     The soluble methane mono-oxygenase of Methylococcus capsulatus
            (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and
            alicyclic, aromatic and heterocyclic compounds.
  JOURNAL   Biochem. J. 165 (1977) 395-402.
  ORGANISM  Methylococcus capsulatus [GN:mca]
REFERENCE   2  [PMID:6870854]
  AUTHORS   Hyman MR, Wood PM.
  TITLE     Methane oxidation by Nitrosomonas europaea.
  JOURNAL   Biochem. J. 212 (1983) 31-7.
  ORGANISM  Nitrosomonas europeae [GN:neu]
REFERENCE   3  [PMID:572296]
  AUTHORS   Stirling DI, Dalton H.
  TITLE     Properties of the methane mono-oxygenase from extracts of
            Methylosinus trichosporium OB3b and evidence for its similarity to
            the enzyme from Methylococcus capsulatus (Bath).
  JOURNAL   Eur. J. Biochem. 96 (1979) 205-12.
  ORGANISM  Methylococcus capsulatus [GN:mca], Methylosinus trichosporium
REFERENCE   4  [PMID:15544]
  AUTHORS   Tonge GM, Harrison DE, Higgins IJ.
  TITLE     Purification and properties of the methane mono-oxygenase enzyme
            system from Methylosinus trichosporium OB3b.
  JOURNAL   Biochem. J. 161 (1977) 333-44.
  ORGANISM  Methylosinus trichosporium
PATHWAY     PATH: map00680  Methane metabolism
ORTHOLOGY   KO: K08684  methane monooxygenase
GENES       MCA: MCA0295(pmoC3) MCA1194(mmoX) MCA1195(mmoY) MCA1196(mmoB)
                 MCA1198(mmoZ) MCA1199(mmoD) MCA1200(mmoC) MCA1796(pmoB)
                 MCA1797(pmoA) MCA1798(pmoC1) MCA2853(pmoB2) MCA2854(pmoA2)
            BUR: Bcep18194_B1122 Bcep18194_B2968
            VEI: Veis_4411
            AZO: azo1219
            BRA: BRADO4348 BRADO4350
            BBT: BBta_1594 BBta_3630 BBta_3632
            RSH: Rsph17029_1508
            ACR: Acry_1381
            MSM: MSMEG_1971 MSMEG_1972
            RHA: RHA1_ro00441
            NCA: Noca_4807 Noca_4809
            FRA: Francci3_2520
STRUCTURES  PDB: 1FYZ  1FZ0  1FZ1  1FZ2  1FZ3  1FZ4  1FZ5  1FZ6  1FZ7  1FZ8  
                 1FZ9  1FZH  1FZI  1JQ4  1MHY  1MHZ  1MMO  1MTY  1TVC  1XMF  
                 1XMG  1XMH  1XU3  1XU5  1XVB  1XVC  1XVD  1XVE  1XVF  1XVG  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.25
            ExPASy - ENZYME nomenclature database: 1.14.13.25
            ExplorEnz - The Enzyme Database: 1.14.13.25
            ERGO genome analysis and discovery system: 1.14.13.25
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.25
            BRENDA, the Enzyme Database: 1.14.13.25
            CAS: 51961-97-8
///
ENTRY       EC 1.14.13.26               Enzyme
NAME        phosphatidylcholine 12-monooxygenase;
            ricinoleic acid synthase;
            oleate Delta12-hydroxylase;
            oleate Delta12-monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     1-acyl-2-oleoyl-sn-glycero-3-phosphocholine,NADH:oxygen
            oxidoreductase (12-hydroxylating)
REACTION    1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + NADH + H+ + O2 =
            1-acyl-2-[(S)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + NAD+ +
            H2O [RN:R03476]
ALL_REAC    R03476
SUBSTRATE   1-acyl-2-oleoyl-sn-glycero-3-phosphocholine [CPD:C01282];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     1-acyl-2-[(S)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine
            [CPD:C04792];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:4289003]
  AUTHORS   Galliard T, Stumpf PK.
  TITLE     Fat metabolism in higher plants. 30. Enzymatic synthesis of
            ricinoleic acid by a microsomal preparation from developing Ricinus
            communis seeds.
  JOURNAL   J. Biol. Chem. 241 (1966) 5806-12.
  ORGANISM  Ricinus communis
REFERENCE   2
  AUTHORS   Moreau, R.A. and Stumpf, P.K.
  TITLE     Recent studies of the enzymic-synthesis of ricinoleic acid by
            developing castor beans.
  JOURNAL   Plant Physiol. 67 (1981) 672-676.
  ORGANISM  Ricinus communis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.26
            ExPASy - ENZYME nomenclature database: 1.14.13.26
            ExplorEnz - The Enzyme Database: 1.14.13.26
            ERGO genome analysis and discovery system: 1.14.13.26
            BRENDA, the Enzyme Database: 1.14.13.26
            CAS: 77950-95-9
///
ENTRY       EC 1.14.13.27               Enzyme
NAME        4-aminobenzoate 1-monooxygenase;
            4-aminobenzoate hydroxylase;
            4-aminobenzoate monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     4-aminobenzoate,NAD(P)H:oxygen oxidoreductase (1-hydroxylating,
            decarboxylating)
REACTION    4-aminobenzoate + NAD(P)H + 2 H+ + O2 = 4-hydroxyaniline + NAD(P)+ +
            H2O + CO2 [RN:R02561 R02562]
ALL_REAC    R02561 R02562
SUBSTRATE   4-aminobenzoate [CPD:C00568];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     4-hydroxyaniline [CPD:C02372];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            CO2 [CPD:C00011]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Acts on anthranilate and 4-aminosalicylate but
            not on salicylate (cf. EC 1.14.13.1 salicylate 1-monooxygenase).
REFERENCE   1  [PMID:3489713]
  AUTHORS   Tsuji H, Ogawa T, Bando N, Sasaoka K.
  TITLE     Purification and properties of 4-aminobenzoate hydroxylase, a new
            monooxygenase from Agaricus bisporus.
  JOURNAL   J. Biol. Chem. 261 (1986) 13203-9.
  ORGANISM  Agaricus bisporus
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.27
            ExPASy - ENZYME nomenclature database: 1.14.13.27
            ExplorEnz - The Enzyme Database: 1.14.13.27
            ERGO genome analysis and discovery system: 1.14.13.27
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.27
            BRENDA, the Enzyme Database: 1.14.13.27
            CAS: 98668-55-4
///
ENTRY       EC 1.14.13.28               Enzyme
NAME        3,9-dihydroxypterocarpan 6a-monooxygenase;
            3,9-dihydroxypterocarpan 6a-hydroxylase;
            3,9-dihydroxypterocarpan 6alpha-monooxygenase (erroneous)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     (6aR,11aR)-3,9-dihydroxypterocarpan,NADPH:oxygen oxidoreductase
            (6a-hydroxylating)
REACTION    (6aR,11aR)-3,9-dihydroxypterocarpan + NADPH + H+ + O2 =
            (6aS,11aS)-3,6a,9-trihydroxypterocarpan + NADP+ + H2O [RN:R03452]
ALL_REAC    R03452
SUBSTRATE   (6aR,11aR)-3,9-dihydroxypterocarpan [CPD:C04271];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (6aS,11aS)-3,6a,9-trihydroxypterocarpan [CPD:C01263];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     Possibly a heme-thiolate protein (P-450). The product of the
            reaction is the biosynthetic precursor of the phytoalexin glyceollin
            in soybean.
REFERENCE   1  [PMID:6540173]
  AUTHORS   Hagmann ML, Heller W, Grisebach H.
  TITLE     Induction of phytoalexin synthesis in soybean. Stereospecific
            3,9-dihydroxypterocarpan 6a-hydroxylase from elicitor-induced
            soybean cell cultures.
  JOURNAL   Eur. J. Biochem. 142 (1984) 127-31.
  ORGANISM  Glycine max [GN:egma]
PATHWAY     PATH: map00943  Isoflavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.28
            ExPASy - ENZYME nomenclature database: 1.14.13.28
            ExplorEnz - The Enzyme Database: 1.14.13.28
            ERGO genome analysis and discovery system: 1.14.13.28
            BRENDA, the Enzyme Database: 1.14.13.28
            CAS: 92584-16-2
///
ENTRY       EC 1.14.13.29               Enzyme
NAME        4-nitrophenol 2-monooxygenase;
            4-nitrophenol hydroxylase;
            4-nitrophenol-2-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     4-nitrophenol,NADH:oxygen oxidoreductase (2-hydroxylating)
REACTION    4-nitrophenol + NADH + H+ + O2 = 4-nitrocatechol + NAD+ + H2O
            [RN:R03023]
ALL_REAC    R03023
SUBSTRATE   4-nitrophenol [CPD:C00870];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     4-nitrocatechol [CPD:C02235];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:6477623]
  AUTHORS   Mitra D, Vaidyanathan CS.
  TITLE     A new 4-nitrophenol 2-hydroxylase from a Nocardia sp.
  JOURNAL   Biochem. Int. 8 (1984) 609-15.
  ORGANISM  Nocardia sp.
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.29
            ExPASy - ENZYME nomenclature database: 1.14.13.29
            ExplorEnz - The Enzyme Database: 1.14.13.29
            ERGO genome analysis and discovery system: 1.14.13.29
            BRENDA, the Enzyme Database: 1.14.13.29
            CAS: 91116-87-9
///
ENTRY       EC 1.14.13.30               Enzyme
NAME        leukotriene-B4 20-monooxygenase;
            leukotriene-B4 20-hydroxylase;
            leucotriene-B4 omega-hydroxylase;
            LTB4 20-hydroxylase;
            LTB4 omega-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate,N
            ADPH:oxygen oxidoreductase (20-hydroxylating)
REACTION    (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate +
            NADPH + H+ + O2 =
            (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-
            tetraenoate + NADP+ + H2O [RN:R03866]
ALL_REAC    R03866
SUBSTRATE   (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate
            [CPD:C02165];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-
            tetraenoate [CPD:C04853];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A heme-thiolate protein (P-450). Not identical with EC 1.14.13.34,
            leukotriene-E4 20-monooxygenase.
REFERENCE   1  [PMID:3027095]
  AUTHORS   Romano MC, Eckardt RD, Bender PE, Leonard TB, Straub KM, Newton JF.
  TITLE     Biochemical characterization of hepatic microsomal leukotriene B4
            hydroxylases.
  JOURNAL   J. Biol. Chem. 262 (1987) 1590-5.
  ORGANISM  human [GN:hsa], rodent
REFERENCE   2  [PMID:4044832]
  AUTHORS   Shak S, Goldstein IM.
  TITLE     Leukotriene B4 omega-hydroxylase in human polymorphonuclear
            leukocytes. Partial purification and identification as a cytochrome
            P-450.
  JOURNAL   J. Clin. Invest. 76 (1985) 1218-28.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:2986111]
  AUTHORS   Soberman RJ, Harper TW, Murphy RC, Austen KF.
  TITLE     Identification and functional characterization of leukotriene B4
            20-hydroxylase of human polymorphonuclear leukocytes.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 2292-5.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00590  Arachidonic acid metabolism
ORTHOLOGY   KO: K00490  cytochrome P450, family 4, subfamily F (leukotriene-B4
                        20-monooxygenase)
GENES       HSA: 4051(CYP4F3) 8529(CYP4F2)
            MMU: 106648(Cyp4f15) 170716(Cyp4f13) 64385(Cyp4f14) 70101(Cyp4f16)
                 72054(Cyp4f18)
            RNO: 266689(Cyp4f6) 286904(Cyp4f4) 286905(Cyp4f5) 56266(Cyp4f1)
            CFA: 484867(LOC484867)
            SPU: 591685(LOC591685)
            UMA: UM00202.1
            TET: TTHERM_00198320
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.30
            ExPASy - ENZYME nomenclature database: 1.14.13.30
            ExplorEnz - The Enzyme Database: 1.14.13.30
            ERGO genome analysis and discovery system: 1.14.13.30
            BRENDA, the Enzyme Database: 1.14.13.30
            CAS: 90119-11-2
///
ENTRY       EC 1.14.13.31               Enzyme
NAME        2-nitrophenol 2-monooxygenase;
            2-nitrophenol oxygenase;
            nitrophenol oxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     2-nitrophenol,NADPH:oxygen 2-oxidoreductase (2-hydroxylating,
            nitrite-forming)
REACTION    2-nitrophenol + NADPH + H+ + O2 = catechol + nitrite + NADP+ + H2O
            [RN:R00828]
ALL_REAC    R00828
SUBSTRATE   2-nitrophenol [CPD:C01988];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     catechol [CPD:C00090];
            nitrite [CPD:C00088];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     Involved in the metabolism of nitro-aromatic compounds by a strain
            of Pseudomonas putida.
REFERENCE   1  [PMID:3752997]
  AUTHORS   Zeyer J, Kocher HP, Timmis KN.
  TITLE     Influence of para-substituents on the oxidative metabolism of
            o-nitrophenols by Pseudomonas putida B2.
  JOURNAL   Appl. Environ. Microbiol. 52 (1986) 334-9.
  ORGANISM  Pseudomonas putida [GN:ppu]
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.31
            ExPASy - ENZYME nomenclature database: 1.14.13.31
            ExplorEnz - The Enzyme Database: 1.14.13.31
            ERGO genome analysis and discovery system: 1.14.13.31
            BRENDA, the Enzyme Database: 1.14.13.31
            CAS: 104520-84-5
///
ENTRY       EC 1.14.13.32               Enzyme
NAME        albendazole monooxygenase;
            albendazole oxidase;
            albendazole sulfoxidase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     albendazole,NADPH:oxygen oxidoreductase (sulfoxide-forming)
REACTION    albendazole + NADPH + H+ + O2 = albendazole S-oxide + NADP+ + H2O
            [RN:R03712]
ALL_REAC    R03712
SUBSTRATE   albendazole [CPD:C01779];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     albendazole S-oxide [CPD:C02809];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD).
REFERENCE   1  [PMID:3739217]
  AUTHORS   Fargetton X, Galtier P, Delatour P.
  TITLE     Sulfoxidation of albendazole by a cytochrome P450-independent
            monooxygenase from rat liver microsomes.
  JOURNAL   Vet. Res. Commun. 10 (1986) 317-24.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.32
            ExPASy - ENZYME nomenclature database: 1.14.13.32
            ExplorEnz - The Enzyme Database: 1.14.13.32
            ERGO genome analysis and discovery system: 1.14.13.32
            BRENDA, the Enzyme Database: 1.14.13.32
            CAS: 101299-59-6
///
ENTRY       EC 1.14.13.33               Enzyme
NAME        4-hydroxybenzoate 3-monooxygenase [NAD(P)H];
            4-hydroxybenzoate 3-monooxygenase (reduced nicotinamide adenine
            dinucleotide (phosphate));
            4-hydroxybenzoate-3-hydroxylase;
            4-hydroxybenzoate 3-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (3-hydroxylating)
REACTION    4-hydroxybenzoate + NAD(P)H + H+ + O2 = 3,4-dihydroxybenzoate +
            NAD(P)+ + H2O [RN:R01296 R01298]
ALL_REAC    R01296 R01298
SUBSTRATE   4-hydroxybenzoate [CPD:C00156];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     3,4-dihydroxybenzoate [CPD:C00230];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). The enzyme from Corynebacterium cyclohexanicum
            is highly specific for 4-hydroxybenzoate, but uses NADH and NADPH at
            approximately equal rates (cf. EC 1.14.13.2 4-hydroxybenzoate
            3-monooxygenase). It is less specific for NADPH than EC 1.14.13.2.
REFERENCE   1  [PMID:3971979]
  AUTHORS   Fujii T, Kaneda T.
  TITLE     Purification and properties of NADH/NADPH-dependent
            p-hydroxybenzoate hydroxylase from Corynebacterium cyclohexanicum.
  JOURNAL   Eur. J. Biochem. 147 (1985) 97-104.
  ORGANISM  Corynebacterium cyclohexanicum
REFERENCE   2  [PMID:8706756]
  AUTHORS   Seibold B, Matthes M, Eppink MH, Lingens F, Van Berkel WJ, Muller R.
  TITLE     4-Hydroxybenzoate hydroxylase from Pseudomonas sp. CBS3.
            Purification, characterization, gene cloning, sequence analysis and
            assignment of structural features determining the coenzyme
            specificity.
  JOURNAL   Eur. J. Biochem. 239 (1996) 469-78.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00623  2,4-Dichlorobenzoate degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.33
            ExPASy - ENZYME nomenclature database: 1.14.13.33
            ExplorEnz - The Enzyme Database: 1.14.13.33
            ERGO genome analysis and discovery system: 1.14.13.33
            BRENDA, the Enzyme Database: 1.14.13.33
            CAS: 95471-33-3
///
ENTRY       EC 1.14.13.34               Enzyme
NAME        leukotriene-E4 20-monooxygenase;
            leukotriene-E4 omega-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     (7E,9E,11Z,14Z)-(5S,6R)-6-(cystein-S-yl)-5-hydroxyicosa-7,9,11,14-te
            traenoate,NADPH:oxygen oxidoreductase (20-hydroxylating)
REACTION    (7E,9E,11Z,14Z)-(5S,6R)-6-(cystein-S-yl)-5-hydroxyicosa-7,9,11,14-
            tetraenoate + NADPH + H+ + O2 = 20-hydroxyleukotriene E4 + NADP+ +
            H2O [RN:R04256]
ALL_REAC    R04256
SUBSTRATE   (7E,9E,11Z,14Z)-(5S,6R)-6-(cystein-S-yl)-5-hydroxyicosa-7,9,11,14-
            tetraenoate [CPD:C05952];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     20-hydroxyleukotriene E4 [CPD:C03577];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     Also acts on N-acetyl-leukotriene E4, but more slowly. Not identical
            with EC 1.14.13.30 leukotriene-B4 20-monooxygenase.
REFERENCE   1  [PMID:2826163]
  AUTHORS   Orning L.
  TITLE     Omega-oxidation of cysteine-containing leukotrienes by rat-liver
            microsomes. Isolation and characterization of omega-hydroxy and
            omega-carboxy metabolites of leukotriene E4 and N-acetylleukotriene
            E4.
  JOURNAL   Eur. J. Biochem. 170 (1987) 77-85.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00590  Arachidonic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.34
            ExPASy - ENZYME nomenclature database: 1.14.13.34
            ExplorEnz - The Enzyme Database: 1.14.13.34
            ERGO genome analysis and discovery system: 1.14.13.34
            BRENDA, the Enzyme Database: 1.14.13.34
            CAS: 111940-51-3
///
ENTRY       EC 1.14.13.35               Enzyme
NAME        anthranilate 3-monooxygenase (deaminating);
            anthranilate hydroxylase;
            anthranilate 2,3-dioxygenase (deaminating);
            anthranilate hydroxylase (deaminating);
            anthranilic hydroxylase;
            anthranilate 2,3-hydroxylase (deaminating)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     anthranilate,NADPH:oxygen oxidoreductase (3-hydroxylating,
            deaminating)
REACTION    anthranilate + NADPH + H+ + O2 = 2,3-dihydroxybenzoate + NADP+ + NH3
            [RN:R00980]
ALL_REAC    R00980;
            (other) R00144 R00147
SUBSTRATE   anthranilate [CPD:C00108];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     2,3-dihydroxybenzoate [CPD:C00196];
            NADP+ [CPD:C00006];
            NH3 [CPD:C00014]
COMMENT     The enzyme from Aspergillus niger is an iron protein; that from the
            yeast Trichosporon cutaneum is a flavoprotein (FAD).
REFERENCE   1  [PMID:3793735]
  AUTHORS   Powlowski JB, Dagley S, Massey V, Ballou DP.
  TITLE     Properties of anthranilate hydroxylase (deaminating), a flavoprotein
            from Trichosporon cutaneum.
  JOURNAL   J. Biol. Chem. 262 (1987) 69-74.
  ORGANISM  Trichosporon cutaneum
REFERENCE   2  [PMID:6501219]
  AUTHORS   Subramanian V, Vaidyanathan CS.
  TITLE     Anthranilate hydroxylase from Aspergillus niger: new type of
            NADPH-linked nonheme iron monooxygenase.
  JOURNAL   J. Bacteriol. 160 (1984) 651-5.
  ORGANISM  Aspergillus niger
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00629  Carbazole degradation
            PATH: map00910  Nitrogen metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.35
            ExPASy - ENZYME nomenclature database: 1.14.13.35
            ExplorEnz - The Enzyme Database: 1.14.13.35
            ERGO genome analysis and discovery system: 1.14.13.35
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.35
            BRENDA, the Enzyme Database: 1.14.13.35
            CAS: 37256-68-1
///
ENTRY       EC 1.14.13.36               Enzyme
NAME        5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase;
            5-O-(4-coumaroyl)-D-quinate/shikimate 3'-hydroxylase;
            coumaroylquinate(coumaroylshikimate) 3'-monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     trans-5-O-(4-coumaroyl)-D-quinate,NADPH:oxygen oxidoreductase
            (3'-hydroxylating)
REACTION    trans-5-O-(4-coumaroyl)-D-quinate + NADPH + H+ + O2 =
            trans-5-O-caffeoyl-D-quinate + NADP+ + H2O [RN:R04342]
ALL_REAC    R04342;
            (other) R06582
SUBSTRATE   trans-5-O-(4-coumaroyl)-D-quinate [CPD:C12208];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     trans-5-O-caffeoyl-D-quinate [CPD:C12209];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     Also acts on trans-5-O-(4-coumaroyl)shikimate.
REFERENCE   1  [PMID:2821918]
  AUTHORS   Kuhnl T, Koch U, Heller W, Wellmann E.
  TITLE     Chlorogenic acid biosynthesis: characterization of a light-induced
            microsomal 5-O-(4-coumaroyl)-D-quinate/shikimate 3'-hydroxylase from
            carrot (Daucus carota L.) cell suspension cultures.
  JOURNAL   Arch. Biochem. Biophys. 258 (1987) 226-32.
  ORGANISM  Daucus carota
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.36
            ExPASy - ENZYME nomenclature database: 1.14.13.36
            ExplorEnz - The Enzyme Database: 1.14.13.36
            ERGO genome analysis and discovery system: 1.14.13.36
            BRENDA, the Enzyme Database: 1.14.13.36
            CAS: 112131-08-5
///
ENTRY       EC 1.14.13.37               Enzyme
NAME        methyltetrahydroprotoberberine 14-monooxygenase;
            methyltetrahydroprotoberberine 14-hydroxylase;
            (S)-cis-N-methyltetrahydroberberine 14-monooxygenase;
            (S)-cis-N-methyltetrahydroprotoberberine-14-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     (S)-N-methylcanadine,NADPH:oxygen oxidoreductase (14-hydroxylating)
REACTION    (S)-N-methylcanadine + NADPH + H+ + O2 = allocryptopine + NADP+ +
            H2O [RN:R03842]
ALL_REAC    R03842;
            (other) R04700
SUBSTRATE   (S)-N-methylcanadine [CPD:C02915];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     allocryptopine [CPD:C02134];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A heme-thiolate protein (P-450).
REFERENCE   1
  AUTHORS   Rueffer, M. and Zenk, M.H.
  TITLE     Enzymatic formation of protopines by a microsomal cytochrome-P-450
            system of Corydalis vaginans.
  JOURNAL   Tetrahedron Lett. 28 (1987) 5307-5310.
  ORGANISM  Corydalis vaginans
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.37
            ExPASy - ENZYME nomenclature database: 1.14.13.37
            ExplorEnz - The Enzyme Database: 1.14.13.37
            ERGO genome analysis and discovery system: 1.14.13.37
            BRENDA, the Enzyme Database: 1.14.13.37
            CAS: 113478-42-5
///
ENTRY       EC 1.14.13.38               Enzyme
NAME        anhydrotetracycline monooxygenase;
            ATC oxygenase;
            anhydrotetracycline oxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     anhydrotetracycline,NADPH:oxygen oxidoreductase (6-hydroxylating)
REACTION    anhydrotetracycline + NADPH + H+ + O2 = 12-dehydrotetracycline +
            NADP+ + H2O [RN:R04060]
ALL_REAC    R04060
SUBSTRATE   anhydrotetracycline [CPD:C02811];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     12-dehydrotetracycline [CPD:C03206];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     Involved in the biosynthesis of the antibiotics tetracyclines in
            Streptomyces sp.
REFERENCE   1
  AUTHORS   Behal, V.
  TITLE     The tetracycline fermentation and its regulation.
  JOURNAL   CRC Crit. Rev. Biotechnol. 5 (1987) 295-318.
  ORGANISM  Streptomyces aureofaciens
PATHWAY     PATH: map00253  Tetracycline biosynthesis
            PATH: map01057  Biosynthesis of type II polyketide products
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.38
            ExPASy - ENZYME nomenclature database: 1.14.13.38
            ExplorEnz - The Enzyme Database: 1.14.13.38
            ERGO genome analysis and discovery system: 1.14.13.38
            BRENDA, the Enzyme Database: 1.14.13.38
            CAS: 70766-62-0
///
ENTRY       EC 1.14.13.39               Enzyme
NAME        nitric-oxide synthase;
            nitric oxide synthetase;
            endothelium-derived relaxation factor-forming enzyme;
            endothelium-derived relaxing factor synthase;
            NO synthase;
            NADPH-diaphorase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     L-arginine,NADPH:oxygen oxidoreductase (nitric-oxide-forming)
REACTION    L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n
            NADP+ [RN:R00557]
ALL_REAC    R00557;
            (other) R00111 R00558
SUBSTRATE   L-arginine [CPD:C00062];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     citrulline [CPD:C00327];
            nitric oxide [CPD:C00533];
            NADP+ [CPD:C00006]
COFACTOR    Calcium [CPD:C00076]
INHIBITOR   Ngamma-Nitro-L-arginine [CPD:C03417];
            Ngamma-Monomethyl-L-arginine [CPD:C03884];
            Ngamma-Nitro-L-arginine methyl ester [CPD:C04337]
COMMENT     The enzyme in brain, but not that induced in lung or liver by
            endotoxin, requires Ca2+. The stoichiometry is not clear, but may
            involve a two-electron and a one-electron oxidation step.
REFERENCE   1  [PMID:1689048]
  AUTHORS   Bredt DS, Snyder SH.
  TITLE     Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 682-5.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:1700698]
  AUTHORS   Knowles RG, Merrett M, Salter M, Moncada S.
  TITLE     Differential induction of brain, lung and liver nitric oxide
            synthase by endotoxin in the rat.
  JOURNAL   Biochem. J. 270 (1990) 833-6.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:2567594]
  AUTHORS   Moncada S, Palmer RM, Higgs EA.
  TITLE     Biosynthesis of nitric oxide from L-arginine. A pathway for the
            regulation of cell function and communication.
  JOURNAL   Biochem. Pharmacol. 38 (1989) 1709-15.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00330  Arginine and proline metabolism
            PATH: map04020  Calcium signaling pathway
            PATH: map04730  Long-term depression
            PATH: map05222  Small cell lung cancer
ORTHOLOGY   KO: K00491  nitric-oxide synthase
GENES       HSA: 4842(NOS1) 4843(NOS2A) 4846(NOS3)
            MMU: 18125(Nos1) 18126(Nos2) 18127(Nos3)
            RNO: 24598(Nos1) 24599(Nos2) 24600(Nos3)
            CFA: 403784(NOS3) 403822(NOS2A) 477498(NOS1)
            BTA: 282876(NOS2A) 287024(NOS3)
            SSC: 397557(NOS3)
            GGA: 395807(NOS2A) 427721(NOS1)
            SPU: 587111(LOC587111)
            DME: Dmel_CG6713(Nos)
            CAL: CaO19.4076
            AOR: AO090138000170
            BUR: Bcep18194_B1346
            BSU: BG12948(yflM)
            BHA: BH0823
            BAN: BA5695
            BAR: GBAA5695
            BAA: BA_0553
            BAT: BAS5299
            BCE: BC5444
            BCA: BCE_5578
            BCZ: BCZK5141(nos)
            BCY: Bcer98_3061 Bcer98_3961
            BTK: BT9727_5126(nos)
            BTL: BALH_4953(nos)
            BLI: BL03064(nos)
            BLD: BLi00785(yflM)
            BCL: ABC1267
            BPU: BPUM_0714
            OIH: OB2691
            GKA: GK1676
            SAB: SAB1851
            SAJ: SaurJH9_1654 SaurJH9_1970
            SAH: SaurJH1_1689 SaurJH1_2004
            LCA: LSEI_1690
            LRE: Lreu_1237
            RHA: RHA1_ro02793(nos)
            DGE: Dgeo_0268
            NPH: NP1908A(nos)
STRUCTURES  PDB: 1D0C  1D0O  1D1V  1D1W  1D1X  1D1Y  1DD7  1DF1  1DM6  1DM7  
                 1DM8  1DMI  1DMJ  1DMK  1DWV  1DWW  1DWX  1ED4  1ED5  1ED6  
                 1F20  1FOI  1FOJ  1FOL  1FOO  1FOP  1I83  1JWJ  1JWK  1K2R  
                 1K2S  1K2T  1K2U  1LZX  1LZZ  1M00  1M7V  1M7Z  1M8D  1M8E  
                 1M8H  1M8I  1M9J  1M9K  1M9M  1M9Q  1M9R  1M9T  1MJT  1MMV  
                 1MMW  1N2N  1NIW  1NOC  1NOD  1NOS  1NSE  1NSI  1OM4  1OM5  
                 1P6H  1P6I  1P6J  1P6K  1P6L  1P6M  1P6N  1Q2O  1QOM  1QW4  
                 1QW5  1QW6  1QWC  1R35  1RS6  1RS7  1RS8  1RS9  1TLL  1VAF  
                 1VAG  1ZVI  1ZVL  1ZZQ  1ZZR  1ZZS  1ZZT  1ZZU  2AMO  2AN0  
                 2AN2  2BHJ  2FC1  2FC2  2FLQ  2G6H  2G6I  2G6J  2G6K  2G6L  
                 2G6M  2G6N  2G6O  2HX2  2HX3  2HX4  2NOD  2NOS  2NSE  2NSI  
                 2ORO  2ORP  2ORQ  2ORR  2ORS  2ORT  3NOD  3NOS  3NSE  4NOS  
                 4NSE  5NSE  6NSE  7NSE  8NSE  9NSE  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.39
            ExPASy - ENZYME nomenclature database: 1.14.13.39
            ExplorEnz - The Enzyme Database: 1.14.13.39
            ERGO genome analysis and discovery system: 1.14.13.39
            BRENDA, the Enzyme Database: 1.14.13.39
            CAS: 125978-95-2
///
ENTRY       EC 1.14.13.40               Enzyme
NAME        anthraniloyl-CoA monooxygenase;
            anthraniloyl coenzyme A reductase;
            2-aminobenzoyl-CoA monooxygenase/reductase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     2-aminobenzoyl-CoA,NAD(P)H:oxygen oxidoreductase (de-aromatizing)
REACTION    2-aminobenzoyl-CoA + 2 NAD(P)H + 2 H+ + O2 =
            2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+ [RN:R03998
            R03999]
ALL_REAC    R03998 R03999
SUBSTRATE   2-aminobenzoyl-CoA [CPD:C02247];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     2-amino-5-oxocyclohex-1-enecarboxyl-CoA;
            H2O [CPD:C00001];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). The non-aromatic product is unstable and
            releases CO2 and NH3, forming 1,4-cyclohexanedione.
REFERENCE   1  [PMID:2591379]
  AUTHORS   Buder R, Fuchs G.
  TITLE     2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of
            flavoenzyme. Purification and some properties of the enzyme.
  JOURNAL   Eur. J. Biochem. 185 (1989) 629-35.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:2591380]
  AUTHORS   Buder R, Ziegler K, Fuchs G, Langkau B, Ghisla S.
  TITLE     2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of
            flavoenzyme. Studies on the stoichiometry and the course of the
            reaction.
  JOURNAL   Eur. J. Biochem. 185 (1989) 637-43.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:2384085]
  AUTHORS   Langkau B, Ghisla S, Buder R, Ziegler K, Fuchs G.
  TITLE     2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of
            flavoenzyme. Identification of the reaction products.
  JOURNAL   Eur. J. Biochem. 191 (1990) 365-71.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00629  Carbazole degradation
ORTHOLOGY   KO: K09461  anthraniloyl-CoA monooxygenase
GENES       REH: H16_A2461(abmA)
            AZO: azo1934(abmA)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.40
            ExPASy - ENZYME nomenclature database: 1.14.13.40
            ExplorEnz - The Enzyme Database: 1.14.13.40
            ERGO genome analysis and discovery system: 1.14.13.40
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.40
            BRENDA, the Enzyme Database: 1.14.13.40
            CAS: 112692-57-6
///
ENTRY       EC 1.14.13.41               Enzyme
NAME        tyrosine N-monooxygenase;
            tyrosine N-hydroxylase;
            CYP79A1
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     L-tyrosine,NADPH:oxygen oxidoreductase (N-hydroxylating)
REACTION    (1) L-tyrosine + O2 + NADPH + H+ = N-hydroxy-L-tyrosine + NADP+ +
            H2O [RN:R00730];
            (2) N-hydroxy-L-tyrosine + O2 + NADPH + H+ =
            N,N-dihydroxy-L-tyrosine + NADP+ + H2O [RN:R04460];
            (3) N,N-dihydroxy-L-tyrosine = (Z)-[4-hydroxyphenylacetaldehyde
            oxime] + CO2 + H2O [RN:R07190]
ALL_REAC    R00730 R04460 R07190;
            (other) R01260
SUBSTRATE   L-tyrosine [CPD:C00082];
            O2 [CPD:C00007];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            N-hydroxy-L-tyrosine [CPD:C03004];
            N,N-dihydroxy-L-tyrosine [CPD:C15503]
PRODUCT     N-hydroxy-L-tyrosine [CPD:C03004];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            N,N-dihydroxy-L-tyrosine [CPD:C15503];
            (Z)-[4-hydroxyphenylacetaldehyde oxime];
            CO2 [CPD:C00011]
COFACTOR    Heme [CPD:C00032]
COMMENT     A heme-thiolate protein (P-450). This enzyme is involved in the
            biosynthesis of the cyanogenic glucoside dhurrin in sorghum, along
            with EC 1.14.13.68, 4-hydroxyphenylacetaldehyde oxime monooxygenase
            and EC 2.4.1.85, cyanohydrin beta-glucosyltransferase. Some
            2-(4-hydroxyphenyl)-1-nitroethane is formed as a side product.
REFERENCE   1  [PMID:2250015]
  AUTHORS   Halkier BA, Moller BL.
  TITLE     The biosynthesis of cyanogenic glucosides in higher plants.
            Identification of three hydroxylation steps in the biosynthesis of
            dhurrin in Sorghum bicolor (L.) Moench and the involvement of
            1-ACI-nitro-2-(p-hydroxyphenyl)ethane as an intermediate.
  JOURNAL   J. Biol. Chem. 265 (1990) 21114-21.
  ORGANISM  Sorghum bicolor [GN:esbi]
REFERENCE   2  [PMID:7876084]
  AUTHORS   Sibbesen O, Koch B, Halkier BA, Moller BL.
  TITLE     Cytochrome P-450TYR is a multifunctional heme-thiolate enzyme
            catalyzing the conversion of L-tyrosine to
            p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the
            cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench.
  JOURNAL   J. Biol. Chem. 270 (1995) 3506-11.
  ORGANISM  Sorghum bicolor [GN:esbi]
REFERENCE   3  [PMID:10938360]
  AUTHORS   Bak S, Olsen CE, Halkier BA, Moller BL.
  TITLE     Transgenic tobacco and Arabidopsis plants expressing the two
            multifunctional sorghum cytochrome P450 enzymes, CYP79A1 and
            CYP71E1, are cyanogenic and accumulate metabolites derived from
            intermediates in Dhurrin biosynthesis.
  JOURNAL   Plant. Physiol. 123 (2000) 1437-48.
  ORGANISM  Sorghum bicolor [GN:esbi]
REFERENCE   4  [PMID:10759528]
  AUTHORS   Nielsen JS, Moller BL.
  TITLE     Cloning and expression of cytochrome P450 enzymes catalyzing the
            conversion of tyrosine to p-hydroxyphenylacetaldoxime in the
            biosynthesis of cyanogenic glucosides in Triglochin maritima.
  JOURNAL   Plant. Physiol. 122 (2000) 1311-21.
  ORGANISM  Sorghum bicolor [GN:esbi]
REFERENCE   5  [PMID:12114576]
  AUTHORS   Busk PK, Moller BL.
  TITLE     Dhurrin synthesis in sorghum is regulated at the transcriptional
            level and induced by nitrogen fertilization in older plants.
  JOURNAL   Plant. Physiol. 129 (2002) 1222-31.
  ORGANISM  Sorghum bicolor [GN:esbi]
REFERENCE   6  [PMID:15665094]
  AUTHORS   Kristensen C, Morant M, Olsen CE, Ekstrom CT, Galbraith DW, Moller
            BL, Bak S.
  TITLE     Metabolic engineering of dhurrin in transgenic Arabidopsis plants
            with marginal inadvertent effects on the metabolome and
            transcriptome.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 1779-84.
  ORGANISM  Sorghum bicolor [GN:esbi]
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00460  Cyanoamino acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.41
            ExPASy - ENZYME nomenclature database: 1.14.13.41
            ExplorEnz - The Enzyme Database: 1.14.13.41
            ERGO genome analysis and discovery system: 1.14.13.41
            BRENDA, the Enzyme Database: 1.14.13.41
            CAS: 112692-57-6
///
ENTRY       EC 1.14.13.42               Enzyme
NAME        hydroxyphenylacetonitrile 2-monooxygenase;
            4-hydroxyphenylacetonitrile monooxygenase;
            4-hydroxyphenylacetonitrile hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     4-hydroxyphenylacetonitrile,NADPH:oxygen oxidoreductase
            (2-hydroxylating)
REACTION    4-hydroxyphenylacetonitrile + NADPH + H+ + O2 =
            4-hydroxymandelonitrile + NADP+ + H2O [RN:R02708]
ALL_REAC    R02708
SUBSTRATE   4-hydroxyphenylacetonitrile [CPD:C03766];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     4-hydroxymandelonitrile [CPD:C00650];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A heme-thiolate protein (P-450).
REFERENCE   1  [PMID:2250015]
  AUTHORS   Halkier BA, Moller BL.
  TITLE     The biosynthesis of cyanogenic glucosides in higher plants.
            Identification of three hydroxylation steps in the biosynthesis of
            dhurrin in Sorghum bicolor (L.) Moench and the involvement of
            1-ACI-nitro-2-(p-hydroxyphenyl)ethane as an intermediate.
  JOURNAL   J. Biol. Chem. 265 (1990) 21114-21.
  ORGANISM  Sorghum bicolor [GN:esbi]
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.42
            ExPASy - ENZYME nomenclature database: 1.14.13.42
            ExplorEnz - The Enzyme Database: 1.14.13.42
            ERGO genome analysis and discovery system: 1.14.13.42
            BRENDA, the Enzyme Database: 1.14.13.42
            CAS: 89287-41-2
///
ENTRY       EC 1.14.13.43               Enzyme
NAME        questin monooxygenase;
            questin oxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     questin,NADPH:oxygen oxidoreductase (hydroxylating,
            anthraquinone-ring-opening)
REACTION    questin + NADPH + H+ + O2 = demethylsulochrin + NADP+ + H2O
            [RN:R02417]
ALL_REAC    R02417
SUBSTRATE   questin [CPD:C01448];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     demethylsulochrin [CPD:C15504];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     The enzyme cleaves the anthraquinone ring of questin to form a
            benzophenone. Involved in the biosynthesis of the seco-anthraquinone
            (+)-geodin.
REFERENCE   1  [PMID:3182756]
  AUTHORS   Fujii I, Ebizuka Y, Sankawa U.
  TITLE     A novel anthraquinone ring cleavage enzyme from Aspergillus terreus.
  JOURNAL   J. Biochem. (Tokyo). 103 (1988) 878-83.
  ORGANISM  Aspergillus terreus
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.43
            ExPASy - ENZYME nomenclature database: 1.14.13.43
            ExplorEnz - The Enzyme Database: 1.14.13.43
            ERGO genome analysis and discovery system: 1.14.13.43
            BRENDA, the Enzyme Database: 1.14.13.43
            CAS: 115232-45-6
///
ENTRY       EC 1.14.13.44               Enzyme
NAME        2-hydroxybiphenyl 3-monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     2-hydroxybiphenyl,NADH:oxygen oxidoreductase (3-hydroxylating)
REACTION    2-hydroxybiphenyl + NADH + H+ + O2 = 2,3-dihydroxybiphenyl + NAD+ +
            H2O [RN:R03964]
ALL_REAC    R03964
SUBSTRATE   2-hydroxybiphenyl [CPD:C02499];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     2,3-dihydroxybiphenyl [CPD:C02526];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
COMMENT     Also converts 2,2'-dihydroxybiphenyl into
            2,2',3-trihydroxy-biphenyl.
REFERENCE   1  [PMID:3214154]
  AUTHORS   Kohler HP, Kohler-Staub D, Focht DD.
  TITLE     Degradation of 2-hydroxybiphenyl and 2,2'-dihydroxybiphenyl by
            Pseudomonas sp. strain HBP1.
  JOURNAL   Appl. Environ. Microbiol. 54 (1988) 2683-8.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.44
            ExPASy - ENZYME nomenclature database: 1.14.13.44
            ExplorEnz - The Enzyme Database: 1.14.13.44
            ERGO genome analysis and discovery system: 1.14.13.44
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.44
            BRENDA, the Enzyme Database: 1.14.13.44
            CAS: 118251-39-1
///
ENTRY       EC 1.14.13.45     Obsolete  Enzyme
NAME        Transferred to 1.14.18.2
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
COMMENT     Transferred entry: now EC 1.14.18.2 CMP-N-acetylneuraminate
            monooxygenase. (EC 1.14.13.45 created 1992, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.45
            ExPASy - ENZYME nomenclature database: 1.14.13.45
            ExplorEnz - The Enzyme Database: 1.14.13.45
            ERGO genome analysis and discovery system: 1.14.13.45
            BRENDA, the Enzyme Database: 1.14.13.45
///
ENTRY       EC 1.14.13.46               Enzyme
NAME        (-)-menthol monooxygenase;
            l-menthol monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     (-)-menthol,NADPH:oxygen oxidoreductase (8-hydroxylating)
REACTION    (-)-menthol + NADPH + H+ + O2 = p-menthane-3,8-diol + NADP+ + H2O
            [RN:R02178]
ALL_REAC    R02178
SUBSTRATE   (-)-menthol [CPD:C00400];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     p-menthane-3,8-diol [CPD:C02904];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:2906604]
  AUTHORS   Madyastha KM, Srivatsan V.
  TITLE     Studies on the metabolism of l-menthol in rats.
  JOURNAL   Drug. Metab. Dispos. 16 (1988) 765-72.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.46
            ExPASy - ENZYME nomenclature database: 1.14.13.46
            ExplorEnz - The Enzyme Database: 1.14.13.46
            ERGO genome analysis and discovery system: 1.14.13.46
            BRENDA, the Enzyme Database: 1.14.13.46
            CAS: 117590-75-7
///
ENTRY       EC 1.14.13.47               Enzyme
NAME        (S)-limonene 3-monooxygenase;
            (-)-limonene 3-hydroxylase;
            (-)-limonene 3-monooxygenase;
            (-)-limonene,NADPH:oxygen oxidoreductase (3-hydroxylating)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     (S)-limonene,NADPH:oxygen oxidoreductase (3-hydroxylating)
REACTION    (-)-(S)-limonene + NADPH + H+ + O2 = (-)-trans-isopiperitenol +
            NADP+ + H2O [RN:R02469]
ALL_REAC    R02469
SUBSTRATE   (-)-(S)-limonene [CPD:C00521];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (-)-trans-isopiperitenol [CPD:C01123];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     High specificity, but NADH can act instead of NADPH, although more
            slowly. A heme-thiolate protein (P-450).
REFERENCE   1  [PMID:2297225]
  AUTHORS   Karp F, Mihaliak CA, Harris JL, Croteau R.
  TITLE     Monoterpene biosynthesis: specificity of the hydroxylations of
            (-)-limonene by enzyme preparations from peppermint (Mentha
            piperita), spearmint (Mentha spicata), and perilla (Perilla
            frutescens) leaves.
  JOURNAL   Arch. Biochem. Biophys. 276 (1990) 219-26.
  ORGANISM  Mentha piperita
PATHWAY     PATH: map00902  Monoterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.47
            ExPASy - ENZYME nomenclature database: 1.14.13.47
            ExplorEnz - The Enzyme Database: 1.14.13.47
            ERGO genome analysis and discovery system: 1.14.13.47
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.47
            BRENDA, the Enzyme Database: 1.14.13.47
            CAS: 138066-92-9
///
ENTRY       EC 1.14.13.48               Enzyme
NAME        (S)-limonene 6-monooxygenase;
            (-)-limonene 6-hydroxylase;
            (-)-limonene 6-monooxygenase;
            (-)-limonene,NADPH:oxygen oxidoreductase (6-hydroxylating)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     (S)-limonene,NADPH:oxygen oxidoreductase (6-hydroxylating)
REACTION    (-)-(S)-limonene + NADPH + H+ + O2 = (-)-trans-carveol + NADP+ + H2O
            [RN:R02468]
ALL_REAC    R02468
SUBSTRATE   (-)-(S)-limonene [CPD:C00521];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (-)-trans-carveol [CPD:C00964];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     High specificity, but NADH can act instead of NADPH, but more
            slowly. A heme-thiolate protein (P-450).
REFERENCE   1  [PMID:2297225]
  AUTHORS   Karp F, Mihaliak CA, Harris JL, Croteau R.
  TITLE     Monoterpene biosynthesis: specificity of the hydroxylations of
            (-)-limonene by enzyme preparations from peppermint (Mentha
            piperita), spearmint (Mentha spicata), and perilla (Perilla
            frutescens) leaves.
  JOURNAL   Arch. Biochem. Biophys. 276 (1990) 219-26.
  ORGANISM  Mentha spicata
PATHWAY     PATH: map00902  Monoterpenoid biosynthesis
            PATH: map00903  Limonene and pinene degradation
ORTHOLOGY   KO: K07381  (S)-limonene 6-monooxygenase
GENES       HSA: 1557(CYP2C19) 1559(CYP2C9)
            RNO: 29277(Cyp2c)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.48
            ExPASy - ENZYME nomenclature database: 1.14.13.48
            ExplorEnz - The Enzyme Database: 1.14.13.48
            ERGO genome analysis and discovery system: 1.14.13.48
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.48
            BRENDA, the Enzyme Database: 1.14.13.48
            CAS: 138066-93-0
///
ENTRY       EC 1.14.13.49               Enzyme
NAME        (S)-limonene 7-monooxygenase;
            (-)-limonene 7-monooxygenase;
            (-)-limonene hydroxylase;
            (-)-limonene monooxygenase;
            (-)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     (S)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating)
REACTION    (-)-(S)-limonene + NADPH + H+ + O2 = (-)-perillyl alcohol + NADP+ +
            H2O [RN:R02470]
ALL_REAC    R02470
SUBSTRATE   (-)-(S)-limonene [CPD:C00521];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (-)-perillyl alcohol [CPD:C02452];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     High specificity, but NADH can act instead of NADPH, although more
            slowly. A heme-thiolate protein (P-450).
REFERENCE   1  [PMID:2297225]
  AUTHORS   Karp F, Mihaliak CA, Harris JL, Croteau R.
  TITLE     Monoterpene biosynthesis: specificity of the hydroxylations of
            (-)-limonene by enzyme preparations from peppermint (Mentha
            piperita), spearmint (Mentha spicata), and perilla (Perilla
            frutescens) leaves.
  JOURNAL   Arch. Biochem. Biophys. 276 (1990) 219-26.
  ORGANISM  Perilla frutescens
PATHWAY     PATH: map00902  Monoterpenoid biosynthesis
            PATH: map00903  Limonene and pinene degradation
ORTHOLOGY   KO: K07382  (S)-limonene 7-monooxygenase
GENES       HSA: 1557(CYP2C19) 1559(CYP2C9)
            RNO: 29277(Cyp2c)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.49
            ExPASy - ENZYME nomenclature database: 1.14.13.49
            ExplorEnz - The Enzyme Database: 1.14.13.49
            ERGO genome analysis and discovery system: 1.14.13.49
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.49
            BRENDA, the Enzyme Database: 1.14.13.49
            CAS: 122653-75-2
///
ENTRY       EC 1.14.13.50               Enzyme
NAME        pentachlorophenol monooxygenase;
            pentachlorophenol dechlorinase;
            pentachlorophenol dehalogenase;
            pentachlorophenol 4-monooxygenase;
            PCP hydroxylase;
            pentachlorophenol hydroxylase;
            PcpB;
            PCB 4-monooxygenase;
            PCB4MO
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     pentachlorophenol,NADPH:oxygen oxidoreductase (hydroxylating,
            dechlorinating)
REACTION    (1) pentachlorophenol + 2 NADPH + H+ + O2 =
            2,3,5,6-tetrachlorohydroquinone + 2 NADP+ + chloride + H2O
            [RN:R03982];
            (2) 2,3,5,6-tetrachlorophenol + NADPH + H+ + O2 =
            2,3,5,6-tetrachlorohydroquinone + NADP+ + H2O [RN:R07191]
ALL_REAC    R03982 R07191;
            (other) R07779
SUBSTRATE   pentachlorophenol [CPD:C02575];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007];
            2,3,5,6-tetrachlorophenol [CPD:C15505]
PRODUCT     2,3,5,6-tetrachlorohydroquinone [CPD:C03434];
            NADP+ [CPD:C00006];
            chloride [CPD:C00115];
            H2O [CPD:C00001]
COMMENT     A flavoprotein (FAD). The enzyme displaces a diverse range of
            substituents from the 4-position of polyhalogenated phenols but
            requires that a halogen substituent be present at the 2-position
            [2]. The enzyme converts many polyhalogenated phenols into
            hydroquinones, and requires that a halogen substituent be present at
            C-2 [2]. If C-4 carries a halogen substituent, reaction 1 is
            catalysed, e.g. 2,4,6-triiodophenol is oxidized to
            2,6-diiodohydroquinone; if C-4 is unsubstituted, reaction 2 is
            catalysed.
REFERENCE   1  [PMID:2793827]
  AUTHORS   Schenk T, Muller R, Morsberger F, Otto MK, Lingens F.
  TITLE     Enzymatic dehalogenation of pentachlorophenol by extracts from
            Arthrobacter sp. strain ATCC 33790.
  JOURNAL   J. Bacteriol. 171 (1989) 5487-91.
  ORGANISM  Arthrobacter sp.
REFERENCE   2  [PMID:1569020]
  AUTHORS   Xun L, Topp E, Orser CS.
  TITLE     Diverse substrate range of a Flavobacterium pentachlorophenol
            hydroxylase and reaction stoichiometries.
  JOURNAL   J. Bacteriol. 174 (1992) 2898-902.
  ORGANISM  Flavobacterium sp.
REFERENCE   3  [PMID:1512208]
  AUTHORS   Xun L, Topp E, Orser CS.
  TITLE     Confirmation of oxidative dehalogenation of pentachlorophenol by a
            Flavobacterium pentachlorophenol hydroxylase.
  JOURNAL   J. Bacteriol. 174 (1992) 5745-7.
  ORGANISM  Flavobacterium sp.
REFERENCE   4  [PMID:8619798]
  AUTHORS   Lange CC, Schneider BJ, Orser CS.
  TITLE     Verification of the role of PCP 4-monooxygenase in chlorine
            elimination from pentachlorophenol by Flavobacterium sp. strain ATCC
            39723.
  JOURNAL   Biochem. Biophys. Res. Commun. 219 (1996) 146-9.
  ORGANISM  Flavobacterium sp.
REFERENCE   5  [PMID:15262224]
  AUTHORS   Nakamura T, Motoyama T, Hirono S, Yamaguchi I.
  TITLE     Identification, characterization, and site-directed mutagenesis of
            recombinant pentachlorophenol 4-monooxygenase.
  JOURNAL   Biochim. Biophys. Acta. 1700 (2004) 151-9.
  ORGANISM  Sphingobium chlorophenolicum
PATHWAY     PATH: map00627  1,4-Dichlorobenzene degradation
ORTHOLOGY   KO: K03391  pentachlorophenol monooxygenase
GENES       ABO: ABO_0660
            BUR: Bcep18194_A4123 Bcep18194_A4142 Bcep18194_B0743
                 Bcep18194_B1484
            MMC: Mmcs_2852
            MKM: Mkms_2896
            MJL: Mjls_2883
            CGL: NCgl1111(cgl1158)
            RHA: RHA1_ro01939 RHA1_ro03540
            FRA: Francci3_2901
            FAL: FRAAL2325
            SEN: SACE_3057 SACE_3947 SACE_4082
            AVA: Ava_2049
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.50
            ExPASy - ENZYME nomenclature database: 1.14.13.50
            ExplorEnz - The Enzyme Database: 1.14.13.50
            ERGO genome analysis and discovery system: 1.14.13.50
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.50
            BRENDA, the Enzyme Database: 1.14.13.50
            CAS: 124148-88-5
///
ENTRY       EC 1.14.13.51               Enzyme
NAME        6-oxocineole dehydrogenase;
            6-oxocineole oxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     6-oxocineole,NADPH:oxygen oxidoreductase
REACTION    6-oxocineole + NADPH + H+ + O2 =
            1,6,6-trimethyl-2,7-dioxabicyclo[3.2.2]nonan-3-one + NADP+ + H2O
            [RN:R02995]
ALL_REAC    R02995
SUBSTRATE   6-oxocineole [CPD:C00848];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     1,6,6-trimethyl-2,7-dioxabicyclo[3.2.2]nonan-3-one [CPD:C04718];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     The product undergoes non-enzymic cleavage and subsequent ring
            closure to form the lactone
            4,5-dihydro-5,5-dimethyl-4-(3-oxobutyl)furan-2(3H)-one.
REFERENCE   1
  AUTHORS   Williams, D.R., Trudgill, P.W. and Taylor, D.G.
  TITLE     Metabolism of 1,8-cineole by Rhodococcus species: ring cleavage
            reactions.
  JOURNAL   J. Gen. Microbiol. 135 (1989) 1957-1967.
  ORGANISM  Rhodococcus sp.
PATHWAY     PATH: map00900  Terpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.51
            ExPASy - ENZYME nomenclature database: 1.14.13.51
            ExplorEnz - The Enzyme Database: 1.14.13.51
            ERGO genome analysis and discovery system: 1.14.13.51
            BRENDA, the Enzyme Database: 1.14.13.51
            CAS: 122933-80-6
///
ENTRY       EC 1.14.13.52               Enzyme
NAME        isoflavone 3'-hydroxylase;
            isoflavone 3'-monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     formononetin,NADPH:oxygen oxidoreductase (3'-hydroxylating)
REACTION    formononetin + NADPH + H+ + O2 = calycosin + NADP+ + H2O [RN:R03006]
ALL_REAC    R03006;
            (other) R07776
SUBSTRATE   formononetin [CPD:C00858];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     calycosin [CPD:C01562];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A heme-thiolate protein (P-450). Also acts on biochanin A and other
            isoflavones with a 4'-methoxy group. Involved in the biosynthesis of
            the pterocarpin phytoalexins medicarpin and maackiain.
REFERENCE   1
  AUTHORS   Hinderer, W., Flentje, U. and Barz, W.
  TITLE     Microsomal isoflavone 2'-hydroxylases and 3'-hydroxylases from
            chickpea (Cicer arietinum L) cell-suspensions induced for
            pterocarpan phytoalexin formation.
  JOURNAL   FEBS Lett. 214 (1987) 101-106.
  ORGANISM  Cicer arietinum
PATHWAY     PATH: map00943  Isoflavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.52
            ExPASy - ENZYME nomenclature database: 1.14.13.52
            ExplorEnz - The Enzyme Database: 1.14.13.52
            ERGO genome analysis and discovery system: 1.14.13.52
            BRENDA, the Enzyme Database: 1.14.13.52
            CAS: 110183-50-1
///
ENTRY       EC 1.14.13.53               Enzyme
NAME        4'-methoxyisoflavone 2'-hydroxylase;
            isoflavone 2'-monooxygenase (ambiguous);
            isoflavone 2'-hydroxylase (ambiguous)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     formononetin,NADPH:oxygen oxidoreductase (2'-hydroxylating)
REACTION    formononetin + NADPH + H+ + O2 = 2'-hydroxyformononetin + NADP+ +
            H2O [RN:R06560]
ALL_REAC    R06560;
            (other) R06561
SUBSTRATE   formononetin [CPD:C00858];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     2'-hydroxyformononetin [CPD:C02920];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A heme-thiolate protein (P-450). Acts on isoflavones with a
            4'-methoxy group, such as formononetin and biochanin A. Involved in
            the biosynthesis of the pterocarpin phytoalexins medicarpin and
            maackiain. EC 1.14.13.89, isoflavone 2'-hydroxylase, is less
            specific and acts on other isoflavones as well as
            4'-methoxyisoflavones.
REFERENCE   1
  AUTHORS   Hinderer, W., Flentje, U. and Barz, W.
  TITLE     Microsomal isoflavone 2'-hydroxylases and 3'-hydroxylases from
            chickpea (Cicer arietinum L) cell-suspensions induced for
            pterocarpan phytoalexin formation.
  JOURNAL   FEBS Lett. 214 (1987) 101-106.
  ORGANISM  Cicer arietinum
PATHWAY     PATH: map00943  Isoflavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.53
            ExPASy - ENZYME nomenclature database: 1.14.13.53
            ExplorEnz - The Enzyme Database: 1.14.13.53
            ERGO genome analysis and discovery system: 1.14.13.53
            BRENDA, the Enzyme Database: 1.14.13.53
            CAS: 110183-49-8
///
ENTRY       EC 1.14.13.54               Enzyme
NAME        ketosteroid monooxygenase;
            steroid-ketone monooxygenase;
            progesterone, NADPH2:oxygen oxidoreductase (20-hydroxylating,
            ester-producing);
            17alpha-hydroxyprogesterone, NADPH2:oxygen oxidoreductase
            (20-hydroxylating, side-chain cleaving);
            androstenedione, NADPH2:oxygen oxidoreductase (17-hydroxylating,
            lactonizing)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     ketosteroid,NADPH:oxygen oxidoreductase (20-hydroxylating,
            ester-producing/20-hydroxylating, side-chain
            cleaving/17-hydroxylating, lactonizing)
REACTION    (1) ketosteroid + NADPH + H+ + O2 = steroid ester/lactone + NADP+ +
            H2O [RN:R07192 R07193];
            (2) progesterone + NADPH + H+ + O2 = testosterone acetate + NADP+ +
            H2O;
            (3) androstenedione + NADPH + H+ + O2 = testololactone + NADP+ +
            H2O;
            (4) 17alpha-hydroxyprogesterone + NADPH + H+ + O2 = androstenedione
            + acetate + NADP+ + H2O
ALL_REAC    R07192 > R02210;
            R07193
SUBSTRATE   ketosteroid [CPD:C06479];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007];
            progesterone [CPD:C00410];
            androstenedione [CPD:C00280];
            17alpha-hydroxyprogesterone [CPD:C01176]
PRODUCT     steroid ester [CPD:C15506];
            steroid lactone [CPD:C15507];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            testosterone acetate [CPD:C03027];
            testololactone [CPD:C04676];
            androstenedione [CPD:C00280];
            acetate [CPD:C00033]
COMMENT     A single FAD-containing enzyme catalyses three types of
            monooxygenase (Baeyer-Villiger oxidation) reaction. The oxidative
            esterification of a number of derivatives of progesterone to produce
            the corresponding 17alpha-hydroxysteroid 17-acetate ester, such as
            testosterone acetate, is shown in Reaction (1). The oxidative
            lactonization of a number of derivatives of androstenedione to
            produce the 13,17-secoandrosteno-17,13alpha-lactone, such as
            testololactone, is shown in Reaction (2). The oxidative cleavage of
            the 17beta-side-chain of 17alpha-hydroxyprogesterone to produce
            androstenedione and acetate is shown in Reaction (3). Reaction (1)
            is also catalysed by EC 1.14.99.4 (progesterone monooxygenase), and
            Reactions (2) and (3) correspond to that catalysed by EC 1.14.99.12
            (androst-4-ene-3,17-dione monooxygenase). The possibility that a
            single enzyme is responsible for the reactions ascribed to EC
            1.14.99.4 and EC 1.14.99.12 in other tissues cannot be excluded.
REFERENCE   1
  AUTHORS   Katagiri, M. and Itagaki, E.
  TITLE     A steroid ketone monooxygenase from Cylindrocarpon radicicola.
  JOURNAL   In: Muller, F. (Ed.), Chemistry and Biochemistry of Flavoenzymes,
            CRC Press, Florida, 1991, p. 102-108.
REFERENCE   2  [PMID:3486863]
  AUTHORS   Itagaki E.
  TITLE     Studies on steroid monooxygenase from Cylindrocarpon radicicola ATCC
            11011. Purification and characterization.
  JOURNAL   J. Biochem. (Tokyo). 99 (1986) 815-24.
  ORGANISM  Cylindrocarpon radicicola
REFERENCE   3  [PMID:3486864]
  AUTHORS   Itagaki E.
  TITLE     Studies on steroid monooxygenase from Cylindrocarpon radicicola ATCC
            11011. Oxygenative lactonization of androstenedione to
            testololactone.
  JOURNAL   J. Biochem. (Tokyo). 99 (1986) 825-32.
  ORGANISM  Cylindrocarpon radicicola
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.54
            ExPASy - ENZYME nomenclature database: 1.14.13.54
            ExplorEnz - The Enzyme Database: 1.14.13.54
            ERGO genome analysis and discovery system: 1.14.13.54
            BRENDA, the Enzyme Database: 1.14.13.54
            CAS: 9044-53-5
///
ENTRY       EC 1.14.13.55               Enzyme
NAME        protopine 6-monooxygenase;
            protopine 6-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     protopine,NADPH:oxygen oxidoreductase (6-hydroxylating)
REACTION    protopine + NADPH + H+ + O2 = 6-hydroxyprotopine + NADP+ + H2O
            [RN:R04699]
ALL_REAC    R04699
SUBSTRATE   protopine [CPD:C05189];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     6-hydroxyprotopine [CPD:C05190];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450) involved in benzophenanthridine
            alkaloid synthesis in higher plants.
REFERENCE   1
  AUTHORS   Tanahashi, T. and Zenk, M.H.
  TITLE     Elicitor induction and characterization of microsomal
            protopine-6-hydroxylase, the central enzyme in benzophenanthridine
            alkaloid biosynthesis.
  JOURNAL   Phytochemistry 29 (1990) 1113-1122.
  ORGANISM  Eschscholzia californica
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.55
            ExPASy - ENZYME nomenclature database: 1.14.13.55
            ExplorEnz - The Enzyme Database: 1.14.13.55
            ERGO genome analysis and discovery system: 1.14.13.55
            BRENDA, the Enzyme Database: 1.14.13.55
            CAS: 128561-60-4
///
ENTRY       EC 1.14.13.56               Enzyme
NAME        dihydrosanguinarine 10-monooxygenase;
            dihydrosanguinarine 10-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     dihydrosanguinarine,NADPH:oxygen oxidoreductase (10-hydroxylating)
REACTION    dihydrosanguinarine + NADPH + H+ + O2 =
            10-hydroxydihydrosanguinarine + NADP+ + H2O [RN:R04702]
ALL_REAC    R04702
SUBSTRATE   dihydrosanguinarine [CPD:C05191];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     10-hydroxydihydrosanguinarine [CPD:C05247];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450) involved in benzophenanthridine
            alkaloid synthesis in higher plants.
REFERENCE   1
  AUTHORS   De-Eknamkul, W., Tanahashi, T. and Zenk, M.H.
  TITLE     Enzymic 10-hydroxylation and 10-O-methylation of dihydrosanguinarine
            in dihydrochelirubine formation by Eschscholtzia.
  JOURNAL   Phytochemistry 31 (1992) 2713-2717.
  ORGANISM  Eschscholzia californica
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.56
            ExPASy - ENZYME nomenclature database: 1.14.13.56
            ExplorEnz - The Enzyme Database: 1.14.13.56
            ERGO genome analysis and discovery system: 1.14.13.56
            BRENDA, the Enzyme Database: 1.14.13.56
            CAS: 144388-41-0
///
ENTRY       EC 1.14.13.57               Enzyme
NAME        dihydrochelirubine 12-monooxygenase;
            dihydrochelirubine 12-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     dihydrochelirubine,NADPH:oxygen oxidoreductase (12-hydroxylating)
REACTION    dihydrochelirubine + NADPH + H+ + O2 = 12-hydroxydihydrochelirubine
            + NADP+ + H2O [RN:R04708]
ALL_REAC    R04708
SUBSTRATE   dihydrochelirubine [CPD:C05194];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     12-hydroxydihydrochelirubine [CPD:C05193];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450)
REFERENCE   1
  AUTHORS   Kammerer, L., De-Eknamkul, W. and Zenk, M.H.
  TITLE     Enzymic 12-hydroxylation and 12-O-methylation of dihydrochelirubine
            in dihydromacarpine formation by Thalictrum bulgaricum.
  JOURNAL   Phytochemistry 36 (1994) 1409-1416.
  ORGANISM  Thalictrum bulgaricum
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.57
            ExPASy - ENZYME nomenclature database: 1.14.13.57
            ExplorEnz - The Enzyme Database: 1.14.13.57
            ERGO genome analysis and discovery system: 1.14.13.57
            BRENDA, the Enzyme Database: 1.14.13.57
            CAS: 158736-41-5
///
ENTRY       EC 1.14.13.58               Enzyme
NAME        benzoyl-CoA 3-monooxygenase;
            benzoyl-CoA 3-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     benzoyl-CoA,NADPH:oxygen oxidoreductase (3-hydroxylating)
REACTION    benzoyl-CoA + NADPH + H+ + O2 = 3-hydroxybenzoyl-CoA + NADP+ + H2O
            [RN:R02449]
ALL_REAC    R02449
SUBSTRATE   benzoyl-CoA [CPD:C00512];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     3-hydroxybenzoyl-CoA [CPD:C05195];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     The enzyme from the denitrifying bacterium Pseudomonas KB740
            catalyses a flavin-requiring reaction (FAD or FMN). Benzoate is not
            a substrate.
REFERENCE   1  [PMID:7851381]
  AUTHORS   Niemetz R, Altenschmidt U, Brucker S, Fuchs G.
  TITLE     Benzoyl-coenzyme-A 3-monooxygenase, a flavin-dependent hydroxylase.
            Purification, some properties and its role in aerobic benzoate
            oxidation via gentisate in a denitrifying bacterium.
  JOURNAL   Eur. J. Biochem. 227 (1995) 161-8.
  ORGANISM  Pseudomonas sp.
GENES       REH: H16_A1408(bdxA)
            AZO: azo3058(boxA)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.58
            ExPASy - ENZYME nomenclature database: 1.14.13.58
            ExplorEnz - The Enzyme Database: 1.14.13.58
            ERGO genome analysis and discovery system: 1.14.13.58
            BRENDA, the Enzyme Database: 1.14.13.58
            CAS: 151616-61-4
///
ENTRY       EC 1.14.13.59               Enzyme
NAME        L-lysine 6-monooxygenase (NADPH);
            lysine N6-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     L-lysine,NADPH:oxygen oxidoreductase (6-hydroxylating)
REACTION    L-lysine + NADPH + H+ + O2 = N6-hydroxy-L-lysine + NADP+ + H2O
            [RN:R00448]
ALL_REAC    R00448
SUBSTRATE   L-lysine [CPD:C00047];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     N6-hydroxy-L-lysine [CPD:C01028];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A flavoprotein (FAD). The enzyme from strain EN 222 of Escherichia
            coli is highly specific for L-lysine; L-ornithine and L-homolysine
            are, for example, not substrates.
REFERENCE   1  [PMID:2518519]
  AUTHORS   Plattner HJ, Pfefferle P, Romaguera A, Waschutza S, Diekmann H.
  TITLE     Isolation and some properties of lysine N6-hydroxylase from
            Escherichia coli strain EN222.
  JOURNAL   Biol. Met. 2 (1989) 1-5.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:8504838]
  AUTHORS   Macheroux P, Plattner HJ, Romaguera A, Diekmann H.
  TITLE     FAD and substrate analogs as probes for lysine N6-hydroxylase from
            Escherichia coli EN 222.
  JOURNAL   Eur. J. Biochem. 213 (1993) 995-1002.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:8218389]
  AUTHORS   Thariath AM, Fatum KL, Valvano MA, Viswanatha T.
  TITLE     Physico-chemical characterization of a recombinant cytoplasmic form
            of lysine: N6-hydroxylase.
  JOURNAL   Biochim. Biophys. Acta. 1203 (1993) 27-35.
  ORGANISM  Escherichia coli [GN:eco], Enterobacter aerogenes
REFERENCE   4  [PMID:2935523]
  AUTHORS   de Lorenzo V, Bindereif A, Paw BH, Neilands JB.
  TITLE     Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in
            Escherichia coli K-12.
  JOURNAL   J. Bacteriol. 165 (1986) 570-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5
  AUTHORS   Marrone, L., Siemann, S., Beecroft, M. and Viswanatha, T.
  TITLE     Specificity of lysine:N-6-hydroxylase: A hypothesis for a reactive
            substrate intermediate in the catalytic mechanism.
  JOURNAL   Bioorg. Chem. 24 (1996) 401-406.
REFERENCE   6  [PMID:2493814]
  AUTHORS   Goh CJ, Szczepan EW, Menhart N, Viswanatha T.
  TITLE     Studies on lysine:N6-hydroxylation by cell-free systems of
            Aerobacter aerogenes 62-1.
  JOURNAL   Biochim. Biophys. Acta. 990 (1989) 240-5.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K03897  lysine N6-hydroxylase
GENES       ECC: c3624(iucD)
            YPE: YPO0993(iucD)
            YPK: y3384(iucD)
            YPM: YP_3447(iucD)
            YPA: YPA_0271 YPA_0824
            YPN: YPN_2450 YPN_3191
            YPP: YPDSF_0525 YPDSF_1446
            YPS: YPTB3266(iucD)
            SFL: SF3718(iucD)
            SFX: S4053(iucD)
            SFV: SFV_3851(iucD)
            SSN: SSON_3604(iucD)
            SBO: SBO_4340(iucD)
            SPE: Spro_0025 Spro_0919 Spro_2520
            VFI: VFA0164
            PST: PSPTO_0211(iucD)
            PEN: PSEEN0980 PSEEN2502(basC)
            SBL: Sbal_2708
            SBM: Shew185_2730
            SPC: Sputcn32_2411
            SHE: Shewmr4_1454
            SHM: Shewmr7_1520
            SHN: Shewana3_1510
            SHW: Sputw3181_1597
            LPF: lpl1946(iucD)
            NOC: Noc_1811
            CSA: Csal_1054
            MMW: Mmwyl1_1630
            BUR: Bcep18194_A4789
            AAV: Aave_4219
            NMU: Nmul_A1825
            BBA: Bd1573
            RET: RHE_PF00456(vbsO)
            RLE: pRL120314
            OAN: Oant_3254
            GBE: GbCGDNIH1_2375
            BPU: BPUM_1023
            MBO: Mb2399c(mbtG)
            MBB: BCG_2392c(mbtG)
            CJK: jk1814(mbtG)
            RHA: RHA1_ro04716 RHA1_ro08654
            ART: Arth_0286
            FRA: Francci3_3275 Francci3_4057
            STP: Strop_2550
            RXY: Rxyl_0408
            AVA: Ava_2835
            FJO: Fjoh_3173
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.59
            ExPASy - ENZYME nomenclature database: 1.14.13.59
            ExplorEnz - The Enzyme Database: 1.14.13.59
            ERGO genome analysis and discovery system: 1.14.13.59
            BRENDA, the Enzyme Database: 1.14.13.59
            CAS: 64295-82-5
///
ENTRY       EC 1.14.13.60               Enzyme
NAME        27-hydroxycholesterol 7alpha-monooxygenase;
            27-hydroxycholesterol 7alpha-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     27-hydroxycholesterol,NADPH:oxygen oxidoreductase
            (7alpha-hydroxylating)
REACTION    27-hydroxycholesterol + NADPH + H+ + O2 =
            7alpha,27-dihydroxycholesterol + NADP+ + H2O [RN:R05160]
ALL_REAC    R05160
SUBSTRATE   27-hydroxycholesterol [CPD:C06340];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     7alpha,27-dihydroxycholesterol [CPD:C06341];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    Heme-thiolate(P-450) [CPD:C05009]
COMMENT     A heme-thiolate protein (P-450). The enzyme from mammalian liver
            differs from cholesterol 7alpha-monooxygenase (EC 1.14.13.17) in
            having no activity towards cholesterol.
REFERENCE   1
  AUTHORS   Kumiko, O.M., Budai, K. and Javitt, N.B.
  TITLE     Cholesterol and 27-hydroxycholesterol 7alpha-hydroxylation: evidence
            for two different enzymes.
  JOURNAL   J. Lipid Res. 34 (1993) 581-588.
  ORGANISM  hamster
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.60
            ExPASy - ENZYME nomenclature database: 1.14.13.60
            ExplorEnz - The Enzyme Database: 1.14.13.60
            ERGO genome analysis and discovery system: 1.14.13.60
            BRENDA, the Enzyme Database: 1.14.13.60
            CAS: 149316-80-3
///
ENTRY       EC 1.14.13.61               Enzyme
NAME        2-hydroxyquinoline 8-monooxygenase;
            2-oxo-1,2-dihydroquinoline 8-monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     quinolin-2(1H)-one,NADH:oxygen oxidoreductase (8-oxygenating)
REACTION    quinolin-2-ol + NADH + H+ + O2 = quinolin-2,8-diol + NAD+ + H2O
            [RN:R05158]
ALL_REAC    R05158
SUBSTRATE   quinolin-2-ol [CPD:C06338];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     quinolin-2,8-diol [CPD:C06342];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires iron. Quinolin-2-ol exists largely as the
            quinolin-2(1H)-one tautomer.
REFERENCE   1  [PMID:7629085]
  AUTHORS   Rosche B, Tshisuaka B, Fetzner S, Lingens F.
  TITLE     2-Oxo-1,2-dihydroquinoline 8-monooxygenase, a two-component enzyme
            system from Pseudomonas putida 86.
  JOURNAL   J. Biol. Chem. 270 (1995) 17836-42.
  ORGANISM  Pseudomonas putida [GN:ppu]
GENES       AZO: azo1960(oxoR)
STRUCTURES  PDB: 1Z01  1Z02  1Z03  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.61
            ExPASy - ENZYME nomenclature database: 1.14.13.61
            ExplorEnz - The Enzyme Database: 1.14.13.61
            ERGO genome analysis and discovery system: 1.14.13.61
            BRENDA, the Enzyme Database: 1.14.13.61
///
ENTRY       EC 1.14.13.62               Enzyme
NAME        4-hydroxyquinoline 3-monooxygenase;
            quinolin-4(1H)-one 3-monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     quinolin-4(1H)-one,NADH:oxygen oxidoreductase (3-oxygenating)
REACTION    quinolin-4-ol + NADH + H+ + O2 = quinolin-3,4-diol + NAD+ + H2O
            [RN:R05154]
ALL_REAC    R05154
SUBSTRATE   quinolin-4-ol [CPD:C06343];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     quinolin-3,4-diol;
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
COMMENT     Quinolin-4-ol exists largely as the quinolin-4(1H)-one tautomer.
REFERENCE   1  [PMID:1627263]
  AUTHORS   Block DW, Lingens F.
  TITLE     Microbial metabolism of quinoline and related compounds. XIII.
            Purification and properties of 1H-4-oxoquinoline monooxygenase from
            Pseudomonas putida strain 33/1.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 373 (1992) 249-54.
  ORGANISM  Pseudomonas putida [GN:ppu]
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.62
            ExPASy - ENZYME nomenclature database: 1.14.13.62
            ExplorEnz - The Enzyme Database: 1.14.13.62
            ERGO genome analysis and discovery system: 1.14.13.62
            BRENDA, the Enzyme Database: 1.14.13.62
            CAS: 144378-37-0
///
ENTRY       EC 1.14.13.63               Enzyme
NAME        3-hydroxyphenylacetate 6-hydroxylase;
            3-hydroxyphenylacetate 6-monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     3-hydroxyphenylacetate,NAD(P)H:oxygen oxidoreductase
            (6-hydroxylating)
REACTION    3-hydroxyphenylacetate + NAD(P)H + H+ + O2 =
            2,5-dihydroxyphenylacetate + NAD(P)+ + H2O [RN:R02515 R02517]
ALL_REAC    R02515 R02517
SUBSTRATE   3-hydroxyphenylacetate [CPD:C05593];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     2,5-dihydroxyphenylacetate [CPD:C00544];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     3-hydroxyphenylacetate 6-hydroxylase from Flavobacterium sp. is
            highly specific for 3-hydroxyphenylacetate and uses NADH and NADPH
            as electron donors with similar efficiency.
REFERENCE   1  [PMID:1935954]
  AUTHORS   Van Berkel WJ, Van Den Tweel WJ.
  TITLE     Purification and characterisation of 3-hydroxyphenylacetate
            6-hydroxylase: a novel FAD-dependent monooxygenase from a
            Flavobacterium species.
  JOURNAL   Eur. J. Biochem. 201 (1991) 585-92.
  ORGANISM  Flavobacterium sp.
PATHWAY     PATH: map00643  Styrene degradation
ORTHOLOGY   KO: K10438  3-hydroxyphenylacetate 6-hydroxylase
GENES       ANI: AN1397.2
            AFM: AFUA_1G08800
            AOR: AO090005001647
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.63
            ExPASy - ENZYME nomenclature database: 1.14.13.63
            ExplorEnz - The Enzyme Database: 1.14.13.63
            ERGO genome analysis and discovery system: 1.14.13.63
            BRENDA, the Enzyme Database: 1.14.13.63
            CAS: 114705-01-0
///
ENTRY       EC 1.14.13.64               Enzyme
NAME        4-hydroxybenzoate 1-hydroxylase;
            4-hydroxybenzoate 1-monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (1-hydroxylating,
            decarboxylating)
REACTION    4-hydroxybenzoate + NAD(P)H + 2 H+ + O2 = hydroquinone + NAD(P)+ +
            H2O + CO2 [RN:R01297 R01299]
ALL_REAC    R01297 R01299
SUBSTRATE   4-hydroxybenzoate [CPD:C00156];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     hydroquinone [CPD:C00530];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            CO2 [CPD:C00011]
COFACTOR    FAD [CPD:C00016]
COMMENT     Requires FAD. The enzyme from Candida parapsilosis is specific for
            4-hydroxybenzoate derivatives and prefers NADH to NADPH as electron
            donor.
REFERENCE   1  [PMID:7926672]
  AUTHORS   van Berkel WJ, Eppink MH, Middelhoven WJ, Vervoort J, Rietjens IM.
  TITLE     Catabolism of 4-hydroxybenzoate in Candida parapsilosis proceeds
            through initial oxidative decarboxylation by a FAD-dependent
            4-hydroxybenzoate 1-hydroxylase.
  JOURNAL   FEMS. Microbiol. Lett. 121 (1994) 207-15.
  ORGANISM  Candida parapsilosis
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.64
            ExPASy - ENZYME nomenclature database: 1.14.13.64
            ExplorEnz - The Enzyme Database: 1.14.13.64
            ERGO genome analysis and discovery system: 1.14.13.64
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.64
            BRENDA, the Enzyme Database: 1.14.13.64
            CAS: 134214-78-1
///
ENTRY       EC 1.14.13.65     Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
COMMENT     Deleted entry: 2-hydroxyquinoline 8-monooxygenase (EC 1.14.13.65
            created 1999, deleted 2006)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.65
            ExPASy - ENZYME nomenclature database: 1.14.13.65
            ExplorEnz - The Enzyme Database: 1.14.13.65
            ERGO genome analysis and discovery system: 1.14.13.65
            BRENDA, the Enzyme Database: 1.14.13.65
///
ENTRY       EC 1.14.13.66               Enzyme
NAME        2-hydroxycyclohexanone 2-monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     2-hydroxycyclohexan-1-one,NADPH:oxygen 2-oxidoreductase
            (1,2-lactonizing)
REACTION    2-hydroxycyclohexan-1-one + NADPH + H+ + O2 = 6-hydroxyhexan-6-olide
            + NADP+ + H2O [RN:R03281]
ALL_REAC    R03281
SUBSTRATE   2-hydroxycyclohexan-1-one [CPD:C01147];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     6-hydroxyhexan-6-olide [CPD:C03241];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:856571]
  AUTHORS   Davey JF, Trudgill PW.
  TITLE     The metabolism of trans-cyclohexan-1,2-diol by an Acinetobacter
            species.
  JOURNAL   Eur. J. Biochem. 74 (1977) 115-27.
  ORGANISM  Acinetobacter sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.66
            ExPASy - ENZYME nomenclature database: 1.14.13.66
            ExplorEnz - The Enzyme Database: 1.14.13.66
            ERGO genome analysis and discovery system: 1.14.13.66
            BRENDA, the Enzyme Database: 1.14.13.66
            CAS: 62628-31-3
///
ENTRY       EC 1.14.13.67               Enzyme
NAME        quinine 3-monooxygenase;
            quinine 3-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     quinine,NADPH:oxygen oxidoreductase
REACTION    quinine + NADPH + H+ + O2 = 3-hydroxyquinine + NADP+ + H2O
            [RN:R05727]
ALL_REAC    R05727
SUBSTRATE   quinine [CPD:C06526];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     3-hydroxyquinine [CPD:C07344];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:1578365]
  AUTHORS   Relling MV, Evans R, Dass C, Desiderio DM, Nemec J.
  TITLE     Human cytochrome P450 metabolism of teniposide and etoposide.
  JOURNAL   J. Pharmacol. Exp. Ther. 261 (1992) 491-6.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:9088578]
  AUTHORS   Zhang H, Coville PF, Walker RJ, Miners JO, Birkett DJ, Wanwimolruk
            S.
  TITLE     Evidence for involvement of human CYP3A in the 3-hydroxylation of
            quinine.
  JOURNAL   Br. J. Clin. Pharmacol. 43 (1997) 245-52.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:9456308]
  AUTHORS   Zhao XJ, Kawashiro T, Ishizaki T.
  TITLE     Mutual inhibition between quinine and etoposide by human liver
            microsomes. Evidence for cytochrome P4503A4 involvement in their
            major metabolic pathways.
  JOURNAL   Drug. Metab. Dispos. 26 (1998) 188-91.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:8968357]
  AUTHORS   Zhao XJ, Yokoyama H, Chiba K, Wanwimolruk S, Ishizaki T.
  TITLE     Identification of human cytochrome P450 isoforms involved in the
            3-hydroxylation of quinine by human live microsomes and nine
            recombinant human cytochromes P450.
  JOURNAL   J. Pharmacol. Exp. Ther. 279 (1996) 1327-34.
  ORGANISM  human [GN:hsa]
STRUCTURES  PDB: 1W0E  1W0F  1W0G  2J0D  2V0M  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.67
            ExPASy - ENZYME nomenclature database: 1.14.13.67
            ExplorEnz - The Enzyme Database: 1.14.13.67
            ERGO genome analysis and discovery system: 1.14.13.67
            BRENDA, the Enzyme Database: 1.14.13.67
///
ENTRY       EC 1.14.13.68               Enzyme
NAME        4-hydroxyphenylacetaldehyde oxime monooxygenase;
            4-hydroxybenzeneacetaldehyde oxime monooxygenase;
            cytochrome P450II-dependent monooxygenase;
            NADPH-cytochrome P450 reductase (CYP71E1);
            CYP71E1;
            4-hydroxyphenylacetaldehyde oxime,NADPH:oxygen oxidoreductase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     (Z)-4-hydroxyphenylacetaldehyde oxime,NADPH:oxygen oxidoreductase
REACTION    (Z)-4-hydroxyphenylacetaldehyde oxime + NADPH + H+ + O2 =
            (S)-4-hydroxymandelonitrile + NADP+ + 2 H2O [RN:R05728]
ALL_REAC    R05728
SUBSTRATE   (Z)-4-hydroxyphenylacetaldehyde oxime;
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (S)-4-hydroxymandelonitrile [CPD:C03742];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     This enzyme is involved in the biosynthesis of the cyanogenic
            glucoside dhurrin in sorghum, along with EC 1.14.13.41, tyrosine
            N-monooxygenase and EC 2.4.1.85, cyanohydrin
            beta-glucosyltransferase.
REFERENCE   1  [PMID:237909]
  AUTHORS   MacFarlane IJ, Lees EM, Conn EE.
  TITLE     The in vitro biosynthesis of dhurrin, the cyanogenic glycoside of
            Sorghum bicolor.
  JOURNAL   J. Biol. Chem. 250 (1975) 4708-13.
  ORGANISM  Sorghum bicolor [GN:esbi]
REFERENCE   2  [PMID:193443]
  AUTHORS   Shimada M, Conn EE.
  TITLE     The enzymatic conversion of p-hydroxyphenylacetaldoxime to
            p-hydroxymandelonitrile.
  JOURNAL   Arch. Biochem. Biophys. 180 (1977) 199-207.
  ORGANISM  Sorghum sp.
REFERENCE   3  [PMID:12114576]
  AUTHORS   Busk PK, Moller BL.
  TITLE     Dhurrin synthesis in sorghum is regulated at the transcriptional
            level and induced by nitrogen fertilization in older plants.
  JOURNAL   Plant. Physiol. 129 (2002) 1222-31.
  ORGANISM  Sorghum bicolor [GN:esbi]
REFERENCE   4  [PMID:15665094]
  AUTHORS   Kristensen C, Morant M, Olsen CE, Ekstrom CT, Galbraith DW, Moller
            BL, Bak S.
  TITLE     Metabolic engineering of dhurrin in transgenic Arabidopsis plants
            with marginal inadvertent effects on the metabolome and
            transcriptome.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 1779-84.
  ORGANISM  Arabidopsis thaliana [GN:ath]
PATHWAY     PATH: map00350  Tyrosine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.68
            ExPASy - ENZYME nomenclature database: 1.14.13.68
            ExplorEnz - The Enzyme Database: 1.14.13.68
            ERGO genome analysis and discovery system: 1.14.13.68
            BRENDA, the Enzyme Database: 1.14.13.68
///
ENTRY       EC 1.14.13.69               Enzyme
NAME        alkene monooxygenase;
            alkene epoxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     alkene,NADH:oxygen oxidoreductase
REACTION    propene + NADH + H+ + O2 = 1,2-epoxypropane + NAD+ + H2O [RN:R07194]
ALL_REAC    R07194 > R05729 R05730;
            (other) R05444
SUBSTRATE   propene [CPD:C11505];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     1,2-epoxypropane [CPD:C15508];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
COMMENT     The enzyme from Xanthobacter sp. strain Py2 is a multicomponent
            enzyme comprising (1) an NADH reductase, which provides the
            reductant for O2 activation; (2) a Rieske-type ferredoxin, which is
            an electron-transfer protein; (3) an oxygenase, which contains the
            catalytic centre for alkene epoxidation and (4) a small protein of
            unknown function that is essential for activity. Requires Fe(II).
            The enzyme oxygenates C2 to C6 aliphatic alkenes. With
            1,2-epoxypropane as substrate, the stereospecifity of the
            epoxypropane formed is 95% (R) and 5% (S).
REFERENCE   1  [PMID:9312093]
  AUTHORS   Small FJ, Ensign SA.
  TITLE     Alkene monooxygenase from Xanthobacter strain Py2. Purification and
            characterization of a four-component system central to the bacterial
            metabolism of aliphatic alkenes.
  JOURNAL   J. Biol. Chem. 272 (1997) 24913-20.
  ORGANISM  Xanthobacter sp.
REFERENCE   2  [PMID:10103255]
  AUTHORS   Zhou NY, Jenkins A, Chan Kwo Chion CK, Leak DJ.
  TITLE     The alkene monooxygenase from Xanthobacter strain Py2 is closely
            related to aromatic monooxygenases and catalyzes aromatic
            monohydroxylation of benzene, toluene, and phenol.
  JOURNAL   Appl. Environ. Microbiol. 65 (1999) 1589-95.
  ORGANISM  Xanthobacter sp.
REFERENCE   3  [PMID:9266707]
  AUTHORS   Gallagher SC, Cammack R, Dalton H.
  TITLE     Alkene monooxygenase from Nocardia corallina B-276 is a member of
            the class of dinuclear iron proteins capable of stereospecific
            epoxygenation reactions.
  JOURNAL   Eur. J. Biochem. 247 (1997) 635-41.
  ORGANISM  Nocardia corallina
PATHWAY     PATH: map00625  Tetrachloroethene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.69
            ExPASy - ENZYME nomenclature database: 1.14.13.69
            ExplorEnz - The Enzyme Database: 1.14.13.69
            ERGO genome analysis and discovery system: 1.14.13.69
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.69
            BRENDA, the Enzyme Database: 1.14.13.69
///
ENTRY       EC 1.14.13.70               Enzyme
NAME        sterol 14-demethylase;
            obtusufoliol 14-demethylase;
            lanosterol 14-demethylase;
            lanosterol 14alpha-demethylase;
            sterol 14alpha-demethylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     sterol,NADPH:oxygen oxidoreductase (14-methyl cleaving)
REACTION    obtusifoliol + 3 O2 + 3 NADPH + 3 H+ =
            4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate +
            3 NADP+ + 4 H2O [RN:R05731]
ALL_REAC    R05731;
            (other) R05640
SUBSTRATE   obtusifoliol [CPD:C01943];
            O2 [CPD:C00007];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
PRODUCT     4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol
            [CPD:C11508];
            formate [CPD:C00058];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     The heme-thiolate enzyme (P-450) catalyses successive hydroxylations
            of the 14alpha-methyl group and C-15, followed by elimination as
            formate leaving the 14(15) double bond. This enzyme acts on a range
            of steroids with a 14alpha-methyl group.
REFERENCE   1  [PMID:9076987]
  AUTHORS   Bak S, Kahn RA, Olsen CE, Halkier BA.
  TITLE     Cloning and expression in Escherichia coli of the obtusifoliol 14
            alpha-demethylase of Sorghum bicolor (L.) Moench, a cytochrome P450
            orthologous to the sterol 14 alpha-demethylases (CYP51) from fungi
            and mammals.
  JOURNAL   Plant. J. 11 (1997) 191-201.
  ORGANISM  Sorghum bicolor [GN:esbi]
REFERENCE   2  [PMID:1872829]
  AUTHORS   Aoyama Y, Yoshida Y.
  TITLE     Different substrate specificities of lanosterol 14a-demethylase
            (P-45014DM) of Saccharomyces cerevisiae and rat liver for
            24-methylene-24,25-dihydrolanosterol and 24,25-dihydrolanosterol.
  JOURNAL   Biochem. Biophys. Res. Commun. 178 (1991) 1064-71.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], rat [GN:rno]
REFERENCE   3  [PMID:1567403]
  AUTHORS   Aoyama Y, Yoshida Y.
  TITLE     The 4 beta-methyl group of substrate does not affect the activity of
            lanosterol 14 alpha-demethylase (P-450(14)DM) of yeast: difference
            between the substrate recognition by yeast and plant sterol 14
            alpha-demethylases.
  JOURNAL   Biochem. Biophys. Res. Commun. 183 (1992) 1266-72.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4
  AUTHORS   Alexander, K., Akhtar, M., Boar, R.B., McGhie, J.F. and Barton,
            D.H.R.
  TITLE     The removal of the 32-carbon atom as formic acid in cholesterol
            biosynthesis.
  JOURNAL   J. Chem. Soc. Chem. Commun. (1972) 383-385.
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K05917  cytochrome P450, family 51, subfamily A (sterol
                        14-demethylase)
GENES       HSA: 1595(CYP51A1)
            PTR: 463527(CYP51A1)
            MMU: 13121(Cyp51)
            RNO: 25427(Cyp51)
            CFA: 475225(LOC475225)
            BTA: 505060(CYP51)
            SSC: 403334(CYP51)
            GGA: 420548(CYP51)
            XLA: 447600(MGC84806)
            XTR: 548948(cyp51a1)
            DRE: 414331(cyp51)
            SPU: 414330(cyp51)
            ATH: AT1G11680(CYP51G1)
            OSA: 4338097 4338803 4350614
            CME: CMS319C
            SCE: YHR007C(ERG11)
            AGO: AGOS_ADR162W
            PIC: PICST_63421(CP51)
            CAL: CaO19_922(CaO19.922)
            CGR: CAGL0E04334g
            SPO: SPAC13A11.02c(cyp51)
            ANI: AN1901.2 AN8283.2
            AFM: AFUA_4G06890 AFUA_7G03740
            AOR: AO090003000205 AO090026000842
            CNE: CNA00300
            UMA: UM03662.1
            DDI: DDB_0232962(CYP51)
            TET: TTHERM_01398470
            TBR: Tb11.02.4080
            TCR: 506297.260 510101.50
            LMA: LmjF11.1100
            MCA: MCA2711(cyp51)
            MTU: Rv0764c(cyp51)
            MTC: MT0788
            MBO: Mb0787c(cyp51)
            MBB: BCG_0816c(cyp51)
            MPA: MAP0598c
            MAV: MAV_0708
            MSM: MSMEG_5863
            MUL: MUL_0473(cyp51B1)
            MVA: Mvan_5161
            MMC: Mmcs_4582
            NFA: nfa25890(cyp51)
            RHA: RHA1_ro03076 RHA1_ro04671
            SEN: SACE_3928(cyp51)
STRUCTURES  PDB: 1H5Z  1U13  1X8V  2BZ9  2CI0  2CIB  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.70
            ExPASy - ENZYME nomenclature database: 1.14.13.70
            ExplorEnz - The Enzyme Database: 1.14.13.70
            ERGO genome analysis and discovery system: 1.14.13.70
            BRENDA, the Enzyme Database: 1.14.13.70
///
ENTRY       EC 1.14.13.71               Enzyme
NAME        N-methylcoclaurine 3'-monooxygenase;
            N-methylcoclaurine 3'-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     (S)-N-methylcoclaurine,NADPH:oxygen oxidoreductase
            (3'-hydroxylating)
REACTION    (S)-N-methylcoclaurine + NADPH + H+ + O2 =
            (S)-3'-hydroxy-N-methylcoclaurine + NADP+ + H2O [RN:R05732]
ALL_REAC    R05732
SUBSTRATE   (S)-N-methylcoclaurine [CPD:C05176];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (S)-3'-hydroxy-N-methylcoclaurine [CPD:C05202];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450) involved in benzylisoquinoline
            alkaloid synthesis in higher plants.
REFERENCE   1  [PMID:9681018]
  AUTHORS   Pauli HH, Kutchan TM.
  TITLE     Molecular cloning and functional heterologous expression of two
            alleles encoding (S)-N-methylcoclaurine 3'-hydroxylase (CYP80B1), a
            new methyl jasmonate-inducible cytochrome P-450-dependent
            mono-oxygenase of benzylisoquinoline alkaloid biosynthesis.
  JOURNAL   Plant. J. 13 (1998) 793-801.
  ORGANISM  Eschscholzia californica
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.71
            ExPASy - ENZYME nomenclature database: 1.14.13.71
            ExplorEnz - The Enzyme Database: 1.14.13.71
            ERGO genome analysis and discovery system: 1.14.13.71
            BRENDA, the Enzyme Database: 1.14.13.71
///
ENTRY       EC 1.14.13.72               Enzyme
NAME        methylsterol monooxygenase;
            methylsterol hydroxylase;
            4-methylsterol oxidase;
            4,4-dimethyl-5alpha-cholest-7-en-3beta-ol,hydrogen-donor:oxygen
            oxidoreductase (hydroxylating)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     4,4-dimethyl-5alpha-cholest-7-en-3beta-ol,NAD(P)H:oxygen
            oxidoreductase (hydroxylating)
REACTION    (1) 4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + NAD(P)H + H+ + O2 =
            4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol +
            NAD(P)+ + H2O [RN:R04501 R05736];
            (2) 4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol +
            NAD(P)H + H+ + O2 =
            3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde
            + NAD(P)+ + 2 H2O [RN:R05733 R05737];
            (3)
            3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde
            + NAD(P)H + H+ + O2 =
            3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate +
            NAD(P)+ + H2O [RN:R05734 R05738]
ALL_REAC    R04501 R05733 R05734 R05736 R05737 R05738;
            (other) R04328 R07509
SUBSTRATE   4,4-dimethyl-5alpha-cholest-7-en-3beta-ol [CPD:C04530];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007];
            4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol
            [CPD:C04814];
            3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde
            [CPD:C11509]
PRODUCT     4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol
            [CPD:C04814];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde
            [CPD:C11509];
            3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate
            [CPD:C04840]
COMMENT     Requires cytochrome b5. Also acts on
            4alpha-methyl-5alpha-cholest-7-en-3beta-ol. The sterol can be based
            on cycloartenol as well as lanosterol.
REFERENCE   1  [PMID:9240456]
  AUTHORS   Rahier A, Smith M, Taton M.
  TITLE     The role of cytochrome b5 in 4alpha-methyl-oxidation and C5(6)
            desaturation of plant sterol precursors.
  JOURNAL   Biochem. Biophys. Res. Commun. 236 (1997) 434-7.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   2  [PMID:8505296]
  AUTHORS   Pascal S, Taton M, Rahier A.
  TITLE     Plant sterol biosynthesis. Identification and characterization of
            two distinct microsomal oxidative enzymatic systems involved in
            sterol C4-demethylation.
  JOURNAL   J. Biol. Chem. 268 (1993) 11639-54.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   3  [PMID:3949790]
  AUTHORS   Kawata S, Trzaskos JM, Gaylor JL.
  TITLE     Affinity chromatography of microsomal enzymes on immobilized
            detergent-solubilized cytochrome b5.
  JOURNAL   J. Biol. Chem. 261 (1986) 3790-9.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:7228857]
  AUTHORS   Fukushima H, Grinstead GF, Gaylor JL.
  TITLE     Total enzymic synthesis of cholesterol from lanosterol. Cytochrome
            b5-dependence of 4-methyl sterol oxidase.
  JOURNAL   J. Biol. Chem. 256 (1981) 4822-6.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:7430141]
  AUTHORS   Brady DR, Crowder RD, Hayes WJ.
  TITLE     Mixed function oxidases in sterol metabolism. Source of reducing
            equivalents.
  JOURNAL   J. Biol. Chem. 255 (1980) 10624-9.
REFERENCE   6  [PMID:4234469]
  AUTHORS   Gaylor JL, Mason HS.
  TITLE     Investigation of the component reactions of oxidative sterol
            demethylation. Evidence against participation of cytochrome P-450.
  JOURNAL   J. Biol. Chem. 243 (1968) 4966-72.
  ORGANISM  rat [GN:rno]
REFERENCE   7  [PMID:4383278]
  AUTHORS   Miller WL, Kalafer ME, Gaylor JL, Delwiche CV.
  TITLE     Investigation of the component reactions of oxidative sterol
            demethylation. Study of the aerobic and anaerobic processes.
  JOURNAL   Biochemistry. 6 (1967) 2673-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K07750  methylsterol monooxygenase
GENES       HSA: 6307(SC4MOL)
            PTR: 471796(LOC471796)
            MMU: 66234(Sc4mol)
            RNO: 140910(Sc4mol)
            CFA: 475491(SC4MOL) 489163(LOC489163)
            SSC: 396590(SC4MOL)
            GGA: 422423(SC4MOL)
            DRE: 406662(sc4mol)
            SPU: 582397(LOC582397)
            DME: Dmel_CG1998
            CEL: F49E12.9
            ATH: AT1G07420(SMO2-2)
            OSA: 4342171
            CME: CMM277C
            SCE: YGR060W(ERG25)
            AGO: AGOS_AFR572W
            PIC: PICST_74706(ERG25)
            CAL: CaO19.11216 CaO19_4631(CaO19.4631)
            CGR: CAGL0K04477g
            SPO: SPAC630.08c
            ANI: AN8907.2
            AFM: AFUA_4G04820 AFUA_8G02440
            AOR: AO090010000667 AO090206000001
            CNE: CNC02410
            UMA: UM05880.1
            DDI: DDBDRAFT_0190553
            TET: TTHERM_00348230
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.72
            ExPASy - ENZYME nomenclature database: 1.14.13.72
            ExplorEnz - The Enzyme Database: 1.14.13.72
            ERGO genome analysis and discovery system: 1.14.13.72
            BRENDA, the Enzyme Database: 1.14.13.72
            CAS: 37256-80-7
///
ENTRY       EC 1.14.13.73               Enzyme
NAME        tabersonine 16-hydroxylase;
            tabersonine-11-hydroxylase;
            T11H
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     tabersonine,NADPH:oxygen oxidoreductase (16-hydroxylating)
REACTION    tabersonine + NADPH + H+ + O2 = 16-hydroxytabersonine + NADP+ + H2O
            [RN:R05855]
ALL_REAC    R05855
SUBSTRATE   tabersonine [CPD:C09244];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     16-hydroxytabersonine [CPD:C11643];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450).
REFERENCE   1  [PMID:12228585]
  AUTHORS   St-Pierre B, De Luca V.
  TITLE     A Cytochrome P-450 Monooxygenase Catalyzes the First Step in the
            Conversion of Tabersonine to Vindoline in Catharanthus roseus.
  JOURNAL   Plant. Physiol. 109 (1995) 131-139.
  ORGANISM  Catharanthus roseus
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.73
            ExPASy - ENZYME nomenclature database: 1.14.13.73
            ExplorEnz - The Enzyme Database: 1.14.13.73
            ERGO genome analysis and discovery system: 1.14.13.73
            BRENDA, the Enzyme Database: 1.14.13.73
            CAS: 250378-34-8
///
ENTRY       EC 1.14.13.74               Enzyme
NAME        7-deoxyloganin 7-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     7-deoxyloganin,NADPH:oxygen oxidoreductase (7alpha-hydroxylating)
REACTION    7-deoxyloganin + NADPH + H+ + O2 = loganin + NADP+ + H2O [RN:R03556]
ALL_REAC    R03556;
            (other) R05832
SUBSTRATE   7-deoxyloganin [CPD:C06071];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     loganin [CPD:C01433];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450).
REFERENCE   1  [PMID:11524113]
  AUTHORS   Katano N, Yamamoto H, Iio R, Inoue K.
  TITLE     7-Deoxyloganin 7-hydroxylase in Lonicera japonica cell cultures.
  JOURNAL   Phytochemistry. 58 (2001) 53-8.
  ORGANISM  Lonicera japonica
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.74
            ExPASy - ENZYME nomenclature database: 1.14.13.74
            ExplorEnz - The Enzyme Database: 1.14.13.74
            ERGO genome analysis and discovery system: 1.14.13.74
            BRENDA, the Enzyme Database: 1.14.13.74
            CAS: 335305-40-3
///
ENTRY       EC 1.14.13.75               Enzyme
NAME        vinorine hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     vinorine,NADPH:oxygen oxidoreductase (21alpha-hydroxylating)
REACTION    vinorine + NADPH + H+ + O2 = vomilenine + NADP+ + H2O [RN:R05877]
ALL_REAC    R05877
SUBSTRATE   vinorine [CPD:C11807];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     vomilenine [CPD:C01761];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450). Forms a stage in the biosynthesis
            of the indole alkaloid ajmaline.
REFERENCE   1
  AUTHORS   Falkenhagen, H. and Stockligt, J.
  TITLE     Enzymatic biosynthesis of vomilenine, a key intermediate of the
            ajmaline pathway, catalysed by a novel cytochrome P-450-dependent
            enzyme from plant cell cultures of Rauwolfia serpentina.
  JOURNAL   Z. Naturforsch. C: Biosci. 50 (1995) 45-53.
  ORGANISM  Rauwolfia serpentina
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.75
            ExPASy - ENZYME nomenclature database: 1.14.13.75
            ExplorEnz - The Enzyme Database: 1.14.13.75
            ERGO genome analysis and discovery system: 1.14.13.75
            BRENDA, the Enzyme Database: 1.14.13.75
            CAS: 162875-03-8
///
ENTRY       EC 1.14.13.76               Enzyme
NAME        taxane 10beta-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     taxa-4(20),11-dien-5alpha-yl acetate,NADPH:oxygen oxidoreductase
            (10beta-hydroxylating)
REACTION    taxa-4(20),11-dien-5alpha-yl acetate + NADPH + H+ + O2 =
            10beta-hydroxytaxa-4(20),11-dien-5alpha-yl acetate + NADP+ + H2O
            [RN:R06309]
ALL_REAC    R06309
SUBSTRATE   taxa-4(20),11-dien-5alpha-yl acetate;
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     10beta-hydroxytaxa-4(20),11-dien-5alpha-yl acetate;
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:11396929]
  AUTHORS   Wheeler AL, Long RM, Ketchum RE, Rithner CD, Williams RM, Croteau R.
  TITLE     Taxol biosynthesis: differential transformations of taxadien-5
            alpha-ol and its acetate ester by cytochrome P450 hydroxylases from
            Taxus suspension cells.
  JOURNAL   Arch. Biochem. Biophys. 390 (2001) 265-78.
  ORGANISM  Taxus sp.
REFERENCE   2  [PMID:11707604]
  AUTHORS   Jennewein S, Rithner CD, Williams RM, Croteau RB.
  TITLE     Taxol biosynthesis: taxane 13 alpha-hydroxylase is a cytochrome
            P450-dependent monooxygenase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 13595-600.
  ORGANISM  Taxus cuspidata
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.76
            ExPASy - ENZYME nomenclature database: 1.14.13.76
            ExplorEnz - The Enzyme Database: 1.14.13.76
            ERGO genome analysis and discovery system: 1.14.13.76
            BRENDA, the Enzyme Database: 1.14.13.76
            CAS: 337514-75-7
///
ENTRY       EC 1.14.13.77               Enzyme
NAME        taxane 13alpha-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     taxa-4(20),11-dien-5alpha-ol,NADPH:oxygen oxidoreductase
            (13alpha-hydroxylating)
REACTION    taxa-4(20),11-dien-5alpha-ol + NADPH + H+ + O2 =
            taxa-4(20),11-dien-5alpha,13alpha-diol + NADP+ + H2O [RN:R06308]
ALL_REAC    R06308
SUBSTRATE   taxa-4(20),11-dien-5alpha-ol;
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     taxa-4(20),11-dien-5alpha,13alpha-diol;
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:11396929]
  AUTHORS   Wheeler AL, Long RM, Ketchum RE, Rithner CD, Williams RM, Croteau R.
  TITLE     Taxol biosynthesis: differential transformations of taxadien-5
            alpha-ol and its acetate ester by cytochrome P450 hydroxylases from
            Taxus suspension cells.
  JOURNAL   Arch. Biochem. Biophys. 390 (2001) 265-78.
  ORGANISM  Taxus cuspidata
REFERENCE   2  [PMID:11707604]
  AUTHORS   Jennewein S, Rithner CD, Williams RM, Croteau RB.
  TITLE     Taxol biosynthesis: taxane 13 alpha-hydroxylase is a cytochrome
            P450-dependent monooxygenase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 13595-600.
  ORGANISM  Taxus cuspidata
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.77
            ExPASy - ENZYME nomenclature database: 1.14.13.77
            ExplorEnz - The Enzyme Database: 1.14.13.77
            ERGO genome analysis and discovery system: 1.14.13.77
            BRENDA, the Enzyme Database: 1.14.13.77
            CAS: 399030-58-1
///
ENTRY       EC 1.14.13.78               Enzyme
NAME        ent-kaurene oxidase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     ent-kaur-16-ene,NADPH:oxygen oxidoreductase (hydroxylating)
REACTION    (1) ent-kaur-16-ene + NADPH + H+ + O2 = ent-kaur-16-en-19-ol + NADP+
            + H2O [RN:R06291];
            (2) ent-kaur-16-en-19-ol + NADPH + H+ + O2 = ent-kaur-16-en-19-al +
            NADP+ + 2 H2O [RN:R06292];
            (3) ent-kaur-16-en-19-al + NADPH + O2 = ent-kaur-16-en-19-oate +
            NADP+ + H2O [RN:R06293]
ALL_REAC    R06291 R06292 R06293
SUBSTRATE   ent-kaur-16-ene [CPD:C06090];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007];
            ent-kaur-16-en-19-ol [CPD:C11872];
            ent-kaur-16-en-19-al [CPD:C11873]
PRODUCT     ent-kaur-16-en-19-ol [CPD:C11872];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            ent-kaur-16-en-19-al [CPD:C11873];
            ent-kaur-16-en-19-oate [CPD:C11874]
COMMENT     Requires cytochrome P450. Catalyses three sucessive oxidations of
            the 4-methyl group of ent-kaurene giving kaurenoic acid.
REFERENCE   1  [PMID:2223832]
  AUTHORS   Ashman PJ, Mackenzie A, Bramley PM.
  TITLE     Characterization of ent-kaurene oxidase activity from Gibberella
            fujikuroi.
  JOURNAL   Biochim. Biophys. Acta. 1036 (1990) 151-7.
  ORGANISM  Gibberella fujikuroi
REFERENCE   2  [PMID:1397591]
  AUTHORS   Archer C, Ashman PJ, Hedden P, Bowyer JR, Bramley PM.
  TITLE     Purification of ent-kaurene oxidase from Gibberella fujikuroi and
            Cucurbita maxima.
  JOURNAL   Biochem. Soc. Trans. 20 (1992) 218S.
  ORGANISM  Gibberella fujikuroi, Cucurbita maxima
REFERENCE   3  [PMID:9952446]
  AUTHORS   Helliwell CA, Poole A, Peacock WJ, Dennis ES.
  TITLE     Arabidopsis ent-kaurene oxidase catalyzes three steps of gibberellin
            biosynthesis.
  JOURNAL   Plant. Physiol. 119 (1999) 507-10.
  ORGANISM  Gibberella fujikuroi
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
ORTHOLOGY   KO: K04122  ent-kaurene oxidase
GENES       ATH: AT5G25900(GA3)
            OSA: 4341347
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.78
            ExPASy - ENZYME nomenclature database: 1.14.13.78
            ExplorEnz - The Enzyme Database: 1.14.13.78
            ERGO genome analysis and discovery system: 1.14.13.78
            BRENDA, the Enzyme Database: 1.14.13.78
            CAS: 149565-67-3
///
ENTRY       EC 1.14.13.79               Enzyme
NAME        ent-kaurenoic acid oxidase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     ent-kaur-16-en-19-oate,NADPH:oxygen oxidoreductase (hydroxylating)
REACTION    (1) ent-kaur-16-en-19-oate + NADPH + H+ + O2 =
            ent-7alpha-hydroxykaur-16-en-19-oate + NADP+ + H2O [RN:R06294];
            (2) ent-7alpha-hydroxykaur-16-en-19-oate + NADPH + H+ + O2 =
            gibberellin A12 aldehyde + NADP+ + 2 H2O [RN:R06295];
            (3) gibberellin A12 aldehyde + NADPH + O2 = gibberellin A12 + NADP+
            + H2O [RN:R06297]
ALL_REAC    R06294 R06295 R06297;
            (other) R06296
SUBSTRATE   ent-kaur-16-en-19-oate [CPD:C11874];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007];
            ent-7alpha-hydroxykaur-16-en-19-oate [CPD:C11875];
            gibberellin A12 aldehyde [CPD:C06093]
PRODUCT     ent-7alpha-hydroxykaur-16-en-19-oate [CPD:C11875];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            gibberellin A12 aldehyde [CPD:C06093];
            gibberellin A12 [CPD:C11857]
COMMENT     Requires cytochrome P450. Catalyses three sucessive oxidations of
            ent-kaurenoic acid. The second step includes a ring-B contraction
            giving the gibbane skeleton. In pumpkin (Cucurbita maxima)
            ent-6alpha,7alpha-dihydroxykaur-16-en-19-oate is also formed.
REFERENCE   1  [PMID:11172076]
  AUTHORS   Helliwell CA, Chandler PM, Poole A, Dennis ES, Peacock WJ.
  TITLE     The CYP88A cytochrome P450, ent-kaurenoic acid oxidase, catalyzes
            three steps of the gibberellin biosynthesis pathway.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 2065-70.
  ORGANISM  Zea mays [GN:ezma]
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
ORTHOLOGY   KO: K04123  ent-kaurenoic acid hydroxylase
GENES       ATH: AT2G32440(KAO2)
            OSA: 4339885
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.79
            ExPASy - ENZYME nomenclature database: 1.14.13.79
            ExplorEnz - The Enzyme Database: 1.14.13.79
            ERGO genome analysis and discovery system: 1.14.13.79
            BRENDA, the Enzyme Database: 1.14.13.79
            CAS: 337507-95-6
///
ENTRY       EC 1.14.13.80               Enzyme
NAME        (R)-limonene 6-monooxygenase;
            (+)-limonene-6-hydroxylase;
            (+)-limonene 6-monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     (R)-limonene,NADPH:oxygen oxidoreductase (6-hydroxylating)
REACTION    (+)-(R)-limonene + NADPH + H+ + O2 = (+)-trans-carveol + NADP+ + H2O
            [RN:R06119]
ALL_REAC    R06119
SUBSTRATE   (+)-(R)-limonene [CPD:C06099];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (+)-trans-carveol [CPD:C11409];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     The reaction is stereospecific with over 95% yield of
            (+)-trans-carveol from (R)-limonene. (S)-Limonene, the substrate for
            EC 1.14.13.48, (S)-limonene 6-monooxygenase, is not a substrate.
            Forms part of the carvone biosynthesis pathway in Carum carvi
            (caraway) seeds.
REFERENCE   1  [PMID:9662532]
  AUTHORS   Bouwmeester HJ, Gershenzon J, Konings MC, Croteau R.
  TITLE     Biosynthesis of the monoterpenes limonene and carvone in the fruit
            of caraway. I. Demonstration Of enzyme activities and their changes
            with development
  JOURNAL   Plant. Physiol. 117 (1998) 901-12.
  ORGANISM  Carum carvi
REFERENCE   2
  AUTHORS   Bouwmeester, H.J., Konings, M.C.J.M., Gershenzon, J., Karp, F. and
            Croteau, R.
  TITLE     Cytochrome P-450 dependent (+)-limonene-6-hydroxylation in fruits of
            caraway (Carum Carvi).
  JOURNAL   Phytochemistry 50 (1999) 243-248.
  ORGANISM  Carum carvi
PATHWAY     PATH: map00902  Monoterpenoid biosynthesis
            PATH: map00903  Limonene and pinene degradation
ORTHOLOGY   KO: K07383  (R)-limonene 6-monooxygenase
GENES       HSA: 1557(CYP2C19) 1559(CYP2C9)
            RNO: 29277(Cyp2c)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.80
            ExPASy - ENZYME nomenclature database: 1.14.13.80
            ExplorEnz - The Enzyme Database: 1.14.13.80
            ERGO genome analysis and discovery system: 1.14.13.80
            BRENDA, the Enzyme Database: 1.14.13.80
            CAS: 221461-49-0
///
ENTRY       EC 1.14.13.81               Enzyme
NAME        magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase;
            Mg-protoporphyrin IX monomethyl ester (oxidative) cyclase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     magnesium-protoporphyrin-IX 13-monomethyl ester,NADPH:oxygen
            oxidoreductase (hydroxylating)
REACTION    (1) magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + H+ +
            O2 = 131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester +
            NADP+ + H2O [RN:R06265];
            (2) 131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester +
            NADPH + H+ + O2 = 131-oxo-magnesium-protoporphyrin IX 13-monomethyl
            ester + NADP+ + 2 H2O [RN:R06266];
            (3) 131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + NADPH
            + H+ + O2 = divinylprotochlorophyllide + NADP+ + 2 H2O [RN:R06267]
ALL_REAC    R06265 R06266 R06267
SUBSTRATE   magnesium-protoporphyrin IX 13-monomethyl ester [CPD:C04536];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007];
            131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester;
            131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester
PRODUCT     131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester;
            NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester;
            divinylprotochlorophyllide [CPD:C11831]
COMMENT     Requires Fe(II) for activity. The cyclase activity in Chlamydomonas
            reinhardtii is associated exclusively with the membranes, whereas
            that from cucumber cotyledons requires both membrane and soluble
            fractions for activity.
REFERENCE   1  [PMID:12226378]
  AUTHORS   Bollivar DW, Beale SI.
  TITLE     The Chlorophyll Biosynthetic Enzyme Mg-Protoporphyrin IX Monomethyl
            Ester (Oxidative) Cyclase (Characterization and Partial Purification
            from Chlamydomonas reinhardtii and Synechocystis sp. PCC 6803).
  JOURNAL   Plant. Physiol. 112 (1996) 105-114.
  ORGANISM  Chlamydomonas reinhardtii, Synechocystis sp.
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K04035  magnesium-protoporphyrin IX monomethyl ester (oxidative)
                        cyclase
GENES       ATH: AT3G56940(AT103)
            OSA: 4326901
            NOC: Noc_1738
            HHA: Hhal_1625
            BUR: Bcep18194_A4283
            PPD: Ppro_2479 Ppro_2577 Ppro_2638 Ppro_3390
            DVL: Dvul_0353
            SFU: Sfum_0909
            RLE: pRL100097
            BRA: BRADO1649(acsF) BRADO1652(bchE)
            BBT: BBta_6404(bchE) BBta_6407(acsF)
            RPA: RPA1552
            RPB: RPB_2687 RPB_3863 RPB_3971
            RPC: RPC_1323 RPC_3812
            RPD: RPD_1487 RPD_3726
            RPE: RPE_1357
            RSP: RSP_0294
            RSH: Rsph17029_1924
            RSQ: Rsph17025_1000
            JAN: Jann_0151
            RDE: RD1_0129(acsF)
            RRU: Rru_A3548
            FRA: Francci3_1863 Francci3_2496
            SYN: sll1214(acsF) sll1874(AT103) slr0905(chlE)
            SYW: SYNW1198(PNIL34)
            SYC: syc2188_d(ycf59)
            SYF: Synpcc7942_1907
            SYD: Syncc9605_1310
            SYE: Syncc9902_1165
            SYG: sync_1304(acsF)
            SYR: SynRCC307_1476(acsF)
            SYX: SynWH7803_1102(acsF)
            CYA: CYA_2703(acsF)
            CYB: CYB_1254(acsF)
            TEL: tlr1426(acsF) tlr1722
            GVI: gll3625(acsF)
            ANA: all1880 alr1358 alr3300(acsF)
            AVA: Ava_1133 Ava_4776 Ava_4958
            PMA: Pro0992(acsF)
            PMM: PMM0844(PNIL34)
            PMT: PMT2196
            PMN: PMN2A_0227
            PMI: PMT9312_0956
            PMB: A9601_10251(pniL34)
            PMC: P9515_09201(pnilL34)
            PMF: P9303_29201(pniL34)
            PMG: P9301_10241(pniL34)
            PME: NATL1_08941(pnil34)
            TER: Tery_0728
            CCH: Cag_0114 Cag_0229 Cag_0931 Cag_1537
            CPH: Cpha266_2315 Cpha266_2592
            PVI: Cvib_0316 Cvib_1454
            PLT: Plut_0251 Plut_1668
            RRS: RoseRS_1905
            RCA: Rcas_1541
            MBU: Mbur_1602
            MSI: Msm_0385
            SMR: Smar_0664
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.81
            ExPASy - ENZYME nomenclature database: 1.14.13.81
            ExplorEnz - The Enzyme Database: 1.14.13.81
            ERGO genome analysis and discovery system: 1.14.13.81
            BRENDA, the Enzyme Database: 1.14.13.81
            CAS: 92353-62-3
///
ENTRY       EC 1.14.13.82               Enzyme
NAME        vanillate monooxygenase;
            4-hydroxy-3-methoxybenzoate demethylase;
            vanillate demethylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     vanillate:oxygen oxidoreductase (demethylating)
REACTION    vanillate + O2 + NADH + H+ = 3,4-dihydroxybenzoate + NAD+ + H2O +
            formaldehyde [RN:R05274]
ALL_REAC    R05274
SUBSTRATE   vanillate [CPD:C06672];
            O2 [CPD:C00007];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
PRODUCT     3,4-dihydroxybenzoate [CPD:C00230];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001];
            formaldehyde [CPD:C00067]
COMMENT     Forms part of the vanillin degradation pathway in Arthrobacter sp.
REFERENCE   1  [PMID:3170489]
  AUTHORS   Brunel F, Davison J.
  TITLE     Cloning and sequencing of Pseudomonas genes encoding vanillate
            demethylase.
  JOURNAL   J. Bacteriol. 170 (1988) 4924-30.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:9098058]
  AUTHORS   Priefert H, Rabenhorst J, Steinbuchel A.
  TITLE     Molecular characterization of genes of Pseudomonas sp. strain HR199
            involved in bioconversion of vanillin to protocatechuate.
  JOURNAL   J. Bacteriol. 179 (1997) 2595-607.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
ORTHOLOGY   KO: K03461  vanillate monooxygenase
            KO: K03862  vanillate monooxygenase
            KO: K03863  vanillate monooxygenase
GENES       XCC: XCC0296(vanB) XCC0297(vanA) XCC0363(vanA)
            XCB: XC_0307 XC_0308 XC_0375
            XCV: XCV0319 XCV0320 XCV0377
            XAC: XAC0310(vanB) XAC0311(vanA) XAC0363(vanA)
            PAE: PA4904(vanA) PA4905(vanB)
            PAU: PA14_64800(vanA) PA14_64810(vanB)
            PPU: PP_3736(vanA) PP_3737(vanB)
            PST: PSPTO_2904(vanA) PSPTO_2905(vanB)
            PSB: Psyr_2708 Psyr_2709
            PSP: PSPPH_2474(vanB) PSPPH_2475(vanA)
            PFL: PFL_3471(vanA) PFL_3472(vanB)
            ACI: ACIAD0459 ACIAD0979(vanB) ACIAD0980(vanA)
            PAT: Patl_0869
            CSA: Csal_0336 Csal_0344
            RSO: RSp0222(vanA) RSp0223(vanB)
            REU: Reut_B3579 Reut_B4340 Reut_B4341 Reut_B4797 Reut_D6483
            RME: Rmet_5517 Rmet_5546
            BXE: Bxe_A1100 Bxe_A2111 Bxe_A3542 Bxe_B0057 Bxe_C0406 Bxe_C0623
                 Bxe_C0803 Bxe_C0999 Bxe_C1009 Bxe_C1389
            BVI: Bcep1808_3498
            BUR: Bcep18194_B0418 Bcep18194_B0420 Bcep18194_B0787
                 Bcep18194_B1105 Bcep18194_B1448 Bcep18194_C6662
            BAM: Bamb_4330 Bamb_4591 Bamb_4593
            BTE: BTH_II0329
            BBR: BB4317 BB4772(vanB)
            RFR: Rfer_0280 Rfer_0281
            POL: Bpro_0993 Bpro_0995 Bpro_3387
            VEI: Veis_1368 Veis_1370
            MPT: Mpe_A0963 Mpe_A1001 Mpe_A1003 Mpe_A1004 Mpe_A3671 Mpe_B0554
            MMS: mma_0227 mma_1222(vanB3) mma_1223(vanA) mma_1673 mma_2506
            RET: RHE_PC00091(yhc00022)
            RLE: pRL100334
            BJA: bll5527 blr2390(vanA) blr3399
            BRA: BRADO1851(vanB) BRADO1867
            BBT: BBta_2173(vanB) BBta_2184 BBta_3234
            RPA: RPA3619(vanA)
            RPB: RPB_0127 RPB_1908
            CCR: CC_2393 CC_2394
            SIL: SPO1452 SPOA0133
            JAN: Jann_1575 Jann_3952
            RDE: RD1_2360(van) RD1_3683(van)
            ZMO: ZMO0456(vanB)
            NAR: Saro_1488 Saro_1872
            SWI: Swit_1067 Swit_1541 Swit_1543 Swit_1549 Swit_1559 Swit_1687
                 Swit_2285 Swit_2310 Swit_3024 Swit_3264 Swit_3396 Swit_3409
                 Swit_3413 Swit_3416 Swit_4269 Swit_4273
            GOX: GOX2373
            GBE: GbCGDNIH1_0668
            CGL: NCgl2300(cgl2383)
            CGB: cg2616(vanA) cg2617(vanB)
            CEF: CE0634
            NFA: nfa28480
            RHA: RHA1_ro04165
            SCO: SCO6680(SC5A7.30c)
            FAL: FRAAL0416(vanA)
            SEN: SACE_2821
            AVA: Ava_0535 Ava_1303 Ava_1827
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.82
            ExPASy - ENZYME nomenclature database: 1.14.13.82
            ExplorEnz - The Enzyme Database: 1.14.13.82
            ERGO genome analysis and discovery system: 1.14.13.82
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.82
            BRENDA, the Enzyme Database: 1.14.13.82
///
ENTRY       EC 1.14.13.83               Enzyme
NAME        precorrin-3B synthase;
            precorrin-3X synthase;
            CobG
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     precorrin-3A,NADH:oxygen oxidoreductase (20-hydroxylating)
REACTION    precorrin-3A + NADH + H+ + O2 = precorrin-3B + NAD+ + H2O
            [RN:R05217]
ALL_REAC    R05217
SUBSTRATE   precorrin 3A [CPD:C05772];
            NADH [CPD:C00004];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     precorrin 3B [CPD:C06406];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
COMMENT     An iron-sulfur protein. An oxygen atom from dioxygen is incorporated
            into the macrocycle at C-20. In the aerobic cobalamin biosythesis
            pathway, four enzymes are involved in the conversion of precorrin-3A
            to precorrin-6A. The first of the four steps is carried out by EC
            1.14.13.83, precorrin-3B synthase (CobG), yielding precorrin-3B as
            the product. This is followed by three methylation reactions, which
            introduce a methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM;
            EC 2.1.1.133) and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving
            rise to precorrin-4, precorrin-5 and precorrin-6A, respectively.
REFERENCE   1  [PMID:8226690]
  AUTHORS   Debussche L, Thibaut D, Cameron B, Crouzet J, Blanche F.
  TITLE     Biosynthesis of the corrin macrocycle of coenzyme B12 in Pseudomonas
            denitrificans.
  JOURNAL   J. Bacteriol. 175 (1993) 7430-40.
  ORGANISM  Pseudomonas denitrificans
REFERENCE   2  [PMID:8405386]
  AUTHORS   Scott AI, Roessner CA, Stolowich NJ, Spencer JB, Min C, Ozaki SI.
  TITLE     Biosynthesis of vitamin B12. Discovery of the enzymes for oxidative
            ring contraction and insertion of the fourth methyl group.
  JOURNAL   FEBS. Lett. 331 (1993) 105-8.
  ORGANISM  Pseudomonas denitrificans
REFERENCE   3  [PMID:12195810]
  AUTHORS   Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
  TITLE     The biosynthesis of adenosylcobalamin (vitamin B12).
  JOURNAL   Nat. Prod. Rep. 19 (2002) 390-412.
  ORGANISM  Pseudomonas denitrificans
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K02229  precorrin-3B synthase
GENES       PAE: PA2906
            PAP: PSPA7_2248(cobG)
            PPU: PP_4829
            PST: PSPTO_4877
            PSB: Psyr_4417
            PSP: PSPPH_4460
            PFL: PFL_0657(nirA)
            PFO: Pfl_0604
            PEN: PSEEN4871(cobG)
            BMA: BMA1161
            BMN: BMA10247_0896(cobG)
            BXE: Bxe_B1245
            BUR: Bcep18194_A4824
            BCN: Bcen_1194
            BCH: Bcen2424_1674
            BPS: BPSL1759
            BPM: BURPS1710b_2113(cobG)
            BPL: BURPS1106A_1967(cobG)
            BPD: BURPS668_1950(cobG)
            BTE: BTH_I2398
            MLO: mlr1378(cobG)
            SME: SMc03193(cobG)
            ATU: Atu2803(cobG)
            ATC: AGR_C_5083(cobG)
            RET: RHE_PE00455(cobG)
            RLE: pRL110631(cobG)
            BME: BMEI0715
            BMF: BAB1_1304
            BMS: BR1286
            BMB: BruAb1_1287
            BOV: BOV_1249(cobG)
            BRA: BRADO4906
            BBT: BBta_3145
            XAU: Xaut_3285
            SIL: SPO2864
            SIT: TM1040_2211
            JAN: Jann_2930
            RDE: RD1_3826(cobG)
            NAR: Saro_0341
            GBE: GbCGDNIH1_0659
            MTU: Rv2064(cobG)
            MTC: MT2124
            MBO: Mb2090(cobG)
            MPA: MAP1810(cobG)
            MSM: MSMEG_3871(cobG)
            MMC: Mmcs_2489
            CDI: DIP1231
            NFA: nfa31400
            TFU: Tfu_0318
            FRA: Francci3_1519
            FAL: FRAAL2331(cobG)
            SEN: SACE_5953
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.83
            ExPASy - ENZYME nomenclature database: 1.14.13.83
            ExplorEnz - The Enzyme Database: 1.14.13.83
            ERGO genome analysis and discovery system: 1.14.13.83
            BRENDA, the Enzyme Database: 1.14.13.83
///
ENTRY       EC 1.14.13.84               Enzyme
NAME        4-hydroxyacetophenone monooxygenase;
            HAPMO
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     (4-hydroxyphenyl)ethan-1-one,NADPH:oxygen oxidoreductase
            (ester-forming)
REACTION    (4-hydroxyphenyl)ethan-1-one + NADPH + H+ + O2 = 4-hydroxyphenyl
            acetate + NADP+ + H2O [RN:R06892]
ALL_REAC    R06892
SUBSTRATE   (4-hydroxyphenyl)ethan-1-one [CPD:C10700];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     4-hydroxyphenyl acetate [CPD:C13636];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     Contains FAD. The enzyme from Pseudomonas fluorescens ACB catalyses
            the conversion of a wide range of acetophenone derivatives. Highest
            activity occurs with compounds bearing an electron-donating
            substituent at the para position of the aromatic ring [1]. In the
            absence of substrate, the enzyme can act as an NAD(P)H oxidase (EC
            1.6.3.1).
REFERENCE   1  [PMID:11322873]
  AUTHORS   Kamerbeek NM, Moonen MJ, Van Der Ven JG, Van Berkel WJ, Fraaije MW,
            Janssen DB.
  TITLE     4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens
            ACB. A novel flavoprotein catalyzing Baeyer-Villiger oxidation of
            aromatic compounds.
  JOURNAL   Eur. J. Biochem. 268 (2001) 2547-57.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   2  [PMID:12514023]
  AUTHORS   Kamerbeek NM, Olsthoorn AJ, Fraaije MW, Janssen DB.
  TITLE     Substrate specificity and enantioselectivity of
            4-hydroxyacetophenone monooxygenase.
  JOURNAL   Appl. Environ. Microbiol. 69 (2003) 419-26.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00363  Bisphenol A degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.84
            ExPASy - ENZYME nomenclature database: 1.14.13.84
            ExplorEnz - The Enzyme Database: 1.14.13.84
            ERGO genome analysis and discovery system: 1.14.13.84
            BRENDA, the Enzyme Database: 1.14.13.84
///
ENTRY       EC 1.14.13.85               Enzyme
NAME        glyceollin synthase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     2-(or
            4-)dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan,NADPH:oxyge
            n oxidoreductase (cyclizing)
REACTION    2-(or 4-)dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan +
            NADPH + H+ + O2 = glyceollin + NADP+ + 2 H2O [RN:R07356 R07357]
ALL_REAC    R07356 > R07195 R07196;
            R07357 > R07197
SUBSTRATE   2-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan
            [CPD:C15509];
            4-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan
            [CPD:C15510];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     glyceollin [CPD:C01701];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450). Glyceollins II and III are formed
            from 2-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan whereas
            glyceollin I is formed from the 4-isomer.
REFERENCE   1  [PMID:3369863]
  AUTHORS   Welle R, Grisebach H.
  TITLE     Induction of phytoalexin synthesis in soybean: enzymatic cyclization
            of prenylated pterocarpans to glyceollin isomers.
  JOURNAL   Arch. Biochem. Biophys. 263 (1988) 191-8.
  ORGANISM  Glycine max [GN:egma]
PATHWAY     PATH: map00943  Isoflavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.85
            ExPASy - ENZYME nomenclature database: 1.14.13.85
            ExplorEnz - The Enzyme Database: 1.14.13.85
            ERGO genome analysis and discovery system: 1.14.13.85
            BRENDA, the Enzyme Database: 1.14.13.85
///
ENTRY       EC 1.14.13.86               Enzyme
NAME        2-hydroxyisoflavanone synthase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     apigenin,NADPH:oxygen oxidoreductase (isoflavanone-forming)
REACTION    apigenin + 2 NADPH + 2 H+ + O2 = 2-hydroxy-2,3-dihydrogenistein + 2
            NADP+ + H2O [RN:R06792]
ALL_REAC    R06792;
            (other) R07714 R07715 R07777 R07778
SUBSTRATE   apigenin [CPD:C01477];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     2-hydroxy-2,3-dihydrogenistein [CPD:C12631];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450). EC 4.2.1.105, 2-hydroxyisoflavanone
            dehydratase, acts on 2-hydroxy-2,3-dihydrogenistein with loss of
            water and formation of genistein. This may occur spontaneously.
REFERENCE   1  [PMID:3956488]
  AUTHORS   Kochs G, Grisebach H.
  TITLE     Enzymic synthesis of isoflavones.
  JOURNAL   Eur. J. Biochem. 155 (1986) 311-8.
  ORGANISM  Glycine max [GN:egma]
REFERENCE   2  [PMID:10375412]
  AUTHORS   Steele CL, Gijzen M, Qutob D, Dixon RA.
  TITLE     Molecular characterization of the enzyme catalyzing the aryl
            migration reaction of isoflavonoid biosynthesis in soybean.
  JOURNAL   Arch. Biochem. Biophys. 367 (1999) 146-50.
  ORGANISM  Glycine max [GN:egma]
PATHWAY     PATH: map00943  Isoflavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.86
            ExPASy - ENZYME nomenclature database: 1.14.13.86
            ExplorEnz - The Enzyme Database: 1.14.13.86
            ERGO genome analysis and discovery system: 1.14.13.86
            BRENDA, the Enzyme Database: 1.14.13.86
///
ENTRY       EC 1.14.13.87               Enzyme
NAME        licodione synthase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     liquiritigenin,NADPH:oxygen oxidoreductase (licodione-forming)
REACTION    liquiritigenin + NADPH + H+ + O2 = licodione + NADP+ + H2O
            [RN:R07198]
ALL_REAC    R07198
SUBSTRATE   liquiritigenin [CPD:C09762];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     licodione [CPD:C01592];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450). It probably forms
            2-hydroxyliquiritigenin which spontaneously forms licodione. NADH
            can act instead of NADPH, but more slowly.
REFERENCE   1  [PMID:12232298]
  AUTHORS   Otani K, Takahashi T, Furuya T, Ayabe S.
  TITLE     Licodione Synthase, a Cytochrome P450 Monooxygenase Catalyzing
            2-Hydroxylation of 5-Deoxyflavanone, in Cultured Glycyrrhiza
            echinata L. Cells.
  JOURNAL   Plant. Physiol. 105 (1994) 1427-1432.
  ORGANISM  Glycyrrhiza echinata
REFERENCE   2  [PMID:9708921]
  AUTHORS   Akashi T, Aoki T, Ayabe S.
  TITLE     Identification of a cytochrome P450 cDNA encoding (2S)-flavanone
            2-hydroxylase of licorice (Glycyrrhiza echinata L.; Fabaceae) which
            represents licodione synthase and flavone synthase II.
  JOURNAL   FEBS. Lett. 431 (1998) 287-90.
  ORGANISM  Glycyrrhiza echinata
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.87
            ExPASy - ENZYME nomenclature database: 1.14.13.87
            ExplorEnz - The Enzyme Database: 1.14.13.87
            ERGO genome analysis and discovery system: 1.14.13.87
            BRENDA, the Enzyme Database: 1.14.13.87
            CAS: 157972-05-9
///
ENTRY       EC 1.14.13.88               Enzyme
NAME        flavonoid 3',5'-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     flavanone,NADPH:oxygen oxidoreductase
REACTION    (1) a flavanone + NADPH + H+ + O2 = a 3'-hydroxyflavanone + NADP+ +
            H2O [RN:R07369];
            (2) a 3'-hydroxyflavanone + NADPH + H+ + O2 = a
            3',5'-dihydroxyflavanone + NADP+ + H2O [RN:R07370]
ALL_REAC    R07369 > R02442 R03124;
            R07370 > R03639 R04902;
            (other) R02443 R03125 R06557 R06559
SUBSTRATE   flavanone [CPD:C00766];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007];
            3'-hydroxyflavanone [CPD:C15204]
PRODUCT     3'-hydroxyflavanone [CPD:C15204];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            3',5'-dihydroxyflavanone [CPD:C15609]
COMMENT     A heme-thiolate protein (P-450). The 3',5'-dihydroxyflavanone is
            formed via the 3'-hydroxyflavanone. In Petunia hybrida the enzyme
            acts on naringenin, eriodictyol, dihydroquercetin (taxifolin) and
            dihydrokaempferol (aromadendrin). The enzyme catalyses the
            hydroxylation of 5,7,4'-trihydroxyflavanone (naringenin) at either
            the 3' position to form eriodictyol or at both the 3' and 5'
            positions to form 5,7,3',4',5'-pentahydroxyflavanone
            (dihydrotricetin). The enzyme also catalyses the hydroxylation of
            3,5,7,3',4'-pentahydroxyflavanone (taxifolin) at the 5' position,
            forming ampelopsin. NADH is not a good substitute for NADPH.
REFERENCE   1  [PMID:12232356]
  AUTHORS   Menting J, Scopes RK, Stevenson TW.
  TITLE     Characterization of Flavonoid 3[prime],5[prime]-Hydroxylase in
            Microsomal Membrane Fraction of Petunia hybrida Flowers.
  JOURNAL   Plant. Physiol. 106 (1994) 633-642.
  ORGANISM  Petunia hybrida
REFERENCE   2  [PMID:10567704]
  AUTHORS   Shimada Y, Nakano-Shimada R, Ohbayashi M, Okinaka Y, Kiyokawa S,
            Kikuchi Y.
  TITLE     Expression of chimeric P450 genes encoding flavonoid-3',
            5'-hydroxylase in transgenic tobacco and petunia plants(1).
  JOURNAL   FEBS. Lett. 461 (1999) 241-5.
  ORGANISM  Petunia hybrida, Nicotiana tabacum
REFERENCE   3  [PMID:9892710]
  AUTHORS   de Vetten N, ter Horst J, van Schaik HP, de Boer A, Mol J, Koes R.
  TITLE     A cytochrome b5 is required for full activity of flavonoid 3',
            5'-hydroxylase, a cytochrome P450 involved in the formation of blue
            flower colors.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 778-83.
  ORGANISM  Petunia hybrida
PATHWAY     PATH: map00941  Flavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.88
            ExPASy - ENZYME nomenclature database: 1.14.13.88
            ExplorEnz - The Enzyme Database: 1.14.13.88
            ERGO genome analysis and discovery system: 1.14.13.88
            BRENDA, the Enzyme Database: 1.14.13.88
            CAS: 94047-23-1
///
ENTRY       EC 1.14.13.89               Enzyme
NAME        isoflavone 2'-hydroxylase;
            isoflavone 2'-monooxygenase;
            CYP81E1;
            CYP Ge-3
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     isoflavone,NADPH:oxygen oxidoreductase (2'-hydroxylating)
REACTION    an isoflavone + NADPH + H+ + O2 = a 2'-hydroxyisoflavone + NADP+ +
            H2O [RN:R07371]
ALL_REAC    R07371 > R06560 R06561 R06606 R06607 R07746
SUBSTRATE   isoflavone [CPD:C00799];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     2'-hydroxyisoflavone [CPD:C02921];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450). Acts on daidzein, formononetin and
            genistein. EC 1.14.13.53, 4'-methoxyisoflavone 2'-hydroxylase, has
            the same reaction but is more specific as it requires a
            4'-methoxyisoflavone.
REFERENCE   1  [PMID:9790908]
  AUTHORS   Akashi T, Aoki T, Ayabe S.
  TITLE     CYP81E1, a cytochrome P450 cDNA of licorice (Glycyrrhiza echinata
            L.), encodes isoflavone 2'-hydroxylase.
  JOURNAL   Biochem. Biophys. Res. Commun. 251 (1998) 67-70.
  ORGANISM  Glycyrrhiza echinata
PATHWAY     PATH: map00943  Isoflavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.89
            ExPASy - ENZYME nomenclature database: 1.14.13.89
            ExplorEnz - The Enzyme Database: 1.14.13.89
            ERGO genome analysis and discovery system: 1.14.13.89
            BRENDA, the Enzyme Database: 1.14.13.89
///
ENTRY       EC 1.14.13.90               Enzyme
NAME        zeaxanthin epoxidase;
            Zea-epoxidase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     zeaxanthin,NAD(P)H:oxygen oxidoreductase
REACTION    (1) zeaxanthin + NAD(P)H + H+ + O2 = antheraxanthin + NAD(P)+ + H2O
            [RN:R06946 R07199];
            (2) antheraxanthin + NAD(P)H + H+ + O2 = violaxanthin + NAD(P)+ +
            H2O [RN:R06947 R07200]
ALL_REAC    R06946 R06947 R07199 R07200
SUBSTRATE   zeaxanthin [CPD:C06098];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007];
            antheraxanthin [CPD:C08579]
PRODUCT     antheraxanthin [CPD:C08579];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            violaxanthin [CPD:C08614]
COMMENT     A flavoprotein (FAD) that is active under conditions of low light.
            Along with EC 1.10.99.3, violaxanthin de-epoxidase, this enzyme
            forms part of the xanthophyll (or violaxanthin) cycle, which is
            involved in protecting the plant against damage by excess light. It
            will also epoxidize lutein in some higher-plant species.
REFERENCE   1  [PMID:8521963]
  AUTHORS   Buch K, Stransky H, Hager A.
  TITLE     FAD is a further essential cofactor of the NAD(P)H and O2-dependent
            zeaxanthin-epoxidase.
  JOURNAL   FEBS. Lett. 376 (1995) 45-8.
  ORGANISM  Nicotiana plumbaginifolia
REFERENCE   2  [PMID:9624110]
  AUTHORS   Bugos RC, Hieber AD, Yamamoto HY.
  TITLE     Xanthophyll cycle enzymes are members of the lipocalin family, the
            first identified from plants.
  JOURNAL   J. Biol. Chem. 273 (1998) 15321-4.
  ORGANISM  Nicotiana plumbaginifolia
REFERENCE   3  [PMID:10890531]
  AUTHORS   Thompson AJ, Jackson AC, Parker RA, Morpeth DR, Burbidge A, Taylor
            IB.
  TITLE     Abscisic acid biosynthesis in tomato: regulation of zeaxanthin
            epoxidase and 9-cis-epoxycarotenoid dioxygenase mRNAs by light/dark
            cycles, water stress and abscisic acid.
  JOURNAL   Plant. Mol. Biol. 42 (2000) 833-45.
  ORGANISM  Nicotiana plumbaginifolia, Zea mays [GN:ezma]
REFERENCE   4  [PMID:11058750]
  AUTHORS   Hieber AD, Bugos RC, Yamamoto HY.
  TITLE     Plant lipocalins: violaxanthin de-epoxidase and zeaxanthin
            epoxidase.
  JOURNAL   Biochim. Biophys. Acta. 1482 (2000) 84-91.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   5  [PMID:11506368]
  AUTHORS   Frommolt R, Goss R, Wilhelm C.
  TITLE     The de-epoxidase and epoxidase reactions of Mantoniella squamata
            (Prasinophyceae) exhibit different substrate-specific reaction
            kinetics compared to spinach.
  JOURNAL   Planta. 213 (2001) 446-56.
  ORGANISM  Mantoniella squamata, spinach
REFERENCE   6  [PMID:11506368]
  AUTHORS   Frommolt R, Goss R, Wilhelm C.
  TITLE     The de-epoxidase and epoxidase reactions of Mantoniella squamata
            (Prasinophyceae) exhibit different substrate-specific reaction
            kinetics compared to spinach.
  JOURNAL   Planta. 213 (2001) 446-56.
  ORGANISM  Mantoniella squamata, spinach
REFERENCE   7  [PMID:12844265]
  AUTHORS   Matsubara S, Morosinotto T, Bassi R, Christian AL, Fischer-Schliebs
            E, Luttge U, Orthen B, Franco AC, Scarano FR, Forster B, Pogson BJ,
            Osmond CB.
  TITLE     Occurrence of the lutein-epoxide cycle in mistletoes of the
            Loranthaceae and Viscaceae.
  JOURNAL   Planta. 217 (2003) 868-79.
  ORGANISM  Amyema cambagei, Amyema miquelii, Amyema pendulum, Muellerina
            eucalyptoides, Nuytsia floribunda, Phthirusa ovata, Psittachanthus
            dichrous, Psittachanthus robustus, Struthanthus flexicaulis,
            Struthanthus marginatus, Arceuthobium divaricatum, Arceuthobium
            oxycedri, Phoradendron californicum, Phoradendron dipterum,
            Phoradendron emarginatum, Phoradendron hexastichon, Phoradendron
            juniperinum, Phoradendron perrottetii, Phoradendron piauhyanum,
            Phoradendron piperoides, Phoradendron semivenosum, Phoradendron
            tunaeforme, Phoradendron undulatum, Viscum album, Viscum laxum,
            Exocarpos cupressiformis, Melampyrum pratense, Cassytha filiformis
PATHWAY     PATH: map00906  Carotenoid biosynthesis - General
ORTHOLOGY   KO: K09838  zeaxanthin epoxidase
GENES       ATH: AT5G67030(ABA1)
            OSA: 4335984
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.90
            ExPASy - ENZYME nomenclature database: 1.14.13.90
            ExplorEnz - The Enzyme Database: 1.14.13.90
            ERGO genome analysis and discovery system: 1.14.13.90
            BRENDA, the Enzyme Database: 1.14.13.90
///
ENTRY       EC 1.14.13.91               Enzyme
NAME        deoxysarpagine hydroxylase;
            DOSH
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     10-deoxysarpagine,NADPH:oxygen oxidoreductase (10-hydroxylating)
REACTION    10-deoxysarpagine + NADPH + H+ + O2 = sarpagine + NADP+ + H2O
            [RN:R05828]
ALL_REAC    R05828
SUBSTRATE   10-deoxysarpagine [CPD:C11635];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     sarpagine [CPD:C09239];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450).
REFERENCE   1  [PMID:12057637]
  AUTHORS   Yu B, Ruppert M, Stockigt J.
  TITLE     Deoxysarpagine hydroxylase--a novel enzyme closing a short side
            pathway of alkaloid biosynthesis in Rauvolfia.
  JOURNAL   Bioorg. Med. Chem. 10 (2002) 2479-83.
  ORGANISM  Rauvolfia serpentina
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.91
            ExPASy - ENZYME nomenclature database: 1.14.13.91
            ExplorEnz - The Enzyme Database: 1.14.13.91
            ERGO genome analysis and discovery system: 1.14.13.91
            BRENDA, the Enzyme Database: 1.14.13.91
///
ENTRY       EC 1.14.13.92               Enzyme
NAME        phenylacetone monooxygenase;
            PAMO
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     phenylacetone,NADPH:oxygen oxidoreductase
REACTION    phenylacetone + NADPH + H+ + O2 = benzyl acetate + NADP+ + H2O
            [RN:R07201]
ALL_REAC    R07201
SUBSTRATE   phenylacetone [CPD:C15512];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     benzyl acetate [CPD:C15513];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A flavoprotein (FAD). NADH cannot replace NADPH as coenzyme. In
            addition to phenylacetone, which is the best substrate found to
            date, this Baeyer-Villiger monooxygenase can oxidize other aromatic
            ketones [1-(4-hydroxyphenyl)propan-2-one,
            1-(4-hydroxyphenyl)propan-2-one and 3-phenylbutan-2-one], some
            alipatic ketones (e.g. dodecan-2-one) and sulfides (e.g.
            1-methyl-4-(methylsulfanyl)benzene).
REFERENCE   1  [PMID:15328411]
  AUTHORS   Malito E, Alfieri A, Fraaije MW, Mattevi A.
  TITLE     Crystal structure of a Baeyer-Villiger monooxygenase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 13157-62.
  ORGANISM  Thermobifida fusca [GN:tfu]
REFERENCE   2  [PMID:15599520]
  AUTHORS   Fraaije MW, Wu J, Heuts DP, van Hellemond EW, Spelberg JH, Janssen
            DB.
  TITLE     Discovery of a thermostable Baeyer-Villiger monooxygenase by genome
            mining.
  JOURNAL   Appl. Microbiol. Biotechnol. 66 (2005) 393-400.
  ORGANISM  Thermobifida fusca [GN:tfu]
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.92
            ExPASy - ENZYME nomenclature database: 1.14.13.92
            ExplorEnz - The Enzyme Database: 1.14.13.92
            ERGO genome analysis and discovery system: 1.14.13.92
            BRENDA, the Enzyme Database: 1.14.13.92
///
ENTRY       EC 1.14.13.93               Enzyme
NAME        (+)-abscisic acid 8'-hydroxylase;
            (+)-ABA 8'-hydroxylase;
            ABA 8'-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     abscisate,NADPH:oxygen oxidoreductase (8'-hydroxylating)
REACTION    (+)-abscisate + NADPH + H+ + O2 = 8'-hydroxyabscisate + NADP+ + H2O
            [RN:R07202]
ALL_REAC    R07202
SUBSTRATE   (+)-abscisate;
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     8'-hydroxyabscisate [CPD:C15514];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450). Catalyses the first step in the
            oxidative degradation of abscisic acid and is considered to be the
            pivotal enzyme in controlling the rate of degradation of this plant
            hormone [1]. CO inhibits the reaction, but its effects can be
            reversed by the presence of blue light [1]. The 8'-hydroxyabscisate
            formed can be converted into (-)-phaseic acid, most probably
            spontaneously. Other enzymes involved in the abscisic-acid
            biosynthesis pathway are EC 1.1.1.288 (xanthoxin dehydrogenase), EC
            1.2.3.14 (abscisic-aldehyde oxidase) and EC 1.13.11.51
            (9-cis-epoxycarotenoid dioxygenase).
REFERENCE   1
  AUTHORS   Cutler, A.J., Squires, T.M., Loewen, M.K. and Balsevich, J.J.
  TITLE     Induction of (+)-abscisic acid 8' hydroxylase by (+)-abscisic acid
            in cultured maize cells.
  JOURNAL   J. Exp. Bot. 48 (1997) 1787-1795.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   2  [PMID:9808729]
  AUTHORS   Krochko JE, Abrams GD, Loewen MK, Abrams SR, Cutler AJ.
  TITLE     (+)-Abscisic acid 8'-hydroxylase is a cytochrome P450 monooxygenase
  JOURNAL   Plant. Physiol. 118 (1998) 849-60.
  ORGANISM  Zea mays [GN:ezma]
PATHWAY     PATH: map00906  Carotenoid biosynthesis - General
ORTHOLOGY   KO: K09843  (+)-abscisic acid 8'-hydroxylase
GENES       ATH: AT2G29090(CYP707A2) AT3G19270(CYP707A4) AT4G19230(CYP707A1)
                 AT5G45340(CYP707A3)
            OSA: 4330448 4347261
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.93
            ExPASy - ENZYME nomenclature database: 1.14.13.93
            ExplorEnz - The Enzyme Database: 1.14.13.93
            ERGO genome analysis and discovery system: 1.14.13.93
            BRENDA, the Enzyme Database: 1.14.13.93
///
ENTRY       EC 1.14.13.94               Enzyme
NAME        lithocholate 6beta-hydroxylase;
            lithocholate 6beta-monooxygenase;
            CYP3A10;
            6beta-hydroxylase;
            cytochrome P450 3A10/lithocholic acid 6beta-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     lithocholate,NADPH:oxygen oxidoreductase (6beta-hydroxylating)
REACTION    lithocholate + NADPH + H+ + O2 = 6beta-hydroxylithocholate + NADP+ +
            H2O [RN:R07203]
ALL_REAC    R07203
SUBSTRATE   lithocholate [CPD:C03990];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     6beta-hydroxylithocholate [CPD:C15515];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450). Expression of the gene for this
            enzyme is 50-fold higher in male compared to female hamsters [1].
REFERENCE   1  [PMID:1840595]
  AUTHORS   Teixeira J, Gil G.
  TITLE     Cloning, expression, and regulation of lithocholic acid 6
            beta-hydroxylase.
  JOURNAL   J. Biol. Chem. 266 (1991) 21030-6.
  ORGANISM  hamster
REFERENCE   2  [PMID:8484723]
  AUTHORS   Chang TK, Teixeira J, Gil G, Waxman DJ.
  TITLE     The lithocholic acid 6 beta-hydroxylase cytochrome P-450, CYP 3A10,
            is an active catalyst of steroid-hormone 6 beta-hydroxylation.
  JOURNAL   Biochem. J. 291 ( Pt 2) (1993) 429-33.
  ORGANISM  hamster
REFERENCE   3  [PMID:9547277]
  AUTHORS   Subramanian A, Wang J, Gil G.
  TITLE     STAT 5 and NF-Y are involved in expression and growth
            hormone-mediated sexually dimorphic regulation of cytochrome P450
            3A10/lithocholic acid 6beta-hydroxylase.
  JOURNAL   Nucleic. Acids. Res. 26 (1998) 2173-8.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:12543708]
  AUTHORS   Russell DW.
  TITLE     The enzymes, regulation, and genetics of bile acid synthesis.
  JOURNAL   Annu. Rev. Biochem. 72 (2003) 137-74.
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.94
            ExPASy - ENZYME nomenclature database: 1.14.13.94
            ExplorEnz - The Enzyme Database: 1.14.13.94
            ERGO genome analysis and discovery system: 1.14.13.94
            BRENDA, the Enzyme Database: 1.14.13.94
///
ENTRY       EC 1.14.13.95               Enzyme
NAME        7alpha-hydroxycholest-4-en-3-one 12alpha-hydroxylase;
            7alpha-hydroxy-4-cholesten-3-one 12alpha-monooxygenase;
            CYP12;
            sterol 12alpha-hydroxylase (ambiguous);
            HCO 12alpha-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     7alpha-hydroxycholest-4-en-3-one,NADPH:oxygen oxidoreductase
            (12alpha-hydroxylating)
REACTION    7alpha-hydroxycholest-4-en-3-one + NADPH + H+ + O2 =
            7alpha,12alpha-dihydroxycholest-4-en-3-one + NADP+ + H2O [RN:R04826]
ALL_REAC    R04826
SUBSTRATE   7alpha-hydroxycholest-4-en-3-one [CPD:C05455];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     7alpha,12alpha-dihydroxycholest-4-en-3-one [CPD:C05457];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450). Requires EC 1.6.2.4,
            NADPH---hemoprotein reductase and cytochrome b5 for maximal
            activity. This enzyme is important in bile acid biosynthesis, being
            responsible for the balance between the formation of cholic acid and
            chenodeoxycholic acid [2].
REFERENCE   1  [PMID:1400444]
  AUTHORS   Ishida H, Noshiro M, Okuda K, Coon MJ.
  TITLE     Purification and characterization of 7
            alpha-hydroxy-4-cholesten-3-one 12 alpha-hydroxylase.
  JOURNAL   J. Biol. Chem. 267 (1992) 21319-23.
  ORGANISM  rabbit
REFERENCE   2  [PMID:8943286]
  AUTHORS   Eggertsen G, Olin M, Andersson U, Ishida H, Kubota S, Hellman U,
            Okuda KI, Bjorkhem I.
  TITLE     Molecular cloning and expression of rabbit sterol
            12alpha-hydroxylase.
  JOURNAL   J. Biol. Chem. 271 (1996) 32269-75.
  ORGANISM  rabbit
REFERENCE   3  [PMID:12543708]
  AUTHORS   Russell DW.
  TITLE     The enzymes, regulation, and genetics of bile acid synthesis.
  JOURNAL   Annu. Rev. Biochem. 72 (2003) 137-74.
PATHWAY     PATH: map03320  PPAR signaling pathway
ORTHOLOGY   KO: K07431  cytochrome P450, family 8, subfamily B (sterol
                        12-alpha-hydroxylase)
GENES       HSA: 1582(CYP8B1)
            MMU: 13124(Cyp8b1)
            RNO: 81924(Cyp8b1)
            CFA: 485619(LOC485619)
            BTA: 538964(CYP8B1)
            SSC: 403328(CYP8B1)
            GGA: 425055(CYP8B)
            UMA: UM04362.1
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.95
            ExPASy - ENZYME nomenclature database: 1.14.13.95
            ExplorEnz - The Enzyme Database: 1.14.13.95
            ERGO genome analysis and discovery system: 1.14.13.95
            BRENDA, the Enzyme Database: 1.14.13.95
///
ENTRY       EC 1.14.13.96               Enzyme
NAME        5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase;
            5beta-cholestane-3alpha,7alpha-diol 12alpha-monooxygenase;
            sterol 12alpha-hydroxylase (ambiguous);
            CYP8B1;
            cytochrome P450 8B1
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     5beta-cholestane-3alpha,7alpha-diol,NADPH:oxygen oxidoreductase
            (12alpha-hydroxylating)
REACTION    5beta-cholestane-3alpha,7alpha-diol + NADPH + H+ + O2 =
            5beta-cholestane-3alpha,7alpha,12alpha-triol + NADP+ + H2O
            [RN:R07204]
ALL_REAC    R07204
SUBSTRATE   5beta-cholestane-3alpha,7alpha-diol [CPD:C05452];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     5beta-cholestane-3alpha,7alpha,12alpha-triol [CPD:C05454];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450). This is the key enzyme in the
            biosynthesis of the bile acid cholic acid
            (3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoic acid). The
            activity of this enzyme determines the biosynthetic ratio between
            cholic acid and chenodeoxycholic acid [3]. The enzyme can also
            hydroxylate the substrate at the 25 and 26 position, but to a lesser
            extent [1].
REFERENCE   1  [PMID:6811268]
  AUTHORS   Hansson R, Wikvall K.
  TITLE     Hydroxylations in biosynthesis of bile acids. Cytochrome P-450 LM4
            and 12alpha-hydroxylation of 5beta-cholestane-3alpha, 7alpha-diol.
  JOURNAL   Eur. J. Biochem. 125 (1982) 423-9.
  ORGANISM  rabbit
REFERENCE   2  [PMID:6766451]
  AUTHORS   Hansson R, Wikvall K.
  TITLE     Hydroxylations in biosynthesis and metabolism of bile acids.
            Catalytic properties of different forms of cytochrome P-450.
  JOURNAL   J. Biol. Chem. 255 (1980) 1643-9.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:14643796]
  AUTHORS   Lundell K, Wikvall K.
  TITLE     Gene structure of pig sterol 12alpha-hydroxylase (CYP8B1) and
            expression in fetal liver: comparison with expression of
            taurochenodeoxycholic acid 6alpha-hydroxylase (CYP4A21).
  JOURNAL   Biochim. Biophys. Acta. 1634 (2003) 86-96.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:11516175]
  AUTHORS   Lukacin R, Matern U, Junghanns KT, Heskamp ML, Britsch L, Forkmann
            G, Martens S.
  TITLE     Purification and antigenicity of flavone synthase I from irradiated
            parsley cells.
  JOURNAL   Arch. Biochem. Biophys. 393 (2001) 177-83.
REFERENCE   5  [PMID:12069850]
  AUTHORS   Yang Y, Zhang M, Eggertsen G, Chiang JY.
  TITLE     On the mechanism of bile acid inhibition of rat sterol
            12alpha-hydroxylase gene (CYP8B1) transcription: roles of
            alpha-fetoprotein transcription factor and hepatocyte nuclear factor
            4alpha.
  JOURNAL   Biochim. Biophys. Acta. 1583 (2002) 63-73.
  ORGANISM  rat [GN:rno]
REFERENCE   6  [PMID:12543708]
  AUTHORS   Russell DW.
  TITLE     The enzymes, regulation, and genetics of bile acid synthesis.
  JOURNAL   Annu. Rev. Biochem. 72 (2003) 137-74.
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.96
            ExPASy - ENZYME nomenclature database: 1.14.13.96
            ExplorEnz - The Enzyme Database: 1.14.13.96
            ERGO genome analysis and discovery system: 1.14.13.96
            BRENDA, the Enzyme Database: 1.14.13.96
///
ENTRY       EC 1.14.13.97               Enzyme
NAME        taurochenodeoxycholate 6alpha-hydroxylase;
            CYP3A4;
            CYP4A21;
            taurochenodeoxycholate 6alpha-monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     taurochenodeoxycholate,NADPH:oxygen oxidoreductase
            (6alpha-hydroxylating)
REACTION    (1) taurochenodeoxycholate + NADPH + H+ + O2 = taurohyocholate +
            NADP+ + H2O [RN:R07205];
            (2) lithocholate + NADPH + H+ + O2 = hyodeoxycholate + NADP+ + H2O
            [RN:R07206]
ALL_REAC    R07205 R07206
SUBSTRATE   taurochenodeoxycholate [CPD:C05465];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007];
            lithocholate [CPD:C03990]
PRODUCT     taurohyocholate [CPD:C15516];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            hyodeoxycholate [CPD:C15517]
COMMENT     A heme-thiolate protein (P-450). Requires cytochrome b5 for maximal
            activity. Acts on taurochenodeoxycholate, taurodeoxycholate and less
            readily on lithocholate and chenodeoxycholate. In adult pig (Sus
            scrofa), hyocholic acid replaces cholic acid as a primary bile acid
            [5].
REFERENCE   1  [PMID:10216279]
  AUTHORS   Araya Z, Wikvall K.
  TITLE     6alpha-hydroxylation of taurochenodeoxycholic acid and lithocholic
            acid by CYP3A4 in human liver microsomes.
  JOURNAL   Biochim. Biophys. Acta. 1438 (1999) 47-54.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:7649186]
  AUTHORS   Araya Z, Hellman U, Hansson R.
  TITLE     Characterisation of taurochenodeoxycholic acid 6 alpha-hydroxylase
            from pig liver microsomes.
  JOURNAL   Eur. J. Biochem. 231 (1995) 855-61.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:11069906]
  AUTHORS   Kramer W, Sauber K, Baringhaus KH, Kurz M, Stengelin S, Lange G,
            Corsiero D, Girbig F, Konig W, Weyland C.
  TITLE     Identification of the bile acid-binding site of the ileal
            lipid-binding protein by photoaffinity labeling, matrix-assisted
            laser desorption ionization-mass spectrometry, and NMR structure.
  JOURNAL   J. Biol. Chem. 276 (2001) 7291-301.
  ORGANISM  rabbit
REFERENCE   4  [PMID:11113117]
  AUTHORS   Lundell K, Hansson R, Wikvall K.
  TITLE     Cloning and expression of a pig liver taurochenodeoxycholic acid
            6alpha-hydroxylase (CYP4A21): a novel member of the CYP4A subfamily.
  JOURNAL   J. Biol. Chem. 276 (2001) 9606-12.
  ORGANISM  pig [GN:ssc]
REFERENCE   5  [PMID:14643796]
  AUTHORS   Lundell K, Wikvall K.
  TITLE     Gene structure of pig sterol 12alpha-hydroxylase (CYP8B1) and
            expression in fetal liver: comparison with expression of
            taurochenodeoxycholic acid 6alpha-hydroxylase (CYP4A21).
  JOURNAL   Biochim. Biophys. Acta. 1634 (2003) 86-96.
  ORGANISM  pig [GN:ssc]
REFERENCE   6  [PMID:12543708]
  AUTHORS   Russell DW.
  TITLE     The enzymes, regulation, and genetics of bile acid synthesis.
  JOURNAL   Annu. Rev. Biochem. 72 (2003) 137-74.
STRUCTURES  PDB: 2J0D  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.97
            ExPASy - ENZYME nomenclature database: 1.14.13.97
            ExplorEnz - The Enzyme Database: 1.14.13.97
            ERGO genome analysis and discovery system: 1.14.13.97
            BRENDA, the Enzyme Database: 1.14.13.97
///
ENTRY       EC 1.14.13.98               Enzyme
NAME        cholesterol 24-hydroxylase;
            cholesterol 24-monooxygenase;
            CYP46;
            CYP46A1;
            cholesterol 24S-hydroxylase;
            cytochrome P450 46A1
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     cholesterol,NADPH:oxygen oxidoreductase (24-hydroxylating)
REACTION    cholesterol + NADPH + H+ + O2 = (24S)-24-hydroxycholesterol + NADP+
            + H2O [RN:R07207]
ALL_REAC    R07207
SUBSTRATE   cholesterol [CPD:C00187];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (24S)-24-hydroxycholesterol [CPD:C13550];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450). The enzyme can also produce
            25-hydroxycholesterol. In addition, it can further hydroxylate the
            product to 24,25-dihydroxycholesterol and 24,27-dihydroxycholesterol
            [2]. This reaction is the first step in the enzymatic degradation of
            cholesterol in the brain as hydroxycholesterol can pass the
            blood---brain barrier whereas cholesterol cannot [3].
REFERENCE   1  [PMID:10377398]
  AUTHORS   Lund EG, Guileyardo JM, Russell DW.
  TITLE     cDNA cloning of cholesterol 24-hydroxylase, a mediator of
            cholesterol homeostasis in the brain.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 7238-43.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:14640697]
  AUTHORS   Mast N, Norcross R, Andersson U, Shou M, Nakayama K, Bjorkhem I,
            Pikuleva IA.
  TITLE     Broad substrate specificity of human cytochrome P450 46A1 which
            initiates cholesterol degradation in the brain.
  JOURNAL   Biochemistry. 42 (2003) 14284-92.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:12686551]
  AUTHORS   Lund EG, Xie C, Kotti T, Turley SD, Dietschy JM, Russell DW.
  TITLE     Knockout of the cholesterol 24-hydroxylase gene in mice reveals a
            brain-specific mechanism of cholesterol turnover.
  JOURNAL   J. Biol. Chem. 278 (2003) 22980-8.
  ORGANISM  mouse [GN:mmu], human [GN:hsa]
REFERENCE   4  [PMID:11698143]
  AUTHORS   Bogdanovic N, Bretillon L, Lund EG, Diczfalusy U, Lannfelt L,
            Winblad B, Russell DW, Bjorkhem I.
  TITLE     On the turnover of brain cholesterol in patients with Alzheimer's
            disease. Abnormal induction of the cholesterol-catabolic enzyme
            CYP46 in glial cells.
  JOURNAL   Neurosci. Lett. 314 (2001) 45-8.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:12543708]
  AUTHORS   Russell DW.
  TITLE     The enzymes, regulation, and genetics of bile acid synthesis.
  JOURNAL   Annu. Rev. Biochem. 72 (2003) 137-74.
ORTHOLOGY   KO: K07440  cytochrome P450, family 46, subfamily A (cholesterol
                        24(S)-hydroxylase)
GENES       HSA: 10858(CYP46A1)
            PTR: 453154(CYP46A1)
            MMU: 13116(Cyp46a1)
            RNO: 362782(Cyp46a1_predicted)
            CFA: 480432(LOC480432)
            GGA: 423450(LOC423450)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.98
            ExPASy - ENZYME nomenclature database: 1.14.13.98
            ExplorEnz - The Enzyme Database: 1.14.13.98
            ERGO genome analysis and discovery system: 1.14.13.98
            BRENDA, the Enzyme Database: 1.14.13.98
///
ENTRY       EC 1.14.13.99               Enzyme
NAME        24-hydroxycholesterol 7alpha-hydroxylase;
            24-hydroxycholesterol 7alpha-monooxygenase;
            CYP39A1;
            CYP39A1 oxysterol 7alpha-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     (24R)-cholest-5-ene-3beta,24-diol,NADPH:oxygen oxidoreductase
            (7alpha-hydroxylating)
REACTION    (24R)-cholest-5-ene-3beta,24-diol + NADPH + H+ + O2 =
            (24R)-cholest-5-ene-3beta,7alpha,24-triol + NADP+ + H2O [RN:R07208]
ALL_REAC    R07208
SUBSTRATE   (24R)-cholest-5-ene-3beta,24-diol;
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (24R)-cholest-5-ene-3beta,7alpha,24-triol;
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate protein (P-450) that is found in liver microsomes
            and in ciliary non-pigmented epithelium [2]. The enzyme is specific
            for (24R)-cholest-5-ene-3beta,24-diol as substrate.
REFERENCE   1  [PMID:10748047]
  AUTHORS   Li-Hawkins J, Lund EG, Bronson AD, Russell DW.
  TITLE     Expression cloning of an oxysterol 7alpha-hydroxylase selective for
            24-hydroxycholesterol.
  JOURNAL   J. Biol. Chem. 275 (2000) 16543-9.
  ORGANISM  human [GN:hsa], mouse  [GN:mmu]
REFERENCE   2  [PMID:12649335]
  AUTHORS   Ikeda H, Ueda M, Ikeda M, Kobayashi H, Honda Y.
  TITLE     Oxysterol 7alpha-hydroxylase (CYP39A1) in the ciliary nonpigmented
            epithelium of bovine eye.
  JOURNAL   Lab. Invest. 83 (2003) 349-55.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:12543708]
  AUTHORS   Russell DW.
  TITLE     The enzymes, regulation, and genetics of bile acid synthesis.
  JOURNAL   Annu. Rev. Biochem. 72 (2003) 137-74.
ORTHOLOGY   KO: K07439  cytochrome P450, family 39, subfamily A
                        (24-hydroxycholesterol 7alpha-hydroxylase)
GENES       HSA: 51302(CYP39A1)
            PTR: 462743(CYP39A1)
            MMU: 56050(Cyp39a1)
            RNO: 301264(Cyp39a1_predicted)
            CFA: 481825(LOC481825)
            GGA: 422058(LOC422058)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.99
            ExPASy - ENZYME nomenclature database: 1.14.13.99
            ExplorEnz - The Enzyme Database: 1.14.13.99
            ERGO genome analysis and discovery system: 1.14.13.99
            BRENDA, the Enzyme Database: 1.14.13.99
///
ENTRY       EC 1.14.13.100              Enzyme
NAME        25-hydroxycholesterol 7alpha-hydroxylase;
            25-hydroxycholesterol 7alpha-monooxygenase;
            CYP7B1;
            CYP7B1 oxysterol 7alpha-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     cholest-5-ene-3beta,25-diol,NADPH:oxygen oxidoreductase
            (7alpha-hydroxylating)
REACTION    (1) cholest-5-ene-3beta,25-diol + NADPH + H+ + O2 =
            cholest-5-ene-3beta,7alpha,25-triol + NADP+ + H2O;
            (2) cholest-5-ene-3beta,27-diol + NADPH + H+ + O2 =
            cholest-5-ene-3beta,7alpha,27-triol + NADP+ + H2O
ALL_REAC    (other) R07209 R07372
SUBSTRATE   cholest-5-ene-3beta,25-diol [CPD:C15519];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007];
            cholest-5-ene-3beta,27-diol [CPD:C15610]
PRODUCT     cholest-5-ene-3beta,7alpha,25-triol [CPD:C15520];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            cholest-5-ene-3beta,7alpha,27-triol [CPD:C06341]
COMMENT     A heme-thiolate protein (P-450). Unlike EC 1.14.13.99,
            24-hydroxycholesterol 7alpha-monooxygenase, which is specific for
            its oxysterol substrate, this enzyme can also metabolize the
            oxysterols 24,25-epoxycholesterol, 22-hydroxycholesterol and
            24-hydroxycholesterol, but to a lesser extent [2].
REFERENCE   1  [PMID:7925343]
  AUTHORS   Toll A, Wikvall K, Sudjana-Sugiaman E, Kondo KH, Bjorkhem I.
  TITLE     7 alpha hydroxylation of 25-hydroxycholesterol in liver microsomes.
            Evidence that the enzyme involved is different from cholesterol 7
            alpha-hydroxylase.
  JOURNAL   Eur. J. Biochem. 224 (1994) 309-16.
  ORGANISM  rat [GN:rno], pig [GN:ssc], human [GN:hsa]
REFERENCE   2  [PMID:10748047]
  AUTHORS   Li-Hawkins J, Lund EG, Bronson AD, Russell DW.
  TITLE     Expression cloning of an oxysterol 7alpha-hydroxylase selective for
            24-hydroxycholesterol.
  JOURNAL   J. Biol. Chem. 275 (2000) 16543-9.
  ORGANISM  mouse [GN:mmu], human [GN:hsa]
REFERENCE   3  [PMID:12759897]
  AUTHORS   Ren S, Marques D, Redford K, Hylemon PB, Gil G, Vlahcevic ZR, Pandak
            WM.
  TITLE     Regulation of oxysterol 7alpha-hydroxylase (CYP7B1) in the rat.
  JOURNAL   Metabolism. 52 (2003) 636-42.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:12543708]
  AUTHORS   Russell DW.
  TITLE     The enzymes, regulation, and genetics of bile acid synthesis.
  JOURNAL   Annu. Rev. Biochem. 72 (2003) 137-74.
ORTHOLOGY   KO: K07430  cytochrome P450, family 7, subfamily B (oxysterol
                        7-alpha-hydroxylase)
GENES       HSA: 9420(CYP7B1)
            MMU: 13123(Cyp7b1)
            RNO: 25429(Cyp7b1)
            CFA: 486973(LOC486973)
            BTA: 529552(LOC529552)
            GGA: 420164(CYP7B1)
            DRE: 570455(LOC570455)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.100
            ExPASy - ENZYME nomenclature database: 1.14.13.100
            ExplorEnz - The Enzyme Database: 1.14.13.100
            ERGO genome analysis and discovery system: 1.14.13.100
            BRENDA, the Enzyme Database: 1.14.13.100
///
ENTRY       EC 1.14.13.101              Enzyme
NAME        senecionine N-oxygenase;
            senecionine monooxygenase (N-oxide-forming);
            SNO
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     senecionine,NADPH:oxygen oxidoreductase (N-oxide-forming)
REACTION    senecionine + NADPH + H+ + O2 = senecionine N-oxide + NADP+ + H2O
            [RN:R07373]
ALL_REAC    R07373
SUBSTRATE   senecionine [CPD:C06176];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     senecionine N-oxide [CPD:C15612];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A flavoprotein. NADH cannot replace NADPH. While pyrrolizidine
            alkaloids of the senecionine and monocrotaline types are generally
            good substrates (e.g. senecionine, retrorsine and monocrotaline),
            the enzyme does not use ester alkaloids lacking an hydroxy group at
            C-7 (e.g. supinine and phalaenopsine), 1,2-dihydro-alkaloids (e.g.
            sarracine) or unesterified necine bases (e.g. senkirkine) as
            substrates [1]. Senecionine N-oxide is used by insects as a chemical
            defense: senecionine N-oxide is non-toxic, but it is bioactivated to
            a toxic form by the action of cytochrome P-450 oxidase when absorbed
            by insectivores.
REFERENCE   1  [PMID:9182998]
  AUTHORS   Lindigkeit R, Biller A, Buch M, Schiebel HM, Boppre M, Hartmann T.
  TITLE     The two facies of pyrrolizidine alkaloids: the role of the tertiary
            amine and its N-oxide in chemical defense of insects with acquired
            plant alkaloids.
  JOURNAL   Eur. J. Biochem. 245 (1997) 626-36.
  ORGANISM  Creatonotos transiens, Zonocerus variegatus, Arctia caja, Tyria
            jacobaeae
REFERENCE   2  [PMID:11972041]
  AUTHORS   Naumann C, Hartmann T, Ober D.
  TITLE     Evolutionary recruitment of a flavin-dependent monooxygenase for the
            detoxification of host plant-acquired pyrrolizidine alkaloids in the
            alkaloid-defended arctiid moth Tyria jacobaeae.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 6085-90.
  ORGANISM  Tyria jacobaeae
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.101
            ExPASy - ENZYME nomenclature database: 1.14.13.101
            ExplorEnz - The Enzyme Database: 1.14.13.101
            ERGO genome analysis and discovery system: 1.14.13.101
            BRENDA, the Enzyme Database: 1.14.13.101
            CAS: 220581-68-0
///
ENTRY       EC 1.14.13.102              Enzyme
NAME        psoralen synthase;
            CYP71AJ1
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
REACTION    (+)-marmesin + NADPH + H+ + O2 = psoralen + NADP+ + acetone + 2 H2O
SUBSTRATE   (+)-marmesin;
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     psoralen [CPD:C09305];
            NADP+ [CPD:C00006];
            acetone [CPD:C00207];
            H2O [CPD:C00001]
COMMENT     This microsomal cytochrome P450-dependent enzyme is specific for
            (+)-marmesin, and to a much lesser extent 5-hydroxymarmesin, as
            substrate. Furanocoumarins protect plants from fungal invasion and
            herbivore attack. (+)-Columbianetin, the angular furanocoumarin
            analogue of the linear furanocoumarin (+)-marmesin, is not a
            substrate for the enzyme but it is a competitive inhibitor.
REFERENCE   1  [PMID:17068340]
  AUTHORS   Larbat R, Kellner S, Specker S, Hehn A, Gontier E, Hans J, Bourgaud
            F, Matern U.
  TITLE     Molecular cloning and functional characterization of psoralen
            synthase, the first committed monooxygenase of furanocoumarin
            biosynthesis.
  JOURNAL   J. Biol. Chem. 282 (2007) 542-54.
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.102
            ExPASy - ENZYME nomenclature database: 1.14.13.102
            ExplorEnz - The Enzyme Database: 1.14.13.102
            ERGO genome analysis and discovery system: 1.14.13.102
            BRENDA, the Enzyme Database: 1.14.13.102
///
ENTRY       EC 1.14.13.103              Enzyme
NAME        8-dimethylallylnaringenin 2'-hydroxylase;
            8-DMAN 2'-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     sophoraflavanone-B,NADPH:oxygen oxidoreductase (2'-hydroxylating)
REACTION    sophoraflavanone B + NADPH + H+ + O2 = leachianone G + NADP+ + H2O
SUBSTRATE   sophoraflavanone B;
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     leachianone G;
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A membrane-bound heme-thiolate protein that is associated with the
            endoplasmic reticulum [1,2]. This enzyme is specific for
            sophoraflavanone B as substrate. NADPH cannot be replaced by NADH,
            FAD or FMN. Along with EC 2.5.1.70 (naringenin
            8-dimethylallyltransferase) and EC 2.5.1.71 (leachianone G
            2"-dimethylallyltransferase), this enzyme forms part of the
            sophoraflavanone-G-biosynthesis pathway. A member of the
            cytochrome-P450 monooxygenase family.
REFERENCE   1  [PMID:11672730]
  AUTHORS   Yamamoto H, Yatou A, Inoue K.
  TITLE     8-dimethylallylnaringenin 2'-hydroxylase, the crucial cytochrome
            P450 mono-oxygenase for lavandulylated flavanone formation in
            Sophora flavescens cultured cells.
  JOURNAL   Phytochemistry. 58 (2001) 671-6.
REFERENCE   2  [PMID:14551337]
  AUTHORS   Zhao P, Inoue K, Kouno I, Yamamoto H.
  TITLE     Characterization of leachianone G 2"-dimethylallyltransferase, a
            novel prenyl side-chain elongation enzyme for the formation of the
            lavandulyl group of sophoraflavanone G in Sophora flavescens Ait.
            cell suspension cultures.
  JOURNAL   Plant. Physiol. 133 (2003) 1306-13.
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.13.103
            ExPASy - ENZYME nomenclature database: 1.14.13.103
            ExplorEnz - The Enzyme Database: 1.14.13.103
            ERGO genome analysis and discovery system: 1.14.13.103
            BRENDA, the Enzyme Database: 1.14.13.103
///
ENTRY       EC 1.14.13.-                Enzyme
CLASS       Oxidoreductases;
            Acting on paired donors with incorporation of molecular oxygen;
            With NADH or NADPH as one donor, and incorporation of one atom of
            oxygen
REACTION    (1) 2 Hydantoin-5-propionate <=> Oxygen + 2
            4-Imidazolone-5-propanoate [RN:R00069];
            (2) Cholesterol + Oxygen + NADPH <=>
            Cholesterol-5alpha,6beta-epoxide + NADP+ + H2O [RN:R01452];
            (3) Cholesterol + Oxygen + NADPH <=> Cholesterol-5beta,6beta-epoxide
            + NADP+ + H2O [RN:R01453];
            (4) Estrone + H+ + Oxygen + NADH <=> 2-Hydroxyestrone + NAD+ + H2O
            [RN:R02354];
            (5) Estrone + H+ + Oxygen + NADPH <=> 2-Hydroxyestrone + NADP+ + H2O
            [RN:R02355];
            (6) Estrone + H+ + Oxygen + NADPH <=> 16alpha-Hydroxyestrone + NADP+
            + H2O [RN:R02356];
            (7) Tyramine + Oxygen + NADH + H+ <=>
            4-(2-Aminoethyl)-1,2-benzenediol + NAD+ + H2O [RN:R02383];
            (8) Estradiol-17beta + H+ + Oxygen + NADH <=>
            2-Hydroxyestradiol-17beta + NAD+ + H2O [RN:R03088];
            (9) Estradiol-17beta + H+ + Oxygen + NADPH <=> Estriol + NADP+ + H2O
            [RN:R03089];
            (10) Estradiol-17beta + H+ + Oxygen + NADPH <=>
            2-Hydroxyestradiol-17beta + NADP+ + H2O [RN:R03090];
            (11) Indolelactate + Oxygen + NADPH <=> 6-Hydroxyindolelactate +
            NADP+ + H2O [RN:R03811];
            (12) (Z)-4-Hydroxyphenylacetaldehyde-oxime + NADPH + H+ + Oxygen <=>
            4-Hydroxymandelonitrile + NADP+ + 2 H2O [RN:R04306];
            (13) 5-Cholestene + Oxygen + NADPH + H+ <=>
            5,6beta-Epoxy-5beta-cholestane + NADP+ + H2O [RN:R04789];
            (14) 5-Cholestene + NADPH <=> 5,6beta-Epoxy-5alpha-cholestane +
            NADP+ + H2O [RN:R04790];
            (15) 7alpha-Hydroxycholest-4-en-3-one + H+ + Oxygen + NADPH <=>
            7alpha,12alpha-Dihydroxycholest-4-en-3-one + NADP+ + H2O
            [RN:R04826];
            (16) 2-Hexaprenylphenol + Oxygen + NADPH <=>
            2-Hexaprenyl-6-hydroxyphenol + NADP+ + H2O [RN:R04980];
            (17) 2-Hexaprenyl-6-methoxyphenol + Oxygen <=>
            2-Hexaprenyl-6-methoxy-1,4-benzoquinone + H2O [RN:R04982];
            (18) 2-Hexaprenyl-3-methyl-6-methoxy-1,4-benzoquinone + Oxygen +
            NADPH <=> 2-Hexaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone
            + NADP+ + H2O [RN:R04984];
            (19) 2-Octaprenyl-6-methoxyphenol + Oxygen + NADPH <=>
            2-Octaprenyl-6-methoxy-1,4-benzoquinone + NADP+ + H2O [RN:R04989];
            (20) 2-Hydroxyphenylacetate <=> 2,6-Dihydroxyphenylacetate
            [RN:R05001];
            (21) p-Benzoquinone + Nitrite + NADP+ + H2O <=> 4-Nitrophenol +
            Oxygen + NADPH [RN:R05258];
            (22) Toluene-4-sulfonate + Oxygen + NADH <=> 4-Sulfobenzyl alcohol +
            NAD+ + H2O [RN:R05281];
            (23) p-Xylene + Oxygen + NADH + H+ <=> 4-Methylbenzyl alcohol + NAD+
            + H2O [RN:R05288];
            (24) o-Xylene + Oxygen + NADH + H+ <=> 2-Methylbenzyl alcohol + NAD+
            + H2O [RN:R05442];
            (25) m-Xylene + Oxygen + NADH + H+ <=> 3-Methylbenzyl alcohol + NAD+
            + H2O [RN:R05443];
            (26) 2,5-Dichlorohydroquinone + 2 NADH + Oxygen <=>
            5-Chloro-1,2,4-trihydroxybenzene + 2 NAD+ + HO- + Cl- [RN:R05446];
            (27) 2,4,5-Trichlorophenol + 2 NADH + Oxygen <=>
            2,5-Dichlorohydroquinone + 2 NAD+ + HO- + Cl- [RN:R05447];
            (28) 2,6-Dichlorophenol + Oxygen + NADH + H+ <=>
            2,6-Dichlorohydroquinone + NAD+ + H2O [RN:R05448];
            (29) 2,4,6-Trichlorophenol + 2 NADH + Oxygen <=>
            2,6-Dichlorohydroquinone + 2 NAD+ + HO- + Cl- [RN:R05449];
            (30) 2-Hydroxyphenylacetate + Oxygen + NADH + H+ <=> Homogentisate +
            NAD+ + H2O [RN:R05450];
            (31) Phenylacetic acid + Oxygen + NADH + H+ <=>
            2-Hydroxyphenylacetate + NAD+ + H2O [RN:R05487];
            (32) Styrene + Oxygen + NADPH + H+ + FAD <=> Styrene oxide + NADP+ +
            FADH2 + H2O [RN:R05488];
            (33) Trimethylamine + NADH + H+ + Oxygen <=> Trimethylamine N-oxide
            + NAD+ + H2O [RN:R05623];
            (34) Phenanthracene + Oxygen + NADH + H+ <=> Phenanthrene-9,10-oxide
            + H2O + NAD+ [RN:R05653];
            (35) Phenanthracene + Oxygen + NADH + H+ <=> Phenanthrene-1,2-oxide
            + H2O + NAD+ [RN:R05654];
            (36) Phenanthracene + Oxygen + NADH + H+ <=> 1-Phenanthrol + H2O +
            NAD+ [RN:R05655];
            (37) 2-Octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone + Oxygen +
            NADPH + H+ <=>
            2-Octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone + NADP+ +
            H2O [RN:R06146];
            (38) (+)-Limonene + NADH + Oxygen <=> Limonene-1,2-epoxide + NAD+ +
            HO- [RN:R06398];
            (39) (1S,4R)-1-Hydroxy-2-oxolimonene + NADPH + Oxygen <=>
            (3R)-3-Isopropenyl-6-oxoheptanoate + NADP+ + HO- [RN:R06400];
            (40) alpha-Pinene + NADH + H+ + Oxygen <=> alpha-Pinene-oxide + NAD+
            + H2O [RN:R06406];
            (41) Coniferyl aldehyde + NADPH + H+ + Oxygen <=>
            5-Hydroxyconiferaldehyde + NADP+ + H2O [RN:R06572];
            (42) Coniferyl alcohol + NADPH + H+ + Oxygen <=> 5-Hydroxyconiferyl
            alcohol + NADP+ + H2O [RN:R06573];
            (43) Tetracenomycin A2 <=> Tetracenomycin C [RN:R06704];
            (44) 3-(3-Hydroxy-phenyl)-propanoic acid + Oxygen + NADH + H+ <=>
            3-(2,3-Dihydroxyphenyl)propanoate + H2O + NAD+ [RN:R06786];
            (45) trans-3-Hydroxycinnamate + Oxygen + NADH + H+ <=>
            trans-2,3-Dihydroxycinnamate + H2O + NAD+ [RN:R06787];
            (46) p-Benzenediol + NADPH + H+ + Oxygen <=> Benzene-1,2,4-triol +
            NADP+ + H2O [RN:R06851];
            (47) Bisphenol A + NADH + H+ + Oxygen <=>
            1,2-Bis(4-hydroxyphenyl)-2-propanol + NAD+ + H2O [RN:R06883];
            (48) Bisphenol A + NADH + H+ + Oxygen <=>
            2,2-Bis(4-hydroxyphenyl)-1-propanol + NAD+ + H2O [RN:R06884];
            (49) 2,2-Bis(4-hydroxyphenyl)-1-propanol + NADH + H+ + Oxygen <=>
            2,3-Bis(4-hydroxyphenyl)-1,2-propanediol + NAD+ + H2O [RN:R06888];
            (50) 4-Ethylphenol + NADPH + H+ + Oxygen <=>
            1-(4'-Hydroxyphenyl)ethanol + NADP+ + H2O [RN:R06890];
            (51) 1-Methylnaphthalene + Oxygen + NADH + H+ <=>
            1-Hydroxymethylnaphthalene + NAD+ + H2O [RN:R06916];
            (52) 2-Methylnaphthalene + Oxygen + NADH + H+ <=>
            (2-Naphthyl)methanol + NAD+ + H2O [RN:R06926];
            (53) 6-Oxocampestanol + Oxygen + NADPH <=> Cathasterone + NADP+ +
            H2O [RN:R07430];
            (54) Ferulate + NADPH + H+ + Oxygen <=> 5-Hydroxyferulate + NADP+ +
            H2O [RN:R07440];
            (55) Campesterol + Oxygen + NADPH <=> 22alpha-Hydroxy-campesterol +
            NADP+ + H2O [RN:R07445];
            (56) Campest-4-en-3-one + Oxygen + NADPH <=>
            22alpha-Hydroxy-campest-4-en-3-one + NADP+ + H2O [RN:R07452];
            (57) 5alpha-Campestan-3-one + Oxygen + NADPH <=>
            22alpha-Hydroxy-5alpha-campestan-3-one + NADP+ + H2O [RN:R07453];
            (58) Campestanol + Oxygen + NADPH <=> 6-Deoxocathasterone + NADP+ +
            H2O [RN:R07454];
            (59) alpha-Carotene <=> Zeinoxanthin [RN:R07530];
            (60) 2 Toluene-4-sulfonate + Oxygen + 2 H+ <=> 2 4-Cresol + 2 HSO3-
            [RN:R07663];
            (61) 3-Cresol + Oxygen + NADH + H+ <=> 3-Hydroxybenzyl alcohol +
            NAD+ + H2O [RN:R07665];
            (62) Salicylate + NADH + Oxygen + H+ <=> 2,5-Dihydroxybenzoate +
            NAD+ + H2O [RN:R07709];
            (63) Salicylate + NADPH + Oxygen + H+ <=> 2,5-Dihydroxybenzoate +
            NADP+ + H2O [RN:R07710];
            (64) Thiobenzamide + Oxygen + NADPH + H+ <=> Thiobenzamide S-oxide +
            NADP+ + H2O [RN:R07836];
            (65) Thiobenzamide S-oxide + NADPH + H+ + Oxygen <=> Thiobenzamide
            S,S-dioxide + NADP+ + H2O [RN:R07837]
SUBSTRATE   Hydantoin-5-propionate [CPD:C05565];
            Cholesterol [CPD:C00187];
            Oxygen [CPD:C00007];
            NADPH [CPD:C00005];
            Androst-4-ene-3,17-dione [CPD:C00280];
            H+ [CPD:C00080];
            Estrone [CPD:C00468];
            NADH [CPD:C00004];
            Tyramine [CPD:C00483];
            Testosterone [CPD:C00535];
            Estradiol-17beta [CPD:C00951];
            Indolelactate [CPD:C02043];
            beta-Carotene [CPD:C02094];
            (Z)-4-Hydroxyphenylacetaldehyde-oxime [CPD:C04353];
            5-Cholestene [CPD:C05416];
            7alpha-Hydroxycholest-4-en-3-one [CPD:C05455];
            2-Hexaprenylphenol [CPD:C05800];
            2-Hexaprenyl-6-methoxyphenol [CPD:C05802];
            2-Hexaprenyl-3-methyl-6-methoxy-1,4-benzoquinone [CPD:C05804];
            2-Octaprenyl-6-methoxyphenol [CPD:C05812];
            2-Hydroxyphenylacetate [CPD:C05852];
            p-Benzoquinone [CPD:C00472];
            Nitrite [CPD:C00088];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            Toluene-4-sulfonate [CPD:C06677];
            p-Xylene [CPD:C06756];
            o-Xylene [CPD:C07212];
            m-Xylene [CPD:C07208];
            2,5-Dichlorohydroquinone [CPD:C06600];
            2,4,5-Trichlorophenol [CPD:C07101];
            2,6-Dichlorophenol [CPD:C07096];
            2,4,6-Trichlorophenol [CPD:C07098];
            Phenylacetic acid [CPD:C07086];
            Styrene [CPD:C07083];
            FAD [CPD:C00016];
            Trimethylamine [CPD:C00565];
            Phenanthracene [CPD:C11422];
            2-Octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone [CPD:C05814];
            (+)-Limonene [CPD:C06099];
            (1S,4R)-1-Hydroxy-2-oxolimonene [CPD:C11937];
            alpha-Pinene [CPD:C09880];
            Coniferyl aldehyde [CPD:C02666];
            Coniferyl alcohol [CPD:C00590];
            Tetracenomycin A2 [CPD:C12371];
            3-(3-Hydroxy-phenyl)-propanoic acid [CPD:C11457];
            trans-3-Hydroxycinnamate [CPD:C12621];
            Bisphenol A [CPD:C13624];
            2,2-Bis(4-hydroxyphenyl)-1-propanol [CPD:C13631];
            4-Ethylphenol [CPD:C13637];
            4'-Hydroxyacetophenone [CPD:C10700];
            1-Methylnaphthalene [CPD:C14082];
            2-Methylnaphthalene [CPD:C14098]
PRODUCT     Oxygen [CPD:C00007];
            4-Imidazolone-5-propanoate [CPD:C03680];
            Cholesterol-5alpha,6beta-epoxide [CPD:C05419];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            Cholesterol-5beta,6beta-epoxide [CPD:C05418];
            19-Hydroxyandrost-4-ene-3,17-dione [CPD:C05290];
            2-Hydroxyestrone [CPD:C05298];
            NAD+ [CPD:C00003];
            16alpha-Hydroxyestrone [CPD:C05300];
            4-(2-Aminoethyl)-1,2-benzenediol [CPD:C03758];
            19-Hydroxytestosterone [CPD:C05294];
            2-Hydroxyestradiol-17beta [CPD:C05301];
            Estriol [CPD:C05141];
            6-Hydroxyindolelactate [CPD:C05657];
            Zeaxanthin [CPD:C06098];
            4-Hydroxymandelonitrile [CPD:C00650];
            5,6beta-Epoxy-5beta-cholestane [CPD:C05417];
            5,6beta-Epoxy-5alpha-cholestane [CPD:C05423];
            7alpha,12alpha-Dihydroxycholest-4-en-3-one [CPD:C05457];
            2-Hexaprenyl-6-hydroxyphenol [CPD:C05801];
            2-Hexaprenyl-6-methoxy-1,4-benzoquinone [CPD:C05803];
            2-Hexaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone
            [CPD:C05805];
            2-Octaprenyl-6-methoxy-1,4-benzoquinone [CPD:C05813];
            2,6-Dihydroxyphenylacetate [CPD:C06207];
            4-Nitrophenol [CPD:C00870];
            NADPH [CPD:C00005];
            4-Sulfobenzyl alcohol [CPD:C06678];
            4-Methylbenzyl alcohol [CPD:C06757];
            2-Methylbenzyl alcohol [CPD:C07213];
            3-Methylbenzyl alcohol [CPD:C07216];
            5-Chloro-1,2,4-trihydroxybenzene [CPD:C07102];
            HO- [CPD:C01328];
            Cl- [CPD:C00698];
            2,5-Dichlorohydroquinone [CPD:C06600];
            2,6-Dichlorohydroquinone [CPD:C07097];
            Homogentisate [CPD:C00544];
            2-Hydroxyphenylacetate [CPD:C05852];
            Styrene oxide [CPD:C02083];
            FADH2 [CPD:C01352];
            Trimethylamine N-oxide [CPD:C01104];
            Phenanthrene-9,10-oxide [CPD:C11429];
            Phenanthrene-1,2-oxide [CPD:C11431];
            1-Phenanthrol [CPD:C11432];
            2-Octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone
            [CPD:C05815];
            Limonene-1,2-epoxide [CPD:C07271];
            (3R)-3-Isopropenyl-6-oxoheptanoate [CPD:C11405];
            alpha-Pinene-oxide [CPD:C02759];
            5-Hydroxyconiferaldehyde [CPD:C12204];
            5-Hydroxyconiferyl alcohol [CPD:C12205];
            Tetracenomycin C [CPD:C06801];
            3-(2,3-Dihydroxyphenyl)propanoate [CPD:C04044];
            trans-2,3-Dihydroxycinnamate [CPD:C12623];
            1,2-Bis(4-hydroxyphenyl)-2-propanol [CPD:C13629];
            2,2-Bis(4-hydroxyphenyl)-1-propanol [CPD:C13631];
            2,3-Bis(4-hydroxyphenyl)-1,2-propanediol [CPD:C13634];
            1-(4'-Hydroxyphenyl)ethanol [CPD:C13638];
            4-Hydroxyphenyl acetate [CPD:C13636];
            1-Hydroxymethylnaphthalene [CPD:C14089];
            (2-Naphthyl)methanol [CPD:C02909]
///
ENTRY       EC 1.14.14.1                Enzyme
NAME        unspecific monooxygenase;
            microsomal monooxygenase;
            xenobiotic monooxygenase;
            aryl-4-monooxygenase;
            aryl hydrocarbon hydroxylase;
            microsomal P-450;
            flavoprotein-linked monooxygenase;
            flavoprotein monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced flavin or flavoprotein as one donor, and incorporation
            of one atom of oxygen into the other donor
SYSNAME     substrate,reduced-flavoprotein:oxygen oxidoreductase
            (RH-hydroxylating or -epoxidizing)
REACTION    RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
            [RN:R04122]
ALL_REAC    R04122 > R03629 R04121;
            (other) R01840 R02501 R05259 R07000 R07001 R07016 R07020 R07021
            R07022 R07042 R07043 R07044 R07045 R07046 R07048 R07050 R07051
            R07052 R07054 R07055 R07056 R07066 R07068 R07075 R07079 R07080
            R07081 R07085 R07087 R07088 R07089 R07090 R07098 R07099 R07107
            R07112 R07939 R07943 R07945
SUBSTRATE   RH [CPD:C01371];
            reduced flavoprotein [CPD:C03024];
            O2 [CPD:C00007]
PRODUCT     ROH [CPD:C01335];
            oxidized flavoprotein [CPD:C03161];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A group of heme-thiolate proteins (P-450), acting on a wide range of
            substrates including many xenobiotics, steroids, fatty acids,
            vitamins and prostaglandins; reactions catalysed include
            hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and
            O-dealkylations, desulfation, deamination, and reduction of azo,
            nitro and N-oxide groups. Together with EC 1.6.2.4,
            NADPH---hemoprotein reductase, it forms a system in which two
            reducing equivalents are supplied by NADPH. Some of the reactions
            attributed to EC 1.14.15.3, alkane 1-monooxygenase, belong here.
REFERENCE   1  [PMID:13426111]
  AUTHORS   BOOTH J, BOYLAND E.
  TITLE     The biochemistry of aromatic amines.  III.  Enzymic hydroxylation by
            rat-liver microsomes.
  JOURNAL   Biochem. J. 66 (1957) 73-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:5132997]
  AUTHORS   Fujita T, Mannering GJ.
  TITLE     Differences in soluble P-450 hemoproteins from livers of rats
            treated with phenobarbital and 3-methylcholanthrene.
  JOURNAL   Chem. Biol. Interact. 3 (1971) 264-5.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:187601]
  AUTHORS   Haugen DA, Coon MJ.
  TITLE     Properties of electrophoretically homogeneous
            phenobarbital-inducible and beta-naphthoflavone-inducible forms of
            liver microsomal cytochrome P-450.
  JOURNAL   J. Biol. Chem. 251 (1976) 7929-39.
  ORGANISM  rabbit
REFERENCE   4  [PMID:3415241]
  AUTHORS   Imaoka S, Inoue K, Funae Y.
  TITLE     Aminopyrine metabolism by multiple forms of cytochrome P-450 from
            rat liver microsomes: simultaneous quantitation of four aminopyrine
            metabolites by high-performance liquid chromatography.
  JOURNAL   Arch. Biochem. Biophys. 265 (1988) 159-70.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:434823]
  AUTHORS   Johnson EF, Zounes MC, Muller-Eberhard U.
  TITLE     Characterization of three forms of rabbit microsomal cytochrome
            P-450 by peptide mapping utilizing limited proteolysis in sodium
            dodecyl sulfate and analysis by gel electrophoresis.
  JOURNAL   Arch. Biochem. Biophys. 192 (1979) 282-9.
  ORGANISM  rabbit
REFERENCE   6  [PMID:489601]
  AUTHORS   Kupfer D, Miranda GK, Navarro J, Piccolo DE, Theoharides AD.
  TITLE     Effect of inducers and inhibitors of monooxygenase on the
            hydroxylation of prostaglandins in the guinea pig. Evidence for
            several monooxygenases catalyzing omega- and omega-1-hydroxylation.
  JOURNAL   J. Biol. Chem. 254 (1979) 10405-14.
  ORGANISM  guinea pig
REFERENCE   7  [PMID:7298645]
  AUTHORS   Lang MA, Gielen JE, Nebert DW.
  TITLE     Genetic evidence for many unique liver microsomal P-450-mediated
            monooxygenase activities in heterogeneic stock mice.
  JOURNAL   J. Biol. Chem. 256 (1981) 12068-75.
  ORGANISM  mouse [GN:mmu]
REFERENCE   8  [PMID:7298644]
  AUTHORS   Lang MA, Nebert DW.
  TITLE     Structural gene products of the Ah locus. Evidence for many unique
            P-450-mediated monooxygenase activities reconstituted from
            3-methylcholanthrene-treated C57BL/6N mouse liver microsomes.
  JOURNAL   J. Biol. Chem. 256 (1981) 12058-67.
REFERENCE   9  [PMID:2916844]
  AUTHORS   Leo MA, Lasker JM, Raucy JL, Kim CI, Black M, Lieber CS.
  TITLE     Metabolism of retinol and retinoic acid by human liver cytochrome
            P450IIC8.
  JOURNAL   Arch. Biochem. Biophys. 269 (1989) 305-12.
  ORGANISM  human [GN:hsa]
REFERENCE   10 [PMID:4401153]
  AUTHORS   Lu AY, Kuntzman R, West S, Jacobson M, Conney AH.
  TITLE     Reconstituted liver microsomal enzyme system that hydroxylates
            drugs, other foreign compounds, and endogenous substrates. II. Role
            of the cytochrome P-450 and P-448 fractions in drug and steroid
            hydroxylations.
  JOURNAL   J. Biol. Chem. 247 (1972) 1727-34.
  ORGANISM  rat [GN:rno]
REFERENCE   11 [PMID:13314626]
  AUTHORS   MITOMA C, POSNER HS, REITZ HC, UDENFRIEND S.
  TITLE     Enzymatic hydroxylation of aromatic compounds.
  JOURNAL   Arch. Biochem. Biophys. 61 (1956) 431-41.
  ORGANISM  rabbit
REFERENCE   12
  AUTHORS   Mitoma, C. and Udenfriend, S.
  TITLE     Aryl-4-hydroxylase.
  JOURNAL   Methods Enzymol. 5 (1962) 816-819.
REFERENCE   13 [PMID:7295706]
  AUTHORS   Napoli JL, Okita RT, Masters BS, Horst RL.
  TITLE     Identification of 25,26-dihydroxyvitamin D3 as a rat renal
            25-hydroxyvitamin D3 metabolite.
  JOURNAL   Biochemistry. 20 (1981) 5865-71.
  ORGANISM  rat [GN:rno]
REFERENCE   14 [PMID:4387094]
  AUTHORS   Nebert DW, Gelboin HV.
  TITLE     Substrate-inducible microsomal aryl hydroxylase in mammalian cell
            culture. I. Assay and properties of induced enzyme.
  JOURNAL   J. Biol. Chem. 243 (1968) 6242-9.
  ORGANISM  rat [GN:rno]
REFERENCE   15 [PMID:3264134]
  AUTHORS   Suhara K, Ohashi K, Takahashi K, Katagiri M.
  TITLE     Aromatase and nonaromatizing 10-demethylase activity of adrenal
            cortex mitochondrial P-450(11)beta.
  JOURNAL   Arch. Biochem. Biophys. 267 (1988) 31-7.
  ORGANISM  cow [GN:bta], human [GN:hsa]
REFERENCE   16 [PMID:7462235]
  AUTHORS   Theoharides AD, Kupfer D.
  TITLE     Evidence for different hepatic microsomal monooxygenases catalyzing
            omega- and (omega-1)-hydroxylations of prostaglandins E1 and E2.
            Effects of inducers of monooxygenase on the kinetic constants of
            prostaglandin hydroxylation.
  JOURNAL   J. Biol. Chem. 256 (1981) 2168-75.
  ORGANISM  rabbit
REFERENCE   17 [PMID:825720]
  AUTHORS   Thomas PE, Lu AY, Ryan D, West SB, Kawalek J, Levin W.
  TITLE     Immunochemical evidence for six forms of rat liver cytochrome P450
            obtained using antibodies against purified rat liver cytochromes
            P450 and P448.
  JOURNAL   Mol. Pharmacol. 12 (1976) 746-58.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00071  Fatty acid metabolism
            PATH: map00150  Androgen and estrogen metabolism
            PATH: map00232  Caffeine metabolism
            PATH: map00361  gamma-Hexachlorocyclohexane degradation
            PATH: map00380  Tryptophan metabolism
            PATH: map00590  Arachidonic acid metabolism
            PATH: map00591  Linoleic acid metabolism
            PATH: map00980  Metabolism of xenobiotics by cytochrome P450
ORTHOLOGY   KO: K00493  unspecific monooxygenase
            KO: K07408  cytochrome P450, family 1, subfamily A, polypeptide 1
            KO: K07409  cytochrome P450, family 1, subfamily A, polypeptide 2
            KO: K07410  cytochrome P450, family 1, subfamily B, polypeptide 1
            KO: K07411  cytochrome P450, family 2, subfamily A
            KO: K07412  cytochrome P450, family 2, subfamily B
            KO: K07413  cytochrome P450, family 2, subfamily C
            KO: K07414  cytochrome P450, family 2, subfamily D
            KO: K07415  cytochrome P450, family 2, subfamily E
            KO: K07416  cytochrome P450, family 2, subfamily F
            KO: K07418  cytochrome P450, family 2, subfamily J
            KO: K07420  cytochrome P450, family 2, subfamily S
            KO: K07424  cytochrome P450, family 3, subfamily A
            KO: K07426  cytochrome P450, family 4, subfamily B
            KO: K07428  cytochrome P450, family 4, subfamily X
            KO: K07429  cytochrome P450, family 4, subfamily Z
            KO: K07434  cytochrome P450, family 19, subfamily A
GENES       HSA: 11283(CYP4F8) 1543(CYP1A1) 1544(CYP1A2) 1545(CYP1B1)
                 1548(CYP2A6) 1549(CYP2A7) 1551(CYP3A7) 1553(CYP2A13)
                 1555(CYP2B6) 1558(CYP2C8) 1559(CYP2C9) 1562(CYP2C18)
                 1565(CYP2D6) 1571(CYP2E1) 1572(CYP2F1) 1573(CYP2J2)
                 1576(CYP3A4) 1577(CYP3A5) 1580(CYP4B1) 1588(CYP19A1)
                 199974(CYP4Z1) 260293(CYP4X1) 29785(CYP2S1) 57834(CYP4F11)
                 64816(CYP3A43) 66002(CYP4F12)
            PTR: 450857(LOC450857) 450909(CYP2C8) 470228(CYP2D6)
                 472456(LOC472456)
            MCC: 678694(CYP1A1)
            MMU: 107141(Cyp2c50) 13075(Cyp19a1) 13076(Cyp1a1) 13077(Cyp1a2)
                 13078(Cyp1b1) 13085(Cyp2a12) 13086(Cyp2a4) 13087(Cyp2a5)
                 13088(Cyp2b10) 13089(Cyp2b13) 13090(Cyp2b19) 13094(Cyp2b9)
                 13095(Cyp2c29) 13096(Cyp2c37) 13097(Cyp2c38) 13098(Cyp2c39)
                 13099(Cyp2c40) 13101(Cyp2d10) 13105(Cyp2d9) 13106(Cyp2e1)
                 13107(Cyp2f2) 13108(Cyp2g1) 13109(Cyp2j5) 13110(Cyp2j6)
                 13112(Cyp3a11) 13113(Cyp3a13) 13114(Cyp3a16) 13120(Cyp4b1)
                 226105(Cyp2c70) 226143(Cyp2c44) 337924(Cyp3a44)
                 404195(Cyp2c54) 53973(Cyp3a41a) 56388(Cyp3a25) 56448(Cyp2d22)
                 69888(Cyp2c66) 72082(Cyp2c55) 72303(Cyp2c65) 74134(Cyp2s1)
                 74519(Cyp2j9) 76279(Cyp2d26) 81906(Cyp4x1)
            RNO: 171352(Cyp3a9) 171518(Cyp2c22) 171521(Cyp2c13)
                 171522(Cyp2d4v1) 24296(Cyp1a1) 24297(Cyp1a2) 24299(Cyp2a3a)
                 24303(Cyp2d3) 24307(Cyp4b1) 246070(Cyp2c6) 246767(Cyp4x1)
                 24894(Cyp2a1) 24895(Cyp2a2) 25011(Cyp2c12) 25053(Cyp2d2)
                 25086(Cyp2e1) 25251(Cyp2g1) 252931(Cyp3a18) 25426(Cyp1b1)
                 25642(Cyp3a23/3a1) 266682(Cyp3a2) 266684(Cyp2d1)
                 286929(Cyp3a1) 286953(Cyp2b3) 286963(Cyp2d5) 292728(Cyp2b21)
                 29295(Cyp2b15) 29298(Cyp2c7) 313375(Cyp2j3) 54246(Cyp2f4)
                 65210(Cyp2j4) 83790(Cyp2c23)
            CFA: 415120(CYP2D15) 415123(CYP2C41) 415128(CYP2E1)
                 474177(CYPIIB11) 479740(LOC479740) 482505(LOC482505)
                 483038(LOC483038) 484491(LOC484491) 484494(CYP2A13)
                 494003(CYP19) 494010(CYP1A2) 608452(LOC608452)
                 610195(LOC610195) 612477(LOC612477)
            BTA: 281740(CYP19) 282211(CYP2D6) 282213(CYP2E1) 282214(CYP3A4)
                 282870(CYP1A1) 507988(CYP3A4)
            SSC: 397687(CYP2D25) 403103(CYP1A1) 403104(CYP2B22)
                 403107(CYP2C33) 403149(CYP2A19) 403215(CYP2C49) 403216(CYP2E1)
                 403322(CYP3A39) 403324(CYP3A29) 403331(CYP19A1)
                 403333(CYP19A3)
            GGA: 396051(CYP1A1) 414832(CYP3A37) 414833(CYP2C45)
                 414854(CYP19A1) 416477(CYP3A80) 417981(LOC417981)
                 424676(LOC424676) 428832(LOC428832)
            XLA: 373656(p450arom-A) 379297(MGC54008) 379479(cyp2d6-b)
                 398964(MGC68821) 432343(MGC82323) 432347(MGC82264)
                 444542(MGC82129) 446878(cyp2d6-a) 495363(LOC495363)
            XTR: 448236(cyp2c8) 496407(CYP2A13) 496408(Cyp2f2)
                 548503(MGC108372)
            DRE: 140634(cyp1a) 30381(cyp26a1) 30390(cyp19a1a) 60640(cyp19a1b)
                 641501(zgc:123110)
            SPU: 576811(LOC576811) 578655(LOC578655) 581116(LOC581116)
            DME: Dmel_CG11466
            CEL: C49C8.4(cyp-33E1) F42A9.5(cyp-33E2) R08F11.3(cyp-33C8)
                 Y49C4A.9(cyp-33C11)
            OSA: 4341117 4341526 4341631
            SCE: YDR402C(DIT2)
            AGO: AGOS_AFR400C
            PIC: PICST_35590(ALK2) PICST_63000(CYP559)
            CGR: CAGL0F02607g
            ANI: AN2706.2 AN6835.2
            AFM: AFUA_1G04390 AFUA_3G09220 AFUA_5G02620 AFUA_7G00290
            AOR: AO090001000445 AO090005000553 AO090701000436
            UMA: UM06459.1
            TET: TTHERM_00101170 TTHERM_00101290 TTHERM_00112850
                 TTHERM_00185610 TTHERM_00198200 TTHERM_00198220
                 TTHERM_00198230 TTHERM_00198340 TTHERM_00200550
                 TTHERM_00201630 TTHERM_00227020 TTHERM_00313500
                 TTHERM_00395750 TTHERM_00620930 TTHERM_00754700
                 TTHERM_00754730 TTHERM_00898320 TTHERM_01122770
                 TTHERM_01122780 TTHERM_01250020 TTHERM_01280630
                 TTHERM_01369770 TTHERM_01698320
            PEN: PSEEN2155
            FTU: FTT0632c
            FTF: FTF0632c
            REH: H16_B0939(cyp) H16_B1009
            RME: Rmet_3467
            BUR: Bcep18194_B0775 Bcep18194_B1689 Bcep18194_C6803
            MLO: mll8468
            SME: SMc01812
            ATU: Atu1256
            ATC: AGR_C_2319
            RET: RHE_CH01585
            RLE: RL1686
            BJA: blr2882
            BRA: BRADO0283
            BBT: BBta_0276
            RPD: RPD_1820
            RPE: RPE_0057
            SIT: TM1040_1816
            RSP: RSP_1946
            RDE: RD1_2962(cyp)
            ELI: ELI_00100
            BSU: BG12299(yrhJ) BG12871(yetO)
            BAN: BA3221(cypD)
            BAR: GBAA3221(cypD)
            BAT: BAS2993
            BCE: BC3211
            BCA: BCE_3239(cypD)
            BCZ: BCZK2921
            BTK: BT9727_2981
            BLI: BL02398(cypE)
            BLD: BLi02848(yrhJ)
            SCO: SCO3636(SCH10.14c)
            SMA: SAV4539(cyp20)
            FAL: FRAAL1514 FRAAL5644
            SEN: SACE_0125(cyp20) SACE_2802 SACE_4144 SACE_4205(cypD)
                 SACE_5309(cyp20)
            AVA: Ava_1981 Ava_2103 Ava_3921 Ava_4063
            DGE: Dgeo_0944
            HMA: rrnAC0073(cyc) rrnAC3312(cyp1)
            HWA: HQ3721A(cyc)
            NPH: NP2540A(cyc)
            PTO: PTO0085 PTO1399
STRUCTURES  PDB: 1BU7  1BVY  1DT6  1FAG  1FAH  1JME  1JPZ  1N6B  1NR6  1OG2  
                 1OG5  1P0V  1P0W  1P0X  1PO5  1PQ2  1R9O  1SMI  1SMJ  1SUO  
                 1TQN  1W0E  1W0F  1W0G  1YQO  1YQP  1Z10  1Z11  1ZO4  1ZO9  
                 1ZOA  2BDM  2BMH  2F9Q  2FDU  2FDV  2FDW  2FDY  2HI4  2HPD  
                 2IJ2  2IJ3  2IJ4  2J0D  2J1M  2J4S  2NNB  2P85  2PG5  2PG6  
                 2PG7  2UWH  2V0M  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.14.1
            ExPASy - ENZYME nomenclature database: 1.14.14.1
            ExplorEnz - The Enzyme Database: 1.14.14.1
            ERGO genome analysis and discovery system: 1.14.14.1
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.14.1
            BRENDA, the Enzyme Database: 1.14.14.1
            CAS: 62213-32-5
///
ENTRY       EC 1.14.14.2      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced flavin or flavoprotein as one donor, and incorporation
            of one atom of oxygen into the other donor
COMMENT     Deleted entry: benzopyrene 3-monooxygenase. Now included with EC
            1.14.14.1 unspecific monooxygenase (EC 1.14.14.2 created 1972,
            deleted 1976)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.14.2
            ExPASy - ENZYME nomenclature database: 1.14.14.2
            ExplorEnz - The Enzyme Database: 1.14.14.2
            ERGO genome analysis and discovery system: 1.14.14.2
            BRENDA, the Enzyme Database: 1.14.14.2
///
ENTRY       EC 1.14.14.3                Enzyme
NAME        alkanal monooxygenase (FMN-linked);
            bacterial luciferase;
            aldehyde monooxygenase;
            luciferase;
            Vibrio fischeri luciferase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced flavin or flavoprotein as one donor, and incorporation
            of one atom of oxygen into the other donor
SYSNAME     alkanal,reduced-FMN:oxygen oxidoreductase (1-hydroxylating,
            luminescing)
REACTION    RCHO + reduced FMN + O2 = RCOOH + FMN + H2O + hnu [RN:R03536]
ALL_REAC    R03536
SUBSTRATE   RCHO [CPD:C00071];
            reduced FMN [CPD:C01847];
            O2 [CPD:C00007]
PRODUCT     RCOOH;
            FMN [CPD:C00061];
            H2O [CPD:C00001];
            hn [CPD:C00205]
COMMENT     The reaction sequence involves incorporation of a molecule of oxygen
            into reduced FMN, and subsequent reaction with the aldehyde to form
            an activated FMN.H2O complex, which breaks down with emission of
            light. The enzyme is highly specific for reduced FMN, and for
            long-chain aliphatic aldehydes with eight carbons or more.
REFERENCE   1  [PMID:363350]
  AUTHORS   Hastings JW.
  TITLE     Bacterial bioluminescence light emission in the mixed function
            oxidation of reduced flavin and fatty aldehyde.
  JOURNAL   CRC. Crit. Rev. Biochem. 5 (1978) 163-84.
REFERENCE   2  [PMID:199107]
  AUTHORS   Hastings JW, Nealson KH.
  TITLE     Bacterial bioluminescence.
  JOURNAL   Annu. Rev. Microbiol. 31 (1977) 549-95.
REFERENCE   3  [PMID:309549]
  AUTHORS   Hastings JW, Presswood RP.
  TITLE     Bacterial luciferase: FMNH2-aldehyde oxidase.
  JOURNAL   Methods. Enzymol. 53 (1978) 558-70.
REFERENCE   4  [PMID:396467]
  AUTHORS   Nealson KH, Hastings JW.
  TITLE     Bacterial bioluminescence: its control and ecological significance.
  JOURNAL   Microbiol. Rev. 43 (1979) 496-518.
  ORGANISM  Vibrio harveyi, Beneckea splendida, Photobacterium fischeri,
            Photobacterium phosphoreum, Photobacterium leiognathi, Vibrio
            cholerae [GN:vch], Vibrio albensis, Xenorhabdus luminescencens
REFERENCE   5
  AUTHORS   Suzuki, K., Kaidoh, T., Katagiri, M. and Tsuchiya, T.
  TITLE     O2 incorporation into a long-chain fatty-acid during bacterial
            luminescence.
  JOURNAL   Biochim. Biophys. Acta 722 (1983) 297-301.
  ORGANISM  Photobacterium phosphoreum
ORTHOLOGY   KO: K00494  alkanal monooxygenase (FMN-linked)
GENES       PLU: plu2081(luxA) plu2082(luxB)
            XCC: XCC1686
            XCB: XC_2545
            XCV: XCV1740
            XAC: XAC1706
            XOO: XOO2979
            XOM: XOO_2829(XOO2829)
            VFI: VFA0920 VFA0921
            PSP: PSPPH_0041 PSPPH_2911
            PEN: PSEEN0043
            ACI: ACIAD1830
            SHN: Shewana3_3090
            PHA: PSHAb0540(yhbW)
            RSO: RS03171(RSp1227)
            REU: Reut_C5909
            RME: Rmet_5936
            BMA: BMA0580
            BXE: Bxe_A2932 Bxe_C0953
            BUR: Bcep18194_B1412 Bcep18194_C6860
            BAM: Bamb_1048
            BPS: BPSL2400
            BPM: BURPS1710b_2861(amo)
            BTE: BTH_I1765
            RFR: Rfer_3316
            MFA: Mfla_1789
            BBA: Bd2074(yvbT)
            MXA: MXAN_5094
            PLA: Plav_1774 Plav_1793
            RET: RHE_CH02675
            RLE: RL3141 RL3561 RL3984 pRL100245
            BME: BMEI0017 BMEI0894
            BMF: BAB1_1111 BAB1_2052
            BRA: BRADO0667
            BBT: BBta_7516
            RPE: RPE_3771
            NWI: Nwi_2071
            HNE: HNE_1382
            SWI: Swit_4156
            RRU: Rru_A0927
            BCZ: BCZK3086
            BTK: BT9727_3167
            SHA: SH0481
            MSM: MSMEG_5029
            CGL: NCgl2041(cgl2122) NCgl2137(cgl2218) NCgl2229(cgl2311)
            CGB: cg2538 cg3085 cg3256
            FRA: Francci3_0352 Francci3_4140
            FAL: FRAAL0233 FRAAL3343 FRAAL4266 FRAAL4834
            SEN: SACE_1310(amo)
            STP: Strop_2849
            AVA: Ava_0457
            HMA: pNG7033(yvbT) pNG7296(mox)
STRUCTURES  PDB: 1BRL  1BSL  1LUC  1XKJ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.14.3
            ExPASy - ENZYME nomenclature database: 1.14.14.3
            ExplorEnz - The Enzyme Database: 1.14.14.3
            ERGO genome analysis and discovery system: 1.14.14.3
            BRENDA, the Enzyme Database: 1.14.14.3
            CAS: 9014-00-0
///
ENTRY       EC 1.14.14.4      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced flavin or flavoprotein as one donor, and incorporation
            of one atom of oxygen into the other donor
COMMENT     Deleted entry: choline monooxygenase. Identical to EC 1.14.15.7 (EC
            1.14.14.4 created 2000, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.14.4
            ExPASy - ENZYME nomenclature database: 1.14.14.4
            ExplorEnz - The Enzyme Database: 1.14.14.4
            ERGO genome analysis and discovery system: 1.14.14.4
            BRENDA, the Enzyme Database: 1.14.14.4
///
ENTRY       EC 1.14.14.5                Enzyme
NAME        alkanesulfonate monooxygenase;
            SsuD;
            sulfate starvation-induced protein 6
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced flavin or flavoprotein as one donor, and incorporation
            of one atom of oxygen into the other donor
SYSNAME     alkanesulfonate, reduced-FMN:oxygen oxidoreductase
REACTION    an alkanesufonate (R-CH2-SO3H) + FMNH2 + O2 = an aldehyde (R-CHO) +
            FMN + sulfite + H2O [RN:R07210]
ALL_REAC    R07210
SUBSTRATE   alkanesufonate (R-CH2-SO3H);
            FMNH2 [CPD:C01847];
            O2 [CPD:C00007]
PRODUCT     aldehyde [CPD:C00071];
            FMN [CPD:C00061];
            sulfite [CPD:C00094];
            H2O [CPD:C00001]
COMMENT     The enzyme from Escherichia coli catalyses the desulfonation of a
            wide range of aliphatic sulfonates (unsubstituted C1- to
            C14-sulfonates as well as substituted C2-sulfonates). Does not
            desulfonate taurine (2-aminoethanesulfonate) or aromatic sulfonates.
            Does not use FMN as a bound cofactor. Instead, it uses reduced FMN
            (i.e., FMNH2) as a substrate. FMNH2 is provided by SsuE, the
            associated FMN reductase (EC 1.5.1.29).
REFERENCE   1  [PMID:10480865]
  AUTHORS   Eichhorn E, van der Ploeg JR, Leisinger T.
  TITLE     Characterization of a two-component alkanesulfonate monooxygenase
            from Escherichia coli.
  JOURNAL   J. Biol. Chem. 274 (1999) 26639-46.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K04091  alkanesulfonate monooxygenase
GENES       PIC: PICST_36305
            ANI: AN9191.2
            AOR: AO090010000129
            ECO: b0935(ssuD)
            ECJ: JW0918(ssuD)
            ECE: Z1283(ycbN)
            ECS: ECs1018
            ECC: c1078(ycbN)
            ECI: UTI89_C1007(ycbN)
            ECP: ECP_0947
            ECV: APECO1_47(ssuD)
            ECW: EcE24377A_1037(ssuD)
            ECX: EcHS_A1044(ssuD)
            YPE: YPO3625(ssuD)
            YPK: y0244
            YPM: YP_3922(ssuD)
            YPA: YPA_3638
            YPN: YPN_3545
            YPP: YPDSF_0232
            YPS: YPTB3604(ssuD)
            YPI: YpsIP31758_0354(ssuD)
            SFL: SF0934(ycbN)
            SFX: S0999(ycbN)
            SFV: SFV_0939(ycbN)
            SDY: SDY_2321 SDY_2322
            ECA: ECA4411(ssuD)
            SPE: Spro_1737
            XAC: XAC0850(ssuD)
            PAE: PA2356(msuD) PA3444
            PAU: PA14_12710 PA14_19560(ssuD) PA14_34190(msuD)
            PPU: PP_0238(ssuD)
            PPF: Pput_0253
            PST: PSPTO_2590 PSPTO_3466(ssuD)
            PSB: Psyr_2280 Psyr_3247
            PSP: PSPPH_2909 PSPPH_3167 PSPPH_3610
            PFL: PFL_3165 PFL_3172 PFL_4156(msuD) PFL_5936(ssuD)
            PFO: Pfl_3916 Pfl_5413
            PEN: PSEEN0201 PSEEN0219(ssuD) PSEEN3421 PSEEN3428
            PMY: Pmen_4322
            ACI: ACIAD0036(ssuD) ACIAD1505 ACIAD1527
            RSO: RSc1339(ssuD)
            REU: Reut_A1976 Reut_B5047
            REH: H16_A2244(ssuD1) H16_B1865(ssuD2)
            RME: Rmet_1371 Rmet_2218
            BMA: BMA1239(ssuD)
            BMV: BMASAVP1_A1725(ssuD)
            BML: BMA10299_A0382(ssuD)
            BMN: BMA10247_0779(ssuD)
            BXE: Bxe_A2493 Bxe_B1542
            BVI: Bcep1808_1526 Bcep1808_4824 Bcep1808_4937
            BUR: Bcep18194_A4704 Bcep18194_B0310 Bcep18194_B1529
                 Bcep18194_B1532 Bcep18194_B1755 Bcep18194_B2607
                 Bcep18194_C7083 Bcep18194_C7501 Bcep18194_C7713
            BCN: Bcen_1082 Bcen_3933 Bcen_4110
            BCH: Bcen2424_1562 Bcen2424_3531 Bcen2424_4256 Bcen2424_4433
                 Bcen2424_6154
            BAM: Bamb_1463 Bamb_3680 Bamb_3865
            BPS: BPSL1858(ssuD)
            BPM: BURPS1710b_1989(ssuD) BURPS1710b_A2187
            BPL: BURPS1106A_1836(msuD)
            BPD: BURPS668_1821(msuD)
            BTE: BTH_I2501 BTH_II1790(msuD)
            RFR: Rfer_1777
            PNA: Pnap_0560 Pnap_2418
            AAV: Aave_3044
            MPT: Mpe_A0115(ssuD)
            MMS: mma_0740(ssuD1) mma_1022(ssuD2)
            MFA: Mfla_1534 Mfla_1535
            MLO: mll4558 mlr5216
            ATU: Atu3426(ssuD)
            ATC: AGR_L_2796
            RET: RHE_CH02432(ssuD) RHE_PB00119(ntaA) RHE_PB00125 RHE_PC00151
            RLE: RL2769(ssuD) pRL100402 pRL90242 pRL90248 pRL90300
            BJA: bll7010(ssuD) blr7602
            BRA: BRADO3405 BRADO4269(ssuD) BRADO4361(ssuD) BRADO4512(ntaA)
                 BRADO4866 BRADO5912(ssuD)
            BBT: BBta_1866(ssuD) BBta_1980 BBta_2538(ssuD) BBta_2573
                 BBta_2574(ssuD) BBta_3195 BBta_3300(ssuD) BBta_3308(ssuD)
                 BBta_4299 BBta_4737(ntaA) BBta_4800 BBta_4860
            RPA: RPA2612(msuD)
            RPE: RPE_3193
            NWI: Nwi_0682
            XAU: Xaut_1213 Xaut_3456 Xaut_3463
            SIT: TM1040_3362
            JAN: Jann_1941
            RDE: RD1_2310(ssuD)
            PDE: Pden_5013
            NAR: Saro_2443
            SAL: Sala_1660
            SWI: Swit_2509
            GBE: GbCGDNIH1_0256 GbCGDNIH1_0643 GbCGDNIH1_2420
            BSU: BG10658(ssuD)
            BAN: BA2919(ssuD)
            BAR: GBAA2919(ssuD)
            BAA: BA_3427
            BAT: BAS2711
            BCE: BC2909
            BCA: BCE_2958(ssuD)
            BCZ: BCZK2639(ssuD)
            BCY: Bcer98_1997
            BTK: BT9727_2662(ssuD)
            BLI: BL03203(ssuDB) BL05083(ssuDA)
            BLD: BLi00944(ssuD)
            BCL: ABC0599(ssuD) ABC3395
            MSM: MSMEG_2651 MSMEG_4103 MSMEG_4539
            MVA: Mvan_1200 Mvan_4860
            MGI: Mflv_5136
            MMC: Mmcs_0890 Mmcs_3498 Mmcs_4323
            MKM: Mkms_0907 Mkms_3571 Mkms_4409
            MJL: Mjls_0896 Mjls_3511 Mjls_4703
            NFA: nfa11540
            RHA: RHA1_ro00592 RHA1_ro00619 RHA1_ro01768 RHA1_ro02416
                 RHA1_ro02420 RHA1_ro04019 RHA1_ro07050(ssuD1)
                 RHA1_ro07051(ssuD2)
            SMA: SAV1561(ssuD2)
            ART: Arth_0532
            TFU: Tfu_1497 Tfu_1500 Tfu_1502
            FAL: FRAAL3305 FRAAL3541 FRAAL3868 FRAAL4432(ssuD) FRAAL4830(ssuD)
            KRA: Krad_3993
            SEN: SACE_1633 SACE_4062(msuD) SACE_4878
            STP: Strop_2833
            RXY: Rxyl_1777
            AVA: Ava_0105 Ava_0106 Ava_1266 Ava_4142 Ava_4330 Ava_5016
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.14.5
            ExPASy - ENZYME nomenclature database: 1.14.14.5
            ExplorEnz - The Enzyme Database: 1.14.14.5
            ERGO genome analysis and discovery system: 1.14.14.5
            BRENDA, the Enzyme Database: 1.14.14.5
            CAS: 256383-67-2
///
ENTRY       EC 1.14.15.1                Enzyme
NAME        camphor 5-monooxygenase;
            camphor 5-exo-methylene hydroxylase;
            2-bornanone 5-exo-hydroxylase;
            bornanone 5-exo-hydroxylase;
            camphor 5-exo-hydroxylase;
            camphor 5-exohydroxylase;
            camphor hydroxylase;
            d-camphor monooxygenase;
            methylene hydroxylase;
            methylene monooxygenase;
            D-camphor-exo-hydroxylase;
            camphor methylene hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced iron-sulfur protein as one donor, and incorporation of
            one atom of oxygen into the other donor
SYSNAME     (+)-camphor,reduced putidaredoxin:oxygen oxidoreductase
            (5-hydroxylating)
REACTION    (+)-camphor + putidaredoxin + O2 = (+)-exo-5-hydroxycamphor +
            oxidized putidaredoxin + H2O [RN:R03818]
ALL_REAC    R03818
SUBSTRATE   (+)-camphor [CPD:C00808];
            putidaredoxin [CPD:C02069];
            O2 [CPD:C00007]
PRODUCT     (+)-exo-5-hydroxycamphor [CPD:C03448];
            oxidized putidaredoxin [CPD:C03302];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A heme-thiolate protein (P-450). Also acts on (-)-camphor and
            1,2-campholide, forming 5-exo-hydroxy-1,2-campholide.
REFERENCE   1  [PMID:4378858]
  AUTHORS   Hedegaard J, Gunsalus IC.
  TITLE     Mixed function oxidation. IV. An induced methylene hydroxylase in
            camphor oxidation.
  JOURNAL   J. Biol. Chem. 240 (1965) 4038-43.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2  [PMID:4341491]
  AUTHORS   Tyson CA, Lipscomb JD, Gunsalus IC.
  TITLE     The role of putidaredoxin and P450 cam  in methylene hydroxylation.
  JOURNAL   J. Biol. Chem. 247 (1972) 5777-84.
  ORGANISM  Pseudomonas putida [GN:ppu]
GENES       NWI: Nwi_2279
            FAL: FRAAL3826 FRAAL4113 FRAAL5490
STRUCTURES  PDB: 1AKD  1C8J  1CP4  1GEB  1GEK  1GEM  1GJM  1IWI  1IWJ  1IWK  
                 1J51  1K2O  1LWL  1MPW  1NOO  1O76  1P2Y  1P7R  1PHA  1PHB  
                 1PHC  1PHD  1PHE  1PHF  1PHG  1QMQ  1RE9  1RF9  1T85  1T86  
                 1T87  1T88  1YRC  1YRD  2A1M  2A1N  2A1O  2CP4  2CPP  2FE6  
                 2FER  2FEU  2FRZ  2GQX  2GR6  2H7Q  2H7R  2H7S  3CP4  3CPP  
                 4CP4  4CPP  5CP4  5CPP  6CP4  6CPP  7CPP  8CPP  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.15.1
            ExPASy - ENZYME nomenclature database: 1.14.15.1
            ExplorEnz - The Enzyme Database: 1.14.15.1
            ERGO genome analysis and discovery system: 1.14.15.1
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.15.1
            BRENDA, the Enzyme Database: 1.14.15.1
            CAS: 9030-82-4
///
ENTRY       EC 1.14.15.2                Enzyme
NAME        camphor 1,2-monooxygenase;
            2,5-diketocamphane lactonizing enzyme;
            camphor ketolactonase I;
            oxygenase, camphor 1,2-mono;
            ketolactonase I
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced iron-sulfur protein as one donor, and incorporation of
            one atom of oxygen into the other donor
SYSNAME     (+)-camphor,reduced-rubredoxin:oxygen oxidoreductase
            (1,2-lactonizing)
REACTION    (+)-bornane-2,5-dione + reduced rubredoxin + O2 =
            5-oxo-1,2-campholide + oxidized rubredoxin + H2O [RN:R04102]
ALL_REAC    R04102
SUBSTRATE   (+)-bornane-2,5-dione [CPD:C03037];
            reduced rubredoxin [CPD:C00340];
            O2 [CPD:C00007]
PRODUCT     5-oxo-1,2-campholide [CPD:C02952];
            oxidized rubredoxin [CPD:C00435];
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+.
REFERENCE   1  [PMID:14253460]
  AUTHORS   CONRAD HE, DUBUS R, NAMTVEDT MJ, GUNSALUS IC.
  TITLE     MIXED FUNCTION OXIDATION. II. SEPARATION AND PROPERTIES OF THE
            ENZYMES CATALYZING CAMPHOR LACTONIZATION.
  JOURNAL   J. Biol. Chem. 240 (1965) 495-503.
  ORGANISM  Corynebacterium sp.
REFERENCE   2  [PMID:4288652]
  AUTHORS   Trudgill PW, DuBus R, Gunsalus IC.
  TITLE     Mixed function oxidation. VI. Purification of a tightly coupled
            electron transport complex in camphor lactonization.
  JOURNAL   J. Biol. Chem. 241 (1966) 4288-90.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   3  [PMID:4310834]
  AUTHORS   Yu CA, Gunsalus IC.
  TITLE     Monoxygenases. VII. Camphor ketolactonase I and the role of three
            protein components.
  JOURNAL   J. Biol. Chem. 244 (1969) 6149-52.
  ORGANISM  Pseudomonas putida [GN:ppu]
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.15.2
            ExPASy - ENZYME nomenclature database: 1.14.15.2
            ExplorEnz - The Enzyme Database: 1.14.15.2
            ERGO genome analysis and discovery system: 1.14.15.2
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.15.2
            BRENDA, the Enzyme Database: 1.14.15.2
            CAS: 37256-81-8
///
ENTRY       EC 1.14.15.3                Enzyme
NAME        alkane 1-monooxygenase;
            alkane 1-hydroxylase;
            omega-hydroxylase;
            fatty acid omega-hydroxylase;
            alkane monooxygenase;
            1-hydroxylase;
            alkane hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced iron-sulfur protein as one donor, and incorporation of
            one atom of oxygen into the other donor
SYSNAME     alkane,reduced-rubredoxin:oxygen 1-oxidoreductase
REACTION    octane + reduced rubredoxin + O2 = 1-octanol + oxidized rubredoxin +
            H2O [RN:R02879]
ALL_REAC    R02879;
            (other) R01347 R01348 R02281 R07041
SUBSTRATE   octane [CPD:C01387];
            reduced rubredoxin [CPD:C00340];
            O2 [CPD:C00007]
PRODUCT     1-octanol [CPD:C00756];
            oxidized rubredoxin [CPD:C00435];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     Some enzymes in this group are heme-thiolate proteins (P-450). Also
            hydroxylates fatty acids in the omega-position.
REFERENCE   1  [PMID:4317878]
  AUTHORS   Cardini G, Jurtshuk P.
  TITLE     The enzymatic hydroxylation of n-octane by Corynebacterium sp.
            strain 7E1C.
  JOURNAL   J. Biol. Chem. 245 (1970) 2789-96.
REFERENCE   2  [PMID:4395379]
  AUTHORS   McKenna EJ, Coon MJ.
  TITLE     Enzymatic omega-oxidation. IV. Purification and properties of the
            omega-hydroxylase of Pseudomonas oleovorans.
  JOURNAL   J. Biol. Chem. 245 (1970) 3882-9.
REFERENCE   3  [PMID:4294330]
  AUTHORS   Peterson JA, Kusunose M, Kusunose E, Coon MJ.
  TITLE     Enzymatic omega-oxidation. II. Function of rubredoxin as the
            electron carrier in omega-hydroxylation.
  JOURNAL   J. Biol. Chem. 242 (1967) 4334-40.
PATHWAY     PATH: map00071  Fatty acid metabolism
            PATH: map00590  Arachidonic acid metabolism
            PATH: map03320  PPAR signaling pathway
ORTHOLOGY   KO: K00496  alkane 1-monooxygenase
            KO: K07425  cytochrome P450, family 4, subfamily A
GENES       HSA: 1579(CYP4A11) 284541(CYP4A22)
            MMU: 13117(Cyp4a10) 13118(Cyp4a12b) 13119(Cyp4a14)
            RNO: 170544(Cyp4a22) 266674(Cyp4a8) 298423(Cyp4a14) 50549(Cyp4a10)
            CFA: 475366(CYP4A38) 610385(CYP4A11)
            SSC: 403326(CYP4A24) 403327(CYP4A21)
            GGA: 424618(LOC424618)
            PAU: PA14_44700(alkB2)
            PFL: PFL_2935(alkB)
            PMY: Pmen_0443 Pmen_2750
            PRW: PsycPRwf_2053
            ACI: ACIAD1411(alkM)
            MAQ: Maqu_0440 Maqu_0610 Maqu_2843
            LPN: lpg2997
            LPF: lpl2925
            HCH: HCH_04734(alkB)
            ABO: ABO_0122(alkB2) ABO_2707(alkB1)
            BMA: BMA0635(alkB)
            BMV: BMASAVP1_A2377(alkB)
            BML: BMA10299_A2910(alkB)
            BMN: BMA10247_1692(alkB)
            BXE: Bxe_B1208
            BVI: Bcep1808_0897
            BUR: Bcep18194_A4085 Bcep18194_B1222
            BCN: Bcen_0501
            BCH: Bcen2424_0980
            BAM: Bamb_0841
            BPS: BPSL2350
            BPM: BURPS1710b_2801
            BPL: BURPS1106A_2735(alkB)
            BPD: BURPS668_2678(alkB)
            BTE: BTH_I1814
            MPT: Mpe_B0606(alkB)
            BBA: Bd2197
            SIT: TM1040_2646
            RSH: Rsph17029_0118
            RSQ: Rsph17025_0065
            JAN: Jann_0394
            PDE: Pden_2098
            ACR: Acry_1262
            MTU: Rv3252c(alkB)
            MTC: MT3350(alkB)
            MBO: Mb3280c(alkB)
            MBB: BCG_3281c(alkB)
            MPA: MAP3364c
            MSM: MSMEG_1839
            MVA: Mvan_1742 Mvan_3100
            MGI: Mflv_3369 Mflv_4721
            MMC: Mmcs_1333
            MKM: Mkms_1350
            MJL: Mjls_1369
            CJK: jk1916(alkM)
            NFA: nfa46180
            RHA: RHA1_ro02534(alkB) RHA1_ro02535(rubA) RHA1_ro02536(rubB)
            NCA: Noca_0122
            FRA: Francci3_1251
            FAL: FRAAL1986
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.15.3
            ExPASy - ENZYME nomenclature database: 1.14.15.3
            ExplorEnz - The Enzyme Database: 1.14.15.3
            ERGO genome analysis and discovery system: 1.14.15.3
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.15.3
            BRENDA, the Enzyme Database: 1.14.15.3
            CAS: 9059-16-9
///
ENTRY       EC 1.14.15.4                Enzyme
NAME        steroid 11beta-monooxygenase;
            steroid 11beta-hydroxylase;
            steroid 11beta/18-hydroxylase;
            oxygenase, steroid 11beta -mono-
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced iron-sulfur protein as one donor, and incorporation of
            one atom of oxygen into the other donor
SYSNAME     steroid,reduced-adrenal-ferredoxin:oxygen oxidoreductase
            (11beta-hydroxylating)
REACTION    a steroid + reduced adrenal ferredoxin + O2 = an
            11beta-hydroxysteroid + oxidized adrenal ferredoxin + H2O
            [RN:R02726]
ALL_REAC    R02726 > R02218 R02725 R02843 R03329 R03851 R04850
SUBSTRATE   steroid [CPD:C00377];
            reduced adrenal ferredoxin [CPD:C00662];
            O2 [CPD:C00007]
PRODUCT     11beta-hydroxysteroid [CPD:C01058];
            oxidized adrenal ferredoxin [CPD:C00667];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A heme-thiolate protein (P-450). Also hydroxylates steroids at the
            18-position, and converts 18-hydroxycorticosterone into aldosterone.
REFERENCE   1  [PMID:13276417]
  AUTHORS   GRANT JK, BROWNIE AC.
  TITLE     The role of fumarate and TPN in steroid enzymic
            11beta-hydroxylation.
  JOURNAL   Biochim. Biophys. Acta. 18 (1955) 433-4.
REFERENCE   2  [PMID:13211659]
  AUTHORS   HAYANO M, DORFMAN RI.
  TITLE     On the mechanism of the C11 beta-hydroxylation of steroids.
  JOURNAL   J. Biol. Chem. 211 (1954) 227-35.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:13426185]
  AUTHORS   TOMKINS GM, MICHAEL PJ, CURRAN JF.
  TITLE     Studies on the nature of steroid 11-beta hydroxylation.
  JOURNAL   Biochim. Biophys. Acta. 23 (1957) 655-6.
  ORGANISM  cow [GN:bta], rabbit
REFERENCE   4  [PMID:3485096]
  AUTHORS   Yanagibashi K, Haniu M, Shively JE, Shen WH, Hall P.
  TITLE     The synthesis of aldosterone by the adrenal cortex. Two zones
            (fasciculata and glomerulosa) possess one enzyme for 11 beta-,
            18-hydroxylation, and aldehyde synthesis.
  JOURNAL   J. Biol. Chem. 261 (1986) 3556-62.
  ORGANISM  cow [GN:bta], pig [GN:ssc]
REFERENCE   5  [PMID:4967077]
  AUTHORS   Zuidweg MH.
  TITLE     Hydroxylation of Reichstein's compound S with cell-free preparations
            from Curvularia lunata.
  JOURNAL   Biochim. Biophys. Acta. 152 (1968) 144-58.
  ORGANISM  Curvularia lunata
PATHWAY     PATH: map00140  C21-Steroid hormone metabolism
            PATH: map00150  Androgen and estrogen metabolism
ORTHOLOGY   KO: K00497  cytochrome P450, family 11, subfamily B (steroid
                        11beta-monooxygenase)
GENES       HSA: 1584(CYP11B1) 1585(CYP11B2)
            MMU: 13072(Cyp11b2)
            RNO: 24294(Cyp11b2) 353498(Cyp11b3)
            CFA: 482071(CYP11B2)
            BTA: 282422(CYP11B1)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.15.4
            ExPASy - ENZYME nomenclature database: 1.14.15.4
            ExplorEnz - The Enzyme Database: 1.14.15.4
            ERGO genome analysis and discovery system: 1.14.15.4
            BRENDA, the Enzyme Database: 1.14.15.4
            CAS: 9029-66-7
///
ENTRY       EC 1.14.15.5                Enzyme
NAME        corticosterone 18-monooxygenase;
            corticosterone 18-hydroxylase;
            corticosterone methyl oxidase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced iron-sulfur protein as one donor, and incorporation of
            one atom of oxygen into the other donor
SYSNAME     corticosterone,reduced-adrenal-ferredoxin:oxygen oxidoreductase
            (18-hydroxylating)
REACTION    corticosterone + reduced adrenal ferredoxin + O2 =
            18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
            [RN:R03262]
ALL_REAC    R03262
SUBSTRATE   corticosterone [CPD:C02140];
            reduced adrenal ferredoxin [CPD:C00662];
            O2 [CPD:C00007]
PRODUCT     18-hydroxycorticosterone [CPD:C01124];
            oxidized adrenal ferredoxin [CPD:C00667];
            H2O [CPD:C00001]
REFERENCE   1
  AUTHORS   Raman, P.B., Sharma, D.C. and Dorfman, R.I.
  TITLE     Studies on aldosterone biosynthesis in vitro.
  JOURNAL   Biochemistry 5 (1966) 1795.
  ORGANISM  cow [GN:bta], guinea pig, sheep
PATHWAY     PATH: map00140  C21-Steroid hormone metabolism
ORTHOLOGY   KO: K07433  corticosterone 18-monooxygenase
GENES       HSA: 1584(CYP11B1) 1585(CYP11B2)
            MMU: 13072(Cyp11b2)
            RNO: 24294(Cyp11b2) 353498(Cyp11b3)
            CFA: 482071(CYP11B2)
            BTA: 282422(CYP11B1)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.15.5
            ExPASy - ENZYME nomenclature database: 1.14.15.5
            ExplorEnz - The Enzyme Database: 1.14.15.5
            ERGO genome analysis and discovery system: 1.14.15.5
            BRENDA, the Enzyme Database: 1.14.15.5
            CAS: 37256-75-0
///
ENTRY       EC 1.14.15.6                Enzyme
NAME        cholesterol monooxygenase (side-chain-cleaving);
            cholesterol desmolase;
            cytochrome P-450scc;
            desmolase, steroid 20-22;
            C27-side chain cleavage enzyme;
            cholesterol 20-22-desmolase;
            cholesterol C20-22 desmolase;
            cholesterol side-chain cleavage enzyme;
            cholesterol side-chain-cleaving enzyme;
            enzymes, cholesterol side-chain-cleaving;
            steroid 20-22 desmolase;
            steroid 20-22-lyase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced iron-sulfur protein as one donor, and incorporation of
            one atom of oxygen into the other donor
SYSNAME     cholesterol,reduced-adrenal-ferredoxin:oxygen oxidoreductase
            (side-chain-cleaving)
REACTION    cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone +
            4-methylpentanal + oxidized adrenal ferredoxin + H2O [RN:R02724]
ALL_REAC    R02724;
            (other) R01454 R02723 R03933 R04676 R04854 R04855
SUBSTRATE   cholesterol [CPD:C00187];
            reduced adrenal ferredoxin [CPD:C00662];
            O2 [CPD:C00007]
PRODUCT     pregnenolone [CPD:C01953];
            4-methylpentanal [CPD:C02373];
            oxidized adrenal ferredoxin [CPD:C00667];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A heme-thiolate protein. The reaction proceeds in three stages, with
            hydroxylation at C-20 and C-22 preceding scission of the side-chain
            at C-20.
REFERENCE   1  [PMID:6766943]
  AUTHORS   Hanukoglu I, Jefcoate CR.
  TITLE     Mitochondrial cytochrome P-450sec. Mechanism of electron transport
            by adrenodoxin.
  JOURNAL   J. Biol. Chem. 255 (1980) 3057-61.
REFERENCE   2  [PMID:7217084]
  AUTHORS   Hanukoglu I, Spitsberg V, Bumpus JA, Dus KM, Jefcoate CR.
  TITLE     Adrenal mitochondrial cytochrome P-450scc. Cholesterol and
            adrenodoxin interactions at equilibrium and during turnover.
  JOURNAL   J. Biol. Chem. 256 (1981) 4321-8.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00140  C21-Steroid hormone metabolism
ORTHOLOGY   KO: K00498  cytochrome P450, family 11, subfamily A (cholesterol
                        monooxygenase (side-chain-cleaving))
GENES       HSA: 1583(CYP11A1)
            MMU: 13070(Cyp11a1)
            RNO: 29680(Cyp11a1)
            CFA: 478365(LOC478365)
            BTA: 338048(CYP11A1)
            SSC: 403329(CYP11A1)
            GGA: 414838(CYP11A1)
            DRE: 80374(cyp11a1)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.15.6
            ExPASy - ENZYME nomenclature database: 1.14.15.6
            ExplorEnz - The Enzyme Database: 1.14.15.6
            ERGO genome analysis and discovery system: 1.14.15.6
            BRENDA, the Enzyme Database: 1.14.15.6
            CAS: 37292-81-2
///
ENTRY       EC 1.14.15.7                Enzyme
NAME        choline monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced iron-sulfur protein as one donor, and incorporation of
            one atom of oxygen into the other donor
SYSNAME     choline,reduced-ferredoxin:oxygen oxidoreductase
REACTION    choline + O2 + 2 reduced ferredoxin + 2 H+ = betaine aldehyde
            hydrate + H2O + 2 oxidized ferredoxin [RN:R05739]
ALL_REAC    R05739;
            (other) R07409
SUBSTRATE   choline [CPD:C00114];
            O2 [CPD:C00007];
            reduced ferredoxin [CPD:C00138];
            H+ [CPD:C00080]
PRODUCT     betaine aldehyde hydrate [CPD:C07345];
            H2O [CPD:C00001];
            oxidized ferredoxin [CPD:C00139]
COMMENT     The spinach enzyme, which is located in the chloroplast, contains a
            Rieske-type [2Fe-2S] cluster, and probably also a mononuclear Fe
            centre. Requires Mg2+. Catalyses the first step of glycine betaine
            synthesis. In many bacteria, plants and animals, betaine is
            synthesized in two steps: (1) choline to betaine aldehyde and (2)
            betaine aldehyde to betaine. Different enzymes are involved in the
            first reaction. In plants, the reaction is catalysed by this enzyme
            whereas in animals and many bacteria, it is catalysed by either
            membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble
            choline oxidase (EC 1.1.3.17) [7]. The enzyme involved in the second
            step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the
            same in plants, animals and bacteria. In some bacteria, betaine is
            synthesized from glycine through the actions of EC 2.1.1.156,
            glycine/sarcosine N-methyltransferase and EC 2.1.1.157,
            sarcosine/dimethylglycine N-methyltransferase.
REFERENCE   1
  AUTHORS   Brouquisse, R., Weigel, P., Rhodes, D., Yocum, C.F. and Hanson, A.D.
  TITLE     Evidence for a ferredoxin-dependent choline monooxygenase from
            spinach chloroplast stroma.
  JOURNAL   Plant Physiol. 90 (1989) 322-329.
  ORGANISM  spinach
REFERENCE   2  [PMID:12228495]
  AUTHORS   Burnet M, Lafontaine PJ, Hanson AD.
  TITLE     Assay, Purification, and Partial Characterization of Choline
            Monooxygenase from Spinach.
  JOURNAL   Plant. Physiol. 108 (1995) 581-588.
  ORGANISM  spinach
REFERENCE   3  [PMID:9096415]
  AUTHORS   Rathinasabapathi B, Burnet M, Russell BL, Gage DA, Liao PC, Nye GJ,
            Scott P, Golbeck JH, Hanson AD.
  TITLE     Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the
            first step of glycine betaine synthesis in plants: prosthetic group
            characterization and cDNA cloning.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 3454-8.
  ORGANISM  spinach
REFERENCE   4  [PMID:9489025]
  AUTHORS   Russell BL, Rathinasabapathi B, Hanson AD.
  TITLE     Osmotic stress induces expression of choline monooxygenase in sugar
            beet and amaranth.
  JOURNAL   Plant. Physiol. 116 (1998) 859-65.
  ORGANISM  spinach, Beta vulgaris
REFERENCE   5
  AUTHORS   Nuccio, M.L., Russell, B.L., Nolte, K.D., Rathinasabapathi, B.,
            Gage, D.A. and Hanson, A.D.
  TITLE     Glycine betaine synthesis in transgenic tobacco expressing choline
            monooxygenase is limited by the endogenous choline supply.
  JOURNAL   Plant J. 16 (1998) 101-110.
  ORGANISM  Nicotiana tabacum
REFERENCE   6  [PMID:9881168]
  AUTHORS   Nuccio ML, Russell BL, Nolte KD, Rathinasabapathi B, Gage DA, Hanson
            AD.
  TITLE     The endogenous choline supply limits glycine betaine synthesis in
            transgenic tobacco expressing choline monooxygenase.
  JOURNAL   Plant. J. 16 (1998) 487-96.
  ORGANISM  spinach, Nicotiana tabacum
REFERENCE   7  [PMID:12466265]
  AUTHORS   Waditee R, Tanaka Y, Aoki K, Hibino T, Jikuya H, Takano J, Takabe T,
            Takabe T.
  TITLE     Isolation and functional characterization of N-methyltransferases
            that catalyze betaine synthesis from glycine in a halotolerant
            photosynthetic organism Aphanothece halophytica.
  JOURNAL   J. Biol. Chem. 278 (2003) 4932-42.
  ORGANISM  Aphanothece halophytica
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K00499  choline monooxygenase
GENES       ATH: AT4G29890
            LPN: lpg2218
            LPF: lpl2143
            LPP: lpp2170
            BUR: Bcep18194_B0529 Bcep18194_B2214 Bcep18194_C7702
            BAM: Bamb_3247
            BPM: BURPS1710b_A0845
            HAR: HEAR0275
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.15.7
            ExPASy - ENZYME nomenclature database: 1.14.15.7
            ExplorEnz - The Enzyme Database: 1.14.15.7
            ERGO genome analysis and discovery system: 1.14.15.7
            BRENDA, the Enzyme Database: 1.14.15.7
///
ENTRY       EC 1.14.15.-                Enzyme
CLASS       Oxidoreductases;
            Acting on paired donors with incorporation of molecular oxygen;
            With a reduced iron-sulfur protein as one donor, and incorporation
            of one atom of oxygen
REACTION    (1) Benzyl alcohol + NAD+ + H2O <=> Toluene + Oxygen + NADH
            [RN:R02550];
            (2) 4-Cresol + Oxidized ferredoxin + H2O <=> Ferredoxin + Toluene +
            Oxygen [RN:R03569];
            (3) Calcidiol + Oxidized ferredoxin + H2O <=> Vitamin D3 + Reduced
            ferredoxin + Oxygen [RN:R03611];
            (4) o-Xylene + Reduced rubredoxin + Oxygen <=> 2-Methylbenzyl
            alcohol + Oxidized rubredoxin + H2O [RN:R05489];
            (5) p-Xylene + Reduced rubredoxin + Oxygen <=> 4-Methylbenzyl
            alcohol + Oxidized rubredoxin + H2O [RN:R05490];
            (6) m-Xylene + Reduced rubredoxin + Oxygen <=> 3-Methylbenzyl
            alcohol + Oxidized rubredoxin + H2O [RN:R05491];
            (7) 2 Atrazine + Oxygen <=> 2 Deisopropylatrazine + 2 Acetone
            [RN:R05564];
            (8) 2 Atrazine + Oxygen <=> 2 Deethylatrazine + 2 Acetaldehyde
            [RN:R05565];
            (9) 2 Deisopropylatrazine + Oxygen <=> 2 Deisopropyldeethylatrazine
            + 2 Acetaldehyde [RN:R05567];
            (10) 2 Deethylatrazine + Oxygen <=> 2 Deisopropyldeethylatrazine + 2
            Acetone [RN:R05568];
            (11) Cyclohexane + Oxygen + NADH + H+ <=> Cyclohexanol + NAD+ + H2O
            [RN:R06945]
SUBSTRATE   Benzyl alcohol [CPD:C00556];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001];
            4-Cresol [CPD:C01468];
            Oxidized ferredoxin [CPD:C00139];
            Calcidiol [CPD:C01561];
            o-Xylene [CPD:C07212];
            Reduced rubredoxin [CPD:C00340];
            Oxygen [CPD:C00007];
            p-Xylene [CPD:C06756];
            m-Xylene [CPD:C07208];
            Atrazine [CPD:C06551];
            Deisopropylatrazine [CPD:C06556];
            Deethylatrazine [CPD:C06559];
            Cyclohexane [CPD:C11249];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
PRODUCT     Toluene [CPD:C01455];
            Oxygen [CPD:C00007];
            NADH [CPD:C00004];
            Ferredoxin [CPD:C01695];
            Vitamin D3 [CPD:C05443];
            Reduced ferredoxin [CPD:C00138];
            2-Methylbenzyl alcohol [CPD:C07213];
            Oxidized rubredoxin [CPD:C00435];
            H2O [CPD:C00001];
            4-Methylbenzyl alcohol [CPD:C06757];
            3-Methylbenzyl alcohol [CPD:C07216];
            Deisopropylatrazine [CPD:C06556];
            Acetone [CPD:C00207];
            Deethylatrazine [CPD:C06559];
            Acetaldehyde [CPD:C00084];
            Deisopropyldeethylatrazine [CPD:C06560];
            Cyclohexanol [CPD:C00854];
            NAD+ [CPD:C00003]
///
ENTRY       EC 1.14.16.1                Enzyme
NAME        phenylalanine 4-monooxygenase;
            phenylalaninase;
            phenylalanine 4-hydroxylase;
            phenylalanine hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced pteridine as one donor, and incorporation of one atom
            of oxygen into the other donor
SYSNAME     L-phenylalanine,tetrahydrobiopterin:oxygen oxidoreductase
            (4-hydroxylating)
REACTION    L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine +
            4a-hydroxytetrahydrobiopterin [RN:R07211]
ALL_REAC    R07211;
            (other) R01795
SUBSTRATE   L-phenylalanine [CPD:C00079];
            tetrahydrobiopterin [CPD:C00272];
            O2 [CPD:C00007]
PRODUCT     L-tyrosine [CPD:C00082];
            4a-hydroxytetrahydrobiopterin [CPD:C15522]
COFACTOR    Iron [CPD:C00023]
COMMENT     The active centre contains mononuclear iron(II). The reaction
            involves an arene oxide that rearranges to give the phenolic hydroxy
            group. This results in the hydrogen at C-4 migrating to C-3 and in
            part being retained. This process is known as the NIH-shift. The
            4a-hydroxytetrahydrobiopterin formed can dehydrate to
            6,7-dihydrobiopterin, both spontaneously and by the action of EC
            4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase. The
            6,7-dihydrobiopterin can be enzymically reduced back to
            tetrahydrobiopterin, by EC 1.5.1.34, 6,7-dihydropteridine reductase,
            or slowly rearranges into the more stable compound
            7,8-dihydrobiopterin.
REFERENCE   1  [PMID:5773277]
  AUTHORS   Guroff G, Rhoads CA.
  TITLE     Phenylalanine hydroxylation by Pseudomonas species (ATCC 11299a).
            Nature of the cofactor.
  JOURNAL   J. Biol. Chem. 244 (1969) 142-6.
  ORGANISM  Pseudomonas sp.
REFERENCE   2
  AUTHORS   Kaufman, S.
  TITLE     Studies on the mechanism of the enzymic conversion of phenylalanine
            to tyrosine.
  JOURNAL   J. Biol. Chem. 234 (1959) 2677-2682.
  ORGANISM  rat [GN:rno], sheep
REFERENCE   3
  AUTHORS   Mitoma, C.
  TITLE     Studies on partially purified phenylalanine hydroxylase.
  JOURNAL   Arch. Biochem. Biophys. 60 (1956) 476-484.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:14927641]
  AUTHORS   UDENFRIEND S, COOPER JR.
  TITLE     The enzymatic conversion of phenylalanine to tyrosine.
  JOURNAL   J. Biol. Chem. 194 (1952) 503-11.
  ORGANISM  rat [GN:rno], guinea pig, rabbit, dog [GN:cfa], chicken [GN:gga],
            human [GN:hsa]
REFERENCE   5  [PMID:7779797]
  AUTHORS   Carr RT, Balasubramanian S, Hawkins PC, Benkovic SJ.
  TITLE     Mechanism of metal-independent hydroxylation by Chromobacterium
            violaceum phenylalanine hydroxylase.
  JOURNAL   Biochemistry. 34 (1995) 7525-32.
  ORGANISM  Chromobacterium violaceum [GN:cvi]
REFERENCE   6  [PMID:11718561]
  AUTHORS   Andersen OA, Flatmark T, Hough E.
  TITLE     High resolution crystal structures of the catalytic domain of human
            phenylalanine hydroxylase in its catalytically active Fe(II) form
            and binary complex with tetrahydrobiopterin.
  JOURNAL   J. Mol. Biol. 314 (2001) 279-91.
  ORGANISM  human [GN:hsa]
REFERENCE   7  [PMID:12096915]
  AUTHORS   Erlandsen H, Kim JY, Patch MG, Han A, Volner A, Abu-Omar MM, Stevens
            RC.
  TITLE     Structural comparison of bacterial and human iron-dependent
            phenylalanine hydroxylases: similar fold, different stability and
            reaction rates.
  JOURNAL   J. Mol. Biol. 320 (2002) 645-61.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K00500  phenylalanine-4-hydroxylase
GENES       HSA: 5053(PAH)
            MMU: 18478(Pah)
            RNO: 24616(Pah)
            CFA: 475446(PAH)
            GGA: 408024(PAH)
            DRE: 378962(pah)
            CEL: K08F8.4(pah-1)
            CME: CMJ066C
            DDI: DDB_0231664(pah)
            TET: TTHERM_00829460
            LMA: LmjF28.1280
            XCC: XCC0156(pah)
            XCB: XC_0165
            XCV: XCV0157(phhA)
            XAC: XAC0174(pah)
            XOO: XOO0267(pah)
            XOM: XOO_0243(XOO0243)
            VCH: VCA0828
            VCO: VC0395_0407(phhA)
            VVU: VV2_0455
            VVY: VVA1005
            VPA: VPA0576
            PPR: PBPRB1164
            PAE: PA0872(phhA)
            PAU: PA14_52990(phhA)
            PAP: PSPA7_4644(phhA)
            PPU: PP_4490(phhA)
            PST: PSPTO_1822(phhA)
            PSB: Psyr_3575
            PSP: PSPPH_3531(phhA)
            PFL: PFL_1611(phhA)
            PFO: Pfl_1499
            PEN: PSEEN3892(phhA)
            PMY: Pmen_3112
            PCR: Pcryo_1554
            SON: SO_1666(phhA)
            SDN: Sden_2595
            SFR: Sfri_1328
            SAZ: Sama_2222
            SBL: Sbal_1484
            SBM: Shew185_1479
            SLO: Shew_1435
            SPC: Sputcn32_1386
            SSE: Ssed_2930
            SPL: Spea_1448
            SHE: Shewmr4_2607
            SHM: Shewmr7_2674
            SHN: Shewana3_2781
            SHW: Sputw3181_2715
            ILO: IL0725
            CPS: CPS_3766(phhA)
            PHA: PSHAa2043(phhA)
            PAT: Patl_2999
            LPN: lpg2647(phhA)
            LPF: lpl2572(phhA)
            LPP: lpp2700(phhA)
            HCH: HCH_00956(phhA)
            AHA: AHA_1883(phhA)
            CVI: CV_3180(phhA)
            RSO: RSc3355(phhA)
            REU: Reut_A3387
            REH: H16_A3678(phhA)
            RME: Rmet_3533
            BMA: BMA2927(phhA)
            BMV: BMASAVP1_A3383(phhA)
            BML: BMA10299_A1616(phhA)
            BMN: BMA10247_2986(phhA)
            BXE: Bxe_A0011
            BUR: Bcep18194_A3259
            BCN: Bcen_2977
            BCH: Bcen2424_0078
            BAM: Bamb_0069
            BPS: BPSL3424(phhA)
            BPM: BURPS1710b_0206(phhA)
            BPL: BURPS1106A_4075(phhA)
            BPD: BURPS668_4001(phhA)
            BTE: BTH_I3337(phhA)
            POL: Bpro_0168 Bpro_4215
            PNA: Pnap_1117
            AAV: Aave_4193
            AJS: Ajs_0518
            VEI: Veis_2136
            MPT: Mpe_A0347
            BBA: Bd3537
            ADE: Adeh_2800
            MXA: MXAN_5127
            RBE: RBE_1408
            RBO: A1I_07840(phhA)
            MLO: mlr4831
            RET: RHE_CH01742(phhA)
            RLE: RL1860(phhA)
            CCR: CC_1612
            MMR: Mmar10_1853
            HNE: HNE_1395(phhA)
            NAR: Saro_3187
            SAL: Sala_0553 Sala_1392
            ELI: ELI_12050
            ABA: Acid345_1076
            BAN: BA4586
            BAR: GBAA4586
            BAA: BA_5025
            BAT: BAS4253
            BCE: BC4352
            BCA: BCE_4439
            BCZ: BCZK4102(pah)
            BTK: BT9727_4091(pah)
            BTL: BALH_3943(pah)
            NFA: nfa9410
            CHU: CHU_3025(phhA)
            GFO: GFO_0233(phhA)
            FPS: FP1954(phhA)
STRUCTURES  PDB: 1DMW  1J8T  1J8U  1KW0  1LRM  1LTU  1LTV  1LTZ  1MMK  1MMT  
                 1PAH  1PHZ  1TDW  1TG2  2PAH  2PHM  2V27  2V28  3PAH  4PAH  
                 5PAH  6PAH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.16.1
            ExPASy - ENZYME nomenclature database: 1.14.16.1
            ExplorEnz - The Enzyme Database: 1.14.16.1
            ERGO genome analysis and discovery system: 1.14.16.1
            BRENDA, the Enzyme Database: 1.14.16.1
            CAS: 9029-73-6
///
ENTRY       EC 1.14.16.2                Enzyme
NAME        tyrosine 3-monooxygenase;
            L-tyrosine hydroxylase;
            tyrosine 3-hydroxylase;
            tyrosine hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced pteridine as one donor, and incorporation of one atom
            of oxygen into the other donor
SYSNAME     L-tyrosine,tetrahydrobiopterin:oxygen oxidoreductase
            (3-hydroxylating)
REACTION    L-tyrosine + tetrahydrobiopterin + O2 =
            3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin
            [RN:R07212]
ALL_REAC    R07212;
            (other) R01815
SUBSTRATE   L-tyrosine [CPD:C00082];
            tetrahydrobiopterin [CPD:C00272];
            O2 [CPD:C00007]
PRODUCT     3,4-dihydroxy-L-phenylalanine [CPD:C00355];
            4a-hydroxytetrahydrobiopterin [CPD:C15522]
COFACTOR    Iron [CPD:C00023]
COMMENT     The active centre contains mononuclear iron(II). The enzyme is
            activated by phosphorylation, catalysed by EC 2.7.11.27, [acetyl-CoA
            carboxylase] kinase. The 4a-hydroxytetrahydrobiopterin formed can
            dehydrate to 6,7-dihydrobiopterin, both spontaneously and by the
            action of EC 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase.
            The 6,7-dihydrobiopterin can be enzymically reduced back to
            tetrahydrobiopterin, by EC 1.5.1.34 (6,7-dihydropteridine
            reductase), or slowly rearranges into the more stable compound
            7,8-dihydrobiopterin.
REFERENCE   1  [PMID:6133218]
  AUTHORS   El Mestikawy S, Glowinski J, Hamon M.
  TITLE     Tyrosine hydroxylase activation in depolarized dopaminergic
            terminals--involvement of Ca2+-dependent phosphorylation.
  JOURNAL   Nature. 302 (1983) 830-2.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6033458]
  AUTHORS   Ikeda M, Levitt M, Udenfriend S.
  TITLE     Phenylalanine as substrate and inhibitor of tyrosine hydroxylase.
  JOURNAL   Arch. Biochem. Biophys. 120 (1967) 420-7.
  ORGANISM  cow [GN:bta], guinea pig
REFERENCE   3
  AUTHORS   Nagatsu, T., Levitt, M. and Udenfriend, S.
  TITLE     Tyrosine hydroxylase. The initial step in norepinephrine
            biosynthesis.
  JOURNAL   J. Biol. Chem. 239 (1964) 2910-2917.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:2872947]
  AUTHORS   Pigeon D, Drissi-Daoudi R, Gros F, Thibault J.
  TITLE     [Copurification of tyrosine hydroxylase from rat pheochromocytoma by
            protein kinase]
  JOURNAL   C. R. Acad. Sci. III. 302 (1986) 435-8.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:9228951]
  AUTHORS   Goodwill KE, Sabatier C, Marks C, Raag R, Fitzpatrick PF, Stevens
            RC.
  TITLE     Crystal structure of tyrosine hydroxylase at 2.3 A and its
            implications for inherited neurodegenerative diseases.
  JOURNAL   Nat. Struct. Biol. 4 (1997) 578-85.
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map05020  Parkinson's disease
ORTHOLOGY   KO: K00501  tyrosine 3-monooxygenase
GENES       HSA: 7054(TH)
            MMU: 21823(Th)
            RNO: 25085(Th)
            CFA: 403444(TH)
            BTA: 280707(TH)
            GGA: 395592(TH)
            SPU: 581094(LOC581094)
            DME: Dmel_CG10118(ple)
STRUCTURES  PDB: 1TOH  2TOH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.16.2
            ExPASy - ENZYME nomenclature database: 1.14.16.2
            ExplorEnz - The Enzyme Database: 1.14.16.2
            ERGO genome analysis and discovery system: 1.14.16.2
            BRENDA, the Enzyme Database: 1.14.16.2
            CAS: 9036-22-0
///
ENTRY       EC 1.14.16.3                Enzyme
NAME        anthranilate 3-monooxygenase;
            anthranilate 3-hydroxylase;
            anthranilate hydroxylase;
            anthranilic hydroxylase;
            anthranilic acid hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced pteridine as one donor, and incorporation of one atom
            of oxygen into the other donor
SYSNAME     anthranilate,tetrahydrobiopterin:oxygen oxidoreductase
            (3-hydroxylating)
REACTION    anthranilate + tetrahydrobiopterin + O2 = 3-hydroxyanthranilate +
            dihydrobiopterin + H2O [RN:R01816]
ALL_REAC    R01816
SUBSTRATE   anthranilate [CPD:C00108];
            tetrahydrobiopterin [CPD:C00272];
            O2 [CPD:C00007]
PRODUCT     3-hydroxyanthranilate [CPD:C00632];
            dihydrobiopterin [CPD:C00268];
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+.
REFERENCE   1  [PMID:5789774]
  AUTHORS   Jequier E, Robinson DS, Lovenberg W, Sjoerdsma A.
  TITLE     Further studies on tryptophan hydroxylase in rat brainstem and beef
            pineal.
  JOURNAL   Biochem. Pharmacol. 18 (1969) 1071-81.
  ORGANISM  rat [GN:rno], cow [GN:bta]
REFERENCE   2
  AUTHORS   Nair, P.M. and Vaidyanathan, C.S.
  TITLE     Anthranilic acid hydroxylase from Tecoma stans.
  JOURNAL   Biochim. Biophys. Acta 110 (1965) 521-531.
  ORGANISM  Tecoma stans
PATHWAY     PATH: map00380  Tryptophan metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.16.3
            ExPASy - ENZYME nomenclature database: 1.14.16.3
            ExplorEnz - The Enzyme Database: 1.14.16.3
            ERGO genome analysis and discovery system: 1.14.16.3
            BRENDA, the Enzyme Database: 1.14.16.3
            CAS: 37256-79-4
///
ENTRY       EC 1.14.16.4                Enzyme
NAME        tryptophan 5-monooxygenase;
            L-tryptophan hydroxylase;
            indoleacetic acid-5-hydroxylase;
            tryptophan 5-hydroxylase;
            tryptophan hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced pteridine as one donor, and incorporation of one atom
            of oxygen into the other donor
SYSNAME     L-tryptophan,tetrahydrobiopterin:oxygen oxidoreductase
            (5-hydroxylating)
REACTION    L-tryptophan + tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan +
            4a-hydroxytetrahydrobiopterin [RN:R07213]
ALL_REAC    R07213;
            (other) R01814
SUBSTRATE   L-tryptophan [CPD:C00078];
            tetrahydrobiopterin [CPD:C00272];
            O2 [CPD:C00007]
PRODUCT     5-hydroxy-L-tryptophan [CPD:C00643];
            4a-hydroxytetrahydrobiopterin [CPD:C15522]
COFACTOR    Iron [CPD:C00023]
COMMENT     The active centre contains mononuclear iron(II). The enzyme is
            activated by phosphorylation, catalysed by a Ca2+-activated protein
            kinase. The 4a-hydroxytetrahydrobiopterin formed can dehydrate to
            6,7-dihydrobiopterin, both spontaneously and by the action of EC
            4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase. The
            6,7-dihydrobiopterin can be enzymically reduced back to
            tetrahydrobiopterin, by EC 1.5.1.34 (6,7-dihydropteridine
            reductase), or slowly rearranges into the more stable compound
            7,8-dihydrobiopterin.
REFERENCE   1  [PMID:4402511]
  AUTHORS   Friedman PA, Kappelman AH, Kaufman S.
  TITLE     Partial purification and characterization of tryptophan hydroxylase
            from rabbit hindbrain.
  JOURNAL   J. Biol. Chem. 247 (1972) 4165-73.
  ORGANISM  rabbit
REFERENCE   2  [PMID:315449]
  AUTHORS   Hamon M, Bourgoin S, Artaud F, Glowinski J.
  TITLE     The role of intraneuronal 5-HT and of tryptophan hydroxylase
            activation in the control of 5-HT synthesis in rat brain slices
            incubated in K+-enriched medium.
  JOURNAL   J. Neurochem. 33 (1979) 1031-42.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:5309585]
  AUTHORS   Ichiyama A, Nakamura S, Nishizuka Y, Hayaishi O.
  TITLE     Enzymic studies on the biosynthesis of serotonin in mammalian brain.
  JOURNAL   J. Biol. Chem. 245 (1970) 1699-709.
  ORGANISM  guinea pig
REFERENCE   4  [PMID:5789774]
  AUTHORS   Jequier E, Robinson DS, Lovenberg W, Sjoerdsma A.
  TITLE     Further studies on tryptophan hydroxylase in rat brainstem and beef
            pineal.
  JOURNAL   Biochem. Pharmacol. 18 (1969) 1071-81.
  ORGANISM  cow [GN:bta]
REFERENCE   5  [PMID:12379098]
  AUTHORS   Wang L, Erlandsen H, Haavik J, Knappskog PM, Stevens RC.
  TITLE     Three-dimensional structure of human tryptophan hydroxylase and its
            implications for the biosynthesis of the neurotransmitters serotonin
            and melatonin.
  JOURNAL   Biochemistry. 41 (2002) 12569-74.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00380  Tryptophan metabolism
ORTHOLOGY   KO: K00502  tryptophan 5-monooxygenase
GENES       HSA: 121278(TPH2) 7166(TPH1)
            PTR: 467070(TPH2)
            MMU: 216343(Tph2) 21990(Tph1)
            RNO: 24848(Tph1) 317675(Tph2)
            GGA: 395799(SERGEF) 408026(TPH2)
            DRE: 407712(tph2)
            DME: Dmel_CG7399(Hn) Dmel_CG9122(Trh)
            TET: TTHERM_00997520
            SRU: SRU_2069
STRUCTURES  PDB: 1MLW  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.16.4
            ExPASy - ENZYME nomenclature database: 1.14.16.4
            ExplorEnz - The Enzyme Database: 1.14.16.4
            ERGO genome analysis and discovery system: 1.14.16.4
            BRENDA, the Enzyme Database: 1.14.16.4
            CAS: 9037-21-2
///
ENTRY       EC 1.14.16.5                Enzyme
NAME        glyceryl-ether monooxygenase;
            glyceryl-ether cleaving enzyme;
            alkylglycerol monooxygenase;
            glyceryl ether oxygenase;
            glyceryl etherase;
            O-alkylglycerol monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced pteridine as one donor, and incorporation of one atom
            of oxygen into the other donor
SYSNAME     1-alkyl-sn-glycerol,tetrahydrobiopterin:oxygen oxidoreductase
REACTION    1-alkyl-sn-glycerol + tetrahydrobiopterin + O2 =
            1-hydroxyalkyl-sn-glycerol + dihydrobiopterin + H2O [RN:R04044]
ALL_REAC    R04044
SUBSTRATE   1-alkyl-sn-glycerol [CPD:C02773];
            tetrahydrobiopterin [CPD:C00272];
            O2 [CPD:C00007]
PRODUCT     1-hydroxyalkyl-sn-glycerol [CPD:C03658];
            dihydrobiopterin [CPD:C00268];
            H2O [CPD:C00001]
COFACTOR    Glutathione [CPD:C00051];
            Phospholipid [CPD:C00865]
COMMENT     Requires reduced glutathione and phospholipids for full activity.
            The product spontaneously breaks down to form a fatty aldehyde and
            glycerol.
REFERENCE   1  [PMID:6840084]
  AUTHORS   Ishibashi T, Imai Y.
  TITLE     Solubilization and partial characterization of alkylglycerol
            monooxygenase from rat liver microsomes.
  JOURNAL   Eur. J. Biochem. 132 (1983) 23-7.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4383918]
  AUTHORS   Pfleger RC, Piantadosi C, Snyder F.
  TITLE     The biocleavage of isomeric glyceryl ethers by soluble liver enzymes
            in a variety of species.
  JOURNAL   Biochim. Biophys. Acta. 144 (1967) 633-48.
  ORGANISM  dog [GN:cfa], guinea pig, gerbil, mouse [GN:mmu], hamster, rabbit,
            slug
REFERENCE   3  [PMID:4355017]
  AUTHORS   Snyder F, Malone B, Piantadosi C.
  TITLE     Tetrahydropteridine-dependent cleavage enzyme for O-alkyl lipids:
            substrate specificity.
  JOURNAL   Biochim. Biophys. Acta. 316 (1973) 259-65.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:4402391]
  AUTHORS   Soodsma JF, Piantadosi C, Snyder F.
  TITLE     Partial characterization of the alkylglycerol cleavage enzyme system
            of rat liver.
  JOURNAL   J. Biol. Chem. 247 (1972) 3923-9.
  ORGANISM  rat [GN:rno]
REFERENCE   5
  AUTHORS   Tietz, A., Lindberg, M. and Kennedy, E.P.
  TITLE     A new pteridine-requiring enzyme system for the oxidation of
            glyceryl ethers.
  JOURNAL   J. Biol. Chem. 239 (1964) 4081-4090.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.16.5
            ExPASy - ENZYME nomenclature database: 1.14.16.5
            ExplorEnz - The Enzyme Database: 1.14.16.5
            ERGO genome analysis and discovery system: 1.14.16.5
            BRENDA, the Enzyme Database: 1.14.16.5
            CAS: 37256-82-9
///
ENTRY       EC 1.14.16.6                Enzyme
NAME        mandelate 4-monooxygenase;
            L-mandelate 4-hydroxylase;
            mandelic acid 4-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced pteridine as one donor, and incorporation of one atom
            of oxygen into the other donor
SYSNAME     (S)-2-hydroxy-2-phenylacetate,tetrahydrobiopterin:oxygen
            oxidoreductase (4-hydroxylating)
REACTION    (S)-2-hydroxy-2-phenylacetate + tetrahydrobiopterin + O2 =
            (S)-4-hydroxymandelate + dihydrobiopterin + H2O [RN:R03794]
ALL_REAC    R03794
SUBSTRATE   (S)-2-hydroxy-2-phenylacetate [CPD:C01984];
            tetrahydrobiopterin [CPD:C00272];
            O2 [CPD:C00007]
PRODUCT     (S)-4-hydroxymandelate [CPD:C03198];
            dihydrobiopterin [CPD:C00268];
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+.
REFERENCE   1  [PMID:9909]
  AUTHORS   Bhat SG, Vaidyanathan CS.
  TITLE     Purifications and properties of L-mandelate- 4-hydroxylase from
            Pseudomonas convexa.
  JOURNAL   Arch. Biochem. Biophys. 176 (1976) 314-23.
  ORGANISM  Pseudomonas convexa
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.16.6
            ExPASy - ENZYME nomenclature database: 1.14.16.6
            ExplorEnz - The Enzyme Database: 1.14.16.6
            ERGO genome analysis and discovery system: 1.14.16.6
            BRENDA, the Enzyme Database: 1.14.16.6
            CAS: 39459-82-0
///
ENTRY       EC 1.14.16.-                Enzyme
CLASS       Oxidoreductases;
            Acting on paired donors with incorporation of molecular oxygen;
            With reduced pteridine as one donor, and incorporation of one atom
            of oxygen
REACTION    Indole + Oxygen <=> Indoxyl + H2O [RN:R02339]
SUBSTRATE   Indole [CPD:C00463];
            Oxygen [CPD:C00007]
PRODUCT     Indoxyl [CPD:C05658];
            H2O [CPD:C00001]
///
ENTRY       EC 1.14.17.1                Enzyme
NAME        dopamine beta-monooxygenase;
            dopamine beta-hydroxylase;
            MDBH (membrane-associated dopamine beta-monooxygenase);
            SDBH (soluble dopamine beta-monooxygenase);
            dopamine-B-hydroxylase;
            oxygenase, dopamine beta-mono-;
            3,4-dihydroxyphenethylamine beta-oxidase;
            4-(2-aminoethyl)pyrocatechol beta-oxidase;
            dopa beta-hydroxylase;
            dopamine beta-oxidase;
            dopamine hydroxylase;
            phenylamine beta-hydroxylase;
            (3,4-dihydroxyphenethylamine)beta-mono-oxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced ascorbate as one donor, and incorporation of one atom
            of oxygen into the other donor
SYSNAME     3,4-dihydroxyphenethylamine,ascorbate:oxygen oxidoreductase
            (beta-hydroxylating)
REACTION    3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline +
            dehydroascorbate + H2O [RN:R02535]
ALL_REAC    R02535
SUBSTRATE   3,4-dihydroxyphenethylamine [CPD:C03758];
            ascorbate [CPD:C00072];
            O2 [CPD:C00007]
PRODUCT     noradrenaline [CPD:C00547];
            dehydroascorbate [CPD:C00425];
            H2O [CPD:C00001]
COFACTOR    Copper [CPD:C00070];
            PQQ [CPD:C00113];
            Fumarate [CPD:C00122]
COMMENT     A copper protein. Stimulated by fumarate.
REFERENCE   1  [PMID:5846992]
  AUTHORS   Friedman S, Kaufman S.
  TITLE     3,4-dihydroxyphenylethylamine beta-hydroxylase. Physical properties,
            copper content, and role of copper in the catalytic acttivity.
  JOURNAL   J. Biol. Chem. 240 (1965) 4763-73.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   Levin, E.Y., Levenberg, B. and Kaufman, S.
  TITLE     The enzymatic conversion of 3,4-dihydroxyphenylethylamine to
            norepinephrine.
  JOURNAL   J. Biol. Chem. 235 (1960) 2080-2086.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00350  Tyrosine metabolism
ORTHOLOGY   KO: K00503  dopamine beta-monooxygenase
GENES       HSA: 1621(DBH)
            PTR: 464827(DBH)
            MMU: 13166(Dbh)
            RNO: 25699(Dbh)
            CFA: 448806(DBH)
            BTA: 280758(DBH)
            GGA: 395549(DBH)
            DME: Dmel_CG12673(olf413) Dmel_CG12781(nahoda) Dmel_CG1543(Tbh)
                 Dmel_CG6217(knk)
            CEL: H13N06.6(tbh-1)
STRUCTURES  PDB: 1ZHB  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.17.1
            ExPASy - ENZYME nomenclature database: 1.14.17.1
            ExplorEnz - The Enzyme Database: 1.14.17.1
            ERGO genome analysis and discovery system: 1.14.17.1
            BRENDA, the Enzyme Database: 1.14.17.1
            CAS: 9013-38-1
///
ENTRY       EC 1.14.17.2      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced ascorbate as one donor, and incorporation of one atom
            of oxygen into the other donor
COMMENT     Deleted entry: 4-coumarate 3-monooxygenase. Now included with EC
            1.14.18.1 monophenol monooxygenase (EC 1.14.17.2 created 1972,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.17.2
            ExPASy - ENZYME nomenclature database: 1.14.17.2
            ExplorEnz - The Enzyme Database: 1.14.17.2
            ERGO genome analysis and discovery system: 1.14.17.2
            BRENDA, the Enzyme Database: 1.14.17.2
///
ENTRY       EC 1.14.17.3                Enzyme
NAME        peptidylglycine monooxygenase;
            peptidylglycine 2-hydroxylase;
            peptidyl alpha-amidating enzyme;
            peptide-alpha-amide synthetase;
            synthase, peptide alpha-amide;
            peptide alpha-amidating enzyme;
            peptide alpha-amide synthase;
            peptidylglycine alpha-hydroxylase;
            peptidylglycine alpha-amidating monooxygenase;
            PAM-A;
            PAM-B;
            PAM
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced ascorbate as one donor, and incorporation of one atom
            of oxygen into the other donor
SYSNAME     peptidylglycine,ascorbate:oxygen oxidoreductase (2-hydroxylating)
REACTION    peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) +
            dehydroascorbate + H2O [RN:R03912]
ALL_REAC    R03912
SUBSTRATE   peptidylglycine [CPD:C02303];
            ascorbate [CPD:C00072];
            O2 [CPD:C00007]
PRODUCT     peptidyl(2-hydroxyglycine) [CPD:C03718];
            dehydroascorbate [CPD:C00425];
            H2O [CPD:C00001]
COFACTOR    Copper [CPD:C00070]
COMMENT     A copper protein. Peptidylglycines with a neutral amino acid residue
            in the penultimate position are the best substrates for the enzyme.
            The product is unstable and dismutates to glyoxylate and the
            corresponding desglycine peptide amide, a reaction catalysed by EC
            4.3.2.5 peptidylamidoglycolate lyase. Involved in the final step of
            biosynthesis of alpha-melanotropin and related biologically active
            peptides.
REFERENCE   1  [PMID:7099265]
  AUTHORS   Bradbury AF, Finnie MD, Smyth DG.
  TITLE     Mechanism of C-terminal amide formation by pituitary enzymes.
  JOURNAL   Nature. 298 (1982) 686-8.
REFERENCE   2  [PMID:3691506]
  AUTHORS   Bradbury AF, Smyth DG.
  TITLE     Enzyme-catalysed peptide amidation. Isolation of a stable
            intermediate formed by reaction of the amidating enzyme with an
            imino acid.
  JOURNAL   Eur. J. Biochem. 169 (1987) 579-84.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:2994573]
  AUTHORS   Glembotski CC.
  TITLE     Further characterization of the peptidyl alpha-amidating enzyme in
            rat anterior pituitary secretory granules.
  JOURNAL   Arch. Biochem. Biophys. 241 (1985) 673-83.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:2207061]
  AUTHORS   Katopodis AG, Ping D, May SW.
  TITLE     A novel enzyme from bovine neurointermediate pituitary catalyzes
            dealkylation of alpha-hydroxyglycine derivatives, thereby
            functioning sequentially with peptidylglycine alpha-amidating
            monooxygenase in peptide amidation.
  JOURNAL   Biochemistry. 29 (1990) 6115-20.
  ORGANISM  cow [GN:bta]
REFERENCE   5  [PMID:3453894]
  AUTHORS   Murthy AS, Keutmann HT, Eipper BA.
  TITLE     Further characterization of peptidylglycine alpha-amidating
            monooxygenase from bovine neurointermediate pituitary.
  JOURNAL   Mol. Endocrinol. 1 (1987) 290-9.
  ORGANISM  cow [GN:bta]
REFERENCE   6  [PMID:3944110]
  AUTHORS   Murthy AS, Mains RE, Eipper BA.
  TITLE     Purification and characterization of peptidylglycine alpha-amidating
            monooxygenase from bovine neurointermediate pituitary.
  JOURNAL   J. Biol. Chem. 261 (1986) 1815-22.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K00504  peptidylglycine monooxygenase
GENES       HSA: 23077(MYCBP2) 5066(PAM)
            PTR: 461974(PAM)
            MMU: 18484(Pam)
            RNO: 25508(Pam)
            CFA: 479145(PAM)
            BTA: 280890(PAM)
            GGA: 427274(PAM)
            SPU: 579753(LOC579753) 580829(LOC580829)
            DME: Dmel_CG3832(Phm) Dmel_CG5472(Pal)
            RDE: RD1_2432(pam)
            RBA: RB9882(pam)
STRUCTURES  PDB: 1OPM  1PHM  1SDW  1YI9  1YIP  1YJK  1YJL  3PHM  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.17.3
            ExPASy - ENZYME nomenclature database: 1.14.17.3
            ExplorEnz - The Enzyme Database: 1.14.17.3
            ERGO genome analysis and discovery system: 1.14.17.3
            BRENDA, the Enzyme Database: 1.14.17.3
            CAS: 90597-47-0
///
ENTRY       EC 1.14.17.4                Enzyme
NAME        aminocyclopropanecarboxylate oxidase;
            ACC oxidase;
            ethylene-forming enzyme
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With reduced ascorbate as one donor, and incorporation of one atom
            of oxygen into the other donor
SYSNAME     1-aminocyclopropane-1-carboxylate oxygenase (ethylene-forming)
REACTION    1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethylene +
            cyanide + dehydroascorbate + CO2 + 2 H2O [RN:R07214]
ALL_REAC    R07214
SUBSTRATE   1-aminocyclopropane-1-carboxylate [CPD:C01234];
            ascorbate [CPD:C00072];
            O2 [CPD:C00007]
PRODUCT     ethylene [CPD:C06547];
            cyanide [CPD:C00177];
            dehydroascorbate [CPD:C00425];
            CO2 [CPD:C00011];
            H2O [CPD:C00001]
COMMENT     A nonheme iron enzyme. Requires CO2 for activity. In the enzyme from
            plants, the ethylene has signalling functions such as stimulation of
            fruit-ripening.
REFERENCE   1  [PMID:7717997]
  AUTHORS   Zhang Z, Schofield CJ, Baldwin JE, Thomas P, John P.
  TITLE     Expression, purification and characterization of
            1-aminocyclopropane-1-carboxylate oxidase from tomato in Escherichia
            coli.
  JOURNAL   Biochem. J. 307 ( Pt 1) (1995) 77-85.
  ORGANISM  Lycopersicon esculentum [GN:eles]
REFERENCE   2  [PMID:9398335]
  AUTHORS   Zhang Z, Barlow JN, Baldwin JE, Schofield CJ.
  TITLE     Metal-catalyzed oxidation and mutagenesis studies on the iron(II)
            binding site of 1-aminocyclopropane-1-carboxylate oxidase.
  JOURNAL   Biochemistry. 36 (1997) 15999-6007.
  ORGANISM  Lycopersicon esculentum [GN:eles]
REFERENCE   3
  AUTHORS   Pirrung, M.C.
  TITLE     Ethylene biosynthesis from 1-aminocyclopropanecarboxylic acid.
  JOURNAL   Acc. Chem. Res. 32 (1999) 711-718.
  ORGANISM  Lycopersicon esculentum [GN:eles]
REFERENCE   4  [PMID:11361015]
  AUTHORS   Charng YY, Chou SJ, Jiaang WT, Chen ST, Yang SF.
  TITLE     The catalytic mechanism of 1-aminocyclopropane-1-carboxylic acid
            oxidase.
  JOURNAL   Arch. Biochem. Biophys. 385 (2001) 179-85.
  ORGANISM  Lycopersicon esculentum [GN:eles]
REFERENCE   5  [PMID:11583172]
  AUTHORS   Thrower JS, Blalock R 3rd, Klinman JP.
  TITLE     Steady-state kinetics of substrate binding and iron release in
            tomato ACC oxidase.
  JOURNAL   Biochemistry. 40 (2001) 9717-24.
  ORGANISM  Lycopersicon esculentum [GN:eles]
ORTHOLOGY   KO: K05933  aminocyclopropanecarboxylate oxidase
GENES       ATH: AT1G05010(EFE) AT1G12010 AT1G62380(ACO2) AT1G77330
                 AT2G19590(ACO1)
            OSA: 4337818 4347225
STRUCTURES  PDB: 1W9Y  1WA6  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.17.4
            ExPASy - ENZYME nomenclature database: 1.14.17.4
            ExplorEnz - The Enzyme Database: 1.14.17.4
            ERGO genome analysis and discovery system: 1.14.17.4
            BRENDA, the Enzyme Database: 1.14.17.4
///
ENTRY       EC 1.14.18.1                Enzyme
NAME        monophenol monooxygenase;
            tyrosinase;
            phenolase;
            monophenol oxidase;
            cresolase;
            catechol oxidase;
            polyphenolase;
            pyrocatechol oxidase;
            dopa oxidase;
            chlorogenic oxidase;
            catecholase;
            polyphenol oxidase;
            monophenolase;
            o-diphenol oxidase;
            chlorogenic acid oxidase;
            diphenol oxidase;
            o-diphenolase;
            tyrosine-dopa oxidase;
            o-diphenol:oxygen oxidoreductase;
            polyaromatic oxidase;
            monophenol monooxidase;
            o-diphenol oxidoreductase;
            monophenol dihydroxyphenylalanine:oxygen oxidoreductase;
            N-acetyl-6-hydroxytryptophan oxidase;
            monophenol, dihydroxy-L-phenylalanine oxygen oxidoreductase;
            o-diphenol:O2 oxidoreductase;
            phenol oxidase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With another compound as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     monophenol,L-dopa:oxygen oxidoreductase
REACTION    L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O [RN:R02078]
ALL_REAC    R02078;
            (other) R00731 R02363 R02383 R02950 R03674 R04693 R04884
SUBSTRATE   L-tyrosine [CPD:C00082];
            L-dopa [CPD:C00355];
            O2 [CPD:C00007]
PRODUCT     L-dopa [CPD:C00355];
            dopaquinone [CPD:C00822];
            H2O [CPD:C00001]
COFACTOR    Copper [CPD:C00070]
COMMENT     A group of copper proteins that also catalyse the reaction of EC
            1.10.3.1 catechol oxidase, if only 1,2-benzenediols are available as
            substrate.
REFERENCE   1
  AUTHORS   Dawson, C.R. and Tarpley, W.B.
  TITLE     The copper oxidases.
  JOURNAL   In: Sumner, J.B. and Myrback, K. (Eds.), The Enzymes, 1st ed., vol.
            2, Academic Press, New York, 1951, p. 454-498.
REFERENCE   2  [PMID:151279]
  AUTHORS   Lerch K.
  TITLE     Amino acid sequence of tyrosinase from Neurospora crassa.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 75 (1978) 3635-9.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   3
  AUTHORS   Malmstrom, B.G., Andreasson, L.-E. and Reinhammar, B.
  TITLE     Copper-containing oxidases and superoxide dismutase.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 12, Academic
            Press, New York, 1975, p. 507-579.
REFERENCE   4  [PMID:170916]
  AUTHORS   McIntyre RJ, Vaughan PF.
  TITLE     Kinetic studies on the hydroxylation of p-coumaric acid to caffeic
            acid by spinach-beet phenolase.
  JOURNAL   Biochem. J. 149 (1975) 447-61.
  ORGANISM  Beta vulgaris
REFERENCE   5  [PMID:5842066]
  AUTHORS   Patil SS, Zucker M.
  TITLE     Potato phenolases. Purification and properties.
  JOURNAL   J. Biol. Chem. 240 (1965) 3938-43.
  ORGANISM  Solanum tuberosum [GN:estu]
REFERENCE   6
  AUTHORS   Pomerantz, S.H.
  TITLE     Separation, purification, and properties of two tyrosinases from
            hamster melanoma.
  JOURNAL   J. Biol. Chem. 238 (1963) 2351-2357.
  ORGANISM  hamster
REFERENCE   7
  AUTHORS   Robb, D.A.
  TITLE     `Tyrosinase.
  JOURNAL   In: Lontie, R. (Ed.), Copper Proteins and Copper Enzymes, vol. 2,
            CRC Press, Boca Raton, FL, 1984, p. 207-240.
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00740  Riboflavin metabolism
            PATH: map00950  Alkaloid biosynthesis I
            PATH: map04916  Melanogenesis
ORTHOLOGY   KO: K00505  tyrosinase
GENES       HSA: 7299(TYR)
            PTR: 451473(TYR)
            MMU: 22173(Tyr)
            RNO: 308800(Tyr)
            CFA: 403405(TYR)
            BTA: 280951(TYR)
            SSC: 407745(TYR)
            GGA: 373971(TYR)
            XTR: 549915(LOC549915)
            DRE: 30207(tyr)
            DME: Dmel_CG2952(Dox-A3) Dmel_CG5779(Bc)
            CEL: C34G6.2(tyr-4)
            ANI: AN2799.2 AN5311.2
            AFM: AFUA_1G17430 AFUA_3G01070
            AOR: AO090001000383 AO090010000557 AO090023000424
            PFO: Pfl_3461
            CVI: CV_3262
            RSO: RSc1501(mel)
            BUR: Bcep18194_C6986
            BPM: BURPS1710b_A0806
            BTE: BTH_II0649
            NEU: NE1241
            NMU: Nmul_A2156
            SMD: Smed_6129 Smed_6429
            RET: RHE_PD00076(melA)
            RPB: RPB_2167
            NWI: Nwi_0968
            NHA: Nham_2941
            SUS: Acid_5081
            BCA: BCE_A0211
            CEF: CE1756
            SCO: SCO2700(melC2)
            SMA: SAV5362(melC1-2)
            FRA: Francci3_0237
            FAL: FRAAL0531
            RXY: Rxyl_1947
STRUCTURES  PDB: 1WX2  1WX3  1WX4  1WX5  1WXC  2AHK  2AHL  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.18.1
            ExPASy - ENZYME nomenclature database: 1.14.18.1
            ExplorEnz - The Enzyme Database: 1.14.18.1
            ERGO genome analysis and discovery system: 1.14.18.1
            BRENDA, the Enzyme Database: 1.14.18.1
            CAS: 9002-10-2
///
ENTRY       EC 1.14.18.2                Enzyme
NAME        CMP-N-acetylneuraminate monooxygenase;
            CMP-N-acetylneuraminic acid hydroxylase;
            CMP-Neu5Ac hydroxylase;
            cytidine monophosphoacetylneuraminate monooxygenase;
            N-acetylneuraminic monooxygenase;
            cytidine-5'-monophosphate-N-acetylneuraminic acid hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With another compound as one donor, and incorporation of one atom of
            oxygen into the other donor
SYSNAME     CMP-N-acetylneuraminate,ferrocytochrome-b5:oxygen oxidoreductase
            (N-acetyl-hydroxylating)
REACTION    CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+ =
            CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O [RN:R01115]
ALL_REAC    R01115;
            (other) R01803
SUBSTRATE   CMP-N-acetylneuraminate [CPD:C00128];
            ferrocytochrome b5 [CPD:C00999];
            O2 [CPD:C00007];
            H+ [CPD:C00080]
PRODUCT     CMP-N-glycoloylneuraminate [CPD:C03691];
            ferricytochrome b5 [CPD:C00996];
            H2O [CPD:C00001]
COMMENT     This enzyme contains both a Rieske-type [2Fe-2S] cluster and a
            second iron site. The ferricytochrome b5 produced is reduced by NADH
            and cytochrome-b5 reductase (EC 1.6.2.2). The enzyme can be
            activated by Fe2+ or Fe3+.
REFERENCE   1  [PMID:3202954]
  AUTHORS   Shaw L, Schauer R.
  TITLE     The biosynthesis of N-glycoloylneuraminic acid occurs by
            hydroxylation of the CMP-glycoside of N-acetylneuraminic acid.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 369 (1988) 477-86.
REFERENCE   2  [PMID:1964451]
  AUTHORS   Kozutsumi Y, Kawano T, Yamakawa T, Suzuki A.
  TITLE     Participation of cytochrome b5 in CMP-N-acetylneuraminic acid
            hydroxylation in mouse liver cytosol.
  JOURNAL   J. Biochem. (Tokyo). 108 (1990) 704-6.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:7841794]
  AUTHORS   Schneckenburger P, Shaw L, Schauer R.
  TITLE     Purification, characterization and reconstitution of
            CMP-N-acetylneuraminate hydroxylase from mouse liver.
  JOURNAL   Glycoconj. J. 11 (1994) 194-203.
  ORGANISM  mouse [GN:mmu]
REFERENCE   4  [PMID:7608218]
  AUTHORS   Kawano T, Koyama S, Takematsu H, Kozutsumi Y, Kawasaki H, Kawashima
            S, Kawasaki T, Suzuki A.
  TITLE     Molecular cloning of cytidine monophospho-N-acetylneuraminic acid
            hydroxylase. Regulation of species- and tissue-specific expression
            of N-glycolylneuraminic acid.
  JOURNAL   J. Biol. Chem. 270 (1995) 16458-63.
  ORGANISM  mouse [GN:mmu]
REFERENCE   5  [PMID:8647250]
  AUTHORS   Schlenzka W, Shaw L, Kelm S, Schmidt CL, Bill E, Trautwein AX,
            Lottspeich F, Schauer R.
  TITLE     CMP-N-acetylneuraminic acid hydroxylase: the first cytosolic Rieske
            iron-sulphur protein to be described in Eukarya.
  JOURNAL   FEBS. Lett. 385 (1996) 197-200.
  ORGANISM  mouse [GN:mmu], pig [GN:ssc]
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K08080  CMP-N-acetylneuraminate monooxygenase
GENES       PTR: 450121(CMAH)
            MMU: 12763(Cmah)
            RNO: 361245(Cmah)
            CFA: 488248(LOC488248)
            XLA: 379989(cmah)
            DRE: 431739(zgc:92407)
            SPU: 586677(LOC586677)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.18.2
            ExPASy - ENZYME nomenclature database: 1.14.18.2
            ExplorEnz - The Enzyme Database: 1.14.18.2
            ERGO genome analysis and discovery system: 1.14.18.2
            BRENDA, the Enzyme Database: 1.14.18.2
            CAS: 116036-67-0
///
ENTRY       EC 1.14.18.-                Enzyme
CLASS       Oxidoreductases;
            Acting on paired donors with incorporation of molecular oxygen;
            With another compound as one donor, and incorporation of one atom of
            oxygen
REACTION    (1) 5,6-Dihydroxyindole-2-carboxylate <=> Melanin [RN:R06612];
            (2) 2 6-Hydroxypseudooxynicotine + Oxygen <=> 2
            2,6-Dihydroxypseudooxynicotine [RN:R07514]
SUBSTRATE   5,6-Dihydroxyindole-2-carboxylate [CPD:C04185]
PRODUCT     Melanin [CPD:C05606]
///
ENTRY       EC 1.14.19.1                Enzyme
NAME        stearoyl-CoA 9-desaturase;
            Delta9-desaturase;
            acyl-CoA desaturase;
            fatty acid desaturase;
            stearoyl-CoA, hydrogen-donor:oxygen oxidoreductase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With oxidation of a pair of donors resulting in the reduction of O2
            to two molecules of water
SYSNAME     stearoyl-CoA,ferrocytochrome-b5:oxygen oxidoreductase
            (9,10-dehydrogenating)
REACTION    stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2
            ferricytochrome b5 + 2 H2O [RN:R02222]
ALL_REAC    R02222
SUBSTRATE   stearoyl-CoA [CPD:C00412];
            ferrocytochrome b5 [CPD:C00999];
            O2 [CPD:C00007];
            H+ [CPD:C00080]
PRODUCT     oleoyl-CoA [CPD:C00510];
            ferricytochrome b5 [CPD:C00996];
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023]
COMMENT     An iron protein. The rat liver enzyme is an enzyme system involving
            cytochrome b5 and EC 1.6.2.2, cytochrome-b5 reductase. The
            ferricytochrome b5 produced is reduced by NADH and cytochrome-b5
            reductase (EC 1.6.2.2).
REFERENCE   1  [PMID:14167617]
  AUTHORS   FULCO AJ, BLOCH K.
  TITLE     COFACTOR REQUIREMENTS FOR THE FORMATION OF DELTA-9-UNSATURATED FATTY
            ACIDS IN MYCOBACTERIUM PHLEI.
  JOURNAL   J. Biol. Chem. 239 (1964) 993-7.
  ORGANISM  Mycobacterium phlei
REFERENCE   2  [PMID:4382040]
  AUTHORS   Oshino N, Imai Y, Sato R.
  TITLE     Electron-transfer mechanism associated with fatty acid desaturation
            catalyzed by liver microsomes.
  JOURNAL   Biochim. Biophys. Acta. 128 (1966) 13-27.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:5543646]
  AUTHORS   Oshino N, Imai Y, Sato R.
  TITLE     A function of cytochrome b5 in fatty acid desaturation by rat liver
            microsomes.
  JOURNAL   J. Biochem. (Tokyo). 69 (1971) 155-67.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:4373719]
  AUTHORS   Strittmatter P, Spatz L, Corcoran D, Rogers MJ, Setlow B, Redline R.
  TITLE     Purification and properties of rat liver microsomal stearyl coenzyme
            A desaturase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 71 (1974) 4565-9.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map01040  Polyunsaturated fatty acid biosynthesis
            PATH: map03320  PPAR signaling pathway
ORTHOLOGY   KO: K00507  stearoyl-CoA desaturase
            KO: K10204  setearoyl-CoA desaturase
GENES       HSA: 6319(SCD) 79966(SCD5)
            PTR: 450676(SCD) 461211(SCD5)
            MMU: 20249(Scd1) 20250(Scd2) 30049(Scd3)
            RNO: 246074(Scd1) 83792(Scd2)
            CFA: 486839(SCD)
            BTA: 280924(SCD) 617419(SCD5)
            SSC: 396670(SCD)
            GGA: 395706(SCD)
            XLA: 447633(MGC86272)
            DRE: 386661(scd)
            DME: Dmel_CG5887 Dmel_CG5925(desat2) Dmel_CG7923(Fad2)
            CEL: F10D2.9(fat-7) VZK822L.1(fat-6) W06D12.3(fat-5)
            CME: CMJ201C CMM045C
            SCE: YGL055W(OLE1)
            AGO: AGOS_AAR153C
            PIC: PICST_70693(OLE1)
            CGR: CAGL0I00418g
            SPO: SPCC1281.06c
            ANI: AN6731.2
            AFM: AFUA_7G05920
            AOR: AO090005000456 AO090102000339
            CNE: CNJ01180
            DDI: DDBDRAFT_0188116
            PFA: PFE0555w
            TET: TTHERM_00052620 TTHERM_00463280
            TBR: Tb927.8.6000
            XCC: XCC0162 XCC1332(desC)
            XCB: XC_0171 XC_2907
            XCV: XCV0164 XCV1434
            XAC: XAC0180 XAC1378(desC)
            XOO: XOO1917(desC) XOO4514
            XOM: XOO_1815(XOO1815) XOO_4253(XOO4253)
            VVU: VV2_0069
            VVY: VVA0576
            VPA: VPA0707
            VFI: VFA0274
            PPR: PBPRB0742
            PEN: PSEEN5527
            PAR: Psyc_1365
            PCR: Pcryo_0999
            PRW: PsycPRwf_1267
            ACI: ACIAD0630 ACIAD1627(desC)
            ACB: A1S_2881
            SDN: Sden_0229
            SFR: Sfri_0123
            SAZ: Sama_0191
            SBL: Sbal_4181
            SBM: Shew185_0174
            SLO: Shew_0136
            SPC: Sputcn32_3542
            SSE: Ssed_4340
            SPL: Spea_0162
            SHE: Shewmr4_0176
            SHM: Shewmr7_0171
            SHN: Shewana3_0177
            SHW: Sputw3181_3679
            ILO: IL0278
            PHA: PSHAa2897
            PAT: Patl_4032
            PIN: Ping_1494
            MAQ: Maqu_1482
            LPN: lpg0249
            LPF: lpl0303
            LPP: lpp0319
            FTU: FTT1552(ole1)
            FTF: FTF1552(ole1)
            FTL: FTL_0557 FTL_1740
            NOC: Noc_2642 Noc_2775
            HCH: HCH_00335 HCH_03146
            AHA: AHA_0366
            CVI: CV_3397
            RSO: RS02366(RSp1029)
            REH: H16_A3039
            RME: Rmet_2875
            BMA: BMA2237
            BXE: Bxe_A0812
            BVI: Bcep1808_4009 Bcep1808_4010
            BUR: Bcep18194_A5839
            BCH: Bcen2424_2507
            BAM: Bamb_2554
            BPS: BPSL0911
            BPM: BURPS1710b_1130
            BTE: BTH_I0775 BTH_II0278(jamB)
            RFR: Rfer_3182
            POL: Bpro_3804 Bpro_5325 Bpro_5328
            HAR: HEAR2472
            MMS: mma_2567
            AZO: azo3119
            TBD: Tbd_2594
            BBA: Bd3068
            ADE: Adeh_1717
            AFW: Anae109_2085
            RTY: RT0092(aco1)
            RBE: RBE_0124(aco1)
            RET: RHE_CH00426(ypch00158)
            BJA: bll4594
            HNE: HNE_3136
            ABA: Acid345_4171
            SUS: Acid_2401 Acid_3162 Acid_5409
            TFU: Tfu_0413
            FRA: Francci3_1607 Francci3_2261 Francci3_3960
            SEN: SACE_0819 SACE_6758
            RBA: RB12551(scd) RB2032 RB4876 RB9629(desC)
            SYN: sll0541(desC)
            SYW: SYNW2377(desC)
            SYC: syc1549_d(desC)
            SYF: Synpcc7942_2561
            SYD: Syncc9605_2541
            SYE: Syncc9902_2191 Syncc9902_2192
            SYG: sync_2791 sync_2793
            SYX: SynWH7803_2415(desC) SynWH7803_2417(desC)
            CYA: CYA_2349
            CYB: CYB_0861
            TEL: tll1719(desC3) tlr2380(desC1)
            GVI: gll2866(desC) glr1235(desC)
            ANA: all1599(desC) all4991(desC)
            AVA: Ava_2277 Ava_4212
            PMA: Pro1833(OLE1)
            PMM: PMM1672(des9)
            PMT: PMT2172(desC) PMT2174(desC)
            PMN: PMN2A_1271
            PMI: PMT9312_1764
            PMB: A9601_18811(ole1)
            PMC: P9515_18621(ole1)
            PMF: P9303_28931 P9303_28951(ole1)
            PMG: P9301_18621(ole1)
            PME: NATL1_21421(ole1)
            TER: Tery_1437
            CHU: CHU_1063 CHU_1136 CHU_1595 CHU_1686
            GFO: GFO_3404
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.19.1
            ExPASy - ENZYME nomenclature database: 1.14.19.1
            ExplorEnz - The Enzyme Database: 1.14.19.1
            ERGO genome analysis and discovery system: 1.14.19.1
            BRENDA, the Enzyme Database: 1.14.19.1
            CAS: 9014-34-0
///
ENTRY       EC 1.14.19.2                Enzyme
NAME        acyl-[acyl-carrier-protein] desaturase;
            stearyl acyl carrier protein desaturase;
            stearyl-ACP desaturase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With oxidation of a pair of donors resulting in the reduction of O2
            to two molecules of water
SYSNAME     acyl-[acyl-carrier-protein], hydrogen-donor:oxygen oxidoreductase
REACTION    stearoyl-[acyl-carrier-protein] + reduced acceptor + O2 =
            oleoyl-[acyl-carrier-protein] + acceptor + 2 H2O [RN:R03370]
ALL_REAC    R03370
SUBSTRATE   stearoyl-[acyl-carrier-protein];
            reduced acceptor [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     oleoyl-[acyl-carrier-protein];
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
COFACTOR    Ferredoxin [CPD:C01695]
COMMENT     The enzyme from safflower is specific for stearoyl-CoA; that from
            Euglena acts on derivatives of a number of long-chain fatty acids.
            Requires ferredoxin.
REFERENCE   1  [PMID:4831331]
  AUTHORS   Jaworski JG, Stumpf PK.
  TITLE     Fat metabolism in higher plants. Properties of a soluble
            stearyl-acyl carrier protein desaturase from maturing Carthamus
            tinctorius.
  JOURNAL   Arch. Biochem. Biophys. 162 (1974) 158-65.
  ORGANISM  Carthamus tinctorius
REFERENCE   2  [PMID:4300868]
  AUTHORS   Nagai J, Bloch K.
  TITLE     Enzymatic desaturation of stearyl acyl carrier protein.
  JOURNAL   J. Biol. Chem. 243 (1968) 4626-33.
  ORGANISM  Euglena gracilis
PATHWAY     PATH: map01040  Polyunsaturated fatty acid biosynthesis
ORTHOLOGY   KO: K03920  acyl-[acyl-carrier-protein] desaturase
            KO: K03921  acyl-[acyl-carrier-protein] desaturase
            KO: K03922  acyl-[acyl-carrier-protein] desaturase
GENES       BCZ: BCZK2881(staD)
            MTU: Rv0824c(desA1) Rv1094(desA2)
            MTC: MT0846 MT1126
            MBO: Mb0847c(desA1) Mb1124(desA2)
            MBB: BCG_0877c(desA1) BCG_1154(desA2)
            MLE: ML1952(desA2) ML2185(desA1)
            MPA: MAP0658c(desA1) MAP2698c(desA2)
            MSM: MSMEG_5248
            NFA: nfa6080
            RHA: RHA1_ro02258 RHA1_ro04869 RHA1_ro05863
            SCO: SCO6717(SC4C6.27c)
            SMA: SAV1691
            FRA: Francci3_0307
            FAL: FRAAL0670
            FJO: Fjoh_0968
STRUCTURES  PDB: 1OQ4  1OQ7  1OQ9  1OQB  1ZA0  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.19.2
            ExPASy - ENZYME nomenclature database: 1.14.19.2
            ExplorEnz - The Enzyme Database: 1.14.19.2
            ERGO genome analysis and discovery system: 1.14.19.2
            BRENDA, the Enzyme Database: 1.14.19.2
            CAS: 37256-86-3
///
ENTRY       EC 1.14.19.3                Enzyme
NAME        linoleoyl-CoA desaturase;
            Delta6-desaturase;
            Delta6-fatty acyl-CoA desaturase;
            Delta6-acyl CoA desaturase;
            fatty acid Delta6-desaturase;
            fatty acid 6-desaturase;
            linoleate desaturase;
            linoleic desaturase;
            linoleic acid desaturase;
            linoleoyl CoA desaturase;
            linoleoyl-coenzyme A desaturase;
            long-chain fatty acid Delta6-desaturase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With oxidation of a pair of donors resulting in the reduction of O2
            to two molecules of water
SYSNAME     linoleoyl-CoA,hydrogen-donor:oxygen oxidoreductase
REACTION    linoleoyl-CoA + AH2 + O2 = gamma-linolenoyl-CoA + A + 2 H2O
            [RN:R03814]
ALL_REAC    R03814;
            (other) R07063 R07933
SUBSTRATE   linoleoyl-CoA [CPD:C02050];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     gamma-linolenoyl-CoA [CPD:C03035];
            A [CPD:C00028];
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023]
COMMENT     An iron protein. The rat liver enzyme is an enzyme system involving
            cytochrome b5 and EC 1.6.2.2, cytochrome-b5 reductase.
REFERENCE   1  [PMID:7212717]
  AUTHORS   Okayasu T, Nagao M, Ishibashi T, Imai Y.
  TITLE     Purification and partial characterization of linoleoyl-CoA
            desaturase from rat liver microsomes.
  JOURNAL   Arch. Biochem. Biophys. 206 (1981) 21-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00591  Linoleic acid metabolism
ORTHOLOGY   KO: K00508  linoleoyl-CoA desaturase
GENES       TET: TTHERM_00196130
            XCC: XCC3878
            XCB: XC_3964
            XCV: XCV4052
            XAC: XAC3959
            XOO: XOO4446
            XOM: XOO_4186(XOO4186)
            CVI: CV_1644(desD) CV_2452
            ADE: Adeh_1021
            AFW: Anae109_3187
            MTU: Rv3229c
            MTC: MT3326
            MBO: Mb3258c
            MBB: BCG_3259c(desA3_1) BCG_3352c(desA3_2)
            MPA: MAP3343c(desA3_1)
            MSM: MSMEG_1886
            CDI: DIP0704
            NFA: nfa46040
            RHA: RHA1_ro01408
            FAL: FRAAL6454(desA)
            SYN: sll0262(desD)
            CHU: CHU_3762 CHU_3764
            FJO: Fjoh_1748
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.19.3
            ExPASy - ENZYME nomenclature database: 1.14.19.3
            ExplorEnz - The Enzyme Database: 1.14.19.3
            ERGO genome analysis and discovery system: 1.14.19.3
            BRENDA, the Enzyme Database: 1.14.19.3
            CAS: 9014-34-0
///
ENTRY       EC 1.14.20.1                Enzyme
NAME        deacetoxycephalosporin-C synthase;
            DAOCS;
            penicillin N expandase;
            DAOC synthase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With 2-oxoglutarate as one donor, and the other dehydrogenated
SYSNAME     penicillin-N,2-oxoglutarate:oxygen oxidoreductase (ring-expanding)
REACTION    penicillin N + 2-oxoglutarate + O2 = deacetoxycephalosporin C +
            succinate + CO2 + H2O [RN:R05301]
ALL_REAC    R05301
SUBSTRATE   penicillin N [CPD:C06564];
            2-oxoglutarate [CPD:C00026];
            O2 [CPD:C00007]
PRODUCT     deacetoxycephalosporin C [CPD:C06565];
            succinate [CPD:C00042];
            CO2 [CPD:C00011];
            H2O [CPD:C00001]
COMMENT     Forms part of the penicillin biosynthesis pathway (for pathway,
            click here).
REFERENCE   1  [PMID:1354366]
  AUTHORS   Cantwell C, Beckmann R, Whiteman P, Queener SW, Abraham EP.
  TITLE     Isolation of deacetoxycephalosporin C from fermentation broths of
            Penicillium chrysogenum transformants: construction of a new fungal
            biosynthetic pathway.
  JOURNAL   Proc. R. Soc. Lond. B. Biol. Sci. 248 (1992) 283-9.
  ORGANISM  Penicillium chrysogenum
REFERENCE   2  [PMID:11352583]
  AUTHORS   Lee HJ, Lloyd MD, Harlos K, Clifton IJ, Baldwin JE, Schofield CJ.
  TITLE     Kinetic and crystallographic studies on deacetoxycephalosporin C
            synthase (DAOCS).
  JOURNAL   J. Mol. Biol. 308 (2001) 937-48.
  ORGANISM  Streptomyces clavuligerus
REFERENCE   3
  AUTHORS   Yeh, W.K., Ghag, S.K. and Queener, S.W.
  TITLE     Enzymes for epimerization of isopenicillin N, ring expansion of
            penicillin N, and 3'-hydroxylation of deacetoxycephalosporin C.
            Function, evolution, refolding, and enzyme engineering.
  JOURNAL   Ann. N.Y. Acad. Sci. 672 (1992) 396-408.
  ORGANISM  Penicillium chrysogenum
REFERENCE   4  [PMID:9723623]
  AUTHORS   Valegard K, van Scheltinga AC, Lloyd MD, Hara T, Ramaswamy S,
            Perrakis A, Thompson A, Lee HJ, Baldwin JE, Schofield CJ, Hajdu J,
            Andersson I.
  TITLE     Structure of a cephalosporin synthase.
  JOURNAL   Nature. 394 (1998) 805-9.
  ORGANISM  Cephalosporium acremonium
REFERENCE   5  [PMID:2656705]
  AUTHORS   Dotzlaf JE, Yeh WK.
  TITLE     Purification and properties of deacetoxycephalosporin C synthase
            from recombinant Escherichia coli and its comparison with the native
            enzyme purified from Streptomyces clavuligerus.
  JOURNAL   J. Biol. Chem. 264 (1989) 10219-27.
  ORGANISM  Streptomyces clavuligerus
PATHWAY     PATH: map00311  Penicillin and cephalosporin biosynthesis
STRUCTURES  PDB: 1UNB  1UO9  1UOB  1UOF  1UOG  1W28  1W2A  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.20.1
            ExPASy - ENZYME nomenclature database: 1.14.20.1
            ExplorEnz - The Enzyme Database: 1.14.20.1
            ERGO genome analysis and discovery system: 1.14.20.1
            BRENDA, the Enzyme Database: 1.14.20.1
            CAS: 85746-10-7
///
ENTRY       EC 1.14.21.1                Enzyme
NAME        (S)-stylopine synthase;
            (S)-cheilanthifoline oxidase (methylenedioxy-bridge-forming)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and the other dehydrogenated
SYSNAME     (S)-cheilanthifoline,NADPH:oxygen oxidoreductase
            (methylenedioxy-bridge-forming)
REACTION    (S)-cheilanthifoline + NADPH + H+ + O2 = (S)-stylopine + NADP+ + 2
            H2O [RN:R04690]
ALL_REAC    R04690
SUBSTRATE   (S)-cheilanthifoline [CPD:C05174];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (S)-stylopine [CPD:C05175];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate enzyme (P-450) catalysing an oxidative reaction that
            does not incorporate oxygen into the product. Forms the second
            methylenedioxy bridge of the protoberberine alkaloid stylopine from
            oxidative ring closure of adjacent phenolic and methoxy groups of
            cheilanthifoline.
REFERENCE   1
  AUTHORS   Bauer, W. and Zenk, M.H.
  TITLE     Two methylenedioxy bridge-forming cytochrome P-450 dependent enzymes
            are involved in (S)-stylopine biosynthesis.
  JOURNAL   Phytochemistry 30 (1991) 2953-2961.
  ORGANISM  Eschscholzia californica
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.21.1
            ExPASy - ENZYME nomenclature database: 1.14.21.1
            ExplorEnz - The Enzyme Database: 1.14.21.1
            ERGO genome analysis and discovery system: 1.14.21.1
            BRENDA, the Enzyme Database: 1.14.21.1
            CAS: 138791-29-4
///
ENTRY       EC 1.14.21.2                Enzyme
NAME        (S)-cheilanthifoline synthase;
            (S)-scoulerine oxidase (methylenedioxy-bridge-forming)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and the other dehydrogenated
SYSNAME     (S)-scoulerine,NADPH:oxygen oxidoreductase
            (methylenedioxy-bridge-forming)
REACTION    (S)-scoulerine + NADPH + H+ + O2 = (S)-cheilanthifoline + NADP+ + 2
            H2O [RN:R03834]
ALL_REAC    R03834
SUBSTRATE   (S)-scoulerine [CPD:C02106];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (S)-cheilanthifoline [CPD:C05174];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate enzyme (P-450) catalysing an oxidative reaction that
            does not incorporate oxygen into the product. Forms the
            methylenedioxy bridge of the protoberberine alkaloid
            cheilanthifoline from oxidative ring closure of adjacent phenolic
            and methoxy groups of scoulerine.
REFERENCE   1
  AUTHORS   Bauer, W. and Zenk, M.H.
  TITLE     Two methylenedioxy bridge-forming cytochrome P-450 dependent enzymes
            are involved in (S)-stylopine biosynthesis.
  JOURNAL   Phytochemistry 30 (1991) 2953-2961.
  ORGANISM  Eschscholzia californica
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.21.2
            ExPASy - ENZYME nomenclature database: 1.14.21.2
            ExplorEnz - The Enzyme Database: 1.14.21.2
            ERGO genome analysis and discovery system: 1.14.21.2
            BRENDA, the Enzyme Database: 1.14.21.2
            CAS: 138791-27-2
///
ENTRY       EC 1.14.21.3                Enzyme
NAME        berbamunine synthase;
            (S)-N-methylcoclaurine oxidase (C-O phenol-coupling)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and the other dehydrogenated
SYSNAME     (S)-N-methylcoclaurine,NADPH:oxygen oxidoreductase (C-O
            phenol-coupling)
REACTION    (S)-N-methylcoclaurine + (R)-N-methylcoclaurine + NADPH + H+ + O2 =
            berbamunine + NADP+ + 2 H2O [RN:R04694]
ALL_REAC    R04694;
            (other) R05210 R05215
SUBSTRATE   (S)-N-methylcoclaurine [CPD:C05176];
            (R)-N-methylcoclaurine [CPD:C05243];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     berbamunine [CPD:C05177];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate enzyme (P-450). Forms the bisbenzylisoquinoline
            alkaloid berbamunine by phenol oxidation of N-methylcoclaurine
            without the incorporation of oxygen into the product. Reaction of
            two molecules of (R)-N-methylcoclaurine gives the dimer
            guattagaumerine.
REFERENCE   1  [PMID:8380416]
  AUTHORS   Stadler R, Zenk MH.
  TITLE     The purification and characterization of a unique cytochrome P-450
            enzyme from Berberis stolonifera plant cell cultures.
  JOURNAL   J. Biol. Chem. 268 (1993) 823-31.
  ORGANISM  Berberis stolonifera
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
GENES       AZO: azo1622(plsX)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.21.3
            ExPASy - ENZYME nomenclature database: 1.14.21.3
            ExplorEnz - The Enzyme Database: 1.14.21.3
            ERGO genome analysis and discovery system: 1.14.21.3
            BRENDA, the Enzyme Database: 1.14.21.3
            CAS: 144941-42-4
///
ENTRY       EC 1.14.21.4                Enzyme
NAME        salutaridine synthase;
            (R)-reticuline oxidase (C-C phenol-coupling)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and the other dehydrogenated
SYSNAME     (R)-reticuline,NADPH:oxygen oxidoreductase (C-C phenol-coupling)
REACTION    (R)-reticuline + NADPH + H+ + O2 = salutaridine + NADP+ + 2 H2O
            [RN:R04696]
ALL_REAC    R04696
SUBSTRATE   (R)-reticuline [CPD:C05178];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     salutaridine [CPD:C05179];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A heme-thiolate enzyme (P-450). Forms the morphinan alkaloid
            salutaridine by intramolecular phenol oxidation of reticuline
            without the incorporation of oxygen into the product.
REFERENCE   1
  AUTHORS   Gerady, R. and Zenk, M.H.
  TITLE     Formation of salutaridine from (R)-reticuline by a membrane-bound
            cytochrome P-450 enzyme from Papaver somniferum.
  JOURNAL   Phytochemistry 32 (1993) 79-86.
  ORGANISM  Papaver somniferum
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.21.4
            ExPASy - ENZYME nomenclature database: 1.14.21.4
            ExplorEnz - The Enzyme Database: 1.14.21.4
            ERGO genome analysis and discovery system: 1.14.21.4
            BRENDA, the Enzyme Database: 1.14.21.4
            CAS: 149433-84-1
///
ENTRY       EC 1.14.21.5                Enzyme
NAME        (S)-canadine synthase;
            (S)-tetrahydroberberine synthase;
            (S)-tetrahydrocolumbamine oxidase (methylenedioxy-bridge-forming)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and the other dehydrogenated
SYSNAME     (S)-tetrahydrocolumbamine,NADPH:oxygen oxidoreductase
            (methylenedioxy-bridge-forming)
REACTION    (S)-tetrahydrocolumbamine + NADPH + H+ + O2 = (S)-canadine + NADP+ +
            2 H2O [RN:R04400]
ALL_REAC    R04400
SUBSTRATE   (S)-tetrahydrocolumbamine [CPD:C04118];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (S)-canadine [CPD:C03329];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    Heme-thiolate(P-450) [CPD:C05009]
COMMENT     A heme-thiolate enzyme (P-450) catalysing an oxidative reaction that
            does not incorporate oxygen into the product. Oxidation of the
            methoxyphenol group of the alkaloid tetrahydrocolumbamine results in
            the formation of the methylenedioxy bridge of canadine.
REFERENCE   1
  AUTHORS   Rueffer, M. and Zenk, M.H.
  TITLE     Canadine synthase from Thalictrum tuberosum cell cultures catalyses
            the formation of the methylenedioxy bridge in berberine synthesis.
  JOURNAL   Phytochemistry 36 (1994) 1219-1223.
  ORGANISM  Thalictrum tuberosum
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.21.5
            ExPASy - ENZYME nomenclature database: 1.14.21.5
            ExplorEnz - The Enzyme Database: 1.14.21.5
            ERGO genome analysis and discovery system: 1.14.21.5
            BRENDA, the Enzyme Database: 1.14.21.5
            CAS: 114308-22-4
///
ENTRY       EC 1.14.21.6                Enzyme
NAME        lathosterol oxidase;
            Delta7-sterol Delta5-dehydrogenase;
            Delta7-sterol 5-desaturase;
            Delta7-sterol-C5(6)-desaturase;
            5-DES
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            With NADH or NADPH as one donor, and the other dehydrogenated
SYSNAME     5alpha-cholest-7-en-3beta-ol,NAD(P)H:oxygen 5-oxidoreductase
REACTION    5alpha-cholest-7-en-3beta-ol + NAD(P)H + H+ + O2 =
            cholesta-5,7-dien-3beta-ol + NAD(P)+ + 2 H2O [RN:R03310 R07215]
ALL_REAC    R03310 R07215
SUBSTRATE   5alpha-cholest-7-en-3beta-ol [CPD:C01189];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     cholesta-5,7-dien-3beta-ol [CPD:C01164];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016];
            FMN [CPD:C00061]
COMMENT     This enzyme catalyses the introduction of a C5 double bond into the
            B ring of Delta7-sterols to yield the corresponding Delta5,7-sterols
            in mammals, yeast and plants [4]. Forms part of the plant sterol
            biosynthesis pathway.
REFERENCE   1  [PMID:14189869]
  AUTHORS   DEMPSEY ME, SEATON JD, SCHROEPFER GJ Jr, TROCKMAN RW.
  TITLE     THE INTERMEDIARY ROLE OF DELTA-5,7-CHOLESTADIEN-3-BETA-OL IN
            CHOLESTEROL BIOSYNTHESIS.
  JOURNAL   J. Biol. Chem. 239 (1964) 1381-7.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:9056262]
  AUTHORS   Nishino H, Nakaya J, Nishi S, Kurosawa T, Ishibashi T.
  TITLE     Temperature-induced differential kinetic properties between an
            initial burst and the following steady state in membrane-bound
            enzymes: studies on lathosterol 5-desaturase.
  JOURNAL   Arch. Biochem. Biophys. 339 (1997) 298-304.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:8561508]
  AUTHORS   Taton M, Rahier A.
  TITLE     Plant sterol biosynthesis: identification and characterization of
            higher plant delta 7-sterol C5(6)-desaturase.
  JOURNAL   Arch. Biochem. Biophys. 325 (1996) 279-88.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   4  [PMID:10651635]
  AUTHORS   Taton M, Husselstein T, Benveniste P, Rahier A.
  TITLE     Role of highly conserved residues in the reaction catalyzed by
            recombinant Delta7-sterol-C5(6)-desaturase studied by site-directed
            mutagenesis.
  JOURNAL   Biochemistry. 39 (2000) 701-11.
  ORGANISM  Arabidopsis thaliana [GN:ath]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K00227  lathosterol oxidase
GENES       HSA: 6309(SC5DL)
            PTR: 451624(SC5DL)
            MMU: 235293(Sc5d)
            RNO: 114100(Sc5d)
            CFA: 610411(SC5DL)
            XLA: 447026(sc5d)
            DRE: 447891(sc5d)
            SPU: 588561(LOC588561)
            ATH: AT3G02580(STE1)
            OSA: 4325687
            TET: TTHERM_00758950 TTHERM_01194720
            TBR: Tb927.8.3240
            TCR: 473111.10 507853.10
            LMA: LmjF23.1300
            HCH: HCH_01597
            ABU: Abu_1743
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.21.6
            ExPASy - ENZYME nomenclature database: 1.14.21.6
            ExplorEnz - The Enzyme Database: 1.14.21.6
            ERGO genome analysis and discovery system: 1.14.21.6
            BRENDA, the Enzyme Database: 1.14.21.6
            CAS: 37255-37-1
///
ENTRY       EC 1.14.99.1                Enzyme
NAME        prostaglandin-endoperoxide synthase;
            prostaglandin synthase;
            prostaglandin G/H synthase;
            (PG)H synthase;
            PG synthetase;
            prostaglandin synthetase;
            fatty acid cyclooxygenase;
            prostaglandin endoperoxide synthetase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate,hydrogen-donor:oxygen
            oxidoreductase
REACTION    arachidonate + AH2 + 2 O2 = prostaglandin H2 + A + H2O [RN:R01599]
ALL_REAC    R01599;
            (other) R00073 R01590
SUBSTRATE   arachidonate [CPD:C00219];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     prostaglandin H2 [CPD:C00427];
            A [CPD:C00028];
            H2O [CPD:C00001]
INHIBITOR   Aspirin [CPD:C01405];
            Naproxen [CPD:C01517];
            Sulindac [CPD:C01531];
            Ibuprofen [CPD:C01588];
            Piroxicam [CPD:C01608];
            Diclofenac [CPD:C01690];
            Diflunisal [CPD:C01691];
            Ketoprofen [CPD:C01716];
            Indomethacin [CPD:C01926];
            Mefenamic acid [CPD:C02168];
            Tolmetin sodium [CPD:C02328];
            Fenprofen calcium [CPD:C02539];
            Meclofenamate sodium [CPD:C02996]
COMMENT     This enzyme acts both as a dioxygenase and as a peroxidase.
REFERENCE   1  [PMID:3125548]
  AUTHORS   DeWitt DL, Smith WL.
  TITLE     Primary structure of prostaglandin G/H synthase from sheep vesicular
            gland determined from the complementary DNA sequence.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 1412-6.
  ORGANISM  sheep
REFERENCE   2  [PMID:104998]
  AUTHORS   Ohki S, Ogino N, Yamamoto S, Hayaishi O.
  TITLE     Prostaglandin hydroperoxidase, an integral part of prostaglandin
            endoperoxide synthetase from bovine vesicular gland microsomes.
  JOURNAL   J. Biol. Chem. 254 (1979) 829-36.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00590  Arachidonic acid metabolism
ORTHOLOGY   KO: K00509  prostaglandin-endoperoxide synthase
GENES       HSA: 5742(PTGS1) 5743(PTGS2)
            PTR: 464713(PTGS1) 469616(PTGS2)
            MMU: 19224(Ptgs1) 19225(Ptgs2)
            RNO: 24693(Ptgs1) 29527(Ptgs2)
            CFA: 403544(PTGS1) 442942(PTGS2)
            BTA: 282022(PTGS1) 282023(PTGS2)
            SSC: 397590(PGHS-2)
            GGA: 396451(PTGS2) 427752(PTGS1)
            XLA: 446781(ptgs2)
            XTR: 595089(ptgs2)
            DRE: 246226(ptgs1) 246227(ptgs2a) 559020(ptgs2b)
            ANI: AN5028.2
            AOR: AO090003000772
            UMA: UM04571.1
            RDE: RD1_1072
            MVA: Mvan_3099
STRUCTURES  PDB: 1CQE  1CVU  1CX2  1DDX  1DIY  1EBV  1EQG  1EQH  1HT5  1HT8  
                 1PGE  1PGF  1PGG  1PTH  1PXX  1Q4G  1U67  2AYL  2OYE  2OYU  
                 3PGH  4COX  5COX  6COX  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.1
            ExPASy - ENZYME nomenclature database: 1.14.99.1
            ExplorEnz - The Enzyme Database: 1.14.99.1
            ERGO genome analysis and discovery system: 1.14.99.1
            BRENDA, the Enzyme Database: 1.14.99.1
            CAS: 9055-65-6
///
ENTRY       EC 1.14.99.2                Enzyme
NAME        kynurenine 7,8-hydroxylase;
            kynurenic acid hydroxylase;
            kynurenic hydroxylase;
            kynurenate 7,8-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     kynurenate,hydrogen-donor:oxygen oxidoreductase (hydroxylating)
REACTION    kynurenate + AH2 + O2 = 7,8-dihydro-7,8-dihydroxykynurenate + A
            [RN:R03441]
ALL_REAC    R03441 > R03439 R03440
SUBSTRATE   kynurenate [CPD:C01717];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     7,8-dihydro-7,8-dihydroxykynurenate [CPD:C01249];
            A [CPD:C00028]
REFERENCE   1
  AUTHORS   Taniuchi, H. and Hayaishi, O.
  TITLE     Studies on the metabolism of kynurenic acid. III. Enzymatic
            formation of 7,8-dihydroxykynurenic acid from kynurenic acid.
  JOURNAL   J. Biol. Chem. 238 (1963) 283-293.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00380  Tryptophan metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.2
            ExPASy - ENZYME nomenclature database: 1.14.99.2
            ExplorEnz - The Enzyme Database: 1.14.99.2
            ERGO genome analysis and discovery system: 1.14.99.2
            BRENDA, the Enzyme Database: 1.14.99.2
            CAS: 9029-63-4
///
ENTRY       EC 1.14.99.3                Enzyme
NAME        heme oxygenase;
            ORP33 proteins;
            haem oxygenase;
            heme oxygenase (decyclizing);
            heme oxidase;
            haem oxidase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     heme,hydrogen-donor:oxygen oxidoreductase (alpha-methene-oxidizing,
            hydroxylating)
REACTION    heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
            [RN:R00311]
ALL_REAC    R00311;
            (other) R03683
SUBSTRATE   heme [CPD:C00032];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     biliverdin [CPD:C00500];
            Fe2+ [CPD:C14818];
            CO [CPD:C00237];
            A [CPD:C00028];
            H2O [CPD:C00001]
COFACTOR    NADH [CPD:C00004];
            NADPH [CPD:C00005]
INHIBITOR   Zinc protoporphyrin-9 [CPD:C03184]
COMMENT     Requires NAD(P)H and EC 1.6.2.4, NADPH---hemoprotein reductase. The
            terminal oxygen atoms that are incorporated into the carbonyl groups
            of pyrrole rings A and B of biliverdin are derived from two separate
            oxygen molecules [4]. The third oxygen molecule provides the oxygen
            atom that converts the alpha-carbon to CO. The central iron is kept
            in the reduced state by NAD(P)H.
REFERENCE   1  [PMID:18477]
  AUTHORS   Maines MD, Ibrahim NG, Kappas A.
  TITLE     Solubilization and partial purification of heme oxygenase from rat
            liver.
  JOURNAL   J. Biol. Chem. 252 (1977) 5900-3.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6897023]
  AUTHORS   Sunderman FW Jr, Downs JR, Reid MC, Bibeau LM.
  TITLE     Gas-chromatographic assay for heme oxygenase activity.
  JOURNAL   Clin. Chem. 28 (1982) 2026-32.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:4370250]
  AUTHORS   Yoshida T, Takahashi S, Kikuchi G.
  TITLE     Partial purification and reconstitution of the heme oxygenase system
            from pig spleen microsomes.
  JOURNAL   J. Biochem. (Tokyo). 75 (1974) 1187-91.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:105935]
  AUTHORS   Noguchi M, Yoshida T, Kikuchi G.
  TITLE     Specific requirement of NADPH-cytochrome c reductase for the
            microsomal heme oxygenase reaction yielding biliverdin IX alpha.
  JOURNAL   FEBS. Lett. 98 (1979) 281-4.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:12500973]
  AUTHORS   Lad L, Schuller DJ, Shimizu H, Friedman J, Li H, Ortiz de Montellano
            PR, Poulos TL.
  TITLE     Comparison of the heme-free and -bound crystal structures of human
            heme oxygenase-1.
  JOURNAL   J. Biol. Chem. 278 (2003) 7834-43.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K00510  heme oxygenase
GENES       HSA: 3162(HMOX1) 3163(HMOX2)
            PTR: 453880(HMOX2) 470195(HMOX1)
            MMU: 15368(Hmox1) 15369(Hmox2)
            RNO: 24451(Hmox1) 79239(Hmox2)
            CFA: 442987(HMOX1) 479864(HMOX2)
            SSC: 445512(HMOX1)
            GGA: 396287(HMOX1) 416663(HMOX2)
            XLA: 398965(MGC68771) 444101(MGC80397)
            DME: Dmel_CG14716(Ho)
            OSA: 4341462
            CME: CMH209C
            PIC: PICST_86063(HMX1)
            LPN: lpg0229
            LPF: lpl0282
            LPP: lpp0288
            MXA: MXAN_5679
            BRA: BRADO1626(hmuO)
            BBT: BBta_6429(hmuO)
            RPA: RPA1539
            RPB: RPB_3984
            RPC: RPC_1310
            RPD: RPD_3739
            RPE: RPE_1344
            GBE: GbCGDNIH1_0284
            CPE: CPE0214
            CPF: CPF_0205
            CPR: CPR_0203
            CTC: CTC02478
            CNO: NT01CX_0446
            MGI: Mflv_0990
            CGL: NCgl2146(cgl2227)
            CGB: cg2445(hmuO)
            CDI: DIP1669(hmuO)
            CJK: jk0320(hmuO)
            NFA: nfa24730
            RHA: RHA1_ro00883
            SCO: SCO2267(SCC75A.13)
            SMA: SAV5930(hmuO)
            LXX: Lxx24860(hmuO)
            CMI: CMM_0601(hemO)
            TFU: Tfu_2345
            LIL: LB186
            LIC: LIC20148(hol)
            LBJ: LBJ_4165
            LBL: LBL_4180
            SYN: sll1184(ho1) sll1875(ho2)
            SYW: SYNW0171(ho1)
            SYC: syc2236_c(ho1)
            SYF: Synpcc7942_1858
            SYD: Syncc9605_0166
            SYE: Syncc9902_0196
            SYG: sync_0216
            SYR: SynRCC307_0155(ho1)
            SYX: SynWH7803_0221(ho1)
            CYA: CYA_0408
            CYB: CYB_2435
            TEL: tll0365(ho1) tll1721(ho2)
            GVI: gll0410(ho1)
            ANA: all1897 alr3125
            AVA: Ava_3767 Ava_3827
            PMA: Pro1750(ho1)
            PMM: PMM1594(ho1)
            PMT: PMT1685(ho1)
            PMN: PMN2A_1169
            PMI: PMT9312_1686
            PMB: A9601_18031(ho1)
            PMC: P9515_17811(ho1)
            PMF: P9303_22411(ho1)
            PMG: P9301_17861(ho1)
            PME: NATL1_20441(ho1)
            TER: Tery_0335
            CHU: CHU_0149(bphO)
            GFO: GFO_1957
            AAE: aq_153(ctaA)
STRUCTURES  PDB: 1DVE  1DVG  1IRM  1IVJ  1IW0  1IW1  1IX3  1IX4  1J02  1J2C  
                 1J77  1N3U  1N45  1NI6  1OYK  1OYL  1OZE  1OZL  1OZR  1OZW  
                 1P3T  1P3U  1P3V  1S13  1S8C  1SK7  1T5P  1TWN  1TWR  1UBB  
                 1ULX  1V8X  1VGI  1WE1  1WNV  1WNW  1WNX  1WOV  1WOW  1WOX  
                 1WZD  1WZF  1WZG  1XJZ  1XK0  1XK1  1XK2  1XK3  2DY5  2E7E  
                 2Q32  2QPP  2Z68  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.3
            ExPASy - ENZYME nomenclature database: 1.14.99.3
            ExplorEnz - The Enzyme Database: 1.14.99.3
            ERGO genome analysis and discovery system: 1.14.99.3
            BRENDA, the Enzyme Database: 1.14.99.3
            CAS: 9059-22-7
///
ENTRY       EC 1.14.99.4                Enzyme
NAME        progesterone monooxygenase;
            progesterone hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     progesterone,hydrogen-donor:oxygen oxidoreductase (hydroxylating)
REACTION    progesterone + AH2 + O2 = testosterone acetate + A + H2O [RN:R02212]
ALL_REAC    R02212
SUBSTRATE   progesterone [CPD:C00410];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     testosterone acetate [CPD:C03027];
            A [CPD:C00028];
            H2O [CPD:C00001]
COMMENT     Has a wide specificity. A single enzyme from ascomycete the
            Neonectria radicicola (EC 1.14.13.54 ketosteroid monooxygenase)
            catalyses both this reaction and that catalysed by EC 1.14.99.12
            androst-4-ene-3,17-dione monooxygenase.
REFERENCE   1
  AUTHORS   Rahim, M.A. and Sih, C.J.
  TITLE     Mechanisms of steroid oxidation by microorganisms. XI. Enzymatic
            cleavage of the pregnane side chain.
  JOURNAL   J. Biol. Chem. 241 (1966) 3615-3623.
  ORGANISM  Cylindrocarpon radicicola, Cladosporium resinae
GENES       AFM: AFUA_8G00740
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.4
            ExPASy - ENZYME nomenclature database: 1.14.99.4
            ExplorEnz - The Enzyme Database: 1.14.99.4
            ERGO genome analysis and discovery system: 1.14.99.4
            BRENDA, the Enzyme Database: 1.14.99.4
            CAS: 37256-85-2
///
ENTRY       EC 1.14.99.5      Obsolete  Enzyme
NAME        Transferred to 1.14.19.1
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
COMMENT     Transferred entry: now EC 1.14.19.1 stearoyl-CoA 9-desaturase (EC
            1.14.99.5 created 1972, modified 1986, modified 2000, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.5
            ExPASy - ENZYME nomenclature database: 1.14.99.5
            ExplorEnz - The Enzyme Database: 1.14.99.5
            ERGO genome analysis and discovery system: 1.14.99.5
            BRENDA, the Enzyme Database: 1.14.99.5
///
ENTRY       EC 1.14.99.6      Obsolete  Enzyme
NAME        Transferred to 1.14.19.2
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
COMMENT     Transferred entry: now EC 1.14.19.2 acyl-[acyl-carrier-protein]
            desaturase (EC 1.14.99.6 created 1972, modified 2000, deleted 2000)
STRUCTURES  PDB: 1AFR  2J2F  2UW1  
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.6
            ExPASy - ENZYME nomenclature database: 1.14.99.6
            ExplorEnz - The Enzyme Database: 1.14.99.6
            ERGO genome analysis and discovery system: 1.14.99.6
            BRENDA, the Enzyme Database: 1.14.99.6
///
ENTRY       EC 1.14.99.7                Enzyme
NAME        squalene monooxygenase;
            squalene epoxidase;
            squalene-2,3-epoxide cyclase;
            squalene 2,3-oxidocyclase;
            squalene hydroxylase;
            squalene oxydocyclase;
            squalene-2,3-epoxidase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     squalene,hydrogen-donor:oxygen oxidoreductase (2,3-epoxidizing)
REACTION    squalene + AH2 + O2 = (S)-squalene-2,3-epoxide + A + H2O [RN:R02873]
ALL_REAC    R02873 > R02874
SUBSTRATE   squalene [CPD:C00751];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     (S)-squalene-2,3-epoxide [CPD:C01054];
            A [CPD:C00028];
            H2O [CPD:C00001]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). This enzyme, together with EC 5.4.99.7
            lanosterol synthase, was formerly known as squalene oxidocyclase.
REFERENCE   1  [PMID:5918046]
  AUTHORS   Cory EJ, Russey WE, Ortiz de Montellano PR.
  TITLE     2,3-oxidosqualene, an intermediate in the biological synthesis of
            sterols from squalene.
  JOURNAL   J. Am. Chem. Soc. 88 (1966) 4750-1.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Tchen, T.T. and Bloch, K.
  TITLE     On the conversion of squalene to lanosterol in vitro.
  JOURNAL   J. Biol. Chem. 226 (1957) 921-930.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:5918048]
  AUTHORS   Van Tamelen EE, Willett JD, Clayton RB, Lord KE.
  TITLE     Enzymic conversion of squalene 2,3-oxide to lanosterol and
            cholesterol.
  JOURNAL   J. Am. Chem. Soc. 88 (1966) 4752-4.
REFERENCE   4  [PMID:5438357]
  AUTHORS   Yamamoto S, Bloch K.
  TITLE     Studies on squalene epoxidase of rat liver.
  JOURNAL   J. Biol. Chem. 245 (1970) 1670-4.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00100  Biosynthesis of steroids
            PATH: map00900  Terpenoid biosynthesis
ORTHOLOGY   KO: K00511  squalene monooxygenase
GENES       HSA: 6713(SQLE)
            PTR: 464383(SQLE)
            MMU: 20775(Sqle)
            RNO: 29230(Sqle)
            CFA: 608021(SQLE)
            SPU: 584086(LOC584086) 591651(LOC591651)
            ATH: AT1G58440(XF1) AT5G24140(SQP2) AT5G24160
            OSA: 4332152 4332153
            CME: CMH256C
            SCE: YGR175C(ERG1)
            AGO: AGOS_AAL141C
            PIC: PICST_75910(ERG1)
            CGR: CAGL0D05940g
            SPO: SPBC713.12
            AFM: AFUA_5G07780
            AOR: AO090701000685
            CNE: CND06110
            UMA: UM02398.1
            DDI: DDBDRAFT_0192021
            TBR: Tb11.02.0780
            TCR: 509589.20
            LMA: LmjF13.1620
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.7
            ExPASy - ENZYME nomenclature database: 1.14.99.7
            ExplorEnz - The Enzyme Database: 1.14.99.7
            ERGO genome analysis and discovery system: 1.14.99.7
            BRENDA, the Enzyme Database: 1.14.99.7
            CAS: 9029-62-3
///
ENTRY       EC 1.14.99.8      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
COMMENT     Deleted entry: arene monooxygenase (epoxidizing). Now included with
            EC 1.14.14.1 unspecific monooxygenase (EC 1.14.99.8 created 1972,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.8
            ExPASy - ENZYME nomenclature database: 1.14.99.8
            ExplorEnz - The Enzyme Database: 1.14.99.8
            ERGO genome analysis and discovery system: 1.14.99.8
            BRENDA, the Enzyme Database: 1.14.99.8
///
ENTRY       EC 1.14.99.9                Enzyme
NAME        steroid 17alpha-monooxygenase;
            steroid 17alpha-hydroxylase;
            cytochrome P-45017alpha;
            cytochrome P-450 (P-45017alpha,lyase);
            17alpha-hydroxylase-C17,20 lyase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     steroid,hydrogen-donor:oxygen oxidoreductase (17alpha-hydroxylating)
REACTION    a steroid + AH2 + O2 = a 17alpha-hydroxysteroid + A + H2O
            [RN:R02131]
ALL_REAC    R02131 > R02211 R03783 R04852 R04853
SUBSTRATE   steroid [CPD:C00377];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     17alpha-hydroxysteroid [CPD:C03336];
            A [CPD:C00028];
            H2O [CPD:C00001]
COFACTOR    NADH [CPD:C00004];
            NADPH [CPD:C00005];
            Heme [CPD:C00032]
COMMENT     Requires NAD(P)H and P-450.
REFERENCE   1  [PMID:13549484]
  AUTHORS   LYNN WS Jr, BROWN RH.
  TITLE     The conversion of progesterone to androgens by testes.
  JOURNAL   J. Biol. Chem. 232 (1958) 1015-30.
  ORGANISM  guinea pig, rat [GN:rno]
REFERENCE   2  [PMID:6966286]
  AUTHORS   Yoshida KI, Oshima H, Troen P.
  TITLE     Studies of the human testis. XIII. Properties of nicotinamide
            adenine dinucleotide (reduced form)-linked 17 alpha-hydroxylation.
  JOURNAL   J. Clin. Endocrinol. Metab. 50 (1980) 895-9.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00140  C21-Steroid hormone metabolism
ORTHOLOGY   KO: K00512  cytochrome P450, family 17, subfamily A (steroid
                        17alpha-monooxygenase)
GENES       HSA: 1586(CYP17A1)
            PTR: 450141(CYP17A1)
            MMU: 13074(Cyp17a1)
            RNO: 25146(Cyp17a1)
            CFA: 477807(LOC477807)
            BTA: 281739(CYP17)
            SSC: 403330(CYP17A1)
            GGA: 425056(CYP17A1)
            DRE: 399692(cyp17a1)
            SPU: 585029(LOC585029)
            AFM: AFUA_1G11390
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.9
            ExPASy - ENZYME nomenclature database: 1.14.99.9
            ExplorEnz - The Enzyme Database: 1.14.99.9
            ERGO genome analysis and discovery system: 1.14.99.9
            BRENDA, the Enzyme Database: 1.14.99.9
            CAS: 9029-67-8
///
ENTRY       EC 1.14.99.10               Enzyme
NAME        steroid 21-monooxygenase;
            steroid 21-hydroxylase;
            21-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     steroid,hydrogen-donor:oxygen oxidoreductase (21-hydroxylating)
REACTION    a steroid + AH2 + O2 = a 21-hydroxysteroid + A + H2O [RN:R02130]
ALL_REAC    R02130 > R02213 R02838 R03326 R03784 R03849 R04675
SUBSTRATE   steroid [CPD:C00377];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     21-hydroxysteroid [CPD:C02506];
            A [CPD:C00028];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032];
            Flavin [CPD:C00176]
COMMENT     An enzyme system involving a heme-thiolate protein (P-450) and
            flavoprotein.
REFERENCE   1
  AUTHORS   Hayano, M. and Dorfman, R.I.
  TITLE     The action of adrenal homogenates on progesterone,
            17-hydroxyprogesterone and 21-desoxycortisone.
  JOURNAL   Arch. Biochem. Biophys. 36 (1952) 237-239.
REFERENCE   2  [PMID:13031650]
  AUTHORS   PLAGER JE, SAMUELS LT.
  TITLE     Synthesis of C14-17-hydroxy-11-desoxycorticosterone and
            17-hydroxycorticosterone by fractionated extracts of adrenal
            homogenates.
  JOURNAL   Arch. Biochem. Biophys. 42 (1953) 477-8.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:13416221]
  AUTHORS   RYAN KJ, ENGEL LL.
  TITLE     Hydroxylation of steroids at carbon 21.
  JOURNAL   J. Biol. Chem. 225 (1957) 103-14.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00140  C21-Steroid hormone metabolism
ORTHOLOGY   KO: K00513  cytochrome P450, family 21, subfamily A (steroid
                        21-monooxygenase)
GENES       HSA: 1589(CYP21A2)
            PTR: 471972(CYP21A2)
            MMU: 13079(Cyp21a1)
            RNO: 24298(Cyp21a1)
            CFA: 415124(CYP21A)
            BTA: 281741(CYP21) 282425(CYP21A2)
            SSC: 403337(SBAB-514B12.1)
            XLA: 447267(MGC86342)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.10
            ExPASy - ENZYME nomenclature database: 1.14.99.10
            ExplorEnz - The Enzyme Database: 1.14.99.10
            ERGO genome analysis and discovery system: 1.14.99.10
            BRENDA, the Enzyme Database: 1.14.99.10
            CAS: 9029-68-9
///
ENTRY       EC 1.14.99.11               Enzyme
NAME        estradiol 6beta-monooxygenase;
            estradiol 6beta-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     estradiol-17beta,hydrogen-donor:oxygen oxidoreductase
            (6beta-hydroxylating)
REACTION    estradiol-17beta + AH2 + O2 = 6beta-hydroxyestradiol-17beta + A +
            H2O [RN:R03086]
ALL_REAC    R03086
SUBSTRATE   estradiol-17beta [CPD:C00951];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     6beta-hydroxyestradiol-17beta [CPD:C03935];
            A [CPD:C00028];
            H2O [CPD:C00001]
REFERENCE   1
  AUTHORS   Haines, W.J.
  TITLE     The biosynthesis of adrenal cortex hormones.
  JOURNAL   Recent Progr. Hormone Res. 7 (1952) 255-305.
REFERENCE   2
  AUTHORS   Mueller, G.C. and Rumney, G.
  TITLE     Formation of 6beta-hydroxy and 6-keto derivatives of
            estradiol-16-C14 by mouse liver microsomes.
  JOURNAL   J. Am. Chem. Soc. 79 (1957) 1004-1005.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map00150  Androgen and estrogen metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.11
            ExPASy - ENZYME nomenclature database: 1.14.99.11
            ExplorEnz - The Enzyme Database: 1.14.99.11
            ERGO genome analysis and discovery system: 1.14.99.11
            BRENDA, the Enzyme Database: 1.14.99.11
            CAS: 9029-70-3
///
ENTRY       EC 1.14.99.12               Enzyme
NAME        androst-4-ene-3,17-dione monooxygenase;
            androstene-3,17-dione hydroxylase;
            androst-4-ene-3,17-dione 17-oxidoreductase;
            androst-4-ene-3,17-dione hydroxylase;
            androstenedione monooxygenase;
            4-androstene-3,17-dione monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     androst-4-ene-3,17-dione-hydrogen-donor:oxygen oxidoreductase
            (13-hydroxylating, lactonizing)
REACTION    androst-4-ene-3,17-dione + AH2 + O2 =
            3-oxo-13,17-secoandrost-4-ene-17,13alpha-lactone + A + H2O
            [RN:R01833]
ALL_REAC    R01833
SUBSTRATE   androst-4-ene-3,17-dione [CPD:C00280];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     3-oxo-13,17-secoandrost-4-ene-17,13alpha-lactone [CPD:C04676];
            A [CPD:C00028];
            H2O [CPD:C00001]
COMMENT     Has a wide specificity. A single enzyme from the ascomycete
            Neonectria radicicola (EC 1.14.13.54 ketosteroid monooxygenase)
            catalyses both this reaction and that catalysed by EC 1.4.99.4
            aralkylamine dehydrogenase.
REFERENCE   1
  AUTHORS   Prairie, R.L. and Talalay, P.
  TITLE     Enzymatic formation of testololactone.
  JOURNAL   Biochemistry 2 (1963) 203-208.
  ORGANISM  Penicillium lilacinum
PATHWAY     PATH: map00150  Androgen and estrogen metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.12
            ExPASy - ENZYME nomenclature database: 1.14.99.12
            ExplorEnz - The Enzyme Database: 1.14.99.12
            ERGO genome analysis and discovery system: 1.14.99.12
            BRENDA, the Enzyme Database: 1.14.99.12
            CAS: 37256-74-9
///
ENTRY       EC 1.14.99.13     Obsolete  Enzyme
NAME        Transferred to 1.14.13.23
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
COMMENT     Transferred entry: now EC 1.14.13.23 3-hydroxybenzoate
            4-monooxygenase (EC 1.14.99.13 created 1972, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.13
            ExPASy - ENZYME nomenclature database: 1.14.99.13
            ExplorEnz - The Enzyme Database: 1.14.99.13
            ERGO genome analysis and discovery system: 1.14.99.13
            BRENDA, the Enzyme Database: 1.14.99.13
///
ENTRY       EC 1.14.99.14               Enzyme
NAME        progesterone 11alpha-monooxygenase;
            progesterone 11alpha-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     progesterone,hydrogen-donor:oxygen oxidoreductase
            (11alpha-hydroxylating)
REACTION    progesterone + AH2 + O2 = 11alpha-hydroxyprogesterone + A + H2O
            [RN:R02214]
ALL_REAC    R02214
SUBSTRATE   progesterone [CPD:C00410];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     11alpha-hydroxyprogesterone [CPD:C03747];
            A [CPD:C00028];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:5417182]
  AUTHORS   Shibahara M, Moody JA, Smith LL.
  TITLE     Microbial hydroxylations. V. 11-alpha-hydroxylation of progesterone
            by cell-free preparations of Aspergillus ochraceus.
  JOURNAL   Biochim. Biophys. Acta. 202 (1970) 172-9.
  ORGANISM  Aspergillus ochraceus
PATHWAY     PATH: map00140  C21-Steroid hormone metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.14
            ExPASy - ENZYME nomenclature database: 1.14.99.14
            ExplorEnz - The Enzyme Database: 1.14.99.14
            ERGO genome analysis and discovery system: 1.14.99.14
            BRENDA, the Enzyme Database: 1.14.99.14
            CAS: 37256-77-2
///
ENTRY       EC 1.14.99.15               Enzyme
NAME        4-methoxybenzoate monooxygenase (O-demethylating);
            4-methoxybenzoate 4-monooxygenase (O-demethylating);
            4-methoxybenzoate O-demethylase;
            p-anisic O-demethylase;
            piperonylate-4-O-demethylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     4-methoxybenzoate,hydrogen-donor:oxygen oxidoreductase
            (O-demethylating)
REACTION    4-methoxybenzoate + AH2 + O2 = 4-hydroxybenzoate + formaldehyde + A
            + H2O [RN:R01306]
ALL_REAC    R01306
SUBSTRATE   4-methoxybenzoate [CPD:C02519];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     4-hydroxybenzoate [CPD:C00156];
            formaldehyde [CPD:C00067];
            A [CPD:C00028];
            H2O [CPD:C00001]
COMMENT     The bacterial enzyme consists of a ferredoxin-type protein and an
            iron-sulfur flavoprotein (FMN). Also acts on 4-ethoxybenzoate,
            N-methyl-4-aminobenzoate and toluate. The fungal enzyme acts best on
            veratrate.
REFERENCE   1  [PMID:188654]
  AUTHORS   Bernhardt FH, Nastainczyk W, Seydewitz V.
  TITLE     Kinetic studies on a 4-methoxybenzoate O-demethylase from
            Pseudomonas putida.
  JOURNAL   Eur. J. Biochem. 72 (1977) 107-15.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2  [PMID:25369]
  AUTHORS   Paszczynski A, Trojanowski J.
  TITLE     An affinity-column procedure for the purification of veratrate
            O-demethylase from fungi.
  JOURNAL   Microbios. 18 (1977) 111-21.
  ORGANISM  Chaetomium piluliferum, Xerocomus badius
REFERENCE   3  [PMID:6273164]
  AUTHORS   Twilfer H, Bernhardt FH, Gersonde K.
  TITLE     An electron-spin-resonance study on the redox-active centers of the
            4-methoxybenzoate monooxygenase from Pseudomonas putida.
  JOURNAL   Eur. J. Biochem. 119 (1981) 595-602.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.15
            ExPASy - ENZYME nomenclature database: 1.14.99.15
            ExplorEnz - The Enzyme Database: 1.14.99.15
            ERGO genome analysis and discovery system: 1.14.99.15
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.99.15
            BRENDA, the Enzyme Database: 1.14.99.15
            CAS: 37256-78-3
///
ENTRY       EC 1.14.99.16     Obsolete  Enzyme
NAME        Transferred to 1.14.13.72
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
COMMENT     Transferred entry: now EC 1.14.13.72, methylsterol monooxygenase (EC
            1.14.99.16 created 1972, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.16
            ExPASy - ENZYME nomenclature database: 1.14.99.16
            ExplorEnz - The Enzyme Database: 1.14.99.16
            ERGO genome analysis and discovery system: 1.14.99.16
            BRENDA, the Enzyme Database: 1.14.99.16
///
ENTRY       EC 1.14.99.17     Obsolete  Enzyme
NAME        Transferred to 1.14.16.5
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
COMMENT     Transferred entry: now EC 1.14.16.5 glyceryl-ether monooxygenase (EC
            1.14.99.17 created 1972, deleted 1976)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.17
            ExPASy - ENZYME nomenclature database: 1.14.99.17
            ExplorEnz - The Enzyme Database: 1.14.99.17
            ERGO genome analysis and discovery system: 1.14.99.17
            BRENDA, the Enzyme Database: 1.14.99.17
///
ENTRY       EC 1.14.99.18     Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
COMMENT     Deleted entry: CMP-N-acetylneuraminate monooxygenase. (EC 1.14.99.18
            created 1976, modified 1999, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.18
            ExPASy - ENZYME nomenclature database: 1.14.99.18
            ExplorEnz - The Enzyme Database: 1.14.99.18
            ERGO genome analysis and discovery system: 1.14.99.18
            BRENDA, the Enzyme Database: 1.14.99.18
///
ENTRY       EC 1.14.99.19               Enzyme
NAME        plasmanylethanolamine desaturase;
            alkylacylglycerophosphoethanolamine desaturase;
            alkylacylglycero-phosphorylethanolamine dehydrogenase;
            dehydrogenase, alkyl-acylglycerophosphorylethanolamine;
            1-O-alkyl-2-acyl-sn-glycero-3-phosphorylethanolamine desaturase;
            1-O-alkyl 2-acyl-sn-glycero-3-phosphorylethanolamine desaturase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine,hydrogen-donor:oxy
            gen oxidoreductase
REACTION    O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine + AH2 + O2 =
            O-1-alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine + A + 2 H2O
            [RN:R04571]
ALL_REAC    R04571
SUBSTRATE   O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine [CPD:C04475];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     O-1-alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine [CPD:C04756];
            A [CPD:C00028];
            H2O [CPD:C00001]
COFACTOR    ATP [CPD:C00002];
            Manganese [CPD:C00034];
            Magnesium [CPD:C00305]
COMMENT     Requires NADPH or NADH. May involve cytochrome b5. Requires Mg2+ and
            ATP.
REFERENCE   1  [PMID:4144394]
  AUTHORS   Paltauf F, Holasek A.
  TITLE     Enzymatic synthesis of plasmalogens. Characterization of the
            1-O-alkyl-2-acyl-8n-glycero-3-phosphorylethanolamine desaturase from
            mucosa of hamster small intestine.
  JOURNAL   J. Biol. Chem. 248 (1973) 1609-15.
  ORGANISM  hamster
REFERENCE   2  [PMID:4403444]
  AUTHORS   Wykle RL, Blank ML, Malone B, Snyder F.
  TITLE     Evidence for a mixed function oxidase in the biosynthesis of
            ethanolamine plasmalogens from
            1-alkyl-2-acyl-sn-glycero-3-phosphorylethanolamine.
  JOURNAL   J. Biol. Chem. 247 (1972) 5442-7.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00565  Ether lipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.19
            ExPASy - ENZYME nomenclature database: 1.14.99.19
            ExplorEnz - The Enzyme Database: 1.14.99.19
            ERGO genome analysis and discovery system: 1.14.99.19
            BRENDA, the Enzyme Database: 1.14.99.19
            CAS: 39391-13-4
///
ENTRY       EC 1.14.99.20               Enzyme
NAME        phylloquinone monooxygenase (2,3-epoxidizing);
            phylloquinone epoxidase;
            vitamin K 2,3-epoxidase;
            vitamin K epoxidase;
            vitamin K1 epoxidase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     phylloquinone,hydrogen-donor:oxygen oxidoreductase (2,3-epoxidizing)
REACTION    phylloquinone + AH2 + O2 = 2,3-epoxyphylloquinone + A + H2O
            [RN:R03510]
ALL_REAC    R03510
SUBSTRATE   phylloquinone [CPD:C02059];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     2,3-epoxyphylloquinone [CPD:C05849];
            A [CPD:C00028];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:4155625]
  AUTHORS   Willingham AK, Matschiner JT.
  TITLE     Changes in phylloquinone epoxidase activity related to prothrombin
            synthesis and microsomal clotting activity in the rat.
  JOURNAL   Biochem. J. 140 (1974) 435-41.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.20
            ExPASy - ENZYME nomenclature database: 1.14.99.20
            ExplorEnz - The Enzyme Database: 1.14.99.20
            ERGO genome analysis and discovery system: 1.14.99.20
            BRENDA, the Enzyme Database: 1.14.99.20
            CAS: 54596-37-1
///
ENTRY       EC 1.14.99.21               Enzyme
NAME        Latia-luciferin monooxygenase (demethylating);
            luciferase (Latia luciferin);
            Latia luciferin monooxygenase (demethylating)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     Latia-luciferin,hydrogen-donor:oxygen oxidoreductase (demethylating)
REACTION    Latia luciferin + AH2 + 2 O2 = oxidized Latia luciferin + CO2 +
            formate + A + H2O + hnu [RN:R03907]
ALL_REAC    R03907
SUBSTRATE   Latia luciferin [CPD:C02293];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     oxidized Latia luciferin [CPD:C03527];
            CO2 [CPD:C00011];
            formate [CPD:C00058];
            A [CPD:C00028];
            H2O [CPD:C00001];
            hn [CPD:C00205]
COFACTOR    FAD [CPD:C00016];
            Flavoprotein [CPD:C06411]
COMMENT     A flavoprotein. Latia is a bioluminescent mollusc. The reaction
            possibly involves two enzymes, an oxygenase followed by a
            monooxygenase for the actual light-emitting step.
REFERENCE   1  [PMID:5650377]
  AUTHORS   Shimomura O, Johnson FH.
  TITLE     The structure of Latia luciferin.
  JOURNAL   Biochemistry. 7 (1968) 1734-8.
  ORGANISM  Latia neritoides
REFERENCE   2  [PMID:4506078]
  AUTHORS   Shimomura O, Johnson FH, Kohama Y.
  TITLE     Reactions involved in bioluminescence systems of limpet (Latia
            neritoides) and luminous bacteria.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 69 (1972) 2086-9.
  ORGANISM  Latia neritoides
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.21
            ExPASy - ENZYME nomenclature database: 1.14.99.21
            ExplorEnz - The Enzyme Database: 1.14.99.21
            ERGO genome analysis and discovery system: 1.14.99.21
            BRENDA, the Enzyme Database: 1.14.99.21
            CAS: 62213-54-1
///
ENTRY       EC 1.14.99.22               Enzyme
NAME        ecdysone 20-monooxygenase;
            alpha-ecdysone C-20 hydroxylase;
            ecdysone 20-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     Ecdysone,hydrogen-donor:oxygen oxidoreductase (20-hydroxylating)
REACTION    ecdysone + AH2 + O2 = 20-hydroxyecdysone + A + H2O [RN:R02374]
ALL_REAC    R02374
SUBSTRATE   ecdysone [CPD:C00477];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     20-hydroxyecdysone [CPD:C02633];
            A [CPD:C00028];
            H2O [CPD:C00001]
COMMENT     An enzyme from insect fat body or malpighian tubules involving a
            heme-thiolate protein (P-450). NADPH can act as ultimate hydrogen
            donor.
REFERENCE   1  [PMID:606249]
  AUTHORS   Johnson P, Rees HH.
  TITLE     The mechanism of C-20 hydroxylation of alpha-ecdysone in the desert
            locust, Schistocerca gregaria.
  JOURNAL   Biochem. J. 168 (1977) 513-20.
  ORGANISM  Schistocerca gregaria
REFERENCE   2  [PMID:5286]
  AUTHORS   Nigg HN, Svoboda JA, Thompson MJ, Dutky SR, Kaplanis JN, Robbins WE.
  TITLE     Ecdysome 20-hydroxylase from the midgut of the tobacco hornworm
            (Manduca sexta L.).
  JOURNAL   Experientia. 32 (1976) 438-9.
  ORGANISM  Manduca sexta
REFERENCE   3  [PMID:488526]
  AUTHORS   Smith SL, Bollenbacher WE, Cooper DY, Schleyer H, Wielgus JJ,
            Gilbert LI.
  TITLE     Ecdysone 20-monooxygenase: characterization of an insect cytochrome
            p-450 dependent steroid hydroxylase.
  JOURNAL   Mol. Cell. Endocrinol. 15 (1979) 111-33.
  ORGANISM  Manduca sexta
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.22
            ExPASy - ENZYME nomenclature database: 1.14.99.22
            ExplorEnz - The Enzyme Database: 1.14.99.22
            ERGO genome analysis and discovery system: 1.14.99.22
            BRENDA, the Enzyme Database: 1.14.99.22
            CAS: 55071-97-1
///
ENTRY       EC 1.14.99.23               Enzyme
NAME        3-hydroxybenzoate 2-monooxygenase;
            3-hydroxybenzoate 2-hydroxylase;
            3-HBA-2-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     3-hydroxybenzoate,hydrogen-donor:oxygen oxidoreductase
            (2-hydroxylating)
REACTION    3-hydroxybenzoate + AH2 + O2 = 2,3-dihydroxybenzoate + A + H2O
            [RN:R01508]
ALL_REAC    R01508
SUBSTRATE   3-hydroxybenzoate [CPD:C00587];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     2,3-dihydroxybenzoate [CPD:C00196];
            A [CPD:C00028];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:7054148]
  AUTHORS   Daumy GO, McColl AS.
  TITLE     Induction of 3-hydroxybenzoate 2-hydroxylase in a Pseudomonas
            testosteroni mutant.
  JOURNAL   J. Bacteriol. 149 (1982) 384-5.
  ORGANISM  Pseudomonas testosteroni
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.23
            ExPASy - ENZYME nomenclature database: 1.14.99.23
            ExplorEnz - The Enzyme Database: 1.14.99.23
            ERGO genome analysis and discovery system: 1.14.99.23
            BRENDA, the Enzyme Database: 1.14.99.23
            CAS: 73507-96-7
///
ENTRY       EC 1.14.99.24               Enzyme
NAME        steroid 9alpha-monooxygenase;
            steroid 9alpha-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     steroid,hydrogen-donor:oxygen oxidoreductase (9-epoxidizing)
REACTION    pregna-4,9(11)-diene-3,20-dione + AH2 + O2 =
            9,11alpha-epoxypregn-4-ene-3,20-dione + A + H2O [RN:R04392]
ALL_REAC    R04392
SUBSTRATE   pregna-4,9(11)-diene-3,20-dione [CPD:C04084];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     9,11alpha-epoxypregn-4-ene-3,20-dione [CPD:C04379];
            A [CPD:C00028];
            H2O [CPD:C00001]
COFACTOR    FMN [CPD:C00061];
            Iron-sulfur [CPD:C00824]
COMMENT     An enzyme system involving a flavoprotein (FMN) and two iron-sulfur
            proteins.
REFERENCE   1  [PMID:7173200]
  AUTHORS   Strijewski A.
  TITLE     The steroid-9 alpha-hydroxylation system from Nocardia species.
  JOURNAL   Eur. J. Biochem. 128 (1982) 125-35.
  ORGANISM  Nocardia sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.24
            ExPASy - ENZYME nomenclature database: 1.14.99.24
            ExplorEnz - The Enzyme Database: 1.14.99.24
            ERGO genome analysis and discovery system: 1.14.99.24
            BRENDA, the Enzyme Database: 1.14.99.24
            CAS: 82869-33-8
///
ENTRY       EC 1.14.99.25     Obsolete  Enzyme
NAME        Transferred to 1.14.19.3
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
COMMENT     Transferred entry: now EC 1.14.19.3 linoleoyl-CoA desaturase (EC
            1.14.99.25 created 1986, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.25
            ExPASy - ENZYME nomenclature database: 1.14.99.25
            ExplorEnz - The Enzyme Database: 1.14.99.25
            ERGO genome analysis and discovery system: 1.14.99.25
            BRENDA, the Enzyme Database: 1.14.99.25
///
ENTRY       EC 1.14.99.26               Enzyme
NAME        2-hydroxypyridine 5-monooxygenase;
            2-hydroxypyridine oxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     2-hydroxypyridine,hydrogen-donor:oxygen oxidoreductase
            (5-hydroxylating)
REACTION    2-hydroxypyridine + AH2 + O2 = 2,5-dihydroxypyridine + A + H2O
            [RN:R03206]
ALL_REAC    R03206
SUBSTRATE   2-hydroxypyridine [CPD:C02502];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     2,5-dihydroxypyridine [CPD:C01059];
            A [CPD:C00028];
            H2O [CPD:C00001]
COMMENT     Also oxidizes 2,5-dihydroxypyridine, but does not act on
            3-hydroxypyridine, 4-hydroxypyridine or 2,6-dihydroxypyridine.
REFERENCE   1
  AUTHORS   Sharma, M.L., Kaul, S.M. and Shukla, O.P.
  TITLE     Metabolism of 2-hydroxypyridine by Bacillus brevis (INA).
  JOURNAL   Biol. Membr. 9 (1984) 43-52.
  ORGANISM  Bacillus brevis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.26
            ExPASy - ENZYME nomenclature database: 1.14.99.26
            ExplorEnz - The Enzyme Database: 1.14.99.26
            ERGO genome analysis and discovery system: 1.14.99.26
            BRENDA, the Enzyme Database: 1.14.99.26
            CAS: 96779-45-2
///
ENTRY       EC 1.14.99.27               Enzyme
NAME        juglone 3-monooxygenase;
            juglone hydroxylase;
            naphthoquinone hydroxylase;
            naphthoquinone-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     5-hydroxy-1,4-naphthoquinone,hydrogen-donor:oxygen oxidoreductase
            (3-hydroxylating)
REACTION    5-hydroxy-1,4-naphthoquinone + AH2 + O2 =
            3,5-dihydroxy-1,4-naphthoquinone + A + H2O [RN:R04327]
ALL_REAC    R04327
SUBSTRATE   5-hydroxy-1,4-naphthoquinone [CPD:C03840];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     3,5-dihydroxy-1,4-naphthoquinone [CPD:C04110];
            A [CPD:C00028];
            H2O [CPD:C00001]
COMMENT     Also acts on 1,4-naphthoquinone, naphthazarin and
            2-chloro-1,4-naphthoquinone, but not on other related compounds.
REFERENCE   1  [PMID:4041238]
  AUTHORS   Rettenmaier H, Lingens F.
  TITLE     Purification and some properties of two isofunctional juglone
            hydroxylases from Pseudomonas putida J1.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 366 (1985) 637-46.
  ORGANISM  Pseudomonas putida [GN:ppu]
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.27
            ExPASy - ENZYME nomenclature database: 1.14.99.27
            ExplorEnz - The Enzyme Database: 1.14.99.27
            ERGO genome analysis and discovery system: 1.14.99.27
            BRENDA, the Enzyme Database: 1.14.99.27
            CAS: 98865-54-4
///
ENTRY       EC 1.14.99.28               Enzyme
NAME        linalool 8-monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     3,7-dimethylocta-1,6-dien-3-ol,hydrogen-donor:oxygen oxidoreductase
            (8-hydroxylating)
REACTION    3,7-dimethylocta-1,6-dien-3-ol + AH2 + O2 =
            (E)-3,7-dimethylocta-1,6-dien-3,8-diol + A + H2O [RN:R04366]
ALL_REAC    R04366
SUBSTRATE   3,7-dimethylocta-1,6-dien-3-ol [CPD:C03985];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     (E)-3,7-dimethylocta-1,6-diene-3,8-diol [CPD:C04433];
            A [CPD:C00028];
            H2O [CPD:C00001]
COFACTOR    Heme [CPD:C00032]
COMMENT     A heme-thiolate protein (P-450).
REFERENCE   1
  AUTHORS   Bhattacharyya, P.K., Samanta, T.B., Ullah, A.H.J. and Gunsalus, I.C.
  TITLE     Chemical probes into the active centre of a heme thiolate
            monoxygenase.
  JOURNAL   Proc. Indian Acad. Sci., Chem. Sci. 93 (1984) 1289-1304.
ORTHOLOGY   KO: K05525  linalool 8-monooxygenase
GENES       ACI: ACIAD1575(linC)
            BRA: BRADO1377 BRADO1445 BRADO1446 BRADO6084
            BBT: BBta_6659 BBta_6660 BBta_6721
            SAL: Sala_2865
            MSM: MSMEG_3524 MSMEG_3551
            MMC: Mmcs_2991
            MKM: Mkms_3035
            MJL: Mjls_3006
            RHA: RHA1_ro02355 RHA1_ro02510 RHA1_ro04667 RHA1_ro04679
            FAL: FRAAL2558 FRAAL3452 FRAAL4012 FRAAL4085 FRAAL4206
            SEN: SACE_3525 SACE_4143 SACE_4920
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.28
            ExPASy - ENZYME nomenclature database: 1.14.99.28
            ExplorEnz - The Enzyme Database: 1.14.99.28
            ERGO genome analysis and discovery system: 1.14.99.28
            BRENDA, the Enzyme Database: 1.14.99.28
            CAS: 95329-13-8
///
ENTRY       EC 1.14.99.29               Enzyme
NAME        deoxyhypusine monooxygenase;
            deoxyhypusine hydroxylase;
            deoxyhypusine dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     deoxyhypusine,hydrogen-donor:oxygen oxidoreductase (2-hydroxylating)
REACTION    protein N6-(4-aminobutyl)-L-lysine + AH2 + O2 = protein
            N6-[(R)-4-amino-2-hydroxybutyl]-L-lysine + A + H2O [RN:R04437]
ALL_REAC    R04437
SUBSTRATE   protein N6-(4-aminobutyl)-L-lysine [CPD:C07282];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     protein N6-[(R)-4-amino-2-hydroxybutyl]-L-lysine [CPD:C04679];
            A [CPD:C00028];
            H2O [CPD:C00001]
COMMENT     The enzyme catalyses the final step in the formation of the amino
            acid hypusine in the eukaryotic initiation factor 5A.
REFERENCE   1  [PMID:3949761]
  AUTHORS   Abbruzzese A, Park MH, Folk JE.
  TITLE     Deoxyhypusine hydroxylase from rat testis. Partial purification and
            characterization.
  JOURNAL   J. Biol. Chem. 261 (1986) 3085-9.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K06072  deoxyhypusine monooxygenase
GENES       HSA: 83475(DOHH)
            PTR: 455584(DOHH)
            MMU: 102115(Dohh)
            RNO: 314644(RGD1304783)
            CFA: 485060(DOHH)
            BTA: 526521(DOHH)
            GGA: 427066(RCJMB04_24i7)
            XLA: 447153(MGC85454)
            DRE: 321732(dohh)
            DME: Dmel_CG2245(l(3)s1921)
            CEL: C14A4.1(tag-242)
            ATH: AT3G58180
            SCE: YJR070C(LIA1)
            AGO: AGOS_AFR426C
            KLA: KLLA0B14080g
            DHA: DEHA0F24948g
            CAL: CaO19.2286
            CGR: CAGL0F00407g
            SPO: SPAC30C2.02
            ANI: AN7498.2
            AFM: AFUA_2G05490
            AOR: AO090001000660
            CNE: CNL05340
            UMA: UM00319.1
            ECU: ECU06_1490
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.29
            ExPASy - ENZYME nomenclature database: 1.14.99.29
            ExplorEnz - The Enzyme Database: 1.14.99.29
            ERGO genome analysis and discovery system: 1.14.99.29
            BRENDA, the Enzyme Database: 1.14.99.29
            CAS: 101920-83-6
///
ENTRY       EC 1.14.99.30               Enzyme
NAME        carotene 7,8-desaturase;
            zeta-carotene desaturase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     carotene,hydrogen-donor:oxygen oxidoreductase
REACTION    neurosporene + AH2 + O2 = lycopene + A + 2 H2O [RN:R04800]
ALL_REAC    R04800;
            (other) R04798 R04803 R06961 R07511
SUBSTRATE   neurosporene [CPD:C05431];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     lycopene [CPD:C05432];
            A [CPD:C00028];
            H2O [CPD:C00001]
COMMENT     Also acts on zeta-carotene twice to give lycopene and converts
            beta-zeacarotene to gamma-carotene, and pro-zeta-carotene to
            prolycopene (via double reaction)
REFERENCE   1  [PMID:8617254]
  AUTHORS   Albrecht M, Linden H, Sandmann G.
  TITLE     Biochemical characterization of purified zeta-carotene desaturase
            from Anabaena PCC 7120 after expression in Escherichia coli.
  JOURNAL   Eur. J. Biochem. 236 (1996) 115-20.
  ORGANISM  Anabaena sp.
PATHWAY     PATH: map00906  Carotenoid biosynthesis - General
ORTHOLOGY   KO: K00514  zeta-carotene desaturase
GENES       ATH: AT3G04870(ZDS)
            OSA: 4342680
            CME: CMT061C
            ABA: Acid345_1747
            SYN: slr0940(crtQ-2)
            SYW: SYNW2213(crtQ)
            SYC: syc2497_c(zds)
            SYF: Synpcc7942_1512
            SYD: Syncc9605_2356
            SYE: Syncc9902_0335
            SYG: sync_2568
            SYR: SynRCC307_0275(crtQ)
            SYX: SynWH7803_2224(crtQ)
            CYA: CYA_0668(zds)
            CYB: CYB_1060(zds)
            TEL: tll0337(crtQ)
            ANA: all2382(crtQ)
            AVA: Ava_0200
            PMA: Pro0136(crtQ)
            PMM: PMM0115(crtQ)
            PMT: PMT1968(crtQ)
            PMN: PMN2A_1484
            PMI: PMT9312_0118
            TER: Tery_3954
            CTE: CT1414
            CCH: Cag_1590
            CPH: Cpha266_0830
            PVI: Cvib_1233
            PLT: Plut_1415
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.30
            ExPASy - ENZYME nomenclature database: 1.14.99.30
            ExplorEnz - The Enzyme Database: 1.14.99.30
            ERGO genome analysis and discovery system: 1.14.99.30
            BRENDA, the Enzyme Database: 1.14.99.30
///
ENTRY       EC 1.14.99.31               Enzyme
NAME        myristoyl-CoA 11-(E) desaturase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     n-tetradecanoyl-CoA,NAD(P)H:O2 oxidoreductase [11-(E) desaturating]
REACTION    myristoyl-CoA + NAD(P)H + H+ + O2 = (E)-11-tetradecenoyl-CoA +
            NAD(P)+ + 2 H2O [RN:R05321 R07216]
ALL_REAC    R05321 R07216
SUBSTRATE   myristoyl-CoA [CPD:C02593];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (E)-11-tetradecenoyl-CoA [CPD:C06736];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     Involved in sex pheromone synthesis in the moth Spodoptera
            littoralis. (E)-11-Tetradecenoyl-CoA is formed by stereospecific
            removal of the pro-R H at C-11 and the pro-S H at C-12. EC
            1.14.99.32, myristoyl-CoA 11-(Z) desaturase, forms the Z isomer by
            stereospecific cleavage of pro-R H at C-11 and C-12.
REFERENCE   1
  AUTHORS   Navaro, I., Font, I., Fabrias, G. and Camps, F.
  TITLE     Stereospecificity of the (E)- and (Z)-11 myristoyl desaturases in
            the biosynthesis of Spodoptera littoralis sex pheromone.
  JOURNAL   J. Am. Chem. Soc. 119 (1997) 11335-11336.
  ORGANISM  Spodoptera littoralis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.31
            ExPASy - ENZYME nomenclature database: 1.14.99.31
            ExplorEnz - The Enzyme Database: 1.14.99.31
            ERGO genome analysis and discovery system: 1.14.99.31
            BRENDA, the Enzyme Database: 1.14.99.31
///
ENTRY       EC 1.14.99.32               Enzyme
NAME        myristoyl-CoA 11-(Z) desaturase;
            n-tetradecanoyl-CoA,NADPH:O2 oxidoreductase [11-(Z) desaturating]
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     n-tetradecanoyl-CoA,NAD(P)H:O2 oxidoreductase [11-(Z) desaturating]
REACTION    myristoyl-CoA + NAD(P)H + H+ + O2 = (Z)-11-tetradecenoyl-CoA +
            NAD(P)+ + 2 H2O [RN:R05322 R07217]
ALL_REAC    R05322 R07217
SUBSTRATE   myristoyl-CoA [CPD:C02593];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     (Z)-11-tetradecenoyl-CoA [CPD:C06737];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     Involved in sex pheromone synthesis in the moth Spodoptera
            littoralis. (Z)-11-Tetradecenoyl-CoA is formed by stereospecific
            removal of H from the pro-R positions at C-11 and C-12. EC
            1.14.99.31, myristoyl-CoA 11-(E) desaturase, forms the (E)-isomer by
            removing the pro-R H group at C-11 and the pro-S H group at C-12.
REFERENCE   1
  AUTHORS   Navaro, I., Font, I., Fabrias, G. and Camps, F.
  TITLE     Stereospecificity of the (E)- and (Z)-11 myristoyl desaturases in
            the biosynthesis of Spodoptera littoralis sex pheromone.
  JOURNAL   J. Am. Chem. Soc. 119 (1997) 11335-11336.
  ORGANISM  Spodoptera littoralis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.32
            ExPASy - ENZYME nomenclature database: 1.14.99.32
            ExplorEnz - The Enzyme Database: 1.14.99.32
            ERGO genome analysis and discovery system: 1.14.99.32
            BRENDA, the Enzyme Database: 1.14.99.32
///
ENTRY       EC 1.14.99.33               Enzyme
NAME        Delta12-fatty acid dehydrogenase;
            crepenynate synthase;
            linoleate Delta12-fatty acid acetylenase (desaturase)
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     linoleate, hydrogen-donor:oxygen oxidoreductase
            (Delta12-unsaturating)
REACTION    linoleate + AH2 + O2 = crepenynate + A + H2O [RN:R05740]
ALL_REAC    R05740
SUBSTRATE   linoleate [CPD:C01595];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     crepenynate [CPD:C07289];
            A [CPD:C00028];
            H2O [CPD:C00001]
COMMENT     Contains non-heme iron.
REFERENCE   1
  AUTHORS   Banas, A., Bafor, M., Wiberg, E., Lenman, M., Staahl, U. and Stymne,
            S.
  TITLE     Biosynthesis of an acetylenic fatty acid in microsomal preparations
            from developing seeds Crepis alpina. Physiol. Biochem. Mol.
  JOURNAL   Biol. Plant. 12th (1997) 57-59.
REFERENCE   2  [PMID:9572738]
  AUTHORS   Lee M, Lenman M, Banas A, Bafor M, Singh S, Schweizer M, Nilsson R,
            Liljenberg C, Dahlqvist A, Gummeson PO, Sjodahl S, Green A, Stymne
            S.
  TITLE     Identification of non-heme diiron proteins that catalyze triple bond
            and epoxy group formation.
  JOURNAL   Science. 280 (1998) 915-8.
  ORGANISM  Arabidopsis thaliana [GN:ath]
PATHWAY     PATH: map00591  Linoleic acid metabolism
ORTHOLOGY   KO: K08262  delta12-fatty acid dehydrogenase
GENES       SYD: Syncc9605_1972
            PMN: PMN2A_0393
            PMI: PMT9312_1476
            PMB: A9601_15921
            PMC: P9515_15601
            PMF: P9303_21081
            PMG: P9301_15761
            PME: NATL1_10821
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.33
            ExPASy - ENZYME nomenclature database: 1.14.99.33
            ExplorEnz - The Enzyme Database: 1.14.99.33
            ERGO genome analysis and discovery system: 1.14.99.33
            BRENDA, the Enzyme Database: 1.14.99.33
///
ENTRY       EC 1.14.99.34               Enzyme
NAME        monoprenyl isoflavone epoxidase;
            monoprenyl isoflavone monooxygenase;
            7-O-methylluteone:O2 oxidoreductase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     7-O-methylluteone,NADPH:O2 oxidoreductase
REACTION    7-O-methylluteone + NADPH + H+ + O2 = dihydrofurano derivatives +
            NADP+ + H2O [RN:R05741]
ALL_REAC    R05741
SUBSTRATE   7-O-methylluteone [CPD:C07290];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     dihydrofurano derivative [CPD:C07291];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A flavoprotein (FAD) with high specificity for monoprenyl
            isoflavone. The product of the prenyl epoxidation reaction contains
            an oxygen atom derived from O2, but not from H2O. It is slowly and
            nonenzymically converted into the corresponding dihydrofurano
            derivative. The enzyme in the fungus Botrytis cinerea is induced by
            the substrate analogue, 6-prenylnaringenin.
REFERENCE   1
  AUTHORS   Tanaka, M. and Tahara, S.
  TITLE     FAD-dependent epoxidase as a key enzyme in fungal metabolism of
            prenylated flavonoids.
  JOURNAL   Phytochemistry 46 (1997) 433-439.
  ORGANISM  Botrytis cinerea
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.34
            ExPASy - ENZYME nomenclature database: 1.14.99.34
            ExplorEnz - The Enzyme Database: 1.14.99.34
            ERGO genome analysis and discovery system: 1.14.99.34
            BRENDA, the Enzyme Database: 1.14.99.34
///
ENTRY       EC 1.14.99.35               Enzyme
NAME        thiophene-2-carbonyl-CoA monooxygenase;
            thiophene-2-carboxyl-CoA dehydrogenase;
            thiophene-2-carboxyl-CoA hydroxylase;
            thiophene-2-carboxyl-CoA monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     thiophene-2-carbonyl-CoA, hydrogen-donor:oxygen oxidoreductase
REACTION    thiophene-2-carbonyl-CoA + AH2 + O2 =
            5-hydroxythiophene-2-carbonyl-CoA + A + H2O [RN:R05742]
ALL_REAC    R05742
SUBSTRATE   thiophene-2-carbonyl-CoA [CPD:C07347];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     5-hydroxythiophene-2-carbonyl-CoA [CPD:C07348];
            A [CPD:C00028];
            H2O [CPD:C00001]
COMMENT     A molybdenum enzyme. Highly specific for thiophene-2-carbonyl-CoA.
            Tetrazolium salts can act as electron acceptors.
REFERENCE   1  [PMID:9531630]
  AUTHORS   Bambauer A, Rainey FA, Stackebrandt E, Winter J.
  TITLE     Characterization of Aquamicrobium defluvii gen. nov. sp. nov., a
            thiophene-2-carboxylate-metabolizing bacterium from activated
            sludge.
  JOURNAL   Arch. Microbiol. 169 (1998) 293-302.
  ORGANISM  Aquamicrobium defluvii
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.35
            ExPASy - ENZYME nomenclature database: 1.14.99.35
            ExplorEnz - The Enzyme Database: 1.14.99.35
            ERGO genome analysis and discovery system: 1.14.99.35
            UM-BBD (Biocatalysis/Biodegradation Database): 1.14.99.35
            BRENDA, the Enzyme Database: 1.14.99.35
///
ENTRY       EC 1.14.99.36               Enzyme
NAME        beta-carotene 15,15'-monooxygenase;
            beta-carotene 15,15'-dioxygenase, carotene dioxygenase;
            carotene 15,15'-dioxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     beta-carotene:oxygen 15,15'-oxidoreductase (bond-cleaving)
REACTION    beta-carotene + O2 = 2 retinal [RN:R00032]
ALL_REAC    R00032
SUBSTRATE   beta-carotene [CPD:C02094];
            O2 [CPD:C00007]
PRODUCT     retinal [CPD:C00376]
COFACTOR    Iron [CPD:C00023];
            Bile salt [CPD:C01558]
COMMENT     Requires bile salts and Fe(II). The reaction proceeds in three
            stages, epoxidation of the 15,15'-double bond, hydration of the
            double bond leading to ring opening, and oxidative cleavage of the
            diol formed [cf. EC 1.14.15.6, cholesterol monooxygenase
            (side-chain-cleaving)]. Thus only one atom of the dioxygen is
            incorporated into retinal. Formerly in EC 1.13.11 as it had been
            thought to be a dioxygenase.
REFERENCE   1
  AUTHORS   Leuenberger, M.G., Engeloch-Jarret, C. and Woggon, W.D.
  TITLE     The reaction mechanism of the enzyme-catalysed central cleavage of
            beta-carotene to retinal.
  JOURNAL   Angew. Chem. 40 (2001) 2614-2616.
REFERENCE   2
  AUTHORS   Goodman, D.S., Huang, H.S., Kanai, M. and Shiratori, T.
  TITLE     The enzymatic conversion of all-trans beta-carotene into retinal.
  JOURNAL   J. Biol. Chem. 242 (1967) 3543-3554.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:5946623]
  AUTHORS   Goodman DS, Huang HS, Shiratori T.
  TITLE     Mechanism of the biosynthesis of vitamin A from beta-carotene.
  JOURNAL   J. Biol. Chem. 241 (1966) 1929-32.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00830  Retinol metabolism
ORTHOLOGY   KO: K00515  beta-carotene 15,15'-monooxygenase
GENES       HSA: 53630(BCMO1)
            PTR: 468043(BCMO1)
            MMU: 63857(Bcmo1)
            RNO: 114106(Bcmo1)
            CFA: 489695(BCMO1)
            BTA: 534696(BCMO1)
            GGA: 395346(BCMO1)
            DRE: 393580(zgc:63614) 84039(bcmo1)
            DME: Dmel_CG9347(ninaB)
            CEL: F53C3.12
            SYF: Synpcc7942_0196
            AVA: Ava_2047 Ava_2168 Ava_3710
            HWA: HQ2381A
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.36
            ExPASy - ENZYME nomenclature database: 1.14.99.36
            ExplorEnz - The Enzyme Database: 1.14.99.36
            ERGO genome analysis and discovery system: 1.14.99.36
            BRENDA, the Enzyme Database: 1.14.99.36
            CAS: 37256-60-3
///
ENTRY       EC 1.14.99.37               Enzyme
NAME        taxadiene 5alpha-hydroxylase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     taxa-4,11-diene,hydrogen-donor:oxygen oxidoreductase
            (5alpha-hydroxylating)
REACTION    taxa-4,11-diene + AH2 + O2 = taxa-4(20),11-dien-5alpha-ol + A + H2O
            [RN:R06306]
ALL_REAC    R06306
SUBSTRATE   taxa-4,11-diene [CPD:C11894];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     taxa-4(20),11-dien-5alpha-ol;
            A [CPD:C00028];
            H2O [CPD:C00001]
COMMENT     Requires P-450. The reaction includes rearrangement of the
            4(5)-double bond to a 4(20)-double bond, possibly through allylic
            oxidation.
REFERENCE   1  [PMID:8807878]
  AUTHORS   Hefner J, Rubenstein SM, Ketchum RE, Gibson DM, Williams RM, Croteau
            R.
  TITLE     Cytochrome P450-catalyzed hydroxylation of taxa-4(5),11(12)-diene to
            taxa-4(20),11(12)-dien-5alpha-ol: the first oxygenation step in
            taxol biosynthesis.
  JOURNAL   Chem. Biol. 3 (1996) 479-89.
  ORGANISM  Taxus sp.
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.37
            ExPASy - ENZYME nomenclature database: 1.14.99.37
            ExplorEnz - The Enzyme Database: 1.14.99.37
            ERGO genome analysis and discovery system: 1.14.99.37
            BRENDA, the Enzyme Database: 1.14.99.37
            CAS: 9035-51-2
///
ENTRY       EC 1.14.99.38               Enzyme
NAME        cholesterol 25-hydroxylase;
            cholesterol 25-monooxygenase
CLASS       Oxidoreductases;
            Acting on paired donors, with O2 as oxidant and incorporation or
            reduction of oxygen. The oxygen incorporated need not be derived
            from O2;
            Miscellaneous
SYSNAME     cholesterol,hydrogen-donor:oxygen oxidoreductase (25-hydroxylating)
REACTION    cholesterol + AH2 + O2 = 25-hydroxycholesterol + A + H2O [RN:R07218]
ALL_REAC    R07218
SUBSTRATE   cholesterol [CPD:C00187];
            AH2 [CPD:C00030];
            O2 [CPD:C00007]
PRODUCT     25-hydroxycholesterol [CPD:C15519];
            A [CPD:C00028];
            H2O [CPD:C00001]
COMMENT     Unlike most other sterol hydroxylases, this enzyme is not a
            cytochrome P-450. Instead, it uses diiron cofactors to catalyse the
            hydroxylation of hydrophobic substrates [1]. The diiron cofactor can
            be either Fe-O-Fe or Fe-OH-Fe and is bound to the enzyme through
            interactions with clustered histidine or glutamate residues [4,5].
            In cell cultures, this enzyme down-regulates cholesterol synthesis
            and the processing of sterol regulatory element binding proteins
            (SREBPs).
REFERENCE   1  [PMID:9852097]
  AUTHORS   Lund EG, Kerr TA, Sakai J, Li WP, Russell DW.
  TITLE     cDNA cloning of mouse and human cholesterol 25-hydroxylases,
            polytopic membrane proteins that synthesize a potent oxysterol
            regulator of lipid metabolism.
  JOURNAL   J. Biol. Chem. 273 (1998) 34316-27.
  ORGANISM  mouse [GN:mmu], human [GN:hsa]
REFERENCE   2  [PMID:11967195]
  AUTHORS   Chen JJ, Lukyanenko Y, Hutson JC.
  TITLE     25-hydroxycholesterol is produced by testicular macrophages during
            the early postnatal period and influences differentiation of Leydig
            cells in vitro.
  JOURNAL   Biol. Reprod. 66 (2002) 1336-41.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:12390873]
  AUTHORS   Lukyanenko Y, Chen JJ, Hutson JC.
  TITLE     Testosterone regulates 25-hydroxycholesterol production in
            testicular macrophages.
  JOURNAL   Biol. Reprod. 67 (2002) 1435-8.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:7947683]
  AUTHORS   Fox BG, Shanklin J, Ai J, Loehr TM, Sanders-Loehr J.
  TITLE     Resonance Raman evidence for an Fe-O-Fe center in stearoyl-ACP
            desaturase. Primary sequence identity with other diiron-oxo
            proteins.
  JOURNAL   Biochemistry. 33 (1994) 12776-86.
REFERENCE   5  [PMID:12543708]
  AUTHORS   Russell DW.
  TITLE     The enzymes, regulation, and genetics of bile acid synthesis.
  JOURNAL   Annu. Rev. Biochem. 72 (2003) 137-74.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K10223  cholesterol 25-hydroxylase
GENES       HSA: 9023(CH25H)
            MMU: 12642(Ch25h)
            RNO: 309527(Ch25h)
DBLINKS     IUBMB Enzyme Nomenclature: 1.14.99.38
            ExPASy - ENZYME nomenclature database: 1.14.99.38
            ExplorEnz - The Enzyme Database: 1.14.99.38
            ERGO genome analysis and discovery system: 1.14.99.38
            BRENDA, the Enzyme Database: 1.14.99.38
///
ENTRY       EC 1.14.99.-                Enzyme
CLASS       Oxidoreductases;
            Acting on paired donors with incorporation of molecular oxygen;
            Miscellaneous
REACTION    (1) 4-Hydroxybenzoate + Acceptor + H2O <=> 4-Hydroxybenzaldehyde +
            Reduced acceptor + Oxygen [RN:R01303];
            (2) 3beta-Hydroxyandrost-5-en-17-one + H+ + Oxygen + NADPH <=>
            16alpha-Hydroxydehydroepiandrosterone + NADP+ + H2O [RN:R03408];
            (3) Phytoene <=> Phytofluene + Hydrogen [RN:R04786];
            (4) Phytofluene <=> zeta-Carotene + Hydrogen [RN:R04787];
            (5) 1,1,1-Trichloro-2,2-bis(4-chlorophenyl)ethane + Oxygen <=>
            cis-2,3-Dihydrodiol 1,1,1-Trichloro-2,2-bis(4'-chlorophenyl)ethane
            [RN:R05492];
            (6) 15-cis-Phytoene <=> 9,9'-Di-cis-zeta-carotene + 2 Hydrogen
            [RN:R07510];
            (7) 1'-Hydroxy-gamma-carotene <=> 1'-Hydroxytorulene [RN:R07517];
            (8) Lycopene <=> 3,4-Dehydrolycopene + Hydrogen [RN:R07518];
            (9) Rhodopin <=> 3,4-Dehydrorhodopin + 2 Hydrogen [RN:R07520];
            (10) Rhodovibrin <=> Hydroxyspirilloxanthin + Hydrogen [RN:R07523];
            (11) Chloroxanthin <=> Demethylspheroidene + Hydrogen [RN:R07534];
            (12) Dehydrosqualene <=> 4,4'-Diaponeurosporene [RN:R07653];
            (13) 1,6-Naphthalenedisulfonic acid + Oxygen + 2 H+ <=>
            1,2-Dihydroxynaphthalene-6-sulfonate + HSO3- [RN:R07682];
            (14) 2,6-Naphthalenedisulfonic acid + Oxygen + 2 H+ <=>
            1,2-Dihydroxynaphthalene-6-sulfonate + HSO3- [RN:R07683];
            (15) 1-Naphthalenesulfonic acid + Oxygen + 2 H+ <=>
            Naphthalene-1,2-diol + HSO3- [RN:R07698];
            (16) 2-Naphthalenesulfonic acid + Oxygen + 2 H+ <=>
            Naphthalene-1,2-diol + HSO3- [RN:R07699]
SUBSTRATE   Oxygen [CPD:C00007];
            6-Hydroxynicotinate [CPD:C01020];
            4-Hydroxybenzoate [CPD:C00156];
            Acceptor [CPD:C00028];
            H2O [CPD:C00001];
            Estrone [CPD:C00468];
            Formate [CPD:C00058];
            NADP+ [CPD:C00006];
            Estradiol-17beta [CPD:C00951];
            3beta-Hydroxyandrost-5-en-17-one [CPD:C01227];
            H+ [CPD:C00080];
            NADPH [CPD:C00005];
            1,1,1-Trichloro-2,2-bis(4-chlorophenyl)ethane [CPD:C04623]
PRODUCT     2,5-Dihydroxypyridine [CPD:C01059];
            CO2 [CPD:C00011];
            4-Hydroxybenzaldehyde [CPD:C00633];
            Reduced acceptor [CPD:C00030];
            Oxygen [CPD:C00007];
            19-Oxoandrost-4-ene-3,17-dione [CPD:C05297];
            H+ [CPD:C00080];
            NADPH [CPD:C00005];
            19-Oxotestosterone [CPD:C05295];
            16alpha-Hydroxydehydroepiandrosterone [CPD:C05139];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            cis-2,3-Dihydrodiol 1,1,1-Trichloro-2,2-bis(4'-chlorophenyl)ethane
            [CPD:C06649]
///
ENTRY       EC 1.14.-.-                 Enzyme
CLASS       Oxidoreductases;
            Acting on paired donors with incorporation of molecular oxygen
REACTION    (1) Ascorbate <=> Monodehydroascorbate + H+ [RN:R00645];
            (2) 3,4',5-Trihydroxystilbene <=> 3,3',4'5-Tetrahydroxystilbene
            [RN:R04257];
            (3) 4-Nitrocatechol + Oxygen + 3 H+ <=> Benzene-1,2,4-triol +
            Nitrite + H2O [RN:R05265];
            (4) 2 4-Chlorophenoxyacetate + Oxygen <=> 2 4-Chlorophenol + 2
            Glyoxylate [RN:R05493];
            (5) Fluorene + Oxygen + 2 H+ + 2 e- <=> Fluoren-9-ol + H2O
            [RN:R05494];
            (6) alpha-Pinene + Reduced acceptor <=> Myrtenol + H2O + Acceptor
            [RN:R06401];
            (7) alpha-Pinene + Oxygen + H+ <=> Pinocarveol + H2O [RN:R06404];
            (8) Dihydroceramide + Reduced acceptor + Oxygen <=>
            N-Acylsphingosine + Acceptor + 2 H2O [RN:R06519];
            (9) Indole + NADPH + H+ + Oxygen <=> Indolin-2-one + NADP+ + H2O
            [RN:R07403];
            (10) Indolin-2-one + NADPH + H+ + Oxygen <=> 3-Hydroxyindolin-2-one
            + NADP+ + H2O [RN:R07421];
            (11) 3-Hydroxyindolin-2-one + NADPH + H+ + Oxygen <=> HBOA + NADP+ +
            H2O [RN:R07422];
            (12) HBOA + NADPH + H+ + Oxygen <=> DIBOA + NADP+ + H2O [RN:R07423];
            (13) Cathasterone + Oxygen + Reduced acceptor <=> Teasterone + H2O +
            Acceptor [RN:R07431];
            (14) Teasterone <=> 3-Dehydroteasterone [RN:R07444];
            (15) 6-Deoxocathasterone + Oxygen <=> 6-Deoxoteasterone + H2O
            [RN:R07448];
            (16) 6-Deoxoteasterone <=> 3-Dehydro-6-deoxoteasterone [RN:R07449];
            (17) 6-Deoxocastasterone + Oxygen <=> 6alpha-Hydroxy-castasterone +
            H2O [RN:R07450];
            (18) 6-Deoxoteasterone + Oxygen <=> Teasterone + H2O [RN:R07455];
            (19) 3-Dehydro-6-deoxoteasterone + Oxygen <=> 3-Dehydroteasterone +
            H2O [RN:R07457];
            (20) 6-Deoxotyphasterol + Oxygen <=> Typhasterol + H2O [RN:R07458];
            (21) Campestanol + Oxygen + Reduced acceptor <=>
            6alpha-Hydroxycampestanol + H2O + Acceptor [RN:R07467];
            (22) Typhasterol + Oxygen + Reduced acceptor <=> Castasterone + H2O
            + Acceptor [RN:R07470];
            (23) Anthracene + 2 H2O <=> Anthracene-9,10-dihydrodiol [RN:R07687];
            (24) Phenylboronic acid + Oxygen <=> Phenol + H2O [RN:R07697];
            (25) Aniline + Oxygen + 2 H+ <=> Catechol + NH3 [RN:R07700];
            (26) Nitrobenzene + Oxygen + 2 H+ <=> Catechol + Nitrite
            [RN:R07706];
            (27) 4-Chloroaniline + Oxygen + 2 H+ <=> 4-Chlorocatechol + NH3
            [RN:R07793];
            (28) Fluoren-9-one + Oxygen + 2 H+ <=>
            1-Hydro-1,1a-dihydroxy-9-fluorenone [RN:R07799]
SUBSTRATE   Ascorbate [CPD:C00072];
            3,4',5-Trihydroxystilbene [CPD:C03582];
            4-Nitrocatechol [CPD:C02235];
            Oxygen [CPD:C00007];
            H+ [CPD:C00080];
            4-Chlorophenoxyacetate [CPD:C07088];
            Fluorene [CPD:C07715];
            e- [CPD:C05359];
            alpha-Pinene [CPD:C09880];
            Reduced acceptor [CPD:C00030];
            Dihydroceramide [CPD:C12126];
            Indole [CPD:C00463];
            NADPH [CPD:C00005];
            Indolin-2-one [CPD:C12312];
            3-Hydroxyindolin-2-one [CPD:C11130];
            HBOA [CPD:C15769]
PRODUCT     Monodehydroascorbate [CPD:C01041];
            H+ [CPD:C00080];
            3,3',4'5-Tetrahydroxystilbene [CPD:C05901];
            Benzene-1,2,4-triol [CPD:C02814];
            Nitrite [CPD:C00088];
            H2O [CPD:C00001];
            4-Chlorophenol [CPD:C02124];
            Glyoxylate [CPD:C00048];
            Fluoren-9-ol [CPD:C06711];
            Myrtenol [CPD:C11938];
            Acceptor [CPD:C00028];
            Pinocarveol [CPD:C11941];
            N-Acylsphingosine [CPD:C00195];
            Indolin-2-one [CPD:C12312];
            NADP+ [CPD:C00006];
            3-Hydroxyindolin-2-one [CPD:C11130];
            HBOA [CPD:C15769];
            DIBOA [CPD:C15770]
///
ENTRY       EC 1.15.1.1                 Enzyme
NAME        superoxide dismutase;
            superoxidase dismutase;
            copper-zinc superoxide dismutase;
            Cu-Zn superoxide dismutase;
            ferrisuperoxide dismutase;
            superoxide dismutase I;
            superoxide dismutase II;
            SOD;
            Cu,Zn-SOD;
            Mn-SOD;
            Fe-SOD;
            SODF;
            SODS;
            SOD-1;
            SOD-2;
            SOD-3;
            SOD-4;
            hemocuprein;
            erythrocuprein;
            cytocuprein;
            cuprein ;
            hepatocuprein
CLASS       Oxidoreductases;
            Acting on superoxide as acceptor;
            Acting on superoxide as acceptor (only sub-subclass identified to
            date)
SYSNAME     superoxide:superoxide oxidoreductase
REACTION    2 O2.- + 2 H+ = O2 + H2O2 [RN:R00275]
ALL_REAC    R00275
SUBSTRATE   O2.- [CPD:C00704];
            H+ [CPD:C00080]
PRODUCT     O2 [CPD:C00007];
            H2O2 [CPD:C00027]
COFACTOR    Iron [CPD:C00023];
            Manganese [CPD:C00034];
            Zinc [CPD:C00038];
            Copper [CPD:C00070]
COMMENT     A metalloprotein; also known as erythrocuprein, hemocuprein or
            cytocuprein. Enzymes from most eukaryotes contain both copper and
            zinc; those from mitochondria and most prokaryotes contain manganese
            or iron.
REFERENCE   1  [PMID:4324341]
  AUTHORS   Keele BB Jr, McCord JM, Fridovich I.
  TITLE     Further characterization of bovine superoxide dismutase and its
            isolation from bovine heart.
  JOURNAL   J. Biol. Chem. 246 (1971) 2875-80.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:4337330]
  AUTHORS   Sawada Y, Oyama T, Yamazaki I.
  TITLE     Preparation and physicochemical properties of green pea superoxide
            dismutase.
  JOURNAL   Biochim. Biophys. Acta. 268 (1972) 305-12.
  ORGANISM  Pisum sativum, Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4559499]
  AUTHORS   Vance PG, Keele BB Jr, Rajagopalan KV.
  TITLE     Superoxide dismutase from Streptococcus mutans. Isolation and
            characterization of two forms of the enzyme.
  JOURNAL   J. Biol. Chem. 247 (1972) 4782-6.
  ORGANISM  Streptococcus mutans [GN:smu]
PATHWAY     PATH: map01510  Neurodegenerative Disorders
            PATH: map05030  Amyotrophic lateral sclerosis (ALS)
ORTHOLOGY   KO: K00518  superoxide dismutase
            KO: K04564  superoxide dismutase, Fe-Mn family
            KO: K04565  Cu/Zn superoxide dismutase
GENES       HSA: 6647(SOD1) 6648(SOD2) 6649(SOD3)
            MMU: 20655(Sod1) 20656(Sod2) 20657(Sod3)
            RNO: 24786(Sod1) 24787(Sod2) 25352(Sod3)
            CFA: 403559(SOD1) 476258(SOD2) 488855(SOD3)
            BTA: 281495(SOD1) 281496(SOD2)
            GGA: 374042(SOD2) 395938(SOD1) 422810(SOD3)
            XLA: 394274(sod1-a) 444203(MGC80739)
            XTR: 448200(sod2) 496429(ccs)
            DRE: 30553(sod1) 335799(sod2)
            SPU: 579361(LOC579361) 580111(LOC580111) 586977(LOC586977)
            DME: Dmel_CG11793(Sod) Dmel_CG17753(CCS) Dmel_CG5948
                 Dmel_CG8582(Sh3beta) Dmel_CG8905(Sod2)
            CEL: C08A9.1(sod-3) F10D11.1(sod-2) F55H2.1(sod-4) ZK430.3(sod-5)
            ATH: AT1G08830(CSD1) AT2G28190(CSD2) AT3G56350 AT5G18100(CSD3)
            OSA: 4332082 4332846 4338417 4339922 4344210 4346329
            CME: CMN023C CMR158C
            SCE: YHR008C(SOD2) YJR104C(SOD1)
            AGO: AGOS_ADR160W AGOS_AGL321W
            PIC: PICST_34151(SOD3.2) PICST_41302(SOD2.1) PICST_63831(SOD3.1)
                 PICST_87011(SOD4.2) PICST_89018(SOD1)
            CGR: CAGL0A02387g CAGL0C04741g CAGL0E04356g
            SPO: SPAC1486.01 SPAC821.10c(sod1)
            ANI: AN0241.2 AN0785.2 AN5577.2
            AFM: AFUA_1G14550 AFUA_4G11580 AFUA_5G09240 AFUA_6G07210
            AOR: AO090003001062 AO090020000521
            CNE: CND01490 CNI01590
            UMA: UM02453.1 UM03085.1
            ECU: ECU11_1080
            DDI: DDBDRAFT_0188850 DDBDRAFT_0202901 DDBDRAFT_0205599
                 DDB_0191290(sodA) DDB_0232182(sodD)
            PFA: PF08_0071 PFF1130c
            CHO: Chro.50049
            TAN: TA16635 TA17190
            TPV: TP01_1156 TP04_0025
            TET: TTHERM_00313620 TTHERM_00357070 TTHERM_00357080
                 TTHERM_00655520
            TBR: Tb11.01.6660 Tb11.01.7480 Tb11.01.7550 Tb927.5.3350
                 Tb927.6.4030
            TCR: 506819.30 507039.10 507061.30 508445.20 509775.40 511019.90
                 511521.30 511545.120 511715.10 511735.60 511737.3
            LMA: LmjF08.0290 LmjF30.2770 LmjF32.1820 LmjF32.1830 LmjF32.2630
            EHI: 384.t00003
            ECO: b1646(sodC) b1656(sodB) b3908(sodA)
            ECJ: JW1638(sodC) JW1648(sodB) JW3879(sodA)
            ECE: Z2347 Z2661(sodC) Z2678(sodB) Z3312 Z5453(sodA)
            ECS: ECs1120 ECs1989 ECs2355 ECs2365 ECs4834
            ECC: c2038(sodC) c2050(sodB) c4859(sodA)
            ECI: UTI89_C1837(sodC) UTI89_C1847(sodB) UTI89_C4491(sodA)
            ECP: ECP_1592 ECP_1601 ECP_4118
            ECV: APECO1_2560(sodA) APECO1_728(sodC) APECO1_736(sodB)
            ECW: EcE24377A_1857(sodC) EcE24377A_1869(sodB)
                 EcE24377A_4440(sodA)
            ECX: EcHS_A1723(sodC) EcHS_A1735(sodB) EcHS_A4138(sodA)
            STY: STY1682(sodC) STY1691(sodB) STY3816(sodA)
            STT: t1299(sodB) t1308(sodC) t3564(sodA)
            SPT: SPA1413(sodC) SPA1422(sodB) SPA3898(sodA)
            SEC: SC0997(sodC) SC1450(sodB) SC1459(sodC) SC3946(sodA)
            STM: STM0924 STM1044(sodC) STM1431(sodB) STM1440(sodC)
                 STM4055(sodA)
            YPE: YPO2386(sodB) YPO3375(sodC) YPO4061(sodA)
            YPK: y0815(sodC) y1951(sodB) y4080(sodA)
            YPM: YP_0311(sodC) YP_2172(sodB) YP_3972(sodA)
            YPA: YPA_1731 YPA_2873 YPA_3024
            YPN: YPN_0717 YPN_1840 YPN_3708
            YPP: YPDSF_0032 YPDSF_0761 YPDSF_2984
            YPS: YPTB0756(sodC) YPTB2299(sodB) YPTB3925(sodA)
            YPI: YpsIP31758_1756(sodB) YpsIP31758_3315(sodC)
                 YpsIP31758_4121(sodA)
            YEN: YE0752(sodC)
            SFL: SF1673(sodC) SF1684(sodB) SF3985(sodA)
            SFX: S1805(sodC) S1816(sodB) S3763(sodA)
            SFV: SFV_1666(sodC) SFV_1678(sodB) SFV_3587(sodA)
            SSN: SSON_1500(sodB) SSON_1510(sodC) SSON_4078(sodA)
            SBO: SBO_1475(sodB) SBO_1489(sodC) SBO_3926(sodA)
            SDY: SDY_1870(sodC) SDY_1882(sodB) SDY_3838(sodA)
            ECA: ECA0092(sodA) ECA2211
            PLU: plu0075(sodA)
            BUC: BU189(sodA)
            BAS: BUsg183(sodA)
            BAB: bbp178(sodA)
            WBR: WGLp595(sodA)
            SGL: SG0017
            ENT: Ent638_1791 Ent638_1801 Ent638_4063
            SPE: Spro_0081 Spro_2196 Spro_2210
            BFL: Bfl022(sodA)
            BPN: BPEN_021(sodA)
            HIN: HI1088(sodA)
            HIT: NTHI1251(sodA)
            HDU: HD0321(sodA) HD0848(sodC)
            HSO: HS_0464(sodA)
            PMU: PM0001(sodA) PM1952(sodC)
            MSU: MS0389(sodA) MS1704(sodC)
            APL: APL_0004(sodC) APL_0251(sodA)
            ASU: Asuc_0668 Asuc_0800
            XFA: XF1921 XF2614
            XFT: PD0870(sodA) PD1988(sodM)
            XCC: XCC0190(yojM) XCC0191(sodC2) XCC0395(sodM) XCC2278(sodM)
                 XCC2501(sodB)
            XCB: XC_0200 XC_0201 XC_0407 XC_1615 XC_1837
            XCV: XCV0193(sodC1) XCV0194(sodC2) XCV2583(sodM) XCV2827(sodB)
            XAC: XAC0209(yojM) XAC0210(sodC2) XAC2386(sodM) XAC2677(sodB)
            XOO: XOO2712(sodM) XOO2828(sodM) XOO3208(sodB) XOO4481(sodC2)
                 XOO4482(yojM)
            XOM: XOO_2557(XOO2557) XOO_2684(XOO2684) XOO_3041(XOO3041)
                 XOO_4222(XOO4222) XOO_4223(XOO4223)
            VCH: VC1583 VC2045 VC2694
            VCO: VC0395_A1186(sodC) VC0395_A1632(sodB) VC0395_A2266(sodA)
            VVU: VV1_1252 VV1_3107 VV2_1471
            VVY: VV1178 VV3115 VVA0291
            VPA: VP2118 VP2860 VPA1514
            VFI: VF0921
            PPR: PBPRA2569 PBPRA2578(sodB)
            PAE: PA4366(sodB) PA4468(sodM)
            PAU: PA14_56780(sodB) PA14_58000(sodM)
            PAP: PSPA7_5082
            PPU: PP_0915(sodB) PP_0946(sodA)
            PPF: Pput_0954 Pput_0985
            PST: PSPTO_1338(sodC) PSPTO_4363(sodB) PSPTO_4459(sodA)
            PSB: Psyr_1154 Psyr_4059 Psyr_4152
            PSP: PSPPH_1224(sodC) PSPPH_4064(sodB) PSPPH_4156(sodA)
            PFL: PFL_0909 PFL_4826
            PFO: Pfl_0851 Pfl_4486
            PEN: PSEEN1087(sodM) PSEEN1121(sodB)
            PMY: Pmen_3322
            PAR: Psyc_1938(sodB)
            PCR: Pcryo_1900 Pcryo_2231
            PRW: PsycPRwf_0309
            ACI: ACIAD1070(sodM) ACIAD1346(sodB) ACIAD2072(sodM)
            ACB: A1S_3143
            SON: SO_2881(sodB)
            SDN: Sden_1639
            SFR: Sfri_1747
            SAZ: Sama_1920
            SBL: Sbal_1782
            SBM: Shew185_1775
            SLO: Shew_1834
            SPC: Sputcn32_1687
            SSE: Ssed_2445
            SPL: Spea_1963
            SHE: Shewmr4_1572 Shewmr4_2024
            SHM: Shewmr7_1647 Shewmr7_1951
            SHN: Shewana3_1639 Shewana3_2125 Shewana3_4364
            SHW: Sputw3181_2338 Sputw3181_3778
            ILO: IL0798(sodA) IL1805(sodB)
            CPS: CPS_3476(sodB)
            PHA: PSHAa1215(sodB)
            PAT: Patl_1395 Patl_2297
            SDE: Sde_0885
            PIN: Ping_2448
            MAQ: Maqu_2023 Maqu_2653
            CBU: CBU_1708(sodB) CBU_1822(sodC)
            CBD: COXBU7E912_0298(sodB)
            LPN: lpg2348(sodC) lpg2967(sodB)
            LPF: lpl2270(sodC) lpl2897(sodB)
            LPP: lpp2297(sodC) lpp3039(sodB)
            MCA: MCA2067(sodB-1) MCA2458(sodB-2)
            FTU: FTT0068(sodB) FTT0879(sodC)
            FTF: FTF0068(sodB) FTF0879(sodC)
            FTW: FTW_0144(sodB) FTW_1301(sodC)
            FTL: FTL_0380 FTL_1791
            FTH: FTH_0373(sodC) FTH_1728(sodB)
            FTA: FTA_1898
            FTN: FTN_0405(sodC) FTN_1642(sodB)
            TCX: Tcr_0237
            NOC: Noc_2428
            AEH: Mlg_1103
            HHA: Hhal_2155
            HCH: HCH_04606
            CSA: Csal_0397 Csal_1861 Csal_3260
            ABO: ABO_0649(sodB)
            MMW: Mmwyl1_2180
            AHA: AHA_0515 AHA_1403
            DNO: DNO_1348
            BCI: BCI_0483(sodA)
            NME: NMB0884 NMB1398
            NMA: NMA1104(sodB) NMA1617(sodC)
            NMC: NMC0825(sodB) NMC1339(sodC)
            CVI: CV_0867(sodB2) CV_2504(sodB1)
            RSO: RSc2368(sodC) RSc2526(sodB)
            REU: Reut_A0597 Reut_B4338
            REH: H16_A0610(sodA) H16_B1110
            RME: Rmet_0539 Rmet_2757 Rmet_6201
            BMA: BMA0713(sodC) BMA2271(sodB)
            BMV: BMASAVP1_A0566(sodB)
            BML: BMA10299_A1043(sodB)
            BMN: BMA10247_2148(sodB)
            BXE: Bxe_A0769 Bxe_A3479
            BVI: Bcep1808_2636
            BUR: Bcep18194_A5765 Bcep18194_A5874
            BCN: Bcen_1931
            BCH: Bcen2424_2434 Bcen2424_2543
            BAM: Bamb_2481 Bamb_2591
            BPS: BPSL0880(sodB) BPSL1001
            BPM: BURPS1710b_1085(sodB) BURPS1710b_1214(sodC)
            BPL: BURPS1106A_0933(sodB) BURPS1106A_1062(sodC)
            BPD: BURPS668_0930(sodB) BURPS668_1056(sodC)
            BTE: BTH_I0744 BTH_I0859
            PNU: Pnuc_1385
            BPE: BP0193(sodA) BP2067 BP2761(sodB)
            BPA: BPP0767(sodA) BPP1751 BPP2567(sodB)
            BBR: BB0852(sodA) BB2012(sodB) BB3357
            RFR: Rfer_3151
            POL: Bpro_2945 Bpro_3554
            PNA: Pnap_1927
            AAV: Aave_2568 Aave_2662 Aave_4523
            AJS: Ajs_2301
            VEI: Veis_4889
            MPT: Mpe_A2481
            HAR: HEAR0840(sodC) HEAR2498(sodB)
            MMS: mma_1690(sodC) mma_2589(sodB)
            NEU: NE0870(sodB)
            NET: Neut_1204
            NMU: Nmul_A0501
            EBA: ebA5077(sodB)
            AZO: azo0522(sodC) azo1466
            DAR: Daro_2943 Daro_3212
            TBD: Tbd_0659 Tbd_0906 Tbd_1015 Tbd_2256
            MFA: Mfla_0386
            HPY: HP0389(sodB)
            HPJ: jhp0992(sodF)
            HPA: HPAG1_1003
            HHE: HH1832(sodF)
            HAC: Hac_0419(sodB)
            WSU: WS1585(sodB) WS1846
            TDN: Tmden_1129
            CJE: Cj0169(sodB)
            CJR: CJE0164(sodB)
            CJJ: CJJ81176_0205(sodB)
            CJU: C8J_0165(sodB)
            CJD: JJD26997_0184(sodB)
            CFF: CFF8240_0032 CFF8240_1330(sodC)
            CCV: CCV52592_1312
            CHA: CHAB381_0365
            CCO: CCC13826_0328
            ABU: Abu_1576(sodB)
            GSU: GSU1158(sodA)
            GME: Gmet_2410
            PPD: Ppro_1133
            DVU: DVU2410(sodB)
            DVL: Dvul_0204 Dvul_0822
            DDE: Dde_0882
            LIP: LI0005(sodC)
            BBA: Bd0295(sodC) Bd1401(sodC) Bd2407(sodB) Bd3617(sodB)
            DPS: DP0316
            ADE: Adeh_1952
            MXA: MXAN_4826(sodB) MXAN_5862(sodC)
            SAT: SYN_03202
            SFU: Sfum_1767 Sfum_3417 Sfum_3449
            RPR: RP535(sodB)
            RTY: RT0523(sodB)
            RCO: RC0778(sodB)
            RFE: RF_0741(sodB)
            RBE: RBE_1195(sodB)
            OTS: OTBS_1489(sodB)
            WOL: WD0738(sodB)
            WBM: Wbm0220(sodA)
            AMA: AM816(sodB)
            APH: APH_0371(sodB)
            ERU: Erum5270(sodB)
            ERW: ERWE_CDS_05530(sodB)
            ERG: ERGA_CDS_05420(sodB)
            ECN: Ecaj_0535
            ECH: ECH_0493(sodB)
            NSE: NSE_0843(sodB)
            MLO: mlr7636
            MES: Meso_0861 Meso_3220
            PLA: Plav_0187
            SME: SMc00043(sodB) SMc02597(sodC)
            SMD: Smed_0587
            ATU: Atu0876(sodF) Atu4583(sodB) Atu4726(sodB)
            ATC: AGR_C_1601 AGR_L_313 AGR_L_579
            RET: RHE_CH01203(sodB) RHE_CH01400(sodC)
            RLE: RL1340(sodB) RL1521(sodC)
            BME: BMEI1367 BMEII0581
            BMF: BAB1_0591 BAB2_0535(sodC)
            BMS: BR0566 BRA0703(sodC)
            BMB: BruAb1_0588 BruAb2_0527(sodC)
            BOV: BOV_0349 BOV_A0659(sodC)
            OAN: Oant_0434 Oant_2701 Oant_3827
            BJA: bll7559(chrC) bll7774(sodF)
            BRA: BRADO6273(sodB)
            BBT: BBta_1335(sodB)
            RPA: RPA0225(sodC) RPA1693(sodB)
            RPB: RPB_0607 RPB_1677
            RPC: RPC_0485 RPC_3738
            RPD: RPD_0488 RPD_3621
            RPE: RPE_0191 RPE_3840
            NWI: Nwi_0913 Nwi_2796
            NHA: Nham_3432 Nham_3597
            BHE: BH04630(sodB) BH08570(sodC)
            BQU: BQ03820(sodB)
            BBK: BARBAKC583_0420(sodB)
            XAU: Xaut_3319
            CCR: CC_1579 CC_1777 CC_3557
            SIL: SPO2340(sodB)
            SIT: TM1040_0976
            RSP: RSP_1796(sodC) RSP_2693
            RSH: Rsph17029_1350
            RSQ: Rsph17025_1871
            JAN: Jann_2189
            RDE: RD1_1772(sodB)
            PDE: Pden_0518 Pden_1634
            MMR: Mmar10_1895
            HNE: HNE_0696(sodB) HNE_1624(sodA)
            ZMO: ZMO1060(sod)
            NAR: Saro_0483 Saro_3135
            SAL: Sala_0291 Sala_0817
            SWI: Swit_2933 Swit_3164
            ELI: ELI_10235 ELI_13945
            GOX: GOX1800 GOX1879
            GBE: GbCGDNIH1_0954
            ACR: Acry_1181
            RRU: Rru_A1760 Rru_A1782
            MAG: amb2511 amb2978
            ABA: Acid345_3693
            SUS: Acid_0141 Acid_1072
            BSU: BG11676(sodA) BG12676(sodF) BG13565(yojM)
            BHA: BH1409(sodA) BH1563
            BAN: BA1489 BA4499(sodA-1) BA5139(sodC) BA5696(sodA-2)
            BAR: GBAA1489 GBAA4499(sodA-1) GBAA5139(sodC) GBAA5696(sodA-2)
            BAA: BA_0013(sodC) BA_0554 BA_2012 BA_4946
            BAT: BAS1378 BAS4177 BAS4777 BAS5300
            BCE: BC1468 BC4272 BC4907 BC5445
            BCA: BCE_1593 BCE_4355(sodA) BCE_5046(sodC) BCE_5579(sodA)
            BCZ: BCZK1350(sodF) BCZK4025(sodA) BCZK4639(sodC) BCZK5142(sodA)
            BCY: Bcer98_1192 Bcer98_3003 Bcer98_3962
            BTK: BT9727_1351(sodF) BT9727_4015(sodA) BT9727_4617(sodC)
                 BT9727_5127(sodA)
            BTL: BALH_1324(sodF) BALH_3868(sodA) BALH_4448(sodC)
                 BALH_4954(sodA)
            BLI: BL00582(sodF) BL01449 BL03706(sodA)
            BLD: BLi02254(sodF) BLi02263(yojM) BLi02679(sodA)
            BCL: ABC1715(sodA) ABC1819(sodF) ABC3174 ABC3387
            BAY: RBAM_019080(sodF) RBAM_023340(sodA)
            BPU: BPUM_1859(sodF) BPUM_1865(yojM) BPUM_2230(sodA)
            OIH: OB1932 OB2339 OB3080
            GKA: GK2288 GK2457 GK2932
            SAU: SA0128(sodM) SA1382(sodA)
            SAV: SAV0133(sodM) SAV1553(sodA)
            SAM: MW0107(sodM) MW1505(sodA)
            SAR: SAR0135(sodM) SAR1630(sodA)
            SAS: SAS0107 SAS1491
            SAC: SACOL0118(sodA1) SACOL1610(sodA2)
            SAB: SAB0072(sodM) SAB1425c(sodA)
            SAA: SAUSA300_0135 SAUSA300_1513
            SAO: SAOUHSC_00093 SAOUHSC_01653
            SAJ: SaurJH9_0119 SaurJH9_1611
            SAH: SaurJH1_0124 SaurJH1_1645
            SEP: SE1240
            SER: SERP1119(sodA)
            SHA: SH1363(sodA)
            SSP: SSP1203
            LMO: lmo1439(sod)
            LMF: LMOf2365_1458(sod)
            LIN: lin1478(sod)
            LWE: lwe1456(sod)
            LLA: L12227(sodA)
            LLC: LACR_0458
            LLM: llmg_0429(sodA)
            SPY: SPy_1406(sodA)
            SPZ: M5005_Spy_1145(sodA)
            SPM: spyM18_1414(sodA)
            SPG: SpyM3_1071(sodM)
            SPS: SPs0792
            SPH: MGAS10270_Spy1216(sodA)
            SPI: MGAS10750_Spy1252(sodA)
            SPJ: MGAS2096_Spy1211(sodA)
            SPK: MGAS9429_Spy1192(sodA)
            SPF: SpyM50714(sodA)
            SPA: M6_Spy1120
            SPB: M28_Spy1139(sodA)
            SPN: SP_0766
            SPR: spr0674(sodA)
            SPD: SPD_0667(sodA)
            SAG: SAG0788(sodA)
            SAN: gbs0808(sod)
            SAK: SAK_0913(sodA)
            SMU: SMU.629(sod)
            STC: str0720(sodA)
            STL: stu0720(sodA)
            SSA: SSA_0721(sodA)
            SGO: SGO_1599(sodA)
            LSA: LSA0896(sodA)
            LCA: LSEI_1848
            EFA: EF0463(sodA)
            STH: STH1047 STH205
            CAC: CAC1363(sodC) CAC2567
            CPE: CPE1236(sod)
            CPF: CPF_1446(sodF)
            CPR: CPR_1251(sodF)
            CTC: CTC00158 CTC00590
            CNO: NT01CX_0194 NT01CX_1771 NT01CX_1993
            CTH: Cthe_3008
            CDF: CD0827(rbo) CD1631(sodA)
            CBO: CBO0521 CBO3333
            CBA: CLB_2221(sodF)
            CBH: CLC_2204(sodF)
            CBF: CLI_2331(sodF)
            CBE: Cbei_1507 Cbei_1856
            CKL: CKL_0419(sodC) CKL_2771(sod) CKL_3432(sodA)
            AMT: Amet_1897
            DSY: DSY1477 DSY4123
            DRM: Dred_1239
            SWO: Swol_1711
            TTE: TTE0857(sodA)
            MTA: Moth_1285 Moth_1916
            POY: PAM442(sodA)
            AYW: AYWB_326(sodA)
            MTU: Rv0432(sodC) Rv3846(sodA)
            MTC: MT0447(sodC) MT3960(sodM)
            MBO: Mb0440(sodC) Mb3876(sodA)
            MBB: BCG_0471(sodC) BCG_3909(sodA)
            MLE: ML0072(sodA) ML1925(sodC)
            MPA: MAP0187c(sodA) MAP3921(sodC)
            MAV: MAV_0182 MAV_2043 MAV_4362(sodC) MAV_4722(sodC)
            MSM: MSMEG_0835(sodC) MSMEG_6427 MSMEG_6636
            MMC: Mmcs_0572 Mmcs_5044
            MKM: Mkms_5132
            MJL: Mjls_5423
            CGL: NCgl2826(cgl2927)
            CGB: cg3237(sod)
            CEF: CE2250 CE2765(sodA)
            CDI: DIP2261(sodA) DIP2319
            CJK: jk0112(sodA)
            NFA: nfa1210(sodF) nfa52980(sodC)
            RHA: RHA1_ro02173 RHA1_ro04009(sodA)
            SCO: SCO0999(2SCG2.12c) SCO2633(SC8E4A.03) SCO5254(2SC7G11.16c)
            SMA: SAV5413(sodF)
            TWH: TWT299(sodA)
            TWS: TW473(sodA)
            LXX: Lxx11510(sodA)
            ART: Arth_2086
            AAU: AAur_2087(sodA)
            PAC: PPA1818
            NCA: Noca_1725
            TFU: Tfu_0957
            FRA: Francci3_2817
            FAL: FRAAL4337(sodF)
            ACE: Acel_0566
            KRA: Krad_3578
            SEN: SACE_0619(sodF) SACE_5364(sodF) SACE_6419(sodN)
            STP: Strop_3697
            RXY: Rxyl_2920
            RBA: RB6688(sodA)
            CTR: CT294(sodM)
            CTA: CTA_0316(sodM)
            CMU: TC0567
            CPN: CPn0057(sodM)
            CPA: CP0718
            CPJ: CPj0057(sodM)
            CPT: CpB0058
            CCA: CCA00345(sod)
            CAB: CAB337
            CFE: CF0661(sodM)
            PCU: pc0270(sodM) pc1759(sodC)
            BBU: BB0153(sodA)
            BGA: BG0151(sodA)
            BAF: BAPKO_0154(sodA)
            SYN: slr1516(sodB)
            SYC: syc0737_c(sodB)
            SYF: Synpcc7942_0801
            SYD: Syncc9605_1507
            SYE: Syncc9902_0982
            SYG: sync_0755(sodN) sync_1771(sodC)
            SYR: SynRCC307_0325(sodC) SynRCC307_1791(sodB)
            SYX: SynWH7803_0951(sodC) SynWH7803_1742(sodB)
            CYA: CYA_2858(sodB)
            CYB: CYB_2514(sodB)
            TEL: tll1519(sodB) tlr0036(sodB)
            GVI: gll0682(sodB) glr4327(sodB)
            ANA: all0070(sodA) alr2938(sodB)
            AVA: Ava_0963 Ava_1445
            PMB: A9601_14931
            PMC: P9515_14551
            PMF: P9303_19731
            PMG: P9301_14791
            PME: NATL1_17141
            TER: Tery_4533
            BTH: BT_0655
            BFR: BF2527
            BFS: BF2556(sodB)
            PGI: PG1545(sodB)
            SRU: SRU_1724
            CHU: CHU_0108(sodA)
            GFO: GFO_1020 GFO_3377(sodA)
            FJO: Fjoh_1129 Fjoh_2595
            FPS: FP0160(sodA) FP0608 FP1736(sodC)
            CTE: CT1211(sodB)
            CCH: Cag_0967
            CPH: Cpha266_0983
            PVI: Cvib_0978
            PLT: Plut_1224
            DET: DET0956(sod)
            DEH: cbdb_A912(sodA)
            RRS: RoseRS_3237
            RCA: Rcas_3725
            DRA: DR_1279 DR_1546 DR_A0202
            DGE: Dgeo_0830
            TTH: TTC0189
            TTJ: TTHA0557
            AAE: aq_1050(sodC1) aq_1499(sodA) aq_238(sodC2)
            MAC: MA1574(sodB) MA2422(sodC)
            MBA: Mbar_A2345 Mbar_A3589
            MMA: MM_2423
            MTP: Mthe_0685
            MHU: Mhun_2974
            MLA: Mlab_0412
            MEM: Memar_1705
            MBN: Mboo_1503 Mboo_1715
            HAL: VNG1190G(sod1) VNG1332G(sod2)
            HMA: rrnAC0831(sodA)
            HWA: HQ2461A(sod)
            NPH: NP4040A(sod)
            TAC: Ta0013
            TVO: TVN0061
            PTO: PTO0480
            RCI: LRC161(sodC)
            APE: APE_0741
            SSO: SSO0316(sod)
            STO: ST2283
            SAI: Saci_0195(sodF)
            MSE: Msed_1889
            PAI: PAE0274(sod)
            PIS: Pisl_2010
            PCL: Pcal_0229
            PAS: Pars_2167
STRUCTURES  PDB: 1AP5  1AP6  1AR4  1AR5  1AVM  1AZV  1B06  1B4L  1B4T  1BA9  
                 1BS3  1BSM  1BT8  1BZO  1CB4  1CBJ  1COB  1D5N  1DSW  1DT0  
                 1E9O  1EM1  1EN4  1EN5  1EN6  1EQW  1ESO  1F18  1F1A  1F1D  
                 1F1G  1FUN  1GN2  1GN3  1GN4  1GN6  1HL4  1HL5  1I08  1I0H  
                 1IB5  1IBB  1IBD  1IBF  1IBH  1IDS  1ISA  1ISB  1ISC  1IX9  
                 1IXB  1JA8  1JCV  1JK9  1JR9  1KKC  1KMG  1L3N  1LUV  1LUW  
                 1MA1  1MFM  1MMM  1MNG  1MSD  1MY6  1N0J  1N0N  1N18  1N19  
                 1OAJ  1OAL  1OEZ  1OZT  1OZU  1P1V  1P7G  1PL4  1PM9  1PTZ  
                 1PU0  1PZS  1Q0D  1Q0E  1Q0F  1Q0G  1Q0K  1Q0M  1QNM  1QNN  
                 1RK7  1S4I  1SDA  1SDY  1SOS  1SPD  1SRD  1SXA  1SXB  1SXC  
                 1SXN  1SXS  1SXZ  1SZX  1T6I  1T6Q  1T6U  1TO4  1TO5  1UER  
                 1UES  1UNF  1UXL  1UXM  1VAR  1VEW  1WB7  1WB8  1XDC  1XIL  
                 1XRE  1XSO  1XUQ  1Y67  1YAI  1YAZ  1YSO  1Z9N  1Z9P  1ZA5  
                 1ZLZ  1ZSP  1ZTE  1ZUQ  2A03  2ADP  2ADQ  2AEO  2AF2  2AQM  
                 2AQN  2AQP  2AQQ  2AQR  2AQS  2AQT  2AW9  2AWP  2BKB  2BPI  
                 2C9S  2C9U  2C9V  2CDY  2CE4  2CW2  2CW3  2GBT  2GBU  2GBV  
                 2GDS  2GOJ  2JCW  2NNX  2NYB  2P4K  2SOD  2V0A  3MDS  3SDP  
                 3SOD  
DBLINKS     IUBMB Enzyme Nomenclature: 1.15.1.1
            ExPASy - ENZYME nomenclature database: 1.15.1.1
            ExplorEnz - The Enzyme Database: 1.15.1.1
            ERGO genome analysis and discovery system: 1.15.1.1
            BRENDA, the Enzyme Database: 1.15.1.1
            CAS: 9054-89-1
///
ENTRY       EC 1.15.1.2                 Enzyme
NAME        superoxide reductase;
            neelaredoxin;
            desulfoferrodoxin
CLASS       Oxidoreductases;
            Acting on superoxide as acceptor;
            Acting on superoxide as acceptor (only sub-subclass identified to
            date)
SYSNAME     rubredoxin:superoxide oxidoreductase
REACTION    reduced rubredoxin + superoxide + 2 H+ = rubredoxin + H2O2
            [RN:R05743]
ALL_REAC    R05743
SUBSTRATE   reduced rubredoxin [CPD:C00340];
            superoxide;
            H+ [CPD:C00080]
PRODUCT     rubredoxin;
            H2O2 [CPD:C00027]
COMMENT     The enzyme contains non-heme iron.
REFERENCE   1  [PMID:10514376]
  AUTHORS   Jenney FE Jr, Verhagen MF, Cui X, Adams MW.
  TITLE     Anaerobic microbes: oxygen detoxification without superoxide
            dismutase.
  JOURNAL   Science. 286 (1999) 306-9.
  ORGANISM  Pyrococcus furiosus [GN:pfu]
REFERENCE   2  [PMID:10704199]
  AUTHORS   Yeh AP, Hu Y, Jenney FE Jr, Adams MW, Rees DC.
  TITLE     Structures of the superoxide reductase from Pyrococcus furiosus in
            the oxidized and reduced states.
  JOURNAL   Biochemistry. 39 (2000) 2499-508.
  ORGANISM  Pyrococcus furiosus [GN:pfu]
REFERENCE   3  [PMID:10617593]
  AUTHORS   Lombard M, Fontecave M, Touati D, Niviere V.
  TITLE     Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with
            superoxide anion. Evidence for a superoxide reductase activity.
  JOURNAL   J. Biol. Chem. 275 (2000) 115-21.
  ORGANISM  Desulfoarculus baarsii
REFERENCE   4  [PMID:11069658]
  AUTHORS   Abreu IA, Saraiva LM, Carita J, Huber H, Stetter KO, Cabelli D,
            Teixeira M.
  TITLE     Oxygen detoxification in the strict anaerobic archaeon Archaeoglobus
            fulgidus: superoxide scavenging by neelaredoxin.
  JOURNAL   Mol. Microbiol. 38 (2000) 322-34.
  ORGANISM  Archaeoglobus fulgidus [GN:afu]
ORTHOLOGY   KO: K05919  superoxide reductase
GENES       PCA: Pcar_2347
            DVU: DVU3183(rbo)
            DDE: Dde_3193
            LIP: LI0273
            SFU: Sfum_3891
            MGM: Mmc1_2950
            CKL: CKL_3781(rbo)
            TTE: TTE2229
            TMA: TM0658
            TPT: Tpet_0273
            MJA: MJ0741(rbo)
            MMP: MMP1157(rbo)
            MBU: Mbur_1006
            AFU: AF0344
            PHO: PH1083
            PAB: PAB0599
            PFU: PF1281
            TKO: TK0525
            RCI: RCIX2624(sor)
            HBU: Hbut_1161
            NEQ: NEQ011
STRUCTURES  PDB: 1VZG  1VZH  1VZI  1Y07  2AMU  2HVB  2JI1  2JI2  2JI3  
DBLINKS     IUBMB Enzyme Nomenclature: 1.15.1.2
            ExPASy - ENZYME nomenclature database: 1.15.1.2
            ExplorEnz - The Enzyme Database: 1.15.1.2
            ERGO genome analysis and discovery system: 1.15.1.2
            BRENDA, the Enzyme Database: 1.15.1.2
///
ENTRY       EC 1.16.1.1                 Enzyme
NAME        mercury(II) reductase;
            mercuric reductase;
            mercurate(II) reductase;
            mercuric ion reductase;
            mercury reductase;
            reduced NADP+:mercuric ion oxidoreductase;
            mer A
CLASS       Oxidoreductases;
            Oxidizing metal ions;
            With NAD+ or NADP+ as acceptor
SYSNAME     Hg:NADP+ oxidoreductase
REACTION    Hg + NADP+ + H+ = Hg2+ + NADPH [RN:R02807]
ALL_REAC    R02807
SUBSTRATE   Hg [CPD:C01319];
            NADP+ [CPD:C00006];
            H+ [CPD:C00080]
PRODUCT     Hg2+ [CPD:C00703];
            NADPH [CPD:C00005]
COMMENT     A dithiol enzyme.
REFERENCE   1  [PMID:6277900]
  AUTHORS   Fox B, Walsh CT.
  TITLE     Mercuric reductase. Purification and characterization of a
            transposon-encoded flavoprotein containing an
            oxidation-reduction-active disulfide.
  JOURNAL   J. Biol. Chem. 257 (1982) 2498-503.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   2
  AUTHORS   Fox, B.S. and Walsh, C.T.
  TITLE     Mercuric reductase - homology to glutathione-reductase and lipoamide
            dehydrogenase - iodoacetamide alkylation and sequence of the
            active-site peptide.
  JOURNAL   Biochemistry 22 (1983) 4082-4088.
  ORGANISM  Pseudomonas aeruginosa
ORTHOLOGY   KO: K00520  mercuric reductase
GENES       CME: CMJ014C
            STY: HCM1.158(merA) HCM1.231c(merA)
            SEC: SC020(merA)
            SSN: SSON_0320(ykgC)
            XCC: XCC3891
            XCB: XC_3979
            PPR: PBPRA2113
            PAU: PA14_15460(merA)
            PAP: PSPA7_0090(merA2) PSPA7_0104(merA1)
            PAR: Psyc_1392
            PCR: Pcryo_0977
            SFR: Sfri_2957 Sfri_3488
            SHN: Shewana3_4311 Shewana3_4345
            ILO: IL1160(merA_1) IL1646(merA_2)
            PHA: PSHAb0231
            PAT: Patl_0395
            SDE: Sde_3653
            PIN: Ping_2767
            MAQ: Maqu_0145
            LPN: lpg0244 lpg1562(merA1) lpg2101(merA1)
            LPF: lpl1464
            LPP: lpp1519
            MCA: MCA1340(merA)
            FTL: FTL_0277
            FTH: FTH_0276
            FTN: FTN_1526
            NOC: Noc_0589 Noc_2758
            AEH: Mlg_0751
            HCH: HCH_01003
            CSA: Csal_3219
            ABO: ABO_2183
            AHA: AHA_1547 AHA_3827
            RSO: RS02078(RSp1380)
            REU: Reut_A0385 Reut_D6495(merA)
            RME: Rmet_5011 Rmet_6174 Rmet_6183
            BXE: Bxe_A1496 Bxe_C1213
            BPS: BPSS0139
            BPM: BURPS1710b_A1652(lpd)
            RFR: Rfer_1621
            POL: Bpro_1509 Bpro_2228
            MMS: mma_0954 mma_1749
            NEU: NE0839(merA)
            NET: Neut_1309
            EBA: ebA4535 ebA6707(merA)
            TBD: Tbd_1341(merA) Tbd_1472
            GSU: GSU1315(merA-1) GSU3424(merA-2)
            GME: Gmet_0177
            PCA: Pcar_2535
            DVU: DVU1037
            DVL: Dvul_1956
            DDE: Dde_1463
            DPS: DP0504
            MLO: mll5241 mlr2769
            MES: Meso_0352
            SME: SMb21143(merA2) SMc01717(merA1)
            ATU: Atu5537
            ATC: AGR_pAT_803
            RET: RHE_PE00270
            RLE: pRL110384
            BBT: BBta_3385
            SIL: SPO0540
            SIT: TM1040_0315
            RSP: RSP_1057(merA1)
            RSH: Rsph17029_2718
            JAN: Jann_0645
            RDE: RD1_1463(merA) RD1_1464(merA)
            MMR: Mmar10_2329
            HNE: HNE_0408 HNE_1691(merA)
            SAL: Sala_2512 Sala_2683 Sala_2701
            ELI: ELI_00350
            GKA: GK3096
            SAB: SAB0544c
            SEP: SE0085
            SAG: SAG1254(merA-1) SAG2023(merA-2)
            SGO: SGO_0368(merA) SGO_1283
            MSY: MS53_0152
            MPA: MAP1844c(lpd)
            CGL: NCgl2908(cgl3011)
            CGB: cg3339(merA)
            CJK: jk1442(merA)
            SCO: SCO3443(SCE36.10c) SCO3460(SCE46.17)
            ART: Arth_4465
            AAU: AAur_pTC10241(merA)
            FRA: Francci3_0937
            ACE: Acel_0690
            SEN: SACE_3455
            RXY: Rxyl_1767
            FNU: FN0820
            RBA: RB11205(merA)
            SYN: slr1849(merA)
            SYC: syc0431_d
            SYF: Synpcc7942_1118
            CYB: CYB_1977
            GVI: gll0564 glr2871
            ANA: all5185
            TER: Tery_3348
            SRU: SRU_0077 SRU_2392
            GFO: GFO_1127(merA)
            DET: DET0732
            DEH: cbdb_A687
            TTH: TTC0789
            TTJ: TTHA1153
            HMA: pNG6156(merA)
            TAC: Ta1341
            TVO: TVN0251
            PTO: PTO0264
            APE: APE_1458
            SSO: SSO2689(merA)
            STO: ST1075
            SAI: Saci_1708(merA)
            PAI: PAE2623
STRUCTURES  PDB: 1ZK7  1ZX9  
DBLINKS     IUBMB Enzyme Nomenclature: 1.16.1.1
            ExPASy - ENZYME nomenclature database: 1.16.1.1
            ExplorEnz - The Enzyme Database: 1.16.1.1
            ERGO genome analysis and discovery system: 1.16.1.1
            UM-BBD (Biocatalysis/Biodegradation Database): 1.16.1.1
            BRENDA, the Enzyme Database: 1.16.1.1
            CAS: 67880-93-7
///
ENTRY       EC 1.16.1.2                 Enzyme
NAME        diferric-transferrin reductase;
            diferric transferrin reductase;
            NADH diferric transferrin reductase;
            transferrin reductase
CLASS       Oxidoreductases;
            Oxidizing metal ions;
            With NAD+ or NADP+ as acceptor
SYSNAME     transferrin[Fe(II)]2:NAD+ oxidoreductase
REACTION    transferrin[Fe(II)]2 + NAD+ + H+ = transferrin[Fe(III)]2 + NADH
            [RN:R04123]
ALL_REAC    R04123
SUBSTRATE   transferrin[Fe(II)]2 [CPD:C03029];
            NAD+ [CPD:C00003];
            H+ [CPD:C00080]
PRODUCT     transferrin[Fe(III)]2 [CPD:C03179];
            NADH [CPD:C00004]
REFERENCE   1  [PMID:3767994]
  AUTHORS   Low H, Sun IL, Navas P, Grebing C, Crane FL, Morre DJ.
  TITLE     Transplasmalemma electron transport from cells is part of a diferric
            transferrin reductase system.
  JOURNAL   Biochem. Biophys. Res. Commun. 139 (1986) 1117-23.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
STRUCTURES  PDB: 1L5T  
DBLINKS     IUBMB Enzyme Nomenclature: 1.16.1.2
            ExPASy - ENZYME nomenclature database: 1.16.1.2
            ExplorEnz - The Enzyme Database: 1.16.1.2
            ERGO genome analysis and discovery system: 1.16.1.2
            BRENDA, the Enzyme Database: 1.16.1.2
            CAS: 105238-49-1
///
ENTRY       EC 1.16.1.3                 Enzyme
NAME        aquacobalamin reductase;
            aquocobalamin reductase;
            vitamin B12a reductase;
            NADH-linked aquacobalamin reductase;
            B12a reductase;
            NADH2:cob(III)alamin oxidoreductase
CLASS       Oxidoreductases;
            Oxidizing metal ions;
            With NAD+ or NADP+ as acceptor
SYSNAME     cob(II)alamin:NAD+ oxidoreductase
REACTION    2 cob(II)alamin + NAD+ = 2 aquacob(III)alamin + NADH + H+
            [RN:R00097]
ALL_REAC    R00097
SUBSTRATE   cob(II)alamin [CPD:C00541];
            NAD+ [CPD:C00003]
PRODUCT     aquacob(III)alamin [CPD:C00992];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein.
REFERENCE   1  [PMID:4390543]
  AUTHORS   Walker GA, Murphy S, Huennekens FM.
  TITLE     Enzymatic conversion of vitamin B 12a to adenosyl-B 12: evidence for
            the existence of two separate reducing systems.
  JOURNAL   Arch. Biochem. Biophys. 134 (1969) 95-102.
  ORGANISM  Clostridium tetanomorphum
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K05368  aquacobalamin reductase
GENES       ECO: b3844(fre)
            ECJ: JW3820(fre)
            ECE: Z5365(ubiB)
            ECS: ECs4772
            ECC: c4791(ubiB)
            ECI: UTI89_C4429(fre)
            ECP: ECP_4057
            ECV: APECO1_2613(fre)
            ECW: EcE24377A_4363(fre)
            ECX: EcHS_A4066(fre)
            STY: STY3580(ubiB)
            STT: t3318(ubiB)
            SPT: SPA3820(ubiB)
            SEC: SC3877(fre)
            STM: STM3979(ubiB)
            YPE: YPO3768(fadI)
            YPK: y0462(ubiB)
            YPM: YP_3280(fadI)
            YPA: YPA_3438
            YPN: YPN_0196
            YPS: YPTB0265(fadI)
            SFL: SF3920(ubiB)
            SFX: S3832(ubiB)
            SFV: SFV_3656(ubiB)
            SSN: SSON_4017(ubiB)
            SBO: SBO_3856(ubiB)
            SDY: SDY_3901(ubiB)
            ECA: ECA0206(fre)
            PLU: plu4404(fre)
            SGL: SG0117
            VCH: VC0312
            VVU: VV1_0933
            VVY: VV3177
            VPA: VP2995
            VFI: VF0062
            PPR: PBPRA3536(luxG)
            SON: SO_0504(fre)
            SDN: Sden_3058
            SFR: Sfri_3390
            SHE: Shewmr4_0505
            SHM: Shewmr7_3526
            SHN: Shewana3_0505
            ILO: IL2359(ubiB)
            CPS: CPS_0178
            PHA: PSHAa0104(fre)
            AHA: AHA_0102
            BCI: BCI_0060(ubiB)
DBLINKS     IUBMB Enzyme Nomenclature: 1.16.1.3
            ExPASy - ENZYME nomenclature database: 1.16.1.3
            ExplorEnz - The Enzyme Database: 1.16.1.3
            ERGO genome analysis and discovery system: 1.16.1.3
            BRENDA, the Enzyme Database: 1.16.1.3
            CAS: 37256-39-6
///
ENTRY       EC 1.16.1.4                 Enzyme
NAME        cob(II)alamin reductase;
            vitamin B12r reductase;
            B12r reductase;
            NADH2:cob(II)alamin oxidoreductase
CLASS       Oxidoreductases;
            Oxidizing metal ions;
            With NAD+ or NADP+ as acceptor
SYSNAME     cob(I)alamin:NAD+ oxidoreductase
REACTION    2 cob(I)alamin + NAD+ = 2 cob(II)alamin + NADH + H+ [RN:R00099]
ALL_REAC    R00099
SUBSTRATE   cob(I)alamin [CPD:C00853];
            NAD+ [CPD:C00003]
PRODUCT     cob(II)alamin [CPD:C00541];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein.
REFERENCE   1  [PMID:4390543]
  AUTHORS   Walker GA, Murphy S, Huennekens FM.
  TITLE     Enzymatic conversion of vitamin B 12a to adenosyl-B 12: evidence for
            the existence of two separate reducing systems.
  JOURNAL   Arch. Biochem. Biophys. 134 (1969) 95-102.
  ORGANISM  Clostridium tetanomorphum
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.16.1.4
            ExPASy - ENZYME nomenclature database: 1.16.1.4
            ExplorEnz - The Enzyme Database: 1.16.1.4
            ERGO genome analysis and discovery system: 1.16.1.4
            BRENDA, the Enzyme Database: 1.16.1.4
            CAS: 37256-40-9
///
ENTRY       EC 1.16.1.5                 Enzyme
NAME        aquacobalamin reductase (NADPH);
            aquacobalamin (reduced nicotinamide adenine dinucleotide phosphate)
            reductase;
            NADPH-linked aquacobalamin reductase;
            NADPH2:aquacob(III)alamin oxidoreductase
CLASS       Oxidoreductases;
            Oxidizing metal ions;
            With NAD+ or NADP+ as acceptor
SYSNAME     cob(II)alamin:NADP+ oxidoreductase
REACTION    2 cob(II)alamin + NADP+ = 2 aquacob(III)alamin + NADPH + H+
            [RN:R00107]
ALL_REAC    R00107
SUBSTRATE   cob(II)alamin [CPD:C00541];
            NADP+ [CPD:C00006]
PRODUCT     aquacob(III)alamin [CPD:C00992];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein. Acts on aquacob(III)alamin and hydroxycobalamin, but
            not on cyanocobalamin.
REFERENCE   1  [PMID:3114247]
  AUTHORS   Watanabe F, Oki Y, Nakano Y, Kitaoka S.
  TITLE     Purification and characterization of aquacobalamin reductase (NADPH)
            from Euglena gracilis.
  JOURNAL   J. Biol. Chem. 262 (1987) 11514-8.
  ORGANISM  Euglena gracilis
REFERENCE   2  [PMID:8373179]
  AUTHORS   Watanabe F, Yamaji R, Isegawa Y, Yamamoto T, Tamura Y, Nakano Y.
  TITLE     Characterization of aquacobalamin reductase (NADPH) from Euglena
            gracilis.
  JOURNAL   Arch. Biochem. Biophys. 305 (1993) 421-7.
  ORGANISM  Euglena gracilis
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.16.1.5
            ExPASy - ENZYME nomenclature database: 1.16.1.5
            ExplorEnz - The Enzyme Database: 1.16.1.5
            ERGO genome analysis and discovery system: 1.16.1.5
            BRENDA, the Enzyme Database: 1.16.1.5
            CAS: 110777-32-7
///
ENTRY       EC 1.16.1.6                 Enzyme
NAME        cyanocobalamin reductase (cyanide-eliminating);
            cyanocobalamin reductase;
            cyanocobalamin reductase (NADPH, cyanide-eliminating);
            cyanocobalamin reductase (NADPH;
            CN-eliminating);
            NADPH:cyanocob(III)alamin oxidoreductase (cyanide-eliminating)
CLASS       Oxidoreductases;
            Oxidizing metal ions;
            With NAD+ or NADP+ as acceptor
SYSNAME     cob(I)alamin, cyanide:NADP+ oxidoreductase
REACTION    cob(I)alamin + cyanide + NADP+ = cyanocob(III)alamin + NADPH + H+
            [RN:R02999]
ALL_REAC    R02999
SUBSTRATE   cob(I)alamin [CPD:C00853];
            cyanide [CPD:C00177];
            NADP+ [CPD:C00006]
PRODUCT     cyanocob(III)alamin [CPD:C02823];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein.
REFERENCE   1  [PMID:3134526]
  AUTHORS   Watanabe F, Oki Y, Nakano Y, Kitaoka S.
  TITLE     Occurrence and characterization of cyanocobalamin reductase (NADPH;
            CN-eliminating) involved in decyanation of cyanocobalamin in Euglena
            gracilis.
  JOURNAL   J. Nutr. Sci. Vitaminol. (Tokyo). 34 (1988) 1-10.
  ORGANISM  Euglena gracilis
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.16.1.6
            ExPASy - ENZYME nomenclature database: 1.16.1.6
            ExplorEnz - The Enzyme Database: 1.16.1.6
            ERGO genome analysis and discovery system: 1.16.1.6
            BRENDA, the Enzyme Database: 1.16.1.6
            CAS: 131145-00-1
///
ENTRY       EC 1.16.1.7                 Enzyme
NAME        ferric-chelate reductase;
            ferric chelate reductase;
            iron chelate reductase;
            NADH:Fe3+-EDTA reductase;
            NADH2:Fe3+ oxidoreductase
CLASS       Oxidoreductases;
            Oxidizing metal ions;
            With NAD+ or NADP+ as acceptor
SYSNAME     Fe(II):NAD+ oxidoreductase
REACTION    2 Fe(II) + NAD+ = 2 Fe(III) + NADH + H+ [RN:R00092]
ALL_REAC    R00092
SUBSTRATE   Fe(II) [CPD:C14818];
            NAD+ [CPD:C00003]
PRODUCT     Fe(III) [CPD:C14819];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Involved in the transport of iron across plant plasma membranes.
REFERENCE   1
  AUTHORS   Askerlund, P., Larrson, C. and Widell, S.
  TITLE     Localization of donor and acceptor sites of NADH dehydrogenase
            activities using inside-out and right-side-out plasma membrane
            vesicles from plants.
  JOURNAL   FEBS Lett. 239 (1988) 23-28.
  ORGANISM  Beta vulgaris
REFERENCE   2  [PMID:16525561]
  AUTHORS   Freitas MP.
  TITLE     MIA-QSAR modelling of anti-HIV-1 activities of some
            2-amino-6-arylsulfonylbenzonitriles and their thio and sulfinyl
            congeners.
  JOURNAL   Org. Biomol. Chem. 4 (2006) 1154-9.
REFERENCE   3  [PMID:16525561]
  AUTHORS   Freitas MP.
  TITLE     MIA-QSAR modelling of anti-HIV-1 activities of some
            2-amino-6-arylsulfonylbenzonitriles and their thio and sulfinyl
            congeners.
  JOURNAL   Org. Biomol. Chem. 4 (2006) 1154-9.
REFERENCE   4
  AUTHORS   Buckhout, T.J. and Hrubec, T.C.
  TITLE     Pyridine nucleotide-dependent ferricyanide reduction associated with
            isolated plasma membranes of maize (Zea mays L.) roots.
  JOURNAL   Protoplasma 135 (1986) 144-154.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   5
  AUTHORS   Sandelius, A.S., Barr, R., Crane, F.L. and Morre, D.J.
  TITLE     Redox reactions of plasma membranes isolated from soybean hypocotyls
            by phase partition.
  JOURNAL   Plant Sci. 48 (1986) 1-10.
  ORGANISM  Glycine max [GN:egma]
ORTHOLOGY   KO: K00521  ferric-chelate reductase
GENES       SCE: YLL051C(FRE6) YOL152W(FRE7) YOR381W(FRE3) YOR384W(FRE5)
            AGO: AGOS_ADR080W
            PIC: PICST_40289(FRE1.2)
            CGR: CAGL0C03333g
            ANI: AN6400.2
            AFM: AFUA_1G17270 AFUA_4G03940 AFUA_6G13750 AFUA_7G04970
                 AFUA_7G07120
            CNE: CNA02040 CNI01220
            UMA: UM05979.1
            SAT: SYN_02123
            GBE: GbCGDNIH1_2380
DBLINKS     IUBMB Enzyme Nomenclature: 1.16.1.7
            ExPASy - ENZYME nomenclature database: 1.16.1.7
            ExplorEnz - The Enzyme Database: 1.16.1.7
            ERGO genome analysis and discovery system: 1.16.1.7
            BRENDA, the Enzyme Database: 1.16.1.7
            CAS: 122097-10-3
///
ENTRY       EC 1.16.1.8                 Enzyme
NAME        [methionine synthase] reductase;
            methionine synthase cob(II)alamin reductase (methylating);
            methionine synthase reductase;
            [methionine synthase]-cobalamin methyltransferase (cob(II)alamin
            reducing)
CLASS       Oxidoreductases;
            Oxidizing metal ions;
            With NAD+ or NADP+ as acceptor
SYSNAME     [methionine
            synthase]-methylcob(I)alamin,S-adenosylhomocysteine:NADP+
            oxidoreductase
REACTION    2 [methionine synthase]-methylcob(I)alamin + 2
            S-adenosylhomocysteine + NADP+ = 2 [methionine
            synthase]-cob(I)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
            [RN:R05182]
ALL_REAC    R05182
SUBSTRATE   [methionine synthase]-methylcob(I)alamin [CPD:C06410];
            S-adenosylhomocysteine [CPD:C00021];
            NADP+ [CPD:C00006]
PRODUCT     [methionine synthase]-cob(I)alamin [CPD:C06409];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            S-adenosyl-L-methionine [CPD:C00019]
COFACTOR    Flavoprotein [CPD:C06411]
COMMENT     In humans, the enzyme is a flavoprotein containing FAD and FMN. The
            substrate of the enzyme is the inactivated [Co(II)] form of EC
            2.1.1.13, methionine synthase. Electrons are transferred from NADPH
            to FAD to FMN. Defects in this enzyme lead to hereditary
            hyperhomocysteinemia.
REFERENCE   1  [PMID:9501215]
  AUTHORS   Leclerc D, Wilson A, Dumas R, Gafuik C, Song D, Watkins D, Heng HH,
            Rommens JM, Scherer SW, Rosenblatt DS, Gravel RA.
  TITLE     Cloning and mapping of a cDNA for methionine synthase reductase, a
            flavoprotein defective in patients with homocystinuria.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 3059-64.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:11466310]
  AUTHORS   Olteanu H, Banerjee R.
  TITLE     Human methionine synthase reductase, a soluble P-450 reductase-like
            dual flavoprotein, is sufficient for NADPH-dependent methionine
            synthase activation.
  JOURNAL   J. Biol. Chem. 276 (2001) 35558-63.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:12416982]
  AUTHORS   Olteanu H, Munson T, Banerjee R.
  TITLE     Differences in the efficiency of reductive activation of methionine
            synthase and exogenous electron acceptors between the common
            polymorphic variants of human methionine synthase reductase.
  JOURNAL   Biochemistry. 41 (2002) 13378-85.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K00597  [methionine synthase] reductase
GENES       HSA: 4552(MTRR)
            PTR: 461717(MTRR)
            MMU: 210009(Mtrr)
            CFA: 478623(MTRR)
            GGA: 428502(MTRR)
            CEL: C01G6.6(tag-165)
            HAR: HEAR3398
DBLINKS     IUBMB Enzyme Nomenclature: 1.16.1.8
            ExPASy - ENZYME nomenclature database: 1.16.1.8
            ExplorEnz - The Enzyme Database: 1.16.1.8
            ERGO genome analysis and discovery system: 1.16.1.8
            BRENDA, the Enzyme Database: 1.16.1.8
            CAS: 207004-87-3
///
ENTRY       EC 1.16.3.1                 Enzyme
NAME        ferroxidase;
            ceruloplasmin;
            ferroxidase I;
            iron(II): oxygen oxidoreductase;
            caeruloplasmin;
            ferro:O2 oxidoreductase;
            ferroxidase, iron II:oxygen oxidoreductase
CLASS       Oxidoreductases;
            Oxidizing metal ions;
            With oxygen as acceptor
SYSNAME     Fe(II):oxygen oxidoreductase
REACTION    4 Fe(II) + 4 H+ + O2 = 4 Fe(III) + 2 H2O [RN:R00078]
ALL_REAC    R00078
SUBSTRATE   Fe(II) [CPD:C14818];
            H+ [CPD:C00080];
            O2 [CPD:C00007]
PRODUCT     Fe(III) [CPD:C14819];
            H2O [CPD:C00001]
COFACTOR    Copper [CPD:C00070]
COMMENT     A multi-copper protein: ceruloplasmin from animals, rusticyanin in
            Thiobacillus ferroxidans.
REFERENCE   1
  AUTHORS   Cox, J.C. and Boxer, D.H.
  TITLE     The role of rusticyanin, a blue copper protein, in the electron
            transport chain of Thiobacillus ferrooxidans grown on iron or
            thiosulfate.
  JOURNAL   Biotechnol. Appl. Biochem. 8 (1986) 269-275.
  ORGANISM  Thiobacillus ferrooxidans
REFERENCE   2  [PMID:5925868]
  AUTHORS   Osaki S.
  TITLE     Kinetic studies of ferrous ion oxidation with crystalline human
            ferroxidase (ceruloplasmin).
  JOURNAL   J. Biol. Chem. 241 (1966) 5053-9.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:6027241]
  AUTHORS   Osaki S, Walaas O.
  TITLE     Kinetic studies of ferrous ion oxidation with crystalline human
            ferroxidase. II. Rate constants at various steps and formation of a
            possible enzyme-substrate complex.
  JOURNAL   J. Biol. Chem. 242 (1967) 2653-7.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K00522  ferroxidase
GENES       HSA: 1356(CP) 2495(FTH1) 94033(FTMT)
            PTR: 471613(FTMT)
            MMU: 12870(Cp) 14319(Fth1) 67634(Ftmt)
            RNO: 24268(Cp) 25319(Fth1)
            CFA: 403631(FTH1) 442963(CP)
            BTA: 281173(FTH1)
            SSC: 397030(FTH1)
            GGA: 395970(FTH1) 771940(CP)
            XLA: 379339(MGC53066) 379618(MGC68606) 398724(MGC64558)
            XTR: 394820(MGC75752) 448718(MGC89846)
            DRE: 58108(fth1) 84702(cp)
            SPU: 586705(LOC586705) 591499(LOC591499)
            CEL: D1037.3(ferritin)
            ECI: UTI89_C0816(dps)
            ECW: EcE24377A_2138(ftnA)
            ECX: EcHS_A2003(ftnA)
            SPE: Spro_1942
            ASU: Asuc_1607 Asuc_1608
            PAR: Psyc_1620
            SBM: Shew185_0132
            SSE: Ssed_4374
            SPL: Spea_0129
            NOC: Noc_2612
            NET: Neut_0710
            NMU: Nmul_A2394
            HPA: HPAG1_0246
            GUR: Gura_2910
            BBA: Bd2620(dps)
            GBE: GbCGDNIH1_0685
            BAN: BA2013(dpS)
            BAR: GBAA2013(dpS)
            BAA: BA_2517
            BAT: BAS1871
            BCE: BC2011
            BCA: BCE_2092(dpS)
            BCZ: BCZK1825(dps)
            BTK: BT9727_1841(dps)
            SPZ: M5005_Spy_1259(dpr)
            SPH: MGAS10270_Spy1275(dpr)
            SPI: MGAS10750_Spy1367(dpr)
            SPJ: MGAS2096_Spy1279(dpr)
            SPK: MGAS9429_Spy1254(dpr)
            SPA: M6_Spy1280(dps)
            SPB: M28_Spy1198(dpr)
            LSL: LSL_1781(dps)
            CKL: CKL_0113(ftn)
            PMF: P9303_29571
            FJO: Fjoh_0866
            RRS: RoseRS_1855
            RCA: Rcas_3287
            TPT: Tpet_1617
            TME: Tmel_1199
            FNO: Fnod_1381
            MAE: Maeo_0328
STRUCTURES  PDB: 1KCW  2CEI  2CHI  2CIH  2CLU  2CN6  2CN7  2HTN  2IU2  2J5W  
DBLINKS     IUBMB Enzyme Nomenclature: 1.16.3.1
            ExPASy - ENZYME nomenclature database: 1.16.3.1
            ExplorEnz - The Enzyme Database: 1.16.3.1
            ERGO genome analysis and discovery system: 1.16.3.1
            BRENDA, the Enzyme Database: 1.16.3.1
            CAS: 9031-37-2
///
ENTRY       EC 1.16.8.1                 Enzyme
NAME        cob(II)yrinic acid a,c-diamide reductase;
            cob(II)yrinic acid-a,c-diamide:FMN oxidoreductase (incorrect)
CLASS       Oxidoreductases;
            Oxidizing metal ions;
            With a flavin as acceptor
SYSNAME     cob(I)yrinic acid-a,c-diamide:FMN oxidoreductase
REACTION    2 cob(I)yrinic acid a,c-diamide + FMN + 2 H+ = 2 cob(II)yrinic acid
            a,c-diamide + FMNH2 [RN:R05218]
ALL_REAC    R05218
SUBSTRATE   cob(I)yrinic acid a,c-diamide [CPD:C06505];
            FMN [CPD:C00061];
            H+ [CPD:C00080]
PRODUCT     cob(II)yrinic acid a,c-diamide [CPD:C06504];
            FMNH2 [CPD:C01847]
COMMENT     This enzyme also catalyses the reduction of cob(II)yric acid,
            cob(II)inamide, cob(II)inamide phosphate, GDP-cob(II)inamide and
            cob(II)alamin although cob(II)yrinic acid a,c-diamide is thought to
            be the physiological substrate [1]. Also uses FAD and NADH but not
            NADPH.
REFERENCE   1  [PMID:1429467]
  AUTHORS   Blanche F, Maton L, Debussche L, Thibaut D.
  TITLE     Purification and characterization of Cob(II)yrinic acid a,c-diamide
            reductase from Pseudomonas denitrificans.
  JOURNAL   J. Bacteriol. 174 (1992) 7452-4.
  ORGANISM  Pseudomonas denitrificans
REFERENCE   2  [PMID:12195810]
  AUTHORS   Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
  TITLE     The biosynthesis of adenosylcobalamin (vitamin B12).
  JOURNAL   Nat. Prod. Rep. 19 (2002) 390-412.
  ORGANISM  Propionibacterium freundenreichii
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K04719  cob(II)yrinic acid a,c-diamide reductase
GENES       PAE: PA1274
            PAU: PA14_47750
            PPU: PP_1674
            PST: PSPTO_1710
            PSB: Psyr_3679
            PSP: PSPPH_3700
            PFL: PFL_4429
            PFO: Pfl_1643
            PEN: PSEEN1380
            SPL: Spea_0684
            CPS: CPS_2468
            MCA: MCA2289
            HCH: HCH_06460
            MMW: Mmwyl1_1437
            CVI: CV_1555
            RSO: RS03753(RSp0614)
            RME: Rmet_2213
            BMA: BMA2051
            BXE: Bxe_B1657
            BUR: Bcep18194_A3917
            BCN: Bcen_0341
            BCH: Bcen2424_0824
            BAM: Bamb_0704
            BPS: BPSL2735
            BPM: BURPS1710b_3222
            BPD: BURPS668_3169(bluB)
            BTE: BTH_I1401
            RFR: Rfer_2617
            POL: Bpro_2763
            MPT: Mpe_B0452(cysG) Mpe_B0487(cysG)
            EBA: ebA4029
            DAR: Daro_0141
            TBD: Tbd_2717
            MFA: Mfla_0115
            MLO: mll7468
            SME: SMc00166
            ATU: Atu1654
            ATC: AGR_C_3047
            RET: RHE_CH02368
            RLE: RL2681
            BME: BMEII0246
            BMF: BAB2_1015
            BMS: BRA1054
            BMB: BruAb2_0994
            OAN: Oant_1328
            BJA: bll3254
            BRA: BRADO4896
            BBT: BBta_3155
            RPA: RPA0711
            RPB: RPB_0743
            RPC: RPC_3749
            RPD: RPD_0641
            RPE: RPE_2232
            SIL: SPO3254(bluB)
            SIT: TM1040_2608
            RSP: RSP_3218
            RDE: RD1_3815(bluB)
            PDE: Pden_2527
            NAR: Saro_0330
            GBE: GbCGDNIH1_1100
            RRU: Rru_A3536
            MAG: amb1227
            MGM: Mmc1_1683
            MTU: Rv0306
            MTC: MT0319(bluB)
            MBO: Mb0314
            MPA: MAP3792c
            MAV: MAV_4857(bluB)
            MSM: MSMEG_6053(bluB)
            MMC: Mmcs_4721
            NFA: nfa46050
            SCO: SCO1554(SCL11.10c)
            SMA: SAV6795(cobT2)
            TFU: Tfu_2222
            FRA: Francci3_2878
            SEN: SACE_0750
            TER: Tery_4461
            FPS: FP1460(bluB)
            CTE: CT0937
            CCH: Cag_1013
            CPH: Cpha266_1116
            PLT: Plut_1141
            TTH: TT_P0018
            TTJ: TTHB061
            SSO: SSO2560
            SAI: Saci_0250
            MSE: Msed_1226
DBLINKS     IUBMB Enzyme Nomenclature: 1.16.8.1
            ExPASy - ENZYME nomenclature database: 1.16.8.1
            ExplorEnz - The Enzyme Database: 1.16.8.1
            ERGO genome analysis and discovery system: 1.16.8.1
            BRENDA, the Enzyme Database: 1.16.8.1
///
ENTRY       EC 1.17.1.1                 Enzyme
NAME        CDP-4-dehydro-6-deoxyglucose reductase;
            CDP-4-keto-6-deoxyglucose reductase;
            cytidine diphospho-4-keto-6-deoxy-D-glucose reductase;
            cytidine diphosphate 4-keto-6-deoxy-D-glucose-3-dehydrogenase;
            CDP-4-keto-deoxy-glucose reductase;
            CDP-4-keto-6-deoxy-D-glucose-3-dehydrogenase system;
            NAD(P)H:CDP-4-keto-6-deoxy-D-glucose oxidoreductase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With NAD+ or NADP+ as acceptor
SYSNAME     CDP-4-dehydro-3,6-dideoxy-D-glucose:NAD(P)+ 3-oxidoreductase
REACTION    CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O =
            CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+ [RN:R03391 R03392]
ALL_REAC    R03391 R03392
SUBSTRATE   CDP-4-dehydro-3,6-dideoxy-D-glucose [CPD:C04297];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     CDP-4-dehydro-6-deoxy-D-glucose [CPD:C01219];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The enzyme consists of two proteins. One forms an enzyme-bound
            adduct of the CDP-4-dehydro-6-deoxyglucose with pyridoxamine
            phosphate, in which the 3-hydroxy group has been removed. The second
            catalyses the reduction of this adduct by NAD(P)H and release of the
            CDP-4-dehydro-3,6-dideoxy-D-glucose and pyridoxamine phosphate.
REFERENCE   1  [PMID:4389672]
  AUTHORS   Pape H, Strominger JL.
  TITLE     Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. V.
            Partial purification of the two protein components required for
            introduction of the 3-deoxy group.
  JOURNAL   J. Biol. Chem. 244 (1969) 3598-604.
  ORGANISM  Pasteurella pseudotuberculosis, Salmonella typhimurium
REFERENCE   2  [PMID:4152100]
  AUTHORS   Rubenstein PA, Strominger JL.
  TITLE     Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. 8.
            Mechanistic roles of enzyme E-1 and pyridoxamine 5'-phosphate in the
            formation of cytidine diphosphate-4-keto-3,6-dideoxy-D-glucose from
            cytidine diphosphate-4-keto-6-deoxy-D-glucose.
  JOURNAL   J. Biol. Chem. 249 (1974) 3776-81.
  ORGANISM  Pasteurella pseudotuberculosis, Salmonella typhimurium
REFERENCE   3  [PMID:7826006]
  AUTHORS   Liu HW, Thorson JS.
  TITLE     Pathways and mechanisms in the biogenesis of novel deoxysugars by
            bacteria.
  JOURNAL   Annu. Rev. Microbiol. 48 (1994) 223-56.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.1.1
            ExPASy - ENZYME nomenclature database: 1.17.1.1
            ExplorEnz - The Enzyme Database: 1.17.1.1
            ERGO genome analysis and discovery system: 1.17.1.1
            BRENDA, the Enzyme Database: 1.17.1.1
            CAS: 37256-87-4
///
ENTRY       EC 1.17.1.2                 Enzyme
NAME        4-hydroxy-3-methylbut-2-enyl diphosphate reductase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With NAD+ or NADP+ as acceptor
SYSNAME     isopentenyl-diphosphate:NADP+ oxidoreductase
REACTION    (1) isopentenyl diphosphate + NAD(P)+ + H2O =
            (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
            [RN:R05884];
            (2) dimethyallyl diphosphate + NAD(P)+ + H2O =
            (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
            [RN:R07219]
ALL_REAC    R05884 R07219
SUBSTRATE   isopentenyl diphosphate [CPD:C00129];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            dimethyallyl diphosphate
PRODUCT     (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate [CPD:C11811];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     Forms part of an alternative, nonmevalonate pathway for terpenoid
            biosynthesis (for diagram, click here). The enzyme acts in the
            reverse direction producing a 5:1 mixture of isopentenyl diphosphate
            and dimethyallyl diphosphate.
REFERENCE   1  [PMID:11818558]
  AUTHORS   Rohdich F, Hecht S, Gartner K, Adam P, Krieger C, Amslinger S,
            Arigoni D, Bacher A, Eisenreich W.
  TITLE     Studies on the nonmevalonate terpene biosynthetic pathway: metabolic
            role of IspH (LytB) protein.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 1158-63.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:11741609]
  AUTHORS   Hintz M, Reichenberg A, Altincicek B, Bahr U, Gschwind RM, Kollas
            AK, Beck E, Wiesner J, Eberl M, Jomaa H.
  TITLE     Identification of (E)-4-hydroxy-3-methyl-but-2-enyl pyrophosphate as
            a major activator for human gammadelta T cells in Escherichia coli.
  JOURNAL   FEBS. Lett. 509 (2001) 317-22.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Charon, L., Pale-Grosdemange, C. and Rohmer, M.
  TITLE     On the reduction steps in the mevalonate independent
            2-C-methyl-D-erythritol 4-phosphate (MEP) pathway for isoprenoid
            biosynthesis in the bacterium Zymomonas mobilis.
  JOURNAL   Tetrahedron Lett. 40 (1999) 7231-7234.
  ORGANISM  Zymomonas mobilis [GN:zmo]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K03527  4-hydroxy-3-methylbut-2-enyl diphosphate reductase
GENES       ATH: AT4G34350(CLB6)
            OSA: 4334003
            CME: CMJ152C
            PFA: MAL1P1.35
            TAN: TA17670
            TPV: TP03_0674
            ECO: b0029(ispH)
            ECJ: JW0027(ispH)
            ECE: Z0034(lytB)
            ECS: ECs0032
            ECC: c0033(lytB)
            ECI: UTI89_C0031(lytB)
            ECP: ECP_0027
            ECV: APECO1_1954(lytB)
            ECW: EcE24377A_0029(ispH)
            ECX: EcHS_A0031
            STY: STY0058(lytB)
            STT: t0051(lytB)
            SPT: SPA0050(lytB)
            SEC: SC0043(lytB)
            STM: STM0049(lytB)
            YPE: YPO0477(lytB)
            YPK: y3697(lytB)
            YPM: YP_3702(lytB)
            YPA: YPA_4071
            YPN: YPN_0350
            YPP: YPDSF_3154
            YPS: YPTB0620(lytB)
            YPI: YpsIP31758_3457(ispH)
            SFL: SF0026(lytB)
            SFX: S0028(lytB)
            SFV: SFV_0023(lytB)
            SSN: SSON_0034(lytB)
            SBO: SBO_0028(lytB)
            SDY: SDY_0051(lytB)
            ECA: ECA3873(ispH)
            PLU: plu0594(lytB)
            BUC: BU147(lytB)
            BAS: BUsg140(lytB)
            WBR: WGLp292(lytB)
            SGL: SG0417
            ENT: Ent638_0587
            SPE: Spro_0701
            BPN: BPEN_124(ispH)
            HIN: HI1007(lytB)
            HIT: NTHI1182(ispH)
            HIP: CGSHiEE_06935(ispH)
            HIQ: CGSHiGG_08665(ispH)
            HDU: HD0064(ispH)
            HSO: HS_0184(ispH)
            PMU: PM1664(lytB)
            MSU: MS1749(lytB)
            APL: APL_1520(ispH)
            ASU: Asuc_1874
            XFA: XF2416
            XFT: PD1435(lytB)
            XCC: XCC1157(lytB)
            XCB: XC_3085
            XCV: XCV1292(lytB)
            XAC: XAC1256(lytB)
            XOO: XOO1628(lytB)
            XOM: XOO_1514(XOO1514)
            VCH: VC0685
            VVU: VV1_0504
            VVY: VV0690
            VPA: VP0537
            VFI: VF0470
            PPR: PBPRA0594
            PAE: PA4557(lytB)
            PAU: PA14_60330(lytB)
            PAP: PSPA7_3192(ispH2) PSPA7_5197(ispH1)
            PPU: PP_0606(ispH)
            PPF: Pput_0647
            PST: PSPTO_0809(ispH)
            PSB: Psyr_0713
            PSP: PSPPH_0724(ispH)
            PFL: PFL_5318(ispH)
            PFO: Pfl_4849
            PEN: PSEEN4689(ispH)
            PMY: Pmen_0956
            PAR: Psyc_1722(lytB)
            PCR: Pcryo_2002
            PRW: PsycPRwf_0578
            ACI: ACIAD3322(ispH)
            SON: SO_3529(lytB)
            SDN: Sden_2720
            SFR: Sfri_2887
            SAZ: Sama_0927
            SBL: Sbal_1057
            SBM: Shew185_1124
            SLO: Shew_1102
            SPC: Sputcn32_1062
            SSE: Ssed_1197
            SPL: Spea_1086
            SHE: Shewmr4_2954
            SHM: Shewmr7_3036
            SHN: Shewana3_1037 Shewana3_3133
            SHW: Sputw3181_3103
            ILO: IL1125(lytB)
            CPS: CPS_1211(ispH)
            PHA: PSHAa0921(ispH)
            PAT: Patl_3175
            SDE: Sde_2563
            PIN: Ping_3268
            MAQ: Maqu_0865
            MCA: MCA1815(ispH)
            FTU: FTT0833(ispH)
            FTF: FTF0833(ispH)
            FTW: FTW_1353(ispH)
            FTL: FTL_0327
            FTH: FTH_0325
            FTA: FTA_0348(ispH)
            NOC: Noc_1744
            AEH: Mlg_0854
            HHA: Hhal_1834
            HCH: HCH_05930(ispH)
            CSA: Csal_0484
            ABO: ABO_0462(lytB)
            MMW: Mmwyl1_4227
            AHA: AHA_0685(ispH)
            BCI: BCI_0558(ispH)
            RMA: Rmag_1023
            VOK: COSY_0924(lytB)
            NME: NMB1831
            NMA: NMA0624(lytB)
            NGO: NGO0072(lytB)
            CVI: CV_3567(lytB)
            RSO: RSc2442(lytB)
            REU: Reut_A2730 Reut_B4898
            RME: Rmet_2868 Rmet_4169
            BMA: BMA2228(ispH-2) BMAA1962(ispH-1)
            BXE: Bxe_A0820 Bxe_B0018
            BVI: Bcep1808_2577 Bcep1808_3716
            BUR: Bcep18194_A5831 Bcep18194_B0106
            BCN: Bcen_1888 Bcen_5308
            BCH: Bcen2424_2499 Bcen2424_5552
            BAM: Bamb_2546 Bamb_4876
            BPS: BPSL0919(lytB) BPSS2168(ispH)
            BPM: BURPS1710b_1141(ispH) BURPS1710b_A1285(ispH)
            BPL: BURPS1106A_0986(ispH) BURPS1106A_A2929(ispH)
            BPD: BURPS668_0981(ispH) BURPS668_A3054(ispH)
            BTE: BTH_I0783(ispH-1) BTH_II2243(ispH-2)
            PNU: Pnuc_1731
            BPE: BP1237(lytB)
            BPA: BPP1852(lytB)
            BBR: BB3256(lytB)
            RFR: Rfer_3248
            POL: Bpro_0951
            PNA: Pnap_3337
            AAV: Aave_3771
            AJS: Ajs_3448
            VEI: Veis_1652
            MPT: Mpe_A2693
            HAR: HEAR2466(ispH)
            MMS: mma_2549
            NEU: NE0649(lytB)
            NET: Neut_1903
            NMU: Nmul_A0089
            EBA: ebA4444(ispH)
            AZO: azo1202(lytB)
            DAR: Daro_3043
            TBD: Tbd_1860
            MFA: Mfla_2431
            HPY: HP0400(lytB)
            HPJ: jhp0981(lytB)
            HPA: HPAG1_0992 HPAG1_0993
            HHE: HH0138(lytB)
            HAC: Hac_0458(lytB)
            WSU: WS1310
            TDN: Tmden_0872
            CJE: Cj0894c(lytB)
            CJR: CJE0973(ispH)
            CJJ: CJJ81176_0903(ispH)
            CJU: C8J_0831(lytB)
            CJD: JJD26997_0919(ispH)
            CFF: CFF8240_1251(ispH)
            CCV: CCV52592_0515(ispH)
            CHA: CHAB381_0483(ispH)
            CCO: CCC13826_0486 CCC13826_1566(ispH)
            ABU: Abu_2050(ispH)
            NIS: NIS_0662(ispH)
            SUN: SUN_0548(ispH)
            GSU: GSU2604(lytB)
            GME: Gmet_0866
            GUR: Gura_1466
            PCA: Pcar_1883(lytB)
            PPD: Ppro_1349
            DVU: DVU0055(ispH)
            DVL: Dvul_2906
            DDE: Dde_0390
            LIP: LI0728(lytB)
            DPS: DP2166
            ADE: Adeh_1519
            AFW: Anae109_2302
            SAT: SYN_02454
            SFU: Sfum_1812
            WOL: WD1274(lytB)
            WBM: Wbm0046(ispH)
            AMA: AM804(lytB)
            APH: APH_0380(ispH)
            ERU: Erum5180(ispH)
            ERW: ERWE_CDS_05430(ispH)
            ERG: ERGA_CDS_05330(ispH)
            ECN: Ecaj_0526
            ECH: ECH_0502(ispH)
            NSE: NSE_0438(ispH)
            PUB: SAR11_0124(lytB)
            MLO: mlr7502
            MES: Meso_0748
            PLA: Plav_0686
            SME: SMc00016(lytB)
            SMD: Smed_0527
            ATU: Atu0774(lytB)
            ATC: AGR_C_1414(lytB)
            RET: RHE_CH00961(lytB)
            RLE: RL1030(ispH)
            BME: BMEI1459
            BMF: BAB1_0501(lytB)
            BMS: BR0475(lytB)
            BMB: BruAb1_0497(lytB)
            BOV: BOV_0480(ispH)
            OAN: Oant_0589
            BJA: bll3007 blr1314
            BRA: BRADO2632(ispH2) BRADO6588(ispH1)
            BBT: BBta_0948(ispH1) BBta_2972(ispH2)
            RPA: RPA3734(lytB1) RPA4271(lytB2)
            RPB: RPB_1340 RPB_1729
            RPC: RPC_1726 RPC_4078
            RPD: RPD_3570 RPD_4030
            RPE: RPE_1816 RPE_4130
            NWI: Nwi_2266 Nwi_2689
            NHA: Nham_2679 Nham_3745
            BHE: BH04410(lytB)
            BQU: BQ03600(lytB)
            BBK: BARBAKC583_0406(ispH)
            XAU: Xaut_2355
            CCR: CC_3361
            SIL: SPO3207(ispH)
            SIT: TM1040_2569
            RSP: RSP_1666(lytB)
            RSH: Rsph17029_0299
            RSQ: Rsph17025_2580
            JAN: Jann_0507
            RDE: RD1_1355(ispH)
            PDE: Pden_3619
            MMR: Mmar10_2215
            HNE: HNE_2713(ispH)
            ZMO: ZMO0875(lytB)
            NAR: Saro_1087
            SAL: Sala_1136
            SWI: Swit_2692
            ELI: ELI_01560
            GOX: GOX0179
            GBE: GbCGDNIH1_1875
            ACR: Acry_1832
            RRU: Rru_A0059
            MAG: amb0764
            MGM: Mmc1_3428
            ABA: Acid345_1739
            SUS: Acid_1259
            BSU: BG11662(yqfP)
            BHA: BH1382
            BAN: BA4511(lytB)
            BAR: GBAA4511(lytB)
            BAA: BA_4959
            BAT: BAS4190(lytB)
            BCA: BCE_4368(lytB)
            BCZ: BCZK4038(lytB)
            BCY: Bcer98_3015
            BTK: BT9727_4028(lytB)
            BTL: BALH_3881(lytB)
            BLI: BL03721(ispH)
            BLD: BLi02695(yqfP)
            BCL: ABC1694
            BPU: BPUM_2249(yqfP)
            GKA: GK2477
            LMO: lmo1451
            LMF: LMOf2365_1470(ispH)
            STH: STH910
            CPE: CPE1085(lytB)
            CPF: CPF_1341(ispH)
            CPR: CPR_1152(ispH)
            CTC: CTC01314
            CNO: NT01CX_2096
            CBA: CLB_1742
            CBH: CLC_1749
            CBF: CLI_1802
            AMT: Amet_2625
            CSC: Csac_1891
            TTE: TTE1352(lytB)
            MPE: MYPE1330
            MTU: Rv1110(lytB2) Rv3382c(lytB1)
            MTC: MT1141(lytB-1) MT3490(lytB-2)
            MBO: Mb1140(lytB2) Mb3414c(lytB1)
            MLE: ML1938(lytB2)
            MPA: MAP2684c(lytB')
            MAV: MAV_1230(ispH)
            MSM: MSMEG_5224(ispH)
            MVA: Mvan_4631
            MGI: Mflv_2079
            MMC: Mmcs_4105
            MKM: Mkms_4181
            MJL: Mjls_4336
            CGL: NCgl0982(cgl1026)
            CGB: cg1164(lytB)
            CEF: CE1079(ispH)
            CDI: DIP0943(lytB)
            CJK: jk1449(ispH)
            NFA: nfa47950(lytB)
            RHA: RHA1_ro05870
            SCO: SCO5058(lytB)
            SMA: SAV3210(ispH)
            TWH: TWT642(ispH1)
            TWS: TW664(ispH)
            LXX: Lxx16760(lytB)
            ART: Arth_2833
            PAC: PPA0572(ispH)
            NCA: Noca_1075
            TFU: Tfu_0471
            FRA: Francci3_0824 Francci3_3881
            FAL: FRAAL1433(ispH) FRAAL6150(ispH)
            ACE: Acel_1858
            KRA: Krad_1123
            SEN: SACE_0939 SACE_4326(ispH)
            STP: Strop_0879
            BLO: BL1361(ispH)
            BAD: BAD_1081(ispH)
            RXY: Rxyl_2212
            RBA: RB9288(lytB)
            CTR: CT859(lytB)
            CTA: CTA_0937(ispH)
            CMU: TC0249(lytB)
            CPN: CPn1017(lytB)
            CPA: CP0836(lytB)
            CPJ: CPj1017(lytB)
            CPT: CpB1055
            CCA: CCA00744(ispH)
            CAB: CAB711(ispH)
            CFE: CF0272(lytB)
            PCU: pc1078(lytB)
            TPA: TP0547
            TDE: TDE1096(ispH)
            LIL: LA2420(lytB)
            LIC: LIC11529(lytB)
            LBJ: LBJ_1807(lytB)
            LBL: LBL_1476(lytB)
            SYN: slr0348
            SYW: SYNW0252(lytB)
            SYC: syc1431_d(lytB)
            SYF: Synpcc7942_0073
            SYD: Syncc9605_0246
            SYE: Syncc9902_0275
            SYG: sync_0292(ispH)
            SYR: SynRCC307_2319(lytB)
            SYX: SynWH7803_0296(lytB)
            CYA: CYA_1148(ispH)
            CYB: CYB_2643(ispH)
            TEL: tlr1041
            GVI: glr3299
            ANA: all0985
            AVA: Ava_2949
            PMA: Pro0296(lytB)
            PMM: PMM0264(lytB)
            PMT: PMT1854(lytB)
            PMN: PMN2A_1630
            PMI: PMT9312_0266
            PMB: A9601_02861(lytB)
            PMC: P9515_02971(lytB)
            PMF: P9303_24821(lytB)
            PMG: P9301_02871(lytB)
            PMH: P9215_02881(lytB)
            PME: NATL1_03421(lytB)
            TER: Tery_4479
            BTH: BT_2061(lytB)
            BFR: BF3748(lytB)
            BFS: BF3536
            PGI: PG0604(ispH)
            SRU: SRU_1880(ispH)
            CHU: CHU_0087(ispH)
            CTE: CT0283(lytB)
            CCH: Cag_0579
            CPH: Cpha266_0414
            PVI: Cvib_1518
            PLT: Plut_1736
            DET: DET1344(ispH)
            DEH: cbdb_A1294(ispH)
            DEB: DehaBAV1_1155
            DRA: DR_2164
            DGE: Dgeo_1010
            TTH: TTC1983(lytB)
            TTJ: TTHA0015
            AAE: aq_1739(lytB)
            TMA: TM1444
            TPT: Tpet_1350
            TME: Tmel_1623
            FNO: Fnod_1233
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.1.2
            ExPASy - ENZYME nomenclature database: 1.17.1.2
            ExplorEnz - The Enzyme Database: 1.17.1.2
            ERGO genome analysis and discovery system: 1.17.1.2
            BRENDA, the Enzyme Database: 1.17.1.2
///
ENTRY       EC 1.17.1.3                 Enzyme
NAME        leucoanthocyanidin reductase;
            leucocyanidin reductase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With NAD+ or NADP+ as acceptor
SYSNAME     (2R,3S)-catechin:NADP+ 4-oxidoreductase
REACTION    (2R,3S)-catechin + NADP+ + H2O = 2,3-trans-3,4-cis-leucocyanidin +
            NADPH + H+ [RN:R06532]
ALL_REAC    R06532;
            (other) R06533 R06615
SUBSTRATE   (2R,3S)-catechin [CPD:C06562];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     2,3-trans-3,4-cis-leucocyanidin [CPD:C05906];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The enzyme catalyses the synthesis of catechin, catechin-4beta-ol
            (leucocyanidin) and the related flavan-3-ols afzelechin and
            gallocatechin, which are initiating monomers in the synthesis of
            plant polymeric proanthocyanidins or condensed tannins. While
            2,3-trans-3,4-cis-leucocyanidin is the preferred flavan-3,4-diol
            substrate, 2,3-trans-3,4-cis-leucodelphinidin and
            2,3-trans-3,4-cis-leucopelargonidin can also act as substrates, but
            more slowly. NADH can replace NADPH but is oxidized more slowly.
REFERENCE   1  [PMID:8470799]
  AUTHORS   Tanner GJ, Kristiansen KN.
  TITLE     Synthesis of 3,4-cis-[3H]leucocyanidin and enzymatic reduction to
            catechin.
  JOURNAL   Anal. Biochem. 209 (1993) 274-7.
  ORGANISM  Onobrychis viciifolia
REFERENCE   2  [PMID:12788945]
  AUTHORS   Tanner GJ, Francki KT, Abrahams S, Watson JM, Larkin PJ, Ashton AR.
  TITLE     Proanthocyanidin biosynthesis in plants. Purification of legume
            leucoanthocyanidin reductase and molecular cloning of its cDNA.
  JOURNAL   J. Biol. Chem. 278 (2003) 31647-56.
  ORGANISM  Desmodium uncinatum
PATHWAY     PATH: map00941  Flavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.1.3
            ExPASy - ENZYME nomenclature database: 1.17.1.3
            ExplorEnz - The Enzyme Database: 1.17.1.3
            ERGO genome analysis and discovery system: 1.17.1.3
            BRENDA, the Enzyme Database: 1.17.1.3
///
ENTRY       EC 1.17.1.4                 Enzyme
NAME        xanthine dehydrogenase;
            NAD+-xanthine dehydrogenase;
            xanthine-NAD+ oxidoreductase;
            xanthine/NAD+ oxidoreductase;
            xanthine oxidoreductase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With NAD+ or NADP+ as acceptor
SYSNAME     xanthine:NAD+ oxidoreductase
REACTION    xanthine + NAD+ + H2O = urate + NADH + H+ [RN:R02103]
ALL_REAC    R02103;
            (other) R01768
SUBSTRATE   xanthine [CPD:C00385];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     urate [CPD:C00366];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     Acts on a variety of purines and aldehydes, including hypoxanthine.
            The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum
            centre. The animal enzyme can be interconverted to EC 1.17.3.2,
            xanthine oxidase (the oxidase form). That from liver exists in vivo
            mainly in the dehydrogenase form, but can be converted into EC
            1.17.3.2 by storage at -20 _degree_C, by treatment with proteolytic
            agents or organic solvents, or by thiol reagents such as Cu2+,
            N-ethylmaleimide or 4-mercuribenzoate. The effect of thiol reagents
            can be reversed by thiols such as 1,4-dithioerythritol. This enzyme
            can also be converted into EC 1.17.3.2 by EC 1.8.4.7, enzyme-thiol
            transhydrogenase (glutathione-disulfide) in the presence of
            glutathione disulfide. In other animal tissues, the enzyme exists
            almost entirely as EC 1.17.3.2, but can be converted into the
            dehydrogenase form by 1,4-dithioerythritol.
REFERENCE   1  [PMID:6960894]
  AUTHORS   Battelli MG, Lorenzoni E.
  TITLE     Purification and properties of a new glutathione-dependent
            thiol:disulphide oxidoreductase from rat liver.
  JOURNAL   Biochem. J. 207 (1982) 133-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4342395]
  AUTHORS   Corte ED, Stirpe F.
  TITLE     The regulation of rat liver xanthine oxidase. Involvement of thiol
            groups in the conversion of the enzyme activity from dehydrogenase
            (type D) into oxidase (type O) and purification of the enzyme.
  JOURNAL   Biochem. J. 126 (1972) 739-45.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:14264879]
  AUTHORS   PARZEN SD, FOX AS.
  TITLE     PURIFICATION OF XANTHINE DEHYDROGENASE FROM DROSOPHILA MELANOGASTER.
  JOURNAL   Biochim. Biophys. Acta. 92 (1964) 465-71.
  ORGANISM  Drosophila melanogaster [GN:dme]
REFERENCE   4  [PMID:4294045]
  AUTHORS   Rajagopalan KV, Handler P.
  TITLE     Purification and properties of chicken liver xanthine dehydrogenase.
  JOURNAL   J. Biol. Chem. 242 (1967) 4097-107.
  ORGANISM  chicken [GN:gga]
REFERENCE   5  [PMID:6061702]
  AUTHORS   Smith ST, Rajagopalan KV, Handler P.
  TITLE     Purification and properties of xanthine dehydroganase from
            Micrococcus lactilyticus.
  JOURNAL   J. Biol. Chem. 242 (1967) 4108-17.
  ORGANISM  Micrococcus lactilyticus
REFERENCE   6  [PMID:11341925]
  AUTHORS   Parschat K, Canne C, Huttermann J, Kappl R, Fetzner S.
  TITLE     Xanthine dehydrogenase from Pseudomonas putida 86: specificity,
            oxidation-reduction potentials of its redox-active centers, and
            first EPR characterization.
  JOURNAL   Biochim. Biophys. Acta. 1544 (2001) 151-65.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   7  [PMID:8224915]
  AUTHORS   Ichida K, Amaya Y, Noda K, Minoshima S, Hosoya T, Sakai O, Shimizu
            N, Nishino T.
  TITLE     Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase):
            structural analysis of the protein and chromosomal location of the
            gene.
  JOURNAL   Gene. 133 (1993) 279-84.
  ORGANISM  human [GN:hsa]
REFERENCE   8  [PMID:11005854]
  AUTHORS   Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, Pai EF.
  TITLE     Crystal structures of bovine milk xanthine dehydrogenase and
            xanthine oxidase: structure-based mechanism of conversion.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 10723-8.
  ORGANISM  cow [GN:bta]
REFERENCE   9  [PMID:11796116]
  AUTHORS   Truglio JJ, Theis K, Leimkuhler S, Rappa R, Rajagopalan KV, Kisker
            C.
  TITLE     Crystal structures of the active and alloxanthine-inhibited forms of
            xanthine dehydrogenase from Rhodobacter capsulatus.
  JOURNAL   Structure. (Camb). 10 (2002) 115-25.
  ORGANISM  Rhodobacter capsulatus
REFERENCE   10 [PMID:11848841]
  AUTHORS   Hille R.
  TITLE     The Mononuclear Molybdenum Enzymes.
  JOURNAL   Chem. Rev. 96 (1996) 2757-2816.
  ORGANISM  rat [GN:rno], Drosophila melanogaster [GN:dme], chicken [GN:gga],
            Micrococcus lactilyticus, human [GN:hsa], Chlamydomonas reinhardtii
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K00087  xanthine dehydrogenase
GENES       HSA: 7498(XDH)
            MMU: 22436(Xdh)
            RNO: 497811(Xdh)
            CFA: 483028(XDH)
            BTA: 280960(XDH)
            GGA: 396025(XDH)
            SPU: 576712(LOC576712)
            DME: Dmel_CG7642(ry)
            CEL: F15E6.6 F55B11.1
            ATH: AT4G34890(ATXDH1)
            ANI: AN5613.2
            AFM: AFUA_4G11220
            AOR: AO090003001099
            DDI: DDB_0230176(xdh)
            ECO: b0284(yagR) b0285(yagS) b2866(xdhA) b2867(xdhB)
            ECJ: JW0278(yagR) JW0279(yagS) JW2835(xdhB) JW5462(xdhA)
            ECE: Z0350(yagR) Z0351(yagS) Z4205 Z4206(ygeT)
            ECS: ECs0314 ECs0315 ECs3739 ECs3740
            ECC: c3444 c3445(ygeT)
            ECI: UTI89_C3251 UTI89_C3252(ygeT)
            ECP: ECP_2860 ECP_2861
            ECV: APECO1_3658(ygeT)
            ECW: EcE24377A_3192(xdhB)
            ECX: EcHS_A3026(xdhA) EcHS_A3027(xdhB)
            SFL: SF2868(ygeS) SF2869(ygeT)
            SFX: S3068 S3069(ygeT)
            SFV: SFV_2931 SFV_2932(ygeT)
            SSN: SSON_3017 SSON_3018(ygeT)
            SBO: SBO_3118(ygeT) SBO_3119
            SPE: Spro_2301
            XCC: XCC1091 XCC1092 XCC2727(yagR) XCC2728(yagS) XCC3709(yagR)
            XCB: XC_1386 XC_1387 XC_3157 XC_3158 XC_3780
            XCV: XCV1214 XCV1215 XCV3044 XCV3045
            XAC: XAC1187 XAC1188 XAC2893(yagR) XAC2894(yagS)
            PPR: PBPRA2243 PBPRA2244
            PAE: PA1523(xdhB) PA1524(xdhA)
            PAU: PA14_44710(xdhA) PA14_44740(xdhB)
            PAP: PSPA7_3809(xdhA) PSPA7_3810(xdhB)
            PPU: PP_4278(xdhA) PP_4279(xdhB)
            PPF: Pput_1589
            PST: PSPTO_2863 PSPTO_3660 PSPTO_3661
            PSB: Psyr_1814 Psyr_1815
            PSP: PSPPH_1774 PSPPH_1775(xdhA)
            PFL: PFL_1888(xdhB) PFL_1889(xdhA)
            PFO: Pfl_1796 Pfl_1797 Pfl_2107
            PEN: PSEEN1764 PSEEN1765 PSEEN2875
            PMY: Pmen_2752
            PCR: Pcryo_1140 Pcryo_1141 Pcryo_1807
            ACI: ACIAD2466 ACIAD2467(xdhB) ACIAD2468(xdhA)
            SDN: Sden_1106
            SFR: Sfri_0860
            CPS: CPS_4864 CPS_4865
            PAT: Patl_2424 Patl_2425
            HCH: HCH_01098(xdhB) HCH_01099(xdhA)
            CSA: Csal_1788 Csal_1789
            MMW: Mmwyl1_2698
            AHA: AHA_2177 AHA_2178
            RSO: RSc2095(xdhA) RSc2096(xdhB)
            REU: Reut_A2425 Reut_A2426 Reut_A3076 Reut_B3594
            REH: H16_A1016(xdhB1) H16_A1017(xdhA1) H16_B1897(xdhA2)
                 H16_B1898(xdhB2)
            RME: Rmet_0892 Rmet_0893
            BMA: BMA2041 BMA2042
            BXE: Bxe_A0949 Bxe_A0950 Bxe_A3885 Bxe_A3886 Bxe_B1320
            BVI: Bcep1808_0770
            BUR: Bcep18194_A3925 Bcep18194_B1541
            BCN: Bcen_0349
            BCH: Bcen2424_0833 Bcen2424_4420
            BAM: Bamb_0712
            BPS: BPSL2727(xdhB) BPSL2728(xdhA)
            BPM: BURPS1710b_3213(xdhB) BURPS1710b_3215(xdhA)
            BPL: BURPS1106A_3198(xdhB)
            BPD: BURPS668_3159(xdhB) BURPS668_3160(xdhA)
            BTE: BTH_I1408 BTH_I1409
            POL: Bpro_1480 Bpro_1481
            PNA: Pnap_1034
            AAV: Aave_1129 Aave_1485
            AJS: Ajs_3103
            VEI: Veis_5001
            MPT: Mpe_A0798 Mpe_A0799
            MMS: mma_0506(xdhB) mma_0507(xdhA)
            EBA: ebA2062
            AZO: azo2211(xdhA) azo2212(xdhB)
            BBA: Bd2633(xdhA) Bd2634(xdhB)
            DPS: DP2531(coxL)
            SFU: Sfum_2012
            MLO: mlr5134 mlr5135
            MES: Meso_2833 Meso_2834
            SME: SMb20132 SMb20846(xdhB2) SMb21011(xdhA2) SMb21286(xdhA1)
                 SMb21287(xdhB1)
            SMD: Smed_4498 Smed_4621
            ATU: Atu2309(xdhA) Atu2310(xdhB)
            ATC: AGR_C_4202 AGR_C_4204
            RET: RHE_CH03124(xdhA) RHE_CH03125(xdhB)
            RLE: RL3570(xdhA) RL3571(xdhB) pRL120300(yagR) pRL120301(yagS)
                 pRL80025
            BME: BMEI1575 BMEI1576
            BMF: BAB1_0377
            BMS: BR0349 BR0350
            BMB: BruAb1_0375 BruAb1_0376
            BOV: BOV_0365(xdhA)
            OAN: Oant_0452
            BJA: blr5211
            BRA: BRADO2883 BRADO2884 BRADO5140 BRADO5689 BRADO5690 BRADO6665
            BBT: BBta_0870 BBta_5607 BBta_6204 BBta_6205
            RPC: RPC_1131 RPC_4640
            RPE: RPE_3213
            XAU: Xaut_3760
            CCR: CC_2618
            SIL: SPO0653(xdhB) SPO0654(xdhA)
            SIT: TM1040_0498 TM1040_2704 TM1040_2705
            RSP: RSP_3206 RSP_3554(xdhA) RSP_3555(xdhB)
            RSH: Rsph17029_3945
            JAN: Jann_0936 Jann_0937 Jann_2947
            RDE: RD1_1532 RD1_4068(xdhA) RD1_4069(xdhB) RD1_4070(xdhC)
            PDE: Pden_4258
            HNE: HNE_1071 HNE_1072
            SWI: Swit_0835
            GOX: GOX0653 GOX0654
            ACR: Acry_1154
            SUS: Acid_0356
            BSU: BG13988(pucE) BG13989(pucD) BG13990(pucC) BG13992(pucA)
            BCE: BC3165 BC3167 BC3168
            BCL: ABC3740(pucA) ABC3741(pucB) ABC3742(pucC) ABC3743(pucD)
                 ABC3744(pucE)
            CDF: CD2073(xdhA1) CD2074(pucC1) CD2079(xdhA2) CD2080(pucC2)
                 CD3177(xdhA3)
            CBO: CBO0258(xdhA1) CBO0259(xdhB2) CBO1285(xdhA2) CBO1286(xdhB2)
                 CBO2881(xdhAC)
            CBE: Cbei_1984
            AMT: Amet_0607
            MTA: Moth_1959 Moth_1960
            RHA: RHA1_ro00134(xdhB) RHA1_ro00135(xdhA) RHA1_ro05013
            SCO: SCO4971(2SCK31.31) SCO4972(2SCK31.32)
            NCA: Noca_0612 Noca_1169 Noca_1637
            FRA: Francci3_0838
            FAL: FRAAL1457 FRAAL1458 FRAAL1459
            ACE: Acel_1642
            SEN: SACE_1261 SACE_3092(xdhB) SACE_3093(xdhA) SACE_4467(yagS)
                 SACE_4468 SACE_4618 SACE_4872
            RXY: Rxyl_2839
            AVA: Ava_C0126
            RRS: RoseRS_1142
            DRA: DR_A0177 DR_A0178
            DGE: Dgeo_2603 Dgeo_2604
STRUCTURES  PDB: 2E1Q  2E3T  
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.1.4
            ExPASy - ENZYME nomenclature database: 1.17.1.4
            ExplorEnz - The Enzyme Database: 1.17.1.4
            ERGO genome analysis and discovery system: 1.17.1.4
            BRENDA, the Enzyme Database: 1.17.1.4
///
ENTRY       EC 1.17.1.5                 Enzyme
NAME        nicotinate dehydrogenase;
            nicotinic acid hydroxylase;
            nicotinate hydroxylase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With NAD+ or NADP+ as acceptor
SYSNAME     nicotinate:NADP+ 6-oxidoreductase (hydroxylating)
REACTION    nicotinate + H2O + NADP+ = 6-hydroxynicotinate + NADPH + H+
            [RN:R01720]
ALL_REAC    R01720
SUBSTRATE   nicotinate [CPD:C00253];
            H2O [CPD:C00001];
            NADP+ [CPD:C00006]
PRODUCT     6-hydroxynicotinate [CPD:C01020];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023]
COMMENT     A flavoprotein containing non-heme iron. The enzyme is capable of
            acting on a variety of nicotinate analogues to varying degrees,
            including pyrazine-2-carboxylate, pyrazine 2,3-dicarboxylate,
            trigonelline and 6-methylnicotinate. The enzyme from Clostridium
            barkeri also possesses a catalytically essential, labile selenium
            that can be removed by reaction with cyanide.
REFERENCE   1  [PMID:4388026]
  AUTHORS   Holcenberg JS, Stadtman ER.
  TITLE     Nicotinic acid metabolism. 3. Purification and properties of a
            nicotinic acid hydroxylase.
  JOURNAL   J. Biol. Chem. 244 (1969) 1194-203.
  ORGANISM  Clostridium sp.
REFERENCE   2  [PMID:8555176]
  AUTHORS   Gladyshev VN, Khangulov SV, Stadtman TC.
  TITLE     Properties of the selenium- and molybdenum-containing nicotinic acid
            hydroxylase from Clostridium barkeri.
  JOURNAL   Biochemistry. 35 (1996) 212-23.
  ORGANISM  Clostridium barkeri
REFERENCE   3  [PMID:8278371]
  AUTHORS   Gladyshev VN, Khangulov SV, Stadtman TC.
  TITLE     Nicotinic acid hydroxylase from Clostridium barkeri: electron
            paramagnetic resonance studies show that selenium is coordinated
            with molybdenum in the catalytically active selenium-dependent
            enzyme.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 232-6.
  ORGANISM  Clostridium barkeri
REFERENCE   4  [PMID:6838209]
  AUTHORS   Dilworth GL.
  TITLE     Occurrence of molybdenum in the nicotinic acid hydroxylase from
            Clostridium barkeri.
  JOURNAL   Arch. Biochem. Biophys. 221 (1983) 565-9.
  ORGANISM  Clostridium barkeri
REFERENCE   5
  AUTHORS   Dilworth, G.L.
  TITLE     Properties of the selenium-containing moiety of nicotinic-acid
            hydroxylase from Clostridium barkeri.
  JOURNAL   Arch. Biochem. Biophys. 219 (1983) 30-38.
  ORGANISM  Clostridium barkeri
REFERENCE   6
  AUTHORS   Nagel, M. and Andreesen, J.R.
  TITLE     Purification and characterization of the molybdoenzymes nicotinate
            dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus
            niacini.
  JOURNAL   Arch. Microbiol. 154 (1990) 605-613.
  ORGANISM  Bacillus niacini
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.1.5
            ExPASy - ENZYME nomenclature database: 1.17.1.5
            ExplorEnz - The Enzyme Database: 1.17.1.5
            ERGO genome analysis and discovery system: 1.17.1.5
            BRENDA, the Enzyme Database: 1.17.1.5
            CAS: 9059-03-4
///
ENTRY       EC 1.17.1.6       Obsolete  Enzyme
NAME        Transferred to 1.17.99.5
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With NAD+ or NADP+ as acceptor
COMMENT     Transferred entry: now EC 1.17.99.5, bile-acid 7alpha-dehydroxylase.
            It is now known that FAD is the acceptor and not NAD+ as was thought
            previously. (EC 1.17.1.6 created 2005, deleted 2006)
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.1.6
            ExPASy - ENZYME nomenclature database: 1.17.1.6
            ExplorEnz - The Enzyme Database: 1.17.1.6
            ERGO genome analysis and discovery system: 1.17.1.6
            BRENDA, the Enzyme Database: 1.17.1.6
///
ENTRY       EC 1.17.3.1                 Enzyme
NAME        pteridine oxidase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With oxygen as acceptor
SYSNAME     2-amino-4-hydroxypteridine:oxygen oxidoreductase (7-hydroxylating)
REACTION    2-amino-4-hydroxypteridine + O2 = 2-amino-4,7-dihydroxypteridine +
            (?) [RN:R02816]
ALL_REAC    R02816
SUBSTRATE   2-amino-4-hydroxypteridine [CPD:C00715];
            O2 [CPD:C00007]
PRODUCT     2-amino-4,7-dihydroxypteridine [CPD:C03975]
COMMENT     Different from EC 1.17.3.2 xanthine oxidase; does not act on
            hypoxanthine.
REFERENCE   1
  AUTHORS   Yong, Y.-N.
  TITLE     Detection of a pteridine oxidase in plants.
  JOURNAL   Plant Sci. Lett. 18 (1980) 169-175.
  ORGANISM  Ricinus communis
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.3.1
            ExPASy - ENZYME nomenclature database: 1.17.3.1
            ExplorEnz - The Enzyme Database: 1.17.3.1
            ERGO genome analysis and discovery system: 1.17.3.1
            BRENDA, the Enzyme Database: 1.17.3.1
            CAS: 74082-65-8
///
ENTRY       EC 1.17.3.2                 Enzyme
NAME        xanthine oxidase;
            hypoxanthine oxidase;
            hypoxanthine:oxygen oxidoreductase;
            Schardinger enzyme;
            xanthine oxidoreductase;
            hypoxanthine-xanthine oxidase;
            xanthine:O2 oxidoreductase;
            xanthine:xanthine oxidase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With oxygen as acceptor
SYSNAME     xanthine:oxygen oxidoreductase
REACTION    xanthine + H2O + O2 = urate + H2O2 [RN:R02107]
ALL_REAC    R02107;
            (other) R01769 R07942 R07977 R07978 R07979
SUBSTRATE   xanthine [CPD:C00385];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     urate [CPD:C00366];
            H2O2 [CPD:C00027]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023];
            Molybdenum [CPD:C00150];
            Iron-sulfur [CPD:C00824];
            Molybdopterin [CPD:C05924]
INHIBITOR   Disulfiram [CPD:C01692]
COMMENT     An iron-molybdenum flavoprotein (FAD) containing [2Fe-2S] centres.
            Also oxidizes hypoxanthine, some other purines and pterins, and
            aldehydes (i.e. possesses the activity of EC 1.2.3.1, aldehyde
            oxidase). Under some conditions the product is mainly superoxide
            rather than peroxide: RH + H2O + 2 O2 = ROH + 2 O2.- + 2 H+. The
            enzyme from animal tissues can be converted into EC 1.17.1.4,
            xanthine dehydrogenase. That from liver exists in vivo mainly as the
            dehydrogenase form, but can be converted into the oxidase form by
            storage at -20 _degree_C, by treatment with proteolytic enzymes or
            with organic solvents, or by thiol reagents such as Cu2+,
            N-ethylmaleimide or 4-mercuribenzoate. The effect of thiol reagents
            can be reversed by thiols such as 1,4-dithioerythritol. EC 1.17.1.4
            can also be converted into this enzyme by EC 1.8.4.7, enzyme-thiol
            transhydrogenase (glutathione-disulfide) in the presence of
            glutathione disulfide. The Micrococcus enzyme can use ferredoxin as
            acceptor.
REFERENCE   1
  AUTHORS   Avis, P.G., Bergel, F. and Bray, R.C.
  TITLE     Cellular constituents. The chemistry of xanthine oxidase. Part I.
            The preparation of a crystalline xanthine oxidase from cow's milk.
  JOURNAL   J. Chem. Soc. (Lond.) (1955) 1100-1105.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:6960894]
  AUTHORS   Battelli MG, Lorenzoni E.
  TITLE     Purification and properties of a new glutathione-dependent
            thiol:disulphide oxidoreductase from rat liver.
  JOURNAL   Biochem. J. 207 (1982) 133-8.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Bray, R.C.
  TITLE     Xanthine oxidase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 7, Academic Press, New York, 1963, p. 533-556.
REFERENCE   4  [PMID:4342395]
  AUTHORS   Corte ED, Stirpe F.
  TITLE     The regulation of rat liver xanthine oxidase. Involvement of thiol
            groups in the conversion of the enzyme activity from dehydrogenase
            (type D) into oxidase (type O) and purification of the enzyme.
  JOURNAL   Biochem. J. 126 (1972) 739-45.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:2350174]
  AUTHORS   Carpani G, Racchi M, Ghezzi P, Terao M, Garattini E.
  TITLE     Purification and characterization of mouse liver xanthine oxidase.
  JOURNAL   Arch. Biochem. Biophys. 279 (1990) 237-41.
  ORGANISM  mouse [GN:mmu]
REFERENCE   6  [PMID:11092937]
  AUTHORS   Eger BT, Okamoto K, Enroth C, Sato M, Nishino T, Pai EF, Nishino T.
  TITLE     Purification, crystallization and preliminary X-ray diffraction
            studies of xanthine dehydrogenase and xanthine oxidase isolated from
            bovine milk.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 56 Pt 12 (2000) 1656-8.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00232  Caffeine metabolism
ORTHOLOGY   KO: K00106  xanthine oxidase
GENES       HSA: 7498(XDH)
            MMU: 22436(Xdh)
            RNO: 497811(Xdh)
            CFA: 483028(XDH)
            BTA: 280960(XDH)
            GGA: 396025(XDH)
            SPU: 576712(LOC576712)
            CEL: F15E6.6
            ATH: AT4G34890(ATXDH1)
            ANI: AN5613.2
            AFM: AFUA_4G11220
            AOR: AO090003001099
STRUCTURES  PDB: 2CKJ  2E1Q  2E3T  
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.3.2
            ExPASy - ENZYME nomenclature database: 1.17.3.2
            ExplorEnz - The Enzyme Database: 1.17.3.2
            ERGO genome analysis and discovery system: 1.17.3.2
            UM-BBD (Biocatalysis/Biodegradation Database): 1.17.3.2
            BRENDA, the Enzyme Database: 1.17.3.2
            CAS: 9002-17-9
///
ENTRY       EC 1.17.3.3                 Enzyme
NAME        6-hydroxynicotinate dehydrogenase;
            6-hydroxynicotinic acid hydroxylase;
            6-hydroxynicotinic acid dehydrogenase;
            6-hydroxynicotinate hydroxylase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With oxygen as acceptor
SYSNAME     6-hydroxynicotinate:O2 oxidoreductase
REACTION    6-hydroxynicotinate + H2O + O2 = 2,6-dihydroxynicotinate + H2O2
            [RN:R07221]
ALL_REAC    R07221
SUBSTRATE   6-hydroxynicotinate [CPD:C01020];
            H2O [CPD:C00001];
            O2 [CPD:C00007]
PRODUCT     2,6-dihydroxynicotinate [CPD:C15523];
            H2O2 [CPD:C00027]
COMMENT     Contains [2Fe-2S] iron-sulfur centres, FAD and molybdenum. It also
            has a catalytically essential, labile selenium that can be removed
            by reaction with cyanide. In Bacillus niacini, this enzyme is
            required for growth on nicotinic acid.
REFERENCE   1
  AUTHORS   Nagel, M. and Andreesen, J.R.
  TITLE     Molybdenum-dependent degradation of nicotinic acid by Bacillus sp.
            DSM 2923.
  JOURNAL   FEMS Microbiol. Lett. 59 (1989) 147-152.
  ORGANISM  Bacillus sp.
REFERENCE   2
  AUTHORS   Nagel, M. and Andreesen, J.R.
  TITLE     Purification and characterization of the molybdoenzymes nicotinate
            dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus
            niacini.
  JOURNAL   Arch. Microbiol. 154 (1990) 605-613.
  ORGANISM  Bacillus niacini
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.3.3
            ExPASy - ENZYME nomenclature database: 1.17.3.3
            ExplorEnz - The Enzyme Database: 1.17.3.3
            ERGO genome analysis and discovery system: 1.17.3.3
            BRENDA, the Enzyme Database: 1.17.3.3
///
ENTRY       EC 1.17.4.1                 Enzyme
NAME        ribonucleoside-diphosphate reductase;
            ribonucleotide reductase;
            CDP reductase;
            ribonucleoside diphosphate reductase;
            UDP reductase;
            ADP reductase;
            nucleoside diphosphate reductase;
            ribonucleoside 5'-diphosphate reductase;
            ribonucleotide diphosphate reductase;
            2'-deoxyribonucleoside-diphosphate:oxidized-thioredoxin
            2'-oxidoreductase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With a disulfide as acceptor
SYSNAME     2'-deoxyribonucleoside-diphosphate:thioredoxin-disulfide
            2'-oxidoreductase
REACTION    2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O =
            ribonucleoside diphosphate + thioredoxin [RN:R04294]
ALL_REAC    R04294 > R02017 R02018 R02019 R02024
SUBSTRATE   2'-deoxyribonucleoside diphosphate [CPD:C04232];
            thioredoxin disulfide [CPD:C00343];
            H2O [CPD:C00001]
PRODUCT     ribonucleoside diphosphate [CPD:C03723];
            thioredoxin [CPD:C00342]
COFACTOR    ATP [CPD:C00002];
            Iron [CPD:C00023]
COMMENT     An iron protein. Requires ATP.
REFERENCE   1
  AUTHORS   Lammers, M. and Follmann, H.
  TITLE     The ribonucleotide reductases - a unique group of metalloenzymes
            essential for cell-proliferation.
  JOURNAL   Struct. Bonding 54 (1983) 27-91.
REFERENCE   2  [PMID:4543472]
  AUTHORS   Larsson A.
  TITLE     Ribonucleotide reductase from regenerating rat liver. II. Substrate
            phosphorylation level and effect of deoxyadenosine triphosphate.
  JOURNAL   Biochim. Biophys. Acta. 324 (1973) 447-51.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:5330119]
  AUTHORS   Larsson A, Reichard P.
  TITLE     Enzymatic synthesis of deoxyribonucleotides. IX. Allosteric effects
            in the reduction of pyrimidine ribonucleotides by the ribonucleoside
            diphosphate reductase system of Escherichia coli.
  JOURNAL   J. Biol. Chem. 241 (1966) 2533-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:5330120]
  AUTHORS   Larsson A, Reichard P.
  TITLE     Enzymatic synthesis of deoxyribonucleotides. X. Reduction of purine
            ribonucleotides; allosteric behavior and substrate specificity of
            the enzyme system from Escherichia coli B.
  JOURNAL   J. Biol. Chem. 241 (1966) 2540-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:5926184]
  AUTHORS   Moore EC, Hurlbert RB.
  TITLE     Regulation of mammalian deoxyribonucleotide biosynthesis by
            nucleotides as activators and inhibitors.
  JOURNAL   J. Biol. Chem. 241 (1966) 4802-9.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
            PATH: map04115  p53 signaling pathway
ORTHOLOGY   KO: K00524  ribonucleoside-diphosphate reductase
            KO: K00525  ribonucleoside-diphosphate reductase alpha chain
            KO: K00526  ribonucleoside-diphosphate reductase beta chain
GENES       HSA: 50484(RRM2B) 6240(RRM1) 6241(RRM2)
            PTR: 472832(RRM2B)
            MMU: 20133(Rrm1) 20135(Rrm2) 382985(Rrm2b)
            RNO: 304657(RGD1559671_predicted) 362720(Rrm2)
            CFA: 476823(RRM1) 481988(RRM2B) 482963(RRM2)
            GGA: 419081(RCJMB04_2p9) 420253(RRM2B) 421936(RRM2)
            XLA: 379056(MGC52676) 380465(rrm2) 399431(RRM1) 443815(MGC78958)
            XTR: 394645(rrm2) 493274(rrm2)
            DRE: 30733(rrm2) 30740(rrm1)
            SPU: 577596(LOC577596) 581431(LOC581431)
            DME: Dmel_CG5371(RnrL) Dmel_CG8975(RnrS)
            CEL: C03C10.3(rnr-2) F19G12.2 T23G5.1(rnr-1)
            ATH: AT2G21790(R1/RIBONUCLEOTIDE_REDUCTASE) AT3G23580(RNR2/RNR2A)
                 AT3G27060(TSO2)
            OSA: 4331059 4339981 4340258
            CME: CMK035C CML050C CMM323C
            SCE: YER070W(RNR1) YGR180C(RNR4) YIL066C(RNR3) YJL026W(RNR2)
            AGO: AGOS_AAL136C AGOS_ACR155W AGOS_ADL057W
            PIC: PICST_29856(RNR1.1) PICST_70259(RNR2) PICST_75662(RNR1.2)
            CGR: CAGL0D03432g CAGL0G04213g CAGL0J03146g
            SPO: SPAC1F7.05(cdc22) SPBC25D12.04(suc22)
            ANI: AN0067.2 AN4380.2
            AFM: AFUA_4G06690 AFUA_5G12350
            AOR: AO090023000916 AO090120000352
            CNE: CNE03330 CNK01530 CNK02580
            UMA: UM04325.1 UM06368.1
            ECU: ECU06_0730 ECU10_0920
            DDI: DDBDRAFT_0217423 DDB_0230075(rnrA)
            PFA: PF10_0154 PF14_0053 PF14_0352
            CPV: cgd6_1950 cgd6_690
            CHO: Chro.60090 Chro.60091 Chro.60230
            TAN: TA05060 TA06715 TA09665
            TPV: TP01_0725 TP03_0528
            TET: TTHERM_00028540 TTHERM_00242370
            TBR: Tb11.02.5720 Tb11.v4.0004 Tb11.v4.0005 Tb11.v4.0006
                 Tb11.v4.0007
            TCR: 504073.30 506621.30 506933.20 511555.80
            LMA: LmjF22.1290 LmjF27.2050 LmjF28.0890
            ECO: b2234(nrdA) b2235(nrdB) b2675(nrdE) b2676(nrdF)
            ECJ: JW2228(nrdA) JW2229(nrdB) JW2650(nrdE) JW2651(nrdF)
            ECE: Z3489(nrdA) Z3491(nrdB) Z3977(nrdE) Z3978(nrdF)
            ECS: ECs3117 ECs3118 ECs3538 ECs3539
            ECC: c2776(nrdA) c2777(nrdB) c3228(nrdE) c3229(nrdF)
            ECI: UTI89_C2515(nrdA) UTI89_C2516(nrdB) UTI89_C3035(nrdE)
                 UTI89_C3036(nrdF)
            ECP: ECP_2277 ECP_2278 ECP_2640 ECP_2641
            ECV: APECO1_3845(nrdF) APECO1_3846(nrdE) APECO1_4325(nrdB)
                 APECO1_4326(nrdA)
            ECW: EcE24377A_2531(nrdA) EcE24377A_2532(nrdB)
                 EcE24377A_2956(nrdE) EcE24377A_2957(nrdF)
            ECX: EcHS_A2374 EcHS_A2375 EcHS_A2811 EcHS_A2812 EcHS_A2929(rumA)
            STY: HCM2.0121c HCM2.0122c STY2506(nrdA) STY2507(nrdB)
                 STY2932(nrdE) STY2933(nrdF)
            STT: t0586(nrdB) t0587(nrdA) t2704(nrdE) t2705(nrdF)
            SPT: SPA0586(nrdB) SPA0587(nrdA) SPA2665(nrdE)
            SEC: SC2280(nrdA) SC2281(nrdB) SC2741(nrdE) SC2742(nrdF)
            STM: STM2277(nrdA) STM2278(nrdB) STM2807(nrdE) STM2808(nrdF)
            YPE: YPO1213(nrdB) YPO1214(nrdA) YPO2648(nrdF) YPO2649(nrdE)
            YPK: y1222(nrdF) y1223(nrdE) y2974(nrdA) y2975(nrdB)
            YPM: YP_0923(nrdA) YP_0924(nrdB) YP_2450(nrdF) YP_2451(nrdE)
                 YP_pMT046 YP_pMT047
            YPA: YPA_0927 YPA_0928 YPA_2376 YPA_2377
            YPN: YPN_1134 YPN_1135 YPN_2763 YPN_2764
            YPP: YPDSF_1623 YPDSF_1624 YPDSF_2479 YPDSF_2480 YPDSF_4070
                 YPDSF_4071
            YPS: YPTB1253(nrdB) YPTB1254(nrdA) YPTB2957(nrdE) YPTB2958(nrdF)
            YPI: YpsIP31758_1063 YpsIP31758_2769(nrdA) YpsIP31758_2770
            YEN: YE0927(nrdE) YE1393(dnaF)
            SFL: SF2316(nrdA) SF2317(nrdB) SF2703(nrdE) SF2704(nrdF)
            SFX: S2449(nrdA) S2450(nrdB) S2889(nrdE) S2890(nrdF)
            SFV: SFV_2307(nrdA) SFV_2308(nrdB) SFV_2827(nrdF) SFV_2828(nrdE)
            SSN: SSON_2293(nrdA) SSON_2294(nrdB) SSON_2820(nrdE)
                 SSON_2821(nrdF)
            SBO: SBO_2059(nrdB) SBO_2060(nrdA) SBO_2841(nrdF) SBO_2842(nrdE)
            SDY: SDY_2428(nrdA) SDY_2429(nrdB) SDY_2868(nrdE) SDY_2869(nrdF)
            ECA: ECA1198(nrdB) ECA1199(nrdA) ECA3337(nrdE) ECA3338(nrdF)
            PLU: plu1284(nrdF) plu1285(nrdE) plu3052(nrdA) plu3053(nrdB)
            BUC: BU178(nrdB) BU179(nrdA)
            BAS: BUsg172(nrdB) BUsg173(nrdA)
            BAB: bbp167(nrdB) bbp168(nrdA)
            WBR: WGLp609(nrdF) WGLp610(nrdE)
            SGL: SG1584 SG1585
            ENT: Ent638_2801 Ent638_2802 Ent638_3155 Ent638_3156
            SPE: Spro_3271 Spro_3272 Spro_3723 Spro_3724
            BFL: Bfl478(nrdA) Bfl479(nrdB)
            BPN: BPEN_494(nrdA) BPEN_495(nrdB)
            HIN: HI1659(nrdA) HI1660(nrdB)
            HIT: NTHI1961(nrdA) NTHI1962(nrdB)
            HIP: CGSHiEE_03750(nrdB) CGSHiEE_03760
            HIQ: CGSHiGG_01995(nrdB)
            HDU: HD1731(nrdA) HD1732(nrdB)
            HSO: HS_0961(nrdB) HS_1196(nrdA)
            PMU: PM0717(nrdA) PM0719(nrdB)
            MSU: MS0968(nrdF) MS0992(nrdA)
            APL: APL_0147 APL_0148(rnr1) APL_0992(nrdA) APL_0993(nrdB)
            ASU: Asuc_1466 Asuc_1480
            XFA: XF1196 XF1197
            XFT: PD0480(nrdA) PD0481(nrdB)
            XCC: XCC3985(nrdB) XCC3986(nrdA)
            XCB: XC_4075 XC_4076
            XCV: XCV4160(nrdB) XCV4161(nrdA)
            XAC: XAC4074(nrdB) XAC4075(nrdA)
            XOO: XOO0474(nrdA) XOO0475(nrdB)
            XOM: XOO_0439(XOO0439) XOO_0440(XOO0440)
            VCH: VC1255 VC1256
            VCO: VC0395_A0874(nrdB) VC0395_A0875(nrdA)
            VVU: VV1_3041 VV1_3042
            VVY: VV1243 VV1244
            VPA: VP1934 VP1935
            VFI: VF1201 VF1202
            PPR: PBPRA2142 PBPRA2459 PBPRA2460(nrdB)
            PAE: PA1155(nrdB) PA1156(nrdA) PA5497
            PAU: PA14_49460(nrdA) PA14_49470(nrdB)
            PAP: PSPA7_4224 PSPA7_6298
            PPU: PP_1177(nrdB) PP_1179(nrdA)
            PPF: Pput_1209 Pput_1210
            PST: PSPTO_1661(nrdB) PSPTO_1671(nrdA)
            PSB: Psyr_3717 Psyr_3721
            PSP: PSPPH_3738(nrdA) PSPPH_3745(nrdB)
            PFL: PFL_4476 PFL_4524
            PFO: Pfl_4246 Pfl_4295
            PEN: PSEEN1335(nrdB) PSEEN1337(nrdA)
            PMY: Pmen_3151 Pmen_3152
            PAR: Psyc_1263(nrdA) Psyc_1268(nrdB)
            PCR: Pcryo_1117 Pcryo_1122
            PRW: PsycPRwf_1577 PsycPRwf_1578
            ACI: ACIAD0722(nrdB) ACIAD0724(nrdA)
            ACB: A1S_0747
            SON: SO_2415(nrdA) SO_2416(nrdB)
            SDN: Sden_1952 Sden_1953
            SFR: Sfri_2133 Sfri_2134
            SAZ: Sama_1727 Sama_1728
            SBL: Sbal_2058 Sbal_2059
            SBM: Shew185_2290 Shew185_2291
            SLO: Shew_1945 Shew_1946
            SPC: Sputcn32_2073 Sputcn32_2074
            SSE: Ssed_2306 Ssed_2307
            SPL: Spea_2063 Spea_2064
            SHE: Shewmr4_1915 Shewmr4_1916
            SHM: Shewmr7_2062 Shewmr7_2063
            SHN: Shewana3_1968 Shewana3_1969
            SHW: Sputw3181_1938 Sputw3181_1939
            ILO: IL1363(nrdA) IL1364(nrdB)
            CPS: CPS_2327(nrdB) CPS_2328(nrdA)
            PHA: PSHAa1417(nrdB) PSHAa1418(nrdA)
            PAT: Patl_2473 Patl_2474
            SDE: Sde_2458 Sde_2459 Sde_3460
            PIN: Ping_1109 Ping_1112
            MAQ: Maqu_1085 Maqu_3856 Maqu_3857
            CBU: CBU_1553(nrdA) CBU_1554(nrdB)
            CBD: COXBU7E912_0435 COXBU7E912_0436
            LPN: lpg1774(nrdA) lpg1775(nrdB)
            LPF: lpl1738(rir1) lpl1739(rir2)
            LPP: lpp1738(rir1) lpp1739(rir2)
            MCA: MCA1634(nrdA) MCA1637(nrdB) MCA2543
            FTU: FTT0532c(nrdB) FTT0534c(nrdA)
            FTF: FTF0532c(grxC) FTF0534c(nrdA)
            FTW: FTW_1008(nrdA) FTW_1010
            FTL: FTL_0984 FTL_0986
            FTH: FTH_0963 FTH_0965(nrdA)
            FTA: FTA_1039
            FTN: FTN_0981(nrdA) FTN_0983
            TCX: Tcr_0463 Tcr_1763
            NOC: Noc_2527 Noc_2528
            AEH: Mlg_2102 Mlg_2103
            HCH: HCH_04895 HCH_06928 HCH_06929
            CSA: Csal_0379 Csal_0380 Csal_0667 Csal_0668
            ABO: ABO_0710(nrdB) ABO_0711(nrdA)
            MMW: Mmwyl1_2996 Mmwyl1_2997
            AHA: AHA_0870 AHA_2333(nrdA) AHA_2334(nrdB)
            DNO: DNO_0607(nrdA) DNO_0608
            BCI: BCI_0385(nrdB) BCI_0386
            RMA: Rmag_0523 Rmag_0524
            VOK: COSY_0479(nrdA) COSY_0480(nrdB)
            NME: NMB1288 NMB1291
            NMA: NMA1498(nrdB) NMA1501(nrdA)
            NMC: NMC1223(nrdB) NMC1226(nrdA)
            NGO: NGO0614 NGO0615
            CVI: CV_1446(nrdE) CV_2284(nrdB) CV_2287(nrdA)
            RSO: RSc0195(RS00627) RSc2804(nrdB) RSc2805(nrdA)
            REU: Reut_A2113 Reut_A2940 Reut_A2941
            REH: H16_A2390(nrdJ) H16_A3234(nrdB) H16_A3235(nrdA)
            RME: Rmet_2130 Rmet_3087 Rmet_3088
            BMA: BMA2509(nrdB) BMA2510(nrdA) BMAA2027
            BMV: BMASAVP1_A0430(nrdB) BMASAVP1_A0431(nrdA)
            BML: BMA10299_A1289(nrdB) BMA10299_A1290(nrdA)
            BMN: BMA10247_3273(nrdA) BMA10247_3274(nrdB)
            BXE: Bxe_A0521 Bxe_A0523 Bxe_B1704
            BVI: Bcep1808_0570 Bcep1808_0571 Bcep1808_6310
            BUR: Bcep18194_A3679 Bcep18194_A3680
            BCN: Bcen_0112 Bcen_0113
            BCH: Bcen2424_0594 Bcen2424_0596
            BAM: Bamb_0497 Bamb_0498
            BPS: BPSL2991(nrdB) BPSL2992 BPSS0479 BPSS2282
            BPM: BURPS1710b_3510(nrdB) BURPS1710b_3511(nrdA)
                 BURPS1710b_A1422(nrdE) BURPS1710b_A2032(nrdA)
            BPL: BURPS1106A_3511(nrdB) BURPS1106A_3512(nrdA) BURPS1106A_A0649
                 BURPS1106A_A3084(nrd)
            BPD: BURPS668_3473(nrdB) BURPS668_3474(nrdA) BURPS668_A0741
                 BURPS668_A3210(nrd)
            BTE: BTH_I1153 BTH_I1154 BTH_II1936 BTH_II2313
            PNU: Pnuc_0204 Pnuc_0205
            BPE: BP2983(nrdA) BP2984(nrdB)
            BPA: BPP3903(nrdA) BPP3904(nrdB)
            BBR: BB4376(nrdA) BB4377(nrdB)
            RFR: Rfer_2197 Rfer_3011 Rfer_3347 Rfer_3348
            POL: Bpro_1106 Bpro_1107 Bpro_5207 Bpro_5497
            PNA: Pnap_3385 Pnap_3386 Pnap_3755
            AAV: Aave_0667 Aave_0863 Aave_0864
            AJS: Ajs_3632 Ajs_3633
            VEI: Veis_1495 Veis_1496
            MPT: Mpe_A3213 Mpe_A3214 Mpe_B0385
            HAR: HEAR2769(nrdB) HEAR2770(nrdA)
            MMS: mma_2978 mma_2979
            NEU: NE2422(nrdB) NE2423(nrdA)
            NET: Neut_2467 Neut_2468
            NMU: Nmul_A2468 Nmul_A2469
            EBA: ebA4850(nrdA)
            AZO: azo1411
            DAR: Daro_0964
            TBD: Tbd_0058 Tbd_1975 Tbd_1976
            MFA: Mfla_1223 Mfla_1224 Mfla_2541
            HPY: HP0364(nrdB) HP0680(nrdA)
            HPJ: jhp0621(nrdA) jhp1016(nrdB)
            HPA: HPAG1_0662 HPAG1_1029
            HHE: HH0606(nrdB) HH1774(nrdA)
            HAC: Hac_0411(nrdB) Hac_0862(nrdA) Hac_1226
            WSU: WS0420(nrdB) WS1764(nrdA)
            TDN: Tmden_0013 Tmden_2096
            CJE: Cj0024(nrdA) Cj0231c(nrdB)
            CJR: CJE0024(nrdA) CJE0282(nrdB)
            CJJ: CJJ81176_0051(nrdA) CJJ81176_0256(nrdB)
            CJU: C8J_0023(nrdA) C8J_0209(nrdB)
            CJD: JJD26997_0026(nrdA) JJD26997_0229(nrdB)
            CFF: CFF8240_0029 CFF8240_1820
            CCV: CCV52592_1122 CCV52592_2093
            CHA: CHAB381_0195 CHAB381_1730
            CCO: CCC13826_0297 CCC13826_0736(nrdB) CCC13826_1895
            ABU: Abu_0020(nrdA) Abu_0021(nrdB)
            NIS: NIS_0047 NIS_0053(nrdA)
            SUN: SUN_0252 SUN_2372(nrdA) SUN_2398
            GSU: GSU1871
            GME: Gmet_1297
            PCA: Pcar_1852
            DVU: DVU3379
            DDE: Dde_0113
            LIP: LI0476(nrdA) LI0477(nrdB)
            BBA: Bd1196(nrdE) Bd1983(nrdB) Bd1984(nrdA)
            DPS: DP2827
            ADE: Adeh_1613 Adeh_2484
            AFW: Anae109_2198
            MXA: MXAN_2925 MXAN_5057 MXAN_5058
            SAT: SYN_01209 SYN_01226
            SFU: Sfum_0259
            RPR: RP512(nrdB) RP513(nrdA)
            RTY: RT0497(nrdB) RT0498(nrdA)
            RCO: RC0647(nrdA) RC0651(nrdB)
            RFE: RF_0709(nrdA) RF_0710(nrdB)
            RBE: RBE_0732(nrdB) RBE_0733(nrdA)
            RAK: A1C_03470 A1C_03485(nrdF)
            RBO: A1I_04765(nrdF) A1I_04770
            RCM: A1E_02965(nrdF) A1E_03015
            RRI: A1G_03670 A1G_03685(nrdF)
            OTS: OTBS_0026(nrdA) OTBS_0027(nrdB)
            WOL: WD0197(nrdA) WD0212(nrdB)
            WBM: Wbm0267 Wbm0695
            AMA: AM483(nrdB) AM860(nrdA)
            APH: APH_0331(nrdA) APH_0560(nrdB)
            ERU: Erum3270(nrdB) Erum5650(nrdA)
            ERW: ERWE_CDS_03340(nrdB) ERWE_CDS_05920(nrdA)
            ERG: ERGA_CDS_03290(nrdB) ERGA_CDS_05830(nrdA)
            ECN: Ecaj_0310 Ecaj_0566
            ECH: ECH_0459(nrdA) ECH_0766(nrdB)
            NSE: NSE_0411(nrdA) NSE_0520(nrdB)
            PUB: SAR11_0723(nrdE) SAR11_1158(nrdB) SAR11_1159(nrdA)
            MLO: mll0136
            MES: Meso_1332 Meso_2702 Meso_2703
            PLA: Plav_0504 Plav_0505 Plav_3299
            SME: SMc01237(nrd)
            SMD: Smed_1233
            ATU: Atu0070(nrdE) Atu0071(nrdF) Atu1733(nrdE)
            ATC: AGR_C_106 AGR_C_107 AGR_C_3183
            RET: RHE_CH01753(nrd) RHE_CH03715(nrdF) RHE_CH03716(nrdE)
            RLE: RL1945 RL4258(nrdF) RL4259(nrdE)
            BME: BMEI0943 BMEII0929 BMEII0930
            BMF: BAB1_1063 BAB2_0888(nrdF) BAB2_0889(nrdE)
            BMS: BR1043 BRA0316(nrdE) BRA0317(nrdF)
            BMB: BruAb1_1048 BruAb2_0864(nrdF) BruAb2_0865(nrdE)
            BOV: BOV_A0292 BOV_A0293(nrdF)
            OAN: Oant_2131 Oant_2954 Oant_2955
            BJA: bll0006(nrdB) bll0007 bll4274(nrdE)
            BRA: BRADO3475(nrd)
            BBT: BBta_4237(nrd)
            RPA: RPA2977(nrd)
            RPB: RPB_2544
            RPC: RPC_2380 RPC_3518 RPC_3519
            RPD: RPD_2912
            RPE: RPE_2501 RPE_3177
            NWI: Nwi_1571 Nwi_2887 Nwi_2888
            NHA: Nham_2084 Nham_3663 Nham_3664
            BHE: BH01940(nrdE) BH01950(nrdF)
            BQU: BQ01820(nrdE) BQ01830(nrdF)
            BBK: BARBAKC583_0356(nrdE) BARBAKC583_0358(nrdF)
            XAU: Xaut_4674
            CCR: CC_0260 CC_3492
            SIL: SPO2136(nrdJ) SPO3194
            SIT: TM1040_0518 TM1040_0519 TM1040_1151
            RSP: RSP_2495(nrd) RSP_3547
            RSH: Rsph17029_1162
            RSQ: Rsph17025_0933
            JAN: Jann_0951 Jann_2472
            RDE: RD1_3193(nrdJ) RD1_4061
            PDE: Pden_1384 Pden_4377 Pden_4378
            MMR: Mmar10_0399 Mmar10_0401
            HNE: HNE_0373 HNE_0869 HNE_1555
            ZMO: ZMO0443(nrdB) ZMO1039(nrdA)
            NAR: Saro_0271 Saro_0274
            SAL: Sala_1773 Sala_1775
            SWI: Swit_1504 Swit_1506
            ELI: ELI_11600 ELI_11635
            GOX: GOX1993 GOX1994
            GBE: GbCGDNIH1_0887 GbCGDNIH1_0888
            ACR: Acry_0738 Acry_0739
            RRU: Rru_A1444 Rru_A1445 Rru_A2441 Rru_A3258
            MAG: amb2746 amb4446
            MGM: Mmc1_3489
            ABA: Acid345_1124
            SUS: Acid_1665
            BSU: BG11404(nrdE) BG11405(nrdF) BG13723(bnrdE) BG13725(bnrdF)
            BHA: BH0501(nrdA) BH0502(nrdB)
            BAN: BA1371(nrdE) BA1372(nrdF)
            BAR: GBAA1372(nrdF)
            BAA: BA_1896 BA_1897
            BAT: BAS1267 BAS1269 BAS1270
            BCE: BC1354 BC1355
            BCA: BCE_1470(nrdE) BCE_1471(nrdF)
            BCZ: BCZK1242(nrdE) BCZK1243(nrdE) BCZK1244(nrdF)
            BCY: Bcer98_1074 Bcer98_1075 Bcer98_1076
            BTK: BT9727_1240(nrdE) BT9727_1241(nrdE) BT9727_1242(nrdF)
            BTL: BALH_1212(nrdE)
            BLI: BL01192(nrdE) BL01193(nrdF)
            BLD: BLi01966(nrdE) BLi01967(nrdF)
            BCL: ABC3108(nrdE) ABC3109(nrdF)
            BAY: RBAM_017180 RBAM_017190
            BPU: BPUM_1629 BPUM_1630
            OIH: OB3087 OB3089
            GKA: GK0911 GK0912 GK2771
            SAU: SA0686(nrdE) SA0687(nrdF)
            SAV: SAV0731(nrdE) SAV0732(nrdF)
            SAM: MW0693(nrdE) MW0694(nrdF)
            SAR: SAR0785(rir1) SAR0786(rir2)
            SAS: SAS0696 SAS0697
            SAC: SACOL0792(nrdE) SACOL0793(nrdF)
            SAB: SAB0682(rir1) SAB0683(rir2)
            SAA: SAUSA300_0716 SAUSA300_0717
            SAO: SAOUHSC_00742 SAOUHSC_00743
            SAJ: SaurJH9_0755 SaurJH9_0756
            SAH: SaurJH1_0772 SaurJH1_0773
            SEP: SE0513 SE0514
            SER: SERP0397(nrdE) SERP0398(nrdF-1) SERP1510(nrdF-2) SERP1513
            SHA: SH2161(nrdF) SH2162(nrdE)
            SSP: SSP1985 SSP1986
            LMO: lmo2154 lmo2155
            LMF: LMOf2365_2186(nrdB) LMOf2365_2187(nrdA)
            LIN: lin2258 lin2259
            LWE: lwe2171(nrdB) lwe2172(nrdA)
            LLA: L0294(nrdE) L0295(nrdF)
            LLC: LACR_1060 LACR_1061
            LLM: llmg_1543(nrdE) llmg_1544(nrdF)
            SPY: SPy_0425(nrdF.1) SPy_0427(nrdE.1) SPy_1375(nrdE.2)
                 SPy_1378(nrdF.2)
            SPZ: M5005_Spy_0347(nrdF.1) M5005_Spy_0349(nrdE.1)
                 M5005_Spy_1123(nrdE.2) M5005_Spy_1124(nrdF.2)
            SPM: spyM18_0470(nrdF) spyM18_0472 spyM18_1387(nrdE)
                 spyM18_1389(nrdF)
            SPG: SpyM3_0301(nrdF.2) SpyM3_0303(nrdE.2) SpyM3_1049(nrdE.1)
                 SpyM3_1050(nrdF.1)
            SPS: SPs0811 SPs0812 SPs1554 SPs1556
            SPH: MGAS10270_Spy0346(nrdF1) MGAS10270_Spy0348(nrdE1)
                 MGAS10270_Spy1193(nrdE2) MGAS10270_Spy1194(nrdF2)
            SPI: MGAS10750_Spy0349(nrdF1) MGAS10750_Spy0351(nrdE1)
                 MGAS10750_Spy1226(nrdE2) MGAS10750_Spy1228(nrdF2)
            SPJ: MGAS2096_Spy0366(nrdF1) MGAS2096_Spy0368(nrdE1)
                 MGAS2096_Spy1188(nrdE2) MGAS2096_Spy1189(nrdF2)
            SPK: MGAS9429_Spy0350(nrdF1) MGAS9429_Spy0352(nrdE1)
                 MGAS9429_Spy1170(nrdE2) MGAS9429_Spy1171(nrdF2)
            SPF: SpyM50735 SpyM50737 SpyM51512(nrdE) SpyM51514(nrdF)
            SPA: M6_Spy0372 M6_Spy0374 M6_Spy1097 M6_Spy1098
            SPB: M28_Spy0334(nrdF.1) M28_Spy0336(nrdE.1) M28_Spy1116(nrdE.2)
                 M28_Spy1118(nrdF.2)
            SPN: SP_1179 SP_1180
            SPR: spr1065(nrdE) spr1066(nrdF)
            SPD: SPD_1042(nrdE) SPD_1043(nrdF)
            SAG: SAG0418(nrdF-1) SAG0420(nrdE-1) SAG0818(nrdF-2)
                 SAG0819(nrdE-2)
            SAN: gbs0453 gbs0455 gbs0836 gbs0837
            SAK: SAK_0499(nrdF) SAK_0501 SAK_0942(nrdF) SAK_0943
            SMU: SMU.667(nrdG) SMU.668c
            STC: str1270(nrdE) str1271(nrdF)
            STL: stu1270(nrdE) stu1271(nrdF)
            STE: STER_1248
            SSA: SSA_0768(nrdF) SSA_0770(nrdE)
            SGO: SGO_1558(nrdE)
            LPL: lp_0692(nrdF) lp_0693(nrdE)
            LJO: LJ0591
            LAC: LBA0041 LBA1750
            LSA: LSA0940(nrdF) LSA0941(nrdE)
            LSL: LSL_1232(nrdA) LSL_1233(nrdB)
            LBR: LVIS_0595 LVIS_0596 LVIS_1898
            LCA: LSEI_1468 LSEI_1469 LSEI_2287
            LRE: Lreu_0322 Lreu_0323
            EFA: EF0470(nrdF) EF0471(nrdE)
            OOE: OEOE_0140 OEOE_0141
            LME: LEUM_0254
            STH: STH2760 STH321 STH322
            CAC: CAC1047 CAC3276(nrdB) CAC3277(nrdA)
            CPE: CPE2360(nrdB) CPE2361(nrdA)
            CPF: CPF_2670(nrdB) CPF_2671(nrdA)
            CPR: CPR_2355(nrdB) CPR_2356
            CTC: CTC00574
            CNO: NT01CX_2365 NT01CX_2366(nrdA)
            CDF: CD2994(nrdF) CD2995(nrdE)
            CBO: CBO2813(nrdF) CBO2814(nrdE)
            CBA: CLB_2756(nrdB) CLB_2757(nrdA)
            CBH: CLC_2689(nrdB)
            CBF: CLI_2863(nrdB) CLI_2864(nrdA)
            CBE: Cbei_0194 Cbei_0195
            CHY: CHY_0676(nrdJ)
            DSY: DSY0322
            TTE: TTE2336(nrdA)
            MGE: MG_229(nrdF) MG_231(nrdE)
            MPN: MPN322(nrdF) MPN324(nrdE)
            MPU: MYPU_5390(nrdF) MYPU_5410(nrdE)
            MPE: MYPE850(nrdE) MYPE870(nrdF)
            MGA: MGA_0695(nrdA) MGA_0698(nrdF)
            MMY: MSC_0853(nrdE) MSC_0855(nrdF)
            MMO: MMOB0160(nrdA)
            MHY: mhp156(nrdF) mhp158(nrdE)
            MHJ: MHJ_0215(nrdE) MHJ_0217(nrdF)
            MHP: MHP7448_0221(nrdE) MHP7448_0223(nrdF)
            MSY: MS53_0399(nrdF) MS53_0401(nrdE)
            MCP: MCAP_0099(nrdF) MCAP_0101(nrdE)
            POY: PAM054(nrdA) PAM055(nrdF)
            AYW: AYWB_025(nrdA) AYWB_026(nrdF)
            MFL: Mfl528 Mfl530
            MTU: Rv0233(nrdB) Rv0570(nrdZ) Rv1981c(nrdF1) Rv3048c(nrdF2)
                 Rv3051c(nrdE)
            MTC: MT0244 MT0596 MT2033(nrdF-1) MT3133(nrdF-2) MT3137(nrdE)
            MBO: Mb0238(nrdB) Mb0585(nrdZ) Mb2003c(nrdF1) Mb3074c(nrdF2)
                 Mb3077c(nrdE)
            MBB: BCG_0270(nrdB) BCG_3072c(nrdF2) BCG_3075c(nrdE)
            MLE: ML1731(nrdF) ML1734(nrdE)
            MPA: MAP3095c(nrdG) MAP3100c(nrdE) MAP3672(nrdB)
            MAV: MAV_3913 MAV_3919
            MSM: MSMEG_0358 MSMEG_1019 MSMEG_1033 MSMEG_2299 MSMEG_2313
            MUL: MUL_1878(nrdE)
            MVA: Mvan_2042 Mvan_2060
            MGI: Mflv_4286 Mflv_4305
            MMC: Mmcs_1085 Mmcs_1817 Mmcs_1828 Mmcs_4214
            MKM: Mkms_1864 Mkms_1875
            MJL: Mjls_1798 Mjls_1809
            CGL: NCgl2438(cgl2525) NCgl2443(cgl2530)
            CGB: cg2781(nrdF) cg2786(nrdE)
            CEF: CE0879 CE2419(nrdF) CE2423(nrdE)
            CDI: DIP1865(nrdF1) DIP1867(nrdE) DIP1924(nrdF2)
            CJK: jk0225(nrdF2) jk0478(nrdE) jk0480(nrdF1)
            NFA: nfa42980(nrdF) nfa43070(nrdE)
            RHA: RHA1_ro06441 RHA1_ro06442(nrdG)
            SCO: SCO5225(nrdM) SCO5226(nrdL) SCO5805(nrdJ)
            SMA: SAV2461(nrdA) SAV3026(nrdL) SAV3027(nrdM)
            TWH: TWT682(nrdB) TWT683(nrdA)
            TWS: TW701 TW702
            LXX: Lxx17770(nrdB) Lxx17790(nrdA)
            CMI: CMM_2428(nrdB) CMM_2429(nrdA)
            ART: Arth_2355 Arth_2356
            AAU: AAur_2338 AAur_2339
            PAC: PPA1026 PPA2121 PPA2122
            NCA: Noca_3811
            TFU: Tfu_2149 Tfu_3001 Tfu_3002
            FRA: Francci3_3507
            FAL: FRAAL4904 FRAAL5699(nrdJ)
            ACE: Acel_1476 Acel_1724 Acel_1725
            KRA: Krad_0805 Krad_0806
            SEN: SACE_0591 SACE_1282(nrdB) SACE_1283(nrdA) SACE_1764
            STP: Strop_1453 Strop_4387 Strop_4388
            BLO: BL0670(nrdE) BL0671(nrdF)
            RXY: Rxyl_2874
            FNU: FN0102 FN0103
            RBA: RB12762(nrdA)
            CTR: CT827(nrdA) CT828(nrdB)
            CTA: CTA_0901(nrdA) CTA_0902(nrdB)
            CMU: TC0214 TC0215
            CPN: CPn0984(nrdA) CPn0985(nrdB)
            CPA: CP0871 CP0872
            CPJ: CPj0984(nrdA) CPj0985(nrdB)
            CPT: CpB1021 CpB1022
            CCA: CCA00776(nrdB) CCA00777(nrdA)
            CAB: CAB744 CAB745
            CFE: CF0237(nrdA) CF0238(nrdB)
            PCU: pc0111(nrdD) pc1348(nrdA) pc1349(nrdB)
            TPA: TP0053 TP1008
            TDE: TDE0335(nrdB) TDE0341(nrdA)
            LIL: LA2360(nrdA)
            LIC: LIC11587(nrdA)
            LBJ: LBJ_1270(nrdA)
            LBL: LBL_1495(nrdA)
            SYN: slr0591(nrdF) slr1164(nrdA)
            SYW: SYNW1147(nrdJ) SYNW1692(nrdJ)
            SYC: syc0066_d
            SYD: Syncc9605_1277
            SYE: Syncc9902_1200
            SYG: sync_1265
            SYR: SynRCC307_0954
            SYX: SynWH7803_1496
            TEL: tll1327
            PMA: Pro0815
            PMM: PMM0661(nrdJ)
            PMT: PMT0793(nrdJ)
            PMN: PMN2A_0093
            PMB: A9601_04621 A9601_07161(nrdJ)
            PMC: P9515_04731 P9515_07341(nrdJ)
            PMF: P9303_14171(nrdJ) P9303_21141
            PMG: P9301_04311 P9301_07141(nrdJ)
            PME: NATL1_04631 NATL1_07181(nrdJ)
            BTH: BT_2145
            BFR: BF2693 BF2694 BF3827
            BFS: BF2713 BF2714 BF3619
            PGI: PG1129(nrd)
            SRU: SRU_0131 SRU_0132 SRU_0300
            CHU: CHU_0451(nrdA) CHU_0452(nrdB)
            GFO: GFO_2142(nrdA) GFO_3475(nrdA) GFO_3476
            FJO: Fjoh_0521 Fjoh_0522 Fjoh_4065
            FPS: FP0457(nrdA) FP0458(nrdB)
            CTE: CT0578
            CCH: Cag_0703
            CPH: Cpha266_1782
            PVI: Cvib_1199
            PLT: Plut_0577
            DET: DET0244(nrd-1) DET0345(nrd-2) DET0623(nrd-3)
            DEH: cbdb_A251(nrd) cbdb_A287(nrdA) cbdb_A608(nrd)
            DEB: DehaBAV1_0324
            DRA: DR_2374 DR_B0108 DR_B0109
            DGE: Dgeo_0251 Dgeo_1774 Dgeo_1775
            TTH: TTC1930 TT_P0161 TT_P0162
            TTJ: TTHA0075 TTHB208 TTHB209
            AAE: aq_094(nrdA) aq_1505(nrdF)
            TMA: TM0118
            MAC: MA1665(nrd)
            MBA: Mbar_A3615
            MMA: MM_2830
            MTH: MTH652
            AFU: AF1664(nrd)
            HAL: VNG1644G(nrdB2) VNG2383G(nrdA) VNG2384G(nrdB1)
            HMA: rrnAC1622(nrdA)
            HWA: HQ2859A(nrdA)
            NPH: NP3346A(nrdA_2) NP4434A(nrdB_3) NP5066A(nrdB_2)
                 NP6166A(nrdB_1) NP6168A(nrdA_1)
            TAC: Ta1475
            TVO: TVN0092
            PTO: PTO1241
            PHO: PH0363
            PAB: PAB1057(nrd)
            PFU: PF0440
            TKO: TK1736
            APE: APE_2062.1
            SSO: SSO0929(nrd) SSO2498(nrdB)
            STO: ST1259
            SAI: Saci_1112 Saci_1353(nrd) Saci_2188
            PAI: PAE3155
            PCL: Pcal_1797
            PAS: Pars_1670
STRUCTURES  PDB: 1AFT  1AV8  1BIQ  1H0N  1H0O  1JK0  1JPR  1JQC  1MRR  1MXR  
                 1PEM  1PEO  1PEQ  1PEU  1PFR  1PIM  1PIU  1PIY  1PIZ  1PJ0  
                 1PJ1  1PM2  1QFN  1R1R  1R2F  1R65  1RIB  1RLR  1RNR  1RSR  
                 1RSV  1SMQ  1SMS  1SYY  1UZR  1W68  1W69  1XIK  1XJE  1XJF  
                 1XJG  1XJJ  1XJK  1XJM  1XJN  1XSM  1YFD  1ZYZ  1ZZD  2ALX  
                 2ANI  2AV8  2BQ1  2CVS  2CVT  2CVU  2CVV  2CVW  2CVX  2CVY  
                 2EUD  2R1R  2R2F  2RCC  2UW2  3R1R  4R1R  5R1R  6R1R  7R1R  
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.4.1
            ExPASy - ENZYME nomenclature database: 1.17.4.1
            ExplorEnz - The Enzyme Database: 1.17.4.1
            ERGO genome analysis and discovery system: 1.17.4.1
            BRENDA, the Enzyme Database: 1.17.4.1
            CAS: 9047-64-7
///
ENTRY       EC 1.17.4.2                 Enzyme
NAME        ribonucleoside-triphosphate reductase;
            ribonucleotide reductase;
            2'-deoxyribonucleoside-triphosphate:oxidized-thioredoxin
            2'-oxidoreductase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With a disulfide as acceptor
SYSNAME     2'-deoxyribonucleoside-triphosphate:thioredoxin-disulfide
            2'-oxidoreductase
REACTION    2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H2O =
            ribonucleoside triphosphate + thioredoxin [RN:R04315]
ALL_REAC    R04315 > R02014 R02020 R02022 R02023
SUBSTRATE   2'-deoxyribonucleoside triphosphate [CPD:C04283];
            thioredoxin disulfide [CPD:C00343];
            H2O [CPD:C00001]
PRODUCT     ribonucleoside triphosphate [CPD:C03802];
            thioredoxin [CPD:C00342]
COFACTOR    ATP [CPD:C00002];
            Iron [CPD:C00023];
            Cobalt [CPD:C00175];
            Cobamide coenzyme [CPD:C00194]
COMMENT     Requires a cobamide coenzyme and ATP.
REFERENCE   1  [PMID:14299643]
  AUTHORS   BLAKLEY RL.
  TITLE     COBAMIDES AND RIBONUCLEOTIDE REDUCTION. I. COBAMIDE STIMULATION OF
            RIBONUCLEOTIDE REDUCTION IN EXTRACTS OF LACTOBACILLUS LEICHMANNII.
  JOURNAL   J. Biol. Chem. 240 (1965) 2173-80.
  ORGANISM  Lactobacillus leichmannii
REFERENCE   2  [PMID:5924645]
  AUTHORS   Goulian M, Beck WS.
  TITLE     Purification and properties of cobamide-dependent ribonucleotide
            reductase from Lactobacillus leichmannii.
  JOURNAL   J. Biol. Chem. 241 (1966) 4233-42.
  ORGANISM  Lactobacillus leichmannii
REFERENCE   3
  AUTHORS   Lammers, M. and Follmann, H.
  TITLE     The ribonucleotide reductases - a unique group of metalloenzymes
            essential for cell-proliferation.
  JOURNAL   Struct. Bonding 54 (1983) 27-91.
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K00527  ribonucleoside-triphosphate reductase
GENES       ECO: b4238(nrdD)
            ECJ: JW4197(nrdD)
            ECE: Z5848(nrdD)
            ECS: ECs5215
            ECC: c5337(nrdD)
            ECI: UTI89_C4842(nrdD)
            ECP: ECP_4487
            ECV: APECO1_2154(nrdD)
            ECW: EcE24377A_4809(nrdD)
            ECX: EcHS_A4492
            STY: STY4791(nrdD)
            STT: t4486(nrdD)
            SPT: SPA4252(nrdD)
            SEC: SC4307(nrdD)
            STM: STM4452(nrdD)
            YPE: YPO3454(nrdD)
            YPK: y0733(nrdD)
            YPM: YP_0631(nrdD)
            YPA: YPA_2956
            YPN: YPN_0634
            YPP: YPDSF_3264
            YPS: YPTB0519(nrdD)
            YPI: YpsIP31758_3556(nrdD)
            YEN: YE0482(nrdD)
            SFL: SF4252(nrdD)
            SFX: S4514(nrdD)
            SFV: SFV_4253(nrdD)
            SSN: SSON_4419(nrdD)
            SBO: SBO_4208(nrdD)
            SDY: SDY_4257(nrdD)
            ECA: ECA0375(nrdD)
            PLU: plu4499(nrdD)
            ENT: Ent638_0437
            KPN: KPN_04646(nrdD)
            SPE: Spro_0525
            HIN: HI0075(nrdD)
            HIT: NTHI0088(nrdD)
            HIP: CGSHiEE_02930
            HIQ: CGSHiGG_02920
            HSO: HS_1468(nrdD)
            PMU: PM0940(nrdD)
            MSU: MS0633(nrdD)
            ASU: Asuc_1407
            VCH: VCA0511
            VCO: VC0395_0445(nrdD)
            VVU: VV2_0337
            VVY: VVA0895
            VPA: VPA0941
            VFI: VFA0281
            PPR: PBPRB0442
            PAE: PA1920
            PAU: PA14_39690(nrdD)
            PAP: PSPA7_3365(nrdD)
            SON: SO_2834(nrdD)
            SDN: Sden_1419
            SFR: Sfri_2443
            SAZ: Sama_1275
            SBL: Sbal_1665
            SBM: Shew185_1650
            SLO: Shew_2449
            SPC: Sputcn32_1540
            SSE: Ssed_1600
            SPL: Spea_2619
            SHE: Shewmr4_2441
            SHM: Shewmr7_2511
            SHN: Shewana3_2603
            SHW: Sputw3181_2559
            ILO: IL0188
            PIN: Ping_0740
            AHA: AHA_1231(nrdD)
            DNO: DNO_0910(nrdD)
            CVI: CV_2412(nrdD)
            RSO: RSp0963(nrdD)
            RME: Rmet_5139
            BMA: BMA0629(nrdD)
            BMV: BMASAVP1_A2383(nrdD)
            BML: BMA10299_A2904(nrdD)
            BMN: BMA10247_1698(nrdD)
            BPS: BPSL2356
            BPM: BURPS1710b_2809(nrdD)
            BPL: BURPS1106A_2742(nrdD)
            BPD: BURPS668_2685(nrdD)
            BTE: BTH_I1809
            RFR: Rfer_0368
            HAR: HEAR1672
            TBD: Tbd_2171
            WSU: WS0684
            TDN: Tmden_1239
            CFF: CFF8240_0021(nrdD)
            CCV: CCV52592_1124(nrdD)
            CCO: CCC13826_1897(nrdD)
            ABU: Abu_1243(nrdD)
            NIS: NIS_1771(nrdD)
            SUN: SUN_0254(nrdD)
            DVU: DVU0299 DVU2947
            DDE: Dde_0277 Dde_3016
            BBA: Bd2593
            DPS: DP0064
            SAT: SYN_01979 SYN_03522
            RPC: RPC_3517
            RPE: RPE_3176
            MMR: Mmar10_0305
            ZMO: ZMO1025(nrdD)
            RRU: Rru_A1276
            BAN: BA3663
            BAR: GBAA3663
            BAA: BA_4152
            BAT: BAS3398
            BCE: BC3603
            BCA: BCE_3622
            BCZ: BCZK3310(nrdD)
            BCY: Bcer98_2252
            BTK: BT9727_3360(nrdD)
            BLI: BL02468
            BLD: BLi03824
            SAU: SA2410(nrdD)
            SAV: SAV2617(nrdD)
            SAM: MW2537(nrdD)
            SAR: SAR2695(nrdD)
            SAS: SAS2503
            SAC: SACOL2635(nrdD)
            SAB: SAB2491c(nrdD)
            SAA: SAUSA300_2551(nrdD)
            SAO: SAOUHSC_02942
            SAJ: SaurJH9_2640
            SAH: SaurJH1_2694
            SEP: SE2172
            SER: SERP2183(nrdD)
            SSP: SSP0144
            LMO: lmo0279
            LMF: LMOf2365_0299(nrdD)
            LIN: lin0305
            LWE: lwe0253(nrdD)
            LLA: L70400(nrdD)
            LLC: LACR_0277
            LLM: llmg_0281
            SPY: SPy_2110(nrdD)
            SPZ: M5005_Spy_0925(rnhB) M5005_Spy_1793(nrdD)
            SPM: spyM18_2168(nrdD)
            SPG: SpyM3_1794(nrdD)
            SPS: SPs1792
            SPH: MGAS10270_Spy1039(rnhB) MGAS10270_Spy1861(nrdD)
            SPI: MGAS10750_Spy1074(rnhB) MGAS10750_Spy1885(nrdD)
            SPJ: MGAS2096_Spy0984(rnhB) MGAS2096_Spy1826(nrdD)
            SPK: MGAS9429_Spy1028(rnhB) MGAS9429_Spy1804(nrdD)
            SPF: SpyM51752(nrdD)
            SPA: M6_Spy0914 M6_Spy1792
            SPB: M28_Spy0897(rnhB) M28_Spy1777(nrdD)
            SPN: SP_0202
            SPR: spr0183(nrdD)
            SPD: SPD_0187(nrdD)
            SAG: SAG2086(nrdD)
            SAN: gbs2041
            SAK: SAK_2025(nrdD)
            SMU: SMU.2074(nrdD)
            STC: str1963(nrdD)
            STL: stu1963(nrdD)
            STE: STER_1942
            SSA: SSA_2230(nrdD)
            SSU: SSU05_2118
            SSV: SSU98_2124
            SGO: SGO_1203 SGO_2033(nrdD)
            LPL: lp_2932(nrdD)
            LJO: LJ0137
            LAC: LBA0160
            LSA: LSA1459(nrdD)
            LSL: LSL_1332(nrdD)
            LDB: Ldb0096(rtpR) Ldb0211(nrdD)
            LBU: LBUL_0185
            LCA: LSEI_0131
            LGA: LGAS_0138
            LRE: Lreu_1317
            PPE: PEPE_0484
            EFA: EF2754(nrdD)
            OOE: OEOE_1116
            LME: LEUM_1539
            CAC: CAC0480(nrdD) CAC1209(nrdD)
            CPE: CPE0917(nrdD) CPE2507(nrdD)
            CPF: CPF_2830(nrdD)
            CPR: CPR_2516(nrdD)
            CTC: CTC00257
            CDF: CD0108(nrdD)
            CBO: CBO0094(nrdD)
            CBA: CLB_0129(nrdD) CLB_0130(nrdG)
            CBH: CLC_0141(nrdD) CLC_0142(nrdG)
            CBF: CLI_0149(nrdD) CLI_0150(nrdG)
            CBE: Cbei_0068 Cbei_2522
            AMT: Amet_4520
            CHY: CHY_2051(nrdD)
            DSY: DSY0397
            DRM: Dred_0693
            SWO: Swol_2273
            TTE: TTE1850(nrdD)
            MTA: Moth_1449
            MPE: MYPE4960(nrdD)
            CEF: CE2363
            CDI: DIP0465
            PAC: PPA2137
            BLO: BL1752(nrdD)
            BAD: BAD_1216(nrdD)
            FNU: FN0311
            TDE: TDE1331(nrdD)
            CYA: CYA_2169(nrdJ)
            CYB: CYB_0734(nrdJ)
            AVA: Ava_1670
            BTH: BT_1998
            BFR: BF3692
            BFS: BF3484
            PGI: PG1260
            RRS: RoseRS_4577
            RCA: Rcas_0124
            MMP: MMP0227(nrdD)
            MMQ: MmarC5_1471
            MMZ: MmarC7_1227
            MVN: Mevan_1241
            MAC: MA0072(nrdD)
            MBA: Mbar_A1037
            MMA: MM_1367
            MBU: Mbur_2125 Mbur_2140
            MHU: Mhun_2811
            MTH: MTH1539
            MST: Msp_0254
            MKA: MK0901(nrdD)
            PAB: PAB2337
            PFU: PF1971
            TKO: TK2298
            RCI: RCIX705(nrdD)
            NEQ: NEQ345
STRUCTURES  PDB: 1H78  1H79  1H7A  1H7B  1HK8  1L1L  
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.4.2
            ExPASy - ENZYME nomenclature database: 1.17.4.2
            ExplorEnz - The Enzyme Database: 1.17.4.2
            ERGO genome analysis and discovery system: 1.17.4.2
            BRENDA, the Enzyme Database: 1.17.4.2
            CAS: 9068-66-0
///
ENTRY       EC 1.17.4.3                 Enzyme
NAME        4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With a disulfide as acceptor
SYSNAME     (E)-4-hydroxy-3-methylbut-2-en-1-yl-diphosphate:protein-disulfide
            oxidoreductase (hydrating)
REACTION    (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O +
            protein-disulfide = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate +
            protein-dithiol [RN:R05883]
ALL_REAC    R05883
SUBSTRATE   (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate [CPD:C11811];
            H2O [CPD:C00001];
            protein disulfide [CPD:C02582]
PRODUCT     2-C-methyl-D-erythritol 2,4-cyclodiphosphate [CPD:C11453];
            protein dithiol [CPD:C02315]
COMMENT     Forms, in the reverse direction, part of an alternative,
            nonmevalonate pathway for terpenoid biosynthesis (for diagram, click
            here).
REFERENCE   1  [PMID:11752431]
  AUTHORS   Hecht S, Eisenreich W, Adam P, Amslinger S, Kis K, Bacher A, Arigoni
            D, Rohdich F.
  TITLE     Studies on the nonmevalonate pathway to terpenes: the role of the
            GcpE (IspG) protein.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 14837-42.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K03526  4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
GENES       OSA: 4329911
            CME: CML284C
            PFA: PF10_0221
            TAN: TA14455
            TPV: TP02_0667
            ECO: b2515(ispG)
            ECJ: JW2499(ispG)
            ECE: Z3778(gcpE)
            ECS: ECs3377
            ECC: c3037(gcpE)
            ECI: UTI89_C2836(gcpE)
            ECP: ECP_2520
            ECV: APECO1_4009(ispG)
            ECW: EcE24377A_2799(ispG)
            ECX: EcHS_A2666
            STY: STY2768(gcpE)
            STT: t0333(gcpE)
            SPT: SPA0344(gcpE)
            SEC: SC2520(gcpE)
            STM: STM2523(gcpE)
            YPE: YPO2879(aarC)
            YPK: y1353(gcpE)
            YPM: YP_2745(gcpE)
            YPA: YPA_2319
            YPN: YPN_1259
            YPP: YPDSF_2224
            YPS: YPTB2841(aarC)
            YPI: YpsIP31758_1186(ispG)
            SFL: SF2561(gcpE)
            SFX: S2733(gcpE)
            SFV: SFV_2562(gcpE)
            SSN: SSON_2597(gcpE)
            SBO: SBO_2539(gcpE)
            SDY: SDY_2711(gcpE)
            ECA: ECA3220(ispG)
            PLU: plu1376(gcpE)
            BUC: BU287(gcpE)
            BAS: BUsg276(gcpE)
            WBR: WGLp573(gcpE)
            SGL: SG1760
            ENT: Ent638_3009
            SPE: Spro_3609
            BPN: BPEN_551(ispG)
            HIN: HI0368(gcpE)
            HIT: NTHI0488(gcpE)
            HIP: CGSHiEE_01180(ispG)
            HDU: HD1037(ispG)
            HSO: HS_0404(ispE)
            PMU: PM2010(gcpE)
            MSU: MS1919(gcpE)
            APL: APL_1176(ispG)
            ASU: Asuc_2027
            XFA: XF2575
            XFT: PD1956(gcpE)
            XCC: XCC1781
            XCB: XC_2455
            XCV: XCV1829(ispG)
            XAC: XAC1799
            XOO: XOO2229
            XOM: XOO_2095(XOO2095)
            VCH: VC0759
            VVU: VV1_0427(gcpE)
            VVY: VV0766
            VPA: VP0608
            VFI: VF0629
            PPR: PBPRA0763
            PAE: PA3803
            PAU: PA14_14880(gcpE)
            PAP: PSPA7_1311(ispG)
            PPU: PP_0853(ispG)
            PPF: Pput_0883
            PST: PSPTO_1434(ispG)
            PSB: Psyr_1248(ispG)
            PSP: PSPPH_1320(ispG)
            PFL: PFL_4954(ispG)
            PFO: Pfl_4601(ispG)
            PEN: PSEEN1021(ispG)
            PMY: Pmen_3500
            PAR: Psyc_0682(gcpE)
            PCR: Pcryo_0652
            PRW: PsycPRwf_1902
            ACI: ACIAD0561(ispG)
            SON: SO_3312(ispG)
            SDN: Sden_1256
            SFR: Sfri_1116
            SAZ: Sama_2365
            SBL: Sbal_2990
            SBM: Shew185_3005
            SLO: Shew_1290
            SPC: Sputcn32_2652
            SSE: Ssed_1432
            SPL: Spea_1305
            SHE: Shewmr4_1228
            SHM: Shewmr7_1299
            SHN: Shewana3_1229
            SHW: Sputw3181_1355
            ILO: IL2034(gcpE)
            CPS: CPS_4252(ispG)
            PHA: PSHAb0138(ispG)
            PAT: Patl_3126
            SDE: Sde_1434
            PIN: Ping_1168
            MAQ: Maqu_1127
            MCA: MCA2483
            FTU: FTT0607(ispG)
            FTF: FTF0607(ispG)
            FTW: FTW_1121(ispG)
            FTL: FTL_0875
            FTH: FTH_0861(ispG)
            FTA: FTA_0926(ispG)
            FTN: FTN_1076(ispG)
            NOC: Noc_1749
            AEH: Mlg_1461
            HHA: Hhal_0132
            HCH: HCH_04456(ispG)
            CSA: Csal_2854
            ABO: ABO_1860(ispG)
            MMW: Mmwyl1_1356
            AHA: AHA_1759(ispG)
            BCI: BCI_0008(ispG)
            RMA: Rmag_0384
            VOK: COSY_0358(ispG)
            NME: NMB1310
            NMA: NMA1524
            NGO: NGO0594
            CVI: CV_3538
            RSO: RSc1215(RS02710)
            REU: Reut_A2086
            RME: Rmet_2106
            BMA: BMA1345(ispG)
            BMV: BMASAVP1_A1835(ispG)
            BML: BMA10299_A0062(ispG)
            BMN: BMA10247_1107(ispG)
            BXE: Bxe_A1594
            BVI: Bcep1808_1739
            BUR: Bcep18194_A5113
            BCN: Bcen_6267
            BCH: Bcen2424_1812
            BAM: Bamb_1750
            BPS: BPSL1513
            BPM: BURPS1710b_2355(ispG)
            BPL: BURPS1106A_2228(ispG)
            BPD: BURPS668_2190(ispG)
            BTE: BTH_I2234(ispG)
            PNU: Pnuc_1291
            BPE: BP2199(ispG)
            BPA: BPP2855(ispG)
            BBR: BB3176(ispG)
            RFR: Rfer_2307
            POL: Bpro_2608
            PNA: Pnap_1872
            AAV: Aave_1424
            AJS: Ajs_1170
            VEI: Veis_0080
            MPT: Mpe_A1996
            HAR: HEAR1264(ispG)
            MMS: mma_2127
            NEU: NE0148 NE0149
            NET: Neut_2168
            NMU: Nmul_A2377
            EBA: ebA1261(ispG)
            AZO: azo0927(gcpE)
            DAR: Daro_2985
            TBD: Tbd_0594
            MFA: Mfla_1620
            HPY: HP0625(gcpE)
            HPJ: jhp0569
            HPA: HPAG1_0608
            HHE: HH0807(gcpE)
            HAC: Hac_0735(gcpE)
            WSU: WS1302(gcpE)
            TDN: Tmden_0376
            CJE: Cj0686(gcpE)
            CJR: CJE0785(ispG)
            CJJ: CJJ81176_0709(ispG)
            CJU: C8J_0654(ispG)
            CJD: JJD26997_1321(ispG)
            CFF: CFF8240_0983(ispG)
            CCV: CCV52592_0322(ispG) CCV52592_0908
            CHA: CHAB381_0996(ispG)
            CCO: CCC13826_0680(ispG) CCC13826_0886
            ABU: Abu_0656(ispG)
            NIS: NIS_0337(ispG)
            SUN: SUN_2134(ispG)
            GSU: GSU1459(ispG)
            GME: Gmet_1353
            GUR: Gura_2799
            PCA: Pcar_2368
            PPD: Ppro_1751
            DVU: DVU1344(ispG)
            DVL: Dvul_1724
            DDE: Dde_2207
            LIP: LI0024(gcpE)
            DPS: DP1163(gcpE)
            ADE: Adeh_3949
            AFW: Anae109_0476
            SAT: SYN_00906
            SFU: Sfum_2112
            WOL: WD0116
            WBM: Wbm0782
            AMA: AM741(gcpE)
            APH: APH_0442(ispG)
            ERU: Erum4730(ispG)
            ERW: ERWE_CDS_04950(ispG)
            ERG: ERGA_CDS_04850(ispG)
            ECN: Ecaj_0471
            ECH: ECH_0559(ispG)
            NSE: NSE_0799(ispG)
            PUB: SAR11_0517(gcpE)
            MLO: mll3792
            MES: Meso_3337
            PLA: Plav_1746
            SME: SMc03888(gcpE)
            SMD: Smed_3133
            ATU: Atu2723(gcpE)
            ATC: AGR_C_4936
            RET: RHE_CH04009(gcpE)
            RLE: RL4630
            BME: BMEI0269
            BMF: BAB1_1788
            BMS: BR1778(gcpE)
            BMB: BruAb1_1761(gcpE)
            BOV: BOV_1713(ispG)
            OAN: Oant_1123
            BJA: blr0936(gcpE)
            BRA: BRADO0546(ispG)
            BBT: BBta_7633(ispG)
            RPA: RPA0519(gcpE)
            RPB: RPB_0522
            RPC: RPC_0491
            RPD: RPD_0317
            RPE: RPE_0183
            NWI: Nwi_0494
            NHA: Nham_0620
            BHE: BH15270(gcpE)
            BQU: BQ12180(gcpE)
            BBK: BARBAKC583_0119(ispG)
            XAU: Xaut_1889
            CCR: CC_0851
            SIL: SPO2594(ispG)
            SIT: TM1040_0862
            RSP: RSP_2982(gcpE)
            RSH: Rsph17029_1628
            RSQ: Rsph17025_1861
            JAN: Jann_1935
            RDE: RD1_2825(ispG)
            PDE: Pden_1820
            MMR: Mmar10_2256
            HNE: HNE_0621(ispG)
            ZMO: ZMO0180
            NAR: Saro_0417
            SAL: Sala_1848
            SWI: Swit_2126
            ELI: ELI_10365
            GOX: GOX0034
            GBE: GbCGDNIH1_0604
            ACR: Acry_1012
            RRU: Rru_A0747
            MAG: amb1616
            MGM: Mmc1_3591
            ABA: Acid345_1423
            SUS: Acid_1193
            BSU: BG11671(yqfY)
            BHA: BH1401(gcpE)
            BAN: BA4502(gcpE)
            BAR: GBAA4502(gcpE)
            BAA: BA_4950
            BAT: BAS4180
            BCE: BC4276
            BCA: BCE_4358(gcpE)
            BCZ: BCZK4028(gcpE)
            BCY: Bcer98_3006
            BTK: BT9727_4018(gcpE)
            BTL: BALH_3871(ispG)
            BLI: BL03725(ispG)
            BLD: BLi02683(yqfY)
            BCL: ABC1708
            BAY: RBAM_023380 RBAM_023470(yqfP)
            BPU: BPUM_2235
            GKA: GK2466
            LMO: lmo1441
            LMF: LMOf2365_1460(ispG)
            STH: STH1501
            CAC: CAC1797(gcpE)
            CPE: CPE1692(gcpE)
            CPF: CPF_1946(ispG)
            CPR: CPR_1664(ispG)
            CTC: CTC01270(gcpE)
            CNO: NT01CX_2141(ispG)
            CTH: Cthe_0997
            CDF: CD2128(ispG)
            CBA: CLB_2288(gcpE)
            CBH: CLC_2271(gcpE)
            CBF: CLI_2480(gcpE)
            CBE: Cbei_1197
            CKL: CKL_1425(ispG)
            AMT: Amet_2680
            CHY: CHY_1776(ispG)
            DSY: DSY2537
            DRM: Dred_1968
            SWO: Swol_0891
            CSC: Csac_2351
            TTE: TTE1400(gcpE)
            MTA: Moth_1043
            MPE: MYPE9400
            MGA: MGA_1156
            MTU: Rv2868c
            MTC: MT2936(aarC)
            MBO: Mb2893c(gcpE)
            MLE: ML1581(gcpE)
            MPA: MAP2938c(gcpE)
            MAV: MAV_3725(ispG)
            MSM: MSMEG_2580(ispG)
            MVA: Mvan_2262
            MGI: Mflv_4081
            MMC: Mmcs_2044
            MKM: Mkms_2090
            MJL: Mjls_2027
            CGL: NCgl1938(cgl2014)
            CGB: cg2206(ispG)
            CEF: CE1903
            CDI: DIP1498(gcpE)
            CJK: jk1165(ispG)
            NFA: nfa41180
            RHA: RHA1_ro06590(ispG)
            SCO: SCO5696(gcpE) SCO6767(SC6A5.16)
            SMA: SAV1647(ispG2) SAV2561(ispG1)
            TWH: TWT186(ispG)
            TWS: TW586(ispG)
            LXX: Lxx12200(gcpE)
            ART: Arth_1404
            AAU: AAur_1546(ispG)
            PAC: PPA1506
            NCA: Noca_3202
            TFU: Tfu_0749
            FRA: Francci3_3573
            FAL: FRAAL5772(ispG)
            ACE: Acel_1522
            KRA: Krad_1429
            SEN: SACE_5992
            STP: Strop_1352
            BLO: BL0098(ispG)
            BAD: BAD_1157(ispG)
            RXY: Rxyl_1406
            FNU: FN0478(gcpE)
            RBA: RB2118(gcpE)
            CTR: CT057(gcpE)
            CTA: CTA_0061(gcpE)
            CMU: TC0327
            CPN: CPn0373(gcpE)
            CPA: CP0383
            CPJ: CPj0373(gcpE)
            CPT: CpB0385(aarC)
            CCA: CCA00423(gcpE)
            CAB: CAB409
            CFE: CF0584(gcpE)
            PCU: pc0740(gcpE)
            TPA: TP0446
            TDE: TDE1265(ispG)
            LIL: LA3160(gcpE)
            LIC: LIC10955(gcpE)
            LBJ: LBJ_0737(gcpE)
            LBL: LBL_2341(gcpE)
            SYN: slr2136(gcpE)
            SYW: SYNW1174(gcpE)
            SYC: syc0817_d
            SYF: Synpcc7942_0713
            SYD: Syncc9605_1298
            SYE: Syncc9902_1179
            SYG: sync_1674(ispG)
            SYR: SynRCC307_1462(ispG)
            SYX: SynWH7803_1475(ispG)
            CYA: CYA_2387(ispG)
            CYB: CYB_0121(ispG)
            TEL: tlr0996
            GVI: gll3622
            ANA: all2501
            AVA: Ava_0433
            PMA: Pro1015(gcpE)
            PMM: PMM0676(gcpE)
            PMT: PMT0777(gcpE)
            PMN: PMN2A_0109
            PMI: PMT9312_0676
            PMB: A9601_07311(gcpE)
            PMC: P9515_07491(gcpE)
            PMF: P9303_14341(gcpE)
            PMG: P9301_07291(gcpE)
            PMH: P9215_07611(gcpE)
            PME: NATL1_07341(gcpE)
            TER: Tery_4522
            BTH: BT_2517
            BFR: BF4365
            BFS: BF4164
            PGI: PG0952(ispG)
            SRU: SRU_0682(ispG)
            CHU: CHU_2192(ispG)
            CTE: CT0147(gcpE)
            CCH: Cag_0349
            CPH: Cpha266_0225
            PVI: Cvib_1613
            PLT: Plut_1970
            DET: DET0369(ispG)
            DEH: cbdb_A311(ispG)
            DEB: DehaBAV1_0351
            DRA: DR_0386
            DGE: Dgeo_0704
            TTH: TTC1677(gcpE)
            TTJ: TTHA0305
            AAE: aq_1540(gcpE)
            TMA: TM0891
            TPT: Tpet_0036
            TME: Tmel_0263
            FNO: Fnod_0952
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.4.3
            ExPASy - ENZYME nomenclature database: 1.17.4.3
            ExplorEnz - The Enzyme Database: 1.17.4.3
            ERGO genome analysis and discovery system: 1.17.4.3
            BRENDA, the Enzyme Database: 1.17.4.3
///
ENTRY       EC 1.17.5.1                 Enzyme
NAME        phenylacetyl-CoA dehydrogenase;
            phenylacetyl-CoA:acceptor oxidoreductase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With a quinone or similar compound as acceptor
SYSNAME     phenylacetyl-CoA:quinone oxidoreductase
REACTION    phenylacetyl-CoA + H2O + 2 quinone = phenylglyoxylyl-CoA + 2 quinol
            [RN:R07222]
ALL_REAC    R07222
SUBSTRATE   phenylacetyl-CoA [CPD:C00582];
            H2O [CPD:C00001];
            quinone [CPD:C00472]
PRODUCT     phenylglyoxylyl-CoA [CPD:C15524];
            quinol [CPD:C00530]
COMMENT     The enzyme from Thauera aromatica is a membrane-bound
            molybdenum---iron---sulfur protein. The enzyme is specific for
            phenylacetyl-CoA as substrate. Phenylacetate, acetyl-CoA,
            benzoyl-CoA, propanoyl-CoA, crotonyl-CoA, succinyl-CoA and
            3-hydroxybenzoyl-CoA cannot act as substrates. The oxygen atom
            introduced into the product, phenylglyoxylyl-CoA, is derived from
            water and not molecular oxygen. Duroquinone, menaquinone and
            2,6-dichlorophenolindophenol (DCPIP) can act as acceptor, but the
            likely physiological acceptor is ubiquinone [1]. A second enzyme, EC
            3.1.2.25, phenylacetyl-CoA hydrolase, converts the
            phenylglyoxylyl-CoA formed into phenylglyoxylate.
REFERENCE   1  [PMID:10336636]
  AUTHORS   Rhee SK, Fuchs G.
  TITLE     Phenylacetyl-CoA:acceptor oxidoreductase, a membrane-bound
            molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of
            phenylalanine in the denitrifying bacterium Thauera aromatica.
  JOURNAL   Eur. J. Biochem. 262 (1999) 507-15.
  ORGANISM  Thauera aromatica
REFERENCE   2  [PMID:9575237]
  AUTHORS   Schneider S, Fuchs G.
  TITLE     Phenylacetyl-CoA:acceptor oxidoreductase, a new alpha-oxidizing
            enzyme that produces phenylglyoxylate. Assay, membrane localization,
            and differential production in Thauera aromatica.
  JOURNAL   Arch. Microbiol. 169 (1998) 509-16.
  ORGANISM  Thauera aromatica
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.5.1
            ExPASy - ENZYME nomenclature database: 1.17.5.1
            ExplorEnz - The Enzyme Database: 1.17.5.1
            ERGO genome analysis and discovery system: 1.17.5.1
            BRENDA, the Enzyme Database: 1.17.5.1
///
ENTRY       EC 1.17.99.1                Enzyme
NAME        4-cresol dehydrogenase (hydroxylating);
            p-cresol-(acceptor) oxidoreductase (hydroxylating);
            p-cresol methylhydroxylase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With other acceptors
SYSNAME     4-cresol:acceptor oxidoreductase (methyl-hydroxylating)
REACTION    4-cresol + acceptor + H2O = 4-hydroxybenzaldehyde + reduced acceptor
            [RN:R07223]
ALL_REAC    R07223 > R02675
SUBSTRATE   4-cresol [CPD:C01468];
            acceptor [CPD:C00028];
            H2O [CPD:C00001]
PRODUCT     4-hydroxybenzaldehyde [CPD:C00633];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016];
            Cytochrome c [CPD:C00524]
COMMENT     A flavocytochrome c (FAD). Phenazine methosulfate can act as
            acceptor. A quinone methide is probably formed as intermediate. The
            first hydroxylation forms 4-hydroxybenzyl alcohol; a second
            hydroxylation converts this into 4-hydroxybenzaldehyde.
REFERENCE   1  [PMID:588247]
  AUTHORS   Hopper DJ, Taylor DG.
  TITLE     The purification and properties of p-cresol-(acceptor)
            oxidoreductase (hydroxylating), a flavocytochrome from Pseudomonas
            putida.
  JOURNAL   Biochem. J. 167 (1977) 155-62.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2  [PMID:7391034]
  AUTHORS   McIntire W, Edmondson DE, Singer TP, Hopper DJ.
  TITLE     8 alpha-O-Tyrosyl-FAD: a new form of covalently bound flavin from
            p-cresol methylhydroxylase.
  JOURNAL   J. Biol. Chem. 255 (1980) 6553-5.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00622  Toluene and xylene degradation
ORTHOLOGY   KO: K05797  4-cresol dehydrogenase (hydroxylating)
GENES       PAT: Patl_1202
            NOC: Noc_2406
            NET: Neut_1656
            EBA: ebA3165(pchF)
            RRU: Rru_A3112
STRUCTURES  PDB: 1DII  1DIQ  1WVE  1WVF  
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.99.1
            ExPASy - ENZYME nomenclature database: 1.17.99.1
            ExplorEnz - The Enzyme Database: 1.17.99.1
            ERGO genome analysis and discovery system: 1.17.99.1
            UM-BBD (Biocatalysis/Biodegradation Database): 1.17.99.1
            BRENDA, the Enzyme Database: 1.17.99.1
            CAS: 66772-07-4
///
ENTRY       EC 1.17.99.2                Enzyme
NAME        ethylbenzene hydroxylase;
            ethylbenzene dehydrogenase;
            ethylbenzene:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With other acceptors
SYSNAME     ethylbenzene:acceptor oxidoreductase
REACTION    ethylbenzene + H2O + acceptor = (S)-1-phenylethanol + reduced
            acceptor [RN:R05745]
ALL_REAC    R05745
SUBSTRATE   ethylbenzene [CPD:C07111];
            H2O [CPD:C00001];
            acceptor [CPD:C00028]
PRODUCT     (S)-1-phenylethanol [CPD:C11348];
            reduced acceptor [CPD:C00030]
COMMENT     Involved in the anaerobic catabolism of ethylbenzene by denitrifying
            bacteria. Ethylbenzene is the preferred substrate; the enzyme from
            some strains oxidizes propylbenzene, 1-ethyl-4-fluorobenzene,
            3-methylpent-2-ene and ethylidenecyclohexane. Toluene is not
            oxidized. p-Benzoquinone or ferrocenium can act as electron
            acceptor. Contains molybdopterin, [4Fe-4S] clusters and heme b.
REFERENCE   1  [PMID:11294876]
  AUTHORS   Kniemeyer O, Heider J.
  TITLE     Ethylbenzene dehydrogenase, a novel hydrocarbon-oxidizing
            molybdenum/iron-sulfur/heme enzyme.
  JOURNAL   J. Biol. Chem. 276 (2001) 21381-6.
  ORGANISM  Azoarcus sp.
REFERENCE   2  [PMID:11443088]
  AUTHORS   Johnson HA, Pelletier DA, Spormann AM.
  TITLE     Isolation and characterization of anaerobic ethylbenzene
            dehydrogenase, a novel Mo-Fe-S enzyme.
  JOURNAL   J. Bacteriol. 183 (2001) 4536-42.
  ORGANISM  Azoarcus sp.
PATHWAY     PATH: map00642  Ethylbenzene degradation
STRUCTURES  PDB: 2IVF  
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.99.2
            ExPASy - ENZYME nomenclature database: 1.17.99.2
            ExplorEnz - The Enzyme Database: 1.17.99.2
            ERGO genome analysis and discovery system: 1.17.99.2
            UM-BBD (Biocatalysis/Biodegradation Database): 1.17.99.2
            BRENDA, the Enzyme Database: 1.17.99.2
///
ENTRY       EC 1.17.99.3                Enzyme
NAME        3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA
            24-hydroxylase;
            trihydroxycoprostanoyl-CoA oxidase;
            THC-CoA oxidase;
            THCA-CoA oxidase;
            3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase;
            3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate
            24-hydroxylase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With other acceptors
SYSNAME     (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA:ac
            ceptor 24-oxidoreductase (24R-hydroxylating)
REACTION    (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA +
            H2O + acceptor =
            (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-
            oyl-CoA + reduced acceptor [RN:R07374]
ALL_REAC    R07374
SUBSTRATE   (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA
            [CPD:C15613];
            H2O [CPD:C00001];
            acceptor [CPD:C00028]
PRODUCT     (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-
            oyl-CoA [CPD:C15614];
            reduced acceptor [CPD:C00030]
COMMENT     Requires ATP. The reaction in mammals possibly involves
            dehydrogenation to give a 24(25)-double bond followed by hydration
            [1]. However, in amphibians such as the Oriental fire-bellied toad
            (Bombina orientalis), it is probable that the product is formed via
            direct hydroxylation of the saturated side chain of
            (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate and
            not via hydration of a 24(25) double bond [5]. In microsomes, the
            free acid is preferred to the coenzyme A ester, whereas in
            mitochondria, the coenzyme A ester is preferred to the free-acid
            form of the substrate [1].
REFERENCE   1  [PMID:240854]
  AUTHORS   Gustafsson J.
  TITLE     Biosynthesis of cholic acid in rat liver. 24-Hydroxylation of
            3alpha, 7alpha, 12alpha-trihydroxy-5beta-cholestanoic acid.
  JOURNAL   J. Biol. Chem. 250 (1975) 8243-7.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:2156865]
  AUTHORS   Schepers L, Van Veldhoven PP, Casteels M, Eyssen HJ, Mannaerts GP.
  TITLE     Presence of three acyl-CoA oxidases in rat liver peroxisomes. An
            inducible fatty acyl-CoA oxidase, a noninducible fatty acyl-CoA
            oxidase, and a noninducible trihydroxycoprostanoyl-CoA oxidase.
  JOURNAL   J. Biol. Chem. 265 (1990) 5242-6.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:8856068]
  AUTHORS   Dieuaide-Noubhani M, Novikov D, Baumgart E, Vanhooren JC, Fransen M,
            Goethals M, Vandekerckhove J, Van Veldhoven PP, Mannaerts GP.
  TITLE     Further characterization of the peroxisomal 3-hydroxyacyl-CoA
            dehydrogenases from rat liver. Relationship between the different
            dehydrogenases and evidence that fatty acids and the C27 bile acids
            di- and tri-hydroxycoprostanic acids are metabolized by separate
            multifunctional proteins.
  JOURNAL   Eur. J. Biochem. 240 (1996) 660-6.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:8856068]
  AUTHORS   Dieuaide-Noubhani M, Novikov D, Baumgart E, Vanhooren JC, Fransen M,
            Goethals M, Vandekerckhove J, Van Veldhoven PP, Mannaerts GP.
  TITLE     Further characterization of the peroxisomal 3-hydroxyacyl-CoA
            dehydrogenases from rat liver. Relationship between the different
            dehydrogenases and evidence that fatty acids and the C27 bile acids
            di- and tri-hydroxycoprostanic acids are metabolized by separate
            multifunctional proteins.
  JOURNAL   Eur. J. Biochem. 240 (1996) 660-6.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:9218493]
  AUTHORS   Pedersen JI, Eggertsen G, Hellman U, Andersson U, Bjorkhem I.
  TITLE     Molecular cloning and expression of cDNA encoding
            3alpha,7alpha,12alpha-trihydroxy-5beta-chole stanoyl-CoA oxidase
            from rabbit liver.
  JOURNAL   J. Biol. Chem. 272 (1997) 18481-9.
  ORGANISM  rabbit
REFERENCE   6  [PMID:12543708]
  AUTHORS   Russell DW.
  TITLE     The enzymes, regulation, and genetics of bile acid synthesis.
  JOURNAL   Annu. Rev. Biochem. 72 (2003) 137-74.
PATHWAY     PATH: map03320  PPAR signaling pathway
ORTHOLOGY   KO: K10214  3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA
                        24-hydroxylase
GENES       HSA: 8309(ACOX2)
            PTR: 460479(ACOX2)
            MMU: 93732(Acox2)
            RNO: 252898(Acox2)
            CFA: 484710(ACOX2)
            BTA: 514969(MGC159638)
            GGA: 416068(ACOX2)
            XLA: 414480(MGC83074)
            XTR: 548740(LOC548740)
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.99.3
            ExPASy - ENZYME nomenclature database: 1.17.99.3
            ExplorEnz - The Enzyme Database: 1.17.99.3
            ERGO genome analysis and discovery system: 1.17.99.3
            BRENDA, the Enzyme Database: 1.17.99.3
///
ENTRY       EC 1.17.99.4                Enzyme
NAME        uracil/thymine dehydrogenase;
            uracil oxidase;
            uracil-thymine oxidase;
            uracil dehydrogenase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With other acceptors
SYSNAME     uracil:acceptor oxidoreductase
REACTION    (1) uracil + H2O + acceptor = barbiturate + reduced acceptor
            [RN:R00976];
            (2) thymine + H2O + acceptor = 5-methylbarbiturate + reduced
            acceptor [RN:R01413]
ALL_REAC    R00976 R01413
SUBSTRATE   uracil [CPD:C00106];
            H2O [CPD:C00001];
            acceptor [CPD:C00028];
            thymine [CPD:C00178]
PRODUCT     barbiturate [CPD:C00813];
            reduced acceptor [CPD:C00030];
            5-methylbarbiturate [CPD:C05281]
COMMENT     Forms part of the oxidative pyrimidine-degrading pathway in some
            microorganisms, along with EC 3.5.2.1 (barbiturase) and EC 3.5.1.95
            (N-malonylurea hydrolase). Mammals, plants and other microorganisms
            utilize the reductive pathway, comprising EC 1.3.1.1 [dihydrouracil
            dehydrogenase (NAD+)] or EC 1.3.1.2 [dihydropyrimidine dehydrogenase
            (NADP+)], EC 3.5.2.2 (dihydropyrimidinase) and EC 3.5.1.6
            (beta-ureidopropionase), with the ultimate degradation products
            being an L-amino acid, NH3 and CO2 [5].
REFERENCE   1  [PMID:12981104]
  AUTHORS   HAYAISHI O, KORNBERG A.
  TITLE     Metabolism of cytosine, thymine, uracil, and barbituric acid by
            bacterial enzymes.
  JOURNAL   J. Biol. Chem. 197 (1952) 717-32.
  ORGANISM  Corynebacterium sp., Mycobacterium sp.
REFERENCE   2  [PMID:14927671]
  AUTHORS   WANG TP, LAMPEN JO.
  TITLE     Metabolism of pyrimidines by a soil bacterium.
  JOURNAL   J. Biol. Chem. 194 (1952) 775-83.
  ORGANISM  Bacterium sp.
REFERENCE   3  [PMID:14927672]
  AUTHORS   WANG TP, LAMPEN JO.
  TITLE     Uracil oxidase and the isolation of barbituric acid from uracil
            oxidation.
  JOURNAL   J. Biol. Chem. 194 (1952) 785-91.
REFERENCE   4  [PMID:14955523]
  AUTHORS   LARA FJ.
  TITLE     On the decomposition of pyrimidines by bacteria. II. Studies with
            cell-free enzyme preparations.
  JOURNAL   J. Bacteriol. 64 (1952) 279-85.
  ORGANISM  Nocardia corallina
REFERENCE   5  [PMID:11485332]
  AUTHORS   Soong CL, Ogawa J, Shimizu S.
  TITLE     Novel amidohydrolytic reactions in oxidative pyrimidine metabolism:
            analysis of the barbiturase reaction and discovery of a novel
            enzyme, ureidomalonase.
  JOURNAL   Biochem. Biophys. Res. Commun. 286 (2001) 222-6.
  ORGANISM  Corynebacterium sp., Mycobacterium sp.
PATHWAY     PATH: map00240  Pyrimidine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.99.4
            ExPASy - ENZYME nomenclature database: 1.17.99.4
            ExplorEnz - The Enzyme Database: 1.17.99.4
            ERGO genome analysis and discovery system: 1.17.99.4
            BRENDA, the Enzyme Database: 1.17.99.4
            CAS: 9029-00-9
///
ENTRY       EC 1.17.99.5                Enzyme
NAME        bile-acid 7alpha-dehydroxylase;
            cholate 7alpha-dehydroxylase;
            7alpha-dehydroxylase;
            bile acid 7-dehydroxylase;
            deoxycholate:NAD+ oxidoreductase
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With other acceptors
SYSNAME     deoxycholate:FAD oxidoreductase (7alpha-dehydroxylating)
REACTION    (1) deoxycholate + FAD + H2O = cholate + FADH2 [RN:R07220];
            (2) lithocholate + FAD + H2O = chenodeoxycholate + FADH2 [RN:R03978]
ALL_REAC    R03978 R07220
SUBSTRATE   deoxycholate [CPD:C04483];
            FAD [CPD:C00016];
            H2O [CPD:C00001];
            lithocholate [CPD:C03990]
PRODUCT     cholate [CPD:C00695];
            FADH2 [CPD:C01352];
            chenodeoxycholate [CPD:C02528]
COMMENT     Under physiological conditions, the reactions occur in the reverse
            direction to that shown above. This enzyme is highly specific for
            bile-acid substrates and requires a free C-24 carboxy group and an
            unhindered 7alpha-hydroxy group on the B-ring of the steroid nucleus
            for activity, as found in cholate and chenodeoxycholate. The
            reaction is stimulated by the presence of NAD+ but is inhibited by
            excess NADH. This unusual regulation by the NAD+/NADH ratio is most
            likely the result of the intermediates being linked at C-24 by an
            anhydride bond to the 5'-diphosphate of 3'-phospho-ADP [2,5,6].
            Allo-deoxycholate is also formed as a side-product of the
            7alpha-dehydroxylation of cholate [6]. The enzyme is present in
            intestinal anaerobic bacteria [6], even though its products are
            important in mammalian physiology.
REFERENCE   1  [PMID:7276750]
  AUTHORS   White BA, Cacciapuoti AF, Fricke RJ, Whitehead TR, Mosbach EH,
            Hylemon PB.
  TITLE     Cofactor requiremets for 7 alpha-dehydroxylation of cholic and
            chenodeoxycholic acid in cell extracts of the intestinal anaerobic
            bacterium, Eubacterium species V.P.I. 13708.
  JOURNAL   J. Lipid. Res. 22 (1981) 891-8.
  ORGANISM  Eubacterium sp.
REFERENCE   2  [PMID:6833878]
  AUTHORS   White BA, Paone DA, Cacciapuoti AF, Fricke RJ, Mosbach EH, Hylemon
            PB.
  TITLE     Regulation of bile acid 7-dehydroxylase activity by NAD+ and NADH in
            cell extracts of Eubacterium species V.P.I. 12708.
  JOURNAL   J. Lipid. Res. 24 (1983) 20-7.
  ORGANISM  Eubacterium sp.
REFERENCE   3  [PMID:3549693]
  AUTHORS   Coleman JP, White WB, Hylemon PB.
  TITLE     Molecular cloning of bile acid 7-dehydroxylase from Eubacterium sp.
            strain VPI 12708.
  JOURNAL   J. Bacteriol. 169 (1987) 1516-21.
  ORGANISM  Eubacterium sp.
REFERENCE   4  [PMID:12543708]
  AUTHORS   Russell DW.
  TITLE     The enzymes, regulation, and genetics of bile acid synthesis.
  JOURNAL   Annu. Rev. Biochem. 72 (2003) 137-74.
REFERENCE   5  [PMID:3558364]
  AUTHORS   Coleman JP, White WB, Egestad B, Sjovall J, Hylemon PB.
  TITLE     Biosynthesis of a novel bile acid nucleotide and mechanism of 7
            alpha-dehydroxylation by an intestinal Eubacterium species.
  JOURNAL   J. Biol. Chem. 262 (1987) 4701-7.
  ORGANISM  Eubacterium sp.
REFERENCE   6  [PMID:2010697]
  AUTHORS   Hylemon PB, Melone PD, Franklund CV, Lund E, Bjorkhem I.
  TITLE     Mechanism of intestinal 7 alpha-dehydroxylation of cholic acid:
            evidence that allo-deoxycholic acid is an inducible side-product.
  JOURNAL   J. Lipid. Res. 32 (1991) 89-96.
  ORGANISM  Eubacterium sp.
DBLINKS     IUBMB Enzyme Nomenclature: 1.17.99.5
            ExPASy - ENZYME nomenclature database: 1.17.99.5
            ExplorEnz - The Enzyme Database: 1.17.99.5
            ERGO genome analysis and discovery system: 1.17.99.5
            BRENDA, the Enzyme Database: 1.17.99.5
///
ENTRY       EC 1.17.99.-                Enzyme
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups;
            With other acceptors
REACTION    p-Cymene + Oxygen + NADH <=> p-Cumic alcohol + HO- + NAD+
            [RN:R05266]
SUBSTRATE   p-Cymene [CPD:C06575];
            Oxygen [CPD:C00007];
            NADH [CPD:C00004]
PRODUCT     p-Cumic alcohol [CPD:C06576];
            HO- [CPD:C01328];
            NAD+ [CPD:C00003]
///
ENTRY       EC 1.17.-.-                 Enzyme
CLASS       Oxidoreductases;
            Acting on CH or CH2 groups
REACTION    Ethylbenzene + H2O <=> 1-Phenylethanol + 2 H+ [RN:R05495]
SUBSTRATE   Ethylbenzene [CPD:C07111];
            H2O [CPD:C00001]
PRODUCT     1-Phenylethanol [CPD:C07112];
            H+ [CPD:C00080]
///
ENTRY       EC 1.18.1.1                 Enzyme
NAME        rubredoxin-NAD+ reductase;
            rubredoxin reductase;
            rubredoxin-nicotinamide adenine dinucleotide reductase;
            dihydronicotinamide adenine dinucleotide-rubredoxin reductase;
            reduced nicotinamide adenine dinucleotide-rubredoxin reductase;
            NADH-rubredoxin reductase;
            rubredoxin-NAD reductase;
            NADH: rubredoxin oxidoreductase;
            DPNH-rubredoxin reductase;
            NADH-rubredoxin oxidoreductase
CLASS       Oxidoreductases;
            Acting on iron-sulfur proteins as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     rubredoxin:NAD+ oxidoreductase
REACTION    2 reduced rubredoxin + NAD+ + H+ = 2 oxidized rubredoxin + NADH
            [RN:R02000]
ALL_REAC    R02000
SUBSTRATE   reduced rubredoxin [CPD:C00340];
            NAD+ [CPD:C00003];
            H+ [CPD:C00080]
PRODUCT     oxidized rubredoxin [CPD:C00435];
            NADH [CPD:C00004]
COFACTOR    FAD [CPD:C00016];
            Iron [CPD:C00023]
COMMENT     Requires FAD. The enzyme from Clostridium acetobutylicum reduces
            rubredoxin, ferricyanide and dichlorophenolindophenol, but not
            ferredoxin or flavodoxin. The reaction does not occur when NADPH is
            substituted for NADH. Contains iron at the redox centre.
REFERENCE   1  [PMID:4294330]
  AUTHORS   Peterson JA, Kusunose M, Kusunose E, Coon MJ.
  TITLE     Enzymatic omega-oxidation. II. Function of rubredoxin as the
            electron carrier in omega-hydroxylation.
  JOURNAL   J. Biol. Chem. 242 (1967) 4334-40.
  ORGANISM  Pseudomonas oleovorans
REFERENCE   2  [PMID:4335861]
  AUTHORS   .
  TITLE     Enzymatic  -oxidation. VI. Isolation of homogeneous reduced
            diphosphopyridine nucleotide-rubredoxin reductase.
  JOURNAL   J. Biol. Chem. 247 (1972) 2109-16.
  ORGANISM  Pseudomonas oleovorans
REFERENCE   3  [PMID:4403503]
  AUTHORS   Ueda T, Coon MJ.
  TITLE     Enzymatic   oxidation. VII. Reduced diphosphopyridine
            nucleotide-rubredoxin reductase: properties and function as an
            electron carrier in   hydroxylation.
  JOURNAL   J. Biol. Chem. 247 (1972) 5010-6.
  ORGANISM  Pseudomonas oleovorans
REFERENCE   4  [PMID:526302]
  AUTHORS   Petitdemange H, Marczak R, Blusson H, Gay R.
  TITLE     Isolation and properties of reduced nicotinamide adenine
            dinucleotiderubredoxin oxidoreductase of Clostridium acetobutylicum.
  JOURNAL   Biochem. Biophys. Res. Commun. 91 (1979) 1258-65.
  ORGANISM  Clostridium acetobutylicum [GN:cac]
PATHWAY     PATH: map00071  Fatty acid metabolism
ORTHOLOGY   KO: K05297  rubredoxin-NAD+ reductase
GENES       PAE: PA5349
            PAU: PA14_70620(rubB)
            PPU: PP_5314(rubB) PP_5371
            PST: PSPTO_5473(rubB)
            PSB: Psyr_5028
            PSP: PSPPH_5110(rubB)
            PFL: PFL_6103(rubB)
            PFO: Pfl_5601
            PEN: PSEEN5459(rubB)
            ACI: ACIAD1065(rubB)
            SDN: Sden_3466
            CBU: CBU_0276
            TCX: Tcr_0037
            HCH: HCH_00777
            RFR: Rfer_0092
            POL: Bpro_4857
            MPT: Mpe_A3669
            HAR: HEAR0644(norW)
            MMS: mma_0610(rubB)
            NEU: NE1420
            NMU: Nmul_A0171
            EBA: ebA6036
            TBD: Tbd_2315
            MFA: Mfla_2173
            NWI: Nwi_2287
            GOX: GOX1746
            MAG: amb3427
            MGM: Mmc1_3270
STRUCTURES  PDB: 1BFY  
DBLINKS     IUBMB Enzyme Nomenclature: 1.18.1.1
            ExPASy - ENZYME nomenclature database: 1.18.1.1
            ExplorEnz - The Enzyme Database: 1.18.1.1
            ERGO genome analysis and discovery system: 1.18.1.1
            BRENDA, the Enzyme Database: 1.18.1.1
            CAS: 9032-27-3
///
ENTRY       EC 1.18.1.2                 Enzyme
NAME        ferredoxin---NADP+ reductase;
            adrenodoxin reductase;
            ferredoxin-nicotinamide adenine dinucleotide phosphate reductase;
            ferredoxin-NADP+ reductase;
            TPNH-ferredoxin reductase;
            ferredoxin-NADP+ oxidoreductase;
            NADP+:ferredoxin oxidoreductase;
            ferredoxin-TPN reductase;
            reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin
            reductase;
            ferredoxin-NADP+-oxidoreductase;
            NADPH:ferredoxin oxidoreductase;
            ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized)
            reductase;
            ferredoxin---NADP+ reductase
CLASS       Oxidoreductases;
            Acting on iron-sulfur proteins as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     ferredoxin:NADP+ oxidoreductase
REACTION    2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
            [RN:R01195]
ALL_REAC    R01195
SUBSTRATE   reduced ferredoxin [CPD:C00138];
            NADP+ [CPD:C00006];
            H+ [CPD:C00080]
PRODUCT     oxidized ferredoxin [CPD:C00139];
            NADPH [CPD:C00005]
COFACTOR    FAD [CPD:C00016];
            Flavin [CPD:C00176]
COMMENT     A flavoprotein. Can also reduce flavodoxin.
REFERENCE   1
  AUTHORS   Omura, T., Sanders, E., Estabrook, R.W., Cooper, D.Y. and Rosenthal,
            O.
  TITLE     Isolation from adrenal cortex of a nonheme iron protein and a
            flavoprotein functional as a reduced triphosphopyridine
            nucleotide-cytochrome P-450 reductase.
  JOURNAL   Arch. Biochem. Biophys. 117 (1966) 660-673.
  ORGANISM  spinach
REFERENCE   2
  AUTHORS   Shin, M., Tagawa, K. and Arnon, D.I.
  TITLE     Crystallization of ferredoxin-TPN reductase and its role in the
            photosynthetic apparatus of chloroplasts.
  JOURNAL   Biochem. Z. 338 (1963) 84-96.
PATHWAY     PATH: map00195  Photosynthesis
ORTHOLOGY   KO: K00528  ferredoxin--NADP+ reductase
            KO: K02641  ferredoxin--NADP+ reductase
GENES       HSA: 2232(FDXR)
            MMU: 14149(Fdxr)
            RNO: 79122(Fdxr)
            CFA: 475910(FDXR)
            BTA: 282604(FDXR)
            GGA: 769635(FDXR)
            XLA: 495142(LOC495142)
            SPU: 585224(LOC585224)
            DME: Dmel_CG12390(dare)
            CEL: Y62E10A.6
            ATH: AT1G20020(ATLFNR2) AT1G30510(ATRFNR2) AT4G05390(ATRFNR1)
                 AT4G32360 AT5G66190(ATLFNR1)
            OSA: 4328000 4329009 4334338 4339874 4342399
            CME: CMM294C CMR052C
            SCE: YDR376W(ARH1)
            PIC: PICST_52035(ARH1)
            CGR: CAGL0A03014g
            SPO: SPBC3B8.01c
            ANI: AN6272.2
            AFM: AFUA_2G12610
            AOR: AO090026000356
            CNE: CNL05820
            UMA: UM01039.1
            DDI: DDBDRAFT_0187438
            PFA: PF11_0407 PFF1115w
            CPV: cgd8_2710
            CHO: Chro.80316
            TAN: TA09580 TA15585
            TPV: TP01_1180 TP02_0869
            TET: TTHERM_01126420
            TBR: Tb10.70.5510
            TCR: 511367.230
            LMA: LmjF21.0420
            ECO: b3924(fpr)
            ECJ: JW3895(fpr)
            ECE: Z5469(fpr)
            ECS: ECs4849
            ECC: c4876(fpr)
            ECI: UTI89_C4508(fpr)
            ECP: ECP_4133
            ECV: APECO1_2545(fpr)
            ECW: EcE24377A_4458(fpr)
            ECX: EcHS_A4155(fpr)
            STY: STY3786(fpr)
            STT: t3534(fpr)
            SPT: SPA3927(fpr)
            SEC: SC3973(fpr)
            STM: STM4084(fpr)
            YPE: YPO0088(fpr)
            YPK: y0049(fpr)
            YPM: YP_0092(fpr)
            YPA: YPA_3453
            YPN: YPN_3760
            YPS: YPTB0084(fpr)
            YPI: YpsIP31758_0099(fpr)
            SFL: SF4002(fpr)
            SFX: S3745(fpr)
            SFV: SFV_3995(fpr)
            SSN: SSON_4093(fpr)
            SBO: SBO_3941(fpr)
            SDY: SDY_3820(fpr)
            ECA: ECA2073 ECA4269(fpr)
            PLU: plu4769(fpr)
            BUC: BU581(fpr)
            BAS: BUsg560(fpr)
            BAB: bbp527(fpr)
            BCC: BCc_378(fpr)
            WBR: WGLp275(fpr)
            SGL: SG2174
            BFL: Bfl600(fpr)
            BPN: BPEN_622(fpr)
            XFA: XF1889
            XFT: PD0902(fpr)
            XCC: XCC1414(fpr)
            XCB: XC_2824
            XCV: XCV1515
            XAC: XAC1458(fpr)
            XOO: XOO2338(fpr)
            XOM: XOO_2218(XOO2218)
            VVU: VV2_0962
            VVY: VVA1449
            VPA: VPA1586
            VFI: VF1780
            PPR: PBPRA0238
            PAE: PA3397(fpr) PA4615
            PAU: PA14_20140(fpr) PA14_61060(fnr-2)
            PPU: PP_1638(fpr) PP_4646
            PST: PSPTO_4024(fnr-1) PSPTO_4642(fnr-2)
            PSB: Psyr_1387 Psyr_4277
            PSP: PSPPH_3797(fpr1) PSPPH_4334(fpr2)
            PFL: PFL_1241(fpr) PFL_5360(fpr)
            PFO: Pfl_1185 Pfl_4888
            PEN: PSEEN4119(fpr-1) PSEEN4772
            PAR: Psyc_0597 Psyc_0887
            PCR: Pcryo_0586 Pcryo_1535
            ACI: ACIAD0747(fpr) ACIAD2244(fpr)
            ACB: A1S_2293
            SON: SO_0747(fpr)
            SDN: Sden_2896
            SFR: Sfri_0635
            SHE: Shewmr4_3350
            SHN: Shewana3_3520
            ILO: IL0209(fpr) IL2501
            PHA: PSHAb0083(fpr)
            PAT: Patl_0415 Patl_2287
            SDE: Sde_0658
            PIN: Ping_1677
            NOC: Noc_0836
            HCH: HCH_04388
            CSA: Csal_0128
            ABO: ABO_0145(fpr)
            AHA: AHA_0713
            NME: NMB1044 NMB1450
            NMA: NMA1442(fpr) NMA1664
            NMC: NMC1168(fpr)
            NGO: NGO0687 NGO0734
            CVI: CV_0886(fpr) CV_4045
            RSO: RSc1305(fpr)
            REU: Reut_A1764
            REH: H16_B0102 H16_B0739
            BMA: BMA1614(fpr-1) BMA3292(fpr-2)
            BMV: BMASAVP1_A2116(fpr-1) BMASAVP1_A2958(fpr-2)
            BML: BMA10299_A2130(fpr-2) BMA10299_A3199(fpr-1)
            BMN: BMA10247_1389(fpr-1) BMA10247_3388(fpr-2)
            BXE: Bxe_A1424(boxA) Bxe_A4345 Bxe_C0890(boxA)
            BVI: Bcep1808_3138
            BUR: Bcep18194_A6401
            BCN: Bcen_2439
            BCH: Bcen2424_3053
            BAM: Bamb_3098
            BPS: BPSL0241(fpr) BPSL2208(fpr)
            BPM: BURPS1710b_0427(fpr) BURPS1710b_2640(fpr-1)
            BPL: BURPS1106A_2553(fpr)
            BPD: BURPS668_2499(fpr)
            BTE: BTH_I0211
            PNU: Pnuc_1479
            BPE: BP1606(fpr) BP3581
            BPA: BPP2979(fpr) BPP3331
            BBR: BB2945(fpr) BB3782
            RFR: Rfer_0084
            POL: Bpro_4070
            PNA: Pnap_2736
            AAV: Aave_0224
            AJS: Ajs_0153
            VEI: Veis_0852
            HAR: HEAR0930(fpr)
            MMS: mma_1063(fpr)
            EBA: ebA2634(fpr) ebA6110(fpr)
            AZO: azo1280(fpr1) azo2657(fpr2)
            DAR: Daro_1536 Daro_3266
            TBD: Tbd_2358
            MFA: Mfla_0561 Mfla_0729
            ADE: Adeh_3296
            MXA: MXAN_5449(fpr)
            MLO: mll4785
            SME: SMc02122(fpr)
            ATU: Atu1458(mvrA)
            ATC: AGR_C_2692
            RET: RHE_CH02078(fpr)
            RLE: RL2369
            BME: BMEI1591
            BMF: BAB1_0361(fpr)
            BMS: BR0331(fpr)
            BMB: BruAb1_0357(fpr)
            BOV: BOV_0348(fpr)
            BJA: bll0100 blr3195 blr3831(mvrA)
            BRA: BRADO0691(fpr)
            BBT: BBta_6638(boxA) BBta_7495(fpr)
            RPA: RPA1578(fpr)
            RPB: RPB_1477 RPB_1670
            BHE: BH12780(fpr)
            BQU: BQ10090(fpr)
            BBK: BARBAKC583_1092(fpr)
            CCR: CC_3208
            SIL: SPO2637
            SIT: TM1040_1761
            RSP: RSP_1939
            RSH: Rsph17029_0590
            JAN: Jann_1770
            RDE: RD1_2969(fpr)
            PDE: Pden_0658
            MMR: Mmar10_0342
            HNE: HNE_3151
            ZMO: ZMO1753(fpr)
            SWI: Swit_0104
            GOX: GOX1763
            GBE: GbCGDNIH1_1024
            RRU: Rru_A0530
            MGM: Mmc1_0139
            MTU: Rv0886(fprB) Rv3106(fprA)
            MTC: MT0909 MT3189(fprA)
            MBO: Mb0910(fprB) Mb3133(fprA)
            MBB: BCG_0938(fprB) BCG_3131(fprA)
            MLE: ML0666(fprA) ML2134(fprB)
            MPA: MAP0825(fprB) MAP3176(fprA)
            MAV: MAV_1015 MAV_4007 MAV_5072
            MSM: MSMEG_5681
            CGL: NCgl2658(cgl2754) NCgl2719(cgl2818)
            CGB: cg3049(fprA)
            CEF: CE2592 CE2645
            CDI: DIP2056
            CJK: jk0242(fpr1)
            NFA: nfa14090 nfa25880 nfa50890 nfa53620
            RHA: RHA1_ro00406 RHA1_ro00412 RHA1_ro01952 RHA1_ro02240
                 RHA1_ro05112 RHA1_ro07091
            SCO: SCO0681(SCF15.02)
            SMA: SAV1507(fprB)
            TWH: TWT055
            TWS: TW065
            LXX: Lxx01840(frp)
            TFU: Tfu_1915
            FAL: FRAAL3390(fprA)
            KRA: Krad_0656
            SEN: SACE_2001 SACE_4391(fprB)
            BLO: BL0552(fprA)
            BAD: BAD_0061(fprA)
            RBA: RB10463(fpr)
            LIL: LA4327
            LIC: LIC13470
            LBJ: LBJ_2997
            LBL: LBL_0060
            SYN: slr1643(petH)
            SYW: SYNW0751(petH)
            SYC: syc0566_c(petH)
            SYF: Synpcc7942_0978
            SYD: Syncc9605_1917
            SYE: Syncc9902_0749
            SYG: sync_1003
            SYR: SynRCC307_0760(petH)
            SYX: SynWH7803_1560(petH)
            CYA: CYA_1257(petH)
            CYB: CYB_2882(petH)
            TEL: tlr1211(petH)
            GVI: gll2295(petH)
            ANA: all4121(petH)
            AVA: Ava_0782
            PMA: Pro1123(petH)
            PMM: PMM1075(petH)
            PMT: PMT1101(petH)
            PMN: PMN2A_0675(petH)
            PMI: PMT9312_1086
            PMB: A9601_11811(petH)
            PMC: P9515_11651(petH)
            PMF: P9303_09411(petH)
            PMG: P9301_11821(petH)
            PME: NATL1_15081(petH)
            RRS: RoseRS_0005
            RCA: Rcas_4255
            DRA: DR_0496
            DGE: Dgeo_1014
STRUCTURES  PDB: 1B2R  1BJK  1BQE  1BX0  1BX1  1CJC  1E1L  1E62  1E63  1E64  
                 1E6E  1EWY  1FDR  1FNB  1FNC  1FND  1FRN  1FRQ  1GAQ  1GAW  
                 1GJR  1GO2  1GR1  1H42  1H85  1JB9  1OGI  1OGJ  1QFY  1QFZ  
                 1QG0  1QGA  1QGY  1QGZ  1QH0  1QUE  1QUF  1SM4  1W34  1W35  
                 1W87  2B5O  2BGI  2BGJ  2BMW  2BSA  2C7G  2GQW  2GR0  2GR1  
                 2GR2  2GR3  2OK7  2OK8  
DBLINKS     IUBMB Enzyme Nomenclature: 1.18.1.2
            ExPASy - ENZYME nomenclature database: 1.18.1.2
            ExplorEnz - The Enzyme Database: 1.18.1.2
            ERGO genome analysis and discovery system: 1.18.1.2
            BRENDA, the Enzyme Database: 1.18.1.2
            CAS: 9029-33-8
///
ENTRY       EC 1.18.1.3                 Enzyme
NAME        ferredoxin---NAD+ reductase;
            ferredoxin-nicotinamide adenine dinucleotide reductase;
            ferredoxin reductase;
            NAD+-ferredoxin reductase;
            NADH-ferredoxin oxidoreductase;
            reductase, reduced nicotinamide adenine dinucleotide-ferredoxin;
            ferredoxin-NAD+ reductase;
            NADH-ferredoxin reductase;
            NADH2-ferredoxin oxidoreductase;
            NADH flavodoxin oxidoreductase;
            NADH-ferredoxinNAP reductase (component of naphthalene dioxygenase
            multicomponent enzyme system);
            ferredoxin-linked NAD+ reductase;
            NADH-ferredoxinTOL reductase (component of toluene dioxygenase);
            ferredoxin---NAD reductase
CLASS       Oxidoreductases;
            Acting on iron-sulfur proteins as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     ferredoxin:NAD+ oxidoreductase
REACTION    reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH + H+
            [RN:R05875]
ALL_REAC    R05875
SUBSTRATE   reduced ferredoxin [CPD:C00138];
            NAD+ [CPD:C00003]
PRODUCT     oxidized ferredoxin [CPD:C00139];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
REFERENCE   1  [PMID:4147457]
  AUTHORS   Jungermann K, Thauer RK, Leimenstoll G, Decker K.
  TITLE     Function of reduced pyridine nucleotide-ferredoxin oxidoreductases
            in saccharolytic Clostridia.
  JOURNAL   Biochim. Biophys. Acta. 305 (1973) 268-80.
  ORGANISM  Clostridium pasteurianum, Clostridium butyricum
PATHWAY     PATH: map00071  Fatty acid metabolism
ORTHOLOGY   KO: K00529  ferredoxin--NAD+ reductase
GENES       OSA: 4330468
            TET: TTHERM_01104910
            ECO: b2542(hcaD)
            ECJ: JW2526(hcaD)
            ECE: Z3814(hcaD)
            ECS: ECs3408
            ECW: EcE24377A_2827(hcaD)
            ECX: EcHS_A2694(hcaD)
            SFV: SFV_2590(hcaD)
            SSN: SSON_2624(hcaD)
            PLU: plu2209
            XCV: XCV2179
            PEN: PSEEN1146 PSEEN3126 PSEEN3141(benC)
            ACI: ACIAD0991 ACIAD1438(benC) ACIAD1580
            REU: Reut_A1474 Reut_B3777 Reut_B4405
            REH: H16_A1630 H16_B0802
            BMA: BMAA0185(benC) BMAA0206 BMAA1326
            BXE: Bxe_A3591 Bxe_B0185 Bxe_B0913(benC) Bxe_C0579
                 Bxe_C1118(andAa) Bxe_C1193(bphA4)
            BUR: Bcep18194_A3425 Bcep18194_A5822 Bcep18194_A6008
                 Bcep18194_B0579 Bcep18194_B0697 Bcep18194_B0789
                 Bcep18194_B1115 Bcep18194_B1223 Bcep18194_B1344
                 Bcep18194_B1416 Bcep18194_B2322 Bcep18194_B2965
                 Bcep18194_C7008 Bcep18194_C7048
            BCN: Bcen_3668
            BAM: Bamb_2733
            BPS: BPSS0906 BPSS1885 BPSS1905(benC)
            BPM: BURPS1710b_A0980 BURPS1710b_A1001(benC)
                 BURPS1710b_A2504(mopA)
            BTE: BTH_II0491 BTH_II1491
            BPE: BP0585
            BPA: BPP0275
            BBR: BB0278 BB0727
            RFR: Rfer_0300
            MLO: mll9218
            SME: SMc00914
            RET: RHE_CH01347 RHE_CH02643(mocFch) RHE_PE00444(mocFe)
                 RHE_PF00389
            RLE: RL1498 pRL110620 pRL120537
            BJA: blr2831 blr7998
            BRA: BRADO2481 BRADO3963 BRADO4349
            BBT: BBta_1593 BBta_2827 BBta_3631 BBta_4333 BBta_7472
            RPA: RPA3782
            RPB: RPB_3656
            RPC: RPC_1647
            RPE: RPE_1676
            NWI: Nwi_0719
            CCR: CC_3525
            RDE: RD1_0947
            BPU: BPUM_2873
            MSM: MSMEG_1906
            RHA: RHA1_ro01813 RHA1_ro02383 RHA1_ro02386(benC) RHA1_ro02509
                 RHA1_ro02537 RHA1_ro06050 RHA1_ro08162(padAd1)
                 RHA1_ro08163(padAc1) RHA1_ro08179(tpaB1) RHA1_ro08637
                 RHA1_ro08986 RHA1_ro10125(etbAd) RHA1_ro10196(tpaB2)
                 RHA1_ro10212(padAc2) RHA1_ro10213(padAd2) RHA1_ro11067
            ART: Arth_4345
            FRA: Francci3_3074
            FAL: FRAAL3171 FRAAL4010(fprC)
            SEN: SACE_2839(fprC) SACE_3145(fprC) SACE_4511(fprC)
                 SACE_5609(padAd2)
            AVA: Ava_0568 Ava_1533 Ava_2874 Ava_3940 Ava_4258
            CCH: Cag_1567
            HMA: rrnAC0717
            HWA: HQ1120A HQ3319A(hcaD)
            NPH: NP4516A
STRUCTURES  PDB: 1KRH  
DBLINKS     IUBMB Enzyme Nomenclature: 1.18.1.3
            ExPASy - ENZYME nomenclature database: 1.18.1.3
            ExplorEnz - The Enzyme Database: 1.18.1.3
            ERGO genome analysis and discovery system: 1.18.1.3
            BRENDA, the Enzyme Database: 1.18.1.3
            CAS: 39369-37-4
///
ENTRY       EC 1.18.1.4                 Enzyme
NAME        rubredoxin-NAD(P)+ reductase;
            rubredoxin-nicotinamide adenine dinucleotide (phosphate) reductase;
            rubredoxin-nicotinamide adenine;
            dinucleotide phosphate reductase;
            NAD(P)+-rubredoxin oxidoreductase;
            NAD(P)H-rubredoxin oxidoreductase
CLASS       Oxidoreductases;
            Acting on iron-sulfur proteins as donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     rubredoxin:NAD(P)+ oxidoreductase
REACTION    reduced rubredoxin + NAD(P)+ = oxidized rubredoxin + NAD(P)H + H+
            [RN:R02000 R02002]
ALL_REAC    R02000 R02002
SUBSTRATE   reduced rubredoxin [CPD:C00340];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
PRODUCT     oxidized rubredoxin [CPD:C00435];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
COMMENT     The enzyme from Pyrococcus furiosis requires FAD. It reduces a
            number of electron carriers, including benzyl viologen, menadione
            and 2,6-dichloroindophenol, but rubredoxin is the most efficient.
            Ferredoxin is not utilized.
REFERENCE   1  [PMID:6274224]
  AUTHORS   Petitdemange H, Blusson H, Gay R.
  TITLE     Detection of NAD(P)H--rubredoxin oxidoreductases in Clostridia.
  JOURNAL   Anal. Biochem. 116 (1981) 564-70.
  ORGANISM  Clostridium acetobutylicum [GN:cac], Clostridium pasteurianum,
            Clostridium tyrobutyricum
REFERENCE   2  [PMID:10464233]
  AUTHORS   Ma K, Adams MW.
  TITLE     A hyperactive NAD(P)H:Rubredoxin oxidoreductase from the
            hyperthermophilic archaeon Pyrococcus furiosus.
  JOURNAL   J. Bacteriol. 181 (1999) 5530-3.
PATHWAY     PATH: map00071  Fatty acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 1.18.1.4
            ExPASy - ENZYME nomenclature database: 1.18.1.4
            ExplorEnz - The Enzyme Database: 1.18.1.4
            ERGO genome analysis and discovery system: 1.18.1.4
            BRENDA, the Enzyme Database: 1.18.1.4
///
ENTRY       EC 1.18.2.1       Obsolete  Enzyme
NAME        Transferred to 1.18.6.1
CLASS       Oxidoreductases;
            Acting on iron-sulfur proteins as donors;
            With dinitrogen as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.18.6.1, nitrogenase (EC 1.18.2.1 created
            1978, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 1.18.2.1
            ExPASy - ENZYME nomenclature database: 1.18.2.1
            ExplorEnz - The Enzyme Database: 1.18.2.1
            ERGO genome analysis and discovery system: 1.18.2.1
            BRENDA, the Enzyme Database: 1.18.2.1
///
ENTRY       EC 1.18.3.1       Obsolete  Enzyme
NAME        Transferred to 1.12.7.2
CLASS       Oxidoreductases;
            Acting on iron-sulfur proteins as donors;
            With H+ as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.12.7.2, ferredoxin hydrogenase (EC
            1.18.3.1 created 1978, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 1.18.3.1
            ExPASy - ENZYME nomenclature database: 1.18.3.1
            ExplorEnz - The Enzyme Database: 1.18.3.1
            ERGO genome analysis and discovery system: 1.18.3.1
            BRENDA, the Enzyme Database: 1.18.3.1
///
ENTRY       EC 1.18.6.1                 Enzyme
NAME        nitrogenase
CLASS       Oxidoreductases;
            Acting on iron-sulfur proteins as donors;
            With dinitrogen as acceptor
SYSNAME     reduced ferredoxin:dinitrogen oxidoreductase (ATP-hydrolysing)
REACTION    8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized
            ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate [RN:R05185]
ALL_REAC    R05185;
            (other) R00002 R00067 R00153 R01849 R02802 R04782 R05496
SUBSTRATE   reduced ferredoxin [CPD:C00138];
            H+ [CPD:C00080];
            N2 [CPD:C00697];
            ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     oxidized ferredoxin [CPD:C00139];
            H2 [CPD:C00282];
            NH3 [CPD:C00014];
            ADP [CPD:C00008];
            phosphate [CPD:C00009]
COFACTOR    Molybdenum [CPD:C00150];
            Iron-sulfur [CPD:C00824];
            2-Hydroxybutane-1,2,4-tricarboxylate [CPD:C01251];
            Vanadium [CPD:C06267]
INHIBITOR   Oxygen [CPD:C00007]
COMMENT     Requires Mg2+. It is composed of two proteins that can be separated
            but are both required for nitrogenase activity. Dinitrogen reductase
            is a [4Fe-4S] protein, which, with two molecules of ATP and
            ferredoxin, generates an electron. The electron is transferred to
            the other protein, dinitrogenase (molybdoferredoxin). Dinitrogenase
            is a molybdenum-iron protein that reduces dinitrogen in three
            succesive two-electron reductions from nitrogen to diimine to
            hydrazine to two molecules of ammonia. The molybdenum may be
            replaced by vanadium or iron. The reduction is initiated by
            formation of hydrogen in stoichiometric amounts [2]. Acetylene is
            reduced to ethylene (but only very slowly to ethane), azide to
            nitrogen and ammonia, and cyanide to methane and ammonia. In the
            absence of a suitable substrate, hydrogen is slowly formed.
            Ferredoxin may be replaced by flavodoxin [see EC 1.19.6.1
            nitrogenase (flavodoxin)].
REFERENCE   1  [PMID:4390523]
  AUTHORS   Zumft WG, Paneque A, Aparicio PJ, Losada M.
  TITLE     Mechanism of nitrate reduction in Chlorella.
  JOURNAL   Biochem. Biophys. Res. Commun. 36 (1969) 980-6.
REFERENCE   2  [PMID:3200830]
  AUTHORS   Liang J, Burris RH.
  TITLE     Hydrogen burst associated with nitrogenase-catalyzed reactions.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 9446-50.
  ORGANISM  Azotobacter vinelandii
REFERENCE   3  [PMID:15382920]
  AUTHORS   Dance I.
  TITLE     The mechanism of nitrogenase. Computed details of the site and
            geometry of binding of alkyne and alkene substrates and
            intermediates.
  JOURNAL   J. Am. Chem. Soc. 126 (2004) 11852-63.
REFERENCE   4  [PMID:10852721]
  AUTHORS   Chan JM, Wu W, Dean DR, Seefeldt LC.
  TITLE     Construction and characterization of a heterodimeric iron protein:
            defining roles for adenosine triphosphate in nitrogenase catalysis.
  JOURNAL   Biochemistry. 39 (2000) 7221-8.
  ORGANISM  Azotobacter vinelandii
PATHWAY     PATH: map00625  Tetrachloroethene degradation
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00531  nitrogenase
            KO: K02586  nitrogenase molybdenum-iron protein alpha chain
            KO: K02588  nitrogenase iron protein NifH
            KO: K02591  nitrogenase molybdenum-iron protein beta chain
GENES       ECI: UTI89_C2387(mrp)
            ECA: ECA2954(nifK) ECA2955(nifD) ECA2956(nifH)
            MCA: MCA0229(nifH) MCA0230(nifD) MCA0231(nifK)
            HHA: Hhal_0263 Hhal_0264 Hhal_0272 Hhal_0273 Hhal_0274 Hhal_1610
                 Hhal_1634
            BXE: Bxe_B1465(nifH) Bxe_B1466(nifD) Bxe_B1467(nifK)
            BVI: Bcep1808_6015 Bcep1808_6016 Bcep1808_6017 Bcep1808_6020
                 Bcep1808_6021
            PNA: Pnap_2324 Pnap_2325 Pnap_2343 Pnap_2344 Pnap_2345
            AZO: azo0538(nifH) azo0539(nifD) azo0540(nifK)
            DAR: Daro_1413 Daro_1414 Daro_1415
            WSU: WS1391(nifK) WS1392(nifD) WS1394(nifH)
            GSU: GSU2819(nifK) GSU2820(nifD) GSU2821(nifH)
            GME: Gmet_0662 Gmet_0663 Gmet_0664
            GUR: Gura_1175 Gura_1176 Gura_1177 Gura_1201 Gura_3889
            PCA: Pcar_2098 Pcar_2099 Pcar_2100
            PPD: Ppro_3467 Ppro_3468 Ppro_3469 Ppro_3491
            DVU: DVUA0011(nifK) DVUA0012(nifD) DVUA0015(nifH)
            DVL: Dvul_3090 Dvul_3093 Dvul_3094 Dvul_3096 Dvul_3097
            AFW: Anae109_3027 Anae109_3028 Anae109_3029 Anae109_3030
            SFU: Sfum_1012 Sfum_1013 Sfum_1015 Sfum_1016 Sfum_1019
            MLO: mlr5905 mlr5906 mlr5907
            SME: SMa0825(nifH) SMa0827(nifD) SMa0829(nifK)
            SMD: Smed_6181 Smed_6222 Smed_6223 Smed_6224 Smed_6225
            RET: RHE_PD00200(nifK2) RHE_PD00201(nifD3) RHE_PD00202 RHE_PD00260
                 RHE_PD00306(nifK1) RHE_PD00307(nifD1) RHE_PD00308
            RLE: pRL100160(nifK) pRL100161(nifD) pRL100162(nifH)
            BJA: blr1743(nifD) blr1744(nifK) blr1769(nifH)
            BRA: BRADO1618(bchX) BRADO1639(bchN) BRADO1640(bchB)
                 BRADO1642(bchL) BRADO5394(nifH) BRADO5436(nifN)
                 BRADO5437(nifE) BRADO5438(nifK) BRADO5439(nifD)
                 BRADO5440(nifH)
            BBT: BBta_5879(nifH) BBta_5921(nifN) BBta_5922(nifE)
                 BBta_5923(nifK) BBta_5924(nifD) BBta_5925(nifH)
                 BBta_6414(bchL) BBta_6416(bchB) BBta_6417(bchN)
                 BBta_6437(bchX)
            RPA: RPA1376(vnfH) RPA1378(vnfD) RPA1380(vnfK) RPA1435(anfK)
                 RPA1437(anfD) RPA1438(anfH) RPA2348 RPA2353(nifH1)
                 RPA2363(nifD1) RPA2615(nifH2) RPA2635(nifH3) RPA2636(nifD2)
                 RPA4618(nifK) RPA4619(nifD) RPA4620(nifH4)
            RPB: RPB_0969 RPB_0970 RPB_0971 RPB_4001
            RPC: RPC_1293 RPC_4460 RPC_4461 RPC_4462 RPC_4463 RPC_4681
                 RPC_4682 RPC_4683 RPC_4684
            RPD: RPD_1073 RPD_1074 RPD_1075 RPD_1076 RPD_1077 RPD_3756
            RPE: RPE_1327 RPE_3188 RPE_3190 RPE_3881 RPE_3882 RPE_3883
                 RPE_3884 RPE_4529 RPE_4530 RPE_4531 RPE_4532 RPE_4533
            XAU: Xaut_0088 Xaut_0089 Xaut_0090 Xaut_0091 Xaut_0092 Xaut_0143
            RSP: RSP_0262(bchX) RSP_0539(nifK) RSP_0540(nifD) RSP_0541(nifH)
            RSH: Rsph17029_1906 Rsph17029_1929 Rsph17029_1931 Rsph17029_2189
                 Rsph17029_2190 Rsph17029_2191 Rsph17029_2192
            RSQ: Rsph17025_0772 Rsph17025_0774 Rsph17025_1007 Rsph17025_1009
                 Rsph17025_1246 Rsph17025_1247 Rsph17025_1248 Rsph17025_1249
                 Rsph17025_1250 Rsph17025_2036
            JAN: Jann_0158 Jann_0179
            RDE: RD1_0111(bchX)
            ZMO: ZMO1823(nifH) ZMO1824(nifD) ZMO1825(nifK) ZMO1826(nifE)
                 ZMO1827(nifN) ZMO1828(nifX)
            RRU: Rru_A0772 Rru_A0773 Rru_A0793 Rru_A0794 Rru_A0795 Rru_A1010
                 Rru_A1011 Rru_A1012 Rru_A1392 Rru_A1393 Rru_A1394 Rru_A1395
                 Rru_A2285 Rru_A2286 Rru_A2980
            MAG: amb1572 amb1573 amb1574
            MGM: Mmc1_1194 Mmc1_1195 Mmc1_1200 Mmc1_1201 Mmc1_1202
            CAC: CAC0253(nifH) CAC0256(nifD) CAC0257(nifK)
            CTH: Cthe_1565 Cthe_1566 Cthe_1573
            CBO: CBO0690(nifH)
            CBA: CLB_0729(nifH)
            CBH: CLC_0744(nifH)
            CBF: CLI_0759(nifH)
            CBE: Cbei_0612 Cbei_0613 Cbei_0620 Cbei_0621 Cbei_0623 Cbei_0631
                 Cbei_0632 Cbei_1999 Cbei_2002 Cbei_2003 Cbei_2004 Cbei_2005
            CKL: CKL_0370(anfD) CKL_0371(anfG) CKL_0372(anfK) CKL_0825(nifD1)
                 CKL_0826(nifK1) CKL_1033(nifH1) CKL_1034(nifD2)
                 CKL_1035(nifK2) CKL_1042(nifD3) CKL_1043(nifD4)
                 CKL_1044(nifK3) CKL_1045(nifH2) CKL_1046(nifD5)
                 CKL_1047(nifD6) CKL_1048(nifK4) CKL_1745(vnfK) CKL_1746(vnfG)
                 CKL_1747(vnfD) CKL_1748(vnfH) CKL_2461(nifH3) CKL_2780(nifD7)
                 CKL_2781(nifD8) CKL_2784(nifK5) CKL_2785(nifk6)
                 CKL_2786(nifD9) CKL_3077(nifK7) CKL_3078(nifD10)
                 CKL_3081(nifH4) CKL_3671 CKL_3672
            AMT: Amet_3518 Amet_3519 Amet_3520 Amet_3521 Amet_3524
            DSY: DSY3569 DSY4009 DSY4010 DSY4011 DSY4269 DSY4270 DSY4271(nifH)
            DRM: Dred_2815 Dred_2816 Dred_2817 Dred_2818 Dred_2821
            SWO: Swol_0408
            CSC: Csac_2461 Csac_2462 Csac_2463 Csac_2466
            MTA: Moth_0551
            FRA: Francci3_4485(nifE) Francci3_4486 Francci3_4487 Francci3_4488
            FAL: FRAAL6809(nifN) FRAAL6810(nifE) FRAAL6811(nifK)
                 FRAAL6812(nifD) FRAAL6813(nifH)
            FNU: FN0303
            SYF: Synpcc7942_1419
            CYA: CYA_1821(nifK) CYA_1823(nifD) CYA_1824(nifH)
            CYB: CYB_0421(nifH) CYB_0422(nifD) CYB_0423(nifK)
            ANA: all1440(nifK) all1454(nifD) all1455(nifH) alr0874(nifH2)
            AVA: Ava_2332 Ava_3466 Ava_3916 Ava_3917 Ava_3930 Ava_3932
                 Ava_3933 Ava_4026 Ava_4027 Ava_4028 Ava_4029 Ava_4046 Ava_4051
                 Ava_4054 Ava_4247 Ava_4248 Ava_4249 Ava_4251 Ava_4478
            PMN: PMN2A_1872
            PMB: A9601_05991(chlL)
            PMC: P9515_06071(chlL)
            PMF: P9303_07931(chlL)
            PMG: P9301_05691(chlL)
            PME: NATL1_05971(chlL)
            TER: Tery_4136 Tery_4137 Tery_4138 Tery_4139
            CTE: CT1423(bchX) CT1533(nifH) CT1536(nifD) CT1537(nifK)
            CCH: Cag_0324 Cag_0400 Cag_1244 Cag_1247 Cag_1248 Cag_1249(nifE)
                 Cag_1250 Cag_1716 Cag_1813 Cag_1814
            CPH: Cpha266_0738 Cpha266_0740 Cpha266_0741 Cpha266_0744
                 Cpha266_1792 Cpha266_2386
            PVI: Cvib_0283 Cvib_1241 Cvib_1343 Cvib_1346 Cvib_1347 Cvib_1348
                 Cvib_1349
            PLT: Plut_0217 Plut_1423 Plut_1528 Plut_1531 Plut_1532
                 Plut_1533(nifE) Plut_1534
            DET: DET1154(nifK) DET1155(nifD) DET1158(nifH)
            RRS: RoseRS_1198 RoseRS_1199 RoseRS_1201 RoseRS_1908 RoseRS_3260
            RCA: Rcas_1538 Rcas_3746 Rcas_4040 Rcas_4041 Rcas_4043
            MJA: MJ0879(nifH)
            MMP: MMP0147 MMP0853(nifH) MMP0856(nifD) MMP0857(nifK)
                 MMP0858(nifE) MMP0859(nifN) MMP0860(nifX)
            MMQ: MmarC5_0658 MmarC5_0661 MmarC5_0662 MmarC5_0663 MmarC5_0664
                 MmarC5_1528
            MMZ: MmarC7_0098 MmarC7_0101 MmarC7_0102 MmarC7_0103 MmarC7_0104
                 MmarC7_1147
            MAE: Maeo_0506 Maeo_0508 Maeo_1224 Maeo_1426 Maeo_1427 Maeo_1430
                 Maeo_1431 Maeo_1434
            MVN: Mevan_0059 Mevan_0060 Mevan_0061 Mevan_0062 Mevan_0065
                 Mevan_1152
            MAC: MA1205(anfH) MA1208(anfK) MA1210(anfD) MA1213(vnfH)
                 MA1216(vnfD) MA1218(vnfK) MA1633(nifH) MA3627(nifH)
                 MA3895(nifH) MA3898(nifD) MA3899(nifK)
            MBA: Mbar_A0167 Mbar_A0168 Mbar_A0171 Mbar_A0347(iroN) Mbar_A1551
                 Mbar_A1553 Mbar_A2276 Mbar_A2278 Mbar_A2281(iroN)
            MMA: MM_0514(nifH2) MM_0719 MM_0722 MM_0723
            MBU: Mbur_1038
            MTP: Mthe_1178
            MHU: Mhun_0793
            MEM: Memar_1937
            MBN: Mboo_1142 Mboo_1145 Mboo_1146 Mboo_1147 Mboo_1148 Mboo_1997
                 Mboo_1998 Mboo_2003 Mboo_2004 Mboo_2008 Mboo_2009 Mboo_2010
                 Mboo_2083
            MTH: MTH1560(NifH) MTH1563(NifD) MTH1564 MTH1566 MTH643
            MST: Msp_1120(nifH)
            MSI: Msm_1707
            MKA: MK1416(nifH)
            RCI: RCIX1606(nifH-1) RCIX1611(nifD) RCIX1613(nifK)
                 RCIX2002(nifH-2)
STRUCTURES  PDB: 1CP2  1DE0  1FP4  1FP6  1G1M  1G20  1G21  1G5P  1H1L  1L5H  
                 1M1N  1M1Y  1M34  1N2C  1QGU  1QH1  1QH8  1RW4  1XCP  1XD8  
                 1XD9  1XDB  2AFH  2AFI  2AFK  2C8V  2MIN  2NIP  3MIN  
DBLINKS     IUBMB Enzyme Nomenclature: 1.18.6.1
            ExPASy - ENZYME nomenclature database: 1.18.6.1
            ExplorEnz - The Enzyme Database: 1.18.6.1
            ERGO genome analysis and discovery system: 1.18.6.1
            UM-BBD (Biocatalysis/Biodegradation Database): 1.18.6.1
            BRENDA, the Enzyme Database: 1.18.6.1
            CAS: 9013-04-1
///
ENTRY       EC 1.18.96.1      Obsolete  Enzyme
NAME        Transferred to 1.15.1.2
CLASS       Oxidoreductases;
            Acting on iron-sulfur proteins as donors;
            With other, known, acceptors (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.15.1.2 superoxide reductase (EC
            1.18.96.1 created 2001, deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 1.18.96.1
            ExPASy - ENZYME nomenclature database: 1.18.96.1
            ExplorEnz - The Enzyme Database: 1.18.96.1
            ERGO genome analysis and discovery system: 1.18.96.1
            BRENDA, the Enzyme Database: 1.18.96.1
///
ENTRY       EC 1.18.99.1      Obsolete  Enzyme
NAME        Transferred to 1.12.7.2
CLASS       Oxidoreductases;
            Acting on iron-sulfur proteins as donors;
            With H+ as acceptor (deleted sub-subclass)
COMMENT     Transferred entry: now EC 1.12.7.2 ferredoxin hydrogenase (EC
            1.18.99.1 created 1961 as EC 1.98.1.1, transferred 1965 to EC
            1.12.1.1, transferred 1972 to EC 1.12.7.1, transferred 1978 to EC
            1.18.3.1, transferred 1984 to EC 1.18.99.1, deleted 2002)
STRUCTURES  PDB: 1C4A  1C4C  1CC1  1FEH  1FRF  1GX7  1H2A  1HFE  2FRV  
DBLINKS     IUBMB Enzyme Nomenclature: 1.18.99.1
            ExPASy - ENZYME nomenclature database: 1.18.99.1
            ExplorEnz - The Enzyme Database: 1.18.99.1
            ERGO genome analysis and discovery system: 1.18.99.1
            BRENDA, the Enzyme Database: 1.18.99.1
///
ENTRY       EC 1.18.-.-                 Enzyme
CLASS       Oxidoreductases;
            Acting on iron-sulfur proteins as donors
REACTION    Protochlorophyllide + ATP <=> Chlorophyllide + ADP + Orthophosphate
            [RN:R06282]
SUBSTRATE   Protochlorophyllide [CPD:C02880];
            ATP [CPD:C00002]
PRODUCT     Chlorophyllide [CPD:C02139];
            ADP [CPD:C00008];
            Orthophosphate [CPD:C00009]
///
ENTRY       EC 1.19.6.1                 Enzyme
NAME        nitrogenase (flavodoxin)
CLASS       Oxidoreductases;
            Acting on reduced flavodoxin as donor;
            With dinitrogen as acceptor
SYSNAME     reduced flavodoxin:dinitrogen oxidoreductase (ATP-hydrolysing)
REACTION    6 reduced flavodoxin + 6 H+ + N2 + n ATP = 6 oxidized flavodoxin + 2
            NH3 + n ADP + n phosphate [RN:R05186]
ALL_REAC    R05186
SUBSTRATE   reduced flavodoxin [CPD:C02745];
            H+ [CPD:C00080];
            N2 [CPD:C00697];
            ATP [CPD:C00002]
PRODUCT     oxidized flavodoxin [CPD:C02869];
            NH3 [CPD:C00014];
            ADP [CPD:C00008];
            phosphate [CPD:C00009]
COFACTOR    Molybdenum [CPD:C00150];
            Iron-sulfur [CPD:C00824]
COMMENT     The enzyme is a complex of two proteins containing iron-sulfur
            centres and molybdenum.
REFERENCE   1  [PMID:164247]
  AUTHORS   Zumft WG, Mortenson LE.
  TITLE     The nitrogen-fixing complex of bacteria.
  JOURNAL   Biochim. Biophys. Acta. 416 (1975) 1-52.
  ORGANISM  Azotobacter vinelandii, Azotobacter chroococcum, Klebsiella
            pneumoniae, Bacillus polymyxa, Clostridium pasteurianum, Glycine max
            [GN:egma]
PATHWAY     PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00536  nitrogenase (flavodoxin)
GENES       HSO: HS_1210(fldA)
            BCZ: BCZK1264(fldA) BCZK3250
            BTK: BT9727_3300
            AFU: AF2332
DBLINKS     IUBMB Enzyme Nomenclature: 1.19.6.1
            ExPASy - ENZYME nomenclature database: 1.19.6.1
            ExplorEnz - The Enzyme Database: 1.19.6.1
            ERGO genome analysis and discovery system: 1.19.6.1
            BRENDA, the Enzyme Database: 1.19.6.1
            CAS: 9013-04-1
///
ENTRY       EC 1.20.1.1                 Enzyme
NAME        phosphonate dehydrogenase;
            NAD:phosphite oxidoreductase;
            phosphite dehydrogenase
CLASS       Oxidoreductases;
            Acting on phosphorus or arsenic in donors;
            With NAD+ or NADP+ as acceptor
SYSNAME     phosphonate:NAD+ oxidoreductase
REACTION    phosphonate + NAD+ + H2O = phosphate + NADH + H+ [RN:R05746]
ALL_REAC    R05746
SUBSTRATE   phosphonate [CPD:C06701];
            NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     phosphate [CPD:C00009];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
COMMENT     NADP+ is a poor substitute for NAD+ in the enzyme from Pseudomonas
            stutzeri WM88.
REFERENCE   1  [PMID:11278981]
  AUTHORS   Costas AM, White AK, Metcalf WW.
  TITLE     Purification and characterization of a novel phosphorus-oxidizing
            enzyme from Pseudomonas stutzeri WM88.
  JOURNAL   J. Biol. Chem. 276 (2001) 17429-36.
  ORGANISM  Pseudomonas stutzeri
REFERENCE   2  [PMID:11456941]
  AUTHORS   Vrtis JM, White AK, Metcalf WW, van der Donk WA.
  TITLE     Phosphite dehydrogenase: an unusual phosphoryl transfer reaction.
  JOURNAL   J. Am. Chem. Soc. 123 (2001) 2672-3.
  ORGANISM  Pseudomonas stutzeri
GENES       BVI: Bcep1808_7212
            HAR: HEAR3214(ptxD)
DBLINKS     IUBMB Enzyme Nomenclature: 1.20.1.1
            ExPASy - ENZYME nomenclature database: 1.20.1.1
            ExplorEnz - The Enzyme Database: 1.20.1.1
            ERGO genome analysis and discovery system: 1.20.1.1
            UM-BBD (Biocatalysis/Biodegradation Database): 1.20.1.1
            BRENDA, the Enzyme Database: 1.20.1.1
///
ENTRY       EC 1.20.4.1                 Enzyme
NAME        arsenate reductase (glutaredoxin)
CLASS       Oxidoreductases;
            Acting on phosphorus or arsenic in donors;
            With disulfide as acceptor
SYSNAME     glutharedoxin:arsenate oxidoreductase
REACTION    arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H2O
            [RN:R05747]
ALL_REAC    R05747
SUBSTRATE   arsenate [CPD:C11215];
            glutaredoxin [CPD:C07292]
PRODUCT     arsenite [CPD:C06697];
            glutaredoxin disulfide [CPD:C07293];
            H2O [CPD:C00001]
COMMENT     A molybdoenzyme. The glutaredoxins catalyse glutathione-disulfide
            oxidoreductions and have a redox-active disulfide/dithiol in the
            active site (-Cys-Pro-Tyr-Cys-) that forms a disulfide bond in the
            oxidized form [2, 10]. Glutaredoxins have a binding site for
            glutathione, which is required to reduce them to the dithiol form
            [3, 6]. Thioredoxins reduced by NADPH and thioredoxin reductase can
            act as alternative substrates. The enzyme [1, 4, 7, 9] is part of a
            system for detoxifying arsenate. Although the arsenite formed is
            more toxic than arsenate, it can be extruded from some bacteria by
            EC 3.6.3.16, arsenite-transporting ATPase; in other organisms,
            arsenite can be methylated by EC 2.1.1.137, arsenite
            methyltransferase, in a pathway to non-toxic organoarsenical
            compounds.
REFERENCE   1  [PMID:8969183]
  AUTHORS   Gladysheva T, Liu J, Rosen BP.
  TITLE     His-8 lowers the pKa of the essential Cys-12 residue of the ArsC
            arsenate reductase of plasmid R773.
  JOURNAL   J. Biol. Chem. 271 (1996) 33256-60.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:8003492]
  AUTHORS   Gladysheva TB, Oden KL, Rosen BP.
  TITLE     Properties of the arsenate reductase of plasmid R773.
  JOURNAL   Biochemistry. 33 (1994) 7288-93.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:7476363]
  AUTHORS   Holmgren A, Aslund F.
  TITLE     Glutaredoxin.
  JOURNAL   Methods. Enzymol. 252 (1995) 283-92.
REFERENCE   4
  AUTHORS   Ji, G.Y., Garber, E.A.E., Armes, L.G., Chen, C.M., Fuchs, J.A. and
            Silver, S.
  TITLE     Arsenate reductase of Staphylococcus aureus plasmid PI258.
  JOURNAL   Biochemistry 33 (1994) 7294-7299.
REFERENCE   5  [PMID:9738904]
  AUTHORS   Krafft T, Macy JM.
  TITLE     Purification and characterization of the respiratory arsenate
            reductase of Chrysiogenes arsenatis.
  JOURNAL   Eur. J. Biochem. 255 (1998) 647-53.
  ORGANISM  Chrysiogenes arsenatis
REFERENCE   6  [PMID:7788290]
  AUTHORS   Martin JL.
  TITLE     Thioredoxin--a fold for all reasons.
  JOURNAL   Structure. 3 (1995) 245-50.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   7  [PMID:10606519]
  AUTHORS   Messens J, Hayburn G, Desmyter A, Laus G, Wyns L.
  TITLE     The essential catalytic redox couple in arsenate reductase from
            Staphylococcus aureus.
  JOURNAL   Biochemistry. 38 (1999) 16857-65.
  ORGANISM  Staphylococcus aureus
REFERENCE   8  [PMID:10649963]
  AUTHORS   Radabaugh TR, Aposhian HV.
  TITLE     Enzymatic reduction of arsenic compounds in mammalian systems:
            reduction of arsenate to arsenite by human liver arsenate reductase.
  JOURNAL   Chem. Res. Toxicol. 13 (2000) 26-30.
  ORGANISM  human [GN:hsa]
REFERENCE   9  [PMID:9537360]
  AUTHORS   Sato T, Kobayashi Y.
  TITLE     The ars operon in the skin element of Bacillus subtilis confers
            resistance to arsenate and arsenite.
  JOURNAL   J. Bacteriol. 180 (1998) 1655-61.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   10 [PMID:10593884]
  AUTHORS   Shi J, Vlamis-Gardikas A, Aslund F, Holmgren A, Rosen BP.
  TITLE     Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows
            that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed
            arsenate reduction.
  JOURNAL   J. Biol. Chem. 274 (1999) 36039-42.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K00537  arsenate reductase
            KO: K03741  arsenate reductase
GENES       AFM: AFUA_1G16090 AFUA_5G15000
            ECO: b3503(arsC)
            ECJ: JW3470(arsC)
            ECE: Z4905(arsC)
            ECS: ECs4375
            ECC: c4301(arsC)
            ECI: UTI89_C4021(arsC) UTI89_C4152(grxC)
            ECP: ECP_3592
            ECV: APECO1_2952(arsC)
            ECW: EcE24377A_3986(arsC)
            ECX: EcHS_A2629 EcHS_A3705
            YPI: YpsIP31758_1238(arsC)
            YEN: YE3364(arsC) YE3475(arsC2)
            SFL: SF3536(arsC)
            SFX: S4234(arsC)
            SFV: SFV_3515(arsC)
            SSN: SSON_3738(arsC)
            SBO: SBO_3501(arsC)
            SDY: SDY_3559(arsC)
            ECA: ECA1603(arsC)
            SGL: SG0250 SG2069
            ENT: Ent638_4257
            SPE: Spro_2389
            HIN: HI0236(arsC)
            HIT: NTHI0343(arsC)
            HDU: HD0631(arsC)
            HSO: HS_1002(arsC)
            PMU: PM1944
            MSU: MS1959(arsC)
            APL: APL_1089(arsC)
            XCC: XCC0686(arsC)
            XCB: XC_3548
            XCV: XCV3637(arsC)
            XAC: XAC3512(arsC)
            XOO: XOO1074(arsC)
            XOM: XOO_0974(XOO0974)
            PPR: PBPRA2903(arsC)
            PAE: PA0950
            PAU: PA14_51980
            PAP: PSPA7_4559(arsC1)
            PPU: PP_1645(arsC-1)
            PST: PSPTO_1687(arsC)
            PSB: Psyr_3702
            PSP: PSPPH_3723(arsC)
            PFL: PFL_4456(arsC)
            PFO: Pfl_4228
            PEN: PSEEN1354
            PAR: Psyc_0953
            PCR: Pcryo_1465
            SON: SO_2871
            SDN: Sden_1646
            SFR: Sfri_1754
            SHE: Shewmr4_2348
            SHM: Shewmr7_2420
            SHN: Shewana3_1648 Shewana3_2345
            ILO: IL1465
            CPS: CPS_3191(arsC)
            PHA: PSHAa1133
            LPN: lpg0248
            MCA: MCA2520(arsC)
            FTU: FTT0532c(nrdB) FTT0824(arsC1) FTT1527c(arsC2)
            FTF: FTF0532c(grxC) FTF0824(arsC1) FTF1527c(arsC2)
            FTW: FTW_1010
            FTL: FTL_0316 FTL_0587 FTL_0984
            FTH: FTH_0316(arsC1) FTH_0587(arsC2) FTH_0963
            FTN: FTN_0339 FTN_0983 FTN_1435
            TCX: Tcr_1207
            NOC: Noc_0186
            HCH: HCH_01858(arsC)
            CSA: Csal_1896
            ABO: ABO_1544(arsC) ABO_2679(arsC-3)
            AHA: AHA_1678(arsC-1) AHA_1727(arsC-2)
            VOK: COSY_0305(arsC) COSY_0666
            NME: NMB0005
            NMA: NMA0252
            CVI: CV_0770 CV_2036
            RSO: RSc3271(RS02500) RSp1128(arsC)
            REU: Reut_A1525 Reut_A3271
            REH: H16_A2068(arsC1) H16_A3585(arsC2)
            RME: Rmet_0329 Rmet_3436
            BMA: BMAA0558(arsC) BMAA2113
            BMV: BMASAVP1_1142
            BML: BMA10299_0913(arsC) BMA10299_1421
            BMN: BMA10247_A1882(arsC) BMA10247_A2408
            BXE: Bxe_B0302 Bxe_B3030
            BUR: Bcep18194_B0006 Bcep18194_C6562 Bcep18194_C6564
            BCN: Bcen_5167
            BCH: Bcen2424_5692
            BPS: BPSS1432 BPSS2348
            BPM: BURPS1710b_A0456(arsC) BURPS1710b_A1502(arsC)
            BPL: BURPS1106A_A1942(arsC) BURPS1106A_A3174(arsC)
            BPD: BURPS668_A2037(arsC) BURPS668_A3287(arsC)
            BTE: BTH_II0959 BTH_II2370(arsC)
            BPE: BP1306(arsC) BP1681(arsC)
            BPA: BPP2716(arsC) BPP2912(arsC)
            BBR: BB2782(arsC) BB2882(arsC)
            POL: Bpro_2219
            MPT: Mpe_A2343(arsC2)
            HAR: HEAR0500(arsC) HEAR0502(arsC) HEAR1960(arsCb) HEAR1963(arsCa)
                 HEAR3207(arsC) HEAR3302(arsC)
            MMS: mma_3429
            NEU: NE1678(yfgD)
            AZO: azo1658 azo2067 azo2351(arsC1) azo2353(arsC2)
            TBD: Tbd_1425
            WSU: WS0753(arsC) WS0760
            TDN: Tmden_0314
            CJR: CJE1732(arsC)
            CJU: C8J_1458(arsC)
            ABU: Abu_1384 Abu_1935(arsC)
            SUN: SUN_1478
            GSU: GSU2953(arsC)
            GME: Gmet_0521
            PCA: Pcar_1772
            PPD: Ppro_0842
            DVU: DVU1646(arsC)
            DVL: Dvul_1440
            DDE: Dde_2792 Dde_2793 Dde_2820
            DPS: DP1879
            SFU: Sfum_3601
            AMA: AM1083(grxC1)
            MLO: mll2167
            MES: Meso_0324 Meso_4201
            SME: SMc02649(arsC)
            ATU: Atu1490(arsC)
            ATC: AGR_C_2748
            RET: RHE_CH02532(ypch00851) RHE_CH02534(arsC)
            RLE: RL0615 RL2884(arsC1) RL2887(arsC2)
            BME: BMEI0992
            BMF: BAB1_1008
            BMS: BR0989
            BMB: BruAb1_0995
            BOV: BOV_0957(arsC)
            BJA: bll3084(arsC)
            BRA: BRADO4444(arsC) BRADO5106
            BBT: BBta_4662(arsC) BBta_5577
            RPA: RPA2257(arsC1) RPA3554(arsC2)
            RPB: RPB_1971
            RPC: RPC_0617
            RPD: RPD_3418
            RPE: RPE_3658
            NWI: Nwi_1913 Nwi_3124 Nwi_3125
            NHA: Nham_2244 Nham_4429
            CCR: CC_1503
            SIL: SPO2908(arsC-1)
            SIT: TM1040_2798
            RSP: RSP_3127(arsC)
            JAN: Jann_2102 Jann_2964
            RDE: RD1_1071(arsC) RD1_2397(arsC)
            MMR: Mmar10_2883
            HNE: HNE_0991(arsC) HNE_3533
            NAR: Saro_3279
            SAL: Sala_1826 Sala_2404 Sala_2539
            ELI: ELI_00390
            GBE: GbCGDNIH1_0188
            RRU: Rru_A1450 Rru_A1992
            MAG: amb1831
            MGM: Mmc1_0286
            BSU: BG11304(arsC)
            BHA: BH2998(arsC)
            BAN: BA3196(arsC)
            BAR: GBAA3196(arsC)
            BAA: BA_3707
            BAT: BAS2971
            BCE: BC3152
            BCA: BCE_3207(arsC) BCE_A0158(arsC)
            BCZ: BCZK2898(arsC) BCZK3109(spxA)
            BTK: BT9727_2963(arsC)
            BTL: BALH_2854(arsC) BALH_3060 BALH_4524(arsC)
            BLI: BL01871(arsC)
            BLD: BLi02122(arsC)
            BCL: ABC0837(arsC)
            BPU: BPUM_2939
            OIH: OB2423
            GKA: GK0589 GK3222
            SAU: SAP018(arsC)
            SAR: SAR0692(arsC)
            SAC: SACOL1824(arsC)
            SAB: SAB1632
            SAA: SAUSA300_1719(arsC)
            SAO: SAOUHSC_01894
            SEP: SE0134
            SER: SERP0209(arsC-1) SERP2431(arsC-2)
            SHA: SH0101(arsC) SH0108(arsC)
            SSP: SSP1633 SSPP114
            LLA: L11493(arsC)
            LLC: LACR_1707
            LLM: llmg_0902(arsC)
            SPY: SPy_0891(arsC)
            SPZ: M5005_Spy_0697(arsC)
            SPM: spyM18_0952(arsC)
            SPG: SpyM3_0610(arsC)
            SPS: SPs1243
            SPH: MGAS10270_Spy0755(arsC)
            SPI: MGAS10750_Spy0789(arsC)
            SPJ: MGAS2096_Spy0769(arsC)
            SPK: MGAS9429_Spy0753(arsC)
            SPA: M6_Spy0714
            SPB: M28_Spy0677(arsC)
            SAG: SAG1181(arsC)
            SAN: gbs1254
            SAK: SAK_1268(arsC)
            LPL: lp_0059(arsC)
            LJO: LJ0232
            LSL: LSL_0608(arsC) LSL_0888(arsC) LSL_1330(arsC)
            LBR: LVIS_0887
            LCA: LSEI_2761
            CPF: CPF_0834(arsC)
            CPR: CPR_0827(arsC)
            CBO: CBO0751(arsC)
            CBA: CLB_0793
            CBH: CLC_0808
            CBF: CLI_0832
            CKL: CKL_2533(arsC)
            DSY: DSY4147 DSY4671
            TTE: TTE1001(wzb)
            MTU: Rv2643
            MTC: MT2720
            MBO: Mb2676(arsC)
            MPA: MAP0982c(arsC)
            MAV: MAV_1155(arsC)
            MSM: MSMEG_5428(arsC)
            MMC: Mmcs_4250
            CGL: NCgl1049(cgl1094)
            CGB: cg1244
            CEF: CE1150
            CDI: DIP0965(arsC)
            CJK: jk2004(arsC)
            NFA: nfa24500 nfa24510
            RHA: RHA1_ro03369 RHA1_ro05655
            AAU: AAur_3630(arsC) AAur_pTC20058(arsC) AAur_pTC20061(arsC)
                 AAur_pTC20062(arsC)
            FAL: FRAAL3366
            SEN: SACE_5142 SACE_5143
            RXY: Rxyl_2878
            RBA: RB11147(arsC) RB11157(arsC)
            CYB: CYB_2366(arsC)
            GVI: glr0004
            AVA: Ava_3712
            PMB: A9601_01971(grxC) A9601_05691(arsC)
            PMC: P9515_02081(grxC) P9515_05761(arsC)
            PMF: P9303_07481(arsC) P9303_27371(grxC)
            PMG: P9301_01991(grxC) P9301_05391(arsC)
            PME: NATL1_02541(grxC)
            BTH: BT_0115
            CHU: CHU_1588(arsC)
            GFO: GFO_1803(arsC)
            FPS: FP0352 FP1599 FP1603
            CTE: CT1725(arsC)
            CCH: Cag_0397
            DET: DET0143(arsC)
            DEH: cbdb_A168(arsC)
            DRA: DR_A0123
            DGE: Dgeo_2548 Dgeo_2770
            TTH: TTC1502
            TTJ: TTHA1853
            AAE: aq_685(arsC)
            MAC: MA3103(arsC)
            MTH: MTH1355
            HWA: HQ3170A(arsC) HQ3636A(arsC)
            NPH: NP6092A(arsC)
            PFU: PF0553
            TKO: TK0843
STRUCTURES  PDB: 1RXE  1RXI  1S3C  1S3D  1SD8  1SD9  1SJZ  1SK0  1SK1  1SK2  
                 1Z2D  1Z2E  
DBLINKS     IUBMB Enzyme Nomenclature: 1.20.4.1
            ExPASy - ENZYME nomenclature database: 1.20.4.1
            ExplorEnz - The Enzyme Database: 1.20.4.1
            ERGO genome analysis and discovery system: 1.20.4.1
            UM-BBD (Biocatalysis/Biodegradation Database): 1.20.4.1
            BRENDA, the Enzyme Database: 1.20.4.1
///
ENTRY       EC 1.20.4.2                 Enzyme
NAME        methylarsonate reductase;
            MMA(V) reductase
CLASS       Oxidoreductases;
            Acting on phosphorus or arsenic in donors;
            With disulfide as acceptor
SYSNAME     gluthathione:methylarsonate oxidoreductase
REACTION    methylarsonate + 2 glutathione = methylarsonite + glutathione
            disulfide + H2O [RN:R05748]
ALL_REAC    R05748
SUBSTRATE   methylarsonate [CPD:C07294];
            glutathione [CPD:C00051]
PRODUCT     methylarsonite [CPD:C07295];
            glutathione disulfide [CPD:C00127];
            H2O [CPD:C00001]
COMMENT     The product, Me-As(OH)2 (methylarsonous acid), is biologically
            methylated by EC 2.1.1.137, arsenite methyltransferase, to form
            cacodylic acid (dimethylarsinic acid).
REFERENCE   1  [PMID:10604879]
  AUTHORS   Zakharyan RA, Aposhian HV.
  TITLE     Enzymatic reduction of arsenic compounds in mammalian systems: the
            rate-limiting enzyme of rabbit liver arsenic biotransformation is
            MMA(V) reductase.
  JOURNAL   Chem. Res. Toxicol. 12 (1999) 1278-83.
  ORGANISM  rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 1.20.4.2
            ExPASy - ENZYME nomenclature database: 1.20.4.2
            ExplorEnz - The Enzyme Database: 1.20.4.2
            ERGO genome analysis and discovery system: 1.20.4.2
            UM-BBD (Biocatalysis/Biodegradation Database): 1.20.4.2
            BRENDA, the Enzyme Database: 1.20.4.2
///
ENTRY       EC 1.20.98.1                Enzyme
NAME        arsenate reductase (azurin);
            arsenite oxidase
CLASS       Oxidoreductases;
            Acting on phosphorus or arsenic in donors;
            With other, known, acceptors
SYSNAME     arsenite:azurin oxidoreductase
REACTION    arsenite + H2O + 2 azurinox = arsenate + 2 azurinred + 2 H+
            [RN:R05751]
ALL_REAC    R05751
SUBSTRATE   arsenite [CPD:C06697];
            H2O [CPD:C00001];
            azurinox
PRODUCT     arsenate [CPD:C11215];
            azurinred;
            H+ [CPD:C00080]
COMMENT     Contains a molybdopterin centre comprising two molybdopterin
            guanosine dinucleotide cofactors bound to molybdenum, a [3Fe-4S]
            cluster and a Rieske-type [2Fe-2S] cluster. Also uses a c-type
            cytochrome or O2 as acceptors.
REFERENCE   1  [PMID:1331097]
  AUTHORS   Anderson GL, Williams J, Hille R.
  TITLE     The purification and characterization of arsenite oxidase from
            Alcaligenes faecalis, a molybdenum-containing hydroxylase.
  JOURNAL   J. Biol. Chem. 267 (1992) 23674-82.
  ORGANISM  Alcaligenes faecalis
REFERENCE   2  [PMID:11250197]
  AUTHORS   Ellis PJ, Conrads T, Hille R, Kuhn P.
  TITLE     Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes
            faecalis in two crystal forms at 1.64 A and 2.03 A.
  JOURNAL   Structure. (Camb). 9 (2001) 125-32.
  ORGANISM  Alcaligenes faecalis
ORTHOLOGY   KO: K08355  arsenite oxidase small subunit
            KO: K08356  arsenite oxidase large subunit
GENES       RFR: Rfer_3084 Rfer_3085
            HAR: HEAR0478(aoxB) HEAR0479(aoxA)
            NHA: Nham_4426 Nham_4427
            XAU: Xaut_3950
            TTJ: TTHB127 TTHB128
            APE: APE_2563
DBLINKS     IUBMB Enzyme Nomenclature: 1.20.98.1
            ExPASy - ENZYME nomenclature database: 1.20.98.1
            ExplorEnz - The Enzyme Database: 1.20.98.1
            ERGO genome analysis and discovery system: 1.20.98.1
            UM-BBD (Biocatalysis/Biodegradation Database): 1.20.98.1
            BRENDA, the Enzyme Database: 1.20.98.1
///
ENTRY       EC 1.20.99.1                Enzyme
NAME        arsenate reductase (donor);
            arsenate:(acceptor) oxidoreductase
CLASS       Oxidoreductases;
            Acting on phosphorus or arsenic in donors;
            With other acceptors
SYSNAME     arsenate:acceptor oxidoreductase
REACTION    arsenite + acceptor = arsenate + reduced acceptor [RN:R05752]
ALL_REAC    R05752
SUBSTRATE   arsenite [CPD:C06697];
            acceptor [CPD:C00028]
PRODUCT     arsenate [CPD:C11215];
            reduced acceptor [CPD:C00030]
COMMENT     Benzyl viologen can act as an acceptor. Unlike EC 1.20.4.1, arsenate
            reductase (glutaredoxin), reduced glutaredoxin cannot serve as a
            reductant.
REFERENCE   1  [PMID:9738904]
  AUTHORS   Krafft T, Macy JM.
  TITLE     Purification and characterization of the respiratory arsenate
            reductase of Chrysiogenes arsenatis.
  JOURNAL   Eur. J. Biochem. 255 (1998) 647-53.
  ORGANISM  Chrysiogenes arsenatis
REFERENCE   2  [PMID:10649963]
  AUTHORS   Radabaugh TR, Aposhian HV.
  TITLE     Enzymatic reduction of arsenic compounds in mammalian systems:
            reduction of arsenate to arsenite by human liver arsenate reductase.
  JOURNAL   Chem. Res. Toxicol. 13 (2000) 26-30.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 1.20.99.1
            ExPASy - ENZYME nomenclature database: 1.20.99.1
            ExplorEnz - The Enzyme Database: 1.20.99.1
            ERGO genome analysis and discovery system: 1.20.99.1
            BRENDA, the Enzyme Database: 1.20.99.1
///
ENTRY       EC 1.21.3.1                 Enzyme
NAME        isopenicillin-N synthase;
            isopenicillin N synthetase
CLASS       Oxidoreductases;
            Acting on X-H and Y-H to form an X-Y bond;
            With oxygen as acceptor
SYSNAME     N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine:oxygen
            oxidoreductase (cyclizing)
REACTION    N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 =
            isopenicillin N + 2 H2O
ALL_REAC    (other) R04872
SUBSTRATE   N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine;
            O2 [CPD:C00007]
PRODUCT     isopenicillin N [CPD:C05557];
            H2O [CPD:C00001]
COMMENT     Forms part of the penicillin biosynthesis pathway (for pathway,
            click here).
REFERENCE   1  [PMID:1588566]
  AUTHORS   Huffman GW, Gesellchen PD, Turner JR, Rothenberger RB, Osborne HE,
            Miller FD, Chapman JL, Queener SW.
  TITLE     Substrate specificity of isopenicillin N synthase.
  JOURNAL   J. Med. Chem. 35 (1992) 1897-914.
  ORGANISM  Penicillium chrysogenum, Cephalosporium acremonium
REFERENCE   2  [PMID:7791906]
  AUTHORS   Roach PL, Clifton IJ, Fulop V, Harlos K, Barton GJ, Hajdu J,
            Andersson I, Schofield CJ, Baldwin JE.
  TITLE     Crystal structure of isopenicillin N synthase is the first from a
            new structural family of enzymes.
  JOURNAL   Nature. 375 (1995) 700-4.
PATHWAY     PATH: map00311  Penicillin and cephalosporin biosynthesis
ORTHOLOGY   KO: K04126  isopenicillin-N synthase
GENES       VVU: VV2_0260
            VVY: VVA0764
            VPA: VPA0866
            VFI: VF1657
            PPR: PBPRB0800
            ACI: ACIAD2388
            SON: SO_2589
            SDN: Sden_2305
            SHN: Shewana3_2394
            CPS: CPS_1982
            PHA: PSHAa1932
            PAT: Patl_0531
            AHA: AHA_3601
            CVI: CV_0045
            MXA: MXAN_0088
            AVA: Ava_5009
STRUCTURES  PDB: 1ODM  1UZW  1W03  1W04  1W05  1W06  1W3V  1W3X  2BJS  2BU9  
                 2IVI  2IVJ  
DBLINKS     IUBMB Enzyme Nomenclature: 1.21.3.1
            ExPASy - ENZYME nomenclature database: 1.21.3.1
            ExplorEnz - The Enzyme Database: 1.21.3.1
            ERGO genome analysis and discovery system: 1.21.3.1
            BRENDA, the Enzyme Database: 1.21.3.1
///
ENTRY       EC 1.21.3.2                 Enzyme
NAME        columbamine oxidase;
            berberine synthase
CLASS       Oxidoreductases;
            Acting on X-H and Y-H to form an X-Y bond;
            With oxygen as acceptor
SYSNAME     columbamine:oxygen oxidoreductase (cyclizing)
REACTION    2 columbamine + O2 = 2 berberine + 2 H2O [RN:R00044]
ALL_REAC    R00044
SUBSTRATE   columbamine [CPD:C01795];
            O2 [CPD:C00007]
PRODUCT     berberine [CPD:C00757];
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023]
COMMENT     An iron protein. Oxidation of the O-methoxyphenol structure forms
            the methylenedioxy group of berberine.
REFERENCE   1
  AUTHORS   Rueffer, M. and Zenk, M.H.
  TITLE     Berberine synthesis, the methylenedioxy group forming enzyme in
            berberine synthesis.
  JOURNAL   Tetrahedron Lett. 26 (1985) 201-202.
  ORGANISM  Berberis stolonifera
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 1.21.3.2
            ExPASy - ENZYME nomenclature database: 1.21.3.2
            ExplorEnz - The Enzyme Database: 1.21.3.2
            ERGO genome analysis and discovery system: 1.21.3.2
            BRENDA, the Enzyme Database: 1.21.3.2
            CAS: 95329-18-3
///
ENTRY       EC 1.21.3.3                 Enzyme
NAME        reticuline oxidase;
            BBE;
            berberine bridge enzyme;
            berberine-bridge-forming enzyme;
            tetrahydroprotoberberine synthase
CLASS       Oxidoreductases;
            Acting on X-H and Y-H to form an X-Y bond;
            With oxygen as acceptor
SYSNAME     (S)-reticuline:oxygen oxidoreductase (methylene-bridge-forming)
REACTION    (S)-reticuline + O2 = (S)-scoulerine + H2O2 [RN:R03831]
ALL_REAC    R03831
SUBSTRATE   (S)-reticuline [CPD:C02105];
            O2 [CPD:C00007]
PRODUCT     (S)-scoulerine [CPD:C02106];
            H2O2 [CPD:C00027]
COMMENT     The product of the reaction, (S)-scoulerine, is a precursor of
            protopine, protoberberine and benzophenanthridine alkaloid
            biosynthesis in plants. Acts on (S)-reticuline and related
            compounds, converting the N-methyl group into the methylene bridge
            ('berberine bridge') of (S)-tetrahydroprotoberberines.
REFERENCE   1
  AUTHORS   Steffens, P., Nagakura, N. and Zenk, M.H.
  TITLE     The berberine bridge forming enzyme in tetrahydroprotoberberine
            biosynthesis.
  JOURNAL   Tetrahedron Lett. 25 (1984) 951-952.
  ORGANISM  Macleaya microcarpa
REFERENCE   2  [PMID:1946465]
  AUTHORS   Dittrich H, Kutchan TM.
  TITLE     Molecular cloning, expression, and induction of berberine bridge
            enzyme, an enzyme essential to the formation of benzophenanthridine
            alkaloids in the response of plants to pathogenic attack.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 9969-73.
  ORGANISM  Eschscholzia californica
REFERENCE   3  [PMID:7592663]
  AUTHORS   Kutchan TM, Dittrich H.
  TITLE     Characterization and mechanism of the berberine bridge enzyme, a
            covalently flavinylated oxidase of benzophenanthridine alkaloid
            biosynthesis in plants.
  JOURNAL   J. Biol. Chem. 270 (1995) 24475-81.
  ORGANISM  Eschscholzia californica
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
ORTHOLOGY   KO: K00307  reticuline oxidase
DBLINKS     IUBMB Enzyme Nomenclature: 1.21.3.3
            ExPASy - ENZYME nomenclature database: 1.21.3.3
            ExplorEnz - The Enzyme Database: 1.21.3.3
            ERGO genome analysis and discovery system: 1.21.3.3
            BRENDA, the Enzyme Database: 1.21.3.3
            CAS: 152232-28-5
///
ENTRY       EC 1.21.3.4                 Enzyme
NAME        sulochrin oxidase [(+)-bisdechlorogeodin-forming];
            sulochrin oxidase
CLASS       Oxidoreductases;
            Acting on X-H and Y-H to form an X-Y bond;
            With oxygen as acceptor
SYSNAME     sulochrin:oxygen oxidoreductase (cyclizing, (+)-specific)
REACTION    2 sulochrin + O2 = 2 (+)-bisdechlorogeodin + 2 H2O [RN:R00060]
ALL_REAC    R00060
SUBSTRATE   sulochrin [CPD:C00495];
            O2 [CPD:C00007]
PRODUCT     (+)-bisdechlorogeodin [CPD:C03036];
            H2O [CPD:C00001]
COMMENT     Also acts on several diphenols and phenylenediamines, but has low
            affinity for these substrates. Involved in the biosynthesis of mould
            metabolites related to the antibiotic griseofulvin.
REFERENCE   1  [PMID:7049104]
  AUTHORS   Nordlov H, Gatenbeck S.
  TITLE     Enzymatic synthesis of (+)- and (-)-bisdechlorogeodin with sulochrin
            oxidase from Penicillium frequentans and Oospora sulphurea-ochracea.
  JOURNAL   Arch. Microbiol. 131 (1982) 208-11.
  ORGANISM  Penicillium frequentans
DBLINKS     IUBMB Enzyme Nomenclature: 1.21.3.4
            ExPASy - ENZYME nomenclature database: 1.21.3.4
            ExplorEnz - The Enzyme Database: 1.21.3.4
            ERGO genome analysis and discovery system: 1.21.3.4
            BRENDA, the Enzyme Database: 1.21.3.4
            CAS: 82469-87-2
///
ENTRY       EC 1.21.3.5                 Enzyme
NAME        sulochrin oxidase [(-)-bisdechlorogeodin-forming];
            sulochrin oxidase
CLASS       Oxidoreductases;
            Acting on X-H and Y-H to form an X-Y bond;
            With oxygen as acceptor
SYSNAME     sulochrin:oxygen oxidoreductase (cyclizing, (-)-specific)
REACTION    2 sulochrin + O2 = 2 (-)-bisdechlorogeodin + 2 H2O [RN:R00061]
ALL_REAC    R00061
SUBSTRATE   sulochrin [CPD:C00495];
            O2 [CPD:C00007]
PRODUCT     (-)-bisdechlorogeodin [CPD:C03040];
            H2O [CPD:C00001]
COMMENT     Also acts on several diphenols and phenylenediamines, but has low
            affinity for these substrates. Involved in the biosynthesis of mould
            metabolites related to the antibiotic griseofulvin.
REFERENCE   1  [PMID:7049104]
  AUTHORS   Nordlov H, Gatenbeck S.
  TITLE     Enzymatic synthesis of (+)- and (-)-bisdechlorogeodin with sulochrin
            oxidase from Penicillium frequentans and Oospora sulphurea-ochracea.
  JOURNAL   Arch. Microbiol. 131 (1982) 208-11.
  ORGANISM  Oospora sulphurea-ochracea
DBLINKS     IUBMB Enzyme Nomenclature: 1.21.3.5
            ExPASy - ENZYME nomenclature database: 1.21.3.5
            ExplorEnz - The Enzyme Database: 1.21.3.5
            ERGO genome analysis and discovery system: 1.21.3.5
            BRENDA, the Enzyme Database: 1.21.3.5
            CAS: 82469-87-2
///
ENTRY       EC 1.21.3.6                 Enzyme
NAME        aureusidin synthase
CLASS       Oxidoreductases;
            Acting on X-H and Y-H to form an X-Y bond;
            With oxygen as acceptor
SYSNAME     2',4,4',6'-tetrahydroxychalcone:oxygen oxidoreductase
REACTION    (1) 2',4,4',6'-tetrahydroxychalcone + O2 = aureusidin + H2O
            [RN:R07224];
            (2) 2',3,4,4',6'-pentahydroxychalcone + 0.5 O2 = aureusidin + H2O
            [RN:R07225]
ALL_REAC    R07224 R07225
SUBSTRATE   2',4,4',6'-tetrahydroxychalcone;
            O2 [CPD:C00007];
            2',3,4,4',6'-pentahydroxychalcone [CPD:C15525]
PRODUCT     aureusidin [CPD:C08576];
            H2O [CPD:C00001]
COMMENT     A copper-containing glycoprotein that plays a key role in the yellow
            coloration of flowers such as snapdragon. The enzyme is a homologue
            of plant polyphenol oxidase [1] and catalyses two separate chemical
            transformations, i.e. 3-hydroxylation and oxidative cyclization
            (2',alpha-dehydrogenation). H2O2 activates reaction (1) but inhibits
            reaction (2).
REFERENCE   1  [PMID:11073455]
  AUTHORS   Nakayama T, Yonekura-Sakakibara K, Sato T, Kikuchi S, Fukui Y,
            Fukuchi-Mizutani M, Ueda T, Nakao M, Tanaka Y, Kusumi T, Nishino T.
  TITLE     Aureusidin synthase: a polyphenol oxidase homolog responsible for
            flower coloration.
  JOURNAL   Science. 290 (2000) 1163-6.
  ORGANISM  Antirrhinum majus
REFERENCE   2  [PMID:11418122]
  AUTHORS   Nakayama T, Sato T, Fukui Y, Yonekura-Sakakibara K, Hayashi H,
            Tanaka Y, Kusumi T, Nishino T.
  TITLE     Specificity analysis and mechanism of aurone synthesis catalyzed by
            aureusidin synthase, a polyphenol oxidase homolog responsible for
            flower coloration.
  JOURNAL   FEBS. Lett. 499 (2001) 107-11.
  ORGANISM  Antirrhinum majus
REFERENCE   3  [PMID:11164594]
  AUTHORS   Sato T, Nakayama T, Kikuchi S, Fukui Y, Yonekura-Sakakibara K, Ueda
            T, Nishino T, Tanaka Y, Kusumi T.
  TITLE     Enzymatic formation of aurones in the extracts of yellow snapdragon
            flowers.
  JOURNAL   Plant. Sci. 160 (2001) 229-236.
  ORGANISM  Antirrhinum majus
DBLINKS     IUBMB Enzyme Nomenclature: 1.21.3.6
            ExPASy - ENZYME nomenclature database: 1.21.3.6
            ExplorEnz - The Enzyme Database: 1.21.3.6
            ERGO genome analysis and discovery system: 1.21.3.6
            BRENDA, the Enzyme Database: 1.21.3.6
            CAS: 320784-48-3
///
ENTRY       EC 1.21.4.1                 Enzyme
NAME        D-proline reductase (dithiol)
CLASS       Oxidoreductases;
            Acting on X-H and Y-H to form an X-Y bond;
            With a disulfide as acceptor
SYSNAME     5-aminopentanoate:lipoate oxidoreductase (cyclizing)
REACTION    5-aminopentanoate + lipoate = D-proline + dihydrolipoate [RN:R02825]
ALL_REAC    R02825
SUBSTRATE   5-aminopentanoate [CPD:C00431];
            lipoate [CPD:C00725]
PRODUCT     D-proline [CPD:C00763];
            dihydrolipoate [CPD:C02147]
COFACTOR    Pyruvate [CPD:C00022]
COMMENT     The reaction is observed only in the direction of D-proline
            reduction. Other dithiols can function as reducing agents; the
            enzyme contains a pyruvoyl group and a selenocysteine residue, both
            essential for activity.
REFERENCE   1  [PMID:5778643]
  AUTHORS   Hodgins DS, Abeles RH.
  TITLE     Studies of the mechanism of action of D-proline reductase: the
            presence on covalently bound pyruvate and its role in the catalytic
            process.
  JOURNAL   Arch. Biochem. Biophys. 130 (1969) 274-85.
  ORGANISM  Clostridium sticklandii
REFERENCE   2
  AUTHORS   Stadtman, T.C. and Elliott, P.
  TITLE     Studies on the enzymic reduction of amino acids. II. Purification
            and properties of a D-proline reductase and a proline racemase from
            Clostridium sticklandii.
  JOURNAL   J. Biol. Chem. 228 (1957) 983-997.
  ORGANISM  Clostridium sticklandii
REFERENCE   3  [PMID:10085076]
  AUTHORS   Kabisch UC, Grantzdorffer A, Schierhorn A, Rucknagel KP, Andreesen
            JR, Pich A.
  TITLE     Identification of D-proline reductase from Clostridium sticklandii
            as a selenoenzyme and indications for a catalytically active
            pyruvoyl group derived from a cysteine residue by cleavage of a
            proprotein.
  JOURNAL   J. Biol. Chem. 274 (1999) 8445-54.
  ORGANISM  Clostridium sticklandii
PATHWAY     PATH: map00330  Arginine and proline metabolism
GENES       CBA: CLB_2347(prdB) CLB_2349(prdA)
            CBH: CLC_2329(prdB) CLC_2331(prdA)
            CBF: CLI_2522(prdA) CLI_2537(prdB-1) CLI_3800(prdB-2)
            AMT: Amet_0665 Amet_0667 Amet_0669 Amet_0670
DBLINKS     IUBMB Enzyme Nomenclature: 1.21.4.1
            ExPASy - ENZYME nomenclature database: 1.21.4.1
            ExplorEnz - The Enzyme Database: 1.21.4.1
            ERGO genome analysis and discovery system: 1.21.4.1
            BRENDA, the Enzyme Database: 1.21.4.1
            CAS: 37255-43-9
///
ENTRY       EC 1.21.4.2                 Enzyme
NAME        glycine reductase
CLASS       Oxidoreductases;
            Acting on X-H and Y-H to form an X-Y bond;
            With a disulfide as acceptor
SYSNAME     acetyl-phosphate ammonia:thioredoxin disulfide oxidoreductase
            (glycine-forming)
REACTION    acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine +
            phosphate + thioredoxin [RN:R07226]
ALL_REAC    R07226
SUBSTRATE   acetyl phosphate [CPD:C00227];
            NH3 [CPD:C00014];
            thioredoxin disulfide [CPD:C00343];
            H2O [CPD:C00001]
PRODUCT     glycine [CPD:C00037];
            phosphate [CPD:C00009];
            thioredoxin [CPD:C00342]
COMMENT     The reaction is observed only in the direction of glycine reduction.
            The enzyme from Eubacterium acidaminophilum consists of subunits A,
            B and C. Subunit B contains selenocysteine and a pyruvoyl group, and
            is responsible for glycine binding and ammonia release. Subunit A,
            which also contains selenocysteine, is reduced by thioredoxin, and
            is needed to convert the carboxymethyl group into a ketene
            equivalent, in turn used by subunit C to produce acetyl phosphate.
            Only subunit B distinguishes this enzyme from EC 1.21.4.3 (sarcosine
            reductase) and EC 1.21.4.4 (betaine reductase).
REFERENCE   1  [PMID:10091582]
  AUTHORS   Wagner M, Sonntag D, Grimm R, Pich A, Eckerskorn C, Sohling B,
            Andreesen JR.
  TITLE     Substrate-specific selenoprotein B of glycine reductase from
            Eubacterium acidaminophilum. Biochemical and molecular analysis.
  JOURNAL   Eur. J. Biochem. 260 (1999) 38-49.
  ORGANISM  Eubacterium acidaminophilum
REFERENCE   2  [PMID:11422384]
  AUTHORS   Bednarski B, Andreesen JR, Pich A.
  TITLE     In vitro processing of the proproteins GrdE of protein B of glycine
            reductase and PrdA of D-proline reductase from Clostridium
            sticklandii: formation of a pyruvoyl group from a cysteine residue.
  JOURNAL   Eur. J. Biochem. 268 (2001) 3538-44.
  ORGANISM  Clostridium sticklandii
GENES       PPR: PBPRB1543 PBPRB1544(grdE) PBPRB1546 PBPRB1547
            STH: STH2867 STH2869 STH2870(grdE)
            CDF: CD2348(grdD) CD2349(grdC) CD2351(grdB) CD2352(grdA)
                 CD2354(grdE)
            CBO: CBO1257(grdB) CBO1261(grdA) CBO1263(grdC) CBO1264(grdD)
            CBA: CLB_1284(grdE) CLB_1285(grdB) CLB_1290(grdA) CLB_1291(grdC)
                 CLB_1292(grdD)
            CBH: CLC_1296(grdE) CLC_1301(grdC) CLC_1302(grdD)
            CBF: CLI_1342(grdE) CLI_1343(grdB) CLI_1346(grdA) CLI_1347(grdC)
                 CLI_1348(grdD)
            AMT: Amet_3589 Amet_3591 Amet_3592
            CHY: CHY_2391(grdE) CHY_2392(grdA) CHY_2393(grdB)
            TTE: TTE1874(plsX2) TTE1875(fabH4) TTE1879
            TDE: TDE0239(grdD) TDE0240(grdC) TDE0745(grdA) TDE2119(grdB-2)
                 TDE2120(grdE-2)
DBLINKS     IUBMB Enzyme Nomenclature: 1.21.4.2
            ExPASy - ENZYME nomenclature database: 1.21.4.2
            ExplorEnz - The Enzyme Database: 1.21.4.2
            ERGO genome analysis and discovery system: 1.21.4.2
            BRENDA, the Enzyme Database: 1.21.4.2
///
ENTRY       EC 1.21.4.3                 Enzyme
NAME        sarcosine reductase
CLASS       Oxidoreductases;
            Acting on X-H and Y-H to form an X-Y bond;
            With a disulfide as acceptor
SYSNAME     acetyl-phosphate methylamine:thioredoxin disulfide oxidoreductase
            (N-methylglycine-forming)
REACTION    acetyl phosphate + methylamine + thioredoxin disulfide =
            N-methylglycine + phosphate + thioredoxin [RN:R07227]
ALL_REAC    R07227
SUBSTRATE   acetyl phosphate [CPD:C00227];
            methylamine [CPD:C00218];
            thioredoxin disulfide [CPD:C00343]
PRODUCT     N-methylglycine [CPD:C00213];
            phosphate [CPD:C00009];
            thioredoxin [CPD:C00342]
COMMENT     The reaction is observed only in the direction of sarcosine
            reduction. The enzyme from Eubacterium acidaminophilum consists of
            subunits A, B and C. Subunit B contains selenocysteine and a
            pyruvoyl group, and is responsible for sarcosine binding and
            methylamine release. Subunit A, which also contains selenocysteine,
            is reduced by thioredoxin, and is needed to convert the
            carboxymethyl group into a ketene equivalent, in turn used by
            subunit C to produce acetyl phosphate. Only subunit B distinguishes
            this enzyme from EC 1.21.4.2 (glycine reductase) and EC 1.21.4.4
            (betaine reductase).
REFERENCE   1  [PMID:10091582]
  AUTHORS   Wagner M, Sonntag D, Grimm R, Pich A, Eckerskorn C, Sohling B,
            Andreesen JR.
  TITLE     Substrate-specific selenoprotein B of glycine reductase from
            Eubacterium acidaminophilum. Biochemical and molecular analysis.
  JOURNAL   Eur. J. Biochem. 260 (1999) 38-49.
  ORGANISM  Eubacterium acidaminophilum
REFERENCE   2
  AUTHORS   Hormann, K. and Andreesen, J.R.
  TITLE     Reductive cleavage of sarcosine and betaine by Eubacterium
            acidaminophilum via enzyme systems different from glycine reductase.
  JOURNAL   Arch. Microbiol. 153 (1989) 50-59.
  ORGANISM  Eubacterium acidaminophilum
GENES       PPR: PBPRB1546 PBPRB1547
            STH: STH2869
            CDF: CD1740(grdG) CD1741(grdF)
            AMT: Amet_3593
            CHY: CHY_2392(grdA)
            TTE: TTE1874(plsX2) TTE1875(fabH4)
            TDE: TDE0239(grdD) TDE0240(grdC) TDE0745(grdA)
DBLINKS     IUBMB Enzyme Nomenclature: 1.21.4.3
            ExPASy - ENZYME nomenclature database: 1.21.4.3
            ExplorEnz - The Enzyme Database: 1.21.4.3
            ERGO genome analysis and discovery system: 1.21.4.3
            BRENDA, the Enzyme Database: 1.21.4.3
///
ENTRY       EC 1.21.4.4                 Enzyme
NAME        betaine reductase
CLASS       Oxidoreductases;
            Acting on X-H and Y-H to form an X-Y bond;
            With a disulfide as acceptor
SYSNAME     acetyl-phosphate trimethylamine:thioredoxin disulfide oxidoreductase
            (N,N,N-trimethylglycine-forming)
REACTION    acetyl phosphate + trimethylamine + thioredoxin disulfide =
            N,N,N-trimethylglycine + phosphate + thioredoxin [RN:R07228]
ALL_REAC    R07228
SUBSTRATE   acetyl phosphate [CPD:C00227];
            trimethylamine [CPD:C00565];
            thioredoxin disulfide [CPD:C00343]
PRODUCT     N,N,N-trimethylglycine [CPD:C00719];
            phosphate [CPD:C00009];
            thioredoxin [CPD:C00342]
COMMENT     The reaction is observed only in the direction of betaine reduction.
            The enzyme from Eubacterium acidaminophilum consists of subunits A,
            B and C. Subunit B contains selenocysteine and a pyruvoyl group, and
            is responsible for betaine binding and trimethylamine release.
            Subunit A, which also contains selenocysteine, is reduced by
            thioredoxin, and is needed to convert the carboxymethyl group into a
            ketene equivalent, in turn used by subunit C to produce acetyl
            phosphate. Only subunit B distinguishes this enzyme from EC 1.21.4.2
            (glycine reductase) and EC 1.21.4.3 (sarcosine reductase).
REFERENCE   1  [PMID:10091582]
  AUTHORS   Wagner M, Sonntag D, Grimm R, Pich A, Eckerskorn C, Sohling B,
            Andreesen JR.
  TITLE     Substrate-specific selenoprotein B of glycine reductase from
            Eubacterium acidaminophilum. Biochemical and molecular analysis.
  JOURNAL   Eur. J. Biochem. 260 (1999) 38-49.
  ORGANISM  Eubacterium acidaminophilum
REFERENCE   2  [PMID:11422384]
  AUTHORS   Bednarski B, Andreesen JR, Pich A.
  TITLE     In vitro processing of the proproteins GrdE of protein B of glycine
            reductase and PrdA of D-proline reductase from Clostridium
            sticklandii: formation of a pyruvoyl group from a cysteine residue.
  JOURNAL   Eur. J. Biochem. 268 (2001) 3538-44.
  ORGANISM  Clostridium sticklandii
GENES       PPR: PBPRB1546 PBPRB1547
            STH: STH2869
            AMT: Amet_3590
            CHY: CHY_2392(grdA)
            TTE: TTE1874(plsX2) TTE1875(fabH4)
            TDE: TDE0239(grdD) TDE0240(grdC) TDE0745(grdA)
DBLINKS     IUBMB Enzyme Nomenclature: 1.21.4.4
            ExPASy - ENZYME nomenclature database: 1.21.4.4
            ExplorEnz - The Enzyme Database: 1.21.4.4
            ERGO genome analysis and discovery system: 1.21.4.4
            BRENDA, the Enzyme Database: 1.21.4.4
///
ENTRY       EC 1.21.99.1                Enzyme
NAME        beta-cyclopiazonate dehydrogenase;
            beta-cyclopiazonate oxidocyclase;
            beta-cyclopiazonic oxidocyclase;
            beta-cyclopiazonate:(acceptor) oxidoreductase (cyclizing)
CLASS       Oxidoreductases;
            Acting on X-H and Y-H to form an X-Y bond;
            With other acceptors
SYSNAME     beta-cyclopiazonate:acceptor oxidoreductase (cyclizing)
REACTION    beta-cyclopiazonate + acceptor = alpha-cyclopiazonate + reduced
            acceptor [RN:R04080]
ALL_REAC    R04080
SUBSTRATE   beta-cyclopiazonate [CPD:C02899];
            acceptor [CPD:C00028]
PRODUCT     alpha-cyclopiazonate [CPD:C03032];
            reduced acceptor [CPD:C00030]
COFACTOR    FAD [CPD:C00016]
COMMENT     A flavoprotein (FAD). Cytochrome c and various dyes can act as
            acceptor. Cyclopiazonate is a microbial toxin.
REFERENCE   1  [PMID:8076]
  AUTHORS   Edmondson DE, Kenney WC, Singer TP.
  TITLE     Structural elucidation and properties of
            8alpha-(N1-histidyl)riboflavin: the flavin component of thiamine
            dehydrogenase and beta-cyclopiazonate oxidocyclase.
  JOURNAL   Biochemistry. 15 (1976) 2937-45.
REFERENCE   2  [PMID:5143340]
  AUTHORS   Schabort JC, Potgeiter DJ.
  TITLE     -cyclopiazonate oxidocyclase from Penicillium cyclopium. II. Studies
            on electron acceptors, inhibitors, enzyme kinetics, amino acid
            composition, flavin prosthetic group and other properties.
  JOURNAL   Biochim. Biophys. Acta. 250 (1971) 329-45.
  ORGANISM  Penicillium cyclopium
DBLINKS     IUBMB Enzyme Nomenclature: 1.21.99.1
            ExPASy - ENZYME nomenclature database: 1.21.99.1
            ExplorEnz - The Enzyme Database: 1.21.99.1
            ERGO genome analysis and discovery system: 1.21.99.1
            BRENDA, the Enzyme Database: 1.21.99.1
            CAS: 9059-00-1
///
ENTRY       EC 1.97.1.1                 Enzyme
NAME        chlorate reductase;
            chlorate reductase C
CLASS       Oxidoreductases;
            Other oxidoreductases;
            Sole sub-subclass for oxidoreductases that do not belong in the
            other subclasses
SYSNAME     chlorite:acceptor oxidoreductase
REACTION    AH2 + chlorate = A + H2O + chlorite [RN:R03575]
ALL_REAC    R03575
SUBSTRATE   AH2 [CPD:C00030];
            chlorate [CPD:C01485]
PRODUCT     A [CPD:C00028];
            H2O [CPD:C00001];
            chlorite [CPD:C01486]
COMMENT     Flavins or benzylviologen can act as acceptor.
REFERENCE   1  [PMID:4940765]
  AUTHORS   Azoulay E, Mutaftschiev S, Martins Rosado de Sousa.
  TITLE     [Study of chlorate-resistant mutants in Escherichia coli K 12. 3.
            Chlorate-reductase c of mutants chl. C-]
  JOURNAL   Biochim. Biophys. Acta. 237 (1971) 579-90.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 1.97.1.1
            ExPASy - ENZYME nomenclature database: 1.97.1.1
            ExplorEnz - The Enzyme Database: 1.97.1.1
            ERGO genome analysis and discovery system: 1.97.1.1
            UM-BBD (Biocatalysis/Biodegradation Database): 1.97.1.1
            BRENDA, the Enzyme Database: 1.97.1.1
            CAS: 60382-73-2
///
ENTRY       EC 1.97.1.2                 Enzyme
NAME        pyrogallol hydroxytransferase;
            1,2,3,5-tetrahydroxybenzene hydroxyltransferase;
            1,2,3,5-tetrahydroxybenzene:pyrogallol transhydroxylase;
            1,2,3,5-tetrahydroxybenzene-pyrogallol hydroxyltransferase
            (transhydroxylase);
            pyrogallol hydroxyltransferase;
            1,2,3,5-tetrahydroxybenzene:1,2,3-trihydroxybenzene
            hydroxyltransferase
CLASS       Oxidoreductases;
            Other oxidoreductases;
            Sole sub-subclass for oxidoreductases that do not belong in the
            other subclasses
SYSNAME     1,2,3,5-tetrahydroxybenzene:1,2,3-trihydroxybenzene
            hydroxytransferase
REACTION    1,2,3,5-tetrahydroxybenzene + 1,2,3-trihydroxybenzene =
            1,3,5-trihydroxybenzene + 1,2,3,5-tetrahydroxybenzene [RN:R04297]
ALL_REAC    R04297
SUBSTRATE   1,2,3,5-tetrahydroxybenzene [CPD:C03743];
            1,2,3-trihydroxybenzene [CPD:C01108]
PRODUCT     1,3,5-trihydroxybenzene [CPD:C02183];
            1,2,3,5-tetrahydroxybenzene [CPD:C03743]
COMMENT     1,2,3,5-Tetrahydroxybenzene acts as a co-substrate for the
            conversion of pyrogallol into phloroglucinol, and for a number of
            similar isomerizations. The enzyme is provisionally listed here, but
            might be considered as the basis for a new class in the
            transferases, analogous to the aminotransferases.
REFERENCE   1  [PMID:2298693]
  AUTHORS   Brune A, Schink B.
  TITLE     Pyrogallol-to-phloroglucinol conversion and other hydroxyl-transfer
            reactions catalyzed by cell extracts of Pelobacter acidigallici.
  JOURNAL   J. Bacteriol. 172 (1990) 1070-6.
  ORGANISM  Pelobacter acidigallici
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
STRUCTURES  PDB: 1TI2  1TI4  1TI6  1VLD  1VLE  1VLF  
DBLINKS     IUBMB Enzyme Nomenclature: 1.97.1.2
            ExPASy - ENZYME nomenclature database: 1.97.1.2
            ExplorEnz - The Enzyme Database: 1.97.1.2
            ERGO genome analysis and discovery system: 1.97.1.2
            UM-BBD (Biocatalysis/Biodegradation Database): 1.97.1.2
            BRENDA, the Enzyme Database: 1.97.1.2
            CAS: 125978-84-9
///
ENTRY       EC 1.97.1.3                 Enzyme
NAME        sulfur reductase
CLASS       Oxidoreductases;
            Other oxidoreductases;
            Sole sub-subclass for oxidoreductases that do not belong in the
            other subclasses
SYSNAME     (donor):sulfur oxidoreductase
REACTION    reduction of elemental sulfur or polysulfide to hydrogen sulfide
ALL_REAC    (other) R03533
COMMENT     Sulfur can be reduced with hydrogen as donor in the presence of
            hydrogenase, or by photochemical reduction in the presence of
            phenosafranin.
REFERENCE   1
  AUTHORS   Zophel, A., Kennedy, M.C., Beinert, H. and Kroneck, P.M.H.
  TITLE     Investigations on microbial sulfur respiration .1. Activation and
            reduction of elemental sulfur in several strains of Eubacteria.
  JOURNAL   Arch. Microbiol. 150 (1988) 72-77.
  ORGANISM  Desulfovibrio baculatus
DBLINKS     IUBMB Enzyme Nomenclature: 1.97.1.3
            ExPASy - ENZYME nomenclature database: 1.97.1.3
            ExplorEnz - The Enzyme Database: 1.97.1.3
            ERGO genome analysis and discovery system: 1.97.1.3
            BRENDA, the Enzyme Database: 1.97.1.3
            CAS: 101637-43-8
///
ENTRY       EC 1.97.1.4                 Enzyme
NAME        [formate-C-acetyltransferase]-activating enzyme;
            PFL activase;
            PFL-glycine:S-adenosyl-L-methionine H transferase
            (flavodoxin-oxidizing, S-adenosyl-L-methionine-cleaving);
            formate acetyltransferase activating enzyme;
            formate acetyltransferase-glycine
            dihydroflavodoxin:S-adenosyl-L-methionine oxidoreductase
            (S-adenosyl-L-methionine cleaving)
CLASS       Oxidoreductases;
            Other oxidoreductases;
            Sole sub-subclass for oxidoreductases that do not belong in the
            other subclasses
SYSNAME     [formate C-acetyltransferase]-glycine
            dihydroflavodoxin:S-adenosyl-L-methionine oxidoreductase
            (S-adenosyl-L-methionine cleaving)
REACTION    S-adenosyl-L-methionine + dihydroflavodoxin + [formate
            C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine +
            flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl
            radical [RN:R04710]
ALL_REAC    R04710
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            dihydroflavodoxin [CPD:C05196];
            [formate C-acetyltransferase]-glycine [CPD:C05197]
PRODUCT     5'-deoxyadenosine [CPD:C05198];
            L-methionine [CPD:C00073];
            flavodoxin semiquinone [CPD:C05199];
            [formate C-acetyltransferase]-glycin-2-yl radical [CPD:C05312]
COMMENT     An iron-sulfur protein. A single glycine residue in EC 2.3.1.54,
            formate C-acetyltransferase, is oxidized to the corresponding
            radical by transfer of H from its CH2 to AdoMet with concomitant
            cleavage of the latter. The reaction requires Fe2+. The first stage
            is reduction of the AdoMet to give methionine and the
            5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen
            radical from the glycine residue.
REFERENCE   1  [PMID:8175649]
  AUTHORS   Frey M, Rothe M, Wagner AF, Knappe J.
  TITLE     Adenosylmethionine-dependent synthesis of the glycyl radical in
            pyruvate formate-lyase by abstraction of the glycine C-2 pro-S
            hydrogen atom. Studies of [2H]glycine-substituted enzyme and
            peptides homologous to the glycine 734 site.
  JOURNAL   J. Biol. Chem. 269 (1994) 12432-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:1310545]
  AUTHORS   Wagner AF, Frey M, Neugebauer FA, Schafer W, Knappe J.
  TITLE     The free radical in pyruvate formate-lyase is located on
            glycine-734.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 996-1000.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:11395404]
  AUTHORS   Frey PA.
  TITLE     Radical mechanisms of enzymatic catalysis.
  JOURNAL   Annu. Rev. Biochem. 70 (2001) 121-48.
ORTHOLOGY   KO: K00538  formate acetyltransferase activating enzyme
            KO: K04068  anaerobic ribonucleoside-triphosphate reductase
                        activating protein
            KO: K04069  pyruvate formate lyase activating enzyme
            KO: K04070  putative pyruvate formate lyase activating enzyme
GENES       ANI: AN7611.2
            AFM: AFUA_2G15630
            AOR: AO090012000266
            EHI: 76.t00022
            ECO: b0824(ybiY) b0902(pflA) b3952(pflC) b4237(nrdG)
            ECJ: JW0808(ybiY) JW0885(pflA) JW3924(pflC) JW4196(nrdG)
            ECE: Z1047(ybiY) Z1246(pflA) Z5508(pflC) Z5847(nrdG)
            ECS: ECs0902 ECs0985 ECs4881 ECs5214
            ECC: c0909 c1038(pflA) c4538 c4911(pflC) c5336(nrdG)
            ECI: UTI89_C0827 UTI89_C0973(pflA) UTI89_C4543(pflC)
                 UTI89_C4841(nrdG) UTI89_C4963
            ECP: ECP_0837 ECP_0913 ECP_4165 ECP_4486 ECP_4599
            ECV: APECO1_1190(pflA) APECO1_1269(ybiY) APECO1_2155(nrdG)
                 APECO1_2294 APECO1_2515(pflC)
            ECW: EcE24377A_0980(pflA) EcE24377A_4807(nrdG)
            ECX: EcHS_A1008 EcHS_A4490
            STY: STY0883(ybiY) STY0968(pflA) STY4790(nrdG)
            STT: t1964(pflA) t2045(ybiY) t4485(nrdG)
            SPT: SPA1828(pflA) SPA1911(ybiY) SPA4251(nrdG)
            SEC: SC0839(pflE) SC0924(pflA) SC4005(pflC) SC4306(nrdG)
            STM: STM0844(pflE) STM0970(pflA) STM4115(pflC) STM4451(nrdG)
            YPE: YPO1381(pflA) YPO3455(nrdG)
            YPK: y0732(nrdG) y2792(pflA)
            YPM: YP_0630(nrdG2) YP_1212(pflA)
            YPA: YPA_0672 YPA_2957
            YPN: YPN_0633 YPN_2596
            YPP: YPDSF_2314 YPDSF_3265
            YPS: YPTB0518(nrdG) YPTB1406(pflA)
            YPI: YpsIP31758_2591(pflA) YpsIP31758_3557(nrdG)
            YEN: YE0645
            SFL: SF0774(ybiY) SF0897(pflA) SF4029(pflC) SF4253(nrdG)
            SFX: S0817(ybiY) S0961(pflA) S3717(pflC) S4515(nrdG)
            SFV: SFV_0807(ybiY) SFV_0902(pflA) SFV_4021(pflC) SFV_4254(nrdG)
            SSN: SSON_0806(ybiY) SSON_0903(pflA) SSON_4125(pflC)
                 SSON_4418(nrdG)
            SBO: SBO_0714(ybiY) SBO_2188(pflA) SBO_3971(pflC) SBO_4209(nrdG)
            SDY: SDY_0763(ybiY) SDY_2359(pflA) SDY_3787(pflC) SDY_4256(nrdG)
            ECA: ECA0374(nrdG) ECA2597A(pflA) ECA3769
            PLU: plu1612(pflA) plu4500(nrdG)
            SGL: SG0987
            ENT: Ent638_0436 Ent638_1422
            SPE: Spro_1701 Spro_2641
            HIN: HI0179(act) HI1155(nrdG)
            HIT: NTHI0268(pflA) NTHI1324(nrdG)
            HIP: CGSHiEE_02470(pflA)
            HDU: HD0989(pflA)
            HSO: HS_1147(pflA) HS_1467(nrdG)
            PMU: PM0077(act) PM0941(nrdG)
            MSU: MS0403(pflA) MS0632(nrdG)
            APL: APL_1035(pflA)
            ASU: Asuc_0567
            VCH: VC1869 VCA0512
            VCO: VC0395_A1460(pflA)
            VVU: VV1_2095 VV2_0336
            VVY: VV2345 VVA0894
            VPA: VP0992 VPA0940 VPA1568
            VFI: VF1591 VFA0282 VFA0962
            PPR: PBPRA1252 PBPRA2752(pflA) PBPRB0443
            PAE: PA2726
            PAU: PA14_28910
            PFL: PFL_4162
            SON: SO_2833(nrdG) SO_2913(pflA)
            SDN: Sden_1420 Sden_2407
            SFR: Sfri_2442 Sfri_2474
            SAZ: Sama_1276 Sama_1497
            SBL: Sbal_1666 Sbal_2672
            SBM: Shew185_2691
            SLO: Shew_2391 Shew_2448
            SPC: Sputcn32_1541 Sputcn32_2379
            SSE: Ssed_1707
            SPL: Spea_1671
            SHE: Shewmr4_1493 Shewmr4_2440
            SHM: Shewmr7_1560 Shewmr7_2510
            SHN: Shewana3_1554 Shewana3_2602
            SHW: Sputw3181_1630 Sputw3181_2558
            PIN: Ping_0741 Ping_3308
            LPN: lpg1170
            LPF: lpl1178
            LPP: lpp1172
            MCA: MCA0073
            HCH: HCH_05222
            AHA: AHA_1232(nrdG) AHA_1689(pflA) AHA_2855
            DNO: DNO_0911(nrdG) DNO_1333(pflA)
            CVI: CV_1413(pflA) CV_2413(nrdG)
            REU: Reut_C6076
            REH: H16_A1380
            RME: Rmet_5137
            BCH: Bcen2424_6412
            RFR: Rfer_0396
            EBA: c2A302(bssD) ebA6553
            AZO: azo1676(pflA)
            DAR: Daro_1969 Daro_2097
            TBD: Tbd_1585
            TDN: Tmden_1849
            NIS: NIS_1749 NIS_1750
            SUN: SUN_0976 SUN_1453
            GSU: GSU1274 GSU1728 GSU2102
            GME: Gmet_1006 Gmet_1541 Gmet_1772
            PCA: Pcar_0308 Pcar_0943 Pcar_1396 Pcar_2732
            DVU: DVU0300 DVU1404 DVU2271 DVU2825
            DDE: Dde_0278 Dde_1272 Dde_1670 Dde_3054 Dde_3281
            BBA: Bd2592
            DPS: DP0065(pflA) DP1824(pflC) DP3026(pflC)
            ADE: Adeh_0086
            MXA: MXAN_2901
            SAT: SYN_01240 SYN_01999 SYN_03523
            SFU: Sfum_0354 Sfum_1995
            BJA: blr0853(bchE)
            RPC: RPC_1081
            RPE: RPE_3102 RPE_3175
            NHA: Nham_0890
            RSP: RSP_0281(bchE)
            ZMO: ZMO1027(pflA) ZMO1569(pflA)
            RRU: Rru_A0449 Rru_A0916 Rru_A2999
            MAG: amb3680
            MGM: Mmc1_0893
            ABA: Acid345_2948
            BAN: BA0510(pflA)
            BAR: GBAA0510(pflA)
            BAA: BA_1081
            BAT: BAS0482
            BCE: BC0492 BC3602
            BCA: BCE_0564(pflA) BCE_3621(nrdG)
            BCZ: BCZK0421(pflA) BCZK3309(nrdG)
            BCY: Bcer98_0432
            BTK: BT9727_0425(pflA) BT9727_3359(pflA)
            BTL: BALH_0447(pflA)
            BLI: BL01864 BL02467
            BLD: BLi02131 BLi03823 BLi04172
            SAU: SA0219(pflA) SA2409
            SAV: SAV0227(pflA) SAV2616
            SAM: MW0202(pflA) MW2536
            SAR: SAR0218 SAR2694(nrdG)
            SAS: SAS0202 SAS2502
            SAC: SACOL0205(pflA) SACOL2634(nrdG)
            SAB: SAB0165 SAB2490c(nrdG)
            SAA: SAUSA300_0221(pflA) SAUSA300_2550(nrdG)
            SAO: SAOUHSC_00188 SAOUHSC_02941
            SAJ: SaurJH9_0211
            SAH: SaurJH1_0217
            SEP: SE0215 SE2171
            SER: SERP2182(nrdG) SERP2365(pflA)
            SSP: SSP0145
            LMO: lmo0280 lmo1407(pflC)
            LMF: LMOf2365_0300(nrdG) LMOf2365_1426(pflA)
            LIN: lin0306 lin1444(pflC)
            LWE: lwe0254(nrdG) lwe1423(pflC)
            LLA: L63811(pflA) L72609(nrdG)
            LLC: LACR_0278 LACR_1999
            LLM: llmg_0282(nrdG) llmg_1997(pflA)
            SPY: SPy_0379(pflC) SPy_2055 SPy_2105(nrdG)
            SPZ: M5005_Spy_0318(pflC) M5005_Spy_1749 M5005_Spy_1789(nrdG)
            SPM: spyM18_0433 spyM18_2117 spyM18_2164(nrdG)
            SPG: SpyM3_0277(pflC) SpyM3_1755 SpyM3_1791(nrdG)
            SPS: SPs1582 SPs1753 SPs1788
            SPH: MGAS10270_Spy0313(pflC) MGAS10270_Spy1818
                 MGAS10270_Spy1857(nrdG)
            SPI: MGAS10750_Spy0312(pflC) MGAS10750_Spy1843
                 MGAS10750_Spy1881(nrdG)
            SPJ: MGAS2096_Spy0335(pflC) MGAS2096_Spy1783
                 MGAS2096_Spy1822(nrdG)
            SPK: MGAS9429_Spy0317(pflC) MGAS9429_Spy1759
                 MGAS9429_Spy1800(nrdG)
            SPF: SpyM51540(pflC) SpyM51712 SpyM51748(nrdG)
            SPA: M6_Spy0344 M6_Spy1749 M6_Spy1788
            SPB: M28_Spy0307(pflC) M28_Spy1736 M28_Spy1773(nrdG)
            SPN: SP_0205 SP_0245 SP_1976
            SPR: spr0185(nrdG) spr0226(pflE) spr1791(pflC)
            SPD: SPD_0190(nrdG) SPD_1774(pflA)
            SAG: SAG0325(pflA-1) SAG1398(pflA-2) SAG2082(nrdG)
            SAN: gbs0313 gbs1468 gbs2037
            SAK: SAK_0395 SAK_1431(pflA) SAK_2021(nrdG)
            SMU: SMU.1692(pflA) SMU.2071 SMU.490(pflC)
            STC: str1640(pflA) str1966(nrdG)
            STL: stu1640(pflA) stu1966(nrdG)
            SSA: SSA_0277 SSA_1749(pflA) SSA_2226(nrdG)
            SGO: SGO_1649(act) SGO_1794(pflC) SGO_2029(nrdG)
            LPL: lp_2596(pflA1) lp_2931(nrdG) lp_3314(pflA2)
            LJO: LJ0138
            LAC: LBA0161
            LSA: LSA0973(pflA) LSA1458(nrdG)
            LSL: LSL_1331(nrdG) LSL_1872(pflA)
            LDB: Ldb0212(nrdG)
            LBU: LBUL_0186
            LCA: LSEI_1412 LSEI_1742
            LGA: LGAS_0139
            EFA: EF1612(pflA) EF2755(nrdG)
            OOE: OEOE_1115
            STH: STH114
            CAC: CAC0481(nrdG) CAC0981(pflA) CAC1421 CAC3242
            CPE: CPE0994 CPE1154 CPE2503(nrdG)
            CPF: CPF_1251 CPF_1357(pflA) CPF_2826(nrdG)
            CPR: CPR_1063 CPR_1170(pflA) CPR_2512(nrdG)
            CTC: CTC00258 CTC00937 CTC01166 CTC01448
            CNO: NT01CX_0016 NT01CX_0384(pflC) NT01CX_0497(pflC) NT01CX_1001
                 NT01CX_1076 NT01CX_1221(pflC)
            CDF: CD0109(nrdG) CD0758(plfA) CD3283(pflE)
            CBO: CBO0095(nrdG) CBO1002(nrdG) CBO3184 CBO3215(act)
            CBA: CLB_3251(pflA)
            CBH: CLC_3125(pflA)
            CBF: CLI_3353(pflA)
            CBE: Cbei_0316 Cbei_0701 Cbei_1010 Cbei_4060
            CKL: CKL_1106(act)
            AMT: Amet_0507 Amet_0583 Amet_1987 Amet_2210 Amet_3835
            CHY: CHY_0097 CHY_2050(nrdG) CHY_2267
            DSY: DSY0396 DSY0417 DSY1551 DSY3009 DSY5005
            DRM: Dred_0038 Dred_0694
            SWO: Swol_1049 Swol_2272 Swol_2293
            TTE: TTE1779(pflX) TTE1849(pflA) TTE1955(pflA2)
            MTA: Moth_0368 Moth_2294
            MPE: MYPE4970(nrdG)
            MTU: Rv3138(pflA)
            MTC: MT3225
            MBO: Mb3162(pflA)
            MBB: BCG_3161(pflA)
            CEF: CE2362
            CDI: DIP0379
            PAC: PPA2136
            FAL: FRAAL0840
            BLO: BL0950(pflA) BL1726 BL1753(nrdG)
            BAD: BAD_0991(pflA) BAD_1215(nrdG)
            FNU: FN0261 FN0312
            TDE: TDE2402 TDE2506
            CYA: CYA_0475(pflA) CYA_1294
            CYB: CYB_0243(pflA)
            TEL: tlr0226
            ANA: alr0731
            AVA: Ava_4633
            TER: Tery_4772
            BTH: BT_1999 BT_2956 BT_4737
            BFR: BF1338 BF3693 BF4382
            BFS: BF1322(pflA) BF3485 BF4180
            PGI: PG1259(nrdG)
            CTE: CT2022
            DET: DET1314 DET1368
            DEH: cbdb_A1254 cbdb_A1319
            TTH: TTC1347
            TTJ: TTHA1710
            AAE: aq_1861 aq_729
            TMA: TM0109 TM0384 TM0924 TM1237 TM1552
            MJA: MJ0674 MJ0808 MJ1227(act)
            MMP: MMP0544 MMP0580(act)
            MAC: MA0071 MA2410(pfl) MA3448 MA3482
            MBA: Mbar_A1036 Mbar_A2551 Mbar_A3602
            MMA: MM_1366 MM_1477 MM_2565 MM_2581 MM_2989
            MBU: Mbur_2126 Mbur_2404
            MHU: Mhun_1052 Mhun_3220
            MTH: MTH1069 MTH1395 MTH1586 MTH1643 MTH1784 MTH287 MTH345 MTH976
            MST: Msp_1565
            MSI: Msm_0652 Msm_1284
            MKA: MK0187 MK0286 MK0928(pflX) MK0952 MK1086
            AFU: AF0117(act-1) AF1330(act-3) AF1450(pflC) AF1961(pflX)
                 AF2278(act-4)
            TAC: Ta0248
            TVO: TVN1352
            PTO: PTO0959
            PHO: PH0020 PH1113 PH1391
            PAB: PAB0742(pflX) PAB1859 PAB2338
            PFU: PF0631 PF1049 PF1397 PF1972
            TKO: TK0290 TK0893 TK2299
            RCI: LRC104(pflX) RCIX2253(pflA) RCIX706(nrdG)
            APE: APE_1535.1 APE_1865.1
            SSO: SSO0653
            STO: ST1514
            SAI: Saci_1632
            PAI: PAE2191 PAE2451 PAE3184 PAE3672
            NEQ: NEQ381 NEQ494
DBLINKS     IUBMB Enzyme Nomenclature: 1.97.1.4
            ExPASy - ENZYME nomenclature database: 1.97.1.4
            ExplorEnz - The Enzyme Database: 1.97.1.4
            ERGO genome analysis and discovery system: 1.97.1.4
            BRENDA, the Enzyme Database: 1.97.1.4
            CAS: 206367-15-9
///
ENTRY       EC 1.97.1.5       Obsolete  Enzyme
NAME        Transferred to 1.20.4.1
CLASS       Oxidoreductases;
            Other oxidoreductases;
            Sole sub-subclass for oxidoreductases that do not belong in the
            other subclasses
COMMENT     Transferred entry: now EC 1.20.4.1, arsenate reductase
            (glutaredoxin) (EC 1.97.1.5 created 2000 deleted 2001)
STRUCTURES  PDB: 1LJL  1LJU  1LK0  2CD7  
DBLINKS     IUBMB Enzyme Nomenclature: 1.97.1.5
            ExPASy - ENZYME nomenclature database: 1.97.1.5
            ExplorEnz - The Enzyme Database: 1.97.1.5
            ERGO genome analysis and discovery system: 1.97.1.5
            BRENDA, the Enzyme Database: 1.97.1.5
///
ENTRY       EC 1.97.1.6       Obsolete  Enzyme
NAME        Transferred to 1.20.99.1
CLASS       Oxidoreductases;
            Other oxidoreductases;
            Sole sub-subclass for oxidoreductases that do not belong in the
            other subclasses
COMMENT     Transferred entry: now EC 1.20.99.1, arsenate reductase (donor) (EC
            1.97.1.6 created 2000 deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 1.97.1.6
            ExPASy - ENZYME nomenclature database: 1.97.1.6
            ExplorEnz - The Enzyme Database: 1.97.1.6
            ERGO genome analysis and discovery system: 1.97.1.6
            BRENDA, the Enzyme Database: 1.97.1.6
///
ENTRY       EC 1.97.1.7       Obsolete  Enzyme
NAME        Transferred to 1.20.4.2
CLASS       Oxidoreductases;
            Other oxidoreductases;
            Sole sub-subclass for oxidoreductases that do not belong in the
            other subclasses
COMMENT     Transferred entry: now EC 1.20.4.2 methylarsonate reductase (EC
            1.97.1.7 created 2000, deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 1.97.1.7
            ExPASy - ENZYME nomenclature database: 1.97.1.7
            ExplorEnz - The Enzyme Database: 1.97.1.7
            ERGO genome analysis and discovery system: 1.97.1.7
            BRENDA, the Enzyme Database: 1.97.1.7
///
ENTRY       EC 1.97.1.8                 Enzyme
NAME        tetrachloroethene reductive dehalogenase;
            tetrachloroethene reductase
CLASS       Oxidoreductases;
            Other oxidoreductases;
            Sole sub-subclass for oxidoreductases that do not belong in the
            other subclasses
SYSNAME     acceptor:trichloroethene oxidoreductase (chlorinating)
REACTION    trichloroethene + chloride + acceptor = tetrachloroethene + reduced
            acceptor [RN:R05753]
ALL_REAC    R05753;
            (other) R05499 R05500 R05501
SUBSTRATE   trichloroethene [CPD:C06790];
            chloride [CPD:C00115];
            acceptor [CPD:C00028]
PRODUCT     tetrachloroethene [CPD:C06789];
            reduced acceptor [CPD:C00030]
COMMENT     This enzyme allows the common pollutant tetrachloroethene to support
            bacterial growth and is responsible for disposal of a number of
            chlorinated hydrocarbons by this organism. The reaction occurs in
            the reverse direction. The enzyme also reduces trichloroethene to
            dichloroethene. Although the physiological reductant is unknown, the
            supply of reductant in some organisms is via reduced menaquinone,
            itself formed from molecular hydrogen, via EC 1.12.5.1
            (hydrogen:quinone oxidoreductase). The enzyme contains a corrinoid
            and two iron-sulfur clusters. Methyl viologen can act as electron
            donor.
REFERENCE   1
  AUTHORS   Holliger, C, Wohlfarth, G. and Diekert, G.
  TITLE     Reductive dechlorination in the energy metabolism of anaerobic
            bacteria.
  JOURNAL   FEMS Microbiol. Rev. 22 (1998) 383-398.
REFERENCE   2
  AUTHORS   Glod, G., Angst, W., Holliger, C. and Schwarzenbach, R.P.
  TITLE     Corrinoid-mediated reduction of tetrachloroethene, trichloroethene,
            and trichlorofluoroethene in homogeneous aqueous solution: Reaction
            kinetics and reaction mechanisms.
  JOURNAL   Environ. Sci. Technol. 31 (1997) 253-260.
REFERENCE   3  [PMID:8663199]
  AUTHORS   Neumann A, Wohlfarth G, Diekert G.
  TITLE     Purification and characterization of tetrachloroethene reductive
            dehalogenase from Dehalospirillum multivorans.
  JOURNAL   J. Biol. Chem. 271 (1996) 16515-9.
  ORGANISM  Dehalospirillum multivorans
REFERENCE   4  [PMID:9224702]
  AUTHORS   Schumacher W, Holliger C, Zehnder AJ, Hagen WR.
  TITLE     Redox chemistry of cobalamin and iron-sulfur cofactors in the
            tetrachloroethene reductase of Dehalobacter restrictus.
  JOURNAL   FEBS. Lett. 409 (1997) 421-5.
  ORGANISM  Dehalobacter restrictus
REFERENCE   5  [PMID:8636034]
  AUTHORS   Schumacher W, Holliger C.
  TITLE     The proton/electron ration of the menaquinone-dependent electron
            transport from dihydrogen to tetrachloroethene in &quot;Dehalobacter
            restrictus&quot;.
  JOURNAL   J. Bacteriol. 178 (1996) 2328-33.
  ORGANISM  Dehalobacter restrictus
PATHWAY     PATH: map00625  Tetrachloroethene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 1.97.1.8
            ExPASy - ENZYME nomenclature database: 1.97.1.8
            ExplorEnz - The Enzyme Database: 1.97.1.8
            ERGO genome analysis and discovery system: 1.97.1.8
            UM-BBD (Biocatalysis/Biodegradation Database): 1.97.1.8
            BRENDA, the Enzyme Database: 1.97.1.8
///
ENTRY       EC 1.97.1.9                 Enzyme
NAME        selenate reductase
CLASS       Oxidoreductases;
            Other oxidoreductases;
            Sole sub-subclass for oxidoreductases that do not belong in the
            other subclasses
SYSNAME     selenite:reduced acceptor oxidoreductase
REACTION    selenite + H2O + acceptor = selenate + reduced acceptor [RN:R07229]
ALL_REAC    R07229
SUBSTRATE   selenite [CPD:C05684];
            H2O [CPD:C00001];
            acceptor [CPD:C00028]
PRODUCT     selenate [CPD:C05697];
            reduced acceptor [CPD:C00030]
COMMENT     The periplasmic enzyme from Thauera selenatis is a complex
            comprising three heterologous subunits (alpha, beta and gamma) that
            contains molybdenum, iron, acid-labile sulfide and heme b as
            cofactor constituents. Nitrate, nitrite, chlorate and sulfate are
            not substrates. A number of compounds, including acetate, lactate,
            pyruvate, and certain sugars, amino acids, fatty acids, di- and
            tricarboxylic acids, and benzoate can serve as electron donors.
REFERENCE   1  [PMID:9295321]
  AUTHORS   Schroder I, Rech S, Krafft T, Macy JM.
  TITLE     Purification and characterization of the selenate reductase from
            Thauera selenatis.
  JOURNAL   J. Biol. Chem. 272 (1997) 23765-8.
  ORGANISM  Thauera selenatis
REFERENCE   2  [PMID:8427805]
  AUTHORS   Macy JM, Rech S, Auling G, Dorsch M, Stackebrandt E, Sly LI.
  TITLE     Thauera selenatis gen. nov., sp. nov., a member of the beta subclass
            of Proteobacteria with a novel type of anaerobic respiration.
  JOURNAL   Int. J. Syst. Bacteriol. 43 (1993) 135-42.
  ORGANISM  Thauera selenatis
REFERENCE   3  [PMID:10826693]
  AUTHORS   Krafft T, Bowen A, Theis F, Macy JM.
  TITLE     Cloning and sequencing of the genes encoding the
            periplasmic-cytochrome B-containing selenate reductase of Thauera
            selenatis.
  JOURNAL   DNA. Seq. 10 (2000) 365-77.
  ORGANISM  Thauera selenatis
REFERENCE   4  [PMID:10525169]
  AUTHORS   Stolz JF, Oremland RS.
  TITLE     Bacterial respiration of arsenic and selenium.
  JOURNAL   FEMS. Microbiol. Rev. 23 (1999) 615-27.
  ORGANISM  Thauera selenatis, Sulfurospirillum barnesii
GENES       BUR: Bcep18194_B2000 Bcep18194_C6878
            HAR: HEAR1662(narG) HEAR3343
            NWI: Nwi_0774
            MVA: Mvan_4546
            MKM: Mkms_1280
            MJL: Mjls_1289
            ART: Arth_0314
            CCH: Cag_0619 Cag_0953
DBLINKS     IUBMB Enzyme Nomenclature: 1.97.1.9
            ExPASy - ENZYME nomenclature database: 1.97.1.9
            ExplorEnz - The Enzyme Database: 1.97.1.9
            ERGO genome analysis and discovery system: 1.97.1.9
            BRENDA, the Enzyme Database: 1.97.1.9
///
ENTRY       EC 1.97.1.10                Enzyme
NAME        thyroxine 5'-deiodinase;
            diiodothyronine 5'-deiodinase [ambiguous];
            iodothyronine 5'-deiodinase;
            iodothyronine outer ring monodeiodinase;
            type I iodothyronine deiodinase;
            type II iodothyronine deiodinase;
            thyroxine 5-deiodinase [misleading];
            L-thyroxine iodohydrolase (reducing)
CLASS       Oxidoreductases;
            Other oxidoreductases;
            Sole sub-subclass for oxidoreductases that do not belong in the
            other subclasses
SYSNAME     acceptor:3,5,3'-triiodo-L-thyronine oxidoreductase (iodinating)
REACTION    3,5,3'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2
            [RN:R03734]
ALL_REAC    R03734
SUBSTRATE   3,5,3'-triiodo-L-thyronine [CPD:C02465];
            iodide [CPD:C00708];
            A [CPD:C00028];
            H+ [CPD:C00080]
PRODUCT     L-thyroxine [CPD:C01829];
            AH2 [CPD:C00030]
COMMENT     The enzyme activity has only been demonstrated in the direction of
            5'-deiodination, which renders the thyroid hormone more active. The
            enzyme consists of type I and type II enzymes, both containing
            selenocysteine, but with different kinetics. For the type I enzyme
            the first reaction is a reductive deiodination converting the -Se-H
            group of the enzyme into an -Se-I group; the reductant then
            reconverts this into -Se-H, releasing iodide.
REFERENCE   1  [PMID:7053997]
  AUTHORS   Chopra IJ, Chua Teco GN.
  TITLE     Characteristics of inner ring (3 or 5) monodeiodination of
            3,5-diiodothyronine in rat liver: evidence suggesting marked
            similarities of inner and outer ring deiodinases for iodothyronines.
  JOURNAL   Endocrinology. 110 (1982) 89-97.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6176242]
  AUTHORS   Goswami A, Leonard JL, Rosenberg IN.
  TITLE     Inhibition by coumadin anticoagulants of enzymatic outer ring
            monodeiodination of iodothyronines.
  JOURNAL   Biochem. Biophys. Res. Commun. 104 (1982) 1231-8.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:7227308]
  AUTHORS   Smallridge RC, Burman KD, Ward KE, Wartofsky L, Dimond RC, Wright
            FD, Latham KR.
  TITLE     3',5'-diiodothyronine to 3'-monoiodothyronine conversion in the fed
            and fasted rat: enzyme characteristics and evidence for two distinct
            5'-deiodinases.
  JOURNAL   Endocrinology. 108 (1981) 2336-45.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:11898402]
  AUTHORS   Kohrle J.
  TITLE     Iodothyronine deiodinases.
  JOURNAL   Methods. Enzymol. 347 (2002) 125-67.
ORTHOLOGY   KO: K01562  thyroxine 5'-deiodinase
GENES       HSA: 1733(DIO1) 1734(DIO2)
            MMU: 13370(Dio1) 13371(Dio2)
            RNO: 25430(Dio1) 25506(P4hb) 65162(Dio2)
            CFA: 403635(DIO1) 490813(DIO2)
            BTA: 494548(DIO2)
            SSC: 414379(DIO2) 414380(DIO1)
            GGA: 395940(DIO1)
DBLINKS     IUBMB Enzyme Nomenclature: 1.97.1.10
            ExPASy - ENZYME nomenclature database: 1.97.1.10
            ExplorEnz - The Enzyme Database: 1.97.1.10
            ERGO genome analysis and discovery system: 1.97.1.10
            BRENDA, the Enzyme Database: 1.97.1.10
            CAS: 70712-46-8
///
ENTRY       EC 1.97.1.11                Enzyme
NAME        thyroxine 5-deiodinase;
            diiodothyronine 5'-deiodinase[ambiguous];
            iodothyronine 5-deiodinase;
            iodothyronine inner ring monodeiodinase;
            type III iodothyronine deiodinase
CLASS       Oxidoreductases;
            Other oxidoreductases;
            Sole sub-subclass for oxidoreductases that do not belong in the
            other subclasses
SYSNAME     acceptor:3,3',5'-triiodo-L-thyronine oxidoreductase (iodinating)
REACTION    3,3',5'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2
            [RN:R07230]
ALL_REAC    R07230
SUBSTRATE   3,3',5'-triiodo-L-thyronine [CPD:C07639];
            iodide [CPD:C00708];
            A [CPD:C00028];
            H+ [CPD:C00080]
PRODUCT     L-thyroxine [CPD:C01829];
            AH2 [CPD:C00030]
COMMENT     The enzyme activity has only been demonstrated in the direction of
            5-deiodination. This removal of the 5-iodine, i.e. from the inner
            ring, largely inactivates the hormone thyroxine.
REFERENCE   1  [PMID:7053997]
  AUTHORS   Chopra IJ, Chua Teco GN.
  TITLE     Characteristics of inner ring (3 or 5) monodeiodination of
            3,5-diiodothyronine in rat liver: evidence suggesting marked
            similarities of inner and outer ring deiodinases for iodothyronines.
  JOURNAL   Endocrinology. 110 (1982) 89-97.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:11898402]
  AUTHORS   Kohrle J.
  TITLE     Iodothyronine deiodinases.
  JOURNAL   Methods. Enzymol. 347 (2002) 125-67.
  ORGANISM  rat [GN:rno], human [GN:hsa], mouse [GN:mmu]
ORTHOLOGY   KO: K07754  thyroxine 5-deiodinase
GENES       HSA: 1735(DIO3)
            MMU: 107585(Dio3)
            RNO: 29475(Dio3)
            CFA: 490862(LOC490862)
            BTA: 494549(DIO3)
            SSC: 414378(DIO3)
            GGA: 395939(DIO3)
DBLINKS     IUBMB Enzyme Nomenclature: 1.97.1.11
            ExPASy - ENZYME nomenclature database: 1.97.1.11
            ExplorEnz - The Enzyme Database: 1.97.1.11
            ERGO genome analysis and discovery system: 1.97.1.11
            BRENDA, the Enzyme Database: 1.97.1.11
///
ENTRY       EC 1.97.1.-                 Enzyme
CLASS       Oxidoreductases;
            Other oxidoreductases
REACTION    (1) HCl + p-Benzenediol + Glutathione disulfide <=>
            Chlorohydroquinone + 2 Glutathione [RN:R05267];
            (2) 2,5-Dichlorohydroquinone + 2 Glutathione <=> Chlorohydroquinone
            + Glutathione disulfide + HCl [RN:R05269];
            (3) 1,1-Dichloro-2,2-bis(4-chlorophenyl)ethylene <=>
            1-Chloro-2,2-bis(4'-chlorophenyl)ethylene + Chloride [RN:R05497];
            (4) Vinyl chloride + 2 H+ <=> Ethylene + HCl [RN:R05498];
            (5) trans-1,2-Dichloroethene + 2 H+ <=> Vinyl chloride + HCl
            [RN:R05502];
            (6) cis-1,2-Dichloroethene + 2 H+ <=> Vinyl chloride + HCl
            [RN:R05503];
            (7) 5-Chloro-2-hydroxymuconic semialdehyde + H+ <=>
            2-Hydroxymuconate semialdehyde + Cl- [RN:R05504];
            (8) 2,4-Dichlorophenoxyacetate + H+ + 2 e- <=>
            4-Chlorophenoxyacetate + Cl- [RN:R05505];
            (9) Tetrabromobisphenol A <=> Tribromobisphenol A + Hydrobromic acid
            [RN:R06876];
            (10) Tribromobisphenol A <=> Dibromobisphenol A + Hydrobromic acid
            [RN:R06877];
            (11) Dibromobisphenol A <=> Monobromobisphenol A + Hydrobromic acid
            [RN:R06878];
            (12) Monobromobisphenol A <=> Bisphenol A + Hydrobromic acid
            [RN:R06879];
            (13) 2,4-Dichloroaniline + 2 H+ <=> 4-Chloroaniline + HCl
            [RN:R07794]
SUBSTRATE   HCl [CPD:C01327];
            p-Benzenediol [CPD:C00530];
            Glutathione disulfide [CPD:C00127];
            2,5-Dichlorohydroquinone [CPD:C06600];
            Glutathione [CPD:C00051];
            1,1-Dichloro-2,2-bis(4-chlorophenyl)ethylene [CPD:C04596];
            Vinyl chloride [CPD:C06793];
            H+ [CPD:C00080];
            Tetrachloroethene [CPD:C06789];
            Trichloroethene [CPD:C06790];
            trans-1,2-Dichloroethene [CPD:C06791];
            cis-1,2-Dichloroethene [CPD:C06792];
            5-Chloro-2-hydroxymuconic semialdehyde [CPD:C07089];
            2,4-Dichlorophenoxyacetate [CPD:C03664];
            e- [CPD:C05359];
            Tetrabromobisphenol A [CPD:C13620];
            Tribromobisphenol A [CPD:C13621];
            Dibromobisphenol A [CPD:C13622];
            Monobromobisphenol A [CPD:C13623]
PRODUCT     Chlorohydroquinone [CPD:C06601];
            Glutathione [CPD:C00051];
            Glutathione disulfide [CPD:C00127];
            HCl [CPD:C01327];
            1-Chloro-2,2-bis(4'-chlorophenyl)ethylene [CPD:C06637];
            Chloride [CPD:C00115];
            Ethylene [CPD:C06547];
            Trichloroethene [CPD:C06790];
            trans-1,2-Dichloroethene [CPD:C06791];
            cis-1,2-Dichloroethene [CPD:C06792];
            Vinyl chloride [CPD:C06793];
            2-Hydroxymuconate semialdehyde [CPD:C00682];
            Cl- [CPD:C00698];
            4-Chlorophenoxyacetate [CPD:C07088];
            Tribromobisphenol A [CPD:C13621];
            Hydrobromic acid [CPD:C13645];
            Dibromobisphenol A [CPD:C13622];
            Monobromobisphenol A [CPD:C13623];
            Bisphenol A [CPD:C13624]
///
ENTRY       EC 1.98.1.1       Obsolete  Enzyme
NAME        Transferred to 1.12.7.2
CLASS       Oxidoreductases
COMMENT     Transferred entry: Now EC 1.12.7.2, ferredoxin hydrogenase (EC
            1.98.1.1 created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.98.1.1
            ExPASy - ENZYME nomenclature database: 1.98.1.1
            ExplorEnz - The Enzyme Database: 1.98.1.1
            ERGO genome analysis and discovery system: 1.98.1.1
            BRENDA, the Enzyme Database: 1.98.1.1
///
ENTRY       EC 1.99.1.1       Obsolete  Enzyme
NAME        Transferred to 1.12.7.2
CLASS       Oxidoreductases
COMMENT     Transferred entry: Now EC 1.12.7.2, ferredoxin hydrogenase (EC
            1.99.1.1 created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.1.1
            ExPASy - ENZYME nomenclature database: 1.99.1.1
            ExplorEnz - The Enzyme Database: 1.99.1.1
            ERGO genome analysis and discovery system: 1.99.1.1
            BRENDA, the Enzyme Database: 1.99.1.1
///
ENTRY       EC 1.99.1.2       Obsolete  Enzyme
NAME        Transferred to 1.14.16.1
CLASS       Oxidoreductases
COMMENT     Transferred entry: Now EC 1.14.16.1, phenylalanine 4-monooxygenase
            (EC 1.99.1.2 created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.1.2
            ExPASy - ENZYME nomenclature database: 1.99.1.2
            ExplorEnz - The Enzyme Database: 1.99.1.2
            ERGO genome analysis and discovery system: 1.99.1.2
            BRENDA, the Enzyme Database: 1.99.1.2
///
ENTRY       EC 1.99.1.3       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases
COMMENT     Deleted entry: nicotinate 6-hydroxylase (EC 1.99.1.3 created 1961,
            deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.1.3
            ExPASy - ENZYME nomenclature database: 1.99.1.3
            ExplorEnz - The Enzyme Database: 1.99.1.3
            ERGO genome analysis and discovery system: 1.99.1.3
            BRENDA, the Enzyme Database: 1.99.1.3
///
ENTRY       EC 1.99.1.4       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases
COMMENT     Deleted entry: tryptophan 5-hydroxylase (EC 1.99.1.4 created 1961,
            deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.1.4
            ExPASy - ENZYME nomenclature database: 1.99.1.4
            ExplorEnz - The Enzyme Database: 1.99.1.4
            ERGO genome analysis and discovery system: 1.99.1.4
            BRENDA, the Enzyme Database: 1.99.1.4
///
ENTRY       EC 1.99.1.5       Obsolete  Enzyme
NAME        Transferred to 1.14.13.9
CLASS       Oxidoreductases
COMMENT     Transferred entry: Now EC 1.14.13.9, kynurenine 3-monooxygenase (EC
            1.99.1.5 created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.1.5
            ExPASy - ENZYME nomenclature database: 1.99.1.5
            ExplorEnz - The Enzyme Database: 1.99.1.5
            ERGO genome analysis and discovery system: 1.99.1.5
            BRENDA, the Enzyme Database: 1.99.1.5
///
ENTRY       EC 1.99.1.6       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases
COMMENT     Deleted entry: steroid 11alpha-hydroxylase (EC 1.99.1.6 created
            1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.1.6
            ExPASy - ENZYME nomenclature database: 1.99.1.6
            ExplorEnz - The Enzyme Database: 1.99.1.6
            ERGO genome analysis and discovery system: 1.99.1.6
            BRENDA, the Enzyme Database: 1.99.1.6
///
ENTRY       EC 1.99.1.7       Obsolete  Enzyme
NAME        Transferred to 1.14.15.4
CLASS       Oxidoreductases
COMMENT     Transferred entry: Now EC 1.14.15.4, steroid 11beta-monooxygenase
            (EC 1.99.1.7 created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.1.7
            ExPASy - ENZYME nomenclature database: 1.99.1.7
            ExplorEnz - The Enzyme Database: 1.99.1.7
            ERGO genome analysis and discovery system: 1.99.1.7
            BRENDA, the Enzyme Database: 1.99.1.7
///
ENTRY       EC 1.99.1.8       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases
COMMENT     Deleted entry: steroid 6beta-hydroxylase (EC 1.99.1.8 created 1961,
            deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.1.8
            ExPASy - ENZYME nomenclature database: 1.99.1.8
            ExplorEnz - The Enzyme Database: 1.99.1.8
            ERGO genome analysis and discovery system: 1.99.1.8
            BRENDA, the Enzyme Database: 1.99.1.8
///
ENTRY       EC 1.99.1.9       Obsolete  Enzyme
NAME        Transferred to 1.14.99.9
CLASS       Oxidoreductases
COMMENT     Transferred entry: Now EC 1.14.99.9, steroid 17alpha-monooxygenase
            (EC 1.99.1.9 created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.1.9
            ExPASy - ENZYME nomenclature database: 1.99.1.9
            ExplorEnz - The Enzyme Database: 1.99.1.9
            ERGO genome analysis and discovery system: 1.99.1.9
            BRENDA, the Enzyme Database: 1.99.1.9
///
ENTRY       EC 1.99.1.10      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases
COMMENT     Deleted entry: steroid 19-hydroxylase (EC 1.99.1.10 created 1961,
            deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.1.10
            ExPASy - ENZYME nomenclature database: 1.99.1.10
            ExplorEnz - The Enzyme Database: 1.99.1.10
            ERGO genome analysis and discovery system: 1.99.1.10
            BRENDA, the Enzyme Database: 1.99.1.10
///
ENTRY       EC 1.99.1.11      Obsolete  Enzyme
NAME        Transferred to 1.14.99.10
CLASS       Oxidoreductases
COMMENT     Transferred entry: Now EC 1.14.99.10, steroid 21-monooxygenase (EC
            1.99.1.11 created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.1.11
            ExPASy - ENZYME nomenclature database: 1.99.1.11
            ExplorEnz - The Enzyme Database: 1.99.1.11
            ERGO genome analysis and discovery system: 1.99.1.11
            BRENDA, the Enzyme Database: 1.99.1.11
///
ENTRY       EC 1.99.1.12      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases
COMMENT     Deleted entry: alkoxyaryl hydroxylase (EC 1.99.1.12 created 1961,
            deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.1.12
            ExPASy - ENZYME nomenclature database: 1.99.1.12
            ExplorEnz - The Enzyme Database: 1.99.1.12
            ERGO genome analysis and discovery system: 1.99.1.12
            BRENDA, the Enzyme Database: 1.99.1.12
///
ENTRY       EC 1.99.1.13      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Oxidoreductases
COMMENT     Deleted entry: squalene cyclohydroxylase, covered by EC 1.14.99.7
            (squalene monooxygenase) and by EC 5.4.99.7 (lanosterol synthase)
            (EC 1.99.1.13 created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.1.13
            ExPASy - ENZYME nomenclature database: 1.99.1.13
            ExplorEnz - The Enzyme Database: 1.99.1.13
            ERGO genome analysis and discovery system: 1.99.1.13
            BRENDA, the Enzyme Database: 1.99.1.13
///
ENTRY       EC 1.99.1.14      Obsolete  Enzyme
NAME        Transferred to 1.13.11.27
CLASS       Oxidoreductases
COMMENT     Transferred entry: Now EC 1.13.11.27, 4-hydroxyphenylpyruvate
            dioxygenase (EC 1.99.1.14 created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.1.14
            ExPASy - ENZYME nomenclature database: 1.99.1.14
            ExplorEnz - The Enzyme Database: 1.99.1.14
            ERGO genome analysis and discovery system: 1.99.1.14
            BRENDA, the Enzyme Database: 1.99.1.14
///
ENTRY       EC 1.99.2.1       Obsolete  Enzyme
NAME        Transferred to 1.13.11.12
CLASS       Oxidoreductases
COMMENT     Transferred entry: Now EC 1.13.11.12, lipoxygenase (EC 1.99.2.1
            created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.2.1
            ExPASy - ENZYME nomenclature database: 1.99.2.1
            ExplorEnz - The Enzyme Database: 1.99.2.1
            ERGO genome analysis and discovery system: 1.99.2.1
            BRENDA, the Enzyme Database: 1.99.2.1
///
ENTRY       EC 1.99.2.2       Obsolete  Enzyme
NAME        Transferred to 1.13.11.1
CLASS       Oxidoreductases
COMMENT     Transferred entry: Now EC 1.13.11.1, catechol 1,2-dioxygenase (EC
            1.99.2.2 created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.2.2
            ExPASy - ENZYME nomenclature database: 1.99.2.2
            ExplorEnz - The Enzyme Database: 1.99.2.2
            ERGO genome analysis and discovery system: 1.99.2.2
            BRENDA, the Enzyme Database: 1.99.2.2
///
ENTRY       EC 1.99.2.3       Obsolete  Enzyme
NAME        Transferred to 1.13.11.3
CLASS       Oxidoreductases
COMMENT     Transferred entry: Now EC 1.13.11.3, protocatechuate 3,4-dioxygenase
            (EC 1.99.2.3 created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.2.3
            ExPASy - ENZYME nomenclature database: 1.99.2.3
            ExplorEnz - The Enzyme Database: 1.99.2.3
            ERGO genome analysis and discovery system: 1.99.2.3
            BRENDA, the Enzyme Database: 1.99.2.3
///
ENTRY       EC 1.99.2.4       Obsolete  Enzyme
NAME        Transferred to 1.13.11.4
CLASS       Oxidoreductases
COMMENT     Transferred entry: Now EC 1.13.11.4, gentisate 1,2-dioxygenase (EC
            1.99.2.4 created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.2.4
            ExPASy - ENZYME nomenclature database: 1.99.2.4
            ExplorEnz - The Enzyme Database: 1.99.2.4
            ERGO genome analysis and discovery system: 1.99.2.4
            BRENDA, the Enzyme Database: 1.99.2.4
///
ENTRY       EC 1.99.2.5       Obsolete  Enzyme
NAME        Transferred to 1.13.11.5
CLASS       Oxidoreductases
COMMENT     Transferred entry: Now EC 1.13.11.5, homogentisate 1,2-dioxygenase
            (EC 1.99.2.5 created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.2.5
            ExPASy - ENZYME nomenclature database: 1.99.2.5
            ExplorEnz - The Enzyme Database: 1.99.2.5
            ERGO genome analysis and discovery system: 1.99.2.5
            BRENDA, the Enzyme Database: 1.99.2.5
///
ENTRY       EC 1.99.2.6       Obsolete  Enzyme
NAME        Transferred to 1.13.99.1
CLASS       Oxidoreductases
COMMENT     Transferred entry: Now EC 1.13.99.1, inositol oxygenase (EC 1.99.2.6
            created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 1.99.2.6
            ExPASy - ENZYME nomenclature database: 1.99.2.6
            ExplorEnz - The Enzyme Database: 1.99.2.6
            ERGO genome analysis and discovery system: 1.99.2.6
            BRENDA, the Enzyme Database: 1.99.2.6
///
ENTRY       EC 1.-.-.-                  Enzyme
CLASS       Oxidoreductases
REACTION    6-Deoxyerythronolide B + Oxygen <=> Erythronolide B [RN:R05270]
SUBSTRATE   6-Deoxyerythronolide B [CPD:C03240];
            Oxygen [CPD:C00007]
PRODUCT     Erythronolide B [CPD:C06635]
///
ENTRY       EC 2.1.1.1                  Enzyme
NAME        nicotinamide N-methyltransferase;
            nicotinamide methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:nicotinamide N-methyltransferase
REACTION    S-adenosyl-L-methionine + nicotinamide = S-adenosyl-L-homocysteine +
            1-methylnicotinamide [RN:R01269]
ALL_REAC    R01269
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            nicotinamide [CPD:C00153]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            1-methylnicotinamide [CPD:C02918]
REFERENCE   1  [PMID:14832232]
  AUTHORS   CANTONI GL.
  TITLE     Methylation of nicotinamide with soluble enzyme system from rat
            liver.
  JOURNAL   J. Biol. Chem. 189 (1951) 203-16.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K00541  nicotinamide N-methyltransferase
GENES       HSA: 4837(NNMT)
            PTR: 451558(NNMT)
            MMU: 18113(Nnmt)
            CFA: 489396(NNMT)
            PMB: A9601_01861(chlM)
            PMC: P9515_01971(chlM)
            PMF: P9303_27151(chlM)
            PMG: P9301_01881(chlM)
            PME: NATL1_02431(chlM)
STRUCTURES  PDB: 2I62  2IIP  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.1
            ExPASy - ENZYME nomenclature database: 2.1.1.1
            ExplorEnz - The Enzyme Database: 2.1.1.1
            ERGO genome analysis and discovery system: 2.1.1.1
            BRENDA, the Enzyme Database: 2.1.1.1
            CAS: 9029-74-7
///
ENTRY       EC 2.1.1.2                  Enzyme
NAME        guanidinoacetate N-methyltransferase;
            GA methylpherase;
            guanidinoacetate methyltransferase;
            guanidinoacetate transmethylase;
            methionine-guanidinoacetic transmethylase;
            guanidoacetate methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:N-guanidinoacetate methyltransferase
REACTION    S-adenosyl-L-methionine + guanidinoacetate =
            S-adenosyl-L-homocysteine + creatine [RN:R01883]
ALL_REAC    R01883
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            guanidinoacetate [CPD:C00581]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            creatine [CPD:C00300]
REFERENCE   1
  AUTHORS   Cantoni, G.L. and Scarano, E.
  TITLE     The formation of S-adenosylhomocysteine in enzymatic
            transmethylation reactions.
  JOURNAL   J. Am. Chem. Soc. 76 (1954) 4744.
REFERENCE   2  [PMID:13192118]
  AUTHORS   CANTONI GL, VIGNOS PJ Jr.
  TITLE     Enzymatic mechanism of creatine synthesis.
  JOURNAL   J. Biol. Chem. 209 (1954) 647-59.
  ORGANISM  guinea pig, pig [GN:ssc], cow [GN:bta], rabbit
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K00542  guanidinoacetate N-methyltransferase
GENES       HSA: 2593(GAMT)
            MMU: 14431(Gamt)
            RNO: 25257(Gamt)
            CFA: 485085(GAMT)
            GGA: 770737(GAMT)
            XLA: 380384(gamt)
            XTR: 394491(gamt)
            DRE: 403058(gamt)
            PIC: PICST_66076(RMT2)
            FAL: FRAAL4941
STRUCTURES  PDB: 1KHH  1P1B  1P1C  1XCJ  1XCL  1ZX0  2BLN  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.2
            ExPASy - ENZYME nomenclature database: 2.1.1.2
            ExplorEnz - The Enzyme Database: 2.1.1.2
            ERGO genome analysis and discovery system: 2.1.1.2
            BRENDA, the Enzyme Database: 2.1.1.2
            CAS: 9029-75-8
///
ENTRY       EC 2.1.1.3                  Enzyme
NAME        thetin---homocysteine S-methyltransferase;
            dimethylthetin-homocysteine methyltransferase;
            thetin-homocysteine methylpherase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     dimethylsulfonioacetate:L-homocysteine S-methyltransferase
REACTION    dimethylsulfonioacetate + L-homocysteine = S-methylthioglycolate +
            L-methionine [RN:R04153]
ALL_REAC    R04153
SUBSTRATE   dimethylsulfonioacetate [CPD:C03392];
            L-homocysteine [CPD:C00155]
PRODUCT     S-methylthioglycolate [CPD:C03173];
            L-methionine [CPD:C00073]
REFERENCE   1  [PMID:14456704]
  AUTHORS   KLEE WA, RICHARDS HH, CANTONI GL.
  TITLE     The synthesis of methionine by enzymic transmethylation. VII.
            Existence of two separate homocysteine methylpherases on mammalian
            liver.
  JOURNAL   Biochim. Biophys. Acta. 54 (1961) 157-64.
  ORGANISM  rat [GN:rno], horse
REFERENCE   2  [PMID:13315256]
  AUTHORS   MAW GA.
  TITLE     Thetin-homocysteine transmethylase; a preliminary manometric study
            of the enzyme from rat liver.
  JOURNAL   Biochem. J. 63 (1956) 116-24.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:13584318]
  AUTHORS   MAW GA.
  TITLE     Thetin-homocysteine transmethylase; some further characteristics of
            the enzyme from rat liver.
  JOURNAL   Biochem. J. 70 (1958) 168-73.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.3
            ExPASy - ENZYME nomenclature database: 2.1.1.3
            ExplorEnz - The Enzyme Database: 2.1.1.3
            ERGO genome analysis and discovery system: 2.1.1.3
            BRENDA, the Enzyme Database: 2.1.1.3
            CAS: 9029-76-9
///
ENTRY       EC 2.1.1.4                  Enzyme
NAME        acetylserotonin O-methyltransferase;
            hydroxyindole methyltransferase;
            hydroxyindole O-methyltransferase;
            N-acetylserotonin O-methyltransferase;
            acetylserotonin methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:N-acetylserotonin O-methyltransferase
REACTION    S-adenosyl-L-methionine + N-acetylserotonin =
            S-adenosyl-L-homocysteine + melatonin [RN:R03130]
ALL_REAC    R03130;
            (other) R04905
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            N-acetylserotonin [CPD:C00978]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            melatonin [CPD:C01598]
COMMENT     Some other hydroxyindoles also act as acceptor, but more slowly.
REFERENCE   1  [PMID:13685335]
  AUTHORS   AXELROD J, WEISSBACH H.
  TITLE     Purification and properties of hydroxyindole-O-methyl transferase.
  JOURNAL   J. Biol. Chem. 236 (1961) 211-3.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00380  Tryptophan metabolism
ORTHOLOGY   KO: K00543  acetylserotonin N-methyltransferase
GENES       HSA: 438(ASMT)
            MCC: 574350(HIOMT)
            BTA: 281013(ASMT)
            GGA: 396286(ASMT)
            CVI: CV_2261
            REH: H16_A0304(asmT)
            BUR: Bcep18194_C6864
            BPM: BURPS1710b_1210
            CCH: Cag_0115
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.4
            ExPASy - ENZYME nomenclature database: 2.1.1.4
            ExplorEnz - The Enzyme Database: 2.1.1.4
            ERGO genome analysis and discovery system: 2.1.1.4
            BRENDA, the Enzyme Database: 2.1.1.4
            CAS: 9029-77-0
///
ENTRY       EC 2.1.1.5                  Enzyme
NAME        betaine---homocysteine S-methyltransferase;
            betaine-homocysteine methyltransferase;
            betaine-homocysteine transmethylase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     trimethylammonioacetate:L-homocysteine S-methyltransferase
REACTION    trimethylammonioacetate + L-homocysteine = dimethylglycine +
            L-methionine [RN:R02821]
ALL_REAC    R02821
SUBSTRATE   trimethylammonioacetate [CPD:C00719];
            L-homocysteine [CPD:C00155]
PRODUCT     dimethylglycine [CPD:C01026];
            L-methionine [CPD:C00073]
REFERENCE   1  [PMID:14456704]
  AUTHORS   KLEE WA, RICHARDS HH, CANTONI GL.
  TITLE     The synthesis of methionine by enzymic transmethylation. VII.
            Existence of two separate homocysteine methylpherases on mammalian
            liver.
  JOURNAL   Biochim. Biophys. Acta. 54 (1961) 157-64.
  ORGANISM  horse, rat [GN:rno]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K00544  betaine-homocysteine S-methyltransferase
GENES       HSA: 635(BHMT)
            MMU: 12116(Bhmt)
            RNO: 81508(Bhmt)
            CFA: 479171(BHMT)
            BTA: 497025(BHMT)
            GGA: 416371(BHMT)
            XLA: 495275(LOC495275)
            XTR: 496651(LOC496651)
            DRE: 322228(bhmt)
            SPU: 575553(LOC575553)
            CSA: Csal_0065
            REH: H16_A0150(bhmT)
            PUB: SAR11_1173(bhmT)
            MLO: mlr1281
STRUCTURES  PDB: 1LT7  1LT8  1UMY  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.5
            ExPASy - ENZYME nomenclature database: 2.1.1.5
            ExplorEnz - The Enzyme Database: 2.1.1.5
            ERGO genome analysis and discovery system: 2.1.1.5
            BRENDA, the Enzyme Database: 2.1.1.5
            CAS: 9029-78-1
///
ENTRY       EC 2.1.1.6                  Enzyme
NAME        catechol O-methyltransferase;
            COMT I ;
            COMT II;
            S-COMT (soluble form of catechol-O-methyltransferase);
            MB-COMT (membrane-bound form of catechol-O-methyltransferase);
            catechol methyltransferase;
            catecholamine O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:catechol O-methyltransferase
REACTION    S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a
            guaiacol [RN:R07330]
ALL_REAC    R07330 > R00827 R02534 R02920 R03304 R04301 R04881 R04887
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            catechol [CPD:C00090]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            guaiacol [CPD:C01502]
COMMENT     The mammalian enzyme acts more rapidly on catecholamines such as
            adrenaline or noradrenaline than on catechols.
REFERENCE   1  [PMID:13575440]
  AUTHORS   AXELROD J, TOMCHICK R.
  TITLE     Enzymatic O-methylation of epinephrine and other catechols.
  JOURNAL   J. Biol. Chem. 233 (1958) 702-5.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:438821]
  AUTHORS   Gulliver PA, Tipton KF.
  TITLE     The purification and properties of pig brain
            catechol-o-methyltransferase.
  JOURNAL   J. Neurochem. 32 (1979) 1525-9.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:762061]
  AUTHORS   Huh MM, Friedhoff AJ.
  TITLE     Multiple molecular forms of catechol-O-methyltransferase. Evidence
            for two distinct forms, and their purification and physical
            characterization.
  JOURNAL   J. Biol. Chem. 254 (1979) 299-308.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00350  Tyrosine metabolism
ORTHOLOGY   KO: K00545  catechol O-methyltransferase
GENES       HSA: 1312(COMT)
            MMU: 12846(Comt)
            RNO: 24267(Comt)
            CFA: 445450(COMT)
            GGA: 416783(COMT)
            XLA: 379402(MGC53924)
            PIC: PICST_36800(COM1)
            SPO: SPBPB21E7.04c
            ANI: AN6402.2
            AFM: AFUA_2G15085 AFUA_2G17820 AFUA_5G06990
            AOR: AO090701000285
            RLE: RL2915
            GOX: GOX0534
            MTU: Rv1703c
            MBO: Mb1729c
            MBB: BCG_1741c
            MVA: Mvan_3280
            MGI: Mflv_3499
STRUCTURES  PDB: 1H1D  1JR4  1VID  2CL5  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.6
            ExPASy - ENZYME nomenclature database: 2.1.1.6
            ExplorEnz - The Enzyme Database: 2.1.1.6
            ERGO genome analysis and discovery system: 2.1.1.6
            BRENDA, the Enzyme Database: 2.1.1.6
            CAS: 9012-25-3
///
ENTRY       EC 2.1.1.7                  Enzyme
NAME        nicotinate N-methyltransferase;
            furanocoumarin 8-methyltransferase;
            furanocoumarin 8-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:nicotinate N-methyltransferase
REACTION    S-adenosyl-L-methionine + nicotinate = S-adenosyl-L-homocysteine +
            N-methylnicotinate [RN:R01721]
ALL_REAC    R01721
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            nicotinate [CPD:C00253]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            N-methylnicotinate [CPD:C01004]
REFERENCE   1
  AUTHORS   Joshi, J.G. and Handler, P.
  TITLE     Biosynthesis of trigonelline.
  JOURNAL   J. Biol. Chem. 235 (1960) 2981-2983.
  ORGANISM  Pisum sativum
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
STRUCTURES  PDB: 5MHT  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.7
            ExPASy - ENZYME nomenclature database: 2.1.1.7
            ExplorEnz - The Enzyme Database: 2.1.1.7
            ERGO genome analysis and discovery system: 2.1.1.7
            BRENDA, the Enzyme Database: 2.1.1.7
            CAS: 9029-79-2
///
ENTRY       EC 2.1.1.8                  Enzyme
NAME        histamine N-methyltransferase;
            histamine 1-methyltransferase;
            histamine methyltransferase;
            histamine-methylating enzyme;
            imidazolemethyltransferase;
            S-adenosylmethionine-histamine N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:histamine N-tele-methyltransferase
REACTION    S-adenosyl-L-methionine + histamine = S-adenosyl-L-homocysteine +
            Ntau-methylhistamine [RN:R07231]
ALL_REAC    R07231;
            (other) R02155
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            histamine [CPD:C00388]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            Ntau-methylhistamine
REFERENCE   1  [PMID:13804910]
  AUTHORS   BROWN DD, TOMCHICK R, AXELROD J.
  TITLE     The distribution and properties of a histamine-methylating enzyme.
  JOURNAL   J. Biol. Chem. 234 (1959) 2948-50.
  ORGANISM  guinea pig
PATHWAY     PATH: map00340  Histidine metabolism
ORTHOLOGY   KO: K00546  histamine N-methyltransferase
GENES       HSA: 3176(HNMT)
            MMU: 140483(Hnmt)
            RNO: 81676(Hnmt)
            CFA: 476133(HNMT)
            GGA: 424298(HNMT)
            DRE: 445242(hnmt)
STRUCTURES  PDB: 1JQD  1JQE  2AOT  2AOU  2AOV  2AOW  2AOX  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.8
            ExPASy - ENZYME nomenclature database: 2.1.1.8
            ExplorEnz - The Enzyme Database: 2.1.1.8
            ERGO genome analysis and discovery system: 2.1.1.8
            BRENDA, the Enzyme Database: 2.1.1.8
            CAS: 9029-80-5
///
ENTRY       EC 2.1.1.9                  Enzyme
NAME        thiol S-methyltransferase;
            S-methyltransferase;
            thiol methyltransferase;
            TMT
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:thiol S-methyltransferase
REACTION    S-adenosyl-L-methionine + a thiol = S-adenosyl-L-homocysteine + a
            thioether [RN:R01235]
ALL_REAC    R01235;
            (other) R04931
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            thiol [CPD:C00145]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            thioether [CPD:C00297]
COMMENT     H2S and a variety of alkyl, aryl and heterocyclic thiols and hydroxy
            thiols can act as acceptors.
REFERENCE   1  [PMID:623768]
  AUTHORS   Borchardt RT, Cheng CF.
  TITLE     Purification and characterization of rat liver microsomal thiol
            methyltransferase.
  JOURNAL   Biochim. Biophys. Acta. 522 (1978) 340-53.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Bremer, J. and Greenberg, D.M.
  TITLE     Enzymic methylation of foreign sulfhydryl compounds.
  JOURNAL   Biochim. Biophys. Acta 46 (1961) 217-224.
  ORGANISM  rat [GN:rno], mouse [GN:mmu], rabbit, cow [GN:bta], guinea pig,
            chicken [GN:gga], sheep
REFERENCE   3  [PMID:485170]
  AUTHORS   Weisiger RA, Jakoby WB.
  TITLE     Thiol S-methyltransferase from rat liver.
  JOURNAL   Arch. Biochem. Biophys. 196 (1979) 631-7.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00450  Selenoamino acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.9
            ExPASy - ENZYME nomenclature database: 2.1.1.9
            ExplorEnz - The Enzyme Database: 2.1.1.9
            ERGO genome analysis and discovery system: 2.1.1.9
            UM-BBD (Biocatalysis/Biodegradation Database): 2.1.1.9
            BRENDA, the Enzyme Database: 2.1.1.9
            CAS: 9029-81-6
///
ENTRY       EC 2.1.1.10                 Enzyme
NAME        homocysteine S-methyltransferase;
            S-adenosylmethionine homocysteine transmethylase;
            S-methylmethionine homocysteine transmethylase;
            adenosylmethionine transmethylase;
            methylmethionine:homocysteine methyltransferase;
            adenosylmethionine:homocysteine methyltransferase;
            homocysteine methylase;
            homocysteine methyltransferase;
            homocysteine transmethylase;
            L-homocysteine S-methyltransferase;
            S-adenosyl-L-methionine:L-homocysteine methyltransferase;
            S-adenosylmethionine-homocysteine transmethylase;
            S-adenosylmethionine:homocysteine methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:L-homocysteine S-methyltransferase
REACTION    S-adenosyl-L-methionine + L-homocysteine = S-adenosyl-L-homocysteine
            + L-methionine [RN:R00650]
ALL_REAC    R00650
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            L-homocysteine [CPD:C00155]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            L-methionine [CPD:C00073]
COMMENT     The bacterial enzyme uses S-methylmethionine as donor more actively
            than S-adenosylmethionine.
REFERENCE   1  [PMID:4861151]
  AUTHORS   Balish E, Shapiro SK.
  TITLE     Methionine biosynthesis in Escherichia coli: induction and
            repression of methylmethionine(or adenosylmethionine):homocysteine
            methyltransferase.
  JOURNAL   Arch. Biochem. Biophys. 119 (1967) 62-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Shapiro, S.K.
  TITLE     Adenosylmethionine-homocysteine transmethylase.
  JOURNAL   Biochim. Biophys. Acta 29 (1958) 405-409.
  ORGANISM  Escherichia coli [GN:eco], Aerobacter aerogenes, Saccharomyces
            cerevisiae [GN:sce], Torulopsis utilis
REFERENCE   3
  AUTHORS   Shapiro, S.K. and Yphantis, D.A.
  TITLE     Assay of S-methylmethionine and S-adenosylmethionine homocysteine
            transmethylases.
  JOURNAL   Biochim. Biophys. Acta 36 (1959) 241-244.
  ORGANISM  Escherichia coli [GN:eco], Aerobacter aerogenes, Saccharomyces
            cerevisiae [GN:sce]
PATHWAY     PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K00547  homocysteine S-methyltransferase
GENES       XTR: 394486(MGC75760)
            SPU: 587964(LOC587964)
            ATH: AT3G22740(HMT3)
            OSA: 4324713 4332095 4348656
            AGO: AGOS_AFR410W
            PIC: PICST_30270(SAM4)
            ANI: AN3378.2
            AFM: AFUA_5G01500
            AOR: AO090010000103
            CNE: CNJ02520
            UMA: UM01787.1
            TET: TTHERM_00637220
            TBR: Tb927.1.1270
            TCR: 506479.120 508993.20
            LMA: LmjF36.6310
            ECO: b0261(mmuM)
            ECJ: JW0253(mmuM)
            ECA: ECA2797(mmuM)
            XCC: XCC1344(mmuM)
            XCB: XC_2894
            XCV: XCV1449(mmuM)
            XAC: XAC1392(mmuM)
            XOO: XOO1930(mmuM)
            XOM: XOO_1828(XOO1828)
            PFO: Pfl_2779
            AHA: AHA_2807
            MXA: MXAN_6160
            PUB: SAR11_0750(mmuM)
            RET: RHE_PC00163(ypc00089)
            RLE: RL1357 pRL100413
            JAN: Jann_3671
            RDE: RD1_0018 RD1_3753
            GBE: GbCGDNIH1_1976
            BSU: BG12751(ybgG)
            BLI: BL01781
            BLD: BLi00266(ybgG)
            BPU: BPUM_0224 BPUM_1027(yitJ)
            SSP: SSP2172
            SAG: SAG1305
            SAN: gbs1377
            SAK: SAK_1337
            SMU: SMU.952
            STC: str0584(mmuM)
            STL: stu0584(mmuM)
            SSA: SSA_1096(mmuM)
            LPL: lp_1298(mmuM)
            LAC: LBA1003(mmuM)
            LSL: LSL_1692
            LDB: Ldb0311
            LBU: LBUL_0268
            CAC: CAC3348
            CKL: CKL_2259
            MTU: Rv2458(mmuM)
            MTC: MT2533(mmuM)
            MBO: Mb2485(mmuM)
            MBB: BCG_2478(mmuM)
            MLE: ML1478
            MPA: MAP2279
            MAV: MAV_1715
            SCO: SCO6137(SC1A9.01c)
            SMA: SAV2111(mmuM)
            CMI: CMM_2830
            AAU: AAur_3089(mmuM)
            SEN: SACE_3890(mmuM)
            BAD: BAD_0986(mmuM)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.10
            ExPASy - ENZYME nomenclature database: 2.1.1.10
            ExplorEnz - The Enzyme Database: 2.1.1.10
            ERGO genome analysis and discovery system: 2.1.1.10
            BRENDA, the Enzyme Database: 2.1.1.10
            CAS: 9012-40-2
///
ENTRY       EC 2.1.1.11                 Enzyme
NAME        magnesium protoporphyrin IX methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:magnesium-protoporphyrin-IX
            O-methyltransferase
REACTION    S-adenosyl-L-methionine + magnesium protoporphyrin IX =
            S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl
            ester [RN:R04237]
ALL_REAC    R04237
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            magnesium protoporphyrin IX [CPD:C03516]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            magnesium protoporphyrin IX 13-methyl ester [CPD:C04536]
REFERENCE   1  [PMID:14063871]
  AUTHORS   GIBSON KD, NEUBERGER A, TAIT GH.
  TITLE     STUDIES ON THE BIOSYNTHESIS OF PORPHYRIN AND  BACTERIOCHLOROPHYLL BY
            RHODOPSEUDOMONAS SPHEROIDES. 4. S-ADENOSYLMETHIONINEMAGNESIUM
            PROTOPORPHYRIN METHYLTRANSFERASE.
  JOURNAL   Biochem. J. 88 (1963) 325-34.
  ORGANISM  Rhodopseudomonas spheroides
REFERENCE   2  [PMID:12489983]
  AUTHORS   Shepherd M, Reid JD, Hunter CN.
  TITLE     Purification and kinetic characterization of the magnesium
            protoporphyrin IX methyltransferase from Synechocystis PCC6803.
  JOURNAL   Biochem. J. 371 (2003) 351-60.
  ORGANISM  Synechocystis sp.
REFERENCE   3  [PMID:8071204]
  AUTHORS   Bollivar DW, Jiang ZY, Bauer CE, Beale SI.
  TITLE     Heterologous expression of the bchM gene product from Rhodobacter
            capsulatus and demonstration that it encodes
            S-adenosyl-L-methionine:Mg-protoporphyrin IX methyltransferase.
  JOURNAL   J. Bacteriol. 176 (1994) 5290-6.
  ORGANISM  Rhodobacter capsulatus
REFERENCE   4  [PMID:7925960]
  AUTHORS   Gibson LC, Hunter CN.
  TITLE     The bacteriochlorophyll biosynthesis gene, bchM, of Rhodobacter
            sphaeroides encodes S-adenosyl-L-methionine: Mg protoporphyrin IX
            methyltransferase.
  JOURNAL   FEBS. Lett. 352 (1994) 127-30.
  ORGANISM  Rhodopseudomonas spheroides
REFERENCE   5  [PMID:5774480]
  AUTHORS   Ebbon JG, Tait GH.
  TITLE     Studies on S-adenosylmethionine-magnesium protoporphyrin
            methyltransferase in Euglena gracilis strain Z.
  JOURNAL   Biochem. J. 111 (1969) 573-82.
  ORGANISM  Euglena gracilis
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K03428  magnesium-protoporphyrin O-methyltransferase
GENES       OSA: 4340015
            CME: CMI038C
            ECI: UTI89_C0993(smtA)
            BRA: BRADO1643(bchM)
            BBT: BBta_6413(bchM)
            RPA: RPA1546(bchM)
            RPB: RPB_3977
            RPC: RPC_1317
            RPD: RPD_3732
            RPE: RPE_1351
            RSP: RSP_0289(bchM)
            RSH: Rsph17029_1932
            RSQ: Rsph17025_1006
            RDE: RD1_0135(bchM)
            RRU: Rru_A0619
            SYN: slr0525(chlM)
            SYW: SYNW2287
            SYC: syc1079_d(chlM)
            SYF: Synpcc7942_0439
            SYD: Syncc9605_2425
            SYE: Syncc9902_2105
            SYG: sync_2640(chlM)
            SYR: SynRCC307_2263(chlM)
            SYX: SynWH7803_2306(chlM)
            CYA: CYA_0112(chlM)
            CYB: CYB_2107(chlM)
            TEL: tll0451(chlM)
            GVI: glr4402(chlM)
            ANA: alr3201(chlM)
            AVA: Ava_3899
            PMA: Pro0193(chlM)
            PMM: PMM0168(chlM)
            PMT: PMT2040
            PMN: PMN2A_1536
            PMI: PMT9312_0170
            PMB: A9601_01861(chlM)
            PMC: P9515_01971(chlM)
            PMF: P9303_27151(chlM)
            PMG: P9301_01881(chlM)
            PME: NATL1_02431(chlM)
            TER: Tery_4469
            CTE: CT1958(bchM)
            CCH: Cag_0228
            PVI: Cvib_0317
            PLT: Plut_0252
            RRS: RoseRS_1907
            RCA: Rcas_1539
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.11
            ExPASy - ENZYME nomenclature database: 2.1.1.11
            ExplorEnz - The Enzyme Database: 2.1.1.11
            ERGO genome analysis and discovery system: 2.1.1.11
            BRENDA, the Enzyme Database: 2.1.1.11
            CAS: 9029-82-7
///
ENTRY       EC 2.1.1.12                 Enzyme
NAME        methionine S-methyltransferase;
            S-adenosyl methionine:methionine methyl transferase;
            methionine methyltransferase;
            S-adenosylmethionine transmethylase;
            S-adenosylmethionine-methionine methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:L-methionine S-methyltransferase
REACTION    S-adenosyl-L-methionine + L-methionine = S-adenosyl-L-homocysteine +
            S-methyl-L-methionine [RN:R00649]
ALL_REAC    R00649;
            (other) R04772
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            L-methionine [CPD:C00073]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            S-methyl-L-methionine [CPD:C03172]
COFACTOR    Manganese [CPD:C00034];
            Zinc [CPD:C00038]
COMMENT     Requires Zn2+ or Mn2+
REFERENCE   1  [PMID:6078098]
  AUTHORS   Karr D, Tweto J, Albersheim P.
  TITLE     S-adenosyl methionine: methionine methyl transferase from wheat
            germ.
  JOURNAL   Arch. Biochem. Biophys. 121 (1967) 732-8.
  ORGANISM  Triticum aestivum [GN:etae]
PATHWAY     PATH: map00450  Selenoamino acid metabolism
ORTHOLOGY   KO: K08247  methionine S-methyltransferase
GENES       ATH: AT5G49810(MMT)
            OSA: 4337554
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.12
            ExPASy - ENZYME nomenclature database: 2.1.1.12
            ExplorEnz - The Enzyme Database: 2.1.1.12
            ERGO genome analysis and discovery system: 2.1.1.12
            BRENDA, the Enzyme Database: 2.1.1.12
            CAS: 9027-77-4
///
ENTRY       EC 2.1.1.13                 Enzyme
NAME        methionine synthase;
            5-methyltetrahydrofolate---homocysteine S-methyltransferase;
            5-methyltetrahydrofolate---homocysteine transmethylase;
            N-methyltetrahydrofolate:L-homocysteine methyltransferase;
            N5-methyltetrahydrofolate methyltransferase;
            N5-methyltetrahydrofolate-homocysteine cobalamin methyltransferase;
            N5-methyltetrahydrofolic---homocysteine vitamin B12 transmethylase;
            B12 N5-methyltetrahydrofolate homocysteine methyltransferase;
            methyltetrahydrofolate---homocysteine vitamin B12 methyltransferase;
            tetrahydrofolate methyltransferase;
            tetrahydropteroylglutamate methyltransferase;
            tetrahydropteroylglutamic methyltransferase;
            vitamin B12 methyltransferase;
            cobalamin-dependent methionine synthase;
            methionine synthase (cobalamin-dependent);
            MetH
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     5-methyltetrahydrofolate:L-homocysteine S-methyltransferase
REACTION    5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate +
            L-methionine [RN:R00946]
ALL_REAC    R00946
SUBSTRATE   5-methyltetrahydrofolate [CPD:C00440];
            L-homocysteine [CPD:C00155]
PRODUCT     tetrahydrofolate [CPD:C00101];
            L-methionine [CPD:C00073]
COFACTOR    FAD [CPD:C00016];
            Zinc [CPD:C00038];
            Cobamide [CPD:C00210]
COMMENT     Contains zinc and cobamide. The enzyme becomes inactivated
            occasionally during its cycle by oxidation of Co(I) to Co(II).
            Reactivation by reductive methylation is catalysed by the enzyme
            itself, with S-adenosyl-L-methionine as the methyl donor and a
            reducing system. For the mammalian enzyme, the reducing system
            involves NADPH and EC 1.16.1.8, [methionine synthase] reductase. In
            bacteria, the reducing agent is flavodoxin, and no further catalyst
            is needed (the flavodoxin is kept in the reduced state by NADPH and
            EC 1.18.1.2, ferredoxin---NADP+ reductase). Acts on the
            monoglutamate as well as the triglutamate folate, in contrast with
            EC 2.1.1.14, 5-methyltetrahydropteroyltriglutamate---homocysteine
            S-methyltransferase, which acts only on the triglutamate.
REFERENCE   1  [PMID:5799642]
  AUTHORS   Burton EG, Sakami W.
  TITLE     The formation of methionine from the monoglutamate form of
            methyltetrahydrofolate by higher plants.
  JOURNAL   Biochem. Biophys. Res. Commun. 36 (1969) 228-34.
  ORGANISM  spinach, Escherichia coli [GN:eco]
REFERENCE   2  [PMID:14085561]
  AUTHORS   FOSTER MA, DILWORTH MJ, WOODS DD.
  TITLE     COBALAMIN AND THE SYNTHESIS OF METHIONINE BY ESCHERICHIA COLI.
  JOURNAL   Nature. 201 (1964) 39-42.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:5319972]
  AUTHORS   Guest JR, Friedman S, Foster MA, Tejerina G, Woods DD.
  TITLE     Transfer of the methyl group from N5-methyltetrahydrofolates to
            homocysteine in Escherichia coli.
  JOURNAL   Biochem. J. 92 (1964) 497-504.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:14216440]
  AUTHORS   LOUGHLIN RE, ELFORD HL, BUCHANAN JM.
  TITLE     ENZYMATIC SYNTHESIS OF THE METHYL GROUP OF METHIONINE. VII.
            ISOLATION OF A COBALAMIN-CONTAINING TRANSMETHYLASE
            (5-METHYLTETRAHYDRO-FOLATE-HOMOCYSTEINE) FROM MAMMALIAN LIVER.
  JOURNAL   J. Biol. Chem. 239 (1964) 2888-95.
  ORGANISM  Escherichia coli [GN:eco], Aerobacter aerogenes
REFERENCE   5  [PMID:4946148]
  AUTHORS   Taylor RT.
  TITLE     Escherichia coli B N 5 -methyltetrahydrofolate-homocysteine
            cobalamin methyltransferase: gel-filtration behavior of apoenzyme
            and holoenzymes.
  JOURNAL   Biochim. Biophys. Acta. 242 (1971) 355-64.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:9548919]
  AUTHORS   Jarrett JT, Huang S, Matthews RG.
  TITLE     Methionine synthase exists in two distinct conformations that differ
            in reactivity toward methyltetrahydrofolate, adenosylmethionine, and
            flavodoxin.
  JOURNAL   Biochemistry. 37 (1998) 5372-82.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   7
  AUTHORS   Peariso, K., Goulding, C.W., Huang, S., Matthews, R.G. and
            Penner-Hahn, J.E.
  TITLE     Characterization of the zinc binding site in methionine synthase
            enzymes of Escherichia coli: The role of zinc in the methylation of
            homocysteine.
  JOURNAL   J. Am. Chem. Soc. 120 (1998) 8410-8416.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   8  [PMID:10978155]
  AUTHORS   Hall DA, Jordan-Starck TC, Loo RO, Ludwig ML, Matthews RG.
  TITLE     Interaction of flavodoxin with cobalamin-dependent methionine
            synthase.
  JOURNAL   Biochemistry. 39 (2000) 10711-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   9  [PMID:11731805]
  AUTHORS   Bandarian V, Pattridge KA, Lennon BW, Huddler DP, Matthews RG,
            Ludwig ML.
  TITLE     Domain alternation switches B(12)-dependent methionine synthase to
            the activation conformation.
  JOURNAL   Nat. Struct. Biol. 9 (2002) 53-6.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00271  Methionine metabolism
            PATH: map00670  One carbon pool by folate
ORTHOLOGY   KO: K00548  5-methyltetrahydrofolate--homocysteine methyltransferase
GENES       HSA: 4548(MTR)
            MMU: 238505(Mtr)
            RNO: 81522(Mtr)
            CFA: 479190(MTR)
            BTA: 280869(MTR)
            GGA: 422069(RCJMB04_27p10)
            DRE: 378847(mtr)
            CEL: R03D7.1
            OLU: OSTLU_45056(metH)
            DDI: DDB_0230138
            LMA: LmjF07.0090
            ECO: b4019(metH)
            ECJ: JW3979(metH)
            ECE: Z5610(metH)
            ECS: ECs4937
            ECC: c4976(metH)
            ECI: UTI89_C4577(metH)
            ECP: ECP_4228
            ECV: APECO1_2458(metH)
            ECW: EcE24377A_4563(metH)
            ECX: EcHS_A4255
            STY: STY4405(metH)
            STT: t4115(metH)
            SPT: SPA4026(metH)
            SEC: SC4067(metH)
            STM: STM4188.S(metH)
            YPE: YPO3722(metH)
            YPK: y0020(metH)
            YPM: YP_3084(metH)
            YPA: YPA_0021
            YPN: YPN_0018
            YPP: YPDSF_0177
            YPS: YPTB3653(metH)
            YPI: YpsIP31758_0298(metH)
            SFL: SF4085(metH)
            SFX: S3645(metH)
            SFV: SFV_4090(metH)
            SSN: SSON_4190(metH)
            SBO: SBO_4040(metH)
            SDY: SDY_4322(metH)
            ECA: ECA3987(metH)
            HIQ: CGSHiGG_08850(metH)
            MSU: MS1009(metH)
            XCC: XCC1511(metH2) XCC1512(metH1)
            XCB: XC_2724 XC_2725
            XCV: XCV1602(metH) XCV1603(metH)
            XAC: XAC1559(metH) XAC1560(metH)
            XOO: XOO2073(metH2) XOO2074(metH)
            XOM: XOO_1954(XOO1954) XOO_1955(XOO1955)
            VCH: VC0390(metH)
            VCO: VC0395_A2808(metH)
            VVU: VV1_1423
            VVY: VV2960
            VPA: VP2717
            VFI: VF0337(metH)
            PPR: PBPRA3294(metH)
            PAE: PA1843(metH)
            PAU: PA14_40670(metH)
            PAP: PSPA7_3449(metH)
            PPU: PP_2375(metH)
            PST: PSPTO_2732(metH)
            PSB: Psyr_2464
            PSP: PSPPH_2620(metH)
            PFL: PFL_3662(metH)
            PFO: Pfl_3107
            PEN: PSEEN3382(metH)
            PAR: Psyc_0403(metH)
            PCR: Pcryo_0449
            ACI: ACIAD1045(metH)
            ACB: A1S_0971
            SON: SO_1030(metH)
            SDN: Sden_1115
            SFR: Sfri_0872
            SHE: Shewmr4_0838
            SHM: Shewmr7_3184
            SHN: Shewana3_3282
            CPS: CPS_1101(metH)
            PHA: PSHAa2222
            SDE: Sde_2010
            MAQ: Maqu_1526
            MCA: MCA1545(metH)
            TCX: Tcr_0172
            NOC: Noc_1206
            HHA: Hhal_2154
            HCH: HCH_02542(metH)
            CSA: Csal_1889
            ABO: ABO_1324
            AHA: AHA_0432(metH)
            VOK: COSY_0466(metH)
            CVI: CV_0203 CV_1568(cobL)
            RSO: RSc0294(metHb) RSc0295(metHa)
            REU: Reut_A0118 Reut_A0119
            REH: H16_A0151(metH)
            RME: Rmet_0087 Rmet_0088
            BMV: BMASAVP1_A0249(metH-1) BMASAVP1_A0250(metH-2)
            BML: BMA10299_A1344(metH)
            BMN: BMA10247_3218(metH-1) BMA10247_3219(metH-2)
            BXE: Bxe_A4240 Bxe_A4243
            BVI: Bcep1808_3011 Bcep1808_3012
            BUR: Bcep18194_A6259 Bcep18194_A6260
            BCN: Bcen_2302 Bcen_2303
            BCH: Bcen2424_2916 Bcen2424_2917
            BAM: Bamb_2965 Bamb_2966
            BPS: BPSL0385(metH1) BPSL0386(metH2)
            BPM: BURPS1710b_0594(metH) BURPS1710b_0595
            BPL: BURPS1106A_0433(metH) BURPS1106A_0434(metH)
            BPD: BURPS668_0413(metH) BURPS668_0414(metH)
            BTE: BTH_I0357(metH) BTH_I0358
            PNU: Pnuc_1979 Pnuc_1980
            BPE: BP3594(metH)
            BPA: BPP3983(metH)
            BBR: BB4456(metH)
            RFR: Rfer_0460 Rfer_0466
            POL: Bpro_0172 Bpro_0174
            PNA: Pnap_0117
            AAV: Aave_0174 Aave_0214
            AJS: Ajs_0147
            VEI: Veis_0014 Veis_1195
            MPT: Mpe_A0166 Mpe_A0168
            HAR: HEAR0124(metH)
            MMS: mma_0149
            NEU: NE1623(metH)
            NET: Neut_0500
            NMU: Nmul_A0045
            EBA: ebA3184(metH)
            AZO: azo3726(metH)
            DAR: Daro_0046
            TBD: Tbd_0234
            MFA: Mfla_2509
            WSU: WS1234
            TDN: Tmden_2031
            ABU: Abu_0117(metH)
            NIS: NIS_0549(metH)
            SUN: SUN_1818(metH)
            GSU: GSU2921
            GME: Gmet_0549
            PCA: Pcar_2722
            DVU: DVU1585
            DDE: Dde_2115
            DPS: DP2201 DP2202
            ADE: Adeh_0085
            MXA: MXAN_1971(metH)
            SAT: SYN_00176 SYN_02703
            MLO: mlr1220
            MES: Meso_0328
            PLA: Plav_2403
            SME: SMc03112(metH) SMc04325
            SMD: Smed_1776 Smed_1784
            ATU: Atu2155(metH)
            ATC: AGR_C_3907
            RET: RHE_CH02901(metH)
            RLE: RL3362(metH)
            BME: BMEI1759
            BMF: BAB1_0188
            BMS: BR0188(metH)
            BMB: BruAb1_0184(metH)
            BOV: BOV_0182(metH)
            BJA: bll1418(metH)
            BRA: BRADO0994(metH)
            BBT: BBta_7061(metH)
            RPA: RPA3702(metH)
            RPB: RPB_1764
            RPC: RPC_3735
            RPD: RPD_3541
            RPE: RPE_3773
            NWI: Nwi_0283
            NHA: Nham_0363
            CCR: CC_2137 CC_2138
            SIL: SPO1884
            SIT: TM1040_1186 TM1040_1468 TM1040_1470 TM1040_3617 TM1040_3618
            RSP: RSP_2124 RSP_2768 RSP_3346 RSP_3347
            RSH: Rsph17029_0797 Rsph17029_1410 Rsph17029_2997 Rsph17029_2998
            RSQ: Rsph17025_0707 Rsph17025_1028 Rsph17025_3657
            JAN: Jann_2550
            RDE: RD1_2258(mtbC) RD1_2260 RD1_3057(metH) RD1_3659(metH)
                 RD1_3660(metH)
            PDE: Pden_1935
            MMR: Mmar10_2436 Mmar10_2437
            ZMO: ZMO1745(metH)
            NAR: Saro_3206 Saro_3207
            SAL: Sala_0036 Sala_0037
            SWI: Swit_2399
            ELI: ELI_10080 ELI_10090
            GOX: GOX2074
            GBE: GbCGDNIH1_0151
            RRU: Rru_A1531
            MAG: amb0429
            MGM: Mmc1_3690
            ABA: Acid345_1847 Acid345_1848
            BHA: BH1630(metH)
            BAN: BA4478(metH) BA4479
            BAR: GBAA4478(metH) GBAA4479
            BAA: BA_4925 BA_4926
            BAT: BAS4156 BAS4157
            BCE: BC4250 BC4251
            BCA: BCE_4332(metH) BCE_4333
            BCZ: BCZK4005(metH) BCZK4006(metE)
            BTK: BT9727_3995(metH) BT9727_3996(metE)
            BTL: BALH_3850(metH) BALH_3851(metE)
            BLI: BL01308
            BLD: BLi01192
            BCL: ABC1869
            BPU: BPUM_1026
            GKA: GK0716
            SAB: SAB0307c(metE2)
            LPL: lp_1374(metH)
            STH: STH2500
            CAC: CAC0578(metH)
            CPF: CPF_1670
            CPR: CPR_1406
            CTC: CTC01806 CTC01807
            CNO: NT01CX_2109
            CBO: CBO1623(metH)
            CKL: CKL_0976(metH1) CKL_1762(metH2)
            DSY: DSY1509 DSY3646 DSY3647 DSY4482 DSY4972
            SWO: Swol_1442
            TTE: TTE1803(metH2)
            MTA: Moth_0385 Moth_0387 Moth_1207 Moth_1208 Moth_1316 Moth_1318
                 Moth_2115
            MTU: Rv2124c(metH)
            MTC: MT2183(metH)
            MBO: Mb2148c(metH)
            MBB: BCG_2141c(metH)
            MLE: ML1307(metH)
            MPA: MAP1859c(metH)
            MAV: MAV_2379(metH)
            MSM: MSMEG_4185(metH)
            MMC: Mmcs_3149
            CGL: NCgl1450(cgl1507)
            CGB: cg1701(metH)
            CEF: CE1637
            CDI: DIP1259(metH)
            NFA: nfa31930(metH)
            RHA: RHA1_ro00859(metH)
            SCO: SCO1657(SCI46.02c)
            SMA: SAV6667(metH)
            TFU: Tfu_1825
            FRA: Francci3_0112
            FAL: FRAAL0172(metH)
            SEN: SACE_3898(metH)
            FNU: FN0163
            RBA: RB9857(metH)
            LIL: LB108(metH)
            LIC: LIC20085(metH)
            LBJ: LBJ_4091(metH)
            LBL: LBL_4107(metH)
            SYN: slr0212(metH)
            SYW: SYNW1238(metH)
            SYC: syc0184_c(metH)
            SYF: Synpcc7942_1372
            SYD: Syncc9605_1355
            SYE: Syncc9902_1123
            SYG: sync_1353(metH)
            SYR: SynRCC307_1209(metH)
            SYX: SynWH7803_1277(metH)
            CYA: CYA_2411(metH)
            CYB: CYB_2208(metH)
            TEL: tll1027(metH)
            GVI: gll0477(metH)
            ANA: alr0308
            AVA: Ava_3052
            PMA: Pro0959(metH)
            PMM: PMM0877(metH)
            PMT: PMT0729(metH)
            PMN: PMN2A_0333
            PMB: A9601_09841(metH)
            PMC: P9515_09591(metH)
            PMF: P9303_14891(metH)
            PMG: P9301_09821(metH)
            PMH: P9215_10151
            PME: NATL1_10061(metH)
            TER: Tery_1073
            BTH: BT_0180
            BFR: BF3199
            BFS: BF3039(metH)
            CHU: CHU_1433(metH) CHU_1434(metH)
            GFO: GFO_0332 GFO_0333
            FJO: Fjoh_1510
            CTE: CT1857(metH)
            CCH: Cag_1692
            PLT: Plut_0315
            DRA: DR_0966
            DGE: Dgeo_1336
            TTH: TTC0253
            TTJ: TTHA0618
            TMA: TM0268
            MBU: Mbur_1365
            MSI: Msm_0516
            SMR: Smar_0415
            TPE: Tpen_1212 Tpen_1468
STRUCTURES  PDB: 1BMT  1J6R  1K7Y  1K98  1MSK  1Q7M  1Q7Q  1Q7Z  1Q85  1Q8A  
                 1Q8J  2O2K  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.13
            ExPASy - ENZYME nomenclature database: 2.1.1.13
            ExplorEnz - The Enzyme Database: 2.1.1.13
            ERGO genome analysis and discovery system: 2.1.1.13
            BRENDA, the Enzyme Database: 2.1.1.13
            CAS: 9033-23-2
///
ENTRY       EC 2.1.1.14                 Enzyme
NAME        5-methyltetrahydropteroyltriglutamate---homocysteine
            S-methyltransferase;
            tetrahydropteroyltriglutamate methyltransferase;
            homocysteine methylase;
            methyltransferase, tetrahydropteroylglutamate-homocysteine
            transmethylase;
            methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase;
            cobalamin-independent methionine synthase;
            methionine synthase (cobalamin-independent);
            MetE
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     5-methyltetrahydropteroyltri-L-glutamate:L-homocysteine
            S-methyltransferase
REACTION    5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine =
            tetrahydropteroyltri-L-glutamate + L-methionine [RN:R04405]
ALL_REAC    R04405
SUBSTRATE   5-methyltetrahydropteroyltri-L-glutamate [CPD:C04489];
            L-homocysteine [CPD:C00155]
PRODUCT     tetrahydropteroyltri-L-glutamate [CPD:C04144];
            L-methionine [CPD:C00073]
COFACTOR    Orthophosphate [CPD:C00009];
            Zinc [CPD:C00038]
COMMENT     Requires phosphate and contains zinc. The enzyme from Escherichia
            coli also requires a reducing system. Unlike EC 2.1.1.13, methionine
            synthase, this enzyme does not contain cobalamin.
REFERENCE   1  [PMID:5319972]
  AUTHORS   Guest JR, Friedman S, Foster MA, Tejerina G, Woods DD.
  TITLE     Transfer of the methyl group from N5-methyltetrahydrofolates to
            homocysteine in Escherichia coli.
  JOURNAL   Biochem. J. 92 (1964) 497-504.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4904482]
  AUTHORS   Whitfield CD, Steers EJ Jr, Weisbach H.
  TITLE     Purification and properties of
            5-methyltetrahydropteroyltriglutamate-homocysteine transmethylase.
  JOURNAL   J. Biol. Chem. 245 (1970) 390-401.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:7601135]
  AUTHORS   Eichel J, Gonzalez JC, Hotze M, Matthews RG, Schroder J.
  TITLE     Vitamin-B12-independent methionine synthase from a higher plant
            (Catharanthus roseus). Molecular characterization, regulation,
            heterologous expression, and enzyme properties.
  JOURNAL   Eur. J. Biochem. 230 (1995) 1053-8.
  ORGANISM  Catharanthus roseus
REFERENCE   4  [PMID:8823155]
  AUTHORS   Gonzalez JC, Peariso K, Penner-Hahn JE, Matthews RG.
  TITLE     Cobalamin-independent methionine synthase from Escherichia coli: a
            zinc metalloenzyme.
  JOURNAL   Biochemistry. 35 (1996) 12228-34.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5
  AUTHORS   Peariso, K., Goulding, C.W., Huang, S., Matthews, R.G. and
            Penner-Hahn, J.E.
  TITLE     Characterization of the zinc binding site in methionine synthase
            enzymes of Escherichia coli: The role of zinc in the methylation of
            homocysteine.
  JOURNAL   J. Am. Chem. Soc. 120 (1998) 8410-8416.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K00549  5-methyltetrahydropteroyltriglutamate--homocysteine
                        methyltransferase
GENES       SPU: 760986(LOC760986)
            ATH: AT5G20980(ATMS3)
            OSA: 4352833
            CME: CMJ234C
            SCE: YER091C(MET6)
            AGO: AGOS_ABR212C
            PIC: PICST_78051(MET6)
            CGR: CAGL0I04994g
            SPO: SPAC9.09
            ANI: AN4443.2
            AFM: AFUA_4G07360
            AOR: AO090023000837
            CNE: CNK02310
            DDI: DDB_0230069
            TBR: Tb927.8.2610
            LMA: LmjF31.0010
            ECO: b3829(metE)
            ECJ: JW3805(metE)
            ECE: Z5351(metE)
            ECS: ECs4759
            ECC: c4751(metE)
            ECI: UTI89_C4393(metE)
            ECP: ECP_4023
            ECV: APECO1_2647(metE)
            ECW: EcE24377A_4350(metE)
            ECX: EcHS_A4053
            STY: STY3594(metE)
            STT: t3332(metE)
            SPT: SPA3806(metE)
            SEC: SC3864(metE)
            STM: STM3965(metE)
            YPE: YPO3788(metE)
            YPK: y0442(metE)
            YPM: YP_3261(metE)
            YPA: YPA_0236
            YPN: YPN_0176
            YPP: YPDSF_3405
            YPS: YPTB0248(metE)
            YPI: YpsIP31758_0264(metE)
            SFL: SF3907(metE)
            SFX: S3848(metE)
            SFV: SFV_3669(metE)
            SSN: SSON_4003(metE)
            SBO: SBO_3841(metE)
            SDY: SDY_3914(metE)
            ECA: ECA0181(metE) ECA3126(metE)
            PLU: plu4420(metE)
            BUC: BU030(metE)
            BAS: BUsg031(metE)
            BAB: bbp031(metE)
            BCC: BCc_017(metE)
            SGL: SG0092
            ENT: Ent638_3967
            SPE: Spro_0242
            BFL: Bfl625(metE)
            BPN: BPEN_652(metE)
            HIN: HI1702(metE)
            HIT: NTHI0097
            HIP: CGSHiEE_03570
            HIQ: CGSHiGG_02270
            HSO: HS_0824(metE) HS_1226(metE)
            PMU: PM0420(metE)
            APL: APL_1155(metE)
            XFA: XF2272
            XFT: PD1308(metE)
            XCC: XCC0318(metE)
            XCB: XC_0330
            XCV: XCV0345(metE)
            XAC: XAC0336(metE)
            XOO: XOO4333(metE)
            XOM: XOO_4084(XOO4084)
            VCH: VC1704
            VCO: VC0395_A1308(metE)
            VVU: VV1_2219 VV2_0996
            VVY: VV2135 VVA1491
            VPA: VP1974 VP1991
            VFI: VF1721
            PPR: PBPRA1379(metE)
            PAE: PA1927(metE)
            PAU: PA14_39590(metE)
            PAP: PSPA7_1556(metE)
            PPU: PP_2698(metE)
            PPF: Pput_4499
            PST: PSPTO_4179(metE)
            PSB: Psyr_2855 Psyr_3916
            PSP: PSPPH_3910
            PFL: PFL_2404(metE) PFL_3511
            PFO: Pfl_4545
            PEN: PSEEN2747 PSEEN4639(metE)
            PAR: Psyc_0846(metE)
            ACI: ACIAD3523(metE)
            SON: SO_0818(metE)
            SDN: Sden_0732
            SAZ: Sama_2627
            SBM: Shew185_3640
            SLO: Shew_2986
            SHE: Shewmr4_3299
            SHM: Shewmr7_0654
            SHN: Shewana3_3469
            CPS: CPS_1151(metE)
            PHA: PSHAa1470(metE)
            PAT: Patl_0921
            CBU: CBU_2048(metE)
            CBD: COXBU7E912_2144(metE)
            MCA: MCA2260(metE)
            TCX: Tcr_2184
            NOC: Noc_1739
            AEH: Mlg_2105
            HCH: HCH_01174(metE)
            CSA: Csal_0672
            ABO: ABO_0861(metE)
            AHA: AHA_1956(metE)
            BCI: BCI_0017(metE)
            CRP: CRP_025
            RMA: Rmag_0985
            NME: NMB0944
            NMA: NMA1140(metE)
            NMC: NMC0922(metE)
            NGO: NGO0928
            CVI: CV_3604(metE)
            RSO: RSp0676(metE)
            REU: Reut_B4245
            REH: H16_B1581(metE)
            RME: Rmet_4564 Rmet_5073
            BMA: BMA0467(metE)
            BMV: BMASAVP1_A2616(metE)
            BML: BMA10299_A0988(metE)
            BMN: BMA10247_0159(metE)
            BXE: Bxe_B1250
            BUR: Bcep18194_B0362
            BCN: Bcen_3081
            BCH: Bcen2424_5286
            BPS: BPSL2545(metE)
            BPM: BURPS1710b_3029(metE)
            BPL: BURPS1106A_2985(metE)
            BPD: BURPS668_2923(metE)
            BTE: BTH_I1606(metE)
            BPE: BP2543(metE)
            BPA: BPP2636(metE)
            BBR: BB2079(metE)
            POL: Bpro_3466
            VEI: Veis_4447
            HAR: HEAR2136(metE)
            MMS: mma_0750 mma_1322
            NEU: NE1436(metE)
            NET: Neut_1555
            NMU: Nmul_A2634
            TBD: Tbd_2286
            MFA: Mfla_2571
            HHE: HH0852(metE)
            WSU: WS0269(metE) WS1831(metE)
            TDN: Tmden_0899
            CJE: Cj1201(metE)
            CJR: CJE1335(metE)
            CJJ: CJJ81176_1216(metE)
            CJU: C8J_1145(metE)
            CJD: JJD26997_0528(metE)
            CFF: CFF8240_0877(metE)
            CCV: CCV52592_0342(metE) CCV52592_1324
            CCO: CCC13826_2119
            ABU: Abu_2028(metE)
            NIS: NIS_0886(metE)
            SUN: SUN_0525(metE)
            PCA: Pcar_0442
            DVU: DVU3371(metE)
            DDE: Dde_2328
            MLO: mll6123
            MES: Meso_2701
            PLA: Plav_0606
            ATU: Atu3823(metE)
            ATC: AGR_L_2018
            BJA: blr2068 blr5608(metE)
            BRA: BRADO1871
            BBT: BBta_2188
            RPA: RPA2181 RPA2397(metE)
            RPC: RPC_3508
            RPE: RPE_2301 RPE_3169
            NWI: Nwi_2890
            NHA: Nham_3661
            CCR: CC_0482
            RDE: RD1_3941(metE)
            ZMO: ZMO1000(metE)
            SWI: Swit_4786
            GOX: GOX2206
            GBE: GbCGDNIH1_0783
            ACR: Acry_2208
            RRU: Rru_A1718
            BSU: BG12616(metC)
            BHA: BH0438
            BAN: BA4218(metE)
            BAR: GBAA4218(metE)
            BAA: BA_4680
            BAT: BAS3912
            BCE: BC4003
            BCA: BCE_4053(metE)
            BCZ: BCZK3760(metE)
            BCY: Bcer98_2704
            BTK: BT9727_3744(metE)
            BLI: BL03738(metE)
            BLD: BLi01422(metE)
            BCL: ABC1449(metC)
            BAY: RBAM_013040
            BPU: BPUM_1215
            SAU: SA0344(metE)
            SAV: SAV0356(metE)
            SAM: MW0332(metE)
            SAR: SAR0353(metE)
            SAS: SAS0332
            SAC: SACOL0428(metE)
            SAB: SAB0306c(metE1)
            SAA: SAUSA300_0357(metE)
            SAO: SAOUHSC_00338
            SAJ: SaurJH9_0404
            SAH: SaurJH1_0414
            SEP: SE2382
            SER: SERP0034(metE)
            SHA: SH2638(metE)
            SSP: SSP2416
            LMO: lmo1681
            LMF: LMOf2365_1705(metE)
            LIN: lin1789
            LWE: lwe1699
            LLA: L0100(metE)
            LLC: LACR_1368
            LLM: llmg_1225(metE) llmg_1849(metE2)
            SPN: SP_0585
            SPR: spr0514(metE)
            SPD: SPD_0510(metE)
            SAG: SAG2049(metE)
            SAN: gbs2005
            SAK: SAK_1988(metE)
            SMU: SMU.873(metE)
            STC: str0785(metE)
            STL: stu0785(metE)
            SSA: SSA_0416(metE)
            SGO: SGO_0310(metE)
            LPL: lp_1375(metE)
            LSL: LSL_0129(metE)
            LBU: LBUL_1232
            LCA: LSEI_0625
            CKL: CKL_1763(metE)
            DRM: Dred_1751
            SWO: Swol_0933
            CSC: Csac_0302
            MTU: Rv1133c(metE)
            MTC: MT1165(metE)
            MBO: Mb1164c(metE)
            MBB: BCG_1194c(metE)
            MLE: ML0961(metE)
            MPA: MAP2661(metE)
            MAV: MAV_1262(metE) MAV_3869
            MSM: MSMEG_6638(metE)
            CGL: NCgl1094(cgl1139) NCgl2048(cgl2129)
            CGB: cg1290(metE)
            CEF: CE1209
            CDI: DIP2167(metE)
            CJK: jk0234(metE)
            NFA: nfa52280(metE)
            RHA: RHA1_ro02120(metE1) RHA1_ro04928(metE2)
            SCO: SCO0985(metE)
            SMA: SAV2046(metE)
            TWH: TWT162(metE)
            TWS: TW610(metT)
            CMI: CMM_2054(metE2)
            ART: Arth_2366
            AAU: AAur_1856(metE)
            KRA: Krad_0937
            SEN: SACE_4744(metE) SACE_6349(metE)
            BLO: BL0798(metE)
            BAD: BAD_0756(metE)
            CYA: CYA_0148(metE-1) CYA_0167(metE-2)
            CYB: CYB_1886(metE)
            TEL: tlr1090
            SRU: SRU_1269(metE)
            CHU: CHU_3320(metE)
            AAE: aq_1710(metE)
            TMA: TM1286
            MJA: MJ1473(metE)
            MMP: MMP0401(metE)
            MAC: MA0053 MA3549(metE)
            MBA: Mbar_A1022 Mbar_A1023
            MMA: MM_0461 MM_1352 MM_1353
            MHU: Mhun_2447
            MEM: Memar_2152
            MTH: MTH775
            MSI: Msm_0102
            MKA: MK0667(metE)
            HMA: rrnAC0254(metE) rrnAC0255
            HWA: HQ2236A(metE) HQ2880A(metE) HQ2881A(metE)
            NPH: NP3670A(metE_1) NP3672A(metE_2)
            TAC: Ta0977
            TVO: TVN1123
            PTO: PTO0185 PTO0186
            PAB: PAB0608(metE-like1)
            PFU: PF1269
            TKO: TK1446
            APE: APE_2048
            SSO: SSO0407(metE-2)
            STO: ST0385
            SAI: Saci_0828(metE)
            MSE: Msed_2248
            PAI: PAE3655
STRUCTURES  PDB: 1T7L  1U1H  1U1J  1U1U  1U22  1XDJ  1XPG  1XR2  2NQ5  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.14
            ExPASy - ENZYME nomenclature database: 2.1.1.14
            ExplorEnz - The Enzyme Database: 2.1.1.14
            ERGO genome analysis and discovery system: 2.1.1.14
            BRENDA, the Enzyme Database: 2.1.1.14
            CAS: 9068-29-5
///
ENTRY       EC 2.1.1.15                 Enzyme
NAME        fatty-acid O-methyltransferase;
            fatty acid methyltransferase;
            fatty acid O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:fatty-acid O-methyltransferase
REACTION    S-adenosyl-L-methionine + a fatty acid = S-adenosyl-L-homocysteine +
            a fatty acid methyl ester [RN:R01349]
ALL_REAC    R01349
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            fatty acid [CPD:C00162]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            fatty acid methyl ester [CPD:C03395]
COMMENT     Oleic acid is the most effective fatty acid acceptor.
REFERENCE   1  [PMID:4984625]
  AUTHORS   Akamatsu Y, Law JH.
  TITLE     The enzymatic synthesis of fatty acid methyl esters by carboxyl
            group alkylation.
  JOURNAL   J. Biol. Chem. 245 (1970) 709-13.
  ORGANISM  Mycobacterium phlei
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.15
            ExPASy - ENZYME nomenclature database: 2.1.1.15
            ExplorEnz - The Enzyme Database: 2.1.1.15
            ERGO genome analysis and discovery system: 2.1.1.15
            BRENDA, the Enzyme Database: 2.1.1.15
            CAS: 37256-89-6
///
ENTRY       EC 2.1.1.16                 Enzyme
NAME        methylene-fatty-acyl-phospholipid synthase;
            unsaturated-phospholipid methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:unsaturated-phospholipid methyltransferase
            (methenylating)
REACTION    S-adenosyl-L-methionine + phospholipid olefinic fatty acid =
            S-adenosyl-L-homocysteine + phospholipid methylene fatty acid
            [RN:R03410]
ALL_REAC    R03410
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            phospholipid olefinic fatty acid [CPD:C01229]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            phospholipid methylene fatty acid [CPD:C04215]
COMMENT     The enzyme transfers a methyl group to the 10-position of a
            Delta-olefinic acyl chain in phosphatidylglycerol or
            phosphatidylinositol or, more slowly, phosphatidylethanolamine;
            subsequent proton transfer produces a 10-methylene group (cf. EC
            2.1.1.79 cyclopropane-fatty-acyl-phospholipid synthase).
REFERENCE   1  [PMID:4313604]
  AUTHORS   Akamatsu Y, Law JH.
  TITLE     Enzymatic alkylenation of phospholipid fatty acid chains by extracts
            of Mycobacterium phlei.
  JOURNAL   J. Biol. Chem. 245 (1970) 701-8.
  ORGANISM  Mycobacterium phlei
ORTHOLOGY   KO: K00550  methylene-fatty-acyl-phospholipid synthase
GENES       CME: CMP111C
            SCE: YJR073C(OPI3)
            AGO: AGOS_AFR431C
            PIC: PICST_56448(OPI3)
            CGR: CAGL0F00363g
            SPO: SPBC337.16(cho1)
            ANI: AN1376.2
            AFM: AFUA_1G09050
            AOR: AO090005001620
            UMA: UM05725.1
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.16
            ExPASy - ENZYME nomenclature database: 2.1.1.16
            ExplorEnz - The Enzyme Database: 2.1.1.16
            ERGO genome analysis and discovery system: 2.1.1.16
            BRENDA, the Enzyme Database: 2.1.1.16
            CAS: 37256-90-9
///
ENTRY       EC 2.1.1.17                 Enzyme
NAME        phosphatidylethanolamine N-methyltransferase;
            PEMT;
            LMTase;
            lipid methyl transferase;
            phosphatidylethanolamine methyltransferase;
            phosphatidylethanolamine-N-methylase;
            phosphatidylethanolamine-S-adenosylmethionine methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:phosphatidylethanolamine N-methyltransferase
REACTION    S-adenosyl-L-methionine + phosphatidylethanolamine =
            S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
            [RN:R02056]
ALL_REAC    R02056
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            phosphatidylethanolamine [CPD:C00350]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            phosphatidyl-N-methylethanolamine [CPD:C01241]
REFERENCE   1  [PMID:25437]
  AUTHORS   Hirata F, Viveros OH, Diliberto EJ Jr, Axelrod J.
  TITLE     Identification and properties of two methyltransferases in
            conversion of phosphatidylethanolamine to phosphatidylcholine.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 75 (1978) 1718-21.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:5773456]
  AUTHORS   Morgan TE.
  TITLE     Isolation and characterization of lipid N-methylrtansferase from dog
            lung.
  JOURNAL   Biochim. Biophys. Acta. 178 (1969) 21-34.
  ORGANISM  dog [GN:cfa]
REFERENCE   3  [PMID:438165]
  AUTHORS   Schneider WJ, Vance DE.
  TITLE     Conversion of phosphatidylethanolamine to phosphatidylcholine in rat
            liver. Partial purification and characterization of the enzymatic
            activities.
  JOURNAL   J. Biol. Chem. 254 (1979) 3886-91.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00551  phosphatidylethanolamine N-methyltransferase
GENES       HSA: 10400(PEMT)
            PTR: 454478(PEMT)
            MMU: 18618(Pemt)
            RNO: 25511(Pemt)
            CFA: 479526(PEMT)
            BTA: 360197(PEMT)
            SSC: 397654(PEMT)
            GGA: 416508(PEMT)
            XLA: 447155(MGC85461)
            XTR: 448594(pemt)
            SPU: 581512(LOC581512)
            SCE: YGR157W(CHO2)
            AGO: AGOS_AFR110C
            PIC: PICST_57055(CHO2)
            CGR: CAGL0E03201g
            SPO: SPBC26H8.03(cho2)
            ANI: AN2154.2
            AFM: AFUA_2G15970
            AOR: AO090012000204
            DDI: DDBDRAFT_0168929
            LMA: LmjF31.2290 LmjF31.3120
            LPN: lpg2158(pmtA)
            LPF: lpl2086
            LPP: lpp2097
            MCA: MCA3065
            NOC: Noc_0914
            CSA: Csal_2810
            CVI: CV_4378
            NMU: Nmul_A0349
            EBA: ebA6680(pemT)
            DAR: Daro_3485
            PLA: Plav_2189
            RET: RHE_CH00316 RHE_CH01201
            RLE: RL0333(pmtA) RL1338(pmtA)
            BME: BMEI2000
            BMF: BAB1_2131
            BMS: BR2127(pmtA)
            BOV: BOV_2043(pmtA)
            BJA: bll6634(pmtA) bll6994
            RPA: RPA1307 RPA3970
            RPB: RPB_1620 RPB_4115
            RPC: RPC_0988 RPC_1444
            RPD: RPD_1629 RPD_3961
            RPE: RPE_0347 RPE_1038 RPE_1464
            NWI: Nwi_0604 Nwi_0696
            NHA: Nham_0696
            XAU: Xaut_0403
            SIL: SPOA0294(pmtA)
            SIT: TM1040_3086
            RSP: RSP_0721(pmtA)
            RSH: Rsph17029_2376
            RSQ: Rsph17025_2440
            PDE: Pden_4690
            ZMO: ZMO0776(pmtA)
            GOX: GOX1862
            GBE: GbCGDNIH1_0800 GbCGDNIH1_2260
            ACR: Acry_2168
            AYW: AYWB_415
            SEN: SACE_4353
            RBA: RB2970
            AVA: Ava_2605
            SRU: SRU_2332
            TTH: TTC1366
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.17
            ExPASy - ENZYME nomenclature database: 2.1.1.17
            ExplorEnz - The Enzyme Database: 2.1.1.17
            ERGO genome analysis and discovery system: 2.1.1.17
            BRENDA, the Enzyme Database: 2.1.1.17
            CAS: 37256-91-0
///
ENTRY       EC 2.1.1.18                 Enzyme
NAME        polysaccharide O-methyltransferase;
            polysaccharide methyltransferase;
            acylpolysacharide 6-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:1,4-alpha-D-glucan 6-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 1,4-alpha-D-glucooligosaccharide =
            S-adenosyl-L-homocysteine + oligosaccharide containing
            6-methyl-D-glucose units [RN:R04396]
ALL_REAC    R04396
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            1,4-alpha-D-glucooligosaccharide [CPD:C04099]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            oligosaccharide containing 6-methyl-D-glucose units [CPD:C04725]
REFERENCE   1  [PMID:5503262]
  AUTHORS   Ferguson JA, Ballou CE.
  TITLE     Biosynthesis of a mycobacterial lipopolysaccharide. Properties of
            the polysaccharide methyltransferase.
  JOURNAL   J. Biol. Chem. 245 (1970) 4213-23.
  ORGANISM  Mycobacterium phlei
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.18
            ExPASy - ENZYME nomenclature database: 2.1.1.18
            ExplorEnz - The Enzyme Database: 2.1.1.18
            ERGO genome analysis and discovery system: 2.1.1.18
            BRENDA, the Enzyme Database: 2.1.1.18
            CAS: 37205-56-4
///
ENTRY       EC 2.1.1.19                 Enzyme
NAME        trimethylsulfonium---tetrahydrofolate N-methyltransferase;
            trimethylsulfonium-tetrahydrofolate methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     trimethylsulfonium:tetrahydrofolate N-methyltransferase
REACTION    trimethylsulfonium + tetrahydrofolate = dimethylsulfide +
            5-methyltetrahydrofolate [RN:R02573]
ALL_REAC    R02573
SUBSTRATE   trimethylsulfonium [CPD:C01008];
            tetrahydrofolate [CPD:C00101]
PRODUCT     dimethylsulfide;
            5-methyltetrahydrofolate [CPD:C00440]
REFERENCE   1  [PMID:6023571]
  AUTHORS   Wagner C, Lusty SM Jr, Kung HF, Rogers NL.
  TITLE     Preparation and properties of trimethylsulfonium-tetrahydrofolate
            methyltransferase.
  JOURNAL   J. Biol. Chem. 242 (1967) 1287-93.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00670  One carbon pool by folate
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.19
            ExPASy - ENZYME nomenclature database: 2.1.1.19
            ExplorEnz - The Enzyme Database: 2.1.1.19
            ERGO genome analysis and discovery system: 2.1.1.19
            BRENDA, the Enzyme Database: 2.1.1.19
            CAS: 37256-92-1
///
ENTRY       EC 2.1.1.20                 Enzyme
NAME        glycine N-methyltransferase;
            glycine methyltransferase;
            S-adenosyl-L-methionine:glycine methyltransferase;
            GNMT
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:glycine N-methyltransferase
REACTION    S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine +
            sarcosine [RN:R00367]
ALL_REAC    R00367
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            glycine [CPD:C00037]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            sarcosine [CPD:C00213]
COMMENT     This enzyme is thought to play an important role in the regulation
            of methyl group metabolism in the liver and pancreas by regulating
            the ratio between S-adenosyl-L-methionine and
            S-adenosyl-L-homocysteine. It is inhibited by
            5-methyltetrahydrofolate pentaglutamate [4]. Sarcosine, which has no
            physiological role, is converted back into glycine by the action of
            EC 1.5.99.1, sarcosine dehydrogenase.
REFERENCE   1  [PMID:13971907]
  AUTHORS   BLUMENSTEIN J, WILLIAMS GR.
  TITLE     Glycine methyltransferase.
  JOURNAL   Can. J. Biochem. Physiol. 41 (1963) 201-10.
REFERENCE   2  [PMID:9597750]
  AUTHORS   Ogawa H, Gomi T, Takusagawa F, Fujioka M.
  TITLE     Structure, function and physiological role of glycine
            N-methyltransferase.
  JOURNAL   Int. J. Biochem. Cell. Biol. 30 (1998) 13-26.
  ORGANISM  rat [GN:rno], rabbit
REFERENCE   3  [PMID:10608809]
  AUTHORS   Yeo EJ, Briggs WT, Wagner C.
  TITLE     Inhibition of glycine N-methyltransferase by
            5-methyltetrahydrofolate pentaglutamate.
  JOURNAL   J. Biol. Chem. 274 (1999) 37559-64.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:10833353]
  AUTHORS   Martinov MV, Vitvitsky VM, Mosharov EV, Banerjee R, Ataullakhanov
            FI.
  TITLE     A substrate switch: a new mode of regulation in the methionine
            metabolic pathway.
  JOURNAL   J. Theor. Biol. 204 (2000) 521-32.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:12859184]
  AUTHORS   Takata Y, Huang Y, Komoto J, Yamada T, Konishi K, Ogawa H, Gomi T,
            Fujioka M, Takusagawa F.
  TITLE     Catalytic mechanism of glycine N-methyltransferase.
  JOURNAL   Biochemistry. 42 (2003) 8394-402.
  ORGANISM  rat [GN:rno], rabbit, human [GN:hsa], mouse [GN:mmu], guinea pig,
            cow [GN:bta], pig [GN:ssc], sheep, chicken [GN:gga]
REFERENCE   6  [PMID:15340920]
  AUTHORS   Pakhomova S, Luka Z, Grohmann S, Wagner C, Newcomer ME.
  TITLE     Glycine N-methyltransferases: a comparison of the crystal structures
            and kinetic properties of recombinant human, mouse and rat enzymes.
  JOURNAL   Proteins. 57 (2004) 331-7.
  ORGANISM  rat [GN:rno], , human [GN:hsa], mouse [GN:mmu]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K00552  glycine N-methyltransferase
GENES       HSA: 27232(GNMT)
            PTR: 462703(GNMT)
            MMU: 14711(Gnmt)
            RNO: 25134(Gnmt)
            CFA: 474905(GNMT)
            GGA: 769542(GNMT)
            DRE: 403338(gnmt)
            SPU: 579000(LOC579000)
            DME: Dmel_CG6188
STRUCTURES  PDB: 1BHJ  1D2C  1D2G  1D2H  1KIA  1NBH  1NBI  1R74  1XVA  2AZT  
                 2IDJ  2IDK  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.20
            ExPASy - ENZYME nomenclature database: 2.1.1.20
            ExplorEnz - The Enzyme Database: 2.1.1.20
            ERGO genome analysis and discovery system: 2.1.1.20
            BRENDA, the Enzyme Database: 2.1.1.20
            CAS: 37228-72-1
///
ENTRY       EC 2.1.1.21                 Enzyme
NAME        methylamine---glutamate N-methyltransferase;
            N-methylglutamate synthase;
            methylamine-glutamate methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     methylamine:L-glutamate N-methyltransferase
REACTION    methylamine + L-glutamate = NH3 + N-methyl-L-glutamate [RN:R01586]
ALL_REAC    R01586
SUBSTRATE   methylamine [CPD:C00218];
            L-glutamate [CPD:C00025]
PRODUCT     NH3 [CPD:C00014];
            N-methyl-L-glutamate [CPD:C01046]
REFERENCE   1  [PMID:5905132]
  AUTHORS   Shaw WV, Tsai L, Stadtman ER.
  TITLE     The enzymatic synthesis of N-methylglutamic acid.
  JOURNAL   J. Biol. Chem. 241 (1966) 935-45.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00680  Methane metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.21
            ExPASy - ENZYME nomenclature database: 2.1.1.21
            ExplorEnz - The Enzyme Database: 2.1.1.21
            ERGO genome analysis and discovery system: 2.1.1.21
            BRENDA, the Enzyme Database: 2.1.1.21
            CAS: 9045-32-3
///
ENTRY       EC 2.1.1.22                 Enzyme
NAME        carnosine N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:carnosine N-methyltransferase
REACTION    S-adenosyl-L-methionine + carnosine = S-adenosyl-L-homocysteine +
            anserine [RN:R02144]
ALL_REAC    R02144
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            carnosine [CPD:C00386]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            anserine [CPD:C01262]
REFERENCE   1
  AUTHORS   McManus, I.R.
  TITLE     Enzymatic synthesis of anserine in skeletal muscle by N-methylation
            of carnosine.
  JOURNAL   J. Biol. Chem. 237 (1962) 1207-1211.
  ORGANISM  chicken [GN:gga], rat [GN:rno], rabbit, guinea pig, cat
PATHWAY     PATH: map00340  Histidine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.22
            ExPASy - ENZYME nomenclature database: 2.1.1.22
            ExplorEnz - The Enzyme Database: 2.1.1.22
            ERGO genome analysis and discovery system: 2.1.1.22
            BRENDA, the Enzyme Database: 2.1.1.22
            CAS: 37256-93-2
///
ENTRY       EC 2.1.1.23       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
COMMENT     Deleted entry: protein-arginine N-methyltransferase. Now listed as
            EC 2.1.1.124 [cytochrome c]-arginine N-methyltransferase, EC
            2.1.1.125 histone-arginine N-methyltransferase and EC 2.1.1.126
            [myelin basic protein]-arginine N-methyltransferase. (EC 2.1.1.23
            created 1972, modified 1976, modified 1983, deleted 1999)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.23
            ExPASy - ENZYME nomenclature database: 2.1.1.23
            ExplorEnz - The Enzyme Database: 2.1.1.23
            ERGO genome analysis and discovery system: 2.1.1.23
            BRENDA, the Enzyme Database: 2.1.1.23
///
ENTRY       EC 2.1.1.24       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
COMMENT     Deleted entry: protein-gamma-glutamate O-methyltransferase. Now
            listed as EC 2.1.1.77 protein-L-isoaspartate(D-aspartate)
            O-methyltransferase, EC 2.1.1.80 protein-glutamate
            O-methyltransferase and EC 2.1.1.100 protein-S-isoprenylcysteine
            O-methyltransferase. (EC 2.1.1.24 created 1972, modified 1983,
            modified 1989, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.24
            ExPASy - ENZYME nomenclature database: 2.1.1.24
            ExplorEnz - The Enzyme Database: 2.1.1.24
            ERGO genome analysis and discovery system: 2.1.1.24
            BRENDA, the Enzyme Database: 2.1.1.24
///
ENTRY       EC 2.1.1.25                 Enzyme
NAME        phenol O-methyltransferase;
            PMT
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:phenol O-methyltransferase
REACTION    S-adenosyl-L-methionine + phenol = S-adenosyl-L-homocysteine +
            anisole [RN:R01239]
ALL_REAC    R01239;
            (other) R06524
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            phenol [CPD:C00146]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            anisole [CPD:C01403]
COMMENT     Acts on a wide variety of simple alkyl-, methoxy- and halo-phenols.
REFERENCE   1  [PMID:5657870]
  AUTHORS   Axelrod J, Daly J.
  TITLE     Phenol-O-methyltransferase.
  JOURNAL   Biochim. Biophys. Acta. 159 (1968) 472-8.
  ORGANISM  guinea pig, mouse [GN:mmu], rabbit, rat [GN:rno]
PATHWAY     PATH: map00350  Tyrosine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.25
            ExPASy - ENZYME nomenclature database: 2.1.1.25
            ExplorEnz - The Enzyme Database: 2.1.1.25
            ERGO genome analysis and discovery system: 2.1.1.25
            BRENDA, the Enzyme Database: 2.1.1.25
            CAS: 37256-94-3
///
ENTRY       EC 2.1.1.26                 Enzyme
NAME        iodophenol O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:2-iodophenol O-methyltransferase
REACTION    S-adenosyl-L-methionine + 2-iodophenol = S-adenosyl-L-homocysteine +
            2-iodophenol methyl ether [RN:R03746]
ALL_REAC    R03746
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            2-iodophenol [CPD:C01874]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            2-iodophenol methyl ether [CPD:C03575]
REFERENCE   1
  AUTHORS   Tomita, K., Cha, C.-J. and Lardy, H.A.
  TITLE     Enzymic O-methylation of iodinated phenols and thyroid hormones.
  JOURNAL   J. Biol. Chem. 239 (1964) 1202-1207.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.26
            ExPASy - ENZYME nomenclature database: 2.1.1.26
            ExplorEnz - The Enzyme Database: 2.1.1.26
            ERGO genome analysis and discovery system: 2.1.1.26
            BRENDA, the Enzyme Database: 2.1.1.26
            CAS: 37256-95-4
///
ENTRY       EC 2.1.1.27                 Enzyme
NAME        tyramine N-methyltransferase;
            DIB O-methyltransferase (3,5-diiodo-4-hydroxy-benzoic acid);
            S-adenosyl-methionine:tyramine N-methyltransferase;
            tyramine methylpherase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:tyramine N-methyltransferase
REACTION    S-adenosyl-L-methionine + tyramine = S-adenosyl-L-homocysteine +
            N-methyltyramine [RN:R02384]
ALL_REAC    R02384
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            tyramine [CPD:C00483]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            N-methyltyramine [CPD:C02442]
COMMENT     Has some activity on phenylethylamine analogues.
REFERENCE   1
  AUTHORS   Mann, J.D. and Mudd, S.H.
  TITLE     Alkaloids and plant metabolism. IV. The tyramine methylpherase of
            barley roots.
  JOURNAL   J. Biol. Chem. 238 (1963) 381-385.
  ORGANISM  Hordeum vulgare [GN:ehvu]
PATHWAY     PATH: map00350  Tyrosine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.27
            ExPASy - ENZYME nomenclature database: 2.1.1.27
            ExplorEnz - The Enzyme Database: 2.1.1.27
            ERGO genome analysis and discovery system: 2.1.1.27
            BRENDA, the Enzyme Database: 2.1.1.27
            CAS: 37256-96-5
///
ENTRY       EC 2.1.1.28                 Enzyme
NAME        phenylethanolamine N-methyltransferase;
            noradrenaline N-methyltransferase;
            noradrenalin N-methyltransferase;
            norepinephrine methyltransferase;
            norepinephrine N-methyltransferase;
            phenethanolamine methyltransferase;
            phenethanolamine N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:phenylethanolamine N-methyltransferase
REACTION    S-adenosyl-L-methionine + phenylethanolamine =
            S-adenosyl-L-homocysteine + N-methylphenylethanolamine [RN:R04033]
ALL_REAC    R04033;
            (other) R02533
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            phenylethanolamine [CPD:C02735]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            N-methylphenylethanolamine [CPD:C03711]
COMMENT     Acts on various phenylethanolamines; converts noradrenaline into
            adrenaline.
REFERENCE   1  [PMID:13863458]
  AUTHORS   AXELROD J.
  TITLE     Purification and properties of phenylethanolamine-N-methyl
            transferase.
  JOURNAL   J. Biol. Chem. 237 (1962) 1657-60.
  ORGANISM  monkey
REFERENCE   2  [PMID:5412063]
  AUTHORS   Connett RJ, Kirshner N.
  TITLE     Purification and properties of bovine phenylethanolamine
            N-methyltransferase.
  JOURNAL   J. Biol. Chem. 245 (1970) 329-34.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00350  Tyrosine metabolism
ORTHOLOGY   KO: K00553  phenylethanolamine N-methyltransferase
GENES       HSA: 5409(PNMT)
            MMU: 18948(Pnmt)
            CFA: 491023(PNMT)
            BTA: 281413(PNMT)
            GGA: 776803(PNMT)
STRUCTURES  PDB: 1HNN  1N7I  1N7J  1YZ3  2AN3  2AN4  2AN5  2G70  2G71  2G72  
                 2G8N  2OBF  2ONY  2ONZ  2OPB  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.28
            ExPASy - ENZYME nomenclature database: 2.1.1.28
            ExplorEnz - The Enzyme Database: 2.1.1.28
            ERGO genome analysis and discovery system: 2.1.1.28
            BRENDA, the Enzyme Database: 2.1.1.28
            CAS: 9037-68-7
///
ENTRY       EC 2.1.1.29                 Enzyme
NAME        tRNA (cytosine-5-)-methyltransferase;
            transfer ribonucleate cytosine 5-methyltransferase;
            transfer RNA cytosine 5-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:tRNA (cytosine-5-)-methyltransferase
REACTION    S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA
            containing 5-methylcytosine [RN:R00595]
ALL_REAC    R00595
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            tRNA [CPD:C00066]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            tRNA containing 5-methylcytosine [CPD:C04155]
REFERENCE   1  [PMID:69267419]
  AUTHORS   Bjork GR, Svensson I.
  TITLE     Studies on microbial RNA. Fractionation of tRNA methylases from
            Saccharomyces cerevisiae.
  JOURNAL   Eur. J. Biochem. 9 (1969) 207-15.
REFERENCE   2  [PMID:14245404]
  AUTHORS   HURWITZ J, GOLD M, ANDERS M.
  TITLE     THE ENZYMATIC METHYLATION OF RIBONUCLEIC ACID AND DEOXYRIBONUCLEIC
            ACID. 3. PURIFICATION OF SOLUBLE RIBONUCLEIC ACID-METHYLATING
            ENZYMES.
  JOURNAL   J. Biol. Chem. 239 (1964) 3462-73.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:7372600]
  AUTHORS   Keith JM, Winters EM, Moss B.
  TITLE     Purification and characterization of a HeLa cell transfer
            RNA(cytosine-5-)-methyltransferase.
  JOURNAL   J. Biol. Chem. 255 (1980) 4636-44.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.29
            ExPASy - ENZYME nomenclature database: 2.1.1.29
            ExplorEnz - The Enzyme Database: 2.1.1.29
            ERGO genome analysis and discovery system: 2.1.1.29
            BRENDA, the Enzyme Database: 2.1.1.29
            CAS: 37256-97-6
///
ENTRY       EC 2.1.1.30       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
COMMENT     Deleted entry: tRNA (purine-2- or -6-)-methyltransferase. Reactions
            previously described are due to EC 2.1.1.32 tRNA
            (guanine-N2-)-methyltransferase. (EC 2.1.1.30 created 1972, deleted
            1981)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.30
            ExPASy - ENZYME nomenclature database: 2.1.1.30
            ExplorEnz - The Enzyme Database: 2.1.1.30
            ERGO genome analysis and discovery system: 2.1.1.30
            BRENDA, the Enzyme Database: 2.1.1.30
///
ENTRY       EC 2.1.1.31                 Enzyme
NAME        tRNA (guanine-N1-)-methyltransferase;
            transfer ribonucleate guanine 1-methyltransferase;
            tRNA guanine 1-methyltransferase;
            S-adenosyl-L-methionine:tRNA (guanine-1-N-)-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:tRNA (guanine-N1-)-methyltransferase
REACTION    S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA
            containing N1-methylguanine [RN:R00597]
ALL_REAC    R00597
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            tRNA [CPD:C00066]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            tRNA containing N1-methylguanine [CPD:C04157]
REFERENCE   1  [PMID:69267419]
  AUTHORS   Bjork GR, Svensson I.
  TITLE     Studies on microbial RNA. Fractionation of tRNA methylases from
            Saccharomyces cerevisiae.
  JOURNAL   Eur. J. Biochem. 9 (1969) 207-15.
REFERENCE   2  [PMID:629973]
  AUTHORS   Glick JM, Averyhart VM, Leboy PS.
  TITLE     Purification and characterization of two
            tRNA-(guanine)-methyltransferases from rat liver.
  JOURNAL   Biochim. Biophys. Acta. 518 (1978) 158-71.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:14245404]
  AUTHORS   HURWITZ J, GOLD M, ANDERS M.
  TITLE     THE ENZYMATIC METHYLATION OF RIBONUCLEIC ACID AND DEOXYRIBONUCLEIC
            ACID. 3. PURIFICATION OF SOLUBLE RIBONUCLEIC ACID-METHYLATING
            ENZYMES.
  JOURNAL   J. Biol. Chem. 239 (1964) 3462-73.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:1096087]
  AUTHORS   Smolar N, Hellman U, Svensson I.
  TITLE     Two transfer RNA (1-methylguanine) methylases from yeast.
  JOURNAL   Nucleic. Acids. Res. 2 (1975) 993-1004.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], Escherichia coli [GN:eco]
ORTHOLOGY   KO: K00554  tRNA (guanine-N1-)-methyltransferase
GENES       ECO: b2607(trmD)
            ECJ: JW2588(trmD)
            ECE: Z3901(trmD)
            ECS: ECs3470
            ECC: c3128(trmD)
            ECI: UTI89_C2940(trmD)
            ECP: ECP_2608
            ECV: APECO1_3926(trmD) APECO1_39262(trmD)
            ECW: EcE24377A_2891(trmD)
            ECX: EcHS_A2766(trmD)
            STY: STY2861(trmD)
            STT: t2629(trmD)
            SPT: SPA2533(trmD)
            SEC: SC2675(trmD)
            STM: STM2674(trmD)
            YPE: YPO3293(trmD)
            YPK: y0896(trmD)
            YPM: YP_0393(trmD)
            YPA: YPA_2851
            YPN: YPN_0805
            YPP: YPDSF_3068
            YPS: YPTB0836(trmD)
            YPI: YpsIP31758_3226(trmD)
            YEN: YE0845(trmD)
            SFL: SF2667(trmD)
            SFX: S2844(trmD)
            SFV: SFV_2863(trmD)
            SSN: SSON_2764(trmD)
            SBO: SBO_2743(trmD)
            SDY: SDY_2781(trmD)
            ECA: ECA3357(trmD)
            PLU: plu1259(trmD)
            BUC: BU396(trmD)
            BAS: BUsg383(trmD)
            BAB: bbp359(trmD)
            BCC: BCc_248(trmD)
            SGL: SG0548
            ENT: Ent638_3088
            SPE: Spro_0854
            BFL: Bfl175(trmD)
            BPN: BPEN_181(trmD)
            HIN: HI0202(trmD)
            HIT: NTHI0299(trmD)
            HDU: HD1947(trmD)
            HSO: HS_0295(trmD)
            PMU: PM1297(trmD)
            MSU: MS0442(trmD)
            APL: APL_1788(trmD)
            ASU: Asuc_0518
            XFA: XF0109
            XFT: PD0083(trmD)
            XCC: XCC1201(trmD)
            XCB: XC_3041
            XCV: XCV1344(trmD)
            XAC: XAC1294(trmD)
            XOO: XOO1327(trmD)
            XOM: XOO_1221(XOO1221)
            VCH: VC0563
            VCO: VC0395_A0097(trmD)
            VVU: VV1_1617
            VVY: VV2786
            VPA: VP2531
            VFI: VF0551(trmD)
            PPR: PBPRA3039(trmD)
            PAE: PA3743(trmD)
            PAU: PA14_15990(trmD)
            PAP: PSPA7_1376(trmD)
            PPU: PP_1464(trmD)
            PPF: Pput_4257
            PST: PSPTO_1475(trmD)
            PSB: Psyr_1284(trmD)
            PSP: PSPPH_1356(trmD)
            PFL: PFL_1096(trmD)
            PFO: Pfl_1021
            PEN: PSEEN4258(trmD)
            PMY: Pmen_3399
            PAR: Psyc_2017(trmD)
            PCR: Pcryo_2320
            PRW: PsycPRwf_0202
            ACI: ACIAD3311(trmD)
            SON: SO_1359(trmD)
            SDN: Sden_2752
            SFR: Sfri_2918
            SAZ: Sama_0891
            SBL: Sbal_1212
            SBM: Shew185_1256
            SLO: Shew_1065
            SPC: Sputcn32_1170
            SSE: Ssed_1161
            SPL: Spea_1051
            SHE: Shewmr4_2836
            SHM: Shewmr7_2918
            SHN: Shewana3_3015
            SHW: Sputw3181_2994
            ILO: IL1724(trmD)
            CPS: CPS_4067(trmD)
            PHA: PSHAa0946(trmD)
            PAT: Patl_1579
            SDE: Sde_1205
            PIN: Ping_3365
            MAQ: Maqu_2278
            CBU: CBU_0443(trmD)
            CBD: COXBU7E912_1631(trmD)
            LPN: lpg0396(trmD)
            LPF: lpl0440(trmD)
            LPP: lpp0464(trmD)
            MCA: MCA0394(trmD)
            FTU: FTT0152(trmD)
            FTF: FTF0152(trmD)
            FTW: FTW_0242(trmD)
            FTL: FTL_1736
            FTH: FTH_1675(trmD)
            FTA: FTA_1839(trmD)
            FTN: FTN_1560(trmD)
            TCX: Tcr_0649
            NOC: Noc_2258
            AEH: Mlg_0886
            HHA: Hhal_0528
            HCH: HCH_01774(trmD)
            CSA: Csal_3014
            ABO: ABO_0800(trmD)
            MMW: Mmwyl1_3768
            AHA: AHA_0668(trmD)
            DNO: DNO_1009(trmD)
            BCI: BCI_0196(trmD)
            RMA: Rmag_0275
            VOK: COSY_0261(trmD)
            NME: NMB0590
            NMA: NMA0793(trmD)
            NMC: NMC0532(trmD)
            NGO: NGO0172
            CVI: CV_3673(trmD)
            RSO: RSc0935(trmB)
            REU: Reut_A2538(trmD)
            REH: H16_A0896(trmD)
            RME: Rmet_0750
            BMA: BMA0401(trmD)
            BMV: BMASAVP1_A2543(trmD)
            BML: BMA10299_A0917(trmD)
            BMN: BMA10247_0230(trmD)
            BXE: Bxe_A1008
            BVI: Bcep1808_0991
            BUR: Bcep18194_A4185(trmD)
            BCN: Bcen_0592
            BCH: Bcen2424_1071
            BAM: Bamb_0947
            BPS: BPSL2490(trmD)
            BPM: BURPS1710b_2966(trmD)
            BPL: BURPS1106A_2917(trmD)
            BPD: BURPS668_2857(trmD)
            BTE: BTH_I1663(trmD)
            PNU: Pnuc_0519
            BPE: BP1841(trmD)
            BPA: BPP2865(trmD)
            BBR: BB3186(trmD)
            RFR: Rfer_1404
            POL: Bpro_1692
            PNA: Pnap_1463
            AAV: Aave_1886
            AJS: Ajs_3353
            VEI: Veis_3941
            MPT: Mpe_A1106
            HAR: HEAR0625(trmD)
            MMS: mma_0593(trmD)
            NEU: NE1673(trmB)
            NET: Neut_0443
            NMU: Nmul_A0571
            EBA: ebA7168(trmD)
            AZO: azo2900(trmD)
            DAR: Daro_3064
            TBD: Tbd_2375
            MFA: Mfla_2332
            HPY: HP1148(trmD)
            HPA: HPAG1_1087
            HHE: HH0936(trmD)
            HAC: Hac_1315(trmD)
            WSU: WS0551(trmD)
            TDN: Tmden_0454
            CJE: Cj0713(trmD)
            CJR: CJE0813(trmD)
            CJJ: CJJ81176_0736(trmD)
            CJU: C8J_0680(trmD)
            CJD: JJD26997_1293(trmD)
            CFF: CFF8240_1035(trmD)
            CCV: CCV52592_0679(trmD)
            CHA: CHAB381_0560(trmD)
            CCO: CCC13826_1430(trmD) CCC13826_1959
            ABU: Abu_2026(trmD)
            NIS: NIS_1501(trmD)
            SUN: SUN_0371(trmD)
            GSU: GSU0646(trmD)
            GME: Gmet_2868
            GUR: Gura_3760
            PCA: Pcar_2221
            PPD: Ppro_1095
            DVU: DVU0836(trmD)
            DVL: Dvul_2145
            DDE: Dde_1096
            LIP: LI0220(trmD)
            BBA: Bd2119(trmD)
            DPS: DP2803
            ADE: Adeh_1913
            AFW: Anae109_1944
            MXA: MXAN_3548(trmD)
            SAT: SYN_00768
            SFU: Sfum_3000 Sfum_3042
            RPR: RP111(trmD)
            RTY: RT0025(trmD)
            RCO: RC0151(trmD)
            RFE: RF_0099(trmD)
            RBE: RBE_1217(trmD)
            RAK: A1C_00835(trmD)
            RBO: A1I_01150(trmD)
            RCM: A1E_00560(trmD)
            RRI: A1G_00865(trmD)
            OTS: OTBS_0397(trmD)
            WOL: WD1022(trmD)
            WBM: Wbm0228
            AMA: AM1270(trmD)
            APH: APH_1267(trmD)
            ERU: Erum8860(trmD)
            ERW: ERWE_CDS_09370(trmD)
            ERG: ERGA_CDS_09280(trmD)
            ECN: Ecaj_0931
            ECH: ECH_0003(trmD)
            NSE: NSE_0896(trmD)
            PUB: SAR11_0254(trmD)
            MLO: mll4287
            MES: Meso_3444
            PLA: Plav_1421
            SME: SMc03861(trmD)
            SMD: Smed_3099
            ATU: Atu2701(trmD)
            ATC: AGR_C_4898
            RET: RHE_CH03961(trmD)
            RLE: RL4551(trmD)
            BME: BMEI0149
            BMF: BAB1_1914(trmD)
            BMS: BR1914(trmD)
            BMB: BruAb1_1890(trmD)
            BOV: BOV_1842(trmD)
            OAN: Oant_0944
            BJA: blr0486(trmD)
            BRA: BRADO0376(trmD)
            BBT: BBta_0365(trmD)
            RPA: RPA0242(trmD)
            RPB: RPB_0350
            RPC: RPC_0224
            RPD: RPD_0507
            RPE: RPE_0330
            NWI: Nwi_2782
            NHA: Nham_3581
            BHE: BH15820(trmD)
            BQU: BQ12740(trmD)
            BBK: BARBAKC583_0086(trmD)
            XAU: Xaut_2511
            CCR: CC_0198
            SIL: SPO3259(trmD)
            SIT: TM1040_2611
            RSP: RSP_1045(trmD)
            RSH: Rsph17029_2706
            RSQ: Rsph17025_0184
            JAN: Jann_0744
            RDE: RD1_1307(trmD)
            PDE: Pden_3883
            MMR: Mmar10_2898
            HNE: HNE_0045(trmD)
            ZMO: ZMO1078(trmD)
            NAR: Saro_1407
            SAL: Sala_2720
            SWI: Swit_2662
            ELI: ELI_07450
            GOX: GOX0195
            GBE: GbCGDNIH1_1683
            ACR: Acry_2151
            RRU: Rru_A1187
            MAG: amb4065
            MGM: Mmc1_0506
            ABA: Acid345_2875
            SUS: Acid_2569
            BSU: BG12687(trmD)
            BHA: BH2479(trmD)
            BAN: BA3979(trmD)
            BAR: GBAA3979(trmD)
            BAA: BA_4450
            BAT: BAS3692
            BCE: BC3839(trmD)
            BCA: BCE_3883(trmD)
            BCZ: BCZK3600(trmD)
            BCY: Bcer98_2493
            BTK: BT9727_3582(trmD)
            BLI: BL01291(trmD)
            BLD: BLi01823(trmD)
            BCL: ABC2289(trmD)
            BAY: RBAM_015860(trmD)
            BPU: BPUM_1501(trmD)
            OIH: OB1536(trmD)
            GKA: GK1201
            SAU: SA1083(trmD)
            SAV: SAV1240(trmD)
            SAM: MW1123(trmD)
            SAR: SAR1216(trmD)
            SAS: SAS1174
            SAC: SACOL1256(trmD)
            SAB: SAB1104(trmD)
            SAA: SAUSA300_1133(trmD)
            SAO: SAOUHSC_01210
            SAJ: SaurJH9_1299
            SAH: SaurJH1_1324
            SEP: SE0915
            SER: SERP0806(trmD)
            SHA: SH1674(trmD)
            SSP: SSP1527
            LMO: lmo1792(trmD)
            LMF: LMOf2365_1819(trmD)
            LIN: lin1906(trmD)
            LWE: lwe1811(trmD)
            LLA: L6128(trmD)
            LLC: LACR_1658
            LLM: llmg_0937(trmD)
            SPY: SPy_0849(trmD)
            SPZ: M5005_Spy_0656(trmD)
            SPM: spyM18_0908(trmD)
            SPG: SpyM3_0574(trmD)
            SPS: SPs1280
            SPH: MGAS10270_Spy0715(trmD)
            SPI: MGAS10750_Spy0747(trmD)
            SPJ: MGAS2096_Spy0725(trmD) MGAS2096_Spy0726
            SPK: MGAS9429_Spy0711(trmD)
            SPF: SpyM51152(trmD)
            SPA: M6_Spy0675(trmD)
            SPB: M28_Spy0637(trmD)
            SPN: SP_0779
            SPR: spr0687(trmD)
            SPD: SPD_0679(trmD)
            SAG: SAG1354(trmD)
            SAN: gbs1424
            SAK: SAK_1385(trmD)
            SMU: SMU.868(trmD)
            STC: str1418(trmD)
            STL: stu1418(trmD)
            SSA: SSA_1302(trmD)
            SGO: SGO_1315(trmD)
            LPL: lp_1639(trmD)
            LJO: LJ1513
            LAC: LBA1287
            LSA: LSA0718(trmD)
            LSL: LSL_0633(trmD)
            LDB: Ldb1369(trmD)
            LBU: LBUL_1279
            LBR: LVIS_0940
            LCA: LSEI_1598
            LRE: Lreu_1151
            EFA: EF1899(trmD)
            OOE: OEOE_0801
            STH: STH1470
            CAC: CAC1758(trmD)
            CPE: CPE1709(trmD)
            CPF: CPF_1963(trmD)
            CPR: CPR_1681(trmD)
            CTC: CTC01251(trmD)
            CNO: NT01CX_2209(trmD)
            CTH: Cthe_0766
            CDF: CD1256(trmD)
            CBA: CLB_2309(trmD)
            CBH: CLC_2293(trmD)
            CBF: CLI_2501(trmD)
            CBE: Cbei_1179
            AMT: Amet_2743
            CHY: CHY_1430(trmD)
            DSY: DSY2594
            DRM: Dred_2051
            SWO: Swol_1493
            CSC: Csac_2154
            TTE: TTE1458(trmD)
            MTA: Moth_0970
            MGE: MG_445(trmD)
            MPN: MPN659(trmD)
            MPU: MYPU_4680(trmD)
            MPE: MYPE1020(trmD)
            MGA: MGA_0439(trmD)
            MMY: MSC_0427(trmD)
            MMO: MMOB4290(trmD)
            MHY: mhp095(trmD)
            MHJ: MHJ_0277(trmD)
            MHP: MHP7448_0285(trmD)
            MSY: MS53_0011(trmD)
            MCP: MCAP_0545(trmD)
            UUR: UU567(trmD)
            POY: PAM471(trmD)
            AYW: AYWB_307(trmD)
            MFL: Mfl540
            MTU: Rv2906c(trmD)
            MTC: MT2974(trmD)
            MBO: Mb2930c(trmD)
            MBB: BCG_2927c(trmD)
            MLE: ML1615(trmD)
            MPA: MAP2974c(trmD)
            MAV: MAV_3760(trmD)
            MSM: MSMEG_2438(trmD)
            MVA: Mvan_2190
            MGI: Mflv_4172
            MMC: Mmcs_1968
            MKM: Mkms_2014
            MJL: Mjls_1948
            CGL: NCgl1972(trmD)
            CGB: cg2249(trmD)
            CEF: CE1956
            CDI: DIP1530(trmD)
            CJK: jk1190(trmD)
            NFA: nfa41540(trmD)
            RHA: RHA1_ro06538(trmD)
            SCO: SCO5594(trmD)
            SMA: SAV2641(trmD)
            TWH: TWT458(trmD)
            TWS: TW307(trmD)
            LXX: Lxx14850(trmD)
            CMI: CMM_1370(trmD)
            ART: Arth_2480
            AAU: AAur_2449(trmD)
            PAC: PPA1440
            NCA: Noca_3256
            TFU: Tfu_0665
            FRA: Francci3_3591
            FAL: FRAAL5790(trmD)
            ACE: Acel_1558
            KRA: Krad_1401
            SEN: SACE_6050(trmD)
            STP: Strop_1308
            BLO: BL0327(trmD)
            BAD: BAD_0206(trmD)
            RXY: Rxyl_1391
            FNU: FN0283
            RBA: RB12823(trmD)
            CTR: CT027(trmD)
            CTA: CTA_0029(trmD)
            CMU: TC0296
            CPN: CPn0117(trmD)
            CPA: CP0656
            CPJ: CPj0117(trmD)
            CPT: CpB0118
            CCA: CCA00656(trmD)
            CAB: CAB627(trmD)
            CFE: CF0355(rrm5)
            PCU: pc0656(trmD)
            BBU: BB0698(trmD)
            BGA: BG0721(trmD)
            BAF: BAPKO_0742(trmD)
            TPA: TP0908(trmD)
            TDE: TDE0884(trmD)
            LIL: LA2388(trmD)
            LIC: LIC11558(trmD)
            LBJ: LBJ_1433(trmD)
            LBL: LBL_1657(trmD)
            SYN: sll1198(trmD)
            SYW: SYNW1610
            SYC: syc1863_c(trmD)
            SYF: Synpcc7942_2235
            SYD: Syncc9605_0890
            SYE: Syncc9902_1508
            SYG: sync_0775(trmD)
            SYR: SynRCC307_1727(trmD)
            SYX: SynWH7803_1724(trmD)
            CYA: CYA_1775(trmD)
            CYB: CYB_1217(trmD)
            TEL: tlr1611
            GVI: glr0889
            ANA: alr3882
            AVA: Ava_1812(trmD)
            PMA: Pro1354(trmD)
            PMM: PMM1280
            PMT: PMT0356
            PMN: PMN2A_0847
            PMI: PMT9312_1376
            PMB: A9601_14791(trmD)
            PMC: P9515_14411(trmD)
            PMF: P9303_19461(trmD)
            PMG: P9301_14651(trmD)
            PMH: P9215_15081(trmD)
            PME: NATL1_17001(trmD)
            TER: Tery_1962
            BTH: BT_0893
            BFR: BF2402
            BFS: BF2484(trmD)
            PGI: PG2035(trmD)
            SRU: SRU_1627(trmD)
            CHU: CHU_0119(trmD)
            GFO: GFO_0620(trmD)
            FJO: Fjoh_2184
            FPS: FP1874(trmD)
            CTE: CT1164(trmD)
            CCH: Cag_0802(trmD)
            CPH: Cpha266_1522
            PVI: Cvib_0933
            PLT: Plut_0968(trmD)
            DET: DET0339(trmD)
            DEH: cbdb_A279(trmD)
            DEB: DehaBAV1_0318
            RRS: RoseRS_3686
            RCA: Rcas_1332
            DRA: DR_2011
            DGE: Dgeo_1486
            TTH: TTC0670
            TTJ: TTHA1032
            AAE: aq_1489(trmD)
            TMA: TM1569
            TPT: Tpet_1223
            TME: Tmel_1802
            FNO: Fnod_0649
STRUCTURES  PDB: 1OY5  1P9P  1UAJ  1UAK  1UAL  1UAM  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.31
            ExPASy - ENZYME nomenclature database: 2.1.1.31
            ExplorEnz - The Enzyme Database: 2.1.1.31
            ERGO genome analysis and discovery system: 2.1.1.31
            BRENDA, the Enzyme Database: 2.1.1.31
            CAS: 37256-99-8
///
ENTRY       EC 2.1.1.32                 Enzyme
NAME        tRNA (guanine-N2-)-methyltransferase;
            transfer ribonucleate guanine 2-methyltransferase;
            transfer ribonucleate guanine N2-methyltransferase;
            transfer RNA guanine 2-methyltransferase;
            guanine-N2-methylase;
            S-adenosyl-L-methionine:tRNA (guanine-2-N-)-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:tRNA (guanine-N2-)-methyltransferase
REACTION    S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA
            containing N2-methylguanine [RN:R00598]
ALL_REAC    R00598
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            tRNA [CPD:C00066]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            tRNA containing N2-methylguanine [CPD:C04158]
COMMENT     In eukaryotic tRNAs, two N2-guanine methylations occur, at the
            N2-methylguanine at position 10 and the N2-methylguanine at position
            29.
REFERENCE   1  [PMID:4208689]
  AUTHORS   Agris PF, Spremulli LL, Brown GM.
  TITLE     tRNA methylases from HeLa cells: purification and properties of an
            adenine-1-methylase and a guanine-N2-methylase.
  JOURNAL   Arch. Biochem. Biophys. 162 (1974) 38-47.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:4921283]
  AUTHORS   Baguley BC, Staehelin M.
  TITLE     The specificity of transfer ribonucleic acid methylases from rat
            liver.
  JOURNAL   Biochemistry. 7 (1968) 45-50.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:69267419]
  AUTHORS   Bjork GR, Svensson I.
  TITLE     Studies on microbial RNA. Fractionation of tRNA methylases from
            Saccharomyces cerevisiae.
  JOURNAL   Eur. J. Biochem. 9 (1969) 207-15.
REFERENCE   4  [PMID:629973]
  AUTHORS   Glick JM, Averyhart VM, Leboy PS.
  TITLE     Purification and characterization of two
            tRNA-(guanine)-methyltransferases from rat liver.
  JOURNAL   Biochim. Biophys. Acta. 518 (1978) 158-71.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:1208211]
  AUTHORS   Glick JM, Ross S, Leboy PS.
  TITLE     S-adenosylhomocysteine inhibition of three purified tRNA
            methyltransferases from rat liver.
  JOURNAL   Nucleic. Acids. Res. 2 (1975) 1639-51.
  ORGANISM  rat [GN:rno]
REFERENCE   6  [PMID:19056]
  AUTHORS   Izzo P, Gantt R.
  TITLE     Partial purification and characterization of an N2-guanine RNA
            methyltransferase from chicken embryos.
  JOURNAL   Biochemistry. 16 (1977) 3576-81.
  ORGANISM  chicken [GN:gga]
REFERENCE   7
  AUTHORS   Krauss, J. and Stahelin, M.
  TITLE     N2-Guanine specific transfer RNA methyltransferase I from rat liver
            and leukemic rat spleen.
  JOURNAL   Nucleic Acids Res. 1 (1974) 1455-1478.
  ORGANISM  rat [GN:rno]
REFERENCE   8
  AUTHORS   Krauss, J. and Stahelin, M.
  TITLE     N2-Guanine specific transfer RNA methyltransferase II from rat
            liver.
  JOURNAL   Nucleic Acids Res. 1 (1974) 1479-1496.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K00555  tRNA (guanine-N2-)-methyltransferase
GENES       HSA: 55621(TRMT1)
            PTR: 455758(TRMT1)
            MMU: 212528(Trmt1)
            CFA: 476692(TRMT1)
            SPU: 585741(LOC585741)
            DME: Dmel_CG6388
            CEL: ZC376.5(trm-1)
            ATH: AT3G56330 AT5G15810
            OSA: 4334353 4338420
            CME: CMS136C CMS167C
            SCE: YDR120C(TRM1)
            AGO: AGOS_AGR075W
            PIC: PICST_65944(TRM3)
            CGR: CAGL0B01881g
            SPO: SPBC25D12.05
            ANI: AN9406.2
            AFM: AFUA_3G04200
            AOR: AO090124000082
            CNE: CNA00760
            UMA: UM04209.1
            ECU: ECU08_1450
            DDI: DDBDRAFT_0186078
            PFA: PF13_0109
            CPV: cgd4_3250
            CHO: Chro.40369
            TAN: TA13660
            TPV: TP02_0525
            TET: TTHERM_00636860 TTHERM_01166310
            TCR: 511857.40
            EHI: 1.t00080
            SYW: SYNW0682
            SYC: syc1676_d
            SYF: Synpcc7942_2430
            SYD: Syncc9605_1987
            SYE: Syncc9902_0673
            SYG: sync_0902
            SYR: SynRCC307_1690(trm1)
            SYX: SynWH7803_1642(trm1)
            PMT: PMT1174(F18O21.290)
            PMF: P9303_08491
            AAE: aq_841(trm1)
            MMP: MMP0228(trm1)
            MMQ: MmarC5_1472
            MMZ: MmarC7_1228
            MAE: Maeo_0624
            MVN: Mevan_1242
            MAC: MA1455(trm1)
            MBA: Mbar_A3224
            MMA: MM_2528
            MBU: Mbur_0659
            MTP: Mthe_1426
            MHU: Mhun_0626
            MEM: Memar_1698
            MBN: Mboo_1845
            MST: Msp_0291(trm1)
            MSI: Msm_1031
            MKA: MK0154(TRM1_1)
            HAL: VNG2088G(trm1)
            HMA: rrnAC2788(trm1)
            HWA: HQ3646A(trm1)
            NPH: NP0194A(trm1)
            TAC: Ta0997
            TVO: TVN0736
            PTO: PTO0220
            PHO: PH1829
            PAB: PAB2092
            PFU: PF1871
            TKO: TK0970
            RCI: RCIX2707(trm1)
            APE: APE_0782.1
            SMR: Smar_1252
            IHO: Igni_1184
            HBU: Hbut_0460
            SSO: SSO0943
            STO: ST1269
            SAI: Saci_1343(trm1)
            MSE: Msed_1726
            PAI: PAE1628
            PIS: Pisl_1656
            PCL: Pcal_0595
            PAS: Pars_1987
            TPE: Tpen_0379
            NEQ: NEQ108
STRUCTURES  PDB: 2DUL  2EJT  2EJU  2YTZ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.32
            ExPASy - ENZYME nomenclature database: 2.1.1.32
            ExplorEnz - The Enzyme Database: 2.1.1.32
            ERGO genome analysis and discovery system: 2.1.1.32
            BRENDA, the Enzyme Database: 2.1.1.32
            CAS: 37217-31-5
///
ENTRY       EC 2.1.1.33                 Enzyme
NAME        tRNA (guanine-N7-)-methyltransferase;
            transfer ribonucleate guanine 7-methyltransferase;
            7-methylguanine transfer ribonucleate methylase;
            tRNA guanine 7-methyltransferase;
            N7-methylguanine methylase;
            S-adenosyl-L-methionine:tRNA (guanine-7-N-)-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:tRNA (guanine-N7-)-methyltransferase
REACTION    S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA
            containing N7-methylguanine [RN:R00600]
ALL_REAC    R00600
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            tRNA [CPD:C00066]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            tRNA containing N7-methylguanine [CPD:C04160]
REFERENCE   1  [PMID:794833]
  AUTHORS   Aschhoff HJ, Elten H, Arnold HH, Mahal G, Kersten W, Kersten H.
  TITLE     7-Methylguanine specific tRNA-methyltransferase from Escherichia
            coli.
  JOURNAL   Nucleic. Acids. Res. 3 (1976) 3109-22.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:69267419]
  AUTHORS   Bjork GR, Svensson I.
  TITLE     Studies on microbial RNA. Fractionation of tRNA methylases from
            Saccharomyces cerevisiae.
  JOURNAL   Eur. J. Biochem. 9 (1969) 207-15.
REFERENCE   3  [PMID:14245404]
  AUTHORS   HURWITZ J, GOLD M, ANDERS M.
  TITLE     THE ENZYMATIC METHYLATION OF RIBONUCLEIC ACID AND DEOXYRIBONUCLEIC
            ACID. 3. PURIFICATION OF SOLUBLE RIBONUCLEIC ACID-METHYLATING
            ENZYMES.
  JOURNAL   J. Biol. Chem. 239 (1964) 3462-73.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4
  AUTHORS   Salvatore, F., Traboni, C., Colonna, A., Ciliberto, G., Paoletta, C.
            and Cimino, F.
  TITLE     In: Cavallini, D., Gaul, G.E. and Zappia, V. (Eds.), Natural Sulfur
            Compounds, Plenum Press, New York, 1980, p. 25.
ORTHOLOGY   KO: K03439  tRNA (guanine-N7-)-methyltransferase
GENES       HSA: 4234(METTL1)
            MMU: 17299(Mettl1)
            CFA: 607590(METTL1)
            XLA: 414654(MGC81128)
            XTR: 448504(mettl1)
            DME: Dmel_CG4045
            CEL: W02B12.10
            OSA: 4340601
            PIC: PICST_56862(TRM8)
            CGR: CAGL0J09746g
            AOR: AO090009000430
            TAN: TA20995
            TET: TTHERM_00621400
            TBR: Tb09.211.0790
            TCR: 506883.80 510429.20
            LMA: LmjF35.5230
            ECO: b2960(yggH)
            ECJ: JW2927(yggH)
            ECE: Z4305(yggH)
            ECS: ECs3836
            ECC: c3547(yggH)
            ECI: UTI89_C3350(yggH)
            ECP: ECP_2954
            ECV: APECO1_3561(yggH)
            ECW: EcE24377A_3305(trmB)
            ECX: EcHS_A3121(trmB)
            STY: STY3264
            STT: t3022
            SPT: SPA2972(yggH)
            SEC: SC3050(yggH)
            STM: STM3109(yggH)
            YPE: YPO0951
            YPK: y3338
            YPM: YP_3490
            YPA: YPA_0313
            YPN: YPN_3149
            YPP: YPDSF_0563
            YPS: YPTB3223
            YPI: YpsIP31758_0820(trmB)
            SFL: SF2957(yggH)
            SFX: S3160(yggH)
            SFV: SFV_3018(yggH)
            SSN: SSON_3236(yggH)
            SBO: SBO_3030(yggH)
            SDY: SDY_3112(yggH)
            ECA: ECA0977
            PLU: plu1170
            BUC: BU551(yggH)
            BAS: BUsg533(yggH)
            BAB: bbp499(yggH)
            SGL: SG2034
            ENT: Ent638_3365
            SPE: Spro_4042
            HIN: HI0340
            HIT: NTHI0459(trmB)
            HIP: CGSHiEE_01300(trmB)
            HDU: HD0775
            HSO: HS_1666(trmB)
            PMU: PM1317
            MSU: MS0318
            APL: APL_1383
            ASU: Asuc_0539
            XFA: XF0784
            XFT: PD1876(micA)
            XCC: XCC3151(micA)
            XCB: XC_1014
            XCV: XCV3418(trmB)
            XAC: XAC3303(micA)
            XOO: XOO3373(micA)
            XOM: XOO_3178(XOO3178)
            VCH: VC0453
            VCO: VC0395_A0005(trmB)
            VVU: VV1_1516
            VVY: VV2883
            VPA: VP2625
            PPR: PBPRA3152
            PAE: PA0382(micA)
            PAU: PA14_05000(micA)
            PAP: PSPA7_0481(trmB)
            PPU: PP_5103
            PPF: Pput_4976
            PST: PSPTO_0435
            PSB: Psyr_4739
            PSP: PSPPH_4773(trmB)
            PFL: PFL_5849(trmB)
            PFO: Pfl_5329
            PEN: PSEEN0308(trmB)
            PMY: Pmen_4166
            PAR: Psyc_1731
            PCR: Pcryo_2013
            PRW: PsycPRwf_1763
            ACI: ACIAD1302(trmB)
            SON: SO_3367
            SDN: Sden_2697
            SFR: Sfri_2872
            SAZ: Sama_2489
            SBL: Sbal_3038
            SBM: Shew185_3052
            SLO: Shew_1124
            SPC: Sputcn32_2699
            SSE: Ssed_1220
            SPL: Spea_1109
            SHE: Shewmr4_1181
            SHM: Shewmr7_1252
            SHN: Shewana3_1182
            SHW: Sputw3181_1312
            ILO: IL1981
            CPS: CPS_4146(trmB)
            PHA: PSHAa0553(yggH)
            PAT: Patl_0078
            SDE: Sde_3592
            PIN: Ping_0377
            MAQ: Maqu_0526
            LPN: lpg0481
            LPF: lpl0521
            LPP: lpp0545
            MCA: MCA1532(trmB)
            FTH: FTH_0631
            FTA: FTA_0661(trmB)
            FTN: FTN_1400
            TCX: Tcr_0119
            NOC: Noc_1026
            AEH: Mlg_0033
            HHA: Hhal_2398
            HCH: HCH_06365(trmB)
            CSA: Csal_3145
            ABO: ABO_2573
            MMW: Mmwyl1_0765
            AHA: AHA_3482(trmB)
            DNO: DNO_1247(trmB)
            RMA: Rmag_0997
            NME: NMB1328
            NMA: NMA1542
            NGO: NGO0575
            CVI: CV_2030 CV_3786
            RSO: RSc0703(RS01608)
            REU: Reut_A0758
            RME: Rmet_2704
            BMA: BMA2167(trmB)
            BMV: BMASAVP1_A0743(trmB)
            BML: BMA10299_A2576(trmB)
            BMN: BMA10247_2037(trmB)
            BXE: Bxe_A0859
            BVI: Bcep1808_0849
            BUR: Bcep18194_A4022
            BCN: Bcen_0439
            BCH: Bcen2424_0918
            BAM: Bamb_0795
            BPS: BPSL2642
            BPM: BURPS1710b_3119(trmB)
            BPL: BURPS1106A_3091(trmB)
            BPD: BURPS668_3056(trmB)
            BTE: BTH_I1513
            PNU: Pnuc_0262
            BPE: BP3692
            BPA: BPP0505
            BBR: BB0510
            RFR: Rfer_1896
            POL: Bpro_2905
            PNA: Pnap_2936
            AAV: Aave_3033
            AJS: Ajs_1981
            VEI: Veis_1672
            MPT: Mpe_A2850
            HAR: HEAR2695(trmB)
            MMS: mma_0152 mma_2928(trmB)
            NEU: NE0283
            NET: Neut_0322
            NMU: Nmul_A0069
            EBA: c1A43
            AZO: azo1523(yggH) azo3968
            DAR: Daro_3860
            TBD: Tbd_2125
            MFA: Mfla_0231
            HPY: HP0747
            HPJ: jhp0684
            HPA: HPAG1_0732
            HHE: HH0785
            HAC: Hac_0671
            WSU: WS0145
            TDN: Tmden_0785
            CJE: Cj1278c
            CJR: CJE1414(trmB)
            CJJ: CJJ81176_1294(trmB)
            CJU: C8J_1222
            CJD: JJD26997_0447(trmB)
            CFF: CFF8240_0543 CFF8240_1218
            CHA: CHAB381_0617 CHAB381_1287
            ABU: Abu_1001 Abu_1976(kdtA)
            NIS: NIS_0754
            SUN: SUN_1751
            GSU: GSU0521
            GME: Gmet_3034
            GUR: Gura_0955
            PCA: Pcar_0761
            PPD: Ppro_2892
            BBA: Bd0370
            ADE: Adeh_3785
            AFW: Anae109_3907
            MXA: MXAN_5790
            RFE: RF_1344(hemK)
            RAK: A1C_06570
            RBO: A1I_00915
            RCM: A1E_05435
            RRI: A1G_07200
            WOL: WD1091
            MLO: mlr5547
            MES: Meso_3925
            PLA: Plav_3624
            SME: SMc01108
            SMD: Smed_0047
            ATU: Atu0363
            ATC: AGR_C_634
            RET: RHE_CH00369(ypch00142)
            RLE: RL0388
            BME: BMEI1969
            BMF: BAB1_2161
            BMS: BR2161
            BMB: BruAb1_2134
            OAN: Oant_0751
            BJA: bll0788
            BRA: BRADO0048(trmB)
            BBT: BBta_0053(trmB)
            RPA: RPA0442
            RPB: RPB_0596
            RPC: RPC_0474
            RPD: RPD_0236
            RPE: RPE_0200
            NWI: Nwi_0020
            NHA: Nham_0027
            BHE: BH02190
            BQU: BQ02070
            XAU: Xaut_1817
            CCR: CC_0049
            SIL: SPOA0014(trmB)
            SIT: TM1040_0195
            RSP: RSP_3593
            RSH: Rsph17029_3278
            JAN: Jann_0707
            RDE: RD1_3915(trmB)
            PDE: Pden_2227
            MMR: Mmar10_3039
            HNE: HNE_0109(trmB)
            ZMO: ZMO0149(smtA)
            NAR: Saro_0305
            SAL: Sala_3140
            SWI: Swit_3371
            ELI: ELI_14220
            GBE: GbCGDNIH1_2398
            ACR: Acry_1053
            RRU: Rru_A3777
            MAG: amb4470
            MGM: Mmc1_0405
            BSU: BG13890(ytmQ)
            BHA: BH3261
            BAN: BA4950
            BAR: GBAA4950
            BAA: BA_5368
            BAT: BAS4594
            BCE: BC4696
            BCA: BCE_4841
            BCZ: BCZK4449
            BCY: Bcer98_3362
            BTK: BT9727_4431
            BTL: BALH_4273(trmB)
            BLI: BL00042(ytmQ)
            BLD: BLi03141(ytmQ)
            BCL: ABC2778
            BAY: RBAM_027010(trmB)
            OIH: OB2294
            GKA: GK2823
            SAU: SA1569
            SAV: SAV1748
            SAM: MW1691
            SAR: SAR1833
            SAS: SAS1674
            SAC: SACOL1798(trmB)
            SAB: SAB1608c
            SAA: SAUSA300_1694(trmB)
            SAO: SAOUHSC_01865
            SAJ: SaurJH9_1803
            SAH: SaurJH1_1838
            SEP: SE1421
            SER: SERP1307(trmB)
            SHA: SH1174
            SSP: SSP1015
            LMO: lmo1615
            LMF: LMOf2365_1637(trmB)
            LIN: lin1656
            LWE: lwe1631
            LLA: L156302(yhfE)
            LLC: LACR_0793
            LLM: llmg_1811
            SPY: SPy_1726
            SPZ: M5005_Spy_1468
            SPM: spyM18_1734
            SPG: SpyM3_1500
            SPS: SPs0367
            SPH: MGAS10270_Spy1535
            SPI: MGAS10750_Spy1527
            SPJ: MGAS2096_Spy1493
            SPK: MGAS9429_Spy1470
            SPF: SpyM50377
            SPA: M6_Spy1462
            SPB: M28_Spy1457
            SPN: SP_0550
            SPR: spr0476
            SPD: SPD_0477(trmB)
            SAG: SAG0376
            SAN: gbs0412
            SAK: SAK_0449(trmB)
            SMU: SMU.416
            STC: str1606
            STL: stu1606
            SSA: SSA_1902
            LPL: lp_1458
            LJO: LJ1667
            LAC: LBA1582
            LSA: LSA0632
            LSL: LSL_0481
            LDB: Ldb1525
            LBU: LBUL_1416
            LBR: LVIS_1478
            LCA: LSEI_1716
            LRE: Lreu_1260
            EFA: EF0691
            OOE: OEOE_1272
            CAC: CAC2627
            CPE: CPE0424
            CPF: CPF_0427(trmB)
            CPR: CPR_0422(trmB)
            CTC: CTC00794
            CNO: NT01CX_0357(trmB)
            CTH: Cthe_0102
            CDF: CD1942
            CBO: CBO0499
            CBA: CLB_0540(trmB)
            CBH: CLC_0573(trmB)
            CBF: CLI_0579(trmB)
            CBE: Cbei_0833
            CKL: CKL_2811(trmB)
            AMT: Amet_1206
            DSY: DSY2003
            MGE: MG_347
            MPN: MPN522(G12_orf210V)
            MPU: MYPU_1660
            MPE: MYPE2880
            MGA: MGA_1194
            MMY: MSC_0166
            MMO: MMOB4960
            MHY: mhp463
            MHJ: MHJ_0462
            MHP: MHP7448_0465
            MSY: MS53_0113
            MCP: MCAP_0761(trmB)
            UUR: UU269
            MFL: Mfl218
            MTU: Rv0208c
            MTC: MT0218
            MBO: Mb0214c
            MLE: ML2622
            MPA: MAP3643c
            MAV: MAV_4966(trmB)
            MSM: MSMEG_0252(trmB)
            MVA: Mvan_0198
            MGI: Mflv_0454
            MMC: Mmcs_0173
            MKM: Mkms_0182
            MJL: Mjls_0162
            CGL: NCgl2767(trmB)
            CGB: cg3172
            CEF: CE2696
            CDI: DIP2181
            CJK: jk0149
            NFA: nfa54840
            RHA: RHA1_ro05176
            SCO: SCO4111(SCD17A.03c)
            SMA: SAV4115
            LXX: Lxx08920(micA)
            ART: Arth_3782
            AAU: AAur_3557(trmB)
            PAC: PPA1808
            NCA: Noca_3919
            KRA: Krad_3723
            SEN: SACE_7256
            BLO: BL1670
            BAD: BAD_0392
            RXY: Rxyl_2026
            RBA: RB7807
            CTR: CT829(yggH)
            CTA: CTA_0903(yggH)
            CMU: TC0216
            CPN: CPn0986(yggH)
            CPA: CP0869
            CPJ: CPj0986(yggH)
            CPT: CpB1023
            CCA: CCA00775
            CAB: CAB743
            CFE: CF0239(rrm2)
            PCU: pc1285
            TPA: TP0464
            TDE: TDE1130
            LIL: LA0140
            LIC: LIC10126
            LBJ: LBJ_0122
            LBL: LBL_2969
            SYN: sll1300
            SYW: SYNW0285
            SYC: syc1155_d
            SYD: Syncc9605_0280
            SYE: Syncc9902_2064
            SYG: sync_0328(trmB)
            SYR: SynRCC307_2216
            SYX: SynWH7803_0331
            CYA: CYA_2671(trmB)
            CYB: CYB_2166(trmB)
            TEL: tll1983
            ANA: alr1845
            AVA: Ava_4784
            PMA: Pro0270
            PMM: PMM0240
            PMT: PMT1820
            PMN: PMN2A_1607
            PMI: PMT9312_0242
            PMB: A9601_02621
            PMC: P9515_02731
            PMF: P9303_24391
            PMG: P9301_02631
            PME: NATL1_03191
            TER: Tery_0871
            BTH: BT_3894
            BFR: BF3995
            BFS: BF3770
            PGI: PG0960
            CHU: CHU_1543(trmB)
            FJO: Fjoh_1336
            FPS: FP0368(trmB)
            DRA: DR_1680
            DGE: Dgeo_2090
            TTH: TTC1255
            TTJ: TTHA1619
            AAE: aq_065
            TMA: TM0925
            TPT: Tpet_0002
            TME: Tmel_1791
            FNO: Fnod_1013
STRUCTURES  PDB: 1YZH  2FCA  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.33
            ExPASy - ENZYME nomenclature database: 2.1.1.33
            ExplorEnz - The Enzyme Database: 2.1.1.33
            ERGO genome analysis and discovery system: 2.1.1.33
            BRENDA, the Enzyme Database: 2.1.1.33
            CAS: 37257-00-4
///
ENTRY       EC 2.1.1.34                 Enzyme
NAME        tRNA guanosine-2'-O-methyltransferase;
            transfer ribonucleate guanosine 2'-methyltransferase;
            tRNA guanosine 2'-methyltransferase;
            tRNA (guanosine 2')-methyltransferase;
            tRNA (Gm18) 2'-O-methyltransferase;
            tRNA (Gm18) methyltransferase;
            tRNA (guanosine-2'-O-)-methyltransferase;
            S-adenosyl-L-methionine:tRNA (guanosine-2'-O-)-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:tRNA guanosine-2'-O-methyltransferase
REACTION    S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA
            containing 2'-O-methylguanosine [RN:R02917]
ALL_REAC    R02917
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            tRNA [CPD:C00066]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            tRNA containing 2'-O-methylguanosine [CPD:C04545]
COMMENT     Methylates the 2'-hydroxy group of a guanosine present in a GG
            sequence at position 18. Yeast tRNAPhe is one of the best substrate
            tRNAs.
REFERENCE   1  [PMID:4898378]
  AUTHORS   Gefter ML.
  TITLE     The in vitro synthesis of 2'-omethylguanosine and 2-methylthio 6N
            (gamma,gamma, dimethylallyl) adenosine in transfer RNA of
            Escherichia coli.
  JOURNAL   Biochem. Biophys. Res. Commun. 36 (1969) 435-41.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:6990416]
  AUTHORS   Kumagai I, Watanabe K, Oshima T.
  TITLE     Thermally induced biosynthesis of 2'-O-methylguanosine in tRNA from
            an extreme thermophile, Thermus thermophilus HB27.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 77 (1980) 1922-6.
  ORGANISM  Thermus thermophilus
REFERENCE   3  [PMID:9748240]
  AUTHORS   Hori H, Yamazaki N, Matsumoto T, Watanabe Y, Ueda T, Nishikawa K,
            Kumagai I, Watanabe K.
  TITLE     Substrate recognition of tRNA (Guanosine-2'-)-methyltransferase from
            Thermus thermophilus HB27.
  JOURNAL   J. Biol. Chem. 273 (1998) 25721-7.
  ORGANISM  Thermus thermophilus
ORTHOLOGY   KO: K00556  tRNA (guanosine-2'-O-)-methyltransferase
GENES       DDI: DDBDRAFT_0216794
            ECO: b3651(trmH)
            ECJ: JW3626(trmH)
            ECE: Z5077(spoU)
            ECS: ECs4526
            ECC: c4476(spoU)
            ECI: UTI89_C4196(spoU)
            ECP: ECP_3749
            ECV: APECO1_2810(spoU)
            ECW: EcE24377A_4154(trmH)
            ECX: EcHS_A3862(trmH)
            STY: STY4049(trmH)
            STT: t3775(trmH)
            SPT: SPA3595(trmH)
            SEC: SC3667(spoU)
            STM: STM3743(spoU)
            YPE: YPO0037(trmH)
            YPK: y0104(spoU)
            YPM: YP_0038(trmH)
            YPA: YPA_3505
            YPN: YPN_3813
            YPP: YPDSF_3868
            YPS: YPTB0034(trmH)
            YPI: YpsIP31758_0038(trmH)
            SFL: SF3691(spoU)
            SFX: S4078(spoU)
            SFV: SFV_3878(spoU)
            SSN: SSON_3754(spoU)
            SBO: SBO_3726(spoU)
            SDY: SDY_4083(spoU)
            ECA: ECA0037(trmH)
            ENT: Ent638_0088
            SPE: Spro_4870
            VVU: VV1_0853
            VVY: VV0240
            VPA: VP0158
            VFI: VF0103
            PPR: PBPRA0188
            ACI: ACIAD2933
            SDN: Sden_2942
            SFR: Sfri_3115
            SAZ: Sama_0262
            SLO: Shew_3501
            SSE: Ssed_0332
            SPL: Spea_3881
            ILO: IL2375(spoU)
            CPS: CPS_4975(spoU)
            PHA: PSHAa1080(trmH) PSHAa2798(trmH)
            PAT: Patl_0351
            SDE: Sde_2003
            PIN: Ping_3496
            MAQ: Maqu_2737
            NOC: Noc_0219
            AEH: Mlg_0536
            ABO: ABO_0813(spoU)
            AHA: AHA_0038
            BUR: Bcep18194_A4689
            HAR: HEAR1278(rlmB)
            SUN: SUN_1100
            DVU: DVU2355(trmH)
            DVL: Dvul_0906
            DDE: Dde_1484
            LIP: LI0355
            BBA: Bd1203(spoU)
            MXA: MXAN_1472
            PUB: SAR11_0101(spoU)
            BCZ: BCZK4305(spoU)
            BTK: BT9727_4295(spoU)
            BTL: BALH_4143(spoU)
            GKA: GK3460
            LLA: L0330(trmH)
            LAC: LBA0350
            TTE: TTE2630(spoU3)
            CGL: NCgl1334(cgl1388)
            SYW: SYNW1681
            SYD: Syncc9605_0802
            SYE: Syncc9902_1577
            SYG: sync_0690
            SYR: SynRCC307_0572(spoU)
            SYX: SynWH7803_1782(spoU)
            AVA: Ava_1436 Ava_4413
            PMA: Pro0421(spoU)
            PMM: PMM0422
            PMT: PMT0268
            PMN: PMN2A_1756
            PMI: PMT9312_0418
            PMB: A9601_04731
            PMC: P9515_04831
            PMF: P9303_20701
            PMG: P9301_04421
            PMH: P9215_04991(spoU)
            PME: NATL1_04781
            TER: Tery_2249
            GFO: GFO_2995(trmH)
            CTE: CT0879(spoU)
            CPH: Cpha266_1198
            PVI: Cvib_1007
            PLT: Plut_1255
            DRA: DR_2211(spoU)
            DGE: Dgeo_2234
            TTH: TTC1867
            TTJ: TTHA0127
            AAE: aq_1661(spoU)
STRUCTURES  PDB: 1V2X  1ZJR  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.34
            ExPASy - ENZYME nomenclature database: 2.1.1.34
            ExplorEnz - The Enzyme Database: 2.1.1.34
            ERGO genome analysis and discovery system: 2.1.1.34
            BRENDA, the Enzyme Database: 2.1.1.34
            CAS: 37257-01-5
///
ENTRY       EC 2.1.1.35                 Enzyme
NAME        tRNA (uracil-5-)-methyltransferase;
            ribothymidyl synthase;
            transfer RNA uracil 5-methyltransferase;
            transfer RNA uracil methylase;
            tRNA uracil 5-methyltransferase;
            m5U-methyltransferase;
            tRNA:m5U54-methyltransferase;
            RUMT
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:tRNA (uracil-5-)-methyltransferase
REACTION    S-adenosyl-L-methionine + tRNA containing uridine at position 54 =
            S-adenosyl-L-homocysteine + tRNA containing ribothymidine at
            position 54 [RN:R00594]
ALL_REAC    R00594
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            tRNA containing uridine at position 54
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            tRNA containing ribothymidine at position 54
COMMENT     Up to 25% of the bases in mature tRNA are post-translationally
            modified or hypermodified. One almost universal post-translational
            modification is the conversion of U54 into ribothymidine in the
            TPsiC loop, and this modification is found in most species studied
            to date [7]. Unlike this enzyme, EC 2.1.1.74,
            methylenetetrahydrofolate---tRNA-(uracil-5-)-methyltransferase
            (FADH2-oxidizing), uses 5,10-methylenetetrahydrofolate and FADH2 to
            supply the atoms for methylation of U54 [4].
REFERENCE   1  [PMID:69267419]
  AUTHORS   Bjork GR, Svensson I.
  TITLE     Studies on microbial RNA. Fractionation of tRNA methylases from
            Saccharomyces cerevisiae.
  JOURNAL   Eur. J. Biochem. 9 (1969) 207-15.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:6997293]
  AUTHORS   Greenberg R, Dudock B.
  TITLE     Isolation and chracterization of m5U-methyltransferase from
            Escherichia coli.
  JOURNAL   J. Biol. Chem. 255 (1980) 8296-302.
REFERENCE   3  [PMID:14245404]
  AUTHORS   HURWITZ J, GOLD M, ANDERS M.
  TITLE     THE ENZYMATIC METHYLATION OF RIBONUCLEIC ACID AND DEOXYRIBONUCLEIC
            ACID. 3. PURIFICATION OF SOLUBLE RIBONUCLEIC ACID-METHYLATING
            ENZYMES.
  JOURNAL   J. Biol. Chem. 239 (1964) 3462-73.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:6768721]
  AUTHORS   Delk AS, Nagle DP Jr, Rabinowitz JC.
  TITLE     Methylenetetrahydrofolate-dependent biosynthesis of ribothymidine in
            transfer RNA of Streptococcus faecalis. Evidence for reduction of
            the 1-carbon unit by FADH2.
  JOURNAL   J. Biol. Chem. 255 (1980) 4387-90.
  ORGANISM  Streptococcus faecalis, Bacillus subtilis [GN:bsu]
REFERENCE   5  [PMID:7748948]
  AUTHORS   Kealey JT, Gu X, Santi DV.
  TITLE     Enzymatic mechanism of tRNA (m5U54)methyltransferase.
  JOURNAL   Biochimie. 76 (1994) 1133-42.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:8794745]
  AUTHORS   Gu X, Ivanetich KM, Santi DV.
  TITLE     Recognition of the T-arm of tRNA by tRNA (m5U54)-methyltransferase
            is not sequence specific.
  JOURNAL   Biochemistry. 35 (1996) 11652-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   7  [PMID:9417931]
  AUTHORS   Becker HF, Motorin Y, Sissler M, Florentz C, Grosjean H.
  TITLE     Major identity determinants for enzymatic formation of ribothymidine
            and pseudouridine in the T psi-loop of yeast tRNAs.
  JOURNAL   J. Mol. Biol. 274 (1997) 505-18.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K00557  tRNA (uracil-5-)-methyltransferase
GENES       PIC: PICST_50774(TRM1) PICST_51919(TRM2)
            ECO: b3965(trmA)
            ECJ: JW3937(trmA)
            ECE: Z5526(trmA)
            ECS: ECs4896
            ECC: c4928(trmA)
            ECI: UTI89_C4560(trmA)
            ECP: ECP_4182
            ECV: APECO1_2498(trmA)
            ECW: EcE24377A_4506(trmA)
            ECX: EcHS_A4199(trmA)
            STY: STY3745(trmA)
            STT: t3496(trmA)
            SPT: SPA3967(trmA)
            SEC: SC4018(trmA)
            STM: STM4129(trmA)
            YPE: YPO3911(trmA)
            YPK: y0324(trmA)
            YPM: YP_3137(trmA2)
            YPA: YPA_0111
            YPN: YPN_0056
            YPP: YPDSF_3523
            YPS: YPTB0124(trmA)
            YPI: YpsIP31758_0141(trmA)
            SFL: SF4047(trmA)
            SFX: S3697(trmA)
            SFV: SFV_4038(trmA)
            SSN: SSON_4138(trmA)
            SBO: SBO_3984(trmA)
            SDY: SDY_3763(trmA)
            ECA: ECA4239(trmA)
            PLU: plu4736(trmA)
            SGL: SG2154
            ENT: Ent638_4021
            SPE: Spro_4771
            HIN: HI0848(trmA)
            HIT: NTHI1014(trmA)
            HIP: CGSHiEE_07810
            HIQ: CGSHiGG_07795
            HDU: HD0723(trmA)
            HSO: HS_0306(trmA)
            PMU: PM1803(trmA)
            MSU: MS2367(trmA)
            APL: APL_1979(trmA)
            ASU: Asuc_0429
            VCH: VC0154
            VCO: VC0395_A2367(trmA)
            VVU: VV1_1171
            VVY: VV0129
            VPA: VP2939
            VFI: VF2436
            PPR: PBPRA3465
            PAE: PA4720(trmA)
            PAU: PA14_62450(trmA)
            PAP: PSPA7_5436(trmA)
            PPU: PP_4654(trmA)
            PPF: Pput_4516
            PST: PSPTO_4654(trmA)
            PSB: Psyr_4287
            PSP: PSPPH_4345(trmA)
            PFL: PFL_5373
            PFO: Pfl_4898
            PEN: PSEEN4780(trmA)
            PMY: Pmen_0831
            ACI: ACIAD1645(trmA)
            SON: SO_0206(trmA)
            SDN: Sden_0231
            SFR: Sfri_0125
            SAZ: Sama_0193
            SBL: Sbal_4178
            SBM: Shew185_0176
            SLO: Shew_0138
            SPC: Sputcn32_3510
            SSE: Ssed_4338
            SPL: Spea_0164
            SHE: Shewmr4_0178
            SHM: Shewmr7_0173
            SHN: Shewana3_0179
            SHW: Sputw3181_3677
            ILO: IL2273(trmA)
            CPS: CPS_0336(trmA)
            PHA: PSHAa0250(trmA)
            PAT: Patl_4030
            SDE: Sde_1616
            PIN: Ping_0628
            TCX: Tcr_0173
            NOC: Noc_0801
            CSA: Csal_1339
            MMW: Mmwyl1_4311
            AHA: AHA_4191(trmA)
            DNO: DNO_1163(trmA)
            NME: NMB1679
            NMA: NMA1938(trmA)
            NMC: NMC1597(trmA)
            NGO: NGO1330
            REH: H16_A2370(trmA)
            BUR: Bcep18194_A5118
            HAR: HEAR1258(rumA)
            EBA: ebA595(trmA)
            AZO: azo1312
            DAR: Daro_1823
            HHE: HH0693(trmA)
            WSU: WS2094(trmA)
            TDN: Tmden_1018
            CJE: Cj0831c(trmA)
            CJR: CJE0918(trmA)
            CJJ: CJJ81176_0848(trmA)
            CJU: C8J_0778(trmA)
            CJD: JJD26997_1184(trmA)
            CFF: CFF8240_0976(trmA)
            CCV: CCV52592_1420(trmA)
            CHA: CHAB381_1374(trmA)
            CCO: CCC13826_1404(trmA) CCC13826_1983
            ABU: Abu_2207(trmA)
            NIS: NIS_0702(trmA)
            SUN: SUN_1832(trmA)
            GOX: GOX0093
            GBE: GbCGDNIH1_1318
            BTL: BALH_0425(trmA)
            BPU: BPUM_0753(trmA)
            SPZ: M5005_Spy_1098
            SPH: MGAS10270_Spy1435
            SPI: MGAS10750_Spy1428
            SPJ: MGAS2096_Spy1340
            SPK: MGAS9429_Spy1313
            SPA: M6_Spy1337
            LSL: LSL_0369(trmA)
            CTC: CTC01941 CTC02481
            MMO: MMOB5020(trmA)
            AVA: Ava_3634
            CCH: Cag_2028
            DGE: Dgeo_1777
            TTH: TTC0988
            TTJ: TTHA1353
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.35
            ExPASy - ENZYME nomenclature database: 2.1.1.35
            ExplorEnz - The Enzyme Database: 2.1.1.35
            ERGO genome analysis and discovery system: 2.1.1.35
            BRENDA, the Enzyme Database: 2.1.1.35
            CAS: 37257-02-6
///
ENTRY       EC 2.1.1.36                 Enzyme
NAME        tRNA (adenine-N1-)-methyltransferase;
            transfer ribonucleate adenine 1-methyltransferase;
            transfer RNA (adenine-1) methyltransferase;
            1-methyladenine transfer RNA methyltransferase;
            adenine-1-methylase;
            S-adenosyl-L-methionine:tRNA (adenine-1-N-)-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:tRNA (adenine-N1-)-methyltransferase
REACTION    S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA
            containing N1-methyladenine [RN:R00596]
ALL_REAC    R00596
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            tRNA [CPD:C00066]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            tRNA containing N1-methyladenine [CPD:C04156]
COMMENT     The enzymes from different sources are specific for different
            adenine residues in tRNA.
REFERENCE   1  [PMID:4921283]
  AUTHORS   Baguley BC, Staehelin M.
  TITLE     The specificity of transfer ribonucleic acid methylases from rat
            liver.
  JOURNAL   Biochemistry. 7 (1968) 45-50.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:69267419]
  AUTHORS   Bjork GR, Svensson I.
  TITLE     Studies on microbial RNA. Fractionation of tRNA methylases from
            Saccharomyces cerevisiae.
  JOURNAL   Eur. J. Biochem. 9 (1969) 207-15.
REFERENCE   3  [PMID:4611497]
  AUTHORS   Dubois EG, Dirheimer G, Weil JH.
  TITLE     Methylation of yeast tRNA Asp by enzymes from cytoplasm,
            chloroplasts and mitochondria of phaseolus vulgaris.
  JOURNAL   Biochim. Biophys. Acta. 374 (1974) 332-41.
  ORGANISM  Phaseolus vulgaris
REFERENCE   4  [PMID:17605]
  AUTHORS   Glick JM, Leboy PS.
  TITLE     Purification and properties of tRNA(adenine-1)-methyltransferase
            from rat liver.
  JOURNAL   J. Biol. Chem. 252 (1977) 4790-5.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K07442  tRNA (adenine-N1-)-methyltransferase
GENES       HSA: 115708(C14orf172)
            MMU: 328162(6720458F09Rik)
            RNO: 314462(RGD1359191)
            BTA: 510283(MGC165793)
            SCE: YJL125C(GCD14)
            AGO: AGOS_AFL214C
            KLA: KLLA0E15290g
            PIC: PICST_65994(GCD14)
            CAL: CaO19_7291(CaO19.7291)
            CGR: CAGL0L05566g
            SPO: SPAC9G1.12
            CNE: CNH01430
            UMA: UM00894.1
            DVU: DVU3053
            DDE: Dde_0539
            LIP: LI0357(pcm)
            TTE: TTE0474(gcd14)
            MTU: Rv2118c
            MTC: MT2178
            MBO: Mb2142c
            MLE: ML1313
            MPA: MAP1842c
            MSM: MSMEG_3906
            MVA: Mvan_3462
            MGI: Mflv_3065
            MMC: Mmcs_3136
            MKM: Mkms_3198
            MJL: Mjls_3148
            CGL: NCgl1441(cgl1498)
            CEF: CE1627
            CDI: DIP1249
            RHA: RHA1_ro00851
            SCO: SCO1651(SCI41.34c)
            SMA: SAV6674
            TWS: TW454
            LXX: Lxx08280(gcd14)
            ART: Arth_2172
            NCA: Noca_2638
            TFU: Tfu_1810
            FRA: Francci3_2632
            ACE: Acel_1182
            SEN: SACE_2244
            BLO: BL0800(pimT)
            BAD: BAD_0753
            TTH: TTC0244
            TTJ: TTHA0609
            AAE: aq_311
            TMA: TM0748
            FNO: Fnod_1692
            MJA: MJ0134
            MMP: MMP1375
            MBU: Mbur_2122
            MHU: Mhun_2273
            MTH: MTH1414
            MST: Msp_0004
            MSI: Msm_1173
            MKA: MK1415
            AFU: AF0216
            HAL: VNG0425G(pimT2)
            NPH: NP0356A
            TAC: Ta0852
            PTO: PTO1341
            PHO: PH1858
            PAB: PAB0283(pimT-like)
            PFU: PF1896
            RCI: RCIX1025(pimT)
            APE: APE_2486.1
            SSO: SSO0427
            STO: ST0370
            SAI: Saci_0844
            PAI: PAE2166(pimT)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.36
            ExPASy - ENZYME nomenclature database: 2.1.1.36
            ExplorEnz - The Enzyme Database: 2.1.1.36
            ERGO genome analysis and discovery system: 2.1.1.36
            BRENDA, the Enzyme Database: 2.1.1.36
            CAS: 37257-03-7
///
ENTRY       EC 2.1.1.37                 Enzyme
NAME        DNA (cytosine-5-)-methyltransferase;
            EcoRI methylase;
            DNA 5-cytosine methylase;
            DNA cytosine c5 methylase;
            DNA cytosine methylase;
            DNA methylase;
            DNA methyltransferase;
            DNA transmethylase;
            DNA-cytosine 5-methylase;
            DNA-cytosine methyltransferase;
            HpaII methylase;
            HpaII' methylase;
            M.BsuRIa;
            M.BsuRIb;
            Type II DNA methylase;
            cytosine 5-methyltransferase;
            cytosine DNA methylase;
            cytosine DNA methyltransferase;
            cytosine-specific DNA methyltransferase;
            deoxyribonucleate methylase;
            deoxyribonucleate methyltransferase;
            deoxyribonucleic (cytosine-5-)-methyltransferase;
            deoxyribonucleic acid (cytosine-5-)-methyltransferase;
            deoxyribonucleic acid methylase;
            deoxyribonucleic acid methyltransferase;
            deoxyribonucleic acid modification methylase;
            deoxyribonucleic methylase;
            methylphosphotriester-DNA methyltransferase;
            modification methylase;
            restriction-modification system;
            site-specific DNA-methyltransferase (cytosine-specific)
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:DNA (cytosine-5-)-methyltransferase
REACTION    S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA
            containing 5-methylcytosine [RN:R00380]
ALL_REAC    R00380 > R04858
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            DNA [CPD:C00039]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            DNA containing 5-methylcytosine [CPD:C02967]
REFERENCE   1
  AUTHORS   Gold, M. and Hurwitz, J.
  TITLE     The enzymatic methylation of ribonucleic acid and deoxyribonucleic
            acid. V. Purification and properties of the deoxyribonucleic
            acid-methylating activity of Escherichia coli.
  JOURNAL   J. Biol. Chem. 239 (1964) 3858-2865.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4975067]
  AUTHORS   Kalousek F, Morris NR.
  TITLE     The purification and properties of deoxyribonucleic acid methylase
            from rat spleen.
  JOURNAL   J. Biol. Chem. 244 (1969) 1157-63.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:1187340]
  AUTHORS   Roy PH, Weissbach A.
  TITLE     DNA methylase from HeLa cell nuclei.
  JOURNAL   Nucleic. Acids. Res. 2 (1975) 1669-84.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:673848]
  AUTHORS   Simon D, Grunert F, von Acken U, Doring HP, Kroger H.
  TITLE     DNA-methylase from regenerating rat liver: purification and
            characterisation.
  JOURNAL   Nucleic. Acids. Res. 5 (1978) 2153-67.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:171625]
  AUTHORS   Sneider TW, Teague WM, Rogachevsky LM.
  TITLE     S-adenosylmethionine: DNA-cytosine 5-methyltransferase from a
            Novikoff rat hepatoma cell line.
  JOURNAL   Nucleic. Acids. Res. 2 (1975) 1685-700.
  ORGANISM  rat [GN:rno]
REFERENCE   6  [PMID:131936]
  AUTHORS   Turnbull JF, Adams RL.
  TITLE     DNA methylase: purification from ascites cells and the effect of
            various DNA substrates on its activity.
  JOURNAL   Nucleic. Acids. Res. 3 (1976) 677-95.
  ORGANISM  Escherichia coli [GN:eco], cow [GN:bta]
REFERENCE   7  [PMID:2172084]
  AUTHORS   Kessler C, Manta V.
  TITLE     Specificity of restriction endonucleases and DNA modification
            methyltransferases a review (Edition 3).
  JOURNAL   Gene. 92 (1990) 1-248.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   8  [PMID:2159140]
  AUTHORS   Roberts RJ.
  TITLE     Restriction enzymes and their isoschizomers.
  JOURNAL   Nucleic. Acids. Res. 18 Suppl (1990) 2331-65.
REFERENCE   9  [PMID:6267988]
  AUTHORS   Yuan R.
  TITLE     Structure and mechanism of multifunctional restriction
            endonucleases.
  JOURNAL   Annu. Rev. Biochem. 50 (1981) 285-319.
PATHWAY     PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K00558  DNA (cytosine-5-)-methyltransferase
GENES       HSA: 1786(DNMT1) 1788(DNMT3A) 1789(DNMT3B)
            PTR: 455696(DNMT1)
            MMU: 13433(Dnmt1) 13435(Dnmt3a) 13436(Dnmt3b)
            CFA: 476715(DNMT1) 482996(DNMT3A)
            BTA: 281119(DNMT1) 353354(DNMT3B)
            MDO: 497245(DNMT1) 497246(CA1)
            GGA: 396011(DNMT1) 419287(DNMT3B) 421991(DNMT3A)
            XLA: 399257(dnmt1)
            DRE: 30430(dnmt1) 30659(dnmt3)
            SPU: 574665(LOC574665)
            DME: Dmel_CG10692(Dnmt2)
            ATH: AT4G13610(MEE57) AT4G14140(MET2) AT5G49160(MET1)
            OSA: 4342575
            CME: CMR026C
            ANI: AN6638.2
            AFM: AFUA_6G03740
            AOR: AO090701000174
            PFA: MAL7P1.151
            ECO: b1961(dcm)
            ECJ: JW1944(dcm)
            ECE: Z2389 Z3054(dcm)
            ECS: ECs1953 ECs2699
            ECC: c2380(dcm)
            ECI: UTI89_C2162(dcm)
            ECP: ECP_1894
            ECV: APECO1_998(dcm)
            ECW: EcE24377A_2193(dcm)
            ECX: EcHS_A2063
            STY: HCM1.187c STY2200(dcm)
            STT: t0886(dcm)
            SPT: SPA0878(dcm)
            SEC: SC1995(dcm)
            STM: STM1992(dcm)
            YEN: YE1681
            SFL: SF2005(dcm)
            SFX: S2100(dcm)
            SFV: SFV_2002(dcm)
            SSN: SSON_2018(dcm)
            SBO: SBO_1047(dcm)
            SDY: SDY_1045(dcm)
            PLU: plu0338(dcm)
            ENT: Ent638_2551
            SPE: Spro_0573 Spro_2532 Spro_3066
            HIN: HI1041
            HIT: NTHI1460 NTHI1487 NTHI1787(haeIIM)
            HSO: HS_1422
            APL: APL_1202
            XFA: XF1774
            XFT: PD0577(dcm)
            XCB: XC_2063
            XCV: XCV2286 XCV2345 XCV2405 XCVd0145
            XAC: XAC2213
            XOO: XOO0607
            VCH: VCA0198
            PPU: PP_3989
            PAR: Psyc_0401(dcm)
            SPL: Spea_1270
            SHE: Shewmr4_3202
            PAT: Patl_0727
            LPF: lpl0145
            LPP: lpp1078
            MCA: MCA1616
            FTA: FTA_1963 FTA_1964 FTA_1965
            HHA: Hhal_0414
            HCH: HCH_02488
            ABO: ABO_0129(rsmB)
            MMW: Mmwyl1_4374
            AHA: AHA_1077
            NME: NMB0725 NMB0826 NMB1033 NMB1290
            NMA: NMA0193 NMA0427 NMA1035(nmgII) NMA1453 NMA1500
            NGO: NGO0365 NGO0676 NGO1209 NGO1795(dcmB) NGO1894 NGO1991(ngoIM)
            RSO: RSc3438(RS01819)
            BXE: Bxe_A1222 Bxe_A3354
            BVI: Bcep1808_2131
            BCN: Bcen_2558
            BCH: Bcen2424_0006
            BPL: BURPS1106A_3681
            BTE: BTH_II1364
            BBR: BB1668
            RFR: Rfer_3077
            PNA: Pnap_4973
            AJS: Ajs_0566 Ajs_2196 Ajs_4252
            VEI: Veis_1175
            HAR: HEAR1841
            NET: Neut_0115
            EBA: ebA6339(dcm)
            AZO: azo0354
            HPY: HP0051(ddeM) HP0054 HP1121(BSP6IM)
            HPJ: jhp0435 jhp1050
            HPA: HPAG1_0047 HPAG1_0051 HPAG1_0460 HPAG1_1059
            HAC: Hac_0091(DDEM_fragment_4) Hac_0093(DDEM_fragment_2)
                 Hac_0283(dcm) Hac_0360 Hac_0595(BSP6IM) Hac_1213
            TDN: Tmden_0121 Tmden_1565 Tmden_1839 Tmden_1855
            CCV: CCV52592_0047
            CHA: CHAB381_0056
            CCO: CCC13826_0819
            ABU: Abu_1481
            PCA: Pcar_0419
            PPD: Ppro_3855
            DVU: DVU2842
            LIP: LI0389
            DPS: DP2034
            ADE: Adeh_3442
            MXA: MXAN_3598
            SFU: Sfum_1322 Sfum_2797
            RFE: RF_0138
            SME: SMc03763
            RET: RHE_PF00108(ypf00052)
            RLE: RL1932
            OAN: Oant_0230
            BBT: BBta_1159
            RPB: RPB_0472 RPB_2193 RPB_3325
            RPC: RPC_4309
            RPD: RPD_1972
            RPE: RPE_3254
            CCR: CC_1033
            SIL: SPO1049
            RSP: RSP_3758
            RSH: Rsph17029_3387
            JAN: Jann_2858 Jann_2889
            RDE: RD1_C0014
            MMR: Mmar10_2163 Mmar10_3057
            SWI: Swit_2462 Swit_2535
            ACR: Acry_3325 Acry_3583
            ABA: Acid345_1127 Acid345_4264
            BSU: BG12627(mtbP)
            BHA: BH3508
            BCE: BC0941
            BCA: BCE_0365
            BCY: Bcer98_0182 Bcer98_0752 Bcer98_2446 Bcer98_3357
            BTK: BT9727_0840(ddeI) BT9727_0841(hpaII)
            BPU: BPUM_0561(ydiP) BPUM_0656
            OIH: OB0173 OB3333 OB3336
            SAB: SAB2369c
            SER: SERP1523
            LWE: lwe0291(lcmA)
            SPZ: M5005_Spy_0800
            SPH: MGAS10270_Spy0913
            SPI: MGAS10750_Spy0948
            SPJ: MGAS2096_Spy0872
            SPK: MGAS9429_Spy0915
            SPA: M6_Spy1143 M6_Spy1160
            SPB: M28_Spy0774
            SPN: SP_1336
            SAG: SAG1297 SAG1869
            SAN: gbs1370
            SAK: SAK_0739
            SSA: SSA_1812
            LBU: LBUL_1142
            EFA: EF2340
            STH: STH1310
            CAC: CAC1222 CAC1501
            CPF: CPF_0139 CPF_1017(dcm) CPF_1018(dcm)
            CTH: Cthe_1728 Cthe_1749 Cthe_2320
            CBF: CLI_2130
            AMT: Amet_0966 Amet_3394 Amet_3816
            MPU: MYPU_0430 MYPU_0440 MYPU_1850 MYPU_1860
            MPE: MYPE4940 MYPE9800
            MMY: MSC_0216(dcm)
            MHY: mhp633
            MHJ: MHJ_0615(ddeM)
            MHP: MHP7448_0614(ddeM)
            MSY: MS53_0440
            UUR: UU528(dcm)
            MVA: Mvan_1093
            MMC: Mmcs_0817
            MKM: Mkms_0833
            MJL: Mjls_0824
            CGL: NCgl1703(cgl1776)
            CGB: cg1996(cglIM)
            RHA: RHA1_ro04149
            NCA: Noca_2284
            FAL: FRAAL0689
            SEN: SACE_1123 SACE_1558
            BLO: BL1473
            BAD: BAD_1283(kpn2kIM)
            RXY: Rxyl_2232
            SYN: slr0214
            SYC: syc1644_d
            SYF: Synpcc7942_2460
            ANA: alr2276(dmtC) alr4173(dmtD,avaIXM,dmnC) alr4815(avaIVM)
            AVA: Ava_0101 Ava_0731 Ava_B0330 Ava_C0232
            PMB: A9601_04331(dcm)
            PMC: P9515_04441(dcm)
            TER: Tery_0531 Tery_4525 Tery_4652 Tery_4678 Tery_4810
            BTH: BT_4754
            BFR: BF3681
            FPS: FP0736 FP0858 FP2150 FP2274(hpaIIM)
            CCH: Cag_1628
            CPH: Cpha266_0080 Cpha266_0083
            PVI: Cvib_0062 Cvib_0077
            RCA: Rcas_2076 Rcas_3651
            AAE: aq_644
            TPT: Tpet_1563
            MJA: MJ0563 MJ1200
            MMP: MMP0011
            MMQ: MmarC5_1673
            MMZ: MmarC7_1008
            MAE: Maeo_0459
            MMA: MM_0278
            MTH: MTH495
            MSI: Msm_0531
            MKA: MK1520(dcm)
            PHO: PH0039
            PAB: PAB2317
            PFU: PF0049
            RCI: RCIX2529(dcm)
            APE: APE_0872.1 APE_2002
            SMR: Smar_0919
            SSO: SSO0265
            STO: ST0335
            SAI: Saci_0651
            MSE: Msed_1513
            PAI: PAE1659 PAE3201
            PIS: Pisl_1675
            PCL: Pcal_0576
            PAS: Pars_1839
            TPE: Tpen_0416
STRUCTURES  PDB: 1G55  1HMY  1KHC  1SKM  1SVU  2C7O  2C7P  2C7Q  2C7R  2Z6A  
                 2Z6Q  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.37
            ExPASy - ENZYME nomenclature database: 2.1.1.37
            ExplorEnz - The Enzyme Database: 2.1.1.37
            ERGO genome analysis and discovery system: 2.1.1.37
            BRENDA, the Enzyme Database: 2.1.1.37
            CAS: 9037-42-7
///
ENTRY       EC 2.1.1.38                 Enzyme
NAME        O-demethylpuromycin O-methyltransferase;
            O-demethylpuromycin methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:O-demethylpuromycin O-methyltransferase
REACTION    S-adenosyl-L-methionine + O-demethylpuromycin =
            S-adenosyl-L-homocysteine + puromycin [RN:R03633]
ALL_REAC    R03633;
            (other) R05676
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            O-demethylpuromycin [CPD:C02864]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            puromycin [CPD:C01610]
COMMENT     Puromycin is the antibiotic derived from N6-dimethyladenosine by
            replacing the 3'-hydroxy group with an amino group and acylating
            this with 4-O-methyltyrosine.
REFERENCE   1  [PMID:5773275]
  AUTHORS   Rao MM, Rebello PF, Pogell BM.
  TITLE     Biosynthesis of puromycin in Streptomyces alboniger. Enzymatic
            methylation of O-demethylpuromycin.
  JOURNAL   J. Biol. Chem. 244 (1969) 112-8.
  ORGANISM  Streptomyces alboniger
PATHWAY     PATH: map00231  Puromycin biosynthesis
GENES       YEN: YE1418
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.38
            ExPASy - ENZYME nomenclature database: 2.1.1.38
            ExplorEnz - The Enzyme Database: 2.1.1.38
            ERGO genome analysis and discovery system: 2.1.1.38
            BRENDA, the Enzyme Database: 2.1.1.38
            CAS: 37257-04-8
///
ENTRY       EC 2.1.1.39                 Enzyme
NAME        inositol 3-methyltransferase;
            inositol L-1-methyltransferase;
            myo-inositol 1-methyltransferase;
            S-adenosylmethionine:myo-inositol 1-methyltransferase;
            myo-inositol 1-O-methyltransferase (name based on 1L-numbering
            system and not 1D-numbering);
            S-adenosyl-L-methionine:myo-inositol 1-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:1D-myo-inositol 3-O-methyltransferase
REACTION    S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine +
            1D-3-O-methyl-myo-inositol [RN:R01189]
ALL_REAC    R01189
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            myo-inositol [CPD:C00137]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            1D-3-O-methyl-myo-inositol [CPD:C03660]
REFERENCE   1  [PMID:5362621]
  AUTHORS   Hofmann H, Wagner I, Hoffmann-Ostenhof O.
  TITLE     [Biosynthesis of cyclitols. XXIV. A soluble enzyme from Vinca rosea
            methylating myo-inositol to L-bornesitol]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 350 (1969) 1465-8.
  ORGANISM  Vinca rosea
PATHWAY     PATH: map00562  Inositol phosphate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.39
            ExPASy - ENZYME nomenclature database: 2.1.1.39
            ExplorEnz - The Enzyme Database: 2.1.1.39
            ERGO genome analysis and discovery system: 2.1.1.39
            BRENDA, the Enzyme Database: 2.1.1.39
            CAS: 37257-05-9
///
ENTRY       EC 2.1.1.40                 Enzyme
NAME        inositol 1-methyltransferase;
            inositol D-1-methyltransferase;
            S-adenosylmethionine:myo-inositol 3-methyltransferase;
            myo-inositol 3-O-methyltransferase;
            inositol 3-O-methyltransferase (name based on 1L-numbering system
            and not 1D-numbering);
            S-adenosyl-L-methionine:myo-inositol 3-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:1D-myo-inositol 1-O-methyltransferase
REACTION    S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine +
            1D-1-O-methyl-myo-inositol [RN:R01188]
ALL_REAC    R01188
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            myo-inositol [CPD:C00137]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            1D-1-O-methyl-myo-inositol [CPD:C03659]
REFERENCE   1  [PMID:5362620]
  AUTHORS   Wagner I, Hofmann H, Hoffmann-Ostenhof O.
  TITLE     [Biosynthesis of cyclitols. 23. A soluble enzyme from pea seedlings
            methylating myo-inositol to D-bornesitol]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 350 (1969) 1460-4.
  ORGANISM  Pisum sativum
PATHWAY     PATH: map00562  Inositol phosphate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.40
            ExPASy - ENZYME nomenclature database: 2.1.1.40
            ExplorEnz - The Enzyme Database: 2.1.1.40
            ERGO genome analysis and discovery system: 2.1.1.40
            BRENDA, the Enzyme Database: 2.1.1.40
            CAS: 37257-06-0
///
ENTRY       EC 2.1.1.41                 Enzyme
NAME        sterol 24-C-methyltransferase;
            Delta24-methyltransferase;
            Delta24-sterol methyltransferase;
            zymosterol-24-methyltransferase;
            S-adenosyl-4-methionine:sterol Delta24-methyltransferase;
            SMT1;
            24-sterol C-methyltransferase;
            S-adenosyl-L-methionine:Delta24(23)-sterol methyltransferase;
            phytosterol methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:zymosterol 24-C-methyltransferase
REACTION    S-adenosyl-L-methionine + 5alpha-cholesta-8,24-dien-3beta-ol =
            S-adenosyl-L-homocysteine +
            24-methylene-5alpha-cholest-8-en-3beta-ol [RN:R04427]
ALL_REAC    R04427;
            (other) R07481
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            5alpha-cholesta-8,24-dien-3beta-ol [CPD:C05437]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            24-methylene-5alpha-cholest-8-en-3beta-ol [CPD:C04525]
COFACTOR    Glutathione [CPD:C00051]
COMMENT     Requires glutathione. Acts on a range of sterols with a
            24(25)-double bond in the sidechain. While zymosterol is the
            preferred substrate it also acts on desmosterol,
            5alpha-cholesta-7,24-dien-3beta-ol,
            5alpha-cholesta-5,7,24-trien-3beta-ol, 4alpha-methylzymosterol and
            others. S-Adenosyl-L-methionine attacks the Si-face of the 24(25)
            double bond and the C-24 hydrogen is transferred to C-25 on the Re
            face of the double bond.
REFERENCE   1  [PMID:5354959]
  AUTHORS   Moore JT, Gaylor JL.
  TITLE     Isolation and purification of an S-adenosylmethionine: delta
            24-sterol methyltransferase from yeast.
  JOURNAL   J. Biol. Chem. 244 (1969) 6334-40.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:8597586]
  AUTHORS   Venkatramesh M, Guo DA, Jia Z, Nes WD.
  TITLE     Mechanism and structural requirements for transformation of
            substrates by the (S)-adenosyl-L-methionine:delta 24(25)-sterol
            methyl transferase from Saccharomyces cerevisiae.
  JOURNAL   Biochim. Biophys. Acta. 1299 (1996) 313-24.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Tong, Y., McCourt, B.S., Guo, D., Mangla, A.T., Zhou, W.X., Jenkins,
            M.D., Zhou, W., Lopez, M. and Nes, W.D.
  TITLE     , Stereochemical features of C-methylation on the path to
            Delta24(28)-methylene and Delta24(28)-ethylidene sterols: studies on
            the recombinant phytosterol methyl transferase from Arabidopsis
            thaliana.
  JOURNAL   Tetrahedron Lett. 38 (1997) 6115-6118.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   4  [PMID:9746350]
  AUTHORS   Bouvier-Nave P, Husselstein T, Benveniste P.
  TITLE     Two families of sterol methyltransferases are involved in the first
            and the second methylation steps of plant sterol biosynthesis.
  JOURNAL   Eur. J. Biochem. 256 (1998) 88-96.
  ORGANISM  Nicotiana tabacum
REFERENCE   5  [PMID:9606964]
  AUTHORS   Nes WD, McCourt BS, Zhou WX, Ma J, Marshall JA, Peek LA, Brennan M.
  TITLE     Overexpression, purification, and stereochemical studies of the
            recombinant (S)-adenosyl-L-methionine: delta 24(25)- to delta
            24(28)-sterol methyl transferase enzyme from Saccharomyces
            cerevisiae.
  JOURNAL   Arch. Biochem. Biophys. 353 (1998) 297-311.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K00559  sterol 24-C-methyltransferase
GENES       ATH: AT5G13710(SMT1)
            OSA: 4342690
            CME: CMP275C
            SCE: YML008C(ERG6)
            AGO: AGOS_ADR196W
            PIC: PICST_80971
            CAL: CaO19_1631(CaO19.1631)
            CGR: CAGL0H04653g
            SPO: SPBC16E9.05
            ANI: AN7146.2
            AFM: AFUA_4G03630 AFUA_4G09190
            AOR: AO090011000289
            CNE: CNB03100
            UMA: UM03182.1
            DDI: DDBDRAFT_0188166
            TBR: Tb10.6k15.3820
            TCR: 504191.10 505683.10 510185.10
            LMA: LmjF36.2380 LmjF36.2390
            NOC: Noc_0994
            HMA: pNG6036(mitN)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.41
            ExPASy - ENZYME nomenclature database: 2.1.1.41
            ExplorEnz - The Enzyme Database: 2.1.1.41
            ERGO genome analysis and discovery system: 2.1.1.41
            BRENDA, the Enzyme Database: 2.1.1.41
            CAS: 37257-07-1
///
ENTRY       EC 2.1.1.42                 Enzyme
NAME        luteolin O-methyltransferase;
            o-dihydric phenol methyltransferase;
            luteolin methyltransferase;
            luteolin 3'-O-methyltransferase;
            o-diphenol m-O-methyltransferase;
            o-dihydric phenol meta-O-methyltransferase;
            S-adenosylmethionine:flavone/flavonol 3'-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:5,7,3',4'-tetrahydroxyflavone
            3'-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavone =
            S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavone
            [RN:R03587]
ALL_REAC    R03587
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            5,7,3',4'-tetrahydroxyflavone [CPD:C01514]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            5,7,4'-trihydroxy-3'-methoxyflavone [CPD:C04293]
COMMENT     Also acts on luteolin 7-O-beta-D-glucoside.
REFERENCE   1  [PMID:5026305]
  AUTHORS   Ebel J, Hahlbrock K, Grisebach H.
  TITLE     Purification and properties of an o-dihydricphenol
            meta-O-methyltransferase from cell suspension cultures of parsley
            and its relation to flavonoid biosynthesis.
  JOURNAL   Biochim. Biophys. Acta. 268 (1972) 313-26.
  ORGANISM  Petroselinum hortense
PATHWAY     PATH: map00941  Flavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.42
            ExPASy - ENZYME nomenclature database: 2.1.1.42
            ExplorEnz - The Enzyme Database: 2.1.1.42
            ERGO genome analysis and discovery system: 2.1.1.42
            BRENDA, the Enzyme Database: 2.1.1.42
            CAS: 37205-55-3
///
ENTRY       EC 2.1.1.43                 Enzyme
NAME        histone-lysine N-methyltransferase;
            protein methylase III;
            protein methylase 3;
            protein (lysine) methyltransferase;
            protein methyltransferase II;
            protein-lysine N-methyltransferase;
            histone H1-specific S-adenosylmethionine:protein-lysine
            N-methyltransferase;
            S-adenosyl-L-methionine:histone-L-lysine 6-N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:histone-L-lysine N6-methyltransferase
REACTION    S-adenosyl-L-methionine + histone L-lysine =
            S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
ALL_REAC    R03938;
            (other) R03875 R04866 R04867
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            histone L-lysine
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            histone N6-methyl-L-lysine [CPD:C03702]
COMMENT     One of a group of enzymes methylating proteins; see also EC
            2.1.1.59, [cytochrome-c]-lysine N-methyltransferase and EC 2.1.1.60,
            calmodulin-lysine N-methyltransferase.
REFERENCE   1  [PMID:5484460]
  AUTHORS   Paik WK, Kim S.
  TITLE     Solubilization and partial purification of protein methylase 3 from
            calf thymus nuclei.
  JOURNAL   J. Biol. Chem. 245 (1970) 6010-5.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:391266]
  AUTHORS   Venkatesan M, McManus IR.
  TITLE     Partial purification and characterization of a protein lysine
            methyltransferase from plasmodia of Physarum polycephalum.
  JOURNAL   Biochemistry. 18 (1979) 5365-71.
  ORGANISM  Physarum polycephalum
PATHWAY     PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K05302  histone-lysine N-methyltransferase
GENES       HSA: 10919(EHMT2) 64324(NSD1) 6839(SUV39H1) 79723(SUV39H2)
                 79813(EHMT1) 80854(SETD7) 84444(DOT1L) 9739(SETD1A)
                 9869(SETDB1)
            PTR: 462572(EHMT2) 465618(LOC465618) 469481(SETDB1)
            MMU: 110147(Ehmt2) 20937(Suv39h1) 64707(Suv39h2) 73251(Setd7)
                 84505(Setdb1)
            CFA: 474851(EHMT2) 476079(SETD7) 477995(SUV39H2) 483186(LOC483186)
                 491224(LOC491224) 491868(LOC491868)
            GGA: 395847(SETDB1) 417250(EHMT1) 422443(SETD7)
                 426314(RCJMB04_5f7)
            DME: Dmel_CG10272(gpp) Dmel_CG2995 Dmel_CG6476(Su(var)3-9)
            AGO: AGOS_ABR136W
            PIC: PICST_44298(RMS1)
            CAL: CaO19_13430(CaO19.13430)
            SPO: SPBC428.08c(clr4) SPCC306.04c
            ANI: AN5795.2
            AFM: AFUA_1G11090 AFUA_5G12110 AFUA_6G06335
            AOR: AO090003000002 AO090038000300 AO090120000327
            CNE: CND03610 CNH00720
            UMA: UM02677.1
            DDI: DDBDRAFT_0187845
            BUR: Bcep18194_A3254
            BRA: BRADO5005
            BBT: BBta_5473
            NWI: Nwi_2161
STRUCTURES  PDB: 1H3I  1ML9  1MT6  1MUF  1O9S  1PEG  1U2Z  1XQH  1ZKK  2BQZ  
                 2F69  2IGQ  2J8A  2O8J  2QXV  2R3A  2YSM  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.43
            ExPASy - ENZYME nomenclature database: 2.1.1.43
            ExplorEnz - The Enzyme Database: 2.1.1.43
            ERGO genome analysis and discovery system: 2.1.1.43
            BRENDA, the Enzyme Database: 2.1.1.43
            CAS: 9055-08-7
///
ENTRY       EC 2.1.1.44                 Enzyme
NAME        dimethylhistidine N-methyltransferase;
            dimethylhistidine methyltransferase;
            histidine-alpha-N-methyltransferase;
            S-adenosyl-L-methionine:alpha-N,alpha-N-dimethyl-L-histidine
            alpha-N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:Nalpha,Nalpha-dimethyl-L-histidine
            Nalpha-methyltransferase
REACTION    S-adenosyl-L-methionine + Nalpha,Nalpha-dimethyl-L-histidine =
            S-adenosyl-L-homocysteine +
            Nalpha,Nalpha,Nalpha-trimethyl-L-histidine [RN:R04436]
ALL_REAC    R04436
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            Nalpha,Nalpha-dimethyl-L-histidine [CPD:C04259]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            Nalpha,Nalpha,Nalpha-trimethyl-L-histidine [CPD:C05575]
COMMENT     Methylhistidine and histidine can also act as methyl acceptors, with
            trimethylhistidine being formed in both cases.
REFERENCE   1  [PMID:5484456]
  AUTHORS   Ishikawa Y, Melville DB.
  TITLE     The enzymatic alpha-N-methylation of histidine.
  JOURNAL   J. Biol. Chem. 245 (1970) 5967-73.
  ORGANISM  Neurospora crassa [GN:dncr]
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.44
            ExPASy - ENZYME nomenclature database: 2.1.1.44
            ExplorEnz - The Enzyme Database: 2.1.1.44
            ERGO genome analysis and discovery system: 2.1.1.44
            BRENDA, the Enzyme Database: 2.1.1.44
            CAS: 62213-53-0
///
ENTRY       EC 2.1.1.45                 Enzyme
NAME        thymidylate synthase;
            dTMP synthase;
            thymidylate synthetase;
            methylenetetrahydrofolate:dUMP C-methyltransferase;
            TMP synthetase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     5,10-methylenetetrahydrofolate:dUMP C-methyltransferase
REACTION    5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
            [RN:R02101]
ALL_REAC    R02101
SUBSTRATE   5,10-methylenetetrahydrofolate [CPD:C00143];
            dUMP [CPD:C00365]
PRODUCT     dihydrofolate [CPD:C00415];
            dTMP [CPD:C00364]
INHIBITOR   5-Fluorodeoxyuridine monophosphate [CPD:C04242]
REFERENCE   1
  AUTHORS   Blakley, R.L.
  TITLE     The biosynthesis of thymidylic acid. IV. Further studies on
            thymidylate synthase.
  JOURNAL   J. Biol. Chem. 238 (1963) 2113-2118.
  ORGANISM  Escherichia coli [GN:eco], Streptococcus faecalis
REFERENCE   2  [PMID:34155]
  AUTHORS   Lockshin A, Moran RG, Danenberg PV.
  TITLE     Thymidylate synthetase purified to homogeneity from human leukemic
            cells.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 750-4.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:6990200]
  AUTHORS   Slavik K, Slavikova V.
  TITLE     Purification of thymidylate synthetase from enzyme-poor sources by
            affinity chromatography.
  JOURNAL   Methods. Enzymol. 66 (1980) 709-23.
REFERENCE   4
  AUTHORS   Wahba, A.J. and Friedkin, M.
  TITLE     The enzymatic synthesis of thymidylate. I. Early steps in the
            purification of thymidylate synthetase of Escherichia coli.
  JOURNAL   J. Biol. Chem. 237 (1962) 3794-3801.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00240  Pyrimidine metabolism
            PATH: map00670  One carbon pool by folate
ORTHOLOGY   KO: K00560  thymidylate synthase
GENES       HSA: 7298(TYMS)
            MMU: 22171(Tyms)
            RNO: 29261(Tyms)
            CFA: 476100(LOC476100) 607417(LOC607417)
            GGA: 421060(TYMS)
            SPU: 592043(LOC592043) 593137(LOC593137)
            DME: Dmel_CG3181
            CEL: Y110A7A.4
            ATH: AT2G16370(THY-1)
            OSA: 4350527
            CME: CMS462C
            SCE: YOR074C(CDC21)
            AGO: AGOS_ADR219C
            PIC: PICST_37780(TMP1)
            CGR: CAGL0K05467g
            SPO: SPAC15E1.04
            CNE: CNJ01230
            ECU: ECU08_0090
            PFA: PFD0805w
            CPV: cgd4_4460
            CHO: Chro.40506
            TAN: TA08775
            TPV: TP04_0504
            TET: TTHERM_00312120
            TBR: Tb927.7.5480
            TCR: 509153.90 510303.320
            LMA: LmjF06.0860
            ECO: b2827(thyA)
            ECJ: JW2795(thyA)
            ECE: Z4144(thyA)
            ECS: ECs3684
            ECC: c3422(thyA)
            ECI: UTI89_C3229(thyA)
            ECP: ECP_2840
            ECV: APECO1_3678(thyA)
            ECW: EcE24377A_3147(thyA)
            ECX: EcHS_A2973(thyA)
            STY: STY3142(thyA)
            STT: t2910(thyA)
            SPT: SPA2866(thyA)
            SEC: SC2940(thyA)
            STM: STM3001(thyA)
            YPE: YPO0783(thyA)
            YPK: y3171(thyA)
            YPM: YP_2875(thyA)
            YPA: YPA_0485
            YPN: YPN_2988
            YPP: YPDSF_1702
            YPS: YPTB3033(thyA)
            YPI: YpsIP31758_0984(thyA)
            SFL: SF2837(thyA)
            SFX: S3035(thyA)
            SFV: SFV_2905(thyA)
            SSN: SSON_2984(thyA)
            SBO: SBO_2719(thyA)
            SDY: SDY_3044(thyA)
            ECA: ECA0988(thyA)
            PLU: plu0623(thyA)
            BUC: BU440(thyA)
            BAS: BUsg425(thyA)
            BAB: bbp386(thyA)
            WBR: WGLp320(thyA)
            SGL: SG1977
            ENT: Ent638_3269
            KPN: KPN_03236(thyA)
            SPE: Spro_3821
            HIT: NTHI1072(thyA)
            HIP: CGSHiEE_07500(thyA)
            HDU: HD1005(thyA)
            HSO: HS_1619(thyA)
            PMU: PM0079(thyA)
            MSU: MS0405(thyA)
            APL: APL_0115(thyA)
            ASU: Asuc_0725
            XFA: XF2332
            XFT: PD1364(thyA)
            XCC: XCC0787(thyA)
            XCB: XC_3444
            XCV: XCV0895(thyA)
            XAC: XAC0842(thyA)
            XOO: XOO3752(thyA)
            XOM: XOO_3543(XOO3543)
            VCH: VC0675
            VCO: VC0395_A0207(thyA)
            VVU: VV1_0516
            VVY: VV0679
            VPA: VP0524
            VFI: VF0460
            PPR: PBPRA0581(thyA)
            PAE: PA0342(thyA)
            PAU: PA14_04480(thyA)
            PAP: PSPA7_0436(thyA)
            PPU: PP_5141(thyA)
            PPF: Pput_5043 Pput_5048
            PST: PSPTO_5282(thyA)
            PSB: Psyr_4840
            PSP: PSPPH_4623 PSPPH_4872(thyA)
            PFL: PFL_5895(thyA)
            PFO: Pfl_5373
            PEN: PSEEN5234(thyA)
            PMY: Pmen_4213
            PAR: Psyc_2011(thyA)
            PCR: Pcryo_2314
            PRW: PsycPRwf_2331
            ACI: ACIAD0515(thyA)
            SON: SO_1335(thyA)
            SDN: Sden_2779
            SFR: Sfri_2942
            SAZ: Sama_0867
            SBL: Sbal_1188
            SBM: Shew185_1232
            SLO: Shew_1041
            SPC: Sputcn32_1146
            SSE: Ssed_1135
            SPL: Spea_1024
            SHE: Shewmr4_2861
            SHM: Shewmr7_2943
            SHW: Sputw3181_3018
            ILO: IL0507(thyA)
            CPS: CPS_3621(thyA)
            PHA: PSHAa0749(thyA)
            PAT: Patl_3837
            SDE: Sde_0350
            PIN: Ping_0506
            MAQ: Maqu_2432
            CBU: CBU_1547(thyA)
            CBD: COXBU7E912_0442(thyA)
            LPN: lpg2868(thyA)
            LPF: lpl2781(thyA)
            LPP: lpp2927(thyA)
            MCA: MCA2728(thyA)
            FTU: FTT1229(thyA)
            FTF: FTF1229(thyA)
            FTW: FTW_0717(thyA)
            FTL: FTL_0715
            FTH: FTH_0717(thyA)
            FTA: FTA_0755(thyA)
            FTN: FTN_1248(thyA)
            TCX: Tcr_0572
            NOC: Noc_0234
            AEH: Mlg_0371
            HHA: Hhal_2047
            HCH: HCH_05857(thiA)
            CSA: Csal_2572
            ABO: ABO_2344(thyA)
            MMW: Mmwyl1_3742
            AHA: AHA_0675(thyA)
            DNO: DNO_0569(thyA)
            BCI: BCI_0544(thyA)
            RMA: Rmag_0616
            VOK: COSY_0568(thyA)
            NME: NMB1709
            NMA: NMA1963(thyA)
            NMC: NMC1624(thyA)
            NGO: NGO1357
            CVI: CV_1027(thyA)
            RSO: RSc0947(thyA)
            REU: Reut_A0915
            REH: H16_A2703(thyA)
            RME: Rmet_2568
            BMA: BMA0382(thyA)
            BMV: BMASAVP1_A2523(thyA)
            BML: BMA10299_A0897(thyA)
            BMN: BMA10247_0251(thyA)
            BXE: Bxe_A0214 Bxe_A1031
            BVI: Bcep1808_1005
            BUR: Bcep18194_A4199
            BCN: Bcen_0606
            BCH: Bcen2424_1085
            BAM: Bamb_0961
            BPS: BPSL2473 BPSS1106
            BPM: BURPS1710b_2946(thyA) BURPS1710b_A0064
            BPL: BURPS1106A_2895(thyA)
            BPD: BURPS668_2833(thyA)
            BTE: BTH_I1680(thyA) BTH_II1303
            PNU: Pnuc_0381
            BPE: BP3154
            BPA: BPP0787
            BBR: BB0872
            RFR: Rfer_1063 Rfer_2986
            POL: Bpro_1823
            PNA: Pnap_2772
            AAV: Aave_1450
            AJS: Ajs_1197
            VEI: Veis_3172
            MPT: Mpe_A2051 Mpe_B0137
            HAR: HEAR1056(thyA)
            MMS: mma_1193(thyA)
            NEU: NE0568(thyB)
            NET: Neut_1021
            NMU: Nmul_A1962
            EBA: ebA4415(thyA)
            AZO: azo3197(thyA)
            DAR: Daro_0593
            TBD: Tbd_2040
            MFA: Mfla_0906 Mfla_1050
            BBA: Bd3230(thyA)
            MXA: MXAN_5942(thyA)
            RTY: RT0292(thyA)
            MLO: mll1467
            MES: Meso_1751
            PLA: Plav_2448
            SME: SMc01444(thyA)
            SMD: Smed_2021
            ATU: Atu2047(thyA)
            ATC: AGR_C_3709
            RET: RHE_CH02799(thyA)
            RLE: RL3256(thyA)
            BME: BMEI0608
            BMF: BAB1_1418(thyA)
            BMS: BR1399(thyA)
            BMB: BruAb1_1394(thyA)
            BOV: BOV_1355(thyA)
            OAN: Oant_1792
            BJA: bll6512(thyA)
            BRA: BRADO5578(thyA)
            BBT: BBta_6100(thyA)
            RPA: RPA3493(thyA)
            RPB: RPB_2036
            RPC: RPC_3266
            RPD: RPD_3354
            RPE: RPE_2149 RPE_2150
            NWI: Nwi_2351
            NHA: Nham_2730
            BHE: BH10980(thyA)
            BQU: BQ08630(thyA)
            BBK: BARBAKC583_0926(thyA)
            XAU: Xaut_3514
            CCR: CC_2124
            SIT: TM1040_1729
            RSP: RSP_0390
            RSH: Rsph17029_2044
            RSQ: Rsph17025_0846
            RDE: RD1_1874(thyA)
            MMR: Mmar10_2027
            HNE: HNE_0459(thyB)
            ZMO: ZMO1755(thyB)
            NAR: Saro_1977
            SAL: Sala_1332
            SWI: Swit_3787
            ELI: ELI_05150
            MAG: amb1327
            BSU: BG10794(thyB) BG11190(thyA)
            BHA: BH3451(thyB)
            BAN: BA2236(thyA)
            BAR: GBAA2236(thyA)
            BAA: BA_2740
            BAT: BAS2082
            BCE: BC2191
            BCA: BCE_2266(thyA)
            BCZ: BCZK2020(thyA)
            BCY: Bcer98_1639
            BTK: BT9727_2020(thyA)
            BLI: BL02642(thyA)
            BLD: BLi02029(thyA)
            BCL: ABC2955(thyB)
            BAY: RBAM_019970(thyB)
            BPU: BPUM_1916(thyB)
            OIH: OB1740
            GKA: GK1776
            SAU: SA1260(thyA)
            SAV: SAV1427(thyA)
            SAM: MW1317(thyA)
            SAR: SAR1440(thyA)
            SAS: SAS1370
            SAC: SACOL1462(thyA)
            SAB: SAB1282c(thyA)
            SAA: SAUSA300_1320(thyA)
            SAO: SAOUHSC_01435
            SAJ: SaurJH9_1487
            SAH: SaurJH1_1516
            SEP: SE1120
            SER: SERP1003(thyA-1) SERP1582(thyA-2)
            SHA: SH1479(thyA)
            SSP: SSP1312
            LMO: lmo1874
            LMF: LMOf2365_1904(thyA)
            LIN: lin1988
            LWE: lwe1894(thyA)
            LLA: L182559(thyA)
            LLC: LACR_1631
            LLM: llmg_0964(thyA)
            SPY: SPy_0882(thyA)
            SPZ: M5005_Spy_0688(thyA)
            SPM: spyM18_0943(thyA)
            SPG: SpyM3_0601(thyA)
            SPS: SPs1252
            SPH: MGAS10270_Spy0746(thyA)
            SPI: MGAS10750_Spy0780(thyA)
            SPJ: MGAS2096_Spy0760(thyA)
            SPK: MGAS9429_Spy0744(thyA)
            SPF: SpyM51120(thyA)
            SPA: M6_Spy0705
            SPB: M28_Spy0668(thyA)
            SPN: SP_0669
            SPR: spr0585(thyA)
            SPD: SPD_0581(thyA)
            SAG: SAG1315(thyA)
            SAN: gbs1385(thyA)
            SAK: SAK_1346(thyA)
            SMU: SMU.944(thyA)
            STC: str0578(thyA)
            STL: stu0578(thyA)
            SSA: SSA_1091(thyA)
            SGO: SGO_1143(thyA)
            LPL: lp_1870(thyA)
            LJO: LJ1471
            LAC: LBA0901(thyA)
            LSA: LSA1001(thyA)
            LSL: LSL_0708(thyA)
            LDB: Ldb0787(thyA)
            LBU: LBUL_0720
            LBR: LVIS_0784
            LCA: LSEI_1387
            LRE: Lreu_0769
            EFA: EF1576(thyA)
            OOE: OEOE_0782
            STH: STH3117
            CAC: CAC3003(thyA)
            CTC: CTC02216
            CTH: Cthe_1227
            CBA: CLB_0810(thyA)
            CBH: CLC_0824(thyA)
            CBF: CLI_0854(thyA)
            CBE: Cbei_4952
            MGE: MG_227(thyA)
            MPN: MPN320(thyA)
            MPU: MYPU_5380(thyA)
            MPE: MYPE6870(thyA)
            MGA: MGA_0699(thyA)
            MMO: MMOB0340(thyA)
            MSY: MS53_0398(thyA)
            POY: PAM293(thyA)
            AYW: AYWB_430(thyA)
            MFL: Mfl419
            MTU: Rv2764c(thyA)
            MTC: MT2834(thyA)
            MBO: Mb2786c(thyA)
            MBB: BCG_2781c(thyA)
            MLE: ML1519(thyA)
            MPA: MAP2869c(thyA)
            MAV: MAV_3652(thyA)
            MSM: MSMEG_2670(thyA)
            MUL: MUL_2178(thyA)
            MVA: Mvan_2380
            MGI: Mflv_4007
            MMC: Mmcs_2112
            MKM: Mkms_2158
            MJL: Mjls_2099
            CGL: NCgl0810(cgl0844)
            CGB: cg0966(thyA)
            CEF: CE0919
            CDI: DIP0825(thyA)
            CJK: jk0441(thyA)
            NFA: nfa50220(thyA)
            RHA: RHA1_ro02248
            LXX: Lxx09930(thyA)
            ART: Arth_3018
            AAU: AAur_2992(thyA)
            PAC: PPA1672
            NCA: Noca_2311
            KRA: Krad_4439
            BLO: BL1665(thyA)
            BAD: BAD_0388(thyA)
            FNU: FN0240
            RBA: RB12614(thyA)
            LIL: LA0789
            BTH: BT_2047
            BFR: BF3734
            BFS: BF3523(thyB)
            PGI: PG2060(thyA)
            SRU: SRU_0419(thyA)
            CHU: CHU_1289(thyA)
            GFO: GFO_0288(thyA)
            FJO: Fjoh_1471
            FPS: FP0333(thyA)
            DET: DET0819
            DEH: cbdb_A796(thyA)
            DRA: DR_2630
            MMP: MMP0986(thyA) MMP1379(thyA)
            MMQ: MmarC5_0199
            MAC: MA4543(thyA)
            MBA: Mbar_A0890
            MMA: MM_1237
            MBU: Mbur_1079
            MTP: Mthe_0710
            MHU: Mhun_1795
            MST: Msp_1237(thyA)
            MSI: Msm_1734
            MKA: MK1370(thyA)
            HWA: HQ2456A(thyA)
            NPH: NP2924A(thyA)
            RCI: LRC337(thyA)
STRUCTURES  PDB: 1AIQ  1AJM  1AN5  1AOB  1AXW  1B02  1BDU  1BID  1BJG  1BKO  
                 1BKP  1BO7  1BO8  1BP0  1BP6  1BPJ  1BQ1  1BQ2  1BSF  1BSP  
                 1CI7  1DDU  1DNA  1EV5  1EV8  1EVF  1EVG  1F28  1F4B  1F4C  
                 1F4D  1F4E  1F4F  1F4G  1FFL  1FWM  1HVY  1HW3  1HW4  1HZW  
                 1I00  1J3I  1J3J  1J3K  1JG0  1JMF  1JMG  1JMH  1JMI  1JTQ  
                 1JTU  1JU6  1JUJ  1JUT  1KCE  1KZI  1KZJ  1LCA  1LCB  1LCE  
                 1NCE  1NJA  1NJB  1NJC  1NJD  1NJE  1QQQ  1QZF  1RTS  1SEJ  
                 1SYN  1TDA  1TDB  1TDC  1TDU  1THY  1TIS  1TJS  1TLC  1TLS  
                 1TRG  1TSD  1TSL  1TSM  1TSN  1TSV  1TSW  1TSX  1TSY  1TSZ  
                 1TVU  1TVV  1TVW  1TYS  1VZA  1VZB  1VZC  1VZD  1VZE  1YPV  
                 1ZPR  2A9W  2AAZ  2BBQ  2FTN  2FTO  2FTQ  2G86  2G89  2G8A  
                 2G8D  2G8M  2G8O  2G8X  2KCE  2OIP  2TDD  2TDM  2TSC  2TSR  
                 3TMS  4TMS  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.45
            ExPASy - ENZYME nomenclature database: 2.1.1.45
            ExplorEnz - The Enzyme Database: 2.1.1.45
            ERGO genome analysis and discovery system: 2.1.1.45
            BRENDA, the Enzyme Database: 2.1.1.45
            CAS: 9031-61-2
///
ENTRY       EC 2.1.1.46                 Enzyme
NAME        isoflavone 4'-O-methyltransferase;
            4'-hydroxyisoflavone methyltransferase;
            isoflavone methyltransferase;
            isoflavone O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:isoflavone 4'-O-methyltransferase
REACTION    S-adenosyl-L-methionine + an isoflavone = S-adenosyl-L-homocysteine
            + a 4'-O-methylisoflavone [RN:R07331]
ALL_REAC    R07331 > R02931 R06564
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            isoflavone [CPD:C00799]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            4'-O-methylisoflavone [CPD:C03074]
REFERENCE   1  [PMID:4452353]
  AUTHORS   Wengenmayer H, Ebel J, Grisebach H.
  TITLE     Purification and properties of a S-adenosylmethionine: isoflavone
            4'-O-methyltransferase from cell suspension cultures of Cicer
            arietinum L.
  JOURNAL   Eur. J. Biochem. 50 (1974) 135-43.
  ORGANISM  Cicer arietinum
PATHWAY     PATH: map00943  Isoflavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.46
            ExPASy - ENZYME nomenclature database: 2.1.1.46
            ExplorEnz - The Enzyme Database: 2.1.1.46
            ERGO genome analysis and discovery system: 2.1.1.46
            BRENDA, the Enzyme Database: 2.1.1.46
            CAS: 55071-80-2
///
ENTRY       EC 2.1.1.47                 Enzyme
NAME        indolepyruvate C-methyltransferase;
            indolepyruvate methyltransferase;
            indolepyruvate 3-methyltransferase;
            indolepyruvic acid methyltransferase;
            S-adenosyl-L-methionine:indolepyruvate C-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine: (indol-3-yl)pyruvate C-methyltransferase
REACTION    S-adenosyl-L-methionine + (indol-3-yl)pyruvate =
            S-adenosyl-L-homocysteine + (3S)-3-(indol-3-yl)-3-oxobutanoate
            [RN:R01972]
ALL_REAC    R01972;
            (other) R01973
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            (indol-3-yl)pyruvate [CPD:C00331]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            (3S)-3-(indol-3-yl)-3-oxobutanoate
REFERENCE   1  [PMID:5490210]
  AUTHORS   Hornemann U, Speedie MK, Hurley LH, Floss HG.
  TITLE     Demonstration of a C-methylating enzyme in cell free extracts of
            indolmycin-producing Streptomyces griseus.
  JOURNAL   Biochem. Biophys. Res. Commun. 39 (1970) 594-9.
  ORGANISM  Streptomyces griseus
PATHWAY     PATH: map00380  Tryptophan metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.47
            ExPASy - ENZYME nomenclature database: 2.1.1.47
            ExplorEnz - The Enzyme Database: 2.1.1.47
            ERGO genome analysis and discovery system: 2.1.1.47
            BRENDA, the Enzyme Database: 2.1.1.47
            CAS: 54576-88-4
///
ENTRY       EC 2.1.1.48                 Enzyme
NAME        rRNA (adenine-N6-)-methyltransferase;
            ribosomal ribonucleate adenine 6-methyltransferase;
            gene ksgA methyltransferase;
            ribonucleic acid-adenine (N6) methylase;
            ErmC 23S rRNA methyltransferase;
            S-adenosyl-L-methionine:rRNA (adenine-6-N-)-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:rRNA (adenine-N6-)-methyltransferase
REACTION    S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA
            containing N6-methyladenine [RN:R07232]
ALL_REAC    R07232
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            rRNA [CPD:C00240]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            rRNA containing N6-methyladenine [CPD:C04154]
COMMENT     Also methylates 2-aminoadenosine to 2-methylaminoadenosine.
REFERENCE   1  [PMID:4622906]
  AUTHORS   Sipe JE, Anderson WM Jr, Remy CN, Love SH.
  TITLE     Characterization of S-adenosylmethionine: ribosomal ribonucleic
            acid-adenine (N 6 -) methyltransferase of Escherichia coli strain B.
  JOURNAL   J. Bacteriol. 110 (1972) 81-91.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K00561  rRNA (adenine-N6-)-methyltransferase
GENES       TET: TTHERM_00726120
            PPF: Pput_0435
            PMY: Pmen_4013
            PHA: PSHAa2635(ksgA)
            PIN: Ping_1047
            MAQ: Maqu_3507
            NOC: Noc_1721
            NME: NMB0066
            BUR: Bcep18194_A6035
            VEI: Veis_4810
            HAR: HEAR0369(ksgA)
            GUR: Gura_2309
            PPD: Ppro_2492
            AMA: AM558(ksgA)
            NWI: Nwi_1682(ksgA)
            SUS: Acid_5541
            BHA: BH0380
            BCY: Bcer98_0036
            BCL: ABC3508
            OIH: OB0921
            SAU: SA0048(ermA) SA0766(ermA) SA1480(ermA) SA1951(ermA)
                 SA2384(ermA)
            SAV: SAV0052(ermA) SAV1655(ermA)
            SAR: SAR0050(ermA1) SAR1735(ermA2)
            SAA: SAUSA300_pUSA0307(ermC)
            SAJ: SaurJH9_0039 SaurJH9_1713
            SAH: SaurJH1_0039 SaurJH1_1747
            SER: SERP1220(ermA-1) SERP1343(ermA-2) SERP2510(ermA-3)
            SPI: MGAS10750_Spy1703
            LSA: LSA1655(ksgA)
            LRE: Lreu_0213
            EFA: EFA0007
            CTH: Cthe_2092
            CDF: CD2007(erm2(B)) CD2010(erm1(B))
            DRM: Dred_0077
            STP: Strop_3669
            AVA: Ava_4886(ksgA)
            CCH: Cag_1193
            CPH: Cpha266_1169
            PLT: Plut_1287
            DEB: DehaBAV1_0383
            RRS: RoseRS_0251
            RCA: Rcas_0285
            AAE: aq_262
            FNO: Fnod_0456
            MAE: Maeo_0376
            MTP: Mthe_0996
            MSI: Msm_1448
            AFU: AF2194
STRUCTURES  PDB: 1QAM  1QAN  1QAO  1QAQ  1YUB  2ERC  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.48
            ExPASy - ENZYME nomenclature database: 2.1.1.48
            ExplorEnz - The Enzyme Database: 2.1.1.48
            ERGO genome analysis and discovery system: 2.1.1.48
            BRENDA, the Enzyme Database: 2.1.1.48
            CAS: 9076-81-7
///
ENTRY       EC 2.1.1.49                 Enzyme
NAME        amine N-methyltransferase;
            nicotine N-methyltransferase;
            tryptamine N-methyltransferase;
            arylamine N-methyltransferase;
            tryptamine methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:amine N-methyltransferase
REACTION    S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a
            methylated amine [RN:R02808]
ALL_REAC    R02808 > R02174 R02910
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            amine [CPD:C00706]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            methylated amine [CPD:C02436]
COMMENT     An enzyme of very broad specificity; many primary, secondary and
            tertiary amines can act as acceptors, including tryptamine, aniline,
            nicotine and a variety of drugs and other xenobiotics.
REFERENCE   1  [PMID:3949799]
  AUTHORS   Ansher SS, Jakoby WB.
  TITLE     Amine N-methyltransferases from rabbit liver.
  JOURNAL   J. Biol. Chem. 261 (1986) 3996-4001.
  ORGANISM  rabbit
REFERENCE   2  [PMID:3377829]
  AUTHORS   Crooks PA, Godin CS, Damani LA, Ansher SS, Jakoby WB.
  TITLE     Formation of quaternary amines by N-methylation of azaheterocycles
            with homogeneous amine N-methyltransferases.
  JOURNAL   Biochem. Pharmacol. 37 (1988) 1673-7.
  ORGANISM  rabbit
PATHWAY     PATH: map00380  Tryptophan metabolism
ORTHOLOGY   KO: K00562  amine N-methyltransferase
GENES       HSA: 11185(INMT)
STRUCTURES  PDB: 2A14  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.49
            ExPASy - ENZYME nomenclature database: 2.1.1.49
            ExplorEnz - The Enzyme Database: 2.1.1.49
            ERGO genome analysis and discovery system: 2.1.1.49
            BRENDA, the Enzyme Database: 2.1.1.49
            CAS: 51377-47-0
///
ENTRY       EC 2.1.1.50                 Enzyme
NAME        loganate O-methyltransferase;
            loganate methyltransferase;
            S-adenosyl-L-methionine:loganic acid methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:loganate 11-O-methyltransferase
REACTION    S-adenosyl-L-methionine + loganate = S-adenosyl-L-homocysteine +
            loganin [RN:R03554]
ALL_REAC    R03554;
            (other) R05834
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            loganate [CPD:C01512]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            loganin [CPD:C01433]
COMMENT     Also acts on secologanate. Methylates the 11-carboxy group of the
            monoterpenoid loganate.
REFERENCE   1  [PMID:4698228]
  AUTHORS   Madyastha KM, Guarnaccia R, Baxter C, Coscia CJ.
  TITLE     S-Adenosyl-L-methionine: loganic acid methyltransferase. A
            carboxyl-alkylating enzyme from Vinca rosea.
  JOURNAL   J. Biol. Chem. 248 (1973) 2497-501.
  ORGANISM  Vinca rosea
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.50
            ExPASy - ENZYME nomenclature database: 2.1.1.50
            ExplorEnz - The Enzyme Database: 2.1.1.50
            ERGO genome analysis and discovery system: 2.1.1.50
            BRENDA, the Enzyme Database: 2.1.1.50
            CAS: 39391-10-1
///
ENTRY       EC 2.1.1.51                 Enzyme
NAME        rRNA (guanine-N1-)-methyltransferase;
            ribosomal ribonucleate guanine 1-methyltransferase;
            S-adenosyl-L-methionine:rRNA (guanine-1-N-)-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:rRNA (guanine-N1-)-methyltransferase
REACTION    S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA
            containing N1-methylguanine [RN:R07233]
ALL_REAC    R07233
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            rRNA [CPD:C00240]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            rRNA containing N1-methylguanine [CPD:C04152]
REFERENCE   1  [PMID:4580201]
  AUTHORS   Isaksson LA.
  TITLE     Partial purification of ribosomal RNA(m1G)- and rRNA(m2G)-methylases
            from Escherichia coli and demonstration of some proteins affecting
            their apparent activity.
  JOURNAL   Biochim. Biophys. Acta. 312 (1973) 122-33.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K00563  rRNA (guanine-N1-)-methyltransferase
GENES       PFA: PFB0855c
            ECO: b1822(rrmA)
            ECJ: JW1811(rrmA)
            ECE: Z2866(yebH)
            ECS: ECs2532
            ECC: c2229(yebH)
            ECI: UTI89_C2020(yebH)
            ECP: ECP_1765
            ECV: APECO1_879(yebH)
            ECW: EcE24377A_2049(rrmA)
            ECX: EcHS_A1912(rrmA)
            STY: STY1964(rrmA)
            STT: t1043(rrmA)
            SPT: SPA1038(rrmA)
            SEC: SC1829(rrmA)
            STM: STM1835(rrmA)
            YPE: YPO1748(rrmA)
            YPK: y2561
            YPM: YP_1488(rrmA)
            YPA: YPA_1122
            YPN: YPN_2374
            YPP: YPDSF_1375
            YPS: YPTB1626(rrmA)
            YPI: YpsIP31758_2376(rrmA)
            SFL: SF1404(rrmA)
            SFX: S1519(yebH)
            SFV: SFV_1406(yebH)
            SSN: SSON_1338(yebH)
            SBO: SBO_1235(yebH)
            SDY: SDY_1968(yebH)
            ECA: ECA2390(rrmA)
            PLU: plu2702(rrmA)
            SGL: SG1322
            ENT: Ent638_2391
            SPE: Spro_2820
            VCH: VC2003
            VVU: VV1_2021
            VVY: VV2392
            VPA: VP2160
            VFI: VF1796
            PPR: PBPRA2791
            PAE: PA1161(rrmA)
            PAU: PA14_49390(rrmA)
            PPU: PP_1524
            PPF: Pput_4200
            PST: PSPTO_1522
            PSB: Psyr_1330
            PSP: PSPPH_3851(rrmA)
            PFL: PFL_1164(rrmA)
            PFO: Pfl_1087
            PEN: PSEEN4233
            PMY: Pmen_3067
            PAR: Psyc_2050(rrmA)
            PCR: Pcryo_2374
            PRW: PsycPRwf_0138
            ACI: ACIAD3362(rrm)
            SON: SO_1294 SO_2788(rrmA)
            SDN: Sden_2286 Sden_2825
            SFR: Sfri_1692
            SAZ: Sama_1971
            SBL: Sbal_1707
            SBM: Shew185_1704
            SLO: Shew_1005 Shew_1613
            SPC: Sputcn32_1571
            SSE: Ssed_2615
            SPL: Spea_2486
            SHE: Shewmr4_2408 Shewmr4_2899
            SHM: Shewmr7_2478 Shewmr7_2981
            SHN: Shewana3_1087 Shewana3_1613 Shewana3_2570 Shewana3_3078
            SHW: Sputw3181_2451
            ILO: IL2509
            CPS: CPS_3174(rrmA)
            PHA: PSHAa1337
            PAT: Patl_3381
            SDE: Sde_1475
            PIN: Ping_3309
            MAQ: Maqu_1334
            ABO: ABO_0661(rrmA)
            MMW: Mmwyl1_1753
            DAR: Daro_3178
            TBD: Tbd_1059
            BSU: BG11151(yxjB)
            BLD: BLi01753 BLi01754(yxjB)
            BCL: ABC3306
            LMO: lmo1872
            LMF: LMOf2365_1902
            LIN: lin1986
            LLA: L55507(yuhD)
            LLC: LACR_1451 LACR_2254
            LLM: llmg_2246(rrmA)
            SPN: SP_2103
            SPR: spr1913(rrmA)
            SPD: SPD_1929(rrmA)
            SAG: SAG1778
            SAN: gbs1821
            SAK: SAK_1800
            STC: str1842(rrmA)
            STL: stu1842(rrmA)
            SSA: SSA_0173(rrmA)
            SGO: SGO_1930(rrmA)
            LPL: lp_2215(rrmA)
            LSA: LSA0478
            LSL: LSL_1137
            LBR: LVIS_1460
            LCA: LSEI_0913
            EFA: EF2666
            CTC: pE88_28(ctp27)
            CBE: Cbei_3998
            DSY: DSY0346
            CGB: cg1266(rrmA)
            CJK: jk1386(rrmA)
            RHA: RHA1_ro05973
            FAL: FRAAL0999
            SEN: SACE_1994(rrmA)
            RBA: RB11756(rrmA)
STRUCTURES  PDB: 1P91  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.51
            ExPASy - ENZYME nomenclature database: 2.1.1.51
            ExplorEnz - The Enzyme Database: 2.1.1.51
            ERGO genome analysis and discovery system: 2.1.1.51
            BRENDA, the Enzyme Database: 2.1.1.51
            CAS: 50812-25-4
///
ENTRY       EC 2.1.1.52                 Enzyme
NAME        rRNA (guanine-N2-)-methyltransferase;
            ribosomal ribonucleate guanine-2-methyltransferase;
            S-adenosyl-L-methionine:rRNA (guanine-2-N-)-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:rRNA (guanine-N2-)-methyltransferase
REACTION    S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA
            containing N2-methylguanine [RN:R07234]
ALL_REAC    R07234
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            rRNA [CPD:C00240]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            rRNA containing N2-methylguanine [CPD:C04153]
REFERENCE   1  [PMID:4580201]
  AUTHORS   Isaksson LA.
  TITLE     Partial purification of ribosomal RNA(m1G)- and rRNA(m2G)-methylases
            from Escherichia coli and demonstration of some proteins affecting
            their apparent activity.
  JOURNAL   Biochim. Biophys. Acta. 312 (1973) 122-33.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K00564  rRNA (guanine-N2-)-methyltransferase
GENES       OSA: 4340217
            ECO: b3084(ygjO) b4371(rsmC)
            ECJ: JW4333(rsmC)
            ECE: Z4437(ygjO) Z5972(yjjT)
            ECS: ECs3966 ECs5329
            ECC: c3842(ygjO) c5450(rsmC)
            ECI: UTI89_C3522(ygjO) UTI89_C5079(yjjT)
            ECP: ECP_3175 ECP_4754
            ECV: APECO1_2055(yjjT)
            ECW: EcE24377A_4966(rsmC)
            ECX: EcHS_A4605(rsmC)
            STY: STY3400(ygjO) STY4906
            STT: t3140(ygjO) t4599
            SPT: SPA3088(ygjO) SPA4370(rsmC)
            SEC: SC3167(ygjO) SC4405(rsmC)
            STM: STM3220(ygjO) STM4556(rsmC)
            YPE: YPO0427(rsmC) YPO0588
            YPK: y3590 y3753
            YPM: YP_2908(rsmC1) YP_3754(rsmC2)
            YPA: YPA_3200 YPA_3857
            YPN: YPN_0298 YPN_0457
            YPP: YPDSF_0375 YPDSF_3205
            YPS: YPTB0572(rsmC) YPTB3470
            SFL: SF3124(ygjO) SF4402(rsmC)
            SFX: S3331(ygjO) S4674(yjjT)
            SFV: SFV_3126(ygjO) SFV_4405(yjjT)
            SSN: SSON_3121(ygjO) SSON_4521(yjjT)
            SBO: SBO_2945(ygjO) SBO_4432(yjjT)
            SDY: SDY_3267(ygjO) SDY_4630(yjjT)
            ECA: ECA0654 ECA0735(rsmC)
            PLU: plu4252(rsmC)
            BUC: BU328(yjjT)
            BAS: BUsg319(yjjT)
            BAB: bbp305(rsmC)
            BCC: BCc_206(rsmC)
            SGL: SG0389
            ENT: Ent638_0530 Ent638_3540
            SPE: Spro_0649 Spro_4312
            HIN: HI0012
            HIT: NTHI0016(rsmC)
            HDU: HD0210(rsmC)
            PMU: PM0958
            MSU: MS1588(rsmC)
            APL: APL_2005(rsmC)
            ASU: Asuc_0933
            XCC: XCC3639(rsmC)
            XCB: XC_3710
            XCV: XCV3800(rsmC)
            XAC: XAC3679(rsmC)
            XOO: XOO0702(rsmC)
            XOM: XOO_0640(XOO0640)
            VCH: VC0623
            VVU: VV1_1675(rsmC) VV1_1819(rsmC)
            VVY: VV2592(rsmC) VV2731(rsmC)
            VPA: VP2477
            VFI: VF0723 VF2137
            PPR: PBPRA0527(rsmC) PBPRA0819
            PAE: PA4617 PA4627
            PAU: PA14_61090 PA14_61220(rsmC)
            PPU: PP_0761 PP_4648
            PPF: Pput_0789 Pput_4510
            PST: PSPTO_1146(rsmC) PSPTO_4645
            PSB: Psyr_0986 Psyr_4279
            PSP: PSPPH_1037(rsmC) PSPPH_4337
            PFL: PFL_5122 PFL_5361
            PFO: Pfl_4712 Pfl_4890
            PEN: PSEEN0906 PSEEN4774
            PMY: Pmen_0751 Pmen_3665
            ACI: ACIAD0701(rsmC)
            ACB: A1S_2837
            SON: SO_0828 SO_1097
            SDN: Sden_2937 Sden_2977
            SFR: Sfri_0540 Sfri_3101
            SAZ: Sama_0569 Sama_2548
            SBL: Sbal_0918 Sbal_3530
            SBM: Shew185_0806 Shew185_3444
            SLO: Shew_2886 Shew_3230
            SPC: Sputcn32_0934 Sputcn32_3164
            SSE: Ssed_3436 Ssed_3978
            SPL: Spea_0597 Spea_3107
            SHE: Shewmr4_0687 Shewmr4_0930
            SHM: Shewmr7_0968 Shewmr7_3335
            SHN: Shewana3_0932 Shewana3_3447
            SHW: Sputw3181_0779 Sputw3181_3242
            ILO: IL0493(rsmC)
            CPS: CPS_0711 CPS_4494(rsmC)
            PHA: PSHAa0552(rsmC) PSHAa2245(rsmD)
            PAT: Patl_0079 Patl_0447
            PIN: Ping_2296 Ping_3032
            MAQ: Maqu_1942
            HCH: HCH_02224(rsmC)
            CSA: Csal_2559
            ABO: ABO_1448(rsmC)
            MMW: Mmwyl1_0100
            AHA: AHA_3802
            ABU: Abu_0853
            RET: RHE_CH00110(ypch00037)
            RLE: RL0119
            RSP: RSP_0685(rsmC)
            RDE: RD1_1280(rsmC)
            MAG: amb2478
            MGM: Mmc1_2217 Mmc1_3702
            BTL: BALH_0099
            LLC: LACR_1532
            LLM: llmg_1059(rsmC)
            SPZ: M5005_Spy_0944
            SPH: MGAS10270_Spy1058
            SPI: MGAS10750_Spy1093
            SPJ: MGAS2096_Spy1003
            SPK: MGAS9429_Spy1047
            SPA: M6_Spy0933
            SPB: M28_Spy0916
            SAK: SAK_1047
            SSA: SSA_1034
            SGO: SGO_1078
            LSA: LSA0333
            RHA: RHA1_ro05839
            SCO: SCO1041(SCG20A.21)
            SMA: SAV1444(rsmC)
            PAC: PPA2050
            FNU: FN0907
            RBA: RB9141(rsmC)
            DGE: Dgeo_1622
            TTH: TTC0165
            TTJ: TTHA0533
STRUCTURES  PDB: 2PJD  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.52
            ExPASy - ENZYME nomenclature database: 2.1.1.52
            ExplorEnz - The Enzyme Database: 2.1.1.52
            ERGO genome analysis and discovery system: 2.1.1.52
            BRENDA, the Enzyme Database: 2.1.1.52
            CAS: 50812-26-5
///
ENTRY       EC 2.1.1.53                 Enzyme
NAME        putrescine N-methyltransferase;
            putrescine methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:putrescine N-methyltransferase
REACTION    S-adenosyl-L-methionine + putrescine = S-adenosyl-L-homocysteine +
            N-methylputrescine [RN:R01153]
ALL_REAC    R01153
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            putrescine [CPD:C00134]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            N-methylputrescine [CPD:C02723]
REFERENCE   1
  AUTHORS   Mizusaki, S., Tanabe, Y., Noguchi, M. and Tamaki, E.
  TITLE     Phytochemical studies on tobacco alkaloids. XIV. The occurence and
            properties of putrescine N-methyltransferase in tobacco roots.
  JOURNAL   Plant Cell Physiol. 12 (1971) 633-640.
  ORGANISM  Nicotiana tabacum
PATHWAY     PATH: map00960  Alkaloid biosynthesis II
ORTHOLOGY   KO: K05353  putrescine N-methyltransferase
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.53
            ExPASy - ENZYME nomenclature database: 2.1.1.53
            ExplorEnz - The Enzyme Database: 2.1.1.53
            ERGO genome analysis and discovery system: 2.1.1.53
            BRENDA, the Enzyme Database: 2.1.1.53
            CAS: 9075-39-2
///
ENTRY       EC 2.1.1.54                 Enzyme
NAME        deoxycytidylate C-methyltransferase;
            deoxycytidylate methyltransferase;
            dCMP methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     5,10-methylenetetrahydrofolate:dCMP C-methyltransferase
REACTION    5,10-methylenetetrahydrofolate + dCMP = dihydrofolate +
            deoxy-5-methylcytidylate [RN:R01670]
ALL_REAC    R01670
SUBSTRATE   5,10-methylenetetrahydrofolate [CPD:C00143];
            dCMP [CPD:C00239]
PRODUCT     dihydrofolate [CPD:C00415];
            deoxy-5-methylcytidylate [CPD:C03495]
COMMENT     dCMP is methylated by formaldehyde in the presence of
            tetrahydrofolate. CMP, dCTP and CTP can act as acceptors, but more
            slowly.
REFERENCE   1  [PMID:980110]
  AUTHORS   Kuo TT, Tu J.
  TITLE     Enzymatic synthesis of deoxy-5-methyl-cytidylic acid replacing
            deoxycytidylic acid in Xanthomonas oryzae phage Xp12DNA.
  JOURNAL   Nature. 263 (1976) 615.
  ORGANISM  Xanthomonas oryzae
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.54
            ExPASy - ENZYME nomenclature database: 2.1.1.54
            ExplorEnz - The Enzyme Database: 2.1.1.54
            ERGO genome analysis and discovery system: 2.1.1.54
            BRENDA, the Enzyme Database: 2.1.1.54
            CAS: 61970-01-2
///
ENTRY       EC 2.1.1.55                 Enzyme
NAME        tRNA (adenine-N6-)-methyltransferase;
            S-adenosyl-L-methionine:tRNA (adenine-6-N-)-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:tRNA (adenine-N6-)-methyltransferase
REACTION    S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA
            containing N6-methyladenine [RN:R00599]
ALL_REAC    R00599
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            tRNA [CPD:C00066]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            tRNA containing N6-methyladenine [CPD:C04159]
REFERENCE   1  [PMID:4996578]
  AUTHORS   Mandel LR, Hacker B, Maag TA.
  TITLE     Altered transfer RNA methylase patterns in Marek's disease tumors.
  JOURNAL   Cancer. Res. 31 (1971) 613-6.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:4292682]
  AUTHORS   Mittelman A, Hall RH, Yohn DS, Grace JT Jr.
  TITLE     The in vitro soluble RNA methylase activity of SV40-induced hamster
            tumors.
  JOURNAL   Cancer. Res. 27 (1967) 1409-14.
  ORGANISM  hamster
REFERENCE   3  [PMID:4349332]
  AUTHORS   Sharma OK.
  TITLE     Differences in the transfer RNA methyltransferases from normal rat
            liver and Novikoff hepatoma.
  JOURNAL   Biochim. Biophys. Acta. 299 (1973) 415-27.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.55
            ExPASy - ENZYME nomenclature database: 2.1.1.55
            ExplorEnz - The Enzyme Database: 2.1.1.55
            ERGO genome analysis and discovery system: 2.1.1.55
            BRENDA, the Enzyme Database: 2.1.1.55
            CAS: 9014-53-3
///
ENTRY       EC 2.1.1.56                 Enzyme
NAME        mRNA (guanine-N7-)-methyltransferase;
            messenger ribonucleate guanine 7-methyltransferase;
            guanine-7-methyltransferase;
            messenger RNA guanine 7-methyltransferase;
            S-adenosyl-L-methionine:mRNA (guanine-7-N-)-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:mRNA (guanine-N7-)-methyltransferase
REACTION    S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine
            + m7G(5')pppR-RNA (mRNA containing an N7-methylguanine cap)
            [RN:R03805]
ALL_REAC    R03805
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            G(5')pppR-RNA [CPD:C02031]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            m7G(5')pppR-RNA [CPD:C02339]
COMMENT     R (in the reaction field) may be guanosine or adenosine.
REFERENCE   1  [PMID:1058472]
  AUTHORS   Ensinger MJ, Martin SA, Paoletti E, Moss B.
  TITLE     Modification of the 5'-terminus of mRNA by soluble guanylyl and
            methyl transferases from vaccinia virus.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 72 (1975) 2525-9.
  ORGANISM  vaccinia virus
REFERENCE   2  [PMID:629955]
  AUTHORS   Groner Y, Gilboa E, Aviv H.
  TITLE     Methylation and capping of RNA polymerase II primary transcripts by
            HeLa nuclear homogenates.
  JOURNAL   Biochemistry. 17 (1978) 977-82.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:1194287]
  AUTHORS   Martin SA, Moss B.
  TITLE     Modification of RNA by mRNA guanylyltransferase and mRNA
            (guanine-7-)methyltransferase from vaccinia virions.
  JOURNAL   J. Biol. Chem. 250 (1975) 9330-5.
  ORGANISM  vaccinia virus
REFERENCE   4  [PMID:1194286]
  AUTHORS   Martin SA, Paoletti E, Moss B.
  TITLE     Purification of mRNA guanylyltransferase and mRNA (guanine-7-)
            methyltransferase from vaccinia virions.
  JOURNAL   J. Biol. Chem. 250 (1975) 9322-9.
  ORGANISM  vaccinia virus
ORTHOLOGY   KO: K00565  mRNA (guanine-N7-)-methyltransferase
GENES       HSA: 8731(RNMT)
            MMU: 67897(Rnmt)
            RNO: 291534(Rnmt)
            CFA: 476200(RNMT)
            GGA: 421046(RNMT)
            SPU: 580278(LOC580278)
            DME: Dmel_CG3688(l(2)35Bd)
            ATH: AT3G20650
            OSA: 4344818
            SCE: YBR236C(ABD1)
            AGO: AGOS_AFL026W
            KLA: KLLA0F10527g
            DHA: DEHA0F05940g
            PIC: PICST_66228(ABD1)
            CAL: CaO19_14008(CaO19.14008)
            CGR: CAGL0K07051g
            SPO: SPCC330.10
            MGR: MGG_06505
            AFM: AFUA_6G07690
            AOR: AO090003000177
            CNE: CNC01440
            TET: TTHERM_00431250
STRUCTURES  PDB: 1Z3C  2HV9  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.56
            ExPASy - ENZYME nomenclature database: 2.1.1.56
            ExplorEnz - The Enzyme Database: 2.1.1.56
            ERGO genome analysis and discovery system: 2.1.1.56
            BRENDA, the Enzyme Database: 2.1.1.56
            CAS: 56941-25-4
///
ENTRY       EC 2.1.1.57                 Enzyme
NAME        mRNA (nucleoside-2'-O-)-methyltransferase;
            messenger ribonucleate nucleoside 2'-methyltransferase;
            messenger RNA (nucleoside-2'-)-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:mRNA (nucleoside-2'-O-)-methyltransferase
REACTION    S-adenosyl-L-methionine + m7G(5')pppR-RNA =
            S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA (mRNA containing a
            2'-O-methylpurine cap) [RN:R03922]
ALL_REAC    R03922
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            m7G(5')pppR-RNA [CPD:C02339]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            m7G(5')pppRm-RNA (mRNA containing a 2'-O-methylpurine cap)
            [CPD:C04802]
COMMENT     In the reaction given, R may be guanosine or adenosine. The
            formation of a 2'-O-methyladenosine cap was formerly listed as EC
            2.1.1.58.
REFERENCE   1  [PMID:701281]
  AUTHORS   Barbosa E, Moss B.
  TITLE     mRNA(nucleoside-2'-)-methyltransferase from vaccinia virus.
            Purification and physical properties.
  JOURNAL   J. Biol. Chem. 253 (1978) 7692-7.
  ORGANISM  vaccinia virus
REFERENCE   2  [PMID:701282]
  AUTHORS   Barbosa E, Moss B.
  TITLE     mRNA(nucleoside-2'-)-methyltransferase from vaccinia virus.
            Characteristics and substrate specificity.
  JOURNAL   J. Biol. Chem. 253 (1978) 7698-702.
  ORGANISM  vaccinia virus
REFERENCE   3  [PMID:833934]
  AUTHORS   Boone RF, Ensinger MJ, Moss B.
  TITLE     Synthesis of mRNA guanylyltransferase and mRNA methyltransferases in
            cells infected with vaccinia virus.
  JOURNAL   J. Virol. 21 (1977) 475-83.
  ORGANISM  vaccinia virus
REFERENCE   4  [PMID:1058472]
  AUTHORS   Ensinger MJ, Martin SA, Paoletti E, Moss B.
  TITLE     Modification of the 5'-terminus of mRNA by soluble guanylyl and
            methyl transferases from vaccinia virus.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 72 (1975) 2525-9.
  ORGANISM  vaccinia virus
REFERENCE   5  [PMID:629955]
  AUTHORS   Groner Y, Gilboa E, Aviv H.
  TITLE     Methylation and capping of RNA polymerase II primary transcripts by
            HeLa nuclear homogenates.
  JOURNAL   Biochemistry. 17 (1978) 977-82.
  ORGANISM  human [GN:hsa]
GENES       CVI: CV_0121(ksgA)
STRUCTURES  PDB: 2GA9  2GAF  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.57
            ExPASy - ENZYME nomenclature database: 2.1.1.57
            ExplorEnz - The Enzyme Database: 2.1.1.57
            ERGO genome analysis and discovery system: 2.1.1.57
            BRENDA, the Enzyme Database: 2.1.1.57
            CAS: 61970-02-3
///
ENTRY       EC 2.1.1.58       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
COMMENT     Deleted entry: mRNA (adenosine-2'-O-)-methyltransferase. Now
            included with EC 2.1.1.57 mRNA (nucleoside-2'-O-)-methyltransferase.
            (EC 2.1.1.58 created 1981, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.58
            ExPASy - ENZYME nomenclature database: 2.1.1.58
            ExplorEnz - The Enzyme Database: 2.1.1.58
            ERGO genome analysis and discovery system: 2.1.1.58
            BRENDA, the Enzyme Database: 2.1.1.58
///
ENTRY       EC 2.1.1.59                 Enzyme
NAME        [cytochrome c]-lysine N-methyltransferase;
            cytochrome c (lysine) methyltransferase;
            cytochrome c methyltransferase;
            cytochrome c-specific protein methylase III;
            cytochrome c-specific protein-lysine methyltransferase;
            S-adenosyl-L-methionine:[cytochrome c]-L-lysine
            6-N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:[cytochrome c]-L-lysine N6-methyltransferase
REACTION    S-adenosyl-L-methionine + [cytochrome c]-L-lysine =
            S-adenosyl-L-homocysteine + [cytochrome c]-N6-methyl-L-lysine
            [RN:R04145]
ALL_REAC    R04145;
            (other) R03875 R04866 R04867
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            [cytochrome c]-L-lysine
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            [cytochrome c]-N6-methyl-L-lysine
COMMENT     One of a group of enzymes methylating proteins; see also EC 2.1.1.43
            histone-lysine N-methyltransferase and EC 2.1.1.60 calmodulin-lysine
            N-methyltransferase.
REFERENCE   1  [PMID:203592]
  AUTHORS   Durban E, Nochumson S, Kim S, Paik WK, Chan SK.
  TITLE     Cytochrome c-specific protein-lysine methyltransferase from
            Neurospora crassa. Purification, characterization, and substrate
            requirements.
  JOURNAL   J. Biol. Chem. 253 (1978) 1427-35.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2  [PMID:196592]
  AUTHORS   Nochumson S, Durban E, Kim S, Paik WK.
  TITLE     Cytochrome c-specific protein methylase III from Neurospora crassa.
  JOURNAL   Biochem. J. 165 (1977) 11-8.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   3  [PMID:6282265]
  AUTHORS   Valentine J, Pettigrew GW.
  TITLE     A cytochrome c methyltransferase from Crithidia oncopelti.
  JOURNAL   Biochem. J. 201 (1982) 329-38.
  ORGANISM  Crithidia oncopelti
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.59
            ExPASy - ENZYME nomenclature database: 2.1.1.59
            ExplorEnz - The Enzyme Database: 2.1.1.59
            ERGO genome analysis and discovery system: 2.1.1.59
            BRENDA, the Enzyme Database: 2.1.1.59
            CAS: 82047-78-7
///
ENTRY       EC 2.1.1.60                 Enzyme
NAME        calmodulin-lysine N-methyltransferase;
            S-adenosylmethionine:calmodulin (lysine) N-methyltransferase;
            S-adenosyl-L-methionine:calmodulin-L-lysine 6-N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:calmodulin-L-lysine N6-methyltransferase
REACTION    S-adenosyl-L-methionine + calmodulin L-lysine =
            S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
            [RN:R04062]
ALL_REAC    R04062;
            (other) R03875 R04866 R04867
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            calmodulin L-lysine [CPD:C02816]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            calmodulin N6-methyl-L-lysine [CPD:C03941]
COMMENT     One of a group of enzymes methylating proteins; see also EC 2.1.1.43
            histone-lysine N-methyltransferase and EC 2.1.1.59
            [cytochrome-c]-lysine N-methyltransferase.
REFERENCE   1  [PMID:6773954]
  AUTHORS   Sitaramayya A, Wright LS, Siegel FL.
  TITLE     Enzymatic methylation of calmodulin in rat brain cytosol.
  JOURNAL   J. Biol. Chem. 255 (1980) 8894-900.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.60
            ExPASy - ENZYME nomenclature database: 2.1.1.60
            ExplorEnz - The Enzyme Database: 2.1.1.60
            ERGO genome analysis and discovery system: 2.1.1.60
            BRENDA, the Enzyme Database: 2.1.1.60
            CAS: 75603-20-2
///
ENTRY       EC 2.1.1.61                 Enzyme
NAME        tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase;
            transfer ribonucleate 5-methylaminomethyl-2-thiouridylate
            5-methyltransferase;
            tRNA 5-methylaminomethyl-2-thiouridylate 5'-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:tRNA
            (5-methylaminomethyl-2-thio-uridylate)-methyltransferase
REACTION    S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA
            containing 5-methylaminomethyl-2-thiouridylate [RN:R00601]
ALL_REAC    R00601
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            tRNA [CPD:C00066]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            tRNA containing 5-methylaminomethyl-2-thiouridylate [CPD:C04728]
COMMENT     This enzyme is specific for the terminal methyl group of
            5-methylaminomethyl-2-thiouridylate.
REFERENCE   1  [PMID:4703553]
  AUTHORS   Taya Y, Nishimura S.
  TITLE     Biosynthesis of 5-methylaminomethyl-2-thiouridylate. I. Isolation of
            a new tRNA-methylase specific for
            5-methylaminomethyl-2-thiouridylate.
  JOURNAL   Biochem. Biophys. Res. Commun. 51 (1973) 1062-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Taya, Y. and Nishimura, S.
  TITLE     In: Salvatore, F., Borek, E., Zappia, V., Williams-Ashman, H.G. and
            Schlenk, F. (Eds.), The Biochemistry of Adenosylmethionine, Columbia
            University Press, New York, 1977, p. 251.
ORTHOLOGY   KO: K00566  tRNA
                        (5-methylaminomethyl-2-thiouridylate)-methyltransferase
GENES       HSA: 55687(TRMU)
            MMU: 72026(Trmu)
            CFA: 481204(TRMU)
            GGA: 425909(RCJMB04_8p20)
            DME: Dmel_CG3021
            CEL: B0035.16
            ATH: AT1G51310
            OSA: 4331793
            CME: CMT278C CMT380C
            SCE: YDL033C(SLM3)
            AGO: AGOS_AEL087C
            PIC: PICST_34443
            CGR: CAGL0K01529g
            SPO: SPAC23H4.04
            CNE: CNM00110
            DDI: DDBDRAFT_0188196
            TAN: TA12620
            TPV: TP02_0339
            TBR: Tb927.8.1830
            LMA: LmjF07.0130
            ECO: b1133(mnmA)
            ECJ: JW1119(trmU)
            ECE: Z1862(ycfB)
            ECS: ECs1605
            ECC: c1512(ycfB)
            ECI: UTI89_C0446(yajK) UTI89_C1262
            ECP: ECP_1128
            ECV: APECO1_215(ycfB)
            ECW: EcE24377A_1296(trmU) EcE24377A_2619(mnmC)
            ECX: EcHS_A1253(trmU) EcHS_A2475
            STY: STY1274(trmU)
            STT: t1686(trmU)
            SPT: SPA1616(trmU)
            SEC: SC1185(trmU)
            STM: STM1234.S(trmU)
            YPE: YPO1638(trmU)
            YPK: y1799
            YPM: YP_1768(trmU)
            YPA: YPA_1886
            YPN: YPN_1993
            YPP: YPDSF_1810
            YPS: YPTB2430(trmU)
            YPI: YpsIP31758_1612(trmU)
            SFL: SF1152(trmU)
            SFX: S1235(ycfB)
            SFV: SFV_1168(ycfB)
            SSN: SSON_1151(ycfB)
            SBO: SBO_1906(ycfB)
            SDY: SDY_2019(ycfB)
            ECA: ECA2442(trmU)
            PLU: plu2804(trmU)
            BUC: BU261(trmU)
            BAS: BUsg252(trmU)
            BAB: bbp242(trmU)
            BCC: BCc_166(trmU)
            WBR: WGLp104(ycfB)
            SGL: SG1085
            ENT: Ent638_1646
            SPE: Spro_2022
            BFL: Bfl392(trmU)
            BPN: BPEN_404(trmU)
            HIN: HI0174
            HIT: NTHI0262(trmU)
            HIP: CGSHiEE_02405(trmU)
            HDU: HD0389(trmU)
            HSO: HS_1683(trmU)
            PMU: PM1336
            MSU: MS0301(trmU)
            APL: APL_0158(trmU)
            ASU: Asuc_0607
            XFA: XF1440
            XFT: PD0662(trmU)
            XCC: XCC1964(trmU)
            XCB: XC_2221
            XCV: XCV2046(trmU)
            XAC: XAC1998(trmU)
            XOO: XOO2556(trmU)
            XOM: XOO_2415(XOO2415)
            VCH: VC1128
            VCO: VC0395_A0646(trmU)
            VVU: VV1_2926
            VVY: VV1343
            VPA: VP1130
            VFI: VF1784
            PPR: PBPRA1147(ycfB)
            PAE: PA2626(trmU)
            PAU: PA14_30150(trmU)
            PAP: PSPA7_2581(trmU)
            PPU: PP_4014(trmU)
            PPF: Pput_1819
            PST: PSPTO_3358(trmU)
            PSB: Psyr_3190
            PSP: PSPPH_3102(trmU)
            PFL: PFL_3891(trmU)
            PFO: Pfl_3596
            PEN: PSEEN2200(trmU)
            PMY: Pmen_2399
            PAR: Psyc_1244(trmU)
            PCR: Pcryo_1148
            PRW: PsycPRwf_0961
            ACI: ACIAD1221(trmU)
            SON: SO_2633(trmU)
            SDN: Sden_1828
            SFR: Sfri_2260
            SAZ: Sama_2062
            SBL: Sbal_2478
            SBM: Shew185_2471
            SLO: Shew_1560
            SPC: Sputcn32_2233
            SSE: Ssed_1881
            SPL: Spea_2538
            SHE: Shewmr4_1603
            SHM: Shewmr7_1678
            SHN: Shewana3_1747 Shewana3_2428
            SHW: Sputw3181_1776
            ILO: IL1310(trmU)
            CPS: CPS_2900(trmU)
            PHA: PSHAa1690(mnmA)
            PAT: Patl_2379
            SDE: Sde_1677
            PIN: Ping_0963
            MAQ: Maqu_1762
            CBU: CBU_1147(trmU)
            CBD: COXBU7E912_1245(trmU)
            LPN: lpg1389
            LPF: lpl1340(trmU)
            LPP: lpp1344(trmU)
            MCA: MCA1785(trmU)
            FTU: FTT1677c(trmU)
            FTF: FTF1677c(trmU)
            FTW: FTW_1940(trmU)
            FTL: FTL_0072
            FTH: FTH_0068(trmU)
            FTA: FTA_0080(trmU)
            FTN: FTN_0108(trmU)
            TCX: Tcr_1099
            NOC: Noc_2040
            AEH: Mlg_1451
            HHA: Hhal_1404
            HCH: HCH_02333(trmU)
            CSA: Csal_2444
            ABO: ABO_1275(trmU) ABO_2264(trmU) ABO_2271(trmH)
            MMW: Mmwyl1_3265
            AHA: AHA_1415(trmU)
            DNO: DNO_0627(trmU)
            BCI: BCI_0422(trmU)
            CRP: CRP_036
            RMA: Rmag_0747
            VOK: COSY_0691(trmU)
            NME: NMB1556
            NMA: NMA1744(trmU)
            NMC: NMC1473(trmU)
            NGO: NGO1214
            CVI: CV_3402(trmU)
            RSO: RSc2723(trmU)
            REU: Reut_A2821
            REH: H16_A3126(trmU)
            RME: Rmet_2958
            BMA: BMA2364(trmU)
            BMV: BMASAVP1_A0278(trmU)
            BML: BMA10299_A1140(trmU)
            BMN: BMA10247_2544(trmU)
            BXE: Bxe_A4010
            BVI: Bcep1808_0663
            BUR: Bcep18194_A3784
            BCN: Bcen_0214
            BCH: Bcen2424_0698
            BAM: Bamb_0591
            BPS: BPSL2889(trmU)
            BPM: BURPS1710b_3396(trmU)
            BPL: BURPS1106A_3389(trmU)
            BPD: BURPS668_3354(trmU)
            BTE: BTH_I1257(trmU)
            PNU: Pnuc_1796
            BPE: BP2893(trmU)
            BPA: BPP2503(trmU)
            BBR: BB1950(trmU)
            RFR: Rfer_3756
            POL: Bpro_4559
            PNA: Pnap_3817
            AAV: Aave_4724
            AJS: Ajs_4068
            VEI: Veis_0297
            MPT: Mpe_A3566
            HAR: HEAR0326(mnmA)
            MMS: mma_0373(trmU)
            NEU: NE0963(trmU)
            NET: Neut_2336
            NMU: Nmul_A2243
            EBA: ebA986(trmU)
            AZO: azo2772
            DAR: Daro_3291
            TBD: Tbd_0851
            MFA: Mfla_2115
            HPY: HP1335
            HPJ: jhp1254(trmU)
            HPA: HPAG1_0013 HPAG1_1282
            HHE: HH0956(trmU)
            HAC: Hac_0264(trmU) Hac_1695(trmU)
            WSU: WS1636
            TDN: Tmden_0710
            CJE: Cj0053c(trmU)
            CJR: CJE0048(trmU)
            CJJ: CJJ81176_0090(trmU)
            CJU: C8J_0050(trmU)
            CJD: JJD26997_0062(trmU)
            CFF: CFF8240_1482(trmU)
            CCV: CCV52592_0211(trmU) CCV52592_1442(trmU)
            CHA: CHAB381_1206(trmU)
            CCO: CCC13826_1016(trmU)
            ABU: Abu_0484(trmU1) Abu_0485(trmU2)
            NIS: NIS_0434(trmU)
            SUN: SUN_1043(trmU)
            GSU: GSU2569(trmU)
            GME: Gmet_0873
            GUR: Gura_1492
            PCA: Pcar_1858
            PPD: Ppro_1837
            DVU: DVU0807(trmU)
            DVL: Dvul_2170
            DDE: Dde_1019
            LIP: LI0203(trmU)
            BBA: Bd1939(trmU)
            DPS: DP2955
            ADE: Adeh_1482
            AFW: Anae109_2351
            MXA: MXAN_3499(trmU)
            SAT: SYN_00798 SYN_01256 SYN_01419
            SFU: Sfum_0167
            RPR: RP306
            RTY: RT0296(trmU)
            RCO: RC0410(trmU)
            RFE: RF_0496(trmU)
            RBE: RBE_0531(trmU)
            RAK: A1C_02285(trmU)
            RBO: A1I_03045(trmU)
            RRI: A1G_02335(trmU)
            OTS: OTBS_2088(trmU)
            WOL: WD1259(trmU)
            WBM: Wbm0155
            AMA: AM335(trmU)
            APH: APH_0910(trmU)
            ERU: Erum2230(trmU)
            ERW: ERWE_CDS_02250(trmU)
            ERG: ERGA_CDS_02210(trmU)
            ECN: Ecaj_0226
            ECH: ECH_0872(trmU)
            NSE: NSE_0468(trmU)
            PUB: SAR11_0828(trmU)
            MLO: mlr2824
            MES: Meso_2217
            PLA: Plav_2188
            SME: SMc00659(trmU)
            SMD: Smed_2600
            ATU: Atu3703(trmU)
            ATC: AGR_L_2270
            RET: RHE_CH03452(trmU)
            RLE: RL3957
            BME: BMEI0428
            BMF: BAB1_1607(trmU)
            BMS: BR1591(trmU)
            BMB: BruAb1_1578(trmU)
            BOV: BOV_1534(trmU)
            OAN: Oant_1576
            BJA: bll6995(trmU)
            BRA: BRADO5894(trmU)
            BBT: BBta_1881(trmU)
            RPA: RPA1306(trmU)
            RPB: RPB_4116
            RPC: RPC_0987
            RPD: RPD_3962
            RPE: RPE_1039
            NWI: Nwi_0603
            NHA: Nham_0695
            BHE: BH12020(trmU)
            BQU: BQ09430(trmU)
            BBK: BARBAKC583_1016(trmU)
            XAU: Xaut_0404
            CCR: CC_0897
            SIL: SPO1677(trmU)
            SIT: TM1040_1401
            RSP: RSP_2619(trmU)
            RSH: Rsph17029_1277
            RSQ: Rsph17025_1905
            JAN: Jann_2507
            RDE: RD1_2599(trmU)
            PDE: Pden_4098
            MMR: Mmar10_0693
            HNE: HNE_0641(trmU)
            ZMO: ZMO0769(trmU)
            NAR: Saro_0043
            SAL: Sala_2030
            SWI: Swit_4751
            ELI: ELI_13465
            GOX: GOX1371
            ACR: Acry_1764
            RRU: Rru_A2024
            MAG: amb3019
            MGM: Mmc1_0953
            ABA: Acid345_2270
            SUS: Acid_0599
            BSU: BG13787(trmU)
            BHA: BH1261
            BAN: BA4625(trmU)
            BAR: GBAA4625(trmU)
            BAA: BA_5065
            BAT: BAS4291
            BCE: BC4391
            BCA: BCE_4479(trmU)
            BCZ: BCZK4139(trmU)
            BCY: Bcer98_3108
            BTK: BT9727_4128(trmU)
            BTL: BALH_3978(trmU)
            BLI: BL02039(trmU)
            BLD: BLi02875(trmU)
            BCL: ABC1586(trmU)
            BPU: BPUM_2391(trmU)
            OIH: OB2014(trmU)
            GKA: GK1009 GK2563
            SAU: SA1449
            SAV: SAV1621
            SAM: MW1571
            SAR: SAR1701
            SAS: SAS1557
            SAC: SACOL1676(trmU)
            SAB: SAB1492c(trmU)
            SAA: SAUSA300_1578(trmU)
            SAO: SAOUHSC_01725 SAOUHSC_01726
            SAJ: SaurJH9_1679
            SAH: SaurJH1_1712
            SEP: SE1304
            SER: SERP1185(trmU)
            SHA: SH1298
            SSP: SSP1140
            LMO: lmo1512
            LMF: LMOf2365_1531(trmU)
            LIN: lin1547
            LWE: lwe1525(trmU)
            LLA: L52034(trmU)
            LLC: LACR_0895
            LLM: llmg_1725(trmU)
            SPY: SPy_2188
            SPZ: M5005_Spy_1840(trmU)
            SPM: spyM18_2222(trmU)
            SPG: SpyM3_1840(trmU)
            SPS: SPs1836
            SPH: MGAS10270_Spy1959(trmU)
            SPI: MGAS10750_Spy1956(trmU)
            SPJ: MGAS2096_Spy1871(trmU)
            SPK: MGAS9429_Spy1851(trmU)
            SPF: SpyM51812
            SPA: M6_Spy1857
            SPB: M28_Spy1872(trmU)
            SPN: SP_0118
            SPR: spr0122(trmU)
            SPD: SPD_0127(trmU)
            SAG: SAG2144(trmU)
            SAN: gbs2103
            SAK: SAK_2102(trmU)
            SMU: SMU.2143c
            STC: str2003(trmU)
            STL: stu2003(trmU)
            SSA: SSA_2360(trmU)
            SGO: SGO_0022(trmU)
            LPL: lp_2178(trmU)
            LJO: LJ0986
            LAC: LBA0822
            LSA: LSA0794(trmU)
            LSL: LSL_0862(trmU)
            LDB: Ldb0755(trmU)
            LBU: LBUL_0688
            LBR: LVIS_1434
            LCA: LSEI_1292
            LRE: Lreu_0605
            EFA: EF2070(trmU)
            STH: STH2389
            CAC: CAC2233
            CPE: CPE1783
            CPF: CPF_2037(trmU)
            CPR: CPR_1753(trmU)
            CTC: CTC01052 CTC01457(trmU)
            CNO: NT01CX_2281(trmU)
            CTH: Cthe_0722
            CDF: CD1281(trmU)
            CBO: CBO1185(asuE1) CBO2905(asuE2)
            CBA: CLB_1216(trmU-1) CLB_2868(trmU-2)
            CBH: CLC_1228(trmU-1) CLC_2801(trmU-2)
            CBF: CLI_1267(trmU-1) CLI_2962(trmU-2)
            CBE: Cbei_1100
            CKL: CKL_1088(trmU)
            AMT: Amet_3658
            CHY: CHY_2197(trmU)
            DSY: DSY2424
            DRM: Dred_0766
            SWO: Swol_0464
            CSC: Csac_2252
            TTE: TTE1243(trmU) TTE2464(trmU2)
            MTA: Moth_1650
            MGE: MG_295
            MPN: MPN422(A05_orf370)
            MPU: MYPU_5580(trmU)
            MPE: MYPE8250(trmD)
            MMY: MSC_0447(trmU)
            MMO: MMOB4400(trmU)
            MHY: mhp433(trmU)
            MHJ: MHJ_0428(trmU)
            MHP: MHP7448_0430(trmU)
            MSY: MS53_0375(trmU)
            MCP: MCAP_0523(trmU)
            UUR: UU402(trmU)
            POY: PAM125(trmU)
            AYW: AYWB_597(trmU)
            MFL: Mfl412
            MTU: Rv3024c(trmU)
            MTC: MT3108(trmU)
            MBO: Mb3050c(trmU)
            MBB: BCG_3047c(trmU)
            MLE: ML1707
            MPA: MAP3057c
            MAV: MAV_3871(trmU)
            MSM: MSMEG_2358(trmU)
            MVA: Mvan_2106
            MGI: Mflv_4254
            MMC: Mmcs_1876
            MKM: Mkms_1922
            MJL: Mjls_1856
            CGL: NCgl1192(cgl1240)
            CGB: cg1397
            CEF: CE1334
            CDI: DIP1074(trmU)
            CJK: jk1320(trmU)
            NFA: nfa42670
            RHA: RHA1_ro06467
            SCO: SCO5488(SC2A11.22)
            SMA: SAV2753(trmU)
            TWH: TWT415(trmU)
            TWS: TW353(trmU)
            LXX: Lxx14390(trmU)
            CMI: CMM_1403(trmU)
            ART: Arth_2727
            AAU: AAur_2710(trmU)
            PAC: PPA1117
            NCA: Noca_3445
            TFU: Tfu_0597
            FRA: Francci3_3649
            FAL: FRAAL5861(mnmA)
            ACE: Acel_0689
            KRA: Krad_1308
            SEN: SACE_6187(trmU)
            STP: Strop_1214
            RXY: Rxyl_1354
            FNU: FN0563 FN0765 FN1920
            RBA: RB6554(trmU)
            CTR: CT287(ycbF)
            CTA: CTA_0309(trmU)
            CMU: TC0560
            CPN: CPn0438(ycbF)
            CPA: CP0315
            CPJ: CPj0438(ycbF)
            CPT: CpB0453
            CCA: CCA00354(trmU)
            CAB: CAB345(trmU)
            CFE: CF0653(rrm8)
            PCU: pc1800(ycfB)
            BBU: BB0682
            BGA: BG0705
            TDE: TDE0690(trmU)
            LIL: LA1487(trmU)
            LIC: LIC12269(trmU)
            LBJ: LBJ_0986(trmU)
            LBL: LBL_2047(trmU)
            SYN: sll0844
            SYW: SYNW1622
            SYC: syc2494_d(trmU)
            SYF: Synpcc7942_1509
            SYD: Syncc9605_0877
            SYE: Syncc9902_1521
            SYG: sync_0759(trmU)
            SYR: SynRCC307_1702(trmU)
            SYX: SynWH7803_1738(trmU)
            CYA: CYA_0046(trmU)
            CYB: CYB_1191(trmU)
            TEL: tlr2256
            GVI: gll0551
            ANA: all1359
            AVA: Ava_4065
            PMA: Pro1365(trmU)
            PMM: PMM1291
            PMT: PMT0344
            PMN: PMN2A_0858
            PMI: PMT9312_1387
            PMB: A9601_14901(trmU) A9601_17781
            PMC: P9515_14521(trmU) P9515_17581
            PMF: P9303_19621(trmU) P9303_22871
            PMG: P9301_14761(trmU) P9301_17621
            PMH: P9215_15191(trmU)
            PME: NATL1_17111(trmU)
            TER: Tery_0725
            BTH: BT_0155 BT_3354 BT_3888
            BFR: BF0215 BF1407 BF4001
            BFS: BF0174 BF1343(trmU) BF3776
            PGI: PG0268(trmU)
            SRU: SRU_2494(trmU)
            CHU: CHU_1602(trmU)
            GFO: GFO_2222(trmU)
            FJO: Fjoh_2388
            FPS: FP1775(trmU)
            CTE: CT1855(trmU)
            CCH: Cag_0254
            CPH: Cpha266_2100
            PVI: Cvib_0384
            PLT: Plut_0318
            DET: DET0779(trmU)
            DEH: cbdb_A754(trmU)
            DEB: DehaBAV1_0705
            RRS: RoseRS_2136
            RCA: Rcas_1735
            DRA: DR_1759
            DGE: Dgeo_0792
            TTH: TTC1727
            TTJ: TTHA0258
            AAE: aq_1224
            TMA: TM0520
            TPT: Tpet_0401
            TME: Tmel_1559
            FNO: Fnod_1772
            HMA: rrnAC2860(trmU)
            HWA: HQ3682A(trmU)
STRUCTURES  PDB: 2DER  2DET  2DEU  2HMA  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.61
            ExPASy - ENZYME nomenclature database: 2.1.1.61
            ExplorEnz - The Enzyme Database: 2.1.1.61
            ERGO genome analysis and discovery system: 2.1.1.61
            BRENDA, the Enzyme Database: 2.1.1.61
            CAS: 39391-17-8
///
ENTRY       EC 2.1.1.62                 Enzyme
NAME        mRNA (2'-O-methyladenosine-N6-)-methyltransferase;
            messenger ribonucleate 2'-O-methyladenosine NG-methyltransferase;
            S-adenosyl-L-methionine:mRNA
            (2'-O-methyladenosine-6-N-)-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:mRNA
            (2'-O-methyladenosine-N6-)-methyltransferase
REACTION    S-adenosyl-L-methionine + m7G(5')pppAm = S-adenosyl-L-homocysteine +
            m7G(5')pppm6Am (mRNA containing an N6,2'-O-dimethyladenosine cap)
            [RN:R03788]
ALL_REAC    R03788
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            m7G(5')pppAm [CPD:C01972]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            m7G(5')pppm6Am (mRNA containing an N6,2'-O-dimethyladenosine cap)
            [CPD:C04833]
REFERENCE   1  [PMID:670176]
  AUTHORS   Keith JM, Ensinger MJ, Mose B.
  TITLE     HeLa cell RNA (2'-O-methyladenosine-N6-)-methyltransferase specific
            for the capped 5'-end of messenger RNA.
  JOURNAL   J. Biol. Chem. 253 (1978) 5033-9.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K05925  mRNA (2'-O-methyladenosine-N6-)-methyltransferase
GENES       HSA: 56339(METTL3)
            PTR: 452765(METTL3)
            MMU: 56335(Mettl3)
            CFA: 475404(METTL3)
            XLA: 414662(MGC81069)
            DME: Dmel_CG5933
            OSA: 4330284
            PFA: PF07_0123
            TET: TTHERM_00388490 TTHERM_00704040 TTHERM_00962190
            CVI: CV_0121(ksgA)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.62
            ExPASy - ENZYME nomenclature database: 2.1.1.62
            ExplorEnz - The Enzyme Database: 2.1.1.62
            ERGO genome analysis and discovery system: 2.1.1.62
            BRENDA, the Enzyme Database: 2.1.1.62
            CAS: 68009-87-0
///
ENTRY       EC 2.1.1.63                 Enzyme
NAME        methylated-DNA---[protein]-cysteine S-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     DNA-6-O-methylguanine:[protein]-L-cysteine S-methyltransferase
REACTION    DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA
            (without 6-O-methylguanine) + protein S-methyl-L-cysteine
            [RN:R04314]
ALL_REAC    R04314
SUBSTRATE   DNA containing 6-O-methylguanine [CPD:C04250];
            protein L-cysteine [CPD:C02743]
PRODUCT     DNA [CPD:C00039];
            protein S-methyl-L-cysteine [CPD:C03800]
COMMENT     This protein is involved in the repair of alkylated DNA. It acts
            only on the alkylated DNA (cf. EC 3.2.2.20, DNA-3-methyladenine
            glycosidase I and EC 3.2.2.21, DNA-3-methyladenine glycosidase II).
            This enzyme catalyses only one turnover and therefore is not
            strictly catalytic.
REFERENCE   1  [PMID:7008792]
  AUTHORS   Foote RS, Mitra S, Pal BC.
  TITLE     Demethylation of O6-methylguanine in a synthetic DNA polymer by an
            inducible activity in Escherichia coli.
  JOURNAL   Biochem. Biophys. Res. Commun. 97 (1980) 654-9.
REFERENCE   2  [PMID:7000780]
  AUTHORS   Olsson M, Lindahl T.
  TITLE     Repair of alkylated DNA in Escherichia coli. Methyl group transfer
            from O6-methylguanine to a protein cysteine residue.
  JOURNAL   J. Biol. Chem. 255 (1980) 10569-71.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:1544541]
  AUTHORS   Pegg AE, Byers TL.
  TITLE     Repair of DNA containing O6-alkylguanine.
  JOURNAL   FASEB. J. 6 (1992) 2302-10.
ORTHOLOGY   KO: K00567  methylated-DNA-[protein]-cysteine S-methyltransferase
GENES       HSA: 4255(MGMT)
            MMU: 17314(Mgmt)
            RNO: 25332(Mgmt)
            CFA: 442978(MGMT)
            GGA: 423965(MGMT)
            XLA: 446289(LOC446289)
            XTR: 496878(mgmt)
            DME: Dmel_CG1303(agt)
            SCE: YDL200C(MGT1)
            PIC: PICST_44707(ADA1) PICST_49425
            CGR: CAGL0J09768g
            AFM: AFUA_2G02090 AFUA_5G06350
            DDI: DDB_0232973(MGMT)
            CHO: Chro.80616
            TVA: TVAG_401340
            ECO: b1335(ogt) b2213(ada)
            ECJ: JW1329(ogt) JW2201(ada)
            ECE: Z2432(ogt) Z3471(ada)
            ECS: ECs1916 ECs3102
            ECC: c1808(ogt) c2754(ada)
            ECI: UTI89_C0482(ybaZ) UTI89_C1606(ogt) UTI89_C2493(ada)
            ECP: ECP_1389 ECP_2256
            ECV: APECO1_4346(ada) APECO1_488(ogt)
            ECW: EcE24377A_0490 EcE24377A_2512(ada)
            ECX: EcHS_A0437 EcHS_A0531 EcHS_A1451 EcHS_A2352
            STY: STY1405(ogt) STY2491(ada)
            STT: t0599(ada) t1563(ogt)
            SPT: SPA0599(ada) SPA1225(ogt)
            SEC: SC1655(ogt) SC2269(ada)
            STM: STM1659(ogt) STM2265(ada)
            YPE: YPO0072 YPO2299(ogt)
            YPK: y0070(ada) y2131(ogt)
            YPM: YP_0072(ada) YP_2084(ada2)
            YPA: YPA_1648 YPA_3471
            YPN: YPN_1760 YPN_3779
            YPP: YPDSF_0844 YPDSF_3834
            YPS: YPTB0068 YPTB2221(ogt)
            YPI: YpsIP31758_0082(ada) YpsIP31758_1834(ogt) YpsIP31758_3074
            SFL: SF1835(ogt) SF2297
            SFX: S1435(ogt) S2427(ada)
            SFV: SFV_1824(ogt) SFV_2288(ada)
            SSN: SSON_1798(ogt) SSON_2271(ada)
            SBO: SBO_1726(ogt) SBO_2094(ada)
            SDY: SDY_0863(ada) SDY_1416(ogt)
            ECA: ECA0908(ada) ECA2208(ogt) ECA2454(ogt)
            PLU: plu1288(ogt)
            ENT: Ent638_0045 Ent638_1854 Ent638_2793
            SPE: Spro_0260 Spro_0667 Spro_1282 Spro_2581
            HIN: HI0402(ogt)
            HIT: NTHI0523(ogt)
            HDU: HD1077(ogt)
            HSO: HS_1549(dat1)
            PMU: PM1068(dat1)
            MSU: MS0637(ada)
            APL: APL_0934(ogt)
            ASU: Asuc_1080 Asuc_1904
            XFA: XF2598
            XFT: PD1975(ogt)
            XCC: XCC2652(ada) XCC2653(ogt)
            XCB: XC_1464 XC_1465(ada)
            XCV: XCV2983(ada) XCV2984(ogt)
            XAC: XAC2822(Ada) XAC2823(ogt)
            XOO: XOO1538(ogt) XOO1539(ada)
            XOM: XOO_1428(XOO1428) XOO_1429(XOO1429)
            VCH: VCA1017 VCA1018
            VCO: VC0395_0223(ogt)
            VVU: VV2_1208 VV2_1209
            VVY: VVA0035 VVA0037
            VPA: VPA0045 VPA0046
            VFI: VFA0177
            PPR: PBPRA2433 PBPRB0209 PBPRB0210(dat)
            PAE: PA0995(ogt) PA2118(ada) PA3596
            PAU: PA14_17760(ada) PA14_37190(ada) PA14_51440(ogt)
            PAP: PSPA7_3190 PSPA7_4403
            PPU: PP_0706(ada) PP_3017(ogt)
            PPF: Pput_1260 Pput_2662 Pput_4506
            PST: PSPTO_3595(ada)
            PSB: Psyr_3365
            PSP: PSPPH_3285(ada)
            PFL: PFL_0379(ada) PFL_3409(ada) PFL_5108(ogt)
            PFO: Pfl_2158 Pfl_2938 Pfl_3566
            PEN: PSEEN0845(ada) PSEEN2569 PSEEN3169(ogt)
            PMY: Pmen_0756 Pmen_1282 Pmen_1887
            PAR: Psyc_0935
            PCR: Pcryo_1480
            PRW: PsycPRwf_0827 PsycPRwf_1002 PsycPRwf_1964
            ACI: ACIAD0344(ada) ACIAD0692(ogt)
            ACB: A1S_0711
            SON: SO_3126(ogt) SO_3127
            SDN: Sden_1493 Sden_2530 Sden_2531
            SFR: Sfri_2711 Sfri_2712
            SAZ: Sama_2204
            SBL: Sbal_2799
            SBM: Shew185_1999 Shew185_2152 Shew185_2819 Shew185_3219
            SLO: Shew_1453
            SPC: Sputcn32_2496
            SSE: Ssed_2326 Ssed_2903 Ssed_3370
            SPL: Spea_1459 Spea_2243 Spea_3032
            SHE: Shewmr4_1367 Shewmr4_1368
            SHM: Shewmr7_1432 Shewmr7_1433
            SHN: Shewana3_1420 Shewana3_1421 Shewana3_2691
            SHW: Sputw3181_1512
            ILO: IL0070(ada)
            CPS: CPS_0155 CPS_3353
            PHA: PSHAb0291 PSHAb0293(ogt)
            PAT: Patl_3876
            SDE: Sde_3879
            PIN: Ping_1414
            CBU: CBU_0441(ogt)
            CBD: COXBU7E912_0849 COXBU7E912_1633
            LPN: lpg0394 lpg1150
            LPF: lpl0438 lpl1156
            LPP: lpp0462 lpp1152
            MCA: MCA0584(ogt)
            FTU: FTT1518(ogt)
            FTF: FTF1518(ogt)
            FTW: FTW_0773
            FTL: FTL_0275
            FTH: FTH_0274
            FTN: FTN_1528
            TCX: Tcr_2200
            NOC: Noc_2104 Noc_2256
            AEH: Mlg_2037
            HCH: HCH_04648 HCH_04649 HCH_05579
            CSA: Csal_2795 Csal_2796
            ABO: ABO_1412(ada)
            MMW: Mmwyl1_2197 Mmwyl1_3659 Mmwyl1_4096
            AHA: AHA_0647 AHA_1045
            NME: NMB1528
            NMA: NMA1728
            NMC: NMC1457
            NGO: NGO0988
            CVI: CV_0088 CV_0220 CV_0391(ADA) CV_1423(ogt) CV_3671
            RSO: RSc2505(RS05743) RSc2506(ogt) RSc2543(RS00722)
                 RSc2566(RS00760) RSc2570(ada)
            REU: Reut_A0578 Reut_B4734 Reut_B5314 Reut_B5315
            REH: H16_A0591 H16_B1093(ada) H16_B2550(ogt)
            RME: Rmet_0520 Rmet_3765 Rmet_3767 Rmet_5912 Rmet_5913
            BMA: BMA0115(ada) BMA0368(ogt)
            BMV: BMASAVP1_A0668(ogt) BMASAVP1_A2836(ada)
            BML: BMA10299_A2249(ada) BMA10299_A2503(ogt)
            BMN: BMA10247_0117(ogt) BMA10247_2300 BMA10247_2323(ada)
            BXE: Bxe_A0749 Bxe_A4482 Bxe_B0556
            BVI: Bcep1808_3300 Bcep1808_3985
            BUR: Bcep18194_A4920 Bcep18194_A4925 Bcep18194_A4929
                 Bcep18194_A4931 Bcep18194_A5892 Bcep18194_A6508
                 Bcep18194_B2719 Bcep18194_B2720
            BCN: Bcen_1949
            BCH: Bcen2424_2560 Bcen2424_3152 Bcen2424_3449 Bcen2424_3450
            BAM: Bamb_2608 Bamb_3205 Bamb_5231
            BPS: BPSL0100 BPSL0862
            BPM: BURPS1710b_0322
            BPL: BURPS1106A_0132(ada) BURPS1106A_0913(ogt)
            BPD: BURPS668_0116 BURPS668_0910(ogt)
            BTE: BTH_I0085 BTH_I0725
            BPE: BP0339(ogt) BP0391(ogt)
            BPA: BPP1020(ada) BPP4040(ogt) BPP4193(ogt)
            BBR: BB1234(ada) BB4513(ogt) BB4663(ogt)
            RFR: Rfer_1704 Rfer_3000 Rfer_3001
            POL: Bpro_1637 Bpro_1638 Bpro_2560
            PNA: Pnap_1100
            AAV: Aave_2824
            AJS: Ajs_2019
            VEI: Veis_2561
            MPT: Mpe_A2142 Mpe_A3753
            HAR: HEAR0111(ogt) HEAR0419
            MMS: mma_0135 mma_0136 mma_0473
            NEU: NE0885(ogt)
            NET: Neut_1220
            NMU: Nmul_A0747
            EBA: ebA4378(ada) ebA7193(ada)
            AZO: azo2292(ada)
            DAR: Daro_0538
            TBD: Tbd_2377
            MFA: Mfla_2330
            HPY: HP0676(dat1)
            HPA: HPAG1_0659
            HHE: HH1037(ogt)
            HAC: Hac_0859(dat1)
            WSU: WS1539 WS1612
            TDN: Tmden_0684 Tmden_1946
            CJE: Cj0836(ogt)
            CJR: CJE0923(ogt)
            CJJ: CJJ81176_0853(ogt)
            CJU: C8J_0783(ogt)
            CJD: JJD26997_0987(ogt)
            CFF: CFF8240_0998
            CCV: CCV52592_1412
            CHA: CHAB381_1422
            CCO: CCC13826_1409
            ABU: Abu_1461(ada) Abu_1763(ogt)
            SUN: SUN_0951
            GSU: GSU1173
            GME: Gmet_0090
            GUR: Gura_0130 Gura_0199
            PCA: Pcar_3000
            PPD: Ppro_1338
            DVU: DVU0791
            DDE: Dde_0998
            LIP: LI0023(ogt)
            BBA: Bd0252 Bd0253(ada) Bd0389(ogt)
            DPS: DP0920
            ADE: Adeh_0099 Adeh_0969
            AFW: Anae109_3413 Anae109_3549 Anae109_3565
            MXA: MXAN_2611(ogt) MXAN_5899(ada)
            SFU: Sfum_1733
            RCO: RC0870(dat)
            RFE: RF_0915 RF_0916(dat)
            RBE: RBE_0693(dat)
            PUB: SAR11_1021(ada)
            MLO: mlr1858 mlr1860 mlr2526 mlr3180
            MES: Meso_2104 Meso_3569
            PLA: Plav_0043 Plav_0734 Plav_3485
            SME: SMb20708 SMc01728(ada) SMc02841
            SMD: Smed_0699 Smed_0729
            ATU: Atu0901(ada) Atu1220 Atu4459(ada)
            ATC: AGR_C_1643 AGR_C_2253 AGR_L_818
            RET: RHE_CH00287(ypch00105) RHE_CH00423(ada)
                 RHE_CH03669(ypch01307)
            RLE: RL0293 RL0442(ada) RL4205
            BME: BMEI1558 BMEI1762 BMEII0405
            BMF: BAB1_0185 BAB1_0398 BAB2_0347
            BMS: BR0185(ogt) BR0368(ada) BRA0889
            BMB: BruAb1_0181(ogt) BruAb1_0394(ada) BruAb2_0343
            BOV: BOV_0179(ogt) BOV_0383(ada)
            OAN: Oant_0429 Oant_0562
            BJA: bll0687 bll1113 bll7808 blr0915(ogt)
            BRA: BRADO0154 BRADO6430(ogt) BRADO6764(ogt2)
            BBT: BBta_0199 BBta_0775(ogt2) BBta_1204(ogt)
            RPA: RPA0341(ogt) RPA4427(ogt1) RPA4762(ogt2)
            RPB: RPB_0437 RPB_0800 RPB_4236
            RPC: RPC_1345 RPC_4898
            RPD: RPD_0383 RPD_0909 RPD_4087
            RPE: RPE_0486 RPE_4328 RPE_4869
            NWI: Nwi_0203 Nwi_0571 Nwi_0572
            NHA: Nham_0160 Nham_0663
            BHE: BH04820
            BQU: BQ04020
            XAU: Xaut_1183 Xaut_2402
            CCR: CC_0659 CC_0689 CC_3729
            SIL: SPO3134(ogt) SPO3311 SPO3578
            SIT: TM1040_2450 TM1040_2682
            RSP: RSP_0567 RSP_1032
            RSQ: Rsph17025_1064
            JAN: Jann_1668 Jann_3470
            RDE: RD1_0965(ada) RD1_2075(ogt)
            PDE: Pden_2432
            HNE: HNE_3385(ada)
            ZMO: ZMO1989
            SWI: Swit_1248 Swit_4092 Swit_4715
            GOX: GOX1069
            GBE: GbCGDNIH1_0015
            ACR: Acry_0403 Acry_1541
            RRU: Rru_A3358 Rru_A3621
            MAG: amb4556
            MGM: Mmc1_0135
            ABA: Acid345_0273 Acid345_1283
            SUS: Acid_1258 Acid_4002
            BSU: BG10166(adaA) BG10167(adaB) BG10848(ogt)
            BHA: BH0393(adaB) BH0394(adaA) BH1021(dat)
            BAN: BA2039(ogt-1) BA3869(adaA) BA3870(ogt-2)
            BAR: GBAA2039(ogt-1) GBAA3869(adaA) GBAA3870(ogt-2)
            BAA: BA_2538 BA_4344 BA_4345
            BAT: BAS1892 BAS3585 BAS3586
            BCE: BC2024 BC3740 BC3741
            BCA: BCE_2107(ogt) BCE_3772(adaA) BCE_3773(ogt)
            BCZ: BCZK1844(ogt) BCZK2914(adaA) BCZK3497(adaA) BCZK3498(ogt)
            BCY: Bcer98_0077 Bcer98_1530
            BTK: BT9727_1854(ogt) BT9727_3485(adaA) BT9727_3486(ogt)
            BTL: BALH_1799 BALH_3368(adaA) BALH_3369
            BLI: BL00477(adaB) BL03537(ogt) BL05281(adaA)
            BLD: BLi01510(ogt) BLi02837(adaB)
            BCL: ABC1467(ogt) ABC3154(adaB)
            BAY: RBAM_013320 RBAM_037960
            BPU: BPUM_1248
            OIH: OB0736
            GKA: GK0945
            SAU: SA2335(adaB)
            SAV: SAV2547(adaB)
            SAM: MW2468(adaB)
            SAR: SAR2627
            SAS: SAS2433
            SAC: SACOL2562(ogt)
            SAB: SAB2422c(adaB)
            SAA: SAUSA300_2485
            SAO: SAOUHSC_02861
            SAJ: SaurJH9_0548
            SAH: SaurJH1_0562
            SEP: SE2111
            SER: SERP2123(ogt)
            SHA: SH0507
            SSP: SSP0322
            LMO: lmo0076 lmo0996 lmo2242
            LMF: LMOf2365_0093(ada) LMOf2365_0600(ogt-1) LMOf2365_1017(ogt-2)
            LIN: lin0068 lin0995 lin2344
            LWE: lwe0537(ogt) lwe0979 lwe2259 lwe2260
            LLA: L118481(ogt)
            LLM: llmg_0498(ogt) llmg_0499(adaA)
            SPN: SP_1463
            SPR: spr1317(ogt)
            SPD: SPD_1292(ogt)
            SAG: SAG1565(ogt)
            SAN: gbs1618
            SAK: SAK_1583
            SMU: SMU.1652(ogt)
            SSA: SSA_1583(ogt) SSA_1771
            SSU: SSU05_0668
            SSV: SSU98_0668
            SGO: SGO_1535(ogt) SGO_1662
            LPL: lp_2848(ogt)
            LJO: LJ0252
            LAC: LBA0255
            LSA: LSA1843(ogt)
            LSL: LSL_0559(ada)
            LBR: LVIS_0321
            LCA: LSEI_0144
            LGA: LGAS_0245
            LRE: Lreu_0301
            EFA: EF0277(ogt)
            OOE: OEOE_0799
            STH: STH1026
            CAC: CAC3261(ada)
            CPE: CPE0342
            CPF: CPF_0326(ogt)
            CTC: CTC01413
            CTH: Cthe_1554
            CDF: CD0601(ogt1) CD1770(ogt2)
            CBO: CBO1532(ogt)
            CBA: CLB_1552(ogt)
            CBH: CLC_1564(ogt)
            CBF: CLI_1611(ogt)
            CBE: Cbei_0126 Cbei_0456 Cbei_0792
            CKL: CKL_0119(ogt)
            AMT: Amet_0017 Amet_4511
            CHY: CHY_0809(ogt)
            DSY: DSY1018 DSY1019 DSY4032 DSY4761
            SWO: Swol_1600
            CSC: Csac_1088 Csac_1347 Csac_1777
            TTE: TTE2519(ada)
            MTA: Moth_1354
            MPU: MYPU_0950(ogt)
            MPE: MYPE1850
            MTU: Rv1316c(ogt) Rv1317c(alkA)
            MTC: MT1357(ogt) MT1358
            MBO: Mb1349c(ogt) Mb1350c(alkAb) Mb1351c(alkAa)
            MBB: BCG_1377c(ogt) BCG_1378c(alkA)
            MLE: ML1151(ogt)
            MPA: MAP2443(alkA) MAP2445(ogt)
            MAV: MAV_1536 MAV_4152
            MSM: MSMEG_1939 MSMEG_4316 MSMEG_4928
            MUL: MUL_3946(ogt)
            MVA: Mvan_4323
            MGI: Mflv_2325
            MMC: Mmcs_2223 Mmcs_3871
            MKM: Mkms_3945
            MJL: Mjls_3857
            CGL: NCgl2901(cgl3003)
            CGB: cg3331(ogt)
            CEF: CE2837
            CJK: jk0188(ogt)
            NFA: nfa47900(alkA) nfa47910 nfa53680
            RHA: RHA1_ro02330 RHA1_ro02332 RHA1_ro05553
            SCO: SCO1969(SC3C9.04) SCO6150(SC1A9.14) SCO6151(SC1A9.15)
                 SCO6461(SC9B5.28) SCO6462(SC9B5.29)
            SMA: SAV1933(ogt1) SAV1934(alkA1) SAV2053(ogt2) SAV2085(alkA2)
                 SAV6270(ogt3)
            TWH: TWT465(ogt)
            TWS: TW300
            LXX: Lxx07100(ada)
            CMI: CMM_0242(ogtA) CMM_1173(ogtB)
            AAU: AAur_0021 AAur_0023
            PAC: PPA1428
            NCA: Noca_3300
            TFU: Tfu_0366
            FRA: Francci3_0147 Francci3_0149
            FAL: FRAAL0154(ada) FRAAL4287(ogt) FRAAL6049
            ACE: Acel_1884
            KRA: Krad_0603 Krad_3557
            SEN: SACE_0955(alkA) SACE_2073(ogt3) SACE_3676(alkA1)
                 SACE_3677(ogt1) SACE_4099 SACE_6024(ogt)
            STP: Strop_4269
            BLO: BL0335(ogt)
            BAD: BAD_0634
            FNU: FN0117
            RBA: RB1606
            CTR: CT477(ada)
            CTA: CTA_0523(ada)
            CMU: TC0762
            CPN: CPn0596(ada)
            CPA: CP0152
            CPJ: CPj0596(ada)
            CPT: CpB0620
            CCA: CCA00145(ada)
            CAB: CAB143(ada)
            CFE: CF0862(ada)
            PCU: pc1834(alkA) pc1835(ada)
            TPA: TP0141
            TDE: TDE0217(ogt)
            LIL: LA4251
            LIC: LIC13402(ada)
            LBJ: LBJ_2922(ada)
            LBL: LBL_0141(ada)
            SYC: syc1356_d
            SYF: Synpcc7942_0149
            GVI: glr3609 glr3610
            ANA: alr4990
            AVA: Ava_2278
            PMF: P9303_20691
            BTH: BT_1411
            BFR: BF4302
            BFS: BF4111
            PGI: PG0486(ogt)
            SRU: SRU_2179
            CHU: CHU_3799(ada)
            GFO: GFO_0122 GFO_3234
            FJO: Fjoh_0828 Fjoh_0876 Fjoh_4055
            FPS: FP0033(ogt1) FP0370(ogt2)
            CTE: CT1289(ogt)
            CCH: Cag_0890
            CPH: Cpha266_1565
            DET: DET1460(ogt)
            DEH: cbdb_A1428(ogt)
            DEB: DehaBAV1_0052 DehaBAV1_1338
            RRS: RoseRS_0438 RoseRS_1732
            RCA: Rcas_1004 Rcas_2017
            TTH: TTC1199
            TTJ: TTHA1564
            AAE: aq_1495(ogt)
            TMA: TM0887
            TPT: Tpet_0725 Tpet_1147
            TME: Tmel_0023 Tmel_1583
            FNO: Fnod_0363 Fnod_1309
            MMZ: MmarC7_0488
            MAE: Maeo_0546
            MVN: Mevan_0556
            MAC: MA4322(ogt)
            MBA: Mbar_A0598
            MMA: MM_1020
            MBU: Mbur_2220
            MHU: Mhun_0964
            MST: Msp_1499
            MKA: MK0130(ada)
            HWA: HQ1160A(ogt)
            PTO: PTO1429
            PAB: PAB0260(ogt)
            PFU: PF1878
            TKO: TK1971
            APE: APE_0959
            IHO: Igni_0641
            SSO: SSO2487(ogt)
            STO: ST0967
            SAI: Saci_1260
            MSE: Msed_1586
            PAI: PAE2012
STRUCTURES  PDB: 1EH6  1EH7  1EH8  1MGT  1QNT  1SFE  1T38  1T39  1WRJ  1YFH  
                 2G7H  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.63
            ExPASy - ENZYME nomenclature database: 2.1.1.63
            ExplorEnz - The Enzyme Database: 2.1.1.63
            ERGO genome analysis and discovery system: 2.1.1.63
            BRENDA, the Enzyme Database: 2.1.1.63
            CAS: 77271-19-3
///
ENTRY       EC 2.1.1.64                 Enzyme
NAME        3-demethylubiquinone-9 3-O-methyltransferase;
            5-demethylubiquinone-9 methyltransferase;
            OMHMB-methyltransferase;
            2-Octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone
            methyltransferase;
            S-adenosyl-L-methionine:2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-
            1,4-benzoquinone-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:2-nonaprenyl-3-methyl-5-hydroxy-6-methoxy-1,
            4-benzoquinone 3-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 3-demethylubiquinone-9 =
            S-adenosyl-L-homocysteine + ubiquinone-9 [RN:R07235]
ALL_REAC    R07235;
            (other) R04988 R05614
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            3-demethylubiquinone-9 [CPD:C03226]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            ubiquinone-9 [CPD:C01967]
REFERENCE   1  [PMID:863914]
  AUTHORS   Houser RM, Olson RE.
  TITLE     5-demethylubiquinone-9-methyltransferase from rat liver
            mitochondria. Characterization, localization, and solubilization.
  JOURNAL   J. Biol. Chem. 252 (1977) 4017-21.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:769831]
  AUTHORS   Leppik RA, Stroobant P, Shineberg B, Young IG, Gibson F.
  TITLE     Membrane-associated reactions in ubiquinone biosynthesis.
            2-Octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone
            methyltransferase.
  JOURNAL   Biochim. Biophys. Acta. 428 (1976) 146-56.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00130  Ubiquinone biosynthesis
ORTHOLOGY   KO: K00568  3-demethylubiquinone-9 3-methyltransferase
GENES       AFM: AFUA_4G10370
            CNE: CNK00940
            UMA: UM03054.1
            PFA: MAL7P1.130
            TET: TTHERM_00803600
            TBR: Tb09.211.1960
            TCR: 506147.60 508461.30
            LMA: LmjF35.4250
            ECO: b2232(ubiG)
            ECJ: JW2226(ubiG)
            ECE: Z3486(ubiG)
            ECS: ECs3115
            ECC: c2774(ubiG)
            ECI: UTI89_C2513(ubiG)
            ECP: ECP_2275
            ECV: APECO1_4328(ubiG)
            ECW: EcE24377A_2527(ubiG)
            ECX: EcHS_A2372(ubiG)
            STY: STY2505(ubiG)
            STT: t0588(ubiG)
            SPT: SPA0588(ubiG)
            SEC: SC2279(ubiG)
            STM: STM2276(ubiG)
            YPE: YPO1215(ubiG)
            YPK: y2973(ubiG)
            YPM: YP_0922(ubiG)
            YPA: YPA_0929
            YPN: YPN_2762
            YPP: YPDSF_2478
            YPS: YPTB1255(ubiG)
            YPI: YpsIP31758_2768(ubiG)
            YEN: YE1394(pufX)
            SFL: SF2312(ubiG)
            SFX: S2445(ubiG)
            SFV: SFV_2303(ubiG)
            SSN: SSON_2290(ubiG)
            SBO: SBO_2064(ubiG)
            SDY: SDY_2424(ubiG)
            ECA: ECA1200(ubiG)
            PLU: plu3051(ubiG)
            WBR: WGLp444(ubiG)
            SGL: SG1583
            ENT: Ent638_2800
            KPN: KPN_02641(ubiG)
            SPE: Spro_3270
            BFL: Bfl477(ubiG)
            BPN: BPEN_493(ubiG)
            HDU: HD1750(ubiG)
            HSO: HS_1162(ubiG)
            PMU: PM0840(ubiG)
            APL: APL_0285(ubiG)
            XFA: XF2471
            XFT: PD1488(ubiG)
            XCC: XCC2269(ubiG)
            XCB: XC_1846
            XCV: XCV2574(ubiG)
            XAC: XAC2377(ubiG)
            XOO: XOO2702(ubiG)
            XOM: XOO_2548(XOO2548)
            VCH: VC1257
            VCO: VC0395_A0876(ubiG)
            VVU: VV1_3040
            VVY: VV1246
            VPA: VP1933
            VFI: VF1203
            PPR: PBPRA2457
            PAE: PA3171(ubiG)
            PAU: PA14_23220(ubiG)
            PAP: PSPA7_1958(ubiG)
            PPU: PP_1765(ubiG)
            PPF: Pput_3949
            PST: PSPTO_1742(ubiG)
            PSB: Psyr_3650
            PSP: PSPPH_3670(ubiG)
            PFL: PFL_4317(ubiG)
            PFO: Pfl_4081
            PEN: PSEEN1484(ubiG)
            PMY: Pmen_1845
            PAR: Psyc_0121(ubiG)
            PCR: Pcryo_0130
            PRW: PsycPRwf_2117
            ACI: ACIAD0044(ubiG)
            SON: SO_2413(ubiG)
            SDN: Sden_1949
            SFR: Sfri_2131
            SAZ: Sama_1730
            SBL: Sbal_2061
            SBM: Shew185_2288
            SLO: Shew_1948 Shew_3858
            SPC: Sputcn32_2071
            SSE: Ssed_2304 Ssed_4499
            SPL: Spea_2066
            SHE: Shewmr4_1918
            SHM: Shewmr7_2060
            SHN: Shewana3_1971
            SHW: Sputw3181_1941
            ILO: IL1361(ubiG)
            CPS: CPS_2330(ubiG)
            PHA: PSHAa1420(ubiG)
            PAT: Patl_2471
            SDE: Sde_2150
            PIN: Ping_1113 Ping_2534
            MAQ: Maqu_2495
            CBU: CBU_0350(ubiG)
            CBD: COXBU7E912_1729(ubiG)
            LPN: lpg1699(ubiG)
            LPF: lpl1658(ubiG)
            LPP: lpp1664(ubiG)
            MCA: MCA1272(ubiG)
            FTU: FTT1590c(ubiG)
            FTF: FTF1590c(ubiG)
            FTL: FTL_1638
            FTH: FTH_1581(ubiG)
            FTN: FTN_0321(ubiG)
            TCX: Tcr_1190
            NOC: Noc_2296
            AEH: Mlg_0910
            HHA: Hhal_0575
            HCH: HCH_04357(ubiG1)
            CSA: Csal_1858
            ABO: ABO_1753(ubiG)
            MMW: Mmwyl1_2861
            RMA: Rmag_0608
            VOK: COSY_0561(ubiG)
            NME: NMB2030
            NMA: NMA0410(ubiG)
            NMC: NMC2009(ubiG)
            NGO: NGO2074
            CVI: CV_1031(ubiG)
            RSO: RSc0898(ubiG)
            REU: Reut_A2580
            REH: H16_A0787(ubiG) H16_A1649
            RME: Rmet_0711
            BMA: BMA0437(ubiG)
            BMV: BMASAVP1_A2582(ubiG)
            BML: BMA10299_A0956(ubiG)
            BMN: BMA10247_0191(ubiG)
            BXE: Bxe_A0972
            BVI: Bcep1808_0959
            BUR: Bcep18194_A4151 Bcep18194_B1676
            BCN: Bcen_0559
            BCH: Bcen2424_1038
            BAM: Bamb_0914
            BPS: BPSL2523(ubiG)
            BPM: BURPS1710b_3003(ubiG)
            BPL: BURPS1106A_2954(ubiG)
            BPD: BURPS668_2892(ubiG)
            BTE: BTH_I1630(ubiG)
            PNU: Pnuc_0491
            BPE: BP0942(ubiG)
            BPA: BPP3136(ubiG)
            BBR: BB3475(ubiG)
            RFR: Rfer_2828
            POL: Bpro_1797
            PNA: Pnap_2788
            AAV: Aave_3278
            AJS: Ajs_2462
            VEI: Veis_3117
            MPT: Mpe_A2236
            HAR: HEAR2584(ubiG)
            MMS: mma_2678(ubiG)
            NEU: NE2547(ubiG)
            NET: Neut_2507
            NMU: Nmul_A2186
            EBA: ebA914(ubiG)
            AZO: azo2589(ubiG)
            DAR: Daro_1227
            TBD: Tbd_0946
            MFA: Mfla_1576
            BBA: Bd3625(ubiG)
            SFU: Sfum_3425
            RPR: RP622(ubiG)
            RTY: RT0613(ubiG)
            RCO: RC0965(ubiG)
            RFE: RF_0414(ubiG)
            RBE: RBE_0456(ubiG)
            RAK: A1C_04890
            RBO: A1I_05420
            RCM: A1E_01645
            RRI: A1G_05300
            OTS: OTBS_1641(ubiG)
            WOL: WD0350
            WBM: Wbm0195
            AMA: AM566(ubiG) AM571(ubiG)
            APH: APH_0606(ubiG)
            ERU: Erum4110(ubiG)
            ERW: ERWE_CDS_04270(ubiG)
            ERG: ERGA_CDS_04210(ubiG)
            ECN: Ecaj_0402
            ECH: ECH_0637(ubiG)
            NSE: NSE_0628(ubiG)
            PUB: SAR11_0515(ubiG)
            MLO: mlr3442
            MES: Meso_3002
            PLA: Plav_1742
            SME: SMc02440(ubiG)
            SMD: Smed_2506
            ATU: Atu3508(ubiG)
            ATC: AGR_L_2640
            RET: RHE_CH02423 RHE_CH03759(ubiG)
            RLE: RL1651(ubiG) RL2758 RL2996 RL4286(ubiG)
            BME: BMEI0188 BMEI0923
            BMF: BAB1_1085 BAB1_1875(ubiG)
            BMS: BR1872(ubiG)
            BOV: BOV_1803(ubiG)
            OAN: Oant_1033
            BJA: bll0214(ubiG)
            BRA: BRADO0576(ubiG) BRADO2072 BRADO4440 BRADO6627(ubiG)
            BBT: BBta_0908(ubiG) BBta_7600(ubiG)
            RPA: RPA0603(ubiG)
            RPB: RPB_0079
            RPC: RPC_0515
            RPD: RPD_0100
            RPE: RPE_0157
            NWI: Nwi_0381
            NHA: Nham_0474
            BHE: BH04020(ubiG)
            BQU: BQ03050(ubiG)
            BBK: BARBAKC583_0369(ubiG)
            XAU: Xaut_3086
            CCR: CC_0840
            SIL: SPO0067(ubiG)
            SIT: TM1040_2906
            RSP: RSP_1175(ubiG)
            RSH: Rsph17029_2837
            RSQ: Rsph17025_2768
            JAN: Jann_0298
            RDE: RD1_0392(ubiG) RD1_0737(ubiG)
            PDE: Pden_2589
            MMR: Mmar10_2260
            HNE: HNE_0617(ubiG)
            ZMO: ZMO1654(ubiG) ZMO1889
            NAR: Saro_3303
            SAL: Sala_2143
            SWI: Swit_4502
            ELI: ELI_14535
            GOX: GOX0038
            GBE: GbCGDNIH1_0599
            ACR: Acry_1007
            RRU: Rru_A0742
            MAG: amb1611
            MGM: Mmc1_2130
            ABA: Acid345_1669
            CGL: NCgl1242(cgl1291)
            RHA: RHA1_ro05098 RHA1_ro06461 RHA1_ro07034
            FAL: FRAAL0024 FRAAL2062 FRAAL6458
            RBA: RB8612(ubiG)
            LIL: LA1350(ubiG)
            LBL: LBL_2333
            SRU: SRU_0613
            DRA: DR_2562
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.64
            ExPASy - ENZYME nomenclature database: 2.1.1.64
            ExplorEnz - The Enzyme Database: 2.1.1.64
            ERGO genome analysis and discovery system: 2.1.1.64
            BRENDA, the Enzyme Database: 2.1.1.64
            CAS: 63774-48-1
///
ENTRY       EC 2.1.1.65                 Enzyme
NAME        licodione 2'-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:licodione 2'-O-methyltransferase
REACTION    S-adenosyl-L-methionine + licodione = S-adenosyl-L-homocysteine +
            2'-O-methyllicodione [RN:R03623]
ALL_REAC    R03623
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            licodione [CPD:C01592]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            2'-O-methyllicodione [CPD:C02922]
COMMENT     As well as licodione
            [1-(2,4-dihydroxyphenyl)-3-(4-hydroxyphenyl)-1,3-propanedione], the
            2"-hydroxy-derivative and isoliquiritigenin can act as acceptors,
            but more slowly.
REFERENCE   1
  AUTHORS   Ayabe, S.-I., Yoshikawa, T., Kobayashi, M. and Furuya, T.
  TITLE     Biosynthesis of retrochalcone, echinatin: involvement of
            O-methyltransferase to licodione.
  JOURNAL   Phytochemistry 19 (1980) 2331-2336.
  ORGANISM  Glycyrrhiza echinata
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.65
            ExPASy - ENZYME nomenclature database: 2.1.1.65
            ExplorEnz - The Enzyme Database: 2.1.1.65
            ERGO genome analysis and discovery system: 2.1.1.65
            BRENDA, the Enzyme Database: 2.1.1.65
            CAS: 77000-07-8
///
ENTRY       EC 2.1.1.66                 Enzyme
NAME        rRNA (adenosine-2'-O-)-methyltransferase;
            ribosomal ribonucleate adenosine 2'-methyltransferase;
            rRNA adenosine 2'-methylase;
            RNA-pentose methylase;
            thiostrepton-resistance methylase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:rRNA (adenosine-2'-O)-methyltransferase
REACTION    S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA
            containing a single residue of 2'-O-methyladenosine [RN:R01675]
ALL_REAC    R01675
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            rRNA [CPD:C00240]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            rRNA containing a single residue of 2'-O-methyladenosine
            [CPD:C04779]
REFERENCE   1
  AUTHORS   Thompson, J. and Cundliffe, E.
  TITLE     Purification and properties of an RNA methylase produced by
            Streptomyces azureus and involved in resistance to thiostrepton.
  JOURNAL   J. Gen. Microbiol. 124 (1981) 291-297.
  ORGANISM  Streptomyces azureus
ORTHOLOGY   KO: K05926  
GENES       CGL: NCgl0791(cgl0825)
            RBA: RB8060(spoU)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.66
            ExPASy - ENZYME nomenclature database: 2.1.1.66
            ExplorEnz - The Enzyme Database: 2.1.1.66
            ERGO genome analysis and discovery system: 2.1.1.66
            BRENDA, the Enzyme Database: 2.1.1.66
            CAS: 80146-87-8
///
ENTRY       EC 2.1.1.67                 Enzyme
NAME        thiopurine S-methyltransferase;
            mercaptopurine methyltransferase;
            thiopurine methyltransferase;
            6-thiopurine transmethylase;
            TPMT
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:thiopurine S-methyltransferase
REACTION    S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine +
            a thiopurine S-methylether [RN:R03701]
ALL_REAC    R03701
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            thiopurine [CPD:C01756]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            thiopurine S-methylether [CPD:C03542]
COMMENT     Also acts, more slowly, on thiopyrimidines and aromatic thiols. Not
            identical with EC 2.1.1.9 thiol S-methyltransferase.
REFERENCE   1
  AUTHORS   Remy, C.N.
  TITLE     Metabolism of thiopyrimidines and thiopurines. S-Methylation with
            S-adenosylmethionine transmethylase and catabolism in mammalian
            tissues.
  JOURNAL   J. Biol. Chem. 238 (1963) 1078-1084.
  ORGANISM  Escherichia coli [GN:eco], rat [GN:rno]
REFERENCE   2  [PMID:6633508]
  AUTHORS   Woodson LC, Ames MM, Selassie CD, Hansch C, Weinshilboum RM.
  TITLE     Thiopurine methyltransferase. Aromatic thiol substrates and
            inhibition by benzoic acid derivatives.
  JOURNAL   Mol. Pharmacol. 24 (1983) 471-8.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:6838629]
  AUTHORS   Woodson LC, Weinshilboum RM.
  TITLE     Human kidney thiopurine methyltransferase. Purification and
            biochemical properties.
  JOURNAL   Biochem. Pharmacol. 32 (1983) 819-26.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K00569  thiopurine S-methyltransferase
GENES       HSA: 7172(TPMT)
            PTR: 471863(TPMT)
            MMU: 22017(Tpmt)
            CFA: 403536(TPMT)
            GGA: 420830(TPMT)
            XCC: XCC1394(tpmT)
            XCB: XC_2843
            XCV: XCV1496(tpmT)
            XAC: XAC1439(tpmT)
            VCH: VC1226
            VCO: VC0395_A0849
            VVU: VV1_2377
            VVY: VV1964
            VPA: VP1296
            VFI: VF1512
            PPR: PBPRA1684
            PAE: PA2832(tpm)
            PAU: PA14_27460(tpm)
            PPU: PP_1870(tpm)
            PPF: Pput_3845
            PST: PSPTO_1777(tpm)
            PSB: Psyr_3617
            PFL: PFL_4249
            PFO: Pfl_3985
            PEN: PSEEN1581(tpm)
            PMY: Pmen_2525
            PCR: Pcryo_1333 Pcryo_2081 Pcryo_2244
            PRW: PsycPRwf_0288
            ACI: ACIAD2922(tpm)
            SON: SO_0582(tpm)
            SDN: Sden_0541
            SFR: Sfri_3498
            SAZ: Sama_0543
            SBL: Sbal_0541
            SBM: Shew185_3784
            SLO: Shew_3261
            SPC: Sputcn32_3296
            SSE: Ssed_4010
            SPL: Spea_0588
            SHE: Shewmr4_0581
            SHM: Shewmr7_3449
            SHN: Shewana3_0580
            SHW: Sputw3181_0645
            CPS: CPS_3096
            PAT: Patl_1524
            MAQ: Maqu_3055
            LPN: lpg2835(tpm)
            LPF: lpl2747
            LPP: lpp2892
            MCA: MCA0794
            FTU: FTT1661(tmpT)
            FTF: FTF1661(tmpT)
            FTL: FTL_0032
            FTH: FTH_0031(tpmT)
            FTA: FTA_0039
            FTN: FTN_0023(tmpT)
            TCX: Tcr_1758
            HCH: HCH_01328
            CSA: Csal_2332
            MMW: Mmwyl1_1365
            AHA: AHA_1996(tpm)
            BPE: BP0873(tpm)
            BPA: BPP2160(tpm)
            BBR: BB1557(tpm)
            NET: Neut_2272
            NMU: Nmul_A2259
            DAR: Daro_0514
            XAU: Xaut_2726
            GOX: GOX0680
            MGM: Mmc1_0515
            LBJ: LBJ_0800
            SYX: SynWH7803_0885
            GFO: GFO_2405(tpm)
STRUCTURES  PDB: 1PJZ  2BZG  2GB4  2H11  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.67
            ExPASy - ENZYME nomenclature database: 2.1.1.67
            ExplorEnz - The Enzyme Database: 2.1.1.67
            ERGO genome analysis and discovery system: 2.1.1.67
            BRENDA, the Enzyme Database: 2.1.1.67
            CAS: 67339-09-7
///
ENTRY       EC 2.1.1.68                 Enzyme
NAME        caffeate O-methyltransferase;
            caffeate methyltransferase;
            caffeate 3-O-methyltransferase;
            S-adenosyl-L-methionine:caffeic acid-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:3,4-dihydroxy-trans-cinnamate
            3-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate =
            S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
            [RN:R03366]
ALL_REAC    R03366;
            (other) R02379 R06574 R06575 R06576 R06577
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            3,4-dihydroxy-trans-cinnamate [CPD:C01197]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            3-methoxy-4-hydroxy-trans-cinnamate [CPD:C01494]
COMMENT     3,4-Dihydroxybenzaldehyde and catechol can act as acceptors, but
            more slowly.
REFERENCE   1  [PMID:4472044]
  AUTHORS   Ebel J, Schaller-Hekeler B, Knobloch KH, Wellman E, Grisebach H,
            Hahlbrock K.
  TITLE     Coordinated changes in enzyme activities of phenylpropanoid
            metabolism during the growth of soybean cell suspension cultures.
  JOURNAL   Biochim. Biophys. Acta. 362 (1974) 417-24.
  ORGANISM  Glycine max [GN:egma]
REFERENCE   2  [PMID:241400]
  AUTHORS   Poulton JE, Butt VS.
  TITLE     Purification and properties of S-adenosyl-L-methionine: caffeic acid
            O-methyltransferase from leaves of spinach beet (Beta vulgaris L).
  JOURNAL   Biochim. Biophys. Acta. 403 (1975) 301-14.
  ORGANISM  Beta vulgaris
REFERENCE   3
  AUTHORS   Shimada, M., Kuroda, H. and Higuchi, T.
  TITLE     Evidence for the formation of methoxyl groups of ferulic and sinapic
            acid in Bambusa by the same O-methyltransferase.
  JOURNAL   Phytochemistry 12 (1973) 2873-2875.
  ORGANISM  Bambusa sp.
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
STRUCTURES  PDB: 1KYW  1KYZ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.68
            ExPASy - ENZYME nomenclature database: 2.1.1.68
            ExplorEnz - The Enzyme Database: 2.1.1.68
            ERGO genome analysis and discovery system: 2.1.1.68
            BRENDA, the Enzyme Database: 2.1.1.68
            CAS: 50936-45-3
///
ENTRY       EC 2.1.1.69                 Enzyme
NAME        5-hydroxyfuranocoumarin 5-O-methyltransferase;
            furanocoumarin 5-methyltransferase;
            furanocoumarin 5-O-methyltransferase;
            bergaptol 5-O-methyltransferase;
            bergaptol O-methyltransferase;
            bergaptol methyltransferase;
            S-adenosyl-L-methionine:bergaptol O-methyltransferase;
            BMT;
            S-adenosyl-L-methionine:5-hydroxyfuranocoumarin
            5-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:5-hydroxyfurocoumarin 5-O-methyltransferase
REACTION    (1) S-adenosyl-L-methionine + a 5-hydroxyfurocoumarin =
            S-adenosyl-L-homocysteine + a 5-methoxyfurocoumarin (general
            reaction);
            (2) S-adenosyl-L-methionine + bergaptol = S-adenosyl-L-homocysteine
            + bergapten [RN:R02882]
ALL_REAC    R02882
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            5-hydroxyfurocoumarin;
            bergaptol [CPD:C00758]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            5-methoxyfurocoumarin;
            bergapten [CPD:C01557]
COMMENT     Converts bergaptol into bergapten, which has therapeutic potential
            in the treatment of psoriasis as it has photosensitizing and
            antiproliferative activities [4]. The enzyme methylates the
            5-hydroxy group of some hydroxy- and methylcoumarins, but has little
            activity on non-coumarin phenols [1]. Caffeate, 5-hydroxyferulate
            and daphnetin are not substrates [4]. Cu2+, Zn2+ and Co2+ cause
            enzyme inhibition [4]. (see also EC 2.1.1.70,
            8-hydroxyfuranocoumarin 8-O-methyltransferase)
REFERENCE   1  [PMID:28084]
  AUTHORS   Thompson HJ, Sharma SK, Brown SA.
  TITLE     O-methyltransferases of furanocoumarin biosynthesis.
  JOURNAL   Arch. Biochem. Biophys. 188 (1978) 272-81.
  ORGANISM  Ruta graveolens, Heracleum lanatum
REFERENCE   2  [PMID:156999]
  AUTHORS   Sharma SK, Garrett JM, Brown SA.
  TITLE     Separation of the S-adenosylmethionine: 5- and
            8-hydroxyfuranocoumarin O-methyltransferases of Ruta graveolens L.
            by general ligand affinity chromatography.
  JOURNAL   Z. Naturforsch. [C]. 34C (1979) 387-91.
REFERENCE   3
  AUTHORS   Hauffe, K.D., Hahlbrock, K. and Scheel, D.
  TITLE     Elicitor-stimulated furanocoumarin biosynthesis in cultured parsley
            cells - S-adenosyl-L-methionine-bergaptol and
            S-adenosyl-L-methionine-xanthotoxol O-methyltransferases.
  JOURNAL   Z. Naturforsch. C: Biosci. 41 (1986) 228-239.
REFERENCE   4  [PMID:15009205]
  AUTHORS   Hehmann M, Lukacin R, Ekiert H, Matern U.
  TITLE     Furanocoumarin biosynthesis in Ammi majus L. Cloning of bergaptol
            O-methyltransferase.
  JOURNAL   Eur. J. Biochem. 271 (2004) 932-40.
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.69
            ExPASy - ENZYME nomenclature database: 2.1.1.69
            ExplorEnz - The Enzyme Database: 2.1.1.69
            ERGO genome analysis and discovery system: 2.1.1.69
            BRENDA, the Enzyme Database: 2.1.1.69
            CAS: 67339-12-2
///
ENTRY       EC 2.1.1.70                 Enzyme
NAME        8-hydroxyfuranocoumarin 8-O-methyltransferase;
            furanocoumarin 8-methyltransferase;
            furanocoumarin 8-O-methyl-transferase;
            xanthotoxol 8-O-methyltransferase;
            XMT;
            8-hydroxyfuranocoumarin 8-O-methyltransferase;
            S-adenosyl-L-methionine:8-hydroxyfuranocoumarin
            8-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:8-hydroxyfurocoumarin 8-O-methyltransferase
REACTION    (1) S-adenosyl-L-methionine + an 8-hydroxyfurocoumarin =
            S-adenosyl-L-homocysteine + an 8-methoxyfurocoumarin (general
            reaction) [RN:R02982];
            (2) S-adenosyl-L-methionine + xanthotoxol =
            S-adenosyl-L-homocysteine + xanthotoxin
ALL_REAC    R02982
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            8-hydroxyfurocoumarin;
            xanthotoxol [CPD:C00841]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            8-methoxyfurocoumarin;
            xanthotoxin [CPD:C01864]
COMMENT     Converts xanthotoxol into xanthotoxin, which has therapeutic
            potential in the treatment of psoriasis as it has photosensitizing
            and antiproliferative activities [4]. Methylates the 8-hydroxy group
            of some hydroxy- and methylcoumarins, but has little activity on
            non-coumarin phenols. (see also EC 2.1.1.69, 5-hydroxyfuranocoumarin
            5-O-methyltransferase)
REFERENCE   1  [PMID:28084]
  AUTHORS   Thompson HJ, Sharma SK, Brown SA.
  TITLE     O-methyltransferases of furanocoumarin biosynthesis.
  JOURNAL   Arch. Biochem. Biophys. 188 (1978) 272-81.
  ORGANISM  Ruta graveolens, Heracleum lanatum
REFERENCE   2
  AUTHORS   Hauffe, K.D., Hahlbrock, K. and Scheel, D.
  TITLE     Elicitor-stimulated furanocoumarin biosynthesis in cultured parsley
            cells - S-adenosyl-L-methionine-bergaptol and
            S-adenosyl-L-methionine-xanthotoxol O-methyltransferases.
  JOURNAL   Z. Naturforsch. C: Biosci. 41 (1986) 228-239.
REFERENCE   3  [PMID:156999]
  AUTHORS   Sharma SK, Garrett JM, Brown SA.
  TITLE     Separation of the S-adenosylmethionine: 5- and
            8-hydroxyfuranocoumarin O-methyltransferases of Ruta graveolens L.
            by general ligand affinity chromatography.
  JOURNAL   Z. Naturforsch. [C]. 34C (1979) 387-91.
REFERENCE   4  [PMID:15009205]
  AUTHORS   Hehmann M, Lukacin R, Ekiert H, Matern U.
  TITLE     Furanocoumarin biosynthesis in Ammi majus L. Cloning of bergaptol
            O-methyltransferase.
  JOURNAL   Eur. J. Biochem. 271 (2004) 932-40.
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.70
            ExPASy - ENZYME nomenclature database: 2.1.1.70
            ExplorEnz - The Enzyme Database: 2.1.1.70
            ERGO genome analysis and discovery system: 2.1.1.70
            BRENDA, the Enzyme Database: 2.1.1.70
            CAS: 67339-13-3
///
ENTRY       EC 2.1.1.71                 Enzyme
NAME        phosphatidyl-N-methylethanolamine N-methyltransferase;
            phosphatidylmonomethylethanolamine methyltransferase;
            methyltransferase II;
            phospholipid methyltransferase;
            PLMT;
            phosphatidyl-N-methylethanolamine methyltransferase;
            phosphatidyl-N-monomethylethanolamine methyltransferase;
            phosphatidylethanolamine methyltransferase I;
            phosphatidylmonomethylethanolamine methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:phosphatidyl-N-methylethanolamine
            N-methyltransferase
REACTION    S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine =
            S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine
            [RN:R03424]
ALL_REAC    R03424;
            (other) R01320
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            phosphatidyl-N-methylethanolamine [CPD:C01241]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            phosphatidyl-N-dimethylethanolamine [CPD:C04308]
COMMENT     The enzyme also catalyses the transfer of a further methyl group,
            producing phosphatidylcholine.
REFERENCE   1  [PMID:25437]
  AUTHORS   Hirata F, Viveros OH, Diliberto EJ Jr, Axelrod J.
  TITLE     Identification and properties of two methyltransferases in
            conversion of phosphatidylethanolamine to phosphatidylcholine.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 75 (1978) 1718-21.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:438165]
  AUTHORS   Schneider WJ, Vance DE.
  TITLE     Conversion of phosphatidylethanolamine to phosphatidylcholine in rat
            liver. Partial purification and characterization of the enzymatic
            activities.
  JOURNAL   J. Biol. Chem. 254 (1979) 3886-91.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00570  phosphatidyl-N-methylethanolamine N-methyltransferase
GENES       CME: CMA134C
            RET: RHE_CH00316
            RLE: RL0333(pmtA)
            BME: BMEI2000
            GBE: GbCGDNIH1_0800 GbCGDNIH1_2260
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.71
            ExPASy - ENZYME nomenclature database: 2.1.1.71
            ExplorEnz - The Enzyme Database: 2.1.1.71
            ERGO genome analysis and discovery system: 2.1.1.71
            BRENDA, the Enzyme Database: 2.1.1.71
            CAS: 67167-73-1
///
ENTRY       EC 2.1.1.72                 Enzyme
NAME        site-specific DNA-methyltransferase (adenine-specific);
            modification methylase;
            restriction-modification system
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
REACTION    S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine +
            DNA 6-methylaminopurine [RN:R02961]
ALL_REAC    R02961
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            DNA adenine [CPD:C00821]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            DNA 6-methylaminopurine [CPD:C03391]
COMMENT     This is a large group of enzymes, most of which, with enzymes of
            similar site specificity listed as EC 3.1.21.3 type 1 site-specific
            deoxyribonuclease, EC 3.1.21.4 type II site-specific
            deoxyribonuclease or EC 3.1.21.5.
REFERENCE   1  [PMID:2172084]
  AUTHORS   Kessler C, Manta V.
  TITLE     Specificity of restriction endonucleases and DNA modification
            methyltransferases a review (Edition 3).
  JOURNAL   Gene. 92 (1990) 1-248.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:2159140]
  AUTHORS   Roberts RJ.
  TITLE     Restriction enzymes and their isoschizomers.
  JOURNAL   Nucleic. Acids. Res. 18 Suppl (1990) 2331-65.
REFERENCE   3  [PMID:6267988]
  AUTHORS   Yuan R.
  TITLE     Structure and mechanism of multifunctional restriction
            endonucleases.
  JOURNAL   Annu. Rev. Biochem. 50 (1981) 285-319.
ORTHOLOGY   KO: K00571  site-specific DNA-methyltransferase (adenine-specific)
            KO: K03427  type I restriction enzyme M protein
            KO: K06223  DNA adenine methylase
            KO: K07316  adenine-specific DNA-methyltransferase
            KO: K07317  adenine-specific DNA-methyltransferase
            KO: K07318  adenine-specific DNA-methyltransferase
            KO: K07319  putative adenine-specific DNA-methyltransferase
            KO: K07320  putative adenine-specific DNA-methyltransferase
GENES       HSA: 29104(N6AMT1)
            ECO: b2330(yfcB) b3262(yhdJ) b3387(dam) b4349(hsdM)
            ECJ: JW3350(dam) JW4312(hsdM) JW5543(yhdJ) JW5841(prmB)
            ECE: Z2060 Z3593(yfcB) Z4622(yhdJ) Z4740(dam) Z5947
            ECS: ECs1780 ECs3215 ECs4134 ECs4229 ECs5307
            ECC: c0941 c2876(yfcB) c4028(yhdJ) c4157(dam) c5373 c5424
            ECI: UTI89_C1481 UTI89_C2615(prmB) UTI89_C3704(yhdJ)
                 UTI89_C3885(dam) UTI89_C5051(hsdM) UTI89_P075
            ECP: ECP_2369 ECP_3355 ECP_3472 ECP_4677
            ECV: APECO1_2077(hsdM) APECO1_3076(dam) APECO1_3176(yhdJ)
                 APECO1_4234(prmB)
            ECW: EcE24377A_3857(dam)
            ECX: EcHS_A0917 EcHS_A3583
            STY: HCM1.59 STY0388(mod) STY1014 STY2617 STY3566(yhdJ) STY3667
                 STY4312(dam) STY4636 STY4883(hsdM)
            STT: t0479 t1926 t2507(mod) t3301(yhdJ) t3409 t4022(dam) t4329
            SPT: SPA0479(yfcB) SPA2366(mod) SPA2591 SPA3349(dam) SPA4346(hsdM)
            SEC: SC0398(mod) SC2387(yfcB) SC3324(yhdJ) SC3416(dam)
            STM: PSLT059 STM0357(mod) STM2385(yfcB) STM2730 STM3386(yhdJ)
                 STM3484(dam) STM4525(hsdM)
            YPE: YPMT1.64c YPO0154(dam) YPO2750
            YPK: y1584 y3937(dam)
            YPM: YP_0156(dam) YP_2413(hemK2) YP_pMT105
            YPA: YPA_2093 YPA_3315 YPA_MT0084
            YPN: YPN_2196 YPN_3911 YPN_MT0088
            YPP: YPDSF_0081 YPDSF_2010
            YPS: YPTB0537 YPTB1797 YPTB1863(dam) YPTB2633 YPTB3747(dam)
                 YPTB3882(hsdM)
            YPI: YpsIP31758_3963(dam)
            YEN: YE1280 YE2361(dam)
            SFL: SF2407(yfcB) SF3300(yhdJ) SF3405(dam) SF4365
            SFX: S2542(yfcB) S3517(yhdJ) S4357(dam)
            SFV: SFV_2400(yfcB) SFV_3287(yhdJ) SFV_3392(dam) SFV_4366
            SSN: SSON_1899 SSON_2389(yfcB) SSON_3403(yhdJ) SSON_3518(dam)
            SBO: SBO_0751 SBO_1934 SBO_2368(yfcB) SBO_3256(yhdJ) SBO_3374(dam)
                 SBO_4159
            SDY: SDY_2530(yfcB) SDY_3692(dam)
            ECA: ECA2629 ECA3070 ECA3121(hsdM) ECA4090(dam)
            PLU: plu0087(dam) plu3190 plu4319(hsdM)
            WBR: WGLp409(yfcB)
            SGL: SG0472 SG1208 SG1566 SG1628 SG2306
            ENT: Ent638_2878 Ent638_3800
            KPN: KPN_02720(yfcB)
            SPE: Spro_3375 Spro_4602
            BFL: Bfl499(yfcB)
            BPN: BPEN_515(yfcB)
            HIN: HI0209(dam) HI0215(hsdM) HI0513(hindIIM) HI1201 HI1287(hsdM)
                 HI1392(hindIIIM)
            HIT: NTHI0188(hsdM1) NTHI0307(dam) NTHI0314(hsdM2) NTHI1372
                 NTHI1495 NTHI1838(hsdM3)
            HDU: HD0420(dam) HD1686
            HSO: HS_1115(dam) HS_1353
            PMU: PM0390 PM0698 PM1222(dam) PM1537(hsdM)
            MSU: MS1026 MS1265(hemK) MS1967(dam) MS2165(hsdM)
            APL: APL_0192(dam) APL_0633(hsdM3) APL_0705 APL_0813(mod) APL_0943
                 APL_1194
            ASU: Asuc_0262 Asuc_1340
            XFA: XF0641 XF1368 XF2297 XF2313 XF2723 XF2724 XF2728 XF2742
            XFT: PD0606(yfcB) PD1324 PD1339(dpnA) PD2072(hsdM) PD2076(hsdM)
            XCC: XCC0466 XCC2553(yfcB) XCC2902(hsdM) XCC2967
            XCB: XC_0480 XC_1207 XC_1565 XC_3183
            XCV: XCV0513(hsdM1) XCV1191(hsdM2) XCV2878 XCVd0131
            XAC: XAC2639 XAC2726(yfcB) XAC2900(hsdM)
            XOO: XOO3262(yfcB) XOO3457(hsdM-1) XOO3463(hsdM-2)
            XOM: XOO_1611(XOO1611) XOO_3090(XOO3090) XOO_3262(XOO3262)
                 XOO_3268(XOO3268)
            VCH: VC1769 VC2118 VC2626 VCA0447
            VCO: VC0395_A2203(dam)
            VVU: VV1_1385 VV1_1980 VV1_2031
            VVY: VV0266 VV0816 VV2202 VV2206 VV2208 VV2435 VV2986
            VPA: VP0388 VP0394 VP2203 VP2742
            VFI: VF1806 VF2289 VFA0535 VFA0537
            PPR: PBPRA0283(dam) PBPRA0882(hsdM) PBPRA0967(yfcB) PBPRA1803
            PAE: PA1678 PA2735
            PAU: PA14_42790
            PAP: PSPA7_6045
            PPU: PP_1827 PP_4741(hsdM)
            PST: PSPTO_0005 PSPTO_1086(hsdM) PSPTO_2040
            PSB: Psyr_1850(hemK)
            PSP: PSPPH_0107 PSPPH_1809
            PFL: PFL_2965(hsdM) PFL_4351
            PFO: Pfl_1719(hemK)
            PEN: PSEEN0753 PSEEN1525(prmB)
            PMY: Pmen_2739
            PAR: Psyc_0877(hsdM-1) Psyc_1456(hemK)
            PCR: Pcryo_0952 Pcryo_1359 Pcryo_1636
            PRW: PsycPRwf_0928
            ACI: ACIAD0248 ACIAD2029 ACIAD3432
            SON: SO_0289(dam) SO_0383(hsdM-1) SO_3080 SO_4265(hsdM-2)
            SDN: Sden_0264 Sden_1235 Sden_1536
            SFR: Sfri_0378 Sfri_1953 Sfri_2608 Sfri_2668
            SAZ: Sama_2160 Sama_3365
            SBL: Sbal_2753 Sbal_4110
            SBM: Shew185_2770 Shew185_4081
            SLO: Shew_0216 Shew_2417
            SPC: Sputcn32_2452 Sputcn32_3703
            SSE: Ssed_1637 Ssed_4262
            SPL: Spea_0241 Spea_2589
            SHE: Shewmr4_1415 Shewmr4_3695
            SHM: Shewmr7_0250 Shewmr7_1480 Shewmr7_2863
            SHN: Shewana3_0268 Shewana3_1468 Shewana3_2027 Shewana3_2961
                 Shewana3_3794 Shewana3_3891 Shewana3_4162 Shewana3_4240
            SHW: Sputw3181_1556 Sputw3181_3844
            ILO: IL0642(hsdM) IL0893 IL2475(dam)
            CPS: CPS_0475(dam) CPS_3151
            PHA: PSHAa0982(prmB) PSHAa1059(prmC) PSHAa2094(hsdM)
                 PSHAa2712(dam)
            PAT: Patl_0663 Patl_1540
            SDE: Sde_2092
            PIN: Ping_0166
            MAQ: Maqu_1569
            LPN: lpg0654(dam) lpg2075(dam) lpg2304
            LPF: lpl0690(dam) lpl2223
            LPP: lpp0708(dam) lpp2252
            MCA: MCA0278 MCA0701 MCA1888(hsdM)
            FTU: FTT1171c(hsdM) FTT1617(hemK)
            FTF: FTF1171c(hsdM) FTF1617(hemK)
            FTW: FTW_0300
            FTL: FTL_1684
            FTH: FTH_1623(hemK)
            FTA: FTA_1782
            FTN: FTN_0311 FTN_0704 FTN_1152 FTN_1491
            TCX: Tcr_0332 Tcr_1546
            NOC: Noc_0344 Noc_0393(hemK) Noc_0439 Noc_1201 Noc_1809 Noc_2687
                 Noc_2903 Noc_2928 Noc_2934(hemK)
            AEH: Mlg_0499 Mlg_0866
            HHA: Hhal_0822
            HCH: HCH_02420 HCH_05029(hsdM1) HCH_05730(hsdM2)
            CSA: Csal_0084 Csal_1368 Csal_1401 Csal_2467
            ABO: ABO_1474(yfcB) ABO_1830(hsdM)
            MMW: Mmwyl1_2243
            AHA: AHA_2356 AHA_3186
            DNO: DNO_0223(hsdM) DNO_1161(dam)
            BCI: BCI_0360(prmB)
            NME: NMB0727 NMB0829 NMB1655
            NMA: NMA0059 NMA0191 NMA1038 NMA1912
            NGO: NGO0008 NGO0702 NGO1300
            CVI: CV_0005 CV_2111 CV_2171
            RSO: RSc1388(RS04671) RSc1982(RS03556) RSc3396(RS01704)
            REU: Reut_A1896(hemK) Reut_A2305
            REH: H16_A2613
            RME: Rmet_1419 Rmet_2466 Rmet_5483
            BMA: BMA1569 BMA2674 BMAA1720
            BMV: BMASAVP1_1650
            BML: BMA10299_1859
            BMN: BMA10247_A0530(rsrIM)
            BXE: Bxe_A0224 Bxe_A1667 Bxe_B2880 Bxe_C0463
            BVI: Bcep1808_0038 Bcep1808_1939
            BUR: Bcep18194_A3213 Bcep18194_A3596(hemK) Bcep18194_A5342(hemK)
                 Bcep18194_B2124
            BCN: Bcen_0042 Bcen_4408 Bcen_6044
            BCH: Bcen2424_0028 Bcen2424_2033 Bcen2424_3959
            BAM: Bamb_0020 Bamb_1850 Bamb_2065 Bamb_3349
            BPS: BPSL0042 BPSL0948 BPSL2172 BPSS1698
            BPM: BURPS1710b_0259(mod) BURPS1710b_1697 BURPS1710b_2500
                 BURPS1710b_2597 BURPS1710b_A0768
            BPL: BURPS1106A_A2306(rsrIM)
            BPD: BURPS668_A2444(rsrIM)
            BTE: BTH_I0041 BTH_I2013 BTH_I2743 BTH_II0680 BTH_II1068
                 BTH_II1338
            PNU: Pnuc_1460
            BPE: BP1762
            BPA: BPP1993
            BBR: BB0912 BB2181 BB3607
            RFR: Rfer_0032 Rfer_1059 Rfer_1365 Rfer_1822 Rfer_2043 Rfer_4006
            POL: Bpro_1940 Bpro_1993 Bpro_3313 Bpro_3351 Bpro_3728
            PNA: Pnap_1809
            AAV: Aave_0159 Aave_2481
            AJS: Ajs_2070
            VEI: Veis_0278
            MPT: Mpe_A0005 Mpe_A1803 Mpe_A2383
            HAR: HEAR0697 HEAR1320 HEAR2198 HEAR3068
            MMS: mma_0578 mma_2073(hemK2)
            NEU: NE0385(hsdM) NE0436 NE2497(hsdM) NE2522 NE2524
            NET: Neut_0541 Neut_0593 Neut_1942 Neut_2448
            NMU: Nmul_A1854 Nmul_A2179
            EBA: ebA2607(hsdM) ebA6390 ebA670 p2A48(hsdS_2)
            AZO: azo0004(hsdM) azo2008
            DAR: Daro_1303 Daro_1723(hemK) Daro_3449
            TBD: Tbd_1270(hemK) Tbd_2680
            MFA: Mfla_1177 Mfla_1220 Mfla_1870 Mfla_2604 Mfla_2682
            HPY: HP0050(dpnA) HP0092(hsdM) HP0263(hpaim) HP0463(hsdM) HP0478
                 HP0481(MFOKI) HP0593(mod) HP0850(hsdM) HP0910 HP1208 HP1352
                 HP1367(mod) HP1403(hsdM) HP1472(mod) HP1517(ECO57IR)
            HPJ: jhp0043 jhp0085 jhp0248 jhp0415(hsdM_1) jhp0433
                 jhp0786(hsdM_2) jhp0846 jhp1131(M.HpyI) jhp1271 jhp1411(mod_2)
                 jhp1423(hsdM_3)
            HPA: HPAG1_0046 HPAG1_0093 HPAG1_0262 HPAG1_0265 HPAG1_0438
                 HPAG1_0455 HPAG1_0458 HPAG1_0833 HPAG1_0892 HPAG1_1149
                 HPAG1_1300 HPAG1_1328 HPAG1_1393 HPAG1_1395 HPAG1_1413
                 HPAG1_1414 HPAG1_1441 HPAG1_1442 HPAG1_1443 HPAG1_1464
                 HPAG1_1465
            HHE: HH0238 HH1038 HH1050 HH1091 HH1423
            HAC: Hac_0007(mod_fragment_1) Hac_0008(mod_fragment_2)
                 Hac_0011(ECO57IR_fragment_1) Hac_0012(ECO57IR_fragment_2)
                 Hac_0085(dpnA_fragment_3) Hac_0187(mod_fragment_2)
                 Hac_0306(hpyIM) Hac_0494 Hac_0520(hpaim) Hac_1075(MFOKI)
                 Hac_1111(hsdM) Hac_1297(HINDIIM) Hac_1348 Hac_1417(mod)
                 Hac_1512 Hac_1721(mod) Hac_1732(mod)
            WSU: WS1136(hsdM) WS1442(hsdM_2)
            TDN: Tmden_0130 Tmden_0697 Tmden_0942 Tmden_1355
            CJE: Cj0208 Cj1553c
            CJR: CJE0201 CJE0220(dam) CJE1724(hsdM)
            CJJ: CJJ81176_1539
            CJU: C8J_0197 C8J_1452(hsdM)
            CJD: JJD26997_1850(hsdM)
            CFF: CFF8240_0990(hsdM)
            CCV: CCV52592_1716
            CHA: CHAB381_0064 CHAB381_0065 CHAB381_0636 CHAB381_1065
            CCO: CCC13826_1412(hsdM)
            ABU: Abu_1650 Abu_1717(hsdM)
            NIS: NIS_1707
            GUR: Gura_4390
            PCA: Pcar_2925 Pcar_2927
            DVU: DVU1098 DVU1709(hsdM) DVU2733
            DDE: Dde_0922 Dde_1300 Dde_1743 Dde_1861 Dde_2498 Dde_2868
                 Dde_3427 Dde_3429
            LIP: LI0652
            BBA: Bd3696(hsdM)
            ADE: Adeh_2329 Adeh_2855
            SAT: SYN_00494 SYN_01825
            SFU: Sfum_1714 Sfum_3806
            RFE: RF_0123(dam) RF_p07
            RBE: RBE_0406 RBE_0415(dam2)
            ECN: Ecaj_0793
            PUB: SAR11_0109(babIM)
            MLO: mlr7520
            MES: Meso_0543 Meso_0763
            SME: SMc00021(ccrM) SMc02296(hsdM)
            SMD: Smed_5436
            ATU: Atu0794
            ATC: AGR_C_1453
            RET: RHE_CH00995(ccrM) RHE_CH01977
            RLE: RL1075 RL1098(hsdM2) RL1099(hsdM1) pRL110098(hsdM)
            BME: BMEI1444 BMEII0451
            BMF: BAB1_0516(babI) BAB2_0397(hsdM)
            BMS: BR0491(babI) BRA0840(hsdM)
            BMB: BruAb1_0513(babI) BruAb2_0391(hsdM)
            BOV: BOV_0495(babI) BOV_A0788(hsdM)
            BJA: bll2509(gst) bll5014 blr7474
            BRA: BRADO1375 BRADO2010 BRADO6060
            BBT: BBta_1723 BBta_2332 BBta_6611(rsrIM)
            RPA: RPA1026 RPA1167(yfcB)
            RPB: RPB_1073 RPB_1173 RPB_3056
            RPC: RPC_0905 RPC_4366
            RPD: RPD_1200 RPD_1277
            RPE: RPE_0561 RPE_0928 RPE_4431
            NWI: Nwi_0269 Nwi_0376(hemK) Nwi_0847 Nwi_1254 Nwi_1546
                 Nwi_2522(hemK) Nwi_2603
            NHA: Nham_3225
            BHE: BH04530(ccrM)
            BQU: BQ03720(ccrM)
            BBK: BARBAKC583_0413(ccrMIM)
            CCR: CC_0378 CC_0620
            SIL: SPO2733(hsdM) SPO3451
            SIT: TM1040_1587 TM1040_3541 TM1040_3551
            RSP: RSP_1468 RSP_1627 RSP_2052 RSP_3360 RSP_3635 RSP_3769
            RDE: RD1_0298(ccrM) RD1_2233 RD1_4053(hsdM)
            PDE: Pden_3838
            MMR: Mmar10_0161
            HNE: HNE_1901(ccrM) HNE_2542
            ZMO: ZMO0575(mboA) ZMO1005(babI)
            NAR: Saro_1840
            SAL: Sala_0965 Sala_2300
            SWI: Swit_3234
            ELI: ELI_02295
            GOX: GOX0344 GOX2569
            GBE: GbCGDNIH1_1859
            ACR: Acry_2422
            RRU: Rru_A0241 Rru_A0751 Rru_A3210
            MAG: amb1631 amb3988
            MGM: Mmc1_0129 Mmc1_0303 Mmc1_0787 Mmc1_1281
            ABA: Acid345_1093 Acid345_3396 Acid345_3758
            BHA: BH4004
            BCE: BC4459 BC4638
            BCA: BCE_0841 BCE_1018
            BCZ: BCZK4382
            BCY: Bcer98_3991
            BTK: BT9727_4372
            BTL: BALH_4216
            BLI: BL02330 BL02384
            BLD: BLi00744 BLi04318
            BCL: ABC2741
            BPU: BPUM_1394(ylbH) BPUM_1950
            GKA: GK0343 GK1380 GK2906
            SAU: SA0391(hsdM) SA1626
            SAV: SAV0431(hsdM) SAV1808
            SAM: MW0392(hsdM) MW1751(hsdM)
            SAR: SAR0433 SAR1899
            SAS: SAS0027 SAS0394 SAS1732
            SAC: SACOL0346 SACOL1862(hsdM2)
            SAB: SAB0384(hsdM) SAB1668c(hsdM)
            SAA: SAUSA300_0405(hsdM) SAUSA300_1752(hsdM)
            SAO: SAOUHSC_00397 SAOUHSC_01933
            SER: SERP2472(hsdM)
            SHA: SH0064(hsdM)
            SSP: SSP0053
            LIN: lin0522
            LWE: lwe0478(hsdM)
            LLA: L0309(hsdM)
            LLC: LACR_1215 LACR_2296
            LLM: llmg_0659(hsdM)
            SPY: SPy_1906(hsdM)
            SPZ: M5005_Spy_0093 M5005_Spy_1444 M5005_Spy_1623(hsdM)
            SPM: spyM18_1976(hsdM)
            SPG: SpyM3_1644(hsdM)
            SPS: SPs1644
            SPH: MGAS10270_Spy0095 MGAS10270_Spy0563 MGAS10270_Spy1691(hsdM)
            SPI: MGAS10750_Spy0100 MGAS10750_Spy0588
            SPJ: MGAS2096_Spy0096 MGAS2096_Spy0574 MGAS2096_Spy1124
                 MGAS2096_Spy1128 MGAS2096_Spy1470 MGAS2096_Spy1647(hsdM)
            SPK: MGAS9429_Spy0094 MGAS9429_Spy1446 MGAS9429_Spy1626(hsdM)
            SPF: SpyM51599
            SPA: M6_Spy0141 M6_Spy1144 M6_Spy1631
            SPB: M28_Spy0091 M28_Spy1612(hsdM)
            SPN: SP_0509 SP_0886 SP_1431
            SPR: spr0449(hsdM) spr0790(hsdM) spr1287(spnIM)
            SAK: SAK_1754(hsdM)
            SMU: SMU.504(dam) SMU.505 SMU.891(hsdM)
            STL: stu0711(hsdM1)
            SSA: SSA_1717(spnIM) SSA_1718(dam)
            SGO: SGO_0560(hsdM)
            LPL: lp_0939(hsdM)
            LSA: LSA0143 LSA0146 LSA1299
            LSL: LSL_0432
            LDB: Ldb1052(hsdM) Ldb1230(mod)
            LBR: LVIS_0044 LVIS_1191 LVIS_1622 LVIS_1625
            LCA: LSEI_1029 LSEI_2094
            STH: STH1435 STH1910 STH2525 STH334
            CAC: CAC3358 CAC3534
            CPF: CPF_0361 CPF_2599(hsdM)
            CPR: CPR_C0051
            CTC: CTC00387 CTC02250(bstV)
            CNO: NT01CX_1803 NT01CX_2408
            CTH: Cthe_1513 Cthe_2470
            CDF: CD2758
            CBO: CBO0678(hsdM)
            CHY: CHY_2213
            DSY: DSY0067 DSY0234 DSY1492 DSY4572
            SWO: Swol_0512 Swol_0838 Swol_1548 Swol_2258
            CSC: Csac_0634
            TTE: TTE1547(hsdM)
            MTA: Moth_1213 Moth_1672 Moth_1737
            MGE: MG_184
            MPN: MPN108(C09_orf404) MPN111(C09_orf422) MPN198(mte1)
                 MPN342(hsdM)
            MPU: MYPU_0810(hsdM) MYPU_0820(hsdM) MYPU_3960 MYPU_3970 MYPU_3980
                 MYPU_4330(hsdM) MYPU_4800 MYPU_6780(hsdM)
            MPE: MYPE1230(dam) MYPE1790(dam) MYPE8210(hsdM)
            MGA: MGA_0537(hsdM)
            MMY: MSC_0200(mod) MSC_0951(dam)
            MMO: MMOB2840(hsdM) MMOB2860(hsdM) MMOB3450(dam)
            MHY: mhp330(mod) mhp641
            MHJ: MHJ_0383 MHJ_0423 MHJ_0623(dam)
            MHP: MHP7448_0388 MHP7448_0622(dam)
            MSY: MS53_0161
            MCP: MCAP_0012 MCAP_0048 MCAP_0049(dam) MCAP_0182 MCAP_0297
            UUR: UU098(hsdM-1) UU100(hsdM-2)
            POY: PAM409(dam) PAM565(dam)
            AYW: AYWB_379(dam)
            MTU: Rv2756c
            MTC: MT2826(hsdM)
            MBO: Mb2777c(hsdM)
            MAV: MAV_5027
            MMC: Mmcs_0022
            CGL: NCgl0866(cgl0902)
            CGB: cg1028
            CEF: CE0048 CE0257 CE1493 CE2327
            CDI: DIP2314
            CJK: jk0526(modA) jk0897(hsdM1) jk1239(modB) jk1254(hsdM2)
            NFA: nfa27610(hsdM)
            RHA: RHA1_ro11151(hsdM)
            SCO: SCO6885(SC7F9.37)
            TWS: TW783
            LXX: Lxx01520(xbaIM)
            ART: Arth_2786
            AAU: AAur_2771
            NCA: Noca_3707
            FRA: Francci3_0192 Francci3_4014
            FAL: FRAAL0528 FRAAL3317(hsdM) FRAAL4992
            SEN: SACE_0871
            BLO: BL1782(hsdM)
            RXY: Rxyl_1835
            FNU: FN0416 FN1923 FN1935
            RBA: RB10768(hsdM) RB11379 RB11411(hsdM) RB11618 RB11642 RB12724
            TPA: TP0810(dam)
            TDE: TDE0099 TDE0369(hsdM-1) TDE0706 TDE2746(hsdM-2)
            LIL: LA2668 LA3197(hsdM)
            LIC: LIC10932
            LBJ: LBJ_0305(hsdM) LBJ_1937
            LBL: LBL_1347 LBL_2771(hsdM)
            SYN: sll0729 slr1803(mbpA)
            SYC: syc0488_c syc2303_c(mbpA)
            SYF: Synpcc7942_1060 Synpcc7942_1790
            CYA: CYA_0956
            CYB: CYB_2715
            TEL: tll2228 tlr1578 tlr1640 tlr1878
            GVI: glr2709
            ANA: all0061(dmtA) all2688 all2689 all4411(avaIIIM) alr0499
                 alr1152(dmtB) alr3475 alr3620 alr4597
            AVA: Ava_1159 Ava_1484 Ava_2663 Ava_3271 Ava_3498 Ava_4407
            PMA: Pro0708(hsdM)
            TER: Tery_3905
            BTH: BT_4518 BT_4538
            BFS: BF1077 BF1120 BF1458 BF1838(hsdM) BF3418
            SRU: SRU_1098
            CHU: CHU_2941 CHU_3354(hsdM)
            GFO: GFO_0677 GFO_2592
            FPS: FP2169
            CTE: CT0675(hsdM-1) CT0908(mod) CT1881(hsdM-2)
            CCH: Cag_0807 Cag_1120 Cag_1392 Cag_1402 Cag_1425(hemK) Cag_1525
            DET: DET1112
            DEH: cbdb_A104
            RRS: RoseRS_0124 RoseRS_0233
            RCA: Rcas_0884 Rcas_1080 Rcas_1425 Rcas_2228 Rcas_2236
            DGE: Dgeo_2017
            TTH: TTC0041
            TMA: TM0328
            TME: Tmel_0308
            MJA: MJ0132 MJ0598 MJ1220 MJ1328 MJ1498 MJECL42
            MMP: MMP0735
            MMQ: MmarC5_0847
            MMZ: MmarC7_1756
            MVN: Mevan_0154
            MAC: MA2116 MA2414(hsdM)
            MBA: Mbar_A1016 Mbar_A2666 Mbar_A3269
            MMA: MM_0156 MM_0193 MM_0429 MM_1669 MM_2198 MM_2294 MM_2704
                 MM_2740 MM_2981 MM_3147
            MBU: Mbur_0483 Mbur_1222 Mbur_1843
            MHU: Mhun_1945
            MEM: Memar_0517 Memar_1477
            MBN: Mboo_1003
            MTH: MTH942
            MST: Msp_0143 Msp_0479
            AFU: AF1715m
            HAL: VNG0106G(rmeM)
            TAC: Ta0644m Ta0829 Ta1168
            TVO: TVN0849
            PTO: PTO0078 PTO0585 PTO1076
            PHO: PH0584 PH1032
            PAB: PAB2149
            RCI: LRC82 RCIX1317(hsdM-2) RCIX973(hsdM-1)
STRUCTURES  PDB: 1AQI  1AQJ  1EG2  1G38  1G60  1NW5  1NW6  1NW7  1NW8  1Q0S  
                 1Q0T  1YF3  1YFJ  1YFL  2ADM  2AR0  2DPM  2G1P  2IBS  2IBT  
                 2JG3  2OKC  2ORE  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.72
            ExPASy - ENZYME nomenclature database: 2.1.1.72
            ExplorEnz - The Enzyme Database: 2.1.1.72
            ERGO genome analysis and discovery system: 2.1.1.72
            BRENDA, the Enzyme Database: 2.1.1.72
///
ENTRY       EC 2.1.1.73       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
COMMENT     Deleted entry: site-specific DNA-methyltransferase
            (cytosine-specific). Reaction is that of EC 2.1.1.37, DNA
            (cytosine-5-)-methyltransferase. (EC 2.1.1.73 created 1984, deleted
            2003)
STRUCTURES  PDB: 10MH  1DCT  1FJX  1M0E  1MHT  2HMY  2HR1  3MHT  4MHT  6MHT  
                 7MHT  8MHT  9MHT  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.73
            ExPASy - ENZYME nomenclature database: 2.1.1.73
            ExplorEnz - The Enzyme Database: 2.1.1.73
            ERGO genome analysis and discovery system: 2.1.1.73
            BRENDA, the Enzyme Database: 2.1.1.73
///
ENTRY       EC 2.1.1.74                 Enzyme
NAME        methylenetetrahydrofolate---tRNA-(uracil-5-)-methyltransferase
            (FADH2-oxidizing);
            folate-dependent ribothymidyl synthase;
            methylenetetrahydrofolate-transfer ribonucleate uracil
            5-methyltransferase;
            5,10-methylenetetrahydrofolate:tRNA-UPsiC
            (uracil-5-)-methyl-transferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     5,10-methylenetetrahydrofolate:tRNA (uracil-5-)-methyl-transferase
REACTION    5,10-methylenetetrahydrofolate + tRNA containing uridine at position
            54 + FADH2 = tetrahydrofolate + tRNA containing ribothymidine at
            position 54 + FAD [RN:R03704]
ALL_REAC    R03704
SUBSTRATE   5,10-methylenetetrahydrofolate [CPD:C00143];
            tRNA containing uridine at position 54;
            FADH2 [CPD:C01352]
PRODUCT     tetrahydrofolate [CPD:C00101];
            tRNA containing ribothymidine at position 54;
            FAD [CPD:C00016]
COMMENT     Up to 25% of the bases in mature tRNA are post-translationally
            modified or hypermodified. One almost universal post-translational
            modification is the conversion of U54 into ribothymidine in the
            TPsiC loop, and this modification is found in most species studied
            to date [2]. Unlike this enzyme, which uses
            5,10-methylenetetrahydrofolate and FADH2 to supply the atoms for
            methylation of U54, EC 2.1.1.35, RNA (uracil-5-)-methyltransferase,
            uses S-adenosyl-L-methionine.
REFERENCE   1  [PMID:6768721]
  AUTHORS   Delk AS, Nagle DP Jr, Rabinowitz JC.
  TITLE     Methylenetetrahydrofolate-dependent biosynthesis of ribothymidine in
            transfer RNA of Streptococcus faecalis. Evidence for reduction of
            the 1-carbon unit by FADH2.
  JOURNAL   J. Biol. Chem. 255 (1980) 4387-90.
  ORGANISM  Streptococcus faecalis
REFERENCE   2  [PMID:9417931]
  AUTHORS   Becker HF, Motorin Y, Sissler M, Florentz C, Grosjean H.
  TITLE     Major identity determinants for enzymatic formation of ribothymidine
            and pseudouridine in the T psi-loop of yeast tRNAs.
  JOURNAL   J. Mol. Biol. 274 (1997) 505-18.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.74
            ExPASy - ENZYME nomenclature database: 2.1.1.74
            ExplorEnz - The Enzyme Database: 2.1.1.74
            ERGO genome analysis and discovery system: 2.1.1.74
            BRENDA, the Enzyme Database: 2.1.1.74
            CAS: 74665-78-4
///
ENTRY       EC 2.1.1.75                 Enzyme
NAME        apigenin 4'-O-methyltransferase;
            flavonoid O-methyltransferase;
            flavonoid methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:5,7,4'-trihydroxyflavone
            4'-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 5,7,4'-trihydroxyflavone =
            S-adenosyl-L-homocysteine + 4'-methoxy-5,7-dihydroxyflavone
            [RN:R03571]
ALL_REAC    R03571
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            5,7,4'-trihydroxyflavone [CPD:C01477]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            4'-methoxy-5,7-dihydroxyflavone [CPD:C01470]
COMMENT     Converts apigenin into acacetin. Naringenin
            (5,7,4'-trihydroxy-flavanone) can also act as an acceptor, but more
            slowly.
REFERENCE   1
  AUTHORS   Kuroki, G. and Poulton, J.E.
  TITLE     The para-O-methylation of apigenin to acacetin by cell-free extracts
            of Robinia pseudoacacia L.
  JOURNAL   Z. Naturforsch. C: Biosci. 36 (1981) 916-920.
  ORGANISM  Robinia pseudoacacia
PATHWAY     PATH: map00941  Flavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.75
            ExPASy - ENZYME nomenclature database: 2.1.1.75
            ExplorEnz - The Enzyme Database: 2.1.1.75
            ERGO genome analysis and discovery system: 2.1.1.75
            BRENDA, the Enzyme Database: 2.1.1.75
            CAS: 118251-36-8
///
ENTRY       EC 2.1.1.76                 Enzyme
NAME        quercetin 3-O-methyltransferase;
            flavonol 3-O-methyltransferase;
            flavonoid 3-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:3,5,7,3',4'-pentahydroxyflavone
            3-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 3,5,7,3',4'-pentahydroxyflavone =
            S-adenosyl-L-homocysteine + 3-methoxy-5,7,3',4'-tetrahydroxyflavone
            [RN:R02157]
ALL_REAC    R02157;
            (other) R05035
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            3,5,7,3',4'-pentahydroxyflavone [CPD:C00389]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            3-methoxy-5,7,3',4'-tetrahydroxyflavone [CPD:C04443]
COMMENT     Specific for quercetin. Related enzymes bring about the
            3-O-methylation of other flavonols, such as galangin and kaempferol.
REFERENCE   1  [PMID:16526094]
  AUTHORS   Foucher AL, McIntosh A, Douce G, Wastling J, Tait A, Turner CM.
  TITLE     A proteomic analysis of arsenical drug resistance in Trypanosoma
            brucei.
  JOURNAL   Proteomics. 6 (2006) 2726-32.
REFERENCE   2  [PMID:3994393]
  AUTHORS   De Luca V, Ibrahim RK.
  TITLE     Enzymatic synthesis of polymethylated flavonols in Chrysosplenium
            americanum. I. Partial purification and some properties of
            S-adenosyl-L-methionine:flavonol 3-, 6-, 7-, and
            4'-O-methyltransferases.
  JOURNAL   Arch. Biochem. Biophys. 238 (1985) 596-605.
  ORGANISM  Chrysosplenium americanum
REFERENCE   3  [PMID:3994394]
  AUTHORS   De Luca V, Ibrahim RK.
  TITLE     Enzymatic synthesis of polymethylated flavonols in Chrysosplenium
            americanum. II. Substrate interaction and product inhibition studies
            of flavonol 3-, 6-, and 4'-O-methyltransferases.
  JOURNAL   Arch. Biochem. Biophys. 238 (1985) 606-18.
  ORGANISM  Chrysosplenium americanum
REFERENCE   4
  AUTHORS   Ibrahim, R.K. and De Luca, V.
  TITLE     Polymethylated flavonol synthesis is catalyzed by distinct
            O-methyltransferases.
  JOURNAL   Naturwissenschaften 69 (1982) 41-42.
  ORGANISM  Chrysosplenium americanum
PATHWAY     PATH: map00941  Flavonoid biosynthesis
ORTHOLOGY   KO: K05279  flavonol 3-O-methyltransferase
GENES       ATH: AT5G54160(ATOMT1)
            OSA: 4344702
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.76
            ExPASy - ENZYME nomenclature database: 2.1.1.76
            ExplorEnz - The Enzyme Database: 2.1.1.76
            ERGO genome analysis and discovery system: 2.1.1.76
            BRENDA, the Enzyme Database: 2.1.1.76
            CAS: 75603-21-3
///
ENTRY       EC 2.1.1.77                 Enzyme
NAME        protein-L-isoaspartate(D-aspartate) O-methyltransferase;
            protein-L-isoaspartate O-methyltransferase;
            protein-beta-aspartate O-methyltransferase;
            D-aspartyl/L-isoaspartyl methyltransferase;
            L-isoaspartyl/D-aspartyl protein carboxyl methyltransferase;
            protein (D-aspartate) methyltransferase;
            protein D-aspartate methyltransferase;
            protein L-isoaspartate methyltransferase;
            protein L-isoaspartyl methyltransferase;
            protein O-methyltransferase (L-isoaspartate);
            L-aspartyl/L-isoaspartyl protein methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:protein-L-isoaspartate O-methyltransferase
REACTION    S-adenosyl-L-methionine + protein L-isoaspartate =
            S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl
            ester [RN:R04190]
ALL_REAC    R04190
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            protein L-isoaspartate [CPD:C03306]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            protein L-isoaspartate alpha-methyl ester [CPD:C04311]
COMMENT     D-Aspartate (but not L-aspartate) residues in proteins can also act
            as acceptors. Previously also listed as EC 2.1.1.24.
REFERENCE   1
  AUTHORS   Aswad, D.W. and Johnson, B.A.
  TITLE     The unusual substrate-specificity of eukaryotic protein carboxyl
            methyltransferases.
  JOURNAL   Trends Biochem. Sci. 12 (1987) 155-158.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:3896126]
  AUTHORS   Clarke S.
  TITLE     Protein carboxyl methyltransferases: two distinct classes of
            enzymes.
  JOURNAL   Annu. Rev. Biochem. 54 (1985) 479-506.
REFERENCE   3  [PMID:5438363]
  AUTHORS   Kim S, Paik WK.
  TITLE     Purification and properties of protein methylaase II.
  JOURNAL   J. Biol. Chem. 245 (1970) 1806-13.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:3597386]
  AUTHORS   Ota IM, Ding L, Clarke S.
  TITLE     Methylation at specific altered aspartyl and asparaginyl residues in
            glucagon by the erythrocyte protein carboxyl methyltransferase.
  JOURNAL   J. Biol. Chem. 262 (1987) 8522-31.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K00573  protein-L-isoaspartate(D-aspartate) O-methyltransferase
GENES       HSA: 5110(PCMT1)
            PTR: 463062(PCMT1)
            MMU: 18537(Pcmt1)
            RNO: 25604(Pcmt1)
            CFA: 476242(PCMT1)
            BTA: 613854(PCMT1)
            GGA: 423008(LOC423008) 428607(RCJMB04_11o11)
            XLA: 380580(pcmt1) 495685(LOC495685)
            DRE: 30751(pcmt)
            SPU: 581433(LOC581433)
            DME: Dmel_CG2152(Pcmt)
            CEL: C10F3.5(pcm-1)
            ATH: AT5G50240(PIMT2)
            OSA: 4336186 4346293
            CME: CMI267C
            SPO: SPAC869.08
            ANI: AN3464.2
            AFM: AFUA_3G05390
            AOR: AO090020000009
            CNE: CNB03250
            DDI: DDB_0214947(pcmA)
            PFA: PF14_0309
            TET: TTHERM_00086830 TTHERM_00283890
            TBR: Tb10.6k15.2720
            TCR: 503779.40 506247.410
            LMA: LmjF36.6550
            ECO: b2743(pcm)
            ECJ: JW2713(pcm)
            ECE: Z4051(pcm)
            ECS: ECs3597
            ECC: c3310(pcm)
            ECI: UTI89_C3114(pcm)
            ECP: ECP_2724 ECP_2725
            ECV: APECO1_3780(pcm)
            ECW: EcE24377A_3044(pcm)
            ECX: EcHS_A2881
            STY: STY3051(pcm)
            STT: t2827(pcm)
            SPT: SPA2782(pcm)
            SEC: SC2858(pcm)
            STM: STM2926(pcm)
            YPE: YPO3357(pcm)
            YPK: y0832(pcm)
            YPM: YP_0330(pcm)
            YPA: YPA_2786
            YPN: YPN_0736
            YPP: YPDSF_3003
            YPS: YPTB0774(pcm)
            YPI: YpsIP31758_3295(pcm)
            YEN: YE0773(pcm)
            SFL: SF2766(pcm)
            SFX: S2959(pcm)
            SFV: SFV_2755(pcm)
            SSN: SSON_2891(pcm)
            SBO: SBO_2777(pcm)
            SDY: SDY_2942(pcm)
            ECA: ECA3532(pcm)
            PLU: plu0717(pcm)
            SGL: SG0529
            ENT: Ent638_3214
            SPE: Spro_0830
            XFA: XF0857 XF2585
            XFT: PD1818(pcm) PD1963(pcm)
            XCC: XCC1707(pcm) XCC3335(pcm)
            XCB: XC_0829 XC_2524
            XCV: XCV1759 XCV3590(pcm)
            XAC: XAC1726(pcm) XAC3462(pcm)
            XOO: XOO0928(pcm) XOO2955(pcm)
            XOM: XOO_0852(XOO0852) XOO_2807(XOO2807)
            VCH: VC0532
            VCO: VC0395_A0060(pcm)
            VVU: VV1_1586
            VVY: VV2811
            VPA: VP2555
            VFI: VF2069
            PPR: PBPRA3073(pcm)
            PAE: PA3624(pcm)
            PAU: PA14_17460(pcm)
            PAP: PSPA7_1515(pcm)
            PPU: PP_1621(pcm)
            PPF: Pput_4156
            PST: PSPTO_1563(pcm)
            PSB: Psyr_1372(pcm)
            PSP: PSPPH_3811(pcm)
            PFL: PFL_1205(pcm)
            PFO: Pfl_1130
            PEN: PSEEN4191(pcm)
            PMY: Pmen_3023
            SON: SO_3434(pcm)
            SDN: Sden_1202
            SFR: Sfri_1058
            SAZ: Sama_1042
            SBL: Sbal_3121
            SBM: Shew185_3130
            SLO: Shew_1211
            SPC: Sputcn32_2751
            SSE: Ssed_1296 Ssed_2790
            SPL: Spea_1191
            SHE: Shewmr4_1121
            SHM: Shewmr7_1192
            SHN: Shewana3_1122
            SHW: Sputw3181_1261
            ILO: IL0748(pcm)
            CPS: CPS_1076(pcm)
            PHA: PSHAa0688(pcm)
            PAT: Patl_3861
            SDE: Sde_1250
            MAQ: Maqu_0927 Maqu_2892
            LPN: lpg0700(pcm)
            LPF: lpl0737(pcm)
            LPP: lpp0755(pcm)
            MCA: MCA1211(pcm-1) MCA2419(pcm-2) MCA2831(pcm-3)
            FTU: FTT1725c(pcm)
            FTF: FTF1725c(pcm)
            FTW: FTW_0073
            FTL: FTL_1866
            FTH: FTH_1794(pcm)
            FTN: FTN_1704(pcm)
            TCX: Tcr_1069 Tcr_1256 Tcr_1671
            NOC: Noc_0790 Noc_1546 Noc_2617
            AEH: Mlg_1828 Mlg_2640
            HHA: Hhal_1430 Hhal_2315
            HCH: HCH_01874(pcm)
            CSA: Csal_2634
            ABO: ABO_1169(pcm)
            MMW: Mmwyl1_1305
            AHA: AHA_0827(pcm)
            RMA: Rmag_0964
            VOK: COSY_0865(pcm)
            NME: NMB1885
            NMA: NMA0572
            NMC: NMC0336
            NGO: NGO0019
            CVI: CV_0234(pcm2) CV_3680(pcm1)
            RSO: RSc0697(pcm) RSc1205(RS02685)
            REU: Reut_A0751 Reut_A2097
            REH: H16_A1622 H16_A2375 H16_A2877(pcm)
            RME: Rmet_2117 Rmet_2709
            BMA: BMA1356(pcm) BMA2173
            BMV: BMASAVP1_A0736 BMASAVP1_A1846(pcm)
            BML: BMA10299_A0051(pcm) BMA10299_A2569
            BMN: BMA10247_1118(pcm) BMA10247_2044
            BXE: Bxe_A2352 Bxe_A3677 Bxe_C1354
            BVI: Bcep1808_0843 Bcep1808_1749
            BUR: Bcep18194_A4016 Bcep18194_A5123
            BCN: Bcen_0433 Bcen_6257
            BCH: Bcen2424_0912 Bcen2424_1822
            BAM: Bamb_0789 Bamb_1760
            BPS: BPSL1503 BPSL2648(pcm)
            BPM: BURPS1710b_2367(pcm) BURPS1710b_3124(pcm)
            BPL: BURPS1106A_2238(pcm) BURPS1106A_3099
            BPD: BURPS668_2200(pcm) BURPS668_3063
            BTE: BTH_I1507 BTH_I2224
            PNU: Pnuc_1298
            BPE: BP1720(pcm) BP3599
            BPA: BPP3056(pcm) BPP3988
            BBR: BB3019(pcm) BB4461
            RFR: Rfer_2602 Rfer_2781
            POL: Bpro_1666 Bpro_2641 Bpro_3060 Bpro_4278
            PNA: Pnap_1128 Pnap_2578
            AAV: Aave_1415 Aave_2816
            AJS: Ajs_1161 Ajs_2028
            VEI: Veis_0089
            MPT: Mpe_A1042 Mpe_A1253
            HAR: HEAR1255 HEAR2708
            MMS: mma_2932
            NEU: NE0037(pcm) NE0949
            NET: Neut_0197 Neut_2323
            NMU: Nmul_A0151 Nmul_A0496 Nmul_A2284
            EBA: ebA1645(pcm) ebA781(pcm1)
            AZO: azo0848(pcm1) azo1088(pcm2)
            DAR: Daro_2523 Daro_3924
            TBD: Tbd_0836 Tbd_2695
            MFA: Mfla_1825 Mfla_2531
            HPY: HP0363(pcm)
            HPJ: jhp1017(pcm)
            HPA: HPAG1_1030
            HHE: HH0604(pcm)
            HAC: Hac_0412(pcm)
            WSU: WS0418
            TDN: Tmden_0015
            CJE: Cj0228c(pcm)
            CJR: CJE0279(pcm)
            CJJ: CJJ81176_0253(pcm)
            CJU: C8J_0206(pcm)
            CJD: JJD26997_0226(pcm)
            CFF: CFF8240_0031(pcm)
            CCV: CCV52592_2087(pcm) CCV52592_2091(pcm)
            CHA: CHAB381_0196(pcm)
            CCO: CCC13826_0294(pcm) CCC13826_0733(pcm)
            NIS: NIS_0045(pcm)
            SUN: SUN_0978 SUN_2400(pcm)
            GSU: GSU1524(pcM)
            GME: Gmet_1420
            GUR: Gura_1616 Gura_2618 Gura_3331
            PCA: Pcar_1427
            PPD: Ppro_2738 Ppro_2838
            DVU: DVU1849(pcm)
            DVL: Dvul_1313
            DDE: Dde_2077
            LIP: LI0375(pcm)
            BBA: Bd2618(pcm)
            DPS: DP0275
            ADE: Adeh_1726
            AFW: Anae109_2075 Anae109_4121
            MXA: MXAN_3407(pcm)
            SAT: SYN_01000
            SFU: Sfum_2181 Sfum_2480 Sfum_2864
            PUB: SAR11_0528(smtA)
            MLO: mll1078 mll1108 mll2628
            MES: Meso_1568 Meso_1801
            PLA: Plav_3032
            SME: SMa1547 SMc02062(pcm) SMc02083
            SMD: Smed_1169 Smed_4048
            ATU: Atu1701(pcm) Atu1721(pcm)
            ATC: AGR_C_3127 AGR_C_3159
            RET: RHE_CH01809(pcm1) RHE_CH01828(pcm2) RHE_PB00041(ypb00021)
            RLE: RL2033 RL2051(pcm) pRL120378
            BME: BMEI1030 BMEI1080
            BMF: BAB1_0906 BAB1_0962
            BMS: BR0887 BR0944
            BMB: BruAb1_0899 BruAb1_0953
            OAN: Oant_2340 Oant_4285
            BJA: bll474(pcm) bll5351 blr4472(pcm)
            BRA: BRADO3885 BRADO4040(pcm) BRADO6231
            BBT: BBta_3944 BBta_4410(pcm) BBta_4958 BBta_6647
            RPA: RPA0376(pimt1) RPA2580 RPA2838(pimt2)
            RPB: RPB_0447 RPB_2737 RPB_2895
            RPC: RPC_2521 RPC_2567
            RPD: RPD_2576 RPD_2782
            RPE: RPE_2196 RPE_2705 RPE_2747
            NWI: Nwi_1773 Nwi_1780
            NHA: Nham_1787 Nham_1794 Nham_1929
            BHE: BH05620(pcm1) BH10660(pcm2)
            BQU: BQ04780(pcm1) BQ08380(pcm2)
            XAU: Xaut_4234 Xaut_4414
            CCR: CC_1997
            SIL: SPO1239(pcm-1) SPO2687(pcm-2)
            SIT: TM1040_1792 TM1040_1992
            RSP: RSP_0252 RSP_2544
            RSH: Rsph17029_1204 Rsph17029_1895
            RSQ: Rsph17025_1978 Rsph17025_2025
            JAN: Jann_1067 Jann_3258
            RDE: RD1_1741(pcm) RD1_3250(pcm)
            PDE: Pden_2730
            MMR: Mmar10_1002 Mmar10_1903
            HNE: HNE_1679 HNE_1928(pcm)
            NAR: Saro_0187
            ELI: ELI_12910
            GBE: GbCGDNIH1_0514 GbCGDNIH1_0931
            RRU: Rru_A1768 Rru_A1799
            MAG: amb2244 amb2519
            MGM: Mmc1_0372 Mmc1_0964
            ABA: Acid345_2473
            SUS: Acid_7349
            PTH: PTH_2678(pcm)
            SWO: Swol_2438
            CGB: cg1692(pimT)
            CJK: jk0949
            SCO: SCO6928(SC1B2.34c)
            TWH: TWT318
            NCA: Noca_4541
            FRA: Francci3_1128 Francci3_1819 Francci3_2034 Francci3_3316
                 Francci3_4467
            FAL: FRAAL2698(pcm) FRAAL2702 FRAAL2867
            RXY: Rxyl_1185
            RBA: RB12080
            PCU: pc0856(pcm)
            LIL: LA1131
            LIC: LIC12550(pcm)
            LBJ: LBJ_2677
            LBL: LBL_0403
            CYA: CYA_0908(pcm)
            CYB: CYB_2184(pcm)
            GVI: glr1699
            AVA: Ava_2940
            SRU: SRU_1945(pcm)
            CHU: CHU_1928(pcm)
            GFO: GFO_0668(pcm)
            FJO: Fjoh_3446
            FPS: FP1909(pcm)
            CTE: CT0202(pcm)
            CPH: Cpha266_0339
            PVI: Cvib_1573
            PLT: Plut_1923
            RRS: RoseRS_3811
            RCA: Rcas_0989
            TMA: TM0704
            TPT: Tpet_0226
            TME: Tmel_1682
            FNO: Fnod_0742
            MJA: MJ0172(pcm)
            MMP: MMP0102(pcm)
            MMQ: MmarC5_1574
            MMZ: MmarC7_1101
            MAE: Maeo_1317
            MVN: Mevan_1112
            MAC: MA0543(pcm-2) MA0544(pcm-1)
            MBA: Mbar_A1517
            MMA: MM_1706
            MBU: Mbur_1894
            MTP: Mthe_1699
            MHU: Mhun_2850
            MEM: Memar_2225
            MBN: Mboo_0258
            MKA: MK0282(pcm)
            AFU: AF2322(pcm-2)
            HAL: VNG0089G(pimT1)
            HMA: rrnAC0215(pimT) rrnAC0962(pcm3) rrnAC2256(pcm2)
                 rrnAC2258(pcm1)
            HWA: HQ1357A(pimT)
            NPH: NP0018A(pimT_1) NP0020A(pimT_2)
            TVO: TVN0955
            PHO: PH1886
            PAB: PAB1206(pcm)
            PFU: PF1922
            TKO: TK0051 TK1328
            RCI: RCIX2158(pcm)
            APE: APE_1011.1
            SMR: Smar_0720
            IHO: Igni_0877
            HBU: Hbut_0632
            SSO: SSO2599(pcm)
            STO: ST0182 ST1123
            SAI: Saci_0434
            MSE: Msed_2163
            PAI: PAE0701(pcmT)
            PIS: Pisl_0680
            PCL: Pcal_2118
            PAS: Pars_2349
            NEQ: NEQ337
STRUCTURES  PDB: 1DL5  1I1N  1JG1  1JG2  1JG3  1JG4  1KR5  1R18  1VBF  2PBF  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.77
            ExPASy - ENZYME nomenclature database: 2.1.1.77
            ExplorEnz - The Enzyme Database: 2.1.1.77
            ERGO genome analysis and discovery system: 2.1.1.77
            BRENDA, the Enzyme Database: 2.1.1.77
            CAS: 105638-50-4
///
ENTRY       EC 2.1.1.78                 Enzyme
NAME        isoorientin 3'-O-methyltransferase;
            isoorientin 3'-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:isoorientin 3'-O-methyltransferase
REACTION    S-adenosyl-L-methionine + isoorientin = S-adenosyl-L-homocysteine +
            isoscoparin [RN:R03731]
ALL_REAC    R03731
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            isoorientin [CPD:C01821]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            isoscoparin [CPD:C05990]
COMMENT     Also acts on isoorientin 2"-O-rhamnoside. Involved in the
            biosynthesis of flavones.
REFERENCE   1  [PMID:16525953]
  AUTHORS   Hildebrand F, van Griensven M, Giannoudis P, Schreiber T, Frink M,
            Probst C, Grotz M, Krettek C, Pape HC.
  TITLE     Impact of hypothermia on the immunologic response after trauma and
            elective surgery.
  JOURNAL   Surg. Technol. Int. 14 (2005) 41-50.
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.78
            ExPASy - ENZYME nomenclature database: 2.1.1.78
            ExplorEnz - The Enzyme Database: 2.1.1.78
            ERGO genome analysis and discovery system: 2.1.1.78
            BRENDA, the Enzyme Database: 2.1.1.78
            CAS: 83061-51-2
///
ENTRY       EC 2.1.1.79                 Enzyme
NAME        cyclopropane-fatty-acyl-phospholipid synthase;
            cyclopropane synthetase;
            unsaturated-phospholipid methyltransferase;
            cyclopropane synthase;
            cyclopropane fatty acid synthase;
            cyclopropane fatty acid synthetase;
            CFA synthase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:unsaturated-phospholipid methyltransferase
            (cyclizing)
REACTION    S-adenosyl-L-methionine + phospholipid olefinic fatty acid =
            S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
            [RN:R03411]
ALL_REAC    R03411
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            phospholipid olefinic fatty acid [CPD:C01229]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            phospholipid cyclopropane fatty acid [CPD:C04340]
COMMENT     The enzyme adds a methylene group across the 9,10 position of a
            Delta9-olefinic acyl chain in phosphatidylethanolamine or, more
            slowly, phosphatidylglycerol or phosphatidylinositol, forming a
            cyclopropane derivative (cf. EC 2.1.1.16
            methylene-fatty-acyl-phospholipid synthase).
REFERENCE   1
  AUTHORS   Chung, A.E. and Law, J.H.
  TITLE     Cyclopropane fatty acid synthetase: Partial purification and
            properties.
  JOURNAL   Biochemistry 3 (1964) 967-974.
  ORGANISM  Clostridium butyricum
REFERENCE   2
  AUTHORS   Zalkin, H., Law, J.H. and Goldfine, H.
  TITLE     Enzymatic synthesis of cyclopropane fatty acids catalyzed by
            bacterial extracts.
  JOURNAL   J. Biol. Chem. 238 (1963) 1242-1248.
  ORGANISM  Clostridium butyricum, Escherichia coli [GN:eco], Serratia
            marcescens
ORTHOLOGY   KO: K00574  cyclopropane-fatty-acyl-phospholipid synthase
GENES       ATH: AT3G23510
            OSA: 4343210
            ANI: AN7375.2
            AFM: AFUA_7G04190
            AOR: AO090012000713
            UMA: UM00846.1
            DDI: DDBDRAFT_0185725
            ECO: b1661(cfa)
            ECJ: JW1653(cfa)
            ECE: Z2686(cfa)
            ECS: ECs2370
            ECC: c2055(cfa)
            ECI: UTI89_C1852(cfa)
            ECP: ECP_1608
            ECW: EcE24377A_1875(cfa)
            ECX: EcHS_A1741(cfa)
            STY: STY1695(cfa)
            STT: t1295(cfa)
            SPT: SPA1426(cfa)
            SEC: SC1446(cfa)
            STM: STM1427(cfa)
            YPE: YPO2390(cfa)
            YPK: y1947(cfa)
            YPM: YP_2176(cfa)
            YPA: YPA_1735
            YPN: YPN_1844
            YPP: YPDSF_0757
            YPS: YPTB2303(cfa)
            YPI: YpsIP31758_1752(cfa)
            SFL: SF1689(cfa)
            SFX: S1821(cfa)
            SFV: SFV_1683(cfa)
            SSN: SSON_1495(cfa)
            SBO: SBO_1470(cfa)
            SDY: SDY_1887(cfa)
            ECA: ECA1924(cfa) ECA2212
            PLU: plu2608(cfa)
            ENT: Ent638_1487 Ent638_1786
            SPE: Spro_1154 Spro_2192
            XCC: XCC1326 XCC1329(cfaA)
            XCB: XC_2910 XC_2913
            XCV: XCV1428(cfa) XCV1431(cfa)
            XAC: XAC1372 XAC1375(cfaA)
            XOO: XOO1911 XOO1914(cfaA)
            XOM: XOO_1809(XOO1809) XOO_1812(XOO1812)
            VCH: VC1122
            VCO: VC0395_A0640(cfa)
            VVU: VV1_2932
            VVY: VV1337
            VPA: VP1123
            VFI: VFA0760
            PPR: PBPRB1573
            PAE: PA5546
            PAU: PA14_73140
            PPU: PP_2734(cfa) PP_5365
            PPF: Pput_3019 Pput_5273
            PST: PSPTO_1116(cfa)
            PSB: Psyr_0956 Psyr_5080
            PSP: PSPPH_1005(cfa1) PSPPH_5162(cfa2)
            PFL: PFL_5152 PFL_6187
            PFO: Pfl_4741 Pfl_5666
            PEN: PSEEN2702 PSEEN5518 PSEEN5532
            PMY: Pmen_1066
            PAR: Psyc_0741(cfa)
            PCR: Pcryo_0730
            PRW: PsycPRwf_1177
            ACI: ACIAD1630(cfa)
            SON: SO_3379(cfa)
            SDN: Sden_3368
            SFR: Sfri_3031
            SAZ: Sama_0816
            SBL: Sbal_3049
            SBM: Shew185_3063
            SLO: Shew_1484
            SPC: Sputcn32_2709
            SHE: Shewmr4_1170
            SHM: Shewmr7_1241
            SHN: Shewana3_1171
            SHW: Sputw3181_1303
            ILO: IL1383 IL2166(cfa)
            CPS: CPS_1385(cfa)
            PHA: PSHAb0458
            PAT: Patl_1326
            SDE: Sde_2466
            PIN: Ping_1003
            MAQ: Maqu_1487 Maqu_3480
            LPN: lpg1131(cfa)
            LPF: lpl1137(cfa)
            LPP: lpp1133(cfa)
            MCA: MCA2223(cfa)
            FTL: FTL_0561
            FTH: FTH_0562(cfa)
            FTN: FTN_1456(cfa)
            AEH: Mlg_0317 Mlg_2254
            HHA: Hhal_0913 Hhal_1504
            HCH: HCH_00338 HCH_00340(cfa)
            CSA: Csal_0460 Csal_1480
            ABO: ABO_0769(cfa) ABO_0828
            MMW: Mmwyl1_4070
            AHA: AHA_1106
            CVI: CV_0978(cfa) CV_3226(CFA)
            RSO: RS02216(RSp1657) RSc0766(cfa2) RSp1446(cfa1)
            REU: Reut_A0814 Reut_C6098
            REH: H16_A2803
            RME: Rmet_2643
            BMA: BMA0358
            BMV: BMASAVP1_A0658(cfa)
            BMN: BMA10247_0106(cfa)
            BXE: Bxe_A0740 Bxe_A3431 Bxe_B0199
            BVI: Bcep1808_2663 Bcep1808_5905
            BUR: Bcep18194_A5901 Bcep18194_C6581 Bcep18194_C6585
            BCN: Bcen_1958
            BCH: Bcen2424_2569
            BAM: Bamb_2617
            BPS: BPSL0853 BPSS2039
            BPM: BURPS1710b_1060(cfa2) BURPS1710b_A1158
            BPL: BURPS1106A_0903(cfa) BURPS1106A_A1480
            BPD: BURPS668_0900(cfa) BURPS668_A1568
            BTE: BTH_I0716 BTH_II0279
            PNU: Pnuc_1973
            BPA: BPP1739
            BBR: BB3369
            RFR: Rfer_0826 Rfer_2417
            POL: Bpro_3190 Bpro_5326
            PNA: Pnap_1175 Pnap_1451
            AAV: Aave_0777 Aave_3573
            AJS: Ajs_0460 Ajs_1494 Ajs_2676 Ajs_2969
            VEI: Veis_0493
            MPT: Mpe_A0234 Mpe_A0333
            HAR: HEAR0447(cfa) HEAR2259 HEAR2423
            MMS: mma_0525(cfa1)
            EBA: ebA4362(cfa)
            AZO: azo0956(cfa1) azo3311(cfaA)
            DAR: Daro_0492
            TBD: Tbd_1047 Tbd_1109
            MFA: Mfla_1678
            HPY: HP0416(cfa)
            HPA: HPAG1_0978
            HAC: Hac_0604(cfa)
            CJE: Cj1183c(cfa)
            CJR: CJE1317
            CJU: C8J_1127
            ABU: Abu_1204(cfa)
            GSU: GSU2329(cfa)
            GME: Gmet_2187
            GUR: Gura_1633
            PPD: Ppro_0127
            DPS: DP2150
            ADE: Adeh_2228
            SAT: SYN_01675
            SFU: Sfum_1333
            PUB: SAR11_0092(cdfA) SAR11_0530 SAR11_0672 SAR11_1144(cfa)
            MLO: mll0368 mll4091 mll7842
            MES: Meso_0988 Meso_3871
            PLA: Plav_2992
            SME: SMc00358(cfa1) SMc02645(cfa2)
            SMD: Smed_3479
            ATU: Atu0649(cfa) Atu1979
            ATC: AGR_C_1155 AGR_C_3601
            RET: RHE_CH00892(cfa)
            RLE: RL0953(cfa) RL1982(cfa) pRL120574
            BME: BMEI1484
            BMF: BAB1_0476(cfa)
            BMS: BR0451(cfa)
            BMB: BruAb1_0473(cfa)
            BOV: BOV_0457(cfa)
            OAN: Oant_3080
            BJA: blr1512
            BRA: BRADO1113 BRADO3304 BRADO3908
            BBT: BBta_3810 BBta_3928 BBta_6936
            RPA: RPA2569(cfa1) RPA3082(cfa2)
            RPB: RPB_2906
            RPC: RPC_2291 RPC_2554
            RPD: RPD_2565
            RPE: RPE_0658 RPE_2735
            NWI: Nwi_2012
            NHA: Nham_2287
            XAU: Xaut_3122 Xaut_4728
            CCR: CC_1427
            SIL: SPO1483 SPO1918(cfa)
            SIT: TM1040_0412
            RSP: RSP_2144(cfaS)
            RSH: Rsph17029_0818
            RSQ: Rsph17025_0816
            JAN: Jann_1990
            RDE: RD1_2296(cfa)
            PDE: Pden_2392
            MMR: Mmar10_0271
            HNE: HNE_1795
            ZMO: ZMO1033(cfa)
            NAR: Saro_1760 Saro_2592
            SAL: Sala_0492 Sala_1545
            SWI: Swit_0580 Swit_2964
            ELI: ELI_07035 ELI_07845
            GOX: GOX0303
            GBE: GbCGDNIH1_1403
            ACR: Acry_3143
            RRU: Rru_A0725 Rru_A1910
            BAN: BA3460(cfa)
            BAR: GBAA3460(cfa)
            BAA: BA_3957
            BAT: BAS3207
            BCE: BC3407
            BCZ: BCZK0295(cfa) BCZK3113(cfa)
            BCY: Bcer98_0301
            BTK: BT9727_3185(cfa)
            LLC: LACR_2162
            LLM: llmg_2161(cfa)
            SAG: SAG1748(cfa)
            SAN: gbs1792
            SAK: SAK_1771(cfa)
            STC: str0128(cfa)
            STL: stu0128(cfa)
            STE: STER_0187
            LPL: lp_1696(cfa1) lp_3174(cfa2)
            LJO: LJ1503
            LAC: LBA1274
            LSA: LSA0045(cfa)
            LSL: LSL_0949(cfa)
            LDB: Ldb1461(cfa)
            LBU: LBUL_1356
            LBR: LVIS_0719 LVIS_2047
            LCA: LSEI_2108
            LGA: LGAS_0798
            LRE: Lreu_0129
            PPE: PEPE_1712
            EFA: EF0203(cfa)
            OOE: OEOE_1176
            LME: LEUM_0790
            CAC: CAC0877(cfa)
            CPE: CPE1051(cfa)
            CPF: CPF_1307(cfa)
            CPR: CPR_1123(cfa)
            CTC: CTC01889
            CNO: NT01CX_2333
            CDF: CD0177
            CBO: CBO0616
            CBA: CLB_0656(cfa)
            CBH: CLC_0671(cfa)
            CBF: CLI_0696(cfa)
            CBE: Cbei_4121 Cbei_5003
            MTU: Rv0447c(ufaA1) Rv0503c(cmaA2) Rv0645c(mmaA1) Rv3392c(cmaA1)
            MTC: MT0463(cfa-1) MT0486(cmaC) MT0524(cma2) MT0670(mma4)
                 MT0671(mma3) MT0672(mma2) MT0673(mma1) MT3499(cma1)
                 MT3823(cfa-2)
            MBO: Mb0455c(ufaA1) Mb0478(umaA1) Mb0479c(pcaA) Mb0515c(cmaA2)
                 Mb0661c(mmaA4) Mb0662c(mmaA3) Mb0663c(mmaA2) Mb0664c(mmaA1)
                 Mb3424c(cmaA1) Mb3747
            MBB: BCG_0486c(ufaA1) BCG_0546c(cmaA2) BCG_3461c(cmaA1)
            MLE: ML1900(mmaA1) ML1903(mmaA4) ML2334 ML2426(cmaA2)
                 ML2459(umaA2)
            MPA: MAP0135(cmaA1) MAP0321 MAP3963(umaA1) MAP3964c(umaA2)
                 MAP3995c(cmaA2) MAP4095c(mmaA2) MAP4116c(mmaA4)
                 MAP4117c(mmaA1)
            MAV: MAV_0130 MAV_0383 MAV_4517 MAV_4541 MAV_4647 MAV_4679
            MSM: MSMEG_0902 MSMEG_1205 MSMEG_1350 MSMEG_1351 MSMEG_3538
                 MSMEG_6284
            MVA: Mvan_0803 Mvan_1239 Mvan_3025 Mvan_4948 Mvan_4949 Mvan_5532
            MGI: Mflv_1283 Mflv_1800 Mflv_1801 Mflv_3304 Mflv_5113
            MMC: Mmcs_0786 Mmcs_0787 Mmcs_0951 Mmcs_0952 Mmcs_2735 Mmcs_2885
                 Mmcs_4908
            MKM: Mkms_0801 Mkms_0802 Mkms_0969 Mkms_0970 Mkms_2779 Mkms_2929
                 Mkms_4997
            MJL: Mjls_0782 Mjls_0783 Mjls_0972 Mjls_0973 Mjls_2765 Mjls_2915
                 Mjls_5276
            CGL: NCgl0548(cgl0573) NCgl1410(cgl1466)
            CGB: cg0663(cma) cg1657(ufaA)
            CEF: CE1594
            CDI: DIP1218
            CJK: jk0915(cfa)
            NFA: nfa2880
            RHA: RHA1_ro02559 RHA1_ro04207 RHA1_ro04839 RHA1_ro07105
            SCO: SCO3091(SCE25.32c)
            SMA: SAV3528(cfa)
            ART: Arth_2360
            NCA: Noca_4538
            TFU: Tfu_2160
            FRA: Francci3_1605 Francci3_1926 Francci3_2870
            FAL: FRAAL3451 FRAAL4409(cfa)
            SEN: SACE_1992 SACE_6753
            STP: Strop_1077
            BLO: BL1672
            CYA: CYA_2534
            CYB: CYB_0142
            GVI: gll1936 gll1939
            SRU: SRU_2461
            CTE: CT1969(cfa)
            CPH: Cpha266_1075 Cpha266_1076
            PVI: Cvib_0773
            PLT: Plut_1184
            DRA: DR_2187
            DGE: Dgeo_0050
            AAE: aq_1737(cfa)
            HMA: rrnB0259(fapS)
STRUCTURES  PDB: 1KP9  1KPG  1KPH  1KPI  1L1E  1TPY  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.79
            ExPASy - ENZYME nomenclature database: 2.1.1.79
            ExplorEnz - The Enzyme Database: 2.1.1.79
            ERGO genome analysis and discovery system: 2.1.1.79
            BRENDA, the Enzyme Database: 2.1.1.79
            CAS: 51845-48-8
///
ENTRY       EC 2.1.1.80                 Enzyme
NAME        protein-glutamate O-methyltransferase;
            methyl-accepting chemotaxis protein O-methyltransferase;
            S-adenosylmethionine-glutamyl methyltransferase;
            methyl-accepting chemotaxis protein methyltransferase II;
            S-adenosylmethionine:protein-carboxyl O-methyltransferase;
            protein methylase II;
            MCP methyltransferase I;
            MCP methyltransferase II;
            protein O-methyltransferase;
            protein(aspartate)methyltransferase;
            protein(carboxyl)methyltransferase;
            protein carboxyl-methylase;
            protein carboxyl-O-methyltransferase;
            protein carboxylmethyltransferase II;
            protein carboxymethylase;
            protein carboxymethyltransferase;
            protein methyltransferase II
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:protein-L-glutamate O-methyltransferase
REACTION    S-adenosyl-L-methionine + protein L-glutamate =
            S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
            [RN:R02623]
ALL_REAC    R02623
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            protein L-glutamate [CPD:C00614]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            protein L-glutamate methyl ester [CPD:C04142]
COMMENT     Forms ester groups with L-glutamate residues in a number of membrane
            proteins.
REFERENCE   1  [PMID:6806296]
  AUTHORS   Burgess-Cassler A, Ullah AH, Ordal GW.
  TITLE     Purification and characterization of Bacillus subtilis
            methyl-accepting chemotaxis protein methyltransferase II.
  JOURNAL   J. Biol. Chem. 257 (1982) 8412-7.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   2  [PMID:16888]
  AUTHORS   Kleene SJ, Toews ML, Adler J.
  TITLE     Isolation of glutamic acid methyl ester from an Escherichia coli
            membrane protein involved in chemotaxis.
  JOURNAL   J. Biol. Chem. 252 (1977) 3214-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:3298235]
  AUTHORS   Simms SA, Stock AM, Stock JB.
  TITLE     Purification and characterization of the
            S-adenosylmethionine:glutamyl methyltransferase that modifies
            membrane chemoreceptor proteins in bacteria.
  JOURNAL   J. Biol. Chem. 262 (1987) 8537-43.
  ORGANISM  Salmonella typhimurium
REFERENCE   4  [PMID:322131]
  AUTHORS   Springer WR, Koshland DE Jr.
  TITLE     Identification of a protein methyltransferase as the cheR gene
            product in the bacterial sensing system.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 74 (1977) 533-7.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map02030  Bacterial chemotaxis - General
            PATH: map02031  Bacterial chemotaxis - Organism-specific
ORTHOLOGY   KO: K00575  chemotaxis protein methyltransferase CheR
GENES       ECO: b1884(cheR)
            ECJ: JW1873(cheR)
            ECE: Z2938(cheR)
            ECS: ECs2594
            ECC: c2299(cheR)
            ECI: UTI89_C2088(cheR)
            ECP: ECP_1829
            ECV: APECO1_933(cheR)
            ECW: EcE24377A_2117(cheR)
            ECX: EcHS_A1980(cheR)
            STY: STY2127(cheR)
            STT: t0959(cheR)
            SPT: SPA0950(cheR)
            SEC: SC1925(cheR)
            STM: STM1918(cheR)
            YPE: YPO1678(cheR)
            YPK: y1839(cheR)
            YPM: YP_1808(cheR)
            YPA: YPA_1844
            YPN: YPN_1953
            YPP: YPDSF_1770
            YPS: YPTB2399(cheR)
            YPI: YpsIP31758_1644(cheR)
            SFL: SF1933(cheR)
            SFX: S2024(cheR)
            SFV: SFV_1930(cheR)
            SSN: SSON_1233(cheR)
            SBO: SBO_1116(cheR)
            ECA: ECA1692(cheR)
            PLU: plu1855(cheR)
            ENT: Ent638_2455
            SPE: Spro_2981
            XCC: XCC1184(cheR) XCC1868(cheR) XCC2704(cheR) XCC3686(cheR)
            XCB: XC_1410 XC_2321 XC_3058 XC_3757
            XCV: XCV1331(cheR1) XCV1932(cheR2) XCV3024(cheR3) XCV3849(cheR4)
            XAC: XAC1281(cheR) XAC1890(cheR) XAC2869(cheR) XAC3730(cheR)
            XOO: XOO0644(cheR) XOO0645(cheR) XOO1466(cheR) XOO2857(cheR)
            XOM: XOO_0593(XOO0593) XOO_1367(XOO1367) XOO_2712(XOO2712)
            VCH: VC1399(cheR) VC2201(cheR) VCA1091(cheR)
            VCO: VC0395_A1793(cheR-2)
            VVU: VV1_0227(cheR) VV2_0377 VV2_1163
            VVY: VV0959 VVA0934 VVA1687
            VPA: VP0774(cheR)
            VFI: VF1878
            PPR: PBPRA0777 PBPRA0900(cheR)
            PAE: PA0175 PA0412(pilK) PA3348 PA3706
            PAU: PA14_02200(cheR) PA14_16450(wspC) PA14_20760(cheR)
            PPU: PP_1490 PP_3760 PP_4392(cheR)
            PPF: Pput_1462 Pput_4232
            PST: PSPTO_0910(cheR-1) PSPTO_1495 PSPTO_1928(cheR-2) PSPTO_2713
            PSB: Psyr_0783 Psyr_1305 Psyr_2446 Psyr_3485
            PSP: PSPPH_0802(cheR1) PSPPH_2602(cheR2) PSPPH_3412(cheR3)
                 PSPPH_3879(wspC)
            PFL: PFL_1131(cheR) PFL_3250(cheR-2) PFL_4481(cheR)
            PFO: Pfl_1054 Pfl_2647 Pfl_4252
            PEN: PSEEN0238 PSEEN1247 PSEEN3204 PSEEN3844(cheR)
            PMY: Pmen_0407 Pmen_1565 Pmen_2851
            PAR: Psyc_1814(pilK)
            SON: SO_2124(cheR-1) SO_2325(cheR-3) SO_3251(cheR-2)
            SDN: Sden_1302 Sden_3299
            SFR: Sfri_1160
            SAZ: Sama_2319 Sama_3498
            SBL: Sbal_2115 Sbal_2948
            SBM: Shew185_2244 Shew185_2963
            SLO: Shew_0110 Shew_1344
            SPC: Sputcn32_2598
            SSE: Ssed_0183 Ssed_1647 Ssed_3088
            SPL: Spea_1339
            SHE: Shewmr4_1258 Shewmr4_2090
            SHM: Shewmr7_1328 Shewmr7_1884
            SHN: Shewana3_1320 Shewana3_1943 Shewana3_2215
            SHW: Sputw3181_1405
            ILO: IL1148(cheR)
            CPS: CPS_1476(cheR)
            PHA: PSHAa0767(cheR)
            PAT: Patl_3101
            SDE: Sde_2214 Sde_3104 Sde_3630
            PIN: Ping_3720
            MAQ: Maqu_1177 Maqu_3771
            MCA: MCA0829 MCA1246
            TCX: Tcr_0757
            NOC: Noc_0127 Noc_1601
            AEH: Mlg_0892 Mlg_1118
            HHA: Hhal_0370 Hhal_0521 Hhal_2162
            HCH: HCH_00461 HCH_03705 HCH_03850 HCH_04717
            CSA: Csal_2021
            ABO: ABO_0105(cheR) ABO_1308(cheR)
            MMW: Mmwyl1_1069 Mmwyl1_3302
            AHA: AHA_1032(cheR-1) AHA_2532(cheR-2) AHA_2843(cheR-3)
            CVI: CV_2507(cheR1) CV_3437(cheR2) CV_3693(cheR3)
            RSO: RS02206(RSp1647) RSp1405(cheR)
            REU: Reut_B3651 Reut_B4915 Reut_B5191 Reut_B5610
            REH: H16_B0241(cheR1)
            RME: Rmet_3691 Rmet_3971
            BMA: BMA2856(cheR) BMAA0219
            BMV: BMASAVP1_A3431(cheR) BMASAVP1_A3432
            BML: BMA10299_A1687(cheR)
            BMN: BMA10247_3119(cheR)
            BXE: Bxe_A0122 Bxe_B1217
            BVI: Bcep1808_0218 Bcep1808_4175
            BUR: Bcep18194_A3361 Bcep18194_B2306
            BCN: Bcen_2848 Bcen_4575
            BCH: Bcen2424_0259 Bcen2424_3788
            BAM: Bamb_0172 Bamb_5515
            BPS: BPSL3303(cheR) BPSS1873
            BPM: BURPS1710b_0073(cheR) BURPS1710b_A0966
            BPL: BURPS1106A_3933(cheR)
            BPD: BURPS668_3852 BURPS668_A0207(cheR)
            BTE: BTH_I3179(cheR) BTH_II0159(cheR) BTH_II0503
            BPA: BPP1475(cheR)
            BBR: BB2549(cheR)
            RFR: Rfer_0569 Rfer_0904 Rfer_2355 Rfer_3013
            POL: Bpro_2459
            AAV: Aave_3546 Aave_4376
            AJS: Ajs_3788
            VEI: Veis_2174
            MPT: Mpe_A2700(cheR)
            HAR: HEAR1303(cheR)
            MMS: mma_0016(cheR2) mma_2093(cheR1)
            NEU: NE1861(cheR)
            NET: Neut_1171
            NMU: Nmul_A0330
            EBA: ebA2146 ebA790(cheR)
            AZO: azo0403(cheR1) azo1455(cheR2)
            DAR: Daro_0730 Daro_1146 Daro_2045
            TBD: Tbd_1617
            MFA: Mfla_1932 Mfla_2588
            HHE: HH0455(cheR)
            WSU: WS1212(cheR)
            TDN: Tmden_0975 Tmden_1940
            CJE: Cj0923c(cheR)
            CJR: CJE1001(cheR)
            CJJ: CJJ81176_0930(cheR)
            CJU: C8J_0860(cheR)
            CFF: CFF8240_0803(cheR)
            CCV: CCV52592_0716 CCV52592_1333(cheR)
            CCO: CCC13826_1077
            ABU: Abu_1186(cheR)
            GSU: GSU0295(cheR-1) GSU1143(cheR-2) GSU2215(cheR-3) GSU3195
            GME: Gmet_0780 Gmet_1077 Gmet_2305 Gmet_2420 Gmet_2641 Gmet_2707
                 Gmet_3212 Gmet_3267
            GUR: Gura_0725 Gura_2166 Gura_2454 Gura_2689 Gura_2691 Gura_2984
                 Gura_3139 Gura_4168 Gura_4421
            PCA: Pcar_1199 Pcar_2491
            PPD: Ppro_0077 Ppro_0878 Ppro_1610
            DVU: DVU0449 DVU1595(cheR-1) DVU2076(cheR-2)
            DVL: Dvul_1152 Dvul_1539
            DDE: Dde_1198 Dde_1573 Dde_2105
            LIP: LI1139(cheR)
            BBA: Bd2830(cheR) Bd3468(cheR)
            DPS: DP1792(cheR) DP2645(cheR)
            ADE: Adeh_0601 Adeh_0615 Adeh_1196 Adeh_1371 Adeh_1382 Adeh_2731
                 Adeh_2941 Adeh_3183 Adeh_3954
            AFW: Anae109_0466 Anae109_0541 Anae109_0645 Anae109_0659
                 Anae109_2294 Anae109_2370
            MXA: MXAN_0713 MXAN_2682(cheR) MXAN_4138(frzF) MXAN_4753(cheR)
                 MXAN_5144(cheR) MXAN_6948 MXAN_6960(cheR) MXAN_7103(cheR)
            SAT: SYN_00434 SYN_00970
            AMA: AM1084(hemK)
            MLO: mll9515
            MES: Meso_0597 Meso_1943
            SME: SMa1552 SMb20515 SMc03009(cheR)
            SMD: Smed_0237 Smed_5115
            ATU: Atu0518(CheR)
            ATC: AGR_C_914(cheR)
            RET: RHE_CH00641(cheRch1) RHE_CH03516(cheRch2) RHE_PF00076(cheRf)
            RLE: RL0690(cheR) RL4029(cheR)
            BJA: bll0390(cheR1) blr2196(cheR) blr2348(cheR)
            BRA: BRADO0820(cheR) BRADO1477(cheR) BRADO1825(cheR)
                 BRADO7000(cheR)
            BBT: BBta_0527(cheR) BBta_1533 BBta_2146(cheR) BBta_6555(cheR)
                 BBta_6731(cheR) BBta_7834(cheR)
            RPA: RPA0138(cheR1) RPA1631(cheR2) RPA1678(cheR3) RPA3316
            RPB: RPB_3855 RPB_3916
            RPC: RPC_3801 RPC_4243 RPC_4609 RPC_4669
            RPD: RPD_1494 RPD_3674
            RPE: RPE_1196 RPE_3633 RPE_3924 RPE_4280 RPE_4670
            NWI: Nwi_0524
            NHA: Nham_3372
            CCR: CC_0435(cheR) CC_0598(cheR) CC_3472(cheR)
            SIT: TM1040_3204 TM1040_3243
            RSP: RSP_0048(cheR3) RSP_1587(cheR2) RSP_2229 RSP_2434(cheR1)
            RSH: Rsph17029_0239 Rsph17029_1098 Rsph17029_1683
            RSQ: Rsph17025_0267 Rsph17025_1636 Rsph17025_1796
            JAN: Jann_2839
            RDE: RD1_3061(cheR) RD1_3107
            MMR: Mmar10_0662
            HNE: HNE_0640(cheR)
            ZMO: ZMO0082(cheR)
            SAL: Sala_1736
            SWI: Swit_0069
            ELI: ELI_11245
            GOX: GOX1554(cheR)
            GBE: GbCGDNIH1_1133
            ACR: Acry_2710
            RRU: Rru_A0524 Rru_A1405 Rru_A1500 Rru_A2325
            MAG: amb0322 amb1963 amb3003 amb3654 amb3879
            MGM: Mmc1_0625 Mmc1_1481 Mmc1_1831 Mmc1_3390 Mmc1_3582
            ABA: Acid345_1529 Acid345_1772
            SUS: Acid_5370
            BSU: BG10283(cheR)
            BHA: BH1655(cheR)
            BAN: BA0995 BA1665(cheR)
            BAR: GBAA0995 GBAA1665(cheR)
            BAA: BA_1563(cheR) BA_2180
            BAT: BAS0931 BAS1547(cheR)
            BCE: BC1007 BC1632
            BCA: BCE_1089 BCE_1754(cheR)
            BCZ: BCZK0899(cheR) BCZK1511(cheR)
            BCY: Bcer98_1347
            BTK: BT9727_0916(cheR) BT9727_1522(cheR)
            BLI: BL02780(cheR)
            BLD: BLi02407(cheR)
            BCL: ABC1891(cheR)
            BAY: RBAM_020880(cheR)
            BPU: BPUM_2003(cheR)
            OIH: OB1786(cheR)
            GKA: GK2208(cheR)
            LMO: lmo0683
            LMF: LMOf2365_0719(cheR)
            LIN: lin0691
            LWE: lwe0652(cheR)
            STH: STH1542(cheR)
            CAC: CAC0121(cheR) CAC2221(cheR)
            CTC: CTC01732(cheR)
            CNO: NT01CX_1863
            CTH: Cthe_0288 Cthe_0717 Cthe_0808 Cthe_2282 Cthe_2820
            CDF: CD0541(cheR)
            CBO: CBO2749(cheR)
            CBA: CLB_2690(cheR)
            CBH: CLC_2623(cheR)
            CBF: CLI_2799(cheR)
            CBE: Cbei_4181 Cbei_4308 Cbei_4827
            CKL: CKL_2130(cheR)
            AMT: Amet_2623
            CHY: CHY_1016(cheR1) CHY_1028(cheR2)
            DSY: DSY3036
            DRM: Dred_2384
            SWO: Swol_0695 Swol_1330 Swol_1457
            CSC: Csac_0816 Csac_0981
            TTE: TTE1037(cheR) TTE1355(cheR2)
            MTA: Moth_0801
            MAV: MAV_2216(cheR) MAV_4065(cheR)
            MSM: MSMEG_5553(cheR)
            MGI: Mflv_1001
            NCA: Noca_3598
            ACE: Acel_0223 Acel_1788
            KRA: Krad_0322 Krad_1849
            RBA: RB4511
            BBU: BB0040(cheR-1) BB0414(cheR-2)
            BGA: BG0040(cheR-1) BG0416(cheR-2)
            BAF: BAPKO_0040(cheR-1)
            TPA: TP0630
            TDE: TDE0647(cheR)
            LIL: LA1743(cheR1) LA2042(cheR2)
            LIC: LIC11871(cheR) LIC12062
            LBJ: LBJ_0483(cheR) LBJ_1248
            LBL: LBL_1297 LBL_2596(cheR)
            GVI: gll1854 glr3330 glr3562
            ANA: all1716 all1848
            AVA: Ava_0314 Ava_4781
            TER: Tery_4228
            SRU: SRU_0336(cheB) SRU_2605(cheR)
            CHU: CHU_2079(cheR)
            FJO: Fjoh_3352
            CCH: Cag_0563
            RRS: RoseRS_0033 RoseRS_0993
            RCA: Rcas_3195 Rcas_4209
            TMA: TM0464
            TPT: Tpet_0456
            TME: Tmel_0987
            FNO: Fnod_1104
            MMP: MMP0930(cheR)
            MMQ: MmarC5_0737
            MMZ: MmarC7_0177
            MVN: Mevan_0259
            MAC: MA0013(cheR) MA3063(cheR) MA3542
            MBA: Mbar_A0983
            MMA: MM_0325(cheR) MM_1324
            MBU: Mbur_0364
            MHU: Mhun_0961 Mhun_0992
            MEM: Memar_1545
            MBN: Mboo_1581
            AFU: AF1037(cheR)
            HAL: VNG0966G(cheR)
            HMA: rrnAC2206(cheR)
            NPH: NP2170A(cheR)
            PHO: PH0481
            PAB: PAB1329(cheR)
            TKO: TK0631
STRUCTURES  PDB: 1AF7  1BC5  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.80
            ExPASy - ENZYME nomenclature database: 2.1.1.80
            ExplorEnz - The Enzyme Database: 2.1.1.80
            ERGO genome analysis and discovery system: 2.1.1.80
            BRENDA, the Enzyme Database: 2.1.1.80
            CAS: 9055-09-8
///
ENTRY       EC 2.1.1.81       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
COMMENT     Deleted entry: nicotine N-methyltransferase. Now included with EC
            2.1.1.49 amine N-methyltransferase. (EC 2.1.1.81 created 1989,
            deleted 1990)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.81
            ExPASy - ENZYME nomenclature database: 2.1.1.81
            ExplorEnz - The Enzyme Database: 2.1.1.81
            ERGO genome analysis and discovery system: 2.1.1.81
            BRENDA, the Enzyme Database: 2.1.1.81
///
ENTRY       EC 2.1.1.82                 Enzyme
NAME        3-methylquercetin 7-O-methyltransferase;
            flavonol 7-O-methyltransferase;
            flavonol 7-methyltransferase;
            7-OMT;
            S-adenosyl-L-methionine:3',4',5,7-tetrahydroxy-3-methoxyflavone
            7-O-methyltransferase;
            3-methylquercitin 7-O-methyltransferase [mis-spelt]
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:5,7,3',4'-tetrahydroxy-3-methoxyflavone
            7-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxy-3-methoxyflavone =
            S-adenosyl-L-homocysteine + 5,3',4'-trihydroxy-3,7-dimethoxyflavone
            [RN:R05323]
ALL_REAC    R05323
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            5,7,3',4'-tetrahydroxy-3-methoxyflavone
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            5,3',4'-trihydroxy-3,7-dimethoxyflavone
COMMENT     Involved with EC 2.1.1.76 quercetin 3-O-methyltransferase and EC
            2.1.1.83 3,7-dimethylquercetin 4'-O-methyltransferase in the
            methylation of quercetin to 3,7,4'-trimethylquercetin in
            Chrysosplenium americanum. Does not act on flavones,
            dihydroflavonols, or their glucosides.
REFERENCE   1  [PMID:3994393]
  AUTHORS   De Luca V, Ibrahim RK.
  TITLE     Enzymatic synthesis of polymethylated flavonols in Chrysosplenium
            americanum. I. Partial purification and some properties of
            S-adenosyl-L-methionine:flavonol 3-, 6-, 7-, and
            4'-O-methyltransferases.
  JOURNAL   Arch. Biochem. Biophys. 238 (1985) 596-605.
  ORGANISM  Chrysosplenium americanum
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.82
            ExPASy - ENZYME nomenclature database: 2.1.1.82
            ExplorEnz - The Enzyme Database: 2.1.1.82
            ERGO genome analysis and discovery system: 2.1.1.82
            BRENDA, the Enzyme Database: 2.1.1.82
            CAS: 96477-62-2
///
ENTRY       EC 2.1.1.83                 Enzyme
NAME        3,7-dimethylquercetin 4'-O-methyltransferase;
            flavonol 4'-O-methyltransferase;
            flavonol 4'-methyltransferase;
            4'-OMT;
            S-adenosyl-L-methionine:3',4',5-trihydroxy-3,7-dimethoxyflavone
            4'-O-methyltransferase;
            3,7-dimethylquercitin 4'-O-methyltransferase [mis-spelt]
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:5,3',4'-trihydroxy-3,7-dimethoxyflavone
            4'-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 5,3',4'-trihydroxy-3,7-dimethoxyflavone =
            S-adenosyl-L-homocysteine + 5,3'-dihydroxy-3,7,4'-trimethoxyflavone
            [RN:R03456]
ALL_REAC    R03456
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            5,3',4'-trihydroxy-3,7-dimethoxyflavone
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            5,3'-dihydroxy-3,7,4'-trimethoxyflavone
COMMENT     3,7-Dimethylquercetagetin can also act as acceptor. Involved with EC
            2.1.1.76 quercetin 3-O-methyltransferase and EC 2.1.1.82
            3-methylquercetin 7-O-methyltransferase in the methylation of
            quercetin to 3,7,4'-trimethylquercetin in Chrysosplenium americanum.
            Does not act on flavones, dihydroflavonols, or their glucosides.
REFERENCE   1  [PMID:3994393]
  AUTHORS   De Luca V, Ibrahim RK.
  TITLE     Enzymatic synthesis of polymethylated flavonols in Chrysosplenium
            americanum. I. Partial purification and some properties of
            S-adenosyl-L-methionine:flavonol 3-, 6-, 7-, and
            4'-O-methyltransferases.
  JOURNAL   Arch. Biochem. Biophys. 238 (1985) 596-605.
  ORGANISM  Chrysosplenium americanum
REFERENCE   2  [PMID:3994394]
  AUTHORS   De Luca V, Ibrahim RK.
  TITLE     Enzymatic synthesis of polymethylated flavonols in Chrysosplenium
            americanum. II. Substrate interaction and product inhibition studies
            of flavonol 3-, 6-, and 4'-O-methyltransferases.
  JOURNAL   Arch. Biochem. Biophys. 238 (1985) 606-18.
  ORGANISM  Chrysosplenium americanum
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.83
            ExPASy - ENZYME nomenclature database: 2.1.1.83
            ExplorEnz - The Enzyme Database: 2.1.1.83
            ERGO genome analysis and discovery system: 2.1.1.83
            BRENDA, the Enzyme Database: 2.1.1.83
            CAS: 96477-60-0
///
ENTRY       EC 2.1.1.84                 Enzyme
NAME        methylquercetagetin 6-O-methyltransferase;
            flavonol 6-O-methyltransferase;
            flavonol 6-methyltransferase;
            6-OMT;
            S-adenosyl-L-methionine:3',4',5,6-tetrahydroxy-3,7-dimethoxyflavone
            6-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:3',4',5,6-tetrahydroxy-3,7-dimethoxyflavone
            6-O-methyltransferase
REACTION    S-adenosyl-L-methionine +
            5,6,3',4'-tetrahydroxy-3,7-dimethoxyflavone =
            S-adenosyl-L-homocysteine +
            5,3',4'-trihydroxy-3,6,7-trimethoxyflavone [RN:R04505]
ALL_REAC    R04505
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            5,6,3',4'-tetrahydroxy-3,7-dimethoxyflavone
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            5,3',4'-trihydroxy-3,6,7-trimethoxyflavone
COMMENT     The enzymes from Chrysosplenium americanum also methylates
            3,7,3'-trimethylquercetagetin at the 6-position. Does not act on
            flavones, dihydroflavonols, or their glucosides.
REFERENCE   1  [PMID:3994393]
  AUTHORS   De Luca V, Ibrahim RK.
  TITLE     Enzymatic synthesis of polymethylated flavonols in Chrysosplenium
            americanum. I. Partial purification and some properties of
            S-adenosyl-L-methionine:flavonol 3-, 6-, 7-, and
            4'-O-methyltransferases.
  JOURNAL   Arch. Biochem. Biophys. 238 (1985) 596-605.
  ORGANISM  Chrysosplenium americanum
REFERENCE   2  [PMID:3994394]
  AUTHORS   De Luca V, Ibrahim RK.
  TITLE     Enzymatic synthesis of polymethylated flavonols in Chrysosplenium
            americanum. II. Substrate interaction and product inhibition studies
            of flavonol 3-, 6-, and 4'-O-methyltransferases.
  JOURNAL   Arch. Biochem. Biophys. 238 (1985) 606-18.
  ORGANISM  Chrysosplenium americanum
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.84
            ExPASy - ENZYME nomenclature database: 2.1.1.84
            ExplorEnz - The Enzyme Database: 2.1.1.84
            ERGO genome analysis and discovery system: 2.1.1.84
            BRENDA, the Enzyme Database: 2.1.1.84
            CAS: 96477-60-0
///
ENTRY       EC 2.1.1.85                 Enzyme
NAME        protein-histidine N-methyltransferase;
            protein methylase IV;
            protein (histidine) methyltransferase;
            actin-specific histidine methyltransferase;
            S-adenosyl methionine:protein-histidine N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:protein-L-histidine N-tele-methyltransferase
REACTION    S-adenosyl-L-methionine + protein L-histidine =
            S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine
            [RN:R02627]
ALL_REAC    R02627
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            protein L-histidine [CPD:C00615]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            protein Ntau-methyl-L-histidine [CPD:C04087]
COMMENT     Highly specific for histidine residues, for example, in actin.
REFERENCE   1  [PMID:3801515]
  AUTHORS   Vijayasarathy C, Rao BS.
  TITLE     Partial purification and characterisation of
            S-adenosylmethionine:protein-histidine N-methyltransferase from
            rabbit skeletal muscle.
  JOURNAL   Biochim. Biophys. Acta. 923 (1987) 156-65.
  ORGANISM  rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.85
            ExPASy - ENZYME nomenclature database: 2.1.1.85
            ExplorEnz - The Enzyme Database: 2.1.1.85
            ERGO genome analysis and discovery system: 2.1.1.85
            BRENDA, the Enzyme Database: 2.1.1.85
            CAS: 108022-17-9
///
ENTRY       EC 2.1.1.86                 Enzyme
NAME        tetrahydromethanopterin S-methyltransferase;
            tetrahydromethanopterin methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     5-methyl-5,6,7,8-tetrahydromethanopterin:2-mercaptoethanesulfonate
            2-methyltransferase
REACTION    5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
            = 5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
            [RN:R04347]
ALL_REAC    R04347
SUBSTRATE   5-methyl-5,6,7,8-tetrahydromethanopterin [CPD:C04488];
            2-mercaptoethanesulfonate [CPD:C03576]
PRODUCT     5,6,7,8-tetrahydromethanopterin [CPD:C01217];
            2-(methylthio)ethanesulfonate [CPD:C03920]
COMMENT     Involved in the formation of methane from CO in Methanobacterium
            thermoautotrophicum. Methanopterin is a pterin analogue. The
            reaction involves the export of one or two sodium ions in Archaea.
REFERENCE   1  [PMID:3085670]
  AUTHORS   Sauer FD.
  TITLE     Tetrahydromethanopterin methyltransferase, a component of the
            methane synthesizing complex of Methanobacterium
            thermoautotrophicum.
  JOURNAL   Biochem. Biophys. Res. Commun. 136 (1986) 542-7.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K00576  tetrahydromethanopterin S-methyltransferase
            KO: K00577  tetrahydromethanopterin S-methyltransferase 23 kD
                        subunit
            KO: K00578  tetrahydromethanopterin S-methyltransferase 12.5 kD
                        subunit
            KO: K00579  tetrahydromethanopterin S-methyltransferase 24 kD
                        subunit
            KO: K00580  tetrahydromethanopterin S-methyltransferase 21 kD
                        subunit
            KO: K00581  tetrahydromethanopterin S-methyltransferase 28 kD
                        subunit
            KO: K00582  tetrahydromethanopterin S-methyltransferase 12 kD
                        subunit
            KO: K00583  tetrahydromethanopterin S-methyltransferase 13 kD
                        subunit
            KO: K00584  tetrahydromethanopterin S-methyltransferase 34 kD
                        subunit
GENES       DSY: DSY3157
            MJA: MJ0847(mtrE) MJ0848(mtrD) MJ0849(mtrC) MJ0850(mtrB)
                 MJ0851(mtrA) MJ0852(mtrF) MJ0853(mtrG) MJ0854(mtrH)
            MMP: MMP1560(mtrE) MMP1561(mtrD) MMP1562(mtrC) MMP1563(mtrB)
                 MMP1564(mtrA) MMP1565(or900) MMP1566(mtrG) MMP1567(mtrH)
            MMQ: MmarC5_0016
            MMZ: MmarC7_0807 MmarC7_0808 MmarC7_0809 MmarC7_0810 MmarC7_0811
                 MmarC7_0812 MmarC7_0814
            MAE: Maeo_1269 Maeo_1270 Maeo_1271 Maeo_1273 Maeo_1274 Maeo_1276
            MVN: Mevan_0873 Mevan_0874 Mevan_0875 Mevan_0877 Mevan_0878
                 Mevan_0880
            MAC: MA0269(mtrH) MA0270(mtrG) MA0271(mtrF) MA0272(mtrA)
                 MA0273(mtrB) MA0274(mtrC) MA0275(mtrD) MA0276(mtrE)
                 MA1804(mtxH) MA1805(mtxA)
            MBA: Mbar_A0410 Mbar_A1255 Mbar_A1256 Mbar_A1257 Mbar_A1258
                 Mbar_A1259 Mbar_A1260 Mbar_A1261 Mbar_A1262 Mbar_A1713
                 Mbar_A2072 Mbar_A2073
            MMA: MM_0255 MM_0256 MM_1540 MM_1541 MM_1542 MM_1543 MM_1544
                 MM_1545 MM_1546 MM_1547 MM_2251
            MBU: Mbur_1518 Mbur_1519 Mbur_1520 Mbur_1521 Mbur_1522 Mbur_1523
                 Mbur_1524 Mbur_1525 Mbur_2244
            MTP: Mthe_1379 Mthe_1380 Mthe_1382 Mthe_1385
            MHU: Mhun_2168 Mhun_2169 Mhun_2170 Mhun_2171 Mhun_2172 Mhun_2173
                 Mhun_2175
            MLA: Mlab_0779
            MEM: Memar_0612
            MBN: Mboo_0573
            MTH: MTH1156(mtrH) MTH1157(mtrG) MTH1158(mtrF) MTH1159(mtrA)
                 MTH1160(mtrB) MTH1161(mtrC) MTH1162(mtrD) MTH1163(mtrE)
            MST: Msp_0300(mtrE) Msp_0301(mtrD) Msp_0302(mtrC) Msp_0303(mtrB)
                 Msp_0304(mtrA) Msp_0305(mtrF) Msp_0306(mtrG) Msp_0307(mtrH)
            MSI: Msm_1007 Msm_1010 Msm_1012 Msm_1013 Msm_1014
            MKA: MK0656(mtrE) MK0657(mtrD) MK0658(mtrC) MK0659(mtrB)
                 MK0660(mtrA) MK0661(mtrG) MK0662(mtrH) MK1485(mtrF)
            AFU: AF0009(mtr)
            RCI: RCIX2064(mtrE) RCIX2065(mtrD) RCIX2066(mtrC) RCIX2067(mtrB)
                 RCIX2068(mtrA-1) RCIX2069(mtrA-2) RCIX2070(mtrG)
                 RCIX2071(mtrH)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.86
            ExPASy - ENZYME nomenclature database: 2.1.1.86
            ExplorEnz - The Enzyme Database: 2.1.1.86
            ERGO genome analysis and discovery system: 2.1.1.86
            UM-BBD (Biocatalysis/Biodegradation Database): 2.1.1.86
            BRENDA, the Enzyme Database: 2.1.1.86
            CAS: 103406-60-6
///
ENTRY       EC 2.1.1.87                 Enzyme
NAME        pyridine N-methyltransferase;
            pyridine methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:pyridine N-methyltransferase
REACTION    S-adenosyl-L-methionine + pyridine = S-adenosyl-L-homocysteine +
            N-methylpyridinium [RN:R02862]
ALL_REAC    R02862
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            pyridine [CPD:C00747]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            N-methylpyridinium [CPD:C02724]
REFERENCE   1  [PMID:3751119]
  AUTHORS   Damani LA, Shaker MS, Crooks PA, Godin CS, Nwosu C.
  TITLE     N-methylation and quaternization of pyridine in vitro by rabbit
            lung, liver and kidney N-methyltransferases: an
            S-adenosyl-L-methionine-dependent reaction.
  JOURNAL   Xenobiotica. 16 (1986) 645-50.
  ORGANISM  rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.87
            ExPASy - ENZYME nomenclature database: 2.1.1.87
            ExplorEnz - The Enzyme Database: 2.1.1.87
            ERGO genome analysis and discovery system: 2.1.1.87
            BRENDA, the Enzyme Database: 2.1.1.87
            CAS: 104327-10-8
///
ENTRY       EC 2.1.1.88                 Enzyme
NAME        8-hydroxyquercetin 8-O-methyltransferase;
            flavonol 8-O-methyltransferase;
            flavonol 8-methyltransferase;
            S-adenosyl-L-methionine:3,3',4',5,7,8-hexahydroxyflavone
            8-O-methyltransferase;
            8-hydroxyquercitin 8-O-methyltransferase [mis-spelt]
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:3,5,7,8,3',4'-hexahydroxyflavone
            8-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 3,5,7,8,3',4'-hexahydroxyflavone =
            S-adenosyl-L-homocysteine +
            3,5,7,3',4'-pentahydroxy-8-methoxyflavone [RN:R04398]
ALL_REAC    R04398
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            3,5,7,8,3',4'-hexahydroxyflavone
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            3,5,7,3',4'-pentahydroxy-8-methoxyflavone
COMMENT     Also acts on 8-hydroxykaempferol, but not on the glycosides of
            8-hydroxyflavonols. An enzyme from the flower buds of Lotus
            corniculatus.
REFERENCE   1  [PMID:4076180]
  AUTHORS   Jay M, De Luca V, Ibrahim RK.
  TITLE     Purification, properties and kinetic mechanism of flavonol
            8-O-methyltransferase from Lotus corniculatus L.
  JOURNAL   Eur. J. Biochem. 153 (1985) 321-5.
  ORGANISM  Lotus corniculatus [GN:elco]
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.88
            ExPASy - ENZYME nomenclature database: 2.1.1.88
            ExplorEnz - The Enzyme Database: 2.1.1.88
            ERGO genome analysis and discovery system: 2.1.1.88
            BRENDA, the Enzyme Database: 2.1.1.88
            CAS: 99775-17-4
///
ENTRY       EC 2.1.1.89                 Enzyme
NAME        tetrahydrocolumbamine 2-O-methyltransferase;
            tetrahydrocolumbamine methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:5,8,13,13a-tetrahydrocolumbamine
            2-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 5,8,13,13a-tetrahydrocolumbamine =
            S-adenosyl-L-homocysteine + tetrahydropalmatine [RN:R04077]
ALL_REAC    R04077
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            5,8,13,13a-tetrahydrocolumbamine [CPD:C04118]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            tetrahydropalmatine [CPD:C02890]
COMMENT     Involved in the biosynthesis of the berberine alkaloids.
REFERENCE   1
  AUTHORS   Beecher, C.W.W. and Kelleher, W.J.
  TITLE     Enzymatic study of the late stages of protoberberine alkaloid
            biosynthesis.
  JOURNAL   Tetrahedron Lett. 25 (1984) 4595-4598.
  ORGANISM  Berberis aggregata
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.89
            ExPASy - ENZYME nomenclature database: 2.1.1.89
            ExplorEnz - The Enzyme Database: 2.1.1.89
            ERGO genome analysis and discovery system: 2.1.1.89
            BRENDA, the Enzyme Database: 2.1.1.89
            CAS: 93792-09-7
///
ENTRY       EC 2.1.1.90                 Enzyme
NAME        methanol---5-hydroxybenzimidazolylcobamide Co-methyltransferase;
            methanol cobalamin methyltransferase;
            methanol:5-hydroxybenzimidazolylcobamide methyltransferase;
            MT 1
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     methanol:5-hydroxybenzimidazolylcobamide Co-methyltransferase
REACTION    methanol + 5-hydroxybenzimidazolylcobamide =
            Co-methyl-Co-5-hydroxybenzimidazolylcob(I)amide + H2O [RN:R04384]
ALL_REAC    R04384
SUBSTRATE   methanol [CPD:C00132];
            5-hydroxybenzimidazolylcobamide [CPD:C04054]
PRODUCT     Co-methyl-Co-5-hydroxybenzimidazolylcob(I)amide [CPD:C04665];
            H2O [CPD:C00001]
COMMENT     The enzyme from Methanosarcina barkeri contains three-four molecules
            of bound 5-hydroxybenzimidazolylcobamide that act as methyl
            acceptor. Inactivated by oxygen and other oxidizing agents, and
            reactivated by catalytic amounts of ATP and hydrogen.
REFERENCE   1  [PMID:6438059]
  AUTHORS   van der Meijden P, te Brommelstroet BW, Poirot CM, van der Drift C,
            Vogels GD.
  TITLE     Purification and properties of
            methanol:5-hydroxybenzimidazolylcobamide methyltransferase from
            Methanosarcina barkeri.
  JOURNAL   J. Bacteriol. 160 (1984) 629-35.
  ORGANISM  Methanosarcina barkeri [GN:mba]
GENES       RCI: RCIX1973(mtaC) RCIX1974(mtaB)
STRUCTURES  PDB: 2I2X  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.90
            ExPASy - ENZYME nomenclature database: 2.1.1.90
            ExplorEnz - The Enzyme Database: 2.1.1.90
            ERGO genome analysis and discovery system: 2.1.1.90
            BRENDA, the Enzyme Database: 2.1.1.90
            CAS: 86611-98-5
///
ENTRY       EC 2.1.1.91                 Enzyme
NAME        isobutyraldoxime O-methyltransferase;
            aldoxime methyltransferase;
            S-adenosylmethionine:aldoxime O-methyltransferase;
            aldoxime O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:2-methylpropanal-oxime O-methyltransferase
REACTION    S-adenosyl-L-methionine + 2-methylpropanal oxime =
            S-adenosyl-L-homocysteine + 2-methylpropanal O-methyloxime
            [RN:R04169]
ALL_REAC    R04169
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            2-methylpropanal oxime [CPD:C03219]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            2-methylpropanal O-methyloxime [CPD:C03982]
COMMENT     Oximes of C4 to C6 aldehydes can act as acceptors; the most active
            substrate is 2-methylbutyroaldoxime.
REFERENCE   1  [PMID:3977861]
  AUTHORS   Harper DB, Kennedy JT.
  TITLE     Purification and properties of S-adenosylmethionine: aldoxime
            O-methyltransferase from Pseudomonas sp. N.C.I.B. 11652.
  JOURNAL   Biochem. J. 226 (1985) 147-53.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.91
            ExPASy - ENZYME nomenclature database: 2.1.1.91
            ExplorEnz - The Enzyme Database: 2.1.1.91
            ERGO genome analysis and discovery system: 2.1.1.91
            BRENDA, the Enzyme Database: 2.1.1.91
            CAS: 95471-32-2
///
ENTRY       EC 2.1.1.92       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
COMMENT     Deleted entry: bergaptol O-methyltransferase. Now included with EC
            2.1.1.69, 5-hydroxyfuranocoumarin 5-O-methyltransferase. The
            reaction with bergaptol is a specific example of the general
            reaction associated with EC 2.1.1.69. (EC 2.1.1.92 created 1989,
            deleted 2006)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.92
            ExPASy - ENZYME nomenclature database: 2.1.1.92
            ExplorEnz - The Enzyme Database: 2.1.1.92
            ERGO genome analysis and discovery system: 2.1.1.92
            BRENDA, the Enzyme Database: 2.1.1.92
///
ENTRY       EC 2.1.1.93                 Enzyme
NAME        xanthotoxol O-methyltransferase;
            xanthotoxol methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:xanthotoxol O-methyltransferase
REACTION    S-adenosyl-L-methionine + xanthotoxol = S-adenosyl-L-homocysteine +
            O-methylxanthotoxol [RN:R02982]
ALL_REAC    R02982
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            xanthotoxol [CPD:C00841]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            O-methylxanthotoxol
COMMENT     Also acts on 5-hydroxyxanthotoxin, formingisopimpinellin.
REFERENCE   1
  AUTHORS   Hauffe, K.D., Hahlbrock, K. and Scheel, D.
  TITLE     Elicitor-stimulated furanocoumarin biosynthesis in cultured parsley
            cells - S-adenosyl-L-methionine-bergaptol and
            S-adenosyl-L-methionine-xanthotoxol O-methyltransferases.
  JOURNAL   Z. Naturforsch. C: Biosci. 41 (1986) 228-239.
  ORGANISM  Petroselinum crispum
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.93
            ExPASy - ENZYME nomenclature database: 2.1.1.93
            ExplorEnz - The Enzyme Database: 2.1.1.93
            ERGO genome analysis and discovery system: 2.1.1.93
            BRENDA, the Enzyme Database: 2.1.1.93
            CAS: 101637-32-5
///
ENTRY       EC 2.1.1.94                 Enzyme
NAME        tabersonine 16-O-methyltransferase;
            11-demethyl-17-deacetylvindoline 11-methyltransferase;
            11-O-demethyl-17-O-deacetylvindoline O-methyltransferase;
            S-adenosyl-L-methionine:11-O-demethyl-17-O-deacetylvindoline
            11-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:16-hydroxytabersonine 16-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 16-hydroxytabersonine =
            S-adenosyl-L-homocysteine + 16-methoxytabersonine [RN:R05885]
ALL_REAC    R05885;
            (other) R03229
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            16-hydroxytabersonine [CPD:C11643]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            16-methoxytabersonine [CPD:C11675]
COMMENT     Involved in the biosynthesis of vindoline from tabersonine in the
            Madagascar periwinkle, Catharanthus roseus.
REFERENCE   1  [PMID:16526094]
  AUTHORS   Foucher AL, McIntosh A, Douce G, Wastling J, Tait A, Turner CM.
  TITLE     A proteomic analysis of arsenical drug resistance in Trypanosoma
            brucei.
  JOURNAL   Proteomics. 6 (2006) 2726-32.
REFERENCE   2
  AUTHORS   Fahn, W., Laussermair, E., Deus-Neumann, B. and Stockigt, J.
  TITLE     Late enzymes of vindoline biosynthesis.
            S-Adenosyl-L-methionine:11-O-demethyl-17-O-deacetylvindoline
            11-O-methylase and unspecific acetylesterase.
  JOURNAL   Plant Cell Rep. 4 (1985) 337-340.
  ORGANISM  Catharanthus roseus
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.94
            ExPASy - ENZYME nomenclature database: 2.1.1.94
            ExplorEnz - The Enzyme Database: 2.1.1.94
            ERGO genome analysis and discovery system: 2.1.1.94
            BRENDA, the Enzyme Database: 2.1.1.94
            CAS: 100984-95-0
///
ENTRY       EC 2.1.1.95                 Enzyme
NAME        tocopherol O-methyltransferase;
            gamma-tocopherol methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:gamma-tocopherol 5-O-methyltransferase
REACTION    S-adenosyl-L-methionine + gamma-tocopherol =
            S-adenosyl-L-homocysteine + alpha-tocopherol [RN:R07236]
ALL_REAC    R07236;
            (other) R07504
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            gamma-tocopherol [CPD:C02483]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            alpha-tocopherol [CPD:C02477]
REFERENCE   1
  AUTHORS   Camara, B. and D'Harlingue, A.
  TITLE     Demonstration and solubilization of S-adenosylmethionine -
            gamma-tocopherol methyltransferase from capsicum chromoplasts.
  JOURNAL   Plant Cell Rep. 4 (1985) 31-32.
  ORGANISM  capsicum
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K05928  tocopherol O-methyltransferase
GENES       ATH: AT1G64970(G-TMT)
            SYN: slr0089(VTE4)
            CYA: CYA_2254
            CYB: CYB_2403
            GVI: glr3090
            ANA: alr1803
            AVA: Ava_4806
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.95
            ExPASy - ENZYME nomenclature database: 2.1.1.95
            ExplorEnz - The Enzyme Database: 2.1.1.95
            ERGO genome analysis and discovery system: 2.1.1.95
            BRENDA, the Enzyme Database: 2.1.1.95
            CAS: 84788-82-9
///
ENTRY       EC 2.1.1.96                 Enzyme
NAME        thioether S-methyltransferase;
            S-adenosyl-L-methionine:thioether S-methyltransferase;
            thioether methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:dimethyl-sulfide S-methyltransferase
REACTION    S-adenosyl-L-methionine + dimethyl sulfide =
            S-adenosyl-L-homocysteine + trimethylsulfonium [RN:R02572]
ALL_REAC    R02572
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            dimethyl sulfide [CPD:C00580]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            trimethylsulfonium [CPD:C01008]
COMMENT     Also acts on dimethyl selenide, dimethyl telluride, diethyl sulfide,
            1,4-dithiane and many other thioethers.
REFERENCE   1  [PMID:3350800]
  AUTHORS   Mozier NM, McConnell KP, Hoffman JL.
  TITLE     S-adenosyl-L-methionine:thioether S-methyltransferase, a new enzyme
            in sulfur and selenium metabolism.
  JOURNAL   J. Biol. Chem. 263 (1988) 4527-31.
  ORGANISM  mouse [GN:mmu]
ORTHOLOGY   KO: K00585  thioether S-methyltransferase
GENES       MMU: 21743(Inmt)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.96
            ExPASy - ENZYME nomenclature database: 2.1.1.96
            ExplorEnz - The Enzyme Database: 2.1.1.96
            ERGO genome analysis and discovery system: 2.1.1.96
            BRENDA, the Enzyme Database: 2.1.1.96
            CAS: 114797-02-3
///
ENTRY       EC 2.1.1.97                 Enzyme
NAME        3-hydroxyanthranilate 4-C-methyltransferase;
            3-hydroxyanthranilate 4-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:3-hydroxyanthranilate 4-C-methyltransferase
REACTION    S-adenosyl-L-methionine + 3-hydroxyanthranilate =
            S-adenosyl-L-homocysteine + 3-hydroxy-4-methylanthranilate
            [RN:R02667]
ALL_REAC    R02667
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            3-hydroxyanthranilate [CPD:C00632]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            3-hydroxy-4-methylanthranilate [CPD:C03986]
COMMENT     Involved in the biosynthesis of the antibiotic actinomycin in
            Streptomyces antibioticus.
REFERENCE   1  [PMID:2450873]
  AUTHORS   Fawaz F, Jones GH.
  TITLE     Actinomycin synthesis in Streptomyces antibioticus. Purification and
            properties of a 3-hydroxyanthranilate 4-methyltransferase.
  JOURNAL   J. Biol. Chem. 263 (1988) 4602-6.
  ORGANISM  Streptomyces antibioticus
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.97
            ExPASy - ENZYME nomenclature database: 2.1.1.97
            ExplorEnz - The Enzyme Database: 2.1.1.97
            ERGO genome analysis and discovery system: 2.1.1.97
            BRENDA, the Enzyme Database: 2.1.1.97
            CAS: 112445-22-4
///
ENTRY       EC 2.1.1.98                 Enzyme
NAME        diphthine synthase;
            S-adenosyl-L-methionine:elongation factor 2 methyltransferase;
            diphthine methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:2-(3-carboxy-3-aminopropyl)-L-histidine
            methyltransferase
REACTION    S-adenosyl-L-methionine + 2-(3-carboxy-3-aminopropyl)-L-histidine =
            S-adenosyl-L-homocysteine +
            2-[3-carboxy-3-(methylammonio)propyl]-L-histidine [RN:R04481]
ALL_REAC    R04481
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            2-(3-carboxy-3-aminopropyl)-L-histidine [CPD:C04441]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            2-[3-carboxy-3-(methylammonio)propyl]-L-histidine [CPD:C04692]
COMMENT     2-[3-Carboxy-3-(methylammonio)propyl]-L-histidine and the
            corresponding dimethyl compound can also act as acceptors; the
            trimethylated product, diphthine, is converted into diphthamide by
            EC 6.3.2.22 diphthine---ammonia ligase.
REFERENCE   1  [PMID:3042777]
  AUTHORS   Chen JY, Bodley JW.
  TITLE     Biosynthesis of diphthamide in Saccharomyces cerevisiae. Partial
            purification and characterization of a specific
            S-adenosylmethionine:elongation factor 2 methyltransferase.
  JOURNAL   J. Biol. Chem. 263 (1988) 11692-6.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:3346227]
  AUTHORS   Moehring JM, Moehring TJ.
  TITLE     The post-translational trimethylation of diphthamide studied in
            vitro.
  JOURNAL   J. Biol. Chem. 263 (1988) 3840-4.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], hamster, mouse [GN:mmu], rat
            [GN:rno], rabbit, human [GN:hsa], monkey, cow [GN:bta], Indian
            muntjak, chicken [GN:gga], newt, gypsy moth, Triticum aestivum
            [GN:etae], Schizophyllum commune
ORTHOLOGY   KO: K00586  diphthine synthase
GENES       HSA: 51611(DPH5)
            MMU: 69740(Dph5)
            CFA: 612092(DPH5)
            GGA: 424463(DPH5)
            XLA: 380263(cgi-30)
            XTR: 448611(MGC89330)
            SPU: 577892(LOC577892)
            DME: Dmel_CG31289(Dph5)
            CEL: B0491.7
            OSA: 4332866
            CME: CMJ181C
            SCE: YLR172C(DPH5)
            AGO: AGOS_AFR123W
            PIC: PICST_78373(DPH5)
            CGR: CAGL0B04961g
            SPO: SPCC576.14
            ANI: AN0720.2
            AFM: AFUA_1G14020
            AOR: AO090012000475
            CNE: CNF03650
            UMA: UM04406.1
            ECU: ECU11_1430
            DDI: DDBDRAFT_0169516
            PFA: PF10_0087
            CPV: cgd6_1200
            CHO: Chro.60154
            TAN: TA03050
            TPV: TP01_0634
            TET: TTHERM_00833850
            TBR: Tb927.4.4650
            TCR: 407477.30 511389.130
            LMA: LmjF31.1610
            EHI: 129.t00009
            MMP: MMP0588(dph5)
            MMQ: MmarC5_1019
            MMZ: MmarC7_1609
            MAE: Maeo_0435
            MVN: Mevan_1459
            MAC: MA1370(dph5)
            MBA: Mbar_A2900
            MMA: MM_2355
            MBU: Mbur_0971
            MTP: Mthe_1120
            MHU: Mhun_0788
            MLA: Mlab_0199
            MEM: Memar_1783
            MBN: Mboo_2068
            MST: Msp_1017(dphB)
            MSI: Msm_0801
            MKA: MK0747(DPH5)
            HAL: VNG1118G(lds)
            HMA: rrnAC1406(dph5)
            HWA: HQ1603A(dph5)
            NPH: NP1884A
            TAC: Ta0883
            TVO: TVN0982
            PTO: PTO1233
            PHO: PH0725
            PAB: PAB1501(dph5)
            PFU: PF0595
            TKO: TK0106
            RCI: RRC519(dphB)
            APE: APE_0931
            SMR: Smar_0509
            IHO: Igni_0657
            SSO: SSO0953
            STO: ST1278
            SAI: Saci_1334
            MSE: Msed_1735
            PAI: PAE1139(dph5)
            PIS: Pisl_1283
            PCL: Pcal_0705
            PAS: Pars_0230
            TPE: Tpen_0689
            NEQ: NEQ422
STRUCTURES  PDB: 1VCE  1VHV  1WDE  1WNG  2DEK  2DSG  2DSH  2DSI  2DV3  2DV4  
                 2DV5  2DV7  2DXV  2DXW  2DXX  2E07  2E08  2E15  2E16  2E17  
                 2E4N  2E4R  2E7R  2E8H  2E8Q  2E8R  2E8S  2ED3  2ED5  2EEQ  
                 2EGB  2EGL  2EGS  2EH2  2EH4  2EH5  2EHC  2EHL  2EJJ  2EJK  
                 2EJZ  2EK2  2EK3  2EK4  2EK7  2EKA  2EL0  2EL1  2EL2  2EL3  
                 2ELD  2ELE  2EMR  2EMU  2EN5  2ENI  2HR8  2HUQ  2HUT  2HUV  
                 2HUX  2OWF  2OWG  2OWK  2OWU  2OWV  2P2X  2P5C  2P5F  2P6D  
                 2P6I  2P6K  2P6L  2P9D  2PB4  2PB5  2PB6  2PCA  2PCG  2PCH  
                 2PCI  2PCK  2PCM  2Z6R  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.98
            ExPASy - ENZYME nomenclature database: 2.1.1.98
            ExplorEnz - The Enzyme Database: 2.1.1.98
            ERGO genome analysis and discovery system: 2.1.1.98
            BRENDA, the Enzyme Database: 2.1.1.98
            CAS: 114514-25-9
///
ENTRY       EC 2.1.1.99                 Enzyme
NAME        3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase;
            16-methoxy-2,3-dihydro-3-hydroxytabersonine methyltransferase;
            NMT;
            16-methoxy-2,3-dihydro-3-hydroxytabersonine N-methyltransferase;
            S-adenosyl-L-methionine:16-methoxy-2,3-dihydro-3-hydroxytabersonine
            N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:3-hydroxy-16-methoxy-2,3-dihydrotabersonine
            N-methyltransferase
REACTION    S-adenosyl-L-methionine +
            3-hydroxy-16-methoxy-2,3-dihydrotabersonine =
            S-adenosyl-L-homocysteine + deacetoxyvindoline [RN:R04013]
ALL_REAC    R04013
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            3-hydroxy-16-methoxy-2,3-dihydrotabersonine
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            deacetoxyvindoline [CPD:C02673]
COMMENT     Involved in the biosynthesis of vindoline from tabersonine in the
            Madagascar periwinkle Catharanthus roseus.
REFERENCE   1  [PMID:16526094]
  AUTHORS   Foucher AL, McIntosh A, Douce G, Wastling J, Tait A, Turner CM.
  TITLE     A proteomic analysis of arsenical drug resistance in Trypanosoma
            brucei.
  JOURNAL   Proteomics. 6 (2006) 2726-32.
REFERENCE   2  [PMID:16526094]
  AUTHORS   Foucher AL, McIntosh A, Douce G, Wastling J, Tait A, Turner CM.
  TITLE     A proteomic analysis of arsenical drug resistance in Trypanosoma
            brucei.
  JOURNAL   Proteomics. 6 (2006) 2726-32.
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.99
            ExPASy - ENZYME nomenclature database: 2.1.1.99
            ExplorEnz - The Enzyme Database: 2.1.1.99
            ERGO genome analysis and discovery system: 2.1.1.99
            BRENDA, the Enzyme Database: 2.1.1.99
            CAS: 113478-40-3
///
ENTRY       EC 2.1.1.100                Enzyme
NAME        protein-S-isoprenylcysteine O-methyltransferase;
            farnesyl cysteine C-terminal methyltransferase;
            farnesyl-protein carboxymethyltransferase;
            protein C-terminal farnesylcysteine O-methyltransferase;
            farnesylated protein C-terminal O-methyltransferase;
            isoprenylated protein methyltransferase;
            prenylated protein methyltransferase;
            protein S-farnesylcysteine C-terminal methyltransferase;
            S-farnesylcysteine methyltransferase;
            prenylcysteine carboxylmethyltransferase [misleading];
            prenylcysteine carboxymethyltransferase [misleading];
            prenylcysteine methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:protein-C-terminal-S-farnesyl-L-cysteine
            O-methyltransferase
REACTION    S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine =
            S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine
            methyl ester [RN:R04496]
ALL_REAC    R04496
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            protein C-terminal S-farnesyl-L-cysteine [CPD:C04506]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            protein C-terminal S-farnesyl-L-cysteine methyl ester [CPD:C04748]
COMMENT     C-terminal S-geranylgeranylcysteine and S-geranylcysteine residues
            are also methylated, but more slowly.
REFERENCE   1  [PMID:3290900]
  AUTHORS   Clarke S, Vogel JP, Deschenes RJ, Stock J.
  TITLE     Posttranslational modification of the Ha-ras oncogene protein:
            evidence for a third class of protein carboxyl methyltransferases.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 4643-7.
  ORGANISM  Tremella mesenterica, Tremella brasiliensis
REFERENCE   2  [PMID:2753892]
  AUTHORS   Ota IM, Clarke S.
  TITLE     Enzymatic methylation of 23-29-kDa bovine retinal rod outer segment
            membrane proteins. Evidence for methyl ester formation at
            carboxyl-terminal cysteinyl residues.
  JOURNAL   J. Biol. Chem. 264 (1989) 12879-84.
  ORGANISM  Tremella mesenterica, Tremella brasiliensis, Saccharomyces
            cerevisiae [GN:sce]
REFERENCE   3  [PMID:2398053]
  AUTHORS   Stephenson RC, Clarke S.
  TITLE     Identification of a C-terminal protein carboxyl methyltransferase in
            rat liver membranes utilizing a synthetic farnesyl
            cysteine-containing peptide substrate.
  JOURNAL   J. Biol. Chem. 265 (1990) 16248-54.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K00587  protein-S-isoprenylcysteine O-methyltransferase
GENES       HSA: 23463(ICMT)
            MMU: 57295(Icmt)
            CFA: 489628(ICMT)
            GGA: 419373(ICMT)
            XLA: 397717(LOC397717)
            SPU: 590850(LOC590850)
            DME: Dmel_CG11268
            CEL: F21F3.3
            ATH: AT5G08335(ATSTE14B) AT5G23320(ATSTE14)
            OSA: 4336894
            CME: CMH202C
            SCE: YDR410C(STE14)
            AGO: AGOS_AAR122C
            PIC: PICST_60928
            CGR: CAGL0F02805g
            SPO: SPAC10F6.12c(mam4)
            ANI: AN6162.2
            AFM: AFUA_2G08420
            AOR: AO090011000860
            CNE: CNC01050
            TBR: Tb09.211.3640
            TCR: 510743.40
            LMA: LmjF35.3030
            EHI: 3.t00074 83.t00023
            XCC: XCC0107
            XCB: XC_0112
            XCV: XCV0113
            XOO: XOO0023
            XOM: XOO_0023(XOO0023)
            ABA: Acid345_1952
            BAY: RBAM_020190(ypbQ)
            LIL: LA2466
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.100
            ExPASy - ENZYME nomenclature database: 2.1.1.100
            ExplorEnz - The Enzyme Database: 2.1.1.100
            ERGO genome analysis and discovery system: 2.1.1.100
            BRENDA, the Enzyme Database: 2.1.1.100
            CAS: 130731-20-3
///
ENTRY       EC 2.1.1.101                Enzyme
NAME        macrocin O-methyltransferase;
            macrocin methyltransferase;
            S-adenosyl-L-methionine-macrocin O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:macrocin 3"'-O-methyltransferase
REACTION    S-adenosyl-L-methionine + macrocin = S-adenosyl-L-homocysteine +
            tylosin [RN:R02858]
ALL_REAC    R02858
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            macrocin [CPD:C00744]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            tylosin [CPD:C01457]
COMMENT     The 3-hydroxy group of a 2-O-methyl-6-deoxy-D-allose residue in the
            macrolide antibiotic macrosin acts as methyl acceptor; also converts
            lactenosin into desmycocin. Not identical with EC 2.1.1.102
            demethylmacrocin O-methyltransferase.
REFERENCE   1  [PMID:3170601]
  AUTHORS   Bauer NJ, Kreuzman AJ, Dotzlaf JE, Yeh WK.
  TITLE     Purification, characterization, and kinetic mechanism of
            S-adenosyl-L-methionine:macrocin O-methyltransferase from
            Streptomyces fradiae.
  JOURNAL   J. Biol. Chem. 263 (1988) 15619-25.
  ORGANISM  Streptomyces fradiae
REFERENCE   2  [PMID:3170602]
  AUTHORS   Kreuzman AJ, Turner JR, Yeh WK.
  TITLE     Two distinctive O-methyltransferases catalyzing penultimate and
            terminal reactions of macrolide antibiotic (tylosin) biosynthesis.
            Substrate specificity, enzyme inhibition, and kinetic mechanism.
  JOURNAL   J. Biol. Chem. 263 (1988) 15626-33.
  ORGANISM  Streptomyces fradiae
ORTHOLOGY   KO: K05303  macrocin O-methyltransferase
GENES       BXE: Bxe_A3043
            MLO: mll2453
            BAN: BA1221
            BAR: GBAA1221
            BAA: BA_1757
            BAT: BAS1129
            BCE: BC1206
            BCA: BCE_1328
            BCZ: BCZK1103(cloP)
            BTK: BT9727_1109(cloP)
            MSM: MSMEG_0388(tylF)
            FRA: Francci3_1291
            FAL: FRAAL2038
            SEN: SACE_0650(cloP)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.101
            ExPASy - ENZYME nomenclature database: 2.1.1.101
            ExplorEnz - The Enzyme Database: 2.1.1.101
            ERGO genome analysis and discovery system: 2.1.1.101
            BRENDA, the Enzyme Database: 2.1.1.101
            CAS: 79468-52-3
///
ENTRY       EC 2.1.1.102                Enzyme
NAME        demethylmacrocin O-methyltransferase;
            demethylmacrocin methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:demethylmacrocin 2"'-O-methyltransferase
REACTION    S-adenosyl-L-methionine + demethylmacrocin =
            S-adenosyl-L-homocysteine + macrocin [RN:R02859]
ALL_REAC    R02859
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            demethylmacrocin [CPD:C02400]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            macrocin [CPD:C00744]
COMMENT     The 2-hydroxy group of a 6-deoxy-D-allose residue in
            demethylmacrocin acts as a methyl acceptor. Not identical with EC
            2.1.1.101 macrocin O-methyltransferase.
REFERENCE   1  [PMID:3170602]
  AUTHORS   Kreuzman AJ, Turner JR, Yeh WK.
  TITLE     Two distinctive O-methyltransferases catalyzing penultimate and
            terminal reactions of macrolide antibiotic (tylosin) biosynthesis.
            Substrate specificity, enzyme inhibition, and kinetic mechanism.
  JOURNAL   J. Biol. Chem. 263 (1988) 15626-33.
  ORGANISM  Streptomyces fradiae
PATHWAY     PATH: map00522  Biosynthesis of 12-, 14- and 16-membered macrolides
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.102
            ExPASy - ENZYME nomenclature database: 2.1.1.102
            ExplorEnz - The Enzyme Database: 2.1.1.102
            ERGO genome analysis and discovery system: 2.1.1.102
            BRENDA, the Enzyme Database: 2.1.1.102
            CAS: 120313-64-6
///
ENTRY       EC 2.1.1.103                Enzyme
NAME        phosphoethanolamine N-methyltransferase;
            phosphoethanolamine methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:ethanolamine-phosphate N-methyltransferase
REACTION    S-adenosyl-L-methionine + ethanolamine phosphate =
            S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
            [RN:R02037]
ALL_REAC    R02037;
            (other) R06868 R06869
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            ethanolamine phosphate [CPD:C00346]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            N-methylethanolamine phosphate [CPD:C01210]
COMMENT     The enzyme may catalyse the transfer of two further methyl groups to
            the product.
REFERENCE   1
  AUTHORS   Datko, A.H. and Mudd, S.H.
  TITLE     Enzymes of phosphatidylcholine synthesis in Lemna, soybean, and
            carrot.
  JOURNAL   Plant Physiol. 88 (1988) 1338-1348.
  ORGANISM  Daucus carota, Glycine max [GN:egma], Lemna paucicostata
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K05929  phosphoethanolamine N-methyltransferase
GENES       PFA: MAL13P1.214
            NOC: Noc_2926
            BPM: BURPS1710b_A0069
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.103
            ExPASy - ENZYME nomenclature database: 2.1.1.103
            ExplorEnz - The Enzyme Database: 2.1.1.103
            ERGO genome analysis and discovery system: 2.1.1.103
            BRENDA, the Enzyme Database: 2.1.1.103
            CAS: 171040-79-2
///
ENTRY       EC 2.1.1.104                Enzyme
NAME        caffeoyl-CoA O-methyltransferase;
            caffeoyl coenzyme A methyltransferase;
            caffeoyl-CoA 3-O-methyltransferase;
            trans-caffeoyl-CoA 3-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:caffeoyl-CoA 3-O-methyltransferase
REACTION    S-adenosyl-L-methionine + caffeoyl-CoA = S-adenosyl-L-homocysteine +
            feruloyl-CoA [RN:R01942]
ALL_REAC    R01942;
            (other) R06578
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            caffeoyl-CoA [CPD:C00323]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            feruloyl-CoA [CPD:C00406]
REFERENCE   1  [PMID:16526012]
  AUTHORS   Saekho S, Yip CY, Noll DC, Boada FE, Stenger VA.
  TITLE     Fast-kz three-dimensional tailored radiofrequency pulse for reduced
            B1 inhomogeneity.
  JOURNAL   Magn. Reson. Med. 55 (2006) 719-24.
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
ORTHOLOGY   KO: K00588  caffeoyl-CoA O-methyltransferase
GENES       ATH: AT4G34050
            OSA: 4340240
            PMY: Pmen_1748
            FTL: FTL_0091
            NOC: Noc_1264
            AEH: Mlg_0966
            MMW: Mmwyl1_2374 Mmwyl1_2598
            BUR: Bcep18194_B2421
            MMR: Mmar10_2832
            SUS: Acid_6458
            BCE: BC2388 BC4378
            BCL: ABC1597
            SGO: SGO_1573
            CTC: CTC01062
            CGL: NCgl0174(cgl0177)
            TFU: Tfu_0966
            FRA: Francci3_3031
            FAL: FRAAL5009
            SEN: SACE_3384
            STP: Strop_0850
            FNU: FN0314
            SYF: Synpcc7942_2505
            AVA: Ava_1652 Ava_2427 Ava_3857
            TER: Tery_2976
STRUCTURES  PDB: 1SUI  1SUS  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.104
            ExPASy - ENZYME nomenclature database: 2.1.1.104
            ExplorEnz - The Enzyme Database: 2.1.1.104
            ERGO genome analysis and discovery system: 2.1.1.104
            BRENDA, the Enzyme Database: 2.1.1.104
            CAS: 120433-42-3
///
ENTRY       EC 2.1.1.105                Enzyme
NAME        N-benzoyl-4-hydroxyanthranilate 4-O-methyltransferase;
            N-benzoyl-4-hydroxyanthranilate 4-methyltransferase;
            benzoyl-CoA:anthranilate N-benzoyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:N-benzoyl-4-O-hydroxyanthranilate
            4-O-methyltransferase
REACTION    S-adenosyl-L-methionine + N-benzoyl-4-hydroxyanthranilate =
            S-adenosyl-L-homocysteine + N-benzoyl-4-methoxyanthranilate
            [RN:R04421]
ALL_REAC    R04421
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            N-benzoyl-4-hydroxyanthranilate [CPD:C04207]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            N-benzoyl-4-methoxyanthranilate
COMMENT     Involved in the biosynthesis of phytoalexins.
REFERENCE   1  [PMID:2817901]
  AUTHORS   Reinhard K, Matern U.
  TITLE     The biosynthesis of phytoalexins in Dianthus caryophyllus L. cell
            cultures: induction of benzoyl-CoA:anthranilate N-benzoyltransferase
            activity.
  JOURNAL   Arch. Biochem. Biophys. 275 (1989) 295-301.
  ORGANISM  Dianthus caryophyllus
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.105
            ExPASy - ENZYME nomenclature database: 2.1.1.105
            ExplorEnz - The Enzyme Database: 2.1.1.105
            ERGO genome analysis and discovery system: 2.1.1.105
            BRENDA, the Enzyme Database: 2.1.1.105
            CAS: 125498-68-2
///
ENTRY       EC 2.1.1.106                Enzyme
NAME        tryptophan 2-C-methyltransferase;
            tryptophan 2-methyltransferase;
            S-adenosylmethionine:tryptophan 2-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:L-tryptophan 2-C-methyltransferase
REACTION    S-adenosyl-L-methionine + L-tryptophan = S-adenosyl-L-homocysteine +
            L-2-methyltryptophan [RN:R00683]
ALL_REAC    R00683
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            L-tryptophan [CPD:C00078]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            L-2-methyltryptophan [CPD:C02983]
COMMENT     D-Tryptophan and (indol-3-yl)pyruvate can also act as acceptors, but
            more slowly.
REFERENCE   1  [PMID:2321967]
  AUTHORS   Frenzel T, Zhou P, Floss HG.
  TITLE     Formation of 2-methyltryptophan in the biosynthesis of thiostrepton:
            isolation of S-adenosylmethionine:tryptophan 2-methyltransferase.
  JOURNAL   Arch. Biochem. Biophys. 278 (1990) 35-40.
  ORGANISM  Streptomyces laurentii
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.106
            ExPASy - ENZYME nomenclature database: 2.1.1.106
            ExplorEnz - The Enzyme Database: 2.1.1.106
            ERGO genome analysis and discovery system: 2.1.1.106
            BRENDA, the Enzyme Database: 2.1.1.106
            CAS: 126626-83-3
///
ENTRY       EC 2.1.1.107                Enzyme
NAME        uroporphyrinogen-III C-methyltransferase;
            uroporphyrinogen methyltransferase;
            uroporphyrinogen-III methyltransferase;
            adenosylmethionine-uroporphyrinogen III methyltransferase;
            S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase;
            uroporphyrinogen-III methylase;
            SirA;
            CysG;
            CobA [ambiguous - see EC 2.5.1.17] SUMT;
            uroporphyrin-III C-methyltransferase (incorrect);
            S-adenosyl-L-methionine:uroporphyrin-III C-methyltransferase
            (incorrect)
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:uroporphyrinogen-III C-methyltransferase
REACTION    (1) S-adenosyl-L-methionine + uroporphyrinogen III =
            S-adenosyl-L-homocysteine + precorrin-1 [RN:R07237];
            (2) S-adenosyl-L-methionine + precorrin-1 =
            S-adenosyl-L-homocysteine + precorrin-2 [RN:R07238]
ALL_REAC    R07237 R07238;
            (other) R03194 R03947 R03950
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            uroporphyrinogen III [CPD:C01051];
            precorrin 1 [CPD:C15527]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            precorrin 1 [CPD:C15527];
            precorrin 2 [CPD:C02463]
COMMENT     This enzyme catalyses two sequential methylation reactions, the
            first forming precorrin-1 and the second leading to the formation of
            precorrin-2. It is the first of three steps leading to the formation
            of siroheme from uroporphyrinogen III. The second step involves an
            NAD+-dependent dehydrogenation to form sirohydrochlorin from
            precorrin-2 (EC 1.3.1.76, precorrin-2 dehydrogenase) and the third
            step involves the chelation of Fe2+ to sirohydrochlorin to form
            siroheme (EC 4.99.1.4, sirohydrochlorin ferrochelatase). In
            Saccharomyces cerevisiae, the last two steps are carried out by a
            single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are
            catalysed by a single multifunctional protein called CysG, whereas
            in Bacillus megaterium, three separate enzymes carry out each of the
            steps, with SirA being responsible for the above reaction. Also
            involved in the biosynthesis of cobalamin.
REFERENCE   1
  AUTHORS   Warren, M.J., Gonzalez, M.D., Williams, H.J., Stolowich, N.J. and
            Scott, A.I.
  TITLE     Uroporphyrinogen-III methylase catalyzes the enzymatic-synthesis of
            sirohydrochlorin-II and sirohydrochlorin-IV by a clockwise
            mechanism.
  JOURNAL   J. Am. Chem. Soc. 112 (1990) 5343-5345.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:2407234]
  AUTHORS   Warren MJ, Roessner CA, Santander PJ, Scott AI.
  TITLE     The Escherichia coli cysG gene encodes
            S-adenosylmethionine-dependent uroporphyrinogen III methylase.
  JOURNAL   Biochem. J. 265 (1990) 725-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:11980703]
  AUTHORS   Schubert HL, Raux E, Brindley AA, Leech HK, Wilson KS, Hill CP,
            Warren MJ.
  TITLE     The structure of Saccharomyces cerevisiae Met8p, a bifunctional
            dehydrogenase and ferrochelatase.
  JOURNAL   EMBO. J. 21 (2002) 2068-75.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K00589  uroporphyrin-III C-methyltransferase
            KO: K02302  uroporphyrin-III C-methyltransferase
            KO: K02496  uroporphyrin-III C-methyltransferase
GENES       DME: Dmel_CG9589
            ATH: AT5G40850(UPM1)
            OSA: 4326671
            CME: CMB055C
            SCE: YKR069W(MET1)
            AGO: AGOS_AGR298C
            PIC: PICST_31820(MET1) PICST_63116(MET8)
            CAL: CaO19_5811(CaO19.5811)
            CGR: CAGL0G01903g
            SPO: SPCC1739.06c
            ANI: AN4774.2
            AFM: AFUA_3G06600
            AOR: AO090020000339
            ECO: b3368(cysG) b3803(hemX)
            ECJ: JW3331(cysG) JW3775(hemX)
            ECE: Z4729(cysG) Z5317(hemX)
            ECS: ECs4219 ECs4733
            ECC: c4144(cysG) c4722(hemX)
            ECI: UTI89_C3872(cysG) UTI89_C4362(hemX)
            ECP: ECP_3459 ECP_3995
            ECV: APECO1_2675(hemX) APECO1_3088(cysG)
            ECW: EcE24377A_3838(cysG)
            ECX: EcHS_A3564(cysG)
            STY: STY3623(hemX) STY4319(cysG)
            STT: t3361(hemX) t4028(cysG)
            SPT: SPA3343(cysG) SPA3777(hemX)
            SEC: SC3411(cysG) SC3837(hemX)
            STM: STM3477(cysG) STM3936(hemX)
            YPE: YPO0158(cysG) YPO3367(cysG) YPO3851(hemX)
            YPK: y0379(hemX) y3941(cysG)
            YPM: YP_0160(cysG1)
            YPA: YPA_0170 YPA_2776 YPA_3311
            YPN: YPN_0112 YPN_0726 YPN_3907
            YPS: YPTB0182(hemX) YPTB0764(cysG) YPTB3743(cysG)
            YPI: YpsIP31758_3305(cysG2) YpsIP31758_3959(cysG1)
            YEN: YE4038(cobA)
            SFL: SF3387(cysG) SF3875(hemX)
            SFX: S3881(hemX) S4376(cysG)
            SFV: SFV_3374(cysG) SFV_3699(hemX)
            SSN: SSON_3499(cysG) SSON_3975(hemX)
            SBO: SBO_3350(cysG) SBO_3814(hemX)
            SDY: SDY_3530(cysG) SDY_3943(hemX)
            ECA: ECA2989(nirE) ECA3544(cysG1) ECA4081(cysG2) ECA4190(hemX)
            PLU: plu0708(cysG) plu2968 plu4646(hemX)
            BUC: BU425(cysG)
            SGL: SG0520 SG2368
            BFL: Bfl161(cysG)
            BPN: BPEN_166(cysG)
            HIT: NTHI0858(hemX)
            HDU: HD1741(hemX)
            HSO: HS_0046(hemX)
            PMU: PM1814
            MSU: MS0274(hemX) MS1254(cysG)
            APL: APL_1008(hemX)
            XFA: XF0832 XF1798
            XFT: PD1069 PD1840(cysG)
            XCC: XCC0197 XCC2010(cysG) XCC3181(cysG)
            XCB: XC_0207 XC_0983 XC_2174
            XCV: XCV0200 XCV2096 XCV3458(cysG)
            XAC: XAC0215 XAC2157(cysG) XAC3340(cysG)
            XOO: XOO3408(cysG) XOO4087
            XOM: XOO_3208(XOO3208) XOO_3861(XOO3861)
            VCH: VC0118 VC2561
            VCO: VC0395_A2138(cysG)
            VVU: VV1_0727 VV1_1120 VV2_0367 VV2_0397
            VVY: VV0079 VV0410 VVA0924 VVA0956
            VPA: VP0291 VP2990 VPA0984 VPA1064
            VFI: VF0064 VF0773
            PPR: PBPRA1425 PBPRA2524 PBPRA3312 PBPRA3530
            PAE: PA0510 PA1778(cobA) PA2611(cysG) PA5258
            PAU: PA14_06660(nirE) PA14_41563(cobA) PA14_69430(hemX)
            PPU: PP_0188 PP_2090(cobA-1) PP_3999(cobA-2)
            PST: PSPTO_0130 PSPTO_2300(cobA) PSPTO_3344(cysG)
            PSB: Psyr_0060 Psyr_2098 Psyr_3174
            PSP: PSPPH_0065 PSPPH_2069(cobA) PSPPH_3088(cysG)
            PFL: PFL_3875 PFL_6000
            PFO: Pfl_1778 Pfl_3581 Pfl_5485(hemX)
            PEN: PSEEN2217(cysG) PSEEN5351
            PAR: Psyc_1065(cysG) Psyc_1909
            ACI: ACIAD2934(cysG)
            SON: SO_3728(cobA) SO_4315(hemX)
            SDN: Sden_0386 Sden_0958 Sden_3717
            SFR: Sfri_0438 Sfri_1506 Sfri_3188
            SHE: Shewmr4_0386 Shewmr4_3073
            SHM: Shewmr7_0899 Shewmr7_3640
            SHN: Shewana3_0384 Shewana3_0862
            CPS: CPS_0072(hemX) CPS_1126(cobA1) CPS_4228(cobA2)
            PHA: PSHAa0099(hemDX) PSHAa0213(cysG)
            PAT: Patl_0340 Patl_0417
            SDE: Sde_3665
            CBU: CBU_2080
            LPN: lpg2737
            LPF: lpl2662(hemX)
            LPP: lpp2793(hemX)
            MCA: MCA2089(cysG) MCA3061(hemDX)
            TCX: Tcr_1160
            NOC: Noc_0863
            AEH: Mlg_1679 Mlg_2668
            HCH: HCH_00289(hemX) HCH_02450(cysG)
            CSA: Csal_3107
            ABO: ABO_1295(cysG) ABO_2320(hemX)
            AHA: AHA_0467 AHA_2578 AHA_3413(cobA) AHA_3568 AHA_4121
            BCI: BCI_0215(cysG)
            VOK: COSY_0254(cysG)
            NME: NMB0778 NMB1156 NMB1194
            NMA: NMA0989 NMA1367(cysG)
            NMC: NMC1096(cysG)
            NGO: NGO0360
            CVI: CV_0051(hemX) CV_0813(cobA2) CV_1569(cobA1)
            RSO: RSc2356(RS01190) RSc2420(nirE)
            REU: Reut_A0701(hemX) Reut_A2691 Reut_B5019
            REH: H16_A2919(hemXD) H16_A2994(cysG) H16_B2285(nirE)
            RME: Rmet_2748 Rmet_2811 Rmet_3168
            BMA: BMA0668(cobA-1) BMA0731 BMAA1089(cobA-2)
            BMV: BMASAVP1_0086(cobA-2) BMASAVP1_A2343(cobA-1)
            BML: BMA10299_0334(cobA-2) BMA10299_A2942(cobA-1)
            BMN: BMA10247_1657(cobA-1) BMA10247_A1254(cobA-2)
            BXE: Bxe_A2215 Bxe_A3410 Bxe_A3659 Bxe_B1649
            BUR: Bcep18194_A4802 Bcep18194_A5801 Bcep18194_B1341
            BCN: Bcen_1174 Bcen_3859
            BCH: Bcen2424_1654 Bcen2424_4509
            BAM: Bamb_1554 Bamb_2519
            BPS: BPSL0961 BPSL1016 BPSS1245
            BPM: BURPS1710b_1171(cobA) BURPS1710b_1231(hemX)
                 BURPS1710b_A0245(cobA-2)
            BPL: BURPS1106A_1018(cobA) BURPS1106A_A1669(cobA)
            BPD: BURPS668_1011(cobA) BURPS668_A1758(cobA)
            BTE: BTH_I0819(cobA-1) BTH_I0873 BTH_II1168(cobA-2)
            BPE: BP1055(cysG) BP2535
            BPA: BPP1151(cysG) BPP2644
            BBR: BB1367(cysG) BB2087
            RFR: Rfer_1717 Rfer_2883
            POL: Bpro_2765 Bpro_3281
            PNA: Pnap_1402
            AAV: Aave_2103
            AJS: Ajs_2843
            VEI: Veis_2292
            MPT: Mpe_A1498 Mpe_A2321
            HAR: HEAR0437(cysG) HEAR2397
            MMS: mma_0487(cobA) mma_0979 mma_1144(hemX) mma_2457(cysG)
            NEU: NE0532(cysG) NE0592 NE1403
            NET: Neut_1002 Neut_1039
            NMU: Nmul_A2313 Nmul_A2688
            EBA: ebA1162(nirE) ebA4025(cysG) ebA885(cysG)
            AZO: azo0945(cobA1) azo0995(hemX) azo3551(cobA2)
            DAR: Daro_3275 Daro_3672(hemX)
            TBD: Tbd_2471 Tbd_2566
            MFA: Mfla_0033 Mfla_0322 Mfla_0652
            WSU: WS1003(cysG)
            TDN: Tmden_1989
            ABU: Abu_0365(cysG)
            GSU: GSU3286
            GME: Gmet_3235
            PCA: Pcar_3062
            DVU: DVU0734
            DDE: Dde_2837
            LIP: LI0117(cysG)
            DPS: DP1734(hemD)
            ADE: Adeh_3154
            MXA: MXAN_2338(cobA)
            SAT: SYN_02272
            SFU: Sfum_3201
            MLO: mll3232 mlr1386
            MES: Meso_3989
            SME: SMb20987 SMc01053(cysG) SMc04284(cobA)
            ATU: Atu1454(cysG) Atu2794(cobA) Atu3899(cysG)
            ATC: AGR_C_2683 AGR_C_5071(uroM) AGR_L_1897
            RET: RHE_CH01958(cysG) RHE_CH02484(cobA)
            RLE: RL2288(cysG2) RL2824(cobA) pRL120460
            BME: BMEI0704 BMEI1768 BMEII0787
            BMF: BAB1_0179(cysG) BAB1_1317
            BMS: BR0179(cysG) BR1297(cobA)
            BMB: BruAb1_0175(cysG) BruAb1_1298(cobA) BruAb2_0745
            BOV: BOV_1260(cobA)
            BJA: blr1477 blr3273(cobA)
            BRA: BRADO1065(cysG)
            BBT: BBta_6982(cysG)
            RPA: RPA2082(cobA) RPA4215(cysG)
            RPB: RPB_1399 RPB_3186
            RPC: RPC_1880 RPC_4015
            RPD: RPD_1379 RPD_2312
            RPE: RPE_1763 RPE_2217
            NWI: Nwi_2762
            CCR: CC_0618 CC_1118
            SIL: SPO2632(cobA-1) SPO2873(cobA-2) SPOA0221(nirE)
            SIT: TM1040_1756 TM1040_2220
            RSP: RSP_1944 RSP_2820(cobA)
            RDE: RD1_1566(nirE) RD1_2964(cysG) RD1_3817(cobA) RD1_4164(cysG)
            MMR: Mmar10_0347
            HNE: HNE_0322(cysG) HNE_2230(cobA)
            ZMO: ZMO0006(cysG) ZMO1271(cysG)
            NAR: Saro_2556
            SAL: Sala_0772
            ELI: ELI_01890
            GOX: GOX2065
            GBE: GbCGDNIH1_0735
            RRU: Rru_A1933 Rru_A3362
            MAG: amb0515 amb1400 amb3363
            MGM: Mmc1_2225
            BSU: BG11098(nasF) BG13380(ylnD)
            BHA: BH1495
            BAN: BA1445(cysG) BA2144
            BAR: GBAA1445(cysG) GBAA2144
            BAA: BA_1966 BA_2640
            BAT: BAS1335 BAS1995
            BCE: BC1426 BC2134
            BCA: BCE_1549(cysG)
            BCZ: BCZK0032 BCZK1309(cysG) BCZK1947
            BTK: BT9727_1308(cysG) BT9727_1968
            BTL: BALH_0032(cobA)
            BLI: BL01771(nasF) BL02286(cysG)
            BLD: BLi00486(nasF) BLi01782(ylnD)
            BCL: ABC0615 ABC0617 ABC1620(nasF)
            BAY: RBAM_003490
            BPU: BPUM_1460(cysG)
            OIH: OB1655
            GKA: GK0413 GK1792
            SAU: SA2186(nasF)
            SAV: SAV2398(nasF)
            SAM: MW2320(nasF)
            SAR: SAR2487
            SAS: SAS2289
            SAC: SACOL2396
            SAB: SAB2278c
            SAA: SAUSA300_2344
            SAO: SAOUHSC_02682
            SEP: SE1976 SE2178
            SER: SERP1988 SERP2189
            SHA: SH0416 SH0653(nasF)
            SSP: SSP2406
            LMO: lmo1201
            LMF: LMOf2365_1210
            LIN: lin1164
            LWE: lwe1158(hemD)
            SSA: SSA_0474
            CAC: CAC0098(hemD)
            CPE: CPE1434(hemX)
            CPF: CPF_1687(hemD)
            CPR: CPR_1421(hemD)
            CTC: CTC00728
            CNO: NT01CX_0261
            CDF: CD3420(hemD)
            CBO: CBO0921(hemD)
            CBA: CLB_0962(cobA)
            CBH: CLC_0976(cobA)
            CBF: CLI_1008(cobA)
            CHY: CHY_0778(cobA) CHY_2407
            DSY: DSY2224
            MTA: Moth_1248
            MTU: Rv0511(hemD) Rv2847c(cysG)
            MTC: MT0532 MT2913(cysG)
            MBO: Mb0524(hemD) Mb2872c(cysG)
            MBB: BCG_0554(hemD) BCG_2867c(cysG)
            MLE: ML2420(hemD)
            MPA: MAP2916c(cysG2) MAP4004(cysG)
            MAV: MAV_3703(cobA)
            MSM: MSMEG_2618(cobA)
            MMC: Mmcs_2074
            CGL: NCgl0414(cgl0429) NCgl1923(cgl1998)
            CGB: cg0510(hemD) cg0918
            CEF: CE0450 CE1892
            CDI: DIP0402 DIP1484
            CJK: jk1149(cobA) jk1900(hemD)
            NFA: nfa40770(cysG) nfa51680(hemDX)
            RHA: RHA1_ro02051 RHA1_ro06617
            SCO: SCO1553(SCL11.09c) SCO3317(SCE68.15c)
            SMA: SAV4741(hemD) SAV6796(cysG)
            AAU: AAur_1397(cobA) AAur_3076(cobA)
            PAC: PPA0323 PPA0439
            TFU: Tfu_2221 Tfu_2731
            FRA: Francci3_0487 Francci3_0528 Francci3_0796
            FAL: FRAAL0985(hemD) FRAAL1020(corA) FRAAL1357(cysG)
            ACE: Acel_0236
            SEN: SACE_5957 SACE_6944(hemD)
            FNU: FN0644
            RBA: RB7020(hemD)
            CTR: CT433
            CTA: CTA_0473
            CMU: TC0717
            CPN: CPn0522
            CPA: CP0231
            CPJ: CPj0522
            CPT: CpB0543
            CCA: CCA00223
            CAB: CAB219
            CFE: CF0783
            LIL: LA4218(cysG)
            LIC: LIC13369(cobA)
            LBJ: LBJ_2839
            LBL: LBL_0232
            SYN: sll0166(cobA/hemD) sll0378(cobA)
            SYW: SYNW2475(cobA)
            SYC: syc1242_c(cobA) syc1500_d(cobA)
            SYF: Synpcc7942_0271 Synpcc7942_2610
            SYD: Syncc9605_2654
            SYE: Syncc9902_2282
            SYG: sync_2896(cobA)
            SYR: SynRCC307_2479(cobA)
            SYX: SynWH7803_2489(cobA)
            CYA: CYA_0529(cobA) CYA_0929(cobA)
            CYB: CYB_0566(cobA) CYB_1040(cobA)
            TEL: tlr0144(cobA) tlr2155(cobA/hemD)
            GVI: glr1234(cobA/hemD) glr2580(cobA)
            ANA: alr0520(cobA) alr3450(cobA/hemD)
            AVA: Ava_2922 Ava_3474
            PMA: Pro1858(cysG)
            PMM: PMM1694(cobA)
            PMT: PMT2237(cobA)
            PMN: PMN2A_1296
            PMI: PMT9312_1787
            PMB: A9601_19041(cysG)
            PMC: P9515_18851(cysG)
            PMF: P9303_29821(cysG)
            PMG: P9301_18851(cysG)
            PME: NATL1_21681(cysG)
            TER: Tery_1175 Tery_3325
            CHU: CHU_2635(cysG) CHU_2636(cysG)
            GFO: GFO_0328(corA) GFO_0628 GFO_3356
            CTE: CT0390(cobA) CT1763 CT2238
            CCH: Cag_1942
            PLT: Plut_0050
            DRA: DR_A0011
            DGE: Dgeo_2131
            TTH: TTC0308 TT_P0017
            TTJ: TTHA0667 TTHB060
            AAE: aq_207(cobA)
            MJA: MJ0965(cobA)
            MMP: MMP0966(cobA)
            MAC: MA3033
            MBA: Mbar_A1791
            MMA: MM_0307
            MBU: Mbur_1105
            MHU: Mhun_2558
            MTH: MTH167
            MSI: Msm_1550
            MKA: MK1548(cysG_2)
            AFU: AF0422(cysG-1) AF1243(cysG-2)
            HAL: VNG2331G(uroM)
            HMA: rrnAC3087(cysG2)
            HWA: HQ3451A(hemX)
            NPH: NP1328A(hemX)
            TAC: Ta0653
            TVO: TVN0923
            PTO: PTO1435
            RCI: RCIX915(cysG)
            APE: APE_0236.1
            HBU: Hbut_0835
            SSO: SSO2435(cobA) SSO2908(cysG)
            STO: ST0563
            SAI: Saci_0914 Saci_2200(uroM)
            PAI: PAE0590
STRUCTURES  PDB: 1PJQ  1PJS  1PJT  1S4D  1V9A  1VA0  1VE2  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.107
            ExPASy - ENZYME nomenclature database: 2.1.1.107
            ExplorEnz - The Enzyme Database: 2.1.1.107
            ERGO genome analysis and discovery system: 2.1.1.107
            BRENDA, the Enzyme Database: 2.1.1.107
            CAS: 73665-99-3
///
ENTRY       EC 2.1.1.108                Enzyme
NAME        6-hydroxymellein O-methyltransferase;
            6-hydroxymellein methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:6-hydroxymellein 6-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 6-hydroxymellein =
            S-adenosyl-L-homocysteine + 6-methoxymellein [RN:R03934]
ALL_REAC    R03934
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            6-hydroxymellein [CPD:C02379]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            6-methoxymellein [CPD:C02381]
COMMENT     3,4-Dehydro-6-hydroxymellein can also act as acceptor.
            6-Methoxymellein is a phytoalexin produced by carrot tissue.
REFERENCE   1
  AUTHORS   Kurosaki, F. and Nishi, A.
  TITLE     A methyltransferase for synthesis of the phytoalexin
            6-methoxymellein in carrot cells.
  JOURNAL   FEBS Lett. 227 (1988) 183-186.
  ORGANISM  Daucus carota
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.108
            ExPASy - ENZYME nomenclature database: 2.1.1.108
            ExplorEnz - The Enzyme Database: 2.1.1.108
            ERGO genome analysis and discovery system: 2.1.1.108
            BRENDA, the Enzyme Database: 2.1.1.108
            CAS: 124149-02-6
///
ENTRY       EC 2.1.1.109                Enzyme
NAME        demethylsterigmatocystin 6-O-methyltransferase;
            demethylsterigmatocystin methyltransferase;
            O-methyltransferase I
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:6-demethylsterigmatocystin
            6-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 6-demethylsterigmatocystin =
            S-adenosyl-L-homocysteine + sterigmatocystin [RN:R03112]
ALL_REAC    R03112
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            6-demethylsterigmatocystin [CPD:C03683]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            sterigmatocystin [CPD:C00961]
COMMENT     Dihydrodemethylsterigmatocystin can also act as acceptor. Involved
            in the biosynthesis of aflatoxins in fungi.
REFERENCE   1  [PMID:2802602]
  AUTHORS   Yabe K, Ando Y, Hashimoto J, Hamasaki T.
  TITLE     Two distinct O-methyltransferases in aflatoxin biosynthesis.
  JOURNAL   Appl. Environ. Microbiol. 55 (1989) 2172-7.
  ORGANISM  Aspergillus parasiticus
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.109
            ExPASy - ENZYME nomenclature database: 2.1.1.109
            ExplorEnz - The Enzyme Database: 2.1.1.109
            ERGO genome analysis and discovery system: 2.1.1.109
            BRENDA, the Enzyme Database: 2.1.1.109
            CAS: 123516-47-2
///
ENTRY       EC 2.1.1.110                Enzyme
NAME        sterigmatocystin 8-O-methyltransferase;
            sterigmatocystin methyltransferase;
            O-methyltransferase II;
            sterigmatocystin 7-O-methyltransferase (incorrect);
            S-adenosyl-L-methionine:sterigmatocystin 7-O-methyltransferase
            (incorrect)
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:sterigmatocystin 8-O-methyltransferase
REACTION    S-adenosyl-L-methionine + sterigmatocystin =
            S-adenosyl-L-homocysteine + 8-O-methylsterigmatocystin [RN:R03111]
ALL_REAC    R03111
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            sterigmatocystin [CPD:C00961]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            8-O-methylsterigmatocystin [CPD:C03686]
COMMENT     Dihydrosterigmatocystin can also act as acceptor. Involved in the
            biosynthesis of aflatoxins in fungi.
REFERENCE   1  [PMID:3111363]
  AUTHORS   Bhatnagar D, McCormick SP, Lee LS, Hill RA.
  TITLE     Identification of O-methylsterigmatocystin as an aflatoxin B1 and G1
            precursor in Aspergillus parasiticus.
  JOURNAL   Appl. Environ. Microbiol. 53 (1987) 1028-33.
  ORGANISM  Aspergillus parasiticus
REFERENCE   2  [PMID:2802602]
  AUTHORS   Yabe K, Ando Y, Hashimoto J, Hamasaki T.
  TITLE     Two distinct O-methyltransferases in aflatoxin biosynthesis.
  JOURNAL   Appl. Environ. Microbiol. 55 (1989) 2172-7.
  ORGANISM  Aspergillus parasiticus
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.110
            ExPASy - ENZYME nomenclature database: 2.1.1.110
            ExplorEnz - The Enzyme Database: 2.1.1.110
            ERGO genome analysis and discovery system: 2.1.1.110
            BRENDA, the Enzyme Database: 2.1.1.110
            CAS: 116958-29-3
///
ENTRY       EC 2.1.1.111                Enzyme
NAME        anthranilate N-methyltransferase;
            anthranilic acid N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:anthranilate N-methyltransferase
REACTION    S-adenosyl-L-methionine + anthranilate = S-adenosyl-L-homocysteine +
            N-methylanthranilate [RN:R00984]
ALL_REAC    R00984
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            anthranilate [CPD:C00108]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            N-methylanthranilate [CPD:C03005]
COMMENT     Involved in the biosynthesis of acridine alkaloids in plant tissues.
REFERENCE   1
  AUTHORS   Eilert, U. and Wolters, B.
  TITLE     Elicitor induction of S-adenosyl-L-methionine-anthranilic acid
            N-methyltransferase activity in cell-suspension and organ-cultures
            of Ruta graveolens L.
  JOURNAL   Plant Cell, Tissue Organ Cult. 18 (1989) 1-18.
  ORGANISM  Ruta graveolens
PATHWAY     PATH: map01058  Acridone alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.111
            ExPASy - ENZYME nomenclature database: 2.1.1.111
            ExplorEnz - The Enzyme Database: 2.1.1.111
            ERGO genome analysis and discovery system: 2.1.1.111
            BRENDA, the Enzyme Database: 2.1.1.111
            CAS: 123779-15-7
///
ENTRY       EC 2.1.1.112                Enzyme
NAME        glucuronoxylan 4-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:glucuronoxylan-D-glucuronate
            4-O-methyltransferase
REACTION    S-adenosyl-L-methionine + glucuronoxylan D-glucuronate =
            S-adenosyl-L-homocysteine + glucuronoxylan 4-O-methyl-D-glucuronate
            [RN:R04332]
ALL_REAC    R04332
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            glucuronoxylan D-glucuronate [CPD:C03866]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            glucuronoxylan 4-O-methyl-D-glucuronate [CPD:C04459]
REFERENCE   1
  AUTHORS   Baydoun, E.A.-H., Usta, J.A.-R., Waldron, K.W. and Brett, C.T.
  TITLE     A methyltransferase involved in the biosynthesis of
            4-O-methylglucuronoxylan in etiolated pea epicotyls.
  JOURNAL   J. Plant Physiol. 135 (1989) 81-85.
  ORGANISM  Pisum sativum
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.112
            ExPASy - ENZYME nomenclature database: 2.1.1.112
            ExplorEnz - The Enzyme Database: 2.1.1.112
            ERGO genome analysis and discovery system: 2.1.1.112
            BRENDA, the Enzyme Database: 2.1.1.112
            CAS: 123644-79-1
///
ENTRY       EC 2.1.1.113                Enzyme
NAME        site-specific DNA-methyltransferase (cytosine-N4-specific);
            modification methylase;
            restriction-modification system;
            DNA[cytosine-N4]methyltransferase;
            m4C-forming MTase;
            S-adenosyl-L-methionine:DNA-cytosine 4-N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:DNA-cytosine N4-methyltransferase
REACTION    S-adenosyl-L-methionine + DNA cytosine = S-adenosyl-L-homocysteine +
            DNA N4-methylcytosine [RN:R03003]
ALL_REAC    R03003
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            DNA cytosine [CPD:C00856]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            DNA N4-methylcytosine [CPD:C03110]
COMMENT     This is a large group of enzymes, most of which, with enzymes of
            similar site specificity listed as EC 3.1.21.3 (type 1 site-specific
            deoxyribonuclease), EC 3.1.21.4 (type II site-specific
            deoxyribonuclease) or EC 3.1.21.5 (type III site-specific
            deoxyribonuclease), form so-called 'restriction-modification
            systems'. A complete listing of all of these enzymes has been
            produced by R.J. Roberts and is available on-line at
            http://rebase.neb.com/rebase/rebase.html.
REFERENCE   1  [PMID:2172084]
  AUTHORS   Kessler C, Manta V.
  TITLE     Specificity of restriction endonucleases and DNA modification
            methyltransferases a review (Edition 3).
  JOURNAL   Gene. 92 (1990) 1-248.
REFERENCE   2  [PMID:2690010]
  AUTHORS   Klimasauskas S, Timinskas A, Menkevicius S, Butkiene D, Butkus V,
            Janulaitis A.
  TITLE     Sequence motifs characteristic of
            DNA[cytosine-N4]methyltransferases: similarity to adenine and
            cytosine-C5 DNA-methylases.
  JOURNAL   Nucleic. Acids. Res. 17 (1989) 9823-32.
  ORGANISM  Micrococcus varians, Citrobacter freundii
REFERENCE   3  [PMID:2159140]
  AUTHORS   Roberts RJ.
  TITLE     Restriction enzymes and their isoschizomers.
  JOURNAL   Nucleic. Acids. Res. 18 Suppl (1990) 2331-65.
REFERENCE   4  [PMID:6267988]
  AUTHORS   Yuan R.
  TITLE     Structure and mechanism of multifunctional restriction
            endonucleases.
  JOURNAL   Annu. Rev. Biochem. 50 (1981) 285-319.
ORTHOLOGY   KO: K00590  site-specific DNA-methyltransferase
                        (cytosine-N4-specific)
GENES       XCV: XCV1110
            BPM: BURPS1710b_1670
            BTE: BTH_II1029
            HPY: HP1368(mod)
            HAC: Hac_0185
            CJD: JJD26997_1650
            GBE: GbCGDNIH1_2326
            SGO: SGO_0640
            FRA: Francci3_2345
            LIL: LA1547
            ANA: all3632(avaIM)
            AVA: Ava_3014 Ava_3181
            CCH: Cag_1099
            MJA: MJ0985 MJ1448 MJ1498
            HAL: VNG1543G(zim)
            HMA: rrnAC1876(zim)
            RCI: RCIX2329(zim)
            SAI: Saci_1975
STRUCTURES  PDB: 1BOO  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.113
            ExPASy - ENZYME nomenclature database: 2.1.1.113
            ExplorEnz - The Enzyme Database: 2.1.1.113
            ERGO genome analysis and discovery system: 2.1.1.113
            BRENDA, the Enzyme Database: 2.1.1.113
///
ENTRY       EC 2.1.1.114                Enzyme
NAME        hexaprenyldihydroxybenzoate methyltransferase;
            3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase;
            dihydroxyhexaprenylbenzoate methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:3-hexaprenyl-4,5-dihydroxylate
            O-methyltransferase
REACTION    S-adenosyl-L-methionine + 3-hexaprenyl-4,5-dihydroxybenzoate =
            S-adenosyl-L-homocysteine + 3-hexaprenyl-4-hydroxy-5-methoxybenzoate
            [RN:R04711]
ALL_REAC    R04711;
            (other) R02175
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            3-hexaprenyl-4,5-dihydroxybenzoate [CPD:C05200]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            3-hexaprenyl-4-hydroxy-5-methoxybenzoate [CPD:C05313]
COMMENT     Involved in the pathway of ubiquinone synthesis. This enzyme has
            been listed as EC 2.1.1.64 3-demethylubiquinone-9
            3-O-methyltransferase in some sequence databases; but that enzyme
            catalyses a different reaction.
REFERENCE   1  [PMID:1885593]
  AUTHORS   Clarke CF, Williams W, Teruya JH.
  TITLE     Ubiquinone biosynthesis in Saccharomyces cerevisiae. Isolation and
            sequence of COQ3, the 3,4-dihydroxy-5-hexaprenylbenzoate
            methyltransferase gene.
  JOURNAL   J. Biol. Chem. 266 (1991) 16636-44.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00130  Ubiquinone biosynthesis
ORTHOLOGY   KO: K00591  hexaprenyldihydroxybenzoate methyltransferase
GENES       HSA: 51805(COQ3)
            PTR: 472079(COQ3)
            MMU: 230027(Coq3)
            RNO: 29309(Coq3)
            CFA: 475004(COQ3)
            GGA: 421797(COQ3)
            DME: Dmel_CG9249
            OSA: 4340157
            CME: CMI016C
            SCE: YOL096C(COQ3)
            AGO: AGOS_ADR115W
            PIC: PICST_31991(COQ3)
            CAL: CaO19_3400(CaO19.3400)
            CGR: CAGL0I07601g
            SPO: SPCC162.05
            DDI: DDB_0231592(coq3)
            CHO: Chro.20298
            TAN: TA11825
            TPV: TP02_0197
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.114
            ExPASy - ENZYME nomenclature database: 2.1.1.114
            ExplorEnz - The Enzyme Database: 2.1.1.114
            ERGO genome analysis and discovery system: 2.1.1.114
            BRENDA, the Enzyme Database: 2.1.1.114
            CAS: 139569-30-5
///
ENTRY       EC 2.1.1.115                Enzyme
NAME        (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase;
            norreticuline N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline
            N-methyltransferase
REACTION    S-adenosyl-L-methionine +
            (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline =
            S-adenosyl-L-homocysteine +
            N-methyl-(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline [RN:R04713]
ALL_REAC    R04713;
            (other) R04692 R05211 R05216
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline [CPD:C05201]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            N-methyl-(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline [CPD:C05314]
COMMENT     Broad substrate specificity for
            (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinolines; including coclaurine,
            norcoclaurine, isococlaurine, norarmepavine, norreticuline and
            tetrahydropapaverine. Both R- and S-enantiomers are methylated. The
            enzyme participates in the pathway leading to benzylisoquinoline
            alkaloid synthesis in plants. The physiological substrate is likely
            to be coclaurine. The enzyme was earlier termed norreticuline
            N-methyltransferase. However, norreticuline has not been found to
            occur in nature and that name does not reflect the broad specificity
            of the enzyme for (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinolines.
REFERENCE   1
  AUTHORS   Frenzel, T., Zenk, M.H.
  TITLE     Purification and characterization of three isoforms of
            S-adenosyl-L-methionine: (R,S)-tetrahydrobenzyl-isoquinoline
            N-methyltransferase from Berberis koetineana cell cultures.
  JOURNAL   Phytochemistry 29 (1990) 3491-3497.
  ORGANISM  Berberis koetineana
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.115
            ExPASy - ENZYME nomenclature database: 2.1.1.115
            ExplorEnz - The Enzyme Database: 2.1.1.115
            ERGO genome analysis and discovery system: 2.1.1.115
            BRENDA, the Enzyme Database: 2.1.1.115
            CAS: 132084-82-3
///
ENTRY       EC 2.1.1.116                Enzyme
NAME        3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:3'-hydroxy-N-methyl-(S)-coclaurine
            4'-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 3'-hydroxy-N-methyl-(S)-coclaurine =
            S-adenosyl-L-homocysteine + (S)-reticuline [RN:R03832]
ALL_REAC    R03832;
            (other) R05212
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            3'-hydroxy-N-methyl-(S)-coclaurine [CPD:C05202]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            (S)-reticuline [CPD:C02105]
COMMENT     Involved in isoquinoline alkaloid metabolism in plants. The enzyme
            has also been shown to catalyse the methylation of
            (RS)-laudanosoline, (S)-3'-hydroxycoclaurine and
            (RS)-7-O-methylnorlaudanosoline.
REFERENCE   1
  AUTHORS   Frenzel, T., Zenk, M.H.
  TITLE     S-Adenosyl-L-methionine: 3'-hydroxy-N-methyl-(S)-coclaurine
            4'-O-methyltransferase, a regio- and stereoselective enzyme of the
            (S)-reticuline pathway.
  JOURNAL   Phytochemistry 29 (1990) 3505-3511.
  ORGANISM  Berberis koetineuna
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.116
            ExPASy - ENZYME nomenclature database: 2.1.1.116
            ExplorEnz - The Enzyme Database: 2.1.1.116
            ERGO genome analysis and discovery system: 2.1.1.116
            BRENDA, the Enzyme Database: 2.1.1.116
            CAS: 132084-81-2
///
ENTRY       EC 2.1.1.117                Enzyme
NAME        (S)-scoulerine 9-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:(S)-scoulerine 9-O-methyltransferase
REACTION    S-adenosyl-L-methionine + (S)-scoulerine = S-adenosyl-L-homocysteine
            + (S)-tetrahydrocolumbamine [RN:R03835]
ALL_REAC    R03835
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            (S)-scoulerine [CPD:C02106]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            (S)-tetrahydrocolumbamine [CPD:C04118]
COMMENT     The product of this reaction is a precursor for protoberberine
            alkaloids in plants
REFERENCE   1
  AUTHORS   Muemmler, S., Rueffer, M., Nagakura, N., Zenk, M.H.
  TITLE     S-Adenosyl-L-methionine:(S)-scoulerine 9-O-methyltransferase, a
            highly stereo- and regiospecific enzyme in tetrahydroberberine
            biosynthesis.
  JOURNAL   Plant Cell Reports 4 (1985) 36-39.
  ORGANISM  Berberis wilsoniae
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.117
            ExPASy - ENZYME nomenclature database: 2.1.1.117
            ExplorEnz - The Enzyme Database: 2.1.1.117
            ERGO genome analysis and discovery system: 2.1.1.117
            BRENDA, the Enzyme Database: 2.1.1.117
///
ENTRY       EC 2.1.1.118                Enzyme
NAME        columbamine O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:columbamine O-methyltransferase
REACTION    S-adenosyl-L-methionine + columbamine = S-adenosyl-L-homocysteine +
            palmatine [RN:R03721]
ALL_REAC    R03721
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            columbamine [CPD:C01795]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            palmatine [CPD:C05315]
COMMENT     The product of this reaction is a protoberberine alkaloid that is
            widely distributed in the plant kingdom. This enzyme is distinct in
            specificity from EC 2.1.1.88, 8-hydroxyquercetin
            8-O-methyltransferase.
REFERENCE   1
  AUTHORS   Rueffer, M., Amann, M., Zenk, M.H.
  TITLE     S-Adenosyl-L-methionine:columbamine O-methyltransferase, a
            compartmentalized enzyme in protoberberine biosynthesis.
  JOURNAL   Plant Cell Reports 3 (1986) 182-185.
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.118
            ExPASy - ENZYME nomenclature database: 2.1.1.118
            ExplorEnz - The Enzyme Database: 2.1.1.118
            ERGO genome analysis and discovery system: 2.1.1.118
            BRENDA, the Enzyme Database: 2.1.1.118
            CAS: 105843-76-3
///
ENTRY       EC 2.1.1.119                Enzyme
NAME        10-hydroxydihydrosanguinarine 10-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:10-hydroxydihydrosanguinarine
            10-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 10-hydroxydihydrosanguinarine =
            S-adenosyl-L-homocysteine + dihydrochelirubine [RN:R04707]
ALL_REAC    R04707
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            10-hydroxydihydrosanguinarine [CPD:C05247]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            dihydrochelirubine [CPD:C05194]
COMMENT     This reaction is part of the pathway for synthesis of
            benzophenanthridine alkaloids in plants.
REFERENCE   1
  AUTHORS   De-Eknamkul, W., Tanahashi, T. and Zenk, M.H.
  TITLE     Enzymic 10-hydroxylation and 10-O-methylation of dihydrosanguinarine
            in dihydrochelirubine formation by Eschscholtzia.
  JOURNAL   Phytochemistry 31 (1992) 2713-2717.
  ORGANISM  Eschscholzia californica
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.119
            ExPASy - ENZYME nomenclature database: 2.1.1.119
            ExplorEnz - The Enzyme Database: 2.1.1.119
            ERGO genome analysis and discovery system: 2.1.1.119
            BRENDA, the Enzyme Database: 2.1.1.119
            CAS: 144388-39-6
///
ENTRY       EC 2.1.1.120                Enzyme
NAME        12-hydroxydihydrochelirubine 12-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:12-hydroxydihydrochelirubine
            12-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 12-hydroxydihydrochelirubine =
            S-adenosyl-L-homocysteine + dihydromacarpine [RN:R04705]
ALL_REAC    R04705
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            12-hydroxydihydrochelirubine [CPD:C05193]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            dihydromacarpine [CPD:C05316]
COMMENT     This reaction is part of the pathway for synthesis of
            benzophenanthridine alkaloid macarpine in plants.
REFERENCE   1
  AUTHORS   Kammerer, L., De-Eknamkul, W. and Zenk, M.H.
  TITLE     Enzymic 12-hydroxylation and 12-O-methylation of dihydrochelirubine
            in dihydromacarpine formation by Thalictrum bulgaricum.
  JOURNAL   Phytochemistry 36 (1994) 1409-1416.
  ORGANISM  Thalictrum bulgaricum
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.120
            ExPASy - ENZYME nomenclature database: 2.1.1.120
            ExplorEnz - The Enzyme Database: 2.1.1.120
            ERGO genome analysis and discovery system: 2.1.1.120
            BRENDA, the Enzyme Database: 2.1.1.120
            CAS: 158736-40-4
///
ENTRY       EC 2.1.1.121                Enzyme
NAME        6-O-methylnorlaudanosoline 5'-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:6-O-methylnorlaudanosoline
            5'-O-methyltransferase
REACTION    S-adenosyl-L-methionine + 6-O-methylnorlaudanosoline =
            S-adenosyl-L-homocysteine + nororientaline [RN:R04714]
ALL_REAC    R04714;
            (other) R05213
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            6-O-methylnorlaudanosoline [CPD:C05203]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            nororientaline [CPD:C05317]
COMMENT     Nororientaline is a precursor of the alkaloid papaverine.
REFERENCE   1
  AUTHORS   Rueffer, M., Nagakura, N., Zenk, M.H.
  TITLE     A highly specific O-methyltransferase for nororientaline synthesis
            isolated from Argemone platyceras cell cultures.
  JOURNAL   Planta Med. 49 (1983) 196-198.
  ORGANISM  Argemone platyceras
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.121
            ExPASy - ENZYME nomenclature database: 2.1.1.121
            ExplorEnz - The Enzyme Database: 2.1.1.121
            ERGO genome analysis and discovery system: 2.1.1.121
            BRENDA, the Enzyme Database: 2.1.1.121
            CAS: 89511-99-9
///
ENTRY       EC 2.1.1.122                Enzyme
NAME        (S)-tetrahydroprotoberberine N-methyltransferase;
            tetrahydroprotoberberine cis-N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:(S)-7,8,13,14-tetrahydroprotoberberine
            cis-N-methyltransferase
REACTION    S-adenosyl-L-methionine + (S)-7,8,13,14-tetrahydroprotoberberine =
            S-adenosyl-L-homocysteine +
            cis-N-methyl-(S)-7,8,13,14-tetrahydroprotoberberine [RN:R04716]
ALL_REAC    R04716;
            (other) R04691
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            (S)-7,8,13,14-tetrahydroprotoberberine [CPD:C05204]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            cis-N-methyl-(S)-7,8,13,14-tetrahydroprotoberberine [CPD:C05318]
COMMENT     Involved in the biosynthesis of isoquinoline alkaloids in plants.
REFERENCE   1
  AUTHORS   Rueffer, M., Zumstein, G., Zenk, M.H.
  TITLE     Partial purification and characterization of
            S-adenosyl-L-methionine:(S)-tetrahydroprotoberberine
            cis-N-methyltransferase from suspension-cultured cells of
            Eschscholtzia and Corydalis.
  JOURNAL   Phytochemistry 29 (1990) 3727-3733.
  ORGANISM  Eschscholzia californica, Corydalis vaginans
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.122
            ExPASy - ENZYME nomenclature database: 2.1.1.122
            ExplorEnz - The Enzyme Database: 2.1.1.122
            ERGO genome analysis and discovery system: 2.1.1.122
            BRENDA, the Enzyme Database: 2.1.1.122
            CAS: 106878-42-6
///
ENTRY       EC 2.1.1.123                Enzyme
NAME        [cytochrome-c]-methionine S-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:[cytochrome c]-methionine
            S-methyltransferase
REACTION    S-adenosyl-L-methionine + [cytochrome c]-methionine =
            S-adenosyl-L-homocysteine + [cytochrome c]-S-methyl-methionine
            [RN:R04717]
ALL_REAC    R04717
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            [cytochrome c] methionine [CPD:C05205]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            [cytochrome c]-S-methyl-methionine
COMMENT     The enzyme from Euglena gracilis methylates Met-65 of horse heart
            cytochrome c.
REFERENCE   1  [PMID:2981218]
  AUTHORS   Farooqui JZ, Tuck M, Paik WK.
  TITLE     Purification and characterization of enzymes from Euglena gracilis
            that methylate methionine and arginine residues of cytochrome c.
  JOURNAL   J. Biol. Chem. 260 (1985) 537-45.
  ORGANISM  Euglena gracilis
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.123
            ExPASy - ENZYME nomenclature database: 2.1.1.123
            ExplorEnz - The Enzyme Database: 2.1.1.123
            ERGO genome analysis and discovery system: 2.1.1.123
            BRENDA, the Enzyme Database: 2.1.1.123
            CAS: 93585-98-9
///
ENTRY       EC 2.1.1.124                Enzyme
NAME        [cytochrome c]-arginine N-methyltransferase;
            S-adenosyl-L-methionine:[cytochrome c]-arginine
            omega-N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:[cytochrome c]-arginine
            Nomega-methyltransferase
REACTION    S-adenosyl-L-methionine + [cytochrome c]-arginine =
            S-adenosyl-L-homocysteine + [cytochrome c]-Nomega-methyl-arginine
            [RN:R07239]
ALL_REAC    R07239;
            (other) R04717
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            [cytochrome c]-arginine [CPD:C15528]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            [cytochrome c]-Nomega-methyl-arginine
COMMENT     The enzyme from Euglena gracilis methylates Arg-38 of horse heart
            cytochrome c to form the Nomega-monomethyl-arginine derivative. This
            enzyme was previously listed together with EC 2.1.1.25 phenol
            O-methyltransferase and EC 2.1.1.26 iodophenol O-methyltransferase
            as a single, now deleted, entry (EC 2.1.1.23, protein-arginine
            N-methyltransferase).
REFERENCE   1  [PMID:2981218]
  AUTHORS   Farooqui JZ, Tuck M, Paik WK.
  TITLE     Purification and characterization of enzymes from Euglena gracilis
            that methylate methionine and arginine residues of cytochrome c.
  JOURNAL   J. Biol. Chem. 260 (1985) 537-45.
  ORGANISM  Euglena gracilis
ORTHOLOGY   KO: K05930  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.124
            ExPASy - ENZYME nomenclature database: 2.1.1.124
            ExplorEnz - The Enzyme Database: 2.1.1.124
            ERGO genome analysis and discovery system: 2.1.1.124
            BRENDA, the Enzyme Database: 2.1.1.124
            CAS: 9055-07-6
///
ENTRY       EC 2.1.1.125                Enzyme
NAME        histone-arginine N-methyltransferase;
            histone protein methylase I;
            nuclear protein (histone) N-methyltransferase;
            protein methylase I;
            S-adenosyl-L-methionine:histone-arginine omega-N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:histone-arginine Nomega-methyltransferase
REACTION    S-adenosyl-L-methionine + histone-arginine =
            S-adenosyl-L-homocysteine + histone-Nomega-methyl-arginine
            [RN:R04718]
ALL_REAC    R04718
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            histone-arginine [CPD:C05206]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            histone-Nomega-methyl-arginine
COMMENT     The enzyme forms the Nomega-monomethyl- and Nomega,Nomega'-dimethyl,
            but not the Nomega,Nomega-dimethyl-arginine derivatives. The name
            protein methylase I is misleading since it has been used for a
            number of enzymes with different specificities.
REFERENCE   1  [PMID:8288564]
  AUTHORS   Rajpurohit R, Lee SO, Park JO, Paik WK, Kim S.
  TITLE     Enzymatic methylation of recombinant heterogeneous nuclear RNP
            protein A1. Dual substrate specificity for
            S-adenosylmethionine:histone-arginine N-methyltransferase.
  JOURNAL   J. Biol. Chem. 269 (1994) 1075-82.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:8002954]
  AUTHORS   Rawal N, Rajpurohit R, Paik WK, Kim S.
  TITLE     Purification and characterization of
            S-adenosylmethionine-protein-arginine N-methyltransferase from rat
            liver.
  JOURNAL   Biochem. J. 300 ( Pt 2) (1994) 483-9.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map04111  Cell cycle - yeast
ORTHOLOGY   KO: K02516  protein arginine N-methyltransferase HSL7,negative
                        regulator of Swe1 kinase
            KO: K05931  
GENES       DME: Dmel_CG5358(Art4)
            SCE: YBR133C(HSL7)
            AGO: AGOS_ABR110W
            UMA: UM00877.1
STRUCTURES  PDB: 1OR8  1ORH  1ORI  2V74  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.125
            ExPASy - ENZYME nomenclature database: 2.1.1.125
            ExplorEnz - The Enzyme Database: 2.1.1.125
            ERGO genome analysis and discovery system: 2.1.1.125
            BRENDA, the Enzyme Database: 2.1.1.125
            CAS: 445295-80-7
///
ENTRY       EC 2.1.1.126                Enzyme
NAME        [myelin basic protein]-arginine N-methyltransferase;
            myelin basic protein methylase I;
            protein methylase I;
            S-adenosyl-L-methionine:[myelin-basic-protein]-arginine
            omega-N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:[myelin-basic-protein]-arginine
            Nomega-methyltransferase
REACTION    S-adenosyl-L-methionine + [myelin basic protein]-arginine =
            S-adenosyl-L-homocysteine + [myelin basic
            protein]-Nomega-methyl-arginine [RN:R04719]
ALL_REAC    R04719
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            [myelin basic protein]-arginine [CPD:C05207]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            [myelin basic protein]-Nomega-methyl-arginine
COMMENT     The enzyme from mammalian brain forms the Nomega-monomethyl-,
            Nomega,Nomega-dimethyl- and Nomega,Nomega'-dimethyl-arginine
            derivatives. The name protein methylase I is misleading since it has
            been used for a number of enzymes with different specificities.
REFERENCE   1  [PMID:2461933]
  AUTHORS   Ghosh SK, Paik WK, Kim S.
  TITLE     Purification and molecular identification of two protein methylases
            I from calf brain. Myelin basic protein- and histone-specific
            enzyme.
  JOURNAL   J. Biol. Chem. 263 (1988) 19024-33.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K05932  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.126
            ExPASy - ENZYME nomenclature database: 2.1.1.126
            ExplorEnz - The Enzyme Database: 2.1.1.126
            ERGO genome analysis and discovery system: 2.1.1.126
            BRENDA, the Enzyme Database: 2.1.1.126
            CAS: 9055-07-6
///
ENTRY       EC 2.1.1.127                Enzyme
NAME        [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase;
            rubisco methyltransferase;
            ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase;
            ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
            epsilonN-methyltransferase;
            S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase
            (dimerizing)]-lysine 6-N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase
            (dimerizing)]-lysine N6-methyltransferase
REACTION    S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate
            carboxylase]-lysine = S-adenosyl-L-homocysteine +
            [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
            [RN:R05179]
ALL_REAC    R05179
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            [ribulose-1,5-bisphosphate carboxylase]-lysine
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
COMMENT     The enzyme methylates Lys-14 in the large subunits of hexadecameric
            higher plant ribulose-bisphosphate-carboxylase (EC 4.1.1.39).
REFERENCE   1  [PMID:8527940]
  AUTHORS   Wang P, Royer M, Houtz RL.
  TITLE     Affinity purification of ribulose-1,5-bisphosphate
            carboxylase/oxygenase large subunit epsilon N-methyltransferase.
  JOURNAL   Protein. Expr. Purif. 6 (1995) 528-36.
  ORGANISM  Pisum sativum, spinach
REFERENCE   2  [PMID:8980518]
  AUTHORS   Ying Z, Janney N, Houtz RL.
  TITLE     Organization and characterization of the ribulose-1,5-bisphosphate
            carboxylase/oxygenase large subunit epsilon N-methyltransferase gene
            in tobacco.
  JOURNAL   Plant. Mol. Biol. 32 (1996) 663-71.
ORTHOLOGY   KO: K00592  [ribulose-bisphosphate carboxylase]-lysine
                        N-methyltransferase
GENES       ATH: AT1G14030
STRUCTURES  PDB: 1MLV  1OZV  1P0Y  2H21  2H23  2H2E  2H2J  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.127
            ExPASy - ENZYME nomenclature database: 2.1.1.127
            ExplorEnz - The Enzyme Database: 2.1.1.127
            ERGO genome analysis and discovery system: 2.1.1.127
            BRENDA, the Enzyme Database: 2.1.1.127
            CAS: 139171-98-5
///
ENTRY       EC 2.1.1.128                Enzyme
NAME        (RS)-norcoclaurine 6-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:(RS)-norcoclaurine 6-O-methyltransferase
REACTION    S-adenosyl-L-methionine + (RS)-norcoclaurine =
            S-adenosyl-L-homocysteine + (RS)-coclaurine [RN:R05162]
ALL_REAC    R05162 > R05123;
            (other) R04715 R05214
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            (R,S)-norcoclaurine [CPD:C06346]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            (R,S)-coclaurine [CPD:C06348]
COMMENT     The enzyme will also catalyse the 6-O-methylation of
            (RS)-norlaudanosoline to form 6-O-methyl-norlaudanosoline, but this
            alkaloid has not been found to occur in plants.
REFERENCE   1
  AUTHORS   Rueffer, M., Nagakura, N., Zenk, M.H.
  TITLE     Partial purification and properties of
            S-adenosyl-L-methionine:(R),(S)-norlaudanosoline-6-O-methyltransfera
            se from Argemone platyceras cell cultures.
  JOURNAL   Planta Med. 49 (1983) 131-137.
  ORGANISM  Argemone platyceras
REFERENCE   2  [PMID:7925429]
  AUTHORS   Sato F, Tsujita T, Katagiri Y, Yoshida S, Yamada Y.
  TITLE     Purification and characterization of S-adenosyl-L-methionine:
            norcoclaurine 6-O-methyltransferase from cultured Coptis japonica
            cells.
  JOURNAL   Eur. J. Biochem. 225 (1994) 125-31.
  ORGANISM  Coptis japonica
REFERENCE   3
  AUTHORS   Stadler, R., Zenk, M.H.
  TITLE     A revision of the generally accepted pathway for the biosynthesis of
            the benzyltetrahydroisoquinoline reticuline.
  JOURNAL   Liebigs Ann. Chem. (1990) 555-562.
  ORGANISM  Berberis stolonifera, Eschscholzia californica, Peumus boldus
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.128
            ExPASy - ENZYME nomenclature database: 2.1.1.128
            ExplorEnz - The Enzyme Database: 2.1.1.128
            ERGO genome analysis and discovery system: 2.1.1.128
            BRENDA, the Enzyme Database: 2.1.1.128
            CAS: 167398-06-3
///
ENTRY       EC 2.1.1.129                Enzyme
NAME        inositol 4-methyltransferase;
            myo-inositol 4-O-methyltransferase;
            S-adenosyl-L-methionine:myo-inositol 4-O-methyltransferase;
            myo-inositol 6-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:1D-myo-inositol 4-methyltransferase
REACTION    S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine +
            1D-4-O-methyl-myo-inositol [RN:R01190]
ALL_REAC    R01190;
            (other) R01191
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            myo-inositol [CPD:C00137]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            1D-4-O-methyl-myo-inositol [CPD:C06352]
COMMENT     The enzyme from the rice bean Vigna umbellata (Fabaceae) is highly
            specific for S-adenosyl-L-methionine. The enzyme also methylates
            1L-1,2,4/3,5-cyclohexanepentol, 2,4,6/3,5-pentahydroxycyclohexanone,
            D,L-2,3,4,6/5-pentacyclohexanone and
            2,2'-anhydro-2-C-hydroxymethyl-myo-inositol, but at lower rates than
            that of myo-inositol.
REFERENCE   1  [PMID:1600940]
  AUTHORS   Vernon DM, Bohnert HJ.
  TITLE     A novel methyl transferase induced by osmotic stress in the
            facultative halophyte Mesembryanthemum crystallinum.
  JOURNAL   EMBO. J. 11 (1992) 2077-85.
  ORGANISM  Mesembryanthemum crystallinum
REFERENCE   2
  AUTHORS   Wanek, W. and Richter, A.
  TITLE     Purification and characterization of myo-inositol
            6-O-methyltransferase from Vigna umbellata Ohwi et Ohashi.
  JOURNAL   Planta 197 (1995) 427-434.
  ORGANISM  Vigna umbellata
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.129
            ExPASy - ENZYME nomenclature database: 2.1.1.129
            ExplorEnz - The Enzyme Database: 2.1.1.129
            ERGO genome analysis and discovery system: 2.1.1.129
            BRENDA, the Enzyme Database: 2.1.1.129
///
ENTRY       EC 2.1.1.130                Enzyme
NAME        precorrin-2 C20-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:precorrin-4 C20-methyltransferase
REACTION    S-adenosyl-L-methionine + precorrin-2 = S-adenosyl-L-homocysteine +
            precorrin-3A [RN:R03948]
ALL_REAC    R03948
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            precorrin 2 [CPD:C02463]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            precorrin 3A [CPD:C05772]
REFERENCE   1  [PMID:1451790]
  AUTHORS   Roessner CA, Warren MJ, Santander PJ, Atshaves BP, Ozaki S,
            Stolowich NJ, Iida K, Scott AI.
  TITLE     Expression of 9 Salmonella typhimurium enzymes for cobinamide
            synthesis. Identification of the 11-methyl and 20-methyl
            transferases of corrin biosynthesis.
  JOURNAL   FEBS. Lett. 301 (1992) 73-8.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:7606163]
  AUTHORS   Roessner CA, Spencer JB, Ozaki S, Min C, Atshaves BP, Nayar P,
            Anousis N, Stolowich NJ, Holderman MT, Scott AI.
  TITLE     Overexpression in Escherichia coli of 12 vitamin B12 biosynthetic
            enzymes.
  JOURNAL   Protein. Expr. Purif. 6 (1995) 155-63.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:8226690]
  AUTHORS   Debussche L, Thibaut D, Cameron B, Crouzet J, Blanche F.
  TITLE     Biosynthesis of the corrin macrocycle of coenzyme B12 in Pseudomonas
            denitrificans.
  JOURNAL   J. Bacteriol. 175 (1993) 7430-40.
  ORGANISM  Pseudomonas denitrificans
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K00593  precorrin-2 C20-methyltransferase
GENES       YEN: YE2715(cbiL)
            PAE: PA2904(cobI)
            PAU: PA14_26510(cobI)
            PAP: PSPA7_2250(cobI)
            PPU: PP_4827(cobI)
            PST: PSPTO_4875(cobI)
            PSB: Psyr_4415
            PSP: PSPPH_4458(cobI)
            PFL: PFL_0659(cobI)
            PFO: Pfl_0606
            PEN: PSEEN4869(cobI)
            MCA: MCA2295
            HCH: HCH_06475(cobI)
            CVI: CV_1565(cbiL)
            RSO: RSp0621(cbiL)
            BMA: BMA1163(cobI)
            BMV: BMASAVP1_A1604(cobI)
            BML: BMA10299_A0266(cobI)
            BMN: BMA10247_0894(cobI)
            BXE: Bxe_B1243
            BUR: Bcep18194_A4822
            BCN: Bcen_1192
            BCH: Bcen2424_1672
            BAM: Bamb_1572
            BPS: BPSL1761(cobI)
            BPM: BURPS1710b_2111(cobI)
            BPL: BURPS1106A_1965(cobI)
            BPD: BURPS668_1948(cobI)
            BTE: BTH_I2400(cobI)
            POL: Bpro_2774
            MPT: Mpe_B0443(cobF) Mpe_B0478(cobF)
            AZO: azo3534(cbiL)
            DAR: Daro_1688
            GSU: GSU2995(cobI)
            GME: Gmet_0482
            PCA: Pcar_0476
            DVU: DVU0646(cobI)
            DDE: Dde_3107
            DPS: DP0211(cobI)
            SFU: Sfum_2135
            MLO: mlr1380
            SME: SMc03191(cobI)
            ATU: Atu2801(cobI)
            ATC: AGR_C_5080
            RET: RHE_PE00453(cobI)
            RLE: pRL110629(cobI)
            BME: BMEI0713
            BMF: BAB1_1306(cobI)
            BMS: BR1288(cobI)
            BMB: BruAb1_1289(cobI)
            BOV: BOV_1251(cobI)
            BJA: blr3266(cobI)
            BRA: BRADO4904(cobI)
            BBT: BBta_3147(cobI)
            RPA: RPA2089(cobI)
            RPB: RPB_3179
            RPC: RPC_1887
            RPD: RPD_2319
            RPE: RPE_2224
            SIL: SPO2866(cobI)
            SIT: TM1040_2213
            RSP: RSP_2826(cobI)
            JAN: Jann_2928
            RDE: RD1_3824(cobI)
            NAR: Saro_0339
            GBE: GbCGDNIH1_0661
            RRU: Rru_A2990
            MAG: amb0297
            MGM: Mmc1_3131
            GKA: GK1799
            SSA: SSA_0476
            CPF: CPF_1431(cobI)
            CBO: CBO0946(cbiL)
            CBA: CLB_0988(cobI)
            CBH: CLC_1002(cobI)
            CBF: CLI_1035(cobI)
            CKL: CKL_0727(cbiL)
            DSY: DSY4070(cobI)
            MTA: Moth_1091
            MTU: Rv2066(cobI)
            MTC: MT2126(cobIJ)
            MBO: Mb2092(cobI)
            MBB: BCG_2085(cobI)
            MPA: MAP1812(cobI)
            MAV: MAV_2430
            MSM: MSMEG_3873
            MUL: MUL_2290(cobI)
            MVA: Mvan_3431
            MGI: Mflv_3104
            MMC: Mmcs_2487
            MKM: Mkms_2532
            MJL: Mjls_2524
            CDI: DIP1233(cobIJ)
            NFA: nfa31520(cobIJ)
            RHA: RHA1_ro00174
            SCO: SCO1853(cobI)
            SMA: SAV6411(cobI)
            PAC: PPA0420
            TFU: Tfu_0316
            FRA: Francci3_1521
            FAL: FRAAL2333(cobI)
            SEN: SACE_5951
            RXY: Rxyl_0639
            LIL: LB159(cobI)
            LIC: LIC20129(cobI)
            LBJ: LBJ_4183(cobF)
            LBL: LBL_4198(cobF)
            SYW: SYNW0653(cobI)
            SYC: syc2241_c(cobI)
            SYF: Synpcc7942_1853
            SYD: Syncc9605_2022
            SYE: Syncc9902_0650
            SYG: sync_0590(cobI)
            SYR: SynRCC307_0460(cobI)
            SYX: SynWH7803_0561(cobI)
            CYA: CYA_0903(cobI)
            CYB: CYB_2189(cobI)
            TEL: tlr1449(cobI)
            GVI: gll0377(cobI)
            ANA: all0455
            AVA: Ava_2865
            PMA: Pro0386(cobF)
            PMM: PMM0389(cobI)
            PMT: PMT0198(cobI)
            PMN: PMN2A_1723
            PMI: PMT9312_0385
            PMB: A9601_04401(cobI)
            PMC: P9515_04511(cobI)
            PMF: P9303_21591(cobI)
            PMG: P9301_04091(cobI)
            PME: NATL1_04401(cobI)
            TER: Tery_0768
            DGE: Dgeo_2358
            SSO: SSO2301(cbiL)
            STO: ST1817
            SAI: Saci_0395
STRUCTURES  PDB: 2E0K  2E0N  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.130
            ExPASy - ENZYME nomenclature database: 2.1.1.130
            ExplorEnz - The Enzyme Database: 2.1.1.130
            ERGO genome analysis and discovery system: 2.1.1.130
            BRENDA, the Enzyme Database: 2.1.1.130
///
ENTRY       EC 2.1.1.131                Enzyme
NAME        precorrin-3B C17-methyltransferase;
            precorrin-3 methyltransferase;
            CobJ
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:precorrin-3B C17-methyltransferase
REACTION    S-adenosyl-L-methionine + precorrin-3B = S-adenosyl-L-homocysteine +
            precorrin-4 [RN:R05180]
ALL_REAC    R05180;
            (other) R05809
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            precorrin 3B [CPD:C06406]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            precorrin 4 [CPD:C06407]
COMMENT     In the aerobic cobalamin biosythesis pathway, four enzymes are
            involved in the conversion of precorrin-3A to precorrin-6A. The
            first of the four steps is carried out by EC 1.14.13.83,
            precorrin-3B synthase (CobG), yielding precorrin-3B as the product.
            This is followed by three methylation reactions, which introduce a
            methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; EC 2.1.1.133)
            and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to
            precorrin-4, precorrin-5 and precorrin-6A, respectively.
REFERENCE   1  [PMID:8405386]
  AUTHORS   Scott AI, Roessner CA, Stolowich NJ, Spencer JB, Min C, Ozaki SI.
  TITLE     Biosynthesis of vitamin B12. Discovery of the enzymes for oxidative
            ring contraction and insertion of the fourth methyl group.
  JOURNAL   FEBS. Lett. 331 (1993) 105-8.
  ORGANISM  Pseudomonas denitrificans
REFERENCE   2  [PMID:8226690]
  AUTHORS   Debussche L, Thibaut D, Cameron B, Crouzet J, Blanche F.
  TITLE     Biosynthesis of the corrin macrocycle of coenzyme B12 in Pseudomonas
            denitrificans.
  JOURNAL   J. Bacteriol. 175 (1993) 7430-40.
  ORGANISM  Pseudomonas denitrificans
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K05934  precorrin-3B C17-methyltransferase
GENES       ECI: UTI89_C3106(ygbN)
            STY: STY2232(cbiH)
            STT: t0847(cbiH)
            SPT: SPA0844(cbiH)
            SEC: SC2035(cbiH)
            STM: STM2027(cbiH)
            YEN: YE2718(cbiH)
            PLU: plu2991(cbiH)
            PAE: PA2903(cobJ)
            PAU: PA14_26530(cobJ)
            PPU: PP_4826(cobJ)
            PST: PSPTO_4874
            PSB: Psyr_4414
            PSP: PSPPH_4457
            PFL: PFL_0660
            PFO: Pfl_0607
            PEN: PSEEN4868(cobJ)
            MCA: MCA2293
            HHA: Hhal_1344
            CVI: CV_1562(cbiJ)
            RSO: RSp0618(cbiJH)
            BMA: BMA1164(cbiG)
            BMV: BMASAVP1_A1605(cbiG)
            BML: BMA10299_A0267(cbiG)
            BMN: BMA10247_0893(cbiG)
            BXE: Bxe_B1242
            BUR: Bcep18194_A4821
            BCN: Bcen_1191
            BCH: Bcen2424_1671
            BAM: Bamb_1571
            BPS: BPSL1762(cobJ)
            BPM: BURPS1710b_2110(cobJ)
            BPL: BURPS1106A_1964(cbiG)
            BPD: BURPS668_1947(cbiG)
            BTE: BTH_I2401
            POL: Bpro_2767
            PNA: Pnap_2153
            AAV: Aave_0077
            MPT: Mpe_B0445(cbiG) Mpe_B0447(cobJ) Mpe_B0480(cbiG)
            AZO: azo3536(cbiGb) azo3537(cbiH)
            DAR: Daro_1685
            PCA: Pcar_0471(cobJ)
            DVU: DVU3170(cobJ)
            DDE: Dde_3181
            DPS: DP0224(cobJ)
            MLO: mlr1381
            SME: SMc03190(cobJ)
            ATU: Atu2800(cobJ)
            ATC: AGR_C_5079
            RET: RHE_CH02486(cobE) RHE_PE00452(cobJ)
            RLE: RL2826(cobE) pRL110628(cobJ)
            BME: BMEI0700 BMEI0712
            BMF: BAB1_1307 BAB1_1321
            BMS: BR1289 BR1301
            BMB: BruAb1_1290 BruAb1_1302
            BJA: blr3267(cobJ)
            BRA: BRADO4903(cobJ)
            BBT: BBta_3148(cobJ)
            RPA: RPA2088(cobJ)
            RPB: RPB_3180
            RPC: RPC_1886
            RPD: RPD_2318
            RPE: RPE_2223
            SIL: SPO2867(cobJ)
            SIT: TM1040_2214
            RSP: RSP_2824(cobJ)
            RSH: Rsph17029_1471
            JAN: Jann_2927
            RDE: RD1_3823(cobJ)
            PDE: Pden_2536
            NAR: Saro_0338
            GBE: GbCGDNIH1_0662
            RRU: Rru_A2989
            MAG: amb0298
            MGM: Mmc1_3128
            GKA: GK1805
            LMO: lmo1199(cbiH)
            LMF: LMOf2365_1208(cobJ)
            LIN: lin1162(cbiH)
            LWE: lwe1156(cbiH)
            SSA: SSA_0472
            CAC: CAC1382(cbiH)
            CPE: CPE1220(cbiH)
            CPF: CPF_1428(cobJ)
            CPR: CPR_1234(cobJ)
            CTC: CTC00739
            CNO: NT01CX_0575(cobJ)
            CBO: CBO0949(cbiH)
            CBA: CLB_0991(cobJ)
            CBH: CLC_1005(cobJ)
            CBF: CLI_1038(cobJ)
            CKL: CKL_0730(cbiH)
            CHY: CHY_0764(cobJ)
            DSY: DSY4066(cobJ)
            MTA: Moth_1094
            MTU: Rv2066(cobI)
            MTC: MT2126(cobIJ)
            MBO: Mb2092(cobI)
            MBB: BCG_2085(cobI)
            MPA: MAP1812(cobI)
            MAV: MAV_2430
            MSM: MSMEG_3873
            MUL: MUL_2290(cobI)
            MVA: Mvan_3431
            MGI: Mflv_3104
            MMC: Mmcs_2487
            MKM: Mkms_2532
            MJL: Mjls_2524
            CDI: DIP1233(cobIJ)
            NFA: nfa31520(cobIJ)
            RHA: RHA1_ro00174
            SCO: SCO1857(SCI39.04)
            SMA: SAV6407(cobJ)
            TFU: Tfu_0316
            FRA: Francci3_1521
            FAL: FRAAL2333(cobI)
            SEN: SACE_5951 SACE_5960(cobJ)
            FNU: FN0951
            TDE: TDE0623(cobJ)
            LIL: LB157(cbiH)
            LIC: LIC20127(cobJ)
            LBJ: LBJ_4185(cobJ)
            LBL: LBL_4200(cobJ)
            SYN: slr0969(cbiG/cbiH)
            SYW: SYNW2126(cbiG)
            SYC: syc2240_c(cobJ)
            SYF: Synpcc7942_1854
            SYD: Syncc9605_0329
            SYE: Syncc9902_1997
            SYG: sync_0391(cbiG)
            SYR: SynRCC307_2160(cbiG)
            SYX: SynWH7803_0388(cbiG)
            CYA: CYA_1591(cbiG) CYA_1847(cbiG)
            CYB: CYB_0397(cbiG)
            TEL: tll1307(cobJ)
            GVI: gll2546(cobJ)
            ANA: all0453
            AVA: Ava_2863
            PMA: Pro1671(cobJ)
            PMM: PMM1525(cbiG)
            PMT: PMT1772(cbiG)
            PMN: PMN2A_1081
            PMI: PMT9312_1617
            PMB: A9601_17291(cobJ)
            PMC: P9515_17041(cobJ)
            PMF: P9303_23501(cobJ)
            PMG: P9301_17171(cobJ)
            PME: NATL1_19561(cobJ)
            BFR: BF2518
            BFS: BF2547(cobJ)
            PGI: PG0213
            CTE: CT0387(cbiCH)
            TTH: TT_P0013
            TTJ: TTHB056
            MJA: MJ0813
            MMP: MMP0953(cbiH)
            MAC: MA4259(cbiH)
            MBA: Mbar_A0629
            MMA: MM_0995
            MBU: Mbur_2356
            MHU: Mhun_3213
            MTH: MTH1403
            MST: Msp_1582(cbiH)
            MSI: Msm_1273
            MKA: MK1376(cobJ)
            AFU: AF0724(cbiH)
            HAL: VNG1555G(cobH) VNG1557G(cbiH)
            HMA: rrnAC3005(cobH) rrnAC3008(cbiH)
            HWA: HQ3033A(cbiH2) HQ3034A(cbiH1)
            NPH: NP1114A(cbiH_2) NP1116A(cbiH_1)
            TAC: Ta0655
            TVO: TVN0921
            PTO: PTO0993
            SSO: SSO2306(cbiH)
            STO: ST1823
            SAI: Saci_0398
            PAI: PAE0344(cbiF)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.131
            ExPASy - ENZYME nomenclature database: 2.1.1.131
            ExplorEnz - The Enzyme Database: 2.1.1.131
            ERGO genome analysis and discovery system: 2.1.1.131
            BRENDA, the Enzyme Database: 2.1.1.131
            CAS: 152787-64-9
///
ENTRY       EC 2.1.1.132                Enzyme
NAME        precorrin-6Y C5,15-methyltransferase (decarboxylating);
            precorrin-6 methyltransferase;
            precorrin-6Y methylase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:1-precorrin-6Y C5,15-methyltransferase
            (C-12-decarboxylating)
REACTION    2 S-adenosyl-L-methionine + precorrin-6Y = 2
            S-adenosyl-L-homocysteine + precorrin-8X + CO2 [RN:R05149]
ALL_REAC    R05149;
            (other) R05813
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            precorrin 6Y [CPD:C06319]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            precorrin 8X [CPD:C06408];
            CO2 [CPD:C00011]
COMMENT     The enzyme from Pseudomonas denitrificans has
            S-adenosyl-L-methionine-dependent methyltransferase and
            decarboxylase activities.
REFERENCE   1  [PMID:1732195]
  AUTHORS   Blanche F, Famechon A, Thibaut D, Debussche L, Cameron B, Crouzet J.
  TITLE     Biosynthesis of vitamin B12 in Pseudomonas denitrificans: the
            biosynthetic sequence from precorrin-6y to precorrin-8x is catalyzed
            by the cobL gene product.
  JOURNAL   J. Bacteriol. 174 (1992) 1050-2.
  ORGANISM  Pseudomonas denitrificans
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K00595  precorrin-6Y C5,15-methyltransferase
            KO: K03399  precorrin-6Y C5,15-methyltransferase
            KO: K05935  
GENES       STY: STY2236(cbiE)
            STT: t0843(cbiE)
            SPT: SPA0840(cbiE)
            SEC: SC2039(cbiE)
            STM: STM2031(cbiE)
            YEN: YE2721(cbiE)
            PLU: plu2995(cbiE)
            PAE: PA2907(cobL)
            PPU: PP_4830(cobL)
            PPF: Pput_4708
            PST: PSPTO_4878(cobL)
            PSB: Psyr_4418
            PSP: PSPPH_4461(cobL)
            PFL: PFL_0656(cobL)
            PFO: Pfl_0603
            PEN: PSEEN4872(cobL)
            PMY: Pmen_4570
            SSE: Ssed_2082
            MCA: MCA2296(cobL)
            HHA: Hhal_1348
            HCH: HCH_06474(cobL)
            MMW: Mmwyl1_3375
            RSO: RS03743(RSp0624)
            BMA: BMA1160(cobL)
            BMV: BMASAVP1_A1601(cobL)
            BML: BMA10299_A0262(cobL)
            BMN: BMA10247_0898(cobL)
            BXE: Bxe_B1246
            BVI: Bcep1808_1611
            BUR: Bcep18194_A4826
            BCN: Bcen_1195
            BCH: Bcen2424_1675
            BAM: Bamb_1575
            BPS: BPSL1758(cobL)
            BPM: BURPS1710b_2114
            BPL: BURPS1106A_1969(cobL)
            BPD: BURPS668_1952(cobL)
            BTE: BTH_I2397
            POL: Bpro_2775
            PNA: Pnap_2159
            AAV: Aave_0072
            MPT: Mpe_B0442(cobL) Mpe_B0477(cobL)
            AZO: azo3533(cbiE)
            DAR: Daro_1689
            GSU: GSU2996(cobL)
            GME: Gmet_0481
            PCA: Pcar_2739
            DVU: DVU2749(cobL)
            DVL: Dvul_0558
            DDE: Dde_0803
            DPS: DP0221(cobL)
            SFU: Sfum_2130
            MLO: mlr1383
            SME: SMc03188(cobL)
            SMD: Smed_2813
            ATU: Atu2798(cobL)
            ATC: AGR_C_5077
            RET: RHE_PE00450(cobL)
            RLE: pRL110626(cobL)
            BME: BMEI0716
            BMF: BAB1_1303
            BMS: BR1285(cobL)
            BMB: BruAb1_1286(cobL)
            BOV: BOV_1248(cobL)
            OAN: Oant_1900
            BJA: blr3269(cobL)
            BRA: BRADO4901(cobL)
            BBT: BBta_3150(cobL)
            RPA: RPA2086(cobL)
            RPB: RPB_3182(cbiE)
            RPC: RPC_1884
            RPD: RPD_2316
            RPE: RPE_2221
            XAU: Xaut_3280
            SIL: SPO2869(cobL)
            SIT: TM1040_2216
            RSP: RSP_2823(cobL)
            RSH: Rsph17029_1473
            RSQ: Rsph17025_1523
            JAN: Jann_2925
            RDE: RD1_3821(cobL)
            PDE: Pden_2538
            NAR: Saro_0336
            GBE: GbCGDNIH1_0663
            RRU: Rru_A2992
            MAG: amb0296
            MGM: Mmc1_3132
            GKA: GK1800
            LMO: lmo1195(cbiE)
            LMF: LMOf2365_1204(cbiE)
            LIN: lin1158(cbiE)
            LWE: lwe1152(cbiE)
            SSA: SSA_0468
            CAC: CAC0584
            CPE: CPE1225(cbiE)
            CPF: CPF_1432(cbiT) CPF_1433(cbiE)
            CPR: CPR_1238(cbiT) CPR_1239(cbiE)
            CTC: CTC00734(cbiT)
            CNO: NT01CX_0580(cbiE)
            CBO: CBO0937(cbiE)
            CBA: CLB_0978(cbiE) CLB_0980(cbiT)
            CBH: CLC_0992(cbiE) CLC_0994(cbiT)
            CBF: CLI_1024(cbiE) CLI_1026(cbiT)
            CHY: CHY_0760(cbiT)
            DSY: DSY4071(cobL)
            MTU: Rv2072c
            MTC: MT2132(cobL)
            MBO: Mb2098c(cobLb) Mb2099c(cobLa)
            MBB: BCG_2091c(cobLb) BCG_2092c(cobLa)
            MPA: MAP1817c(cobL)
            MAV: MAV_2424(cobL)
            MSM: MSMEG_3878(cobL)
            MVA: Mvan_3434
            MGI: Mflv_3101
            MMC: Mmcs_2483
            MKM: Mkms_2528
            MJL: Mjls_2520
            CGL: NCgl1428(cgl1483)
            CGB: cg1678(cobL)
            CEF: CE1611
            CDI: DIP1236
            NFA: nfa31560(cobL)
            RHA: RHA1_ro00828(cobL)
            SCO: SCO1856(SCI39.03)
            SMA: SAV6408(cobL1)
            NCA: Noca_2890
            TFU: Tfu_0314
            FRA: Francci3_2980(cbiE)
            FAL: FRAAL4916(cobL)
            SEN: SACE_5944(cobL) SACE_5961
            RXY: Rxyl_0642
            FNU: FN0966
            TDE: TDE2373
            LIL: LB160(cbiE)
            LIC: LIC20130(cobL)
            LBJ: LBJ_4182(cobL)
            LBL: LBL_4197(cobL)
            SYN: sll0099(cobL,cbiE/cbiT)
            SYW: SYNW1596(cobL)
            SYC: syc2244_d(cobL)
            SYF: Synpcc7942_1850
            SYD: Syncc9605_0917
            SYE: Syncc9902_1492
            SYG: sync_0810(cbiE)
            SYR: SynRCC307_1746(cobL)
            SYX: SynWH7803_1707(cobL)
            CYA: CYA_0463(cbiE) CYA_2746(cbiT)
            CYB: CYB_0227(cbiE) CYB_0362(cbiT)
            TEL: tll0172(cobL)
            GVI: gll0378(cobL)
            ANA: all3722
            AVA: Ava_1817 Ava_3558
            PMA: Pro1342(cobL)
            PMM: PMM1268(cobL)
            PMT: PMT0370(cobL)
            PMN: PMN2A_0834
            PMI: PMT9312_1362
            PMB: A9601_14671(cobL)
            PMC: P9515_14291(cobL)
            PMF: P9303_19311(cobL)
            PMG: P9301_14531(cobL)
            PME: NATL1_16871(cobL)
            TER: Tery_0210
            BFR: BF2519
            BFS: BF2548
            PGI: PG0212(cobL)
            CTE: CT0386(cbiET)
            DET: DET0240 DET0296
            RRS: RoseRS_0569
            RCA: Rcas_0640
            DGE: Dgeo_2361
            TTH: TT_P0010
            TTJ: TTHB053
            MJA: MJ1522(cbiE)
            MMP: MMP1227(cbiE)
            MAC: MA0520(cbiE)
            MBA: Mbar_A1492
            MMA: MM_1680
            MHU: Mhun_3216
            MTH: MTH1514
            MST: Msp_1464(cbiE)
            MSI: Msm_1167
            MKA: MK1428(cobL_2)
            AFU: AF0722(cbiE)
            HAL: VNG1568G(cbiJ)
            HMA: rrnAC3021(cbiJ)
            HWA: HQ2298A(cbiE)
            NPH: NP1088A(cbiE)
            TAC: Ta0660
            TVO: TVN0916
            PTO: PTO1434
            SSO: SSO2296(cbiE)
            STO: ST1825
            SAI: Saci_0400
            PAI: PAE0340(cbiE)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.132
            ExPASy - ENZYME nomenclature database: 2.1.1.132
            ExplorEnz - The Enzyme Database: 2.1.1.132
            ERGO genome analysis and discovery system: 2.1.1.132
            BRENDA, the Enzyme Database: 2.1.1.132
///
ENTRY       EC 2.1.1.133                Enzyme
NAME        precorrin-4 C11-methyltransferase;
            precorrin-3 methylase;
            CobM
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:precorrin-4 C11 methyltransferase
REACTION    S-adenosyl-L-methionine + precorrin-4 = S-adenosyl-L-homocysteine +
            precorrin-5 [RN:R05181]
ALL_REAC    R05181;
            (other) R05810
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            precorrin 4 [CPD:C06407]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            precorrin 5 [CPD:C06416]
COMMENT     In the aerobic cobalamin biosythesis pathway, four enzymes are
            involved in the conversion of precorrin-3A to precorrin-6A. The
            first of the four steps is carried out by EC 1.14.13.83,
            precorrin-3B synthase (CobG), yielding precorrin-3B as the product.
            This is followed by three methylation reactions, which introduce a
            methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; EC 2.1.1.133)
            and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to
            precorrin-4, precorrin-5 and precorrin-6A, respectively.
REFERENCE   1  [PMID:2211521]
  AUTHORS   Crouzet J, Cameron B, Cauchois L, Rigault S, Rouyez MC, Blanche F,
            Thibaut D, Debussche L.
  TITLE     Genetic and sequence analysis of an 8.7-kilobase Pseudomonas
            denitrificans fragment carrying eight genes involved in
            transformation of precorrin-2 to cobyrinic acid.
  JOURNAL   J. Bacteriol. 172 (1990) 5980-90.
  ORGANISM  Pseudomonas denitrificans
REFERENCE   2  [PMID:8501034]
  AUTHORS   Roth JR, Lawrence JG, Rubenfield M, Kieffer-Higgins S, Church GM.
  TITLE     Characterization of the cobalamin (vitamin B12) biosynthetic genes
            of Salmonella typhimurium.
  JOURNAL   J. Bacteriol. 175 (1993) 3303-16.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K05936  precorrin-4 C11-methyltransferase
GENES       STY: STY2234(cbiF)
            STT: t0845(cbiF)
            SPT: SPA0842(cbiF)
            SEC: SC2037(cbiF)
            STM: STM2029(cbiF)
            YEN: YE2719a(cbiF)
            PLU: plu2993(cbiF)
            PAE: PA2948(cobM)
            PAU: PA14_25920(cobM)
            PAP: PSPA7_2213(cobM)
            PPU: PP_3410(cobM)
            PST: PSPTO_3154(cobM)
            PSB: Psyr_3020
            PSP: PSPPH_2221(cobM)
            PFL: PFL_3659(cobM)
            PFO: Pfl_3103
            PEN: PSEEN2427(cobM)
            PMY: Pmen_4589
            MCA: MCA2300(cobM)
            HHA: Hhal_1351
            HCH: HCH_06479(cobM)
            MMW: Mmwyl1_1375
            CVI: CV_1564(cbiF)
            RSO: RSp0620(cbiF)
            BMA: BMA1157(cobM)
            BMV: BMASAVP1_A1598(cobM)
            BML: BMA10299_A0259(cobM)
            BMN: BMA10247_0901(cobM)
            BXE: Bxe_B1249
            BVI: Bcep1808_1614
            BUR: Bcep18194_A4829
            BCN: Bcen_1198
            BCH: Bcen2424_1678
            BAM: Bamb_1578
            BPS: BPSL1755(cobM)
            BPM: BURPS1710b_2117(cobM)
            BPL: BURPS1106A_1972(cobM)
            BPD: BURPS668_1955(cobM)
            BTE: BTH_I2394(cobM)
            MPT: Mpe_B0438(cobM) Mpe_B0473(cobM)
            AZO: azo3529
            DAR: Daro_1693
            GSU: GSU2994(cobM)
            GME: Gmet_0483
            GUR: Gura_0039
            PCA: Pcar_0473
            PPD: Ppro_3231
            DVU: DVU2748(cobM)
            DDE: Dde_0801
            DPS: DP0222(cobM)
            SFU: Sfum_2129
            MLO: mlr1385
            SME: SMc03187(cobM)
            ATU: Atu2796(cobM)
            ATC: AGR_C_5074
            RET: RHE_PE00449(cobM)
            RLE: pRL110625(cobM)
            BME: BMEI0701
            BMF: BAB1_1320
            BMS: BR1300(cobM)
            BMB: BruAb1_1301(cobM)
            BOV: BOV_1262(cobM)
            BJA: blr3271(cobM)
            BRA: BRADO4899(cobM)
            BBT: BBta_3152(cobM)
            RPA: RPA2084(cobM)
            RPB: RPB_3184
            RPC: RPC_1882
            RPD: RPD_2314
            RPE: RPE_2219
            SIL: SPO2871(cobM)
            SIT: TM1040_2218
            RSP: RSP_2821(cobM)
            RDE: RD1_3819(cobM)
            NAR: Saro_0334
            GBE: GbCGDNIH1_0665
            RRU: Rru_A3384
            MAG: amb0514
            MGM: Mmc1_3136
            GKA: GK1798
            LMO: lmo1197(cbiF)
            LMF: LMOf2365_1206(cobM)
            LIN: lin1160(cbiF)
            LWE: lwe1154(cbiF)
            SSA: SSA_0470(cobM)
            LRE: Lreu_1716
            CAC: CAC1380(cbiF)
            CPE: CPE1222(cbiF)
            CPF: CPF_1430(cobM)
            CPR: CPR_1236(cobM)
            CTC: CTC00736
            CNO: NT01CX_0577(cobM)
            CBO: CBO0947(cbiF)
            CBA: CLB_0989(cobM)
            CBH: CLC_1003(cobM)
            CBF: CLI_1036(cobM)
            CBE: Cbei_2316
            CKL: CKL_0728(cbiF)
            CHY: CHY_0762(cobM)
            DSY: DSY4068(cobM)
            DRM: Dred_2711
            MTA: Moth_1092
            MTU: Rv2071c(cobM)
            MTC: MT2131(cobM)
            MBO: Mb2097c(cobM)
            MBB: BCG_2090c(cobM)
            MPA: MAP1816c(cobM)
            MAV: MAV_2425(cobM)
            MSM: MSMEG_3877(cobM)
            MMC: Mmcs_2484
            MKM: Mkms_2529
            MJL: Mjls_2521
            CDI: DIP1235(cobM)
            NFA: nfa50340
            RHA: RHA1_ro00827(cobM)
            SCO: SCO1855(SCI39.02)
            SMA: SAV6409(cobM)
            PAC: PPA0421
            TFU: Tfu_0315
            FRA: Francci3_1523
            FAL: FRAAL2335(cobM)
            SEN: SACE_5945(cobM)
            RXY: Rxyl_0640
            FNU: FN0957
            TDE: TDE0614(cobM)
            LIL: LB156(cbiF)
            LIC: LIC20126(cobM)
            LBJ: LBJ_4186(cobM)
            LBL: LBL_4201(cobM)
            SYN: slr0239(cbiF)
            SYW: SYNW1844(cobM)
            SYC: syc0321_d(cobM)
            SYF: Synpcc7942_1229
            SYD: Syncc9605_0625
            SYE: Syncc9902_1737
            SYG: sync_2146(cobM)
            SYR: SynRCC307_0701(cobM)
            SYX: SynWH7803_1853(cobM)
            CYA: CYA_1504(cobM)
            CYB: CYB_2708(cobM)
            TEL: tlr0563(cobM)
            GVI: gll1377(cobM)
            ANA: all4698
            AVA: Ava_1968
            PMA: Pro0457(cobM)
            PMM: PMM0459(cobM)
            PMT: PMT1325(cobM)
            PMN: PMN2A_1791
            PMI: PMT9312_0459
            PMB: A9601_05151(cobM)
            PMC: P9515_05231(cobM)
            PMF: P9303_06621(cobM)
            PMG: P9301_04841(cobM)
            PME: NATL1_05141(cobM)
            TER: Tery_1552
            BFR: BF2520
            BFS: BF2549
            PGI: PG0211(cbiGF)
            CTE: CT0385(cbiGF)
            RCA: Rcas_0638
            DGE: Dgeo_2357
            TTH: TT_P0012
            TME: Tmel_0702
            MJA: MJ1578(cbiF)
            MMP: MMP1662(cbiF)
            MMQ: MmarC5_1747
            MMZ: MmarC7_0934
            MAE: Maeo_1342
            MVN: Mevan_0962
            MAC: MA4261(cbiF)
            MBA: Mbar_A0627
            MMA: MM_0998
            MBU: Mbur_2358
            MHU: Mhun_3211
            MTH: MTH602
            MST: Msp_0988(cbiF)
            MSI: Msm_0101
            MKA: MK1375(cobM)
            AFU: AF0726(cbiF)
            HAL: VNG1553G(cbiF)
            HMA: rrnAC3001(cbiF)
            HWA: HQ1832A(cbiF)
            NPH: NP1120A(cbiF)
            TAC: Ta0659
            TVO: TVN0917
            PTO: PTO1432
            SSO: SSO2299(cbiF)
            STO: ST1816
            SAI: Saci_0394
            PAI: PAE0349(cbiF)
            PCL: Pcal_1521
STRUCTURES  PDB: 1CBF  2CBF  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.133
            ExPASy - ENZYME nomenclature database: 2.1.1.133
            ExplorEnz - The Enzyme Database: 2.1.1.133
            ERGO genome analysis and discovery system: 2.1.1.133
            BRENDA, the Enzyme Database: 2.1.1.133
///
ENTRY       EC 2.1.1.134      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
COMMENT     Deleted entry: myo-inositol 6-O-methyltransferase. Now included with
            EC 2.1.1.129, inositol 4-methyltransferase (EC 2.1.1.134 created
            1999, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.134
            ExPASy - ENZYME nomenclature database: 2.1.1.134
            ExplorEnz - The Enzyme Database: 2.1.1.134
            ERGO genome analysis and discovery system: 2.1.1.134
            BRENDA, the Enzyme Database: 2.1.1.134
///
ENTRY       EC 2.1.1.135      Obsolete  Enzyme
NAME        Transferred to 1.16.1.8
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
COMMENT     Transferred entry: now EC 1.16.1.8 [methionine synthase] reductase.
            (EC 2.1.1.135 created 1999, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.135
            ExPASy - ENZYME nomenclature database: 2.1.1.135
            ExplorEnz - The Enzyme Database: 2.1.1.135
            ERGO genome analysis and discovery system: 2.1.1.135
            BRENDA, the Enzyme Database: 2.1.1.135
///
ENTRY       EC 2.1.1.136                Enzyme
NAME        chlorophenol O-methyltransferase;
            halogenated phenol O-methyltransferase, trichlorophenol
            O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:trichlorophenol O-methyltransferase
REACTION    S-adenosyl-L-methionine + trichlorophenol =
            S-adenosyl-L-homocysteine + trichloroanisole [RN:R05754]
ALL_REAC    R05754
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            trichlorophenol
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            trichloroanisole
COMMENT     The enzyme from Trichoderma virgatum, when cultured in the presence
            of halogenated phenol, also acts on a range of mono-, di- and
            trichlorophenols.
REFERENCE   1
  AUTHORS   Kikuchi, T. and Oe, T.
  TITLE     Halogenated phenol O-methyltransferase, its production and
            deodorization using the same.
  JOURNAL   Chem. Abstr. 127 (1994) 27468.
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.136
            ExPASy - ENZYME nomenclature database: 2.1.1.136
            ExplorEnz - The Enzyme Database: 2.1.1.136
            ERGO genome analysis and discovery system: 2.1.1.136
            BRENDA, the Enzyme Database: 2.1.1.136
///
ENTRY       EC 2.1.1.137                Enzyme
NAME        arsenite methyltransferase;
            S-adenosyl-L-methionine:arsenic(III) methyltransferase;
            S-adenosyl-L-methionine:methylarsonite As-methyltransferase;
            methylarsonite methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:arsenite As-methyltransferase
REACTION    (1) S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine +
            methylarsonate [RN:R05755];
            (2) S-adenosyl-L-methionine + methylarsonite =
            S-adenosyl-L-homocysteine + dimethylarsinate [RN:R05756]
ALL_REAC    R05755 R05756
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            arsenite [CPD:C06697];
            methylarsonite [CPD:C07295]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            methylarsonate [CPD:C07294];
            dimethylarsinate [CPD:C07308]
COMMENT     An enzyme of the biotransformation pathway that forms
            dimethylarsinate from inorganic arsenite and arsenate. It methylates
            arsenite to form methylarsonate, Me-AsO3H2, which is reduced by EC
            1.20.4.2, methylarsonate reductase, to methylarsonite, Me-As(OH)2.
            Methylarsonite is also a substrate for this enzyme (EC 2.1.1.137),
            which converts it into the much less toxic compound dimethylarsinate
            (cacodylate), Me2As(O)-OH.
REFERENCE   1  [PMID:10604879]
  AUTHORS   Zakharyan RA, Aposhian HV.
  TITLE     Enzymatic reduction of arsenic compounds in mammalian systems: the
            rate-limiting enzyme of rabbit liver arsenic biotransformation is
            MMA(V) reductase.
  JOURNAL   Chem. Res. Toxicol. 12 (1999) 1278-83.
  ORGANISM  rabbit
REFERENCE   2  [PMID:10387927]
  AUTHORS   Zakharyan RA, Ayala-Fierro F, Cullen WR, Carter DM, Aposhian HV.
  TITLE     Enzymatic methylation of arsenic compounds. VII. Monomethylarsonous
            acid (MMAIII) is the substrate for MMA methyltransferase of rabbit
            liver and human hepatocytes.
  JOURNAL   Toxicol. Appl. Pharmacol. 158 (1999) 9-15.
  ORGANISM  rabbit, human [GN:hsa]
REFERENCE   3  [PMID:8806872]
  AUTHORS   Zakharyan RA, Wildfang E, Aposhian HV.
  TITLE     Enzymatic methylation of arsenic compounds. III. The marmoset and
            tamarin, but not the rhesus, monkeys are deficient in
            methyltransferases that methylate inorganic arsenic.
  JOURNAL   Toxicol. Appl. Pharmacol. 140 (1996) 77-84.
  ORGANISM  rabbit, marmoset
REFERENCE   4  [PMID:8605285]
  AUTHORS   Zakharyan R, Wu Y, Bogdan GM, Aposhian HV.
  TITLE     Enzymatic methylation of arsenic compounds: assay, partial
            purification, and properties of arsenite methyltransferase and
            monomethylarsonic acid methyltransferase of rabbit liver.
  JOURNAL   Chem. Res. Toxicol. 8 (1995) 1029-38.
  ORGANISM  rabbit
REFERENCE   5  [PMID:11790780]
  AUTHORS   Lin S, Shi Q, Nix FB, Styblo M, Beck MA, Herbin-Davis KM, Hall LL,
            Simeonsson JB, Thomas DJ.
  TITLE     A novel S-adenosyl-L-methionine:arsenic(III) methyltransferase from
            rat liver cytosol.
  JOURNAL   J. Biol. Chem. 277 (2002) 10795-803.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K07755  arsenite methyltransferase
GENES       HSA: 57412(AS3MT)
            PTR: 450703(AS3MT)
            MMU: 57344(As3mt)
            RNO: 140925(As3mt)
            CFA: 486865(AS3MT)
            SPU: 579047(LOC579047)
            AFM: AFUA_1G16110 AFUA_5G15020
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.137
            ExPASy - ENZYME nomenclature database: 2.1.1.137
            ExplorEnz - The Enzyme Database: 2.1.1.137
            ERGO genome analysis and discovery system: 2.1.1.137
            UM-BBD (Biocatalysis/Biodegradation Database): 2.1.1.137
            BRENDA, the Enzyme Database: 2.1.1.137
///
ENTRY       EC 2.1.1.138      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
COMMENT     Deleted entry: methylarsonite methyltransferase. Reaction due to EC
            2.1.1.137, arsonite methyltransferase. (EC 2.1.1.138 created 2000,
            deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.138
            ExPASy - ENZYME nomenclature database: 2.1.1.138
            ExplorEnz - The Enzyme Database: 2.1.1.138
            ERGO genome analysis and discovery system: 2.1.1.138
            BRENDA, the Enzyme Database: 2.1.1.138
///
ENTRY       EC 2.1.1.139                Enzyme
NAME        3'-demethylstaurosporine O-methyltransferase;
            3'-demethoxy-3'-hydroxystaurosporine O-methyltransferase;
            staurosporine synthase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:3'-demethylstaurosporine O-methyltransferase
REACTION    S-adenosyl-L-methionine + 3'-demethylstaurosporine =
            S-adenosyl-L-homocysteine + staurosporine [RN:R05757]
ALL_REAC    R05757
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            3'-demethylstaurosporine [CPD:C07349]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            staurosporine [CPD:C02079]
COMMENT     Catalyses the final step in the biosynthesis of staurosporine, an
            alkaloidal antibiotic that is a potent inhibitor of protein kinases,
            especially protein kinase C.
REFERENCE   1  [PMID:9727395]
  AUTHORS   Weidner S, Kittelmann M, Goeke K, Ghisalba O, Zahner H.
  TITLE     3'-Demethoxy-3'-hydroxystaurosporine-O-methyltransferase from
            Streptomyces longisporoflavus catalyzing the last step in the
            biosynthesis of staurosporine.
  JOURNAL   J. Antibiot. (Tokyo). 51 (1998) 679-82.
  ORGANISM  Streptomyces longisporoflavus
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.139
            ExPASy - ENZYME nomenclature database: 2.1.1.139
            ExplorEnz - The Enzyme Database: 2.1.1.139
            ERGO genome analysis and discovery system: 2.1.1.139
            BRENDA, the Enzyme Database: 2.1.1.139
///
ENTRY       EC 2.1.1.140                Enzyme
NAME        (S)-coclaurine-N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:(S)-coclaurine-N-methyltransferase
REACTION    S-adenosyl-L-methionine + (S)-coclaurine = S-adenosyl-L-homocysteine
            + (S)-N-methylcoclaurine [RN:R04692]
ALL_REAC    R04692
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            (S)-coclaurine [CPD:C06161]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            (S)-N-methylcoclaurine [CPD:C05176]
COMMENT     The enzyme is specific for the (S)-isomer of coclaurine.
            Norcoclaurine can also act as an acceptor.
REFERENCE   1
  AUTHORS   Loeffler, S., Deus-Neumann, B. and Zenk, M.H.
  TITLE     S-Adenosyl-L-methionine: (S)-coclaurine-N-methyltransferase from
            Tinospora cordifolia.
  JOURNAL   Phytochemistry 38 (1995) 1387-1395.
  ORGANISM  Tinospora cordifolia
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.140
            ExPASy - ENZYME nomenclature database: 2.1.1.140
            ExplorEnz - The Enzyme Database: 2.1.1.140
            ERGO genome analysis and discovery system: 2.1.1.140
            BRENDA, the Enzyme Database: 2.1.1.140
///
ENTRY       EC 2.1.1.141                Enzyme
NAME        jasmonate O-methyltransferase;
            jasmonic acid carboxyl methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:jasmonate O-methyltransferase
REACTION    S-adenosyl-L-methionine + jasmonate = S-adenosyl-L-homocysteine +
            methyl jasmonate [RN:R05759]
ALL_REAC    R05759
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            jasmonate [CPD:C08491]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            methyl jasmonate [CPD:C11512]
COMMENT     9,10-Dihydrojasmonic acid is a poor substrate for the enzyme. The
            enzyme does not convert 12-oxo-phytodienoic acid (a precursor of
            jasmonic acid), salicylic acid, benzoic acid, linolenic acid or
            cinnamic acid into their corresponding methyl esters. Enzyme
            activity is inhibited by the presence of divalent cations, e.g.,
            Ca2+, Cu2+, Mg2+ and Zn2+.
REFERENCE   1  [PMID:11287667]
  AUTHORS   Seo HS, Song JT, Cheong JJ, Lee YH, Lee YW, Hwang I, Lee JS, Choi
            YD.
  TITLE     Jasmonic acid carboxyl methyltransferase: a key enzyme for
            jasmonate-regulated plant responses.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 4788-93.
  ORGANISM  Arabidopsis thaliana [GN:ath]
PATHWAY     PATH: map00592  alpha-Linolenic acid metabolism
ORTHOLOGY   KO: K08241  jasmonate O-methyltransferase
GENES       ATH: AT1G19640(JMT)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.141
            ExPASy - ENZYME nomenclature database: 2.1.1.141
            ExplorEnz - The Enzyme Database: 2.1.1.141
            ERGO genome analysis and discovery system: 2.1.1.141
            BRENDA, the Enzyme Database: 2.1.1.141
///
ENTRY       EC 2.1.1.142                Enzyme
NAME        cycloartenol 24-C-methyltransferase;
            sterol C-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:cycloartenol 24-C-methyltransferase
REACTION    S-adenosyl-L-methionine + cycloartenol = S-adenosyl-L-homocysteine +
            (24R)-24-methylcycloart-25-en-3beta-ol [RN:R05760]
ALL_REAC    R05760
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            cycloartenol [CPD:C01902]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            (24R)-24-methylcycloart-25-en-3beta-ol
COMMENT     S-Adenosyl-L-methionine methylates the Si face of the 24(25)-double
            bond with elimination of a hydrogen atom from the pro-Z methyl group
            at C-25.
REFERENCE   1  [PMID:10882005]
  AUTHORS   Mangla AT, Nes WD.
  TITLE     Sterol C-methyl transferase from Prototheca wickerhamii mechanism,
            sterol specificity and inhibition.
  JOURNAL   Bioorg. Med. Chem. 8 (2000) 925-36.
  ORGANISM  Prototheca wickerhamii
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.142
            ExPASy - ENZYME nomenclature database: 2.1.1.142
            ExplorEnz - The Enzyme Database: 2.1.1.142
            ERGO genome analysis and discovery system: 2.1.1.142
            BRENDA, the Enzyme Database: 2.1.1.142
///
ENTRY       EC 2.1.1.143                Enzyme
NAME        24-methylenesterol C-methyltransferase;
            SMT2;
            24-methylenelophenol C-241-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:24-methylenelophenol C-methyltransferase
REACTION    S-adenosyl-L-methionine + 24-methylenelophenol =
            S-adenosyl-L-homocysteine + (Z)-24-ethylidenelophenol [RN:R05776]
ALL_REAC    R05776
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            24-methylenelophenol
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            (Z)-24-ethylidenelophenol [CPD:C11523]
COMMENT     This is the second methylation step of plant sterol biosynthesis (cf
            EC 2.1.1.142, cycloartenol 24-C-methyltransferase).
REFERENCE   1  [PMID:9746350]
  AUTHORS   Bouvier-Nave P, Husselstein T, Benveniste P.
  TITLE     Two families of sterol methyltransferases are involved in the first
            and the second methylation steps of plant sterol biosynthesis.
  JOURNAL   Eur. J. Biochem. 256 (1998) 88-96.
  ORGANISM  Nicotiana tabacum
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K08242  24-methylenesterol C-methyltransferase
GENES       ATH: AT1G20330(SMT2) AT1G76090(SMT3)
            OSA: 4331540
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.143
            ExPASy - ENZYME nomenclature database: 2.1.1.143
            ExplorEnz - The Enzyme Database: 2.1.1.143
            ERGO genome analysis and discovery system: 2.1.1.143
            BRENDA, the Enzyme Database: 2.1.1.143
///
ENTRY       EC 2.1.1.144                Enzyme
NAME        trans-aconitate 2-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:(E)-prop-1-ene-1,2,3-tricarboxylate
            2'-O-methyltransferase
REACTION    S-adenosyl-L-methionine + trans-aconitate =
            S-adenosyl-L-homocysteine + (E)-3-(methoxycarbonyl)pent-2-enedioate
            [RN:R05763]
ALL_REAC    R05763
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            trans-aconitate [CPD:C02341]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            (E)-3-(methoxycarbonyl)pent-2-enedioate [CPD:C11514]
COMMENT     Also catalyses the formation of the methyl monoester of
            cis-aconitate, isocitrate and citrate, but more slowly. While the
            enzyme from Escherichia coli forms
            (E)-3-(methoxycarbonyl)-pent-2-enedioate as the product, that from
            Saccharomyces cerevisiae forms
            (E)-2-(methoxycarbonylmethyl)butenedioate and is therefore
            classified as a separate enzyme (cf. EC 2.1.1.145, trans-aconitate
            3-methyltransferase).
REFERENCE   1  [PMID:10224113]
  AUTHORS   Cai H, Clarke S.
  TITLE     A novel methyltransferase catalyzes the methyl esterification of
            trans-aconitate in Escherichia coli.
  JOURNAL   J. Biol. Chem. 274 (1999) 13470-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:11329290]
  AUTHORS   Cai H, Strouse J, Dumlao D, Jung ME, Clarke S.
  TITLE     Distinct reactions catalyzed by bacterial and yeast trans-aconitate
            methyltransferases.
  JOURNAL   Biochemistry. 40 (2001) 2210-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:11695919]
  AUTHORS   Cai H, Dumlao D, Katz JE, Clarke S.
  TITLE     Identification of the gene and characterization of the activity of
            the trans-aconitate methyltransferase from Saccharomyces cerevisiae.
  JOURNAL   Biochemistry. 40 (2001) 13699-709.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K00598  trans-aconitate 2-methyltransferase
GENES       ANI: AN7224.2
            AOR: AO090005000426
            UMA: UM02124.1
            ECO: b1519(tam)
            ECJ: JW1512(tam)
            ECE: Z2186
            ECS: ECs2126
            ECC: c1942(tam)
            ECI: UTI89_C1738(tam)
            ECP: ECP_1503
            ECV: APECO1_639(tam)
            ECW: EcE24377A_1719(tam)
            ECX: EcHS_A1601(tam)
            YPE: YPO2509(tam)
            YPK: y1678
            YPM: YP_2324(tam)
            YPA: YPA_2001
            YPN: YPN_2104
            YPP: YPDSF_1921
            YPS: YPTB2545(tam)
            YPI: YpsIP31758_1498(tam)
            SFL: SF1576(tam)
            SFX: S1702
            SFV: SFV_1576
            SDY: SDY_1625
            ENT: Ent638_2018
            PAE: PA2564
            PPU: PP_2545
            PPF: Pput_3170
            PFL: PFL_1326(tam)
            PFO: Pfl_1276 Pfl_1327
            PEN: PSEEN2396
            PMY: Pmen_2425
            REU: Reut_A3459
            REH: H16_A0107
            RME: Rmet_3612
            BXE: Bxe_A2203
            BUR: Bcep18194_B2805
            BCN: Bcen_4775
            BCH: Bcen2424_3392
            BAM: Bamb_5169
            BTE: BTH_I2673
            AAV: Aave_2207
            AJS: Ajs_2790
            HAR: HEAR1671(bioC)
            AZO: azo2633(tam)
            AFW: Anae109_0474
            MXA: MXAN_6659(tam)
            MLO: mll1606
            SME: SMc00225(tam)
            SMD: Smed_0581
            ATU: Atu0870(tam)
            ATC: AGR_C_1589
            RET: RHE_CH01186(tam)
            RLE: RL1316(tam)
            BME: BMEI0554
            BMF: BAB1_1473
            BMS: BR1455(tam)
            OAN: Oant_1719
            BJA: blr2748(tam)
            RPA: RPA3605
            RPB: RPB_1922
            RPC: RPC_2136
            RPD: RPD_3451
            RPE: RPE_2044
            NWI: Nwi_2481
            NHA: Nham_2909
            XAU: Xaut_1142
            RSQ: Rsph17025_0567
            MAG: amb4352
            SUS: Acid_4185
            MTU: Rv0294(tam)
            MTC: MT0307(tam)
            MBO: Mb0302(tam)
            MPA: MAP3790
            MAV: MAV_4859
            MSM: MSMEG_0629
            MVA: Mvan_0425
            MGI: Mflv_0316
            MMC: Mmcs_0386
            MKM: Mkms_0395
            MJL: Mjls_0374
            RHA: RHA1_ro02298 RHA1_ro05782
            SCO: SCO3132(SCE66.11c)
            SMA: SAV3570
            ART: Arth_2075
            AAU: AAur_2078(tam)
            NCA: Noca_3852
            FAL: FRAAL3382
            SEN: SACE_1508(tam)
            STP: Strop_1778
            RXY: Rxyl_0277
            ANA: all1988
            AVA: Ava_0005 Ava_0823 Ava_4335
            FJO: Fjoh_3939
            DRA: DR_0422
STRUCTURES  PDB: 2P35  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.144
            ExPASy - ENZYME nomenclature database: 2.1.1.144
            ExplorEnz - The Enzyme Database: 2.1.1.144
            ERGO genome analysis and discovery system: 2.1.1.144
            BRENDA, the Enzyme Database: 2.1.1.144
///
ENTRY       EC 2.1.1.145                Enzyme
NAME        trans-aconitate 3-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:(E)-prop-1-ene-1,2,3-tricarboxylate
            3'-O-methyltransferase
REACTION    S-adenosyl-L-methionine + trans-aconitate =
            S-adenosyl-L-homocysteine +
            (E)-2-(methoxycarbonylmethyl)butenedioate [RN:R05764]
ALL_REAC    R05764
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            trans-aconitate [CPD:C02341]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            (E)-2-(methoxycarbonylmethyl)butenedioate [CPD:C11515]
COMMENT     Also catalyses the formation of the methyl monoester of
            cis-aconitate, isocitrate and citrate, but more slowly. While the
            enzyme from Saccharomyces cerevisiae forms
            (E)-2-(methoxycarbonylmethyl)butenedioate as the product, that from
            Escherichia coli forms (E)-3-(methoxycarbonyl)-pent-2-enedioate and
            is therefore classified as a separate enzyme (cf. EC 2.1.1.144,
            trans-aconitate 2-methyltransferase)
REFERENCE   1  [PMID:10224113]
  AUTHORS   Cai H, Clarke S.
  TITLE     A novel methyltransferase catalyzes the methyl esterification of
            trans-aconitate in Escherichia coli.
  JOURNAL   J. Biol. Chem. 274 (1999) 13470-9.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:11329290]
  AUTHORS   Cai H, Strouse J, Dumlao D, Jung ME, Clarke S.
  TITLE     Distinct reactions catalyzed by bacterial and yeast trans-aconitate
            methyltransferases.
  JOURNAL   Biochemistry. 40 (2001) 2210-9.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.145
            ExPASy - ENZYME nomenclature database: 2.1.1.145
            ExplorEnz - The Enzyme Database: 2.1.1.145
            ERGO genome analysis and discovery system: 2.1.1.145
            BRENDA, the Enzyme Database: 2.1.1.145
///
ENTRY       EC 2.1.1.146                Enzyme
NAME        (iso)eugenol O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:isoeugenol O-methyltransferase
REACTION    S-adenosyl-L-methionine + isoeugenol = S-adenosyl-L-homocysteine +
            isomethyleugenol [RN:R07240]
ALL_REAC    R07240
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            isoeugenol [CPD:C10469]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            isomethyleugenol [CPD:C10478]
COMMENT     Acts on eugenol and chavicol as well as isoeugenol.
REFERENCE   1  [PMID:9439593]
  AUTHORS   Wang J, Pichersky E.
  TITLE     Characterization of S-adenosyl-L-methionine:(iso)eugenol
            O-methyltransferase involved in floral scent production in Clarkia
            breweri.
  JOURNAL   Arch. Biochem. Biophys. 349 (1998) 153-60.
  ORGANISM  Clarkia breweri
REFERENCE   2  [PMID:11884690]
  AUTHORS   Gang DR, Lavid N, Zubieta C, Chen F, Beuerle T, Lewinsohn E, Noel
            JP, Pichersky E.
  TITLE     Characterization of phenylpropene O-methyltransferases from sweet
            basil: facile change of substrate specificity and convergent
            evolution within a plant O-methyltransferase family.
  JOURNAL   Plant. Cell. 14 (2002) 505-19.
  ORGANISM  Clarkia breweri, Ocimum basilicum
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.146
            ExPASy - ENZYME nomenclature database: 2.1.1.146
            ExplorEnz - The Enzyme Database: 2.1.1.146
            ERGO genome analysis and discovery system: 2.1.1.146
            BRENDA, the Enzyme Database: 2.1.1.146
            CAS: 191744-33-9
///
ENTRY       EC 2.1.1.147                Enzyme
NAME        corydaline synthase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:protoberberine 13-C-methyltransferase
REACTION    S-adenosyl-L-methionine + palmatine + 2 NADPH + H+ =
            S-adenosyl-L-homocysteine + corydaline + 2 NADP+ [RN:R07241]
ALL_REAC    R07241
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            palmatine [CPD:C05315];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            corydaline [CPD:C15530];
            NADP+ [CPD:C00006]
COMMENT     Also acts on 7,8-dihydropalmatine.
REFERENCE   1
  AUTHORS   Rueffer, M., Bauer, W. and Zenk, M.H.
  TITLE     The formation of corydaline and related alkaloids in Corydalis cava
            in vivo and in vitro.
  JOURNAL   Canad. J. Chem. 72 (1994) 170-175.
  ORGANISM  Corydalis cava
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.147
            ExPASy - ENZYME nomenclature database: 2.1.1.147
            ExplorEnz - The Enzyme Database: 2.1.1.147
            ERGO genome analysis and discovery system: 2.1.1.147
            BRENDA, the Enzyme Database: 2.1.1.147
            CAS: 155807-67-3
///
ENTRY       EC 2.1.1.148                Enzyme
NAME        thymidylate synthase (FAD);
            Thy1;
            ThyX
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     5,10-methylenetetrahydrofolate,FADH2:dUMP C-methyltransferase
REACTION    5,10-methylenetetrahydrofolate + dUMP + FADH2 = dTMP +
            tetrahydrofolate + FAD [RN:R06613]
ALL_REAC    R06613
SUBSTRATE   5,10-methylenetetrahydrofolate [CPD:C00143];
            dUMP [CPD:C00365];
            FADH2 [CPD:C01352]
PRODUCT     dTMP [CPD:C00364];
            tetrahydrofolate [CPD:C00101];
            FAD [CPD:C00016]
COMMENT     FMN can replace FAD. Reaction shown is distinct from that of the
            classical thymidylate synthase, ThyA (EC 2.1.1.45).
REFERENCE   1  [PMID:12029065]
  AUTHORS   Myllykallio H, Lipowski G, Leduc D, Filee J, Forterre P, Liebl U.
  TITLE     An alternative flavin-dependent mechanism for thymidylate synthesis.
  JOURNAL   Science. 297 (2002) 105-7.
  ORGANISM  Helicobacter pylori, Campylobacter jejuni, Rickettsia prowazekii
            [GN:rpr], Borrelia burgdorferi [GN:bbu], Treponema pallidum
            [GN:tpa], Chlamydia sp., Mycobacterium tuberculosis, Pyrococcus
            abyssi [GN:pab], Pyrococcus horikoshii [GN:pho], Sulfolobus
            solfaraticus, Dictyostelium discoideum [GN:ddi]
PATHWAY     PATH: map00240  Pyrimidine metabolism
            PATH: map00670  One carbon pool by folate
ORTHOLOGY   KO: K03465  thymidylate synthase (FAD)
GENES       DDI: DDB_0214905(thyA)
            HPY: HP1533
            HPJ: jhp1421
            HPA: HPAG1_1383
            HAC: Hac_1786(thyX)
            WSU: WS2228
            TDN: Tmden_0017
            CJE: Cj0026c
            CJR: CJE0026(thyX)
            CJJ: CJJ81176_0053(thyX)
            CJU: C8J_0025
            CJD: JJD26997_0028(thyX)
            CFF: CFF8240_1800(thyX)
            CCV: CCV52592_2063(thyX)
            CHA: CHAB381_1762(thyX)
            CCO: CCC13826_1861(thyX)
            ABU: Abu_2330(thyX)
            NIS: NIS_1855
            SUN: SUN_2288
            GSU: GSU3106
            GME: Gmet_0378
            GUR: Gura_4063
            PCA: Pcar_2693
            PPD: Ppro_2649
            DVL: Dvul_0990
            DDE: Dde_2321
            LIP: LI1188(thyA)
            ADE: Adeh_1139
            AFW: Anae109_1187
            RPR: RP301(thyA)
            RCO: RC0405(thyA)
            RFE: RF_0491(thyX)
            RBE: RBE_0275(thyX)
            RAK: A1C_02260(thyX)
            RBO: A1I_06415(thyX)
            RRI: A1G_02310(thyX)
            OTS: OTBS_0340(thyX)
            WOL: WD1198
            WBM: Wbm0741
            AMA: AM170(thyL)
            APH: APH_0163(thyX)
            ERU: Erum6790(thy1)
            ERW: ERWE_CDS_07140(thyX)
            ERG: ERGA_CDS_07060(thyX)
            ECN: Ecaj_0686
            ECH: ECH_0317(thyX)
            NSE: NSE_0163(thyX)
            PUB: SAR11_0010(thyX)
            SIL: SPO1273(thyX)
            JAN: Jann_1091
            PDE: Pden_0934
            GOX: GOX1427
            GBE: GbCGDNIH1_1809
            ACR: Acry_0045
            RRU: Rru_A2792
            MGM: Mmc1_0404
            BCZ: BCZK3445(thyX)
            CPE: CPE2425
            CPF: CPF_2735(thyX)
            CPR: CPR_2421(thyX)
            CTC: CTC02620
            CNO: NT01CX_1095(thyX)
            CDF: CD0054(thyX)
            CBO: CBO3500(thyX)
            CBA: CLB_3559(thyX)
            CBH: CLC_3448(thyX)
            CBF: CLI_3686(thyX)
            CKL: CKL_2204(thyX)
            AMT: Amet_4498
            CHY: CHY_2336(thyX)
            DSY: DSY0449
            DRM: Dred_0195 Dred_1200
            CSC: Csac_1367
            MTU: Rv2754c(thyX)
            MTC: MT2824(thyX)
            MBO: Mb2775c
            MLE: ML1514
            MPA: MAP2865c
            MAV: MAV_3645(thyX)
            MSM: MSMEG_2683(thyX)
            MVA: Mvan_2386
            MGI: Mflv_4001
            MMC: Mmcs_2115
            MKM: Mkms_2161
            MJL: Mjls_2102
            CGL: NCgl1897(cgl1972)
            CGB: cg2162
            CEF: CE1865
            CDI: DIP1465
            CJK: jk1130
            RHA: RHA1_ro06746
            SCO: SCO5743(SC9A10.07)
            TWH: TWT616(thyX)
            TWS: TW633
            CMI: CMM_2037(thyX)
            TFU: Tfu_1387(thyX)
            FRA: Francci3_3547
            FAL: FRAAL5743(thyX)
            ACE: Acel_1504
            SEN: SACE_5902(thyX)
            STP: Strop_1388
            RXY: Rxyl_2633
            BBU: BBA76(thy1)
            BAF: BAPKO_2074(thyX)
            TPA: TP1007
            TDE: TDE0311
            SYN: sll1635
            SYW: SYNW0279(thyX)
            SYC: syc0504_d
            SYF: Synpcc7942_1044
            SYD: Syncc9605_0273
            SYE: Syncc9902_2071
            SYG: sync_0320(thyX)
            SYR: SynRCC307_2347(thyX)
            SYX: SynWH7803_0323(thyX)
            CYA: CYA_0237(thyX)
            CYB: CYB_1781(thyX)
            GVI: glr2321
            ANA: alr0515
            AVA: Ava_2917
            PMN: PMN2A_1609
            PMI: PMT9312_0245
            PMB: A9601_02651(thy1)
            PMC: P9515_02761(thy1)
            PMF: P9303_03851(thy1)
            PMG: P9301_02661(thy1)
            PME: NATL1_03211(thy1)
            CTE: CT1554
            CCH: Cag_0390
            CPH: Cpha266_2031
            PVI: Cvib_0423
            PLT: Plut_0366
            DET: DET1489(thyX)
            DEH: cbdb_A1457(thyX)
            DEB: DehaBAV1_1279
            DGE: Dgeo_2027
            TTH: TTC0731
            TTJ: TTHA1096
            AAE: aq_640(thy)
            TMA: TM0449
            TPT: Tpet_0471
            TME: Tmel_1909
            FNO: Fnod_1336
            HAL: VNG1325C
            HMA: rrnAC1121(thyX)
            PHO: PH0762
            PAB: PAB0861
            PFU: PF0540
            TKO: TK0870
            APE: APE_2064.1
            SMR: Smar_1078
            SSO: SSO0321
            STO: ST2215
            SAI: Saci_2347(thyX)
            MSE: Msed_1894
            PAI: PAE1837
            PIS: Pisl_1753
            PAS: Pars_0709
            NEQ: NEQ015
STRUCTURES  PDB: 2AF6  2CFA  2GQ2  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.148
            ExPASy - ENZYME nomenclature database: 2.1.1.148
            ExplorEnz - The Enzyme Database: 2.1.1.148
            ERGO genome analysis and discovery system: 2.1.1.148
            BRENDA, the Enzyme Database: 2.1.1.148
///
ENTRY       EC 2.1.1.149                Enzyme
NAME        myricetin O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:myricetin O-methyltransferase
REACTION    2 S-adenosyl-L-methionine + myricetin = 2 S-adenosyl-L-homocysteine
            + syringetin [RN:R06815 R06816]
ALL_REAC    R06815 R06816
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            myricetin [CPD:C10107]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            syringetin [CPD:C11620]
COMMENT     The enzyme from Catharanthus roseus (Madagascar periwinkle) is
            unusual as it carries out two methylations of the same substrate.
            Also catalyses the methylation of dihydromyricetin.
REFERENCE   1  [PMID:12482447]
  AUTHORS   Cacace S, Schroder G, Wehinger E, Strack D, Schmidt J, Schroder J.
  TITLE     A flavonol O-methyltransferase from Catharanthus roseus performing
            two sequential methylations.
  JOURNAL   Phytochemistry. 62 (2003) 127-37.
  ORGANISM  Catharanthus roseus
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.149
            ExPASy - ENZYME nomenclature database: 2.1.1.149
            ExplorEnz - The Enzyme Database: 2.1.1.149
            ERGO genome analysis and discovery system: 2.1.1.149
            BRENDA, the Enzyme Database: 2.1.1.149
///
ENTRY       EC 2.1.1.150                Enzyme
NAME        isoflavone 7-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:hydroxyisoflavone 7-O-methyltransferase
REACTION    S-adenosyl-L-methionine + a 7-hydroxyisoflavone =
            S-adenosyl-L-homocysteine + a 7-methoxyisoflavone [RN:R07375]
ALL_REAC    R07375 > R06794 R07724
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            7-hydroxyisoflavone [CPD:C15615]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            7-methoxyisoflavone [CPD:C15616]
COMMENT     The enzyme from alfalfa can methylate daidzein, genistein and
            6,7,4'-trihydroxyisoflavone but not flavones or flavanones.
REFERENCE   1
  AUTHORS   Edwards, R. and Dixon, R.A.
  TITLE     Isoflavone O-methyltransferase activities in elicitor-treated cell
            suspension cultures of Medicago sativa.
  JOURNAL   Phytochemistry 30 (1991) 2597-2606.
  ORGANISM  alfalfa
REFERENCE   2  [PMID:11006341]
  AUTHORS   He XZ, Dixon RA.
  TITLE     Genetic manipulation of isoflavone 7-O-methyltransferase enhances
            biosynthesis of 4'-O-methylated isoflavonoid phytoalexins and
            disease resistance in alfalfa.
  JOURNAL   Plant. Cell. 12 (2000) 1689-702.
  ORGANISM  alfalfa
REFERENCE   3  [PMID:8951042]
  AUTHORS   He XZ, Dixon RA.
  TITLE     Affinity chromatography, substrate/product specificity, and amino
            acid sequence analysis of an isoflavone O-methyltransferase from
            alfalfa (Medicago sativa L.).
  JOURNAL   Arch. Biochem. Biophys. 336 (1996) 121-9.
  ORGANISM  alfalfa
REFERENCE   4  [PMID:9484461]
  AUTHORS   He XZ, Reddy JT, Dixon RA.
  TITLE     Stress responses in alfalfa (Medicago sativa L). XXII. cDNA cloning
            and characterization of an elicitor-inducible isoflavone
            7-O-methyltransferase.
  JOURNAL   Plant. Mol. Biol. 36 (1998) 43-54.
  ORGANISM  alfalfa
REFERENCE   5  [PMID:11752378]
  AUTHORS   Liu CJ, Dixon RA.
  TITLE     Elicitor-induced association of isoflavone O-methyltransferase with
            endomembranes prevents the formation and 7-O-methylation of daidzein
            during isoflavonoid phytoalexin biosynthesis.
  JOURNAL   Plant. Cell. 13 (2001) 2643-58.
  ORGANISM  alfalfa
REFERENCE   6  [PMID:11224575]
  AUTHORS   Zubieta C, He XZ, Dixon RA, Noel JP.
  TITLE     Structures of two natural product methyltransferases reveal the
            basis for substrate specificity in plant O-methyltransferases.
  JOURNAL   Nat. Struct. Biol. 8 (2001) 271-9.
  ORGANISM  alfalfa
REFERENCE   7  [PMID:9484434]
  AUTHORS   Christensen AB, Gregersen PL, Olsen CE, Collinge DB.
  TITLE     A flavonoid 7-O-methyltransferase is expressed in barley leaves in
            response to pathogen attack.
  JOURNAL   Plant. Mol. Biol. 36 (1998) 219-27.
  ORGANISM  Hordeum vulgare [GN:ehvu]
PATHWAY     PATH: map00943  Isoflavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.150
            ExPASy - ENZYME nomenclature database: 2.1.1.150
            ExplorEnz - The Enzyme Database: 2.1.1.150
            ERGO genome analysis and discovery system: 2.1.1.150
            BRENDA, the Enzyme Database: 2.1.1.150
            CAS: 136111-54-1
///
ENTRY       EC 2.1.1.151                Enzyme
NAME        cobalt-factor II C20-methyltransferase;
            CbiL
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:cobalt-factor-II C20-methyltransferase
REACTION    S-adenosyl-L-methionine + cobalt-factor II =
            S-adenosyl-L-homocysteine + cobalt-factor III [RN:R05808]
ALL_REAC    R05808
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            cobalt-factor II
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            cobalt-factor III
COMMENT     Involved in the anaerobic biosynthesis of vitamin B12.
REFERENCE   1  [PMID:9778368]
  AUTHORS   Spencer P, Stolowich NJ, Sumner LW, Scott AI.
  TITLE     Definition of the redox states of cobalt-precorrinoids:
            investigation of the substrate and redox specificity of CbiL from
            Salmonella typhimurium.
  JOURNAL   Biochemistry. 37 (1998) 14917-27.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K03394  cobalt-factor-2 C20-methyltransferase
GENES       STY: STY2228(cbiL)
            STT: t0850(cbiL)
            SPT: SPA0847(cbiL)
            SEC: SC2032(cbiL)
            STM: STM2024(cbiL)
            PLU: plu2988(cbiL)
            LMO: lmo1203(cbiL)
            LMF: LMOf2365_1212(cobI)
            LIN: lin1166(cbiL)
            LWE: lwe1160(cbiL)
            CAC: CAC1379(cobI)
            CPE: CPE1223(cbiL)
            CPR: CPR_1237(cobI)
            CTC: CTC00735
            CNO: NT01CX_0578(cobI)
            FNU: FN0959
            TDE: TDE2657
            SYN: slr1879(cbiL)
            BFR: BF2191
            BFS: BF2245
            PGI: PG0480
            CTE: CT0388(cbiL)
            TTH: TT_P0011
            TTJ: TTHB054
            MJA: MJ0771
            MMP: MMP0319(cbiL)
            MAC: MA4262(cbiL)
            MBA: Mbar_A0626
            MMA: MM_0999
            MBU: Mbur_2359
            MTH: MTH1348
            MST: Msp_0038(cbiL)
            MSI: Msm_1351
            MKA: MK1038(cobF)
            AFU: AF0727(cbiL)
            HAL: VNG1551G(cbiL)
            HMA: rrnAC3000(cbiL)
            HWA: HQ1833A(cbiL)
            NPH: NP1122A(cbiL)
            TAC: Ta0658
            TVO: TVN0918
            PTO: PTO1433
            PAI: PAE0348(cbiF)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.151
            ExPASy - ENZYME nomenclature database: 2.1.1.151
            ExplorEnz - The Enzyme Database: 2.1.1.151
            ERGO genome analysis and discovery system: 2.1.1.151
            BRENDA, the Enzyme Database: 2.1.1.151
///
ENTRY       EC 2.1.1.152                Enzyme
NAME        precorrin-6A synthase (deacetylating);
            precorrin-6X synthase (deacetylating);
            CobF
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:precorrin-5 C1-methyltransferase
            (deacetylating)
REACTION    S-adenosyl-L-methionine + precorrin-5 + H2O =
            S-adenosyl-L-homocysteine + precorrin-6A + acetate [RN:R05219]
ALL_REAC    R05219
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            precorrin 5 [CPD:C06416];
            H2O [CPD:C00001]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            precorrin 6A [CPD:C06320];
            acetate [CPD:C00033]
COMMENT     In the aerobic cobalamin biosythesis pathway, four enzymes are
            involved in the conversion of precorrin-3A to precorrin-6A. The
            first of the four steps is carried out by EC 1.14.13.83,
            precorrin-3B synthase (CobG), yielding precorrin-3B as the product.
            This is followed by three methylation reactions, which introduce a
            methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; EC 2.1.1.133)
            and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to
            precorrin-4, precorrin-5 and precorrin-6A, respectively.
REFERENCE   1  [PMID:8226690]
  AUTHORS   Debussche L, Thibaut D, Cameron B, Crouzet J, Blanche F.
  TITLE     Biosynthesis of the corrin macrocycle of coenzyme B12 in Pseudomonas
            denitrificans.
  JOURNAL   J. Bacteriol. 175 (1993) 7430-40.
  ORGANISM  Pseudomonas denitrificans
REFERENCE   2  [PMID:12195810]
  AUTHORS   Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
  TITLE     The biosynthesis of adenosylcobalamin (vitamin B12).
  JOURNAL   Nat. Prod. Rep. 19 (2002) 390-412.
  ORGANISM  Pseudomonas denitrificans
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K02228  precorrin-6A synthase
GENES       PPU: PP_3763
            PPF: Pput_2000
            PST: PSPTO_2709
            PSB: Psyr_2442
            PSP: PSPPH_2598
            PFL: PFL_2249
            PFO: Pfl_2061
            PEN: PSEEN3208
            PMY: Pmen_4583
            MLO: mlr1461
            SME: SMc03194(cobF)
            RET: RHE_PE00456(cobF)
            RLE: pRL110632(cobF)
            BJA: blr3275(cobF)
            RPA: RPA2097(cobF)
            RPB: RPB_3174
            RPC: RPC_1896
            RPD: RPD_2326
            RPE: RPE_2230
            SIL: SPO2874(cobF)
            SIT: TM1040_2224
            RSP: RSP_2819(cobF)
            RSH: Rsph17029_1477
            RSQ: Rsph17025_1527
            JAN: Jann_2920
            RDE: RD1_3816(cobF)
            PDE: Pden_2542
            NAR: Saro_0332
            RRU: Rru_A2970
            MPA: MAP0888
            MAV: MAV_1065(cobF)
            MSM: MSMEG_5548(cobF)
            MVA: Mvan_0376
            MGI: Mflv_0361
            MMC: Mmcs_4338
            MKM: Mkms_4424
            MJL: Mjls_4718
            CDI: DIP0822
            NFA: nfa50210
            RHA: RHA1_ro02247
            SCO: SCO6971(SC6F7.24c)
            SMA: SAV1600(cobF)
            PAC: PPA1920
            NCA: Noca_2879
            TFU: Tfu_0320
            FRA: Francci3_2657
            FAL: FRAAL2802
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.152
            ExPASy - ENZYME nomenclature database: 2.1.1.152
            ExplorEnz - The Enzyme Database: 2.1.1.152
            ERGO genome analysis and discovery system: 2.1.1.152
            BRENDA, the Enzyme Database: 2.1.1.152
///
ENTRY       EC 2.1.1.153                Enzyme
NAME        vitexin 2"-O-rhamnoside 7-O-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:vitexin-2"-O-beta-L-rhamnoside
            7-O-methyltransferase
REACTION    S-adenosyl-L-methionine + vitexin 2"-O-beta-L-rhamnoside =
            S-adenosyl-L-homocysteine + 7-O-methylvitexin 2"-O-beta-L-rhamnoside
            [RN:R06824]
ALL_REAC    R06824
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            vitexin 2''-O-beta-L-rhamnoside [CPD:C12628]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            7-O-methylvitexin 2''-O-beta-L-rhamnoside [CPD:C12629]
COMMENT     The flavonoids vitexin and isovitexin 2"-O-arabinoside do not act as
            substrates for the enzyme from oats (Avena sativa).
REFERENCE   1  [PMID:6705789]
  AUTHORS   Knogge W, Weissenbock G.
  TITLE     Purification, characterization, and kinetic mechanism of
            S-adenosyl-L-methionine: vitexin 2&quot;-O-rhamnoside
            7-O-methyltransferase of Avena sativa L.
  JOURNAL   Eur. J. Biochem. 140 (1984) 113-8.
  ORGANISM  Avena sativa
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.153
            ExPASy - ENZYME nomenclature database: 2.1.1.153
            ExplorEnz - The Enzyme Database: 2.1.1.153
            ERGO genome analysis and discovery system: 2.1.1.153
            BRENDA, the Enzyme Database: 2.1.1.153
///
ENTRY       EC 2.1.1.154                Enzyme
NAME        isoliquiritigenin 2'-O-methyltransferase;
            chalcone OMT;
            CHMT
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:isoliquiritigenin 2'-O-methyltransferase
REACTION    S-adenosyl-L-methionine + isoliquiritigenin =
            S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin [RN:R07242]
ALL_REAC    R07242
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            isoliquiritigenin [CPD:C08650]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            2'-O-methylisoliquiritigenin [CPD:C15531]
COMMENT     Not identical to EC 2.1.1.65, licodione 2'-O-methyltransferase [2].
            While EC 2.1.1.154, isoliquiritigenin 2'-O-methyltransferase can use
            licodione as a substrate, EC 2.1.1.65 cannot use isoliquiritigenin
            as a substrate.
REFERENCE   1  [PMID:1731632]
  AUTHORS   Maxwell CA, Edwards R, Dixon RA.
  TITLE     Identification, purification, and characterization of
            S-adenosyl-L-methionine: isoliquiritigenin 2'-O-methyltransferase
            from alfalfa (Medicago sativa L.).
  JOURNAL   Arch. Biochem. Biophys. 293 (1992) 158-66.
  ORGANISM  alfalfa
REFERENCE   2  [PMID:9055445]
  AUTHORS   Ichimura M, Furuno T, Takahashi T, Dixon RA, Ayabe S.
  TITLE     Enzymic O-methylation of isoliquiritigenin and licodione in alfalfa
            and licorice cultures.
  JOURNAL   Phytochemistry. 44 (1997) 991-5.
  ORGANISM  alfalfa
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.154
            ExPASy - ENZYME nomenclature database: 2.1.1.154
            ExplorEnz - The Enzyme Database: 2.1.1.154
            ERGO genome analysis and discovery system: 2.1.1.154
            BRENDA, the Enzyme Database: 2.1.1.154
            CAS: 139317-14-9
///
ENTRY       EC 2.1.1.155                Enzyme
NAME        kaempferol 4'-O-methyltransferase;
            S-adenosyl-L-methionine:flavonoid 4'-O-methyltransferase;
            F 4'-OMT
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:kaempferol 4'-O-methyltransferase
REACTION    S-adenosyl-L-methionine + kaempferol = S-adenosyl-L-homocysteine +
            kaempferide [RN:R06807]
ALL_REAC    R06807
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            kaempferol [CPD:C05903]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            kaempferide [CPD:C10098]
COMMENT     The enzyme acts on the hydroxy group in the 4'-position of some
            flavones, flavanones and isoflavones. Kaempferol, apigenin and
            kaempferol triglucoside are substrates, as is genistein, which
            reacts more slowly. Compounds with an hydroxy group in the 3' and 4'
            positions, such as quercetin and eriodictyol, do not act as
            substrates. Similar to EC 2.1.1.75, apigenin 4'-O-methyltransferase
            and EC 2.1.1.83, 3,7-dimethylquercetin 4'-O-methyltransferase.
REFERENCE   1  [PMID:12899699]
  AUTHORS   Curir P, Lanzotti V, Dolci M, Dolci P, Pasini C, Tollin G.
  TITLE     Purification and properties of a new
            S-adenosyl-L-methionine:flavonoid 4'-O-methyltransferase from
            carnation (Dianthus caryophyllus L.).
  JOURNAL   Eur. J. Biochem. 270 (2003) 3422-31.
  ORGANISM  carnation
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.155
            ExPASy - ENZYME nomenclature database: 2.1.1.155
            ExplorEnz - The Enzyme Database: 2.1.1.155
            ERGO genome analysis and discovery system: 2.1.1.155
            BRENDA, the Enzyme Database: 2.1.1.155
///
ENTRY       EC 2.1.1.156                Enzyme
NAME        glycine/sarcosine N-methyltransferase;
            ApGSMT;
            glycine-sarcosine methyltransferase;
            GSMT;
            GMT;
            glycine sarcosine N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:sarcosine N-methyltransferase
REACTION    (1) S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine +
            sarcosine [RN:R00367];
            (2) S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine
            + N,N-dimethylglycine [RN:R07243]
ALL_REAC    R00367 R07243
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            glycine [CPD:C00037];
            sarcosine [CPD:C00213]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            sarcosine [CPD:C00213];
            N,N-dimethylglycine [CPD:C01026]
COMMENT     Cells of the oxygen-evolving halotolerant cyanobacterium
            Aphanocthece halophytica synthesize betaine from glycine by a
            three-step methylation process. This is the first enzyme and it
            leads to the formation of either sarcosine or N,N-dimethylglycine,
            which is further methylated to yield betaine
            (N,N,N-trimethylglycine) by the action of EC 2.1.1.157,
            sarcosine/dimethylglycine N-methyltransferase. Differs from EC
            2.1.1.20, glycine N-methyltransferase, as it can further methylate
            the product of the first reaction. Acetate, dimethylglycine and
            S-adenosyl-L-homocysteine can inhibit the reaction [3].
REFERENCE   1  [PMID:10896953]
  AUTHORS   Nyyssola A, Kerovuo J, Kaukinen P, von Weymarn N, Reinikainen T.
  TITLE     Extreme halophiles synthesize betaine from glycine by methylation.
  JOURNAL   J. Biol. Chem. 275 (2000) 22196-201.
  ORGANISM  Actinopolyspora halophila, Ectothiorhodospira halochloris
REFERENCE   2  [PMID:11319079]
  AUTHORS   Nyyssola A, Reinikainen T, Leisola M.
  TITLE     Characterization of glycine sarcosine N-methyltransferase and
            sarcosine dimethylglycine N-methyltransferase.
  JOURNAL   Appl. Environ. Microbiol. 67 (2001) 2044-50.
  ORGANISM  Ectothiorhodospira halochloris
REFERENCE   3  [PMID:12466265]
  AUTHORS   Waditee R, Tanaka Y, Aoki K, Hibino T, Jikuya H, Takano J, Takabe T,
            Takabe T.
  TITLE     Isolation and functional characterization of N-methyltransferases
            that catalyze betaine synthesis from glycine in a halotolerant
            photosynthetic organism Aphanothece halophytica.
  JOURNAL   J. Biol. Chem. 278 (2003) 4932-42.
  ORGANISM  Actinopolyspora halophila
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.156
            ExPASy - ENZYME nomenclature database: 2.1.1.156
            ExplorEnz - The Enzyme Database: 2.1.1.156
            ERGO genome analysis and discovery system: 2.1.1.156
            BRENDA, the Enzyme Database: 2.1.1.156
///
ENTRY       EC 2.1.1.157                Enzyme
NAME        sarcosine/dimethylglycine N-methyltransferase;
            ApDMT;
            sarcosine-dimethylglycine methyltransferase;
            SDMT;
            sarcosine dimethylglycine N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:N,N-dimethylglycine N-methyltransferase
REACTION    (1) S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine
            + N,N-dimethylglycine [RN:R07243];
            (2) S-adenosyl-L-methionine + N,N-dimethylglycine =
            S-adenosyl-L-homocysteine + betaine [RN:R07244]
ALL_REAC    R07243 R07244
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            sarcosine [CPD:C00213];
            N,N-dimethylglycine [CPD:C01026]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            N,N-dimethylglycine [CPD:C01026];
            betaine [CPD:C00719]
COMMENT     Cells of the oxygen-evolving halotolerant cyanobacterium
            Aphanocthece halophytica synthesize betaine from glycine by a
            three-step methylation process. The first enzyme, EC 2.1.1.156,
            glycine/sarcosine N-methyltransferase, leads to the formation of
            either sarcosine or N,N-dimethylglycine, which is further methylated
            to yield betaine (N,N,N-trimethylglycine) by the action of this
            enzyme. Both of these enzymes can catalyse the formation of
            N,N-dimethylglycine from sarcosine [3]. The reactions are strongly
            inhibited by S-adenosyl-L-homocysteine.
REFERENCE   1  [PMID:10896953]
  AUTHORS   Nyyssola A, Kerovuo J, Kaukinen P, von Weymarn N, Reinikainen T.
  TITLE     Extreme halophiles synthesize betaine from glycine by methylation.
  JOURNAL   J. Biol. Chem. 275 (2000) 22196-201.
  ORGANISM  Actinopolyspora halophila, Ectothiorhodospira halochloris
REFERENCE   2  [PMID:11319079]
  AUTHORS   Nyyssola A, Reinikainen T, Leisola M.
  TITLE     Characterization of glycine sarcosine N-methyltransferase and
            sarcosine dimethylglycine N-methyltransferase.
  JOURNAL   Appl. Environ. Microbiol. 67 (2001) 2044-50.
  ORGANISM  Ectothiorhodospira halochloris
REFERENCE   3  [PMID:12466265]
  AUTHORS   Waditee R, Tanaka Y, Aoki K, Hibino T, Jikuya H, Takano J, Takabe T,
            Takabe T.
  TITLE     Isolation and functional characterization of N-methyltransferases
            that catalyze betaine synthesis from glycine in a halotolerant
            photosynthetic organism Aphanothece halophytica.
  JOURNAL   J. Biol. Chem. 278 (2003) 4932-42.
  ORGANISM  Actinopolyspora halophila
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.157
            ExPASy - ENZYME nomenclature database: 2.1.1.157
            ExplorEnz - The Enzyme Database: 2.1.1.157
            ERGO genome analysis and discovery system: 2.1.1.157
            BRENDA, the Enzyme Database: 2.1.1.157
///
ENTRY       EC 2.1.1.158                Enzyme
NAME        7-methylxanthosine synthase;
            xanthosine methyltransferase;
            XMT;
            xanthosine:S-adenosyl-L-methionine methyltransferase;
            CtCS1;
            CmXRS1;
            CaXMT1;
            S-adenosyl-L-methionine:xanthosine 7-N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:xanthosine N7-methyltransferase
REACTION    S-adenosyl-L-methionine + xanthosine = S-adenosyl-L-homocysteine +
            7-methylxanthosine [RN:R07917]
ALL_REAC    R07917
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            xanthosine [CPD:C01762]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            7-methylxanthosine [CPD:C16352]
COMMENT     The enzyme is specific for xanthosine, as XMP and xanthine cannot
            act as substrates [2,4]. The enzyme does not have N1- or N3-
            methylation activity [2]. This is the first methylation step in the
            production of caffeine.
REFERENCE   1
  AUTHORS   Negishi, O., Ozawa, T. and Imagawa, H.
  TITLE     The role of xanthosine in the biosynthesis of caffeine in coffee
            plants.
  JOURNAL   Agric. Biol. Chem. 49 (1985) 2221-2222.
REFERENCE   2  [PMID:12860386]
  AUTHORS   Mizuno K, Kato M, Irino F, Yoneyama N, Fujimura T, Ashihara H.
  TITLE     The first committed step reaction of caffeine biosynthesis:
            7-methylxanthosine synthase is closely homologous to caffeine
            synthases in coffee (Coffea arabica L.).
  JOURNAL   FEBS. Lett. 547 (2003) 56-60.
REFERENCE   3  [PMID:12746542]
  AUTHORS   Uefuji H, Ogita S, Yamaguchi Y, Koizumi N, Sano H.
  TITLE     Molecular cloning and functional characterization of three distinct
            N-methyltransferases involved in the caffeine biosynthetic pathway
            in coffee plants.
  JOURNAL   Plant. Physiol. 132 (2003) 372-80.
REFERENCE   4  [PMID:16333668]
  AUTHORS   Yoneyama N, Morimoto H, Ye CX, Ashihara H, Mizuno K, Kato M.
  TITLE     Substrate specificity of N-methyltransferase involved in purine
            alkaloids synthesis is dependent upon one amino acid residue of the
            enzyme.
  JOURNAL   Mol. Genet. Genomics. 275 (2006) 125-35.
PATHWAY     PATH: map00232  Caffeine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.158
            ExPASy - ENZYME nomenclature database: 2.1.1.158
            ExplorEnz - The Enzyme Database: 2.1.1.158
            ERGO genome analysis and discovery system: 2.1.1.158
            BRENDA, the Enzyme Database: 2.1.1.158
///
ENTRY       EC 2.1.1.159                Enzyme
NAME        theobromine synthase;
            monomethylxanthine methyltransferase;
            MXMT;
            CTS1;
            CTS2;
            S-adenosyl-L-methionine:7-methylxanthine 3-N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:7-methylxanthine N3-methyltransferase
REACTION    S-adenosyl-L-methionine + 7-methylxanthine =
            S-adenosyl-L-homocysteine + 3,7-dimethylxanthine [RN:R07919]
ALL_REAC    R07919
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            7-methylxanthine [CPD:C16353]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            3,7-dimethylxanthine [CPD:C07480]
COMMENT     This is the third enzyme in the caffeine-biosynthesis pathway. This
            enzyme can also catalyse the conversion of paraxanthine into
            caffeine, although the paraxanthine pathway is considered to be a
            minor pathway for caffeine biosynthesis [2,3].
REFERENCE   1  [PMID:11108716]
  AUTHORS   Ogawa M, Herai Y, Koizumi N, Kusano T, Sano H.
  TITLE     7-Methylxanthine methyltransferase of coffee plants. Gene isolation
            and enzymatic properties.
  JOURNAL   J. Biol. Chem. 276 (2001) 8213-8.
REFERENCE   2  [PMID:12746542]
  AUTHORS   Uefuji H, Ogita S, Yamaguchi Y, Koizumi N, Sano H.
  TITLE     Molecular cloning and functional characterization of three distinct
            N-methyltransferases involved in the caffeine biosynthetic pathway
            in coffee plants.
  JOURNAL   Plant. Physiol. 132 (2003) 372-80.
REFERENCE   3  [PMID:16333668]
  AUTHORS   Yoneyama N, Morimoto H, Ye CX, Ashihara H, Mizuno K, Kato M.
  TITLE     Substrate specificity of N-methyltransferase involved in purine
            alkaloids synthesis is dependent upon one amino acid residue of the
            enzyme.
  JOURNAL   Mol. Genet. Genomics. 275 (2006) 125-35.
PATHWAY     PATH: map00232  Caffeine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.159
            ExPASy - ENZYME nomenclature database: 2.1.1.159
            ExplorEnz - The Enzyme Database: 2.1.1.159
            ERGO genome analysis and discovery system: 2.1.1.159
            BRENDA, the Enzyme Database: 2.1.1.159
///
ENTRY       EC 2.1.1.160                Enzyme
NAME        caffeine synthase;
            dimethylxanthine methyltransferase;
            3N-methyltransferase;
            DXMT;
            CCS1;
            S-adenosyl-L-methionine:3,7-dimethylxanthine 1-N-methyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
SYSNAME     S-adenosyl-L-methionine:3,7-dimethylxanthine N1-methyltransferase
REACTION    (1) S-adenosyl-L-methionine + 3,7-dimethylxanthine =
            S-adenosyl-L-homocysteine + 1,3,7-trimethylxanthine [RN:R07920];
            (2) S-adenosyl-L-methionine + 1,7-dimethylxanthine =
            S-adenosyl-L-homocysteine + 1,3,7-trimethylxanthine [RN:R07921];
            (3) S-adenosyl-L-methionine + 7-methylxanthine =
            S-adenosyl-L-homocysteine + 3,7-dimethylxanthine [RN:R07919]
ALL_REAC    R07919 R07920 R07921
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            3,7-dimethylxanthine [CPD:C07480];
            1,7-dimethylxanthine [CPD:C13747];
            7-methylxanthine [CPD:C16353]
PRODUCT     S-adenosyl-L-homocysteine [CPD:C00021];
            1,3,7-trimethylxanthine [CPD:C07481];
            3,7-dimethylxanthine [CPD:C07480]
COMMENT     Paraxanthine is the best substrate for this enzyme but the
            paraxanthine pathway is considered to be a minor pathway for
            caffeine biosynthesis [2,3].
REFERENCE   1  [PMID:10364410]
  AUTHORS   Kato M, Mizuno K, Fujimura T, Iwama M, Irie M, Crozier A, Ashihara
            H.
  TITLE     Purification and characterization of caffeine synthase from tea
            leaves.
  JOURNAL   Plant. Physiol. 120 (1999) 579-86.
REFERENCE   2  [PMID:12527364]
  AUTHORS   Mizuno K, Okuda A, Kato M, Yoneyama N, Tanaka H, Ashihara H,
            Fujimura T.
  TITLE     Isolation of a new dual-functional caffeine synthase gene encoding
            an enzyme for the conversion of 7-methylxanthine to caffeine from
            coffee (Coffea arabica L.).
  JOURNAL   FEBS. Lett. 534 (2003) 75-81.
REFERENCE   3  [PMID:12746542]
  AUTHORS   Uefuji H, Ogita S, Yamaguchi Y, Koizumi N, Sano H.
  TITLE     Molecular cloning and functional characterization of three distinct
            N-methyltransferases involved in the caffeine biosynthetic pathway
            in coffee plants.
  JOURNAL   Plant. Physiol. 132 (2003) 372-80.
REFERENCE   4  [PMID:10984041]
  AUTHORS   Kato M, Mizuno K, Crozier A, Fujimura T, Ashihara H.
  TITLE     Caffeine synthase gene from tea leaves.
  JOURNAL   Nature. 406 (2000) 956-7.
PATHWAY     PATH: map00232  Caffeine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.1.160
            ExPASy - ENZYME nomenclature database: 2.1.1.160
            ExplorEnz - The Enzyme Database: 2.1.1.160
            ERGO genome analysis and discovery system: 2.1.1.160
            BRENDA, the Enzyme Database: 2.1.1.160
///
ENTRY       EC 2.1.1.-                  Enzyme
CLASS       Transferases;
            Transferring one-carbon groups;
            Methyltransferases
REACTION    (1) L-Histidine + S-Adenosyl-L-methionine <=>
            N(pi)-Methyl-L-histidine + S-Adenosyl-L-homocysteine [RN:R01159];
            (2) 3-Hydroxyanthranilate + Activated methyl group <=>
            3-Methoxyanthranilate [RN:R02671];
            (3) 3-(2-Aminoethyl)-1H-indol-5-ol + Activated methyl group <=>
            5-Methoxytryptamine [RN:R02912];
            (4) N-Methyltyramine + S-Adenosyl-L-methionine <=> Hordenine +
            S-Adenosyl-L-homocysteine [RN:R03943];
            (5) Xanthurenic acid <=> 8-Methoxykynurenate [RN:R03955];
            (6) 2-Hydroxyestradiol-17beta + S-Adenosyl-L-methionine <=>
            2-Methoxyestradiol-17beta + S-Adenosyl-L-homocysteine [RN:R04764];
            (7) R + Se-Adenosylselenomethionine <=> CH3-R +
            Se-Adenosylselenohomocysteine [RN:R04939];
            (8) 2-Hexaprenyl-6-hydroxyphenol + S-Adenosyl-L-methionine <=>
            2-Hexaprenyl-6-methoxyphenol + S-Adenosyl-L-homocysteine
            [RN:R04981];
            (9) 2-Hexaprenyl-6-methoxy-1,4-benzoquinone +
            S-Adenosyl-L-methionine <=>
            2-Hexaprenyl-3-methyl-6-methoxy-1,4-benzoquinone +
            S-Adenosyl-L-homocysteine [RN:R04983];
            (10) 2-Octaprenyl-6-methoxy-1,4-benzoquinone +
            S-Adenosyl-L-methionine <=>
            2-Octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone +
            S-Adenosyl-L-homocysteine [RN:R04990];
            (11) 2-Demethylmenaquinone + S-Adenosyl-L-methionine <=> Menaquinone
            + S-Adenosyl-L-homocysteine [RN:R04993];
            (12) 2-Demethylmenaquinone + S-Adenosyl-L-methionine <=>
            Phylloquinol + S-Adenosyl-L-homocysteine [RN:R04994];
            (13) 2-Hydroxypropylphosphonate + Vitamin B12 <=> Methylcobalamin +
            Phosphonoacetaldehyde [RN:R05201];
            (14) 1-Phenanthrol + CH3-R <=> 1-Methoxyphenanthrene + R
            [RN:R05657];
            (15) Cobalt-precorrin 5 + S-Adenosyl-L-methionine + H2O <=>
            Cobalt-precorrin 6 + S-Adenosyl-L-homocysteine + Acetaldehyde
            [RN:R05811];
            (16) 2-Phytyl-1,4-naphthoquinone + S-Adenosyl-L-methionine <=>
            Phylloquinone + S-Adenosyl-L-homocysteine [RN:R06859];
            (17) 3,4-Dehydrorhodopin + S-Adenosyl-L-methionine <=>
            Anhydrorhodovibrin + S-Adenosyl-L-homocysteine [RN:R07521];
            (18) Hydroxyspirilloxanthin + S-Adenosyl-L-methionine <=>
            Spirilloxanthin + S-Adenosyl-L-homocysteine [RN:R07524];
            (19) Rhodopin + S-Adenosyl-L-methionine <=>
            3,4-Dihydroanhydrorhodovibrin + S-Adenosyl-L-homocysteine
            [RN:R07527];
            (20) 3',4'-Dihydrorhodovibrin + S-Adenosyl-L-methionine <=>
            3,4,3',4'-Tetrahydrospirilloxanthin + S-Adenosyl-L-homocysteine
            [RN:R07529];
            (21) Demethylspheroidene + S-Adenosyl-L-methionine <=> Spheroidene +
            S-Adenosyl-L-homocysteine [RN:R07535];
            (22) Cyanidin-3-(p-coumaroyl)-rutinoside-5-glucoside <=>
            Peonidin-3-(p-coumaroyl)-rutinoside-5-glucoside [RN:R07901];
            (23) Delphinidin-3-(p-coumaroyl)-rutinoside-5-glucoside <=>
            Petunidin-3-(p-coumaroyl)-rutinoside-5-glucoside [RN:R07905];
            (24) Petunidin-3-(p-coumaroyl)-rutinoside-5-glucoside <=>
            Malvidin-3-(p-coumaroyl)-rutinoside-5-glucoside [RN:R07906];
            (25) Delphinidin-3-(p-coumaroyl)-rutinoside-5-glucoside <=>
            Malvidin-3-(p-coumaroyl)-rutinoside-5-glucoside [RN:R07907]
SUBSTRATE   L-Histidine [CPD:C00135];
            S-Adenosyl-L-methionine [CPD:C00019];
            3-Hydroxyanthranilate [CPD:C00632];
            Activated methyl group [CPD:C10905];
            3-(2-Aminoethyl)-1H-indol-5-ol [CPD:C00780];
            N-Methyltyramine [CPD:C02442];
            Xanthurenic acid [CPD:C02470];
            2-Hydroxyestradiol-17beta [CPD:C05301];
            R [CPD:C05693];
            Se-Adenosylselenomethionine [CPD:C05691];
            2-Hexaprenyl-6-hydroxyphenol [CPD:C05801];
            2-Hexaprenyl-6-methoxy-1,4-benzoquinone [CPD:C05803];
            2-Octaprenyl-6-methoxy-1,4-benzoquinone [CPD:C05813];
            2-Demethylmenaquinone [CPD:C05818];
            2-Hydroxypropylphosphonate [CPD:C06452];
            Vitamin B12 [CPD:C05776];
            1-Phenanthrol [CPD:C11432];
            CH3-R [CPD:C05694];
            Cobalt-precorrin 5 [CPD:C11541];
            H2O [CPD:C00001];
            2-Phytyl-1,4-naphthoquinone [CPD:C13309]
PRODUCT     N(pi)-Methyl-L-histidine [CPD:C01152];
            S-Adenosyl-L-homocysteine [CPD:C00021];
            3-Methoxyanthranilate [CPD:C05831];
            5-Methoxytryptamine [CPD:C05659];
            Hordenine [CPD:C06199];
            8-Methoxykynurenate [CPD:C05830];
            2-Methoxyestradiol-17beta [CPD:C05302];
            CH3-R [CPD:C05694];
            Se-Adenosylselenohomocysteine [CPD:C05692];
            2-Hexaprenyl-6-methoxyphenol [CPD:C05802];
            2-Hexaprenyl-3-methyl-6-methoxy-1,4-benzoquinone [CPD:C05804];
            2-Octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone [CPD:C05814];
            Menaquinone [CPD:C00828];
            Phylloquinol [CPD:C06245];
            Methylcobalamin [CPD:C06453];
            Phosphonoacetaldehyde [CPD:C03167];
            1-Methoxyphenanthrene [CPD:C11433];
            R [CPD:C05693];
            Cobalt-precorrin 6 [CPD:C11542];
            Acetaldehyde [CPD:C00084];
            Phylloquinone [CPD:C02059]
///
ENTRY       EC 2.1.2.1                  Enzyme
NAME        glycine hydroxymethyltransferase;
            serine aldolase;
            threonine aldolase;
            serine hydroxymethylase;
            serine hydroxymethyltransferase;
            allothreonine aldolase;
            L-serine hydroxymethyltransferase;
            L-threonine aldolase;
            serine hydroxymethyltransferase;
            serine transhydroxymethylase
CLASS       Transferases;
            Transferring one-carbon groups;
            Hydroxymethyl-, formyl- and related transferases
SYSNAME     5,10-methylenetetrahydrofolate:glycine hydroxymethyltransferase
REACTION    5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate +
            L-serine [RN:R00945]
ALL_REAC    R00945;
            (other) R03284
SUBSTRATE   5,10-methylenetetrahydrofolate [CPD:C00143];
            glycine [CPD:C00037];
            H2O [CPD:C00001]
PRODUCT     tetrahydrofolate [CPD:C00101];
            L-serine [CPD:C00065]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also catalyses the reaction of
            glycine with acetaldehyde to form L-threonine, and with
            4-trimethylammoniobutanal to form
            3-hydroxy-N6,N6,N6-trimethyl-L-lysine.
REFERENCE   1  [PMID:5017703]
  AUTHORS   Akhtar M, el-Obeid HA.
  TITLE     Inactivation of serine transhydroxymethylase and threonine aldolase
            activities.
  JOURNAL   Biochim. Biophys. Acta. 258 (1972) 791-9.
  ORGANISM  Candida humicola
REFERENCE   2  [PMID:16748851]
  AUTHORS   Blakley RL.
  TITLE     A spectrophotometric study of the reaction catalysed by serine
            transhydroxymethylase.
  JOURNAL   Biochem. J. 77 (1960) 459-65.
  ORGANISM  rabbit
REFERENCE   3  [PMID:5808700]
  AUTHORS   Fujioka M.
  TITLE     Purification and properties of serine hydroxymethylase from soluble
            and mitochondrial fractions of rabbit liver.
  JOURNAL   Biochim. Biophys. Acta. 185 (1969) 338-49.
  ORGANISM  rabbit
REFERENCE   4  [PMID:5017702]
  AUTHORS   Kumagai H, Nagate T, Yoshida H, Yamada H.
  TITLE     Threonine aldolase from Candida humicola. II. Purification,
            crystallization and properties.
  JOURNAL   Biochim. Biophys. Acta. 258 (1972) 779-90.
  ORGANISM  rabbit
REFERENCE   5  [PMID:5699057]
  AUTHORS   Schirch L, Gross T.
  TITLE     Serine transhydroxymethylase. Identification as the threonine and
            allothreonine aldolases.
  JOURNAL   J. Biol. Chem. 243 (1968) 5651-5.
  ORGANISM  rabbit
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00310  Lysine degradation
            PATH: map00460  Cyanoamino acid metabolism
            PATH: map00670  One carbon pool by folate
            PATH: map00680  Methane metabolism
ORTHOLOGY   KO: K00600  glycine hydroxymethyltransferase
GENES       HSA: 6470(SHMT1) 6472(SHMT2)
            PTR: 452007(SHMT2)
            MCC: 701186(LOC701186)
            MMU: 108037(Shmt2) 20425(Shmt1)
            CFA: 489536(SHMT1)
            GGA: 416520(SHMT1)
            XLA: 380048(shmt1) 447193(MGC79128)
            XTR: 493265(shmt2)
            DRE: 394021(shmt1)
            SPU: 593509(LOC593509)
            DME: Dmel_CG3011
            CEL: C05D11.11(mel-32)
            ATH: AT1G22020(SHM6) AT4G13890(SHM5) AT4G13930(SHM4)
                 AT4G32520(SHM3) AT4G37930(SHM1)
            OSA: 4324773 4334048 4338868 4350456
            CME: CMI091C CMN332C CMO142C
            SCE: YBR263W(SHM1) YLR058C(SHM2)
            AGO: AGOS_ACR215C AGOS_AEL188W
            PIC: PICST_67292(SHM2) PICST_78806(SHM1)
            CGR: CAGL0F01749g CAGL0I09284g
            SPO: SPAC18G6.04c(shm2) SPAC24C9.12c
            ANI: AN3058.2
            AFM: AFUA_3G09320
            AOR: AO090005001302
            CNE: CNJ00410 CNJ00430
            DDI: DDB_0230072 DDB_0230073
            PFA: MAL13P1.67 PFL1720w
            CPV: cgd8_2610
            CHO: Chro.80306
            TAN: TA20940
            TPV: TP01_0390
            TET: TTHERM_00193410 TTHERM_00463450
            TCR: 509937.150 510407.90
            LMA: LmjF14.1320 LmjF28.2370
            ECO: b2551(glyA)
            ECJ: JW2535(glyA)
            ECE: Z3827(glyA)
            ECS: ECs3417
            ECC: c3073(glyA)
            ECI: UTI89_C2870(glyA)
            ECP: ECP_2552
            ECV: APECO1_3980(glyA)
            ECW: EcE24377A_2836(glyA)
            ECX: EcHS_A2704(glyA)
            STY: STY2802(glyA) STY3764
            STT: t0301(glyA) t3514
            SPT: SPA0311(glyA)
            SEC: SC2549(glyA)
            STM: STM2555(glyA)
            YPE: YPO2907(glyA)
            YPK: y1322(glyA)
            YPM: YP_2548(glyA)
            YPA: YPA_2347
            YPN: YPN_1232
            YPP: YPDSF_2251
            YPS: YPTB2869(glyA)
            YPI: YpsIP31758_1158(glyA)
            YEN: YE1047(glyA)
            SFL: SF2598(glyA)
            SFX: S2770(glyA)
            SFV: SFV_2599(glyA)
            SSN: SSON_2634(glyA)
            SBO: SBO_2579(glyA)
            SDY: SDY_2741(glyA)
            ECA: ECA3250(glyA) ECA4046
            PLU: plu3291(glyA)
            BUC: BU289(glyA)
            BAS: BUsg278(glyA)
            BAB: bbp268(glyA)
            BCC: BCc_178(glyA)
            WBR: WGLp501(glyA)
            SGL: SG1775
            ENT: Ent638_3036
            KPN: KPN_02876(glyA)
            SPE: Spro_3638
            BFL: Bfl536(glyA)
            BPN: BPEN_556(glyA)
            HIN: HI0889(glyA)
            HIT: NTHI1054(glyA)
            HIP: CGSHiEE_07585(glyA)
            HSO: HS_1627(glyA)
            PMU: PM0225(glyA)
            MSU: MS1295(glyA)
            APL: APL_0211(glyA)
            ASU: Asuc_1360
            XFA: XF0946
            XFT: PD1750(glyA)
            XCC: XCC0690(glyA)
            XCB: XC_3544
            XCV: XCV0794(glyA)
            XAC: XAC0743(glyA)
            XOO: XOO3860(glyA)
            XOM: XOO_3639(XOO3639)
            VCH: VC0941 VCA0278
            VCO: VC0395_0952(glyA-2) VC0395_A0465(glyA-1)
            VVU: VV1_0286 VV2_0188
            VVY: VV0898 VVA0693
            VPA: VP0715 VPA0803
            VFI: VF0695
            PPR: PBPRA0795(glyA) PBPRB1322
            PAE: PA2444(glyA2) PA4602(glyA3) PA5415(glyA1)
            PAU: PA14_33010(glyA2) PA14_60890(glyA) PA14_71460(glyA1)
            PPU: PP_0322(glyA-1) PP_0671(glyA-2)
            PPF: Pput_0344 Pput_0702
            PST: PSPTO_0461(glyA-1) PSPTO_2427 PSPTO_4632(glyA-2)
            PSB: Psyr_4270 Psyr_4712
            PSP: PSPPH_4327(glyA1) PSPPH_4750(glyA)
            PFL: PFL_5028(glyA) PFL_5346(glyA) PFL_5729(glyA)
            PFO: Pfl_2312 Pfl_4877 Pfl_5208
            PEN: PSEEN0806(glyA-1) PSEEN3863(glyA-3) PSEEN5162(glyA-2)
            PMY: Pmen_0759 Pmen_1344 Pmen_4132
            PSA: PST_0940(glyA3)
            PAR: Psyc_0290(glyA)
            PCR: Pcryo_0318
            PRW: PsycPRwf_2083
            ACI: ACIAD2255(glyA)
            ACB: A1S_2307
            SON: SO_3471(glyA)
            SDN: Sden_0631 Sden_1142
            SFR: Sfri_1033
            SAZ: Sama_1014
            SBL: Sbal_3162
            SBM: Shew185_3161
            SLO: Shew_1185
            SPC: Sputcn32_2780
            SSE: Ssed_1271
            SPL: Spea_1160
            SHE: Shewmr4_1094
            SHM: Shewmr7_1160
            SHN: Shewana3_1094
            SHW: Sputw3181_1232
            ILO: IL1872(glyA)
            CPS: CPS_0728(glyA1) CPS_2477(glyA2) CPS_3844(glyA3)
                 CPS_4031(glyA4)
            PHA: PSHAa2376(glyA)
            PAT: Patl_1299
            SDE: Sde_0417
            PIN: Ping_1438
            MAQ: Maqu_0841
            CBU: CBU_1419
            CBD: COXBU7E912_0577(glyA)
            LPN: lpg0725(glyA3)
            LPF: lpl0762(glyA)
            LPP: lpp0791(glyA)
            MCA: MCA1660(glyA)
            FTU: FTT1241(glyA)
            FTF: FTF1241(glyA)
            FTW: FTW_0703(glyA)
            FTL: FTL_0703
            FTH: FTH_0705(glyA)
            FTA: FTA_0743(glyA)
            FTN: FTN_1259(glyA)
            TCX: Tcr_1402
            NOC: Noc_2027
            AEH: Mlg_0373
            HHA: Hhal_0902
            HCH: HCH_03860 HCH_05959
            CSA: Csal_2617
            ABO: ABO_2176(glyA)
            MMW: Mmwyl1_2283
            AHA: AHA_3336(glyA)
            DNO: DNO_0476(glyA)
            BCI: BCI_0004(glyA)
            CRP: CRP_031
            RMA: Rmag_0632
            VOK: COSY_0584(glyA)
            NME: NMB1055
            NMA: NMA1254(glyA)
            NMC: NMC1017(glyA)
            NGO: NGO0866
            CVI: CV_1286(glyA)
            RSO: RSc0729(glyA1) RSp0055(glyA2)
            REU: Reut_A0790 Reut_B4822
            REH: H16_A2834(glyA)
            RME: Rmet_2680
            BMA: BMA2075(glyA-1) BMAA0471(glyA-2)
            BMV: BMASAVP1_0710(glyA-2) BMASAVP1_A0834(glyA-1)
            BML: BMA10299_1006(glyA-2) BMA10299_A2668(glyA-1)
            BMN: BMA10247_1942(glyA-1) BMA10247_A1979(glyA-2)
            BXE: Bxe_A3914 Bxe_B1585
            BVI: Bcep1808_0738 Bcep1808_3423 Bcep1808_3948 Bcep1808_7032
            BUR: Bcep18194_A3895 Bcep18194_B0571 Bcep18194_B2754
            BCN: Bcen_0323 Bcen_3283
            BCH: Bcen2424_0806 Bcen2424_5085
            BAM: Bamb_0683 Bamb_4497 Bamb_5200 Bamb_5759
            BPS: BPSL2758(glyA) BPSS0547(glyA)
            BPM: BURPS1710b_3250(glyA) BURPS1710b_A2106(glyA)
            BPL: BURPS1106A_3234(glyA) BURPS1106A_A0740(glyA)
            BPD: BURPS668_3196(glyA) BURPS668_A0828(glyA)
            BTE: BTH_I1379 BTH_II1868(glyA)
            PNU: Pnuc_0279
            BPE: BP2952(glyA)
            BPA: BPP0701(glyA) BPP3875(glyA)
            BBR: BB0708(glyA) BB4348(glyA)
            RFR: Rfer_2658
            POL: Bpro_2874
            PNA: Pnap_2907
            AAV: Aave_2992
            AJS: Ajs_1660
            VEI: Veis_4246
            MPT: Mpe_A2938 Mpe_A3262
            HAR: HEAR2380(glyA)
            MMS: mma_2443(glyA)
            NEU: NE1433(glyA)
            NET: Neut_1552
            NMU: Nmul_A0004
            EBA: ebA1042(glyA)
            AZO: azo2801(glyA)
            DAR: Daro_0603
            TBD: Tbd_2165
            MFA: Mfla_1917
            HPY: HP0183(glyA)
            HPJ: jhp0171(glyA)
            HPA: HPAG1_0180
            HHE: HH1665(glyA)
            HAC: Hac_0369(glyA)
            WSU: WS0085(glyA3)
            TDN: Tmden_1274 Tmden_1947
            CJE: Cj0402(glyA)
            CJR: CJE0451(glyA)
            CJJ: CJJ81176_0425(glyA)
            CJU: C8J_0377(glyA)
            CJD: JJD26997_1555(glyA)
            CFF: CFF8240_1141(glyA)
            CCV: CCV52592_1350(glyA)
            CHA: CHAB381_1647(glyA)
            CCO: CCC13826_0226(glyA) CCC13826_1692
            ABU: Abu_0653(glyA1) Abu_1460(glyA2)
            NIS: NIS_1178(glyA)
            SUN: SUN_0477(glyA)
            GSU: GSU1607(glyA)
            GME: Gmet_1605
            GUR: Gura_1881
            PCA: Pcar_1442
            PPD: Ppro_1748
            DVU: DVU1203(glyA)
            DVL: Dvul_1854
            DDE: Dde_2432
            LIP: LI0159(glyA)
            BBA: Bd2007(glyA)
            DPS: DP1875(glyA)
            ADE: Adeh_2744
            AFW: Anae109_2733
            MXA: MXAN_4766(glyA)
            SAT: SYN_02367
            SFU: Sfum_1377
            RPR: RP743(glyA)
            RTY: RT0728(glyA)
            RCO: RC1146(glyA)
            RFE: RF_1188(glyA)
            RBE: RBE_1308(glyA)
            RAK: A1C_05770(glyA)
            RBO: A1I_00320(glyA)
            RCM: A1E_04810(glyA)
            RRI: A1G_06305(glyA)
            OTS: OTBS_0253(glyA)
            WOL: WD1035(glyA)
            WBM: Wbm0005
            AMA: AM164(glyA)
            APH: APH_0154(glyA)
            ERU: Erum6840(glyA)
            ERW: ERWE_CDS_07190(glyA)
            ERG: ERGA_CDS_07110(glyA)
            ECN: Ecaj_0692
            ECH: ECH_0311(glyA)
            NSE: NSE_0218(glyA)
            PUB: SAR11_1048(glyA)
            MLO: mlr6114 mlr8400
            MES: Meso_1134
            PLA: Plav_0608 Plav_2908
            SME: SMa2135(glyA2) SMc01770(glyA1)
            SMD: Smed_0816 Smed_2096
            ATU: Atu1165(glyA) Atu4314(glyA)
            ATC: AGR_C_2156(shmT) AGR_L_1099(shmT)
            RET: RHE_CH01508(glyA)
            RLE: RL1620(glyA) RL3034(glyA)
            BME: BMEI1191 BMEI1192
            BMF: BAB1_0787(glyA)
            BMS: BR0765(glyA)
            BMB: BruAb1_0781(glyA)
            BOV: BOV_0758(glyA)
            OAN: Oant_2530
            BJA: bll5033(glyA)
            BRA: BRADO4430(glyA)
            BBT: BBta_4649(glyA)
            RPA: RPA2724(glyA1) RPA2796(glyA2)
            RPB: RPB_2634
            RPC: RPC_2659
            RPD: RPD_2305 RPD_2671
            RPE: RPE_2808
            NWI: Nwi_1727
            NHA: Nham_1814
            BHE: BH07540(glyA)
            BQU: BQ05390(glyA)
            BBK: BARBAKC583_0629(glyA)
            XAU: Xaut_0870 Xaut_4276
            CCR: CC_1357
            SIL: SPO1572(glyA-1) SPO2940(glyA-2) SPO3529(glyA-3)
            SIT: TM1040_1579
            RSP: RSP_0823(SHMT)
            RSH: Rsph17029_2481
            RSQ: Rsph17025_0354
            JAN: Jann_2079 Jann_2991
            RDE: RD1_1165(glyA) RD1_3991(glyA) RD1_4249(glyA)
            PDE: Pden_0920
            MMR: Mmar10_1537
            HNE: HNE_2060(glyA)
            ZMO: ZMO1201(glyA)
            NAR: Saro_2240
            SAL: Sala_0791
            SWI: Swit_1131
            ELI: ELI_05650
            GOX: GOX2310
            GBE: GbCGDNIH1_1008
            ACR: Acry_2123
            RRU: Rru_A1142 Rru_A1827
            MAG: amb2339
            MGM: Mmc1_0169
            ABA: Acid345_1264
            SUS: Acid_7017
            BSU: BG10944(glyA)
            BHA: BH3765(glyA)
            BAN: BA5558(glyA)
            BAR: GBAA5558(glyA)
            BAT: BAS5165
            BCE: BC5316(glyA)
            BCA: BCE_5441(glyA)
            BCZ: BCZK5015(glyA)
            BCY: Bcer98_3835
            BTK: BT9727_4998(glyA)
            BTL: BALH_4816(glyA)
            BLI: BL03991(glyA)
            BLD: BLi03935(glyA)
            BCL: ABC3863(glyA)
            BAY: RBAM_034060(glyA)
            BPU: BPUM_3335(glyA)
            OIH: OB2985(glyA)
            GKA: GK3369(glyA)
            SAU: SA1915(glyA)
            SAV: SAV2113(glyA)
            SAM: MW2037(glyA)
            SAR: SAR2201(glyA)
            SAS: SAS2016
            SAC: SACOL2105(glyA)
            SAB: SAB1997c(glyA)
            SAA: SAUSA300_2067(glyA)
            SAO: SAOUHSC_02354
            SAJ: SaurJH9_2149
            SAH: SaurJH1_2187
            SEP: SE1710
            SER: SERP1719(glyA)
            SHA: SH0922(glyA)
            SSP: SSP0771
            LMO: lmo2539(glyA)
            LMF: LMOf2365_2512(glyA)
            LIN: lin2683(glyA)
            LWE: lwe2488(glyA)
            LLA: L0082(glyA)
            LLC: LACR_0617
            LLM: llmg_0563(glyA)
            SPY: SPy_1145(glyA)
            SPZ: M5005_Spy_0867(glyA)
            SPM: spyM18_1105(glyA)
            SPG: SpyM3_0803
            SPS: SPs1002
            SPH: MGAS10270_Spy0981(glyA)
            SPI: MGAS10750_Spy1016(glyA)
            SPJ: MGAS2096_Spy0941(glyA)
            SPK: MGAS9429_Spy0984(glyA)
            SPF: SpyM50923(glyA)
            SPA: M6_Spy0863
            SPB: M28_Spy0841(glyA)
            SPN: SP_1024
            SPR: spr0928(glyA)
            SPD: SPD_0910(glyA)
            SAG: SAG1074
            SAN: gbs1106(glyA)
            SAK: SAK_1160(glyA)
            SMU: SMU.1082(glyA)
            STC: str0755(glyA)
            STL: stu0755(glyA)
            STE: STER_0796
            SSA: SSA_1155(glyA)
            SSU: SSU05_0852
            SSV: SSU98_0850
            SGO: SGO_1151(glyA)
            LPL: lp_2375(glyA)
            LJO: LJ0263
            LAC: LBA0261(glyA)
            LSA: LSA1134(glyA)
            LSL: LSL_0878(glyA)
            LBR: LVIS_1287
            LCA: LSEI_1158
            LGA: LGAS_0256
            LRE: Lreu_0455
            PPE: PEPE_1327
            EFA: EF2550(glyA)
            OOE: OEOE_0778
            LME: LEUM_0788
            STH: STH1917
            CAC: CAC2264(glyA)
            CPE: CPE1929(glyA)
            CPF: CPF_2184(glyA)
            CPR: CPR_1895(glyA)
            CNO: NT01CX_1853(glyA)
            CTH: Cthe_1058
            CDF: CD2726(glyA) CD2834(glyA)
            CBO: CBO2595(glyA)
            CBA: CLB_2536(glyA)
            CBH: CLC_2467(glyA)
            CBF: CLI_2658(glyA)
            CBE: Cbei_1868
            CKL: CKL_1284(glyA)
            AMT: Amet_2365 Amet_3116
            CHY: CHY_2557(glyA)
            DSY: DSY4927
            DRM: Dred_3162
            SWO: Swol_2392
            CSC: Csac_2061
            TTE: TTE2130(glyA)
            MTA: Moth_2390
            MGE: MG_394(glyA)
            MPN: MPN576(glyA)
            MPU: MYPU_3390(glyA)
            MPE: MYPE2730
            MGA: MGA_1146(glyA)
            MMY: MSC_0894(glyA)
            MMO: MMOB4710(glyA)
            MHY: mhp154(glyA)
            MHJ: MHJ_0218(glyA)
            MHP: MHP7448_0224(glyA)
            MSY: MS53_0305(glyA)
            MCP: MCAP_0075(glyA)
            POY: PAM181(glyA)
            AYW: AYWB_538(glyA)
            MFL: Mfl106
            MTU: Rv0070c(glyA2) Rv1093(glyA1)
            MTC: MT0076(glyA-1) MT1125(glyA-2)
            MBO: Mb0071c(glyA2) Mb1123(glyA1)
            MBB: BCG_0101c(glyA2) BCG_1153(glyA1)
            MLE: ML1953(glyA)
            MPA: MAP2699c(glyA)
            MAV: MAV_1215(glyA)
            MSM: MSMEG_5249(glyA)
            MVA: Mvan_4656
            MGI: Mflv_2060
            MMC: Mmcs_4131
            MKM: Mkms_4206
            MJL: Mjls_4362
            CGL: NCgl0954(cgl0996)
            CGB: cg1133(glyA)
            CEF: CE1058(glyA)
            CDI: DIP0932(glyA)
            CJK: jk1465(glyA)
            NFA: nfa48130(glyA)
            RHA: RHA1_ro01820(glyA1) RHA1_ro02933(glyA2) RHA1_ro05335(glyA3)
                 RHA1_ro05859(glyA4)
            SCO: SCO4837(glyA1) SCO5470(glyA2)
            SMA: SAV2775(glyA1) SAV2908(glyA2) SAV3419(glyA3)
            TWH: TWT635(glyA)
            TWS: TW655(glyA)
            LXX: Lxx18640(glyA)
            CMI: CMM_2522(glyA)
            ART: Arth_0767 Arth_1115 Arth_3705
            AAU: AAur_1227(glyA) AAur_3825(glyA) AAur_4004(glyA)
            PAC: PPA0369
            NCA: Noca_2352
            TFU: Tfu_2353
            FRA: Francci3_0624 Francci3_3717
            FAL: FRAAL1125(glyA) FRAAL5942(glyA)
            ACE: Acel_1537
            KRA: Krad_3981
            SEN: SACE_4495(glyA2) SACE_5702(glyA2)
            STP: Strop_2093
            BLO: BL1035(glyA)
            BAD: BAD_0902(glyA)
            RXY: Rxyl_0469 Rxyl_1649
            RBA: RB6215(glyA)
            CTR: CT432(glyA)
            CTA: CTA_0472(glyA)
            CMU: TC0716
            CPN: CPn0521(glyA)
            CPA: CP0232
            CPJ: CPj0521(glyA)
            CPT: CpB0542
            CCA: CCA00224(glyA)
            CAB: CAB220(glyA)
            CFE: CF0782(glyA)
            PCU: pc0444(glyA)
            BGA: BG0614(glyA)
            BAF: BAPKO_0634(glyA)
            TPA: TP0329
            TDE: TDE2668(glyA)
            LIL: LA1409(glyA)
            LIC: LIC12335(glyA)
            LBJ: LBJ_2130(glyA)
            LBL: LBL_2127(glyA)
            SYN: sll1931(glyA)
            SYW: SYNW0259(glyA)
            SYC: syc1231_d(gylA)
            SYF: Synpcc7942_0282
            SYD: Syncc9605_0253
            SYE: Syncc9902_2091
            SYG: sync_0300(glyA)
            SYR: SynRCC307_2328(glyA)
            SYX: SynWH7803_0303(glyA)
            CYA: CYA_2015(glyA)
            CYB: CYB_2810(glyA)
            TEL: tlr2127(gylA)
            GVI: glr4369(gylA)
            ANA: alr4806
            AVA: Ava_2076
            PMA: Pro0290(glyA)
            PMM: PMM0258(glyA)
            PMT: PMT1847(glyA)
            PMN: PMN2A_1624
            PMI: PMT9312_0260
            PMB: A9601_02801(glyA)
            PMC: P9515_02911(glyA)
            PMF: P9303_24721(glyA)
            PMG: P9301_02811(glyA)
            PMH: P9215_02821(glyA)
            PME: NATL1_03361(glyA)
            TER: Tery_2660
            BTH: BT_0738
            BFR: BF2204
            BFS: BF2258(glyA)
            PGI: PG0042(glyA)
            SRU: SRU_0775(glyA)
            CHU: CHU_3633(glyA)
            GFO: GFO_2262(glyA)
            FJO: Fjoh_3410
            FPS: FP0681(glyA)
            CTE: CT1590(glyA)
            CCH: Cag_1789
            CPH: Cpha266_0601
            PVI: Cvib_1381
            PLT: Plut_1590
            DET: DET0436(glyA)
            DEH: cbdb_A390(glyA)
            DEB: DehaBAV1_0413
            RRS: RoseRS_0389
            RCA: Rcas_1155
            DRA: DR_0038
            DGE: Dgeo_0221
            TTH: TTC1160
            TTJ: TTHA1524
            AAE: aq_479(glyA)
            TMA: TM0720
            TPT: Tpet_0209
            TME: Tmel_0686
            FNO: Fnod_0085
            MJA: MJ1597(glyA)
            MAE: Maeo_1046
            MAC: MA3520(glyA)
            MBA: Mbar_A2316
            MMA: MM_0442
            MBU: Mbur_1813
            MTP: Mthe_1241
            MHU: Mhun_0023
            MEM: Memar_1833
            MBN: Mboo_2187
            MTH: MTH1380(glyA)
            MST: Msp_1475(glyA)
            MSI: Msm_1337
            MKA: MK0122(glyA)
            HAL: VNG1414G(glyA)
            HMA: rrnAC0999(glyA)
            HWA: HQ2791A(glyA)
            NPH: NP2050A(glyA)
            TAC: Ta0811 Ta1509
            TVO: TVN0047 TVN0796
            PTO: PTO0611 PTO0858
            PHO: PH1654
            PAB: PAB2018(glyA)
            PFU: PF1778
            TKO: TK0528
            RCI: RCIX1736(glyA)
            APE: APE_1962.1
            IHO: Igni_1091
            HBU: Hbut_1252
            SSO: SSO0530(glyA)
            STO: ST1354
            SAI: Saci_1358(glyA)
            MSE: Msed_1650
            PAI: PAE0798
            PIS: Pisl_1090
            PCL: Pcal_0014
            PAS: Pars_0048
STRUCTURES  PDB: 1BJ4  1DFO  1EJI  1EQB  1KKJ  1KKP  1KL1  1KL2  1LS3  1RV3  
                 1RV4  1RVU  1RVY  1YJS  1YJY  1YJZ  2A7V  2DKJ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.2.1
            ExPASy - ENZYME nomenclature database: 2.1.2.1
            ExplorEnz - The Enzyme Database: 2.1.2.1
            ERGO genome analysis and discovery system: 2.1.2.1
            BRENDA, the Enzyme Database: 2.1.2.1
            CAS: 9029-83-8
///
ENTRY       EC 2.1.2.2                  Enzyme
NAME        phosphoribosylglycinamide formyltransferase;
            2-amino-N-ribosylacetamide 5'-phosphate transformylase;
            GAR formyltransferase;
            GAR transformylase;
            glycinamide ribonucleotide transformylase;
            GAR TFase;
            5,10-methenyltetrahydrofolate:2-amino-N-ribosylacetamide
            ribonucleotide transformylase
CLASS       Transferases;
            Transferring one-carbon groups;
            Hydroxymethyl-, formyl- and related transferases
SYSNAME     10-formyltetrahydrofolate:5'-phosphoribosylglycinamide
            N-formyltransferase
REACTION    10-formyltetrahydrofolate + N1-(5-phospho-D-ribosyl)glycinamide =
            tetrahydrofolate + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide
            [RN:R04325]
ALL_REAC    R04325;
            (other) R04326
SUBSTRATE   10-formyltetrahydrofolate [CPD:C00234];
            N1-(5-phospho-D-ribosyl)glycinamide [CPD:C03838]
PRODUCT     tetrahydrofolate [CPD:C00101];
            N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide [CPD:C04376]
REFERENCE   1  [PMID:13672969]
  AUTHORS   HARTMAN SC, BUCHANAN JM.
  TITLE     Biosynthesis of the purines. XXVI. The identification of the formyl
            donors of the transformylation reactions.
  JOURNAL   J. Biol. Chem. 234 (1959) 1812-6.
  ORGANISM  avian
REFERENCE   2  [PMID:7284307]
  AUTHORS   Smith GK, Benkovic PA, Benkovic SJ.
  TITLE     L(-)-10-Formyltetrahydrofolate is the cofactor for glycinamide
            ribonucleotide transformylase from chicken liver.
  JOURNAL   Biochemistry. 20 (1981) 4034-6.
  ORGANISM  chicken [GN:gga]
REFERENCE   3  [PMID:13502326]
  AUTHORS   WARREN L, BUCHANAN JM.
  TITLE     Biosynthesis of the purines. XIX. 2-Amino-N-ribosylacetamide
            5'-phosphate (glycinamide ribotide) transformylase.
  JOURNAL   J. Biol. Chem. 229 (1957) 613-26.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00670  One carbon pool by folate
ORTHOLOGY   KO: K00601  phosphoribosylglycinamide formyltransferase
GENES       HSA: 2618(GART)
            MMU: 14450(Gart)
            CFA: 487740(LOC487740)
            BTA: 281183(GART)
            GGA: 395315(GART)
            DME: Dmel_CG31628(ade3)
            CEL: F38B6.4(GARS\\/AIRS\\/GART)
            ATH: AT1G31220
            OSA: 4338261 4345953
            CME: CMT058C
            SCE: YDR408C(ADE8)
            AGO: AGOS_AAR120C
            PIC: PICST_34864(PUR3)
            CGR: CAGL0F02761g
            AFM: AFUA_2G10855
            DDI: DDB_0230085(purN)
            ECO: b2500(purN)
            ECJ: JW2485(purN)
            ECE: Z3763(purN)
            ECS: ECs3362
            ECC: c3018(purN)
            ECI: UTI89_C2816(purN)
            ECP: ECP_2502
            ECV: APECO1_4069(purN)
            ECW: EcE24377A_2783(purN)
            ECX: EcHS_A2635
            STY: STY2741(purN)
            STT: t0357(purN)
            SPT: SPA0367(purN)
            SEC: SC2497(purN)
            STM: STM2500(purN)
            YPE: YPO2829(purN)
            YPK: y1406(purN)
            YPM: YP_2697(purN)
            YPA: YPA_2266
            YPN: YPN_1309
            YPP: YPDSF_2179
            YPS: YPTB2796(purN)
            YPI: YpsIP31758_1233(purN)
            YEN: YE1125(purN)
            SFL: SF2544(purN)
            SFX: S2693(purN)
            SFV: SFV_2545(purN)
            SSN: SSON_2582(purN)
            SBO: SBO_2521(purN)
            SDY: SDY_2689(purN)
            ECA: ECA1253(purN)
            PLU: plu2761(purN)
            HIN: HI1428(purN)
            HIT: NTHI1706(purN)
            HIP: CGSHiEE_04720(purN)
            HIQ: CGSHiGG_01010(purN)
            HSO: HS_0913(purN)
            PMU: PM0020(purN)
            MSU: MS0627(purN)
            XFA: XF0585
            XFT: PD1566(purN)
            XCC: XCC2791(purN)
            XCB: XC_1322
            XCV: XCV1269(purT) XCV3106(purN)
            XAC: XAC2961(purN)
            XOO: XOO1294(purN)
            XOM: XOO_1195(XOO1195)
            VCH: VC2227
            VCO: VC0395_A1820(purN)
            VVU: VV1_1899(purN)
            VVY: VV2516(purN)
            VPA: VP2286
            VFI: VF1929
            PPR: PBPRA2911
            PAE: PA0944(purN)
            PAU: PA14_52050(purN)
            PAP: PSPA7_4565(purN)
            PPU: PP_1664(purN)
            PST: PSPTO_1699(purN)
            PSB: Psyr_3690
            PSP: PSPPH_3711(purN)
            PFL: PFL_4441(purN)
            PFO: Pfl_1632
            PEN: PSEEN1369(purN)
            PAR: Psyc_1625(purN)
            PCR: Pcryo_1857
            ACI: ACIAD2635(purN)
            SON: SO_2761(purN)
            SDN: Sden_2095
            SFR: Sfri_1451
            SAZ: Sama_2098
            SBL: Sbal_1734
            SLO: Shew_1512
            SHE: Shewmr4_2381
            SHM: Shewmr7_2453
            SHN: Shewana3_2546
            SHW: Sputw3181_2427
            ILO: IL1662(purN)
            CPS: CPS_3197(purN)
            PHA: PSHAa1948(purN)
            PAT: Patl_2490
            SDE: Sde_0893
            PIN: Ping_1068
            MAQ: Maqu_0945
            CBU: CBU_1737(purN)
            CBD: COXBU7E912_0264(purN)
            LPN: lpg1672
            LPF: lpl1637(purN)
            LPP: lpp1644(purN)
            FTU: FTT0895(purN)
            FTF: FTF0895(purN)
            FTW: FTW_1284(purN)
            FTL: FTL_0397
            FTH: FTH_0087(purT) FTH_0389(purN)
            FTA: FTA_0420(purN)
            FTN: FTN_0421(purN)
            TCX: Tcr_1045
            NOC: Noc_1181
            AEH: Mlg_0515
            HHA: Hhal_0711
            HCH: HCH_01905(purN)
            CSA: Csal_2113
            ABO: ABO_1574(purN)
            AHA: AHA_2822(purN)
            DNO: DNO_0207(purN)
            BCI: BCI_0073(purN)
            VOK: COSY_0249(purN)
            NME: NMB1566
            NMA: NMA1755(purN)
            NMC: NMC1486(purN)
            NGO: NGO1224
            CVI: CV_3616(purN)
            RSO: RSc2454(purN)
            REU: Reut_A2741
            REH: H16_A3042(purN)
            RME: Rmet_2878
            BMA: BMA2240(purN)
            BMV: BMASAVP1_A2656(purN)
            BML: BMA10299_A1031(purN)
            BMN: BMA10247_2110(purN)
            BXE: Bxe_A0809
            BUR: Bcep18194_A5842
            BCN: Bcen_1899
            BCH: Bcen2424_2510
            BAM: Bamb_2557
            BPS: BPSL0908(purN)
            BPM: BURPS1710b_1126(purN)
            BPL: BURPS1106A_0973(purN)
            BPD: BURPS668_0969(purN)
            BTE: BTH_I0772(purN)
            BPE: BP1755(purN)
            BPA: BPP1986(purN)
            BBR: BB2174(purN)
            RFR: Rfer_1649
            POL: Bpro_3843
            MPT: Mpe_A2638
            HAR: HEAR2475(purN)
            MMS: mma_2570
            NEU: NE0087(purN)
            NET: Neut_2278
            NMU: Nmul_A2618
            EBA: ebA655(purN)
            AZO: azo3124
            DAR: Daro_3161
            TBD: Tbd_2666
            HHE: HH0470(purN)
            WSU: WS1050(purN)
            TDN: Tmden_1617
            CJE: Cj0187c(purN)
            CJR: CJE0180(purN)
            CJJ: CJJ81176_0218(purN)
            CJU: C8J_0176(purN)
            CJD: JJD26997_0197(purN)
            CFF: CFF8240_1687(purN)
            CCV: CCV52592_1504(purN)
            CHA: CHAB381_0021(purN)
            CCO: CCC13826_1786(purN) CCC13826_2170
            ABU: Abu_2334(purN)
            NIS: NIS_0171(purN)
            SUN: SUN_0159(purN)
            GSU: GSU1759(purN)
            GME: Gmet_1845
            PCA: Pcar_1292
            DVU: DVU0736(purN)
            DDE: Dde_2835
            LIP: LI0118(purN)
            BBA: Bd3005(purN)
            DPS: DP1615
            ADE: Adeh_1254
            MXA: MXAN_2700(purN)
            SAT: SYN_00888
            WOL: WD0763
            WBM: Wbm0420(purN)
            AMA: AM957
            APH: APH_0230(purN)
            ERU: Erum6370(purN)
            ERW: ERWE_CDS_06680(purN)
            ERG: ERGA_CDS_06590(purN)
            ECN: Ecaj_0461 Ecaj_0641
            ECH: ECH_0370(purN) ECH_0575
            NSE: NSE_0474(purN)
            PUB: SAR11_0718(purN)
            MLO: mll7961
            MES: Meso_1967
            SME: SMc00614(purN)
            ATU: Atu1140(purN)
            ATC: AGR_C_2109
            RET: RHE_CH01487(purN)
            RLE: RL1595(purN)
            BME: BMEI1241
            BMF: BAB1_0730(purN)
            BMS: BR0709(purN)
            BMB: BruAb1_0728(purN)
            BOV: BOV_0700(purN)
            BJA: blr4126(purN)
            BRA: BRADO3345(purN)
            BBT: BBta_3853(purN)
            RPA: RPA3052(purN)
            RPB: RPB_2488
            RPC: RPC_2325
            RPD: RPD_2956
            RPE: RPE_3285
            NWI: Nwi_1598
            NHA: Nham_2119
            BHE: BH09570(purN)
            BQU: BQ07390(purN)
            BBK: BARBAKC583_0764(purN)
            CCR: CC_1702
            SIL: SPO2168(purN)
            SIT: TM1040_1475
            RSP: RSP_1970
            JAN: Jann_1837
            RDE: RD1_2253
            MMR: Mmar10_1246
            HNE: HNE_2264(purN)
            ZMO: ZMO0708(purN)
            GOX: GOX1933
            GBE: GbCGDNIH1_2038
            RRU: Rru_A2168
            MAG: amb2847
            MGM: Mmc1_2317
            ABA: Acid345_3012
            BSU: BG10709(purN)
            BHA: BH0632(purN)
            BAN: BA0297(purN)
            BAR: GBAA0297(purN)
            BAA: BA_0869
            BAT: BAS0284
            BCE: BC0332
            BCA: BCE_0326(purN)
            BCZ: BCZK0272(purN)
            BTK: BT9727_0269(purN)
            BTL: BALH_0291(purN)
            BLI: BL01485(purN)
            BLD: BLi00702(purN)
            BCL: ABC1033(purN)
            BAY: RBAM_006930
            BPU: BPUM_0605
            OIH: OB0748
            GKA: GK0266
            SAU: SA0924(purN)
            SAV: SAV1072(purN)
            SAM: MW0955(purN)
            SAR: SAR1046(purN)
            SAS: SAS1008
            SAC: SACOL1081(purN)
            SAB: SAB0939(purN)
            SAA: SAUSA300_0974(purN)
            SAO: SAOUHSC_01016
            SEP: SE0770
            SER: SERP0657(purN)
            SHA: SH1885(purN)
            SSP: SSP1718
            LMO: lmo1766(purN)
            LMF: LMOf2365_1791(purN)
            LIN: lin1878(purN)
            LWE: lwe1784(purN)
            LLA: L164626(purN)
            LLC: LACR_1610
            LLM: llmg_0988(purN)
            SPY: SPy_0028(purN)
            SPZ: M5005_Spy_0026(purN)
            SPM: spyM18_0029(purN)
            SPG: SpyM3_0023(purN)
            SPS: SPs0024
            SPH: MGAS10270_Spy0027(purN)
            SPI: MGAS10750_Spy0026(purN)
            SPJ: MGAS2096_Spy0027(purN)
            SPK: MGAS9429_Spy0026(purN)
            SPF: SpyM50025(purN)
            SPA: M6_Spy0075
            SPB: M28_Spy0026(purN)
            SPN: SP_0048
            SPR: spr0049(purN)
            SPD: SPD_0055(purN)
            SAG: SAG0028(purN)
            SAN: gbs0027
            SAK: SAK_0061(purN)
            SMU: SMU.35(purN)
            STC: str0034(purN)
            STL: stu0034(purN)
            SSA: SSA_0033(purN)
            SGO: SGO_0038(purN)
            LPL: lp_2721(purN)
            LAC: LBA1553(purN)
            LSA: LSA0661(purN)
            LSL: LSL_0669(purN)
            LDB: Ldb1437(purN)
            LBU: LBUL_1332
            LCA: LSEI_1748
            EFA: EF1779(purN)
            OOE: OEOE_1130
            STH: STH2852
            CAC: CAC1394(purN)
            CPE: CPE0685(purN)
            CPF: CPF_0676(purN)
            CPR: CPR_0674(purN)
            CTC: CTC01963
            CNO: NT01CX_2420(purN)
            CDF: CD0222(purN)
            CBO: CBO2874(purN)
            CBA: CLB_2839(purN)
            CBH: CLC_2772(purN)
            CBF: CLI_2932(purN)
            CKL: CKL_2685(purN)
            CHY: CHY_1077(purN)
            DSY: DSY3928
            SWO: Swol_1776
            TTE: TTE0591(purN)
            MTA: Moth_2045
            MTU: Rv0956(purN)
            MTC: MT0983(purN)
            MBO: Mb0981(purN)
            MBB: BCG_1010(purN)
            MLE: ML0160(purN)
            MPA: MAP0902(purN)
            MAV: MAV_1080(purN)
            MSM: MSMEG_5516(purN)
            MMC: Mmcs_4320
            CGL: NCgl0826(cgl0860)
            CGB: cg0983(purN)
            CEF: CE0936(purN)
            CDI: DIP0838(purN)
            CJK: jk1557(purN)
            NFA: nfa49870(purN)
            RHA: RHA1_ro05578(purN)
            SCO: SCO4813(purN)
            SMA: SAV3445(purN)
            TWH: TWT083(purN)
            TWS: TW093(purN)
            LXX: Lxx19640(purN)
            CMI: CMM_2545(purN)
            AAU: AAur_1193(purN)
            PAC: PPA1748
            TFU: Tfu_2573
            FRA: Francci3_0656
            FAL: FRAAL1161(purN)
            ACE: Acel_0383
            SEN: SACE_6665(purN)
            RXY: Rxyl_0999
            FNU: FN0985
            RBA: RB7260(pur3)
            TDE: TDE1897(purN)
            LIL: LA2282(purN) LA4266(purT)
            LIC: LIC11656(purN)
            LBJ: LBJ_1330(purN)
            LBL: LBL_1555(purN)
            SYN: slr0477(purN)
            SYW: SYNW1261(purN)
            SYC: syc0584_d(purN)
            SYF: Synpcc7942_0958
            SYD: Syncc9605_1388
            SYE: Syncc9902_1100
            SYG: sync_1381(purN)
            SYR: SynRCC307_1352(purN)
            SYX: SynWH7803_1254(purN)
            CYA: CYA_0632(purN)
            CYB: CYB_0901(purN)
            TEL: tlr2326(purN)
            GVI: glr1401(purN)
            ANA: all0788
            AVA: Ava_0564
            PMA: Pro0945(purN)
            PMM: PMM0891(purN)
            PMT: PMT0710(purN)
            PMN: PMN2A_0319 PMN2A_0821
            PMB: A9601_09701(purN)
            PMC: P9515_09731(purN)
            PMF: P9303_15111(purN)
            PMG: P9301_09681(purN)
            PMH: P9215_10011
            PME: NATL1_09921(purN)
            TER: Tery_4633
            BTH: BT_2883 BT_3360
            BFR: BF0221
            BFS: BF0180(purN)
            PGI: PG1766(purN)
            SRU: SRU_1638(purN)
            CHU: CHU_3310(purN)
            GFO: GFO_3381(purN)
            FPS: FP0199(purN) FP0411(purT)
            CTE: CT0319(purN)
            CCH: Cag_0504
            DRA: DR_2026
            DGE: Dgeo_1546
            AAE: aq_857(purN)
            TMA: TM1248
            MMP: MMP0123(purT)
            MAC: MA0316 MA3522(purN)
            MBA: Mbar_A1295 Mbar_A2317
            MMA: MM_0443
            MBU: Mbur_1812
            MHU: Mhun_3012
            HMA: rrnAC0189(purH) rrnAC3272(purU)
            HWA: HQ1661A(purNH)
            NPH: NP1662A(purNH)
            TAC: Ta0082
            TVO: TVN0171
            PTO: PTO0379
            PAI: PAE0219
STRUCTURES  PDB: 1C2T  1C3E  1CDD  1CDE  1GAR  1GRC  1JKX  1MEJ  1MEN  1MEO  
                 1NJS  1RBM  1RBQ  1RBY  1RBZ  1RC0  1RC1  1ZLX  1ZLY  2GAR  
                 2QK4  3GAR  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.2.2
            ExPASy - ENZYME nomenclature database: 2.1.2.2
            ExplorEnz - The Enzyme Database: 2.1.2.2
            ERGO genome analysis and discovery system: 2.1.2.2
            BRENDA, the Enzyme Database: 2.1.2.2
            CAS: 9032-02-4
///
ENTRY       EC 2.1.2.3                  Enzyme
NAME        phosphoribosylaminoimidazolecarboxamide formyltransferase;
            5-amino-4-imidazolecarboxamide ribonucleotide transformylase;
            AICAR transformylase;
            10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-
            imidazolecarboxamide formyltransferase;
            5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase;
            5-amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate
            transformylase;
            5-amino-4-imidazolecarboxamide ribotide transformylase;
            AICAR formyltransferase;
            aminoimidazolecarboxamide ribonucleotide transformylase
CLASS       Transferases;
            Transferring one-carbon groups;
            Hydroxymethyl-, formyl- and related transferases
SYSNAME     10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazole-carb
            oxamide N-formyltransferase
REACTION    10-formyltetrahydrofolate +
            5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide =
            tetrahydrofolate +
            5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
            [RN:R04560]
ALL_REAC    R04560
SUBSTRATE   10-formyltetrahydrofolate [CPD:C00234];
            5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide [CPD:C04677]
PRODUCT     tetrahydrofolate [CPD:C00101];
            5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
            [CPD:C04734]
REFERENCE   1  [PMID:13672969]
  AUTHORS   HARTMAN SC, BUCHANAN JM.
  TITLE     Biosynthesis of the purines. XXVI. The identification of the formyl
            donors of the transformylation reactions.
  JOURNAL   J. Biol. Chem. 234 (1959) 1812-6.
  ORGANISM  avian
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00670  One carbon pool by folate
ORTHOLOGY   KO: K00602  phosphoribosylaminoimidazolecarboxamide
                        formyltransferase
GENES       HSA: 471(ATIC)
            MMU: 108147(Atic)
            RNO: 81643(Atic)
            CFA: 488513(ATIC)
            BTA: 506343(ATIC)
            GGA: 396091(ATIC)
            XTR: 448061(atic)
            SPU: 588680(LOC588680)
            DME: Dmel_CG11089
            CME: CML194C
            SCE: YLR028C(ADE16) YMR120C(ADE17)
            AGO: AGOS_AFR213C
            SPO: SPCPB16A4.03c
            ANI: AN4464.2
            AFM: AFUA_4G07690
            AOR: AO090023000806
            CNE: CNA06790
            UMA: UM01023.1
            DDI: DDB_0230095(purH)
            ECO: b4006(purH)
            ECJ: JW3970(purH)
            ECE: Z5583(purH)
            ECS: ECs4929
            ECC: c4964(purH)
            ECI: UTI89_C3814(purH)
            ECP: ECP_4219
            ECV: APECO1_2469(purH)
            ECW: EcE24377A_4550(purH)
            ECX: EcHS_A4240
            STY: STY3709(purH)
            STT: t3455(purH)
            SPT: SPA4013(purH)
            STM: STM4176(purH)
            YPE: YPO3728(purH)
            YPK: y0502(purH)
            YPM: YP_3091(purH)
            YPA: YPA_3601
            YPN: YPN_0237
            YPP: YPDSF_3726
            YPS: YPTB0300(purH)
            YPI: YpsIP31758_3843(purH)
            SFL: SF4078(purH)
            SFX: S3657(purH)
            SFV: SFV_4078(purH)
            SSN: SSON_4179(purH)
            SBO: SBO_4027(purH)
            SDY: SDY_3720(purH)
            ECA: ECA0241(purH)
            PLU: plu0495(purH)
            BUC: BU031(purH)
            BAS: BUsg032(purH)
            BAB: bbp032(purH)
            WBR: WGLp511(purH)
            SGL: SG0143
            BFL: Bfl555(purH)
            BPN: BPEN_575(purH)
            HIT: NTHI1051(purH)
            HDU: HD1703(purH)
            HSO: HS_1625(purH)
            PMU: PM0222(purH)
            MSU: MS1297(purH)
            APL: APL_0958(purH)
            XFA: XF1975
            XFT: PD0828(purH)
            XCC: XCC0498(purH)
            XCB: XC_0510
            XCV: XCV0547(purH)
            XAC: XAC0513(purH)
            XOO: XOO0539(purH)
            XOM: XOO_0506(XOO0506)
            VCH: VC0276(purH)
            VCO: VC0395_A2653(purH)
            VVU: VV1_1227(purH)
            VVY: VV3142
            VPA: VP2896
            VFI: VF2394(purH)
            PPR: PBPRA3419
            PAE: PA4854(purH)
            PAU: PA14_64200(purH)
            PAP: PSPA7_5574(purH)
            PPU: PP_4822(purH)
            PPF: Pput_4697
            PST: PSPTO_4866(purH)
            PSB: Psyr_4406
            PSP: PSPPH_4449(purH)
            PFL: PFL_0666(purH)
            PFO: Pfl_0613
            PEN: PSEEN4863(purH)
            PAR: Psyc_1472(purH)
            PCR: Pcryo_1651
            ACI: ACIAD2447(purH)
            SON: SO_0442(purH)
            SDN: Sden_3407
            SFR: Sfri_0493
            SAZ: Sama_0395
            SBL: Sbal_0420
            SBM: Shew185_3913
            SLO: Shew_3412
            SPC: Sputcn32_3401
            SPL: Spea_0432
            SHE: Shewmr4_0445
            SHM: Shewmr7_3584
            SHN: Shewana3_0441
            SHW: Sputw3181_0542
            ILO: IL2290(purH)
            CPS: CPS_0552(purH)
            PHA: PSHAa0345(purH)
            PAT: Patl_0268
            SDE: Sde_0806
            PIN: Ping_3220
            MAQ: Maqu_3450
            CBU: CBU_0336(purH)
            CBD: COXBU7E912_1743(purH)
            LPN: lpg0460(purH)
            LPF: lpl0502(purH)
            LPP: lpp0526(purH)
            MCA: MCA1747(purH)
            FTU: FTT0203c(purH)
            FTF: FTF0203c(purH)
            FTW: FTW_1885(purH)
            FTL: FTL_1929
            FTH: FTH_1849(purH)
            FTA: FTA_2038(purH)
            FTN: FTN_0177(purH)
            TCX: Tcr_0439
            NOC: Noc_1048
            AEH: Mlg_0611
            HHA: Hhal_2000
            HCH: HCH_06011(purH)
            CSA: Csal_2289
            ABO: ABO_2015(purH)
            MMW: Mmwyl1_2987
            AHA: AHA_0841(purH)
            BCI: BCI_0035(purH)
            RMA: Rmag_0969
            VOK: COSY_0869(purH)
            NME: NMB0983
            NMA: NMA1182(purH)
            NMC: NMC0963(purH)
            NGO: NGO1466
            CVI: CV_0546(purH)
            RSO: RSc0504(purH)
            REU: Reut_A0487
            RME: Rmet_0427
            BMA: BMA2356(purH)
            BMV: BMASAVP1_A0269(purH)
            BML: BMA10299_A1131(purH)
            BMN: BMA10247_2535(purH)
            BXE: Bxe_A0619
            BVI: Bcep1808_0656
            BUR: Bcep18194_A3777(purH)
            BCN: Bcen_0208
            BCH: Bcen2424_0691
            BAM: Bamb_0584
            BPS: BPSL2896(purH)
            BPM: BURPS1710b_3403(purH)
            BPL: BURPS1106A_3398(purH)
            BPD: BURPS668_3363(purH)
            BTE: BTH_I1250(purH)
            BPE: BP3416(purH)
            BPA: BPP3566(purH)
            BBR: BB4001(purH)
            RFR: Rfer_1582
            POL: Bpro_1132
            PNA: Pnap_3358
            AAV: Aave_0896
            VEI: Veis_3025
            MPT: Mpe_A0485
            HAR: HEAR0255(purH)
            MMS: mma_0308
            NEU: NE0876(purH)
            NET: Neut_1210
            NMU: Nmul_A0133
            EBA: ebA1153(purH)
            DAR: Daro_3667
            TBD: Tbd_2458
            MFA: Mfla_0349
            HHE: HH0483(purH)
            WSU: WS1885(purH)
            TDN: Tmden_0550
            CJE: Cj0953c(purH)
            CJR: CJE1033(purH)
            CJJ: CJJ81176_0976(purH)
            CJU: C8J_0895(purH)
            CJD: JJD26997_0828(purH)
            CFF: CFF8240_0558(purH)
            CCV: CCV52592_1838(purH)
            CHA: CHAB381_0670(purH)
            CCO: CCC13826_1632(purH)
            ABU: Abu_1638(purH)
            NIS: NIS_0948(purH)
            SUN: SUN_1564(purH)
            GSU: GSU0609(purH)
            GME: Gmet_2905
            GUR: Gura_3847
            PCA: Pcar_2232
            PPD: Ppro_2592
            DVU: DVU3206
            DVL: Dvul_0153 Dvul_0180
            DDE: Dde_0174 Dde_0377
            LIP: LI0200(purH)
            BBA: Bd3002(purH)
            DPS: DP1741(purH)
            ADE: Adeh_2468
            MXA: MXAN_2914(purH)
            SAT: SYN_02440
            SFU: Sfum_2760 Sfum_3083
            WOL: WD0867(purH)
            WBM: Wbm0411(purH)
            AMA: AM1099(purH)
            APH: APH_1207(purH)
            ERU: Erum8290(purH)
            ERW: ERWE_CDS_08780(purH)
            ERG: ERGA_CDS_08690(purH)
            ECN: Ecaj_0866
            ECH: ECH_1074(purH)
            NSE: NSE_0185(purH)
            PUB: SAR11_0319(purH)
            MLO: mlr4101
            MES: Meso_3420
            SME: SMc04088(purH)
            ATU: Atu2823(purH)
            ATC: AGR_C_5117
            RET: RHE_CH04107(purH)
            RLE: RL4722(purH)
            BME: BMEI0233
            BMF: BAB1_1824(purH)
            BMS: BR1816(purH)
            BMB: BruAb1_1796(purH)
            BOV: BOV_1749(purH)
            OAN: Oant_1087
            BJA: blr0581(purH)
            BRA: BRADO0338(purH)
            BBT: BBta_0323(purH)
            RPA: RPA0028(purH)
            RPB: RPB_0084
            RPC: RPC_0023
            RPD: RPD_0719
            RPE: RPE_0026
            NWI: Nwi_0158(purH)
            NHA: Nham_0195
            BHE: BH15970(purH)
            BQU: BQ12870(purH)
            BBK: BARBAKC583_0074(purH)
            CCR: CC_0086
            SIL: SPO3374(purH)
            SIT: TM1040_0091
            RSP: RSP_1100(purH)
            RSH: Rsph17029_2763
            JAN: Jann_4042
            RDE: RD1_0655(purH)
            MMR: Mmar10_2928
            HNE: HNE_3372(purH)
            ZMO: ZMO0027(purH)
            NAR: Saro_0106
            SAL: Sala_3123
            SWI: Swit_0447
            ELI: ELI_12540
            GOX: GOX0428
            GBE: GbCGDNIH1_1647
            RRU: Rru_A3655
            MAG: amb0100
            MGM: Mmc1_3468
            ABA: Acid345_4470
            SUS: Acid_6430
            BSU: BG10710(purH)
            BHA: BH0633(purH)
            BAN: BA0298(purH)
            BAR: GBAA0298(purH)
            BAA: BA_0870
            BAT: BAS0285
            BCE: BC0333
            BCA: BCE_0327(purH)
            BCZ: BCZK0273(purH)
            BTK: BT9727_0270(purH)
            BTL: BALH_0292(purH)
            BLI: BL01486(purH)
            BLD: BLi00703(purH)
            BCL: ABC1034(purH)
            BAY: RBAM_006940
            BPU: BPUM_0606
            OIH: OB0749(purH)
            GKA: GK0267(purH)
            SAU: SA0925(purH)
            SAV: SAV1073(purH)
            SAM: MW0956(purH)
            SAR: SAR1047(purH)
            SAS: SAS1009
            SAC: SACOL1082(purH)
            SAB: SAB0940(purH)
            SAA: SAUSA300_0975(purH)
            SAO: SAOUHSC_01017
            SEP: SE0771
            SER: SERP0658(purH)
            SHA: SH1884(purH)
            SSP: SSP1717
            LMO: lmo1765(purH)
            LMF: LMOf2365_1790(purH)
            LIN: lin1877(purH)
            LWE: lwe1783(purH)
            LLA: L158710(purH)
            LLC: LACR_1605
            SPZ: M5005_Spy_0027(purH)
            SPM: spyM18_0030(purH)
            SPG: SpyM3_0024(purH)
            SPS: SPs0025
            SPH: MGAS10270_Spy0028
            SPI: MGAS10750_Spy0027
            SPJ: MGAS2096_Spy0028
            SPK: MGAS9429_Spy0027
            SPA: M6_Spy0076(purH)
            SPN: SP_0050
            SPR: spr0051(purH)
            SPD: SPD_0057(purH)
            SAG: SAG0030(purH)
            SAN: gbs0029
            SAK: SAK_0063(purH)
            SMU: SMU.37(purH)
            STC: str0035(purH)
            STL: stu0035(purH)
            SSA: SSA_0035(purH)
            LPL: lp_2720(purH)
            LAC: LBA1552(purH)
            LSA: LSA0662(purH)
            LSL: LSL_0670(purH)
            LDB: Ldb1436(purH)
            LBU: LBUL_1331
            LCA: LSEI_1747
            LRE: Lreu_0144
            EFA: EF1778(purH)
            OOE: OEOE_1129
            STH: STH2850
            CAC: CAC1395(purH)
            CPE: CPE0686(purH)
            CPF: CPF_0677(purH)
            CPR: CPR_0675(purH)
            CTC: CTC01962(purH)
            CTH: Cthe_1246
            CDF: CD0223(purH)
            CBO: CBO2873(purH)
            CBA: CLB_2838(purH)
            CBH: CLC_2771(purH)
            CBF: CLI_2931(purH)
            CBE: Cbei_3561
            CKL: CKL_2684(purH)
            CHY: CHY_1078(purH)
            DSY: DSY3927
            DRM: Dred_2362
            SWO: Swol_1775
            TTE: TTE0592(purH)
            MTA: Moth_2044
            MTU: Rv0957(purH)
            MTC: MT0984(purH)
            MBO: Mb0982(purH)
            MBB: BCG_1011(purH)
            MLE: ML0161(purH)
            MPA: MAP0903(purH)
            MAV: MAV_1081(purH)
            MSM: MSMEG_5515(purH)
            MVA: Mvan_4856
            MGI: Mflv_1875
            MMC: Mmcs_4319
            MKM: Mkms_4405
            MJL: Mjls_4699
            CGL: NCgl0827(purH)
            CGB: cg0984(purH)
            CEF: CE0937(purH)
            CDI: DIP0839(purH)
            CJK: jk1556(purH)
            NFA: nfa49860(purHJ)
            RHA: RHA1_ro05579(purH)
            SCO: SCO4814(purH)
            SMA: SAV3444(purH)
            TWH: TWT084(purH)
            TWS: TW094(purH)
            LXX: Lxx19650(purH)
            CMI: CMM_2544(purH)
            ART: Arth_1090
            PAC: PPA1747
            NCA: Noca_3583
            TFU: Tfu_2572
            FRA: Francci3_0657
            FAL: FRAAL1162(purH)
            ACE: Acel_0384
            KRA: Krad_3995
            SEN: SACE_6664(purH)
            STP: Strop_3806
            BLO: BL0735(purH)
            BAD: BAD_0811(purH)
            RXY: Rxyl_1000
            FNU: FN0982(purH)
            RBA: RB10113(purH)
            TDE: TDE1896(purH)
            LIL: LA2283(purH)
            LIC: LIC11655(purH)
            LBJ: LBJ_1329(purH)
            LBL: LBL_1554(purH)
            SYN: slr0597(purH)
            SYW: SYNW0249(purH)
            SYC: syc1119_c(purH)
            SYF: Synpcc7942_0396
            SYD: Syncc9605_0243
            SYE: Syncc9902_0272
            SYG: sync_0289(purH)
            SYR: SynRCC307_2316(purH)
            SYX: SynWH7803_0293(purH)
            CYA: CYA_2813(purH)
            CYB: CYB_2851(purH)
            TEL: tlr1547(purH)
            GVI: glr0559(purH)
            ANA: all3093(purH)
            AVA: Ava_3818(purH)
            PMA: Pro0298(purH)
            PMM: PMM0266(purH)
            PMT: PMT1857(purH)
            PMN: PMN2A_1632
            PMI: PMT9312_0268
            PMB: A9601_02881(purH)
            PMC: P9515_02991(purH)
            PMF: P9303_24851(purH)
            PMG: P9301_02891(purH)
            PMH: P9215_02901
            PME: NATL1_03441(purH)
            TER: Tery_1128
            BTH: BT_3812(purH)
            BFR: BF4101
            BFS: BF3917(purH)
            PGI: PG1397(purH)
            SRU: SRU_1639(purH)
            CHU: CHU_3309(purH)
            GFO: GFO_2957(purH)
            FPS: FP2416(purH)
            CTE: CT0320(purH)
            CCH: Cag_0258(purH)
            CPH: Cpha266_0657
            PLT: Plut_0432
            DET: DET1417(purH)
            DEH: cbdb_A1381(purH)
            DEB: DehaBAV1_1225
            RRS: RoseRS_0206
            RCA: Rcas_4336
            DRA: DR_0868
            DGE: Dgeo_0513
            TTH: TTC0561
            TTJ: TTHA0930
            AAE: aq_1963(purH)
            TMA: TM1249
            TME: Tmel_0387
            MAC: MA4012(purH)
            MBA: Mbar_A0571
            MMA: MM_0898
            MBU: Mbur_1928
            MTP: Mthe_1511
            MHU: Mhun_3032
            MEM: Memar_1063
            MBN: Mboo_1205
            HAL: VNG0414G(purH)
            HMA: rrnAC0189(purH)
            HWA: HQ1661A(purNH)
            NPH: NP1662A(purNH)
            TAC: Ta0060
            TVO: TVN0016
            PTO: PTO0745
STRUCTURES  PDB: 1G8M  1M9N  1OZ0  1P4R  1PKX  1PL0  1THZ  2B1G  2B1I  2IU0  
                 2IU3  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.2.3
            ExPASy - ENZYME nomenclature database: 2.1.2.3
            ExplorEnz - The Enzyme Database: 2.1.2.3
            ERGO genome analysis and discovery system: 2.1.2.3
            BRENDA, the Enzyme Database: 2.1.2.3
            CAS: 9032-03-5
///
ENTRY       EC 2.1.2.4                  Enzyme
NAME        glycine formimidoyltransferase;
            formiminoglycine formiminotransferase;
            FIG formiminotransferase;
            glycine formiminotransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Hydroxymethyl-, formyl- and related transferases
SYSNAME     5-formimidoyltetrahydrofolate:glycine N-formimidoyltransferase
REACTION    5-formimidoyltetrahydrofolate + glycine = tetrahydrofolate +
            N-formimidoylglycine [RN:R02729]
ALL_REAC    R02729
SUBSTRATE   5-formimidoyltetrahydrofolate [CPD:C00664];
            glycine [CPD:C00037]
PRODUCT     tetrahydrofolate [CPD:C00101];
            N-formimidoylglycine [CPD:C02718]
REFERENCE   1
  AUTHORS   Rabinowitz, J.C. and Pricer, W.E.
  TITLE     Formiminotetrahydrofolic acid and methenyltetrahydrofolic acid as
            intermediates in the formation of N10-formyltetrahydrofolic acid.
  JOURNAL   J. Am. Chem. Soc. 78 (1956) 5702-5704.
  ORGANISM  Clostridium cylindrosporum
REFERENCE   2
  AUTHORS   Rabinowitz, J.C. and Pricer, W.E.
  TITLE     Formation, isolation and properties of 5-formiminotetrahydrofolic
            acid.
  JOURNAL   Fed. Proc. 16 (1957) 236.
  ORGANISM  Clostridium cylindrosporum
REFERENCE   3
  AUTHORS   Sagers, R.D., Beck, J.V., Gruber, W. and Gunsalus, I.C.
  TITLE     A tetrahydrofolic acid linked formimino transfer enzyme.
  JOURNAL   J. Am. Chem. Soc. 78 (1956) 694-695.
  ORGANISM  Clostridium cylindrosporum, Clostridium acidi-urici
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00670  One carbon pool by folate
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.2.4
            ExPASy - ENZYME nomenclature database: 2.1.2.4
            ExplorEnz - The Enzyme Database: 2.1.2.4
            ERGO genome analysis and discovery system: 2.1.2.4
            BRENDA, the Enzyme Database: 2.1.2.4
            CAS: 9029-84-9
///
ENTRY       EC 2.1.2.5                  Enzyme
NAME        glutamate formimidoyltransferase;
            glutamate formyltransferase;
            formiminoglutamic acid transferase;
            formiminoglutamic formiminotransferase;
            glutamate formiminotransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Hydroxymethyl-, formyl- and related transferases
SYSNAME     5-formimidoyltetrahydrofolate:L-glutamate N-formimidoyltransferase
REACTION    5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate +
            N-formimidoyl-L-glutamate [RN:R02287]
ALL_REAC    R02287;
            (other) R03189
SUBSTRATE   5-formimidoyltetrahydrofolate [CPD:C00664];
            L-glutamate [CPD:C00025]
PRODUCT     tetrahydrofolate [CPD:C00101];
            N-formimidoyl-L-glutamate [CPD:C00439]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also catalyses formyl transfer from
            5-formyltetrahydrofolate to L-glutamate (a reaction formerly listed
            as EC 2.1.2.6). In eukaryotes, it occurs as a bifunctional enzyme
            that also has formimidoyltetrahydrofolate cyclodeaminase (EC
            4.3.1.4) activity.
REFERENCE   1  [PMID:13475327]
  AUTHORS   MILLER A, WAELSCH H.
  TITLE     Formimino transfer from formamidinoglutaric acid to tetrahydrofolic
            acid.
  JOURNAL   J. Biol. Chem. 228 (1957) 397-417.
  ORGANISM  rat [GN:rno], cow [GN:bta]
REFERENCE   2  [PMID:13428739]
  AUTHORS   SILVERMAN M, KERESZTESY JC, KOVAL GJ, GARDINER RC.
  TITLE     Citrovorum factor and the synthesis of formylglutamic acid.
  JOURNAL   J. Biol. Chem. 226 (1957) 83-94.
  ORGANISM  horse
REFERENCE   3
  AUTHORS   Tabor, H. and Wyngarden, L.
  TITLE     The enzymatic formation of formiminotetrahydrofolic acid,
            5,10-methenyltetrahydrofolic acid, and 10-formyltetrahydrofolic acid
            in the metabolism of formiminoglutamic acid.
  JOURNAL   J. Biol. Chem. 234 (1959) 1830-1849.
  ORGANISM  pig [GN:ssc], rabbit
PATHWAY     PATH: map00340  Histidine metabolism
            PATH: map00670  One carbon pool by folate
ORTHOLOGY   KO: K00603  glutamate formiminotransferase
GENES       HSA: 10841(FTCD)
            MMU: 14317(Ftcd)
            RNO: 89833(Ftcd)
            SSC: 397517(FTCD)
            XLA: 379483(MGC64458)
            XTR: 448617(TGas028n11.1)
            SPU: 584654(LOC584654)
            DDI: DDBDRAFT_0187716
            DPS: DP2350
            SAT: SYN_00461
            SUS: Acid_5208
            SPZ: M5005_Spy_1772
            SPH: MGAS10270_Spy1838
            SPI: MGAS10750_Spy1864
            SPJ: MGAS2096_Spy1805
            SPK: MGAS9429_Spy1783
            SPF: SpyM51730
            SPA: M6_Spy1769
            SPB: M28_Spy1756
            SSA: SSA_0434
            SGO: SGO_1806(ftcD) SGO_1807
            CTC: CTC02305
            AMT: Amet_4073
            CHY: CHY_0695(ftcD)
            TTE: TTE0450
            FNU: FN0741 FN1407
            TDE: TDE0296
            BFR: BF4147
            BFS: BF3969(ftcD)
            PGI: PG0329
            TPT: Tpet_0084
            FNO: Fnod_0808
            PTO: PTO1242
STRUCTURES  PDB: 1QD1  1TT9  2PFD  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.2.5
            ExPASy - ENZYME nomenclature database: 2.1.2.5
            ExplorEnz - The Enzyme Database: 2.1.2.5
            ERGO genome analysis and discovery system: 2.1.2.5
            BRENDA, the Enzyme Database: 2.1.2.5
            CAS: 9032-83-1
///
ENTRY       EC 2.1.2.6        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring one-carbon groups;
            Hydroxymethyl-, formyl- and related transferases
COMMENT     Deleted entry: glutamate formyltransferase. Now included with EC
            2.1.2.5, glutamate formimidoyltransferase (EC 2.1.2.6 created 1965,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.2.6
            ExPASy - ENZYME nomenclature database: 2.1.2.6
            ExplorEnz - The Enzyme Database: 2.1.2.6
            ERGO genome analysis and discovery system: 2.1.2.6
            BRENDA, the Enzyme Database: 2.1.2.6
///
ENTRY       EC 2.1.2.7                  Enzyme
NAME        D-alanine 2-hydroxymethyltransferase;
            2-methylserine hydroxymethyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Hydroxymethyl-, formyl- and related transferases
SYSNAME     5,10-methylenetetrahydrofolate:D-alanine 2-hydroxymethyltransferase
REACTION    5,10-methylenetetrahydrofolate + D-alanine + H2O = tetrahydrofolate
            + 2-methylserine [RN:R01225]
ALL_REAC    R01225
SUBSTRATE   5,10-methylenetetrahydrofolate [CPD:C00143];
            D-alanine [CPD:C00133];
            H2O [CPD:C00001]
PRODUCT     tetrahydrofolate [CPD:C00101];
            2-methylserine [CPD:C02115]
COMMENT     Also acts on 2-hydroxymethylserine.
REFERENCE   1
  AUTHORS   Wilson, E.M. and Snell, E.E.
  TITLE     Metabolism of alpha-methylserine. I. alpha-Methylserine
            hydroxymethyltransferase.
  JOURNAL   J. Biol. Chem. 237 (1962) 3171-3179.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00670  One carbon pool by folate
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.2.7
            ExPASy - ENZYME nomenclature database: 2.1.2.7
            ExplorEnz - The Enzyme Database: 2.1.2.7
            ERGO genome analysis and discovery system: 2.1.2.7
            BRENDA, the Enzyme Database: 2.1.2.7
            CAS: 9075-76-7
///
ENTRY       EC 2.1.2.8                  Enzyme
NAME        deoxycytidylate 5-hydroxymethyltransferase;
            dCMP hydroxymethylase;
            d-cytidine 5'-monophosphate hydroxymethylase;
            deoxyCMP hydroxymethylase;
            deoxycytidylate hydroxymethylase;
            deoxycytidylic hydroxymethylase
CLASS       Transferases;
            Transferring one-carbon groups;
            Hydroxymethyl-, formyl- and related transferases
SYSNAME     5,10-methylenetetrahydrofolate:deoxycytidylate
            5-hydroxymethyltransferase
REACTION    5,10-methylenetetrahydrofolate + H2O + deoxycytidylate =
            tetrahydrofolate + 5-hydroxymethyldeoxycytidylate [RN:R01669]
ALL_REAC    R01669
SUBSTRATE   5,10-methylenetetrahydrofolate [CPD:C00143];
            H2O [CPD:C00001];
            deoxycytidylate [CPD:C00239]
PRODUCT     tetrahydrofolate [CPD:C00101];
            5-hydroxymethyldeoxycytidylate [CPD:C03997]
REFERENCE   1
  AUTHORS   Mathews, C.K., Brown, F. and Cohen, S.S.
  TITLE     Virus-induced acquisition of metabolic function. VII. Biosynthesis
            de novo of deoxycytidylate hydroxymethylase.
  JOURNAL   J. Biol. Chem. 239 (1964) 2957-2963.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00240  Pyrimidine metabolism
            PATH: map00670  One carbon pool by folate
STRUCTURES  PDB: 1B49  1B5D  1B5E  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.2.8
            ExPASy - ENZYME nomenclature database: 2.1.2.8
            ExplorEnz - The Enzyme Database: 2.1.2.8
            ERGO genome analysis and discovery system: 2.1.2.8
            BRENDA, the Enzyme Database: 2.1.2.8
            CAS: 9012-68-4
///
ENTRY       EC 2.1.2.9                  Enzyme
NAME        methionyl-tRNA formyltransferase;
            N10-formyltetrahydrofolic-methionyl-transfer ribonucleic
            transformylase;
            formylmethionyl-transfer ribonucleic synthetase;
            methionyl ribonucleic formyltransferase;
            methionyl-tRNA Met formyltransferase;
            methionyl-tRNA transformylase;
            methionyl-transfer RNA transformylase;
            methionyl-transfer ribonucleate methyltransferase;
            methionyl-transfer ribonucleic transformylase
CLASS       Transferases;
            Transferring one-carbon groups;
            Hydroxymethyl-, formyl- and related transferases
SYSNAME     10-formyltetrahydrofolate:L-methionyl-tRNA N-formyltransferase
REACTION    10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O =
            tetrahydrofolate + N-formylmethionyl-tRNAfMet [RN:R03940]
ALL_REAC    R03940
SUBSTRATE   10-formyltetrahydrofolate [CPD:C00234];
            L-methionyl-tRNAfMet;
            H2O [CPD:C00001]
PRODUCT     tetrahydrofolate [CPD:C00101];
            N-formylmethionyl-tRNAfMet
REFERENCE   1  [PMID:5337045]
  AUTHORS   Dickerman HW, Steers E Jr, Redfield BG, Weissbach H.
  TITLE     Methionyl soluble ribonucleic acid transformylase. I. Purification
            and partial characterization.
  JOURNAL   J. Biol. Chem. 242 (1967) 1522-5.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00271  Methionine metabolism
            PATH: map00670  One carbon pool by folate
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K00604  methionyl-tRNA formyltransferase
GENES       HSA: 123263(MTFMT)
            PTR: 453511(MTFMT)
            MMU: 69606(Mtfmt)
            CFA: 610763(MTFMT)
            BTA: 286855(MtFMT)
            GGA: 415532(MTFMT)
            ATH: AT1G66520(PDE194)
            OSA: 4324118
            CME: CMG198C
            SCE: YBL013W(FMT1)
            AGO: AGOS_AFR488W
            PIC: PICST_52982(FMT1)
            CGR: CAGL0E02871g
            SPO: SPAC1805.09c
            ANI: AN5738.2
            AOR: AO090003000074 AO090003000793
            UMA: UM04844.1
            DDI: DDBDRAFT_0217948
            PFA: MAL13P1.67
            TET: TTHERM_01035710
            TBR: Tb11.01.7110
            ECO: b3288(fmt)
            ECJ: JW3249(fmt)
            ECE: Z4658(fmt)
            ECS: ECs4153
            ECC: c4048(fmt)
            ECI: UTI89_C3732(fmt)
            ECP: ECP_3375
            ECV: APECO1_3159(fmt)
            ECW: EcE24377A_3770(fmt)
            ECX: EcHS_A3481(fmt)
            STY: STY4390(fmt)
            STT: t4097(fmt)
            SPT: SPA3274(fmt)
            SEC: SC3343(fmt)
            STM: STM3407(fmt)
            YPE: YPO0241(fmt)
            YPK: y4022(fmt)
            YPM: YP_0239(fmt)
            YPA: YPA_3232
            YPN: YPN_3828
            YPP: YPDSF_0163
            YPS: YPTB3666(fmt)
            YPI: YpsIP31758_3883(fmt)
            SFL: SF3319(fmt)
            SFX: S3544(fmt)
            SFV: SFV_3307(fmt)
            SSN: SSON_3428(fmt)
            SBO: SBO_3281(fmt)
            SDY: SDY_3464(fmt)
            ECA: ECA4000(fmt)
            PLU: plu4696(fmt)
            BUC: BU497(fmt)
            BAS: BUsg478(fmt)
            BAB: bbp440(fmt)
            BCC: BCc_314(fmt)
            WBR: WGLp495(fmt)
            SGL: SG2247
            ENT: Ent638_3719
            KPN: KPN_03688(fmt)
            BFL: Bfl218(fmt)
            BPN: BPEN_225(fmt)
            HIN: HI0623(fmt)
            HIT: NTHI0724(fmt)
            HIP: CGSHiEE_09115(fmt)
            HDU: HD2029(fmt)
            HSO: HS_0040(fmt)
            PMU: PM1560(fmt)
            MSU: MS2202(fmt)
            APL: APL_1587(fmt)
            XFA: XF0927
            XFT: PD1762(fmt)
            XCC: XCC3748(fmt)
            XCB: XC_3818
            XCV: XCV3925(fmt)
            XAC: XAC3800(fmt)
            XOO: XOO0586(fmt)
            XOM: XOO_0547(XOO0547)
            VCH: VC0045
            VCO: VC0395_A2474(fmt)
            VVU: VV1_1047
            VVY: VV3226
            VPA: VP3043
            VFI: VF2544
            PPR: PBPRA3580
            PAE: PA0018(fmt)
            PAU: PA14_00190(fmt)
            PAP: PSPA7_0019(fmt)
            PPU: PP_0067(fmt)
            PST: PSPTO_0178(fmt)
            PSB: Psyr_0018
            PSP: PSPPH_0020(fmt)
            PFL: PFL_0021(fmt)
            PFO: Pfl_0016
            PEN: PSEEN0024(fmt)
            PMY: Pmen_0054
            PAR: Psyc_0659 Psyc_2139(fmt)
            PCR: Pcryo_2467
            ACI: ACIAD3637(fmt)
            SON: SO_0031(fmt)
            SDN: Sden_0023
            SFR: Sfri_0023
            SAZ: Sama_0042 Sama_2246
            SBL: Sbal_0031
            SLO: Shew_3737
            SPC: Sputcn32_0023
            SHE: Shewmr4_0028
            SHM: Shewmr7_0026
            SHN: Shewana3_0034
            SHW: Sputw3181_0023
            ILO: IL0017(fmt)
            CPS: CPS_0019(fmt)
            PHA: PSHAa0022(fmt)
            PAT: Patl_0022
            SDE: Sde_0020
            PIN: Ping_0079
            MAQ: Maqu_0042
            CBU: CBU_1997(fmt)
            CBD: COXBU7E912_2096(fmt)
            LPN: lpg2594(fmt)
            LPF: lpl2517(fmt)
            LPP: lpp2647(fmt)
            MCA: MCA2844(fmt)
            FTU: FTT0925(fmt)
            FTF: FTF0925(fmt)
            FTW: FTW_0818(fmt)
            FTL: FTL_1285
            FTH: FTH_1257(fmt)
            FTA: FTA_1358(fmt)
            FTN: FTN_0803(fmt)
            TCX: Tcr_0192
            NOC: Noc_3015
            AEH: Mlg_2627
            HCH: HCH_00029(fmt)
            CSA: Csal_2868
            ABO: ABO_0130(fmt)
            AHA: AHA_0257(fmt)
            DNO: DNO_0157(fmt)
            BCI: BCI_0415(fmt)
            VOK: COSY_0715(fmt)
            NME: NMB0111
            NMA: NMA0163(fmt)
            NMC: NMC0103(fmt)
            NGO: NGO1870
            CVI: CV_0748 CV_2818(fmt2) CV_4264(fmt)
            RSO: RSc0072(fmt) RSc1320(RS02841)
            REU: Reut_A3407 Reut_B3975
            REH: H16_A3699(fmt)
            RME: Rmet_3564 Rmet_4591
            BMA: BMA0143(fmt) BMA1392
            BMV: BMASAVP1_A2805(fmt)
            BML: BMA10299_A2275(fmt)
            BMN: BMA10247_2353(fmt)
            BXE: Bxe_A4415
            BUR: Bcep18194_A5162 Bcep18194_A6477
            BCN: Bcen_2512
            BCH: Bcen2424_3126
            BAM: Bamb_1799 Bamb_3181 Bamb_5891
            BPS: BPSL0122(fmt)
            BPM: BURPS1710b_0347(fmt) BURPS1710b_2403
            BPL: BURPS1106A_0160(fmt)
            BPD: BURPS668_0151(fmt)
            BTE: BTH_I0129(fmt)
            PNU: Pnuc_0641
            BPE: BP0551(fmt)
            BPA: BPP0244(fmt)
            BBR: BB0248(fmt)
            RFR: Rfer_3859
            POL: Bpro_4638
            MPT: Mpe_A0284
            HAR: HEAR0119(fmt) HEAR0886
            MMS: mma_0144(fmt)
            NEU: NE1971(fmt)
            NET: Neut_0391
            NMU: Nmul_A0393
            EBA: ebA2954(fmt)
            AZO: azo0100(fmt)
            DAR: Daro_0022
            TBD: Tbd_0015
            MFA: Mfla_0186
            HPY: HP1141
            HPJ: jhp1069(fmt)
            HPA: HPAG1_1079
            HHE: HH0420(fmt)
            HAC: Hac_0573(fmt)
            WSU: WS0507(FMT)
            TDN: Tmden_1412
            CJE: Cj0098(fmt)
            CJR: CJE0093(fmt)
            CJJ: CJJ81176_0133(fmt)
            CJU: C8J_0091(fmt)
            CJD: JJD26997_0105(fmt)
            CFF: CFF8240_1534(fmt)
            CCV: CCV52592_1664 CCV52592_1729(fmt)
            CHA: CHAB381_0678(fmt)
            CCO: CCC13826_0347(fmt) CCC13826_0782 CCC13826_1522
            ABU: Abu_1606(fmt)
            NIS: NIS_1229(fmt)
            SUN: SUN_1780(fmt)
            GSU: GSU0130(fmt)
            GME: Gmet_0884 Gmet_3339
            PCA: Pcar_0244
            PPD: Ppro_0055
            DVU: DVU3365(fmt)
            DDE: Dde_0014
            LIP: LI0766(fmt)
            BBA: Bd2757(fmt)
            DPS: DP0747
            ADE: Adeh_3969
            MXA: MXAN_1399(fmt)
            SAT: SYN_02707
            SFU: Sfum_0148
            RPR: RP209(fmt)
            RTY: RT0198(fmt)
            RCO: RC0279(fmt)
            RFE: RF_0325(fmt)
            RBE: RBE_0561(fmt)
            RAK: A1C_01565(fmt)
            RBO: A1I_03210(fmt)
            RCM: A1E_01215(fmt)
            RRI: A1G_01600(fmt)
            OTS: OTBS_1848(fmt)
            WOL: WD0866(fmt)
            WBM: Wbm0656
            AMA: AM313(fmt)
            APH: APH_0965(fmt)
            ERU: Erum2030(fmt)
            ERW: ERWE_CDS_02050(fmt)
            ERG: ERGA_CDS_02000(fmt)
            ECN: Ecaj_0205
            ECH: ECH_0897(fmt)
            NSE: NSE_0094(fmt)
            PUB: SAR11_0457(fmt)
            MLO: mll4854
            MES: Meso_0393
            SME: SMc01100(fmt)
            ATU: Atu0367(fmt)
            ATC: AGR_C_642
            RET: RHE_CH00414(fmt)
            RLE: RL0433(fmt)
            BME: BMEII0265
            BMF: BAB2_0996(fmt)
            BMS: BRA1034(fmt)
            BMB: BruAb2_0974(fmt)
            BOV: BOV_A0975(fmt)
            BJA: bll8108(fmt)
            BRA: BRADO0771(fmt) BRADO3974
            BBT: BBta_4344 BBta_7336(fmt)
            RPA: RPA0622(fmt)
            RPB: RPB_0674
            RPC: RPC_0806
            RPD: RPD_0080
            RPE: RPE_0655
            NWI: Nwi_3065
            NHA: Nham_3694
            BHE: BH00750(fmt)
            BQU: BQ00680(fmt)
            BBK: BARBAKC583_1320(fmt)
            CCR: CC_0279
            SIL: SPO3216(fmt)
            SIT: TM1040_2577
            RSP: RSP_0875(fmt)
            JAN: Jann_0469
            RDE: RD1_1339(fmt)
            MMR: Mmar10_0446
            HNE: HNE_0513(fmt)
            ZMO: ZMO0811(fmt)
            NAR: Saro_2894
            SAL: Sala_0249
            ELI: ELI_02065
            GOX: GOX1835
            GBE: GbCGDNIH1_0691
            RRU: Rru_A3351
            MAG: amb0242
            MGM: Mmc1_0143
            ABA: Acid345_4228
            BSU: BG11937(fmt)
            BHA: BH2508(fmt)
            BAN: BA4004(fmt)
            BAR: GBAA4004(fmt)
            BAA: BA_4475
            BAT: BAS3717
            BCE: BC2629 BC3864(fmt)
            BCA: BCE_3908
            BCZ: BCZK3523(fmt) BCZK3625(fmt)
            BTK: BT9727_3607(fmt)
            BLI: BL02298(fmt)
            BLD: BLi01794(fmt)
            BCL: ABC2318(fmt)
            BAY: RBAM_015560(fmt)
            BPU: BPUM_1472(fmt)
            OIH: OB1506(fmt)
            GKA: GK1172(fmt) GK3125
            SAU: SA1059
            SAV: SAV1216
            SAM: MW1099
            SAR: SAR1192
            SAS: SAS1150
            SAC: SACOL1228(fmt)
            SAB: SAB1080(fmt)
            SAA: SAUSA300_1109(fmt)
            SAO: SAOUHSC_01183
            SEP: SE0891
            SER: SERP0782(fmt)
            SHA: SH1699(fmt)
            SSP: SSP1556
            LMO: lmo1823(fmt)
            LMF: LMOf2365_1851(fmt)
            LIN: lin1937(fmt)
            LWE: lwe1842(fmt)
            LLA: L0362(fmt)
            LLC: LACR_2150
            LLM: llmg_2147(fmt)
            SPY: SPy_1628(fmt)
            SPZ: M5005_Spy_1338
            SPM: spyM18_1638(fmt)
            SPG: SpyM3_1372(fmt)
            SPS: SPs0490
            SPH: MGAS10270_Spy1454
            SPI: MGAS10750_Spy1447
            SPJ: MGAS2096_Spy1359
            SPK: MGAS9429_Spy1333
            SPF: SpyM50453(fmt)
            SPA: M6_Spy1384
            SPB: M28_Spy1379
            SPN: SP_1735
            SPR: spr1580(fmt)
            SPD: SPD_1545(fmt)
            SAG: SAG0316(fmt)
            SAN: gbs0304(fmt)
            SAK: SAK_0386(fmt)
            SMU: SMU.481
            STC: str1428(fmt)
            STL: stu1428(fmt)
            SSA: SSA_1848(fmt)
            SGO: SGO_0597(fmt)
            LPL: lp_1616(fmt)
            LJO: LJ1540
            LAC: LBA1321
            LSA: LSA0689(fmt)
            LSL: LSL_0614(fmt)
            LDB: Ldb1412(fmt)
            LBU: LBUL_1309
            LBR: LVIS_0965
            LCA: LSEI_1625
            LGA: LGAS_0761
            LRE: Lreu_1172
            PPE: PEPE_0829
            EFA: EF3123(fmt)
            OOE: OEOE_0787
            STH: STH1344
            CAC: CAC1723(fmt)
            CPE: CPE1743(fmt)
            CPF: CPF_1005(fmt) CPF_1996(fmt)
            CPR: CPR_1714(fmt)
            CTC: CTC01220(fmt)
            CNO: NT01CX_2244
            CDF: CD2584(fmt)
            CBO: CBO2509
            CBA: CLB_2382(fmt)
            CBH: CLC_2364(fmt)
            CBF: CLI_2570(fmt)
            CHY: CHY_1483(fmt)
            DSY: DSY2693
            SWO: Swol_1231
            TTE: TTE1506(fmt)
            MTA: Moth_0898
            MGE: MG_365(fmt)
            MPN: MPN543(fmt)
            MPU: MYPU_0450(fmt)
            MPE: MYPE500(fmt)
            MGA: MGA_0846(fmt)
            MMY: MSC_0450(fmt)
            MMO: MMOB4050(fmt)
            MSY: MS53_0524(fmt)
            MCP: MCAP_0520(fmt)
            UUR: UU463(fmt)
            MFL: Mfl409
            MTU: Rv1406(fmt)
            MTC: MT1450(fmt)
            MBO: Mb1441(fmt)
            MBB: BCG_1467(fmt)
            MLE: ML0552(fmt)
            MPA: MAP1133(fmt)
            MAV: MAV_3372(fmt)
            MSM: MSMEG_3064(fmt)
            MMC: Mmcs_2383
            CGL: NCgl1538(cgl1600)
            CGB: cg1803(fmt)
            CEF: CE1719
            CDI: DIP1322(fmt)
            CJK: jk1013(fmt)
            NFA: nfa36080(fmt)
            RHA: RHA1_ro04712 RHA1_ro07163(fmt)
            SCO: SCO1473(fmt)
            SMA: SAV6877(fmt)
            TWH: TWT358(fmt)
            TWS: TW411(fmt)
            LXX: Lxx11170(fmt)
            AAU: AAur_1822(fmt)
            PAC: PPA1195
            TFU: Tfu_1075
            FRA: Francci3_3190
            FAL: FRAAL5225(fmt)
            SEN: SACE_2113(fmt) SACE_2691
            BLO: BL1789(fmt)
            BAD: BAD_0544(fmt)
            RXY: Rxyl_1467
            FNU: FN1489
            RBA: RB12854(fmt)
            CTR: CT530(fmt)
            CTA: CTA_0579(fmt)
            CMU: TC0817
            CPN: CPn0649(fmt)
            CPA: CP0098
            CPJ: CPj0649(fmt)
            CPT: CpB0675
            CCA: CCA00091(fmt)
            CAB: CAB091(fmt)
            CFE: CF0915(fmt)
            PCU: pc0404(fmt)
            BGA: BG0063(fmt)
            BAF: BAPKO_0064(fmt)
            TPA: TP0756
            TDE: TDE1644(fmt)
            LIL: LA1596 LA2396
            LIC: LIC11552(fmt) LIC12186
            LBJ: LBJ_1439(fmt)
            LBL: LBL_1663(fmt)
            SYN: slr0070(fmt)
            SYW: SYNW1195(fmt)
            SYC: syc1982_d(fmt)
            SYF: Synpcc7942_2110
            SYD: Syncc9605_1307
            SYE: Syncc9902_1168
            SYG: sync_1301(fmt)
            SYR: SynRCC307_1473(fmt)
            SYX: SynWH7803_1099(fmt)
            CYA: CYA_1691(fmt)
            CYB: CYB_1993(fmt)
            TEL: tlr1873(zam) tlr1874(fmt)
            GVI: glr1831(fmt)
            ANA: alr3460
            AVA: Ava_3481
            PMA: Pro0997(fmt)
            PMM: PMM0841(fmt)
            PMT: PMT0772(fmt)
            PMN: PMN2A_0366
            PMB: A9601_10281(fmt)
            PMC: P9515_09171(fmt)
            PMF: P9303_14401(fmt)
            PMG: P9301_10271(fmt)
            PMH: P9215_10601(fmt)
            PME: NATL1_10481(fmt)
            TER: Tery_1769
            BTH: BT_3945
            BFR: BF3903
            BFS: BF3673(fmt)
            PGI: PG2023(fmt)
            SRU: SRU_2171(fmt)
            CHU: CHU_1570(fmt)
            GFO: GFO_1444(fmt) GFO_2018(fmt)
            FPS: FP2009(fmt)
            CTE: CT1453(fmt)
            CCH: Cag_0487
            PLT: Plut_1472
            DET: DET1642(fmt)
            DEH: cbdb_A1742(fmt)
            DRA: DR_2435
            DGE: Dgeo_2291
            TTH: TTC1663
            TTJ: TTHA0320
            AAE: aq_2131(fmt)
            TMA: TM0528
STRUCTURES  PDB: 1FMT  2FMT  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.2.9
            ExPASy - ENZYME nomenclature database: 2.1.2.9
            ExplorEnz - The Enzyme Database: 2.1.2.9
            ERGO genome analysis and discovery system: 2.1.2.9
            BRENDA, the Enzyme Database: 2.1.2.9
            CAS: 9015-76-3
///
ENTRY       EC 2.1.2.10                 Enzyme
NAME        aminomethyltransferase;
            S-aminomethyldihydrolipoylprotein:(6S)-tetrahydrofolate
            aminomethyltransferase (ammonia-forming);
            T-protein;
            glycine synthase;
            tetrahydrofolate aminomethyltransferase;
            [protein]-8-S-aminomethyldihydrolipoyllysine:tetrahydrofolate
            aminomethyltransferase (ammonia-forming)
CLASS       Transferases;
            Transferring one-carbon groups;
            Hydroxymethyl-, formyl- and related transferases
SYSNAME     [protein]-S8-aminomethyldihydrolipoyllysine:tetrahydrofolate
            aminomethyltransferase (ammonia-forming)
REACTION    [protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate =
            [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
            [RN:R04125]
ALL_REAC    R04125;
            (other) R01221 R02300
SUBSTRATE   [protein]-S8-aminomethyldihydrolipoyllysine [CPD:C01242];
            tetrahydrofolate [CPD:C00101]
PRODUCT     [protein]-dihydrolipoyllysine [CPD:C02972];
            5,10-methylenetetrahydrofolate [CPD:C00143];
            NH3 [CPD:C00014]
COMMENT     A component, with EC 1.4.4.2 glycine dehydrogenase (decarboxylating)
            and EC 1.8.1.4, dihydrolipoyl dehydrogenanse, of the glycine
            cleavage system, formerly known as glycine synthase. The glycine
            cleavage system is composed of four components that only loosely
            associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10),
            the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein [3].
REFERENCE   1  [PMID:7053363]
  AUTHORS   Okamura-Ikeda K, Fujiwara K, Motokawa Y.
  TITLE     Purification and characterization of chicken liver T-protein, a
            component of the glycine cleavage system.
  JOURNAL   J. Biol. Chem. 257 (1982) 135-9.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:10966480]
  AUTHORS   Perham RN.
  TITLE     Swinging arms and swinging domains in multifunctional enzymes:
            catalytic machines for multistep reactions.
  JOURNAL   Annu. Rev. Biochem. 69 (2000) 961-1004.
REFERENCE   3  [PMID:15642479]
  AUTHORS   Nesbitt NM, Baleanu-Gogonea C, Cicchillo RM, Goodson K, Iwig DF,
            Broadwater JA, Haas JA, Fox BG, Booker SJ.
  TITLE     Expression, purification, and physical characterization of
            Escherichia coli lipoyl(octanoyl)transferase.
  JOURNAL   Protein. Expr. Purif. 39 (2005) 269-82.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00670  One carbon pool by folate
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00605  aminomethyltransferase
GENES       HSA: 275(AMT)
            MMU: 434437(Amt)
            RNO: 306586(Amt)
            CFA: 484770(AMT)
            BTA: 280719(AMT)
            GGA: 395566(LOC395566)
            DRE: 450000(amt)
            SPU: 579900(LOC579900)
            DME: Dmel_CG6415
            CEL: F25B4.1(aminomethytransferase)
            OSA: 4337051
            CME: CMG086C
            SCE: YDR019C(GCV1)
            PIC: PICST_83560(GCV1)
            CGR: CAGL0D04356g
            SPO: SPAC31G5.14
            ANI: AN1198.2
            AFM: AFUA_1G10780
            AOR: AO090038000338
            CNE: CNC04350
            DDI: DDB_0231218(gcvT)
            PFA: PF13_0345
            TAN: TA20635
            TBR: Tb09.211.1380 Tb11.01.1440
            TCR: 504017.40 511231.50
            LMA: LmjF36.3800 LmjF36.3810
            ECO: b2905(gcvT)
            ECJ: JW2873(gcvT)
            ECE: Z4242(gcvT)
            ECS: ECs3776
            ECC: c3485(gcvT)
            ECI: UTI89_C3290(gcvT)
            ECP: ECP_2898
            ECV: APECO1_3623(gcvT)
            ECW: EcE24377A_3232(gcvT)
            ECX: EcHS_A3064(gcvT)
            STY: STY3211(gcvT)
            STT: t2973(gcvT)
            SPT: SPA2923(gcvT)
            SEC: SC2996(gcvT)
            STM: STM3055(gcvT)
            YPE: YPO0907(gcvT)
            YPK: y3294(gcvT)
            YPM: YP_3604(gcvT)
            YPA: YPA_0360
            YPN: YPN_3106
            YPP: YPDSF_0607
            YPS: YPTB3182(gcvT)
            YPI: YpsIP31758_0863(gcvT)
            SFL: SF2891(gcvT)
            SFX: S3090(gcvT)
            SFV: SFV_2953(gcvT)
            SSN: SSON_3058(gcvT)
            SBO: SBO_3087(gcvT)
            SDY: SDY_3176(gcvT)
            ECA: ECA0743(gcvT)
            PLU: plu3598(gcvT)
            SGL: SG2002
            XFA: XF0183
            XFT: PD0149(gcvT)
            XCC: XCC2877(gcvT)
            XCB: XC_1232
            XCV: XCV3196(gcvT)
            XAC: XAC3061(gcvT)
            XOO: XOO1794(gcvT)
            XOM: XOO_1697(XOO1697)
            VCO: VC0395_0949(gcvT)
            VVU: VV2_0190
            VVY: VVA0696
            VPA: VPA0805
            VFI: VFA0700
            PPR: PBPRB1319
            PAE: PA2442(gcvT2) PA5215(gcvT1)
            PAU: PA14_33040(gcvT2) PA14_68870(gcvT1)
            PAP: PSPA7_2809(gcvT2) PSPA7_5960(gcvT1)
            PPU: PP_0986(gcvT-1) PP_5194(gcvT-2)
            PST: PSPTO_0316(gcvT-1) PSPTO_1275(gcvT-2)
            PSB: Psyr_0246 Psyr_1095
            PSP: PSPPH_0234(gcvT1) PSPPH_1161(gcvT2)
            PFL: PFL_4643(gcvT) PFL_5962(gcvT)
            PFO: Pfl_4394 Pfl_5428
            PEN: PSEEN4438(gcvT-2) PSEEN5309(gcvT-1)
            PAR: Psyc_0799(gcvT)
            PCR: Pcryo_0806
            SON: SO_0779(gcvT)
            SDN: Sden_0833
            SFR: Sfri_3151
            SAZ: Sama_2721
            SBL: Sbal_0617
            SLO: Shew_3064
            SHE: Shewmr4_3331
            SHM: Shewmr7_0622
            SHN: Shewana3_3501
            SHW: Sputw3181_0730
            ILO: IL2094(gcvT)
            CPS: CPS_1274(gcvT1) CPS_3841(gcvT2)
            PHA: PSHAa2475(gcvT)
            PAT: Patl_3592
            SDE: Sde_0338
            PIN: Ping_2726
            CBU: CBU_1716(gcvT)
            CBD: COXBU7E912_0289(gcvT)
            LPN: lpg0118(gcvT1)
            LPF: lpl0117(gcvT)
            LPP: lpp0132(gcvT)
            MCA: MCA0350(gcvT)
            FTU: FTT0407(gcvT)
            FTF: FTF0407(gcvT)
            FTW: FTW_1666(gcvT)
            FTL: FTL_0477
            FTH: FTH_0475(gcvT)
            FTA: FTA_0503(gcvT)
            FTN: FTN_0505(gcvT)
            TCX: Tcr_1349
            NOC: Noc_0500
            AEH: Mlg_2576
            HHA: Hhal_1190
            HCH: HCH_03858(gcvT)
            CSA: Csal_1815
            ABO: ABO_2594(gcvT)
            AHA: AHA_1718(gcvT)
            DNO: DNO_1197(gcvT)
            RMA: Rmag_0924
            VOK: COSY_0830(gcvT)
            NME: NMB0574
            NMA: NMA0758(gcvT)
            NMC: NMC0516(gcvT)
            NGO: NGO1406
            CVI: CV_3431(gcvT)
            RSO: RSc3293(gcvT)
            REU: Reut_A3329 Reut_B4806 Reut_B4828
            REH: H16_A1567(gcvT2) H16_A3619(gcvT1)
            RME: Rmet_3480
            BMA: BMA2994.1(gcvT)
            BMV: BMASAVP1_A3309(gcvT)
            BML: BMA10299_A1542(gcvT)
            BMN: BMA10247_3061(gcvT)
            BXE: Bxe_A0056
            BVI: Bcep1808_3457
            BUR: Bcep18194_A3325 Bcep18194_B0488
            BCN: Bcen_2909 Bcen_3218
            BCH: Bcen2424_0146 Bcen2424_5149
            BAM: Bamb_0133 Bamb_4544
            BPS: BPSL3360(gcvT)
            BPM: BURPS1710b_0127(gcvT)
            BPL: BURPS1106A_3997(gcvT)
            BPD: BURPS668_3926(gcvT)
            BTE: BTH_I3255
            BPE: BP0195(gcvT)
            BPA: BPP0769(gcvT)
            BBR: BB0854(gcvT)
            RFR: Rfer_3019
            POL: Bpro_1868
            PNA: Pnap_2683
            AAV: Aave_3145
            AJS: Ajs_1938
            VEI: Veis_3957 Veis_4048
            MPT: Mpe_A1433
            NEU: NE0607(gcvT)
            NET: Neut_1955
            NMU: Nmul_A0214
            EBA: ebA6126(gcvT)
            AZO: azo1287(gcvT) azo1593
            DAR: Daro_2463
            TBD: Tbd_0178
            MFA: Mfla_0439 Mfla_0454
            GSU: GSU0375(gcvT)
            GME: Gmet_3155
            DVU: DVU1684(gcvT)
            DDE: Dde_1996
            BBA: Bd0684
            DPS: DP0301
            ADE: Adeh_1245
            MXA: MXAN_3040(gcvT) MXAN_6341(gcvT)
            APH: APH_1270
            ERU: Erum0890
            ERW: ERWE_CDS_00850
            ECN: Ecaj_0089
            PUB: SAR11_0246 SAR11_0621 SAR11_0666(gcvT) SAR11_1265 SAR11_1303
            MLO: mll7302 mlr0883 mlr3677 mlr4790 mlr7320
            MES: Meso_1018 Meso_4268
            SME: SMa2145 SMc02047(gcvT) SMc04148
            ATU: Atu1464(gcvT)
            ATC: AGR_C_2701
            RET: RHE_CH02241(gcvT) RHE_PE00406(ype00213) RHE_PE00415(ype00217)
            RLE: RL2572(gcvT) pRL110541 pRL110552
            BME: BMEII0559
            BMF: BAB2_0513(gcvT)
            BMS: BRA0727(gcvT)
            BMB: BruAb2_0504(gcvT)
            BOV: BOV_A0681(gcvT)
            BJA: blr5751(gcvT)
            BRA: BRADO2047 BRADO4982(gcvT)
            BBT: BBta_2375 BBta_5449(gcvT)
            RPA: RPA3848(gcvT2)
            RPB: RPB_3738
            RPC: RPC_1570
            RPD: RPD_1733
            RPE: RPE_1597
            NWI: Nwi_1286
            NHA: Nham_1620
            BHE: BH12840(gcvT)
            BQU: BQ10130(gcvT)
            BBK: BARBAKC583_1096(gcvT)
            CCR: CC_3355
            SIL: SPO1562 SPOA0057(gcvT)
            SIT: TM1040_0971 TM1040_1444 TM1040_2393
            RSP: RSP_2193(gcvT)
            RSH: Rsph17029_0868
            JAN: Jann_2379 Jann_3620
            RDE: RD1_0003 RD1_1222(gcvT) RD1_1747 RD1_2288 RD1_3858
            PDE: Pden_2348
            MMR: Mmar10_2211
            HNE: HNE_2719(gcvT)
            NAR: Saro_1850
            SAL: Sala_1871
            ELI: ELI_10075
            GOX: GOX1095 GOX2022
            GBE: GbCGDNIH1_1824 GbCGDNIH1_1826
            RRU: Rru_A3051
            MAG: amb0766
            MGM: Mmc1_1559
            ABA: Acid345_1269 Acid345_2461 Acid345_2628
            SUS: Acid_0484
            BSU: BG11509(gcvT)
            BHA: BH2816
            BAN: BA4449(gcvT)
            BAR: GBAA4449(gcvT)
            BAA: BA_4903
            BAT: BAS4131
            BCE: BC4226
            BCA: BCE_4305(gcvT)
            BCZ: BCZK3981(gcvT)
            BTK: BT9727_3971(gcvT)
            BTL: BALH_3829(gcvT)
            BLI: BL01562(gcvT)
            BLD: BLi02631(gcvT)
            BCL: ABC2495(gcvT)
            BAY: RBAM_022890(gcvT)
            BPU: BPUM_2189(gcvT)
            OIH: OB1904
            GKA: GK2425
            SAU: SA1367
            SAV: SAV1537
            SAM: MW1489
            SAR: SAR1614(gcvT)
            SAS: SAS1475
            SAC: SACOL1595(gcvT)
            SAB: SAB1409c(gcvT)
            SAA: SAUSA300_1498(gcvT)
            SAO: SAOUHSC_01634
            SEP: SE1222
            SER: SERP1102(gcvT)
            SHA: SH1379
            SSP: SSP1218
            LMO: lmo1348
            LMF: LMOf2365_1365(gcvT)
            LIN: lin1385
            LWE: lwe1363(gcvT)
            STH: STH1922
            CDF: CD1657
            CBO: CBO0696(gcvT)
            CBA: CLB_0735(gcvT)
            CBH: CLC_0750(gcvT)
            CBF: CLI_0765(gcvT)
            CKL: CKL_1774(gcvT)
            CHY: CHY_0489(gcvT)
            DSY: DSY2880
            DRM: Dred_0720
            SWO: Swol_1983
            TTE: TTE0296(gcvT)
            MTA: Moth_1945
            MTU: Rv2211c(gcvT)
            MTC: MT2267(gcvT)
            MBO: Mb2234c(gcvT)
            MBB: BCG_2227c(gcvT)
            MLE: ML0865(gcvT)
            MPA: MAP1951c(gcvT)
            MAV: MAV_2280(gcvT)
            MSM: MSMEG_4278(gcvT)
            MGI: Mflv_5134
            MMC: Mmcs_3309
            CGB: cg2852
            CJK: jk0210(gcvT)
            NFA: nfa16960(gcvT)
            RHA: RHA1_ro01148(gcvT1) RHA1_ro02931(gcvT2)
            SCO: SCO5472(gcvT)
            SMA: SAV2773(gcvT)
            TWH: TWT638(gcvT)
            TWS: TW659(gcvT)
            CMI: CMM_2197(gcvT)
            AAU: AAur_0988(gcvT) AAur_4006(gcvT)
            PAC: PPA0744
            TFU: Tfu_2351
            FRA: Francci3_3132
            FAL: FRAAL5148(gcvT)
            SEN: SACE_5617 SACE_5701(gcvT)
            RXY: Rxyl_0470 Rxyl_0764 Rxyl_0767 Rxyl_2496 Rxyl_3184
            RBA: RB7587(gcvT)
            PCU: pc0281(gcvT)
            TDE: TDE1627(gcvT)
            LIL: LA0362
            LIC: LIC10311(gcvT)
            LBJ: LBJ_2730(gcvT)
            LBL: LBL_0340(gcvT)
            SYN: sll0171(gcvT)
            SYW: SYNW2425(gcvT)
            SYC: syc1794_c(gcvT)
            SYF: Synpcc7942_2308
            SYD: Syncc9605_2594
            SYE: Syncc9902_2232
            SYG: sync_2853(gcvT)
            SYR: SynRCC307_2437(gcvT)
            SYX: SynWH7803_2457(gcvT)
            CYA: CYA_1242(gcvT)
            CYB: CYB_1141(gcvT)
            TEL: tll0745
            GVI: glr3530
            ANA: all4609
            AVA: Ava_1651 Ava_2760
            PMA: Pro1851(gcvT)
            PMM: PMM1687(gcvT)
            PMT: PMT2215(gcvT)
            PMN: PMN2A_1289
            PMI: PMT9312_1780
            PMB: A9601_18971(gcvT)
            PMC: P9515_18781(gcvT)
            PMF: P9303_29531(gcvT)
            PMG: P9301_18781(gcvT)
            PMH: P9215_19601(gcvT)
            PME: NATL1_21611(gcvT)
            TER: Tery_2041
            BTH: BT_4584
            BFR: BF1303
            BFS: BF1290(gcvT)
            PGI: PG1559(gcvT)
            SRU: SRU_1617(gcvT)
            CHU: CHU_2824(gcvT)
            GFO: GFO_1498(gcvT)
            FPS: FP0836(gcvT)
            CTE: CT1788(gcvT)
            CCH: Cag_1656
            PVI: Cvib_0451
            PLT: Plut_0396
            DRA: DR_1812
            DGE: Dgeo_1905
            TTH: TTC0148
            TTJ: TTHA0523
            AAE: aq_1458(gcvT)
            TMA: TM0211
            HAL: VNG1606G(gcvT1) VNG2640G(gcvT2)
            HMA: pNG7361(gcvT5) pNG7366(gcvT3) pNG7370(gcvT1) rrnAC1500(gcvT2)
                 rrnAC2552(gcvT4)
            HWA: HQ1760A(gcvT) HQ1761A(gcvT) HQ1856A(gcvT) HQ3112A(gcvT)
            NPH: NP0436A(gcvT_2) NP4774A(gcvT)
            TAC: Ta0010m
            TVO: TVN0058
            PTO: PTO0503
            PAB: PAB1638
            PFU: PF1341
            TKO: TK2035
            APE: APE_1695.1
            SSO: SSO0919(gcvT)
            STO: ST1206
            SAI: Saci_1383(gcvT)
STRUCTURES  PDB: 1V5V  1VLO  1WOO  1WOP  1WOR  1WOS  1WSR  1WSV  1YX2  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.2.10
            ExPASy - ENZYME nomenclature database: 2.1.2.10
            ExplorEnz - The Enzyme Database: 2.1.2.10
            ERGO genome analysis and discovery system: 2.1.2.10
            BRENDA, the Enzyme Database: 2.1.2.10
            CAS: 37257-08-2
///
ENTRY       EC 2.1.2.11                 Enzyme
NAME        3-methyl-2-oxobutanoate hydroxymethyltransferase;
            alpha-ketoisovalerate hydroxymethyltransferase;
            dehydropantoate hydroxymethyltransferase;
            ketopantoate hydroxymethyltransferase;
            oxopantoate hydroxymethyltransferase;
            5,10-methylene tetrahydrofolate:alpha-ketoisovalerate
            hydroxymethyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Hydroxymethyl-, formyl- and related transferases
SYSNAME     5,10-methylenetetrahydrofolate:3-methyl-2-oxobutanoate
            hydroxymethyltransferase
REACTION    5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O =
            tetrahydrofolate + 2-dehydropantoate [RN:R01226]
ALL_REAC    R01226
SUBSTRATE   5,10-methylenetetrahydrofolate [CPD:C00143];
            3-methyl-2-oxobutanoate [CPD:C00141];
            H2O [CPD:C00001]
PRODUCT     tetrahydrofolate [CPD:C00101];
            2-dehydropantoate [CPD:C00966]
REFERENCE   1  [PMID:6463]
  AUTHORS   Powers SG, Snell EE.
  TITLE     Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and
            regulatory properties.
  JOURNAL   J. Biol. Chem. 251 (1976) 3786-93.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:776976]
  AUTHORS   Teller JH, Powers SG, Snell EE.
  TITLE     Ketopantoate hydroxymethyltransferase. I. Purification and role in
            pantothenate biosynthesis.
  JOURNAL   J. Biol. Chem. 251 (1976) 3780-5.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K00606  3-methyl-2-oxobutanoate hydroxymethyltransferase
GENES       OSA: 4326739
            CME: CML076C
            SCE: YBR176W(ECM31)
            AGO: AGOS_ABR186W
            PIC: PICST_38073(ECM31)
            CGR: CAGL0M06215g
            SPO: SPAC5H10.09c
            ANI: AN1778.2
            AFM: AFUA_6G09170
            AOR: AO090001000594
            DDI: DDB_0231509
            ECO: b0134(panB)
            ECJ: JW0130(panB)
            ECE: Z0145(panB)
            ECS: ECs0138
            ECC: c0165(panB)
            ECI: UTI89_C0148(panB)
            ECP: ECP_0143
            ECV: APECO1_1851(panB)
            ECW: EcE24377A_0137(panB)
            ECX: EcHS_A0138
            STY: STY0200(panB)
            STT: t0183(panB)
            SPT: SPA0188(panB)
            SEC: SC0182(panB)
            STM: STM0182(panB)
            YPE: YPO3401(panB)
            YPK: y0786(panB)
            YPM: YP_0284(panB)
            YPA: YPA_2902
            YPN: YPN_0688
            YPP: YPDSF_2955
            YPS: YPTB0730(panB)
            YPI: YpsIP31758_3343(panB)
            YEN: YE0720(panB)
            SFX: S0133(panB)
            SFV: SFV_0124(panB)
            SSN: SSON_0142(panB)
            SBO: SBO_0123(panB)
            SDY: SDY_0154(panB)
            ECA: ECA3321(panB)
            PLU: plu0872(panB)
            BUC: BU197(panB)
            BAS: BUsg191(panB)
            WBR: WGLp449(panB)
            SGL: SG0488
            ENT: Ent638_0681
            SPE: Spro_3991
            XFA: XF0229
            XFT: PD0187(panB)
            XCC: XCC1768(panB)
            XCB: XC_2468
            XCV: XCV1816(panB)
            XAC: XAC1785(panB)
            XOO: XOO2364(panB)
            XOM: XOO_2245(XOO2245)
            VCH: VC0592
            VCO: VC0395_A0123(panB)
            VVU: VV1_1643
            VVY: VV2763
            VPA: VP2506
            VFI: VF2169 VFA0628
            PPR: PBPRA3175
            PAE: PA1598 PA4729
            PAU: PA14_43830(panB) PA14_62580(panB)
            PAP: PSPA7_3676(panB2) PSPA7_5446(panB1)
            PPU: PP_4699(panB)
            PPF: Pput_4564
            PST: PSPTO_0961(panB)
            PSB: Psyr_0828(panB)
            PSP: PSPPH_0854(panB)
            PFL: PFL_5227(panB) PFL_5277(panB)
            PFO: Pfl_4811(panB)
            PEN: PSEEN2896(panB-2) PSEEN4735(panB)
            PMY: Pmen_3592
            PAR: Psyc_0116(panB)
            PCR: Pcryo_0125
            PRW: PsycPRwf_2131
            ACI: ACIAD3061(panB)
            SON: SO_0870(panB)
            SDN: Sden_3174
            SFR: Sfri_3280
            SAZ: Sama_0776
            SBL: Sbal_2858 Sbal_3494
            SBM: Shew185_0845 Shew185_2875
            SLO: Shew_3133
            SPC: Sputcn32_3132
            SSE: Ssed_3903
            SPL: Spea_0694
            SHE: Shewmr4_0726
            SHM: Shewmr7_3296
            SHN: Shewana3_3408
            SHW: Sputw3181_0811
            ILO: IL2254(panB)
            CPS: CPS_4312(panB)
            PHA: PSHAa0602(panB)
            PAT: Patl_3933
            SDE: Sde_3379
            PIN: Ping_0580
            MAQ: Maqu_0667
            CBU: CBU_0424(panB)
            CBD: COXBU7E912_1649(panB)
            LPN: lpg2661(panB)
            LPF: lpl2588(panB)
            LPP: lpp2715(panB)
            MCA: MCA2314(panB)
            FTU: FTT1389(panB)
            FTF: FTF1389(panB)
            FTW: FTW_0499(panB)
            FTL: FTL_0674
            FTH: FTH_0677(panB)
            FTA: FTA_0709(panB)
            FTN: FTN_1352(panB)
            TCX: Tcr_1526
            NOC: Noc_0885
            AEH: Mlg_0564
            HHA: Hhal_0675
            HCH: HCH_00810(panB1) HCH_06264(panB2)
            CSA: Csal_3065
            ABO: ABO_0337(panB)
            MMW: Mmwyl1_4016
            AHA: AHA_3538(panB)
            BCI: BCI_0230(panB)
            RMA: Rmag_0415
            VOK: COSY_0384(panB)
            NME: NMB0870
            NMA: NMA1088(panB)
            NMC: NMC0811(panB)
            NGO: NGO0436
            CVI: CV_1635(panB) CV_3290
            RSO: RSc2630(panB)
            REU: Reut_A2780(panB)
            REH: H16_A3084(panB)
            RME: Rmet_2917
            BMA: BMA2323(panB)
            BMV: BMASAVP1_A0504(panB)
            BML: BMA10299_A1095(panB)
            BMN: BMA10247_2202(panB)
            BXE: Bxe_A3958
            BVI: Bcep1808_0715
            BUR: Bcep18194_A3842(panB) Bcep18194_B2722
            BCN: Bcen_0271
            BCH: Bcen2424_0755 Bcen2424_3447
            BAM: Bamb_0649 Bamb_5229
            BPS: BPSL2824(panB)
            BPM: BURPS1710b_3317(panB)
            BPL: BURPS1106A_3307(panB)
            BPD: BURPS668_3274(panB)
            BTE: BTH_I1311(panB)
            PNU: Pnuc_1767
            BPE: BP2850(panB)
            BPA: BPP4094(panB)
            BBR: BB4565(panB)
            RFR: Rfer_3033
            POL: Bpro_0896
            PNA: Pnap_0934
            AAV: Aave_3852
            AJS: Ajs_3499
            VEI: Veis_0028
            MPT: Mpe_A0783 Mpe_A1156
            HAR: HEAR2641(panB)
            MMS: mma_2878
            NEU: NE0072(panB)
            NET: Neut_2293
            NMU: Nmul_A0879
            EBA: ebA7119(panB)
            AZO: azo3144(panB)
            DAR: Daro_3185
            TBD: Tbd_2053
            MFA: Mfla_0597
            HPY: HP1058
            HPJ: jhp0367(panB)
            HPA: HPAG1_0389
            HHE: HH0507(panB)
            HAC: Hac_1169(panB)
            WSU: WS1826
            TDN: Tmden_1679
            CJE: Cj0298c(panB)
            CJR: CJE0343(panB)
            CJJ: CJJ81176_0321(panB)
            CJU: C8J_0275(panB)
            CJD: JJD26997_1666(panB)
            CFF: CFF8240_0469(panB)
            CCV: CCV52592_0667 CCV52592_1923(panB)
            CHA: CHAB381_0735(panB)
            CCO: CCC13826_0378(panB) CCC13826_0813(panB)
            ABU: Abu_1775(panB)
            NIS: NIS_0373(panB)
            SUN: SUN_2097(panB)
            GSU: GSU1705(panB)
            GME: Gmet_1642
            GUR: Gura_2078
            PCA: Pcar_1830
            PPD: Ppro_3536
            DVU: DVU2446(panB)
            DVL: Dvul_0789
            DDE: Dde_1500
            BBA: Bd3560(panB)
            DPS: DP2907
            ADE: Adeh_3682
            AFW: Anae109_3809
            MXA: MXAN_2055(panB)
            SAT: SYN_02773
            SFU: Sfum_2737
            AMA: AM142(panB)
            PUB: SAR11_0653(panB)
            MLO: mll0197 mll1731 mlr7631
            MES: Meso_2559
            PLA: Plav_3495
            SME: SMb20821 SMc01881(panB)
            SMD: Smed_2059
            ATU: Atu3483(panB)
            ATC: AGR_L_2695
            RET: RHE_PE00443(ype00224) RHE_PF00002(panB)
            RLE: pRL110619 pRL120360(panB)
            BME: BMEI1592
            BMF: BAB1_0360(panB)
            BMS: BR0330(panB)
            BMB: BruAb1_0356(panB)
            BOV: BOV_0347(panB)
            OAN: Oant_0427
            BJA: blr1626 blr2101(panB) blr4048(panB)
            BBT: BBta_3771(panB)
            RPA: RPA3098(panB)
            RPB: RPB_2445
            RPC: RPC_2276
            RPD: RPD_3008
            RPE: RPE_3348
            NWI: Nwi_2024
            NHA: Nham_1683
            BHE: BH05130(panB)
            BQU: BQ04320(panB)
            BBK: BARBAKC583_0477(panB)
            XAU: Xaut_1442
            CCR: CC_1651
            SIL: SPO0102(panB)
            SIT: TM1040_3438
            RSP: RSP_1756(panB)
            RSH: Rsph17029_0402
            RSQ: Rsph17025_2496
            RDE: RD1_0093(panB)
            PDE: Pden_1657
            MMR: Mmar10_1200
            HNE: HNE_0771(panB)
            ZMO: ZMO1952(panB) ZMO1970(panB)
            NAR: Saro_2043
            SAL: Sala_2206
            SWI: Swit_3123
            ELI: ELI_05345
            GBE: GbCGDNIH1_1251
            ACR: Acry_0665
            RRU: Rru_A3321
            MAG: amb4370
            MGM: Mmc1_0040
            ABA: Acid345_4746
            BSU: BG11519(panB)
            BHA: BH1687(panB)
            BAN: BA1562(panB)
            BAR: GBAA1562(panB)
            BAA: BA_2081
            BAT: BAS1449
            BCE: BC1540
            BCA: BCE_1668(panB)
            BCZ: BCZK1422(panB)
            BCY: Bcer98_1262
            BTK: BT9727_1421(panB)
            BTL: BALH_1392
            BLI: BL02752(panB)
            BLD: BLi02378(panB)
            BCL: ABC2067(panB)
            BAY: RBAM_020580
            BPU: BPUM_1974
            OIH: OB3274
            GKA: GK2179(panB)
            SAU: SA2392(panB)
            SAV: SAV2599(panB)
            SAM: MW2518(panB)
            SAR: SAR2677(panB)
            SAS: SAS2484
            SAC: SACOL2615(panB)
            SAB: SAB2472c(panB)
            SAA: SAUSA300_2534(panB)
            SAO: SAOUHSC_02919
            SAJ: SaurJH9_2621
            SAH: SaurJH1_2675
            SEP: SE2141
            SER: SERP2152(panB)
            SHA: SH0181(panB)
            SSP: SSP0154
            LMO: lmo1902(panB)
            LMF: LMOf2365_1931(panB)
            LIN: lin2016(panB)
            LWE: lwe1921(panB)
            EFA: EF1860(panB)
            CAC: CAC2914(panB)
            CNO: NT01CX_1071(panB)
            CTH: Cthe_0902
            CDF: CD1513(panB)
            CBO: CBO0425(panB)
            CBA: CLB_0458(panB)
            CBH: CLC_0491(panB)
            CBF: CLI_0510(panB)
            CBE: Cbei_2610
            CKL: CKL_0637(panB)
            AMT: Amet_1189
            CHY: CHY_2377(panB)
            DSY: DSY0428
            DRM: Dred_0160 Dred_1788
            SWO: Swol_0101
            CSC: Csac_2710
            MTA: Moth_0121
            MTU: Rv2225(panB)
            MTC: MT2284(panB)
            MBO: Mb2249(panB)
            MBB: BCG_2242(panB)
            MLE: ML1635(panB)
            MPA: MAP1970(panB)
            MAV: MAV_2239(panB)
            MSM: MSMEG_4298(panB)
            MVA: Mvan_3602
            MGI: Mflv_2903
            MMC: Mmcs_3332
            MKM: Mkms_3394
            MJL: Mjls_3343
            CGL: NCgl0113(cgl0114)
            CGB: cg0149(panB)
            CEF: CE0116(panB)
            CDI: DIP2358(panB)
            CJK: jk0674(panB)
            NFA: nfa16500(panB)
            RHA: RHA1_ro01169(panB)
            SCO: SCO2256(panB)
            SMA: SAV5943(panB)
            TWH: TWT260(panB)
            TWS: TW510(panB)
            LXX: Lxx10000(panB)
            CMI: CMM_1633(panB)
            ART: Arth_1591
            AAU: AAur_1730(panB)
            NCA: Noca_2042
            TFU: Tfu_0981
            FRA: Francci3_3149
            FAL: FRAAL5171(panB)
            ACE: Acel_0917
            KRA: Krad_3298
            SEN: SACE_1604(panB)
            STP: Strop_3341
            RBA: RB9090(panB)
            LIL: LA3958(panB)
            LIC: LIC13163(panB)
            LBJ: LBJ_0347(panB)
            LBL: LBL_2729(panB)
            SYN: slr0526(panB)
            SYW: SYNW1645(panB)
            SYC: syc1724_c(panB)
            SYF: Synpcc7942_2381
            SYD: Syncc9605_0845
            SYE: Syncc9902_1545
            SYG: sync_0730(panB)
            SYR: SynRCC307_0599(panB)
            SYX: SynWH7803_1760(panB)
            CYA: CYA_2489(panB)
            CYB: CYB_0701(panB)
            TEL: tlr0279(panB)
            GVI: gll0762(panB)
            ANA: all1522
            AVA: Ava_3909
            PMA: Pro1384(panB)
            PMM: PMM1310(panB)
            PMT: PMT0318(panB)
            PMN: PMN2A_0876
            PMI: PMT9312_1406
            PMB: A9601_15091(panB)
            PMC: P9515_14711(panB)
            PMF: P9303_19981(panB)
            PMG: P9301_14961(panB)
            PMH: P9215_15391
            PME: NATL1_17301(panB)
            TER: Tery_4423
            BTH: BT_0698
            BFR: BF2163
            BFS: BF2220(panB)
            PGI: PG0588(panB)
            SRU: SRU_1843(panB)
            CHU: CHU_3218(panB)
            GFO: GFO_2090(panB)
            FJO: Fjoh_4711
            FPS: FP0885(panB1) FP1580(panB2)
            CTE: CT1341(panB)
            CCH: Cag_0907
            CPH: Cpha266_1658
            PVI: Cvib_0725
            PLT: Plut_1328
            DET: DET0803(panB)
            DEH: cbdb_A781(panB)
            DEB: DehaBAV1_0727
            RRS: RoseRS_0745
            RCA: Rcas_0334
            DRA: DR_2615
            DGE: Dgeo_0411
            TTH: TTC0039
            TTJ: TTHA0407
            AAE: aq_1973(panB)
            TMA: TM1728
            TPT: Tpet_1023
            TME: Tmel_1307
            FNO: Fnod_1213
            HAL: VNG1478G(panB)
            HMA: rrnAC0878(panB)
            NPH: NP4334A(panB)
            PHO: PH0951
            PAB: PAB0570(nB)
            PFU: PF1143
            TKO: TK0363
            APE: APE_0676
            SMR: Smar_1381
            IHO: Igni_0392
            HBU: Hbut_1523
            SSO: SSO2400(panB)
            STO: ST0533
            SAI: Saci_0948(panB)
            MSE: Msed_0615
            PAI: PAE3410
            PIS: Pisl_1362
            PCL: Pcal_1504
            PAS: Pars_2004
STRUCTURES  PDB: 1M3U  1O66  1O68  1OY0  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.2.11
            ExPASy - ENZYME nomenclature database: 2.1.2.11
            ExplorEnz - The Enzyme Database: 2.1.2.11
            ERGO genome analysis and discovery system: 2.1.2.11
            BRENDA, the Enzyme Database: 2.1.2.11
            CAS: 56093-17-5
///
ENTRY       EC 2.1.2.12       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring one-carbon groups;
            Hydroxymethyl-, formyl- and related transferases
COMMENT     Deleted entry: now EC 2.1.1.74
            methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase
            (FADH2-oxidizing) (EC 2.1.2.12 created 1983, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.2.12
            ExPASy - ENZYME nomenclature database: 2.1.2.12
            ExplorEnz - The Enzyme Database: 2.1.2.12
            ERGO genome analysis and discovery system: 2.1.2.12
            BRENDA, the Enzyme Database: 2.1.2.12
///
ENTRY       EC 2.1.2.-                  Enzyme
CLASS       Transferases;
            Transferring one-carbon groups;
            Hydroxymethyl-, formyl- and related transferases
REACTION    (1) Formate + ATP + 5'-Phosphoribosylglycinamide <=> ADP +
            Orthophosphate + 5'-Phosphoribosyl-N-formylglycinamide [RN:R06974];
            (2) 10-Formyltetrahydrofolate + UDP-L-Ara4N <=> Tetrahydrofolate +
            UDP-L-Ara4FN [RN:R07660]
SUBSTRATE   Formate [CPD:C00058];
            ATP [CPD:C00002];
            5'-Phosphoribosylglycinamide [CPD:C03838]
PRODUCT     ADP [CPD:C00008];
            Orthophosphate [CPD:C00009];
            5'-Phosphoribosyl-N-formylglycinamide [CPD:C04376]
///
ENTRY       EC 2.1.3.1                  Enzyme
NAME        methylmalonyl-CoA carboxytransferase;
            transcarboxylase;
            methylmalonyl coenzyme A carboxyltransferase;
            methylmalonyl-CoA transcarboxylase;
            oxalacetic transcarboxylase;
            methylmalonyl-CoA carboxyltransferase;
            methylmalonyl-CoA carboxyltransferase;
            (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase;
            (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxytransferase
            carboxytransferase [incorrect]
CLASS       Transferases;
            Transferring one-carbon groups;
            Carboxy- and carbamoyltransferases
SYSNAME     (S)-methylmalonyl-CoA:pyruvate carboxytransferase
REACTION    (S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate
            [RN:R00930]
ALL_REAC    R00930;
            (other) R00353
SUBSTRATE   (S)-methylmalonyl-CoA [CPD:C00683];
            pyruvate [CPD:C00022]
PRODUCT     propanoyl-CoA [CPD:C00100];
            oxaloacetate [CPD:C00036]
COFACTOR    Zinc [CPD:C00038];
            Biotin [CPD:C00120];
            Cobalt [CPD:C00175]
COMMENT     A biotinyl-protein, containing cobalt and zinc.
REFERENCE   1  [PMID:2920730]
  AUTHORS   Hoffmann A, Hilpert W, Dimroth P.
  TITLE     The carboxyltransferase activity of the sodium-ion-translocating
            methylmalonyl-CoA decarboxylase of Veillonella alcalescens.
  JOURNAL   Eur. J. Biochem. 179 (1989) 645-50.
  ORGANISM  Veillonella alcalescens
REFERENCE   2
  AUTHORS   Swick, R.W. and Wood, H.G.
  TITLE     The role of transcarboxylation in propionic acid fermentation.
  JOURNAL   Proc. Natl. Acad. Sci. USA 46 (1960) 28-41.
  ORGANISM  Propionibacterium shermanii
PATHWAY     PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K03416  methylmalonyl-CoA carboxyltransferase
GENES       MSM: MSMEG_6577
            CGL: NCgl1273(cgl1327)
            PAC: PPA2007 PPA2008
STRUCTURES  PDB: 1DCZ  1DD2  1ON3  1ON9  1RQB  1RQE  1RQH  1RR2  1S3H  1U5J  
                 2D5D  2EVB  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.3.1
            ExPASy - ENZYME nomenclature database: 2.1.3.1
            ExplorEnz - The Enzyme Database: 2.1.3.1
            ERGO genome analysis and discovery system: 2.1.3.1
            UM-BBD (Biocatalysis/Biodegradation Database): 2.1.3.1
            BRENDA, the Enzyme Database: 2.1.3.1
            CAS: 9029-86-1
///
ENTRY       EC 2.1.3.2                  Enzyme
NAME        aspartate carbamoyltransferase;
            carbamylaspartotranskinase;
            aspartate transcarbamylase;
            aspartate carbamyltransferase;
            aspartic acid transcarbamoylase;
            aspartic carbamyltransferase;
            aspartic transcarbamylase;
            carbamylaspartotranskinase;
            L-aspartate transcarbamoylase;
            L-aspartate transcarbamylase;
            carbamoylaspartotranskinase;
            aspartate transcarbamylase;
            aspartate transcarbamoylase;
            ATCase
CLASS       Transferases;
            Transferring one-carbon groups;
            Carboxy- and carbamoyltransferases
SYSNAME     carbamoyl-phosphate:L-aspartate carbamoyltransferase
REACTION    carbamoyl phosphate + L-aspartate = phosphate +
            N-carbamoyl-L-aspartate [RN:R01397]
ALL_REAC    R01397
SUBSTRATE   carbamoyl phosphate [CPD:C00169];
            L-aspartate [CPD:C00049]
PRODUCT     phosphate [CPD:C00009];
            N-carbamoyl-L-aspartate [CPD:C00438]
INHIBITOR   CTP [CPD:C00063];
            UTP [CPD:C00075]
EFFECTOR    ATP [CPD:C00002]
REFERENCE   1  [PMID:13319326]
  AUTHORS   LOWENSTEIN JM, COHEN PP.
  TITLE     Studies on the biosynthesis of carbamylaspartic acid.
  JOURNAL   J. Biol. Chem. 220 (1956) 57-70.
  ORGANISM  Streptococcus faecalis
REFERENCE   2
  AUTHORS   Reichard, P. and Hanshoff, G.
  TITLE     Aspartate carbamyl transferase from Escherichia coli.
  JOURNAL   Acta Chem. Scand. 10 (1956) 548-566.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Shepherson, M. and Pardee, A.B.
  TITLE     Production and crystallization of aspartate transcarbamylase.
  JOURNAL   J. Biol. Chem. 235 (1960) 3233-3237.
  ORGANISM  Streptococcus faecalis
PATHWAY     PATH: map00240  Pyrimidine metabolism
            PATH: map00252  Alanine and aspartate metabolism
ORTHOLOGY   KO: K00608  aspartate carbamoyltransferase
            KO: K00609  aspartate carbamoyltransferase catalytic chain
            KO: K00610  aspartate carbamoyltransferase regulatory chain
GENES       HSA: 790(CAD)
            MMU: 69719(Cad)
            CFA: 483009(CAD)
            DME: Dmel_CG18572(r)
            CEL: D2085.1(pyr-1)
            ATH: AT3G20330
            OSA: 4345071
            CME: CMQ255C
            SCE: YJL130C(URA2)
            AGO: AGOS_ACR263C
            CAL: CaO19.2360 CaO19_4630(CaO19.4630)
            CGR: CAGL0L05676g
            SPO: SPAC22G7.06c(ura1)
            ANI: AN0565.2
            AFM: AFUA_6G11310
            AOR: AO090023000483
            CNE: CNA06000
            DDI: DDB_0201646(pyr1-3)
            PFA: MAL13P1.221
            TAN: TA05175 TA20650
            TPV: TP01_0476
            TBR: Tb927.5.3820
            TCR: 507091.50 508375.30 511643.30 511923.110
            LMA: LmjF16.0540
            ECO: b4244(pyrI) b4245(pyrB)
            ECJ: JW4203(pyrI) JW4204(pyrB)
            ECE: Z5855(pyrI) Z5856(pyrB)
            ECS: ECs5221 ECs5222
            ECC: c5344(pyrI) c5345(pyrB)
            ECI: UTI89_C4850(pyrI) UTI89_C4851(pyrB)
            ECP: ECP_4494 ECP_4495
            ECV: APECO1_2147(pyrB) APECO1_2148(pyrI)
            ECW: EcE24377A_4818(pyrB)
            ECX: EcHS_A4501
            STY: STY4799(pyrI) STY4800(pyrB)
            STT: t4494(pyrI) t4495(pyrB)
            SPT: SPA4260(pyrI) SPA4261(pyrB)
            SEC: SC4314(pyrI) SC4315(pyrB)
            STM: STM4459(pyrI) STM4460(pyrB)
            YPE: YPO3588(pyrB) YPO3589(pyrI)
            YPK: y0161(pyrB) y0162(pyrI)
            YPM: YP_3842(pyrB) YP_3843(pyrI)
            YPA: YPA_3714 YPA_3715
            YPN: YPN_3470 YPN_3471
            YPP: YPDSF_0309
            YPS: YPTB3531(pyrB) YPTB3532(pyrI)
            YPI: YpsIP31758_0436(pyrB)
            SFL: SF4245(pyrB) SF4246(pyrI)
            SFX: S4507(pyrB) S4508(pyrI)
            SFV: SFV_4247(pyrB) SFV_4248(pyrI)
            SSN: SSON_4425(pyrI) SSON_4426(pyrB)
            SBO: SBO_4201(pyrB) SBO_4202(pyrI)
            SDY: SDY_4263(pyrI) SDY_4264(pyrB)
            ECA: ECA0381(pyrI) ECA0382(pyrB)
            PLU: plu4492(pyrB) plu4497(pyrI)
            BUC: BU369(pyrB) BU370(pyrI)
            BAS: BUsg357(pyrB) BUsg358(pyrI)
            WBR: WGLp461(pyrB) WGLp590(pyrI)
            SGL: SG2115 SG2116
            ENT: Ent638_0447
            SPE: Spro_0545
            XFA: XF2226
            XFT: PD1274(pyrB)
            XCC: XCC2746(pyrB)
            XCB: XC_1367
            XCV: XCV3061(pyrB)
            XAC: XAC2916(pyrB)
            XOO: XOO1427(pyrB)
            XOM: XOO_1311(XOO1311)
            VCH: VC2510 VC2511
            VCO: VC0395_A2092(pyrB)
            VVU: VV1_1464 VV1_1465
            VVY: VV2920 VV2921
            VPA: VP2654 VP2655
            VFI: VF0405 VF0406
            PPR: PBPRA0473(pyrI) PBPRA0474(pyrB)
            PAE: PA0402(pyrB)
            PAU: PA14_05260(pyrB)
            PAP: PSPA7_0502(pyrB)
            PPU: PP_4998(pyrB)
            PST: PSPTO_5040(pyrB)
            PSB: Psyr_0482
            PSP: PSPPH_0473(pyrB)
            PFL: PFL_5833(pyrB)
            PFO: Pfl_5314
            PEN: PSEEN5061(pyrB)
            PMY: Pmen_0397
            PAR: Psyc_0542(pyrB)
            PCR: Pcryo_0531
            PRW: PsycPRwf_1856
            ACI: ACIAD1270(pyrB)
            SON: SO_1301(pyrB)
            SDN: Sden_2818
            SFR: Sfri_2979
            SAZ: Sama_0840
            SBL: Sbal_1160
            SBM: Shew185_1205
            SLO: Shew_1013
            SPC: Sputcn32_1120
            SSE: Ssed_1089
            SPL: Spea_0975
            SHE: Shewmr4_2892
            SHM: Shewmr7_2974
            SHN: Shewana3_3070
            SHW: Sputw3181_3044
            ILO: IL1527 IL2244(pyrB)
            CPS: CPS_4628(pyrB)
            PHA: PSHAa2254(pyrB)
            PAT: Patl_0496
            SDE: Sde_2385
            PIN: Ping_3294
            MAQ: Maqu_3761
            CBU: CBU_2095(pyrB)
            CBD: COXBU7E912_2195(pyrB)
            LPN: lpg0588(pyrB)
            LPF: lpl0622(pyrB)
            LPP: lpp0638(pyrB)
            MCA: MCA2333(pyrB)
            FTU: FTT1665(pyrB)
            FTF: FTF1665(pyrB)
            FTW: FTW_1954(pyrB)
            FTL: FTL_0028
            FTH: FTH_0027(pyrB)
            FTA: FTA_0035(pyrB)
            FTN: FTN_0019(pyrB)
            TCX: Tcr_1829
            NOC: Noc_0365(pyrB) Noc_0778
            AEH: Mlg_0346
            HCH: HCH_00553(pyrB)
            CSA: Csal_0063
            ABO: ABO_0035(pyrB)
            MMW: Mmwyl1_0542
            AHA: AHA_4087(pyrB) AHA_4088(pyrI)
            DNO: DNO_0490(pyrB)
            BCI: BCI_0258(pyrB) BCI_0259(pyrI)
            VOK: COSY_0049(pyrB)
            NME: NMB0106 NMB0107
            NMA: NMA0167(pyrI) NMA0168(pyrB)
            NMC: NMC0098(pyrB)
            NGO: NGO1876(pyrI) NGO1877(pyrB)
            CVI: CV_0369(pyrB) CV_0370(pyrI)
            RSO: RSc0678(pyrB)
            REU: Reut_A0708
            REH: H16_A2913(pyrB)
            RME: Rmet_2740
            BMA: BMA1994(pyrB)
            BMV: BMASAVP1_A0919(pyrB)
            BML: BMA10299_A2749(pyrB)
            BMN: BMA10247_1856(pyrB)
            BXE: Bxe_A3808 Bxe_B2108
            BVI: Bcep1808_5307
            BUR: Bcep18194_A3965 Bcep18194_B0897
            BCN: Bcen_3560
            BCH: Bcen2424_0867 Bcen2424_4807
            BAM: Bamb_0740 Bamb_4187
            BPS: BPSL2690(pyrB) BPSS1203(pyrB)
            BPM: BURPS1710b_3167(pyrB) BURPS1710b_A0197(pyrB)
            BPL: BURPS1106A_3145(pyrB) BURPS1106A_A1605(pyrB)
            BPD: BURPS668_3109(pyrB) BURPS668_A1687(pyrB)
            BTE: BTH_I1465(pyrB-1) BTH_II1204(pyrB-2)
            BPE: BP0321(pyrB) BP2562(pyrB)
            BPA: BPP2617(pyrB) BPP3930(pyrB)
            BBR: BB2060(pyrB) BB4403(pyrB)
            RFR: Rfer_1380
            POL: Bpro_1145
            MPT: Mpe_A0708
            HAR: HEAR2737(pyrB)
            MMS: mma_2947
            NEU: NE1665(pyrB)
            NET: Neut_0451
            NMU: Nmul_A2481
            EBA: ebA1759(pyrB)
            AZO: azo3462(pyrB)
            DAR: Daro_3890
            TBD: Tbd_2582
            MFA: Mfla_2102
            HPY: HP1084(pyrB)
            HPJ: jhp0341(pyrB)
            HPA: HPAG1_0363
            HHE: HH0521(pyrB)
            HAC: Hac_0799(pyrB)
            WSU: WS0580(pyrB)
            TDN: Tmden_0461
            CJE: Cj1098(pyrB)
            CJR: CJE1241(pyrB)
            CJJ: CJJ81176_1116(pyrB)
            CJU: C8J_1039(pyrB)
            CJD: JJD26997_0624(pyrB)
            CFF: CFF8240_1475(pyrB)
            CCV: CCV52592_0155(pyrB)
            CHA: CHAB381_0964(pyrB)
            CCO: CCC13826_0309 CCC13826_2039(pyrB)
            ABU: Abu_0261(pyrB)
            NIS: NIS_0376(pyrB)
            SUN: SUN_2068(pyrB)
            GSU: GSU1271(pyrB)
            GME: Gmet_1769
            GUR: Gura_1856
            PCA: Pcar_1615
            DVU: DVU2901(pyrB)
            DDE: Dde_2964
            LIP: LI0818(pyrB)
            BBA: Bd0855(pyrB)
            DPS: DP0106
            ADE: Adeh_1618
            AFW: Anae109_2193
            MXA: MXAN_3510(pyrB)
            SAT: SYN_01532
            SFU: Sfum_2090
            WOL: WD0895(pyrB)
            WBM: Wbm0385
            AMA: AM662(pyrB)
            APH: APH_0503(pyrB)
            ERU: Erum4250(pyrB)
            ERW: ERWE_CDS_04420(pyrB)
            ERG: ERGA_CDS_04370(pyrB)
            ECN: Ecaj_0418
            ECH: ECH_0621(pyrB)
            NSE: NSE_0510(pyrB)
            PUB: SAR11_1080(pyrB)
            MLO: mlr0686
            MES: Meso_1359
            SME: SMc01360(pyrB)
            ATU: Atu1308(pyrB)
            ATC: AGR_C_2407(pyrB)
            RET: RHE_CH01642(pyrB)
            RLE: RL1739(pyrB)
            BME: BMEII0670
            BMF: BAB2_0641(pyrB)
            BMS: BRA0599(pyrB)
            BMB: BruAb2_0625(pyrB)
            BOV: BOV_A0564(pyrB)
            OAN: Oant_3666
            BJA: blr5099(pyrB)
            BRA: BRADO4502(pyrB)
            BBT: BBta_4725(pyrB)
            RPA: RPA3117(pyrB)
            RPB: RPB_2424
            RPC: RPC_2247
            RPD: RPD_3028
            RPE: RPE_3373
            NWI: Nwi_2007(pyrB)
            NHA: Nham_2282
            BHE: BH08200(pyrB)
            BQU: BQ06380(pyrB)
            BBK: BARBAKC583_0839(pyrB)
            XAU: Xaut_3919
            CCR: CC_2443
            SIL: SPO0287(pyrB)
            SIT: TM1040_3070
            RSP: RSP_1002(pyrB)
            JAN: Jann_3902
            RDE: RD1_3427(pyrB)
            MMR: Mmar10_1713
            HNE: HNE_2302(pyrB)
            ZMO: ZMO0791(pyrB)
            NAR: Saro_3061
            SAL: Sala_0924
            ELI: ELI_01030
            GOX: GOX1267
            GBE: GbCGDNIH1_0809
            ACR: Acry_0733
            RRU: Rru_A3190
            MAG: amb3615
            MGM: Mmc1_0103
            ABA: Acid345_4569
            SUS: Acid_5512
            BSU: BG10713(pyrB)
            BHA: BH2539(pyrB)
            BAN: BA4028(pyrB)
            BAR: GBAA4028(pyrB)
            BAA: BA_4499
            BAT: BAS3740
            BCE: BC3889
            BCA: BCE_3934(pyrB)
            BCZ: BCZK3648(pyrB)
            BTK: BT9727_3631(pyrB)
            BLI: BL02273(pyrB)
            BLD: BLi01769(pyrB)
            BCL: ABC2336(pyrB)
            BAY: RBAM_015320
            BPU: BPUM_1448
            OIH: OB1488(pyrB)
            GKA: GK1149(pyrB)
            SAU: SA1043(pyrB)
            SAV: SAV1200(pyrB)
            SAM: MW1083(pyrB)
            SAR: SAR1176(pyrB)
            SAS: SAS1134
            SAC: SACOL1212(pyrB)
            SAB: SAB1064(pyrB)
            SAA: SAUSA300_1093(pyrB)
            SAO: SAOUHSC_01166
            SEP: SE0876
            SER: SERP0766(pyrB)
            SHA: SH1714(pyrB)
            SSP: SSP1572
            LMO: lmo1838(pyrB)
            LMF: LMOf2365_1866(pyrB)
            LIN: lin1952(pyrB)
            LWE: lwe1857(pyrB)
            LLA: L45002(pyrB)
            LLC: LACR_1710
            LLM: llmg_0893(pyrB)
            SPY: SPy_0832(pyrB)
            SPZ: M5005_Spy_0641(pyrB)
            SPM: spyM18_0892(pyrB)
            SPG: SpyM3_0560(pyrB)
            SPS: SPs1294
            SPH: MGAS10270_Spy0699(pyrB)
            SPI: MGAS10750_Spy0730(pyrB)
            SPJ: MGAS2096_Spy0708(pyrB)
            SPK: MGAS9429_Spy0696(pyrB)
            SPF: SpyM51166(pyrB)
            SPA: M6_Spy0659
            SPB: M28_Spy0621(pyrB)
            SPN: SP_1277
            SPR: spr1155(pyrB)
            SPD: SPD_1133(pyrB)
            SAG: SAG1044(pyrB)
            SAN: gbs1079
            SAK: SAK_1134(pyrB)
            SMU: SMU.858(pyrB)
            STC: str0525(pyrB)
            STL: stu0525(pyrB)
            SSA: SSA_1343(pyrB)
            SGO: SGO_1109(pyrB)
            LPL: lp_2703(pyrB)
            LJO: LJ1279
            LAC: LBA1382(pyrB)
            LSA: LSA0952(pyrB)
            LSL: LSL_0190(pyrB)
            LDB: Ldb2112(pyrB1)
            LBU: LBUL_1953
            LCA: LSEI_1455
            EFA: EF1719(pyrB)
            OOE: OEOE_0258
            STH: STH1257
            CAC: CAC2653(pyrI) CAC2654
            CPE: CPE1183(pyrB)
            CPF: CPF_1387(pyrB)
            CPR: CPR_1201(pyrB)
            CTC: CTC02383 CTC02384
            CNO: NT01CX_0395(pyrB)
            CTH: Cthe_0953
            CDF: CD0184(pyrB)
            CBO: CBO3241(pyrB)
            CBA: CLB_3278(pyrB)
            CBH: CLC_3152(pyrB)
            CBF: CLI_3380(pyrB)
            CBE: Cbei_1000
            CKL: CKL_3361(pyrB)
            AMT: Amet_4200
            CHY: CHY_1502(pyrB)
            DSY: DSY2862
            DRM: Dred_1681
            SWO: Swol_1284
            CSC: Csac_1931
            TTE: TTE1534(pyrB)
            MTA: Moth_0879
            MPE: MYPE7890(pyrB)
            MTU: Rv1380(pyrB)
            MTC: MT1424(pyrB)
            MBO: Mb1415(pyrB)
            MBB: BCG_1441(pyrB)
            MLE: ML0532(pyrB)
            MPA: MAP1115(pyrB)
            MAV: MAV_3393(pyrB)
            MSM: MSMEG_3043(pyrB)
            MMC: Mmcs_2363
            CGL: NCgl1550(pyrB)
            CGB: cg1816(pyrB)
            CEF: CE1732
            CDI: DIP1334(pyrB)
            CJK: jk1025(pyrB)
            NFA: nfa36230(pyrB)
            RHA: RHA1_ro07148(pyrB)
            SCO: SCO1487(pyrB)
            SMA: SAV6863(pyrB)
            TWH: TWT196(pyrB)
            TWS: TW576(pyrB)
            LXX: Lxx11060(pyrB)
            CMI: CMM_1786(pyrB)
            AAU: AAur_2269(pyrB)
            PAC: PPA0997
            NCA: Noca_1631
            TFU: Tfu_1054
            FRA: Francci3_3202
            FAL: FRAAL5238(pyrB)
            SEN: SACE_2079(pyrB)
            STP: Strop_1853
            BLO: BL0793(pyrI) BL0794(pyrB)
            BAD: BAD_0759(pyrB) BAD_0760(pyrI)
            RXY: Rxyl_1480
            FNU: FN0419
            RBA: RB13301(pyrB) RB7429(pyrB)
            TDE: TDE0129(pyrBI)
            LIL: LA0778(pyrB)
            LIC: LIC12839(pyrB)
            LBJ: LBJ_0731(pyrB)
            LBL: LBL_2345(pyrB)
            SYN: slr1476(pyrB)
            SYW: SYNW0296(pyrB) SYNW2454(pyrB)
            SYC: syc0859_c(pyrB)
            SYF: Synpcc7942_0670
            SYD: Syncc9605_0292(pyrB) Syncc9605_2634
            SYE: Syncc9902_2051(pyrB) Syncc9902_2261
            SYG: sync_0343(pyrB)
            SYR: SynRCC307_1125(pyrB) SynRCC307_2204(pyrB)
            SYX: SynWH7803_0344(pyrB)
            CYA: CYA_1730(pyrB)
            CYB: CYB_1917(pyrB)
            TEL: tll1558(pyrB)
            GVI: gll2875(pyrB)
            ANA: all1681
            AVA: Ava_1174(pyrB)
            PMA: Pro0262(pyrB)
            PMM: PMM0233(pyrB)
            PMT: PMT1807(pyrB)
            PMN: PMN2A_1600
            PMB: A9601_02541(pyrB)
            PMC: P9515_02651(pyrB)
            PMF: P9303_23931(pyrB)
            PMG: P9301_02551(pyrB)
            PMH: P9215_02551
            PME: NATL1_03121(pyrB)
            TER: Tery_4368
            BTH: BT_0741 BT_0742
            BFR: BF2207 BF2208
            BFS: BF2261(pyrI) BF2262(pyrB)
            PGI: PG0357(pyrB) PG0358(pyrI)
            SRU: SRU_1334(pyrB)
            CHU: CHU_0084(pyrB)
            GFO: GFO_1843(pyrB)
            FPS: FP1795(pyrB)
            CTE: CT1800(pyrB)
            CCH: Cag_1334
            PVI: Cvib_0548
            PLT: Plut_0492
            DET: DET1199(pyrB)
            DEH: cbdb_A1113(pyrB)
            DEB: DehaBAV1_1009
            RRS: RoseRS_2863
            RCA: Rcas_2434
            DRA: DR_1109
            DGE: Dgeo_0503
            TTH: TTC0427
            TTJ: TTHA0782
            AAE: aq_409(pyrB)
            TMA: TM1642
            MJA: MJ1406(pyrI) MJ1581(pyrB)
            MMP: MMP1104(pyrI) MMP1659(pyrB)
            MMQ: MmarC5_1750
            MMZ: MmarC7_0931
            MAE: Maeo_1339
            MVN: Mevan_0959
            MAC: MA4501(pyrI) MA4502(pyrB)
            MBA: Mbar_A1167 Mbar_A1168
            MMA: MM_1212 MM_1213
            MBU: Mbur_0065 Mbur_0066
            MTP: Mthe_1256
            MHU: Mhun_0618 Mhun_0619
            MEM: Memar_1689
            MTH: MTH1413 MTH850
            MST: Msp_0003(pyrB) Msp_0521(pyrI)
            MSI: Msm_0862 Msm_1263
            MKA: MK1480(pyrB) MK1481(pyrI)
            AFU: AF0106(pyrB) AF0107(pyrI)
            HAL: VNG6309G(pyrB) VNG6311G(pyrI)
            HMA: rrnAC1224(pyrI) rrnAC1225(pyrB)
            HWA: HQ1878A(pyrI) HQ1879A(pyrB)
            NPH: NP3518A(pyrB) NP3520A(pyrI)
            TAC: Ta0574 Ta0575
            TVO: TVN0631 TVN0632
            PTO: PTO0965 PTO0966
            PHO: PH0720 PH0721
            PAB: PAB1498(pyrB) PAB1499(pyrI)
            PFU: PF0598 PF0599
            TKO: TK2195 TK2196
            RCI: RCIX1029(pyrB)
            APE: APE_1662.1 APE_1663.1
            IHO: Igni_0044
            HBU: Hbut_0110
            SSO: SSO0613(pyrI) SSO0614(pyrB)
            STO: ST1479 ST1480
            SAI: Saci_1595(pyrI) Saci_1596(pyrB)
            PAI: PAE0770(pyrB) PAE3265(pyrI)
            PIS: Pisl_1066
            PCL: Pcal_2154
            PAS: Pars_0028
STRUCTURES  PDB: 1ACM  1AT1  1D09  1EKX  1EZZ  1F1B  1GQ3  1I5O  1ML4  1NBE  
                 1PG5  1Q95  1R0B  1R0C  1RAA  1RAB  1RAC  1RAD  1RAE  1RAF  
                 1RAG  1RAH  1RAI  1SKU  1TTH  1TU0  1TUG  1XJW  1ZA1  1ZA2  
                 2A0F  2AIR  2AT1  2AT2  2ATC  2BE7  2BE9  2FZC  2FZG  2FZK  
                 2H3E  2HSE  2IPO  3AT1  3CSU  4AT1  5AT1  6AT1  7AT1  8AT1  
                 8ATC  9ATC  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.3.2
            ExPASy - ENZYME nomenclature database: 2.1.3.2
            ExplorEnz - The Enzyme Database: 2.1.3.2
            ERGO genome analysis and discovery system: 2.1.3.2
            BRENDA, the Enzyme Database: 2.1.3.2
            CAS: 9012-49-1
///
ENTRY       EC 2.1.3.3                  Enzyme
NAME        ornithine carbamoyltransferase;
            citrulline phosphorylase;
            ornithine transcarbamylase;
            OTC;
            carbamylphosphate-ornithine transcarbamylase;
            L-ornithine carbamoyltransferase;
            L-ornithine carbamyltransferase;
            L-ornithine transcarbamylase;
            ornithine carbamyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Carboxy- and carbamoyltransferases
SYSNAME     carbamoyl-phosphate:L-ornithine carbamoyltransferase
REACTION    carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
            [RN:R01398]
ALL_REAC    R01398
SUBSTRATE   carbamoyl phosphate [CPD:C00169];
            L-ornithine [CPD:C00077]
PRODUCT     phosphate [CPD:C00009];
            L-citrulline [CPD:C00327]
COMMENT     The plant enzyme also catalyses the reactions of EC 2.1.3.6
            putrescine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC
            3.5.3.12 agmatine deiminase, thus acting as putrescine synthase,
            converting agmatine [(4-aminobutyl)guanidine] and ornithine into
            putrescine and citrulline, respectively.
REFERENCE   1  [PMID:6034676]
  AUTHORS   Bishop SH, Grisolia S.
  TITLE     Crystalline ornithine transcarbamylase.
  JOURNAL   Biochim. Biophys. Acta. 139 (1967) 344-8.
  ORGANISM  Streptococcus sp.
REFERENCE   2  [PMID:4622303]
  AUTHORS   Marshall M, Cohen PP.
  TITLE     Ornithine transcarbamylase from Streptococcus faecalis and bovine
            liver. I. Isolation and subunit structure.
  JOURNAL   J. Biol. Chem. 247 (1972) 1641-53.
  ORGANISM  Streptococcus faecalis, cow [GN:bta]
REFERENCE   3  [PMID:4622304]
  AUTHORS   Marshall M, Cohen PP.
  TITLE     Ornithine transcarbamylase from Streptococcus faecalis and bovine
            liver. II. Multiple binding sites for carbamyl-P and L-norvaline,
            correlation with steady state kinetics.
  JOURNAL   J. Biol. Chem. 247 (1972) 1654-68.
  ORGANISM  Streptococcus faecalis, cow [GN:bta]
REFERENCE   4  [PMID:4622305]
  AUTHORS   Marshall M, Cohen PP.
  TITLE     Ornithine transcarbamylase from Streptococcus faecalis and bovine
            liver. 3. Effects of chemical modifications of specific residues on
            ligand binding and enzymatic activity.
  JOURNAL   J. Biol. Chem. 247 (1972) 1669-82.
  ORGANISM  Streptococcus faecalis, cow [GN:bta]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K00611  ornithine carbamoyltransferase
GENES       HSA: 5009(OTC)
            MMU: 18416(Otc)
            RNO: 25611(Otc)
            CFA: 480878(OTC)
            BTA: 280887(OTC)
            GGA: 395735(OTC)
            XTR: 448273(otc)
            SPU: 588878(LOC588878)
            ATH: AT1G75330(OTC)
            OSA: 4330456
            CME: CML214C
            SCE: YJL088W(ARG3)
            AGO: AGOS_AFR098W
            PIC: PICST_35868(ARG3)
            CGR: CAGL0I10791g
            SPO: SPAC4G9.10(arg3)
            ANI: AN4409.2
            AFM: AFUA_4G07190
            AOR: AO090023000856
            ANG: An14g03400(argB)
            CNE: CNC04300
            UMA: UM03537.1
            ECO: b0273(argF) b4254(argI)
            ECJ: JW0266(argF) JW4211(argI)
            ECE: Z5866(argI)
            ECS: ECs5231
            ECC: c5348 c5353(argI)
            ECI: UTI89_C4855(argF) UTI89_C4860(argI)
            ECP: ECP_4498
            ECV: APECO1_2140(argI) APECO1_2144(argF)
            ECW: EcE24377A_4825(argF)
            ECX: EcHS_A4510
            STY: STY4803 STY4807
            STT: t4499 t4503
            SPT: SPA4265 SPA4269(argI)
            SEC: SC4319(otcC) SC4324(argI)
            STM: STM4465 STM4469(argI)
            YPE: YPO3446(argI)
            YPK: y0740(argI)
            YPM: YP_0638(argI)
            YPA: YPA_2947 YPA_2948
            YPN: YPN_0642
            YPS: YPTB0526(argI)
            YPI: YpsIP31758_3549(argF)
            YEN: YE0494(argI)
            SFL: SF4235(argI)
            SFX: S4496(argI)
            SFV: SFV_4239(argI)
            SSN: SSON_4436(argI)
            SBO: SBO_4188(argI)
            SDY: SDY_4276(argI)
            ECA: ECA0384(argI)
            PLU: plu4490(argI)
            BUC: BU368(argF)
            BAS: BUsg356(argF)
            BAB: bbp333(argF)
            BCC: BCc_224(argF)
            SGL: SG2113
            ENT: Ent638_0459
            SPE: Spro_1648
            BFL: Bfl032(argI)
            BPN: BPEN_032(argI)
            HIN: HI0596(arcB)
            HIT: NTHI0733(argF)
            HIQ: CGSHiGG_06290 CGSHiGG_06325
            HDU: HD0232(arcB1)
            PMU: PM0808(arg)
            MSU: MS1073(argF)
            APL: APL_1317(arcB)
            ASU: Asuc_1744
            XFA: XF0998
            XFT: PD0290(argF)
            XCC: XCC2249(argF)
            XCB: XC_1869
            XCV: XCV2551(argF)
            XAC: XAC2352(argF)
            XOO: XOO2676(argF)
            XOM: XOO_2522(XOO2522)
            VCH: VC2508
            VCO: VC0395_A2091(argF)
            VVU: VV1_1466
            VVY: VV2919
            VPA: VP2653
            VFI: VF0407
            PPR: PBPRA0475(arcB) PBPRB1921 PBPRB1924(arcB)
            PAE: PA3537(argF) PA5172(arcB)
            PAU: PA14_18610(argF) PA14_68340(arcB)
            PAP: PSPA7_1609(argF2) PSPA7_5912(argF1)
            PPU: PP_1000(argI) PP_1079(argF)
            PPF: Pput_5084
            PST: PSPTO_4164(argF)
            PSB: Psyr_2685 Psyr_3901
            PSP: PSPPH_3895(argF) PSPPH_4319(argK)
            PFL: PFL_4636(argF) PFL_4863(argF)
            PFO: Pfl_4387 Pfl_4527
            PEN: PSEEN1201(argI) PSEEN4429(argF)
            PMY: Pmen_0349
            PAR: Psyc_0957(argF)
            PCR: Pcryo_1461
            PRW: PsycPRwf_1063
            ACI: ACIAD1366(argF)
            ACB: A1S_1980
            SON: SO_0277(argF)
            SDN: Sden_0252
            SFR: Sfri_0193
            SAZ: Sama_0258
            SBL: Sbal_4122
            SBM: Shew185_1169
            SLO: Shew_0204
            SPC: Sputcn32_3715
            SSE: Ssed_1064
            SPL: Spea_0949
            SHE: Shewmr4_3707
            SHM: Shewmr7_0238
            SHN: Shewana3_3903
            SHW: Sputw3181_3858
            ILO: IL0614(argF)
            CPS: CPS_0462(argF)
            PHA: PSHAa2289(argF)
            PAT: Patl_0980
            SDE: Sde_2441
            MAQ: Maqu_2317
            LPN: lpg0496(argF)
            LPF: lpl0534(argF)
            LPP: lpp0558(argF)
            MCA: MCA2080(atpD-2)
            TCX: Tcr_0532
            NOC: Noc_2430
            AEH: Mlg_1101
            HHA: Hhal_0726
            HCH: HCH_01762(argF1) HCH_05489(argF2)
            CSA: Csal_2130
            ABO: ABO_0718(argF)
            MMW: Mmwyl1_3520
            AHA: AHA_0595(argF-1) AHA_2161 AHA_4091(argF-2)
            DNO: DNO_1074(argF-1) DNO_1335(argF-2)
            CRP: CRP_011
            RMA: Rmag_0452
            VOK: COSY_0418(argF)
            NME: NMB1573
            NMA: NMA1762(argF)
            NMC: NMC1493(argF)
            NGO: NGO1232
            CVI: CV_1993(argI) CV_3781(arcB)
            RSO: RSc2554(argF)
            REU: Reut_A2763
            REH: H16_A3063(argF)
            RME: Rmet_2902
            BMA: BMA0375(argF) BMA1146(arcB)
            BMV: BMASAVP1_A0675(argF) BMASAVP1_A1586(arcB)
            BML: BMA10299_A0245(arcB) BMA10299_A2510(argF)
            BMN: BMA10247_0124(argF) BMA10247_0914(arcB)
            BXE: Bxe_A0757 Bxe_A1876 Bxe_C0747
            BVI: Bcep1808_2646
            BUR: Bcep18194_A5885
            BCN: Bcen_1942
            BCH: Bcen2424_2553
            BAM: Bamb_2601
            BPS: BPSL0869(argF) BPSL1744(arcB)
            BPM: BURPS1710b_1073(argF) BURPS1710b_2127(argF)
            BPL: BURPS1106A_0921(argF) BURPS1106A_1986(arcB)
            BPD: BURPS668_0917(argF) BURPS668_1967(arcB)
            BTE: BTH_I0732(argF-1) BTH_I2385(argF-2)
            PNU: Pnuc_1754
            BPE: BP3538(argF)
            BPA: BPP2542(argF)
            BBR: BB1987(argF)
            RFR: Rfer_2120
            POL: Bpro_3573
            PNA: Pnap_3012
            AAV: Aave_1163
            AJS: Ajs_3003
            VEI: Veis_1902
            MPT: Mpe_A3030
            HAR: HEAR0872(argF)
            MMS: mma_0848
            NEU: NE1438(argF)
            NET: Neut_2066
            NMU: Nmul_A1042
            EBA: ebA5096(argF)
            AZO: azo2187(argF)
            DAR: Daro_3032
            TBD: Tbd_1850
            MFA: Mfla_1709
            HHE: HH0977(argF)
            WSU: WS1753(argF)
            TDN: Tmden_0386
            CJE: Cj0994c(argF)
            CJR: CJE1074(argF)
            CJJ: CJJ81176_1012(argF)
            CJU: C8J_0931(argF)
            CJD: JJD26997_0795(argF)
            CFF: CFF8240_1573(argF)
            CCV: CCV52592_0157(argF)
            CHA: CHAB381_1697(argF)
            CCO: CCC13826_0885(argF) CCC13826_1033
            ABU: Abu_1244(argF)
            NIS: NIS_0361
            SUN: SUN_2090(argF)
            GSU: GSU0152(argF)
            GME: Gmet_0205
            PCA: Pcar_2415
            PPD: Ppro_3172
            DVU: DVU1096(argF)
            DVL: Dvul_1899
            DDE: Dde_2532
            LIP: LI1113(argF)
            DPS: DP0437
            ADE: Adeh_2691
            MXA: MXAN_5104(argF)
            SAT: SYN_02156
            SFU: Sfum_0062
            AMA: AM1217(argF)
            ERU: Erum0510(argF)
            ERW: ERWE_CDS_00410(argF)
            ERG: ERGA_CDS_00400(argF)
            ECN: Ecaj_0046
            ECH: ECH_0077(argF)
            PUB: SAR11_0503(argF)
            MLO: mlr5647
            MES: Meso_0008 Meso_2240
            PLA: Plav_1549
            SME: SMa0695(arcB) SMc02137(argF1)
            SMD: Smed_0313
            ATU: Atu0429(argF)
            ATC: AGR_C_755
            RET: RHE_CH00517(argF)
            RLE: RL0550(argF) RL4105(argF)
            BME: BMEI1620
            BMF: BAB1_0332
            BMS: BR0302(argF)
            BMB: BruAb1_0328(argF)
            BOV: BOV_0315(argF)
            OAN: Oant_0395 Oant_2805 Oant_3925
            BJA: blr1099(argF)
            BRA: BRADO6778(argF)
            BBT: BBta_0760(argF)
            RPA: RPA4772(argF)
            RPB: RPB_0784
            RPC: RPC_4915
            RPD: RPD_0896
            RPE: RPE_4883
            NWI: Nwi_0514
            NHA: Nham_0643
            BBK: BARBAKC583_1291(argF)
            XAU: Xaut_2943
            CCR: CC_2242
            SIL: SPO0963(argF)
            SIT: TM1040_0666
            RSP: RSP_2009(argF)
            RSH: Rsph17029_0719
            RSQ: Rsph17025_3106
            JAN: Jann_1023
            RDE: RD1_1677(argF)
            PDE: Pden_2039
            MMR: Mmar10_0364
            HNE: HNE_0592(argF)
            ZMO: ZMO0409(argF)
            NAR: Saro_3140
            SAL: Sala_1358
            ELI: ELI_13920
            GOX: GOX1236
            GBE: GbCGDNIH1_2273
            RRU: Rru_A3276
            MAG: amb0317
            MGM: Mmc1_3743
            ABA: Acid345_1819 Acid345_4159
            SUS: Acid_2505
            BSU: BG10197(argF)
            BHA: BH2894(argF)
            BAN: BA4351(argF)
            BAR: GBAA4351(argF)
            BAA: BA_4808
            BAT: BAS4036
            BCE: BC0407 BC4126
            BCA: BCE_0473(argF) BCE_4199(argF)
            BCZ: BCZK3883(argF)
            BCY: Bcer98_1009
            BTK: BT9727_0342(arcB) BT9727_3875(argF)
            BTL: BALH_0363(arcB)
            BLI: BL01914 BL03247(argF)
            BLD: BLi01212(argF) BLi04129 BLi04164
            BCL: ABC2552(argF)
            BAY: RBAM_011250
            BPU: BPUM_1048
            OIH: OB0460
            GKA: GK0796
            SAU: SA1012(argF) SA2427(arcB)
            SAV: SAV1169(argF) SAV2634(arcB)
            SAM: MW1050(argF) MW2555(arcB)
            SAR: SAR1142(otc) SAR2713(arcB)
            SAS: SAS1102 SAS2520
            SAC: SACOL1181(arcB1) SACOL2656(arcB2)
            SAB: SAB1033 SAB2509c(arcB)
            SAA: SAUSA300_0062(arcB) SAUSA300_1062(argF) SAUSA300_2569(arcB)
            SAO: SAOUHSC_01128 SAOUHSC_02968
            SEP: SE0103 SE0229 SE2216
            SER: SERP2249(arcB-1) SERP2351(arcB-2)
            SHA: SH0258(argF)
            SSP: SSP0232
            LMO: lmo0036 lmo1587(argF)
            LMF: LMOf2365_0045(argF-1) LMOf2365_1609(argF-2)
            LIN: lin1629(argF)
            LWE: lwe1600(argF)
            LLA: L0108(argF) L0109(arcB) L0113(otcA)
            LLC: LACR_0860 LACR_2321
            LLM: llmg_1754(argF) llmg_2312(arcB)
            SPY: SPy_1544(arcB)
            SPZ: M5005_Spy_1273(arcB)
            SPM: spyM18_1562(arcB)
            SPG: SpyM3_1194(arcB)
            SPS: SPs0668
            SPH: MGAS10270_Spy1288(arcB)
            SPI: MGAS10750_Spy1380(arcB)
            SPJ: MGAS2096_Spy1292(arcB)
            SPK: MGAS9429_Spy1267(arcB)
            SPF: SpyM50579(arcB)
            SPA: M6_Spy1294
            SPB: M28_Spy1211(arcB)
            SPN: SP_2150
            SPR: spr1957(arcB)
            SPD: SPD_1976(argF)
            SAG: SAG2126(argF-1) SAG2165(argF-2)
            SAN: gbs2085 gbs2124
            SAK: SAK_2065(argF) SAK_2123(argF)
            SMU: SMU.262(otcA) SMU.563
            STC: str0603(argF)
            STL: stu0603(argF)
            SSA: SSA_0738(arc)
            SGO: SGO_1592(arcB)
            LPL: lp_0532(argF)
            LSA: LSA0067 LSA0371(arcB)
            LBR: LVIS_2026 LVIS_2210
            LRE: Lreu_1644
            PPE: PEPE_1631
            EFA: EF0105(argF-1) EF0732(argF-2)
            STH: STH3019
            CAC: CAC0316(argF)
            CPE: CPE0169(arcB)
            CPF: CPF_0162(argF)
            CPR: CPR_0158(argF)
            CNO: NT01CX_0745(argF)
            CTH: Cthe_1869
            CDF: CD2030(argF)
            CBO: CBO2593(arcB)
            CBA: CLB_2534(argF)
            CBH: CLC_2465(argF)
            CBF: CLI_2656(argF)
            CBE: Cbei_4938
            CKL: CKL_2376(argF)
            CHY: CHY_2261(argF)
            DSY: DSY0784
            DRM: Dred_0276
            SWO: Swol_2287
            TTE: TTE0532(argF)
            MTA: Moth_1996 Moth_2286
            MPN: MPN306(argI)
            MPE: MYPE6090(arcB)
            MMY: MSC_0703(arcB)
            MCP: MCAP_0090(arcB) MCAP_0654(argF)
            MTU: Rv1656(argF)
            MTC: MT1694(argF)
            MBO: Mb1684(argF)
            MBB: BCG_1695(argF)
            MLE: ML1410(argF)
            MPA: MAP1365(argF)
            MAV: MAV_3114(argF)
            MSM: MSMEG_3772(argF) MSMEG_4750
            MVA: Mvan_1390 Mvan_3310
            MGI: Mflv_3526
            MMC: Mmcs_2968
            MJL: Mjls_2983
            CGL: NCgl0990(cgl1034) NCgl1344(cgl1398)
            CGB: cg1174(arcB) cg1584(argF)
            CEF: CE1530(argF)
            CDI: DIP1171(argF)
            CJK: jk0845(argF)
            NFA: nfa19400(argF)
            RHA: RHA1_ro00952(argF)
            SCO: SCO5976(arcB)
            SMA: SAV2319(argF) SAV3641
            LXX: Lxx06070(argF)
            CMI: CMM_1997(argF)
            AAU: AAur_1635(argF)
            PAC: PPA0584
            NCA: Noca_1632
            TFU: Tfu_1992
            FRA: Francci3_3171
            FAL: FRAAL5204(argF)
            ACE: Acel_1259
            SEN: SACE_4292 SACE_5258(argF)
            BLO: BL1060(argF)
            BAD: BAD_0921(argF)
            RXY: Rxyl_2889
            RBA: RB5986(argF)
            BBU: BB0842
            BGA: BG0869(arcB)
            BAF: BAPKO_0897(arcB)
            TDE: TDE0929(argF)
            LIL: LA2840(argF)
            LIC: LIC11195(argF)
            LBJ: LBJ_2022(argF)
            LBL: LBL_1028(argF)
            SYN: sll0902(argF)
            SYW: SYNW1586(argF)
            SYC: syc1592_c(argF)
            SYF: Synpcc7942_2514
            SYD: Syncc9605_0926
            SYE: Syncc9902_1482
            SYG: sync_0826(argF)
            SYR: SynRCC307_1755(argF)
            SYX: SynWH7803_1688(argF)
            CYA: CYA_2817(argF)
            CYB: CYB_0821(argF)
            TEL: tll1106(argF)
            GVI: gll3101(argF)
            ANA: alr4907
            AVA: Ava_2197
            PMA: Pro1337(argF)
            PMM: PMM1263
            PMT: PMT0379
            PMN: PMN2A_0829
            PMI: PMT9312_1357
            PMB: A9601_14621(argF)
            PMC: P9515_14241(argF)
            PMF: P9303_19151(argF)
            PMG: P9301_14481(argF)
            PMH: P9215_14881
            PME: NATL1_16811(argF)
            TER: Tery_1323
            BTH: BT_3717
            BFR: BF0494
            BFS: BF0439
            SRU: SRU_2218
            CHU: CHU_3085(argF)
            CTE: CT1112(argF)
            CCH: Cag_0775
            CPH: Cpha266_1323
            PVI: Cvib_0880
            PLT: Plut_1046
            DET: DET1394(argF)
            DEH: cbdb_A1353(argF)
            DEB: DehaBAV1_1203
            RRS: RoseRS_1644
            RCA: Rcas_2838
            DRA: DR_0080
            DGE: Dgeo_1605
            TTH: TTC0838
            TTJ: TTHA1199
            AAE: aq_1711(argF)
            TMA: TM1097
            TPT: Tpet_1405
            TME: Tmel_0566
            FNO: Fnod_0372
            MMP: MMP0553(argF)
            MMQ: MmarC5_1054
            MAC: MA3310(argF)
            MBA: Mbar_A3512
            MMA: MM_0145
            MBU: Mbur_1057
            MTP: Mthe_0975
            MHU: Mhun_1113
            MLA: Mlab_0268
            MEM: Memar_0999
            MBN: Mboo_0839
            MST: Msp_0031(argF)
            MSI: Msm_1226
            MKA: MK1070(argF)
            HAL: VNG6315G(arcB)
            HMA: rrnAC2672(arcB)
            HWA: HQ3719A(argF)
            NPH: NP5268A(argF)
            TAC: Ta1330
            TVO: TVN0272
            PTO: PTO0732
            PAB: PAB1502(argF)
            PFU: PF0594
            TKO: TK0871
            RCI: RCIX2167(argF)
            APE: APE_1992.1
            SMR: Smar_0224 Smar_0227 Smar_0278
            HBU: Hbut_1203
            SSO: SSO0871(argF)
            STO: ST1245
            SAI: Saci_1408(argF)
            PAI: PAE1985(argF)
            PIS: Pisl_1807
            PCL: Pcal_1594
            PAS: Pars_2058
            TPE: Tpen_0407
STRUCTURES  PDB: 1A1S  1AKM  1C9Y  1DUV  1DXH  1EP9  1FB5  1FVO  1ORT  1PVV  
                 1VLV  1ZQ2  1ZQ6  1ZQ8  2EF0  2I6U  2OTC  2P2G  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.3.3
            ExPASy - ENZYME nomenclature database: 2.1.3.3
            ExplorEnz - The Enzyme Database: 2.1.3.3
            ERGO genome analysis and discovery system: 2.1.3.3
            BRENDA, the Enzyme Database: 2.1.3.3
            CAS: 9001-69-8
///
ENTRY       EC 2.1.3.4        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring one-carbon groups;
            Carboxy- and carbamoyltransferases
COMMENT     Deleted entry: malonyl-CoA carboxyltransferase. (EC 2.1.3.4 created
            1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.3.4
            ExPASy - ENZYME nomenclature database: 2.1.3.4
            ExplorEnz - The Enzyme Database: 2.1.3.4
            ERGO genome analysis and discovery system: 2.1.3.4
            BRENDA, the Enzyme Database: 2.1.3.4
///
ENTRY       EC 2.1.3.5                  Enzyme
NAME        oxamate carbamoyltransferase;
            oxamic transcarbamylase
CLASS       Transferases;
            Transferring one-carbon groups;
            Carboxy- and carbamoyltransferases
SYSNAME     carbamoyl-phosphate:oxamate carbamoyltransferase
REACTION    carbamoyl phosphate + oxamate = phosphate + oxalureate [RN:R02937]
ALL_REAC    R02937
SUBSTRATE   carbamoyl phosphate [CPD:C00169];
            oxamate [CPD:C01444]
PRODUCT     phosphate [CPD:C00009];
            oxalureate [CPD:C00802]
REFERENCE   1
  AUTHORS   Bojanowski, R., Gaudy, E., Valentine, R.C. and Wolfe, R.S.
  TITLE     Oxamic transcarbamylase of Streptococcus allantoicus.
  JOURNAL   J. Bacteriol. 87 (1964) 75-80.
  ORGANISM  Streptococcus allantoicus
PATHWAY     PATH: map00230  Purine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.3.5
            ExPASy - ENZYME nomenclature database: 2.1.3.5
            ExplorEnz - The Enzyme Database: 2.1.3.5
            ERGO genome analysis and discovery system: 2.1.3.5
            BRENDA, the Enzyme Database: 2.1.3.5
            CAS: 62213-52-9
///
ENTRY       EC 2.1.3.6                  Enzyme
NAME        putrescine carbamoyltransferase;
            PTCase;
            putrescine synthase;
            putrescine transcarbamylase
CLASS       Transferases;
            Transferring one-carbon groups;
            Carboxy- and carbamoyltransferases
SYSNAME     carbamoyl-phosphate:putrescine carbamoyltransferase
REACTION    carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine
            [RN:R01399]
ALL_REAC    R01399
SUBSTRATE   carbamoyl phosphate [CPD:C00169];
            putrescine [CPD:C00134]
PRODUCT     phosphate [CPD:C00009];
            N-carbamoylputrescine [CPD:C00436]
COMMENT     The plant enzyme also catalyses the reactions of EC 2.1.3.3
            ornithine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC
            3.5.3.12 agmatine deiminase, thus acting as putrescine synthase,
            converting agmatine [(4-aminobutyl)guanidine] and ornithine into
            putrescine and citrulline, respectively.
REFERENCE   1  [PMID:4621632]
  AUTHORS   Roon RJ, Barker HA.
  TITLE     Fermentation of agmatine in Streptococcus faecalis: occurrence of
            putrescine transcarbamoylase.
  JOURNAL   J. Bacteriol. 109 (1972) 44-50.
  ORGANISM  Streptococcus faecalis
REFERENCE   2  [PMID:6895223]
  AUTHORS   Srivenugopal KS, Adiga PR.
  TITLE     Enzymic conversion of agmatine to putrescine in Lathyrus sativus
            seedlings. Purification and properties of a multifunctional enzyme
            (putrescine synthase).
  JOURNAL   J. Biol. Chem. 256 (1981) 9532-41.
  ORGANISM  Lathyrus sativus
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.3.6
            ExPASy - ENZYME nomenclature database: 2.1.3.6
            ExplorEnz - The Enzyme Database: 2.1.3.6
            ERGO genome analysis and discovery system: 2.1.3.6
            BRENDA, the Enzyme Database: 2.1.3.6
            CAS: 9076-55-5
///
ENTRY       EC 2.1.3.7                  Enzyme
NAME        3-hydroxymethylcephem carbamoyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Carboxy- and carbamoyltransferases
SYSNAME     carbamoyl-phosphate:3-hydroxymethylceph-3-em-4-carboxylate
            carbamoyltransferase
REACTION    carbamoyl phosphate + a 3-hydroxymethylceph-3-em-4-carboxylate =
            phosphate + a 3-carbamoyloxymethylcephem [RN:R04281]
ALL_REAC    R04281
SUBSTRATE   carbamoyl phosphate [CPD:C00169];
            3-hydroxymethylceph-3-em-4-carboxylate
PRODUCT     phosphate [CPD:C00009];
            3-carbamoyloxymethylcephem [CPD:C03674]
EFFECTOR    ATP [CPD:C00002]
COMMENT     Acts on a wide range of 3-hydroxymethylcephems (a subclass of the
            cephalosporin antibiotics). Activated by ATP.
REFERENCE   1  [PMID:6248024]
  AUTHORS   Brewer SJ, Taylor PM, Turner MK.
  TITLE     An adenosine triphosphate-dependent
            carbamoylphosphate--3-hydroxymethylcephem O-carbamoyltransferase
            from Streptomyces clavuligerus.
  JOURNAL   Biochem. J. 185 (1980) 555-64.
  ORGANISM  Streptomyces clavuligerus
GENES       GFO: GFO_3195
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.3.7
            ExPASy - ENZYME nomenclature database: 2.1.3.7
            ExplorEnz - The Enzyme Database: 2.1.3.7
            ERGO genome analysis and discovery system: 2.1.3.7
            BRENDA, the Enzyme Database: 2.1.3.7
            CAS: 74315-96-1
///
ENTRY       EC 2.1.3.8                  Enzyme
NAME        lysine carbamoyltransferase;
            lysine transcarbamylase
CLASS       Transferases;
            Transferring one-carbon groups;
            Carboxy- and carbamoyltransferases
SYSNAME     carbamoyl-phosphate:L-lysine carbamoyltransferase
REACTION    carbamoyl phosphate + L-lysine = phosphate + L-homocitrulline
            [RN:R01396]
ALL_REAC    R01396
SUBSTRATE   carbamoyl phosphate [CPD:C00169];
            L-lysine [CPD:C00047]
PRODUCT     phosphate [CPD:C00009];
            L-homocitrulline [CPD:C02427]
COMMENT     Not identical with EC 2.1.3.3 ornithine carbamoyltransferase.
REFERENCE   1  [PMID:6409607]
  AUTHORS   Hommes FA, Eller AG, Scott DF, Carter AL.
  TITLE     Separation of ornithine and lysine activities of the
            ornithine-transcarbamylase-catalyzed reaction.
  JOURNAL   Enzyme. 29 (1983) 271-7.
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.3.8
            ExPASy - ENZYME nomenclature database: 2.1.3.8
            ExplorEnz - The Enzyme Database: 2.1.3.8
            ERGO genome analysis and discovery system: 2.1.3.8
            BRENDA, the Enzyme Database: 2.1.3.8
            CAS: 86352-19-4
///
ENTRY       EC 2.1.3.9                  Enzyme
NAME        N-acetylornithine carbamoyltransferase;
            acetylornithine transcarbamylase;
            N-acetylornithine transcarbamylase;
            AOTC;
            carbamoyl-phosphate:2-N-acetyl-L-ornithine carbamoyltransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Carboxy- and carbamoyltransferases
SYSNAME     carbamoyl-phosphate:N2-acetyl-L-ornithine carbamoyltransferase
REACTION    carbamoyl phosphate + N2-acetyl-L-ornithine = phosphate +
            N-acetyl-L-citrulline [RN:R07245]
ALL_REAC    R07245
SUBSTRATE   carbamoyl phosphate [CPD:C00169];
            N2-acetyl-L-ornithine [CPD:C00437]
PRODUCT     phosphate [CPD:C00009];
            N-acetyl-L-citrulline [CPD:C15532]
COMMENT     Differs from EC 2.1.3.3, ornithine carbamoyltransferase. This enzyme
            replaces EC 2.1.3.3 in the canonic arginine biosynthetic pathway of
            several Eubacteria and has no catalytic activity with L-ornithine as
            substrate.
REFERENCE   1  [PMID:15731101]
  AUTHORS   Shi D, Morizono H, Yu X, Roth L, Caldovic L, Allewell NM, Malamy MH,
            Tuchman M.
  TITLE     Crystal structure of N-acetylornithine transcarbamylase from
            Xanthomonas campestris: a novel enzyme in a new arginine
            biosynthetic pathway found in several eubacteria.
  JOURNAL   J. Biol. Chem. 280 (2005) 14366-9.
  ORGANISM  Xanthomonas campestris
GENES       GFO: GFO_2103(argF)
STRUCTURES  PDB: 2G65  2G68  2G6A  2G6C  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.3.9
            ExPASy - ENZYME nomenclature database: 2.1.3.9
            ExplorEnz - The Enzyme Database: 2.1.3.9
            ERGO genome analysis and discovery system: 2.1.3.9
            BRENDA, the Enzyme Database: 2.1.3.9
            CAS: 890853-54-0
///
ENTRY       EC 2.1.3.-                  Enzyme
CLASS       Transferases;
            Transferring one-carbon groups;
            Carboxy- and carbamoyltransferases
REACTION    Deacetylcephalosporin C + Carbamoyl phosphate <=>
            O-Carbamoyl-deacetylcephalosporin C + Orthophosphate [RN:R05230]
SUBSTRATE   Deacetylcephalosporin C [CPD:C03112];
            Carbamoyl phosphate [CPD:C00169]
PRODUCT     O-Carbamoyl-deacetylcephalosporin C [CPD:C06568];
            Orthophosphate [CPD:C00009]
///
ENTRY       EC 2.1.4.1                  Enzyme
NAME        glycine amidinotransferase;
            arginine-glycine amidinotransferase;
            arginine-glycine transamidinase;
            glycine transamidinase
CLASS       Transferases;
            Transferring one-carbon groups;
            Amidinotransferases
SYSNAME     L-arginine:glycine amidinotransferase
REACTION    L-arginine + glycine = L-ornithine + guanidinoacetate [RN:R00565]
ALL_REAC    R00565;
            (other) R01989
SUBSTRATE   L-arginine [CPD:C00062];
            glycine [CPD:C00037]
PRODUCT     L-ornithine [CPD:C00077];
            guanidinoacetate [CPD:C00581]
COMMENT     Canavanine can act instead of arginine.
REFERENCE   1
  AUTHORS   Borsook, H. and Dubnoff, J.W.
  TITLE     The formation of glycocyamine in animal tissues.
  JOURNAL   J. Biol. Chem. 138 (1941) 389-403.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:14304853]
  AUTHORS   CONCONI F, GRAZI E.
  TITLE     TRANSAMIDINASE OF HOG KIDNEY. I. PURIFICATION AND PROPERTIES.
  JOURNAL   J. Biol. Chem. 240 (1965) 2461-4.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:6766137]
  AUTHORS   McGuire DM, Tormanen CD, Segal IS, Van Pilsum JF.
  TITLE     The effect of growth hormone and thyroxine on the amount of
            L-arginine:glycine amidinotransferase in kidneys of
            hypophysectomized rats. Purification and some properties of rat
            kidney transamidinase.
  JOURNAL   J. Biol. Chem. 255 (1980) 1152-9.
  ORGANISM  rat [GN:rno]
REFERENCE   4
  AUTHORS   Ratner, S.
  TITLE     Transamidination.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 6, Academic Press, New York, 1962, p. 267-275.
REFERENCE   5  [PMID:13355454]
  AUTHORS   RATNER S, ROCHOVANSKY O.
  TITLE     Biosynthesis of guanidinoacetic acid.  I.  Purification and
            properties of transamidinase.
  JOURNAL   Arch. Biochem. Biophys. 63 (1956) 277-95.
  ORGANISM  rat [GN:rno]
REFERENCE   6  [PMID:13355455]
  AUTHORS   RATNER S, ROCHOVANSKY O.
  TITLE     Biosynthesis of guanidinoacetic acid.  II.  Mechanism of amidine
            group transfer.
  JOURNAL   Arch. Biochem. Biophys. 63 (1956) 296-315.
  ORGANISM  pig [GN:ssc]
REFERENCE   7  [PMID:13278360]
  AUTHORS   WALKER JB.
  TITLE     Biosynthesis of arginine from canavanine and ornithine in kidney.
  JOURNAL   J. Biol. Chem. 218 (1956) 549-56.
  ORGANISM  pig [GN:ssc]
REFERENCE   8  [PMID:13398387]
  AUTHORS   WALKER JB.
  TITLE     Studies on the mechanism of action of kidney transamidinase.
  JOURNAL   J. Biol. Chem. 224 (1957) 57-66.
  ORGANISM  rat [GN:rno], pig [GN:ssc]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K00613  glycine amidinotransferase
GENES       HSA: 2628(GATM)
            PTR: 453401(GATM)
            MMU: 67092(Gatm)
            RNO: 81660(Gatm)
            CFA: 414733(GATM)
            BTA: 414732(GATM)
            GGA: 395504(GATM)
            XLA: 379386(MGC53198)
            XTR: 394568(MGC75983)
            DRE: 266799(gatm)
            SPU: 581473(LOC581473)
            PLU: plu0158
            PPR: PBPRA0993(AT)
            PST: PSPTO_0873
            PSP: PSPPH_4303
            PUB: SAR11_0688(gatM)
            NWI: Nwi_2321
            JAN: Jann_0016
            RDE: RD1_1472(gatM)
            PAC: PPA0632
            SEN: SACE_4336
            TER: Tery_3130
STRUCTURES  PDB: 1JDW  1JDX  2JDW  2JDX  3JDW  4JDW  5JDW  6JDW  7JDW  8JDW  
                 9JDW  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.4.1
            ExPASy - ENZYME nomenclature database: 2.1.4.1
            ExplorEnz - The Enzyme Database: 2.1.4.1
            ERGO genome analysis and discovery system: 2.1.4.1
            BRENDA, the Enzyme Database: 2.1.4.1
            CAS: 9027-35-4
///
ENTRY       EC 2.1.4.2                  Enzyme
NAME        scyllo-inosamine-4-phosphate amidinotransferase;
            L-arginine:inosamine-P-amidinotransferase;
            inosamine-P amidinotransferase;
            L-arginine:inosamine phosphate amidinotransferase;
            inosamine-phosphate amidinotransferase
CLASS       Transferases;
            Transferring one-carbon groups;
            Amidinotransferases
SYSNAME     L-arginine:1-amino-1-deoxy-scyllo-inositol-4-phosphate
            amidinotransferase
REACTION    L-arginine + 1-amino-1-deoxy-scyllo-inositol 4-phosphate =
            L-ornithine + 1-guanidino-1-deoxy-scyllo-inositol 4-phosphate
            [RN:R03477]
ALL_REAC    R03477
SUBSTRATE   L-arginine [CPD:C00062];
            1-amino-1-deoxy-scyllo-inositol 4-phosphate [CPD:C01283]
PRODUCT     L-ornithine [CPD:C00077];
            1-guanidino-1-deoxy-scyllo-inositol 4-phosphate [CPD:C01294]
COMMENT     1D-1-Guanidino-3-amino-1,3-dideoxy-scyllo-inositol 6-phosphate,
            streptamine phosphate and 2-deoxystreptamine phosphate can also act
            as acceptors; canavanine can act as donor.
REFERENCE   1
  AUTHORS   Walker, M.S. and Walker, J.B.
  TITLE     Enzymic studies on the biosynthesis of streptomycin, transamidation
            of inosamine and streptamine derivatives.
  JOURNAL   J. Biol. Chem. 241 (1966) 1262-1269.
  ORGANISM  Streptomyces griseus, Streptomyces bikiniensis
PATHWAY     PATH: map00521  Streptomycin biosynthesis
ORTHOLOGY   KO: K04340  scyllo-inosamine-4-phosphate amidinotransferase
GENES       STP: Strop_1716
STRUCTURES  PDB: 1BWD  
DBLINKS     IUBMB Enzyme Nomenclature: 2.1.4.2
            ExPASy - ENZYME nomenclature database: 2.1.4.2
            ExplorEnz - The Enzyme Database: 2.1.4.2
            ERGO genome analysis and discovery system: 2.1.4.2
            BRENDA, the Enzyme Database: 2.1.4.2
            CAS: 52227-63-1
///
ENTRY       EC 2.2.1.1                  Enzyme
NAME        transketolase;
            glycolaldehydetransferase
CLASS       Transferases;
            Transferring aldehyde or ketonic groups;
            Transketolases and transaldolases
SYSNAME     sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate
            glycolaldehydetransferase
REACTION    sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose
            5-phosphate + D-xylulose 5-phosphate [RN:R07246]
ALL_REAC    R07246 > R01641;
            (other) R01067 R01830 R06590 R06861 R06863
SUBSTRATE   sedoheptulose 7-phosphate [CPD:C00281];
            D-glyceraldehyde 3-phosphate [CPD:C00118]
PRODUCT     D-ribose 5-phosphate [CPD:C00117];
            D-xylulose 5-phosphate [CPD:C00231]
COFACTOR    Thiamin diphosphate [CPD:C00068];
            Magnesium [CPD:C00305]
COMMENT     A thiamine-diphosphate protein. Wide specificity for both reactants,
            e.g. converts hydroxypyruvate and R-CHO into CO2 and
            R-CHOH-CO-CH2OH. Transketolase from Alkaligenes faecalis shows high
            activity with D-erythrose as acceptor.
REFERENCE   1  [PMID:14367398]
  AUTHORS   DE LA HABA G, LEDER IG, RACKER E.
  TITLE     Crystalline transketolase from bakers' yeast: isolation and
            properties.
  JOURNAL   J. Biol. Chem. 214 (1955) 409-26.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2
  AUTHORS   Domagk, G.F. and Horecker, B.L.
  TITLE     Fructose and erythrose metabolism in Alcaligenes faecalis.
  JOURNAL   Arch. Biochem. Biophys. 109 (1965) 342-349.
  ORGANISM  Alcaligenes faecalis
REFERENCE   3  [PMID:13385248]
  AUTHORS   HORECKER BL, HURWITZ J, SMYRNIOTIS PZ.
  TITLE     The role of xylulose 5-phosphate in the transketolase reaction.
  JOURNAL   J. Biol. Chem. 223 (1956) 1009-19.
  ORGANISM  spinach
REFERENCE   4
  AUTHORS   Racker, E.
  TITLE     Transketolase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 5, Academic Press, New York, 1961, p. 397-412.
PATHWAY     PATH: map00030  Pentose phosphate pathway
            PATH: map00710  Carbon fixation
            PATH: map01051  Biosynthesis of ansamycins
ORTHOLOGY   KO: K00615  transketolase
GENES       HSA: 7086(TKT) 84076(TKTL2)
            PTR: 461583(TKTL2)
            MCC: 706986(LOC706986)
            MMU: 21881(Tkt) 74419(Tktl2) 83553(Tktl1)
            RNO: 290685(Tktl2_predicted) 64524(Tkt)
            CFA: 476588(TKT) 481083(TKTL1)
            BTA: 445425(TKT) 509186(LOC509186)
            GGA: 415991(TKT)
            XLA: 379575(MGC69114) 398860(MGC68785)
            XTR: 394835(MGC76292)
            DRE: 378713(tkt)
            SPU: 576207(LOC576207)
            DME: Dmel_CG5103
            CEL: F01G10.1(transketolase)
            ATH: AT2G45290 AT3G60750
            OSA: 4335330 4340025
            CME: CMO128C
            SCE: YBR117C(TKL2) YPR074C(TKL1)
            AGO: AGOS_ADL366W
            PIC: PICST_53327(DHA1) PICST_67105(TKT1)
            CGR: CAGL0D01298g
            SPO: SPBC2G5.05
            ANI: AN0688.2 AN8551.2
            AFM: AFUA_1G13500
            AOR: AO090012000526 AO090023000345
            CNE: CND00940 CNE00140 CNM01730
            UMA: UM04967.1
            ECU: ECU06_0120
            DDI: DDBDRAFT_0217422
            PFA: PFF0530w
            TET: TTHERM_00112550
            TBR: Tb927.8.6170
            TCR: 511903.120
            LMA: LmjF24.2060
            EHI: 145.t00016 162.t00017 196.t00019 196.t00020 382.t00004
                 407.t00010
            ECO: b2465(tktB) b2935(tktA)
            ECJ: JW2449(tktB) JW5478(tktA)
            ECE: Z3721(tktB) Z4279(tktA)
            ECS: ECs3327 ECs3810
            ECC: c2990(tktB) c3520(tktA) c4759
            ECI: UTI89_C2789(tktB) UTI89_C3323(tktA) UTI89_C4400
            ECP: ECP_2477 ECP_2929 ECP_4029
            ECV: APECO1_2641 APECO1_3594(tktA) APECO1_4092(tktB)
            ECW: EcE24377A_2743(tktB) EcE24377A_3269(tkt)
            ECX: EcHS_A2594(tktB) EcHS_A3093(tkt)
            STY: STY2570 STY2571 STY2711(tktB) STY3236(tktA)
            STT: t0385(tktB) t0523 t0524 t2996(tktA)
            SPT: SPA0395(tktB) SPA0523 SPA0524 SPA2947(tktA)
            SEC: SC2341(tktC) SC2342(tktN) SC2470(tktB) SC3018(tktA)
            STM: STM2340 STM2341 STM2474(tktB) STM3076(tktA)
            YPE: YPO0926(tktA) YPO3313 YPO3314
            YPK: y3310(tktA)
            YPM: YP_0372(tktA1) YP_0373(tktA2) YP_3516(tktA3)
            YPA: YPA_0340 YPA_2830 YPA_2831
            YPN: YPN_0779 YPN_0780 YPN_3123
            YPP: YPDSF_0589
            YPS: YPTB0816 YPTB0817 YPTB3198(tktA)
            YPI: YpsIP31758_0847(tkt)
            SFL: SF2507(tktB) SF2925(tktA)
            SFX: S2658(tktB) S3127(tktA)
            SFV: SFV_2509(tktB) SFV_2987(tktA)
            SSN: SSON_2545(tktB) SSON_3089(tktA)
            SBO: SBO_3054(tktA)
            SDY: SDY_3141(tktA)
            ECA: ECA0861(tktA1) ECA1950 ECA1951 ECA3914(tktA2)
            PLU: plu0946(tktA)
            BUC: BU094(tktB)
            BAS: BUsg086(tkt)
            BAB: bbp088(tktB)
            BCC: BCc_058(tktB)
            WBR: WGLp582(tktB)
            SGL: SG1715
            ENT: Ent638_2960 Ent638_3341
            KPN: KPN_03357(tktA)
            SPE: Spro_3480 Spro_3954
            BFL: Bfl516(tktA)
            BPN: BPEN_533(tktA)
            HIN: HI1023(tktA)
            HIT: NTHI1189(tktA)
            HIQ: CGSHiGG_08735
            HDU: HD1723(tktA)
            HSO: HS_0551(tktB)
            PMU: PM1242(tkt_1) PM1638(tkt_2)
            MSU: MS0057(tktA)
            APL: APL_0983(tktA)
            XFA: XF1936
            XFT: PD0861(tktA)
            XCC: XCC3220(tktA)
            XCB: XC_0929
            XCV: XCV3490(tktA)
            XAC: XAC3372(tktA)
            XOO: XOO1176(tktA)
            XOM: XOO_1070(XOO1070)
            VCH: VC0473 VCA0624
            VCO: VC0395_0565(tktA-2) VC0395_A0026(tktA-1)
            VVU: VV1_1537 VV2_0553
            VVY: VV2862 VVA1102
            VPA: VP2605 VPA1181
            VFI: VF0440 VFA0686
            PPR: PBPRA3133 PBPRB0058
            PAE: PA0548(tktA)
            PAU: PA14_07130(tktA)
            PAP: PSPA7_0651(tkt)
            PPU: PP_4965(tktA)
            PPF: Pput_4838
            PST: PSPTO_0385(tkt) PSPTO_2401 PSPTO_2402
            PSB: Psyr_4792
            PSP: PSPPH_1255 PSPPH_1256 PSPPH_4821(tkt)
            PFL: PFL_5786(tkt)
            PFO: Pfl_2718 Pfl_2719 Pfl_5267
            PEN: PSEEN5024(tktA)
            PMY: Pmen_0458
            PAR: Psyc_1617(tktA)
            PCR: Pcryo_1849
            PRW: PsycPRwf_1538
            ACI: ACIAD2035(tkt)
            SON: SO_0930(tkt)
            SDN: Sden_1083
            SFR: Sfri_0647
            SAZ: Sama_2759
            SBL: Sbal_0827
            SBM: Shew185_3540
            SPC: Sputcn32_0872
            SSE: Ssed_0874
            SPL: Spea_0788
            SHE: Shewmr4_0773
            SHM: Shewmr7_3250
            SHN: Shewana3_3353
            SHW: Sputw3181_3301
            ILO: IL2214(tktA)
            CPS: CPS_3872(tkt)
            PHA: PSHAa0671(tktA)
            PAT: Patl_3330
            SDE: Sde_0472
            PIN: Ping_0339
            MAQ: Maqu_3040
            CBU: CBU_1784(tkt)
            CBD: COXBU7E912_0224(tkt)
            LPN: lpg0139(tktA)
            LPF: lpl0139(tkt)
            LPP: lpp0154(tkt)
            MCA: MCA3040(tkt-1) MCA3046(tkt-2)
            FTU: FTT1369c(tktA)
            FTF: FTF1369c(tktA)
            FTW: FTW_0522(tktA)
            FTL: FTL_1145
            FTH: FTH_1120(tktA)
            FTA: FTA_1208(tkt)
            FTN: FTN_1333(tktA)
            TCX: Tcr_0244
            NOC: Noc_0268 Noc_2808
            AEH: Mlg_2261 Mlg_2841
            HCH: HCH_01535(tkt)
            CSA: Csal_0384
            ABO: ABO_2615(tktA)
            MMW: Mmwyl1_4319
            AHA: AHA_3123(tkt)
            DNO: DNO_1035(tkt)
            BCI: BCI_0075(tktA)
            CRP: CRP_013
            RMA: Rmag_0062
            VOK: COSY_0070(tktA)
            NME: NMB1457
            NMA: NMA1669(tkt)
            NMC: NMC1395(tkt)
            NGO: NGO1028
            CVI: CV_0191(tktA)
            RSO: RSc2750(tktA)
            REU: Reut_A2841 Reut_B4777 Reut_B4778
            REH: H16_A3147(tktA) H16_B1388(cbbT2)
            RME: Rmet_1513 Rmet_2980
            BMA: BMA1628 BMA1629 BMA2469(tkt)
            BMV: BMASAVP1_A0389(tkt)
            BML: BMA10299_A1249(tkt)
            BMN: BMA10247_3317(tkt)
            BXE: Bxe_A0565 Bxe_B1309 Bxe_B2448 Bxe_B2699
            BUR: Bcep18194_A3722
            BCN: Bcen_0155 Bcen_5284 Bcen_6387 Bcen_6422 Bcen_6423
            BCH: Bcen2424_0638 Bcen2424_5573 Bcen2424_6620 Bcen2424_6657
                 Bcen2424_6658
            BAM: Bamb_0538
            BPS: BPSL2222 BPSL2223 BPSL2953(tktA)
            BPM: BURPS1710b_2655 BURPS1710b_2656(tkt3) BURPS1710b_3467(tkt)
            BPL: BURPS1106A_3468(tkt)
            BPD: BURPS668_3431(tkt)
            BTE: BTH_I1195(tkt) BTH_I1962 BTH_I1963
            PNU: Pnuc_0227
            BPE: BP0999(tktA)
            BPA: BPP1164(tktA)
            BBR: BB1380(tktA)
            RFR: Rfer_4112
            POL: Bpro_1461 Bpro_1462 Bpro_4827
            PNA: Pnap_1984
            MPT: Mpe_A0259(tktA) Mpe_A2790(cbbT)
            HAR: HEAR0848(tkt)
            MMS: mma_0831(tktA)
            NEU: NE0328(cbbT)
            NET: Neut_1577
            NMU: Nmul_A0388 Nmul_A0468
            EBA: ebA1101(tktA)
            AZO: azo2836(tkt)
            DAR: Daro_3591 Daro_3626
            TBD: Tbd_0159(cbbT)
            MFA: Mfla_2249
            HPY: HP1088
            HPA: HPAG1_0359
            HHE: HH0026(tktA)
            HAC: Hac_0794(tktA)
            WSU: WS0561
            TDN: Tmden_0338
            CJE: Cj1645(tkt)
            CJR: CJE1817(tkt)
            CJJ: CJJ81176_1636(tkt)
            CJU: C8J_1547(tkt)
            CJD: JJD26997_2005(tkt)
            CFF: CFF8240_0069(tkt)
            CCV: CCV52592_0069(tkt)
            CHA: CHAB381_0202(tkt)
            CCO: CCC13826_1735(tkt)
            ABU: Abu_0182(tkt)
            NIS: NIS_0258
            SUN: SUN_0166
            GSU: GSU2918 GSU2919 GSU3423(tkt)
            GME: Gmet_0178 Gmet_0551 Gmet_0552
            GUR: Gura_0970
            PCA: Pcar_2719 Pcar_2720 Pcar_3125
            DVU: DVU2530(tkt)
            DVL: Dvul_0715
            DDE: Dde_2631
            LIP: LI0219(tkt)
            BBA: Bd3475
            ADE: Adeh_0289
            MXA: MXAN_7358(tkt)
            SAT: SYN_01447
            SFU: Sfum_1302
            WOL: WD0387(tkt)
            WBM: Wbm0664
            AMA: AM852(tktA)
            APH: APH_0340(tkt)
            ERU: Erum5600(tkt)
            ERW: ERWE_CDS_05870(tktA)
            ERG: ERGA_CDS_05780(tktA)
            ECN: Ecaj_0561
            ECH: ECH_0465(tkt)
            NSE: NSE_0704
            PUB: SAR11_0536(tktC) SAR11_0537(tktN) SAR11_0587(tktB)
            MLO: mll5764 mll5765 mlr3749
            MES: Meso_3440 Meso_3617 Meso_3618
            SME: SMb20200(cbbT) SMc00269 SMc00270 SMc02342(tkt1)
                 SMc03978(tkt2)
            SMD: Smed_2479
            ATU: Atu1901(tktB) Atu1902(tkt) Atu3736(tktA)
            ATC: AGR_C_3490 AGR_C_3491 AGR_L_2197
            RET: RHE_CH02397(tktA) RHE_CH02398(tktB) RHE_CH03495(tkt)
            RLE: RL2718 RL2719 RL4006(cbbT) pRL100453
            BME: BMEI0311
            BMF: BAB1_1740(tkt)
            BMS: BR1727(tkt)
            BMB: BruAb1_1712(tkt)
            BOV: BOV_1669(tkt)
            BJA: bll1524(tktA) blr2168 blr2169 blr2583(cbbT) blr5426(tktB)
                 blr5427
            BRA: BRADO1126(cbbT) BRADO1657(cbbT) BRADO4763 BRADO4764 BRADO5169
                 BRADO5170
            BBT: BBta_0447(cbbT) BBta_3268 BBta_3269 BBta_5636 BBta_5637
                 BBta_6399(cbbT) BBta_6923(cbbT)
            RPA: RPA0945(cbbT2) RPA4643(cbbT1)
            RPB: RPB_0949 RPB_4466
            RPC: RPC_2897 RPC_3878 RPC_3879 RPC_4766
            RPD: RPD_1052 RPD_4312
            RPE: RPE_1517 RPE_1518 RPE_2684 RPE_4238 RPE_4729
            NWI: Nwi_2734
            NHA: Nham_3531
            BHE: BH15090(tktA)
            BQU: BQ12020(tktA)
            BBK: BARBAKC583_0137(tkt)
            XAU: Xaut_3074
            CCR: CC_3620
            SIL: SPO1865(tkt)
            SIT: TM1040_1113
            RSP: RSP_2956(tktA) RSP_3268(tklB)
            RSQ: Rsph17025_4011
            JAN: Jann_1700
            RDE: RD1_2982(tktA)
            PDE: Pden_1275
            MMR: Mmar10_2430
            HNE: HNE_3455(tkt)
            ZMO: ZMO0176(tklB)
            NAR: Saro_1968
            SAL: Sala_1320
            ELI: ELI_05205
            GOX: GOX1703
            GBE: GbCGDNIH1_0856
            RRU: Rru_A0595 Rru_A2405
            MAG: amb0066 amb0067 amb1381
            MGM: Mmc1_0615 Mmc1_1058 Mmc1_1059 Mmc1_3479
            ABA: Acid345_2237 Acid345_2808
            BSU: BG11247(tkt)
            BHA: BH2352(tkt)
            BAN: BA3432(tkt-1) BA3744(tkt-2)
            BAR: GBAA3432(tkt-1) GBAA3744(tkt-2)
            BAA: BA_3930 BA_4224
            BAT: BAS3181 BAS3470
            BCE: BC3682
            BCA: BCE_3411(tkt) BCE_3718(tkt)
            BCZ: BCZK3082(tkt) BCZK3388(tkt)
            BTK: BT9727_3165(tkt) BT9727_3436(tkt)
            BLI: BL01777(tktA) BL02934(tkt) BL05028
            BLD: BLi00495 BLi00496 BLi02036(tkt)
            BCL: ABC0948 ABC1106 ABC2164(tkt)
            BAY: RBAM_017690(tkt)
            BPU: BPUM_1690(tkt)
            OIH: OB1672(tkt)
            GKA: GK1332(tkt)
            SAU: SA1177(tkt)
            SAV: SAV1342(tkt)
            SAM: MW1229(tkt)
            SAR: SAR1352
            SAS: SAS1282
            SAC: SACOL1377(tkt)
            SAB: SAB1200
            SAA: SAUSA300_1239(tkt)
            SAO: SAOUHSC_01337
            SEP: SE1025
            SER: SERP0912(tkt)
            SHA: SH1565(tkt)
            SSP: SSP1416
            LMO: lmo0342 lmo1032 lmo1033 lmo1305(tkt) lmo2660
            LMF: LMOf2365_0362(tkt-1) LMOf2365_1053 LMOf2365_1054
                 LMOf2365_1323(tkt-2) LMOf2365_2640(tkt-3)
            LIN: lin0360 lin1343(tkt) lin2809
            LWE: lwe0298 lwe1320(tkt) lwe2609(tkt)
            LLA: L0043(tkt)
            LLC: LACR_1734
            LLM: llmg_0868(tkt)
            SPY: SPy_1676(tkt)
            SPZ: M5005_Spy_1375(tkt)
            SPM: spyM18_1687
            SPG: SpyM3_1462(tkt)
            SPS: SPs0404
            SPH: MGAS10270_Spy1493(tkt)
            SPI: MGAS10750_Spy1485(tkt) MGAS10750_Spy1486
            SPJ: MGAS2096_Spy1398(tkt)
            SPK: MGAS9429_Spy1373(tkt)
            SPF: SpyM50415(tkt)
            SPA: M6_Spy1423
            SPB: M28_Spy1418(tkt)
            SPN: SP_2030 SP_2127 SP_2128
            SPR: spr1841(tktA) spr1936(tktC) spr1937(tktN)
            SPD: SPD_1839(tkt)
            SAG: SAG0199 SAG0200 SAG0278(tkt)
            SAN: gbs0194 gbs0195 gbs0268
            SAK: SAK_0262 SAK_0350(tkt) SAK_1756(tkt)
            SMU: SMU.291(tkt)
            STC: str0312(tkt)
            STL: stu0312(tkt)
            SSA: SSA_2075(tkt)
            LPL: lp_1083(tkt2) lp_3135(tkt3) lp_3538(tkt4)
            LJO: LJ1266 LJ1267
            LAC: LBA1489 LBA1490
            LSL: LSL_1946(tktA)
            LBR: LVIS_1420
            OOE: OEOE_1480
            STH: STH2121 STH2310 STH2311
            CAC: CAC0944(tkt) CAC1348
            CPE: CPE0296(tktN) CPE0297(tktC)
            CPF: CPF_0292 CPF_0293
            CPR: CPR_0287 CPR_0288
            CTC: CTC01332
            CNO: NT01CX_1267 NT01CX_1268
            CDF: CD2321(tkt') CD2322(tkt) CD3459(tkt') CD3460(tkt)
            CBO: CBO3394(tkt') CBO3395(tkt)
            CKL: CKL_3577(tktB) CKL_3578(tktA)
            CHY: CHY_0165 CHY_0166
            DSY: DSY4867 DSY4868
            SWO: Swol_0243 Swol_0244
            TTE: TTE0190(tktA)
            MTA: Moth_0236 Moth_0237
            MGE: MG_066(tktA)
            MPN: MPN082(tklB)
            MPU: MYPU_5110(tkt)
            MPE: MYPE4510(tktA) MYPE770(tkt)
            MGA: MGA_0342(tktA) MGA_0666(tktA)
            MMY: MSC_0372(tkt)
            MMO: MMOB5530(tktA)
            MHY: mhp431(tktA)
            MHJ: MHJ_0426(tkt)
            MHP: MHP7448_0428(tkt)
            MSY: MS53_0181(tktA)
            MCP: MCAP_0610(tkt)
            UUR: UU586(tktA)
            MFL: Mfl349
            MTU: Rv1449c(tkt)
            MTC: MT1496(tkt)
            MBO: Mb1484c(tkt)
            MBB: BCG_1510c(tkt)
            MLE: ML0583(tkt)
            MPA: MAP1178c(tkt)
            MAV: MAV_3327(tkt)
            MSM: MSMEG_2165 MSMEG_2166 MSMEG_3103(tkt) MSMEG_4436
            MMC: Mmcs_2414
            MKM: Mkms_2460
            MJL: Mjls_2454
            CGL: NCgl1512(cgl1574)
            CGB: cg1774(tkt)
            CEF: CE1694(tkt)
            CDI: DIP1302(tkt)
            CJK: jk0992(tkt)
            NFA: nfa32320 nfa32330 nfa35730
            RHA: RHA1_ro00814 RHA1_ro00815 RHA1_ro03843 RHA1_ro03844
                 RHA1_ro07186
            SCO: SCO1935(SCC22.17) SCO6497(tktA2) SCO6663(tktB)
            SMA: SAV1623 SAV1766(tkt1) SAV1891(tkt3) SAV6315(tkt2)
            TWH: TWT340(tkt)
            TWS: TW431(tkt)
            LXX: Lxx11620(tktA1)
            CMI: CMM_1734(tktA)
            AAU: AAur_2097(tkt)
            PAC: PPA2318
            TFU: Tfu_2002
            FRA: Francci3_1278
            FAL: FRAAL2021(tktB)
            SEN: SACE_2160(tkt) SACE_3326(tktA2) SACE_4350 SACE_5763
            BLO: BL0716(tkt)
            BAD: BAD_0829(tkt)
            RXY: Rxyl_0049
            FNU: FN0294 FN0295
            RBA: RB12921(tkt)
            CTR: CT750(tktB)
            CTA: CTA_0819(tktB)
            CMU: TC0131
            CPN: CPn0893(tktB_1)
            CPA: CP0973
            CPJ: CPj0893(tktB_1)
            CPT: CpB0924
            CCA: CCA00875(tkt)
            CAB: CAB841
            CFE: CF0141(tkt)
            PCU: pc1514(tkt)
            TPA: TP0560
            TDE: TDE1308(tkt)
            LIL: LA1586(tktC1) LA2632(tktC2) LA3219(tktN2)
            LIC: LIC10913(tktA) LIC11355(tkt) LIC12194(tktC)
            LBJ: LBJ_1644(tktC) LBJ_2615(tktN)
            LBL: LBL_0493(tktN) LBL_1863(tktC)
            SYN: sll1070(tktA)
            SYW: SYNW0141(tktA)
            SYC: syc0983_c(tktA)
            SYF: Synpcc7942_0538
            SYD: Syncc9605_0124
            SYE: Syncc9902_0168
            SYG: sync_0130(tkt)
            SYR: SynRCC307_0130(tktA)
            SYX: SynWH7803_0195(tktA)
            CYA: CYA_2346(tkt)
            CYB: CYB_1119(tkt)
            TEL: tll1870
            GVI: glr2297
            ANA: all4052 alr3344
            AVA: Ava_1655 Ava_3645
            PMA: Pro1280 Pro1281 Pro1770(tktA)
            PMM: PMM1235 PMM1236 PMM1610(tktA)
            PMT: PMT1957(tktA)
            PMN: PMN2A_1187
            PMB: A9601_14541 A9601_14551 A9601_18201(tktA)
            PMC: P9515_17981(tktA)
            PMF: P9303_26081(tktA)
            PMG: P9301_18031(tktA)
            PMH: P9215_18841(tktA)
            PME: NATL1_20621(tktA)
            TER: Tery_0450
            BTH: BT_0347
            BFR: BF1652
            BFS: BF1660(tktB)
            PGI: PG1748(tkt)
            SRU: SRU_0275(tkt)
            CHU: CHU_1894(tktA) CHU_1895(tktC) CHU_1992(tktA)
            GFO: GFO_0703(tktA) GFO_0704(tktB)
            FPS: FP0682(tktN) FP0683(tktC)
            CTE: CT0804 CT0963 CT1870(tkt)
            CCH: Cag_1192 Cag_1437
            PLT: Plut_0309 Plut_1192 Plut_1286
            DET: DET0644(tkt-1) DET0678(tkt-2)
            DEH: cbdb_A629(tkt)
            DRA: DR_2256
            DGE: Dgeo_2283
            TTH: TTC1896
            TTJ: TTHA0108
            AAE: aq_1765(tktA)
            TMA: TM0953 TM0954 TM1762
            TME: Tmel_1753
            MMP: MMP1113 MMP1115
            MVN: Mevan_0440
            TAC: Ta0617 Ta0618
            TVO: TVN0667 TVN0668
            PTO: PTO0690 PTO0691
            PAB: PAB0295(tkt1) PAB0296(tkt2)
            PFU: PF1688 PF1689
            TKO: TK0269 TK0270
            APE: APE_0583 APE_0586.1
            SSO: SSO0297(tkt-1) SSO0299(tkt-2)
            STO: ST2268 ST2269
            SAI: Saci_0180 Saci_0181
            PAI: PAE1927 PAE1929
STRUCTURES  PDB: 1AY0  1GPU  1ITZ  1NGS  1QGD  1R9J  1TKA  1TKB  1TKC  1TRK  
DBLINKS     IUBMB Enzyme Nomenclature: 2.2.1.1
            ExPASy - ENZYME nomenclature database: 2.2.1.1
            ExplorEnz - The Enzyme Database: 2.2.1.1
            ERGO genome analysis and discovery system: 2.2.1.1
            BRENDA, the Enzyme Database: 2.2.1.1
            CAS: 9014-48-6
///
ENTRY       EC 2.2.1.2                  Enzyme
NAME        transaldolase;
            dihydroxyacetonetransferase;
            dihydroxyacetone synthase;
            formaldehyde transketolase
CLASS       Transferases;
            Transferring aldehyde or ketonic groups;
            Transketolases and transaldolases
SYSNAME     sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate
            glyceronetransferase
REACTION    sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate =
            D-erythrose 4-phosphate + D-fructose 6-phosphate [RN:R07378]
ALL_REAC    R07378 > R01827
SUBSTRATE   sedoheptulose 7-phosphate [CPD:C00281];
            D-glyceraldehyde 3-phosphate [CPD:C00118]
PRODUCT     D-erythrose 4-phosphate [CPD:C00279];
            D-fructose 6-phosphate [CPD:C00085]
REFERENCE   1  [PMID:14353883]
  AUTHORS   HORECKER BL, SMYRNIOTIS PZ.
  TITLE     Purification and properties of yeast transaldolase.
  JOURNAL   J. Biol. Chem. 212 (1955) 811-25.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2
  AUTHORS   Racker, E.
  TITLE     Transaldolase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 5, Academic Press, New York, 1961, p. 407-412.
REFERENCE   3
  AUTHORS   Tsolas, O. and Horecker, B.L.
  TITLE     Transaldolase.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 7, Academic Press,
            New York, 1972, p. 259-280.
PATHWAY     PATH: map00030  Pentose phosphate pathway
ORTHOLOGY   KO: K00616  transaldolase
GENES       HSA: 6888(TALDO1)
            PTR: 450933(TALDO1)
            MMU: 21351(Taldo1)
            RNO: 83688(Taldo1)
            CFA: 475937(TALDO1)
            GGA: 423019(RCJMB04_9n21)
            XLA: 495027(LOC495027)
            SPU: 587780(LOC587780)
            DME: Dmel_CG2827(Tal)
            CEL: Y24D9A.8
            ATH: AT1G12230 AT5G13420
            OSA: 4327239 4344683
            SCE: YGR043C(NQM1) YLR354C(TAL1)
            AGO: AGOS_ACL196W
            PIC: PICST_74289(TAL1)
            CGR: CAGL0B03069g CAGL0K04235g
            SPO: SPCC1020.06c(tal1)
            ANI: AN0240.2 AN6113.2
            AFM: AFUA_5G09230
            AOR: AO090020000520
            CNE: CNB05080 CNK03170
            UMA: UM04138.1 UM06453.1
            DDI: DDB_0231283(tal)
            TET: TTHERM_00043910
            TBR: Tb927.8.5600
            TCR: 503477.20 507889.10
            LMA: LmjF16.0760
            ECO: b0008(talB) b2464(talA)
            ECJ: JW0007(talB) JW2448(talA)
            ECE: Z0008(talB) Z3720(talA)
            ECS: ECs0008 ECs3326
            ECC: c0012(talB) c2989(talA)
            ECI: UTI89_C0009(talB) UTI89_C2788(talA)
            ECP: ECP_0009 ECP_2476
            ECV: APECO1_1970(talB) APECO1_4093(talA)
            ECW: EcE24377A_0008(tal2) EcE24377A_2742(tal1)
            ECX: EcHS_A0009(tal2) EcHS_A2593(tal1)
            STY: STY0007(talB) STY2710(talA)
            STT: t0007(talB) t0386(talA)
            SPT: SPA0007(talB) SPA0396(talA)
            SEC: SC0007(talB) SC2469(talA)
            STM: STM0007(talB) STM2473(talA)
            YPE: YPO0463(talB)
            YPK: y3712(talB)
            YPM: YP_3718(talB)
            YPA: YPA_4056
            YPN: YPN_0335
            YPP: YPDSF_0902 YPDSF_3169
            YPS: YPTB0606(talB)
            YPI: YpsIP31758_3472(tal)
            YEN: YE0604(talB)
            SFL: SF0009(talB) SF2506(talA)
            SFX: S0008(talB) S2657(talA)
            SFV: SFV_0007(talB) SFV_2508(talA)
            SSN: SSON_0009(talB) SSON_2544(talA)
            SBO: SBO_0009(talB)
            SDY: SDY_0008(talB)
            ECA: ECA0862(talA) ECA3887(talB)
            PLU: plu0568(talB)
            BUC: BU093(talA)
            BAS: BUsg085(tal)
            BAB: bbp087(talA)
            BCC: BCc_057(talA)
            WBR: WGLp583(talA)
            SGL: SG1714
            ENT: Ent638_0570 Ent638_1319 Ent638_2959
            KPN: KPN_02798(talA)
            SPE: Spro_0688 Spro_3479
            BFL: Bfl515(talA)
            BPN: BPEN_532(talA)
            HIN: HI1125(talB)
            HIT: NTHI1293(talB)
            HDU: HD0310(tal)
            HSO: HS_0204(tal)
            PMU: PM1602(tal_1) PM1639(tal_2)
            MSU: MS2355(mipB)
            APL: APL_0062(mipB)
            ASU: Asuc_0582
            XCC: XCC0830(talB)
            XCB: XC_3400
            XCV: XCV0939(talB)
            XAC: XAC0902(talB)
            XOO: XOO3649(talB)
            XOM: XOO_3451(XOO3451)
            VCH: VCA0623
            VCO: VC0395_0564(talB)
            VVU: VV2_0552
            VVY: VVA1101
            VPA: VPA1180
            VFI: VFA0685
            PPR: PBPRB0059
            PAE: PA2796(tal)
            PAU: PA14_27960(tal)
            PAP: PSPA7_2361(tal)
            PPU: PP_2168(tal)
            PPF: Pput_3574
            PST: PSPTO_2119(tal)
            PSB: Psyr_1914
            PSP: PSPPH_1869(tal)
            PFL: PFL_1974(tal)
            PFO: Pfl_3847
            PEN: PSEEN3692(tal)
            PMY: Pmen_1931
            PAR: Psyc_1187(tal)
            PCR: Pcryo_1203
            PRW: PsycPRwf_1251
            ACI: ACIAD1980(tal)
            SON: SO_3546(tal)
            SDN: Sden_2734
            SFR: Sfri_2900
            SAZ: Sama_0913
            SBL: Sbal_1044
            SBM: Shew185_1111
            SLO: Shew_1089
            SPC: Sputcn32_1049
            SSE: Ssed_1185
            SPL: Spea_1074
            SHE: Shewmr4_2967
            SHM: Shewmr7_3049
            SHN: Shewana3_3147
            SHW: Sputw3181_3116
            CPS: CPS_4104(tal)
            PHA: PSHAa2559(talB)
            PAT: Patl_3622
            SDE: Sde_0775 Sde_1485
            PIN: Ping_0086 Ping_2054
            MAQ: Maqu_1919
            CBD: COXBU7E912_0688
            MCA: MCA3045(tal)
            FTU: FTT1093c(talA)
            FTF: FTF1093c(talA)
            FTW: FTW_1399(tal)
            FTL: FTL_1109
            FTH: FTH_1082(talA)
            FTA: FTA_1169(tal)
            FTN: FTN_0781(talA)
            NOC: Noc_0269 Noc_2057
            AEH: Mlg_0221
            HCH: HCH_02352(tal1) HCH_02473(tal2)
            CSA: Csal_0354 Csal_0645
            ABO: ABO_1514(talB)
            MMW: Mmwyl1_2514
            AHA: AHA_3140(tal)
            BCI: BCI_0076(talB)
            CRP: CRP_113
            NME: NMB0351
            NMA: NMA2136(tal)
            NMC: NMC1818(tal)
            NGO: NGO1610
            CVI: CV_0564(talA) CV_2247(talC)
            RSO: RSc1231(tal)
            REU: Reut_A2069
            REH: H16_A2346(tal)
            RME: Rmet_2089
            BMA: BMA1940(tal)
            BMV: BMASAVP1_A1013(tal)
            BML: BMA10299_A0852(tal)
            BMN: BMA10247_0296(tal)
            BXE: Bxe_A3318
            BVI: Bcep1808_2425
            BUR: Bcep18194_A5677
            BCN: Bcen_1723
            BCH: Bcen2424_2335
            BAM: Bamb_2374
            BPS: BPSL1095(talB)
            BPM: BURPS1710b_1326(tal)
            BPL: BURPS1106A_1174(tal)
            BPD: BURPS668_1166(tal)
            BTE: BTH_I0962(tal)
            PNU: Pnuc_1265
            BPE: BP1451(talB)
            BPA: BPP1228(talB)
            BBR: BB1445(talB)
            RFR: Rfer_1126
            POL: Bpro_0752 Bpro_4350
            PNA: Pnap_0654
            AAV: Aave_0943
            AJS: Ajs_0696
            VEI: Veis_1779
            MPT: Mpe_A3095
            HAR: HEAR1082(tal)
            MMS: mma_2315(tal)
            NEU: NE2136(tal)
            NET: Neut_2089
            NMU: Nmul_A1622
            EBA: ebA4676(talA)
            AZO: azo1464(tal)
            DAR: Daro_2062
            TBD: Tbd_0665
            MFA: Mfla_1655
            HPY: HP1495
            HPJ: jhp1388(tal)
            HPA: HPAG1_1418
            HHE: HH1140(tal)
            HAC: Hac_1755(tal)
            WSU: WS2080
            TDN: Tmden_0464
            CJE: Cj0281c(tal)
            CJR: CJE0329(tal)
            CJJ: CJJ81176_0307(tal)
            CJU: C8J_0257(tal)
            CJD: JJD26997_1690(tal)
            CFF: CFF8240_0334(tal)
            CCV: CCV52592_1660(tal)
            CHA: CHAB381_1306(tal)
            CCO: CCC13826_0503 CCC13826_1583(tal)
            ABU: Abu_0222(tal)
            NIS: NIS_0382(tal)
            SUN: SUN_2063
            GSU: GSU2977
            GME: Gmet_0497
            GUR: Gura_0705
            PCA: Pcar_0248
            PPD: Ppro_0294
            DVU: DVU1658
            DVL: Dvul_1428
            DDE: Dde_1070
            LIP: LIC016(tal)
            BBA: Bd0049(talC)
            DPS: DP0428
            ADE: Adeh_4063
            AFW: Anae109_0364
            MXA: MXAN_5922
            SAT: SYN_02165
            SFU: Sfum_0051
            WOL: WD0551
            WBM: Wbm0686
            AMA: AM664
            APH: APH_0492
            ERU: Erum4570(tal)
            ERW: ERWE_CDS_04790(tal)
            ERG: ERGA_CDS_04690(tal)
            NSE: NSE_0761
            PUB: SAR11_0577(tal)
            MLO: mlr4072
            MES: Meso_3212
            PLA: Plav_1459
            SME: SMc02495
            SMD: Smed_2928
            ATU: Atu4464(talB)
            ATC: AGR_L_812
            RET: RHE_CH03667(tal)
            RLE: RL4203(talB)
            BME: BMEI0244
            BMF: BAB1_1813
            BMS: BR1805
            BMB: BruAb1_1785
            OAN: Oant_1099
            BJA: blr6758
            BRA: BRADO5809
            BBT: BBta_6315 BBta_p0088
            RPA: RPA3634(tal)
            RPB: RPB_1892
            RPC: RPC_3670
            RPD: RPD_3474
            RPE: RPE_1508 RPE_3708
            NWI: Nwi_2641
            BHE: BH15370(talC)
            BQU: BQ12290(talC)
            BBK: BARBAKC583_0106
            CCR: CC_3614
            SIT: TM1040_2379
            RSP: RSP_0561
            RSH: Rsph17029_2213
            RSQ: Rsph17025_1224
            JAN: Jann_1032
            RDE: RD1_2080(tal)
            PDE: Pden_2499
            MMR: Mmar10_1147
            HNE: HNE_3235
            NAR: Saro_2390
            SAL: Sala_1807
            SWI: Swit_0219
            ELI: ELI_08705
            GOX: GOX1704
            GBE: GbCGDNIH1_0855
            RRU: Rru_A1357
            ABA: Acid345_2810 Acid345_3708
            SUS: Acid_6703
            BSU: BG10413(ywjH)
            BHA: BH3785
            BAN: BA0670 BA3430
            BAR: GBAA0670 GBAA3430
            BAA: BA_1258 BA_3928
            BAT: BAS0637 BAS3179
            BCE: BC0665 BC3371
            BCA: BCE_0738 BCE_3409
            BCZ: BCZK0580(tal) BCZK3080(tal)
            BCY: Bcer98_0565
            BTK: BT9727_0581(tal) BT9727_3163(tal)
            BTL: BALH_0613
            BLI: BL03970(tal)
            BLD: BLi03959(ywjH)
            BCL: ABC3882
            BAY: RBAM_034270(tal)
            BPU: BPUM_3356(ywjH)
            OIH: OB3004
            GKA: GK3385
            SAC: SACOL1831(tal)
            SAB: SAB1639c
            SAA: SAUSA300_1725
            SER: SERP1336(tal)
            SHA: SH1145
            LMO: lmo0343 lmo2743
            LMF: LMOf2365_0363 LMOf2365_2730
            LIN: lin0361 lin2886
            LWE: lwe0299 lwe2691
            SPY: SPy_1678
            SPZ: M5005_Spy_1376 M5005_Spy_1661
            SPM: spyM18_1689
            SPG: SpyM3_1463(tal)
            SPS: SPs0403
            SPH: MGAS10270_Spy1494 MGAS10270_Spy1729 MGAS10270_Spy1811(mipB)
            SPI: MGAS10750_Spy1487 MGAS10750_Spy1755 MGAS10750_Spy1836(mipB)
            SPJ: MGAS2096_Spy1399 MGAS2096_Spy1684 MGAS2096_Spy1776(mipB)
            SPK: MGAS9429_Spy1374 MGAS9429_Spy1662 MGAS9429_Spy1751(mipB)
            SPF: SpyM50414 SpyM51705(fsa)
            SPA: M6_Spy1424 M6_Spy1669
            SPB: M28_Spy1419 M28_Spy1649
            SPD: SPD_0236(talC)
            SAG: SAG1809
            SAN: gbs1850
            SAK: SAK_1757 SAK_1829
            SSA: SSA_0286
            LPL: lp_3539(tal2)
            LSL: LSL_1888(mipB) LSL_1947(mipB)
            LBR: LVIS_0764
            LCA: LSEI_0367
            STH: STH66
            CAC: CAC1347
            CPE: CPE0692
            CPF: CPF_0684
            CPR: CPR_0683
            CTC: CTC00228
            CNO: NT01CX_0748
            CDF: CD2329(tal1)
            CBO: CBO1292(tal)
            CBA: CLB_1321 CLB_2092
            CBH: CLC_1331 CLC_2097
            CBF: CLI_1378 CLI_2200
            CBE: Cbei_0317 Cbei_0338 Cbei_2386 Cbei_4454 Cbei_4645
            CKL: CKL_0998(tal)
            AMT: Amet_0319
            CHY: CHY_0129
            DSY: DSY4938
            DRM: Dred_3175
            SWO: Swol_2410
            CSC: Csac_2036
            TTE: TTE1918(mipB)
            MTA: Moth_2403
            MTU: Rv1448c(tal)
            MTC: MT1495(tal)
            MBO: Mb1483c(tal)
            MBB: BCG_1509c(tal)
            MLE: ML0582(tal)
            MPA: MAP1177c(tal)
            MAV: MAV_3328(tal)
            MSM: MSMEG_3102(tal) MSMEG_4415(tal)
            MMC: Mmcs_2413
            CGL: NCgl1513(cgl1575)
            CGB: cg1776(tal)
            CEF: CE1695
            CDI: DIP1303(tal)
            CJK: jk0993(tal)
            NFA: nfa35740
            RHA: RHA1_ro07185(tal) RHA1_ro08277
            SCO: SCO1936(SCC22.18) SCO6662(tal1)
            SMA: SAV1767(tal1) SAV6314(tal2)
            TWH: TWT341(tal)
            TWS: TW430(tal)
            LXX: Lxx11610(tal2)
            CMI: CMM_1735(talA)
            AAU: AAur_2096(tal)
            PAC: PPA0454
            TFU: Tfu_2003
            FRA: Francci3_1648
            FAL: FRAAL4574(tal)
            SEN: SACE_2159(tal)
            BLO: BL0715(tal)
            BAD: BAD_0830(tal)
            RXY: Rxyl_0048
            RBA: RB3193
            CTR: CT313(tal)
            CTA: CTA_0335(tal)
            CMU: TC0587
            CPN: CPn0083(tal)
            CPA: CP0692
            CPJ: CPj0083(tal)
            CPT: CpB0083
            CCA: CCA00689(tal)
            CAB: CAB659(talA)
            CFE: CF0322(talA)
            PCU: pc1691(talB) pc1983(talB)
            LIL: LA1585(tktN1) LA2286
            LIC: LIC11652(tal) LIC12195
            LBJ: LBJ_1326(mipB)
            LBL: LBL_1551(mipB)
            SYN: slr1793(talB)
            SYW: SYNW1759(tal)
            SYC: syc1803_d(tal)
            SYF: Synpcc7942_2297
            SYD: Syncc9605_0705
            SYE: Syncc9902_1653
            SYG: sync_2008(tal)
            SYR: SynRCC307_0863(tal)
            SYX: SynWH7803_0634(tal)
            CYA: CYA_0725(tal)
            CYB: CYB_1112(tal)
            TEL: tll0467
            GVI: gll1597 glr3377
            ANA: all2563(tal) all4020(tal)
            AVA: Ava_0493 Ava_1681
            PMA: Pro0519(tal)
            PMM: PMM0519(tal)
            PMT: PMT1248(tal)
            PMN: PMN2A_1851
            PMI: PMT9312_0519
            PMB: A9601_05751(tal)
            PMC: P9515_05831(tal)
            PMF: P9303_07571(tal)
            PMG: P9301_05451(tal)
            PMH: P9215_06001(tal)
            PME: NATL1_05761(tal)
            TER: Tery_0283 Tery_0519 Tery_0683
            BTH: BT_1658
            BFR: BF3242
            BFS: BF3082(tal)
            PGI: PG0230
            SRU: SRU_0080(tal) SRU_0276
            CHU: CHU_2529(talAB)
            GFO: GFO_0702(tal) GFO_2258(tal)
            FJO: Fjoh_2002 Fjoh_4567
            FPS: FP1048(tal)
            CTE: CT0010(tal)
            CCH: Cag_0074
            CPH: Cpha266_2698
            PVI: Cvib_1728
            PLT: Plut_2088
            DET: DET1409
            DEH: cbdb_A1370(tal)
            DEB: DehaBAV1_1216
            RRS: RoseRS_4615
            RCA: Rcas_0417
            DRA: DR_1337
            DGE: Dgeo_1102
            TTH: TTC0701
            TTJ: TTHA1066
            AAE: aq_119(talC)
            TMA: TM0295
            TPT: Tpet_0617
            TME: Tmel_1619
            FNO: Fnod_1229
            MJA: MJ0960(tal)
            MMP: MMP1308(tal)
            MMQ: MmarC5_0285
            MMZ: MmarC7_0553
            MAE: Maeo_0278
            MVN: Mevan_0618
            TAC: Ta0616
            TVO: TVN0666
            PTO: PTO0689
STRUCTURES  PDB: 1F05  1I2N  1I2O  1I2P  1I2Q  1I2R  1ONR  1UCW  1VPX  1WX0  
                 2A7G  2CWN  
DBLINKS     IUBMB Enzyme Nomenclature: 2.2.1.2
            ExPASy - ENZYME nomenclature database: 2.2.1.2
            ExplorEnz - The Enzyme Database: 2.2.1.2
            ERGO genome analysis and discovery system: 2.2.1.2
            BRENDA, the Enzyme Database: 2.2.1.2
            CAS: 9014-46-4
///
ENTRY       EC 2.2.1.3                  Enzyme
NAME        formaldehyde transketolase;
            dihydroxyacetone synthase
CLASS       Transferases;
            Transferring aldehyde or ketonic groups;
            Transketolases and transaldolases
SYSNAME     D-xylulose-5-phosphate:formaldehyde glycolaldehydetransferase
REACTION    D-xylulose 5-phosphate + formaldehyde = glyceraldehyde 3-phosphate +
            glycerone
ALL_REAC    (other) R06861 R06862
SUBSTRATE   D-xylulose 5-phosphate [CPD:C00231];
            formaldehyde [CPD:C00067]
PRODUCT     glyceraldehyde 3-phosphate;
            glycerone [CPD:C00184]
COFACTOR    Thiamin diphosphate [CPD:C00068]
COMMENT     A thiamine-diphosphate protein. Not identical with EC 2.2.1.1
            transketolase. Also converts hydroxypyruvate and formaldehyde into
            glycerone and CO2.
REFERENCE   1  [PMID:7249920]
  AUTHORS   Bystrykh LV, Sokolov AP, Trotsenko IuA.
  TITLE     [Separation of transketolase and dihydroxyacetone synthase from
            methylotrophic yeasts]
  JOURNAL   Dokl. Akad. Nauk. SSSR. 258 (1981) 499-501.
REFERENCE   2  [PMID:7074134]
  AUTHORS   Kato N, Higuchi T, Sakazawa C, Nishizawa T, Tani Y, Yamada H.
  TITLE     Purification and properties of a transketolase responsible for
            formaldehyde fixation in a methanol-utilizing yeast, candida
            boidinii (Kloeckera sp.) No. 2201.
  JOURNAL   Biochim. Biophys. Acta. 715 (1982) 143-50.
  ORGANISM  Candida boidinii
REFERENCE   3  [PMID:6276498]
  AUTHORS   Waites MJ, Quayle JR.
  TITLE     The interrelation transketolase and dihydroxyacetone synthase
            activities in the methylotrophic yeast Candida boidinii.
  JOURNAL   J. Gen. Microbiol. 124 (1981) 309-16.
  ORGANISM  Candida boidinii
PATHWAY     PATH: map00680  Methane metabolism
GENES       AFM: AFUA_3G02910
DBLINKS     IUBMB Enzyme Nomenclature: 2.2.1.3
            ExPASy - ENZYME nomenclature database: 2.2.1.3
            ExplorEnz - The Enzyme Database: 2.2.1.3
            ERGO genome analysis and discovery system: 2.2.1.3
            BRENDA, the Enzyme Database: 2.2.1.3
            CAS: 76774-46-4
///
ENTRY       EC 2.2.1.4                  Enzyme
NAME        acetoin---ribose-5-phosphate transaldolase;
            1-deoxy-D-altro-heptulose-7-phosphate synthetase;
            1-deoxy-D-altro-heptulose-7-phosphate synthase;
            3-hydroxybutan-2-one:D-ribose-5-phosphate aldehydetransferase [wrong
            substrate name]
CLASS       Transferases;
            Transferring aldehyde or ketonic groups;
            Transketolases and transaldolases
SYSNAME     3-hydroxybutan-2-one:D-ribose-5-phosphate aldehydetransferase
REACTION    3-hydroxybutan-2-one + D-ribose 5-phosphate = acetaldehyde +
            1-deoxy-D-altro-heptulose 7-phosphate [RN:R02345]
ALL_REAC    R02345
SUBSTRATE   3-hydroxybutan-2-one [CPD:C00466];
            D-ribose 5-phosphate [CPD:C00117]
PRODUCT     acetaldehyde [CPD:C00084];
            1-deoxy-D-altro-heptulose 7-phosphate [CPD:C04359]
COFACTOR    Thiamin diphosphate [CPD:C00068]
COMMENT     A thiamine-diphosphate protein.
REFERENCE   1
  AUTHORS   Yokota, A. and Sasajima, K.
  TITLE     Enzymatic formation of a new monosaccharide,
            1-deoxy-D-altro-heptulose phosphate, from DL-acetoin and D-ribose
            5-phosphate by a transketolase mutant of Bacillus pumilus.
  JOURNAL   Agric. Biol. Chem. 47 (1983) 1545-1553.
  ORGANISM  Bacillus pumilus
DBLINKS     IUBMB Enzyme Nomenclature: 2.2.1.4
            ExPASy - ENZYME nomenclature database: 2.2.1.4
            ExplorEnz - The Enzyme Database: 2.2.1.4
            ERGO genome analysis and discovery system: 2.2.1.4
            BRENDA, the Enzyme Database: 2.2.1.4
            CAS: 87843-76-3
///
ENTRY       EC 2.2.1.5                  Enzyme
NAME        2-hydroxy-3-oxoadipate synthase;
            2-hydroxy-3-oxoadipate glyoxylate-lyase (carboxylating);
            alpha-ketoglutaric-glyoxylic carboligase;
            oxoglutarate: glyoxylate carboligase
CLASS       Transferases;
            Transferring aldehyde or ketonic groups;
            Transketolases and transaldolases
REACTION    2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO2
            [RN:R00474]
ALL_REAC    R00474
SUBSTRATE   2-oxoglutarate [CPD:C00026];
            glyoxylate [CPD:C00048]
PRODUCT     2-hydroxy-3-oxoadipate [CPD:C03217];
            CO2 [CPD:C00011]
COFACTOR    Thiamin diphosphate [CPD:C00068]
COMMENT     The bacterial enzyme requires thiamine diphosphate. The product
            decarboxylates to 5-hydroxy-4-oxopentanoate. The enzyme can
            decarboxylate 2-oxoglutarate. Acetaldehyde can replace glyoxylate.
REFERENCE   1  [PMID:5418712]
  AUTHORS   Schlossberg MA, Bloom RJ, Richert DA, Westerfeld WW.
  TITLE     Carboligase activity of alpha-ketoglutarate dehydrogenase.
  JOURNAL   Biochemistry. 9 (1970) 1148-53.
  ORGANISM  rat [GN:rno], pig [GN:ssc]
REFERENCE   2  [PMID:4320439]
  AUTHORS   Schlossberg MA, Richert DA, Bloom RJ, Westerfeld WW.
  TITLE     Isolation and identification of 5-hydroxy-4-ketovaleric acid as a
            product of alpha-ketoglutarate: glyoxylate carboligase.
  JOURNAL   Biochemistry. 7 (1968) 333-7.
  ORGANISM  cow [GN:bta]
REFERENCE   3
  AUTHORS   Stewart, P.R. and Quayle, J.R.
  TITLE     The synergistic decarboxylation of glyoxalate and 2-oxoglutarate by
            an enzyme system from pig-liver mitochondria.
  JOURNAL   Biochem. J. 102 (1967) 885-897.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.2.1.5
            ExPASy - ENZYME nomenclature database: 2.2.1.5
            ExplorEnz - The Enzyme Database: 2.2.1.5
            ERGO genome analysis and discovery system: 2.2.1.5
            BRENDA, the Enzyme Database: 2.2.1.5
            CAS: 9054-72-2
///
ENTRY       EC 2.2.1.6                  Enzyme
NAME        acetolactate synthase;
            alpha-acetohydroxy acid synthetase;
            alpha-acetohydroxyacid synthase;
            alpha-acetolactate synthase;
            alpha-acetolactate synthetase;
            acetohydroxy acid synthetase;
            acetohydroxyacid synthase;
            acetolactate pyruvate-lyase (carboxylating);
            acetolactic synthetase
CLASS       Transferases;
            Transferring aldehyde or ketonic groups;
            Transketolases and transaldolases
SYSNAME     pyruvate:pyruvate acetaldehydetransferase (decarboxylating)
REACTION    2 pyruvate = 2-acetolactate + CO2 [RN:R00006]
ALL_REAC    R00006 > R00226;
            (other) R00014 R03050 R04672 R04673
SUBSTRATE   pyruvate [CPD:C00022]
PRODUCT     2-acetolactate [CPD:C00900];
            CO2 [CPD:C00011]
COFACTOR    FAD [CPD:C00016];
            Thiamin diphosphate [CPD:C00068]
INHIBITOR   Chlorsulfuron [CPD:C05071];
            Imazaquin [CPD:C05076];
            Sulphometuron methyl [CPD:C05085];
            Ubiquinone-0 [CPD:C05251]
COMMENT     This enzyme requires thiamine diphosphate. The reaction shown is in
            the pathway of biosynthesis of valine; the enzyme can also transfer
            the acetaldehyde from pyruvate to 2-oxobutanoate, forming
            2-ethyl-2-hydroxy-3-oxobutanoate, also known as
            2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of
            isoleucine.
REFERENCE   1  [PMID:14243762]
  AUTHORS   BAUERLE RH, FRUENDLICH M, STORMER FC, UMBARGER HE.
  TITLE     CONTROL OF ISOLEUCINE, VALINE AND LEUCINE BIOSYNTHESIS. II.
            ENDPRODUCT INHIBITION BY VALINE OF ACETOHYDROXY ACID SYNTHETASE IN
            SALMONELLA TYPHIMURIUM.
  JOURNAL   Biochim. Biophys. Acta. 92 (1964) 142-9.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:5560406]
  AUTHORS   Huseby NE, Christensen TB, Olsen BR, Stormer FC.
  TITLE     The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes.
            Subunit structure.
  JOURNAL   Eur. J. Biochem. 20 (1971) 209-14.
  ORGANISM  Aerobacter aerogenes
REFERENCE   3  [PMID:5823101]
  AUTHORS   Stormer FC, Solberg Y, Hovig T.
  TITLE     The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes.
            Molecular properties.
  JOURNAL   Eur. J. Biochem. 10 (1969) 251-60.
  ORGANISM  Aerobacter aerogenes
REFERENCE   4  [PMID:3301814]
  AUTHORS   Barak Z, Chipman DM, Gollop N.
  TITLE     Physiological implications of the specificity of acetohydroxy acid
            synthase isozymes of enteric bacteria.
  JOURNAL   J. Bacteriol. 169 (1987) 3750-6.
  ORGANISM  Salmonella typhimurium, Escherichia coli [GN:eco]
PATHWAY     PATH: map00290  Valine, leucine and isoleucine biosynthesis
            PATH: map00650  Butanoate metabolism
            PATH: map00660  C5-Branched dibasic acid metabolism
            PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K01651  acetolactate synthase
            KO: K01652  acetolactate synthase large subunit
            KO: K01653  acetolactate synthase small subunit
GENES       HSA: 10994(ILVBL)
            MMU: 216136(Ilvbl)
            CEL: T26C12.1
            ATH: AT3G48560(CSR1)
            OSA: 4329450 4329938
            SCE: YCL009C(ILV6) YMR108W(ILV2)
            AGO: AGOS_AAL021W AGOS_AEL305C
            PIC: PICST_44973(ILV2) PICST_80460(ILV6)
            CAL: CaO19_1613(CaO19.1613) CaO19_4650(CaO19.4650)
            CGR: CAGL0H03905g CAGL0K03465g
            SPO: SPBC14C8.04 SPBP35G2.07(ilv1)
            ANI: AN4430.2 AN4956.2
            AFM: AFUA_3G10310 AFUA_4G07210
            AOR: AO090003000571 AO090023000854 AO090166000076
            CNE: CNA02570 CNN01460
            DDI: DDBDRAFT_0184361
            ECO: b0077(ilvI) b0078(ilvH) b3670(ilvN) b3671(ilvB) b3769(ilvM)
                 b4488(ilvG)
            ECJ: JW0076(ilvI) JW0077(ilvH) JW3645(ilvN) JW3646(ilvB)
                 JW3740(ilvG) JW3742(ilvM)
            ECE: Z0087(ilvI) Z0088(ilvH) Z5164(ilvN) Z5165(ilvB) Z5279(ilvG)
                 Z5280(ilvM)
            ECS: ECs0081 ECs0082 ECs4611 ECs4612 ECs4702 ECs4703
            ECC: c0095(ilvI) c0096(ilvH) c4595(ilvN) c4596(ilvB) c4690(ilvG)
                 c4691(ilvM)
            ECI: UTI89_C0085(ilvI) UTI89_C0086(ilvH) UTI89_C4226(ilvN)
                 UTI89_C4227(ilvB) UTI89_C4324(ilvG) UTI89_C4325(ilvM)
            ECP: ECP_0079 ECP_0080 ECP_3877 ECP_3878 ECP_3962
            ECV: APECO1_1906(ilvH) APECO1_1907(ilvI) APECO1_2702(ilvM)
                 APECO1_2703(ilvG) APECO1_2781(ilvB) APECO1_2782(ilvN)
            ECW: EcE24377A_0079(ilvI) EcE24377A_0080(ilvH)
                 EcE24377A_4179(ilvN) EcE24377A_4180(ilvB) EcE24377A_4279(ilvG)
                 EcE24377A_4280(ilvM)
            ECX: EcHS_A0083 EcHS_A0084 EcHS_A3883 EcHS_A3884 EcHS_A3985
                 EcHS_A3986
            STY: STY0135(ilvI) STY0136(ilvH) STY3655(ilvM) STY3656(ilvG)
                 STY3986(ilvB) STY3987(ilvN)
            STT: t0120(ilvI) t0121(ilvH) t3396(ilvM) t3397(ilvG) t3722(ilvB)
                 t3723(ilvN)
            SPT: SPA0118(ilvI) SPA0119(ilvH) SPA3645(ilvN) SPA3646(ilvB)
                 SPA3740(ilvG) SPA3741(ilvM)
            SEC: SC0113(ilvI) SC0114(ilvH) SC3715(ilvN) SC3716(ilvB)
                 SC3807(ilvM)
            STM: STM0116(ilvI) STM0117(ilvH) STM3795(ilvN) STM3796(ilvB)
                 STM3901(ilvG) STM3902(ilvM)
            YPE: YPO0539(ilvI) YPO0540(ilvH) YPO2293(ilvB) YPO2294(ilvN)
                 YPO3900(ilvM) YPO3901(ilvG)
            YPK: y0336(ilvG) y2126(ilvB) y2127(ilvN) y3639(ilvH) y3640(ilvI)
            YPM: YP_2079(ilvB2) YP_2080(ilvN) YP_3147(ilvG) YP_3148(ilvM)
                 YP_3646(ilvI) YP_3647(ilvH)
            YPA: YPA_0121 YPA_0122 YPA_1642 YPA_1643 YPA_3559 YPA_3560
            YPN: YPN_0066 YPN_0067 YPN_0407 YPN_0408 YPN_1755
            YPP: YPDSF_3102 YPDSF_3513
            YPS: YPTB0134(ilvG) YPTB0135(ilvM) YPTB0675(ilvI) YPTB0676(ilvH)
                 YPTB2216(ilvB) YPTB2217(ilvN)
            YPI: YpsIP31758_0154(ilvB3) YpsIP31758_0155(ilvM)
                 YpsIP31758_1839(ilvB2) YpsIP31758_3400(ilvN)
                 YpsIP31758_3401(ilvB1)
            YEN: YE0148(ilvG) YE0658(ilvI) YE4017(budB)
            SFL: SF0072(ilvI) SF0073(ilvH) SF3790(ilvB) SF3791(ilvN)
                 SF3843(ilvG) SF3844(ilvM)
            SFX: S0074(ilvI) S0075(ilvH) S3915(ilvM) S3917(ilvG) S3977(ilvN)
                 S3978(ilvB)
            SFV: SFV_0068(ilvI) SFV_0069(ilvH) SFV_3733(ilvM) SFV_3734(ilvG)
                 SFV_3838(ilvB) SFV_3839(ilvN)
            SSN: SSON_0084(ilvI) SSON_0085(ilvH) SSON_3624(ilvN)
                 SSON_3625(ilvB) SSON_3939(ilvG) SSON_3940(ilvM)
            SBO: SBO_0065(ilvI) SBO_0066(ilvH) SBO_3698(ilvB) SBO_3699(ilvN)
                 SBO_3779(ilvG) SBO_3780(ilvM)
            SDY: SDY_0107(ilvI) SDY_0108(ilvH) SDY_3979(ilvM) SDY_3980(ilvG)
                 SDY_4154(ilvN) SDY_4155(ilvB)
            ECA: ECA0741(budB) ECA1426 ECA3828(ilvH) ECA3829(ilvI)
                 ECA3848(ilvB) ECA3849(ilvN) ECA4228(ilvM) ECA4229(ilvG)
            PLU: plu3665(ilvH) plu3666(ilvI) plu4684(ilvM) plu4685(ilvG)
            BUC: BU225(ilvH) BU226(ilvI)
            BAS: BUsg219(ilvH) BUsg220(ilvI)
            BAB: bbp207(ilvH) bbp208(ilvI)
            BCC: BCc_138(ilvH) BCc_139(ilvI)
            SGL: SG2396 SG2397
            SPE: Spro_0748
            BFL: Bfl592(ilvM) Bfl593(ilvG)
            BPN: BPEN_613(ilvM) BPEN_614(ilvG)
            HIN: HI0737(ilvG) HI1584(ilvH) HI1585(ilvI)
            HIT: NTHI0894(ilvG) NTHI1468(ilvI) NTHI1469(ilvH)
            HIP: CGSHiEE_05520(ilvH) CGSHiEE_05540
            HIQ: CGSHiGG_10210(ilvH)
            HSO: HS_0147(ilvG) HS_0148(ilvM)
            PMU: PM0869(ilvH) PM0870(ilvI) PM1627(ilvM) PM1628(ilvG)
            MSU: MS1318(ilvH) MS1319(ilvB) MS2222(ilvH) MS2223(ilvB)
            APL: APL_0098(ilvM) APL_0099(ilvG) APL_0727(ilvI) APL_0728(ilvH)
            XFA: XF1820 XF1821
            XFT: PD1044(ilvG) PD1045(ilvM)
            XCC: XCC3324(ilvG) XCC3325(ilvM)
            XCB: XC_0839 XC_0840
            XCV: XCV3580(ilvG) XCV3581
            XAC: XAC3452(ilvG) XAC3453(ilvM)
            XOO: XOO0944(ilvM) XOO0945(ilvG)
            XOM: XOO_0863(XOO0863) XOO_0864(XOO0864)
            VCH: VC0030 VC0031 VC1590 VC2482 VC2483
            VCO: VC0395_A1192(alsS) VC0395_A2058(ilvH) VC0395_A2059(ilvI)
                 VC0395_A2488(ilvG) VC0395_A2489(ilvM)
            VVU: VV1_0647 VV1_0648 VV1_1031 VV1_1032
            VVY: VV0495 VV0496 VV3240 VV3241
            VPA: VP0352 VP0353 VP3058 VP3059
            VFI: VF0185 VF2262 VF2263 VF2556 VF2557
            PPR: PBPRA0425(ilvI) PBPRA0426 PBPRA3593(ilvG_1)
            PAE: PA1417 PA2035 PA4180 PA4695(ilvH) PA4696(ilvI)
            PAU: PA14_09820 PA14_38200(ilvG) PA14_62150(ilvH) PA14_62160(ilvI)
            PAP: PSPA7_5409(ilvN) PSPA7_5410(ilvB)
            PPU: PP_1157 PP_1394 PP_3365 PP_4679(ilvN) PP_4680(ilvB)
            PST: PSPTO_0981(ilvB) PSPTO_0982(ilvN)
            PSB: Psyr_0846 Psyr_0847
            PSP: PSPPH_0872(ilvB) PSPPH_0873(ilvN)
            PFL: PFL_3478(ilvB-1) PFL_4812 PFL_5018 PFL_5097(ilvB)
                 PFL_5254(ilvN) PFL_5255(ilvB)
            PFO: Pfl_4471 Pfl_4787 Pfl_4788
            PEN: PSEEN1319 PSEEN4350 PSEEN4710(ilvH) PSEEN4711(ilvI)
            PAR: Psyc_0527(ilvB) Psyc_0528(ilvH)
            PCR: Pcryo_0522 Pcryo_0523
            ACI: ACIAD0999 ACIAD3103(ilvH) ACIAD3104(ilvI)
            ACB: A1S_0543
            SON: SO_2278(ilvH) SO_2279(ilvI) SO_3262(ilvB) SO_4346(ilvM)
                 SO_4347(ilvG)
            SDN: Sden_2122 Sden_2123 Sden_3413 Sden_3414
            SFR: Sfri_0422 Sfri_0423 Sfri_1627 Sfri_1628
            SAZ: Sama_2018 Sama_3281
            SBL: Sbal_2386
            SLO: Shew_0289 Shew_1776
            SHE: Shewmr4_0362 Shewmr4_0363 Shewmr4_1749 Shewmr4_1750
            SHM: Shewmr7_1829 Shewmr7_1830 Shewmr7_3663 Shewmr7_3664
            SHN: Shewana3_0356 Shewana3_0357 Shewana3_2269 Shewana3_2270
            SHW: Sputw3181_1873
            ILO: IL2585(ilvB)
            CPS: CPS_3236(ilvI) CPS_3237(ilvH) CPS_3360 CPS_4843(ilvG)
                 CPS_4844(ilvM)
            PHA: PSHAa2770(ilvM) PSHAa2771(ilvG) PSHAb0463(ilvH)
                 PSHAb0464(ilvI)
            PAT: Patl_0624 Patl_0625 Patl_3850
            SDE: Sde_2543
            PIN: Ping_3430
            MAQ: Maqu_0882
            MCA: MCA1837(ilvK) MCA2270(ilvB) MCA2271(ilvN)
            FTU: FTT0642(ilvH)
            FTF: FTF0642(ilvH)
            FTL: FTL_0915
            FTH: FTH_0895(ilvH)
            FTA: FTA_0964
            FTN: FTN_1041(ilvN) FTN_1042(ilvB)
            TCX: Tcr_0051 Tcr_0634 Tcr_0635 Tcr_2032
            NOC: Noc_1266 Noc_2519 Noc_2520
            AEH: Mlg_0543 Mlg_2038
            HCH: HCH_02178 HCH_05915(ilvN) HCH_05916(ilvB1) HCH_06858(ilvB2)
                 HCH_06859(ilvM)
            CSA: Csal_0501 Csal_0502 Csal_0538
            ABO: ABO_0481(ilvB-1) ABO_0482(ilvN) ABO_0704(ilvB-2)
            AHA: AHA_0887(ilvB-1) AHA_0889(ilvN) AHA_1126(alsS)
                 AHA_4204(ilvB-2)
            CRP: CRP_127
            RMA: Rmag_0445 Rmag_0446
            VOK: COSY_0411(ilvI) COSY_0412(ilvH)
            NME: NMB1576 NMB1577
            NMA: NMA1765(ilvH) NMA1766(ilvI)
            NMC: NMC1496(ilvH) NMC1497(ilvI)
            NGO: NGO1235(ilvH) NGO1236(ilvI)
            CVI: CV_0586(ilvI) CV_0587(ilvH) CV_3889(ilvB)
            RSO: RSc1353(ilvG) RSc2076(ilvH) RSc2077(ilvI)
            REU: Reut_A0947 Reut_A0948 Reut_A1497 Reut_B3510 Reut_B4490
            REH: H16_A1035(ilvB) H16_A1036(ilvH) H16_A2231 H16_B0313 H16_B0735
                 H16_B2452
            RME: Rmet_0911 Rmet_0912 Rmet_1620 Rmet_1636 Rmet_1895 Rmet_3896
                 Rmet_4360 Rmet_5039
            BMA: BMA1847(ilvN) BMA1848(ilvB) BMA2989 BMAA0212
            BMV: BMASAVP1_A1113(ilvB) BMASAVP1_A1114(ilvN)
            BML: BMA10299_A0752(ilvN) BMA10299_A0753(ilvB)
            BMN: BMA10247_0396(ilvB) BMA10247_0397(ilvN)
            BXE: Bxe_A0051 Bxe_A3230 Bxe_A3231 Bxe_A3298 Bxe_B0691(xsc)
                 Bxe_B1115 Bxe_C0294 Bxe_C0664 Bxe_C1114 Bxe_C1163
            BUR: Bcep18194_A3318 Bcep18194_A4566 Bcep18194_A5591
                 Bcep18194_A5592 Bcep18194_B1111 Bcep18194_B2312
                 Bcep18194_C6721
            BCN: Bcen_1653 Bcen_1654
            BCH: Bcen2424_0138 Bcen2424_2264 Bcen2424_2265 Bcen2424_3782
                 Bcen2424_4703 Bcen2424_6310
            BAM: Bamb_0128 Bamb_2302 Bamb_2303
            BPS: BPSL1196(ilvI) BPSL1197(ilvH) BPSL3366(ilvG) BPSS0414
                 BPSS1879
            BPM: BURPS1710b_0133(ilvG) BURPS1710b_1419(ilvB)
                 BURPS1710b_1420(ilvN) BURPS1710b_A0974 BURPS1710b_A1956
                 BURPS1710b_A2500
            BPL: BURPS1106A_1281(ilvB) BURPS1106A_1282(ilvN) BURPS1106A_A0561
                 BURPS1106A_A1240(ilvB)
            BPD: BURPS668_1274(ilvB) BURPS668_1275(ilvN) BURPS668_A0654
                 BURPS668_A1313(ilvB)
            BTE: BTH_I1045(ilvB) BTH_I1046(ilvN) BTH_I3250 BTH_II0497
                 BTH_II1495
            PNU: Pnuc_1063
            BPE: BP0467 BP0773 BP0784(ilvB) BP0789(ilvI) BP0790(ilvH) BP0860
                 BP1535 BP1538(ilvG) BP1860(ilvG) BP3453
            BPA: BPP0334 BPP0346(ilvB) BPP0829 BPP1210(ilvG) BPP1571(ilvG)
                 BPP2813(ilvB) BPP3371 BPP3436(ilvH) BPP3437(ilvI) BPP4381
            BBR: BB0349(ilvB) BB0923 BB1424 BB1427(ilvG) BB2649(ilvG)
                 BB3134(ilvB) BB3822 BB3886(ilvH) BB3887(ilvI) BB4967
            RFR: Rfer_0882 Rfer_2478 Rfer_3322 Rfer_3323 Rfer_3509
            POL: Bpro_2317 Bpro_2318 Bpro_2817
            PNA: Pnap_1717
            AAV: Aave_3112
            AJS: Ajs_1769
            VEI: Veis_1745
            MPT: Mpe_A1557 Mpe_A2104 Mpe_A2105 Mpe_B0544
            HAR: HEAR1237(ilvI) HEAR1238(ilvH)
            MMS: mma_2149 mma_2150
            NEU: NE1324(ilvH) NE1325(ilvI)
            NET: Neut_1261 Neut_1262
            NMU: Nmul_A0473 Nmul_A0474
            EBA: ebA4751(ilvB) ebA7130(ilvI) ebA7132(ilvH) ebB162(ilvN)
            AZO: azo1034(ilvB) azo1035(ilvN) azo2474(alsS) azo3154(ilvI)
                 azo3155(ilvH)
            DAR: Daro_1619 Daro_1620 Daro_3074 Daro_3075
            TBD: Tbd_1876 Tbd_1990 Tbd_1991
            MFA: Mfla_2119 Mfla_2120
            HHE: HH0863(ilvH) HH0864(ilvI)
            WSU: WS0102(ilvH) WS0103(ilvI)
            TDN: Tmden_1140 Tmden_1141
            CJE: Cj0574(ilvI) Cj0575(ilvH)
            CJR: CJE0677(ilvB) CJE0678(ilvH)
            CJJ: CJJ81176_0602(ilvB) CJJ81176_0603(ilvH)
            CJU: C8J_0536(ilvB) C8J_0537(ilvH)
            CJD: JJD26997_1095(ilvH) JJD26997_1096(ilvB)
            CFF: CFF8240_0816(ilvB) CFF8240_0817(ilvN)
            CCV: CCV52592_1428(ilvB) CCV52592_1429(ilvN)
            CHA: CHAB381_1165(ilvB) CHAB381_1166(ilvN)
            CCO: CCC13826_0139(ilvN) CCC13826_0140(ilvB) CCC13826_1162(ilvH)
            ABU: Abu_1156(ilvI) Abu_1157(ilvH) Abu_2149(ilvB)
            NIS: NIS_0810(ilvI) NIS_0811(ilvH)
            SUN: SUN_1822(ilvH) SUN_1823(ilvI) SUN_2140
            GSU: GSU1910(ilvN) GSU1911(ilvB)
            GME: Gmet_1260 Gmet_1261
            PCA: Pcar_1121 Pcar_1909 Pcar_1910
            DVU: DVU0360(ilvB-1) DVU0361 DVU0626(ilvN-1) DVU1376(ilvB-2)
                 DVU1377(ilvN-2) DVU3293
            DVL: Dvul_1692 Dvul_2624
            DDE: Dde_0398 Dde_0399 Dde_2167 Dde_2168 Dde_3130
            LIP: LI0106(ilv)
            DPS: DP2769(ilvI) DP2770
            ADE: Adeh_1015 Adeh_1977 Adeh_1978
            MXA: MXAN_2843(alsS)
            SAT: SYN_01196 SYN_01710 SYN_01711 SYN_01712 SYN_01713 SYN_01965
            SFU: Sfum_0296 Sfum_2980 Sfum_2981 Sfum_2982 Sfum_2983 Sfum_3023
                 Sfum_3024 Sfum_3025
            PUB: SAR11_0002(ilvH) SAR11_0003(ilvB) SAR11_0527
            MLO: mll1432 mll1433 mll3567 mlr1615 mlr5207 mlr6648 mlr7164
            MES: Meso_1488 Meso_1489 Meso_2037 Meso_3590
            SME: SMa0958(atrC) SMa2211(ilvB2) SMc01430(ilvH) SMc01431(ilvI)
                 SMc02263(ilvB1) SMc04455(ilvG)
            ATU: Atu2035(ilvH) Atu2036(ilvI) Atu2128(iivG) Atu5123(atrC)
            ATC: AGR_C_3688 AGR_C_3689 AGR_C_3859 AGR_pAT_179
            RET: RHE_CH02789(ilvH) RHE_CH02790(ilvI) RHE_CH02878(ilvG)
                 RHE_PF00274(ilvB)
            RLE: RL3244(ilvH) RL3245(ilvI) RL3338(ilvG) pRL100055
                 pRL120271(budB)
            BME: BMEI0617 BMEI0618 BMEII0351
            BMF: BAB1_1407(ilvN) BAB1_1408(ilvB) BAB2_0289
            BMS: BR1388(ilvN) BR1389(ilvB) BRA0945
            BMB: BruAb1_1384(ilvN) BruAb1_1385(ilvB) BruAb2_0288
            BOV: BOV_1345(ilvN) BOV_1346(ilvB)
            BJA: bll2965 bll6501(ilvH) bll6503(ilvI) bll6813(iivG) bll7231
                 blr4023
            BRA: BRADO1717 BRADO2591 BRADO4456 BRADO5562(ilvH) BRADO5564(ilvI)
            BBT: BBta_1253 BBta_2028 BBta_2937 BBta_4676 BBta_6085(ilvH)
                 BBta_6087(ilvI)
            RPA: RPA1618(ilvX) RPA2001 RPA2031(ilvI) RPA2032(ilvH) RPA2326
                 RPA3763(ilvB) RPA3917 RPA4054
            RPB: RPB_0998 RPB_1703 RPB_3134 RPB_3344 RPB_3345 RPB_3802
                 RPB_3930
            RPC: RPC_1693 RPC_2090 RPC_3253 RPC_3255 RPC_3491 RPC_4260
            RPD: RPD_1101 RPD_2098 RPD_2100 RPD_3594 RPD_3688
            RPE: RPE_1801 RPE_2004 RPE_2187 RPE_2189 RPE_4300
            NWI: Nwi_2342 Nwi_2343 Nwi_3016
            NHA: Nham_2721 Nham_2722
            BHE: BH10920(ilvB)
            CCR: CC_0393 CC_2100 CC_2101
            SIL: SPO2578(ilvB) SPO2579(ilvN) SPO2883 SPO2885 SPOA0065 SPOA0418
            SIT: TM1040_0874 TM1040_0875 TM1040_1530 TM1040_1932 TM1040_3213
            RSP: RSP_2636(ilvH) RSP_2637 RSP_3155 RSP_3284(iolD)
                 RSP_4011(ilvB2)
            JAN: Jann_0137 Jann_1893 Jann_1897 Jann_3204
            RDE: RD1_1674(alsS) RD1_1943(ilvB) RD1_2449(ilvB) RD1_2812(ilvB)
                 RD1_2813(ilvN)
            MMR: Mmar10_0289
            HNE: HNE_0449(ilvN) HNE_0451(ilvB)
            ZMO: ZMO0687(budB) ZMO1139(ilvI) ZMO1140(ilvH)
            NAR: Saro_2261 Saro_2262
            SAL: Sala_1470 Sala_1471
            ELI: ELI_03930 ELI_04475 ELI_05510 ELI_05515
            GOX: GOX1087 GOX1088
            GBE: GbCGDNIH1_1480 GbCGDNIH1_1481
            RRU: Rru_A0284 Rru_A0467 Rru_A0468
            MAG: amb0792 amb2550 amb3507 amb3508
            MGM: Mmc1_0898 Mmc1_0899
            ABA: Acid345_2843 Acid345_3107 Acid345_3108
            SUS: Acid_0180
            BSU: BG10471(alsS) BG10670(ilvB) BG10671(ilvN)
            BHA: BH3060(ilvN) BH3061 BH3873
            BAN: BA0866(alsS) BA1417(ilvB-1) BA1418(ilvN) BA1850(ilvB-2)
            BAR: GBAA0866(alsS) GBAA1417(ilvB-1) GBAA1418(ilvN)
                 GBAA1850(ilvB-2)
            BAA: BA_1937 BA_1938 BA_2353 BA_2354
            BAT: BAS0823 BAS1308 BAS1309 BAS1714 BAS1715
            BCE: BC0883 BC1398 BC1777
            BCA: BCE_0956(alsS) BCE_1517(ilvB) BCE_1518(ilvN) BCE_1934(ilvB)
                 BCE_1935
            BCZ: BCZK0772(alsS) BCZK1282(ilvB) BCZK1283(ilvH) BCZK1666(ilvB)
                 BCZK1667
            BTK: BT9727_0771(alsS) BT9727_1281(alsS) BT9727_1282(ilvH)
                 BT9727_1691(ilvB) BT9727_1692
            BTL: BALH_1252(alsS) BALH_1253 BALH_1624(ilvB) BALH_1625
            BLI: BL00608(ilvB) BL00609(ilvH) BL02480(alsS)
            BLD: BLi02960(ilvH) BLi02961(ilvB) BLi03848(alsS)
            BCL: ABC2009 ABC2644(ilvN) ABC2645(ilvB)
            BAY: RBAM_033170
            BPU: BPUM_2471 BPUM_2472 BPUM_3271
            OIH: OB2281 OB2622(ilvN) OB2623(ilvB) OB3237
            GKA: GK0373 GK2660 GK2661
            SAU: SA1859(ilvB) SA1860 SA2008(alsS)
            SAV: SAV2054(ilvB) SAV2055 SAV2207(alsS)
            SAM: MW1978(ilvB) MW1979 MW2132(alsS)
            SAR: SAR2141(ilvB) SAR2297
            SAS: SAS1959 SAS1960 SAS2106
            SAC: SACOL2043(ilvB) SACOL2044 SACOL2199(budB)
            SAB: SAB1939(ilvB) SAB1940(ilvH) SAB2087c
            SAA: SAUSA300_2007(ilvB) SAUSA300_2008(ilvN) SAUSA300_2166(alsS)
            SAO: SAOUHSC_02282 SAOUHSC_02283 SAOUHSC_02468
            SEP: SE1655 SE1656 SE2144
            SER: SERP1666(ilvB) SERP1667 SERP2155(budB)
            SHA: SH0461(alsS) SH0978 SH0979(ilvB)
            SSP: SSP0082 SSP0823 SSP0824
            LMO: lmo1984(ilvB) lmo1985(ilvN) lmo2006(alsS)
            LMF: LMOf2365_2007(ilvB) LMOf2365_2008(ilvN) LMOf2365_2030(alsS)
            LIN: lin2091(ilvB) lin2092(ilvN) lin2114(alsS)
            LWE: lwe2003(ilvB) lwe2004(ilvN) lwe2026(alsS)
            LLA: L0078(ilvB) L0079(ilvN) L210(als)
            LLC: LACR_1310 LACR_1311 LACR_1349
            LLM: llmg_1278(ilvN) llmg_1279(ilvB) llmg_1309(als)
            SPN: SP_0445 SP_0446
            SPR: spr0401(ilvB) spr0402(ilvN)
            SPD: SPD_0404(ilvB) SPD_0405(ilvN)
            SAG: SAG1192(ilvK)
            SAN: gbs1265
            SAK: SAK_1279(budB)
            SMU: SMU.1452(alsS) SMU.231(ilvB) SMU.232(ilvH)
            STC: str0923(als) str1872(ilvN) str1873(ilvB)
            STL: stu0923(als) stu1872(ilvN) stu1873(ilvB)
            STE: STER_1849
            SSA: SSA_1969(ilvN) SSA_1970(ilvB)
            SGO: SGO_0526(ilvB) SGO_0527(ilvN)
            LPL: lp_1005(als)
            LJO: LJ1124
            LSA: LSA0982(als)
            LSL: LSL_0186
            LBR: LVIS_0491
            LCA: LSEI_1841
            EFA: EF1213
            OOE: OEOE_1703 OEOE_1763
            STH: STH1014 STH2684 STH2689
            CAC: CAC3169(ilvB) CAC3176(ilvN) CAC3652(alsS)
            CNO: NT01CX_2029(ilvB)
            CTH: Cthe_2714
            CBE: Cbei_0217
            CKL: CKL_1081(ilvB1) CKL_1617(ilvH) CKL_1618(ilvI) CKL_2103(ilvB2)
            CHY: CHY_0517(ilvB1) CHY_0518(ilvN1) CHY_0520(ilvB2)
                 CHY_1594(ilvN2)
            DSY: DSY1366 DSY1367 DSY2457 DSY2458
            DRM: Dred_0281 Dred_0284
            SWO: Swol_2145 Swol_2146
            TTE: TTE0014(ilvH) TTE0021(ilvB)
            MTA: Moth_2256 Moth_2257 Moth_2258
            MTU: Rv1820(ilvG) Rv3002c(ilvN) Rv3003c(ilvB1) Rv3470c(ilvB2)
                 Rv3509c(ilvX)
            MTC: MT1868 MT3082(ilvN) MT3083(ilvB) MT3576
            MBO: Mb1851(ilvG) Mb3027c(ilvN) Mb3028c(ilvB1) Mb3499c(ilvB2)
                 Mb3539c(ilvX)
            MBB: BCG_1855(ilvG) BCG_3024c(ilvN) BCG_3025c(ilvB1)
                 BCG_3535c(ilvB2) BCG_3573c(ilvX)
            MLE: ML0354(ilvX) ML1695(ilvN) ML1696(ilvB) ML2083(ilvG)
            MPA: MAP0553(ilvX) MAP1532 MAP1533 MAP3037c(ilvN) MAP3038c(ilvB_1)
                 MAP3675(ilvB_2)
            MAV: MAV_3851(ilvN)
            MSM: MSMEG_2372(ilvB) MSMEG_2373(ilvN) MSMEG_4348 MSMEG_4460
            MMC: Mmcs_1906 Mmcs_1907
            CGL: NCgl1222(cgl1271) NCgl1223(cgl1272)
            CGB: cg0202(iolD) cg1435(ilvB) cg1436(ilvN)
            CEF: CE1365 CE1366
            CDI: DIP1098(ilvB) DIP1099(ilvH)
            CJK: jk1299(ilvN) jk1300(ilvB)
            NFA: nfa30060(ilvB2) nfa42310(ilvN) nfa42320(ilvB)
            RHA: RHA1_ro01259(ilvB1) RHA1_ro01353 RHA1_ro03582(xsc)
                 RHA1_ro03980 RHA1_ro04554(ilvB2) RHA1_ro04562(ilvB3)
                 RHA1_ro05712(ilvB4) RHA1_ro06486(ilvB5) RHA1_ro06487(ilvH)
                 RHA1_ro08312(ilvB6)
            SCO: SCO2769(SCC57A.40c) SCO5512(ilvB) SCO5513(ilvN) SCO6584
            SMA: SAV1819(ilvB3) SAV2732(ilvN) SAV2733(ilvB1) SAV5286(ilvB4)
            TWH: TWT205(ilvB) TWT206(ilvH)
            TWS: TW566(ilvN) TW567(ilvB)
            LXX: Lxx13180(ilvN) Lxx13200(ilvB)
            CMI: CMM_0682(ilvG) CMM_1094(ilvB) CMM_1095(ilvH)
            AAU: AAur_2508(ilvN) AAur_2509(ilvB)
            PAC: PPA1373
            TFU: Tfu_0553 Tfu_0611 Tfu_0612
            FRA: Francci3_3639 Francci3_3640
            FAL: FRAAL5850(ilvH) FRAAL5851(ilvI)
            ACE: Acel_0706 Acel_0707
            SEN: SACE_0604(ilvB) SACE_3465(ilvB1) SACE_3908(ilvX)
                 SACE_4565(ilvB1) SACE_5632(ilvB4) SACE_6158(ilvN)
                 SACE_6159(ilvB)
            STP: Strop_1234
            BLO: BL0296(ilvB) BL0297(ilvN)
            BAD: BAD_0220(ilvN) BAD_0221(ilvB1)
            RXY: Rxyl_3125
            RBA: RB12905 RB8231(ilvH) RB9871(ilvN)
            LIL: LA0863(ilvB1) LA0864(ilvA) LA2569(ilvH) LA2570(ilvB2)
            LIC: LIC11409 LIC11410(ilvH) LIC12764(ilvB)
            LBJ: LBJ_1076 LBJ_1077(ilvH)
            LBL: LBL_1133 LBL_1134(ilvH)
            SYN: sll0065(ilvN) sll1981(ilvB) slr2088(ilvG)
            SYW: SYNW0680(ilvN) SYNW1746(ilvB)
            SYC: syc1366_c(ilvB) syc1672_c(ilvN)
            SYF: Synpcc7942_0139 Synpcc7942_2434
            SYD: Syncc9605_0520 Syncc9605_0717 Syncc9605_1989
            SYE: Syncc9902_0671 Syncc9902_1642
            SYG: sync_0900(ilvN) sync_1999(ilvB)
            SYR: SynRCC307_0853(ilvB) SynRCC307_1692(ilvH)
            SYX: SynWH7803_0645(ilvB) SynWH7803_1644(ilvH)
            CYA: CYA_1964 CYA_2073(ilvB) CYA_2130(ilvN)
            CYB: CYB_0648(ilvB) CYB_0971(ilvN) CYB_2144
            TEL: tll0880(ilvN) tll1824(ilvB) tlr1296(ilvG)
            GVI: gll1136(ilvN) gll2804(ilvB) glr3279(ilvG)
            ANA: all3555(ilvB) all4613(ilvG) alr4627(ilvN)
            AVA: Ava_2035 Ava_2757 Ava_3533
            PMA: Pro0526(ilvB) Pro1251(ilvH)
            PMM: PMM0526(ilvH) PMM1154(ilvH)
            PMT: PMT1176(ilvN) PMT1239(ilvB)
            PMN: PMN2A_0764 PMN2A_1858
            PMI: PMT9312_0526 PMT9312_1253
            PMB: A9601_05821(ilvB) A9601_13311(ilvN)
            PMC: P9515_05901(ilvB) P9515_13211(ilvN)
            PMF: P9303_01441 P9303_07681(ilvB) P9303_08471(ilvN)
            PMG: P9301_05521(ilvB) P9301_13461(ilvN)
            PMH: P9215_06071 P9215_13601
            PME: NATL1_05831(ilvB) NATL1_16041(ilvN)
            TER: Tery_1850 Tery_1928 Tery_2843
            BTH: BT_2076 BT_2077
            BFR: BF3761 BF3762
            BFS: BF3549 BF3550(ilvB)
            SRU: SRU_2145(ilvB)
            CHU: CHU_3746(ilvB)
            GFO: GFO_2111(ilvH) GFO_2112(ilvB)
            FJO: Fjoh_2861
            FPS: FP0447(ilvH) FP0448(ilvB)
            CTE: CT0617(ilvN) CT0618(ilvB)
            CCH: Cag_1903 Cag_1905
            PLT: Plut_0605 Plut_0608
            DET: DET0832(ilvN) DET0833(ilvB)
            DEH: cbdb_A812(ilvN) cbdb_A813(ilvB)
            DRA: DR_1516 DR_1517(ilvN)
            DGE: Dgeo_0601 Dgeo_0602
            TTH: TTC0851 TTC0852
            TTJ: TTHA1212 TTHA1213
            AAE: aq_1851(ilvH) aq_451(ilvB)
            TMA: TM0548 TM0549
            MJA: MJ0161(ilvN) MJ0277(ilvB) MJ0663
            MMP: MMP0142 MMP0650(ilvB) MMP0651(ilvN)
            MAC: MA1354 MA1958 MA3791 MA3792 MA3854
            MBA: Mbar_A0218 Mbar_A0219 Mbar_A0428 Mbar_A2541
            MMA: MM_0669 MM_0670 MM_0677 MM_2340 MM_2841
            MBU: Mbur_0174 Mbur_0208 Mbur_0709 Mbur_0710
            MTP: Mthe_0110
            MHU: Mhun_1241 Mhun_1242
            MLA: Mlab_0605
            MEM: Memar_1070
            MBN: Mboo_1443
            MTH: MTH1443 MTH1444 MTH1602 MTH476
            MST: Msp_0025(ilvH1) Msp_0026(ilvB1) Msp_0028(ilvH2)
                 Msp_0029(ilvB2) Msp_0605
            MSI: Msm_1224 Msm_1225
            MKA: MK0531(ilvB_2) MK0545(ilvH) MK1236
            AFU: AF1672 AF1719(ilvN) AF1720(ilvB-1) AF1780(ilvB-2)
                 AF2015(ilvB-3) AF2100(ilvB-4)
            HMA: rrnAC0134(ilvB1) rrnAC0330(ilvB2) rrnAC0331(ilvN)
                 rrnB0209(ilvB3)
            HWA: HQ2702A(ilvB) HQ2703A(ilvN)
            NPH: NP1904A(ilvB_2) NP2200A(ilvN) NP2202A(ilvB)
            TAC: Ta0691
            PTO: PTO1075
            PAB: PAB0888(ilvB)
            PFU: PF0935
            RCI: LRC533(ilvN) LRC534(ilvB)
            APE: APE_2509
            SSO: SSO0579(ilvB-2)
            STO: ST1447
            SAI: Saci_1137 Saci_1561
            PAI: PAE3299 PAE3300(ilvB)
STRUCTURES  PDB: 1T9A  1T9B  1T9C  1T9D  1YBH  1YHY  1YHZ  1YI0  1YI1  1Z8N  
                 2F1F  2FGC  
DBLINKS     IUBMB Enzyme Nomenclature: 2.2.1.6
            ExPASy - ENZYME nomenclature database: 2.2.1.6
            ExplorEnz - The Enzyme Database: 2.2.1.6
            ERGO genome analysis and discovery system: 2.2.1.6
            BRENDA, the Enzyme Database: 2.2.1.6
            CAS: 9027-45-6
///
ENTRY       EC 2.2.1.7                  Enzyme
NAME        1-deoxy-D-xylulose-5-phosphate synthase;
            1-deoxy-D-xylulose-5-phosphate pyruvate-lyase (carboxylating);
            DXP-synthase
CLASS       Transferases;
            Transferring aldehyde or ketonic groups;
            Transketolases and transaldolases
SYSNAME     pyruvate:D-glyceraldehyde-3-phosphate acetaldehydetransferase
            (decarboxylating)
REACTION    pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose
            5-phosphate + CO2 [RN:R05636]
ALL_REAC    R05636
SUBSTRATE   pyruvate [CPD:C00022];
            D-glyceraldehyde 3-phosphate [CPD:C00118]
PRODUCT     1-deoxy-D-xylulose 5-phosphate [CPD:C11437];
            CO2 [CPD:C00011]
COMMENT     Requires thiamine diphosphate. The enzyme forms part of an
            alternative nonmevalonate pathway for terpenoid biosynthesis (for
            diagram, click here).
REFERENCE   1  [PMID:9371765]
  AUTHORS   Sprenger GA, Schorken U, Wiegert T, Grolle S, de Graaf AA, Taylor
            SV, Begley TP, Bringer-Meyer S, Sahm H.
  TITLE     Identification of a thiamin-dependent synthase in Escherichia coli
            required for the formation of the 1-deoxy-D-xylulose 5-phosphate
            precursor to isoprenoids, thiamin, and pyridoxol.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 12857-62.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:10648511]
  AUTHORS   Kuzuyama T, Takagi M, Takahashi S, Seto H.
  TITLE     Cloning and characterization of 1-deoxy-D-xylulose 5-phosphate
            synthase from Streptomyces sp. Strain CL190, which uses both the
            mevalonate and nonmevalonate pathways for isopentenyl diphosphate
            biosynthesis.
  JOURNAL   J. Bacteriol. 182 (2000) 891-7.
  ORGANISM  Streptomyces sp.
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K01662  1-deoxy-D-xylulose-5-phosphate synthase
GENES       ATH: AT3G21500(DXPS1) AT4G15560(CLA1) AT5G11380(DXPS3)
            OSA: 4338768 4340090 4342614
            CME: CMF089C
            PFA: MAL13P1.186
            TAN: TA20470
            TPV: TP01_0516
            ECO: b0420(dxs)
            ECJ: JW0410(dxs)
            ECE: Z0523(dxs)
            ECS: ECs0474
            ECC: c0531(dxs)
            ECI: UTI89_C0443(dxs)
            ECP: ECP_0479
            ECV: APECO1_1590(dxs)
            ECW: EcE24377A_0451(dxs)
            ECX: EcHS_A0491
            STY: STY0461(dxs)
            STT: t2441(dxs)
            SPT: SPA2301(dxs)
            SEC: SC0463(dxs)
            STM: STM0422(dxs)
            YPE: YPO3177(dxs)
            YPK: y1008(dxs)
            YPM: YP_0754(dxs)
            YPA: YPA_2671
            YPN: YPN_0911
            YPP: YPDSF_2812
            YPS: YPTB0939(dxs)
            YPI: YpsIP31758_3112(dxs)
            SFL: SF0357(dxs)
            SFX: S0365(dxs)
            SFV: SFV_0385(dxs)
            SSN: SSON_0397(dxs)
            SBO: SBO_0314(dxs)
            SDY: SDY_0310(dxs)
            ECA: ECA1131(dxs)
            PLU: plu3887(dxs)
            BUC: BU464(dxs)
            BAS: BUsg448(dxs)
            WBR: WGLp144(dxs)
            SGL: SG0656
            KPN: KPN_00372(dxs)
            BFL: Bfl238(dxs)
            BPN: BPEN_244(dxs)
            HIN: HI1439(dxs)
            HIT: NTHI1691(dxs)
            HIP: CGSHiEE_04795
            HIQ: CGSHiGG_01080
            HDU: HD0441(dxs)
            HSO: HS_0905(dxs)
            PMU: PM0532(dxs)
            MSU: MS1059(dxs)
            APL: APL_0207(dxs)
            XFA: XF2249
            XFT: PD1293(dxs)
            XCC: XCC2434(dxs)
            XCB: XC_1678
            XCV: XCV2764(dxs)
            XAC: XAC2565(dxs)
            XOO: XOO2017(dxs)
            XOM: XOO_1900(XOO1900)
            VCH: VC0889
            VVU: VV1_0315
            VVY: VV0868
            VPA: VP0686
            VFI: VF0711
            PPR: PBPRA0805
            PAE: PA4044(dxs)
            PAU: PA14_11550(dxs)
            PAP: PSPA7_1057(dxs)
            PPU: PP_0527(dxs)
            PST: PSPTO_0698(dxs)
            PSB: Psyr_0604
            PSP: PSPPH_0599(dxs)
            PFL: PFL_5510(dxs)
            PFO: Pfl_5007
            PEN: PSEEN0600(dxs)
            PMY: Pmen_3844
            PAR: Psyc_0221(dxs)
            PCR: Pcryo_0245
            ACI: ACIAD3247(dxs)
            SON: SO_1525(dxs)
            SDN: Sden_2571
            SFR: Sfri_2790
            SAZ: Sama_2436
            SBL: Sbal_1357
            SLO: Shew_2771
            SHE: Shewmr4_2731
            SHM: Shewmr7_2804
            SHN: Shewana3_2901
            SHW: Sputw3181_2831
            ILO: IL2138(dxs)
            CPS: CPS_1088(dxs)
            PHA: PSHAa2366(dxs)
            PAT: Patl_1319
            SDE: Sde_3381
            PIN: Ping_2240
            MAQ: Maqu_2438
            MCA: MCA0817(dxs)
            FTU: FTT1018c(dxs)
            FTF: FTF1018c(dxs)
            FTW: FTW_0925(dxs)
            FTL: FTL_1072
            FTH: FTH_1047(dxs)
            FTA: FTA_1131(dxs)
            FTN: FTN_0896(dxs)
            NOC: Noc_1743
            AEH: Mlg_1381
            HCH: HCH_05866(dxs)
            CSA: Csal_0099
            ABO: ABO_2166(dxs)
            AHA: AHA_3321(dxs)
            BCI: BCI_0275(dxs)
            VOK: COSY_0360(dxs)
            NME: NMB1867
            NMA: NMA0589(dxs)
            NMC: NMC0352(dxs)
            NGO: NGO0036
            CVI: CV_2692(dxs)
            RSO: RSc2221(dxs)
            REU: Reut_A0882
            REH: H16_A2732(dxs)
            RME: Rmet_2615
            BMA: BMAA0330(dxs)
            BMV: BMASAVP1_1512(dxs)
            BML: BMA10299_1706(dxs)
            BMN: BMA10247_A0364(dxs)
            BXE: Bxe_B2827
            BUR: Bcep18194_B2211
            BCN: Bcen_4486
            BCH: Bcen2424_3879
            BAM: Bamb_3250
            BPS: BPSS1762(dxs)
            BPM: BURPS1710b_A0842(dxs)
            BPL: BURPS1106A_A2392(dxs)
            BPD: BURPS668_A2534(dxs)
            BTE: BTH_II0614(dxs)
            BPE: BP2798(dxs)
            BPA: BPP2464(dxs)
            BBR: BB1912(dxs)
            RFR: Rfer_2875
            POL: Bpro_1747
            PNA: Pnap_1501
            AJS: Ajs_1038
            MPT: Mpe_A2631
            HAR: HEAR0279(dxs)
            MMS: mma_0331
            NEU: NE1161(dxs)
            NET: Neut_1501
            NMU: Nmul_A0236
            EBA: ebA4439(dxs)
            AZO: azo1198(dxs)
            DAR: Daro_3061
            TBD: Tbd_0879
            MFA: Mfla_2133
            HPY: HP0354(dxs)
            HPJ: jhp0328(dxs)
            HPA: HPAG1_0349
            HHE: HH0608(dxs)
            HAC: Hac_0968(dxs)
            WSU: WS1996
            TDN: Tmden_0475
            CJE: Cj0321(dxs)
            CJR: CJE0366(dxs)
            CJJ: CJJ81176_0343(dxs)
            CJU: C8J_0298(dxs)
            CJD: JJD26997_1642(dxs)
            CFF: CFF8240_0264(dxs)
            CCV: CCV52592_1671(dxs) CCV52592_1722
            CHA: CHAB381_1297(dxs)
            CCO: CCC13826_1594(dxs)
            ABU: Abu_2139(dxs)
            NIS: NIS_0391(dxs)
            SUN: SUN_2055(dxs)
            GSU: GSU0686(dxs-1) GSU1764(dxs-2)
            GME: Gmet_1934 Gmet_2822
            PCA: Pcar_1667
            PPD: Ppro_2403
            DVU: DVU1350(dxs)
            DVL: Dvul_1718
            DDE: Dde_2200
            LIP: LI0408(dsx)
            DPS: DP2700
            ADE: Adeh_1097
            MXA: MXAN_4643(dxs)
            SAT: SYN_02456
            SFU: Sfum_1418
            PUB: SAR11_0611(dxs)
            MLO: mlr7474
            MES: Meso_0735
            SME: SMc00972(dxs)
            ATU: Atu0745(dxs)
            ATC: AGR_C_1351
            RET: RHE_CH00913(dxs)
            RLE: RL0973(dxs)
            BME: BMEI1498
            BMF: BAB1_0462(dxs)
            BMS: BR0436(dxs)
            BMB: BruAb1_0458(dxs)
            BOV: BOV_0443(dxs)
            BJA: bll2651(dxs)
            BRA: BRADO2161(dxs)
            BBT: BBta_2479(dxs)
            RPA: RPA0952(dxs)
            RPB: RPB_4460
            RPC: RPC_1149
            RPD: RPD_4305
            RPE: RPE_1067
            NWI: Nwi_0633
            NHA: Nham_0778
            BHE: BH04350(dxs)
            BQU: BQ03540(dxs)
            BBK: BARBAKC583_0400(dxs)
            CCR: CC_2068
            SIL: SPO0247(dxs)
            SIT: TM1040_2920
            RSP: RSP_0254(dxsA) RSP_1134(dxs)
            JAN: Jann_0088 Jann_0170
            RDE: RD1_0101(dxs) RD1_0548(dxs)
            MMR: Mmar10_0849
            HNE: HNE_1838(dxs)
            ZMO: ZMO1234(dxs) ZMO1598(dxs)
            NAR: Saro_0161
            SAL: Sala_2354
            ELI: ELI_12520
            GOX: GOX0252
            GBE: GbCGDNIH1_0221 GbCGDNIH1_2404
            RRU: Rru_A0054 Rru_A2619
            MAG: amb2904
            MGM: Mmc1_1048
            SUS: Acid_1783
            BSU: BG11715(dxs)
            BHA: BH2779
            BAN: BA4400(dxs)
            BAR: GBAA4400(dxs)
            BAA: BA_4853
            BAT: BAS4081
            BCE: BC4176(dxs)
            BCA: BCE_4249(dxs)
            BCZ: BCZK3930(dxs)
            BTK: BT9727_3919(dxs)
            BTL: BALH_3785(dxs)
            BLI: BL01523(dxs)
            BLD: BLi02598(dxs)
            BCL: ABC2462(dxs)
            BAY: RBAM_022600
            BPU: BPUM_2159
            GKA: GK2392
            GTN: GTNG_2322
            LMO: lmo1365(tktB)
            LMF: LMOf2365_1382(dxs)
            LIN: lin1402(tktB)
            LWE: lwe1380(tktB)
            LLA: L108911(dxsA) L123365(dxsB)
            LLC: LACR_1572 LACR_1843
            LLM: llmg_0749(dxsB)
            SAK: SAK_0263
            LPL: lp_2610(dxs)
            LJO: LJ0406
            LAC: LBA0356
            LSL: LSL_0209(dxs)
            LGA: LGAS_0350
            STH: STH1842
            CAC: CAC2077 CA_P0106(dxs)
            CPE: CPE1819
            CPF: CPF_2073(dxs)
            CPR: CPR_1787(dxs)
            CTC: CTC01575
            CNO: NT01CX_1983
            CTH: Cthe_0828
            CDF: CD1207(dxs)
            CBO: CBO1881(dxs)
            CBA: CLB_1818(dxs)
            CBH: CLC_1825(dxs)
            CBF: CLI_1945(dxs)
            CKL: CKL_1231(dxs)
            CHY: CHY_1985(dxs)
            DSY: DSY2348
            DRM: Dred_1078
            PTH: PTH_1196(dxs)
            SWO: Swol_0582
            CSC: Csac_1853
            TTE: TTE1298(dxs)
            MTA: Moth_1511
            MPE: MYPE730
            MGA: MGA_1268(dxs)
            MTU: Rv2682c(dxs1) Rv3379c(dxs2)
            MTC: MT2756(dxs)
            MBO: Mb2701c(dxs1) Mb3413c(dxs2)
            MLE: ML1038(dxs)
            MPA: MAP2803c(dxs)
            MAV: MAV_3577(dxs)
            MSM: MSMEG_2776(dxs)
            MMC: Mmcs_2208
            CGL: NCgl1827(cgl1902)
            CGB: cg2083(dxs)
            CEF: CE1796
            CDI: DIP1397(dxs)
            CJK: jk1078(dxs)
            NFA: nfa37410(dxs)
            RHA: RHA1_ro06843
            SCO: SCO6013(SC1C3.01) SCO6768(SC6A5.17)
            SMA: SAV1646(dxs1) SAV2244(dxs2)
            TWH: TWT484
            TWS: TW280(Dxs)
            LXX: Lxx10450(dxs)
            CMI: CMM_1660(dxsA)
            AAU: AAur_1790(dxs)
            PAC: PPA1062
            TFU: Tfu_1917
            FRA: Francci3_1326
            FAL: FRAAL2088(dxs)
            SEN: SACE_1815(dxs) SACE_4351
            BLO: BL1132(dxs)
            BAD: BAD_0513(dxs)
            FNU: FN1208 FN1464
            RBA: RB2143(dxs)
            CTR: CT331(dxs)
            CTA: CTA_0359(dxs)
            CMU: TC0608
            CPN: CPn1060(tktB_2)
            CPA: CP0790
            CPJ: CPj1060(tktB_2)
            CPT: CpB1102
            CCA: CCA00304(dxs)
            CAB: CAB301(dxs)
            CFE: CF0699(dxs)
            PCU: pc0619(dxs)
            TPA: TP0824
            TDE: TDE1910(dxs)
            LIL: LA3285(dxs)
            LIC: LIC10863(dxs)
            LBJ: LBJ_0917(dxs)
            LBL: LBL_0932(dxs)
            SYN: sll1945(dxs)
            SYW: SYNW1292(Dxs)
            SYC: syc1087_c(dxs)
            SYF: Synpcc7942_0430
            SYD: Syncc9605_1430
            SYE: Syncc9902_1069
            SYG: sync_1410(dxs)
            SYR: SynRCC307_1390(dxs)
            SYX: SynWH7803_1223(dxs)
            CYA: CYA_1701(dxs)
            CYB: CYB_1983(dxs)
            TEL: tll0623
            GVI: gll0194
            ANA: alr0599
            AVA: Ava_4532
            PMA: Pro0928(dxs)
            PMM: PMM0907(Dxs)
            PMT: PMT0685(dxs)
            PMN: PMN2A_0300
            PMI: PMT9312_0893
            PMB: A9601_09541(dxs)
            PMC: P9515_09901(dxs)
            PMF: P9303_15371(dxs)
            PMG: P9301_09521(dxs)
            PMH: P9215_09851
            PME: NATL1_09721(dxs)
            TER: Tery_3042
            BTH: BT_1403 BT_4099
            BFR: BF0873 BF4306
            BFS: BF0796(dxs) BF4114
            PGI: PG2217(dxs)
            CHU: CHU_3643(dxs)
            GFO: GFO_3470(dxs)
            FPS: FP0279(dxs)
            CTE: CT0337(dxs)
            CPH: Cpha266_0671
            PVI: Cvib_0498
            PLT: Plut_0450
            DET: DET0745(dxs)
            DEH: cbdb_A720(dxs)
            DRA: DR_1475
            DGE: Dgeo_0994
            TTH: TTC1614
            TTJ: TTHA0006
            AAE: aq_881
            TMA: TM1770
STRUCTURES  PDB: 2O1S  2O1X  
DBLINKS     IUBMB Enzyme Nomenclature: 2.2.1.7
            ExPASy - ENZYME nomenclature database: 2.2.1.7
            ExplorEnz - The Enzyme Database: 2.2.1.7
            ERGO genome analysis and discovery system: 2.2.1.7
            BRENDA, the Enzyme Database: 2.2.1.7
            CAS: 202218-79-9
///
ENTRY       EC 2.2.1.8                  Enzyme
NAME        fluorothreonine transaldolase
CLASS       Transferases;
            Transferring aldehyde or ketonic groups;
            Transketolases and transaldolases
SYSNAME     fluoroacetaldehyde:L-threonine aldehydetransferase
REACTION    L-threonine + fluoroacetaldehyde = acetaldehyde +
            4-fluoro-L-threonine [RN:R07247]
ALL_REAC    R07247
SUBSTRATE   L-threonine [CPD:C00188];
            fluoroacetaldehyde [CPD:C15488]
PRODUCT     acetaldehyde [CPD:C00084];
            4-fluoro-L-threonine [CPD:C15533]
COMMENT     A pyridoxal phosphate protein. Can also convert chloroacetaldehyde
            into4-chloro-L-threonine. Unlike EC 2.1.2.1, glycine
            hydroxymethyltransferase, does not use glycine as a substrate.
REFERENCE   1  [PMID:12404452]
  AUTHORS   Murphy CD, O'Hagan D, Schaffrath C.
  TITLE     Identification of a PLP-Dependent Threonine Transaldolase: A Novel
            Enzyme Involved in 4-Fluorothreonine Biosynthesis in Streptomyces
            cattleya This work was supported by the Biotechnological and
            Biological Sciences Research Council and the University of St
            Andrews.
  JOURNAL   Angew. Chem. Int. Ed. Engl. 40 (2001) 4479-4481.
  ORGANISM  Streptomyces cattleya
REFERENCE   2  [PMID:12738270]
  AUTHORS   Murphy CD, Schaffrath C, O'Hagan D.
  TITLE     Fluorinated natural products: the biosynthesis of fluoroacetate and
            4-fluorothreonine in Streptomyces cattleya.
  JOURNAL   Chemosphere. 52 (2003) 455-61.
  ORGANISM  Streptomyces cattleya
DBLINKS     IUBMB Enzyme Nomenclature: 2.2.1.8
            ExPASy - ENZYME nomenclature database: 2.2.1.8
            ExplorEnz - The Enzyme Database: 2.2.1.8
            ERGO genome analysis and discovery system: 2.2.1.8
            BRENDA, the Enzyme Database: 2.2.1.8
///
ENTRY       EC 2.3.1.1                  Enzyme
NAME        amino-acid N-acetyltransferase;
            N-acetylglutamate synthase;
            AGAS;
            acetylglutamate acetylglutamate synthetase;
            acetylglutamic synthetase;
            amino acid acetyltransferase;
            N-acetyl-L-glutamate synthetase;
            N-acetylglutamate synthetase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:L-glutamate N-acetyltransferase
REACTION    acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate [RN:R00259]
ALL_REAC    R00259
SUBSTRATE   acetyl-CoA [CPD:C00024];
            L-glutamate [CPD:C00025]
PRODUCT     CoA [CPD:C00010];
            N-acetyl-L-glutamate [CPD:C00624]
COMMENT     Also acts with L-aspartate and, more slowly, with some other amino
            acids.
REFERENCE   1
  AUTHORS   Maas, W.K., Novelli, G.D. and Lipmann, F.
  TITLE     Acetylation of glutamic acid by extracts of Escherichia coli.
  JOURNAL   Proc. Natl. Acad. Sci. USA 39 (1953) 1004-1008.
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K00618  amino-acid N-acetyltransferase
            KO: K00619  amino-acid N-acetyltransferase
            KO: K00620  amino-acid N-acetyltransferase
GENES       HSA: 162417(NAGS)
            PTR: 468274(NAGS)
            MMU: 217214(Nags)
            CFA: 490943(NAGS)
            SPU: 591447(LOC591447)
            ATH: AT2G37500
            OSA: 4332434 4333177
            CME: CMB127C CMS424C
            SCE: YMR062C(ECM40)
            AGO: AGOS_ADR138C
            PIC: PICST_51037(ARG2) PICST_60752(ECM40) PICST_76181(NAT3)
            CGR: CAGL0F06501g
            SPO: SPBC1271.14 SPBC725.14
            ANI: AN5867.2 AN7722.2
            AFM: AFUA_2G11490 AFUA_5G08120
            AOR: AO090026000498 AO090701000729
            CNE: CND03570
            DDI: DDB_0231449(argJ)
            PFA: MAL1P2.22
            TAN: TA10830
            ECO: b2818(argA)
            ECJ: JW2786(argA)
            ECE: Z4135(argA)
            ECS: ECs3675
            ECC: c3412(argA)
            ECI: UTI89_C3219(argA)
            ECP: ECP_2830
            ECV: APECO1_3687(argA)
            ECW: EcE24377A_3138(argA)
            ECX: EcHS_A2964
            STY: STY3130(argA)
            STT: t2900(argA)
            SPT: SPA2857(argA)
            SEC: SC2930(argA)
            STM: STM2992(argA)
            YPE: YPO1022(argA)
            YPK: y3162(argA)
            YPM: YP_2828(argA)
            YPA: YPA_0494
            YPN: YPN_2979
            YPS: YPTB3023(argA)
            YPI: YpsIP31758_0993(argA)
            SFL: SF2829(argA)
            SFX: S3026(argA)
            SFV: SFV_2896(argA)
            SSN: SSON_2975(argA)
            SBO: SBO_2708(argA)
            SDY: SDY_3035(argA)
            ECA: ECA0999(argA)
            PLU: plu0644(argA)
            BUC: BU456(argA)
            BAS: BUsg441(argA)
            HDU: HD1384(argA)
            PMU: PM0828(argA)
            APL: APL_0698(argA)
            VCH: VC2316
            VCO: VC0395_A1901(argA)
            VVU: VV1_1799
            VVY: VV2611
            VPA: VP2371
            VFI: VF0585 VF2303
            PPR: PBPRA2996(argA)
            PAE: PA4402(argJ) PA5204(argA)
            PAU: PA14_57210(argJ) PA14_68740(argA)
            PAP: PSPA7_4973(argJ) PSPA7_5949(argA)
            PPU: PP_1346(argJ) PP_5185(argA)
            PPF: Pput_4378
            PST: PSPTO_0324(argA) PSPTO_4399(argJ)
            PSB: Psyr_0254 Psyr_4093(argJ)
            PSP: PSPPH_0242(argA) PSPPH_4099(argJ)
            PFL: PFL_4780(argJ) PFL_5941(argA)
            PFO: Pfl_4427 Pfl_5419(argA)
            PEN: PSEEN4476(argJ) PSEEN5300(argA)
            PMY: Pmen_0932
            PAR: Psyc_1198(argJ) Psyc_2089(argA)
            PCR: Pcryo_2405
            PRW: PsycPRwf_1257
            ACI: ACIAD0039(argA) ACIAD0650(argJ)
            SON: SO_4245(argA)
            SDN: Sden_0329
            SFR: Sfri_3825
            SAZ: Sama_0330
            SLO: Shew_3478
            SPL: Spea_3834
            SHE: Shewmr4_3594
            SHM: Shewmr7_0362
            SHN: Shewana3_3767
            CPS: CPS_0465(argA) CPS_1312(argJ)
            PHA: PSHAa2287(argHA)
            PAT: Patl_0977
            SDE: Sde_0360
            PIN: Ping_0872
            MCA: MCA1679(argJ) MCA2084(argA)
            TCX: Tcr_0590 Tcr_0598
            NOC: Noc_2013 Noc_2850
            AEH: Mlg_0363 Mlg_2085
            HCH: HCH_01030(argA)
            CSA: Csal_0713 Csal_2180
            ABO: ABO_0608(argJ) ABO_2306(argA)
            MMW: Mmwyl1_2606
            AHA: AHA_2569(argA)
            VOK: COSY_0655(argJ)
            NME: NMB1876 NMB2005
            NMA: NMA0435(argJ) NMA0580(argA)
            NMC: NMC0343(argA) NMC1982(argJ)
            NGO: NGO0027 NGO1194
            CVI: CV_0478(argJ) CV_3355(argA)
            RSO: RSc1250(argA) RSc2833(argJ)
            REU: Reut_A2066(argA) Reut_A2969(argJ)
            REH: H16_A2343(argAB) H16_A3263(argJ)
            RME: Rmet_2070 Rmet_3117
            BMA: BMA1751(argA) BMA2539(argJ)
            BMV: BMASAVP1_A2260(argA)
            BML: BMA10299_A3059(argA)
            BMN: BMA10247_1532(argA)
            BXE: Bxe_A0496 Bxe_A1512
            BVI: Bcep1808_2235
            BUR: Bcep18194_A3655 Bcep18194_A5465(argA)
            BCN: Bcen_5921
            BCH: Bcen2424_2156
            BAM: Bamb_2193
            BPS: BPSL2325 BPSL3015(argJ)
            BPM: BURPS1710b_2777(argA) BURPS1710b_3534(argJ)
            BPL: BURPS1106A_2699(argA) BURPS1106A_3539(argJ)
            BPD: BURPS668_2643(argA) BURPS668_3514(argJ)
            BTE: BTH_I1128(argJ) BTH_I1837(argA)
            BPE: BP2335(argA) BP3807(argJ)
            BPA: BPP1704(argA) BPP3953(argJ)
            BBR: BB4426(argJ)
            RFR: Rfer_2105 Rfer_2910
            POL: Bpro_0829 Bpro_2397
            MPT: Mpe_A1373 Mpe_A2743
            HAR: HEAR1078(argA) HEAR2797(argJ)
            MMS: mma_1179 mma_3004
            NEU: NE0778(argA) NE2213(argJ)
            NET: Neut_0655 Neut_1048
            NMU: Nmul_A0380(argA) Nmul_A1010(argJ)
            EBA: ebA1090(argA) ebA1431(argJ)
            AZO: azo2830(argA)
            DAR: Daro_3487(argJ) Daro_3584(argA)
            TBD: Tbd_0029(argJ) Tbd_0154(argA)
            MFA: Mfla_2232
            HHE: HH1291(argJ)
            WSU: WS0330(argJ)
            TDN: Tmden_1600
            CFF: CFF8240_0973(argJ)
            CCV: CCV52592_0720(argJ) CCV52592_1326
            CHA: CHAB381_0772(argJ)
            ABU: Abu_0982 Abu_1791(argJ)
            NIS: NIS_0318(argJ)
            SUN: SUN_2160
            GSU: GSU2049(argJ)
            GME: Gmet_0952(argJ)
            GUR: Gura_1795
            PCA: Pcar_2322(argJ)
            DVU: DVU0823(argJ)
            DVL: Dvul_2157
            DDE: Dde_1081(argJ)
            LIP: LI0714(argJ)
            DPS: DP2741
            ADE: Adeh_0587
            AFW: Anae109_0632 Anae109_1203
            SAT: SYN_01035 SYN_02861
            SFU: Sfum_1201
            ERU: Erum3800(argJ)
            ERW: ERWE_CDS_03920(argJ)
            ERG: ERGA_CDS_03880(argJ)
            ECN: Ecaj_0370(argJ)
            ECH: ECH_0676(argJ)
            PUB: SAR11_0513(argJ)
            MLO: mll3461
            MES: Meso_3012
            PLA: Plav_1732
            SME: SMc02450(argJ)
            SMD: Smed_2516
            ATU: Atu3518(argJ)
            ATC: AGR_L_2624
            RET: RHE_CH03768(argJ)
            RLE: RL4296(argJ)
            BME: BMEI0124
            BMF: BAB1_1942(argJ)
            BMS: BR1941(argJ)
            BMB: BruAb1_1917(argJ)
            BOV: BOV_1868(argJ)
            OAN: Oant_1023
            BJA: blr0206(argJ)
            BRA: BRADO0588(argJ)
            BBT: BBta_7590(argJ)
            RPA: RPA0592(argJ)
            RPB: RPB_0030(argJ)
            RPC: RPC_0524
            RPD: RPD_0111
            RPE: RPE_0148
            NWI: Nwi_0388(argJ)
            NHA: Nham_0483
            BHE: BH02010(argJ)
            BQU: BQ01890(argJ)
            BBK: BARBAKC583_0363(argJ)
            XAU: Xaut_2584
            CCR: CC_3066
            SIL: SPO0059(argJ)
            SIT: TM1040_2915
            RSP: RSP_1167(argJ)
            RSQ: Rsph17025_2759
            JAN: Jann_0291
            RDE: RD1_0384(argJ)
            PDE: Pden_2597
            HNE: HNE_3174(argJ)
            ZMO: ZMO0923
            NAR: Saro_1993
            SAL: Sala_0155
            SWI: Swit_2685
            ELI: ELI_05085
            GOX: GOX1676
            GBE: GbCGDNIH1_0624
            ACR: Acry_2244
            RRU: Rru_A0394
            MAG: amb0510
            BSU: BG10192(argJ)
            BHA: BH2899(argJ)
            BAN: BA0831 BA4354(argJ)
            BAR: GBAA4354(argJ)
            BAA: BA_4811(argJ)
            BAT: BAS4039
            BCE: BC4129
            BCA: BCE_4202(argJ)
            BCZ: BCZK3886(argJ)
            BCY: Bcer98_2828
            BTK: BT9727_3878(argJ)
            BLI: BL03242(argJ)
            BLD: BLi01207(argJ)
            BCL: ABC2557(argJ)
            BPU: BPUM_1043
            OIH: OB1076(argJ)
            GKA: GK0791
            SAU: SA0177(argJ)
            SAV: SAV0183(argJ)
            SAM: MW0157(argJ)
            SAR: SAR0184(argJ)
            SAS: SAS0158
            SAC: SACOL0168(argJ)
            SAA: SAUSA300_0185(argJ)
            SAO: SAOUHSC_00148
            SAJ: SaurJH9_0168
            SAH: SaurJH1_0173
            SEP: SE1211
            SER: SERP1091(argJ)
            SSP: SSP0222
            LMO: lmo1590(argJ)
            LMF: LMOf2365_1612(argJ)
            LIN: lin1632(argJ)
            LWE: lwe1603(argJ)
            LLA: L0105(argJ)
            LLC: LACR_0857
            SMU: SMU.664(argJ)
            STC: str0465(argJ)
            STL: stu0465(argJ)
            SSA: SSA_0758(argJ)
            LPL: lp_0529(argJ)
            STH: STH2890
            CAC: CAC2391(argJ) CAC3020
            CDF: CD2033(argJ)
            CBE: Cbei_4518
            CKL: CKL_1554(argJ)
            AMT: Amet_3382
            CHY: CHY_2264(argJ)
            DSY: DSY0761
            DRM: Dred_0272
            SWO: Swol_2290
            TTE: TTE2497(argJ)
            MTA: Moth_2289(argJ)
            MTU: Rv1653(argJ)
            MTC: MT1691(argJ)
            MBO: Mb1681(argJ)
            MLE: ML1407(argJ)
            MPA: MAP1362(argJ)
            MAV: MAV_3117(argJ)
            MSM: MSMEG_3775(argJ)
            MVA: Mvan_3313
            MMC: Mmcs_2971
            MKM: Mkms_3015
            MJL: Mjls_2986
            CGL: NCgl1341(argJ)
            CGB: cg1581(argJ)
            CEF: CE1527(argJ)
            CDI: DIP1168(argJ)
            CJK: jk0842(argJ)
            NFA: nfa19370(argJ)
            RHA: RHA1_ro00955(argJ)
            SCO: SCO1579(argJ)
            SMA: SAV6764(argJ)
            LXX: Lxx06040(argJ)
            ART: Arth_1497
            NCA: Noca_2469
            TFU: Tfu_2056(argJ)
            FRA: Francci3_3174(argJ)
            FAL: FRAAL5207(argJ)
            ACE: Acel_1262
            KRA: Krad_3160
            SEN: SACE_5261(argJ)
            BLO: BL1063(argJ)
            BAD: BAD_0924(argJ)
            RXY: Rxyl_2886
            RBA: RB3255(argJ) RB8540(argA)
            LIL: LA4105(argJ)
            LIC: LIC13271(argJ)
            LBJ: LBJ_0184(argJ)
            LBL: LBL_2899(argJ)
            SYN: sll1883(argJ)
            SYW: SYNW2353(argJ)
            SYC: syc2199_d(argJ)
            SYF: Synpcc7942_1896
            SYD: Syncc9605_2489(argJ)
            SYE: Syncc9902_2166(argJ)
            SYG: sync_2736(argJ)
            SYR: SynRCC307_2373(argJ)
            SYX: SynWH7803_2383(argJ)
            CYA: CYA_1327(argJ)
            CYB: CYB_2548(argJ)
            TEL: tll1911(argJ)
            GVI: glr4034(argJ)
            ANA: alr2073 alr4235(argJ)
            AVA: Ava_0671(argJ) Ava_3118(argJ)
            PMA: Pro0054(argJ)
            PMM: PMM0050(argJ)
            PMT: PMT2135(argJ)
            PMN: PMN2A_1383(argJ)
            PMI: PMT9312_0051
            PMB: A9601_00511(argJ)
            PMC: P9515_00571(argJ)
            PMF: P9303_28231(argJ)
            PMG: P9301_00531(argJ)
            PME: NATL1_00641(argJ)
            TER: Tery_0043
            CTE: CT1110(argJ)
            CCH: Cag_0773(argJ) Cag_1870
            CPH: Cpha266_1321
            PLT: Plut_1048(argJ)
            DET: DET1256(argJ)
            DEH: cbdb_A1179(argJ)
            DEB: DehaBAV1_1067
            RRS: RoseRS_4059
            RCA: Rcas_3355
            DRA: DR_1704
            DGE: Dgeo_0742
            TTH: TTC0835 TTC1703
            TTJ: TTHA1196
            AAE: aq_970(argJ)
            TMA: TM1783
            MJA: MJ0186(argJ)
            MMP: MMP0897(argJ)
            MMZ: MmarC7_0145
            MVN: Mevan_0023
            MAC: MA3564(argJ) MA4339
            MBA: Mbar_A0587 Mbar_A2003
            MMA: MM_0474 MM_1035 MM_1519
            MBU: Mbur_0051 Mbur_1340
            MTP: Mthe_0491
            MEM: Memar_0153
            MTH: MTH182
            MSI: Msm_0379
            MKA: MK0865
            AFU: AF1147(argJ)
STRUCTURES  PDB: 1VRA  2I00  2I79  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.1
            ExPASy - ENZYME nomenclature database: 2.3.1.1
            ExplorEnz - The Enzyme Database: 2.3.1.1
            ERGO genome analysis and discovery system: 2.3.1.1
            BRENDA, the Enzyme Database: 2.3.1.1
            CAS: 9029-88-3
///
ENTRY       EC 2.3.1.2                  Enzyme
NAME        imidazole N-acetyltransferase;
            imidazole acetylase;
            imidazole acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:imidazole N-acetyltransferase
REACTION    acetyl-CoA + imidazole = CoA + N-acetylimidazole [RN:R03621]
ALL_REAC    R03621
SUBSTRATE   acetyl-CoA [CPD:C00024];
            imidazole [CPD:C01589]
PRODUCT     CoA [CPD:C00010];
            N-acetylimidazole [CPD:C02560]
COMMENT     Also acts with propanoyl-CoA.
REFERENCE   1
  AUTHORS   Kinsky, S.C.
  TITLE     Assay, purification, and properties of imidazole acetylase.
  JOURNAL   J. Biol. Chem. 235 (1960) 94-98.
  ORGANISM  Clostridium kluyveri
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.2
            ExPASy - ENZYME nomenclature database: 2.3.1.2
            ExplorEnz - The Enzyme Database: 2.3.1.2
            ERGO genome analysis and discovery system: 2.3.1.2
            BRENDA, the Enzyme Database: 2.3.1.2
            CAS: 9029-89-4
///
ENTRY       EC 2.3.1.3                  Enzyme
NAME        glucosamine N-acetyltransferase;
            glucosamine acetylase;
            glucosamine acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:D-glucosamine N-acetyltransferase
REACTION    acetyl-CoA + D-glucosamine = CoA + N-acetyl-D-glucosamine
            [RN:R01204]
ALL_REAC    R01204
SUBSTRATE   acetyl-CoA [CPD:C00024];
            D-glucosamine [CPD:C00329]
PRODUCT     CoA [CPD:C00010];
            N-acetyl-D-glucosamine [CPD:C00140]
REFERENCE   1  [PMID:12980946]
  AUTHORS   CHOU TC, SOODAK M.
  TITLE     The acetylation of d-glucosamine by pigeon liver extracts.
  JOURNAL   J. Biol. Chem. 196 (1952) 105-9.
  ORGANISM  pigeon
PATHWAY     PATH: map00530  Aminosugars metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.3
            ExPASy - ENZYME nomenclature database: 2.3.1.3
            ExplorEnz - The Enzyme Database: 2.3.1.3
            ERGO genome analysis and discovery system: 2.3.1.3
            BRENDA, the Enzyme Database: 2.3.1.3
            CAS: 9032-94-4
///
ENTRY       EC 2.3.1.4                  Enzyme
NAME        glucosamine-phosphate N-acetyltransferase;
            phosphoglucosamine transacetylase;
            phosphoglucosamine acetylase;
            glucosamine-6-phosphate acetylase;
            D-glucosamine-6-P N-acetyltransferase;
            aminodeoxyglucosephosphate acetyltransferase;
            glucosamine 6-phosphate acetylase;
            glucosamine 6-phosphate N-acetyltransferase;
            N-acetylglucosamine-6-phosphate synthase;
            phosphoglucosamine N-acetylase;
            glucosamine-phosphate N-acetyltransferase;
            glucosamine-6-phosphate N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:D-glucosamine-6-phosphate N-acetyltransferase
REACTION    acetyl-CoA + D-glucosamine 6-phosphate = CoA +
            N-acetyl-D-glucosamine 6-phosphate [RN:R02058]
ALL_REAC    R02058
SUBSTRATE   acetyl-CoA [CPD:C00024];
            D-glucosamine 6-phosphate [CPD:C00352]
PRODUCT     CoA [CPD:C00010];
            N-acetyl-D-glucosamine 6-phosphate [CPD:C00357]
REFERENCE   1
  AUTHORS   Davidson, E.A.
  TITLE     Glucosamine 6-phosphate N-acetylase.
  JOURNAL   Methods Enzymol. 9 (1966) 704-707.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2  [PMID:13428743]
  AUTHORS   DAVIDSON EA, BLUMENTHAL HJ, ROSEMAN S.
  TITLE     Glucosamine metabolism.  II.  Studies on glucosamine 6-phosphate
            N-acetylase.
  JOURNAL   J. Biol. Chem. 226 (1957) 125-33.
  ORGANISM  Streptococcus sp., Penicillium sp., Neurospora crassa [GN:dncr],
            rabbit, dog [GN:cfa], human [GN:hsa]
REFERENCE   3  [PMID:14484387]
  AUTHORS   PATTABIRAMAN TN, BACHHAWAT BK.
  TITLE     Purification of glucosamine-6-phosphate N-acetylase from sheep
            brain.
  JOURNAL   Biochim. Biophys. Acta. 59 (1962) 681-9.
  ORGANISM  sheep
REFERENCE   4  [PMID:10777580]
  AUTHORS   Boehmelt G, Fialka I, Brothers G, McGinley MD, Patterson SD, Mo R,
            Hui CC, Chung S, Huber LA, Mak TW, Iscove NN.
  TITLE     Cloning and characterization of the murine glucosamine-6-phosphate
            acetyltransferase EMeg32. Differential expression and intracellular
            membrane association.
  JOURNAL   J. Biol. Chem. 275 (2000) 12821-32.
  ORGANISM  murine
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K00621  glucosamine-phosphate N-acetyltransferase
GENES       HSA: 64841(GNPNAT1)
            PTR: 467460(GNPNAT1)
            MMU: 54342(Gnpnat1)
            CFA: 480325(GNPNAT1)
            GGA: 423588(GNPNAT1)
            XLA: 379524(MGC68838)
            XTR: 448201(MGC88872)
            DME: Dmel_CG1969
            CEL: B0024.12(gna-1)
            ATH: AT5G15770
            OSA: 4347432
            CME: CMN031C CMS020C
            SCE: YFL017C(GNA1)
            AGO: AGOS_AFR510W
            PIC: PICST_77083(GNA1)
            CGR: CAGL0D02156g
            AFM: AFUA_6G02460
            AOR: AO090120000132
            CNE: CNF03220
            ECU: ECU07_1760
            DDI: DDBDRAFT_0205790
            TET: TTHERM_01048070
            TBR: Tb11.01.2886
            TCR: 508831.120 511671.70
            LMA: LmjF28.3005
            EHI: 34.t00022 405.t00007
            RLE: RL3475
            FNU: FN1991
STRUCTURES  PDB: 1I12  1I1D  1I21  2HUZ  2O28  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.4
            ExPASy - ENZYME nomenclature database: 2.3.1.4
            ExplorEnz - The Enzyme Database: 2.3.1.4
            ERGO genome analysis and discovery system: 2.3.1.4
            BRENDA, the Enzyme Database: 2.3.1.4
            CAS: 9031-91-8
///
ENTRY       EC 2.3.1.5                  Enzyme
NAME        arylamine N-acetyltransferase;
            arylamine acetylase;
            beta-naphthylamine N-acetyltransferase;
            4-aminobiphenyl N-acetyltransferase;
            acetyl CoA-arylamine N-acetyltransferase;
            2-naphthylamine N-acetyltransferase;
            arylamine acetyltransferase;
            indoleamine N-acetyltransferase;
            N-acetyltransferase;
            p-aminosalicylate N-acetyltransferase;
            serotonin acetyltransferase;
            serotonin N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:arylamine N-acetyltransferase
REACTION    acetyl-CoA + an arylamine = CoA + an N-acetylarylamine [RN:R02387]
ALL_REAC    R02387;
            (other) R07940
SUBSTRATE   acetyl-CoA [CPD:C00024];
            arylamine [CPD:C00292]
PRODUCT     CoA [CPD:C00010];
            N-acetylarylamine [CPD:C02558]
COMMENT     Wide specificity for aromatic amines, including serotonin; also
            catalyses acetyl-transfer between arylamines without CoA.
REFERENCE   1  [PMID:12980945]
  AUTHORS   CHOU TC, LIPMANN F.
  TITLE     Separation of acetyl transfer enzymes in pigeon liver extract.
  JOURNAL   J. Biol. Chem. 196 (1952) 89-103.
  ORGANISM  pigeon
REFERENCE   2  [PMID:4748369]
  AUTHORS   Paul RC, Ratledge C.
  TITLE     Further studies on anthranilate N-acetyltransferase and the
            metabolism of N-acetylanthranilic acid in Aerobacter aerogenes.
  JOURNAL   Biochim. Biophys. Acta. 320 (1973) 9-15.
  ORGANISM  Aerobacter aerogenes
REFERENCE   3
  AUTHORS   Tabor, H., Mehler, A.H. and Stadtman, E.R.
  TITLE     The enzymatic acetylation of amines.
  JOURNAL   J. Biol. Chem. 204 (1953) 127-138.
  ORGANISM  pigeon
REFERENCE   4
  AUTHORS   Weissbach, H., Redfield, B.G. and Axelrod, J.
  TITLE     The enzymic acetylation of serotonin and other naturally occurring
            amines.
  JOURNAL   Biochim. Biophys. Acta 54 (1961) 190-192.
  ORGANISM  rat [GN:rno], rabbit, cow [GN:bta]
PATHWAY     PATH: map00232  Caffeine metabolism
ORTHOLOGY   KO: K00622  arylamine N-acetyltransferase
GENES       HSA: 10(NAT2) 9(NAT1)
            PTR: 464023(NAT1)
            MMU: 17960(Nat1) 17961(Nat2) 17962(Nat3)
            RNO: 116631(Nat1) 116632(Nat2) 290681(Nat3)
            GGA: 396283(NAT1) 396537(NAT) 415809(NAT2)
            PAU: PA14_63830
            REU: Reut_B4044
            REH: H16_B1241(nhoA)
            RME: Rmet_4744
            BXE: Bxe_B1830
            BVI: Bcep1808_5210
            BCN: Bcen_3680
            BCH: Bcen2424_4687
            AZO: azo0788
            MLO: mlr4870
            PLA: Plav_1447
            RET: RHE_CH00591
            BRA: BRADO6242
            BBT: BBta_1363
            NAR: Saro_0952
            SAL: Sala_2373
            SWI: Swit_4676
            BSU: BG12404(nat)
            MTU: Rv3566c(nat)
            MTC: MT3671(nhoA)
            MBO: Mb3596c(nat)
            MBB: BCG_3630c(nat)
            MPA: MAP0501(nhoA)
            MAV: MAV_0595
            MSM: MSMEG_0306
            MVA: Mvan_0235
            MGI: Mflv_0433
            MMC: Mmcs_0211
            MKM: Mkms_0221
            MJL: Mjls_0201
            NFA: nfa18420
            RHA: RHA1_ro02470(nat)
            SEN: SACE_0058
STRUCTURES  PDB: 1GX3  1W5R  1W6F  2BSZ  2IJA  2PFR  2PQT  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.5
            ExPASy - ENZYME nomenclature database: 2.3.1.5
            ExplorEnz - The Enzyme Database: 2.3.1.5
            ERGO genome analysis and discovery system: 2.3.1.5
            UM-BBD (Biocatalysis/Biodegradation Database): 2.3.1.5
            BRENDA, the Enzyme Database: 2.3.1.5
            CAS: 9027-33-2
///
ENTRY       EC 2.3.1.6                  Enzyme
NAME        choline O-acetyltransferase;
            choline acetylase;
            choline acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:choline O-acetyltransferase
REACTION    acetyl-CoA + choline = CoA + O-acetylcholine [RN:R01023]
ALL_REAC    R01023
SUBSTRATE   acetyl-CoA [CPD:C00024];
            choline [CPD:C00114]
PRODUCT     CoA [CPD:C00010];
            O-acetylcholine [CPD:C01996]
COMMENT     Propanoyl-CoA can act, more slowly, in place of acetyl-CoA.
REFERENCE   1  [PMID:13115440]
  AUTHORS   BERMAN R, WILSON IB, NACHMANSOHN D.
  TITLE     Choline acetylase specificity in relation to biological function.
  JOURNAL   Biochim. Biophys. Acta. 12 (1953) 315-24.
  ORGANISM  electric fish
REFERENCE   2  [PMID:13799882]
  AUTHORS   BERRY JF, WHITTAKER VP.
  TITLE     The acyl-group specificity of choline acetylase.
  JOURNAL   Biochem. J. 73 (1959) 447-58.
  ORGANISM  pigeon
REFERENCE   3  [PMID:14299645]
  AUTHORS   FRITZ IB, SCHULTZ SK.
  TITLE     CARNITINE ACETYLTRANSFERASE. II. INHIBIITON BY CARNITINE ANALOGUES
            AND BY SULFHYDRYL REAGENTS.
  JOURNAL   J. Biol. Chem. 240 (1965) 2188-92.
  ORGANISM  pig [GN:ssc]
REFERENCE   4
  AUTHORS   Schuberth, J.
  TITLE     Choline acetyltransferase. Purification and effect of salts on the
            mechanism of the enzyme-catalysed reaction.
  JOURNAL   Biochim. Biophys. Acta 122 (1966) 470-481.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00623  choline O-acetyltransferase
GENES       HSA: 1103(CHAT)
            MMU: 12647(Chat)
            CFA: 486775(CHAT)
            SSC: 396896(CHAT)
            GGA: 395314(CHAT)
            SPU: 574696(LOC574696)
            DME: Dmel_CG12345(Cha)
STRUCTURES  PDB: 1Q6X  1T1U  2FY2  2FY3  2FY4  2FY5  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.6
            ExPASy - ENZYME nomenclature database: 2.3.1.6
            ExplorEnz - The Enzyme Database: 2.3.1.6
            ERGO genome analysis and discovery system: 2.3.1.6
            BRENDA, the Enzyme Database: 2.3.1.6
            CAS: 9012-78-6
///
ENTRY       EC 2.3.1.7                  Enzyme
NAME        carnitine O-acetyltransferase;
            acetyl-CoA-carnitine O-acetyltransferase;
            acetylcarnitine transferase;
            carnitine acetyl coenzyme A transferase;
            carnitine acetylase;
            carnitine acetyltransferase;
            carnitine-acetyl-CoA transferase;
            CATC
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:carnitine O-acetyltransferase
REACTION    acetyl-CoA + carnitine = CoA + O-acetylcarnitine [RN:R02396]
ALL_REAC    R02396
SUBSTRATE   acetyl-CoA [CPD:C00024];
            carnitine [CPD:C00487]
PRODUCT     CoA [CPD:C00010];
            O-acetylcarnitine [CPD:C02571]
COMMENT     Also acts on propanoyl-CoA and butanoyl-CoA (cf. EC 2.3.1.21
            carnitine O-palmitoyltransferase and EC 2.3.1.137 carnitine
            O-octanoyltransferase).
REFERENCE   1
  AUTHORS   Chase, J.F.A., Pearson, D.J. and Tubbs, P.K.
  TITLE     The preparation of crystalline carnitine acetyltransferase.
  JOURNAL   Biochim. Biophys. Acta 96 (1965) 162-165.
  ORGANISM  pigeon, pig [GN:ssc]
REFERENCE   2  [PMID:13275966]
  AUTHORS   FRIEDMAN S, FRAENKEL G.
  TITLE     Reversible enzymatic acetylation of carnitine.
  JOURNAL   Arch. Biochem. Biophys. 59 (1955) 491-501.
  ORGANISM  pigeon
REFERENCE   3
  AUTHORS   Miyazawa, S., Ozasa, H., Furuta, S., Osumi, T. and Hashimoto, T.
  TITLE     Purification and properties of carnitine acetyl transferase from rat
            liver.
  JOURNAL   J. Biochem. (Tokyo) 93 (1983) 439-451.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
ORTHOLOGY   KO: K00624  carnitine O-acetyltransferase
GENES       HSA: 1384(CRAT)
            PTR: 464783(CRAT)
            MMU: 12908(Crat)
            CFA: 491304(CRAT)
            GGA: 417195(CRAT)
            SPU: 593866(LOC593866)
            DME: Dmel_CG5265
            CEL: B0395.3
            SCE: YAR035W(YAT1) YML042W(CAT2)
            AGO: AGOS_AAR124C AGOS_AER224W
            PIC: PICST_34304(CAT2) PICST_68034(YAT1)
            CGR: CAGL0C05027g CAGL0J11836g
            ANI: AN6279.2
            AFM: AFUA_1G12340 AFUA_2G12530
            AOR: AO090001000295 AO090026000404
            CNE: CNA05200 CNF04660
            UMA: UM00789.1 UM01835.1
            TBR: Tb11.18.0006
            TCR: 511303.40
            SSE: Ssed_1774
            MPN: MPN114(cpt2)
            MPU: MYPU_7750(cat)
            SCO: SCO7519(SCBAC25F8.11c)
            FRA: Francci3_1063
            FAL: FRAAL1805
            SEN: SACE_3158
            STP: Strop_2064
STRUCTURES  PDB: 1NDB  1NDF  1NDI  1NM8  1S5O  1T7O  1T7Q  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.7
            ExPASy - ENZYME nomenclature database: 2.3.1.7
            ExplorEnz - The Enzyme Database: 2.3.1.7
            ERGO genome analysis and discovery system: 2.3.1.7
            BRENDA, the Enzyme Database: 2.3.1.7
            CAS: 9029-90-7
///
ENTRY       EC 2.3.1.8                  Enzyme
NAME        phosphate acetyltransferase;
            phosphotransacetylase;
            phosphoacylase;
            PTA
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:phosphate acetyltransferase
REACTION    acetyl-CoA + phosphate = CoA + acetyl phosphate [RN:R00230]
ALL_REAC    R00230;
            (other) R00921
SUBSTRATE   acetyl-CoA [CPD:C00024];
            phosphate [CPD:C00009]
PRODUCT     CoA [CPD:C00010];
            acetyl phosphate [CPD:C00227]
COMMENT     Also acts with other short-chain acyl-CoAs.
REFERENCE   1  [PMID:14087284]
  AUTHORS   BERGMEYER HU, HOLZ G, KLOTZSCH H, LANG G.
  TITLE     [PHOSPHOTRANSACETYLASE FROM  CLOSTRIDIUM KLUYVERI. CULTURE OF THE
            BACTERIUM, ISOLATION, CRYSTALLIZATION AND PROPERTIES OF THE ENZYME.]
  JOURNAL   Biochem. Z. 338 (1963) 114-21.
  ORGANISM  Clostridium kluyveri
REFERENCE   2  [PMID:12980995]
  AUTHORS   STADTMAN ER.
  TITLE     The purification and properties of phosphotransacetylase.
  JOURNAL   J. Biol. Chem. 196 (1952) 527-34.
  ORGANISM  Clostridium kluyveri
REFERENCE   3
  AUTHORS   Stadtman, E.R.
  TITLE     Phosphotransacetylase from Clostridium kluyveri.
  JOURNAL   Methods Enzymol. 1 (1955) 596-599.
  ORGANISM  Clostridium kluyveri
PATHWAY     PATH: map00430  Taurine and hypotaurine metabolism
            PATH: map00620  Pyruvate metabolism
            PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K00625  phosphate acetyltransferase
GENES       ECO: b2297(pta)
            ECJ: JW2294(pta)
            ECE: Z3559(pta)
            ECS: ECs3181
            ECC: c2840(pta)
            ECI: UTI89_C2581(pta) UTI89_C2782(eutD)
            ECP: ECP_2336
            ECW: EcE24377A_2735(pta)
            ECX: EcHS_A2447 EcHS_A2587 EcHS_A2691(hcaF)
            STY: STY2568(pta)
            STT: t0526(pta)
            SPT: SPA0526(pta)
            SEC: SC2339(pta)
            STM: STM2338(pta)
            YPE: YPO2567(pta)
            YPK: y1620(pta)
            YPM: YP_2378(pta)
            YPA: YPA_2056 YPA_2222
            YPN: YPN_1351 YPN_2159
            YPP: YPDSF_1974 YPDSF_2139
            YPS: YPTB2598(pta)
            YPI: YpsIP31758_1442(pta)
            YEN: YE1333(pta)
            SFL: SF2373(pta)
            SFX: S2508(pta)
            SFV: SFV_2364(pta)
            SSN: SSON_2354(pta)
            SBO: SBO_2332(pta)
            SDY: SDY_2493(pta)
            ECA: ECA3040(pta)
            PLU: plu3096(pta)
            BUC: BU176(pta)
            BAS: BUsg170(pta)
            BAB: bbp165(pta)
            BCC: BCc_115(pta)
            WBR: WGLp180(pta)
            SGL: SG1607
            ENT: Ent638_2841 Ent638_2958
            SPE: Spro_3317 Spro_3472
            HIN: HI1203(pta)
            HIT: NTHI1374(pta)
            HIP: CGSHiEE_06025
            HIQ: CGSHiGG_09735
            HDU: HD1457(pta)
            HSO: HS_0802(pta)
            PMU: PM0705(pta)
            MSU: MS0998(pta)
            APL: APL_0644(pta)
            ASU: Asuc_1662
            VCH: VC1097
            VCO: VC0395_A0615(pta)
            VVU: VV1_2220
            VVY: VV2134
            VPA: VP2083
            VFI: VF0836
            PPR: PBPRA2799
            PAE: PA0835(pta)
            PAU: PA14_53480(pta)
            PAP: PSPA7_4685
            PPU: PP_0774(pta)
            PPF: Pput_0799
            PST: PSPTO_1169(pta)
            PSB: Psyr_1007
            PSP: PSPPH_1056(pta)
            PFL: PFL_0938(pta)
            PFO: Pfl_0880
            PEN: PSEEN0916(pta)
            PMY: Pmen_3645
            PAR: Psyc_0196
            PCR: Pcryo_0216 Pcryo_0997
            PRW: PsycPRwf_0345 PsycPRwf_1269
            ACI: ACIAD0540(pta) ACIAD2287
            ACB: A1S_0481
            SON: SO_2916(pta)
            SDN: Sden_2410
            SFR: Sfri_2477
            SAZ: Sama_1494
            SBL: Sbal_2675
            SLO: Shew_2394
            SSE: Ssed_1704
            SHE: Shewmr4_1490
            SHM: Shewmr7_1557
            SHN: Shewana3_1551
            SHW: Sputw3181_1627
            CPS: CPS_3177(pta)
            PAT: Patl_2591
            PIN: Ping_3312
            MAQ: Maqu_1132 Maqu_1231
            LPN: lpg2261
            LPF: lpl2187(pta)
            LPP: lpp2215(pta)
            FTU: FTT1754(pta)
            FTF: FTF1754(pta)
            FTW: FTW_1992(pta)
            FTL: FTL_0016
            FTH: FTH_0016(pta)
            FTA: FTA_0018
            FTN: FTN_0126(pta)
            NOC: Noc_1582
            AEH: Mlg_0246
            HHA: Hhal_1029
            HCH: HCH_04451(pta)
            AHA: AHA_0890
            DNO: DNO_0020(maeB) DNO_0448(pta)
            BCI: BCI_0383(pta)
            NME: NMB0631
            NMA: NMA0841
            NMC: NMC0575
            NGO: NGO0214
            CVI: CV_1530(pta) CV_3744(ptb)
            REU: Reut_A2441 Reut_A2847 Reut_B3772
            REH: H16_B1631(pta1) H16_B1871(pta2)
            RME: Rmet_0563 Rmet_3046
            BMA: BMAA0121
            BXE: Bxe_B0357 Bxe_B0690(pta) Bxe_C0052
            BVI: Bcep1808_0300 Bcep1808_0605 Bcep1808_3396 Bcep1808_5358
            BUR: Bcep18194_A3417 Bcep18194_A3713 Bcep18194_B1994
                 Bcep18194_B2662
            BCN: Bcen_0148 Bcen_2788 Bcen_3494
            BCH: Bcen2424_0318 Bcen2424_0631 Bcen2424_3496 Bcen2424_4872
            BAM: Bamb_0237 Bamb_0532 Bamb_4462
            BPS: BPSS1955
            BPM: BURPS1710b_0019(maeB-2) BURPS1710b_A1058
            BTE: BTH_II0417
            PNU: Pnuc_0224
            RFR: Rfer_0093 Rfer_0262 Rfer_1424 Rfer_2974
            POL: Bpro_1421 Bpro_4858
            PNA: Pnap_1010 Pnap_4071
            AAV: Aave_1095 Aave_4759
            AJS: Ajs_1112 Ajs_4106
            VEI: Veis_0807 Veis_1646
            HAR: HEAR0648 HEAR1516
            NEU: NE0298(pta)
            NET: Neut_1995
            EBA: ebA2247(pta)
            AZO: azo3638(pta)
            DAR: Daro_0975
            MFA: Mfla_0740
            HPY: HP0905(pta)
            HPJ: jhp0841(pta)
            HPA: HPAG1_0885 HPAG1_0886 HPAG1_0887
            HHE: HH1309(pta)
            HAC: Hac_1290(pta)
            TDN: Tmden_0055
            CJE: Cj0688(pta)
            CJR: CJE0787(pta)
            CJJ: CJJ81176_0711(pta)
            CJU: C8J_0656(pta)
            CJD: JJD26997_1319(pta)
            CFF: CFF8240_0813
            CCV: CCV52592_1159
            CHA: CHAB381_1163
            CCO: CCC13826_1128
            ABU: Abu_0493(pta)
            SUN: SUN_1995(pta)
            GSU: GSU2706
            GME: Gmet_1035
            GUR: Gura_2073 Gura_3395 Gura_3484
            PCA: Pcar_2542 Pcar_2850
            PPD: Ppro_1290
            DVU: DVU3029(pta)
            DVL: Dvul_0344
            DDE: Dde_3241
            LIP: LI0279(pta)
            DPS: DP0558
            ADE: Adeh_2896 Adeh_3930
            AFW: Anae109_0502 Anae109_3100
            SFU: Sfum_1472 Sfum_2777
            RPR: RP109
            RTY: RT0027(pta) RT0361(tme)
            RCO: RC0147 RC0507(tme)
            RFE: RF_0096(pta) RF_0584(tme)
            RBE: RBE_0869(tme) RBE_1210 RBE_1211
            RAK: A1C_00825
            RBO: A1I_01120
            PUB: SAR11_0802(pta)
            PLA: Plav_3598
            SME: SMb21532(pta)
            SMD: Smed_0029 Smed_1558 Smed_4674 Smed_4869
            OAN: Oant_0158 Oant_2100 Oant_3501
            BJA: blr3457(pta)
            RPA: RPA4567(pta)
            RPB: RPB_2497
            RPC: RPC_0643 RPC_0834 RPC_1079 RPC_2007 RPC_2337
            RPD: RPD_2946
            RPE: RPE_3275 RPE_3863
            NWI: Nwi_1587
            NHA: Nham_2110
            XAU: Xaut_3143 Xaut_3251
            SIL: SPO0115 SPO3560(pta)
            SIT: TM1040_1573 TM1040_2877
            RSP: RSP_1255 RSP_4009(pta)
            RSH: Rsph17029_0246 Rsph17029_2878
            RSQ: Rsph17025_0274 Rsph17025_2654
            JAN: Jann_0210 Jann_2847
            RDE: RD1_0421(tme) RD1_0821(pta)
            PDE: Pden_0848 Pden_1008 Pden_1640 Pden_2224 Pden_4275
            MMR: Mmar10_1333 Mmar10_3020
            NAR: Saro_3291
            SAL: Sala_2792
            SWI: Swit_1904 Swit_2760
            ACR: Acry_2289
            RRU: Rru_A1378 Rru_A2997 Rru_A3542
            MAG: amb2556
            SUS: Acid_1084 Acid_4539
            BSU: BG10634(pta)
            BHA: BH3823(pta)
            BAN: BA5636(pta)
            BAR: GBAA5636(pta)
            BAA: BA_0493
            BAT: BAS5238
            BCE: BC5387
            BCA: BCE_5516(pta)
            BCZ: BCZK5085(pta)
            BCY: Bcer98_3908
            BTK: BT9727_5068(pta)
            BTL: BALH_1708 BALH_4886(pta)
            BLI: BL03905(pta)
            BLD: BLi03997(pta)
            BCL: ABC3910(pta)
            BAY: RBAM_034850
            BPU: BPUM_2148 BPUM_3415
            OIH: OB3022
            GKA: GK3415
            SAU: SA0545(pta)
            SAV: SAV0588(pta)
            SAM: MW0543(pta)
            SAR: SAR0594(pta)
            SAS: SAS0547
            SAC: SACOL0634(pta)
            SAB: SAB0538(pta)
            SAA: SAUSA300_0570(pta)
            SAO: SAOUHSC_00574
            SAJ: SaurJH9_0611
            SAH: SaurJH1_0626
            SEP: SE0359
            SER: SERP0236(pta)
            SHA: SH2404(pta)
            SSP: SSP2124
            LMO: lmo2103(pta)
            LMF: LMOf2365_2135(pta)
            LIN: lin2207(pta)
            LWE: lwe2124(pta)
            LLA: L107797(pta)
            LLC: LACR_1824
            LLM: llmg_0763(pta)
            SPY: SPy_1128(pta)
            SPZ: M5005_Spy_0851
            SPM: spyM18_1089(pta)
            SPG: SpyM3_0787(pta)
            SPS: SPs0988
            SPH: MGAS10270_Spy0966(pta)
            SPI: MGAS10750_Spy1001(pta)
            SPJ: MGAS2096_Spy0926(pta)
            SPK: MGAS9429_Spy0969(pta)
            SPF: SpyM50938(pta)
            SPA: M6_Spy0848
            SPB: M28_Spy0826(pta)
            SPN: SP_1100
            SPR: spr1007(pta)
            SPD: SPD_0985(pta)
            SAG: SAG1092
            SAN: gbs1159(pta)
            SAK: SAK_1177(pta)
            SMU: SMU.1043c
            STC: str1455(pta)
            STL: stu1455(pta)
            SSA: SSA_1207(pta)
            SGO: SGO_1219(pta)
            LPL: lp_0807(pta)
            LJO: LJ0884
            LAC: LBA0704
            LSA: LSA1343(pta)
            LSL: LSL_1151(pta)
            LDB: Ldb0643(pta)
            LBU: LBUL_0574
            LBR: LVIS_0674
            LCA: LSEI_0996
            LRE: Lreu_0398
            EFA: EF0949(pta)
            OOE: OEOE_1435
            CAC: CAC1742(pta)
            CPE: CPE1725(pta)
            CPF: CPF_1978(pta)
            CPR: CPR_1696(pta)
            CTC: CTC01239
            CNO: NT01CX_2225
            CBO: CBO2459(pta)
            CBA: CLB_2325(pta)
            CBH: CLC_2309(pta)
            CBF: CLI_2517(pta)
            CBE: Cbei_3402
            CKL: CKL_1390(pta)
            CHY: CHY_1456(pta)
            SWO: Swol_0767
            TTE: TTE1482(pta) TTE2204(pta3)
            MGE: MG_299(pta)
            MPN: MPN428(pta)
            MPU: MYPU_2370(pta)
            MPE: MYPE5030(pta)
            MGA: MGA_0432(pta)
            MMY: MSC_0269(pta)
            MMO: MMOB1680(pta)
            MHY: mhp506(pta)
            MHJ: MHJ_0506(pta)
            MHP: MHP7448_0509(pta)
            MSY: MS53_0653(pta)
            MCP: MCAP_0229(pta)
            UUR: UU066(pta)
            MFL: Mfl043
            MTU: Rv0408(pta)
            MTC: MT0421(pta)
            MBO: Mb0416(pta)
            MBB: BCG_0447(pta)
            MPA: MAP3885(pta)
            MAV: MAV_4760
            MSM: MSMEG_0783(pta)
            MVA: Mvan_0700
            MGI: Mflv_0205
            MMC: Mmcs_0537
            MKM: Mkms_0549
            MJL: Mjls_0527
            CGL: NCgl2657(cgl2753)
            CGB: cg3048(pta)
            CEF: CE2591
            CDI: DIP2055(pta)
            CJK: jk0250(pta)
            NFA: nfa53460(pta)
            RHA: RHA1_ro02197(pta)
            SCO: SCO5425(pta)
            SMA: SAV2823(pta)
            LXX: Lxx03410(pta)
            CMI: CMM_0895(ptaA)
            ART: Arth_3240
            NCA: Noca_2954
            KRA: Krad_0857
            STP: Strop_3692
            BLO: BL0968(pta)
            BAD: BAD_0688(pta)
            FNU: FN1172
            RBA: RB9654(pta)
            BGA: BG0602(pta)
            BAF: BAPKO_0620(pta)
            TPA: TP0094
            TDE: TDE0042(pta)
            SYN: slr2132(pta)
            SYG: sync_2172
            BTH: BT_3692
            BFR: BF0478
            BFS: BF0423(ptaA) BF4138
            PGI: PG1082(pta)
            FJO: Fjoh_0748 Fjoh_1651 Fjoh_3529
            RRS: RoseRS_1806
            DRA: DR_0073
            DGE: Dgeo_0051
            TMA: TM1130
            TPT: Tpet_1615
            MAC: MA3607(pta)
            MBA: Mbar_A1821
            MMA: MM_0496
            HWA: HQ2736A(mdh)
            NPH: NP0132A(mdh_1) NP1772A(mdh_2)
STRUCTURES  PDB: 1QZT  1R5J  1TD9  1VMI  1XCO  2AF3  2AF4  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.8
            ExPASy - ENZYME nomenclature database: 2.3.1.8
            ExplorEnz - The Enzyme Database: 2.3.1.8
            ERGO genome analysis and discovery system: 2.3.1.8
            UM-BBD (Biocatalysis/Biodegradation Database): 2.3.1.8
            BRENDA, the Enzyme Database: 2.3.1.8
            CAS: 9029-91-8
///
ENTRY       EC 2.3.1.9                  Enzyme
NAME        acetyl-CoA C-acetyltransferase;
            acetoacetyl-CoA thiolase;
            beta-acetoacetyl coenzyme A thiolase;
            2-methylacetoacetyl-CoA thiolase [misleading];
            3-oxothiolase;
            acetyl coenzyme A thiolase;
            acetyl-CoA acetyltransferase;
            acetyl-CoA:N-acetyltransferase;
            thiolase II
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:acetyl-CoA C-acetyltransferase
REACTION    2 acetyl-CoA = CoA + acetoacetyl-CoA [RN:R00238]
ALL_REAC    R00238;
            (other) R01177
SUBSTRATE   acetyl-CoA [CPD:C00024]
PRODUCT     CoA [CPD:C00010];
            acetoacetyl-CoA [CPD:C00332]
REFERENCE   1  [PMID:13115439]
  AUTHORS   LYNEN F, OCHOA S.
  TITLE     Enzymes of fatty acid metabolism.
  JOURNAL   Biochim. Biophys. Acta. 12 (1953) 299-314.
  ORGANISM  Clostridium kluyveri
REFERENCE   2
  AUTHORS   Stern, J.R., Drummond, G.I., Coon, M.J. and del Campillo, A.
  TITLE     Enzymes of ketone body metabolism. I. Purification of an
            acetoacetate-synthesizing enzyme from ox liver.
  JOURNAL   J. Biol. Chem. 235 (1960) 313-317.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00071  Fatty acid metabolism
            PATH: map00072  Synthesis and degradation of ketone bodies
            PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00310  Lysine degradation
            PATH: map00380  Tryptophan metabolism
            PATH: map00620  Pyruvate metabolism
            PATH: map00632  Benzoate degradation via CoA ligation
            PATH: map00640  Propanoate metabolism
            PATH: map00650  Butanoate metabolism
            PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K00626  acetyl-CoA C-acetyltransferase
GENES       HSA: 38(ACAT1) 39(ACAT2)
            PTR: 451528(ACAT1)
            MMU: 110446(Acat1) 110460(Acat2)
            RNO: 25014(Acat1)
            CFA: 484063(ACAT2) 489421(ACAT1)
            GGA: 418968(ACAT1) 421587(RCJMB04_34i5)
            XLA: 379569(MGC69098) 414622(MGC81403) 414639(MGC81256)
                 444457(MGC83664)
            XTR: 394562(acat2)
            DRE: 30643(acat2)
            SPU: 759502(LOC759502)
            DME: Dmel_CG10932 Dmel_CG9149
            CEL: T02G5.4 T02G5.7 T02G5.8(kat-1)
            ATH: AT5G48230(ACAT2/EMB1276)
            OSA: 4326136 4346520
            CME: CMA042C CME087C
            SCE: YPL028W(ERG10)
            AGO: AGOS_ADR165C
            PIC: PICST_31707(ERG10)
            CAL: CaO19.1591(erg10)
            CGR: CAGL0L12364g
            SPO: SPBC215.09c
            ANI: AN1409.2
            AFM: AFUA_6G14200 AFUA_8G04000
            AOR: AO090103000012 AO090103000406
            CNE: CNC05280
            UMA: UM03571.1
            DDI: DDB_0231621
            PFA: PF14_0484
            TET: TTHERM_00091590 TTHERM_00277470 TTHERM_00926980
            TCR: 511003.60
            ECO: b2224(atoB)
            ECJ: JW2218(atoB) JW5453(yqeF)
            ECE: Z4164(yqeF)
            ECS: ECs3701
            ECC: c2767(atoB) c3441(yqeF)
            ECI: UTI89_C2506(atoB) UTI89_C3247(yqeF)
            ECP: ECP_2268 ECP_2857
            ECV: APECO1_3662(yqeF) APECO1_4335(atoB) APECO1_43352(atoB)
            ECX: EcHS_A2365
            STY: STY3164(yqeF)
            STT: t2929(yqeF)
            SPT: SPA2886(yqeF)
            SEC: SC2958(yqeF)
            STM: STM3019(yqeF)
            SFL: SF2854(yqeF)
            SFX: S3052(yqeF)
            SFV: SFV_2922(yqeF)
            SSN: SSON_2283(atoB) SSON_3004(yqeF)
            SBO: SBO_2736(yqeF)
            ECA: ECA1282(atoB)
            ENT: Ent638_3299
            SPE: Spro_0592
            HIT: NTHI0932(atoB)
            XCC: XCC1297(atoB)
            XCB: XC_2943
            XCV: XCV1401(thlA)
            XAC: XAC1348(atoB)
            XOO: XOO1881(atoB)
            XOM: XOO_1778(XOO1778)
            VCH: VCA0690
            VCO: VC0395_0630
            VVU: VV2_0494 VV2_0741
            VVY: VVA1043 VVA1210
            VPA: VPA0620 VPA1123 VPA1204
            PPR: PBPRB1112 PBPRB1840
            PAE: PA2001(atoB) PA2553 PA3454 PA3589 PA3925
            PAU: PA14_38630(atoB)
            PPU: PP_2051(atoB) PP_2215(fadAx) PP_3754 PP_4636
            PPF: Pput_2009 Pput_2403 Pput_3523 Pput_4498
            PST: PSPTO_0957(phbA-1) PSPTO_3164(phbA-2)
            PSB: Psyr_0824 Psyr_3031
            PSP: PSPPH_0850(phbA1) PSPPH_2209(phbA2)
            PFL: PFL_1478(atoB-2) PFL_2321 PFL_3066 PFL_4330(atoB-2) PFL_5283
            PFO: Pfl_1269 Pfl_1739 Pfl_2074 Pfl_2868
            PEN: PSEEN3197 PSEEN3547(fadAx) PSEEN4635(phbA)
            PMY: Pmen_1138 Pmen_2036 Pmen_3597 Pmen_3662 Pmen_3820
            PAR: Psyc_0252 Psyc_1169
            PCR: Pcryo_0278 Pcryo_1236 Pcryo_1260
            PRW: PsycPRwf_2011
            ACI: ACIAD0694 ACIAD1612 ACIAD2516(atoB)
            SON: SO_1677(atoB)
            SDN: Sden_1943
            SFR: Sfri_1338 Sfri_2063
            SAZ: Sama_1375
            SBL: Sbal_1495
            SBM: Shew185_1489
            SLO: Shew_1667 Shew_2858
            SPC: Sputcn32_1397
            SSE: Ssed_1473 Ssed_3533
            SPL: Spea_2783
            SHE: Shewmr4_2597
            SHM: Shewmr7_2664
            SHN: Shewana3_2771
            SHW: Sputw3181_2704
            ILO: IL0872
            CPS: CPS_1605 CPS_2626
            PHA: PSHAa0908 PSHAa1454(atoB) PSHAa1586(atoB)
            PAT: Patl_2923
            SDE: Sde_3149
            PIN: Ping_0659 Ping_2401
            MAQ: Maqu_2117 Maqu_2489 Maqu_2696 Maqu_3162
            CBU: CBU_0974
            LPN: lpg1825(atoB)
            LPF: lpl1789
            LPP: lpp1788
            FTW: FTW_0400
            NOC: Noc_1891
            AEH: Mlg_0688 Mlg_2706
            HHA: Hhal_1685
            HCH: HCH_05299
            CSA: Csal_0301 Csal_3068
            ABO: ABO_0648(fadAx)
            MMW: Mmwyl1_0073 Mmwyl1_3021 Mmwyl1_3053 Mmwyl1_3097 Mmwyl1_4182
            AHA: AHA_2143(atoB)
            CVI: CV_2088(atoB) CV_2790(phaA)
            RSO: RSc0276(atoB) RSc1632(phbA) RSc1637(bktB) RSc1761(RS02948)
            REU: Reut_A0138 Reut_A1348 Reut_A1353 Reut_B4561 Reut_B4738
                 Reut_B5587 Reut_C5943 Reut_C6062
            REH: H16_A0170 H16_A0867 H16_A0868 H16_A0872 H16_A1297
                 H16_A1438(phaA) H16_A1445(bktB) H16_A1528 H16_A1713 H16_A1720
                 H16_A1887 H16_A2148 H16_B0380 H16_B0381 H16_B0406 H16_B0662
                 H16_B0668 H16_B0759 H16_B1369 H16_B1771
            RME: Rmet_0106 Rmet_1357 Rmet_1362 Rmet_5156
            BMA: BMA1316 BMA1321(phbA) BMA1436
            BMV: BMASAVP1_A1805(bktB) BMASAVP1_A1810(phbA)
            BML: BMA10299_A0086(phbA) BMA10299_A0091
            BMN: BMA10247_1076(bktB) BMA10247_1081(phbA)
            BXE: Bxe_A2273 Bxe_A2335 Bxe_A2342 Bxe_A4255 Bxe_B0377 Bxe_B0739
                 Bxe_C0332 Bxe_C0574 Bxe_C0915
            BVI: Bcep1808_0519 Bcep1808_1717 Bcep1808_2877 Bcep1808_3594
                 Bcep1808_4015 Bcep1808_5507 Bcep1808_5644
            BUR: Bcep18194_A3629 Bcep18194_A5080 Bcep18194_A5091
                 Bcep18194_A6102 Bcep18194_B0263 Bcep18194_B1439
                 Bcep18194_C6652 Bcep18194_C6802 Bcep18194_C6874
                 Bcep18194_C7118 Bcep18194_C7151 Bcep18194_C7332
            BCN: Bcen_1553 Bcen_1599 Bcen_2158 Bcen_2563 Bcen_2998 Bcen_6289
            BCH: Bcen2424_0542 Bcen2424_1790 Bcen2424_2772 Bcen2424_5368
                 Bcen2424_6232 Bcen2424_6276
            BAM: Bamb_0447 Bamb_1728 Bamb_2824 Bamb_4717 Bamb_5771 Bamb_5969
            BPS: BPSL1426 BPSL1535(phbA) BPSL1540
            BPM: BURPS1710b_2325(bktB) BURPS1710b_2330(phbA)
                 BURPS1710b_2453(atoB-2)
            BPL: BURPS1106A_2197(bktB) BURPS1106A_2202(phbA)
            BPD: BURPS668_2160(bktB) BURPS668_2165(phbA)
            BTE: BTH_I2144 BTH_I2256 BTH_I2261
            PNU: Pnuc_0927
            BPE: BP0447 BP0668 BP2059
            BPA: BPP0608 BPP1744 BPP3805 BPP4216 BPP4361
            BBR: BB0614 BB3364 BB4250 BB4804 BB4947
            RFR: Rfer_0272 Rfer_1000 Rfer_1871 Rfer_2273 Rfer_2561 Rfer_2594
                 Rfer_3839
            POL: Bpro_1577 Bpro_2140 Bpro_3113 Bpro_4187
            PNA: Pnap_0060 Pnap_0458 Pnap_0867 Pnap_1159 Pnap_2136 Pnap_2804
            AAV: Aave_0031 Aave_2478 Aave_3944 Aave_4368
            AJS: Ajs_0014 Ajs_0124 Ajs_1931 Ajs_2073 Ajs_2317 Ajs_3548
                 Ajs_3738 Ajs_3776
            VEI: Veis_1331 Veis_3818 Veis_4193
            MPT: Mpe_A1536 Mpe_A1776 Mpe_A1869 Mpe_A3367
            HAR: HEAR0577(phbA)
            MMS: mma_0555
            NEU: NE2262(bktB)
            NET: Neut_0610
            EBA: ebA5202 p2A409(tioL)
            AZO: azo2172(thlA)
            DAR: Daro_0098 Daro_3022
            HPY: HP0690(fadA)
            HPA: HPAG1_0675
            HAC: Hac_0958(atoB)
            GME: Gmet_1719 Gmet_2074 Gmet_2213 Gmet_2268 Gmet_3302
            GUR: Gura_3043
            BBA: Bd0404(atoB) Bd2095
            ADE: Adeh_0062 Adeh_2365
            AFW: Anae109_0064 Anae109_1504
            MXA: MXAN_3791
            SAT: SYN_02642
            SFU: Sfum_2280 Sfum_3582
            RPR: RP737
            RCO: RC1134 RC1135
            RFE: RF_0163(paaJ)
            RBE: RBE_0139(paaJ)
            RAK: A1C_05820
            RBO: A1I_07215
            RCM: A1E_04760
            PUB: SAR11_0428(thlA)
            MLO: mlr3847
            MES: Meso_3374
            PLA: Plav_1573 Plav_2783
            SME: SMa1450 SMc03879(phbA)
            SMD: Smed_0499 Smed_3117 Smed_5094 Smed_5096
            ATU: Atu2769(atoB) Atu3475
            ATC: AGR_C_5022(phbA) AGR_L_2713
            RET: RHE_CH04018(phbAch) RHE_PC00068(ypc00040) RHE_PF00014(phbAf)
            RLE: RL4621(phaA) pRL100301 pRL120369
            BME: BMEI0274 BMEII0817
            BMF: BAB1_1783(phbA-1) BAB2_0790(phbA-2)
            BMS: BR1772(phbA-1) BRA0448(phbA-2)
            BMB: BruAb1_1756(phbA-1) BruAb2_0774(phbA-2)
            BOV: BOV_1707(phbA-1)
            OAN: Oant_1130 Oant_3107 Oant_3718 Oant_4020
            BJA: bll0226(atoB) bll3949 bll7400 bll7819 blr3724(phbA)
            BRA: BRADO0562(phbA) BRADO0983(pimB) BRADO3110 BRADO3134(atoB)
            BBT: BBta_3558 BBta_3575(atoB) BBta_5147(pimB) BBta_7072(pimB)
                 BBta_7614(phbA)
            RPA: RPA0513(pcaF) RPA0531 RPA3715(pimB)
            RPB: RPB_0509 RPB_0525 RPB_1748
            RPC: RPC_0504 RPC_0636 RPC_0641 RPC_0832 RPC_1050 RPC_2005
                 RPC_2194 RPC_2228
            RPD: RPD_0306 RPD_0320 RPD_3105 RPD_3306
            RPE: RPE_0168 RPE_0248 RPE_3827
            NWI: Nwi_3060
            XAU: Xaut_3108 Xaut_4665
            CCR: CC_0510 CC_0894 CC_3462
            SIL: SPO0142(bktB) SPO0326(phbA) SPO0773 SPO3408
            SIT: TM1040_0067 TM1040_2790 TM1040_3026 TM1040_3735
            RSP: RSP_0745 RSP_1354 RSP_3184
            RSH: Rsph17029_0022 Rsph17029_2401 Rsph17029_3179 Rsph17029_3921
            RSQ: Rsph17025_0012 Rsph17025_2466 Rsph17025_2833
            JAN: Jann_0262 Jann_0493 Jann_4050
            RDE: RD1_0025 RD1_0201(bktB) RD1_3394(phbA)
            PDE: Pden_2026 Pden_2663 Pden_2870 Pden_2907 Pden_4811 Pden_5022
            MMR: Mmar10_0697
            HNE: HNE_2706 HNE_3065 HNE_3133
            NAR: Saro_0809 Saro_1069 Saro_1222 Saro_2306 Saro_2349
            SAL: Sala_0781 Sala_1244 Sala_2896 Sala_3158
            SWI: Swit_0632 Swit_0752 Swit_2893 Swit_3602 Swit_4887 Swit_5019
                 Swit_5309
            ELI: ELI_01475 ELI_06705 ELI_12035
            GBE: GbCGDNIH1_0447
            ACR: Acry_1847 Acry_2256
            RRU: Rru_A0274 Rru_A1380 Rru_A1469 Rru_A1946 Rru_A3387
            MAG: amb0842
            MGM: Mmc1_1165
            ABA: Acid345_3239
            BSU: BG11319(mmgA) BG13063(yhfS)
            BHA: BH1997 BH2029 BH3801(mmgA)
            BAN: BA3687 BA4240 BA5589
            BAR: GBAA3687 GBAA4240 GBAA5589
            BAA: BA_0445 BA_4172 BA_4700
            BAT: BAS3418 BAS3932 BAS5193
            BCE: BC3627 BC4023 BC5344
            BCA: BCE_3646 BCE_4076 BCE_5475
            BCZ: BCZK3329(mmgA) BCZK3780(thl) BCZK5044(atoB)
            BCY: Bcer98_2722 Bcer98_3865
            BTK: BT9727_3379(mmgA) BT9727_3765(thl) BT9727_5028(atoB)
            BTL: BALH_3262(mmgA) BALH_3642(fadA) BALH_4843(atoB)
            BLI: BL03925(mmgA)
            BLD: BLi03968(mmgA)
            BCL: ABC0345 ABC3617 ABC3891(mmgA)
            BAY: RBAM_022450
            BPU: BPUM_2374(yhfS) BPUM_2941 BPUM_3373
            OIH: OB0676 OB0689 OB2632 OB3013
            GKA: GK1658 GK3397
            SAU: SA0342 SA0534(vraB)
            SAV: SAV0354 SAV0576(vraB)
            SAM: MW0330 MW0531(vraB)
            SAR: SAR0351(thl) SAR0581
            SAS: SAS0330 SAS0534
            SAC: SACOL0426 SACOL0622(atoB)
            SAB: SAB0304(th1) SAB0526
            SAA: SAUSA300_0355 SAUSA300_0560(vraB)
            SAO: SAOUHSC_00336 SAOUHSC_00558
            SAJ: SaurJH9_0402
            SAH: SaurJH1_0412
            SEP: SE0346 SE2384
            SER: SERP0032 SERP0220
            SHA: SH0510(mvaC) SH2417
            SSP: SSP0325 SSP2145
            LMO: lmo1414
            LMF: LMOf2365_1433
            LIN: lin1453
            LWE: lwe1431
            LLA: L11745(thiL) L25946(fadA)
            LLC: LACR_1665 LACR_1956
            LLM: llmg_0930(thiL)
            SPY: SPy_0140 SPy_1637(atoB)
            SPZ: M5005_Spy_0119 M5005_Spy_0432 M5005_Spy_1344(atoB)
            SPM: spyM18_0136 spyM18_1645(atoB)
            SPG: SpyM3_0108 SpyM3_1378(atoB)
            SPS: SPs0110 SPs0484
            SPH: MGAS10270_Spy0121 MGAS10270_Spy0433 MGAS10270_Spy1461(atoB)
            SPI: MGAS10750_Spy0124 MGAS10750_Spy0452 MGAS10750_Spy1453(atoB)
            SPJ: MGAS2096_Spy0123 MGAS2096_Spy0451 MGAS2096_Spy1365(atoB)
            SPK: MGAS9429_Spy0121 MGAS9429_Spy0431 MGAS9429_Spy1339(atoB)
            SPF: SpyM50447(atoB2)
            SPA: M6_Spy0166 M6_Spy0466 M6_Spy1390
            SPB: M28_Spy0117 M28_Spy0420 M28_Spy1385(atoB)
            SAK: SAK_0568
            LJO: LJ1609
            LAC: LBA0626(thiL)
            LSA: LSA1486
            LDB: Ldb0879
            LBU: LBUL_0804
            LBR: LVIS_2218
            LCA: LSEI_1787
            LRE: Lreu_0052
            EFA: EF1364
            OOE: OEOE_0529
            STH: STH2913 STH725 STH804
            CAC: CAC2873 CA_P0078(thiL)
            CPE: CPE2195(atoB)
            CPF: CPF_2460
            CPR: CPR_2170
            CTC: CTC00312
            CNO: NT01CX_0538 NT01CX_0603
            CDF: CD1059(thlA1) CD2676(thlA2)
            CBO: CBO3200(thl)
            CBE: Cbei_0411 Cbei_3630
            CKL: CKL_3696(thlA1) CKL_3697(thlA2) CKL_3698(thlA3)
            AMT: Amet_4630
            CHY: CHY_1288 CHY_1355(atoB) CHY_1604 CHY_1738
            DSY: DSY0632 DSY0639 DSY1567 DSY1710 DSY2402 DSY3302
            DRM: Dred_0400 Dred_1491 Dred_1784 Dred_1892
            SWO: Swol_0308 Swol_0675 Swol_0789 Swol_1486 Swol_1934 Swol_2051
            TTE: TTE0549(paaJ)
            MTA: Moth_1260
            MTU: Rv1135A Rv1323(fadA4) Rv3546(fadA5)
            MTC: MT1365(phbA)
            MBO: Mb1167 Mb1358(fadA4) Mb3576(fadA5) Mb3586c(fadA6)
            MBB: BCG_1197 BCG_1385(fadA4) BCG_3610(fadA5) BCG_3620c(fadA6)
            MLE: ML1158(fadA4)
            MPA: MAP2407c(fadA3) MAP2436c(fadA4)
            MAV: MAV_1544 MAV_1863 MAV_5081
            MSM: MSMEG_2224 MSMEG_4920
            MVA: Mvan_1976 Mvan_1988 Mvan_4305 Mvan_4677 Mvan_4891
            MGI: Mflv_1347 Mflv_1484 Mflv_2040 Mflv_2340 Mflv_4356 Mflv_4368
            MMC: Mmcs_1758 Mmcs_1769 Mmcs_3796 Mmcs_3864
            MKM: Mkms_1805 Mkms_1816 Mkms_3869 Mkms_3938
            MJL: Mjls_1739 Mjls_1750 Mjls_3800 Mjls_3850 Mjls_4110 Mjls_4383
            CGL: NCgl2309(cgl2392)
            CGB: cg2625(pcaF)
            CEF: CE0731 CE2295
            CJK: jk1543(fadA3)
            NFA: nfa10750(fadA4)
            RHA: RHA1_ro01455 RHA1_ro01623 RHA1_ro01876 RHA1_ro02517(catF)
                 RHA1_ro03022 RHA1_ro03024 RHA1_ro03391 RHA1_ro03892
                 RHA1_ro04599 RHA1_ro05257 RHA1_ro08871
            SCO: SCO5399(SC8F4.03)
            SMA: SAV1384(fadA5) SAV2856(fadA1)
            ART: Arth_1160 Arth_2986 Arth_3268 Arth_4073
            NCA: Noca_1371 Noca_1797 Noca_1828 Noca_2764 Noca_4142
            TFU: Tfu_1520 Tfu_2394
            FRA: Francci3_3687
            FAL: FRAAL2514 FRAAL2618 FRAAL5910(atoB)
            ACE: Acel_0626 Acel_0672
            SEN: SACE_1192(mmgA) SACE_2736(fadA6) SACE_4011(catF)
                 SACE_6236(fadA4)
            STP: Strop_3610
            RXY: Rxyl_1582 Rxyl_1842 Rxyl_2389 Rxyl_2530
            FNU: FN0495
            BGA: BG0110(fadA)
            BAF: BAPKO_0110(fadA)
            LIL: LA0457(thiL1) LA0828(thiL2)
            LIC: LIC10396(phbA)
            LBJ: LBJ_2862(paaJ-4)
            LBL: LBL_0209(paaJ-4)
            SYN: slr1993(phaA)
            SRU: SRU_1211(atoB) SRU_1547
            CHU: CHU_1910(atoB)
            GFO: GFO_1507(atoB)
            FJO: Fjoh_4612
            FPS: FP0770 FP1586 FP1725
            RRS: RoseRS_3911 RoseRS_4348
            RCA: Rcas_0702 Rcas_3206
            DRA: DR_1072 DR_1428 DR_1960 DR_2480 DR_A0053
            DGE: Dgeo_0755 Dgeo_1305 Dgeo_1441 Dgeo_1883
            TTH: TTC0191 TTC0330
            TTJ: TTHA0559
            TME: Tmel_1134
            FNO: Fnod_0314
            HMA: rrnAC0896(acaB3) rrnAC2815(aca2) rrnAC3497(yqeF)
                 rrnB0240(aca1) rrnB0242(acaB2) rrnB0309(acaB1)
            TAC: Ta0582
            TVO: TVN0649
            PTO: PTO1505
            APE: APE_2108
            SSO: SSO2377(acaB-4)
            STO: ST0514
            SAI: Saci_0963 Saci_1361(acaB1)
            MSE: Msed_0656
            PAI: PAE1220
            PIS: Pisl_0029 Pisl_1301
            PCL: Pcal_0781
            PAS: Pars_0309 Pars_1071
STRUCTURES  PDB: 1DLU  1DLV  1DM3  1M1O  1M1T  1M3K  1M3Z  1M4S  1M4T  1NL7  
                 1OU6  1QFL  1WL4  1WL5  2F2S  2IB7  2IB8  2IB9  2IBU  2IBW  
                 2IBY  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.9
            ExPASy - ENZYME nomenclature database: 2.3.1.9
            ExplorEnz - The Enzyme Database: 2.3.1.9
            ERGO genome analysis and discovery system: 2.3.1.9
            UM-BBD (Biocatalysis/Biodegradation Database): 2.3.1.9
            BRENDA, the Enzyme Database: 2.3.1.9
            CAS: 9027-46-7
///
ENTRY       EC 2.3.1.10                 Enzyme
NAME        hydrogen-sulfide S-acetyltransferase;
            hydrogen-sulfide acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:hydrogen-sulfide S-acetyltransferase
REACTION    acetyl-CoA + hydrogen sulfide = CoA + thioacetate [RN:R01850]
ALL_REAC    R01850
SUBSTRATE   acetyl-CoA [CPD:C00024];
            hydrogen sulfide [CPD:C00283]
PRODUCT     CoA [CPD:C00010];
            thioacetate [CPD:C01857]
REFERENCE   1  [PMID:13221570]
  AUTHORS   BRADY RO, STADTMAN ER.
  TITLE     Enzymatic thioltransacetylation.
  JOURNAL   J. Biol. Chem. 211 (1954) 621-9.
  ORGANISM  Clostridium kluyveri, pigeon
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.10
            ExPASy - ENZYME nomenclature database: 2.3.1.10
            ExplorEnz - The Enzyme Database: 2.3.1.10
            ERGO genome analysis and discovery system: 2.3.1.10
            BRENDA, the Enzyme Database: 2.3.1.10
            CAS: 9029-92-9
///
ENTRY       EC 2.3.1.11                 Enzyme
NAME        thioethanolamine S-acetyltransferase;
            thioltransacetylase B;
            thioethanolamine acetyltransferase;
            acetyl-CoA:thioethanolamine S-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:2-aminoethanethiol S-acetyltransferase
REACTION    acetyl-CoA + 2-aminoethanethiol = CoA + S-(2-aminoethyl)thioacetate
            [RN:R03668]
ALL_REAC    R03668
SUBSTRATE   acetyl-CoA [CPD:C00024];
            2-aminoethanethiol [CPD:C01678]
PRODUCT     CoA [CPD:C00010];
            S-(2-aminoethyl)thioacetate
COMMENT     2-Sulfanylethanol (2-mercaptoethanol) can act as a substrate [1].
REFERENCE   1  [PMID:13221570]
  AUTHORS   BRADY RO, STADTMAN ER.
  TITLE     Enzymatic thioltransacetylation.
  JOURNAL   J. Biol. Chem. 211 (1954) 621-9.
  ORGANISM  Clostridium kluyveri, pigeon
REFERENCE   2
  AUTHORS   Gunsalus, I.C.
  TITLE     Group transfer and acyl-generating functions of lipoic acid
            derivatives.
  JOURNAL   In: McElroy, W.D. and Glass, B. (Eds.), A Symposium on the Mechanism
            of Enzyme Action, Johns Hopkins Press, Baltimore, 1954, p. 545-580.
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.11
            ExPASy - ENZYME nomenclature database: 2.3.1.11
            ExplorEnz - The Enzyme Database: 2.3.1.11
            ERGO genome analysis and discovery system: 2.3.1.11
            BRENDA, the Enzyme Database: 2.3.1.11
            CAS: 9029-93-0
///
ENTRY       EC 2.3.1.12                 Enzyme
NAME        dihydrolipoyllysine-residue acetyltransferase;
            acetyl-CoA:dihydrolipoamide S-acetyltransferase;
            dihydrolipoamide S-acetyltransferase;
            dihydrolipoate acetyltransferase;
            dihydrolipoic transacetylase;
            dihydrolipoyl acetyltransferase;
            lipoate acetyltransferase;
            lipoate transacetylase;
            lipoic acetyltransferase;
            lipoic acid acetyltransferase;
            lipoic transacetylase;
            lipoylacetyltransferase;
            thioltransacetylase A;
            transacetylase X;
            enzyme-dihydrolipoyllysine:acetyl-CoA S-acetyltransferase;
            acetyl-CoA:enzyme 6-N-(dihydrolipoyl)lysine S-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:enzyme N6-(dihydrolipoyl)lysine S-acetyltransferase
REACTION    acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme
            N6-(S-acetyldihydrolipoyl)lysine [RN:R02569]
ALL_REAC    R02569;
            (other) R00209
SUBSTRATE   acetyl-CoA [CPD:C00024];
            enzyme N6-(dihydrolipoyl)lysine [CPD:C15973]
PRODUCT     CoA [CPD:C00010];
            enzyme N6-(S-acetyldihydrolipoyl)lysine
COMMENT     A multimer (24-mer or 60-mer, depending on the source) of this
            enzyme forms the core of the pyruvate dehydrogenase multienzyme
            complex, and binds tightly both EC 1.2.4.1, pyruvate dehydrogenase
            (acetyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase.
            The lipoyl group of this enzyme is reductively acetylated by EC
            1.2.4.1, and the only observed direction catalysed by EC 2.3.1.12 is
            that where the acetyl group is passed to coenzyme A.
REFERENCE   1  [PMID:13221570]
  AUTHORS   BRADY RO, STADTMAN ER.
  TITLE     Enzymatic thioltransacetylation.
  JOURNAL   J. Biol. Chem. 211 (1954) 621-9.
  ORGANISM  pigeon
REFERENCE   2
  AUTHORS   Gunsalus, I.C.
  TITLE     Group transfer and acyl-generating functions of lipoic acid
            derivatives.
  JOURNAL   In: McElroy, W.D. and Glass, B. (Eds.), A Symposium on the Mechanism
            of Enzyme Action, Johns Hopkins Press, Baltimore, 1954, p. 545-580.
REFERENCE   3
  AUTHORS   Gunsalus, I.C., Barton, L.S. and Gruber, W.
  TITLE     Biosynthesis and structure of lipoic acid derivatives.
  JOURNAL   J. Am. Chem. Soc. 78 (1956) 1763-1766.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:10966480]
  AUTHORS   Perham RN.
  TITLE     Swinging arms and swinging domains in multifunctional enzymes:
            catalytic machines for multistep reactions.
  JOURNAL   Annu. Rev. Biochem. 69 (2000) 961-1004.
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00252  Alanine and aspartate metabolism
            PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K00627  pyruvate dehydrogenase E2 component (dihydrolipoamide
                        acetyltransferase)
GENES       HSA: 1737(DLAT)
            PTR: 451120(PDHX) 466780(DLAT)
            MMU: 235339(Dlat)
            RNO: 81654(Dlat)
            CFA: 475942(PDHX) 489406(DLAT)
            SSC: 397054(DLAT)
            GGA: 419796(DLAT) 423154(RCJMB04_17g4)
            XLA: 447247(MGC86218)
            DRE: 324201(dlat)
            SPU: 757556(LOC757556)
            CEL: C30H6.7 F23B12.5 ZK669.4
            OSA: 4339859 4341113 4343003 4351678
            CME: CMI273C CMN017C CMN233C
            SCE: YNL071W(LAT1)
            AGO: AGOS_AER364W
            PIC: PICST_68297(KGD2) PICST_81177(PDX1) PICST_82614(LAT1)
            CGR: CAGL0J10186g
            SPO: SPCC794.07
            ANI: AN6708.2
            AFM: AFUA_7G05720
            AOR: AO090005000436
            CNE: CND02450
            UMA: UM00594.1
            DDI: DDB_0215387(pdhC)
            PFA: PF10_0407
            TET: TTHERM_00530750
            TBR: Tb10.6k15.3080 Tb10.70.5380
            TCR: 509717.20 510105.170 511367.70
            LMA: LmjF21.0550 LmjF36.2660
            ECO: b0115(aceF)
            ECJ: JW0111(aceF)
            ECE: Z0125(aceF)
            ECS: ECs0119
            ECI: UTI89_C0128(aceF)
            ECP: ECP_0122
            ECV: APECO1_1870(aceF)
            ECW: EcE24377A_0117(aceF)
            ECX: EcHS_A0119
            STY: STY0176(aceF)
            STT: t0159(aceF)
            SPT: SPA0157(aceF)
            SEC: SC0152(aceF)
            STM: STM0153(aceF)
            YPE: YPO3418(aceF)
            YPK: y0768(aceF)
            YPM: YP_0266(aceF)
            YPA: YPA_2920
            YPN: YPN_0670
            YPS: YPTB0714(aceF)
            YPI: YpsIP31758_3362(aceF)
            YEN: YE0701(aceF)
            SFL: SF0112(aceF)
            SFX: S0114(aceF)
            SFV: SFV_0106(aceF)
            SSN: SSON_0123(aceF)
            SBO: SBO_0104(aceF)
            SDY: SDY_0145(aceF)
            ECA: ECA3788(aceF)
            PLU: plu3622(aceF)
            BUC: BU206(aceF)
            BAS: BUsg200(aceF)
            BAB: bbp190(aceF)
            BCC: BCc_132(aceF)
            WBR: WGLp322(aceF)
            SGL: SG0468
            BFL: Bfl152(aceF)
            BPN: BPEN_157(aceF)
            HIN: HI1232(aceF)
            HIT: NTHI1934(aceF)
            HDU: HD1624(aceF)
            HSO: HS_1094(aceF)
            PMU: PM0894(aceF)
            MSU: MS1335(aceF)
            APL: APL_0772(aceF)
            XFA: XF0869
            XFT: PD1809(pdhB)
            XCC: XCC0427(pdhB) XCC0542(phdB)
            XCB: XC_0441 XC_3691
            XCV: XCV0473 XCV3779
            XAC: XAC0443(pdhB) XAC3661(phdB)
            XOO: XOO0720(phdB)
            XOM: XOO_0656(XOO0656)
            VCH: VC2413
            VCO: VC0395_A1989(aceF)
            VVU: VV1_1631 VV2_0471
            VVY: VV2772 VVA1023
            VPA: VP2518 VPA0645
            VFI: VF2179
            PPR: PBPRA3195 PBPRB1096
            PAE: PA2249(bkdB) PA3415 PA4152 PA5016(aceF)
            PAU: PA14_66310(aceF)
            PAP: PSPA7_5752(aceF)
            PPU: PP_0338(aceF) PP_0553(acoC) PP_4403(bkdB)
            PST: PSPTO_5006(aceF)
            PSB: Psyr_0517
            PSP: PSPPH_0507(aceF)
            PFL: PFL_0508(aceF) PFL_2172(acoC)
            PFO: Pfl_0462
            PAR: Psyc_1327(aceF)
            ACI: ACIAD1019(acoC) ACIAD3506(aceF)
            SON: SO_0425(aceF) SO_2341
            SDN: Sden_1788
            SHN: Shewana3_0427 Shewana3_2129
            ILO: IL1678
            CPS: CPS_1584 CPS_4806(aceF)
            PHA: PSHAa0392(aceF)
            SDE: Sde_2572
            CBU: CBU_0462(pdhC) CBU_0638
            CBD: COXBU7E912_0649(pdhC) COXBU7E912_1613(aceF)
            LPN: lpg1503(aceF) lpg1560
            LPF: lpl1466 lpl1523(aceF)
            LPP: lpp1460(aceF) lpp1517
            MCA: MCA3001(aceF)
            FTU: FTT1484c(aceF)
            FTF: FTF1484c(aceF)
            FTW: FTW_0809(aceF)
            FTL: FTL_0310
            FTH: FTH_0311(aceF)
            FTA: FTA_0329(aceF)
            FTN: FTN_1493(aceF)
            TCX: Tcr_1002
            NOC: Noc_1255
            HCH: HCH_01273(aceF) HCH_03685(sucB1)
            CSA: Csal_0856
            ABO: ABO_0623(aceF) ABO_1197
            AHA: AHA_2564 AHA_2865 AHA_3862(aceF)
            DNO: DNO_0545(aceF)
            BCI: BCI_0511(aceF)
            VOK: COSY_0863(aceF)
            NME: NMB1342
            NMA: NMA1555(aceF)
            NMC: NMC1279(aceF)
            NGO: NGO0564
            CVI: CV_0527(aceF)
            RSO: RSc1601(aceF) RSc1799(RS04200)
            REU: Reut_A1304 Reut_B4978 Reut_B5552
            REH: H16_A1375(pdhB) H16_B0146(acoC)
            RME: Rmet_1197 Rmet_4132
            BMA: BMA1720(aceF) BMAA2011
            BMV: BMASAVP1_A2229(aceF)
            BML: BMA10299_A3091(aceF)
            BMN: BMA10247_1501(aceF)
            BXE: Bxe_A1542 Bxe_B0315 Bxe_C0854
            BUR: Bcep18194_A5138
            BAM: Bamb_1775 Bamb_2173
            BPS: BPSL2300(pdhB) BPSS2271(bkdB)
            BPM: BURPS1710b_2744(aceF) BURPS1710b_A1409(bkdB)
            BPL: BURPS1106A_2666(pdhB)
            BPD: BURPS668_2611(pdhB)
            BTE: BTH_I1865(aceF) BTH_II0239 BTH_II0930 BTH_II2302
            BPE: BP0994(aceF)
            BPA: BPP1463(aceF)
            BBR: BB2537(aceF) BB4703
            RFR: Rfer_0385 Rfer_2213 Rfer_3552
            POL: Bpro_0275 Bpro_0764 Bpro_2671
            AAV: Aave_2463
            MPT: Mpe_A1600 Mpe_A2127
            HAR: HEAR0747(aceF)
            MMS: mma_0674
            NEU: NE0360(aceF)
            NET: Neut_1609
            NMU: Nmul_A0359
            EBA: ebA135(aceF) ebA2188
            AZO: azo1372(pdhB) azo2295
            DAR: Daro_0441
            MFA: Mfla_2075
            ABU: Abu_1473(aceF)
            GSU: GSU2435 GSU2656(aceF)
            GME: Gmet_2511 Gmet_2752
            PCA: Pcar_0345
            BBA: Bd0779(pdhC)
            DPS: DP2094(phdC) DPPB40
            ADE: Adeh_1825
            MXA: MXAN_2668(pdhC) MXAN_4217
            SFU: Sfum_2646
            RPR: RP530
            RTY: RT0517(pdhC)
            RCO: RC0764(pdhC)
            RFE: RF_0761(pdhC)
            RBE: RBE_0300(pdhC)
            OTS: OTBS_1346(sucB)
            WOL: WD1177(aceF)
            WBM: Wbm0747
            AMA: AM1192(pdhC)
            APH: APH_1257
            ERU: Erum0670(pdhC)
            ERW: ERWE_CDS_00610(pdhC)
            ERG: ERGA_CDS_00580(pdhC)
            ECN: Ecaj_0061
            ECH: ECH_0098(pdhC)
            NSE: NSE_0953(pdhC)
            PUB: SAR11_0430(aceF)
            MLO: mll3627 mll4471 mlr0385
            MES: Meso_1628
            SME: SMc01032(pdhB) SMc03203(bkdB)
            ATU: Atu1432(aceF) Atu3471(bkdB)
            ATC: AGR_C_2641 AGR_L_2719
            RET: RHE_CH01935(pdhB) RHE_PC00072(bkdB)
            RLE: RL2243(pdhC) pRL100305 pRL80081
            BME: BMEI0856 BMEII0060 BMEII0746
            BMF: BAB1_1150(aceF) BAB2_0032 BAB2_0713 BAB2_1042
            BMS: BR1127(aceF) BRA0033 BRA0526
            BMB: BruAb1_1133(aceF) BruAb2_0033 BruAb2_0698 BruAb2_1023
            BOV: BOV_1085
            BJA: bll4779 blr3721(aceF)
            BRA: BRADO4084(pdhC)
            BBT: BBta_4460(pdhC)
            RPA: RPA2864
            BHE: BH05770(pdhC)
            BQU: BQ04930(pdhC)
            BBK: BARBAKC583_0536(pdhC)
            CCR: CC_1729
            SIL: SPO2242(pdhC) SPO3790(acoC)
            SIT: TM1040_2776
            RSP: RSP_4050(pdhB)
            RDE: RD1_3014(pdhC)
            MMR: Mmar10_1420
            HNE: HNE_1975(pdhC)
            ZMO: ZMO0510(pdhC)
            GOX: GOX2291
            GBE: GbCGDNIH1_1185
            ABA: Acid345_2791
            BSU: BG10209(pdhC) BG12560(acoC)
            BHA: BH0215 BH0778 BH1824(acoC) BH2653(pdhC)
            BAN: BA2774(acoC) BA4182(pdhC)
            BAR: GBAA2774(acoC) GBAA4182(pdhC)
            BAA: BA_3298 BA_4648
            BAT: BAS2586 BAS3881
            BCE: BC2777 BC3971
            BCA: BCE_2802(acoC) BCE_4019(pdhC)
            BCZ: BCZK2503(acoC) BCZK3729(pdhC)
            BTK: BT9727_2537(acoC) BT9727_3713(pdhC)
            BLI: BL01618(pdhC) BL03014(acoC)
            BLD: BLi00851(acoC) BLi01676(pdhC)
            BCL: ABC2418(pdhC) ABC2784(acoC)
            BAY: RBAM_014440
            BPU: BPUM_1173 BPUM_1357
            OIH: OB1414(pdhC) OB2875
            GKA: GK0712 GK1060 GK3218
            SAU: SA0945(pdhC)
            SAV: SAV1095(pdhC)
            SAM: MW0978(pdhC)
            SAR: SAR1069(pdhC)
            SAS: SAS1030
            SAC: SACOL1104(pdhC)
            SAB: SAB0961(pdhC)
            SAA: SAUSA300_0995
            SAO: SAOUHSC_01042
            SEP: SE0256 SE0793
            SER: SERP0682(pdhC) SERP2324
            SHA: SH0226 SH1857(pdhC)
            SSP: SSP1694
            LMO: lmo1054(pdhC)
            LMF: LMOf2365_1075
            LIN: lin1046(pdhC)
            LWE: lwe1030(pdhC)
            LLA: L0035(pdhC)
            LLC: LACR_0049
            LLM: llmg_0072(pdhC)
            SPY: SPy_1029(acoC)
            SPZ: M5005_Spy_0753(acoC)
            SPM: spyM18_1011(acoC)
            SPG: SpyM3_0663(acoC)
            SPS: SPs1190
            SPH: MGAS10270_Spy0871(acoC)
            SPI: MGAS10750_Spy0905(acoC)
            SPJ: MGAS2096_Spy0826(acoC)
            SPK: MGAS9429_Spy0867(acoC)
            SPF: SpyM51006(pdhC)
            SPA: M6_Spy0778
            SPB: M28_Spy0732(acoC)
            SPN: SP_1162
            SPR: spr1049(acoC)
            SPD: SPD_1026
            SAG: SAG0880
            SAN: gbs0897
            SAK: SAK_1003
            SMU: SMU.129(adhC) SMU.1421(pdhC)
            STC: str1049(acoC)
            STL: stu1049(acoC)
            SSA: SSA_1140(pdhC) SSA_1175(acoC)
            SGO: SGO_1131(sucB)
            LPL: lp_2152(pdhC)
            LSA: LSA1083(pdhC)
            LSL: LSL_0155(aceF)
            LBR: LVIS_1408
            LCA: LSEI_1307
            EFA: EF1355(aceF)
            OOE: OEOE_0330
            STH: STH413
            CDF: CD0038(acoC)
            CBO: CBO1633(acoC)
            CBA: CLB_1650(acoC)
            CBH: CLC_1659(acoC)
            CBF: CLI_1710(acoC)
            CKL: CKL_2269(pdhC)
            TTE: TTE0188(aceF) TTE0690(aceF2)
            MGE: MG_272(pdhC)
            MPN: MPN391(pdhC)
            MPU: MYPU_7620(pdhC)
            MPE: MYPE5100(pdhC)
            MGA: MGA_0162(aceF)
            MMY: MSC_0267(pdhC)
            MHJ: MHJ_0503(pdhC)
            MHP: MHP7448_0506(pdhC)
            MSY: MS53_0274(pdhC)
            MCP: MCAP_0227(pdhC)
            POY: PAM602(aceF)
            AYW: AYWB_138(aceF)
            MFL: Mfl041
            MTU: Rv2495c(pdhC)
            MTC: MT2570
            MBO: Mb2523c(pdhC)
            MBB: BCG_2515c(pdhC)
            MPA: MAP2307c(pdhC)
            MAV: MAV_4567
            MSM: MSMEG_4710
            MMC: Mmcs_1093 Mmcs_3624
            NFA: nfa10230
            RHA: RHA1_ro01578 RHA1_ro03319(pdhC) RHA1_ro03378
            SCO: SCO3815(bkdC1) SCO3829(bkdC2)
            SMA: SAV4364(bkdC) SAV4378(bkdH)
            TWH: TWT788(pdhC)
            TWS: TW797(pdhC)
            LXX: Lxx25050(pdhC)
            CMI: CMM_2942
            AAU: AAur_1523 AAur_3154 AAur_3891
            PAC: PPA2092
            TFU: Tfu_0182 Tfu_3051
            FRA: Francci3_0056 Francci3_2486
            FAL: FRAAL0069(aceF)
            ACE: Acel_0588
            SEN: SACE_2405 SACE_3954(bkdC2) SACE_4756(acoC) SACE_5544(bkdC2)
                 SACE_5674 SACE_7296(bkdC1)
            RBA: RB3423(aceF)
            CTR: CT247(pdhC)
            CTA: CTA_0269(pdhC)
            CMU: TC0518
            CPN: CPn0306(pdhC)
            CPA: CP0452
            CPJ: CPj0306(pdhC)
            CPT: CpB0315
            CCA: CCA00476(pdhC)
            CAB: CAB462(pdhC)
            CFE: CF0531(pdhC)
            PCU: pc1731(pdhC)
            LIL: LA2008(pdhC)
            LBJ: LBJ_1968
            LBL: LBL_1316
            SYN: sll1841(odhB)
            SYW: SYNW0671
            SYC: syc0481_c(pdhC)
            SYF: Synpcc7942_1068
            SYD: Syncc9605_2009
            SYE: Syncc9902_0662
            SYR: SynRCC307_1794(pdhC)
            SYX: SynWH7803_0582(pdhC)
            CYA: CYA_0742
            CYB: CYB_1116
            TEL: tll1299
            GVI: gll1092 gll2569
            ANA: alr3606
            PMA: Pro0401(aceF)
            PMM: PMM0405(pdhC)
            PMT: PMT0220(pdhC)
            PMN: PMN2A_1739
            PMI: PMT9312_0400
            PMB: A9601_04551(pdhC)
            PMC: P9515_04661(pdhC)
            PMF: P9303_21291(pdhC)
            PMG: P9301_04241(pdhC)
            PME: NATL1_04561(pdhC)
            SRU: SRU_1969
            CHU: CHU_1755(pdhC) CHU_2527(pdhC)
            GFO: GFO_1680(aceF) GFO_2888
            FPS: FP1384(pdhC)
            DRA: DR_0032 DR_0256
            DGE: Dgeo_1886 Dgeo_2341
            TTH: TTC1754 TTC1802
            TTJ: TTHA0184 TTHA0232
            HAL: VNG2219G(dsa)
            HMA: rrnAC2955(pdhC2) rrnB0198(pdhC1)
            NPH: NP0556A(dsa)
            TAC: Ta1436
            TVO: TVN0100
            PTO: PTO0547
            RCI: RRC124(pdhC)
            APE: APE_1671
            SSO: SSO1529(pdhC) SSO1530(pdhC)
            PAI: PAE2648
STRUCTURES  PDB: 1B5S  1DPB  1DPC  1DPD  1EAA  1EAB  1EAC  1EAD  1EAE  1EAF  
                 1FYC  1IYU  1IYV  1LAB  1LAC  1W3D  1W4E  1W4F  1W4G  1W4H  
                 1W4I  1W4J  1W4K  1W85  1W88  1Y8N  1Y8O  1Y8P  2DNE  2PNR  
                 2Q8I  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.12
            ExPASy - ENZYME nomenclature database: 2.3.1.12
            ExplorEnz - The Enzyme Database: 2.3.1.12
            ERGO genome analysis and discovery system: 2.3.1.12
            BRENDA, the Enzyme Database: 2.3.1.12
            CAS: 9032-29-5
///
ENTRY       EC 2.3.1.13                 Enzyme
NAME        glycine N-acyltransferase;
            glycine acyltransferase;
            glycine-N-acylase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:glycine N-acyltransferase
REACTION    acyl-CoA + glycine = CoA + N-acylglycine [RN:R00395]
ALL_REAC    R00395
SUBSTRATE   acyl-CoA [CPD:C00040];
            glycine [CPD:C00037]
PRODUCT     CoA [CPD:C00010];
            N-acylglycine [CPD:C02055]
COMMENT     The CoA derivatives of a number of aliphatic and aromatic acids, but
            not phenylacetyl-CoA or (indol-3-yl)acetyl-CoA, can act as donor.
            Not identical with EC 2.3.1.68 glutamine N-acyltransferase or EC
            2.3.1.71 glycine N-benzoyltransferase.
REFERENCE   1  [PMID:457678]
  AUTHORS   Nandi DL, Lucas SV, Webster LT Jr.
  TITLE     Benzoyl-coenzyme A:glycine N-acyltransferase and
            phenylacetyl-coenzyme A:glycine N-acyltransferase from bovine liver
            mitochondria. Purification and characterization.
  JOURNAL   J. Biol. Chem. 254 (1979) 7230-7.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:13174534]
  AUTHORS   SCHACHTER D, TAGGART JV.
  TITLE     Glycine N-acylase: purification and properties.
  JOURNAL   J. Biol. Chem. 208 (1954) 263-75.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:931988]
  AUTHORS   Webster LT, Siddiqui UA, Lucas SV, Strong JM, Mieyal JJ.
  TITLE     Identification of separate acyl- CoA:glycine and
            acyl-CoA:L-glutamine N-acyltransferase activities in mitochondrial
            fractions from liver of rhesus monkey and man.
  JOURNAL   J. Biol. Chem. 251 (1976) 3352-8.
  ORGANISM  monkey, human [GN:hsa]
ORTHOLOGY   KO: K00628  glycine N-acyltransferase
GENES       HSA: 10249(GLYAT)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.13
            ExPASy - ENZYME nomenclature database: 2.3.1.13
            ExplorEnz - The Enzyme Database: 2.3.1.13
            ERGO genome analysis and discovery system: 2.3.1.13
            BRENDA, the Enzyme Database: 2.3.1.13
            CAS: 9029-95-2
///
ENTRY       EC 2.3.1.14                 Enzyme
NAME        glutamine N-phenylacetyltransferase;
            glutamine phenylacetyltransferase;
            phenylacetyl-CoA:L-glutamine N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     phenylacetyl-CoA:L-glutamine alpha-N-phenylacetyltransferase
REACTION    phenylacetyl-CoA + L-glutamine = CoA +
            alpha-N-phenylacetyl-L-glutamine [RN:R02576]
ALL_REAC    R02576;
            (other) R04776
SUBSTRATE   phenylacetyl-CoA [CPD:C00582];
            L-glutamine [CPD:C00064]
PRODUCT     CoA [CPD:C00010];
            alpha-N-phenylacetyl-L-glutamine [CPD:C04148]
REFERENCE   1
  AUTHORS   Moldave, K. and Meister, A.
  TITLE     Synthesis of phenylacetylglutamine by human tissue.
  JOURNAL   J. Biol. Chem. 229 (1957) 463-476.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.14
            ExPASy - ENZYME nomenclature database: 2.3.1.14
            ExplorEnz - The Enzyme Database: 2.3.1.14
            ERGO genome analysis and discovery system: 2.3.1.14
            BRENDA, the Enzyme Database: 2.3.1.14
            CAS: 9030-00-6
///
ENTRY       EC 2.3.1.15                 Enzyme
NAME        glycerol-3-phosphate O-acyltransferase;
            alpha-glycerophosphate acyltransferase;
            3-glycerophosphate acyltransferase;
            ACP:sn-glycerol-3-phosphate acyltransferase;
            glycerol 3-phosphate acyltransferase;
            glycerol phosphate acyltransferase;
            glycerol phosphate transacylase;
            glycerophosphate acyltransferase;
            glycerophosphate transacylase;
            sn-glycerol 3-phosphate acyltransferase;
            sn-glycerol-3-phosphate acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:sn-glycerol-3-phosphate 1-O-acyltransferase
REACTION    acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol
            3-phosphate [RN:R00851]
ALL_REAC    R00851 > R02617
SUBSTRATE   acyl-CoA [CPD:C00040];
            sn-glycerol 3-phosphate [CPD:C00093]
PRODUCT     CoA [CPD:C00010];
            1-acyl-sn-glycerol 3-phosphate [CPD:C00681]
COMMENT     Acyl-[acyl-carrier-protein] can also act as acyl donor. The enzyme
            acts only on derivatives of fatty acids of chain length above C10
REFERENCE   1
  AUTHORS   Bertrams, M. and Heinz, E.
  TITLE     Positional specificity and fatty-acid selectivity of purified
            sn-glycerol 3-phosphate acyltransferases from chloroplasts.
  JOURNAL   Plant Physiol. 68 (1981) 653-657.
  ORGANISM  Pisum sativum, spinach
REFERENCE   2  [PMID:6825679]
  AUTHORS   Frentzen M, Heinz E, McKeon TA, Stumpf PK.
  TITLE     Specificities and selectivities of glycerol-3-phosphate
            acyltransferase and monoacylglycerol-3-phosphate acyltransferase
            from pea and spinach chloroplasts.
  JOURNAL   Eur. J. Biochem. 129 (1983) 629-36.
  ORGANISM  Pisum sativum, spinach
REFERENCE   3  [PMID:6350296]
  AUTHORS   Green PR, Vanaman TC, Modrich P, Bell RM.
  TITLE     Partial NH2- and COOH-terminal sequence and cyanogen bromide peptide
            analysis of Escherichia coli sn-glycerol-3-phosphate
            acyltransferase.
  JOURNAL   J. Biol. Chem. 258 (1983) 10862-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:4650158]
  AUTHORS   Yamashita S, Numa S.
  TITLE     Partial purification and properties of glycerophosphate
            acyltransferase from rat liver. Formation of 1-acylglycerol
            3-phosphate from sn-glycerol 3-phosphate and palmityl coenzyme A.
  JOURNAL   Eur. J. Biochem. 31 (1972) 565-73.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00561  Glycerolipid metabolism
            PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00629  glycerol-3-phosphate O-acyltransferase
            KO: K00630  glycerol-3-phosphate O-acyltransferase
            KO: K00631  glycerol-3-phosphate O-acyltransferase
GENES       HSA: 57678(GPAM)
            PTR: 450738(GPAM)
            MMU: 14732(Gpam)
            RNO: 29653(Gpam)
            CFA: 486890(GPAM)
            BTA: 497202(GPAM)
            GGA: 423895(GPAM)
            SPU: 585988(LOC585988)
            CME: CMJ027C
            PFA: PF13_0100
            TAN: TA19480
            ECO: b4041(plsB)
            ECJ: JW4001(plsB)
            ECE: Z5640(plsB)
            ECS: ECs5024
            ECC: c5011(plsB)
            ECI: UTI89_C4611(plsB)
            ECV: APECO1_2428(plsB)
            ECW: EcE24377A_4594(plsB)
            ECX: EcHS_A4281
            STY: STY4431(plsB)
            STT: t4141(plsB)
            SPT: SPA4052(plsB)
            SEC: SC4114(plsB)
            STM: STM4235(plsB)
            YPE: YPO0312(plsB)
            YPK: y0570(plsB)
            YPM: YP_0468(plsB)
            YPA: YPA_3972
            YPN: YPN_3357
            YPP: YPDSF_3659
            YPS: YPTB0368(pslB)
            YPI: YpsIP31758_3772(plsB)
            SFL: SF4164(plsB)
            SFX: S3567(plsB)
            SFV: SFV_4172(plsB)
            SSN: SSON_4221(plsB)
            SBO: SBO_4076(plsB)
            SDY: SDY_4533(plsB)
            ECA: ECA0628(plsB)
            PLU: plu4376(plsB)
            WBR: WGLp128(plsB)
            SGL: SG2142
            ENT: Ent638_0245
            SPE: Spro_4462
            HIN: HI0748(plsB)
            HIT: NTHI0904(plsB)
            HIP: CGSHiEE_08370
            HIQ: CGSHiGG_07235
            HDU: HD0546(plsB)
            HSO: HS_0385(plsB)
            PMU: PM1182(plsB)
            MSU: MS0745(plsB)
            APL: APL_1107(plsB)
            ASU: Asuc_1763
            XFA: XF1031
            XFT: PD0316(plsB)
            XCC: XCC4128(plsB)
            XCB: XC_4220
            XCV: XCV4371(plsB)
            XAC: XAC4270(plsB)
            XOO: XOO0254(plsB)
            XOM: XOO_0232(XOO0232)
            VCH: VC0093
            VCO: VC0395_A2422(plsB)
            VVU: VV1_1165
            VVY: VV0122
            VPA: VP2947
            VFI: VF2443
            PPR: PBPRA0164
            PAE: PA3673(plsB)
            PAU: PA14_16860(plsB)
            PPU: PP_1520(plsB)
            PPF: Pput_4203
            PST: PSPTO_1520(plsB)
            PSB: Psyr_1328
            PSP: PSPPH_3853(plsB)
            PFL: PFL_1161
            PFO: Pfl_1084
            PEN: PSEEN4236(plsB)
            PMY: Pmen_3091
            PAR: Psyc_0134
            PCR: Pcryo_0145
            PRW: PsycPRwf_0165
            ACI: ACIAD3232(plsB)
            SON: SO_4602(plsB)
            SDN: Sden_3514
            SFR: Sfri_0261
            SAZ: Sama_3480
            SBL: Sbal_0157
            SBM: Shew185_4177
            SLO: Shew_3530
            SPC: Sputcn32_3779
            SSE: Ssed_0201
            SPL: Spea_3996
            SHE: Shewmr4_3788
            SHM: Shewmr7_3861
            SHN: Shewana3_3988
            SHW: Sputw3181_0136
            ILO: IL0263(plsB)
            CPS: CPS_0133(plsB)
            PHA: PSHAa0142(plsB)
            PAT: Patl_4248
            PIN: Ping_0194
            MAQ: Maqu_2228
            HCH: HCH_05086
            CSA: Csal_0861
            ABO: ABO_1132(plsB)
            AHA: AHA_0182(plsB)
            BCI: BCI_0020(plsB)
            ADE: Adeh_1289
            AFW: Anae109_2476
            SFU: Sfum_3097
            SIL: SPO0369
            RDE: RD1_1636
            SAL: Sala_0194
            MTU: Rv1551(plsB1) Rv2482c(plsB2)
            MTC: MT1601 MT2555
            MBO: Mb1577(plsB1) Mb2507c(plsB2)
            MBB: BCG_2500c(plsB2)
            MLE: ML1246(plsB)
            MPA: MAP1261(plsB1) MAP2298c(plsB2)
            MSM: MSMEG_4703
            MGI: Mflv_2565
            MMC: Mmcs_3618
            NFA: nfa6180(plsB)
            RHA: RHA1_ro05648(plsB)
            CTR: CT807(plsB)
            CTA: CTA_0879(plsB)
            CMU: TC0192
            CPN: CPn0958(plsB)
            CPA: CP0902
            CPJ: CPj0958(plsB)
            CPT: CpB0995
            CCA: CCA00811
            CAB: CAB781
            CFE: CF0204(plsB)
            PCU: pc1318(ats1)
            BBU: BB0327
            BGA: BG0328
            BAF: BAPKO_0336
STRUCTURES  PDB: 1IUQ  1K30  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.15
            ExPASy - ENZYME nomenclature database: 2.3.1.15
            ExplorEnz - The Enzyme Database: 2.3.1.15
            ERGO genome analysis and discovery system: 2.3.1.15
            BRENDA, the Enzyme Database: 2.3.1.15
            CAS: 9029-96-3
///
ENTRY       EC 2.3.1.16                 Enzyme
NAME        acetyl-CoA C-acyltransferase;
            beta-ketothiolase;
            3-ketoacyl-CoA thiolase;
            KAT;
            beta-ketoacyl coenzyme A thiolase;
            beta-ketoacyl-CoA thiolase;
            beta-ketoadipyl coenzyme A thiolase;
            beta-ketoadipyl-CoA thiolase;
            3-ketoacyl CoA thiolase;
            3-ketoacyl coenzyme A thiolase;
            3-ketoacyl thiolase;
            3-ketothiolase;
            3-oxoacyl-CoA thiolase;
            3-oxoacyl-coenzyme A thiolase;
            6-oxoacyl-CoA thiolase;
            acetoacetyl-CoA beta-ketothiolase;
            acetyl-CoA acyltransferase;
            ketoacyl-CoA acyltransferase;
            ketoacyl-coenzyme A thiolase;
            long-chain 3-oxoacyl-CoA thiolase;
            oxoacyl-coenzyme A thiolase;
            pro-3-ketoacyl-CoA thiolase;
            thiolase I;
            2-methylacetoacetyl-CoA thiolase [misleading]
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:acetyl-CoA C-acyltransferase
REACTION    acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA [RN:R00391]
ALL_REAC    R00391 > R00238 R00829 R00927 R01177 R03778 R03858 R03991 R04742
            R04747 R05506 R07891 R07895 R07899 R07937 R07953;
            (other) R03719 R04546 R04811
SUBSTRATE   acyl-CoA [CPD:C00040];
            acetyl-CoA [CPD:C00024]
PRODUCT     CoA [CPD:C00010];
            3-oxoacyl-CoA [CPD:C00264]
REFERENCE   1
  AUTHORS   Beinert, H., Bock, R.M., Goldman, D.S., Green, D.E., Mahler, H.R.,
            Mii, S., Stansly, P.G. and Wakil, S.J.
  TITLE     A synthesis of dl-cortisone acetate.
  JOURNAL   J. Am. Chem. Soc. 75 (1953) 4111-4112.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:13174544]
  AUTHORS   GOLDMAN DS.
  TITLE     Studies on the fatty acid oxidizing system of animal tissues. VII.
            The beta-ketoacyl coenzyme A cleavage enzyme.
  JOURNAL   J. Biol. Chem. 208 (1954) 345-57.
  ORGANISM  cow [GN:bta]
REFERENCE   3
  AUTHORS   Stern, J.R., Coon, M.J. and del Campillo, A.
  TITLE     Enzymatic breakdown and synthesis of acetoacetate.
  JOURNAL   Nature 171 (1953) 28-30.
PATHWAY     PATH: map00062  Fatty acid elongation in mitochondria
            PATH: map00071  Fatty acid metabolism
            PATH: map00120  Bile acid biosynthesis
            PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00592  alpha-Linolenic acid metabolism
            PATH: map01040  Polyunsaturated fatty acid biosynthesis
            PATH: map03320  PPAR signaling pathway
ORTHOLOGY   KO: K00632  acetyl-CoA acyltransferase
            KO: K07508  acetyl-CoA acyltransferase 2
            KO: K07509  acetyl-CoA acyltransferase
            KO: K07513  acetyl-CoA acyltransferase 1
GENES       HSA: 10449(ACAA2) 30(ACAA1) 3032(HADHB)
            PTR: 455414(ACAA2) 459080(HADHB)
            MMU: 113868(Acaa1a) 231086(Hadhb) 235674(Acaa1b) 52538(Acaa2)
            RNO: 170465(Acaa2) 171155(Hadhb) 24157(Acaa1)
                 501072(RGD1562373_predicted)
            CFA: 477023(ACAA1) 481043(LOC481043) 490568(LOC490568)
                 607926(HADHB)
            BTA: 281811(HADHB) 508324(MGC128200)
            SSC: 397017(LCTHIO)
            GGA: 421995(HADHB) 426847(ACAA2) 770094(ACAA1)
            XLA: 379769(thiolase) 380296(acaa1) 380424(acaa2)
            XTR: 394747(TGas042k20.1)
            DRE: 336606(hadhb) 406325(zgc:56036) 431754(acaa1)
            SPU: 588288(LOC588288) 594080(LOC594080)
            DME: Dmel_CG4581 Dmel_CG4600(yip2)
            CEL: B0303.3 F53A2.7(Thiolases)
            ATH: AT1G04710 AT2G33150(PED1) AT5G48880(KAT5/PKT1/PKT2)
            OSA: 4331150
            SCE: YIL160C(POT1)
            AGO: AGOS_AFR302W
            PIC: PICST_55180(POT13) PICST_79854(POT11)
            CAL: CaO19.1591(erg10)
            CGR: CAGL0H06787g
            ANI: AN5646.2
            AFM: AFUA_2G11350 AFUA_4G10950 AFUA_7G04080
            AOR: AO090003001121
            CNE: CNA04700
            UMA: UM03298.1
            ECU: ECU06_0940
            DDI: DDBDRAFT_0167887
            PFA: PF14_0484
            TET: TTHERM_00899460
            TBR: Tb927.8.2540
            TCR: 509463.30 510507.20 511389.150
            LMA: LmjF23.0690 LmjF31.1630 LmjF31.1640
            ECO: b2342(yfcY) b3845(fadA)
            ECJ: JW2339(yfcY) JW5578(fadA)
            ECE: Z3605 Z5366(fadA)
            ECS: ECs3225 ECs4773
            ECC: c2887 c4792(fadA)
            ECI: UTI89_C2626 UTI89_C4430(fadA)
            ECP: ECP_2380 ECP_4058
            ECV: APECO1_2612(fadA) APECO1_4224(yfcY)
            ECW: EcE24377A_2638(fadI) EcE24377A_4364(fadA)
            ECX: EcHS_A2493(fadI) EcHS_A4068(fadA)
            STY: STY2621 STY3578(fadA)
            STT: t0475 t3316(fadA)
            SPT: SPA0475(yfcY) SPA3822(fadA)
            SEC: SC2391(yfcY) SC3879(fadA)
            STM: STM2389(yfcY) STM3982(fadA)
            YPE: YPO2746 YPO3767(fadA)
            YPK: y0463(fadA) y1579
            YPM: YP_2418(paaJ) YP_3281(fadA)
            YPA: YPA_2098 YPA_3437
            YPN: YPN_0197 YPN_2201
            YPP: YPDSF_2014 YPDSF_3387
            YPS: YPTB0266(fadA) YPTB2637
            YPI: YpsIP31758_0282(fadA) YpsIP31758_1399(fadI)
            YEN: YE0267(fadA)
            SFL: SF2420(yfcY) SF3921(fadA)
            SFX: S2555 S3831(fadA)
            SFV: SFV_2410 SFV_3655(fadA)
            SSN: SSON_2398 SSON_4018(fadA)
            SBO: SBO_2380 SBO_3857(fadA)
            SDY: SDY_2543 SDY_3900(fadA)
            ECA: ECA0207(fadA) ECA3079
            PLU: plu0146 plu3201 plu4403(fadA)
            ENT: Ent638_2882 Ent638_3950
            SPE: Spro_3081 Spro_3379 Spro_4857
            XCC: XCC0194(yfcY) XCC0366(pcaF) XCC1978(fadA)
            XCB: XC_0204 XC_0378 XC_2206
            XCV: XCV0198 XCV0380(pcaF) XCV2063(fadA)
            XAC: XAC0213(yfcY) XAC0366(pcaF) XAC2012(fadA)
            XOO: XOO0481(pcaF) XOO2538(fadA) XOO4084(yfcY)
            XOM: XOO_0447(XOO0447) XOO_2396(XOO2396) XOO_3858(XOO3858)
            VCH: VC1046 VC2759
            VCO: VC0395_A2533(fadA)
            VVU: VV1_0982 VV1_1975
            VVY: VV0028 VV2441
            VPA: VP0029 VP2209
            VFI: VF0024 VF1811
            PPR: PBPRA0063(fadA) PBPRA0961
            PAE: PA1736 PA2940 PA3013(foaB) PA4785
            PAU: PA14_25090(foaB) PA14_26010(phaA) PA14_63250(yfcY)
            PAP: PSPA7_2146(fadA)
            PPU: PP_0582 PP_2137(fadA) PP_3280(phaD)
            PPF: Pput_2479 Pput_3605 Pput_3690 Pput_4346
            PST: PSPTO_0744 PSPTO_3516(fadA)
            PSB: Psyr_0645 Psyr_2725 Psyr_3289 Psyr_4011
            PSP: PSPPH_2436 PSPPH_3209(fadA) PSPPH_4650
            PFL: PFL_0706 PFL_1835(fadA6) PFL_1941 PFL_2942(fadA2)
                 PFL_3644(acaB-12)
            PFO: Pfl_0656 Pfl_3878 Pfl_4096
            PEN: PSEEN0664 PSEEN2543 PSEEN2795(pcaF-2) PSEEN3727(fadA)
            PMY: Pmen_1581 Pmen_1725 Pmen_2591 Pmen_3228
            PAR: Psyc_1310 Psyc_1398(fadA4) Psyc_1933(fadA)
            PCR: Pcryo_1068 Pcryo_1538 Pcryo_2226
            PRW: PsycPRwf_1186 PsycPRwf_1390 PsycPRwf_2099
            ACI: ACIAD0334(fadA) ACIAD1569 ACIAD1706(pcaF) ACIAD1977 ACIAD2988
            SON: SO_0020(fadA) SO_3089
            SDN: Sden_0014 Sden_1529
            SFR: Sfri_0012 Sfri_2677
            SAZ: Sama_0031 Sama_2168
            SBL: Sbal_0020 Sbal_2761
            SBM: Shew185_0015 Shew185_2781
            SLO: Shew_0018 Shew_2426
            SPC: Sputcn32_0012 Sputcn32_2460
            SSE: Ssed_0022 Ssed_1628
            SPL: Spea_0017 Spea_2161 Spea_2170 Spea_2599
            SHE: Shewmr4_0017 Shewmr4_1407
            SHM: Shewmr7_0015 Shewmr7_1472
            SHN: Shewana3_0023 Shewana3_1460
            SHW: Sputw3181_0012 Sputw3181_1548
            ILO: IL0010(fadA) IL0994
            CPS: CPS_0392(fadA) CPS_3157(fadI)
            PHA: PSHAa0010(fadA) PSHAa0966(fadI) PSHAa2128
            PAT: Patl_0202 Patl_1663 Patl_1917
            SDE: Sde_1606
            PIN: Ping_2605
            MAQ: Maqu_1145 Maqu_2016
            CBU: CBU_0574
            LPN: lpg1353(fadA) lpg1597
            LPF: lpl1306(fadA) lpl1428
            LPP: lpp1307(fadA) lpp1555
            FTU: FTT1531(fadA)
            FTF: FTF1531(fadA)
            FTL: FTL_0583
            FTH: FTH_0583(fadA)
            FTN: FTN_1439(fadA)
            NOC: Noc_0827 Noc_1734
            AEH: Mlg_2110 Mlg_2125
            HCH: HCH_02186 HCH_03408 HCH_04754
            CSA: Csal_2392
            ABO: ABO_0253(fadA1) ABO_0983(pcaF) ABO_1567(fadA) ABO_1653(fadA2)
                 ABO_1712 ABO_2452(fadA3)
            MMW: Mmwyl1_1579
            AHA: AHA_0138(fadA) AHA_2153(fadI)
            CVI: CV_2719(fadA) CV_2790(phaA) CV_4291(catF)
            RSO: RSc0475(RS04420) RSc2252(pacF)
            REU: Reut_A0448 Reut_A1407 Reut_A1565 Reut_A1572 Reut_A1669
                 Reut_B3611
            REH: H16_A0462 H16_A0840(paaJ) H16_A1290 H16_B0200(pcaF) H16_B0378
                 H16_B0390
            RME: Rmet_0387 Rmet_3669 Rmet_5510
            BMA: BMA0096(fadA) BMA0199
            BMV: BMASAVP1_A2746 BMASAVP1_A3085(fadA)
            BML: BMA10299_A2010(fadA) BMA10299_A2332
            BMN: BMA10247_2277(fadA) BMA10247_2412
            BXE: Bxe_A0469 Bxe_A2763 Bxe_A2764 Bxe_A2777 Bxe_A3601 Bxe_A4036
                 Bxe_B2167(pcaF) Bxe_C0281 Bxe_C0597
            BVI: Bcep1808_1836 Bcep1808_2825
            BUR: Bcep18194_A5205 Bcep18194_A6046 Bcep18194_B1445
                 Bcep18194_B3098 Bcep18194_C7185 Bcep18194_C7559
            BCN: Bcen_2107 Bcen_6175
            BCH: Bcen2424_1904 Bcen2424_2719
            BAM: Bamb_1892 Bamb_2771
            BPS: BPSL0062 BPSL0371 BPSL0650
            BPM: BURPS1710b_0286 BURPS1710b_0579(fadA) BURPS1710b_0585(atoB)
                 BURPS1710b_0859(fadA) BURPS1710b_3565(pcaF)
            BPL: BURPS1106A_0697
            BPD: BURPS668_0682
            BTE: BTH_I0061 BTH_I0344 BTH_I0566
            BPE: BP2759
            BPA: BPP2340 BPP2344 BPP2569 BPP2724
            BBR: BB1791 BB1795 BB2014 BB2774
            RFR: Rfer_0226 Rfer_1034 Rfer_2385 Rfer_2753 Rfer_3283 Rfer_3516
            POL: Bpro_1231 Bpro_2572 Bpro_3015 Bpro_3953
            PNA: Pnap_0797 Pnap_1843 Pnap_3474
            AAV: Aave_2879 Aave_4085
            AJS: Ajs_0105 Ajs_0595 Ajs_1685
            VEI: Veis_0302 Veis_1791 Veis_4458 Veis_4960
            MPT: Mpe_A0416 Mpe_A0879
            HAR: HEAR2836(paaJ)
            MMS: mma_3089(fadA)
            NEU: NE1527
            NET: Neut_0725
            NMU: Nmul_A0098
            EBA: c1A212(fadA) ebA2314 ebA3639 p2A394(ditO)
            AZO: azo0310(paaJ1) azo0464(fadA1) azo0469(fadA2) azo2497(paaJ2)
                 azo3059
            DAR: Daro_0375 Daro_1545 Daro_1550 Daro_2352
            GME: Gmet_2058 Gmet_2197
            GUR: Gura_1592
            BBA: Bd1835 Bd2070
            ADE: Adeh_0359 Adeh_0407
            AFW: Anae109_2876 Anae109_4163
            MXA: MXAN_5135 MXAN_6988
            SAT: SYN_01681
            SFU: Sfum_1403
            RTY: RT0722(fadA)
            MLO: mll4180 mlr5628 mlr7614
            MES: Meso_0022 Meso_1523 Meso_2825 Meso_3505
            PLA: Plav_0090 Plav_0359 Plav_0464 Plav_0494 Plav_1545 Plav_2698
            SME: SMb20589(pcaF) SMc00262 SMc02228(fadA)
            SMD: Smed_0145
            ATU: Atu0502 Atu4549(pcaF) Atu4823(acaB)
            ATC: AGR_C_886 AGR_L_121(acaB) AGR_L_640
            RET: RHE_CH00558(fadA) RHE_PE00203(pcaF)
            RLE: RL0592 pRL110289(pcaF)
            BME: BMEII0496
            BMF: BAB2_0443 BAB2_0606(pcaF)
            BMS: BRA0636(pcaF) BRA0794
            BMB: BruAb2_0438
            OAN: Oant_4032
            BJA: blr0925(pcaF) blr1159 blr2427 blr3924 blr7806
            BRA: BRADO2393 BRADO6724
            BBT: BBta_0816 BBta_2746
            RPA: RPA0817 RPA1703 RPA2304 RPA3466 RPA4346
            RPB: RPB_1682 RPB_4151 RPB_4605
            RPC: RPC_0736
            RPD: RPD_0805 RPD_3551 RPD_3611 RPD_3991
            RPE: RPE_0673 RPE_2372 RPE_3778 RPE_4198
            NWI: Nwi_0279 Nwi_2160 Nwi_2994
            NHA: Nham_0358 Nham_1086
            XAU: Xaut_0625 Xaut_0916 Xaut_1122 Xaut_4443
            CCR: CC_0077 CC_0779 CC_1111 CC_1432 CC_2407 CC_3111
            SIL: SPO1013 SPO2918 SPOA0425
            SIT: TM1040_0361 TM1040_1561 TM1040_3272
            RSP: RSP_2197 RSP_3536
            RSH: Rsph17029_0872
            RSQ: Rsph17025_2295
            JAN: Jann_0650 Jann_2975
            RDE: RD1_3972(fadA)
            PDE: Pden_3226
            MMR: Mmar10_0542 Mmar10_2665
            HNE: HNE_0671
            NAR: Saro_0867
            SAL: Sala_0110 Sala_1005 Sala_1637 Sala_2162
            SWI: Swit_0345 Swit_1006 Swit_1771 Swit_3636 Swit_3795 Swit_4336
            ELI: ELI_12090
            ACR: Acry_0005 Acry_1257 Acry_1576
            RRU: Rru_A1310
            MAG: amb3598
            MGM: Mmc1_3557
            ABA: Acid345_2470
            SUS: Acid_0251 Acid_5545 Acid_5695
            BSU: BG14023(yusK)
            BHA: BH3487
            BAN: BA5248
            BAR: GBAA5248
            BAA: BA_0113
            BAT: BAS4876
            BCE: BC5003
            BCA: BCE_5143
            BCZ: BCZK4733(acaB)
            BCY: Bcer98_3596
            BTK: BT9727_4718(acaB)
            BTL: BALH_4546(acaB)
            BLI: BL02179(yusK)
            BLD: BLi03465(yusK)
            BCL: ABC2989
            OIH: OB2394 OB2672
            GKA: GK1320 GK3007
            SAU: SA0223
            SAV: SAV0231
            SAM: MW0207
            SAR: SAR0223(fadA)
            SAS: SAS0207
            SAC: SACOL0211
            SAB: SAB0170c
            SAA: SAUSA300_0225(fadA)
            SAO: SAOUHSC_00195
            SAJ: SaurJH9_0215 SaurJH9_0599
            SAH: SaurJH1_0221 SaurJH1_0613
            SSP: SSP2423
            STH: STH3011
            CHY: CHY_1608 CHY_1743
            DSY: DSY3368
            DRM: Dred_0348
            MTU: Rv0243(fadA2) Rv0859(fadA) Rv0914c Rv2790c(ltp1) Rv3522(ltp4)
                 Rv3523(ltp3) Rv3556c(fadA6)
            MTC: MT0257 MT0882 MT0939 MT1104 MT2860 MT3623 MT3650 MT3660
            MBO: Mb0249(fadA2) Mb0882(fadA) Mb0938c Mb1103c(fadA3)
                 Mb2813c(ltp1) Mb3553
            MBB: BCG_0281(fadA2) BCG_0966c BCG_3587
            MLE: ML2162(fadA) ML2564(fadA2)
            MPA: MAP0510(fadA6_1) MAP0521c(fadA5) MAP0542c MAP0789(fadA_1)
                 MAP1020c MAP1021c MAP1714(fadA_2) MAP2897c(ltp1)
                 MAP3337(fadA6_4) MAP3693(fadA2)
            MSM: MSMEG_0373 MSMEG_3012 MSMEG_4833 MSMEG_5199 MSMEG_5608
                 MSMEG_5721 MSMEG_5923 MSMEG_5996 MSMEG_6008
            MVA: Mvan_0260 Mvan_0916 Mvan_2617 Mvan_4206 Mvan_4589 Mvan_5067
                 Mvan_5259 Mvan_5282
            MGI: Mflv_0411 Mflv_1507 Mflv_1691 Mflv_2116 Mflv_2445 Mflv_3782
            MMC: Mmcs_0241 Mmcs_1517 Mmcs_2317 Mmcs_3099 Mmcs_3741 Mmcs_4080
                 Mmcs_4152 Mmcs_4174 Mmcs_4493 Mmcs_4636 Mmcs_4678 Mmcs_4690
            MKM: Mkms_0251 Mkms_1540 Mkms_2364 Mkms_3814 Mkms_4156 Mkms_4227
                 Mkms_4580 Mkms_4764 Mkms_4776
            MJL: Mjls_0231 Mjls_2356 Mjls_3753 Mjls_4310 Mjls_4876 Mjls_5063
                 Mjls_5075
            CEF: CE0325 CE0673 CE1270
            CJK: jk0160(fadA1) jk0823(fadA2)
            NFA: nfa20950 nfa2850(fadA) nfa34130(fadA6) nfa35170(fadA7)
                 nfa43320(fadA8) nfa46060(fadA9) nfa48350(fadA10)
                 nfa4890(fadA2) nfa5170(fadA3) nfa5210 nfa54600(fadA11)
                 nfa55420(fadA12)
            RHA: RHA1_ro01340(pcaF) RHA1_ro03460 RHA1_ro04204 RHA1_ro05543
                 RHA1_ro05841 RHA1_ro06115 RHA1_ro06853 RHA1_ro10318
                 RHA1_ro11185
            SCO: SCO1324(2SCG61.06c) SCO3079(SCE25.20) SCO4502(SCD35.09)
                 SCO6701(pcaF) SCO6731(SC5F2A.14) SCO6788(SC6A5.37)
                 SCO6967(pcaF)
            SMA: SAV1242 SAV1604(pcaF1) SAV1681(fadA4) SAV3512(fadA2)
                 SAV5842(fadA7) SAV5866(ltp1) SAV6199(fadA3) SAV7026(fadA6)
            CMI: CMM_1662(fadA)
            ART: Arth_1655 Arth_2110 Arth_2144
            NCA: Noca_1013 Noca_2740 Noca_2847 Noca_2853 Noca_4563
            TFU: Tfu_0253 Tfu_0436 Tfu_0875 Tfu_1278 Tfu_1903
            FRA: Francci3_1330 Francci3_2244 Francci3_2474 Francci3_2502
                 Francci3_2997 Francci3_4451
            FAL: FRAAL2097 FRAAL4934(fadA) FRAAL5482(fadA)
            KRA: Krad_3502
            SEN: SACE_3994(fadA) SACE_6363(fadA) SACE_7304
            STP: Strop_0142 Strop_0908 Strop_1359 Strop_2608 Strop_2613
                 Strop_2801
            RXY: Rxyl_2056 Rxyl_2360 Rxyl_2454
            LIL: LA2689(thl) LA3135(fadE) LA4114 LA4139(fadA)
            LIC: LIC10974 LIC11311(erg10) LIC13279
            SRU: SRU_1460(hadHB)
            CHU: CHU_3590(fadA)
            GFO: GFO_1045(fadA)
            FJO: Fjoh_3321
            RRS: RoseRS_2969
            RCA: Rcas_1886
            DGE: Dgeo_0618
            TTH: TTC0535 TTC0623
            TTJ: TTHA0891 TTHA0987
            MJA: MJ1549
            MMP: MMP1212
            MAC: MA4042
            MBA: Mbar_A0550
            MMA: MM_0870
            MBU: Mbur_1933
            MHU: Mhun_0150
            MTH: MTH793
            MST: Msp_0116
            MSI: Msm_1562
            MKA: MK1378
            HAL: VNG0678G(acaB1) VNG0931G(acaB2) VNG2063G(aca)
            HMA: rrnAC0929(acaB4) rrnB0242(acaB2)
            HWA: HQ1590A(acaB) HQ1985A(acaB) HQ2307A(acaB)
            NPH: NP2214A(acaB_8) NP2260A(acaB_6) NP2606A(acaB_1)
                 NP2612A(acaB_2) NP3420A(acaB_3) NP3438A(acaB_4)
                 NP3650A(acaB_7) NP4580A(acaB_5)
            TAC: Ta0030 Ta0296 Ta1456
            TVO: TVN0069 TVN0131 TVN1304
            PTO: PTO0383 PTO1023
            PAB: PAB0907(acaB)
            PFU: PF0973
            TKO: TK0180
            RCI: RCIX150(paaJ)
            APE: APE_0929.1 APE_1872.1 APE_2382.1 APE_2384
            SSO: SSO0534(acaB-1) SSO2061(acaB-2) SSO2062(acaB-3)
                 SSO2496(acaB-5) SSO2625(acaB-7) SSO2697(acaB-8)
                 SSO2874(acaB-9)
            STO: ST0079 ST0096 ST1350 ST1799 ST1800 ST2418
            SAI: Saci_1114 Saci_1121 Saci_1728 Saci_2209 Saci_2232 Saci_2233
                 Saci_2288
            PAI: PAE1377 PAE2183 PAE2471 PAE2486 PAE2488 PAE3656
            PCL: Pcal_0649
STRUCTURES  PDB: 1AFW  1PXT  1WDK  1WDL  1WDM  2C7Y  2C7Z  2D3T  2IIK  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.16
            ExPASy - ENZYME nomenclature database: 2.3.1.16
            ExplorEnz - The Enzyme Database: 2.3.1.16
            ERGO genome analysis and discovery system: 2.3.1.16
            UM-BBD (Biocatalysis/Biodegradation Database): 2.3.1.16
            BRENDA, the Enzyme Database: 2.3.1.16
            CAS: 9029-97-4
///
ENTRY       EC 2.3.1.17                 Enzyme
NAME        aspartate N-acetyltransferase;
            aspartate acetyltransferase;
            L-aspartate N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:L-aspartate N-acetyltransferase
REACTION    acetyl-CoA + L-aspartate = CoA + N-acetyl-L-aspartate [RN:R00487]
ALL_REAC    R00487
SUBSTRATE   acetyl-CoA [CPD:C00024];
            L-aspartate [CPD:C00049]
PRODUCT     CoA [CPD:C00010];
            N-acetyl-L-aspartate [CPD:C01042]
REFERENCE   1
  AUTHORS   Goldstein, F.B.
  TITLE     Biosynthesis of N-acetyl-L-aspartic acid.
  JOURNAL   J. Biol. Chem. 234 (1959) 2702-2706.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6061408]
  AUTHORS   Knizley H Jr.
  TITLE     The enzymatic synthesis of N-acetyl-L-aspartic acid by a
            water-insoluble preparation of a cat brain acetone powder.
  JOURNAL   J. Biol. Chem. 242 (1967) 4619-22.
  ORGANISM  cat
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.17
            ExPASy - ENZYME nomenclature database: 2.3.1.17
            ExplorEnz - The Enzyme Database: 2.3.1.17
            ERGO genome analysis and discovery system: 2.3.1.17
            BRENDA, the Enzyme Database: 2.3.1.17
            CAS: 9029-99-6
///
ENTRY       EC 2.3.1.18                 Enzyme
NAME        galactoside O-acetyltransferase;
            thiogalactoside acetyltransferase;
            galactoside acetyltransferase;
            thiogalactoside transacetylase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:beta-D-galactoside 6-acetyltransferase
REACTION    acetyl-CoA + a beta-D-galactoside = CoA + a
            6-acetyl-beta-D-galactoside [RN:R02616]
ALL_REAC    R02616
SUBSTRATE   acetyl-CoA [CPD:C00024];
            beta-D-galactoside [CPD:C00602]
PRODUCT     CoA [CPD:C00010];
            6-acetyl-beta-D-galactoside [CPD:C03773]
COMMENT     Acts on thiogalactosides and phenylgalactoside.
REFERENCE   1
  AUTHORS   Zabin, I.
  TITLE     Crystalline thiogalactoside transacetylase.
  JOURNAL   J. Biol. Chem. 238 (1963) 3300-3306.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Zabin, I., Kepes, A. and Monod, J.
  TITLE     Thiogalactoside transacetylase.
  JOURNAL   J. Biol. Chem. 237 (1962) 253-257.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K00633  galactoside O-acetyltransferase
GENES       ECO: b0342(lacA)
            ECJ: JW0333(lacA)
            ECE: Z0438(lacA)
            ECS: ECs0395
            ECC: c0457(lacA)
            ECI: UTI89_C0369(lacA) UTI89_C4472(yiiD)
            ECP: ECP_0415
            ECV: APECO1_1651(lacA) APECO1_2579(yiiD)
            SBO: SBO_3902(yiiD)
            SDY: SDY_3855(yiiD)
            MSU: MS0417(wbbJ)
            VVU: VV2_0105
            VVY: VVA0614
            VPA: VP1758
            SHE: Shewmr4_1322
            ILO: IL0543
            NOC: Noc_2179
            BXE: Bxe_A2414
            BUR: Bcep18194_A6294
            BAM: Bamb_2989
            ABU: Abu_0669
            DVU: DVU0340
            DDE: Dde_3688
            LIP: LI0123(lacA)
            RLE: pRL0241A(wbbJ) pRL120540 pRL90153
            BAN: BA3580
            BAR: GBAA3580
            BAA: BA_4071
            BAT: BAS3319
            BCE: BC1945
            BCA: BCE_2028
            BCZ: BCZK3234(vioB)
            BTK: BT9727_3282(vioB)
            BTL: BALH_3168(vioB)
            SAC: SACOL2570
            SAB: SAB2429c
            LLA: L0026(thgA)
            LLC: LACR_1850
            LPL: lp_0393(thgA1) lp_1933(thgA2) lp_2861(thgA3)
            LBR: LVIS_2245
            CAC: CAC2692
            CPF: CPF_0251(lacA)
            CBO: CBO2159(lacA)
            SCO: SCO7405(SC10G8.33c)
            BLO: BL1080(lacA)
            LIL: LA1622(lacA)
            AVA: Ava_3000
            BTH: BT_0521
            BFR: BF3488 BF4300
            BFS: BF3298 BF4109(lacA)
            CHU: CHU_0849(lacA)
            TTH: TTC1875
            MJA: MJ1064(lacA)
            MAC: MA0513(maa)
            MBA: Mbar_A3469
            MMA: MM_1673
            NPH: NP4198A(maa_3) NP4490A(maa_1) NP6236A(maa_2)
STRUCTURES  PDB: 1KQA  1KRR  1KRU  1KRV  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.18
            ExPASy - ENZYME nomenclature database: 2.3.1.18
            ExplorEnz - The Enzyme Database: 2.3.1.18
            ERGO genome analysis and discovery system: 2.3.1.18
            BRENDA, the Enzyme Database: 2.3.1.18
            CAS: 9029-94-1
///
ENTRY       EC 2.3.1.19                 Enzyme
NAME        phosphate butyryltransferase;
            phosphotransbutyrylase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     butanoyl-CoA:phosphate butanoyltransferase
REACTION    butanoyl-CoA + phosphate = CoA + butanoyl phosphate [RN:R01174]
ALL_REAC    R01174
SUBSTRATE   butanoyl-CoA [CPD:C00136];
            phosphate [CPD:C00009]
PRODUCT     CoA [CPD:C00010];
            butanoyl phosphate [CPD:C02527]
REFERENCE   1
  AUTHORS   Valentine, R.C. and Wolfe, R.S.
  TITLE     Purification and role of phosphotransbutyrylase.
  JOURNAL   J. Biol. Chem. 235 (1960) 1948-1952.
  ORGANISM  Clostridium butyricum
PATHWAY     PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K00634  phosphate butyryltransferase
GENES       AEH: Mlg_2378
            HHA: Hhal_2061
            REU: Reut_A0626 Reut_A1202
            BVI: Bcep1808_6175
            BUR: Bcep18194_B2634
            BAM: Bamb_3821
            BPE: BP1004
            BPA: BPP1169
            BBR: BB1385
            PNA: Pnap_3568
            VEI: Veis_3998
            GME: Gmet_2098
            DVU: DVU0627(ptb)
            DVL: Dvul_2331
            DDE: Dde_3129
            ADE: Adeh_0041
            AFW: Anae109_0044
            SAT: SYN_00653 SYN_00654 SYN_01211 SYN_01212 SYN_02080 SYN_02081
            PLA: Plav_3451
            BRA: BRADO6360
            BBT: BBta_2656 BBta_7293
            RPB: RPB_1026
            RPD: RPD_1127
            RPE: RPE_3163
            NHA: Nham_0864
            RSH: Rsph17029_2915
            RSQ: Rsph17025_2693
            RDE: RD1_0842(ptb)
            PDE: Pden_4209
            ACR: Acry_3031
            RRU: Rru_A1468
            BSU: BG11722(ptb)
            BAN: BA4388(yqiS)
            BAR: GBAA4388(yqiS)
            BAA: BA_4843
            BAT: BAS4071
            BCE: BC4163
            BCA: BCE_4238(yqiS)
            BCZ: BCZK3918(ptb)
            BCY: Bcer98_2860
            BTK: BT9727_3909(ptb)
            BTL: BALH_3776(ptb)
            BLI: BL01500(ptb)
            BLD: BLi02586(ptb)
            BAY: RBAM_022370
            BPU: BPUM_2148
            GKA: GK2382
            SSP: SSP1236
            LMO: lmo1369
            LMF: LMOf2365_1386
            LIN: lin1406
            LWE: lwe1384
            LCA: LSEI_1448
            CAC: CAC3076(ptb)
            CPE: CPE2348(ptb)
            CPF: CPF_2657(ptb)
            CPR: CPR_2343
            CTC: CTC02546
            CDF: CD0112(ptb) CD0715 CD2425
            CBO: CBO3118(ptb1) CBO3427(ptb2)
            CBA: CLB_3483(ptb)
            CBH: CLC_3371(ptb)
            CBF: CLI_3609(ptb)
            CBE: Cbei_0203
            AMT: Amet_1726 Amet_4309
            DSY: DSY2400
            BTH: BT_2551
            BFR: BF4337
            PLT: Plut_1074
            RRS: RoseRS_3886
            RCA: Rcas_3315
            TMA: TM1755
            TPT: Tpet_1042
            TME: Tmel_0108 Tmel_1928
            FNO: Fnod_0107 Fnod_1789
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.19
            ExPASy - ENZYME nomenclature database: 2.3.1.19
            ExplorEnz - The Enzyme Database: 2.3.1.19
            ERGO genome analysis and discovery system: 2.3.1.19
            BRENDA, the Enzyme Database: 2.3.1.19
            CAS: 9030-01-7
///
ENTRY       EC 2.3.1.20                 Enzyme
NAME        diacylglycerol O-acyltransferase;
            diglyceride acyltransferase;
            1,2-diacylglycerol acyltransferase;
            diacylglycerol acyltransferase;
            diglyceride O-acyltransferase;
            palmitoyl-CoA-sn-1,2-diacylglycerol acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:1,2-diacylglycerol O-acyltransferase
REACTION    acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol [RN:R02251]
ALL_REAC    R02251 > R02694
SUBSTRATE   acyl-CoA [CPD:C00040];
            1,2-diacylglycerol [CPD:C00641]
PRODUCT     CoA [CPD:C00010];
            triacylglycerol [CPD:C00422]
COMMENT     Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
REFERENCE   1  [PMID:947894]
  AUTHORS   Coleman R, Bell RM.
  TITLE     Triacylglycerol synthesis in isolated fat cells. Studies on the
            microsomal diacylglycerol acyltransferase activity using
            ethanol-dispersed diacylglycerols.
  JOURNAL   J. Biol. Chem. 251 (1976) 4537-43.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6289909]
  AUTHORS   Grigor MR, Bell RM.
  TITLE     Separate monoacylglycerol and diacylglycerol acyltransferases
            function in intestinal triacylglycerol synthesis.
  JOURNAL   Biochim. Biophys. Acta. 712 (1982) 464-72.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:3422635]
  AUTHORS   Kawasaki T, Snyder F.
  TITLE     Synthesis of a novel acetylated neutral lipid related to
            platelet-activating factor by
            acyl-CoA:1-O-alkyl-2-acetyl-sn-glycerol acyltransferase in HL-60
            cells.
  JOURNAL   J. Biol. Chem. 263 (1988) 2593-6.
  ORGANISM  human [GN:hsa]
REFERENCE   4
  AUTHORS   Weiss, S.B., Kennedy, E.P. and Kiyasu, J.Y.
  TITLE     The enzymatic synthesis of triglycerides.
  JOURNAL   J. Biol. Chem. 235 (1960) 40-44.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00561  Glycerolipid metabolism
ORTHOLOGY   KO: K00635  diacylglycerol O-acyltransferase
GENES       HSA: 84649(DGAT2) 8694(DGAT1)
            PTR: 464460(DGAT1)
            MMU: 13350(Dgat1) 67800(Dgat2)
            RNO: 252900(Dgat2) 84497(Dgat1)
            CFA: 482093(DGAT1)
            BTA: 282609(DGAT1)
            SSC: 397118(DGAT)
            XTR: 395003(MGC76066)
            DRE: 565316(dgat2)
            SPU: 575003(LOC575003)
            OSA: 4341317
            ANI: AN6159.2
            AFM: AFUA_2G08380
            AOR: AO090011000863
            DDI: DDBDRAFT_0202877
            PFA: MAL3P7.29
            CPV: cgd2_1090
            CHO: Chro.20121
            TAN: TA19620
            TET: TTHERM_00971690
            ACI: ACIAD0832(wax-dgaT)
            ABO: ABO_1804(atfA2) ABO_2742(atfA1)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.20
            ExPASy - ENZYME nomenclature database: 2.3.1.20
            ExplorEnz - The Enzyme Database: 2.3.1.20
            ERGO genome analysis and discovery system: 2.3.1.20
            BRENDA, the Enzyme Database: 2.3.1.20
            CAS: 9029-98-5
///
ENTRY       EC 2.3.1.21                 Enzyme
NAME        carnitine O-palmitoyltransferase;
            CPT;
            CPTo;
            outer malonyl-CoA inhibitable carnitine palmitoyltransferase;
            CPTi;
            CPT I (outer membrane carnitine palmitoyl transferase);
            carnitine palmitoyltransferase I;
            carnitine palmitoyltransferase II;
            CPT-A;
            CPT-B;
            acylcarnitine transferase;
            carnitine palmitoyltransferase;
            carnitine palmitoyltransferase-A;
            L-carnitine palmitoyltransferase;
            palmitoylcarnitine transferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     palmitoyl-CoA:L-carnitine O-palmitoyltransferase
REACTION    palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine [RN:R01923]
ALL_REAC    R01923;
            (other) R01046
SUBSTRATE   palmitoyl-CoA [CPD:C00154];
            L-carnitine [CPD:C00318]
PRODUCT     CoA [CPD:C00010];
            L-palmitoylcarnitine [CPD:C02990]
COMMENT     Broad specificity to acyl group, over the range C8 to C18; optimal
            activity with palmitoyl-CoA. cf. EC 2.3.1.7 carnitine
            O-acetyltransferase and EC 2.3.1.137 carnitine
            O-octanoyltransferase.
REFERENCE   1
  AUTHORS   Derrick, J.P., Tubbs, P.K. and Ramsay, R.R.
  TITLE     Purification and properties of an easily solubilized L-carnitine
            palmitoyltransferase from beef-liver mitochondria.
  JOURNAL   Biochem. Soc. Trans. 14 (1986) 698.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:3342008]
  AUTHORS   Healy MJ, Kerner J, Bieber LL.
  TITLE     Enzymes of carnitine acylation. Is overt carnitine
            palmitoyltransferase of liver peroxisomal carnitine
            octanoyltransferase?
  JOURNAL   Biochem. J. 249 (1988) 231-7.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:6630173]
  AUTHORS   Miyazawa S, Ozasa H, Osumi T, Hashimoto T.
  TITLE     Purification and properties of carnitine octanoyltransferase and
            carnitine palmitoyltransferase from rat liver.
  JOURNAL   J. Biochem. (Tokyo). 94 (1983) 529-42.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00071  Fatty acid metabolism
            PATH: map03320  PPAR signaling pathway
            PATH: map04920  Adipocytokine signaling pathway
ORTHOLOGY   KO: K00636  carnitine O-palmitoyltransferase
            KO: K08765  carnitine O-palmitoyltransferase 1
            KO: K08766  carnitine O-palmitoyltransferase 2
GENES       HSA: 126129(CPT1C) 1374(CPT1A) 1375(CPT1B) 1376(CPT2)
            PTR: 451382(CPT1A) 470253(CPT1B)
            MMU: 12894(Cpt1a) 12895(Cpt1b) 12896(Cpt2) 78070(Cpt1c)
            RNO: 25413(Cpt2) 25756(Cpt1b) 25757(Cpt1a)
            CFA: 403583(CPT1A) 476410(CPT1C) 481184(CPT1B) 489585(CPT2)
            BTA: 504502(CPT2) 509459(CPT1B) 513710(LOC513710)
                 618627(LOC618627)
            SSC: 399528(CPT1B)
            GGA: 423118(CPT1A) 424649(RCJMB04_12h19)
            XLA: 379393(MGC53498) 379893(cg2107) 495682(LOC495682)
            XTR: 394801(cpt2)
            DRE: 560000(LOC560000)
            SPU: 577222(LOC577222) 577810(LOC577810) 577934(LOC577934)
            DME: Dmel_CG12891(CPTI) Dmel_CG2107
            CEL: R07H5.2(cpt-2) Y46G5A.17(cpt-1)
            TBR: Tb927.3.3900 Tb927.7.2250
            TCR: 507211.10 511807.284
            LMA: LmjF22.0310
STRUCTURES  PDB: 2DEB  2FW3  2FYO  2H4T  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.21
            ExPASy - ENZYME nomenclature database: 2.3.1.21
            ExplorEnz - The Enzyme Database: 2.3.1.21
            ERGO genome analysis and discovery system: 2.3.1.21
            BRENDA, the Enzyme Database: 2.3.1.21
            CAS: 9068-41-1
///
ENTRY       EC 2.3.1.22                 Enzyme
NAME        2-acylglycerol O-acyltransferase;
            acylglycerol palmitoyltransferase;
            monoglyceride acyltransferase;
            acyl coenzyme A-monoglyceride acyltransferase;
            monoacylglycerol acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:2-acylglycerol O-acyltransferase
REACTION    acyl-CoA + 2-acylglycerol = CoA + diacylglycerol [RN:R01368]
ALL_REAC    R01368 > R03838;
            (other) R03755 R03756
SUBSTRATE   acyl-CoA [CPD:C00040];
            2-acylglycerol [CPD:C02112]
PRODUCT     CoA [CPD:C00010];
            diacylglycerol [CPD:C00165]
COMMENT     Various 2-acylglycerols can act as acceptor; palmitoyl-CoA and other
            long-chain acyl-CoAs can act as donors. The sn-1 position and the
            sn-3 position are both acylated, at about the same rate.
REFERENCE   1  [PMID:4016575]
  AUTHORS   Manganaro F, Kuksis A.
  TITLE     Purification and preliminary characterization of 2-monoacylglycerol
            acyltransferase from rat intestinal villus cells.
  JOURNAL   Can. J. Biochem. Cell. Biol. 63 (1985) 341-7.
PATHWAY     PATH: map00561  Glycerolipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.22
            ExPASy - ENZYME nomenclature database: 2.3.1.22
            ExplorEnz - The Enzyme Database: 2.3.1.22
            ERGO genome analysis and discovery system: 2.3.1.22
            BRENDA, the Enzyme Database: 2.3.1.22
            CAS: 9055-17-8
///
ENTRY       EC 2.3.1.23                 Enzyme
NAME        1-acylglycerophosphocholine O-acyltransferase;
            lysolecithin acyltransferase;
            1-acyl-sn-glycero-3-phosphocholine acyltransferase;
            acyl coenzyme A-monoacylphosphatidylcholine acyltransferase;
            acyl-CoA:1-acyl-glycero-3-phosphocholine transacylase;
            lysophosphatide acyltransferase;
            lysophosphatidylcholine acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:1-acyl-sn-glycero-3-phosphocholine O-acyltransferase
REACTION    acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA +
            1,2-diacyl-sn-glycero-3-phosphocholine [RN:R01318]
ALL_REAC    R01318;
            (other) R04480
SUBSTRATE   acyl-CoA [CPD:C00040];
            1-acyl-sn-glycero-3-phosphocholine [CPD:C04230]
PRODUCT     CoA [CPD:C00010];
            1,2-diacyl-sn-glycero-3-phosphocholine [CPD:C00157]
COMMENT     Acts preferentially with unsaturated acyl-CoA derivatives.
            1-Acyl-sn-glycero-3-phosphoinositol can also act as acceptor.
REFERENCE   1  [PMID:6250446]
  AUTHORS   Bell RM, Coleman RA.
  TITLE     Enzymes of glycerolipid synthesis in eukaryotes.
  JOURNAL   Annu. Rev. Biochem. 49 (1980) 459-87.
REFERENCE   2  [PMID:5661029]
  AUTHORS   Hill EE, Lands WE.
  TITLE     Incorporation of long-chain and polyunsaturated acids into
            phosphatidate and phosphatidylcholine.
  JOURNAL   Biochim. Biophys. Acta. 152 (1968) 645-8.
  ORGANISM  rat [GN:rno], guinea pig
REFERENCE   3  [PMID:598375]
  AUTHORS   Miki Y, Hosaka K, Yamashita S, Handa H, Numa S.
  TITLE     Acyl-acceptor specificities of 1-acylglycerolphosphate
            acyltransferase and 1-acylglycerophosphorylcholine acyltransferase
            resolved from rat liver microsomes.
  JOURNAL   Eur. J. Biochem. 81 (1977) 433-41.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:6078124]
  AUTHORS   van den Bosch H, van Golde LM, Eibl H, van Deenen LL.
  TITLE     The acylation of 1-acylglycero-3-phosphorylcholines by rat-liver
            microsomes.
  JOURNAL   Biochim. Biophys. Acta. 144 (1967) 613-23.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.23
            ExPASy - ENZYME nomenclature database: 2.3.1.23
            ExplorEnz - The Enzyme Database: 2.3.1.23
            ERGO genome analysis and discovery system: 2.3.1.23
            BRENDA, the Enzyme Database: 2.3.1.23
            CAS: 9027-64-9
///
ENTRY       EC 2.3.1.24                 Enzyme
NAME        sphingosine N-acyltransferase;
            ceramide synthetase;
            sphingosine acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:sphingosine N-acyltransferase
REACTION    acyl-CoA + sphingosine = CoA + N-acylsphingosine [RN:R01496]
ALL_REAC    R01496;
            (other) R02543 R06517
SUBSTRATE   acyl-CoA [CPD:C00040];
            sphingosine [CPD:C00319]
PRODUCT     CoA [CPD:C00010];
            N-acylsphingosine [CPD:C00195]
COMMENT     Acts on sphingosine or its 2-epimer.
REFERENCE   1  [PMID:5973195]
  AUTHORS   Sribney M.
  TITLE     Enzymatic synthesis of ceramide.
  JOURNAL   Biochim. Biophys. Acta. 125 (1966) 542-7.
  ORGANISM  chicken [GN:gga], rat [GN:rno], guinea pig
PATHWAY     PATH: map00600  Sphingolipid metabolism
ORTHOLOGY   KO: K04709  Acyl-CoA-dependent ceramide synthase
            KO: K04710  Acyl-CoA-dependent ceramide synthase
GENES       SCE: YHL003C(LAG1)
            AGO: AGOS_ABR009W
            PIC: PICST_32904(LAG1.1) PICST_45900(LAG1.3)
            CAL: CaO19_3249(CaO19.3249)
            CGR: CAGL0K02739g
            CNE: CNE04480
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.24
            ExPASy - ENZYME nomenclature database: 2.3.1.24
            ExplorEnz - The Enzyme Database: 2.3.1.24
            ERGO genome analysis and discovery system: 2.3.1.24
            BRENDA, the Enzyme Database: 2.3.1.24
            CAS: 37257-09-3
///
ENTRY       EC 2.3.1.25                 Enzyme
NAME        plasmalogen synthase;
            lysoplasmenylcholine acyltransferase;
            O-1-alkenylglycero-3-phosphorylcholine acyltransferase;
            1-alkenyl-glycero-3-phosphorylcholine:acyl-CoA acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:1-O-alk-1-enyl-glycero-3-phosphocholine 2-O-acyltransferase
REACTION    acyl-CoA + 1-O-alk-1-enyl-glycero-3-phosphocholine = CoA +
            plasmenylcholine [RN:R03109]
ALL_REAC    R03109
SUBSTRATE   acyl-CoA [CPD:C00040];
            1-O-alk-1-enyl-glycero-3-phosphocholine [CPD:C04517]
PRODUCT     CoA [CPD:C00010];
            plasmenylcholine [CPD:C00958]
REFERENCE   1  [PMID:5689955]
  AUTHORS   Waku K, Lands WE.
  TITLE     Acyl coenzyme A:1-alkenyl-glycero-3-phosphorylcholine
            acyltransferase action in plasmalogen biosynthesis.
  JOURNAL   J. Biol. Chem. 243 (1968) 2654-9.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00565  Ether lipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.25
            ExPASy - ENZYME nomenclature database: 2.3.1.25
            ExplorEnz - The Enzyme Database: 2.3.1.25
            ERGO genome analysis and discovery system: 2.3.1.25
            BRENDA, the Enzyme Database: 2.3.1.25
            CAS: 37257-10-6
///
ENTRY       EC 2.3.1.26                 Enzyme
NAME        sterol O-acyltransferase;
            cholesterol acyltransferase;
            sterol-ester synthase;
            sterol-ester synthetase;
            sterol-ester synthase;
            acyl coenzyme A-cholesterol-O-acyltransferase;
            acyl-CoA:cholesterol acyltransferase;
            ACAT;
            acylcoenzyme A:cholesterol O-acyltransferase;
            cholesterol ester synthase;
            cholesterol ester synthetase;
            cholesteryl ester synthetase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:cholesterol O-acyltransferase
REACTION    acyl-CoA + cholesterol = CoA + cholesterol ester [RN:R01461]
ALL_REAC    R01461
SUBSTRATE   acyl-CoA [CPD:C00040];
            cholesterol [CPD:C00187]
PRODUCT     CoA [CPD:C00010];
            cholesterol ester [CPD:C02530]
COMMENT     The animal enzyme is highly specific for transfer of acyl groups
            with a single cis double bond that is nine carbon atoms distant from
            the carboxy group.
REFERENCE   1  [PMID:5439042]
  AUTHORS   Sgoutas DS.
  TITLE     Effect of geometry and position of ethylenic bond upon acyl coenzyme
            A--cholesterol-O-acyltransferase.
  JOURNAL   Biochemistry. 9 (1970) 1826-33.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:42927]
  AUTHORS   Spector AA, Mathur SN, Kaduce TL.
  TITLE     Role of acylcoenzyme A: cholesterol o-acyltransferase in cholesterol
            metabolism.
  JOURNAL   Prog. Lipid. Res. 18 (1979) 31-53.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:389289]
  AUTHORS   Taketani S, Nishino T, Katsuki H.
  TITLE     Characterization of sterol-ester synthetase in Saccharomyces
            cerevisiae.
  JOURNAL   Biochim. Biophys. Acta. 575 (1979) 148-55.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00120  Bile acid biosynthesis
ORTHOLOGY   KO: K00637  sterol O-acyltransferase
GENES       HSA: 6646(SOAT1) 8435(SOAT2)
            MMU: 20652(Soat1) 223920(Soat2)
            RNO: 81782(Soat1)
            CFA: 486511(SOAT2) 490325(SOAT1)
            GGA: 424424(SOAT1)
            XLA: 446863(soat1)
            SPU: 583194(LOC583194)
            DME: Dmel_CG31991(mdy) Dmel_CG8112
            CEL: B0395.2
            SCE: YCR048W(ARE1) YNR019W(ARE2)
            AGO: AGOS_AAR065C
            PIC: PICST_33115(ARE2)
            CGR: CAGL0C02981g CAGL0M10571g
            SPO: SPAC13G7.05
            AFM: AFUA_1G06040
            AOR: AO090009000480
            CNE: CNF01130
            UMA: UM05355.1
            TET: TTHERM_00046260 TTHERM_00732710 TTHERM_00895740
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.26
            ExPASy - ENZYME nomenclature database: 2.3.1.26
            ExplorEnz - The Enzyme Database: 2.3.1.26
            ERGO genome analysis and discovery system: 2.3.1.26
            BRENDA, the Enzyme Database: 2.3.1.26
            CAS: 9027-63-8
///
ENTRY       EC 2.3.1.27                 Enzyme
NAME        cortisol O-acetyltransferase;
            cortisol acetyltransferase;
            corticosteroid acetyltransferase;
            corticosteroid-21-O-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:cortisol O-acetyltransferase
REACTION    acetyl-CoA + cortisol = CoA + cortisol 21-acetate [RN:R02837]
ALL_REAC    R02837
SUBSTRATE   acetyl-CoA [CPD:C00024];
            cortisol [CPD:C00735]
PRODUCT     CoA [CPD:C00010];
            cortisol 21-acetate [CPD:C02821]
REFERENCE   1  [PMID:4971640]
  AUTHORS   Thomas PJ.
  TITLE     Cortisol acetyltransferase from baboon brain.
  JOURNAL   Biochem. J. 109 (1968) 695-6.
  ORGANISM  baboon
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.27
            ExPASy - ENZYME nomenclature database: 2.3.1.27
            ExplorEnz - The Enzyme Database: 2.3.1.27
            ERGO genome analysis and discovery system: 2.3.1.27
            BRENDA, the Enzyme Database: 2.3.1.27
            CAS: 9076-48-6
///
ENTRY       EC 2.3.1.28                 Enzyme
NAME        chloramphenicol O-acetyltransferase;
            chloramphenicol acetyltransferase;
            chloramphenicol acetylase;
            chloramphenicol transacetylase;
            CAT I;
            CAT II;
            CAT III
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:chloramphenicol 3-O-acetyltransferase
REACTION    acetyl-CoA + chloramphenicol = CoA + chloramphenicol 3-acetate
            [RN:R03065]
ALL_REAC    R03065
SUBSTRATE   acetyl-CoA [CPD:C00024];
            chloramphenicol [CPD:C00918]
PRODUCT     CoA [CPD:C00010];
            chloramphenicol 3-acetate [CPD:C03601]
REFERENCE   1  [PMID:5335032]
  AUTHORS   Shaw WV.
  TITLE     The enzymatic acetylation of chloramphenicol by extracts of R
            factor-resistant Escherichia coli.
  JOURNAL   J. Biol. Chem. 242 (1967) 687-93.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4965980]
  AUTHORS   Shaw WV, Brodsky RF.
  TITLE     Characterization of chloramphenicol acetyltransferase from
            chloramphenicol-resistant Staphylococcus aureus.
  JOURNAL   J. Bacteriol. 95 (1968) 28-36.
  ORGANISM  Staphylococcus aureus
ORTHOLOGY   KO: K00638  chloramphenicol O-acetyltransferase
GENES       ECE: Z3906m(yfjD)
            STY: HCM1.206(cat)
            SEC: SC011(cat2)
            PLU: plu2449(cat3)
            ENT: Ent638_1533
            SPE: Spro_3634
            ASU: Asuc_1765
            VCH: VCA0300
            VVU: VV2_0610
            VVY: VVA1162
            VPA: VPA1748
            VFI: VFA0790
            PPR: PBPRB0068
            PAE: PA0706(cat)
            PAU: PA14_55170(cat)
            PAP: PSPA7_4187 PSPA7_4802
            PFL: PFL_2085
            PEN: PSEEN4077
            SON: SO_4299(cat)
            SBM: Shew185_4229
            SSE: Ssed_0017
            SHN: Shewana3_0322
            PHA: PSHAa1168
            LPN: lpg0047
            LPF: lpl0046
            LPP: lpp0048
            MMW: Mmwyl1_2950
            AHA: AHA_0037 AHA_3656
            ABU: Abu_0782(cat)
            DVU: DVU1992
            DDE: Dde_1494
            DPS: DP1720 DP2058
            MLO: mll2311
            ATU: Atu4738(cat)
            ATC: AGR_L_286
            BME: BMEI0594
            BMF: BAB1_1434
            SIT: TM1040_2320
            JAN: Jann_0057
            ZMO: ZMO1143(cat3)
            BAN: BA2409
            BAR: GBAA2409
            BAA: BA_2907
            BAT: BAS2245
            BCE: BC2447 BC3545
            BCA: BCE_2444
            BCZ: BCZK2165(cat)
            BTK: BT9727_2179(cat)
            BTL: BALH_2245 BALH_3185
            BLI: BL03127
            BLD: BLi02835
            BCL: ABC1978
            BPU: BPUM_1131(cat) BPUM_1805(cat86)
            LPL: lp_1787(cat)
            LSA: LSA1239
            LBR: LVIS_1824
            CAC: CAC0235 CA_P0060(cat)
            CTC: CTC01425
            CBO: CBO0619(cat) CBO2021(catB)
            CBA: CLB_0659(cat-1) CLB_1568(cat-2) CLB_1961(cat-3)
            CBH: CLC_0674(cat-1) CLC_1966(cat-2)
            CBF: CLI_0699(cat-1) CLI_2087(cat-2)
            CBE: Cbei_2295 Cbei_3217 Cbei_3515
            AMT: Amet_1902
            DSY: DSY0040
            RHA: RHA1_ro02201
            SEN: SACE_3683
            SYF: Synpcc7942_0704
            BTH: BT_0702
            BFR: BF2405 BF4582
            BFS: BF2487 BF4368
            DRA: DR_2303
            MMP: MMP1355
            MAC: MA1703(cat)
            MBA: Mbar_A2711
            MMA: MM_2551
STRUCTURES  PDB: 1CIA  1CLA  1NOC  1PD5  1Q23  1QCA  2CLA  3CLA  4CLA  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.28
            ExPASy - ENZYME nomenclature database: 2.3.1.28
            ExplorEnz - The Enzyme Database: 2.3.1.28
            ERGO genome analysis and discovery system: 2.3.1.28
            BRENDA, the Enzyme Database: 2.3.1.28
            CAS: 9040-07-7
///
ENTRY       EC 2.3.1.29                 Enzyme
NAME        glycine C-acetyltransferase;
            2-amino-3-ketobutyrate CoA ligase;
            2-amino-3-ketobutyrate coenzyme A ligase;
            2-amino-3-ketobutyrate-CoA ligase;
            glycine acetyltransferase;
            aminoacetone synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:glycine C-acetyltransferase
REACTION    acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate [RN:R00370]
ALL_REAC    R00370 > R00371
SUBSTRATE   acetyl-CoA [CPD:C00024];
            glycine [CPD:C00037]
PRODUCT     CoA [CPD:C00010];
            2-amino-3-oxobutanoate [CPD:C03214]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
REFERENCE   1  [PMID:5821726]
  AUTHORS   McGilvray D, Morris JG.
  TITLE     Utilization of L-threonine by a species of Arthrobacter. A novel
            catabolic role for &quot;aminoacetone synthase&quot;.
  JOURNAL   Biochem. J. 112 (1969) 657-71.
  ORGANISM  Arthrobacter sp.
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K00639  glycine C-acetyltransferase
GENES       HSA: 23464(GCAT)
            MMU: 26912(Gcat)
            CFA: 481262(GCAT)
            BTA: 319141(GCAT)
            GGA: 427905(GCAT)
            XLA: 380495(gcat)
            XTR: 394899(MGC76130)
            SPU: 583773(LOC583773)
            CEL: T25B9.1
            CME: CMO139C
            TBR: Tb927.8.6060
            TCR: 511071.140 511899.40
            LMA: LmjF35.0320
            ECO: b3617(kbl)
            ECJ: JW3592(kbl)
            ECE: Z5044(kbl)
            ECS: ECs4495
            ECC: c4444(kbl)
            ECI: UTI89_C4163(kbl)
            ECP: ECP_3718
            ECV: APECO1_2838(kbl)
            ECW: EcE24377A_4121(kbl)
            ECX: EcHS_A3829(kbl)
            STY: STY4086(kbl)
            STT: t3810(kbl)
            SPT: SPA3561(kbl)
            SEC: SC3632(kbl)
            STM: STM3709(kbl)
            YPE: YPO0059(kbl)
            YPK: y0081(kbl)
            YPM: YP_0060(kbl)
            YPA: YPA_3483
            YPN: YPN_3791
            YPP: YPDSF_3846
            YPS: YPTB0056(kbl)
            YPI: YpsIP31758_0071(kbl)
            SFL: SF3657(kbl)
            SFX: S4110(kbl)
            SFV: SFV_3911(kbl)
            SSN: SSON_3787(kbl)
            SBO: SBO_3623(kbl)
            SDY: SDY_4050(kbl)
            ECA: ECA0167(kbl)
            PLU: plu4846(kbl)
            ENT: Ent638_0118
            SPE: Spro_4824
            XCC: XCC0939(kbl)
            XCB: XC_3296
            XCV: XCV1046(kbl)
            XAC: XAC1016(kbl)
            XOO: XOO3691(kbl)
            XOM: XOO_3486(XOO3486)
            VCH: VCA0886
            VCO: VC0395_0352(kbl)
            VVU: VV2_1484
            VVY: VVA0304
            VPA: VPA1510
            VFI: VFA0418
            PPR: PBPRA1729
            SON: SO_4674(kbl)
            SDN: Sden_3615
            SFR: Sfri_3938
            SAZ: Sama_0098
            SBL: Sbal_0058
            SBM: Shew185_4340
            SLO: Shew_3709
            SPC: Sputcn32_3901
            SSE: Ssed_0101
            SPL: Spea_0107
            SHE: Shewmr4_3900
            SHM: Shewmr7_3992
            SHN: Shewana3_4104
            SHW: Sputw3181_0050
            ILO: IL0270(kbl)
            CPS: CPS_0120(kbl)
            PHA: PSHAa2316(kbl)
            PAT: Patl_0061
            PIN: Ping_1852
            CBU: CBU_0111(kbl)
            CBD: COXBU7E912_1996(kbl)
            LPN: lpg0701(kbl)
            LPF: lpl0738(kbl)
            LPP: lpp0756(kbl)
            FTU: FTT0714c(kbl)
            FTF: FTF0714c(kbl)
            FTW: FTW_1527(kbl)
            FTL: FTL_1522
            FTH: FTH_1472(kbl)
            FTA: FTA_1606(kbl)
            FTN: FTN_0626(kbl)
            HCH: HCH_01633(kbl)
            MMW: Mmwyl1_3792
            AHA: AHA_4234(kbl)
            CVI: CV_1650(kbl)
            RSO: RSp0961(kbl)
            REU: Reut_B4803
            REH: H16_B0819(kbl)
            RME: Rmet_4805
            BMA: BMAA0005(kbl)
            BMV: BMASAVP1_1151(kbl)
            BML: BMA10299_1431(kbl)
            BMN: BMA10247_A0006(kbl)
            BXE: Bxe_B3021
            BVI: Bcep1808_3788
            BUR: Bcep18194_A3875 Bcep18194_A4993 Bcep18194_B3179
            BCN: Bcen_5158
            BCH: Bcen2424_5701
            BAM: Bamb_4972
            BPS: BPSS0005(kbl)
            BPM: BURPS1710b_A1510(kbl)
            BPL: BURPS1106A_A0005(kbl)
            BPD: BURPS668_A0005(kbl)
            BTE: BTH_II0005(kbl)
            POL: Bpro_4048 Bpro_4366
            TBD: Tbd_0669
            ADE: Adeh_2094
            AFW: Anae109_2930
            SAT: SYN_00565
            SFU: Sfum_2235
            MLO: mll9204 mlr8297
            MES: Meso_0443
            SME: SMc01565(kbl)
            SMD: Smed_2225
            RET: RHE_CH02952(kbl)
            RLE: RL3405(kbl)
            BBT: BBta_1580
            SIL: SPO3360(kbl)
            SIT: TM1040_3024
            RSP: RSP_2376(kbl)
            RSH: Rsph17029_1036
            RSQ: Rsph17025_1900
            RDE: RD1_0199(kbl)
            MMR: Mmar10_1598
            SAL: Sala_2171
            ABA: Acid345_3919
            SUS: Acid_5166
            BSU: BG12610(kbl)
            BAN: BA0620
            BAR: GBAA0620
            BAA: BA_1203
            BAT: BAS0586
            BCE: BC0621
            BCA: BCE_0688
            BCZ: BCZK0530(bioF)
            BCY: Bcer98_0533
            BTK: BT9727_0530(bioF)
            BTL: BALH_0558(kbl)
            BLI: BL03659(kbl)
            BLD: BLi01924(kbl)
            BAY: RBAM_016840(kbl)
            BPU: BPUM_1604(kbl)
            OIH: OB3054
            SAU: SA0508
            SAV: SAV0550
            SAM: MW0505
            SAR: SAR0555(kbl)
            SAS: SAS0508
            SAC: SACOL0596
            SAB: SAB0501(kbl)
            SAA: SAUSA300_0535
            SAO: SAOUHSC_00532
            SAJ: SaurJH9_0573
            SAH: SaurJH1_0587
            SHA: SH2457
            SSP: SSP2205
            LSA: LSA0509(kbl)
            STH: STH1872
            AMT: Amet_3634
            CSC: Csac_1225
            SCO: SCO6800(kbl)
            SMA: SAV1627(kbl)
            ART: Arth_1311
            AAU: AAur_1460(kbl)
            PAC: PPA0403
            NCA: Noca_3756
            SEN: SACE_6390(kbl)
            PCU: pc0811
            TDE: TDE2194
            BTH: BT_1371
            BFR: BF2988
            BFS: BF2864(kbl)
            PGI: PG0481(kbl)
            SRU: SRU_0382(kbl)
            CHU: CHU_1310(kbl)
            GFO: GFO_3375(kbl)
            FJO: Fjoh_0698
            FPS: FP0157(kbl)
            DRA: DR_2346
            DGE: Dgeo_0057
            TTH: TTC1219
            TTJ: TTHA1582
            TME: Tmel_1346
            FNO: Fnod_1307
STRUCTURES  PDB: 1FC4  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.29
            ExPASy - ENZYME nomenclature database: 2.3.1.29
            ExplorEnz - The Enzyme Database: 2.3.1.29
            ERGO genome analysis and discovery system: 2.3.1.29
            BRENDA, the Enzyme Database: 2.3.1.29
            CAS: 37257-11-7
///
ENTRY       EC 2.3.1.30                 Enzyme
NAME        serine O-acetyltransferase;
            SATase;
            L-serine acetyltransferase;
            serine acetyltransferase;
            serine transacetylase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:L-serine O-acetyltransferase
REACTION    acetyl-CoA + L-serine = CoA + O-acetyl-L-serine [RN:R00586]
ALL_REAC    R00586
SUBSTRATE   acetyl-CoA [CPD:C00024];
            L-serine [CPD:C00065]
PRODUCT     CoA [CPD:C00010];
            O-acetyl-L-serine [CPD:C00979]
REFERENCE   1  [PMID:5332668]
  AUTHORS   Kredich NM, Tomkins GM.
  TITLE     The enzymic synthesis of L-cysteine in Escherichia coli and
            Salmonella typhimurium.
  JOURNAL   J. Biol. Chem. 241 (1966) 4955-65.
  ORGANISM  Escherichia coli [GN:eco], Salmonella typhimurium
REFERENCE   2  [PMID:5550822]
  AUTHORS   Smith IK, Thompson JF.
  TITLE     Purification and characterization of L-serine transacetylase and
            O-acetyl-L-serine sulfhydrylase from kidney bean seedlings
            (Phaseolus vulgaris).
  JOURNAL   Biochim. Biophys. Acta. 227 (1971) 288-95.
  ORGANISM  Phaseolus vulgaris
PATHWAY     PATH: map00272  Cysteine metabolism
            PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K00640  serine O-acetyltransferase
GENES       ATH: AT1G55920(AtSerat2;1) AT5G56760(AtSerat1;1)
            OSA: 4324655 4328659 4331528 4331861 4331941 4339425
            CME: CMA007C CMI299C
            OLU: OSTLU_87889(SAT1)
            SPO: SPAC1039.08
            TCR: 504013.40 510879.80
            LMA: LmjF34.2850
            EHI: 13.t00033 141.t00002 200.t00006 253.t00006
            ECO: b3607(cysE)
            ECJ: JW3582(cysE)
            ECE: Z5034(cysE)
            ECS: ECs4485
            ECC: c4429(cysE)
            ECI: UTI89_C4148(cysE)
            ECP: ECP_3708
            ECV: APECO1_2848(cysE)
            ECW: EcE24377A_4111(cysE)
            ECX: EcHS_A3819(cysE)
            STY: STY4096(cysE)
            STT: t3820(cysE)
            SPT: SPA3551(cysE)
            SEC: SC3622(cysE)
            STM: STM3699(cysE)
            YPE: YPO0070(cysE)
            YPK: y0072(cysE)
            YPM: YP_0070(cysE)
            YPA: YPA_3473
            YPN: YPN_3781
            YPP: YPDSF_3836
            YPS: YPTB0066(cysE)
            YPI: YpsIP31758_0080(cysE)
            SFL: SF3646(cysE)
            SFX: S4122(cysE)
            SFV: SFV_3924(cysE)
            SSN: SSON_3798(cysE)
            SBO: SBO_3613(cysE)
            SDY: SDY_4040(cysE)
            ECA: ECA0174(cysE)
            PLU: plu4837(cysE)
            BUC: BU054(cysE)
            BAS: BUsg051(cysE)
            BAB: bbp051(cysE)
            SGL: SG2183
            ENT: Ent638_0128
            SPE: Spro_2495 Spro_4814
            BFL: Bfl603(cysE)
            BPN: BPEN_625(cysE)
            HIT: NTHI0861(cysE)
            HIP: CGSHiEE_02005(cysE)
            HIQ: CGSHiGG_06970(cysE)
            HDU: HD0659(cysE)
            HSO: HS_0154(cysE)
            PMU: PM1430(cysE)
            MSU: MS2212(cysE)
            APL: APL_1511(cysE)
            ASU: Asuc_0384
            VCH: VC2649
            VCO: VC0395_A2225(cysE)
            VVU: VV1_1276
            VVY: VV3088
            VPA: VP2833
            VFI: VF2346 VF2347
            PPR: PBPRA0228
            PAE: PA3816(cysE)
            PAU: PA14_14700(cysE) PA14_54880
            PAP: PSPA7_1297
            PPU: PP_0228 PP_0840(cysE)
            PPF: Pput_0243 Pput_0870 Pput_1149
            PST: PSPTO_1421(cysE) PSPTO_5178
            PSB: Psyr_0360 Psyr_1235 Psyr_4324
            PSP: PSPPH_0344 PSPPH_1307(cysE1) PSPPH_1714(cysE2)
            PFL: PFL_0250 PFL_4967
            PFO: Pfl_0246 Pfl_4614
            PEN: PSEEN0208(srpH) PSEEN1007(cysE) PSEEN2446
            PMY: Pmen_3513
            PAR: Psyc_1180(cysE)
            PCR: Pcryo_1210
            PRW: PsycPRwf_1244
            ACI: ACIAD1584(srpH) ACIAD1763(srpH) ACIAD2091(cysE)
            SON: SO_2262(cysE)
            SDN: Sden_1456
            SFR: Sfri_2426
            SAZ: Sama_1291
            SBL: Sbal_2399
            SBM: Shew185_2388
            SLO: Shew_2319
            SPC: Sputcn32_2151
            SSE: Ssed_2873 Ssed_4170
            SPL: Spea_1486
            SHE: Shewmr4_1737
            SHM: Shewmr7_1817
            SHN: Shewana3_2282
            SHW: Sputw3181_1860
            ILO: IL0031(cysE)
            CPS: CPS_1130(cysE)
            PHA: PSHAa0645(cysE)
            PAT: Patl_1236 Patl_4078
            SDE: Sde_1084
            PIN: Ping_3299
            MAQ: Maqu_1120
            MCA: MCA1830(cysE-1) MCA2611(cysE-2)
            TCX: Tcr_0616
            NOC: Noc_1647
            AEH: Mlg_1246
            HHA: Hhal_1794
            HCH: HCH_04463(cysE)
            CSA: Csal_2551
            ABO: ABO_0514(cysE)
            MMW: Mmwyl1_3403
            AHA: AHA_0192(cysE)
            BCI: BCI_0172(cysE)
            RMA: Rmag_0579
            VOK: COSY_0534(cysE)
            NME: NMB0560
            NMA: NMA0742(cysE)
            NMC: NMC0501(cysE)
            NGO: NGO1423
            CVI: CV_0044(cysE)
            RSO: RSc1162(cysE2) RSp1439(cysE1)
            REU: Reut_A1117
            REH: H16_A1216(cysE)
            RME: Rmet_1080
            BMA: BMA1662(cysE) BMAA0041 BMAA0930
            BMV: BMASAVP1_A2165(cysE)
            BML: BMA10299_A3151(cysE)
            BMN: BMA10247_1438(cysE)
            BXE: Bxe_A1621 Bxe_B0616 Bxe_B1555 Bxe_B2247 Bxe_C0121
            BVI: Bcep1808_1985 Bcep1808_3748 Bcep1808_5986
            BUR: Bcep18194_A5389 Bcep18194_B2625 Bcep18194_B3134
                 Bcep18194_C7395
            BCN: Bcen_5118 Bcen_5994
            BCH: Bcen2424_2083 Bcen2424_3514 Bcen2424_5741
            BAM: Bamb_2118 Bamb_5012
            BPS: BPSL2248 BPSS0038 BPSS1344
            BPM: BURPS1710b_2686(cysE) BURPS1710b_3267(wcaB)
                 BURPS1710b_A0365(srpH) BURPS1710b_A1547(cysE)
            BPL: BURPS1106A_2602(cysE)
            BPD: BURPS668_2551(cysE) BURPS668_A0062
            BTE: BTH_I1936 BTH_II0041
            PNU: Pnuc_0852
            BPE: BP1972(srpH)
            BPA: BPP2351(srpH)
            BBR: BB1802(srpH)
            RFR: Rfer_2890
            POL: Bpro_3291
            PNA: Pnap_0539 Pnap_1382 Pnap_2311
            AAV: Aave_2076
            AJS: Ajs_1047
            VEI: Veis_4258 Veis_4712
            MPT: Mpe_A0026 Mpe_A2839
            HAR: HEAR0722 HEAR1279(cysE)
            MMS: mma_0640(cysE1) mma_2113(cysE2) mma_2487(cysE3)
            NEU: NE0575 NE1695
            NET: Neut_0426
            NMU: Nmul_A2073
            EBA: ebA6405(cysE)
            AZO: azo0366(srpH) azo0550(nifP) azo2019(cysE)
            DAR: Daro_1397 Daro_1947
            TBD: Tbd_1162
            MFA: Mfla_0615 Mfla_0811
            HPY: HP1210(cysE)
            HPA: HPAG1_1152
            HHE: HH1234(cysE)
            HAC: Hac_0304(cysE)
            WSU: WS0553(cysE)
            TDN: Tmden_1133
            CJE: Cj0763c(cysE)
            CJR: CJE0854(cysE)
            CJJ: CJJ81176_0784(cysE)
            CJU: C8J_0714(cysE)
            CJD: JJD26997_1249(cysE)
            CFF: CFF8240_0896(cysE)
            CCV: CCV52592_0718(cysE)
            CHA: CHAB381_0927(cysE)
            CCO: CCC13826_0082(cysE) CCC13826_1773(cysE)
            ABU: Abu_0963(cysE)
            NIS: NIS_0816
            SUN: SUN_1361
            GSU: GSU2572(cysE)
            GME: Gmet_0870
            GUR: Gura_1495
            PCA: Pcar_1862
            PPD: Ppro_0748
            DVU: DVU0662(cysE)
            DVL: Dvul_2298
            DDE: Dde_3081
            BBA: Bd3116(cysE)
            DPS: DP1241
            ADE: Adeh_1281
            AFW: Anae109_2486
            SAT: SYN_01257
            SFU: Sfum_2682
            PUB: SAR11_0790(cysE)
            MLO: mlr0175
            MES: Meso_1729
            PLA: Plav_2624
            SME: SMc02113(cysE)
            SMD: Smed_1113
            ATU: Atu1571(cysE)
            ATC: AGR_C_2895
            RET: RHE_CH01903(cysE1) RHE_CH03627(cysE2)
            RLE: RL2209(cysE) RL4152(cysE)
            BME: BMEI0734
            BMF: BAB1_1281
            BMS: BR1262(cysE)
            BMB: BruAb1_1265(cysE)
            BOV: BOV_1224
            OAN: Oant_1926
            BJA: bll5586(cysE) bll7158(cysE) blr2371(cysE)
            BRA: BRADO2093 BRADO2940 BRADO4275(srpH) BRADO5389(cysE)
            BBT: BBta_1006 BBta_1008 BBta_2405 BBta_3294(srpH) BBta_5231
                 BBta_5874(cysE)
            RPA: RPA1425(cysE1) RPA3429(cysE2)
            RPB: RPB_2135
            RPC: RPC_2024 RPC_3144 RPC_3638
            RPD: RPD_3226 RPD_3288
            RPE: RPE_2312 RPE_3185
            NWI: Nwi_2176
            NHA: Nham_2579
            XAU: Xaut_0151 Xaut_3208
            CCR: CC_2651
            SIL: SPO2247(cysE)
            SIT: TM1040_0510 TM1040_1075
            RSP: RSP_2481(cysE) RSP_3060(cysE)
            RSH: Rsph17029_1146
            RSQ: Rsph17025_0756 Rsph17025_1091
            JAN: Jann_1648
            RDE: RD1_1129(cysE) RD1_3015(cysE)
            PDE: Pden_2885 Pden_5016
            MMR: Mmar10_1067
            HNE: HNE_1850(cysE)
            ZMO: ZMO1730(cysE)
            NAR: Saro_0902
            SAL: Sala_0528
            SWI: Swit_3585 Swit_4420
            ELI: ELI_08835
            GOX: GOX0747(cysE)
            GBE: GbCGDNIH1_2272
            ACR: Acry_1767
            RRU: Rru_A0792 Rru_A2029
            MAG: amb1852 amb3031
            MGM: Mmc1_3065
            ABA: Acid345_2097
            SUS: Acid_3878
            BSU: BG10155(cysE)
            BHA: BH0110(cysE)
            BAN: BA0088(cysE)
            BAR: GBAA0088(cysE)
            BAA: BA_0677
            BAT: BAS0088
            BCE: BC0109
            BCA: BCE_0088(cysE)
            BCZ: BCZK0084(cysE) BCZK4978(sat)
            BCY: Bcer98_0083
            BTK: BT9727_0085(cysE) BT9727_4948(cysE)
            BTL: BALH_0088(cysE)
            BLI: BL03268(cysE)
            BLD: BLi00111(cysE)
            BCL: ABC0128(cysE)
            BAY: RBAM_001180(cysE)
            BPU: BPUM_0078(cysE) BPUM_1018
            OIH: OB0098(cysE)
            GKA: GK0084 GK3309
            SAU: SA0487(cysE)
            SAV: SAV0529(cysE)
            SAM: MW0484(cysE)
            SAR: SAR0532(cysE)
            SAS: SAS0486
            SAC: SACOL0575(cysE)
            SAB: SAB0479(cysE)
            SAA: SAUSA300_0514(cysE)
            SAO: SAOUHSC_00510
            SAJ: SaurJH9_0551
            SAH: SaurJH1_0565
            SEP: SE0291
            SER: SERP0169(cysE)
            SHA: SH2480(cysE)
            SSP: SSP2227
            LMO: lmo0238(cysE)
            LMF: LMOf2365_0250(cysE)
            LIN: lin0270(cysE)
            LWE: lwe0201(cysE)
            LLA: L0087(cysE)
            LLC: LACR_2045
            LLM: llmg_2042(cysE)
            SPY: SPy_1944(cysE)
            SPZ: M5005_Spy_1658(cysE)
            SPM: spyM18_2012
            SPG: SpyM3_1674(cysE)
            SPS: SPs1676
            SPH: MGAS10270_Spy1726(cysE)
            SPI: MGAS10750_Spy1752(cysE)
            SPJ: MGAS2096_Spy1681(cysE)
            SPK: MGAS9429_Spy1659(cysE)
            SPF: SpyM51631(cysE)
            SPA: M6_Spy1666
            SPB: M28_Spy1646(cysE)
            SPN: SP_0589
            SPR: spr0517(cysE)
            SPD: SPD_0513(cysE)
            SAG: SAG0205(cysE)
            SAN: gbs0200(cysE)
            SAK: SAK_0268(cysE)
            SMU: SMU.157(cysE)
            STC: str0083(cysE1) str0848(cysE2)
            STL: stu0083(cysE1) stu0848(cysE2)
            SSA: SSA_2048(cysE)
            SGO: SGO_0345(cysE)
            LPL: lp_0254(cysE)
            EFA: EF0044(cysE)
            OOE: OEOE_1757
            STH: STH3120
            CAC: CAC0687(cysE)
            CPE: CPE1321(cysE)
            CPF: CPF_1528(cysE)
            CPR: CPR_0457 CPR_1321(cysE)
            CTC: CTC00351
            CNO: NT01CX_1391 NT01CX_1782
            CTH: Cthe_2066
            CDF: CD1595(cysA)
            CBO: CBO0206(cysA)
            CBA: CLB_0247(cysE)
            CBH: CLC_0262(cysE)
            CBF: CLI_0271(cysE)
            CBE: Cbei_0578
            AMT: Amet_4502
            CHY: CHY_2339(cysE)
            DSY: DSY0446
            DRM: Dred_0192
            SWO: Swol_2356
            CSC: Csac_0707
            TTE: TTE2316(cysE)
            MTA: Moth_2485
            MTU: Rv2335(cysE)
            MTC: MT2398
            MBO: Mb2363(cysE)
            MBB: BCG_2357
            MLE: ML0838(cysE)
            MPA: MAP2124(cysE)
            MAV: MAV_2051(cysE)
            MSM: MSMEG_5947(cysE)
            CGL: NCgl2474(cgl2563)
            CGB: cg2834(cysE)
            CEF: CE2447
            CDI: DIP1891(cysE)
            CJK: jk0393(cysE)
            RHA: RHA1_ro05440
            LXX: Lxx06920(cysE)
            CMI: CMM_0654(cysE)
            ART: Arth_2447
            AAU: AAur_2418(cysE)
            PAC: PPA1765
            NCA: Noca_4306
            FRA: Francci3_2426
            FAL: FRAAL3351(cysE) FRAAL6257
            SEN: SACE_2889(cysE)
            RBA: RB5098
            LIL: LA0062(cysE1) LA1598(cysE2) LA1821(cysE3)
            LIC: LIC10055(cysE) LIC12184
            LBJ: LBJ_0053(cysE)
            LBL: LBL_3007(cysE)
            SYN: slr1348(cysE)
            SYW: SYNW0090(cysE)
            SYC: syc1686_c(cysE)
            SYF: Synpcc7942_2420 Synpcc7942_B2663
            SYD: Syncc9605_0082
            SYE: Syncc9902_0129
            SYG: sync_0087(cysE)
            SYR: SynRCC307_0087(cysE)
            SYX: SynWH7803_0142(cysE)
            CYA: CYA_0556(cysE)
            CYB: CYB_2852(cysE)
            TEL: tlr0851(cysE)
            GVI: gll1785 glr2514(cysE)
            ANA: all4037 alr1404
            AVA: Ava_1668 Ava_3953 Ava_5017
            PMA: Pro1800(cysE)
            PMM: PMM1638(cysE)
            PMT: PMT0117(cysE)
            PMN: PMN2A_1217
            PMI: PMT9312_1731
            PMB: A9601_18481(cysE)
            PMC: P9515_18271(cysE)
            PMF: P9303_01521(cysE)
            PMG: P9301_18291(cysE)
            PME: NATL1_20921(cysE)
            TER: Tery_3017 Tery_4132
            BTH: BT_0607 BT_3256
            BFR: BF0087
            BFS: BF0099
            PGI: PG0115
            CHU: CHU_0685(cysE) CHU_1816(cysE)
            GFO: GFO_1531(cysE)
            FJO: Fjoh_2505
            CTE: CT1436(cysE)
            CCH: Cag_1261
            CPH: Cpha266_1806
            PVI: Cvib_1254
            PLT: Plut_1437
            DET: DET1588(cysE)
            DEH: cbdb_A1678(cysE)
            DEB: DehaBAV1_1336
            RCA: Rcas_2139
            DGE: Dgeo_0348
            TMA: TM0666
            TPT: Tpet_0265
            TME: Tmel_1230
            FNO: Fnod_0465
            MVN: Mevan_0177
            MAC: MA2721 MA3442(cysE)
            MBA: Mbar_A2421
            MMA: MM_2939 MM_3269
            MBU: Mbur_0414
            MHU: Mhun_2211
            MEM: Memar_0453
            MBN: Mboo_1982
            MST: Msp_0450
            MSI: Msm_0270
            HAL: VNG1481G(sat)
            HMA: pNG7330(cysE1) rrnAC1087(cysE2)
            HWA: HQ1785A(cysE)
            NPH: NP4172A(cysE)
STRUCTURES  PDB: 1S80  1SSM  1SSQ  1SST  1T3D  1Y7L  2ISQ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.30
            ExPASy - ENZYME nomenclature database: 2.3.1.30
            ExplorEnz - The Enzyme Database: 2.3.1.30
            ERGO genome analysis and discovery system: 2.3.1.30
            BRENDA, the Enzyme Database: 2.3.1.30
            CAS: 9023-16-9
///
ENTRY       EC 2.3.1.31                 Enzyme
NAME        homoserine O-acetyltransferase;
            homoserine acetyltransferase;
            homoserine transacetylase;
            homoserine-O-transacetylase;
            L-homoserine O-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:L-homoserine O-acetyltransferase
REACTION    acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine [RN:R01776]
ALL_REAC    R01776
SUBSTRATE   acetyl-CoA [CPD:C00024];
            L-homoserine [CPD:C00263]
PRODUCT     CoA [CPD:C00010];
            O-acetyl-L-homoserine [CPD:C01077]
REFERENCE   1  [PMID:6037552]
  AUTHORS   Nagai S, Flavin M.
  TITLE     Acetylhomoserine. An intermediate in the fungal biosynthesis of
            methionine.
  JOURNAL   J. Biol. Chem. 242 (1967) 3884-95.
  ORGANISM  Neurospora sp.
PATHWAY     PATH: map00271  Methionine metabolism
            PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K00641  homoserine O-acetyltransferase
GENES       SPU: 584214(LOC584214)
            SCE: YNL277W(MET2)
            AGO: AGOS_AEL098W AGOS_AFR682C
            PIC: PICST_30795(MET23) PICST_76901(MET2)
            CAL: CaO19.1159
            CGR: CAGL0J08316g
            SPO: SPBC106.17c SPBC56F2.11
            ANI: AN0875.2 AN2229.2 AN8565.2
            AFM: AFUA_1G15350 AFUA_5G07210 AFUA_5G08600
            AOR: AO090005001181 AO090120000210 AO090701000235
            CNE: CNL04980
            UMA: UM03425.1
            HIN: HI1263(met2)
            HIT: NTHI1901(metX)
            HSO: HS_1076(metX)
            PMU: PM0866(met2)
            MSU: MS0924(mET2)
            APL: APL_0441(metX)
            ASU: Asuc_1733
            XFA: XF0863 XF2465
            XFT: PD1484(met2) PD1813(met2)
            XCC: XCC2228(met) XCC2857(metA)
            XCB: XC_1251 XC_1889
            XCV: XCV2531(metX) XCV3177
            XAC: XAC2332(met) XAC3040(metA)
            XOO: XOO1817(metA) XOO2093(met)
            XOM: XOO_1716(XOO1716) XOO_1980(XOO1980)
            PAE: PA0390(metX)
            PAU: PA14_05080(metX)
            PAP: PSPA7_0489(metX)
            PPU: PP_5097(metX)
            PPF: Pput_4970
            PST: PSPTO_5049
            PSB: Psyr_0474
            PSP: PSPPH_0465(metX)
            PFL: PFL_5842
            PFO: Pfl_5323
            PEN: PSEEN0315(metX)
            PMY: Pmen_4155
            PAR: Psyc_0375(metX)
            PCR: Pcryo_0414
            PRW: PsycPRwf_2058
            ACI: ACIAD0529(metX)
            ILO: IL2013 IL2157
            PHA: PSHAa2945(metX)
            PAT: Patl_1978
            SDE: Sde_3644
            MAQ: Maqu_0532
            TCX: Tcr_1839
            AEH: Mlg_0338
            HHA: Hhal_0949
            HCH: HCH_06359(metX)
            CSA: Csal_3057
            ABO: ABO_2576(metX)
            MMW: Mmwyl1_4332
            NME: NMB0940
            NMA: NMA1136(metX)
            NGO: NGO0933
            CVI: CV_0786
            RSO: RSc0027(metX)
            REU: Reut_A0186
            REH: H16_A0211(metX)
            RME: Rmet_0143
            BMA: BMA3246
            BMV: BMASAVP1_A2907(metX)
            BML: BMA10299_A2182(metX)
            BMN: BMA10247_3441(metX)
            BXE: Bxe_A4388 Bxe_B0598
            BVI: Bcep1808_3183
            BUR: Bcep18194_A6450
            BCN: Bcen_2485
            BCH: Bcen2424_3099
            BAM: Bamb_3154
            BPS: BPSL0197
            BPM: BURPS1710b_0377(metX)
            BPL: BURPS1106A_0192(metX)
            BPD: BURPS668_0182(metX)
            BTE: BTH_I0157(metX)
            PNU: Pnuc_2011
            BPE: BP0047(metX)
            BPA: BPP4083(metX)
            BBR: BB4554(metX)
            RFR: Rfer_0406
            POL: Bpro_3324 Bpro_4889
            PNA: Pnap_4102
            AAV: Aave_4778
            AJS: Ajs_4125
            VEI: Veis_0147
            MPT: Mpe_A0896 Mpe_A3584 Mpe_B0611
            HAR: HEAR0152(metX)
            MMS: mma_0181
            NEU: NE2186(metX)
            NET: Neut_0528
            NMU: Nmul_A0221
            EBA: ebA2806(metX)
            AZO: azo3971(metX)
            DAR: Daro_0130
            MFA: Mfla_2480 Mfla_2563
            WSU: WS1893(pyrB)
            TDN: Tmden_0764
            CJR: CJE1895(metX)
            CJJ: CJJ81176_0023(metX)
            CJD: JJD26997_2102(metX)
            CFF: CFF8240_0613(metX)
            CCV: CCV52592_0980(metX)
            CHA: CHAB381_0909(metX)
            CCO: CCC13826_0275(metX)
            ABU: Abu_1376(metX)
            NIS: NIS_1276
            SUN: SUN_1790
            GSU: GSU2462
            GME: Gmet_2783
            GUR: Gura_0583
            PCA: Pcar_0422
            PPD: Ppro_3500
            DPS: DP1243
            ADE: Adeh_1400
            AFW: Anae109_2430
            SAT: SYN_01260
            PUB: SAR11_0217(metX)
            MLO: mlr3538
            PLA: Plav_1581
            RLE: pRL100137(metX)
            BJA: bll7862 blr1399(metX)
            BRA: BRADO0669 BRADO5724 BRADO5867 BRADO6461(metX)
            BBT: BBta_1186(metX) BBta_6236 BBta_7515
            RPA: RPA4437(metX)
            RPB: RPB_4252
            RPC: RPC_4281
            RPD: RPD_4099
            RPE: RPE_4340
            NWI: Nwi_0585
            NHA: Nham_0676
            XAU: Xaut_1909
            CCR: CC_0525
            MMR: Mmar10_2619
            ZMO: ZMO0225(metX)
            SAL: Sala_2886
            SWI: Swit_3005
            ELI: ELI_11410
            GOX: GOX0203
            GBE: GbCGDNIH1_0142
            ACR: Acry_0437
            RRU: Rru_A3266
            MAG: amb3972
            MGM: Mmc1_3190
            ABA: Acid345_3918 Acid345_4498
            SUS: Acid_1433 Acid_4622
            BAN: BA4983
            BAR: GBAA4983
            BAA: BA_5402
            BAT: BAS4629
            BCE: BC4730
            BCA: BCE_4873
            BCZ: BCZK4482(metX)
            BTK: BT9727_4463(metX)
            BTL: BALH_4306(metX)
            SAU: SA0011
            SAV: SAV0012
            SAM: MW0012
            SAR: SAR0012
            SAC: SACOL0012
            SAB: SAB0012
            SAA: SAUSA300_0012
            SAO: SAOUHSC_00013
            SEP: SE0011
            SER: SERP2541
            SHA: SH0011
            SSP: SSP0012
            LMO: lmo0594
            LMF: LMOf2365_0623(metX)
            LIN: lin0603
            LWE: lwe0561(metX)
            STH: STH1685 STH2786
            CHY: CHY_1903(metX)
            CSC: Csac_1575
            MTA: Moth_1308
            MTU: Rv3341(metA)
            MTC: MT3444(metA)
            MBO: Mb3373(metA)
            MBB: BCG_3411(metA)
            MLE: ML0682(metA)
            MPA: MAP3458(metA)
            MAV: MAV_4316(metX)
            MSM: MSMEG_1651(metX)
            MVA: Mvan_1553
            MGI: Mflv_4876
            MMC: Mmcs_0036 Mmcs_1207
            MKM: Mkms_0045 Mkms_1224
            MJL: Mjls_0026 Mjls_1234
            CGL: NCgl0624(metX) NCgl0805(cgl0839)
            CGB: cg0754(metX) cg0961
            CEF: CE0678(metX)
            CDI: DIP0623(metX)
            CJK: jk1695(metX)
            NFA: nfa9220
            RHA: RHA1_ro06236(metX1) RHA1_ro08186 RHA1_ro10186(metX2)
            LXX: Lxx18950(metA)
            CMI: CMM_1335(metX)
            ART: Arth_1318
            AAU: AAur_1475(metX)
            NCA: Noca_3630
            TFU: Tfu_2822
            FRA: Francci3_2831
            FAL: FRAAL4363(metX)
            KRA: Krad_0514
            RXY: Rxyl_1089
            RBA: RB8222(metX)
            LIL: LA2061(metX)
            LIC: LIC11853(metX)
            LBJ: LBJ_1944(metX)
            LBL: LBL_1340(metX)
            SYC: syc2377_c(metX)
            SYF: Synpcc7942_1714
            CYB: CYB_2913
            GVI: gll2500
            AVA: Ava_4076
            SRU: SRU_0480(metX)
            CHU: CHU_0136(metX)
            GFO: GFO_0317(metX)
            FPS: FP0256(metX)
            CTE: CT0605(met2)
            CCH: Cag_1206
            CPH: Cpha266_1766
            PVI: Cvib_1183
            PLT: Plut_0593
            RRS: RoseRS_1759
            RCA: Rcas_2039
            DRA: DR_0872
            DGE: Dgeo_0517 Dgeo_0807
            TTH: TTC0407
            TTJ: TTHA0759
            MAC: MA2714(metA)
            MBA: Mbar_A2428
            MBU: Mbur_0798
            MHU: Mhun_2201
            MBN: Mboo_2043
            MST: Msp_0676(metX) Msp_1526
            MSI: Msm_0175
            HAL: VNG2420G(metA)
            HMA: rrnAC3064(metA)
            HWA: HQ3700A(metA)
            NPH: NP0282A(metA)
            RCI: RCIX1556(metX)
STRUCTURES  PDB: 2B61  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.31
            ExPASy - ENZYME nomenclature database: 2.3.1.31
            ExplorEnz - The Enzyme Database: 2.3.1.31
            ERGO genome analysis and discovery system: 2.3.1.31
            BRENDA, the Enzyme Database: 2.3.1.31
            CAS: 9030-72-2
///
ENTRY       EC 2.3.1.32                 Enzyme
NAME        lysine N-acetyltransferase;
            lysine acetyltransferase;
            acetyl-phosphate:L-lysine 6-N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-phosphate:L-lysine N6-acetyltransferase
REACTION    acetyl phosphate + L-lysine = phosphate + N6-acetyl-L-lysine
            [RN:R01620]
ALL_REAC    R01620
SUBSTRATE   acetyl phosphate [CPD:C00227];
            L-lysine [CPD:C00047]
PRODUCT     phosphate [CPD:C00009];
            N6-acetyl-L-lysine [CPD:C02727]
REFERENCE   1  [PMID:14240571]
  AUTHORS   PAIK WK, KIM S.
  TITLE     ENZYMIC SYNTHESIS OF EPSILON-N-ACETYL-L-LYSINE.
  JOURNAL   Arch. Biochem. Biophys. 108 (1964) 221-9.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.32
            ExPASy - ENZYME nomenclature database: 2.3.1.32
            ExplorEnz - The Enzyme Database: 2.3.1.32
            ERGO genome analysis and discovery system: 2.3.1.32
            BRENDA, the Enzyme Database: 2.3.1.32
            CAS: 37257-12-8
///
ENTRY       EC 2.3.1.33                 Enzyme
NAME        histidine N-acetyltransferase;
            acetylhistidine synthetase;
            histidine acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:L-histidine N-acetyltransferase
REACTION    acetyl-CoA + L-histidine = CoA + N-acetyl-L-histidine [RN:R01160]
ALL_REAC    R01160
SUBSTRATE   acetyl-CoA [CPD:C00024];
            L-histidine [CPD:C00135]
PRODUCT     CoA [CPD:C00010];
            N-acetyl-L-histidine [CPD:C02997]
REFERENCE   1  [PMID:5971525]
  AUTHORS   Baslow MH.
  TITLE     N -acetyl-L-histidine synthetase activity from the brain of the
            killifish.
  JOURNAL   Brain. Res. 3 (1966) 210-3.
  ORGANISM  killifish
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.33
            ExPASy - ENZYME nomenclature database: 2.3.1.33
            ExplorEnz - The Enzyme Database: 2.3.1.33
            ERGO genome analysis and discovery system: 2.3.1.33
            BRENDA, the Enzyme Database: 2.3.1.33
            CAS: 9027-59-2
///
ENTRY       EC 2.3.1.34                 Enzyme
NAME        D-tryptophan N-acetyltransferase;
            D-tryptophan acetyltransferase;
            acetyl-CoA-D-tryptophan-alpha-N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:D-tryptophan N-acetyltransferase
REACTION    acetyl-CoA + D-tryptophan = CoA + N-acetyl-D-tryptophan [RN:R02481]
ALL_REAC    R02481
SUBSTRATE   acetyl-CoA [CPD:C00024];
            D-tryptophan [CPD:C00525]
PRODUCT     CoA [CPD:C00010];
            N-acetyl-D-tryptophan [CPD:C03137]
REFERENCE   1
  AUTHORS   Zenk, M.H. and Schmitt, J.
  TITLE     Enzymatische Acetylierung von D-Tryptophan.
  JOURNAL   Naturwissenschaften 51 (1964) 510-511.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.34
            ExPASy - ENZYME nomenclature database: 2.3.1.34
            ExplorEnz - The Enzyme Database: 2.3.1.34
            ERGO genome analysis and discovery system: 2.3.1.34
            BRENDA, the Enzyme Database: 2.3.1.34
            CAS: 37257-13-9
///
ENTRY       EC 2.3.1.35                 Enzyme
NAME        glutamate N-acetyltransferase;
            ornithine transacetylase;
            alpha-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase;
            acetylglutamate synthetase;
            acetylglutamate-acetylornithine transacetylase;
            acetylglutamic synthetase;
            acetylglutamic-acetylornithine transacetylase;
            acetylornithinase;
            acetylornithine glutamate acetyltransferase;
            glutamate acetyltransferase;
            N-acetyl-L-glutamate synthetase;
            N-acetylglutamate synthase;
            N-acetylglutamate synthetase;
            ornithine acetyltransferase;
            2-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     N2-acetyl-L-ornithine:L-glutamate N-acetyltransferase
REACTION    N2-acetyl-L-ornithine + L-glutamate = L-ornithine +
            N-acetyl-L-glutamate [RN:R02282]
ALL_REAC    R02282
SUBSTRATE   N2-acetyl-L-ornithine [CPD:C00437];
            L-glutamate [CPD:C00025]
PRODUCT     L-ornithine [CPD:C00077];
            N-acetyl-L-glutamate [CPD:C00624]
COMMENT     Also has some hydrolytic activity on acetyl-L-ornithine, but the
            rate is 1% of that of transferase activity.
REFERENCE   1  [PMID:5972370]
  AUTHORS   Staub M, Denes G.
  TITLE     Mechanism of arginine biosynthesis in Chlamydomonas reinhardti. I.
            Purification and properties of ornithine acetyltransferase.
  JOURNAL   Biochim. Biophys. Acta. 128 (1966) 82-91.
  ORGANISM  Chlamydomonas reinhardti
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K00642  glutamate N-acetyltransferase
GENES       ATH: AT2G37500
            OSA: 4332434
            CME: CMS424C
            SCE: YJL071W(ARG2) YMR062C(ECM40)
            AGO: AGOS_ADR138C
            PIC: PICST_60752(ECM40)
            CGR: CAGL0F06501g
            SPO: SPBC1271.14
            ANI: AN7722.2
            AFM: AFUA_5G08120
            AOR: AO090701000729
            CNE: CND03570
            DDI: DDB_0231449(argJ)
            PAE: PA4402(argJ)
            PAU: PA14_57210(argJ)
            PAP: PSPA7_4973(argJ)
            PPU: PP_1346(argJ)
            PST: PSPTO_4399(argJ)
            PSB: Psyr_4093(argJ)
            PSP: PSPPH_4099(argJ)
            PFL: PFL_4780(argJ)
            PFO: Pfl_4427
            PEN: PSEEN4476(argJ)
            PAR: Psyc_1198(argJ)
            PCR: Pcryo_1193
            ACI: ACIAD0650(argJ)
            CPS: CPS_1312(argJ)
            SDE: Sde_0857
            MAQ: Maqu_2442
            MCA: MCA1679(argJ)
            TCX: Tcr_0590
            NOC: Noc_2850
            AEH: Mlg_2085
            HHA: Hhal_2026
            HCH: HCH_05872(argJ)
            CSA: Csal_2180
            ABO: ABO_0608(argJ)
            RMA: Rmag_0704
            NME: NMB2005
            NMA: NMA0435(argJ)
            NMC: NMC1982(argJ)
            NGO: NGO1194
            CVI: CV_0478(argJ)
            RSO: RSc2833(argJ)
            REU: Reut_A2969(argJ)
            RME: Rmet_3117
            BMA: BMA2539(argJ)
            BMV: BMASAVP1_A0461(argJ)
            BML: BMA10299_A1319(argJ)
            BMN: BMA10247_3243(argJ)
            BVI: Bcep1808_0545
            BUR: Bcep18194_A3655
            BCN: Bcen_0088
            BCH: Bcen2424_0570
            BAM: Bamb_0473
            BPS: BPSL3015(argJ)
            BPM: BURPS1710b_3534(argJ)
            BPL: BURPS1106A_3539(argJ)
            BPD: BURPS668_3514(argJ)
            BTE: BTH_I1128(argJ)
            PNU: Pnuc_0179
            BPE: BP3807(argJ)
            BPA: BPP3953(argJ)
            BBR: BB4426(argJ)
            RFR: Rfer_2910
            POL: Bpro_0829
            PNA: Pnap_0739
            AAV: Aave_3688
            AJS: Ajs_0797
            VEI: Veis_3927
            HAR: HEAR2797(argJ)
            MMS: mma_3004
            NEU: NE2213(argJ)
            NET: Neut_0655
            NMU: Nmul_A1010(argJ)
            EBA: ebA1431(argJ)
            DAR: Daro_3487(argJ)
            TBD: Tbd_0029(argJ)
            HHE: HH1291(argJ)
            WSU: WS0330(argJ)
            TDN: Tmden_1600
            CFF: CFF8240_0973(argJ)
            CCV: CCV52592_0720(argJ) CCV52592_1326
            CHA: CHAB381_0772(argJ)
            ABU: Abu_1791(argJ)
            NIS: NIS_0318(argJ)
            SUN: SUN_2160
            GSU: GSU2049(argJ)
            GME: Gmet_0952(argJ)
            PCA: Pcar_2322(argJ)
            PPD: Ppro_0715
            DVU: DVU0823(argJ)
            DDE: Dde_1081(argJ)
            LIP: LI0714(argJ)
            DPS: DP2741
            ADE: Adeh_0587 Adeh_1156
            SAT: SYN_01035
            SFU: Sfum_1201
            ERU: Erum3800(argJ)
            ERW: ERWE_CDS_03920(argJ)
            ERG: ERGA_CDS_03880(argJ)
            ECN: Ecaj_0370(argJ)
            ECH: ECH_0676(argJ)
            MLO: mll3461
            MES: Meso_3012
            SME: SMc02450(argJ)
            ATU: Atu3518(argJ)
            ATC: AGR_L_2624
            RET: RHE_CH03768(argJ)
            RLE: RL4296(argJ)
            BME: BMEI0124
            BMF: BAB1_1942(argJ)
            BMS: BR1941(argJ)
            BMB: BruAb1_1917(argJ)
            BOV: BOV_1868(argJ)
            BJA: blr0206(argJ)
            RPA: RPA0592(argJ)
            RPB: RPB_0030(argJ)
            RPC: RPC_0524
            RPD: RPD_0111
            RPE: RPE_0148
            NWI: Nwi_0388(argJ)
            BHE: BH02010(argJ)
            BQU: BQ01890(argJ)
            BBK: BARBAKC583_0363(argJ)
            CCR: CC_3066
            SIL: SPO0059(argJ)
            RSP: RSP_1167(argJ)
            RSH: Rsph17029_2829
            RDE: RD1_0384(argJ)
            HNE: HNE_3174(argJ)
            ZMO: ZMO0923
            NAR: Saro_1993
            SAL: Sala_0155
            ELI: ELI_05085
            GOX: GOX1676
            GBE: GbCGDNIH1_0624
            RRU: Rru_A0394
            MAG: amb0510
            MGM: Mmc1_1396
            SUS: Acid_2748
            BSU: BG10192(argJ)
            BHA: BH2899(argJ)
            BAN: BA4354(argJ)
            BAR: GBAA4354(argJ)
            BAA: BA_4811(argJ)
            BAT: BAS4039
            BCE: BC4129
            BCA: BCE_4202(argJ)
            BCZ: BCZK3886(argJ)
            BTK: BT9727_3878(argJ)
            BLI: BL03242(argJ)
            BLD: BLi01207(argJ)
            BCL: ABC2557(argJ)
            BAY: RBAM_011200
            BPU: BPUM_1043
            OIH: OB1076(argJ)
            GKA: GK0791
            SAU: SA0177(argJ)
            SAV: SAV0183(argJ)
            SAM: MW0157(argJ)
            SAR: SAR0184(argJ)
            SAS: SAS0158
            SAC: SACOL0168(argJ)
            SAB: SAB0123c
            SAA: SAUSA300_0185(argJ)
            SAO: SAOUHSC_00148
            SEP: SE1211
            SER: SERP1091(argJ)
            SSP: SSP0222
            LMO: lmo1590(argJ)
            LMF: LMOf2365_1612(argJ)
            LIN: lin1632(argJ)
            LWE: lwe1603(argJ)
            LLA: L0105(argJ)
            LLC: LACR_0857
            LLM: llmg_1757(argJ)
            SMU: SMU.664(argJ)
            STC: str0465(argJ)
            STL: stu0465(argJ)
            SSA: SSA_0758(argJ)
            SGO: SGO_1568(argJ)
            LPL: lp_0529(argJ)
            STH: STH2890
            CAC: CAC2391(argJ) CAC3020
            CNO: NT01CX_2378(argJ)
            CTH: Cthe_0081
            CDF: CD2033(argJ)
            CKL: CKL_1554(argJ)
            CHY: CHY_2264(argJ)
            DSY: DSY0761
            SWO: Swol_2290
            TTE: TTE2497(argJ)
            MTA: Moth_2289(argJ)
            MTU: Rv1653(argJ)
            MTC: MT1691(argJ)
            MBO: Mb1681(argJ)
            MBB: BCG_1692(argJ)
            MLE: ML1407(argJ)
            MPA: MAP1362(argJ)
            MAV: MAV_3117(argJ)
            MSM: MSMEG_3775(argJ)
            MGI: Mflv_3529
            CGL: NCgl1341(argJ)
            CGB: cg1581(argJ)
            CEF: CE1527(argJ)
            CDI: DIP1168(argJ)
            CJK: jk0842(argJ)
            NFA: nfa19370(argJ)
            RHA: RHA1_ro00955(argJ)
            SCO: SCO1579(argJ)
            SMA: SAV6764(argJ)
            LXX: Lxx06040(argJ)
            CMI: CMM_2000(argJ)
            AAU: AAur_1632(argJ)
            PAC: PPA1349(argJ)
            TFU: Tfu_2056(argJ)
            FRA: Francci3_3174(argJ)
            FAL: FRAAL5207(argJ)
            ACE: Acel_1262
            SEN: SACE_5261(argJ)
            STP: Strop_1889
            BLO: BL1063(argJ)
            RXY: Rxyl_2886
            RBA: RB3255(argJ)
            LIL: LA4105(argJ)
            LIC: LIC13271(argJ)
            LBJ: LBJ_0184(argJ)
            LBL: LBL_2899(argJ)
            SYN: sll1883(argJ)
            SYW: SYNW2353(argJ)
            SYC: syc2199_d(argJ)
            SYF: Synpcc7942_1896
            SYD: Syncc9605_2489(argJ)
            SYE: Syncc9902_2166(argJ)
            SYG: sync_2736(argJ)
            SYR: SynRCC307_2373(argJ)
            SYX: SynWH7803_2383(argJ)
            CYA: CYA_1327(argJ)
            CYB: CYB_2548(argJ)
            TEL: tll1911(argJ)
            GVI: glr4034(argJ)
            ANA: alr2073 alr4235(argJ)
            AVA: Ava_0671(argJ) Ava_3118(argJ)
            PMA: Pro0054(argJ)
            PMM: PMM0050(argJ)
            PMT: PMT2135(argJ)
            PMN: PMN2A_1383(argJ)
            PMI: PMT9312_0051
            PMB: A9601_00511(argJ)
            PMC: P9515_00571(argJ)
            PMF: P9303_28231(argJ)
            PMG: P9301_00531(argJ)
            PME: NATL1_00641(argJ)
            TER: Tery_0043
            CTE: CT1110(argJ)
            CCH: Cag_0773(argJ)
            PVI: Cvib_0878
            DET: DET1256(argJ)
            DEH: cbdb_A1179(argJ)
            RRS: RoseRS_0886
            RCA: Rcas_4089
            DRA: DR_1704
            TTH: TTC0835
            TTJ: TTHA1196
            AAE: aq_970(argJ)
            TMA: TM1783
            TPT: Tpet_1070
            MJA: MJ0186(argJ)
            MMP: MMP0897(argJ)
            MMQ: MmarC5_0705
            MAE: Maeo_0823
            MAC: MA3564(argJ)
            MBA: Mbar_A2003
            MMA: MM_0474
            MBU: Mbur_1340
            MHU: Mhun_3229
            MBN: Mboo_0070
            MTH: MTH182
            MKA: MK0865
            AFU: AF1147(argJ)
STRUCTURES  PDB: 1VRA  1VZ6  1VZ7  1VZ8  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.35
            ExPASy - ENZYME nomenclature database: 2.3.1.35
            ExplorEnz - The Enzyme Database: 2.3.1.35
            ERGO genome analysis and discovery system: 2.3.1.35
            BRENDA, the Enzyme Database: 2.3.1.35
            CAS: 37257-14-0
///
ENTRY       EC 2.3.1.36                 Enzyme
NAME        D-amino-acid N-acetyltransferase;
            D-amino acid acetyltransferase;
            D-amino acid-alpha-N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:D-amino-acid N-acetyltransferase
REACTION    acetyl-CoA + a D-amino acid = CoA + an N-acetyl-D-amino acid
            [RN:R02191]
ALL_REAC    R02191 > R03903
SUBSTRATE   acetyl-CoA [CPD:C00024];
            D-amino acid [CPD:C00405]
PRODUCT     CoA [CPD:C00010];
            N-acetyl-D-amino acid [CPD:C03135]
REFERENCE   1
  AUTHORS   Zenk, M.H. and Schmitt, J.
  TITLE     Reinigung und Eigenschaften von
            Acetyl-CoA:D-Aminosaure-alpha-N-Acetyltransferase aus Hefe.
  JOURNAL   Biochem. Z. 342 (1965) 54-65.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00360  Phenylalanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.36
            ExPASy - ENZYME nomenclature database: 2.3.1.36
            ExplorEnz - The Enzyme Database: 2.3.1.36
            ERGO genome analysis and discovery system: 2.3.1.36
            BRENDA, the Enzyme Database: 2.3.1.36
            CAS: 37257-15-1
///
ENTRY       EC 2.3.1.37                 Enzyme
NAME        5-aminolevulinate synthase;
            ALAS;
            ALA synthase;
            alpha-aminolevulinic acid synthase;
            delta-aminolevulinate synthase;
            delta-aminolevulinate synthetase;
            delta-aminolevulinic acid synthase;
            delta-aminolevulinic acid synthetase;
            delta-aminolevulinic synthetase;
            5-aminolevulinate synthetase;
            5-aminolevulinic acid synthetase;
            ALA synthetase;
            aminolevulinate synthase;
            aminolevulinate synthetase;
            aminolevulinic acid synthase;
            aminolevulinic acid synthetase;
            aminolevulinic synthetase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     succinyl-CoA:glycine C-succinyltransferase (decarboxylating)
REACTION    succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 [RN:R00830]
ALL_REAC    R00830;
            (other) R00371 R00831 R02270
SUBSTRATE   succinyl-CoA [CPD:C00091];
            glycine [CPD:C00037]
PRODUCT     5-aminolevulinate [CPD:C00430];
            CoA [CPD:C00010];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. The enzyme in erythrocytes is
            genetically distinct from that in other tissues.
REFERENCE   1
  AUTHORS   Bishop, D.F., Henderson, A.S. and Astrin, K.H.
  TITLE     Human delta-aminolevulinate synthase - assignment of the
            housekeeping gene to 3p21 and the erythroid-specific gene to the
            X-chromosome.
  JOURNAL   Genomics 7 (1990) 207-214.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:13598764]
  AUTHORS   KIKUCHI G, KUMAR A, TALMAGE P, SHEMIN D.
  TITLE     The enzymatic synthesis of delta-aminolevulinic acid.
  JOURNAL   J. Biol. Chem. 233 (1958) 1214-9.
  ORGANISM  Rhodopseudomonas spheroides, Rhodospirillum rubrum [GN:rru]
REFERENCE   3  [PMID:4685279]
  AUTHORS   Ramaswamy NK, Nair PM.
  TITLE     -Aminolevulinic acid synthetase from cold-stored potatoes.
  JOURNAL   Biochim. Biophys. Acta. 293 (1973) 269-77.
  ORGANISM  Solanum tuberosum [GN:estu]
REFERENCE   4  [PMID:4624703]
  AUTHORS   Scholnick PL, Hammaker LE, Marver HS.
  TITLE     Souble  -aminolevulinic acid synthetase of rat liver. I. Some
            properties of the partially purified enzyme.
  JOURNAL   J. Biol. Chem. 247 (1972) 4126-31.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:5035685]
  AUTHORS   Scholnick PL, Hammaker LE, Marver HS.
  TITLE     Soluble  -aminolevulinic acid synthetase of rat liver. II. Studies
            related to the mechanism of enzyme action and hemin inhibition.
  JOURNAL   J. Biol. Chem. 247 (1972) 4132-7.
  ORGANISM  rat [GN:rno]
REFERENCE   6  [PMID:4722442]
  AUTHORS   Tait GH.
  TITLE     Aminolaevulinate synthetase of Micrococcus denitrificans.
            Purification and properties of the enzyme, and the effect of growth
            conditions on the enzyme activity in cells.
  JOURNAL   Biochem. J. 131 (1973) 389-403.
  ORGANISM  Micrococcus denitrificans
REFERENCE   7  [PMID:5315997]
  AUTHORS   Warnick GR, Burnham BF.
  TITLE     Regulation of prophyrin biosynthesis. Purification and
            characterization of -aminolevulinic acid synthase.
  JOURNAL   J. Biol. Chem. 246 (1971) 6880-5.
  ORGANISM  Rhodopseudomonas spheroides
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K00643  5-aminolevulinate synthase
GENES       HSA: 211(ALAS1) 212(ALAS2)
            PTR: 473626(ALAS2)
            MMU: 11655(Alas1) 11656(Alas2)
            RNO: 25748(Alas2) 65155(Alas1)
            CFA: 476600(ALAS1) 491498(ALAS2)
            GGA: 552895(ALAS1)
            XLA: 398824(MGC68700) 444480(MGC81838) 447323(MGC82115)
            XTR: 448773(alas2) 493434(MGC79710)
            DRE: 64607(alas2) 64608(alas1)
            SCE: YDR232W(HEM1)
            AGO: AGOS_ABL104C
            PIC: PICST_89623(HEM1)
            CGR: CAGL0B02607g
            SPO: SPAC2F3.09
            ANI: AN2284.2
            AFM: AFUA_5G06270
            AOR: AO090009000630
            CNE: CNB04260
            UMA: UM05059.1
            PFA: PFL2210w
            TET: TTHERM_01014670
            SPE: Spro_1830
            CVI: CV_0803
            RPR: RP841
            RTY: RT0829(hemA)
            RCO: RC1303(hemA)
            RFE: RF_1334(hemA)
            RBE: RBE_0631(hemA)
            RAK: A1C_06520
            RBO: A1I_04395
            RCM: A1E_05390
            RRI: A1G_07150
            OTS: OTBS_0349(hemA)
            WOL: WD1279(hemA)
            WBM: Wbm0133
            AMA: AM1202(hemA)
            APH: APH_1243(hemA)
            ERU: Erum0630(hemA)
            ERW: ERWE_CDS_00540(hemA)
            ERG: ERGA_CDS_00530(hemA)
            ECN: Ecaj_0056
            ECH: ECH_0092(hemA)
            NSE: NSE_0826(hemA)
            MLO: mll5695 mll6600(alaS)
            MES: Meso_0088
            PLA: Plav_2905
            SME: SMc03104(hemA)
            SMD: Smed_2880
            ATU: Atu2613(hemA)
            ATC: AGR_C_4738
            RET: RHE_PF00489(hemAf)
            RLE: pRL90008(hemA)
            BME: BMEI1604
            BMF: BAB1_0349
            BMS: BR0319(hemA)
            BMB: BruAb1_0345(hemA)
            BOV: BOV_0335(hemA)
            OAN: Oant_0412
            BJA: bll1200(hemA)
            BRA: BRADO1266(hemA) BRADO1651(hemA) BRADO3594(hemA)
                 BRADO6672(hemA)
            BBT: BBta_0861(hemA) BBta_4023(hemA) BBta_6405(hemA)
            RPA: RPA0854(hemO) RPA1554(hemA)
            RPB: RPB_3969 RPB_4563
            RPC: RPC_1325 RPC_4824
            RPD: RPD_0838 RPD_2301 RPD_3724
            RPE: RPE_1359 RPE_4787
            NWI: Nwi_0242
            NHA: Nham_0276
            XAU: Xaut_2126
            CCR: CC_1355
            SIL: SPO2596(hemA-1) SPOA0194(hemA-2)
            SIT: TM1040_0860
            RSP: RSP_2984(hemA) RSP_3028(hemT)
            RSH: Rsph17029_1630 Rsph17029_3755
            RSQ: Rsph17025_1863
            JAN: Jann_0149 Jann_1933
            RDE: RD1_0127(hemA) RD1_1576(hemA) RD1_2827(hemA) RD1_3778(hemA)
            PDE: Pden_1822
            MMR: Mmar10_1540
            HNE: HNE_2062(hemA)
            ZMO: ZMO1198(hemA)
            NAR: Saro_1797
            SAL: Sala_1206
            SWI: Swit_3823
            ELI: ELI_04785
            GOX: GOX1636
            GBE: GbCGDNIH1_0308
            ACR: Acry_0044
            RRU: Rru_A0798 Rru_A1146 Rru_A2508
            MAG: amb1683
            SAB: SAB1880c
STRUCTURES  PDB: 1H7D  1H7J  2BWN  2BWO  2BWP  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.37
            ExPASy - ENZYME nomenclature database: 2.3.1.37
            ExplorEnz - The Enzyme Database: 2.3.1.37
            ERGO genome analysis and discovery system: 2.3.1.37
            BRENDA, the Enzyme Database: 2.3.1.37
            CAS: 9037-14-3
///
ENTRY       EC 2.3.1.38                 Enzyme
NAME        [acyl-carrier-protein] S-acetyltransferase;
            acetyl coenzyme A-acyl-carrier-protein transacylase;
            [acyl-carrier-protein]acetyltransferase;
            [ACP]acetyltransferase;
            ACAT
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:[acyl-carrier-protein] S-acetyltransferase
REACTION    acetyl-CoA + [acyl-carrier-protein] = CoA +
            acetyl-[acyl-carrier-protein] [RN:R01624]
ALL_REAC    R01624
SUBSTRATE   acetyl-CoA [CPD:C00024];
            [acyl-carrier-protein]
PRODUCT     CoA [CPD:C00010];
            acetyl-[acyl-carrier-protein]
COMMENT     This enzyme, along with EC 2.3.1.39, [acyl-carrier-protein]
            S-malonyltransferase, is essential for the initiation of fatty-acid
            biosynthesis in bacteria. The substrate acetyl-CoA protects the
            enzyme against inhibition by N-ethylmaleimide or iodoacetamide [4].
            This is one of the activities associated with beta-ketoacyl-ACP
            synthase III (EC 2.3.1.180) [5].
REFERENCE   1  [PMID:4561013]
  AUTHORS   Prescott DJ, Vagelos PR.
  TITLE     Acyl carrier protein.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 36 (1972) 269-311.
REFERENCE   2  [PMID:4698221]
  AUTHORS   Vance DE, Mitsuhashi O, Bloch K.
  TITLE     Purification and properties of the fatty acid synthetase from
            Mycobacterium phlei.
  JOURNAL   J. Biol. Chem. 248 (1973) 2303-9.
  ORGANISM  Mycobacterium phlei
REFERENCE   3  [PMID:5330116]
  AUTHORS   Williamson IP, Wakil SJ.
  TITLE     Studies on the mechanism of fatty acid synthesis. XVII. Preparation
            and general properties of acetyl coenzyme A and malonyl coenzyme
            A-acyl carrier protein transacylases.
  JOURNAL   J. Biol. Chem. 241 (1966) 2326-32.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:3291856]
  AUTHORS   Lowe PN, Rhodes S.
  TITLE     Purification and characterization of [acyl-carrier-protein]
            acetyltransferase from Escherichia coli.
  JOURNAL   Biochem. J. 250 (1988) 789-96.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:1551888]
  AUTHORS   Tsay JT, Oh W, Larson TJ, Jackowski S, Rock CO.
  TITLE     Isolation and characterization of the beta-ketoacyl-acyl carrier
            protein synthase III gene (fabH) from Escherichia coli K-12.
  JOURNAL   J. Biol. Chem. 267 (1992) 6807-14.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:9115261]
  AUTHORS   Rangan VS, Smith S.
  TITLE     Alteration of the substrate specificity of the
            malonyl-CoA/acetyl-CoA:acyl carrier protein S-acyltransferase domain
            of the multifunctional fatty acid synthase by mutation of a single
            arginine residue.
  JOURNAL   J. Biol. Chem. 272 (1997) 11975-8.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00061  Fatty acid biosynthesis
ORTHOLOGY   KO: K00644  [acyl-carrier-protein] S-acetyltransferase
GENES       HSA: 2194(FASN)
            MMU: 14104(Fasn)
            RNO: 50671(Fasn)
            BTA: 281152(FASN)
            GGA: 396061(FASN)
            CEL: F32H2.5(fasn-1)
            SCE: YKL182W(FAS1)
            AGO: AGOS_AER085C
            CGR: CAGL0D00528g
            SPO: SPAC926.09c(fas1)
            CNE: CNE04370
            CKL: CKL_0103(acp1)
            CGB: cg0957(fas-IB) cg2743(fas-IA)
            AVA: Ava_1613
STRUCTURES  PDB: 2PFF  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.38
            ExPASy - ENZYME nomenclature database: 2.3.1.38
            ExplorEnz - The Enzyme Database: 2.3.1.38
            ERGO genome analysis and discovery system: 2.3.1.38
            BRENDA, the Enzyme Database: 2.3.1.38
            CAS: 37257-16-2
///
ENTRY       EC 2.3.1.39                 Enzyme
NAME        [acyl-carrier-protein] S-malonyltransferase;
            malonyl coenzyme A-acyl carrier protein transacylase;
            malonyl transacylase;
            malonyl transferase;
            malonyl-CoA-acyl carrier protein transacylase;
            [acyl carrier protein]malonyltransferase;
            MAT;
            FabD;
            malonyl-CoA:acyl carrier protein transacylase;
            malonyl-CoA:ACP transacylase;
            MCAT;
            malonyl-CoA:AcpM transacylase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     malonyl-CoA:[acyl-carrier-protein] S-malonyltransferase
REACTION    malonyl-CoA + [acyl-carrier-protein] = CoA +
            malonyl-[acyl-carrier-protein] [RN:R01626]
ALL_REAC    R01626
SUBSTRATE   malonyl-CoA [CPD:C00083];
            [acyl-carrier-protein]
PRODUCT     CoA [CPD:C00010];
            malonyl-[acyl-carrier-protein]
COMMENT     This enzyme, along with EC 2.3.1.38, [acyl-carrier-protein]
            S-acetyltransferase, is essential for the initiation of fatty-acid
            biosynthesis in bacteria. This enzyme also provides the malonyl
            groups for polyketide biosynthesis [7]. The product of the reaction,
            malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis.
            In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7,
            holo-[acyl-carrier-protein] synthase) is the preferred substrate
            [5].
REFERENCE   1
  AUTHORS   Alberts, A.W., Majerus, P.W. and Vagelos, P.R.
  TITLE     Acetyl-CoA acyl carrier protein transacylase.
  JOURNAL   Methods Enzymol. 14 (1969) 50-53.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4561013]
  AUTHORS   Prescott DJ, Vagelos PR.
  TITLE     Acyl carrier protein.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 36 (1972) 269-311.
REFERENCE   3  [PMID:5330116]
  AUTHORS   Williamson IP, Wakil SJ.
  TITLE     Studies on the mechanism of fatty acid synthesis. XVII. Preparation
            and general properties of acetyl coenzyme A and malonyl coenzyme
            A-acyl carrier protein transacylases.
  JOURNAL   J. Biol. Chem. 241 (1966) 2326-32.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:4934182]
  AUTHORS   Joshi VC, Wakil SJ.
  TITLE     Studies on the mechanism of fatty acid synthesis. XXVI. Purification
            and properties of malonyl-coenzyme A--acyl carrier protein
            transacylase of Escherichia coli.
  JOURNAL   Arch. Biochem. Biophys. 143 (1971) 493-505.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:11373295]
  AUTHORS   Kremer L, Nampoothiri KM, Lesjean S, Dover LG, Graham S, Betts J,
            Brennan PJ, Minnikin DE, Locht C, Besra GS.
  TITLE     Biochemical characterization of acyl carrier protein (AcpM) and
            malonyl-CoA:AcpM transacylase (mtFabD), two major components of
            Mycobacterium tuberculosis fatty acid synthase II.
  JOURNAL   J. Biol. Chem. 276 (2001) 27967-74.
  ORGANISM  Mycobacterium tuberculosis
REFERENCE   6  [PMID:12575934]
  AUTHORS   Keatinge-Clay AT, Shelat AA, Savage DF, Tsai SC, Miercke LJ,
            O'Connell JD 3rd, Khosla C, Stroud RM.
  TITLE     Catalysis, specificity, and ACP docking site of Streptomyces
            coelicolor malonyl-CoA:ACP transacylase.
  JOURNAL   Structure. 11 (2003) 147-54.
  ORGANISM  Streptomyces coelicolor [GN:sco]
REFERENCE   7  [PMID:11814333]
  AUTHORS   Szafranska AE, Hitchman TS, Cox RJ, Crosby J, Simpson TJ.
  TITLE     Kinetic and mechanistic analysis of the malonyl CoA:ACP transacylase
            from Streptomyces coelicolor indicates a single catalytically
            competent serine nucleophile at the active site.
  JOURNAL   Biochemistry. 41 (2002) 1421-7.
  ORGANISM  Streptomyces coelicolor [GN:sco]
PATHWAY     PATH: map00061  Fatty acid biosynthesis
ORTHOLOGY   KO: K00645  [acyl-carrier-protein] S-malonyltransferase
GENES       HSA: 2194(FASN) 27349(MCAT)
            PTR: 470233(MCAT)
            MMU: 14104(Fasn) 223722(Mcat)
            RNO: 50671(Fasn)
            CFA: 609532(MCAT)
            BTA: 281152(FASN)
            GGA: 396061(FASN) 427934(MCAT)
            XLA: 496310(LOC496310)
            XTR: 448008(mcat)
            SPU: 592878(LOC592878)
            DME: Dmel_CG3524(v(2)k05816) Dmel_CG7842
            CEL: C50D2.7 F32H2.5(fasn-1)
            ATH: AT2G30200
            OSA: 4332547
            CME: CMT420C
            SCE: YKL182W(FAS1)
            AGO: AGOS_AER085C
            PIC: PICST_65214(MCT1)
            CGR: CAGL0D00528g
            SPO: SPAC11G7.05c SPAC926.09c(fas1)
            AFM: AFUA_4G05850
            AOR: AO090672000003
            CNE: CNE04370
            DDI: DDBDRAFT_0201763
            PFA: PF13_0066
            TET: TTHERM_00885790
            ECO: b1092(fabD)
            ECJ: JW1078(fabD)
            ECE: Z1731(fabD)
            ECS: ECs1470
            ECC: c1361(fabD)
            ECI: UTI89_C1217(fabD) UTI89_C2217
            ECP: ECP_1084 ECP_1974
            ECV: APECO1_173(fabD)
            ECW: EcE24377A_1213(fabD)
            ECX: EcHS_A1214(fabD)
            STY: STY1233(fabD)
            STT: t1726(fabD)
            SPT: SPA1657(fabD)
            SEC: SC1142(fabD)
            STM: STM1194(fabD)
            YPE: YPO1463 YPO1598(fabD)
            YPK: y1757(fabD)
            YPM: YP_1355(fabD1) YP_2256(fabD2)
            YPA: YPA_0756 YPA_1927
            YPN: YPN_2031 YPN_2515
            YPP: YPDSF_1849
            YPS: YPTB2472(fabD)
            YPI: YpsIP31758_1577(fabD)
            YEN: YE1634(fabD)
            SFL: SF1096(fabD)
            SFX: S1176(fabD)
            SFV: SFV_1112(fabD)
            SSN: SSON_1112(fabD)
            SBO: SBO_1971(fabD)
            SDY: SDY_2058(fabD)
            ECA: ECA1796(fabD)
            PLU: plu2834(fabD)
            BAS: BUsg338(fabD)
            BAB: bbp320(fabD)
            BCC: BCc_216(fabD)
            WBR: WGLp090(fabD)
            SGL: SG1059
            BFL: Bfl405(fabD)
            BPN: BPEN_417(fabD)
            HIT: NTHI0245(fabD)
            HDU: HD0707(fabD)
            HSO: HS_0166(fabD)
            PMU: PM1915(fabD)
            MSU: MS1873(fabD)
            APL: APL_1993(fabD)
            XFA: XF0670
            XFT: PD1504(fabD)
            XCC: XCC1017(fabD) XCC3615(mdcH)
            XCB: XC_0578 XC_3228
            XCV: XCV0600(mdcH) XCV1145(fabD)
            XAC: XAC0566(mdcH) XAC1126(fabD)
            XOO: XOO0880(fabD)
            XOM: XOO_0805(XOO0805)
            VCH: VC2022
            VCO: VC0395_A1608(fabD)
            VVU: VV1_3010
            VVY: VV1274
            VPA: VP2055
            VFI: VF1741
            PPR: PBPRA1194
            PAE: PA0214 PA2968(fabD)
            PAU: PA14_02620(mdcH) PA14_25650(fabD)
            PAP: PSPA7_2193(fabD)
            PPU: PP_1913(fabD)
            PST: PSPTO_3833(fabD) PSPTO_5081
            PSB: Psyr_0448 Psyr_1646
            PSP: PSPPH_0439(mdcH) PSPPH_1640(fabD)
            PFL: PFL_1795(fabD) PFL_5814(fabD)
            PFO: Pfl_4158 Pfl_5296
            PEN: PSEEN1617(fabD)
            PMY: Pmen_1627
            PAR: Psyc_0520(fabD) Psyc_1140(mdcG)
            PCR: Pcryo_0515
            ACI: ACIAD0870(fabD) ACIAD1759(mdcH)
            SON: SO_2777(fabD)
            SDN: Sden_2294
            SFR: Sfri_1498
            SAZ: Sama_1981
            SBL: Sbal_1718
            SLO: Shew_1602
            SHE: Shewmr4_2397
            SHM: Shewmr7_2467
            SHN: Shewana3_2559
            SHW: Sputw3181_2441
            ILO: IL1341(fabD)
            CPS: CPS_2296(fabD)
            PHA: PSHAa1809(fabD)
            PAT: Patl_2123
            SDE: Sde_1628
            PIN: Ping_1088
            MAQ: Maqu_1868
            CBU: CBU_0494(fabD)
            CBD: COXBU7E912_1582(fabD)
            LPN: lpg1394
            LPF: lpl1345(fabD)
            LPP: lpp1349(fabD)
            MCA: MCA2002(fabD)
            FTU: FTT1374
            FTF: FTF1374
            FTW: FTW_0517(fabD)
            FTL: FTL_1140
            FTH: FTH_1115(fabD)
            FTA: FTA_1203(fabD)
            FTN: FTN_1338(fabD)
            TCX: Tcr_0711
            NOC: Noc_1666
            AEH: Mlg_1422
            HCH: HCH_02143(fabD)
            CSA: Csal_1600
            ABO: ABO_1068(fabD)
            AHA: AHA_2250(fabD)
            DNO: DNO_1208(fabD)
            BCI: BCI_0435(fabD)
            RMA: Rmag_0917
            VOK: COSY_0823(fabD)
            NME: NMB1918
            NMA: NMA0536(fabD)
            NMC: NMC0305(fabD)
            NGO: NGO2166
            CVI: CV_3415(fabD)
            RSO: RSc1051(fabD)
            REU: Reut_A2264 Reut_B4931
            REH: H16_A2568(fabD)
            RME: Rmet_2429
            BMA: BMA0531(fabD-1) BMA3031 BMAA1209 BMAA1458(fabD-2)
            BMV: BMASAVP1_0174 BMASAVP1_A2478(fabD)
            BML: BMA10299_0451 BMA10299_2155(fabD-2) BMA10299_A2803(fabD-1)
            BMN: BMA10247_1801(fabD-2) BMA10247_A0839(fabD-1) BMA10247_A1125
            BXE: Bxe_A1073 Bxe_B1850
            BUR: Bcep18194_A4234 Bcep18194_A4418
            BCN: Bcen_0794
            BCH: Bcen2424_1122 Bcen2424_1275
            BAM: Bamb_0998 Bamb_1153
            BPS: BPSL1335 BPSL2441(fabD) BPSS0300 BPSS1004
            BPM: BURPS1710b_1590 BURPS1710b_2906(fabD) BURPS1710b_A1850(fabD)
                 BURPS1710b_A2616(pedD)
            BPL: BURPS1106A_2852(fabD) BURPS1106A_A0428(fabD)
                 BURPS1106A_A1389(fabD)
            BPD: BURPS668_1458(fabD) BURPS668_2791(fabD) BURPS668_A0524(fabD)
                 BURPS668_A1475(fabD)
            BTE: BTH_I1718(fabD-1) BTH_I2797 BTH_II2098(fabD-2)
            BPE: BP2442(fabD)
            BPA: BPP3306(fabD)
            BBR: BB3757(fabD)
            RFR: Rfer_1731 Rfer_1849
            POL: Bpro_3648
            MPT: Mpe_A0637 Mpe_A0788
            HAR: HEAR1475(mdcH) HEAR2076(fabD)
            MMS: mma_0110 mma_1357(fabD)
            NEU: NE1647(fabD)
            NET: Neut_0469
            NMU: Nmul_A1073
            EBA: ebA5456(fabD)
            AZO: azo1624(fabD)
            DAR: Daro_2016 Daro_4014
            TBD: Tbd_1550
            MFA: Mfla_1506
            HPY: HP0090
            HPA: HPAG1_0091
            HHE: HH1282(fabD)
            HAC: Hac_1515(fabD)
            WSU: WS0527(fabD)
            TDN: Tmden_1393
            CJE: Cj0116(fabD)
            CJR: CJE0111(fabD)
            CJJ: CJJ81176_0151(fabD)
            CJU: C8J_0109(fabD)
            CJD: JJD26997_0123(fabD)
            CFF: CFF8240_1516(fabD)
            CCV: CCV52592_1747(fabD)
            CHA: CHAB381_0697(fabD)
            CCO: CCC13826_0926(fabD)
            ABU: Abu_1586(fabD)
            NIS: NIS_1211(fabD)
            SUN: SUN_1756(fabD)
            GSU: GSU1602(fabD)
            GME: Gmet_1600
            PCA: Pcar_1437
            DVU: DVU1249(fabD)
            DDE: Dde_2294
            LIP: LI0227(fabD)
            BBA: Bd2013(fabD) Bd3096(fabD)
            DPS: DP2550
            ADE: Adeh_2749
            MXA: MXAN_3942(fabD) MXAN_4771(fabD)
            SAT: SYN_01700
            RPR: RP735
            RTY: RT0720(fabD)
            RCO: RC1116(fabD)
            RFE: RF_0171(fabD)
            RBE: RBE_0671(fabD)
            WOL: WD0869(fabD)
            WBM: Wbm0402(fabD)
            AMA: AM110(fabD)
            APH: APH_0092(fabD)
            ERU: Erum7470(fabD)
            ERW: ERWE_CDS_07870(fabD)
            ERG: ERGA_CDS_07780(fabD)
            ECN: Ecaj_0781
            ECH: ECH_0227(fabD)
            NSE: NSE_0960(fabD)
            PUB: SAR11_0706(fabD)
            MLO: mlr7849
            MES: Meso_1769
            SME: SMc00571(fabD)
            ATU: Atu1094(fabD)
            ATC: AGR_C_2025
            RET: RHE_CH01442(fabD)
            RLE: RL1557(fabD)
            BME: BMEI1478
            BMF: BAB1_0482(fabD)
            BMS: BR0457(fabD)
            BMB: BruAb1_0479(fabD)
            BOV: BOV_0462(fabD)
            BJA: bll0263 bll1271(mdcH) blr4082(fabD)
            BRA: BRADO3310(fabD)
            BBT: BBta_3817(fabD)
            RPA: RPA3075(fabD)
            RPB: RPB_2466
            RPC: RPC_2298 RPC_4587
            RPD: RPD_2983
            RPE: RPE_3307
            NWI: Nwi_1690
            NHA: Nham_2354
            BHE: BH05340(fabD)
            BQU: BQ04520(fabD)
            BBK: BARBAKC583_0496(fabD)
            CCR: CC_1674
            SIL: SPO2276(fabD)
            SIT: TM1040_1050
            RSP: RSP_2682(fabD)
            JAN: Jann_1624
            RDE: RD1_2925(fabD) RD1_3040(fabD)
            MMR: Mmar10_1213
            HNE: HNE_2160(fabD)
            ZMO: ZMO1223(fabD)
            NAR: Saro_1427
            SAL: Sala_1897
            ELI: ELI_07340
            GOX: GOX2039
            GBE: GbCGDNIH1_2212
            RRU: Rru_A0415
            MAG: amb2105
            MGM: Mmc1_1875
            BSU: BG11836(fabD)
            BHA: BH2492(fabD)
            BAN: BA3990(fabD)
            BAR: GBAA3990(fabD)
            BAA: BA_4461
            BAT: BAS3703
            BCE: BC3850
            BCA: BCE_3894(fabD)
            BCZ: BCZK3611(fabD)
            BTK: BT9727_3593(fabD)
            BLI: BL02314(fabD)
            BLD: BLi01811(fabD)
            BCL: ABC2302(fabD)
            BAY: RBAM_015730(fabD) RBAM_016910(baeC) RBAM_016920(baeD)
                 RBAM_016930(baeE) RBAM_018190(bmyD)
            BPU: BPUM_1489(fabD)
            OIH: OB1523(fabD)
            GKA: GK1189
            SAU: SA1073(fabD)
            SAV: SAV1230(fabD)
            SAM: MW1113(fabD)
            SAR: SAR1206(fabD)
            SAS: SAS1164
            SAC: SACOL1244(fabD)
            SAB: SAB1094(fabD)
            SAA: SAUSA300_1123(fabD)
            SAO: SAOUHSC_01198
            SEP: SE0905
            SER: SERP0796(fabD)
            SHA: SH1684(fabD)
            SSP: SSP1539
            LMO: lmo1808(fabD)
            LMF: LMOf2365_1836(fabD)
            LIN: lin1922(fabD)
            LWE: lwe1827(fabD)
            LLA: L0184(fabD)
            LLC: LACR_0823
            LLM: llmg_1785(fabD)
            SPY: SPy_1750(fabD)
            SPZ: M5005_Spy_1491(fabD)
            SPM: spyM18_1822
            SPG: SpyM3_1524(fabD)
            SPS: SPs0342
            SPH: MGAS10270_Spy1559(fabD)
            SPI: MGAS10750_Spy1550(fabD)
            SPJ: MGAS2096_Spy1519(fabD)
            SPK: MGAS9429_Spy1493(fabD)
            SPF: SpyM50354(fabD)
            SPA: M6_Spy1485
            SPB: M28_Spy1480(fabD)
            SPN: SP_0420
            SPR: spr0380(fabD)
            SPD: SPD_0383(fabD)
            SAG: SAG0347(fabD)
            SAN: gbs0334
            SAK: SAK_0421(fabD)
            SMU: SMU.1741(fabD)
            STC: str0386(fabD)
            STL: stu0386(fabD)
            SSA: SSA_1937(fabD)
            SGO: SGO_1694(fabD)
            LPL: lp_1673(fabD)
            LSA: LSA0815(fabD)
            LSL: LSL_0453(fabD)
            LDB: Ldb0902(fabD)
            LBU: LBUL_0820
            LBR: LVIS_0933
            LCA: LSEI_2116
            EFA: EF2882(fabD)
            OOE: OEOE_1590
            STH: STH1450
            CAC: CAC3575(fabD)
            CPE: CPE1069(fabD)
            CPF: CPF_1325(fabD)
            CPR: CPR_1137(fabD)
            CTC: CTC00129
            CNO: NT01CX_0924(fabD)
            CDF: CD1181(fabD)
            CBO: CBO3601(fabD)
            CBA: CLB_3681(fabD)
            CBH: CLC_3579(fabD)
            CBF: CLI_3826(fabD)
            CKL: CKL_0105(fabD)
            CHY: CHY_1448(fabD)
            DSY: DSY2661
            SWO: Swol_1851
            TTE: TTE1473(fabD)
            MTA: Moth_0947
            MTU: Rv0649(fabD2) Rv2243(fabD)
            MTC: MT2303(fabD)
            MBO: Mb0668(fabD2) Mb2267(fabD)
            MBB: BCG_0698(fabD2) BCG_2260(fabD)
            MLE: ML1653(fabD)
            MPA: MAP1996(fabD)
            MAV: MAV_2194
            MSM: MSMEG_4325
            MMC: Mmcs_3364
            MKM: Mkms_3426
            MJL: Mjls_3375
            CGB: cg0957(fas-IB) cg2743(fas-IA)
            NFA: nfa16150(fabD)
            RHA: RHA1_ro01199(fabD)
            SCO: SCO2387(fabD)
            SMA: SAV5788(fabD)
            TWH: TWT254(fabD)
            TWS: TW516(fabD)
            LXX: Lxx12720(fabD)
            CMI: CMM_1619(fabD)
            PAC: PPA0984
            NCA: Noca_1990
            TFU: Tfu_1973
            FRA: Francci3_3481
            FAL: FRAAL5668
            ACE: Acel_0878
            SEN: SACE_1526(fabD)
            RXY: Rxyl_1379
            FNU: FN0149
            RBA: RB314(fabD)
            CTR: CT238(fabD)
            CTA: CTA_0260(fabD)
            CMU: TC0509
            CPN: CPn0297(fabD)
            CPA: CP0461
            CPJ: CPj0297(fabD)
            CPT: CpB0306(fabD)
            CCA: CCA00485(fabD)
            CAB: CAB471(fabD)
            CFE: CF0522(fabD)
            PCU: pc1719(fabD)
            TDE: TDE0601
            SYN: slr2023(fabD)
            SYW: SYNW2249(fabD)
            SYC: syc0101_c
            SYF: Synpcc7942_1456
            SYD: Syncc9605_2387
            SYE: Syncc9902_0305
            SYG: sync_2600(fabD)
            SYR: SynRCC307_0247(fabD)
            SYX: SynWH7803_2251(fabD)
            CYA: CYA_2365(fabD)
            CYB: CYB_2339(fabD)
            TEL: tlr0041(fabD)
            GVI: gll2145
            ANA: alr0240
            AVA: Ava_2730
            PMA: Pro0159(fabD)
            PMM: PMM0137(fabD)
            PMT: PMT1997(fabD)
            PMN: PMN2A_1503
            PMI: PMT9312_0139
            PMB: A9601_01541(fabD)
            PMC: P9515_01651(fabD)
            PMF: P9303_26561(fabD)
            PMG: P9301_01561(fabD)
            PMH: P9215_01541(fabD)
            PME: NATL1_02091(fabD)
            BTH: BT_0789
            BFR: BF2258
            BFS: BF2352(fabD)
            PGI: PG0138(fabD)
            SRU: SRU_0043(fabD)
            CHU: CHU_2469(fabD)
            GFO: GFO_0276(fabD)
            FPS: FP0408(fabD)
            CTE: CT2115(fabD)
            CCH: Cag_1663
            PLT: Plut_0132
            DET: DET1276(fabD)
            DEH: cbdb_A1204(fabD)
            DRA: DR_1945
            DGE: Dgeo_0434
            TTH: TTC0048
            TTJ: TTHA0416
            AAE: aq_892(fabD)
            TMA: TM0798
STRUCTURES  PDB: 1NM2  2CUY  2G1H  2G2O  2G2Y  2G2Z  2H1Y  2PFF  2QC3  2QJ3  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.39
            ExPASy - ENZYME nomenclature database: 2.3.1.39
            ExplorEnz - The Enzyme Database: 2.3.1.39
            ERGO genome analysis and discovery system: 2.3.1.39
            BRENDA, the Enzyme Database: 2.3.1.39
            CAS: 37257-17-3
///
ENTRY       EC 2.3.1.40                 Enzyme
NAME        acyl-[acyl-carrier-protein]---phospholipid O-acyltransferase;
            acyl-[acyl-carrier
            protein]:O-(2-acyl-sn-glycero-3-phospho)-ethanolamine
            O-acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-[acyl-carrier
            protein]:O-(2-acyl-sn-glycero-3-phospho)ethanolamine
            O-acyltransferase
REACTION    acyl-[acyl-carrier protein] +
            O-(2-acyl-sn-glycero-3-phospho)ethanolamine = [acyl-carrier protein]
            + O-(1,2-diacyl-sn-glycero-3-phospho)ethanolamine [RN:R04864]
ALL_REAC    R04864
SUBSTRATE   acyl-[acyl-carrier protein] [CPD:C00173];
            O-(2-acyl-sn-glycero-3-phospho)ethanolamine
PRODUCT     [acyl-carrier protein] [CPD:C00229];
            O-(1,2-diacyl-sn-glycero-3-phospho)ethanolamine
REFERENCE   1  [PMID:4902888]
  AUTHORS   Taylor SS, Heath EC.
  TITLE     The incorporation of beta-hydroxy fatty acids into a phospholipid of
            Escherichia coli B.
  JOURNAL   J. Biol. Chem. 244 (1969) 6605-16.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K05939  acyl-[acyl-carrier-protein]-phospholipid
                        O-acyltransferase
GENES       ECO: b2836(aas)
            ECJ: JW2804(aas)
            ECE: Z4154(aas)
            ECS: ECs3693
            ECC: c3431(aas)
            ECI: UTI89_C3240(aas)
            ECP: ECP_2849
            ECV: APECO1_3670(aas)
            ECW: EcE24377A_3156(aas)
            ECX: EcHS_A2983
            STY: STY3153(aas)
            STT: t2919(aas)
            SPT: SPA2875(aas)
            SEC: SC2949(aas)
            STM: STM3010(aas)
            YPE: YPO0793(aas)
            YPK: y3181(aas)
            YPM: YP_2864(aas)
            YPA: YPA_0476
            YPN: YPN_2996 YPN_2997
            YPS: YPTB3042(aas)
            YPI: YpsIP31758_0975(aas)
            SFL: SF2846(aas)
            SFX: S3044(aas)
            SFV: SFV_2914(aas)
            SSN: SSON_2996(aas)
            SBO: SBO_2728(aas)
            SDY: SDY_3053(aas)
            ECA: ECA3641(aas)
            PLU: plu1246(aas)
            LPN: lpg0597(aas)
            LPF: lpl0631
            LPP: lpp0647
            DAR: Daro_0402
            HHE: HH0306
            CJE: Cj0938c(aas)
            CJR: CJE1016(aas)
            CJU: C8J_0881(aas)
            SUN: SUN_1164
            GSU: GSU3029
            GME: Gmet_0086
            PCA: Pcar_2776
            RPR: RP620(aas)
            RTY: RT0611(aas)
            RCO: RC0962(aas)
            RFE: RF_0417(aas)
            MLO: mlr5451
            BJA: bll2324
            BRA: BRADO5289
            BBT: BBta_5738
            MMR: Mmar10_1427
            HNE: HNE_2022(aas)
            GBE: GbCGDNIH1_2359
            MAG: amb2972
            RBA: RB6533(aas)
            PCU: pc1236(aas)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.40
            ExPASy - ENZYME nomenclature database: 2.3.1.40
            ExplorEnz - The Enzyme Database: 2.3.1.40
            ERGO genome analysis and discovery system: 2.3.1.40
            BRENDA, the Enzyme Database: 2.3.1.40
            CAS: 37257-18-4
///
ENTRY       EC 2.3.1.41                 Enzyme
NAME        beta-ketoacyl-acyl-carrier-protein synthase I;
            beta-ketoacyl-ACP synthase I;
            beta-ketoacyl synthetase;
            beta-ketoacyl-ACP synthetase;
            beta-ketoacyl-acyl carrier protein synthetase;
            beta-ketoacyl-[acyl carrier protein] synthase;
            beta-ketoacylsynthase;
            condensing enzyme;
            3-ketoacyl-acyl carrier protein synthase;
            fatty acid condensing enzyme;
            acyl-malonyl(acyl-carrier-protein)-condensing enzyme;
            acyl-malonyl acyl carrier protein-condensing enzyme;
            beta-ketoacyl acyl carrier protein synthase;
            3-oxoacyl-[acyl-carrier-protein] synthase;
            3-oxoacyl:ACP synthase I;
            KASI;
            KAS I;
            FabF1;
            FabB
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-[acyl-carrier-protein]:malonyl-[acyl-carrier-protein]
            C-acyltransferase (decarboxylating)
REACTION    an acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = a
            3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]
            [RN:R02768]
ALL_REAC    R02768 > R04355 R04726 R04952 R04957 R04960 R04963 R04968;
            (other) R01624
SUBSTRATE   acyl-[acyl-carrier-protein];
            malonyl-[acyl-carrier-protein]
PRODUCT     3-oxoacyl-[acyl-carrier-protein];
            CO2 [CPD:C00011];
            [acyl-carrier-protein]
COMMENT     This enzyme is responsible for the chain-elongation step of
            dissociated (type II) fatty-acid biosynthesis, i.e. the addition of
            two C atoms to the fatty-acid chain. Escherichia coli mutants that
            lack this enzyme are deficient in unsaturated fatty acids. The
            enzyme can use fatty acyl thioesters of ACP (C2 to C16) as
            substrates, as well as fatty acyl thioesters of Co-A (C4 to C16)
            [4]. The substrate specificity is very similar to that of EC
            2.3.1.179, beta-ketoacyl-ACP synthase II, with the exception that
            the latter enzyme is far more active with palmitoleoyl-ACP
            (C16Delta9) as substrate, allowing the organism to regulate its
            fatty-acid composition with changes in temperature [4,5].
REFERENCE   1
  AUTHORS   Alberts, A.W., Majerus, P.W. and Vagelos, P.R.
  TITLE     Acetyl-CoA acyl carrier protein transacylase.
  JOURNAL   Methods Enzymol. 14 (1969) 50-53.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4561013]
  AUTHORS   Prescott DJ, Vagelos PR.
  TITLE     Acyl carrier protein.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 36 (1972) 269-311.
REFERENCE   3  [PMID:5327099]
  AUTHORS   Toomey RE, Wakil SJ.
  TITLE     Studies on the mechanism of fatty acid synthesis. XVI. Preparation
            and general properties of acyl-malonyl acyl carrier
            protein-condensing enzyme from Escherichia coli.
  JOURNAL   J. Biol. Chem. 241 (1966) 1159-65.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:237914]
  AUTHORS   D'Agnolo G, Rosenfeld IS, Vagelos PR.
  TITLE     Multiple forms of beta-ketoacyl-acyl carrier protein synthetase in
            Escherichia coli.
  JOURNAL   J. Biol. Chem. 250 (1975) 5289-94.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:7002930]
  AUTHORS   Garwin JL, Klages AL, Cronan JE Jr.
  TITLE     Structural, enzymatic, and genetic studies of beta-ketoacyl-acyl
            carrier protein synthases I and II of Escherichia coli.
  JOURNAL   J. Biol. Chem. 255 (1980) 11949-56.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:15194690]
  AUTHORS   Wang H, Cronan JE.
  TITLE     Functional replacement of the FabA and FabB proteins of Escherichia
            coli fatty acid synthesis by Enterococcus faecalis FabZ and FabF
            homologues.
  JOURNAL   J. Biol. Chem. 279 (2004) 34489-95.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   7
  AUTHORS   Cronan, J.E., Jr. and Rock, C.O.
  TITLE     Biosynthesis of membrane lipids.
  JOURNAL   In: Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular
            and Molecular Biology, 2nd ed., vol. 1, ASM Press, Washington, DC,
            1996, p. 612-636.
PATHWAY     PATH: map00061  Fatty acid biosynthesis
ORTHOLOGY   KO: K00646  3-oxoacyl-[acyl-carrier-protein] synthase
            KO: K00647  3-oxoacyl-[acyl-carrier-protein] synthase I
GENES       HSA: 2194(FASN)
            MMU: 14104(Fasn)
            RNO: 50671(Fasn)
            BTA: 281152(FASN)
            GGA: 396061(FASN)
            CEL: F32H2.5(fasn-1)
            ATH: AT2G04540
            OSA: 4328619 4340392 4343906
            CME: CML329C
            SCE: YER061C(CEM1) YPL231W(FAS2)
            AGO: AGOS_ADL072C AGOS_AFL138W
            PIC: PICST_64208(CEM1)
            CAL: CaO19_5977(CaO19.5977)
            CGR: CAGL0E06138g CAGL0J02970g
            SPO: SPAC4A8.11c(lsd1)
            AFM: AFUA_3G02530
            CNE: CNE04360
            PFA: PFB0505c
            TET: TTHERM_00192050
            TBR: Tb927.2.3910
            TCR: 504157.20
            ECO: b2323(fabB)
            ECJ: JW2320(fabB)
            ECE: Z3586(fabB)
            ECS: ECs3207
            ECC: c2869(fabB)
            ECI: UTI89_C2608(fabB)
            ECP: ECP_2362
            ECV: APECO1_4241(fabB)
            ECW: EcE24377A_1212(fabH) EcE24377A_1216(fabF)
                 EcE24377A_2618(fabB)
            ECX: EcHS_A1213(fabH) EcHS_A1217(fabF) EcHS_A2474(fabB)
            STY: STY2609(fabB)
            STT: t0486(fabB)
            SPT: SPA0486(fabB)
            SEC: SC2380(fabB)
            STM: STM2378(fabB)
            YPE: YPO1455 YPO2757(fabB)
            YPK: y1591(fabB) y2714(fabF)
            YPM: YP_1347(fabF3) YP_2406(fabB)
            YPA: YPA_0748 YPA_2086
            YPN: YPN_2189 YPN_2523
            YPP: YPDSF_1850 YPDSF_2003
            YPS: YPTB1473 YPTB2626(fabB)
            YPI: YpsIP31758_1411(fabB) YpsIP31758_1576(fabH)
                 YpsIP31758_1580(fabF)
            YEN: YE0911(fabF) YE1287(fabB)
            SFL: SF2399(fabB)
            SFX: S2534(fabB)
            SFV: SFV_2392(fabB)
            SSN: SSON_2381(fabB)
            SBO: SBO_2360(fabB)
            SDY: SDY_2522(fabB)
            ECA: ECA3063(fabB)
            PLU: plu3184(fabB)
            BUC: BU092(fabB)
            BAS: BUsg084(fabB)
            BAB: bbp086(fabB)
            BCC: BCc_056(fabB)
            WBR: WGLp408(fabB)
            SGL: SG1623
            ENT: Ent638_1606 Ent638_2871
            KPN: KPN_02713(fabB)
            SPE: Spro_1904 Spro_2869
            BFL: Bfl498(fabB)
            BPN: BPEN_514(fabB)
            HIN: HI1533(fabB)
            HIT: NTHI1600(fabB)
            HIP: CGSHiEE_02505 CGSHiEE_05245
            HIQ: CGSHiGG_00290
            HDU: HD0612(fabB)
            HSO: HS_0105(fabF) HS_0665(fabB)
            PMU: PM0339(fabB)
            MSU: MS1591(fabB)
            APL: APL_1055(fabB) APL_1384(fabH)
            ASU: Asuc_2003
            XFA: XF1639
            XFT: PD1142(fabB)
            XCC: XCC0581(fabB) XCC3998(fabF)
            XCB: XC_3652 XC_4087
            XCV: XCV3742(fabB) XCV4172(fabF)
            XAC: XAC3625(fabB) XAC4086(fabF)
            XOO: XOO0463(fabF) XOO0761(fabB)
            XOM: XOO_0427(XOO0427) XOO_0691(XOO0691)
            VCO: VC0395_0689(fabH-2) VC0395_A1605(fabF) VC0395_A1609(fabH-1)
                 VC0395_A1693(fabB)
            VVU: VV1_1986 VV1_3006 VV1_3007
            VVY: VV2429
            VPA: VP2194
            VFI: VF0857 VF1700
            PPR: PBPRA2658(fabB)
            PAE: PA1609(fabB)
            PAU: PA14_43690(fabB)
            PAP: PSPA7_2196(fabF) PSPA7_4011 PSPA7_4286
            PPU: PP_4175(fabB)
            PPF: Pput_1345 Pput_1488
            PST: PSPTO_2210(fabB)
            PSB: Psyr_2019
            PSP: PSPPH_0415 PSPPH_1989(fabB)
            PFL: PFL_0464(fabF-2) PFL_1736
            PFO: Pfl_4039 Pfl_4213
            PEN: PSEEN0348 PSEEN3623(fabB)
            PMY: Pmen_1545 Pmen_2470
            PSA: PST_1892(fabB)
            PAR: Psyc_1899(fabB)
            PCR: Pcryo_2189
            PRW: PsycPRwf_1458
            ACI: ACIAD0580 ACIAD0879(fabB)
            ACB: A1S_0080
            SON: SO_3072(fabB)
            SDN: Sden_1482 Sden_3119 Sden_3120
            SFR: Sfri_1391
            SAZ: Sama_1510 Sama_1527 Sama_2154
            SBL: Sbal_2634 Sbal_2746
            SBM: Shew185_1714 Shew185_2669 Shew185_2683
            SLO: Shew_1333 Shew_1334 Shew_2366 Shew_2410
            SPC: Sputcn32_1580 Sputcn32_2355 Sputcn32_2368 Sputcn32_2445
            SSE: Ssed_1758 Ssed_2626
            SPL: Spea_1700 Spea_2496
            SHE: Shewmr4_1422
            SHM: Shewmr7_1487
            SHN: Shewana3_1475
            SHW: Sputw3181_1563 Sputw3181_1641 Sputw3181_1654
            ILO: IL1021(fabB)
            CPS: CPS_3807(fabB)
            PHA: PSHAa1382 PSHAa2080(fabB)
            PAT: Patl_3383
            SDE: Sde_0998
            PIN: Ping_1995
            MAQ: Maqu_1591 Maqu_3148
            CBU: CBU_0035
            CBD: COXBU7E912_1579(fabF) COXBU7E912_1583(fabH)
            LPN: lpg0102(fabF) lpg0361(fabF) lpg0362(fabF)
            LPF: lpl0102(fabF) lpl0402 lpl0403
            LPP: lpp0116(fabF) lpp0426 lpp0427
            MCA: MCA2879(fabB)
            FTA: FTA_1200 FTA_1204
            TCX: Tcr_1945
            NOC: Noc_1777
            AEH: Mlg_1373
            HHA: Hhal_0018
            HCH: HCH_06402
            CSA: Csal_0456
            ABO: ABO_0647(fabB) ABO_0834(fabB)
            MMW: Mmwyl1_2158
            AHA: AHA_1920(fabB)
            DNO: DNO_0315(fabB) DNO_1211(fabF)
            BCI: BCI_0362(fabB)
            RMA: Rmag_1004
            VOK: COSY_0446(fabH) COSY_0521(fabF) COSY_0900(fabB)
            NMC: NMC0216(fabF) NMC1617(fabF2)
            NGO: NGO1352
            CVI: CV_3948 CV_3949
            RSO: RS00773(RSp0361) RSc0427(RS03396) RSp0357(fabB)
            REH: H16_B1667(fabB)
            BMV: BMASAVP1_A2475(fabF) BMASAVP1_A3453
            BML: BMA10299_A2806(fabF)
            BMN: BMA10247_1798(fabF) BMA10247_3095(fabH-1) BMA10247_3097
            BXE: Bxe_A0096 Bxe_A0098 Bxe_A0937 Bxe_A0941
            BVI: Bcep1808_1040
            BUR: Bcep18194_A4991 Bcep18194_A6096 Bcep18194_C6697
            BAM: Bamb_3612 Bamb_5765 Bamb_5766
            BPM: BURPS1710b_A2609(pksF)
            BPL: BURPS1106A_2849(fabF) BURPS1106A_3957 BURPS1106A_3959(fabH)
            BPD: BURPS668_2788(fabF) BURPS668_3875 BURPS668_3877(fabH)
            RFR: Rfer_3984
            AAV: Aave_4180
            AJS: Ajs_0526
            VEI: Veis_2160
            MPT: Mpe_A0640
            HAR: HEAR2073(fabF) HEAR2876
            MMS: mma_0919(fabF1) mma_1020(fabF2) mma_1356(fabH)
                 mma_1360(fabF3)
            AZO: azo0292(darB) azo1627(fabF1) azo3911(fabF2)
            MFA: Mfla_1893 Mfla_2642
            WSU: WS0629(fabB)
            CJJ: CJJ81176_0350(fabH) CJJ81176_0469(fabF)
            CJU: C8J_0305(fabH) C8J_0417(fabF)
            CJD: JJD26997_1495(fabF) JJD26997_1630(fabH)
            CFF: CFF8240_0237
            CCV: CCV52592_1699
            CHA: CHAB381_0229(fabF) CHAB381_1492
            CCO: CCC13826_0560(fabF) CCC13826_1208
            ABU: Abu_0295(fabH) Abu_2056(fabF)
            NIS: NIS_0315(fabF) NIS_0399(fabH)
            SUN: SUN_2048(fabH) SUN_2165
            GSU: GSU0459
            GUR: Gura_0135 Gura_1875
            PCA: Pcar_2650 Pcar_2664 Pcar_2666
            DVU: DVU2563
            DVL: Dvul_1850
            DDE: Dde_2660
            DPS: DP1840 DP1849 DP2403
            AFW: Anae109_0005 Anae109_2739
            MXA: MXAN_6400(fabF)
            SAT: SYN_01694 SYN_02566
            SFU: Sfum_2631
            RAK: A1C_05945 A1C_06015
            RBO: A1I_07280 A1I_07360
            RCM: A1E_04915 A1E_04950
            RRI: A1G_06510 A1G_06570
            OTS: OTBS_0383(fabF)
            AMA: AM338(fabB)
            PUB: SAR11_0396(fabB)
            MLO: mll5566 mlr1177
            MES: Meso_1318 Meso_3938
            PLA: Plav_0744 Plav_2923
            SME: SMc00327(fabB) SMc04273
            SMD: Smed_0829
            ATU: Atu0150(fabB) Atu1596(fabF)
            ATC: AGR_C_244 AGR_C_2934
            RET: RHE_CH00108(fabB) RHE_CH02475
            RLE: RL0117(fabB) RL2814(fabF1)
            BME: BMEI1113 BMEI1957
            BMF: BAB1_0872 BAB1_2173(fabB)
            BMS: BR0853 BR2172(fabB)
            BMB: BruAb1_0865 BruAb1_2145(fabB)
            BOV: BOV_0465(fabF) BOV_0769(fabH) BOV_2084(fabB)
            OAN: Oant_2519 Oant_2819
            BJA: bll3808 blr0770(fabB)
            BRA: BRADO0062(fabB) BRADO3314(fabF) BRADO4417(fabH) BRADO4677
                 BRADO4678(fabF)
            BBT: BBta_0068(fabB) BBta_3519(fabF) BBta_3520 BBta_3820(fabF)
                 BBta_4631(fabH)
            RPA: RPA0426(fabB) RPA2019
            RPB: RPB_0612 RPB_3356
            RPC: RPC_0348 RPC_2108
            RPD: RPD_0221 RPD_2087
            RPE: RPE_0256 RPE_2020
            NWI: Nwi_0033 Nwi_1243
            NHA: Nham_0041 Nham_1503
            BHE: BH01280(fabB) BH07440(fabF2)
            BQU: BQ01210(fabB) BQ05290(fabF2)
            BBK: BARBAKC583_0499(fabF) BARBAKC583_0638(fabH) BARBAKC583_1269
            XAU: Xaut_2921 Xaut_4385
            CCR: CC_3719
            SIL: SPOA0440(fabB)
            SIT: TM1040_0181 TM1040_0628
            RSP: RSP_3177(fabB)
            RSH: Rsph17029_1270 Rsph17029_3914
            RSQ: Rsph17025_1912 Rsph17025_3935
            JAN: Jann_1656
            RDE: RD1_2623 RD1_3924(fabB)
            PDE: Pden_0669 Pden_1650 Pden_1861
            MMR: Mmar10_0799 Mmar10_3059
            SWI: Swit_3556
            ELI: ELI_06740
            GOX: GOX1396
            GBE: GbCGDNIH1_0031
            ACR: Acry_0269
            RRU: Rru_A0045
            SUS: Acid_7389
            BHA: BH1840(fabF)
            BCZ: pE33L466_0418(fabH)
            BCY: Bcer98_0890 Bcer98_1823 Bcer98_2187
            BAY: RBAM_010400(fabHB) RBAM_011330(fabHA) RBAM_011340(fabF)
            BPU: BPUM_1058(fabF)
            LLM: llmg_1783(fabF) llmg_1787(fabH)
            SPF: SpyM50351(fabH) SpyM50356(fabF)
            SSA: SSA_1935(fabF) SSA_1940(fabH) SSA_2346
            SGO: SGO_1692 SGO_1698
            LSA: LSA0817(fabF)
            LRE: Lreu_0991
            EFA: EF2880(fabF-2)
            CAC: CAC2008(pksF) CA_P0088(abf)
            CTH: Cthe_0130 Cthe_0132 Cthe_0936
            CDF: CD1179(fabH) CD1184(fabF)
            CBO: CBO0718 CBO3599(fabF) CBO3604(fabH)
            CBA: CLB_3679(fabF) CLB_3684(fabH)
            CBH: CLC_3577(fabF) CLC_3582(fabH)
            CBF: CLI_3824(fabF) CLI_3829(fabH)
            CBE: Cbei_1068 Cbei_4032
            CKL: CKL_0102(fabH1) CKL_0107(fabF) CKL_3513(fabH2)
            AMT: Amet_2758
            DRM: Dred_2075
            CSC: Csac_1603
            TTE: TTE1470(fabB)
            MTU: Rv2245(kasA) Rv2246(kasB) Rv2947c(pks15)
            MTC: MT2305(fabF-1) MT2306(fabF-2) MT3021.1
            MBO: Mb2269(kasA) Mb2270(kasB)
            MBB: BCG_0577c(fabH) BCG_2262(kasA) BCG_2263(kasB)
            MLE: ML1655(kasA) ML1656(kasB)
            MPA: MAP1998(kasA) MAP1999(kasB_1)
            MAV: MAV_2191 MAV_2192 MAV_4343
            MSM: MSMEG_1204 MSMEG_4327 MSMEG_4328
            MGI: Mflv_2540
            MMC: Mmcs_3366 Mmcs_3367
            MKM: Mkms_3477
            MJL: Mjls_3425
            CGB: cg0957(fas-IB) cg2743(fas-IA)
            NFA: nfa16170(kasA)
            RHA: RHA1_ro01201(fabF) RHA1_ro01257
            SCO: SCO0548(fabB2) SCO1266(2SCG18.13c) SCO3248(fabF3)
            SMA: SAV2944(fabB2) SAV5785(fabB1)
            CMI: CMM_0681(fabB) CMM_1616(fabF) CMM_1618(fabH) CMM_2155
            AAU: AAur_2336 AAur_2436(fabH) AAur_2438
            PAC: PPA0980
            NCA: Noca_1989
            TFU: Tfu_1976
            FRA: Francci3_1934 Francci3_2596
            FAL: FRAAL1288 FRAAL2990 FRAAL3652(fabF) FRAAL4387 FRAAL4649
                 FRAAL5671(fab)
            ACE: Acel_0875
            KRA: Krad_3344
            SEN: SACE_0606(fabF) SACE_1523(fabF) SACE_1525 SACE_4133
                 SACE_4575(pksF) SACE_5538(fabF) SACE_5540
            STP: Strop_2499 Strop_3379
            RBA: RB1586(fabF) RB3714(fabB) RB4527 RB7171(fabF)
            LIL: LA1430
            LIC: LIC12317(sch1)
            SYN: slr1332(fabF)
            SYW: SYNW0401(fabB)
            SYD: Syncc9605_2213
            SYE: Syncc9902_0465
            SYR: SynRCC307_0131(fabF) SynRCC307_0194(fabF)
                 SynRCC307_0248(fabH)
            SYX: SynWH7803_0196(fabF) SynWH7803_2250(fabH)
            TEL: tlr0622
            GVI: gll1091 gll2520
            ANA: all4286
            AVA: Ava_1238
            PMA: Pro1769(fabB)
            PMB: A9601_01531(fabH) A9601_18191(fabF)
            PMC: P9515_01641(fabH) P9515_17971(fabF)
            PMF: P9303_26071(fabF) P9303_26551(fabH)
            PMG: P9301_01551(fabH) P9301_18021(fabF)
            PMH: P9215_01531(fabH) P9215_18831(fabF)
            PME: NATL1_02081(fabH) NATL1_20611(fabF)
            TER: Tery_0510
            SRU: SRU_2739(fabF)
            CHU: CHU_0384(fabF) CHU_1586(fabF) CHU_2114(fabF) CHU_2115(fabG)
                 CHU_2118(fabF) CHU_2863(fabF)
            GFO: GFO_1607 GFO_1660 GFO_1663 GFO_2339(fabH) GFO_2876(fabH)
                 GFO_3343(fabH) GFO_3383(fabF) GFO_3565
            FJO: Fjoh_0255 Fjoh_0446 Fjoh_0646 Fjoh_1102 Fjoh_3231
            FPS: FP0201(fabF) FP1374(fabH1) FP1501(fabH2) FP2264 FP2265 FP2269
                 FP2279(darB) FP2284(fabB) FP2327 FP2379(fabH3)
            CPH: Cpha266_2490
            PVI: Cvib_0200
            RRS: RoseRS_2614
            RCA: Rcas_1803
            TMA: TM0802
            FNO: Fnod_0534
STRUCTURES  PDB: 1B3N  1DD8  1E5M  1EBL  1EK4  1F91  1FJ4  1FJ8  1G5X  1H4F  
                 1HN9  1HND  1HNH  1HNJ  1HNK  1HZP  1J3N  1KAS  1M1M  1MZJ  
                 1MZS  1OX0  1OXH  1TQY  1U6E  1U6S  1UB7  1W0I  1ZOW  2AHB  
                 2AJ9  2ALM  2AQ7  2AQB  2BUH  2BUI  2BYW  2BYX  2BYY  2BYZ  
                 2BZ3  2BZ4  2C9H  2EBD  2EFT  2GFV  2GFW  2GFX  2GFY  2GP6  
                 2GQD  2GYO  2IWY  2IWZ  2IX4  2PFF  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.41
            ExPASy - ENZYME nomenclature database: 2.3.1.41
            ExplorEnz - The Enzyme Database: 2.3.1.41
            ERGO genome analysis and discovery system: 2.3.1.41
            BRENDA, the Enzyme Database: 2.3.1.41
            CAS: 9077-10-5
///
ENTRY       EC 2.3.1.42                 Enzyme
NAME        glycerone-phosphate O-acyltransferase;
            dihydroxyacetone phosphate acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:glycerone-phosphate O-acyltransferase
REACTION    acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate
            [RN:R01013]
ALL_REAC    R01013
SUBSTRATE   acyl-CoA [CPD:C00040];
            glycerone phosphate [CPD:C00111]
PRODUCT     CoA [CPD:C00010];
            acylglycerone phosphate [CPD:C03372]
COMMENT     A membrane protein. Uses CoA derivatives of palmitate, stearate and
            oleate, with highest activity on palmitoyl-CoA.
REFERENCE   1  [PMID:6271231]
  AUTHORS   Ballas LM, Bell RM.
  TITLE     Topography of glycerolipid synthetic enzymes. Synthesis of
            phosphatidylserine, phosphatidylinositol and glycerolipid
            intermediates occurs on the cytoplasmic surface of rat liver
            microsomal vesicles.
  JOURNAL   Biochim. Biophys. Acta. 665 (1981) 586-95.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6746639]
  AUTHORS   Declercq PE, Haagsman HP, Van Veldhoven P, Debeer LJ, Van Golde LM,
            Mannaerts GP.
  TITLE     Rat liver dihydroxyacetone-phosphate acyltransferases and their
            contribution to glycerolipid synthesis.
  JOURNAL   J. Biol. Chem. 259 (1984) 9064-75.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:5656381]
  AUTHORS   Hajra AK.
  TITLE     Biosynthesis of acyl dihydroxyacetone phosphate in guinea pig liver
            mitochondria.
  JOURNAL   J. Biol. Chem. 243 (1968) 3458-65.
  ORGANISM  guinea pig
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00649  glyceronephosphate O-acyltransferase
GENES       HSA: 8443(GNPAT)
            MMU: 14712(Gnpat)
            RNO: 84470(Gnpat)
            CFA: 479204(GNPAT)
            GGA: 421548(GNPAT)
            XLA: 444573(MGC84007)
            DME: Dmel_CG4625(Dhap-at)
            TBR: Tb927.4.3160
            LMA: LmjF34.1090
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.42
            ExPASy - ENZYME nomenclature database: 2.3.1.42
            ExplorEnz - The Enzyme Database: 2.3.1.42
            ERGO genome analysis and discovery system: 2.3.1.42
            BRENDA, the Enzyme Database: 2.3.1.42
            CAS: 37257-19-5
///
ENTRY       EC 2.3.1.43                 Enzyme
NAME        phosphatidylcholine---sterol O-acyltransferase;
            lecithin---cholesterol acyltransferase;
            phospholipid---cholesterol acyltransferase;
            LCAT (lecithin-cholesterol acyltransferase);
            lecithin:cholesterol acyltransferase;
            lysolecithin acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     phosphatidylcholine:sterol O-acyltransferase
REACTION    phosphatidylcholine + a sterol = 1-acylglycerophosphocholine + a
            sterol ester [RN:R02114]
ALL_REAC    R02114
SUBSTRATE   phosphatidylcholine [CPD:C00157];
            sterol [CPD:C00370]
PRODUCT     1-acylglycerophosphocholine [CPD:C04230];
            sterol ester [CPD:C01958]
COMMENT     Palmitoyl, oleoyl and linoleoyl residues can be transferred; a
            number of sterols, including cholesterol, can act as acceptors. The
            bacterial enzyme also catalyses the reactions of EC 3.1.1.4
            phospholipase A2 and EC 3.1.1.5 lysophospholipase.
REFERENCE   1
  AUTHORS   Bartlett, K., Keat, M.J. and Mercer, E.I.
  TITLE     Biosynthesis of sterol esters in Phycomyces blakesleeanus.
  JOURNAL   Phytochemistry 13 (1974) 1107-1113.
  ORGANISM  Phycomyces blakesleeanus
REFERENCE   2  [PMID:7061477]
  AUTHORS   Buckley JT, Halasa LN, MacIntyre S.
  TITLE     Purification and partial characterization of a bacterial
            phospholipid: cholesterol acyltransferase.
  JOURNAL   J. Biol. Chem. 257 (1982) 3320-5.
  ORGANISM  Aeromonas salmonicida
REFERENCE   3  [PMID:4868699]
  AUTHORS   Glomset JA.
  TITLE     The plasma lecithins:cholesterol acyltransferase reaction.
  JOURNAL   J. Lipid. Res. 9 (1968) 155-67.
  ORGANISM  rat [GN:rno], human [GN:hsa]
REFERENCE   4  [PMID:4877146]
  AUTHORS   Vahouny GV, Treadwell CR.
  TITLE     Enzymatic synthesis and hydrolysis of cholesterol esters.
  JOURNAL   Methods. Biochem. Anal. 16 (1968) 219-72.
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00650  lecithin-cholesterol acyltransferase
GENES       HSA: 3931(LCAT)
            MMU: 16816(Lcat)
            RNO: 24530(Lcat)
            CFA: 479680(LCAT)
            XLA: 447501(MGC82035)
            XTR: 448241(lcat)
            CEL: M05B5.4
            PFA: PFF1420w
            EHI: 33.t00023 63.t00024
            AHA: AHA_3791
            BUR: Bcep18194_A6375
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.43
            ExPASy - ENZYME nomenclature database: 2.3.1.43
            ExplorEnz - The Enzyme Database: 2.3.1.43
            ERGO genome analysis and discovery system: 2.3.1.43
            BRENDA, the Enzyme Database: 2.3.1.43
            CAS: 9031-14-5
///
ENTRY       EC 2.3.1.44                 Enzyme
NAME        N-acetylneuraminate 4-O-acetyltransferase;
            sialate O-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:N-acetylneuraminate 4-O-acetyltransferase
REACTION    acetyl-CoA + N-acetylneuraminate = CoA +
            N-acetyl-4-O-acetylneuraminate [RN:R01806]
ALL_REAC    R01806
SUBSTRATE   acetyl-CoA [CPD:C00024];
            N-acetylneuraminate [CPD:C00270]
PRODUCT     CoA [CPD:C00010];
            N-acetyl-4-O-acetylneuraminate [CPD:C04015]
COMMENT     Both free and glycosidically bound N-acetyl- and N-glycolyl-
            neuraminates can act as O-acetyl acceptors.
REFERENCE   1  [PMID:5446640]
  AUTHORS   Schauer R.
  TITLE     [Biosynthesis of N-acetyl-O-acetylneuraminic acids. I. Incorporation
            of (14C) acetate into sections of the submaxillary salivary gland of
            ox and horse]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 351 (1970) 595-602.
  ORGANISM  cow [GN:bta], horse
REFERENCE   2  [PMID:5425947]
  AUTHORS   Schauer R.
  TITLE     [Biosynthesis of N-acetyl-O-acetylneuraminic acids. II. Substrate
            and intracellular localization of bovine acetyl-coenzyme A:
            N-acetylneuraminate-7- and 8-O-acetyltransferase]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 351 (1970) 749-58.
  ORGANISM  cow [GN:bta]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.44
            ExPASy - ENZYME nomenclature database: 2.3.1.44
            ExplorEnz - The Enzyme Database: 2.3.1.44
            ERGO genome analysis and discovery system: 2.3.1.44
            BRENDA, the Enzyme Database: 2.3.1.44
            CAS: 51004-25-2
///
ENTRY       EC 2.3.1.45                 Enzyme
NAME        N-acetylneuraminate 7-O(or 9-O)-acetyltransferase;
            N-acetylneuraminate 7(8)-O-acetyltransferase;
            sialate O-acetyltransferase;
            N-acetylneuraminate 7,8-O-acetyltransferase;
            acetyl-CoA:N-acetylneuraminate-7- or 8-O-acetyltransferase;
            acetyl-CoA:N-acetylneuraminate-7- and/or 8-O-acetyltransferase;
            glycoprotein 7(9)-O-acetyltransferase;
            acetyl-CoA:N-acetylneuraminate-9(7)-O-acetyltransferase;
            N-acetylneuraminate O7-(or O9-)acetyltransferase;
            acetyl-CoA:N-acetylneuraminate-9(or 7)-O-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:N-acetylneuraminate 7-O(or 9-O)-acetyltransferase
REACTION    acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-7-O(or
            9-O)-acetylneuraminate [RN:R01807 R01808]
ALL_REAC    R01807 R01808
SUBSTRATE   acetyl-CoA [CPD:C00024];
            N-acetylneuraminate [CPD:C00270]
PRODUCT     CoA [CPD:C00010];
            N-acetyl-7-O-acetylneuraminate [CPD:C04016];
            N-acetyl-9-O-acetylneuraminate [CPD:C04017]
COMMENT     Both free and glycosidically bound N-acetyl- and
            N-glycolylneuraminates can act as O-acetyl acceptors.
REFERENCE   1  [PMID:5446640]
  AUTHORS   Schauer R.
  TITLE     [Biosynthesis of N-acetyl-O-acetylneuraminic acids. I. Incorporation
            of (14C) acetate into sections of the submaxillary salivary gland of
            ox and horse]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 351 (1970) 595-602.
  ORGANISM  cow [GN:bta], horse
REFERENCE   2  [PMID:5425947]
  AUTHORS   Schauer R.
  TITLE     [Biosynthesis of N-acetyl-O-acetylneuraminic acids. II. Substrate
            and intracellular localization of bovine acetyl-coenzyme A:
            N-acetylneuraminate-7- and 8-O-acetyltransferase]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 351 (1970) 749-58.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K03377  N-acetylneuraminate 7(9)-O-acetyltransferase
GENES       PFA: PFB0505c
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.45
            ExPASy - ENZYME nomenclature database: 2.3.1.45
            ExplorEnz - The Enzyme Database: 2.3.1.45
            ERGO genome analysis and discovery system: 2.3.1.45
            BRENDA, the Enzyme Database: 2.3.1.45
            CAS: 9054-50-6
///
ENTRY       EC 2.3.1.46                 Enzyme
NAME        homoserine O-succinyltransferase;
            homoserine O-transsuccinylase;
            homoserine succinyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     succinyl-CoA:L-homoserine O-succinyltransferase
REACTION    succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine
            [RN:R01777]
ALL_REAC    R01777
SUBSTRATE   succinyl-CoA [CPD:C00091];
            L-homoserine [CPD:C00263]
PRODUCT     CoA [CPD:C00010];
            O-succinyl-L-homoserine [CPD:C01118]
REFERENCE   1
  AUTHORS   Rowbury, R.J. and Woods, D.D.
  TITLE     O-Succinylhomoserine as an intermediate in the synthesis of
            cystathionine by Escherichia coli.
  JOURNAL   J. Gen. Microbiol. 36 (1964) 341-358.
PATHWAY     PATH: map00271  Methionine metabolism
            PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K00651  homoserine O-succinyltransferase
GENES       ECO: b4013(metA)
            ECJ: JW3973(metA)
            ECE: Z5599(metA)
            ECS: ECs4931
            ECC: c4970(metA)
            ECI: UTI89_C4572(metA)
            ECP: ECP_4223
            ECV: APECO1_2463(metA)
            ECW: EcE24377A_4555(metA)
            ECX: EcHS_A4247
            STY: STY4400(metA)
            STT: t4110(metA)
            SPT: SPA4020(metA)
            SEC: SC4061(metA)
            STM: STM4182(metA)
            YPE: YPO3727(metA)
            YPK: y0013(metA)
            YPM: YP_3089(metA)
            YPA: YPA_0015
            YPN: YPN_0012
            YPP: YPDSF_0171
            YPS: YPTB3658(metA)
            YPI: YpsIP31758_0292(metA)
            SFX: S3651(metA)
            SFV: SFV_4084(metA)
            SSN: SSON_4185(metA)
            SBO: SBO_4033(metA)
            SDY: SDY_4330(metA)
            ECA: ECA3992(metA)
            PLU: plu4397(metA)
            SGL: SG2152
            ENT: Ent638_0217
            SPE: Spro_4504
            BFL: Bfl630(metA)
            BPN: BPEN_657(metA)
            XOO: XOO1388
            XOM: XOO_1274(XOO1274)
            VCH: VC1611
            VCO: VC0395_A1216(metA)
            VVU: VV1_2772
            VVY: VV1492
            VPA: VP1751
            VFI: VF2063
            PPR: PBPRA0369
            SON: SO_1676(metA)
            SDN: Sden_2588
            SFR: Sfri_1336
            SAZ: Sama_1374
            SBL: Sbal_1493
            SBM: Shew185_1488
            SLO: Shew_2551
            SPC: Sputcn32_1395
            SSE: Ssed_1472
            SPL: Spea_2784
            SHE: Shewmr4_2598
            SHM: Shewmr7_2665
            SHN: Shewana3_2772
            SHW: Sputw3181_2706
            CPS: CPS_1100(metA)
            PHA: PSHAa2224(metA)
            PAT: Patl_3021
            PIN: Ping_0112
            MCA: MCA1876
            AHA: AHA_0489(metA)
            BCI: BCI_0019(metA)
            RMA: Rmag_0018
            VOK: COSY_0017(metA)
            TBD: Tbd_0246
            HHE: HH0637(metA)
            CJE: Cj1726c(metA)
            CJR: CJE1894(metA)
            CJJ: CJJ81176_0022(metA)
            MES: Meso_3083
            SME: SMc03797(metA)
            SMD: Smed_3030
            ATU: Atu2718(metA)
            ATC: AGR_C_4927
            RET: RHE_CH04033(metA)
            RLE: RL4606(metA)
            BME: BMEII0781
            BMF: BAB2_0751(metA)
            BMS: BRA0486(metA)
            BMB: BruAb2_0737(metA)
            BOV: BOV_A0424(metA)
            OAN: Oant_3489
            BJA: bll0244
            BRA: BRADO6913(metA)
            RPA: RPA4590
            RPB: RPB_1002
            RPD: RPD_1105
            SIL: SPO1729(metA)
            SIT: TM1040_1379
            RSP: RSP_0010
            RSH: Rsph17029_1640
            RSQ: Rsph17025_2166
            JAN: Jann_2351
            RDE: RD1_2784(metA)
            PDE: Pden_4499
            HNE: HNE_3283(metA)
            NAR: Saro_0684
            SWI: Swit_0586
            BSU: BG11534(metB)
            BHA: BH2280
            BAN: BA5655(metA)
            BAR: GBAA5655(metA)
            BAA: BA_0513
            BAT: BAS5257
            BCE: BC5405
            BCA: BCE_5534(metA)
            BCZ: BCZK5103(metA)
            BCY: Bcer98_3924
            BTK: BT9727_5086(metA)
            BTL: BALH_4906(metA)
            BLI: BL01365(metA)
            BLD: BLi02329(metA)
            BCL: ABC2149
            BAY: RBAM_020050
            BPU: BPUM_1927
            OIH: OB0438
            GKA: GK1787
            LLA: L0101(metA)
            LLM: llmg_2182(metA)
            SPN: SP_1576
            SPR: spr1434(metA)
            SPD: SPD_1406(metA)
            SMU: SMU.1466(metA)
            STC: str1222(metA)
            STL: stu1222(metA)
            SSA: SSA_1420(metA)
            SGO: SGO_1002(metA)
            LPL: lp_2537(metA)
            LAC: LBA1237(metA)
            LSL: LSL_1717(metA)
            LBU: LBUL_0089 LBUL_1353
            LCA: LSEI_0479
            LRE: Lreu_1791
            OOE: OEOE_0767
            CAC: CAC1825(metB)
            CTC: CTC01152
            CNO: NT01CX_1211(metA)
            CTH: Cthe_1845
            CDF: CD1826(metA)
            CBO: CBO1874(metA)
            CBA: CLB_1811(metA)
            CBH: CLC_1818(metA)
            CBF: CLI_1938(metA)
            CBE: Cbei_1279
            CKL: CKL_1609(metA1) CKL_1631(metA2)
            AMT: Amet_3708
            DSY: DSY4686
            FRA: Francci3_2001
            BLO: BL0365(metA)
            BAD: BAD_1434(metA)
            SYW: SYNW0850(metA)
            SYC: syc1142_c(metA)
            SYF: Synpcc7942_0371
            SYD: Syncc9605_1800
            SYE: Syncc9902_0855
            SYG: sync_1181(metA)
            SYR: SynRCC307_0796(metA)
            SYX: SynWH7803_1408(metA)
            PMA: Pro0801(metA)
            PMM: PMM0643(metA)
            PMT: PMT0876(metA)
            PMN: PMN2A_0084
            PMI: PMT9312_0643
            PMB: A9601_06991(metA)
            PMC: P9515_07091(metA)
            PMF: P9303_13181(metA)
            PMG: P9301_06701(metA)
            PMH: P9215_07261
            PME: NATL1_07081(metA)
            BTH: BT_2413
            BFR: BF0598
            BFS: BF0548(metA)
            TMA: TM0881
            TPT: Tpet_0046
STRUCTURES  PDB: 2GHR  2H2W  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.46
            ExPASy - ENZYME nomenclature database: 2.3.1.46
            ExplorEnz - The Enzyme Database: 2.3.1.46
            ERGO genome analysis and discovery system: 2.3.1.46
            BRENDA, the Enzyme Database: 2.3.1.46
            CAS: 62213-51-8
///
ENTRY       EC 2.3.1.47                 Enzyme
NAME        8-amino-7-oxononanoate synthase;
            7-keto-8-aminopelargonic acid synthetase;
            7-keto-8-aminopelargonic synthetase;
            8-amino-7-oxopelargonate synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     6-carboxyhexanoyl-CoA:L-alanine C-carboxyhexanoyltransferase
            (decarboxylating)
REACTION    6-carboxyhexanoyl-CoA + L-alanine = 8-amino-7-oxononanoate + CoA +
            CO2 [RN:R03210]
ALL_REAC    R03210
SUBSTRATE   6-carboxyhexanoyl-CoA [CPD:C01063];
            L-alanine [CPD:C00041]
PRODUCT     8-amino-7-oxononanoate [CPD:C01092];
            CoA [CPD:C00010];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:4879561]
  AUTHORS   Eisenberg MA, Star C.
  TITLE     Synthesis of 7-oxo-8-aminopelargonic acid, a biotin vitamer, in
            cell-free extracts of Escherichia coli biotin auxotrophs.
  JOURNAL   J. Bacteriol. 96 (1968) 1291-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:9813126]
  AUTHORS   Alexeev D, Alexeeva M, Baxter RL, Campopiano DJ, Webster SP, Sawyer
            L.
  TITLE     The crystal structure of 8-amino-7-oxononanoate synthase: a
            bacterial PLP-dependent, acyl-CoA-condensing enzyme.
  JOURNAL   J. Mol. Biol. 284 (1998) 401-19.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:9914476]
  AUTHORS   Ploux O, Breyne O, Carillon S, Marquet A.
  TITLE     Slow-binding and competitive inhibition of 8-amino-7-oxopelargonate
            synthase, a pyridoxal-5'-phosphate-dependent enzyme involved in
            biotin biosynthesis, by substrate and intermediate analogs. Kinetic
            and binding studies.
  JOURNAL   Eur. J. Biochem. 259 (1999) 63-70.
  ORGANISM  Escherichia coli [GN:eco], Bacillus sphaericus
REFERENCE   4  [PMID:10642176]
  AUTHORS   Webster SP, Alexeev D, Campopiano DJ, Watt RM, Alexeeva M, Sawyer L,
            Baxter RL.
  TITLE     Mechanism of 8-amino-7-oxononanoate synthase: spectroscopic,
            kinetic, and crystallographic studies.
  JOURNAL   Biochemistry. 39 (2000) 516-28.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00780  Biotin metabolism
ORTHOLOGY   KO: K00652  8-amino-7-oxononanoate synthase
GENES       OSA: 4327870
            CME: CML225C
            AOR: AO090009000589
            DDI: DDB_0231416(hemA)
            TET: TTHERM_01107480
            EHI: 6.t00099
            ECO: b0776(bioF)
            ECJ: JW0759(bioF)
            ECE: Z0995(bioF)
            ECS: ECs0854
            ECC: c0856(bioF)
            ECI: UTI89_C0774(bioF)
            ECP: ECP_0790
            ECV: APECO1_1313(bioF) APECO1_3443
            ECW: EcE24377A_0839(bioF)
            ECX: EcHS_A0830(bioF)
            STY: STY0828(bioF)
            STT: t2092(bioF)
            SPT: SPA1957(bioF)
            SEC: SC0793(bioF)
            STM: STM0795(bioF)
            YPE: YPO1152(bioF)
            YPK: y3030(bioF)
            YPM: YP_1008(bioF)
            YPA: YPA_1059
            YPN: YPN_2849
            YPP: YPDSF_2545
            YPS: YPTB1183(bioF)
            YPI: YpsIP31758_2843(bioF)
            SFL: SF0726(bioF)
            SFX: S0767(bioF)
            SFV: SFV_0759(bioF)
            SSN: SSON_0755(bioF)
            SBO: SBO_0663(bioF)
            SDY: SDY_0830(bioF)
            ECA: ECA2824(bioF)
            PLU: plu1486(bioF)
            BAB: bbp271(bioF)
            WBR: WGLp454(bioF)
            SGL: SG0904
            ENT: Ent638_1267
            SPE: Spro_1312
            HIT: NTHI1580(bioF)
            HIP: CGSHiEE_05345
            HIQ: CGSHiGG_00200
            HDU: HD1684(bioF)
            PMU: PM1901(bioF)
            APL: APL_0941(bioF)
            XFA: XF1357
            XFT: PD0598(bioF)
            XCC: XCC0387(bioF)
            XCB: XC_0399
            XCV: XCV0402(bioF)
            XAC: XAC0387(bioF)
            XOO: XOO0456(bioF)
            XOM: XOO_0420(XOO0420)
            VCH: VC1113
            VCO: VC0395_A0631(bioF)
            VVU: VV1_2942
            VVY: VV1328
            VPA: VP1114
            VFI: VFA0747
            PPR: PBPRA2328
            PAE: PA0501(bioF)
            PAU: PA14_06510(bioF)
            PAP: PSPA7_0601(bioF)
            PPU: PP_0363(bioF)
            PPF: Pput_0389 Pput_3920
            PST: PSPTO_0495(bioF)
            PSB: Psyr_4686
            PSP: PSPPH_4720(bioF)
            PFL: PFL_5692(bioF)
            PFO: Pfl_5175
            PEN: PSEEN5120(bioF)
            PMY: Pmen_4087
            PAR: Psyc_2130(bioF)
            PCR: Pcryo_2454
            ACI: ACIAD0857(bioF)
            SON: SO_2739(bioF)
            SDN: Sden_1659
            SFR: Sfri_1476
            SAZ: Sama_1439
            SBL: Sbal_1759
            SBM: Shew185_1752
            SLO: Shew_1720
            SPC: Sputcn32_2344
            SSE: Ssed_2775
            SHE: Shewmr4_2358
            SHM: Shewmr7_2430
            SHN: Shewana3_2518
            SHW: Sputw3181_1664
            ILO: IL1323(bioF)
            CPS: CPS_2595
            PHA: PSHAa1608(bioF)
            PAT: Patl_2556
            SDE: Sde_3138
            PIN: Ping_1923
            MAQ: Maqu_2755
            CBU: CBU_1006(bioF)
            CBD: COXBU7E912_1041(bioF)
            LPN: lpg1473(bioF)
            LPF: lpl1555(bioF)
            LPP: lpp1429(bioF)
            MCA: MCA1126(bioF)
            FTU: FTT0936c(bioF)
            FTF: FTF0936c(bioF)
            FTL: FTL_1273
            FTH: FTH_1246(bioF)
            FTN: FTN_0814(bioF)
            TCX: Tcr_1979
            NOC: Noc_2100
            AEH: Mlg_2435
            HHA: Hhal_0962
            HCH: HCH_05370(bioF)
            CSA: Csal_1166
            ABO: ABO_2219(bioF)
            MMW: Mmwyl1_3456
            AHA: AHA_1490(bioF)
            BCI: BCI_0247(bioF)
            RMA: Rmag_0835
            VOK: COSY_0760(bioF)
            NME: NMB0472
            NMA: NMA2013(bioF)
            NMC: NMC1676(bioF)
            NGO: NGO1483
            CVI: CV_4380(bioF)
            RSO: RSc1478(bioF)
            REU: Reut_A0148
            REH: H16_A0181(bioF)
            RME: Rmet_0115
            BMA: BMA0101(bioF)
            BMV: BMASAVP1_A3079(bioF)
            BML: BMA10299_A2015(bioF)
            BMN: BMA10247_2271(bioF)
            BXE: Bxe_A4264
            BVI: Bcep1808_3027
            BUR: Bcep18194_A6276
            BCN: Bcen_0301 Bcen_2318
            BCH: Bcen2424_0784 Bcen2424_2932
            BAM: Bamb_2981
            BPS: BPSL0366(bioF)
            BPM: BURPS1710b_0573(bioF)
            BPL: BURPS1106A_0411(bioF)
            BPD: BURPS668_0390(bioF)
            BTE: BTH_I0339(bioF)
            PNU: Pnuc_0154
            BPE: BP2164
            BPA: BPP1775
            BBR: BB3333
            POL: Bpro_0898 Bpro_1579
            PNA: Pnap_4032
            AAV: Aave_3843
            AJS: Ajs_3076
            MPT: Mpe_A0530
            HAR: HEAR1669(bioF)
            MMS: mma_0121(bioF)
            NEU: NE2299(bioF)
            NET: Neut_0461 Neut_2137
            NMU: Nmul_A0228 Nmul_A1130
            EBA: ebA6018(bioF)
            AZO: azo1889(bioF)
            DAR: Daro_2897
            TBD: Tbd_0320
            MFA: Mfla_2163
            HPY: HP0598(bioF)
            HPJ: jhp0545(bioF)
            HPA: HPAG1_0578
            HHE: HH1209(bioF)
            HAC: Hac_1410(bioF)
            WSU: WS2048(bioF)
            TDN: Tmden_1894
            CJE: Cj0306c(bioF)
            CJR: CJE0351(bioF)
            CJJ: CJJ81176_0328(bioF)
            CJU: C8J_0283(bioF)
            CJD: JJD26997_1659(bioF)
            CFF: CFF8240_0086
            ABU: Abu_0254(bioF)
            NIS: NIS_1523
            SUN: SUN_0349
            GSU: GSU2629(bioF)
            GME: Gmet_0842
            GUR: Gura_3246
            PCA: Pcar_1665
            PPD: Ppro_2093 Ppro_2767
            DVU: DVU2564(bioF)
            DDE: Dde_2662
            LIP: LI0421(bioF)
            DPS: DP2547(bioF)
            ADE: Adeh_3452
            AFW: Anae109_3561
            MXA: MXAN_1258(bioF)
            SAT: SYN_02568
            SFU: Sfum_3712
            AMA: AM268
            APH: APH_0979 APH_1016(bioF)
            ERU: Erum1740(bioF)
            ERW: ERWE_CDS_01730(bioF)
            ERG: ERGA_CDS_01680(bioF)
            ECN: Ecaj_0171
            ECH: ECH_0950(bioF)
            NSE: NSE_0613(bioF)
            MLO: mll5830 mll6006 mll9099
            PLA: Plav_0039
            SMD: Smed_0196
            ATU: Atu3998(bioF)
            ATC: AGR_L_1707(bioF)
            RET: RHE_CH02952(kbl) RHE_CH03846(hemAch) RHE_PF00489(hemAf)
            RLE: RL4379(hemA)
            BME: BMEII0776
            BMF: BAB2_0745
            BMS: BRA0491(bioF)
            BMB: BruAb2_0731(bioF)
            BOV: BOV_A0429(bioF)
            OAN: Oant_2822
            BJA: blr2097(bioF)
            BBT: BBta_2777(bioF)
            RPA: RPA2972(bioF)
            RPB: RPB_4344
            RPC: RPC_2099
            RPD: RPD_4240
            RPE: RPE_3400
            NWI: Nwi_2421
            NHA: Nham_2816
            XAU: Xaut_2918 Xaut_3804
            CCR: CC_1576
            PDE: Pden_2917
            MMR: Mmar10_1346
            HNE: HNE_1248(bioF)
            ZMO: ZMO1917(bioF)
            NAR: Saro_0718 Saro_3111
            SAL: Sala_1473
            SWI: Swit_1254 Swit_3900
            GOX: GOX0720
            GBE: GbCGDNIH1_0498
            ACR: Acry_1868
            MAG: amb2759
            MGM: Mmc1_0031
            SUS: Acid_5448
            BSU: BG11527(bioF)
            BHA: BH3907(bioF)
            BAN: BA4339(bioF)
            BAR: GBAA4339(bioF)
            BAA: BA_4798
            BAT: BAS4026
            BCE: BC4117
            BCA: BCE_4187(bioF)
            BCZ: BCZK3873(bioF)
            BCY: Bcer98_2816
            BTK: BT9727_3859(bioF)
            BTL: BALH_3733(bioF)
            BLI: BL00954(bioF)
            BLD: BLi00768(bioF)
            BAY: RBAM_018270(bioF)
            GKA: GK2128
            SAU: SA2212
            SAV: SAV2424
            SAM: MW2347
            SAR: SAR2514
            SAS: SAS2315
            SAC: SACOL2425
            SAB: SAB2305c
            SAA: SAUSA300_2370
            SAO: SAOUHSC_02713
            SAJ: SaurJH9_2450
            SAH: SaurJH1_2498
            SEP: SE0181
            SER: SERP2394
            CTH: Cthe_0022
            TTE: TTE2406(bioF)
            MMO: MMOB5780(bioF)
            MTU: Rv0032(bioF2) Rv1569(bioF1)
            MTC: MT0037 MT1620(bioF)
            MBO: Mb0033(bioF2) Mb1596(bioF1)
            MBB: BCG_0063(bioF2) BCG_1622(bioF1)
            MLE: ML1217(bioF)
            MPA: MAP1275(bioF)
            MAV: MAV_3205(bioF)
            MSM: MSMEG_3189(bioF)
            MVA: Mvan_2789
            MGI: Mflv_3628
            MMC: Mmcs_3077
            MKM: Mkms_3137
            MJL: Mjls_3094
            CDI: DIP1382
            NFA: nfa18190(bioF)
            RHA: RHA1_ro01054(bioF)
            SCO: SCO1243(2SCG1.18c)
            SMA: SAV7094(bioF)
            AAU: AAur_1088(bioF)
            PAC: PPA1866
            NCA: Noca_3413
            FRA: Francci3_3761
            FAL: FRAAL6001(bioF)
            ACE: Acel_1053
            SEN: SACE_0977(bioF) SACE_4477(bioF) SACE_4685(bioF)
            STP: Strop_1570 Strop_1724
            FNU: FN0849
            RBA: RB3176
            CTR: CT777(bioF)
            CTA: CTA_0847(bioF)
            CMU: TC0158
            CPN: CPn0923(bioF_1) CPn1043(bioF_2)
            CPA: CP0809 CP0943
            CPJ: CPj0923(bioF_1) CPj1043(bioF_2)
            CPT: CpB0956 CpB1083
            CCA: CCA00846
            CAB: CAB686(bioF) CAB811
            CFE: CF0170(bioF1) CF0297(bioF2)
            LIL: LA2140(bioF)
            LIC: LIC11780(bioF)
            LBJ: LBJ_1873(bioF)
            LBL: LBL_1411(bioF)
            SYN: slr0917(bioF)
            SYW: SYNW0634(bioF)
            SYC: syc1470_c(bioF)
            SYF: Synpcc7942_0027
            SYD: Syncc9605_2048
            SYE: Syncc9902_0624
            SYG: sync_2338(bioF)
            SYR: SynRCC307_1924(bioF)
            SYX: SynWH7803_2042(bioF)
            TEL: tlr1331(bioF)
            GVI: gll0397(bioF)
            ANA: all0374(bioF)
            AVA: Ava_2819
            PMA: Pro1622(cioF)
            PMM: PMM1468(bioF)
            PMT: PMT1488(bioF)
            PMN: PMN2A_0999
            PMI: PMT9312_1561
            PMB: A9601_16701(bioF)
            PMC: P9515_16481(bioF)
            PMF: P9303_04591(bioF)
            PMG: P9301_16581(bioF)
            PMH: P9215_17361(bioF)
            PME: NATL1_18681(bioF)
            TER: Tery_0352 Tery_1973
            BTH: BT_0870 BT_1443
            BFR: BF1602 BF2377
            BFS: BF1616(bioF) BF2461
            PGI: PG1195(bioF-2) PG1780(bioF-3)
            SRU: SRU_0517(bioF)
            CHU: CHU_2978(bioF)
            GFO: GFO_3561(bioF)
            FJO: Fjoh_0814 Fjoh_2419
            CTE: CT0051(bioF-2) CT1951(bioF-1)
            CCH: Cag_0079 Cag_0226
            CPH: Cpha266_0113 Cpha266_2306
            PVI: Cvib_0322 Cvib_1710
            PLT: Plut_0257 Plut_2069
            AAE: aq_626(bioF)
            MMP: MMP1574(bioF)
            MMQ: MmarC5_0002
            MMZ: MmarC7_0821
            MAE: Maeo_1419
            MVN: Mevan_0886
            HMA: rrnAC0885(bioF)
            NPH: NP4232A(bioF)
            TAC: Ta1189
            TVO: TVN0398
            PHO: PH0292
            PAB: PAB1244
            PFU: PF0265
            TKO: TK2217
STRUCTURES  PDB: 1BS0  1DJ9  1DJE  2G6W  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.47
            ExPASy - ENZYME nomenclature database: 2.3.1.47
            ExplorEnz - The Enzyme Database: 2.3.1.47
            ERGO genome analysis and discovery system: 2.3.1.47
            BRENDA, the Enzyme Database: 2.3.1.47
            CAS: 9075-61-0
///
ENTRY       EC 2.3.1.48                 Enzyme
NAME        histone acetyltransferase;
            nucleosome-histone acetyltransferase;
            histone acetokinase;
            histone acetylase;
            histone transacetylase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:histone acetyltransferase
REACTION    acetyl-CoA + histone = CoA + acetylhistone [RN:R03552]
ALL_REAC    R03552
SUBSTRATE   acetyl-CoA [CPD:C00024];
            histone [CPD:C01429]
PRODUCT     CoA [CPD:C00010];
            acetylhistone [CPD:C01997]
COMMENT     A group of enzymes with differing specificities towards histone
            acceptors.
REFERENCE   1  [PMID:5031160]
  AUTHORS   Gallwitz D, Sures I.
  TITLE     Histone acetylation. Purification and properties of three
            histone-specific acetyltransferases from rat thymus nuclei.
  JOURNAL   Biochim. Biophys. Acta. 263 (1972) 315-28.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map01510  Neurodegenerative Disorders
            PATH: map04110  Cell cycle
            PATH: map04310  Wnt signaling pathway
            PATH: map04330  Notch signaling pathway
            PATH: map04350  TGF-beta signaling pathway
            PATH: map04520  Adherens junction
            PATH: map04630  Jak-STAT signaling pathway
            PATH: map04720  Long-term potentiation
            PATH: map04916  Melanogenesis
            PATH: map05040  Huntington's disease
            PATH: map05211  Renal cell carcinoma
            PATH: map05215  Prostate cancer
ORTHOLOGY   KO: K00653  histone acetyltransferase
            KO: K04498  E1A/CREB-binding protein
            KO: K06062  p300/CBP-associated factor
GENES       HSA: 10524(HTATIP) 11143(MYST2) 1387(CREBBP) 2033(EP300)
                 203611(CDY2B) 23522(MYST4) 253175(CDY1B) 2648(GCN5L2)
                 7994(MYST3) 8202(NCOA3) 84148(MYST1) 8520(HAT1) 8648(NCOA1)
                 8850(PCAF) 9085(CDY1) 9329(GTF3C4) 9426(CDY2A)
            PTR: 450123(CDY2A) 451329(HTATIP) 454677(GCN5L2) 454678(RAB5C)
                 455108(MYST2) 460219(PCAF) 464147(MYST3) 467891(CREBBP)
                 468102(LOC468102)
            MMU: 107435(Hat1) 12914(Crebbp) 14534(Gcn5l2) 17977(Ncoa1)
                 17979(Ncoa3) 18519(Pcaf) 217127(Myst2) 244349(Myst3)
                 269252(Gtf3c4) 330129(EG330129) 67773(Myst1) 81601(Htatip)
            RNO: 192218(Htatip) 301164(Pcaf) 303470(Myst2)
                 303539(Gcn5l2_predicted) 306571(Myst3) 310194(Myst1)
                 313929(Ncoa1_predicted) 54244(Crebbp) 84584(Ncoa3)
            CFA: 475684(NCOA1) 477052(PCAF) 479777(LOC479777) 479866(CREBBP)
                 483728(HTATIP) 485915(NCOA3) 490971(GCN5L2) 611269(LOC611269)
            BTA: 407215(PCAF) 505453(LOC505453) 514420(LOC514420)
                 523707(LOC523707) 525346(LOC525346)
            SSC: 574068(NCOA1)
            GGA: 374037(HAT1) 374232(GCN5L2) 416667(CREBBP) 418000(EP300)
                 419208(NCOA3) 420877(CDYL) 422016(RCJMB04_27h20) 423734(MYST4)
                 425530(RCJMB04_13m17) 426789(MYST3) 428441(PCAF)
            XLA: 379685(MGC68869) 447734(MGC81978) 495689(LOC495689)
            DRE: 323181(myst2) 335570(myst1) 563942(si:ch211-1j13.2)
            SPU: 577009(LOC577009) 577224(LOC577224) 579684(LOC579684)
                 579906(LOC579906) 580902(LOC580902) 585201(LOC585201)
            DME: Dmel_CG11290(enok) Dmel_CG15319(nej) Dmel_CG1966(Acf1)
                 Dmel_CG3025(mof) Dmel_CG33520(Rpb4) Dmel_CG4107
                 Dmel_CG5229(chm) Dmel_CG6121(Tip60) Dmel_CG7098(dik)
                 Dmel_CG9638(Ada2b)
            CEL: M03C11.4(tag-235) R10E11.1(bromodomain) Y47G6A.6(pcaf-1)
            ATH: AT5G09740 AT5G56740 AT5G64610
            OSA: 4343971 4346812
            CME: CMS083C
            SCE: YOR244W(ESA1)
            AGO: AGOS_ACR138W AGOS_AGL001W
            KLA: KLLA0F11209g
            PIC: PICST_40548 PICST_52077(HAT1) PICST_82300
            CAL: CaO19_12871(CaO19.12871) CaO19_7387(CaO19.7387)
            CGR: CAGL0F08283g CAGL0J03696g CAGL0L09042g
            SPO: SPAC139.06 SPAC1952.05 SPAC637.12c
            ANI: AN3621.2 AN6214.2
            AFM: AFUA_2G05530 AFUA_2G12030 AFUA_4G12650
            AOR: AO090001000664 AO090009000327 AO090026000444
            CNE: CNA05430 CNB03160
            UMA: UM02567.1 UM03302.1 UM05240.1
            DDI: DDBDRAFT_0167416 DDBDRAFT_0167844 DDB_0220684(gcn5)
            PFA: PF08_0034
            CPV: cgd3_3190 cgd7_60
            CHO: Chro.30361 Chro.70018
            TAN: TA06835 TA20705
            TPV: TP01_0465
            TET: TTHERM_00046760 TTHERM_00248390 TTHERM_00319970
            TBR: Tb927.8.3310
            TCR: 509769.110
            LMA: LmjF23.1350
            EHI: 60.t00011 67.t00013
            CHU: CHU_1154(hat)
            DEB: DehaBAV1_0586
            MMP: MMP1577(hat)
            MMZ: MmarC7_0824
            MAE: Maeo_0279
            MVN: Mevan_0889
            MAC: MA0826(hat)
            MMA: MM_1974
            RCI: RRC19(hat)
STRUCTURES  PDB: 1BOB  1F68  1N72  1P4Q  1QSM  1QSO  1TOT  1U2N  1WGS  1WO3  
                 1WO4  1WO5  1WO6  1WO7  1WUG  1WUM  1XIU  1YGH  1Z4R  1ZAF  
                 1ZOQ  1ZS5  2A3I  2BUD  2C52  2D82  2EKO  2FVJ  2GIV  2GTK  
                 2NV7  2OU2  2OZU  2P0W  2P54  2PQ8  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.48
            ExPASy - ENZYME nomenclature database: 2.3.1.48
            ExplorEnz - The Enzyme Database: 2.3.1.48
            ERGO genome analysis and discovery system: 2.3.1.48
            BRENDA, the Enzyme Database: 2.3.1.48
            CAS: 9054-51-7
///
ENTRY       EC 2.3.1.49                 Enzyme
NAME        deacetyl-[citrate-(pro-3S)-lyase] S-acetyltransferase;
            S-acetyl phosphopantetheine:deacetyl citrate lyase
            S-acetyltransferase;
            deacetyl-[citrate-(pro-3S)-lyase] acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     S-acetylphosphopantetheine:deacetyl-[citrate-oxaloacetate-lyase((pro
            -3S)-CH2COO-->acetate)] S-acetyltransferase
REACTION    S-acetylphosphopantetheine +
            deacetyl-[citrate-oxaloacetate-lyase((pro-3S)-CH2COO-->acetate)] =
            phosphopantetheine +
            [citrate-oxaloacetate-lyase((pro-3S)-CH2COO-->acetate)] [RN:R04588]
ALL_REAC    R04588
SUBSTRATE   S-acetylphosphopantetheine [CPD:C03725];
            deacetyl-[citrate-oxaloacetate-lyase((pro-3S)-CH2COO-->acetate)]
            [CPD:C04829]
PRODUCT     phosphopantetheine [CPD:C01134];
            [citrate-oxaloacetate-lyase((pro-3S)-CH2COO-->acetate)] [CPD:C04747]
COMMENT     Both this enzyme and EC 6.2.1.22, [citrate (pro-3S)-lyase] ligase,
            acetylate and activate EC 4.1.3.6, citrate (pro-3S)-lyase.
REFERENCE   1  [PMID:4741546]
  AUTHORS   Singh M, Bottger B, Stewart C, Brooks GC, Srere PA.
  TITLE     S-acetyl phosphopantetheine: deacetyl citrate lyase S-acetyl
            transferase from Klebsiella aerogenes.
  JOURNAL   Biochem. Biophys. Res. Commun. 53 (1973) 1-9.
  ORGANISM  Klebsiella aerogenes
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.49
            ExPASy - ENZYME nomenclature database: 2.3.1.49
            ExplorEnz - The Enzyme Database: 2.3.1.49
            ERGO genome analysis and discovery system: 2.3.1.49
            BRENDA, the Enzyme Database: 2.3.1.49
            CAS: 42616-18-2
///
ENTRY       EC 2.3.1.50                 Enzyme
NAME        serine C-palmitoyltransferase;
            serine palmitoyltransferase;
            SPT;
            3-oxosphinganine synthetase;
            acyl-CoA:serine C-2 acyltransferase decarboxylating
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     palmitoyl-CoA:L-serine C-palmitoyltransferase (decarboxylating)
REACTION    palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
            [RN:R01281]
ALL_REAC    R01281
SUBSTRATE   palmitoyl-CoA [CPD:C00154];
            L-serine [CPD:C00065]
PRODUCT     CoA [CPD:C00010];
            3-dehydro-D-sphinganine [CPD:C02934];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:4388074]
  AUTHORS   Brady RN, Di Mari SJ, Snell EE.
  TITLE     Biosynthesis of sphingolipid bases. 3. Isolation and
            characterization of ketonic intermediates in the synthesis of
            sphingosine and dihydrosphingosine by cell-free extracts of
            Hansenula ciferri.
  JOURNAL   J. Biol. Chem. 244 (1969) 491-6.
  ORGANISM  Hansenula ciferri
REFERENCE   2  [PMID:4386961]
  AUTHORS   Stoffel W, LeKim D, Sticht G.
  TITLE     Biosynthesis of dihydrosphingosine in vitro.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 349 (1968) 664-70.
  ORGANISM  Hansenula ciferri, rat [GN:rno]
PATHWAY     PATH: map00600  Sphingolipid metabolism
ORTHOLOGY   KO: K00654  serine palmitoyltransferase
GENES       HSA: 10558(SPTLC1) 9517(SPTLC2)
            PTR: 464590(LOC464590)
            MMU: 20773(Sptlc2) 268656(Sptlc1)
            CFA: 480403(SPTLC2)
            GGA: 423379(SPTLC2) 426145(SPTLC1)
            XLA: 432022(MGC81520) 444190(MGC80715)
            SPU: 579033(LOC579033)
            DME: Dmel_CG4016(Spt-I) Dmel_CG4162
            CEL: F43H9.2(sptl-2) T22G5.5(sptl-3)
            ATH: AT3G48780 AT3G48790 AT5G23670(LCB2)
            OSA: 4326966 4331075 4332274
            SCE: YDR062W(LCB2) YMR296C(LCB1)
            AGO: AGOS_ABR145C AGOS_AGR127C
            PIC: PICST_84331(LCB2) PICST_90811(LCB1)
            CGR: CAGL0G05071g
            SPO: SPAC21E11.08(lcb2) SPBC29A3.20c
            ANI: AN1102.2 AN3728.2
            AFM: AFUA_1G11890 AFUA_6G00300 AFUA_6G12390
            AOR: AO090001000375
            CNE: CNA07210
            ECU: ECU05_0730
            DDI: DDB_0232040(sptA) DDB_0232041(sptB)
            TBR: Tb10.70.3220 Tb927.4.1020
            TCR: 503453.100 506405.50
            LMA: LmjF34.3740
            EHI: 32.t00018
            ZMO: ZMO1270
            GOX: GOX2056
            GBE: GbCGDNIH1_0239
STRUCTURES  PDB: 2JG2  2JGT  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.50
            ExPASy - ENZYME nomenclature database: 2.3.1.50
            ExplorEnz - The Enzyme Database: 2.3.1.50
            ERGO genome analysis and discovery system: 2.3.1.50
            BRENDA, the Enzyme Database: 2.3.1.50
            CAS: 62213-50-7
///
ENTRY       EC 2.3.1.51                 Enzyme
NAME        1-acylglycerol-3-phosphate O-acyltransferase;
            1-acyl-sn-glycero-3-phosphate acyltransferase;
            1-acyl-sn-glycerol 3-phosphate acyltransferase;
            1-acylglycero-3-phosphate acyltransferase;
            1-acylglycerolphosphate acyltransferase;
            1-acylglycerophosphate acyltransferase;
            lysophosphatidic acid-acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:1-acyl-sn-glycerol-3-phosphate 2-O-acyltransferase
REACTION    acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA +
            1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
ALL_REAC    R02241 > R02760;
            (other) R04361
SUBSTRATE   acyl-CoA [CPD:C00040];
            1-acyl-sn-glycerol 3-phosphate [CPD:C00681]
PRODUCT     CoA [CPD:C00010];
            1,2-diacyl-sn-glycerol 3-phosphate [CPD:C00416]
COMMENT     Acyl-[acyl-carrier-protein] can also act as an acyl donor. The
            animal enzyme is specific for the transfer of unsaturated fatty acyl
            groups.
REFERENCE   1  [PMID:6825679]
  AUTHORS   Frentzen M, Heinz E, McKeon TA, Stumpf PK.
  TITLE     Specificities and selectivities of glycerol-3-phosphate
            acyltransferase and monoacylglycerol-3-phosphate acyltransferase
            from pea and spinach chloroplasts.
  JOURNAL   Eur. J. Biochem. 129 (1983) 629-36.
  ORGANISM  Pisum sativum, spinach
REFERENCE   2  [PMID:5661029]
  AUTHORS   Hill EE, Lands WE.
  TITLE     Incorporation of long-chain and polyunsaturated acids into
            phosphatidate and phosphatidylcholine.
  JOURNAL   Biochim. Biophys. Acta. 152 (1968) 645-8.
  ORGANISM  rat [GN:rno], guinea pig
REFERENCE   3  [PMID:4774123]
  AUTHORS   Yamashita S, Hosaka K, Numa S.
  TITLE     Acyl-donor specificities of partially purified
            1-acylglycerophosphate acyltransferase, 2-acylglycerophosphate
            acyltransferase and 1-acylglycerophosphorylcholine acyltransferase
            from rat-liver microsomes.
  JOURNAL   Eur. J. Biochem. 38 (1973) 25-31.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00561  Glycerolipid metabolism
            PATH: map00564  Glycerophospholipid metabolism
            PATH: map00565  Ether lipid metabolism
ORTHOLOGY   KO: K00655  1-acyl-sn-glycerol-3-phosphate acyltransferase
GENES       HSA: 10554(AGPAT1) 10555(AGPAT2) 137964(AGPAT6) 56894(AGPAT3)
                 56895(AGPAT4)
            PTR: 462582(AGPAT1) 464140(AGPAT6)
            MMU: 102247(Agpat6) 28169(Agpat3) 55979(Agpat1) 67512(Agpat2)
                 68262(Agpat4)
            RNO: 170919(Agpat4)
            CFA: 474857(AGPAT1) 475572(AGPAT6) 612306(AGPAT4)
            BTA: 282137(AGPAT1) 511614(LOC511614)
            GGA: 418550(AGPAT3) 419941(AGPAT1) 421578(AGPAT4) 426788(AGPAT6)
                 770506(LOC770506)
            XLA: 380148(agpat3) 432108(MGC80025) 443578(LOC443578)
                 447483(MGC81841) 447513(MGC82195)
            XTR: 493481(agpat3) 496716(agpat4)
            DRE: 406265(agpat4) 406734(agpat3)
            SPU: 576124(LOC576124) 586692(LOC586692)
            DME: Dmel_CG17608 Dmel_CG3209 Dmel_CG3812
            CEL: F59F4.4(acl-1) T06E8.1(acl-2)
            ATH: AT4G30580(ATS2)
            OSA: 4337061 4349006
            CME: CMF185C CMJ021C
            SCE: YDL052C(SLC1)
            AGO: AGOS_AFR592W
            CGR: CAGL0I04070g
            SPO: SPAC1851.02
            ANI: AN6139.2
            AFM: AFUA_2G08600
            AOR: AO090011000843
            CNE: CNH03840
            UMA: UM06426.1
            DDI: DDBDRAFT_0183825
            TAN: TA14465
            TET: TTHERM_00354810 TTHERM_00812730
            TBR: Tb11.01.6800
            TCR: 509157.60
            LMA: LmjF32.1960
            ECO: b3018(plsC)
            ECJ: JW2986(plsC)
            ECE: Z4372(plsC)
            ECS: ECs3902
            ECC: c3758(plsC)
            ECI: UTI89_C3444(plsC)
            ECP: ECP_3107
            ECV: APECO1_3401(plsC)
            ECW: EcE24377A_3486(plsC)
            ECX: EcHS_A3196
            STY: STY3350(plsC)
            STT: t3094(plsC)
            SPT: SPA3042(plsC)
            SEC: SC3117(plsC)
            STM: STM3173(plsC)
            YPE: YPO0672(plsC)
            YPK: y3506(plsC)
            YPM: YP_2988(plsC2)
            YPA: YPA_3119
            YPN: YPN_0530
            YPP: YPDSF_0455
            YPS: YPTB3391(plsC)
            YPI: YpsIP31758_0582
            SFL: SF3062(plsC)
            SFX: S3266(plsC)
            SFV: SFV_3067(plsC)
            SSN: SSON_3160(plsC)
            SBO: SBO_2880(plsC)
            SDY: SDY_3219(plsC)
            ECA: ECA0346(plsC)
            PLU: plu3948(plsC)
            WBR: WGLp498(plsC)
            SGL: SG0276
            ENT: Ent638_3426
            SPE: Spro_4258
            BFL: Bfl066(plsC)
            BPN: BPEN_068(plsC)
            HIT: NTHI0891(plsC)
            HDU: HD0049(plsC)
            HSO: HS_0499(plsC)
            PMU: PM0103(plsC)
            MSU: MS0510(plsC)
            APL: APL_1488(plsC)
            ASU: Asuc_2071
            XCC: XCC0179 XCC4010(plsC)
            XCB: XC_0188 XC_4099
            XCV: XCV0180 XCV4187
            XAC: XAC0197 XAC4099(plsC)
            XOO: XOO4318 XOO4496
            XOM: XOO_4068(XOO4068) XOO_4236(XOO4236)
            VCH: VC2513
            VCO: VC0395_A2095(plsC)
            VVU: VV1_0678 VV1_2699
            VVY: VV0462 VV1561
            VPA: VP2657
            VFI: VF0402 VF0845
            PPR: PBPRA0468 PBPRB1496
            PAE: PA0005
            PAU: PA14_00060 PA14_56570
            PPU: PP_0058 PP_1844(plsC)
            PPF: Pput_3866
            PST: PSPTO_0187
            PSB: Psyr_0009
            PSP: PSPPH_0009(plsC) PSPPH_4054
            PFL: PFL_0011 PFL_1839
            PFO: Pfl_0007 Pfl_1743
            PEN: PSEEN0014(hdtS) PSEEN1136 PSEEN1546
            PMY: Pmen_2584
            SON: SO_0567(plsC)
            SDN: Sden_0530
            SFR: Sfri_3514
            SAZ: Sama_3139
            SBL: Sbal_0529
            SBM: Shew185_3796
            SLO: Shew_0450
            SPC: Sputcn32_3308
            SSE: Ssed_0619
            SPL: Spea_3713
            SHE: Shewmr4_0569
            SHM: Shewmr7_3461
            SHN: Shewana3_0568 Shewana3_3590
            SHW: Sputw3181_0633
            ILO: IL1952(plsC)
            CPS: CPS_1016(plsC) CPS_4740
            PHA: PSHAa2584(plsC) PSHAa2845
            PAT: Patl_1030
            SDE: Sde_0011
            PIN: Ping_0863
            MAQ: Maqu_3682
            LPN: lpg0551(plsC)
            LPF: lpl0594
            LPP: lpp0612
            MCA: MCA2052
            FTU: FTT1762c FTT1763c
            FTF: FTF1762c FTF1763c
            FTL: FTL_0087 FTL_0088
            FTH: FTH_0083
            FTN: FTN_1749 FTN_1750
            TCX: Tcr_0357
            NOC: Noc_0375 Noc_1727
            AEH: Mlg_0009
            HCH: HCH_01719
            CSA: Csal_0455
            ABO: ABO_0006(plsC) ABO_0683(plsC2) ABO_1917(plsC1)
            MMW: Mmwyl1_4060
            AHA: AHA_3740(plsC)
            BCI: BCI_0624(plsC)
            VOK: COSY_0450(plsC)
            NME: NMB1294 NMB2034
            NMA: NMA0404(nlaB) NMA1504(plsC)
            NMC: NMC1231 NMC2015(nlaB)
            NGO: NGO0611 NGO2069
            CVI: CV_1658 CV_4063(plsC)
            RSO: RS00796(RSp0371) RSc0522(RS04959) RSc0680(plsC)
            REU: Reut_A0505
            REH: H16_A0519(plsC1) H16_A2911(plsC2)
            RME: Rmet_0444 Rmet_2738
            BMA: BMA0216 BMA1992
            BXE: Bxe_A0927 Bxe_A1359 Bxe_A3806 Bxe_A4015 Bxe_B1022
            BUR: Bcep18194_A3967 Bcep18194_A4604 Bcep18194_A6031
            BCN: Bcen_0387
            BCH: Bcen2424_1459
            BAM: Bamb_0742 Bamb_1340 Bamb_2756
            BPS: BPSL0665 BPSL1963 BPSL2688(plsC)
            BPM: BURPS1710b_0878(nlaB) BURPS1710b_1865 BURPS1710b_3165(plsC)
            BTE: BTH_I0582 BTH_I1467 BTH_I2615
            BPE: BP0036
            BPA: BPP3657
            BBR: BB4092
            RFR: Rfer_3693
            POL: Bpro_4200
            MPT: Mpe_A0710 Mpe_A3378
            HAR: HEAR0373 HEAR2735(plsC)
            MMS: mma_0423 mma_2945
            NEU: NE0612(plsC) NE1184(nlaB)
            NET: Neut_1866 Neut_1950
            NMU: Nmul_A0207 Nmul_A0548
            EBA: ebA1327(nlaB) ebA3306(plsC) ebA5567(plsC)
            AZO: azo0667 azo0854(plsC)
            DAR: Daro_3537
            TBD: Tbd_2345
            MFA: Mfla_0468 Mfla_0642
            HPY: HP1348(plsC)
            HPA: HPAG1_1295
            HHE: HH1623(plsC)
            HAC: Hac_0277(plsC)
            WSU: WS0603(plsC)
            TDN: Tmden_0487
            CJE: Cj0516(plsC)
            CJR: CJE0623
            CJU: C8J_0480
            CFF: CFF8240_0949
            CCV: CCV52592_2001
            CHA: CHAB381_0843
            ABU: Abu_2125(plsC)
            NIS: NIS_0870(plsC)
            SUN: SUN_1465(plsC)
            GSU: GSU3116
            GME: Gmet_0363
            GUR: Gura_4396
            PCA: Pcar_0644
            PPD: Ppro_0380
            DVU: DVU1688
            DDE: Dde_1136 Dde_2001
            LIP: LI0013
            BBA: Bd0348 Bd1844
            DPS: DP0336
            ADE: Adeh_1600 Adeh_2078 Adeh_3927
            AFW: Anae109_0276 Anae109_0508
            MXA: MXAN_0147 MXAN_3330 MXAN_3969 MXAN_5578
            SAT: SYN_01275
            SFU: Sfum_0937 Sfum_1596
            RPR: RP469
            RTY: RT0456(plsC)
            RCO: RC0711(plsC)
            RFE: RF_0825(plsC)
            RBE: RBE_0789(plsC)
            OTS: OTBS_0216(plsC)
            WOL: WD1149
            WBM: Wbm0733
            AMA: AM1235(plsC)
            APH: APH_1373
            ERU: Erum0550(plsC)
            ERW: ERWE_CDS_00460(plsC)
            ERG: ERGA_CDS_00450(plsC)
            ECN: Ecaj_0042
            ECH: ECH_0072
            NSE: NSE_0407
            PUB: SAR11_0412(plsC)
            MLO: mlr3529
            MES: Meso_3088
            SME: SMc00714
            ATU: Atu3609(plsC)
            ATC: AGR_L_2433
            RET: RHE_CH00377(olsA) RHE_CH03805(plsC)
            RLE: RL0396 RL4333 pRL90201
            BME: BMEI0075 BMEI1977
            BMF: BAB1_1994 BAB1_2153
            BMS: BR1994
            BMB: BruAb1_1969 BruAb1_2126
            BJA: blr1393(plsC)
            BRA: BRADO6467
            BBT: BBta_1179
            RPA: RPA4334 RPA4733(plsC)
            RPB: RPB_0837 RPB_1289
            RPC: RPC_4127 RPC_4864
            RPD: RPD_0946
            RPE: RPE_4180 RPE_4829
            NWI: Nwi_0579
            NHA: Nham_0670 Nham_0698
            BHE: BH16290(plsC)
            BQU: BQ13210(plsC)
            CCR: CC_2219
            SIL: SPO0339 SPO2451
            SIT: TM1040_1209 TM1040_3500
            RSP: RSP_0735 RSP_3827
            JAN: Jann_2435
            RDE: RD1_1601 RD1_2655
            MMR: Mmar10_2377
            HNE: HNE_3392
            ZMO: ZMO0099(plsC) ZMO0419(plsC)
            SAL: Sala_0193
            GOX: GOX0276 GOX2010
            GBE: GbCGDNIH1_0119 GbCGDNIH1_0134
            RRU: Rru_A3257 Rru_A3769
            MAG: amb4445 amb4462
            MGM: Mmc1_2324
            ABA: Acid345_0120 Acid345_2618
            BAN: BA2240
            BAR: GBAA2240
            BAA: BA_2745(plsC)
            BAT: BAS2086
            BCE: BC0228 BC2195
            BCA: BCE_2270
            BCZ: BCZK0197 BCZK2024(plsC)
            BCY: Bcer98_1643
            BTK: BT9727_2026(plsC)
            BTL: BALH_0207(plsC)
            BCL: ABC1873(plsC)
            BPU: BPUM_0903
            OIH: OB0869 OB1801
            GKA: GK2226
            SAB: SAB1585c
            SAA: SAUSA300_1673
            SAO: SAOUHSC_01837
            LWE: lwe1663
            LLC: LACR_0098
            LLM: llmg_0119
            SPY: SPy_1410
            SPZ: M5005_Spy_1149
            SPM: spyM18_1418
            SPG: SpyM3_1075
            SPS: SPs0788
            SPH: MGAS10270_Spy1221
            SPI: MGAS10750_Spy1257
            SPJ: MGAS2096_Spy1217
            SPK: MGAS9429_Spy1197
            SPA: M6_Spy1177
            SPB: M28_Spy1145
            SPN: SP_1624
            SPR: spr1465
            SPD: SPD_1437
            SMU: SMU.624
            STC: str1563
            STL: stu1563
            STE: STER_1522
            SSA: SSA_0713(plsC)
            SGO: SGO_1604
            LPL: lp_2060(plsC)
            LJO: LJ1502
            LAC: LBA1272
            LSA: LSA1268(plsC)
            LSL: LSL_0508(plsC)
            LDB: Ldb1347
            LBU: LBUL_1256
            LBR: LVIS_1355
            LCA: LSEI_1589
            LGA: LGAS_0799
            LRE: Lreu_0680
            EFA: EF2691
            LME: LEUM_1202
            STH: STH1669
            CAC: CAC0965
            CPE: CPE1418
            CPF: CPF_1526(plsD) CPF_1671
            CPR: CPR_1319 CPR_1407
            CTC: CTC00354 CTC00551
            CNO: NT01CX_0141 NT01CX_1393
            CHY: CHY_1926(plsC)
            DSY: DSY2256
            SWO: Swol_1345
            TTE: TTE1351(plsC) TTE2192(plsC2)
            MTA: Moth_1330
            MGE: MG_212(plsC)
            MPN: MPN299(plsB)
            MPU: MYPU_1140(plsC)
            MPE: MYPE370(plsC)
            MGA: MGA_0039(plsC)
            MMY: MSC_0577(plsC)
            MMO: MMOB4780(plsC)
            MHY: mhp652
            MHJ: MHJ_0632(plsC)
            MHP: MHP7448_0631(plsC)
            MSY: MS53_0097(plsC)
            MCP: MCAP_0402
            UUR: UU344(plsC)
            POY: PAM295(plsC)
            AYW: AYWB_428(plsC)
            MFL: Mfl382
            MTU: Rv2182c Rv2483c(plsC)
            MTC: MT2237
            MBO: Mb2204c Mb2508c(plsC)
            MBB: BCG_2197c BCG_2501c(plsC)
            MLE: ML0892
            MPA: MAP1920c
            MSM: MSMEG_4248
            MVA: Mvan_4075
            MMC: Mmcs_3277 Mmcs_3619
            MKM: Mkms_3692
            MJL: Mjls_3624
            CGL: NCgl2104(cgl2184)
            CGB: cg2398(plsC)
            CEF: CE2077
            CDI: DIP1618
            CJK: jk0729(plsC)
            NFA: nfa17120
            RHA: RHA1_ro04047(plsC) RHA1_ro04182 RHA1_ro05647 RHA1_ro06465
            SCO: SCO1228(2SCG1.03) SCO1566(SCL24.02) SCO2122(SC6E10.16c)
            SMA: SAV6080(plsC3) SAV6783(plsC4) SAV7111(plsC6)
            TWH: TWT214(plsC)
            TWS: TW557
            LXX: Lxx12140(plsC) Lxx15420(plsC)
            CMI: CMM_0531(plsC)
            PAC: PPA0724 PPA2237
            TFU: Tfu_1036 Tfu_1417
            FRA: Francci3_3088
            FAL: FRAAL4897 FRAAL5087
            SEN: SACE_1702 SACE_1791(plsC) SACE_5233(plsC) SACE_6138(plsC)
            BLO: BL1424
            BAD: BAD_1015
            RXY: Rxyl_1439
            CTR: CT453(plsC) CT775
            CTA: CTA_0495(plsC) CTA_0845
            CMU: TC0156 TC0738
            CPN: CPn0569(plsC) CPn0921
            CPA: CP0180 CP0945
            CPJ: CPj0569(plsC) CPj0921
            CPT: CpB0591 CpB0953
            CCA: CCA00173 CCA00848
            CAB: CAB170 CAB813
            CFE: CF0168(sga) CF0834(plsC)
            PCU: pc0318(plsC)
            BBU: BB0037(plsC)
            BGA: BG0037(plsC)
            BAF: BAPKO_0037(plsC)
            TPA: TP0361
            TDE: TDE1989
            SYN: sll1848(plsC)
            SYW: SYNW2250(plsC)
            SYC: syc0100_c(plsC)
            SYF: Synpcc7942_1457
            SYD: Syncc9605_2388
            SYE: Syncc9902_0304
            SYG: sync_2601
            SYR: SynRCC307_0246(plsC)
            SYX: SynWH7803_2252(plsC)
            CYA: CYA_0326
            CYB: CYB_1706
            TEL: tlr0042
            GVI: gll3009
            ANA: alr0241
            AVA: Ava_2141 Ava_2731
            PMA: Pro0160(plsC)
            PMM: PMM0138(plsC)
            PMT: PMT1998(plsC)
            PMN: PMN2A_1504
            PMI: PMT9312_0140
            PMB: A9601_01551
            PMC: P9515_01661
            PMF: P9303_26571
            PMG: P9301_01571
            PME: NATL1_02101
            TER: Tery_1819
            BTH: BT_0243
            BFR: BF3148
            BFS: BF2983
            PGI: PG1249
            SRU: SRU_2301
            CHU: CHU_2690(plsC) CHU_2828(plsC)
            GFO: GFO_3250
            FPS: FP0052(plsC) FP2256
            CTE: CT2036(plsC)
            CCH: Cag_0137
            CPH: Cpha266_2547
            PVI: Cvib_1631
            PLT: Plut_1988
            TTH: TTC0983
            TTJ: TTHA1348
            TMA: TM1693
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.51
            ExPASy - ENZYME nomenclature database: 2.3.1.51
            ExplorEnz - The Enzyme Database: 2.3.1.51
            ERGO genome analysis and discovery system: 2.3.1.51
            BRENDA, the Enzyme Database: 2.3.1.51
            CAS: 51901-16-7
///
ENTRY       EC 2.3.1.52                 Enzyme
NAME        2-acylglycerol-3-phosphate O-acyltransferase;
            2-acylglycerophosphate acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:2-acyl-sn-glycerol 3-phosphate O-acyltransferase
REACTION    acyl-CoA + 2-acyl-sn-glycerol 3-phosphate = CoA +
            1,2-diacyl-sn-glycerol 3-phosphate [RN:R02242]
ALL_REAC    R02242
SUBSTRATE   acyl-CoA [CPD:C00040];
            2-acyl-sn-glycerol 3-phosphate [CPD:C03974]
PRODUCT     CoA [CPD:C00010];
            1,2-diacyl-sn-glycerol 3-phosphate [CPD:C00416]
COMMENT     Saturated acyl-CoA thioesters are the most effective acyl donors.
REFERENCE   1  [PMID:4774123]
  AUTHORS   Yamashita S, Hosaka K, Numa S.
  TITLE     Acyl-donor specificities of partially purified
            1-acylglycerophosphate acyltransferase, 2-acylglycerophosphate
            acyltransferase and 1-acylglycerophosphorylcholine acyltransferase
            from rat-liver microsomes.
  JOURNAL   Eur. J. Biochem. 38 (1973) 25-31.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.52
            ExPASy - ENZYME nomenclature database: 2.3.1.52
            ExplorEnz - The Enzyme Database: 2.3.1.52
            ERGO genome analysis and discovery system: 2.3.1.52
            BRENDA, the Enzyme Database: 2.3.1.52
            CAS: 51901-17-8
///
ENTRY       EC 2.3.1.53                 Enzyme
NAME        phenylalanine N-acetyltransferase;
            acetyl-CoA-L-phenylalanine alpha-N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:L-phenylalanine N-acetyltransferase
REACTION    acetyl-CoA + L-phenylalanine = CoA + N-acetyl-L-phenylalanine
            [RN:R00693]
ALL_REAC    R00693
SUBSTRATE   acetyl-CoA [CPD:C00024];
            L-phenylalanine [CPD:C00079]
PRODUCT     CoA [CPD:C00010];
            N-acetyl-L-phenylalanine [CPD:C03519]
COMMENT     Also acts, more slowly, on L-histidine and L-alanine.
REFERENCE   1  [PMID:5238989]
  AUTHORS   Leuzinger W, Baker AL, Cauvin E.
  TITLE     Acetylcholinesterase. II. Crystallization, absorption spectra,
            isoionic point.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 59 (1968) 620-3.
PATHWAY     PATH: map00360  Phenylalanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.53
            ExPASy - ENZYME nomenclature database: 2.3.1.53
            ExplorEnz - The Enzyme Database: 2.3.1.53
            ERGO genome analysis and discovery system: 2.3.1.53
            BRENDA, the Enzyme Database: 2.3.1.53
            CAS: 9075-16-5
///
ENTRY       EC 2.3.1.54                 Enzyme
NAME        formate C-acetyltransferase;
            pyruvate formate-lyase;
            pyruvic formate-lyase;
            formate acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:formate C-acetyltransferase
REACTION    acetyl-CoA + formate = CoA + pyruvate [RN:R00212]
ALL_REAC    R00212;
            (other) R06987
SUBSTRATE   acetyl-CoA [CPD:C00024];
            formate [CPD:C00058]
PRODUCT     CoA [CPD:C00010];
            pyruvate [CPD:C00022]
REFERENCE   1  [PMID:4615902]
  AUTHORS   Knappe J, Blaschkowski HP, Grobner P, Schmitt T.
  TITLE     Pyruvate formate-lyase of Escherichia coli: the acetyl-enzyme
            intermediate.
  JOURNAL   Eur. J. Biochem. 50 (1974) 253-63.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00620  Pyruvate metabolism
            PATH: map00640  Propanoate metabolism
            PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K00656  formate C-acetyltransferase
GENES       ECO: b0903(pflB) b3114(tdcE)
            ECJ: JW0807(ybiW) JW0886(pflB) JW3923(pflD) JW5522(tdcE)
            ECE: Z1046m Z1248(pflB) Z4466(tdcE) Z5507(pflD)
            ECS: ECs0986 ECs3994 ECs4880
            ECC: c0908(ybiW) c3872(tdcE) c4537 c4910(pflD)
            ECI: UTI89_C0826(ybiW) UTI89_C0974(pflB) UTI89_C3549(tdcE)
                 UTI89_C4542(pflD)
            ECP: ECP_0836 ECP_0914 ECP_4164 ECP_4600
            ECV: APECO1_2293 APECO1_3310(tdcE)
            ECW: EcE24377A_0894 EcE24377A_1000(pflB2) EcE24377A_3588(pflB1)
                 EcE24377A_4490
            ECX: EcHS_A0881 EcHS_A1009 EcHS_A3302 EcHS_A4185
            STY: STY0882(ybiW) STY0973(pflB) STY3423(tdcE)
            STT: t1961(pflB) t2046(ybiW) t3161(tdcE)
            SPT: SPA1825(pflB) SPA1912(ybiW) SPA3110(tdcE)
            SEC: SC0838(pflF) SC0927(pflB) SC3187(tdcE)
            STM: STM0843(pflF) STM0973(pflB) STM3241(tdcE) STM4114(pflD)
            YPE: YPO1383(pflB)
            YPK: y2790(pflB)
            YPM: YP_1210(pflB)
            YPA: YPA_0674
            YPN: YPN_2594
            YPP: YPDSF_2312
            YPS: YPTB1408(pflB)
            YPI: YpsIP31758_2589(pflB)
            YEN: YE0646
            SFL: SF0773(ybiW) SF0898(pflB) SF3154(tdcE) SF4028(pflD)
            SFX: S0816(ybiW) S0962(pflB) S3366(tdcE) S3718(pflD)
            SFV: SFV_0806(ybiW) SFV_0903(pflB) SFV_3155(tdcE) SFV_4020(pflD)
            SSN: SSON_0805(ybiW) SSON_0904(pflB) SSON_3271(tdcE)
            SBO: SBO_0713(ybiW) SBO_2189(pflB) SBO_2979(tdcE) SBO_3970(pflD)
            SDY: SDY_0764(ybiW) SDY_2358(pflB) SDY_3306(tdcE) SDY_3786(pflD)
            ECA: ECA2597(pflB) ECA3768
            PLU: plu1613(pflB)
            SGL: SG0988
            ENT: Ent638_1317 Ent638_1423 Ent638_3561
            SPE: Spro_1702 Spro_2642
            HIT: NTHI0269(pflB)
            HDU: HD0990(pflB)
            HSO: HS_1136(pflB)
            PMU: PM0075(pflB)
            MSU: MS0401(pflD)
            APL: APL_1036(pflB)
            ASU: Asuc_0207
            VCH: VC1866
            VCO: VC0395_A1457(pflB)
            VVU: VV1_2098
            VVY: VV2342
            VPA: VP0994 VPA1567
            VFI: VF1590 VF2115 VFA0142
            PPR: PBPRA2750
            SON: SO_2912(pflB)
            SDN: Sden_2406
            SFR: Sfri_2473
            SAZ: Sama_1498
            SBL: Sbal_2671
            SBM: Shew185_2690
            SLO: Shew_2390
            SPC: Sputcn32_0208 Sputcn32_2378
            SSE: Ssed_1708
            SPL: Spea_1672
            SHE: Shewmr4_1494
            SHM: Shewmr7_1561
            SHN: Shewana3_1555
            SHW: Sputw3181_0427 Sputw3181_1631
            PIN: Ping_3307
            AHA: AHA_1330 AHA_1941(pflB) AHA_2856
            DNO: DNO_1334(pflB)
            CVI: CV_1412(pflB)
            DAR: Daro_2096
            GSU: GSU2101
            PCA: Pcar_0937 Pcar_1397
            DVU: DVU2272 DVU2824
            DVL: Dvul_0491 Dvul_0979
            DDE: Dde_1273 Dde_3039 Dde_3055 Dde_3282
            DPS: DP0616(pflD) DP1823 DP3027
            RPC: RPC_1080 RPC_1163 RPC_2980
            RPE: RPE_3101
            NHA: Nham_0889
            ZMO: ZMO1570(pfl)
            RRU: Rru_A0903 Rru_A3000
            BAN: BA0509(pfl)
            BAR: GBAA0509(pfl)
            BAA: BA_1080
            BAT: BAS0481
            BCE: BC0491
            BCA: BCE_0563(pfl)
            BCZ: BCZK0420(pflB)
            BCY: Bcer98_0431
            BTK: BT9727_0424(pflB)
            BTL: BALH_0446(pflB)
            BLI: BL01863
            BLD: BLi02132
            SAU: SA0218(pflB)
            SAV: SAV0226(pflB)
            SAM: MW0201(pflB)
            SAR: SAR0217
            SAS: SAS0201
            SAC: SACOL0204(pflB)
            SAB: SAB0164
            SAA: SAUSA300_0220(pflB)
            SAO: SAOUHSC_00187
            SAJ: SaurJH9_0210
            SAH: SaurJH1_0216
            SEP: SE0214
            SER: SERP2366(pflB)
            LMO: lmo1406(pflB) lmo1917(pflA)
            LMF: LMOf2365_1425(pfl-1) LMOf2365_1946(pfl-2)
            LIN: lin1443(pflB) lin2031(pflA)
            LWE: lwe1422(pflB) lwe1943
            LLA: L57408(pfl)
            LLC: LACR_0691
            LLM: llmg_0629(pfl)
            SPY: SPy_1849(pfl) SPy_2049(pflD)
            SPZ: M5005_Spy_1569(pfl) M5005_Spy_1743(pflD)
            SPM: spyM18_1912(pfl) spyM18_2110(pflD)
            SPG: SpyM3_1596(pfl) SpyM3_1749(pflD)
            SPS: SPs0271 SPs1747
            SPH: MGAS10270_Spy1636(pfl) MGAS10270_Spy1812(pflD)
            SPI: MGAS10750_Spy1628(pfl) MGAS10750_Spy1837(pflD)
            SPJ: MGAS2096_Spy1594(pfl) MGAS2096_Spy1777(pflD)
            SPK: MGAS9429_Spy1574(pfl) MGAS9429_Spy1752 MGAS9429_Spy1753(pflD)
            SPF: SpyM50281(pfl) SpyM51706(pflD)
            SPA: M6_Spy1581 M6_Spy1743
            SPB: M28_Spy1557(pfl) M28_Spy1730(pflD)
            SPN: SP_0251 SP_0459
            SPR: spr0232(pflF) spr0415(pfl)
            SPD: SPD_0235(pfl) SPD_0420(pflB)
            SAG: SAG0331(pflD-1) SAG1727(pflD-2)
            SAN: gbs0319 gbs1772
            SAK: SAK_0401 SAK_1735(pflB)
            SMU: SMU.402(pfl) SMU.493(pfl2)
            STC: str1657(pfl)
            STL: stu1657(pfl)
            SSA: SSA_0285 SSA_0342
            SGO: SGO_0247(pfl) SGO_1788
            LPL: lp_2598(pflB1) lp_3313(pflB2)
            LSA: LSA0974(pflB)
            LSL: LSL_1873(pflD)
            LCA: LSEI_1410
            EFA: EF1613(pflB)
            STH: STH115
            CAC: CAC0980(pflB)
            CPE: CPE1153(pflA)
            CPF: CPF_1356(pfl)
            CPR: CPR_1169(pfl)
            CTC: CTC00936 CTC01449
            CNO: NT01CX_0015(pflB) NT01CX_0385 NT01CX_0498 NT01CX_1220
            CTH: Cthe_0505
            CDF: CD0759(plfB) CD3282(pflD)
            CBO: CBO3183 CBO3216(pflA)
            CBA: CLB_2055 CLB_3219 CLB_3252(pfl)
            CBH: CLC_2060 CLC_3093 CLC_3126(pfl)
            CBF: CLI_2161 CLI_3322 CLI_3354(pfl)
            CBE: Cbei_0315 Cbei_0705 Cbei_1009 Cbei_1011 Cbei_4061
            CKL: CKL_1107(pfl)
            AMT: Amet_0506 Amet_0584 Amet_1986 Amet_2211 Amet_3836
            DSY: DSY0416 DSY3016 DSY5006
            DRM: Dred_0039 Dred_2750 Dred_2753 Dred_2965 Dred_3278
            SWO: Swol_1048
            CMI: CMM_1875
            BLO: BL0951(pfl)
            BAD: BAD_0992(pfl)
            FNU: FN0262
            CYA: CYA_0477(pflB)
            CYB: CYB_0245(pflB)
            TEL: tll0990
            GVI: glr3745
            BTH: BT_2955 BT_4738
            BFR: BF1339 BF4383
            BFS: BF1323(pflB) BF4181(pflD)
            TKO: TK0289
STRUCTURES  PDB: 1CM5  1H16  1H17  1H18  1MZO  1QHM  2PFL  3PFL  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.54
            ExPASy - ENZYME nomenclature database: 2.3.1.54
            ExplorEnz - The Enzyme Database: 2.3.1.54
            ERGO genome analysis and discovery system: 2.3.1.54
            BRENDA, the Enzyme Database: 2.3.1.54
            CAS: 9068-08-0
///
ENTRY       EC 2.3.1.55       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
COMMENT     Deleted entry: kanamycin 6'-N-acetyltransferase identical to EC
            2.3.1.82 aminoglycoside N6'-acetyltransferase (EC 2.3.1.55 created
            1976, deleted 1999)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.55
            ExPASy - ENZYME nomenclature database: 2.3.1.55
            ExplorEnz - The Enzyme Database: 2.3.1.55
            ERGO genome analysis and discovery system: 2.3.1.55
            BRENDA, the Enzyme Database: 2.3.1.55
///
ENTRY       EC 2.3.1.56                 Enzyme
NAME        aromatic-hydroxylamine O-acetyltransferase;
            aromatic hydroxylamine acetyltransferase;
            arylhydroxamate acyltransferase;
            arylhydroxamate N,O-acetyltransferase;
            arylhydroxamic acid N,O-acetyltransferase;
            arylhydroxamic acyltransferase;
            N,O-acetyltransferase;
            N-hydroxy-2-acetylaminofluorene N-O acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     N-hydroxy-4-acetylaminobiphenyl:N-hydroxy-4-aminobiphenyl
            O-acetyltransferase
REACTION    N-hydroxy-4-acetylaminobiphenyl + N-hydroxy-4-aminobiphenyl =
            N-hydroxy-4-aminobiphenyl + N-acetoxy-4-aminobiphenyl [RN:R04271]
ALL_REAC    R04271
SUBSTRATE   N-hydroxy-4-acetylaminobiphenyl [CPD:C04081];
            N-hydroxy-4-aminobiphenyl [CPD:C03622]
PRODUCT     N-hydroxy-4-aminobiphenyl [CPD:C03622];
            N-acetoxy-4-aminobiphenyl [CPD:C03621]
COMMENT     Transfers the N-acetyl group of some aromatic acethydroxamates to
            the O-position of some aromatic hydroxylamines.
REFERENCE   1  [PMID:4699998]
  AUTHORS   Bartsch H, Dworkin C, Miller EC, Miller JA.
  TITLE     Formation of electrophilic N-acetoxyarylamines in cytosoles from rat
            mammary gland and other tissues by transacetylation from the
            carcinogen N-hydroxy-4-acetylaminobiphenyl.
  JOURNAL   Biochim. Biophys. Acta. 304 (1973) 42-55.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.56
            ExPASy - ENZYME nomenclature database: 2.3.1.56
            ExplorEnz - The Enzyme Database: 2.3.1.56
            ERGO genome analysis and discovery system: 2.3.1.56
            BRENDA, the Enzyme Database: 2.3.1.56
            CAS: 52660-15-8
///
ENTRY       EC 2.3.1.57                 Enzyme
NAME        diamine N-acetyltransferase;
            spermidine acetyltransferase;
            putrescine acetyltransferase;
            putrescine (diamine)-acetylating enzyme;
            diamine acetyltransferase;
            spermidine/spermine N1-acetyltransferase;
            spermidine N1-acetyltransferase;
            acetyl-coenzyme A-1,4-diaminobutane N-acetyltransferase;
            putrescine acetylase;
            putrescine N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:alkane-alpha,omega-diamine N-acetyltransferase
REACTION    acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an
            N-acetyldiamine [RN:R03910]
ALL_REAC    R03910 > R01154
SUBSTRATE   acetyl-CoA [CPD:C00024];
            alkane-alpha,omega-diamine [CPD:C03687]
PRODUCT     CoA [CPD:C00010];
            N-acetyldiamine [CPD:C02297]
COMMENT     Acts on propane-1,3-diamine, pentane-1,5-diamine, putrescine,
            spermidine (forming N1- and N8-acetylspermidine), spermine,
            N1-acetylspermidine and N8-acetylspermidine.
REFERENCE   1  [PMID:7150547]
  AUTHORS   Ragione FD, Pegg AE.
  TITLE     Purification and characterization of spermidine/spermine
            N1-acetyltransferase from rat liver.
  JOURNAL   Biochemistry. 21 (1982) 6152-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K00657  diamine N-acetyltransferase
GENES       HSA: 112483(SAT2) 6303(SAT1)
            PTR: 455216(SAT2) 465538(SAT1)
            MMU: 20229(Sat1) 69215(Sat2)
            CFA: 479486(SAT2) 480865(SAT1)
            BTA: 359722(SSAT2)
            SSC: 397645(SAT)
            GGA: 374006(SAT1)
            XLA: 447322(MGC82057)
            XTR: 493359(TGas043d12.1)
            SPU: 591752(LOC591752)
            ECO: b1584(speG)
            ECJ: JW1576(speG)
            ECE: Z2571(speG)
            ECS: ECs2290
            ECC: c1974(speG)
            ECI: UTI89_C1771(speG)
            ECP: ECP_1532
            ECV: APECO1_667
            ECW: EcE24377A_1791(speG)
            ECX: EcHS_A1657(speG)
            STY: STY1561(speG)
            STT: t1423(speG)
            SPT: SPA1353(speG)
            SEC: SC1519(speG)
            STM: STM1502(speG)
            YPE: YPO2830(speG)
            YPK: y1405(speG)
            YPM: YP_2698(speG)
            YPA: YPA_2267
            YPN: YPN_1308
            YPP: YPDSF_3916
            YPS: YPTB2797(speG)
            YPI: YpsIP31758_1232(speG)
            SFV: SFV_3756(glmU)
            ECA: ECA4509(glmU)
            PLU: plu2762(speG) plu3536
            WBR: WGpWb0002
            SGL: SG1899
            VCH: VCA0947
            VCO: VC0395_0291(speG)
            VPA: VPA0474
            VFI: VFA0385
            PAE: PA4114
            PAU: PA14_10740 PA14_73220(glmU)
            PAR: Psyc_2073(glmU)
            ACI: ACIAD3575(glmU)
            ILO: IL2617(glmU)
            CBU: CBU_1678(speG)
            CBD: COXBU7E912_0323(speG)
            FTU: FTT0387(glmU)
            FTF: FTF0387(glmU)
            FTN: FTN_0484(glmU)
            ABO: ABO_2330 ABO_2724(glmU)
            AHA: AHA_2716
            NMC: NMC0015(glmU)
            BXE: Bxe_A4477
            BUR: Bcep18194_A5735 Bcep18194_A6513
            BCH: Bcen2424_3157
            BAM: Bamb_3209
            BPS: BPSL0096(speG)
            BPM: BURPS1710b_0317(speG)
            BPL: BURPS1106A_0126(speG)
            BPD: BURPS668_0111(speG)
            BTE: BTH_I0081(speG)
            MMS: mma_3441(glmU)
            AZO: azo3637(glmU)
            MFA: Mfla_1085
            CCV: CCV52592_2131
            BBA: Bd3425(glmU)
            MLO: mlr1969
            BRA: BRADO3760(glmU) BRADO5577
            BBT: BBta_4168(glmU) BBta_6099
            RSP: RSP_2503(glmU)
            GOX: GOX0006(glmU)
            GBE: GbCGDNIH1_1186
            BSU: BG10906(bltD)
            BAN: BA2022 BA2675(bltD) BA3295 BA5323(speG)
            BAR: GBAA2022 GBAA2675(bltD) GBAA3295 GBAA5323(speG)
            BAA: BA_0183 BA_2526 BA_3191
            BAT: BAS1880 BAS2491 BAS3058 BAS4945
            BCE: BC2020 BC2684 BC5073
            BCA: BCE_2102 BCE_2712(bltD) BCE_5220(speG)
            BCZ: BCZK1834(bltD) BCZK2422(bltD) BCZK4806(speG)
            BTK: BT9727_1850(bltD) BT9727_2451(bltD) BT9727_2968(bltD)
                 BT9727_4788(speG)
            BTL: BALH_1792(bltD) BALH_2397(bltD) BALH_2409(bltD)
                 BALH_4612(speG)
            BLI: BL03216
            BLD: BLi02012
            BAY: RBAM_006040(bltD)
            OIH: OB1723
            SAA: SAUSA300_0053(speG)
            SEP: SE0026 SE0046
            SER: SERP0118 SERP2470
            SHA: SH2531
            SSP: SSP1043
            LMO: lmo0009 lmo2400
            LMF: LMOf2365_0009(speG) LMOf2365_2374
            LIN: lin0009 lin2499
            LWE: lwe0009(speG) lwe2347 lwe2607
            LLA: L56232(yqfF)
            LLC: LACR_1724
            LLM: llmg_0879(speG)
            SPN: SP_1019
            SPR: spr0923(bltD)
            LJO: LJ1226
            EFA: EF1086
            OOE: OEOE_0717
            CDF: CD1212(bltD)
            CBF: CLI_1999(bltD)
            NFA: nfa22170 nfa27360
            TWH: TWT188
            TWS: TW584
            FNU: FN1057
            TDE: TDE0542 TDE0808
            PMB: A9601_06671(glmU)
            PMC: P9515_06761(glmU)
            PMF: P9303_18871(glmU)
            PMG: P9301_06371(glmU)
            PMH: P9215_06931(glmU)
            BTH: BT_1079
            BFR: BF2055
            BFS: BF2108
            PGI: PG1254
            SRU: SRU_2319
            AAE: aq_1966
            MMA: MM_0180
STRUCTURES  PDB: 2B3U  2B3V  2B4B  2B4D  2B58  2B5G  2BEI  2F5I  2FXF  2G3T  
                 2JEV  2Q4V  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.57
            ExPASy - ENZYME nomenclature database: 2.3.1.57
            ExplorEnz - The Enzyme Database: 2.3.1.57
            ERGO genome analysis and discovery system: 2.3.1.57
            BRENDA, the Enzyme Database: 2.3.1.57
            CAS: 54596-36-0
///
ENTRY       EC 2.3.1.58                 Enzyme
NAME        2,3-diaminopropionate N-oxalyltransferase;
            oxalyldiaminopropionate synthase;
            ODAP synthase;
            oxalyl-CoA:L-alpha,beta-diaminopropionic acid oxalyltransferase;
            oxalyldiaminopropionic synthase;
            oxalyl-CoA:L-2,3-diaminopropanoate 3-N-oxalyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     oxalyl-CoA:L-2,3-diaminopropanoate N3-oxalyltransferase
REACTION    oxalyl-CoA + L-2,3-diaminopropanoate = CoA +
            N3-oxalyl-L-2,3-diaminopropanoate [RN:R04211]
ALL_REAC    R04211
SUBSTRATE   oxalyl-CoA [CPD:C00313];
            L-2,3-diaminopropanoate [CPD:C03401]
PRODUCT     CoA [CPD:C00010];
            N3-oxalyl-L-2,3-diaminopropanoate [CPD:C04209]
REFERENCE   1
  AUTHORS   Malathi, K., Padmanaban, G. and Sarma, P.S.
  TITLE     Biosynthesis of beta-N-oxalyl-L-alpha,beta-diaminopropionic acid,
            the Lathyrus sativus neurotoxin.
  JOURNAL   Phytochemistry 9 (1970) 1603-1610.
  ORGANISM  Lathyrus sativus
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.58
            ExPASy - ENZYME nomenclature database: 2.3.1.58
            ExplorEnz - The Enzyme Database: 2.3.1.58
            ERGO genome analysis and discovery system: 2.3.1.58
            BRENDA, the Enzyme Database: 2.3.1.58
            CAS: 62213-48-3
///
ENTRY       EC 2.3.1.59                 Enzyme
NAME        gentamicin 2'-N-acetyltransferase;
            gentamycin acetyltransferase II;
            gentamycin 2'-N-acetyltransferase;
            acetyl-CoA:gentamycin-C1a N2'-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:gentamicin-C1a N2'-acetyltransferase
REACTION    acetyl-CoA + gentamicin C1a = CoA + N2'-acetylgentamicin C1a
            [RN:R03056]
ALL_REAC    R03056
SUBSTRATE   acetyl-CoA [CPD:C00024];
            gentamicin C1a [CPD:C00908]
PRODUCT     CoA [CPD:C00010];
            N2'-acetylgentamicin C1a [CPD:C03524]
COMMENT     The antibiotics gentamicin A, sisomicin, tobramycin, paromomycin,
            neomycin B, kanamycin B and kanamycin C can also act as acceptors.
REFERENCE   1  [PMID:4209515]
  AUTHORS   Benveniste R, Davies J.
  TITLE     Aminoglycoside antibiotic-inactivating enzymes in actinomycetes
            similar to those present in clinical isolates of
            antibiotic-resistant bacteria.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 70 (1973) 2276-80.
  ORGANISM  Streptomyces kanamyceticus
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.59
            ExPASy - ENZYME nomenclature database: 2.3.1.59
            ExplorEnz - The Enzyme Database: 2.3.1.59
            ERGO genome analysis and discovery system: 2.3.1.59
            BRENDA, the Enzyme Database: 2.3.1.59
            CAS: 50864-40-9
///
ENTRY       EC 2.3.1.60                 Enzyme
NAME        gentamicin 3'-N-acetyltransferase;
            gentamycin acetyltransferase I;
            aminoglycoside acetyltransferase AAC(3)-1;
            gentamycin 3'-N-acetyltransferase;
            acetyl-CoA:gentamycin-C N3'-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:gentamicin-C N3'-acetyltransferase
REACTION    acetyl-CoA + gentamicin C = CoA + N3'-acetylgentamicin C [RN:R03767]
ALL_REAC    R03767
SUBSTRATE   acetyl-CoA [CPD:C00024];
            gentamicin C [CPD:C01918]
PRODUCT     CoA [CPD:C00010];
            N3'-acetylgentamicin C [CPD:C03297]
COMMENT     Also acetylates sisomicin.
REFERENCE   1  [PMID:6281224]
  AUTHORS   Angelatou F, Litsas SB, Kontomichalou P.
  TITLE     Purification and properties of two gentamicin-modifying enzymes,
            coded by a single plasmid pPK237 originating from Pseudomonas
            aeruginosa.
  JOURNAL   J. Antibiot. (Tokyo). 35 (1982) 235-44.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   2  [PMID:820250]
  AUTHORS   Biddlecome S, Haas M, Davies J, Miller GH, Rane DF, Daniels PJ.
  TITLE     Enzymatic modification of aminoglycoside antibiotics: a new
            3-N-acetylating enzyme from a Pseudomonas aeruginosa isolate.
  JOURNAL   Antimicrob. Agents. Chemother. 9 (1976) 951-5.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   3  [PMID:764855]
  AUTHORS   Williams JW, Northrop DB.
  TITLE     Purification and properties of gentamicin acetyltransferase I.
  JOURNAL   Biochemistry. 15 (1976) 125-31.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K03395  gentamicin 3'-N-acetyltransferase
GENES       PMY: Pmen_3087
            PDE: Pden_3159 Pden_3355
            SAL: Sala_0626
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.60
            ExPASy - ENZYME nomenclature database: 2.3.1.60
            ExplorEnz - The Enzyme Database: 2.3.1.60
            ERGO genome analysis and discovery system: 2.3.1.60
            BRENDA, the Enzyme Database: 2.3.1.60
            CAS: 58500-58-6
///
ENTRY       EC 2.3.1.61                 Enzyme
NAME        dihydrolipoyllysine-residue succinyltransferase;
            dihydrolipoamide S-succinyltransferase;
            dihydrolipoamide succinyltransferase;
            dihydrolipoic transsuccinylase;
            dihydrolipolyl transsuccinylase;
            dihydrolipoyl transsuccinylase;
            lipoate succinyltransferase (Escherichia coli);
            lipoic transsuccinylase;
            lipoyl transsuccinylase;
            succinyl-CoA:dihydrolipoamide S-succinyltransferase;
            succinyl-CoA:dihydrolipoate S-succinyltransferase;
            enzyme-dihydrolipoyllysine:succinyl-CoA S-succinyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     succinyl-CoA:enzyme-N6-(dihydrolipoyl)lysine S-succinyltransferase
REACTION    succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme
            N6-(S-succinyldihydrolipoyl)lysine [RN:R02570]
ALL_REAC    R02570;
            (other) R02571
SUBSTRATE   succinyl-CoA [CPD:C00091];
            enzyme N6-(dihydrolipoyl)lysine [CPD:C15973]
PRODUCT     CoA [CPD:C00010];
            enzyme N6-(S-succinyldihydrolipoyl)lysine
COMMENT     A multimer (24-mer) of this enzyme forms the core of the multienzyme
            complex, and binds tightly both EC 1.2.4.2, oxoglutarate
            dehydrogenase (succinyl-transferring) and EC 1.8.1.4, dihydrolipoyl
            dehydrogenase. The lipoyl group of this enzyme is reductively
            succinylated by EC 1.2.4.2, and the only observed direction
            catalysed by EC 2.3.1.61 is that where this succinyl group is passed
            to coenzyme A.
REFERENCE   1  [PMID:4942179]
  AUTHORS   Derosier DJ, Oliver RM, Reed LJ.
  TITLE     Crystallization and preliminary structural analysis of dihydrolipoyl
            transsuccinylase, the core of the 2-oxoglutarate dehydrogenase
            complex.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 68 (1971) 1135-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Reed, L.J. and Cox, D.J.
  TITLE     Multienzyme complexes.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 1, Academic Press,
            New York, 1970, p. 213-240.
REFERENCE   3  [PMID:9677295]
  AUTHORS   Knapp JE, Mitchell DT, Yazdi MA, Ernst SR, Reed LJ, Hackert ML.
  TITLE     Crystal structure of the truncated cubic core component of the
            Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex.
  JOURNAL   J. Mol. Biol. 280 (1998) 655-68.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:10966480]
  AUTHORS   Perham RN.
  TITLE     Swinging arms and swinging domains in multifunctional enzymes:
            catalytic machines for multistep reactions.
  JOURNAL   Annu. Rev. Biochem. 69 (2000) 961-1004.
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K00658  2-oxoglutarate dehydrogenase E2 component
                        (dihydrolipoamide succinyltransferase)
GENES       HSA: 1743(DLST)
            PTR: 453039(DLST)
            MMU: 78920(Dlst)
            CFA: 480388(DLST)
            SSC: 397690(DLST)
            GGA: 423357(RCJMB04_39i8)
            XLA: 380395(dlst)
            XTR: 448316(MGC89125)
            DRE: 368262(dlst)
            SPU: 576084(LOC576084)
            DME: Dmel_CG5214
            CEL: W02F12.5
            ATH: AT5G55070
            OSA: 4335689
            CME: CMJ055C
            SCE: YDR148C(KGD2)
            AGO: AGOS_AGL200W
            PIC: PICST_68297(KGD2)
            CGR: CAGL0E01287g
            SPO: SPBC776.15c
            ANI: AN3466.2
            AFM: AFUA_3G05370
            AOR: AO090005001174 AO090020000008
            CNE: CNB00990
            UMA: UM01517.1
            DDI: DDB_0230198(odhB)
            PFA: PF13_0121
            TAN: TA19690
            TPV: TP01_0262
            TET: TTHERM_00105450
            TBR: Tb11.01.3550
            TCR: 503935.20 506025.60
            LMA: LmjF28.2420
            ECO: b0727(sucB)
            ECJ: JW0716(sucB)
            ECE: Z0881(sucB)
            ECS: ECs0752
            ECC: c0804(sucB) c5034
            ECI: UTI89_C0722(sucB) UTI89_C4632
            ECP: ECP_0738 ECP_4275
            ECV: APECO1_1352(sucB) APECO1_2409
            ECW: EcE24377A_0753(sucB)
            ECX: EcHS_A0774(sucB)
            STY: STY0780(sucB)
            STT: t2139(sucB)
            SPT: SPA2006(sucB)
            SEC: SC0741(sucB)
            STM: STM0737(sucB)
            YPE: YPO1114(sucB)
            YPK: y3066(sucB)
            YPM: YP_1042(sucB)
            YPA: YPA_0592
            YPN: YPN_2884
            YPP: YPDSF_2936
            YPS: YPTB1148(sucB)
            YPI: YpsIP31758_2880(sucB)
            SFL: SF0570(sucB)
            SFX: S0583(sucB)
            SFV: SFV_0609(sucB)
            SSN: SSON_0678(sucB)
            SBO: SBO_0585(sucB)
            SDY: SDY_0665(sucB)
            ECA: ECA1362(sucB)
            PLU: plu1431(sucB)
            BUC: BU303(sucB)
            BAS: BUsg293(sucB)
            BAB: bbp281(sucB)
            BCC: BCc_185(sucB)
            WBR: WGLp418(sucB)
            SGL: SG0877
            ENT: Ent638_0661
            SPE: Spro_4010
            BFL: Bfl332(sucB)
            BPN: BPEN_342(sucB)
            HIT: NTHI1963(sucB)
            HDU: HD1334(sucB)
            HSO: HS_0958(sucB)
            PMU: PM0278(sucB)
            MSU: MS1354(aceF)
            APL: APL_0454(sucB)
            ASU: Asuc_0943
            XFA: XF1549
            XFT: PD0759(sucB)
            XCC: XCC1486(sucB)
            XCB: XC_2750
            XCV: XCV1577(sucB)
            XAC: XAC1534(sucB)
            XOO: XOO2043(sucB)
            XOM: XOO_1924(XOO1924)
            VCH: VC2086
            VCO: VC0395_A1672(sucB)
            VVU: VV1_0156
            VVY: VV1033
            VPA: VP0848
            VFI: VF0824
            PPR: PBPRA1049(sucB)
            PAE: PA1586(sucB)
            PAU: PA14_44000(sucB)
            PAP: PSPA7_3688(sucB)
            PPU: PP_4188(kgdB)
            PPF: Pput_0363
            PST: PSPTO_2200(sucB)
            PSB: Psyr_2010
            PSP: PSPPH_1981(sucB)
            PFL: PFL_1719(sucB)
            PFO: Pfl_1615
            PEN: PSEEN3639(sucB) PSEEN5146(aceF)
            PMY: Pmen_0575
            PAR: Psyc_0103(sucB)
            PCR: Pcryo_0112
            PRW: PsycPRwf_1403
            ACI: ACIAD2875(sucB)
            SON: SO_1931(sucB)
            SDN: Sden_2182 Sden_3382
            SFR: Sfri_2342 Sfri_3776
            SAZ: Sama_0376 Sama_1428
            SBL: Sbal_3912
            SBM: Shew185_3933
            SLO: Shew_3430
            SPC: Sputcn32_3416
            SSE: Ssed_0432
            SPL: Spea_0420
            SHE: Shewmr4_0429 Shewmr4_1636
            SHM: Shewmr7_1711 Shewmr7_3598
            SHN: Shewana3_1711
            SHW: Sputw3181_0527
            ILO: IL1502(sucB)
            CPS: CPS_2220(sucB)
            PHA: PSHAa1646(sucB)
            PAT: Patl_1800 Patl_3351
            SDE: Sde_2105
            PIN: Ping_2926(sucB)
            MAQ: Maqu_1155 Maqu_3327
            CBU: CBU_1398(sucB)
            CBD: COXBU7E912_0595(sucB)
            LPN: lpg0533(sucB)
            LPF: lpl0579(sucB)
            LPP: lpp0598(sucB)
            MCA: MCA1953(sucB)
            FTU: FTT0077(sucB)
            FTF: FTF0077(sucB)
            FTW: FTW_0153(sucB)
            FTL: FTL_1783
            FTH: FTH_1719(sucB)
            FTA: FTA_1889(sucB)
            FTN: FTN_1634(sucB)
            NOC: Noc_0112 Noc_2109
            AEH: Mlg_0270 Mlg_2608
            HCH: HCH_04744(sucB2)
            CSA: Csal_1218
            ABO: ABO_1495(sucB)
            MMW: Mmwyl1_2306 Mmwyl1_2799
            AHA: AHA_1928(sucB)
            DNO: DNO_0331(sucB)
            NME: NMB0956
            NMA: NMA1150(sucB)
            NMC: NMC0932(sucB)
            NGO: NGO0916
            CVI: CV_1072(sucB)
            RSO: RSc1270(sucB)
            REU: Reut_A2046
            REH: H16_A2324(odhB)
            RME: Rmet_2049
            BMA: BMA1051(sucB)
            BMV: BMASAVP1_A1497(sucB)
            BML: BMA10299_A0165(sucB)
            BMN: BMA10247_1001(sucB)
            BXE: Bxe_A2811
            BVI: Bcep1808_2216
            BUR: Bcep18194_A4650 Bcep18194_A5442
            BCN: Bcen_1029 Bcen_5941
            BCH: Bcen2424_1509 Bcen2424_2136
            BAM: Bamb_1391
            BPS: BPSL1908(sucB)
            BPM: BURPS1710b_1925(sucB)
            BPL: BURPS1106A_1773(sucB)
            BPD: BURPS668_1751(sucB)
            BTE: BTH_I2555(sucB)
            PNU: Pnuc_0735
            BPE: BP1125(odhB)
            BPA: BPP3216(odhB)
            BBR: BB3668(odhB)
            RFR: Rfer_2320
            POL: Bpro_2623
            PNA: Pnap_1782
            AJS: Ajs_2124
            MPT: Mpe_A2012
            HAR: HEAR1771(sucB)
            MMS: mma_1513(sucB)
            NEU: NE2375(sucB)
            NET: Neut_0859
            NMU: Nmul_A0856
            EBA: ebA6684(sucB)
            AZO: azo1556(odhB)
            DAR: Daro_2858
            TBD: Tbd_1189
            GSU: GSU2448(sucB)
            GME: Gmet_2766
            PCA: Pcar_2941
            BBA: Bd2729(sucB)
            ADE: Adeh_0782 Adeh_2131
            AFW: Anae109_4127
            MXA: MXAN_6036(sucB)
            SFU: Sfum_3548
            RPR: RP179
            RTY: RT0170(sucB)
            RCO: RC0226(sucB)
            RFE: RF_1093(sucB)
            RBE: RBE_1098(sucB)
            RAK: A1C_01295
            RBO: A1I_01835
            RCM: A1E_00955
            RRI: A1G_01290
            OTS: OTBS_1491(sucB)
            WOL: WD0544(sucB)
            WBM: Wbm0108
            AMA: AM1087(sucB)
            APH: APH_1198(sucB)
            ERU: Erum8200(sucB)
            ERW: ERWE_CDS_08690(sucB)
            ERG: ERGA_CDS_08590(sucB)
            ECN: Ecaj_0857
            ECH: ECH_1065(sucB)
            NSE: NSE_0548(sucB)
            PUB: SAR11_0236(sucB)
            MLO: mll4300
            MES: Meso_3399
            PLA: Plav_3139
            SME: SMb20019(sucB) SMc02483(sucB)
            SMD: Smed_1078 Smed_4111
            ATU: Atu2635(sucB)
            ATC: AGR_C_4775
            RET: RHE_CH03887(sucB)
            RLE: RL4433(citM)
            BME: BMEI0141
            BMF: BAB1_1922(sucB)
            BMS: BR1922(sucB)
            BMB: BruAb1_1898(sucB)
            BOV: BOV_1851(sucB)
            OAN: Oant_2061
            BJA: bll0451(sucB)
            BRA: BRADO0407(sucB)
            BBT: BBta_0396(sucB)
            RPA: RPA0188(sucB)
            RPB: RPB_0277 RPB_2768
            RPC: RPC_0190 RPC_2492
            RPD: RPD_0545 RPD_2809
            RPE: RPE_0296 RPE_2616
            NWI: Nwi_0423 Nwi_1816 Nwi_1817
            NHA: Nham_0541 Nham_1751
            BHE: BH16530(sucB)
            BQU: BQ13410(sucB)
            BBK: BARBAKC583_0026(sucB)
            XAU: Xaut_3891
            CCR: CC_0340
            SIL: SPO0343(sucB)
            SIT: TM1040_1077 TM1040_3510
            RSP: RSP_0964(sucB)
            RSH: Rsph17029_1147
            RSQ: Rsph17025_0076 Rsph17025_1092
            JAN: Jann_0832 Jann_1688
            RDE: RD1_1608(sucB)
            PDE: Pden_1603 Pden_3890
            MMR: Mmar10_2816
            HNE: HNE_0313(sucB)
            NAR: Saro_1179 Saro_1946
            SAL: Sala_1235 Sala_2227
            SWI: Swit_1367
            ELI: ELI_08005
            GOX: GOX1073
            GBE: GbCGDNIH1_2067
            ACR: Acry_2821
            RRU: Rru_A1214 Rru_A1879
            MAG: amb3962
            MGM: Mmc1_2396
            ABA: Acid345_4350
            SUS: Acid_0914
            BSU: BG10273(odhB)
            BHA: BH2205
            BAN: BA1269(odhB)
            BAR: GBAA1269(odhB)
            BAA: BA_1801
            BAT: BAS1176
            BCE: BC1251
            BCA: BCE_1379(odhB)
            BCZ: BCZK1151(odhB)
            BTK: BT9727_1157(odhB)
            BLI: BL01453(odhB)
            BLD: BLi02259(odhB)
            BCL: ABC2113(odhB)
            BAY: RBAM_019120
            BPU: BPUM_1861
            OIH: OB1090
            GKA: GK1024
            SAU: SA1244(odhB)
            SAV: SAV1412(odhB)
            SAM: MW1302(odhB)
            SAR: SAR1424(odhB)
            SAS: SAS1355
            SAC: SACOL1448(sucB)
            SAB: SAB1268c(odhB)
            SAA: SAUSA300_1305(sucB)
            SAO: SAOUHSC_01416
            SAJ: SaurJH9_1155
            SAH: SaurJH1_1177
            SEP: SE1096
            SER: SERP0985(sucB)
            SHA: SH1493(odhB)
            SSP: SSP1326
            LRE: Lreu_0633
            MMO: MMOB5810(pdhC) MMOB5820(pdhC)
            MTU: Rv2215(dlaT)
            MTC: MT2272
            MBO: Mb2238(dlaT)
            MBB: BCG_2231(dlaT)
            MLE: ML0861
            MPA: MAP1956(sucB)
            MAV: MAV_2273(sucB)
            MSM: MSMEG_4283(sucB)
            CGL: NCgl2126(cgl2207)
            CGB: cg2421(sucB)
            CEF: CE2098
            CDI: DIP1002(kgd) DIP1639(pdhC)
            CJK: jk0707(sucB)
            NFA: nfa16900(sucB)
            RHA: RHA1_ro00543 RHA1_ro01151 RHA1_ro06012(odhA)
                 RHA1_ro11029(sucB)
            SCO: SCO2181(SC5F7.20) SCO7123(SC4B10.24c)
            SMA: SAV6022(sucB)
            TWH: TWT503(sucB)
            TWS: TW259
            LXX: Lxx10140(pdhB)
            PAC: PPA0693
            TFU: Tfu_0993
            FRA: Francci3_3135
            FAL: FRAAL3041 FRAAL3226 FRAAL5152(sucB) FRAAL5981(sucA)
            ACE: Acel_0935
            KRA: Krad_3279
            SEN: SACE_1638(sucB)
            STP: Strop_3320
            RXY: Rxyl_2534
            RBA: RB9215(sucB)
            CTR: CT055(sucB_1) CT400(sucB_2)
            CTA: CTA_0059(sucB_1) CTA_0435(sucB_2)
            CMU: TC0325 TC0680
            CPN: CPn0377(sucB_1) CPn0527(sucB_2)
            CPA: CP0225 CP0379
            CPJ: CPj0377(sucB_1) CPj0527(sucB_2)
            CPT: CpB0389 CpB0548
            CCA: CCA00218 CCA00421(sucB)
            CAB: CAB214 CAB407(sucB)
            CFE: CF0586(sucB1) CF0789(sucB2)
            PCU: pc1089(sucB)
            LIL: LA1222(sucB)
            LIC: LIC12476(sucB)
            LBJ: LBJ_2125(aceF)
            LBL: LBL_2122(aceF)
            AVA: Ava_3176
            PMB: A9601_04551(pdhC)
            PMC: P9515_04661(pdhC)
            PMF: P9303_21291(pdhC)
            PMG: P9301_04241(pdhC)
            PMH: P9215_04811
            PME: NATL1_04561(pdhC)
            TER: Tery_1831
            CHU: CHU_3361(sucB)
            GFO: GFO_3082(sucB)
            FJO: Fjoh_1552
            FPS: FP2409(sucB)
            RRS: RoseRS_1726
            RCA: Rcas_2011
            DRA: DR_0083
            DGE: Dgeo_0139
            TTH: TTC1699
            TTJ: TTHA0288
STRUCTURES  PDB: 1BAL  1BBL  1C4T  1E2O  1GHJ  1GHK  1PMR  1SCZ  2BTG  2BTH  
                 2CYU  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.61
            ExPASy - ENZYME nomenclature database: 2.3.1.61
            ExplorEnz - The Enzyme Database: 2.3.1.61
            ERGO genome analysis and discovery system: 2.3.1.61
            BRENDA, the Enzyme Database: 2.3.1.61
            CAS: 9032-28-4
///
ENTRY       EC 2.3.1.62                 Enzyme
NAME        2-acylglycerophosphocholine O-acyltransferase;
            2-acylglycerol-3-phosphorylcholine acyltransferase;
            2-acylglycerophosphocholine acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:2-acyl-sn-glycero-3-phosphocholine O-acyltransferase
REACTION    acyl-CoA + 2-acyl-sn-glycero-3-phosphocholine = CoA +
            phosphatidylcholine [RN:R01319]
ALL_REAC    R01319
SUBSTRATE   acyl-CoA [CPD:C00040];
            2-acyl-sn-glycero-3-phosphocholine [CPD:C04233]
PRODUCT     CoA [CPD:C00010];
            phosphatidylcholine [CPD:C00157]
REFERENCE   1
  AUTHORS   Lands, W.E.M. and Hart, P.
  TITLE     Metabolism of glycerolipids. VI. Specificities of acyl coenzyme
            A:phospholipid acyltransferases.
  JOURNAL   J. Biol. Chem. 240 (1965) 1905-1911.
  ORGANISM  guinea pig, cow [GN:bta], pig [GN:ssc], rat [GN:rno]
REFERENCE   2  [PMID:5660084]
  AUTHORS   Van Den Bosch H, Van Golde MG, Slotboom AJ, Van Deenen LL.
  TITLE     The acylation of isomeric monoacyl phosphatidylcholines.
  JOURNAL   Biochim. Biophys. Acta. 152 (1968) 694-703.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.62
            ExPASy - ENZYME nomenclature database: 2.3.1.62
            ExplorEnz - The Enzyme Database: 2.3.1.62
            ERGO genome analysis and discovery system: 2.3.1.62
            BRENDA, the Enzyme Database: 2.3.1.62
            CAS: 64295-73-4
///
ENTRY       EC 2.3.1.63                 Enzyme
NAME        1-alkylglycerophosphocholine O-acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:1-alkyl-sn-glycero-3-phosphocholine O-acyltransferase
REACTION    acyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA +
            2-acyl-1-alkyl-sn-glycero-3-phosphocholine [RN:R03438]
ALL_REAC    R03438
SUBSTRATE   acyl-CoA [CPD:C00040];
            1-alkyl-sn-glycero-3-phosphocholine [CPD:C04317]
PRODUCT     CoA [CPD:C00010];
            2-acyl-1-alkyl-sn-glycero-3-phosphocholine [CPD:C05212]
COMMENT     May be identical with EC 2.3.1.23 1-acylglycerophosphocholine
            O-acyltransferase.
REFERENCE   1  [PMID:5488773]
  AUTHORS   Waku K, Nakazawa Y.
  TITLE     Acyltransferase activity to 1-O-alkyl-glycero-3-phosphorylcholine in
            sarcoplasmic reticulum.
  JOURNAL   J. Biochem. (Tokyo). 68 (1970) 459-66.
  ORGANISM  rabbit, human [GN:hsa]
REFERENCE   2  [PMID:4644313]
  AUTHORS   Waku K, Nakazawa Y.
  TITLE     Acyltransferae activity to 1-acyl-, 1-O-alkenyl-, and
            1-O-alkyl-glycero-3-phosphorylcholine in Ehrlich ascites tumor
            cells.
  JOURNAL   J. Biochem. (Tokyo). 72 (1972) 495-7.
  ORGANISM  rabbit
PATHWAY     PATH: map00565  Ether lipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.63
            ExPASy - ENZYME nomenclature database: 2.3.1.63
            ExplorEnz - The Enzyme Database: 2.3.1.63
            ERGO genome analysis and discovery system: 2.3.1.63
            BRENDA, the Enzyme Database: 2.3.1.63
            CAS: 58693-63-3
///
ENTRY       EC 2.3.1.64                 Enzyme
NAME        agmatine N4-coumaroyltransferase;
            p-coumaroyl-CoA-agmatine N-p-coumaroyltransferase;
            agmatine coumaroyltransferase;
            4-coumaroyl-CoA:agmatine 4-N-coumaroyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     4-coumaroyl-CoA:agmatine N4-coumaroyltransferase
REACTION    4-coumaroyl-CoA + agmatine = CoA +
            N-(4-guanidinobutyl)-4-hydroxycinnamamide [RN:R01617]
ALL_REAC    R01617
SUBSTRATE   4-coumaroyl-CoA [CPD:C00223];
            agmatine [CPD:C00179]
PRODUCT     CoA [CPD:C00010];
            N-(4-guanidinobutyl)-4-hydroxycinnamamide
REFERENCE   1
  AUTHORS   Bird, C.R. and Smith, T.A.
  TITLE     The biosynthesis of coumarylagmatine in barley seedlings.
  JOURNAL   Phytochemistry 20 (1981) 2345-2346.
  ORGANISM  Hordeum vulgare [GN:ehvu]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.64
            ExPASy - ENZYME nomenclature database: 2.3.1.64
            ExplorEnz - The Enzyme Database: 2.3.1.64
            ERGO genome analysis and discovery system: 2.3.1.64
            BRENDA, the Enzyme Database: 2.3.1.64
            CAS: 85030-72-4
///
ENTRY       EC 2.3.1.65                 Enzyme
NAME        bile acid-CoA:amino acid N-acyltransferase;
            glycine---taurine N-acyltransferase;
            amino acid N-choloyltransferase;
            BAT;
            glycine N-choloyltransferase;
            BACAT;
            cholyl-CoA glycine-taurine N-acyltransferase;
            cholyl-CoA:taurine N-acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     choloyl-CoA:glycine N-choloyltransferase
REACTION    choloyl-CoA + glycine = CoA + glycocholate [RN:R03718]
ALL_REAC    R03718;
            (other) R03720 R04828
SUBSTRATE   choloyl-CoA [CPD:C01794];
            glycine [CPD:C00037]
PRODUCT     CoA [CPD:C00010];
            glycocholate [CPD:C01921]
COMMENT     Also acts on CoA derivatives of other bile acids. Taurine and
            2-fluoro-beta-alanine can act as substrates, but more slowly [4].
            The enzyme can also conjugate fatty acids to glycine and can act as
            a very-long-chain acyl-CoA thioesterase [7]. Bile-acid---amino-acid
            conjugates serve as detergents in the gastrointestinal tract,
            solubilizing long chain fatty acids, mono- and diglycerides,
            fat-soluble vitamins and cholesterol [4]. This is the second enzyme
            in a two-step process leading to the conjugation of bile acids with
            amino acids; the first step is the conversion of bile acids into
            their acyl-CoA thioesters, which is catalysed by EC 6.2.1.7,
            cholate---CoA ligase.
REFERENCE   1  [PMID:7372637]
  AUTHORS   Czuba B, Vessey DA.
  TITLE     Kinetic characterization of cholyl-CoA glycine-taurine
            N-acyltransferase from bovine liver.
  JOURNAL   J. Biol. Chem. 255 (1980) 5296-9.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   Jordan, T.W., Lee, R. and Lim, W.C.
  TITLE     Isoelectric focussing of soluble and particulate benzoyl-CoA and
            cholyl-CoA:amino acid N-acyltransferases from rat liver.
  JOURNAL   Biochem. Int. 1 (1980) 325-330.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:422567]
  AUTHORS   Vessey DA.
  TITLE     The co-purification and common identity of cholyl CoA:glycine- and
            cholyl CoA:taurine-N-acyltransferase activities from bovine liver.
  JOURNAL   J. Biol. Chem. 254 (1979) 2059-63.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:2037576]
  AUTHORS   Johnson MR, Barnes S, Kwakye JB, Diasio RB.
  TITLE     Purification and characterization of bile acid-CoA:amino acid
            N-acyltransferase from human liver.
  JOURNAL   J. Biol. Chem. 266 (1991) 10227-33.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:12454267]
  AUTHORS   Falany CN, Xie X, Wheeler JB, Wang J, Smith M, He D, Barnes S.
  TITLE     Molecular cloning and expression of rat liver bile acid CoA ligase.
  JOURNAL   J. Lipid. Res. 43 (2002) 2062-71.
  ORGANISM  rat [GN:rno]
REFERENCE   6  [PMID:12951368]
  AUTHORS   He D, Barnes S, Falany CN.
  TITLE     Rat liver bile acid CoA:amino acid N-acyltransferase: expression,
            characterization, and peroxisomal localization.
  JOURNAL   J. Lipid. Res. 44 (2003) 2242-9.
  ORGANISM  rat [GN:rno]
REFERENCE   7  [PMID:12810727]
  AUTHORS   O'Byrne J, Hunt MC, Rai DK, Saeki M, Alexson SE.
  TITLE     The human bile acid-CoA:amino acid N-acyltransferase functions in
            the conjugation of fatty acids to glycine.
  JOURNAL   J. Biol. Chem. 278 (2003) 34237-44.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00120  Bile acid biosynthesis
            PATH: map00430  Taurine and hypotaurine metabolism
ORTHOLOGY   KO: K00659  glycine N-choloyltransferase
GENES       HSA: 570(BAAT)
            RNO: 29725(Baat)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.65
            ExPASy - ENZYME nomenclature database: 2.3.1.65
            ExplorEnz - The Enzyme Database: 2.3.1.65
            ERGO genome analysis and discovery system: 2.3.1.65
            BRENDA, the Enzyme Database: 2.3.1.65
            CAS: 74506-32-4
///
ENTRY       EC 2.3.1.66                 Enzyme
NAME        leucine N-acetyltransferase;
            leucine acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:L-leucine N-acetyltransferase
REACTION    acetyl-CoA + L-leucine = CoA + N-acetyl-L-leucine [RN:R01089]
ALL_REAC    R01089
SUBSTRATE   acetyl-CoA [CPD:C00024];
            L-leucine [CPD:C00123]
PRODUCT     CoA [CPD:C00010];
            N-acetyl-L-leucine [CPD:C02710]
COMMENT     Propanoyl-CoA can act as a donor, but more slowly. L-Arginine,
            L-valine, L-phenylalanine and peptides containing L-leucine can act
            as acceptors.
REFERENCE   1
  AUTHORS   Suzukake, S., Hayashi, H., Hori, M. and Umezawa, H.
  TITLE     Biosnthesis of leupeptin III. Isolation and properties of an enzyme
            synthesizing acetyl-L-leucine.
  JOURNAL   J. Antibiot. 33 (1982) 857-862.
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.66
            ExPASy - ENZYME nomenclature database: 2.3.1.66
            ExplorEnz - The Enzyme Database: 2.3.1.66
            ERGO genome analysis and discovery system: 2.3.1.66
            BRENDA, the Enzyme Database: 2.3.1.66
            CAS: 75496-56-9
///
ENTRY       EC 2.3.1.67                 Enzyme
NAME        1-alkylglycerophosphocholine O-acetyltransferase;
            acetyl-CoA:1-alkyl-2-lyso-sn-glycero-3-phosphocholine
            2-O-acetyltransferase;
            acetyl-CoA:lyso-PAF acetyltransferase;
            1-alkyl-2-lysolecithin acetyltransferase;
            acyl-CoA:1-alkyl-sn-glycero-3-phosphocholine acyltransferase;
            blood platelet-activating factor acetyltransferase;
            lyso-GPC:acetyl CoA acetyltransferase;
            lyso-platelet activating factor:acetyl-CoA acetyltransferase;
            lysoPAF:acetyl CoA acetyltransferase;
            PAF acetyltransferase;
            platelet-activating factor acylhydrolase;
            platelet-activating factor-synthesizing enzyme;
            1-alkyl-2-lyso-sn-glycero-3-phosphocholine acetyltransferase;
            lyso-platelet-activating factor:acetyl-CoA acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:1-alkyl-sn-glycero-3-phosphocholine 2-O-acetyltransferase
REACTION    acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA +
            2-acetyl-1-alkyl-sn-glycero-3-phosphocholine [RN:R03437]
ALL_REAC    R03437
SUBSTRATE   acetyl-CoA [CPD:C00024];
            1-alkyl-sn-glycero-3-phosphocholine [CPD:C04317]
PRODUCT     CoA [CPD:C00010];
            2-acetyl-1-alkyl-sn-glycero-3-phosphocholine [CPD:C04598]
REFERENCE   1  [PMID:7430122]
  AUTHORS   Wykle RL, Malone B, Snyder F.
  TITLE     Enzymatic synthesis of 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine,
            a hypotensive and platelet-aggregating lipid.
  JOURNAL   J. Biol. Chem. 255 (1980) 10256-60.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00565  Ether lipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.67
            ExPASy - ENZYME nomenclature database: 2.3.1.67
            ExplorEnz - The Enzyme Database: 2.3.1.67
            ERGO genome analysis and discovery system: 2.3.1.67
            BRENDA, the Enzyme Database: 2.3.1.67
            CAS: 76773-96-1
///
ENTRY       EC 2.3.1.68                 Enzyme
NAME        glutamine N-acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:L-glutamine N-acyltransferase
REACTION    acyl-CoA + L-glutamine = CoA + N-acyl-L-glutamine [RN:R00577]
ALL_REAC    R00577
SUBSTRATE   acyl-CoA [CPD:C00040];
            L-glutamine [CPD:C00064]
PRODUCT     CoA [CPD:C00010];
            N-acyl-L-glutamine [CPD:C02716]
COMMENT     Phenylacetyl-CoA and (indol-3-yl)acetyl-CoA, but not benzoyl-CoA,
            can act as acyl donors. Not identical with EC 2.3.1.13 glycine
            N-acyltransferase or EC 2.3.1.71 glycine N-benzoyltransferase.
REFERENCE   1  [PMID:931988]
  AUTHORS   Webster LT, Siddiqui UA, Lucas SV, Strong JM, Mieyal JJ.
  TITLE     Identification of separate acyl- CoA:glycine and
            acyl-CoA:L-glutamine N-acyltransferase activities in mitochondrial
            fractions from liver of rhesus monkey and man.
  JOURNAL   J. Biol. Chem. 251 (1976) 3352-8.
  ORGANISM  monkey, human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.68
            ExPASy - ENZYME nomenclature database: 2.3.1.68
            ExplorEnz - The Enzyme Database: 2.3.1.68
            ERGO genome analysis and discovery system: 2.3.1.68
            BRENDA, the Enzyme Database: 2.3.1.68
            CAS: 9030-00-6
///
ENTRY       EC 2.3.1.69                 Enzyme
NAME        monoterpenol O-acetyltransferase;
            menthol transacetylase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:monoterpenol O-acetyltransferase
REACTION    acetyl-CoA + a monoterpenol = CoA + a monoterpenol acetate ester
            [RN:R03017]
ALL_REAC    R03017
SUBSTRATE   acetyl-CoA [CPD:C00024];
            monoterpenol [CPD:C00863]
PRODUCT     CoA [CPD:C00010];
            monoterpenol acetate ester [CPD:C03707]
COMMENT     (-)-Menthol, (+)-neomenthol, borneol, and also cyclohexanol and
            decan-1-ol can be acetylated.
REFERENCE   1
  AUTHORS   Croteau, R. and Hooper, C.L.
  TITLE     Metabolism of monoterpenes. Acetylation of (-)-menthol by a soluble
            enzyme preparation from peppermint (Mentha piperita) leaves.
  JOURNAL   Plant Physiol. 61 (1978) 737-742.
  ORGANISM  Mentha piperita
REFERENCE   2
  AUTHORS   Martinkus, C. and Croteau, R.
  TITLE     Metabolism of monoterpenes - evidence for compartmentation of
            L-menthone metabolism in peppermint (Mentha piperita) leaves.
  JOURNAL   Plant Physiol. 68 (1981) 99-106.
  ORGANISM  Mentha piperita
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.69
            ExPASy - ENZYME nomenclature database: 2.3.1.69
            ExplorEnz - The Enzyme Database: 2.3.1.69
            ERGO genome analysis and discovery system: 2.3.1.69
            BRENDA, the Enzyme Database: 2.3.1.69
            CAS: 78990-59-7
///
ENTRY       EC 2.3.1.70                 Enzyme
NAME        CDP-acylglycerol O-arachidonoyltransferase;
            CDP-acylglycerol O-arachidonyltransferase;
            arachidonyl-CoA:CDP-acylglycerol O-arachidonyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     arachidonoyl-CoA:CDP-acylglycerol O-arachidonoyltransferase
REACTION    arachidonoyl-CoA + CDP-acylglycerol = CoA + CDP-diacylglycerol
            [RN:R01798]
ALL_REAC    R01798
SUBSTRATE   arachidonoyl-CoA [CPD:C02249];
            CDP-acylglycerol [CPD:C02255]
PRODUCT     CoA [CPD:C00010];
            CDP-diacylglycerol [CPD:C00269]
COMMENT     Highly specific for both donor and acceptor.
REFERENCE   1  [PMID:429352]
  AUTHORS   Thompson W, MacDonald G.
  TITLE     Isolation of a specific arachidonoyl coenzyme A: cytidine
            diphosphate monoacylglycerol acyltransferase.
  JOURNAL   J. Biol. Chem. 254 (1979) 3311-4.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.70
            ExPASy - ENZYME nomenclature database: 2.3.1.70
            ExplorEnz - The Enzyme Database: 2.3.1.70
            ERGO genome analysis and discovery system: 2.3.1.70
            BRENDA, the Enzyme Database: 2.3.1.70
            CAS: 70771-22-1
///
ENTRY       EC 2.3.1.71                 Enzyme
NAME        glycine N-benzoyltransferase;
            benzoyl CoA-amino acid N-acyltransferase;
            benzoyl-CoA:glycine N-acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     benzoyl-CoA:glycine N-benzoyltransferase
REACTION    benzoyl-CoA + glycine = CoA + N-benzoylglycine
ALL_REAC    (other) R02452
SUBSTRATE   benzoyl-CoA [CPD:C00512];
            glycine [CPD:C00037]
PRODUCT     CoA [CPD:C00010];
            N-benzoylglycine [CPD:C01586]
COMMENT     Not identical with EC 2.3.1.13 glycine N-acyltransferase or EC
            2.3.1.68 glutamine N-acyltransferase
REFERENCE   1  [PMID:457678]
  AUTHORS   Nandi DL, Lucas SV, Webster LT Jr.
  TITLE     Benzoyl-coenzyme A:glycine N-acyltransferase and
            phenylacetyl-coenzyme A:glycine N-acyltransferase from bovine liver
            mitochondria. Purification and characterization.
  JOURNAL   J. Biol. Chem. 254 (1979) 7230-7.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00360  Phenylalanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.71
            ExPASy - ENZYME nomenclature database: 2.3.1.71
            ExplorEnz - The Enzyme Database: 2.3.1.71
            ERGO genome analysis and discovery system: 2.3.1.71
            BRENDA, the Enzyme Database: 2.3.1.71
            CAS: 71567-07-2
///
ENTRY       EC 2.3.1.72                 Enzyme
NAME        indoleacetylglucose-inositol O-acyltransferase;
            indole-3-acetyl-beta-1-D-glucoside:myo-inositol
            indoleacetyltransferase;
            1-O-(indol-3-ylacetyl)-beta-D-glucose:myo-inositol
            indole-3-ylacetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     1-O-(indol-3-yl)acetyl-beta-D-glucose:myo-inositol
            (indol-3-yl)acetyltransferase
REACTION    1-O-(indol-3-yl)acetyl-beta-D-glucose + myo-inositol = D-glucose +
            O-(indol-3-yl)acetyl-myo-inositol [RN:R04333]
ALL_REAC    R04333
SUBSTRATE   1-O-(indol-3-yl)acetyl-beta-D-glucose;
            myo-inositol [CPD:C00137]
PRODUCT     D-glucose [CPD:C00031];
            O-(indol-3-yl)acetyl-myo-inositol
COMMENT     The position of acylation is indeterminate because of the ease of
            acyl transfer between hydroxy groups.
REFERENCE   1  [PMID:6218801]
  AUTHORS   Michalczuk L, Bandurski RS.
  TITLE     Enzymic synthesis of 1-O-indol-3-ylacetyl-beta-D-glucose and
            indol-3-ylacetyl-myo-inositol.
  JOURNAL   Biochem. J. 207 (1982) 273-81.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   2  [PMID:6446303]
  AUTHORS   Michalczuk L, Bandurski RS.
  TITLE     UDP-glucose: indoleacetic acid glucosyl transferase and
            indoleacetyl-glucose: myo-inositol indoleacetyl transferase.
  JOURNAL   Biochem. Biophys. Res. Commun. 93 (1980) 588-92.
  ORGANISM  Zea mays [GN:ezma]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.72
            ExPASy - ENZYME nomenclature database: 2.3.1.72
            ExplorEnz - The Enzyme Database: 2.3.1.72
            ERGO genome analysis and discovery system: 2.3.1.72
            BRENDA, the Enzyme Database: 2.3.1.72
            CAS: 74082-57-8
///
ENTRY       EC 2.3.1.73                 Enzyme
NAME        diacylglycerol---sterol O-acyltransferase;
            1,2-diacyl-sn-glycerol:sterol acyl transferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     1,2-diacyl-sn-glycerol:sterol O-acyltransferase
REACTION    1,2-diacyl-sn-glycerol + sterol = monoacylglycerol + sterol ester
            [RN:R02693]
ALL_REAC    R02693 > R02692
SUBSTRATE   1,2-diacyl-sn-glycerol [CPD:C00641];
            sterol [CPD:C00370]
PRODUCT     monoacylglycerol [CPD:C01885];
            sterol ester [CPD:C01958]
COMMENT     Cholesterol, sitosterol, campesterol and diacylglycerol can act as
            acceptors. Transfers a number of long-chain fatty acyl groups.
REFERENCE   1
  AUTHORS   Bartlett, K., Keat, M.J. and Mercer, E.I.
  TITLE     Biosynthesis of sterol esters in Phycomyces blakesleeanus.
  JOURNAL   Phytochemistry 13 (1974) 1107-1113.
REFERENCE   2  [PMID:742884]
  AUTHORS   Garcia RE, Mudd JB.
  TITLE     Metabolism of monoacylglycerol and diacylglycerol by enzyme
            preparations from spinach leaves.
  JOURNAL   Arch. Biochem. Biophys. 191 (1978) 487-93.
  ORGANISM  spinach
REFERENCE   3
  AUTHORS   Garcia, R.E. and Mudd, J.B.
  TITLE     1,2-Diacyl-sn-glycerol:sterol acyl transferase from spinach leaves
            (Spinacia oleracea L.).
  JOURNAL   Methods Enzymol. 71 (1981) 768-772.
  ORGANISM  spinach
PATHWAY     PATH: map00120  Bile acid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.73
            ExPASy - ENZYME nomenclature database: 2.3.1.73
            ExplorEnz - The Enzyme Database: 2.3.1.73
            ERGO genome analysis and discovery system: 2.3.1.73
            BRENDA, the Enzyme Database: 2.3.1.73
            CAS: 79586-23-5
///
ENTRY       EC 2.3.1.74                 Enzyme
NAME        naringenin-chalcone synthase;
            chalcone synthase;
            flavanone synthase;
            6'-deoxychalcone synthase;
            chalcone synthetase;
            DOCS;
            CHS
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     malonyl-CoA:4-coumaroyl-CoA malonyltransferase (cyclizing)
REACTION    3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3
            CO2 [RN:R01613]
ALL_REAC    R01613;
            (other) R06568
SUBSTRATE   malonyl-CoA [CPD:C00083];
            4-coumaroyl-CoA [CPD:C00223]
PRODUCT     CoA [CPD:C00010];
            naringenin chalcone [CPD:C06561];
            CO2 [CPD:C00011]
COMMENT     In the presence of NADH and a reductase, 6'-deoxychalcone is
            produced.
REFERENCE   1  [PMID:3355160]
  AUTHORS   Ayabe S, Udagawa A, Furuya T.
  TITLE     NAD(P)H-dependent 6'-deoxychalcone synthase activity in Glycyrrhiza
            echinata cells induced by yeast extract.
  JOURNAL   Arch. Biochem. Biophys. 261 (1988) 458-62.
  ORGANISM  Glycyrrhiza echinata
REFERENCE   2  [PMID:7436427]
  AUTHORS   Heller W, Hahlbrock K.
  TITLE     Highly purified &quot;flavanone synthase&quot; from parsley
            catalyzes the formation of naringenin chalcone.
  JOURNAL   Arch. Biochem. Biophys. 200 (1980) 617-9.
  ORGANISM  Petroselinum hotiense
PATHWAY     PATH: map00941  Flavonoid biosynthesis
ORTHOLOGY   KO: K00660  chalcone synthase
GENES       ATH: AT1G02050 AT5G13930(CHS)
            OSA: 4334901 4342725 4350636
            EHI: 242.t00002
            SGL: SG2219
            PAR: Psyc_0421
            PIN: Ping_0256
            BBA: Bd0331(bcsA)
            RET: RHE_CH00744(ypch00249) RHE_PD00024(ypd00006)
            RLE: RL0786
            BRA: BRADO0151
            BBT: BBta_0202
            NHA: Nham_4105
            RSP: RSP_0226
            ABA: Acid345_3105
            BSU: BG11523(bcsA)
            BHA: BH0617(bcsA)
            BLD: BLi02345(bcsA)
            BCL: ABC0998(bcsA)
            BAY: RBAM_020200(bcsA)
            BPU: BPUM_1941(bcsA)
            OIH: OB1748
            GKA: GK1551(bcsA)
            MTU: Rv1660(pks10) Rv1665(pks11)
            MTC: MT1698 MT1705
            MBO: Mb1688(pks10) Mb1693(pks11)
            MBB: BCG_1699(pks10) BCG_1704(pks11)
            MPA: MAP1369(pks10) MAP1372(pks11)
            MSM: MSMEG_0808
            MMC: Mmcs_1059
            SCO: SCO7671(SC4C2.06c)
            SMA: SAV7131(rppA)
            CMI: CMM_1534(chsA)
            ART: Arth_2198
            FRA: Francci3_2458
            FAL: FRAAL6460
            KRA: Krad_2809
            SEN: SACE_1243(rppA)
            RXY: Rxyl_1084
            RBA: RB8853(chsA)
            SYW: SYNW0993
            SYE: Syncc9902_1339
            SYG: sync_1460
            SYX: SynWH7803_1003
            PMT: PMT0412
            PMF: P9303_18741(bcsA)
            CHU: CHU_3794(bcsA)
            GFO: GFO_1610(bcsA)
            DRA: DR_2091
            DGE: Dgeo_1684
STRUCTURES  PDB: 1BI5  1BQ6  1CGK  1CGZ  1CHW  1CML  1D6F  1D6H  1D6I  1EE0  
                 1I86  1I88  1I89  1I8B  1JWX  1QLV  1TED  1TEE  1U0V  1U0W  
                 2P0U  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.74
            ExPASy - ENZYME nomenclature database: 2.3.1.74
            ExplorEnz - The Enzyme Database: 2.3.1.74
            ERGO genome analysis and discovery system: 2.3.1.74
            BRENDA, the Enzyme Database: 2.3.1.74
            CAS: 56803-04-4
///
ENTRY       EC 2.3.1.75                 Enzyme
NAME        long-chain-alcohol O-fatty-acyltransferase;
            wax synthase;
            wax-ester synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:long-chain-alcohol O-acyltransferase
REACTION    acyl-CoA + a long-chain alcohol = CoA + a long-chain ester
            [RN:R01999]
ALL_REAC    R01999
SUBSTRATE   acyl-CoA [CPD:C00040];
            long-chain alcohol [CPD:C00339]
PRODUCT     CoA [CPD:C00010];
            long-chain ester [CPD:C02434]
COMMENT     Transfers saturated or unsaturated acyl residues of chain-length C18
            to C20 to long-chain alcohols, forming waxes. The best acceptor is
            cis-icos-11-en-1-ol.
REFERENCE   1
  AUTHORS   Wu, X.-Y., Moreau, R.A. and Stumpf, P.K.
  TITLE     Studies of biosynthesis of waxes by developing jojoba seed. 3.
            Biosynthesis of wax esters from acyl-CoA and long-chain alcohols.
  JOURNAL   Lipids 16 (1981) 897-902.
  ORGANISM  Simmondsia chinensis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.75
            ExPASy - ENZYME nomenclature database: 2.3.1.75
            ExplorEnz - The Enzyme Database: 2.3.1.75
            ERGO genome analysis and discovery system: 2.3.1.75
            BRENDA, the Enzyme Database: 2.3.1.75
            CAS: 64060-40-8
///
ENTRY       EC 2.3.1.76                 Enzyme
NAME        retinol O-fatty-acyltransferase;
            retinol acyltransferase;
            retinol fatty-acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:retinol O-acyltransferase
REACTION    acyl-CoA + retinol = CoA + retinyl ester [RN:R02366]
ALL_REAC    R02366 > R02367
SUBSTRATE   acyl-CoA [CPD:C00040];
            retinol [CPD:C00473]
PRODUCT     CoA [CPD:C00010];
            retinyl ester [CPD:C02075]
COMMENT     Acts on palmitoyl-CoA and other long-chain fatty-acyl derivatives of
            CoA.
REFERENCE   1  [PMID:6826734]
  AUTHORS   Helgerud P, Petersen LB, Norum KR.
  TITLE     Retinol esterification by microsomes from the mucosa of human small
            intestine. Evidence for acyl-Coenzyme A retinol acyltransferase
            activity.
  JOURNAL   J. Clin. Invest. 71 (1983) 747-53.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:7061433]
  AUTHORS   Ross AC.
  TITLE     Retinol esterification by rat liver microsomes. Evidence for a fatty
            acyl coenzyme A: retinol acyltransferase.
  JOURNAL   J. Biol. Chem. 257 (1982) 2453-9.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00830  Retinol metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.76
            ExPASy - ENZYME nomenclature database: 2.3.1.76
            ExplorEnz - The Enzyme Database: 2.3.1.76
            ERGO genome analysis and discovery system: 2.3.1.76
            BRENDA, the Enzyme Database: 2.3.1.76
            CAS: 81295-48-9
///
ENTRY       EC 2.3.1.77                 Enzyme
NAME        triacylglycerol---sterol O-acyltransferase;
            triacylglycerol:sterol acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     triacylglycerol:3beta-hydroxysterol O-acyltransferase
REACTION    triacylglycerol + a 3beta-hydroxysterol = diacylglycerol + a
            3beta-hydroxysterol ester [RN:R04055]
ALL_REAC    R04055
SUBSTRATE   triacylglycerol [CPD:C00422];
            3beta-hydroxysterol [CPD:C02799]
PRODUCT     diacylglycerol [CPD:C00165];
            3beta-hydroxysterol ester [CPD:C03587]
COMMENT     Tripalmitoylglycerol and, more slowly, other triacylglycerols
            containing C6 to C22 fatty acids, can act as donors. The best
            acceptors are 3beta-hydroxysterols with a planar ring system.
REFERENCE   1
  AUTHORS   Zimowski, J. and Wojciechowski, Z.A.
  TITLE     Acyl donors for sterol esterification by cell-free preparations from
            Sinapis alba roots.
  JOURNAL   Phytochemistry 20 (1981) 1799-1803.
  ORGANISM  Sinapis alba
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.77
            ExPASy - ENZYME nomenclature database: 2.3.1.77
            ExplorEnz - The Enzyme Database: 2.3.1.77
            ERGO genome analysis and discovery system: 2.3.1.77
            BRENDA, the Enzyme Database: 2.3.1.77
            CAS: 80487-96-3
///
ENTRY       EC 2.3.1.78                 Enzyme
NAME        heparan-alpha-glucosaminide N-acetyltransferase;
            acetyl-CoA:alpha-glucosaminide N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:heparan-alpha-D-glucosaminide N-acetyltransferase
REACTION    acetyl-CoA + heparan sulfate alpha-D-glucosaminide = CoA + heparan
            sulfate N-acetyl-alpha-D-glucosaminide [RN:R04466 R07815]
ALL_REAC    R04466 R07815(G)
SUBSTRATE   acetyl-CoA [CPD:C00024];
            heparan sulfate alpha-D-glucosaminide [CPD:C04384]
PRODUCT     CoA [CPD:C00010];
            heparan sulfate N-acetyl-alpha-D-glucosaminide [CPD:C04649]
COMMENT     Brings about the acetylation of glucosamine groups of heparan
            sulfate and heparin from which the sulfate has been removed. Also
            acts on heparin. Not identical with EC 2.3.1.3 glucosamine
            N-acetyltransferase or EC 2.3.1.4 glucosamine-phosphate
            N-acetyltransferase.
REFERENCE   1  [PMID:33384]
  AUTHORS   Klein U, Kresse H, von Figura K.
  TITLE     Sanfilippo syndrome type C: deficiency of
            acetyl-CoA:alpha-glucosaminide N-acetyltransferase in skin
            fibroblasts.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 75 (1978) 5185-9.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:7346380]
  AUTHORS   Pohlmann R, Klein U, Fromme HG, von Figura K.
  TITLE     Localisation of acetyl-CoA: alpha-glucosaminide N-acetyltransferase
            in microsomes and lysosomes of rat liver.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 362 (1981) 1199-207.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00531  Glycosaminoglycan degradation
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K10532  heparan-alpha-glucosaminide N-acetyltransferase
GENES       HSA: 138050(HGSNAT)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.78
            ExPASy - ENZYME nomenclature database: 2.3.1.78
            ExplorEnz - The Enzyme Database: 2.3.1.78
            ERGO genome analysis and discovery system: 2.3.1.78
            BRENDA, the Enzyme Database: 2.3.1.78
            CAS: 79955-83-2
///
ENTRY       EC 2.3.1.79                 Enzyme
NAME        maltose O-acetyltransferase;
            maltose transacetylase;
            maltose O-acetyltransferase;
            MAT
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:maltose O-acetyltransferase
REACTION    acetyl-CoA + maltose = CoA +
            6-O-acetyl-alpha-D-glucopyranosyl-(1->4)-D-glucose [RN:R01556
            R06251]
ALL_REAC    R01556 R06251(G)
SUBSTRATE   acetyl-CoA [CPD:C00024];
            maltose [CPD:C00208]
PRODUCT     CoA [CPD:C00010];
            6-O-acetyl-alpha-D-glucopyranosyl-(1->4)-D-glucose
COMMENT     Not identical with EC 2.3.1.18, galactoside O-acetyltransferase. The
            acetyl group is added exclusively to the C6 position of glucose and
            to the C6 position of the non-reducing glucose residue of maltose
            [3]. Other substrates of this enzyme are glucose, which is a better
            substrate than maltose [2], and mannose and frucose, which are
            poorer substrates than maltose [2]. Isopropyl-beta-thio-galactose,
            which is a good substrate for EC 2.3.1.118 is a poor substrate for
            this enzyme [3].
REFERENCE   1  [PMID:7041741]
  AUTHORS   Freundlieb S, Boos W.
  TITLE     Maltose transacetylase of Escherichia coli: a preliminary report.
  JOURNAL   Ann. Microbiol. (Paris). 133A (1982) 181-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:1856235]
  AUTHORS   Brand B, Boos W.
  TITLE     Maltose transacetylase of Escherichia coli. Mapping and cloning of
            its structural, gene, mac, and characterization of the enzyme as a
            dimer of identical polypeptides with a molecular weight of 20,000.
  JOURNAL   J. Biol. Chem. 266 (1991) 14113-8.
REFERENCE   3  [PMID:12731863]
  AUTHORS   Lo Leggio L, Dal Degan F, Poulsen P, Andersen SM, Larsen S.
  TITLE     The structure and specificity of Escherichia coli maltose
            acetyltransferase give new insight into the LacA family of
            acyltransferases.
  JOURNAL   Biochemistry. 42 (2003) 5225-35.
ORTHOLOGY   KO: K00661  maltose O-acetyltransferase
GENES       CNE: CND00030 CNL05940
            DDI: DDBDRAFT_0217720
            EHI: 131.t00004 373.t00004
            ECO: b0459(maa)
            ECJ: JW0448(maa)
            ECE: Z0571(ylaD)
            ECS: ECs0512
            ECC: c0577(ylaD)
            ECI: UTI89_C0486(maa)
            ECP: ECP_0520
            ECV: APECO1_15532(maa)
            ECW: EcE24377A_0494(maa)
            ECX: EcHS_A0535
            STY: STY0515(maA)
            STT: t2388(maA)
            SPT: SPA2250(maA)
            SEC: SC0514(maa)
            STM: STM0472(maa)
            SFV: SFV_0433(ylaD)
            SSN: SSON_0446(ylaD)
            SBO: SBO_0359(ylaD)
            SDY: SDY_0460(ylaD)
            XCC: XCC4025(nodL)
            XCB: XC_4114
            XCV: XCV4246
            XAC: XAC4150(nodL)
            VPA: VPA1135
            VFI: VFA0915
            PPR: PBPRB0009 PBPRB0480
            PEN: PSEEN5256
            SON: SO_1961(maa)
            SBM: Shew185_2655
            SHM: Shewmr7_2366
            SHN: Shewana3_2484
            PHA: PSHAa2996
            HCH: HCH_03881
            AHA: AHA_0602 AHA_3822
            CVI: CV_2255(maa)
            BUR: Bcep18194_A3978
            NMU: Nmul_A1396
            EBA: ebA2867(maa)
            DDE: Dde_0665
            LIP: LI0592(maa)
            AFW: Anae109_2162
            MXA: MXAN_3892
            MLO: mll2768(nodL)
            SMD: Smed_6263
            ATU: Atu0304(nodL)
            ATC: AGR_C_527
            RET: RHE_CH00246(nodL) RHE_CH00750(ypch00252)
            RLE: RL0252(nodL) pRL100181(nodL)
            RPA: RPA4378
            RPB: RPB_4185
            RPC: RPC_1398
            RPD: RPD_4039
            RPE: RPE_1411
            RDE: RD1_2959(maa)
            BSU: BG10043(maa)
            BHA: BH3001
            BAN: BA3402(maA)
            BAR: GBAA3402(maA)
            BAA: BA_3901
            BAT: BAS3155
            BCE: BC4658
            BCA: BCE_3375(maa)
            BCZ: BCZK3050(maa)
            BTK: BT9727_3140(maa)
            BTL: BALH_3029(maa)
            BLI: BL01948(maa)
            BLD: BLi01298(maa)
            OIH: OB1064
            GKA: GK1921
            LMO: lmo0664
            LMF: LMOf2365_0698
            LIN: lin0669
            LWE: lwe0632
            LLA: L1734467(maa)
            LLM: llmg_0742(maa) llmg_1709(maa2)
            SSA: SSA_1186 SSA_2079
            SGO: SGO_1199
            LPL: lp_2550(maa1) lp_2878(maa2) lp_3553(maa3)
            LSA: LSA0054(maa) LSA1867
            LSL: LSL_0924
            LBR: LVIS_0266 LVIS_1739
            LRE: Lreu_0483
            CPE: CPE2587
            CPF: CPF_2912(maa)
            CPR: CPR_2590(maa)
            CTC: CTC00916
            CDF: CD0872(maa)
            CBO: CBO1116(maa)
            CBA: CLB_1155(maa)
            CBH: CLC_1167(maa)
            CBF: CLI_1204(maa)
            CBE: Cbei_3438 Cbei_3719
            CGB: cg0180(maa)
            TFU: Tfu_1260
            BAD: BAD_0431
            RBA: RB12315(maa) RB2502
            GVI: glr1818
            ANA: all1011
            AVA: Ava_3668 Ava_3876
            BTH: BT_3870
            BFR: BF4020
            BFS: BF1269 BF3794(maa)
            CCH: Cag_1480
            HMA: rrnAC2459(maa)
            NPH: NP4198A(maa_3) NP4490A(maa_1) NP6236A(maa_2)
            RCI: RCIX2576(maa)
STRUCTURES  PDB: 1OCX  2IC7  2P2O  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.79
            ExPASy - ENZYME nomenclature database: 2.3.1.79
            ExplorEnz - The Enzyme Database: 2.3.1.79
            ERGO genome analysis and discovery system: 2.3.1.79
            BRENDA, the Enzyme Database: 2.3.1.79
            CAS: 81295-47-8
///
ENTRY       EC 2.3.1.80                 Enzyme
NAME        cysteine-S-conjugate N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:S-substituted L-cysteine N-acetyltransferase
REACTION    acetyl-CoA + an S-substituted L-cysteine = CoA + an S-substituted
            N-acetyl-L-cysteine [RN:R04240]
ALL_REAC    R04240;
            (other) R04950
SUBSTRATE   acetyl-CoA [CPD:C00024];
            S-substituted L-cysteine [CPD:C03540]
PRODUCT     CoA [CPD:C00010];
            S-substituted N-acetyl-L-cysteine [CPD:C04345]
COMMENT     S-Benzyl-L-cysteine and, in decreasing order of activity,
            S-butyl-L-cysteine, S-propyl-L-cysteine, O-benzyl-L-serine and
            S-ethyl-L-cysteine, can act as acceptors.
REFERENCE   1  [PMID:6892478]
  AUTHORS   Duffel MW, Jakoby WB.
  TITLE     Cysteine S-conjugate N-acetyltransferase from rat kidney microsomes.
  JOURNAL   Mol. Pharmacol. 21 (1982) 444-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00480  Glutathione metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.80
            ExPASy - ENZYME nomenclature database: 2.3.1.80
            ExplorEnz - The Enzyme Database: 2.3.1.80
            ERGO genome analysis and discovery system: 2.3.1.80
            BRENDA, the Enzyme Database: 2.3.1.80
            CAS: 81725-80-6
///
ENTRY       EC 2.3.1.81                 Enzyme
NAME        aminoglycoside N3'-acetyltransferase;
            3'-aminoglycoside acetyltransferase;
            3-N-aminoglycoside acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:2-deoxystreptamine-antibiotic N3'-acetyltransferase
REACTION    acetyl-CoA + a 2-deoxystreptamine antibiotic = CoA +
            N3'-acetyl-2-deoxystreptamine antibiotic [RN:R04348]
ALL_REAC    R04348
SUBSTRATE   acetyl-CoA [CPD:C00024];
            2-deoxystreptamine antibiotic [CPD:C03922]
PRODUCT     CoA [CPD:C00010];
            N3'-acetyl-2-deoxystreptamine antibiotic [CPD:C04504]
COMMENT     Different from EC 2.3.1.60 gentamicin 3'-N-acetyltransferase. A wide
            range of antibiotics containing the 2-deoxystreptamine ring can act
            as acceptors, including gentamicin, kanamycin, tobramycin, neomycin
            and apramycin.
REFERENCE   1  [PMID:356726]
  AUTHORS   Davies J, O'Connor S.
  TITLE     Enzymatic modification of aminoglycoside antibiotics:
            3-N-acetyltransferase with broad specificity that determines
            resistance to the novel aminoglycoside apramycin.
  JOURNAL   Antimicrob. Agents. Chemother. 14 (1978) 69-72.
  ORGANISM  Escherichia coli [GN:eco], Pseudomonas aeruginosa, Klebsiella
            pneumoniae
ORTHOLOGY   KO: K00662  aminoglycoside N3'-acetyltransferase
GENES       SME: SMc02813(aacC)
            SMD: Smed_2214
            RET: RHE_CH01086(aacC1)
            RLE: RL1183(aacC)
            PDE: Pden_3154
            GOX: GOX0638
            BAN: BA2930(aacC7)
            BAR: GBAA2930(aacC7)
            BAA: BA_3440
            BAT: BAS2722
            BCE: BC2919
            BCA: BCE_2969(aacC7)
            BCZ: BCZK2651(yokD)
            BCY: Bcer98_2002
            BTK: BT9727_2673(yokD)
            BPU: BPUM_0309(yokD)
            LMF: LMOf2365_1732
            LLC: LACR_D33
            LAC: LBA0034
            LBR: LVIS_0098
            CBE: Cbei_4839
            SEN: SACE_3604(aacC1)
            HMA: rrnAC1974(aacC)
            RCI: RCIX166(aacC)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.81
            ExPASy - ENZYME nomenclature database: 2.3.1.81
            ExplorEnz - The Enzyme Database: 2.3.1.81
            ERGO genome analysis and discovery system: 2.3.1.81
            BRENDA, the Enzyme Database: 2.3.1.81
            CAS: 60120-42-5
///
ENTRY       EC 2.3.1.82                 Enzyme
NAME        aminoglycoside N6'-acetyltransferase;
            aminoglycoside 6'-N-acetyltransferase;
            aminoglycoside-6'-acetyltransferase;
            aminoglycoside-6-N-acetyltransferase;
            kanamycin acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:kanamycin-B N6'-acetyltransferase
REACTION    acetyl-CoA + kanamycin-B = CoA + N6'-acetylkanamycin-B [RN:R01889]
ALL_REAC    R01889
SUBSTRATE   acetyl-CoA [CPD:C00024];
            kanamycin B [CPD:C00825]
PRODUCT     CoA [CPD:C00010];
            N6'-acetylkanamycin-B [CPD:C03154]
COMMENT     The antibiotics kanamycin A, kanamycin B, neomycin, gentamicin C1a,
            gentamicin C2 and sisomicin are substrates. The antibiotics
            gentamicin, tobramycin and neomycin, but not paromomycin, can also
            act as acceptors. The 6-amino group of the purpurosamine ring is
            acetylated.
REFERENCE   1  [PMID:4614862]
  AUTHORS   Le Goffic F, Martel A.
  TITLE     [Resistance to aminosides induced by an isoenzyme, kanamycin
            acetyltransferase]
  JOURNAL   Biochimie. 56 (1974) 893-7.
REFERENCE   2  [PMID:4935296]
  AUTHORS   Benveniste R, Davies J.
  TITLE     Enzymatic acetylation of aminoglycoside antibiotics by Escherichia
            coli carrying an R factor.
  JOURNAL   Biochemistry. 10 (1971) 1787-96.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:836013]
  AUTHORS   Dowding JE.
  TITLE     Mechanisms of gentamicin resistance in Staphylococcus aureus.
  JOURNAL   Antimicrob. Agents. Chemother. 11 (1977) 47-50.
  ORGANISM  Staphylococcus aureus
ORTHOLOGY   KO: K00663  aminoglycoside N6'-acetyltransferase
GENES       CBU: CBU_0817(aacA4)
            CVI: CV_0230
            BPD: BURPS668_A0462
            BBA: Bd0508(rhbD)
            MLO: mll5006
            SME: SMb21552(aacC4)
            RET: RHE_CH02150(aacC2)
            RLE: RL0050
            BJA: bll0648
            BRA: BRADO0209
            HNE: HNE_3127
            BAN: BA2555
            BAR: GBAA2555
            BAA: BA_3057
            BAT: BAS2378
            BCE: BC2494 BC3473
            BCA: BCE_2557
            BCZ: BCZK2296
            BTK: BT9727_2335
            BTL: BALH_2296
            BCL: ABC3830
            RHA: RHA1_ro03788
            FAL: FRAAL3380
            LIL: LA1094
            GVI: glr2416
            ANA: alr7015
            AVA: Ava_0811 Ava_2836 Ava_3994
STRUCTURES  PDB: 1S3Z  1S5K  1S60  2A4N  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.82
            ExPASy - ENZYME nomenclature database: 2.3.1.82
            ExplorEnz - The Enzyme Database: 2.3.1.82
            ERGO genome analysis and discovery system: 2.3.1.82
            BRENDA, the Enzyme Database: 2.3.1.82
            CAS: 56467-65-3
///
ENTRY       EC 2.3.1.83                 Enzyme
NAME        phosphatidylcholine---dolichol O-acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     3-sn-phosphatidylcholine:dolichol O-acyltransferase
REACTION    3-sn-phosphatidylcholine + dolichol =
            1-acyl-sn-glycero-3-phosphocholine + acyldolichol [RN:R04227]
ALL_REAC    R04227
SUBSTRATE   3-sn-phosphatidylcholine [CPD:C00157];
            dolichol [CPD:C00381]
PRODUCT     1-acyl-sn-glycero-3-phosphocholine [CPD:C04230];
            acyldolichol [CPD:C01884]
REFERENCE   1  [PMID:4095]
  AUTHORS   Keenan RW, Kruczek ME.
  TITLE     The esterification of dolichol by rat liver microsomes.
  JOURNAL   Biochemistry. 15 (1976) 1586-91.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:506613]
  AUTHORS   Radominska-Pyrek A, Chojnacki T, Zulczyk W.
  TITLE     Acyl esters of polyprenols: specificity of microsomal transacylase
            for polyprenols of different chain length and saturation.
  JOURNAL   Acta. Biochim. Pol. 26 (1979) 125-34.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.83
            ExPASy - ENZYME nomenclature database: 2.3.1.83
            ExplorEnz - The Enzyme Database: 2.3.1.83
            ERGO genome analysis and discovery system: 2.3.1.83
            BRENDA, the Enzyme Database: 2.3.1.83
            CAS: 9012-30-0
///
ENTRY       EC 2.3.1.84                 Enzyme
NAME        alcohol O-acetyltransferase;
            alcohol acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:alcohol O-acetyltransferase
REACTION    acetyl-CoA + an alcohol = CoA + an acetyl ester [RN:R00627]
ALL_REAC    R00627
SUBSTRATE   acetyl-CoA [CPD:C00024];
            alcohol [CPD:C00069]
PRODUCT     CoA [CPD:C00010];
            acetyl ester [CPD:C01883]
COMMENT     Acts on a range of short-chain aliphatic alcohols, including
            methanol and ethanol
REFERENCE   1
  AUTHORS   Yoshioka, K. and Hashimoto, N.
  TITLE     Ester formation by alcohol acetyltransferase from brewers' yeast.
  JOURNAL   Agric. Biol. Chem. 45 (1981) 2183-2190.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K00664  alcohol O-acetyltransferase
GENES       SCE: YGR177C(ATF2) YOR377W(ATF1)
            CGR: CAGL0D05918g
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.84
            ExPASy - ENZYME nomenclature database: 2.3.1.84
            ExplorEnz - The Enzyme Database: 2.3.1.84
            ERGO genome analysis and discovery system: 2.3.1.84
            BRENDA, the Enzyme Database: 2.3.1.84
            CAS: 80237-89-4
///
ENTRY       EC 2.3.1.85                 Enzyme
NAME        fatty-acid synthase;
            yeast fatty acid synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl-
            and enoyl-reducing and thioester-hydrolysing)
REACTION    acetyl-CoA + n malonyl-CoA + 2n NADPH + 2n H+ = a long-chain fatty
            acid + (n+1) CoA + n CO2 + 2n NADP+ [RN:R05188]
ALL_REAC    R05188;
            (other) R01624 R01626 R01706 R04355 R04533 R04534 R04535 R04536
            R04537 R04543 R04544 R04566 R04568 R04725 R04726 R04952 R04953
            R04954 R04956 R04957 R04959 R04960 R04962 R04963 R04964 R04965
            R04967 R04968 R04970
SUBSTRATE   acetyl-CoA [CPD:C00024];
            malonyl-CoA [CPD:C00083];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
PRODUCT     long-chain fatty acid [CPD:C00638];
            CoA [CPD:C00010];
            CO2 [CPD:C00011];
            NADP+ [CPD:C00006]
COMMENT     The animal enzyme is a multi-functional protein catalysing the
            reactions of EC 2.3.1.38 [acyl-carrier-protein] S-acetyltransferase,
            EC 2.3.1.39 [acyl-carrier-protein] S-malonyltransferase, EC 2.3.1.41
            3-oxoacyl-[acyl-carrier-protein] synthase, EC 1.1.1.100
            3-oxoacyl-[acyl-carrier-protein] reductase, EC 4.2.1.61
            3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase, EC 1.3.1.10
            enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) and EC
            3.1.2.14 oleoyl-[acyl-carrier-protein] hydrolase.
REFERENCE   1  [PMID:457689]
  AUTHORS   Stoops JK, Ross P, Arslanian MJ, Aune KC, Wakil SJ, Oliver RM.
  TITLE     Physicochemical studies of the rat liver and adipose fatty acid
            synthetases.
  JOURNAL   J. Biol. Chem. 254 (1979) 7418-26.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6137188]
  AUTHORS   Wakil SJ, Stoops JK, Joshi VC.
  TITLE     Fatty acid synthesis and its regulation.
  JOURNAL   Annu. Rev. Biochem. 52 (1983) 537-79.
PATHWAY     PATH: map00061  Fatty acid biosynthesis
            PATH: map04910  Insulin signaling pathway
ORTHOLOGY   KO: K00665  fatty-acid synthase
GENES       HSA: 2194(FASN)
            MMU: 14104(Fasn)
            RNO: 50671(Fasn)
            BTA: 281152(FASN)
            GGA: 396061(FASN)
            DME: Dmel_CG3523
            CEL: F32H2.5(fasn-1)
            PFA: PF13_0066 PFB0505c PFI1125c
            CGL: NCgl0802(cgl0836) NCgl2409(cgl2495)
            CGB: cg0957(fas-IB) cg2743(fas-IA)
            CEF: CE0913(fasA) CE2392(fasB)
            CDI: DIP1846(fas)
STRUCTURES  PDB: 1N8L  2CF2  2CG5  2JFD  2JFK  2PNG  2PX6  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.85
            ExPASy - ENZYME nomenclature database: 2.3.1.85
            ExplorEnz - The Enzyme Database: 2.3.1.85
            ERGO genome analysis and discovery system: 2.3.1.85
            BRENDA, the Enzyme Database: 2.3.1.85
            CAS: 9045-77-6
///
ENTRY       EC 2.3.1.86                 Enzyme
NAME        fatty-acyl-CoA synthase;
            yeast fatty acid synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl-
            and enoyl- reducing)
REACTION    acetyl-CoA + n malonyl-CoA + 2n NADH + 2n NADPH + 4n H+ =
            long-chain-acyl-CoA + n CoA + n CO2 + 2n NAD+ + 2n NADP+ [RN:R05190]
ALL_REAC    R05190;
            (other) R01624 R01626 R04355 R04429 R04533 R04534 R04535 R04536
            R04537 R04543 R04544 R04566 R04568 R04724 R04726 R04952 R04953
            R04954 R04955 R04957 R04958 R04960 R04961 R04963 R04964 R04965
            R04966 R04968 R04969
SUBSTRATE   acetyl-CoA [CPD:C00024];
            malonyl-CoA [CPD:C00083];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
PRODUCT     long-chain-acyl-CoA;
            CoA [CPD:C00010];
            CO2 [CPD:C00011];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
COMMENT     The yeast enzyme is a multi-functional protein catalysing the
            reactions of EC 2.3.1.38 [acyl-carrier-protein] S-acetyltransferase,
            EC 2.3.1.39 [acyl-carrier-protein] S-malonyltransferase, EC 2.3.1.41
            3-oxoacyl-[acyl-carrier-protein] synthase, EC 1.1.1.100
            3-oxoacyl-[acyl-carrier-protein] reductase, EC 1.1.1.279,
            (R)-3-hydroxyacid ester dehydrogenase, EC 4.2.1.61
            3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase and EC 1.3.1.9
            enoyl-[acyl-carrier-protein] reductase (NADH).
REFERENCE   1  [PMID:4590449]
  AUTHORS   Schweizer E, Kniep B, Castorph H, Holzner U.
  TITLE     Pantetheine-free mutants of the yeast fatty-acid-synthetase complex.
  JOURNAL   Eur. J. Biochem. 39 (1973) 353-62.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:6137188]
  AUTHORS   Wakil SJ, Stoops JK, Joshi VC.
  TITLE     Fatty acid synthesis and its regulation.
  JOURNAL   Annu. Rev. Biochem. 52 (1983) 537-79.
PATHWAY     PATH: map00061  Fatty acid biosynthesis
ORTHOLOGY   KO: K00666  fatty-acyl-CoA synthase
            KO: K00667  fatty-acyl-CoA synthase, subunit alpha
            KO: K00668  fatty-acyl-CoA synthase, subunit beta
GENES       SCE: YKL182W(FAS1) YPL231W(FAS2)
            AGO: AGOS_AER085C AGOS_AFL138W
            PIC: PICST_80966(FAS2)
            CGR: CAGL0D00528g CAGL0E06138g
            SPO: SPAC4A8.11c(lsd1) SPAC926.09c(fas1)
            CNE: CNE04360 CNE04370
            RHA: RHA1_ro01426
STRUCTURES  PDB: 2PFF  2UV8  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.86
            ExPASy - ENZYME nomenclature database: 2.3.1.86
            ExplorEnz - The Enzyme Database: 2.3.1.86
            ERGO genome analysis and discovery system: 2.3.1.86
            BRENDA, the Enzyme Database: 2.3.1.86
            CAS: 9045-77-6
///
ENTRY       EC 2.3.1.87                 Enzyme
NAME        aralkylamine N-acetyltransferase;
            serotonin acetyltransferase;
            serotonin acetylase;
            arylalkylamine N-acetyltransferase;
            serotonin N-acetyltransferase;
            AANAT;
            melatonin rhythm enzyme
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:2-arylethylamine N-acetyltransferase
REACTION    acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
            [RN:R03760]
ALL_REAC    R03760 > R02911
SUBSTRATE   acetyl-CoA [CPD:C00024];
            2-arylethylamine [CPD:C15534]
PRODUCT     CoA [CPD:C00010];
            N-acetyl-2-arylethylamine [CPD:C15535]
COMMENT     Narrow specificity towards 2-arylethylamines, including serotonin
            (5-hydroxytryptamine), tryptamine, 5-methoxytryptamine and
            phenylethylamine. This is the penultimate enzyme in the production
            of melatonin (5-methoxy-N-acetyltryptamine) and controls its
            synthesis (cf. EC 2.1.1.4, acetylserotonin O-methyltransferase).
            Differs from EC 2.3.1.5 arylamine N-acetyltransferase.
REFERENCE   1  [PMID:6469990]
  AUTHORS   Voisin P, Namboodiri MA, Klein DC.
  TITLE     Arylamine N-acetyltransferase and arylalkylamine N-acetyltransferase
            in the mammalian pineal gland.
  JOURNAL   J. Biol. Chem. 259 (1984) 10913-8.
  ORGANISM  rat [GN:rno], sheep
REFERENCE   2  [PMID:10722724]
  AUTHORS   Ferry G, Loynel A, Kucharczyk N, Bertin S, Rodriguez M, Delagrange
            P, Galizzi JP, Jacoby E, Volland JP, Lesieur D, Renard P, Canet E,
            Fauchere JL, Boutin JA.
  TITLE     Substrate specificity and inhibition studies of human serotonin
            N-acetyltransferase.
  JOURNAL   J. Biol. Chem. 275 (2000) 8794-805.
  ORGANISM  human [GN:hsa]
REFERENCE   3
  AUTHORS   Khalil, E.M. and Cole, P.A.
  TITLE     A potent inhibitor of the melatonin rhythm enzyme.
  JOURNAL   J. Am. Chem. Soc. 120 (1998) 6195-6196.
PATHWAY     PATH: map00380  Tryptophan metabolism
ORTHOLOGY   KO: K00669  arylalkylamine N-acetyltransferase
GENES       HSA: 15(AANAT)
            PTR: 503504(AANAT)
            MMU: 11298(Aanat)
            RNO: 25120(Aanat)
            CFA: 483331(AANAT)
            BTA: 281583(AANAT)
            GGA: 396066(AANAT)
            DRE: 30685(aanat2) 393677(aanat1)
            DME: Dmel_CG3318(Dat)
            PIC: PICST_62543(SNA1)
STRUCTURES  PDB: 1B6B  1IB1  1KUV  1KUX  1KUY  1L0C  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.87
            ExPASy - ENZYME nomenclature database: 2.3.1.87
            ExplorEnz - The Enzyme Database: 2.3.1.87
            ERGO genome analysis and discovery system: 2.3.1.87
            BRENDA, the Enzyme Database: 2.3.1.87
            CAS: 92941-56-5
///
ENTRY       EC 2.3.1.88                 Enzyme
NAME        peptide alpha-N-acetyltransferase;
            beta-endorphin acetyltransferase;
            peptide acetyltransferase;
            protein N-terminal acetyltransferase;
            NAT;
            Nalpha-acetyltransferase;
            amino-terminal amino acid-acetylating enzyme;
            acetyl-CoA:peptide alpha-N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:peptide Nalpha-acetyltransferase
REACTION    acetyl-CoA + peptide = Nalpha-acetylpeptide + CoA [RN:R00234]
ALL_REAC    R00234
SUBSTRATE   acetyl-CoA [CPD:C00024];
            peptide [CPD:C00012]
PRODUCT     Nalpha-acetylpeptide [CPD:C03011];
            CoA [CPD:C00010]
COMMENT     Acetylates N-terminal alanine, serine, methionine and glutamate
            residues in a number of peptides and proteins, including
            beta-endorphin, corticotropins and melanotropin. cf. EC 2.3.1.108
            alpha-tubulin N-acetyltransferase.
REFERENCE   1  [PMID:3902358]
  AUTHORS   Driessen HP, de Jong WW, Tesser GI, Bloemendal H.
  TITLE     The mechanism of N-terminal acetylation of proteins.
  JOURNAL   CRC. Crit. Rev. Biochem. 18 (1985) 281-325.
REFERENCE   2  [PMID:6286657]
  AUTHORS   Glembotski CC.
  TITLE     Characterization of the peptide acetyltransferase activity in bovine
            and rat intermediate pituitaries responsible for the acetylation of
            beta-endorphin and alpha-melanotropin.
  JOURNAL   J. Biol. Chem. 257 (1982) 10501-9.
  ORGANISM  cow [GN:bta], rat [GN:rno]
REFERENCE   3  [PMID:6296134]
  AUTHORS   O'Donohue TL.
  TITLE     Identification of endorphin acetyltransferase in rat brain and
            pituitary gland.
  JOURNAL   J. Biol. Chem. 258 (1983) 2163-7.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:6244269]
  AUTHORS   Tsunasawa S, Kamitani K, Narita K.
  TITLE     Partial purification and properties of the amino-terminal amino
            acid-acetylating enzyme from hen's oviduct.
  JOURNAL   J. Biochem. (Tokyo). 87 (1980) 645-50.
  ORGANISM  chicken [GN:gga]
ORTHOLOGY   KO: K00670  peptide alpha-N-acetyltransferase
GENES       DME: Dmel_CG11989(Ard1) Dmel_CG12202
            SCE: YDL040C(NAT1) YGR147C(NAT2)
            AGO: AGOS_ADR310W
            PIC: PICST_73563
            CGR: CAGL0C05313g
STRUCTURES  PDB: 2OB0  2PSW  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.88
            ExPASy - ENZYME nomenclature database: 2.3.1.88
            ExplorEnz - The Enzyme Database: 2.3.1.88
            ERGO genome analysis and discovery system: 2.3.1.88
            BRENDA, the Enzyme Database: 2.3.1.88
            CAS: 83452-29-3
///
ENTRY       EC 2.3.1.89                 Enzyme
NAME        tetrahydrodipicolinate N-acetyltransferase;
            tetrahydrodipicolinate acetylase;
            tetrahydrodipicolinate:acetyl-CoA acetyltransferase;
            acetyl-CoA:L-2,3,4,5-tetrahydrodipicolinate N2-acetyltransferase;
            acetyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate
            2-N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate
            N2-acetyltransferase
REACTION    acetyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H2O
            = CoA + L-2-acetamido-6-oxoheptanedioate [RN:R04364]
ALL_REAC    R04364
SUBSTRATE   acetyl-CoA [CPD:C00024];
            (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate [CPD:C03972];
            H2O [CPD:C00001]
PRODUCT     CoA [CPD:C00010];
            L-2-acetamido-6-oxoheptanedioate [CPD:C05539]
REFERENCE   1
  AUTHORS   Chatterjee, S.P. and White, P.J.
  TITLE     Activities and regulation of the enzymes of lysine biosynthesis in a
            lysine-excreting strain of Bacillus megaterium.
  JOURNAL   J. Gen. Microbiol. 128 (1982) 1073-1081.
  ORGANISM  Bacillus megaterium
PATHWAY     PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K05822  tetrahydrodipicolinate N-acetyltransferase
GENES       BSU: BG13301(dapD)
            BHA: BH2669
            BAN: BA4194
            BAR: GBAA4194
            BAA: BA_4658
            BAT: BAS3891
            BCE: BC3981
            BCA: BCE_4030
            BCZ: BCZK3739
            BTK: BT9727_3723
            BTL: BALH_3603(dapD)
            BLI: BL03591
            BLD: BLi01632(ykuQ)
            BAY: RBAM_013950(ykuQ)
            OIH: OB1402
            GKA: GK1049
            SAU: SA1229(dapD)
            SAV: SAV1397(dapD)
            SAM: MW1285(dapD)
            SAR: SAR1409(dapD)
            SAS: SAS1338
            SAB: SAB1252(dapD)
            SEP: SE1077
            SER: SERP0967(dapD)
            SHA: SH1514(dapD)
            LMO: lmo1011
            LMF: LMOf2365_1032
            LIN: lin1010
            LWE: lwe0995
            LSL: LSL_0468
            MSI: Msm_0189
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.89
            ExPASy - ENZYME nomenclature database: 2.3.1.89
            ExplorEnz - The Enzyme Database: 2.3.1.89
            ERGO genome analysis and discovery system: 2.3.1.89
            BRENDA, the Enzyme Database: 2.3.1.89
            CAS: 83588-91-4
///
ENTRY       EC 2.3.1.90                 Enzyme
NAME        beta-glucogallin O-galloyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     1-O-galloyl-beta-D-glucose:1-O-galloyl-beta-D-glucose
            O-galloyltransferase
REACTION    2 1-O-galloyl-beta-D-glucose = D-glucose +
            1-O,6-O-digalloyl-beta-D-glucose [RN:R00049]
ALL_REAC    R00049
SUBSTRATE   1-O-galloyl-beta-D-glucose [CPD:C01158]
PRODUCT     D-glucose [CPD:C00031];
            1-O,6-O-digalloyl-beta-D-glucose [CPD:C04101]
COMMENT     beta-Glucogallin can act as donor and as acceptor. Digalloylglucose
            can also act as acceptor, with the formation of
            1-O,2-O,6-O-trigalloylglucose
REFERENCE   1
  AUTHORS   Denzel, K., Schilling, G. and Gross, G.G.
  TITLE     Biosynthesis of gallotannins - enzymatic conversion of
            1,6-digalloylglucose to 1,2,6-trigalloylglucose.
  JOURNAL   Planta 176 (1988) 135-137.
  ORGANISM  Rhus typhina
REFERENCE   2
  AUTHORS   Gross, G.G.
  TITLE     Synthesis of mono-galloyl-beta-D-glucose di-galloyl-beta-D-glucose
            and trigalloyl-beta-D-glucose by beta-glucogallin-dependent
            galloyltransferases from oak leaves.
  JOURNAL   Z. Natursforsch. C: Biosci. 38 (1983) 519-523.
  ORGANISM  oak
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.90
            ExPASy - ENZYME nomenclature database: 2.3.1.90
            ExplorEnz - The Enzyme Database: 2.3.1.90
            ERGO genome analysis and discovery system: 2.3.1.90
            BRENDA, the Enzyme Database: 2.3.1.90
            CAS: 87502-55-4
///
ENTRY       EC 2.3.1.91                 Enzyme
NAME        sinapoylglucose---choline O-sinapoyltransferase;
            sinapine synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     1-O-(4-hydroxy-3,5-dimethoxycinnamoyl)-beta-D-glucose:choline
            1-O-(4-hydroxy-3,5-dimethoxycinnamoyl)transferase
REACTION    1-O-sinapoyl-beta-D-glucose + choline = D-glucose + sinapoylcholine
            [RN:R03075]
ALL_REAC    R03075
SUBSTRATE   1-O-sinapoyl-beta-D-glucose [CPD:C01175];
            choline [CPD:C00114]
PRODUCT     D-glucose [CPD:C00031];
            sinapoylcholine [CPD:C00933]
REFERENCE   1  [PMID:16525708]
  AUTHORS   Karacapilidis N, Koukouras D.
  TITLE     A web-based system for supporting collaboration towards resolving
            oncology issues.
  JOURNAL   Oncol. Rep. 15 Spec no. (2006) 1101-7.
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
ORTHOLOGY   KO: K09756  sinapoylglucose-choline O-sinapoyltransferase
GENES       ATH: AT5G09640(SNG2)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.91
            ExPASy - ENZYME nomenclature database: 2.3.1.91
            ExplorEnz - The Enzyme Database: 2.3.1.91
            ERGO genome analysis and discovery system: 2.3.1.91
            BRENDA, the Enzyme Database: 2.3.1.91
            CAS: 85205-00-1
///
ENTRY       EC 2.3.1.92                 Enzyme
NAME        sinapoylglucose---malate O-sinapoyltransferase;
            1-sinapoylglucose-L-malate sinapoyltransferase;
            sinapoylglucose:malate sinapoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     1-O-sinapoyl-beta-D-glucose:(S)-malate O-sinapoyltransferase
REACTION    1-O-sinapoyl-beta-D-glucose + (S)-malate = D-glucose +
            sinapoyl-(S)-malate [RN:R03323]
ALL_REAC    R03323
SUBSTRATE   1-O-sinapoyl-beta-D-glucose [CPD:C01175];
            (S)-malate [CPD:C00149]
PRODUCT     D-glucose [CPD:C00031];
            sinapoyl-(S)-malate [CPD:C02887]
REFERENCE   1
  AUTHORS   Strack, D.
  TITLE     Development of 1-O-sinapoyl-beta-D-glucose-l-malate
            sinapoyltransferase activity in cotyledons of red radish (Raphanus
            sativus L. var sativus).
  JOURNAL   Planta 155 (1982) 31-36.
  ORGANISM  Raphanus sativus
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
ORTHOLOGY   KO: K09757  sinapoylglucose-malate O-sinapoyltransferase
GENES       ATH: AT2G22990(SNG1)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.92
            ExPASy - ENZYME nomenclature database: 2.3.1.92
            ExplorEnz - The Enzyme Database: 2.3.1.92
            ERGO genome analysis and discovery system: 2.3.1.92
            BRENDA, the Enzyme Database: 2.3.1.92
            CAS: 76095-65-3
///
ENTRY       EC 2.3.1.93                 Enzyme
NAME        13-hydroxylupinine O-tigloyltransferase;
            tigloyl-CoA:13-hydroxylupanine O-tigloyltransferase;
            13-hydroxylupanine acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     (E)-2-methylcrotonoyl-CoA:13-hydroxylupinine
            O-2-methylcrotonoyltransferase
REACTION    (E)-2-methylcrotonoyl-CoA + 13-hydroxylupinine = CoA +
            13-(2-methylcrotonoyl)oxylupinine [RN:R04205]
ALL_REAC    R04205
SUBSTRATE   (E)-2-methylcrotonoyl-CoA [CPD:C03345];
            13-hydroxylupinine [CPD:C02621]
PRODUCT     CoA [CPD:C00010];
            13-(2-methylcrotonoyl)oxylupinine [CPD:C04170]
COMMENT     Benzoyl-CoA and, more slowly, pentanoyl-CoA, 3-methylbutanoyl-CoA
            and butanoyl-CoA can act as acyl donors. Involved in the synthesis
            of lupinine alkaloids.
REFERENCE   1
  AUTHORS   Wink, M. and Hartmann, T.
  TITLE     Enzymatic synthesis of quinolizidine alkaloid esters: a
            tigloyl-CoA:13-hydroxylupanine O-tigloyl transferase from Lupinus
            albus L.
  JOURNAL   Planta 156 (1982) 560-565.
  ORGANISM  Lupinus albus
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.93
            ExPASy - ENZYME nomenclature database: 2.3.1.93
            ExplorEnz - The Enzyme Database: 2.3.1.93
            ERGO genome analysis and discovery system: 2.3.1.93
            BRENDA, the Enzyme Database: 2.3.1.93
            CAS: 85341-00-0
///
ENTRY       EC 2.3.1.94                 Enzyme
NAME        erythronolide synthase;
            erythronolide condensing enzyme;
            malonyl-CoA:propionyl-CoA malonyltransferase (cyclizing)
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     malonyl-CoA:propanoyl-CoA malonyltransferase (cyclizing)
REACTION    6 malonyl-CoA + propanoyl-CoA = 7 CoA + 6-deoxyerythronolide b
            [RN:R00918]
ALL_REAC    R00918
SUBSTRATE   malonyl-CoA [CPD:C00083];
            propanoyl-CoA [CPD:C00100]
PRODUCT     CoA [CPD:C00010];
            6-deoxyerythronolide b [CPD:C03240]
COMMENT     The product, which contains a 14-membered lactone ring, is an
            intermediate in the biosynthesis of erythromycin antibiotics. cf. EC
            2.3.1.74 naringenin-chalcone synthase.
REFERENCE   1
  AUTHORS   Omura, S. and Nakagawa, A.
  TITLE     Biosynthesis of 16-membered macrolide antibiotics.
  JOURNAL   Antibiotics 4 (1981) 175-192.
REFERENCE   2
  AUTHORS   Roberts, G. and Leadley, P.F.
  TITLE     Use of [3H]tetrahydrocerulenin to assay condensing enzyme activity
            in Streptomyces erythreus.
  JOURNAL   Biochem. Soc. Trans. 12 (1984) 642-643.
  ORGANISM  Streptomyces erythreus
PATHWAY     PATH: map00522  Biosynthesis of 12-, 14- and 16-membered macrolides
GENES       SAZ: Sama_1115
            SBM: Shew185_1419
            SPC: Sputcn32_1326
            SSE: Ssed_3202
            SPL: Spea_2907
            SHW: Sputw3181_2777
            PIN: Ping_1684(pfaA)
            BUR: Bcep18194_A3873
            GUR: Gura_2012 Gura_3094 Gura_3096
            RRU: Rru_A2120
            CBE: Cbei_0251
            MAV: MAV_2011 MAV_2450 MAV_3108
            FAL: FRAAL0348 FRAAL0349 FRAAL4071
            SEN: SACE_4475
            STP: Strop_1022
            AVA: Ava_2590 Ava_2591 Ava_2592 Ava_2593 Ava_3985 Ava_4108
                 Ava_4742 Ava_4744 Ava_4745 Ava_4747 Ava_4749 Ava_4750 Ava_4834
STRUCTURES  PDB: 1KEZ  1MO2  1PZQ  1PZR  2HG4  2JU1  2JU2  2QO3  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.94
            ExPASy - ENZYME nomenclature database: 2.3.1.94
            ExplorEnz - The Enzyme Database: 2.3.1.94
            ERGO genome analysis and discovery system: 2.3.1.94
            BRENDA, the Enzyme Database: 2.3.1.94
            CAS: 87683-77-0
///
ENTRY       EC 2.3.1.95                 Enzyme
NAME        trihydroxystilbene synthase;
            resveratrol synthase;
            stilbene synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     malonyl-CoA:4-coumaroyl-CoA malonyltransferase (cyclizing)
REACTION    3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + 3,4',5-trihydroxy-stilbene
            + 4 CO2 [RN:R01614]
ALL_REAC    R01614
SUBSTRATE   malonyl-CoA [CPD:C00083];
            4-coumaroyl-CoA [CPD:C00223]
PRODUCT     CoA [CPD:C00010];
            3,4',5-trihydroxy-stilbene;
            CO2 [CPD:C00011]
COMMENT     Not identical with EC 2.3.1.74 naringenin-chalcone synthase or EC
            2.3.1.146 pinosylvin synthase.
REFERENCE   1  [PMID:6427224]
  AUTHORS   Schoppner A, Kindl H.
  TITLE     Purification and properties of a stilbene synthase from induced cell
            suspension cultures of peanut.
  JOURNAL   J. Biol. Chem. 259 (1984) 6806-11.
  ORGANISM  Arachis hypogaea
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
STRUCTURES  PDB: 1Z1E  1Z1F  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.95
            ExPASy - ENZYME nomenclature database: 2.3.1.95
            ExplorEnz - The Enzyme Database: 2.3.1.95
            ERGO genome analysis and discovery system: 2.3.1.95
            BRENDA, the Enzyme Database: 2.3.1.95
            CAS: 128449-70-7
///
ENTRY       EC 2.3.1.96                 Enzyme
NAME        glycoprotein N-palmitoyltransferase;
            mucus glycoprotein fatty acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     palmitoyl-CoA:glycoprotein N-palmitoyltransferase
REACTION    palmitoyl-CoA + glycoprotein = CoA + N-palmitoylglycoprotein
            [RN:R01952]
ALL_REAC    R01952
SUBSTRATE   palmitoyl-CoA [CPD:C00154];
            glycoprotein [CPD:C00326]
PRODUCT     CoA [CPD:C00010];
            N-palmitoylglycoprotein [CPD:C03412]
EFFECTOR    Dithiothreitol [CPD:C00265]
COMMENT     Acts on mucins. Activated by 1,4-dithiothreitol.
REFERENCE   1  [PMID:4018446]
  AUTHORS   Liau YH, Slomiany BL, Slomiany A, Piasek A, Palmer D, Rosenthal WS.
  TITLE     Identification of mucus glycoprotein fatty acyltransferase activity
            in human gastric mucosa.
  JOURNAL   Digestion. 32 (1985) 57-62.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00530  Aminosugars metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.96
            ExPASy - ENZYME nomenclature database: 2.3.1.96
            ExplorEnz - The Enzyme Database: 2.3.1.96
            ERGO genome analysis and discovery system: 2.3.1.96
            BRENDA, the Enzyme Database: 2.3.1.96
            CAS: 97162-74-8
///
ENTRY       EC 2.3.1.97                 Enzyme
NAME        glycylpeptide N-tetradecanoyltransferase;
            peptide N-myristoyltransferase;
            myristoyl-CoA-protein N-myristoyltransferase;
            myristoyl-coenzyme A:protein N-myristoyl transferase;
            myristoylating enzymes;
            protein N-myristoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     tetradecanoyl-CoA:glycylpeptide N-tetradecanoyltransferase
REACTION    tetradecanoyl-CoA + glycylpeptide = CoA +
            N-tetradecanoylglycylpeptide [RN:R03992]
ALL_REAC    R03992
SUBSTRATE   tetradecanoyl-CoA [CPD:C02593];
            glycylpeptide [CPD:C02038]
PRODUCT     CoA [CPD:C00010];
            N-tetradecanoylglycylpeptide [CPD:C03881]
COMMENT     The enzyme from yeast is highly specific for tetradecanoyl-CoA, and
            highly specific for N-terminal glycine in oligopeptides containing
            serine in the 5-position. The enzyme from mammalian heart transfers
            acyl groups to a specific 51 kDa acceptor protein.
REFERENCE   1  [PMID:3566958]
  AUTHORS   Guertin D, Grise-Miron L, Riendeau D.
  TITLE     Identification of a 51-kilodalton polypeptide fatty acyl chain
            acceptor in soluble extracts from mouse cardiac tissue.
  JOURNAL   Biochem. Cell. Biol. 64 (1986) 1249-55.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:3123489]
  AUTHORS   Heuckeroth RO, Towler DA, Adams SP, Glaser L, Gordon JI.
  TITLE     11-(Ethylthio)undecanoic acid. A myristic acid analogue of altered
            hydrophobicity which is functional for peptide N-myristoylation with
            wheat germ and yeast acyltransferase.
  JOURNAL   J. Biol. Chem. 263 (1988) 2127-33.
  ORGANISM  Triticum aestivum [GN:etae], Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K00671  glycylpeptide N-tetradecanoyltransferase
GENES       HSA: 4836(NMT1) 9397(NMT2)
            PTR: 450321(NMT2)
            MMU: 18107(Nmt1) 18108(Nmt2)
            RNO: 259274(Nmt1)
            CFA: 480494(NMT1)
            BTA: 281351(NMT1) 282049(NMT2)
            GGA: 419966(NMT1) 420529(NMT2)
            XLA: 379884(nmt1) 444545(MGC83363)
            SPU: 755543(LOC755543)
            DME: Dmel_CG7436(Nmt)
            CEL: T17E9.2
            ATH: AT5G57020(NMT1)
            OSA: 4327681
            CME: CMC071C
            SCE: YLR195C(NMT1)
            AGO: AGOS_AAR077C
            PIC: PICST_80771(NMT1)
            CGR: CAGL0A04059g
            SPO: SPBC2G2.11
            ANI: AN3839.2
            AFM: AFUA_4G08070
            AOR: AO090023000762
            CNE: CNN00080
            UMA: UM02657.1
            DDI: DDBDRAFT_0217694
            PFA: PF14_0127
            CPV: cgd3_320
            CHO: Chro.30047
            TAN: TA13465
            TPV: TP02_0057
            TET: TTHERM_00825080
            TBR: Tb10.61.2550
            TCR: 506525.80 511283.90
            LMA: LmjF32.0080
            EHI: 88.t00002
STRUCTURES  PDB: 1IIC  1IID  1IYK  1IYL  1RXT  2NMT  2P6E  2P6F  2P6G  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.97
            ExPASy - ENZYME nomenclature database: 2.3.1.97
            ExplorEnz - The Enzyme Database: 2.3.1.97
            ERGO genome analysis and discovery system: 2.3.1.97
            BRENDA, the Enzyme Database: 2.3.1.97
            CAS: 110071-61-9
///
ENTRY       EC 2.3.1.98                 Enzyme
NAME        chlorogenate---glucarate O-hydroxycinnamoyltransferase;
            chlorogenate:glucarate caffeoyltransferase;
            chlorogenic acid:glucaric acid O-caffeoyltransferase;
            chlorogenate:glucarate caffeoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     chlorogenate:glucarate O-(hydroxycinnamoyl)transferase
REACTION    chlorogenate + glucarate = quinate + 2-O-caffeoylglucarate
            [RN:R02998]
ALL_REAC    R02998
SUBSTRATE   chlorogenate [CPD:C00852];
            glucarate [CPD:C00767]
PRODUCT     quinate [CPD:C00296];
            2-O-caffeoylglucarate [CPD:C03062]
COMMENT     Galactarate can act as acceptor, more slowly. Involved with EC
            2.3.1.99 quinate O-hydroxycinnamoyltransferase in the formation of
            caffeoylglucarate in tomato.
REFERENCE   1  [PMID:16667263]
  AUTHORS   Strack D, Gross W.
  TITLE     Properties and Activity Changes of Chlorogenic Acid:Glucaric Acid
            Caffeoyltransferase From Tomato (Lycopersicon esculentum).
  JOURNAL   Plant. Physiol. 92 (1990) 41-47.
  ORGANISM  Lycopersicon esculentum [GN:eles]
REFERENCE   2  [PMID:16665274]
  AUTHORS   Strack D, Gross W, Wray V, Grotjahn L.
  TITLE     Enzymic Synthesis of Caffeoylglucaric Acid from Chlorogenic Acid and
            Glucaric Acid by a Protein Preparation from Tomato Cotyledons.
  JOURNAL   Plant. Physiol. 83 (1987) 475-478.
  ORGANISM  Lycopersicon esculentum [GN:eles]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.98
            ExPASy - ENZYME nomenclature database: 2.3.1.98
            ExplorEnz - The Enzyme Database: 2.3.1.98
            ERGO genome analysis and discovery system: 2.3.1.98
            BRENDA, the Enzyme Database: 2.3.1.98
            CAS: 126124-92-3
///
ENTRY       EC 2.3.1.99                 Enzyme
NAME        quinate O-hydroxycinnamoyltransferase;
            hydroxycinnamoyl coenzyme A-quinate transferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     feruloyl-CoA:quinate O-(hydroxycinnamoyl)transferase
REACTION    feruloyl-CoA + quinate = CoA + O-feruloylquinate [RN:R02195]
ALL_REAC    R02195;
            (other) R01945
SUBSTRATE   feruloyl-CoA [CPD:C00406];
            quinate [CPD:C00296]
PRODUCT     CoA [CPD:C00010];
            O-feruloylquinate [CPD:C02572]
COMMENT     Caffeoyl-CoA and 4-coumaroyl-CoA can also act as donors, but more
            slowly. Involved in the biosynthesis of chlorogenic acid in sweet
            potato and, with EC 2.3.1.98 chlorogenate---glucarate
            O-hydroxycinnamoyltransferase, in the formation of caffeoyl-CoA in
            tomato.
REFERENCE   1  [PMID:16665274]
  AUTHORS   Strack D, Gross W, Wray V, Grotjahn L.
  TITLE     Enzymic Synthesis of Caffeoylglucaric Acid from Chlorogenic Acid and
            Glucaric Acid by a Protein Preparation from Tomato Cotyledons.
  JOURNAL   Plant. Physiol. 83 (1987) 475-478.
  ORGANISM  Lycopersicon esculentum [GN:eles]
REFERENCE   2
  AUTHORS   Strack, D., Keller, H. and Weissenbock, G.
  TITLE     Enzymatic-synthesis of hydroxycinnamic acid-esters of sugar acids
            and hydroaromatic acids by protein preparations from rye (Secale
            cereale) primary leaves.
  JOURNAL   J. Plant Physiol. 131 (1987) 61-73.
  ORGANISM  Secale cereale
REFERENCE   3  [PMID:3722170]
  AUTHORS   Villegas RJ, Kojima M.
  TITLE     Purification and characterization of hydroxycinnamoyl D-glucose.
            Quinate hydroxycinnamoyl transferase in the root of sweet potato,
            Ipomoea batatas Lam.
  JOURNAL   J. Biol. Chem. 261 (1986) 8729-33.
  ORGANISM  Ipomoea batatas
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
GENES       MMS: mma_2557
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.99
            ExPASy - ENZYME nomenclature database: 2.3.1.99
            ExplorEnz - The Enzyme Database: 2.3.1.99
            ERGO genome analysis and discovery system: 2.3.1.99
            BRENDA, the Enzyme Database: 2.3.1.99
            CAS: 60321-02-0
///
ENTRY       EC 2.3.1.100                Enzyme
NAME        [myelin-proteolipid] O-palmitoyltransferase;
            myelin PLP acyltransferase;
            acyl-protein synthetase;
            myelin-proteolipid O-palmitoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     palmitoyl-CoA:[myelin-proteolipid] O-palmitoyltransferase
REACTION    palmitoyl-CoA + [myelin proteolipid] = CoA + O-palmitoyl-[myelin
            proteolipid] [RN:R04022]
ALL_REAC    R04022
SUBSTRATE   palmitoyl-CoA [CPD:C00154];
            myelin proteolipid [CPD:C02706]
PRODUCT     CoA [CPD:C00010];
            O-palmitoyl-[myelin proteolipid] [CPD:C04386]
COMMENT     The enzyme in brain transfers long-chain acyl residues to the
            endogenous myelin proteolipid
REFERENCE   1  [PMID:3818589]
  AUTHORS   Bizzozero OA, McGarry JF, Lees MB.
  TITLE     Acylation of endogenous myelin proteolipid protein with different
            acyl-CoAs.
  JOURNAL   J. Biol. Chem. 262 (1987) 2138-45.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.100
            ExPASy - ENZYME nomenclature database: 2.3.1.100
            ExplorEnz - The Enzyme Database: 2.3.1.100
            ERGO genome analysis and discovery system: 2.3.1.100
            BRENDA, the Enzyme Database: 2.3.1.100
            CAS: 82657-98-5
///
ENTRY       EC 2.3.1.101                Enzyme
NAME        formylmethanofuran-tetrahydromethanopterin N-formyltransferase;
            formylmethanofuran-tetrahydromethanopterin formyltransferase;
            formylmethanofuran:tetrahydromethanopterin formyltransferase;
            N-formylmethanofuran(CHO-MFR):tetrahydromethanopterin(H4MPT)
            formyltransferase;
            FTR;
            formylmethanofuran:5,6,7,8-tetrahydromethanopterin
            N5-formyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     formylmethanofuran:5,6,7,8-tetrahydromethanopterin
            5-formyltransferase
REACTION    formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran
            + 5-formyl-5,6,7,8-tetrahydromethanopterin [RN:R03390]
ALL_REAC    R03390
SUBSTRATE   formylmethanofuran [CPD:C01001];
            5,6,7,8-tetrahydromethanopterin [CPD:C01217]
PRODUCT     methanofuran [CPD:C00862];
            5-formyl-5,6,7,8-tetrahydromethanopterin [CPD:C01274]
COMMENT     Methanofuran is a complex 4-substituted furfurylamine and is
            involved in the formation of methane from CO2 in Methanobacterium
            thermoautotrophicum.
REFERENCE   1  [PMID:3097011]
  AUTHORS   Donnelly MI, Wolfe RS.
  TITLE     The role of formylmethanofuran: tetrahydromethanopterin
            formyltransferase in methanogenesis from carbon dioxide.
  JOURNAL   J. Biol. Chem. 261 (1986) 16653-9.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
REFERENCE   2
  AUTHORS   Leigh, J.A., Rinehart, K.L. and Wolfe, R.S.
  TITLE     Structure of methanofuran, the carbon-dioxide reduction factor of
            Methanobacterium thermoautotrophicum.
  JOURNAL   J. Am. Chem. Soc. 106 (1984) 3636-3640.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K00672  formylmethanofuran--tetrahydromethanopterin
                        N-formyltransferase
GENES       MCA: MCA2858
            NOC: Noc_0023
            BXE: Bxe_B2463(fhcD)
            MPT: Mpe_A2625
            MFA: Mfla_1664
            XAU: Xaut_1794
            GBE: GbCGDNIH1_0780
            RBA: RB9835(ffsA)
            MMP: MMP1609(ftr)
            MMQ: MmarC5_1799
            MMZ: MmarC7_0857
            MAE: Maeo_0224
            MVN: Mevan_0919
            MAC: MA0010(ftr)
            MBA: Mbar_A0980
            MMA: MM_1321
            MBU: Mbur_1728
            MTP: Mthe_1643
            MHU: Mhun_1808
            MEM: Memar_0628
            MBN: Mboo_0593 Mboo_0993
            MTH: MTH403
            MST: Msp_0070(ftr2) Msp_1502(ftr1)
            MSI: Msm_1092
            MKA: MK0116(ftr_1) MK0816(ftr_2)
            AFU: AF2073(ftr-1) AF2207(ftr)
            RCI: LRC202(ftr)
STRUCTURES  PDB: 1FTR  1M5H  1M5S  2FHJ  2FHK  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.101
            ExPASy - ENZYME nomenclature database: 2.3.1.101
            ExplorEnz - The Enzyme Database: 2.3.1.101
            ERGO genome analysis and discovery system: 2.3.1.101
            UM-BBD (Biocatalysis/Biodegradation Database): 2.3.1.101
            BRENDA, the Enzyme Database: 2.3.1.101
            CAS: 105669-83-8
///
ENTRY       EC 2.3.1.102                Enzyme
NAME        N6-hydroxylysine O-acetyltransferase;
            N6-hydroxylysine:acetyl CoA N6-transacetylase;
            N6-hydroxylysine acetylase;
            acetyl-CoA:6-N-hydroxy-L-lysine 6-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:N6-hydroxy-L-lysine 6-acetyltransferase
REACTION    acetyl-CoA + N6-hydroxy-L-lysine = CoA +
            N6-acetyl-N6-hydroxy-L-lysine [RN:R03168]
ALL_REAC    R03168
SUBSTRATE   acetyl-CoA [CPD:C00024];
            N6-hydroxy-L-lysine [CPD:C01028]
PRODUCT     CoA [CPD:C00010];
            N6-acetyl-N6-hydroxy-L-lysine [CPD:C03955]
COMMENT     Involved in the synthesis of aerobactin from lysine in a strain of
            Escherichia coli.
REFERENCE   1  [PMID:3521734]
  AUTHORS   Coy M, Paw BH, Bindereif A, Neilands JB.
  TITLE     Isolation and properties of N epsilon-hydroxylysine:acetyl coenzyme
            A N epsilon-transacetylase from Escherichia coli pABN11.
  JOURNAL   Biochemistry. 25 (1986) 2485-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:2935523]
  AUTHORS   de Lorenzo V, Bindereif A, Paw BH, Neilands JB.
  TITLE     Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in
            Escherichia coli K-12.
  JOURNAL   J. Bacteriol. 165 (1986) 570-8.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K03896  acetyl CoA:N6-hydroxylysine acetyl transferase
GENES       ECC: c3626(iucB)
            YPE: YPO0991(iucB)
            YPK: y3382(iucB)
            YPM: YP_3449(iucB)
            YPA: YPA_0273
            YPN: YPN_3189
            YPS: YPTB3264(iucB)
            SFL: SF3716(iucB)
            SFX: S4055(iucB)
            SFV: SFV_3853(iucB)
            SSN: SSON_3602(iucB)
            SBO: SBO_4338(iucB)
            VFI: VFA0162
            PEN: PSEEN1813(pvdZ)
            NOC: Noc_1813(iucB)
            BUR: Bcep18194_A4792
            BBA: Bd1575(iucB)
            RET: RHE_PF00459(vbsA)
            RLE: pRL120316
            GBE: GbCGDNIH1_2377
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.102
            ExPASy - ENZYME nomenclature database: 2.3.1.102
            ExplorEnz - The Enzyme Database: 2.3.1.102
            ERGO genome analysis and discovery system: 2.3.1.102
            BRENDA, the Enzyme Database: 2.3.1.102
            CAS: 101077-53-6
///
ENTRY       EC 2.3.1.103                Enzyme
NAME        sinapoylglucose---sinapoylglucose O-sinapoyltransferase;
            hydroxycinnamoylglucose-hydroxycinnamoylglucose
            hydroxycinnamoyltransferase;
            1-(hydroxycinnamoyl)-glucose:1-(hydroxycinnamoyl)-glucose
            hydroxycinnamoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     1-O-(4-hydroxy-3,5-dimethoxycinnamoyl)-beta-D-glucoside:1-O-(4-hydro
            xy-3,5-dimethoxycinnamoyl-beta-D-glucoside 1-O-sinapoyltransferase
REACTION    2 1-O-sinapoyl beta-D-glucoside = D-glucose + 1,2-bis-O-sinapoyl
            beta-D-glucoside [RN:R00063]
ALL_REAC    R00063
SUBSTRATE   1-O-sinapoyl beta-D-glucoside [CPD:C03915]
PRODUCT     D-glucose [CPD:C00031];
            1,2-bis-O-sinapoyl beta-D-glucoside
REFERENCE   1
  AUTHORS   Dahlbender, B. and Strack, D.
  TITLE     Purification and properties of
            1-(hydroxycinnamoyl)-glucose-1-(hydroxycinnamoyl)-glucose
            hydroxycinnamoyl-transferase from radish seedlings.
  JOURNAL   Phytochemistry 25 (1986) 1043-1046.
  ORGANISM  Raphanus sativus
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.103
            ExPASy - ENZYME nomenclature database: 2.3.1.103
            ExplorEnz - The Enzyme Database: 2.3.1.103
            ERGO genome analysis and discovery system: 2.3.1.103
            BRENDA, the Enzyme Database: 2.3.1.103
            CAS: 103537-11-7
///
ENTRY       EC 2.3.1.104                Enzyme
NAME        1-alkenylglycerophosphocholine O-acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:1-alkenylglycerophosphocholine O-acyltransferase
REACTION    acyl-CoA + 1-alkenylglycerophosphocholine = CoA +
            1-alkenyl-2-acylglycerophosphocholine [RN:R03109]
ALL_REAC    R03109
SUBSTRATE   acyl-CoA [CPD:C00040];
            1-alkenylglycerophosphocholine [CPD:C04517]
PRODUCT     CoA [CPD:C00010];
            1-alkenyl-2-acylglycerophosphocholine [CPD:C00958]
COMMENT     Not identical with EC 2.3.1.121 1-alkenylglycerophosphoethanolamine
            O-acyltransferase.
REFERENCE   1  [PMID:3753462]
  AUTHORS   Arthur G, Choy PC.
  TITLE     Acylation of 1-alkenyl-glycerophosphocholine and
            1-acyl-glycerophosphocholine in guinea pig heart.
  JOURNAL   Biochem. J. 236 (1986) 481-7.
  ORGANISM  guinea pig
PATHWAY     PATH: map00565  Ether lipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.104
            ExPASy - ENZYME nomenclature database: 2.3.1.104
            ExplorEnz - The Enzyme Database: 2.3.1.104
            ERGO genome analysis and discovery system: 2.3.1.104
            BRENDA, the Enzyme Database: 2.3.1.104
            CAS: 102925-32-6
///
ENTRY       EC 2.3.1.105                Enzyme
NAME        alkylglycerophosphate 2-O-acetyltransferase;
            alkyllyso-GP:acetyl-CoA acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:1-alkyl-sn-glycero-3-phosphate 2-O-acetyltransferase
REACTION    acetyl-CoA + 1-alkyl-sn-glycero-3-phosphate = CoA +
            1-alkyl-2-acetyl-sn-glycero-3-phosphate [RN:R03455]
ALL_REAC    R03455
SUBSTRATE   acetyl-CoA [CPD:C00024];
            1-alkyl-sn-glycero-3-phosphate [CPD:C03968]
PRODUCT     CoA [CPD:C00010];
            1-alkyl-2-acetyl-sn-glycero-3-phosphate
COMMENT     Involved in the biosynthesis of thrombocyte activating factor in
            animal tissues.
REFERENCE   1  [PMID:3007498]
  AUTHORS   Lee TC, Malone B, Snyder F.
  TITLE     A new de novo pathway for the formation of
            1-alkyl-2-acetyl-sn-glycerols, precursors of platelet activating
            factor. Biochemical characterization of
            1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase in rat
            spleen.
  JOURNAL   J. Biol. Chem. 261 (1986) 5373-7.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00565  Ether lipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.105
            ExPASy - ENZYME nomenclature database: 2.3.1.105
            ExplorEnz - The Enzyme Database: 2.3.1.105
            ERGO genome analysis and discovery system: 2.3.1.105
            BRENDA, the Enzyme Database: 2.3.1.105
            CAS: 76773-96-1
///
ENTRY       EC 2.3.1.106                Enzyme
NAME        tartronate O-hydroxycinnamoyltransferase;
            tartronate sinapoyltransferase;
            hydroxycinnamoyl-coenzyme-A:tartronate hydroxycinnamoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     sinapoyl-CoA:2-hydroxymalonate O-(hydroxycinnamoyl)transferase
REACTION    sinapoyl-CoA + 2-hydroxymalonate = CoA + sinapoyltartronate
            [RN:R03965]
ALL_REAC    R03965
SUBSTRATE   sinapoyl-CoA [CPD:C00411];
            2-hydroxymalonate [CPD:C02500]
PRODUCT     CoA [CPD:C00010];
            sinapoyltartronate [CPD:C02750]
COMMENT     4-Coumaroyl-CoA (4-hydroxycinnamoyl-CoA), caffeoyl-CoA
            (3,4-dihydroxycinnamoyl-CoA) and feruloyl-CoA
            (4-hydroxy-3-methoxycinnamoyl-CoA) can also act as donors for the
            enzyme from the mung bean (Vigna radiata).
REFERENCE   1
  AUTHORS   Strack, D., Ruhoff, R. and Grawe, W.
  TITLE     Hydroxycinnamoyl-Coenzyme-A-tartronate hydroxycinnamoyltransferase
            in protein preparations from mung bean.
  JOURNAL   Phytochemistry 25 (1986) 833-837.
  ORGANISM  Phaseolus radiatus
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.106
            ExPASy - ENZYME nomenclature database: 2.3.1.106
            ExplorEnz - The Enzyme Database: 2.3.1.106
            ERGO genome analysis and discovery system: 2.3.1.106
            BRENDA, the Enzyme Database: 2.3.1.106
            CAS: 102484-57-1
///
ENTRY       EC 2.3.1.107                Enzyme
NAME        deacetylvindoline O-acetyltransferase;
            deacetylvindoline acetyltransferase;
            DAT;
            17-O-deacetylvindoline-17-O-acetyltransferase;
            acetylcoenzyme A-deacetylvindoline 4-O-acetyltransferase;
            acetyl-CoA-17-O-deacetylvindoline 17-O-acetyltransferase;
            acetylcoenzyme A:deacetylvindoline 4-O-acetyltransferase;
            acetylcoenzyme A:deacetylvindoline O-acetyltransferase;
            17-O-deacetylvindoline O-acetyltransferase;
            acetyl-CoA:17-O-deacetylvindoline 17-O-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:deacetylvindoline 4-O-acetyltransferase
REACTION    acetyl-CoA + deacetylvindoline = CoA + vindoline [RN:R03230]
ALL_REAC    R03230
SUBSTRATE   acetyl-CoA [CPD:C00024];
            deacetylvindoline [CPD:C01091]
PRODUCT     CoA [CPD:C00010];
            vindoline [CPD:C01626]
COMMENT     Catalyses the final step in the biosynthesis of vindoline from
            tabersonine in the Madagascar periwinkle, Catharanthus roseus.
REFERENCE   1
  AUTHORS   Fahn, W., Gundlach, H., Deus-Neumann, B. and Stockigt, J.
  TITLE     Late enzymes of vindoline biosynthesis.
            Acetyl-CoA:17-O-deactylvindoline 17-O-acetyl-transferase.
  JOURNAL   Plant Cell Rep. 4 (1985) 333-336.
  ORGANISM  Catharanthus roseus
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.107
            ExPASy - ENZYME nomenclature database: 2.3.1.107
            ExplorEnz - The Enzyme Database: 2.3.1.107
            ERGO genome analysis and discovery system: 2.3.1.107
            BRENDA, the Enzyme Database: 2.3.1.107
            CAS: 100630-41-9
///
ENTRY       EC 2.3.1.108                Enzyme
NAME        alpha-tubulin N-acetyltransferase;
            alpha-tubulin acetylase;
            TAT;
            alpha-tubulin acetyltransferase;
            tubulin N-acetyltransferase;
            acetyl-CoA:alpha-tubulin-L-lysine N-acetyltransferase;
            acetyl-CoA:[alpha-tubulin]-L-lysine 6-N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:[alpha-tubulin]-L-lysine N6-acetyltransferase
REACTION    acetyl-CoA + [alpha-tubulin]-L-lysine = CoA +
            [alpha-tubulin]-N6-acetyl-L-lysine [RN:R04192]
ALL_REAC    R04192
SUBSTRATE   acetyl-CoA [CPD:C00024];
            [alpha-tubulin]-L-lysine
PRODUCT     CoA [CPD:C00010];
            [alpha-tubulin]-N6-acetyl-L-lysine
COMMENT     The enzyme from Chlamydomonas flagella also acetylates mammalian
            brain alpha-tubulin.
REFERENCE   1  [PMID:4066751]
  AUTHORS   Greer K, Maruta H, L'Hernault SW, Rosenbaum JL.
  TITLE     Alpha-tubulin acetylase activity in isolated Chlamydomonas flagella.
  JOURNAL   J. Cell. Biol. 101 (1985) 2081-4.
  ORGANISM  Chlamydomonas flagella
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.108
            ExPASy - ENZYME nomenclature database: 2.3.1.108
            ExplorEnz - The Enzyme Database: 2.3.1.108
            ERGO genome analysis and discovery system: 2.3.1.108
            BRENDA, the Enzyme Database: 2.3.1.108
            CAS: 99889-90-4
///
ENTRY       EC 2.3.1.109                Enzyme
NAME        arginine N-succinyltransferase;
            arginine succinyltransferase;
            AstA;
            arginine and ornithine N2-succinyltransferase;
            AOST;
            AST;
            succinyl-CoA:L-arginine 2-N-succinyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     succinyl-CoA:L-arginine N2-succinyltransferase
REACTION    succinyl-CoA + L-arginine = CoA + N2-succinyl-L-arginine [RN:R00832]
ALL_REAC    R00832
SUBSTRATE   succinyl-CoA [CPD:C00091];
            L-arginine [CPD:C00062]
PRODUCT     CoA [CPD:C00010];
            N2-succinyl-L-arginine [CPD:C03296]
COMMENT     Also acts on L-ornithine. This is the first enzyme in the arginine
            succinyltransferase (AST) pathway for the catabolism of arginine
            [1]. This pathway converts the carbon skeleton of arginine into
            glutamate, with the concomitant production of ammonia and conversion
            of succinyl-CoA into succinate and CoA. The five enzymes involved in
            this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC
            3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.81
            (succinylornithine transaminase), EC 1.2.1.71
            (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96
            (succinylglutamate desuccinylase) [2,6].
REFERENCE   1  [PMID:3144259]
  AUTHORS   Vander Wauven C, Jann A, Haas D, Leisinger T, Stalon V.
  TITLE     N2-succinylornithine in ornithine catabolism of Pseudomonas
            aeruginosa.
  JOURNAL   Arch. Microbiol. 150 (1988) 400-4.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   2  [PMID:2865249]
  AUTHORS   Vander Wauven C, Stalon V.
  TITLE     Occurrence of succinyl derivatives in the catabolism of arginine in
            Pseudomonas cepacia.
  JOURNAL   J. Bacteriol. 164 (1985) 882-6.
  ORGANISM  Pseudomonas cepacia
REFERENCE   3  [PMID:7523119]
  AUTHORS   Tricot C, Vander Wauven C, Wattiez R, Falmagne P, Stalon V.
  TITLE     Purification and properties of a succinyltransferase from
            Pseudomonas aeruginosa specific for both arginine and ornithine.
  JOURNAL   Eur. J. Biochem. 224 (1994) 853-61.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   4  [PMID:9393691]
  AUTHORS   Itoh Y.
  TITLE     Cloning and characterization of the aru genes encoding enzymes of
            the catabolic arginine succinyltransferase pathway in Pseudomonas
            aeruginosa.
  JOURNAL   J. Bacteriol. 179 (1997) 7280-90.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   5  [PMID:9696779]
  AUTHORS   Schneider BL, Kiupakis AK, Reitzer LJ.
  TITLE     Arginine catabolism and the arginine succinyltransferase pathway in
            Escherichia coli.
  JOURNAL   J. Bacteriol. 180 (1998) 4278-86.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:3534538]
  AUTHORS   Cunin R, Glansdorff N, Pierard A, Stalon V.
  TITLE     Biosynthesis and metabolism of arginine in bacteria.
  JOURNAL   Microbiol. Rev. 50 (1986) 314-52.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   7
  AUTHORS   Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V.
  TITLE     Erratum report: Biosynthesis and metabolism of arginine in bacteria.
  JOURNAL   Microbiol. Rev. 51 (1987) 178.
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K00673  arginine N-succinyltransferase
GENES       ECO: b1747(astA)
            ECJ: JW1736(astA)
            ECE: Z2779
            ECS: ECs2453
            ECC: c2147
            ECI: UTI89_C1942(astA)
            ECP: ECP_1693
            ECV: APECO1_816(astA)
            ECW: EcE24377A_1969(astA)
            ECX: EcHS_A1830
            STY: STY1810(astA)
            SPT: SPA1540(astA)
            SEC: SC1327(astA)
            STM: STM1304(astA)
            YPE: YPO1963(astA)
            YPK: y2348
            YPM: YP_1708(astA)
            YPA: YPA_1345
            YPP: YPDSF_1160
            YPS: YPTB1960(astA)
            YPI: YpsIP31758_2120(astA)
            SFL: SF1479(astA)
            SFX: S1596
            SFV: SFV_1473
            SSN: SSON_1410
            SBO: SBO_1343
            SDY: SDY_1530
            PLU: plu3109(astA)
            ENT: Ent638_1697
            SPE: Spro_2843
            VCH: VC2617
            VVU: VV1_1314
            VVY: VV3053
            VPA: VP2796
            VFI: VF2283
            PPR: PBPRA0290
            PAE: PA0896(aruF) PA0897(aruG)
            PAU: PA14_52690(aruG) PA14_52700(aruF)
            PAP: PSPA7_4618(astA) PSPA7_4619(aruF)
            PPU: PP_4479(aruG) PP_4480(aruF)
            PPF: Pput_1435 Pput_1436
            PST: PSPTO_1833(aruF) PSPTO_1834(aruG)
            PSB: Psyr_3563 Psyr_3564
            PSP: PSPPH_3519(aruG) PSPPH_3520(aruF)
            PFL: PFL_2241 PFL_2242 PFL_3055(astA) PFL_4513 PFL_4514
            PFO: Pfl_2053 Pfl_2054 Pfl_4283 Pfl_4284
            PEN: PSEEN3880(aruG) PSEEN3881(aruF)
            PMY: Pmen_2909 Pmen_2910
            ACI: ACIAD1286(astA)
            SON: SO_0618(astA)
            SDN: Sden_1055 Sden_3192
            SFR: Sfri_3298
            SAZ: Sama_1627 Sama_3010
            SBL: Sbal_0572
            SBM: Shew185_3753
            SLO: Shew_0579
            SPC: Sputcn32_0646
            SSE: Ssed_0810
            SPL: Spea_3515
            SHE: Shewmr4_0612
            SHM: Shewmr7_3418
            SHN: Shewana3_0611 Shewana3_3548
            SHW: Sputw3181_3528
            ILO: IL2317
            CPS: CPS_0635(astA)
            PHA: PSHAa0195(astA) PSHAb0427
            PAT: Patl_0164 Patl_0650
            MAQ: Maqu_2890 Maqu_3317 Maqu_3318
            LPN: lpg1706
            LPF: lpl1665(astA)
            LPP: lpp1671(astA)
            HCH: HCH_01948(aruF) HCH_01949(aruG)
            CSA: Csal_2806 Csal_2807
            MMW: Mmwyl1_3668 Mmwyl1_3669
            AHA: AHA_3179(astA)
            CVI: CV_1497(aruF) CV_1498(astA)
            BMA: BMA0592 BMA0593
            BMV: BMASAVP1_A2423 BMASAVP1_A2424
            BML: BMA10299_A2867 BMA10299_A2868
            BMN: BMA10247_1734 BMA10247_1735
            BXE: Bxe_A2921 Bxe_A2922
            BVI: Bcep1808_1100 Bcep1808_1101
            BUR: Bcep18194_A4292 Bcep18194_A4293
            BCN: Bcen_0702 Bcen_0703
            BCH: Bcen2424_1181 Bcen2424_1182
            BAM: Bamb_1062 Bamb_1063
            BPS: BPSL2388 BPSL2389
            BPM: BURPS1710b_2845(astA) BURPS1710b_2846(astA)
            BPL: BURPS1106A_2783 BURPS1106A_2784
            BPD: BURPS668_2725 BURPS668_2726
            BTE: BTH_I1776 BTH_I1777(astA)
            BBA: Bd0130(astA)
            ADE: Adeh_0178
            AFW: Anae109_0195
            MXA: MXAN_6454
            CCR: CC_0581 CC_1606
            MMR: Mmar10_1857
            HNE: HNE_1996(astA)
            ZMO: ZMO0657(aruG)
            NAR: Saro_0883
            SAL: Sala_1940
            SWI: Swit_0526 Swit_0528
            ELI: ELI_08920
STRUCTURES  PDB: 1YLE  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.109
            ExPASy - ENZYME nomenclature database: 2.3.1.109
            ExplorEnz - The Enzyme Database: 2.3.1.109
            ERGO genome analysis and discovery system: 2.3.1.109
            BRENDA, the Enzyme Database: 2.3.1.109
            CAS: 99676-48-9
///
ENTRY       EC 2.3.1.110                Enzyme
NAME        tyramine N-feruloyltransferase;
            tyramine N-feruloyl-CoA transferase;
            feruloyltyramine synthase;
            feruloyl-CoA tyramine N-feruloyl-CoA transferase;
            tyramine feruloyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     feruloyl-CoA:tyramine N-(hydroxycinnamoyl)transferase
REACTION    feruloyl-CoA + tyramine = CoA + N-feruloyltyramine [RN:R02385]
ALL_REAC    R02385
SUBSTRATE   feruloyl-CoA [CPD:C00406];
            tyramine [CPD:C00483]
PRODUCT     CoA [CPD:C00010];
            N-feruloyltyramine [CPD:C02717]
COMMENT     Cinnamoyl-CoA, 4-coumaroyl-CoA and sinapoyl-CoA can also act as
            donors, and some aromatic amines can act as acceptors.
REFERENCE   1
  AUTHORS   Negrel, J. and Martin, C.
  TITLE     The biosynthesis of feruloyltyramine in Nicotiana tabacum.
  JOURNAL   Phytochemistry 23 (1984) 2797-2801.
  ORGANISM  Nicotiana tabacum
GENES       BUR: Bcep18194_A4218
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.110
            ExPASy - ENZYME nomenclature database: 2.3.1.110
            ExplorEnz - The Enzyme Database: 2.3.1.110
            ERGO genome analysis and discovery system: 2.3.1.110
            BRENDA, the Enzyme Database: 2.3.1.110
            CAS: 95567-96-7
///
ENTRY       EC 2.3.1.111                Enzyme
NAME        mycocerosate synthase;
            mycocerosic acid synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:methylmalonyl-CoA C-acyltransferase (decarboxylating,
            oxoacyl- and enoyl-reducing)
REACTION    acyl-CoA + n methylmalonyl-CoA + 2n NADPH + 2n H+ =
            multi-methyl-branched acyl-CoA + n CoA + n CO2 + 2n NADP+
            [RN:R05189]
ALL_REAC    R05189
SUBSTRATE   acyl-CoA [CPD:C00040];
            methylmalonyl-CoA [CPD:C02557];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
PRODUCT     multi-methyl-branched acyl-CoA [CPD:C04013];
            CoA [CPD:C00010];
            CO2 [CPD:C00011];
            NADP+ [CPD:C00006]
COMMENT     The enzyme elongates CoA esters of fatty acids from C6 to C20 by
            incorporation of methylmalonyl, but not malonyl, residues, to form
            multimethyl-branched fatty-acyl-CoAs such as
            2,4,6,8-tetramethyl-octanoyl-CoA.
REFERENCE   1  [PMID:3880746]
  AUTHORS   Rainwater DL, Kolattukudy PE.
  TITLE     Fatty acid biosynthesis in Mycobacterium tuberculosis var. bovis
            Bacillus Calmette-Guerin. Purification and characterization of a
            novel fatty acid synthase, mycocerosic acid synthase, which
            elongates n-fatty acyl-CoA with methylmalonyl-CoA.
  JOURNAL   J. Biol. Chem. 260 (1985) 616-23.
  ORGANISM  Mycobacterium tuberculosis
GENES       GUR: Gura_3098
            MAV: MAV_1321 MAV_2370
            MSM: MSMEG_6767
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.111
            ExPASy - ENZYME nomenclature database: 2.3.1.111
            ExplorEnz - The Enzyme Database: 2.3.1.111
            ERGO genome analysis and discovery system: 2.3.1.111
            BRENDA, the Enzyme Database: 2.3.1.111
            CAS: 95229-19-9
///
ENTRY       EC 2.3.1.112                Enzyme
NAME        D-tryptophan N-malonyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     malonyl-CoA:D-tryptophan N-malonyltransferase
REACTION    malonyl-CoA + D-tryptophan = CoA + N2-malonyl-D-tryptophan
            [RN:R02482]
ALL_REAC    R02482
SUBSTRATE   malonyl-CoA [CPD:C00083];
            D-tryptophan [CPD:C00525]
PRODUCT     CoA [CPD:C00010];
            N2-malonyl-D-tryptophan [CPD:C03414]
COMMENT     1-Aminocyclopropane-1-carboxylate can act instead of malonyl-CoA.
REFERENCE   1  [PMID:6497391]
  AUTHORS   Matern U, Feser C, Heller W.
  TITLE     N-malonyltransferases from peanut.
  JOURNAL   Arch. Biochem. Biophys. 235 (1984) 218-27.
  ORGANISM  Arachis hypogaea
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.112
            ExPASy - ENZYME nomenclature database: 2.3.1.112
            ExplorEnz - The Enzyme Database: 2.3.1.112
            ERGO genome analysis and discovery system: 2.3.1.112
            BRENDA, the Enzyme Database: 2.3.1.112
            CAS: 94490-01-4
///
ENTRY       EC 2.3.1.113                Enzyme
NAME        anthranilate N-malonyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     malonyl-CoA:anthranilate N-malonyltransferase
REACTION    malonyl-CoA + anthranilate = CoA + N-malonylanthranilate [RN:R00989]
ALL_REAC    R00989
SUBSTRATE   malonyl-CoA [CPD:C00083];
            anthranilate [CPD:C00108]
PRODUCT     CoA [CPD:C00010];
            N-malonylanthranilate [CPD:C03147]
REFERENCE   1  [PMID:6497391]
  AUTHORS   Matern U, Feser C, Heller W.
  TITLE     N-malonyltransferases from peanut.
  JOURNAL   Arch. Biochem. Biophys. 235 (1984) 218-27.
  ORGANISM  Arachis hypogaea
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.113
            ExPASy - ENZYME nomenclature database: 2.3.1.113
            ExplorEnz - The Enzyme Database: 2.3.1.113
            ERGO genome analysis and discovery system: 2.3.1.113
            BRENDA, the Enzyme Database: 2.3.1.113
            CAS: 94489-98-2
///
ENTRY       EC 2.3.1.114                Enzyme
NAME        3,4-dichloroaniline N-malonyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     malonyl-CoA:3,4-dichloroaniline N-malonyltransferase
REACTION    malonyl-CoA + 3,4-dichloroaniline = CoA +
            N-(3,4-dichlorophenyl)-malonamate [RN:R04050]
ALL_REAC    R04050
SUBSTRATE   malonyl-CoA [CPD:C00083];
            3,4-dichloroaniline [CPD:C02791]
PRODUCT     CoA [CPD:C00010];
            N-(3,4-dichlorophenyl)-malonamate [CPD:C04205]
REFERENCE   1  [PMID:6497391]
  AUTHORS   Matern U, Feser C, Heller W.
  TITLE     N-malonyltransferases from peanut.
  JOURNAL   Arch. Biochem. Biophys. 235 (1984) 218-27.
  ORGANISM  Arachis hypogaea
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.114
            ExPASy - ENZYME nomenclature database: 2.3.1.114
            ExplorEnz - The Enzyme Database: 2.3.1.114
            ERGO genome analysis and discovery system: 2.3.1.114
            BRENDA, the Enzyme Database: 2.3.1.114
            CAS: 94489-99-3
///
ENTRY       EC 2.3.1.115                Enzyme
NAME        isoflavone-7-O-beta-glucoside 6"-O-malonyltransferase;
            flavone/flavonol 7-O-beta-D-glucoside malonyltransferase;
            flavone (flavonol) 7-O-glycoside malonyltransferase;
            malonyl-CoA:flavone/flavonol 7-O-glucoside malonyltransferase;
            MAT-7;
            malonyl-coenzyme A:isoflavone 7-O-glucoside-6"-malonyltransferase;
            malonyl-coenzyme A:flavone/flavonol-7-O-glycoside malonyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     malonyl-CoA:isoflavone-7-O-beta-D-glucoside 6"-O-malonyltransferase
REACTION    malonyl-CoA + biochanin A 7-O-beta-D-glucoside = CoA + biochanin A
            7-O-(6-O-malonyl-beta-D-glucoside) [RN:R06796]
ALL_REAC    R06796;
            (other) R04618 R06821 R07719 R07721 R07731 R07741 R07754 R07757
SUBSTRATE   malonyl-CoA [CPD:C00083];
            biochanin A 7-O-beta-D-glucoside [CPD:C05376]
PRODUCT     CoA [CPD:C00010];
            biochanin A 7-O-(6-O-malonyl-beta-D-glucoside) [CPD:C12625]
COMMENT     The 6-position of the glucose residue of formononetin can also act
            as acceptor; some other 7-O-glucosides of isoflavones, flavones and
            flavonols can also act, but more slowly.
REFERENCE   1  [PMID:6497385]
  AUTHORS   Koester J, Bussmann R, Barz W.
  TITLE     Malonyl-coenzyme A:isoflavone
            7-O-glucoside-6&quot;-O-malonyltransferase from roots of chick pea
            (Cicer arietinum L.).
  JOURNAL   Arch. Biochem. Biophys. 234 (1984) 513-21.
  ORGANISM  Cicer arietinum
REFERENCE   2  [PMID:6639051]
  AUTHORS   Matern U, Feser C, Hammer D.
  TITLE     Further characterization and regulation of malonyl-coenzyme A:
            flavonoid glucoside malonyltransferases from parsley cell suspension
            cultures.
  JOURNAL   Arch. Biochem. Biophys. 226 (1983) 206-17.
  ORGANISM  parsley
PATHWAY     PATH: map00941  Flavonoid biosynthesis
            PATH: map00943  Isoflavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.115
            ExPASy - ENZYME nomenclature database: 2.3.1.115
            ExplorEnz - The Enzyme Database: 2.3.1.115
            ERGO genome analysis and discovery system: 2.3.1.115
            BRENDA, the Enzyme Database: 2.3.1.115
            CAS: 93585-97-8
///
ENTRY       EC 2.3.1.116                Enzyme
NAME        flavonol-3-O-beta-glucoside O-malonyltransferase;
            flavonol 3-O-glucoside malonyltransferase;
            MAT-3;
            malonyl-coenzyme A:flavonol-3-O-glucoside malonyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     malonyl-CoA:flavonol-3-O-beta-D-glucoside 6"-O-malonyltransferase
REACTION    malonyl-CoA + flavonol 3-O-beta-D-glucoside = CoA + flavonol
            3-O-(6-O-malonyl-beta-D-glucoside) [RN:R04356]
ALL_REAC    R04356 > R06797
SUBSTRATE   malonyl-CoA [CPD:C00083];
            flavonol 3-O-beta-D-glucoside [CPD:C03946]
PRODUCT     CoA [CPD:C00010];
            flavonol 3-O-(6-O-malonyl-beta-D-glucoside) [CPD:C04385]
REFERENCE   1  [PMID:6639051]
  AUTHORS   Matern U, Feser C, Hammer D.
  TITLE     Further characterization and regulation of malonyl-coenzyme A:
            flavonoid glucoside malonyltransferases from parsley cell suspension
            cultures.
  JOURNAL   Arch. Biochem. Biophys. 226 (1983) 206-17.
  ORGANISM  parsley
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.116
            ExPASy - ENZYME nomenclature database: 2.3.1.116
            ExplorEnz - The Enzyme Database: 2.3.1.116
            ERGO genome analysis and discovery system: 2.3.1.116
            BRENDA, the Enzyme Database: 2.3.1.116
            CAS: 78413-11-3
///
ENTRY       EC 2.3.1.117                Enzyme
NAME        2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase;
            tetrahydropicolinate succinylase;
            tetrahydrodipicolinate N-succinyltransferase;
            tetrahydrodipicolinate succinyltransferase;
            succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase;
            succinyl-CoA:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate
            N-succinyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     succinyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate
            N-succinyltransferase
REACTION    succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate +
            H2O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate [RN:R04365]
ALL_REAC    R04365
SUBSTRATE   succinyl-CoA [CPD:C00091];
            (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate [CPD:C03972];
            H2O [CPD:C00001]
PRODUCT     CoA [CPD:C00010];
            N-succinyl-L-2-amino-6-oxoheptanedioate [CPD:C04462]
COMMENT     Involved in the biosynthesis of lysine in bacteria (including
            cyanobacteria) and higher plants. The 1992 edition of the Enzyme
            List erroneously gave the name
            2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase to
            this enzyme.
REFERENCE   1  [PMID:6365916]
  AUTHORS   Simms SA, Voige WH, Gilvarg C.
  TITLE     Purification and characterization of succinyl-CoA:
            tetrahydrodipicolinate N-succinyltransferase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 259 (1984) 2734-41.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K00674  2,3,4,5-tetrahydropyridine-2-carboxylate
                        N-succinyltransferase
GENES       ECO: b0166(dapD)
            ECJ: JW0161(dapD)
            ECE: Z0176(dapD)
            ECS: ECs0168
            ECC: c0201(dapD)
            ECI: UTI89_C0180(dapD)
            ECP: ECP_0174
            ECV: APECO1_1821(dapD)
            ECW: EcE24377A_0169(dapD)
            ECX: EcHS_A0168
            STY: STY0236(dapD)
            STT: t0214(dapD)
            SPT: SPA0219(dapD)
            SEC: SC0213(dapD)
            STM: STM0213(dapD)
            YPE: YPO1041(dapD)
            YPK: y3140(dapD)
            YPM: YP_2810(dapD)
            YPA: YPA_0515
            YPN: YPN_2960
            YPP: YPDSF_1672
            YPS: YPTB3006(dapD)
            YPI: YpsIP31758_1010(dapD)
            SFL: SF0156(dapD)
            SFX: S0159(dapD)
            SFV: SFV_0149(dapD)
            SSN: SSON_0178(dapD)
            SBO: SBO_0154(dapD)
            SDY: SDY_0182(dapD)
            ECA: ECA1028(dapD)
            PLU: plu0669(dapD)
            BUC: BU229(dapD)
            BAS: BUsg223(dapD)
            BAB: bbp211(dapD)
            BCC: BCc_140(dapD)
            WBR: WGLp394(dapD)
            SGL: SG1946
            ENT: Ent638_0704
            SPE: Spro_3793
            BFL: Bfl269(dapD)
            BPN: BPEN_277(dapD)
            HIT: NTHI1406(dapD)
            HIP: CGSHiEE_05845(dapD)
            HDU: HD0630(dapD)
            HSO: HS_0785(dapD)
            PMU: PM0658(dapD)
            MSU: MS1177(dapD)
            APL: APL_1861(dapD)
            ASU: Asuc_1388
            XFA: XF0114
            XFT: PD0086(dapD)
            XCC: XCC1384(dapD)
            XCB: XC_2854
            XCV: XCV1487(dapD)
            XAC: XAC1430(dapD)
            XOO: XOO1985(dapD)
            XOM: XOO_1876(XOO1876)
            VCH: VC2329
            VCO: VC0395_A1909(dapD)
            VVU: VV1_1790
            VVY: VV2622
            VPA: VP2380
            VFI: VF0576
            PPR: PBPRA3004
            PAE: PA3666(dapD)
            PAU: PA14_16950(dapD)
            PPU: PP_1530
            PST: PSPTO_1528
            PSB: Psyr_1336
            PSP: PSPPH_3846
            PFL: PFL_1170
            PFO: Pfl_1093
            PEN: PSEEN4227
            PAR: Psyc_0737(dapD)
            PCR: Pcryo_0725
            PRW: PsycPRwf_0897
            ACI: ACIAD2599(dapD)
            SON: SO_1625(dapD)
            SDN: Sden_1551
            SFR: Sfri_1267
            SAZ: Sama_1136
            SBL: Sbal_1447
            SBM: Shew185_1442
            SLO: Shew_2638
            SPC: Sputcn32_1345
            SSE: Ssed_3164
            SPL: Spea_2888
            SHE: Shewmr4_2644
            SHM: Shewmr7_2711
            SHN: Shewana3_2818
            SHW: Sputw3181_2758
            ILO: IL0848(dapD)
            CPS: CPS_1548(dapD) CPS_4493
            PHA: PSHAa0179(dapD) PSHAa2039(dapD)
            PAT: Patl_3394
            SDE: Sde_2606
            CBU: CBU_0667(dapD)
            CBD: COXBU7E912_0677(dapD)
            LPN: lpg0888(dapD)
            LPF: lpl0919(dapD)
            LPP: lpp0949(dapD)
            MCA: MCA1490(dapD)
            FTN: FTN_1727(dapD)
            TCX: Tcr_1289
            NOC: Noc_2125
            AEH: Mlg_1867
            HHA: Hhal_1470
            HCH: HCH_05259
            CSA: Csal_0558
            ABO: ABO_1138(dapD)
            AHA: AHA_1170(dapD)
            DNO: DNO_0817(dapD)
            CRP: CRP_018
            RMA: Rmag_0074
            VOK: COSY_0080(dapD)
            NME: NMB0335
            NMA: NMA2153(dapD)
            NMC: NMC1835(dapD)
            NGO: NGO1667
            CVI: CV_0450(dapD)
            RSO: RSc1393(dapD)
            REU: Reut_A1892
            REH: H16_A2066(dapD)
            RME: Rmet_1423
            BMA: BMA1566(dapD)
            BMV: BMASAVP1_A2069(dapD)
            BML: BMA10299_A3243(dapD)
            BMN: BMA10247_1341(dapD)
            BXE: Bxe_A1670 Bxe_C0823
            BVI: Bcep1808_1936
            BUR: Bcep18194_A5339
            BCN: Bcen_6047
            BCH: Bcen2424_2030
            BAM: Bamb_2062
            BPS: BPSL2169(dapD)
            BPM: BURPS1710b_2594(dapD)
            BPL: BURPS1106A_2505(dapD)
            BPD: BURPS668_2449(dapD)
            BTE: BTH_I2016(dapD)
            PNU: Pnuc_1458
            BPE: BP1764(dapD)
            BPA: BPP1995(dapD)
            BBR: BB2183(dapD)
            RFR: Rfer_2046
            POL: Bpro_1996
            PNA: Pnap_1812
            AAV: Aave_2484
            AJS: Ajs_2067
            VEI: Veis_0275
            MPT: Mpe_A1806
            HAR: HEAR1324(dapD)
            MMS: mma_2069
            NEU: NE2462(dapD)
            NET: Neut_0229
            NMU: Nmul_A1851
            EBA: ebA6386(dapD)
            AZO: azo2005(dapD)
            DAR: Daro_1726
            TBD: Tbd_1220
            MFA: Mfla_1866
            HPY: HP0626(dapD)
            HPA: HPAG1_0609
            HHE: HH0719(dapD)
            HAC: Hac_0734(dapD)
            WSU: WS0161(cysE) WS0786(dapD)
            TDN: Tmden_1093
            CJE: Cj1605c(dapD)
            CJR: CJE1777
            CJU: C8J_1506(dapD)
            ABU: Abu_1392(dapD)
            NIS: NIS_1643
            SUN: SUN_1588
            BBA: Bd1775(dapD)
            ADE: Adeh_3829
            AFW: Anae109_3943
            MXA: MXAN_6779
            RPR: RP194
            RTY: RT0183(dapD)
            RCO: RC0243(dapD)
            RFE: RF_1073(dapD)
            RBE: RBE_1143(dapD)
            RAK: A1C_01385(dapD)
            RCM: A1E_00850 A1E_00870(dapD)
            RRI: A1G_01390(dapD)
            OTS: OTBS_0115(dapD)
            WOL: WD0714(dapD)
            WBM: Wbm0449
            AMA: AM1331(dapD)
            ERU: Erum0390(dapD)
            ERW: ERWE_CDS_00280(dapD)
            ERG: ERGA_CDS_00270(dapD)
            ECN: Ecaj_0031
            ECH: ECH_0058(dapD)
            PUB: SAR11_0463(dapD)
            MLO: mlr4843
            MES: Meso_0387
            PLA: Plav_0267
            SME: SMc01732(dapD)
            SMD: Smed_0069
            ATU: Atu0371(dapD)
            ATC: AGR_C_648
            RET: RHE_CH00418(dapD)
            RLE: RL0437(dapD)
            BME: BMEII0270
            BMF: BAB2_0991(dapD)
            BMS: BRA1028(dapD)
            BMB: BruAb2_0968(dapD)
            BOV: BOV_A0969(dapD)
            OAN: Oant_1354
            BJA: blr8104(dapD)
            BRA: BRADO0775(dapD)
            BBT: BBta_7332(dapD)
            RPA: RPA0626(dapD)
            RPB: RPB_0677
            RPC: RPC_0811
            RPD: RPD_0075
            RPE: RPE_0651
            NWI: Nwi_3069
            NHA: Nham_3698
            BHE: BH00720(dapD)
            BQU: BQ00650(dapD)
            BBK: BARBAKC583_1323(dapD)
            XAU: Xaut_2647
            CCR: CC_0281
            SIL: SPO3337(dapD)
            SIT: TM1040_3009
            RSP: RSP_1131(dapD)
            RSH: Rsph17029_2792
            RSQ: Rsph17025_0046
            JAN: Jann_0349
            RDE: RD1_0189(dapD)
            PDE: Pden_2514
            MMR: Mmar10_0454
            HNE: HNE_0421(dapD)
            ZMO: ZMO0431(dapD)
            NAR: Saro_1835
            SAL: Sala_2828
            SWI: Swit_2911
            ELI: ELI_09640
            GOX: GOX1831
            GBE: GbCGDNIH1_0686
            ACR: Acry_1530
            RRU: Rru_A3479
            MAG: amb3873
            MGM: Mmc1_0045 Mmc1_0521
            ABA: Acid345_2087
            SUS: Acid_6979
            BCL: ABC2433(dapD)
            BPU: BPUM_1315
            SAC: SACOL1432(dapD)
            SAA: SAUSA300_1290(dapD)
            SAO: SAOUHSC_01398
            LLA: L79267(ychH)
            LLC: LACR_0293
            LLM: llmg_0291(dapD)
            SPN: SP_2097
            SPR: spr1907(dapD)
            SPD: SPD_1923
            SMU: SMU.317
            STC: str1839(dapD)
            STL: stu1839(dapD)
            SSA: SSA_2174(dapD)
            SGO: SGO_0158
            LPL: lp_2264(dapD)
            LAC: LBA0852(dapD)
            LCA: LSEI_0097
            EFA: EF1133(dapD)
            OOE: OEOE_0772
            CAC: CAC2381(dapD)
            CPE: CPE1909(dapD)
            CPF: CPF_2165
            CPR: CPR_1876
            CNO: NT01CX_1738
            CDF: CD3227(dapD)
            CKL: CKL_3211(dapD)
            TTE: TTE0830(dapD)
            MTU: Rv1201c
            MTC: MT1239
            MBO: Mb1233c
            MLE: ML1058
            MPA: MAP2578
            MSM: MSMEG_5104
            MMC: Mmcs_4013
            CGL: NCgl1061(cgl1106) NCgl1063(cgl1108)
            CGB: cg1256(dapD) cg1259(dapD2)
            CEF: CE1163(dapD) CE1165
            CDI: DIP0979 DIP0981
            CJK: jk1392(dapD)
            NFA: nfa47420
            RHA: RHA1_ro05962(dapD)
            SCO: SCO1916(SCI7.34c)
            SMA: SAV6339(dapD)
            LXX: Lxx09040(dapD)
            CMI: CMM_1177(dapD)
            PAC: PPA0630
            TFU: Tfu_0494
            FRA: Francci3_3856
            FAL: FRAAL6124(dapD)
            ACE: Acel_1844
            SEN: SACE_1013(dapD)
            BLO: BL1734
            BAD: BAD_0461
            RXY: Rxyl_0073
            SRU: SRU_0969(dapD)
            CHU: CHU_2022(dapD)
            GFO: GFO_2275(dapD)
            FJO: Fjoh_2524
            FPS: FP1628(dapD)
            CTE: CT2259(dapD)
            CCH: Cag_1990
            CPH: Cpha266_0041
            PVI: Cvib_0017
            PLT: Plut_0013
            TMA: TM1519
            MKA: MK0435(dapD)
            HMA: rrnAC0204(dapD)
            HWA: HQ1509A(dapD)
            NPH: NP1494A(dapD)
STRUCTURES  PDB: 1KGQ  1KGT  2TDT  3TDT  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.117
            ExPASy - ENZYME nomenclature database: 2.3.1.117
            ExplorEnz - The Enzyme Database: 2.3.1.117
            ERGO genome analysis and discovery system: 2.3.1.117
            BRENDA, the Enzyme Database: 2.3.1.117
            CAS: 88086-34-4
///
ENTRY       EC 2.3.1.118                Enzyme
NAME        N-hydroxyarylamine O-acetyltransferase;
            arylhydroxamate N,O-acetyltransferase;
            arylamine N-acetyltransferase;
            N-hydroxy-2-aminofluorene-O-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:N-hydroxyarylamine O-acetyltransferase
REACTION    acetyl-CoA + an N-hydroxyarylamine = CoA + an N-acetoxyarylamine
            [RN:R04024]
ALL_REAC    R04024
SUBSTRATE   acetyl-CoA [CPD:C00024];
            N-hydroxyarylamine [CPD:C02720]
PRODUCT     CoA [CPD:C00010];
            N-acetoxyarylamine [CPD:C02709]
COMMENT     The enzyme from liver, but not that from bacteria, can also catalyse
            N-acetylation of arylamines and N,O-acetylation of arylhydroxamates.
REFERENCE   1  [PMID:3745141]
  AUTHORS   Saito K, Shinohara A, Kamataki T, Kato R.
  TITLE     N-hydroxyarylamine O-acetyltransferase in hamster liver: identity
            with arylhydroxamic acid N,O-acetyltransferase and arylamine
            N-acetyltransferase.
  JOURNAL   J. Biochem. (Tokyo). 99 (1986) 1689-97.
  ORGANISM  hamster
ORTHOLOGY   KO: K00675  N-hydroxyarylamine O-acetyltransferase
GENES       ECO: b1463(nhoA)
            ECJ: JW1458(nhoA)
            ECE: Z2250
            ECS: ECs2066
            ECC: c1895(nhoA)
            ECI: UTI89_C1681(nhoA)
            ECP: ECP_1465
            ECV: APECO1_600(nhoA)
            ECW: EcE24377A_1644
            ECX: EcHS_A1547
            STY: STY1483
            STT: t1492
            SPT: SPA1286(nhoA)
            STM: STM1582(nhoA)
            SSN: SSON_1662
            ENT: Ent638_2068
            VPA: VPA0072
            PMY: Pmen_3693
            CPS: CPS_2729
            LPN: lpg2451
            LPF: lpl2369
            LPP: lpp2516
            HCH: HCH_05574
            BMA: BMAA1313(nhoA)
            BMV: BMASAVP1_0295(nhoA)
            BML: BMA10299_0570(nhoA)
            BMN: BMA10247_A0998(nhoA)
            BUR: Bcep18194_B1133
            BAM: Bamb_4081
            BPS: BPSS0916
            BPM: BURPS1710b_A2514(nhoA)
            BTE: BTH_II1481
            NET: Neut_0684
            AZO: azo0342(nhoA)
            MLO: mll5814
            RET: RHE_PE00167(ype00075)
            BRA: BRADO6241
            BBT: BBta_1364
            CCR: CC_1563
            BAN: BA2717
            BAR: GBAA2717
            BAA: BA_3239 BA_4042
            BAT: BAS2531 BAS3292
            BCE: BC2140 BC2725 BC3483
            BCA: BCE_2744 BCE_3501
            BCZ: BCZK2456(nhoA) BCZK3206(nhoA)
            BTK: BT9727_2491(nhoA) BT9727_3262(yvcN)
            BPU: BPUM_3111
            LLM: llmg_0500(nhoA)
            DSY: DSY3777
STRUCTURES  PDB: 1E2T  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.118
            ExPASy - ENZYME nomenclature database: 2.3.1.118
            ExplorEnz - The Enzyme Database: 2.3.1.118
            ERGO genome analysis and discovery system: 2.3.1.118
            BRENDA, the Enzyme Database: 2.3.1.118
            CAS: 100984-92-7
///
ENTRY       EC 2.3.1.119                Enzyme
NAME        icosanoyl-CoA synthase;
            acyl-CoA elongase;
            C18-CoA elongase;
            stearoyl-CoA elongase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     stearoyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating,
            oxoacyl- and enoyl-reducing)
REACTION    stearoyl-CoA + malonyl-CoA + 2 NAD(P)H + 2 H+ = icosanoyl-CoA + CO2
            + CoA + 2 NAD(P)+ + H2O [RN:R02223 R02224]
ALL_REAC    R02223 R02224
SUBSTRATE   stearoyl-CoA [CPD:C00412];
            malonyl-CoA [CPD:C00083];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
PRODUCT     icosanoyl-CoA [CPD:C02041];
            CO2 [CPD:C00011];
            CoA [CPD:C00010];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     Icosanoyl-CoA can act in place of stearoyl-CoA. The membrane enzyme
            brings about the elongation of these long-chain fatty-acyl-CoAs.
REFERENCE   1  [PMID:2913944]
  AUTHORS   Bessoule JJ, Lessire R, Cassagne C.
  TITLE     Partial purification of the acyl-CoA elongase of Allium porrum
            leaves.
  JOURNAL   Arch. Biochem. Biophys. 268 (1989) 475-84.
  ORGANISM  Allium porrum
REFERENCE   2  [PMID:3552725]
  AUTHORS   Bessoule JJ, Lessire R, Rigoulet M, Guerin B, Cassagne C.
  TITLE     Fatty acid synthesis in mitochondria from Saccharomyces cerevisiae.
  JOURNAL   FEBS. Lett. 214 (1987) 158-62.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Lessire, R., Bessoule, J.-J. and Cassagne, C.
  TITLE     Solubilization of C18 CoA and C20 CoA elongases from Allium porrum
            L. epidermal-cell microsomes.
  JOURNAL   FEBS Lett. 187 (1985) 314-320.
  ORGANISM  Allium porrum
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.119
            ExPASy - ENZYME nomenclature database: 2.3.1.119
            ExplorEnz - The Enzyme Database: 2.3.1.119
            ERGO genome analysis and discovery system: 2.3.1.119
            BRENDA, the Enzyme Database: 2.3.1.119
            CAS: 141256-55-5
///
ENTRY       EC 2.3.1.120      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
COMMENT     Deleted entry: 6'-deoxychalcone synthase. The reaction listed is due
            to EC 2.3.1.74 naringenin-chalcone synthase (EC 2.3.1.120 created
            1990, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.120
            ExPASy - ENZYME nomenclature database: 2.3.1.120
            ExplorEnz - The Enzyme Database: 2.3.1.120
            ERGO genome analysis and discovery system: 2.3.1.120
            BRENDA, the Enzyme Database: 2.3.1.120
///
ENTRY       EC 2.3.1.121                Enzyme
NAME        1-alkenylglycerophosphoethanolamine O-acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:1-alkenylglycerophosphoethanolamine O-acyltransferase
REACTION    acyl-CoA + 1-alkenylglycerophosphoethanolamine = CoA +
            1-alkenyl-2-acylglycerophosphoethanolamine [RN:R04413]
ALL_REAC    R04413
SUBSTRATE   acyl-CoA [CPD:C00040];
            1-alkenylglycerophosphoethanolamine [CPD:C04635]
PRODUCT     CoA [CPD:C00010];
            1-alkenyl-2-acylglycerophosphoethanolamine
COMMENT     Long-chain unsaturated acyl-CoAs are the best substrates. Not
            identical with EC 2.3.1.104 1-alkenylglycerophosphocholine
            O-acyltransferase.
REFERENCE   1  [PMID:3651487]
  AUTHORS   Arthur G, Page L, Choy PC.
  TITLE     Acylation of 1-alkenylglycerophosphoethanolamine and
            1-acylglycerophosphoethanolamine in guinea-pig heart microsomes.
  JOURNAL   Biochim. Biophys. Acta. 921 (1987) 259-65.
  ORGANISM  guinea pig
PATHWAY     PATH: map00565  Ether lipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.121
            ExPASy - ENZYME nomenclature database: 2.3.1.121
            ExplorEnz - The Enzyme Database: 2.3.1.121
            ERGO genome analysis and discovery system: 2.3.1.121
            BRENDA, the Enzyme Database: 2.3.1.121
            CAS: 112445-17-7
///
ENTRY       EC 2.3.1.122                Enzyme
NAME        trehalose O-mycolyltransferase;
            alpha,alpha'-trehalose 6-monomycolate:alpha,alpha'-trehalose
            mycolyltransferase;
            alpha,alpha'-trehalose-6-mycolate:alpha,alpha'-trehalose-6-mycolate
            6'-mycolyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     alpha,alpha-trehalose-6-mycolate:alpha,alpha-trehalose-6-mycolate
            6'-mycolyltransferase
REACTION    2 alpha,alpha-trehalose 6-mycolate = alpha,alpha-trehalose +
            alpha,alpha-trehalose 6,6'-bismycolate [RN:R07248]
ALL_REAC    R07248
SUBSTRATE   alpha,alpha'-trehalose 6-mycolate [CPD:C04218]
PRODUCT     alpha,alpha-trehalose [CPD:C01083];
            alpha,alpha'-trehalose 6,6'-bismycolate [CPD:C04465]
COMMENT     Catalyses the exchange of mycolic acid between trehalose, trehalose
            mycolate and trehalose bismycolate. Trehalose 6-palmitate can also
            act as donor.
REFERENCE   1  [PMID:3654621]
  AUTHORS   Sathyamoorthy N, Takayama K.
  TITLE     Purification and characterization of a novel mycolic acid exchange
            enzyme from Mycobacterium smegmatis.
  JOURNAL   J. Biol. Chem. 262 (1987) 13417-23.
  ORGANISM  Mycobacterium smegmatis [GN:msm]
GENES       CGB: cg0413(cmt1) cg1052(cmt3) cg1170(cmt5) cg2394(cmt4)
                 cg3182(cop1) cg3186(cmt2)
            CJK: jk0133(cmtB) jk0134(cmtC) jk1937(cmtA)
            SEN: SACE_2339(cmtC)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.122
            ExPASy - ENZYME nomenclature database: 2.3.1.122
            ExplorEnz - The Enzyme Database: 2.3.1.122
            ERGO genome analysis and discovery system: 2.3.1.122
            BRENDA, the Enzyme Database: 2.3.1.122
            CAS: 111694-11-2
///
ENTRY       EC 2.3.1.123                Enzyme
NAME        dolichol O-acyltransferase;
            acyl-CoA:dolichol acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     palmitoyl-CoA:dolichol O-palmitoyltransferase
REACTION    palmitoyl-CoA + dolichol = CoA + dolichyl palmitate [RN:R02138]
ALL_REAC    R02138
SUBSTRATE   palmitoyl-CoA [CPD:C00154];
            dolichol [CPD:C00381]
PRODUCT     CoA [CPD:C00010];
            dolichyl palmitate [CPD:C02536]
COMMENT     Other acyl-CoAs can also act, but more slowly. alpha-Saturated
            dolichols are acylated more rapidly than the alpha-unsaturated
            analogues.
REFERENCE   1  [PMID:3121628]
  AUTHORS   Tollbom O, Valtersson C, Chojnacki T, Dallner G.
  TITLE     Esterification of dolichol in rat liver.
  JOURNAL   J. Biol. Chem. 263 (1988) 1347-52.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.123
            ExPASy - ENZYME nomenclature database: 2.3.1.123
            ExplorEnz - The Enzyme Database: 2.3.1.123
            ERGO genome analysis and discovery system: 2.3.1.123
            BRENDA, the Enzyme Database: 2.3.1.123
            CAS: 111839-04-4
///
ENTRY       EC 2.3.1.124      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
COMMENT     Deleted entry: already listed as EC 2.3.1.20 diacylglycerol
            O-acyltransferase (EC 2.3.1.124 created 1990, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.124
            ExPASy - ENZYME nomenclature database: 2.3.1.124
            ExplorEnz - The Enzyme Database: 2.3.1.124
            ERGO genome analysis and discovery system: 2.3.1.124
            BRENDA, the Enzyme Database: 2.3.1.124
///
ENTRY       EC 2.3.1.125                Enzyme
NAME        1-alkyl-2-acetylglycerol O-acyltransferase;
            1-hexadecyl-2-acetylglycerol acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:1-O-alkyl-2-acetyl-sn-glycerol O-acyltransferase
REACTION    acyl-CoA + 1-O-alkyl-2-acetyl-sn-glycerol = CoA +
            1-O-alkyl-2-acetyl-3-acyl-sn-glycerol [RN:R04363]
ALL_REAC    R04363
SUBSTRATE   acyl-CoA [CPD:C00040];
            1-O-alkyl-2-acetyl-sn-glycerol [CPD:C03820]
PRODUCT     CoA [CPD:C00010];
            1-O-alkyl-2-acetyl-3-acyl-sn-glycerol [CPD:C04361]
COMMENT     A number of acyl-CoAs can act as acyl donor; maximum activity is
            obtained with linoleoyl-CoA. Not identical with EC 2.3.1.20
            diacylglycerol O-acyltransferase.
REFERENCE   1  [PMID:3422635]
  AUTHORS   Kawasaki T, Snyder F.
  TITLE     Synthesis of a novel acetylated neutral lipid related to
            platelet-activating factor by
            acyl-CoA:1-O-alkyl-2-acetyl-sn-glycerol acyltransferase in HL-60
            cells.
  JOURNAL   J. Biol. Chem. 263 (1988) 2593-6.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00565  Ether lipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.125
            ExPASy - ENZYME nomenclature database: 2.3.1.125
            ExplorEnz - The Enzyme Database: 2.3.1.125
            ERGO genome analysis and discovery system: 2.3.1.125
            BRENDA, the Enzyme Database: 2.3.1.125
            CAS: 114704-90-4
///
ENTRY       EC 2.3.1.126                Enzyme
NAME        isocitrate O-dihydroxycinnamoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     caffeoyl-CoA:isocitrate 3-O-(3,4-dihydroxycinnamoyl)transferase
REACTION    caffeoyl-CoA + isocitrate = CoA + 2-caffeoylisocitrate [RN:R01946]
ALL_REAC    R01946
SUBSTRATE   caffeoyl-CoA [CPD:C00323];
            isocitrate [CPD:C00311]
PRODUCT     CoA [CPD:C00010];
            2-caffeoylisocitrate [CPD:C02927]
COMMENT     Feruloyl-CoA and 4-coumaroyl-CoA can also act as donors.
REFERENCE   1
  AUTHORS   Strack, D., Leicht, P., Bokern, M., Wray, V. and Grotjahn, L.
  TITLE     Hydroxycinnamic acid-esters of isocitric acid - accumulation and
            enzymatic-synthesis in Amaranthus cruentus.
  JOURNAL   Phytochemistry 26 (1987) 2919-2922.
  ORGANISM  Amaranthus cruentus
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.126
            ExPASy - ENZYME nomenclature database: 2.3.1.126
            ExplorEnz - The Enzyme Database: 2.3.1.126
            ERGO genome analysis and discovery system: 2.3.1.126
            BRENDA, the Enzyme Database: 2.3.1.126
            CAS: 112352-88-2
///
ENTRY       EC 2.3.1.127                Enzyme
NAME        ornithine N-benzoyltransferase;
            ornithine N-acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     benzoyl-CoA:L-ornithine N-benzoyltransferase
REACTION    2 benzoyl-CoA + L-ornithine = 2 CoA + N2,N5-dibenzoyl-L-ornithine
            [RN:R00664]
ALL_REAC    R00664
SUBSTRATE   benzoyl-CoA [CPD:C00512];
            L-ornithine [CPD:C00077]
PRODUCT     CoA [CPD:C00010];
            N2,N5-dibenzoyl-L-ornithine [CPD:C03712]
REFERENCE   1
  AUTHORS   Seymour, M.A., Millburn, P. and Tait, G.H.
  TITLE     Renal biosynthesis of ornithuric acid in quail.
  JOURNAL   Biochem. Soc. Trans. 15 (1987) 1108-1109.
  ORGANISM  quail
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.127
            ExPASy - ENZYME nomenclature database: 2.3.1.127
            ExplorEnz - The Enzyme Database: 2.3.1.127
            ERGO genome analysis and discovery system: 2.3.1.127
            BRENDA, the Enzyme Database: 2.3.1.127
            CAS: 111693-97-1
///
ENTRY       EC 2.3.1.128                Enzyme
NAME        ribosomal-protein-alanine N-acetyltransferase;
            ribosomal protein S18 acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:ribosomal-protein-L-alanine N-acetyltransferase
REACTION    acetyl-CoA + ribosomal-protein L-alanine = CoA + ribosomal-protein
            N-acetyl-L-alanine [RN:R04316]
ALL_REAC    R04316
SUBSTRATE   acetyl-CoA [CPD:C00024];
            ribosomal-protein L-alanine [CPD:C03803]
PRODUCT     CoA [CPD:C00010];
            ribosomal-protein N-acetyl-L-alanine [CPD:C04341]
COMMENT     A group of enzymes in Escherichia coli that acetylate the N-terminal
            alanine residues of specific ribosomal proteins. cf. EC 2.3.1.88,
            peptide alpha-N-acetyltransferase.
REFERENCE   1  [PMID:2828880]
  AUTHORS   Yoshikawa A, Isono S, Sheback A, Isono K.
  TITLE     Cloning and nucleotide sequencing of the genes rimI and rimJ which
            encode enzymes acetylating ribosomal proteins S18 and S5 of
            Escherichia coli K12.
  JOURNAL   Mol. Gen. Genet. 209 (1987) 481-8.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K00676  ribosomal-protein-alanine N-acetyltransferase
            KO: K03789  ribosomal-protein-alanine N-acetyltransferase
            KO: K03790  ribosomal-protein-alanine N-acetyltransferase
GENES       AFM: AFUA_3G09940
            UMA: UM01623.1
            EHI: 12.t00070 294.t00008
            ECO: b1066(rimJ) b4373(rimI)
            ECJ: JW1053(rimJ) JW4335(rimI)
            ECE: Z1703(rimJ) Z5974(rimI)
            ECS: ECs1444 ECs5331
            ECC: c1333(rimJ) c5453(rimI)
            ECI: UTI89_C1191(rimJ) UTI89_C5082(rimI)
            ECP: ECP_1058 ECP_4756
            ECV: APECO1_148(rimJ) APECO1_2053
            ECW: EcE24377A_1189(rimJ) EcE24377A_4968(rimI)
            ECX: EcHS_A1189(rimJ) EcHS_A4607(rimI)
            STY: STY1205(rimJ) STY4908(rimI)
            STT: t1753(rimJ) t4601(rimI)
            SPT: SPA1684(rimJ) SPA4372(rimI)
            SEC: SC1115(rimJ)
            STM: STM1167(rimJ) STM4558(rimI)
            YPE: YPO0429(rimI) YPO2041(rimJ)
            YPK: y2271(rimJ) y3751(rimI)
            YPM: YP_1884(rimJ) YP_3752(rimI3)
            YPA: YPA_1423 YPA_3855
            YPN: YPN_0300 YPN_1518
            YPP: YPDSF_3204
            YPS: YPTB0574(rimI) YPTB1890(yjcK) YPTB2023(rimJ)
            YPI: YpsIP31758_2049(rimJ) YpsIP31758_3505(rimI)
            SFL: SF1072(rimJ) SF4404(rimI)
            SFX: S1150(rimJ) S4676(rimI)
            SFV: SFV_1088(rimJ) SFV_4407(rimI)
            SSN: SSON_1086(rimJ) SSON_4523(rimI)
            SBO: SBO_1998(rimJ) SBO_4434(rimI)
            SDY: SDY_2086(rimJ) SDY_4632(rimI)
            ECA: ECA0733(rimI) ECA2524(rimJ) ECA3191
            PLU: plu2090(rimJ) plu4250(rimI)
            SGL: SG0391 SG1246
            ENT: Ent638_0532
            SPE: Spro_0651
            HIN: HI0010(rimI)
            HIT: NTHI0013(rimI)
            HIP: CGSHiEE_03265(rimI)
            HIQ: CGSHiGG_02510(rimI)
            HDU: HD0212(rimI)
            HSO: HS_0491(rimI)
            PMU: PM0960(rimI)
            MSU: MS1590(rimI)
            APL: APL_2007(rimI)
            ASU: Asuc_1442
            XFA: XF0441
            XFT: PD1639(rimI)
            XCC: XCC0643(rimI) XCC2918(rimJ)
            XCB: XC_1191 XC_3592
            XCV: XCV3226(rimJ) XCV3688
            XAC: XAC3095(rimJ) XAC3563(rimI)
            XOO: XOO0812(rimI) XOO1754(rimJ)
            XOM: XOO_0741(XOO0741) XOO_1654(XOO1654)
            VCH: VC0657 VC1309
            VCO: VC0395_A0189(rimI) VC0395_A0927(rimJ)
            VVU: VV1_1718 VV1_2271
            VVY: VV2074 VV2686
            VPA: VP1868 VP2441
            VFI: VF0499 VF1382 VF1389 VFA0750
            PPR: PBPRA0624(rimI) PBPRA2432
            PAE: PA1928(rimJ) PA4678(rimI)
            PAU: PA14_39580(rimJ) PA14_61880(rimI)
            PAP: PSPA7_5385(rimI)
            PPU: PP_0697
            PST: PSPTO_0992(rimI)
            PSB: Psyr_0857
            PSP: PSPPH_0888(rimI) PSPPH_3302(rimJ)
            PFL: PFL_2384 PFL_5211 PFL_5237(rimI)
            PFO: Pfl_0732 Pfl_4775
            PEN: PSEEN0835 PSEEN0985
            PAR: Psyc_0385(rimI)
            PCR: Pcryo_0426
            ACI: ACIAD0887(rimI)
            SON: SO_1160(rimI)
            SDN: Sden_2855
            SFR: Sfri_0691
            SHE: Shewmr4_0983
            SHM: Shewmr7_1048
            SHN: Shewana3_0987 Shewana3_1501
            ILO: IL0459(aceF) IL1884(rimI)
            CPS: CPS_1114(rimI)
            PHA: PSHAa0202 PSHAa0653(rimI) PSHAa1577
            PAT: Patl_1349
            SDE: Sde_2521
            CBU: CBU_0505 CBU_0801(rimI)
            CBD: COXBU7E912_0868(rimI)
            LPN: lpg1501
            LPF: lpl1525
            LPP: lpp1458
            MCA: MCA2277(rimI)
            FTU: FTT1054c(rimI)
            FTF: FTF1054c(rimI)
            FTL: FTL_1032
            FTH: FTH_1008
            FTN: FTN_0943(rimI)
            TCX: Tcr_0613
            NOC: Noc_2514
            AEH: Mlg_0553
            HCH: HCH_02991 HCH_05906(rimI)
            CSA: Csal_2992
            ABO: ABO_0640
            AHA: AHA_0724(rimI) AHA_0849
            DNO: DNO_0933(rimI)
            NME: NMB1872
            NMA: NMA0584
            NGO: NGO0031
            CVI: CV_0166(rimJ) CV_2317 CV_2338 CV_3453(rimI) CV_4043
            RSO: RSc1368(RS04651)
            REU: Reut_A1938
            RME: Rmet_1396
            BMA: BMA1581(rimI)
            BMV: BMASAVP1_A2083(rimI)
            BML: BMA10299_A3229(rimI)
            BMN: BMA10247_1356(rimI)
            BXE: Bxe_A1655
            BUR: Bcep18194_A5353
            BCN: Bcen_6033
            BCH: Bcen2424_2044 Bcen2424_4559
            BAM: Bamb_2076
            BPS: BPSL2184
            BPM: BURPS1710b_2609(rimI)
            BPL: BURPS1106A_2520(rimI)
            BPD: BURPS668_2464(rimI)
            BTE: BTH_I2002
            RFR: Rfer_0188
            POL: Bpro_4620
            MPT: Mpe_A0302
            HAR: HEAR1763
            MMS: mma_1521(rimI1)
            NEU: NE1399
            NET: Neut_1297
            NMU: Nmul_A2122
            EBA: ebA6491
            AZO: azo1712
            DAR: Daro_1982
            TBD: Tbd_1724
            MFA: Mfla_0413
            CCV: CCV52592_0407(rimI)
            GSU: GSU1757(rimI)
            GME: Gmet_1843
            PCA: Pcar_1294
            DVU: DVU1678(rimI)
            DDE: Dde_1990
            LIP: LI1133(rimJ)
            BBA: Bd1544 Bd2558
            DPS: DP0102
            ADE: Adeh_1293
            MXA: MXAN_0332(rimJ) MXAN_3294(rimI)
            SAT: SYN_02847
            SFU: Sfum_2064
            RPR: RP693(rimJ)
            RTY: RT0688(rimJ)
            RCO: RC1069(rimJ)
            RFE: RF_0218(rimJ)
            RBE: RBE_0498(rimJ)
            MLO: mll7514 mlr5531
            MES: Meso_0758 Meso_3917
            SME: SMc00075(rimJ) SMc01117(rimI)
            ATU: Atu0353 Atu0785(rimJ)
            ATC: AGR_C_1436 AGR_C_619
            RET: RHE_CH00379(rimI) RHE_CH00977(rimJ) RHE_CH01860(ypch00614)
            RLE: RL0398 RL1060 RL2080 RL2397 RL3167
            BME: BMEI1452 BMEI1978
            BMF: BAB1_0508 BAB1_2152
            BMS: BR0482 BR2151
            BMB: BruAb1_0504 BruAb1_2125
            BOV: BOV_2064(rimI)
            BJA: bll0798 blr1183(rimJ)
            BRA: BRADO0038
            BBT: BBta_0043
            RPA: RPA0451(rimI) RPA0841
            RPB: RPB_0587 RPB_4576
            RPC: RPC_0465 RPC_4797
            RPD: RPD_0245 RPD_0824
            RPE: RPE_0209 RPE_4761
            NWI: Nwi_0012 Nwi_0231
            NHA: Nham_0019 Nham_0264
            BHE: BH02270
            BQU: BQ02150
            CCR: CC_0058 CC_3397
            SIL: SPO0380 SPO3069
            SIT: TM1040_2328
            RSP: RSP_1833 RSP_2212(rimI)
            RDE: RD1_1314 RD1_1648 RD1_2143 RD1_3192
            MMR: Mmar10_2226 Mmar10_3030
            HNE: HNE_0526(rimI)
            NAR: Saro_0986
            SAL: Sala_2068
            ELI: ELI_08475
            GOX: GOX0774
            GBE: GbCGDNIH1_0387
            RRU: Rru_A3764
            MAG: amb4457
            MGM: Mmc1_0638
            ABA: Acid345_2362
            BSU: BG12201(ydiD) BG13164(yjcK)
            BHA: BH0547 BH0585
            BAN: BA0260(rimI) BA1588 BA1876 BA2404 BA2420 BA2701 BA2847 BA3010
                 BA3075 BA4369
            BAR: GBAA0260(rimI) GBAA1588 GBAA1876 GBAA2404 GBAA2420 GBAA2701
                 GBAA2847 GBAA3010 GBAA3075 GBAA4369
            BAA: BA_0830 BA_2105 BA_2377 BA_2902 BA_2919 BA_3222 BA_3370
                 BA_3518 BA_3582 BA_4825
            BAT: BAS0246 BAS1472 BAS1738 BAS2240 BAS2255 BAS2516 BAS2656
                 BAS2798 BAS2861 BAS4053
            BCE: BC0288 BC0964 BC1567 BC1799 BC2051 BC2263 BC2338 BC2356
                 BC2709 BC2847 BC2992 BC3051 BC3632 BC4144 BC4195
            BCA: BCE_0281(rimI) BCE_1694 BCE_1955 BCE_2439 BCE_2452 BCE_2730
                 BCE_2876 BCE_3046 BCE_3103 BCE_4217
            BCZ: BCZK0234(rimI) BCZK1445 BCZK1688 BCZK1831 BCZK2160(rimI)
                 BCZK2168(rimI) BCZK2175(rimI) BCZK2442 BCZK2575 BCZK2729
                 BCZK2793 BCZK3899(rimI)
            BTK: BT9727_0232(rimI) BT9727_1444 BT9727_1714 BT9727_2174(rimI)
                 BT9727_2181(rimI) BT9727_2214(rimI) BT9727_2477 BT9727_2607
                 BT9727_2749 BT9727_2833 BT9727_3892(rimI)
            BTL: BALH_0245(rimI) BALH_1414 BALH_1652 BALH_1789 BALH_2159(rimI)
                 BALH_2555 BALH_2694 BALH_2746 BALH_3759(rimI) BALH_3950
            BLI: BL00844 BL02628(yjcK)
            BLD: BLi00614(ydiD) BLi00739(yjcK)
            BCL: ABC0093 ABC0283 ABC0710 ABC0870 ABC1216 ABC2442
            BPU: BPUM_0524(rimI) BPUM_1821(yjcK) BPUM_2233
            OIH: OB0647
            GKA: GK0238
            SAU: SA1855
            SAV: SAV2050
            SAM: MW1974
            SAR: SAR2137
            SAS: SAS1955
            SAC: SACOL2039
            SAB: SAB1935c
            SAA: SAUSA300_2003(rimI)
            SAO: SAOUHSC_02278
            SEP: SE1651
            SER: SERP1662
            SHA: SH0983
            SSP: SSP0828
            LMO: lmo1698 lmo2076
            LMF: LMOf2365_1722 LMOf2365_2108(rimI)
            LIN: lin1806 lin2182
            LWE: lwe1716 lwe2001 lwe2097(rimI) lwe2465
            LLA: L93051(ycjD)
            LLC: LACR_0328 LACR_0329 LACR_0775
            LLM: llmg_0307 llmg_0308(rimI2)
            SPY: SPy_1873
            SPZ: M5005_Spy_1105 M5005_Spy_1592
            SPM: spyM18_1938(rimI)
            SPG: SpyM3_1617
            SPS: SPs0250
            SPH: MGAS10270_Spy1162 MGAS10270_Spy1663
            SPI: MGAS10750_Spy1204 MGAS10750_Spy1650
            SPJ: MGAS2096_Spy1167 MGAS2096_Spy1618
            SPK: MGAS9429_Spy1149 MGAS9429_Spy1597
            SPA: M6_Spy1077 M6_Spy1603
            SPB: M28_Spy1097 M28_Spy1584
            SPN: SP_0128
            SPR: spr0130(rimI)
            SPD: SPD_0135(rimI)
            SAG: SAG1758
            SAN: gbs1801
            SAK: SAK_1780(rimI)
            SMU: SMU.386
            STC: str1771(rimI)
            STL: stu1771(rimI)
            SSA: SSA_0317(rimI) SSA_1652
            SGO: SGO_0222
            LPL: lp_0718(rimI1) lp_0720(rimI2) lp_2909
            LJO: LJ0435
            LAC: LBA0389
            LSA: LSA0350
            LSL: LSL_1217(rimI)
            LDB: Ldb1622
            LBU: LBUL_1502
            LBR: LVIS_0611
            LCA: LSEI_2249
            LGA: LGAS_0380
            PPE: PEPE_1473
            EFA: EF2473 EF2474
            OOE: OEOE_1400
            STH: STH2923
            CAC: CAC0152 CAC2840
            CPE: CPE0059 CPE2166
            CPF: CPF_0066 CPF_2424(rimI)
            CPR: CPR_2134(rimI)
            CTC: CTC02445
            CNO: NT01CX_0504(rimI) NT01CX_0802
            CDF: CD0151(rimI)
            CBA: CLB_3380(rimI)
            CBH: CLC_3267(rimI)
            CBF: CLI_3495(rimI)
            CHY: CHY_0724(rimI)
            DSY: DSY1320 DSY1398 DSY3975
            SWO: Swol_1867
            TTE: TTE0537(rimI3)
            MTA: Moth_2158
            MPE: MYPE1290
            UUR: UU311(ard1)
            MTU: Rv0995 Rv3420c(rimI)
            MTC: MT1024(rimJ) MT3529
            MBO: Mb1022(rimJ) Mb3454c(rimI)
            MBB: BCG_1050(rimJ) BCG_3490c(rimI)
            MLE: ML0184(rimJ)
            MPA: MAP0926(rimJ) MAP4262(rimI)
            MAV: MAV_4368(rimI)
            MSM: MSMEG_1579(rimI) MSMEG_5469
            MMC: Mmcs_1150
            CGL: NCgl0568(cgl0593) NCgl0848(cgl0884)
            CGB: cg0686 cg1006
            CEF: CE0598 CE0958
            CDI: DIP0573 DIP0864
            CJK: jk1523(rimJ)
            NFA: nfa49510(rimJ) nfa8830
            RHA: RHA1_ro05634 RHA1_ro06184
            SCO: SCO4751(SC6G4.29) SCO6490(SC9C7.26)
            SMA: SAV1896 SAV3669(rimJ) SAV4973
            LXX: Lxx05920(rimJ) Lxx19920
            AAU: AAur_2884(rimI)
            PAC: PPA0495 PPA1783
            TFU: Tfu_0377 Tfu_2603
            FRA: Francci3_0628 Francci3_4036
            FAL: FRAAL1129 FRAAL6393
            ACE: Acel_0170 Acel_0359
            SEN: SACE_0776(rimJ) SACE_6724(rimI)
            BLO: BL1456(rimI) BL1556
            BAD: BAD_0290 BAD_0858(rimI)
            RXY: Rxyl_0811
            FNU: FN0055 FN0369 FN1294
            RBA: RB5015(rimI)
            CTA: CTA_0500(yhhY)
            LIL: LA3587
            LIC: LIC10612
            LBJ: LBJ_0327
            LBL: LBL_2749
            SYN: slr0853(rimI)
            SYW: SYNW0937 SYNW1379(rimI)
            SYC: syc1252_d(rimI)
            SYF: Synpcc7942_0261
            SYD: Syncc9605_1561 Syncc9605_1628
            SYE: Syncc9902_1390 Syncc9902_1816
            SYG: sync_1028(rimI)
            CYA: CYA_1768(rimI)
            CYB: CYB_1212(rimI)
            TEL: tll0471
            GVI: glr2063 glr2230
            ANA: alr1302 alr2998
            AVA: Ava_0911 Ava_3025
            PMA: Pro0877(wecD) Pro1106(rimI)
            PMM: PMM0333(rimI) PMM1089
            PMT: PMT0510(rimI) PMT1060
            PMN: PMN2A_0207 PMN2A_0659
            PMI: PMT9312_1100
            PMB: A9601_03581 A9601_11951
            PMC: P9515_03651 P9515_11801
            PMF: P9303_09921 P9303_17571
            PMG: P9301_03591 P9301_11961
            PMH: P9215_12251(rimI)
            PME: NATL1_08391 NATL1_14911
            TER: Tery_2436
            BTH: BT_0780
            DET: DET0608(rimI)
            DEH: cbdb_A591(rimI)
            TTH: TTC1448
            AAE: aq_567(rimI)
            MJA: MJ1530
            MMP: MMP1184 MMP1351
            MAC: MA2815 MA2816 MA4633
            MBA: Mbar_A0957 Mbar_A2251 Mbar_A2252 Mbar_A3398
            MMA: MM_1016 MM_1293 MM_2474 MM_2476 MM_2658 MM_2659 MM_2920
            MBU: Mbur_1771 Mbur_1957
            MHU: Mhun_2553
            MTH: MTH999
            MSI: Msm_0893
            MKA: MK0549
            AFU: AF0739
            HAL: VNG2575G(rimI)
            HMA: rrnAC2157(rimI)
            HWA: HQ3118A(rimI)
            NPH: NP0402A
            TAC: Ta0058
            PTO: PTO0743
            PHO: PH0296
            PAB: PAB1098
            PFU: PF0267
            TKO: TK2214
            APE: APE_1954
            SSO: SSO0082 SSO0209
            STO: ST0258 ST2077
            SAI: Saci_0073 Saci_0459
            PAI: PAE0771 PAE2246
STRUCTURES  PDB: 2CNM  2CNS  2CNT  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.128
            ExPASy - ENZYME nomenclature database: 2.3.1.128
            ExplorEnz - The Enzyme Database: 2.3.1.128
            ERGO genome analysis and discovery system: 2.3.1.128
            BRENDA, the Enzyme Database: 2.3.1.128
            CAS: 113383-52-1
///
ENTRY       EC 2.3.1.129                Enzyme
NAME        acyl-[acyl-carrier-protein]---UDP-N-acetylglucosamine
            O-acyltransferase;
            UDP-N-acetylglucosamine acyltransferase;
            uridine diphosphoacetylglucosamine acyltransferase;
            acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine
            O-acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein]:UDP-N-acetylglucos
            amine 3-O-(3-hydroxytetradecanoyl)transferase
REACTION    (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] +
            UDP-N-acetylglucosamine = [acyl-carrier-protein] +
            UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine [RN:R04567]
ALL_REAC    R04567
SUBSTRATE   (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein];
            UDP-N-acetylglucosamine [CPD:C00043]
PRODUCT     [acyl-carrier-protein];
            UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine [CPD:C04738]
COMMENT     Involved with EC 2.4.1.182 (lipid-A-disaccharide synthase) and EC
            2.7.1.130 (tetraacyldisaccharide 4'-kinase) in the biosynthesis of
            the phosphorylated glycolipid, Lipid A, in the outer membrane of
            Escherichia coli.
REFERENCE   1  [PMID:3905795]
  AUTHORS   Anderson MS, Bulawa CE, Raetz CR.
  TITLE     The biosynthesis of gram-negative endotoxin. Formation of lipid A
            precursors from UDP-GlcNAc in extracts of Escherichia coli.
  JOURNAL   J. Biol. Chem. 260 (1985) 15536-41.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00540  Lipopolysaccharide biosynthesis
ORTHOLOGY   KO: K00677  UDP-N-acetylglucosamine acyltransferase
GENES       OSA: 4324662
            ECO: b0181(lpxA)
            ECJ: JW0176(lpxA)
            ECE: Z0193(lpxA)
            ECS: ECs0183
            ECC: c0218(lpxA)
            ECI: UTI89_C0196(lpxA)
            ECP: ECP_0189
            ECV: APECO1_1806(lpxA)
            ECW: EcE24377A_0185(lpxA)
            ECX: EcHS_A0183(lpxA)
            STY: STY0251(lpxA)
            STT: t0229(lpxA)
            SPT: SPA0235(lpxA)
            SEC: SC0228(lpxA)
            STM: STM0228(lpxA)
            YPE: YPO1056(lpxA)
            YPK: y3123(lpxA)
            YPM: YP_2794(lpxA)
            YPA: YPA_0532
            YPN: YPN_2944
            YPP: YPDSF_1656
            YPS: YPTB2991(lpxA)
            YPI: YpsIP31758_1025(lpxA)
            YEN: YE2286(lpxA2)
            SFL: SF0171(lpxA)
            SFX: S0174(lpxA)
            SFV: SFV_0164(lpxA)
            SSN: SSON_0193(lpxA)
            SBO: SBO_0169(lpxA)
            SDY: SDY_0197(lpxA)
            ECA: ECA1043(lpxA)
            PLU: plu0684(lpxA)
            WBR: WGLp381(lpxA)
            SGL: SG1931
            ENT: Ent638_0719
            SPE: Spro_2352 Spro_3778
            BFL: Bfl283(lpxA)
            BPN: BPEN_291(lpxA)
            HIN: HI1061(lpxA)
            HIT: NTHI1222(lpxA)
            HIP: CGSHiEE_06865
            HIQ: CGSHiGG_08950
            HDU: HD1187(lpxA)
            HSO: HS_1359(lpxA)
            PMU: PM1996(lpxA)
            MSU: MS0461(lpxA)
            APL: APL_0407(lpxA)
            ASU: Asuc_1894
            XFA: XF1043
            XFT: PD0323(lpxA)
            XCC: XCC1361(lpxA)
            XCB: XC_2877
            XCV: XCV1466(lpxA)
            XAC: XAC1409(lpxA)
            XOO: XOO1965(lpxA)
            XOM: XOO_1855(XOO1855)
            VCH: VC2248
            VCO: VC0395_A1839(lpxA)
            VVU: VV1_1872
            VVY: VV2545
            VPA: VP2306
            VFI: VF1950
            PPR: PBPRA2956(lpxA)
            PAE: PA3644(lpxA)
            PAU: PA14_17210(lpxA)
            PAP: PSPA7_1495(lpxA)
            PPU: PP_1603(lpxA)
            PPF: Pput_4174
            PST: PSPTO_1546(lpxA)
            PSB: Psyr_1355
            PSP: PSPPH_3828(lpxA)
            PFL: PFL_1188(lpxA)
            PFO: Pfl_1113
            PEN: PSEEN4208(lpxA)
            PMY: Pmen_3041
            PAR: Psyc_1526(lpxA)
            PCR: Pcryo_0615 Pcryo_1705
            PRW: PsycPRwf_1793
            ACI: ACIAD1382(lpxA)
            SON: SO_1641(lpxA)
            SDN: Sden_1566
            SFR: Sfri_1282
            SAZ: Sama_1151
            SBL: Sbal_1462
            SBM: Shew185_1457
            SLO: Shew_2623
            SPC: Sputcn32_1360
            SSE: Ssed_3149
            SPL: Spea_2873
            SHE: Shewmr4_2629
            SHM: Shewmr7_2696
            SHN: Shewana3_2803
            SHW: Sputw3181_2743
            ILO: IL0833(lpxA)
            CPS: CPS_1565(lpxA)
            PHA: PSHAa2024(lpxA)
            PAT: Patl_1261
            SDE: Sde_2585
            PIN: Ping_2964
            MAQ: Maqu_2536
            CBU: CBU_0615(lpxA)
            CBD: COXBU7E912_0627(lpxA)
            LPN: lpg0511(lpxA) lpg2943
            LPF: lpl0549(lpxA) lpl2874(lpxA)
            LPP: lpp0573(lpxA) lpp3016(lpxA)
            MCA: MCA0397(lpxA-1) MCA2444(lpxA-2)
            FTU: FTT1569c(lpxA)
            FTF: FTF1569c(lpxA)
            FTW: FTW_0357(lpxA)
            FTL: FTL_0539
            FTH: FTH_0541(lpxA)
            FTA: FTA_0572(lpxA)
            FTN: FTN_1478(lpxA)
            TCX: Tcr_1274
            NOC: Noc_0229(lpxD) Noc_0819 Noc_1752
            AEH: Mlg_1852
            HHA: Hhal_1456
            HCH: HCH_05239(lpxA)
            CSA: Csal_0575
            ABO: ABO_1155(lpxA)
            MMW: Mmwyl1_1284
            AHA: AHA_1185(lpxA)
            DNO: DNO_0685(lpxA)
            RMA: Rmag_0556
            VOK: COSY_0510(lpxA)
            NME: NMB0178
            NMA: NMA0090(lpxA)
            NMC: NMC0168(lpxA)
            NGO: NGO1806
            CVI: CV_2208(lpxA)
            RSO: RSc1416(lpxA)
            REU: Reut_A1869
            REH: H16_A2043(lpxA)
            RME: Rmet_1447
            BMA: BMA1543(lpxA)
            BMV: BMASAVP1_A2043(lpxA)
            BML: BMA10299_A3268(lpxA)
            BMN: BMA10247_1315(lpxA)
            BXE: Bxe_A1694
            BVI: Bcep1808_1913
            BUR: Bcep18194_A5317 Bcep18194_A5319(lpxD)
            BCN: Bcen_6070
            BCH: Bcen2424_2007
            BAM: Bamb_2040
            BPS: BPSL2147(lpxA)
            BPM: BURPS1710b_2570(lpxA)
            BPL: BURPS1106A_2480(lpxA)
            BPD: BURPS668_2424(lpxA)
            BTE: BTH_I2039(lpxA)
            PNU: Pnuc_1439
            BPE: BP1431(lpxA)
            BPA: BPP1539(lpxA)
            BBR: BB2617(lpxA)
            RFR: Rfer_2000
            POL: Bpro_2683
            PNA: Pnap_1770
            AAV: Aave_1835
            AJS: Ajs_2573
            VEI: Veis_1450
            MPT: Mpe_A1968
            HAR: HEAR1345(lpxD) HEAR1347(lpxA)
            MMS: mma_2046(lpxA)
            NMU: Nmul_A2199
            EBA: ebA6000(lpxA)
            AZO: azo1897(lpxA)
            DAR: Daro_1754
            TBD: Tbd_0797
            MFA: Mfla_1518
            HPY: HP1375(lpxA)
            HPJ: jhp1289(lpxA)
            HPA: HPAG1_1321
            HHE: HH1182(lpxA)
            HAC: Hac_0063(lpxA)
            WSU: WS0059(lpxA)
            TDN: Tmden_0900 Tmden_1463
            CJE: Cj0274(lpxA)
            CJR: CJE0323(lpxA)
            CJJ: CJJ81176_0301(lpxA)
            CJU: C8J_0251(lpxA)
            CJD: JJD26997_1696(lpxA)
            CFF: CFF8240_0315(lpxA)
            CCV: CCV52592_0866(lpxA)
            CHA: CHAB381_1354(lpxA)
            CCO: CCC13826_1880
            ABU: Abu_2215(lpxA)
            NIS: NIS_0541(lpxA)
            SUN: SUN_1111(lpxA)
            GSU: GSU0999 GSU2264(lpxA)
            GME: Gmet_2353 Gmet_2567
            GUR: Gura_3233
            PCA: Pcar_1255 Pcar_1495
            PPD: Ppro_3021
            DVU: DVU2367(lpxA)
            DVL: Dvul_0896
            DDE: Dde_1372 Dde_1374
            LIP: LI1019(lpxA)
            BBA: Bd1495(lpxA)
            DPS: DP2943
            ADE: Adeh_1085
            AFW: Anae109_1124
            MXA: MXAN_4724(lpxA)
            SAT: SYN_01567
            SFU: Sfum_3749
            RPR: RP007
            RTY: RT0006(lpxA)
            RCO: RC0008(lpxA)
            RFE: RF_0006(lpxA)
            RBE: RBE_1187(lpxA)
            RAK: A1C_00030
            RBO: A1I_01345
            RCM: A1E_00030
            RRI: A1G_00035
            PUB: SAR11_0917(lpxA)
            MLO: mll0633
            MES: Meso_1391
            PLA: Plav_3184
            SME: SMc02091(lpxA)
            SMD: Smed_1141
            ATU: Atu1384(lpxA)
            ATC: AGR_C_2560
            RET: RHE_CH01923(lpxA)
            RLE: RL2231(lpxA)
            BME: BMEI0833
            BMF: BAB1_1173(lpxA)
            BMS: BR1151(lpxA)
            BMB: BruAb1_1157(lpxA)
            BOV: BOV_1109(lpxA)
            OAN: Oant_2039
            BJA: bll4849(lpxA)
            BRA: BRADO4129(lpxA)
            BBT: BBta_4506(lpxA)
            RPA: RPA2911(lpxA)
            RPB: RPB_2817
            RPC: RPC_2447
            RPD: RPD_2846
            RPE: RPE_2564
            NWI: Nwi_1848 Nwi_1850(lpxD) Nwi_3100(lpxD)
            NHA: Nham_1705
            BHE: BH06310(lpxA)
            BQU: BQ06920(lpxA)
            BBK: BARBAKC583_0592(lpxA)
            XAU: Xaut_4428
            CCR: CC_1911
            SIL: SPO1673(lpxA)
            SIT: TM1040_1404
            RSP: RSP_2714(lpxA)
            RSH: Rsph17029_1372
            RSQ: Rsph17025_2143
            JAN: Jann_2450
            RDE: RD1_2596(lpxA)
            PDE: Pden_3907
            MMR: Mmar10_1392
            HNE: HNE_1779(lpxA)
            GOX: GOX1822
            GBE: GbCGDNIH1_0944
            ACR: Acry_2448
            RRU: Rru_A1597
            MAG: amb2486
            MGM: Mmc1_1851
            ABA: Acid345_0235
            SUS: Acid_2855 Acid_6203
            RHA: RHA1_ro04101
            FNU: FN0595
            RBA: RB4936(lpxA)
            CTR: CT531(lpxA)
            CTA: CTA_0580(lpxA)
            CMU: TC0818
            CPN: CPn0650(lpxA)
            CPA: CP0097
            CPJ: CPj0650(lpxA)
            CPT: CpB0676
            CCA: CCA00090(lpxA)
            CAB: CAB090(lpxA)
            CFE: CF0916(lpxA)
            PCU: pc0403(lpxA)
            LIL: LA3949(lpxA)
            LIC: LIC13154(lpxA)
            LBJ: LBJ_0408(lpxA)
            LBL: LBL_2669(lpxA)
            SYN: sll0379(lpxA)
            SYW: SYNW0558(lpxA)
            SYC: syc0611_c(lpxA) syc1734_d
            SYF: Synpcc7942_0931 Synpcc7942_2371
            SYD: Syncc9605_2116
            SYE: Syncc9902_0557
            SYG: sync_2212(lpxA)
            SYR: SynRCC307_1816(lpxA)
            SYX: SynWH7803_1956(lpxA)
            CYA: CYA_1960(lpxA)
            CYB: CYB_2787(lpxA)
            TEL: tll2224 tlr1792
            GVI: glr1867
            ANA: alr2272
            AVA: Ava_0097 Ava_0837(lpxD)
            PMA: Pro1416(lpxA)
            PMM: PMM1335(lpxA)
            PMT: PMT1410(lpxA)
            PMN: PMN2A_0906
            PMI: PMT9312_1433
            PMB: A9601_15351(lpxA)
            PMC: P9515_14961(lpxA)
            PMF: P9303_05521(lpxA)
            PMG: P9301_15211(lpxA)
            PMH: P9215_15641(lpxA)
            PME: NATL1_17621(lpxA)
            TER: Tery_3320
            BTH: BT_3336 BT_4205
            BFR: BF0188 BF0905
            BFS: BF0153 BF0827(lpxA)
            PGI: PG0070(lpxA)
            CHU: CHU_1036(lpxA)
            GFO: GFO_1774(lpxA)
            FJO: Fjoh_2902
            FPS: FP0976(lpxA)
            CTE: CT2008(lpxA)
            CCH: Cag_0198 Cag_1154(lpxD)
            CPH: Cpha266_2373
            PVI: Cvib_0290
            PLT: Plut_0224
            AAE: aq_604(lpxA)
STRUCTURES  PDB: 1J2Z  1LXA  2AQ9  2JF2  2JF3  2QIA  2QIV  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.129
            ExPASy - ENZYME nomenclature database: 2.3.1.129
            ExplorEnz - The Enzyme Database: 2.3.1.129
            ERGO genome analysis and discovery system: 2.3.1.129
            BRENDA, the Enzyme Database: 2.3.1.129
            CAS: 105843-69-4
///
ENTRY       EC 2.3.1.130                Enzyme
NAME        galactarate O-hydroxycinnamoyltransferase;
            galacturate hydroxycinnamoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     feruloyl-CoA:galactarate O-(hydroxycinnamoyl)transferase
REACTION    feruloyl-CoA + galactarate = CoA + O-feruloylgalactarate [RN:R03727]
ALL_REAC    R03727
SUBSTRATE   feruloyl-CoA [CPD:C00406];
            galactarate [CPD:C01807]
PRODUCT     CoA [CPD:C00010];
            O-feruloylgalactarate [CPD:C03156]
COMMENT     Sinapoyl-CoA and 4-coumaroyl-CoA can also act as donors.
REFERENCE   1
  AUTHORS   Strack, D., Keller, H. and Weissenbock, G.
  TITLE     Enzymatic-synthesis of hydroxycinnamic acid-esters of sugar acids
            and hydroaromatic acids by protein preparations from rye (Secale
            cereale) primary leaves.
  JOURNAL   J. Plant Physiol. 131 (1987) 61-73.
  ORGANISM  Secale cereale
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.130
            ExPASy - ENZYME nomenclature database: 2.3.1.130
            ExplorEnz - The Enzyme Database: 2.3.1.130
            ERGO genome analysis and discovery system: 2.3.1.130
            BRENDA, the Enzyme Database: 2.3.1.130
            CAS: 112956-50-0
///
ENTRY       EC 2.3.1.131                Enzyme
NAME        glucarate O-hydroxycinnamoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     sinapoyl-CoA:glucarate O-(hydroxycinnamoyl)transferase
REACTION    sinapoyl-CoA + glucarate = CoA + O-sinapoylglucarate [RN:R02899]
ALL_REAC    R02899
SUBSTRATE   sinapoyl-CoA [CPD:C00411];
            glucarate [CPD:C00767]
PRODUCT     CoA [CPD:C00010];
            O-sinapoylglucarate [CPD:C02866]
COMMENT     4-Coumaroyl-CoA, feruloyl-CoA and caffeoyl-CoA can also act as
            donors, but more slowly.
REFERENCE   1
  AUTHORS   Strack, D., Keller, H. and Weissenbock, G.
  TITLE     Enzymatic-synthesis of hydroxycinnamic acid-esters of sugar acids
            and hydroaromatic acids by protein preparations from rye (Secale
            cereale) primary leaves.
  JOURNAL   J. Plant Physiol. 131 (1987) 61-73.
  ORGANISM  Secale cereale
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.131
            ExPASy - ENZYME nomenclature database: 2.3.1.131
            ExplorEnz - The Enzyme Database: 2.3.1.131
            ERGO genome analysis and discovery system: 2.3.1.131
            BRENDA, the Enzyme Database: 2.3.1.131
            CAS: 112956-51-1
///
ENTRY       EC 2.3.1.132                Enzyme
NAME        glucarolactone O-hydroxycinnamoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     sinapoyl-CoA:glucarolactone O-(hydroxycinnamoyl)transferase
REACTION    sinapoyl-CoA + glucarolactone = CoA + O-sinapoylglucarolactone
            [RN:R03861]
ALL_REAC    R03861
SUBSTRATE   sinapoyl-CoA [CPD:C00411];
            glucarolactone
PRODUCT     CoA [CPD:C00010];
            O-sinapoylglucarolactone [CPD:C03526]
COMMENT     4-Coumaroyl-CoA, feruloyl-CoA and caffeoyl-CoA can also act as
            donors, but more slowly.
REFERENCE   1
  AUTHORS   Strack, D., Keller, H. and Weissenbock, G.
  TITLE     Enzymatic-synthesis of hydroxycinnamic acid-esters of sugar acids
            and hydroaromatic acids by protein preparations from rye (Secale
            cereale) primary leaves.
  JOURNAL   J. Plant Physiol. 131 (1987) 61-73.
  ORGANISM  Secale cereale
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.132
            ExPASy - ENZYME nomenclature database: 2.3.1.132
            ExplorEnz - The Enzyme Database: 2.3.1.132
            ERGO genome analysis and discovery system: 2.3.1.132
            BRENDA, the Enzyme Database: 2.3.1.132
            CAS: 112956-52-2
///
ENTRY       EC 2.3.1.133                Enzyme
NAME        shikimate O-hydroxycinnamoyltransferase;
            shikimate hydroxycinnamoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     4-coumaroyl-CoA:shikimate O-(hydroxycinnamoyl)transferase
REACTION    4-coumaroyl-CoA + shikimate = CoA + 4-coumaroylshikimate [RN:R02416]
ALL_REAC    R02416;
            (other) R07432 R07433 R07434
SUBSTRATE   4-coumaroyl-CoA [CPD:C00223];
            shikimate [CPD:C00493]
PRODUCT     CoA [CPD:C00010];
            4-coumaroylshikimate [CPD:C02947]
COMMENT     Caffeoyl-CoA, feruloyl-CoA and sinapoyl-CoA can also act as donors,
            but more slowly.
REFERENCE   1
  AUTHORS   Strack, D., Keller, H. and Weissenbock, G.
  TITLE     Enzymatic-synthesis of hydroxycinnamic acid-esters of sugar acids
            and hydroaromatic acids by protein preparations from rye (Secale
            cereale) primary leaves.
  JOURNAL   J. Plant Physiol. 131 (1987) 61-73.
  ORGANISM  Secale cereale
REFERENCE   2
  AUTHORS   Ulbrich, B. and Zenk, M.H.
  TITLE     Partial purification and properties of
            p-hydroxycinnamoyl-CoA:shikimate-p-hydroxycinnamoyl transferase from
            higher plants.
  JOURNAL   Phytochemistry 19 (1980) 1625-1629.
  ORGANISM  Cichorium endivia
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.133
            ExPASy - ENZYME nomenclature database: 2.3.1.133
            ExplorEnz - The Enzyme Database: 2.3.1.133
            ERGO genome analysis and discovery system: 2.3.1.133
            BRENDA, the Enzyme Database: 2.3.1.133
            CAS: 73904-44-6
///
ENTRY       EC 2.3.1.134                Enzyme
NAME        galactolipid O-acyltransferase;
            galactolipid:galactolipid acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     mono-beta-D-galactosyldiacylglycerol:mono-beta-D-galactosyldiacylgly
            cerol acyltransferase
REACTION    2 mono-beta-D-galactosyldiacylglycerol =
            acylmono-beta-D-galactosyldiacylglycerol +
            mono-beta-D-galactosylacylglycerol [RN:R04474]
ALL_REAC    R04474
SUBSTRATE   mono-beta-D-galactosyldiacylglycerol
PRODUCT     acylmono-beta-D-galactosyldiacylglycerol [CPD:C06038];
            mono-beta-D-galactosylacylglycerol [CPD:C04315]
COMMENT     Di-D-galactosyldiacylglycerol can also act as acceptor.
REFERENCE   1
  AUTHORS   Heemskerk, J.W.M., Wintermans, J.F.G.M., Joyard, J., Block, M.A.,
            Dorne, A.-J. and Douce, R.
  TITLE     Localization of galactolipid:galactolipid galactosyltransferase and
            acyltransferase in outer envelope membrane of spinach chloroplasts.
  JOURNAL   Biochim. Biophys. Acta 877 (1986) 281-289.
  ORGANISM  spinach,
REFERENCE   2
  AUTHORS   Heinz, E.
  TITLE     Some properties of the acyl galactoside-forming enzyme from leaves.
  JOURNAL   Z. Pflanzenphysiol. 69 (1973) 359-376.
  ORGANISM  Vicia faba
PATHWAY     PATH: map00561  Glycerolipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.134
            ExPASy - ENZYME nomenclature database: 2.3.1.134
            ExplorEnz - The Enzyme Database: 2.3.1.134
            ERGO genome analysis and discovery system: 2.3.1.134
            BRENDA, the Enzyme Database: 2.3.1.134
            CAS: 103537-09-3
///
ENTRY       EC 2.3.1.135                Enzyme
NAME        phosphatidylcholine---retinol O-acyltransferase;
            lecithin---retinol acyltransferase;
            phosphatidylcholine:retinol-(cellular-retinol-binding-protein)
            O-acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     phosphatidylcholine:retinol---[cellular-retinol-binding-protein]
            O-acyltransferase
REACTION    phosphatidylcholine + retinol---[cellular-retinol-binding-protein] =
            2-acylglycerophosphocholine +
            retinyl-ester---[cellular-retinol-binding-protein] [RN:R04514]
ALL_REAC    R04514
SUBSTRATE   phosphatidylcholine [CPD:C00157];
            retinol---[cellular-retinol-binding-protein]
PRODUCT     2-acylglycerophosphocholine;
            retinyl-ester---[cellular-retinol-binding-protein]
COMMENT     Specific for transfer of the sn-1-acyl residue of
            phosphatidylcholine.
REFERENCE   1  [PMID:3410848]
  AUTHORS   MacDonald PN, Ong DE.
  TITLE     Evidence for a lecithin-retinol acyltransferase activity in the rat
            small intestine.
  JOURNAL   J. Biol. Chem. 263 (1988) 12478-82.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:2722792]
  AUTHORS   Saari JC, Bredberg DL.
  TITLE     Lecithin:retinol acyltransferase in retinal pigment epithelial
            microsomes.
  JOURNAL   J. Biol. Chem. 264 (1989) 8636-40.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K00678  phosphatidylcholine-retinol O-acyltransferase
GENES       HSA: 9227(LRAT)
            PTR: 471328(LRAT)
            MMU: 79235(Lrat)
            RNO: 64047(Lrat)
            CFA: 482660(LRAT)
            BTA: 281285(LRAT)
            GGA: 422403(LRAT)
            XLA: 443823(MGC80134)
            XTR: 394746(MGC75880)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.135
            ExPASy - ENZYME nomenclature database: 2.3.1.135
            ExplorEnz - The Enzyme Database: 2.3.1.135
            ERGO genome analysis and discovery system: 2.3.1.135
            BRENDA, the Enzyme Database: 2.3.1.135
            CAS: 117444-03-8
///
ENTRY       EC 2.3.1.136                Enzyme
NAME        polysialic-acid O-acetyltransferase;
            lecithin:retinol acyltransferase;
            lecithin-retinol acyltransferase;
            retinyl ester synthase;
            LRAT;
            lecithin retinol acyl transferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:polysialic-acid O-acetyltransferase
REACTION    acetyl-CoA + an alpha-2,8-linked polymer of sialic acid = CoA +
            polysialic acid acetylated on O-7 or O-9 [RN:R04484 R07249]
ALL_REAC    R04484 R07249
SUBSTRATE   acetyl-CoA [CPD:C00024];
            alpha-2,8-linked polymer of sialic acid [CPD:C04466]
PRODUCT     CoA [CPD:C00010];
            polysialic acid acetylated on O-7;
            polysialic acid acetylated on O-9
COMMENT     Acts only on substrates containing more than 14 sialosyl residues.
            Catalyses the modification of capsular polysaccharides in some
            strains of Escherichia coli.
REFERENCE   1  [PMID:2897964]
  AUTHORS   Higa HH, Varki A.
  TITLE     Acetyl-coenzyme A:polysialic acid O-acetyltransferase from
            K1-positive Escherichia coli. The enzyme responsible for the
            O-acetyl plus phenotype and for O-acetyl form variation.
  JOURNAL   J. Biol. Chem. 263 (1988) 8872-8.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.136
            ExPASy - ENZYME nomenclature database: 2.3.1.136
            ExplorEnz - The Enzyme Database: 2.3.1.136
            ERGO genome analysis and discovery system: 2.3.1.136
            BRENDA, the Enzyme Database: 2.3.1.136
            CAS: 116412-21-6
///
ENTRY       EC 2.3.1.137                Enzyme
NAME        carnitine O-octanoyltransferase;
            medium-chain/long-chain carnitine acyltransferase;
            carnitine medium-chain acyltransferase;
            easily solubilized mitochondrial carnitine palmitoyltransferase;
            overt mitochondrial carnitine palmitoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     octanoyl-CoA:L-carnitine O-octanoyltransferase
REACTION    octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine [RN:R03779]
ALL_REAC    R03779
SUBSTRATE   octanoyl-CoA [CPD:C01944];
            L-carnitine [CPD:C00318]
PRODUCT     CoA [CPD:C00010];
            L-octanoylcarnitine [CPD:C02838]
COMMENT     Acts on a range of acyl-CoAs, with optimal activity with C6 or C8
            acyl groups. cf. EC 2.3.1.7 (carnitine O-acetyltransferase) and EC
            2.3.1.21 (carnitine O-palmitoyltransferase).
REFERENCE   1  [PMID:6436243]
  AUTHORS   Farrell SO, Fiol CJ, Reddy JK, Bieber LL.
  TITLE     Properties of purified carnitine acyltransferases of mouse liver
            peroxisomes.
  JOURNAL   J. Biol. Chem. 259 (1984) 13089-95.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:3342008]
  AUTHORS   Healy MJ, Kerner J, Bieber LL.
  TITLE     Enzymes of carnitine acylation. Is overt carnitine
            palmitoyltransferase of liver peroxisomal carnitine
            octanoyltransferase?
  JOURNAL   Biochem. J. 249 (1988) 231-7.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:6630173]
  AUTHORS   Miyazawa S, Ozasa H, Osumi T, Hashimoto T.
  TITLE     Purification and properties of carnitine octanoyltransferase and
            carnitine palmitoyltransferase from rat liver.
  JOURNAL   J. Biochem. (Tokyo). 94 (1983) 529-42.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K05940  
GENES       HSA: 54677(CROT)
            MCC: 706186(LOC706186)
            MMU: 74114(Crot)
            RNO: 83842(Crot)
            CFA: 482283(CROT)
            BTA: 281092(CROT)
            GGA: 420533(CROT)
            SPU: 585404(LOC585404)
STRUCTURES  PDB: 1XL7  1XL8  1XMC  1XMD  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.137
            ExPASy - ENZYME nomenclature database: 2.3.1.137
            ExplorEnz - The Enzyme Database: 2.3.1.137
            ERGO genome analysis and discovery system: 2.3.1.137
            BRENDA, the Enzyme Database: 2.3.1.137
            CAS: 39369-19-2
///
ENTRY       EC 2.3.1.138                Enzyme
NAME        putrescine N-hydroxycinnamoyltransferase;
            caffeoyl-CoA putrescine N-caffeoyl transferase;
            PHT;
            putrescine hydroxycinnamoyl transferase;
            hydroxycinnamoyl-CoA:putrescine hydroxycinnamoyltransferase;
            putrescine hydroxycinnamoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     caffeoyl-CoA:putrescine N-(3,4-dihydroxycinnamoyl)transferase
REACTION    caffeoyl-CoA + putrescine = CoA + N-caffeoylputrescine [RN:R01944]
ALL_REAC    R01944
SUBSTRATE   caffeoyl-CoA [CPD:C00323];
            putrescine [CPD:C00134]
PRODUCT     CoA [CPD:C00010];
            N-caffeoylputrescine [CPD:C03002]
COMMENT     Feruloyl-CoA, cinnamoyl-CoA and sinapoyl-CoA can also act as donors,
            but more slowly.
REFERENCE   1
  AUTHORS   Negrel, J.
  TITLE     The biosynthesis of cinnamoylputrescines in callus-tissue cultures
            of Nicotiana tabacum.
  JOURNAL   Phytochemistry 28 (1989) 477-481.
  ORGANISM  Nicotiana tabacum
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.138
            ExPASy - ENZYME nomenclature database: 2.3.1.138
            ExplorEnz - The Enzyme Database: 2.3.1.138
            ERGO genome analysis and discovery system: 2.3.1.138
            BRENDA, the Enzyme Database: 2.3.1.138
            CAS: 120598-69-8
///
ENTRY       EC 2.3.1.139                Enzyme
NAME        ecdysone O-acyltransferase;
            acyl-CoA:ecdysone acyltransferase;
            fatty acyl-CoA:ecdysone acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     palmitoyl-CoA:ecdysone palmitoyltransferase
REACTION    palmitoyl-CoA + ecdysone = CoA + ecdysone palmitate [RN:R02375]
ALL_REAC    R02375
SUBSTRATE   palmitoyl-CoA [CPD:C00154];
            ecdysone [CPD:C00477]
PRODUCT     CoA [CPD:C00010];
            ecdysone palmitate [CPD:C02681]
REFERENCE   1
  AUTHORS   Slinger, A.J. and Isaac, R.E.
  TITLE     Acyl-CoA-ecdysone acyltransferase activity from the ovary of P.
            americana.
  JOURNAL   Insect Biochem. 18 (1988) 779-784.
  ORGANISM  Periplaneta americana
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.139
            ExPASy - ENZYME nomenclature database: 2.3.1.139
            ExplorEnz - The Enzyme Database: 2.3.1.139
            ERGO genome analysis and discovery system: 2.3.1.139
            BRENDA, the Enzyme Database: 2.3.1.139
            CAS: 120038-26-8
///
ENTRY       EC 2.3.1.140                Enzyme
NAME        rosmarinate synthase;
            rosmarinic acid synthase;
            caffeoyl-coenzyme A:3,4-dihydroxyphenyllactic acid
            caffeoyltransferase;
            4-coumaroyl-CoA:4-hydroxyphenyllactic acid 4-coumaroyl transferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     caffeoyl-CoA:3-(3,4-dihydroxyphenyl)lactate
            2'-O-caffeoyl-transferase
REACTION    caffeoyl-CoA + 3-(3,4-dihydroxyphenyl)lactate = CoA + rosmarinate
            [RN:R03374]
ALL_REAC    R03374
SUBSTRATE   caffeoyl-CoA [CPD:C00323];
            3-(3,4-dihydroxyphenyl)lactate [CPD:C01207]
PRODUCT     CoA [CPD:C00010];
            rosmarinate [CPD:C01850]
COMMENT     Involved, with EC 1.1.1.237 (hydroxyphenylpyruvate reductase) in the
            biosynthesis of rosmarinic acid.
REFERENCE   1
  AUTHORS   Petersen, M. and Alfermann, A.W.
  TITLE     Two new enzymes of rosmarinic acid biosynthesis from cell cultures
            of Coleus blumei: hydroxyphenylpyruvate reductase and rosmarinic
            acid synthase.
  JOURNAL   Z. Naturforsch. C: Biosci. 43 (1988) 501-504.
  ORGANISM  Coleus blumei
PATHWAY     PATH: map00350  Tyrosine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.140
            ExPASy - ENZYME nomenclature database: 2.3.1.140
            ExplorEnz - The Enzyme Database: 2.3.1.140
            ERGO genome analysis and discovery system: 2.3.1.140
            BRENDA, the Enzyme Database: 2.3.1.140
            CAS: 117590-80-4
///
ENTRY       EC 2.3.1.141                Enzyme
NAME        galactosylacylglycerol O-acyltransferase;
            acyl-acyl-carrier protein: lysomonogalactosyldiacylglycerol
            acyltransferase;
            acyl-ACP:lyso-MGDG acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-[acyl-carrier-protein]:D-galactosylacylglycerol
            O-acyltransferase
REACTION    acyl-[acyl-carrier-protein] + sn-3-D-galactosyl-sn-2-acylglycerol =
            [acyl-carrier-protein] + D-galactosyldiacylglycerol [RN:R04473]
ALL_REAC    R04473
SUBSTRATE   acyl-[acyl-carrier-protein];
            sn-3-D-galactosyl-sn-2-acylglycerol [CPD:C04315]
PRODUCT     [acyl-carrier-protein];
            D-galactosyldiacylglycerol [CPD:C03692]
COMMENT     Transfers long-chain acyl groups to the sn-1 position of the
            glycerol residue.
REFERENCE   1  [PMID:3143419]
  AUTHORS   Chen HH, Wickrema A, Jaworski JG.
  TITLE     Acyl-acyl-carrier protein: lysomonogalactosyldiacylglycerol
            acyltransferase from the cyanobacterium Anabaena variabilis.
  JOURNAL   Biochim. Biophys. Acta. 963 (1988) 493-500.
  ORGANISM  Anabaena variabilis [GN:ava]
PATHWAY     PATH: map00561  Glycerolipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.141
            ExPASy - ENZYME nomenclature database: 2.3.1.141
            ExplorEnz - The Enzyme Database: 2.3.1.141
            ERGO genome analysis and discovery system: 2.3.1.141
            BRENDA, the Enzyme Database: 2.3.1.141
            CAS: 119129-68-9
///
ENTRY       EC 2.3.1.142                Enzyme
NAME        glycoprotein O-fatty-acyltransferase;
            protein acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     fatty-acyl-CoA:mucus-glycoprotein fatty-acyltransferase
REACTION    palmitoyl-CoA + mucus glycoprotein = CoA + O-palmitoylglycoprotein
            [RN:R04021]
ALL_REAC    R04021
SUBSTRATE   palmitoyl-CoA [CPD:C00154];
            mucus glycoprotein [CPD:C02705]
PRODUCT     CoA [CPD:C00010];
            O-palmitoylglycoprotein [CPD:C03422]
REFERENCE   1  [PMID:2318887]
  AUTHORS   Kasinathan C, Grzelinska E, Okazaki K, Slomiany BL, Slomiany A.
  TITLE     Purification of protein fatty acyltransferase and determination of
            its distribution and topology.
  JOURNAL   J. Biol. Chem. 265 (1990) 5139-44.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.142
            ExPASy - ENZYME nomenclature database: 2.3.1.142
            ExplorEnz - The Enzyme Database: 2.3.1.142
            ERGO genome analysis and discovery system: 2.3.1.142
            BRENDA, the Enzyme Database: 2.3.1.142
            CAS: 122191-29-1
///
ENTRY       EC 2.3.1.143                Enzyme
NAME        beta-glucogallin---tetrakisgalloylglucose O-galloyltransferase;
            beta-glucogallin-tetragalloylglucose 4-galloyltransferase;
            beta-glucogallin:1,2,3,6-tetra-O-galloylglucose
            4-O-galloyltransferase;
            beta-glucogallin:1,2,3,6-tetra-O-galloyl-beta-D-glucose
            4-O-galloyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     1-O-galloyl-beta-D-glucose:1,2,3,6-tetrakis-O-galloyl-beta-D-glucose
            4-O-galloyltransferase
REACTION    1-O-galloyl-beta-D-glucose +
            1,2,3,6-tetrakis-O-galloyl-beta-D-glucose = D-glucose +
            1,2,3,4,6-pentakis-O-galloyl-beta-D-glucose [RN:R04498]
ALL_REAC    R04498
SUBSTRATE   1-O-galloyl-beta-D-glucose [CPD:C01158];
            1,2,3,6-tetrakis-O-galloyl-beta-D-glucose [CPD:C04516]
PRODUCT     D-glucose [CPD:C00031];
            1,2,3,4,6-pentakis-O-galloyl-beta-D-glucose [CPD:C04576]
REFERENCE   1  [PMID:2757399]
  AUTHORS   Cammann J, Denzel K, Schilling G, Gross GG.
  TITLE     Biosynthesis of gallotannins: beta-glucogallin-dependent formation
            of 1,2,3,4,6-pentagalloylglucose by enzymatic galloylation of
            1,2,3,6-tetragalloylglucose.
  JOURNAL   Arch. Biochem. Biophys. 273 (1989) 58-63.
  ORGANISM  Quercus robur
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.143
            ExPASy - ENZYME nomenclature database: 2.3.1.143
            ExplorEnz - The Enzyme Database: 2.3.1.143
            ERGO genome analysis and discovery system: 2.3.1.143
            BRENDA, the Enzyme Database: 2.3.1.143
            CAS: 122653-70-7
///
ENTRY       EC 2.3.1.144                Enzyme
NAME        anthranilate N-benzoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     benzoyl-CoA:anthranilate N-benzoyltransferase
REACTION    benzoyl-CoA + anthranilate = CoA + N-benzoylanthranilate [RN:R02453]
ALL_REAC    R02453
SUBSTRATE   benzoyl-CoA [CPD:C00512];
            anthranilate [CPD:C00108]
PRODUCT     CoA [CPD:C00010];
            N-benzoylanthranilate [CPD:C03141]
COMMENT     Cinnamoyl-CoA, 4-coumaroyl-CoA and salicyloyl-CoA can act as donors,
            but more slowly. Involved in the biosynthesis of phytoalexins.
REFERENCE   1  [PMID:2817901]
  AUTHORS   Reinhard K, Matern U.
  TITLE     The biosynthesis of phytoalexins in Dianthus caryophyllus L. cell
            cultures: induction of benzoyl-CoA:anthranilate N-benzoyltransferase
            activity.
  JOURNAL   Arch. Biochem. Biophys. 275 (1989) 295-301.
  ORGANISM  Dianthus caryophyllus
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.144
            ExPASy - ENZYME nomenclature database: 2.3.1.144
            ExplorEnz - The Enzyme Database: 2.3.1.144
            ERGO genome analysis and discovery system: 2.3.1.144
            BRENDA, the Enzyme Database: 2.3.1.144
            CAS: 125498-59-1
///
ENTRY       EC 2.3.1.145                Enzyme
NAME        piperidine N-piperoyltransferase;
            piperidine piperoyltransferase;
            piperoyl-CoA:piperidine N-piperoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     (E,E)-piperoyl-CoA:piperidine N-piperoyltransferase
REACTION    (E,E)-piperoyl-CoA + piperidine = CoA +
            N-[(E,E)-piperoyl]-piperidine [RN:R03994]
ALL_REAC    R03994
SUBSTRATE   (E,E)-piperoyl-CoA [CPD:C02611];
            piperidine [CPD:C01746]
PRODUCT     CoA [CPD:C00010];
            N-[(E,E)-piperoyl]-piperidine
COMMENT     Pyrrolidine and 3-pyrroline can also act as acceptors, but more
            slowly.
REFERENCE   1
  AUTHORS   Geisler, J.G. and Gross, G.G.
  TITLE     The biosynthesis of piperine in Piper nigrum.
  JOURNAL   Phytochemistry 29 (1990) 489-492.
  ORGANISM  Piper nigrum
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.145
            ExPASy - ENZYME nomenclature database: 2.3.1.145
            ExplorEnz - The Enzyme Database: 2.3.1.145
            ERGO genome analysis and discovery system: 2.3.1.145
            BRENDA, the Enzyme Database: 2.3.1.145
            CAS: 126806-22-2
///
ENTRY       EC 2.3.1.146                Enzyme
NAME        pinosylvin synthase;
            stilbene synthase;
            pine stilbene synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     malonyl-CoA:cinnamoyl-CoA malonyltransferase (cyclizing)
REACTION    3 malonyl-CoA + cinnamoyl-CoA = 4 CoA + pinosylvin + 4 CO2
            [RN:R02505]
ALL_REAC    R02505
SUBSTRATE   malonyl-CoA [CPD:C00083];
            cinnamoyl-CoA [CPD:C00540]
PRODUCT     CoA [CPD:C00010];
            pinosylvin [CPD:C01745];
            CO2 [CPD:C00011]
COMMENT     Not identical with EC 2.3.1.74 (naringenin-chalcone synthase) or EC
            2.3.1.95 (trihydroxystilbene synthase).
REFERENCE   1
  AUTHORS   Gehlert, R., Schoppner, A. and Kindl, H.
  TITLE     Stilbene synthase from seedlings of Pinus sylvestris - purification
            and induction in response to fungal infection.
  JOURNAL   Mol. Plant-Microbe Interaction 3 (1990) 444-449.
  ORGANISM  Pinus sylvestris
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.146
            ExPASy - ENZYME nomenclature database: 2.3.1.146
            ExplorEnz - The Enzyme Database: 2.3.1.146
            ERGO genome analysis and discovery system: 2.3.1.146
            BRENDA, the Enzyme Database: 2.3.1.146
            CAS: 72994-49-1
///
ENTRY       EC 2.3.1.147                Enzyme
NAME        glycerophospholipid arachidonoyl-transferase (CoA-independent)
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine:1-organyl-2-lys
            o-sn-glycero-3-phosphoethanolamine arachidonoyltransferase
            (CoA-independent)
REACTION    1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine +
            1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine =
            1-organyl-2-arachidonoyl-sn-glycero-3-phosphoethanolamine +
            1-organyl-2-lyso-sn-glycero-3-phosphocholine [RN:R04720]
ALL_REAC    R04720
SUBSTRATE   1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine;
            1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine [CPD:C05209]
PRODUCT     1-organyl-2-arachidonoyl-sn-glycero-3-phosphoethanolamine;
            1-organyl-2-lyso-sn-glycero-3-phosphocholine [CPD:C04317]
COMMENT     Catalyses the transfer of arachidonate and other polyenoic fatty
            acids from intact choline or ethanolamine-containing
            glycerophospholipids to the sn-2 position of a
            lyso-glycerophospholipid. The organyl group on sn-1 of the donor or
            acceptor molecule can be alkyl, acyl or alk-1-enyl. The term 'radyl'
            has sometimes been used to refer to such substituting groups.
            Differs from EC 2.3.1.148 glycerophospholipid acyltransferase
            (CoA-dependent) in not requiring CoA and in its specificity for
            poly-unsaturated acyl groups.
REFERENCE   1  [PMID:4008481]
  AUTHORS   Robinson M, Blank ML, Snyder F.
  TITLE     Acylation of lysophospholipids by rabbit alveolar macrophages.
            Specificities of CoA-dependent and CoA-independent reactions.
  JOURNAL   J. Biol. Chem. 260 (1985) 7889-95.
  ORGANISM  rabbit
REFERENCE   2  [PMID:1641397]
  AUTHORS   Snyder F, Lee TC, Blank ML.
  TITLE     The role of transacylases in the metabolism of arachidonate and
            platelet activating factor.
  JOURNAL   Prog. Lipid. Res. 31 (1992) 65-86.
  ORGANISM  rabbit, human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.147
            ExPASy - ENZYME nomenclature database: 2.3.1.147
            ExplorEnz - The Enzyme Database: 2.3.1.147
            ERGO genome analysis and discovery system: 2.3.1.147
            BRENDA, the Enzyme Database: 2.3.1.147
            CAS: 102347-79-5
///
ENTRY       EC 2.3.1.148                Enzyme
NAME        glycerophospholipid acyltransferase (CoA-dependent)
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     1-organyl-2-acyl-sn-glycero-3-phosphocholine:1-organyl-2-lyso-sn-gly
            cero-3-phosphoethanolamine acyltransferase (CoA-dependent)
REACTION    1-organyl-2-acyl-sn-glycero-3-phosphocholine +
            1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine =
            1-organyl-2-acyl-sn-glycero-3-phosphoethanolamine +
            1-organyl-2-lyso-sn-glycero-3-phosphocholine [RN:R04721]
ALL_REAC    R04721
SUBSTRATE   1-organyl-2-acyl-sn-glycero-3-phosphocholine [CPD:C05212];
            1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine [CPD:C05209]
PRODUCT     1-organyl-2-acyl-sn-glycero-3-phosphoethanolamine [CPD:C04475];
            1-organyl-2-lyso-sn-glycero-3-phosphocholine [CPD:C04317]
COMMENT     Catalyses the transfer of fatty acids from intact choline- or
            ethanolamine-containing glycerophospholipids to the sn-2 position of
            a lyso-glycerophospholipid. The organyl group on sn-1 of the donor
            or acceptor molecule can be alkyl, acyl or alk-1-enyl. The term
            'radyl' has sometimes been used to refer to such substituting
            groups. Differs from EC 2.3.1.147 glycerophospholipid
            arachidonoyl-transferase (CoA-independent) in requiring CoA and not
            favouring the transfer of polyunsaturated acyl groups.
REFERENCE   1  [PMID:526311]
  AUTHORS   Irvine RF, Dawson RM.
  TITLE     Transfer of arachidonic acid between phospholipids in rat liver
            microsomes.
  JOURNAL   Biochem. Biophys. Res. Commun. 91 (1979) 1399-405.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4008481]
  AUTHORS   Robinson M, Blank ML, Snyder F.
  TITLE     Acylation of lysophospholipids by rabbit alveolar macrophages.
            Specificities of CoA-dependent and CoA-independent reactions.
  JOURNAL   J. Biol. Chem. 260 (1985) 7889-95.
  ORGANISM  rabbit
REFERENCE   3  [PMID:1641397]
  AUTHORS   Snyder F, Lee TC, Blank ML.
  TITLE     The role of transacylases in the metabolism of arachidonate and
            platelet activating factor.
  JOURNAL   Prog. Lipid. Res. 31 (1992) 65-86.
  ORGANISM  rabbit, human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.148
            ExPASy - ENZYME nomenclature database: 2.3.1.148
            ExplorEnz - The Enzyme Database: 2.3.1.148
            ERGO genome analysis and discovery system: 2.3.1.148
            BRENDA, the Enzyme Database: 2.3.1.148
            CAS: 9054-54-0
///
ENTRY       EC 2.3.1.149                Enzyme
NAME        platelet-activating factor acetyltransferase;
            PAF acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     1-alkyl-2-acyl-sn-glycero-3-phosphocholine:1-organyl-2-lyso-sn-glyce
            ro-3-phospholipid acetyltransferase
REACTION    1-alkyl-2-acetyl-sn-glycero-3-phosphocholine +
            1-organyl-2-lyso-sn-glycero-3-phospholipid =
            1-organyl-2-lyso-sn-glycero-3-phosphocholine +
            1-alkyl-2-acetyl-sn-glycero-3-phospholipid [RN:R04722]
ALL_REAC    R04722
SUBSTRATE   1-alkyl-2-acetyl-sn-glycero-3-phosphocholine;
            1-organyl-2-lyso-sn-glycero-3-phospholipid [CPD:C05217]
PRODUCT     1-organyl-2-lyso-sn-glycero-3-phosphocholine [CPD:C04317];
            1-alkyl-2-acetyl-sn-glycero-3-phospholipid [CPD:C05218]
COMMENT     Catalyses the transfer of the acetyl group from
            1-alkyl-2-acetyl-sn-glycero-3-phosphocholine (platelet-activating
            factor) to the sn-2 position of lyso-glycerophospholipids containing
            ethanolamine, choline, serine, inositol or phosphate groups at the
            sn-3 position as well as to sphingosine and long-chain fatty
            alcohols. The organyl group can be alkyl, acyl or alk-1-enyl
            (sometimes also collectively referred to as 'radyl').
REFERENCE   1  [PMID:1400315]
  AUTHORS   Lee TC, Uemura Y, Snyder F.
  TITLE     A novel CoA-independent transacetylase produces the ethanolamine
            plasmalogen and acyl analogs of platelet-activating factor (PAF)
            with PAF as the acetate donor in HL-60 cells.
  JOURNAL   J. Biol. Chem. 267 (1992) 19992-20001.
  ORGANISM  cow [GN:bta], human [GN:hsa], rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.149
            ExPASy - ENZYME nomenclature database: 2.3.1.149
            ExplorEnz - The Enzyme Database: 2.3.1.149
            ERGO genome analysis and discovery system: 2.3.1.149
            BRENDA, the Enzyme Database: 2.3.1.149
            CAS: 9012-30-0
///
ENTRY       EC 2.3.1.150                Enzyme
NAME        salutaridinol 7-O-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:salutaridinol 7-O-acetyltransferase
REACTION    acetyl-CoA + salutaridinol = CoA + 7-O-acetylsalutaridinol
            [RN:R04723]
ALL_REAC    R04723
SUBSTRATE   acetyl-CoA [CPD:C00024];
            salutaridinol [CPD:C05220]
PRODUCT     CoA [CPD:C00010];
            7-O-acetylsalutaridinol [CPD:C05322]
COMMENT     The enzyme is present in the poppy, Papaver somniferum. At pH 8-9
            the product, 7-O-acetylsalutaridinol, spontaneously closes the 4->5
            oxide bridge by allylic elimination to form the morphine precursor
            thebaine
REFERENCE   1
  AUTHORS   Lenz, R., Zenk, M.H.
  TITLE     Closure of the oxide bridge in morphine biosynthesis.
  JOURNAL   Tetrahedron Lett. 35 (1994) 3897-3900.
  ORGANISM  Papaver somniferum
REFERENCE   2  [PMID:8537369]
  AUTHORS   Lenz R, Zenk MH.
  TITLE     Acetyl coenzyme A:salutaridinol-7-O-acetyltransferase from papaver
            somniferum plant cell cultures. The enzyme catalyzing the formation
            of thebaine in morphine biosynthesis.
  JOURNAL   J. Biol. Chem. 270 (1995) 31091-6.
  ORGANISM  Papaver somniferum
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.150
            ExPASy - ENZYME nomenclature database: 2.3.1.150
            ExplorEnz - The Enzyme Database: 2.3.1.150
            ERGO genome analysis and discovery system: 2.3.1.150
            BRENDA, the Enzyme Database: 2.3.1.150
            CAS: 156859-13-1
///
ENTRY       EC 2.3.1.151                Enzyme
NAME        benzophenone synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     malonyl-CoA:3-hydroxybenzoyl-CoA malonyltransferase
REACTION    3 malonyl-CoA + 3-hydroxybenzoyl-CoA = 4 CoA +
            2,3',4,6-tetrahydroxybenzophenone + 3 CO2 [RN:R04709]
ALL_REAC    R04709;
            (other) R02447
SUBSTRATE   malonyl-CoA [CPD:C00083];
            3-hydroxybenzoyl-CoA [CPD:C05195]
PRODUCT     CoA [CPD:C00010];
            2,3',4,6-tetrahydroxybenzophenone [CPD:C06355];
            CO2 [CPD:C00011]
COMMENT     Involved in the biosynthesis of plant xanthomes. Benzoyl-CoA can
            replace 3-hydroxybenzoyl-CoA.
REFERENCE   1  [PMID:8925910]
  AUTHORS   Beerhues L.
  TITLE     Benzophenone synthase from cultured cells of Centaurium erythraea.
  JOURNAL   FEBS. Lett. 383 (1996) 264-6.
  ORGANISM  Centaurium erythraea
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.151
            ExPASy - ENZYME nomenclature database: 2.3.1.151
            ExplorEnz - The Enzyme Database: 2.3.1.151
            ERGO genome analysis and discovery system: 2.3.1.151
            BRENDA, the Enzyme Database: 2.3.1.151
            CAS: 175780-21-9
///
ENTRY       EC 2.3.1.152                Enzyme
NAME        alcohol O-cinnamoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     1-O-trans-cinnamoyl-beta-D-glucopyranose:alcohol
            O-cinnamoyltransferase
REACTION    1-O-trans-cinnamoyl-beta-D-glucopyranose + ROH = alkyl cinnamate +
            glucose [RN:R04411]
ALL_REAC    R04411 > R04409 R04410 R05061
SUBSTRATE   1-O-trans-cinnamoyl-beta-D-glucopyranose [CPD:C04164];
            ROH [CPD:C01335]
PRODUCT     alkyl cinnamate [CPD:C06357];
            glucose [CPD:C00293]
COMMENT     Acceptor alcohols (ROH) include methanol, ethanol and propanol. No
            cofactors are required as 1-O-trans-cinnamoyl-beta-D-glucopyranose
            itself is an "energy-rich" (activated) acyl-donor, comparable to
            CoA-thioesters. 1-O-trans-Cinnamoyl-beta-D-gentobiose can also act
            as the acyl donor, but with much less affinity.
REFERENCE   1
  AUTHORS   Mock, H.-P., Strack, D.
  TITLE     Energetics of uridine 5'-diphosphoglucose-hydroxy-cinnamic acid
            acyl-glucotransferase reaction.
  JOURNAL   Phytochemistry 32 (1993) 575-579.
  ORGANISM  Raphanus sativus
REFERENCE   2
  AUTHORS   Latza, S., Gansser, D., Berger, R.G.
  TITLE     Carbohydrate esters of cinnamic acid from fruits of Physalis
            peruviana, Psidium guajava and Vaccinium vitis IDAEA.
  JOURNAL   Phytochemistry 43 (1996) 481-485.
  ORGANISM  Physalis peruviana, Psidium guajava, Vaccinium vitis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.152
            ExPASy - ENZYME nomenclature database: 2.3.1.152
            ExplorEnz - The Enzyme Database: 2.3.1.152
            ERGO genome analysis and discovery system: 2.3.1.152
            BRENDA, the Enzyme Database: 2.3.1.152
            CAS: 74082-53-4
///
ENTRY       EC 2.3.1.153                Enzyme
NAME        anthocyanin 5-aromatic acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     hydroxycinnamoyl-CoA:anthocyanidin 3,5-diglucoside
            5-O-glucoside-6"'-O-hydroxycinnamoyltransferase
REACTION    hydroxycinnamoyl-CoA + anthocyanidin-3,5-diglucoside = CoA +
            anthocyanidin 3-glucoside-5-hydroxycinnamoylglucoside [RN:R05163]
ALL_REAC    R05163 > R07880 R07882 R07883 R07930 R07931 R07944
SUBSTRATE   hydroxycinnamoyl-CoA [CPD:C06362];
            anthocyanidin-3,5-diglucoside [CPD:C06361]
PRODUCT     CoA [CPD:C00010];
            anthocyanidin 3-glucoside-5-hydroxycinnamoylglucoside [CPD:C06363]
COMMENT     Transfers the hydroxycinnamoyl group only to the C-5 glucoside of
            anthocyanin. Malonyl-CoA cannot act as a donor.
REFERENCE   1  [PMID:9363752]
  AUTHORS   Fujiwara H, Tanaka Y, Fukui Y, Nakao M, Ashikari T, Kusumi T.
  TITLE     Anthocyanin 5-aromatic acyltransferase from Gentiana triflora.
            Purification, characterization and its role in anthocyanin
            biosynthesis.
  JOURNAL   Eur. J. Biochem. 249 (1997) 45-51.
  ORGANISM  Gentiana triflora
PATHWAY     PATH: map00942  Anthocyanin biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.153
            ExPASy - ENZYME nomenclature database: 2.3.1.153
            ExplorEnz - The Enzyme Database: 2.3.1.153
            ERGO genome analysis and discovery system: 2.3.1.153
            BRENDA, the Enzyme Database: 2.3.1.153
            CAS: 179466-49-0
///
ENTRY       EC 2.3.1.154                Enzyme
NAME        propionyl-CoA C2-trimethyltridecanoyltransferase;
            3-oxopristanoyl-CoA hydrolase;
            3-oxopristanoyl-CoA thiolase;
            peroxisome sterol carrier protein thiolase;
            sterol carrier protein;
            oxopristanoyl-CoA thiolase;
            peroxisomal 3-oxoacyl coenzyme A thiolase;
            SCPx;
            4,8,12-trimethyltridecanoyl-CoA:propanoyl-CoA
            2-C-4,8,12-trimethyltridecanoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     4,8,12-trimethyltridecanoyl-CoA:propanoyl-CoA
            C2-4,8,12-trimethyltridecanoyltransferase
REACTION    4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA =
            3-oxopristanoyl-CoA + CoA [RN:R05330]
ALL_REAC    R05330
SUBSTRATE   4,8,12-trimethyltridecanoyl-CoA [CPD:C07296];
            propanoyl-CoA [CPD:C00100]
PRODUCT     3-oxopristanoyl-CoA [CPD:C07297];
            CoA [CPD:C00010]
COMMENT     The peroxisomal protein sterol carrier protein X (SCPx) combines
            this thiolase activity with its carrier function, and is involved in
            branched chain fatty acid beta-oxidation in peroxisomes. It also
            acts on 3-oxopalmitoyl-CoA as a substrate but differs from EC
            2.3.1.16 (acetyl-CoA C-acyltransferase), which has little activity
            towards the 3-oxoacyl-CoA esters of 2-methyl-branched chain fatty
            acids such as 3-oxopristanoyl-CoA.
REFERENCE   1  [PMID:8063752]
  AUTHORS   Seedorf U, Brysch P, Engel T, Schrage K, Assmann G.
  TITLE     Sterol carrier protein X is peroxisomal 3-oxoacyl coenzyme A
            thiolase with intrinsic sterol carrier and lipid transfer activity.
  JOURNAL   J. Biol. Chem. 269 (1994) 21277-83.
  ORGANISM  rat [GN:rno], mouse [GN:mmu], human [GN:hsa]
REFERENCE   2  [PMID:9245689]
  AUTHORS   Wanders RJ, Denis S, Wouters F, Wirtz KW, Seedorf U.
  TITLE     Sterol carrier protein X (SCPx) is a peroxisomal branched-chain
            beta-ketothiolase specifically reacting with 3-oxo-pristanoyl-CoA: a
            new, unique role for SCPx in branched-chain fatty acid metabolism in
            peroxisomes.
  JOURNAL   Biochem. Biophys. Res. Commun. 236 (1997) 565-9.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.154
            ExPASy - ENZYME nomenclature database: 2.3.1.154
            ExplorEnz - The Enzyme Database: 2.3.1.154
            ERGO genome analysis and discovery system: 2.3.1.154
            BRENDA, the Enzyme Database: 2.3.1.154
///
ENTRY       EC 2.3.1.155                Enzyme
NAME        acetyl-CoA C-myristoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     myristoyl-CoA:acetyl-CoA C-myristoyltransferase
REACTION    myristoyl-CoA + acetyl-CoA = 3-oxopalmitoyl-CoA + CoA [RN:R03991]
ALL_REAC    R03991
SUBSTRATE   myristoyl-CoA [CPD:C02593];
            acetyl-CoA [CPD:C00024]
PRODUCT     3-oxopalmitoyl-CoA [CPD:C05259];
            CoA [CPD:C00010]
COMMENT     A peroxisomal enzyme involved in branched chain fatty acid
            beta-oxidation in peroxisomes. It differs from EC 2.3.1.154
            (propionyl-CoA C2-trimethyldecanoyltransferase) in not being active
            towards 3-oxopristanoyl-CoA.
REFERENCE   1  [PMID:6117552]
  AUTHORS   Miyazawa S, Furuta S, Osumi T, Hashimoto T, Ui N.
  TITLE     Properties of peroxisomal 3-ketoacyl-coA thiolase from rat liver.
  JOURNAL   J. Biochem. (Tokyo). 90 (1981) 511-9.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.155
            ExPASy - ENZYME nomenclature database: 2.3.1.155
            ExplorEnz - The Enzyme Database: 2.3.1.155
            ERGO genome analysis and discovery system: 2.3.1.155
            BRENDA, the Enzyme Database: 2.3.1.155
///
ENTRY       EC 2.3.1.156                Enzyme
NAME        phloroisovalerophenone synthase;
            valerophenone synthase;
            3-methyl-1-(trihydroxyphenyl)butan-1-one synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     isovaleryl-CoA:malonyl-CoA acyltransferase
REACTION    isovaleryl-CoA + 3 malonyl-CoA = 4 CoASH + 3 CO2 +
            3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one [RN:R05331]
ALL_REAC    R05331
SUBSTRATE   isovaleryl-CoA [CPD:C02939];
            malonyl-CoA [CPD:C00083]
PRODUCT     CoASH;
            CO2 [CPD:C00011];
            3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one [CPD:C07350]
COMMENT     Closely related to EC 2.3.1.74, naringenin-chalcone synthase. The
            product, 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one, is
            phloroisovalerophenone. Also acts on isobutyryl-CoA as substrate to
            give phlorisobutyrophenone. The products are intermediates in the
            biosynthesis of the bitter (alpha) acids in hops (Humulus lupulus).
REFERENCE   1
  AUTHORS   Fung, S.Y., Zuurbier, K.W.M., Paniego, N.B., Scheffer, J.J.C. and
            Verpoorte, R.
  TITLE     Enzymes from the biosynthesis of hop alpha and beta acids.
  JOURNAL   Proc. 26th Congr. Eur. Brew. Conv. (1997) 215-221.
  ORGANISM  Humulus lupulus
REFERENCE   2
  AUTHORS   Zuurbier, K.W.M., Leser, J., Berger, T., Hofte, A.J.P., Schroder,
            G., Verpoorte, R. and Schroder, J.
  TITLE     4-Hydroxy-2-pyrone formation by chalcone and stilbene synthase with
            nonphysiological substrates.
  JOURNAL   Phytochemistry 49 (1998) 1945-1951.
  ORGANISM  Humulus lupulus
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.156
            ExPASy - ENZYME nomenclature database: 2.3.1.156
            ExplorEnz - The Enzyme Database: 2.3.1.156
            ERGO genome analysis and discovery system: 2.3.1.156
            BRENDA, the Enzyme Database: 2.3.1.156
///
ENTRY       EC 2.3.1.157                Enzyme
NAME        glucosamine-1-phosphate N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:alpha-D-glucosamine-1-phosphate N-acetyltransferase
REACTION    acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA +
            N-acetyl-alpha-D-glucosamine 1-phosphate
ALL_REAC    (other) R05332
SUBSTRATE   acetyl-CoA [CPD:C00024];
            alpha-D-glucosamine 1-phosphate [CPD:C06156]
PRODUCT     CoA [CPD:C00010];
            N-acetyl-alpha-D-glucosamine 1-phosphate [CPD:C04501]
COMMENT     The enzyme from several bacteria (e.g., Escherichia coli, Bacillus
            subtilis and Haemophilus influenzae) has been shown to be
            bifunctional and also to possess the activity of EC 2.7.7.23,
            UDP-N-acetylglucosamine diphosphorylase.
REFERENCE   1  [PMID:8083170]
  AUTHORS   Mengin-Lecreulx D, van Heijenoort J.
  TITLE     Copurification of glucosamine-1-phosphate acetyltransferase and
            N-acetylglucosamine-1-phosphate uridyltransferase activities of
            Escherichia coli: characterization of the glmU gene product as a
            bifunctional enzyme catalyzing two subsequent steps in the pathway
            for UDP-N-acetylglucosamine synthesis.
  JOURNAL   J. Bacteriol. 176 (1994) 5788-95.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K04042  glucosamine-1-phosphate N-acetyltransferase
GENES       ECO: b3730(glmU)
            ECJ: JW3708(glmU)
            ECE: Z5228(glmU)
            ECS: ECs4672
            ECC: c4655(glmU)
            ECI: UTI89_C4282(glmU)
            ECP: ECP_3929
            ECV: APECO1_2731(glmU)
            ECW: EcE24377A_4245(glmU)
            ECX: EcHS_A3945(glmU)
            STY: STY3916(glmU)
            STT: t3657(glmU)
            SPT: SPA3701(glmU)
            SEC: SC3775(glmU)
            STM: STM3862(glmU)
            YPE: YPO4119(glmU)
            YPK: y4133(glmU)
            YPM: YP_4026(glmU)
            YPA: YPA_4164
            YPN: YPN_3976
            YPS: YPTB3965(glmU)
            SFL: SF3810(glmU)
            SFX: S3958(glmU)
            SSN: SSON_3889(glmU)
            SBO: SBO_3757(glmU)
            SDY: SDY_4018(glmU)
            PLU: plu0038(glmU)
            BUC: BU027(glmU)
            BAS: BUsg028(glmU)
            BAB: bbp029(glmU)
            WBR: WGLp010(glmU)
            SGL: SG2416
            ENT: Ent638_4135
            BFL: Bfl010(glmU)
            BPN: BPEN_010(glmU)
            HIN: HI0642(glmU)
            HIT: NTHI0762(glmU)
            HDU: HD1511(glmU)
            HSO: HS_0333(glmU)
            PMU: PM1806(glmU)
            MSU: MS1949(glmU)
            APL: APL_0588(glmU)
            XFA: XF1140
            XFT: PD0425(glmU)
            XCC: XCC0558(glmU)
            XCB: XC_3674
            XCV: XCV3762(glmU)
            XAC: XAC3644(glmU)
            XOO: XOO0736(glmU)
            XOM: XOO_0673(XOO0673)
            VCH: VC2762
            VVU: VV1_1023
            VVY: VV3249
            VPA: VP3067
            VFI: VF2562
            PPR: PBPRA3601
            PAE: PA5552(glmU)
            PAP: PSPA7_6354(glmU)
            PPU: PP_5411(glmU)
            PST: PSPTO_5597(glmU)
            PSB: Psyr_5119
            PSP: PSPPH_5205(glmU)
            PFL: PFL_6214(glmU)
            PFO: Pfl_5728
            PEN: PSEEN5540(glmU)
            PCR: Pcryo_2396
            SON: SO_4745(glmU)
            SDN: Sden_3748
            SFR: Sfri_4043
            SBL: Sbal_4364
            SHN: Shewana3_4128
            CPS: CPS_4944(glmU)
            PHA: PSHAa3006(glmU)
            PAT: Patl_3879
            MAQ: Maqu_3873
            CBU: CBU_1947(glmU)
            LPN: lpg2875(glmU)
            LPF: lpl2788(glmU)
            LPP: lpp2934(glmU)
            MCA: MCA0014(glmU)
            FTF: FTF0387(glmU)
            FTW: FTW_1687(glmU)
            FTL: FTL_0453
            FTH: FTH_0450(glmU)
            TCX: Tcr_2163
            NOC: Noc_3072
            AEH: Mlg_2867
            AHA: AHA_4260(glmU)
            RMA: Rmag_1030
            VOK: COSY_0932(glmU)
            NME: NMB0038
            NMA: NMA0284(glmU)
            NGO: NGO2053
            RSO: RSc0177(glmU)
            BXE: Bxe_A0207
            BPE: BP3730(glmU)
            BPA: BPP4229(glmU)
            BBR: BB4817(glmU)
            RFR: Rfer_1083
            POL: Bpro_0671
            PNA: Pnap_0533
            AAV: Aave_4039
            NEU: NE0208(glmU)
            NET: Neut_0279
            DAR: Daro_0220
            TBD: Tbd_2794
            HPY: HP0683(glmU)
            HPJ: jhp0624(glmU)
            HPA: HPAG1_0667
            HHE: HH0691(glmU)
            HAC: Hac_0863(glmU)
            WSU: WS2089
            TDN: Tmden_1014
            CJE: Cj0821(glmU)
            CJR: CJE0908(glmU)
            CJU: C8J_0768(glmU)
            CFF: CFF8240_0753
            CCV: CCV52592_1268(glmU)
            CHA: CHAB381_0968(glmU)
            CCO: CCC13826_0692(glmU)
            ABU: Abu_2204(glmU)
            NIS: NIS_1103(glmU)
            SUN: SUN_1836(glmU)
            GSU: GSU0271(glmU)
            GME: Gmet_0103
            PCA: Pcar_2934
            DVU: DVU2668
            DDE: Dde_0981 Dde_3640
            LIP: LI0801(glmU)
            DPS: DP1737
            WOL: WD0133(glmU)
            WBM: Wbm0088
            AMA: AM058(glmU)
            PUB: SAR11_0986(kdtB)
            MLO: mll0836
            MES: Meso_1770
            SME: SMc00232(glmU)
            ATU: Atu1787(glmU)
            ATC: AGR_C_3287
            RET: RHE_CH02090(glmU)
            RLE: RL2381
            BME: BMEII0684
            BMF: BAB2_0657
            BMS: BRA0583(glmU)
            BMB: BruAb2_0641(glmU)
            BJA: bll4608(glmU)
            RPA: RPA2659(glmU)
            RPB: RPB_2855
            RPC: RPC_2605
            RPD: RPD_2617
            RPE: RPE_2785
            NWI: Nwi_1784
            BHE: BH09930(glmU)
            BQU: BQ07650(glmU)
            CCR: CC_2304
            SIL: SPO2797(glmU)
            RSH: Rsph17029_1165
            RDE: RD1_3304(glmU)
            MMR: Mmar10_0970
            ZMO: ZMO0498(glmU)
            NAR: Saro_1199
            SAL: Sala_1370
            ELI: ELI_08815
            MAG: amb1280
            MGM: Mmc1_3456
            BSU: BG10113(gcaD)
            BHA: BH0065(gcaD)
            BAN: BA0048(gcaD)
            BAR: GBAA0048(gcaD)
            BAA: BA_0637
            BAT: BAS0048
            BCE: BC0054
            BCA: BCE_0047(gcaD)
            BCZ: BCZK0044(gcaD)
            BTK: BT9727_0044(gcaD)
            BTL: BALH_0044(gcaD)
            BLI: BL00520(gcaD)
            BLD: BLi00063(gcaD)
            BCL: ABC0078(gcaD)
            OIH: OB0058
            GKA: GK0043
            SAU: SA0457(gcaD)
            SAV: SAV0499(gcaD)
            SAM: MW0454(gcaD)
            SAR: SAR0500(gcaD)
            SAS: SAS0456
            SAC: SACOL0543(glmU)
            SAB: SAB0448(gcaD)
            SAO: SAOUHSC_00471
            SEP: SE2284
            SER: SERP0137(glmU)
            SHA: SH2512(gcaD)
            SSP: SSP2257
            LMO: lmo0198(gcaD)
            LMF: LMOf2365_0209
            LIN: lin0237(gcaD)
            LWE: lwe0167(gcaD)
            LLA: L134450(glmU)
            LLC: LACR_2079
            SPY: SPy_0443(gcaD)
            SPM: spyM18_0486(glmU)
            SPG: SpyM3_0312(glmU)
            SPS: SPs1545
            SPI: MGAS10750_Spy0364(gcaD)
            SPJ: MGAS2096_Spy0381(gcaD)
            SPF: SpyM51503(gcaD)
            SPA: M6_Spy0386
            SPN: SP_0988
            SPR: spr0891(gcaD)
            SAG: SAG1538(glmU)
            SAN: gbs1594
            SAK: SAK_1561(glmU)
            SMU: SMU.1635(glmU)
            STC: str0563(gcaD)
            STL: stu0563(gcaD)
            STE: STER_0603
            SSA: SSA_1642(glmU)
            SSU: SSU05_1584
            SSV: SSU98_1594
            LPL: lp_0467(glmU)
            LJO: LJ0208
            LAC: LBA0219
            LSA: LSA1648(glmU)
            LDB: Ldb0348(gcaD)
            LBU: LBUL_0303
            LBR: LVIS_0475
            LGA: LGAS_0211
            PPE: PEPE_0293
            EFA: EF0059(glmU)
            OOE: OEOE_1542
            STH: STH3240
            CAC: CAC3222(gcaD)
            CPE: CPE2490
            CPF: CPF_2813(glmU)
            CPR: CPR_2499(glmU)
            CTC: CTC00187
            CNO: NT01CX_1014
            CDF: CD3515(gcaD)
            CBO: CBO3545(glmU)
            CHY: CHY_0192(glmU)
            DSY: DSY0152
            SWO: Swol_0067
            TTE: TTE2572(glmU)
            MTA: Moth_0075
            MTU: Rv1018c(glmU)
            MTC: MT1046(glmU)
            MBO: Mb1046c(glmU)
            MLE: ML0249(glmU)
            MPA: MAP0984c(glmU)
            MAV: MAV_1157(glmU)
            MGI: Mflv_1944
            CGL: NCgl0906(cgl0943)
            CGB: cg1076(glmU)
            CEF: CE1016
            CDI: DIP0904
            CJK: jk1492(glmU)
            NFA: nfa48780(glmU)
            RHA: RHA1_ro05724
            SCO: SCO3122(SCE41.31)
            SMA: SAV3561(glmU)
            LXX: Lxx17430(glmU)
            ART: Arth_1217
            PAC: PPA0530
            TFU: Tfu_0414
            FRA: Francci3_3961
            FAL: FRAAL5808(coaD)
            ACE: Acel_1947
            SEN: SACE_0817(glmU)
            BLO: BL0964(glmU)
            RXY: Rxyl_0894
            SYN: sll0899(glmU)
            SYW: SYNW1003(glmU)
            SYC: syc1224_d(glmU)
            SYF: Synpcc7942_0288
            SYD: Syncc9605_1129
            SYE: Syncc9902_1328
            SYG: sync_1533
            SYR: SynRCC307_1148(glmU)
            SYX: SynWH7803_1030(glmU)
            CYA: CYA_1151(glmU)
            CYB: CYB_2635(glmU)
            TEL: tlr0393
            GVI: glr0443
            ANA: alr3921
            AVA: Ava_1776
            PMA: Pro1050(glmU)
            PMM: PMM0611(glmU)
            PMT: PMT0400(glmU)
            PMN: PMN2A_0047
            PMI: PMT9312_0611
            PMB: A9601_06671(glmU)
            PMC: P9515_06761(glmU)
            PMF: P9303_18871(glmU)
            PMG: P9301_06371(glmU)
            PMH: P9215_06931(glmU)
            CCH: Cag_1451
            DRA: DR_0808
            DGE: Dgeo_1967
            TTH: TTC0017
            TTJ: TTHA0385
            AAE: aq_607(glmU)
            TMA: TM1629
STRUCTURES  PDB: 2OI5  2OI6  2OI7  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.157
            ExPASy - ENZYME nomenclature database: 2.3.1.157
            ExplorEnz - The Enzyme Database: 2.3.1.157
            ERGO genome analysis and discovery system: 2.3.1.157
            BRENDA, the Enzyme Database: 2.3.1.157
///
ENTRY       EC 2.3.1.158                Enzyme
NAME        phospholipid:diacylglycerol acyltransferase;
            PDAT
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     phospholipid:1,2-diacyl-sn-glycerol O-acyltransferase
REACTION    phospholipid + 1,2-diacylglycerol = lysophospholipid +
            triacylglycerol [RN:R05333]
ALL_REAC    R05333
SUBSTRATE   phospholipid [CPD:C00865];
            1,2-diacylglycerol [CPD:C00641]
PRODUCT     lysophospholipid [CPD:C06254];
            triacylglycerol [CPD:C00422]
COMMENT     This enzyme differs from EC 2.3.1.20, diacylglycerol
            O-acyltransferase, by synthesising triacylglycerol using an
            acyl-CoA-independent mechanism. The specificity of the enzyme for
            the acyl group in the phospholipid varies with species, e.g., the
            enzyme from castor bean (Ricinus communis) preferentially
            incorporates vernoloyl (12,13-epoxyoctadec-9-enoyl) groups into
            triacylglycerol, whereas that from the hawk's beard (Crepis
            palaestina) incorporates both ricinoleoyl
            (12-hydroxyoctadec-9-enoyl) and vernoloyl groups. The enzyme from
            the yeast Saccharomyces cerevisiae specifically transfers acyl
            groups from the sn-2 position of the phospholipid to diacylglycerol,
            thus forming an sn-1-lysophospholipid.
REFERENCE   1  [PMID:10829075]
  AUTHORS   Dahlqvist A, Stahl U, Lenman M, Banas A, Lee M, Sandager L, Ronne H,
            Stymne S.
  TITLE     Phospholipid:diacylglycerol acyltransferase: an enzyme that
            catalyzes the acyl-CoA-independent formation of triacylglycerol in
            yeast and plants.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 6487-92.
  ORGANISM  Crepis palaestina
PATHWAY     PATH: map00561  Glycerolipid metabolism
ORTHOLOGY   KO: K00679  phospholipid:diacylglycerol acyltransferase
GENES       SCE: YNR008W(LRO1)
            AGO: AGOS_AFL179C
            PIC: PICST_72946(LRO1)
            CGR: CAGL0I05786g
            SPO: SPBC776.14
            ANI: AN4992.2
            AFM: AFUA_3G09950
            AOR: AO090003000514
            CNE: CNL04710
            TBR: Tb11.01.4790
            TCR: 506757.10 510359.340
            LMA: LmjF09.1040
            EHI: 40.t00043 57.t00020
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.158
            ExPASy - ENZYME nomenclature database: 2.3.1.158
            ExplorEnz - The Enzyme Database: 2.3.1.158
            ERGO genome analysis and discovery system: 2.3.1.158
            BRENDA, the Enzyme Database: 2.3.1.158
///
ENTRY       EC 2.3.1.159                Enzyme
NAME        acridone synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     malonyl-CoA:N-methylanthraniloyl-CoA malonyltransferase (cyclizing)
REACTION    3 malonyl-CoA + N-methylanthraniloyl-CoA = 4 CoA +
            1,3-dihydroxy-N-methylacridone + 3 CO2 [RN:R07250]
ALL_REAC    R07250
SUBSTRATE   malonyl-CoA [CPD:C00083];
            N-methylanthraniloyl-CoA [CPD:C12092]
PRODUCT     CoA [CPD:C00010];
            1,3-dihydroxy-N-methylacridone [CPD:C12093];
            CO2 [CPD:C00011]
COMMENT     Belongs to a superfamily of plant polyketide synthases. Has many
            similarities to chalcone and stilbene synthases (see reaction
            synthesis)
REFERENCE   1  [PMID:8148006]
  AUTHORS   Baumert A, Maier W, Groger D, Deutzmann R.
  TITLE     Purification and properties of acridone synthase from cell
            suspension cultures of Ruta graveolens L.
  JOURNAL   Z. Naturforsch. [C]. 49 (1994) 26-32.
  ORGANISM  Ruta graveolens
REFERENCE   2
  AUTHORS   Maier, W., Baumert, A., Schumann, B., Furukawa, H. and Groger, D.
  TITLE     Synthesis of 1,3-dihydroxy-N-methylacridone and its conversion to
            rutacridone by cell-free extracts of Ruta-graveolens cell cultures.
  JOURNAL   Phytochemistry 32 (1993) 691-698.
  ORGANISM  Ruta graveolens
REFERENCE   3  [PMID:10217426]
  AUTHORS   Lukacin R, Springob K, Urbanke C, Ernwein C, Schroder G, Schroder J,
            Matern U.
  TITLE     Native acridone synthases I and II from Ruta graveolens L. form
            homodimers.
  JOURNAL   FEBS. Lett. 448 (1999) 135-40.
  ORGANISM  Ruta graveolens
REFERENCE   4  [PMID:9747538]
  AUTHORS   Junghanns KT, Kneusel RE, Groger D, Matern U.
  TITLE     Differential regulation and distribution of acridone synthase in
            Ruta graveolens.
  JOURNAL   Phytochemistry. 49 (1998) 403-11.
  ORGANISM  Ruta graveolens
PATHWAY     PATH: map01058  Acridone alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.159
            ExPASy - ENZYME nomenclature database: 2.3.1.159
            ExplorEnz - The Enzyme Database: 2.3.1.159
            ERGO genome analysis and discovery system: 2.3.1.159
            BRENDA, the Enzyme Database: 2.3.1.159
            CAS: 99085-53-7
///
ENTRY       EC 2.3.1.160                Enzyme
NAME        vinorine synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:16-epivellosimine O-acetyltransferase (cyclizing)
REACTION    acetyl-CoA + 16-epivellosimine = CoA + vinorine [RN:R05876]
ALL_REAC    R05876
SUBSTRATE   acetyl-CoA [CPD:C00024];
            16-epivellosimine [CPD:C11633]
PRODUCT     CoA [CPD:C00010];
            vinorine [CPD:C11807]
COMMENT     The reaction proceeds in two stages. The indole nitrogen of
            16-epivellosimine interacts with its aldehyde group giving an
            hydroxy-substituted new ring. This alcohol is then acetylated. Also
            acts on gardneral (11-methoxy-16-epivellosimine). Generates the
            ajmalan skeleton, which forms part of the route to ajmaline.
REFERENCE   1
  AUTHORS   Pfitzner, A., Polz, L. and Stockligt, J.
  TITLE     Properties of vinorine synthase the Rauwolfia enzyme involved in the
            formation of the ajmaline skeleton.
  JOURNAL   Z. Naturforsch. C: Biosci. 41 (1986) 103-114.
  ORGANISM  Rauwolfia serpentina
REFERENCE   2  [PMID:15110860]
  AUTHORS   Bayer A, Ma X, Stockigt J.
  TITLE     Acetyltransfer in natural product biosynthesis--functional cloning
            and molecular analysis of vinorine synthase.
  JOURNAL   Bioorg. Med. Chem. 12 (2004) 2787-95.
REFERENCE   3  [PMID:15450182]
  AUTHORS   Ma X, Koepke J, Bayer A, Linhard V, Fritzsch G, Zhang B, Michel H,
            Stockigt J.
  TITLE     Vinorine synthase from Rauvolfia: the first example of
            crystallization and preliminary X-ray diffraction analysis of an
            enzyme of the BAHD superfamily.
  JOURNAL   Biochim. Biophys. Acta. 1701 (2004) 129-32.
REFERENCE   4  [PMID:15665331]
  AUTHORS   Ma X, Koepke J, Panjikar S, Fritzsch G, Stockigt J.
  TITLE     Crystal structure of vinorine synthase, the first representative of
            the BAHD superfamily.
  JOURNAL   J. Biol. Chem. 280 (2005) 13576-83.
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
STRUCTURES  PDB: 2BGH  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.160
            ExPASy - ENZYME nomenclature database: 2.3.1.160
            ExplorEnz - The Enzyme Database: 2.3.1.160
            ERGO genome analysis and discovery system: 2.3.1.160
            BRENDA, the Enzyme Database: 2.3.1.160
            CAS: 88844-97-7
///
ENTRY       EC 2.3.1.161                Enzyme
NAME        lovastatin nonaketide synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl-
            and enoyl-reducing, thioester-hydrolysing)
REACTION    acetyl-CoA + 8 malonyl-CoA + 11 NADPH + 10 H+ +
            S-adenosyl-L-methionine = dihydromonacolin L + 9 CoA + 8 CO2 + 11
            NADP+ + S-adenosyl-L-homocysteine + 6 H2O [RN:R07251]
ALL_REAC    R07251
SUBSTRATE   acetyl-CoA [CPD:C00024];
            malonyl-CoA [CPD:C00083];
            NADPH [CPD:C00005];
            H+ [CPD:C00080];
            S-adenosyl-L-methionine [CPD:C00019]
PRODUCT     dihydromonacolin L [CPD:C15536];
            CoA [CPD:C00010];
            CO2 [CPD:C00011];
            NADP+ [CPD:C00006];
            S-adenosyl-L-homocysteine [CPD:C00021];
            H2O [CPD:C00001]
COMMENT     The microbial enzyme is a multi-functional protein catalysing many
            of the chain building reactions of EC 2.3.1.85, fatty-acid synthase,
            as well as a reductive methylation and a Diels-Alder reaction.
REFERENCE   1
  AUTHORS   Auclair, K., Sutherland, A., Kennedy, J., Witter, D.J., van der
            Heever, J.P., Hutchinson, C.R. and Vederas, J.C.
  TITLE     Lovastatin nonaketide synthase catalyses an intramolecular
            Diels-Alder reaction of a substrate analogue.
  JOURNAL   J. Am. Chem. Soc. 122 (2000) 11519-11520.
  ORGANISM  Aspergillus terreus
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.161
            ExPASy - ENZYME nomenclature database: 2.3.1.161
            ExplorEnz - The Enzyme Database: 2.3.1.161
            ERGO genome analysis and discovery system: 2.3.1.161
            BRENDA, the Enzyme Database: 2.3.1.161
            CAS: 235426-97-8
///
ENTRY       EC 2.3.1.162                Enzyme
NAME        taxadien-5alpha-ol O-acetyltransferase;
            acetyl coenzyme A:taxa-4(20),11(12)-dien-5alpha-ol O-acetyl
            transferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:taxa-4(20),11-dien-5alpha-ol O-acetyltransferase
REACTION    acetyl-CoA + taxa-4(20),11-dien-5alpha-ol = CoA +
            taxa-4(20),11-dien-5alpha-yl acetate [RN:R06307]
ALL_REAC    R06307
SUBSTRATE   acetyl-CoA [CPD:C00024];
            taxa-4(20),11-dien-5alpha-ol
PRODUCT     CoA [CPD:C00010];
            taxa-4(20),11-dien-5alpha-yl acetate
REFERENCE   1  [PMID:10190984]
  AUTHORS   Walker K, Ketchum RE, Hezari M, Gatfield D, Goleniowski M, Barthol
            A, Croteau R.
  TITLE     Partial purification and characterization of acetyl coenzyme A:
            taxa-4(20),11(12)-dien-5alpha-ol O-acetyl transferase that catalyzes
            the first acylation step of taxol biosynthesis.
  JOURNAL   Arch. Biochem. Biophys. 364 (1999) 273-9.
  ORGANISM  Taxus canadensis, Taxus cuspidata
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.162
            ExPASy - ENZYME nomenclature database: 2.3.1.162
            ExplorEnz - The Enzyme Database: 2.3.1.162
            ERGO genome analysis and discovery system: 2.3.1.162
            BRENDA, the Enzyme Database: 2.3.1.162
            CAS: 229032-29-5
///
ENTRY       EC 2.3.1.163                Enzyme
NAME        10-hydroxytaxane O-acetyltransferase;
            acetyl coenzyme A: 10-hydroxytaxane O-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:taxan-10beta-ol O-acetyltransferase
REACTION    acetyl-CoA + 10-desacetyltaxuyunnanin C = CoA + taxuyunnanin C
            [RN:R07252]
ALL_REAC    R07252
SUBSTRATE   acetyl-CoA [CPD:C00024];
            10-desacetyltaxuyunnanin C [CPD:C15538]
PRODUCT     CoA [CPD:C00010];
            taxuyunnanin C [CPD:C15537]
COMMENT     Acts on a number of related taxane diterpenoids with a free
            10beta-hydroxy group. May be identical to EC 2.3.1.167,
            10-deacetylbaccatin III 10-O-acetyltransferase.
REFERENCE   1  [PMID:10192963]
  AUTHORS   Menhard B, Zenk MH.
  TITLE     Purification and characterization of acetyl coenzyme A:
            10-hydroxytaxane O-acetyltransferase from cell suspension cultures
            of Taxus chinensis.
  JOURNAL   Phytochemistry. 50 (1999) 763-74.
  ORGANISM  Taxus chinensis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.163
            ExPASy - ENZYME nomenclature database: 2.3.1.163
            ExplorEnz - The Enzyme Database: 2.3.1.163
            ERGO genome analysis and discovery system: 2.3.1.163
            BRENDA, the Enzyme Database: 2.3.1.163
            CAS: 227465-96-5
///
ENTRY       EC 2.3.1.164                Enzyme
NAME        isopenicillin-N N-acyltransferase;
            acyl-coenzyme A:isopenicillin N acyltransferase;
            isopenicillin N:acyl-CoA: acyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:isopenicillin N N-acyltransferase
REACTION    phenylacetyl-CoA + isopenicillin N + H2O = CoA + penicillin G +
            L-2-aminohexanedioate [RN:R04868]
ALL_REAC    R04868;
            (other) R06361
SUBSTRATE   phenylacetyl-CoA [CPD:C00582];
            isopenicillin N [CPD:C05557];
            H2O [CPD:C00001]
PRODUCT     CoA [CPD:C00010];
            penicillin G [CPD:C05551];
            L-2-aminohexanedioate [CPD:C00956]
COMMENT     Proceeds by a two stage mechanism via 6-aminopenicillanic acid.
            Different from EC 3.5.1.11, penicillin amidase.
REFERENCE   1  [PMID:2120195]
  AUTHORS   Tobin MB, Fleming MD, Skatrud PL, Miller JR.
  TITLE     Molecular characterization of the acyl-coenzyme A:isopenicillin N
            acyltransferase gene (penDE) from Penicillium chrysogenum and
            Aspergillus nidulans and activity of recombinant enzyme in
            Escherichia coli.
  JOURNAL   J. Bacteriol. 172 (1990) 5908-14.
  ORGANISM  Penicillium chrysogenum, Aspergillus nidulans [GN:ani]
REFERENCE   2  [PMID:8396910]
  AUTHORS   Aplin RT, Baldwin JE, Roach PL, Robinson CV, Schofield CJ.
  TITLE     Investigations into the post-translational modification and
            mechanism of isopenicillin N:acyl-CoA acyltransferase using
            electrospray mass spectrometry.
  JOURNAL   Biochem. J. 294 ( Pt 2) (1993) 357-63.
  ORGANISM  Penicillium chrysogenum
PATHWAY     PATH: map00311  Penicillin and cephalosporin biosynthesis
GENES       BUR: Bcep18194_B2777
            SEN: SACE_5325
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.164
            ExPASy - ENZYME nomenclature database: 2.3.1.164
            ExplorEnz - The Enzyme Database: 2.3.1.164
            ERGO genome analysis and discovery system: 2.3.1.164
            BRENDA, the Enzyme Database: 2.3.1.164
            CAS: 54576-90-8
///
ENTRY       EC 2.3.1.165                Enzyme
NAME        6-methylsalicylic-acid synthase;
            MSAS;
            6-methylsalicylic acid synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating,
            oxoacyl-reducing, thioester-hydrolysing and cyclizing)
REACTION    acetyl-CoA + 3 malonyl-CoA + NADPH + H+ = 6-methylsalicylate + 4 CoA
            + 3 CO2 + NADP+ + H2O [RN:R07253]
ALL_REAC    R07253
SUBSTRATE   acetyl-CoA [CPD:C00024];
            malonyl-CoA [CPD:C00083];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
PRODUCT     6-methylsalicylate [CPD:C02657];
            CoA [CPD:C00010];
            CO2 [CPD:C00011];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     A multienzyme complex with a 4'-phosphopantetheine prosthetic group
            on the acyl carrier protein. It has a similar sequence to vertebrate
            type I fatty acid synthase. Acetoacetyl-CoA can also act as a
            starter molecule.
REFERENCE   1  [PMID:1471999]
  AUTHORS   Spencer JB, Jordan PM.
  TITLE     Purification and properties of 6-methylsalicylic acid synthase from
            Penicillium patulum.
  JOURNAL   Biochem. J. 288 ( Pt 3) (1992) 839-46.
  ORGANISM  Penicillium patulum
REFERENCE   2  [PMID:8823160]
  AUTHORS   Child CJ, Spencer JB, Bhogal P, Shoolingin-Jordan PM.
  TITLE     Structural similarities between 6-methylsalicylic acid synthase from
            Penicillium patulum and vertebrate type I fatty acid synthase:
            evidence from thiol modification studies.
  JOURNAL   Biochemistry. 35 (1996) 12267-74.
  ORGANISM  Penicillium patulum
REFERENCE   3  [PMID:10935930]
  AUTHORS   Richardson MT, Pohl NL, Kealey JT, Khosla C.
  TITLE     Tolerance and specificity of recombinant 6-methylsalicyclic acid
            synthase.
  JOURNAL   Metab. Eng. 1 (1999) 180-7.
  ORGANISM  Penicillium patulum
GENES       FAL: FRAAL0348 FRAAL0349
            AVA: Ava_3986
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.165
            ExPASy - ENZYME nomenclature database: 2.3.1.165
            ExplorEnz - The Enzyme Database: 2.3.1.165
            ERGO genome analysis and discovery system: 2.3.1.165
            BRENDA, the Enzyme Database: 2.3.1.165
            CAS: 9045-37-8
///
ENTRY       EC 2.3.1.166                Enzyme
NAME        2alpha-hydroxytaxane 2-O-benzoyltransferase;
            benzoyl-CoA:taxane 2alpha-O-benzoyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     benzoyl-CoA:taxan-2alpha-ol O-benzoyltransferase
REACTION    benzoyl-CoA + 10-deacetyl-2-debenzoylbaccatin III = CoA +
            10-deacetylbaccatin III [RN:R06310]
ALL_REAC    R06310
SUBSTRATE   benzoyl-CoA [CPD:C00512];
            10-deacetyl-2-debenzoylbaccatin III [CPD:C11899]
PRODUCT     CoA [CPD:C00010];
            10-deacetylbaccatin III [CPD:C11700]
COMMENT     The enzyme was studied using the semisynthetic substrate
            2-debenzoyl-7,13-diacetylbaccatin III. It will not acylate the
            hydroxy group at 1beta, 7beta, 10beta or 13alpha of 10-deacetyl
            baccatin III, or at 2alpha or 5alpha of
            taxa-4(20),11-diene-2alpha,5alpha-diol.
REFERENCE   1  [PMID:11095755]
  AUTHORS   Walker K, Croteau R.
  TITLE     Taxol biosynthesis: molecular cloning of a benzoyl-CoA:taxane
            2alpha-O-benzoyltransferase cDNA from taxus and functional
            expression in Escherichia coli.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 13591-6.
  ORGANISM  Taxus cuspidata
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.166
            ExPASy - ENZYME nomenclature database: 2.3.1.166
            ExplorEnz - The Enzyme Database: 2.3.1.166
            ERGO genome analysis and discovery system: 2.3.1.166
            BRENDA, the Enzyme Database: 2.3.1.166
            CAS: 329318-50-5
///
ENTRY       EC 2.3.1.167                Enzyme
NAME        10-deacetylbaccatin III 10-O-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:taxan-10beta-ol O-acetyltransferase
REACTION    acetyl-CoA + 10-deacetylbaccatin III = CoA + baccatin III
            [RN:R06311]
ALL_REAC    R06311
SUBSTRATE   acetyl-CoA [CPD:C00024];
            10-deacetylbaccatin III [CPD:C11700]
PRODUCT     CoA [CPD:C00010];
            baccatin III [CPD:C11900]
COMMENT     The enzyme will not acylate the hydroxy group at 1beta, 7beta or
            13alpha of 10-deacetyl baccatin III, or at 5alpha of
            taxa-4(20),11-dien-5alpha-ol. May be identical to EC 2.3.1.163,
            10-hydroxytaxane O-acetyltransferase.
REFERENCE   1  [PMID:10639122]
  AUTHORS   Walker K, Croteau R.
  TITLE     Molecular cloning of a 10-deacetylbaccatin III-10-O-acetyl
            transferase cDNA from Taxus and functional expression in Escherichia
            coli.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 583-7.
  ORGANISM  Taxus cuspidata
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.167
            ExPASy - ENZYME nomenclature database: 2.3.1.167
            ExplorEnz - The Enzyme Database: 2.3.1.167
            ERGO genome analysis and discovery system: 2.3.1.167
            BRENDA, the Enzyme Database: 2.3.1.167
            CAS: 220946-63-4
///
ENTRY       EC 2.3.1.168                Enzyme
NAME        dihydrolipoyllysine-residue (2-methylpropanoyl)transferase;
            dihydrolipoyl transacylase;
            enzyme-dihydrolipoyllysine:2-methylpropanoyl-CoA
            S-(2-methylpropanoyl)transferase;
            2-methylpropanoyl-CoA:enzyme-6-N-(dihydrolipoyl)lysine
            S-(2-methylpropanoyl)transferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     2-methylpropanoyl-CoA:enzyme-N6-(dihydrolipoyl)lysine
            S-(2-methylpropanoyl)transferase
REACTION    2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA +
            enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine [RN:R02662]
ALL_REAC    R02662;
            (other) R03174 R04097
SUBSTRATE   2-methylpropanoyl-CoA [CPD:C00630];
            enzyme N6-(dihydrolipoyl)lysine [CPD:C15973]
PRODUCT     CoA [CPD:C00010];
            enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
COMMENT     A multimer (24-mer) of this enzyme forms the core of the multienzyme
            3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly
            both EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase
            (2-methylpropanoyl-transferring) and EC 1.8.1.4, dihydrolipoyl
            dehydrogenase. The lipoyl group of this enzyme is reductively
            2-methylpropanoylated by EC 1.2.4.4, and the only observed direction
            catalysed by EC 2.3.1.168 is that where this 2-methylpropanoyl is
            passed to coenzyme A. In addition to the 2-methylpropanoyl group,
            formed when EC 1.2.4.4 acts on the oxoacid that corresponds with
            valine, this enzyme also transfers the 3-methylbutanoyl and
            S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the
            oxo acids corresponding with leucine and isoleucine.
REFERENCE   1  [PMID:773366]
  AUTHORS   Massey LK, Sokatch JR, Conrad RS.
  TITLE     Branched-chain amino acid catabolism in bacteria.
  JOURNAL   Bacteriol. Rev. 40 (1976) 42-54.
REFERENCE   2  [PMID:6746648]
  AUTHORS   Chuang DT, Hu CC, Ku LS, Niu WL, Myers DE, Cox RP.
  TITLE     Catalytic and structural properties of the dihydrolipoyl
            transacylase component of bovine branched-chain alpha-keto acid
            dehydrogenase.
  JOURNAL   J. Biol. Chem. 259 (1984) 9277-84.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:7913832]
  AUTHORS   Wynn RM, Davie JR, Zhi W, Cox RP, Chuang DT.
  TITLE     In vitro reconstitution of the 24-meric E2 inner core of bovine
            mitochondrial branched-chain alpha-keto acid dehydrogenase complex:
            requirement for chaperonins GroEL and GroES.
  JOURNAL   Biochemistry. 33 (1994) 8962-8.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:10966480]
  AUTHORS   Perham RN.
  TITLE     Swinging arms and swinging domains in multifunctional enzymes:
            catalytic machines for multistep reactions.
  JOURNAL   Annu. Rev. Biochem. 69 (2000) 961-1004.
  ORGANISM  Escherichia coli [GN:eco], Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
ORTHOLOGY   KO: K09699  dihydrolipoyllysine-residue
                        (2-methylpropanoyl)transferase
GENES       HSA: 1629(DBT)
            PTR: 457056(DBT)
            MMU: 13171(Dbt)
            RNO: 29611(Dbt)
            CFA: 479929(DBT)
            BTA: 280759(DBT)
            GGA: 395374(DBT)
            XLA: 447616(MGC85493)
            XTR: 549717(dbt)
            SPU: 582235(LOC582235)
            ANI: AN3639.2
            AFM: AFUA_1G00490
            AOR: AO090003001008
            TET: TTHERM_00794540
            PFL: PFL_2532
            PEN: PSEEN3855(bkdB)
            SBM: Shew185_2151
            SSE: Ssed_2327
            SPL: Spea_2244
            PHA: PSHAa1630(dbt)
            NOC: Noc_1433
            REH: H16_B2235(bkdB)
            BUR: Bcep18194_A4362
            BAM: Bamb_1125
            BCY: Bcer98_2672
            BCL: ABC2449(bkdB)
            BPU: BPUM_2142(bfmBB)
            SAO: SAOUHSC_01611
            FPS: FP0590(bfmBB)
STRUCTURES  PDB: 1ZWV  2COO  2IHW  2II3  2II4  2II5  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.168
            ExPASy - ENZYME nomenclature database: 2.3.1.168
            ExplorEnz - The Enzyme Database: 2.3.1.168
            ERGO genome analysis and discovery system: 2.3.1.168
            BRENDA, the Enzyme Database: 2.3.1.168
///
ENTRY       EC 2.3.1.169                Enzyme
NAME        CO-methylating acetyl-CoA synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:corrinoid protein O-acetyltransferase
REACTION    acetyl-CoA + corrinoid protein = CO + methylcorrinoid protein + CoA
SUBSTRATE   acetyl-CoA [CPD:C00024];
            corrinoid protein
PRODUCT     CO [CPD:C00237];
            methylcorrinoid protein;
            CoA [CPD:C00010]
COMMENT     Contains nickel, copper and iron-sulfur clusters. Also catalyses
            exchange reactions of carbon between C-1 of acetyl-CoA and CO, and
            between C-2 of acetyl-CoA and methyl corrinoid protein. Involved,
            together with EC 1.2.7.4, carbon-monoxide dehydrogenase
            (ferredoxin), in the synthesis of acetyl-CoA from CO2 and H2. To
            follow its stoichiometry, the reaction can be written
            as:CH3-CO-S-CoA + protein Co+ + H+ = CO + protein Co2+-CH3 + HS-CoA.
REFERENCE   1  [PMID:2984190]
  AUTHORS   Ragsdale SW, Wood HG.
  TITLE     Acetate biosynthesis by acetogenic bacteria. Evidence that carbon
            monoxide dehydrogenase is the condensing enzyme that catalyzes the
            final steps of the synthesis.
  JOURNAL   J. Biol. Chem. 260 (1985) 3970-7.
  ORGANISM  Clostridium thermoaceticum
REFERENCE   2  [PMID:12386327]
  AUTHORS   Doukov TI, Iverson TM, Seravalli J, Ragsdale SW, Drennan CL.
  TITLE     A Ni-Fe-Cu center in a bifunctional carbon monoxide
            dehydrogenase/acetyl-CoA synthase.
  JOURNAL   Science. 298 (2002) 567-72.
  ORGANISM  Clostridium thermoaceticum
GENES       AMT: Amet_2028
            DEB: DehaBAV1_0635
            MMQ: MmarC5_0803
            MMZ: MmarC7_0225
            MAE: Maeo_1171
            MVN: Mevan_0309
            MBU: Mbur_0860
            MTP: Mthe_0290
            MHU: Mhun_0688
            MBN: Mboo_1196 Mboo_1371
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.169
            ExPASy - ENZYME nomenclature database: 2.3.1.169
            ExplorEnz - The Enzyme Database: 2.3.1.169
            ERGO genome analysis and discovery system: 2.3.1.169
            BRENDA, the Enzyme Database: 2.3.1.169
///
ENTRY       EC 2.3.1.170                Enzyme
NAME        6'-deoxychalcone synthase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     malonyl-CoA:4-coumaroyl-CoA malonyltransferase (cyclizing, reducing)
REACTION    3 malonyl-CoA + 4-coumaroyl-CoA + NADPH + H+ = 4 CoA +
            isoliquiritigenin + 3 CO2 + NADP+ + H2O [RN:R07254]
ALL_REAC    R07254
SUBSTRATE   malonyl-CoA [CPD:C00083];
            4-coumaroyl-CoA [CPD:C00223];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
PRODUCT     CoA [CPD:C00010];
            isoliquiritigenin [CPD:C08650];
            CO2 [CPD:C00011];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
COMMENT     Isoliquiritigenin is the precursor of liquiritigenin, a
            5-deoxyflavanone.
REFERENCE   1  [PMID:3355160]
  AUTHORS   Ayabe S, Udagawa A, Furuya T.
  TITLE     NAD(P)H-dependent 6'-deoxychalcone synthase activity in Glycyrrhiza
            echinata cells induced by yeast extract.
  JOURNAL   Arch. Biochem. Biophys. 261 (1988) 458-62.
  ORGANISM  Glycyrrhiza echinata
ORTHOLOGY   KO: K08243  6'-deoxychalcone synthase
GENES       ATH: AT1G59950 AT1G59960
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.170
            ExPASy - ENZYME nomenclature database: 2.3.1.170
            ExplorEnz - The Enzyme Database: 2.3.1.170
            ERGO genome analysis and discovery system: 2.3.1.170
            BRENDA, the Enzyme Database: 2.3.1.170
            CAS: 114308-23-5
///
ENTRY       EC 2.3.1.171                Enzyme
NAME        anthocyanin 6"-O-malonyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     malonyl-CoA:anthocyanidin-3-O-beta-D-glucoside
            6"-O-malonyltransferase
REACTION    malonyl-CoA + an anthocyanidin 3-O-beta-D-glucoside = CoA + an
            anthocyanidin 3-O-(6-O-malonyl-beta-D-glucoside) [RN:R07255]
ALL_REAC    R07255 > R06801 R06817 R07938
SUBSTRATE   malonyl-CoA [CPD:C00083];
            anthocyanidin 3-O-beta-D-glucoside [CPD:C15539]
PRODUCT     CoA [CPD:C00010];
            anthocyanidin 3-O-(6-O-malonyl-beta-D-glucoside) [CPD:C15540]
COMMENT     Acts on pelargonidin 3-O-glucoside in dahlia (Dahlia variabilis),
            delphinidin 3-O-glucoside, and on cyanidin 3-O-glucoside in
            transgenic petunia (Petunia hybrida).
REFERENCE   1  [PMID:12481098]
  AUTHORS   Suzuki H, Nakayama T, Yonekura-Sakakibara K, Fukui Y, Nakamura N,
            Yamaguchi MA, Tanaka Y, Kusumi T, Nishino T.
  TITLE     cDNA cloning, heterologous expressions, and functional
            characterization of malonyl-coenzyme a:anthocyanidin
            3-o-glucoside-6&quot;-o-malonyltransferase from dahlia flowers.
  JOURNAL   Plant. Physiol. 130 (2002) 2142-51.
  ORGANISM  Dahlia variabilis
PATHWAY     PATH: map00942  Anthocyanin biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.171
            ExPASy - ENZYME nomenclature database: 2.3.1.171
            ExplorEnz - The Enzyme Database: 2.3.1.171
            ERGO genome analysis and discovery system: 2.3.1.171
            BRENDA, the Enzyme Database: 2.3.1.171
///
ENTRY       EC 2.3.1.172                Enzyme
NAME        anthocyanin 5-O-glucoside 6'''-O-malonyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     malonyl-CoA:pelargonidin-3-O-(6-caffeoyl-beta-D-glucoside)-5-O-beta-
            D-glucoside 6'''-O-malonyltransferase
REACTION    malonyl-CoA + pelargonidin 3-O-(6-caffeoyl-beta-D-glucoside)
            5-O-beta-D-glucoside = CoA + 4'''-demalonylsalvianin [RN:R06799]
ALL_REAC    R06799;
            (other) R07910
SUBSTRATE   malonyl-CoA [CPD:C00083];
            pelargonidin 3-O-(6-caffeoyl-beta-D-glucoside) 5-O-beta-D-glucoside
            [CPD:C12640]
PRODUCT     CoA [CPD:C00010];
            4'''-demalonylsalvianin [CPD:C12641]
COMMENT     Specific for the penultimate step in salvianin biosynthesis. The
            enzyme also catalyses the malonylation of shisonin to
            malonylshisonin [cyanidin
            3-O-(6"-O-p-coumaryl-beta-D-glucoside)-5-(6'''-O-malonyl-beta-D-gluc
            oside)]. The compounds 4'''-demalonylsalvianin, salvianin,
            pelargonidin 3,5-diglucoside and delphinidin 3,5-diglucoside cannot
            act as substrates.
REFERENCE   1  [PMID:11598135]
  AUTHORS   Suzuki H, Nakayama T, Yonekura-Sakakibara K, Fukui Y, Nakamura N,
            Nakao M, Tanaka Y, Yamaguchi MA, Kusumi T, Nishino T.
  TITLE     Malonyl-CoA:anthocyanin 5-O-glucoside-6&quot;'-O-malonyltransferase
            from scarlet sage (Salvia splendens) flowers. Enzyme purification,
            gene cloning, expression, and characterization.
  JOURNAL   J. Biol. Chem. 276 (2001) 49013-9.
  ORGANISM  Salvia splendens
PATHWAY     PATH: map00942  Anthocyanin biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.172
            ExPASy - ENZYME nomenclature database: 2.3.1.172
            ExplorEnz - The Enzyme Database: 2.3.1.172
            ERGO genome analysis and discovery system: 2.3.1.172
            BRENDA, the Enzyme Database: 2.3.1.172
///
ENTRY       EC 2.3.1.173                Enzyme
NAME        flavonol-3-O-triglucoside O-coumaroyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     4-coumaroyl-CoA:flavonol-3-O-[beta-D-glucosyl-(1->2)-beta-D-glucosid
            e] 6'''-O-4-coumaroyltransferase
REACTION    4-coumaroyl-CoA + a flavonol
            3-O-[beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-beta-D-glucoside]
            = CoA + a flavonol
            3-O-[6-(4-coumaroyl)-beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-
            beta-D-glucoside]
ALL_REAC    (other) R06806
SUBSTRATE   4-coumaroyl-CoA [CPD:C00223];
            flavonol
            3-O-beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-beta-D-glucoside
            [CPD:C15582]
PRODUCT     CoA [CPD:C00010];
            flavonol
            3-O-[6-(4-coumaroyl)-beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-
            beta-D-glucoside]
COMMENT     Acylates kaempferol 3-O-triglucoside on the terminal glucosyl unit,
            almost certainly at C-6.
REFERENCE   1  [PMID:145116]
  AUTHORS   Saylor MH, Mansell RL.
  TITLE     Hydroxycinnamoyl: coenzyme A transferase involved in the
            biosynthesis of kaempferol-3-(p-coumaroyl triglucoside) in Pisum
            sativum.
  JOURNAL   Z. Naturforsch. [C]. 32 (1977) 764-8.
  ORGANISM  Pisum sativum
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.173
            ExPASy - ENZYME nomenclature database: 2.3.1.173
            ExplorEnz - The Enzyme Database: 2.3.1.173
            ERGO genome analysis and discovery system: 2.3.1.173
            BRENDA, the Enzyme Database: 2.3.1.173
///
ENTRY       EC 2.3.1.174                Enzyme
NAME        3-oxoadipyl-CoA thiolase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     succinyl-CoA:acetyl-CoA C-succinyltransferase
REACTION    succinyl-CoA + acetyl-CoA = CoA + 3-oxoadipyl-CoA [RN:R00829]
ALL_REAC    R00829
SUBSTRATE   succinyl-CoA [CPD:C00091];
            acetyl-CoA [CPD:C00024]
PRODUCT     CoA [CPD:C00010];
            3-oxoadipyl-CoA [CPD:C02232]
REFERENCE   1  [PMID:11741862]
  AUTHORS   Kaschabek SR, Kuhn B, Muller D, Schmidt E, Reineke W.
  TITLE     Degradation of aromatics and chloroaromatics by Pseudomonas sp.
            strain B13: purification and characterization of
            3-oxoadipate:succinyl-coenzyme A (CoA) transferase and
            3-oxoadipyl-CoA thiolase.
  JOURNAL   J. Bacteriol. 184 (2002) 207-15.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:11741863]
  AUTHORS   Gobel M, Kassel-Cati K, Schmidt E, Reineke W.
  TITLE     Degradation of aromatics and chloroaromatics by Pseudomonas sp.
            strain B13: cloning, characterization, and analysis of sequences
            encoding 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and
            3-oxoadipyl-CoA thiolase.
  JOURNAL   J. Bacteriol. 184 (2002) 216-23.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
ORTHOLOGY   KO: K07823  3-oxoadipyl-CoA thiolase
GENES       PAE: PA0228(pcaF)
            PPU: PP_1377(pcaF)
            PST: PSPTO_4307(catF)
            PEN: PSEEN1165(pcaF)
            ACI: ACIAD1450(catF)
            ABA: Acid345_3492
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.174
            ExPASy - ENZYME nomenclature database: 2.3.1.174
            ExplorEnz - The Enzyme Database: 2.3.1.174
            ERGO genome analysis and discovery system: 2.3.1.174
            BRENDA, the Enzyme Database: 2.3.1.174
///
ENTRY       EC 2.3.1.175                Enzyme
NAME        deacetylcephalosporin-C acetyltransferase;
            acetyl-CoA:deacetylcephalosporin-C acetyltransferase;
            DAC acetyltransferase;
            cefG;
            deacetylcephalosporin C acetyltransferase;
            acetyl coenzyme A:DAC acetyltransferase;
            acetyl-CoA:DAC acetyltransferase;
            CPC acetylhydrolase;
            acetyl-CoA:DAC O-acetyltransferase;
            DAC-AT
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:deacetylcephalosporin-C O-acetyltransferase
REACTION    acetyl-CoA + deacetylcephalosporin C = CoA + cephalosporin C
            [RN:R03064]
ALL_REAC    R03064
SUBSTRATE   acetyl-CoA [CPD:C00024];
            deacetylcephalosporin C [CPD:C03112]
PRODUCT     CoA [CPD:C00010];
            cephalosporin C [CPD:C00916]
COMMENT     This enzyme catalyses the final step in the biosynthesis of
            cephalosporin C.
REFERENCE   1  [PMID:1368946]
  AUTHORS   Matsuyama K, Matsumoto H, Matsuda A, Sugiura H, Komatsu K, Ichikawa
            S.
  TITLE     Purification of acetyl coenzyme A: deacetylacephalosporin C
            O-acetyltransferase from Acremonium chrysogenum.
  JOURNAL   Biosci. Biotechnol. Biochem. 56 (1992) 1410-2.
  ORGANISM  Acremonium chrysogenum
REFERENCE   2  [PMID:1569032]
  AUTHORS   Gutierrez S, Velasco J, Fernandez FJ, Martin JF.
  TITLE     The cefG gene of Cephalosporium acremonium is linked to the cefEF
            gene and encodes a deacetylcephalosporin C acetyltransferase closely
            related to homoserine O-acetyltransferase.
  JOURNAL   J. Bacteriol. 174 (1992) 3056-64.
  ORGANISM  Cephalosporium acremonium
REFERENCE   3  [PMID:1632779]
  AUTHORS   Matsuda A, Sugiura H, Matsuyama K, Matsumoto H, Ichikawa S, Komatsu
            K.
  TITLE     Cloning and disruption of the cefG gene encoding acetyl coenzyme A:
            deacetylcephalosporin C o-acetyltransferase from Acremonium
            chrysogenum.
  JOURNAL   Biochem. Biophys. Res. Commun. 186 (1992) 40-6.
  ORGANISM  Acremonium chrysogenum
REFERENCE   4  [PMID:9421924]
  AUTHORS   Gutierrez S, Velasco J, Marcos AT, Fernandez FJ, Fierro F, Barredo
            JL, Diez B, Martin JF.
  TITLE     Expression of the cefG gene is limiting for cephalosporin
            biosynthesis in Acremonium chrysogenum.
  JOURNAL   Appl. Microbiol. Biotechnol. 48 (1997) 606-14.
  ORGANISM  Acremonium chrysogenum
REFERENCE   5  [PMID:9895280]
  AUTHORS   Velasco J, Gutierrez S, Campoy S, Martin JF.
  TITLE     Molecular characterization of the Acremonium chrysogenum cefG gene
            product: the native deacetylcephalosporin C acetyltransferase is not
            processed into subunits.
  JOURNAL   Biochem. J. 337 ( Pt 3) (1999) 379-85.
  ORGANISM  Acremonium chrysogenum
REFERENCE   6  [PMID:7847890]
  AUTHORS   Martin JF, Gutierrez S, Fernandez FJ, Velasco J, Fierro F, Marcos
            AT, Kosalkova K.
  TITLE     Expression of genes and processing of enzymes for the biosynthesis
            of penicillins and cephalosporins.
  JOURNAL   Antonie. Van. Leeuwenhoek. 65 (1994) 227-43.
  ORGANISM  Acremonium chrysogenum
PATHWAY     PATH: map00311  Penicillin and cephalosporin biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.175
            ExPASy - ENZYME nomenclature database: 2.3.1.175
            ExplorEnz - The Enzyme Database: 2.3.1.175
            ERGO genome analysis and discovery system: 2.3.1.175
            BRENDA, the Enzyme Database: 2.3.1.175
///
ENTRY       EC 2.3.1.176                Enzyme
NAME        propanoyl-CoA C-acyltransferase;
            peroxisomal thiolase 2;
            sterol carrier protein-;
            SCP;
            PTE-2 (ambiguous)
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA:propanoyl-CoA
            C-acyltransferase
REACTION    3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA + propanoyl-CoA
            = CoA +
            3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA
SUBSTRATE   3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA;
            propanoyl-CoA [CPD:C00100]
PRODUCT     CoA [CPD:C00010];
            3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA
COMMENT     Also acts on dihydroxy-5beta-cholestanoyl-CoA and other branched
            chain acyl-CoA derivatives. The enzyme catalyses the penultimate
            step in the formation of bile acids. The bile acid moiety is
            transferred from the acyl-CoA thioester (RCO-SCoA) to either glycine
            or taurine (NH2R') by EC 2.3.1.65, bile acid-CoA:amino acid
            N-acyltransferase [4].
REFERENCE   1  [PMID:7461136]
  AUTHORS   Pedersen JI, Gustafsson J.
  TITLE     Conversion of 3 alpha, 7 alpha, 12 alpha-trihydroxy-5
            beta-cholestanoic acid into cholic acid by rat liver peroxisomes.
  JOURNAL   FEBS. Lett. 121 (1980) 345-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6668450]
  AUTHORS   Kase F, Bjorkhem I, Pedersen JI.
  TITLE     Formation of cholic acid from 3 alpha, 7 alpha, 12
            alpha-trihydroxy-5 beta-cholestanoic acid by rat liver peroxisomes.
  JOURNAL   J. Lipid. Res. 24 (1983) 1560-7.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:12543708]
  AUTHORS   Russell DW.
  TITLE     The enzymes, regulation, and genetics of bile acid synthesis.
  JOURNAL   Annu. Rev. Biochem. 72 (2003) 137-74.
  ORGANISM  rat [GN:rno], mouse [GN:mmu]
REFERENCE   4  [PMID:8034703]
  AUTHORS   Falany CN, Johnson MR, Barnes S, Diasio RB.
  TITLE     Glycine and taurine conjugation of bile acids by a single enzyme.
            Molecular cloning and expression of human liver bile acid CoA:amino
            acid N-acyltransferase.
  JOURNAL   J. Biol. Chem. 269 (1994) 19375-9.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map03320  PPAR signaling pathway
ORTHOLOGY   KO: K08764  sterol carrier protein 2
GENES       HSA: 6342(SCP2)
            PTR: 456862(SCP2)
            MMU: 20280(Scp2)
            RNO: 25541(Scp2)
            CFA: 479564(SCP2)
            BTA: 508918(SCP2)
            GGA: 396550(SCP2)
            OSA: 4340463
            TET: TTHERM_01299660
            SMD: Smed_1439
            XAU: Xaut_1335 Xaut_4071
            SWI: Swit_0342 Swit_1611 Swit_1855 Swit_3625 Swit_4119
            ACR: Acry_2397
            MAV: MAV_3681
            STP: Strop_2644
            MAE: Maeo_0021
            MSE: Msed_0386 Msed_1290
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.176
            ExPASy - ENZYME nomenclature database: 2.3.1.176
            ExplorEnz - The Enzyme Database: 2.3.1.176
            ERGO genome analysis and discovery system: 2.3.1.176
            BRENDA, the Enzyme Database: 2.3.1.176
///
ENTRY       EC 2.3.1.177                Enzyme
NAME        biphenyl synthase;
            BIS
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     malonyl-CoA:benzoyl-CoA malonyltransferase
REACTION    3 malonyl-CoA + benzoyl-CoA = 4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
SUBSTRATE   malonyl-CoA [CPD:C00083];
            benzoyl-CoA [CPD:C00512]
PRODUCT     CoA [CPD:C00010];
            3,5-dihydroxybiphenyl;
            CO2 [CPD:C00011]
COMMENT     A polyketide synthase that is involved in the production of the
            phytoalexin aucuparin. 2-Hydroxybenzoyl-CoA can also act as
            substrate but it leads to the derailment product
            2-hydroxybenzoyltriacetic acid lactone. This enzyme uses the same
            starter substrate as EC 2.3.1.151, benzophenone synthase.
REFERENCE   1  [PMID:14595561]
  AUTHORS   Liu B, Beuerle T, Klundt T, Beerhues L.
  TITLE     Biphenyl synthase from yeast-extract-treated cell cultures of Sorbus
            aucuparia.
  JOURNAL   Planta. 218 (2004) 492-6.
  ORGANISM  Sorbus aucuparia
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.177
            ExPASy - ENZYME nomenclature database: 2.3.1.177
            ExplorEnz - The Enzyme Database: 2.3.1.177
            ERGO genome analysis and discovery system: 2.3.1.177
            BRENDA, the Enzyme Database: 2.3.1.177
///
ENTRY       EC 2.3.1.178                Enzyme
NAME        diaminobutyrate acetyltransferase;
            L-2,4-diaminobutyrate acetyltransferase;
            L-2,4-diaminobutanoate acetyltransferase;
            EctA;
            diaminobutyric acid acetyltransferase;
            DABA acetyltransferase;
            2,4-diaminobutanoate acetyltransferase;
            DAB acetyltransferase;
            DABAcT;
            acetyl-CoA:L-2,4-diaminobutanoate 4-N-acetyltransferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:L-2,4-diaminobutanoate N4-acetyltransferase
REACTION    acetyl-CoA + L-2,4-diaminobutanoate = CoA +
            N4-acetyl-L-2,4-diaminobutanoate
ALL_REAC    (other) R06978
SUBSTRATE   acetyl-CoA [CPD:C00024];
            L-2,4-diaminobutanoate [CPD:C03283]
PRODUCT     CoA [CPD:C00010];
            N4-acetyl-L-2,4-diaminobutanoate
COMMENT     Requires Na+ or K+ for maximal activity [3]. Ornithine, lysine,
            aspartate, and alpha-, beta- and gamma-aminobutanoate cannot act as
            substrates [3]. However, acetyl-CoA can be replaced by
            propanoyl-CoA, although the reaction proceeds more slowly [3]. Forms
            part of the ectoine-biosynthesis pathway, the other enzymes involved
            being EC 2.6.1.76, diaminobutyrate---2-oxoglutarate transaminase and
            EC 4.2.1.108, ectoine synthase.
REFERENCE   1
  AUTHORS   Peters, P., Galinski, E.A. and Truper, H.G.
  TITLE     The biosynthesis of ectoine.
  JOURNAL   FEMS Microbiol. Lett. 71 (1990) 157-162.
  ORGANISM  Halomonas elongata, Ectothiorhodospira halochloris
REFERENCE   2  [PMID:9864317]
  AUTHORS   Ono H, Sawada K, Khunajakr N, Tao T, Yamamoto M, Hiramoto M, Shinmyo
            A, Takano M, Murooka Y.
  TITLE     Characterization of biosynthetic enzymes for ectoine as a compatible
            solute in a moderately halophilic eubacterium, Halomonas elongata.
  JOURNAL   J. Bacteriol. 181 (1999) 91-9.
  ORGANISM  Halomonas elongata
REFERENCE   3  [PMID:16212543]
  AUTHORS   Reshetnikov AS, Mustakhimov II, Khmelenina VN, Trotsenko YA.
  TITLE     Cloning, purification, and characterization of diaminobutyrate
            acetyltransferase from the halotolerant methanotroph
            Methylomicrobium alcaliphilum 20Z.
  JOURNAL   Biochemistry. (Mosc). 70 (2005) 878-83.
  ORGANISM  Methylomicrobium alcaliphilum
REFERENCE   4  [PMID:11823218]
  AUTHORS   Kuhlmann AU, Bremer E.
  TITLE     Osmotically regulated synthesis of the compatible solute ectoine in
            Bacillus pasteurii and related Bacillus spp.
  JOURNAL   Appl. Environ. Microbiol. 68 (2002) 772-83.
  ORGANISM  Bacillus pasteurii, Bacillus spp.
REFERENCE   5  [PMID:9141677]
  AUTHORS   Louis P, Galinski EA.
  TITLE     Characterization of genes for the biosynthesis of the compatible
            solute ectoine from Marinococcus halophilus and osmoregulated
            expression in Escherichia coli.
  JOURNAL   Microbiology. 143 ( Pt 4) (1997) 1141-9.
  ORGANISM  Marinococcus halophilus
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K06718  L-2,4-diaminobutyric acid acetyltransferase
GENES       VCH: VCA0825
            VPA: VP1722
            VFI: VFA1122
            SDE: Sde_1189
            TCX: Tcr_0518
            NOC: Noc_1562
            AEH: Mlg_1192
            HCH: HCH_01510
            CSA: Csal_1876
            ABO: ABO_2150(ectA)
            BPE: BP2215(ectA)
            BPA: BPP1888(ectA)
            BBR: BB3220(ectA)
            WSU: WS0854
            SIT: TM1040_0551
            HNE: HNE_1639(ectA)
            SAL: Sala_2949
            BHA: BH0920
            BCL: ABC0334(ectA)
            MSM: MSMEG_3901(ectA)
            MMC: Mmcs_4190
            NFA: nfa27160(ectA)
            RHA: RHA1_ro01305
            SCO: SCO1864(SCI39.11)
            SMA: SAV6398(ectA)
            TFU: Tfu_0300
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.178
            ExPASy - ENZYME nomenclature database: 2.3.1.178
            ExplorEnz - The Enzyme Database: 2.3.1.178
            ERGO genome analysis and discovery system: 2.3.1.178
            BRENDA, the Enzyme Database: 2.3.1.178
///
ENTRY       EC 2.3.1.179                Enzyme
NAME        beta-ketoacyl-acyl-carrier-protein synthase II;
            KASII;
            KAS II;
            FabF;
            3-oxoacyl-acyl carrier protein synthase I;
            beta-ketoacyl-ACP synthase II
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     (Z)-hexadec-11-enoyl-[acyl-carrier-protein]:malonyl-[acyl-carrier-pr
            otein] C-acyltransferase (decarboxylating)
REACTION    (Z)-hexadec-11-enoyl-[acyl-carrier-protein] +
            malonyl-[acyl-carrier-protein] =
            (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 +
            [acyl-carrier-protein]
ALL_REAC    (other) R01624 R04355 R04726 R04952 R04957 R04960 R04963 R04968
SUBSTRATE   (Z)-hexadec-11-enoyl-[acyl-carrier-protein];
            malonyl-[acyl-carrier-protein]
PRODUCT     (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein];
            CO2 [CPD:C00011];
            [acyl-carrier-protein]
COMMENT     Involved in the dissociated (or type II) fatty acid biosynthesis
            system that occurs in plants and bacteria. While the substrate
            specificity of this enzyme is very similar to that of EC 2.3.1.41,
            beta-ketoacyl-ACP synthase I, it differs in that palmitoleoyl-ACP is
            not a good substrate of EC 2.3.1.41 but is an excellent substrate of
            this enzyme [1,2]. The fatty-acid composition of Escherichia coli
            changes as a function of growth temperature, with the proportion of
            unsaturated fatty acids increasing with lower growth temperature.
            This enzyme controls the temperature-dependent regulation of
            fatty-acid composition, with mutants lacking this acivity being
            deficient in the elongation of palmitoleate to cis-vaccenate at low
            temperatures [3,4].
REFERENCE   1  [PMID:237914]
  AUTHORS   D'Agnolo G, Rosenfeld IS, Vagelos PR.
  TITLE     Multiple forms of beta-ketoacyl-acyl carrier protein synthetase in
            Escherichia coli.
  JOURNAL   J. Biol. Chem. 250 (1975) 5289-94.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:7002930]
  AUTHORS   Garwin JL, Klages AL, Cronan JE Jr.
  TITLE     Structural, enzymatic, and genetic studies of beta-ketoacyl-acyl
            carrier protein synthases I and II of Escherichia coli.
  JOURNAL   J. Biol. Chem. 255 (1980) 11949-56.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:12837788]
  AUTHORS   Price AC, Rock CO, White SW.
  TITLE     The 1.3-Angstrom-resolution crystal structure of beta-ketoacyl-acyl
            carrier protein synthase II from Streptococcus pneumoniae.
  JOURNAL   J. Bacteriol. 185 (2003) 4136-43.
  ORGANISM  Streptococcus pneumoniae
REFERENCE   4  [PMID:6988423]
  AUTHORS   Garwin JL, Klages AL, Cronan JE Jr.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase II of Escherichia coli.
            Evidence for function in the thermal regulation of fatty acid
            synthesis.
  JOURNAL   J. Biol. Chem. 255 (1980) 3263-5.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:7768872]
  AUTHORS   Magnuson K, Carey MR, Cronan JE Jr.
  TITLE     The putative fabJ gene of Escherichia coli fatty acid synthesis is
            the fabF gene.
  JOURNAL   J. Bacteriol. 177 (1995) 3593-5.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6
  AUTHORS   Cronan, J.E., Jr. and Rock, C.O.
  TITLE     Biosynthesis of membrane lipids.
  JOURNAL   In: Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular
            and Molecular Biology, 2nd ed., vol. 1, ASM Press, Washington, DC,
            1996, p. 612-636.
PATHWAY     PATH: map00061  Fatty acid biosynthesis
ORTHOLOGY   KO: K09458  3-oxoacyl-[acyl-carrier-protein] synthase II
GENES       HSA: 54995(OXSM)
            MMU: 71147(Oxsm)
            RNO: 289934(RGD1311092)
            CFA: 477043(OXSM)
            BTA: 513530(MGC142360)
            GGA: 420656(OXSM)
            SPU: 589426(LOC589426)
            DME: Dmel_CG12170
            OSA: 4335962
            CME: CMM286C
            SPO: SPBC887.13c
            ANI: AN7489.2
            AOR: AO090001000695
            PFA: PFF1275c(FabB/FabF)
            ECO: b1095(fabF)
            ECJ: JW1081(fabF)
            ECE: Z1734(fabF) Z4866
            ECS: ECs1473 ECs4341
            ECC: c1186 c1365(fabF)
            ECI: UTI89_C1221(fabF)
            ECP: ECP_1087
            ECV: APECO1_176(fabF)
            STY: STY1236(fabF)
            STT: t1723(fabF)
            SPT: SPA1654(fabF)
            SEC: SC1145(fabF)
            STM: STM1197(fabF)
            YPE: YPO1601(fabF)
            YPK: y1760(fabF) y2744(fabF)
            YPM: YP_2253(fabF4)
            YPA: YPA_0719 YPA_1924
            YPN: YPN_2028 YPN_2552
            YPS: YPTB1449(fabF2) YPTB2469(fabF)
            SFL: SF1099(fabF)
            SFX: S1179(fabF)
            SFV: SFV_1115(fabF)
            SSN: SSON_1115(fabF)
            SBO: SBO_1968(fabF)
            SDY: SDY_2055(fabF) SDY_3629
            ECA: ECA1799(fabF) ECA2928 ECA4491
            PLU: plu2217 plu2831(fabF)
            SGL: SG1062
            HSO: HS_0108(fab)
            XFA: XF0673
            XFT: PD1501(fabB)
            XCC: XCC1020(fabF)
            XCB: XC_3225
            XCV: XCV1148(fabF)
            XAC: XAC1129(fabF)
            XOO: XOO0883(fabF)
            XOM: XOO_0808(XOO0808)
            VCH: VC2019
            VVU: VV1_0061
            VVY: VV1066 VV1277
            VPA: VP0881 VP2052
            VFI: VF0860 VF1738
            PPR: PBPRA1197(fabF-1) PBPRB0104
            PAE: PA1373(fabF2) PA2965(fabF1)
            PAU: PA14_25690(fabF1) PA14_46490(fabF2)
            PPU: PP_1916(fabF) PP_3303
            PST: PSPTO_3830(fabF) PSPTO_5110
            PSB: Psyr_0422 Psyr_1649
            PSP: PSPPH_0412 PSPPH_1643(fabF)
            PFL: PFL_0461(fabF-2) PFL_1798(fabF-1) PFL_3434(fabF)
            PFO: Pfl_0422 Pfl_4038 Pfl_4155
            PEN: PSEEN0345 PSEEN1621(fabF)
            PAR: Psyc_1972(fabF)
            PCR: Pcryo_2271
            ACI: ACIAD0583(fabF)
            SON: SO_2774(fabF-1) SO_4383(fabF-2)
            SDN: Sden_2291
            SFR: Sfri_0337 Sfri_1501
            SAZ: Sama_1978
            SBL: Sbal_1721
            SLO: Shew_1605
            SHE: Shewmr4_0335 Shewmr4_2394
            SHM: Shewmr7_2464 Shewmr7_3691
            SHN: Shewana3_0326 Shewana3_2557
            SHW: Sputw3181_2438
            ILO: IL0143
            CPS: CPS_2299(fabF)
            PHA: PSHAa1806(fabF) PSHAb0410
            PAT: Patl_2120
            SDE: Sde_1631
            CBU: CBU_0497(fabF)
            LPN: lpg1397(fabF1)
            LPF: lpl1348(fabF)
            LPP: lpp1352(fabF)
            MCA: MCA1999(fabF)
            FTU: FTT1377(fabF)
            FTF: FTF1377(fabF)
            FTW: FTW_0514(fabF)
            FTL: FTL_1137
            FTH: FTH_1112(fabF)
            FTN: FTN_1341(fabF)
            TCX: Tcr_0714
            NOC: Noc_1663
            AEH: Mlg_1419
            CSA: Csal_1603 Csal_2911
            ABO: ABO_1071(fabF)
            AHA: AHA_2253 AHA_3382
            NME: NMB0219 NMB1703
            NMA: NMA0044(fabF) NMA1957(fabF2)
            NGO: NGO1763(fabF)
            CVI: CV_1541 CV_3412(fabF)
            RSO: RSc1054(fabF1) RSp0358(fabF2)
            REU: Reut_A2261
            REH: H16_A2565(fabF)
            RME: Rmet_2426 Rmet_4392
            BMA: BMA0534(fabF)
            BXE: Bxe_A0940 Bxe_A1076
            BUR: Bcep18194_A4237 Bcep18194_B1918
            BCN: Bcen_0645
            BCH: Bcen2424_1125
            BAM: Bamb_1001 Bamb_3611
            BPS: BPSL2438(fabF)
            BPM: BURPS1710b_2903(fabF)
            BTE: BTH_I1721
            BPE: BP2439(fabF)
            BPA: BPP3303(fabF)
            BBR: BB3754(fabF)
            RFR: Rfer_1734 Rfer_3139
            POL: Bpro_3645
            NEU: NE1650(fabF1)
            NET: Neut_0466
            NMU: Nmul_A1076
            EBA: ebA5459(fabF)
            DAR: Daro_2019
            TBD: Tbd_1547
            MFA: Mfla_1503
            HPY: HP0558(fabF)
            HPJ: jhp0505(fabB)
            HPA: HPAG1_0536
            HHE: HH0727(fabF)
            HAC: Hac_0779(fabF)
            TDN: Tmden_1609
            CJE: Cj0442(fabF)
            CJR: CJE0494(fabF)
            GSU: GSU0460(fabF-1) GSU1605(fabF-2)
            GME: Gmet_1603
            PCA: Pcar_1440
            DVU: DVU1204(fabF)
            DDE: Dde_2431
            LIP: LI0160(fabF)
            BBA: Bd2010(fabF)
            DPS: DP1859 DP2788
            ADE: Adeh_2746
            MXA: MXAN_4768(fabF)
            SAT: SYN_02365
            SFU: Sfum_1375
            RPR: RP764(fabF)
            RTY: RT0750(fabF)
            RCO: RC1186(fabF)
            RFE: RF_1224(fabF)
            RBE: RBE_0114(fabF)
            WOL: WD1194(fabF)
            WBM: Wbm0739
            APH: APH_0930(fabF)
            ERU: Erum2150(fabF)
            ERW: ERWE_CDS_02170(fabF)
            ERG: ERGA_CDS_02130(fabF)
            ECN: Ecaj_0218
            ECH: ECH_0882(fabF)
            NSE: NSE_0453(fabF)
            MLO: mlr1176 mlr2832 mlr7852
            MES: Meso_1319 Meso_1766
            SME: SMc00574(fabF) SMc04275
            ATU: Atu1097(fabF) Atu1597(fabF) Atu4216(fabF)
            ATC: AGR_C_2030 AGR_C_2935 AGR_L_1284
            RET: RHE_CH01445(fabF1) RHE_CH02120(fabF2) RHE_CH02476
            RLE: RL1560(fabF) RL2409(fabF) RL2815(fabF2)
            BME: BMEI1112 BMEI1473
            BMF: BAB1_0486 BAB1_0873
            BMS: BR0461(fabF) BR0854
            BMB: BruAb1_0483(fabF) BruAb1_0866
            BJA: bll2529(fabF) bll3809(fabF) blr4085(fabF)
            RPA: RPA2020 RPA3072(fabF)
            RPB: RPB_2469 RPB_3355
            RPC: RPC_2109 RPC_2302
            RPD: RPD_2088 RPD_2977
            RPE: RPE_2021 RPE_3304
            NWI: Nwi_1244 Nwi_1686
            NHA: Nham_1504 Nham_2351
            BHE: BH05370(fabF1) BH07450(fabF3)
            BQU: BQ04550(fabF1) BQ05300(fabF3)
            CCR: CC_1678
            SIL: SPO2271(fabF)
            SIT: TM1040_1054
            RSP: RSP_2464(fabF)
            JAN: Jann_1629
            RDE: RD1_3036(fabF)
            MMR: Mmar10_1217
            HNE: HNE_2156(fabF)
            ZMO: ZMO1278(fabF)
            NAR: Saro_1340
            SAL: Sala_0281
            ELI: ELI_03990
            GOX: GOX2042
            GBE: GbCGDNIH1_2208
            RRU: Rru_A0418
            MAG: amb2108
            MGM: Mmc1_1872
            ABA: Acid345_4506
            SUS: Acid_1167
            BSU: BG13128(fabF)
            BHA: BH2882
            BAN: BA1185(fabF)
            BAR: GBAA1185(fabF)
            BAA: BA_1723
            BAT: BAS1096
            BCE: BC1174
            BCA: BCE_1294(fabF)
            BCZ: BCZK1072(fabF)
            BTK: BT9727_1078(fabF)
            BLI: BL03314(fabF)
            BLD: BLi01222(fabF)
            BCL: ABC2546(fabF)
            OIH: OB1205
            GKA: GK0805
            SAU: SA0843(fab)
            SAV: SAV0984
            SAM: MW0866(fab)
            SAR: SAR0947(fabF)
            SAS: SAS0854
            SAC: SACOL0988(fabF)
            SAB: SAB0849(fabF)
            SAA: SAUSA300_0886(fabF)
            SAO: SAOUHSC_00921
            SEP: SE0678
            SER: SERP0568(fabF)
            SHA: SH1972(fab)
            SSP: SSP1797
            LMO: lmo2201
            LMF: LMOf2365_2234(fabF)
            LIN: lin2304
            LWE: lwe2218(fabF)
            LLA: L0186(fabF)
            LLC: LACR_0825
            SPY: SPy_1748(fabF)
            SPZ: M5005_Spy_1489(fabF)
            SPM: spyM18_1820
            SPG: SpyM3_1522(fabF)
            SPS: SPs0344
            SPH: MGAS10270_Spy1557(fabF)
            SPI: MGAS10750_Spy1548(fabF)
            SPJ: MGAS2096_Spy1517(fabF)
            SPK: MGAS9429_Spy1491(fabF)
            SPA: M6_Spy1483
            SPB: M28_Spy1478(fabF)
            SPN: SP_0422
            SPR: spr0382(fabF)
            SPD: SPD_0385(fabF)
            SAG: SAG0349(fabF)
            SAN: gbs0336
            SAK: SAK_0423(fabF)
            SMU: SMU.1739(fabF)
            STC: str0388(fabF)
            STL: stu0388(fabF)
            STE: STER_0434
            LPL: lp_1675(fabF)
            LSL: LSL_0455(fabB)
            LDB: Ldb0904(fabF)
            LBU: LBUL_0822
            LBR: LVIS_0931
            LCA: LSEI_2114
            EFA: EF0283(fabF-1)
            OOE: OEOE_1588
            LME: LEUM_0314
            STH: STH960
            CAC: CAC3573(fabF)
            CPE: CPE1071(fabF)
            CPF: CPF_1327(fabF)
            CPR: CPR_1139(fabF)
            CTC: CTC00131
            CNO: NT01CX_0926
            CHY: CHY_1445(fabF)
            DSY: DSY2657
            SWO: Swol_1848
            MTA: Moth_0950
            MTU: Rv2245(kasA) Rv2246(kasB)
            MTC: MT2305(fabF-1) MT2306(fabF-2)
            MBO: Mb2269(kasA) Mb2270(kasB)
            MLE: ML1655(kasA) ML1656(kasB)
            MPA: MAP1998(kasA) MAP1999(kasB_1)
            MAV: MAV_2191 MAV_2192
            MSM: MSMEG_4327 MSMEG_4328
            MMC: Mmcs_3366 Mmcs_3367
            NFA: nfa16170(kasA)
            SCO: SCO2390(fabF) SCO5886(redR)
            SMA: SAV2292(fabF)
            TWH: TWT251(kasA)
            TWS: TW519(fabF)
            LXX: Lxx12750(fabF)
            FRA: Francci3_2092 Francci3_3484
            ACE: Acel_1199
            RXY: Rxyl_1383
            FNU: FN0151
            RBA: RB320(fabF)
            CTR: CT770(fabF)
            CTA: CTA_0840(fabF)
            CMU: TC0151
            CPN: CPn0916(fabF)
            CPA: CP0950
            CPJ: CPj0916(fabF)
            CPT: CpB0948
            CCA: CCA00853(fabF)
            CAB: CAB818(fabF)
            CFE: CF0163(fabF)
            PCU: pc1238(fabF)
            TDE: TDE0038(fabF)
            SYN: sll1069(fabF)
            SYW: SYNW0142(fabF)
            SYC: syc0984_c(fabF)
            SYF: Synpcc7942_0537
            SYD: Syncc9605_0125
            SYE: Syncc9902_0169
            SYG: sync_0131(fabF)
            CYA: CYA_2873(fabF)
            CYB: CYB_1666(fabF)
            TEL: tll1871
            GVI: gll4014
            ANA: alr3343
            AVA: Ava_3646
            PMM: PMM1609(fabF)
            PMT: PMT1956(fabF)
            PMN: PMN2A_1186
            PMI: PMT9312_1702
            TER: Tery_0451
            BTH: BT_3358
            BFR: BF0219
            BFS: BF0178
            PGI: PG1764(fabF)
            SRU: SRU_2753(fabF)
            CHU: CHU_1397(fabF)
            CTE: CT2118(fabF)
            CCH: Cag_1660
            PLT: Plut_0129
            DET: DET0963(fabF)
            DEH: cbdb_A921(fabF)
            DRA: DR_1941
            DGE: Dgeo_0437
            TTH: TTC0045
            TTJ: TTHA0413
            AAE: aq_1717(fabF)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.179
            ExPASy - ENZYME nomenclature database: 2.3.1.179
            ExplorEnz - The Enzyme Database: 2.3.1.179
            ERGO genome analysis and discovery system: 2.3.1.179
            BRENDA, the Enzyme Database: 2.3.1.179
///
ENTRY       EC 2.3.1.180                Enzyme
NAME        beta-ketoacyl-[acyl-carrier-protein] synthase III;
            3-oxoacyl:ACP synthase III;
            3-ketoacyl-acyl carrier protein synthase III;
            KASIII;
            KAS III;
            FabH;
            beta-ketoacyl-acyl carrier protein synthase III;
            beta-ketoacyl-ACP synthase III;
            beta-ketoacyl (acyl carrier protein) synthase III;
            beta-ketoacyl-acyl-carrier-protein synthase III
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     acetyl-CoA:malonyl-[acyl-carrier-protein] C-acyltransferase
REACTION    acetyl-CoA + malonyl-[acyl-carrier-protein] =
            acetoacetyl-[acyl-carrier-protein] + CoA + CO2
ALL_REAC    (other) R01624 R04355 R04726 R04952 R04957 R04960 R04963 R04968
SUBSTRATE   acetyl-CoA [CPD:C00024];
            malonyl-[acyl-carrier-protein]
PRODUCT     acetoacetyl-[acyl-carrier-protein];
            CoA [CPD:C00010];
            CO2 [CPD:C00011]
COMMENT     Involved in the dissociated (or type II) fatty-acid biosynthesis
            system that occurs in plants and bacteria. In contrast to EC
            2.3.1.41 (beta-ketoacyl-ACP synthase I) and EC 2.3.1.179
            (beta-ketoacyl-ACP synthase II), this enzyme specifically uses CoA
            thioesters rather than acyl-ACP as the primer [1]. In addition to
            the above reaction, the enzyme can also catalyse the reaction of EC
            2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, but to a much
            lesser extent [1]. The enzyme is responsible for initiating both
            straight- and branched-chain fatty-acid biosynthesis [2], with the
            substrate specificity in an organism reflecting the fatty-acid
            composition found in that organism [2,5]. For example, Streptococcus
            pneumoniae, a Gram-positive bacterium, is able to use both straight-
            and branched-chain (C4---C6) acyl-CoA primers [3] whereas
            Escherichia coli, a Gram-negative organism, uses primarily short
            straight-chain acyl CoAs, with a preference for acetyl-CoA [4,5].
REFERENCE   1  [PMID:1551888]
  AUTHORS   Tsay JT, Oh W, Larson TJ, Jackowski S, Rock CO.
  TITLE     Isolation and characterization of the beta-ketoacyl-acyl carrier
            protein synthase III gene (fabH) from Escherichia coli K-12.
  JOURNAL   J. Biol. Chem. 267 (1992) 6807-14.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:9721286]
  AUTHORS   Han L, Lobo S, Reynolds KA.
  TITLE     Characterization of beta-ketoacyl-acyl carrier protein synthase III
            from Streptomyces glaucescens and its role in initiation of fatty
            acid biosynthesis.
  JOURNAL   J. Bacteriol. 180 (1998) 4481-6.
  ORGANISM  Streptomyces glaucescens
REFERENCE   3  [PMID:11375394]
  AUTHORS   Khandekar SS, Gentry DR, Van Aller GS, Warren P, Xiang H, Silverman
            C, Doyle ML, Chambers PA, Konstantinidis AK, Brandt M, Daines RA,
            Lonsdale JT.
  TITLE     Identification, substrate specificity, and inhibition of the
            Streptococcus pneumoniae beta-ketoacyl-acyl carrier protein synthase
            III (FabH).
  JOURNAL   J. Biol. Chem. 276 (2001) 30024-30.
  ORGANISM  Streptococcus pneumoniae
REFERENCE   4  [PMID:10840036]
  AUTHORS   Choi KH, Kremer L, Besra GS, Rock CO.
  TITLE     Identification and substrate specificity of beta -ketoacyl (acyl
            carrier protein) synthase III (mtFabH) from Mycobacterium
            tuberculosis.
  JOURNAL   J. Biol. Chem. 275 (2000) 28201-7.
  ORGANISM  Mycobacterium tuberculosis
REFERENCE   5  [PMID:15987898]
  AUTHORS   Qiu X, Choudhry AE, Janson CA, Grooms M, Daines RA, Lonsdale JT,
            Khandekar SS.
  TITLE     Crystal structure and substrate specificity of the
            beta-ketoacyl-acyl carrier protein synthase III (FabH) from
            Staphylococcus aureus.
  JOURNAL   Protein. Sci. 14 (2005) 2087-94.
  ORGANISM  Staphylococcus aureus
REFERENCE   6  [PMID:15901703]
  AUTHORS   Li Y, Florova G, Reynolds KA.
  TITLE     Alteration of the fatty acid profile of Streptomyces coelicolor by
            replacement of the initiation enzyme 3-ketoacyl acyl carrier protein
            synthase III (FabH).
  JOURNAL   J. Bacteriol. 187 (2005) 3795-9.
  ORGANISM  Streptomyces coelicolor [GN:sco]
REFERENCE   7
  AUTHORS   Cronan, J.E., Jr. and Rock, C.O.
  TITLE     Biosynthesis of membrane lipids.
  JOURNAL   In: Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular
            and Molecular Biology, 2nd ed., vol. 1, ASM Press, Washington, DC,
            1996, p. 612-636.
PATHWAY     PATH: map00061  Fatty acid biosynthesis
ORTHOLOGY   KO: K00648  3-oxoacyl-[acyl-carrier-protein] synthase III
GENES       ATH: AT1G62640(KAS_III)
            OSA: 4337178
            ECO: b1091(fabH)
            ECJ: JW1077(fabH)
            ECE: Z1730(fabH)
            ECS: ECs1469
            ECC: c1360(fabH) c1689
            ECI: UTI89_C1216(fabH)
            ECP: ECP_1083
            ECV: APECO1_172(fabH)
            STY: STY1232(fabH)
            STT: t1727(fabH)
            SPT: SPA1658(fabH)
            SEC: SC1141(fabH)
            STM: STM1193(fabH)
            YPE: YPO1597(fabH)
            YPK: y1756(fabH) y2334 y2335
            YPM: YP_2257(fabH2)
            YPA: YPA_1359 YPA_1360 YPA_1928
            YPN: YPN_2032
            YPS: YPTB1971 YPTB2473(fabH)
            SFL: SF1095(fabH)
            SFX: S1175(fabH)
            SFV: SFV_1111(fabH)
            SSN: SSON_1111(fabH)
            SBO: SBO_1972(fabH)
            SDY: SDY_2059(fabH)
            ECA: ECA0109 ECA1795(fabH)
            PLU: plu2164 plu2835(fabH)
            SGL: SG1058
            BFL: Bfl406(fabH)
            BPN: BPEN_418(fabH)
            HIN: HI0157(fabH)
            HIT: NTHI0247(fabH)
            HDU: HD0774(fabH)
            HSO: HS_0165(fabH)
            PMU: PM1914(fabH)
            MSU: MS1871(fabH)
            XFA: XF1817 XF1970
            XFT: PD0832(fabH) PD1048(fabH)
            XCC: XCC0212(fabH) XCC1016(fabH) XCC2440(fabH)
            XCB: XC_0222 XC_1672(gumO) XC_3229
            XCV: XCV0239(fabH) XCV1143(fabH) XCV2011(fabH) XCV2770(fabH)
            XAC: XAC0233(fabH) XAC1123(fabH) XAC1964(fabH) XAC2571(fabH)
            XOO: XOO0878(fabH) XOO2592(fabH) XOO4209(fabH)
            XOM: XOO_0803(XOO0803) XOO_2450(XOO2450) XOO_3978(XOO3978)
            VCH: VC2023 VCA0751
            VVU: VV1_1846 VV1_3011 VV2_0349
            VVY: VV1273 VVA0906
            VPA: VP2056 VPA0971
            VFI: VF1742
            PPR: PBPRA1193(fabH) PBPRA1462 PBPRA2001
            PAE: PA0999(fabH1) PA3286 PA3333(fabH2)
            PAU: PA14_20950(fabH2) PA14_21540(fabH-2) PA14_51390(pqsD)
            PPU: PP_4379 PP_4545
            PST: PSPTO_1916 PSPTO_1948 PSPTO_4094
            PSB: Psyr_3467 Psyr_3830
            PSP: PSPPH_1429 PSPPH_3393 PSPPH_3423
            PFL: PFL_1532(fabH) PFL_1626(fabH) PFL_1657 PFL_6132(fabH)
            PFO: Pfl_1421 Pfl_1524
            PEN: PSEEN3827 PSEEN3967
            PAR: Psyc_1052
            PCR: Pcryo_1412
            ACI: ACIAD2101
            SON: SO_1742 SO_2778(fabH-1) SO_2853 SO_2901(fabH-2)
            SDN: Sden_1369 Sden_1381 Sden_2295 Sden_2519
            SFR: Sfri_1365 Sfri_1497 Sfri_1550 Sfri_2467
            SAZ: Sama_1982
            SBL: Sbal_1717
            SLO: Shew_1601
            SHE: Shewmr4_1502 Shewmr4_1520 Shewmr4_2398 Shewmr4_2548
            SHM: Shewmr7_1569 Shewmr7_1587 Shewmr7_2468 Shewmr7_2615
            SHN: Shewana3_1563 Shewana3_1581 Shewana3_2560 Shewana3_2715
            SHW: Sputw3181_2442
            ILO: IL1342(fabH) IL1864
            CPS: CPS_1068 CPS_2153
            PHA: PSHAb0304(fabH)
            PAT: Patl_2124 Patl_3297
            SDE: Sde_0626 Sde_1517
            PIN: Ping_1087
            MAQ: Maqu_1374
            CBU: CBU_0038 CBU_0493(fabH)
            LPN: lpg1393(fabH) lpg1631 lpg2228 lpg2232(fabH)
            LPF: lpl1344(fabH) lpl2153 lpl2158
            LPP: lpp1348(fabH) lpp1601 lpp2180 lpp2185
            MCA: MCA2003(fabH-1)
            FTU: FTT1373(fabH)
            FTF: FTF1373(fabH)
            FTW: FTW_0518(fabH)
            FTL: FTL_1141
            FTH: FTH_1116(fabH)
            FTN: FTN_1337(fabH)
            TCX: Tcr_0710
            NOC: Noc_1667
            AEH: Mlg_1423
            HHA: Hhal_1235
            HCH: HCH_02403(fabH) HCH_02649 HCH_05519
            CSA: Csal_1470
            ABO: ABO_1520(fabB)
            AHA: AHA_1040 AHA_2249(fabH) AHA_3035
            DNO: DNO_1207(fabH)
            BCI: BCI_0436(fabH)
            RMA: Rmag_0483
            NME: NMB1916
            NMA: NMA0538(fabH)
            NMC: NMC0307(fabH)
            NGO: NGO2168(fabH)
            CVI: CV_0805 CV_1096 CV_2446 CV_3416(fabH)
            RSO: RS04707(RSp0194) RSc1050(fabH)
            REU: Reut_A2265(fabH)
            REH: H16_A2569(fabH)
            RME: Rmet_2430
            BMA: BMA0530(fabH) BMA2878 BMA2880
            BMV: BMASAVP1_A2479(fabH-1)
            BML: BMA10299_A2802(fabH)
            BMN: BMA10247_1802(fabH-2)
            BXE: Bxe_A1072
            BUR: Bcep18194_A4233(fabH)
            BCN: Bcen_0641
            BCH: Bcen2424_1121
            BAM: Bamb_0997 Bamb_6224 Bamb_6232
            BPS: BPSL2442(fabH) BPSL3324 BPSL3326 BPSS0484(fabH)
            BPM: BURPS1710b_0096(fabH) BURPS1710b_0099(fabH)
                 BURPS1710b_2907(fabH) BURPS1710b_A2037(fabH)
            BPL: BURPS1106A_2853(fabH)
            BPD: BURPS668_2792(fabH)
            BTE: BTH_I1717 BTH_II1932(fabH)
            PNU: Pnuc_0398
            BPE: BP2443(fabH)
            BPA: BPP0107 BPP3307(fabH)
            BBR: BB0106 BB3758(fabH)
            RFR: Rfer_1730 Rfer_2770 Rfer_3974
            POL: Bpro_3650
            PNA: Pnap_3076
            AAV: Aave_1183
            AJS: Ajs_3280
            VEI: Veis_3252
            MPT: Mpe_A0636
            HAR: HEAR2077(fabH)
            NEU: NE1646(fabH)
            NET: Neut_0470
            NMU: Nmul_A1072
            EBA: ebA5455(fabH)
            AZO: azo1623(fabH)
            DAR: Daro_2015(fabH) Daro_2368
            TBD: Tbd_1551(fabH)
            MFA: Mfla_1507
            HPY: HP0202(fabH)
            HPJ: jhp0188(fabH)
            HPA: HPAG1_0196
            HHE: HH0681(fabH)
            HAC: Hac_0387(fabH)
            WSU: WS1988
            TDN: Tmden_1771
            CJE: Cj0328c(fabH) Cj1303(fabH2)
            CJR: CJE0373(fabH) CJE1492
            GSU: GSU0290(fabH-1) GSU1601(fabH-2)
            GME: Gmet_1599 Gmet_3272
            PCA: Pcar_1436 Pcar_2987
            PPD: Ppro_0016 Ppro_1516
            DVU: DVU1207(fabH)
            DDE: Dde_2428
            LIP: LI0162(fabH)
            BBA: Bd0280(fabH) Bd2014(fabH)
            DPS: DP0741 DP1817 DP2793
            ADE: Adeh_0005 Adeh_2750
            MXA: MXAN_0215 MXAN_0853
            SAT: SYN_01149 SYN_01150 SYN_01698
            SFU: Sfum_0113 Sfum_0933
            RPR: RP772(fabH)
            RTY: RT0759(fabH)
            RCO: RC1202(fabH)
            RFE: RF_1235(fabH)
            RBE: RBE_0128(fabH)
            WOL: WD0985(fabH)
            WBM: Wbm0614
            AMA: AM869(fabH)
            APH: APH_0317(fabH)
            ERU: Erum5720(fabH)
            ERW: ERWE_CDS_06010(fabH)
            ERG: ERGA_CDS_05920(fabH)
            ECN: Ecaj_0574(fabH)
            ECH: ECH_0448(fabH)
            NSE: NSE_0630(fabH)
            MLO: mll1602 mll5827 mll9094 mlr8424
            MES: Meso_1146
            SME: SMc01785(fabH)
            ATU: Atu1179(fabH) Atu4001(fabH)
            ATC: AGR_C_2178 AGR_L_1702
            RET: RHE_CH01532(fabH)
            RLE: RL1639(fabH)
            BME: BMEI1180 BMEII0779
            BMF: BAB1_0798 BAB2_0748
            BMS: BR0777(fabH) BRA0488
            BMB: BruAb1_0792(fabH) BruAb2_0734
            BJA: bll5020(fabH)
            RPA: RPA1298 RPA2741(fabH)
            RPB: RPB_2650 RPB_4123
            RPC: RPC_2676 RPC_2800
            RPD: RPD_2686 RPD_3969
            RPE: RPE_0742 RPE_2826
            NWI: Nwi_1407
            NHA: Nham_1586
            BHE: BH07630(fabH)
            BQU: BQ05480(fabH)
            CCR: CC_0865 CC_1369 CC_1442
            SIL: SPO0918(fabH-1) SPO2494(fabH-2)
            SIT: TM1040_0914
            RSP: RSP_2612(fabH)
            JAN: Jann_1784 Jann_3320
            RDE: RD1_3156(fabH) RD1_3492(fabH)
            MMR: Mmar10_0802 Mmar10_1523
            HNE: HNE_0857 HNE_1162(fabH)
            ZMO: ZMO1899(fabH)
            NAR: Saro_2366
            SAL: Sala_1418 Sala_3145
            ELI: ELI_03745 ELI_08620
            GOX: GOX0115
            GBE: GbCGDNIH1_1014
            RRU: Rru_A1667
            MAG: amb2354
            MGM: Mmc1_1645
            ABA: Acid345_2017
            SUS: Acid_7048
            BSU: BG13048(fabH2) BG13127(fabH1)
            BHA: BH0764 BH1844(fabH) BH2883
            BAN: BA1184(fabH) BA1826 BA1930 BA3251
            BAR: GBAA1184(fabH) GBAA1826 GBAA1930 GBAA3251
            BAA: BA_1722 BA_2331 BA_2433 BA_3759
            BAT: BAS1095 BAS1691 BAS1791 BAS3018
            BCE: BC1173 BC1760
            BCA: BCE_1293(fabH) BCE_1914
            BCZ: BCZK1071(fabH1) BCZK1648(fabH) BCZK1748(fabH) BCZK2940(fabH)
            BTK: BT9727_1077(fabH1) BT9727_1672(fabH) BT9727_3003(fabH)
            BTL: BALH_1709(fabH)
            BLI: BL01107(fabHB) BL03313(fabHA)
            BLD: BLi01097(fabHB) BLi01221(fabHA)
            BCL: ABC2547(fabH1)
            BPU: BPUM_1057(fabHA)
            OIH: OB1204
            GKA: GK0804
            SAU: SA0842(FabH)
            SAV: SAV0983(fabH)
            SAM: MW0865(FabH)
            SAR: SAR0946(fabH)
            SAS: SAS0853
            SAC: SACOL0987(fabH)
            SAB: SAB0848(fabH)
            SAA: SAUSA300_0885(fabH)
            SAO: SAOUHSC_00920
            SEP: SE0677 SE_p512
            SER: SERP0567(fabH)
            SHA: SH1973(fabH)
            SSP: SSP1798
            LMO: lmo2202
            LMF: LMOf2365_2235(fabH)
            LIN: lin2305
            LWE: lwe2219(fabH)
            LLA: L0182(fabH)
            LLC: LACR_0821
            SPY: SPy_1754(fabH)
            SPZ: M5005_Spy_1494(fabH)
            SPM: spyM18_1826
            SPG: SpyM3_1527(fabH)
            SPS: SPs0339
            SPH: MGAS10270_Spy1562(fabH)
            SPI: MGAS10750_Spy1554(fabH)
            SPJ: MGAS2096_Spy1522(fabH)
            SPK: MGAS9429_Spy1496(fabH)
            SPA: M6_Spy1488
            SPB: M28_Spy1483(fabH)
            SPN: SP_0417
            SPR: spr0377(fabH)
            SPD: SPD_0380(fabH)
            SAG: SAG0344(fabH)
            SAN: gbs0331
            SAK: SAK_0418(fabH)
            SMU: SMU.1744(fabH)
            STC: str0382(fabH)
            STL: stu0382(fabH)
            STE: STER_0429
            LPL: lp_0588(fabH1) lp_1671(fabH2)
            LSA: LSA0813(fabH)
            LSL: LSL_0451(fabH) LSL_1257(fabH)
            LDB: Ldb0900(fabH)
            LBU: LBUL_0818
            LBR: LVIS_0935
            LCA: LSEI_2119
            PPE: PEPE_0855 PEPE_1511
            EFA: EF2885(fabH)
            OOE: OEOE_1593
            LME: LEUM_0323
            STH: STH1448 STH2191
            CAC: CAC0814 CAC3578(fabH)
            CPE: CPE1068(fabH)
            CPF: CPF_1324(fabH)
            CPR: CPR_1136(fabH)
            CTC: CTC00127 CTC00859
            CNO: NT01CX_0098 NT01CX_0921 NT01CX_2292
            CHY: CHY_1450(fabH)
            DSY: DSY2663
            SWO: Swol_1853
            TTE: TTE0553(fabH) TTE0557(fabH2) TTE1475(fabH3)
            MTA: Moth_0945
            MTU: Rv0533c(fabH)
            MTC: MT0557(fabH)
            MBO: Mb0547c(fabH)
            MPA: MAP4028c(fabH)
            MAV: MAV_4612
            MSM: MSMEG_1490
            MMC: Mmcs_2936 Mmcs_3413
            NFA: nfa49790(fabH2) nfa52820(fabH) nfa53970(fabH3)
            RHA: RHA1_ro00057 RHA1_ro02213 RHA1_ro05206
            SCO: SCO1271(2SCG18.18c) SCO2388(fabH) SCO3246(fabH4)
                 SCO5888(redP) SCO6564(fabH2) SCP1.233B(mmyC)
            SMA: SAV1831(fabH2) SAV2290(fabH3) SAV5787(fabH1) SAV609(fabH4)
            TWH: TWT253(fabH)
            TWS: TW517(fabH)
            LXX: Lxx12730(fabH)
            ART: Arth_2467 Arth_2954
            PAC: PPA0983
            TFU: Tfu_1974(fabH)
            FRA: Francci3_0990 Francci3_2090 Francci3_3482
            FAL: FRAAL0996(fabH) FRAAL4077 FRAAL5669(fabH)
            ACE: Acel_0877
            RXY: Rxyl_1378
            FNU: FN0148 FN1850
            RBA: RB12812(fabH) RB5678(fabH) RB6272(fabH)
            CTR: CT239(fabH)
            CTA: CTA_0261(fabH)
            CMU: TC0510
            CPN: CPn0298(fabH)
            CPA: CP0460
            CPJ: CPj0298(fabH)
            CPT: CpB0307(yjaX)
            CCA: CCA00484(fabH)
            CAB: CAB470(fabH)
            CFE: CF0523(fabH)
            PCU: pc1720(fabH)
            TDE: TDE0602(fabH)
            LIL: LA1423(fabH)
            LIC: LIC12323
            LBJ: LBJ_2184(fabH)
            LBL: LBL_2178(fabH)
            SYN: slr1511(fabH)
            SYW: SYNW2248(fabH)
            SYC: syc0102_c(fabH)
            SYF: Synpcc7942_1455
            SYD: Syncc9605_2386
            SYE: Syncc9902_0306
            SYG: sync_2599(fabH)
            CYA: CYA_2366(fabH)
            CYB: CYB_2340(fabH)
            TEL: tlr0845(fabH)
            GVI: glr3692
            ANA: alr0239
            AVA: Ava_2729
            PMA: Pro0158(fabH)
            PMM: PMM0136(fabH)
            PMT: PMT1996(fabH)
            PMN: PMN2A_1502(fabH)
            PMI: PMT9312_0138
            TER: Tery_1817
            BTH: BT_0122 BT_3834
            BFR: BF0822 BF3208 BF4089
            BFS: BF3047 BF3904(fabH)
            PGI: PG2141(fabH)
            SRU: SRU_0042(fabH)
            CHU: CHU_0390(fabH) CHU_1624 CHU_1896(fabH)
            CTE: CT2114(fabH)
            CCH: Cag_1664
            PLT: Plut_0133
            DRA: DR_1946 DR_1947
            DGE: Dgeo_0433
            TTH: TTC0049 TTC0343
            TTJ: TTHA0417
            AAE: aq_1099(fabH)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.180
            ExPASy - ENZYME nomenclature database: 2.3.1.180
            ExplorEnz - The Enzyme Database: 2.3.1.180
            ERGO genome analysis and discovery system: 2.3.1.180
            BRENDA, the Enzyme Database: 2.3.1.180
///
ENTRY       EC 2.3.1.181                Enzyme
NAME        lipoyl(octanoyl) transferase;
            LipB;
            lipoyl (octanoyl)-[acyl-carrier-protein]-protein
            N-lipoyltransferase;
            lipoyl (octanoyl)-acyl carrier protein:protein transferase;
            lipoate/octanoate transferase;
            lipoyltransferase;
            octanoyl-[acyl carrier protein]-protein N-octanoyltransferase;
            lipoyl(octanoyl)transferase
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
SYSNAME     octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase
REACTION    octanoyl-[acyl-carrier-protein] + protein = protein
            N6-(octanoyl)lysine + acyl carrier protein [RN:R07766]
ALL_REAC    R07766;
            (other) R07769
SUBSTRATE   octanoyl-[acyl-carrier-protein];
            protein [CPD:C00017]
PRODUCT     protein N6-(octanoyl)lysine [CPD:C16236];
            acyl carrier protein
COMMENT     This is the first committed step in the biosynthesis of lipoyl
            cofactor. Lipoylation is essential for the function of several key
            enzymes involved in oxidative metabolism, as it converts apoprotein
            into the biologically active holoprotein. Examples of such
            lipoylated proteins include pyruvate dehydrogenase (E2 domain),
            2-oxoglutarate dehydrogenase (E2 domain), the branched-chain
            2-oxoacid dehydrogenases and the glycine cleavage system (H protein)
            [2,3]. Lipoyl-ACP can also act as a substrate [4] although
            octanoyl-ACP is likely to be the true substrate [6] . The other
            enzyme involved in the biosynthesis of lipoyl cofactor is EC
            2.8.1.8, lipoyl synthase. An alternative lipoylation pathway
            involves EC 2.7.7.63, lipoate---protein ligase, which can lipoylate
            apoproteins using exogenous lipoic acid (or its analogues).
REFERENCE   1  [PMID:15642479]
  AUTHORS   Nesbitt NM, Baleanu-Gogonea C, Cicchillo RM, Goodson K, Iwig DF,
            Broadwater JA, Haas JA, Fox BG, Booker SJ.
  TITLE     Expression, purification, and physical characterization of
            Escherichia coli lipoyl(octanoyl)transferase.
  JOURNAL   Protein. Expr. Purif. 39 (2005) 269-82.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:1655709]
  AUTHORS   Vanden Boom TJ, Reed KE, Cronan JE Jr.
  TITLE     Lipoic acid metabolism in Escherichia coli: isolation of null
            mutants defective in lipoic acid biosynthesis, molecular cloning and
            characterization of the E. coli lip locus, and identification of the
            lipoylated protein of the glycine cleavage system.
  JOURNAL   J. Bacteriol. 173 (1991) 6411-20.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:9218413]
  AUTHORS   Jordan SW, Cronan JE Jr.
  TITLE     A new metabolic link. The acyl carrier protein of lipid synthesis
            donates lipoic acid to the pyruvate dehydrogenase complex in
            Escherichia coli and mitochondria.
  JOURNAL   J. Biol. Chem. 272 (1997) 17903-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:14700636]
  AUTHORS   Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE.
  TITLE     Assembly of the covalent linkage between lipoic acid and its cognate
            enzymes.
  JOURNAL   Chem. Biol. 10 (2003) 1293-302.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:11427685]
  AUTHORS   Wada M, Yasuno R, Jordan SW, Cronan JE Jr, Wada H.
  TITLE     Lipoic acid metabolism in Arabidopsis thaliana: cloning and
            characterization of a cDNA encoding lipoyltransferase.
  JOURNAL   Plant. Cell. Physiol. 42 (2001) 650-6.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   6  [PMID:10966480]
  AUTHORS   Perham RN.
  TITLE     Swinging arms and swinging domains in multifunctional enzymes:
            catalytic machines for multistep reactions.
  JOURNAL   Annu. Rev. Biochem. 69 (2000) 961-1004.
PATHWAY     PATH: map00785  Lipoic acid metabolism
ORTHOLOGY   KO: K03801  lipoyl(octanoyl) transferase
GENES       HSA: 387787(LOC387787) 650826(LOC650826)
            PTR: 451421(LOC451421)
            MMU: 67164(2610209A20Rik)
            RNO: 365314(RGD1305211_predicted)
            CFA: 485196(LOC485196)
            BTA: 527628(LOC527628)
            XTR: 779684(MGC146528)
            DRE: 664765(zgc:136925)
            SPU: 588984(LOC588984)
            DME: Dmel_CG9804
            CEL: ZC410.7(lpl-1)
            ATH: AT1G04640(LIP2) AT4G31050
            OSA: 4332681 4352692
            CME: CML014C CMR277C
            SCE: YLR239C(LIP2)
            AGO: AGOS_AGL107W
            PIC: PICST_62311(LAB2)
            CAL: CaO19_10528(CaO19.10528) CaO19_3010(CaO19.3010)
            CGR: CAGL0G08404g
            SPO: SPAC4F10.05c
            ANI: AN4781.2
            AFM: AFUA_3G06680
            AOR: AO090020000330
            CNE: CNG01190
            PFA: MAL8P1.37
            TBR: Tb11.01.1160
            TCR: 508851.40 511587.120
            LMA: LmjF36.3080
            ECO: b0630(lipB)
            ECJ: JW5089(lipB)
            ECE: Z0775(lipB)
            ECS: ECs0668
            ECC: c0720(lipB)
            ECI: UTI89_C0632(lipB)
            ECP: ECP_0660
            ECV: APECO1_1425(lipB)
            STY: STY0686(lipB)
            STT: t2232(lipB)
            SPT: SPA2099(lipB)
            SEC: SC0664(lipB)
            STM: STM0635.S(lipB)
            YPE: YPO2599(lipB)
            YPK: y1173(lipB)
            YPM: YP_1114(lipB)
            YPA: YPA_2500
            YPN: YPN_1084
            YPP: YPDSF_2654
            YPS: YPTB1092(lipB)
            YEN: YE3007(lipB)
            SFL: SF0651(lipB)
            SFX: S0673(lipB)
            SFV: SFV_0696(lipB)
            SSN: SSON_0584(lipB)
            SBO: SBO_0494(lipB)
            SDY: SDY_0552(lipB)
            ECA: ECA1298(lipB)
            PLU: plu1292(lipB)
            BUC: BU268(lipB)
            BAS: BUsg258(lipB)
            BAB: bbp249(lipB)
            BCC: BCc_169(lipB)
            WBR: WGLp175(lipB)
            SGL: SG0793
            HIN: HI0027(lipB)
            HIT: NTHI0034(lipB)
            HDU: HD2013(lipB)
            HSO: HS_0316(lipB)
            PMU: PM1929(lipB)
            MSU: MS1827(lipB)
            APL: APL_1594(lipB)
            XFA: XF1270
            XFT: PD0531(lipB)
            XCC: XCC3452(lipB)
            XCB: XC_0712
            XCV: XCV0728(lipB)
            XAC: XAC0667(lipB)
            XOO: XOO3953(lipB)
            XOM: XOO_3731(XOO3731)
            VCH: VC0944
            VVU: VV1_0283
            VVY: VV0901
            VPA: VP0717
            VFI: VF0743
            PPR: PBPRA2895
            PAE: PA3997(lipB)
            PAU: PA14_12120(lipB)
            PPU: PP_4801(lipB)
            PST: PSPTO_4819(lipB)
            PSB: Psyr_4359
            PSP: PSPPH_4400(lipB)
            PFL: PFL_5446(lipB)
            PFO: Pfl_4964
            PEN: PSEEN4820(lipB)
            PAR: Psyc_1295(lipB)
            PCR: Pcryo_1084
            ACI: ACIAD2927(lipB)
            ACB: A1S_2704
            SON: SO_1162(lipB)
            SDN: Sden_0868
            SFR: Sfri_0693
            SAZ: Sama_2594
            SBL: Sbal_3281
            SLO: Shew_2941
            SHE: Shewmr4_0985
            SHM: Shewmr7_1050
            SHN: Shewana3_0989
            SHW: Sputw3181_1028
            ILO: IL0959(lipB)
            CPS: CPS_1710(lipB)
            PHA: PSHAa1020(lipB)
            PAT: Patl_1554
            SDE: Sde_3335
            PIN: Ping_3029
            MAQ: Maqu_2408
            CBU: CBU_1265(lipB)
            LPN: lpg1511
            LPF: lpl1514(lssX)
            LPP: lpp1469(lssX)
            MCA: MCA0109(lipB)
            FTU: FTT1031(lipB)
            FTF: FTF1031(lipB)
            FTW: FTW_0938(lipB)
            FTL: FTL_1058
            FTH: FTH_1034(lipB)
            FTN: FTN_0909(lipB)
            TCX: Tcr_1638
            NOC: Noc_2630
            AEH: Mlg_0179
            HHA: Hhal_1015
            HCH: HCH_05837(lipB)
            CSA: Csal_1551
            ABO: ABO_1963(lipB)
            AHA: AHA_3261(lipB)
            BCI: BCI_0237(lipB)
            RMA: Rmag_0542
            NME: NMB1217
            NMA: NMA1379(lipB)
            NMC: NMC1111(lipB)
            NGO: NGO0792
            CVI: CV_3096(lipB)
            RSO: RSc0323(lipB)
            REU: Reut_A0085
            REH: H16_A0122(lipB)
            RME: Rmet_0060
            BMA: BMA0053(lipB)
            BMV: BMASAVP1_A0219(lipB)
            BML: BMA10299_A1374(lipB)
            BMN: BMA10247_3187(lipB)
            BXE: Bxe_A4213
            BUR: Bcep18194_A6231
            BCN: Bcen_2273
            BCH: Bcen2424_2888
            BAM: Bamb_2938
            BPS: BPSL0413(lipB)
            BPM: BURPS1710b_0626(lipB)
            BPL: BURPS1106A_0463(lipB)
            BPD: BURPS668_0443(lipB)
            BTE: BTH_I0385(lipB)
            PNU: Pnuc_1962
            BPE: BP0105(lipB)
            BPA: BPP0169(lipB)
            BBR: BB0171(lipB)
            RFR: Rfer_3935
            POL: Bpro_0314
            PNA: Pnap_0243
            AAV: Aave_0363
            AJS: Ajs_0299
            VEI: Veis_0471
            MPT: Mpe_A0315
            HAR: HEAR3002(lipB)
            NEU: NE1488(lipB)
            NET: Neut_0758
            NMU: Nmul_A1988
            EBA: ebA3048(lipB)
            AZO: azo0183(lipB)
            DAR: Daro_0288
            TBD: Tbd_0269
            MFA: Mfla_2500
            GSU: GSU2434(lipB)
            GME: Gmet_2747
            PCA: Pcar_0350
            PPD: Ppro_1031
            DVU: DVU0906(lipB)
            DVL: Dvul_2078
            DDE: Dde_2713
            BBA: Bd0766(lipB)
            DPS: DP0297(lipB)
            ADE: Adeh_1821
            MXA: MXAN_4215(lipB)
            SFU: Sfum_1675
            RPR: RP876(lipB)
            RTY: RT0867(lipB)
            RCO: RC1357(lipB)
            RFE: RF_1383(lipB)
            RBE: RBE_0052(lipB)
            WOL: WD1014(lipB)
            WBM: Wbm0235
            AMA: AM941(lipB)
            APH: APH_0243(lipB)
            ERU: Erum6360(lipB)
            ERW: ERWE_CDS_06670(lipB)
            ERG: ERGA_CDS_06580(lipB)
            ECN: Ecaj_0640
            ECH: ECH_0371(lipB)
            NSE: NSE_0100(lipB)
            PUB: SAR11_1090(rfaL)
            MLO: mlr1337
            MES: Meso_1045
            SME: SMc01268(lipB)
            ATU: Atu1556(lipB)
            ATC: AGR_C_2865
            RET: RHE_CH02223(lipB)
            RLE: RL2555(lipB)
            BME: BMEII0678
            BMF: BAB2_0651(lipB)
            BMS: BRA0589(lipB)
            BMB: BruAb2_0635(lipB)
            BJA: blr5257(lipB)
            BRA: BRADO3259(lipB)
            RPA: RPA3169(lipB)
            RPB: RPB_2371
            RPC: RPC_3348
            RPD: RPD_3083
            RPE: RPE_3436
            NWI: Nwi_1731(lipB)
            NHA: Nham_2163
            BHE: BH07850(lipB)
            BQU: BQ06600(lipB)
            BBK: BARBAKC583_0898(lipB)
            CCR: CC_2176
            SIL: SPO1389(lipB)
            SIT: TM1040_3088
            RSP: RSP_1878(lipB)
            RSH: Rsph17029_0528
            JAN: Jann_1252
            RDE: RD1_1970(lipB)
            PDE: Pden_1936
            MMR: Mmar10_1745
            HNE: HNE_1062(lipB)
            ZMO: ZMO1302(lipB)
            NAR: Saro_0094
            SAL: Sala_1350
            ELI: ELI_00410
            GOX: GOX0046
            GBE: GbCGDNIH1_0587
            RRU: Rru_A1996
            MAG: amb0721
            MGM: Mmc1_0528
            ABA: Acid345_4305
            SUS: Acid_0913
            TTE: TTE1673(lipB)
            MTU: Rv2217(lipB)
            MTC: MT2274(lipB)
            MBO: Mb2240(lipB)
            MBB: BCG_2233(lipB)
            MLE: ML0859(lipB)
            MPA: MAP1958(lipB)
            MAV: MAV_2271(lipB)
            MSM: MSMEG_4285(lipB)
            MUL: MUL_1344(lipB)
            MVA: Mvan_3581
            MMC: Mmcs_3315
            MKM: Mkms_3377
            MJL: Mjls_3326
            CGL: NCgl2127(lipB)
            CGB: cg2422(lipB)
            CEF: CE2099
            CDI: DIP1640(lipB)
            CJK: jk0706(lipB)
            NFA: nfa16870(lipB)
            RHA: RHA1_ro01153
            SCO: SCO2193(lipB)
            SMA: SAV6010(lipB)
            TWH: TWT463(lipB)
            TWS: TW302(lipB)
            LXX: Lxx10110(lipB)
            ART: Arth_1605
            AAU: AAur_1748(lipB)
            PAC: PPA0692
            TFU: Tfu_0992
            FRA: Francci3_2135
            FAL: FRAAL5156(lipB)
            ACE: Acel_0927
            SEN: SACE_1636(lipB)
            STP: Strop_3326
            RXY: Rxyl_2547
            LIL: LA1731(lipB)
            LIC: LIC12072(lipB)
            LBJ: LBJ_1236(lipB)
            LBL: LBL_1287(lipB)
            SYN: slr0994(lipB)
            SYW: SYNW0668(lipB)
            SYC: syc1750_c(lipB)
            SYF: Synpcc7942_2353
            SYD: Syncc9605_2012
            SYE: Syncc9902_0659
            SYG: sync_0607(lipB)
            CYA: CYA_1727(lipB)
            CYB: CYB_1921(lipB)
            TEL: tll0832
            GVI: gll4414
            ANA: alr3185
            AVA: Ava_3883(lipB)
            PMA: Pro0398(lipB)
            PMM: PMM0401(lipB)
            PMT: PMT0214(lipB)
            PMN: PMN2A_1736
            PMI: PMT9312_0397
            PMB: A9601_04521(lipB)
            PMC: P9515_04631(lipB)
            PMF: P9303_21401(lipB)
            PMG: P9301_04211(lipB)
            PME: NATL1_04531(lipB)
            TER: Tery_3184
            BTH: BT_1089
            BFR: BF2034
            BFS: BF2088
            PGI: PG1343(lipB)
            SRU: SRU_2551(lipB)
            CHU: CHU_0466(lipB)
            GFO: GFO_2925(lipB)
            DRA: DR_0764
            DGE: Dgeo_1741
            TTH: TTC1746
            TTJ: TTHA0240
            PTO: PTO1260
            PAI: PAE2651
            PCL: Pcal_1401
            PAS: Pars_1183
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.181
            ExPASy - ENZYME nomenclature database: 2.3.1.181
            ExplorEnz - The Enzyme Database: 2.3.1.181
            ERGO genome analysis and discovery system: 2.3.1.181
            BRENDA, the Enzyme Database: 2.3.1.181
///
ENTRY       EC 2.3.1.182                Enzyme
NAME        (R)-citramalate synthase;
            CimA
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than aminoacyl groups
REACTION    acetyl-CoA + pyruvate = CoA + (2R)-2-hydroxy-2-methylbutanedioate
SUBSTRATE   acetyl-CoA [CPD:C00024];
            pyruvate [CPD:C00022]
PRODUCT     CoA [CPD:C00010];
            (2R)-2-hydroxy-2-methylbutanedioate
COMMENT     One of the enzymes involved in a novel pyruvate pathway for
            isoleucine biosynthesis that is found in some, mainly archaeal,
            bacteria [1,2]. The enzyme can be inhibited by isoleucine, the
            end-product of the pathway, but not by leucine [2]. The enzyme is
            highly specific for pyruvate as substrate, as the 2-oxo acids
            3-methyl-2-oxobutanoate, 2-oxobutanoate, 4-methyl-2-oxopentanoate,
            2-oxohexanoate and 2-oxoglutarate cannot act as substrate [1,2].
REFERENCE   1  [PMID:9864346]
  AUTHORS   Howell DM, Xu H, White RH.
  TITLE     (R)-citramalate synthase in methanogenic archaea.
  JOURNAL   J. Bacteriol. 181 (1999) 331-3.
REFERENCE   2  [PMID:15292141]
  AUTHORS   Xu H, Zhang Y, Guo X, Ren S, Staempfli AA, Chiao J, Jiang W, Zhao G.
  TITLE     Isoleucine biosynthesis in Leptospira interrogans serotype lai
            strain 56601 proceeds via a threonine-independent pathway.
  JOURNAL   J. Bacteriol. 186 (2004) 5400-9.
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.1.182
            ExPASy - ENZYME nomenclature database: 2.3.1.182
            ExplorEnz - The Enzyme Database: 2.3.1.182
            ERGO genome analysis and discovery system: 2.3.1.182
            BRENDA, the Enzyme Database: 2.3.1.182
///
ENTRY       EC 2.3.1.-                  Enzyme
CLASS       Transferases;
            Acyltransferases;
            Transferring groups other than amino-acyl groups
REACTION    (1) L-Alanine + Acetyl-CoA <=> 2-Amino-4-oxopentanoic acid + CoA
            [RN:R00399];
            (2) L-Lysine + Acetyl-CoA <=> N6-Acetyl-L-lysine + CoA [RN:R00454];
            (3) 1H-Imidazole-4-ethanamine + Acetyl-CoA <=>
            4-(beta-Acetylaminoethyl)imidazole + CoA [RN:R02152];
            (4) (R)-3-Hydroxybutanoyl-CoA <=> Poly-beta-hydroxybutyrate
            [RN:R04254];
            (5) UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + Acyl-carrier
            protein <=> UDP-3-O-(3-hydroxytetradecanoyl)-D-glucosamine +
            (3R)-3-Hydroxytetradecanoyl-[acyl-carrier protein] [RN:R04550];
            (6) 4-Hydroxyphenylacetyl-CoA + Glycine <=>
            4-Hydroxyphenylacetylglycine + CoA [RN:R04777];
            (7) Di[3-deoxy-D-manno-octulosonyl]-lipid A + Acyl-carrier protein
            <=> Tetradecanoyl-[acp] + Lauroyl-KDO2-lipid IV(A) [RN:R05075];
            (8) Lauroyl-KDO2-lipid IV(A) + Acyl-carrier protein <=>
            Dodecanoyl-[acyl-carrier protein] +
            Di[3-deoxy-D-manno-octulosonyl]-lipid IV(A) [RN:R05146];
            (9) Benzoyl acetyl-CoA + CoA <=> S-Benzoate coenzyme A + Acetyl-CoA
            [RN:R05506];
            (10) 3-Oxopimeloyl-CoA + CoA <=> Glutaryl-CoA + Acetyl-CoA
            [RN:R05586];
            (11) Benzoylsuccinyl-CoA + CoA <=> S-Benzoate coenzyme A +
            Succinyl-CoA [RN:R05587];
            (12) Phenylacetyl-CoA + Glycine <=> Phenylacetylglycine + CoA
            [RN:R05841];
            (13) 2,6-Dimethyl-5-methylene-3-oxo-heptanoyl-CoA + CoA <=>
            3-Isopropylbut-3-enoyl-CoA + Propanoyl-CoA [RN:R06414];
            (14) Cyanidin 3-O-glucoside + p-Coumaroyl-CoA <=> Cyanidin
            3-O-(6-O-p-coumaroyl)glucoside + CoA [RN:R06544];
            (15) Cyanin + p-Coumaroyl-CoA <=> Cyanidin
            3-O-(6-O-p-coumaroyl)glucoside-5-O-glucoside + CoA [RN:R06545];
            (16) Tropine <=> Acetyltropine [RN:R06735];
            (17) Pseudotropine <=> Acetylpseudotropine [RN:R06736];
            (18) Naphthyl-2-oxomethyl-succinyl-CoA + CoA <=> 2-Naphthoyl-CoA +
            Succinyl-CoA [RN:R06908];
            (19) 1-(1-Alkenyl)-sn-glycero-3-phosphate + Acyl-CoA <=>
            2-Acyl-1-(1-alkenyl)-sn-glycero-3-phosphate + CoA [RN:R07382];
            (20) Glycosyl-4,4'-diaponeurosporenoate <=> Staphyloxanthin
            [RN:R07656];
            (21) Malonyl-CoA + Palmitoyl-CoA <=> 3-Oxostearoyl-CoA + CoA + CO2
            [RN:R07758];
            (22) Hexadecanoyl-[acp] + Malonyl-[acyl-carrier protein] <=>
            3-Oxostearoyl-[acp] + Acyl-carrier protein + CO2 [RN:R07762];
            (23) 3-Hydroxy-5-oxohexanoyl-CoA + CoA <=> (S)-3-Hydroxybutanoyl-CoA
            + Acetyl-CoA [RN:R07833];
            (24) Pelargonidin 3-O-glucoside + Caffeoyl-CoA <=> Pelargonidin
            3-O-(6-caffeoyl-beta-D-glucoside) + CoA [RN:R07873];
            (25) Pelargonin + Caffeoyl-CoA <=> Pelargonidin
            3-O-(6-caffeoyl-beta-D-glucoside) 5-O-beta-D-glucoside + CoA
            [RN:R07876];
            (26) Pelargonidin 3-O-(6-O-malonyl-beta-D-glucoside) + Malonyl-CoA
            <=> Pelargonidin 3-O-3'',6''-O-dimalonylglucoside + CoA [RN:R07884];
            (27) Cyanidin 3-O-(6-O-malonyl-beta-D-glucoside) + Malonyl-CoA <=>
            Cyanidin 3-O-3'',6''-O-dimalonylglucoside + CoA [RN:R07885];
            (28) Delphinidin 3-O-(6-O-malonyl-beta-D-glucoside) + Malonyl-CoA
            <=> Delphinidin 3-O-3'',6''-O-dimalonylglucoside + CoA [RN:R07886];
            (29) Albireodelphin <=> Gentiodelphin [RN:R07924];
            (30) Delphinidin 3-O-glucoside + Caffeoyl-CoA <=> Delphinidin
            3-O-(6-caffeoyl-beta-D-glucoside) + CoA [RN:R07926];
            (31) Pelargonidin 3-O-glucoside + p-Coumaroyl-CoA <=> Pelargonidin
            3-(6-p-coumaroyl)glucoside + CoA [RN:R07927];
            (32) Cyanidin 3-O-glucoside + Caffeoyl-CoA <=> Cyanidin
            3-(6-p-caffeoyl)glucoside + CoA [RN:R07928];
            (33) Delphinidin 3-O-glucoside + p-Coumaroyl-CoA <=> Delphinidin
            3-(6-p-coumaroyl)glucoside + CoA [RN:R07929]
SUBSTRATE   L-Alanine [CPD:C00041];
            Acetyl-CoA [CPD:C00024];
            L-Lysine [CPD:C00047];
            3-Methyl-2-oxobutanoic acid [CPD:C00141];
            Enzyme N6-(lipoyl)lysine [CPD:C15972];
            1H-Imidazole-4-ethanamine [CPD:C00388];
            2-Methylpropanoyl-CoA [CPD:C00630];
            Enzyme N6-(dihydrolipoyl)lysine [CPD:C15973];
            (S)-2-Methylbutanoyl-CoA [CPD:C15980];
            3-Methylbutanoyl-CoA [CPD:C02939];
            (R)-3-Hydroxybutanoyl-CoA [CPD:C03561];
            UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine [CPD:C04652];
            Acyl-carrier protein [CPD:C00229];
            4-Hydroxyphenylacetyl-CoA [CPD:C05338];
            Glycine [CPD:C00037];
            Di[3-deoxy-D-manno-octulosonyl]-lipid A [CPD:C06026];
            Lauroyl-KDO2-lipid IV(A) [CPD:C06251];
            Benzoyl acetyl-CoA [CPD:C07118];
            CoA [CPD:C00010];
            3-Oxopimeloyl-CoA [CPD:C06715];
            Benzoylsuccinyl-CoA [CPD:C09820];
            Phenylacetyl-CoA [CPD:C00582];
            2,6-Dimethyl-5-methylene-3-oxo-heptanoyl-CoA [CPD:C11948];
            Cyanidin 3-O-glucoside [CPD:C08604];
            p-Coumaroyl-CoA [CPD:C00223];
            Cyanin [CPD:C08639];
            Tropine [CPD:C00729];
            Pseudotropine [CPD:C02066];
            Naphthyl-2-oxomethyl-succinyl-CoA [CPD:C14119];
            1-(1-Alkenyl)-sn-glycero-3-phosphate [CPD:C15646];
            Acyl-CoA [CPD:C00040]
PRODUCT     2-Amino-4-oxopentanoic acid [CPD:C03341];
            CoA [CPD:C00010];
            N6-Acetyl-L-lysine [CPD:C02727];
            [Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]
            S-(2-methylpropanoyl)dihydrolipoyllysine [CPD:C15977];
            CO2 [CPD:C00011];
            4-(beta-Acetylaminoethyl)imidazole [CPD:C05135];
            [Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]
            S-(2-methylbutanoyl)dihydrolipoyllysine [CPD:C15979];
            [Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]
            S-(3-methylbutanoyl)dihydrolipoyllysine [CPD:C15975];
            Poly-beta-hydroxybutyrate [CPD:C06143];
            UDP-3-O-(3-hydroxytetradecanoyl)-D-glucosamine [CPD:C06022];
            (3R)-3-Hydroxytetradecanoyl-[acyl-carrier protein] [CPD:C04688];
            4-Hydroxyphenylacetylglycine [CPD:C05596];
            Tetradecanoyl-[acp] [CPD:C05761];
            Lauroyl-KDO2-lipid IV(A) [CPD:C06251];
            Dodecanoyl-[acyl-carrier protein] [CPD:C05223];
            Di[3-deoxy-D-manno-octulosonyl]-lipid IV(A) [CPD:C06025];
            S-Benzoate coenzyme A [CPD:C00512];
            Acetyl-CoA [CPD:C00024];
            Glutaryl-CoA [CPD:C00527];
            Succinyl-CoA [CPD:C00091];
            Phenylacetylglycine [CPD:C05598];
            3-Isopropylbut-3-enoyl-CoA [CPD:C11949];
            Propanoyl-CoA [CPD:C00100];
            Cyanidin 3-O-(6-O-p-coumaroyl)glucoside [CPD:C12095];
            Cyanidin 3-O-(6-O-p-coumaroyl)glucoside-5-O-glucoside [CPD:C12096];
            Acetyltropine [CPD:C12452];
            Acetylpseudotropine [CPD:C12453];
            2-Naphthoyl-CoA [CPD:C14120];
            2-Acyl-1-(1-alkenyl)-sn-glycero-3-phosphate [CPD:C15647]
///
ENTRY       EC 2.3.2.1                  Enzyme
NAME        D-glutamyltransferase;
            D-glutamyl transpeptidase;
            D-gamma-glutamyl transpeptidase
CLASS       Transferases;
            Acyltransferases;
            Aminoacyltransferases
SYSNAME     glutamine:D-glutamyl-peptide 5-glutamyltransferase
REACTION    L(or D)-glutamine + D-glutamyl-peptide = NH3 +
            5-glutamyl-D-glutamyl-peptide [RN:R04011 R04012]
ALL_REAC    R04011 R04012
SUBSTRATE   L-glutamine [CPD:C00064];
            D-glutamine [CPD:C00819];
            D-glutamyl-peptide [CPD:C02671]
PRODUCT     NH3 [CPD:C00014];
            5-glutamyl-D-glutamyl-peptide [CPD:C03933]
REFERENCE   1
  AUTHORS   Williams, W.J., Litwin, J. and Thorne, C.B.
  TITLE     Further studies on the biosynthesis of gamma-glutamyl peptides by
            transfer reactions.
  JOURNAL   J. Biol. Chem. 212 (1955) 427-438.
  ORGANISM  Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00471  D-Glutamine and D-glutamate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.2.1
            ExPASy - ENZYME nomenclature database: 2.3.2.1
            ExplorEnz - The Enzyme Database: 2.3.2.1
            ERGO genome analysis and discovery system: 2.3.2.1
            BRENDA, the Enzyme Database: 2.3.2.1
            CAS: 9030-02-8
///
ENTRY       EC 2.3.2.2                  Enzyme
NAME        gamma-glutamyltransferase;
            glutamyl transpeptidase;
            alpha-glutamyl transpeptidase;
            gamma-glutamyl peptidyltransferase;
            gamma-glutamyl transpeptidase;
            gamma-GPT;
            gamma-GT;
            gamma-GTP;
            L-gamma-glutamyl transpeptidase;
            L-gamma-glutamyltransferase;
            L-glutamyltransferase;
            GGT;
            gamma-glutamyltranspeptidase
CLASS       Transferases;
            Acyltransferases;
            Aminoacyltransferases
SYSNAME     (5-L-glutamyl)-peptide:amino-acid 5-glutamyltransferase
REACTION    (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl
            amino acid [RN:R04159]
ALL_REAC    R04159 > R01262 R01687 R04935;
            (other) R00494 R03867 R03916 R03970 R03971
SUBSTRATE   (5-L-glutamyl)-peptide [CPD:C03193];
            amino acid [CPD:C00045]
PRODUCT     peptide [CPD:C00012];
            5-L-glutamyl amino acid [CPD:C03363]
REFERENCE   1  [PMID:6030345]
  AUTHORS   Goore MY, Thompson JF.
  TITLE     Gamma-glutamyl transpeptidase from kidney bean fruit. I.
            Purification and mechanism of action.
  JOURNAL   Biochim. Biophys. Acta. 132 (1967) 15-26.
  ORGANISM  kidney bean
REFERENCE   2
  AUTHORS   Leibach, F.H. and Binkley, F.
  TITLE     gamma-Glutamyl transferase of swine kidney.
  JOURNAL   Arch. Biochem. Biophys. 127 (1968) 292-301.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00430  Taurine and hypotaurine metabolism
            PATH: map00450  Selenoamino acid metabolism
            PATH: map00460  Cyanoamino acid metabolism
            PATH: map00480  Glutathione metabolism
            PATH: map00590  Arachidonic acid metabolism
ORTHOLOGY   KO: K00681  gamma-glutamyltranspeptidase
GENES       HSA: 2678(GGT1) 2686(GGTL3) 91227(GGTL4)
            PTR: 458194(GGTL3) 458711(GGTLA1) 470168(GGT1)
            MMU: 14598(Ggt1) 207182(Ggtl3) 23887(Ggtla1)
            RNO: 116568(Ggt1) 156275(Ggtl3) 29566(Ggtla1)
            CFA: 485847(GGTL3) 486400(GGT1) 486401(GGTLA1)
            BTA: 615582(LOC615582)
            SSC: 397095(GGT1)
            GGA: 416943(GGTLA1) 416945(GGT1) 419121(GGTL3)
            XLA: 444291(MGC80945)
            XTR: 448376(ggt1)
            DRE: 566746(LOC566746) 569014(LOC569014)
            SPU: 583278(LOC583278) 585045(LOC585045) 586229(LOC586229)
                 592729(LOC592729)
            DME: Dmel_CG1492 Dmel_CG6461
            CEL: C53D5.5(gamma-glutamyltranspeptidase)
                 T03D8.6(Gamma-glutamyltranspeptidase)
                 Y7A9A.1(gamma-glutamyltranspeptidase)
            ATH: AT4G39640(GGT1)
            OSA: 4324526 4336033
            CME: CMM265C CMQ101C
            SCE: YLR299W(ECM38)
            AGO: AGOS_AAR144W
            PIC: PICST_58626(EMC37) PICST_78698(EMC38)
            CAL: CaO19_13474(CaO19.13474)
            CGR: CAGL0I00506g
            SPO: SPAC56E4.06c SPAC664.09
            ANI: AN3767.2 AN5658.2
            AFM: AFUA_4G13580 AFUA_7G04760
            AOR: AO090005000169 AO090009000211 AO090023000537 AO090113000029
            CNE: CND01560 CNG04350
            UMA: UM02291.1
            ECU: ECU05_1240
            ECO: b3447(ggt)
            ECJ: JW3412(ggt)
            ECE: Z4813(ggt)
            ECS: ECs4293
            ECC: c4236(ggt)
            ECI: UTI89_C3954(ggt)
            ECP: ECP_3540
            ECV: APECO1_3012(ggt)
            ECW: EcE24377A_3924(ggt)
            ECX: EcHS_A3644(ggt)
            STY: STY4260(ggt)
            STT: t3970(ggt)
            SPT: SPA3403(ggt)
            SEC: SC3480(ggt)
            STM: STM3551(ggt)
            YPK: y0985(ggt)
            YPA: YPA_2691
            YPN: YPN_0891 YPN_0892
            YPP: YPDSF_2831
            YPS: YPTB0924(ggt)
            YPI: YpsIP31758_3128(ggt)
            YEN: YE3175(ggt)
            SFL: SF3464(ggt)
            SFX: S4298(ggt)
            SFV: SFV_3450(ggt)
            SSN: SSON_3685(ggt)
            SBO: SBO_3443(ggt)
            SDY: SDY_3595(ggt)
            ECA: ECA3497 ECA4379(ggt)
            PLU: plu3908(ggt)
            ENT: Ent638_0756 Ent638_3850
            SPE: Spro_0930 Spro_1057 Spro_2484
            ASU: Asuc_1161
            XFA: XF0984
            XFT: PD0278(ggt)
            XCC: XCC0291(ggt) XCC2388(ggt) XCC3322(ggt)
            XCB: XC_0301 XC_0842 XC_1726
            XCV: XCV0314(ggt1) XCV2706(ggt2) XCV3578
            XAC: XAC0305(ggt) XAC2523(ggt) XAC3450(ggt)
            XOO: XOO2505(ggt)
            XOM: XOO_2369(XOO2369)
            VCH: VC0194 VCA0558
            VCO: VC0395_A2574(ggt)
            VPA: VP3011
            VFI: VFA0086
            PPR: PBPRA3512
            PAE: PA0164 PA0361 PA1338(ggt)
            PAU: PA14_02050 PA14_04730 PA14_46960(ggt)
            PAP: PSPA7_0455(ggt2) PSPA7_4047(ggt1)
            PPU: PP_3535(ggt-1) PP_4659(ggt-2)
            PPF: Pput_2238 Pput_4521
            PST: PSPTO_0787(ggt)
            PSB: Psyr_0691 Psyr_2681
            PSP: PSPPH_0701(ggt) PSPPH_2783(ggtA)
            PFL: PFL_0771(ggt) PFL_5184(ggt)
            PFO: Pfl_3565 Pfl_4764
            PEN: PSEEN0288 PSEEN0716(ggt)
            PMY: Pmen_3832 Pmen_4193
            PAR: Psyc_1176(ggt)
            PCR: Pcryo_1221
            PRW: PsycPRwf_1373
            ACI: ACIAD0485 ACIAD0929(ggt)
            SON: SO_0741(ggt-1) SO_1952(ggt-2)
            SDN: Sden_1655
            SFR: Sfri_2330
            SAZ: Sama_0669 Sama_1566
            SBL: Sbal_0604 Sbal_2620
            SBM: Shew185_2658 Shew185_3690
            SLO: Shew_2158
            SPC: Sputcn32_1667 Sputcn32_3224
            SSE: Ssed_0948 Ssed_2689
            SPL: Spea_1864
            SHE: Shewmr4_2297 Shewmr4_3344
            SHM: Shewmr7_0609 Shewmr7_2369
            SHN: Shewana3_2487 Shewana3_3514
            SHW: Sputw3181_0717 Sputw3181_2358
            ILO: IL0716(ggt_1) IL0739(ggt_2)
            CPS: CPS_2150(ggt1) CPS_4931(ggt2)
            PHA: PSHAa1566
            PAT: Patl_1885 Patl_2054 Patl_3459
            SDE: Sde_1303
            PIN: Ping_2396 Ping_2425
            MAQ: Maqu_1019
            LPN: lpg0549
            LPF: lpl0591
            LPP: lpp0610
            MCA: MCA2148(ggt)
            FTU: FTT1181c(ggt)
            FTF: FTF1181c(ggt)
            FTW: FTW_1228(ggt)
            FTL: FTL_0766
            FTH: FTH_0767(ggt)
            FTA: FTA_0809(ggt)
            FTN: FTN_1159(ggt)
            TCX: Tcr_1413 Tcr_1715
            NOC: Noc_0769
            AEH: Mlg_0917 Mlg_2047 Mlg_2514 Mlg_2654
            HCH: HCH_06798(ggt)
            CSA: Csal_1740 Csal_2329
            ABO: ABO_0080(ggt)
            MMW: Mmwyl1_0452 Mmwyl1_0916
            AHA: AHA_3049
            NME: NMB1057
            NMA: NMA1255(ggt)
            NMC: NMC1018(ggt)
            CVI: CV_1415(ggt)
            RSO: RSc2501(RS01094) RSc2921(ggt2) RSp0274(ggt1)
            REU: Reut_A0841 Reut_A1005 Reut_B3965
            REH: H16_A0784(ggt2a) H16_A1098 H16_A2780(ggt2b) H16_B0984(ggt2c)
            RME: Rmet_0822 Rmet_0970 Rmet_1957 Rmet_4046
            BMA: BMA0245(ggt-1) BMA3237(ggt-2) BMAA0996(ggt)
            BMV: BMASAVP1_0371(ggt) BMASAVP1_A0214(ggt-2)
                 BMASAVP1_A2701(ggt-1)
            BML: BMA10299_0268(ggt) BMA10299_A1379(ggt-2)
                 BMA10299_A2376(ggt-1)
            BMN: BMA10247_2457(ggt-1) BMA10247_2806(ggt-2) BMA10247_A1328(ggt)
            BXE: Bxe_A0644 Bxe_A1308 Bxe_B0629 Bxe_B1050
            BVI: Bcep1808_2785 Bcep1808_2978 Bcep1808_4747 Bcep1808_5154
                 Bcep1808_5277
            BUR: Bcep18194_A6001 Bcep18194_A6223 Bcep18194_B0996
                 Bcep18194_B1850 Bcep18194_C6623
            BCN: Bcen_2062 Bcen_2267 Bcen_3613 Bcen_4185 Bcen_5852
            BCH: Bcen2424_2673 Bcen2424_2882 Bcen2424_4181 Bcen2424_4754
                 Bcen2424_6219
            BAM: Bamb_2726 Bamb_2936 Bamb_3593 Bamb_4137 Bamb_5982
            BPS: BPSL0416 BPSL0692 BPSS1288
            BPM: BURPS1710b_0630(ggt-2) BURPS1710b_0911(ggt-1)
                 BURPS1710b_A0297(ggt)
            BPL: BURPS1106A_0467(ggt) BURPS1106A_A1739(ggt)
            BPD: BURPS668_0447(ggt) BURPS668_A1823(ggt)
            BTE: BTH_I0389 BTH_I0604 BTH_II1134(ggt)
            PNU: Pnuc_0445 Pnuc_1163
            BPE: BP0252(ggt) BP2693 BP3052 BP3107
            BPA: BPP0885(ggt) BPP1442 BPP2201 BPP3529 BPP3615(ggt) BPP3778
            BBR: BB0978(ggt) BB1598 BB2516 BB3964 BB4050(ggt) BB4223 BB4243
            RFR: Rfer_3386
            POL: Bpro_1819 Bpro_3094 Bpro_3878
            PNA: Pnap_1607
            AAV: Aave_0589 Aave_1114 Aave_1410 Aave_2313 Aave_3307
            AJS: Ajs_1042 Ajs_4154
            VEI: Veis_0623 Veis_1932 Veis_3445 Veis_3531 Veis_4194
            MPT: Mpe_A3041 Mpe_A3055
            HAR: HEAR0614 HEAR2460 HEAR2479(ggt) HEAR2674
            MMS: mma_0581(ggt1) mma_0601(ggt2) mma_2541(ggt3) mma_2574(ggt4)
                 mma_2912(ggt5) mma_2915(ggt6)
            NEU: NE1331(ggt2)
            NET: Neut_1843
            EBA: ebA2869(ggt)
            AZO: azo1475(ggt)
            TBD: Tbd_1410
            HPY: HP1118(ggt)
            HPJ: jhp1046(ggt)
            HPA: HPAG1_1056
            HAC: Hac_0598(ggt)
            CJJ: CJJ81176_0067(ggt)
            CJD: JJD26997_0042(ggt)
            ABU: Abu_0961(ggt)
            DDE: Dde_1641
            BBA: Bd3478(ggt)
            ADE: Adeh_3957
            AFW: Anae109_0464
            MXA: MXAN_1383(ggt)
            MLO: mll6984 mlr5711
            MES: Meso_1044 Meso_1509
            PLA: Plav_0310 Plav_1569
            SME: SMb20585(ggt)
            SMD: Smed_4199
            ATU: Atu4722(ggt) Atu5507(ggt)
            ATC: AGR_L_319 AGR_pAT_750
            RET: RHE_CH02146(ggt1) RHE_CH03536(ggt2)
            RLE: RL4050(ggt) RL4578(ggt) pRL120335
            OAN: Oant_4407
            BJA: bll2872(ggt) bll8231 blr0583(ggt) blr2404(ggt) blr7156(ggt)
            BRA: BRADO0336(ggt) BRADO1399 BRADO1534 BRADO1881 BRADO2507
            BBT: BBta_0321(ggt) BBta_2197 BBta_2852 BBta_6509 BBta_6704
                 BBta_7627
            RPA: RPA0025(ggt1) RPA0776 RPA2331(ggt2) RPA4419(ggt3)
            RPB: RPB_0082 RPB_4227 RPB_4650
            RPC: RPC_0021 RPC_1352 RPC_2965
            RPD: RPD_0722 RPD_0763 RPD_2474 RPD_4079
            RPE: RPE_0024 RPE_1368
            NWI: Nwi_0161
            NHA: Nham_0191
            XAU: Xaut_0189
            CCR: CC_0104 CC_0531 CC_0984
            SIL: SPO0633(ggt) SPO0866 SPO3411
            SIT: TM1040_0064 TM1040_0482 TM1040_3598
            RSP: RSP_1499 RSP_3272(ggt)
            RSH: Rsph17029_0149 Rsph17029_4005
            RSQ: Rsph17025_2904
            JAN: Jann_2637 Jann_4054
            RDE: RD1_0028(ggtA) RD1_2179(ggtA) RD1_3436(ggt)
            PDE: Pden_0660
            MMR: Mmar10_0462
            HNE: HNE_2791(ggt1) HNE_3148(ggt2)
            ZMO: ZMO1388(ggt)
            NAR: Saro_0192
            SAL: Sala_0681 Sala_1982
            SWI: Swit_1433 Swit_2655 Swit_4426
            ELI: ELI_12820
            GOX: GOX0521 GOX0605 GOX1295 GOX1532
            GBE: GbCGDNIH1_0379 GbCGDNIH1_0974 GbCGDNIH1_1117
            ACR: Acry_2749
            RRU: Rru_A0385 Rru_A1349 Rru_A2424 Rru_A3318
            MAG: amb4309
            ABA: Acid345_1464 Acid345_3078 Acid345_4599
            SUS: Acid_2807 Acid_3929 Acid_4698 Acid_6385
            BSU: BG11838(ggt) BG12523(ywrD)
            BHA: BH0867
            BAR: GBAA_pXO2_0063(ggt)
            BAA: BXB0063(ggt)
            BLI: BL02481(ywrD) BL03798(ggt)
            BLD: BLi01364(ggt) BLi03850(ywrD)
            BCL: ABC1262
            BAY: RBAM_018540(ggt)
            BPU: BPUM_1164(ggt)
            OIH: OB0203 OB1303 OB3267
            GKA: GK3338
            SAU: SA0202
            SAV: SAV0209
            SAM: MW0185
            SAR: SAR0202
            SAS: SAS0185
            SAC: SACOL0188(ggt)
            SAB: SAB0148
            SAA: SAUSA300_0204(ggt)
            SAO: SAOUHSC_00171
            SAJ: SaurJH9_0194
            SAH: SaurJH1_0200
            SEP: SE2089
            SER: SERP2103(dep)
            SHA: SH0535
            SSP: SSP0352
            STH: STH3166
            AMT: Amet_0676 Amet_3745
            DSY: DSY2708
            MTU: Rv0773c(ggtA) Rv2394(ggtB)
            MTC: MT0797(ggt-1) MT2464(ggt-2)
            MBO: Mb0796c(ggtA) Mb2415(ggtB)
            MBB: BCG_0825c(ggtA) BCG_2408(ggtB)
            MPA: MAP0607c(ggtA)
            MAV: MAV_0717(ggt)
            MSM: MSMEG_0184 MSMEG_1463 MSMEG_1615(ggt) MSMEG_3076(ggt)
            MVA: Mvan_1330
            MGI: Mflv_3716
            MMC: Mmcs_0872 Mmcs_2394
            MKM: Mkms_0889 Mkms_2441
            MJL: Mjls_0878 Mjls_2435
            CGL: NCgl0916(cgl0954)
            CGB: cg1090(ggtB)
            CEF: CE1029
            NFA: nfa35970(ggt)
            RHA: RHA1_ro04237 RHA1_ro04377
            SCO: SCO5945(SC7H1.15) SCO6407(SC3C8.26) SCO6444(SC9B5.11)
            SMA: SAV1938(ggt1) SAV1957(ggt2)
            ART: Arth_0896 Arth_2007
            AAU: AAur_3482(ggt)
            NCA: Noca_4279
            KRA: Krad_0148
            SEN: SACE_0096(ggt1) SACE_2111(ggt2)
            STP: Strop_2446
            RXY: Rxyl_0295 Rxyl_1269
            FNU: FN0876 FN0941
            LIL: LA2105
            LIC: LIC11813(ggt)
            LBJ: LBJ_1904(ggt)
            LBL: LBL_1380(ggt)
            SYN: slr1269(ggt)
            SYW: SYNW1394
            SYC: syc1325_c(ggt)
            SYF: Synpcc7942_0185 Synpcc7942_B2624
            SYD: Syncc9605_1559
            SYE: Syncc9902_0798
            SYR: SynRCC307_1652(ggt)
            SYX: SynWH7803_0866(ggt)
            CYA: CYA_2484(ggt)
            CYB: CYB_2091(ggt)
            GVI: gll0680 gll3004(ggt) glr2359(ggt)
            ANA: alr2051
            AVA: Ava_3091
            PMA: Pro1522(ggt)
            TER: Tery_0909 Tery_2633
            SRU: SRU_0895(ggt) SRU_2660(ggt)
            GFO: GFO_1955(ggt)
            FJO: Fjoh_4506
            FPS: FP1721(ggt)
            RRS: RoseRS_2169 RoseRS_3730
            RCA: Rcas_1448 Rcas_1497
            DRA: DR_1524
            DGE: Dgeo_1141
            TTH: TTC0403
            TTJ: TTHA0755
            HWA: HQ1488A(ggt)
            NPH: NP1844A(ggt)
            TAC: Ta0994
            TVO: TVN0893
            PTO: PTO1185
            APE: APE_0137
            SMR: Smar_1215
            SSO: SSO3216
            STO: ST2355
            SAI: Saci_0425
            MSE: Msed_0243
            PAI: PAE3371
            PIS: Pisl_0601
            PCL: Pcal_1718
            PAS: Pars_1773
STRUCTURES  PDB: 2DBU  2DBW  2DBX  2DG5  2E0W  2E0X  2E0Y  2NQO  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.2.2
            ExPASy - ENZYME nomenclature database: 2.3.2.2
            ExplorEnz - The Enzyme Database: 2.3.2.2
            ERGO genome analysis and discovery system: 2.3.2.2
            BRENDA, the Enzyme Database: 2.3.2.2
            CAS: 9046-27-9
///
ENTRY       EC 2.3.2.3                  Enzyme
NAME        lysyltransferase
CLASS       Transferases;
            Acyltransferases;
            Aminoacyltransferases
SYSNAME     L-lysyl-tRNA:phosphatidylglycerol 3-O-lysyltransferase
REACTION    L-lysyl-tRNA + phosphatidylglycerol = tRNA +
            3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol [RN:R03771]
ALL_REAC    R03771
SUBSTRATE   L-lysyl-tRNA [CPD:C01931];
            phosphatidylglycerol [CPD:C00344]
PRODUCT     tRNA [CPD:C00066];
            3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol [CPD:C04482]
REFERENCE   1  [PMID:6049461]
  AUTHORS   Lennarz WJ, Bonsen PP, van Deenen LL.
  TITLE     Substrate specificity of O-L-lysylphosphatidylglycerol synthetase.
            Enzymatic studies on the structure of O-L-lysylphosphatidylglycerol.
  JOURNAL   Biochemistry. 6 (1967) 2307-12.
  ORGANISM  Staphylococcus aureus
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.2.3
            ExPASy - ENZYME nomenclature database: 2.3.2.3
            ExplorEnz - The Enzyme Database: 2.3.2.3
            ERGO genome analysis and discovery system: 2.3.2.3
            BRENDA, the Enzyme Database: 2.3.2.3
            CAS: 37257-20-8
///
ENTRY       EC 2.3.2.4                  Enzyme
NAME        gamma-glutamylcyclotransferase;
            gamma-glutamyl-amino acid cyclotransferase;
            gamma-L-glutamylcyclotransferase;
            L-glutamic cyclase
CLASS       Transferases;
            Acyltransferases;
            Aminoacyltransferases
SYSNAME     (5-L-glutamyl)-L-amino-acid 5-glutamyltransferase (cyclizing)
REACTION    (5-L-glutamyl)-L-amino acid = 5-oxoproline + L-amino acid
            [RN:R03749]
ALL_REAC    R03749 > R02743
SUBSTRATE   (5-L-glutamyl)-L-amino acid [CPD:C03740]
PRODUCT     5-oxoproline [CPD:C01879];
            L-amino acid [CPD:C00151]
COMMENT     The enzyme acts on derivatives of L-glutamate, L-2-aminobutanoate,
            L-alanine and glycine.
REFERENCE   1
  AUTHORS   Bodnaryk, R.P. and McGirr, L.
  TITLE     Purification, properties and function of a unique gamma-glutamyl
            cyclotransferase from the housefly, Musca domestica L.
  JOURNAL   Biochim. Biophys. Acta 315 (1973) 352-362.
  ORGANISM  Musca domestica
REFERENCE   2
  AUTHORS   Orlowski, M., Richman, P.G. and Meister, A.
  TITLE     Isolation and properties of gamma-L-glutamylcyclotransferase from
            human brain.
  JOURNAL   Biochemistry 8 (1969) 1048-1055.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00480  Glutathione metabolism
ORTHOLOGY   KO: K00682  gamma-glutamylcyclotransferase
STRUCTURES  PDB: 2PN7  2RBH  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.2.4
            ExPASy - ENZYME nomenclature database: 2.3.2.4
            ExplorEnz - The Enzyme Database: 2.3.2.4
            ERGO genome analysis and discovery system: 2.3.2.4
            BRENDA, the Enzyme Database: 2.3.2.4
            CAS: 9045-44-7
///
ENTRY       EC 2.3.2.5                  Enzyme
NAME        glutaminyl-peptide cyclotransferase;
            glutaminyl-tRNA cyclotransferase;
            glutaminyl cyclase;
            glutaminyl-transfer ribonucleate cyclotransferase
CLASS       Transferases;
            Acyltransferases;
            Aminoacyltransferases
SYSNAME     L-glutaminyl-peptide gamma-glutamyltransferase (cyclizing)
REACTION    L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH3 [RN:R04058]
ALL_REAC    R04058
SUBSTRATE   L-glutaminyl-peptide [CPD:C02986]
PRODUCT     5-oxoprolyl-peptide [CPD:C02805];
            NH3 [CPD:C00014]
COMMENT     Involved in the formation of thyrotropin-releasing hormone and other
            biologically active peptides containing N-terminal pyroglutamyl
            residues. The enzyme from papaya also acts on glutaminyl-tRNA.
REFERENCE   1  [PMID:3597387]
  AUTHORS   Busby WH Jr, Quackenbush GE, Humm J, Youngblood WW, Kizer JS.
  TITLE     An enzyme(s) that converts glutaminyl-peptides into
            pyroglutamyl-peptides. Presence in pituitary, brain, adrenal
            medulla, and lymphocytes.
  JOURNAL   J. Biol. Chem. 262 (1987) 8532-6.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:3473473]
  AUTHORS   Fischer WH, Spiess J.
  TITLE     Identification of a mammalian glutaminyl cyclase converting
            glutaminyl into pyroglutamyl peptides.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 3628-32.
  ORGANISM  cow [GN:bta]
REFERENCE   3
  AUTHORS   Messer, M. and Ottesen, M.
  TITLE     Isolation and properties of glutamine cyclotransferase of dried
            papaya latex.
  JOURNAL   C.R. Trav. Lab. Carlsberg 35 (1965) 1-24.
  ORGANISM  papaya
ORTHOLOGY   KO: K00683  glutaminyl-peptide cyclotransferase
GENES       HSA: 25797(QPCT)
            MMU: 70536(Qpct)
            RNO: 313837(RGD1562284_predicted)
            CFA: 403861(QPCT)
            BTA: 281437(QPCT)
            GGA: 421479(QPCT)
            XLA: 447416(MGC84238)
            DME: Dmel_CG5976
            CGR: CAGL0K10406g
            AOR: AO090701000860
            DDI: DDBDRAFT_0219916
            TBR: Tb927.7.6940
            YPN: YPN_0089
            YPI: YpsIP31758_0172
            XCC: XCC2216
            XCB: XC_1901
            XCV: XCV2519
            XAC: XAC2320
            XOO: XOO2159
            XOM: XOO_2028(XOO2028)
            MMR: Mmar10_1722
            SUS: Acid_7734
            SPZ: M5005_Spy_0416
            SPH: MGAS10270_Spy0417
            SPI: MGAS10750_Spy0429
            SPJ: MGAS2096_Spy0435
            SPK: MGAS9429_Spy0415
            SPA: M6_Spy0443
            SPB: M28_Spy0404
            CGB: cg0940
            SEN: SACE_0597
            GFO: GFO_2260
            DGE: Dgeo_1980
STRUCTURES  PDB: 2AFM  2AFO  2AFS  2AFU  2AFW  2AFX  2AFZ  2IWA  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.2.5
            ExPASy - ENZYME nomenclature database: 2.3.2.5
            ExplorEnz - The Enzyme Database: 2.3.2.5
            ERGO genome analysis and discovery system: 2.3.2.5
            BRENDA, the Enzyme Database: 2.3.2.5
            CAS: 37257-21-9
///
ENTRY       EC 2.3.2.6                  Enzyme
NAME        leucyltransferase;
            leucyl, phenylalanine-tRNA-protein transferase;
            leucyl-phenylalanine-transfer ribonucleate-protein
            aminoacyltransferase;
            leucyl-phenylalanine-transfer ribonucleate-protein transferase
CLASS       Transferases;
            Acyltransferases;
            Aminoacyltransferases
SYSNAME     L-leucyl-tRNA:protein leucyltransferase
REACTION    L-leucyl-tRNA + protein = tRNA + L-leucyl-protein [RN:R03813]
ALL_REAC    R03813
SUBSTRATE   L-leucyl-tRNA [CPD:C02047];
            protein [CPD:C00017]
PRODUCT     tRNA [CPD:C00066];
            L-leucyl-protein [CPD:C02429]
COMMENT     Also transfers phenylalanyl groups. Requires a univalent cation.
            Peptides and proteins containing an N-terminal arginine, lysine or
            histidine residue can act as acceptors.
REFERENCE   1  [PMID:4894363]
  AUTHORS   Leibowitz MJ, Soffer RL.
  TITLE     A soluble enzyme from Escherichia coli which catalyzes the transfer
            of leucine and phenylalanine from tRNA to acceptor proteins.
  JOURNAL   Biochem. Biophys. Res. Commun. 36 (1969) 47-53.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4909560]
  AUTHORS   Leibowitz MJ, Soffer RL.
  TITLE     Enzymatic modification of proteins. 3. Purification and properties
            of a leucyl, phenylalanyl transfer ribonucleic acid protein
            transferase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 245 (1970) 2066-73.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4587124]
  AUTHORS   Soffer RL.
  TITLE     Peptide acceptors in the leucine, phenylalanine transfer reaction.
  JOURNAL   J. Biol. Chem. 248 (1973) 8424-8.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K00684  leucyl/phenylalanyl-tRNA--protein transferase
GENES       ECO: b0885(aat)
            ECJ: JW0868(aat)
            ECE: Z1229(aat)
            ECS: ECs0970
            ECC: c1022(aat)
            ECI: UTI89_C0900(aat)
            ECP: ECP_0899
            ECV: APECO1_1204(aat)
            ECW: EcE24377A_0958(aat)
            STY: STY0953(aat)
            STT: t1979(aat)
            SPT: SPA1843(aat)
            SEC: SC0909(aat)
            STM: STM0955(aat)
            YPE: YPO1371(aat)
            YPK: y2806(aat)
            YPM: YP_1222(aat1)
            YPA: YPA_0661
            YPN: YPN_2609
            YPP: YPDSF_2324
            YPS: YPTB1396(aat)
            YPI: YpsIP31758_2603(aat)
            YEN: YE1520(aat)
            SFL: SF0844(aat)
            SFX: S0885(aat)
            SFV: SFV_0876(aat)
            SSN: SSON_0886(aat)
            SBO: SBO_0818(aat)
            SDY: SDY_2376(aat)
            ECA: ECA2652(aat)
            PLU: plu1596(aat)
            ENT: Ent638_1409
            SPE: Spro_1676
            XFA: XF1446
            XFT: PD0667(aat)
            XCC: XCC1969(aat)
            XCB: XC_2216
            XCV: XCV2052(aat)
            XAC: XAC2003(aat)
            XOO: XOO2551(aat)
            XOM: XOO_2410(XOO2410)
            VCH: VC1735
            VVU: VV1_3222
            VPA: VP1018
            VFI: VF1762
            PPR: PBPRA1155
            PAE: PA2617(aat)
            PAU: PA14_30270(aat)
            PAP: PSPA7_2590(aat)
            PPU: PP_4005(aat)
            PPF: Pput_1828
            PST: PSPTO_3350(aat)
            PSB: Psyr_3180(aat)
            PSP: PSPPH_3094(aat)
            PFL: PFL_3882(aat)
            PFO: Pfl_3587(aat)
            PEN: PSEEN2210(aat)
            PMY: Pmen_2390
            PAR: Psyc_0387
            PCR: Pcryo_0428
            PRW: PsycPRwf_0618
            ACI: ACIAD0889(aat)
            SON: SO_2623(aat)
            SDN: Sden_1837
            SFR: Sfri_2251
            SAZ: Sama_2053
            SBL: Sbal_2469
            SBM: Shew185_2462
            SLO: Shew_1569
            SPC: Sputcn32_2224
            SSE: Ssed_1889
            SPL: Spea_2529
            SHE: Shewmr4_1651
            SHM: Shewmr7_1726
            SHN: Shewana3_2418
            SHW: Sputw3181_1785
            ILO: IL0671(aat)
            CPS: CPS_2763(aat)
            PHA: PSHAa1721(aat)
            PAT: Patl_2371
            SDE: Sde_1691
            PIN: Ping_2258
            LPN: lpg1768(aat)
            LPF: lpl1732(aat)
            LPP: lpp1732(aat)
            MCA: MCA1792(aat)
            TCX: Tcr_1114
            NOC: Noc_2596
            AEH: Mlg_1713
            HHA: Hhal_1397
            HCH: HCH_02343(aat)
            CSA: Csal_2437
            MMW: Mmwyl1_3258
            AHA: AHA_1860(aat)
            NME: NMB0206
            NMA: NMA0063(aat)
            NGO: NGO1778(aat)
            CVI: CV_1798(aat)
            RSO: RSc1617(aat)
            REU: Reut_A1319(aat)
            REH: H16_A1403(aat)
            RME: Rmet_1216
            BMA: BMA1251(aat)
            BXE: Bxe_A2505
            BVI: Bcep1808_1520
            BUR: Bcep18194_A4698(aat)
            BCN: Bcen_1076
            BCH: Bcen2424_1556
            BAM: Bamb_1457
            BPS: BPSL1864
            BPM: BURPS1710b_1980(aat)
            BTE: BTH_I2509
            PNU: Pnuc_0743
            BPA: BPP3538(aat)
            BBR: BB3973(aat)
            RFR: Rfer_2349
            POL: Bpro_2326
            PNA: Pnap_1725
            AAV: Aave_3104
            AJS: Ajs_1988
            VEI: Veis_3622
            MPT: Mpe_A1469
            HAR: HEAR2442(aat)
            MMS: mma_2511
            NEU: NE2219(aat)
            NET: Neut_0648
            NMU: Nmul_A2709
            EBA: ebA4891(aat)
            AZO: azo2208(aat)
            DAR: Daro_1196
            TBD: Tbd_2043(aat)
            MFA: Mfla_0932 Mfla_1076
            WSU: WS0338
            TDN: Tmden_0456
            CJE: Cj1109(aat)
            CJR: CJE1252(aat)
            CJU: C8J_1050(aat)
            CFF: CFF8240_0707(aat)
            ABU: Abu_1095(aat)
            NIS: NIS_0381(aat)
            SUN: SUN_2064(aat)
            PCA: Pcar_2259
            DVU: DVU1603(aat)
            DVL: Dvul_1531
            DDE: Dde_2098
            LIP: LI0619(aat)
            BBA: Bd0990(aat)
            DPS: DP1903
            ADE: Adeh_0792
            AFW: Anae109_0837
            MXA: MXAN_1311(aat)
            SAT: SYN_02379
            SFU: Sfum_0044
            MLO: mll0202
            MES: Meso_1717
            PLA: Plav_3294
            SME: SMc01346(aat)
            SMD: Smed_0951
            ATU: Atu1329(aat)
            ATC: AGR_C_2449
            RET: RHE_CH01868(aat)
            RLE: RL2087(aat)
            BME: BMEI1064
            BMF: BAB1_0923(aat)
            BMS: BR0905(aat)
            BMB: BruAb1_0916(aat)
            OAN: Oant_2275
            BJA: bll4286(aat)
            BRA: BRADO3496(aat)
            BBT: BBta_4220(aat)
            RPA: RPA2429(aat)
            RPB: RPB_3025
            RPC: RPC_2875 RPC_2882
            RPD: RPD_2425
            RPE: RPE_2994
            NWI: Nwi_1757
            NHA: Nham_2193
            XAU: Xaut_3496
            CCR: CC_1885
            SIL: SPO1009(aat)
            SIT: TM1040_1519
            RSP: RSP_0192(aat)
            RSH: Rsph17029_1825
            RSQ: Rsph17025_1453
            JAN: Jann_2717
            RDE: RD1_2852(aat)
            PDE: Pden_1270
            MMR: Mmar10_1264
            HNE: HNE_2251(aat)
            ZMO: ZMO0927(aat)
            NAR: Saro_0826
            SAL: Sala_2292
            SWI: Swit_2552
            ELI: ELI_11120
            GOX: GOX1657
            GBE: GbCGDNIH1_1956
            ACR: Acry_0682
            RRU: Rru_A2436
            MAG: amb2740
            MGM: Mmc1_3260
            CTH: Cthe_1218
            CBE: Cbei_2567
            PAC: PPA2221
            NCA: Noca_0154
            FRA: Francci3_3741
            FAL: FRAAL5973(aat)
            KRA: Krad_3260
            RXY: Rxyl_1076
            TDE: TDE2125(aat)
            LIL: LA0108(aat)
            LIC: LIC10096(aat)
            LBJ: LBJ_0088(aat)
            LBL: LBL_0048(aat)
            SYN: sll0869(aat)
            SYC: syc0918_d(aat)
            SYF: Synpcc7942_0606
            TEL: tlr0861(aat)
            GVI: glr1034
            ANA: all3967
            AVA: Ava_1734(aat)
            TER: Tery_3272
            GFO: GFO_3042(aat)
            FJO: Fjoh_1595
            FPS: FP2352(aat)
            CTE: CT0346(aat)
            CPH: Cpha266_0677
            PVI: Cvib_0504
            PLT: Plut_0456
            RRS: RoseRS_2120
            RCA: Rcas_1749
            DRA: DR_1713
            DGE: Dgeo_0708
STRUCTURES  PDB: 2CXA  2DPS  2DPT  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.2.6
            ExPASy - ENZYME nomenclature database: 2.3.2.6
            ExplorEnz - The Enzyme Database: 2.3.2.6
            ERGO genome analysis and discovery system: 2.3.2.6
            BRENDA, the Enzyme Database: 2.3.2.6
            CAS: 37257-22-0
///
ENTRY       EC 2.3.2.7                  Enzyme
NAME        aspartyltransferase;
            beta-aspartyl transferase;
            aspartotransferase
CLASS       Transferases;
            Acyltransferases;
            Aminoacyltransferases
SYSNAME     L-asparagine:hydroxylamine gamma-aspartyltransferase
REACTION    L-asparagine + hydroxylamine = NH3 + L-aspartylhydroxamate
            [RN:R01485]
ALL_REAC    R01485
SUBSTRATE   L-asparagine [CPD:C00152];
            hydroxylamine [CPD:C00192]
PRODUCT     NH3 [CPD:C00014];
            L-aspartylhydroxamate [CPD:C03124]
REFERENCE   1
  AUTHORS   Jayaram, H.N., Ramakrishnan, T. and Vaidyanathan, C.S.
  TITLE     Aspartotransferase from Mycobacterium tuberculosis H37Ra.
  JOURNAL   Indian J. Biochem. 6 (1969) 106-110.
  ORGANISM  Mycobacterium tuberculosis
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.2.7
            ExPASy - ENZYME nomenclature database: 2.3.2.7
            ExplorEnz - The Enzyme Database: 2.3.2.7
            ERGO genome analysis and discovery system: 2.3.2.7
            BRENDA, the Enzyme Database: 2.3.2.7
            CAS: 37257-23-1
///
ENTRY       EC 2.3.2.8                  Enzyme
NAME        arginyltransferase;
            arginine transferase;
            arginyl-transfer ribonucleate-protein aminoacyltransferase;
            arginyl-transfer ribonucleate-protein transferase;
            arginyl-tRNA protein transferase
CLASS       Transferases;
            Acyltransferases;
            Aminoacyltransferases
SYSNAME     L-arginyl-tRNA:protein arginyltransferase
REACTION    L-arginyl-tRNA + protein = tRNA + L-arginyl-protein [RN:R03862]
ALL_REAC    R03862
SUBSTRATE   L-arginyl-tRNA [CPD:C02163];
            protein [CPD:C00017]
PRODUCT     tRNA [CPD:C00066];
            L-arginyl-protein [CPD:C00613]
COFACTOR    Mercaptoethanol [CPD:C00928];
            Cation [CPD:C01373]
COMMENT     Requires mercaptoethanol and a univalent cation. Peptides and
            proteins containing an N-terminal glutamate, aspartate or cystine
            residue can act as acceptors.
REFERENCE   1  [PMID:5416661]
  AUTHORS   Soffer RL.
  TITLE     Enzymatic modification of proteins. II. Purification and properties
            of the arginyl transfer ribonucleic acid-protein transferase from
            rabbit liver cytoplasm.
  JOURNAL   J. Biol. Chem. 245 (1970) 731-7.
  ORGANISM  rabbit
REFERENCE   2  [PMID:4572514]
  AUTHORS   Soffer RL.
  TITLE     Peptide acceptors in the arginine transfer reaction.
  JOURNAL   J. Biol. Chem. 248 (1973) 2918-21.
  ORGANISM  rabbit
REFERENCE   3  [PMID:5811819]
  AUTHORS   Soffer RL, Horinishi H.
  TITLE     Enzymic modification of proteins. I. General characteristics of the
            arginine-transfer reaction in rabbit liver cytoplasm.
  JOURNAL   J. Mol. Biol. 43 (1969) 163-75.
  ORGANISM  rabbit
ORTHOLOGY   KO: K00685  arginine-tRNA-protein transferase
GENES       HSA: 11101(ATE1)
            PTR: 450786(ATE1)
            MMU: 11907(Ate1)
            CFA: 486919(ATE1)
            GGA: 423936(RCJMB04_3h21)
            SPU: 584881(LOC584881)
            DME: Dmel_CG9204(Ate1)
            CEL: K07A1.9
            ATH: AT3G11240 AT5G05700(ATE1)
            OSA: 4338945
            CME: CML065C
            SCE: YGL017W(ATE1)
            AGO: AGOS_AGR165W
            PIC: PICST_82344(ATE1)
            CGR: CAGL0A00319g
            SPO: SPAC3C7.07c
            ANI: AN6250.2
            AFM: AFUA_2G13070
            UMA: UM05746.1
            DDI: DDBDRAFT_0202361
            TET: TTHERM_00310660
            XFA: XF1018
            XFT: PD0309(ate1)
            XCC: XCC1141(ate1)
            XCB: XC_3101
            XCV: XCV1273(ate)
            XAC: XAC1239(ate1)
            XOO: XOO1611(ate1)
            XOM: XOO_1494(XOO1494)
            VCH: VC1736
            VVY: VV2320
            VPA: VP1017
            VFI: VF1763
            PPR: PBPRA1154
            PAE: PA2618
            PAU: PA14_30260(ate1)
            PPU: PP_4006
            PPF: Pput_1827
            PST: PSPTO_3351
            PSB: Psyr_3181
            PSP: PSPPH_3095
            PFL: PFL_3883
            PFO: Pfl_3588
            PEN: PSEEN2209
            PMY: Pmen_2391
            PRW: PsycPRwf_0617
            ACI: ACIAD0888
            ACB: A1S_0873
            SON: SO_2624
            SDN: Sden_1836
            SFR: Sfri_2252
            SAZ: Sama_2054
            SBL: Sbal_2470
            SBM: Shew185_2463
            SLO: Shew_1568
            SPC: Sputcn32_2225
            SSE: Ssed_1888
            SPL: Spea_2530
            SHE: Shewmr4_1650
            SHM: Shewmr7_1725
            SHN: Shewana3_1755
            SHW: Sputw3181_1784
            ILO: IL0672
            CPS: CPS_2764
            PAT: Patl_2372
            SDE: Sde_1690
            MAQ: Maqu_1755
            MCA: MCA1791
            NOC: Noc_2597
            AEH: Mlg_1714
            HHA: Hhal_1398
            HCH: HCH_02342
            CSA: Csal_2438
            ABO: ABO_1287
            AHA: AHA_1859
            CVI: CV_1799(ate1)
            RSO: RSc1616(RS03979)
            REU: Reut_A1318
            REH: H16_A1402(ate)
            RME: Rmet_1214
            BMA: BMA1252
            BXE: Bxe_A2506
            BVI: Bcep1808_1519
            BUR: Bcep18194_A4697
            BCN: Bcen_1075
            BCH: Bcen2424_1555
            BAM: Bamb_1456
            BPS: BPSL1865
            BPM: BURPS1710b_1979
            BTE: BTH_I2510
            PNU: Pnuc_0742
            BPE: BP3443
            BPA: BPP3539
            BBR: BB3974
            RFR: Rfer_2348
            POL: Bpro_2325
            PNA: Pnap_1724
            AAV: Aave_3105
            AJS: Ajs_1987
            VEI: Veis_3623
            MPT: Mpe_A1468
            HAR: HEAR2443
            MMS: mma_2512
            NEU: NE2220
            NET: Neut_0647
            NMU: Nmul_A2708
            EBA: ebA4890(ate)
            AZO: azo2209(ate)
            DAR: Daro_1195
            TBD: Tbd_2042
            MFA: Mfla_0931 Mfla_1075
            HHE: HH1829
            WSU: WS1276
            TDN: Tmden_0358
            CJE: Cj1035c
            CJR: CJE1179
            CJU: C8J_0972
            CFF: CFF8240_0678
            ABU: Abu_1772(ate)
            NIS: NIS_0160
            SUN: SUN_1699
            DPS: DP2839
            MXA: MXAN_2360
            MLO: mll8364
            MES: Meso_1127
            PLA: Plav_2883
            SME: SMc01764
            SMD: Smed_0810
            ATU: Atu1159
            ATC: AGR_C_2146
            RET: RHE_CH01502(ate)
            RLE: RL1614
            BME: BMEI1199
            BMF: BAB1_0778
            BMS: BR0755
            BMB: BruAb1_0772
            OAN: Oant_2538
            BJA: blr5039
            BRA: BRADO4438
            BBT: BBta_4657
            RPA: RPA2710
            RPB: RPB_2621
            RPC: RPC_2649
            RPD: RPD_2658
            RPE: RPE_3011
            NWI: Nwi_1911
            NHA: Nham_2242
            XAU: Xaut_4292
            CCR: CC_1572
            SIL: SPO2569(ate)
            SIT: TM1040_0882
            RSP: RSP_2639
            RSH: Rsph17029_1296
            RSQ: Rsph17025_1175
            JAN: Jann_1903
            RDE: RD1_2805(ate)
            PDE: Pden_2168
            MMR: Mmar10_1559
            HNE: HNE_0893(ate)
            NAR: Saro_1101
            SAL: Sala_0342
            SWI: Swit_2393
            ELI: ELI_01635
            GOX: GOX0072
            GBE: GbCGDNIH1_0996
            ACR: Acry_0237
            RRU: Rru_A1845
            MAG: amb2581
            MGM: Mmc1_0019
            RBA: RB10567(ate1)
            LIL: LA1974
            LIC: LIC11930
            LBJ: LBJ_1540
            LBL: LBL_1764
            CHU: CHU_2143(ate)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.2.8
            ExPASy - ENZYME nomenclature database: 2.3.2.8
            ExplorEnz - The Enzyme Database: 2.3.2.8
            ERGO genome analysis and discovery system: 2.3.2.8
            BRENDA, the Enzyme Database: 2.3.2.8
            CAS: 37257-24-2
///
ENTRY       EC 2.3.2.9                  Enzyme
NAME        agaritine gamma-glutamyltransferase;
            (gamma-L-glutamyl)-N1-(4-hydroxymethylphenyl)hydrazine:(acceptor)
            gamma-glutamyltransferase;
            (gamma-L-glutamyl)-1-N-(4-hydroxymethylphenyl)hydrazine:(acceptor)
            gamma-glutamyltransferase;
            (gamma-L-glutamyl)-1-N-(4-hydroxymethylphenyl)hydrazine:acceptor
            gamma-glutamyltransferase
CLASS       Transferases;
            Acyltransferases;
            Aminoacyltransferases
SYSNAME     (gamma-L-glutamyl)-N1-(4-hydroxymethylphenyl)hydrazine:acceptor
            gamma-glutamyltransferase
REACTION    agaritine + acceptor = 4-hydroxymethylphenylhydrazine +
            gamma-L-glutamyl-acceptor [RN:R03609]
ALL_REAC    R03609
SUBSTRATE   agaritine [CPD:C01550];
            acceptor [CPD:C00028]
PRODUCT     4-hydroxymethylphenylhydrazine [CPD:C03994];
            gamma-L-glutamyl-acceptor [CPD:C03649]
COMMENT     4-Hydroxyaniline, cyclohexylamine, 1-naphthylhydrazine and similar
            compounds can act as acceptors; the enzyme also catalyses the
            hydrolysis of agaritine.
REFERENCE   1  [PMID:14209959]
  AUTHORS   GIGLIOTTI HJ, LEVENBERG B.
  TITLE     STUDIES ON THE GAMMA-GLUTAMYLTRANSFERASE OF AGARICUS BISPORUS.
  JOURNAL   J. Biol. Chem. 239 (1964) 2274-84.
  ORGANISM  Agaricus bisporus
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.2.9
            ExPASy - ENZYME nomenclature database: 2.3.2.9
            ExplorEnz - The Enzyme Database: 2.3.2.9
            ERGO genome analysis and discovery system: 2.3.2.9
            BRENDA, the Enzyme Database: 2.3.2.9
            CAS: 37257-25-3
///
ENTRY       EC 2.3.2.10                 Enzyme
NAME        UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase;
            alanyl-transfer ribonucleate-uridine
            diphosphoacetylmuramoylpentapeptide transferase;
            UDP-N-acetylmuramoylpentapeptide lysine N6-alanyltransferase;
            uridine diphosphoacetylmuramoylpentapeptide lysine
            N6-alanyltransferase;
            L-alanyl-tRNA:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-
            alanyl-D-alanine 6-N-alanyltransferase
CLASS       Transferases;
            Acyltransferases;
            Aminoacyltransferases
SYSNAME     L-alanyl-tRNA:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-ala
            nyl-D-alanine N6-alanyltransferase
REACTION    L-alanyl-tRNA +
            UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
            = tRNA +
            UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-
            alanyl-D-alanine [RN:R04613]
ALL_REAC    R04613;
            (other) R05029 R05031 R05034
SUBSTRATE   L-alanyl-tRNA [CPD:C00886];
            UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
            [CPD:C04846]
PRODUCT     tRNA [CPD:C00066];
            UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-
            alanyl-D-alanine [CPD:C04894]
COMMENT     Also acts on L-seryl-tRNA.
REFERENCE   1  [PMID:4248527]
  AUTHORS   Plapp R, Strominger JL.
  TITLE     Biosynthesis of the peptidoglycan of bacterial cell walls. 18.
            Purification and properties of L-alanyl transfer ribonucleic
            acid-uridine diphosphate-N-acetylmuramyl-pentapeptide transferase
            from Lactobacillus viridescens.
  JOURNAL   J. Biol. Chem. 245 (1970) 3675-82.
  ORGANISM  Lactobacillus viridescens
PATHWAY     PATH: map00550  Peptidoglycan biosynthesis
ORTHOLOGY   KO: K05363  UDP-N-acetylmuramoylpentapeptide-lysine
                        N6-alanyltransferase
GENES       SPZ: M5005_Spy_0511(murM) M5005_Spy_0920
            SPH: MGAS10270_Spy0505(murM) MGAS10270_Spy1034
            SPI: MGAS10750_Spy0530(murM) MGAS10750_Spy1069
            SPJ: MGAS2096_Spy0523(murM) MGAS2096_Spy0979
            SPK: MGAS9429_Spy0501(murM) MGAS9429_Spy1022
            SPA: M6_Spy0909
            SPB: M28_Spy0892
STRUCTURES  PDB: 1P4N  1XE4  1XF8  1XIX  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.2.10
            ExPASy - ENZYME nomenclature database: 2.3.2.10
            ExplorEnz - The Enzyme Database: 2.3.2.10
            ERGO genome analysis and discovery system: 2.3.2.10
            BRENDA, the Enzyme Database: 2.3.2.10
            CAS: 37257-26-4
///
ENTRY       EC 2.3.2.11                 Enzyme
NAME        alanylphosphatidylglycerol synthase;
            O-alanylphosphatidylglycerol synthase;
            alanyl phosphatidylglycerol synthetase
CLASS       Transferases;
            Acyltransferases;
            Aminoacyltransferases
SYSNAME     L-alanyl-tRNA:phosphatidylglycerol alanyltransferase
REACTION    L-alanyl-tRNA + phosphatidylglycerol = tRNA +
            3-O-L-alanyl-1-O-phosphatidylglycerol [RN:R03039]
ALL_REAC    R03039
SUBSTRATE   L-alanyl-tRNA [CPD:C00886];
            phosphatidylglycerol [CPD:C00344]
PRODUCT     tRNA [CPD:C00066];
            3-O-L-alanyl-1-O-phosphatidylglycerol [CPD:C04372]
REFERENCE   1  [PMID:4297471]
  AUTHORS   Gould RM, Thornton MP, Liepkalns V, Lennarz WJ.
  TITLE     Participation of aminoacyl transfer ribonucleic acid in aminoacyl
            phosphatidylglycerol synthesis. II. Specificity of alanyl
            phosphatidylglycerol synthetase.
  JOURNAL   J. Biol. Chem. 243 (1968) 3096-104.
  ORGANISM  Clostridium welchii
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.2.11
            ExPASy - ENZYME nomenclature database: 2.3.2.11
            ExplorEnz - The Enzyme Database: 2.3.2.11
            ERGO genome analysis and discovery system: 2.3.2.11
            BRENDA, the Enzyme Database: 2.3.2.11
            CAS: 37257-27-5
///
ENTRY       EC 2.3.2.12                 Enzyme
NAME        peptidyltransferase;
            transpeptidase;
            ribosomal peptidyltransferase
CLASS       Transferases;
            Acyltransferases;
            Aminoacyltransferases
SYSNAME     peptidyl-tRNA:aminoacyl-tRNA N-peptidyltransferase
REACTION    peptidyl-tRNA1 + aminoacyl-tRNA2 = tRNA1 + peptidyl(aminoacyl-tRNA2
            ) [RN:R04685]
ALL_REAC    R04685
SUBSTRATE   peptidyl-tRNA1;
            aminoacyl-tRNA2
PRODUCT     tRNA1;
            peptidyl(aminoacyl-tRNA2 )
COMMENT     An enzyme found in ribosomes.
REFERENCE   1  [PMID:5329275]
  AUTHORS   Rychlik I.
  TITLE     Release of lysine peptides by puromycin from polylysyl-transfer
            ribonucleic acid in the presence of ribosomes.
  JOURNAL   Biochim. Biophys. Acta. 114 (1966) 425-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4897787]
  AUTHORS   Rychlik I, Cerna J, Chladek S, Zemlicka J, Haladova Z.
  TITLE     Substrate specificity of ribosomal peptidyl transferase:
            2'(3')-O-aminoacyl nucleosides as acceptors of the peptide chain on
            the amino acid site.
  JOURNAL   J. Mol. Biol. 43 (1969) 13-24.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Traut, R.R. and Monro, R.E.
  TITLE     The puromycin reaction and its relation to protein synthesis.
  JOURNAL   J. Mol. Biol. 10 (1964) 63-72.
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.2.12
            ExPASy - ENZYME nomenclature database: 2.3.2.12
            ExplorEnz - The Enzyme Database: 2.3.2.12
            ERGO genome analysis and discovery system: 2.3.2.12
            BRENDA, the Enzyme Database: 2.3.2.12
            CAS: 9059-29-4
///
ENTRY       EC 2.3.2.13                 Enzyme
NAME        protein-glutamine gamma-glutamyltransferase;
            transglutaminase;
            Factor XIIIa;
            fibrinoligase;
            fibrin stabilizing factor;
            glutaminylpeptide gamma-glutamyltransferase;
            polyamine transglutaminase;
            tissue transglutaminase;
            R-glutaminyl-peptide:amine gamma-glutamyl transferase
CLASS       Transferases;
            Acyltransferases;
            Aminoacyltransferases
SYSNAME     protein-glutamine:amine gamma-glutamyltransferase
REACTION    protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
            [RN:R03983]
ALL_REAC    R03983
SUBSTRATE   protein glutamine [CPD:C02583];
            alkylamine [CPD:C01664]
PRODUCT     protein N5-alkylglutamine [CPD:C03636];
            NH3 [CPD:C00014]
COFACTOR    Calcium [CPD:C00076]
COMMENT     Requires Ca2+. The gamma-carboxamide groups of peptide-bound
            glutamine residues act as acyl donors, and the 6-amino-groups of
            protein- and peptide-bound lysine residues act as acceptors, to give
            intra- and inter-molecular N6-(5-glutamyl)-lysine crosslinks. Formed
            by proteolytic cleavage from plasma Factor XIII
REFERENCE   1  [PMID:4151471]
  AUTHORS   Folk JE, Chung SI.
  TITLE     Molecular and catalytic properties of transglutaminases.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 38 (1973) 109-91.
  ORGANISM  guinea pig
REFERENCE   2  [PMID:5928192]
  AUTHORS   Folk JE, Cole PW.
  TITLE     Mechanism of action of guinea pig liver transglutaminase. I.
            Purification and properties of the enzyme: identification of a
            functional cysteine essential for activity.
  JOURNAL   J. Biol. Chem. 241 (1966) 5518-25.
  ORGANISM  guinea pig
REFERENCE   3  [PMID:73346]
  AUTHORS   Folk JE, Finlayson JS.
  TITLE     The epsilon-(gamma-glutamyl)lysine crosslink and the catalytic role
            of transglutaminases.
  JOURNAL   Adv. Protein. Chem. 31 (1977) 1-133.
REFERENCE   4  [PMID:2877456]
  AUTHORS   Takahashi N, Takahashi Y, Putnam FW.
  TITLE     Primary structure of blood coagulation factor XIIIa (fibrinoligase,
            transglutaminase) from human placenta.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 8019-23.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04610  Complement and coagulation cascades
            PATH: map05040  Huntington's disease
ORTHOLOGY   KO: K00686  protein-glutamine gamma-glutamyltransferase
            KO: K03917  coagulation factor XIII A1 polypeptide
            KO: K05619  transglutaminase 1
            KO: K05620  transglutaminase 3
            KO: K05621  transglutaminase 4
            KO: K05622  transglutaminase 5
            KO: K05623  transglutaminase 7
            KO: K05624  transglutaminase 6
            KO: K05625  transglutaminase 2
GENES       HSA: 116179(TGM7) 2162(F13A1) 2165(F13B) 343641(TGM6) 7047(TGM4)
                 7051(TGM1) 7052(TGM2) 7053(TGM3) 9333(TGM5)
            PTR: 452814(TGM1) 453375(TGM5) 462413(F13A1) 469937(TGM2)
            MMU: 14060(F13b) 21816(Tgm1) 21817(Tgm2) 21818(Tgm3) 241636(Tgm6)
                 331046(Tgm4) 74145(F13a1) 74176(Tgm5)
            RNO: 56083(Tgm2) 60327(F13a1) 60335(Tgm1) 64679(Tgm4)
            CFA: 403630(TGM1) 477180(TGM3) 478711(F13A1) 485807(TGM6)
                 485867(TGM2) 487522(TGM5) 487523(TGM7)
            BTA: 281528(TGM2) 407997(TGM1)
            GGA: 395420(F13A1) 396432(TGM2) 419215(TGM3) 420706(TGM4)
                 771144(TGM6)
            XLA: 443836(MGC82568)
            DRE: 323856(tgm2b)
            BSU: BG10946(tgl)
            BHA: BH3970(tgl)
            BAN: BA4173
            BAR: GBAA4173
            BAA: BA_4644
            BAT: BAS3875
            BCE: BC3963
            BCZ: BCZK3723(tgl)
            BCY: Bcer98_2665
            BTK: BT9727_3708(tgl)
            BLI: BL02523(tgl)
            BLD: BLi03298(tgl)
            BCL: ABC2191(tgl)
            BAY: RBAM_028330(tgl)
            BPU: BPUM_2792(tgl)
            GKA: GK2914(tgl)
            CKL: CKL_0538(tgl)
STRUCTURES  PDB: 1EVU  1EX0  1F13  1FIE  1G0D  1GGT  1GGU  1GGY  1IU4  1KV3  
                 1L9M  1L9N  1NUD  1NUF  1NUG  1QRK  1RLE  1SGX  1VJJ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.2.13
            ExPASy - ENZYME nomenclature database: 2.3.2.13
            ExplorEnz - The Enzyme Database: 2.3.2.13
            ERGO genome analysis and discovery system: 2.3.2.13
            BRENDA, the Enzyme Database: 2.3.2.13
            CAS: 80146-85-6
///
ENTRY       EC 2.3.2.14                 Enzyme
NAME        D-alanine gamma-glutamyltransferase
CLASS       Transferases;
            Acyltransferases;
            Aminoacyltransferases
SYSNAME     L-glutamine:D-alanine gamma-glutamyltransferase
REACTION    L-glutamine + D-alanine = NH3 + gamma-L-glutamyl-D-alanine
            [RN:R01149]
ALL_REAC    R01149
SUBSTRATE   L-glutamine [CPD:C00064];
            D-alanine [CPD:C00133]
PRODUCT     NH3 [CPD:C00014];
            gamma-L-glutamyl-D-alanine [CPD:C03738]
COMMENT     D-Phenylalanine and D-2-aminobutyrate can also act as acceptors, but
            more slowly. The enzyme also catalyses some of the reactions of EC
            2.3.2.2 (gamma-glutamyltransferase).
REFERENCE   1
  AUTHORS   Kawasaki, Y., Ogawa, T. and Sasaoka, K.
  TITLE     Occurrence and some properties of a novel gamma-glutamyltransferase
            responsible for the synthesis of gamma-L-glutamyl-D-alanine in
            pea-seedlings.
  JOURNAL   Biochim. Biophys. Acta 716 (1982) 194-200.
  ORGANISM  Pisum sativum
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.2.14
            ExPASy - ENZYME nomenclature database: 2.3.2.14
            ExplorEnz - The Enzyme Database: 2.3.2.14
            ERGO genome analysis and discovery system: 2.3.2.14
            BRENDA, the Enzyme Database: 2.3.2.14
            CAS: 9046-27-9
///
ENTRY       EC 2.3.2.15                 Enzyme
NAME        glutathione gamma-glutamylcysteinyltransferase;
            phytochelatin synthase;
            gamma-glutamylcysteine dipeptidyl transpeptidase
CLASS       Transferases;
            Acyltransferases;
            Aminoacyltransferases
SYSNAME     glutathione:poly(4-glutamyl-cysteinyl)glycine
            4-glutamylcysteinyltransferase
REACTION    glutathione + [Glu(-Cys)]n-Gly = Gly + [Glu(-Cys)]n+1-Gly
            [RN:R03956]
ALL_REAC    R03956
SUBSTRATE   glutathione [CPD:C00051];
            [Glu(-Cys)]n-Gly [CPD:C02471]
PRODUCT     Gly [CPD:C00037];
            [Glu(-Cys)]n+1-Gly [CPD:C02755]
REFERENCE   1
  AUTHORS   Grill, E., Loffler, S., Winnacker, E.-L. and Zenk, M.H.
  TITLE     Phytochelatins, the heavy-metal-binding peptides of plants, are
            synthesized from glutathione by a specific gamma-glutamylcysteine
            dipeptidyl transpeptidase (phytochelatin synthase).
  JOURNAL   Proc. Natl. Acad. Sci. USA 86 (1989) 6838-6842.
ORTHOLOGY   KO: K05941  
GENES       CEL: F54D5.1(pcs-1)
STRUCTURES  PDB: 2BTW  2BU3  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.2.15
            ExPASy - ENZYME nomenclature database: 2.3.2.15
            ExplorEnz - The Enzyme Database: 2.3.2.15
            ERGO genome analysis and discovery system: 2.3.2.15
            BRENDA, the Enzyme Database: 2.3.2.15
            CAS: 125390-02-5
///
ENTRY       EC 2.3.2.-                  Enzyme
CLASS       Transferases;
            Acyltransferases;
            Aminoacyltransferases
REACTION    (1) Leukotriene D4 + H2O <=> Leukotriene E4 + Glycine [RN:R05055];
            (2) Leukotriene E4 + L-Glutamate <=> Leukotriene F4 + H2O
            [RN:R05207]
SUBSTRATE   Leukotriene D4 [CPD:C05951];
            H2O [CPD:C00001];
            Leukotriene E4 [CPD:C05952];
            L-Glutamate [CPD:C00025]
PRODUCT     Leukotriene E4 [CPD:C05952];
            Glycine [CPD:C00037];
            Leukotriene F4 [CPD:C06462];
            H2O [CPD:C00001]
///
ENTRY       EC 2.3.3.1                  Enzyme
NAME        citrate (Si)-synthase;
            (R)-citric synthase;
            citrate condensing enzyme;
            citrate oxaloacetate-lyase [(pro-3S)-CH2COO-->acetyl-CoA];
            citrate oxaloacetate-lyase, CoA-acetylating;
            citrate synthase;
            citrate synthetase;
            citric synthase;
            citric-condensing enzyme;
            citrogenase;
            condensing enzyme;
            oxaloacetate transacetase;
            oxalacetic transacetase
CLASS       Transferases;
            Acyltransferases;
            Acyl groups converted into alkyl groups on transfer
SYSNAME     acetyl-CoA:oxaloacetate C-acetyltransferase [thioester-hydrolysing,
            (pro-S)-carboxymethyl forming]
REACTION    acetyl-CoA + H2O + oxaloacetate = citrate + CoA [RN:R00351]
ALL_REAC    R00351
SUBSTRATE   acetyl-CoA [CPD:C00024];
            H2O [CPD:C00001];
            oxaloacetate [CPD:C00036]
PRODUCT     citrate [CPD:C00158];
            CoA [CPD:C00010]
COMMENT     The stereospecificity of this enzyme is opposite to that of EC
            2.3.3.3, citrate (Re)-synthase, which is found in some anaerobes.
REFERENCE   1  [PMID:4974734]
  AUTHORS   Gottschalk G.
  TITLE     Partial purification and some properties of the (R)-citrate synthase
            from Clostridium acidi-urici.
  JOURNAL   Eur. J. Biochem. 7 (1969) 301-6.
  ORGANISM  Clostridium acidi-urici
REFERENCE   2  [PMID:14907759]
  AUTHORS   OCHOA S, STERN JR, SCHNEIDER MC.
  TITLE     Enzymatic synthesis of citric acid. II. Crystalline condensing
            enzyme.
  JOURNAL   J. Biol. Chem. 193 (1951) 691-702.
  ORGANISM  pig [GN:ssc]
REFERENCE   3
  AUTHORS   Stern, J.R.
  TITLE     Oxalacetate transacetase (condensing enzyme, citrogenase).
  JOURNAL   In: Boyer, P,D., Lardy, H and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 5, Academic Press, New York, 1961, p. 367-380.
REFERENCE   4  [PMID:7819205]
  AUTHORS   Rault-Leonardon M, Atkinson MA, Slaughter CA, Moomaw CR, Srere PA.
  TITLE     Azotobacter vinelandii citrate synthase.
  JOURNAL   Biochemistry. 34 (1995) 257-63.
  ORGANISM  Azotobacter vinelandii
REFERENCE   5
  AUTHORS   Muir, J.M., Russell, R.J., Hough, D.W. and Danson, M.J.
  TITLE     Citrate synthase from the hyperthermophilic Archaeon, Pyrococcus
            furiosus.
  JOURNAL   Prot. Eng. 8 (1995) 583-592.
  ORGANISM  Pyrococcus furiosus [GN:pfu]
REFERENCE   6  [PMID:9254593]
  AUTHORS   Russell RJ, Ferguson JM, Hough DW, Danson MJ, Taylor GL.
  TITLE     The crystal structure of citrate synthase from the hyperthermophilic
            archaeon pyrococcus furiosus at 1.9 A resolution,.
  JOURNAL   Biochemistry. 36 (1997) 9983-94.
  ORGANISM  Pyrococcus furiosus [GN:pfu]
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K01647  citrate synthase
GENES       HSA: 1431(CS)
            MMU: 12974(Cs) 71832(Csl)
            RNO: 170587(Cs)
            CFA: 474403(CS)
            BTA: 280682(CS)
            SSC: 397519(CS)
            XLA: 379886(cs)
            DRE: 322339(cs)
            DME: Dmel_CG3861(l(1)G0030)
            CEL: T20G5.2(cts-1)
            ATH: AT2G42790(CSY3) AT3G58740(CSY1) AT3G58750(CSY2)
                 AT3G60100(CSY5)
            OSA: 4328598 4328812
            CME: CMA040C CMJ293C CMM068C CMQ191C
            SCE: YCR005C(CIT2) YNR001C(CIT1) YPR001W(CIT3)
            AGO: AGOS_AAR004C AGOS_AGR002W
            PIC: PICST_85554(CIT1)
            CGR: CAGL0H03993g CAGL0L09086g
            SPO: SPAC6C3.04
            ANI: AN6650.2 AN7593.2 AN8275.2
            AFM: AFUA_5G04230 AFUA_6G03590
            AOR: AO090009000568 AO090010000170 AO090012000318 AO090102000627
            CNE: CNA00510
            UMA: UM01627.1
            DDI: DDB_0191110(cshA) DDB_0214944(gltA) DDB_0220638
            PFA: PF10_0218
            TAN: TA14450
            TPV: TP02_0666
            TET: TTHERM_00049070 TTHERM_00318570 TTHERM_00383610
                 TTHERM_00529790 TTHERM_00655610
            TBR: Tb10.05.0150
            TCR: 509801.30 511277.110
            LMA: LmjF18.0670 LmjF18.0680
            ECO: b0720(gltA)
            ECJ: JW0710(gltA)
            ECE: Z0873(gltA)
            ECS: ECs0745
            ECC: c0796(gltA) c0797
            ECI: UTI89_C0715(gltA)
            ECP: ECP_0731
            ECV: APECO1_1358(gltA)
            ECW: EcE24377A_0747(gltA)
            ECX: EcHS_A0768(gltA)
            STY: STY0773(gltA)
            STT: t2146(gltA)
            SPT: SPA2013(gltA)
            SEC: SC0736(gltA)
            STM: STM0730(gltA)
            YPE: YPO1108(gltA)
            YPK: y3072(gltA)
            YPM: YP_1048(gltA)
            YPA: YPA_0586
            YPN: YPN_2890
            YPP: YPDSF_2589
            YPS: YPTB1142(gltA)
            YPI: YpsIP31758_2886(gltA)
            SFL: SF0577(gltA)
            SFX: S0590(gltA)
            SFV: SFV_0615(gltA)
            SSN: SSON_0671(gltA)
            SBO: SBO_0578(gltA)
            SDY: SDY_0658(gltA)
            ECA: ECA1356(gltA) ECA4121
            PLU: plu1425(gltA)
            SGL: SG0871
            ENT: Ent638_1221
            SPE: Spro_1262
            HSO: HS_0960(gltA)
            PMU: PM0276(gltA)
            MSU: MS2371(gltA)
            XFA: XF1535
            XFT: PD0750(gltA)
            XCC: XCC3235(gltA)
            XCB: XC_0944
            XCV: XCV3504(gltA)
            XAC: XAC3388(gltA)
            XOO: XOO1154(gltA)
            XOM: XOO_1051(XOO1051)
            VCH: VC2092
            VCO: VC0395_A1678(gltA)
            VVU: VV1_0162
            VVY: VV1027
            VPA: VP0842
            VFI: VF0818
            PPR: PBPRA1043
            PAE: PA1580(gltA)
            PAU: PA14_44070(gltA)
            PAP: PSPA7_3694(gltA)
            PPU: PP_4194(gltA)
            PPF: Pput_1660
            PST: PSPTO_2194(gltA)
            PSB: Psyr_2004
            PSP: PSPPH_1974(gltA)
            PFL: PFL_1713(gltA)
            PFO: Pfl_1609
            PEN: PSEEN3646(gltA)
            PMY: Pmen_2508
            PAR: Psyc_0097(gltA)
            PCR: Pcryo_0106
            PRW: PsycPRwf_0260
            ACI: ACIAD2886(gltA)
            SON: SO_1926(gltA)
            SDN: Sden_2189
            SFR: Sfri_2348
            SAZ: Sama_1422
            SBL: Sbal_2520
            SBM: Shew185_2513
            SLO: Shew_1650
            SPC: Sputcn32_2274
            SSE: Ssed_2819
            SPL: Spea_1783
            SHE: Shewmr4_1630
            SHM: Shewmr7_1705
            SHN: Shewana3_1705
            SHW: Sputw3181_1734
            ILO: IL1508(gltA)
            CPS: CPS_2214(gltA)
            PHA: PSHAa1653(gltA)
            PAT: Patl_1794
            SDE: Sde_2111
            PIN: Ping_2257 Ping_2617
            MAQ: Maqu_1149
            CBU: CBU_1410(gltA)
            CBD: COXBU7E912_0586(gltA)
            LPN: lpg1415(gltA)
            LPF: lpl1366(gltA)
            LPP: lpp1370(gltA)
            MCA: MCA0847(gltA)
            FTU: FTT0071c(gltA)
            FTF: FTF0071c(gltA)
            FTW: FTW_0147(gltA)
            FTL: FTL_1789
            FTH: FTH_1725(gltA)
            FTA: FTA_1895(gltA)
            FTN: FTN_1640(gltA)
            TCX: Tcr_0350
            NOC: Noc_2628
            AEH: Mlg_2752
            HHA: Hhal_2251
            HCH: HCH_04750(gltA)
            CSA: Csal_1212
            ABO: ABO_1501(gltA)
            MMW: Mmwyl1_2805
            AHA: AHA_1922(gltA)
            RMA: Rmag_1063
            VOK: COSY_0962(gltA)
            NME: NMB0954
            NMA: NMA1148(gltA)
            NMC: NMC0930(gltA) NMC1732(prpC)
            NGO: NGO0918
            CVI: CV_1070(gtlA)
            RSO: RSc1991(gltA)
            REU: Reut_A2320 Reut_C6294 Reut_C6318 Reut_C6352
            REH: H16_A1229 H16_A2627(cisY) H16_B0357 H16_B0414 H16_B2211
            RME: Rmet_2481 Rmet_4144 Rmet_4268 Rmet_5380
            BMA: BMAA1744(gltA)
            BMV: BMASAVP1_1626(gltA)
            BML: BMA10299_1834(gltA)
            BMN: BMA10247_A0504(gltA)
            BXE: Bxe_B1134 Bxe_B2890 Bxe_C0986
            BVI: Bcep1808_4415
            BUR: Bcep18194_B1148 Bcep18194_B2147 Bcep18194_C6702
            BCN: Bcen_4428 Bcen_4951
            BCH: Bcen2424_3209 Bcen2424_3939
            BAM: Bamb_3316
            BPS: BPSL0890 BPSS1715(gltA)
            BPM: BURPS1710b_1097(cisZ) BURPS1710b_A0788(gltA)
            BPL: BURPS1106A_A2329(gltA)
            BPD: BURPS668_A2467(gltA)
            BTE: BTH_II0665(gltA)
            PNU: Pnuc_0763
            BPE: BP2358(gltA)
            BPA: BPP3225(gltA)
            BBR: BB3677(gltA)
            RFR: Rfer_1796
            POL: Bpro_3605
            PNA: Pnap_3037
            AAV: Aave_2199
            AJS: Ajs_2798
            VEI: Veis_1400 Veis_4350
            MPT: Mpe_A2165
            HAR: HEAR1773(gltA)
            MMS: mma_1511(gltA)
            NEU: NE2373(gltA)
            NET: Neut_0861
            NMU: Nmul_A0858
            EBA: ebA6687(gltA)
            AZO: azo1554(gltA)
            DAR: Daro_2860
            TBD: Tbd_1187
            MFA: Mfla_0061
            HPY: HP0026(gltA)
            HPJ: jhp0022(gltA)
            HPA: HPAG1_0024
            HHE: HH1493(gltA)
            HAC: Hac_0040(gltA)
            WSU: WS1453(gltA)
            TDN: Tmden_2100
            CJE: Cj1682c(gltA)
            CJR: CJE1851(gltA)
            CJJ: CJJ81176_1675(gltA)
            CJU: C8J_1580(gltA)
            CJD: JJD26997_2055(gltA)
            CFF: CFF8240_0178(gltA)
            CCV: CCV52592_0576(gltA)
            CHA: CHAB381_1548(gltA)
            CCO: CCC13826_2287(gltA)
            ABU: Abu_0310(gltA)
            SUN: SUN_2395(gltA)
            GSU: GSU1106
            GME: Gmet_1124 Gmet_2689
            GUR: Gura_1576
            PCA: Pcar_1991
            PPD: Ppro_1134
            BBA: Bd0562(citZ) Bd2511(cit)
            DPS: DP0394 DP1088
            ADE: Adeh_3670
            AFW: Anae109_3798
            MXA: MXAN_0407(citZ) MXAN_3519(gltA)
            SFU: Sfum_1533 Sfum_2105
            RPR: RP844(gltA)
            RTY: RT0832(gltA)
            RCO: RC1308(gltA)
            RFE: RF_1338(gltA)
            RBE: RBE_1325(gltA)
            RAK: A1C_06540(gltA)
            RBO: A1I_00225(gltA)
            RCM: A1E_05425(gltA)
            RRI: A1G_07170(gltA)
            WOL: WD1151(gltA)
            WBM: Wbm0735
            AMA: AM1187(gltA)
            APH: APH_1232(gltA)
            ERU: Erum0750(gltA)
            ERW: ERWE_CDS_00690(gltA)
            ERG: ERGA_CDS_00660(gltA)
            ECN: Ecaj_0075
            ECH: ECH_0124(gltA)
            NSE: NSE_0730(gltA)
            PUB: SAR11_1156(prpC)
            MLO: mll3842 mlr0629
            MES: Meso_1646
            PLA: Plav_0857 Plav_3181
            SME: SMc02087(gltA)
            SMD: Smed_1144
            ATU: Atu1392(cisY) Atu5306(cis)
            ATC: AGR_C_2572 AGR_pAT_439
            RET: RHE_CH01926(gltA) RHE_CH02182(cisZ)
            RLE: RL2234(ccsA) RL2508(gltA) RL2509(citA)
            BME: BMEI0836
            BMF: BAB1_1170(gltA)
            BMS: BR1148(gltA)
            BMB: BruAb1_1154(gltA)
            BOV: BOV_1106(gltA)
            OAN: Oant_2042 Oant_2103
            BJA: bll6374 blr0183(cis) blr4839(gltA)
            BRA: BRADO0613 BRADO0614 BRADO4126(gltA)
            BBT: BBta_4502(gltA) BBta_7567 BBta_7568
            RPA: RPA2907(cisY)
            RPB: RPB_2813
            RPC: RPC_2450
            RPD: RPD_2843
            RPE: RPE_2567
            NWI: Nwi_1845
            NHA: Nham_1708
            BHE: BH06380(gltA)
            BQU: BQ06850(gltA)
            BBK: BARBAKC583_0599(gltA)
            XAU: Xaut_4425
            CCR: CC_1906 CC_3642
            SIL: SPO2157(gltA)
            SIT: TM1040_1132 TM1040_2728
            RSP: RSP_1994(gltA)
            RSH: Rsph17029_0704
            RSQ: Rsph17025_3091
            JAN: Jann_1841
            RDE: RD1_3219(gltA)
            PDE: Pden_3716
            MMR: Mmar10_1395
            HNE: HNE_1782(gltA) HNE_3453 HNE_3454
            ZMO: ZMO1963(gltA)
            NAR: Saro_2032
            SAL: Sala_0829
            SWI: Swit_3212
            ELI: ELI_06545
            GOX: GOX1999
            GBE: GbCGDNIH1_0896
            ACR: Acry_1731
            RRU: Rru_A1600
            MAG: amb2804
            MGM: Mmc1_0897
            ABA: Acid345_2276
            SUS: Acid_1653 Acid_4792
            BSU: BG10854(citA) BG10855(citZ) BG11322(mmgD)
            BHA: BH3160(citZ) BH3924(mmgD)
            BAN: BA2348(mmgD) BA4839(citZ)
            BAR: GBAA2348(mmgD) GBAA4839(citZ)
            BAA: BA_2844 BA_5262
            BAT: BAS2188 BAS4488
            BCE: BC2285 BC4594
            BCA: BCE_2376(mmgD) BCE_4725(citZ)
            BCZ: BCZK2111(mmgD) BCZK4335(citZ)
            BCY: Bcer98_1724 Bcer98_3278
            BTK: BT9727_2125(mmgD) BT9727_4323(citZ)
            BTL: BALH_2093(mmgD) BALH_4178(citZ)
            BLI: BL00399(citZ) BL00561(mmgD) BL02891(citA)
            BLD: BLi01010(citA) BLi03062(citZ) BLi04094(mmgD)
            BCL: ABC1805(mmgD) ABC2715(citZ) ABC4043(citA)
            BPU: BPUM_1848 BPUM_2556(citZ)
            OIH: OB2168(citZ) OB2269
            GKA: GK2736
            SAU: SA1518(citZ)
            SAV: SAV1695(citZ)
            SAM: MW1639(citZ)
            SAR: SAR1774(citZ)
            SAS: SAS1623
            SAC: SACOL1742(gltA)
            SAB: SAB1554c(citZ)
            SAA: SAUSA300_1641(gltA)
            SAO: SAOUHSC_01802
            SAJ: SaurJH9_1752
            SAH: SaurJH1_1786
            SEP: SE1371
            SER: SERP1258(gltA)
            SHA: SH1230(citZ)
            SSP: SSP1071
            LMO: lmo1567(citZ)
            LMF: LMOf2365_1589
            LIN: lin1602(citZ)
            LWE: lwe1580(citZ)
            LLA: L67186(gltA)
            LLM: llmg_0635(gltA)
            SMU: SMU.671(citZ)
            STC: str1267(gltA)
            STL: stu1267(gltA)
            SSA: SSA_0703
            SGO: SGO_1612(citZ)
            STH: STH2542
            CNO: NT01CX_0234
            CTH: Cthe_3027
            CKL: CKL_0044
            DSY: DSY4425
            MTA: Moth_1122
            MTU: Rv0889c(citA) Rv0896(gltA2) Rv1131(gltA1)
            MTC: MT0912(gltA-1) MT0920(gltA-2) MT1163(gltA-3)
            MBO: Mb0913c(citA) Mb0920(gltA2) Mb1162(gltA1)
            MBB: BCG_0941c(citA) BCG_0948(gltA2) BCG_1192(gltA1)
            MLE: ML2130(gltA2)
            MPA: MAP0295c(gltA1) MAP0827c(citA) MAP0829(gltA2)
            MAV: MAV_0344
            MSM: MSMEG_4035 MSMEG_5672(gltA) MSMEG_5676 MSMEG_6647
            MVA: Mvan_5022 Mvan_5025
            MGI: Mflv_1726 Mflv_1729
            MMC: Mmcs_4456 Mmcs_4459
            MKM: Mkms_4543 Mkms_4546
            MJL: Mjls_4838 Mjls_4841
            CGL: NCgl0795(cgl0829)
            CGB: cg0798(prpC1) cg0949(gltA)
            CEF: CE0905(gltA)
            CDI: DIP0785(gltA)
            CJK: jk0426(gltA)
            NFA: nfa6580(gltA) nfa6610
            RHA: RHA1_ro00355(citA1) RHA1_ro01610 RHA1_ro04993(citA2)
                 RHA1_ro04998 RHA1_ro06955 RHA1_ro08450(citA3)
                 RHA1_ro08812(citA4)
            SCO: SCO2736(citA) SCO4388(SCD10.20) SCO5832
            SMA: SAV2427(citA3) SAV3859(citA2) SAV5330(citA1)
            LXX: Lxx16220(gltA2)
            CMI: CMM_2171(gltA2) CMM_2371(gltA1)
            ART: Arth_1523 Arth_2811
            AAU: AAur_1660(gltA) AAur_2795(gltA) AAur_pTC20150(gltA)
            PAC: PPA1423 PPA2272
            NCA: Noca_0733 Noca_0888
            TFU: Tfu_0247
            FRA: Francci3_0081 Francci3_0083
            FAL: FRAAL0109 FRAAL0111(gltA) FRAAL2379(citA1) FRAAL2380
            ACE: Acel_0115 Acel_1658
            KRA: Krad_0109 Krad_1140
            SEN: SACE_0632(citA4) SACE_0633(citA) SACE_0649(gltA-2)
            STP: Strop_0423 Strop_2136
            BLO: BL1733(gltA2)
            BAD: BAD_0460(gltA2)
            RXY: Rxyl_1676 Rxyl_2556 Rxyl_2557
            RBA: RB6683(gltA)
            PCU: pc1771(gltA)
            LIL: LA0671(gltA1) LA0790(gltA2)
            LIC: LIC12829(gltA) LIC12925
            LBJ: LBJ_0747(gltA-1) LBJ_2538(gltA-2)
            LBL: LBL_0574(gltA-2) LBL_2331(gltA-1)
            SYN: sll0401(gltA)
            SYW: SYNW2275(gltA)
            SYC: syc0912_d(gltA)
            SYF: Synpcc7942_0612
            SYD: Syncc9605_2413
            SYE: Syncc9902_0279
            SYG: sync_2626(citZ)
            SYR: SynRCC307_2276(gltA)
            SYX: SynWH7803_2292(gltA)
            CYA: CYA_1739
            CYB: CYB_1908
            TEL: tlr2393
            GVI: glr3012
            ANA: alr0222(gltA)
            AVA: Ava_2713
            PMA: Pro0185(gltA)
            PMM: PMM0161(gltA)
            PMT: PMT2021(gltA)
            PMN: PMN2A_1528
            PMI: PMT9312_0163
            PMB: A9601_01791(gltA)
            PMC: P9515_01901(gltA)
            PMF: P9303_26921(gltA)
            PMG: P9301_01811(gltA)
            PMH: P9215_01791(gltA)
            PME: NATL1_02341(gltA)
            TER: Tery_1580
            BTH: BT_2070
            BFR: BF3753
            BFS: BF3541
            SRU: SRU_0488(citA)
            CHU: CHU_1275(gltA)
            GFO: GFO_2807(gltA)
            FJO: Fjoh_0367
            FPS: FP1308(gltA)
            CTE: CT1834(gltA)
            CCH: Cag_0317
            CPH: Cpha266_2083
            PVI: Cvib_0401
            PLT: Plut_0336
            RRS: RoseRS_3488
            RCA: Rcas_0581
            DRA: DR_0757
            DGE: Dgeo_1526
            TTH: TTC0978
            TTJ: TTHA1343
            AAE: aq_150(gltA)
            TMA: TM0290
            TPT: Tpet_0622
            MAC: MA0249
            MBA: Mbar_A0715
            MMA: MM_1527
            MTH: MTH1726 MTH962
            MSI: Msm_0446
            AFU: AF1340(citZ)
            HAL: VNG2102G(citZ)
            HMA: rrnAC2511(citZ)
            HWA: HQ1349A(citZ)
            NPH: NP1314A(citZ)
            TAC: Ta0169 Ta0819
            TVO: TVN0239
            PTO: PTO0889
            PFU: PF0203
            APE: APE_1713
            SSO: SSO2589
            STO: ST0587 ST1805
            SAI: Saci_0243(cisY)
            MSE: Msed_0281 Msed_1522
            PAI: PAE1689 PAE3584 PAE3585
            PIS: Pisl_1692
            PCL: Pcal_0154 Pcal_0563
            PAS: Pars_1035 Pars_2234
STRUCTURES  PDB: 1VGM  1VGP  2C6X  2H12  2IBP  2IFC  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.3.1
            ExPASy - ENZYME nomenclature database: 2.3.3.1
            ExplorEnz - The Enzyme Database: 2.3.3.1
            ERGO genome analysis and discovery system: 2.3.3.1
            BRENDA, the Enzyme Database: 2.3.3.1
            CAS: 9027-96-7
///
ENTRY       EC 2.3.3.2                  Enzyme
NAME        decylcitrate synthase;
            2-decylcitrate synthase;
            (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate oxaloacetate-lyase
            (CoA-acylating)
CLASS       Transferases;
            Acyltransferases;
            Acyl groups converted into alkyl groups on transfer
SYSNAME     dodecanoyl-CoA:oxaloacetate C-dodecanoyltransferase
            (thioester-hydrolysing, 1-carboxyundecyl-forming)
REACTION    lauroyl-CoA + H2O + oxaloacetate =
            (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate + CoA [RN:R03735]
ALL_REAC    R03735
SUBSTRATE   lauroyl-CoA [CPD:C01832];
            H2O [CPD:C00001];
            oxaloacetate [CPD:C00036]
PRODUCT     (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate [CPD:C04655];
            CoA [CPD:C00010]
REFERENCE   1  [PMID:5719165]
  AUTHORS   Mahlen A, Gatenbeck S.
  TITLE     A metabolic variation in Penicillium spiculisporum Lehman. II.
            Purification and some properties of the enzyme synthesizing
            (--)-decylcitric acid.
  JOURNAL   Acta. Chem. Scand. 22 (1968) 2617-23.
  ORGANISM  Penicillium spiculisporum
REFERENCE   2  [PMID:5099208]
  AUTHORS   Mahlen A.
  TITLE     Properties of 2-decylcitrate synthase from Penicillium spiculisporum
            Lehman.
  JOURNAL   Eur. J. Biochem. 22 (1971) 104-14.
  ORGANISM  Penicillium spiculisporum
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.3.2
            ExPASy - ENZYME nomenclature database: 2.3.3.2
            ExplorEnz - The Enzyme Database: 2.3.3.2
            ERGO genome analysis and discovery system: 2.3.3.2
            BRENDA, the Enzyme Database: 2.3.3.2
            CAS: 9068-72-8
///
ENTRY       EC 2.3.3.3                  Enzyme
NAME        citrate (Re)-synthase;
            (R)-citrate synthase;
            Re-citrate-synthase;
            citrate oxaloacetate-lyase [(pro-3R)-CH2COO-->acetyl-CoA]
CLASS       Transferases;
            Acyltransferases;
            Acyl groups converted into alkyl groups on transfer
SYSNAME     acetyl-CoA:oxaloacetate C-acetyltransferase [thioester-hydrolysing,
            (pro-R)-carboxymethyl-forming]
REACTION    acetyl-CoA + H2O + oxaloacetate = citrate + CoA [RN:R00351]
ALL_REAC    R00351
SUBSTRATE   acetyl-CoA [CPD:C00024];
            H2O [CPD:C00001];
            oxaloacetate [CPD:C00036]
PRODUCT     citrate [CPD:C00158];
            CoA [CPD:C00010]
COMMENT     This enzyme is inactivated by oxygen and is found in some anaerobes.
            Its stereospecificity is opposite to that of EC 2.3.3.1, citrate
            (Si)-synthase.
REFERENCE   1  [PMID:5808294]
  AUTHORS   Dittbrenner S, Chowdhury AA, Gottschalk G.
  TITLE     The stereospecificity of the (R)-citrates synthase in the presence
            of p-chloromercuribenzoate.
  JOURNAL   Biochem. Biophys. Res. Commun. 36 (1969) 802-8.
  ORGANISM  Clostridium acidi-urici, Clostridium kluyveri
REFERENCE   2  [PMID:4974734]
  AUTHORS   Gottschalk G.
  TITLE     Partial purification and some properties of the (R)-citrate synthase
            from Clostridium acidi-urici.
  JOURNAL   Eur. J. Biochem. 7 (1969) 301-6.
  ORGANISM  Clostridium acidi-urici
REFERENCE   3  [PMID:5958189]
  AUTHORS   Gottschalk G, Barker HA.
  TITLE     Synthesis of glutamate and citrate by Clostridium kluyveri. A new
            type of citrate synthase.
  JOURNAL   Biochemistry. 5 (1966) 1125-33.
  ORGANISM  Clostridium kluyveri
GENES       CKL: CKL_0973
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.3.3
            ExPASy - ENZYME nomenclature database: 2.3.3.3
            ExplorEnz - The Enzyme Database: 2.3.3.3
            ERGO genome analysis and discovery system: 2.3.3.3
            BRENDA, the Enzyme Database: 2.3.3.3
            CAS: 9077-70-7
///
ENTRY       EC 2.3.3.4                  Enzyme
NAME        decylhomocitrate synthase;
            2-decylhomocitrate synthase;
            3-hydroxytetradecane-1,3,4-tricarboxylate 2-oxoglutarate-lyase
            (CoA-acylating)
CLASS       Transferases;
            Acyltransferases;
            Acyl groups converted into alkyl groups on transfer
SYSNAME     dodecanoyl-CoA:2-oxoglutarate C-dodecanoyltransferase
            (thioester-hydrolysing, 1-carboxyundecyl-forming)
REACTION    dodecanoyl-CoA + H2O + 2-oxoglutarate =
            (3S,4S)-3-hydroxytetradecane-1,3,4-tricarboxylate + CoA [RN:R03859]
ALL_REAC    R03859
SUBSTRATE   dodecanoyl-CoA [CPD:C01832];
            H2O [CPD:C00001];
            2-oxoglutarate [CPD:C00026]
PRODUCT     (3S,4S)-3-hydroxytetradecane-1,3,4-tricarboxylate [CPD:C04529];
            CoA [CPD:C00010]
COMMENT     Decanoyl-CoA can act instead of dodecanoyl-CoA, but 2-oxoglutarate
            cannot be replaced by oxaloacetate or pyruvate.
REFERENCE   1  [PMID:4774124]
  AUTHORS   Mahlen A.
  TITLE     Purification and some properties of 2-decylhomocitrate synthase from
            Penicillium spiculisporum.
  JOURNAL   Eur. J. Biochem. 38 (1973) 32-9.
  ORGANISM  Penicillium spiculisporum
REFERENCE   2  [PMID:16518427]
  AUTHORS   Kumar R, Prem S, Mahapatra M, Seth T, Chowdhary DR, Mishra P, Pillai
            L, Narendra AM, Mehra NK, Saxena R, Choudhry VP.
  TITLE     Fludarabine, cyclophosphamide and horse antithymocyte globulin
            conditioning regimen for allogeneic peripheral blood stem cell
            transplantation performed in non-HEPA filter rooms for multiply
            transfused patients with severe aplastic anemia.
  JOURNAL   Bone. Marrow. Transplant. 37 (2006) 745-9.
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.3.4
            ExPASy - ENZYME nomenclature database: 2.3.3.4
            ExplorEnz - The Enzyme Database: 2.3.3.4
            ERGO genome analysis and discovery system: 2.3.3.4
            BRENDA, the Enzyme Database: 2.3.3.4
            CAS: 51845-40-0
///
ENTRY       EC 2.3.3.5                  Enzyme
NAME        2-methylcitrate synthase;
            2-methylcitrate oxaloacetate-lyase;
            MCS;
            methylcitrate synthase;
            methylcitrate synthetase
CLASS       Transferases;
            Acyltransferases;
            Acyl groups converted into alkyl groups on transfer
SYSNAME     propanoyl-CoA:oxaloacetate C-propanoyltransferase
            (thioester-hydrolysing, 1-carboxyethyl-forming)
REACTION    propanoyl-CoA + H2O + oxaloacetate =
            (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA [RN:R00931]
ALL_REAC    R00931
SUBSTRATE   propanoyl-CoA [CPD:C00100];
            H2O [CPD:C00001];
            oxaloacetate [CPD:C00036]
PRODUCT     (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate [CPD:C02225];
            CoA [CPD:C00010]
COMMENT     The enzyme acts on acetyl-CoA, propanoyl-CoA, butanoyl-CoA and
            pentanoyl-CoA. The relative rate of condensation of acetyl-CoA and
            oxaloacetate is 140% of that of propanoyl-CoA and oxaloacetate, but
            the enzyme has been separated from EC 2.3.3.1 citrate (Si)-synthase.
            Oxaloacetate cannot be replaced by glyoxylate, pyruvate or
            2-oxoglutarate.
REFERENCE   1
  AUTHORS   Uchiyama, H. and Tabuchi, T.
  TITLE     Properties of methylcitrate synthase from Candida lipolytica.
  JOURNAL   Agric. Biol. Chem. 40 (1976) 1411-1418.
  ORGANISM  Candida lipolytica
REFERENCE   2  [PMID:9325432]
  AUTHORS   Textor S, Wendisch VF, De Graaf AA, Muller U, Linder MI, Linder D,
            Buckel W.
  TITLE     Propionate oxidation in Escherichia coli: evidence for operation of
            a methylcitrate cycle in bacteria.
  JOURNAL   Arch. Microbiol. 168 (1997) 428-36.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:10482501]
  AUTHORS   Horswill AR, Escalante-Semerena JC.
  TITLE     Salmonella typhimurium LT2 catabolizes propionate via the
            2-methylcitric acid cycle.
  JOURNAL   J. Bacteriol. 181 (1999) 5615-23.
  ORGANISM  Salmonella typhimurium
REFERENCE   4  [PMID:7707698]
  AUTHORS   van Rooyen JP, Mienie LJ, Erasmus E, De Wet WJ, Ketting D, Duran M,
            Wadman SK.
  TITLE     Identification of the stereoisomeric configurations of methylcitric
            acid produced by si-citrate synthase and methylcitrate synthase
            using capillary gas chromatography-mass spectrometry.
  JOURNAL   J. Inherit. Metab. Dis. 17 (1994) 738-47.
  ORGANISM  Candida lipolytica
PATHWAY     PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K01659  2-methylcitrate synthase
GENES       DDI: DDB_0220637
            TET: TTHERM_00537060
            ECO: b0333(prpC)
            ECJ: JW0324(prpC)
            ECE: Z0428(prpC)
            ECS: ECs0386
            ECC: c0452(prpC)
            ECI: UTI89_C0364(prpC)
            ECP: ECP_0408
            ECV: APECO1_1656(prpC)
            ECW: EcE24377A_0357(prpC)
            ECX: EcHS_A0398
            STY: STY0401(prpC)
            STT: t2495(prpC)
            SPT: SPA2354(prpC)
            SEC: SC0410(prpC)
            STM: STM0369(prpC)
            PLU: plu3541(prpC)
            XCC: XCC1032(prpC)
            XCB: XC_3214
            XCV: XCV1157
            XAC: XAC1138(prpC)
            XOO: XOO0893(prpC)
            XOM: XOO_0818(XOO0818)
            VCH: VC1337
            VVU: VV1_2731
            VVY: VV1530
            VPA: VP1647
            PPR: PBPRA1247 PBPRB0236
            PAE: PA0795(prpC)
            PAU: PA14_53950(prpC)
            PPU: PP_2335
            PPF: Pput_3435
            PST: PSPTO_2288(prpC)
            PSB: Psyr_2086
            PSP: PSPPH_2057(prpC)
            PFL: PFL_1862(prpC)
            PFO: Pfl_1765
            PEN: PSEEN1903(prpC)
            PMY: Pmen_2081
            PAR: Psyc_1111(prpC)
            PCR: Pcryo_1310
            PRW: PsycPRwf_1198
            ACI: ACIAD2756(prpC)
            SON: SO_0344(prpC)
            SDN: Sden_1665
            SFR: Sfri_1858
            SAZ: Sama_3295
            SBL: Sbal_4048
            SBM: Shew185_4022
            SLO: Shew_1821
            SPC: Sputcn32_3645
            SSE: Ssed_2112
            SPL: Spea_2321
            SHE: Shewmr4_3630
            SHM: Shewmr7_0314
            SHN: Shewana3_3826
            SHW: Sputw3181_3785
            ILO: IL1426(prpC)
            CPS: CPS_2821
            PHA: PSHAa1774(prpC)
            PAT: Patl_1420
            PIN: Ping_1868
            MAQ: Maqu_1665
            CBU: CBU_0772(prpC)
            CBD: COXBU7E912_0820(prpC)
            LPN: lpg1530
            LPF: lpl1496(prpC)
            LPP: lpp1487(prpC)
            NOC: Noc_2208
            AEH: Mlg_2604
            HHA: Hhal_1071
            HCH: HCH_02711
            CSA: Csal_2420
            ABO: ABO_1432(prpC)
            MMW: Mmwyl1_0924
            AHA: AHA_2266
            NME: NMB0431
            NMA: NMA2054(prpC)
            NGO: NGO1525
            CVI: CV_2056(prpC)
            RSO: RSp0121(prpC)
            REU: Reut_A1809 Reut_A2329
            REH: H16_A1906(prpC1) H16_A2636(prpC2)
            RME: Rmet_1586
            BMA: BMAA1869
            BXE: Bxe_B2302 Bxe_B2900
            BVI: Bcep1808_3679
            BUR: Bcep18194_B0142
            BCN: Bcen_5345
            BCH: Bcen2424_5516
            BAM: Bamb_4841
            BPS: BPSS0207(prpC)
            BPM: BURPS1710b_A1737(prpC)
            BPL: BURPS1106A_A0289(prpC)
            BPD: BURPS668_A0383(prpC)
            BTE: BTH_II2188
            BPE: BP2368(prpC)
            BPA: BPP3234(prpC)
            BBR: BB3686(prpC)
            AJS: Ajs_1635
            VEI: Veis_4451
            HAR: HEAR3267(prpC)
            MMS: mma_3488
            NMU: Nmul_A0866
            HHE: HH0398(prpC)
            ABU: Abu_0277(prpC)
            GUR: Gura_0072
            RPA: RPA2394(prpC)
            RPC: RPC_3511
            PDE: Pden_1347
            SWI: Swit_4790
            ACR: Acry_0621
            RRU: Rru_A2319
            CGL: NCgl0630(cgl0659) NCgl0666(cgl0696)
            CGB: cg0762(prpC2)
            CEF: CE0718
            CJK: jk1665(prpC)
            RXY: Rxyl_2401
            PTO: PTO0169
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.3.5
            ExPASy - ENZYME nomenclature database: 2.3.3.5
            ExplorEnz - The Enzyme Database: 2.3.3.5
            ERGO genome analysis and discovery system: 2.3.3.5
            BRENDA, the Enzyme Database: 2.3.3.5
            CAS: 57827-78-8
///
ENTRY       EC 2.3.3.6                  Enzyme
NAME        2-ethylmalate synthase;
            (R)-2-ethylmalate 2-oxobutanoyl-lyase (CoA-acetylating);
            2-ethylmalate-3-hydroxybutanedioate synthase;
            propylmalate synthase;
            propylmalic synthase
CLASS       Transferases;
            Acyltransferases;
            Acyl groups converted into alkyl groups on transfer
SYSNAME     acetyl-CoA:2-oxobutanoate C-acetyltransferase
            (thioester-hydrolysing, carboxymethyl-forming)
REACTION    acetyl-CoA + H2O + 2-oxobutanoate = (R)-2-ethylmalate + CoA
            [RN:R00998]
ALL_REAC    R00998
SUBSTRATE   acetyl-CoA [CPD:C00024];
            H2O [CPD:C00001];
            2-oxobutanoate [CPD:C00109]
PRODUCT     (R)-2-ethylmalate [CPD:C02488];
            CoA [CPD:C00010]
COMMENT     Also acts on (R)-2-(n-propyl)-malate. Formerly wrongly included with
            EC 2.3.3.7 3-ethylmalate synthase.
REFERENCE   1  [PMID:6052435]
  AUTHORS   Strassman M, Ceci LN.
  TITLE     A study of acetyl-CoA condensation with alpha-keto acids.
  JOURNAL   Arch. Biochem. Biophys. 119 (1967) 420-8.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00620  Pyruvate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.3.6
            ExPASy - ENZYME nomenclature database: 2.3.3.6
            ExplorEnz - The Enzyme Database: 2.3.3.6
            ERGO genome analysis and discovery system: 2.3.3.6
            BRENDA, the Enzyme Database: 2.3.3.6
            CAS: 9024-01-5
///
ENTRY       EC 2.3.3.7                  Enzyme
NAME        3-ethylmalate synthase;
            2-ethyl-3-hydroxybutanedioate synthase;
            3-ethylmalate glyoxylate-lyase (CoA-butanoylating)
CLASS       Transferases;
            Acyltransferases;
            Acyl groups converted into alkyl groups on transfer
SYSNAME     butanoyl-CoA:glyoxylate C-butanoyltransferase
            (thioester-hydrolysing, 1-carboxypropyl-forming)
REACTION    butanoyl-CoA + H2O + glyoxylate = 3-ethylmalate + CoA [RN:R01180]
ALL_REAC    R01180
SUBSTRATE   butanoyl-CoA [CPD:C00136];
            H2O [CPD:C00001];
            glyoxylate [CPD:C00048]
PRODUCT     3-ethylmalate [CPD:C01989];
            CoA [CPD:C00010]
REFERENCE   1  [PMID:13314642]
  AUTHORS   RAMASARMA T, GIRI KV.
  TITLE     Phosphoglucose isomerase of green gram (Phaseolus radiatus).
  JOURNAL   Arch. Biochem. Biophys. 62 (1956) 91-6.
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.3.7
            ExPASy - ENZYME nomenclature database: 2.3.3.7
            ExplorEnz - The Enzyme Database: 2.3.3.7
            ERGO genome analysis and discovery system: 2.3.3.7
            BRENDA, the Enzyme Database: 2.3.3.7
            CAS: 9024-01-5
///
ENTRY       EC 2.3.3.8                  Enzyme
NAME        ATP citrate synthase;
            ATP-citric lyase;
            ATP:citrate oxaloacetate-lyase [(pro-S)-CH2COO-->acetyl-CoA]
            (ATP-dephosphorylating);
            acetyl-CoA:oxaloacetate acetyltransferase (isomerizing;
            ADP-phosphorylating);
            adenosine triphosphate citrate lyase;
            citrate cleavage enzyme;
            citrate-ATP lyase;
            citric cleavage enzyme;
            ATP citrate (pro-S)-lyase
CLASS       Transferases;
            Acyltransferases;
            Acyl groups converted into alkyl groups on transfer
SYSNAME     acetyl-CoA:oxaloacetate C-acetyltransferase
            [(pro-S)-carboxymethyl-forming, ADP-phosphorylating]
REACTION    ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA
            [RN:R00352]
ALL_REAC    R00352
SUBSTRATE   ADP [CPD:C00008];
            phosphate [CPD:C00009];
            acetyl-CoA [CPD:C00024];
            oxaloacetate [CPD:C00036]
PRODUCT     ATP [CPD:C00002];
            citrate [CPD:C00158];
            CoA [CPD:C00010]
COMMENT     The enzyme can be dissociated into components, two of which are
            identical with EC 4.1.3.34 (citryl-CoA lyase) and EC 6.2.1.18
            (citrate---CoA ligase).
REFERENCE   1  [PMID:6749502]
  AUTHORS   Lill U, Schreil A, Eggerer H.
  TITLE     Isolation of enzymically active fragments formed by limited
            proteolysis of ATP citrate lyase.
  JOURNAL   Eur. J. Biochem. 125 (1982) 645-50.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Srere, P.A. and Lipmann, F.
  TITLE     An enzymatic reaction between citrate, adenosine triphosphate and
            coenzyme A.
  JOURNAL   J. Am. Chem. Soc. 75 (1953) 4874.
  ORGANISM  pigeon
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00720  Reductive carboxylate cycle (CO2 fixation)
ORTHOLOGY   KO: K01648  ATP citrate (pro-S)-lyase
GENES       HSA: 47(ACLY)
            PTR: 454672(ACLY)
            MMU: 104112(Acly)
            RNO: 24159(Acly)
            CFA: 607852(ACLY)
            GGA: 395373(RCJMB04_6f14)
            XLA: 495086(LOC495086) 495316(LOC495316)
            XTR: 493390(acly)
            SPU: 587157(LOC587157)
            DME: Dmel_CG8322(ATPCL)
            CEL: B0365.1 D1005.1
            ATH: AT3G06650(ACLB-1) AT5G49460(ACLB-2)
            OSA: 4325777
            CME: CMB118C CMB128C
            SPO: SPAC22A12.16 SPBC1703.07
            ANI: AN2435.2 AN2436.2
            AFM: AFUA_6G10650 AFUA_6G10660
            AOR: AO090023000205 AO090023000206
            CNE: CNJ00800
            UMA: UM01005.1
            DDI: DDBDRAFT_0205386 DDBDRAFT_0205389
            TDN: Tmden_0570 Tmden_0571
            NIS: NIS_0652 NIS_0653
            SUN: SUN_0541 SUN_0542
            CCH: Cag_0797
            NPH: NP4244A(citE)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.3.8
            ExPASy - ENZYME nomenclature database: 2.3.3.8
            ExplorEnz - The Enzyme Database: 2.3.3.8
            ERGO genome analysis and discovery system: 2.3.3.8
            BRENDA, the Enzyme Database: 2.3.3.8
            CAS: 9027-95-6
///
ENTRY       EC 2.3.3.9                  Enzyme
NAME        malate synthase;
            L-malate glyoxylate-lyase (CoA-acetylating);
            glyoxylate transacetylase;
            glyoxylate transacetase;
            glyoxylic transacetase;
            malate condensing enzyme;
            malate synthetase;
            malic synthetase;
            malic-condensing enzyme
CLASS       Transferases;
            Acyltransferases;
            Acyl groups converted into alkyl groups on transfer
SYSNAME     acetyl-CoA:glyoxylate C-acetyltransferase (thioester-hydrolysing,
            carboxymethyl-forming)
REACTION    acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA [RN:R00472]
ALL_REAC    R00472
SUBSTRATE   acetyl-CoA [CPD:C00024];
            H2O [CPD:C00001];
            glyoxylate [CPD:C00048]
PRODUCT     (S)-malate [CPD:C00149];
            CoA [CPD:C00010]
REFERENCE   1  [PMID:13816984]
  AUTHORS   DIXON GH, KORNBERG HL, LUND P.
  TITLE     Purification and properties of malate synthetase.
  JOURNAL   Biochim. Biophys. Acta. 41 (1960) 217-33.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], Pseudomonas ovalis
PATHWAY     PATH: map00620  Pyruvate metabolism
            PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K01638  malate synthase
GENES       ATH: AT5G03860
            SCE: YIR031C(DAL7) YNL117W(MLS1)
            AGO: AGOS_ACR268C
            PIC: PICST_53620(MLS1.1) PICST_90814(MLS1.2)
            CGR: CAGL0L03982g
            ANI: AN6653.2
            AFM: AFUA_6G03540
            AOR: AO090009000557
            CNE: CNH02910
            UMA: UM03270.1
            TET: TTHERM_00878160
            ECO: b2976(glcB) b4014(aceB)
            ECJ: JW2943(glcB) JW3974(aceB)
            ECE: Z5600(aceB)
            ECS: ECs4932
            ECC: c3705(glcB) c4971(aceB)
            ECI: UTI89_C3392(glcB) UTI89_C4573(aceB)
            ECP: ECP_3053 ECP_4224
            ECV: APECO1_2462(aceB) APECO1_3451(glcB)
            ECW: EcE24377A_3435(glcB) EcE24377A_4556(aceB)
            ECX: EcHS_A3148(glcB) EcHS_A4248
            STY: STY4401(aceB)
            STT: t4111(aceB)
            SPT: SPA4021(aceB)
            SEC: SC4062(aceB)
            STM: STM4183(aceB)
            YPE: YPO3726(aceB)
            YPK: y0015(aceB)
            YPM: YP_3088(aceB)
            YPA: YPA_0017
            YPN: YPN_0014
            YPP: YPDSF_0173
            YPS: YPTB3657(aceB)
            YPI: YpsIP31758_0294(aceB)
            SFL: SF3015(glcB)
            SFX: S3216(glcB)
            SFV: SFV_3031(glcB)
            SSN: SSON_4186(aceB)
            SBO: SBO_4034(aceB)
            ECA: ECA3991(aceB)
            PLU: plu4396(aceB)
            ENT: Ent638_0218
            SPE: Spro_4503
            XCC: XCC0237(mls)
            XCB: XC_0247
            XCV: XCV0264
            XAC: XAC0256(mls)
            VCH: VC0734
            VCO: VC0395_A0266(aceB)
            VVU: VV1_0450
            VVY: VV0741
            VPA: VP0583
            VFI: VF1973
            PPR: PBPRA0737 PBPRA2276(aceB)
            PAE: PA0482(glcB)
            PAU: PA14_06290(glcB)
            PAP: PSPA7_0585(glcB)
            PPU: PP_0356(glcB)
            PPF: Pput_0382
            PST: PSPTO_0480(glcB-1) PSPTO_3559(glcB-2)
            PSB: Psyr_4700
            PSP: PSPPH_4734(glcB)
            PFL: PFL_5700(glcB)
            PFO: Pfl_5183
            PEN: PSEEN5127(glcB)
            PMY: Pmen_0199 Pmen_4096
            PAR: Psyc_1643
            PCR: Pcryo_1878
            PRW: PsycPRwf_1672
            ACI: ACIAD2335(glcB)
            ACB: A1S_1601
            SON: SO_1483(aceB)
            SDN: Sden_0217 Sden_1245
            SFR: Sfri_1101 Sfri_3137 Sfri_3904
            SAZ: Sama_2381
            SBL: Sbal_1316
            SBM: Shew185_1307
            SLO: Shew_1275
            SPC: Sputcn32_1238
            SSE: Ssed_1414 Ssed_2351
            SPL: Spea_1290 Spea_2043
            SHE: Shewmr4_2767 Shewmr4_3852
            SHM: Shewmr7_2845 Shewmr7_3945
            SHN: Shewana3_2943 Shewana3_4060
            SHW: Sputw3181_2866
            ILO: IL0609(aceB)
            CPS: CPS_1228(glcB) CPS_4874
            PHA: PSHAb0061(glcB)
            PAT: Patl_1213
            PIN: Ping_0303
            MAQ: Maqu_1843
            AEH: Mlg_1646
            HHA: Hhal_2247
            HCH: HCH_01653(glcB)
            CSA: Csal_3154
            ABO: ABO_1267(glcB)
            MMW: Mmwyl1_1179
            AHA: AHA_2816(aceB)
            CVI: CV_3304(aceB)
            RSO: RSc1363(aceB)
            REU: Reut_A1951
            REH: H16_A2217(aceB)
            RME: Rmet_1390
            BMA: BMA1590(aceB)
            BMV: BMASAVP1_A2092(aceB)
            BML: BMA10299_A3220(aceB)
            BMN: BMA10247_1365(aceB)
            BXE: Bxe_A1647 Bxe_A2223
            BVI: Bcep1808_1958 Bcep1808_3817 Bcep1808_6794
            BUR: Bcep18194_A5361 Bcep18194_B0029
            BCN: Bcen_5190 Bcen_6025
            BCH: Bcen2424_2052 Bcen2424_5669
            BAM: Bamb_2084 Bamb_4942
            BPS: BPSL2192(aceB)
            BPM: BURPS1710b_2617(aceB)
            BPL: BURPS1106A_2528(aceB)
            BPD: BURPS668_2475(aceB)
            BTE: BTH_I1994(aceB) BTH_II2061(glcB)
            PNU: Pnuc_1280
            BPE: BP3680(glcB)
            BPA: BPP0096(glcB)
            BBR: BB0095(glcB)
            RFR: Rfer_3581
            POL: Bpro_4517
            PNA: Pnap_3683
            AAV: Aave_0408
            AJS: Ajs_0338
            VEI: Veis_1635
            MPT: Mpe_A0159
            HAR: HEAR1688(aceB)
            MMS: mma_1942
            EBA: ebA819(glcB)
            AZO: azo1159(aceB)
            DAR: Daro_3101
            DVU: DVU0701(glcB)
            DVL: Dvul_2263
            DDE: Dde_1174
            ADE: Adeh_2998
            MXA: MXAN_6441(aceB)
            PUB: SAR11_0510(glcB)
            MLO: mlr4664
            MES: Meso_3915
            PLA: Plav_0593
            SME: SMc02581(glcB)
            SMD: Smed_3270
            ATU: Atu0047(glcB)
            ATC: AGR_C_78
            RET: RHE_CH00052(glcB)
            RLE: RL0054(glcB)
            BME: BMEI0380
            BMF: BAB1_1663
            BMS: BR1648(glcB)
            BMB: BruAb1_1636(glcB)
            BOV: BOV_1595(glcB)
            OAN: Oant_1269
            BJA: bll1474(glcB)
            BRA: BRADO1059(glcB)
            BBT: BBta_6991(glcB)
            RPA: RPA4216(glcB)
            RPB: RPB_1395
            RPC: RPC_4022
            RPD: RPD_1375
            RPE: RPE_1757
            NWI: Nwi_2765
            NHA: Nham_3565
            XAU: Xaut_4252
            CCR: CC_1765
            SIL: SPO2839(glcB)
            SIT: TM1040_0711
            RSP: RSP_1980(glcB)
            RSH: Rsph17029_0690
            RSQ: Rsph17025_3079
            JAN: Jann_1845
            RDE: RD1_3325(glcB)
            PDE: Pden_1364 Pden_4051
            MMR: Mmar10_1624
            HNE: HNE_1238(aceB)
            NAR: Saro_0885
            SAL: Sala_1935
            SWI: Swit_3838
            ELI: ELI_08910
            GBE: GbCGDNIH1_2371
            ACR: Acry_1243
            ABA: Acid345_4707
            SUS: Acid_3107 Acid_5702
            BHA: BH2133
            BAN: BA1131(aceB)
            BAR: GBAA1131(aceB)
            BAA: BA_1678
            BAT: BAS1051
            BCE: BC1127
            BCA: BCE_1228(aceB)
            BCZ: BCZK1029(aceB)
            BCY: Bcer98_0853
            BTK: BT9727_1026(aceB)
            BLI: BL02644
            BLD: BLi04208
            BCL: ABC2174
            OIH: OB2405
            GKA: GK1533
            STH: STH589
            MTU: Rv1837c(glcB)
            MTC: MT1885(aceB)
            MBO: Mb1868c(glcB)
            MBB: BCG_1872c(glcB)
            MLE: ML2069(glcB)
            MPA: MAP1549c(glcB)
            MAV: MAV_2880(glcB)
            MSM: MSMEG_3640(glcB)
            MUL: MUL_3055(glcB)
            MVA: Mvan_3097
            MGI: Mflv_3367
            MMC: Mmcs_2817
            MKM: Mkms_2861
            MJL: Mjls_2844
            CGL: NCgl2247(cgl2329)
            CGB: cg2559(aceB)
            CEF: CE2231(masZ)
            CJK: jk1932(aceB)
            NFA: nfa25030(glcB)
            RHA: RHA1_ro00899(glcB) RHA1_ro02564
            SCO: SCO0983(aceB2) SCO6243(aceB1)
            SMA: SAV2000(aceB1) SAV2044(aceB2)
            ART: Arth_0582 Arth_3433
            AAU: AAur_0721(aceB) AAur_3407(aceB)
            TFU: Tfu_0819
            FRA: Francci3_1228
            FAL: FRAAL2356(aceB) FRAAL5481(aceB)
            KRA: Krad_2227
            SEN: SACE_6756(aceB)
            RXY: Rxyl_2064
            FJO: Fjoh_1738
            RRS: RoseRS_4165
            RCA: Rcas_4376
            DRA: DR_1155 DR_A0277
            DGE: Dgeo_2611 Dgeo_2616
            TTH: TTC0130
            TTJ: TTHA0506
            SSO: SSO1334(aceB)
            SAI: Saci_2190(mas)
            PAI: PAE1287(glcB)
STRUCTURES  PDB: 1P7T  1Y8B  2GQ3  2JQX  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.3.9
            ExPASy - ENZYME nomenclature database: 2.3.3.9
            ExplorEnz - The Enzyme Database: 2.3.3.9
            ERGO genome analysis and discovery system: 2.3.3.9
            BRENDA, the Enzyme Database: 2.3.3.9
            CAS: 9013-48-3
///
ENTRY       EC 2.3.3.10                 Enzyme
NAME        hydroxymethylglutaryl-CoA synthase;
            (S)-3-hydroxy-3-methylglutaryl-CoA acetoacetyl-CoA-lyase
            (CoA-acetylating);
            3-hydroxy-3-methylglutaryl CoA synthetase;
            3-hydroxy-3-methylglutaryl coenzyme A synthase;
            3-hydroxy-3-methylglutaryl coenzyme A synthetase;
            3-hydroxy-3-methylglutaryl-CoA synthase;
            3-hydroxy-3-methylglutaryl-coenzyme A synthase;
            beta-hydroxy-beta-methylglutaryl-CoA synthase;
            HMG-CoA synthase;
            acetoacetyl coenzyme A transacetase;
            hydroxymethylglutaryl coenzyme A synthase;
            hydroxymethylglutaryl coenzyme A-condensing enzyme
CLASS       Transferases;
            Acyltransferases;
            Acyl groups converted into alkyl groups on transfer
SYSNAME     acetyl-CoA:acetoacetyl-CoA C-acetyltransferase
            (thioester-hydrolysing, carboxymethyl-forming)
REACTION    acetyl-CoA + H2O + acetoacetyl-CoA =
            (S)-3-hydroxy-3-methylglutaryl-CoA + CoA [RN:R01978]
ALL_REAC    R01978
SUBSTRATE   acetyl-CoA [CPD:C00024];
            H2O [CPD:C00001];
            acetoacetyl-CoA [CPD:C00332]
PRODUCT     (S)-3-hydroxy-3-methylglutaryl-CoA [CPD:C00356];
            CoA [CPD:C00010]
REFERENCE   1  [PMID:13449080]
  AUTHORS   RUDNEY H.
  TITLE     The biosynthesis of beta-hydroxy-beta-methylglutaric acid.
  JOURNAL   J. Biol. Chem. 227 (1957) 363-77.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00072  Synthesis and degradation of ketone bodies
            PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K01641  hydroxymethylglutaryl-CoA synthase
GENES       HSA: 3157(HMGCS1) 3158(HMGCS2)
            PTR: 461892(HMGCS1)
            MMU: 15360(Hmgcs2) 208715(Hmgcs1)
            RNO: 24450(Hmgcs2) 29637(Hmgcs1)
            CFA: 479344(HMGCS1) 607923(HMGCS2)
            BTA: 407767(HMGCS1)
            SSC: 397673(CH242-38B5.1)
            GGA: 396379(HMGCS1)
            XLA: 380091(hmgcs1) 447204(MGC80816)
            DRE: 394060(hmgcs1)
            SPU: 578259(LOC578259)
            DME: Dmel_CG4311(Hmgs)
            CEL: F25B4.6
            ATH: AT4G11820(BAP1)
            OSA: 4331418 4347614
            CME: CMM189C
            SCE: YML126C(ERG13)
            AGO: AGOS_ADL356C
            PIC: PICST_83020
            CAL: CaO19_7312(CaO19.7312)
            CGR: CAGL0H04081g
            SPO: SPAC4F8.14c(hcs)
            ANI: AN4923.2
            AFM: AFUA_3G10660 AFUA_8G07210
            AOR: AO090003000611 AO090010000487
            CNE: CNC05080 CNG02670
            UMA: UM05362.1
            ECU: ECU10_0510
            DDI: DDBDRAFT_0217522 DDB_0219924(hgsA)
            TET: TTHERM_00691190
            TBR: Tb927.8.6110
            YPE: YPO1457
            YPK: y2712(pksG)
            YPM: YP_1349(pksG)
            YPA: YPA_0750
            YPN: YPN_2521
            YPS: YPTB1475
            CBD: COXBU7E912_1931
            TCX: Tcr_1719
            DNO: DNO_0799
            BPS: BPSS1002
            BPM: BURPS1710b_A2613
            BTE: BTH_II1670
            MXA: MXAN_3948(tac) MXAN_4267(mvaS)
            BSU: BG10926(pksG)
            OIH: OB2248
            SAU: SA2334(mvaS)
            SAV: SAV2546(mvaS)
            SAM: MW2467(mvaS)
            SAR: SAR2626(mvaS)
            SAS: SAS2432
            SAC: SACOL2561
            SAB: SAB2420(mvaS)
            SAA: SAUSA300_2484
            SAO: SAOUHSC_02860
            SAJ: SaurJH9_2569
            SAH: SaurJH1_2622
            SEP: SE2110
            SER: SERP2122
            SHA: SH0508(mvaS)
            SSP: SSP0324
            LMO: lmo1415
            LMF: LMOf2365_1434(mvaS)
            LIN: lin1454
            LWE: lwe1432(mvaS)
            LLA: L13187(hmcM)
            LLC: LACR_1666
            LLM: llmg_0929(hmcM)
            SPY: SPy_0881(mvaS.2)
            SPZ: M5005_Spy_0687(mvaS.1)
            SPM: spyM18_0942(mvaS2)
            SPG: SpyM3_0600(mvaS.2)
            SPS: SPs1253
            SPH: MGAS10270_Spy0745(mvaS1)
            SPI: MGAS10750_Spy0779(mvaS1)
            SPJ: MGAS2096_Spy0759(mvaS1)
            SPK: MGAS9429_Spy0743(mvaS1)
            SPF: SpyM51121(mvaS)
            SPA: M6_Spy0704
            SPB: M28_Spy0667(mvaS.1)
            SPN: SP_1727
            SPR: spr1571(mvaS)
            SPD: SPD_1537(mvaS)
            SAG: SAG1316
            SAN: gbs1386
            SAK: SAK_1347
            SMU: SMU.943c
            STC: str0577(mvaS)
            STL: stu0577(mvaS)
            SSA: SSA_0338(mvaS)
            SGO: SGO_0244
            LPL: lp_2067(mvaS)
            LJO: LJ1607
            LAC: LBA0628(hmcS)
            LSA: LSA1484(mvaS)
            LSL: LSL_0526
            LDB: Ldb0881(mvaS)
            LBU: LBUL_0806
            LBR: LVIS_1363
            LCA: LSEI_1785
            LRE: Lreu_0676
            EFA: EF1363
            OOE: OEOE_0968
            NFA: nfa22120
            SEN: SACE_4570(pksG)
            BBU: BB0683
            BGA: BG0706
            BAF: BAPKO_0727
            FJO: Fjoh_0678
            HAL: VNG1615G(mvaB)
            HMA: rrnAC1740(mvaS)
            HWA: HQ2868A(mvaB)
            NPH: NP2608A(mvaB_1) NP4836A(mvaB_2)
STRUCTURES  PDB: 1XPK  1XPL  1XPM  2P8U  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.3.10
            ExPASy - ENZYME nomenclature database: 2.3.3.10
            ExplorEnz - The Enzyme Database: 2.3.3.10
            ERGO genome analysis and discovery system: 2.3.3.10
            BRENDA, the Enzyme Database: 2.3.3.10
            CAS: 9027-44-5
///
ENTRY       EC 2.3.3.11                 Enzyme
NAME        2-hydroxyglutarate synthase;
            2-hydroxyglutaratic synthetase;
            2-hydroxyglutaric synthetase;
            alpha-hydroxyglutarate synthase;
            hydroxyglutarate synthase;
            2-hydroxyglutarate glyoxylate-lyase (CoA-propanoylating)
CLASS       Transferases;
            Acyltransferases;
            Acyl groups converted into alkyl groups on transfer
SYSNAME     propanoyl-CoA:glyoxylate C-propanoyltransferase
            (thioester-hydrolysing, 2-carboxyethyl-forming)
REACTION    propanoyl-CoA + H2O + glyoxylate = 2-hydroxyglutarate + CoA
            [RN:R00932]
ALL_REAC    R00932
SUBSTRATE   propanoyl-CoA [CPD:C00100];
            H2O [CPD:C00001];
            glyoxylate [CPD:C00048]
PRODUCT     2-hydroxyglutarate [CPD:C02630];
            CoA [CPD:C00010]
REFERENCE   1
  AUTHORS   Reeves, H.C. and Ajl, S.J.
  TITLE     alpha-Hydroxyglutaric acid synthetase.
  JOURNAL   J. Bacteriol. 84 (1962) 186-187.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00660  C5-Branched dibasic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.3.11
            ExPASy - ENZYME nomenclature database: 2.3.3.11
            ExplorEnz - The Enzyme Database: 2.3.3.11
            ERGO genome analysis and discovery system: 2.3.3.11
            BRENDA, the Enzyme Database: 2.3.3.11
            CAS: 9024-02-6
///
ENTRY       EC 2.3.3.12                 Enzyme
NAME        3-propylmalate synthase;
            3-(n-propyl)-malate synthase;
            3-propylmalate glyoxylate-lyase (CoA-pentanoylating);
            beta-n-propylmalate synthase;
            n-propylmalate synthase
CLASS       Transferases;
            Acyltransferases;
            Acyl groups converted into alkyl groups on transfer
SYSNAME     pentanoyl-CoA:glyoxylate C-pentanoyltransferase
            (thioester-hydrolysing, 1-carboxybutyl-forming)
REACTION    pentanoyl-CoA + H2O + glyoxylate = 3-propylmalate + CoA [RN:R03040]
ALL_REAC    R03040
SUBSTRATE   pentanoyl-CoA [CPD:C00888];
            H2O [CPD:C00001];
            glyoxylate [CPD:C00048]
PRODUCT     3-propylmalate [CPD:C02123];
            CoA [CPD:C00010]
REFERENCE   1  [PMID:14085361]
  AUTHORS   IMAI K, REEVES HC, AJL SJ.
  TITLE     N-PROPYLMALATE SYNTHETASE.
  JOURNAL   J. Biol. Chem. 238 (1963) 3193-8.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.3.12
            ExPASy - ENZYME nomenclature database: 2.3.3.12
            ExplorEnz - The Enzyme Database: 2.3.3.12
            ERGO genome analysis and discovery system: 2.3.3.12
            BRENDA, the Enzyme Database: 2.3.3.12
            CAS: 37290-62-3
///
ENTRY       EC 2.3.3.13                 Enzyme
NAME        2-isopropylmalate synthase;
            3-carboxy-3-hydroxy-4-methylpentanoate 3-methyl-2-oxobutanoate-lyase
            (CoA-acetylating);
            alpha-isopropylmalate synthetase;
            alpha-isopropylmalate synthase;
            alpha-isopropylmalic synthetase;
            isopropylmalate synthase;
            isopropylmalate synthetase
CLASS       Transferases;
            Acyltransferases;
            Acyl groups converted into alkyl groups on transfer
SYSNAME     acetyl-CoA:3-methyl-2-oxobutanoate C-acetyltransferase
            (thioester-hydrolysing, carboxymethyl-forming)
REACTION    acetyl-CoA + 3-methyl-2-oxobutanoate + H2O = (2S)-2-isopropylmalate
            + CoA [RN:R01213]
ALL_REAC    R01213
SUBSTRATE   acetyl-CoA [CPD:C00024];
            3-methyl-2-oxobutanoate [CPD:C00141];
            H2O [CPD:C00001]
PRODUCT     (2S)-2-isopropylmalate [CPD:C02504];
            CoA [CPD:C00010]
COFACTOR    Potassium [CPD:C00238]
COMMENT     Requires K+.
REFERENCE   1  [PMID:4976555]
  AUTHORS   Kohlhaw G, Leary TR, Umbarger HE.
  TITLE     Alpha-isopropylmalate synthase from Salmonella typhimurium.
            Purification and properties.
  JOURNAL   J. Biol. Chem. 244 (1969) 2218-25.
  ORGANISM  Salmonella typhimurium
REFERENCE   2
  AUTHORS   Webster, R.E. and Gross, S.R.
  TITLE     The alpha-isopropylmalate synthetase of Neurospora. I. The kinetics
            and end product control of alpha-isopropylmalate synthetase
            function.
  JOURNAL   Biochemistry 4 (1965) 2309-2327.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   3  [PMID:4270046]
  AUTHORS   Cole FE, Kalyanpur MG, Stevens CM.
  TITLE     Absolute configuration of alpha isopropylmalate and the mechanism of
            its conversion to beta isopropylmalate in the biosynthesis of
            leucine.
  JOURNAL   Biochemistry. 12 (1973) 3346-50.
  ORGANISM  Salmonella typhimurium, Neurospora crassa [GN:dncr]
PATHWAY     PATH: map00290  Valine, leucine and isoleucine biosynthesis
            PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K01649  2-isopropylmalate synthase
GENES       ATH: AT1G18500(IPMS1/MAML-4) AT1G74040(IMS1) AT5G23010(MAM1)
                 AT5G23020(MAM-L)
            OSA: 4351460
            CME: CMO208C CMQ337C
            SCE: YNL104C(LEU4)
            AGO: AGOS_ADL015C AGOS_AFL229W
            PIC: PICST_68770(LEU4)
            CAL: CaO19.4506
            CGR: CAGL0G06732g
            ANI: AN0840.2
            AFM: AFUA_1G15000
            AOR: AO090005001230
            CNE: CNH01520
            UMA: UM04156.1
            ECO: b0074(leuA)
            ECJ: JW0073(leuA)
            ECE: Z0083(leuA)
            ECS: ECs0078
            ECC: c0091(leuA)
            ECI: UTI89_C0081(leuA)
            ECP: ECP_0076
            ECW: EcE24377A_0077(leuA)
            ECX: EcHS_A0079(leuA)
            STY: STY0132(leuA)
            STT: t0117(leuA)
            SPT: SPA0115(leuA)
            SEC: SC0109(leuA)
            STM: STM0113(leuA)
            YPE: YPO0533(leuA)
            YPK: y3645(leuA)
            YPM: YP_3649(leuA)
            YPA: YPA_3564
            YPN: YPN_0403
            YPS: YPTB0672(leuA)
            YPI: YpsIP31758_3405(leuA)
            SFL: SF0069(leuA)
            SFX: S0071(leuA)
            SFV: SFV_0066(leuA)
            SSN: SSON_0081(leuA)
            SBO: SBO_0061(leuA)
            SDY: SDY_0101(leuA)
            ECA: ECA3831(leuA)
            PLU: plu3673(leuA)
            BUC: BUpL04(leuA)
            BAB: bbp493(leuA)
            SGL: SG0437
            BFL: Bfl133(leuA)
            BPN: BPEN_137(leuA)
            HIN: HI0986(leuA)
            HIT: NTHI1160(leuA)
            HIP: CGSHiEE_07040
            HSO: HS_0392(leuA)
            PMU: PM1962(leuA)
            MSU: MS0599(leuA)
            APL: APL_0393(leuA)
            XFA: XF1818
            XFT: PD1047(leuA)
            XCC: XCC3327(leuA)
            XCB: XC_0837
            XCV: XCV3583(leuA)
            XAC: XAC3455(leuA)
            XOO: XOO0941(leuA)
            XOM: XOO_0861(XOO0861)
            VCH: VC2490
            VCO: VC0395_A2065(leuA)
            VVU: VV1_0654
            VVY: VV0487
            VPA: VP0346
            VFI: VF0295
            PPR: PBPRA0419
            PAE: PA1217 PA3792(leuA)
            PAU: PA14_15030(leuA) PA14_48570
            PAP: PSPA7_1323(leuA2) PSPA7_2117(leuA1)
            PPU: PP_1025(leuA)
            PST: PSPTO_1444(leuA)
            PSB: Psyr_1257
            PSP: PSPPH_1329(leuA)
            PFL: PFL_4123 PFL_4946(leuA)
            PFO: Pfl_4594
            PEN: PSEEN4399(leuA)
            PMY: Pmen_3492
            PAR: Psyc_1229(leuA)
            PCR: Pcryo_1162
            ACI: ACIAD0530(leuA)
            SON: SO_4236(leuA)
            SDN: Sden_0334
            SFR: Sfri_3820
            SHE: Shewmr4_3588
            SHM: Shewmr7_0368
            SHN: Shewana3_3761
            CPS: CPS_4208(leuA)
            PHA: PSHAa2894(leuA)
            PAT: Patl_1479 Patl_3268
            SDE: Sde_2298 Sde_2523
            MCA: MCA2275(leuA)
            FTU: FTT0252(leuA)
            FTF: FTF0252(leuA)
            FTL: FTL_0129 FTL_0130
            FTA: FTA_0141 FTA_0960
            FTN: FTN_0062(leuA)
            TCX: Tcr_0611 Tcr_1878
            NOC: Noc_2516
            AEH: Mlg_0551
            HCH: HCH_05146(leuA1) HCH_05908(leuA2)
            CSA: Csal_2515 Csal_2535
            ABO: ABO_0638(leuA) ABO_2437(leuA)
            AHA: AHA_0882(leuA-1) AHA_2722(leuA-2)
            CRP: CRP_078
            VOK: COSY_0415(leuA)
            NME: NMB1070
            NMA: NMA1270(leuA)
            NMC: NMC1034(leuA)
            NGO: NGO0848
            CVI: CV_0595(leuA)
            RSO: RSc2072(leuA1) RSp0322(leuA2)
            REU: Reut_A0953 Reut_A1687
            REH: H16_A1041(leuA1) H16_B0081(leuA2)
            RME: Rmet_0918 Rmet_5887
            BMA: BMA3135(leuA)
            BMV: BMASAVP1_A0104(leuA-1) BMASAVP1_A1118(leuA-2)
            BML: BMA10299_A1484(leuA)
            BMN: BMA10247_0401(leuA-2) BMA10247_2913(leuA-1)
            BXE: Bxe_A1435 Bxe_A3225
            BVI: Bcep1808_2917
            BUR: Bcep18194_A5587 Bcep18194_A6142 Bcep18194_B2932
            BCN: Bcen_1648 Bcen_2198 Bcen_4981
            BCH: Bcen2424_2259 Bcen2424_2812 Bcen2424_3179
            BAM: Bamb_2298 Bamb_2872
            BPS: BPSL0507 BPSL1201(leuA)
            BPM: BURPS1710b_0734(leuA) BURPS1710b_1424(leuA)
            BPL: BURPS1106A_0567(leuA) BURPS1106A_1286(leuA)
            BPD: BURPS668_0551(leuA) BURPS668_1279(leuA)
            BTE: BTH_I0459(leuA-1) BTH_I1050(leuA-2)
            BPE: BP0131(leuA) BP0287(leuA)
            BPA: BPP0427(leuA) BPP4338(leuA)
            BBR: BB0429(leuA) BB4924(leuA)
            RFR: Rfer_2345
            POL: Bpro_2321 Bpro_2322
            AAV: Aave_0019
            AJS: Ajs_1773
            MPT: Mpe_A2101
            HAR: HEAR1035 HEAR1242(leuA)
            MMS: mma_1198(leuA2) mma_2145(leuA1)
            NEU: NE1320(leuA1)
            NET: Neut_1244
            NMU: Nmul_A0453
            EBA: ebA7154(leuA)
            AZO: azo3162(leuA1) azo3523(leuA2)
            DAR: Daro_0511 Daro_3071
            TBD: Tbd_1986
            MFA: Mfla_0517 Mfla_0748
            HHE: HH1137(leuA)
            WSU: WS0624(leuA)
            TDN: Tmden_1890
            CJE: Cj1719c(leuA)
            CJR: CJE1889(leuA)
            CJJ: CJJ81176_0017(leuA)
            CJU: C8J_1625(leuA)
            CJD: JJD26997_2096(leuA)
            CFF: CFF8240_1344(leuA)
            CCV: CCV52592_0766 CCV52592_1193(leuA)
            CHA: CHAB381_0491(leuA)
            CCO: CCC13826_0438(leuA)
            ABU: Abu_0456(leuA1) Abu_1570(leuA2)
            NIS: NIS_1407(leuA)
            SUN: SUN_1956(leuA)
            GSU: GSU1798 GSU1906(leuA)
            GME: Gmet_1265 Gmet_1879
            PCA: Pcar_1007 Pcar_1907
            DVU: DVU1914 DVU2981(leuA)
            DDE: Dde_2049 Dde_3218
            DPS: DP0660 DP2768
            ADE: Adeh_1981 Adeh_2071 Adeh_3037
            AFW: Anae109_1753
            MXA: MXAN_1284
            SAT: SYN_00090 SYN_02194
            SFU: Sfum_0306
            PUB: SAR11_1147 SAR11_1374(leuA)
            MLO: mlr2792 mlr7805
            MES: Meso_0969 Meso_2190
            PLA: Plav_0013
            SME: SMc02546(leuA2) SMc02717(leuA1)
            ATU: Atu2264(leuA)
            ATC: AGR_C_4114
            RET: RHE_CH01419(leuA1) RHE_CH03067(leuA2)
            RLE: RL1538(leuA) RL3513(leuA)
            BME: BMEI0451 BMEI1270 BMEI1271
            BMF: BAB1_0699 BAB1_0701 BAB1_1583(leuA)
            BMS: BR0679 BR1566(leuA)
            BMB: BruAb1_0698 BruAb1_1555(leuA)
            BOV: BOV_1513(leuA)
            BJA: bll6435(leuA) blr3792
            BRA: BRADO5528(leuA)
            BBT: BBta_6044(leuA)
            RPA: RPA2000(leuA) RPA2046(leuI) RPA4665(leuA)
            RPB: RPB_3330 RPB_3371
            RPC: RPC_2089 RPC_3235
            RPD: RPD_2069 RPD_2112
            RPE: RPE_2002 RPE_2209
            NWI: Nwi_1231 Nwi_2338
            NHA: Nham_1490 Nham_2715
            XAU: Xaut_4715
            CCR: CC_1541
            SIL: SPO0422(leuA) SPO2130
            SIT: TM1040_1154 TM1040_2282
            RSP: RSP_2330(leuA) RSP_2723 RSP_4159
            JAN: Jann_1959 Jann_3643
            RDE: RD1_1211(leuA) RD1_3182
            HNE: HNE_0440(leuA)
            ZMO: ZMO0903(leuA)
            NAR: Saro_2267
            SAL: Sala_0974
            ELI: ELI_05465
            GOX: GOX1733
            GBE: GbCGDNIH1_1472
            RRU: Rru_A0695 Rru_A1461 Rru_A1928
            MAG: amb2130 amb3468 amb3512
            MGM: Mmc1_0903 Mmc1_0967 Mmc1_2965
            BSU: BG11948(leuA)
            BHA: BH3058(leuA)
            BAN: BA1420(leuA)
            BAR: GBAA1420(leuA)
            BAA: BA_1940
            BAT: BAS1311
            BCE: BC1400
            BCA: BCE_1520(leuA)
            BCZ: BCZK1285(leuA)
            BTK: BT9727_1284(leuA)
            BLI: BL00611(leuA)
            BLD: BLi02958(leuA)
            BCL: ABC2642(leuA)
            BPU: BPUM_0582 BPUM_2469(leuA)
            OIH: OB2620(leuA)
            GKA: GK2658
            SAU: SA1862(leuA)
            SAV: SAV2057(leuA)
            SAM: MW1981(leuA)
            SAR: SAR2144(leuA)
            SAS: SAS1962
            SAC: SACOL2046(leuA)
            SAB: SAB1942(leuA)
            SAA: SAUSA300_2010(leuA)
            SAO: SAOUHSC_00914 SAOUHSC_02285
            SAJ: SaurJH9_0976
            SAH: SaurJH1_0995
            SEP: SE1658
            SER: SERP1669(leuA)
            SHA: SH0976(leuA)
            SSP: SSP0821
            LMO: lmo1987(leuA)
            LMF: LMOf2365_2010(leuA)
            LIN: lin2094(leuA)
            LWE: lwe2006(leuA)
            LLC: LACR_1323
            SPN: SP_1258
            SPR: spr1136 spr1137
            SMU: SMU.1384(leuA)
            STC: str1203(leuA)
            STL: stu1203(leuA)
            SSA: SSA_0975(leuA)
            SGO: SGO_0906(leuA)
            OOE: OEOE_1723
            STH: STH1988 STH2687
            CAC: CAC0273 CAC3174(leuA)
            CDF: CD0989(leuA)
            CBE: Cbei_0213 Cbei_2175
            CKL: CKL_0047(leuA1) CKL_2160(leuA2)
            CHY: CHY_0521(leuA) CHY_0525
            DSY: DSY4310
            SWO: Swol_2139 Swol_2143
            TTE: TTE0016(leuA)
            MTA: Moth_2251 Moth_2255
            MTU: Rv3710(leuA)
            MTC: MT3813(leuA)
            MBO: Mb3737(leuA)
            MBB: BCG_3770(leuA)
            MLE: ML2324(leuA)
            MPA: MAP0312(leuA)
            MAV: MAV_0392(leuA)
            MSM: MSMEG_6271(leuA)
            MGI: Mflv_1293
            MMC: Mmcs_4898
            MKM: Mkms_4987
            MJL: Mjls_5266
            CGL: NCgl0245(cgl0248)
            CGB: cg0303(leuA)
            CEF: CE0216(leuA)
            CDI: DIP0266(leuA)
            CJK: jk2002(leuA)
            NFA: nfa30390(leuA2) nfa3080(leuA)
            RHA: RHA1_ro04225(leuA1) RHA1_ro05165(leuA2)
            SCO: SCO2528(leuA) SCO5529(SC1C2.10)
            SMA: SAV2710(leuA1) SAV5601(leuA2)
            LXX: Lxx14490(leuA)
            CMI: CMM_1576(leuA)
            ART: Arth_2226
            AAU: AAur_2225(leuA)
            PAC: PPA0941
            NCA: Noca_3364
            TFU: Tfu_0617 Tfu_0850
            FRA: Francci3_3628 Francci3_3635
            FAL: FRAAL5838(leuA2) FRAAL5846(leuA)
            ACE: Acel_0712 Acel_0794
            KRA: Krad_3377
            SEN: SACE_0274(leuA) SACE_5707(leuA2) SACE_6151(leuA2)
            STP: Strop_0224 Strop_1243
            BLO: BL0488(leuA)
            BAD: BAD_0145
            RXY: Rxyl_3129 Rxyl_3131
            RBA: RB12756(leuA) RB1317(leuA)
            LIL: LA0469(leuA2) LA2202(leuA1) LA2350(cimA)
            LIC: LIC10409 LIC11597(leuA2) LIC11726(leuA)
            LBJ: LBJ_1280(leuA-3) LBJ_1362(leuA-2) LBJ_2321(leuA-1)
            LBL: LBL_0786(leuA-1) LBL_1505(leuA-3) LBL_1587(leuA-2)
            SYN: sll1564(leuA) slr0186(leuA)
            SYW: SYNW0730(leuA)
            SYC: syc0145_d(leuA) syc1089_d(leuA)
            SYF: Synpcc7942_0428 Synpcc7942_1410
            SYD: Syncc9605_1939
            SYE: Syncc9902_0727
            SYG: sync_0976(leuA)
            SYR: SynRCC307_0746(leuA)
            SYX: SynWH7803_1586(leuA)
            CYA: CYA_0566 CYA_2223(leuA)
            CYB: CYB_1307 CYB_1442(leuA)
            TEL: tll1397(leuA) tlr0850
            GVI: gll0421(leuA) gll2290(leuA)
            ANA: alr3522(leuA) alr4840(leuA)
            AVA: Ava_2111 Ava_3216
            PMA: Pro1134(leuA)
            PMM: PMM1066(leuA)
            PMT: PMT1121(leuA)
            PMN: PMN2A_0686
            PMI: PMT9312_1077
            PMB: A9601_11711(leuA)
            PMC: P9515_11561(leuA)
            PMF: P9303_09181(leuA)
            PMG: P9301_11721(leuA)
            PMH: P9215_12011(leuA)
            PME: NATL1_15201(leuA)
            TER: Tery_0286 Tery_2253 Tery_3757
            BTH: BT_1858 BT_1861
            BFR: BF3445(leuA) BF3448(leuA)
            BFS: BF3264 BF3267(leuA)
            SRU: SRU_2149(leuA) SRU_2154
            CHU: CHU_3741(leuA)
            GFO: GFO_2095(leuA)
            CTE: CT0612(leuA-1) CT2107(leuA-2)
            CCH: Cag_1673 Cag_1898
            CPH: Cpha266_0846
            PLT: Plut_0138 Plut_0599 Plut_0602
            DET: DET0825 DET0830(leuA)
            DEH: cbdb_A803 cbdb_A808(leuA)
            DEB: DehaBAV1_0744 DehaBAV1_1360
            DRA: DR_1482
            DGE: Dgeo_0599
            TTH: TTC0847 TTC0849
            TTJ: TTHA1208 TTHA1210
            AAE: aq_2090(leuA2) aq_356(leuA1)
            TMA: TM0552 TM0553
            MJA: MJ0503 MJ1195
            MMP: MMP0153(aksA) MMP1063(leuA)
            MAC: MA3342(leuA) MA4615(leuA)
            MBA: Mbar_A0942 Mbar_A2192
            MMA: MM_1284 MM_2785
            MBU: Mbur_0854 Mbur_1781
            MHU: Mhun_2360
            MTH: MTH1481 MTH1630
            MST: Msp_0199(leuA1) Msp_1099(leuA2)
            MSI: Msm_0722 Msm_1246
            MKA: MK0391 MK1209(leuA)
            AFU: AF0219(leuA-2) AF0957(leuA-1)
            HMA: rrnAC0329(leuA2) rrnAC1690(leuA1)
            HWA: HQ1292A(leuA)
            NPH: NP0624A(leuA_2) NP2206A(leuA_1) NP2994A(leuA_3)
            TVO: TVN0909
            PTO: PTO0913 PTO1466
            PHO: PH1727
            PAB: PAB0286(leuA-2) PAB0890(leuA-1) PAB0894(leuA-3)
            PFU: PF0937 PF0941 PF1678
            TKO: TK0283
            RCI: LRC535(leuA-1) RCIX1793(leuA-3) RCIX2647(leuA-4)
                 RCIX673(leuA-2)
            SSO: SSO0127(leuA-1) SSO0977(leuA-2) SSO2407(leuA-3)
            STO: ST0538 ST1301 ST2203
            SAI: Saci_0940 Saci_1304
            PAI: PAE1330(leuA) PAE1986 PAE1993
STRUCTURES  PDB: 1SR9  
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.3.13
            ExPASy - ENZYME nomenclature database: 2.3.3.13
            ExplorEnz - The Enzyme Database: 2.3.3.13
            ERGO genome analysis and discovery system: 2.3.3.13
            BRENDA, the Enzyme Database: 2.3.3.13
            CAS: 9030-98-2
///
ENTRY       EC 2.3.3.14                 Enzyme
NAME        homocitrate synthase;
            2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase
            (CoA-acetylating);
            acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase;
            homocitrate synthetase
CLASS       Transferases;
            Acyltransferases;
            Acyl groups converted into alkyl groups on transfer
SYSNAME     acetyl-CoA:2-oxoglutarate C-acetyltransferase
            (thioester-hydrolysing, carboxymethyl forming)
REACTION    acetyl-CoA + H2O + 2-oxoglutarate =
            (R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA [RN:R00271]
ALL_REAC    R00271
SUBSTRATE   acetyl-CoA [CPD:C00024];
            H2O [CPD:C00001];
            2-oxoglutarate [CPD:C00026]
PRODUCT     (R)-2-hydroxybutane-1,2,4-tricarboxylate;
            CoA [CPD:C00010]
COMMENT     Belongs in the alpha-aminoadipate pathway of lysine synthesis, along
            with EC 4.2.1.36, homoaconitate hydratase. The enzyme also acts with
            oxaloacetate as substrate, but more slowly [2,3].
REFERENCE   1  [PMID:5836514]
  AUTHORS   Strassman M, Ceci LN.
  TITLE     Enzymatic formation of homocitric acid, an intermediate in lysine
            biosynthesis.
  JOURNAL   Biochem. Biophys. Res. Commun. 14 (1964) 262-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:12095615]
  AUTHORS   Wulandari AP, Miyazaki J, Kobashi N, Nishiyama M, Hoshino T, Yamane
            H.
  TITLE     Characterization of bacterial homocitrate synthase involved in
            lysine biosynthesis.
  JOURNAL   FEBS. Lett. 522 (2002) 35-40.
REFERENCE   3  [PMID:15362863]
  AUTHORS   Andi B, West AH, Cook PF.
  TITLE     Kinetic mechanism of histidine-tagged homocitrate synthase from
            Saccharomyces cerevisiae.
  JOURNAL   Biochemistry. 43 (2004) 11790-5.
PATHWAY     PATH: map00300  Lysine biosynthesis
            PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K01655  homocitrate synthase
GENES       SCE: YDL131W(LYS21) YDL182W(LYS20)
            AGO: AGOS_ADR107W
            PIC: PICST_28701(LYS21) PICST_89386(LYS22)
            CAL: CaO19.4506
            CGR: CAGL0J06402g CAGL0J09240g
            SPO: SPBC1105.02c
            ANI: AN1990.2
            AFM: AFUA_4G10460
            AOR: AO090003001165
            CNE: CND01200
            UMA: UM04115.1
            ECA: ECA2944(nifV)
            MCA: MCA0254(nifV)
            BXE: Bxe_B1438
            AZO: azo0551(nifV)
            DAR: Daro_1398
            WSU: WS1396(nifV1)
            GSU: GSU0937(nifV)
            GME: Gmet_0692
            ADE: Adeh_1436
            BRA: BRADO3681(hmgL) BRADO5390(nifV)
            BBT: BBta_4049(hmgL) BBta_5875(nifV)
            RPA: RPA4607(nifV)
            RPB: RPB_0982
            RPC: RPC_4450
            RPD: RPD_1086
            RPE: RPE_4520
            RSP: RSP_0529(nifV)
            ZMO: ZMO1835(nifV)
            RRU: Rru_A2269
            MAG: amb1562
            MGM: Mmc1_1190
            CBE: Cbei_2012
            CKL: CKL_1757(nifV1) CKL_1758(nifV2)
            CHY: CHY_1104(nifV)
            DSY: DSY3883 DSY4262
            TTE: TTE0472(leuA2)
            MTA: Moth_1938
            FRA: Francci3_4489
            FAL: FRAAL6814(nifV)
            CYA: CYA_1820(nifV)
            CYB: CYB_0424(nifV)
            ANA: alr1407(nifV1) alr2968(nifV2)
            AVA: Ava_0938 Ava_3956 Ava_4041
            CTE: CT1528(nifV)
            CCH: Cag_1229
            PLT: Plut_1526
            DET: DET1614
            DEH: cbdb_A1708
            DRA: DR_1238
            DGE: Dgeo_1257
            TTH: TTC1550
            TTJ: TTHA1914
            NPH: NP2994A(leuA_3)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.3.14
            ExPASy - ENZYME nomenclature database: 2.3.3.14
            ExplorEnz - The Enzyme Database: 2.3.3.14
            ERGO genome analysis and discovery system: 2.3.3.14
            BRENDA, the Enzyme Database: 2.3.3.14
            CAS: 9075-60-9
///
ENTRY       EC 2.3.3.15                 Enzyme
NAME        sulfoacetaldehyde acetyltransferase;
            Xsc
CLASS       Transferases;
            Acyltransferases;
            Acyl groups converted into alkyl groups on transfer
SYSNAME     acetyl-phosphate:sulfite S-acetyltransferase (acyl-phosphate
            hydrolysing, 2-oxoethyl-forming)
REACTION    acetyl phosphate + sulfite = 2-sulfoacetaldehyde + phosphate
            [RN:R05651]
ALL_REAC    R05651
SUBSTRATE   acetyl phosphate [CPD:C00227];
            sulfite [CPD:C00094]
PRODUCT     2-sulfoacetaldehyde [CPD:C00593];
            phosphate [CPD:C00009]
COMMENT     The reaction occurs in the reverse direction to that shown above.
            Requires Mg2+.
REFERENCE   1  [PMID:12358600]
  AUTHORS   Ruff J, Denger K, Cook AM.
  TITLE     Sulphoacetaldehyde acetyltransferase yields acetyl phosphate:
            purification from Alcaligenes defragrans and gene clusters in
            taurine degradation.
  JOURNAL   Biochem. J. 369 (2003) 275-85.
  ORGANISM  Alcaligenes defragrans
PATHWAY     PATH: map00430  Taurine and hypotaurine metabolism
ORTHOLOGY   KO: K03852  sulfoacetaldehyde acetyltransferase
GENES       REH: H16_B1870(xsc)
            BUR: Bcep18194_B1993
            DPS: DP0872
            SME: SMb21530(ilvB2)
            RPE: RPE_3201
            SIL: SPO3561(xsc)
            RDE: RD1_0826(xsc) RD1_0977(xsc)
DBLINKS     IUBMB Enzyme Nomenclature: 2.3.3.15
            ExPASy - ENZYME nomenclature database: 2.3.3.15
            ExplorEnz - The Enzyme Database: 2.3.3.15
            ERGO genome analysis and discovery system: 2.3.3.15
            BRENDA, the Enzyme Database: 2.3.3.15
///
ENTRY       EC 2.3.3.-                  Enzyme
CLASS       Transferases;
            Acyltransferases;
            Acyl groups converted into alkyl on transfer
REACTION    Acetyl-CoA + Pyruvate + H2O <=> (R)-2-Methylmalate + CoA [RN:R07399]
SUBSTRATE   Acetyl-CoA [CPD:C00024];
            Pyruvate [CPD:C00022];
            H2O [CPD:C00001]
PRODUCT     (R)-2-Methylmalate [CPD:C02612];
            CoA [CPD:C00010]
///
ENTRY       EC 2.3.-.-                  Enzyme
CLASS       Transferases;
            Acyltransferases
REACTION    G00144 + Palmitoyl-CoA <=> G00145 + CoA [RN:R05918]
SUBSTRATE   [GL:G00144];
            Palmitoyl-CoA [CPD:C00154]
PRODUCT     [GL:G00145];
            CoA [CPD:C00010]
///
ENTRY       EC 2.4.1.1                  Enzyme
NAME        phosphorylase;
            muscle phosphorylase a and b;
            amylophosphorylase;
            polyphosphorylase;
            amylopectin phosphorylase;
            glucan phosphorylase;
            alpha-glucan phosphorylase;
            1,4-alpha-glucan phosphorylase;
            glucosan phosphorylase;
            glycogen phosphorylase;
            granulose phosphorylase;
            maltodextrin phosphorylase;
            muscle phosphorylase;
            myophosphorylase;
            potato phosphorylase;
            starch phosphorylase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     1,4-alpha-D-glucan:phosphate alpha-D-glucosyltransferase
REACTION    (1,4-alpha-D-glucosyl)n + phosphate = (1,4-alpha-D-glucosyl)n-1 +
            alpha-D-glucose 1-phosphate [RN:R01821 R06050]
ALL_REAC    R01821 R06050(G);
            (other) R02111 R06185(G)
SUBSTRATE   (1,4-alpha-D-glucosyl)n [CPD:C00718];
            phosphate [CPD:C00009]
PRODUCT     (1,4-alpha-D-glucosyl)n-1 [CPD:C00718];
            alpha-D-glucose 1-phosphate [CPD:C00103]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
INHIBITOR   D-Glucono-1,5-lactone [CPD:C00198];
            Glucose [CPD:C00293];
            Purine [CPD:C15587]
EFFECTOR    AMP [CPD:C00020];
            D-Glucose 6-phosphate [CPD:C00092];
            IMP [CPD:C00130]
COMMENT     The accepted name should be qualified in each instance by adding the
            name of the natural substrate, e.g. maltodextrin phosphorylase,
            starch phosphorylase, glycogen phosphorylase.
REFERENCE   1
  AUTHORS   Baum, H. and Gilbert, G.A.
  TITLE     A simple method for the preparation of crystalline potato
            phosphorylase and Q-enzyme.
  JOURNAL   Nature 171 (1953) 983-984.
  ORGANISM  Solanum tuberosum [GN:estu]
REFERENCE   2  [PMID:4878695]
  AUTHORS   Chen GS, Segel IH.
  TITLE     Purification and properties of glycogen phosphorylase from
            Escherichia coli.
  JOURNAL   Arch. Biochem. Biophys. 127 (1968) 175-86.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:13812491]
  AUTHORS   COWGILL RW.
  TITLE     Lobster muscle phosphorylase: purification and properties.
  JOURNAL   J. Biol. Chem. 234 (1959) 3146-53.
  ORGANISM  rabbit
REFERENCE   4
  AUTHORS   Fischer, E.H., Pocker, A. and Saari, J.C.
  TITLE     The structure, function and control of glycogen phosphorylase.
  JOURNAL   In: Campbell, P.N. and Greville, G.D. (Eds.), Essays in
            Biochemistry, vol. 6, Academic Press, London and New York, 1970, p.
            23-68.
REFERENCE   5
  AUTHORS   Green, A.A. and Cori, G.T.
  TITLE     Crystalline muscle phosphorylase. I. Preparation, properties, and
            molecular weight.
  JOURNAL   J. Biol. Chem. 151 (1943) 21-29.
  ORGANISM  Solanum tuberosum [GN:estu], Saccharomyces cerevisiae [GN:sce],
            Pisum sativum, rabbit
REFERENCE   6
  AUTHORS   Hanes, C.S.
  TITLE     The breakdown and synthesis of starch by an enzyme from pea seeds.
  JOURNAL   Proc. R. Soc. Lond. B Biol. Sci. 128 (1940) 421-450.
  ORGANISM  Pisum sativum
PATHWAY     PATH: map00500  Starch and sucrose metabolism
            PATH: map04910  Insulin signaling pathway
ORTHOLOGY   KO: K00688  starch phosphorylase
GENES       HSA: 5834(PYGB) 5836(PYGL) 5837(PYGM)
            PTR: 469908(PYGB)
            MMU: 110078(Pygb) 110095(Pygl) 19309(Pygm)
            RNO: 24701(Pygm) 25739(Pygb) 64035(Pygl)
            CFA: 611078(PYGM)
            BTA: 327664(PYGM)
            GGA: 378909(PYGL) 421248(RCJMB04_2f16)
            XLA: 379862(pygb) 432134(MGC80198) 494832(pygl)
            XTR: 431680(pygb)
            DRE: 403051(pygb)
            DME: Dmel_CG7254(GlyP)
            CEL: T22F3.3
            ATH: AT3G29320 AT3G46970(ATPHS2/PHS2)
            OSA: 4324810 4334171
            CME: CMD184C
            SCE: YPR160W(GPH1)
            AGO: AGOS_AFR547W
            PIC: PICST_72279(GPH1)
            CGR: CAGL0F04895g
            ANI: AN1015.2
            AFM: AFUA_1G12920
            AOR: AO090012000601
            CNE: CNF03530
            DDI: DDB_0191397(glpD) DDB_0215010(glpV)
            CPV: cgd6_2450
            CHO: Chro.60284
            TET: TTHERM_00074320 TTHERM_00534080
            EHI: 187.t00014 24.t00009 7.t00058
            ECO: b3417(malP) b3428(glgP)
            ECJ: JW3391(glgP) JW5689(malP)
            ECE: Z4772(malP) Z4790(glgP)
            ECS: ECs4259 ECs4273
            ECC: c4194(malP) c4215(glgP)
            ECI: UTI89_C3918(malP) UTI89_C3937(glgP)
            ECP: ECP_3503 ECP_3522
            ECV: APECO1_3029(glgP) APECO1_3049(malP)
            ECW: EcE24377A_3893(malP) EcE24377A_3907(glgP)
            ECX: EcHS_A3615 EcHS_A3628(glgP)
            STY: STY4276(glgP) STY4282(malP)
            STT: t3986(glgP) t3992(malP)
            SPT: SPA3379(malP) SPA3385(glgP)
            SEC: SC3446(malP) SC3464(glgP)
            STM: STM3514(malP) STM3534(glgP)
            YPE: YPO3938(glgP)
            YPK: y3890(glgP)
            YPM: YP_3300(glgP)
            YPA: YPA_3344 YPA_3345 YPA_3767
            YPN: YPN_3586 YPN_3940
            YPP: YPDSF_0052 YPDSF_3303
            YPS: YPTB3775 YPTB3783(glgP)
            YPI: YpsIP31758_3993(malP) YpsIP31758_4002(glgP)
            YEN: YE3991(malP)
            SFL: SF3440(malP) SF3451(glgP)
            SFX: S4312(glgP) S4325(malP)
            SFV: SFV_3425(malP) SFV_3437(glgP)
            SSN: SSON_3549(malP) SSON_3668(glgP)
            SBO: SBO_3406(malP) SBO_3426(glgP)
            SDY: SDY_3574(glgP) SDY_3659(malP)
            ECA: ECA4136(malP) ECA4147(glgP)
            PLU: plu0470(malP)
            ENT: Ent638_3830 Ent638_3836
            SPE: Spro_4636 Spro_4643
            HIN: HI1361
            HIT: NTHI1803(glgP)
            HSO: HS_0885(glgP)
            PMU: PM0545(glgP)
            MSU: MS1119(glgP) MS2073(glgP)
            APL: APL_0350(glgP) APL_1232(malP)
            ASU: Asuc_0313 Asuc_1356
            VCH: VCA0013
            VCO: VC0395_0119(malP)
            VVU: VV2_1250
            VVY: VVA0077
            VPA: VPA1620
            VFI: VFA0810
            PPR: PBPRB1330
            PAE: PA2144(glgP)
            PAU: PA14_36840(glgP)
            PPU: PP_5041(glgP)
            PPF: Pput_4915
            PST: PSPTO_5165(glgP)
            PSB: Psyr_0374
            PSP: PSPPH_0356(glgP)
            PFL: PFL_0390(glgP)
            PFO: Pfl_0349
            PEN: PSEEN5107(glgP)
            PMY: Pmen_2288
            SON: SO_1496
            SFR: Sfri_2163
            SAZ: Sama_2451
            SBL: Sbal_1333
            SBM: Shew185_1323
            SLO: Shew_1170
            SPC: Sputcn32_1250
            SHE: Shewmr4_2756
            SHM: Shewmr7_2834
            SHN: Shewana3_2932
            SHW: Sputw3181_2854
            PAT: Patl_2197
            SDE: Sde_0989
            PIN: Ping_0880
            MAQ: Maqu_1428 Maqu_1436
            MCA: MCA0067(glgP-1) MCA2540(glgP-2)
            FTU: FTT0417(malP)
            FTF: FTF0417(malP)
            FTW: FTW_1656(glgP)
            FTL: FTL_0487
            FTH: FTH_0485(glgP)
            FTN: FTN_0517(glgP)
            TCX: Tcr_0513
            NOC: Noc_2115
            AEH: Mlg_0956
            HHA: Hhal_1109
            AHA: AHA_2431
            REU: Reut_B4232
            BXE: Bxe_B2201
            BTE: BTH_II0941
            RFR: Rfer_0511 Rfer_3895
            PNA: Pnap_1105
            NEU: NE0074 NE0466
            NET: Neut_2054 Neut_2291
            NMU: Nmul_A0715
            EBA: ebA6232
            DAR: Daro_0582
            TBD: Tbd_2056
            MFA: Mfla_0879 Mfla_1023
            NIS: NIS_0944 NIS_0947
            SUN: SUN_1278
            GSU: GSU0371 GSU2066(glgP)
            GME: Gmet_0940 Gmet_2767 Gmet_3159
            GUR: Gura_1705 Gura_2661 Gura_3854 Gura_4193
            PCA: Pcar_1731
            PPD: Ppro_0415 Ppro_2240 Ppro_3415
            DVU: DVU2349
            DVL: Dvul_0912
            DDE: Dde_1424 Dde_3088
            LIP: LI0332(glgP)
            ADE: Adeh_0864
            AFW: Anae109_0921
            MXA: MXAN_5831(glgP)
            SAT: SYN_00231 SYN_00298 SYN_00879 SYN_01331 SYN_02600 SYN_02761
                 SYN_02880
            SFU: Sfum_1198 Sfum_1470 Sfum_2957
            MLO: mlr7586
            SME: SMc04460(glgP)
            SMD: Smed_2739
            ATU: Atu4078(glgP)
            ATC: AGR_L_1556
            RET: RHE_CH03593(glgP)
            RLE: RL4114(glgP)
            BJA: blr8139(glgP)
            BRA: BRADO0743(glgP)
            BBT: BBta_7363(glgP)
            RPA: RPA4727(glgA2)
            RPB: RPB_0844
            RPC: RPC_4861
            RPD: RPD_0952
            RPE: RPE_4826
            NWI: Nwi_1204
            NHA: Nham_1460
            RSP: RSP_2887(glgP)
            RSH: Rsph17029_1533
            RSQ: Rsph17025_1132
            JAN: Jann_3118
            RDE: RD1_2876(glgP)
            PDE: Pden_4429
            NAR: Saro_1659
            GBE: GbCGDNIH1_2414
            ACR: Acry_0130
            RRU: Rru_A2244
            MAG: amb3062
            MGM: Mmc1_1520 Mmc1_3435
            ABA: Acid345_0820 Acid345_3051
            SUS: Acid_0409
            BSU: BG10911(glgP)
            BHA: BH1084(glgP)
            BAN: BA5119(glgP)
            BAR: GBAA5119(glgP)
            BAT: BAS4757
            BCE: BC4863
            BCA: BCE_5024(glgP)
            BCZ: BCZK4617(glgP)
            BCY: Bcer98_3500
            BTK: BT9727_4595(glgP)
            BTL: BALH_4428(glgP)
            BLI: BL01415(glgP)
            BLD: BLi03226(glgP)
            OIH: OB0410
            LLA: L99884(glgP)
            LLC: LACR_0727
            LLM: llmg_1871(glgP)
            SPY: SPy_1291(glgP)
            SPZ: M5005_Spy_1055(glgP)
            SPM: spyM18_1311(glgP)
            SPG: SpyM3_0980(glgP)
            SPS: SPs0874
            SPH: MGAS10270_Spy1111(glgP)
            SPI: MGAS10750_Spy1147(glgP)
            SPJ: MGAS2096_Spy1057(glgP)
            SPK: MGAS9429_Spy1101(glgP)
            SPF: SpyM50805(glgP)
            SPA: M6_Spy1029
            SPB: M28_Spy1036(glgP)
            SPN: SP_2106
            SPR: spr1916(malP)
            SPD: SPD_1932(malP)
            SAG: SAG1438(glgP)
            SAN: gbs1507
            SAK: SAK_1472(glgP)
            SMU: SMU.1535(phsG) SMU.1564(glgP)
            STC: str1012(glgP)
            STL: stu1012(glgP)
            SSA: SSA_0779(glgP) SSA_2265(malP)
            SGO: SGO_0106(glgP-2) SGO_1550(glgP-1)
            LPL: lp_0024(glgP)
            LAC: LBA0685
            LSL: LSL_1290(glgP)
            LCA: LSEI_2036
            CAC: CAC0857 CAC1664(glgP)
            CPE: CPE0065(glgP) CPE2337(glgP)
            CPF: CPF_2646(glgP)
            CPR: CPR_0083 CPR_2332
            CNO: NT01CX_0970 NT01CX_1243
            CTH: Cthe_0357
            CDF: CD0885(glgP)
            CBE: Cbei_0285 Cbei_0865 Cbei_4907
            CKL: CKL_3496(glgP)
            AMT: Amet_1678 Amet_2945
            DSY: DSY2039
            DRM: Dred_0443 Dred_1364
            CSC: Csac_0780
            TTE: TTE1805(glgP)
            MTA: Moth_1852
            MTU: Rv1328(glgP)
            MTC: MT1370
            MBO: Mb1363(glgP)
            MBB: BCG_1390(glgP)
            MPA: MAP2432c(glgP)
            MSM: MSMEG_4915
            MVA: Mvan_1192 Mvan_4300
            MGI: Mflv_2345 Mflv_5144
            MMC: Mmcs_3859
            MKM: Mkms_3933
            MJL: Mjls_3845
            CGL: NCgl1255(cgl1308) NCgl2006(cgl2087)
            CGB: cg1479(glgP1) cg2289(glgP2)
            CEF: CE1987
            CDI: DIP1552
            CJK: jk1268(glgP)
            NFA: nfa10800(glgP)
            RHA: RHA1_ro01447
            SCO: SCO5444(glgP)
            SMA: SAV2800(glgP)
            CMI: CMM_1399(glgP)
            ART: Arth_0736
            AAU: AAur_0907(glgP)
            PAC: PPA0081
            NCA: Noca_1811
            TFU: Tfu_0586
            FRA: Francci3_3664
            FAL: FRAAL5884(glgP)
            ACE: Acel_0680
            KRA: Krad_1298
            BLO: BL0597(glgP)
            BAD: BAD_0030(glgP)
            RXY: Rxyl_0301
            FNU: FN0857
            RBA: RB8383(glgP)
            CTR: CT248(glgP)
            CTA: CTA_0270(glgP)
            CMU: TC0519
            CPN: CPn0307(glgP)
            CPA: CP0451
            CPJ: CPj0307(glgP)
            CPT: CpB0316
            CCA: CCA00475(glgP)
            CAB: CAB461(glgP)
            CFE: CF0532(glgP)
            PCU: pc0106(glgP)
            TDE: TDE2411(glgP)
            SYN: sll1356(glgP) slr1367(glgP)
            SYW: SYNW0156
            SYC: syc1269_d(glgP)
            SYF: Synpcc7942_0244
            SYD: Syncc9605_0152
            SYE: Syncc9902_0182
            SYG: sync_0205
            SYR: SynRCC307_0140
            SYX: SynWH7803_0208
            CYA: CYA_2127(glgP) CYA_2752
            CYB: CYB_0632 CYB_2688(glgP)
            TEL: tll2079 tlr0782
            GVI: gll0694 gll3878 glr0687 glr0998
            ANA: all1272 all2806
            AVA: Ava_1084 Ava_2996
            PMA: Pro1759(glgP)
            PMM: PMM1601
            PMT: PMT1946
            PMN: PMN2A_1176
            PMI: PMT9312_1693
            PMB: A9601_18101(glgP)
            PMC: P9515_17881(glgP)
            PMF: P9303_25951(glgP)
            PMG: P9301_17931(glgP)
            PMH: P9215_18741(glgP)
            PME: NATL1_20511(glgP)
            TER: Tery_0218 Tery_3694
            BTH: BT_1100 BT_1293
            BFR: BF2726
            BFS: BF2741
            PGI: PG0699(malP)
            CHU: CHU_0308(glgP)
            CTE: CT1596
            CCH: Cag_1784
            CPH: Cpha266_0594
            PVI: Cvib_1386
            PLT: Plut_1595
            RRS: RoseRS_4181
            RCA: Rcas_0897
            DRA: DR_2195
            DGE: Dgeo_1198
            TTH: TTC0808
            TTJ: TTHA1172
            AAE: aq_717(glgP)
            TPT: Tpet_1581
            TME: Tmel_1798
            FNO: Fnod_1446
            MJA: MJ1631(glgP)
            MMP: MMP1220(glgP)
            MMQ: MmarC5_0370
            MMZ: MmarC7_0467
            MAE: Maeo_0980
            MVN: Mevan_0535
            MAC: MA1874(malP)
            MBA: Mbar_A2997 Mbar_A3640
            MMA: MM_3109
            MTP: Mthe_1399
            MHU: Mhun_1203
            MEM: Memar_1262 Memar_2480
            MBN: Mboo_1526
            PHO: PH1512
            PAB: PAB2414(agpA)
            PFU: PF1535
            TKO: TK1406
            SSO: SSO2538(glgP)
            STO: ST0893
            SAI: Saci_0294
            PAI: PAE3422
STRUCTURES  PDB: 1A8I  1ABB  1AHP  1AXR  1B4D  1BX3  1C50  1C8K  1C8L  1E1Y  
                 1E4O  1EM6  1EXV  1FA9  1FC0  1FS4  1FTQ  1FTW  1FTY  1FU4  
                 1FU7  1FU8  1GFZ  1GG8  1GGN  1GPA  1GPB  1GPY  1H5U  1HLF  
                 1K06  1K08  1KTI  1L5S  1L5V  1L5W  1L6I  1L7X  1LWN  1LWO  
                 1NOI  1NOJ  1NOK  1P29  1P2B  1P2D  1P2G  1P4G  1P4H  1P4J  
                 1PYG  1QM5  1UZU  1WUT  1WUY  1WV0  1WV1  1WW2  1WW3  1XC7  
                 1XKX  1XL0  1XL1  1XOI  1Z62  1Z6P  1Z6Q  1Z8D  2AMV  2ASV  
                 2ATI  2AV6  2AW3  2AZD  2C4M  2ECP  2F3P  2F3Q  2F3S  2F3U  
                 2FET  2FF5  2FFR  2G9Q  2G9R  2G9U  2G9V  2GJ4  2GM9  2GPA  
                 2GPB  2GPN  2IEG  2IEI  2OFF  2PRI  2PRJ  2SKC  2SKD  2SKE  
                 3AMV  3GPB  4GPB  5GPB  6GPB  7GPB  8GPB  9GPB  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.1
            ExPASy - ENZYME nomenclature database: 2.4.1.1
            ExplorEnz - The Enzyme Database: 2.4.1.1
            ERGO genome analysis and discovery system: 2.4.1.1
            BRENDA, the Enzyme Database: 2.4.1.1
            CAS: 9035-74-9
///
ENTRY       EC 2.4.1.2                  Enzyme
NAME        dextrin dextranase;
            dextrin 6-glucosyltransferase;
            dextran dextrinase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     1,4-alpha-D-glucan:1,6-alpha-D-glucan 6-alpha-D-glucosyltransferase
REACTION    (1,4-alpha-D-glucosyl)n + (1,6-alpha-D-glucosyl)m =
            (1,4-alpha-D-glucosyl)n-1 + (1,6-alpha-D-glucosyl)m+1 [RN:R02121
            R06184]
ALL_REAC    R02121 R06184(G)
SUBSTRATE   (1,4-alpha-D-glucosyl)n [CPD:C00718];
            (1,6-alpha-D-glucosyl)m [CPD:C00372]
PRODUCT     (1,4-alpha-D-glucosyl)n-1 [CPD:C00718];
            (1,6-alpha-D-glucosyl)m+1 [CPD:C00372]
REFERENCE   1
  AUTHORS   Hehre, E.J.
  TITLE     Enzymic synthesis of polysaccharides: a biological type of
            polymerization.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297-337.
REFERENCE   2
  AUTHORS   Hehre, E.J. and Hamilton, D.M.
  TITLE     Bacterial conversion of dextrin into a polysaccharide with the
            serological properties of dextran.
  JOURNAL   Proc. Soc. Exp. Biol. Med. 71 (1949) 336-339.
  ORGANISM  Acetobacter capsdatum, Acetobacter viscosum
REFERENCE   3
  AUTHORS   Hehre, E.J. and Hamilton, D.M.
  TITLE     The biological synthesis of dextran from dextrins.
  JOURNAL   J. Biol. Chem. 192 (1953) 161-174.
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.2
            ExPASy - ENZYME nomenclature database: 2.4.1.2
            ExplorEnz - The Enzyme Database: 2.4.1.2
            ERGO genome analysis and discovery system: 2.4.1.2
            BRENDA, the Enzyme Database: 2.4.1.2
            CAS: 9032-13-7
///
ENTRY       EC 2.4.1.3        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: amylomaltase. Now included with EC 2.4.1.25,
            4-alpha-glucanotransferase (EC 2.4.1.3 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.3
            ExPASy - ENZYME nomenclature database: 2.4.1.3
            ExplorEnz - The Enzyme Database: 2.4.1.3
            ERGO genome analysis and discovery system: 2.4.1.3
            BRENDA, the Enzyme Database: 2.4.1.3
///
ENTRY       EC 2.4.1.4                  Enzyme
NAME        amylosucrase;
            sucrose---glucan glucosyltransferase;
            sucrose-1,4-alpha-glucan glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     sucrose:1,4-alpha-D-glucan 4-alpha-D-glucosyltransferase
REACTION    sucrose + (1,4-alpha-D-glucosyl)n = D-fructose +
            (1,4-alpha-D-glucosyl)n+1 [RN:R01823 R06052]
ALL_REAC    R01823 R06052(G)
SUBSTRATE   sucrose [CPD:C00089];
            (1,4-alpha-D-glucosyl)n [CPD:C00718]
PRODUCT     D-fructose [CPD:C00095];
            (1,4-alpha-D-glucosyl)n+1 [CPD:C00718]
REFERENCE   1  [PMID:13398406]
  AUTHORS   AVIGAD G, FEINGOLD DS, HESTRIN S.
  TITLE     Enzymatic synthesis and reactions of a sucrose isomer
            alpha-D-galactopyranosyl-beta-D-fructofuranoside.
  JOURNAL   J. Biol. Chem. 224 (1957) 295-307.
  ORGANISM  Neisseria perflava
REFERENCE   2
  AUTHORS   Hehre, E.J.
  TITLE     Enzymic synthesis of polysaccharides: a biological type of
            polymerization.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297-337.
REFERENCE   3
  AUTHORS   Hehre, E.J., Hamilton, D.M. and Carlson, A.S.
  TITLE     Synthesis of a polsaccharide of the starch glycogen class from
            sucrose by a cell-free, bacterial enzyme system (amylosucrase).
  JOURNAL   J. Biol. Chem. 177 (1949) 267-279.
  ORGANISM  Neisseria perflava
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K05341  amylosucrase
GENES       XCC: XCC3359
            XCB: XC_0805
            XCV: XCV3618(suh)
            XAC: XAC3490
            XOO: XOO1098
            XOM: XOO_0996(XOO0996)
            TCX: Tcr_1797
            MFA: Mfla_2611
            MGM: Mmc1_3514
            RBA: RB5196
            DGE: Dgeo_0572
STRUCTURES  PDB: 1G5A  1JG9  1JGI  1MVY  1MW0  1MW1  1MW2  1MW3  1S46  1ZS2  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.4
            ExPASy - ENZYME nomenclature database: 2.4.1.4
            ExplorEnz - The Enzyme Database: 2.4.1.4
            ERGO genome analysis and discovery system: 2.4.1.4
            BRENDA, the Enzyme Database: 2.4.1.4
            CAS: 9032-11-5
///
ENTRY       EC 2.4.1.5                  Enzyme
NAME        dextransucrase;
            sucrose 6-glucosyltransferase;
            SGE;
            CEP;
            sucrose-1,6-alpha-glucan glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     sucrose:1,6-alpha-D-glucan 6-alpha-D-glucosyltransferase
REACTION    sucrose + (1,6-alpha-D-glucosyl)n = D-fructose +
            (1,6-alpha-D-glucosyl)n+1 [RN:R02120 R06066]
ALL_REAC    R02120 R06066(G)
SUBSTRATE   sucrose [CPD:C00089];
            (1,6-alpha-D-glucosyl)n [CPD:C00372]
PRODUCT     D-fructose [CPD:C00095];
            (1,6-alpha-D-glucosyl)n+1 [CPD:C00372]
REFERENCE   1  [PMID:13651133]
  AUTHORS   BAILEY RW.
  TITLE     Transglucosidase activity of rumen strains of Streptococcus bovis.
            2. Isolation and properties of dextransucrase.
  JOURNAL   Biochem. J. 72 (1959) 42-9.
  ORGANISM  Streptococcus bovis
REFERENCE   2
  AUTHORS   Bailey, R.W., Barker, S.A., Bourne, E.J. and Stacey, M.
  TITLE     Immunopolysaccharides. Part VI. The isolation and properties of the
            dextransucrase of Betacoccus arabinosaceous.
  JOURNAL   J. Chem. Soc. (Lond.) (1957) 3530-3536.
  ORGANISM  Betacoccus arabinosaceous
REFERENCE   3
  AUTHORS   Hehre, E.J.
  TITLE     Enzymic synthesis of polysaccharides: a biological type of
            polymerization.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297-337.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
            PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K00689  dextransucrase
GENES       SAA: SAUSA300_0939
            LLM: llmg_0458
            SMU: SMU.1004(gtfB) SMU.1005(gtfC) SMU.910(gtfD)
            SSA: SSA_0613(gtfP)
            SGO: SGO_0497(gtfG)
            LSL: LSL_1517
            LRE: Lreu_1346
            OOE: OEOE_0544
            CHU: CHU_1410
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.5
            ExPASy - ENZYME nomenclature database: 2.4.1.5
            ExplorEnz - The Enzyme Database: 2.4.1.5
            ERGO genome analysis and discovery system: 2.4.1.5
            BRENDA, the Enzyme Database: 2.4.1.5
            CAS: 9032-14-8
///
ENTRY       EC 2.4.1.6        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: maltose 3-glycosyltransferase (EC 2.4.1.6 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.6
            ExPASy - ENZYME nomenclature database: 2.4.1.6
            ExplorEnz - The Enzyme Database: 2.4.1.6
            ERGO genome analysis and discovery system: 2.4.1.6
            BRENDA, the Enzyme Database: 2.4.1.6
///
ENTRY       EC 2.4.1.7                  Enzyme
NAME        sucrose phosphorylase;
            sucrose glucosyltransferase;
            disaccharide glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     sucrose:phosphate alpha-D-glucosyltransferase
REACTION    sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
            [RN:R00803 R06034]
ALL_REAC    R00803 R06034(G)
SUBSTRATE   sucrose [CPD:C00089];
            phosphate [CPD:C00009]
PRODUCT     D-fructose [CPD:C00095];
            alpha-D-glucose 1-phosphate [CPD:C00103]
COMMENT     In the forward reaction, arsenate may replace phosphate. In the
            reverse reaction, various ketoses and L-arabinose may replace
            D-fructose.
REFERENCE   1
  AUTHORS   Doudoroff, M.
  TITLE     Disaccharide phosphorylases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 5, Academic Press, New York, 1961, p. 229-236.
REFERENCE   2  [PMID:14783033]
  AUTHORS   HASSID WZ, DOUDOROFF M.
  TITLE     Enzymatic synthesis of sucrose and other disaccharides.
  JOURNAL   Adv. Carbohydr. Chem. 5 (1950) 29-48.
REFERENCE   3  [PMID:4381552]
  AUTHORS   Silverstein R, Voet J, Reed D, Abeles RH.
  TITLE     Purification and mechanism of action of sucrose phosphorylase.
  JOURNAL   J. Biol. Chem. 242 (1967) 1338-46.
  ORGANISM  Pseudomonas saccharophila
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K00690  sucrose phosphorylase
GENES       ECO: b1309(ycjM)
            ECJ: JW1302(ycjM)
            ECE: Z2475m
            ECC: c1780(ycjM)
            ECI: UTI89_C1579(ycjM)
            ECP: ECP_1361
            ECV: APECO1_462(ycjM)
            SGL: SG2323
            VVY: VVA1393
            SFR: Sfri_3990
            SBL: Sbal_4288
            SBM: Shew185_0061
            SHE: Shewmr4_0064
            SHM: Shewmr7_0062
            SHN: Shewana3_0066
            CPS: CPS_0506
            PAT: Patl_2164
            SDE: Sde_3210
            TCX: Tcr_0774
            HCH: HCH_00269
            CSA: Csal_2588
            SAT: SYN_02630
            ATU: Atu6135(splA)
            ATC: AGR_pTi_251
            SIT: TM1040_0418
            RDE: RD1_3715(gtfA)
            SUS: Acid_2070
            LMO: lmo2735 lmo2840
            LMF: LMOf2365_0271(gtfA) LMOf2365_2722 LMOf2365_2831
            LIN: lin2973
            LWE: lwe0226(gtfA) lwe2770
            SPN: SP_1894
            SPR: spr1709(gtfA)
            SPD: SPD_1673(gtfA)
            SMU: SMU.881(gtfA)
            SSA: SSA_1006(gtfA)
            LJO: LJ0262
            LAC: LBA0507(gtfA) LBA1437
            LBU: LBUL_0059
            LRE: Lreu_1542
            OOE: OEOE_1779
            POY: PAM723
            BLO: BL0536(spl)
            BAD: BAD_0078(spl)
            RBA: RB12343
            SYW: SYNW2435
            SYD: Syncc9605_2606
            SYE: Syncc9902_2243
            SYG: sync_0361
            SYR: SynRCC307_2002
            SYX: SynWH7803_2474
            PMA: Pro0728(amyA)
            PMM: PMM0961
            PMN: PMN2A_0246
            PMI: PMT9312_0838
            PMB: A9601_08971
            PMC: P9515_10441
            PMG: P9301_08951
            PMH: P9215_09271
            PME: NATL1_09141(amyA)
STRUCTURES  PDB: 1R7A  2GDU  2GDV  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.7
            ExPASy - ENZYME nomenclature database: 2.4.1.7
            ExplorEnz - The Enzyme Database: 2.4.1.7
            ERGO genome analysis and discovery system: 2.4.1.7
            BRENDA, the Enzyme Database: 2.4.1.7
            CAS: 9074-06-0
///
ENTRY       EC 2.4.1.8                  Enzyme
NAME        maltose phosphorylase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     maltose:phosphate 1-beta-D-glucosyltransferase
REACTION    maltose + phosphate = D-glucose + beta-D-glucose 1-phosphate
            [RN:R01555 R06040]
ALL_REAC    R01555 R06040(G)
SUBSTRATE   maltose [CPD:C00208];
            phosphate [CPD:C00009]
PRODUCT     D-glucose [CPD:C00031];
            beta-D-glucose 1-phosphate [CPD:C00663]
REFERENCE   1
  AUTHORS   Doudoroff, M.
  TITLE     Disaccharide phosphorylases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 5, Academic Press, New York, 1961, p. 229-236.
REFERENCE   2  [PMID:12999827]
  AUTHORS   FITTING C, DOUDOROFF M.
  TITLE     Phosphorolysis of maltose by enzyme preparations from Neisseria
            meningitidis.
  JOURNAL   J. Biol. Chem. 199 (1952) 153-63.
  ORGANISM  Neisseria meningitidis
REFERENCE   3
  AUTHORS   Putman, E.W., Litt, C.F. and Hassid, W.Z.
  TITLE     The structure of D-glucose-D-xylose synthesized by maltose
            phosphorylase.
  JOURNAL   J. Am. Chem. Soc. 77 (1955) 4351-4353.
  ORGANISM  Neisseria meningitidis
REFERENCE   4
  AUTHORS   Wood, B.J.B. and Rainbow, C.
  TITLE     The maltophosphorylase of beer lactobacilli.
  JOURNAL   Biochem. J. 78 (1961) 204-209.
  ORGANISM  Neisseria meningitidis
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K00691  maltose phosphorylase
GENES       ECI: UTI89_C1587(ycjT)
            NME: NMB0390
            NMA: NMA2094(mapA') NMA2098(mapA)
            NMC: NMC1777(mapA)
            BSU: BG12420(yvdK)
            BLI: BL00492(yvdK)
            BLD: BLi00663(yvdK)
            LMO: lmo2121
            LMF: LMOf2365_2155
            LIN: lin2226
            LWE: lwe2141
            LLA: L128690(mapA)
            LLC: LACR_1847
            LLM: llmg_0455(trePP) llmg_0745(mapA)
            LPL: lp_0028(map1) lp_0181(map2) lp_1730(map3) lp_3530(map4)
            LJO: LJ0213
            LAC: LBA1870
            LSL: LSL_1280(mapA)
            LBR: LVIS_0358 LVIS_1517
            LCA: LSEI_0982
            LGA: LGAS_0216
            PPE: PEPE_0967
            EFA: EF0957
            LME: LEUM_0995
            CAC: CAC2685
            CDF: CD2188(mapA)
            MMO: MMOB3950
            MCP: MCAP_0190
            BFR: BF3310
            BFS: BF3149
            SRU: SRU_0074(malP)
STRUCTURES  PDB: 1H54  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.8
            ExPASy - ENZYME nomenclature database: 2.4.1.8
            ExplorEnz - The Enzyme Database: 2.4.1.8
            ERGO genome analysis and discovery system: 2.4.1.8
            BRENDA, the Enzyme Database: 2.4.1.8
            CAS: 9030-19-7
///
ENTRY       EC 2.4.1.9                  Enzyme
NAME        inulosucrase;
            sucrose 1-fructosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     sucrose:2,1-beta-D-fructan 1-beta-D-fructosyltransferase
REACTION    sucrose + (2,1-beta-D-fructosyl)n = glucose +
            (2,1-beta-D-fructosyl)n+1 [RN:R04194 R06059]
ALL_REAC    R04194 R06059(G)
SUBSTRATE   sucrose [CPD:C00089];
            (2,1-beta-D-fructosyl)n [CPD:C03323]
PRODUCT     glucose [CPD:C00293];
            (2,1-beta-D-fructosyl)n+1 [CPD:C03323]
COMMENT     Converts sucrose into inulin and D-glucose. Some other sugars can
            act as D-fructosyl acceptors.
REFERENCE   1  [PMID:13260192]
  AUTHORS   BHATIA IS, SATYANARAYANA MN, SRINIVASAN M.
  TITLE     Transfructosidase from Agave vera cruz Mill.
  JOURNAL   Biochem. J. 61 (1955) 171-4.
  ORGANISM  Agave cera cruz
REFERENCE   2  [PMID:14935737]
  AUTHORS   DEDONDER R.
  TITLE     [The glucides of the Jerusalem artichoke. III. Synthesis of
            glucofructosanes in vitro by extracts of different organs of the
            artichoke.]
  JOURNAL   Bull. Soc. Chim. Biol. (Paris). 34 (1952) 171-82.
REFERENCE   3  [PMID:14886320]
  AUTHORS   EDELMAN J, BACON JS.
  TITLE     Transfructosidation in extracts of the tubers of Helianthus
            tuberosus L.
  JOURNAL   Biochem. J. 49 (1951) 529-40.
  ORGANISM  Helianthus tuberosus
GENES       HCH: HCH_01365
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.9
            ExPASy - ENZYME nomenclature database: 2.4.1.9
            ExplorEnz - The Enzyme Database: 2.4.1.9
            ERGO genome analysis and discovery system: 2.4.1.9
            BRENDA, the Enzyme Database: 2.4.1.9
            CAS: 9030-16-4
///
ENTRY       EC 2.4.1.10                 Enzyme
NAME        levansucrase;
            sucrose 6-fructosyltransferase;
            beta-2,6-fructosyltransferase;
            beta-2,6-fructan:D-glucose 1-fructosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     sucrose:2,6-beta-D-fructan 6-beta-D-fructosyltransferase
REACTION    sucrose + (2,6-beta-D-fructosyl)n = glucose +
            (2,6-beta-D-fructosyl)n+1 [RN:R04195 R06060]
ALL_REAC    R04195 R06060(G) > R05140 R06079(G)
SUBSTRATE   sucrose [CPD:C00089];
            (2,6-beta-D-fructosyl)n [CPD:C06215]
PRODUCT     glucose [CPD:C00293];
            (2,6-beta-D-fructosyl)n+1 [CPD:C06215]
COMMENT     Some other sugars can act as D-fructosyl acceptors.
REFERENCE   1
  AUTHORS   Hehre, E.J.
  TITLE     Enzymic synthesis of polysaccharides: a biological type of
            polymerization.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297-337.
REFERENCE   2  [PMID:13363847]
  AUTHORS   AVIGAD G, FEINGOLD DS, HESTRIN S.
  TITLE     The mechanism of polysaccharide production from sucrose.  3.
            Donor-acceptor specificity of levansucrase from Aerobacter
            levanicum.
  JOURNAL   Biochem. J. 64 (1956) 340-51.
  ORGANISM  Aerobacter levanicum
REFERENCE   3  [PMID:5940635]
  AUTHORS   Reese ET, Avigad G.
  TITLE     Purification of levansucrase by precipitation with levan.
  JOURNAL   Biochim. Biophys. Acta. 113 (1966) 79-83.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
            PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K00692  levansucrase
GENES       PST: PSPTOA0032(lsc-3) PSPTO_1453(lsc-1)
            PSB: Psyr_0754 Psyr_2103
            PSP: PSPPH_2074 PSPPH_4994 PSPPH_A0027
            BMA: BMAA0466(sacB)
            BMV: BMASAVP1_0714(sacB)
            BML: BMA10299_1010(sacB)
            BMN: BMA10247_A1984(sacB)
            BVI: Bcep1808_4836
            BCN: Bcen_4096
            BCH: Bcen2424_4270
            BAM: Bamb_3698 Bamb_6116
            BPS: BPSS0543
            BPM: BURPS1710b_A2102(sacB)
            BPL: BURPS1106A_A0735(sacB)
            BPD: BURPS668_A0822(sacB)
            BTE: BTH_II1872
            ZMO: ZMO0374(sacB)
            NAR: Saro_1879
            ELI: ELI_04235
            GOX: GOX0873
            BSU: BG10388(sacB)
            BLD: BLi03706(sacB)
            BAY: RBAM_037650(sacB)
            SMU: SMU.2028(sacB)
            LJO: LJ0913
            CAC: CAC1772(sacB1)
            CMI: CMM_0614(sacB)
            ART: Arth_0405
            AAU: AAur_1402(sacB)
            FAL: FRAAL2465
            HMA: rrnAC1478(sacB)
STRUCTURES  PDB: 1OYG  1PT2  1W18  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.10
            ExPASy - ENZYME nomenclature database: 2.4.1.10
            ExplorEnz - The Enzyme Database: 2.4.1.10
            ERGO genome analysis and discovery system: 2.4.1.10
            BRENDA, the Enzyme Database: 2.4.1.10
            CAS: 9030-17-5
///
ENTRY       EC 2.4.1.11                 Enzyme
NAME        glycogen(starch) synthase;
            UDP-glucose---glycogen glucosyltransferase;
            glycogen (starch) synthetase;
            UDP-glucose-glycogen glucosyltransferase;
            UDP-glycogen synthase;
            UDPG-glycogen synthetase;
            UDPG-glycogen transglucosylase;
            uridine diphosphoglucose-glycogen glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:glycogen 4-alpha-D-glucosyltransferase
REACTION    UDP-glucose + (1,4-alpha-D-glucosyl)n = UDP +
            (1,4-alpha-D-glucosyl)n+1 [RN:R00292 R06051]
ALL_REAC    R00292 R06051(G)
SUBSTRATE   UDP-glucose [CPD:C00029];
            (1,4-alpha-D-glucosyl)n [CPD:C00718]
PRODUCT     UDP [CPD:C00015];
            (1,4-alpha-D-glucosyl)n+1 [CPD:C00718]
COMMENT     The accepted name varies according to the source of the enzyme and
            the nature of its synthetic product (cf. EC 2.4.1.1, phosphorylase).
            Glycogen synthase from animal tissues is a complex of a catalytic
            subunit and the protein glycogenin. The enzyme requires glucosylated
            glycogenin as a primer; this is the reaction product of EC 2.4.1.186
            (glycogenin glucosyltransferase). A similar enzyme utilizes
            ADP-glucose (EC 2.4.1.21, starch synthase).
REFERENCE   1  [PMID:13682402]
  AUTHORS   ALGRANATI ID, CABIB E.
  TITLE     The synthesis of glycogen in yeast.
  JOURNAL   Biochim. Biophys. Acta. 43 (1960) 141-2.
  ORGANISM  sheep
REFERENCE   2  [PMID:13687710]
  AUTHORS   BASU DK, BACHHAWAT BK.
  TITLE     Purification of uridine diphosphoglucose-glycogen transglucosylase
            from sheep brain.
  JOURNAL   Biochim. Biophys. Acta. 50 (1961) 123-8.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Leloir, L.F. and Cardini, C.E.
  TITLE     UDPG-glycogen transglucosylase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 6, Academic Press, New York, 1962, p. 317-326.
REFERENCE   4
  AUTHORS   Leloir, L.F. and Goldemberg, S.H.
  TITLE     Synthesis of glycogen from uridine diphosphate glucose in liver.
  JOURNAL   J. Biol. Chem. 235 (1960) 919-923.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:2970965]
  AUTHORS   Pitcher J, Smythe C, Cohen P.
  TITLE     Glycogenin is the priming glucosyltransferase required for the
            initiation of glycogen biogenesis in rabbit skeletal muscle.
  JOURNAL   Eur. J. Biochem. 176 (1988) 391-5.
  ORGANISM  rabbit
PATHWAY     PATH: map00500  Starch and sucrose metabolism
            PATH: map04910  Insulin signaling pathway
ORTHOLOGY   KO: K00693  glycogen(starch) synthase
GENES       HSA: 2997(GYS1) 2998(GYS2)
            PTR: 465336(GYS2)
            MMU: 14936(Gys1) 232493(Gys2)
            RNO: 25623(Gys2)
            CFA: 403737(GYS2)
            GGA: 418201(GYS2)
            XLA: 431912(MGC82298)
            CEL: Y46G5A.31(gsy-1)
            ATH: AT1G32900 AT3G01180
            SCE: YFR015C(GSY1) YLR258W(GSY2)
            AGO: AGOS_AAR008W
            PIC: PICST_81231(GSY1)
            CGR: CAGL0F04719g CAGL0K10626g
            ANI: AN8010.2
            AFM: AFUA_5G02480
            AOR: AO090102000361
            CNE: CNJ00590
            UMA: UM01009.1
            DDI: DDB_0231962(glcS)
            SAT: SYN_00879
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.11
            ExPASy - ENZYME nomenclature database: 2.4.1.11
            ExplorEnz - The Enzyme Database: 2.4.1.11
            ERGO genome analysis and discovery system: 2.4.1.11
            BRENDA, the Enzyme Database: 2.4.1.11
            CAS: 9014-56-6
///
ENTRY       EC 2.4.1.12                 Enzyme
NAME        cellulose synthase (UDP-forming);
            UDP-glucose---beta-glucan glucosyltransferase;
            UDP-glucose-cellulose glucosyltransferase;
            GS-I;
            beta-1,4-glucosyltransferase;
            uridine diphosphoglucose-1,4-beta-glucan glucosyltransferase;
            beta-1,4-glucan synthase;
            beta-1,4-glucan synthetase;
            beta-glucan synthase;
            1,4-beta-D-glucan synthase;
            1,4-beta-glucan synthase;
            glucan synthase;
            UDP-glucose-1,4-beta-glucan glucosyltransferase;
            uridine diphosphoglucose-cellulose glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:1,4-beta-D-glucan 4-beta-D-glucosyltransferase
REACTION    UDP-glucose + (1,4-beta-D-glucosyl)n = UDP +
            (1,4-beta-D-glucosyl)n+1 [RN:R02889 R06023]
ALL_REAC    R02889 R06023(G)
SUBSTRATE   UDP-glucose [CPD:C00029];
            (1,4-beta-D-glucosyl)n [CPD:C00760]
PRODUCT     UDP [CPD:C00015];
            (1,4-beta-D-glucosyl)n+1 [CPD:C00760]
COMMENT     Involved in the synthesis of cellulose. A similar enzyme utilizes
            GDP-glucose [EC 2.4.1.29 cellulose synthase (GDP-forming)].
REFERENCE   1  [PMID:13549448]
  AUTHORS   GLASER L.
  TITLE     The synthesis of cellulose in cell-free extracts of Acetobacter
            xylinum.
  JOURNAL   J. Biol. Chem. 232 (1958) 627-36.
  ORGANISM  Acetobacter xylinum
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K00694  cellulose synthase (UDP-forming)
GENES       ECO: b3533(yhjO)
            ECE: Z4948(yhjOP)
            ECS: ECs4413
            ECC: c4345(yhjO)
            ECI: UTI89_C4062(yhjL) UTI89_C4065(yhjO)
            ECP: ECP_3632 ECP_3633
            ECW: EcE24377A_4021(bcsA)
            STY: STY4181(yhjO)
            STT: t3898(yhjO)
            STM: STM3619(yhjO)
            YEN: YE4074(bcsA)
            SBO: SBO_3529(yhjL) SBO_3532(yhjO)
            SDY: SDY_4553(yhjO)
            ECA: ECA4370(bcsA)
            ENT: Ent638_3930 Ent638_3940
            SPE: Spro_0148
            XCV: XCV3643(bcsA) XCV3644(bcsA)
            XAC: XAC3518(bcsA)
            VFI: VFA0883 VFA0884
            PPR: PBPRA1720(yhjO)
            PPU: PP_2635
            PPF: Pput_2136
            PST: PSPTO_1027(wssB)
            SPL: Spea_0298
            PHA: PSHAa2162(bcsA)
            HHA: Hhal_0208
            CVI: CV_0228 CV_2675(bscC) CV_2678(bscA)
            REU: Reut_B3521 Reut_B5236 Reut_C6029
            RME: Rmet_2256
            BMA: BMAA1585
            BXE: Bxe_B2040
            BVI: Bcep1808_1355 Bcep1808_6502
            BUR: Bcep18194_A4530 Bcep18194_B0865
            BCN: Bcen_0903
            BCH: Bcen2424_1385
            BAM: Bamb_1263
            BPS: BPSS1577(bcsA)
            BPM: BURPS1710b_A0626(bcsA)
            BPL: BURPS1106A_A2140(celA)
            BPD: BURPS668_A2226(celA)
            BTE: BTH_II0797
            PNU: Pnuc_1171
            NET: Neut_1975
            ABU: Abu_1451
            ADE: Adeh_2031
            AFW: Anae109_3128
            SMD: Smed_3726 Smed_5208
            RET: RHE_CH00070 RHE_CH01542(celA) RHE_PE00363
            RLE: RL0079(acsAB) RL0558 RL1646(bcsA)
            BME: BMEII0728 BMEII0729
            BRA: BRADO3754
            BBT: BBta_3605 BBta_4173
            RSP: RSP_0158
            RSH: Rsph17029_1978
            RSQ: Rsph17025_0962
            ACR: Acry_0569
            BAY: RBAM_007620
            LSL: LSL_1018
            CDF: CD2545
            MMC: Mmcs_0406
            MKM: Mkms_0415
            MJL: Mjls_0394
            RHA: RHA1_ro03574
            ART: Arth_0281
            NCA: Noca_2832
            FRA: Francci3_3257
            SYW: SYNW0654
            SYF: Synpcc7942_0466 Synpcc7942_1398 Synpcc7942_2151
            SYD: Syncc9605_0794
            SYR: SynRCC307_0570
            CYA: CYA_2050
            CYB: CYB_0740
            ANA: alr3757
            AVA: Ava_1568
            CCH: Cag_0340
            PLT: Plut_0992
            RRS: RoseRS_3768
            RCA: Rcas_1116
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.12
            ExPASy - ENZYME nomenclature database: 2.4.1.12
            ExplorEnz - The Enzyme Database: 2.4.1.12
            ERGO genome analysis and discovery system: 2.4.1.12
            BRENDA, the Enzyme Database: 2.4.1.12
            CAS: 9027-19-4
///
ENTRY       EC 2.4.1.13                 Enzyme
NAME        sucrose synthase;
            UDPglucose-fructose glucosyltransferase;
            sucrose synthetase;
            sucrose-UDP glucosyltransferase;
            sucrose-uridine diphosphate glucosyltransferase;
            uridine diphosphoglucose-fructose glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     NDP-glucose:D-fructose 2-alpha-D-glucosyltransferase
REACTION    NDP-glucose + D-fructose = NDP + sucrose [RN:R07256]
ALL_REAC    R07256 > R00806 R06036(G)
SUBSTRATE   NDP-glucose [CPD:C15541];
            D-fructose [CPD:C00095]
PRODUCT     NDP [CPD:C00454];
            sucrose [CPD:C00089]
COMMENT     Although UDP is generally considered to be the preferred nucleoside
            diphosphate for sucrose synthase, numerous studies have shown that
            ADP serves as an effective acceptor molecule to produce ADP-glucose
            [3-9]. Sucrose synthase has a dual role in producing both
            UDP-glucose (necessary for cell wall and glycoprotein biosynthesis)
            and ADP-glucose (necessary for starch biosynthesis) [10].
REFERENCE   1
  AUTHORS   Avigad, G. and Milner, Y.
  TITLE     UDP-glucose:fructose transglucosylase from sugar beet roots.
  JOURNAL   Methods Enzymol. 8 (1966) 341-345.
  ORGANISM  Beta vulgaris
REFERENCE   2  [PMID:14367373]
  AUTHORS   CARDINI CE, LELOIR LF, CHIRIBOGA J.
  TITLE     The biosynthesis of sucrose.
  JOURNAL   J. Biol. Chem. 214 (1955) 149-55.
  ORGANISM  Pseudomonas saccharophila
REFERENCE   3  [PMID:4624446]
  AUTHORS   Delmer DP.
  TITLE     The purification and properties of sucrose synthetase from etiolated
            Phaseolus aureus seedlings.
  JOURNAL   J. Biol. Chem. 247 (1972) 3822-8.
  ORGANISM  Phaseolus aureus
REFERENCE   4  [PMID:5941994]
  AUTHORS   Murata T, Sugiyama T, Minamikawa T, Akazawa T.
  TITLE     Enzymic mechanism of starch synthesis in ripening rice grains. 3.
            Mechanism of the sucrose-starch conversion.
  JOURNAL   Arch. Biochem. Biophys. 113 (1966) 34-44.
  ORGANISM  Oryza sativa [GN:eosa]
REFERENCE   5  [PMID:10050318]
  AUTHORS   Nakai T, Konishi T, Zhang XQ, Chollet R, Tonouchi N, Tsuchida T,
            Yoshinaga F, Mori H, Sakai F, Hayashi T.
  TITLE     An increase in apparent affinity for sucrose of mung bean sucrose
            synthase is caused by in vitro phosphorylation or directed
            mutagenesis of Ser11.
  JOURNAL   Plant. Cell. Physiol. 39 (1998) 1337-41.
  ORGANISM  Vigna radiata
REFERENCE   6  [PMID:10592030]
  AUTHORS   Porchia AC, Curatti L, Salerno GL.
  TITLE     Sucrose metabolism in cyanobacteria: sucrose synthase from Anabaena
            sp. strain PCC 7119 is remarkably different from the plant enzymes
            with respect to substrate affinity and amino-terminal sequence.
  JOURNAL   Planta. 210 (1999) 34-40.
  ORGANISM  Anabaena sp.
REFERENCE   7
  AUTHORS   Ross, H.A. and Davies, H.V.
  TITLE     Purification and characterization of sucrose synthase from the
            cotyledons of Vicia fava L.
  JOURNAL   Plant Physiol. 100 (1992) 1008-1013.
  ORGANISM  Vicia fava
REFERENCE   8
  AUTHORS   Silvius, J.E. and Snyder, F.W.
  TITLE     Comparative enzymic studies of sucrose metabolism in the taproots
            and fibrous roots of Beta vulgaris L.
  JOURNAL   Plant Physiol. 64 (1979) 1070-1073.
  ORGANISM  Beta vulgaris
REFERENCE   9  [PMID:10845453]
  AUTHORS   Tanase K, Yamaki S.
  TITLE     Purification and characterization of two sucrose synthase isoforms
            from Japanese pear fruit.
  JOURNAL   Plant. Cell. Physiol. 41 (2000) 408-14.
  ORGANISM  Japanese pear fruit
REFERENCE   10 [PMID:12773636]
  AUTHORS   Baroja-Fernandez E, Munoz FJ, Saikusa T, Rodriguez-Lopez M, Akazawa
            T, Pozueta-Romero J.
  TITLE     Sucrose synthase catalyzes the de novo production of ADPglucose
            linked to starch biosynthesis in heterotrophic tissues of plants.
  JOURNAL   Plant. Cell. Physiol. 44 (2003) 500-9.
  ORGANISM  Hordeum vulgare [GN:ehvu]
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K00695  sucrose synthase
GENES       ATH: AT3G43190(SUS4) AT5G20830(SUS1) AT5G49190(SUS2)
            OSA: 4331252 4332788 4333062 4340386
            NOC: Noc_3068
            NEU: NE1214(ss2)
            NET: Neut_1079
            NMU: Nmul_A2266
            FAL: FRAAL3934
            TEL: tlr1047
            GVI: gll3607(spsA)
            ANA: all1059 all4985(susA)
            AVA: Ava_2283 Ava_3753
            TME: Tmel_0533
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.13
            ExPASy - ENZYME nomenclature database: 2.4.1.13
            ExplorEnz - The Enzyme Database: 2.4.1.13
            ERGO genome analysis and discovery system: 2.4.1.13
            BRENDA, the Enzyme Database: 2.4.1.13
            CAS: 9030-05-1
///
ENTRY       EC 2.4.1.14                 Enzyme
NAME        sucrose-phosphate synthase;
            UDP-glucose---fructose-phosphate glucosyltransferase;
            sucrosephosphate---UDP glucosyltransferase;
            UDP-glucose-fructose-phosphate glucosyltransferase;
            SPS;
            uridine diphosphoglucose-fructose phosphate glucosyltransferase;
            sucrose 6-phosphate synthase;
            sucrose phosphate synthetase;
            sucrose phosphate-uridine diphosphate glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:D-fructose-6-phosphate 2-alpha-D-glucosyltransferase
REACTION    UDP-glucose + D-fructose 6-phosphate = UDP + sucrose 6-phosphate
            [RN:R00766 R06073]
ALL_REAC    R00766 R06073(G)
SUBSTRATE   UDP-glucose [CPD:C00029];
            D-fructose 6-phosphate [CPD:C00085]
PRODUCT     UDP [CPD:C00015];
            sucrose 6-phosphate [CPD:C02591]
REFERENCE   1
  AUTHORS   Mendicino, J.
  TITLE     Sucrose phosphate synthesis in wheat germ and green leaves.
  JOURNAL   J. Biol. Chem. 235 (1960) 3347-3352.
  ORGANISM  spinach, Triticum aestivum [GN:etae]
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K00696  sucrose-phosphate synthase
GENES       ATH: AT5G20280(ATSPS1F)
            OSA: 4328527 4345220
            TCX: Tcr_1794
            NOC: Noc_3069
            NEU: NE1213(sps)
            NET: Neut_1080
            NMU: Nmul_A2267
            MFA: Mfla_2610
            MGM: Mmc1_3516
            CGB: cg0481
            RBA: RB5197(sps)
            SYN: sll0045(spsA)
            SYW: SYNW2520(sps)
            SYC: syc0730_d(sps)
            SYF: Synpcc7942_0808
            SYD: Syncc9605_2689
            SYE: Syncc9902_2315
            SYG: sync_2936
            SYR: SynRCC307_2529(sps)
            TEL: tlr0582(sps)
            PMA: Pro1880(rfaG)
            PMM: PMM1711(sps)
            PMT: PMT2268(sps)
            PMN: PMN2A_1322
            PMI: PMT9312_1803
            PMB: A9601_19201
            PMC: P9515_19021
            PMF: P9303_30171(sps)
            PMG: P9301_19011
            PME: NATL1_21951(sps)
            FJO: Fjoh_3967
            FNO: Fnod_0446
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.14
            ExPASy - ENZYME nomenclature database: 2.4.1.14
            ExplorEnz - The Enzyme Database: 2.4.1.14
            ERGO genome analysis and discovery system: 2.4.1.14
            BRENDA, the Enzyme Database: 2.4.1.14
            CAS: 9030-06-2
///
ENTRY       EC 2.4.1.15                 Enzyme
NAME        alpha,alpha-trehalose-phosphate synthase (UDP-forming);
            UDP-glucose---glucose-phosphate glucosyltransferase;
            trehalosephosphate-UDP glucosyltransferase;
            UDP-glucose-glucose-phosphate glucosyltransferase;
            alpha,alpha-trehalose phosphate synthase (UDP-forming);
            phosphotrehalose-uridine diphosphate transglucosylase;
            trehalose 6-phosphate synthase;
            trehalose 6-phosphate synthetase;
            trehalose phosphate synthase;
            trehalose phosphate synthetase;
            trehalose phosphate-uridine diphosphate glucosyltransferase;
            trehalose-P synthetase;
            transglucosylase;
            uridine diphosphoglucose phosphate glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:D-glucose-6-phosphate 1-alpha-D-glucosyltransferase
REACTION    UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose
            6-phosphate [RN:R00836 R06043]
ALL_REAC    R00836 R06043(G) > R02737 R06226(G)
SUBSTRATE   UDP-glucose [CPD:C00029];
            D-glucose 6-phosphate [CPD:C00092]
PRODUCT     UDP [CPD:C00015];
            alpha,alpha'-trehalose 6-phosphate [CPD:C00689]
COMMENT     See also EC 2.4.1.36 [alpha,alpha-trehalose-phosphate synthase
            (GDP-forming)].
REFERENCE   1  [PMID:13538966]
  AUTHORS   CABIB E, LELOIR LF.
  TITLE     The biosynthesis of trehalose phosphate.
  JOURNAL   J. Biol. Chem. 231 (1958) 259-75.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:13690400]
  AUTHORS   CANDY DJ, KILBY BA.
  TITLE     The biosynthesis of trehalose in the locust fat body.
  JOURNAL   Biochem. J. 78 (1961) 531-6.
  ORGANISM  Schistocerca gregaria
REFERENCE   3  [PMID:14216421]
  AUTHORS   LORNITZO FA, GOLDMAN DS.
  TITLE     PURIFICATION AND PROPERTIES OF THE TRANSGLUCOSYLASE INHIBITOR OF
            MYCOBACTERIUM TUBERCULOSIS.
  JOURNAL   J. Biol. Chem. 239 (1964) 2730-4.
  ORGANISM  Mycobacterium tuberculosis
REFERENCE   4  [PMID:14285483]
  AUTHORS   MURPHY TA, WYATT GR.
  TITLE     THE ENZYMES OF GLYCOGEN AND TREHALOSE SYNTHESIS IN SILK MOTH FAT
            BODY.
  JOURNAL   J. Biol. Chem. 240 (1965) 1500-8.
  ORGANISM  Hyalophora cecropia
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K00697  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
GENES       DME: Dmel_CG4104(Tps1)
            ATH: AT1G06410(ATTPS7)
            CME: CMI293C CMO053C CMP219C
            SCE: YBR126C(TPS1) YDR074W(TPS2) YML100W(TSL1) YMR261C(TPS3)
            AGO: AGOS_ADL378W AGOS_AER276C AGOS_AGR132W
            PIC: PICST_41330(TPS1) PICST_60441(TPS3)
            CAL: CaO19_3038(CaO19.3038)
            CGR: CAGL0G05335g CAGL0J06468g CAGL0J09812g
            SPO: SPAC19G12.15c SPAC22F8.05 SPAC328.03(tps1) SPACUNK4.16c
            ANI: AN4262.2 AN5523.2
            AFM: AFUA_2G04010 AFUA_2G04020 AFUA_3G05650 AFUA_4G03190
                 AFUA_5G14300 AFUA_6G12950 AFUA_7G03940
            AOR: AO090003000417 AO090020000035 AO090026000820
            ANG: An08g10510(tpsA)
            CNE: CNB02610 CNH03390
            ECU: ECU01_0800
            DDI: DDB_0231979(tpsA) DDB_0231987(tpsB)
            CHO: Chro.80565
            TAN: TA20125
            TET: TTHERM_00077390 TTHERM_00180940
            ECO: b1896(otsA)
            ECJ: JW5312(otsA)
            ECE: Z2949(otsA)
            ECS: ECs2604
            ECC: c2310(otsA)
            ECI: UTI89_C2097(otsA)
            ECP: ECP_1838
            ECV: APECO1_942(otsA)
            ECW: EcE24377A_2128(otsA)
            ECX: EcHS_A1993
            STY: STY2137(otsA)
            STT: t0949(otsA)
            SPT: SPA0940(otsA)
            SEC: SC1935(otsA)
            STM: STM1928(otsA)
            SSN: SSON_1221(otsA)
            SDY: SDY_1193(otsA)
            SGL: SG1241
            ENT: Ent638_2472
            XCC: XCC3082(ostA)
            XCB: XC_1076
            XCV: XCV3336(ostA2)
            XAC: XAC3211(ostA)
            XOO: XOO1601(ostA)
            XOM: XOO_1485(XOO1485)
            PCR: Pcryo_1802
            ACI: ACIAD1774(otsA)
            AEH: Mlg_0007
            HHA: Hhal_1120
            CSA: Csal_0234
            RSO: RS01697(RSp0731) RSp1105(otsA)
            REU: Reut_A0416
            REH: H16_A0430
            RME: Rmet_0357
            BMA: BMA0566(otsA-1) BMA3010(otsA-2)
            BMV: BMASAVP1_A0964(otsA-2) BMASAVP1_A2442(otsA-1)
            BML: BMA10299_A2839(otsA-1) BMA10299_A3032(otsA-2)
            BMN: BMA10247_1564(otsA-2) BMA10247_1765(otsA-1)
            BXE: Bxe_A1242 Bxe_A2256 Bxe_A3374 Bxe_C0845
            BVI: Bcep1808_1076 Bcep1808_2483 Bcep1808_4994
            BUR: Bcep18194_A4270 Bcep18194_A5719 Bcep18194_B1522
            BCN: Bcen_0679 Bcen_1781 Bcen_3925
            BCH: Bcen2424_1158 Bcen2424_2393 Bcen2424_4442
            BAM: Bamb_1036 Bamb_2438 Bamb_3873
            BPS: BPSL1044(otsA) BPSL2410(otsA)
            BPM: BURPS1710b_1263(otsA) BURPS1710b_2872(otsA)
            BPL: BURPS1106A_1109(otsA) BURPS1106A_2814(otsA)
            BPD: BURPS668_1104(otsA) BURPS668_2754(otsA)
            BTE: BTH_I0900 BTH_I1753
            RFR: Rfer_2163
            POL: Bpro_3918
            PNA: Pnap_0524
            AAV: Aave_2074 Aave_4212
            AJS: Ajs_0501
            MPT: Mpe_A3790
            GSU: GSU2337
            PCA: Pcar_3112
            PPD: Ppro_3271
            DDE: Dde_2060
            ADE: Adeh_0450 Adeh_1441
            AFW: Anae109_2390 Anae109_3011
            MXA: MXAN_1192(otsAB)
            SAT: SYN_00622 SYN_02628
            MLO: mll0691
            MES: Meso_1527
            PLA: Plav_0308
            SME: SMa0233(otsA)
            SMD: Smed_5911
            RET: RHE_CH00476(otsAch) RHE_PA00087(otsAa)
            RLE: RL0503(otsA)
            OAN: Oant_2713
            BJA: bll0322(otsA)
            BRA: BRADO6952(otsA)
            BBT: BBta_0578(otsA)
            RPA: RPA4660(otsA)
            RPB: RPB_0917 RPB_1021
            RPC: RPC_1943 RPC_4523
            RPD: RPD_1028
            RPE: RPE_1278 RPE_4553
            NWI: Nwi_3024
            NHA: Nham_3615
            XAU: Xaut_1721
            RSP: RSP_0948(otsA)
            RSH: Rsph17029_2608
            RSQ: Rsph17025_2944
            JAN: Jann_2063
            MMR: Mmar10_1020
            HNE: HNE_1575(otsA)
            NAR: Saro_1505
            SWI: Swit_3610
            ELI: ELI_04690
            GOX: GOX1119
            GBE: GbCGDNIH1_0746 GbCGDNIH1_1731
            ACR: Acry_0865
            RRU: Rru_A2485
            SUS: Acid_1156
            CHY: CHY_0670(otsA)
            MTA: Moth_1367
            MTU: Rv3490(otsA)
            MTC: MT3594(otsA)
            MBO: Mb3520(otsA)
            MBB: BCG_3554(otsA)
            MLE: ML2254(otsA)
            MPA: MAP0573c(otsA)
            MAV: MAV_0666(otsA)
            MSM: MSMEG_5892
            MVA: Mvan_5192
            MGI: Mflv_1566
            MMC: Mmcs_4609
            MKM: Mkms_4697
            MJL: Mjls_4992
            CGL: NCgl2535(cgl2624)
            CGB: cg2907(otsA)
            CEF: CE2508
            CDI: DIP1966
            CJK: jk0332(otsA)
            NFA: nfa5470
            RHA: RHA1_ro00090 RHA1_ro04708
            SCO: SCO4290(SCD95A.23c)
            SMA: SAV3936(otsA)
            LXX: Lxx13230(otsA)
            CMI: CMM_1085(otsA)
            ART: Arth_0752
            AAU: AAur_0931(otsA)
            PAC: PPA0961
            NCA: Noca_3994
            TFU: Tfu_0225
            FRA: Francci3_1478 Francci3_4395
            FAL: FRAAL2283 FRAAL6698(otsA)
            ACE: Acel_1953
            KRA: Krad_0920
            SEN: SACE_0462(otsA)
            STP: Strop_3271 Strop_3543
            RXY: Rxyl_2972
            SRU: SRU_0569
            CHU: CHU_0400(otsA)
            GFO: GFO_1041
            DGE: Dgeo_0059
            MTP: Mthe_0799
            MEM: Memar_2216
            HMA: rrnAC0237(otsA)
            TAC: Ta1210
            TVO: TVN1254
            PTO: PTO1209
            PIS: Pisl_1339
            PCL: Pcal_1363
            PAS: Pars_0598
STRUCTURES  PDB: 1GZ5  1UQT  1UQU  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.15
            ExPASy - ENZYME nomenclature database: 2.4.1.15
            ExplorEnz - The Enzyme Database: 2.4.1.15
            ERGO genome analysis and discovery system: 2.4.1.15
            BRENDA, the Enzyme Database: 2.4.1.15
            CAS: 9030-07-3
///
ENTRY       EC 2.4.1.16                 Enzyme
NAME        chitin synthase;
            chitin-UDP N-acetylglucosaminyltransferase;
            chitin-uridine diphosphate acetylglucosaminyltransferase;
            chitin synthetase;
            trans-N-acetylglucosaminosylase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:chitin
            4-beta-N-acetylglucosaminyl-transferase
REACTION    UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n =
            UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1 [RN:R02335 R06028]
ALL_REAC    R02335 R06028(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            [1,4-(N-acetyl-beta-D-glucosaminyl)]n [CPD:C00461]
PRODUCT     UDP [CPD:C00015];
            [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1 [CPD:C00461]
COMMENT     Converts UDP-N-acetyl-D-glucosamine into chitin and UDP.
REFERENCE   1  [PMID:13475355]
  AUTHORS   GLASER L, BROWN DH.
  TITLE     The synthesis of chitin in cell-free extracts of Neurospora crassa.
  JOURNAL   J. Biol. Chem. 228 (1957) 729-42.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2  [PMID:2945823]
  AUTHORS   Sburlati A, Cabib E.
  TITLE     Chitin synthetase 2, a presumptive participant in septum formation
            in Saccharomyces cerevisiae.
  JOURNAL   J. Biol. Chem. 261 (1986) 15147-52.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K00698  chitin synthase
GENES       DME: Dmel_CG2666(kkv) Dmel_CG7464(CS-2)
            SCE: YBR023C(CHS3) YBR038W(CHS2) YNL192W(CHS1)
            AGO: AGOS_ABL153W AGOS_AEL189W AGOS_AEL190W
            PIC: PICST_29105(CHS3) PICST_29807(CSH8) PICST_42812(CHS1)
                 PICST_51281(CHS2.2) PICST_65597(CHS2)
            CGR: CAGL0B04389g CAGL0I04818g CAGL0J11506g
            SPO: SPAC13G6.12c(chs1)
            ANI: AN4566.2
            AFM: AFUA_1G12600 AFUA_2G01870 AFUA_2G13430 AFUA_2G13440
                 AFUA_3G14420 AFUA_4G04180 AFUA_5G00760 AFUA_8G05630
            AOR: AO090005000579 AO090011000449 AO090206000079
            CNE: CNA05300 CNG02520 CNG04660 CNH02270 CNN02110
            UMA: UM00474.1 UM02569.1 UM03052.1 UM03204.1 UM05480.1
            TET: TTHERM_00006080 TTHERM_00011640 TTHERM_00113030
                 TTHERM_00113040 TTHERM_00113050 TTHERM_00113060
                 TTHERM_00113090 TTHERM_00599940 TTHERM_00822150
            EHI: 186.t00006
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.16
            ExPASy - ENZYME nomenclature database: 2.4.1.16
            ExplorEnz - The Enzyme Database: 2.4.1.16
            ERGO genome analysis and discovery system: 2.4.1.16
            BRENDA, the Enzyme Database: 2.4.1.16
            CAS: 9030-18-6
///
ENTRY       EC 2.4.1.17                 Enzyme
NAME        glucuronosyltransferase;
            1-naphthol glucuronyltransferase;
            1-naphthol-UDP-glucuronosyltransferase;
            17beta-hydroxysteroid UDP-glucuronosyltransferase;
            3alpha-hydroxysteroid UDP-glucuronosyltransferase;
            4-hydroxybiphenyl UDP-glucuronosyltransferase;
            4-methylumbelliferone UDP-glucuronosyltransferase;
            4-nitrophenol UDP-glucuronyltransferase;
            4-nitrophenol UDPGT;
            17-OH steroid UDPGT;
            3-OH androgenic UDPGT;
            bilirubin uridine diphosphoglucuronyltransferase;
            bilirubin UDP-glucuronosyltransferase;
            bilirubin monoglucuronide glucuronyltransferase;
            bilirubin UDPGT;
            bilirubin glucuronyltransferase;
            ciramadol UDP-glucuronyltransferase;
            estriol UDP-glucuronosyltransferase;
            estrone UDP-glucuronosyltransferase;
            uridine diphosphoglucuronosyltransferase;
            uridine diphosphoglucuronate-bilirubin glucuronoside
            glucuronosyltransferase;
            uridine diphosphoglucuronate-bilirubin glucuronosyltransferase;
            uridine diphosphoglucuronate-estriol glucuronosyltransferase;
            uridine diphosphoglucuronate-estradiol glucuronosyltransferase;
            uridine diphosphoglucuronate-4-hydroxybiphenyl
            glucuronosyltransferase;
            uridine diphosphoglucuronate-1,2-diacylglycerol
            glucuronosyltransferase;
            uridine diphosphoglucuronate-estriol
            16alpha-glucuronosyltransferase;
            uridine diphosphoglucuronosyltransferase;
            GT;
            morphine glucuronyltransferase;
            p-hydroxybiphenyl UDP glucuronyltransferase;
            p-nitrophenol UDP-glucuronosyltransferase;
            p-nitrophenol UDP-glucuronyltransferase;
            p-nitrophenylglucuronosyltransferase;
            p-phenylphenol glucuronyltransferase;
            phenyl-UDP-glucuronosyltransferase;
            PNP-UDPGT;
            UDP glucuronate-estradiol-glucuronosyltransferase;
            UDP glucuronosyltransferase;
            UDP glucuronate-estriol glucuronosyltransferase;
            UDP glucuronic acid transferase;
            UDP glucuronyltransferase;
            UDP-glucuronate-4-hydroxybiphenyl glucuronosyltransferase;
            UDP-glucuronate-bilirubin glucuronyltransferase;
            UDP-glucuronosyltransferase;
            UDP-glucuronyltransferase;
            UDPGA transferase;
            UDPGA-glucuronyltransferase;
            UDPGT;
            uridine diphosphoglucuronyltransferase;
            uridine diphosphoglucuronate-bilirubin glucuronosyltransferase;
            uridine diphosphate glucuronyltransferase;
            uridine 5'-diphosphoglucuronyltransferase;
            uridine diphosphoglucuronosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucuronate beta-D-glucuronosyltransferase (acceptor-unspecific)
REACTION    UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
            [RN:R01383]
ALL_REAC    R01383 > R02358 R02389 R02478 R02502 R02902 R03091 R04352 R04353
            R04354 R04683 R07106
SUBSTRATE   UDP-glucuronate [CPD:C00167];
            acceptor [CPD:C00028]
PRODUCT     UDP [CPD:C00015];
            acceptor beta-D-glucuronoside [CPD:C03033]
COMMENT     This entry denotes a family of enzymes accepting a wide range of
            substrates, including phenols, alcohols, amines and fatty acids.
            Some of the activities catalysed were previously listed separately
            as EC 2.4.1.42, EC 2.4.1.59, EC 2.4.1.61, EC 2.4.1.76, EC 2.4.1.77,
            EC 2.4.1.84, EC 2.4.1.107 and EC 2.4.1.108. A temporary nomenclature
            for the various forms, whose delineation is in a state of flux, is
            suggested in Ref. 1.
REFERENCE   1  [PMID:6404284]
  AUTHORS   Bock KW, Burchell B, Dutton GJ, Hanninen O, Mulder GJ, Owens IS,
            Siest G, Tephly TR.
  TITLE     UDP-glucuronosyltransferase activities. Guidelines for consistent
            interim terminology and assay conditions.
  JOURNAL   Biochem. Pharmacol. 32 (1983) 953-5.
  ORGANISM  rat [GN:rno], rabbit
REFERENCE   2  [PMID:111930]
  AUTHORS   Bock KW, Josting D, Lilienblum W, Pfeil H.
  TITLE     Purification of rat-liver microsomal UDP-glucuronyltransferase.
            Separation of two enzyme forms inducible by 3-methylcholanthrene or
            phenobarbital.
  JOURNAL   Eur. J. Biochem. 98 (1979) 19-26.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Burchell, B.
  TITLE     Identification and purification of multiple forms of
            UDP-glucuronosyltransferase.
  JOURNAL   Rev. Biochem. Toxicol. 3 (1981) 1-32.
REFERENCE   4
  AUTHORS   Dutton, G.J.
  TITLE     Glucuronidation of Drugs and Other Compounds, C.R.C. Press, Boca
            Raton, Florida, 1980.
REFERENCE   5  [PMID:3931633]
  AUTHORS   Green MD, Falany CN, Kirkpatrick RB, Tephly TR.
  TITLE     Strain differences in purified rat hepatic 3 alpha-hydroxysteroid
            UDP-glucuronosyltransferase.
  JOURNAL   Biochem. J. 230 (1985) 403-9.
  ORGANISM  rat [GN:rno]
REFERENCE   6
  AUTHORS   Jansen, P.L.M.
  TITLE     The enzyme-catalyzed formation of bilirubin diglucuronide by a
            solublized preparation from cat liver microsomes.
  JOURNAL   Biochim. Biophys. Acta 338 (1974) 170-182.
  ORGANISM  cat
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00150  Androgen and estrogen metabolism
            PATH: map00500  Starch and sucrose metabolism
            PATH: map00860  Porphyrin and chlorophyll metabolism
            PATH: map00980  Metabolism of xenobiotics by cytochrome P450
ORTHOLOGY   KO: K00699  glucuronosyltransferase
GENES       HSA: 10720(UGT2B11) 10941(UGT2A1) 54490(UGT2B28) 54575(UGT1A10)
                 54576(UGT1A8) 54577(UGT1A7) 54578(UGT1A6) 54579(UGT1A5)
                 54600(UGT1A9) 54657(UGT1A4) 54658(UGT1A1) 54659(UGT1A3)
                 7363(UGT2B4) 7364(UGT2B7) 7365(UGT2B10) 7366(UGT2B15)
                 7367(UGT2B17) 79799(UGT2A3)
            PTR: 461285(UGT2B4) 461289(UGT2B15) 471218(UGT2B7) 471220(UGT2A3)
            MMU: 22236(Ugt1a2) 22238(Ugt2b5) 394430(Ugt1a10) 394432(Ugt1a7c)
                 394433(Ugt1a5) 394434(Ugt1a9) 394435(Ugt1a6b) 394436(Ugt1a1)
                 552899(Ugt2a2) 71773(Ugt2b1) 72094(Ugt2a3) 94215(Ugt2a1)
                 94284(Ugt1a6a)
            RNO: 113992(Ugt1a6) 154516(Ugt1a7) 24861(Ugt1a1) 24862(Ugt2b)
                 266685(Ugt2b3) 286954(Udpgtr2) 289533(Ugt2a3_predicted)
                 29623(Ugt2b5) 301595(Ugt1a8) 396527(Ugt1a2) 396551(Ugt1a3)
                 396552(Ugt1a10) 574523(Ugt1a5) 63867(Ugt2a1) 83808(Ugt2b4)
            CFA: 403629(UGT1A6) 442984(UGT2B31) 480777(LOC480777)
                 608760(LOC608760)
            BTA: 286792(UGT1A4) 511743(MGC139210) 533587(UGT2B4)
                 540615(LOC540615) 615303(LOC615303)
            GGA: 422660(UGT2A1) 424028(UGT1A1)
            DRE: 406731(zgc:66393) 570913(LOC570913)
            SPU: 578573(LOC578573) 592958(LOC592958) 593427(LOC593427)
            DME: Dmel_CG11012(Ugt37a1) Dmel_CG11289 Dmel_CG13270 Dmel_CG13271
                 Dmel_CG15902(Ugt86Dj) Dmel_CG17200(Ugt86Dg)
                 Dmel_CG17932(Ugt36Bc) Dmel_CG18578 Dmel_CG3881(GlcAT-S)
                 Dmel_CG4414(Ugt58Fa) Dmel_CG4739(Ugt86Dc) Dmel_CG4772(Ugt86Dh)
                 Dmel_CG6207(GlcAT-P) Dmel_CG6633 Dmel_CG6644(Ugt35a)
                 Dmel_CG6649(Ugt35b) Dmel_CG6653(Ugt86De) Dmel_CG6658(Ugt86Di)
                 Dmel_CG8652(Ugt37c1) Dmel_CG9481(Ugt37b1)
            CEL: B0310.5(ugt-46) C18C4.3(ugt-48)
                 F35H8.6(UDP-glucuronosyltransferase) F39G3.1(ugt-61)
                 T04H1.7(UDP-sugartransferase)
                 T04H1.8(UDP-glucuronosyltransferase) T07C5.1(ugt-50)
            AHA: AHA_3280
            BUR: Bcep18194_A5063
            BAM: Bamb_1700
            BBT: BBta_4109
            BCZ: pE33L466_0393
            BPU: BPUM_3097
            FAL: FRAAL1553 FRAAL2903 FRAAL2910
            SEN: SACE_2346
STRUCTURES  PDB: 2O6L  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.17
            ExPASy - ENZYME nomenclature database: 2.4.1.17
            ExplorEnz - The Enzyme Database: 2.4.1.17
            ERGO genome analysis and discovery system: 2.4.1.17
            BRENDA, the Enzyme Database: 2.4.1.17
            CAS: 9030-08-4
///
ENTRY       EC 2.4.1.18                 Enzyme
NAME        1,4-alpha-glucan branching enzyme;
            branching enzyme;
            amylo-(1,4->1,6)-transglycosylase;
            Q-enzyme;
            alpha-glucan-branching glycosyltransferase;
            amylose isomerase;
            enzymatic branching factor;
            branching glycosyltransferase;
            enzyme Q;
            glucosan transglycosylase;
            glycogen branching enzyme;
            plant branching enzyme;
            alpha-1,4-glucan:alpha-1,4-glucan-6-glycosyltransferase;
            starch branching enzyme
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     1,4-alpha-D-glucan:1,4-alpha-D-glucan
            6-alpha-D-(1,4-alpha-D-glucano)-transferase
REACTION    Transfers a segment of a 1,4-alpha-D-glucan chain to a primary
            hydroxy group in a similar glucan chain [RN:R02110 R06186]
ALL_REAC    R02110 R06186(G)
COMMENT     Converts amylose into amylopectin. The accepted name requires a
            qualification depending on the product, glycogen or amylopectin,
            e.g. glycogen branching enzyme, amylopectin branching enzyme. The
            latter has frequently been termed Q-enzyme.
REFERENCE   1
  AUTHORS   Barker, S.A., Bourne, E. and Peat, S.
  TITLE     The enzymic synthesis and degradation of starch. Part IV. The
            purification and storage of the Q-enzyme of the potato.
  JOURNAL   J. Chem. Soc. (Lond.) (1949) 1705-1711.
  ORGANISM  Solanum tuberosum [GN:estu]
REFERENCE   2
  AUTHORS   Baum, H. and Gilbert, G.A.
  TITLE     A simple method for the preparation of crystalline potato
            phosphorylase and Q-enzyme.
  JOURNAL   Nature 171 (1953) 983-984.
  ORGANISM  Solanum tuberosum [GN:estu]
REFERENCE   3
  AUTHORS   Hehre, E.J.
  TITLE     Enzymic synthesis of polysaccharides: a biological type of
            polymerization.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297-337.
REFERENCE   4  [PMID:16522734]
  AUTHORS   Allan CM, Wang Y, Jimenez M, Marshan B, Spaliviero J, Illingworth P,
            Handelsman DJ.
  TITLE     Follicle-stimulating hormone increases primordial follicle reserve
            in mature female hypogonadal mice.
  JOURNAL   J. Endocrinol. 188 (2006) 549-57.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K00700  1,4-alpha-glucan branching enzyme
GENES       HSA: 2632(GBE1)
            PTR: 460520(GBE1)
            MMU: 74185(Gbe1)
            RNO: 288333(Gbe1)
            CFA: 478380(GBE1)
            GGA: 427964(GBE1)
            XLA: 446356(gbe1) 495215(LOC495215)
            DME: Dmel_CG33138
            ATH: AT2G36390(SBE2.1) AT5G03650(SBE2.2)
            OSA: 4329532 4342117
            CME: CMH144C
            SCE: YEL011W(GLC3)
            AGO: AGOS_AEL044W
            PIC: PICST_88710(GLC3)
            CGR: CAGL0M03377g
            ANI: AN2314.2
            AFM: AFUA_5G10540
            AOR: AO090010000483
            CNE: CNA03810
            UMA: UM04470.1
            DDI: DDB_0214943(glgB)
            CPV: cgd6_3280
            CHO: Chro.60381
            TET: TTHERM_00666570 TTHERM_01435670
            EHI: 448.t00005 74.t00006
            ECO: b3432(glgB)
            ECJ: JW3395(glgB)
            ECE: Z4796(glgB)
            ECS: ECs4277
            ECC: c4219(glgB)
            ECI: UTI89_C3941(glgB)
            ECP: ECP_3526
            ECW: EcE24377A_3911(glgB)
            ECX: EcHS_A3632(glgB)
            STY: STY4272(glgB)
            STT: t3982(glgB)
            SPT: SPA3389(glgB)
            SEC: SC3468(glgB)
            STM: STM3538(glgB)
            YPE: YPO3942(glgB)
            YPK: y3886(glgB)
            YPM: YP_3304(glgB)
            YPA: YPA_3771
            YPN: YPN_3590
            YPS: YPTB3787(glgB)
            YPI: YpsIP31758_4006(glgB)
            SFL: SF3455(glgB)
            SFX: S4308(glgB)
            SFV: SFV_3441(glgB)
            SSN: SSON_3672(glgB)
            SBO: SBO_3430(glgB)
            SDY: SDY_3578(glgB)
            ECA: ECA4151(glgB)
            HIN: HI1357(glgB)
            HIT: NTHI1809(glgB)
            HIP: CGSHiEE_04320
            HIQ: CGSHiGG_00445
            HSO: HS_0889(glgB)
            PMU: PM0541(glgB)
            MSU: MS1123(glgB)
            APL: APL_0346(glgB)
            XCC: XCC0135(glgB1) XCC0409(glgB2)
            XCB: XC_0143 XC_0422
            XCV: XCV0141(glgB1) XCV0452(glgB2)
            XAC: XAC0156(glgB1) XAC0426(glgB2)
            XOO: XOO0113(glgB2) XOO0194(glgB1)
            XOM: XOO_0065(XOO0065) XOO_0173(XOO0173)
            VCH: VCA0015 VCA0016
            VCO: VC0395_0117(glgB)
            VVU: VV2_1252
            VVY: VVA0079
            VPA: VPA1618
            VFI: VFA0808
            PPR: PBPRB1328
            PAE: PA2153(glgB)
            PAU: PA14_36710(glgB)
            PAP: PSPA7_3153(glgB)
            PPU: PP_4058(glgB)
            PST: PSPTO_2762(glgB)
            PSB: Psyr_2491
            PSP: PSPPH_2648(glgB)
            PFL: PFL_2874(glgB)
            PFO: Pfl_2536
            PEN: PSEEN2046(glgB)
            SON: SO_1494(glgB)
            SFR: Sfri_2165
            SBL: Sbal_1331
            SLO: Shew_1168
            SHE: Shewmr4_2758
            SHM: Shewmr7_2836
            SHN: Shewana3_2934
            SHW: Sputw3181_2856
            PAT: Patl_1636
            SDE: Sde_0987
            MAQ: Maqu_1434
            MCA: MCA1475(glgB)
            FTU: FTT0413c(glgB)
            FTF: FTF0413c(glgB)
            FTW: FTW_1660(glgB)
            FTL: FTL_0483
            FTH: FTH_0481(glgB)
            FTA: FTA_0509(glgB)
            FTN: FTN_0513(glgB)
            TCX: Tcr_0511
            NOC: Noc_0904 Noc_1681
            AEH: Mlg_0958
            AHA: AHA_3616(glgB)
            RSO: RSp0239(glgB)
            REU: Reut_B4229
            REH: H16_B1559(glgB)
            BMV: BMASAVP1_A1338(glgB) BMASAVP1_A1339
            BML: BMA10299_A0535(glgB-1) BMA10299_A0536(glgB-2)
            BMN: BMA10247_0619(glgB) BMA10247_0620
            BXE: Bxe_B2863
            BUR: Bcep18194_C7032
            BCN: Bcen_1332
            BCH: Bcen2424_6497
            BAM: Bamb_5592
            BPS: BPSL2076(glgB)
            BPM: BURPS1710b_1737(glgB) BURPS1710b_A0879
            BPL: BURPS1106A_1566(glgB)
            BPD: BURPS668_1543(glgB)
            BTE: BTH_II0939(glgB)
            BPE: BP1328(glgB)
            BPA: BPP2892(glgB)
            BBR: BB2864(glgB)
            RFR: Rfer_2162
            PNA: Pnap_1104
            AAV: Aave_2024
            NEU: NE2029(glgB)
            NET: Neut_1291
            NMU: Nmul_A0717 Nmul_A1403
            EBA: ebA6920 ebA7003(glgB)
            AZO: azo1725(glgB1) azo1796(glgB2)
            DAR: Daro_0586
            TBD: Tbd_1173 Tbd_2058
            MFA: Mfla_1367
            NIS: NIS_0936(glgB)
            SUN: SUN_1268(glgB)
            DVU: DVU2243(glgB)
            DDE: Dde_2285
            MXA: MXAN_3682(glgB)
            SAT: SYN_02257
            SFU: Sfum_3451
            MLO: mlr7587
            MES: Meso_2677
            SME: SMb21447(glgB2) SMc03922(glgB1)
            ATU: Atu4077(glgB) Atu5284
            ATC: AGR_L_1558 AGR_pAT_409
            RET: RHE_CH03594(glgBch) RHE_PF00263 RHE_PF00275(glgBf)
            RLE: RL2413 RL4115(glgB) pRL120710(glgB) pRL120722
            BJA: blr6768(glgB)
            BRA: BRADO3025 BRADO5817(glgB)
            BBT: BBta_5116 BBta_6323(glgB)
            RPA: RPA3644(glgB) RPA3646
            RPB: RPB_1882
            RPC: RPC_3680
            RPD: RPD_3484
            RPE: RPE_3718
            NWI: Nwi_1207
            NHA: Nham_1464
            RSP: RSP_2448(glgB1)
            RSH: Rsph17029_1111
            JAN: Jann_3113
            RDE: RD1_2875(glgB)
            NAR: Saro_1658
            GBE: GbCGDNIH1_0750
            RRU: Rru_A0506 Rru_A2576
            MAG: amb3065
            MGM: Mmc1_1392 Mmc1_1518
            SUS: Acid_7335
            BSU: BG10907(glgB)
            BAN: BA5123(glgB)
            BAR: GBAA5123(glgB)
            BAA: BA_5542
            BAT: BAS4761
            BCE: BC4867
            BCA: BCE_5028(glgB)
            BCZ: BCZK4621(glgB)
            BTK: BT9727_4599(glgB)
            BTL: BALH_4432(glgB)
            BLI: BL01419(glgB)
            BLD: BLi03230(glgB)
            OIH: OB0406
            LLC: LACR_0145
            LLM: llmg_0158(glgB)
            SPN: SP_1121
            SPR: spr1029(glgB)
            SPD: SPD_1005(glgB)
            SAG: SAG0853(glgB)
            SAN: gbs0871
            SAK: SAK_0976(glgB)
            SMU: SMU.1539(glgB)
            SSA: SSA_0775(glgB)
            SGO: SGO_1554(glgB)
            LPL: lp_0020(glgB)
            LAC: LBA0680(glgB)
            LSL: LSL_1294(glgB)
            LCA: LSEI_2040
            CPE: CPE0063(glgB) CPE1588(glgB)
            CPF: CPF_1840(glgB)
            CPR: CPR_0081(glgB) CPR_1559(glgB)
            CTH: Cthe_2191
            CDF: CD2526(gbeA)
            CKL: CKL_3498(glgB)
            DSY: DSY2040
            MMO: MMOB4010(glgB)
            MTU: Rv1326c(glgB)
            MTC: MT1368(glgB)
            MBO: Mb1361c(glgB)
            MBB: BCG_1388c(glgB)
            MPA: MAP2434(glgB)
            MSM: MSMEG_4918(glgB)
            MMC: Mmcs_3861
            CGL: NCgl1177(cgl1224)
            CGB: cg1381(glgB)
            CEF: CE1323
            CDI: DIP1065(glgB)
            CJK: jk1330(glgB)
            NFA: nfa10780(glgB)
            RHA: RHA1_ro01449(glgB)
            SCO: SCO5440(glgBI) SCO7332(glgBII)
            SMA: SAV2805(glgB) SAV7398 SAV7399
            LXX: Lxx12570(glgB)
            CMI: CMM_1397(glgB)
            ART: Arth_0739
            AAU: AAur_0910(glgB)
            PAC: PPA1111
            NCA: Noca_1806
            TFU: Tfu_0582
            FRA: Francci3_3681
            FAL: FRAAL5902(glgB)
            ACE: Acel_0676
            BLO: BL0999(glgB)
            BAD: BAD_0667(glgB)
            RXY: Rxyl_0316
            FNU: FN0856
            RBA: RB2638(glgB) RB548(glgB)
            CTR: CT866(glgB)
            CTA: CTA_0946(glgB)
            CMU: TC0257
            CPN: CPn0475(glgB)
            CPA: CP0279
            CPJ: CPj0475(glgB)
            CPT: CpB0494
            CCA: CCA00268(glgB)
            CAB: CAB262(glgB)
            CFE: CF0740(glgB)
            PCU: pc1761(glgB)
            SYN: sll0158(glgB)
            SYW: SYNW1494(glgB)
            SYC: syc0464_c(glgB)
            SYF: Synpcc7942_1085
            SYD: Syncc9605_1018
            SYE: Syncc9902_0919
            SYG: sync_1886(glgB)
            SYR: SynRCC307_0920
            CYA: CYA_2062(glgB)
            CYB: CYB_1978(glgB)
            TEL: tll0578(glgB)
            GVI: gll1431 glr1306(glgB)
            ANA: all0713(glgB) all0875(lti2)
            AVA: Ava_4479 Ava_4616
            PMA: Pro1078(glgB)
            PMM: PMM0584(glgB)
            PMT: PMT0444(glgB)
            PMN: PMN2A_0020
            PMI: PMT9312_0584
            PMB: A9601_06401(glgB)
            PMC: P9515_06491(glgB)
            PMF: P9303_18371(glgB)
            PMG: P9301_06101(glgB)
            PMH: P9215_06661(glgB)
            PME: NATL1_06401(glgB)
            TER: Tery_1837
            BTH: BT_0771
            BFR: BF2243
            BFS: BF2338
            PGI: PG1793(glgB)
            SRU: SRU_0846(glgB)
            CHU: CHU_1345(glgB)
            GFO: GFO_2997(glgB)
            DRA: DR_1848
            DGE: Dgeo_0981
            AAE: aq_722(glgB)
            MEM: Memar_1265
            PTO: PTO0067 PTO0068
STRUCTURES  PDB: 1M7X  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.18
            ExPASy - ENZYME nomenclature database: 2.4.1.18
            ExplorEnz - The Enzyme Database: 2.4.1.18
            ERGO genome analysis and discovery system: 2.4.1.18
            BRENDA, the Enzyme Database: 2.4.1.18
            CAS: 9001-97-2
///
ENTRY       EC 2.4.1.19                 Enzyme
NAME        cyclomaltodextrin glucanotransferase;
            Bacillus macerans amylase;
            cyclodextrin glucanotransferase;
            alpha-cyclodextrin glucanotransferase;
            alpha-cyclodextrin glycosyltransferase;
            beta-cyclodextrin glucanotransferase;
            beta-cyclodextrin glycosyltransferase;
            gamma-cyclodextrin glycosyltransferase;
            cyclodextrin glycosyltransferase;
            cyclomaltodextrin glucotransferase;
            cyclomaltodextrin glycosyltransferase;
            konchizaimu;
            alpha-1,4-glucan 4-glycosyltransferase, cyclizing;
            BMA;
            CGTase;
            neutral-cyclodextrin glycosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     1,4-alpha-D-glucan 4-alpha-D-(1,4-alpha-D-glucano)-transferase
            (cyclizing)
REACTION    Cyclizes part of a 1,4-alpha-D-glucan chain by formation of a
            1,4-alpha-D-glucosidic bond
COMMENT     Cyclomaltodextrins (Schardinger dextrins) of various sizes (6,7,8,
            etc. glucose units) are formed reversibly from starch and similar
            substrates. Will also disproportionate linear maltodextrins without
            cyclizing (cf. EC 2.4.1.25, 4-alpha-glucanotransferase).
REFERENCE   1  [PMID:5758537]
  AUTHORS   DePinto JA, Campbell LL.
  TITLE     Purification and properties of the amylase of Bacillus macerans.
  JOURNAL   Biochemistry. 7 (1968) 114-20.
  ORGANISM  Bacillus macerans
REFERENCE   2
  AUTHORS   French, D., Levine, M.L., Norberg, E., Norden, P., Pazur, J.H. and
            Wild, G.M.
  TITLE     Studies on the Schardinger dextrins. VII. Co-substrate specificity
            in coupling reactions of Macerans amylase.
  JOURNAL   J. Am. Chem. Soc. 76 (1954) 2387-2390.
  ORGANISM  Bacillus macerans
REFERENCE   3
  AUTHORS   Hehre, E.J.
  TITLE     Enzymic synthesis of polysaccharides: a biological type of
            polymerization.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297-337.
REFERENCE   4  [PMID:13031665]
  AUTHORS   SCHWIMMER S.
  TITLE     Evidence for the purity of Schardinger dextrinogenase.
  JOURNAL   Arch. Biochem. Biophys. 43 (1953) 108-17.
  ORGANISM  Bacillus macerans
ORTHOLOGY   KO: K00701  cyclomaltodextrin glucanotransferase
GENES       XCC: XCC2465(cgt)
            XCB: XC_1648
            XCV: XCV2797(cgt)
            XAC: XAC2596(cgt)
            SPY: SPy_1302(amyA)
            SPH: MGAS10270_Spy1121(amyA)
            SPI: MGAS10750_Spy1157 MGAS10750_Spy1158(amyA)
            TTE: TTE1832(amyA2)
            GVI: glr0373
            ANA: alr0169
            AVA: Ava_1429
            SRU: SRU_2409
STRUCTURES  PDB: 1A47  1CDG  1CGT  1CGU  1CGV  1CGW  1CGX  1CGY  1CIU  1CXE  
                 1CXF  1CXH  1CXI  1CXK  1CXL  1CYG  1D3C  1D7F  1DED  1DTU  
                 1EO5  1EO7  1I75  1KCK  1KCL  1OT1  1OT2  1PAM  1PEZ  1PJ9  
                 1TCM  1UKQ  1UKS  1UKT  1V3J  1V3K  1V3L  1V3M  2CXG  2DIJ  
                 3CGT  4CGT  5CGT  6CGT  7CGT  8CGT  9CGT  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.19
            ExPASy - ENZYME nomenclature database: 2.4.1.19
            ExplorEnz - The Enzyme Database: 2.4.1.19
            ERGO genome analysis and discovery system: 2.4.1.19
            BRENDA, the Enzyme Database: 2.4.1.19
            CAS: 9030-09-5
///
ENTRY       EC 2.4.1.20                 Enzyme
NAME        cellobiose phosphorylase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     cellobiose:phosphate alpha-D-glucosyltransferase
REACTION    cellobiose + phosphate = alpha-D-glucose 1-phosphate + D-glucose
            [RN:R00952 R06056]
ALL_REAC    R00952 R06056(G)
SUBSTRATE   cellobiose [CPD:C00185];
            phosphate [CPD:C00009]
PRODUCT     alpha-D-glucose 1-phosphate [CPD:C00103];
            D-glucose [CPD:C00031]
REFERENCE   1  [PMID:5653182]
  AUTHORS   Alexander JK.
  TITLE     Purification and specificity of cellobiose phosphorylase from
            Clostridium thermocellum.
  JOURNAL   J. Biol. Chem. 243 (1968) 2899-904.
  ORGANISM  Clostridium thermocellum [GN:cth]
REFERENCE   2  [PMID:13795349]
  AUTHORS   AYERS WA.
  TITLE     Phosphorolysis and synthesis of cellobiose by cell extracts from
            Ruminococcus flavefaciens.
  JOURNAL   J. Biol. Chem. 234 (1959) 2819-22.
  ORGANISM  Ruminococcus flavefaciens
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K00702  cellobiose phosphorylase
GENES       ECI: UTI89_C1926(ydjC)
            CVI: CV_1158
            BXE: Bxe_C1346
            AZO: azo0748
            BME: BMEI1837
STRUCTURES  PDB: 2CQS  2CQT  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.20
            ExPASy - ENZYME nomenclature database: 2.4.1.20
            ExplorEnz - The Enzyme Database: 2.4.1.20
            ERGO genome analysis and discovery system: 2.4.1.20
            BRENDA, the Enzyme Database: 2.4.1.20
            CAS: 9030-20-0
///
ENTRY       EC 2.4.1.21                 Enzyme
NAME        starch synthase;
            ADP-glucose---starch glucosyltransferase;
            adenosine diphosphate glucose-starch glucosyltransferase;
            adenosine diphosphoglucose-starch glucosyltransferase;
            ADP-glucose starch synthase;
            ADP-glucose synthase;
            ADP-glucose transglucosylase;
            ADP-glucose-starch glucosyltransferase;
            ADPG starch synthetase;
            ADPG-starch glucosyltransferase;
            starch synthetase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     ADP-glucose:1,4-alpha-D-glucan 4-alpha-D-glucosyltransferase
REACTION    ADP-glucose + (1,4-alpha-D-glucosyl)n = ADP +
            (1,4-alpha-D-glucosyl)n+1 [RN:R02421 R06049]
ALL_REAC    R02421 R06049(G)
SUBSTRATE   ADP-glucose [CPD:C00498];
            (1,4-alpha-D-glucosyl)n [CPD:C00718]
PRODUCT     ADP [CPD:C00008];
            (1,4-alpha-D-glucosyl)n+1 [CPD:C00718]
COMMENT     The accepted name varies according to the source of the enzyme and
            the nature of its synthetic product, e.g. starch synthase, bacterial
            glycogen synthase. Similar to EC 2.4.1.11 [glycogen(starch)
            synthase] but the preferred or mandatory nucleoside diphosphate
            sugar substrate is ADP-glucose. The entry covers starch and glycogen
            synthases utilizing ADP-glucose.
REFERENCE   1  [PMID:4317490]
  AUTHORS   Chambers J, Elbein AD.
  TITLE     Biosynthesis of glucans in mung bean seedlings. Formation of
            beta-(1,4)-glucans from GDP-glucose and beta-(1,3)-glucans from
            UDP-glucose.
  JOURNAL   Arch. Biochem. Biophys. 138 (1970) 620-31.
  ORGANISM  Phaseolus aureus
REFERENCE   2  [PMID:14298833]
  AUTHORS   FRYDMAN RB, CARDINI CE.
  TITLE     STUDIES ON ADENOSINE DIPHOSPHATE D-GLUCOSE: ALPHA-1,4-GLUCAN
            ALPHA-4-GLUCOSYLTRANSFERASE OF SWEET-CORN ENDOSPERM.
  JOURNAL   Biochim. Biophys. Acta. 96 (1965) 294-303.
  ORGANISM  Solanum tuberosum [GN:estu], Zea mays [GN:ezma]
REFERENCE   3
  AUTHORS   Greenberg, E. and Preiss, J.
  TITLE     Biosynthesis of bacterial glycogen. II. Purification and properties
            of the adenosine diphosphoglucose:glycogen transglucosylase of
            arthrobacter species NRRL B1973.
  JOURNAL   J. Biol. Chem. 240 (1965) 2341-2348.
  ORGANISM  Arthrobacter sp.
REFERENCE   4
  AUTHORS   Leloir, L.F., de Fekete, M.A. and Cardini, C.E.
  TITLE     Starch and oligosaccharide synthesis from uridine diphosphate
            glucose.
  JOURNAL   J. Biol. Chem. 236 (1961) 636-641.
REFERENCE   5
  AUTHORS   Preiss, J., Govins, S., Eidels, L., Lammel, C., Greenberg, E.,
            Edelmann, P. and Sabraw, A.
  TITLE     Regulatory mechanisms in the biosynthesis of alpha-1,4-glucans in
            bacteria and plants.
  JOURNAL   In: Whelan, W.J. and Schultz, J. (Eds.), Miami Winter Symposia, vol.
            1, North Holland, Utrecht, 1970, p. 122-138.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K00703  starch synthase
GENES       CFA: 611993(LOC611993)
            OSA: 4340018 4340567
            TET: TTHERM_00725970
            EHI: 94.t00005
            ECO: b3429(glgA)
            ECJ: JW3392(glgA)
            ECE: Z4791(glgA)
            ECS: ECs4274
            ECC: c4216(glgA)
            ECI: UTI89_C3938(glgA)
            ECP: ECP_3523
            ECV: APECO1_3028(glgA)
            ECW: EcE24377A_3908(glgA)
            ECX: EcHS_A3629(glgA)
            STY: STY4275(glgA)
            STT: t3985(glgA)
            SPT: SPA3386(glgA)
            SEC: SC3465(glgA)
            STM: STM3535(glgA)
            YPE: YPO3939(glgA)
            YPK: y3889(glgA)
            YPM: YP_3301(glgA)
            YPA: YPA_3768
            YPN: YPN_3587
            YPP: YPDSF_3304
            YPS: YPTB3784(glgA)
            YPI: YpsIP31758_4003(glgA)
            SFL: SF3452(glgA)
            SFX: S4311(glgA)
            SFV: SFV_3438(glgA)
            SSN: SSON_3669(glgA)
            SBO: SBO_3427(glgA)
            SDY: SDY_3575(glgA)
            ECA: ECA4148(glgA)
            HIN: HI1360(glgA)
            HIT: NTHI1806(glgA)
            HIP: CGSHiEE_04335(glgA)
            HIQ: CGSHiGG_00460(glgA)
            HSO: HS_0886(glgA)
            PMU: PM0544(glgA)
            MSU: MS1120(glgA)
            APL: APL_0349(glgA)
            ASU: Asuc_1355
            XCC: XCC0408(glgA)
            XCB: XC_0421
            XCV: XCV0451(glgA)
            XAC: XAC0425(glgA)
            XOO: XOO0112(glgA)
            XOM: XOO_0066(XOO0066)
            VCH: VC1726
            VCO: VC0395_A1329(glgA)
            VVU: VV1_2132
            VVY: VV2312
            VPA: VP1024
            VFI: VFA0805
            PPR: PBPRB0406
            PAE: PA2165
            PAU: PA14_36570(glgA)
            PPU: PP_4050(glgA)
            PST: PSPTO_3125(glgA)
            PSB: Psyr_2992
            PSP: PSPPH_2248(glgA)
            PFL: PFL_2887(glgA)
            PFO: Pfl_2549
            PEN: PSEEN2054
            PMY: Pmen_2277
            SON: SO_1499(glgA)
            SFR: Sfri_2161
            SAZ: Sama_2449
            SBL: Sbal_1335
            SLO: Shew_1172
            SPC: Sputcn32_1252
            SHE: Shewmr4_2754
            SHM: Shewmr7_2832
            SHN: Shewana3_2930
            SHW: Sputw3181_2852
            PAT: Patl_0080
            SDE: Sde_0991
            PIN: Ping_2348 Ping_3035
            MAQ: Maqu_1435
            MCA: MCA1476(glgA) MCA2606
            FTU: FTT0416(glgA)
            FTF: FTF0416(glgA)
            FTW: FTW_1657(glgA)
            FTL: FTL_0486
            FTH: FTH_0484(glgA)
            FTA: FTA_0512
            FTN: FTN_0516(glgA)
            TCX: Tcr_0512
            NOC: Noc_0100 Noc_0771
            AEH: Mlg_0957
            HHA: Hhal_1104
            AHA: AHA_3804
            RSO: RSp0242(glgA)
            BXE: Bxe_A2935 Bxe_B1279
            BUR: Bcep18194_B2268 Bcep18194_B2867
            BTE: BTH_II0940
            BPA: BPP2889(glgA)
            BBR: BB2861(glgA)
            RFR: Rfer_0512
            PNA: Pnap_1107
            AAV: Aave_2986
            NEU: NE2264(glgA1)
            NET: Neut_0608
            NMU: Nmul_A0716
            EBA: ebA6917(glgA)
            AZO: azo1801(glgA)
            DAR: Daro_0580
            TBD: Tbd_2057
            MFA: Mfla_1472
            NIS: NIS_0937
            SUN: SUN_1269 SUN_1271
            GSU: GSU1023(glgA-1) GSU3257(glgA-2)
            GME: Gmet_0707 Gmet_3175
            PCA: Pcar_2954
            PPD: Ppro_0293
            DVU: DVU2244(glgA)
            DDE: Dde_2286
            ADE: Adeh_0135
            AFW: Anae109_0139
            MXA: MXAN_1296(glgA)
            SAT: SYN_00877
            SFU: Sfum_2113
            MLO: mlr7589
            SME: SMb20704(glgA2) SMc03924(glgA1)
            SMD: Smed_2742 Smed_4276
            ATU: Atu4075(glgA) Atu5285(glgA)
            ATC: AGR_L_1562 AGR_pAT_410
            RET: RHE_CH03596(glgA)
            RLE: RL4117(glgA)
            BJA: bll2778(glgA) blr6459(glgA)
            BRA: BRADO2453(glgA) BRADO6612(glgA)
            BBT: BBta_0923(glgA) BBta_2800(glgA) BBta_p0155(glgA)
            RPA: RPA0382(glgA1)
            RPB: RPB_0441
            RPC: RPC_0612
            RPD: RPD_0344
            RPE: RPE_0800
            RSP: RSP_2885(glgA)
            RSH: Rsph17029_1531
            RSQ: Rsph17025_1135
            JAN: Jann_3115
            RDE: RD1_2873 RD1_3845
            PDE: Pden_4426
            NAR: Saro_1656
            GBE: GbCGDNIH1_2341
            RRU: Rru_A2245
            MAG: amb2111
            MGM: Mmc1_1517 Mmc1_1521
            ABA: Acid345_3349
            SUS: Acid_0307
            BSU: BG10910(glgA)
            BHA: BH1085(glgA)
            BAN: BA5120(glgA)
            BAR: GBAA5120(glgA)
            BAA: BA_5539
            BAT: BAS4758
            BCE: BC4864(glgA)
            BCA: BCE_5025(glgA)
            BCZ: BCZK4618(glgA)
            BTK: BT9727_4596(glgA)
            BTL: BALH_4429(glgA)
            BLI: BL01416(glgA)
            BLD: BLi03227(glgA)
            OIH: OB0409
            LWE: lwe2640
            LLA: L98347(glgA)
            LLC: LACR_0726
            LLM: llmg_1872(glgA)
            SPN: SP_1124
            SPR: spr1032(glgA)
            SPD: SPD_1008(glgA)
            SAG: SAG0856(glgA)
            SAN: gbs0874
            SAK: SAK_0979(glgA)
            SMU: SMU.1536(glgA)
            SSA: SSA_0778(glgA)
            SGO: SGO_1551(glgA)
            LPL: lp_0023(glgA)
            LAC: LBA0683
            LSL: LSL_1291(glgA)
            LCA: LSEI_2037
            CAC: CAC2239(glgA)
            CPE: CPE0064(glgA)
            CPR: CPR_0082
            CNO: NT01CX_1242
            CTH: Cthe_1284
            CDF: CD0884(glgA)
            CKL: CKL_3497(glgA)
            DSY: DSY2036
            MTA: Moth_1936
            MMO: MMOB4020(glgA)
            FNU: FN0853
            RBA: RB6654(glgA)
            CTR: CT798(glgA)
            CTA: CTA_0869(glgA)
            CMU: TC0181
            CPN: CPn0948(glgA)
            CPA: CP0911
            CPJ: CPj0948(glgA)
            CPT: CpB0983(glgA)
            CCA: CCA00821(glgA)
            CAB: CAB790
            CFE: CF0193(glgA)
            PCU: pc1596(glgA)
            TDE: TDE1582(glgA)
            SYN: sll0945(glgA) sll1393(glgA)
            SYW: SYNW1000
            SYC: syc1589_d(glgA)
            SYF: Synpcc7942_2518
            SYD: Syncc9605_1126
            SYE: Syncc9902_1331
            SYG: sync_1529(glgA)
            SYR: SynRCC307_1144(glgA)
            SYX: SynWH7803_1026(glgA)
            CYA: CYA_2071(glgA-1) CYA_2648(glgA-2)
            CYB: CYB_0646(glgA-1) CYB_1734(glgA-2)
            TEL: tll0763(glgA)
            GVI: glr0932(glgA)
            ANA: alr0031 alr1879
            AVA: Ava_0090 Ava_1041 Ava_1122 Ava_1362 Ava_2631 Ava_3301
                 Ava_3411 Ava_4775 Ava_5045
            PMA: Pro1052(glgA)
            PMM: PMM0609
            PMT: PMT0403
            PMN: PMN2A_0045
            PMI: PMT9312_0609
            PMB: A9601_06651(glgA)
            PMC: P9515_06741(glgA)
            PMF: P9303_18831(glgA)
            PMG: P9301_06351(glgA)
            PMH: P9215_06911(glgA)
            PME: NATL1_06651(glgA)
            TER: Tery_2147
            SRU: SRU_0791
            CHU: CHU_1581(glgA) CHU_3836(glgA)
            GFO: GFO_2808(glgA)
            FJO: Fjoh_0824 Fjoh_2742
            CTE: CT2012(glgA)
            CCH: Cag_1808 Cag_1868
            CPH: Cpha266_2377
            PVI: Cvib_0286
            PLT: Plut_0168 Plut_0220
            RRS: RoseRS_1081
            RCA: Rcas_2787
            DRA: DR_0594
            DGE: Dgeo_1988
            TTH: TTC1980
            TTJ: TTHA0018
            AAE: aq_721(glgA)
            TMA: TM0895
            MJA: MJ1606(glgA)
            MMP: MMP1294(glgA)
            MMQ: MmarC5_0299
            MMZ: MmarC7_0539
            PAB: PAB2292
            PFU: PF2044
            TKO: TK1768
            SMR: Smar_1393
            SSO: SSO0987
            STO: ST0818
            SAI: Saci_1201
            MSE: Msed_1417
            PAI: PAE3429
            PIS: Pisl_0968
            PCL: Pcal_1038
            PAS: Pars_1878
            TPE: Tpen_0792
STRUCTURES  PDB: 1RZU  1RZV  2BFW  2BIS  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.21
            ExPASy - ENZYME nomenclature database: 2.4.1.21
            ExplorEnz - The Enzyme Database: 2.4.1.21
            ERGO genome analysis and discovery system: 2.4.1.21
            BRENDA, the Enzyme Database: 2.4.1.21
            CAS: 9030-10-8
///
ENTRY       EC 2.4.1.22                 Enzyme
NAME        lactose synthase;
            UDP-galactose---glucose galactosyltransferase;
            N-acetyllactosamine synthase;
            uridine diphosphogalactose-glucose galactosyltransferase;
            lactose synthetase;
            UDP-galactose:D-glucose 4-beta-D-galactotransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:D-glucose 4-beta-D-galactosyltransferase
REACTION    UDP-galactose + D-glucose = UDP + lactose [RN:R00503 R06067]
ALL_REAC    R00503 R06067(G)
SUBSTRATE   UDP-galactose [CPD:C00052];
            D-glucose [CPD:C00031]
PRODUCT     UDP [CPD:C00015];
            lactose [CPD:C00243]
COMMENT     The enzyme is a complex of two proteins, A and B. In the absence of
            the B protein (alpha-lactalbumin), the enzyme catalyses the transfer
            of galactose from UDP-galactose to N-acetylglucosamine (EC 2.4.1.90
            N-acetyllactosamine synthase).
REFERENCE   1  [PMID:5440844]
  AUTHORS   Fitzgerald DK, Brodbeck U, Kiyosawa I, Mawal R, Colvin B, Ebner KE.
  TITLE     Alpha-lactalbumin and the lactose synthetase reaction.
  JOURNAL   J. Biol. Chem. 245 (1970) 2103-8.
  ORGANISM  rat [GN:rno], guinea pig, cow [GN:bta]
REFERENCE   2  [PMID:812340]
  AUTHORS   Hill RL, Brew K.
  TITLE     Lactose synthetase.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 43 (1975) 411-90.
REFERENCE   3  [PMID:14005251]
  AUTHORS   WATKINS WM, HASSID WZ.
  TITLE     The synthesis of lactose by particulate enzyme preparations from
            guinea pig and bovine mammary glands.
  JOURNAL   J. Biol. Chem. 237 (1962) 1432-40.
  ORGANISM  guinea pig, cow [GN:bta]
PATHWAY     PATH: map00052  Galactose metabolism
ORTHOLOGY   KO: K00704  lactose synthase
GENES       HSA: 2683(B4GALT1) 3906(LALBA) 8704(B4GALT2)
            MMU: 14595(B4galt1) 16770(Lalba) 53418(B4galt2)
            RNO: 24390(B4galt1_predicted) 24528(Lalba)
                 313536(B4galt2_predicted)
            CFA: 403730(LALBA) 481579(B4GALT1) 482527(B4GALT2)
            BTA: 281781(B4GALT1) 281894(LALBA)
            SSC: 397647(LALBA)
            GGA: 396121(B4GALT1) 396122(B4GALT2)
            XTR: 549418(b4galt2)
STRUCTURES  PDB: 1A4V  1FKQ  1FKV  1HFX  1HFY  1HFZ  1HMK  1HML  1NF5  1NHE  
                 1NKH  1NMM  1NQI  1PZY  1TVY  1TW1  1TW5  1YRO  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.22
            ExPASy - ENZYME nomenclature database: 2.4.1.22
            ExplorEnz - The Enzyme Database: 2.4.1.22
            ERGO genome analysis and discovery system: 2.4.1.22
            BRENDA, the Enzyme Database: 2.4.1.22
            CAS: 9030-11-9
///
ENTRY       EC 2.4.1.23                 Enzyme
NAME        sphingosine beta-galactosyltransferase;
            psychosine---UDP galactosyltransferase;
            galactosyl-sphingosine transferase;
            psychosine-uridine diphosphate galactosyltransferase;
            UDP-galactose:sphingosine O-galactosyl transferase;
            uridine diphosphogalactose-sphingosine beta-galactosyltransferase;
            UDP-galactose:sphingosine 1-beta-galactotransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:sphingosine 1-beta-galactosyltransferase
REACTION    UDP-galactose + sphingosine = UDP + psychosine [RN:R01928]
ALL_REAC    R01928
SUBSTRATE   UDP-galactose [CPD:C00052];
            sphingosine [CPD:C00319]
PRODUCT     UDP [CPD:C00015];
            psychosine [CPD:C01747]
REFERENCE   1  [PMID:13810623]
  AUTHORS   CLELAND WW, KENNEDY EP.
  TITLE     The enzymatic synthesis of psychosine.
  JOURNAL   J. Biol. Chem. 235 (1960) 45-51.
  ORGANISM  guinea pig, rat [GN:rno]
PATHWAY     PATH: map00600  Sphingolipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.23
            ExPASy - ENZYME nomenclature database: 2.4.1.23
            ExplorEnz - The Enzyme Database: 2.4.1.23
            ERGO genome analysis and discovery system: 2.4.1.23
            BRENDA, the Enzyme Database: 2.4.1.23
            CAS: 9032-90-0
///
ENTRY       EC 2.4.1.24                 Enzyme
NAME        1,4-alpha-glucan 6-alpha-glucosyltransferase;
            oligoglucan-branching glycosyltransferase;
            1,4-alpha-D-glucan 6-alpha-D-glucosyltransferase;
            T-enzyme;
            D-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     1,4-alpha-D-glucan:1,4-alpha-D-glucan(D-glucose)
            6-alpha-D-glucosyltransferase
REACTION    Transfers an alpha-D-glucosyl residue in a 1,4-alpha-D-glucan to the
            primary hydroxy group of glucose, free or combined in a
            1,4-alpha-D-glucan
REFERENCE   1
  AUTHORS   Abdullah, M. and Whelan, W.J.
  TITLE     Synthesis of alpha-1:6-glucosidic linkages by a transglycosylase
            from potato.
  JOURNAL   Biochem. J. 75 (1960) 12P.
REFERENCE   2
  AUTHORS   Barker, S.A. and Carrington, T.R.
  TITLE     Studies of Aspergillus niger. Part II. Transglycosidation by
            Aspergillus niger.
  JOURNAL   J. Chem. Soc. (Lond.) (1953) 3588-3593.
  ORGANISM  Aspergillus niger
REFERENCE   3
  AUTHORS   Saroja, K., Venkataraman, R. and Giri, K.V.
  TITLE     Transglucosidation in Penicillium chrysogenum Q-176. Isolation and
            identification of the oligosaccharide.
  JOURNAL   Biochem. J. 60 (1955) 399-403.
  ORGANISM  Penicillium chrysogenum
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.24
            ExPASy - ENZYME nomenclature database: 2.4.1.24
            ExplorEnz - The Enzyme Database: 2.4.1.24
            ERGO genome analysis and discovery system: 2.4.1.24
            BRENDA, the Enzyme Database: 2.4.1.24
            CAS: 9030-12-0
///
ENTRY       EC 2.4.1.25                 Enzyme
NAME        4-alpha-glucanotransferase;
            disproportionating enzyme;
            dextrin glycosyltransferase;
            D-enzyme;
            debranching enzyme maltodextrin glycosyltransferase;
            amylomaltase;
            dextrin transglycosylase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase
REACTION    Transfers a segment of a 1,4-alpha-D-glucan to a new position in an
            acceptor, which may be glucose or a 1,4-alpha-D-glucan
ALL_REAC    (other) R05196 R06069(G)
COMMENT     This entry covers the former separate entry for EC 2.4.1.3
            (amylomaltase). The plant enzyme has been termed D-enzyme. An
            enzymic activity of this nature forms part of the mammalian and
            yeast glycogen debranching system (see EC 3.2.1.33
            amylo-alpha-1,6-glucosidase).
REFERENCE   1
  AUTHORS   Hehre, E.J.
  TITLE     Enzymic synthesis of polysaccharides: a biological type of
            polymerization.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297-337.
REFERENCE   2
  AUTHORS   Lukomskaya, I.S.
  TITLE     Synthesis of oligosaccharides with alpha-1,6-bonds by enzyme
            preparations from liver and muscle.
  JOURNAL   Dokl. Akad. Nauk S.S.S.R. 129 (1959) 1172-1175.
REFERENCE   3  [PMID:4972097]
  AUTHORS   Pazur JH, Okada S.
  TITLE     The isolation and mode of action of a bacterial
            glucanosyltransferase.
  JOURNAL   J. Biol. Chem. 243 (1968) 4732-8.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   4
  AUTHORS   Walker, G.J. and Whelan, W.J.
  TITLE     Synthesis of amylose by potato D-enzyme.
  JOURNAL   Nature 183 (1959) 46.
  ORGANISM  Solanum tuberosum [GN:estu]
REFERENCE   5
  AUTHORS   Whelan, W.H.
  TITLE     Enzymic explorations of the structures of starch and glycogen.
  JOURNAL   Biochem. J. 122 (1971) 609-622.
  ORGANISM  Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K00705  4-alpha-glucanotransferase
GENES       HSA: 178(AGL)
            PTR: 469392(AGL)
            MMU: 77559(Agl)
            GGA: 424474(AGL)
            CEL: R06A4.8
            ATH: AT2G40840(DPE2) AT5G64860(DPE1)
            OSA: 4343975 4344192
            CME: CMP352C CMT204C
            SCE: YPR184W(GDB1)
            AGO: AGOS_AEL276C
            PIC: PICST_74319(GDB1)
            CGR: CAGL0G09977g
            AFM: AFUA_1G02140
            AOR: AO090005000884
            CNE: CNJ03090
            UMA: UM03949.1
            DDI: DDBDRAFT_0185931 DDBDRAFT_0219237
            CPV: cgd6_880
            EHI: 1.t00098
            ECO: b3416(malQ)
            ECJ: JW3379(malQ)
            ECE: Z4771(malQ)
            ECS: ECs4258
            ECC: c4193(malQ)
            ECI: UTI89_C3917(malQ)
            ECP: ECP_3502
            ECW: EcE24377A_3892(malQ)
            ECX: EcHS_A3614
            STY: STY4283(malQ)
            STT: t3993(malQ)
            SPT: SPA3378(malQ)
            SEC: SC3445(malQ)
            STM: STM3513(malQ)
            YPE: YPO0126(malQ)
            YPK: y3902(malQ)
            YPM: YP_0127(malQ)
            YPA: YPA_3343
            YPN: YPN_3939
            YPP: YPDSF_0053
            YPS: YPTB3774(malQ)
            YPI: YpsIP31758_3992(malQ)
            SFL: SF3439(malQ)
            SFX: S4326(malQ)
            SFV: SFV_3424(malQ)
            SSN: SSON_3548(malQ)
            SBO: SBO_3405(malQ)
            SDY: SDY_3660(malQ)
            ECA: ECA4135(malQ)
            PLU: plu0469(malQ)
            ENT: Ent638_3829
            SPE: Spro_4635
            HIT: NTHI1810(malQ)
            HSO: HS_0890(malQ)
            PMU: PM0540(malQ)
            MSU: MS1124(malQ) MS2074(malQ)
            APL: APL_1240(malQ)
            ASU: Asuc_0312 Asuc_1351
            XCC: XCC0411(malQ)
            XCB: XC_0424
            XCV: XCV0454(malQ)
            XAC: XAC0428(malQ)
            XOO: XOO0115(malQ)
            XOM: XOO_0063(XOO0063)
            VCH: VCA0014
            VCO: VC0395_0118(malQ)
            VVU: VV2_1251
            VVY: VVA0078
            VPA: VPA1619
            VFI: VFA0809
            PPR: PBPRB1329
            PAE: PA2163
            PAU: PA14_36590(malQ)
            PAP: PSPA7_3143(malQ)
            PPU: PP_4052(malQ)
            PPF: Pput_1791
            PST: PSPTO_3127(malQ)
            PSB: Psyr_2994
            PSP: PSPPH_2246(malQ)
            PFL: PFL_2885(malQ)
            PFO: Pfl_2547
            PEN: PSEEN2052
            PMY: Pmen_2279
            SON: SO_1493(malQ)
            SFR: Sfri_2166
            SAZ: Sama_2454
            SBL: Sbal_1330
            SBM: Shew185_1320
            SLO: Shew_1167
            SPC: Sputcn32_1247
            SHE: Shewmr4_2759
            SHM: Shewmr7_2837
            SHN: Shewana3_2935
            SHW: Sputw3181_2857
            PAT: Patl_1635
            SDE: Sde_0986
            PIN: Ping_2365
            MAQ: Maqu_1431
            MCA: MCA1473(malQ)
            FTU: FTT0418(malQ)
            FTF: FTF0418(malA)
            FTW: FTW_1655(malQ)
            FTL: FTL_0488
            FTH: FTH_0486(malQ)
            FTA: FTA_0514(malQ)
            FTN: FTN_0518(malQ)
            TCX: Tcr_0510
            NOC: Noc_0906 Noc_1826
            AEH: Mlg_0961
            HHA: Hhal_1108
            AHA: AHA_3617(malQ)
            RSO: RS05187(RSp0236)
            REU: Reut_B4231
            REH: H16_B1561(malQ)
            BMA: BMA0817(malQ)
            BMV: BMASAVP1_A1335(malQ)
            BML: BMA10299_A0539(malQ)
            BMN: BMA10247_0616(malQ)
            BXE: Bxe_B2866
            BVI: Bcep1808_5809
            BUR: Bcep18194_C7029
            BCN: Bcen_1335
            BCH: Bcen2424_6494
            BAM: Bamb_5595
            BPS: BPSL2079
            BPM: BURPS1710b_1734(malQ)
            BPL: BURPS1106A_1563(malQ)
            BPD: BURPS668_1540(malQ)
            BPE: BP1324(malQ)
            BPA: BPP2897(malQ)
            BBR: BB2867(malQ)
            RFR: Rfer_0514
            PNA: Pnap_1102
            AAV: Aave_2985
            NET: Neut_1294
            NMU: Nmul_A1402
            TBD: Tbd_2059
            MFA: Mfla_1370
            NIS: NIS_0940
            SUN: SUN_1273
            GSU: GSU1182(malQ)
            GME: Gmet_2391
            GUR: Gura_3250
            PCA: Pcar_0554
            PPD: Ppro_1738 Ppro_3264
            DVU: DVU3148(malQ)
            DVL: Dvul_0237
            DDE: Dde_0510
            ADE: Adeh_0294 Adeh_3001
            AFW: Anae109_0318 Anae109_2966
            MXA: MXAN_6463(malQ)
            SAT: SYN_00881 SYN_01069
            SFU: Sfum_3452
            MES: Meso_2674
            PLA: Plav_0545
            RET: RHE_PF00262(malQ)
            RLE: pRL120723(malQ)
            BJA: bll6765
            BRA: BRADO5815
            BBT: BBta_6321
            RPA: RPA3641(malQ)
            RPB: RPB_1885
            RPC: RPC_3677 RPC_3778
            RPD: RPD_3481
            RPE: RPE_3644 RPE_3715
            NWI: Nwi_1210
            NHA: Nham_1467
            RSP: RSP_2451
            RSH: Rsph17029_1114
            RSQ: Rsph17025_1780
            RDE: RD1_2871(malQ)
            PDE: Pden_4424
            GBE: GbCGDNIH1_0748
            ACR: Acry_2938
            RRU: Rru_A1607
            MAG: amb3063
            ABA: Acid345_1486 Acid345_2764
            SUS: Acid_2892 Acid_5317
            LLA: L93919(ygjD) L94405(malQ)
            LLC: LACR_0723
            SPY: SPy_1292(malM)
            SPZ: M5005_Spy_1056(malM)
            SPM: spyM18_1312(malQ)
            SPG: SpyM3_0981(malQ)
            SPS: SPs0873
            SPH: MGAS10270_Spy1112(malM)
            SPI: MGAS10750_Spy1148(malM)
            SPJ: MGAS2096_Spy1058(malM) MGAS2096_Spy1059
            SPK: MGAS9429_Spy1102(malM)
            SPF: SpyM50804(malM)
            SPA: M6_Spy1030
            SPB: M28_Spy1037(malM)
            SPN: SP_2107
            SPR: spr1917(malM)
            SPD: SPD_1933(malQ)
            SAG: SAG1439(malQ)
            SAN: gbs1508
            SAK: SAK_1473(malQ)
            SMU: SMU.1565(malQ)
            STC: str1013(malQ)
            STL: stu1013(malQ)
            STE: STER_1017
            SSA: SSA_2266(malQ)
            SGO: SGO_0105(malQ)
            CPE: CPE2338(malQ)
            CPF: CPF_2647(malQ)
            CPR: CPR_2333(malQ)
            CNO: NT01CX_0969(malQ)
            CBE: Cbei_0233 Cbei_0864
            AMT: Amet_1677
            DRM: Dred_1459
            MTA: Moth_1850
            MTU: Rv1781c(malQ)
            MTC: MT1831(malQ)
            MBO: Mb1810c(malQ)
            MBB: BCG_1814c(malQ)
            MPA: MAP1500c
            MAV: MAV_2934(malQ)
            MSM: MSMEG_3673(malQ)
            MVA: Mvan_3175
            MGI: Mflv_0996 Mflv_3421
            MMC: Mmcs_2869
            MKM: Mkms_2913
            MJL: Mjls_2899
            CGL: NCgl2217(cgl2297)
            CGB: cg2523(malQ)
            CEF: CE2196
            CDI: DIP1726
            CJK: jk0596(malQ)
            RHA: RHA1_ro04830
            SCO: SCO2649(SC8E4A.19c)
            SMA: SAV5391(malQ)
            ART: Arth_2153
            PAC: PPA1683
            TFU: Tfu_2205
            FRA: Francci3_1157
            FAL: FRAAL1852(malQ)
            ACE: Acel_1601
            KRA: Krad_3529
            BLO: BL0527(malQ) BL1570(malQ1)
            BAD: BAD_0308(malQ1) BAD_1560(malQ)
            RXY: Rxyl_0251
            FNU: FN0858
            RBA: RB4161(malQ)
            CTR: CT087(malQ)
            CTA: CTA_0092(malQ)
            CMU: TC0362
            CPN: CPn0326(malQ)
            CPA: CP0431
            CPJ: CPj0326(malQ)
            CPT: CpB0336
            CCA: CCA00456(malQ)
            CAB: CAB442(malQ)
            CFE: CF0551(malQ)
            PCU: pc0745(malQ)
            BBU: BB0166
            BGA: BG0164(malQ)
            BAF: BAPKO_0167(malQ)
            TDE: TDE2387(malQ)
            SYN: sll1676(malQ)
            SYW: SYNW0962(malQ)
            SYC: syc0527_c
            SYF: Synpcc7942_1019
            SYD: Syncc9605_1614
            SYE: Syncc9902_1375
            SYG: sync_1015(malQ)
            SYR: SynRCC307_0775(malQ)
            SYX: SynWH7803_1549(malQ)
            CYA: CYA_2436(malQ)
            CYB: CYB_1490(malQ)
            TEL: tlr0708
            GVI: gll3316
            ANA: alr3871
            AVA: Ava_1822 Ava_2025
            PMA: Pro1116(malQ)
            PMM: PMM1081(malQ)
            PMT: PMT1071(malQ)
            PMN: PMN2A_0669
            PMI: PMT9312_1092
            PMB: A9601_11871(malQ)
            PMC: P9515_11711(malQ)
            PMF: P9303_09791(malQ)
            PMG: P9301_11881(malQ)
            PME: NATL1_15011(malQ)
            TER: Tery_1296
            BTH: BT_2146
            BFR: BF3828
            BFS: BF3620
            PGI: PG0767(malQ)
            SRU: SRU_0660(malQ)
            CHU: CHU_2290(malQ)
            RRS: RoseRS_1575 RoseRS_3111
            RCA: Rcas_2645 Rcas_2968
            DGE: Dgeo_0667
            TTH: TTC0897
            TTJ: TTHA1261
            AAE: aq_723(malM)
            TMA: TM0364
            MHU: Mhun_0552
            MEM: Memar_1054 Memar_1263
            HMA: rrnAC1957(malQ)
            HWA: HQ2578A(malQ)
            SMR: Smar_1392
            PAI: PAE1209(malQ)
            PIS: Pisl_1316
            PCL: Pcal_0768
            PAS: Pars_0206
STRUCTURES  PDB: 1CWY  1ESW  1FP8  1FP9  1K1W  1K1X  1K1Y  1LWH  1LWJ  1TZ7  
                 1X1N  2OWC  2OWW  2OWX  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.25
            ExPASy - ENZYME nomenclature database: 2.4.1.25
            ExplorEnz - The Enzyme Database: 2.4.1.25
            ERGO genome analysis and discovery system: 2.4.1.25
            BRENDA, the Enzyme Database: 2.4.1.25
            CAS: 9032-09-1
///
ENTRY       EC 2.4.1.26                 Enzyme
NAME        DNA alpha-glucosyltransferase;
            uridine diphosphoglucose-deoxyribonucleate
            alpha-glucosyltransferase;
            UDP-glucose-DNA alpha-glucosyltransferase;
            uridine diphosphoglucose-deoxyribonucleate
            alpha-glucosyltransferase;
            T2-HMC-alpha-glucosyl transferase;
            T4-HMC-alpha-glucosyl transferase;
            T6-HMC-alpha-glucosyl transferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:DNA alpha-D-glucosyltransferase
REACTION    Transfers an alpha-D-glucosyl residue from UDP-glucose to an
            hydroxymethylcytosine residue in DNA
REFERENCE   1
  AUTHORS   Kornberg, S.R., Zimmerman, S.B. and Kornberg, A.
  TITLE     Glucosylation of deoxyribonucleic acid by enzymes from
            bacteriophage-infected Escherichia coli.
  JOURNAL   J. Biol. Chem. 236 (1961) 1487-1493.
  ORGANISM  bacteriophage T2, bacteriophage T4, bacteriophage T6
STRUCTURES  PDB: 1XV5  1Y6F  1Y6G  1Y8Z  1YA6  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.26
            ExPASy - ENZYME nomenclature database: 2.4.1.26
            ExplorEnz - The Enzyme Database: 2.4.1.26
            ERGO genome analysis and discovery system: 2.4.1.26
            BRENDA, the Enzyme Database: 2.4.1.26
            CAS: 9030-13-1
///
ENTRY       EC 2.4.1.27                 Enzyme
NAME        DNA beta-glucosyltransferase;
            T4-HMC-beta-glucosyl transferase;
            T4-beta-glucosyl transferase;
            T4 phage beta-glucosyltransferase;
            UDP glucose-DNA beta-glucosyltransferase;
            uridine diphosphoglucose-deoxyribonucleate beta-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:DNA beta-D-glucosyltransferase
REACTION    Transfers a beta-D-glucosyl residue from UDP-glucose to an
            hydroxymethylcytosine residue in DNA
REFERENCE   1
  AUTHORS   Kornberg, S.R., Zimmerman, S.B. and Kornberg, A.
  TITLE     Glucosylation of deoxyribonucleic acid by enzymes from
            bacteriophage-infected Escherichia coli.
  JOURNAL   J. Biol. Chem. 236 (1961) 1487-1493.
  ORGANISM  bacteriophage T4
STRUCTURES  PDB: 1BGT  1BGU  1C3J  1IXY  1J39  1JEJ  1JG6  1JG7  1JIU  1JIV  
                 1JIX  1M5R  1NVK  1NZD  1NZF  1QKJ  1SXP  1SXQ  2BGT  2BGU  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.27
            ExPASy - ENZYME nomenclature database: 2.4.1.27
            ExplorEnz - The Enzyme Database: 2.4.1.27
            ERGO genome analysis and discovery system: 2.4.1.27
            BRENDA, the Enzyme Database: 2.4.1.27
            CAS: 9030-14-2
///
ENTRY       EC 2.4.1.28                 Enzyme
NAME        glucosyl-DNA beta-glucosyltransferase;
            T6-glucosyl-HMC-beta-glucosyl transferase;
            T6-beta-glucosyl transferase;
            uridine diphosphoglucose-glucosyldeoxyribonucleate
            beta-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:D-glucosyl-DNA beta-D-glucosyltransferase
REACTION    Transfers a beta-D-glucosyl residue from UDP-glucose to a
            glucosylhydroxymethylcytosine residue in DNA
REFERENCE   1
  AUTHORS   Kornberg, S.R., Zimmerman, S.B. and Kornberg, A.
  TITLE     Glucosylation of deoxyribonucleic acid by enzymes from
            bacteriophage-infected Escherichia coli.
  JOURNAL   J. Biol. Chem. 236 (1961) 1487-1493.
  ORGANISM  bacteriophage T6
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.28
            ExPASy - ENZYME nomenclature database: 2.4.1.28
            ExplorEnz - The Enzyme Database: 2.4.1.28
            ERGO genome analysis and discovery system: 2.4.1.28
            BRENDA, the Enzyme Database: 2.4.1.28
            CAS: 9030-15-3
///
ENTRY       EC 2.4.1.29                 Enzyme
NAME        cellulose synthase (GDP-forming);
            cellulose synthase (guanosine diphosphate-forming);
            cellulose synthetase;
            guanosine diphosphoglucose-1,4-beta-glucan glucosyltransferase;
            guanosine diphosphoglucose-cellulose glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-glucose:1,4-beta-D-glucan 4-beta-D-glucosyltransferase
REACTION    GDP-glucose + (1,4-beta-D-glucosyl)n = GDP +
            (1,4-beta-D-glucosyl)n+1 [RN:R02890 R06030]
ALL_REAC    R02890 R06030(G)
SUBSTRATE   GDP-glucose [CPD:C00394];
            (1,4-beta-D-glucosyl)n [CPD:C00760]
PRODUCT     GDP [CPD:C00035];
            (1,4-beta-D-glucosyl)n+1 [CPD:C00760]
COMMENT     Involved in the synthesis of cellulose. A similar enzyme [EC
            2.4.1.12, cellulose synthase (UDP-forming)] utilizes UDP-glucose.
REFERENCE   1  [PMID:4317490]
  AUTHORS   Chambers J, Elbein AD.
  TITLE     Biosynthesis of glucans in mung bean seedlings. Formation of
            beta-(1,4)-glucans from GDP-glucose and beta-(1,3)-glucans from
            UDP-glucose.
  JOURNAL   Arch. Biochem. Biophys. 138 (1970) 620-31.
  ORGANISM  Vigna radiata
REFERENCE   2  [PMID:5824571]
  AUTHORS   Flowers HM, Batra KK, Kemp J, Hassid WZ.
  TITLE     Biosynthesis of cellulose in vitro from guanosine diphosphate
            D-glucose with enzymic preparations from Phaseolus aureus and
            Lupinus albus.
  JOURNAL   J. Biol. Chem. 244 (1969) 4969-74.
  ORGANISM  Vigna radiata, Lupinus albus
PATHWAY     PATH: map00500  Starch and sucrose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.29
            ExPASy - ENZYME nomenclature database: 2.4.1.29
            ExplorEnz - The Enzyme Database: 2.4.1.29
            ERGO genome analysis and discovery system: 2.4.1.29
            BRENDA, the Enzyme Database: 2.4.1.29
            CAS: 9027-18-3
///
ENTRY       EC 2.4.1.30                 Enzyme
NAME        1,3-beta-oligoglucan phosphorylase;
            beta-1,3-oligoglucan:orthophosphate glucosyltransferase II;
            beta-1,3-oligoglucan phosphorylase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     1,3-beta-D-oligoglucan:phosphate alpha-D-glucosyltransferase
REACTION    (1,3-beta-D-glucosyl)n + phosphate = (1,3-beta-D-glucosyl)n-1 +
            alpha-D-glucose 1-phosphate [RN:R03116 R06018]
ALL_REAC    R03116 R06018(G)
SUBSTRATE   (1,3-beta-D-glucosyl)n [CPD:C00965];
            phosphate [CPD:C00009]
PRODUCT     (1,3-beta-D-glucosyl)n-1 [CPD:C00965];
            alpha-D-glucose 1-phosphate [CPD:C00103]
COMMENT     Does not act on laminarin. Differs in specificity from EC 2.4.1.31
            (laminaribiose phosphorylase) and EC 2.4.1.97 (1,3-beta-D-glucan
            phosphorylase).
REFERENCE   1  [PMID:6066291]
  AUTHORS   Marechal LR.
  TITLE     Beta-1,3-oligoglucan:orthophosphate glucosyltransferases from
            Euglena gracilis. I. Isolation and some properties of a
            beta-1,3-oligoglucan phosphorylase.
  JOURNAL   Biochim. Biophys. Acta. 146 (1967) 417-30.
  ORGANISM  Euglena gracilis
REFERENCE   2  [PMID:6066292]
  AUTHORS   Marechal LR.
  TITLE     Beta-1,3-oligoglucan: orthophosphate glucosyltransferases from
            Euglena gracilis. II. Comparative studies between laminaribiose- and
            beta-1,3-oligoglucan phosphorylase.
  JOURNAL   Biochim. Biophys. Acta. 146 (1967) 431-42.
  ORGANISM  Euglena gracilis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.30
            ExPASy - ENZYME nomenclature database: 2.4.1.30
            ExplorEnz - The Enzyme Database: 2.4.1.30
            ERGO genome analysis and discovery system: 2.4.1.30
            BRENDA, the Enzyme Database: 2.4.1.30
            CAS: 37257-28-6
///
ENTRY       EC 2.4.1.31                 Enzyme
NAME        laminaribiose phosphorylase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     3-beta-D-glucosyl-D-glucose:phosphate alpha-D-glucosyltransferase
REACTION    3-beta-D-glucosyl-D-glucose + phosphate = D-glucose +
            alpha-D-glucose 1-phosphate [RN:R00953 R06058]
ALL_REAC    R00953 R06058(G)
SUBSTRATE   3-beta-D-glucosyl-D-glucose [CPD:C02048];
            phosphate [CPD:C00009]
PRODUCT     D-glucose [CPD:C00031];
            alpha-D-glucose 1-phosphate [CPD:C00103]
COMMENT     Also acts on 1,3-beta-D-oligoglucans. Differs in specificity from EC
            2.4.1.30 (1,3-beta-oligoglucan phosphorylase) and EC 2.4.1.97
            (1,3-beta-D-glucan phosphorylase).
REFERENCE   1  [PMID:5901055]
  AUTHORS   Goldemberg SH, Marechal LR, De Souza BC.
  TITLE     Beta-1,3-oligoglucan: orthophosphate glucosyltransferase from
            Euglena gracilis.
  JOURNAL   J. Biol. Chem. 241 (1966) 45-50.
  ORGANISM  Euglena gracilis
REFERENCE   2  [PMID:6057111]
  AUTHORS   Manners DJ, Taylor DC.
  TITLE     Studies on carbohydrate metabolizing enzymes. XVI. Specificity of
            laminaribiose phosphorylase from Astasia ocellata.
  JOURNAL   Arch. Biochem. Biophys. 121 (1967) 443-51.
  ORGANISM  Astasia ocellata
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.31
            ExPASy - ENZYME nomenclature database: 2.4.1.31
            ExplorEnz - The Enzyme Database: 2.4.1.31
            ERGO genome analysis and discovery system: 2.4.1.31
            BRENDA, the Enzyme Database: 2.4.1.31
            CAS: 37257-29-7
///
ENTRY       EC 2.4.1.32                 Enzyme
NAME        glucomannan 4-beta-mannosyltransferase;
            GDP-man-beta-mannan manosyltransferase;
            glucomannan-synthase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDPmannose:glucomannan 1,4-beta-D-mannosyltransferase
REACTION    GDP-mannose + (glucomannan)n = GDP + (glucomannan)n+1 [RN:R03829]
ALL_REAC    R03829
SUBSTRATE   GDP-mannose [CPD:C00096];
            (glucomannan)n [CPD:C02101]
PRODUCT     GDP [CPD:C00035];
            (glucomannan)n+1 [CPD:C02101]
REFERENCE   1  [PMID:4304230]
  AUTHORS   Elbein AD.
  TITLE     Biosynthesis of a cell wall glucomannan in mung bean seedlings.
  JOURNAL   J. Biol. Chem. 244 (1969) 1608-16.
  ORGANISM  Vigna radiata
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.32
            ExPASy - ENZYME nomenclature database: 2.4.1.32
            ExplorEnz - The Enzyme Database: 2.4.1.32
            ERGO genome analysis and discovery system: 2.4.1.32
            BRENDA, the Enzyme Database: 2.4.1.32
            CAS: 37257-30-0
///
ENTRY       EC 2.4.1.33                 Enzyme
NAME        alginate synthase;
            mannuronosyl transferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-D-mannuronate:alginate D-mannuronyltransferase
REACTION    GDP-D-mannuronate + (alginate)n = GDP + (alginate)n+1 [RN:R03129]
ALL_REAC    R03129
SUBSTRATE   GDP-D-mannuronate [CPD:C00976];
            (alginate)n [CPD:C01768]
PRODUCT     GDP [CPD:C00035];
            (alginate)n+1 [CPD:C01768]
REFERENCE   1  [PMID:5954796]
  AUTHORS   Lin TY, Hassid WZ.
  TITLE     Pathway of algnic acid synthesis in the marine brown alga, Fucus
            gardneri Silva.
  JOURNAL   J. Biol. Chem. 241 (1966) 5284-97.
  ORGANISM  Fucus gardneri
PATHWAY     PATH: map00051  Fructose and mannose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.33
            ExPASy - ENZYME nomenclature database: 2.4.1.33
            ExplorEnz - The Enzyme Database: 2.4.1.33
            ERGO genome analysis and discovery system: 2.4.1.33
            BRENDA, the Enzyme Database: 2.4.1.33
            CAS: 37257-31-1
///
ENTRY       EC 2.4.1.34                 Enzyme
NAME        1,3-beta-glucan synthase;
            1,3-beta-D-glucan---UDP glucosyltransferase;
            UDP-glucose---1,3-beta-D-glucan glucosyltransferase;
            callose synthetase;
            1,3-beta-D-glucan-UDP glucosyltransferase;
            UDP-glucose-1,3-beta-D-glucan glucosyltransferase;
            paramylon synthetase;
            UDP-glucose-beta-glucan glucosyltransferase;
            GS-II;
            (1,3)-beta-glucan (callose) synthase;
            beta-1,3-glucan synthase;
            beta-1,3-glucan synthetase;
            1,3-beta-D-glucan synthetase;
            1,3-beta-D-glucan synthase;
            1,3-beta-glucan-uridine diphosphoglucosyltransferase;
            callose synthase;
            UDP-glucose-1,3-beta-glucan glucosyltransferase;
            UDP-glucose:(1,3)beta-glucan synthase;
            uridine diphosphoglucose-1,3-beta-glucan glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:1,3-beta-D-glucan 3-beta-D-glucosyltransferase
REACTION    UDP-glucose + (1,3-beta-D-glucosyl)n = UDP +
            (1,3-beta-D-glucosyl)n+1 [RN:R03118 R06020]
ALL_REAC    R03118 R06020(G)
SUBSTRATE   UDP-glucose [CPD:C00029];
            (1,3-beta-D-glucosyl)n [CPD:C00965]
PRODUCT     UDP [CPD:C00015];
            (1,3-beta-D-glucosyl)n+1 [CPD:C00965]
REFERENCE   1  [PMID:14245356]
  AUTHORS   MARECHAL LR, GOLDEMBERG SH.
  TITLE     URIDINE DIPHOSPHATE GLUCOSE-BETA-1,3-GLUCAN
            BETA-3-GLUCOSYLTRANSFERASE FROM EUGLENA GRACILIS.
  JOURNAL   J. Biol. Chem. 239 (1964) 3163-7.
  ORGANISM  Euglena gracilis
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K00706  1,3-beta-glucan synthase
GENES       SCE: YGR032W(GSC2) YLR342W(FKS1) YMR306W(FKS3)
            AGO: AGOS_AAR053W AGOS_ACL181C AGOS_AGL353W
            PIC: PICST_38184(FKS3) PICST_43247(SMI1.1) PICST_67249(GSL2)
                 PICST_86938(GSC2)
            CGR: CAGL0G01034g CAGL0K04037g CAGL0M13827g
            SPO: SPAC19B12.03 SPAC24C9.07c SPBC19G7.05c SPCC1840.02c
            ANI: AN3729.2
            AFM: AFUA_6G12400
            AOR: AO090009000174
            CNE: CNN02320
            UMA: UM01639.1
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.34
            ExPASy - ENZYME nomenclature database: 2.4.1.34
            ExplorEnz - The Enzyme Database: 2.4.1.34
            ERGO genome analysis and discovery system: 2.4.1.34
            BRENDA, the Enzyme Database: 2.4.1.34
            CAS: 9037-30-3
///
ENTRY       EC 2.4.1.35                 Enzyme
NAME        phenol beta-glucosyltransferase;
            UDPglucosyltransferase;
            phenol-beta-D-glucosyltransferase;
            UDP glucosyltransferase;
            UDP-glucose glucosyltransferase;
            uridine diphosphoglucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:phenol beta-D-glucosyltransferase
REACTION    UDP-glucose + a phenol = UDP + an aryl beta-D-glucoside
ALL_REAC    (other) R01240 R03526
SUBSTRATE   UDP-glucose [CPD:C00029];
            phenol [CPD:C00146]
PRODUCT     UDP [CPD:C00015];
            aryl beta-D-glucoside [CPD:C03097]
COMMENT     Acts on a wide range of phenols.
REFERENCE   1  [PMID:5961845]
  AUTHORS   Dutton GJ.
  TITLE     Uridine diphosphate glucose and the synthesis of phenolic glucosides
            by mollusks.
  JOURNAL   Arch. Biochem. Biophys. 116 (1966) 399-405.
  ORGANISM  Arion ater, Helix pomatia
PATHWAY     PATH: map00500  Starch and sucrose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.35
            ExPASy - ENZYME nomenclature database: 2.4.1.35
            ExplorEnz - The Enzyme Database: 2.4.1.35
            ERGO genome analysis and discovery system: 2.4.1.35
            BRENDA, the Enzyme Database: 2.4.1.35
            CAS: 9046-69-9
///
ENTRY       EC 2.4.1.36                 Enzyme
NAME        alpha,alpha-trehalose-phosphate synthase (GDP-forming);
            GDP-glucose---glucose-phosphate glucosyltransferase;
            guanosine diphosphoglucose-glucose phosphate glucosyltransferase;
            trehalose phosphate synthase (GDP-forming)
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-glucose:D-glucose-6-phosphate 1-alpha-D-glucosyltransferase
REACTION    GDP-glucose + glucose 6-phosphate = GDP + alpha,alpha-trehalose
            6-phosphate [RN:R02168 R06125]
ALL_REAC    R02168 R06125(G)
SUBSTRATE   GDP-glucose [CPD:C00394];
            glucose 6-phosphate [CPD:C00092]
PRODUCT     GDP [CPD:C00035];
            alpha,alpha'-trehalose 6-phosphate [CPD:C00689]
COMMENT     See also EC 2.4.1.15 [alpha,alpha-trehalose-phosphate synthase
            (UDP-forming)].
REFERENCE   1  [PMID:6022837]
  AUTHORS   Elbein AD.
  TITLE     Carbohydrate metabolism in Streptomyces hygroscopicus. I. Enzymatic
            synthesis of trehalose phosphate from guanosine diphosphate
            D-glucose-14C.
  JOURNAL   J. Biol. Chem. 242 (1967) 403-6.
  ORGANISM  Streptomyces hygroscopicus
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.36
            ExPASy - ENZYME nomenclature database: 2.4.1.36
            ExplorEnz - The Enzyme Database: 2.4.1.36
            ERGO genome analysis and discovery system: 2.4.1.36
            BRENDA, the Enzyme Database: 2.4.1.36
            CAS: 37257-32-2
///
ENTRY       EC 2.4.1.37                 Enzyme
NAME        fucosylgalactoside 3-alpha-galactosyltransferase;
            UDP-galactose:O-alpha-L-fucosyl(1->2)D-galactose
            alpha-D-galactosyltransferase;
            UDPgalactose:glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose
            3-alpha-D-galactosyltransferase;
            [blood group substance] alpha-galactosyltransferase;
            blood-group substance B-dependent galactosyltransferase;
            glycoprotein-fucosylgalactoside alpha-galactosyltransferase;
            histo-blood group B transferase;
            histo-blood substance B-dependent galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:alpha-L-fucosyl-(1->2)-D-galactoside
            3-alpha-D-galactosyltransferase
REACTION    UDP-galactose + alpha-L-fucosyl-(1->2)-D-galactosyl-R = UDP +
            alpha-D-galactosyl-(1->3)-[alpha-L-fucosyl(1->2)]-D-galactosyl-R
            [RN:R04548]
ALL_REAC    R04548 > R06029(G) R06168(G) R06190(G)
SUBSTRATE   UDP-galactose [CPD:C00052];
            alpha-L-fucosyl-(1->2)-D-galactosyl-R [CPD:C04648]
PRODUCT     UDP [CPD:C00015];
            alpha-D-galactosyl-(1->3)-[alpha-L-fucosyl(1->2)]-D-galactosyl-R
            [CPD:C04866]
COMMENT     Acts on blood group substance, and can use a number of
            2-fucosyl-galactosides as acceptors.
REFERENCE   1
  AUTHORS   Race, C., Ziderman, D. and Watkins, W.M.
  TITLE     An alpha-D-galactosyltransferase associated with the blood-group B
            character.
  JOURNAL   Biochem. J. 107 (1968) 733-735.
  ORGANISM  human [GN:hsa], baboon
PATHWAY     PATH: map00601  Glycosphingolipid biosynthesis - lactoseries
            PATH: map00602  Glycosphingolipid biosynthesis - neo-lactoseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K00707  fucosylglycoprotein 3-alpha-galactosyltransferase
GENES       HSA: 28(ABO)
            PTR: 450164(ABO)
            MMU: 80908(Abo)
            RNO: 65270(Abo)
            CFA: 491265(ABO)
            SSC: 396713(A)
STRUCTURES  PDB: 1R7U  1R7X  1R80  1R82  2A8W  2PGV  2PGY  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.37
            ExPASy - ENZYME nomenclature database: 2.4.1.37
            ExplorEnz - The Enzyme Database: 2.4.1.37
            ERGO genome analysis and discovery system: 2.4.1.37
            BRENDA, the Enzyme Database: 2.4.1.37
            CAS: 37257-33-3
///
ENTRY       EC 2.4.1.38                 Enzyme
NAME        beta-N-acetylglucosaminylglycopeptide
            beta-1,4-galactosyltransferase;
            UDP-galactose---glycoprotein galactosyltransferase;
            glycoprotein 4-beta-galactosyl-transferase;
            beta-N-acetyl-beta1-4-galactosyltransferase;
            thyroid glycoprotein beta-galactosyltransferase;
            glycoprotein beta-galactosyltransferase;
            thyroid galactosyltransferase;
            uridine diphosphogalactose-glycoprotein galactosyltransferase;
            beta-N-acetylglucosaminyl-glycopeptide
            beta-1,4-galactosyltransferase;
            GalT
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:N-acetyl-beta-D-glucosaminylglycopeptide
            beta-1,4-galactosyltransferase
REACTION    UDP-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP +
            beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminylglycopeptide
            [RN:R04495]
ALL_REAC    R04495 > R05989(G)
SUBSTRATE   UDP-galactose [CPD:C00052];
            N-acetyl-beta-D-glucosaminylglycopeptide
PRODUCT     UDP [CPD:C00015];
            beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminylglycopeptide
            [CPD:C04818]
COMMENT     Terminal N-acetyl-beta-D-glucosaminyl residues in polysaccharides,
            glycoproteins and glycopeptides can act as acceptor. High activity
            is shown towards such residues in branched-chain polysaccharides
            when these are linked by beta-1,6-links to galactose residues; lower
            activity towards residues linked to galactose by beta-1,3-links. A
            component of EC 2.4.1.22 (lactose synthase).
REFERENCE   1  [PMID:6784450]
  AUTHORS   Beyer TA, Sadler JE, Rearick JI, Paulson JC, Hill RL.
  TITLE     Glycosyltransferases and their use in assessing oligosaccharide
            structure and structure-function relationships.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 52 (1981) 23-175.
REFERENCE   2  [PMID:6816588]
  AUTHORS   Blanken WM, Hooghwinkel GJ, Van Den Eijnden DH.
  TITLE     Biosynthesis of blood-group I and i substances. Specificity of
            bovine colostrum beta-N-acetyl-D-glucosaminide beta 1 leads to 4
            galactosyltransferase.
  JOURNAL   Eur. J. Biochem. 127 (1982) 547-52.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:3932335]
  AUTHORS   Blanken WM, Van den Eijnden DH.
  TITLE     Biosynthesis of terminal Gal alpha 1----3Gal beta 1----4GlcNAc-R
            oligosaccharide sequences on glycoconjugates. Purification and
            acceptor specificity of a UDP-Gal:N-acetyllactosaminide alpha
            1----3-galactosyltransferase from calf thymus.
  JOURNAL   J. Biol. Chem. 260 (1985) 12927-34.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:5726898]
  AUTHORS   Spiro MJ, Spiro RG.
  TITLE     Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid
            galactosyltransferase.
  JOURNAL   J. Biol. Chem. 243 (1968) 6529-37.
  ORGANISM  cow [GN:bta], human [GN:hsa]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map00533  Keratan sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00708  beta-N-acetylglucosaminylglycopeptide
                        beta-1,4-galactosyltransferase
GENES       HSA: 2683(B4GALT1) 8703(B4GALT3) 8704(B4GALT2)
            PTR: 457451(B4GALT3)
            MMU: 14595(B4galt1) 53418(B4galt2) 57370(B4galt3)
            RNO: 24390(B4galt1_predicted) 313536(B4galt2_predicted)
                 494342(B4galt3)
            CFA: 481579(B4GALT1) 482527(B4GALT2) 488650(B4GALT3)
            BTA: 281781(B4GALT1) 515771(B4GALT3)
            GGA: 396121(B4GALT1) 396122(B4GALT2) 418342(B4GALT3)
            XLA: 379106(MGC52827)
            XTR: 448369(b4galt3) 549418(b4galt2)
            DRE: 561756(LOC561756)
STRUCTURES  PDB: 1FGX  1FR8  1NF5  1NHE  1NKH  1NMM  1NQI  1OQM  1PZY  1TVY  
                 1TW1  1TW5  1YRO  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.38
            ExPASy - ENZYME nomenclature database: 2.4.1.38
            ExplorEnz - The Enzyme Database: 2.4.1.38
            ERGO genome analysis and discovery system: 2.4.1.38
            BRENDA, the Enzyme Database: 2.4.1.38
            CAS: 37237-43-7
///
ENTRY       EC 2.4.1.39                 Enzyme
NAME        steroid N-acetylglucosaminyltransferase;
            hydroxy steroid acetylglucosaminyltransferase;
            steroid acetylglucosaminyltransferase;
            uridine diphosphoacetylglucosamine-steroid
            acetylglucosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:estradiol-17alpha-3-D-glucuronoside
            17alpha-N-acetylglucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine + estradiol-17alpha 3-D-glucuronoside =
            UDP + 17alpha-(N-acetyl-D-glucosaminyl)-estradiol 3-D-glucuronoside
            [RN:R04451]
ALL_REAC    R04451
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            estradiol-17alpha 3-D-glucuronoside [CPD:C04300]
PRODUCT     UDP [CPD:C00015];
            17alpha-(N-acetyl-D-glucosaminyl)-estradiol 3-D-glucuronoside
            [CPD:C04806]
REFERENCE   1  [PMID:5660254]
  AUTHORS   Collins DC, Jirku H, Layne DS.
  TITLE     Steroid N-acetylglucosaminyl transferase. Localization and some
            properties of the enzyme in rabbit tissues.
  JOURNAL   J. Biol. Chem. 243 (1968) 2928-33.
  ORGANISM  rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.39
            ExPASy - ENZYME nomenclature database: 2.4.1.39
            ExplorEnz - The Enzyme Database: 2.4.1.39
            ERGO genome analysis and discovery system: 2.4.1.39
            BRENDA, the Enzyme Database: 2.4.1.39
            CAS: 9033-56-1
///
ENTRY       EC 2.4.1.40                 Enzyme
NAME        glycoprotein-fucosylgalactoside
            alpha-N-acetylgalactosaminyltransferase;
            A-transferase;
            histo-blood group A glycosyltransferase
            (Fucalpha1->2Galalpha1->3-N-acetylgalactosaminyltransferase);
            UDP-GalNAc:Fucalpha1->2Galalpha1->3-N-
            acetylgalactosaminyltransferase;
            alpha-3-N-acetylgalactosaminyltransferase;
            blood-group substance alpha-acetyltransferase;
            blood-group substance A-dependent acetylgalactosaminyltransferase;
            fucosylgalactose acetylgalactosaminyltransferase;
            histo-blood group A acetylgalactosaminyltransferase;
            histo-blood group A transferase;
            UDP-N-acetyl-D-galactosamine:alpha-L-fucosyl-1,2-D-galactose
            3-N-acetyl-D-galactosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-galactosamine:glycoprotein-alpha-L-fucosyl-(1,2)-D-ga
            lactose 3-N-acetyl-D-galactosaminyltransferase
REACTION    UDP-N-acetyl-D-galactosamine +
            glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose = UDP +
            glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1,3)-[alpha-L-fucosyl-
            (1,2)]-D-galactose [RN:R04423]
ALL_REAC    R04423;
            (other) R06167(G) R06187(G) R06191(G) R06193(G) R06197(G)
SUBSTRATE   UDP-N-acetyl-D-galactosamine [CPD:C00203];
            glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose
PRODUCT     UDP [CPD:C00015];
            glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1,3)-[alpha-L-fucosyl-
            (1,2)]-D-galactose [CPD:C06483]
COMMENT     Acts on blood group substance, and can use a number of
            2-fucosyl-galactosides as acceptors.
REFERENCE   1  [PMID:5661629]
  AUTHORS   Kobata A, Grollman EF, Ginsburg V.
  TITLE     An enzymic basis for blood type A in humans.
  JOURNAL   Arch. Biochem. Biophys. 124 (1968) 609-12.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:2341371]
  AUTHORS   Takeya A, Hosomi O, Ishiura M.
  TITLE     Complete purification and characterization of
            alpha-3-N-acetylgalactosaminyltransferase encoded by the human blood
            group A gene.
  JOURNAL   J. Biochem. (Tokyo). 107 (1990) 360-8.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:6434182]
  AUTHORS   Yates AD, Feeney J, Donald AS, Watkins WM.
  TITLE     Characterisation of a blood-group A-active tetrasaccharide
            synthesised by a blood-group B gene-specified glycosyltransferase.
  JOURNAL   Carbohydr. Res. 130 (1984) 251-60.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00601  Glycosphingolipid biosynthesis - lactoseries
            PATH: map00602  Glycosphingolipid biosynthesis - neo-lactoseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K00709  fucosylglycoprotein
                        alpha-N-acetylgalactosaminyltransferase
GENES       HSA: 28(ABO)
            PTR: 450164(ABO)
            MMU: 80908(Abo)
            RNO: 65270(Abo)
            CFA: 491265(ABO)
            SSC: 396713(A)
STRUCTURES  PDB: 1LZ0  1LZI  1R7T  1R7V  1R7Y  1R81  1WSZ  1WT0  1WT1  1WT2  
                 1WT3  1XZ6  1ZHJ  1ZI1  1ZI3  1ZI4  1ZI5  1ZJO  2A8W  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.40
            ExPASy - ENZYME nomenclature database: 2.4.1.40
            ExplorEnz - The Enzyme Database: 2.4.1.40
            ERGO genome analysis and discovery system: 2.4.1.40
            BRENDA, the Enzyme Database: 2.4.1.40
            CAS: 9067-69-0
///
ENTRY       EC 2.4.1.41                 Enzyme
NAME        polypeptide N-acetylgalactosaminyltransferase;
            protein-UDP acetylgalactosaminyltransferase;
            UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase;
            UDP-N-acetylgalactosamine:kappa-casein polypeptide
            N-acetylgalactosaminyltransferase;
            uridine diphosphoacetylgalactosamine-glycoprotein
            acetylgalactosaminyltransferase;
            glycoprotein acetylgalactosaminyltransferase;
            polypeptide-N-acetylgalactosamine transferase;
            UDP-acetylgalactosamine-glycoprotein
            acetylgalactosaminyltransferase;
            UDP-acetylgalactosamine:peptide-N-galactosaminyltransferase;
            UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase;
            UDP-N-acetyl-alpha-D-galactosamine:polypeptide
            N-acetylgalactosaminyltransferase;
            UDP-N-acetylgalactosamine-glycoprotein
            N-acetylgalactosaminyltransferase;
            UDP-N-acetylgalactosamine-protein N-acetylgalactosaminyltransferase;
            UDP-N-acetylgalactosamine:polypeptide
            N-acetylgalactosaminyltransferase;
            UDP-N-acetylgalactosamine:protein N-acetylgalactosaminyl transferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-galactosamine:polypeptide
            N-acetylgalactosaminyl-transferase
REACTION    UDP-N-acetyl-D-galactosamine + polypeptide = UDP +
            N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
ALL_REAC    R02183 > R05907(G)
SUBSTRATE   UDP-N-acetyl-D-galactosamine [CPD:C00203];
            polypeptide [CPD:C00403]
PRODUCT     UDP [CPD:C00015];
            N-acetyl-D-galactosaminyl-polypeptide [CPD:C04387]
COFACTOR    Manganese [CPD:C00034];
            Calcium [CPD:C00076]
COMMENT     Requires both Mn2+ and Ca2+. The glycosyl residue is transferred to
            threonine or serine hydroxy groups on the polypeptide core of
            submaxillary mucin, kappa-casein, apofetuin and some other acceptors
            of high molecular mass.
REFERENCE   1  [PMID:6809738]
  AUTHORS   Sugiura M, Kawasaki T, Yamashina I.
  TITLE     Purification and characterization of UDP-GalNAc:polypeptide
            N-acetylgalactosamine transferase from an ascites hepatoma, AH 66.
  JOURNAL   J. Biol. Chem. 257 (1982) 9501-7.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   Takeuchi, M., Yoshikawa, M., Sasaki, R. and Chiba, H.
  TITLE     Purification and characterization of
            UDP-N-acetylgalactosamine-kappa-casein polypeptide
            N-acetylgalactosaminyltransferase from mammary-gland of lactating
            cow.
  JOURNAL   Agric. Biol. Chem. 49 (1985) 1059-1069.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00512  O-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00710  polypeptide N-acetylgalactosaminyltransferase
            KO: K09667  polypeptide N-acetylglucosaminyltransferase
GENES       HSA: 11226(GALNT6) 11227(GALNT5) 114805(GALNT13) 117248(GALNTL2)
                 168391(GALNTL5) 2589(GALNT1) 2590(GALNT2) 2591(GALNT3)
                 26290(GALNT8) 374378(GALNTL4) 442117(GALNT17) 50614(GALNT9)
                 51809(GALNT7) 55568(GALNT10) 57452(GALNTL1) 63917(GALNT11)
                 64409(WBSCR17) 79623(GALNT14) 79695(GALNT12) 8473(OGT)
                 8693(GALNT4)
            PTR: 451904(GALNT6) 463459(LOC463459) 463877(GALNT11) 465702(OGT)
                 467488(GALNTL1) 468521(GALNT1) 470563(GALNT5)
                 471350(LOC471350)
            MMU: 108148(Galnt2) 108150(Galnt7) 108155(Ogt) 108760(Galntl1)
                 14423(Galnt1) 14425(Galnt3) 14426(Galnt4) 171212(Galnt10)
                 207839(Galnt6) 212996(Wbscr17) 230145(Galnt12) 231050(Galnt11)
                 233733(Galntl4) 241391(Galnt5) 271786(Galnt13) 67909(Galntl5)
                 71685(Galnt14) 78754(Galntl2)
            RNO: 170501(Galnt10) 26295(Ogt) 311039(Galnt13) 313878(Galnt14)
                 366061(Galnt3) 499968(Galntl5) 683264(LOC683264) 79214(Galnt1)
            CFA: 474777(GALNT12) 477056(GALNTL2) 478753(GALNT13)
                 480161(GALNT1) 480370(GALNTL1) 480955(OGT) 482809(GALNT11)
                 483025(GALNT14) 485390(GALNTL4) 488359(LOC488359)
                 489165(GALNT10) 489790(LOC489790) 607787(GALNT6)
                 611040(GALNTL5)
            BTA: 282241(GALNT1) 532053(OGT) 617031(LOC617031)
            SSC: 664652(OGT)
            GGA: 416260(GALNT10) 417480(LOC417480) 420436(GALNT11)
                 420642(GALNTL2) 420955(GALNT1) 421305(GALNT14) 421540(GALNT2)
                 422203(OGT) 422560(GALNT17) 422561(GALNT7) 423034(GALNTL4)
                 423263(GALNTL1) 424177(GALNT3) 424319(GALNT13) 424324(GALNT5)
                 429501(RCJMB04_1b1)
            XLA: 398911(MGC68664) 431894(MGC78803) 432105(MGC81150)
                 444557(MGC83963) 447314(MGC81846) 447694(ogt)
            XTR: 407859(galnt7) 448751(galnt11) 553157(ogt)
            DRE: 337685(ogt) 406477(zgc:77836)
            SPU: 574835(LOC574835) 579289(LOC579289) 579469(LOC579469)
            DME: Dmel_CG10392(Ogt) Dmel_CG2103(pgant6) Dmel_CG30463
                 Dmel_CG31651(pgant5) Dmel_CG31956(pgant4) Dmel_CG3254(pgant2)
                 Dmel_CG4445(pgant3) Dmel_CG6394(GalNAc-T2) Dmel_CG7297(pgant8)
                 Dmel_CG7480(Pgant35A) Dmel_CG8182
            CEL: K04G7.3(ogt-1) Y116F11B.12(gly-4) Y39E4B.12(gly-5)
                 Y45F10D.3(gly-10) Y46H3A.6(N-acetylgalactosaminyltransferase)
                 ZK688.8(UDP-GalNAc)
STRUCTURES  PDB: 1XHB  2D7I  2D7R  2FFU  2FFV  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.41
            ExPASy - ENZYME nomenclature database: 2.4.1.41
            ExplorEnz - The Enzyme Database: 2.4.1.41
            ERGO genome analysis and discovery system: 2.4.1.41
            BRENDA, the Enzyme Database: 2.4.1.41
            CAS: 9075-15-4
///
ENTRY       EC 2.4.1.42       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: UDP-glucuronate-estriol
            17beta-D-glucuronosyltransferase. Now included with EC 2.4.1.17,
            glucuronosyltransferase (EC 2.4.1.42 created 1972, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.42
            ExPASy - ENZYME nomenclature database: 2.4.1.42
            ExplorEnz - The Enzyme Database: 2.4.1.42
            ERGO genome analysis and discovery system: 2.4.1.42
            BRENDA, the Enzyme Database: 2.4.1.42
///
ENTRY       EC 2.4.1.43                 Enzyme
NAME        polygalacturonate 4-alpha-galacturonosyltransferase;
            UDP galacturonate-polygalacturonate alpha-galacturonosyltransferase;
            uridine diphosphogalacturonate-polygalacturonate
            alpha-galacturonosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-D-galacturonate:1,4-alpha-poly-D-galacturonate
            4-alpha-D-galacturonosyltransferase
REACTION    UDP-D-galacturonate + (1,4-alpha-D-galacturonosyl)n = UDP +
            (1,4-alpha-D-galacturonosyl)n+1 [RN:R04343 R06072]
ALL_REAC    R04343 R06072(G);
            (other) R05191 R06278(G)
SUBSTRATE   UDP-D-galacturonate [CPD:C00617];
            (1,4-alpha-D-galacturonosyl)n [CPD:C03909]
PRODUCT     UDP [CPD:C00015];
            (1,4-alpha-D-galacturonosyl)n+1 [CPD:C03909]
REFERENCE   1  [PMID:5961848]
  AUTHORS   Villemez CL, Swanson AL, Hassid WZ.
  TITLE     Properties of a polygalacturonic acid-synthesizing enzyme system
            from Phaseolus aureus seedlings.
  JOURNAL   Arch. Biochem. Biophys. 116 (1966) 446-52.
  ORGANISM  Phaseolus aureus
PATHWAY     PATH: map00500  Starch and sucrose metabolism
            PATH: map00520  Nucleotide sugars metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.43
            ExPASy - ENZYME nomenclature database: 2.4.1.43
            ExplorEnz - The Enzyme Database: 2.4.1.43
            ERGO genome analysis and discovery system: 2.4.1.43
            BRENDA, the Enzyme Database: 2.4.1.43
            CAS: 37277-53-5
///
ENTRY       EC 2.4.1.44                 Enzyme
NAME        lipopolysaccharide 3-alpha-galactosyltransferase;
            UDP-galactose:lipopolysaccharide alpha,3-galactosyltransferase;
            UDP-galactose:polysaccharide galactosyltransferase;
            uridine diphosphate galactose:lipopolysaccharide
            alpha-3-galactosyltransferase;
            uridine diphosphogalactose-lipopolysaccharide
            alpha,3-galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:lipopolysaccharide 3-alpha-D-galactosyltransferase
REACTION    UDP-galactose + lipopolysaccharide = UDP +
            3-alpha-D-galactosyl-[lipopolysaccharide glucose] [RN:R01997]
ALL_REAC    R01997
SUBSTRATE   UDP-galactose [CPD:C00052];
            lipopolysaccharide [CPD:C00338]
PRODUCT     UDP [CPD:C00015];
            3-alpha-D-galactosyl-[lipopolysaccharide glucose] [CPD:C04473]
COMMENT     Transfers D-galactosyl residues to D-glucose in the partially
            completed core of lipopolysaccharide [cf. EC 2.4.1.56
            (lipopolysaccharide N-acetylglucosaminyltransferase), EC 2.4.1.58
            (lipopolysaccharide glucosyltransferase I) and EC 2.4.1.73
            (lipopolysaccharide glucosyltransferase II)].
REFERENCE   1  [PMID:4898284]
  AUTHORS   Endo A, Rothfield L.
  TITLE     Studies of a phospholipid-requiring bacterial enzyme. I.
            Purification and properties of uridine diphosphate galactose:
            lipopolysaccharide alpha-3-galactosyl transferase.
  JOURNAL   Biochemistry. 8 (1969) 3500-7.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:6403519]
  AUTHORS   Wollin R, Creeger ES, Rothfield LI, Stocker BA, Lindberg AA.
  TITLE     Salmonella typhimurium mutants defective in
            UDP-D-galactose:lipopolysaccharide alpha
            1,6-D-galactosyltransferase. Structural, immunochemical, and
            enzymologic studies of rfaB mutants.
  JOURNAL   J. Biol. Chem. 258 (1983) 3769-74.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00540  Lipopolysaccharide biosynthesis
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K03278  galactosyltransferase
            KO: K05943  
GENES       ECC: c4453(rfaI)
            ECI: UTI89_C4172(rafI)
            ECV: APECO1_2829(rafI)
            ECW: EcE24377A_4130(rfaI)
            ECX: EcHS_A3838(rfaI)
            STY: STY4077(rfaI)
            STT: t3801(waaI)
            SPT: SPA3570(waaI)
            SEC: SC3641(rfaI)
            STM: STM3718(rfaI)
            SSN: SSON_3778(waaI)
            SBO: SBO_3631(waaI)
            SDY: SDY_4059(rfaI)
            ECA: ECA0158(waaI)
STRUCTURES  PDB: 1GA8  1SS9  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.44
            ExPASy - ENZYME nomenclature database: 2.4.1.44
            ExplorEnz - The Enzyme Database: 2.4.1.44
            ERGO genome analysis and discovery system: 2.4.1.44
            BRENDA, the Enzyme Database: 2.4.1.44
            CAS: 9073-98-7
///
ENTRY       EC 2.4.1.45                 Enzyme
NAME        2-hydroxyacylsphingosine 1-beta-galactosyltransferase;
            uridine diphosphogalactose-2-hydroxyacylsphingosine
            galactosyltransferase;
            UDPgalactose-2-hydroxyacylsphingosine galactosyltransferase;
            UDP-galactose:ceramide galactosyltransferase;
            UDP-galactose:2-2-hydroxyacylsphingosine galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:2-(2-hydroxyacyl)sphingosine
            1-beta-D-galactosyl-transferase
REACTION    UDP-galactose + 2-(2-hydroxyacyl)sphingosine = UDP +
            1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine [RN:R04322]
ALL_REAC    R04322
SUBSTRATE   UDP-galactose [CPD:C00052];
            2-(2-hydroxyacyl)sphingosine [CPD:C03823]
PRODUCT     UDP [CPD:C00015];
            1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine [CPD:C04708]
COMMENT     Highly specific.
REFERENCE   1  [PMID:5090043]
  AUTHORS   Basu S, Schultz AM, Basu M, Roseman S.
  TITLE     Enzymatic synthesis of galactocerebroside by a galactosyltransferase
            from embryonic chicken brain.
  JOURNAL   J. Biol. Chem. 246 (1971) 4272-9.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:5793706]
  AUTHORS   Morell P, Radin NS.
  TITLE     Synthesis of cerebroside by brain from uridine diphosphate galactose
            and ceramide containing hydroxy fatty acid.
  JOURNAL   Biochemistry. 8 (1969) 506-12.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K00711  2-hydroxyacylsphingosine 1-beta-galactosyltransferase
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.45
            ExPASy - ENZYME nomenclature database: 2.4.1.45
            ExplorEnz - The Enzyme Database: 2.4.1.45
            ERGO genome analysis and discovery system: 2.4.1.45
            BRENDA, the Enzyme Database: 2.4.1.45
            CAS: 37277-54-6
///
ENTRY       EC 2.4.1.46                 Enzyme
NAME        monogalactosyldiacylglycerol synthase;
            uridine diphosphogalactose-1,2-diacylglycerol galactosyltransferase;
            UDP-galactose:diacylglycerol galactosyltransferase;
            MGDG synthase;
            UDP galactose-1,2-diacylglycerol galactosyltransferase;
            UDP-galactose-diacylglyceride galactosyltransferase;
            UDP-galactose:1,2-diacylglycerol 3-beta-D-galactosyltransferase;
            1beta-MGDG;
            1,2-diacylglycerol 3-beta-galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:1,2-diacyl-sn-glycerol 3-beta-D-galactosyltransferase
REACTION    UDP-galactose + 1,2-diacyl-sn-glycerol = UDP +
            3-beta-D-galactosyl-1,2-diacyl-sn-glycerol [RN:R02691]
ALL_REAC    R02691
SUBSTRATE   UDP-galactose [CPD:C00052];
            1,2-diacyl-sn-glycerol [CPD:C00641]
PRODUCT     UDP [CPD:C00015];
            3-beta-D-galactosyl-1,2-diacyl-sn-glycerol
COMMENT     This enzyme adds only one galactosyl group to the diacylglycerol; EC
            2.4.1.241, digalactosyldiacylglycerol synthase, adds a galactosyl
            group to the product of the above reaction. There are three isoforms
            in Arabidopsis that can be divided into two types, A-type (MGD1) and
            B-type (MGD2 and MGD3). MGD1 is the isoform responsible for the bulk
            of monogalactosyldiacylglycerol (MGDG) synthesis in Arabidopsis [4].
REFERENCE   1  [PMID:4838219]
  AUTHORS   Veerkamp JH.
  TITLE     Biochemical changes in Bifidobacterium bifidum var. pennsylvanicus
            after cell-wall inhibition. VI. Biosynthesis of the
            galactosyldiglycerides.
  JOURNAL   Biochim. Biophys. Acta. 348 (1974) 23-34.
  ORGANISM  Bifidobacterium bifidum
REFERENCE   2  [PMID:5681471]
  AUTHORS   Wenger DA, Petitpas JW, Pieringer RA.
  TITLE     The metabolism of glyceride glycolipids. II. Biosynthesis of
            monogalactosyl diglyceride from uridine diphosphate galactose and
            diglyceride in brain.
  JOURNAL   Biochemistry. 7 (1968) 3700-7.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:10518794]
  AUTHORS   Miege C, Marechal E, Shimojima M, Awai K, Block MA, Ohta H, Takamiya
            K, Douce R, Joyard J.
  TITLE     Biochemical and topological properties of type A MGDG synthase, a
            spinach chloroplast envelope enzyme catalyzing the synthesis of both
            prokaryotic and eukaryotic MGDG.
  JOURNAL   Eur. J. Biochem. 265 (1999) 990-1001.
  ORGANISM  Arabidopsis thaliana [GN:ath], Cucumis sativa, spinach
REFERENCE   4  [PMID:15590685]
  AUTHORS   Benning C, Ohta H.
  TITLE     Three enzyme systems for galactoglycerolipid biosynthesis are
            coordinately regulated in plants.
  JOURNAL   J. Biol. Chem. 280 (2005) 2397-400.
  ORGANISM  Arabidopsis sp.
PATHWAY     PATH: map00561  Glycerolipid metabolism
ORTHOLOGY   KO: K03715  1,2-diacylglycerol 3-beta-galactosyltransferase
GENES       ATH: AT2G11810(MGDC) AT4G31780(MGD1) AT5G20410(MGD2)
            BAY: RBAM_020060(ugtP)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.46
            ExPASy - ENZYME nomenclature database: 2.4.1.46
            ExplorEnz - The Enzyme Database: 2.4.1.46
            ERGO genome analysis and discovery system: 2.4.1.46
            BRENDA, the Enzyme Database: 2.4.1.46
            CAS: 37277-55-7
///
ENTRY       EC 2.4.1.47                 Enzyme
NAME        N-acylsphingosine galactosyltransferase;
            UDP galactose-N-acylsphingosine galactosyltransferase;
            uridine diphosphogalactose-acylsphingosine galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:N-acylsphingosine D-galactosyltransferase
REACTION    UDP-galactose + N-acylsphingosine = UDP + D-galactosylceramide
            [RN:R01500 R06277]
ALL_REAC    R01500 R06277(G)
SUBSTRATE   UDP-galactose [CPD:C00052];
            N-acylsphingosine [CPD:C00195]
PRODUCT     UDP [CPD:C00015];
            D-galactosylceramide [CPD:C02686]
REFERENCE   1  [PMID:5807218]
  AUTHORS   Fujino Y, Nakano M.
  TITLE     Enzymic synthesis of cerebroside from ceramide and uridine
            diphosphate galactose.
  JOURNAL   Biochem. J. 113 (1969) 573-5.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00600  Sphingolipid metabolism
ORTHOLOGY   KO: K04628  UDP-galactose ceramide galactosyltransferase
GENES       HSA: 7368(UGT8)
            PTR: 461446(UGT8)
            MMU: 22239(Ugt8a)
            RNO: 50555(Ugt8)
            CFA: 487910(UGT8)
            BTA: 281566(UGT8)
            GGA: 374033(UGT8)
            DRE: 553508(zgc:136652)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.47
            ExPASy - ENZYME nomenclature database: 2.4.1.47
            ExplorEnz - The Enzyme Database: 2.4.1.47
            ERGO genome analysis and discovery system: 2.4.1.47
            BRENDA, the Enzyme Database: 2.4.1.47
            CAS: 37277-56-8
///
ENTRY       EC 2.4.1.48                 Enzyme
NAME        heteroglycan alpha-mannosyltransferase;
            GDP mannose alpha-mannosyltransferase;
            guanosine diphosphomannose-heteroglycan alpha-mannosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-mannose:heteroglycan 2-(or 3-)-alpha-D-mannosyltransferase
REACTION    GDP-mannose + heteroglycan = GDP + 2(or
            3)-alpha-D-mannosyl-heteroglycan [RN:R03768 R03769]
ALL_REAC    R03768 R03769
SUBSTRATE   GDP-mannose [CPD:C00096];
            heteroglycan [CPD:C01923]
PRODUCT     GDP [CPD:C00035];
            2-alpha-D-mannosyl-heteroglycan;
            3-alpha-D-mannosyl-heteroglycan
COMMENT     The acceptor is a heteroglycan primer containing mannose, galactose
            and xylose. 1,2- and 1,3-mannosyl bonds are formed.
REFERENCE   1  [PMID:5492958]
  AUTHORS   Garancis JC, Ankel H, Ankel E, Schutzbach JS.
  TITLE     Mannosyl transfer in Cryptococcus laurentii.
  JOURNAL   J. Biol. Chem. 245 (1970) 3945-55.
  ORGANISM  Cryptococcus laurentii
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.48
            ExPASy - ENZYME nomenclature database: 2.4.1.48
            ExplorEnz - The Enzyme Database: 2.4.1.48
            ERGO genome analysis and discovery system: 2.4.1.48
            BRENDA, the Enzyme Database: 2.4.1.48
            CAS: 37277-57-9
///
ENTRY       EC 2.4.1.49                 Enzyme
NAME        cellodextrin phosphorylase;
            beta-1,4-oligoglucan:orthophosphate glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     1,4-beta-D-oligo-D-glucan:phosphate alpha-D-glucosyltransferase
REACTION    (1,4-beta-D-glucosyl)n + phosphate = (1,4-beta-D-glucosyl)n-1 +
            alpha-D-glucose 1-phosphate [RN:R02888 R06022]
ALL_REAC    R02888 R06022(G)
SUBSTRATE   (1,4-beta-D-glucosyl)n [CPD:C00760];
            phosphate [CPD:C00009]
PRODUCT     (1,4-beta-D-glucosyl)n-1 [CPD:C00760];
            alpha-D-glucose 1-phosphate [CPD:C00103]
REFERENCE   1  [PMID:5773308]
  AUTHORS   Sheth K, Alexander JK.
  TITLE     Purification and properties of beta-1,4-oligoglucan:orthophosphate
            glucosyltransferase from Clostridium thermocellum.
  JOURNAL   J. Biol. Chem. 244 (1969) 457-64.
  ORGANISM  Clostridium thermocellum [GN:cth]
GENES       RSP: RSP_2431
            FAL: FRAAL4362
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.49
            ExPASy - ENZYME nomenclature database: 2.4.1.49
            ExplorEnz - The Enzyme Database: 2.4.1.49
            ERGO genome analysis and discovery system: 2.4.1.49
            BRENDA, the Enzyme Database: 2.4.1.49
            CAS: 37277-58-0
///
ENTRY       EC 2.4.1.50                 Enzyme
NAME        procollagen galactosyltransferase;
            hydroxylysine galactosyltransferase;
            collagen galactosyltransferase;
            collagen hydroxylysyl galactosyltransferase;
            UDP galactose-collagen galactosyltransferase;
            uridine diphosphogalactose-collagen galactosyltransferase;
            UDPgalactose:5-hydroxylysine-collagen galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:procollagen-5-hydroxy-L-lysine D-galactosyltransferase
REACTION    UDP-galactose + procollagen 5-hydroxy-L-lysine = UDP + procollagen
            5-(D-galactosyloxy)-L-lysine [RN:R03380]
ALL_REAC    R03380;
            (other) R03379
SUBSTRATE   UDP-galactose [CPD:C00052];
            procollagen 5-hydroxy-L-lysine [CPD:C01211]
PRODUCT     UDP [CPD:C00015];
            procollagen 5-(D-galactosyloxy)-L-lysine [CPD:C05547]
COMMENT     Probably involved in the synthesis of carbohydrate units in
            complement (cf EC 2.4.1.66 procollagen glucosyltransferase).
REFERENCE   1  [PMID:5722225]
  AUTHORS   Bosmann HB, Eylar EH.
  TITLE     Glycoprotein biosynthesis: the biosynthesis of the
            hydroxylysine-galactose linkage in collagen.
  JOURNAL   Biochem. Biophys. Res. Commun. 33 (1968) 340-6.
  ORGANISM  guinea pig
REFERENCE   2
  AUTHORS   Kivirikko, K.I. and Myllyla, R.
  TITLE     In: Hall, D.A. and Jackson, D.S. (Eds.), International Review of
            Connective Tissue Research, vol. 8, Academic Press, New York, 1979,
            p. 23.
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.50
            ExPASy - ENZYME nomenclature database: 2.4.1.50
            ExplorEnz - The Enzyme Database: 2.4.1.50
            ERGO genome analysis and discovery system: 2.4.1.50
            BRENDA, the Enzyme Database: 2.4.1.50
            CAS: 9028-07-3
///
ENTRY       EC 2.4.1.51       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: UDP-N-acetylglucosaminemdashglycoprotein
            N-acetylglucosaminyltransferase. Now listed as EC 2.4.1.101
            (alpha-1,3-mannosyl-glycoprotein
            2-beta-N-acetylglucosaminyltransferase), EC 2.4.1.143
            (alpha-1,6-mannosyl-glycoprotein
            2-beta-N-acetylglucosaminyltransferase), EC 2.4.1.144
            (beta-1,4-mannosyl-glycoprotein
            4-beta-N-acetylglucosaminyltransferase) and EC 2.4.1.145
            (alpha-1,3-mannosyl-glycoprotein
            4-beta-N-acetylglucosaminyltransferase) (EC 2.4.1.51 created 1972,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.51
            ExPASy - ENZYME nomenclature database: 2.4.1.51
            ExplorEnz - The Enzyme Database: 2.4.1.51
            ERGO genome analysis and discovery system: 2.4.1.51
            BRENDA, the Enzyme Database: 2.4.1.51
///
ENTRY       EC 2.4.1.52                 Enzyme
NAME        poly(glycerol-phosphate) alpha-glucosyltransferase;
            UDP glucose-poly(glycerol-phosphate) alpha-glucosyltransferase;
            uridine diphosphoglucose-poly(glycerol-phosphate)
            alpha-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:poly(glycerol-phosphate) alpha-D-glucosyltransferase
REACTION    UDP-glucose + poly(glycerol phosphate) = UDP +
            O-(alpha-D-glucosyl)poly(glycerol phosphate) [RN:R04041]
ALL_REAC    R04041
SUBSTRATE   UDP-glucose [CPD:C00029];
            poly(glycerol phosphate) [CPD:C02768]
PRODUCT     UDP [CPD:C00015];
            O-(alpha-D-glucosyl)poly(glycerol phosphate)
REFERENCE   1  [PMID:14245359]
  AUTHORS   GLASER L, BURGER MM.
  TITLE     THE SYNTHESIS OF TEICHOIC ACIDS. 3. GLUCOSYLATION OF
            POLYGLYCEROPHOSPHATE.
  JOURNAL   J. Biol. Chem. 239 (1964) 3187-91.
  ORGANISM  Bacillus subtilis [GN:bsu]
ORTHOLOGY   KO: K00712  poly(glycerol-phosphate) alpha-glucosyltransferase
GENES       BSU: BG10724(tagE)
            BPU: BPUM_3229(tagE)
            SAB: SAB0514 SAB0515c
            SAA: SAUSA300_0939
            SAJ: SaurJH9_0587 SaurJH9_0588
            SAH: SaurJH1_0601 SaurJH1_0602
            SPN: SP_1758
            SSA: SSA_0837 SSA_1022
            SGO: SGO_0975(gtaA)
            LPL: lp_1299(tagE1) lp_1311(tagE2) lp_1312(tagE3) lp_2498(tagE4)
                 lp_2843(tagE5) lp_2844(tagE6)
            RBA: RB2471
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.52
            ExPASy - ENZYME nomenclature database: 2.4.1.52
            ExplorEnz - The Enzyme Database: 2.4.1.52
            ERGO genome analysis and discovery system: 2.4.1.52
            BRENDA, the Enzyme Database: 2.4.1.52
            CAS: 37277-60-4
///
ENTRY       EC 2.4.1.53                 Enzyme
NAME        poly(ribitol-phosphate) beta-glucosyltransferase;
            UDP glucose-poly(ribitol-phosphate) beta-glucosyltransferase;
            uridine diphosphoglucose-poly(ribitol-phosphate)
            beta-glucosyltransferase;
            UDP-D-glucose polyribitol phosphate glucosyl transferase;
            UDP-D-glucose:polyribitol phosphate glucosyl transferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:poly(ribitol-phosphate) beta-D-glucosyltransferase
REACTION    UDP-glucose + poly(ribitol phosphate) = UDP +
            (beta-D-glucosyl)poly(ribitol phosphate) [RN:R02716 R06181]
ALL_REAC    R02716 R06181(G)
SUBSTRATE   UDP-glucose [CPD:C00029];
            poly(ribitol phosphate) [CPD:C00653]
PRODUCT     UDP [CPD:C00015];
            (beta-D-glucosyl)poly(ribitol phosphate)
REFERENCE   1  [PMID:4960203]
  AUTHORS   Chin T, Burger MM, Glaser L.
  TITLE     Synthesis of teichoic acids. VI. The formation of multiple wall
            polymers in Bacillus subtilis W-23.
  JOURNAL   Arch. Biochem. Biophys. 116 (1966) 358-67.
  ORGANISM  Bacillus subtilis [GN:bsu]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.53
            ExPASy - ENZYME nomenclature database: 2.4.1.53
            ExplorEnz - The Enzyme Database: 2.4.1.53
            ERGO genome analysis and discovery system: 2.4.1.53
            BRENDA, the Enzyme Database: 2.4.1.53
            CAS: 37277-61-5
///
ENTRY       EC 2.4.1.54                 Enzyme
NAME        undecaprenyl-phosphate mannosyltransferase;
            guanosine diphosphomannose-undecaprenyl phosphate
            mannosyltransferase;
            GDP mannose-undecaprenyl phosphate mannosyltransferase;
            GDP-D-mannose:lipid phosphate transmannosylase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-mannose:undecaprenyl-phosphate D-mannosyltransferase
REACTION    GDP-mannose + undecaprenyl phosphate = GDP +
            D-mannosyl-1-phosphoundecaprenol [RN:R07257]
ALL_REAC    R07257
SUBSTRATE   GDP-mannose [CPD:C00096];
            undecaprenyl phosphate [CPD:C00348]
PRODUCT     GDP [CPD:C00035];
            D-mannosyl-1-phosphoundecaprenol [CPD:C15542]
COFACTOR    Phosphatidylglycerol [CPD:C00344]
COMMENT     Requires phosphatidylglycerol.
REFERENCE   1  [PMID:5350943]
  AUTHORS   Lahav M, Chiu TH, Lennarz WJ.
  TITLE     Studies on the biosynthesis of mannan in Micrococcus lysodeikticus.
            II. The enzymatic synthesis of mannosyl-l-phosphoryl-undecaprenol.
  JOURNAL   J. Biol. Chem. 244 (1969) 5890-8.
  ORGANISM  Micrococcus lysodeikticus
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.54
            ExPASy - ENZYME nomenclature database: 2.4.1.54
            ExplorEnz - The Enzyme Database: 2.4.1.54
            ERGO genome analysis and discovery system: 2.4.1.54
            BRENDA, the Enzyme Database: 2.4.1.54
            CAS: 37277-62-6
///
ENTRY       EC 2.4.1.55       Obsolete  Enzyme
NAME        Transferred to 2.7.8.14
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Transferred entry: now EC 2.7.8.14 CDP-ribitol
            ribitolphosphotransferase (EC 2.4.1.55 created 1972, deleted 1982)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.55
            ExPASy - ENZYME nomenclature database: 2.4.1.55
            ExplorEnz - The Enzyme Database: 2.4.1.55
            ERGO genome analysis and discovery system: 2.4.1.55
            BRENDA, the Enzyme Database: 2.4.1.55
///
ENTRY       EC 2.4.1.56                 Enzyme
NAME        lipopolysaccharide N-acetylglucosaminyltransferase;
            UDP-N-acetylglucosamine-lipopolysaccharide
            N-acetylglucosaminyltransferase;
            uridine diphosphoacetylglucosamine-lipopolysaccharide
            acetylglucosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:lipopolysaccharide
            N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine + lipopolysaccharide = UDP +
            N-acetyl-D-glucosaminyllipopolysaccharide [RN:R01996]
ALL_REAC    R01996
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            lipopolysaccharide [CPD:C00338]
PRODUCT     UDP [CPD:C00015];
            N-acetyl-D-glucosaminyllipopolysaccharide [CPD:C04539]
COMMENT     Transfers N-acetylglucosaminyl residues to a D-galactose residue in
            the partially completed lipopolysaccharide core [cf. EC 2.4.1.44
            (lipopolysaccharide 3-alpha-galactosyltransferase), EC 2.4.1.58
            (lipopolysaccharide glucosyltransferase I) and EC 2.4.1.73
            (lipopolysaccharide glucosyltransferase II)].
REFERENCE   1
  AUTHORS   Osborn, M.J. and D'Ari, L.
  TITLE     Enzymatic incorporation of N-acetylglucosamine into cell wall
            lipopolysaccharide in a mutant strain of Salmonella typhimurium.
  JOURNAL   Biochem. Biophys. Res. Commun. 16 (1964) 568-575.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00540  Lipopolysaccharide biosynthesis
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K03280  acetylglucosaminyltransferase
            KO: K05944  
GENES       STY: STY4081(waaK)
            STT: t3805(waaK)
            SPT: SPA3566(waaK)
            SEC: SC3637(rfaK)
            STM: STM3714(rfaK)
            SAT: SYN_00818
            PUB: SAR11_0559(rfaK)
            BRA: BRADO7071
            AVA: Ava_3573
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.56
            ExPASy - ENZYME nomenclature database: 2.4.1.56
            ExplorEnz - The Enzyme Database: 2.4.1.56
            ERGO genome analysis and discovery system: 2.4.1.56
            BRENDA, the Enzyme Database: 2.4.1.56
            CAS: 37277-64-8
///
ENTRY       EC 2.4.1.57                 Enzyme
NAME        phosphatidylinositol alpha-mannosyltransferase;
            GDP mannose-phosphatidyl-myo-inositol alpha-mannosyltransferase;
            GDPmannose:1-phosphatidyl-myo-inositol alpha-D-mannosyltransferase;
            guanosine diphosphomannose-phosphatidyl-inositol
            alpha-mannosyltransferase;
            phosphatidyl-myo-inositol alpha-mannosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-mannose:1-phosphatidyl-1D-myo-inositol
            alpha-D-mannosyltransferase
REACTION    Transfers one or more alpha-D-mannose residues from GDP-mannose to
            positions 2,6 and others in 1-phosphatidyl-myo-inositol
REFERENCE   1  [PMID:4295288]
  AUTHORS   Brennan P, Ballou CE.
  TITLE     Phosphatidylmyoinositol monomannoside in Propionibacterium
            shermanii.
  JOURNAL   Biochem. Biophys. Res. Commun. 30 (1968) 69-75.
  ORGANISM  Propionibacterium shermanii
ORTHOLOGY   KO: K08256  phosphatidylinositol alpha-mannosyltransferase
GENES       NOC: Noc_1972 Noc_2889
            BUR: Bcep18194_A3352 Bcep18194_B2111 Bcep18194_B2267
            BAM: Bamb_3364
            BTE: BTH_I0524
            HAR: HEAR1144
            ADE: Adeh_2418 Adeh_3504 Adeh_4147
            AFW: Anae109_1460 Anae109_4290
            RBE: RBE_0702
            RLE: RL3817 pRL90136
            RRU: Rru_A2492 Rru_A3091 Rru_A3376 Rru_A3658
            MTU: Rv2610c(pimA)
            MTC: MT2685
            MBO: Mb2642c(pimA)
            MLE: ML0452
            MPA: MAP2712c
            MAV: MAV_3486
            MSM: MSMEG_2935
            MUL: MUL_3252(pimA)
            MVA: Mvan_2562
            MGI: Mflv_3834
            MMC: Mmcs_2246
            MKM: Mkms_2293
            MJL: Mjls_2285
            CGL: NCgl1603(cgl1667)
            CGB: cg1876
            CEF: CE1781
            CDI: DIP1384
            CJK: jk1062(pimA)
            NFA: nfa37080
            RHA: RHA1_ro06882
            SCO: SCO1525(SCL2.15c)
            SMA: SAV6828
            TFU: Tfu_2101
            FRA: Francci3_1364
            FAL: FRAAL1773 FRAAL2134
            ACE: Acel_1353
            STP: Strop_1788
            RXY: Rxyl_2620
            SYG: sync_0085
            AVA: Ava_0439 Ava_0842 Ava_0853 Ava_2434 Ava_2581 Ava_3445
                 Ava_3572 Ava_4841 Ava_5057
            CCH: Cag_1294
            DET: DET0978
            DEH: cbdb_A942
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.57
            ExPASy - ENZYME nomenclature database: 2.4.1.57
            ExplorEnz - The Enzyme Database: 2.4.1.57
            ERGO genome analysis and discovery system: 2.4.1.57
            BRENDA, the Enzyme Database: 2.4.1.57
            CAS: 37277-65-9
///
ENTRY       EC 2.4.1.58                 Enzyme
NAME        lipopolysaccharide glucosyltransferase I;
            UDP-glucose:lipopolysaccharide glucosyltransferase I;
            lipopolysaccharide glucosyltransferase;
            uridine diphosphate glucose:lipopolysaccharide glucosyltransferase
            I;
            uridine diphosphoglucose-lipopolysaccharide glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:lipopolysaccharide glucosyltransferase
REACTION    UDP-glucose + lipopolysaccharide = UDP +
            D-glucosyl-lipopolysaccharide [RN:R01994]
ALL_REAC    R01994
SUBSTRATE   UDP-glucose [CPD:C00029];
            lipopolysaccharide [CPD:C00338]
PRODUCT     UDP [CPD:C00015];
            D-glucosyl-lipopolysaccharide
COMMENT     Transfers glucosyl residues to the backbone portion of
            lipopolysaccharide [cf. EC 2.4.1.44 (lipopolysaccharide
            3-alpha-galactosyltransferase, EC 2.4.1.56 (lipopolysaccharide
            N-acetylglucosaminyltransferase) and EC 2.4.1.73 (lipopolysaccharide
            glucosyltransferase II)].
REFERENCE   1  [PMID:4553445]
  AUTHORS   Muller E, Hinckley A, Rothfield L.
  TITLE     Studies of phospholipid-requiring bacterial enzymes. 3. Purification
            and properties of uridine diphosphate glucose:lipopolysaccharide
            glucosyltransferase I.
  JOURNAL   J. Biol. Chem. 247 (1972) 2614-22.
  ORGANISM  Salmonella typhimurium
REFERENCE   2
  AUTHORS   Rothfield, L., Osborn, M.J. and Horecker, B.L.
  TITLE     Biosynthesis of bacterial lipopolysaccharide. II. Incorporation of
            glucose and galactose catalyzed by particulate and soluble enzymes
            in salmonella.
  JOURNAL   J. Biol. Chem. 239 (1964) 2788-2795.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00540  Lipopolysaccharide biosynthesis
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K03276  glucosyltransferase
            KO: K03279  glucosyltransferase
            KO: K05945  
GENES       ECO: b3626(rfaJ)
            ECJ: JW3601(rfaJ)
            ECC: c4452(rfaJ)
            ECI: UTI89_C4171(rfaJ)
            ECV: APECO1_2830(rfaJ)
            ECW: EcE24377A_4129(rfaJ)
            ECX: EcHS_A3837(rfaJ2)
            STY: STY4078(rfaJ)
            STT: t3802(waaJ)
            SPT: SPA3569(waaJ)
            SEC: SC3640(rfaJ)
            STM: STM3717(rfaJ)
            SSN: SSON_3779(waaJ)
            SBO: SBO_3630(waaJ)
            SDY: SDY_4058(rfaJ)
            ECA: ECA0157(waaJ)
            SGL: SG2200
            CVI: CV_0821(rfaB) CV_0822(rfaQ)
            HAC: Hac_1545(rfaJ)
            BFR: BF0225
            BFS: BF0184
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.58
            ExPASy - ENZYME nomenclature database: 2.4.1.58
            ExplorEnz - The Enzyme Database: 2.4.1.58
            ERGO genome analysis and discovery system: 2.4.1.58
            BRENDA, the Enzyme Database: 2.4.1.58
            CAS: 9074-00-4
///
ENTRY       EC 2.4.1.59       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: UDP-glucuronate-estradiol glucuronosyltransferase.
            Now included with EC 2.4.1.17, glucuronosyltransferase (EC 2.4.1.59
            created 1972, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.59
            ExPASy - ENZYME nomenclature database: 2.4.1.59
            ExplorEnz - The Enzyme Database: 2.4.1.59
            ERGO genome analysis and discovery system: 2.4.1.59
            BRENDA, the Enzyme Database: 2.4.1.59
///
ENTRY       EC 2.4.1.60                 Enzyme
NAME        abequosyltransferase;
            trihexose diphospholipid abequosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     CDP-abequose:D-mannosyl-L-rhamnosyl-D-galactose-1-diphospholipid
            D-abequosyltransferase
REACTION    CDP-abequose + D-mannosyl-L-rhamnosyl-D-galactose-1-diphospholipid =
            CDP + D-abequosyl-D-mannosyl-rhamnosyl-D-galactose-1-diphospholipid
            [RN:R04581]
ALL_REAC    R04581
SUBSTRATE   CDP-abequose [CPD:C01788];
            D-mannosyl-L-rhamnosyl-D-galactose-1-diphospholipid [CPD:C04724]
PRODUCT     CDP [CPD:C00112];
            D-abequosyl-D-mannosyl-rhamnosyl-D-galactose-1-diphospholipid
            [CPD:C04808]
REFERENCE   1  [PMID:4297268]
  AUTHORS   Osborn MJ, Weiner IM.
  TITLE     Biosynthesis of a bacterial lipopolysaccharide. VI. Mechanism of
            incorporation of abequose into the O-antigen of Salmonella
            typhimurium.
  JOURNAL   J. Biol. Chem. 243 (1968) 2631-9.
  ORGANISM  Salmonella typhimurium
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.60
            ExPASy - ENZYME nomenclature database: 2.4.1.60
            ExplorEnz - The Enzyme Database: 2.4.1.60
            ERGO genome analysis and discovery system: 2.4.1.60
            BRENDA, the Enzyme Database: 2.4.1.60
            CAS: 37277-67-1
///
ENTRY       EC 2.4.1.61       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: UDP-glucuronate-estriol
            16alpha-glucuronosyltransferase. Now included with EC 2.4.1.17,
            glucuronosyltransferase (EC 2.4.1.61 created 1972, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.61
            ExPASy - ENZYME nomenclature database: 2.4.1.61
            ExplorEnz - The Enzyme Database: 2.4.1.61
            ERGO genome analysis and discovery system: 2.4.1.61
            BRENDA, the Enzyme Database: 2.4.1.61
///
ENTRY       EC 2.4.1.62                 Enzyme
NAME        ganglioside galactosyltransferase;
            UDP-galactose---ceramide galactosyltransferase;
            uridine diphosphogalactose-ceramide galactosyltransferase;
            UDP galactose-LAC Tet-ceramide alpha-galactosyltransferase;
            UDP-galactose-GM2 galactosyltransferase;
            uridine diphosphogalactose-GM2 galactosyltransferase;
            uridine diphosphate D-galactose:glycolipid galactosyltransferase;
            UDP-galactose:N-acetylgalactosaminyl-(N-acetylneuraminyl)
            galactosyl-glucosyl-ceramide galactosyltransferase;
            UDP-galactose-GM2 ganglioside galactosyltransferase;
            GM1-synthase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galac
            tosyl-D-glucosyl-N-acylsphingosine beta-1,3-D-galactosyltransferase
REACTION    UDP-galactose +
            N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-1,4-
            beta-D-glucosyl-N-acylsphingosine = UDP +
            D-galactosyl-1,3-beta-N-acetyl-D-galactosaminyl-(N-
            acetylneuraminyl)-D-galactosyl-D-glucosyl-N-acylsphingosine
            [RN:R04631 R05941]
ALL_REAC    R04631 R05941(G);
            (other) R05110 R05111 R05948(G) R05953(G) R05956(G)
SUBSTRATE   UDP-galactose [CPD:C00052];
            N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-1,4-
            beta-D-glucosyl-N-acylsphingosine [CPD:C04884]
PRODUCT     UDP [CPD:C00015];
            D-galactosyl-1,3-beta-N-acetyl-D-galactosaminyl-(N-
            acetylneuraminyl)-D-galactosyl-D-glucosyl-N-acylsphingosine
            [CPD:C04911]
COMMENT     The substrate is also known as GM2.
REFERENCE   1  [PMID:5842076]
  AUTHORS   Basu S, Kaufman B, Roseman S.
  TITLE     Conversion of Tay-Sachs ganglioside to monosialoganglioside by brain
            uridine diphosphate D-galactose: glycolipid galactosyltransferase.
  JOURNAL   J. Biol. Chem. 240 (1965) 4115-7.
  ORGANISM  chicken [GN:gga], rat [GN:rno], pig [GN:ssc]
REFERENCE   2  [PMID:4987145]
  AUTHORS   Yip GB, Dain JA.
  TITLE     The enzymic synthesis of ganglioside. II. UDP-galactose:
            N-acetylgalactosaminyl-(N-acetylneuraminyl)galactosyl-glucosyl-ceram
            ide galactosyltransferase in rat brain.
  JOURNAL   Biochim. Biophys. Acta. 206 (1970) 252-60.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:5484669]
  AUTHORS   Yip MC, Dain JA.
  TITLE     Frog brain uridine diphosphate
            galactose-N-acetylgalactosaminyl-N-acetylneuraminylgalactosylglucosy
            lceram ide galactosyltransferase.
  JOURNAL   Biochem. J. 118 (1970) 247-52.
  ORGANISM  frog
PATHWAY     PATH: map00604  Glycosphingolipid biosynthesis - ganglioseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K00715  ganglioside galactosyltransferase
GENES       HSA: 8705(B3GALT4)
            MMU: 54218(B3galt4)
            RNO: 171079(B3galt4)
            CFA: 481737(B3GALT4)
            BTA: 768038(B3GALT4)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.62
            ExPASy - ENZYME nomenclature database: 2.4.1.62
            ExplorEnz - The Enzyme Database: 2.4.1.62
            ERGO genome analysis and discovery system: 2.4.1.62
            BRENDA, the Enzyme Database: 2.4.1.62
            CAS: 37217-28-0
///
ENTRY       EC 2.4.1.63                 Enzyme
NAME        linamarin synthase;
            uridine diphosphoglucose-ketone glucosyltransferase;
            uridine diphosphate-glucose-ketone cyanohydrin
            beta-glucosyltransferase;
            UDP glucose ketone cyanohydrin glucosyltransferase;
            UDP-glucose:ketone cyanohydrin beta-glucosyltransferase;
            uridine diphosphoglucose-ketone cyanohydrin glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:2-hydroxy-2-methylpropanenitrile
            beta-D-glucosyltransferase
REACTION    UDP-glucose + 2-hydroxy-2-methylpropanenitrile = UDP + linamarin
            [RN:R03625]
ALL_REAC    R03625
SUBSTRATE   UDP-glucose [CPD:C00029];
            2-hydroxy-2-methylpropanenitrile [CPD:C02659]
PRODUCT     UDP [CPD:C00015];
            linamarin [CPD:C01594]
COMMENT     The enzyme glucosylates the cyanohydrins of butanone and
            pentan-3-one as well as that of acetone.
REFERENCE   1  [PMID:5417265]
  AUTHORS   Hahlbrock K, Conn EE.
  TITLE     The biosynthesis of cyanogenic glycosides in higher plants. I.
            Purification and properties of a uridine diphosphate-glucose-ketone
            cyanohydrin beta-glucosyltransferase from Linum usitatissimum L.
  JOURNAL   J. Biol. Chem. 245 (1970) 917-22.
  ORGANISM  Linum usitatissimum
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.63
            ExPASy - ENZYME nomenclature database: 2.4.1.63
            ExplorEnz - The Enzyme Database: 2.4.1.63
            ERGO genome analysis and discovery system: 2.4.1.63
            BRENDA, the Enzyme Database: 2.4.1.63
            CAS: 37277-68-2
///
ENTRY       EC 2.4.1.64                 Enzyme
NAME        alpha,alpha-trehalose phosphorylase;
            trehalose phosphorylase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     alpha,alpha-trehalose:phosphate beta-D-glucosyltransferase
REACTION    alpha,alpha-trehalose + phosphate = D-glucose + beta-D-glucose
            1-phosphate [RN:R02727 R06053]
ALL_REAC    R02727 R06053(G)
SUBSTRATE   alpha,alpha-trehalose [CPD:C01083];
            phosphate [CPD:C00009]
PRODUCT     D-glucose [CPD:C00031];
            beta-D-glucose 1-phosphate [CPD:C00663]
REFERENCE   1  [PMID:5413942]
  AUTHORS   Belocopitow E, Marechal LR.
  TITLE     Trehalose phosphorylase from Euglena gracilis.
  JOURNAL   Biochim. Biophys. Acta. 198 (1970) 151-4.
  ORGANISM  Euglena gracilis
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K05342  alpha,alpha-trehalose phosphorylase
GENES       PAC: PPA1108
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.64
            ExPASy - ENZYME nomenclature database: 2.4.1.64
            ExplorEnz - The Enzyme Database: 2.4.1.64
            ERGO genome analysis and discovery system: 2.4.1.64
            BRENDA, the Enzyme Database: 2.4.1.64
            CAS: 37205-59-7
///
ENTRY       EC 2.4.1.65                 Enzyme
NAME        3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase;
            (Lea)-dependent (alpha-3/4)-fucosyltransferase;
            alpha(1,3/1,4) fucosyltransferase III;
            alpha-(1->4)-L-fucosyltransferase;
            alpha-4-L-fucosyltransferase;
            beta-acetylglucosaminylsaccharide fucosyltransferase;
            FucT-II;
            Lewis alpha-(1->3/4)-fucosyltransferase;
            Lewis blood group alpha-(1->3/4)-fucosyltransferase;
            Lewis(Le) blood group gene-dependent
            alpha-(1->3/4)-L-fucosyltransferase;
            blood group Lewis alpha-4-fucosyltransferase;
            blood-group substance Lea-dependent fucosyltransferase;
            guanosine diphosphofucose-beta-acetylglucosaminylsaccharide
            4-alpha-L-fucosyltransferase;
            guanosine diphosphofucose-glycoprotein 4-alpha-L-fucosyltransferase;
            guanosine diphosphofucose-glycoprotein 4-alpha-fucosyltransferase;
            3-alpha-galactosyl-N-acetylglucosaminide
            4-alpha-L-fucosyltransferase;
            GDP-beta-L-fucose:3-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R
            4I-alpha-L-fucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-L-fucose:3-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R
            4I-alpha-L-fucosyltransferase
REACTION    GDP-beta-L-fucose +
            beta-D-galactosyl-(1->3)-N-acetyl-D-glucosaminyl-R = GDP +
            beta-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-beta-D-
            glucosaminyl-R [RN:R04553]
ALL_REAC    R04553 > R06155(G);
            (other) R06162(G) R06163(G) R06164(G) R06165(G)
SUBSTRATE   GDP-beta-L-fucose [CPD:C00325];
            beta-D-galactosyl-(1->3)-N-acetyl-D-glucosaminyl-R
PRODUCT     GDP [CPD:C00035];
            beta-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-beta-D-
            glucosaminyl-R
COMMENT     This enzyme is the product of the Lewis blood group gene. Normally
            acts on a glycoconjugate where R (see reaction) is a glycoprotein or
            glycolipid. Although it is a 4-fucosyltransferase, it has a
            persistent 3-fucosyltransferase activity towards the glucose residue
            in free lactose. This enzyme fucosylates on O-4 of an
            N-acetylglucosamine that carries a galactosyl group on O-3, unlike
            EC 2.4.1.152, 4-galactosyl-N-acetylglucosaminide
            3-alpha-L-fucosyltransferase, which fucosylates on O-3 of an
            N-acetylglucosamine that carries a galactosyl group on O-4. Enzymes
            catalysing the 4-alpha-fucosylation of the GlcNAc in
            beta-D-Gal-(1->3)-beta-GlcNAc sequences (with some activity also as
            3-alpha-fucosyltransferases) are present in plants, where the
            function in vivo is the modification of N-glycans. In addition, the
            fucTa gene of Helicobacter strain UA948 encodes a fucosyltransferase
            with both 3-alpha- and 4-alpha-fucosyltransferase activities.
REFERENCE   1  [PMID:7287719]
  AUTHORS   Prieels JP, Monnom D, Dolmans M, Beyer TA, Hill RL.
  TITLE     Co-purification of the Lewis blood group N-acetylglucosaminide alpha
            1 goes to 4 fucosyltransferase and an N-acetylglucosaminide alpha 1
            goes to 3 fucosyltransferase from human milk.
  JOURNAL   J. Biol. Chem. 256 (1981) 10456-63.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:10671538]
  AUTHORS   Rasko DA, Wang G, Palcic MM, Taylor DE.
  TITLE     Cloning and characterization of the alpha(1,3/4) fucosyltransferase
            of Helicobacter pylori.
  JOURNAL   J. Biol. Chem. 275 (2000) 4988-94.
  ORGANISM  Helicobacter pylori
REFERENCE   3  [PMID:12084979]
  AUTHORS   Wilson IB.
  TITLE     Identification of a cDNA encoding a plant Lewis-type
            alpha1,4-fucosyltransferase.
  JOURNAL   Glycoconj. J. 18 (2001) 439-47.
  ORGANISM  Lycopersicon esculentum [GN:eles]
REFERENCE   4  [PMID:12676935]
  AUTHORS   Ma B, Wang G, Palcic MM, Hazes B, Taylor DE.
  TITLE     C-terminal amino acids of Helicobacter pylori alpha1,3/4
            fucosyltransferases determine type I and type II transfer.
  JOURNAL   J. Biol. Chem. 278 (2003) 21893-900.
  ORGANISM  Helicobacter pylori
PATHWAY     PATH: map00601  Glycosphingolipid biosynthesis - lactoseries
            PATH: map00602  Glycosphingolipid biosynthesis - neo-lactoseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K00716  galactoside 3(4)-fucosyltransferase 3
            KO: K07633  galactoside alpha-1,3-fucosyltransferase 5
            KO: K07634  galactoside alpha-1,3-fucosyltransferase 6
GENES       HSA: 2525(FUT3) 2527(FUT5) 2528(FUT6)
            PTR: 455628(FUT5) 493975(FUT3) 493976(FUT6)
            CFA: 449024(FUT6)
            BTA: 338077(FUT)
            GGA: 428341(FUT3)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.65
            ExPASy - ENZYME nomenclature database: 2.4.1.65
            ExplorEnz - The Enzyme Database: 2.4.1.65
            ERGO genome analysis and discovery system: 2.4.1.65
            BRENDA, the Enzyme Database: 2.4.1.65
            CAS: 37277-69-3
///
ENTRY       EC 2.4.1.66                 Enzyme
NAME        procollagen glucosyltransferase;
            galactosylhydroxylysine glucosyltransferase;
            collagen glucosyltransferase;
            collagen hydroxylysyl glucosyltransferase;
            galactosylhydroxylysyl glucosyltransferase;
            UDP-glucose-collagenglucosyltransferase;
            uridine diphosphoglucose-collagen glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:5-(D-galactosyloxy)-L-lysine-procollagen
            D-glucosyltransferase
REACTION    UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen = UDP +
            1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen [RN:R04491]
ALL_REAC    R04491
SUBSTRATE   UDP-glucose [CPD:C00029];
            5-(D-galactosyloxy)-L-lysine-procollagen [CPD:C04487]
PRODUCT     UDP [CPD:C00015];
            1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen [CPD:C04759]
COMMENT     Probably involved in the synthesis of carbohydrate units in
            complement (cf. EC 2.4.1.50 procollagen galactosyltransferase).
REFERENCE   1  [PMID:5637038]
  AUTHORS   Bosmann HB, Eylar EH.
  TITLE     Attachment of carbohydrate to collagen. Isolation, purification and
            properties of the glucosyl transferase.
  JOURNAL   Biochem. Biophys. Res. Commun. 30 (1968) 89-94.
  ORGANISM  guinea pig
REFERENCE   2  [PMID:4968368]
  AUTHORS   Bosmann HB, Eylar EH.
  TITLE     Collagen-glucosyl transferase in fibriblasts transformed by
            oncogenic viruses.
  JOURNAL   Nature. 218 (1968) 582-3.
REFERENCE   3  [PMID:4288358]
  AUTHORS   Butler WT, Cunningham LW.
  TITLE     Evidence for the linkage of a disaccharide to hydroxylysine in
            tropocollagen.
  JOURNAL   J. Biol. Chem. 241 (1966) 3882-8.
  ORGANISM  guinea pig
REFERENCE   4
  AUTHORS   Kivirikko, K.I. and Myllyla, R.
  TITLE     In: Hall, D.A. and Jackson, D.S. (Eds.), International Review of
            Connective Tissue Research, vol. 8, Academic Press, New York, 1979,
            p. 23.
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.66
            ExPASy - ENZYME nomenclature database: 2.4.1.66
            ExplorEnz - The Enzyme Database: 2.4.1.66
            ERGO genome analysis and discovery system: 2.4.1.66
            BRENDA, the Enzyme Database: 2.4.1.66
            CAS: 9028-08-4
///
ENTRY       EC 2.4.1.67                 Enzyme
NAME        galactinol---raffinose galactosyltransferase;
            galactinol-raffinose galactosyltransferase;
            stachyose synthetase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     alpha-D-galactosyl-(1->3)-myo-inositol:raffinose
            galactosyltransferase
REACTION    alpha-D-galactosyl-(1->3)-1D-myo-inositol + raffinose = myo-inositol
            + stachyose [RN:R03418 R06042]
ALL_REAC    R03418 R06042(G)
SUBSTRATE   alpha-D-galactosyl-(1->3)-1D-myo-inositol;
            raffinose [CPD:C00492]
PRODUCT     myo-inositol [CPD:C00137];
            stachyose [CPD:C01613]
COMMENT     This enzyme also catalyses galactosyl transfer from stachyose to
            raffinose (shown by labelling) [4]. For synthesis of the substrate,
            see EC 2.4.1.123, inositol 3-alpha-galactosyltransferase. See also
            EC 2.4.1.82, galactinol---sucrose galactosyltransferase.
REFERENCE   1
  AUTHORS   Tanner, W.
  TITLE     Die Biosynthese der Stachyose.
  JOURNAL   Ber. Dtsch. Bot. Ges. 80 (1967) 111.
  ORGANISM  Phaseolus vulgaris
REFERENCE   2  [PMID:5655499]
  AUTHORS   Tanner W, Kandler O.
  TITLE     Myo-inositol, a cofactor in the biosynthesis of stachyose.
  JOURNAL   Eur. J. Biochem. 4 (1968) 233-9.
  ORGANISM  Phaseolus vulgaris
REFERENCE   3  [PMID:4774118]
  AUTHORS   Lehle L, Tanner W.
  TITLE     The function of myo-inositol in the biosynthesis of raffinose.
            Purification and characterization of galactinol:sucrose
            6-galactosyltransferase from Vicia faba seeds.
  JOURNAL   Eur. J. Biochem. 38 (1973) 103-10.
  ORGANISM  Vicia faba
REFERENCE   4
  AUTHORS   Kandler, O. and Hopf, H.
  TITLE     Occurrence, metabolism and function of oligosaccharides.
  JOURNAL   In: Preiss, J. (Ed.), The Biochemistry of Plant, vol. 3, Academic
            Press, New York, 1980, p. 221-270.
PATHWAY     PATH: map00052  Galactose metabolism
ORTHOLOGY   KO: K06611  stachyose synthetase
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.67
            ExPASy - ENZYME nomenclature database: 2.4.1.67
            ExplorEnz - The Enzyme Database: 2.4.1.67
            ERGO genome analysis and discovery system: 2.4.1.67
            BRENDA, the Enzyme Database: 2.4.1.67
            CAS: 37277-70-6
///
ENTRY       EC 2.4.1.68                 Enzyme
NAME        glycoprotein 6-alpha-L-fucosyltransferase;
            GDP-fucose---glycoprotein fucosyltransferase;
            GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1->6fucosyltransferase;
            GDP-L-fucose-glycoprotein fucosyltransferase;
            glycoprotein fucosyltransferase;
            guanosine diphosphofucose-glycoprotein fucosyltransferase;
            GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked
            N-acetylglucosamine of
            4-N-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-
            acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-
            mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-
            glucosaminyl}asparagine) 6-alpha-L-fucosyltransferase;
            FucT
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked
            N-acetylglucosamine of
            N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-a
            cetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-man
            nosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glu
            cosaminyl}asparagine) 6-alpha-L-fucosyltransferase
REACTION    GDP-L-fucose +
            N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-
            acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-
            mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-
            glucosaminyl}asparagine = GDP +
            N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-
            acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-
            mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-
            fucosyl-(1->6)]-N-acetyl-beta-D-glucosaminyl}asparagine [RN:R05988]
ALL_REAC    R05988(G)
SUBSTRATE   GDP-L-fucose [CPD:C00325];
            N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-
            acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-
            mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-
            glucosaminyl}asparagine
PRODUCT     GDP [CPD:C00035];
            N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-
            acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-
            mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-
            fucosyl-(1->6)]-N-acetyl-beta-D-glucosaminyl}asparagine
COMMENT     This enzyme catalyses a reaction similar to that of EC 2.4.1.214,
            glycoprotein 3-alpha-L-fucosyltransferase, but transfers the
            L-fucosyl group from GDP-beta-L-fucose to form an alpha1,6-linkage
            rather than an alpha1,3-linkage.
REFERENCE   1  [PMID:7083256]
  AUTHORS   Longmore GD, Schachter H.
  TITLE     Product-identification and substrate-specificity studies of the
            GDP-L-fucose:2-acetamido-2-deoxy-beta-D-glucoside (FUC goes to
            Asn-linked GlcNAc) 6-alpha-L-fucosyltransferase in a Golgi-rich
            fraction from porcine liver.
  JOURNAL   Carbohydr. Res. 100 (1982) 365-92.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:3364733]
  AUTHORS   Voynow JA, Scanlin TF, Glick MC.
  TITLE     A quantitative method for GDP-L-Fuc:N-acetyl-beta-D-glucosaminide
            alpha 1----6fucosyltransferase activity with lectin affinity
            chromatography.
  JOURNAL   Anal. Biochem. 168 (1988) 367-73.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:8910378]
  AUTHORS   Uozumi N, Yanagidani S, Miyoshi E, Ihara Y, Sakuma T, Gao CX,
            Teshima T, Fujii S, Shiba T, Taniguchi N.
  TITLE     Purification and cDNA cloning of porcine brain
            GDP-L-Fuc:N-acetyl-beta-D-glucosaminide
            alpha1--&gt;6fucosyltransferase.
  JOURNAL   J. Biol. Chem. 271 (1996) 27810-7.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map00533  Keratan sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00717  glycoprotein 6-alpha-L-fucosyltransferase
GENES       HSA: 2530(FUT8)
            PTR: 449506(FUT8)
            MMU: 53618(Fut8)
            RNO: 432392(Fut8)
            CFA: 448804(FUT8)
            BTA: 281177(FUT8)
            SSC: 396933(FUT8)
            GGA: 423178(FUT8)
            XTR: 407913(fut8)
            DRE: 445378(fut8)
            SPU: 592434(LOC592434)
            DME: Dmel_CG2448
            CEL: C10F3.6(fut-8)
STRUCTURES  PDB: 2DE0  2HHC  2HLH  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.68
            ExPASy - ENZYME nomenclature database: 2.4.1.68
            ExplorEnz - The Enzyme Database: 2.4.1.68
            ERGO genome analysis and discovery system: 2.4.1.68
            BRENDA, the Enzyme Database: 2.4.1.68
            CAS: 9033-08-3
///
ENTRY       EC 2.4.1.69                 Enzyme
NAME        galactoside 2-alpha-L-fucosyltransferase;
            blood group H alpha-2-fucosyltransferase;
            guanosine diphosphofucose-galactoside 2-L-fucosyltransferase;
            alpha-(1->2)-L-fucosyltransferase;
            alpha-2-fucosyltransferase;
            alpha-2-L-fucosyltransferase;
            blood-group substance H-dependent fucosyltransferase;
            guanosine diphosphofucose-glycoprotein 2-alpha-fucosyltransferase;
            guanosine diphosphofucose-lactose fucosyltransferase;
            GDP fucose-lactose fucosyltransferase;
            guanosine diphospho-L-fucose-lactose fucosyltransferase;
            guanosine
            diphosphofucose-beta-D-galactosyl-alpha-2-L-fucosyltransferase;
            guanosine
            diphosphofucose-
            galactosylacetylglucosaminylgalactosylglucosylceramide
            alpha-L-fucosyltransferase;
            guanosine diphosphofucose-glycoprotein 2-alpha-L-fucosyltransferase;
            H-gene-encoded beta-galactoside alpha1->2fucosyltransferase;
            secretor-type beta-galactoside alpha1->2fucosyltransferase;
            beta-galactoside alpha1->2fucosyltransferase;
            GDP-L-fucose:lactose fucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-beta-L-fucose:beta-D-galactosyl-R 2-alpha-L-fucosyltransferase
REACTION    GDP-beta-L-fucose + beta-D-galactosyl-R = GDP +
            alpha-L-fucosyl-1,2-beta-D-galactosyl-R [RN:R04081]
ALL_REAC    R04081 > R05968(G) R06024(G) R06031(G) R06035(G) R06041(G) R06085(G)
            R06086(G) R06089(G) R06090(G) R06156(G);
            (other) R06170(G)
SUBSTRATE   GDP-beta-L-fucose [CPD:C00325];
            beta-D-galactosyl-R [CPD:C02900]
PRODUCT     GDP [CPD:C00035];
            alpha-L-fucosyl-1,2-beta-D-galactosyl-R [CPD:C04467]
COMMENT     Free lactose can act as acceptor. Normally acts on a glycoconjugate
            where R (see reaction) is a glycoprotein or glycolipid. The action
            on glycolipid was previously listed as EC 2.4.1.89.
REFERENCE   1  [PMID:804484]
  AUTHORS   Basu S, Basu M, Chien JL.
  TITLE     Enzymatic synthesis of a blood group H-related glycosphingolipid by
            an alpha-fucosyltransferase from bovine spleen.
  JOURNAL   J. Biol. Chem. 250 (1975) 2956-62.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:7372640]
  AUTHORS   Beyer TA, Hill RL.
  TITLE     Enzymatic properties of the beta-galactoside alpha 1 leads to 2
            fucosyltransferase from porcine submaxillary gland.
  JOURNAL   J. Biol. Chem. 255 (1980) 5373-9.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:6246105]
  AUTHORS   Beyer TA, Sadler JE, Hill RL.
  TITLE     Purification to homogeneity of H blood group beta-galactoside alpha
            1 leads to 2 fucosyltransferase from porcine submaxillary gland.
  JOURNAL   J. Biol. Chem. 255 (1980) 5364-72.
  ORGANISM  pig [GN:ssc]
REFERENCE   4
  AUTHORS   Grollman, A.P.
  TITLE     GDP-L-fucose:lactose fucosyltransferase from mammary gland.
  JOURNAL   Methods Enzymol. 8 (1966) 351-353.
  ORGANISM  dog [GN:cfa]
PATHWAY     PATH: map00601  Glycosphingolipid biosynthesis - lactoseries
            PATH: map00602  Glycosphingolipid biosynthesis - neo-lactoseries
            PATH: map00603  Glycosphingolipid biosynthesis - globoseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K00718  galactoside 2-L-fucosyltransferase
GENES       HSA: 2523(FUT1) 2524(FUT2)
            PTR: 468944(FUT2) 468947(FUT1)
            MMU: 14343(Fut1)
            RNO: 58924(Fut2) 81919(Fut1)
            CFA: 484396(FUT1) 484398(FUT2)
            BTA: 281174(FUT1) 281175(FUT2)
            SSC: 397138(FUT1) 397139(FUT2)
            XTR: 447958(fut1)
            ATH: AT2G03220(FT1)
            OSA: 4330827
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.69
            ExPASy - ENZYME nomenclature database: 2.4.1.69
            ExplorEnz - The Enzyme Database: 2.4.1.69
            ERGO genome analysis and discovery system: 2.4.1.69
            BRENDA, the Enzyme Database: 2.4.1.69
            CAS: 56093-23-3
///
ENTRY       EC 2.4.1.70                 Enzyme
NAME        poly(ribitol-phosphate) N-acetylglucosaminyl-transferase;
            UDP acetylglucosamine-poly(ribitol phosphate)
            acetylglucosaminyltransferase;
            uridine diphosphoacetylglucosamine-poly(ribitol phosphate)
            acetylglucosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:poly(ribitol-phosphate)
            N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine + poly(ribitol phosphate) = UDP +
            (N-acetyl-D-glucosaminyl)poly(ribitol phosphate) [RN:R02717 R06182]
ALL_REAC    R02717 R06182(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            poly(ribitol phosphate) [CPD:C00653]
PRODUCT     UDP [CPD:C00015];
            (N-acetyl-D-glucosaminyl)poly(ribitol phosphate)
COMMENT     Involved in the synthesis of teichoic acids.
REFERENCE   1
  AUTHORS   Nathenson, S.G., Ishimoto, N. and Strominger, J.L.
  TITLE     UDP-N-acetylglucosamine:polyribitol phosphate
            N-acetylglucosaminyltransferases from Staphylococcus aureus.
  JOURNAL   Methods Enzymol. 8 (1966) 426-429.
  ORGANISM  Staphylococcus aureus
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.70
            ExPASy - ENZYME nomenclature database: 2.4.1.70
            ExplorEnz - The Enzyme Database: 2.4.1.70
            ERGO genome analysis and discovery system: 2.4.1.70
            BRENDA, the Enzyme Database: 2.4.1.70
            CAS: 37277-71-7
///
ENTRY       EC 2.4.1.71                 Enzyme
NAME        arylamine glucosyltransferase;
            UDP glucose-arylamine glucosyltransferase;
            uridine diphosphoglucose-arylamine glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:arylamine N-D-glucosyltransferase
REACTION    UDP-glucose + an arylamine = UDP + an N-D-glucosylarylamine
            [RN:R02388]
ALL_REAC    R02388
SUBSTRATE   UDP-glucose [CPD:C00029];
            arylamine [CPD:C00292]
PRODUCT     UDP [CPD:C00015];
            N-D-glucosylarylamine [CPD:C03142]
REFERENCE   1
  AUTHORS   Frear, D.S.
  TITLE     Herbicide metabolism in plants. I. Purification and properties of
            UDP-glucose:arylamine N-glucosyl-transferase from soybean.
  JOURNAL   Phytochemistry 7 (1968) 381-390.
  ORGANISM  Glycine max [GN:egma]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.71
            ExPASy - ENZYME nomenclature database: 2.4.1.71
            ExplorEnz - The Enzyme Database: 2.4.1.71
            ERGO genome analysis and discovery system: 2.4.1.71
            BRENDA, the Enzyme Database: 2.4.1.71
            CAS: 37277-72-8
///
ENTRY       EC 2.4.1.72       Obsolete  Enzyme
NAME        Transferred to 2.4.2.24
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Transferred entry: now EC 2.4.2.24 1,4-beta-D-xylan synthase (EC
            2.4.1.72 created 1972, deleted 1976)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.72
            ExPASy - ENZYME nomenclature database: 2.4.1.72
            ExplorEnz - The Enzyme Database: 2.4.1.72
            ERGO genome analysis and discovery system: 2.4.1.72
            BRENDA, the Enzyme Database: 2.4.1.72
///
ENTRY       EC 2.4.1.73                 Enzyme
NAME        lipopolysaccharide glucosyltransferase II;
            uridine diphosphoglucose-galactosylpolysaccharide
            glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:galactosyl-lipopolysaccharide
            alpha-D-glucosyltransferase
REACTION    UDP-glucose + lipopolysaccharide = UDP +
            alpha-D-glucosyl-lipopolysaccharide [RN:R01995]
ALL_REAC    R01995
SUBSTRATE   UDP-glucose [CPD:C00029];
            lipopolysaccharide [CPD:C00338]
PRODUCT     UDP [CPD:C00015];
            alpha-D-glucosyl-lipopolysaccharide
COMMENT     Transfers glucosyl residues to the D-galactosyl-D-glucosyl
            side-chains in the partially completed core of lipopolysaccharides.
            cf. EC 2.4.1.44 (lipopolysaccharide 3-alpha-galactosyltransferase),
            EC 2.4.1.56 (lipopolysaccharide N-acetylglucosaminyltransferase) and
            EC 2.4.1.58 (lipopolysaccharide glucosyltransferase I).
REFERENCE   1  [PMID:5341482]
  AUTHORS   Edstrom RD, Heath EC.
  TITLE     The biosynthesis of cell wall lipopolysaccharide in Escherichia
            coli. VI. Enzymatic transfer of galactose, glucose,
            N-acetylglucosamine, and colitose into the polymer.
  JOURNAL   J. Biol. Chem. 242 (1967) 3581-8.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.73
            ExPASy - ENZYME nomenclature database: 2.4.1.73
            ExplorEnz - The Enzyme Database: 2.4.1.73
            ERGO genome analysis and discovery system: 2.4.1.73
            BRENDA, the Enzyme Database: 2.4.1.73
            CAS: 51004-27-4
///
ENTRY       EC 2.4.1.74                 Enzyme
NAME        glycosaminoglycan galactosyltransferase;
            uridine diphosphogalactose-mucopolysaccharide galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:glycosaminoglycan D-galactosyltransferase
REACTION    UDP-galactose + glycosaminoglycan = UDP +
            D-galactosylglycosaminoglycan [RN:R03981]
ALL_REAC    R03981
SUBSTRATE   UDP-galactose [CPD:C00052];
            glycosaminoglycan [CPD:C02545]
PRODUCT     UDP [CPD:C00015];
            D-galactosylglycosaminoglycan [CPD:C03942]
COMMENT     Involved in the biosynthesis of galactose-containing
            glycosaminoglycan of Dictyostelium discoideum.
REFERENCE   1
  AUTHORS   Sussman, M. and Osborn, M.J.
  TITLE     UDP-glucose polysaccharide transferase in the cellular slime mold
            Dictyostelium discoideum: appearance and dissappearance of activity
            during cell differentiation.
  JOURNAL   Proc. Natl. Acad. Sci. USA 52 (1964) 81-87.
  ORGANISM  Dictyostelium discoideum [GN:ddi]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.74
            ExPASy - ENZYME nomenclature database: 2.4.1.74
            ExplorEnz - The Enzyme Database: 2.4.1.74
            ERGO genome analysis and discovery system: 2.4.1.74
            BRENDA, the Enzyme Database: 2.4.1.74
            CAS: 51004-28-5
///
ENTRY       EC 2.4.1.75       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: insufficient evidence to conclude that this is a
            different enzyme from EC 2.4.1.43, polygalacturonate
            4-alpha-galacturonosyltransferase (EC 2.4.1.75 created 1976, deleted
            2005)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.75
            ExPASy - ENZYME nomenclature database: 2.4.1.75
            ExplorEnz - The Enzyme Database: 2.4.1.75
            ERGO genome analysis and discovery system: 2.4.1.75
            BRENDA, the Enzyme Database: 2.4.1.75
///
ENTRY       EC 2.4.1.76       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: UDP-glucuronate-bilirubin glucuronosyltransferase.
            Now included with EC 2.4.1.17, glucuronosyltransferase (EC 2.4.1.76
            created 1976, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.76
            ExPASy - ENZYME nomenclature database: 2.4.1.76
            ExplorEnz - The Enzyme Database: 2.4.1.76
            ERGO genome analysis and discovery system: 2.4.1.76
            BRENDA, the Enzyme Database: 2.4.1.76
///
ENTRY       EC 2.4.1.77       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: UDP-glucuronate-bilirubin-glucuronoside
            glucuronosyltransferase. Now included with EC 2.4.1.17,
            glucuronosyltransferase (EC 2.4.1.77 created 1976, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.77
            ExPASy - ENZYME nomenclature database: 2.4.1.77
            ExplorEnz - The Enzyme Database: 2.4.1.77
            ERGO genome analysis and discovery system: 2.4.1.77
            BRENDA, the Enzyme Database: 2.4.1.77
///
ENTRY       EC 2.4.1.78                 Enzyme
NAME        phosphopolyprenol glucosyltransferase;
            uridine diphosphoglucose-polyprenol monophosphate
            glucosyltransferase;
            UDP-glucose:polyprenol monophosphate glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:phosphopolyprenol D-glucosyltransferase
REACTION    UDP-glucose + polyprenyl phosphate = UDP +
            polyprenylphosphate-glucose [RN:R03190]
ALL_REAC    R03190
SUBSTRATE   UDP-glucose [CPD:C00029];
            polyprenyl phosphate [CPD:C01048]
PRODUCT     UDP [CPD:C00015];
            polyprenylphosphate-glucose [CPD:C03799]
COMMENT     Ficaprenyl phosphate is the best substrate; other polyprenols can
            also act as substrates, but more slowly.
REFERENCE   1  [PMID:4373050]
  AUTHORS   Jankowski W, Mankowski T, Chojnacki T.
  TITLE     Formation of polyprenol monophosphate glucose in Shigella flexneri.
  JOURNAL   Biochim. Biophys. Acta. 337 (1974) 153-62.
  ORGANISM  Shigella flexneri
GENES       GBE: GbCGDNIH1_0717
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.78
            ExPASy - ENZYME nomenclature database: 2.4.1.78
            ExplorEnz - The Enzyme Database: 2.4.1.78
            ERGO genome analysis and discovery system: 2.4.1.78
            BRENDA, the Enzyme Database: 2.4.1.78
            CAS: 55576-46-0
///
ENTRY       EC 2.4.1.79                 Enzyme
NAME        globotriaosylceramide 3-beta-N-acetylgalactosaminyltransferase;
            uridine
            diphosphoacetylgalactosamine-galactosylgalactosylglucosylceramide
            acetylgalactosaminyltransferase;
            globoside synthetase;
            UDP-N-acetylgalactosamine:globotriaosylceramide
            beta-3-N-acetylgalactosaminyltransferase;
            galactosylgalactosylglucosylceramide
            beta-D-acetylgalactosaminyltransferase;
            UDP-N-acetylgalactosamine:globotriaosylceramide
            beta1,3-N-acetylgalactosaminyltransferase;
            globoside synthase;
            galactosylgalactosylglucosylceramide
            beta-D-acetylgalactosaminyltransferase;
            UDP-N-acetyl-D-galactosamine:D-galactosyl-1,4-D-galactosyl-1,4-D-
            glucosylceramide beta-N-acetyl-D-galactosaminyltransferase;
            beta3GalNAc-T1;
            UDP-N-acetyl-D-galactosamine:alpha-D-galactosyl-(1->4)-beta-D-
            galactosyl-(1->4)-beta-D-glucosylceramide
            3III-beta-N-acetyl-D-galactosaminyltransferase;
            UDP-N-acetyl-D-galactosamine:alpha-D-galactosyl-(1->4)-beta-D-
            galactosyl-(1->4)-beta-D-glucosyl-(11)-ceramide
            3III-beta-N-acetyl-D-galactosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-galactosamine:alpha-D-galactosyl-(1->4)-beta-D-galact
            osyl-(1->4)-beta-D-glucosyl-(11)-ceramide
            III3-beta-N-acetyl-D-galactosaminyltransferase
REACTION    UDP-N-acetyl-D-galactosamine +
            alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
            (11)-ceramide = UDP +
            N-acetyl-beta-D-galactosaminyl-(1->3)-alpha-D-galactosyl-(1->4)-
            beta-D-galactosyl-(1->4)-beta-D-glucosyl-(11)-ceramide [RN:R05631
            R05962]
ALL_REAC    R05631 R05962(G)
SUBSTRATE   UDP-N-acetyl-D-galactosamine [CPD:C00203];
            alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
            (11)-ceramide
PRODUCT     UDP [CPD:C00015];
            N-acetyl-beta-D-galactosaminyl-(1->3)-alpha-D-galactosyl-(1->4)-
            beta-D-galactosyl-(1->4)-beta-D-glucosyl-(11)-ceramide
COMMENT     Globoside is a neutral glycosphingolipid in human erythrocytes and
            has blood-group-P-antigen activity [4]. The enzyme requires a
            divalent cation for activity, with Mn2+ required for maximal
            activity [3]. UDP-GalNAc is the only sugar donor that is used
            efficiently by the enzyme: UDP-Gal and UDP-GlcNAc result in very low
            enzyme activity [3]. Lactosylceramide, globoside and gangliosides
            GM3 and GD3 are not substrates [4]. For explanation of the
            superscripted '3' in the systematic name, see GL-5.3.4.
REFERENCE   1  [PMID:4632917]
  AUTHORS   Chien JL, Williams T, Basu S.
  TITLE     Biosynthesis of a globoside-type glycosphingolipid by a
            -N-acetylgalactosaminyltransferase from embryonic chicken brain.
  JOURNAL   J. Biol. Chem. 248 (1973) 1778-85.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:4433547]
  AUTHORS   Ishibashi T, Kijimoto S, Makita A.
  TITLE     Biosynthesis of globoside and Forssman hapten from
            trihexosylceramide and properties of
            beta-N-acetyl-galactosaminyltransferase of guinea pig kidney.
  JOURNAL   Biochim. Biophys. Acta. 337 (1974) 92-106.
  ORGANISM  guinea pig
REFERENCE   3  [PMID:6425294]
  AUTHORS   Taniguchi N, Makita A.
  TITLE     Purification and characterization of UDP-N-acetylgalactosamine:
            globotriaosylceramide beta-3-N-acetylgalactosaminyltransferase, a
            synthase of human blood group P antigen, from canine spleen.
  JOURNAL   J. Biol. Chem. 259 (1984) 5637-42.
  ORGANISM  dog [GN:cfa]
REFERENCE   4  [PMID:10993897]
  AUTHORS   Okajima T, Nakamura Y, Uchikawa M, Haslam DB, Numata SI, Furukawa K,
            Urano T, Furukawa K.
  TITLE     Expression cloning of human globoside synthase cDNAs. Identification
            of beta 3Gal-T3 as UDP-N-acetylgalactosamine:globotriaosylceramide
            beta 1,3-N-acetylgalactosaminyltransferase.
  JOURNAL   J. Biol. Chem. 275 (2000) 40498-503.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00603  Glycosphingolipid biosynthesis - globoseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K00719  galactosylgalactosylglucosylceramide
                        beta-D-acetylgalactosaminyltransferase
GENES       HSA: 8706(B3GALNT1)
            PTR: 460824(B3GALNT1)
            MMU: 26879(B3galnt1)
            RNO: 310508(B3galt3)
            BTA: 767844(B3GALNT1)
            SSC: 397634(B3GALT3)
            GGA: 425010(B3GALNT1)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.79
            ExPASy - ENZYME nomenclature database: 2.4.1.79
            ExplorEnz - The Enzyme Database: 2.4.1.79
            ERGO genome analysis and discovery system: 2.4.1.79
            BRENDA, the Enzyme Database: 2.4.1.79
            CAS: 62213-46-1
///
ENTRY       EC 2.4.1.80                 Enzyme
NAME        ceramide glucosyltransferase;
            UDP-glucose:ceramide glucosyltransferase;
            ceramide:UDP-Glc glucosyltransferase;
            uridine diphosphoglucose-ceramide glucosyltransferase;
            ceramide:UDP-glucose glucosyltransferase;
            glucosylceramide synthase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:N-acylsphingosine D-glucosyltransferase
REACTION    UDP-glucose + an N-acylsphingosine = UDP + a
            D-glucosyl-N-acylsphingosine [RN:R01497 R06275]
ALL_REAC    R01497 R06275(G)
SUBSTRATE   UDP-glucose [CPD:C00029];
            N-acylsphingosine [CPD:C00195]
PRODUCT     UDP [CPD:C00015];
            D-glucosyl-N-acylsphingosine [CPD:C01190]
COMMENT     Sphingosine and dihydrosphingosine can also act as acceptors;
            CDP-glucose can act as donor.
REFERENCE   1  [PMID:4631392]
  AUTHORS   Basu S, Kaufman B, Roseman S.
  TITLE     Enzymatic synthesis of glucocerebroside by a glucosyltransferase
            from embryonic chicken brain.
  JOURNAL   J. Biol. Chem. 248 (1973) 1388-94.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00600  Sphingolipid metabolism
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K00720  ceramide glucosyltransferase
GENES       HSA: 7357(UGCG)
            PTR: 464660(UGCG)
            RNO: 83626(Ugcg)
            CFA: 481666(UGCG)
            BTA: 514357(MGC142606)
            GGA: 427335(UGCG)
            XLA: 399204(Ugcg) 495444(LOC495444)
            XTR: 548887(LOC548887)
            DRE: 553944(ugcg)
            SPU: 591961(LOC591961)
            DME: Dmel_CG6437
            CEL: F59G1.1(cgt-3)
            PIC: PICST_34303(CGT1)
            AFM: AFUA_5G09550
            AOR: AO090020000582
            CNE: CNH02280
            UMA: UM04496.1
            YPA: YPA_1365
            YPS: YPTB1976
            XCC: XCC2437
            XCB: XC_1675
            XCV: XCV2767
            XAC: XAC2568
            REU: Reut_B4900
            REH: H16_B2171
            RME: Rmet_3407
            BMA: BMA0578 BMA3350
            BXE: Bxe_A2063 Bxe_A2068 Bxe_B0384
            BUR: Bcep18194_A4282 Bcep18194_B0471
            BAM: Bamb_1049
            BPS: BPSL0293 BPSL2399
            BPM: BURPS1710b_0488 BURPS1710b_2860
            BTE: BTH_I0264 BTH_I1766
            GSU: GSU0697
            GME: Gmet_2815
            GUR: Gura_1031
            MXA: MXAN_4793
            MLO: mlr5650
            ATU: Atu1808(ugcG)
            ATC: AGR_C_3323
            RSP: RSP_2152
            ZMO: ZMO0972
            GOX: GOX0615
            GBE: GbCGDNIH1_2402
            MAG: amb3484
            ABA: Acid345_0723 Acid345_0724
            SSA: SSA_1324
            FNU: FN1845
            SYN: slr0813
            TEL: tll0064
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.80
            ExPASy - ENZYME nomenclature database: 2.4.1.80
            ExplorEnz - The Enzyme Database: 2.4.1.80
            ERGO genome analysis and discovery system: 2.4.1.80
            BRENDA, the Enzyme Database: 2.4.1.80
            CAS: 37237-44-8
///
ENTRY       EC 2.4.1.81                 Enzyme
NAME        flavone 7-O-beta-glucosyltransferase;
            UDP-glucose-apigenin beta-glucosyltransferase;
            UDP-glucose-luteolin beta-D-glucosyltransferase;
            uridine diphosphoglucose-luteolin glucosyltransferase;
            uridine diphosphoglucose-apigenin 7-O-glucosyltransferase;
            UDP-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:5,7,3',4'-tetrahydroxyflavone
            7-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + 5,7,3',4'-tetrahydroxyflavone = UDP +
            7-O-beta-D-glucosyl-5,7,3',4'-tetrahydroxyflavone [RN:R03588]
ALL_REAC    R03588;
            (other) R03574
SUBSTRATE   UDP-glucose [CPD:C00029];
            5,7,3',4'-tetrahydroxyflavone [CPD:C01514]
PRODUCT     UDP [CPD:C00015];
            7-O-beta-D-glucosyl-5,7,3',4'-tetrahydroxyflavone [CPD:C03951]
COMMENT     A number of flavones, flavanones and flavonols can function as
            acceptors. Different from EC 2.4.1.91 (flavonol
            3-O-glucosyltransferase).
REFERENCE   1  [PMID:5058406]
  AUTHORS   Sutter A, Ortmann R, Grisebach H.
  TITLE     Purification and properties of an enzyme from cell suspension
            cultures of parsley catalyzing the transfer of D-glucose from
            UDP-D-glucose to flavonoids.
  JOURNAL   Biochim. Biophys. Acta. 258 (1972) 71-87.
  ORGANISM  Petroselinum hortense
PATHWAY     PATH: map00941  Flavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.81
            ExPASy - ENZYME nomenclature database: 2.4.1.81
            ExplorEnz - The Enzyme Database: 2.4.1.81
            ERGO genome analysis and discovery system: 2.4.1.81
            BRENDA, the Enzyme Database: 2.4.1.81
            CAS: 37332-50-6
///
ENTRY       EC 2.4.1.82                 Enzyme
NAME        galactinol---sucrose galactosyltransferase;
            1-alpha-D-galactosyl-myo-inositol:sucrose
            6-alpha-D-galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     alpha-D-galactosyl-(1->3)-myo-inositol:sucrose
            6-alpha-D-galactosyltransferase
REACTION    alpha-D-galactosyl-(1->3)-1D-myo-inositol + sucrose = myo-inositol +
            raffinose [RN:R02411 R06071]
ALL_REAC    R02411 R06071(G)
SUBSTRATE   alpha-D-galactosyl-(1->3)-1D-myo-inositol;
            sucrose [CPD:C00089]
PRODUCT     myo-inositol [CPD:C00137];
            raffinose [CPD:C00492]
COMMENT     4-Nitrophenyl alpha-D-galactopyranoside can also act as donor. The
            enzyme also catalyses an exchange reaction between raffinose and
            sucrose (cf. EC 2.4.1.123, inositol 3-alpha-galactosyltransferase).
REFERENCE   1  [PMID:4774118]
  AUTHORS   Lehle L, Tanner W.
  TITLE     The function of myo-inositol in the biosynthesis of raffinose.
            Purification and characterization of galactinol:sucrose
            6-galactosyltransferase from Vicia faba seeds.
  JOURNAL   Eur. J. Biochem. 38 (1973) 103-10.
  ORGANISM  Vicia faba
REFERENCE   2  [PMID:5491608]
  AUTHORS   Lehle L, Tanner W, Kandler O.
  TITLE     Myo-inositol, a cofactor in the biosynthesis of raffinose.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 351 (1970) 1494-8.
  ORGANISM  Vicia faba
PATHWAY     PATH: map00052  Galactose metabolism
ORTHOLOGY   KO: K06617  raffinose synthase
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.82
            ExPASy - ENZYME nomenclature database: 2.4.1.82
            ExplorEnz - The Enzyme Database: 2.4.1.82
            ERGO genome analysis and discovery system: 2.4.1.82
            BRENDA, the Enzyme Database: 2.4.1.82
            CAS: 62213-45-0
///
ENTRY       EC 2.4.1.83                 Enzyme
NAME        dolichyl-phosphate beta-D-mannosyltransferase;
            GDP-Man:DolP mannosyltransferase;
            dolichyl mannosyl phosphate synthase;
            dolichyl-phospho-mannose synthase;
            GDP-mannose:dolichyl-phosphate mannosyltransferase;
            guanosine diphosphomannose-dolichol phosphate mannosyltransferase;
            dolichol phosphate mannose synthase;
            dolichyl phosphate mannosyltransferase;
            dolichyl-phosphate mannose synthase;
            GDP-mannose-dolichol phosphate mannosyltransferase;
            GDP-mannose-dolichylmonophosphate mannosyltransferase;
            mannosylphosphodolichol synthase;
            mannosylphosphoryldolichol synthase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-mannose:dolichyl-phosphate beta-D-mannosyltransferase
REACTION    GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl
            phosphate [RN:R01009]
ALL_REAC    R01009
SUBSTRATE   GDP-mannose [CPD:C00096];
            dolichyl phosphate [CPD:C00110]
PRODUCT     GDP [CPD:C00035];
            dolichyl D-mannosyl phosphate [CPD:C03862]
COMMENT     Acts only on long-chain polyprenyl phosphates and
            alpha-dihydropolyprenyl phosphates that are larger than C35.
REFERENCE   1  [PMID:6989607]
  AUTHORS   Babczinski P, Haselbeck A, Tanner W.
  TITLE     Yeast mannosyl transferases requiring dolichyl phosphate and
            dolichyl phosphate mannose as substrate. Partial purification and
            characterization of the solubilized enzyme.
  JOURNAL   Eur. J. Biochem. 105 (1980) 509-15.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:4726855]
  AUTHORS   Bretthauer RK, Wu S, Irwin WE.
  TITLE     Enzymatic transfer of mannose from guanosine diphosphate mannose to
            dolichol phosphate in yeast (Hansenula holstii). A possible step in
            mannan synthesis.
  JOURNAL   Biochim. Biophys. Acta. 304 (1973) 736-47.
  ORGANISM  Hansenula holstii
REFERENCE   3  [PMID:2659345]
  AUTHORS   Haselbeck A.
  TITLE     Purification of GDP mannose:dolichyl-phosphate
            O-beta-D-mannosyltransferase from Saccharomyces cerevisiae.
  JOURNAL   Eur. J. Biochem. 181 (1989) 663-8.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4  [PMID:6445267]
  AUTHORS   Palamarczyk G, Lehle L, Mankowski T, Chojnacki T, Tanner W.
  TITLE     Specificity of solubilized yeast glycosyl transferases for
            polyprenyl derivatives.
  JOURNAL   Eur. J. Biochem. 105 (1980) 517-23.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   5  [PMID:4655455]
  AUTHORS   Richards JB, Hemming FW.
  TITLE     The transfer of mannose from guanosine diphosphate mannose to
            dolichol phosphate and protein by pig liver endoplasmic reticulum.
  JOURNAL   Biochem. J. 130 (1972) 77-93.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
ORTHOLOGY   KO: K00721  dolichol-phosphate mannosyltransferase
GENES       HSA: 8813(DPM1)
            MMU: 13480(Dpm1)
            RNO: 296394(Dpm1_predicted)
            CFA: 477264(DPM1)
            BTA: 534097(MGC140708)
            GGA: 419349(DPM1)
            XTR: 496884(dpm1)
            DRE: 445202(dpm1)
            SPU: 589166(LOC589166)
            DME: Dmel_CG10166
            CEL: Y66H1A.2
            ATH: AT1G20575
            OSA: 4334626
            CME: CMS169C
            SCE: YPR183W(DPM1)
            AGO: AGOS_AEL275C
            PIC: PICST_87591(DPM1)
            CAL: CaO19_12539(CaO19.12539)
            CGR: CAGL0G09955g
            SPO: SPAC31G5.16c(dpm1)
            ANI: AN4947.2
            AFM: AFUA_3G10400
            AOR: AO090003000589
            CNE: CNB02480
            ECU: ECU04_1060
            DDI: DDB_0231708(dgtB)
            PFA: PF11_0427
            CHO: Chro.50175
            TAN: TA14850
            TPV: TP02_0741
            TBR: Tb10.70.2610
            TCR: 506581.10 508169.60
            LMA: LmjF36.0220
            EHI: 167.t00003
            XFA: XF2278
            XFT: PD1313(dpm1)
            XCC: XCC3854(dpm1)
            XCV: XCV4022
            XAC: XAC3909(dpm1)
            XOO: XOO0501(dpm1)
            XOM: XOO_0468(XOO0468)
            PSP: PSPPH_0960
            CVI: CV_0749
            BUR: Bcep18194_A5161
            BAM: Bamb_1798
            POL: Bpro_4007
            HAR: HEAR1604
            NET: Neut_0464
            NMU: Nmul_A0277 Nmul_A1764
            GUR: Gura_1919
            PCA: Pcar_1271
            PPD: Ppro_2422
            DVU: DVU2052
            DDE: Dde_1596
            ADE: Adeh_2624
            AFW: Anae109_2588
            MLO: mll5672
            RET: RHE_CH02756
            RLE: RL0280 RL3210 pRL110390
            BJA: bll3112
            BRA: BRADO2877
            BBT: BBta_5297
            RPA: RPA3784 RPA4057
            RPB: RPB_3658
            RPC: RPC_1645
            RPD: RPD_1800
            RPE: RPE_1674 RPE_2726
            NWI: Nwi_2195
            NHA: Nham_2598
            XAU: Xaut_3310
            RDE: RD1_0575
            ZMO: ZMO0503(dpm1)
            NAR: Saro_2663
            GOX: GOX0129 GOX1109
            ACR: Acry_1904
            RRU: Rru_A1005
            MGM: Mmc1_0613 Mmc1_2869
            ABA: Acid345_2849
            SUS: Acid_4359
            BSU: BG13230(ykcC)
            BAN: BA5684
            BAR: GBAA5684
            BAA: BA_0542
            BAT: BAS5287
            BCZ: BCZK5129
            BTK: BT9727_5112
            BLI: BL01936
            BLD: BLi04189(ykcC)
            GKA: GK2052
            LMO: lmo0933
            SSA: SSA_0425
            LCA: LSEI_0708
            CAC: CAC0194 CAC3661
            DSY: DSY2282
            SWO: Swol_2157
            MTA: Moth_2359
            MSM: MSMEG_3859
            MVA: Mvan_3418
            MGI: Mflv_3118
            MMC: Mmcs_2503
            MKM: Mkms_2548
            MJL: Mjls_2540
            CJK: jk0935(ppm1)
            RHA: RHA1_ro00145
            SCO: SCO4658(SCD40A.04)
            SMA: SAV3293(dpm)
            ART: Arth_2187
            NCA: Noca_1562 Noca_1604 Noca_2667
            TFU: Tfu_1850
            FRA: Francci3_0964 Francci3_2271
            FAL: FRAAL1592 FRAAL5056 FRAAL6118
            ACE: Acel_1211
            SEN: SACE_0180 SACE_0181 SACE_1412(dmt) SACE_2289
            STP: Strop_1759
            FNU: FN1094
            RBA: RB12831 RB13211 RB289 RB6305 RB8905
            LIL: LA3071
            LIC: LIC11024
            SYN: sll1004 sll1540(dpm1) slr1943(dpm1)
            SYC: syc1355_d
            SYF: Synpcc7942_0150
            CYA: CYA_0955 CYA_1073
            CYB: CYB_0176 CYB_0997
            TEL: tlr2019
            GVI: gll0700 gll3331 glr1357
            ANA: all0143 all2770 all4126 all5118 alr3380
            AVA: Ava_0022 Ava_0778 Ava_1512 Ava_2346 Ava_3351 Ava_3397
            PMA: Pro0380(wcaA)
            PMM: PMM1200
            PMB: A9601_17261
            PMC: P9515_17011
            PMF: P9303_23431 P9303_25741 P9303_26101
            PMG: P9301_17141
            PME: NATL1_19621
            TER: Tery_0804 Tery_3784
            PGI: PG0334
            FJO: Fjoh_0554
            CCH: Cag_0345 Cag_0506 Cag_0605
            CPH: Cpha266_0221
            PVI: Cvib_1617
            PLT: Plut_1974
            AAE: aq_1899(dmt)
            MJA: MJ0544 MJ1222
            MMP: MMP0590 MMP1170
            MAC: MA4330
            MBA: Mbar_A1132
            MMA: MM_1026 MM_1147
            MBU: Mbur_1615
            MEM: Memar_1468
            MBN: Mboo_2450
            MSI: Msm_1623
            MKA: MK0880
            HWA: HQ2694A(gtl)
            NPH: NP4658A(gtl_1)
            TAC: Ta0760
            TVO: TVN0854
            PTO: PTO1478
            PHO: PH0051
            PAB: PAB2307
            PFU: PF0058
            TKO: TK1909
            APE: APE_0426.1
            SMR: Smar_0112
            SSO: SSO3241
            STO: ST2337
            SAI: Saci_1011
            PAI: PAE1555
            PIS: Pisl_1623
            PCL: Pcal_0526
            PAS: Pars_0656
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.83
            ExPASy - ENZYME nomenclature database: 2.4.1.83
            ExplorEnz - The Enzyme Database: 2.4.1.83
            ERGO genome analysis and discovery system: 2.4.1.83
            BRENDA, the Enzyme Database: 2.4.1.83
            CAS: 62213-44-9
///
ENTRY       EC 2.4.1.84       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: UDP-glucuronate-1,2-diacylglycerol
            glucuronosyltransferase. Now included with EC 2.4.1.17,
            glucuronosyltransferase (EC 2.4.1.84 created 1976, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.84
            ExPASy - ENZYME nomenclature database: 2.4.1.84
            ExplorEnz - The Enzyme Database: 2.4.1.84
            ERGO genome analysis and discovery system: 2.4.1.84
            BRENDA, the Enzyme Database: 2.4.1.84
///
ENTRY       EC 2.4.1.85                 Enzyme
NAME        cyanohydrin beta-glucosyltransferase;
            uridine diphosphoglucose-p-hydroxymandelonitrile
            glucosyltransferase;
            UDP-glucose-p-hydroxymandelonitrile glucosyltransferase;
            uridine diphosphoglucose-cyanohydrin glucosyltransferase;
            uridine diphosphoglucose:aldehyde cyanohydrin
            beta-glucosyltransferase;
            UDP-glucose:(S)-4-hydroxymandelonitrile beta-D-glucosyltransferase;
            UGT85B1;
            UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-D-glucose:(S)-4-hydroxymandelonitrile beta-D-glucosyltransferase
REACTION    UDP-D-glucose + (S)-4-hydroxymandelonitrile = UDP +
            (S)-4-hydroxymandelonitrile beta-D-glucoside [RN:R04296]
ALL_REAC    R04296;
            (other) R04948
SUBSTRATE   UDP-D-glucose [CPD:C00029];
            (S)-4-hydroxymandelonitrile [CPD:C03742]
PRODUCT     UDP [CPD:C00015];
            (S)-4-hydroxymandelonitrile beta-D-glucoside [CPD:C05143]
COMMENT     Acts on a wide range of substrates in vitro, including cyanohydrins,
            terpenoids, phenolics, hexanol derivatives and plant hormones, in a
            regiospecific manner [3]. This enzyme is involved in the
            biosynthesis of the cyanogenic glucoside dhurrin in sorghum, along
            with EC 1.14.13.41, tyrosine N-monooxygenase and EC 1.14.13.68,
            4-hydroxyphenylacetaldehyde oxime monooxygenase. This reaction
            prevents the disocciation and release of toxic hydrogen cyanide [3].
REFERENCE   1  [PMID:4416442]
  AUTHORS   Reay PF, Conn EE.
  TITLE     The purification and properties of a uridine diphosphate glucose:
            aldehyde cyanohydrin beta-glucosyltransferase from sorghum
            seedlings.
  JOURNAL   J. Biol. Chem. 249 (1974) 5826-30.
  ORGANISM  Sorghum bicolor [GN:esbi]
REFERENCE   2  [PMID:10585420]
  AUTHORS   Jones PR, Moller BL, Hoj PB.
  TITLE     The UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase that
            catalyzes the last step in synthesis of the cyanogenic glucoside
            dhurrin in Sorghum bicolor. Isolation, cloning, heterologous
            expression, and substrate specificity.
  JOURNAL   J. Biol. Chem. 274 (1999) 35483-91.
  ORGANISM  Sorghum bicolor [GN:esbi]
REFERENCE   3  [PMID:12946413]
  AUTHORS   Hansen KS, Kristensen C, Tattersall DB, Jones PR, Olsen CE, Bak S,
            Moller BL.
  TITLE     The in vitro substrate regiospecificity of recombinant UGT85B1, the
            cyanohydrin glucosyltransferase from Sorghum bicolor.
  JOURNAL   Phytochemistry. 64 (2003) 143-51.
  ORGANISM  Sorghum bicolor [GN:esbi]
REFERENCE   4  [PMID:12114576]
  AUTHORS   Busk PK, Moller BL.
  TITLE     Dhurrin synthesis in sorghum is regulated at the transcriptional
            level and induced by nitrogen fertilization in older plants.
  JOURNAL   Plant. Physiol. 129 (2002) 1222-31.
  ORGANISM  Sorghum bicolor [GN:esbi]
REFERENCE   5  [PMID:15665094]
  AUTHORS   Kristensen C, Morant M, Olsen CE, Ekstrom CT, Galbraith DW, Moller
            BL, Bak S.
  TITLE     Metabolic engineering of dhurrin in transgenic Arabidopsis plants
            with marginal inadvertent effects on the metabolome and
            transcriptome.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 1779-84.
  ORGANISM  Sorghum bicolor [GN:esbi]
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00460  Cyanoamino acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.85
            ExPASy - ENZYME nomenclature database: 2.4.1.85
            ExplorEnz - The Enzyme Database: 2.4.1.85
            ERGO genome analysis and discovery system: 2.4.1.85
            BRENDA, the Enzyme Database: 2.4.1.85
            CAS: 55354-52-4
///
ENTRY       EC 2.4.1.86                 Enzyme
NAME        glucosaminylgalactosylglucosylceramide beta-galactosyltransferase;
            uridine
            diphosphogalactose-acetyl-glucosaminylgalactosylglucosylceramide
            galactosyltransferase;
            GalT-4;
            paragloboside synthase;
            glucosaminylgalactosylglucosylceramide 4-beta-galactosyltransferase;
            lactotriaosylceramide 4-beta-galactosyltransferase;
            UDP-galactose:N-acetyl-D-glucosaminyl-1,3-D-galactosyl-1,4-D-
            glucosylceramide beta-D-galactosyltransferase;
            UDP-Gal:LcOse3Cer(beta 1-4)galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-
            (1->4)-beta-D-glucosylceramide 3-beta-D-galactosyltransferase
REACTION    UDP-galactose +
            N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-
            glucosyl-(11)-ceramide = UDP +
            beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
            galactosyl-(1->4)-beta-D-glucosyl-(11)-ceramide [RN:R04610 R06006]
ALL_REAC    R04610 R06006(G)
SUBSTRATE   UDP-galactose [CPD:C00052];
            N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-
            glucosyl-(11)-ceramide
PRODUCT     UDP [CPD:C00015];
            beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
            galactosyl-(1->4)-beta-D-glucosyl-(11)-ceramide
REFERENCE   1  [PMID:4335001]
  AUTHORS   Basu M, Basu S.
  TITLE     Enzymatic synthesis of a tetraglycosylceramide by a
            galactosyltransferase from rabbit bone marrow.
  JOURNAL   J. Biol. Chem. 247 (1972) 1489-95.
  ORGANISM  rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.86
            ExPASy - ENZYME nomenclature database: 2.4.1.86
            ExplorEnz - The Enzyme Database: 2.4.1.86
            ERGO genome analysis and discovery system: 2.4.1.86
            BRENDA, the Enzyme Database: 2.4.1.86
            CAS: 9073-46-5
///
ENTRY       EC 2.4.1.87                 Enzyme
NAME        N-acetyllactosaminide 3-alpha-galactosyltransferase;
            alpha-galactosyltransferase;
            UDP-Gal:beta-D-Gal(1,4)-D-GlcNAc alpha(1,3)-galactosyltransferase;
            UDP-Gal:N-acetyllactosaminide alpha(1,3)-galactosyltransferase;
            UDP-Gal:N-acetyllactosaminide alpha-1,3-D-galactosyltransferase;
            UDP-Gal:Galbeta1->4GlcNAc-R alpha1->3-galactosyltransferase;
            UDP-galactose-acetyllactosamine alpha-D-galactosyltransferase;
            UDPgalactose:beta-D-galactosyl-beta-1,4-N-acetyl-D-glucosaminyl-
            glycopeptide alpha-1,3-D-galactosyltransferase;
            glucosaminylglycopeptide alpha-1,3-galactosyltransferase;
            uridine diphosphogalactose-acetyllactosamine
            alpha1->3-galactosyltransferase;
            uridine diphosphogalactose-acetyllactosamine galactosyltransferase;
            uridine
            diphosphogalactose-
            galactosylacetylglucosaminylgalactosylglucosylceramide
            galactosyltransferase;
            beta-D-galactosyl-N-acetylglucosaminylglycopeptide
            alpha-1,3-galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:N-acetyllactosaminide 3-alpha-D-galactosyltransferase
REACTION    UDP-galactose +
            beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R = UDP +
            alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-
            acetylglucosaminyl-R [RN:R02791]
ALL_REAC    R02791 > R04531 R04605 R05978(G) R06145(G) R06169(G)
SUBSTRATE   UDP-galactose [CPD:C00052];
            beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R [CPD:C00694]
PRODUCT     UDP [CPD:C00015];
            alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-
            acetylglucosaminyl-R [CPD:C04855]
COMMENT     Acts on beta-galactosyl-1,4-N-acetylglucosaminyl termini on
            asialo-alpha1-acid glycoprotein and N-acetyllactosamine
            (beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine), but not on
            2'-fucosylated-N-acetyllactosamine. The non-reducing terminal
            N-acetyllactosamine residues of glycoproteins can also act as
            acceptor. Now includes EC 2.4.1.124 and EC 2.4.1.151.
REFERENCE   1  [PMID:4632915]
  AUTHORS   Basu M, Basu S.
  TITLE     Enzymatic synthesis of a blood group B-related pentaglycosylceramide
            by an alpha-galactosyltransferase from rabbit bone marrow.
  JOURNAL   J. Biol. Chem. 248 (1973) 1700-6.
  ORGANISM  rabbit
REFERENCE   2  [PMID:3932335]
  AUTHORS   Blanken WM, Van den Eijnden DH.
  TITLE     Biosynthesis of terminal Gal alpha 1----3Gal beta 1----4GlcNAc-R
            oligosaccharide sequences on glycoconjugates. Purification and
            acceptor specificity of a UDP-Gal:N-acetyllactosaminide alpha
            1----3-galactosyltransferase from calf thymus.
  JOURNAL   J. Biol. Chem. 260 (1985) 12927-34.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:6787040]
  AUTHORS   Blake DA, Goldstein IJ.
  TITLE     An alpha-D-galactosyltransferase activity in Ehrlich ascites tumor
            cells. Biosynthesis and characterization of a trisaccharide
            (alpha-D-galactose-(1 goes to 3)-N-acetyllactosamine).
  JOURNAL   J. Biol. Chem. 256 (1981) 5387-93.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map00601  Glycosphingolipid biosynthesis - lactoseries
            PATH: map00602  Glycosphingolipid biosynthesis - neo-lactoseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K00743  N-acetyllactosaminide 3-alpha-galactosyltransferase
GENES       MMU: 14594(Ggta1)
            RNO: 246766(Ggta1)
            CFA: 491357(LOC491357)
            BTA: 281780(GGTA1)
            SSC: 396733(GGTA1)
            AAE: aq_516(mtfC)
            AFU: AF1728
STRUCTURES  PDB: 2JCF  2JCK  2JCL  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.87
            ExPASy - ENZYME nomenclature database: 2.4.1.87
            ExplorEnz - The Enzyme Database: 2.4.1.87
            ERGO genome analysis and discovery system: 2.4.1.87
            BRENDA, the Enzyme Database: 2.4.1.87
            CAS: 128449-51-4
///
ENTRY       EC 2.4.1.88                 Enzyme
NAME        globoside alpha-N-acetylgalactosaminyltransferase;
            uridine diphosphoacetylgalactosamine-globoside
            alpha-acetylgalactosaminyltransferase;
            Forssman synthase;
            globoside acetylgalactosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-galactosamine:N-acetyl-D-galactosaminyl-1,3-D-galacto
            syl-1,4-D-galactosyl-1,4-D-glucosylceramide
            alpha-N-acetyl-D-galactosaminyltransferase
REACTION    UDP-N-acetyl-D-galactosamine +
            N-acetyl-D-galactosaminyl-1,3-D-galactosyl-1,4-D-galactosyl-1,4-D-
            glucosylceramide = UDP +
            N-acetyl-D-galactosaminyl-N-acetyl-D-galactosaminyl-1,3-D-
            galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide [RN:R04182
            R05965]
ALL_REAC    R04182 R05965(G)
SUBSTRATE   UDP-N-acetyl-D-galactosamine [CPD:C00203];
            N-acetyl-D-galactosaminyl-1,3-D-galactosyl-1,4-D-galactosyl-1,4-D-
            glucosylceramide [CPD:C03272]
PRODUCT     UDP [CPD:C00015];
            N-acetyl-D-galactosaminyl-N-acetyl-D-galactosaminyl-1,3-D-
            galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide [CPD:C04925]
REFERENCE   1  [PMID:4823436]
  AUTHORS   Kijimoto S, Ishibashi T, Makita A.
  TITLE     Biosynthesis of Forssman hapten from globoside by
            alpha-N-acetylgalactosaminyltransferase of guinea pig tissues.
  JOURNAL   Biochem. Biophys. Res. Commun. 56 (1974) 177-84.
  ORGANISM  guinea pig
PATHWAY     PATH: map00603  Glycosphingolipid biosynthesis - globoseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K00722  globoside alpha-N-acetylgalactosaminyltransferase
GENES       HSA: 26301(GBGT1)
            PTR: 464823(GBGT1)
            MMU: 227671(Gbgt1)
            CFA: 403833(GBGT1)
            BTA: 618517(MGC140602)
            GGA: 417163(RCJMB04_5m5)
            DRE: 387303(zgc:66417)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.88
            ExPASy - ENZYME nomenclature database: 2.4.1.88
            ExplorEnz - The Enzyme Database: 2.4.1.88
            ERGO genome analysis and discovery system: 2.4.1.88
            BRENDA, the Enzyme Database: 2.4.1.88
            CAS: 52037-97-5
///
ENTRY       EC 2.4.1.89       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: Galactosylglucosaminylgalactosylglucosylceramide
            alpha-L-fucosyltransferase - now included with EC 2.4.1.69
            galactoside 2-alpha-L-fucosyltransferase (EC 2.4.1.89 created 1976,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.89
            ExPASy - ENZYME nomenclature database: 2.4.1.89
            ExplorEnz - The Enzyme Database: 2.4.1.89
            ERGO genome analysis and discovery system: 2.4.1.89
            BRENDA, the Enzyme Database: 2.4.1.89
///
ENTRY       EC 2.4.1.90                 Enzyme
NAME        N-acetyllactosamine synthase;
            UDP-galactose---N-acetylglucosamine beta-D-galactosyltransferase;
            uridine diphosphogalactose-acetylglucosamine galactosyltransferase;
            beta-1,4-galactosyltransferase;
            acetyllactosamine synthetase;
            lactosamine synthase;
            lactosamine synthetase;
            lactose synthetase A protein;
            N-acetyllactosamine synthetase;
            UDP-galactose N-acetylglucosamine beta-4-galactosyltransferase;
            UDP-galactose-acetylglucosamine galactosyltransferase;
            UDP-galactose-N-acetylglucosamine beta-1,4-galactosyltransferase;
            UDP-galactose-N-acetylglucosamine galactosyltransferase;
            beta1-4-galactosyltransferase;
            UDP-Gal:N-acetylglucosamine beta1-4-galactosyltransferase;
            beta1-4GalT;
            NAL synthetase;
            UDP-beta-1,4-galactosyltransferase;
            Gal-T;
            UDP-galactose:N-acetylglucosaminide beta1-4-galactosyltransferase;
            UDPgalactose:N-acetylglucosaminyl(beta1-4)galactosyltransferase;
            beta-N-acetylglucosaminide beta1-4-galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:N-acetyl-D-glucosamine 4-beta-D-galactosyltransferase
REACTION    UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine
            [RN:R01205 R06055]
ALL_REAC    R01205 R06055(G)
SUBSTRATE   UDP-galactose [CPD:C00052];
            N-acetyl-D-glucosamine [CPD:C00140]
PRODUCT     UDP [CPD:C00015];
            N-acetyllactosamine [CPD:C00611]
COMMENT     The reaction is catalysed by a component of EC 2.4.1.22 (lactose
            synthase), which is identical with EC 2.4.1.38
            (beta-N-acetylglucosaminyl-glycopeptide
            beta-1,4-galactosyltransferase), and by an enzyme from the Golgi
            apparatus of animal tissues. Formerly listed also as EC 2.4.1.98.
REFERENCE   1  [PMID:99178]
  AUTHORS   Deshmukh DS, Bear WD, Soifer D.
  TITLE     Isolation and characterization of an enriched Golgi fraction from
            rat brain.
  JOURNAL   Biochim. Biophys. Acta. 542 (1978) 284-95.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4631039]
  AUTHORS   Helting T, Erbing B.
  TITLE     Galactosyltransfer in mouse mastocytoma: purification and properties
            of N-acetyllactosamine synthetase.
  JOURNAL   Biochim. Biophys. Acta. 293 (1973) 94-104.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:812340]
  AUTHORS   Hill RL, Brew K.
  TITLE     Lactose synthetase.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 43 (1975) 411-90.
REFERENCE   4  [PMID:6201486]
  AUTHORS   Humphreys-Beher MG.
  TITLE     Isolation and characterization of UDP-galactose:N-acetylglucosamine
            4 beta-galactosyltransferase activity induced in rat parotid glands
            treated with isoproterenol.
  JOURNAL   J. Biol. Chem. 259 (1984) 5797-802.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:4392041]
  AUTHORS   Schachter H, Jabbal I, Hudgin RL, Pinteric L, McGuire EJ, Roseman S.
  TITLE     Intracellular localization of liver sugar nucleotide glycoprotein
            glycosyltransferases in a Golgi-rich fraction.
  JOURNAL   J. Biol. Chem. 245 (1970) 1090-100.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K00723  N-acetyllactosamine synthase
GENES       HSA: 2683(B4GALT1) 8702(B4GALT4) 8703(B4GALT3) 8704(B4GALT2)
            PTR: 457451(B4GALT3)
            MMU: 14595(B4galt1) 53418(B4galt2) 56375(B4galt4) 57370(B4galt3)
            RNO: 24390(B4galt1_predicted) 313536(B4galt2_predicted)
                 494342(B4galt3)
            CFA: 481579(B4GALT1) 482527(B4GALT2) 488650(B4GALT3)
            BTA: 281781(B4GALT1) 515771(B4GALT3)
            GGA: 396121(B4GALT1) 396122(B4GALT2) 418341(B4GALT4)
                 418342(B4GALT3)
            XLA: 379106(MGC52827)
            XTR: 448369(b4galt3) 549418(b4galt2)
            DRE: 561756(LOC561756)
STRUCTURES  PDB: 1NF5  1NHE  1NKH  1NMM  1NQI  1NWG  1O0R  1O23  1PZT  1PZY  
                 1TVY  1TW1  1TW5  1YRO  2AE7  2AEC  2AES  2AGD  2AH9  2FY7  
                 2FYA  2FYB  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.90
            ExPASy - ENZYME nomenclature database: 2.4.1.90
            ExplorEnz - The Enzyme Database: 2.4.1.90
            ERGO genome analysis and discovery system: 2.4.1.90
            BRENDA, the Enzyme Database: 2.4.1.90
            CAS: 9054-94-8
///
ENTRY       EC 2.4.1.91                 Enzyme
NAME        flavonol 3-O-glucosyltransferase;
            GTI;
            uridine diphosphoglucose-flavonol 3-O-glucosyltransferase;
            UDP-glucose:flavonol 3-O-glucosyltransferase;
            UDPG:flavonoid-3-O-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:flavonol 3-O-D-glucosyltransferase
REACTION    UDP-glucose + a flavonol = UDP + a flavonol 3-O-beta-D-glucoside
            [RN:R03267]
ALL_REAC    R03267 > R02158 R06611
SUBSTRATE   UDP-glucose [CPD:C00029];
            flavonol [CPD:C01495]
PRODUCT     UDP [CPD:C00015];
            flavonol 3-O-beta-D-glucoside [CPD:C03946]
COMMENT     Acts on a variety of flavonols, including quercetin and quercetin
            7-O-glucoside. Different from EC 2.4.1.81 (flavone
            7-O-beta-glucosyltransferase).
REFERENCE   1
  AUTHORS   Kleinehollenhorst, G., Behrens, H., Pegels, G., Srunk, N. and
            Wiermann, R.
  TITLE     Formation of flavonol 3-O-diglycosides and flavonol
            3-O-triglycosides by enzyme extracts from anthers of Tulipa cv
            apeldoorn - characterization and activity of 3 different
            O-glycosyltransferases during anther development.
  JOURNAL   Z. Natursforsch. C: Biosci. 37 (1982) 587-599.
  ORGANISM  Tulipa sp.
REFERENCE   2  [PMID:4731963]
  AUTHORS   Sutter A, Grisebach H.
  TITLE     UDP-glucose: flavonol 3-0-glucosyltransferase from cell suspension
            cultures of parsley.
  JOURNAL   Biochim. Biophys. Acta. 309 (1973) 289-95.
  ORGANISM  Petroselinum hortense
PATHWAY     PATH: map00941  Flavonoid biosynthesis
ORTHOLOGY   KO: K00724  flavonol 3-O-glucosyltransferase
GENES       ATH: AT1G30530 AT4G15280 AT5G17030 AT5G17040 AT5G17050
            OSA: 4340373
STRUCTURES  PDB: 2C1X  2C1Z  2C9Z  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.91
            ExPASy - ENZYME nomenclature database: 2.4.1.91
            ExplorEnz - The Enzyme Database: 2.4.1.91
            ERGO genome analysis and discovery system: 2.4.1.91
            BRENDA, the Enzyme Database: 2.4.1.91
            CAS: 50812-18-5
///
ENTRY       EC 2.4.1.92                 Enzyme
NAME        (N-acetylneuraminyl)-galactosylglucosylceramide
            N-acetylgalactosaminyltransferase;
            uridine diphosphoacetylgalactosamine-ganglioside GM3
            acetylgalactosaminyltransferase;
            ganglioside GM2 synthase;
            ganglioside GM3 acetylgalactosaminyltransferase;
            GM2 synthase;
            UDP
            acetylgalactosamine-(N-acetylneuraminyl)-D-galactosyl-D-
            glucosylceramide acetylgalactosaminyltransferase;
            UDP-N-acetylgalactosamine GM3 N-acetylgalactosaminyltransferase;
            uridine
            diphosphoacetylgalactosamine-
            acetylneuraminylgalactosylglucosylceramide
            acetylgalactosaminyltransferase;
            uridine diphosphoacetylgalactosamine-hematoside
            acetylgalactosaminyltransferase;
            GM2/GD2-synthase;
            beta-1,4N-aetylgalactosaminyltransferase;
            asialo-GM2 synthase;
            GalNAc-T;
            UDP-N-acetyl-D-galactosamine:(N-acetylneuraminyl)-D-galactosyl-D-
            glucosylceramide N-acetyl-D-galactosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-galactosamine:1-O-[O-(N-acetyl-alpha-neuraminosyl)-(2
            ->3)-O-beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranosyl]-ceramid
            e 1,4-beta-N-acetyl-D-galactosaminyltransferase
REACTION    UDP-N-acetyl-D-galactosamine +
            1-O-[O-(N-acetyl-alpha-neuraminosyl)-(2->3)-O-beta-D-
            galactopyranosyl-(1->4)-beta-D-glucopyranosyl]-ceramide = UDP +
            1-O-[O-2-(acetylamino)-2-deoxy-beta-D-galactopyranosyl-(1->4)-O-[N-
            acetyl-alpha-neuraminosyl-(2->3)]-O-beta-D-galactopyranosyl-(1->4)-
            beta-D-glucopyranosyl]-ceramide [RN:R04584 R05939]
ALL_REAC    R04584 R05939(G);
            (other) R03490 R05109 R05938(G) R05946(G) R05952(G)
SUBSTRATE   UDP-N-acetyl-D-galactosamine [CPD:C00203];
            1-O-[O-(N-acetyl-alpha-neuraminosyl)-(2->3)-O-beta-D-
            galactopyranosyl-(1->4)-beta-D-glucopyranosyl]-ceramide
PRODUCT     UDP [CPD:C00015];
            1-O-[O-2-(acetylamino)-2-deoxy-beta-D-galactopyranosyl-(1->4)-O-[N-
            acetyl-alpha-neuraminosyl-(2->3)]-O-beta-D-galactopyranosyl-(1->4)-
            beta-D-glucopyranosyl]-ceramide
COMMENT     This enzyme catalyses the formation of the gangliosides (i.e.
            sialic-acid-containing glycosphingolipids) GM2, GD2 and SM2 from
            GM3, GD3 and SM3, respectively. Asialo-GM3 [3] and lactosylceramide
            [2] are also substrates, but glycoproteins and oligosaccharides are
            not substrates.
REFERENCE   1  [PMID:5554906]
  AUTHORS   Dicesare JL, Dain JA.
  TITLE     The enzymic synthesis of ganglioside. IV. UDP-N-acetylgalactosamine:
            (N-acetylneuraminyl)-galactosylglucosyl ceramide
            N-acetylgalactosaminyltransferase in rat brain.
  JOURNAL   Biochim. Biophys. Acta. 231 (1971) 385-93.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:3140234]
  AUTHORS   Pohlentz G, Klein D, Schwarzmann G, Schmitz D, Sandhoff K.
  TITLE     Both GA2, GM2, and GD2 synthases and GM1b, GD1a, and GT1b synthases
            are single enzymes in Golgi vesicles from rat liver.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 7044-8.
REFERENCE   3  [PMID:7980468]
  AUTHORS   Hidari JK, Ichikawa S, Furukawa K, Yamasaki M, Hirabayashi Y.
  TITLE     beta 1-4N-acetylgalactosaminyltransferase can synthesize both
            asialoglycosphingolipid GM2 and glycosphingolipid GM2 in vitro and
            in vivo: isolation and characterization of a beta
            1-4N-acetylgalactosaminyltransferase cDNA clone from rat ascites
            hepatoma cell line AH7974F.
  JOURNAL   Biochem. J. 303 ( Pt 3) (1994) 957-65.
REFERENCE   4  [PMID:8245020]
  AUTHORS   Hashimoto Y, Sekine M, Iwasaki K, Suzuki A.
  TITLE     Purification and characterization of UDP-N-acetylgalactosamine
            GM3/GD3 N-acetylgalactosaminyltransferase from mouse liver.
  JOURNAL   J. Biol. Chem. 268 (1993) 25857-64.
REFERENCE   5  [PMID:3115968]
  AUTHORS   Nagai K, Ishizuka I.
  TITLE     Biosynthesis of monosulfogangliotriaosylceramide and GM2 by
            N-acetylgalactosaminyltransferase from rat brain.
  JOURNAL   J. Biochem. (Tokyo). 101 (1987) 1115-27.
REFERENCE   6  [PMID:12417418]
  AUTHORS   Furukawa K, Takamiya K, Furukawa K.
  TITLE     Beta1,4-N-acetylgalactosaminyltransferase--GM2/GD2 synthase: a key
            enzyme to control the synthesis of brain-enriched complex
            gangliosides.
  JOURNAL   Biochim. Biophys. Acta. 1573 (2002) 356-62.
REFERENCE   7  [PMID:15710896]
  AUTHORS   Yamashita T, Wu YP, Sandhoff R, Werth N, Mizukami H, Ellis JM,
            Dupree JL, Geyer R, Sandhoff K, Proia RL.
  TITLE     Interruption of ganglioside synthesis produces central nervous
            system degeneration and altered axon-glial interactions.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 2725-30.
PATHWAY     PATH: map00604  Glycosphingolipid biosynthesis - ganglioseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K00725  (N-Acetylneuraminyl)-galactosylglucosylceramide
                        N-acetylgalactosaminyltransferase
GENES       HSA: 2583(B4GALNT1)
            PTR: 452021(B4GALNT1)
            MMU: 14421(B4galnt1)
            RNO: 64828(B4galnt1)
            CFA: 481129(B4GALNT1)
            BTA: 520159(GALGT)
            XLA: 379299(MGC53523)
            DRE: 569600(LOC569600)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.92
            ExPASy - ENZYME nomenclature database: 2.4.1.92
            ExplorEnz - The Enzyme Database: 2.4.1.92
            ERGO genome analysis and discovery system: 2.4.1.92
            BRENDA, the Enzyme Database: 2.4.1.92
            CAS: 67338-98-1
///
ENTRY       EC 2.4.1.93       Obsolete  Enzyme
NAME        Transferred to 4.2.2.18
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Transferred entry: Now EC 4.2.2.18, inulin fructotransferase
            (DFA-III-forming). The enzyme was wrongly classified as a
            transferase rather than a lyase. (EC 2.4.1.93 created 1976, deleted
            2004)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.93
            ExPASy - ENZYME nomenclature database: 2.4.1.93
            ExplorEnz - The Enzyme Database: 2.4.1.93
            ERGO genome analysis and discovery system: 2.4.1.93
            BRENDA, the Enzyme Database: 2.4.1.93
///
ENTRY       EC 2.4.1.94                 Enzyme
NAME        protein N-acetylglucosaminyltransferase;
            uridine diphosphoacetylglucosamine-protein
            acetylglucosaminyltransferase;
            uridine diphospho-N-acetylglucosamine:polypeptide
            beta-N-acetylglucosaminyltransferase;
            O-GlcNAc transferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:protein
            beta-N-acetyl-D-glucosaminyl-transferase
REACTION    UDP-N-acetyl-D-glucosamine + protein = UDP +
            4-N-(N-acetyl-D-glucosaminyl)-protein [RN:R00417]
ALL_REAC    R00417
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            protein [CPD:C00017]
PRODUCT     UDP [CPD:C00015];
            4-N-(N-acetyl-D-glucosaminyl)-protein [CPD:C04375]
COMMENT     The acceptor is the asparagine residue in a sequence of the form
            Asn-Xaa-Thr or Asn-Xaa-Ser.
REFERENCE   1  [PMID:1156375]
  AUTHORS   Khalkhall Z, Marshall RD.
  TITLE     Glycosylation of ribonuclease A catalysed by rabbit liver extracts.
  JOURNAL   Biochem. J. 146 (1975) 299-307.
  ORGANISM  rabbit
REFERENCE   2  [PMID:986874]
  AUTHORS   Khalkhali Z, Marshall RD.
  TITLE     UDP-N-acetyl-D-glucosamine-asparagine sequon
            N-acetyl-beta-D-glucosaminyl-transferase-activity in human serum.
  JOURNAL   Carbohydr. Res. 49 (1976) 455-73.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:795426]
  AUTHORS   Khalkhali Z, Marshall RD, Reuvers F, Habets-Willems C, Boer P.
  TITLE     Glycosylation in vitro of an asparagine sequon catalysed by
            preparations of yeast cell membranes.
  JOURNAL   Biochem. J. 160 (1976) 37-41.
  ORGANISM  cow [GN:bta]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.94
            ExPASy - ENZYME nomenclature database: 2.4.1.94
            ExplorEnz - The Enzyme Database: 2.4.1.94
            ERGO genome analysis and discovery system: 2.4.1.94
            BRENDA, the Enzyme Database: 2.4.1.94
            CAS: 72319-34-7
///
ENTRY       EC 2.4.1.95                 Enzyme
NAME        bilirubin-glucuronoside glucuronosyltransferase;
            bilirubin monoglucuronide transglucuronidase;
            bilirubin glucuronoside glucuronosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     bilirubin-glucuronoside:bilirubin-glucuronoside
            D-glucuronosyltransferase
REACTION    2 bilirubin-glucuronoside = bilirubin + bilirubin-bisglucuronoside
            [RN:R00062]
ALL_REAC    R00062
SUBSTRATE   bilirubin-glucuronoside [CPD:C03374]
PRODUCT     bilirubin [CPD:C00486];
            bilirubin-bisglucuronoside [CPD:C05787]
REFERENCE   1  [PMID:15996]
  AUTHORS   Jansen PL, Chowdhury JR, Fischberg EB, Arias IM.
  TITLE     Enzymatic conversion of bilirubin monoglucuronide to diglucuronide
            by rat liver plasma membranes.
  JOURNAL   J. Biol. Chem. 252 (1977) 2710-6.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.95
            ExPASy - ENZYME nomenclature database: 2.4.1.95
            ExplorEnz - The Enzyme Database: 2.4.1.95
            ERGO genome analysis and discovery system: 2.4.1.95
            BRENDA, the Enzyme Database: 2.4.1.95
            CAS: 71822-22-5
///
ENTRY       EC 2.4.1.96                 Enzyme
NAME        sn-glycerol-3-phosphate 1-galactosyltransferase;
            isofloridoside-phosphate synthase;
            UDP-Gal:sn-glycero-3-phosphoric acid 1-alpha-galactosyl-transferase;
            UDPgalactose:sn-glycerol-3-phosphate alpha-D-galactosyltransferase;
            uridine diphosphogalactose-glycerol phosphate galactosyltransferase;
            glycerol 3-phosphate 1alpha-galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:sn-glycerol-3-phosphate
            1-alpha-D-galactosyltransferase
REACTION    UDP-galactose + sn-glycerol 3-phosphate = UDP +
            alpha-D-galactosyl-(1,1')-sn-glycerol 3-phosphate [RN:R00854]
ALL_REAC    R00854
SUBSTRATE   UDP-galactose [CPD:C00052];
            sn-glycerol 3-phosphate [CPD:C00093]
PRODUCT     UDP [CPD:C00015];
            alpha-D-galactosyl-(1,1')-sn-glycerol 3-phosphate [CPD:C04703]
COMMENT     The product is hydrolysed by a phosphatase to isofloridoside, which
            is involved in osmoregulation (cf. EC 2.4.1.137
            sn-glycerol-3-phosphate 2-alpha-galactosyltransferase).
REFERENCE   1
  AUTHORS   Kauss, H. and Quader, H.
  TITLE     In vitro activation of a galactosyl transferase involved in the
            osmotic regulation of Ochromonas.
  JOURNAL   Plant Physiol. 58 (1976) 295-298.
  ORGANISM  Ochromonas malhamensis
REFERENCE   2  [PMID:11946194]
  AUTHORS   Kauss H, Schobert B.
  TITLE     First demonstration of UDP-GAL: sn-glycero-3-phosphoric acid
            1-alpha-galactosyl-transferase and its possible role in
            osmoregulation.
  JOURNAL   FEBS. Lett. 19 (1971) 131-135.
  ORGANISM  Ochromonas malhamensis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.96
            ExPASy - ENZYME nomenclature database: 2.4.1.96
            ExplorEnz - The Enzyme Database: 2.4.1.96
            ERGO genome analysis and discovery system: 2.4.1.96
            BRENDA, the Enzyme Database: 2.4.1.96
            CAS: 9076-70-4
///
ENTRY       EC 2.4.1.97                 Enzyme
NAME        1,3-beta-D-glucan phosphorylase;
            laminarin phosphoryltransferase;
            1,3-beta-D-glucan:orthophosphate glucosyltransferase;
            laminarin phosphoryltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     1,3-beta-D-glucan:phosphate alpha-D-glucosyltransferase
REACTION    (1,3-beta-D-glucosyl)n + phosphate = (1,3-beta-D-glucosyl)n-1 +
            alpha-D-glucose 1-phosphate [RN:R03116 R06018]
ALL_REAC    R03116 R06018(G)
SUBSTRATE   (1,3-beta-D-glucosyl)n [CPD:C00965];
            phosphate [CPD:C00009]
PRODUCT     (1,3-beta-D-glucosyl)n-1 [CPD:C00965];
            alpha-D-glucose 1-phosphate [CPD:C00103]
COMMENT     Acts on a range of beta-1,3-oligoglucans, and on glucans of
            laminarin type. Different from EC 2.4.1.30 (1,3-beta-oligoglucan
            phosphorylase) and EC 2.4.1.31 (laminaribiose phosphorylase).
REFERENCE   1
  AUTHORS   Albrecht, G.J. and Kauss, H.
  TITLE     Purification, crystallization and properties of a beta-(1->3)-glucan
            phosphorylase from Ochromonas malhamensis.
  JOURNAL   Phytochemistry 10 (1971) 1293-1298.
  ORGANISM  Ochromonas malhamensis
GENES       REH: H16_B1562(glgP)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.97
            ExPASy - ENZYME nomenclature database: 2.4.1.97
            ExplorEnz - The Enzyme Database: 2.4.1.97
            ERGO genome analysis and discovery system: 2.4.1.97
            BRENDA, the Enzyme Database: 2.4.1.97
            CAS: 37340-31-1
///
ENTRY       EC 2.4.1.98       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: UDP-galactose-N-acetylglucosamine
            beta-D-galactosyl-transferase. Now included with EC 2.4.1.90,
            N-acetyllactosamine synthase (EC 2.4.1.98 created 1980, deleted
            1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.98
            ExPASy - ENZYME nomenclature database: 2.4.1.98
            ExplorEnz - The Enzyme Database: 2.4.1.98
            ERGO genome analysis and discovery system: 2.4.1.98
            BRENDA, the Enzyme Database: 2.4.1.98
///
ENTRY       EC 2.4.1.99                 Enzyme
NAME        sucrose:sucrose fructosyltransferase;
            SST;
            sucrose:sucrose 1-fructosyltransferase;
            sucrose-sucrose 1-fructosyltransferase;
            sucrose 1F-fructosyltransferase;
            sucrose:sucrose 1F-beta-D-fructosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     sucrose:sucrose 1'-beta-D-fructosyltransferase
REACTION    2 sucrose = D-glucose +
            beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl
            alpha-D-glucopyranoside [RN:R00015 R06135]
ALL_REAC    R00015 R06135(G)
SUBSTRATE   sucrose [CPD:C00089]
PRODUCT     D-glucose [CPD:C00031];
            beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl
            alpha-D-glucopyranoside
REFERENCE   1
  AUTHORS   Henry, R.J. and Darbyshire, B.
  TITLE     Sucrose:sucrose fructosyltransferase and fructan:fructan
            fructosyltransferase from Allium cepa.
  JOURNAL   Phytochemistry 19 (1980) 1017-1020.
  ORGANISM  Allium cepa
REFERENCE   2  [PMID:11080298]
  AUTHORS   Luscher M, Hochstrasser U, Vogel G, Aeschbacher R, Galati V, Nelson
            CJ, Boller T, Wiemken A.
  TITLE     Cloning and functional analysis of sucrose:sucrose
            1-fructosyltransferase from tall fescue.
  JOURNAL   Plant. Physiol. 124 (2000) 1217-28.
  ORGANISM  Festuca arundinacea
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.99
            ExPASy - ENZYME nomenclature database: 2.4.1.99
            ExplorEnz - The Enzyme Database: 2.4.1.99
            ERGO genome analysis and discovery system: 2.4.1.99
            BRENDA, the Enzyme Database: 2.4.1.99
            CAS: 73379-56-3
///
ENTRY       EC 2.4.1.100                Enzyme
NAME        2,1-fructan:2,1-fructan 1-fructosyltransferase;
            1,2-beta-D-fructan 1F-fructosyltransferase;
            fructan:fructan fructosyl transferase;
            FFT;
            1,2-beta-fructan 1F-fructosyltransferase;
            1,2-beta-D-fructan:1,2-beta-D-fructan
            1F-beta-D-fructosyltransferase;
            fructan:fructan 1-fructosyl transferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     2,1-beta-D-fructan:2,1-beta-D-fructan 1-beta-D-fructosyltransferase
REACTION    [beta-D-fructosyl-(2->1)-]m + [beta-D-fructosyl-(2->1)-]n =
            [beta-D-fructosyl-(2->1)-]m-1 + [beta-D-fructosyl-(2->1)-]n+1
            [RN:R04193 R06183]
ALL_REAC    R04193 R06183(G)
SUBSTRATE   [beta-D-fructosyl-(2->1)-]m;
            [beta-D-fructosyl-(2->1)-]n
PRODUCT     [beta-D-fructosyl-(2->1)-]m-1;
            [beta-D-fructosyl-(2->1)-]n+1
REFERENCE   1
  AUTHORS   Henry, R.J. and Darbyshire, B.
  TITLE     Sucrose:sucrose fructosyltransferase and fructan:fructan
            fructosyltransferase from Allium cepa.
  JOURNAL   Phytochemistry 19 (1980) 1017-1020.
  ORGANISM  Allium cepa
REFERENCE   2  [PMID:12970504]
  AUTHORS   Vergauwen R, Van Laere A, Van den Ende W.
  TITLE     Properties of fructan:fructan 1-fructosyltransferases from chicory
            and globe thistle, two Asteracean plants storing greatly different
            types of inulin.
  JOURNAL   Plant. Physiol. 133 (2003) 391-401.
  ORGANISM  Cynara scolymus, Echinops ritro, Cichorium intybus, Helianthus
            tuberosus
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.100
            ExPASy - ENZYME nomenclature database: 2.4.1.100
            ExplorEnz - The Enzyme Database: 2.4.1.100
            ERGO genome analysis and discovery system: 2.4.1.100
            BRENDA, the Enzyme Database: 2.4.1.100
            CAS: 73379-55-2
///
ENTRY       EC 2.4.1.101                Enzyme
NAME        alpha-1,3-mannosyl-glycoprotein
            2-beta-N-acetylglucosaminyltransferase;
            N-acetylglucosaminyltransferase I;
            N-glycosyl-oligosaccharide-glycoprotein
            N-acetylglucosaminyltransferase I;
            uridine diphosphoacetylglucosamine-alpha-1,3-mannosylglycoprotein
            beta-1,2-N-acetylglucosaminyltransferase;
            UDP-N-acetylglucosaminyl:alpha-1,3-D-mannoside-beta-1,2-N-
            acetylglucosaminyltransferase I;
            UDP-N-acetylglucosaminyl:alpha-3-D-mannoside
            beta-1,2-N-acetylglucosaminyltransferase I;
            alpha-1,3-mannosyl-glycoprotein
            beta-1,2-N-acetylglucosaminyltransferase;
            GnTI
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:3-(alpha-D-mannosyl)-beta-D-mannosyl-glyc
            oprotein 2-beta-N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R
            = UDP +
            3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-
            mannosyl-R [RN:R05983]
ALL_REAC    R05983(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            3-(alpha-D-mannosyl)-beta-D-mannosyl-R [CPD:C04614]
PRODUCT     UDP [CPD:C00015];
            3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-
            mannosyl-R [CPD:C04880]
COMMENT     R represents the remainder of the N-linked oligosaccharide in the
            glycoprotein acceptor. Note that this enzyme acts before
            N-acetylglucosaminyltransferases II, III, IV, V and VI (click here
            for diagram).
REFERENCE   1  [PMID:6445358]
  AUTHORS   Harpaz N, Schachter H.
  TITLE     Control of glycoprotein synthesis. Bovine colostrum
            UDP-N-acetylglucosamine:alpha-D-mannoside beta
            2-N-acetylglucosaminyltransferase I. Separation from
            UDP-N-acetylglucosamine:alpha-D-mannoside beta
            2-N-acetylglucosaminyltransferase II, partial purification, and
            substrate specificity.
  JOURNAL   J. Biol. Chem. 255 (1980) 4885-93.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:6452163]
  AUTHORS   Mendicino J, Chandrasekaran EV, Anumula KR, Davila M.
  TITLE     Isolation and properties of
            alpha-D-mannose:beta-1,2-N-acetylglucosaminyltransferase from
            trachea mucosa.
  JOURNAL   Biochemistry. 20 (1981) 967-76.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:6170335]
  AUTHORS   Miyagi T, Tsuiki S.
  TITLE     Studies on UDP-N-acetylglucosamine : alpha-mannoside
            beta-N-acetylglucosaminyltransferase of rat liver and hepatomas.
  JOURNAL   Biochim. Biophys. Acta. 661 (1981) 148-57.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:6457827]
  AUTHORS   Oppenheimer CL, Eckhardt AE, Hill RL.
  TITLE     The nonidentity of porcine N-acetylglucosaminyltransferases I and
            II.
  JOURNAL   J. Biol. Chem. 256 (1981) 11477-82.
  ORGANISM  pig [GN:ssc]
REFERENCE   5  [PMID:6450208]
  AUTHORS   Oppenheimer CL, Hill RL.
  TITLE     Purification and characterization of a rabbit liver alpha 1 goes to
            3 mannoside beta 1 goes to 2 N-acetylglucosaminyltransferase.
  JOURNAL   J. Biol. Chem. 256 (1981) 799-804.
  ORGANISM  rabbit
REFERENCE   6  [PMID:6366476]
  AUTHORS   Schachter H, Narasimhan S, Gleeson P, Vella G.
  TITLE     Glycosyltransferases involved in elongation of N-glycosidically
            linked oligosaccharides of the complex or N-acetyllactosamine type.
  JOURNAL   Methods. Enzymol. 98 (1983) 98-134.
REFERENCE   7  [PMID:6235906]
  AUTHORS   Vella GJ, Paulsen H, Schachter H.
  TITLE     Control of glycoprotein synthesis. IX. A terminal Man alpha l-3Man
            beta 1- sequence in the substrate is the minimum requirement for
            UDP-N-acetyl-D-glucosamine: alpha-D-mannoside (GlcNAc to Man alpha
            1-3) beta 2-N-acetylglucosaminyltransferase I.
  JOURNAL   Can. J. Biochem. Cell. Biol. 62 (1984) 409-17.
  ORGANISM  cow [GN:bta]
REFERENCE   8  [PMID:11032794]
  AUTHORS   Unligil UM, Zhou S, Yuwaraj S, Sarkar M, Schachter H, Rini JM.
  TITLE     X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I:
            catalytic mechanism and a new protein superfamily.
  JOURNAL   EMBO. J. 19 (2000) 5269-80.
  ORGANISM  rabbit
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00726  alpha-1,3-mannosyl-glycoprotein
                        beta-1,2-N-acetylglucosaminyltransferase
GENES       HSA: 4245(MGAT1)
            PTR: 462340(MGAT1)
            MMU: 17308(Mgat1)
            RNO: 81519(Mgat1)
            CFA: 491674(MGAT1)
            BTA: 534248(MGAT1)
            XLA: 379038(gntI) 379047(MGC52514)
            XTR: 496815(mgat1)
            DRE: 393649(zgc:66030) 558524(zgc:153912)
            SPU: 594485(LOC594485)
            DME: Dmel_CG13431(Mgat1)
            CEL: B0416.6(gly-13) F48E3.1(gly-12) M01F1.1(gly-14)
            ATH: AT4G38240(CGL1)
            OSA: 4331263
            DDI: DDB_0231456(gnt3)
STRUCTURES  PDB: 1FO8  1FO9  1FOA  2AM3  2AM4  2AM5  2APC  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.101
            ExPASy - ENZYME nomenclature database: 2.4.1.101
            ExplorEnz - The Enzyme Database: 2.4.1.101
            ERGO genome analysis and discovery system: 2.4.1.101
            BRENDA, the Enzyme Database: 2.4.1.101
            CAS: 102576-81-8
///
ENTRY       EC 2.4.1.102                Enzyme
NAME        beta-1,3-galactosyl-O-glycosyl-glycoprotein
            beta-1,6-N-acetylglucosaminyltransferase;
            O-glycosyl-oligosaccharide-glycoprotein
            N-acetylglucosaminyltransferase I;
            beta6-N-acetylglucosaminyltransferase;
            uridine diphosphoacetylglucosamine-mucin
            beta-(1->6)-acetylglucosaminyltransferase;
            core 2 acetylglucosaminyltransferase;
            core 6-beta-GlcNAc-transferase A
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein
            (N-acetyl-D-glucosamine to N-acetyl-D-galactosamine of
            beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R)
            beta-1,6-N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine +
            beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R = UDP +
            beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-
            galactosaminyl-R [RN:R04575 R05912]
ALL_REAC    R04575 R05912(G);
            (other) R05910(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R [CPD:C04750]
PRODUCT     UDP [CPD:C00015];
            beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-
            galactosaminyl-R [CPD:C04902]
COMMENT     cf. EC 2.4.1.146 (beta-1,3-galactosyl-O-glycosyl-glycoprotein
            beta-1,3-N-acetylglucosaminyltransferase), EC 2.4.1.147
            (acetylgalactosaminyl-O-glycosyl-glycoprotein
            beta-1,3-N-acetylglucosaminyltransferase) and EC 2.4.1.148
            (acetylgalactosaminyl-O-glycosyl-glycoprotein
            beta-1,6-N-acetylglucosaminyltransferase).
REFERENCE   1  [PMID:6226356]
  AUTHORS   Brockhausen I, Rachaman ES, Matta KL, Schachter H.
  TITLE     The separation by liquid chromatography (under elevated pressure) of
            phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides.
            Analysis of substrates and products for four
            N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis.
  JOURNAL   Carbohydr. Res. 120 (1983) 3-16.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6449508]
  AUTHORS   Williams D, Longmore G, Matta KL, Schachter H.
  TITLE     Mucin synthesis. II. Substrate specificity and product
            identification studies on canine submaxillary gland UDP-GlcNAc:Gal
            beta 1-3GalNAc(GlcNAc leads to GalNAc) beta
            6-N-acetylglucosaminyltransferase.
  JOURNAL   J. Biol. Chem. 255 (1980) 11253-61.
  ORGANISM  dog [GN:cfa]
REFERENCE   3  [PMID:6449507]
  AUTHORS   Williams D, Schachter H.
  TITLE     Mucin synthesis. I. Detection in canine submaxillary glands of an
            N-acetylglucosaminyltransferase which acts on mucin substrates.
  JOURNAL   J. Biol. Chem. 255 (1980) 11247-52.
  ORGANISM  pig, sheep
PATHWAY     PATH: map00512  O-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00727  beta-1,3-galactosyl-O-glycosyl-glycoprotein
                        beta-1,6-N-acetylglucosaminyltransferase
GENES       HSA: 2650(GCNT1)
            PTR: 472959(GCNT1)
            MMU: 14537(Gcnt1)
            RNO: 64043(Gcnt1)
            CFA: 484158(GCNT1)
            BTA: 281778(GCNT1)
            GGA: 427260(GCNT1)
            XLA: 380501(gcnt1)
            CEL: T15D6.2(acetylglucosaminyltransferase)
STRUCTURES  PDB: 2GAK  2GAM  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.102
            ExPASy - ENZYME nomenclature database: 2.4.1.102
            ExplorEnz - The Enzyme Database: 2.4.1.102
            ERGO genome analysis and discovery system: 2.4.1.102
            BRENDA, the Enzyme Database: 2.4.1.102
            CAS: 95978-15-7
///
ENTRY       EC 2.4.1.103                Enzyme
NAME        alizarin 2-beta-glucosyltransferase;
            uridine diphosphoglucose-alizarin glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:1,2-dihydroxy-9,10-anthraquinone
            2-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + alizarin = UDP +
            1-hydroxy-2-(beta-D-glucosyloxy)-9,10-anthraquinone [RN:R03573]
ALL_REAC    R03573
SUBSTRATE   UDP-glucose [CPD:C00029];
            alizarin [CPD:C01474]
PRODUCT     UDP [CPD:C00015];
            1-hydroxy-2-(beta-D-glucosyloxy)-9,10-anthraquinone [CPD:C04719]
COMMENT     Acts on other hydroxy- and dihydroxy-derivatives of
            9,10-anthraquinone.
REFERENCE   1  [PMID:38193]
  AUTHORS   Mateju J, Cudlin J, Steinerova N, Blumauerova M, Vanek Z.
  TITLE     Partial purification and properties of glucosyltransferase from
            Streptomyces aureofaciens.
  JOURNAL   Folia. Microbiol. (Praha). 24 (1979) 205-10.
  ORGANISM  Streptomyces aureofaciens
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.103
            ExPASy - ENZYME nomenclature database: 2.4.1.103
            ExplorEnz - The Enzyme Database: 2.4.1.103
            ERGO genome analysis and discovery system: 2.4.1.103
            BRENDA, the Enzyme Database: 2.4.1.103
            CAS: 74506-41-5
///
ENTRY       EC 2.4.1.104                Enzyme
NAME        o-dihydroxycoumarin 7-O-glucosyltransferase;
            uridine diphosphoglucose-o-dihydroxycoumarin
            7-O-glucosyltransferase;
            UDP-glucose:o-dihydroxycoumarin glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:7,8-dihydroxycoumarin 7-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + 7,8-dihydroxycoumarin = UDP + daphnin [RN:R03548]
ALL_REAC    R03548
SUBSTRATE   UDP-glucose [CPD:C00029];
            7,8-dihydroxycoumarin [CPD:C03093]
PRODUCT     UDP [CPD:C00015];
            daphnin [CPD:C01421]
COMMENT     Converts the aglycone daphetin into daphnin and, more slowly,
            esculetin into cichoriin, umbelliferone into skimmin, hydrangetin
            into hydrangin and scopoletin into scopolin.
REFERENCE   1
  AUTHORS   Ibrahim, R.K. and Boulay, B.
  TITLE     Purification and some properties of UDP-glucose:o-hydroxycoumarin
            7-O-glucosyltransferase from tobacco cell cultures.
  JOURNAL   Plant Sci. Lett. 18 (1980) 177-184.
  ORGANISM  Nicotiana tabacum
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.104
            ExPASy - ENZYME nomenclature database: 2.4.1.104
            ExplorEnz - The Enzyme Database: 2.4.1.104
            ERGO genome analysis and discovery system: 2.4.1.104
            BRENDA, the Enzyme Database: 2.4.1.104
            CAS: 74114-37-7
///
ENTRY       EC 2.4.1.105                Enzyme
NAME        vitexin beta-glucosyltransferase;
            uridine diphosphoglucose-vitexin 2"-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:vitexin 2
REACTION    UDP-glucose + vitexin = UDP + vitexin 2"-O-beta-D-glucoside
            [RN:R03565]
ALL_REAC    R03565
SUBSTRATE   UDP-glucose [CPD:C00029];
            vitexin [CPD:C01460]
PRODUCT     UDP [CPD:C00015];
            vitexin 2''-O-beta-D-glucoside [CPD:C04024]
COMMENT     Vitexin is a flavonoid from Cannabis sativa (hemp) and some
            populations of Silene alba.
REFERENCE   1
  AUTHORS   Heinsbroek, R., Van Brederode, J., Van Nigtevecht, G., Maas, J.,
            Kamsteeg, J., Besson, E. and Chopin, J.
  TITLE     The 2''-O-glucosylation of vitexin and isovitexin in petals of
            Silene alba is catalysed by two dfferent enzymes.
  JOURNAL   Phytochemistry 19 (1980) 1935-1937.
  ORGANISM  Silene alba
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.105
            ExPASy - ENZYME nomenclature database: 2.4.1.105
            ExplorEnz - The Enzyme Database: 2.4.1.105
            ERGO genome analysis and discovery system: 2.4.1.105
            BRENDA, the Enzyme Database: 2.4.1.105
            CAS: 76828-68-7
///
ENTRY       EC 2.4.1.106                Enzyme
NAME        isovitexin beta-glucosyltransferase;
            uridine diphosphoglucose-isovitexin 2"-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:isovitexin 2''-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + isovitexin = UDP + isovitexin 2"-O-beta-D-glucoside
            [RN:R03686]
ALL_REAC    R03686
SUBSTRATE   UDP-glucose [CPD:C00029];
            isovitexin [CPD:C01714]
PRODUCT     UDP [CPD:C00015];
            isovitexin 2''-O-beta-D-glucoside [CPD:C04199]
COMMENT     Isovitexin is a flavonoid from petals of Silene alba.
REFERENCE   1
  AUTHORS   Heinsbroek, R., Van Brederode, J., Van Nigtevecht, G., Maas, J.,
            Kamsteeg, J., Besson, E. and Chopin, J.
  TITLE     The 2''-O-glucosylation of vitexin and isovitexin in petals of
            Silene alba is catalysed by two dfferent enzymes.
  JOURNAL   Phytochemistry 19 (1980) 1935-1937.
  ORGANISM  Silene alba
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.106
            ExPASy - ENZYME nomenclature database: 2.4.1.106
            ExplorEnz - The Enzyme Database: 2.4.1.106
            ERGO genome analysis and discovery system: 2.4.1.106
            BRENDA, the Enzyme Database: 2.4.1.106
            CAS: 72102-99-9
///
ENTRY       EC 2.4.1.107      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: UDP-glucuronate-testosterone glucuronosyltransferase.
            Now included with EC 2.4.1.17, glucuronosyltransferase (EC 2.4.1.107
            created 1983, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.107
            ExPASy - ENZYME nomenclature database: 2.4.1.107
            ExplorEnz - The Enzyme Database: 2.4.1.107
            ERGO genome analysis and discovery system: 2.4.1.107
            BRENDA, the Enzyme Database: 2.4.1.107
///
ENTRY       EC 2.4.1.108      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: UDP-glucuronate-phenol glucuronosyltransferase. Now
            included with EC 2.4.1.17, glucuronosyltransferase (EC 2.4.1.108
            created 1983, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.108
            ExPASy - ENZYME nomenclature database: 2.4.1.108
            ExplorEnz - The Enzyme Database: 2.4.1.108
            ERGO genome analysis and discovery system: 2.4.1.108
            BRENDA, the Enzyme Database: 2.4.1.108
///
ENTRY       EC 2.4.1.109                Enzyme
NAME        dolichyl-phosphate-mannose-protein mannosyltransferase;
            dolichol phosphomannose-protein mannosyltransferase;
            protein O-D-mannosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     dolichyl-phosphate-D-mannose:protein O-D-mannosyltransferase
REACTION    dolichyl phosphate D-mannose + protein = dolichyl phosphate +
            O-D-mannosylprotein [RN:R04072]
ALL_REAC    R04072;
            (other) R07620(G)
SUBSTRATE   dolichyl phosphate D-mannose [CPD:C03862];
            protein [CPD:C00017]
PRODUCT     dolichyl phosphate [CPD:C00110];
            O-D-mannosylprotein [CPD:C02863]
COMMENT     The enzyme transfers mannosyl residues to the hydroxy group of
            serine or threonine residues, producing cell-wall mannoproteins. It
            acts only on long-chain alpha-dihydropolyprenyl derivatives, larger
            than C35.
REFERENCE   1  [PMID:6989607]
  AUTHORS   Babczinski P, Haselbeck A, Tanner W.
  TITLE     Yeast mannosyl transferases requiring dolichyl phosphate and
            dolichyl phosphate mannose as substrate. Partial purification and
            characterization of the solubilized enzyme.
  JOURNAL   Eur. J. Biochem. 105 (1980) 509-15.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:6445267]
  AUTHORS   Palamarczyk G, Lehle L, Mankowski T, Chojnacki T, Tanner W.
  TITLE     Specificity of solubilized yeast glycosyl transferases for
            polyprenyl derivatives.
  JOURNAL   Eur. J. Biochem. 105 (1980) 517-23.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K00728  dolichyl-phosphate-mannose-protein mannosyltransferase
GENES       HSA: 10585(POMT1) 29954(POMT2)
            PTR: 453067(POMT2) 473076(POMT1)
            MMU: 217734(Pomt2) 99011(Pomt1)
            RNO: 681879(LOC681879) 84430(Pomt1)
            CFA: 480400(POMT2) 608039(POMT1)
            BTA: 537054(LOC537054) 617609(POMT1)
            GGA: 417175(RCJMB04_13j5) 423373(POMT2)
            XTR: 448433(pomt1)
            DRE: 563878(zgc:158749) 569769(pomt1)
            SPU: 580971(LOC580971) 588991(LOC588991)
            DME: Dmel_CG12311(Pomt2) Dmel_CG6097(rt)
            CME: CMJ319C
            SCE: YAL023C(PMT2) YDL093W(PMT5) YDL095W(PMT1) YDR307W
                 YGR199W(PMT6) YJR143C(PMT4) YOR321W(PMT3)
            AGO: AGOS_AAL050W AGOS_ABL085W AGOS_ACR290W AGOS_ADR279C
            PIC: PICST_53466(PTM6) PICST_70572(PMT2) PICST_72313 PICST_90238
            CGR: CAGL0F00759g CAGL0J08734g CAGL0K00979g CAGL0L07216g
                 CAGL0M00220g
            SPO: SPAC22A12.07c SPAPB1E7.09 SPBC16C6.09
            ANI: AN1459.2 AN4761.2 AN5105.2
            AFM: AFUA_1G07690 AFUA_3G06450 AFUA_8G04500
            AOR: AO090012001021 AO090020000105 AO090023000336
            ANG: An07g10350(pmtA)
            CNE: CND01240 CND06150 CNJ01930
            UMA: UM05433.1 UM05474.1 UM06173.1
            ECU: ECU02_1300
            FTU: FTT0455c
            FTF: FTF0455c
            FTL: FTL_1609
            FTH: FTH_1555
            FTN: FTN_0546
            BMA: BMA1388
            BPS: BPSL1474
            BPM: BURPS1710b_2399(ubiE)
            AZO: azo2381
            CHY: CHY_1049
            FAL: FRAAL6290
            CYA: CYA_0756 CYA_1457 CYA_1689
            CYB: CYB_0310 CYB_0649
            AVA: Ava_3845
            HMA: rrnAC1432(dpm5)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.109
            ExPASy - ENZYME nomenclature database: 2.4.1.109
            ExplorEnz - The Enzyme Database: 2.4.1.109
            ERGO genome analysis and discovery system: 2.4.1.109
            BRENDA, the Enzyme Database: 2.4.1.109
            CAS: 74315-99-4
///
ENTRY       EC 2.4.1.110                Enzyme
NAME        tRNA-queuosine beta-mannosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-mannose:tRNAAsp-queuosine O-5"-beta-D-mannosyltransferase
REACTION    GDP-mannose + tRNAAsp-queuosine = GDP +
            tRNAAsp-O-5"-beta-D-mannosylqueuosine [RN:R04082]
ALL_REAC    R04082
SUBSTRATE   GDP-mannose [CPD:C00096];
            tRNAAsp-queuosine
PRODUCT     GDP [CPD:C00035];
            tRNAAsp-O-5''-beta-D-mannosylqueuosine
REFERENCE   1  [PMID:20603]
  AUTHORS   Okada N, Nishimura S.
  TITLE     Enzymatic synthesis of Q nucleoside containing mannose in the
            anticodon of tRNA: isolation of a novel mannosyltransferase from a
            cell-free extract of rat liver.
  JOURNAL   Nucleic. Acids. Res. 4 (1977) 2931-8.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.110
            ExPASy - ENZYME nomenclature database: 2.4.1.110
            ExplorEnz - The Enzyme Database: 2.4.1.110
            ERGO genome analysis and discovery system: 2.4.1.110
            BRENDA, the Enzyme Database: 2.4.1.110
            CAS: 9055-06-5
///
ENTRY       EC 2.4.1.111                Enzyme
NAME        coniferyl-alcohol glucosyltransferase;
            uridine diphosphoglucose-coniferyl alcohol glucosyltransferase;
            UDP-glucose coniferyl alcohol glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:coniferyl-alcohol 4'-beta-D-glucosyltransferase
REACTION    UDP-glucose + coniferyl alcohol = UDP + coniferin [RN:R02594]
ALL_REAC    R02594;
            (other) R03605 R04005
SUBSTRATE   UDP-glucose [CPD:C00029];
            coniferyl alcohol [CPD:C00590]
PRODUCT     UDP [CPD:C00015];
            coniferin [CPD:C00761]
COMMENT     Sinapyl alcohol can also act as acceptor.
REFERENCE   1  [PMID:10853]
  AUTHORS   Ibrahim RK, Grisebach H.
  TITLE     Purification and properties of UDP-glucose: coniferyl alcohol
            glucosyltransferase from suspension culturesof Paul's scarlet rose.
  JOURNAL   Arch. Biochem. Biophys. 176 (1976) 700-8.
  ORGANISM  Rosa sp., Linum usitatissimum, Glycine max [GN:egma], Petroselinum
            hortense, Parthenocissus tricuspidata, Nicotiana tabacum, Cicer
            arietinum
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.111
            ExPASy - ENZYME nomenclature database: 2.4.1.111
            ExplorEnz - The Enzyme Database: 2.4.1.111
            ERGO genome analysis and discovery system: 2.4.1.111
            BRENDA, the Enzyme Database: 2.4.1.111
            CAS: 61116-23-2
///
ENTRY       EC 2.4.1.112      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: The protein referred to in this entry is now known to
            be glycogenin so the entry has been incorporated into EC 2.4.1.186,
            glycogenin glucosyltransferase (EC 2.4.1.112 created 1984, deleted
            2007)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.112
            ExPASy - ENZYME nomenclature database: 2.4.1.112
            ExplorEnz - The Enzyme Database: 2.4.1.112
            ERGO genome analysis and discovery system: 2.4.1.112
            BRENDA, the Enzyme Database: 2.4.1.112
///
ENTRY       EC 2.4.1.113                Enzyme
NAME        alpha-1,4-glucan-protein synthase (ADP-forming);
            ADP-glucose:protein glucosyltransferase;
            adenosine diphosphoglucose-protein glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     ADP-glucose:protein 4-alpha-D-glucosyltransferase
REACTION    ADP-glucose + protein = ADP + alpha-D-glucosyl-protein [RN:R02420]
ALL_REAC    R02420
SUBSTRATE   ADP-glucose [CPD:C00498];
            protein [CPD:C00017]
PRODUCT     ADP [CPD:C00008];
            alpha-D-glucosyl-protein [CPD:C01140]
COMMENT     The enzyme builds up alpha-1,4-glucan chains covalently bound to
            protein, thus acting as an initiator of glycogen synthesis.
REFERENCE   1  [PMID:418819]
  AUTHORS   Barengo R, Krisman CR.
  TITLE     Initiation of glycogen biosynthesis in Escherichia coli. Studies of
            the properties of the enzymes involved.
  JOURNAL   Biochim. Biophys. Acta. 540 (1978) 190-6.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.113
            ExPASy - ENZYME nomenclature database: 2.4.1.113
            ExplorEnz - The Enzyme Database: 2.4.1.113
            ERGO genome analysis and discovery system: 2.4.1.113
            BRENDA, the Enzyme Database: 2.4.1.113
            CAS: 67053-99-0
///
ENTRY       EC 2.4.1.114                Enzyme
NAME        2-coumarate O-beta-glucosyltransferase;
            uridine diphosphoglucose-o-coumarate glucosyltransferase;
            UDPG:o-coumaric acid O-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:trans-2-hydroxycinnamate O-beta-D-glucosyltransferase
REACTION    UDP-glucose + trans-2-hydroxycinnamate = UDP +
            trans-beta-D-glucosyl-2-hydroxycinnamate [RN:R03710]
ALL_REAC    R03710
SUBSTRATE   UDP-glucose [CPD:C00029];
            trans-2-hydroxycinnamate [CPD:C01772]
PRODUCT     UDP [CPD:C00015];
            trans-beta-D-glucosyl-2-hydroxycinnamate [CPD:C05158]
COMMENT     Coumarinate (cis-2-hydroxycinnamate) does not act as acceptor.
REFERENCE   1
  AUTHORS   Kleinhofs, A., Haskins, F.A. and Gorz, H.J.
  TITLE     trans-o-Hydroxylcinnamic acid glucosylation in cell-free extracts of
            Melilotus alba.
  JOURNAL   Phytochemistry 6 (1967) 1313-1318.
  ORGANISM  Melilotus alba
REFERENCE   2
  AUTHORS   Poulton, J.E., McRee, B.E. and Conn, E.E.
  TITLE     Intracellular localization of two enzymes involved in coumarin
            biosynthesis in Melilotus alba.
  JOURNAL   Plant Physiol. 65 (1980) 171-175.
  ORGANISM  Melilotus alba
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.114
            ExPASy - ENZYME nomenclature database: 2.4.1.114
            ExplorEnz - The Enzyme Database: 2.4.1.114
            ERGO genome analysis and discovery system: 2.4.1.114
            BRENDA, the Enzyme Database: 2.4.1.114
            CAS: 73665-97-1
///
ENTRY       EC 2.4.1.115                Enzyme
NAME        anthocyanidin 3-O-glucosyltransferase;
            uridine diphosphoglucose-anthocyanidin 3-O-glucosyltransferase;
            UDP-glucose:anthocyanidin/flavonol 3-O-glucosyltransferase;
            UDP-glucose:cyanidin-3-O-glucosyltransferase;
            UDP-glucose:anthocyanidin 3-O-D-glucosyltransferase;
            3-GT
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-D-glucose:anthocyanidin 3-O-beta-D-glucosyltransferase
REACTION    UDP-D-glucose + an anthocyanidin = UDP + an
            anthocyanidin-3-O-beta-D-glucoside [RN:R03797]
ALL_REAC    R03797 > R06534 R06535 R06536
SUBSTRATE   UDP-D-glucose [CPD:C00029];
            anthocyanidin [CPD:C02003]
PRODUCT     UDP [CPD:C00015];
            anthocyanidin-3-O-beta-D-glucoside [CPD:C03940]
COMMENT     The anthocyanidin compounds cyanidin, delphinidin, peonidin and to a
            lesser extent pelargonidin can act as substrates. The enzyme does
            not catalyse glucosylation of the 5-position of cyanidin and does
            not act on flavanols such as quercetin and kaempferol (cf. EC
            2.4.1.91 flavonol 3-O-glucosyltransferase). In conjunction with EC
            1.14.11.19, leucocyanidin oxygenase, it is involved in the
            conversion of leucoanthocyanidin into anthocyanidin 3-glucoside. It
            may act on the pseudobase precursor of the anthocyanidin rather than
            on the anthocyanidin itself [3].
REFERENCE   1  [PMID:751640]
  AUTHORS   Kamsteeg J, van Brederode J, van Nigtevecht G.
  TITLE     Identification and properties of UDP-glucose:
            cyanidin-3-O-glucosyltransferase isolated from petals of the red
            campion (Silene dioica).
  JOURNAL   Biochem. Genet. 16 (1978) 1045-58.
  ORGANISM  Silene dioica
REFERENCE   2  [PMID:9535914]
  AUTHORS   Ford CM, Boss PK, Hoj PB.
  TITLE     Cloning and characterization of Vitis vinifera UDP-glucose:flavonoid
            3-O-glucosyltransferase, a homologue of the enzyme encoded by the
            maize Bronze-1 locus that may primarily serve to glucosylate
            anthocyanidins in vivo.
  JOURNAL   J. Biol. Chem. 273 (1998) 9224-33.
  ORGANISM  Vitis vinifera [GN:evvi]
REFERENCE   3  [PMID:11316805]
  AUTHORS   Nakajima  J, Tanaka Y, Yamazaki M, Saito K.
  TITLE     Reaction mechanism from leucoanthocyanidin to anthocyanidin
            3-glucoside, a key reaction for coloring in anthocyanin
            biosynthesis.
  JOURNAL   J. Biol. Chem. 276 (2001) 25797-803.
  ORGANISM  Petunia hybrida
PATHWAY     PATH: map00942  Anthocyanin biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.115
            ExPASy - ENZYME nomenclature database: 2.4.1.115
            ExplorEnz - The Enzyme Database: 2.4.1.115
            ERGO genome analysis and discovery system: 2.4.1.115
            BRENDA, the Enzyme Database: 2.4.1.115
            CAS: 65607-32-1
///
ENTRY       EC 2.4.1.116                Enzyme
NAME        cyanidin 3-O-rutinoside 5-O-glucosyltransferase;
            uridine diphosphoglucose-cyanidin 3-rhamnosylglucoside
            5-O-glucosyltransferase;
            cyanidin-3-rhamnosylglucoside 5-O-glucosyltransferase;
            UDP-glucose:cyanidin-3-O-D-rhamnosyl-1,6-D-glucoside
            5-O-D-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:cyanidin-3-O-beta-L-rhamnosyl-(1->6)-beta-D-glucoside
            5-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + cyanidin 3-O-rutinoside = UDP + cyanidin
            3-O-rutinoside 5-O-beta-D-glucoside
ALL_REAC    (other) R06803 R06819
SUBSTRATE   UDP-glucose [CPD:C00029];
            cyanidin 3-O-rutinoside [CPD:C08620]
PRODUCT     UDP [CPD:C00015];
            cyanidin 3-O-rutinoside 5-O-beta-D-glucoside [CPD:C12646]
COMMENT     Also acts on pelargonidin-3-rutinoside. The enzyme does not catalyse
            the glucosylation of the 5-hydroxy group of cyanidin-3-glucoside.
REFERENCE   1  [PMID:751641]
  AUTHORS   Kamsteeg J, van Brederode J, van Nigtevecht G.
  TITLE     Identification, properties, and genetic control of UDP-glucose:
            cyanidin-3-rhamnosyl-(1 leads to
            6)-glucoside-5-O-glucosyltransferase isolated from petals of the red
            campion (Silene dioica).
  JOURNAL   Biochem. Genet. 16 (1978) 1059-71.
  ORGANISM  Silene dioica
PATHWAY     PATH: map00942  Anthocyanin biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.116
            ExPASy - ENZYME nomenclature database: 2.4.1.116
            ExplorEnz - The Enzyme Database: 2.4.1.116
            ERGO genome analysis and discovery system: 2.4.1.116
            BRENDA, the Enzyme Database: 2.4.1.116
            CAS: 70248-66-7
///
ENTRY       EC 2.4.1.117                Enzyme
NAME        dolichyl-phosphate beta-glucosyltransferase;
            polyprenyl phosphate:UDP-D-glucose glucosyltransferase;
            UDP-glucose dolichyl-phosphate glucosyltransferase;
            uridine diphosphoglucose-dolichol glucosyltransferase;
            UDP-glucose:dolichol phosphate glucosyltransferase;
            UDP-glucose:dolicholphosphoryl glucosyltransferase;
            UDP-glucose:dolichyl monophosphate glucosyltransferase;
            UDP-glucose:dolichyl phosphate glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:dolichyl-phosphate beta-D-glucosyltransferase
REACTION    UDP-glucose + dolichyl phosphate = UDP + dolichyl beta-D-glucosyl
            phosphate [RN:R01005]
ALL_REAC    R01005
SUBSTRATE   UDP-glucose [CPD:C00029];
            dolichyl phosphate [CPD:C00110]
PRODUCT     UDP [CPD:C00015];
            dolichyl beta-D-glucosyl phosphate [CPD:C01246]
COMMENT     Solanesyl phosphate and ficaprenyl phosphate can act as acceptors,
            but more slowly.
REFERENCE   1  [PMID:5273893]
  AUTHORS   Behrens NH, Leloir LF.
  TITLE     Dolichol monophosphate glucose: an intermediate in glucose transfer
            in liver.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 66 (1970) 153-9.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:849929]
  AUTHORS   Herscovics A, Bugge B, Jeanloz RW.
  TITLE     Glucosyltransferase activity in calf pancreas microsomes. Formation
            of dolichyl D[14C]glucosyl phosphate and 14C-labeled lipid-linked
            oligosaccharides from UDP-D-[14C]glucose.
  JOURNAL   J. Biol. Chem. 252 (1977) 2271-7.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:438216]
  AUTHORS   Villemez CL, Carlo PL.
  TITLE     Properties of a soluble polyprenyl phosphate: UDP-D-glucose
            glucosyltransferase.
  JOURNAL   J. Biol. Chem. 254 (1979) 4814-9.
  ORGANISM  Acanthamoeba castellani
PATHWAY     PATH: map00510  N-Glycan biosynthesis
ORTHOLOGY   KO: K00729  dolichyl-phosphate beta-glucosyltransferase
GENES       HSA: 29880(ALG5)
            PTR: 452541(ALG5)
            MMU: 66248(Alg5)
            RNO: 295051(Alg5)
            CFA: 477301(ALG5)
            BTA: 506566(ALG5)
            GGA: 418898(ALG5)
            XLA: 379570(MGC69100) 380326(alg5)
            XTR: 448472(alg5)
            DRE: 751635(zgc:153378)
            SPU: 578155(LOC578155)
            DME: Dmel_CG7870
            CEL: H43I07.3
            ATH: AT2G39630
            OSA: 4334604
            CME: CMK197C
            SCE: YPL227C(ALG5)
            AGO: AGOS_AFL133C
            PIC: PICST_57548(ALG5)
            CGR: CAGL0E06028g
            SPO: SPBC56F2.10c
            ANI: AN7715.2
            AFM: AFUA_5G08210
            AOR: AO090701000739
            UMA: UM01231.1
            DDI: DDB_0191396(dgtA)
            CPV: cgd5_2590
            CHO: Chro.50118
            TET: TTHERM_00047110
            GME: Gmet_0242
            PCA: Pcar_1758
            BBA: Bd2270
            ABA: Acid345_0505
            RHA: RHA1_ro04108
            FAL: FRAAL3989 FRAAL4856
            HWA: HQ1250A HQ1489A(dpg)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.117
            ExPASy - ENZYME nomenclature database: 2.4.1.117
            ExplorEnz - The Enzyme Database: 2.4.1.117
            ERGO genome analysis and discovery system: 2.4.1.117
            BRENDA, the Enzyme Database: 2.4.1.117
            CAS: 71061-42-2
///
ENTRY       EC 2.4.1.118                Enzyme
NAME        cytokinin 7-beta-glucosyltransferase;
            uridine diphosphoglucose-zeatin 7-glucosyltransferase;
            cytokinin 7-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:zeatin 7-glucosyltransferase
REACTION    UDP-glucose + N6-alkylaminopurine = UDP +
            N6-alkylaminopurine-7-beta-D-glucoside [RN:R04071]
ALL_REAC    R04071
SUBSTRATE   UDP-glucose [CPD:C00029];
            N6-alkylaminopurine [CPD:C02860]
PRODUCT     UDP [CPD:C00015];
            N6-alkylaminopurine-7-beta-D-glucoside [CPD:C04422]
COMMENT     Acts on a range of N6-substituted adenines, including zeatin and
            N6-benzylaminopurine, but not N6-benzyladenine. With some acceptors,
            9-beta-D-glucosides are also formed.
REFERENCE   1
  AUTHORS   Entsch, B. and Letham, D.S.
  TITLE     Enzymic glucosylation of the cytokinin, 6-benzylaminopurine.
  JOURNAL   Plant Sci. Lett. 14 (1979) 205-212.
  ORGANISM  Raphanus sativus
REFERENCE   2  [PMID:486500]
  AUTHORS   Entsch B, Parker CW, Letham DS, Summons RE.
  TITLE     Preparation and characterization, using high-performance liquid
            chromatography, of an enzyme forming glucosides of cytokinins.
  JOURNAL   Biochim. Biophys. Acta. 570 (1979) 124-39.
  ORGANISM  Raphanus sativus
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.118
            ExPASy - ENZYME nomenclature database: 2.4.1.118
            ExplorEnz - The Enzyme Database: 2.4.1.118
            ERGO genome analysis and discovery system: 2.4.1.118
            BRENDA, the Enzyme Database: 2.4.1.118
            CAS: 72103-03-8
///
ENTRY       EC 2.4.1.119                Enzyme
NAME        dolichyl-diphosphooligosaccharide---protein glycotransferase;
            dolichyldiphosphooligosaccharide-protein glycosyltransferase;
            asparagine N-glycosyltransferase;
            dolichyldiphosphooligosaccharide-protein oligosaccharyltransferase;
            dolichylpyrophosphodiacetylchitobiose-protein glycosyltransferase;
            oligomannosyltransferase;
            oligosaccharide transferase;
            dolichyldiphosphoryloligosaccharide-protein
            oligosaccharyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     dolichyl-diphosphooligosaccharide:protein-L-asparagine
            oligopolysaccharidotransferase
REACTION    dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl
            diphosphate + a glycoprotein with the oligosaccharide chain attached
            by N-glycosyl linkage to protein L-asparagine [RN:R04216]
ALL_REAC    R04216 > R05976(G)
SUBSTRATE   dolichyl diphosphooligosaccharide [CPD:C04213];
            protein L-asparagine [CPD:C03021]
PRODUCT     dolichyl diphosphate [CPD:C00621];
            glycoprotein with the oligosaccharide chain attached by N-glycosyl
            linkage to protein L-asparagine [CPD:C11572]
COMMENT     Transfers the glucosyl-mannosyl-glucosamine polysaccharide
            side-chains of glycoproteins to an asparagine residue in the
            sequence Asn-Xaa-Ser or Asn-Xaa-Thr in the nascent polypeptide
            chains of the protein moiety.
REFERENCE   1  [PMID:6933437]
  AUTHORS   Das RC, Heath EC.
  TITLE     Dolichyldiphosphoryloligosaccharide--protein
            oligosaccharyltransferase; solubilization, purification, and
            properties.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 77 (1980) 3811-5.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00730  dolichyl-diphosphooligosaccharide--protein
                        glycosyltransferase
GENES       HSA: 1650(DDOST) 201595(STT3B) 6184(RPN1) 6185(RPN2)
            MMU: 103963(Rpn1) 13200(Ddost) 20014(Rpn2) 68292(Stt3b)
            RNO: 25596(Rpn1) 313648(Ddost_predicted) 64701(Rpn2)
            CFA: 404012(DDOST) 476516(RPN1) 477223(RPN2)
            BTA: 534231(RPN2) 539818(MGC152360)
            SSC: 396981(RPN2) 397385(OST48) 397606(RPN1)
            GGA: 395343(DAD1) 416017(RPN1) 425542(DDOST) 428444(RCJMB04_8n14)
            XLA: 379348(MGC53764) 398514(MGC52808) 398521(MGC52894)
                 444283(DDOST)
            XTR: 395031(TNeu084m06.1) 496959(LOC496959)
            DRE: 325561(rpn1) 335985(rpn2) 406408(ddost)
            SPU: 577281(LOC577281) 578649(LOC578649) 581211(LOC581211)
            DME: Dmel_CG9022(Ost48)
            CEL: T09A5.11 T22D1.4(glycotransferase)
            ATH: AT1G76400 AT5G66680(DGL1)
            OSA: 4338348 4342702
            CME: CMK108C
            SCE: YDL232W(OST4) YEL002C(WBP1) YGL022W(STT3) YGL226C-A(OST5)
                 YJL002C(OST1) YML019W(OST6) YMR149W(SWP1) YOR085W(OST3)
                 YOR103C(OST2)
            AGO: AGOS_AAL170W AGOS_ABL170C AGOS_ADL003C AGOS_ADL261C
                 AGOS_AER330W AGOS_AER413C
            PIC: PICST_42114(OST1) PICST_56184(OST6) PICST_58859(OST2)
                 PICST_65168(OST3) PICST_82607(STT3) PICST_86222(WBP1)
            CGR: CAGL0B04499g CAGL0D05742g CAGL0J08569g CAGL0L02365g
            SPO: SPAC27F1.07 SPAC6F6.05 SPAPB17E12.11 SPCC338.15
            ANI: AN4683.2 AN7472.2
            AFM: AFUA_1G03810 AFUA_2G05790 AFUA_5G08970
            AOR: AO090001000698 AO090020000468
            CNE: CNJ01460 CNJ01740
            UMA: UM04198.1 UM04994.1 UM05769.1
            DDI: DDB_0233146(ost1) DDB_0233148(wbp1)
            PFA: PFI0960w
            CPV: cgd2_1650 cgd6_5070
            CHO: Chro.20179 Chro.60585
            TET: TTHERM_00043890 TTHERM_00772030 TTHERM_01006550
            EHI: 192.t00010 248.t00006 32.t00005 364.t00008
STRUCTURES  PDB: 1RKL  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.119
            ExPASy - ENZYME nomenclature database: 2.4.1.119
            ExplorEnz - The Enzyme Database: 2.4.1.119
            ERGO genome analysis and discovery system: 2.4.1.119
            BRENDA, the Enzyme Database: 2.4.1.119
            CAS: 75302-32-8
///
ENTRY       EC 2.4.1.120                Enzyme
NAME        sinapate 1-glucosyltransferase;
            uridine diphosphoglucose-sinapate glucosyltransferase;
            UDP-glucose:sinapic acid glucosyltransferase;
            uridine 5'-diphosphoglucose-hydroxycinnamic acid
            acylglucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:sinapate D-glucosyltransferase
REACTION    UDP-glucose + sinapate = UDP + 1-sinapoyl-D-glucose [RN:R02380]
ALL_REAC    R02380
SUBSTRATE   UDP-glucose [CPD:C00029];
            sinapate [CPD:C00482]
PRODUCT     UDP [CPD:C00015];
            1-sinapoyl-D-glucose [CPD:C02919]
COMMENT     Some other hydroxycinnamates, including 4-coumarate, ferulate and
            caffeate, can act as acceptors, but more slowly. Only glucose
            esters, not glucosides, are formed (cf. EC 2.4.1.126
            hydroxycinnamate 4-beta-glucosyltransferase).
REFERENCE   1
  AUTHORS   Strack, D.
  TITLE     Enzymatic synthesis of 1-sinapoylglucose from free sinapic acid and
            UDP-glucose by a cell free system from Raphanus sativus seedlings.
  JOURNAL   Z. Naturforsch. C: Biosci. 35 (1980) 204-208.
  ORGANISM  Raphanus sativus
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.120
            ExPASy - ENZYME nomenclature database: 2.4.1.120
            ExplorEnz - The Enzyme Database: 2.4.1.120
            ERGO genome analysis and discovery system: 2.4.1.120
            BRENDA, the Enzyme Database: 2.4.1.120
            CAS: 74082-53-4
///
ENTRY       EC 2.4.1.121                Enzyme
NAME        indole-3-acetate beta-glucosyltransferase;
            uridine diphosphoglucose-indoleacetate glucosyltransferase;
            UDPG-indol-3-ylacetyl glucosyl transferase;
            UDP-glucose:indol-3-ylacetate glucosyltransferase;
            indol-3-ylacetylglucose synthase;
            UDP-glucose:indol-3-ylacetate glucosyl-transferase;
            IAGlu synthase;
            IAA-glucose synthase;
            UDP-glucose:indole-3-acetate beta-D-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:(indol-3-yl)acetate beta-D-glucosyltransferase
REACTION    UDP-glucose + (indol-3-yl)acetate = UDP +
            1-O-(indol-3-yl)acetyl-beta-D-glucose [RN:R03094]
ALL_REAC    R03094
SUBSTRATE   UDP-glucose [CPD:C00029];
            (indol-3-yl)acetate [CPD:C00954]
PRODUCT     UDP [CPD:C00015];
            1-O-(indol-3-yl)acetyl-beta-D-glucose
REFERENCE   1  [PMID:6218801]
  AUTHORS   Michalczuk L, Bandurski RS.
  TITLE     Enzymic synthesis of 1-O-indol-3-ylacetyl-beta-D-glucose and
            indol-3-ylacetyl-myo-inositol.
  JOURNAL   Biochem. J. 207 (1982) 273-81.
  ORGANISM  Zea mays [GN:ezma]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.121
            ExPASy - ENZYME nomenclature database: 2.4.1.121
            ExplorEnz - The Enzyme Database: 2.4.1.121
            ERGO genome analysis and discovery system: 2.4.1.121
            BRENDA, the Enzyme Database: 2.4.1.121
            CAS: 74082-56-7
///
ENTRY       EC 2.4.1.122                Enzyme
NAME        glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase;
            uridine diphosphogalactose-mucin beta-(1->3)-galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:glycoprotein-N-acetyl-D-galactosamine
            3-beta-D-galactosyltransferase
REACTION    UDP-galactose + glycoprotein N-acetyl-D-galactosamine = UDP +
            glycoprotein D-galactosyl-1,3-N-acetyl-D-galactosamine [RN:R05908]
ALL_REAC    R05908(G)
SUBSTRATE   UDP-galactose [CPD:C00052];
            glycoprotein N-acetyl-D-galactosamine
PRODUCT     UDP [CPD:C00015];
            glycoprotein D-galactosyl-1,3-N-acetyl-D-galactosamine [CPD:C04750]
COMMENT     The non-reducing O-serine-linked N-acetylgalactosamine residues in
            mucin glycoproteins can act as acceptors.
REFERENCE   1  [PMID:6789880]
  AUTHORS   Hesford FJ, Berger EG, Van den Eijnden DH.
  TITLE     Identification of the product formed by human erythrocyte
            galactosyltransferase.
  JOURNAL   Biochim. Biophys. Acta. 659 (1981) 302-11.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:6801057]
  AUTHORS   Mendicino J, Sivakami S, Davila M, Chandrasekaran EV.
  TITLE     Purification and properties of UDP-gal:N-acetylgalactosaminide
            mucin: beta 1,3-galactosyltransferase from swine trachea mucosa.
  JOURNAL   J. Biol. Chem. 257 (1982) 3987-94.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:6366476]
  AUTHORS   Schachter H, Narasimhan S, Gleeson P, Vella G.
  TITLE     Glycosyltransferases involved in elongation of N-glycosidically
            linked oligosaccharides of the complex or N-acetyllactosamine type.
  JOURNAL   Methods. Enzymol. 98 (1983) 98-134.
PATHWAY     PATH: map00512  O-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00731  glycoprotein-N-acetylgalactosamine
                        3-beta-galactosyltransferase
GENES       HSA: 56913(C1GALT1)
            PTR: 472288(C1GALT1)
            MMU: 94192(C1galt1)
            RNO: 65044(C1galt1)
            CFA: 482314(C1GALT1)
            BTA: 539417(MGC142672)
            GGA: 420575(C1GALT1)
            DRE: 337131(c1galt1)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.122
            ExPASy - ENZYME nomenclature database: 2.4.1.122
            ExplorEnz - The Enzyme Database: 2.4.1.122
            ERGO genome analysis and discovery system: 2.4.1.122
            BRENDA, the Enzyme Database: 2.4.1.122
            CAS: 97089-61-7
///
ENTRY       EC 2.4.1.123                Enzyme
NAME        inositol 3-alpha-galactosyltransferase;
            UDP-D-galactose:inositol galactosyltransferase;
            UDP-galactose:myo-inositol 1-alpha-D-galactosyltransferase;
            UDPgalactose:myo-inositol 1-alpha-D-galactosyltransferase;
            galactinol synthase;
            inositol 1-alpha-galactosyltransferase;
            uridine diphosphogalactose-inositol galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:myo-inositol 3-alpha-D-galactosyltransferase
REACTION    UDP-galactose + myo-inositol = UDP +
            O-alpha-D-galactosyl-(1->3)-1D-myo-inositol [RN:R01192 R06214]
ALL_REAC    R01192 R06214(G)
SUBSTRATE   UDP-galactose [CPD:C00052];
            myo-inositol [CPD:C00137]
PRODUCT     UDP [CPD:C00015];
            O-alpha-D-galactosyl-(1->3)-1D-myo-inositol
COMMENT     An enzyme from plants involved in the formation of raffinose and
            stachyose [cf. EC 2.4.1.67 (galactinol---raffinose
            galactosyltransferase) and EC 2.4.1.82 (galactinol---sucrose
            galactosyltransferase)].
REFERENCE   1
  AUTHORS   Pharr, D.M., Sox, H.N., Locy, R.D. and Huber, S.C.
  TITLE     Partial characterization of the galactinol forming enzyme from
            leaves of Cucumis sativus L.
  JOURNAL   Plant Sci. Lett. 23 (1981) 25-33.
  ORGANISM  Cucumis sativus
PATHWAY     PATH: map00052  Galactose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.123
            ExPASy - ENZYME nomenclature database: 2.4.1.123
            ExplorEnz - The Enzyme Database: 2.4.1.123
            ERGO genome analysis and discovery system: 2.4.1.123
            BRENDA, the Enzyme Database: 2.4.1.123
            CAS: 79955-89-8
///
ENTRY       EC 2.4.1.124      Obsolete  Enzyme
NAME        Transferred to 2.4.1.87
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Transferred entry: now EC 2.4.1.87 N-acetyllactosaminide
            3-alpha-galactosyltransferase (EC 2.4.1.124 created 1984, deleted
            2002)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.124
            ExPASy - ENZYME nomenclature database: 2.4.1.124
            ExplorEnz - The Enzyme Database: 2.4.1.124
            ERGO genome analysis and discovery system: 2.4.1.124
            BRENDA, the Enzyme Database: 2.4.1.124
///
ENTRY       EC 2.4.1.125                Enzyme
NAME        sucrose---1,6-alpha-glucan 3(6)-alpha-glucosyltransferase;
            water-soluble-glucan synthase;
            GTF-S;
            sucrose-1,6-alpha-glucan 3(6)-alpha-glucosyltransferase;
            sucrose:1,6-alpha-D-glucan 3-alpha- and 6-alpha-glucosyltransferase;
            sucrose:1,6-, 1,3-alpha-D-glucan 3-alpha- and
            6-alpha-D-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     sucrose:1,6-alpha-D-glucan 3(6)-alpha-D-glucosyltransferase
REACTION    sucrose + (1,6-alpha-D-glucosyl)n = D-fructose +
            (1,6-alpha-D-glucosyl)n+1 [RN:R02120 R06066]
ALL_REAC    R02120 R06066(G)
SUBSTRATE   sucrose [CPD:C00089];
            (1,6-alpha-D-glucosyl)n [CPD:C00372]
PRODUCT     D-fructose [CPD:C00095];
            (1,6-alpha-D-glucosyl)n+1 [CPD:C00372]
COMMENT     Also transfers glucosyl residues to the 3-position on glucose
            residues in glucans, producing a highly-branched 1,6-alpha-D-glucan.
REFERENCE   1  [PMID:6216919]
  AUTHORS   Mukasa H, Shimamura A, Tsumori H.
  TITLE     Purification and characterization of basic glucosyltransferase from
            Streptococcus mutans serotype c.
  JOURNAL   Biochim. Biophys. Acta. 719 (1982) 81-9.
  ORGANISM  Streptococcus mutans [GN:smu]
REFERENCE   2  [PMID:6461359]
  AUTHORS   Shimamura A, Tsumori H, Mukasa H.
  TITLE     Purification and properties of Streptococcus mutans extracellular
            glucosyltransferase.
  JOURNAL   Biochim. Biophys. Acta. 702 (1982) 72-80.
  ORGANISM  Streptococcus mutans [GN:smu]
REFERENCE   3  [PMID:2937877]
  AUTHORS   Tsumori H, Shimamura A, Mukasa H.
  TITLE     Purification and properties of extracellular glucosyltransferase
            synthesizing 1,6-, 1,3-alpha-D-glucan from Streptococcus mutans
            serotype a.
  JOURNAL   J. Gen. Microbiol. 131 (1985) 3347-53.
  ORGANISM  Streptococcus mutans [GN:smu]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.125
            ExPASy - ENZYME nomenclature database: 2.4.1.125
            ExplorEnz - The Enzyme Database: 2.4.1.125
            ERGO genome analysis and discovery system: 2.4.1.125
            BRENDA, the Enzyme Database: 2.4.1.125
            CAS: 81725-87-3
///
ENTRY       EC 2.4.1.126                Enzyme
NAME        hydroxycinnamate 4-beta-glucosyltransferase;
            uridine diphosphoglucose-hydroxycinnamate glucosyltransferase;
            UDP-glucose-hydroxycinnamate glucosyltransferase;
            hydroxycinnamoyl glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:trans-4-hydroxycinnamate 4-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + trans-4-hydroxycinnamate = UDP +
            4-O-beta-D-glucosyl-4-hydroxycinnamate [RN:R02951]
ALL_REAC    R02951
SUBSTRATE   UDP-glucose [CPD:C00029];
            trans-4-hydroxycinnamate [CPD:C00811]
PRODUCT     UDP [CPD:C00015];
            4-O-beta-D-glucosyl-4-hydroxycinnamate [CPD:C04415]
COMMENT     Acts on 4-coumarate, ferulate, caffeate and sinapate, forming a
            mixture of 4-glucosides and glucose esters (cf. EC 2.4.1.120
            sinapate 1-glucosyltransferase).
REFERENCE   1
  AUTHORS   Fleuriet, A., Macheix, J.J., Suen, R. and Ibrahim, R.K.
  TITLE     Partial purifiction and some properties of a hydroxycinnamoyl
            glucosyltransferase from tomato fruits.
  JOURNAL   Z. Naturforsch. C: Biosci. 35 (1980) 967-972.
  ORGANISM  Lycopersicon esculentum [GN:eles]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.126
            ExPASy - ENZYME nomenclature database: 2.4.1.126
            ExplorEnz - The Enzyme Database: 2.4.1.126
            ERGO genome analysis and discovery system: 2.4.1.126
            BRENDA, the Enzyme Database: 2.4.1.126
            CAS: 77848-85-2
///
ENTRY       EC 2.4.1.127                Enzyme
NAME        monoterpenol beta-glucosyltransferase;
            uridine diphosphoglucose-monoterpenol glucosyltransferase;
            UDPglucose:monoterpenol glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:(-)-menthol O-beta-D-glucosyltransferase
REACTION    UDP-glucose + (-)-menthol = UDP + (-)-menthyl O-beta-D-glucoside
            [RN:R02179]
ALL_REAC    R02179
SUBSTRATE   UDP-glucose [CPD:C00029];
            (-)-menthol [CPD:C00400]
PRODUCT     UDP [CPD:C00015];
            (-)-menthyl O-beta-D-glucoside [CPD:C03962]
COMMENT     (+)-Neomenthol can also act as acceptor.
REFERENCE   1
  AUTHORS   Fleuriet, A., Macheix, J.J., Suen, R. and Ibrahim, R.K.
  TITLE     Partial purifiction and some properties of a hydroxycinnamoyl
            glucosyltransferase from tomato fruits.
  JOURNAL   Z. Naturforsch. C: Biosci. 35 (1980) 967-972.
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.127
            ExPASy - ENZYME nomenclature database: 2.4.1.127
            ExplorEnz - The Enzyme Database: 2.4.1.127
            ERGO genome analysis and discovery system: 2.4.1.127
            BRENDA, the Enzyme Database: 2.4.1.127
            CAS: 78990-64-4
///
ENTRY       EC 2.4.1.128                Enzyme
NAME        scopoletin glucosyltransferase;
            uridine diphosphoglucose-scopoletin glucosyltransferase;
            UDP-glucose:scopoletin glucosyltransferase;
            SGTase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:scopoletin O-beta-D-glucosyltransferase
REACTION    UDP-glucose + scopoletin = UDP + scopolin [RN:R03594]
ALL_REAC    R03594
SUBSTRATE   UDP-glucose [CPD:C00029];
            scopoletin [CPD:C01752]
PRODUCT     UDP [CPD:C00015];
            scopolin [CPD:C01527]
REFERENCE   1
  AUTHORS   Hino, F., Okazaki, M. and Miura, Y.
  TITLE     Effect of 2,4-dichlorophenoxyacetic acid on glucosylation of
            scopoletin to scopolin in tobacco tissue-culture.
  JOURNAL   Plant Physiol. 69 (1982) 810-813.
  ORGANISM  Nicotiana tabacum
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.128
            ExPASy - ENZYME nomenclature database: 2.4.1.128
            ExplorEnz - The Enzyme Database: 2.4.1.128
            ERGO genome analysis and discovery system: 2.4.1.128
            BRENDA, the Enzyme Database: 2.4.1.128
            CAS: 81210-69-7
///
ENTRY       EC 2.4.1.129                Enzyme
NAME        peptidoglycan glycosyltransferase;
            PG-II;
            bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-
            pentapeptide:peptidoglycan
            N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase;
            penicillin binding protein (3 or 1B);
            peptidoglycan transglycosylase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1->4)-(N-acetyl-D-mu
            ramoylpentapeptide):undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(
            1->4)-N-acetyl-D-muramoylpentapeptide) disaccharidetransferase
REACTION    [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-
            diphosphoundecaprenol +
            GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
            diphosphoundecaprenol =
            [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-
            diphosphoundecaprenol + undecaprenyl diphosphate [RN:R06178 R06179]
ALL_REAC    R06178 R06179(G);
            (other) R04519 R06177(G)
SUBSTRATE   [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-
            diphosphoundecaprenol;
            GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
            diphosphoundecaprenol
PRODUCT     [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-
            diphosphoundecaprenol;
            undecaprenyl diphosphate [CPD:C03543]
COMMENT     The enzyme also works when the lysine residue is replaced by
            meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm)
            combined with adjacent residues through its L-centre, as it is in
            Gram-negative and some Gram-positive organisms. The undecaprenol
            involved is ditrans,octacis-undecaprenol (for definitions, click
            here). Involved in the synthesis of cell-wall peptidoglycan.
REFERENCE   1  [PMID:6802846]
  AUTHORS   Taku A, Stuckey M, Fan DP.
  TITLE     Purification of the peptidoglycan transglycosylase of Bacillus
            megaterium.
  JOURNAL   J. Biol. Chem. 257 (1982) 5018-22.
  ORGANISM  Bacillus megaterium
REFERENCE   2  [PMID:9841666]
  AUTHORS   Goffin C, Ghuysen JM.
  TITLE     Multimodular penicillin-binding proteins: an enigmatic family of
            orthologs and paralogs.
  JOURNAL   Microbiol. Mol. Biol. Rev. 62 (1998) 1079-93.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:11320055]
  AUTHORS   van Heijenoort  J.
  TITLE     Formation of the glycan chains in the synthesis of bacterial
            peptidoglycan.
  JOURNAL   Glycobiology. 11 (2001) 25R-36R.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00550  Peptidoglycan biosynthesis
ORTHOLOGY   KO: K03587  cell division protein FtsI (penicillin binding protein
                        3)
            KO: K05364  peptidoglycan glycosyltransferase
            KO: K05365  penicillin binding protein 1B
GENES       ECO: b0084(ftsI) b0149(mrcB)
            ECJ: JW0082(ftsI) JW0145(mrcB)
            ECE: Z0094(ftsI) Z0160(mrcB)
            ECS: ECs0088 ECs0153
            ECC: c0102(ftsI) c0183(mrcB)
            ECI: UTI89_C0093(ftsI) UTI89_C0164(mrcB)
            ECP: ECP_0086 ECP_0159
            ECV: APECO1_1836(mrcB) APECO1_1902(ftsI)
            ECW: EcE24377A_0086(ftsI) EcE24377A_0153(mrcB)
            ECX: EcHS_A0090(ftsI) EcHS_A0152
            STY: STY0142(ftsI) STY0215(mrcB)
            STT: t0126(ftsI) t0198(mrcB)
            SPT: SPA0124(ftsI) SPA0196(mrcB)
            SEC: SC0119(ftsI) SC0190(mrcB)
            STM: STM0122(ftsI) STM0190(mrcB)
            YPE: YPO0549(ftsI) YPO3393(mrcB)
            YPK: y0795(mrcB) y3632(ftsI)
            YPM: YP_0292(mrcB) YP_3635(ftsI)
            YPA: YPA_2893 YPA_3552
            YPN: YPN_0415 YPN_0697
            YPP: YPDSF_2649 YPDSF_2963 YPDSF_3093
            YPS: YPTB0682(ftsI) YPTB0738(mrcB)
            SFL: SF0081(ftsI) SF0141(mrcB)
            SFX: S0083(ftsI) S0144(mrcB)
            SFV: SFV_0077(ftsI) SFV_0134(mrcB)
            SSN: SSON_0092(ftsI) SSON_0161(mrcB)
            SBO: SBO_0072(ftsI) SBO_0138(mrcB)
            SDY: SDY_0114(ftsI) SDY_0165(mrcB)
            ECA: ECA3313(mrcB) ECA3821(ftsI)
            PLU: plu0883(mrcB) plu3660(ftsI)
            BUC: BU200(mrcB) BU222(ftsI)
            BAS: BUsg216(ftsI)
            BAB: bbp186(mrcB) bbp204(ftsI)
            WBR: WGLp212(ftsI) WGLp596(mrcB)
            SGL: SG0443 SG0494
            ENT: Ent638_0630 Ent638_0689 Ent638_1170 Ent638_2392
            SPE: Spro_0755 Spro_1201 Spro_2356 Spro_2357 Spro_3981
            BFL: Bfl136(ftsI) Bfl154(mrcB)
            BPN: BPEN_140(ftsI) BPEN_159(mrcB)
            HIN: HI1132(ftsI) HI1725(ponB)
            HIT: NTHI1299(ftsI) NTHI2031(mrcB)
            HDU: HD0241(ftsI)
            HSO: HS_0352(ftsI) HS_0825(ponB)
            PMU: PM0136(ftsI) PM0456(ponB)
            MSU: MS1673(ftsI)
            APL: APL_0012(ftsI) APL_1823(pbpB)
            ASU: Asuc_0697 Asuc_1028 Asuc_1938
            XFA: XF0792 XF0884
            XFT: PD1796(ponB) PD1871(ftsI)
            XCC: XCC0720(ftsI) XCC2932(ponB)
            XCB: XC_1176 XC_3515
            XCV: XCV0825(ftsI) XCV3241(mcrB)
            XAC: XAC0774(ftsI) XAC3109(ponB)
            XOO: XOO1739(ponB) XOO3831(ftsI)
            XOM: XOO_1640(XOO1640) XOO_3609(XOO3609)
            VCH: VC0602 VC2407
            VVU: VV1_0584(ftsI) VV1_1651
            VVY: VV0608(ftsI) VV2756
            VPA: VP0454 VP2497
            VFI: VF2162 VF2207(ftsI)
            PPR: PBPRA3167(mrcB) PBPRA3221 PBPRB0616(mrcB)
            PAE: PA4418(ftsI) PA4700(mrcB)
            PAU: PA14_57425(ftsI) PA14_62200(mrcB)
            PPU: PP_1331(ftsI) PP_4683(mrcB)
            PPF: Pput_2022 Pput_4393 Pput_4547 Pput_4682 Pput_4957
            PST: PSPTO_0977 PSPTO_4414
            PSB: Psyr_0842 Psyr_4108
            PSP: PSPPH_0868 PSPPH_4114(ftsI)
            PFL: PFL_5067 PFL_5258
            PFO: Pfl_3903 Pfl_4679 Pfl_4792
            PEN: PSEEN2489 PSEEN4491(ftsI) PSEEN4715(mrcB) PSEEN4826(pbpA)
            PMY: Pmen_0541 Pmen_0916 Pmen_1002 Pmen_3798
            PAR: Psyc_1468(mrcB) Psyc_2054(ftsI)
            PCR: Pcryo_1646 Pcryo_1745 Pcryo_2378
            PRW: PsycPRwf_0134 PsycPRwf_0800 PsycPRwf_1620
            ACI: ACIAD2234(mrcB) ACIAD3366(ftsI)
            SON: SO_0633(mrcB) SO_4225(ftsI)
            SDN: Sden_0349 Sden_0855 Sden_3164
            SFR: Sfri_0699 Sfri_3270 Sfri_3810
            SAZ: Sama_0348 Sama_2588 Sama_2971
            SBL: Sbal_0396 Sbal_0583 Sbal_3275
            SBM: Shew185_0395 Shew185_3317 Shew185_3742
            SLO: Shew_2935 Shew_3123 Shew_3459
            SPC: Sputcn32_0481 Sputcn32_0656 Sputcn32_2869
            SSE: Ssed_0404 Ssed_3485 Ssed_3894 Ssed_4271
            SPL: Spea_0705 Spea_3149 Spea_3817
            SHE: Shewmr4_0624 Shewmr4_0991 Shewmr4_3576
            SHM: Shewmr7_0380 Shewmr7_1056 Shewmr7_3406
            SHN: Shewana3_0623 Shewana3_3540 Shewana3_3749
            SHW: Sputw3181_0384 Sputw3181_1034 Sputw3181_3518
            ILO: IL0430(ftsI) IL2246(mrcB)
            CPS: CPS_4301 CPS_4471(ftsI)
            PHA: PSHAa2256(mrcB) PSHAa2510(ftsI)
            PAT: Patl_0489 Patl_1560 Patl_3525
            SDE: Sde_0825 Sde_0842 Sde_3341
            PIN: Ping_0596 Ping_1135 Ping_1141 Ping_2163
            MAQ: Maqu_0679 Maqu_0825 Maqu_2413 Maqu_2458
            CBU: CBU_0118(pbpB)
            LPN: lpg0916(pbpB)
            LPF: lpl0947(ftsI)
            LPP: lpp0977(ftsI)
            MCA: MCA1672 MCA2434(ftsI)
            FTU: FTT0697(ftsI)
            FTF: FTF0697(ftsI)
            FTW: FTW_1546
            FTL: FTL_1539
            FTH: FTH_1489(ftsI)
            FTN: FTN_0607(ftsI)
            TCX: Tcr_0562 Tcr_1633
            NOC: Noc_2867
            AEH: Mlg_0172 Mlg_1154 Mlg_2199
            HHA: Hhal_1008 Hhal_2097 Hhal_2253
            HCH: HCH_05889(ftsI) HCH_06250(mrcB)
            CSA: Csal_1545 Csal_2196
            ABO: ABO_0351(mrcB) ABO_0592(ftsI)
            MMW: Mmwyl1_1239 Mmwyl1_2620 Mmwyl1_2848 Mmwyl1_4121
            AHA: AHA_3530(mrcB) AHA_3890(ftsI)
            DNO: DNO_0987(ftsI)
            RMA: Rmag_0296 Rmag_0797
            NME: NMB0413
            NMA: NMA2072(penA)
            NGO: NGO1542
            CVI: CV_4349(ftsI)
            RSO: RSc2850(ftsI)
            REU: Reut_A0079 Reut_A2985 Reut_B3673 Reut_B4875
            REH: H16_A3279(ftsI1)
            RME: Rmet_3134 Rmet_4835
            BMA: BMA2557(ftsI) BMAA1056 BMAA1082
            BMV: BMASAVP1_A0478(ftsI)
            BML: BMA10299_A1337(ftsI)
            BMN: BMA10247_3226(ftsI)
            BXE: Bxe_A0480 Bxe_B2238
            BVI: Bcep1808_0369 Bcep1808_0529 Bcep1808_3197 Bcep1808_3519
                 Bcep1808_4797 Bcep1808_4891
            BUR: Bcep18194_A3639 Bcep18194_A5259 Bcep18194_A6464
                 Bcep18194_B0214 Bcep18194_B0392 Bcep18194_B0509
                 Bcep18194_B1290 Bcep18194_B1659 Bcep18194_B1788
            BCN: Bcen_0071 Bcen_2499 Bcen_3108 Bcen_4006 Bcen_4139 Bcen_5424
            BCH: Bcen2424_0553 Bcen2424_3113 Bcen2424_4227 Bcen2424_4361
                 Bcen2424_5259 Bcen2424_5438
            BAM: Bamb_0306 Bamb_0457 Bamb_3168 Bamb_3649 Bamb_3770 Bamb_4779
            BPS: BPSL3031(ftsI) BPSS1219 BPSS1240(ftsI)
            BPM: BURPS1710b_3551(ftsI) BURPS1710b_A0213(ftsI)
                 BURPS1710b_A0239(ftsI)
            BTE: BTH_I1112 BTH_II1197
            PNU: Pnuc_0092 Pnuc_0161 Pnuc_2024
            BPE: BP3028(ftsI)
            BPA: BPP3757(ftsI)
            BBR: BB4203(ftsI)
            RFR: Rfer_3431 Rfer_3920
            POL: Bpro_0225 Bpro_1069 Bpro_2084
            PNA: Pnap_0176 Pnap_0671 Pnap_3423
            AAV: Aave_0297 Aave_0815 Aave_0995
            AJS: Ajs_0242 Ajs_0729 Ajs_3676
            VEI: Veis_0023 Veis_1607 Veis_4564
            MPT: Mpe_A0456
            HAR: HEAR1632 HEAR2817(ftsI) HEAR3126(mrcA)
            NEU: NE0985(ftsI)
            NET: Neut_0252 Neut_1589
            NMU: Nmul_A2500
            EBA: ebA1451(ftsI) ebA1739(mtgA)
            AZO: azo0878(ftsI)
            DAR: Daro_3504
            TBD: Tbd_0113
            MFA: Mfla_2275 Mfla_2494
            HPA: HPAG1_1505 HPAG1_1514
            HAC: Hac_1663(ftsI)
            TDN: Tmden_0362 Tmden_1073
            ABU: Abu_1902(pbpA)
            GSU: GSU3075
            GME: Gmet_0406
            GUR: Gura_2430 Gura_2858 Gura_3980 Gura_4406
            PCA: Pcar_2208 Pcar_2557
            PPD: Ppro_0080 Ppro_2545 Ppro_3195 Ppro_3295
            DVU: DVU2510
            DVL: Dvul_0735 Dvul_2187 Dvul_2326
            DDE: Dde_0993 Dde_1036 Dde_3124
            LIP: LI1098(ftsI)
            BBA: Bd3213
            DPS: DP2417
            ADE: Adeh_2498 Adeh_3765
            AFW: Anae109_0060 Anae109_1370 Anae109_3405 Anae109_3878
            MXA: MXAN_5610
            SAT: SYN_01739
            SFU: Sfum_0290 Sfum_2589 Sfum_3465
            RFE: RF_0902(pbpA2)
            RBE: RBE_0542(pbpA2)
            WOL: WD1273
            AMA: AM418(pbpA2)
            PUB: SAR11_0029(ftsI)
            MLO: mll1561
            MES: Meso_2013
            PLA: Plav_0008 Plav_0897 Plav_2415 Plav_2482 Plav_3276
            SME: SMc01860(ftsI)
            SMD: Smed_0626 Smed_0960 Smed_2088 Smed_3388 Smed_5367
            ATU: Atu2100
            RET: RHE_CH02853(ftsI)
            RLE: RL3313
            BME: BMEI0573
            BMS: BR1437
            BMB: BruAb1_1432
            OAN: Oant_0131 Oant_1738 Oant_2266 Oant_2677
            BJA: bll6608
            BRA: BRADO0522 BRADO2718 BRADO3920(pbpC) BRADO5665(ftsI)
            BBT: BBta_3056 BBta_3916(pbpC) BBta_6180(ftsI) BBta_7653
            RPA: RPA3536
            RPB: RPB_1988 RPB_3506
            RPC: RPC_1787 RPC_2188
            RPD: RPD_0124 RPD_1953 RPD_3400
            RPE: RPE_0224 RPE_1880 RPE_2101
            NWI: Nwi_0132 Nwi_1045 Nwi_1716
            NHA: Nham_0227 Nham_1273 Nham_1403
            BQU: BQ08920(ftsI)
            XAU: Xaut_0362 Xaut_1653 Xaut_1850 Xaut_4669
            CCR: CC_2560
            SIL: SPO1181
            SIT: TM1040_0470 TM1040_0867 TM1040_2017 TM1040_2628
            RSP: RSP_2098(ftsI)
            RSH: Rsph17029_0023 Rsph17029_0774 Rsph17029_1000 Rsph17029_1624
                 Rsph17029_2548
            RSQ: Rsph17025_0013 Rsph17025_0118 Rsph17025_0685 Rsph17025_1603
                 Rsph17025_1857
            JAN: Jann_2534 Jann_2767 Jann_3648 Jann_4055
            RDE: RD1_3366
            PDE: Pden_0585 Pden_1816 Pden_2033 Pden_4035
            MMR: Mmar10_0916 Mmar10_2014 Mmar10_2084 Mmar10_2868
            NAR: Saro_1127 Saro_2131 Saro_3329
            SAL: Sala_1630 Sala_1887 Sala_2976
            SWI: Swit_0495 Swit_2817 Swit_3846 Swit_3953
            ELI: ELI_01765
            GOX: GOX0152
            ACR: Acry_0057 Acry_0497 Acry_0658 Acry_1687 Acry_2241
            RRU: Rru_A0105 Rru_A0473 Rru_A0956 Rru_A2147 Rru_A2520 Rru_A3393
            MAG: amb3842
            MGM: Mmc1_0759 Mmc1_1415 Mmc1_2321
            ABA: Acid345_1065 Acid345_1465 Acid345_3635 Acid345_4231
            SUS: Acid_2004 Acid_2509 Acid_4180 Acid_7317
            BAN: BA1474
            BAR: GBAA1474
            BAT: BAS1363
            BCE: BC1455
            BCA: BCE_1578
            BCZ: BCZK1336(pbp2A) BCZK2246(pbp2) BCZK2802(pbp2)
            BCY: Bcer98_1641 Bcer98_2565 Bcer98_2566
            BTK: BT9727_1337(pbp2A)
            BTL: BALH_1310(pbp2A)
            BPU: BPUM_1409(ftsI)
            GKA: GK1608
            SAJ: SaurJH9_0029 SaurJH9_1240
            SAH: SaurJH1_0029 SaurJH1_1265
            LWE: lwe2246
            SPK: MGAS9429_Spy0082(pbp1b)
            SGO: SGO_0586(pbp1a) SGO_1928(pbp1b) SGO_2010(pbp2a)
            LRE: Lreu_0587
            CAC: CAC0329(spoVD)
            CTH: Cthe_0091 Cthe_0979 Cthe_1011 Cthe_3047
            CBE: Cbei_1578 Cbei_1579 Cbei_1900 Cbei_4860
            AMT: Amet_0335 Amet_2223 Amet_2473 Amet_2885
            DSY: DSY1624 DSY2686 DSY3176
            DRM: Dred_0669 Dred_0902 Dred_2100 Dred_2545
            SWO: Swol_0489 Swol_0820 Swol_1109 Swol_1638
            CSC: Csac_0371 Csac_0919 Csac_1869
            TTE: TTE1916(ftsI4)
            MTA: Moth_0540 Moth_0911 Moth_1710
            MTU: Rv2163c(pbpB)
            MTC: MT2221
            MLE: ML0908(pbpB)
            MPA: MAP1903c(pbpB)
            MAV: MAV_0020
            MSM: MSMEG_4233
            MVA: Mvan_3529
            MGI: Mflv_2982
            MMC: Mmcs_0017 Mmcs_3262
            MKM: Mkms_0025 Mkms_3324
            MJL: Mjls_0017 Mjls_3273
            CGL: NCgl2084(cgl2164)
            CEF: CE2059(ftsI)
            CDI: DIP1604(ftsI)
            CJK: jk0744(ftsI)
            NFA: nfa17600
            RHA: RHA1_ro01094 RHA1_ro03441 RHA1_ro03449 RHA1_ro03698
            SCO: SCO2090(ftsI)
            TWH: TWT222(pbpB)
            TWS: TW548(pbp)
            LXX: Lxx15320
            CMI: CMM_1865(ftsI)
            ART: Arth_0022 Arth_1564
            NCA: Noca_0024 Noca_3069 Noca_3462
            TFU: Tfu_1104 Tfu_3064
            FRA: Francci3_1214 Francci3_1409 Francci3_4434
            FAL: FRAAL1919 FRAAL2190(ftsI) FRAAL6857
            ACE: Acel_0020 Acel_0751 Acel_1004
            KRA: Krad_0073 Krad_3205
            SEN: SACE_0046 SACE_5864(ftsI)
            STP: Strop_0046
            BLO: BL1317(ftsI)
            BAD: BAD_0040(pbpA) BAD_1107(ftsI)
            RXY: Rxyl_0022 Rxyl_1138 Rxyl_1310 Rxyl_1498 Rxyl_2308
            CTA: CTA_0292(pbp3)
            CAB: CAB362
            CFE: CF0634(ftsI2)
            BAF: BAPKO_0138(pbp-1)
            LIL: LA3698(ftsI)
            LIC: LIC10528(pbpB)
            LBJ: LBJ_0430(pBP3)
            LBL: LBL_2647(pbp3)
            SYN: sll1833(ftsI)
            SYW: SYNW1760(ftsI)
            SYF: Synpcc7942_0482 Synpcc7942_0580 Synpcc7942_2000
            SYD: Syncc9605_0704
            SYE: Syncc9902_1259 Syncc9902_1654
            SYG: sync_2009(ftsI)
            SYR: SynRCC307_0864(ftsI)
            SYX: SynWH7803_0633(ftsI)
            CYA: CYA_1072
            CYB: CYB_0996
            TEL: tlr2074
            GVI: glr2929
            ANA: alr0718
            AVA: Ava_0950 Ava_2356 Ava_2473 Ava_4620
            PMN: PMN2A_1373 PMN2A_1850
            PMI: PMT9312_0041 PMT9312_0518
            PMB: A9601_05741
            PMC: P9515_05821
            PMF: P9303_07561
            PMG: P9301_05441
            PMH: P9215_05991(ftsI)
            PME: NATL1_05751
            TER: Tery_0878 Tery_1840 Tery_2090 Tery_3016
            BFR: BF0311
            PGI: PG0575
            SRU: SRU_0555
            CHU: CHU_2746(ftsI)
            FJO: Fjoh_1455 Fjoh_1805
            FPS: FP2062(ftsI)
            CTE: CT0040(ftsI)
            CCH: Cag_0049 Cag_0590 Cag_1164
            CPH: Cpha266_0817 Cpha266_2727
            PVI: Cvib_1205 Cvib_1759
            PLT: Plut_0571 Plut_2116
            RRS: RoseRS_1118 RoseRS_1280 RoseRS_2871 RoseRS_3780 RoseRS_3840
            RCA: Rcas_0508 Rcas_0579 Rcas_1101 Rcas_1673 Rcas_2605 Rcas_3956
            DGE: Dgeo_0768 Dgeo_1068 Dgeo_1895
            TTJ: TTHA1078
            TPT: Tpet_0057 Tpet_0327
            TME: Tmel_1175 Tmel_1726
            FNO: Fnod_0890
STRUCTURES  PDB: 2BG1  2UWX  2UWY  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.129
            ExPASy - ENZYME nomenclature database: 2.4.1.129
            ExplorEnz - The Enzyme Database: 2.4.1.129
            ERGO genome analysis and discovery system: 2.4.1.129
            BRENDA, the Enzyme Database: 2.4.1.129
            CAS: 79079-04-2
///
ENTRY       EC 2.4.1.130                Enzyme
NAME        dolichyl-phosphate-mannose---glycolipid alpha-mannosyltransferase;
            dolichol phosphomannose-oligosaccharide-lipid mannosyltransferase;
            oligomannosylsynthase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     dolichyl-phosphate-D-mannose:glycolipid alpha-D-mannosyltransferase
REACTION    Transfers an alpha-D-mannosyl residue from dolichyl-phosphate
            D-mannose into membrane lipid-linked oligosaccharide
COMMENT     Four of the nine mannosyl residues in the main membrane lipid-linked
            oligosaccharide of the structure Glc3Man9GlcNAc2 are produced by the
            action of this enzyme.
REFERENCE   1  [PMID:6163773]
  AUTHORS   Rearick JI, Fujimoto K, Kornfeld S.
  TITLE     Identification of the mannosyl donors involved in the synthesis of
            lipid-linked oligosaccharides.
  JOURNAL   J. Biol. Chem. 256 (1981) 3762-9.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K03845  alpha-1,3-mannosyltransferase
            KO: K03847  alpha-1,6-mannosyltransferase
GENES       HSA: 10195(ALG3) 79087(ALG12)
            PTR: 460886(ALG3)
            MMU: 208624(Alg3) 223774(Alg12)
            RNO: 287983(Alg3) 315212(Alg12_predicted)
            CFA: 478653(ALG3) 481196(ALG12)
            BTA: 614624(MGC142824)
            GGA: 417733(RCJMB04_1n22) 424952(ALG3) 769008(ALG12)
            XTR: 548874(LOC548874)
            DRE: 553725(alg3) 569494(alg12)
            SPU: 576672(LOC576672)
            DME: Dmel_CG4084(l(2)not) Dmel_CG8412
            CEL: K09E4.2 ZC513.5
            ATH: AT2G47760
            OSA: 4327643
            CME: CMK113C
            SCE: YBL082C(ALG3) YNR030W(ALG12)
            AGO: AGOS_AAR043C AGOS_AGL299C
            PIC: PICST_31100(ECM39) PICST_58095(RHK1)
            CAL: CaO19.1092(rhk1)
            CGR: CAGL0A04587g CAGL0M10769g
            SPO: SPAC7D4.06c SPBC1734.12c
            ANI: AN0104.2 AN3588.2
            AFM: AFUA_4G12900 AFUA_5G11990
            AOR: AO090009000318 AO090120000319
            CNE: CNC03430 CNL04800
            DDI: DDB_0231368(alg3) DDB_0231450(alg12)
            TBR: Tb10.70.0260
            TCR: 509317.50 510187.404
            LMA: LmjF36.2040
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.130
            ExPASy - ENZYME nomenclature database: 2.4.1.130
            ExplorEnz - The Enzyme Database: 2.4.1.130
            ERGO genome analysis and discovery system: 2.4.1.130
            BRENDA, the Enzyme Database: 2.4.1.130
            CAS: 77967-76-1
///
ENTRY       EC 2.4.1.131                Enzyme
NAME        glycolipid 2-alpha-mannosyltransferase;
            guanosine diphosphomannose-oligosaccharide-lipid
            mannosyltransferase;
            GDP-mannose-oligosaccharide-lipid mannosyltransferase;
            oligosaccharide-lipid mannosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-mannose:glycolipid 1,2-alpha-D-mannosyltransferase
REACTION    Transfers an alpha-D-mannosyl residue from GDP-mannose into
            lipid-linked oligosaccharide, forming an
            alpha-1,2-D-mannosyl-D-mannose linkage
ALL_REAC    (other) R06127(G) R06128(G)
COMMENT     The two 1,2-linked mannosyl residues in the mammalian lipid-linked
            oligosaccharide of the structure Glc3Man9GlcNAc2 are produced by the
            action of this enzyme.
REFERENCE   1  [PMID:6154707]
  AUTHORS   Schutzbach JS, Springfield JD, Jensen JW.
  TITLE     The biosynthesis of oligosaccharide-lipids. Formation of an
            alpha-1,2-mannosyl-mannose linkage.
  JOURNAL   J. Biol. Chem. 255 (1980) 4170-5.
  ORGANISM  rabbit
ORTHOLOGY   KO: K00732  mannosyltransferase
GENES       SCE: YBR199W(KTR4) YPL053C(KTR6)
            CAL: CaO19.1010(mnt3) CaO19.4494
            SPO: SPCC777.07
            CNE: CNB03210
STRUCTURES  PDB: 1S4N  1S4O  1S4P  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.131
            ExPASy - ENZYME nomenclature database: 2.4.1.131
            ExplorEnz - The Enzyme Database: 2.4.1.131
            ERGO genome analysis and discovery system: 2.4.1.131
            BRENDA, the Enzyme Database: 2.4.1.131
            CAS: 74506-43-7
///
ENTRY       EC 2.4.1.132                Enzyme
NAME        glycolipid 3-alpha-mannosyltransferase;
            mannosyltransferase II;
            guanosine diphosphomannose-oligosaccharide-lipid II
            mannosyltransferase;
            GDP-mannose-oligosaccharide-lipid mannosyltransferase II
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-mannose:glycolipid 1,3-alpha-D-mannosyltransferase
REACTION    Transfers an alpha-D-mannosyl residue from GDP-mannose into
            lipid-linked oligosaccharide, forming an
            alpha-1,3-D-mannosyl-D-mannose linkage [RN:R05002 R05973]
ALL_REAC    R05002 R05973(G)
COMMENT     The 1,3-linked mannosyl residue in the mammalian lipid-linked
            oligosaccharide of the structure Glc3Man9GlcNAc2 is produced by this
            enzyme.
REFERENCE   1  [PMID:7309740]
  AUTHORS   Jensen JW, Schutzbach JS.
  TITLE     The biosynthesis of oligosaccharide-lipids. Partial purification and
            characterization of mannosyltransferase II.
  JOURNAL   J. Biol. Chem. 256 (1981) 12899-904.
  ORGANISM  rabbit
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K03843  alpha-1,3/alpha-1,6-mannosyltransferase
GENES       HSA: 85365(ALG2)
            PTR: 472993(ALG2)
            MMU: 56737(Alg2)
            RNO: 313231(Alg2)
            CFA: 474780(ALG2)
            BTA: 538899(ALG2)
            XLA: 446622(alg2)
            XTR: 595052(alg2)
            SPU: 589943(LOC589943)
            DME: Dmel_CG1291
            CEL: F09E5.2
            ATH: AT1G78800
            OSA: 4336813
            CME: CMT168C
            SCE: YGL065C(ALG2)
            AGO: AGOS_AFL098W
            PIC: PICST_89290(ALG2)
            CGR: CAGL0M05731g
            SPO: SPBC11B10.01
            ANI: AN6874.2
            AFM: AFUA_5G13210
            AOR: AO090120000461
            CNE: CND00660
            UMA: UM02653.1
            DDI: DDB_0231364(alg2)
            CPV: cgd1_230
            CHO: Chro.10033
            TET: TTHERM_00335960
            TBR: Tb927.4.2230
            TCR: 506559.420
            LMA: LmjF34.2420
            EHI: 90.t00023
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.132
            ExPASy - ENZYME nomenclature database: 2.4.1.132
            ExplorEnz - The Enzyme Database: 2.4.1.132
            ERGO genome analysis and discovery system: 2.4.1.132
            BRENDA, the Enzyme Database: 2.4.1.132
            CAS: 81181-76-2
///
ENTRY       EC 2.4.1.133                Enzyme
NAME        xylosylprotein 4-beta-galactosyltransferase;
            UDP-D-galactose:D-xylose galactosyltransferase;
            UDP-D-galactose:xylose galactosyltransferase;
            galactosyltransferase I;
            uridine diphosphogalactose-xylose galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:O-beta-D-xylosylprotein 4-beta-D-galactosyltransferase
REACTION    UDP-galactose + O-beta-D-xylosylprotein = UDP +
            4-beta-D-galactosyl-O-beta-D-xylosylprotein [RN:R05926]
ALL_REAC    R05926(G)
SUBSTRATE   UDP-galactose [CPD:C00052];
            O-beta-D-xylosylprotein [CPD:C03424]
PRODUCT     UDP [CPD:C00015];
            4-beta-D-galactosyl-O-beta-D-xylosylprotein
COFACTOR    Manganese [CPD:C00034]
COMMENT     Involved in the biosynthesis of the linkage region of
            glycosaminoglycan chains as part of proteoglycan biosynthesis
            (chondroitin, dermatan and heparan sulfates). Requires Mn2+.
REFERENCE   1  [PMID:1150655]
  AUTHORS   Schwartz NB, Roden L.
  TITLE     Biosynthesis of chondroitin sulfate. Solubilization of chondroitin
            sulfate glycosyltransferases and partial purification of uridine
            diphosphate-D-galactose:D-xylose galactosyltrans.
  JOURNAL   J. Biol. Chem. 250 (1975) 5200-7.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:10438455]
  AUTHORS   Okajima T, Yoshida K, Kondo T, Furukawa K.
  TITLE     Human homolog of Caenorhabditis elegans sqv-3 gene is
            galactosyltransferase I involved in the biosynthesis of the
            glycosaminoglycan-protein linkage region of proteoglycans.
  JOURNAL   J. Biol. Chem. 274 (1999) 22915-8.
  ORGANISM  human [GN:hsa], Caenorhabditis elegans [GN:cel]
PATHWAY     PATH: map00532  Chondroitin sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00733  xylosylprotein 4-beta-galactosyltransferase
GENES       HSA: 11285(B4GALT7)
            PTR: 664711(B4GALT7)
            MMU: 218271(B4galt7)
            RNO: 364675(B4galt7)
            CFA: 481445(B4GALT7)
            BTA: 507559(B4GALT7)
            GGA: 416359(B4GALT7)
            XLA: 495369(LOC495369)
            DRE: 445022(b4galt7)
            SPU: 588378(LOC588378)
            DME: Dmel_CG11780(beta4GalT7)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.133
            ExPASy - ENZYME nomenclature database: 2.4.1.133
            ExplorEnz - The Enzyme Database: 2.4.1.133
            ERGO genome analysis and discovery system: 2.4.1.133
            BRENDA, the Enzyme Database: 2.4.1.133
            CAS: 52227-72-2
///
ENTRY       EC 2.4.1.134                Enzyme
NAME        galactosylxylosylprotein 3-beta-galactosyltransferase;
            galactosyltransferase II;
            uridine diphosphogalactose-galactosylxylose galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:4-beta-D-galactosyl-O-beta-D-xylosylprotein
            3-beta-D-galactosyltransferase
REACTION    UDP-galactose + 4-beta-D-galactosyl-O-beta-D-xylosylprotein = UDP +
            3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
            [RN:R05927]
ALL_REAC    R05927(G)
SUBSTRATE   UDP-galactose [CPD:C00052];
            4-beta-D-galactosyl-O-beta-D-xylosylprotein
PRODUCT     UDP [CPD:C00015];
            3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
            [CPD:C04825]
COFACTOR    Manganese [CPD:C00034]
COMMENT     Involved in the biosynthesis of the linkage region of
            glycosaminoglycan chains as part of proteoglycan biosynthesis
            (chondroitin, dermatan and heparan sulfates). Requires Mn2+.
REFERENCE   1  [PMID:3924029]
  AUTHORS   Robinson JA, Robinson HC.
  TITLE     Initiation of chondroitin sulphate synthesis by beta-D-galactosides.
            Substrates for galactosyltransferase II.
  JOURNAL   Biochem. J. 227 (1985) 805-14.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:1150655]
  AUTHORS   Schwartz NB, Roden L.
  TITLE     Biosynthesis of chondroitin sulfate. Solubilization of chondroitin
            sulfate glycosyltransferases and partial purification of uridine
            diphosphate-D-galactose:D-xylose galactosyltrans.
  JOURNAL   J. Biol. Chem. 250 (1975) 5200-7.
  ORGANISM  chicken [GN:gga]
REFERENCE   3  [PMID:11551958]
  AUTHORS   Bai X, Zhou D, Brown JR, Crawford BE, Hennet T, Esko JD.
  TITLE     Biosynthesis of the linkage region of glycosaminoglycans: cloning
            and activity of galactosyltransferase II, the sixth member of the
            beta 1,3-galactosyltransferase family (beta 3GalT6).
  JOURNAL   J. Biol. Chem. 276 (2001) 48189-95.
  ORGANISM  human [GN:hsa], mouse [GN:mmu], Drosophila melanogaster [GN:dme],
            Caenorhabditis elegans [GN:cel]
PATHWAY     PATH: map00532  Chondroitin sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00734  galactosylxylosylprotein 3-beta-galactosyltransferase
GENES       HSA: 126792(B3GALT6)
            PTR: 457187(B3GALT6)
            MMU: 117592(B3galt6)
            RNO: 298690(B3galt6_predicted)
            BTA: 522406(LOC522406)
            GGA: 428185(B3GALT6)
            XTR: 548849(LOC548849)
            SPU: 585022(LOC585022) 753784(LOC753784)
            CEL: Y110A2AL.14(sqv-2)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.134
            ExPASy - ENZYME nomenclature database: 2.4.1.134
            ExplorEnz - The Enzyme Database: 2.4.1.134
            ERGO genome analysis and discovery system: 2.4.1.134
            BRENDA, the Enzyme Database: 2.4.1.134
            CAS: 56626-21-2
///
ENTRY       EC 2.4.1.135                Enzyme
NAME        galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase;
            glucuronosyltransferase I;
            uridine diphosphate glucuronic acid:acceptor glucuronosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucuronate:3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xyl
            osyl-protein D-glucuronosyltransferase
REACTION    UDP-glucuronate +
            3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein =
            UDP +
            3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-
            beta-D-xylosylprotein [RN:R04607 R05928]
ALL_REAC    R04607 R05928(G)
SUBSTRATE   UDP-glucuronate [CPD:C00167];
            3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
            [CPD:C04825]
PRODUCT     UDP [CPD:C00015];
            3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-
            beta-D-xylosylprotein [CPD:C04903]
COFACTOR    Manganese [CPD:C00034]
COMMENT     Involved in the biosynthesis of the linkage region of
            glycosaminoglycan chains as part of proteoglycan biosynthesis
            (chondroitin, dermatan and heparan sulfates). Requires Mn2+.
REFERENCE   1  [PMID:5770003]
  AUTHORS   Helting T, Roden L.
  TITLE     Biosynthesis of chondroitin sulfate. II. Glucuronosyl transfer in
            the formation of the carbohydrate-protein linkage region.
  JOURNAL   J. Biol. Chem. 244 (1969) 2799-805.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:4260846]
  AUTHORS   Helting T.
  TITLE     Biosynthesis of heparin. Solubilization and partial purification of
            uridine diphosphate glucuronic acid: acceptor
            glucuronosyltransferase from mouse mastocytoma.
  JOURNAL   J. Biol. Chem. 247 (1972) 4327-32.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:9506957]
  AUTHORS   Kitagawa H, Tone Y, Tamura J, Neumann KW, Ogawa T, Oka S, Kawasaki
            T, Sugahara K.
  TITLE     Molecular cloning and expression of glucuronyltransferase I involved
            in the biosynthesis of the glycosaminoglycan-protein linkage region
            of proteoglycans.
  JOURNAL   J. Biol. Chem. 273 (1998) 6615-8.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00532  Chondroitin sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00735  galactosylgalactosylxylosylprotein
                        3-beta-glucuronosyltransferase 1
            KO: K10157  galactosylgalactosylxylosylprotein
                        3-beta-glucuronosyltransferase 2
            KO: K10158  galactosylgalactosylxylosylprotein
                        3-beta-glucuronosyltransferase 3
GENES       HSA: 135152(B3GAT2) 26229(B3GAT3) 27087(B3GAT1)
            PTR: 462813(B3GAT2) 466859(B3GAT1) 641458(B3GAT3)
            MCC: 695293(LOC695293) 718744(LOC718744)
            MMU: 280645(B3gat2) 72727(B3gat3) 76898(B3gat1)
            RNO: 117108(B3gat1) 64544(B3gat2)
            CFA: 481875(B3GAT2) 483785(B3GAT3) 489265(B3GAT1)
            BTA: 404162(B3GAT3) 541595(b3gat2) 541596(b3gat1)
            MDO: 100010236(LOC100010236) 100016092(LOC100016092)
                 100017866(LOC100017866)
            GGA: 373949(B3GAT1) 408180(LOC408180) 428638(B3GAT2)
            XLA: 494776(LOC494776)
            XTR: 594895(b3gat3) 594896(b3gat1) 594928(b3gat2)
            DRE: 192334(b3gat3) 445060(zgc:91925) 548607(si:dkey-22o20.1)
                 564593(LOC564593) 790914(b3gat3)
            SPU: 579023(LOC579023)
            DME: Dmel_CG32775
            CEL: ZK1307.5(sqv-8)
STRUCTURES  PDB: 1V82  1V83  1V84  2D0J  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.135
            ExPASy - ENZYME nomenclature database: 2.4.1.135
            ExplorEnz - The Enzyme Database: 2.4.1.135
            ERGO genome analysis and discovery system: 2.4.1.135
            BRENDA, the Enzyme Database: 2.4.1.135
            CAS: 9030-08-4
///
ENTRY       EC 2.4.1.136                Enzyme
NAME        gallate 1-beta-glucosyltransferase;
            UDP-glucose---vanillate 1-glucosyltransferase;
            UDPglucose:vanillate 1-O-glucosyltransferase;
            UDPglucose:gallate glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:gallate beta-D-glucosyltransferase
REACTION    UDP-glucose + gallate = UDP + 1-galloyl-beta-D-glucose [RN:R03297]
ALL_REAC    R03297
SUBSTRATE   UDP-glucose [CPD:C00029];
            gallate [CPD:C01424]
PRODUCT     UDP [CPD:C00015];
            1-galloyl-beta-D-glucose
COMMENT     A number of substituted benzoic acids and, more slowly, cinnamic
            acids, can act as acceptors. Vanillin is the best acceptor
            investigated.
REFERENCE   1
  AUTHORS   Gross, G.G.
  TITLE     Synthesis of beta-glucogallin from UDP-glucose and gallic acid by an
            enzyme preparation from oak leaves.
  JOURNAL   FEBS Lett. 148 (1982) 67-70.
  ORGANISM  Quercus robur
REFERENCE   2
  AUTHORS   Gross, G.G.
  TITLE     Partial-purification and properties of UDP-glucose-vanillate
            1-O-glucosyl transferase from oak leaves.
  JOURNAL   Phytochemistry 22 (1983) 2179-2182.
  ORGANISM  Quercus rubra
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.136
            ExPASy - ENZYME nomenclature database: 2.4.1.136
            ExplorEnz - The Enzyme Database: 2.4.1.136
            ERGO genome analysis and discovery system: 2.4.1.136
            BRENDA, the Enzyme Database: 2.4.1.136
            CAS: 89700-30-1
///
ENTRY       EC 2.4.1.137                Enzyme
NAME        sn-glycerol-3-phosphate 2-alpha-galactosyltransferase;
            floridoside-phosphate synthase;
            UDP-galactose:sn-glycerol-3-phosphate-2-D-galactosyl transferase;
            FPS;
            UDP-galactose, sn-3-glycerol phosphate:1->2' galactosyltransferase;
            floridoside phosphate synthetase;
            floridoside phosphate synthase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:sn-glycerol-3-phosphate
            2-alpha-D-galactosyltransferase
REACTION    UDP-galactose + sn-glycerol 3-phosphate = UDP +
            2-(alpha-D-galactosyl)-sn-glycerol 3-phosphate [RN:R00853]
ALL_REAC    R00853
SUBSTRATE   UDP-galactose [CPD:C00052];
            sn-glycerol 3-phosphate [CPD:C00093]
PRODUCT     UDP [CPD:C00015];
            2-(alpha-D-galactosyl)-sn-glycerol 3-phosphate [CPD:C04641]
COMMENT     The product is hydrolysed by a phosphatase to floridoside (cf. EC
            2.4.1.96 sn-glycerol-3-phosphate 1-galactosyltransferase).
REFERENCE   1  [PMID:7083039]
  AUTHORS   Gray NC, Strickland KP.
  TITLE     The purification and characterization of a phospholipase A2 activity
            from the 106,000 X g pellet (microsomal fraction) of bovine brain
            acting on phosphatidylinositol.
  JOURNAL   Can. J. Biochem. 60 (1982) 108-17.
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.137
            ExPASy - ENZYME nomenclature database: 2.4.1.137
            ExplorEnz - The Enzyme Database: 2.4.1.137
            ERGO genome analysis and discovery system: 2.4.1.137
            BRENDA, the Enzyme Database: 2.4.1.137
            CAS: 80747-34-8
///
ENTRY       EC 2.4.1.138                Enzyme
NAME        mannotetraose 2-alpha-N-acetylglucosaminyltransferase;
            alpha-N-acetylglucosaminyltransferase;
            uridine diphosphoacetylglucosamine mannoside
            alpha1->2-alphacetylglucosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:mannotetraose
            alpha-N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine +
            1,3-alpha-D-mannosyl-1,2-alpha-D-mannosyl-1,2-alpha-D-mannosyl-D-
            mannose = UDP +
            1,3-alpha-D-mannosyl-1,2-(N-acetyl-alpha-D-glucosaminyl-alpha-D-
            mannosyl)-1,2-alpha-D-mannosyl-D-mannose [RN:R04619 R06014]
ALL_REAC    R04619 R06014(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            1,3-alpha-D-mannosyl-1,2-alpha-D-mannosyl-1,2-alpha-D-mannosyl-D-
            mannose [CPD:C04861]
PRODUCT     UDP [CPD:C00015];
            1,3-alpha-D-mannosyl-1,2-(N-acetyl-alpha-D-glucosaminyl-alpha-D-
            mannosyl)-1,2-alpha-D-mannosyl-D-mannose
REFERENCE   1  [PMID:6211189]
  AUTHORS   Douglas RH, Ballou CE.
  TITLE     Purification of an alpha-N-acetylglucosaminyltransferase from the
            yeast Kluyveromyces lactis and a study of mutants defective in this
            enzyme activity.
  JOURNAL   Biochemistry. 21 (1982) 1561-70.
  ORGANISM  Kluyveromyces lactis [GN:dkla]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.138
            ExPASy - ENZYME nomenclature database: 2.4.1.138
            ExplorEnz - The Enzyme Database: 2.4.1.138
            ERGO genome analysis and discovery system: 2.4.1.138
            BRENDA, the Enzyme Database: 2.4.1.138
            CAS: 81032-47-5
///
ENTRY       EC 2.4.1.139                Enzyme
NAME        maltose synthase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     alpha-D-glucose-1-phosphate:alpha-D-glucose-1-phosphate
            4-alpha-D-glucosyltransferase (dephosphorylating)
REACTION    2 alpha-D-glucose 1-phosphate + H2O = maltose + 2 phosphate
            [RN:R00957 R06061]
ALL_REAC    R00957 R06061(G)
SUBSTRATE   alpha-D-glucose 1-phosphate [CPD:C00103];
            H2O [CPD:C00001]
PRODUCT     maltose [CPD:C00208];
            phosphate [CPD:C00009]
COMMENT     Neither free phosphate nor maltose 1-phosphate is an intermediate in
            the reaction.
REFERENCE   1
  AUTHORS   Schilling, N.
  TITLE     Characterization of maltose biosynthesis from
            alpha-D-glucose-1-phosphate in Spinacia oleracea L.
  JOURNAL   Planta 154 (1982) 87-93.
  ORGANISM  spinach
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.139
            ExPASy - ENZYME nomenclature database: 2.4.1.139
            ExplorEnz - The Enzyme Database: 2.4.1.139
            ERGO genome analysis and discovery system: 2.4.1.139
            BRENDA, the Enzyme Database: 2.4.1.139
            CAS: 81669-74-1
///
ENTRY       EC 2.4.1.140                Enzyme
NAME        alternansucrase;
            sucrose-1,6(3)-alpha-glucan 6(3)-alpha-glucosyltransferase;
            sucrose:1,6-, 1,3-alpha-D-glucan 3-alpha- and
            6-alpha-D-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     sucrose:1,6(1,3)-alpha-D-glucan 6(3)-alpha-D-glucosyltransferase
REACTION    Transfers alternately an alpha-D-glucosyl residue from sucrose to
            the 6-position and the 3-position of the non-reducing terminal
            residue of an alpha-D-glucan, thus producing a glucan having
            alternating alpha-1,6- and alpha-1,3-linkages
COMMENT     The product, which has quite different properties from other
            dextrans, has been called alternan.
REFERENCE   1  [PMID:7060056]
  AUTHORS   Cote GL, Robyt JF.
  TITLE     Isolation and partial characterization of an extracellular
            glucansucrase from Leuconostoc mesenteroides NRRL B-1355 that
            synthesizes an alternating (1 goes to 6), (1 goes to
            3)-alpha-D-glucan.
  JOURNAL   Carbohydr. Res. 101 (1982) 57-74.
  ORGANISM  Leuconostoc mesenteroides [GN:lme]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.140
            ExPASy - ENZYME nomenclature database: 2.4.1.140
            ExplorEnz - The Enzyme Database: 2.4.1.140
            ERGO genome analysis and discovery system: 2.4.1.140
            BRENDA, the Enzyme Database: 2.4.1.140
            CAS: 100630-46-4
///
ENTRY       EC 2.4.1.141                Enzyme
NAME        N-acetylglucosaminyldiphosphodolichol
            N-acetylglucosaminyltransferase;
            UDP-GlcNAc:dolichyl-pyrophosphoryl-GlcNAc GlcNAc transferase;
            uridine diphosphoacetylglucosamine-dolichylacetylglucosamine
            pyrophosphate acetylglucosaminyltransferase;
            N,N'-diacetylchitobiosylpyrophosphoryldolichol synthase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:N-acetyl-D-glucosaminyl-diphosphodolichol
            N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine +
            N-acetyl-D-glucosaminyl-diphosphodolichol = UDP +
            N,N'-diacetylchitobiosyl-diphosphodolichol [RN:R04494 R05970]
ALL_REAC    R04494 R05970(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            N-acetyl-D-glucosaminyl-diphosphodolichol [CPD:C04500]
PRODUCT     UDP [CPD:C00015];
            N,N'-diacetylchitobiosyl-diphosphodolichol
REFERENCE   1  [PMID:6215245]
  AUTHORS   Sharma CB, Lehle L, Tanner W.
  TITLE     Solubilization and characterization of the initial enzymes of the
            dolichol pathway from yeast.
  JOURNAL   Eur. J. Biochem. 126 (1982) 319-25.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:192724]
  AUTHORS   Turco SJ, Heath EC.
  TITLE     Glucuronosyl-N-acetylglucosaminyl pyrophosphoryldolichol. Formation
            in SV40-transformed human lung fibroblasts and biosynthesis in rat
            lung microsomal preparations.
  JOURNAL   J. Biol. Chem. 252 (1977) 2918-28.
  ORGANISM  human [GN:hsa], rat [GN:rno]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K07432  beta-1,4-N-acetylglucosaminyltransferase
            KO: K07441  beta-1,4-N-acetylglucosaminyltransferase
GENES       HSA: 199857(ALG14) 55849(ALG13)
            MMU: 320302(Glt28d2) 66789(Alg14) 67574(Alg13)
            RNO: 300284(LOC300284) 362031(RGD1312003)
            CFA: 481021(ALG13) 612241(ALG14)
            BTA: 506118(LOC506118) 506537(LOC506537)
            GGA: 422339(ALG13) 424484(ALG14)
            XLA: 431927(MGC84616)
            XTR: 549862(LOC549862)
            DRE: 436733(zgc:92907) 450072(zgc:101623)
            SPU: 575376(LOC575376)
            DME: Dmel_CG14512 Dmel_CG6308
            CEL: M02B7.4 R10D12.12
            ATH: AT4G16710 AT4G18230
            OSA: 4329330 4333143
            CME: CME091C CMS225C
            SCE: YBR070C(ALG14) YGL047W(ALG13)
            AGO: AGOS_AGL042W AGOS_AGL202W
            PIC: PICST_32391 PICST_61591(ALG13)
            CAL: CaO19_13446(CaO19.13446) CaO19_5363(CaO19.5363)
            CGR: CAGL0D06270g CAGL0E04180g
            SPO: SPAC56E4.02c SPAC5D6.06c
            ANI: AN5736.2
            AFM: AFUA_6G06940
            AOR: AO090009000234
            CNE: CNB01840 CNB05490
            DDI: DDB_0231975(ugt1)
            PFA: MAL8P1.133 PFB0515w
            CPV: cgd7_4930
            CHO: Chro.70549
            TPV: TP02_0515
            TBR: Tb927.6.1960
            TCR: 504071.90
            LMA: LmjF30.0530
            EHI: 21.t00050
            AZO: azo1075
            RLE: RL3654 RL3655
            GVI: gll3712
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.141
            ExPASy - ENZYME nomenclature database: 2.4.1.141
            ExplorEnz - The Enzyme Database: 2.4.1.141
            ERGO genome analysis and discovery system: 2.4.1.141
            BRENDA, the Enzyme Database: 2.4.1.141
            CAS: 75536-54-8
///
ENTRY       EC 2.4.1.142                Enzyme
NAME        chitobiosyldiphosphodolichol beta-mannosyltransferase;
            guanosine diphosphomannose-dolichol diphosphochitobiose
            mannosyltransferase;
            GDP-mannose-dolichol diphosphochitobiose mannosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-mannose:chitobiosyldiphosphodolichol beta-D-mannosyltransferase
REACTION    GDP-mannose + chitobiosyldiphosphodolichol = GDP +
            beta-1,4-D-mannosylchitobiosyldiphosphodolichol [RN:R04502 R05972]
ALL_REAC    R04502 R05972(G)
SUBSTRATE   GDP-mannose [CPD:C00096];
            chitobiosyldiphosphodolichol [CPD:C04537]
PRODUCT     GDP [CPD:C00035];
            beta-1,4-D-mannosylchitobiosyldiphosphodolichol [CPD:C05860]
REFERENCE   1  [PMID:6215245]
  AUTHORS   Sharma CB, Lehle L, Tanner W.
  TITLE     Solubilization and characterization of the initial enzymes of the
            dolichol pathway from yeast.
  JOURNAL   Eur. J. Biochem. 126 (1982) 319-25.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:10704531]
  AUTHORS   Takahashi T, Honda R, Nishikawa Y.
  TITLE     Cloning of the human cDNA which can complement the defect of the
            yeast mannosyltransferase I-deficient mutant alg 1.
  JOURNAL   Glycobiology. 10 (2000) 321-7.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K03842  beta-1,4-mannosyltransferase
GENES       HSA: 56052(ALG1)
            PTR: 453895(ALG1)
            MMU: 208211(Alg1)
            RNO: 360475(Alg1_predicted)
            CFA: 490017(ALG1)
            BTA: 507210(LOC507210)
            GGA: 416393(ALG1)
            XTR: 594994(MGC108323)
            DRE: 334161(alg1)
            SPU: 587377(LOC587377)
            DME: Dmel_CG18012
            CEL: T26A5.4(Beta-mannosyltransferase)
            ATH: AT1G16570
            OSA: 4331831
            CME: CMR050C
            SCE: YBR110W(ALG1)
            AGO: AGOS_ADL338C
            PIC: PICST_39314(ALG1)
            CAL: CaO19.4410(alg1)
            SPO: SPAC23C4.14
            ANI: AN5346.2
            AFM: AFUA_6G14180
            AOR: AO090103000403
            CNE: CNA06670
            DDI: DDB_0191150(alg1)
            CPV: cgd7_1810
            CHO: Chro.70211
            TET: TTHERM_00954200
            TBR: Tb10.389.0250
            TCR: 504215.20
            LMA: LmjF18.0900
            EHI: 192.t00014 756.t00001
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.142
            ExPASy - ENZYME nomenclature database: 2.4.1.142
            ExplorEnz - The Enzyme Database: 2.4.1.142
            ERGO genome analysis and discovery system: 2.4.1.142
            BRENDA, the Enzyme Database: 2.4.1.142
            CAS: 83380-85-2
///
ENTRY       EC 2.4.1.143                Enzyme
NAME        alpha-1,6-mannosyl-glycoprotein
            2-beta-N-acetylglucosaminyltransferase;
            N-acetylglucosaminyltransferase II;
            N-glycosyl-oligosaccharide-glycoprotein
            N-acetylglucosaminyltransferase II;
            acetylglucosaminyltransferase II;
            uridine diphosphoacetylglucosamine-mannoside
            alpha1->6-acetylglucosaminyltransferase;
            uridine diphosphoacetylglucosamine-alpha-1,6-mannosylglycoprotein
            beta-1-2-N-acetylglucosaminyltransferase;
            uridine diphosphoacetylglucosamine-alpha-D-mannoside
            beta1-2-acetylglucosaminyltransferase;
            UDP-GlcNAc:mannoside alpha1-6 acetylglucosaminyltransferase;
            alpha-1,6-mannosyl-glycoprotein
            beta-1,2-N-acetylglucosaminyltransferase;
            GnTII
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:6-(alpha-D-mannosyl)-beta-D-mannosyl-glyc
            oprotein 2-beta-N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine + 6-(alpha-D-mannosyl)-beta-D-mannosyl-R
            = UDP +
            6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-
            mannosyl-R [RN:R07258]
ALL_REAC    R07258;
            (other) R04653 R05985(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            6-(alpha-D-mannosyl)-beta-D-mannosyl-R [CPD:C15543]
PRODUCT     UDP [CPD:C00015];
            6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-
            mannosyl-R [CPD:C04944]
COMMENT     R represents the remainder of the N-linked oligosaccharide in the
            glycoprotein acceptor. Note that this enzyme acts after
            N-acetylglucosaminyltransferase I but before
            N-acetylglucosaminyltransferases III, IV, V and VI (click here for
            diagram).
REFERENCE   1  [PMID:2952644]
  AUTHORS   Bendiak B, Schachter H.
  TITLE     Control of glycoprotein synthesis. Purification of
            UDP-N-acetylglucosamine:alpha-D-mannoside beta 1-2
            N-acetylglucosaminyltransferase II from rat liver.
  JOURNAL   J. Biol. Chem. 262 (1987) 5775-83.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6445358]
  AUTHORS   Harpaz N, Schachter H.
  TITLE     Control of glycoprotein synthesis. Bovine colostrum
            UDP-N-acetylglucosamine:alpha-D-mannoside beta
            2-N-acetylglucosaminyltransferase I. Separation from
            UDP-N-acetylglucosamine:alpha-D-mannoside beta
            2-N-acetylglucosaminyltransferase II, partial purification, and
            substrate specificity.
  JOURNAL   J. Biol. Chem. 255 (1980) 4885-93.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:6452163]
  AUTHORS   Mendicino J, Chandrasekaran EV, Anumula KR, Davila M.
  TITLE     Isolation and properties of
            alpha-D-mannose:beta-1,2-N-acetylglucosaminyltransferase from
            trachea mucosa.
  JOURNAL   Biochemistry. 20 (1981) 967-76.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:6457827]
  AUTHORS   Oppenheimer CL, Eckhardt AE, Hill RL.
  TITLE     The nonidentity of porcine N-acetylglucosaminyltransferases I and
            II.
  JOURNAL   J. Biol. Chem. 256 (1981) 11477-82.
  ORGANISM  pig [GN:ssc]
REFERENCE   5  [PMID:6366476]
  AUTHORS   Schachter H, Narasimhan S, Gleeson P, Vella G.
  TITLE     Glycosyltransferases involved in elongation of N-glycosidically
            linked oligosaccharides of the complex or N-acetyllactosamine type.
  JOURNAL   Methods. Enzymol. 98 (1983) 98-134.
REFERENCE   6  [PMID:2952644]
  AUTHORS   Bendiak B, Schachter H.
  TITLE     Control of glycoprotein synthesis. Purification of
            UDP-N-acetylglucosamine:alpha-D-mannoside beta 1-2
            N-acetylglucosaminyltransferase II from rat liver.
  JOURNAL   J. Biol. Chem. 262 (1987) 5775-83.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00736  alpha-1,6-mannosyl-glycoprotein
                        beta-1,2-N-acetylglucosaminyltransferase
GENES       HSA: 4247(MGAT2)
            MMU: 217664(Mgat2)
            RNO: 94273(Mgat2)
            CFA: 480312(MGAT2)
            BTA: 539918(LOC539918)
            XLA: 414590(MGC83215)
            XTR: 448439(mgat2)
            SPU: 593053(LOC593053)
            DME: Dmel_CG7921(Mgat2)
            CEL: C03E10.4(gly-20)
            OSA: 4331021
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.143
            ExPASy - ENZYME nomenclature database: 2.4.1.143
            ExplorEnz - The Enzyme Database: 2.4.1.143
            ERGO genome analysis and discovery system: 2.4.1.143
            BRENDA, the Enzyme Database: 2.4.1.143
            CAS: 105913-04-0
///
ENTRY       EC 2.4.1.144                Enzyme
NAME        beta-1,4-mannosyl-glycoprotein
            4-beta-N-acetylglucosaminyltransferase;
            N-acetylglucosaminyltransferase III;
            N-glycosyl-oligosaccharide-glycoprotein
            N-acetylglucosaminyltransferase III;
            uridine diphosphoacetylglucosamine-glycopeptide
            beta4-acetylglucosaminyltransferase III;
            beta-1,4-mannosyl-glycoprotein
            beta-1,4-N-acetylglucosaminyltransferase;
            GnTIII
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:beta-D-mannosyl-glycoprotein
            4-beta-N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R = UDP +
            4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R [RN:R07259]
ALL_REAC    R07259;
            (other) R05986(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            beta-D-mannosyl-R [CPD:C04942]
PRODUCT     UDP [CPD:C00015];
            4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R [CPD:C15544]
COMMENT     R represents the remainder of the N-linked oligosaccharide in the
            glycoprotein acceptor (click here for diagram). The action of this
            enzyme probably prevents further attachment of N-acetylglucosamine
            residues to the growing carbohydrate chain.
REFERENCE   1  [PMID:6213618]
  AUTHORS   Narasimhan S.
  TITLE     Control of glycoprotein synthesis. UDP-GlcNAc:glycopeptide beta
            4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct
            which adds GlcNAc in beta 1-4 linkage to the beta-linked mannose of
            the trimannosyl core of N-glycosyl oligosaccharides.
  JOURNAL   J. Biol. Chem. 257 (1982) 10235-42.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:6366476]
  AUTHORS   Schachter H, Narasimhan S, Gleeson P, Vella G.
  TITLE     Glycosyltransferases involved in elongation of N-glycosidically
            linked oligosaccharides of the complex or N-acetyllactosamine type.
  JOURNAL   Methods. Enzymol. 98 (1983) 98-134.
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00737  beta-1,4-mannosyl-glycoprotein
                        beta-1,4-N-acetylglucosaminyltransferase
GENES       HSA: 4248(MGAT3)
            PTR: 470218(MGAT3)
            MMU: 17309(Mgat3)
            RNO: 29582(Mgat3)
            CFA: 481244(MGAT3)
            BTA: 520087(LOC520087)
            GGA: 418013(MGAT3)
            DRE: 570828(LOC570828)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.144
            ExPASy - ENZYME nomenclature database: 2.4.1.144
            ExplorEnz - The Enzyme Database: 2.4.1.144
            ERGO genome analysis and discovery system: 2.4.1.144
            BRENDA, the Enzyme Database: 2.4.1.144
            CAS: 83744-93-8
///
ENTRY       EC 2.4.1.145                Enzyme
NAME        alpha-1,3-mannosyl-glycoprotein
            4-beta-N-acetylglucosaminyltransferase;
            N-acetylglucosaminyltransferase IV;
            N-glycosyl-oligosaccharide-glycoprotein
            N-acetylglucosaminyltransferase IV;
            beta-acetylglucosaminyltransferase IV;
            uridine diphosphoacetylglucosamine-glycopeptide
            beta4-acetylglucosaminyltransferase IV;
            alpha-1,3-mannosylglycoprotein
            beta-1,4-N-acetylglucosaminyltransferase;
            GnTIV
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:3-[2-(N-acetyl-beta-D-glucosaminyl)-alpha
            -D-mannosyl]-glycoprotein 4-beta-N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine +
            3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-
            mannosyl-R = UDP +
            3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-
            mannosyl-R [RN:R04662]
ALL_REAC    R04662;
            (other) R05987(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-
            mannosyl-R [CPD:C04880]
PRODUCT     UDP [CPD:C00015];
            3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-
            mannosyl-R [CPD:C04943]
COMMENT     R represents the remainder of the N-linked oligosaccharide in the
            glycoprotein acceptor (click here for diagram). The best acceptor
            for this enzyme is probably the same as that favoured by EC
            2.4.1.144, beta-1,4-mannosyl-glycoprotein
            4-beta-N-acetylglucosaminyltransferase.
REFERENCE   1  [PMID:6222042]
  AUTHORS   Gleeson PA, Schachter H.
  TITLE     Control of glycoprotein synthesis.
  JOURNAL   J. Biol. Chem. 258 (1983) 6162-73.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00738  alpha-1,3-mannosylglycoprotein
                        beta-1,4-N-acetylglucosaminyltransferase
GENES       HSA: 11282(MGAT4B) 11320(MGAT4A)
            PTR: 459434(MGAT4A) 471774(MGAT4B)
            MMU: 103534(Mgat4b) 269181(Mgat4a)
            RNO: 303100(RGD1562836_predicted) 367252(Mgat4a)
            CFA: 474562(MGAT4A) 481458(MGAT4B)
            BTA: 282276(MGAT4A)
            GGA: 416285(MGAT4B) 418692(RCJMB04_3o8)
            XLA: 443870(MGC79124)
            DRE: 431727(zgc:92425) 563038(LOC563038)
            SPU: 579015(LOC579015)
            DME: Dmel_CG9384
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.145
            ExPASy - ENZYME nomenclature database: 2.4.1.145
            ExplorEnz - The Enzyme Database: 2.4.1.145
            ERGO genome analysis and discovery system: 2.4.1.145
            BRENDA, the Enzyme Database: 2.4.1.145
            CAS: 86498-16-0
///
ENTRY       EC 2.4.1.146                Enzyme
NAME        beta-1,3-galactosyl-O-glycosyl-glycoprotein
            beta-1,3-N-acetylglucosaminyltransferase;
            O-glycosyl-oligosaccharide-glycoprotein
            N-acetylglucosaminyltransferase II;
            uridine diphosphoacetylglucosamine-mucin
            beta(1->3)-acetylglucosaminyltransferase (elongating);
            elongation 3beta-GalNAc-transferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein
            (N-acetyl-D-glucosamine to -D-galactose of
            beta-D-galactosyl-1,3-(N-acetyl-D-glucosaminyl-1,6)-N-acetyl-D-galac
            tosaminyl-R) beta-1,3-N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine +
            beta-D-galactosyl-1,3-(N-acetyl-D-glucosaminyl-1,6)-N-acetyl-D-
            galactosaminyl-R = UDP +
            N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,3-(N-acetyl-
            beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R [RN:R04636
            R05901]
ALL_REAC    R04636 R05901(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            beta-D-galactosyl-1,3-(N-acetyl-D-glucosaminyl-1,6)-N-acetyl-D-
            galactosaminyl-R [CPD:C04889]
PRODUCT     UDP [CPD:C00015];
            N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,3-(N-acetyl-
            beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R [CPD:C04930]
COMMENT     cf. EC 2.4.1.102 (beta-1,3-galactosyl-O-glycosyl-glycoprotein
            beta-1,6-N-acetylglucosaminyltransferase), EC 2.4.1.147
            (acetylgalactosaminyl-O-glycosyl-glycoprotein
            beta-1,3-N-acetylglucosaminyltransferase) and EC 2.4.1.148
            (acetylgalactosaminyl-O-glycosyl-glycoprotein
            beta-1,6-N-acetylglucosaminyltransferase).
REFERENCE   1  [PMID:6226356]
  AUTHORS   Brockhausen I, Rachaman ES, Matta KL, Schachter H.
  TITLE     The separation by liquid chromatography (under elevated pressure) of
            phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides.
            Analysis of substrates and products for four
            N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis.
  JOURNAL   Carbohydr. Res. 120 (1983) 3-16.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.146
            ExPASy - ENZYME nomenclature database: 2.4.1.146
            ExplorEnz - The Enzyme Database: 2.4.1.146
            ERGO genome analysis and discovery system: 2.4.1.146
            BRENDA, the Enzyme Database: 2.4.1.146
            CAS: 87927-99-9
///
ENTRY       EC 2.4.1.147                Enzyme
NAME        acetylgalactosaminyl-O-glycosyl-glycoprotein
            beta-1,3-N-acetylglucosaminyltransferase;
            O-glycosyl-oligosaccharide-glycoprotein
            N-acetylglucosaminyltransferase III;
            uridine diphosphoacetylglucosamine-mucin
            beta(1->3)-acetylglucosaminyltransferase;
            mucin core 3 beta3-GlcNAc-transferase;
            Core 3beta-GlcNAc-transferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein
            (N-acetyl-D-glucosamine to N-acetyl-D-galactosaminyl-R)
            beta-1,3-N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-galactosaminyl-R = UDP
            + N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-beta-D-galactosaminyl-R
            [RN:R03513]
ALL_REAC    R03513;
            (other) R05909(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            N-acetyl-beta-D-galactosaminyl-R [CPD:C04135]
PRODUCT     UDP [CPD:C00015];
            N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-beta-D-galactosaminyl-R
            [CPD:C01306]
COMMENT     cf. EC 2.4.1.102 (beta-1,3-galactosyl-O-glycosyl-glycoprotein
            beta-1,6-N-acetylglucosaminyltransferase), EC 2.4.1.146
            (beta-1,3-galactosyl-O-glycosyl-glycoprotein
            beta-1,3-N-acetylglucosaminyltransferase) and EC 2.4.1.148
            (acetylgalactosaminyl-O-glycosyl-glycoprotein
            beta-1,6-N-acetylglucosaminyltransferase).
REFERENCE   1  [PMID:6226356]
  AUTHORS   Brockhausen I, Rachaman ES, Matta KL, Schachter H.
  TITLE     The separation by liquid chromatography (under elevated pressure) of
            phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides.
            Analysis of substrates and products for four
            N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis.
  JOURNAL   Carbohydr. Res. 120 (1983) 3-16.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00512  O-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00739  acetylgalactosaminyl-0-glycosyl-glycoprotein
                        beta-1,3-N-acetylglucosaminyltransferase
GENES       HSA: 192134(B3GNT6)
            PTR: 451437(B3GNT6)
            MMU: 272411(B3gnt6)
            RNO: 292325(RGD1310926_predicted)
            CFA: 485176(B3GNT6)
            BTA: 540848(LOC540848)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.147
            ExPASy - ENZYME nomenclature database: 2.4.1.147
            ExplorEnz - The Enzyme Database: 2.4.1.147
            ERGO genome analysis and discovery system: 2.4.1.147
            BRENDA, the Enzyme Database: 2.4.1.147
            CAS: 87927-96-6
///
ENTRY       EC 2.4.1.148                Enzyme
NAME        acetylgalactosaminyl-O-glycosyl-glycoprotein
            beta-1,6-N-acetylglucosaminyltransferase;
            O-glycosyl-oligosaccharide-glycoprotein
            N-acetylglucosaminyltransferase IV;
            uridine diphosphoacetylglucosamine-mucin
            beta(1->6)-acetylglucosaminyltransferase B;
            core 4 beta6-GalNAc-transferase;
            core 6beta-GalNAc-transferase B
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:O-oligosaccharide-glycoprotein
            (N-acetyl-D-glucosamine to N-acetyl-D-galactosamine of
            N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-D-galactosaminyl-R)
            beta-1,6-N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine +
            N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-D-galactosaminyl-R = UDP +
            N-acetyl-beta-D-glucosaminyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,3)-
            N-acetyl-D-galactosaminyl-R [RN:R03514 R05915]
ALL_REAC    R03514 R05915(G);
            (other) R05910(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-D-galactosaminyl-R
            [CPD:C01306]
PRODUCT     UDP [CPD:C00015];
            N-acetyl-beta-D-glucosaminyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,3)-
            N-acetyl-D-galactosaminyl-R [CPD:C04917]
COMMENT     cf. EC 2.4.1.102 (beta-1,3-galactosyl-O-glycosyl-glycoprotein
            beta-1,6-N-acetylglucosaminyltransferase), EC 2.4.1.146
            (beta-1,3-galactosyl-O-glycosyl-glycoprotein
            beta-1,3-N-acetylglucosaminyltransferase) and EC 2.4.1.147
            (acetylgalactosaminyl-O-glycosyl-glycoprotein
            beta-1,3-N-acetylglucosaminyltransferase).
REFERENCE   1  [PMID:6226356]
  AUTHORS   Brockhausen I, Rachaman ES, Matta KL, Schachter H.
  TITLE     The separation by liquid chromatography (under elevated pressure) of
            phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides.
            Analysis of substrates and products for four
            N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis.
  JOURNAL   Carbohydr. Res. 120 (1983) 3-16.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00512  O-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00740  acetylgalactosaminyl-0-glycosyl-glycoprotein
                        beta-1,6-N-acetylglucosaminyltransferase
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.148
            ExPASy - ENZYME nomenclature database: 2.4.1.148
            ExplorEnz - The Enzyme Database: 2.4.1.148
            ERGO genome analysis and discovery system: 2.4.1.148
            BRENDA, the Enzyme Database: 2.4.1.148
            CAS: 87927-98-8
///
ENTRY       EC 2.4.1.149                Enzyme
NAME        N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase;
            uridine diphosphoacetylglucosamine-acetyllactosaminide
            beta1->3-acetylglucosaminyltransferase;
            poly-N-acetyllactosamine extension enzyme;
            Galbeta1->4GlcNAc-R beta1->3 N-acetylglucosaminyltransferase;
            UDP-GlcNAc:GalR, beta-D-3-N-acetylglucosaminyltransferase;
            N-acetyllactosamine beta(1-3)N-acetylglucosaminyltransferase;
            UDP-GlcNAc:Galbeta1->4GlcNAcbeta-Rbeta1->3-N-
            acetylglucosaminyltransferase;
            GnTE
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:beta-D-galactosyl-1,4-N-acetyl-D-glucosam
            ine beta-1,3-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine +
            beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP +
            N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-
            glucosaminyl-R [RN:R02789]
ALL_REAC    R02789 > R05974(G) R05975(G);
            (other) R04659
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R [CPD:C00694]
PRODUCT     UDP [CPD:C00015];
            N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-
            glucosaminyl-R [CPD:C04890]
COMMENT     Acts on beta-galactosyl-1,4-N-acetylglucosaminyl termini on
            asialo-alpha1-acid glycoprotein and other glycoproteins and
            oligosaccharides.
REFERENCE   1  [PMID:3160874]
  AUTHORS   Takeya A, Hosomi O, Kogure T.
  TITLE     The presence of N-acetyllactosamine and lactose: beta
            (1-3)N-acetylglucosaminyltransferase activity in human urine.
  JOURNAL   Jpn. J. Med. Sci. Biol. 38 (1985) 1-8.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:6219989]
  AUTHORS   van den Eijnden DH, Winterwerp H, Smeeman P, Schiphorst WE.
  TITLE     Novikoff ascites tumor cells contain N-acetyllactosaminide beta 1
            leads to 3 and beta 1 leads to 6 N-acetylglucosaminyltransferase
            activity.
  JOURNAL   J. Biol. Chem. 258 (1983) 3435-7.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00533  Keratan sulfate biosynthesis
            PATH: map00602  Glycosphingolipid biosynthesis - neo-lactoseries
            PATH: map01030  Glycan structures - biosynthesis 1
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K00741  N-acetyllactosaminide
                        beta-1,3-N-acetylglucosaminyltransferase
GENES       HSA: 10678(B3GNT2) 11041(B3GNT1)
            PTR: 451344(B3GNT1)
            MMU: 108902(B3gnt1)
            RNO: 293667(B3gnt6_predicted) 305571(B3gnt1_predicted)
            CFA: 474611(B3GNT2) 476013(B3GNT1)
            BTA: 515585(B3GNT2) 618055(B3GNT1)
            GGA: 421286(B3GNT2)
            XLA: 414647(MGC81185)
            DRE: 403081(zgc:113947) 564450(LOC564450)
            SPU: 577047(LOC577047)
            DME: Dmel_CG3253
            CEL: F22F7.6
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.149
            ExPASy - ENZYME nomenclature database: 2.4.1.149
            ExplorEnz - The Enzyme Database: 2.4.1.149
            ERGO genome analysis and discovery system: 2.4.1.149
            BRENDA, the Enzyme Database: 2.4.1.149
            CAS: 85638-39-7
///
ENTRY       EC 2.4.1.150                Enzyme
NAME        N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase;
            N-acetylglucosaminyltransferase;
            uridine diphosphoacetylglucosamine-acetyllactosaminide
            beta1->6-acetylglucosaminyltransferase;
            Galbeta1->4GlcNAc-R beta1->6 N-acetylglucosaminyltransferase;
            UDP-GlcNAc:Gal-R, beta-D-6-N-acetylglucosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:beta-D-galactosyl-1,4-N-acetyl-D-glucosam
            inide beta-1,6-N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine +
            beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP +
            N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-
            glucosaminyl-R [RN:R02790]
ALL_REAC    R02790;
            (other) R06189(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R [CPD:C00694]
PRODUCT     UDP [CPD:C00015];
            N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-
            glucosaminyl-R [CPD:C04891]
COMMENT     Acts on beta-galactosyl-1,4-N-acetylglucosaminyl termini on
            asialo-alpha1-acid glycoprotein.
REFERENCE   1  [PMID:6219989]
  AUTHORS   van den Eijnden DH, Winterwerp H, Smeeman P, Schiphorst WE.
  TITLE     Novikoff ascites tumor cells contain N-acetyllactosaminide beta 1
            leads to 3 and beta 1 leads to 6 N-acetylglucosaminyltransferase
            activity.
  JOURNAL   J. Biol. Chem. 258 (1983) 3435-7.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00602  Glycosphingolipid biosynthesis - neo-lactoseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K00742  N-acetyllactosaminide
                        beta-1,6-N-acetylglucosaminyltransferase
GENES       HSA: 2651(GCNT2)
            PTR: 462428(GCNT2)
            MMU: 14538(Gcnt2)
            RNO: 306860(Gcnt2)
            CFA: 488215(GCNT2)
            BTA: 520336(LOC520336)
            GGA: 420861(GCNT2)
            XLA: 432275(MGC82474)
            SPU: 579029(LOC579029) 760076(LOC760076)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.150
            ExPASy - ENZYME nomenclature database: 2.4.1.150
            ExplorEnz - The Enzyme Database: 2.4.1.150
            ERGO genome analysis and discovery system: 2.4.1.150
            BRENDA, the Enzyme Database: 2.4.1.150
            CAS: 85638-40-0
///
ENTRY       EC 2.4.1.151      Obsolete  Enzyme
NAME        Transferred to 2.4.1.87
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Transferred entry: now EC 2.4.1.87 N-acetyllactosaminide
            3-alpha-galactosyltransferase (EC 2.4.1.151 created 1984, deleted
            2002)
STRUCTURES  PDB: 1FG5  1G8O  1G93  1GWV  1GWW  1GX0  1GX4  1K4V  1O7O  1O7Q  
                 1VZT  1VZU  1VZX  2JCF  2JCJ  2JCK  2JCL  2JCO  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.151
            ExPASy - ENZYME nomenclature database: 2.4.1.151
            ExplorEnz - The Enzyme Database: 2.4.1.151
            ERGO genome analysis and discovery system: 2.4.1.151
            BRENDA, the Enzyme Database: 2.4.1.151
///
ENTRY       EC 2.4.1.152                Enzyme
NAME        4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase;
            Lewis-negative alpha-3-fucosyltransferase;
            plasma alpha-3-fucosyltransferase;
            guanosine diphosphofucose-glucoside alpha1->3-fucosyltransferase;
            galactoside 3-fucosyltransferase;
            GDP-L-fucose:1,4-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R
            3-L-fucosyltransferase;
            GDP-beta-L-fucose:1,4-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R
            3-L-fucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-beta-L-fucose:1,4-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R
            3-alpha-L-fucosyltransferase
REACTION    GDP-beta-L-fucose + 1,4-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R
            = GDP +
            1,4-beta-D-galactosyl-(alpha-1,3-L-fucosyl)-N-acetyl-D-glucosaminyl-
            R [RN:R03519]
ALL_REAC    R03519 > R05904(G) R06025(G) R06038(G) R06039(G);
            (other) R06075(G) R06076(G) R06095(G)
SUBSTRATE   GDP-beta-L-fucose [CPD:C00325];
            1,4-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R [CPD:C04657]
PRODUCT     GDP [CPD:C00035];
            1,4-beta-D-galactosyl-(alpha-1,3-L-fucosyl)-N-acetyl-D-glucosaminyl-
            R [CPD:C01311]
COMMENT     Normally acts on a glycoconjugate where R (see reaction) is a
            glycoprotein or glycolipid. This enzyme fucosylates on O-3 of an
            N-acetylglucosamine that carries a galactosyl group on O-4, unlike
            EC 2.4.1.65, 3-galactosyl-N-acetylglucosaminide
            4-alpha-L-fucosyltransferase, which fucosylates on O-4 of an
            N-acetylglucosamine that carries a galactosyl group on O-3.
REFERENCE   1  [PMID:7295318]
  AUTHORS   Johnson PH, Yates AD, Watkins WM.
  TITLE     Human salivary fucosyltransferases : evidence for two distinct
            alpha-3-L-fucosyltransferase activities one or which is associated
            with the Lewis blood group Le gene.
  JOURNAL   Biochem. Biophys. Res. Commun. 100 (1981) 1611-8.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:6366476]
  AUTHORS   Schachter H, Narasimhan S, Gleeson P, Vella G.
  TITLE     Glycosyltransferases involved in elongation of N-glycosidically
            linked oligosaccharides of the complex or N-acetyllactosamine type.
  JOURNAL   Methods. Enzymol. 98 (1983) 98-134.
REFERENCE   3  [PMID:12676935]
  AUTHORS   Ma B, Wang G, Palcic MM, Hazes B, Taylor DE.
  TITLE     C-terminal amino acids of Helicobacter pylori alpha1,3/4
            fucosyltransferases determine type I and type II transfer.
  JOURNAL   J. Biol. Chem. 278 (2003) 21893-900.
  ORGANISM  human [GN:hsa], Helicobacter pylori
PATHWAY     PATH: map00602  Glycosphingolipid biosynthesis - neo-lactoseries
            PATH: map00603  Glycosphingolipid biosynthesis - globoseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K03663  4-galactosyl-N-acetylglucosaminide
                        3-alpha-L-fucosyltransferase
GENES       HSA: 10690(FUT9)
            PTR: 449500(FUT9)
            MMU: 14348(Fut9)
            RNO: 84597(Fut9)
            CFA: 449027(FUT9)
            BTA: 282853(FUT9)
            GGA: 771133(FUT9)
            XTR: 548391(fut9)
            DRE: 564968(LOC564968)
            DME: Dmel_CG6869
STRUCTURES  PDB: 2NZW  2NZX  2NZY  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.152
            ExPASy - ENZYME nomenclature database: 2.4.1.152
            ExplorEnz - The Enzyme Database: 2.4.1.152
            ERGO genome analysis and discovery system: 2.4.1.152
            BRENDA, the Enzyme Database: 2.4.1.152
            CAS: 111310-38-4
///
ENTRY       EC 2.4.1.153                Enzyme
NAME        dolichyl-phosphate alpha-N-acetylglucosaminyltransferase;
            uridine diphosphoacetylglucosamine-dolichol phosphate
            acetylglucosaminyltransferase;
            dolichyl phosphate acetylglucosaminyltransferase;
            dolichyl phosphate N-acetylglucosaminyltransferase;
            UDP-N-acetylglucosamine-dolichol phosphate
            N-acetylglucosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:dolichyl-phosphate
            alpha-N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine + dolichyl phosphate = UDP + dolichyl
            N-acetyl-alpha-D-glucosaminyl phosphate [RN:R01008]
ALL_REAC    R01008
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            dolichyl phosphate [CPD:C00110]
PRODUCT     UDP [CPD:C00015];
            dolichyl N-acetyl-alpha-D-glucosaminyl phosphate [CPD:C04678]
REFERENCE   1  [PMID:4717748]
  AUTHORS   Leloir LF, Staneloni RJ, Carminatti H, Behrens NH.
  TITLE     The biosynthesis of a N,N'-diacetylchitobiose containing lipid by
            liver microsomes. A probable dolichol pyrophosphate derivative.
  JOURNAL   Biochem. Biophys. Res. Commun. 52 (1973) 1285-92.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:5113503]
  AUTHORS   Molnar J, Chao H, Ikehara Y.
  TITLE     Phosphoryl-N-acetylglucosamine transfer to a lipid acceptor of liver
            microsomal preparations.
  JOURNAL   Biochim. Biophys. Acta. 239 (1971) 401-10.
  ORGANISM  rabbit
REFERENCE   3  [PMID:4315690]
  AUTHORS   Tetas M, Chao H, Molnar J.
  TITLE     Incorporation of carbohydrates into endogenous acceptors of liver
            microsomal fractions.
  JOURNAL   Arch. Biochem. Biophys. 138 (1970) 135-46.
  ORGANISM  rat [GN:rno], rabbit
REFERENCE   4  [PMID:4371972]
  AUTHORS   Warren CD, Jeanloz RW.
  TITLE     Chemical synthesis of P1-2-acetamido-2-deoxy-alpha-D-glucopyranosyl
            P2-dolichyl pyrophosphate.
  JOURNAL   Carbohydr. Res. 37 (1974) 252-60.
  ORGANISM  pig [GN:ssc]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.153
            ExPASy - ENZYME nomenclature database: 2.4.1.153
            ExplorEnz - The Enzyme Database: 2.4.1.153
            ERGO genome analysis and discovery system: 2.4.1.153
            BRENDA, the Enzyme Database: 2.4.1.153
            CAS: 63363-73-5
///
ENTRY       EC 2.4.1.154      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: globotriosylceramide
            beta-1,6-N-acetylgalactosaminyl-transferase. The enzyme is identical
            to EC 2.4.1.79, globotriaosylceramide
            3-beta-N-acetylgalactosaminyltransferase. The reference cited
            referred to a 1->3 linkage and not to a 1->6 linkage, as indicated
            in the enzyme entry. (EC 2.4.1.154 created 1986, deleted 2006)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.154
            ExPASy - ENZYME nomenclature database: 2.4.1.154
            ExplorEnz - The Enzyme Database: 2.4.1.154
            ERGO genome analysis and discovery system: 2.4.1.154
            BRENDA, the Enzyme Database: 2.4.1.154
///
ENTRY       EC 2.4.1.155                Enzyme
NAME        alpha-1,6-mannosyl-glycoprotein
            6-beta-N-acetylglucosaminyltransferase;
            N-acetylglucosaminyltransferase V;
            alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase;
            uridine diphosphoacetylglucosamine-alpha-mannoside
            beta1->6-acetylglucosaminyltransferase;
            UDP-N-acetylglucosamine:alpha-mannoside-beta1,6
            N-acetylglucosaminyltransferase;
            alpha-1,3(6)-mannosylglycoprotein
            beta-1,6-N-acetylglucosaminyltransferase;
            GnTV
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:6-[2-(N-acetyl-beta-D-glucosaminyl)-alpha
            -D-mannosyl]-glycoprotein 6-beta-N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine +
            6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-
            mannosyl-R = UDP +
            6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-
            mannosyl-R [RN:R04665]
ALL_REAC    R04665;
            (other) R05991(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-
            mannosyl-R [CPD:C04944]
PRODUCT     UDP [CPD:C00015];
            6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-
            mannosyl-R [CPD:C05159]
COMMENT     R represents the remainder of the N-linked oligosaccharide in the
            glycoprotein acceptor (click here for diagram).
REFERENCE   1  [PMID:6216250]
  AUTHORS   Cummings RD, Trowbridge IS, Kornfeld S.
  TITLE     A mouse lymphoma cell line resistant to the leukoagglutinating
            lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc:
            alpha-D-mannoside beta 1,6 N-acetylglucosaminyltransferase.
  JOURNAL   J. Biol. Chem. 257 (1982) 13421-7.
  ORGANISM  Phaseolus vulgaris
REFERENCE   2  [PMID:2834054]
  AUTHORS   Hindsgaul O, Tahir SH, Srivastava OP, Pierce M.
  TITLE     The trisaccharide
            beta-D-GlcpNAc-(1----2)-alpha-D-Manp-(1----6)-beta-D-Manp, as its
            8-methoxycarbonyloctyl glycoside, is an acceptor selective for
            N-acetylglucosaminyltransferase V.
  JOURNAL   Carbohydr. Res. 173 (1988) 263-72.
  ORGANISM  hamster
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00744  alpha-1,3(6)-mannosylglycoprotein
                        beta-1,6-N-acetyl-glucosaminyltransferase
GENES       HSA: 4249(MGAT5)
            PTR: 459625(MGAT5)
            MMU: 107895(Mgat5)
            RNO: 65271(Mgat5)
            CFA: 483895(MGAT5)
            BTA: 537595(LOC537595)
            GGA: 424286(MGAT5)
            DRE: 724006(zgc:136939)
            CEL: C55B7.2(gly-2)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.155
            ExPASy - ENZYME nomenclature database: 2.4.1.155
            ExplorEnz - The Enzyme Database: 2.4.1.155
            ERGO genome analysis and discovery system: 2.4.1.155
            BRENDA, the Enzyme Database: 2.4.1.155
            CAS: 83588-90-3
///
ENTRY       EC 2.4.1.156                Enzyme
NAME        indolylacetyl-myo-inositol galactosyltransferase;
            uridine diphosphogalactose-indolylacetylinositol
            galactosyltransferase;
            indol-3-ylacetyl-myo-inositol galactoside synthase;
            UDP-galactose:indol-3-ylacetyl-myo-inositol
            5-O-D-galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:(indol-3-yl)acetyl-myo-inositol
            5-O-D-galactosyltransferase
REACTION    UDP-galactose + (indol-3-yl)acetyl-myo-inositol = UDP +
            5-O-(indol-3-yl)acetyl-myo-inositol D-galactoside [RN:R04334]
ALL_REAC    R04334
SUBSTRATE   UDP-galactose [CPD:C00052];
            indol-3-ylacetyl-myo-inositol [CPD:C03868]
PRODUCT     UDP [CPD:C00015];
            5-O-(indol-3-yl)acetyl-myo-inositol D-galactoside
REFERENCE   1  [PMID:7159382]
  AUTHORS   Corcuera LJ, Michalczuk L, Bandurski RS.
  TITLE     Enzymic synthesis of indol-3-ylacetyl-myo-inositol galactoside.
  JOURNAL   Biochem. J. 207 (1982) 283-90.
  ORGANISM  Zea mays [GN:ezma]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.156
            ExPASy - ENZYME nomenclature database: 2.4.1.156
            ExplorEnz - The Enzyme Database: 2.4.1.156
            ERGO genome analysis and discovery system: 2.4.1.156
            BRENDA, the Enzyme Database: 2.4.1.156
            CAS: 85537-80-0
///
ENTRY       EC 2.4.1.157                Enzyme
NAME        1,2-diacylglycerol 3-glucosyltransferase;
            UDP-glucose:diacylglycerol glucosyltransferase;
            UDP-glucose:1,2-diacylglycerol glucosyltransferase;
            uridine diphosphoglucose-diacylglycerol glucosyltransferase;
            UDP-glucose-diacylglycerol glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:1,2-diacylglycerol 3-D-glucosyltransferase
REACTION    UDP-glucose + 1,2-diacylglycerol = UDP +
            3-D-glucosyl-1,2-diacylglycerol [RN:R02689]
ALL_REAC    R02689
SUBSTRATE   UDP-glucose [CPD:C00029];
            1,2-diacylglycerol [CPD:C00641]
PRODUCT     UDP [CPD:C00015];
            3-D-glucosyl-1,2-diacylglycerol [CPD:C04046]
COMMENT     Many diacylglycerols with long-chain acyl groups can act as
            acceptors.
REFERENCE   1
  AUTHORS   Sato, N. and Murata, N.
  TITLE     Lipid biosynthesis in the blue-green-alga (cyanobacterium), Anabaena
            variabilis. 3. UDP-glucose-diacylglycerol glucosyltransferase
            activity in vitro.
  JOURNAL   Plant Cell Physiol. 23 (1982) 1115-1120.
  ORGANISM  Anabaena variabilis [GN:ava]
PATHWAY     PATH: map00561  Glycerolipid metabolism
ORTHOLOGY   KO: K03429  1,2-diacylglycerol 3-glucosyltransferase
GENES       BSU: BG11611(ypfP)
            BAN: BA0511
            BAR: GBAA0511
            BAA: BA_1082
            BAT: BAS0483
            BCE: BC0493
            BCA: BCE_0565
            BCZ: BCZK0422(ugtP)
            BTK: BT9727_0426(ugtP)
            BTL: BALH_0448(ugtP)
            BLI: BL01366(ugtP)
            BLD: BLi02330(ugtP)
            BPU: BPUM_1928(ugtP)
            SPZ: M5005_Spy_0426
            SPH: MGAS10270_Spy0427
            SPI: MGAS10750_Spy0439
            SPJ: MGAS2096_Spy0445
            SPK: MGAS9429_Spy0425
            SPF: SpyM51444
            SPA: M6_Spy0453
            SPB: M28_Spy0414
            SSA: SSA_1574
            LSA: LSA0461
            CTC: CTC00289
            DSY: DSY3206
            SYN: sll1377
            SYW: SYNW0060
            SYC: syc0466_c
            SYF: Synpcc7942_1083
            SYD: Syncc9605_0060
            SYE: Syncc9902_0057
            SYG: sync_0061
            CYA: CYA_0245
            CYB: CYB_1788
            TEL: tlr1854
            GVI: glr2559
            ANA: all4933
            AVA: Ava_2217
            PMA: Pro1819
            PMM: PMM1659
            PMT: PMT0058
            PMN: PMN2A_1257
            PMI: PMT9312_1751
            TER: Tery_2749
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.157
            ExPASy - ENZYME nomenclature database: 2.4.1.157
            ExplorEnz - The Enzyme Database: 2.4.1.157
            ERGO genome analysis and discovery system: 2.4.1.157
            BRENDA, the Enzyme Database: 2.4.1.157
            CAS: 83744-96-1
///
ENTRY       EC 2.4.1.158                Enzyme
NAME        13-hydroxydocosanoate 13-beta-glucosyltransferase;
            13-glucosyloxydocosanoate 2'-beta-glucosyltransferase;
            UDP-glucose:13-hydroxydocosanoic acid glucosyltransferase;
            uridine diphosphoglucose-hydroxydocosanoate glucosyltransferase;
            UDP-glucose-13-hydroxydocosanoate glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:13-hydroxydocosanoate 13-beta-D-glucosyltransferase
REACTION    UDP-glucose + 13-hydroxydocosanoate = UDP +
            13-beta-D-glucosyloxydocosanoate [RN:R04127]
ALL_REAC    R04127
SUBSTRATE   UDP-glucose [CPD:C00029];
            13-hydroxydocosanoate [CPD:C03049]
PRODUCT     UDP [CPD:C00015];
            13-beta-D-glucosyloxydocosanoate [CPD:C04103]
COMMENT     13-beta-D-Glucosyloxydocosanoate can also act as acceptor, leading
            to the formation by Candida bogoriensis of the extracellular
            glycolipid, hydroxydocosanoate sophoroside diacetate.
REFERENCE   1  [PMID:6213610]
  AUTHORS   Breithaupt TB, Light RJ.
  TITLE     Affinity chromatography and further characterization of the
            glucosyltransferases involved in hydroxydocosanoic acid sophoroside
            production in Candida bogoriensis.
  JOURNAL   J. Biol. Chem. 257 (1982) 9622-8.
  ORGANISM  Candida bogoriensis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.158
            ExPASy - ENZYME nomenclature database: 2.4.1.158
            ExplorEnz - The Enzyme Database: 2.4.1.158
            ERGO genome analysis and discovery system: 2.4.1.158
            BRENDA, the Enzyme Database: 2.4.1.158
            CAS: 70457-13-5
///
ENTRY       EC 2.4.1.159                Enzyme
NAME        flavonol-3-O-glucoside L-rhamnosyltransferase;
            uridine diphosphorhamnose-flavonol 3-O-glucoside
            rhamnosyltransferase;
            UDP-rhamnose:flavonol 3-O-glucoside rhamnosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-L-rhamnose:flavonol-3-O-D-glucoside 6''-O-L-rhamnosyltransferase
REACTION    UDP-L-rhamnose + a flavonol 3-O-D-glucoside = UDP + a flavonol
            3-O-[beta-L-rhamnosyl-(1->6)-beta-D-glucoside] [RN:R03880]
ALL_REAC    R03880 > R04900
SUBSTRATE   UDP-L-rhamnose [CPD:C02199];
            flavonol 3-O-D-glucoside [CPD:C03946]
PRODUCT     UDP [CPD:C00015];
            flavonol 3-O-[beta-L-rhamnosyl-(1->6)-beta-D-glucoside] [CPD:C04194]
COMMENT     Converts flavonol 3-O-glucosides to 3-O-rutinosides. Also acts, more
            slowly, on rutin, quercetin 3-O-galactoside and flavonol
            3-O-rhamnosides.
REFERENCE   1
  AUTHORS   Kleinehollenhorst, G., Behrens, H., Pegels, G., Srunk, N. and
            Wiermann, R.
  TITLE     Formation of flavonol 3-O-diglycosides and flavonol
            3-O-triglycosides by enzyme extracts from anthers of Tulipa cv
            apeldoorn - characterization and activity of 3 different
            O-glycosyltransferases during anther development.
  JOURNAL   Z. Natursforsch. C: Biosci. 37 (1982) 587-599.
  ORGANISM  Tulipa sp.
REFERENCE   2  [PMID:12900416]
  AUTHORS   Jones P, Messner B, Nakajima J, Schaffner AR, Saito K.
  TITLE     UGT73C6 and UGT78D1, glycosyltransferases involved in flavonol
            glycoside biosynthesis in Arabidopsis thaliana.
  JOURNAL   J. Biol. Chem. 278 (2003) 43910-8.
  ORGANISM  Arabidopsis thaliana [GN:ath]
PATHWAY     PATH: map00941  Flavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.159
            ExPASy - ENZYME nomenclature database: 2.4.1.159
            ExplorEnz - The Enzyme Database: 2.4.1.159
            ERGO genome analysis and discovery system: 2.4.1.159
            BRENDA, the Enzyme Database: 2.4.1.159
            CAS: 83380-89-6
///
ENTRY       EC 2.4.1.160                Enzyme
NAME        pyridoxine 5'-O-beta-D-glucosyltransferase;
            UDP-glucose:pyridoxine 5'-O-beta-glucosyltransferase;
            uridine diphosphoglucose-pyridoxine 5'-beta-glucosyltransferase;
            UDP-glucose-pyridoxine glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:pyridoxine 5'-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + pyridoxine = UDP + 5'-O-beta-D-glucosylpyridoxine
            [RN:R01912]
ALL_REAC    R01912
SUBSTRATE   UDP-glucose [CPD:C00029];
            pyridoxine [CPD:C00314]
PRODUCT     UDP [CPD:C00015];
            5'-O-beta-D-glucosylpyridoxine [CPD:C03996]
COMMENT     4'-Deoxypyridoxine and pyridoxamine can also act as acceptors, but
            more slowly.
REFERENCE   1  [PMID:6217302]
  AUTHORS   Tadera K, Yagi F, Kobayashi A.
  TITLE     Specificity of a particulate glucosyltransferase in seedlings of
            Pisum sativum L. which catalyzes the formation of
            5'-O-(beta-D-glucopyranosyl)pyridoxine.
  JOURNAL   J. Nutr. Sci. Vitaminol. (Tokyo). 28 (1982) 359-66.
  ORGANISM  Pisum sativum
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.160
            ExPASy - ENZYME nomenclature database: 2.4.1.160
            ExplorEnz - The Enzyme Database: 2.4.1.160
            ERGO genome analysis and discovery system: 2.4.1.160
            BRENDA, the Enzyme Database: 2.4.1.160
            CAS: 83744-97-2
///
ENTRY       EC 2.4.1.161                Enzyme
NAME        oligosaccharide 4-alpha-D-glucosyltransferase;
            amylase III;
            1,4-alpha-glucan:1,4-alpha-glucan 4-alpha-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glucosyltransferase
REACTION    Transfers the non-reducing terminal alpha-D-glucose residue from a
            1,4-alpha-D-glucan to the 4-position of an alpha-D-glucan, thus
            bringing about the hydrolysis of oligosaccharides
COMMENT     Acts on amylose, amylopectin, glycogen and maltooligosaccharides,
            but not on maltose. No detectable free glucose is formed.
REFERENCE   1  [PMID:2423097]
  AUTHORS   Nebinger P.
  TITLE     Separation and characterization of four different amylases of
            Entamoeba histolytica. I. Purification and properties.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 367 (1986) 161-7.
  ORGANISM  Entamoeba histolytica [GN:ehi]
REFERENCE   2  [PMID:2423098]
  AUTHORS   Nebinger P.
  TITLE     Separation and characterization of four different amylases of
            Entamoeba histolytica. II. Characterization of amylases.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 367 (1986) 169-76.
  ORGANISM  Entamoeba histolytica [GN:ehi]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.161
            ExPASy - ENZYME nomenclature database: 2.4.1.161
            ExplorEnz - The Enzyme Database: 2.4.1.161
            ERGO genome analysis and discovery system: 2.4.1.161
            BRENDA, the Enzyme Database: 2.4.1.161
            CAS: 9000-92-4
///
ENTRY       EC 2.4.1.162                Enzyme
NAME        aldose beta-D-fructosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     alpha-D-aldosyl-beta-D-fructoside:aldose
            1-beta-D-fructosyltransferase
REACTION    alpha-D-aldosyl1 beta-D-fructoside + D-aldose2 = D-aldose1 +
            alpha-D-aldosyl2 beta-D-fructoside [RN:R04422]
ALL_REAC    R04422
SUBSTRATE   alpha-D-aldosyl1 beta-D-fructoside [CPD:C04219];
            D-aldose2 [CPD:C00737]
PRODUCT     D-aldose1 [CPD:C00737];
            alpha-D-aldosyl2 beta-D-fructoside [CPD:C04219]
REFERENCE   1
  AUTHORS   Cheetham, P.S.J., Hacking, A.J., Vlitos, M.
  TITLE     Synthesis of novel disaccharides by a newly isolated fructosyl
            transferase from Bacillus subtilis.
  JOURNAL   Enzyme Microb. Technol. 11 (1989) 212-219.
  ORGANISM  Bacillus subtilis [GN:bsu]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.162
            ExPASy - ENZYME nomenclature database: 2.4.1.162
            ExplorEnz - The Enzyme Database: 2.4.1.162
            ERGO genome analysis and discovery system: 2.4.1.162
            BRENDA, the Enzyme Database: 2.4.1.162
            CAS: 9031-67-8
///
ENTRY       EC 2.4.1.163                Enzyme
NAME        beta-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide
            beta-1,3-acetylglucosaminyltransferase;
            uridine diphosphoacetylglucosamine-acetyllactosaminide
            beta1->3-acetylglucosaminyltransferase;
            poly-N-acetyllactosamine extension enzyme
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:beta-D-galactosyl-1,4-N-acetyl-beta-D-glu
            cosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide
            beta-1,3-acetylglucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine +
            beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-
            galactosyl-1,4-beta-D-glucosylceramide = UDP +
            N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-
            glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide
            [RN:R04659 R05975]
ALL_REAC    R04659 R05975(G);
            (other) R04654 R06013(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-
            galactosyl-1,4-beta-D-glucosylceramide [CPD:C04922]
PRODUCT     UDP [CPD:C00015];
            N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-
            glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide
            [CPD:C04938]
COFACTOR    Manganese [CPD:C00034]
COMMENT     Requires Mn2+.
REFERENCE   1  [PMID:6238026]
  AUTHORS   Basu M, Basu S.
  TITLE     Biosynthesis in vitro of Ii core glycosphingolipids from
            neolactotetraosylceramide by beta 1-3- and beta
            1-6-N-acetylglucosaminyltransferases from mouse T-lymphoma.
  JOURNAL   J. Biol. Chem. 259 (1984) 12557-62.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map00602  Glycosphingolipid biosynthesis - neo-lactoseries
            PATH: map01031  Glycan structures - biosynthesis 2
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.163
            ExPASy - ENZYME nomenclature database: 2.4.1.163
            ExplorEnz - The Enzyme Database: 2.4.1.163
            ERGO genome analysis and discovery system: 2.4.1.163
            BRENDA, the Enzyme Database: 2.4.1.163
            CAS: 85638-39-7
///
ENTRY       EC 2.4.1.164                Enzyme
NAME        galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide
            beta-1,6-N-acetylglucosaminyltransferase;
            uridine diphosphoacetylglucosamine-acetyllactosaminide
            beta1->6-acetylglucosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:D-galactosyl-1,4-N-acetyl-beta-D-glucosam
            inyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide
            beta-1,6-N-acetylglucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine +
            D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-
            1,4-beta-D-glucosylceramide = UDP +
            N-acetyl-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-
            glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide
            [RN:R04654 R06013]
ALL_REAC    R04654 R06013(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-
            1,4-beta-D-glucosylceramide [CPD:C04922]
PRODUCT     UDP [CPD:C00015];
            N-acetyl-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-
            glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide
            [CPD:C04939]
COFACTOR    Manganese [CPD:C00034]
COMMENT     Requires Mn2+.
REFERENCE   1  [PMID:6238026]
  AUTHORS   Basu M, Basu S.
  TITLE     Biosynthesis in vitro of Ii core glycosphingolipids from
            neolactotetraosylceramide by beta 1-3- and beta
            1-6-N-acetylglucosaminyltransferases from mouse T-lymphoma.
  JOURNAL   J. Biol. Chem. 259 (1984) 12557-62.
  ORGANISM  mouse [GN:mmu]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.164
            ExPASy - ENZYME nomenclature database: 2.4.1.164
            ExplorEnz - The Enzyme Database: 2.4.1.164
            ERGO genome analysis and discovery system: 2.4.1.164
            BRENDA, the Enzyme Database: 2.4.1.164
            CAS: 85638-40-0
///
ENTRY       EC 2.4.1.165                Enzyme
NAME        N-acetylneuraminylgalactosylglucosylceramide
            beta-1,4-N-acetylgalactosaminyltransferase;
            uridine
            diphosphoacetylgalactosamine-acetylneuraminyl(alpha2-
            >3)galactosyl(beta1->4)glucosyl
            beta1->4-acetylgalactosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-galactosamine:N-acetylneuraminyl-2,3-alpha-D-galactos
            yl-1,4-beta-D-glucosylceramide
            beta-1,4-N-acetylgalactosaminyltransferase
REACTION    UDP-N-acetyl-D-galactosamine +
            N-acetylneuraminyl-2,3-alpha-D-galactosyl-1,4-beta-D-
            glucosylceramide = UDP +
            N-acetyl-D-galactosaminyl-1,4-beta-N-acetylneuraminyl-2,3-alpha-D-
            galactosyl-1,4-beta-D-glucosylceramide [RN:R04615 R06011]
ALL_REAC    R04615 R06011(G)
SUBSTRATE   UDP-N-acetyl-D-galactosamine [CPD:C00203];
            N-acetylneuraminyl-2,3-alpha-D-galactosyl-1,4-beta-D-
            glucosylceramide [CPD:C04730]
PRODUCT     UDP [CPD:C00015];
            N-acetyl-D-galactosaminyl-1,4-beta-N-acetylneuraminyl-2,3-alpha-D-
            galactosyl-1,4-beta-D-glucosylceramide [CPD:C04924]
COFACTOR    Manganese [CPD:C00034]
COMMENT     Requires Mn2+. Only substances containing sialic acid residues can
            act as acceptors; bovine fetuin is the best acceptor tested.
REFERENCE   1  [PMID:4632917]
  AUTHORS   Chien JL, Williams T, Basu S.
  TITLE     Biosynthesis of a globoside-type glycosphingolipid by a
            -N-acetylgalactosaminyltransferase from embryonic chicken brain.
  JOURNAL   J. Biol. Chem. 248 (1973) 1778-85.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:2425965]
  AUTHORS   Piller F, Blanchard D, Huet M, Cartron JP.
  TITLE     Identification of a alpha-NeuAc-(2----3)-beta-D-galactopyranosyl
            N-acetyl-beta-D-galactosaminyltransferase in human kidney.
  JOURNAL   Carbohydr. Res. 149 (1986) 171-84.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:3106337]
  AUTHORS   Takeya A, Hosomi O, Kogure T.
  TITLE     Identification and characterization of UDP-GalNAc: NeuAc alpha
            2-3Gal beta 1-4Glc(NAc) beta 1-4(GalNAc to
            Gal)N-acetylgalactosaminyltransferase in human blood plasma.
  JOURNAL   J. Biochem. (Tokyo). 101 (1987) 251-9.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.165
            ExPASy - ENZYME nomenclature database: 2.4.1.165
            ExplorEnz - The Enzyme Database: 2.4.1.165
            ERGO genome analysis and discovery system: 2.4.1.165
            BRENDA, the Enzyme Database: 2.4.1.165
            CAS: 109136-50-7
///
ENTRY       EC 2.4.1.166                Enzyme
NAME        raffinose---raffinose alpha-galactosyltransferase;
            raffinose (raffinose donor) galactosyltransferase;
            raffinose:raffinose alpha-galactosyltransferase;
            raffinose---raffinose alpha-galactotransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     raffinose:raffinose alpha-D-galactosyltransferase
REACTION    2 raffinose = 1F-alpha-D-galactosylraffinose + sucrose [RN:R00039
            R06139]
ALL_REAC    R00039 R06139(G)
SUBSTRATE   raffinose [CPD:C00492]
PRODUCT     1F-alpha-D-galactosylraffinose [CPD:C03971];
            sucrose [CPD:C00089]
COMMENT     The 3F position of raffinose can also act as galactosyl acceptor;
            the enzyme is involved in the accumulation of the tetrasaccharides
            lychnose and isolychnose in the leaves of Cerastium arvense and
            other plants of the family Caryophyllaceae during late autumn.
REFERENCE   1
  AUTHORS   Hopf, H., Gruber, G., Zinn, A. and Kandler, O.
  TITLE     Physiology and biosynthesis of lychnose in Cerastium arvense.
  JOURNAL   Planta 162 (1984) 283-288.
  ORGANISM  Cerastium arvense
ORTHOLOGY   KO: K00745  raffinose-raffinose alpha-galactotransferase
GENES       LLM: llmg_0216(rgpE)
            SPN: SP_1365
            SPR: spr1223(cps23FU)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.166
            ExPASy - ENZYME nomenclature database: 2.4.1.166
            ExplorEnz - The Enzyme Database: 2.4.1.166
            ERGO genome analysis and discovery system: 2.4.1.166
            BRENDA, the Enzyme Database: 2.4.1.166
            CAS: 93389-38-9
///
ENTRY       EC 2.4.1.167                Enzyme
NAME        sucrose 6F-alpha-galactosyltransferase;
            uridine diphosphogalactose-sucrose 6F-alpha-galactosyltransferase;
            UDPgalactose:sucrose 6fru-alpha-galactosyltransferase;
            sucrose 6F-alpha-galactotransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:sucrose 6F-alpha-D-galactosyltransferase
REACTION    UDP-galactose + sucrose = UDP + 6F-alpha-D-galactosylsucrose
            [RN:R00809 R06130]
ALL_REAC    R00809 R06130(G)
SUBSTRATE   UDP-galactose [CPD:C00052];
            sucrose [CPD:C00089]
PRODUCT     UDP [CPD:C00015];
            6F-alpha-D-galactosylsucrose [CPD:C03848]
COMMENT     The enzyme is involved in the synthesis of the trisaccharide
            planteose and higher analogues in the seeds of Plantago and Sesamum
            species.
REFERENCE   1
  AUTHORS   Hopf, H., Spanfelner, M. and Kandler, O.
  TITLE     Planteose synthesis in seeds of Sesamum indicum L.
  JOURNAL   Z. Pflanzenphysiol. 114 (1984) 485-492.
  ORGANISM  Sesamum indicum
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.167
            ExPASy - ENZYME nomenclature database: 2.4.1.167
            ExplorEnz - The Enzyme Database: 2.4.1.167
            ERGO genome analysis and discovery system: 2.4.1.167
            BRENDA, the Enzyme Database: 2.4.1.167
            CAS: 92480-04-1
///
ENTRY       EC 2.4.1.168                Enzyme
NAME        xyloglucan 4-glucosyltransferase;
            uridine diphosphoglucose-xyloglucan 4beta-glucosyltransferase;
            xyloglucan 4beta-D-glucosyltransferase;
            xyloglucan glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:xyloglucan 1,4-beta-D-glucosyltransferase
REACTION    Transfers a beta-D-glucosyl residue from UDP-glucose on to a glucose
            residue in xyloglucan, forming a beta-1,4-D-glucosyl-D-glucose
            linkage
COMMENT     In association with EC 2.4.2.39 (xyloglucan 6-xylosyltransferase),
            this enzyme brings about the synthesis of xyloglucan; concurrent
            transfers of glucose and xylose are essential for this synthesis.
            Not identical with EC 2.4.1.12 cellulose synthase (UDP-forming).
REFERENCE   1  [PMID:6457048]
  AUTHORS   Hayashi T, Matsuda K.
  TITLE     Biosynthesis of xyloglucan in suspension-cultured soybean cells.
            Occurrence and some properties of xyloglucan
            4-beta-D-glucosyltransferase and 6-alpha-D-xylosyltransferase.
  JOURNAL   J. Biol. Chem. 256 (1981) 11117-22.
  ORGANISM  Glycine max [GN:egma]
REFERENCE   2
  AUTHORS   Hayashi, T. and Matsuda, K.
  TITLE     Biosynthesis of xyloglucan in suspension-cultured soybean cells -
            synthesis of xyloglucan from UDP-glucose and UDP-xylose in the
            cell-free system.
  JOURNAL   Plant Cell Physiol. 22 (1981) 517-523.
  ORGANISM  Glycine max [GN:egma]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.168
            ExPASy - ENZYME nomenclature database: 2.4.1.168
            ExplorEnz - The Enzyme Database: 2.4.1.168
            ERGO genome analysis and discovery system: 2.4.1.168
            BRENDA, the Enzyme Database: 2.4.1.168
            CAS: 80237-91-8
///
ENTRY       EC 2.4.1.169      Obsolete  Enzyme
NAME        Transferred to 2.4.2.39
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Transferred entry: now EC 2.4.2.39 xyloglucan 6-xylosyltransferase
            (EC 2.4.1.169 created 1989, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.169
            ExPASy - ENZYME nomenclature database: 2.4.1.169
            ExplorEnz - The Enzyme Database: 2.4.1.169
            ERGO genome analysis and discovery system: 2.4.1.169
            BRENDA, the Enzyme Database: 2.4.1.169
///
ENTRY       EC 2.4.1.170                Enzyme
NAME        isoflavone 7-O-glucosyltransferase;
            uridine diphosphoglucose-isoflavone 7-O-glucosyltransferase;
            UDPglucose-favonoid 7-O-glucosyltransferase;
            UDPglucose:isoflavone 7-O-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:isoflavone 7-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + an isoflavone = UDP + an isoflavone
            7-O-beta-D-glucoside [RN:R07332]
ALL_REAC    R07332 > R02932 R06795 R07718 R07720 R07729 R07740 R07753
SUBSTRATE   UDP-glucose [CPD:C00029];
            isoflavone [CPD:C00799]
PRODUCT     UDP [CPD:C00015];
            isoflavone 7-O-beta-D-glucoside [CPD:C04074]
COMMENT     The 4'-methoxy isoflavones biochanin A and formononetin and, more
            slowly, the 4'-hydroxyisoflavones genistein and daidzein, can act as
            acceptors. The enzyme does not act on isoflavanones, flavones,
            flavanones, flavanols or coumarins.
REFERENCE   1  [PMID:6458246]
  AUTHORS   Koster J, Barz W.
  TITLE     UDP-glucose:isoflavone 7-O-glucosyltransferase from roots of chick
            pea (Cicer arietinum L.).
  JOURNAL   Arch. Biochem. Biophys. 212 (1981) 98-104.
  ORGANISM  Cicer arietinum
PATHWAY     PATH: map00943  Isoflavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.170
            ExPASy - ENZYME nomenclature database: 2.4.1.170
            ExplorEnz - The Enzyme Database: 2.4.1.170
            ERGO genome analysis and discovery system: 2.4.1.170
            BRENDA, the Enzyme Database: 2.4.1.170
            CAS: 97089-62-8
///
ENTRY       EC 2.4.1.171                Enzyme
NAME        methyl-ONN-azoxymethanol beta-D-glucosyltransferase;
            cycasin synthase;
            uridine diphosphoglucose-methylazoxymethanol glucosyltransferase;
            UDP-glucose-methylazoxymethanol glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:methyl-ONN-azoxymethanol beta-D-glucosyltransferase
REACTION    UDP-glucose + methyl-ONN-azoxymethanol = UDP + cycasin [RN:R03547]
ALL_REAC    R03547
SUBSTRATE   UDP-glucose [CPD:C00029];
            methyl-ONN-azoxymethanol
PRODUCT     UDP [CPD:C00015];
            cycasin [CPD:C01418]
COMMENT     Brings about the biosynthesis of the toxic substance cycasin in the
            leaves of Japanese cycad, Cycas revoluta.
REFERENCE   1
  AUTHORS   Tadera, K., Yagi, F., Arima, M. and Kobayashi, A.
  TITLE     Formation of cycasin from methylazoxymethanol by
            UDP-glucosyltransferase from leaves of Japanese cycad.
  JOURNAL   Agric. Biol. Chem. 49 (1985) 2827-2828.
  ORGANISM  Cycas revoluta
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.171
            ExPASy - ENZYME nomenclature database: 2.4.1.171
            ExplorEnz - The Enzyme Database: 2.4.1.171
            ERGO genome analysis and discovery system: 2.4.1.171
            BRENDA, the Enzyme Database: 2.4.1.171
            CAS: 99283-65-5
///
ENTRY       EC 2.4.1.172                Enzyme
NAME        salicyl-alcohol beta-D-glucosyltransferase;
            uridine diphosphoglucose-salicyl alcohol 2-glucosyltransferase;
            UDPglucose:salicyl alcohol phenyl-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:salicyl-alcohol beta-D-glucosyltransferase
REACTION    UDP-glucose + salicyl alcohol = UDP + salicin [RN:R03558]
ALL_REAC    R03558
SUBSTRATE   UDP-glucose [CPD:C00029];
            salicyl alcohol [CPD:C02323]
PRODUCT     UDP [CPD:C00015];
            salicin [CPD:C01451]
REFERENCE   1
  AUTHORS   Mizukami, H., Terao, T. and Ohashi, H.
  TITLE     Partial-purification and characterization of UDP-glucose-salicyl
            alcohol glucosyltransferase from Gardeni jasminoides cell-cultures.
  JOURNAL   Planta Med. 1985 (1985) 104-107.
  ORGANISM  Gardeni jasminoides
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.172
            ExPASy - ENZYME nomenclature database: 2.4.1.172
            ExplorEnz - The Enzyme Database: 2.4.1.172
            ERGO genome analysis and discovery system: 2.4.1.172
            BRENDA, the Enzyme Database: 2.4.1.172
            CAS: 89400-32-8
///
ENTRY       EC 2.4.1.173                Enzyme
NAME        sterol 3beta-glucosyltransferase;
            UDPG:sterol glucosyltransferase;
            UDP-glucose-sterol beta-glucosyltransferase;
            sterol:UDPG glucosyltransferase;
            UDPG-SGTase;
            uridine diphosphoglucose-poriferasterol glucosyltransferase;
            uridine diphosphoglucose-sterol glucosyltransferase;
            sterol glucosyltransferase;
            sterol-beta-D-glucosyltransferase;
            UDP-glucose-sterol glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:sterol 3-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + a sterol = UDP + a sterol 3-beta-D-glucoside
            [RN:R02113]
ALL_REAC    R02113
SUBSTRATE   UDP-glucose [CPD:C00029];
            sterol [CPD:C00370]
PRODUCT     UDP [CPD:C00015];
            sterol 3-beta-D-glucoside [CPD:C03641]
COMMENT     Not identical with EC 2.4.1.192 (nuatigenin
            3beta-glucosyltransferase) or EC 2.4.1.193 (sarsapogenin
            3beta-glucosyltransferase).
REFERENCE   1
  AUTHORS   Duperon, R. and Duperon, P.
  TITLE     Intracellular-localization of UDP-glucose-sterol glucosyl
            transferase and UDP-galactose-sterol galactosyl transferase
            activities in the leaves of tomato (Solanum lycopersicon L,
            Solanaceae).
  JOURNAL   C.R. Acad. Sci. Paris, Ser. 3 304 (1987) 235-238.
  ORGANISM  Solanum lycopersicon
REFERENCE   2
  AUTHORS   Kalinowska, M. and Wojciechowski, Z.A.
  TITLE     Enzymatic-synthesis of nuatigenin 3-beta-D-glucoside in oat (Avena
            sativa) leaves.
  JOURNAL   Phytochemistry 25 (1986) 2525-2529.
  ORGANISM  Avena sativa
REFERENCE   3
  AUTHORS   Kalinowska, M. and Wojciechowski, Z.A.
  TITLE     Subcellular-localization of UDPG-nuatigenin glucosyltransferase in
            oat leaves.
  JOURNAL   Phytochemistry 26 (1987) 353-357.
  ORGANISM  Avena sativa
REFERENCE   4  [PMID:2528379]
  AUTHORS   Murakami-Murofushi K, Ohta J.
  TITLE     Expression of UDP-glucose: poriferasterol glucosyltransferase in the
            process of differentiation of a true slime mold, Physarum
            polycephalum.
  JOURNAL   Biochim. Biophys. Acta. 992 (1989) 412-5.
  ORGANISM  Physarum polycephalum
REFERENCE   5
  AUTHORS   Wojciechowski, Z.A., Zimowski, J. and Tyski, S.
  TITLE     Enzymatic synthesis of steryl 3beta-D-monoglucosides in the slime
            mold Physarum polycephalum.
  JOURNAL   Phytochemistry 16 (1977) 911-914.
  ORGANISM  Physarum polycephalum
ORTHOLOGY   KO: K05841  sterol 3beta-glucosyltransferase
GENES       OSA: 4335001
            SCE: YLR189C(ATG26)
            AGO: AGOS_AFR681W
            PIC: PICST_924(PKH1)
            CAL: CaO19_2616(CaO19.2616)
            ANI: AN4601.2
            AFM: AFUA_2G02220
            AOR: AO090011000498
            CNE: CNC04500
            UMA: UM02058.1 UM02527.1
            DDI: DDB_0191537(ugt52)
            RLE: pRL110335
            CBE: Cbei_2258
            STP: Strop_0168
            RRS: RoseRS_0907
            RCA: Rcas_3770
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.173
            ExPASy - ENZYME nomenclature database: 2.4.1.173
            ExplorEnz - The Enzyme Database: 2.4.1.173
            ERGO genome analysis and discovery system: 2.4.1.173
            BRENDA, the Enzyme Database: 2.4.1.173
            CAS: 123940-38-5
///
ENTRY       EC 2.4.1.174                Enzyme
NAME        glucuronylgalactosylproteoglycan
            4-beta-N-acetylgalactosaminyltransferase;
            N-acetylgalactosaminyltransferase I;
            glucuronylgalactosylproteoglycan
            beta-1,4-N-acetylgalactosaminyltransferase;
            uridine diphosphoacetylgalactosamine-chondroitin
            acetylgalactosaminyltransferase I
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-galactosamine:D-glucuronyl-1,3-beta-D-galactosyl-prot
            eoglycan beta-1,4-N-acetylgalactosaminyltransferase
REACTION    UDP-N-acetyl-D-galactosamine +
            beta-D-glucuronyl-1,3-D-galactosyl-proteoglycan = UDP +
            N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronyl-1,3-beta-D-
            galactosylproteoglycan [RN:R05929]
ALL_REAC    R05929(G)
SUBSTRATE   UDP-N-acetyl-D-galactosamine [CPD:C00203];
            beta-D-glucuronyl-1,3-D-galactosyl-proteoglycan
PRODUCT     UDP [CPD:C00015];
            N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronyl-1,3-beta-D-
            galactosylproteoglycan
COFACTOR    Manganese [CPD:C00034]
COMMENT     Requires Mn2+. Involved in the biosynthesis of chondroitin sulfate.
            Key enzyme activity for the initiation of chondroitin and dermatan
            sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
REFERENCE   1  [PMID:3922754]
  AUTHORS   Rohrmann K, Niemann R, Buddecke E.
  TITLE     Two N-acetylgalactosaminyltransferase are involved in the
            biosynthesis of chondroitin sulfate.
  JOURNAL   Eur. J. Biochem. 148 (1985) 463-9.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:11788602]
  AUTHORS   Uyama T, Kitagawa H, Tamura Ji J, Sugahara K.
  TITLE     Molecular cloning and expression of human chondroitin
            N-acetylgalactosaminyltransferase: the key enzyme for chain
            initiation and elongation of chondroitin/dermatan sulfate on the
            protein linkage region tetrasaccharide shared by heparin/heparan
            sulfate.
  JOURNAL   J. Biol. Chem. 277 (2002) 8841-6.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00532  Chondroitin sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00746  N-acetylgalactosaminyltransferase I
GENES       HSA: 55454(GALNACT-2) 55790(ChGn)
            PTR: 450416(LOC450416) 464030(LOC464030)
            MMU: 234356(4732435N03Rik) 78752(Galnact2)
            RNO: 297554(RGD1563660_predicted) 306375(RGD1307618_predicted)
            CFA: 482831(LOC482831) 486786(LOC486786)
            BTA: 509328(LOC509328) 528057(MGC148954)
            GGA: 422488(LOC422488) 423632(LOC423632)
            SPU: 579124(LOC579124)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.174
            ExPASy - ENZYME nomenclature database: 2.4.1.174
            ExplorEnz - The Enzyme Database: 2.4.1.174
            ERGO genome analysis and discovery system: 2.4.1.174
            BRENDA, the Enzyme Database: 2.4.1.174
            CAS: 96189-39-8
///
ENTRY       EC 2.4.1.175                Enzyme
NAME        glucuronosyl-N-acetylgalactosaminyl-proteoglycan
            4-beta-N-acetylgalactosaminyltransferase;
            N-acetylgalactosaminyltransferase II;
            UDP-N-acetyl-D-galactosamine:D-glucuronyl-N-acetyl-1,3-beta-D-
            galactosaminylproteoglycan
            beta-1,4-N-acetylgalactosaminyltransferase;
            chondroitin synthase;
            glucuronyl-N-acetylgalactosaminylproteoglycan
            beta-1,4-N-acetylgalactosaminyltransferase;
            uridine diphosphoacetylgalactosamine-chondroitin
            acetylgalactosaminyltransferase II
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-galactosamine:beta-D-glucuronosyl-(1->3)-N-acetyl-bet
            a-D-galactosaminyl-proteoglycan
            4-beta-N-acetylgalactosaminyltransferase
REACTION    UDP-N-acetyl-D-galactosamine +
            beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-
            proteoglycan = UDP +
            N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-
            acetyl-beta-D-galactosaminyl-proteoglycan [RN:R04603]
ALL_REAC    R04603 > R05932(G) R05934(G)
SUBSTRATE   UDP-N-acetyl-D-galactosamine [CPD:C00203];
            beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-
            proteoglycan
PRODUCT     UDP [CPD:C00015];
            N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-
            acetyl-beta-D-galactosaminyl-proteoglycan
COMMENT     Involved in the biosynthesis of chondroitin sulfate. The human form
            of this enzyme is a bifunctional glycosyltransferase, which also has
            the 3-beta-glucuronosyltransferase (EC 2.4.1.226,
            N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase)
            activity required for the synthesis of the chondroitin sulfate
            disaccharide repeats. Similar chondroitin synthase 'co-polymerases'
            can be found in Pasteurella multocida and Escherichia coli.
REFERENCE   1  [PMID:3922754]
  AUTHORS   Rohrmann K, Niemann R, Buddecke E.
  TITLE     Two N-acetylgalactosaminyltransferase are involved in the
            biosynthesis of chondroitin sulfate.
  JOURNAL   Eur. J. Biochem. 148 (1985) 463-9.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:11514575]
  AUTHORS   Kitagawa H, Uyama T, Sugahara K.
  TITLE     Molecular cloning and expression of a human chondroitin synthase.
  JOURNAL   J. Biol. Chem. 276 (2001) 38721-6.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:10818104]
  AUTHORS   DeAngelis PL, Padgett-McCue AJ.
  TITLE     Identification and molecular cloning of a chondroitin synthase from
            Pasteurella multocida type F.
  JOURNAL   J. Biol. Chem. 275 (2000) 24124-9.
  ORGANISM  Pasteurella multocida [GN:pmu]
REFERENCE   4  [PMID:11943778]
  AUTHORS   Ninomiya T, Sugiura N, Tawada A, Sugimoto K, Watanabe H, Kimata K.
  TITLE     Molecular cloning and characterization of chondroitin polymerase
            from Escherichia coli strain K4.
  JOURNAL   J. Biol. Chem. 277 (2002) 21567-75.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00532  Chondroitin sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00747  N-Acetylgalactosaminyltransferase II
GENES       HSA: 22856(CHSY1) 337876(CHSY-2) 79586(CHPF)
            PTR: 467777(CHSY1)
            MMU: 269941(Chsy1) 78923(4833446K15Rik)
            RNO: 291577(RGD1560819_predicted) 292999(Chsy1_predicted)
                 316533(D1bwg1363e)
            CFA: 481492(LOC481492) 488538(LOC488538) 488704(CHSY1)
            BTA: 528149(LOC528149) 540002(LOC540002)
            GGA: 415521(CHSY1) 415598(CHSY-2) 769112(LOC769112)
            DRE: 324407(chys1)
            SPU: 579341(LOC579341)
            PMU: PM0775
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.175
            ExPASy - ENZYME nomenclature database: 2.4.1.175
            ExplorEnz - The Enzyme Database: 2.4.1.175
            ERGO genome analysis and discovery system: 2.4.1.175
            BRENDA, the Enzyme Database: 2.4.1.175
            CAS: 96189-40-1
///
ENTRY       EC 2.4.1.176                Enzyme
NAME        gibberellin beta-D-glucosyltransferase;
            uridine diphosphoglucose-gibberellate 7-glucosyltransferase;
            uridine diphosphoglucose-gibberellate 3-O-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:gibberellin 2-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + gibberellin = UDP + gibberellin 2-O-beta-D-glucoside
            [RN:R03680]
ALL_REAC    R03680
SUBSTRATE   UDP-glucose [CPD:C00029];
            gibberellin [CPD:C01699]
PRODUCT     UDP [CPD:C00015];
            gibberellin 2-O-beta-D-glucoside [CPD:C04070]
COMMENT     Acts on the plant hormone gibberellin GA3 and related compounds.
REFERENCE   1
  AUTHORS   Sembdner, G., Knoefel, H.D., Schwarzkopf, E. and Liebisch, H.W.
  TITLE     In vitro glucosylation of gibberellins.
  JOURNAL   Biol. Plant. 27 (1985) 231-236.
  ORGANISM  Phaseolus coccineus, Lycopersicon peruvianum
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.176
            ExPASy - ENZYME nomenclature database: 2.4.1.176
            ExplorEnz - The Enzyme Database: 2.4.1.176
            ERGO genome analysis and discovery system: 2.4.1.176
            BRENDA, the Enzyme Database: 2.4.1.176
            CAS: 99775-14-1
///
ENTRY       EC 2.4.1.177                Enzyme
NAME        cinnamate beta-D-glucosyltransferase;
            uridine diphosphoglucose-cinnamate glucosyltransferase;
            UDPG:t-cinnamate glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:trans-cinnamate beta-D-glucosyltransferase
REACTION    UDP-glucose + trans-cinnamate = UDP + trans-cinnamoyl
            beta-D-glucoside [RN:R02256]
ALL_REAC    R02256
SUBSTRATE   UDP-glucose [CPD:C00029];
            trans-cinnamate [CPD:C00423]
PRODUCT     UDP [CPD:C00015];
            trans-cinnamoyl beta-D-glucoside [CPD:C04164]
COMMENT     4-Coumarate, 2-coumarate, benzoate, feruloate and caffeate can also
            act as acceptors, but more slowly. Involved in the biosynthesis of
            chlorogenic acid in the root of the sweet potato, Ipomoea batatas.
REFERENCE   1  [PMID:6092175]
  AUTHORS   Gamou S, Kim YS, Shimizu N.
  TITLE     Different responses to EGF in two human carcinoma cell lines, A431
            and UCVA-1, possessing high numbers of EGF receptors.
  JOURNAL   Mol. Cell. Endocrinol. 37 (1984) 205-13.
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.177
            ExPASy - ENZYME nomenclature database: 2.4.1.177
            ExplorEnz - The Enzyme Database: 2.4.1.177
            ERGO genome analysis and discovery system: 2.4.1.177
            BRENDA, the Enzyme Database: 2.4.1.177
            CAS: 83744-95-0
///
ENTRY       EC 2.4.1.178                Enzyme
NAME        hydroxymandelonitrile glucosyltransferase;
            cyanohydrin glucosyltransferase;
            uridine diphosphoglucose-cyanohydrin glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:4-hydroxymandelonitrile glucosyltransferase
REACTION    UDP-glucose + 4-hydroxymandelonitrile = UDP + taxiphyllin
            [RN:R02709]
ALL_REAC    R02709
SUBSTRATE   UDP-glucose [CPD:C00029];
            4-hydroxymandelonitrile [CPD:C00650]
PRODUCT     UDP [CPD:C00015];
            taxiphyllin [CPD:C01855]
COMMENT     3,4-Dihydroxymandelonitrile can also act as acceptor.
REFERENCE   1  [PMID:6230992]
  AUTHORS   Hosel W, Schiel O.
  TITLE     Biosynthesis of cyanogenic glucosides: in vitro analysis of the
            glucosylation step.
  JOURNAL   Arch. Biochem. Biophys. 229 (1984) 177-86.
  ORGANISM  Triglochin maritima
REFERENCE   2
  AUTHORS   Poulton, J.E. and Shin, S.-I.
  TITLE     Prunasin biosynthesis by cell-free-extracts from black cherry
            (Prunus serotina Ehrh) fruits and leaves.
  JOURNAL   Z. Naturforsch. C: Biosci. 38 (1983) 369-374.
  ORGANISM  Prunus serotina
PATHWAY     PATH: map00350  Tyrosine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.178
            ExPASy - ENZYME nomenclature database: 2.4.1.178
            ExplorEnz - The Enzyme Database: 2.4.1.178
            ERGO genome analysis and discovery system: 2.4.1.178
            BRENDA, the Enzyme Database: 2.4.1.178
            CAS: 89287-39-8
///
ENTRY       EC 2.4.1.179                Enzyme
NAME        lactosylceramide beta-1,3-galactosyltransferase;
            uridine diphosphogalactose-lactosylceramide
            beta1->3-galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:D-galactosyl-1,4-beta-D-glucosyl-R
            beta-1,3-galactosyltransferase
REACTION    UDP-galactose + D-galactosyl-1,4-beta-D-glucosyl-R = UDP +
            D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosyl-R [RN:R04431]
ALL_REAC    R04431
SUBSTRATE   UDP-galactose [CPD:C00052];
            D-galactosyl-1,4-beta-D-glucosyl-R [CPD:C04247]
PRODUCT     UDP [CPD:C00015];
            D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosyl-R
            [CPD:C04775]
COMMENT     R may be an oligosaccharide or a glycolipid; lactose can also act as
            acceptor, but more slowly. Involved in the elongation of
            oligosaccharide chains, especially in glycolipids.
REFERENCE   1  [PMID:3129295]
  AUTHORS   Bailly P, Piller F, Cartron JP.
  TITLE     Characterization and specific assay for a galactoside
            beta-3-galactosyltransferase of human kidney.
  JOURNAL   Eur. J. Biochem. 173 (1988) 417-22.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.179
            ExPASy - ENZYME nomenclature database: 2.4.1.179
            ExplorEnz - The Enzyme Database: 2.4.1.179
            ERGO genome analysis and discovery system: 2.4.1.179
            BRENDA, the Enzyme Database: 2.4.1.179
            CAS: 106769-64-6
///
ENTRY       EC 2.4.1.180                Enzyme
NAME        lipopolysaccharide N-acetylmannosaminouronosyltransferase;
            ManNAcA transferase;
            uridine
            diphosphoacetylmannosaminuronate-
            acetylglucosaminylpyrophosphorylundecaprenol
            acetylmannosaminuronosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-beta-D-mannosaminouronate:lipopolysaccharide
            N-acetyl-beta-D-mannosaminouronosyltransferase
REACTION    UDP-N-acetyl-beta-D-mannosaminouronate + lipopolysaccharide = UDP +
            N-acetyl-beta-D-mannosaminouronosyl-1,4-lipopolysaccharide
            [RN:R04477]
ALL_REAC    R04477
SUBSTRATE   UDP-N-acetyl-beta-D-mannosaminouronate [CPD:C04427];
            lipopolysaccharide [CPD:C00338]
PRODUCT     UDP [CPD:C00015];
            N-acetyl-beta-D-mannosaminouronosyl-1,4-lipopolysaccharide
            [CPD:C04790]
COMMENT     Involved in the biosynthesis of common antigen in
            Enterobacteriaceae.
REFERENCE   1  [PMID:3275612]
  AUTHORS   Barr K, Ward S, Meier-Dieter U, Mayer H, Rick PD.
  TITLE     Characterization of an Escherichia coli rff mutant defective in
            transfer of N-acetylmannosaminuronic acid (ManNAcA) from UDP-ManNAcA
            to a lipid-linked intermediate involved in enterobacterial common
            antigen synthesis.
  JOURNAL   J. Bacteriol. 170 (1988) 228-33.
  ORGANISM  Escherichia coli [GN:eco], Salmonella typhimurium
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.180
            ExPASy - ENZYME nomenclature database: 2.4.1.180
            ExplorEnz - The Enzyme Database: 2.4.1.180
            ERGO genome analysis and discovery system: 2.4.1.180
            BRENDA, the Enzyme Database: 2.4.1.180
            CAS: 113478-30-1
///
ENTRY       EC 2.4.1.181                Enzyme
NAME        hydroxyanthraquinone glucosyltransferase;
            uridine diphosphoglucose-anthraquinone glucosyltransferase;
            anthraquinone-specific glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:hydroxyanthraquinone O-glucosyltransferase
REACTION    UDP-glucose + an hydroxyanthraquinone = UDP + a
            glucosyloxyanthraquinone [RN:R04108]
ALL_REAC    R04108
SUBSTRATE   UDP-glucose [CPD:C00029];
            hydroxyanthraquinone [CPD:C02980]
PRODUCT     UDP [CPD:C00015];
            glucosyloxyanthraquinone [CPD:C03503]
COMMENT     A range of anthraquinones and some flavones can act as acceptors;
            best substrates are emodin, anthrapurpurin, quinizarin,
            2,6-dihydroanthraquinone and 1,8-dihydroxyanthraquinone.
REFERENCE   1
  AUTHORS   Khouri, H.E. and Ibrahim, R.K.
  TITLE     Purification and some properties of five anthraquinone-specific
            glucosyltransferases from Cinchona succiruba cell suspension
            culture.
  JOURNAL   Phytochemistry 26 (1987) 2531-2535.
  ORGANISM  Cinchona succiruba
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.181
            ExPASy - ENZYME nomenclature database: 2.4.1.181
            ExplorEnz - The Enzyme Database: 2.4.1.181
            ERGO genome analysis and discovery system: 2.4.1.181
            BRENDA, the Enzyme Database: 2.4.1.181
            CAS: 112198-78-4
///
ENTRY       EC 2.4.1.182                Enzyme
NAME        lipid-A-disaccharide synthase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine:2,3-bis-(3-hydroxytet
            radecanoyl)-beta-D-glucosaminyl-1-phosphate
            2,3-bis(3-hydroxytetradecanoyl)-glucosaminyltransferase
REACTION    UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine +
            2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate =
            UDP +
            2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-2,3-bis(3-
            hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate [RN:R04606]
ALL_REAC    R04606
SUBSTRATE   UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine [CPD:C04652];
            2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate
            [CPD:C04824]
PRODUCT     UDP [CPD:C00015];
            2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-2,3-bis(3-
            hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate [CPD:C04932]
COMMENT     Involved with EC 2.3.1.129
            (acyl-[acyl-carrier-protein]---UDP-N-acetylglucosamine
            O-acyltransferase) and EC 2.7.1.130 (tetraacyldisaccharide
            4'-kinase) in the biosynthesis of the phosphorylated glycolipid,
            Lipid A, in the outer membrane of Escherichia coli.
REFERENCE   1  [PMID:2824445]
  AUTHORS   Crowell DN, Reznikoff WS, Raetz CR.
  TITLE     Nucleotide sequence of the Escherichia coli gene for lipid A
            disaccharide synthase.
  JOURNAL   J. Bacteriol. 169 (1987) 5727-34.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:6370995]
  AUTHORS   Ray BL, Painter G, Raetz CR.
  TITLE     The biosynthesis of gram-negative endotoxin. Formation of lipid A
            disaccharides from monosaccharide precursors in extracts of
            Escherichia coli.
  JOURNAL   J. Biol. Chem. 259 (1984) 4852-9.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00540  Lipopolysaccharide biosynthesis
ORTHOLOGY   KO: K00748  lipid-A-disaccharide synthase
GENES       OSA: 4327007
            CME: CMG211C
            TET: TTHERM_00925340
            ECO: b0182(lpxB)
            ECJ: JW0177(lpxB)
            ECE: Z0194(lpxB)
            ECS: ECs0184
            ECC: c0219(lpxB)
            ECI: UTI89_C0197(lpxB)
            ECP: ECP_0190
            ECV: APECO1_1805(lpxB)
            ECW: EcE24377A_0186(lpxB)
            ECX: EcHS_A0184(lpxB)
            STY: STY0252(lpxB)
            STT: t0230(lpxB)
            SPT: SPA0236(lpxB)
            SEC: SC0229(lpxB)
            STM: STM0229(lpxB)
            YPE: YPO1057(lpxB)
            YPK: y3122(lpxB)
            YPM: YP_2793(lpxB)
            YPA: YPA_0533
            YPN: YPN_2943
            YPP: YPDSF_1655
            YPS: YPTB2990(lpxB)
            YPI: YpsIP31758_1026(lpxB)
            SFL: SF0172(lpxB)
            SFX: S0175(lpxB)
            SFV: SFV_0165(lpxB)
            SSN: SSON_0194(lpxB)
            SBO: SBO_0170(lpxB)
            SDY: SDY_0198(lpxB)
            ECA: ECA1044(lpxB)
            PLU: plu0685(lpxB)
            WBR: WGLp380(lpxB)
            SGL: SG1930
            ENT: Ent638_0720
            SPE: Spro_3777
            BFL: Bfl284(lpxB)
            BPN: BPEN_292(lpxB)
            HIN: HI1060(lpxB)
            HIT: NTHI1220(lpxB)
            HIQ: CGSHiGG_08930(lpxB)
            HDU: HD0846(lpxB)
            HSO: HS_1358(lpxB)
            PMU: PM1997(lpxB)
            MSU: MS0422(lpxB)
            APL: APL_0007(lpxB)
            ASU: Asuc_1893
            XFA: XF1042
            XFT: PD0322(lpxB)
            XCC: XCC1360(lpxB)
            XCB: XC_2878
            XCV: XCV1465(lpxB)
            XAC: XAC1408(lpxB)
            XOO: XOO1964(lpxB)
            XOM: XOO_1854(XOO1854)
            VCH: VC2247
            VCO: VC0395_A1838(lpxB)
            VVU: VV1_1873
            VVY: VV2544
            VPA: VP2305
            VFI: VF1949(lpxB)
            PPR: PBPRA2955
            PAE: PA3643(lpxB)
            PAU: PA14_17220(lpxB)
            PAP: PSPA7_1496(lpxB)
            PPU: PP_1604(lpxB)
            PPF: Pput_4173
            PST: PSPTO_1547(lpxB)
            PSB: Psyr_1356(lpxB)
            PSP: PSPPH_3827(lpxB)
            PFL: PFL_1189(lpxB)
            PFO: Pfl_1114(lpxB)
            PEN: PSEEN4207(lpxB)
            PMY: Pmen_3040
            PAR: Psyc_0911(lpxB)
            PCR: Pcryo_1506
            PRW: PsycPRwf_0922
            ACI: ACIAD2324(lpxB)
            SON: SO_1642(lpxB)
            SDN: Sden_1567
            SFR: Sfri_1283
            SAZ: Sama_1152
            SBL: Sbal_1463
            SBM: Shew185_1458
            SLO: Shew_2622
            SPC: Sputcn32_1361
            SSE: Ssed_3148
            SPL: Spea_2872
            SHE: Shewmr4_2628
            SHM: Shewmr7_2695
            SHN: Shewana3_2802
            SHW: Sputw3181_2742
            ILO: IL0832(lpxB)
            CPS: CPS_1568(lpxB)
            PHA: PSHAa2017(lpxB)
            PAT: Patl_1262
            SDE: Sde_2584
            PIN: Ping_2963
            MAQ: Maqu_2535
            CBU: CBU_0620(lpxB)
            CBD: COXBU7E912_0632(lpxB)
            LPN: lpg1371(lpxB) lpg2945(lpxB)
            LPF: lpl1322(lpxB) lpl2872(lpxB)
            LPP: lpp1325(lpxB) lpp3014(lpxB)
            MCA: MCA0400(lpxB)
            FTU: FTT1568c(lpxB)
            FTF: FTF1568c(lpxB)
            FTW: FTW_0358(lpxB)
            FTL: FTL_0540
            FTH: FTH_0542(lpxB)
            FTA: FTA_0573(lpxB)
            FTN: FTN_1477(lpxB)
            TCX: Tcr_1273
            NOC: Noc_1753
            AEH: Mlg_1851
            HHA: Hhal_1455
            HCH: HCH_05238(lpxB)
            CSA: Csal_0576
            ABO: ABO_1156(lpxB)
            MMW: Mmwyl1_1285
            AHA: AHA_1186(lpxB)
            DNO: DNO_0686(lpxB)
            RMA: Rmag_0105
            VOK: COSY_0108(lpxB)
            NME: NMB0199
            NMA: NMA0069(lpxB)
            NMC: NMC0191(lpxB)
            NGO: NGO1782
            CVI: CV_2209(lpxB)
            RSO: RSc1417(lpxB)
            REU: Reut_A1868(lpxB)
            REH: H16_A2042(lpxB)
            RME: Rmet_1448
            BMA: BMA1542(lpxB)
            BMV: BMASAVP1_A2042(lpxB)
            BML: BMA10299_A3269(lpxB)
            BMN: BMA10247_1314(lpxB)
            BXE: Bxe_A1695
            BVI: Bcep1808_1912
            BUR: Bcep18194_A5316(lpxB)
            BCN: Bcen_6071
            BCH: Bcen2424_2006
            BAM: Bamb_2039
            BPS: BPSL2146
            BPM: BURPS1710b_2569(lpxB)
            BPL: BURPS1106A_2479(lpxB)
            BPD: BURPS668_2423(lpxB)
            BTE: BTH_I2040(lpxB)
            PNU: Pnuc_1438
            BPE: BP1432(lpxB)
            BPA: BPP1540(lpxB)
            BBR: BB2618(lpxB)
            RFR: Rfer_2001
            POL: Bpro_2682
            PNA: Pnap_1771
            AAV: Aave_1836
            AJS: Ajs_2572
            VEI: Veis_1451
            MPT: Mpe_A1967
            HAR: HEAR1348(lpxB)
            MMS: mma_2045(lpxB)
            EBA: ebA6002(lpxB)
            AZO: azo1896(lpxB)
            DAR: Daro_1755
            TBD: Tbd_0798
            MFA: Mfla_1517
            HPY: HP0867(lpxB)
            HPJ: jhp0801(lpxB)
            HPA: HPAG1_0850
            HHE: HH0810(lpxB)
            HAC: Hac_1230(lpxB)
            WSU: WS0798(lpxB)
            TDN: Tmden_0903
            CJE: Cj0288c(lpxB)
            CJR: CJE0336(lpxB)
            CJJ: CJJ81176_0314(lpxB)
            CJU: C8J_0264(lpxB)
            CJD: JJD26997_1683(lpxB)
            CFF: CFF8240_0326(lpxB)
            CCV: CCV52592_1652(lpxB)
            CHA: CHAB381_1311(lpxB)
            CCO: CCC13826_0496(lpxB) CCC13826_1576(lpxB)
            ABU: Abu_2217(lpxB)
            NIS: NIS_1314(lpxB)
            SUN: SUN_1114(lpxB)
            GSU: GSU2261(lpxB)
            GME: Gmet_2350(lpxB)
            GUR: Gura_3232
            PCA: Pcar_1258(lpxB)
            PPD: Ppro_3024
            DVU: DVU1361(lpxB)
            DVL: Dvul_1707
            DDE: Dde_2185
            LIP: LI1055(lpxB)
            BBA: Bd1498(lpxB)
            DPS: DP1936(lpxB)
            ADE: Adeh_2625
            AFW: Anae109_2589
            MXA: MXAN_4718(lpxB)
            SAT: SYN_01565
            SFU: Sfum_3751
            RPR: RP321(lpxB)
            RTY: RT0311(lpxB)
            RCO: RC0440(lpxB)
            RFE: RF_0519(lpxB)
            RBE: RBE_0812(lpxB)
            RAK: A1C_02375(lpxB)
            RBO: A1I_05190(lpxB)
            RRI: A1G_02490(lpxB)
            PUB: SAR11_0919(lpxB)
            MLO: mll0630
            MES: Meso_1393
            PLA: Plav_3182
            SME: SMc02089(lpxB)
            SMD: Smed_1143
            ATU: Atu1386(lpxB)
            ATC: AGR_C_2563
            RET: RHE_CH01925(lpxB)
            RLE: RL2233(lpxB)
            BME: BMEI0835
            BMF: BAB1_1171(lpxB)
            BMS: BR1149(lpxB)
            BMB: BruAb1_1155(lpxB)
            BOV: BOV_1107(lpxB)
            OAN: Oant_2041
            BJA: bll4847(lpxB)
            BRA: BRADO4127(lpxB)
            BBT: BBta_4504(lpxB)
            RPA: RPA2909(lpxB)
            RPB: RPB_2815
            RPC: RPC_2449
            RPD: RPD_2844
            RPE: RPE_2566
            NWI: Nwi_1846
            NHA: Nham_1707
            BHE: BH06330(lpxB)
            BQU: BQ06900(lpxB)
            BBK: BARBAKC583_0594(lpxB)
            XAU: Xaut_4426
            CCR: CC_1909
            SIL: SPO1675(lpxB)
            SIT: TM1040_1402
            RSP: RSP_2716(lpxB)
            RSH: Rsph17029_1374
            RSQ: Rsph17025_2141
            JAN: Jann_2448
            RDE: RD1_2598(lpxB)
            PDE: Pden_3909
            MMR: Mmar10_1394
            HNE: HNE_1781(lpxB)
            GOX: GOX0260
            GBE: GbCGDNIH1_1441
            ACR: Acry_0040
            RRU: Rru_A1599
            MAG: amb2484
            MGM: Mmc1_1854
            ABA: Acid345_2535
            SUS: Acid_0771
            FNU: FN0597
            RBA: RB2725(lpxB)
            CTR: CT411(lpxB)
            CTA: CTA_0446(lpxB)
            CMU: TC0692
            CPN: CPn0965(lpxB)
            CPA: CP0895
            CPJ: CPj0965(lpxB)
            CPT: CpB1002
            CCA: CCA00792(lpxB)
            CAB: CAB759
            CFE: CF0221(lpxB)
            PCU: pc1312(lpxB)
            LIL: LA1096(lpxB)
            LIC: LIC12579(lpxB)
            LBJ: LBJ_2279(lpxB)
            LBL: LBL_0828(lpxB)
            SYN: slr0015(lpxB) slr1677
            SYW: SYNW0559(lpxB)
            SYC: syc0178_d syc0610_c(lpxB)
            SYF: Synpcc7942_0932 Synpcc7942_1378
            SYD: Syncc9605_2115(lpxB)
            SYE: Syncc9902_0558(lpxB)
            SYG: sync_2211(lpxB)
            SYR: SynRCC307_1815(lpxB)
            SYX: SynWH7803_1955(lpxB)
            CYA: CYA_1961(lpxB)
            CYB: CYB_2789(lpxB)
            TEL: tll0321 tll1550
            GVI: glr1868 glr2712
            ANA: alr2274(lpxB) alr4005
            AVA: Ava_0098(lpxB) Ava_1699
            PMA: Pro1415(lpxB)
            PMM: PMM1334(lpxB)
            PMT: PMT1409(lpxB)
            PMN: PMN2A_0905(lpxB)
            PMI: PMT9312_1432
            PMB: A9601_15341(lpxB)
            PMC: P9515_14951(lpxB)
            PMF: P9303_05531(lpxB)
            PMG: P9301_15201(lpxB)
            PMH: P9215_15631(lpxB)
            PME: NATL1_17611(lpxB)
            TER: Tery_3228 Tery_3322
            BTH: BT_4004
            BFR: BF0771
            BFS: BF0699
            PGI: PG2162(lpxB)
            CHU: CHU_1391(lpxB)
            GFO: GFO_2966(lpxB)
            FJO: Fjoh_1427
            FPS: FP2330(lpxB)
            CTE: CT0280(lpxB)
            CCH: Cag_0475
            CPH: Cpha266_0411
            PVI: Cvib_1520
            PLT: Plut_1739
            AAE: aq_1427(lpxB)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.182
            ExPASy - ENZYME nomenclature database: 2.4.1.182
            ExplorEnz - The Enzyme Database: 2.4.1.182
            ERGO genome analysis and discovery system: 2.4.1.182
            BRENDA, the Enzyme Database: 2.4.1.182
            CAS: 105843-81-0
///
ENTRY       EC 2.4.1.183                Enzyme
NAME        alpha-1,3-glucan synthase;
            uridine diphosphoglucose-1,3-alpha-glucan glucosyltransferase;
            1,3-alpha-D-glucan synthase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:alpha-D-(1-3)-glucan 3-alpha-D-glucosyltransferase
REACTION    UDP-glucose + [alpha-D-glucosyl-(1-3)]n = UDP +
            [alpha-D-glucosyl-(1-3)]n+1 [RN:R03996 R06045]
ALL_REAC    R03996 R06045(G)
SUBSTRATE   UDP-glucose [CPD:C00029];
            [alpha-D-glucosyl-(1-3)]n
PRODUCT     UDP [CPD:C00015];
            [alpha-D-glucosyl-(1-3)]n+1
COMMENT     A glucan primer is needed to begin the reaction, which brings about
            elongation of the glucan chains.
REFERENCE   1
  AUTHORS   Andoh, M., Yamashita, Y., Shigeoka, T., Hanada, N. and Takehara, T.
  TITLE     [Extension of the length of glucan chain by
            1,3-alpha-D-glucansynthase from Streptococcus mutans serotype.].
  JOURNAL   Koku Eisei Gakkai Zasshi 37 (1987) 516-517.
ORTHOLOGY   KO: K00749  alpha-1,3-glucan synthase
GENES       SPO: SPAC1527.01(mok11) SPBC32H8.13c(mok12) SPCC1281.01k(ags1)
                 SPCC63.04
            AFM: AFUA_1G15440 AFUA_2G11270 AFUA_3G00910
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.183
            ExPASy - ENZYME nomenclature database: 2.4.1.183
            ExplorEnz - The Enzyme Database: 2.4.1.183
            ERGO genome analysis and discovery system: 2.4.1.183
            BRENDA, the Enzyme Database: 2.4.1.183
            CAS: 113478-38-9
///
ENTRY       EC 2.4.1.184                Enzyme
NAME        galactolipid galactosyltransferase;
            galactolipid-galactolipid galactosyltransferase;
            galactolipid:galactolipid galactosyltransferase;
            interlipid galactosyltransferase;
            GGGT;
            DGDG synthase (ambiguous);
            digalactosyldiacylglycerol synthase (ambiguous)
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     3-(beta-D-galactosyl)-1,2-diacyl-sn-glycerol:mono-3-(beta-D-galactos
            yl)-1,2-diacyl-sn-glycerol beta-D-galactosyltransferase
REACTION    2 3-(beta-D-galactosyl)-1,2-diacyl-sn-glycerol =
            3-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-1,2-diacyl-sn-
            glycerol + 1,2-diacyl-sn-glycerol [RN:R04472]
ALL_REAC    R04472
SUBSTRATE   3-(beta-D-galactosyl)-1,2-diacyl-sn-glycerol
PRODUCT     3-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-1,2-diacyl-sn-
            glycerol;
            1,2-diacyl-sn-glycerol [CPD:C00641]
COMMENT     By further transfers of galactosyl residues to the
            digalactosyldiacylglycerol, trigalactosyldiacylglycerol and
            tetragalactosyldiacylglycerol are also formed. This enzyme was
            originally thought to be the major enzyme involved in the production
            of digalactosyldiacylglycerol in plants as it masked the effect of
            the true enzyme (EC 2.4.1.241, digalactosyldiacylglycerol synthase)
            [4,5]. Its activity is localized to chloroplast envelope membranes,
            but it does not contribute to net galactolipid synthesis in plants
            [4].
REFERENCE   1
  AUTHORS   Dorne, A.-J., Block, M.A., Joyard, J. and Douce, R.
  TITLE     The galactolipid-galactolipid galactosyltransferase is located on
            the outer surface of the outer-membrane of the chloroplast envelope.
  JOURNAL   FEBS Lett. 145 (1982) 30-34.
  ORGANISM  spinach
REFERENCE   2
  AUTHORS   Heemskerk, J.W.M., Wintermans, J.F.G.M., Joyard, J., Block, M.A.,
            Dorne, A.-J. and Douce, R.
  TITLE     Localization of galactolipid:galactolipid galactosyltransferase and
            acyltransferase in outer envelope membrane of spinach chloroplasts.
  JOURNAL   Biochim. Biophys. Acta 877 (1986) 281-289.
  ORGANISM  spinach
REFERENCE   3
  AUTHORS   Heemskerk, J.W.M., Jacobs, F.H.H. and Wintermans, J.F.G.M.
  TITLE     UDPgalactose-independent synthesis of monogalactosyldiacylglycerol.
            An enzymatic activity of the spinach chloroplast envelope.
  JOURNAL   Biochim. Biophys. Acta 961 (1988) 38-47.
  ORGANISM  spinach
REFERENCE   4  [PMID:14600212]
  AUTHORS   Kelly AA, Froehlich JE, Dormann P.
  TITLE     Disruption of the two digalactosyldiacylglycerol synthase genes DGD1
            and DGD2 in Arabidopsis reveals the existence of an additional
            enzyme of galactolipid synthesis.
  JOURNAL   Plant. Cell. 15 (2003) 2694-706.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   5  [PMID:15590685]
  AUTHORS   Benning C, Ohta H.
  TITLE     Three enzyme systems for galactoglycerolipid biosynthesis are
            coordinately regulated in plants.
  JOURNAL   J. Biol. Chem. 280 (2005) 2397-400.
  ORGANISM  Arabidopsis sp.
PATHWAY     PATH: map00561  Glycerolipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.184
            ExPASy - ENZYME nomenclature database: 2.4.1.184
            ExplorEnz - The Enzyme Database: 2.4.1.184
            ERGO genome analysis and discovery system: 2.4.1.184
            BRENDA, the Enzyme Database: 2.4.1.184
            CAS: 66676-74-2
///
ENTRY       EC 2.4.1.185                Enzyme
NAME        flavanone 7-O-beta-glucosyltransferase;
            uridine diphosphoglucose-flavanone 7-O-glucosyltransferase;
            naringenin 7-O-glucosyltransferase;
            hesperetin 7-O-glucosyl-transferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:flavanone 7-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + a flavanone = UDP + a flavanone 7-O-beta-D-glucoside
            [RN:R07333]
ALL_REAC    R07333 > R02897
SUBSTRATE   UDP-glucose [CPD:C00029];
            flavanone [CPD:C00766]
PRODUCT     UDP [CPD:C00015];
            flavanone 7-O-beta-D-glucoside [CPD:C04007]
COMMENT     Naringenin and hesperetin can act as acceptors. No action on
            flavones or flavonols.
REFERENCE   1  [PMID:2171434]
  AUTHORS   McIntosh CA, Latchinian L, Mansell RL.
  TITLE     Flavanone-specific 7-O-glucosyltransferase activity in Citrus
            paradisi seedlings: purification and characterization.
  JOURNAL   Arch. Biochem. Biophys. 282 (1990) 50-7.
  ORGANISM  Citrus paradisi
REFERENCE   2
  AUTHORS   McIntosh, C.A. and Mansell, R.L.
  TITLE     Biosynthesis of naringin in Citrus paradisi -
            UDP-glucosyl-transferase activity in grapefruit seedlings.
  JOURNAL   Phytochemistry 29 (1990) 1533-1538.
  ORGANISM  Citrus paradisi
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.185
            ExPASy - ENZYME nomenclature database: 2.4.1.185
            ExplorEnz - The Enzyme Database: 2.4.1.185
            ERGO genome analysis and discovery system: 2.4.1.185
            BRENDA, the Enzyme Database: 2.4.1.185
            CAS: 125752-73-0
///
ENTRY       EC 2.4.1.186                Enzyme
NAME        glycogenin glucosyltransferase;
            glycogenin;
            priming glucosyltransferase;
            UDP-glucose:glycogenin glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-alpha-D-glucose:glycogenin alpha-D-glucosyltransferase
REACTION    UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin
            [RN:R03681]
ALL_REAC    R03681
SUBSTRATE   UDP-alpha-D-glucose [CPD:C00029];
            glycogenin [CPD:C01702]
PRODUCT     UDP [CPD:C00015];
            alpha-D-glucosylglycogenin [CPD:C02687]
COMMENT     The first reaction of this enzyme is to catalyse its own
            glucosylation, normally at Tyr-194 of the protein if this group is
            free. When Tyr-194 is replaced by Thr or Phe, the enzyme's
            Mn2+-dependent self-glucosylation activity is lost but its
            intermolecular transglucosylation ability remains [7]. It continues
            to glucosylate an existing glucosyl group until a length of about
            5---13 residues has been formed. Further lengthening of the glycogen
            chain is then carried out by EC 2.4.1.11, glycogen (starch)
            synthase. The enzyme is not highly specific for the donor, using
            UDP-xylose in addition to UDP-glucose (although not glucosylating or
            xylosylating a xylosyl group so added). It can also use CDP-glucose
            and TDP-glucose, but not ADP-glucose or GDP-glucose. Similarly it is
            not highly specific for the acceptor, using water (i.e. hydrolysing
            UDP-glucose) among others. Various forms of the enzyme exist, and
            different forms predominate in different organs. Thus primate liver
            contains glycogenin-2, of molecular mass 66 kDa, whereas the more
            widespread form is glycogenin-1, with a molecular mass of 38 kDa.
REFERENCE   1  [PMID:809265]
  AUTHORS   Krisman CR, Barengo R.
  TITLE     A precursor of glycogen biosynthesis: alpha-1,4-glucan-protein.
  JOURNAL   Eur. J. Biochem. 52 (1975) 117-23.
REFERENCE   2  [PMID:3121316]
  AUTHORS   Pitcher J, Smythe C, Campbell DG, Cohen P.
  TITLE     Identification of the 38-kDa subunit of rabbit skeletal muscle
            glycogen synthase as glycogenin.
  JOURNAL   Eur. J. Biochem. 169 (1987) 497-502.
  ORGANISM  rabbit
REFERENCE   3  [PMID:2970965]
  AUTHORS   Pitcher J, Smythe C, Cohen P.
  TITLE     Glycogenin is the priming glucosyltransferase required for the
            initiation of glycogen biogenesis in rabbit skeletal muscle.
  JOURNAL   Eur. J. Biochem. 176 (1988) 391-5.
  ORGANISM  rabbit
REFERENCE   4
  AUTHORS   Kennedy, L.D., Kirkman, B.R., Lomako, J., Rodriguez, I.R. and
            Whelan, W.J.
  TITLE     The biogenesis of rabbit-muscle glycogen.
  JOURNAL   In: Berman, M.C. and Opie, L.A. (Eds.), Membranes and Muscle, ICSU
            Press/IRL Press, Oxford, 1985, p. 65-84.
REFERENCE   5  [PMID:4062948]
  AUTHORS   Rodriguez IR, Whelan WJ.
  TITLE     A novel glycosyl-amino acid linkage: rabbit-muscle glycogen is
            covalently linked to a protein via tyrosine.
  JOURNAL   Biochem. Biophys. Res. Commun. 132 (1985) 829-36.
REFERENCE   6  [PMID:2973423]
  AUTHORS   Lomako J, Lomako WM, Whelan WJ.
  TITLE     A self-glucosylating protein is the primer for rabbit muscle
            glycogen biosynthesis.
  JOURNAL   FASEB. J. 2 (1988) 3097-103.
REFERENCE   7  [PMID:7797519]
  AUTHORS   Alonso MD, Lomako J, Lomako WM, Whelan WJ.
  TITLE     Catalytic activities of glycogenin additional to autocatalytic
            self-glucosylation.
  JOURNAL   J. Biol. Chem. 270 (1995) 15315-9.
REFERENCE   8  [PMID:7672505]
  AUTHORS   Alonso MD, Lomako J, Lomako WM, Whelan WJ.
  TITLE     A new look at the biogenesis of glycogen.
  JOURNAL   FASEB. J. 9 (1995) 1126-37.
REFERENCE   9  [PMID:9857012]
  AUTHORS   Mu J, Roach PJ.
  TITLE     Characterization of human glycogenin-2, a self-glucosylating
            initiator of liver glycogen metabolism.
  JOURNAL   J. Biol. Chem. 273 (1998) 34850-6.
REFERENCE   10 [PMID:12051921]
  AUTHORS   Gibbons BJ, Roach PJ, Hurley TD.
  TITLE     Crystal structure of the autocatalytic initiator of glycogen
            biosynthesis, glycogenin.
  JOURNAL   J. Mol. Biol. 319 (2002) 463-77.
ORTHOLOGY   KO: K00750  glycogenin glucosyltransferase
GENES       HSA: 2992(GYG1) 8908(GYG2)
            PTR: 460765(GYG1) 465469(GYG2)
            MMU: 27357(Gyg)
            RNO: 81675(Gyg1)
            CFA: 491717(GYG2) 611614(GYG1)
            BTA: 280812(GYG) 505258(LOC505258)
            GGA: 418660(GYG2) 425050(GYG1)
            XLA: 446485(gyg1)
            XTR: 394883(gyg1) 496877(LOC496877)
            DRE: 415152(gygl)
            SPU: 765322(LOC765322)
            DME: Dmel_CG9480(Glycogenin)
            CEL: T25E12.5(glycogenin)
            ATH: AT3G02230(RGP1) AT3G08900(RGP3) AT5G15650(RGP2)
                 AT5G50750(RGP4)
            PIC: PICST_76484(GLG2) PICST_86206(GLG1)
            RLE: RL3976(sqdD)
STRUCTURES  PDB: 1LL0  1LL2  1LL3  1ZCT  1ZCU  1ZCV  1ZCY  1ZDF  1ZDG  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.186
            ExPASy - ENZYME nomenclature database: 2.4.1.186
            ExplorEnz - The Enzyme Database: 2.4.1.186
            ERGO genome analysis and discovery system: 2.4.1.186
            BRENDA, the Enzyme Database: 2.4.1.186
            CAS: 117590-73-5
///
ENTRY       EC 2.4.1.187                Enzyme
NAME        N-acetylglucosaminyldiphosphoundecaprenol
            N-acetyl-beta-D-mannosaminyltransferase;
            uridine
            diphosphoacetyl-
            mannosamineacetylglucosaminylpyrophosphorylundecaprenol
            acetylmannosaminyltransferase;
            N-acetylmannosaminyltransferase;
            UDP-N-acetylmannosamine:N-acetylglucosaminyl
            diphosphorylundecaprenol N-acetylmannosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-mannosamine:N-acetyl-beta-D-glucosaminyldiphosphounde
            caprenol beta-1,4-N-acetylmannosaminyltransferase
REACTION    UDP-N-acetyl-D-mannosamine +
            N-acetyl-D-glucosaminyldiphosphoundecaprenol = UDP +
            N-acetyl-beta-D-mannosaminyl-1,4-N-acetyl-D-
            glucosaminyldiphosphoundecaprenol [RN:R05566 R06129]
ALL_REAC    R05566 R06129(G)
SUBSTRATE   UDP-N-acetyl-D-mannosamine [CPD:C01170];
            N-acetyl-D-glucosaminyldiphosphoundecaprenol [CPD:C01289]
PRODUCT     UDP [CPD:C00015];
            N-acetyl-beta-D-mannosaminyl-1,4-N-acetyl-D-
            glucosaminyldiphosphoundecaprenol [CPD:C04881]
COMMENT     Involved in the biosynthesis of teichoic acid linkage units in
            bacterial cell walls.
REFERENCE   1  [PMID:2977387]
  AUTHORS   Murazumi N, Kumita K, Araki Y, Ito E.
  TITLE     Partial purification and properties of
            UDP-N-acetylmannosamine:N-acetylglucosaminyl
            pyrophosphorylundecaprenol N-acetylmannosaminyltransferase from
            Bacillus subtilis.
  JOURNAL   J. Biochem. (Tokyo). 104 (1988) 980-4.
  ORGANISM  Bacillus subtilis [GN:bsu]
ORTHOLOGY   KO: K05946  
GENES       SPL: Spea_1424
            PIN: Ping_0436
            BXE: Bxe_B0500
            HAR: HEAR0725
            AFW: Anae109_3040
            SAT: SYN_01098
            BRA: BRADO4814
            BBT: BBta_1010
            RPE: RPE_1096 RPE_3494
            RRU: Rru_A1484
            BSU: BG10450(tagA)
            BAN: BA5669
            BAR: GBAA5669
            BAA: BA_0528
            BAT: BAS5272
            BCE: BC5419
            BCA: BCE_5548
            BCZ: BCZK2598 BCZK5116(tarA)
            BCY: Bcer98_3934
            BTK: BT9727_2627 BT9727_5099(tarA)
            BTL: BALH_2572(tarA) BALH_4923(tarA)
            BLI: BL02432(tagA)
            BLD: BLi03819(tagA)
            BAY: RBAM_032880(tagA)
            BPU: BPUM_3231(tagA)
            SAA: SAUSA300_0623(tagA)
            SAO: SAOUHSC_00640
            SAJ: SaurJH9_0659
            SAH: SaurJH1_0674
            LWE: lwe2469(tagA)
            LAC: LBA0519(tagA)
            LSA: LSA1571(tagA)
            LSL: LSL_1262
            LBR: LVIS_0542
            STH: STH138
            CPR: CPR_0585(tagA) CPR_1839(tagA)
            CTH: Cthe_2701
            CBO: CBO3092(tagA)
            CBE: Cbei_0985
            AMT: Amet_4139
            DSY: DSY4885
            DRM: Dred_3113
            SWO: Swol_2372
            CSC: Csac_1349
            TTE: TTE2163(wecG)
            MTA: Moth_2365
            AVA: Ava_0660 Ava_1375 Ava_4844
            TER: Tery_3422
            RRS: RoseRS_1978
            RCA: Rcas_3785
            TPT: Tpet_0109
            TME: Tmel_1334
            FNO: Fnod_1777
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.187
            ExPASy - ENZYME nomenclature database: 2.4.1.187
            ExplorEnz - The Enzyme Database: 2.4.1.187
            ERGO genome analysis and discovery system: 2.4.1.187
            BRENDA, the Enzyme Database: 2.4.1.187
            CAS: 118731-82-1
///
ENTRY       EC 2.4.1.188                Enzyme
NAME        N-acetylglucosaminyldiphosphoundecaprenol glucosyltransferase;
            UDP-D-glucose:N-acetylglucosaminyl pyrophosphorylundecaprenol
            glucosyltransferase;
            uridine
            diphosphoglucose-acetylglucosaminylpyrophosphorylundecaprenol
            glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:N-acetyl-D-glucosaminyldiphosphoundecaprenol
            4-beta-D-glucosyltransferase
REACTION    UDP-glucose + N-acetyl-D-glucosaminyldiphosphoundecaprenol = UDP +
            beta-D-glucosyl-1,4-N-acetyl-D-glucosaminyldiphosphoundecaprenol
            [RN:R06047 R06062]
ALL_REAC    R06047 R06062(G)
SUBSTRATE   UDP-glucose [CPD:C00029];
            N-acetyl-D-glucosaminyldiphosphoundecaprenol [CPD:C01289]
PRODUCT     UDP [CPD:C00015];
            beta-D-glucosyl-1,4-N-acetyl-D-glucosaminyldiphosphoundecaprenol
            [CPD:C04830]
REFERENCE   1  [PMID:2977388]
  AUTHORS   Kumita K, Murazumi N, Araki Y, Ito E.
  TITLE     Solubilization and properties of UDP-D-glucose:N-acetylglucosaminyl
            pyrophosphorylundecaprenol glucosyltransferase from Bacillus
            coagulans AHU 1366 membranes.
  JOURNAL   J. Biochem. (Tokyo). 104 (1988) 985-8.
  ORGANISM  Bacillus coagulans
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.188
            ExPASy - ENZYME nomenclature database: 2.4.1.188
            ExplorEnz - The Enzyme Database: 2.4.1.188
            ERGO genome analysis and discovery system: 2.4.1.188
            BRENDA, the Enzyme Database: 2.4.1.188
            CAS: 118731-83-2
///
ENTRY       EC 2.4.1.189                Enzyme
NAME        luteolin 7-O-glucuronosyltransferase;
            uridine diphosphoglucuronate-luteolin 7-O-glucuronosyltransferase;
            LGT
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucuronate:luteolin 7-O-glucuronosyltransferase
REACTION    UDP-glucuronate + luteolin = UDP + luteolin 7-O-beta-D-glucuronide
            [RN:R03589]
ALL_REAC    R03589
SUBSTRATE   UDP-glucuronate [CPD:C00167];
            luteolin [CPD:C01514]
PRODUCT     UDP [CPD:C00015];
            luteolin 7-O-beta-D-glucuronide [CPD:C03515]
REFERENCE   1
  AUTHORS   Schulz, M. and Weissenbock, G.
  TITLE     3 specific UDP-glucuronate-flavone-glucuronosyl-transferases from
            primary leaves of Secale cereale.
  JOURNAL   Phytochemistry 27 (1988) 1261-1267.
  ORGANISM  Secale cereale
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.189
            ExPASy - ENZYME nomenclature database: 2.4.1.189
            ExplorEnz - The Enzyme Database: 2.4.1.189
            ERGO genome analysis and discovery system: 2.4.1.189
            BRENDA, the Enzyme Database: 2.4.1.189
            CAS: 115490-49-8
///
ENTRY       EC 2.4.1.190                Enzyme
NAME        luteolin-7-O-glucuronide 2"-O-glucuronosyltransferase;
            uridine diphosphoglucuronate-luteolin 7-O-glucuronide
            glucuronosyltransferase;
            LMT;
            UDP-glucuronate:luteolin 7-O-glucuronide-glucuronosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucuronate:luteolin-7-O-beta-D-glucuronide
            2''-O-glucuronosyltransferase
REACTION    UDP-glucuronate + luteolin 7-O-beta-D-glucuronide = UDP + luteolin
            7-O-[beta-D-glucuronosyl-(1->2)-beta-D-glucuronide] [RN:R06827]
ALL_REAC    R06827
SUBSTRATE   UDP-glucuronate [CPD:C00167];
            luteolin 7-O-beta-D-glucuronide [CPD:C03515]
PRODUCT     UDP [CPD:C00015];
            luteolin 7-O-[beta-D-glucuronosyl-(1->2)-beta-D-glucuronide]
            [CPD:C12632]
REFERENCE   1
  AUTHORS   Schulz, M. and Weissenbock, G.
  TITLE     3 specific UDP-glucuronate-flavone-glucuronosyl-transferases from
            primary leaves of Secale cereale.
  JOURNAL   Phytochemistry 27 (1988) 1261-1267.
  ORGANISM  Secale cereale
REFERENCE   2
  AUTHORS   Anhalt, S. and Weissenbock, G.
  TITLE     Subcellular localization of luteolin glucuronides and related
            enzymes in rye mesophyll.
  JOURNAL   Planta 187 (1992) 83-88.
  ORGANISM  Secale cereale
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.190
            ExPASy - ENZYME nomenclature database: 2.4.1.190
            ExplorEnz - The Enzyme Database: 2.4.1.190
            ERGO genome analysis and discovery system: 2.4.1.190
            BRENDA, the Enzyme Database: 2.4.1.190
            CAS: 115490-51-2
///
ENTRY       EC 2.4.1.191                Enzyme
NAME        luteolin-7-O-diglucuronide 4'-O-glucuronosyltransferase;
            uridine diphosphoglucuronate-luteolin 7-O-diglucuronide
            glucuronosyltransferase;
            UDP-glucuronate:luteolin 7-O-diglucuronide-glucuronosyltransferase;
            UDPglucuronate:luteolin
            7-O-diglucuronide-4'-O-glucuronosyl-transferase;
            LDT
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucuronate:luteolin-7-O-beta-D-diglucuronide
            4'-O-glucuronosyltransferase
REACTION    UDP-glucuronate + luteolin 7-O-beta-D-diglucuronide = UDP + luteolin
            7-O-[beta-D-glucuronosyl-(1->2)-beta-D-glucuronide]-4'-O-beta-D-
            glucuronide [RN:R06828]
ALL_REAC    R06828
SUBSTRATE   UDP-glucuronate [CPD:C00167];
            luteolin 7-O-beta-D-diglucuronide [CPD:C12632]
PRODUCT     UDP [CPD:C00015];
            luteolin
            7-O-[beta-D-glucuronosyl-(1->2)-beta-D-glucuronide]-4'-O-beta-D-
            glucuronide [CPD:C04900]
REFERENCE   1
  AUTHORS   Schulz, M. and Weissenbock, G.
  TITLE     3 specific UDP-glucuronate-flavone-glucuronosyl-transferases from
            primary leaves of Secale cereale.
  JOURNAL   Phytochemistry 27 (1988) 1261-1267.
  ORGANISM  Secale cereale
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.191
            ExPASy - ENZYME nomenclature database: 2.4.1.191
            ExplorEnz - The Enzyme Database: 2.4.1.191
            ERGO genome analysis and discovery system: 2.4.1.191
            BRENDA, the Enzyme Database: 2.4.1.191
            CAS: 115490-50-1
///
ENTRY       EC 2.4.1.192                Enzyme
NAME        nuatigenin 3beta-glucosyltransferase;
            uridine diphosphoglucose-nuatigenin glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:(20S,22S,25S)-22,25-epoxyfurost-5-ene-3beta,26-diol
            3-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + (20S,22S,25S)-22,25-epoxyfurost-5-ene-3beta,26-diol =
            UDP + (20S,22S,25S)-22,25-epoxyfurost-5-ene-3beta,26-diol
            3-O-beta-D-glucoside [RN:R04577]
ALL_REAC    R04577
SUBSTRATE   UDP-glucose [CPD:C00029];
            (20S,22S,25S)-22,25-epoxyfurost-5-ene-3beta,26-diol [CPD:C04715]
PRODUCT     UDP [CPD:C00015];
            (20S,22S,25S)-22,25-epoxyfurost-5-ene-3beta,26-diol
            3-O-beta-D-glucoside [CPD:C04859]
COMMENT     Some other sapogenins can act as glucosyl acceptors. Involved in the
            biosynthesis of plant saponins. Not identical with EC 2.4.1.173
            (sterol 3beta-glucosyltransferase) or EC 2.4.1.193 (sarsapogenin
            3beta-glucosyltransferase).
REFERENCE   1
  AUTHORS   Kalinowska, M. and Wojciechowski, Z.A.
  TITLE     Enzymatic-synthesis of nuatigenin 3-beta-D-glucoside in oat (Avena
            sativa) leaves.
  JOURNAL   Phytochemistry 25 (1986) 2525-2529.
  ORGANISM  Avena sativa
REFERENCE   2
  AUTHORS   Kalinowska, M. and Wojciechowski, Z.A.
  TITLE     Subcellular-localization of UDPG-nuatigenin glucosyltransferase in
            oat leaves.
  JOURNAL   Phytochemistry 26 (1987) 353-357.
  ORGANISM  Avena sativa
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.192
            ExPASy - ENZYME nomenclature database: 2.4.1.192
            ExplorEnz - The Enzyme Database: 2.4.1.192
            ERGO genome analysis and discovery system: 2.4.1.192
            BRENDA, the Enzyme Database: 2.4.1.192
            CAS: 108891-57-2
///
ENTRY       EC 2.4.1.193                Enzyme
NAME        sarsapogenin 3beta-glucosyltransferase;
            uridine diphosphoglucose-sarsapogenin glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:(25S)-5beta-spirostan-3beta-ol
            3-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + (25S)-5beta-spirostan-3beta-ol = UDP +
            (25S)-5beta-spirostan-3beta-ol 3-O-beta-D-glucoside [RN:R04359]
ALL_REAC    R04359
SUBSTRATE   UDP-glucose [CPD:C00029];
            (25S)-5beta-spirostan-3beta-ol [CPD:C03963]
PRODUCT     UDP [CPD:C00015];
            (25S)-5beta-spirostan-3beta-ol 3-O-beta-D-glucoside [CPD:C04716]
COMMENT     Specific to 5beta-spirostanols. Involved in the biosynthesis of
            plant saponins. Not identical with EC 2.4.1.173 (sterol
            3beta-glucosyltransferase) or EC 2.4.1.192 (nuatigenin
            3beta-glucosyltransferase).
REFERENCE   1
  AUTHORS   Paczkowski, C. and Wojciechowski, Z.A.
  TITLE     The occurrence of UDPG-dependent glucosyltransferase specific for
            sarsasapogenin in Asparagus officinalis.
  JOURNAL   Phytochemistry 27 (1988) 2743-2747.
  ORGANISM  Asparagus officinalis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.193
            ExPASy - ENZYME nomenclature database: 2.4.1.193
            ExplorEnz - The Enzyme Database: 2.4.1.193
            ERGO genome analysis and discovery system: 2.4.1.193
            BRENDA, the Enzyme Database: 2.4.1.193
            CAS: 117698-14-3
///
ENTRY       EC 2.4.1.194                Enzyme
NAME        4-hydroxybenzoate 4-O-beta-D-glucosyltransferase;
            uridine diphosphoglucose-4-hydroxybenzoate glucosyltransferase;
            UDP-glucose:4-(beta-D-glucopyranosyloxy)benzoic acid
            glucosyltransferase;
            HBA glucosyltransferase;
            p-hydroxybenzoate glucosyltransferase;
            PHB glucosyltransferase;
            PHB-O-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:4-hydroxybenzoate 4-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + 4-hydroxybenzoate = UDP +
            4-(beta-D-glucosyloxy)benzoate [RN:R01304]
ALL_REAC    R01304
SUBSTRATE   UDP-glucose [CPD:C00029];
            4-hydroxybenzoate [CPD:C00156]
PRODUCT     UDP [CPD:C00015];
            4-(beta-D-glucosyloxy)benzoate [CPD:C03993]
REFERENCE   1
  AUTHORS   Katsumata, T., Shige, H. and Ejiri, S.-I.
  TITLE     Biochemical-studies on pollen. 34. UDP
            glucose-4-(beta-D-glucopyranosyloxy) benzoic-acid
            glucosyltransferase from the pollen of Pinus densiflora.
  JOURNAL   Phytochemistry 28 (1989) 359-362.
  ORGANISM  Pinus densiflora
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.194
            ExPASy - ENZYME nomenclature database: 2.4.1.194
            ExplorEnz - The Enzyme Database: 2.4.1.194
            ERGO genome analysis and discovery system: 2.4.1.194
            BRENDA, the Enzyme Database: 2.4.1.194
            CAS: 120860-68-6
///
ENTRY       EC 2.4.1.195                Enzyme
NAME        N-hydroxythioamide S-beta-glucosyltransferase;
            desulfoglucosinolate-uridine diphosphate glucosyltransferase;
            uridine diphosphoglucose-thiohydroximate glucosyltransferase;
            thiohydroximate beta-D-glucosyltransferase;
            UDPG:thiohydroximate glucosyltransferase;
            thiohydroximate S-glucosyltransferase;
            thiohydroximate glucosyltransferase;
            UDP-glucose:thiohydroximate S-beta-D-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:N-hydroxy-2-phenylethanethioamide
            S-beta-D-glucosyltransferase
REACTION    UDP-glucose + N-hydroxy-2-phenylethanethioamide = UDP +
            desulfoglucotropeolin [RN:R03213]
ALL_REAC    R03213
SUBSTRATE   UDP-glucose [CPD:C00029];
            N-hydroxy-2-phenylethanethioamide
PRODUCT     UDP [CPD:C00015];
            desulfoglucotropeolin [CPD:C01069]
COMMENT     Involved with EC 2.8.2.24, desulfoglucosinolate sulfotransferase, in
            the biosynthesis of thioglucosides in cruciferous plants.
REFERENCE   1  [PMID:2524977]
  AUTHORS   Jain JC, Reed DW, GrootWassink JW, Underhill EW.
  TITLE     A radioassay of enzymes catalyzing the glucosylation and sulfation
            steps of glucosinolate biosynthesis in Brassica species.
  JOURNAL   Anal. Biochem. 178 (1989) 137-40.
  ORGANISM  Brassica napus [GN:ebna]
REFERENCE   2  [PMID:8373190]
  AUTHORS   Reed DW, Davin L, Jain JC, Deluca V, Nelson L, Underhill EW.
  TITLE     Purification and properties of UDP-glucose:thiohydroximate
            glucosyltransferase from Brassica napus L. seedlings.
  JOURNAL   Arch. Biochem. Biophys. 305 (1993) 526-32.
  ORGANISM  Brassica napus [GN:ebna]
REFERENCE   3  [PMID:11198818]
  AUTHORS   Fahey JW, Zalcmann AT, Talalay P.
  TITLE     The chemical diversity and distribution of glucosinolates and
            isothiocyanates among plants.
  JOURNAL   Phytochemistry. 56 (2001) 5-51.
  ORGANISM  Brassica napus [GN:ebna]
REFERENCE   4
  AUTHORS   Grubb, C.D., Zipp, B.J., Ludwig-Muller, J., Masuno, M.N., Molinski,
            T.F. and Abel, S.
  TITLE     Arabidopsis glucosyltransferase UGT74B1 functions in glucosinolate
            biosynthesis and auxin homeostasis.
  JOURNAL   Plant J. 40 (2004) 893-908.
  ORGANISM  Brassica napus [GN:ebna]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.195
            ExPASy - ENZYME nomenclature database: 2.4.1.195
            ExplorEnz - The Enzyme Database: 2.4.1.195
            ERGO genome analysis and discovery system: 2.4.1.195
            BRENDA, the Enzyme Database: 2.4.1.195
            CAS: 9068-14-8
///
ENTRY       EC 2.4.1.196                Enzyme
NAME        nicotinate glucosyltransferase;
            uridine diphosphoglucose-nicotinate N-glucosyltransferase;
            UDP-glucose:nicotinic acid-N-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:nicotinate N-glucosyltransferase
REACTION    UDP-glucose + nicotinate = UDP + N-glucosylnicotinate [RN:R01722]
ALL_REAC    R01722
SUBSTRATE   UDP-glucose [CPD:C00029];
            nicotinate [CPD:C00253]
PRODUCT     UDP [CPD:C00015];
            N-glucosylnicotinate [CPD:C03003]
REFERENCE   1
  AUTHORS   Upmeier, B., Thomzik, J.E. and Barz, W.
  TITLE     Enzymatic studies on the reversible synthesis of nicotinic
            acid-N-glucoside in heterotrophic parsley cell suspension cultures.
  JOURNAL   Z. Naturforsch. C: Biosci. 43 (1988) 835-842.
  ORGANISM  parsley
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.196
            ExPASy - ENZYME nomenclature database: 2.4.1.196
            ExplorEnz - The Enzyme Database: 2.4.1.196
            ERGO genome analysis and discovery system: 2.4.1.196
            BRENDA, the Enzyme Database: 2.4.1.196
            CAS: 120858-56-2
///
ENTRY       EC 2.4.1.197                Enzyme
NAME        high-mannose-oligosaccharide
            beta-1,4-N-acetylglucosaminyltransferase;
            uridine diphosphoacetylglucosamine-oligosaccharide
            acetylglucosaminyltransferase;
            acetylglucosamine-oligosaccharide acetylglucosaminyltransferase;
            UDP-GlcNAc:oligosaccharide beta-N-acetylglucosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:high-mannose-oligosaccharide
            beta-1,4-N-acetylglucosaminyltransferase
REACTION    Transfers an N-acetyl-D-glucosamine residue from
            UDP-N-acetyl-D-glucosamine to the 4-position of a mannose linked
            alpha-1,6 to the core mannose of high-mannose oligosaccharides
            produced by Dictyostelium discoideum
COMMENT     The activity of the intersecting mannose residue as acceptor is
            dependent on two other mannose residues attached by alpha-1,3 and
            alpha-1,6 links.
REFERENCE   1  [PMID:2525124]
  AUTHORS   Sharkey DJ, Kornfeld R.
  TITLE     Identification of an N-acetylglucosaminyltransferase in
            Dictyostelium discoideum that transfers an &quot;intersecting&quot;
            N-acetylglucosamine residue to high mannose oligosaccharides.
  JOURNAL   J. Biol. Chem. 264 (1989) 10411-9.
  ORGANISM  Dictyostelium discoideum [GN:ddi]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.197
            ExPASy - ENZYME nomenclature database: 2.4.1.197
            ExplorEnz - The Enzyme Database: 2.4.1.197
            ERGO genome analysis and discovery system: 2.4.1.197
            BRENDA, the Enzyme Database: 2.4.1.197
            CAS: 123425-54-7
///
ENTRY       EC 2.4.1.198                Enzyme
NAME        phosphatidylinositol N-acetylglucosaminyltransferase;
            UDP-N-acetyl-D-glucosamine:phosphatidylinositol
            N-acetyl-D-glucosaminyltransferase;
            uridine diphosphoacetylglucosamine
            alpha1,6-acetyl-D-glucosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:1-phosphatidyl-1D-myo-inositol
            6-(N-acetyl-alpha-D-glucosaminyl)transferase
REACTION    UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP +
            6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
            [RN:R02654 R05916]
ALL_REAC    R02654 R05916(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            1-phosphatidyl-1D-myo-inositol [CPD:C01194]
PRODUCT     UDP [CPD:C00015];
            6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
COMMENT     Involved in the first step of glycosylphosphatidylinositol (GPI)
            anchor formation in all eukaryotes. In mammalian cells, the enzyme
            is composed of at least five subunits (PIG-A, PIG-H, PIG-C, GPI1 and
            PIG-P). PIG-A subunit is the catalytic subunit. In some species, the
            long-chain acyl groups of the phosphatidyl group are partly replaced
            by long-chain alkyl or alk-1-enyl groups.
REFERENCE   1  [PMID:2525555]
  AUTHORS   Doering TL, Masterson WJ, Englund PT, Hart GW.
  TITLE     Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of
            the trypanosome variant surface glycoprotein. Origin of the
            non-acetylated glucosamine.
  JOURNAL   J. Biol. Chem. 264 (1989) 11168-73.
  ORGANISM  Trypanosoma brucei [GN:tbr]
REFERENCE   2  [PMID:9463366]
  AUTHORS   Watanabe R, Inoue N, Westfall B, Taron CH, Orlean P, Takeda J,
            Kinoshita T.
  TITLE     The first step of glycosylphosphatidylinositol biosynthesis is
            mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1.
  JOURNAL   EMBO. J. 17 (1998) 877-85.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], human [GN:hsa], Plasmodium
            falciparum [GN:pfa], Trypanosoma brucei [GN:tbr]
REFERENCE   3  [PMID:10944123]
  AUTHORS   Watanabe R, Murakami Y, Marmor MD, Inoue N, Maeda Y, Hino J, Kangawa
            K, Julius M, Kinoshita T.
  TITLE     Initial enzyme for glycosylphosphatidylinositol biosynthesis
            requires PIG-P and is regulated by DPM2.
  JOURNAL   EMBO. J. 19 (2000) 4402-11.
  ORGANISM  Plasmodium falciparum [GN:pfa], Trypanosoma brucei [GN:tbr]
PATHWAY     PATH: map00563  Glycosylphosphatidylinositol(GPI)-anchor
                            biosynthesis
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K00751  phosphatidylinositol N-acetylglucosaminyltransferase
            KO: K03857  phosphatidylinositol glycan, class A
            KO: K03858  phosphatidylinositol glycan, class H
            KO: K03859  phosphatidylinositol glycan, class C
            KO: K03860  phosphatidylinositol glycan, class Q
            KO: K03861  phosphatidylinositol glycan, class P
GENES       HSA: 51227(PIGP) 5277(PIGA) 5279(PIGC) 5283(PIGH) 9091(PIGQ)
            PTR: 465507(PIGA) 469583(PIGC)
            MCC: 710780(PIGH)
            MMU: 110417(Pigh) 14755(Pigq) 18700(Piga) 56176(Pigp) 67292(Pigc)
            RNO: 287159(Pigq) 288238(Pigp_predicted) 362756(Pigh_predicted)
                 363464(Piga) 364032(Pigc)
            CFA: 478413(PIGP) 480073(PIGC) 490095(LOC490095) 491748(PIGA)
                 611566(PIGH)
            BTA: 510483(MGC128298) 515306(PIGH) 767951(MGC133558)
            GGA: 418517(PIGP) 418624(RCJMB04_1a24) 423271(PIGH) 424387(PIGC)
                 770171(PIGQ)
            XLA: 444055(MGC82665) 495323(LOC495323)
            XTR: 549621(pigp) 549879(LOC549879)
            DRE: 321218(pigq) 323994(pigc) 325316(pigp) 393921(zgc:56589)
                 436838(zgc:92758)
            SPU: 584339(LOC584339) 587900(LOC587900) 754165(LOC754165)
                 758861(LOC758861)
            DME: Dmel_CG12077 Dmel_CG14550 Dmel_CG32578(Gpi1) Dmel_CG6401
            CEL: D2085.6 T20D3.8
            ATH: AT1G61280 AT2G34980(SETH1) AT3G45100(SETH2) AT4G35530
            OSA: 4330019 4333542 4337911
            SCE: YDR437W(GPI19) YGR216C(GPI1) YNL038W(GPI15) YPL076W(GPI2)
                 YPL175W(SPT14)
            AGO: AGOS_AAL108C AGOS_ACL142W AGOS_AEL247W AGOS_AER333C
            PIC: PICST_23033 PICST_33798 PICST_50490(SPT14) PICST_57819(GPI1)
                 PICST_64550(PIG7)
            CAL: CaO19.11041 CaO19.6977 CaO19_10064(CaO19.10064)
                 CaO19_487(CaO19.487) CaO19_538(CaO19.538)
            CGR: CAGL0B02233g CAGL0F03597g CAGL0H05401g CAGL0J10604g
            SPO: SPAC22A12.13 SPBC30D10.11(gpi1) SPBC3D6.07 SPBC685.05
                 SPCC550.04c
            ANI: AN0636.2 AN8070.2
            AFM: AFUA_1G16950 AFUA_3G07170 AFUA_3G09860 AFUA_3G13360
                 AFUA_5G01810
            AOR: AO090003001344 AO090005000980 AO090020000206
            CNE: CND02330 CND04980 CNH00800 CNH02210
            UMA: UM00213.1
            ECU: ECU03_1250 ECU09_1210
            DDI: DDB_0231698(pigA) DDB_0231724 DDB_0233342(pigC)
                 DDB_0233344(pigH)
            PFA: PF10_0316 PFF0915w PFI0535w PFI1705w
            CPV: cgd1_3380 cgd2_840 cgd4_2100 cgd6_4600
            CHO: Chro.10380 Chro.20095 Chro.40236 Chro.60527
            TAN: TA10130 TA11115
            TPV: TP04_0759
            TET: TTHERM_00449060 TTHERM_00945240
            TBR: Tb10.6k15.0170 Tb10.70.0720 Tb927.2.1780
            TCR: 503781.20 507639.100 508307.100 509215.16
            LMA: LmjF33.1670 LmjF36.1710 LmjF36.4750
            EHI: 109.t00022 32.t00039 80.t00011 9.t00084
            BBT: BBta_1004
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.198
            ExPASy - ENZYME nomenclature database: 2.4.1.198
            ExplorEnz - The Enzyme Database: 2.4.1.198
            ERGO genome analysis and discovery system: 2.4.1.198
            BRENDA, the Enzyme Database: 2.4.1.198
            CAS: 144388-35-2
///
ENTRY       EC 2.4.1.199                Enzyme
NAME        beta-mannosylphosphodecaprenol---mannooligosaccharide
            6-mannosyltransferase;
            mannosylphospholipid-methylmannoside alpha-1,6-mannosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     beta-D-mannosylphosphodecaprenol:1,6-alpha-D-mannosyloligosaccharide
            1,6-alpha-D-mannosyltransferase
REACTION    beta-D-mannosylphosphodecaprenol +
            1,6-alpha-D-mannosyloligosaccharide = decaprenol phosphate +
            1,6-alpha-D-mannosyl-1,6-alpha-D-mannosyl-oligosaccharide [RN:R06046
            R06074]
ALL_REAC    R06046 R06074(G)
SUBSTRATE   beta-D-mannosylphosphodecaprenol [CPD:C04150];
            1,6-alpha-D-mannosyloligosaccharide [CPD:C04276]
PRODUCT     decaprenol phosphate [CPD:C02970];
            1,6-alpha-D-mannosyl-1,6-alpha-D-mannosyl-oligosaccharide
COMMENT     Involved in the formation of mannooligosaccharides in the membrane
            of Mycobacterium smegmatis.
REFERENCE   1  [PMID:2480954]
  AUTHORS   Yokoyama K, Ballou CE.
  TITLE     Synthesis of alpha 1----6-mannooligosaccharides in Mycobacterium
            smegmatis. Function of beta-mannosylphosphoryldecaprenol as the
            mannosyl donor.
  JOURNAL   J. Biol. Chem. 264 (1989) 21621-8.
  ORGANISM  Mycobacterium smegmatis [GN:msm]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.199
            ExPASy - ENZYME nomenclature database: 2.4.1.199
            ExplorEnz - The Enzyme Database: 2.4.1.199
            ERGO genome analysis and discovery system: 2.4.1.199
            BRENDA, the Enzyme Database: 2.4.1.199
            CAS: 125008-27-7
///
ENTRY       EC 2.4.1.200      Obsolete  Enzyme
NAME        Transferred to 4.2.2.17
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Transferred entry: now EC 4.2.2.17, inulin fructotransferase
            (DFA-I-forming). The enzyme was wrongly classified as a transferase
            rather than a lyase. (EC 2.4.1.200 created 1992, deleted 2004)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.200
            ExPASy - ENZYME nomenclature database: 2.4.1.200
            ExplorEnz - The Enzyme Database: 2.4.1.200
            ERGO genome analysis and discovery system: 2.4.1.200
            BRENDA, the Enzyme Database: 2.4.1.200
///
ENTRY       EC 2.4.1.201                Enzyme
NAME        alpha-1,6-mannosyl-glycoprotein
            4-beta-N-acetylglucosaminyltransferase;
            N-acetylglucosaminyltransferase VI;
            N-glycosyl-oligosaccharide-glycoprotein
            N-acetylglucosaminyltransferase VI;
            uridine diphosphoacetylglucosamine-glycopeptide
            beta-1->4-acetylglucosaminyltransferase VI;
            mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase;
            GnTVI
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:2,6-bis(N-acetyl-beta-D-glucosaminyl)-alp
            ha-D-mannosyl-glycoprotein 4-beta-N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine +
            2,6-bis(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl-R = UDP +
            2,4,6-tris(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl-R
            [RN:R04642]
ALL_REAC    R04642 > R05992(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            2,6-bis(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl-R
            [CPD:C04906]
PRODUCT     UDP [CPD:C00015];
            2,4,6-tris(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl-R
            [CPD:C04934]
COMMENT     R represents the remainder of the N-linked oligosaccharide in the
            glycoprotein acceptor (click here for diagram).
REFERENCE   1  [PMID:2525556]
  AUTHORS   Brockhausen I, Hull E, Hindsgaul O, Schachter H, Shah RN, Michnick
            SW, Carver JP.
  TITLE     Control of glycoprotein synthesis. Detection and characterization of
            a novel branching enzyme from hen oviduct,
            UDP-N-acetylglucosamine:GlcNAc beta 1-6 (GlcNAc beta 1-2)Man alpha-R
            (GlcNAc to Man) beta-4-N-acetylglucosaminyltransferase VI.
  JOURNAL   J. Biol. Chem. 264 (1989) 11211-21.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:10903319]
  AUTHORS   Taguchi T, Ogawa T, Inoue S, Inoue Y, Sakamoto Y, Korekane H,
            Taniguchi N.
  TITLE     Purification and characterization of UDP-GlcNAc: GlcNAcbeta
            1-6(GlcNAcbeta 1-2)Manalpha 1-R [GlcNAc to Man]-beta 1,
            4-N-acetylglucosaminyltransferase VI from hen oviduct.
  JOURNAL   J. Biol. Chem. 275 (2000) 32598-602.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.201
            ExPASy - ENZYME nomenclature database: 2.4.1.201
            ExplorEnz - The Enzyme Database: 2.4.1.201
            ERGO genome analysis and discovery system: 2.4.1.201
            BRENDA, the Enzyme Database: 2.4.1.201
            CAS: 119699-68-2
///
ENTRY       EC 2.4.1.202                Enzyme
NAME        2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one
            2-D-glucosyltransferase;
            uridine
            diphosphoglucose-2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one
            2-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one
            2-D-glucosyltransferase
REACTION    UDP-glucose + 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one =
            UDP + 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one
            2-D-glucoside [RN:R04579]
ALL_REAC    R04579
SUBSTRATE   UDP-glucose [CPD:C00029];
            2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one [CPD:C04720]
PRODUCT     UDP [CPD:C00015];
            2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucoside
            [CPD:C04831]
REFERENCE   1
  AUTHORS   Bailey, B.A. and Larson, R.L.
  TITLE     Hydroxamic acid glucosyltransferases from maize seedlings.
  JOURNAL   Plant Physiol. 90 (1989) 1071-1076.
  ORGANISM  Zea mays [GN:ezma]
PATHWAY     PATH: map00402  Benzoxazinone biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.202
            ExPASy - ENZYME nomenclature database: 2.4.1.202
            ExplorEnz - The Enzyme Database: 2.4.1.202
            ERGO genome analysis and discovery system: 2.4.1.202
            BRENDA, the Enzyme Database: 2.4.1.202
            CAS: 122544-56-3
///
ENTRY       EC 2.4.1.203                Enzyme
NAME        trans-zeatin O-beta-D-glucosyltransferase;
            zeatin O-beta-D-glucosyltransferase;
            uridine diphosphoglucose-zeatin O-glucosyltransferase;
            zeatin O-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:trans-zeatin O-beta-D-glucosyltransferase
REACTION    UDP-glucose + trans-zeatin = UDP + O-beta-D-glucosyl-trans-zeatin
            [RN:R02118]
ALL_REAC    R02118
SUBSTRATE   UDP-glucose [CPD:C00029];
            trans-zeatin [CPD:C00371]
PRODUCT     UDP [CPD:C00015];
            O-beta-D-glucosyl-trans-zeatin [CPD:C03423]
COMMENT     Unlike EC 2.4.1.215, cis-zeatin O-beta-D-glucosyltransferase,
            UDP-D-xylose can also act as donor (cf. EC 2.4.2.40, zeatin
            O-beta-D-xylosyltransferase).
REFERENCE   1  [PMID:16666929]
  AUTHORS   Dixon SC, Martin RC, Mok MC, Shaw G, Mok DW.
  TITLE     Zeatin Glycosylation Enzymes in Phaseolus: Isolation of
            O-Glucosyltransferase from P. lunatus and Comparison to
            O-Xylosyltransferase from P. vulgaris.
  JOURNAL   Plant. Physiol. 90 (1989) 1316-1321.
  ORGANISM  Phaseolus lunatus
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.203
            ExPASy - ENZYME nomenclature database: 2.4.1.203
            ExplorEnz - The Enzyme Database: 2.4.1.203
            ERGO genome analysis and discovery system: 2.4.1.203
            BRENDA, the Enzyme Database: 2.4.1.203
            CAS: 123644-76-8
///
ENTRY       EC 2.4.1.204      Obsolete  Enzyme
NAME        Transferred to 2.4.2.40
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Transferred entry: now EC 2.4.2.40 zeatin
            O-beta-D-xylosyltransferase (EC 2.4.1.204 created 1992, deleted
            2003)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.204
            ExPASy - ENZYME nomenclature database: 2.4.1.204
            ExplorEnz - The Enzyme Database: 2.4.1.204
            ERGO genome analysis and discovery system: 2.4.1.204
            BRENDA, the Enzyme Database: 2.4.1.204
///
ENTRY       EC 2.4.1.205                Enzyme
NAME        galactogen 6beta-galactosyltransferase;
            uridine diphosphogalactose-galactogen galactosyltransferase;
            1,6-D-galactosyltransferase;
            beta-(1-6)-D-galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:galactogen beta-1,6-D-galactosyltransferase
REACTION    UDP-galactose + galactogen = UDP + 1,6-beta-D-galactosylgalactogen
            [RN:R03679]
ALL_REAC    R03679
SUBSTRATE   UDP-galactose [CPD:C00052];
            galactogen [CPD:C01698]
PRODUCT     UDP [CPD:C00015];
            1,6-beta-D-galactosylgalactogen [CPD:C04034]
COMMENT     Galactogen from Helix pomatia is the most effective acceptor.
REFERENCE   1  [PMID:2505854]
  AUTHORS   Goudsmit EM, Ketchum PA, Grossens MK, Blake DA.
  TITLE     Biosynthesis of galactogen: identification of a
            beta-(1----6)-D-galactosyltransferase in Helix pomatia albumen
            glands.
  JOURNAL   Biochim. Biophys. Acta. 992 (1989) 289-97.
  ORGANISM  Helix pomatia
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.205
            ExPASy - ENZYME nomenclature database: 2.4.1.205
            ExplorEnz - The Enzyme Database: 2.4.1.205
            ERGO genome analysis and discovery system: 2.4.1.205
            BRENDA, the Enzyme Database: 2.4.1.205
            CAS: 88273-54-5
///
ENTRY       EC 2.4.1.206                Enzyme
NAME        lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase;
            LA2 synthase;
            beta1->3-N-acetylglucosaminyltransferase;
            uridine diphosphoacetylglucosamine-lactosylceramide
            beta-acetylglucosaminyltransferase;
            lactosylceramide beta-acetylglucosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:D-galactosyl-1,4-beta-D-glucosylceramide
            beta-1,3-acetylglucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine +
            D-galactosyl-1,4-beta-D-glucosylceramide = UDP +
            N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-
            glucosylceramide [RN:R04493 R05971]
ALL_REAC    R04493 R05971(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            D-galactosyl-1,4-beta-D-glucosylceramide [CPD:C01290]
PRODUCT     UDP [CPD:C00015];
            N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-
            glucosylceramide [CPD:C04845]
REFERENCE   1  [PMID:1825612]
  AUTHORS   Gottfries J, Percy AK, Mansson JE, Fredman P, Wikstrand CJ, Friedman
            HS, Bigner DD, Svennerholm L.
  TITLE     Glycolipids and glycosyltransferases in permanent cell lines
            established from human medulloblastomas.
  JOURNAL   Biochim. Biophys. Acta. 1081 (1991) 253-61.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:2960671]
  AUTHORS   Holmes EH, Hakomori S, Ostrander GK.
  TITLE     Synthesis of type 1 and 2 lacto series glycolipid antigens in human
            colonic adenocarcinoma and derived cell lines is due to activation
            of a normally unexpressed beta
            1----3N-acetylglucosaminyltransferase.
  JOURNAL   J. Biol. Chem. 262 (1987) 15649-58.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:1901591]
  AUTHORS   Percy AK, Gottfries J, Vilbergsson G, Mansson JE, Svennerholm L.
  TITLE     Glycosphingolipid glycosyltransferases in human fetal brain.
  JOURNAL   J. Neurochem. 56 (1991) 1461-5.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00601  Glycosphingolipid biosynthesis - lactoseries
            PATH: map00602  Glycosphingolipid biosynthesis - neo-lactoseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K03766  beta-1,3-N-acetylglucosaminyltransferase 5
GENES       HSA: 84002(B3GNT5)
            MMU: 108105(B3gnt5)
            RNO: 116740(B3gnt5)
            BTA: 767899(B3GNT5)
            SSC: 397599(B3GNT5)
            GGA: 424960(B3GNT5)
            XLA: 446540(b3gnt5) 496364(LOC496364)
            XTR: 394849(MGC76134)
            DRE: 336526(b3gnt5)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.206
            ExPASy - ENZYME nomenclature database: 2.4.1.206
            ExplorEnz - The Enzyme Database: 2.4.1.206
            ERGO genome analysis and discovery system: 2.4.1.206
            BRENDA, the Enzyme Database: 2.4.1.206
            CAS: 83682-80-8
///
ENTRY       EC 2.4.1.207                Enzyme
NAME        xyloglucan:xyloglucosyl transferase;
            endo-xyloglucan transferase;
            xyloglucan endotransglycosylase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     xyloglucan:xyloglucan xyloglucanotransferase
REACTION    breaks a beta-(1->4) bond in the backbone of a xyloglucan and
            transfers the xyloglucanyl segment on to O-4 of the non-reducing
            terminal glucose residue of an acceptor, which can be a xyloglucan
            or an oligosaccharide of xyloglucan
COMMENT     Does not use cello-oligosaccharides as either donor or acceptor.
REFERENCE   1  [PMID:1554366]
  AUTHORS   Fry SC, Smith RC, Renwick KF, Martin DJ, Hodge SK, Matthews KJ.
  TITLE     Xyloglucan endotransglycosylase, a new wall-loosening enzyme
            activity from plants.
  JOURNAL   Biochem. J. 282 ( Pt 3) (1992) 821-8.
  ORGANISM  Marchantia polymorpha, Mnium hornum, Allium schoenoprasum, Zea mays
            [GN:ezma], Holcus lanatus, Bromus erectus, Lupinus polyphyllus,
            Pisum sativum, Anthriscus sylvestris, Acer pseudoplatanus,
            Lycopersicon esculentum [GN:eles], Taraxacum officinale
REFERENCE   2  [PMID:1400418]
  AUTHORS   Nishitani K, Tominaga R.
  TITLE     Endo-xyloglucan transferase, a novel class of glycosyltransferase
            that catalyzes transfer of a segment of xyloglucan molecule to
            another xyloglucan molecule.
  JOURNAL   J. Biol. Chem. 267 (1992) 21058-64.
  ORGANISM  Vigna angularis
REFERENCE   3  [PMID:16526094]
  AUTHORS   Foucher AL, McIntosh A, Douce G, Wastling J, Tait A, Turner CM.
  TITLE     A proteomic analysis of arsenical drug resistance in Trypanosoma
            brucei.
  JOURNAL   Proteomics. 6 (2006) 2726-32.
REFERENCE   4
  AUTHORS   Lorences, E.P., Fry, S.C.
  TITLE     Xyloglucan oligosaccharides with at least two alpha-D-xylose
            residues act as acceptor substrates for xyloglucan
            endotransglycosylase and promote the depolymerisation of xyloglucan.
  JOURNAL   Plant Physiol. 88 (1993) 105-112.
  ORGANISM  Pisum sativum, Phaseolus vulgaris
ORTHOLOGY   KO: K08235  xyloglucan:xyloglucosyl transferase
GENES       ATH: AT1G10550(XTH33) AT1G11545 AT1G14720(XTR2) AT1G32170(XTR4)
                 AT1G65310(ATXTH17) AT2G01850(EXGT-A3) AT2G06850(EXGT-A1)
                 AT2G14620 AT2G18800 AT2G36870 AT3G23730 AT3G25050(XTH3)
                 AT3G44990(XTR8) AT4G13080 AT4G13090 AT4G14130(XTR7) AT4G18990
                 AT4G25810(XTR6) AT4G25820(XTR9) AT4G28850 AT4G30270(MERI5B)
                 AT4G30280(ATXTH18/XTH18) AT4G30290(ATXTH19) AT4G37800
                 AT5G13870(EXGT-A4) AT5G48070(ATXTH20) AT5G57530 AT5G57540
                 AT5G57550(XTR3) AT5G57560(TCH4) AT5G65730
            OSA: 4341940 4341944 4350662
STRUCTURES  PDB: 1UMZ  1UN1  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.207
            ExPASy - ENZYME nomenclature database: 2.4.1.207
            ExplorEnz - The Enzyme Database: 2.4.1.207
            ERGO genome analysis and discovery system: 2.4.1.207
            BRENDA, the Enzyme Database: 2.4.1.207
///
ENTRY       EC 2.4.1.208                Enzyme
NAME        diglucosyl diacylglycerol synthase;
            monoglucosyl diacylglycerol (1->2) glucosyltransferase;
            MGlcDAG (1->2) glucosyltransferase;
            DGlcDAG synthase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol
            (1->2) glucosyltransferase
REACTION    UDP-glucose + 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol =
            1,2-diacyl-3-O-(alpha-D-glucopyranosyl(1->2)-O-alpha-D-
            glucopyranosyl)sn-glycerol + UDP [RN:R05164]
ALL_REAC    R05164
SUBSTRATE   UDP-glucose [CPD:C00029];
            1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol [CPD:C06364]
PRODUCT     1,2-diacyl-3-O-(alpha-D-glucopyranosyl(1->2)-O-alpha-D-
            glucopyranosyl)sn-glycerol [CPD:C06365];
            UDP [CPD:C00015]
COFACTOR    Magnesium [CPD:C00305]
COMMENT     The enzyme from Acholeplasma laidlawii requires Mg2+.
REFERENCE   1  [PMID:8756472]
  AUTHORS   Karlsson OP, Rytomaa M, Dahlqvist A, Kinnunen PK, Wieslander A.
  TITLE     Correlation between bilayer lipid dynamics and activity of the
            diglucosyldiacylglycerol synthase from Acholeplasma laidlawii
            membranes.
  JOURNAL   Biochemistry. 35 (1996) 10094-102.
  ORGANISM  Acholeplasma laidlawii
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.208
            ExPASy - ENZYME nomenclature database: 2.4.1.208
            ExplorEnz - The Enzyme Database: 2.4.1.208
            ERGO genome analysis and discovery system: 2.4.1.208
            BRENDA, the Enzyme Database: 2.4.1.208
            CAS: 168680-19-1
///
ENTRY       EC 2.4.1.209                Enzyme
NAME        cis-p-coumarate glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:cis-p-coumarate beta-D-glucosyltransferase
REACTION    UDP-glucose + cis-p-coumarate = 4'-O-beta-D-glucosyl-cis-p-coumarate
            + UDP [RN:R05324]
ALL_REAC    R05324
SUBSTRATE   UDP-glucose [CPD:C00029];
            cis-p-coumarate [CPD:C06738]
PRODUCT     4'-O-beta-D-glucosyl-cis-p-coumarate [CPD:C06739];
            UDP [CPD:C00015]
COMMENT     cis-Caffeic acid also serves as a glucosyl acceptor with the enzyme
            from Sphagnum fallax kinggr. The corresponding trans-isomers are not
            substrates.
REFERENCE   1
  AUTHORS   Rasmussen, S. and Rudolph, H.
  TITLE     Isolation, purification and characterization of
            UDP-glucose:cis-p-coumaric acid-beta-D-glucosyltransferase from
            Sphagnum fallax.
  JOURNAL   Phytochemistry 46 (1997) 449-453.
  ORGANISM  Sphagnum fallax
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.209
            ExPASy - ENZYME nomenclature database: 2.4.1.209
            ExplorEnz - The Enzyme Database: 2.4.1.209
            ERGO genome analysis and discovery system: 2.4.1.209
            BRENDA, the Enzyme Database: 2.4.1.209
///
ENTRY       EC 2.4.1.210                Enzyme
NAME        limonoid glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     uridine diphosphoglucose-limonoid glucosyltransferase
REACTION    UDP-glucose + limonin = glucosyl-limonin + UDP [RN:R05325]
ALL_REAC    R05325
SUBSTRATE   UDP-glucose [CPD:C00029];
            limonin [CPD:C03514]
PRODUCT     glucosyl-limonin [CPD:C06740];
            UDP [CPD:C00015]
COMMENT     The enzyme purified from navel orange albedo tissue also acts on the
            related tetranortriterpenoid nomilin.
REFERENCE   1
  AUTHORS   Shin, H., Suhayda, C.G., Hsu, W.-J. and Robertson, G.H.
  TITLE     Purification of limonoid glucosyltransferase from navel orange
            albedo tissue.
  JOURNAL   Phytochemistry 46 (1997) 33-37.
  ORGANISM  Citrus sinensis [GN:ecsi]
ORTHOLOGY   KO: K08236  limonoid glucosyltransferase
GENES       ATH: AT3G21560(UGT84A2) AT4G15480(UGT84A1) AT4G15490(UGT84A3)
                 AT4G15500(UGT84A4)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.210
            ExPASy - ENZYME nomenclature database: 2.4.1.210
            ExplorEnz - The Enzyme Database: 2.4.1.210
            ERGO genome analysis and discovery system: 2.4.1.210
            BRENDA, the Enzyme Database: 2.4.1.210
///
ENTRY       EC 2.4.1.211                Enzyme
NAME        1,3-beta-galactosyl-N-acetylhexosamine phosphorylase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     beta-D-galactopyranosyl-(1->3)-N-acetyl-D-hexosamine:phosphate
            galactosyltransferase
REACTION    beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine + phosphate =
            alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
            [RN:R05326 R06057]
ALL_REAC    R05326 R06057(G)
SUBSTRATE   beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine [CPD:C06372];
            phosphate [CPD:C00009]
PRODUCT     alpha-D-galactopyranose 1-phosphate [CPD:C00446];
            N-acetyl-D-glucosamine [CPD:C00140]
COMMENT     Reaction also occurs with
            beta-D-galactopyranosyl-(1->3)-N-acetyl-D-galactosamine as the
            substrate, giving N-acetyl-D-galactosamine as the product.
REFERENCE   1  [PMID:9889079]
  AUTHORS   Derensy-Dron D, Krzewinski F, Brassart C, Bouquelet S.
  TITLE     Beta-1,3-galactosyl-N-acetylhexosamine phosphorylase from
            Bifidobacterium bifidum DSM 20082: characterization, partial
            purification and relation to mucin degradation.
  JOURNAL   Biotechnol. Appl. Biochem. 29 ( Pt 1) (1999) 3-10.
  ORGANISM  Bifidobacterium bifidum
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.211
            ExPASy - ENZYME nomenclature database: 2.4.1.211
            ExplorEnz - The Enzyme Database: 2.4.1.211
            ERGO genome analysis and discovery system: 2.4.1.211
            BRENDA, the Enzyme Database: 2.4.1.211
///
ENTRY       EC 2.4.1.212                Enzyme
NAME        hyaluronan synthase;
            spHAS;
            seHAS
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     Alternating
            UDP-alpha-N-acetyl-D-glucosamine:beta-D-glucuronosyl-(1->3)-[nascent
            hyaluronan] 4-N-acetyl-beta-D-glucosaminyltransferase and
            UDP-alpha-D-glucuronate:N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent
            hyaluronan] 3-beta-D-glucuronosyltransferase
REACTION    (1) UDP-alpha-N-acetyl-D-glucosamine +
            beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-
            [nascent hyaluronan] = UDP +
            N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-
            acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan] [RN:R05327
            R06068];
            (2) UDP-alpha-D-glucuronate +
            N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-
            [nascent hyaluronan] = UDP +
            beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-
            D-glucuronosyl-(1->3)-[nascent hyaluronan]
ALL_REAC    R05327 R06068(G)
SUBSTRATE   UDP-alpha-N-acetyl-D-glucosamine;
            beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-
            [nascent hyaluronan];
            UDP-alpha-D-glucuronate [CPD:C00167];
            N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-
            [nascent hyaluronan]
PRODUCT     UDP [CPD:C00015];
            N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-
            acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan];
            beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-
            D-glucuronosyl-(1->3)-[nascent hyaluronan]
COMMENT     The enzyme from Streptococcus Group A and Group C requires Mg2+. The
            enzyme adds GlcNAc to nascent hyaluronan when the non-reducing end
            is GlcA, but it adds GlcA when the non-reducing end is GlcNAc [3].
            The enzyme is highly specific for UDP-GlcNAc and UDP-GlcA; no
            copolymerization is observed if either is replaced by UDP-Glc,
            UDP-Gal, UDP-GalNAc or UDP-GalA. Similar enzymes have been found in
            a variety of organisms.
REFERENCE   1  [PMID:8366070]
  AUTHORS   DeAngelis PL, Papaconstantinou J, Weigel PH.
  TITLE     Molecular cloning, identification, and sequence of the hyaluronan
            synthase gene from group A Streptococcus pyogenes.
  JOURNAL   J. Biol. Chem. 268 (1993) 19181-4.
  ORGANISM  Streptococcus pyogenes
REFERENCE   2  [PMID:10988250]
  AUTHORS   Jing W, DeAngelis PL.
  TITLE     Dissection of the two transferase activities of the Pasteurella
            multocida hyaluronan synthase: two active sites exist in one
            polypeptide.
  JOURNAL   Glycobiology. 10 (2000) 883-9.
  ORGANISM  Pasteurella multocida [GN:pmu]
REFERENCE   3  [PMID:10473619]
  AUTHORS   DeAngelis PL.
  TITLE     Molecular directionality of polysaccharide polymerization by the
            Pasteurella multocida hyaluronan synthase.
  JOURNAL   J. Biol. Chem. 274 (1999) 26557-62.
  ORGANISM  Pasteurella multocida [GN:pmu]
ORTHOLOGY   KO: K00752  hyaluronan synthase
GENES       HSA: 3036(HAS1) 3037(HAS2) 3038(HAS3)
            PTR: 454195(HAS3) 472850(HAS2)
            MMU: 15116(Has1) 15117(Has2) 15118(Has3)
            RNO: 25694(Has2) 282821(Has1)
            CFA: 482032(HAS2) 611700(HAS1)
            BTA: 281220(HAS2)
            SSC: 397120(SHAS2) 408053(HAS3)
            GGA: 395594(HAS2)
            XLA: 379383(MGC52910)
            SPY: SPy_2200(hasA)
            SPZ: M5005_Spy_1851(hasA)
            SPM: spyM18_2236(hasA)
            SPG: SpyM3_1851(hasA)
            SPS: SPs1847
            SPH: MGAS10270_Spy1970(hasA)
            SPJ: MGAS2096_Spy1882(hasA)
            SPK: MGAS9429_Spy1862(hasA)
            SPF: SpyM51824(hasA)
            SPA: M6_Spy1869
            SPB: M28_Spy1883 M28_Spy1884(hasA)
            GFO: GFO_0015(hasA)
            FJO: Fjoh_4840
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.212
            ExPASy - ENZYME nomenclature database: 2.4.1.212
            ExplorEnz - The Enzyme Database: 2.4.1.212
            ERGO genome analysis and discovery system: 2.4.1.212
            BRENDA, the Enzyme Database: 2.4.1.212
///
ENTRY       EC 2.4.1.213                Enzyme
NAME        glucosylglycerol-phosphate synthase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     ADP-glucose:sn-glycerol-3-phosphate 2-beta-D-glucosyltransferase
REACTION    ADP-glucose + sn-glycerol 3-phosphate =
            2-(beta-D-glucosyl)-sn-glycerol 3-phosphate + ADP [RN:R05328]
ALL_REAC    R05328
SUBSTRATE   ADP-glucose [CPD:C00498];
            sn-glycerol 3-phosphate [CPD:C00093]
PRODUCT     2-(beta-D-glucosyl)-sn-glycerol 3-phosphate [CPD:C10517];
            ADP [CPD:C00008]
COMMENT     Acts with EC 3.1.3.69 (glucosylglycerol phosphatase) to form
            glucosylglycerol, an osmolyte that endows cyanobacteria with
            resistance to salt.
REFERENCE   1
  AUTHORS   Hagemann, M. and Erdmann, N.
  TITLE     Activation and pathway of glucosylglycerol biosynthesis in the
            cyanobacterium Synechocystis sp. PCC 6803.
  JOURNAL   Microbiology 140 (1994) 1427-1431.
  ORGANISM  Synechocystis sp.
REFERENCE   2  [PMID:9733686]
  AUTHORS   Marin K, Zuther E, Kerstan T, Kunert A, Hagemann M.
  TITLE     The ggpS gene from Synechocystis sp. strain PCC 6803 encoding
            glucosyl-glycerol-phosphate synthase is involved in osmolyte
            synthesis.
  JOURNAL   J. Bacteriol. 180 (1998) 4843-9.
  ORGANISM  Synechocystis sp.
ORTHOLOGY   KO: K03692  glucosylglycerol-phosphate synthase
GENES       PMY: Pmen_3120
            TBD: Tbd_2626
            OOE: OEOE_0646
            SYN: sll1566(ggpS)
            SYD: Syncc9605_1407
            SYE: Syncc9902_1079
            SYG: sync_1401(ggpS)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.213
            ExPASy - ENZYME nomenclature database: 2.4.1.213
            ExplorEnz - The Enzyme Database: 2.4.1.213
            ERGO genome analysis and discovery system: 2.4.1.213
            BRENDA, the Enzyme Database: 2.4.1.213
///
ENTRY       EC 2.4.1.214                Enzyme
NAME        glycoprotein 3-alpha-L-fucosyltransferase;
            GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,3-fucosyltransferase;
            GDP-L-Fuc:Asn-linked GlcNAc alpha1,3-fucosyltransferase;
            GDP-fucose:beta-N-acetylglucosamine (Fuc to
            (Fucalpha1->6GlcNAc)-Asn-peptide) alpha1->3-fucosyltransferase;
            GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked
            N-acetylglucosamine of
            4-N-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-
            acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-
            mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-
            glucosaminyl}asparagine) 3-alpha-L-fucosyl-transferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked
            N-acetylglucosamine of
            N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-a
            cetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-man
            nosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glu
            cosaminyl}asparagine) 3-alpha-L-fucosyl-transferase
REACTION    GDP-L-fucose +
            N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-
            acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-
            mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-
            glucosaminyl}asparagine = GDP +
            N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-
            acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-
            mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-
            fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl}asparagine [RN:R06015]
ALL_REAC    R06015(G)
SUBSTRATE   GDP-L-fucose [CPD:C00325];
            N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-
            acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-
            mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-
            glucosaminyl}asparagine
PRODUCT     GDP [CPD:C00035];
            N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-
            acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-
            mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-
            fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl}asparagine
COMMENT     Requires Mn2+. The enzyme transfers to N-linked oligosaccharide
            structures (N-glycans), generally with a specificity for N-glycans
            with one unsubstituted non-reducing terminal GlcNAc residue. This
            enzyme catalyses a reaction similar to that of EC 2.4.1.68,
            glycoprotein 6-alpha-L-fucosyltransferase, but transferring the
            L-fucosyl group from GDP-beta-L-fucose to form an alpha1,3-linkage
            rather than an alpha1,6-linkage. The N-glycan products of this
            enzyme are present in plants, insects and some other invertebrates
            (e.g., Schistosoma, Haemonchus, Lymnaea).
REFERENCE   1  [PMID:11420147]
  AUTHORS   Wilson IB, Rendic D, Freilinger A, Dumic J, Altmann F, Mucha J,
            Muller S, Hauser MT.
  TITLE     Cloning and expression of cDNAs encoding alpha1,3-fucosyltransferase
            homologues from Arabidopsis thaliana.
  JOURNAL   Biochim. Biophys. Acta. 1527 (2001) 88-96.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   2  [PMID:11382750]
  AUTHORS   Fabini G, Freilinger A, Altmann F, Wilson IB.
  TITLE     Identification of core alpha 1,3-fucosylated glycans and cloning of
            the requisite fucosyltransferase cDNA from Drosophila melanogaster.
            Potential basis of the neural anti-horseadish peroxidase epitope.
  JOURNAL   J. Biol. Chem. 276 (2001) 28058-67.
  ORGANISM  Drosophila melanogaster [GN:dme]
REFERENCE   3  [PMID:10419500]
  AUTHORS   Leiter H, Mucha J, Staudacher E, Grimm R, Glossl J, Altmann F.
  TITLE     Purification, cDNA cloning, and expression of GDP-L-Fuc:Asn-linked
            GlcNAc alpha1,3-fucosyltransferase from mung beans.
  JOURNAL   J. Biol. Chem. 274 (1999) 21830-9.
  ORGANISM  Vigna radiata
REFERENCE   4  [PMID:10567717]
  AUTHORS   van Tetering A, Schiphorst WE, van den Eijnden DH, van Die I.
  TITLE     Characterization of a core alpha1--&gt;3-fucosyltransferase from the
            snail Lymnaea stagnalis that is involved in the synthesis of
            complex-type N-glycans.
  JOURNAL   FEBS. Lett. 461 (1999) 311-4.
  ORGANISM  Lymnaea stagnalis
REFERENCE   5  [PMID:1868856]
  AUTHORS   Staudacher E, Altmann F, Glossl J, Marz L, Schachter H, Kamerling
            JP, Hard K, Vliegenthart JF.
  TITLE     GDP-fucose: beta-N-acetylglucosamine (Fuc to (Fuc alpha
            1----6GlcNAc)-Asn-peptide)alpha 1----3-fucosyltransferase activity
            in honeybee (Apis mellifica) venom glands. The difucosylation of
            asparagine-bound N-acetylglucosamine.
  JOURNAL   Eur. J. Biochem. 199 (1991) 745-51.
  ORGANISM  Apis mellifera [GN:dame]
PATHWAY     PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00753  glycoprotein 3-alpha-L-fucosyltransferase
GENES       HSA: 170384(FUT11)
            PTR: 450526(FUT11)
            MMU: 73068(Fut11)
            RNO: 286971(Fut11)
            CFA: 609950(FUT11)
            BTA: 539329(LOC539329)
            GGA: 395071(FUT11)
            XTR: 444888(fut11)
            DRE: 568888(zgc:153537)
            SPU: 578938(LOC578938)
            ATH: AT3G19280(FUT11)
            HPA: HPAG1_0636 HPAG1_1013
            HAC: Hac_0481(fucT_fragment_3)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.214
            ExPASy - ENZYME nomenclature database: 2.4.1.214
            ExplorEnz - The Enzyme Database: 2.4.1.214
            ERGO genome analysis and discovery system: 2.4.1.214
            BRENDA, the Enzyme Database: 2.4.1.214
            CAS: 68247-53-0
///
ENTRY       EC 2.4.1.215                Enzyme
NAME        cis-zeatin O-beta-D-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:cis-zeatin O-beta-D-glucosyltransferase
REACTION    UDP-glucose + cis-zeatin = UDP + O-beta-D-glucosyl-cis-zeatin
            [RN:R07260]
ALL_REAC    R07260
SUBSTRATE   UDP-glucose [CPD:C00029];
            cis-zeatin [CPD:C15545]
PRODUCT     UDP [CPD:C00015];
            O-beta-D-glucosyl-cis-zeatin
COMMENT     The enzyme from maize can use cis-zeatin and UDP-glucose as
            substrates, but not cis-ribosylzeatin, trans-zeatin or
            trans-ribosylzeatin. Unlike EC 2.4.1.203, trans-zeatin
            O-beta-D-glucosyltransferase, UDP-D-xylose cannot act as a donor.
REFERENCE   1  [PMID:11331778]
  AUTHORS   Martin RC, Mok MC, Habben JE, Mok DW.
  TITLE     A maize cytokinin gene encoding an O-glucosyltransferase specific to
            cis-zeatin.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 5922-6.
  ORGANISM  Zea mays [GN:ezma]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.215
            ExPASy - ENZYME nomenclature database: 2.4.1.215
            ExplorEnz - The Enzyme Database: 2.4.1.215
            ERGO genome analysis and discovery system: 2.4.1.215
            BRENDA, the Enzyme Database: 2.4.1.215
///
ENTRY       EC 2.4.1.216                Enzyme
NAME        trehalose 6-phosphate phosphorylase;
            trehalose 6-phosphate:phosphate beta-D-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     alpha,alpha-trehalose 6-phosphate:phosphate
            beta-D-glucosyltransferase
REACTION    alpha,alpha-trehalose 6-phosphate + phosphate = glucose 6-phosphate
            + beta-D-glucose 1-phosphate [RN:R05767 R06044]
ALL_REAC    R05767 R06044(G)
SUBSTRATE   alpha,alpha'-trehalose 6-phosphate [CPD:C00689];
            phosphate [CPD:C00009]
PRODUCT     glucose 6-phosphate [CPD:C00092];
            beta-D-glucose 1-phosphate [CPD:C00663]
COMMENT     The enzyme from Lactococcus lactis is specific for trehalose
            6-phosphate. Differs from EC 2.4.1.64, alpha,alpha-trehalose
            phosphorylase, in that trehalose is not a substrate.
REFERENCE   1  [PMID:11553642]
  AUTHORS   Andersson U, Levander F, Radstrom P.
  TITLE     Trehalose-6-phosphate phosphorylase is part of a novel metabolic
            pathway for trehalose utilization in Lactococcus lactis.
  JOURNAL   J. Biol. Chem. 276 (2001) 42707-13.
  ORGANISM  Lactococcus lactis
GENES       NOC: Noc_1775
            HHA: Hhal_0346
            AJS: Ajs_2162
            LLA: L39593(yeeA)
            TFU: Tfu_3044
            SEN: SACE_2445 SACE_2447
            CCH: Cag_0927
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.216
            ExPASy - ENZYME nomenclature database: 2.4.1.216
            ExplorEnz - The Enzyme Database: 2.4.1.216
            ERGO genome analysis and discovery system: 2.4.1.216
            BRENDA, the Enzyme Database: 2.4.1.216
///
ENTRY       EC 2.4.1.217                Enzyme
NAME        mannosyl-3-phosphoglycerate synthase;
            MPG synthase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-mannose:3-phosphoglycerate 3-alpha-D-mannosyltransferase
REACTION    GDP-mannose + 3-phospho-D-glycerate = GDP +
            2-(alpha-D-mannosyl)-3-phosphoglycerate [RN:R05768]
ALL_REAC    R05768
SUBSTRATE   GDP-mannose [CPD:C00096];
            3-phospho-D-glycerate [CPD:C00197]
PRODUCT     GDP [CPD:C00035];
            2-(alpha-D-mannosyl)-3-phosphoglycerate [CPD:C11516]
COMMENT     Requires Mg2+. The enzyme is absolutely specific for GDPmannose and
            3-phosphoglycerate, and transfers the mannosyl group with retention
            of configuration. In the hyperthermophilic archaeon Pyrococcus
            horikoshii, the mannosyl-3-phosphoglycerate formed is subsequently
            dephosphorylated by a specific phosphatase, EC 3.1.3.70
            (mannosyl-3-phosphoglycerate phosphatase), producing
            mannosylglycerate.
REFERENCE   1  [PMID:11562374]
  AUTHORS   Empadinhas N, Marugg JD, Borges N, Santos H, da Costa MS.
  TITLE     Pathway for the synthesis of mannosylglycerate in the
            hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and
            genetic characterization of key enzymes.
  JOURNAL   J. Biol. Chem. 276 (2001) 43580-8.
  ORGANISM  Pyrococcus horikoshii [GN:pho]
ORTHOLOGY   KO: K05947  
GENES       DET: DET1363(mpgSP)
            APE: APE_0889.1(mpgS)
            SMR: Smar_0498
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.217
            ExPASy - ENZYME nomenclature database: 2.4.1.217
            ExplorEnz - The Enzyme Database: 2.4.1.217
            ERGO genome analysis and discovery system: 2.4.1.217
            BRENDA, the Enzyme Database: 2.4.1.217
            CAS: 393512-63-5
///
ENTRY       EC 2.4.1.218                Enzyme
NAME        hydroquinone glucosyltransferase;
            arbutin synthase;
            hydroquinone:O-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:hydroquinone-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + hydroquinone = UDP +
            hydroquinone-O-beta-D-glucopyranoside [RN:R05769]
ALL_REAC    R05769
SUBSTRATE   UDP-glucose [CPD:C00029];
            hydroquinone [CPD:C00530]
PRODUCT     UDP [CPD:C00015];
            hydroquinone-O-beta-D-glucopyranoside [CPD:C06186]
COMMENT     Hydroquinone is the most effective acceptor, but over 40 phenolic
            compounds are also glucosylated, but at lower rates.
REFERENCE   1  [PMID:10680170]
  AUTHORS   Arend J, Warzecha H, Stockigt J.
  TITLE     Hydroquinone: O-glucosyltransferase from cultivated Rauvolfia cells:
            enrichment and partial amino acid sequences.
  JOURNAL   Phytochemistry. 53 (2000) 187-93.
  ORGANISM  Rauvolfia serpentina
REFERENCE   2  [PMID:11505382]
  AUTHORS   Arend J, Warzecha H, Hefner T, Stockigt J.
  TITLE     Utilizing genetically engineered bacteria to produce plant-specific
            glucosides.
  JOURNAL   Biotechnol. Bioeng. 76 (2001) 126-31.
  ORGANISM  Rauvolfia serpentina
ORTHOLOGY   KO: K08237  hydroquinone glucosyltransferase
GENES       ATH: AT1G01390 AT1G01420 AT4G01070
STRUCTURES  PDB: 2VCH  2VCU  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.218
            ExPASy - ENZYME nomenclature database: 2.4.1.218
            ExplorEnz - The Enzyme Database: 2.4.1.218
            ERGO genome analysis and discovery system: 2.4.1.218
            BRENDA, the Enzyme Database: 2.4.1.218
///
ENTRY       EC 2.4.1.219                Enzyme
NAME        vomilenine glucosyltransferase;
            UDPG:vomilenine 21-beta-D-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:vomilenine 21-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + vomilenine = UDP + raucaffricine [RN:R05882]
ALL_REAC    R05882
SUBSTRATE   UDP-glucose [CPD:C00029];
            vomilenine [CPD:C01761]
PRODUCT     UDP [CPD:C00015];
            raucaffricine [CPD:C02074]
COMMENT     The indole alkaloid raucaffricine accumulates during the culture of
            Rauvolfia cell suspensions.
REFERENCE   1  [PMID:10234858]
  AUTHORS   Warzecha H, Obitz P, Stockigt J.
  TITLE     Purification, partial amino acid sequence and structure of the
            product of raucaffricine-O-beta-D-glucosidase from plant cell
            cultures of Rauwolfia serpentina.
  JOURNAL   Phytochemistry. 50 (1999) 1099-109.
  ORGANISM  Rauwolfia serpentina
REFERENCE   2  [PMID:10975500]
  AUTHORS   Warzecha H, Gerasimenko I, Kutchan TM, Stockigt J.
  TITLE     Molecular cloning and functional bacterial expression of a plant
            glucosidase specifically involved in alkaloid biosynthesis.
  JOURNAL   Phytochemistry. 54 (2000) 657-66.
  ORGANISM  Rauwolfia serpentina
REFERENCE   3
  AUTHORS   Ruyter, C.M. and Stockigt, J.
  TITLE     Enzymatic formation of raucaffricine, the major indole alkaloid of
            Rauwolfia serpentina cell-suspension cultures.
  JOURNAL   Helv. Chim. Acta 74 (1991) 1707-1712.
  ORGANISM  Rauwolfia serpentina
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.219
            ExPASy - ENZYME nomenclature database: 2.4.1.219
            ExplorEnz - The Enzyme Database: 2.4.1.219
            ERGO genome analysis and discovery system: 2.4.1.219
            BRENDA, the Enzyme Database: 2.4.1.219
///
ENTRY       EC 2.4.1.220                Enzyme
NAME        indoxyl-UDPG glucosyltransferase;
            indoxyl-UDPG-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:indoxyl 3-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + indoxyl = UDP + indican [RN:R06048]
ALL_REAC    R06048
SUBSTRATE   UDP-glucose [CPD:C00029];
            indoxyl [CPD:C05658]
PRODUCT     UDP [CPD:C00015];
            indican [CPD:C08481]
COMMENT     Also acts to a limited extent on 4-, 5-, 6- and 7-hydroxyindole.
            After enzymic or chemical hydrolysis, indican forms indoxyl, which,
            in turn, is converted in the presence of oxygen to the dye indigo.
REFERENCE   1  [PMID:10680172]
  AUTHORS   Marcinek H, Weyler W, Deus-Neumann B, Zenk MH.
  TITLE     Indoxyl-UDPG-glucosyltransferase from Baphicacanthus cusia.
  JOURNAL   Phytochemistry. 53 (2000) 201-7.
  ORGANISM  Baphicacanthus cusia
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.220
            ExPASy - ENZYME nomenclature database: 2.4.1.220
            ExplorEnz - The Enzyme Database: 2.4.1.220
            ERGO genome analysis and discovery system: 2.4.1.220
            BRENDA, the Enzyme Database: 2.4.1.220
            CAS: 258339-72-9
///
ENTRY       EC 2.4.1.221                Enzyme
NAME        peptide-O-fucosyltransferase;
            GDP-L-fucose:polypeptide fucosyltransferase;
            GDP-fucose protein O-fucosyltransferase;
            GDP-fucose:polypeptide fucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-beta-L-fucose:polypeptide O-alpha-L-fucosyltransferase
REACTION    transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the
            serine hydroxy group of a protein acceptor
COMMENT     Involved in the biosynthesis of O-fucosylated epidermal growth
            factor (EGF) and thrombospondin type 1 repeats. The attachment of
            O-linked fucose to serine or threonine occurs on EGF domains within
            the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys.
REFERENCE   1  [PMID:9525914]
  AUTHORS   Wang Y, Spellman MW.
  TITLE     Purification and characterization of a GDP-fucose:polypeptide
            fucosyltransferase from Chinese hamster ovary cells.
  JOURNAL   J. Biol. Chem. 273 (1998) 8112-8.
  ORGANISM  hamster
REFERENCE   2  [PMID:11524432]
  AUTHORS   Wang Y, Shao L, Shi S, Harris RJ, Spellman MW, Stanley P,
            Haltiwanger RS.
  TITLE     Modification of epidermal growth factor-like repeats with O-fucose.
            Molecular cloning and expression of a novel GDP-fucose protein
            O-fucosyltransferase.
  JOURNAL   J. Biol. Chem. 276 (2001) 40338-45.
  ORGANISM  hamster
REFERENCE   3  [PMID:9023546]
  AUTHORS   Wang Y, Lee GF, Kelley RF, Spellman MW.
  TITLE     Identification of a GDP-L-fucose:polypeptide fucosyltransferase and
            enzymatic addition of O-linked fucose to EGF domains.
  JOURNAL   Glycobiology. 6 (1996) 837-42.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:11067851]
  AUTHORS   Hofsteenge J, Huwiler KG, Macek B, Hess D, Lawler J, Mosher DF,
            Peter-Katalinic J.
  TITLE     C-mannosylation and O-fucosylation of the thrombospondin type 1
            module.
  JOURNAL   J. Biol. Chem. 276 (2001) 6485-98.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K03691  peptide-O-fucosyltransferase
GENES       HSA: 23275(POFUT2) 23509(POFUT1)
            PTR: 449504(POFUT1) 449505(POFUT2)
            MMU: 140484(Pofut1) 80294(Pofut2)
            RNO: 309686(Pofut2_predicted) 311551(Pofut1)
            CFA: 609881(POFUT1)
            BTA: 360194(POFUT1) 404083(POFUT2)
            GGA: 395070(RCJMB04_4e3) 395112(POFUT2)
            XTR: 496411(pofut1)
            DRE: 403029(pofut1)
            SPU: 578163(LOC578163) 585387(LOC585387)
            DME: Dmel_CG12366(O-fut1) Dmel_CG14789(O-fut2)
            CEL: C15C7.7 K10G9.3(pad-2)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.221
            ExPASy - ENZYME nomenclature database: 2.4.1.221
            ExplorEnz - The Enzyme Database: 2.4.1.221
            ERGO genome analysis and discovery system: 2.4.1.221
            BRENDA, the Enzyme Database: 2.4.1.221
            CAS: 9033-08-3
///
ENTRY       EC 2.4.1.222                Enzyme
NAME        O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase;
            O-fucosylpeptide beta-1,3-N-acetylglucosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-D-GlcNAc:O-L-fucosylpeptide
            3-beta-N-acetyl-D-glucosaminyltransferase
REACTION    transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose
            residue of a fucosylated protein acceptor
COMMENT     O-Fucosylpeptide 3-beta-N-acetylglucosaminyltransferases are the
            products of fringe genes. O-linked fucose is an unusual form of
            glycosylation where the fucose is attached directly to proteins
            through the hydroxy groups of Ser or Thr residues.
REFERENCE   1  [PMID:10935626]
  AUTHORS   Moloney DJ, Panin VM, Johnston SH, Chen J, Shao L, Wilson R, Wang Y,
            Stanley P, Irvine KD, Haltiwanger RS, Vogt TF.
  TITLE     Fringe is a glycosyltransferase that modifies Notch.
  JOURNAL   Nature. 406 (2000) 369-75.
  ORGANISM  Drosophila sp., mammalian
PATHWAY     PATH: map04330  Notch signaling pathway
ORTHOLOGY   KO: K05948  fringe
GENES       HSA: 3955(LFNG) 4242(MFNG) 5986(RFNG)
            PTR: 458811(MFNG) 472272(LFNG)
            MMU: 16848(Lfng) 17305(Mfng) 19719(Rfng)
            RNO: 170905(Lfng) 315119(Mfng) 60433(Rfng)
            CFA: 483376(RFNG) 489891(LOC489891) 610303(MFNG)
            BTA: 505267(MFNG) 516209(MGC128664) 532242(LOC532242)
            GGA: 395789(RFNG) 395790(LFNG) 418042(MFNG)
            XTR: 549805(lfng)
            DRE: 30158(lfng) 414848(rfng) 493633(mfng)
            SPU: 578181(LOC578181)
            DME: Dmel_CG10580(fng)
STRUCTURES  PDB: 2J0A  2J0B  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.222
            ExPASy - ENZYME nomenclature database: 2.4.1.222
            ExplorEnz - The Enzyme Database: 2.4.1.222
            ERGO genome analysis and discovery system: 2.4.1.222
            BRENDA, the Enzyme Database: 2.4.1.222
            CAS: 299203-70-6
///
ENTRY       EC 2.4.1.223                Enzyme
NAME        glucuronyl-galactosyl-proteoglycan
            4-alpha-N-acetylglucosaminyltransferase;
            alpha-N-acetylglucosaminyltransferase I;
            alpha1,4-N-acetylglucosaminyltransferase;
            glucuronosylgalactosyl-proteoglycan
            4-alpha-N-acetylglucosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:beta-D-glucuronosyl-(1->3)-beta-D-galacto
            syl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan
            4IV-alpha-N-acetyl-D-glucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine +
            beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-
            galactosyl-(1->4)-beta-D-xylosyl-proteoglycan = UDP +
            alpha-N-acetyl-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-
            beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-
            proteoglycan [RN:R05930]
ALL_REAC    R05930(G);
            (other) R07397
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-
            galactosyl-(1->4)-beta-D-xylosyl-proteoglycan
PRODUCT     UDP [CPD:C00015];
            alpha-N-acetyl-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-
            beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-
            proteoglycan
COMMENT     Enzyme involved in the initiation of heparin and heparan sulfate
            synthesis, transferring GlcNAc to the (GlcA-Gal-Gal-Xyl-)Ser core.
            Apparently products of both the human EXTL2 and EXTL3 genes can
            catalyse this reaction. In Caenorhabditis elegans, the product of
            the rib-2 gene displays this activity as well as that of EC
            2.4.1.224, glucuronosyl-N-acetylglucosaminyl-proteoglycan
            4-alpha-N-acetylglucosaminyltransferase. For explanation of the use
            of a superscript in the systematic name, see 2-Carb-37.2.)
REFERENCE   1  [PMID:10318803]
  AUTHORS   Kitagawa H, Shimakawa H, Sugahara K.
  TITLE     The tumor suppressor EXT-like gene EXTL2 encodes an alpha1,
            4-N-acetylhexosaminyltransferase that transfers
            N-acetylgalactosamine and N-acetylglucosamine to the common
            glycosaminoglycan-protein linkage region. The key enzyme for the
            chain initiation of heparan sulfate.
  JOURNAL   J. Biol. Chem. 274 (1999) 13933-7.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:11121397]
  AUTHORS   Kitagawa H, Egusa N, Tamura JI, Kusche-Gullberg M, Lindahl U,
            Sugahara K.
  TITLE     rib-2, a Caenorhabditis elegans homolog of the human tumor
            suppressor EXT genes encodes a novel
            alpha1,4-N-acetylglucosaminyltransferase involved in the
            biosynthetic initiation and elongation of heparan sulfate.
  JOURNAL   J. Biol. Chem. 276 (2001) 4834-8.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00534  Heparan sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K02369  alpha-1,4-N-acetylglucosaminyltransferase EXTL2
            KO: K02370  alpha-1,4-N-acetylglucosaminyltransferase EXTL3
GENES       HSA: 2135(EXTL2) 2137(EXTL3)
            PTR: 457060(EXTL2)
            MMU: 54616(Extl3) 58193(Extl2)
            RNO: 310803(Extl2) 56819(Extl3)
            CFA: 479925(EXTL2) 486091(EXTL3)
            BTA: 540527(LOC540527)
            GGA: 422022(EXTL3)
            XLA: 443929(MGC80258) 447542(MGC83950)
            XTR: 493327(MGC89702) 493398(extl3)
            DRE: 493783(extl3) 558373(zgc:153688)
            SPU: 585810(LOC585810)
            DME: Dmel_CG15110(botv)
            CEL: K01G5.6(rib-2)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.223
            ExPASy - ENZYME nomenclature database: 2.4.1.223
            ExplorEnz - The Enzyme Database: 2.4.1.223
            ERGO genome analysis and discovery system: 2.4.1.223
            BRENDA, the Enzyme Database: 2.4.1.223
            CAS: 9075-15-4
///
ENTRY       EC 2.4.1.224                Enzyme
NAME        glucuronosyl-N-acetylglucosaminyl-proteoglycan
            4-alpha-N-acetylglucosaminyltransferase;
            alpha-N-acetylglucosaminyltransferase II
            glucuronyl-N-acetylglucosaminylproteoglycan
            alpha-1,4-N-acetylglucosaminyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:beta-D-glucuronosyl-(1->4)-N-acetyl-alpha
            -D-glucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
REACTION    UDP-N-acetyl-D-glucosamine +
            beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-
            proteoglycan = UDP +
            N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-
            acetyl-alpha-D-glucosaminyl-proteoglycan [RN:R07334]
ALL_REAC    R07334 > R05936(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-
            proteoglycan
PRODUCT     UDP [CPD:C00015];
            N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-
            acetyl-alpha-D-glucosaminyl-proteoglycan
COMMENT     Involved in the biosynthesis of heparin and heparan sulfate. Some
            forms of the enzyme from human (particularly the enzyme complex
            encoded by the EXT1 and EXT2 genes) act as bifunctional
            glycosyltransferases, which also have the
            4-beta-glucuronosyltransferase (EC 2.4.1.225,
            N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase)
            activity required for the synthesis of the heparan sulfate
            disaccharide repeats. Other human forms of this enzyme (e.g. the
            product of the EXTL1 gene) have only the
            4-alpha-N-acetylglucosaminyltransferase activity. In Caenorhabditis
            elegans, the product of the rib-2 gene displays the activities of
            this enzyme as well as EC 2.4.1.223,
            glucuronyl-galactosyl-proteoglycan
            4-alpha-N-acetylglucosaminyltransferase.
REFERENCE   1  [PMID:11390981]
  AUTHORS   Kim BT, Kitagawa H, Tamura  J, Saito T, Kusche-Gullberg M, Lindahl
            U, Sugahara K.
  TITLE     Human tumor suppressor EXT gene family members EXTL1 and EXTL3
            encode alpha 1,4- N-acetylglucosaminyltransferases that likely are
            involved in heparan sulfate/ heparin biosynthesis.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 7176-81.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:11121397]
  AUTHORS   Kitagawa H, Egusa N, Tamura JI, Kusche-Gullberg M, Lindahl U,
            Sugahara K.
  TITLE     rib-2, a Caenorhabditis elegans homolog of the human tumor
            suppressor EXT genes encodes a novel
            alpha1,4-N-acetylglucosaminyltransferase involved in the
            biosynthetic initiation and elongation of heparan sulfate.
  JOURNAL   J. Biol. Chem. 276 (2001) 4834-8.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:11256613]
  AUTHORS   Senay C, Lind T, Muguruma K, Tone Y, Kitagawa H, Sugahara K, Lidholt
            K, Lindahl U, Kusche-Gullberg M.
  TITLE     The EXT1/EXT2 tumor suppressors: catalytic activities and role in
            heparan sulfate biosynthesis.
  JOURNAL   EMBO. Rep. 1 (2000) 282-6.
  ORGANISM  mouse [GN:mmu]
REFERENCE   4  [PMID:9756849]
  AUTHORS   Lind T, Tufaro F, McCormick C, Lindahl U, Lidholt K.
  TITLE     The putative tumor suppressors EXT1 and EXT2 are
            glycosyltransferases required for the biosynthesis of heparan
            sulfate.
  JOURNAL   J. Biol. Chem. 273 (1998) 26265-8.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00534  Heparan sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K02366  glucuronyl/N-acetylglucosaminyl transferase EXT1
            KO: K02367  glucuronyl/N-acetylglucosaminyl transferase EXT2
            KO: K02368  alpha-1,4-N-acetylglucosaminyltransferase EXTL1
            KO: K02370  alpha-1,4-N-acetylglucosaminyltransferase EXTL3
GENES       HSA: 2131(EXT1) 2132(EXT2) 2134(EXTL1) 2137(EXTL3)
            PTR: 451140(EXT2) 464349(EXT1) 469238(EXTL1)
            MMU: 14042(Ext1) 14043(Ext2) 54616(Extl3) 56219(Extl1)
            RNO: 299907(LOC299907) 311215(Ext2_predicted)
                 313610(Extl1_predicted) 56819(Extl3)
            CFA: 475989(EXT2) 482024(EXT1) 486091(EXTL3) 487363(EXTL1)
            BTA: 281151(EXT2) 511060(LOC511060)
            GGA: 420283(EXT1) 422022(EXTL3) 425859(RCJMB04_7p22)
            XLA: 380140(ext2) 399115(XEXT1) 447542(MGC83950)
            XTR: 448393(ext1) 493398(extl3)
            DRE: 493780(ext2) 493783(extl3) 497280(ext1b)
            SPU: 577995(LOC577995) 585810(LOC585810)
            DME: Dmel_CG10117(ttv) Dmel_CG15110(botv)
            CEL: F12F6.3(rib-1) K01G5.6(rib-2)
            ECI: UTI89_C1045(hyaF)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.224
            ExPASy - ENZYME nomenclature database: 2.4.1.224
            ExplorEnz - The Enzyme Database: 2.4.1.224
            ERGO genome analysis and discovery system: 2.4.1.224
            BRENDA, the Enzyme Database: 2.4.1.224
            CAS: 145539-84-0
///
ENTRY       EC 2.4.1.225                Enzyme
NAME        N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase;
            N-acetylglucosaminylproteoglycan beta-1,4-glucuronyltransferase;
            heparan glucuronyltransferase II
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-alpha-D-glucuronate:N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-
            glucuronosyl-proteoglycan 4-beta-glucuronosyltransferase
REACTION    UDP-alpha-D-glucuronate +
            N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-
            proteoglycan = UDP +
            beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-(1->4)-
            beta-D-glucuronosyl-proteoglycan [RN:R07335]
ALL_REAC    R07335 > R05935(G)
SUBSTRATE   UDP-alpha-D-glucuronate [CPD:C00167];
            N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-
            proteoglycan
PRODUCT     UDP [CPD:C00015];
            beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-(1->4)-
            beta-D-glucuronosyl-proteoglycan
COMMENT     Involved in the biosynthesis of heparin and heparan sulfate. Some
            forms of the human enzyme (particularly the enzyme complex encoded
            by the EXT1 and EXT2 genes) act as bifunctional
            glycosyltransferases, which also have the
            glucuronosyl-N-acetylglucosaminyl-proteoglycan
            4-alpha-N-acetylglucosaminyltransferase (EC 2.4.1.224) activity
            required for the synthesis of the heparan sulfate disaccharide
            repeats.
REFERENCE   1  [PMID:11256613]
  AUTHORS   Senay C, Lind T, Muguruma K, Tone Y, Kitagawa H, Sugahara K, Lidholt
            K, Lindahl U, Kusche-Gullberg M.
  TITLE     The EXT1/EXT2 tumor suppressors: catalytic activities and role in
            heparan sulfate biosynthesis.
  JOURNAL   EMBO. Rep. 1 (2000) 282-6.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:9756849]
  AUTHORS   Lind T, Tufaro F, McCormick C, Lindahl U, Lidholt K.
  TITLE     The putative tumor suppressors EXT1 and EXT2 are
            glycosyltransferases required for the biosynthesis of heparan
            sulfate.
  JOURNAL   J. Biol. Chem. 273 (1998) 26265-8.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00534  Heparan sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K02366  glucuronyl/N-acetylglucosaminyl transferase EXT1
            KO: K02367  glucuronyl/N-acetylglucosaminyl transferase EXT2
GENES       HSA: 2131(EXT1) 2132(EXT2)
            PTR: 451140(EXT2) 464349(EXT1)
            MMU: 14042(Ext1) 14043(Ext2)
            RNO: 299907(LOC299907) 311215(Ext2_predicted)
            CFA: 475989(EXT2) 482024(EXT1)
            BTA: 281151(EXT2)
            GGA: 420283(EXT1) 425859(RCJMB04_7p22)
            XLA: 380140(ext2) 399115(XEXT1)
            XTR: 448393(ext1)
            DRE: 493780(ext2) 497280(ext1b) 497281(ext1c)
            SPU: 577995(LOC577995)
            DME: Dmel_CG10117(ttv)
            CEL: F12F6.3(rib-1)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.225
            ExPASy - ENZYME nomenclature database: 2.4.1.225
            ExplorEnz - The Enzyme Database: 2.4.1.225
            ERGO genome analysis and discovery system: 2.4.1.225
            BRENDA, the Enzyme Database: 2.4.1.225
            CAS: 145539-84-0
///
ENTRY       EC 2.4.1.226                Enzyme
NAME        N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase;
            chondroitin glucuronyltransferase II
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     alpha-D-glucuronate:N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glu
            curonosyl-proteoglycan 3-beta-glucuronosyltransferase
REACTION    UDP-alpha-D-glucuronate +
            N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-
            proteoglycan = UDP +
            beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-
            beta-D-glucuronosyl-proteoglycan [RN:R07336]
ALL_REAC    R07336 > R05931(G) R05933(G)
SUBSTRATE   UDP-alpha-D-glucuronate [CPD:C00167];
            N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-
            proteoglycan
PRODUCT     UDP [CPD:C00015];
            beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-
            beta-D-glucuronosyl-proteoglycan
COMMENT     Involved in the biosynthesis of chondroitin and dermatan sulfate.
            The human chondroitin synthetase is a bifunctional
            glycosyltransferase, which has the 3-beta-glucuronosyltransferase
            and 4-beta-N-acetylgalactosaminyltransferase (EC 2.4.1.175)
            activities required for the synthesis of the chondroitin sulfate
            disaccharide repeats. Similar chondroitin synthase 'co-polymerases'
            can be found in Pasteurella multocida and Escherichia coli. There is
            also another human protein with apparently only the
            3-beta-glucuronosyltransferase activity.
REFERENCE   1  [PMID:11514575]
  AUTHORS   Kitagawa H, Uyama T, Sugahara K.
  TITLE     Molecular cloning and expression of a human chondroitin synthase.
  JOURNAL   J. Biol. Chem. 276 (2001) 38721-6.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:10818104]
  AUTHORS   DeAngelis PL, Padgett-McCue AJ.
  TITLE     Identification and molecular cloning of a chondroitin synthase from
            Pasteurella multocida type F.
  JOURNAL   J. Biol. Chem. 275 (2000) 24124-9.
  ORGANISM  Pasteurella multocida [GN:pmu]
REFERENCE   3  [PMID:11943778]
  AUTHORS   Ninomiya T, Sugiura N, Tawada A, Sugimoto K, Watanabe H, Kimata K.
  TITLE     Molecular cloning and characterization of chondroitin polymerase
            from Escherichia coli strain K4.
  JOURNAL   J. Biol. Chem. 277 (2002) 21567-75.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:12145278]
  AUTHORS   Gotoh M, Yada T, Sato T, Akashima T, Iwasaki H, Mochizuki H, Inaba
            N, Togayachi A, Kudo T, Watanabe H, Kimata K, Narimatsu H.
  TITLE     Molecular cloning and characterization of a novel chondroitin
            sulfate glucuronyltransferase that transfers glucuronic acid to
            N-acetylgalactosamine.
  JOURNAL   J. Biol. Chem. 277 (2002) 38179-88.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00532  Chondroitin sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K03419  N-acetylgalactosaminyl-proteoglycan
                        3-beta-glucuronosyltransferase
GENES       HSA: 22856(CHSY1) 337876(CHSY-2) 54480(CSGlcA-T) 79586(CHPF)
            PTR: 467777(CHSY1)
            MMU: 269941(Chsy1) 74241(D1Bwg1363e) 78923(4833446K15Rik)
            RNO: 291577(RGD1560819_predicted) 292999(Chsy1_predicted)
                 316533(D1bwg1363e)
            CFA: 481492(LOC481492) 482807(LOC482807) 488538(LOC488538)
                 488704(CHSY1)
            BTA: 528149(LOC528149) 540002(LOC540002)
            GGA: 415521(CHSY1) 415598(CHSY-2) 769112(LOC769112)
            DRE: 324407(chys1) 565504(LOC565504)
            SPU: 578984(LOC578984)
            DME: Dmel_CG4351
            CEL: PAR2.4(mig-22)
            PMU: PM0775
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.226
            ExPASy - ENZYME nomenclature database: 2.4.1.226
            ExplorEnz - The Enzyme Database: 2.4.1.226
            ERGO genome analysis and discovery system: 2.4.1.226
            BRENDA, the Enzyme Database: 2.4.1.226
            CAS: 269077-98-7
///
ENTRY       EC 2.4.1.227                Enzyme
NAME        undecaprenyldiphospho-muramoylpentapeptide
            beta-N-acetylglucosaminyltransferase;
            MurG transferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:N-acetyl-alpha-D-muramyl(oyl-L-Ala-gamma-
            D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
            beta-1,4-N-acetylglucosaminlytransferase
REACTION    UDP-N-acetylglucosamine +
            Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
            diphosphoundecaprenol = UDP +
            GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
            diphosphoundecaprenol [RN:R05662 R06173]
ALL_REAC    R05662 R06173(G);
            (other) R05027 R05032 R06172(G) R06174(G)
SUBSTRATE   UDP-N-acetylglucosamine [CPD:C00043];
            Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
            diphosphoundecaprenol
PRODUCT     UDP [CPD:C00015];
            GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
            diphosphoundecaprenol
COMMENT     The enzyme also works when the lysine residue is replaced by
            meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm)
            combined with adjacent residues through its L-centre, as it is in
            Gram-negative and some Gram-positive organisms. The undecaprenol
            involved is ditrans,octacis-undecaprenol (for definitions, click
            here).
REFERENCE   1  [PMID:11699883]
  AUTHORS   van Heijenoort J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit.
  JOURNAL   Nat. Prod. Rep. 18 (2001) 503-19.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00550  Peptidoglycan biosynthesis
ORTHOLOGY   KO: K02563  UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide)
                        pyrophosphoryl-undecaprenol N-acetylglucosamine
                        transferase
            KO: K05949  
GENES       ATH: AT1G73740
            OSA: 4323966
            ECO: b0090(murG)
            ECJ: JW0088(murG)
            ECE: Z0100(murG)
            ECS: ECs0094
            ECC: c0108(murG)
            ECI: UTI89_C0099(murG)
            ECV: APECO1_1896(murG)
            ECW: EcE24377A_0092(murG)
            ECX: EcHS_A0096
            STY: STY0148(murG)
            STT: t0132(murG)
            SPT: SPA0130(murG)
            SEC: SC0125(murG)
            STM: STM0128(murG)
            YPE: YPO0555(murG)
            YPK: y3626(murG)
            YPM: YP_3629(murG)
            YPA: YPA_3546
            YPN: YPN_0421
            YPP: YPDSF_3087
            YPS: YPTB0688(murG)
            YPI: YpsIP31758_3387(murG)
            YEN: YE0672(murG)
            SFL: SF0087(murG)
            SFX: S0089(murG)
            SFV: SFV_0083(murG)
            SSN: SSON_0098(murG)
            SBO: SBO_0078(murG)
            SDY: SDY_0120(murG)
            ECA: ECA3815(murG)
            PLU: plu3654(murG)
            BUC: BU216(murG)
            BAS: BUsg210(murG)
            BAB: bbp198(murG)
            WBR: WGLp206(murG)
            SGL: SG0449
            ENT: Ent638_0636
            SPE: Spro_0761
            BFL: Bfl142(murG)
            BPN: BPEN_146(murG)
            HIN: HI1138(murG)
            HIT: NTHI1305(murG)
            HIP: CGSHiEE_06365(murG)
            HIQ: CGSHiGG_09350(murG)
            HDU: HD0824(murG)
            HSO: HS_0358(murG)
            PMU: PM0142(murG)
            MSU: MS1667(murG)
            APL: APL_0018(murG)
            ASU: Asuc_1932
            XFA: XF0797
            XFT: PD1866(murG)
            XCC: XCC0725(murG)
            XCB: XC_3510
            XCV: XCV0830(murG)
            XAC: XAC0779(murG)
            XOO: XOO3826(murG)
            XOM: XOO_3604(XOO3604)
            VCH: VC2401
            VVU: VV1_0578
            VVY: VV0614
            VPA: VP0460
            VFI: VF2201
            PPR: PBPRA3215
            PAE: PA4412(murG)
            PAU: PA14_57340(murG)
            PAP: PSPA7_4984(murG)
            PPU: PP_1337(murG)
            PPF: Pput_4387
            PST: PSPTO_4408(murG)
            PSB: Psyr_4102(murG)
            PSP: PSPPH_4108(murG)
            PFL: PFL_5061(murG)
            PFO: Pfl_4673(murG)
            PEN: PSEEN4485(murG)
            PMY: Pmen_0922
            PAR: Psyc_1751(murG)
            PCR: Pcryo_2032
            PRW: PsycPRwf_0524
            ACI: ACIAD3517(murG)
            SON: SO_4219(murG)
            SDN: Sden_0355
            SFR: Sfri_3804
            SAZ: Sama_0354
            SBL: Sbal_0402
            SBM: Shew185_0401
            SLO: Shew_3453
            SPC: Sputcn32_0487
            SSE: Ssed_0410
            SPL: Spea_3811
            SHE: Shewmr4_3570
            SHM: Shewmr7_0386
            SHN: Shewana3_3743
            SHW: Sputw3181_0390
            ILO: IL0436(murG)
            CPS: CPS_4465(murG)
            PHA: PSHAa2504(murG)
            PAT: Patl_3519
            SDE: Sde_0848
            PIN: Ping_1147
            MAQ: Maqu_2452
            CBU: CBU_0135(murG)
            CBD: COXBU7E912_1972(murG)
            LPN: lpg0808(murG)
            LPF: lpl0841(murG)
            LPP: lpp0870(murG)
            MCA: MCA2429(murG)
            FTU: FTT0811c(murG)
            FTF: FTF0811c(murG)
            FTW: FTW_0608(murG)
            FTL: FTL_1410
            FTH: FTH_1373(murG)
            FTA: FTA_1498(murG)
            FTN: FTN_1195(murG)
            TCX: Tcr_0568
            NOC: Noc_2861(murG)
            AEH: Mlg_2193
            HHA: Hhal_2091
            HCH: HCH_05883(murG)
            CSA: Csal_2190
            ABO: ABO_0598(murG)
            MMW: Mmwyl1_2614
            AHA: AHA_3884(murG)
            BCI: BCI_0519(murG)
            RMA: Rmag_0500
            VOK: COSY_0460(murG)
            NME: NMB0422
            NMA: NMA2062(murG)
            NGO: NGO1533(murG)
            CVI: CV_4343(murG)
            RSO: RSc2844(murG)
            REU: Reut_A2979(murG)
            REH: H16_A3273(murG)
            RME: Rmet_3128
            BMA: BMA2551(murG)
            BXE: Bxe_A0486
            BVI: Bcep1808_0535
            BUR: Bcep18194_A3645(murG) Bcep18194_B0550
            BCN: Bcen_0077
            BCH: Bcen2424_0559
            BAM: Bamb_0463
            BPS: BPSL3025(murG)
            BPM: BURPS1710b_3545(murG)
            BPL: BURPS1106A_3550(murG)
            BPD: BURPS668_3525(murG)
            BTE: BTH_I1118(murG)
            PNU: Pnuc_0167
            BPE: BP3023(murG)
            BPA: BPP3752(murG)
            BBR: BB4198(murG)
            RFR: Rfer_3425
            POL: Bpro_1075
            PNA: Pnap_3417
            AAV: Aave_0821
            AJS: Ajs_3670
            VEI: Veis_4570
            MPT: Mpe_A0462
            HAR: HEAR2811(murG)
            MMS: mma_3015
            NEU: NE0991(murG)
            NET: Neut_0246
            NMU: Nmul_A2494
            EBA: ebA1444(murG)
            AZO: azo0884(murG)
            DAR: Daro_3498(murG)
            TBD: Tbd_0119(murG)
            MFA: Mfla_2269
            HPY: HP1155(murG)
            HPJ: jhp1082(murG)
            HPA: HPAG1_1094
            HHE: HH0927(murG)
            HAC: Hac_1322(murG)
            WSU: WS0323(murG)
            TDN: Tmden_1807
            CJE: Cj1039(murG)
            CJR: CJE1183(murG)
            CJU: C8J_0976(murG)
            CFF: CFF8240_0845(murG)
            CCV: CCV52592_1988(murG)
            CHA: CHAB381_1048
            CCO: CCC13826_0577 CCC13826_1242(murG)
            ABU: Abu_1909(murG)
            NIS: NIS_1531(murG)
            SUN: SUN_0321(murG)
            GSU: GSU3069(murG)
            GME: Gmet_0412
            GUR: Gura_3974
            PCA: Pcar_2202
            PPD: Ppro_3289
            DVU: DVU2504(murG)
            DVL: Dvul_0741
            DDE: Dde_1042
            LIP: LI1104(murG)
            BBA: Bd3197(murG)
            DPS: DP2898(murG)
            ADE: Adeh_3771
            AFW: Anae109_3884
            MXA: MXAN_5604(murG)
            SAT: SYN_01746
            SFU: Sfum_2756
            RPR: RP412(murG)
            RTY: RT0398(murG)
            RCO: RC0562(murG)
            RFE: RF_0636(murG)
            RBE: RBE_0878(murG)
            RAK: A1C_03060(murG)
            RBO: A1I_02500(murG)
            RRI: A1G_03170(murG)
            OTS: OTBS_1530(murG)
            WOL: WD0323(murG)
            WBM: Wbm0557
            AMA: AM471(murG)
            PUB: SAR11_0024(murG)
            MLO: mll1554
            MES: Meso_2007
            PLA: Plav_2421
            SME: SMc01866(murG)
            SMD: Smed_2082
            ATU: Atu2094(murG)
            ATC: AGR_C_3798
            RET: RHE_CH02847(murG)
            RLE: RL3307(murG)
            BME: BMEI0579
            BMF: BAB1_1450(murG)
            BMS: BR1431(murG)
            BMB: BruAb1_1426(murG)
            BOV: BOV_1388(murG)
            OAN: Oant_1744
            BJA: bll6602(murG)
            BRA: BRADO5659(murG)
            BBT: BBta_6174(murG)
            RPA: RPA3530(murG)
            RPB: RPB_1994
            RPC: RPC_3306
            RPD: RPD_3394
            RPE: RPE_2107
            NWI: Nwi_1051(murG)
            NHA: Nham_1279
            BHE: BH11240(murG)
            BQU: BQ08860(murG)
            BBK: BARBAKC583_0947(murG)
            XAU: Xaut_1191
            CCR: CC_2551
            SIL: SPO1195
            SIT: TM1040_0682
            RSP: RSP_2107(murG)
            RSH: Rsph17029_0783
            RSQ: Rsph17025_0693
            JAN: Jann_2760
            RDE: RD1_3357
            PDE: Pden_4495
            MMR: Mmar10_2078
            HNE: HNE_3024(murG)
            ZMO: ZMO0831(murG)
            NAR: Saro_1133
            SAL: Sala_1881
            SWI: Swit_3947
            ELI: ELI_01795
            GOX: GOX0158
            GBE: GbCGDNIH1_0429
            ACR: Acry_0063
            RRU: Rru_A0950
            MAG: amb3848
            MGM: Mmc1_0753
            ABA: Acid345_3629
            SUS: Acid_7311
            BSU: BG10227(murG)
            BHA: BH2565(murG)
            BAN: BA4049(murG-1) BA4477(murG-2)
            BAR: GBAA4049(murG-1) GBAA4477(murG-2)
            BAA: BA_4519 BA_4924
            BAT: BAS3761 BAS4155
            BCE: BC3748 BC3910 BC4249
            BCA: BCE_3956(murG) BCE_4331(murG)
            BCZ: BCZK3669(murG) BCZK4004(murG)
            BCY: Bcer98_2560
            BTK: BT9727_3652(murG) BT9727_3994(murG)
            BTL: BALH_3379(murG) BALH_3849(murG)
            BLI: BL02243(murG)
            BLD: BLi01739(murG)
            BCL: ABC0086(murG)
            BAY: RBAM_015080
            BPU: BPUM_1415
            OIH: OB1093(murG)
            GKA: GK0219
            SAU: SA1251(murG)
            SAV: SAV1418(murG)
            SAM: MW1307(murG)
            SAR: SAR1430(murG)
            SAS: SAS1360
            SAC: SACOL1453(murG)
            SAB: SAB1273c(murG)
            SAA: SAUSA300_1311(murG)
            SAO: SAOUHSC_01424
            SAJ: SaurJH9_1478
            SAH: SaurJH1_1507
            SEP: SE1110
            SER: SERP0993(murG)
            SHA: SH1488(murG)
            SSP: SSP1321
            LMO: lmo2035(murG)
            LMF: LMOf2365_2067(murG)
            LIN: lin2141(murG)
            LWE: lwe2049(murG)
            LLA: L0238(murG)
            LLC: LACR_1696
            LLM: llmg_0913(murG)
            SPY: SPy_1524(murG)
            SPZ: M5005_Spy_1252(murG)
            SPM: spyM18_1541(murG)
            SPG: SpyM3_1175(murG)
            SPS: SPs0687
            SPH: MGAS10270_Spy1268(murG)
            SPI: MGAS10750_Spy1360(murG)
            SPJ: MGAS2096_Spy1271(murG)
            SPK: MGAS9429_Spy1247(murG)
            SPF: SpyM50600(murG)
            SPA: M6_Spy1273
            SPB: M28_Spy1191(murG)
            SPN: SP_0689
            SPR: spr0604(murG)
            SPD: SPD_0599(murG)
            SAG: SAG0476(murG)
            SAN: gbs0523
            SAK: SAK_0578(murG)
            SMU: SMU.549(murG)
            STC: str0732(murG)
            STL: stu0732(murG)
            SSA: SSA_0653(murG)
            SGO: SGO_0672(murG)
            LPL: lp_2196(murG)
            LJO: LJ0972
            LAC: LBA0809(murG)
            LSA: LSA0748(murG)
            LSL: LSL_1050(murG)
            LDB: Ldb0741(murG)
            LBU: LBUL_0674
            LBR: LVIS_1449
            LCA: LSEI_1272
            LRE: Lreu_0590
            EFA: EF0994(murG)
            OOE: OEOE_1146
            STH: STH1210
            CAC: CAC2231(murG)
            CPE: CPE2063(murG)
            CPF: CPF_2320(murG)
            CPR: CPR_2034(murG)
            CTC: CTC01743
            CNO: NT01CX_2311(murG)
            CDF: CD2651(murG)
            CBO: CBO2761(murG)
            CBA: CLB_2702(murG)
            CBH: CLC_2635(murG)
            CBF: CLI_2811(murG)
            CBE: Cbei_4320
            CKL: CKL_2139(murG1) CKL_3719(murG2)
            AMT: Amet_2879
            CHY: CHY_2069(murG)
            DSY: DSY2907
            DRM: Dred_0675
            SWO: Swol_0826
            TTE: TTE1645(murG)
            MTA: Moth_0843
            MTU: Rv2153c(murG)
            MTC: MT2212(murG)
            MBO: Mb2177c(murG)
            MLE: ML0914(murG)
            MPA: MAP1897c(murG)
            MAV: MAV_2336(murG)
            MSM: MSMEG_4227(murG)
            MVA: Mvan_3523
            MGI: Mflv_2988
            MMC: Mmcs_3256
            MKM: Mkms_3318
            MJL: Mjls_3267
            CGL: NCgl2078(murG)
            CGB: cg2369(murG)
            CEF: CE2053(murG)
            CDI: DIP1598(murG)
            CJK: jk0750(murG)
            NFA: nfa17660(murG)
            RHA: RHA1_ro01088(murG)
            SCO: SCO2084(murG)
            SMA: SAV6122(murG)
            TWH: TWT228(murG)
            TWS: TW542(murG)
            LXX: Lxx15260(murG)
            CMI: CMM_1859(murG)
            ART: Arth_1570
            AAU: AAur_1710(murG)
            PAC: PPA0758
            NCA: Noca_3063
            TFU: Tfu_1110(murG)
            FRA: Francci3_1415
            FAL: FRAAL2196(murG)
            ACE: Acel_1010
            KRA: Krad_3199
            SEN: SACE_5851(murG)
            STP: Strop_0238 Strop_3213
            BLO: BL1323(murG)
            BAD: BAD_1101(murG)
            RXY: Rxyl_1493
            CTR: CT761(murG)
            CTA: CTA_0831(murG)
            CMU: TC0142
            CPN: CPn0904(murG)
            CPA: CP0962
            CPJ: CPj0904(murG)
            CPT: CpB0936
            CCA: CCA00864(murG)
            CAB: CAB830
            CFE: CF0152(murG)
            PCU: pc1248(murG)
            BBU: BB0767(murG)
            BGA: BG0790(murG)
            BAF: BAPKO_0815(murG)
            TPA: TP0523
            TDE: TDE1974(murG)
            LIL: LA2050(murG)
            LIC: LIC11864(murG)
            LBJ: LBJ_0476(murG)
            LBL: LBL_2603(murG)
            SYN: slr1656(murG)
            SYW: SYNW2333(murG)
            SYC: syc1790_c(murG)
            SYF: Synpcc7942_2312
            SYD: Syncc9605_2463
            SYE: Syncc9902_2147
            SYG: sync_2714(murG)
            SYR: SynRCC307_2225
            SYX: SynWH7803_2361
            CYA: CYA_0847(murG)
            CYB: CYB_2152(murG)
            TEL: tlr1809(murG)
            GVI: gll1671
            ANA: alr0477
            AVA: Ava_2890
            PMA: Pro0223(murG)
            PMM: PMM0197(murG)
            PMT: PMT2101(murG)
            PMN: PMN2A_1564(murG)
            PMI: PMT9312_0199
            PMB: A9601_02151(murG)
            PMC: P9515_02261(murG)
            PMF: P9303_27911(murG)
            PMG: P9301_02171(murG)
            PMH: P9215_02151
            PME: NATL1_02731(murG)
            TER: Tery_0207
            BTH: BT_3448
            BFR: BF0306
            BFS: BF0254(murG)
            PGI: PG0580(murG)
            SRU: SRU_0560(murG)
            CHU: CHU_2739(murG)
            GFO: GFO_2768(murG)
            FJO: Fjoh_1810
            FPS: FP2057(murG)
            CTE: CT0034(murG)
            CCH: Cag_0055(murG)
            CPH: Cpha266_2721
            PVI: Cvib_1753
            PLT: Plut_2110(murG)
            RRS: RoseRS_3786
            RCA: Rcas_1095
            DRA: DR_0626
            DGE: Dgeo_1630
            TTH: TTC0719
            TTJ: TTHA1084
            AAE: aq_1177(murG)
            TMA: TM0232
            TPT: Tpet_0692
            TME: Tmel_0891
            FNO: Fnod_1222
            MKA: MK0372(murG)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.227
            ExPASy - ENZYME nomenclature database: 2.4.1.227
            ExplorEnz - The Enzyme Database: 2.4.1.227
            ERGO genome analysis and discovery system: 2.4.1.227
            BRENDA, the Enzyme Database: 2.4.1.227
            CAS: 60976-26-3
///
ENTRY       EC 2.4.1.228                Enzyme
NAME        lactosylceramide 4-alpha-galactosyltransferase;
            Galbeta1-4Glcbeta1-Cer alpha1,4-galactosyltransferase;
            globotriaosylceramide/CD77 synthase;
            histo-blood group Pk UDP-galactose
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:lactosylceramide 4II-alpha-D-galactosyltransferase
REACTION    UDP-galactose + beta-D-galactosyl-(1->4)-D-glucosylceramide = UDP +
            alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-D-
            glucosylceramide [RN:R03486 R05960]
ALL_REAC    R03486 R05960(G)
SUBSTRATE   UDP-galactose [CPD:C00052];
            beta-D-galactosyl-(1->4)-D-glucosylceramide
PRODUCT     UDP [CPD:C00015];
            alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-D-
            glucosylceramide
COMMENT     For explanation of superscript II in systematic name, see 2-carb.37.
REFERENCE   1  [PMID:3099784]
  AUTHORS   Bailly P, Piller F, Cartron JP, Leroy Y, Fournet B.
  TITLE     Identification of UDP-galactose: lactose (lactosylceramide) alpha-4
            and beta-3 galactosyltransferases in human kidney.
  JOURNAL   Biochem. Biophys. Res. Commun. 141 (1986) 84-91.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:10747952]
  AUTHORS   Steffensen R, Carlier K, Wiels J, Levery SB, Stroud M, Cedergren B,
            Nilsson Sojka B, Bennett EP, Jersild C, Clausen H.
  TITLE     Cloning and expression of the histo-blood group Pk UDP-galactose:
            Ga1beta-4G1cbeta1-cer alpha1, 4-galactosyltransferase. Molecular
            genetic basis of the p phenotype.
  JOURNAL   J. Biol. Chem. 275 (2000) 16723-9.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:10748143]
  AUTHORS   Kojima Y, Fukumoto S, Furukawa K, Okajima T, Wiels J, Yokoyama K,
            Suzuki Y, Urano T, Ohta M, Furukawa K.
  TITLE     Molecular cloning of globotriaosylceramide/CD77 synthase, a
            glycosyltransferase that initiates the synthesis of globo series
            glycosphingolipids.
  JOURNAL   J. Biol. Chem. 275 (2000) 15152-6.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00603  Glycosphingolipid biosynthesis - globoseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K01988  lactosylceramide 4-alpha-galactosyltransferase
GENES       HSA: 53947(A4GALT)
            PTR: 470230(A4GALT)
            MMU: 239559(A4galt)
            RNO: 63888(A4galt)
            CFA: 481222(A4GALT)
            GGA: 418223(A4GALT)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.228
            ExPASy - ENZYME nomenclature database: 2.4.1.228
            ExplorEnz - The Enzyme Database: 2.4.1.228
            ERGO genome analysis and discovery system: 2.4.1.228
            BRENDA, the Enzyme Database: 2.4.1.228
            CAS: 52725-57-2
///
ENTRY       EC 2.4.1.229                Enzyme
NAME        [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase;
            Skp1-HyPro GlcNAc-transferase;
            UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide
            GlcNAc-transferase;
            UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase;
            UDP-GlcNAc:hydroxyproline polypeptide GlcNAc-transferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-glucosamine:[Skp1-protein]-hydroxyproline
            N-acetyl-D-glucosaminyl-transferase
REACTION    UDP-N-acetylglucosamine + [Skp1-protein]-hydroxyproline = UDP +
            [Skp1-protein]-O-(N-acetyl-D-glucosaminyl)hydroxyproline
SUBSTRATE   UDP-N-acetylglucosamine [CPD:C00043];
            [Skp1-protein]-hydroxyproline
PRODUCT     UDP [CPD:C00015];
            [Skp1-protein]-O-(N-acetyl-D-glucosaminyl)hydroxyproline
COMMENT     Requires dithiothreitol and a divalent cation for activity. This
            enzyme commences the building up of a pentasaccharide
            (Galalpha1-6Galalpha1-L-Fucalpha1-2Galbeta1-3GlcNAc) on Hyp-143 of
            the Dictyostelium protein Skp1, which is required for the
            ubiquitination of cell-cycle regulatory proteins and transcription
            factors. The fucose residue is probably in the alpha configuration
            [3]. The specificity of the enzyme for Skp1-Hyp-143 and its high
            affinity for this substrate suggests that it is the
            GlcNAc-transferase that modifies Skp1 in vivo.
REFERENCE   1  [PMID:12244115]
  AUTHORS   Van Der Wel H, Morris HR, Panico M, Paxton T, Dell A, Kaplan L, West
            CM.
  TITLE     Molecular cloning and expression of a UDP-N-acetylglucosamine
            (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase that modifies
            Skp1 in the cytoplasm of dictyostelium.
  JOURNAL   J. Biol. Chem. 277 (2002) 46328-37.
  ORGANISM  Dictyostelium discoideum [GN:ddi]
REFERENCE   2  [PMID:10593934]
  AUTHORS   Teng-Umnuay P, van der Wel H, West CM.
  TITLE     Identification of a UDP-GlcNAc:Skp1-hydroxyproline
            GlcNAc-transferase in the cytoplasm of Dictyostelium.
  JOURNAL   J. Biol. Chem. 274 (1999) 36392-402.
  ORGANISM  Dictyostelium discoideum [GN:ddi]
REFERENCE   3  [PMID:11886837]
  AUTHORS   West CM, van der Wel H, Gaucher EA.
  TITLE     Complex glycosylation of Skp1 in Dictyostelium: implications for the
            modification of other eukaryotic cytoplasmic and nuclear proteins.
  JOURNAL   Glycobiology. 12 (2002) 17R-27R.
  ORGANISM  Dictyostelium sp.
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.229
            ExPASy - ENZYME nomenclature database: 2.4.1.229
            ExplorEnz - The Enzyme Database: 2.4.1.229
            ERGO genome analysis and discovery system: 2.4.1.229
            BRENDA, the Enzyme Database: 2.4.1.229
///
ENTRY       EC 2.4.1.230                Enzyme
NAME        kojibiose phosphorylase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     2-alpha-D-glucosyl-D-glucose:phosphate beta-D-glucosyltransferase
REACTION    2-alpha-D-glucosyl-D-glucose + phosphate = D-glucose +
            beta-D-glucose 1-phosphate [RN:R07264]
ALL_REAC    R07264
SUBSTRATE   2-alpha-D-glucosyl-D-glucose [CPD:C15548];
            phosphate [CPD:C00009]
PRODUCT     D-glucose [CPD:C00031];
            beta-D-glucose 1-phosphate [CPD:C00663]
COMMENT     The enzyme from Thermoanaerobacter brockii can act with
            alpha-1,2-oligoglucans, such as selaginose, as substrate, but more
            slowly. The enzyme is inactive when dissaccharides with linkages
            other than alpha-1,2 linkages, such as sophorose, trehalose,
            neotrehalose, nigerose, laminaribiose, maltose, cellobiose,
            isomaltose, gentiobiose, sucrose and lactose, are used as
            substrates.
REFERENCE   1
  AUTHORS   Chaen, H., Yamamoto, T., Nishimoto, T., Nakada, T., Fukuda, S.,
            Sugimoto, T., Kurimoto, M. and Tsujisaka, Y.
  TITLE     Purification and characterization of a novel phosphorylase,
            kojibiose phosphorylase, from Thermoanaerobium brockii.
  JOURNAL   J. Appl. Glycosci. 46 (1999) 423-429.
  ORGANISM  Thermoanaerobium brockii
REFERENCE   2  [PMID:16233080]
  AUTHORS   Chaen H, Nishimoto T, Nakada T, Fukuda S, Kurimoto M, Tsujisaka Y.
  TITLE     Enzymatic synthesis of kojioligosaccharides using kojibiose
            phosphorylase.
  JOURNAL   J. Biosci. Bioeng. 92 (2001) 177-82.
  ORGANISM  Thermoanaerobacter brockii
ORTHOLOGY   KO: K10231  kojibiose phosphorylase
GENES       ENT: Ent638_2158
            LRE: Lreu_0054
            CSC: Csac_0439 Csac_0444
            TTE: TTE0798(ath1)
            MVA: Mvan_5750
            MGI: Mflv_1073
            MMC: Mmcs_1171
            MKM: Mkms_1188
            MJL: Mjls_1198
            ART: Arth_0308
            NCA: Noca_3421
            FRA: Francci3_4347
            KRA: Krad_1472 Krad_3033
            SEN: SACE_3173
            STP: Strop_0438
            AVA: Ava_2279 Ava_3752
            FJO: Fjoh_1401
            CPH: Cpha266_1194
            PVI: Cvib_1015
            PLT: Plut_1264
            TPE: Tpen_1155
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.230
            ExPASy - ENZYME nomenclature database: 2.4.1.230
            ExplorEnz - The Enzyme Database: 2.4.1.230
            ERGO genome analysis and discovery system: 2.4.1.230
            BRENDA, the Enzyme Database: 2.4.1.230
///
ENTRY       EC 2.4.1.231                Enzyme
NAME        alpha,alpha-trehalose phosphorylase (configuration-retaining);
            trehalose phosphorylase[ambiguous]
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     alpha,alpha-trehalose:phosphate alpha-D-glucosyltransferase
REACTION    alpha,alpha-trehalose + phosphate = alpha-D-glucose +
            alpha-D-glucose 1-phosphate [RN:R07265]
ALL_REAC    R07265
SUBSTRATE   alpha,alpha-trehalose [CPD:C01083];
            phosphate [CPD:C00009]
PRODUCT     alpha-D-glucose [CPD:C00267];
            alpha-D-glucose 1-phosphate [CPD:C00103]
COMMENT     Unlike EC 2.4.1.64, alpha,alpha-trehalose phosphorylase, this enzyme
            retains its anomeric configuration. Vanadate is a strong competitive
            inhibitor of this reversible reaction.
REFERENCE   1  [PMID:11931662]
  AUTHORS   Eis C, Nidetzky B.
  TITLE     Substrate-binding recognition and specificity of trehalose
            phosphorylase from Schizophyllum commune examined in steady-state
            kinetic studies with deoxy and deoxyfluoro substrate analogues and
            inhibitors.
  JOURNAL   Biochem. J. 363 (2002) 335-40.
  ORGANISM  Schizophyllum commune
REFERENCE   2  [PMID:11389683]
  AUTHORS   Eis C, Watkins M, Prohaska T, Nidetzky B.
  TITLE     Fungal trehalose phosphorylase: kinetic mechanism, pH-dependence of
            the reaction and some structural properties of the enzyme from
            Schizophyllum commune.
  JOURNAL   Biochem. J. 356 (2001) 757-67.
  ORGANISM  Schizophyllum commune
REFERENCE   3  [PMID:11736665]
  AUTHORS   Nidetzky B, Eis C.
  TITLE     Alpha-retaining glucosyl transfer catalysed by trehalose
            phosphorylase from Schizophyllum commune: mechanistic evidence
            obtained from steady-state kinetic studies with substrate analogues
            and inhibitors.
  JOURNAL   Biochem. J. 360 (2001) 727-36.
  ORGANISM  Schizophyllum commune
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.231
            ExPASy - ENZYME nomenclature database: 2.4.1.231
            ExplorEnz - The Enzyme Database: 2.4.1.231
            ERGO genome analysis and discovery system: 2.4.1.231
            BRENDA, the Enzyme Database: 2.4.1.231
///
ENTRY       EC 2.4.1.232                Enzyme
NAME        initiation-specific alpha-1,6-mannosyltransferase;
            alpha-1,6-mannosyltransferase;
            GDP-mannose:oligosaccharide 1,6-alpha-D-mannosyltransferase;
            GDP-mannose:glycolipid 1,6-alpha-D-mannosyltransferase;
            glycolipid 6-alpha-mannosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     GDP-mannose:oligosaccharide 1,6-alpha-D-mannosyltransferase
REACTION    Transfers an alpha-D-mannosyl residue from GDP-mannose into
            lipid-linked oligosaccharide, forming an
            alpha-1,6-D-mannosyl-D-mannose linkage
ALL_REAC    (other) R06986(G)
COMMENT     Requires Mn2+. In Saccharomyces cerevisiae, this enzyme catalyses an
            essential step in the outer chain elongation of N-linked
            oligosaccharides. Man8GlcNAc and Man9GlcNAc are equally good
            substrates.
REFERENCE   1  [PMID:2644248]
  AUTHORS   Romero PA, Herscovics A.
  TITLE     Glycoprotein biosynthesis in Saccharomyces cerevisiae.
            Characterization of alpha-1,6-mannosyltransferase which initiates
            outer chain formation.
  JOURNAL   J. Biol. Chem. 264 (1989) 1946-50.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:1820199]
  AUTHORS   Reason AJ, Dell A, Romero PA, Herscovics A.
  TITLE     Specificity of the mannosyltransferase which initiates outer chain
            formation in Saccharomyces cerevisiae.
  JOURNAL   Glycobiology. 1 (1991) 387-91.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:8253757]
  AUTHORS   Nakanishi-Shindo Y, Nakayama K, Tanaka A, Toda Y, Jigami Y.
  TITLE     Structure of the N-linked oligosaccharides that show the complete
            loss of alpha-1,6-polymannose outer chain from och1, och1 mnn1, and
            och1 mnn1 alg3 mutants of Saccharomyces cerevisiae.
  JOURNAL   J. Biol. Chem. 268 (1993) 26338-45.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4  [PMID:12784644]
  AUTHORS   Yamamoto K, Okamoto M, Yoko-o T, Jigami Y.
  TITLE     Salt stress induces the expression of Schizosaccharomyces pombe
            och1+, which encodes an initiation-specific
            alpha-1,6-mannosyltransferase for N-linked outer chain synthesis of
            cell wall mannoproteins.
  JOURNAL   Biosci. Biotechnol. Biochem. 67 (2003) 927-9.
  ORGANISM  Schizosaccharomyces pombe [GN:spo]
REFERENCE   5  [PMID:11754484]
  AUTHORS   Cui Z, Horecka J, Jigami Y.
  TITLE     Cdc4 is involved in the transcriptional control of OCH1, a gene
            encoding alpha-1,6-mannosyltransferase in Saccharomyces cerevisiae.
  JOURNAL   Yeast. 19 (2002) 69-77.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   6
  AUTHORS   Tsukahara, K., Watanabe, T., Yoko-o, T. and Chigami, Y.
  TITLE     Schizosaccharomyces pombe och1+ gene encoding
            alpha-1,6-mannosyltransferase and use of och1+ gene knockout fission
            yeast for production of glycoproteins with reduced glycosylation.
  JOURNAL   Jpn. Kokai Tokkyo Koho Koho (2001) 11.
REFERENCE   7  [PMID:9276464]
  AUTHORS   Nakayama K, Nakanishi-Shindo Y, Tanaka A, Haga-Toda Y, Jigami Y.
  TITLE     Substrate specificity of alpha-1,6-mannosyltransferase that
            initiates N-linked mannose outer chain elongation in Saccharomyces
            cerevisiae.
  JOURNAL   FEBS. Lett. 412 (1997) 547-50.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   8  [PMID:8797833]
  AUTHORS   Suzuki A, Shibata N, Suzuki M, Saitoh F, Takata Y, Oshie A, Oyamada
            H, Kobayashi H, Suzuki S, Okawa Y.
  TITLE     Characterization of alpha-1,6-mannosyltransferase responsible for
            the synthesis of branched side chains in Candida albicans mannan.
  JOURNAL   Eur. J. Biochem. 240 (1996) 37-44.
  ORGANISM  Candida albicans [GN:cal]
REFERENCE   9  [PMID:8146181]
  AUTHORS   Yip CL, Welch SK, Klebl F, Gilbert T, Seidel P, Grant FJ, O'Hara PJ,
            MacKay VL.
  TITLE     Cloning and analysis of the Saccharomyces cerevisiae MNN9 and MNN1
            genes required for complex glycosylation of secreted proteins.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 2723-7.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00513  High-mannose type N-glycan biosynthesis
ORTHOLOGY   KO: K05528  alpha 1,6-mannosyltransferase
GENES       SCE: YGL038C(OCH1)
            AGO: AGOS_AFR465C
            PIC: PICST_76016(OCH1)
            CAL: CaO19_7391(CaO19.7391)
            CGR: CAGL0A01738g
            ANI: AN4716.2
            AFM: AFUA_5G08580
            AOR: AO090120000208
            CNE: CNF01430
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.232
            ExPASy - ENZYME nomenclature database: 2.4.1.232
            ExplorEnz - The Enzyme Database: 2.4.1.232
            ERGO genome analysis and discovery system: 2.4.1.232
            BRENDA, the Enzyme Database: 2.4.1.232
            CAS: 346003-17-6
///
ENTRY       EC 2.4.1.233      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: anthocyanidin 3-O-glucosyltransferase. The enzyme is
            identical to EC 2.4.1.115, anthocyanidin 3-O-glucosyltransferase (EC
            2.4.1.233 created 2004, deleted 2005)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.233
            ExPASy - ENZYME nomenclature database: 2.4.1.233
            ExplorEnz - The Enzyme Database: 2.4.1.233
            ERGO genome analysis and discovery system: 2.4.1.233
            BRENDA, the Enzyme Database: 2.4.1.233
///
ENTRY       EC 2.4.1.234                Enzyme
NAME        kaempferol 3-O-galactosyltransferase;
            F3GalTase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:kaempferol 3-O-beta-D-galactosyltransferase
REACTION    UDP-galactose + kaempferol = UDP + kaempferol 3-O-beta-D-galactoside
            [RN:R06808]
ALL_REAC    R06808
SUBSTRATE   UDP-galactose [CPD:C00052];
            kaempferol [CPD:C05903]
PRODUCT     UDP [CPD:C00015];
            kaempferol 3-O-beta-D-galactoside [CPD:C12626]
COMMENT     Acts on the endogenous flavonols kaempferol and quercetin, to a
            lesser extent on myricetin and fisetin, and weakly on galangin and
            isorhamnetin. The reaction can occur equally well in both
            directions.
REFERENCE   1  [PMID:10567367]
  AUTHORS   Miller KD, Guyon V, Evans JN, Shuttleworth WA, Taylor LP.
  TITLE     Purification, cloning, and heterologous expression of a
            catalytically efficient flavonol 3-O-galactosyltransferase expressed
            in the male gametophyte of Petunia hybrida.
  JOURNAL   J. Biol. Chem. 274 (1999) 34011-9.
  ORGANISM  Petunia hybrida
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.234
            ExPASy - ENZYME nomenclature database: 2.4.1.234
            ExplorEnz - The Enzyme Database: 2.4.1.234
            ERGO genome analysis and discovery system: 2.4.1.234
            BRENDA, the Enzyme Database: 2.4.1.234
///
ENTRY       EC 2.4.1.235      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
COMMENT     Deleted entry: Enzyme is identical to EC 2.4.1.116, cyanidin
            3-O-rutinoside 5-O-glucosyltransferase (EC 2.4.1.235 created 2004,
            deleted 2006)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.235
            ExPASy - ENZYME nomenclature database: 2.4.1.235
            ExplorEnz - The Enzyme Database: 2.4.1.235
            ERGO genome analysis and discovery system: 2.4.1.235
            BRENDA, the Enzyme Database: 2.4.1.235
///
ENTRY       EC 2.4.1.236                Enzyme
NAME        flavanone 7-O-glucoside 2"-O-beta-L-rhamnosyltransferase;
            UDP-rhamnose:flavanone-7-O-glucoside-2"-O-rhamnosyltransferase;
            1->2 UDP-rhamnosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-L-rhamnose:flavanone-7-O-glucoside
            2''-O-beta-L-rhamnosyltransferase
REACTION    UDP-L-rhamnose + a flavanone 7-O-glucoside = UDP + a flavanone
            7-O-[beta-L-rhamnosyl-(1->2)-beta-D-glucoside] [RN:R07337]
ALL_REAC    R07337 > R06820;
            (other) R06826 R06829
SUBSTRATE   UDP-L-rhamnose [CPD:C02199];
            flavanone 7-O-glucoside [CPD:C04007]
PRODUCT     UDP [CPD:C00015];
            flavanone 7-O-[beta-L-rhamnosyl-(1->2)-beta-D-glucoside]
            [CPD:C15579]
COMMENT     Acts on the 7-O-glucoside of naringenin and hesperetin, also the
            flavone 7-O-glucosides of luteolin and apigenin.
REFERENCE   1  [PMID:1939145]
  AUTHORS   Bar-Peled M, Lewinsohn E, Fluhr R, Gressel J.
  TITLE     UDP-rhamnose:flavanone-7-O-glucoside-2''-O-rhamnosyltransferase.
            Purification and characterization of an enzyme catalyzing the
            production of bitter compounds in citrus.
  JOURNAL   J. Biol. Chem. 266 (1991) 20953-9.
  ORGANISM  Citrus paradisi, Citrus maxima
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.236
            ExPASy - ENZYME nomenclature database: 2.4.1.236
            ExplorEnz - The Enzyme Database: 2.4.1.236
            ERGO genome analysis and discovery system: 2.4.1.236
            BRENDA, the Enzyme Database: 2.4.1.236
///
ENTRY       EC 2.4.1.237                Enzyme
NAME        flavonol 7-O-beta-glucosyltransferase;
            UDP-glucose:flavonol 7-O-glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:flavonol 7-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + a flavonol = UDP + a flavonol 7-O-beta-D-glucoside
            [RN:R07338]
ALL_REAC    R07338 > R06810
SUBSTRATE   UDP-glucose [CPD:C00029];
            flavonol [CPD:C01495]
PRODUCT     UDP [CPD:C00015];
            flavonol 7-O-beta-D-glucoside [CPD:C15580]
COMMENT     Acts on the flavonols gossypetin (8-hydroxyquercetin) and to a
            lesser extent on quercetin, kaempferol and myricetin.
REFERENCE   1  [PMID:9167271]
  AUTHORS   Stich K, Halbwirth H, Wurst F, Forkmann G.
  TITLE     UDP-glucose: flavonol 7-O-glucosyltransferase activity in flower
            extracts of Chrysanthemum segetum.
  JOURNAL   Z. Naturforsch. [C]. 52 (1997) 153-8.
  ORGANISM  Chrysanthemum segetum
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.237
            ExPASy - ENZYME nomenclature database: 2.4.1.237
            ExplorEnz - The Enzyme Database: 2.4.1.237
            ERGO genome analysis and discovery system: 2.4.1.237
            BRENDA, the Enzyme Database: 2.4.1.237
            CAS: 83682-90-0
///
ENTRY       EC 2.4.1.238                Enzyme
NAME        anthocyanin 3'-O-beta-glucosyltransferase;
            UDP-glucose:anthocyanin 3'-O-glucosyltransferase;
            3'GT
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:anthocyanin 3'-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + an anthocyanin = UDP + an anthocyanin
            3'-O-beta-D-glucoside [RN:R07266]
ALL_REAC    R07266 > R07912 R07913 R07923
SUBSTRATE   UDP-glucose [CPD:C00029];
            anthocyanin [CPD:C15549]
PRODUCT     UDP [CPD:C00015];
            anthocyanin 3'-O-beta-D-glucoside [CPD:C15550]
COMMENT     This enzyme specifically glucosylates the 3'-hydroxy group of
            delphinidin 3,5-di-O-beta-D-glucoside to form delphinidin
            3,5,3'-tri-O-beta-D-glucoside in gentian (Gentiana triflora).
REFERENCE   1  [PMID:12857844]
  AUTHORS   Fukuchi-Mizutani M, Okuhara H, Fukui Y, Nakao M, Katsumoto Y,
            Yonekura-Sakakibara K, Kusumi T, Hase T, Tanaka Y.
  TITLE     Biochemical and molecular characterization of a novel
            UDP-glucose:anthocyanin 3'-O-glucosyltransferase, a key enzyme for
            blue anthocyanin biosynthesis, from gentian.
  JOURNAL   Plant. Physiol. 132 (2003) 1652-63.
  ORGANISM  Gentiana triflora
PATHWAY     PATH: map00942  Anthocyanin biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.238
            ExPASy - ENZYME nomenclature database: 2.4.1.238
            ExplorEnz - The Enzyme Database: 2.4.1.238
            ERGO genome analysis and discovery system: 2.4.1.238
            BRENDA, the Enzyme Database: 2.4.1.238
            CAS: 380231-41-4
///
ENTRY       EC 2.4.1.239                Enzyme
NAME        flavonol-3-O-glucoside glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:flavonol-3-O-glucoside 2''-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + a flavonol 3-O-beta-D-glucoside = UDP + a flavonol
            3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside [RN:R07339]
ALL_REAC    R07339 > R06804 R06812
SUBSTRATE   UDP-glucose [CPD:C00029];
            flavonol 3-O-beta-D-glucoside [CPD:C03946]
PRODUCT     UDP [CPD:C00015];
            flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside [CPD:C15581]
COMMENT     One of three specific glucosyltransferases in pea (Pisum sativum)
            that successively add a beta-D-glucosyl group first to O-3 of
            kaempferol, and then to O-2 of the previously added glucosyl group
            giving the 3-O-sophoroside and then the 3-O-sophorotrioside (see
            also EC 2.4.1.91, flavonol 3-O-glucosyltransferase and EC 2.4.1.240,
            flavonol-3-O-glycoside glucosyltransferase). TDP-glucose can replace
            UDP-glucose as the glucose donor but the reaction proceeds more
            slowly.
REFERENCE   1  [PMID:6462109]
  AUTHORS   Jourdan PS, Mansell RL.
  TITLE     Isolation and partial characterization of three glucosyl
            transferases involved in the biosynthesis of flavonol triglucosides
            in Pisum sativum L.
  JOURNAL   Arch. Biochem. Biophys. 213 (1982) 434-43.
  ORGANISM  Pisum sativum
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.239
            ExPASy - ENZYME nomenclature database: 2.4.1.239
            ExplorEnz - The Enzyme Database: 2.4.1.239
            ERGO genome analysis and discovery system: 2.4.1.239
            BRENDA, the Enzyme Database: 2.4.1.239
///
ENTRY       EC 2.4.1.240                Enzyme
NAME        flavonol-3-O-glycoside glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-glucose:flavonol-3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside
            2'''-O-beta-D-glucosyltransferase
REACTION    UDP-glucose + a flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside
            = UDP + a flavonol
            3-O-beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-beta-D-glucoside
            [RN:R07340]
ALL_REAC    R07340 > R06805 R06813
SUBSTRATE   UDP-glucose [CPD:C00029];
            flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside [CPD:C15581]
PRODUCT     UDP [CPD:C00015];
            flavonol
            3-O-beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-beta-D-glucoside
            [CPD:C15582]
COMMENT     One of three specific glucosyltransferases in pea (Pisum sativum)
            thatsuccessively add a beta-D-glucosyl group first to O-3 of
            kaempferol, and then to O-2 of the previously added glucosyl group
            giving the 3-O-sophoroside and then the 3-O-sophorotrioside (see
            also EC 2.4.1.91 flavonol 3-O-glucosyltransferase, and EC 2.4.1.239
            flavonol-3-O-glucoside glucosyltransferase).
REFERENCE   1  [PMID:6462109]
  AUTHORS   Jourdan PS, Mansell RL.
  TITLE     Isolation and partial characterization of three glucosyl
            transferases involved in the biosynthesis of flavonol triglucosides
            in Pisum sativum L.
  JOURNAL   Arch. Biochem. Biophys. 213 (1982) 434-43.
  ORGANISM  Pisum sativum
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.240
            ExPASy - ENZYME nomenclature database: 2.4.1.240
            ExplorEnz - The Enzyme Database: 2.4.1.240
            ERGO genome analysis and discovery system: 2.4.1.240
            BRENDA, the Enzyme Database: 2.4.1.240
///
ENTRY       EC 2.4.1.241                Enzyme
NAME        digalactosyldiacylglycerol synthase;
            DGD1;
            DGD2;
            DGDG synthase (ambiguous);
            UDP-galactose-dependent DGDG synthase;
            UDP-galactose-dependent digalactosyldiacylglycerol synthase;
            UDP-galactose:MGDG galactosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-galactose:3-(beta-D-galactosyl)-1,2-diacyl-sn-glycerol
            6-alpha-galactosyltransferase
REACTION    UDP-galactose + 3-(beta-D-galactosyl)-1,2-diacyl-sn-glycerol = UDP +
            3-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-1,2-diacyl-sn-
            glycerol [RN:R04469]
ALL_REAC    R04469
SUBSTRATE   UDP-galactose [CPD:C00052];
            3-(beta-D-galactosyl)-1,2-diacyl-sn-glycerol
PRODUCT     UDP [CPD:C00015];
            3-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-1,2-diacyl-sn-
            glycerol
COMMENT     Requires Mg2+. Diacylglycerol cannot serve as an acceptor molecule
            for galactosylation as in the reaction catalysed by EC 2.4.1.46,
            monogalactosyldiacylglyerol synthase. When phosphate is limiting,
            phospholipids in plant membranes are reduced but these are replaced,
            at least in part, by the glycolipids digalactosyldiacylglycerol
            (DGDG) and sulfoquinovosyldiacylglycerol [3]. While both DGD1 and
            DGD2 are increased under phosphate-limiting conditions, DGD2 does
            not contribute significantly under optimal growth conditions. DGD2
            is responsible for the synthesis of DGDG molecular species that are
            rich in C16 fatty acids at sn-1 of diacylglycerol whereas DGD1 leads
            to molecular species rich in C18 fatty acids [3]. The enzyme has
            been localized to the outer side of chloroplast envelope membranes.
REFERENCE   1  [PMID:11696551]
  AUTHORS   Kelly AA, Dormann P.
  TITLE     DGD2, an arabidopsis gene encoding a UDP-galactose-dependent
            digalactosyldiacylglycerol synthase is expressed during growth under
            phosphate-limiting conditions.
  JOURNAL   J. Biol. Chem. 277 (2002) 1166-73.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   2  [PMID:10973486]
  AUTHORS   Hartel H, Dormann P, Benning C.
  TITLE     DGD1-independent biosynthesis of extraplastidic galactolipids after
            phosphate deprivation in Arabidopsis.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 10649-54.
  ORGANISM  Arabidopsis sp.
REFERENCE   3  [PMID:14600212]
  AUTHORS   Kelly AA, Froehlich JE, Dormann P.
  TITLE     Disruption of the two digalactosyldiacylglycerol synthase genes DGD1
            and DGD2 in Arabidopsis reveals the existence of an additional
            enzyme of galactolipid synthesis.
  JOURNAL   Plant. Cell. 15 (2003) 2694-706.
  ORGANISM  Arabidopsis sp.
REFERENCE   4  [PMID:15590685]
  AUTHORS   Benning C, Ohta H.
  TITLE     Three enzyme systems for galactoglycerolipid biosynthesis are
            coordinately regulated in plants.
  JOURNAL   J. Biol. Chem. 280 (2005) 2397-400.
  ORGANISM  Arabidopsis sp.
PATHWAY     PATH: map00561  Glycerolipid metabolism
ORTHOLOGY   KO: K09480  digalactosyldiacylglycerol synthase
GENES       ATH: AT3G11670(DGD1) AT4G00550(DGD2)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.241
            ExPASy - ENZYME nomenclature database: 2.4.1.241
            ExplorEnz - The Enzyme Database: 2.4.1.241
            ERGO genome analysis and discovery system: 2.4.1.241
            BRENDA, the Enzyme Database: 2.4.1.241
///
ENTRY       EC 2.4.1.242                Enzyme
NAME        NDP-glucose---starch glucosyltransferase;
            granule-bound starch synthase;
            starch synthase II (ambiguous);
            waxy protein;
            starch granule-bound nucleoside diphosphate glucose-starch
            glucosyltransferase;
            granule-bound starch synthase I;
            GBSSI;
            granule-bound starch synthase II;
            GBSSII;
            GBSS;
            NDPglucose-starch glucosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     NDP-glucose:1,4-alpha-D-glucan 4-alpha-D-glucosyltransferase
REACTION    NDP-glucose + (1,4-alpha-D-glucosyl)n = NDP +
            (1,4-alpha-D-glucosyl)n+1 [RN:R07261]
ALL_REAC    R07261
SUBSTRATE   NDP-glucose [CPD:C15541];
            (1,4-alpha-D-glucosyl)n [CPD:C00718]
PRODUCT     NDP [CPD:C00454];
            (1,4-alpha-D-glucosyl)n+1 [CPD:C00718]
COMMENT     Unlike EC 2.4.1.11, glycogen(starch) synthase and EC 2.4.1.21,
            starch synthase, which use UDP-glucose and ADP-glucose,
            respectively, this enzyme can use either UDP- or ADP-glucose.
            Mutants that lack the Wx (waxy) allele cannot produce this enzyme,
            which plays an important role in the normal synthesis of amylose. In
            such mutants, only amylopectin is produced in the endosperm [3] or
            pollen [5].
REFERENCE   1  [PMID:4824506]
  AUTHORS   Tsai CY.
  TITLE     The function of the waxy locus in starch synthesis in maize
            endosperm.
  JOURNAL   Biochem. Genet. 11 (1974) 83-96.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   2  [PMID:9765530]
  AUTHORS   Nakamura T, Vrinten P, Hayakawa K, Ikeda J.
  TITLE     Characterization of a granule-bound starch synthase isoform found in
            the pericarp of wheat.
  JOURNAL   Plant. Physiol. 118 (1998) 451-9.
  ORGANISM  Triticum aestivum [GN:etae]
REFERENCE   3  [PMID:9951718]
  AUTHORS   Fujita N, Taira T.
  TITLE     A 56-kDa protein is a novel granule-bound starch synthase existing
            in the pericarps, aleurone layers, and embryos of immature seed in
            diploid wheat (Triticum monococcum L.).
  JOURNAL   Planta. 207 (1998) 125-32.
  ORGANISM  Triticum monococcum
REFERENCE   4  [PMID:10393240]
  AUTHORS   Murai J, Taira T, Ohta D.
  TITLE     Isolation and characterization of the three Waxy genes encoding the
            granule-bound starch synthase in hexaploid wheat.
  JOURNAL   Gene. 234 (1999) 71-9.
  ORGANISM  Triticum aestivum [GN:etae]
REFERENCE   5
  AUTHORS   Nelson, O.E.
  TITLE     The waxy locus in maize. II The location of the controlling element
            alleles.
  JOURNAL   Genetics 60 (1968) 507-524.
  ORGANISM  Zea mays [GN:ezma]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.242
            ExPASy - ENZYME nomenclature database: 2.4.1.242
            ExplorEnz - The Enzyme Database: 2.4.1.242
            ERGO genome analysis and discovery system: 2.4.1.242
            BRENDA, the Enzyme Database: 2.4.1.242
///
ENTRY       EC 2.4.1.243                Enzyme
NAME        6G-fructosyltransferase;
            fructan:fructan 6G-fructosyltransferase;
            1F(1-beta-D-fructofuranosyl)m
            sucrose:1F(1-beta-D-fructofuranosyl)nsucrose
            6G-fructosyltransferase;
            6G-FFT;
            6G-FT;
            6G-fructotransferase
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     1F-oligo[beta-D-fructofuranosyl-(2->1)-]sucrose
            6G-beta-D-fructotransferase
REACTION    [1-beta-D-fructofuranosyl-(2->1)-]m+1 alpha-D-glucopyranoside +
            [1-beta-D-fructofuranosyl-(2->1)-]n+1 alpha-D-glucopyranoside =
            [1-beta-D-fructofuranosyl-(2->1)-]m alpha-D-glucopyranoside +
            [1-beta-D-fructofuranosyl-(2->1)-]n+1
            beta-D-fructofuranosyl-(2->6)-alpha-D-glucopyranoside (m > 0; n >=
            0)
SUBSTRATE   [1-beta-D-fructofuranosyl-(2->1)-]m+1 alpha-D-glucopyranoside;
            [1-beta-D-fructofuranosyl-(2->1)-]n+1 alpha-D-glucopyranoside
PRODUCT     [1-beta-D-fructofuranosyl-(2->1)-]m alpha-D-glucopyranoside;
            [1-beta-D-fructofuranosyl-(2->1)-]n+1
            beta-D-fructofuranosyl-(2->6)-alpha-D-glucopyranoside (m > 0; n >=
            0)
COMMENT     This enzyme catalyses the transfer of the terminal (2->1)-linked
            beta-D-fructosyl group of a mono- or oligosaccharide substituent on
            O-1 of the fructose residue of sucrose onto O-6 of its glucose
            residue [1]. For example, if 1-kestose
            [1F-(beta-D-fructofuranosyl)sucrose] is both the donor and recipient
            in the reaction shown above, i.e., if m = 1 and n = 1, then the
            products will be sucrose and 6G-di-beta-D-fructofuranosylsucrose. In
            this notation, the superscripts F and G are used to specify whether
            the fructose or glucose residue of the sucrose carries the
            substituent. Alternatively, this may be indicated by the presence
            and/or absence of primes (see
            http://www.chem.qmul.ac.uk/iupac/2carb/36.html#362). Sucrose cannot
            be a donor substrate in the reaction (i.e. m cannot be zero) and
            inulin cannot act as an acceptor. Side reactions catalysed are
            transfer of a beta-D-fructosyl group between compounds of the
            structure
            1F-(1-beta-D-fructofuranosyl)m-6G-(1-beta-D-fructofuranosyl)n
            sucrose, where m >= 0 and n = 1 for the donor, and m >= 0 and n >= 0
            for the acceptor.
REFERENCE   1
  AUTHORS   Shiomi, N.
  TITLE     Purification and characterisation of 6G-fructosyltransferase from
            the roots of asparagus (Asparagus officinalis L.).
  JOURNAL   Carbohydr. Res. 96 (1981) 281-292.
  ORGANISM  Asparagus officinalis
REFERENCE   2
  AUTHORS   Shiomi, N.
  TITLE     Reverse reaction of fructosyl transfer catalysed by asparagus
            6G-fructosyltransferase.
  JOURNAL   Carbohydr. Res. 106 (1982) 166-169.
REFERENCE   3
  AUTHORS   Shiomi, N. and Ueno, K.
  TITLE     Cloning and expression of genes encoding fructosyltransferases from
            higher plants in food technology.
  JOURNAL   J. Appl. Glycosci. 51 (2004) 177-183.
  ORGANISM  Asparagus officinalis
REFERENCE   4  [PMID:15720693]
  AUTHORS   Ueno K, Onodera S, Kawakami A, Yoshida M, Shiomi N.
  TITLE     Molecular characterization and expression of a cDNA encoding
            fructan:fructan 6G-fructosyltransferase from asparagus (Asparagus
            officinalis).
  JOURNAL   New. Phytol. 165 (2005) 813-24.
  ORGANISM  Asparagus officinalis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.243
            ExPASy - ENZYME nomenclature database: 2.4.1.243
            ExplorEnz - The Enzyme Database: 2.4.1.243
            ERGO genome analysis and discovery system: 2.4.1.243
            BRENDA, the Enzyme Database: 2.4.1.243
///
ENTRY       EC 2.4.1.244                Enzyme
NAME        N-acetyl-beta-glucosaminyl-glycoprotein
            4-beta-N-acetylgalactosaminyltransferase;
            beta1,4-N-acetylgalactosaminyltransferase III;
            beta4GalNAc-T3;
            beta1,4-N-acetylgalactosaminyltransferase IV;
            beta4GalNAc-T4
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
SYSNAME     UDP-N-acetyl-D-galactosamine:N-acetyl-D-glucosaminyl-group
            beta-1,4-N-acetylgalactosaminyltransferase
REACTION    UDP-N-acetyl-D-galactosamine + N-acetyl-beta-D-glucosaminyl group =
            UDP +
            N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl
            group
ALL_REAC    (other) R07610(G) R07611(G)
SUBSTRATE   UDP-N-acetyl-D-galactosamine [CPD:C00203];
            N-acetyl-beta-D-glucosaminyl group
PRODUCT     UDP [CPD:C00015];
            N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl
            group
COMMENT     The enzyme from human can transfer N-acetyl-D-galactosamine (GalNAc)
            to N-glycan and O-glycan substrates that have N-acetyl-D-glucosamine
            (GlcNAc) but not D-glucuronic acid (GlcUA) at their non-reducing
            end. The N-acetyl-beta-D-glucosaminyl group is normally on a core
            oligosaccharide although benzyl glycosides have been used in
            enzyme-characterization experiments. Some glycohormones, e.g.
            lutropin and thyrotropin contain the N-glycan structure containing
            the
            N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl
            group.
REFERENCE   1  [PMID:12966086]
  AUTHORS   Sato T, Gotoh M, Kiyohara K, Kameyama A, Kubota T, Kikuchi N,
            Ishizuka Y, Iwasaki H, Togayachi A, Kudo T, Ohkura T, Nakanishi H,
            Narimatsu H.
  TITLE     Molecular cloning and characterization of a novel human beta
            1,4-N-acetylgalactosaminyltransferase, beta 4GalNAc-T3, responsible
            for the synthesis of N,N'-diacetyllactosediamine, galNAc beta
            1-4GlcNAc.
  JOURNAL   J. Biol. Chem. 278 (2003) 47534-44.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:15044014]
  AUTHORS   Gotoh M, Sato T, Kiyohara K, Kameyama A, Kikuchi N, Kwon YD,
            Ishizuka Y, Iwai T, Nakanishi H, Narimatsu H.
  TITLE     Molecular cloning and characterization of
            beta1,4-N-acetylgalactosaminyltransferases IV synthesizing
            N,N'-diacetyllactosediamine.
  JOURNAL   FEBS. Lett. 562 (2004) 134-40.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K09656  beta-1,4-N-acetylgalactosaminyltransferase 3
            KO: K09657  beta-1,4-N-acetylgalactosaminyltransferase 4
GENES       HSA: 283358(B4GALNT3) 338707(B4GALNT4)
            PTR: 451738(B4GALNT3)
            MMU: 330406(B4galnt3) 330671(B4galnt4)
            RNO: 309105(RGD1310052_predicted) 500306(RGD1561056_predicted)
            CFA: 486751(B4GALNT3)
            GGA: 770601(B4GALNT4)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.1.244
            ExPASy - ENZYME nomenclature database: 2.4.1.244
            ExplorEnz - The Enzyme Database: 2.4.1.244
            ERGO genome analysis and discovery system: 2.4.1.244
            BRENDA, the Enzyme Database: 2.4.1.244
///
ENTRY       EC 2.4.1.-                  Enzyme
CLASS       Transferases;
            Glycosyltransferases;
            Hexosyltransferases
REACTION    (1) GDP-mannose + Mannan(n) <=> GDP + Mannan(n+1) [RN:R00887];
            (2) GDP-mannose + 1,4-beta-D-Mannan <=> GDP + 1,4-beta-D-Mannan
            [RN:R00890];
            (3) Glucosylceramide + UDP-D-galactose <=>
            beta-D-Galactosyl-1,4-beta-D-glucosylceramide + UDP [RN:R03354];
            (4) Galactosylceramide + UDP-D-galactose <=> Digalactosylceramide +
            UDP [RN:R04016];
            (5) GDP-mannose + N,N'-Diacetylchitobiosyldiphosphodolichol <=> GDP
            + alpha-D-Mannosylchitobiosyldiphosphodolichol [RN:R04331];
            (6) 3-D-Glucosyl-1,2-diacylglycerol + UDP-glucose <=>
            Diglucosyl-diacylglycerol + UDP [RN:R04377];
            (7) UDP-N-acetyl-D-glucosamine + Galactosylgloboside <=> UDP +
            G00102 [RN:R05902];
            (8) UDP-D-galactose + G00102 <=> UDP + G00103 [RN:R05903];
            (9) Dolichyl phosphate D-mannose + G00147 <=> Dolichyl phosphate +
            G00148 [RN:R05921];
            (10) UDP-D-galactose + Lc3Cer <=> UDP + Paragloboside [RN:R05977];
            (11) UDP-D-galactose + G00077 <=> UDP + iso-nLc8Cer [RN:R06021];
            (12) GDP-L-fucose + nLc5Cer <=> GDP + Type II B antigen [RN:R06027];
            (13) UDP-D-galactose + nLc5Cer <=> UDP + nLc6Cer [RN:R06033];
            (14) UDP-D-galactose + nLc7Cer <=> UDP + nLc8Cer [RN:R06097];
            (15) G00005 + GDP-D-mannose <=> G10526 + GDP [RN:R06127];
            (16) G10526 + GDP-D-mannose <=> G00006 + GDP [RN:R06128];
            (17) UDP-D-galactose + G00072 <=> UDP + G00073 [RN:R06192];
            (18) UDP-D-galactose + Type II A antigen <=> UDP + G00057
            [RN:R06198];
            (19) GDP-D-mannose + G10532(n) <=> GDP + G10532(n+1) [RN:R06213];
            (20) GDP-L-fucose + V3Fuc-nLc6Cer <=> GDP + V3Fuc,III3Fuc-nLc6Cer
            [RN:R06221];
            (21) GDP-L-fucose + G00084 <=> GDP + G00085 [RN:R06222];
            (22) GDP-L-fucose + G00085 <=> GDP + G00086 [RN:R06224];
            (23) GDP-L-fucose + G00081 <=> GDP + G00082 [RN:R06227];
            (24) GDP-L-fucose + nLc6Cer <=> GDP + III3Fuc-nLc6Cer [RN:R06230];
            (25) Galactosylceramide + UDP-D-galactose <=> Ga2-Cer + UDP
            [RN:R06234];
            (26) GDP-D-mannose + G00004 <=> GDP + G00005 [RN:R06238];
            (27) Dolichyl phosphate D-mannose + G00006 <=> Dolichyl phosphate +
            G10595 [RN:R06258];
            (28) Dolichyl phosphate D-mannose + G10595 <=> Dolichyl phosphate +
            G10596 [RN:R06259];
            (29) Dolichyl phosphate D-mannose + G10596 <=> Dolichyl phosphate +
            G10597 [RN:R06260];
            (30) Dolichyl phosphate D-mannose + G10597 <=> Dolichyl phosphate +
            G00007 [RN:R06261];
            (31) Dolichyl D-glucosyl phosphate + G00007 <=> Dolichyl phosphate +
            G10598 [RN:R06262];
            (32) Dolichyl D-glucosyl phosphate + G10598 <=> Dolichyl phosphate +
            G10599 [RN:R06263];
            (33) Dolichyl D-glucosyl phosphate + G10599 <=> Dolichyl phosphate +
            G00008 [RN:R06264];
            (34) Glucocerebroside + UDP-D-galactose <=> Lactosylceramide + UDP
            [RN:R06276];
            (35) Cyanidin 3-O-glucoside + UDP-glucose <=> Cyanin + UDP
            [RN:R06546];
            (36) Cyanidin 3-O-(6-O-p-coumaroyl)glucoside <=> Cyanidin
            3-O-(6-O-p-coumaroyl)glucoside-5-O-glucoside [RN:R06547];
            (37) Cyanidin 3-O-glucoside + UDP-L-rhamnose <=> Cyanidin
            3-O-rutinoside + UDP [RN:R06818];
            (38) Zeaxanthin + 2 UDP-glucose <=> Zeaxanthin diglucoside + 2 UDP
            [RN:R07574];
            (39) UDP-N-acetyl-D-galactosamine + Sda antigen - related compound
            <=> UDP + Sda antigen [RN:R07609];
            (40) UDP-N-acetyl-D-galactosamine + G00025 <=> UDP + G13023
            [RN:R07614];
            (41) UDP-N-acetyl-D-galactosamine + G01977 <=> UDP + G13024
            [RN:R07615];
            (42) UDP-N-acetyl-D-galactosamine + G01941 <=> UDP + G13025
            [RN:R07616];
            (43) UDP-D-galactose + G00025 <=> UDP + G11136 [RN:R07617];
            (44) UDP-N-acetyl-D-glucosamine + G13027 <=> UDP + G13026
            [RN:R07619];
            (45) UDP-N-acetyl-D-glucosamine + G13026 <=> UDP + G13028
            [RN:R07621];
            (46) UDP-N-acetyl-D-glucosamine + G00015 <=> UDP + G10818
            [RN:R07622];
            (47) UDP-N-acetyl-D-glucosamine + G00015 <=> UDP + G13030
            [RN:R07623];
            (48) UDP-N-acetyl-D-glucosamine + G10818 <=> UDP + G13029
            [RN:R07624];
            (49) UDP-N-acetyl-D-glucosamine + G13030 <=> UDP + G13029
            [RN:R07625];
            (50) UDP-D-galactose + G00031 <=> UDP + G00032 [RN:R07628];
            (51) 4,4'-Diaponeurosporenic acid <=>
            Glycosyl-4,4'-diaponeurosporenoate [RN:R07655];
            (52) Pelargonidin 3-O-glucoside + UDP-glucose <=> Pelargonin + UDP
            [RN:R07874];
            (53) Pelargonidin 3-O-(6-caffeoyl-beta-D-glucoside) + UDP-glucose
            <=> Pelargonidin 3-O-(6-caffeoyl-beta-D-glucoside)
            5-O-beta-D-glucoside + UDP [RN:R07875];
            (54) Pelargonidin 3-O-glucoside + UDP-glucose <=> Pelargonidin
            3-O-sophoroside + UDP [RN:R07877];
            (55) Cyanidin 3-O-glucoside + UDP-glucose <=> Cyanidin
            3-O-sophoroside + UDP [RN:R07878];
            (56) Delphinidin 3-O-glucoside + UDP-glucose <=> Delphinidin
            3-O-sophoroside + UDP [RN:R07879];
            (57) Delphinidin 3-O-glucoside + UDP-L-rhamnose <=> Tulipanin + UDP
            [RN:R07903];
            (58) Cyanidin <=> Cyanidin 5-O-glucoside [RN:R07908];
            (59) Cyanidin 5-O-glucoside <=> Cyanin [RN:R07909];
            (60) Delphinidin 3-O-glucoside + UDP-glucose <=> Delphin + UDP
            [RN:R07911];
            (61) Delphinidin
            3-O-(6''-O-malonyl)-beta-glucoside-3'-O-beta-glucoside + UDP-glucose
            <=> Ternatin C5 + UDP [RN:R07914];
            (62) Cyanidin 3-O-(6-O-malonyl-beta-D-glucoside) + UDP-glucuronate
            <=> Cyanidin-3-O-(6''-O-malonyl-2''-O-glucuronyl)glucoside + UDP
            [RN:R07932]
SUBSTRATE   GDP-mannose [CPD:C00096];
            Mannan [CPD:C00464];
            1,4-beta-D-Mannan [CPD:C02492];
            Glucosylceramide [CPD:C01190];
            UDP-D-galactose [CPD:C00052];
            Galactosylceramide [CPD:C02686];
            N,N'-Diacetylchitobiosyldiphosphodolichol [CPD:C04537];
            3-D-Glucosyl-1,2-diacylglycerol [CPD:C04046];
            UDP-glucose [CPD:C00029];
            UDP-N-acetyl-D-glucosamine [GL:G10610];
            Galactosylgloboside [GL:G00097];
            UDP-D-galactose [GL:G10609];
            [GL:G00102];
            Dolichyl phosphate D-mannose [GL:G10617];
            [GL:G00147];
            Lc3Cer [GL:G00036];
            [GL:G00077];
            GDP-L-fucose [GL:G10615];
            nLc5Cer [GL:G00051];
            nLc5Cer [GL:G00066];
            nLc7Cer [GL:G00068];
            [GL:G00005];
            GDP-D-mannose [GL:G10614];
            [GL:G10526];
            [GL:G00072];
            Type II A antigen [GL:G00054];
            [GL:G10532];
            V3Fuc-nLc6Cer [GL:G00089];
            [GL:G00084];
            [GL:G00085];
            [GL:G00081];
            nLc6Cer [GL:G00067];
            Galactosylceramide [GL:G11121];
            [GL:G00004];
            [GL:G00006];
            [GL:G10595];
            [GL:G10596];
            [GL:G10597];
            Dolichyl D-glucosyl phosphate [GL:G10618];
            [GL:G00007];
            [GL:G10598];
            [GL:G10599];
            Glucocerebroside [GL:G10238];
            Cyanidin 3-O-glucoside [CPD:C08604];
            Cyanidin 3-O-(6-O-p-coumaroyl)glucoside [CPD:C12095]
PRODUCT     GDP [CPD:C00035];
            Mannan [CPD:C00464];
            1,4-beta-D-Mannan [CPD:C02492];
            beta-D-Galactosyl-1,4-beta-D-glucosylceramide [CPD:C01290];
            UDP [CPD:C00015];
            Digalactosylceramide [CPD:C06126];
            alpha-D-Mannosylchitobiosyldiphosphodolichol [CPD:C04615];
            Diglucosyl-diacylglycerol [CPD:C06040];
            UDP [GL:G10619];
            [GL:G00102];
            [GL:G00103];
            Dolichyl phosphate [GL:G10622];
            [GL:G00148];
            Paragloboside [GL:G00050];
            iso-nLc8Cer [GL:G00078];
            GDP [GL:G10620];
            Type II B antigen [GL:G00052];
            nLc6Cer [GL:G00067];
            nLc8Cer [GL:G00069];
            [GL:G10526];
            [GL:G00006];
            [GL:G00073];
            [GL:G00057];
            [GL:G10532];
            V3Fuc,III3Fuc-nLc6Cer [GL:G00090];
            [GL:G00085];
            [GL:G00086];
            [GL:G00082];
            III3Fuc-nLc6Cer [GL:G00076];
            Ga2-Cer [GL:G00497];
            [GL:G00005];
            [GL:G10595];
            [GL:G10596];
            [GL:G10597];
            [GL:G00007];
            [GL:G10598];
            [GL:G10599];
            [GL:G00008];
            Lactosylceramide [GL:G00092];
            Cyanin [CPD:C08639];
            Cyanidin 3-O-(6-O-p-coumaroyl)glucoside-5-O-glucoside [CPD:C12096]
///
ENTRY       EC 2.4.2.1                  Enzyme
NAME        purine-nucleoside phosphorylase;
            inosine phosphorylase;
            PNPase;
            PUNPI;
            PUNPII;
            inosine-guanosine phosphorylase;
            nucleotide phosphatase;
            purine deoxynucleoside phosphorylase;
            purine deoxyribonucleoside phosphorylase;
            purine nucleoside phosphorylase;
            purine ribonucleoside phosphorylase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     purine-nucleoside:phosphate ribosyltransferase
REACTION    purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
            [RN:R02342]
ALL_REAC    R02342;
            (other) R01561 R01863 R01969 R02147 R02294 R02295 R02297 R02484
            R02557 R02748
SUBSTRATE   purine nucleoside [CPD:C01736];
            phosphate [CPD:C00009]
PRODUCT     purine [CPD:C00465];
            alpha-D-ribose 1-phosphate [CPD:C00620]
COMMENT     Specificity not completely determined. Can also catalyse
            ribosyltransferase reactions of the type catalysed by EC 2.4.2.5,
            nucleoside ribosyltransferase.
REFERENCE   1  [PMID:5768862]
  AUTHORS   Agarwal RP, Parks RE Jr.
  TITLE     Purine nucleoside phosphorylase from human erythrocytes. IV.
            Crystallization and some properties.
  JOURNAL   J. Biol. Chem. 244 (1969) 644-7.
  ORGANISM  human [GN:hsa]
REFERENCE   2
  AUTHORS   Friedkin, M. and Kalckar, H.
  TITLE     Nucleoside phosphorylases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 5, Academic Press, New York, 1961, p. 237-255.
REFERENCE   3  [PMID:12999785]
  AUTHORS   HEPPEL LA, HILMOE RJ.
  TITLE     [Phosphorolysis and hydrolysis of purine ribosides by enzymes from
            yeast.]
  JOURNAL   J. Biol. Chem. 198 (1952) 683-94.
  ORGANISM  rat [GN:rno]
REFERENCE   4
  AUTHORS   Kalckar, H.M.
  TITLE     The enzymatic synthesis of purine ribosides.
  JOURNAL   J. Biol. Chem. 167 (1947) 477-486.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:4978445]
  AUTHORS   Saunders PP, Wilson BA, Saunders GF.
  TITLE     Purification and comparative properties of a pyrimidine nucleoside
            phosphorylase from Bacillus stearothermophilus.
  JOURNAL   J. Biol. Chem. 244 (1969) 3691-7.
  ORGANISM  Bacillus stearothermophilus
REFERENCE   6
  AUTHORS   Tsuboi, K.K. and Hudson, P.B.
  TITLE     Enzymes of the human erythrocyte. I. Purine nucleoside
            phosphorylase; isolation procedure.
  JOURNAL   J. Biol. Chem. 224 (1957) 879-887.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
            PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K00755  purine-nucleoside phosphorylase
            KO: K03783  purine-nucleoside phosphorylase
            KO: K03784  purine-nucleoside phosphorylase
GENES       HSA: 4860(NP)
            MMU: 18950(Pnp)
            CFA: 475393(NP)
            BTA: 493724(NP)
            XLA: 379499(MGC64592)
            XTR: 448370(np)
            DRE: 402953(zgc:77182)
            SPU: 578392(LOC578392)
            CEL: K02D7.1(phosphorylase)
            SCE: YLR209C(PNP1)
            AGO: AGOS_ACR198W
            CAL: CaO19_317(CaO19.317)
            CGR: CAGL0J08800g
            SPO: SPAC1805.16c
            ANI: AN6490.2
            AFM: AFUA_6G05320
            UMA: UM06108.1
            TAN: TA13170
            TET: TTHERM_00794530 TTHERM_01197070
            EHI: 27.t00013 27.t00016 27.t00056 33.t00014
            TVA: TVAG_454490
            ECO: b4384(deoD)
            ECJ: JW4347(deoD)
            ECE: Z5986(deoD)
            ECS: ECs5343
            ECC: c5468(deoD)
            ECI: UTI89_C5155(deoD)
            ECP: ECP_4768
            ECV: APECO1_1997(deoD)
            ECW: EcE24377A_4983(deoD)
            ECX: EcHS_A4619
            STY: STY4921(deoD)
            STT: t4613(deoD)
            SPT: SPA4384(deoD)
            SEC: SC4418(deoD)
            STM: STM4570(deoD)
            YPE: YPO0440(deoD)
            YPK: y3740(deoD)
            YPM: YP_3742(deoD)
            YPA: YPA_3844
            YPN: YPN_0311
            YPP: YPDSF_3194
            YPS: YPTB0584(deoD)
            YPI: YpsIP31758_2824(xapA) YpsIP31758_3495(deoD)
            YEN: YE0574(b4384)
            SFL: SF4416(deoD)
            SFX: S4687(deoD)
            SFV: SFV_4418(deoD)
            SSN: SSON_4535(deoD)
            SBO: SBO_4446(deoD)
            SDY: SDY_4644(deoD)
            ECA: ECA0730(deoD)
            PLU: plu0522(deoD)
            BUC: BU541(deoD)
            BAS: BUsg521(deoD)
            BAB: bbp483(deoD)
            HIN: HI0518(deoD)
            HIT: NTHI0644(deoD)
            HIP: CGSHiEE_00410(deoD)
            HIQ: CGSHiGG_05850(deoD)
            HDU: HD0889(deoD)
            HSO: HS_0288(deoD)
            PMU: PM1291(deoD)
            MSU: MS1899(deoD)
            APL: APL_1014(deoD)
            XCV: XCV1388(deoD)
            VCH: VC2347 VCA0053
            VCO: VC0395_0083(deoD-2) VC0395_A1926(deoD-1)
            VVU: VV1_1728 VV2_1540
            VVY: VV2676 VVA0354
            VPA: VP2433 VPA1475
            VFI: VF0507 VFA0402 VFA0968
            PPR: PBPRA0633 PBPRB0062(deoD)
            SON: SO_0092(deoD-1) SO_1221(deoD-2) SO_2719(deoD-3)
            SDN: Sden_1028
            SFR: Sfri_1005
            SAZ: Sama_0976
            SBL: Sbal_3224
            SLO: Shew_2812
            SPC: Sputcn32_2819
            SHE: Shewmr4_1040
            SHM: Shewmr7_1105
            SHN: Shewana3_1044 Shewana3_2503
            SHW: Sputw3181_1192
            ILO: IL0174(deoD)
            CPS: CPS_1978(deoD)
            PHA: PSHAb0082(deoD)
            PIN: Ping_2864
            FTU: FTT0766(deoD)
            FTF: FTF0766(deoD)
            FTW: FTW_1473(deoD)
            FTL: FTL_1461
            FTH: FTH_1421(deoD)
            FTA: FTA_1547(deoD)
            FTN: FTN_0669(deoD)
            HCH: HCH_03076(deoD)
            CSA: Csal_0828
            AHA: AHA_3010(deoD-1) AHA_3687(deoD-2)
            DNO: DNO_0699(deoD)
            CVI: CV_3698(deoD)
            REU: Reut_A1163
            AZO: azo1998
            HPY: HP1178(deoD)
            HPJ: jhp1104(deoD)
            HPA: HPAG1_1117
            HAC: Hac_0400(deoD)
            CCV: CCV52592_0592
            PCA: Pcar_2018
            DVU: DVU2230(deoD)
            DVL: Dvul_1011
            DDE: Dde_1537
            BBA: Bd3856(pnp)
            ADE: Adeh_0618
            MXA: MXAN_2306(deoD)
            SFU: Sfum_2962
            MLO: mll0765 mlr3159
            MES: Meso_0150 Meso_3656
            SME: SMc04123(deoD)
            ATU: Atu0131(deoD)
            ATC: AGR_C_210
            RET: RHE_CH00192(deoD)
            RLE: RL0201(punA)
            SIL: SPO0366(deoD)
            SIT: TM1040_3108
            RSP: RSP_2207(deoD)
            JAN: Jann_0799
            RDE: RD1_1634(deoD)
            ZMO: ZMO0873(deoD)
            ABA: Acid345_3055
            BSU: BG11330(pupG) BG12581(deoD)
            BHA: BH1531 BH1532
            BAN: BA1483(deoD) BA4308
            BAR: GBAA1483(deoD) GBAA4308
            BAA: BA_2005 BA_4766
            BAT: BAS1372 BAS3996
            BCE: BC1463 BC4086
            BCA: BCE_1588(deoD) BCE_4155
            BCZ: BCZK1344(deoD) BCZK3843(deoD)
            BTK: BT9727_1345(deoD) BT9727_3827(deoD)
            BTL: BALH_1318
            BLI: BL00774(punA) BL01437(deoD)
            BLD: BLi02285(deoD) BLi02499(punA)
            BCL: ABC3722(pupG) ABC4021(deoD)
            BAY: RBAM_002200(ybbK) RBAM_019420 RBAM_021600
            BPU: BPUM_1884 BPUM_2080
            OIH: OB1845(pnp) OB2345
            GKA: GK1580 GK2313
            SAU: SA0131(pnp) SA1940(deoD)
            SAV: SAV0136(pnp) SAV2138(deoD)
            SAM: MW0110(pnp) MW2062(deoD)
            SAR: SAR0138(deoD1) SAR2226(deoD2)
            SAS: SAS0110 SAS2041
            SAC: SACOL0121(deoD1) SACOL2130(deoD2)
            SAB: SAB0075(deoD1) SAB2022(deoD2)
            SAA: SAUSA300_0138(deoD) SAUSA300_2091(deoD)
            SAO: SAOUHSC_00097 SAOUHSC_02380
            SEP: SE1737
            SER: SERP1747(deoD)
            SHA: SH0896(deoD)
            SSP: SSP0746
            LMO: lmo1856(deoD) lmo1953(pnp)
            LMF: LMOf2365_1884(deoD) LMOf2365_1983
            LIN: lin1970(deoD) lin2067(pnp)
            LWE: lwe1875(deoD) lwe1979
            LLA: L156559(deoD)
            LLC: LACR_1003
            LLM: llmg_1599(deoD)
            SPY: SPy_0892(punA) SPy_0894(deoD2)
            SPZ: M5005_Spy_0698(punA) M5005_Spy_0699(deoD2)
            SPM: spyM18_0953(pnp) spyM18_0955(deoD)
            SPG: SpyM3_0611(punA) SpyM3_0612(deoD2)
            SPS: SPs1241 SPs1242
            SPH: MGAS10270_Spy0756(punA) MGAS10270_Spy0757(deoD2)
            SPI: MGAS10750_Spy0790(punA) MGAS10750_Spy0791(deoD2)
            SPJ: MGAS2096_Spy0770(punA) MGAS2096_Spy0771(deoD2)
            SPK: MGAS9429_Spy0754(punA) MGAS9429_Spy0755(deoD2)
            SPF: SpyM51109(deoD) SpyM51110(punA)
            SPA: M6_Spy0715 M6_Spy0716
            SPB: M28_Spy0678(punA) M28_Spy0679(deoD2)
            SPN: SP_0831 SP_0835
            SPR: spr0734(pnp) spr0738(deoD)
            SPD: SPD_0726 SPD_0730(deoD)
            SAG: SAG1178(deoD-1) SAG1180(deoD-2)
            SAN: gbs1251 gbs1253
            SAK: SAK_1265(deoD) SAK_1267(punA)
            SMU: SMU.1227(deoD) SMU.1229(punA)
            STC: str1113(deoD) str1117(punA)
            STL: stu1113(deoD) stu1117(punA)
            SSA: SSA_1258(deoD) SSA_1259(punA)
            SGO: SGO_1260(deoD) SGO_1263
            LSA: LSA0797(deoD) LSA0819(fabZ2)
            LBR: LVIS_1593
            LCA: LSEI_0280
            EFA: EF0186(deoD-1) EF0187(deoD-2)
            STH: STH836
            CAC: CAC2064(deoD)
            CPE: CPE0398(deoD) CPE1398(pfs) CPE2495(punA)
            CPF: CPF_0386 CPF_1652(deoD) CPF_2818(punA)
            CPR: CPR_1391(deoD) CPR_2504(punA)
            CTC: CTC01388 CTC01531 CTC02272
            CNO: NT01CX_1498 NT01CX_2329(deoD)
            CTH: Cthe_1201 Cthe_1575
            CDF: CD1224(deoD)
            CBO: CBO1864(deoD)
            CBA: CLB_1800(punA)
            CBH: CLC_1807(punA)
            CBF: CLI_1866(punA)
            CKL: CKL_1608(punA)
            DSY: DSY2310
            TTE: TTE1752(deoD)
            MGE: MG_049(deoD)
            MPN: MPN062(deoD)
            MPU: MYPU_6450(deoD)
            MPE: MYPE1040(pnp)
            MGA: MGA_0364(deoD)
            MMY: MSC_0835(pnp)
            MMO: MMOB5350(deoD)
            MHY: mhp297(deoD)
            MHJ: MHJ_0080(deoD)
            MHP: MHP7448_0084(deoD)
            MSY: MS53_0447(deoD)
            MCP: MCAP_0849(deoD)
            UUR: UU281(deoD)
            MFL: Mfl665
            MTU: Rv3307(deoD)
            MTC: MT3406(deoD)
            MBO: Mb3335(deoD)
            MBB: BCG_3372(deoD)
            MLE: ML0707(deoD)
            MPA: MAP3429(deoD)
            MAV: MAV_4284
            MSM: MSMEG_1701
            MVA: Mvan_1610
            MGI: Mflv_4828
            MMC: Mmcs_1244
            MKM: Mkms_1261
            MJL: Mjls_1271
            CDI: DIP0271(deoD)
            CJK: jk1674(deoD)
            NFA: nfa9610
            RHA: RHA1_ro06257
            SCO: SCO4917(SCK13.09c)
            SMA: SAV3342(deoD)
            TWH: TWT018(deoD)
            TWS: TW018(punA)
            LXX: Lxx04700(deoD)
            ART: Arth_1262
            AAU: AAur_1403
            PAC: PPA1722
            NCA: Noca_3521
            TFU: Tfu_2242
            FRA: Francci3_0691
            FAL: FRAAL1200(deoD)
            SEN: SACE_6547(deoD)
            FNU: FN0435
            RBA: RB5437(pnp) RB6588(punA)
            TPA: TP0734
            TDE: TDE0463(deoD)
            BTH: BT_1881
            BFR: BF3453
            BFS: BF3274(punA)
            PGI: PG0558
            SRU: SRU_0692 SRU_2131(deoD)
            GFO: GFO_1416(deoD) GFO_3610(punA)
            FPS: FP1472(deoD)
            CTE: CT1815(deoD)
            CCH: Cag_1351
            PLT: Plut_0477
            DRA: DR_2166
            DGE: Dgeo_1497 Dgeo_1596
            TTH: TTC0194 TTC1070
            TTJ: TTHA0562 TTHA1435
            TMA: TM1596 TM1737
            PTO: PTO0123
            APE: APE_0993.1
            SSO: SSO1519(deoD)
            STO: ST2449
STRUCTURES  PDB: 1A69  1A9O  1A9P  1A9Q  1A9R  1A9S  1A9T  1B8N  1B8O  1ECP  
                 1FXU  1G2O  1I80  1K9S  1LV8  1LVU  1M73  1N3I  1NW4  1OTX  
                 1OTY  1OU4  1OUM  1OV6  1OVG  1PBN  1PF7  1PK7  1PK9  1PKE  
                 1PR0  1PR1  1PR2  1PR4  1PR5  1PR6  1PW7  1PWY  1Q1G  1QE5  
                 1RCT  1RFG  1RR6  1RSZ  1RT9  1TCU  1TCV  1TD1  1ULA  1ULB  
                 1V2H  1V3Q  1V41  1V45  1V48  1VFN  1VHJ  1VHW  1VMK  1XE3  
                 1YQQ  1YRY  1Z33  1Z34  1Z35  1Z36  1Z37  1Z38  1Z39  2A0W  
                 2A0X  2A0Y  2AC7  2AI1  2AI2  2AI3  2B94  2BSX  2I4T  2ISC  
                 2OC4  2OC9  2ON6  3PNP  4PNP  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.1
            ExPASy - ENZYME nomenclature database: 2.4.2.1
            ExplorEnz - The Enzyme Database: 2.4.2.1
            ERGO genome analysis and discovery system: 2.4.2.1
            BRENDA, the Enzyme Database: 2.4.2.1
            CAS: 9030-21-1
///
ENTRY       EC 2.4.2.2                  Enzyme
NAME        pyrimidine-nucleoside phosphorylase;
            Py-NPase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     pyrimidine-nucleoside:phosphate alpha-D-ribosyltransferase
REACTION    a pyrimidine nucleoside + phosphate = a pyrimidine base +
            alpha-D-ribose 1-phosphate [RN:R02298]
ALL_REAC    R02298 > R02296
SUBSTRATE   pyrimidine nucleoside [CPD:C03169];
            phosphate [CPD:C00009]
PRODUCT     pyrimidine base [CPD:C00396];
            alpha-D-ribose 1-phosphate [CPD:C00620]
COMMENT     Both uridine and thymidine are substrates [3].
REFERENCE   1
  AUTHORS   Friedkin, M. and Kalckar, H.
  TITLE     Nucleoside phosphorylases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 5, Academic Press, New York, 1961, p. 237-255.
REFERENCE   2  [PMID:4978445]
  AUTHORS   Saunders PP, Wilson BA, Saunders GF.
  TITLE     Purification and comparative properties of a pyrimidine nucleoside
            phosphorylase from Bacillus stearothermophilus.
  JOURNAL   J. Biol. Chem. 244 (1969) 3691-7.
  ORGANISM  Bacillus stearothermophilus
REFERENCE   3  [PMID:8782414]
  AUTHORS   Hamamoto T, Noguchi T, Midorikawa Y.
  TITLE     Purification and characterization of purine nucleoside phosphorylase
            and pyrimidine nucleoside phosphorylase from Bacillus
            stearothermophilus TH 6-2.
  JOURNAL   Biosci. Biotechnol. Biochem. 60 (1996) 1179-80.
  ORGANISM  Bacillus stearothermophilus
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K00756  pyrimidine-nucleoside phosphorylase
GENES       BBA: Bd3855(pdp)
            MXA: MXAN_5710(pdp)
            BSU: BG10985(pdp)
            BHA: BH1533(pdp)
            BAN: BA1894(pyn-1) BA4307(pyn-2)
            BAR: GBAA1894(pyn-1) GBAA4307(pyn-2)
            BAA: BA_4765
            BAT: BAS1756 BAS3995
            BCE: BC1822 BC4085
            BCA: BCE_1977(pyn) BCE_4154(pyn)
            BCZ: BCZK1705(pyn) BCZK3842(pdp)
            BCY: Bcer98_2784
            BTK: BT9727_1734(pyn) BT9727_3826(pdp)
            BLI: BL00227(pdp)
            BLD: BLi04227(pdp)
            BCL: ABC1784(pdp)
            BAY: RBAM_036460
            BPU: BPUM_3585
            OIH: OB1844(pdp)
            GKA: GK2312
            SAU: SA1938(pdp)
            SAV: SAV2136(pdp)
            SAM: MW2060(pdp)
            SAR: SAR2224(pyn)
            SAS: SAS2039
            SAC: SACOL2128(pdp)
            SAA: SAUSA300_2089(pdp)
            SAO: SAOUHSC_02377
            SAJ: SaurJH9_2172
            SAH: SaurJH1_2210
            SEP: SE1735
            SER: SERP1744(pdp)
            LMO: lmo1993(pdp)
            LMF: LMOf2365_2016(pyn)
            LIN: lin2101(pdp)
            LWE: lwe2013(pdp)
            LLA: L64175(pdp)
            LLC: LACR_1531
            LLM: llmg_1060(pdp)
            SPN: SP_0842
            SPR: spr0744(pdp)
            SPD: SPD_0736(pdp)
            SMU: SMU.1124(pdp)
            STC: str0801 str0802 str0803 str0804
            STL: stu0801 stu0802 stu0803 stu0804
            SSA: SSA_1035(pdp)
            SGO: SGO_1079(pdp)
            LSA: LSA0801(pdp)
            LBR: LVIS_1591
            LCA: LSEI_2206
            LRE: Lreu_0113
            EFA: EF0173(pyn)
            STH: STH1039
            CAC: CAC1546(deoA)
            CPE: CPE1807(deoA)
            CPF: CPF_2062(pdp)
            CPR: CPR_1776(pdp)
            CTC: CTC01993
            CNO: NT01CX_1499
            CTH: Cthe_0678
            CDF: CD1225(deoA)
            CBO: CBO1863(pdp)
            CBA: CLB_1799(pdp)
            CBH: CLC_1806(pdp)
            CBF: CLI_1865(pdp)
            CKL: CKL_1243(pdp)
            CHY: CHY_1554(pdp)
            DRM: Dred_1101
            SWO: Swol_0609
            MTA: Moth_2275
            MGE: MG_051(deoA)
            MHY: mhp298(deoA)
            MCP: MCAP_0757(deoA)
            MSM: MSMEG_1675
            RBA: RB10231(pyn)
            TDE: TDE2191(pdp)
            SRU: SRU_1163(pyn)
            DRA: DR_0443
            TMA: TM1653
            TME: Tmel_1840
STRUCTURES  PDB: 1BRW  2DSJ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.2
            ExPASy - ENZYME nomenclature database: 2.4.2.2
            ExplorEnz - The Enzyme Database: 2.4.2.2
            ERGO genome analysis and discovery system: 2.4.2.2
            BRENDA, the Enzyme Database: 2.4.2.2
            CAS: 9055-35-0
///
ENTRY       EC 2.4.2.3                  Enzyme
NAME        uridine phosphorylase;
            pyrimidine phosphorylase;
            UrdPase;
            UPH;
            UPase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     uridine:phosphate alpha-D-ribosyltransferase
REACTION    uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
            [RN:R01876]
ALL_REAC    R01876
SUBSTRATE   uridine [CPD:C00299];
            phosphate [CPD:C00009]
PRODUCT     uracil [CPD:C00106];
            alpha-D-ribose 1-phosphate [CPD:C00620]
REFERENCE   1  [PMID:13449076]
  AUTHORS   CANELLAKIS ES.
  TITLE     Pyrimidine metabolism.  II.  Enzymatic pathways of uracil anabolism.
  JOURNAL   J. Biol. Chem. 227 (1957) 329-38.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:12997187]
  AUTHORS   PAEGE LM, SCHLENK F.
  TITLE     Bacterial uracil riboside phosphorylase.
  JOURNAL   Arch. Biochem. Biophys. 40 (1952) 42-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Pontis, H., Degerstedt, G. and Reichard, P.
  TITLE     Uridine and deoxyuridine phosphorylases from Ehrlich ascites tumor.
  JOURNAL   Biochim. Biophys. Acta 51 (1961) 138-147.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K00757  uridine phosphorylase
GENES       HSA: 151531(UPP2) 7378(UPP1)
            PTR: 470566(UPP2) 472361(UPP1)
            MMU: 22271(Upp1) 76654(Upp2)
            CFA: 480772(UPP1)
            GGA: 420942(UPP1) 424326(UPP2)
            XLA: 496317(LOC496317)
            XTR: 493536(upp2) 496532(upp1)
            DRE: 393113(uppl)
            SPU: 583868(LOC583868)
            CEL: ZK783.2
            DDI: DDB_0230169(udpA) DDB_0230170(udpB)
            PFA: PFE0660c
            TAN: TA13165 TA13175
            TPV: TP02_0437 TP02_0438
            EHI: 107.t00022 30.t00010 41.t00034
            ECO: b3831(udp)
            ECJ: JW3808(udp)
            ECE: Z5353(udp)
            ECS: ECs4761
            ECC: c4773(udp)
            ECI: UTI89_C4411(udp)
            ECP: ECP_4040
            ECV: APECO1_2630(udp)
            ECW: EcE24377A_4352(udp)
            ECX: EcHS_A4055(udp)
            STY: STY3591(udp) STY3644
            STT: t3329(udp) t3386
            SPT: SPA3751 SPA3809(udp)
            SEC: SC3866(udp)
            STM: STM3968(udp)
            YPE: YPO3786(udp)
            YPK: y0444(udp)
            YPM: YP_3263(udp)
            YPA: YPA_0238
            YPN: YPN_0178
            YPP: YPDSF_3403
            YPS: YPTB0250(udp)
            YPI: YpsIP31758_0266(udp)
            YEN: YE0251(udp)
            SFL: SF3909(udp)
            SFX: S3845(udp)
            SFV: SFV_3667(udp)
            SSN: SSON_4006(udp)
            SBO: SBO_3845(udp)
            SDY: SDY_3912(udp)
            ECA: ECA0185(udp)
            PLU: plu4417(udp)
            SGL: SG0107
            ENT: Ent638_3962
            KPN: KPN_04327(udp)
            BFL: Bfl624(udp)
            BPN: BPEN_651(udp)
            HIN: HI0280(udp)
            HIT: NTHI0389(udp)
            HIP: CGSHiEE_01660
            HSO: HS_1519(udp)
            PMU: PM1572(udp)
            MSU: MS2318(udp)
            APL: APL_1839(udp)
            VCH: VC1034 VCA0134
            VCO: VC0395_0004(udp-2) VC0395_A0552(udp-1)
            VVU: VV1_2064 VV2_1373
            VVY: VV2377 VVA0211
            VPA: VP0960 VPA1079
            VFI: VF1521 VFA0530
            PPR: PBPRA1221 PBPRA1431(udp2)
            SON: SO_4133(udp) SO_4297
            SDN: Sden_3074
            SFR: Sfri_3403
            SAZ: Sama_0412
            SBL: Sbal_3852
            SLO: Shew_3390
            SPC: Sputcn32_0543
            SHE: Shewmr4_3505
            SHM: Shewmr7_0447
            SHN: Shewana3_3680
            SHW: Sputw3181_3629
            PHA: PSHAb0316(udp)
            PIN: Ping_2868
            CBU: CBU_0735
            LPN: lpg1416
            LPF: lpl1367
            LPP: lpp1371
            FTU: FTT1326(udp)
            FTF: FTF1326(udp)
            FTW: FTW_1492
            FTL: FTL_1487
            FTH: FTH_1441(udp)
            FTA: FTA_1572
            FTN: FTN_0652(udp)
            AHA: AHA_1464(udp) AHA_3168
            GSU: GSU1663
            PCA: Pcar_2537
            LLA: L54803(udp)
            LLC: LACR_0900
            LLM: llmg_1720(udp)
            SPY: SPy_1869(udp)
            SPZ: M5005_Spy_1587(udp)
            SPM: spyM18_1933(udp)
            SPG: SpyM3_1613(udp)
            SPS: SPs0254
            SPH: MGAS10270_Spy1658(udp)
            SPI: MGAS10750_Spy1645(udp)
            SPJ: MGAS2096_Spy1612(udp)
            SPK: MGAS9429_Spy1592(udp)
            SPF: SpyM50263(udp)
            SPA: M6_Spy1599
            SPB: M28_Spy1580(udp)
            SAG: SAG2072(udp)
            SAN: gbs2026
            SAK: SAK_2011(udp)
            LCA: LSEI_2343
            STH: STH2155
            CPE: CPE0387(udp)
            CPF: CPF_0375(udp)
            CPR: CPR_0370(udp)
            SMA: SAV6653(udp)
            TPA: TP1027
            BTH: BT_4554
            BFR: BF1175
            BFS: BF1142
            PGI: PG1371
            FPS: FP1032(udp)
            HAL: VNG0893G(udp2) VNG1850G(udp1)
            HMA: rrnAC0448(udp2) rrnAC3434(udp1)
            HWA: HQ1892A(udp) HQ2647A(udp) HQ3201A(udp)
            NPH: NP3180A(udp_2) NP3510A(udp_1)
            TKO: TK1479
            APE: APE_2105.1
            HBU: Hbut_0092
            PAI: PAE3111
STRUCTURES  PDB: 1K3F  1LX7  1RXC  1RXS  1RXU  1RXY  1RYZ  1SJ9  1SQ6  1T0U  
                 1TGV  1TGY  1U1C  1U1D  1U1E  1U1F  1U1G  1Y1Q  1Y1R  1Y1S  
                 1Y1T  1ZL2  2HN9  2HRD  2HSW  2HWU  2I8A  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.3
            ExPASy - ENZYME nomenclature database: 2.4.2.3
            ExplorEnz - The Enzyme Database: 2.4.2.3
            ERGO genome analysis and discovery system: 2.4.2.3
            BRENDA, the Enzyme Database: 2.4.2.3
            CAS: 9030-22-2
///
ENTRY       EC 2.4.2.4                  Enzyme
NAME        thymidine phosphorylase;
            pyrimidine phosphorylase;
            thymidine-orthophosphate deoxyribosyltransferase;
            animal growth regulators, blood platelet-derived endothelial cell
            growth factors;
            blood platelet-derived endothelial cell growth factor;
            deoxythymidine phosphorylase;
            gliostatins;
            pyrimidine deoxynucleoside phosphorylase;
            thymidine:phosphate deoxy-D-ribosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     thymidine:phosphate deoxy-alpha-D-ribosyltransferase
REACTION    thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate
            [RN:R01570]
ALL_REAC    R01570;
            (other) R01969 R02484 R02557 R02748
SUBSTRATE   thymidine [CPD:C00214];
            phosphate [CPD:C00009]
PRODUCT     thymine [CPD:C00178];
            2-deoxy-alpha-D-ribose 1-phosphate [CPD:C00672]
COMMENT     The enzyme in some tissues also catalyses deoxyribosyltransferase
            reactions of the type catalysed by EC 2.4.2.6, nucleoside
            deoxyribosyltransferase.
REFERENCE   1  [PMID:13152099]
  AUTHORS   FRIEDKIN M, ROBERTS D.
  TITLE     The enzymatic synthesis of nucleosides. I. Thymidine phosphorylase
            in mammalian tissue.
  JOURNAL   J. Biol. Chem. 207 (1954) 245-56.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   Zimmerman, M. and Seidenberg, J.
  TITLE     Deoxyribosyl transfer. I. Thymidine phosphorylase and nucleoside
            deoxyribosyltransferase in normal and malignant tissues.
  JOURNAL   J. Biol. Chem. 239 (1964) 2618-2621.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Zimmerman, M.
  TITLE     Deoxyribosyl transfer. II. Nucleoside:pyrimidine
            deoxyribosyltransferase activity of three partially purified
            thymidine phosphorylases.
  JOURNAL   J. Biol. Chem. 239 (1964) 2622-2627.
  ORGANISM  human, Escherichia coli [GN:eco]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
            PATH: map05219  Bladder cancer
ORTHOLOGY   KO: K00758  thymidine phosphorylase
GENES       HSA: 1890(ECGF1)
            MMU: 72962(Ecgf1)
            SPU: 592241(LOC592241)
            TET: TTHERM_00790780
            ECO: b4382(deoA)
            ECJ: JW4345(deoA)
            ECE: Z5984(deoA)
            ECS: ECs5341
            ECC: c5466(deoA)
            ECI: UTI89_C5153(deoA)
            ECP: ECP_4766
            ECV: APECO1_1999(deoA)
            ECW: EcE24377A_4981(deoA)
            ECX: EcHS_A4617
            STY: STY4919(deoA)
            STT: t4611(deoA)
            SPT: SPA4382(deoA)
            SEC: SC4416(deoA)
            STM: STM4568(deoA)
            YPM: YP_3744(deoA)
            YPA: YPA_3846
            YPN: YPN_0309
            YPP: YPDSF_3196
            YPS: YPTB0582(deoA)
            YPI: YpsIP31758_3497(deoA)
            YEN: YE0571(deoA)
            SFL: SF4414(deoA)
            SFX: S4685(deoA)
            SFV: SFV_4416(deoA)
            SSN: SSON_4533(deoA)
            SBO: SBO_4444(deoA)
            SDY: SDY_4642(deoA)
            ECA: ECA0728(deoA)
            SGL: SG0395
            ENT: Ent638_0542
            SPE: Spro_0661
            VCH: VC2349
            VCO: VC0395_A1928(deoA)
            VVU: VV1_1726
            VVY: VV2678
            VPA: VP2435
            VFI: VF0505
            PPR: PBPRA0631
            SON: SO_1218(deoA)
            SDN: Sden_1026
            SFR: Sfri_1003
            SAZ: Sama_0974
            SBL: Sbal_3226
            SBM: Shew185_3229
            SLO: Shew_2814
            SPC: Sputcn32_2821
            SSE: Ssed_3377
            SPL: Spea_3047
            SHE: Shewmr4_1038
            SHM: Shewmr7_1103
            SHN: Shewana3_1042
            SHW: Sputw3181_1190
            ILO: IL1882(deoA)
            CPS: CPS_1970(deoA)
            PIN: Ping_2865
            LPN: lpg1022(deoA)
            LPP: lpp2359
            MCA: MCA1717
            HCH: HCH_01516(deoA)
            CSA: Csal_0830
            AHA: AHA_3689(deoA)
            DNO: DNO_0908(deoA)
            CVI: CV_3700(deoA)
            RSO: RSc0204(deoA)
            REU: Reut_B4704
            REH: H16_A2012(deoA)
            BMA: BMAA0114(deoA)
            BMV: BMASAVP1_1276(deoA)
            BMN: BMA10247_A0136(deoA)
            BUR: Bcep18194_C6660
            BCN: Bcen_1591
            BCH: Bcen2424_6240
            BPS: BPSS1960(deoA)
            BPM: BURPS1710b_A1066(deoA)
            BPL: BURPS1106A_A2662(deoA)
            BPD: BURPS668_A2806(deoA)
            BTE: BTH_II0412
            RFR: Rfer_2241
            POL: Bpro_1194
            AJS: Ajs_2690
            ADE: Adeh_0617
            MLO: mlr3160
            MES: Meso_3657 Meso_3880
            SME: SMc04122(deoA)
            ATU: Atu0133(deoA)
            ATC: AGR_C_214
            RET: RHE_CH00194(deoA)
            RLE: RL0203(deoA)
            BJA: bll3117
            BRA: BRADO2724
            BBT: BBta_3062
            RPA: RPA4147
            RPC: RPC_4089
            RPD: RPD_1443
            RPE: RPE_4149
            NHA: Nham_1900
            SIL: SPO2929(deoA)
            SIT: TM1040_1571
            RSP: RSP_1595
            RSH: Rsph17029_0248
            RSQ: Rsph17025_0276
            JAN: Jann_2986
            RDE: RD1_1528 RD1_3979(deoA)
            PDE: Pden_2222
            MMR: Mmar10_0191
            SAB: SAB2020c(pyn)
            SHA: SH0898(deoA)
            SSP: SSP0748
            DSY: DSY2309
            TTE: TTE0464(deoA)
            MPN: MPN064(deoA)
            MPU: MYPU_6460(deoA)
            MPE: MYPE1050(deoA)
            MGA: MGA_0362(deoA)
            MMY: MSC_0830(deoA)
            MMO: MMOB5360(deoA)
            MHJ: MHJ_0079(deoA)
            MHP: MHP7448_0083(deoA)
            MSY: MS53_0446(deoA)
            UUR: UU368(deoA)
            MFL: Mfl119
            MTU: Rv3314c(deoA)
            MTC: MT3415(deoA)
            MBO: Mb3343c(deoA)
            MBB: BCG_3380c(deoA)
            MPA: MAP3439c(deoA)
            MAV: MAV_4295
            MVA: Mvan_1591
            MGI: Mflv_4842
            MMC: Mmcs_1232
            MKM: Mkms_1249
            MJL: Mjls_1258
            NFA: nfa9510(deoA)
            RHA: RHA1_ro06250
            SCO: SCO4890(2SCK8.16)
            SMA: SAV3365(deoA)
            LXX: Lxx04650(deoA)
            ART: Arth_1142
            PAC: PPA1367
            NCA: Noca_3535
            FRA: Francci3_0685
            FAL: FRAAL1194(deoA)
            KRA: Krad_3944
            SEN: SACE_6575(deoA)
            DGE: Dgeo_2180
            TTH: TTC1412
            TTJ: TTHA1771
            MMP: MMP0327(deoA)
            MAC: MA3242(deoA)
            MBA: Mbar_A3188
            MMA: MM_0087
            MBU: Mbur_0255
            MHU: Mhun_2262
            MEM: Memar_0551
            NPH: NP3958A(deoA)
            PAB: PAB1982(deoA)
            PFU: PF1607
            TKO: TK0352
            RCI: RCIX1126(deoA)
STRUCTURES  PDB: 1AZY  1OTP  1TPT  1UOU  2J0F  2TPT  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.4
            ExPASy - ENZYME nomenclature database: 2.4.2.4
            ExplorEnz - The Enzyme Database: 2.4.2.4
            ERGO genome analysis and discovery system: 2.4.2.4
            BRENDA, the Enzyme Database: 2.4.2.4
            CAS: 9030-23-3
///
ENTRY       EC 2.4.2.5                  Enzyme
NAME        nucleoside ribosyltransferase;
            nucleoside N-ribosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     nucleoside:purine(pyrimidine) D-ribosyltransferase
REACTION    D-ribosyl-base1 + base2 = D-ribosyl-base2 + base1 [RN:R03852]
ALL_REAC    R03852
SUBSTRATE   D-ribosyl-base1 [CPD:C02142];
            base2 [CPD:C00701]
PRODUCT     D-ribosyl-base2 [CPD:C02142];
            base1 [CPD:C00701]
COMMENT     Base1 and base2 represent various purines and pyrimidines.
REFERENCE   1  [PMID:13376622]
  AUTHORS   KOCH AL.
  TITLE     Some enzymes of nucleoside metabolism of Escherichia coli.
  JOURNAL   J. Biol. Chem. 223 (1956) 535-49.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.5
            ExPASy - ENZYME nomenclature database: 2.4.2.5
            ExplorEnz - The Enzyme Database: 2.4.2.5
            ERGO genome analysis and discovery system: 2.4.2.5
            BRENDA, the Enzyme Database: 2.4.2.5
            CAS: 9030-31-3
///
ENTRY       EC 2.4.2.6                  Enzyme
NAME        nucleoside deoxyribosyltransferase;
            purine(pyrimidine) nucleoside:purine(pyrimidine) deoxyribosyl
            transferase;
            deoxyribose transferase;
            nucleoside trans-N-deoxyribosylase;
            trans-deoxyribosylase;
            trans-N-deoxyribosylase;
            trans-N-glycosidase;
            nucleoside deoxyribosyltransferase I (purine nucleoside:purine
            deoxyribosyltransferase: strictly specific for transfer between
            purine bases);
            nucleoside deoxyribosyltransferase II [purine(pyrimidine)
            nucleoside:purine(pyrimidine) deoxyribosyltransferase]
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     nucleoside:purine(pyrimidine) deoxy-D-ribosyltransferase
REACTION    2-deoxy-D-ribosyl-base1 + base2 = 2-deoxy-D-ribosyl-base2 + base1
            [RN:R04168]
ALL_REAC    R04168 > R02806
SUBSTRATE   2-deoxy-D-ribosyl-base1 [CPD:C03216];
            base2 [CPD:C00701]
PRODUCT     2-deoxy-D-ribosyl-base2 [CPD:C03216];
            base1 [CPD:C00701]
COMMENT     Base1 and base2 represent various purines and pyrimidines.
REFERENCE   1  [PMID:14915963]
  AUTHORS   KALCKAR HM, MACNUTT WS, HOFF-JORGENSEN E.
  TITLE     Trans-N-glycosidase studied with radioactive adenine.
  JOURNAL   Biochem. J. 50 (1952) 397-400.
  ORGANISM  Lactobacillus helveticus
REFERENCE   2  [PMID:14915962]
  AUTHORS   MACNUTT WS.
  TITLE     The enzymically catalysed transfer of the deoxyribosyl group from
            one purine or pyrimidine to another.
  JOURNAL   Biochem. J. 50 (1952) 384-97.
  ORGANISM  Lactobacillus helveticus
REFERENCE   3  [PMID:13563482]
  AUTHORS   ROUSH AH, BETZ RF.
  TITLE     Purification and properties of trans-N-deoxyribosylase.
  JOURNAL   J. Biol. Chem. 233 (1958) 261-6.
  ORGANISM  Lactobacillus helveticus
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K08728  nucleoside deoxyribosyltransferase
GENES       REH: H16_A0680
            RLE: RL1816
            BAY: RBAM_008240(yfjP)
            LLM: llmg_0478(ntd)
            LJO: LJ0124
            LAC: LBA0145
            LSA: LSA0508 LSA1168
            LSL: LSL_1643
            LDB: Ldb0198(ndt1) Ldb1887(ndt2)
            LBU: LBUL_0172
            LBR: LVIS_0416
            LCA: LSEI_2288
            LGA: LGAS_0124
            LRE: Lreu_0970
            PPE: PEPE_1074
            OOE: OEOE_0891
            LME: LEUM_1182
            RCI: RCIX1004
STRUCTURES  PDB: 1F8X  1F8Y  1S2D  1S2G  1S2I  1S2L  1S3F  2A0K  2F2T  2F62  
                 2F64  2F67  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.6
            ExPASy - ENZYME nomenclature database: 2.4.2.6
            ExplorEnz - The Enzyme Database: 2.4.2.6
            ERGO genome analysis and discovery system: 2.4.2.6
            BRENDA, the Enzyme Database: 2.4.2.6
            CAS: 9026-86-2
///
ENTRY       EC 2.4.2.7                  Enzyme
NAME        adenine phosphoribosyltransferase;
            AMP pyrophosphorylase;
            transphosphoribosidase;
            APRT;
            AMP-pyrophosphate phosphoribosyltransferase;
            adenine phosphoribosylpyrophosphate transferase;
            adenosine phosphoribosyltransferase;
            adenylate pyrophosphorylase;
            adenylic pyrophosphorylase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     AMP:diphosphate phospho-D-ribosyltransferase
REACTION    AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate
            [RN:R00190]
ALL_REAC    R00190;
            (other) R01229 R04378
SUBSTRATE   AMP [CPD:C00020];
            diphosphate [CPD:C00013]
PRODUCT     adenine [CPD:C00147];
            5-phospho-alpha-D-ribose 1-diphosphate [CPD:C00119]
COMMENT     5-Amino-4-imidazolecarboxamide can replace adenine.
REFERENCE   1  [PMID:13475309]
  AUTHORS   FLAKS JG, ERWIN MJ, BUCHANAN JM.
  TITLE     Biosynthesis of the purines. XVI. The synthesis of adenosine
            5'-phosphate and 5-amino-4-imidazolecarboxamide ribotide by a
            nucleotide pyrophosphorylase.
  JOURNAL   J. Biol. Chem. 228 (1957) 201-13.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   Kornberg, A., Lieberman, I. and Simms, E.S.
  TITLE     Enzymatic synthesis of purine nucleotides.
  JOURNAL   J. Biol. Chem. 215 (1955) 417-427.
  ORGANISM  cow [GN:bta], Saccharomyces cerevisiae [GN:sce], sheep, pig
            [GN:ssc], pigeon, chicken [GN:gga], rat [GN:rno]
REFERENCE   3  [PMID:13436452]
  AUTHORS   LUKENS LN, HERRINGTON KA.
  TITLE     Enzymic formation of 6-mercaptopurine tibo tide.
  JOURNAL   Biochim. Biophys. Acta. 24 (1957) 432-3.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K00759  adenine phosphoribosyltransferase
GENES       HSA: 353(APRT)
            MMU: 11821(Aprt)
            CFA: 479615(APRT)
            XTR: 493317(aprt)
            DRE: 393641(aprt)
            SPU: 583890(LOC583890)
            DME: Dmel_CG18315(Aprt)
            CEL: T19B4.3
            ATH: AT1G27450(APT1) AT1G80050(APT2) AT4G12440(APT4)
                 AT4G22570(APT3) AT5G11160(APT5)
            OSA: 4329972 4336327 4343246
            SCE: YDR441C(APT2) YML022W(APT1)
            AGO: AGOS_AER325W
            PIC: PICST_29461(APT1)
            CGR: CAGL0G07106g
            SPO: SPAC23A1.03
            ANI: AN9083.2
            AFM: AFUA_7G02310
            AOR: AO090038000610
            CNE: CND05020
            UMA: UM04565.1
            DDI: DDB_0230173
            TET: TTHERM_00011180
            TBR: Tb927.7.1780 Tb927.7.1790
            TCR: 507519.140 508207.74
            LMA: LmjF26.0140
            ECO: b0469(apt)
            ECJ: JW0458(apt)
            ECE: Z0586(apt)
            ECS: ECs0522
            ECC: c0588(apt)
            ECI: UTI89_C0496(apt)
            ECP: ECP_0530
            ECV: APECO1_1546(apt)
            ECW: EcE24377A_0506(apt)
            ECX: EcHS_A0546
            STY: STY0527(apt)
            STT: t2377(apt)
            SPT: SPA2239(apt)
            SEC: SC0524(apt)
            STM: STM0483(apt)
            YPE: YPO3123(apt) YPO4019
            YPK: y1059(apt) y4040(apt)
            YPM: YP_0806(apt1) YP_3382(apt2)
            YPA: YPA_2617 YPA_4107
            YPN: YPN_0965 YPN_3667
            YPP: YPDSF_2760
            YPS: YPTB0991(apt)
            YPI: YpsIP31758_3060(apt)
            SFL: SF0414(apt)
            SFX: S0421(apt)
            SFV: SFV_0442(apt)
            SSN: SSON_0456(apt)
            SBO: SBO_0369(apt)
            SDY: SDY_0450(apt)
            ECA: ECA1175(apt)
            PLU: plu3842(apt)
            SGL: SG0688
            ENT: Ent638_0949
            SPE: Spro_1134
            BFL: Bfl300(apt)
            BPN: BPEN_308(apt)
            HIT: NTHI1938(apt)
            HIP: CGSHiEE_03890
            HIQ: CGSHiGG_01855
            HDU: HD1818(apt)
            HSO: HS_1201(apt)
            PMU: PM0363(apt)
            MSU: MS0870(apt)
            APL: APL_0266(apt)
            ASU: Asuc_0970
            XCC: XCC2283(apt)
            XCB: XC_1832
            XCV: XCV2588(apt)
            XAC: XAC2391(apt)
            XOO: XOO2717(apt)
            XOM: XOO_2562(XOO2562)
            VCH: VC1053
            VCO: VC0395_A0571(apt)
            VVU: VV1_2002
            VVY: VV2412
            VPA: VP2180
            VFI: VF1688
            PPR: PBPRA1016
            PAE: PA1543(apt)
            PAU: PA14_44500(apt)
            PAP: PSPA7_3789(apt)
            PPU: PP_4266(apt)
            PPF: Pput_1602
            PST: PSPTO_1990(apt)
            PSB: Psyr_3426
            PSP: PSPPH_3352(apt)
            PFL: PFL_1909(apt)
            PFO: Pfl_1810
            PEN: PSEEN1791(apt)
            PMY: Pmen_2616
            PAR: Psyc_1189(apt)
            PCR: Pcryo_1201
            PRW: PsycPRwf_1252
            SON: SO_2012(apt)
            SDN: Sden_2382
            SFR: Sfri_2408
            SAZ: Sama_1309
            SBL: Sbal_2575
            SBM: Shew185_2616
            SLO: Shew_2236
            SPC: Sputcn32_2303
            SSE: Ssed_2853
            SPL: Spea_1507
            SHE: Shewmr4_2255
            SHM: Shewmr7_2327
            SHN: Shewana3_2447
            SHW: Sputw3181_1705
            ILO: IL1850(apt)
            CPS: CPS_3745(apt)
            PHA: PSHAa1200(apt)
            PAT: Patl_2898
            PIN: Ping_2278
            MAQ: Maqu_2814
            MCA: MCA0816(apt)
            FTU: FTT0078(apt)
            FTF: FTF0078(apt)
            FTW: FTW_0154(apt)
            FTL: FTL_1782
            FTH: FTH_1718(apt)
            FTA: FTA_1888(apt)
            FTN: FTN_1633(apt)
            TCX: Tcr_0108
            NOC: Noc_0169
            CSA: Csal_2098
            MMW: Mmwyl1_2232
            AHA: AHA_2210(apt)
            DNO: DNO_0414(apt)
            NME: NMB1662
            NMA: NMA1920(apt)
            NMC: NMC1580(apt)
            NGO: NGO1311
            CVI: CV_3772(apt)
            RSO: RSc0417(apt)
            REU: Reut_A0363
            REH: H16_A0395(apt)
            RME: Rmet_0311
            BMV: BMASAVP1_A0069
            BML: BMA10299_A1521(apt)
            BMN: BMA10247_2949
            BXE: Bxe_A4115
            BVI: Bcep1808_2889
            BUR: Bcep18194_A6114
            BCN: Bcen_2170
            BCH: Bcen2424_2784
            BAM: Bamb_2844
            BPS: BPSL0540
            BPM: BURPS1710b_0772(apt)
            BPL: BURPS1106A_0604(apt)
            BPD: BURPS668_0588(apt)
            BTE: BTH_I0493(apt)
            PNU: Pnuc_0881
            BPE: BP0264(apt)
            BPA: BPP4020(apt)
            BBR: BB4493(apt)
            RFR: Rfer_4239
            AAV: Aave_4787
            AJS: Ajs_4134
            MPT: Mpe_A3812
            NEU: NE0181(apt)
            NET: Neut_0262
            NMU: Nmul_A0935
            MFA: Mfla_2383
            HPY: HP0572
            HPJ: jhp0519(apt)
            HPA: HPAG1_0551
            HHE: HH1370(apt)
            HAC: Hac_1440(apt)
            WSU: WS1350(APT)
            TDN: Tmden_1118
            CJE: Cj0927(apt)
            CJR: CJE1005(apt)
            CJJ: CJJ81176_0934(apt)
            CJU: C8J_0864(apt)
            CJD: JJD26997_0887(apt)
            CFF: CFF8240_1169(apt)
            CCV: CCV52592_1315(apt)
            CHA: CHAB381_1044(apt)
            CCO: CCC13826_0530 CCC13826_1608(apt)
            ABU: Abu_0699(apt)
            NIS: NIS_0707(apt)
            SUN: SUN_0659(apt)
            GSU: GSU1526(apt)
            GME: Gmet_1422
            GUR: Gura_2616
            PCA: Pcar_1431
            PPD: Ppro_2740
            DDE: Dde_0140
            BBA: Bd0845(aprT)
            DPS: DP1516
            ADE: Adeh_0751
            AFW: Anae109_0788
            MXA: MXAN_5352(apt)
            PUB: SAR11_1213(apt)
            MLO: mll2701
            MES: Meso_2163
            PLA: Plav_2246
            SME: SMc02698(apt)
            SMD: Smed_2270
            ATU: Atu2236(apt)
            ATC: AGR_C_4069
            RET: RHE_CH03035(aptch) RHE_PD00341(aptd)
            RLE: RL3483(apt)
            BME: BMEI0476
            BMF: BAB1_1556(apt)
            BMS: BR1540(apt)
            BMB: BruAb1_1529(apt)
            BOV: BOV_1489(apt)
            OAN: Oant_1626
            BJA: blr2490(apt)
            BRA: BRADO1992(apt)
            BBT: BBta_2310(apt)
            RPA: RPA4492(apt)
            RPB: RPB_4317
            RPC: RPC_4387
            RPD: RPD_4212
            NWI: Nwi_2613
            NHA: Nham_3237
            SIL: SPO3066(apt)
            SIT: TM1040_2325
            RSP: RSP_1836(apt)
            RSH: Rsph17029_0485
            RSQ: Rsph17025_0625
            JAN: Jann_3212
            RDE: RD1_2148(apt) RD1_2373(apt)
            PDE: Pden_3620
            MMR: Mmar10_0743
            NAR: Saro_0675
            SAL: Sala_1342
            ELI: ELI_13650
            GOX: GOX0835
            GBE: GbCGDNIH1_0336
            ACR: Acry_0401
            RRU: Rru_A0607
            MAG: amb2849
            ABA: Acid345_3608
            SUS: Acid_7098
            BSU: BG12568(apt)
            BHA: BH1241(apt)
            BAN: BA4638(apt)
            BAR: GBAA4638(apt)
            BAA: BA_5076
            BAT: BAS4303
            BCE: BC4402
            BCA: BCE_4492(apt)
            BCZ: BCZK4152(apt)
            BCY: Bcer98_3124
            BTK: BT9727_4141(apt)
            BTL: BALH_3989(apt)
            BLI: BL01126(apt)
            BLD: BLi02888(apt)
            BCL: ABC1569(apt)
            BAY: RBAM_020260(xpt) RBAM_024720
            BPU: BPUM_2402
            OIH: OB2025(apt)
            GKA: GK2579
            SAU: SA1461(apt)
            SAV: SAV1635(apt)
            SAM: MW1585(apt)
            SAR: SAR1715(apt)
            SAS: SAS1571
            SAC: SACOL1690(apt)
            SAB: SAB1504c(apt)
            SAA: SAUSA300_1591(apt)
            SAO: SAOUHSC_01743
            SAJ: SaurJH9_1692
            SAH: SaurJH1_1725
            SEP: SE1317
            SER: SERP1198(apt)
            SHA: SH1286(apt)
            SSP: SSP1124
            LMO: lmo1524(apt)
            LMF: LMOf2365_1543(apt)
            LIN: lin1559(apt)
            LWE: lwe1537(apt)
            LLA: L22735(apt)
            LLC: LACR_0657
            LLM: llmg_0607(apt)
            SPY: SPy_0927(apt)
            SPZ: M5005_Spy_0728(apt)
            SPM: spyM18_0984(apt)
            SPG: SpyM3_0640(apt)
            SPS: SPs1212
            SPH: MGAS10270_Spy0787(apt)
            SPI: MGAS10750_Spy0822(apt)
            SPJ: MGAS2096_Spy0800(apt)
            SPK: MGAS9429_Spy0786(apt)
            SPF: SpyM51079(apt)
            SPA: M6_Spy0754
            SPB: M28_Spy0708(apt)
            SPN: SP_1577
            SPR: spr1435(apt)
            SPD: SPD_1407(apt)
            SAG: SAG1205(apt)
            SAN: gbs1278
            SAK: SAK_1292(apt)
            SMU: SMU.1467(apt)
            STC: str1223(apt)
            STL: stu1223(apt)
            SSA: SSA_1421(apt)
            SGO: SGO_1001(apt)
            LPL: lp_2086(apt)
            LJO: LJ1474
            LAC: LBA1242(aprT)
            LSA: LSA1276(apt)
            LSL: LSL_1090(apt)
            LDB: Ldb1308(apt)
            LBU: LBUL_1222
            LBR: LVIS_1376
            LCA: LSEI_1557
            EFA: EF1687(apt)
            OOE: OEOE_1069
            STH: STH2438
            CAC: CAC2275(apt)
            CPE: CPE1939(apt)
            CPF: CPF_2194(apt)
            CPR: CPR_1905(apt)
            CTC: CTC02200
            CNO: NT01CX_1843
            CTH: Cthe_1345
            CDF: CD2745(apt)
            CBO: CBO3060(apt)
            CBA: CLB_3089(apt)
            CBH: CLC_2962(apt)
            CBF: CLI_3119(apt)
            CBE: Cbei_1539
            CKL: CKL_3132(apt)
            AMT: Amet_2352
            CHY: CHY_2027(apt)
            DSY: DSY2452
            DRM: Dred_0732
            TTE: TTE1194(apt)
            MGE: MG_276
            MPN: MPN395(apt)
            MPU: MYPU_3220(apt)
            MPE: MYPE10230(apt)
            MGA: MGA_0955(apt)
            MMY: MSC_0474(apt)
            MMO: MMOB1980(apt)
            MHY: mhp266(apt)
            MHJ: MHJ_0110(apt)
            MHP: MHP7448_0114(apt)
            MSY: MS53_0687(apt)
            MCP: MCAP_0497(apt)
            UUR: UU488(apt)
            MFL: Mfl276
            MTU: Rv2584c(apt)
            MTC: MT2661(apt)
            MBO: Mb2615c(apt)
            MBB: BCG_2607c(apt)
            MPA: MAP1046(apt)
            MAV: MAV_3465
            MSM: MSMEG_2964
            MVA: Mvan_2586
            MGI: Mflv_3813
            MMC: Mmcs_2279
            MKM: Mkms_2326
            MJL: Mjls_2318
            CGL: NCgl1591(cgl1654)
            CGB: cg1862(apt)
            CEF: CE1768(apt)
            CDI: DIP1369(apt)
            CJK: jk1049(apt)
            NFA: nfa36880(apt)
            RHA: RHA1_ro06899
            SCO: SCO1514(apt)
            SMA: SAV6839(apt)
            CMI: CMM_2055(aptA)
            ART: Arth_1509
            PAC: PPA1164
            NCA: Noca_2391
            TFU: Tfu_2091
            FRA: Francci3_1375
            FAL: FRAAL2146(apt)
            ACE: Acel_1339
            KRA: Krad_3049
            SEN: SACE_2027(apt)
            BLO: BL0731(apt)
            BAD: BAD_0807(apt)
            RXY: Rxyl_1432
            FNU: FN1483 FN2073
            RBA: RB5847(apt)
            BGA: BG0801(apt)
            BAF: BAPKO_0826(apt)
            TPA: TP1039
            TDE: TDE1684(apt)
            LIL: LB176
            LIC: LIC20142(apt)
            LBJ: LBJ_4170
            LBL: LBL_4185
            SYN: sll1430(apt)
            SYW: SYNW0814
            SYC: syc1650_d(apt)
            SYF: Synpcc7942_2454
            SYD: Syncc9605_1834
            SYE: Syncc9902_0821
            SYG: sync_1226(apt)
            SYR: SynRCC307_0966(apt)
            SYX: SynWH7803_1444(apt)
            CYA: CYA_2018(apt)
            CYB: CYB_2813(apt)
            TEL: tlr2338
            GVI: glr2747
            ANA: alr4582
            AVA: Ava_2470
            PMA: Pro1445(apt)
            PMM: PMM1122(apt)
            PMT: PMT0810
            PMN: PMN2A_0375
            PMI: PMT9312_1133
            PMB: A9601_12301(apt)
            PMC: P9515_12151(apt)
            PMF: P9303_13991(apt)
            PMG: P9301_14411(apt)
            PMH: P9215_14751
            PME: NATL1_10571(apt)
            TER: Tery_0435
            BTH: BT_3267
            BFR: BF0099
            BFS: BF0112(apt)
            CHU: CHU_2005(apt)
            GFO: GFO_0464(apt)
            FJO: Fjoh_2974
            CTE: CT0293(apt)
            CCH: Cag_0565
            CPH: Cpha266_0423
            PVI: Cvib_1509
            PLT: Plut_1727
            RRS: RoseRS_0741
            RCA: Rcas_0332
            DRA: DR_0878
            DGE: Dgeo_1550
            TTH: TTC1249 TTC1250
            TTJ: TTHA1613 TTHA1614
            TMA: TM1384
            TPT: Tpet_1399
            TME: Tmel_1842
            FNO: Fnod_0873
            MMP: MMP0660(apt)
            MMQ: MmarC5_0915
            MMZ: MmarC7_1686
            MVN: Mevan_1531
            MAC: MA0717(hpt)
            MBA: Mbar_A1633
            MMA: MM_1876
            MBU: Mbur_1435
            MTH: MTH1320
            MST: Msp_1538(apt)
            MSI: Msm_1359
            MKA: MK0610
            HAL: VNG0559G(apt)
            HMA: rrnAC1903(apt2) rrnAC3523(apt1)
            HWA: HQ1672A(apt) HQ2050A(apt) HQ3228A(apt)
            NPH: NP1254A(apt_2) NP1426A(apt_1)
            RCI: RCIX1545(apt)
            APE: APE_0060.1
STRUCTURES  PDB: 1G2P  1G2Q  1L1Q  1L1R  1MZV  1ORE  1VCH  1ZN7  1ZN8  1ZN9  
                 2DY0  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.7
            ExPASy - ENZYME nomenclature database: 2.4.2.7
            ExplorEnz - The Enzyme Database: 2.4.2.7
            ERGO genome analysis and discovery system: 2.4.2.7
            BRENDA, the Enzyme Database: 2.4.2.7
            CAS: 9027-80-9
///
ENTRY       EC 2.4.2.8                  Enzyme
NAME        hypoxanthine phosphoribosyltransferase;
            IMP pyrophosphorylase;
            transphosphoribosidase;
            hypoxanthine---guanine phosphoribosyltransferase;
            guanine phosphoribosyltransferase;
            GPRT;
            HPRT;
            guanosine 5'-phosphate pyrophosphorylase;
            IMP-GMP pyrophosphorylase;
            HGPRTase;
            6-hydroxypurine phosphoribosyltransferase;
            6-mercaptopurine phosphoribosyltransferase;
            GMP pyrophosphorylase;
            guanine-hypoxanthine phosphoribosyltransferase;
            guanosine phosphoribosyltransferase;
            guanylate pyrophosphorylase;
            guanylic pyrophosphorylase;
            inosinate pyrophosphorylase;
            inosine 5'-phosphate pyrophosphorylase;
            inosinic acid pyrophosphorylase;
            inosinic pyrophosphorylase;
            6-mercaptopurine phosphoribosyltransferase;
            purine-6-thiol phosphoribosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     IMP:diphosphate phospho-D-ribosyltransferase
REACTION    IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose
            1-diphosphate [RN:R01132]
ALL_REAC    R01132;
            (other) R00190 R01229 R02142
SUBSTRATE   IMP [CPD:C00130];
            diphosphate [CPD:C00013]
PRODUCT     hypoxanthine [CPD:C00262];
            5-phospho-alpha-D-ribose 1-diphosphate [CPD:C00119]
COMMENT     Guanine and 6-mercaptopurine can replace hypoxanthine.
REFERENCE   1
  AUTHORS   Flaks, J.G.
  TITLE     Nucleotide synthesis from 5-phosphoribosylpyrophosphate.
  JOURNAL   Methods Enzymol. 6 (1963) 136-158.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   Kornberg, A., Lieberman, I. and Simms, E.S.
  TITLE     Enzymatic synthesis of purine nucleotides.
  JOURNAL   J. Biol. Chem. 215 (1955) 417-427.
REFERENCE   3  [PMID:13436452]
  AUTHORS   LUKENS LN, HERRINGTON KA.
  TITLE     Enzymic formation of 6-mercaptopurine tibo tide.
  JOURNAL   Biochim. Biophys. Acta. 24 (1957) 432-3.
  ORGANISM  cow [GN:bta]
REFERENCE   4
  AUTHORS   Remy, C.N., Remy, W.T. and Buchanan, J.M.
  TITLE     Biosynthesis of the purines. VIII. Enzymatic synthesis and
            utilization of alpha-5-phosphoribosylpyrophosphate.
  JOURNAL   J. Biol. Chem. 217 (1955) 885-895.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K00760  hypoxanthine phosphoribosyltransferase
GENES       HSA: 3251(HPRT1)
            MMU: 15452(Hprt1)
            RNO: 24465(Hprt)
            CFA: 442945(HPRT1)
            BTA: 281229(HPRT1)
            GGA: 395653(HPRT1) 776388(LOC776388)
            XLA: 446895(MGC80959)
            XTR: 394936(hprt1)
            DRE: 406259(hprt1)
            CEL: Y105E8B.5
            ATH: AT1G71750
            CME: CME008C
            DDI: DDB_0216388(hprT)
            PFA: PF10_0121
            TBR: Tb10.70.6650
            TCR: 506457.30 509693.70
            LMA: LmjF21.0845
            ECO: b0125(hpt)
            ECJ: JW5009(hpt)
            ECE: Z0136(hpt)
            ECS: ECs0129
            ECC: c0154(hpt)
            ECI: UTI89_C0138(hpt)
            ECP: ECP_0133
            ECV: APECO1_1860(hpt)
            ECW: EcE24377A_0127(hpt)
            ECX: EcHS_A0129(hpt)
            STY: STY0192(hpt)
            STT: t0175(hpt)
            SPT: SPA0173(hpt)
            SEC: SC0170(hpt)
            STM: STM0170(hpt)
            YPE: YPO3408(hpt)
            YPK: y0778(hpt)
            YPM: YP_0277(hpt)
            YPA: YPA_2910
            YPN: YPN_0680
            YPP: YPDSF_2947
            YPS: YPTB0723(hpt)
            YPI: YpsIP31758_3351(hpt)
            SFL: SF0122(hpt)
            SFX: S0124(hpt)
            SFV: SFV_0116(hpt)
            SSN: SSON_0133(hpt)
            SBO: SBO_0114(hpt)
            SDY: SDY_0034(hpt)
            ECA: ECA3328(hpt)
            PLU: plu0860 plu0864
            BUC: BU195(hpt)
            BAS: BUsg189(hpt)
            SGL: SG0482
            ENT: Ent638_0673
            SPE: Spro_3998
            HIT: NTHI1321(hpt)
            HDU: HD1399(hpt)
            HSO: HS_0463(hpt)
            PMU: PM0121(hpt)
            MSU: MS0683(hpt)
            APL: APL_0682(hpt)
            ASU: Asuc_0811
            XFA: XF2354
            XFT: PD1382(hpt)
            XCC: XCC1284(hpt)
            XCB: XC_2957
            XCV: XCV1387(hpt)
            XAC: XAC1335(hpt)
            XOO: XOO1868(hpt)
            XOM: XOO_1763(XOO1763)
            VCH: VC0585
            VCO: VC0395_A0117(hpt)
            VVU: VV1_1635 VV1_1636
            VVY: VV2769
            VPA: VP2515
            VFI: VF2176 VFA0019
            PPR: PBPRA3180
            PAE: PA4645
            PAU: PA14_61460(hpt)
            PPU: PP_0747
            PST: PSPTO_1131(hpt)
            PSB: Psyr_0970
            PSP: PSPPH_1019(hpt)
            PFL: PFL_5138
            PFO: Pfl_4727
            PEN: PSEEN0889
            PAR: Psyc_1125(hpt)
            PCR: Pcryo_1293
            ACI: ACIAD3669(hpt)
            SON: SO_3803(hpt-2)
            SDN: Sden_0654
            SFR: Sfri_3233
            SAZ: Sama_0771
            SBL: Sbal_0721
            SBM: Shew185_3590
            SLO: Shew_3142
            SPC: Sputcn32_0829
            SSE: Ssed_3910
            SPL: Spea_0688
            SHE: Shewmr4_3145
            SHM: Shewmr7_0822
            SHN: Shewana3_0793 Shewana3_3385
            SHW: Sputw3181_3344
            CPS: CPS_1752(hpt)
            PHA: PSHAa0609(hpt)
            SDE: Sde_1792
            MAQ: Maqu_3593
            CBU: CBU_1074
            LPN: lpg1519
            LPF: lpl1507(ppt)
            LPP: lpp1476(ppt)
            MCA: MCA1985
            FTU: FTT0205(hpt)
            FTF: FTF0205(hpt)
            FTW: FTW_1883(hpt)
            FTL: FTL_1931
            FTH: FTH_1851(hpt)
            FTA: FTA_2040(hpt)
            FTN: FTN_0179(hpt)
            NOC: Noc_0456
            AEH: Mlg_1328
            HCH: HCH_00775
            CSA: Csal_2065
            ABO: ABO_1020(hpt)
            AHA: AHA_3546(hpt)
            NME: NMB2047
            NMA: NMA0389(hpt)
            NMC: NMC2027(hpt)
            NGO: NGO2035
            CVI: CV_3900(hpt)
            RSO: RSc2812(hprT)
            REU: Reut_A2948
            REH: H16_A3242(hprT)
            RME: Rmet_3095
            BMA: BMA2515
            BXE: Bxe_A0515
            BUR: Bcep18194_A3674
            BCN: Bcen_0107
            BCH: Bcen2424_0589
            BAM: Bamb_0492
            BPS: BPSL2996
            BPM: BURPS1710b_3516
            BTE: BTH_I1148
            NMU: Nmul_A0649
            EBA: ebA3304
            AZO: azo3670(hpt)
            DAR: Daro_1736
            TBD: Tbd_0777
            MFA: Mfla_1280
            HPA: HPAG1_1114
            GSU: GSU1017
            GME: Gmet_2716
            GUR: Gura_3398
            PCA: Pcar_2547
            PPD: Ppro_3004
            DVU: DVU1588(hpt)
            DVL: Dvul_1545
            DDE: Dde_2112
            BBA: Bd0122(hprT) Bd3219(hpt)
            DPS: DP0449
            ADE: Adeh_0127
            AFW: Anae109_0131
            MXA: MXAN_5070(hpt)
            SAT: SYN_02450
            SFU: Sfum_1422
            MLO: mll3520
            MES: Meso_3093
            PLA: Plav_1597
            SME: SMc00719(hpt)
            SMD: Smed_2541
            ATU: Atu3604(hpt)
            ATC: AGR_L_2446
            RET: RHE_CH03800(hpt)
            RLE: RL4328(hprT)
            BME: BMEI0082
            BMF: BAB1_1986(hpt)
            BMS: BR1985(hpt)
            BMB: BruAb1_1961(hpt)
            BOV: BOV_1910(hpt)
            OAN: Oant_0995
            XAU: Xaut_0023
            CCR: CC_2214
            SIL: SPO2097(hpt)
            SIT: TM1040_1368
            RSP: RSP_2786(HPRT)
            RSH: Rsph17029_1428
            RSQ: Rsph17025_1044
            JAN: Jann_2230
            RDE: RD1_2771(hpt)
            HNE: HNE_3388(hpt)
            MGM: Mmc1_0665 Mmc1_3192
            ABA: Acid345_3058
            SUS: Acid_0128 Acid_5665
            BSU: BG10131(hprT)
            BHA: BH0084(hprT)
            BAN: BA0063(hpt-1) BA5074(hpt-2)
            BAR: GBAA0063(hpt-1) GBAA5074(hpt-2)
            BAA: BA_0653 BA_5491
            BAT: BAS0063 BAS4712
            BCE: BC0071 BC4815
            BCA: BCE_0062(hpt) BCE_4975(hpt)
            BCZ: BCZK0059(hprT) BCZK0244 BCZK4569(hpt)
            BCY: Bcer98_0059 Bcer98_3479
            BTK: BT9727_0059(hprT) BT9727_4551(hpt)
            BTL: BALH_0062(hpt) BALH_4389(hpt)
            BLI: BL05003(hprT)
            BLD: BLi00084(hprT)
            BCL: ABC0105(hprT)
            BAY: RBAM_000790(hprT)
            BPU: BPUM_0052(hprT)
            OIH: OB0078
            GKA: GK0061
            GTN: GTNG_0061
            SAU: SA0468
            SAV: SAV0510
            SAM: MW0465
            SAR: SAR0511(hpt)
            SAS: SAS0467
            SAC: SACOL0554(hpt)
            SAB: SAB0459(hpt)
            SAA: SAUSA300_0488(hpt)
            SAO: SAOUHSC_00485
            SAJ: SaurJH9_0532
            SAH: SaurJH1_0545
            SEP: SE2273
            SER: SERP0149(hpt)
            SHA: SH2501
            SSP: SSP2246
            LLA: L160442(hprT) L25115(hpt)
            LLC: LACR_0017 LACR_1606
            LLM: llmg_0020(hpt) llmg_0993(hprT)
            SPZ: M5005_Spy_0012
            SPM: spyM18_0013(hpt)
            SPG: SpyM3_0011(hpt)
            SPS: SPs0012
            SPH: MGAS10270_Spy0012
            SPI: MGAS10750_Spy0012
            SPJ: MGAS2096_Spy0012
            SPK: MGAS9429_Spy0012
            SPF: SpyM50012(hpt)
            SPA: M6_Spy0012
            SPB: M28_Spy0012(hpt)
            SPN: SP_0012
            SPR: spr0011(hgt)
            SPD: SPD_0012(hpt)
            SAG: SAG0015(hpt)
            SAN: gbs0014
            SAK: SAK_0014(hpt)
            SMU: SMU.14(hprT)
            STC: str0011(hpt)
            STL: stu0011(hpt)
            STE: STER_0013
            SSA: SSA_0014(hpt)
            SSU: SSU05_0014
            SSV: SSU98_0017
            SGO: SGO_2134(hpt)
            LPL: lp_0546(hprT)
            LJO: LJ0689 LJ0808
            LAC: LBA0613(hprT)
            LSA: LSA1598(hpt)
            LSL: LSL_1354(hpt)
            LDB: Ldb0538(hprT)
            LBU: LBUL_0480
            LBR: LVIS_0522
            LCA: LSEI_2541
            LGA: LGAS_0472 LGAS_0566
            LRE: Lreu_0267 Lreu_1925
            PPE: PEPE_1546
            EFA: EF0264(hpt)
            OOE: OEOE_0187
            LME: LEUM_0403
            STH: STH500
            CAC: CAC3203(hprT)
            CPE: CPE1960(hprT) CPE2471(hprT)
            CPF: CPF_2216(hpt) CPF_2787(hpt)
            CPR: CPR_1928(hpt) CPR_2473(hpt)
            CTC: CTC00203 CTC02240
            CNO: NT01CX_1039 NT01CX_1811
            CTH: Cthe_2254
            CDF: CD2691(hpt) CD3231(hpt)
            CBO: CBO3081(hpt) CBO3525(hpt)
            CBA: CLB_3110(hpt-1) CLB_3600(hpt-2)
            CBH: CLC_2983(hpt-1) CLC_3489(hpt-2)
            CBF: CLI_3140(hpt-1) CLI_3734(hpt-2)
            CBE: Cbei_0099 Cbei_4228
            CKL: CKL_0171(hpt)
            AMT: Amet_1621 Amet_2903
            CHY: CHY_1067(hpt)
            DSY: DSY3939
            DRM: Dred_2376
            SWO: Swol_1785
            CSC: Csac_1209
            TTE: TTE2394(hpt)
            MTA: Moth_2106
            MGE: MG_458(hpt)
            MPN: MPN672(hpt)
            MPU: MYPU_5510(hpt)
            MPE: MYPE10260(hpt) MYPE5810(htp)
            MGA: MGA_0658(hpt)
            MMY: MSC_0256(hpt) MSC_0848(hpt)
            MMO: MMOB4340(hpt)
            MHY: mhp117(hpt)
            MHJ: MHJ_0254(hpt)
            MHP: MHP7448_0262(hpt)
            MSY: MS53_0381(hpt)
            MCP: MCAP_0216(hpt1) MCAP_0765(hpt2)
            UUR: UU104(hpt)
            MFL: Mfl463
            MTU: Rv3624c(hpt)
            MTC: MT3726(hpt)
            MBO: Mb3648c(hpt)
            MBB: BCG_3682c(hpt)
            MLE: ML0214(hpt)
            MPA: MAP0439(hpt)
            MAV: MAV_0532(hpt)
            MSM: MSMEG_6110(hpt)
            MVA: Mvan_5377
            MGI: Mflv_1412
            MMC: Mmcs_4775
            MKM: Mkms_4861
            MJL: Mjls_5161
            CGL: NCgl2604(cgl2697)
            CGB: cg2985(hpt)
            CEF: CE2543
            CDI: DIP2003(hpt)
            CJK: jk0277(hpt)
            NFA: nfa3890(hpt)
            RHA: RHA1_ro04404(hpt)
            SCO: SCO3405(hprT)
            SMA: SAV4665(hprT)
            TWH: TWT589(hpt)
            TWS: TW172(hpt)
            LXX: Lxx21510(hpt)
            ART: Arth_0150
            AAU: AAur_0134(hpt)
            PAC: PPA0259
            NCA: Noca_0443
            TFU: Tfu_2896
            FRA: Francci3_4313
            FAL: FRAAL6587(hpt)
            ACE: Acel_0203
            KRA: Krad_0530
            SEN: SACE_0395(hpt)
            STP: Strop_4309
            BLO: BL1681(hprT)
            BAD: BAD_0408(hprT)
            RXY: Rxyl_2186 Rxyl_2835
            FNU: FN0288
            RBA: RB6524(hpt)
            LIL: LA4295
            LIC: LIC13438(hpt)
            LBJ: LBJ_2933(hpt)
            LBL: LBL_0130(hpt)
            GVI: glr2790
            BTH: BT_4386
            BFR: BF1119
            BFS: BF1031
            PGI: PG0792(hpt)
            SRU: SRU_1710(hpt)
            FJO: Fjoh_0421
            FPS: FP1360(hpt)
            CTE: CT1527(gpt)
            CPH: Cpha266_1917
            PLT: Plut_1525
            DET: DET0749(hpt-1) DET0792(hpt-2)
            DEH: cbdb_A722(hpt) cbdb_A770(hpt)
            DEB: DehaBAV1_0677 DehaBAV1_0718
            RRS: RoseRS_0321
            RCA: Rcas_0865
            DRA: DR_1376
            DGE: Dgeo_1588
            TTH: TTC1766
            TTJ: TTHA0220
            AAE: aq_544(hpt)
            TMA: TM0206
            TPT: Tpet_0718
            TME: Tmel_1560
            FNO: Fnod_1773
            MMP: MMP0145(hpt)
STRUCTURES  PDB: 1BZY  1CJB  1D6N  1DQN  1DQP  1FSG  1G9S  1G9T  1GRV  1HGX  
                 1HMP  1I0I  1I0L  1I13  1I14  1J7J  1P17  1P18  1P19  1PZM  
                 1QK3  1QK4  1QK5  1R3U  1TC1  1TC2  1YFZ  1Z7G  2GEB  2JBH  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.8
            ExPASy - ENZYME nomenclature database: 2.4.2.8
            ExplorEnz - The Enzyme Database: 2.4.2.8
            ERGO genome analysis and discovery system: 2.4.2.8
            BRENDA, the Enzyme Database: 2.4.2.8
            CAS: 9016-12-0
///
ENTRY       EC 2.4.2.9                  Enzyme
NAME        uracil phosphoribosyltransferase;
            UMP pyrophosphorylase;
            UPRTase;
            UMP:pyrophosphate phosphoribosyltransferase;
            uridine 5'-phosphate pyrophosphorylase;
            uridine monophosphate pyrophosphorylase;
            uridylate pyrophosphorylase;
            uridylic pyrophosphorylase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     UMP:diphosphate phospho-alpha-D-ribosyltransferase
REACTION    UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate
            [RN:R00966]
ALL_REAC    R00966
SUBSTRATE   UMP [CPD:C00105];
            diphosphate [CPD:C00013]
PRODUCT     uracil [CPD:C00106];
            5-phospho-alpha-D-ribose 1-diphosphate [CPD:C00119]
REFERENCE   1
  AUTHORS   Crawford, I., Kornberg, A. and Simms, E.S.
  TITLE     Conversion of uracil and orotate to uridine 5'-phosphate by enzymes
            in lactobacilli.
  JOURNAL   J. Biol. Chem. 226 (1967) 1093-1101.
REFERENCE   2
  AUTHORS   Flaks, J.G.
  TITLE     Nucleotide synthesis from 5-phosphoribosylpyrophosphate.
  JOURNAL   Methods Enzymol. 6 (1963) 136-158.
  ORGANISM  Lactobacillus bifidus, Escherichia coli [GN:eco]
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K00761  uracil phosphoribosyltransferase
            KO: K02825  pyrimidine operon attenuation protein / uracil
                        phosphoribosyltransferase
GENES       HSA: 139596(UPRT)
            BTA: 540851(LOC540851)
            GGA: 422327(RCJMB04_25k2)
            DRE: 404623(zgc:77421)
            SPU: 575128(LOC575128)
            ATH: AT3G53900
            OSA: 4338981
            CME: CML265C
            SCE: YHR128W(FUR1)
            AGO: AGOS_AFR052C
            PIC: PICST_47473(FUR1)
            CGR: CAGL0H09064g
            SPO: SPAC1002.17c SPAC1399.04c SPAC1B3.01c
            ANI: AN2133.2 AN8869.2
            AFM: AFUA_2G16200 AFUA_5G05460
            AOR: AO090009000714 AO090102000246
            ANG: An15g06580(furA)
            CNE: CNE02040 CNE02100
            UMA: UM00093.1 UM03873.1
            DDI: DDB_0230206
            CPV: cgd1_1900
            CHO: Chro.10216
            TET: TTHERM_00388550
            TBR: Tb927.4.3320
            TCR: 506435.410 507739.40
            LMA: LmjF34.1040
            ECO: b2498(upp)
            ECJ: JW2483(upp)
            ECE: Z3761(upp)
            ECS: ECs3360
            ECC: c3015(upp)
            ECI: UTI89_C2814(upp)
            ECP: ECP_2500
            ECV: APECO1_4071(upp)
            ECW: EcE24377A_2781(upp)
            ECX: EcHS_A2633(upp)
            STY: STY2739(upp)
            STT: t0359(upp)
            SPT: SPA0369(upp)
            SEC: SC2495(upp)
            STM: STM2498(upp)
            YPE: YPO2827(upp)
            YPK: y1408(upp)
            YPM: YP_2695(upp)
            YPA: YPA_2264
            YPN: YPN_1311
            YPS: YPTB2794(upp)
            YPI: YpsIP31758_1235(upp)
            SFL: SF2542(upp)
            SFX: S2691(upp)
            SFV: SFV_2543(upp)
            SSN: SSON_2580(upp)
            SBO: SBO_2519(upp)
            SDY: SDY_2687(upp)
            ECA: ECA1255(upp)
            PLU: plu2759(upp)
            SGL: SG1731
            SPE: Spro_3523
            BFL: Bfl520(upp)
            BPN: BPEN_538(upp)
            HIN: HI0459(pyrR)
            HIT: NTHI0589(pyrR) NTHI1940(upp)
            HIP: CGSHiEE_00705 CGSHiEE_03875(upp)
            HIQ: CGSHiGG_01870(upp) CGSHiGG_05535
            HDU: HD1178(upp) HD1181(pyrR)
            HSO: HS_1341(upp) HS_1561(pyrR)
            PMU: PM0019(upp) PM1207(pyrR)
            MSU: MS0628(pyrR) MS1880(upp)
            APL: APL_0398(upp) APL_0401(pyrR)
            ASU: Asuc_0731 Asuc_1771
            XCC: XCC2386(upp)
            XCB: XC_1728
            XCV: XCV2703(upp)
            XAC: XAC2521(upp)
            XOO: XOO2501(upp)
            XOM: XOO_2365(XOO2365)
            VCH: VC2225
            VCO: VC0395_A1818(upp)
            VVU: VV1_1901
            VVY: VV2514
            VPA: VP2284
            VFI: VF1927
            PPR: PBPRA2909
            PAE: PA0403(pyrR) PA4646(upp)
            PAU: PA14_05270(pyrR) PA14_61470(upp)
            PAP: PSPA7_5295(upp)
            PPU: PP_0746(upp) PP_4997(pyrR)
            PPF: Pput_4871
            PST: PSPTO_1130(upp) PSPTO_5039(pyrR)
            PSB: Psyr_0483 Psyr_0969
            PSP: PSPPH_0474(pyrR) PSPPH_1018(upp)
            PFL: PFL_5139(upp) PFL_5832
            PFO: Pfl_4728 Pfl_5313
            PEN: PSEEN0888(upp) PSEEN5060
            PMY: Pmen_0398
            PAR: Psyc_1967(upp)
            PCR: Pcryo_2263
            ACI: ACIAD0744(upp)
            SON: SO_2759(upp)
            SDN: Sden_2093
            SFR: Sfri_1453
            SAZ: Sama_2096
            SBM: Shew185_1731
            SSE: Ssed_1846
            SPL: Spea_2576
            SHE: Shewmr4_2379
            SHM: Shewmr7_2451
            SHN: Shewana3_2544
            CPS: CPS_4319(upp)
            PHA: PSHAb0377(upp)
            PAT: Patl_0086
            MAQ: Maqu_1979
            LPN: lpg2243
            LPF: lpl2168(upp)
            LPP: lpp2196(upp) lpp2199
            MCA: MCA2334
            FTU: FTT0716(upp)
            FTF: FTF0716(upp)
            FTW: FTW_1524(upp)
            FTL: FTL_1520
            FTH: FTH_1470(upp)
            FTA: FTA_1604(upp)
            FTN: FTN_0628(upp)
            NOC: Noc_0366
            AEH: Mlg_0347
            HCH: HCH_00552 HCH_01088(upp)
            CSA: Csal_2095
            ABO: ABO_0036(pyrR) ABO_1991(upp)
            AHA: AHA_2820(upp)
            DNO: DNO_0586(upp)
            NME: NMB0774
            NMA: NMA0985(upp)
            NGO: NGO0353
            CVI: CV_3621(upp)
            RSO: RSc0677(pyrR) RSc2188(upp)
            REU: Reut_A0707 Reut_A2519 Reut_B3987
            REH: H16_A0918(upp1) H16_A2914 H16_B1595(upp2)
            RME: Rmet_0788 Rmet_2741 Rmet_4570
            BMA: BMA1883(upp) BMA1995(pyrR)
            BMV: BMASAVP1_A0918(pyrR) BMASAVP1_A1077(upp)
            BML: BMA10299_A0790(upp) BMA10299_A2748(pyrR)
            BMN: BMA10247_0360(upp) BMA10247_1857(pyrR)
            BXE: Bxe_A3258 Bxe_A3809
            BUR: Bcep18194_A3964 Bcep18194_A5620
            BCN: Bcen_1681
            BCH: Bcen2424_2293
            BAM: Bamb_0739 Bamb_2331
            BPS: BPSL1166(upp) BPSL2691(pyrR)
            BPM: BURPS1710b_1387(upp) BURPS1710b_3168(pyrR)
            BPL: BURPS1106A_1242(upp) BURPS1106A_3146(pyrR)
            BPD: BURPS668_1233(upp) BURPS668_3110(pyrR)
            BTE: BTH_I1016(upp) BTH_I1464(pyrR)
            BPE: BP1052(upp)
            BPA: BPP1149(upp)
            BBR: BB1365(upp)
            RFR: Rfer_1379 Rfer_2073
            POL: Bpro_1144 Bpro_1963
            MPT: Mpe_A0707 Mpe_A1818
            HAR: HEAR2738(pyrR)
            MMS: mma_2948 mma_3567
            NEU: NE1666(pyrR)
            NET: Neut_0450
            NMU: Nmul_A2480
            EBA: ebA1757(pyrR)
            AZO: azo3767(upp)
            DAR: Daro_3891
            TBD: Tbd_2581
            MFA: Mfla_2101
            WSU: WS1653
            CJE: Cj1286c(upp)
            CJR: CJE1478(upp)
            CJJ: CJJ81176_1303(upp)
            CJU: C8J_1229(upp)
            CFF: CFF8240_1559(upp)
            CCV: CCV52592_0546(upp)
            CCO: CCC13826_0240(upp) CCC13826_1941
            NIS: NIS_1764(upp)
            SUN: SUN_1102(upp)
            GSU: GSU0933(upp) GSU1270(pyrR)
            GME: Gmet_1768
            GUR: Gura_1855
            PCA: Pcar_1616(pyrR)
            PPD: Ppro_2530
            DVU: DVU1025(upp) DVU1384(pyrR)
            DVL: Dvul_1686
            DDE: Dde_1448 Dde_2016
            LIP: LI0015(upp)
            BBA: Bd1531(upp)
            DPS: DP0672 DP1616
            ADE: Adeh_1617
            MXA: MXAN_0124(upp)
            SAT: SYN_03702
            SFU: Sfum_1064
            MLO: mll3162
            MES: Meso_3658
            SME: SMc04121(upp)
            SMD: Smed_3343
            ATU: Atu0135(upp)
            ATC: AGR_C_216
            RET: RHE_CH00196(upp)
            RLE: RL0205(upp)
            BME: BMEII0232
            BMF: BAB2_1027
            BMS: BRA1067(upp)
            BMB: BruAb2_1007(upp)
            BOV: BOV_A1005(upp)
            OAN: Oant_1316
            BJA: blr6788(upp) blr7239(upp)
            BRA: BRADO1786(upp) BRADO3518(upp)
            BBT: BBta_2102(upp) BBta_4197(upp)
            CCR: CC_2268
            SIL: SPO2926(upp)
            SIT: TM1040_1569
            RSP: RSP_1598
            RSQ: Rsph17025_0279
            JAN: Jann_2983
            RDE: RD1_3976(upp)
            GOX: GOX0327
            GBE: GbCGDNIH1_2367
            RRU: Rru_A2255
            MGM: Mmc1_0104
            ABA: Acid345_4568
            SUS: Acid_5511
            BSU: BG10712(pyrR) BG10945(upp)
            BHA: BH2541(pyrR) BH3764(upp)
            BAN: BA4030(pyrR) BA5557(upp)
            BAR: GBAA4030(pyrR) GBAA5557(upp)
            BAA: BA_0411 BA_4501
            BAT: BAS3742 BAS5164
            BCE: BC3891 BC5315
            BCA: BCE_3936(pyrR) BCE_5440(upp)
            BCZ: BCZK3650(upp) BCZK5014(upp)
            BCY: Bcer98_2540 Bcer98_3834
            BTK: BT9727_3633(upp) BT9727_4997(upp)
            BTL: BALH_4815(upp)
            BLI: BL02271(pyrR) BL03992(upp)
            BLD: BLi01767(pyrR) BLi03934(upp)
            BCL: ABC2338(pyrR) ABC3862(upp)
            BAY: RBAM_015300 RBAM_034050(upp)
            BPU: BPUM_1446 BPUM_3334(upp)
            OIH: OB1487(pyrR) OB2984(upp)
            GKA: GK1147 GK3368
            SAU: SA1041(pyrR) SA1914(upp)
            SAV: SAV1198(pyrR) SAV2112(upp)
            SAM: MW1081(pyrR) MW2036(upp)
            SAR: SAR1174(pyrR) SAR2200(upp)
            SAS: SAS1132 SAS2015
            SAC: SACOL1210(pyrR) SACOL2104(upp)
            SAB: SAB1062(pyrR) SAB1996c(upp)
            SAA: SAUSA300_1091(pyrR) SAUSA300_2066(upp)
            SAO: SAOUHSC_01164 SAOUHSC_02353
            SAJ: SaurJH9_1257 SaurJH9_2148
            SAH: SaurJH1_1282 SaurJH1_2186
            SEP: SE0873 SE1709
            SER: SERP0764(pyrR) SERP1718(upp)
            SHA: SH0923(upp) SH1716(pyrR)
            SSP: SSP0772 SSP1574
            LMO: lmo1840(pyrR) lmo2538(upp)
            LMF: LMOf2365_1868 LMOf2365_2511(upp)
            LIN: lin1954(pyrR) lin2682(upp)
            LWE: lwe1859(pyrR) lwe1860(pyrR) lwe2487(upp)
            LLA: L0227(pyrR) L175538(upp)
            LLC: LACR_1712 LACR_2185
            LLM: llmg_0890(pyrR) llmg_2176(upp)
            SPY: SPy_0392(upp) SPy_0830(pyrR)
            SPZ: M5005_Spy_0327(upp) M5005_Spy_0639(pyrR)
            SPM: spyM18_0443(upp) spyM18_0890(pyrR)
            SPG: SpyM3_0286(upp) SpyM3_0558(pyrR)
            SPS: SPs1296 SPs1573
            SPH: MGAS10270_Spy0322(upp) MGAS10270_Spy0697(pyrR)
            SPI: MGAS10750_Spy0323(upp) MGAS10750_Spy0728(pyrR)
            SPJ: MGAS2096_Spy0345 MGAS2096_Spy0346(upp) MGAS2096_Spy0706(pyrR)
            SPK: MGAS9429_Spy0326(upp) MGAS9429_Spy0694(pyrR)
            SPF: SpyM51168(pyrR) SpyM51531(upp)
            SPA: M6_Spy0353 M6_Spy0657(pyrR)
            SPB: M28_Spy0316(upp) M28_Spy0619(pyrR)
            SPN: SP_0745 SP_1278
            SPR: spr0655(upp) spr1156(pyrR)
            SPD: SPD_0649(upp) SPD_1134(pyrR)
            SAG: SAG1364(pyrR) SAG1586(upp)
            SAN: gbs1434 gbs1635(upp)
            SAK: SAK_1397(pyrR) SAK_1601(upp)
            SMU: SMU.1673(upp) SMU.856(pyrR)
            STC: str0355(upp) str0523(pyrR)
            STL: stu0355(upp) stu0523(pyrR)
            STE: STER_0555
            SSA: SSA_1345(pyrR) SSA_1732(upp)
            SGO: SGO_1102 SGO_1107 SGO_1633(upp)
            LPL: lp_1782(pyrR2) lp_2374(upp) lp_2704(pyrR1)
            LJO: LJ0933 LJ1275 LJ1280
            LAC: LBA0563(pyrR) LBA0770 LBA1383(pyrR)
            LSA: LSA0950(pyrR) LSA1133(upp)
            LSL: LSL_0593(upp) LSL_0827(pyrR)
            LDB: Ldb0704(upp) Ldb1638(pyrR2) Ldb2113(pyrR1)
            LBU: LBUL_0636 LBUL_1518 LBUL_1954
            LBR: LVIS_0831 LVIS_1286
            LCA: LSEI_1159 LSEI_1457
            LGA: LGAS_1091
            LRE: Lreu_0071 Lreu_0456
            PPE: PEPE_0942
            EFA: EF1721(pyrR) EF2549(upp)
            OOE: OEOE_1579
            LME: LEUM_1372
            STH: STH1256 STH79(upp)
            CAC: CAC2113(pyrR) CAC2879(upp)
            CPE: CPE1849 CPE2197(upp)
            CPF: CPF_2103(pyrR) CPF_2462(upp)
            CPR: CPR_1817(pyrR) CPR_2172(upp)
            CTC: CTC00308(upp) CTC01613(pyrR)
            CNO: NT01CX_0542 NT01CX_1953
            CTH: Cthe_0954
            CDF: CD2595(pyrR) CD3479(upp)
            CBO: CBO0145(upp) CBO1478(pyrR) CBO2821(pyrR)
            CBA: CLB_0181(upp) CLB_1502(pyrR-1) CLB_2764(pyrR-2)
            CBH: CLC_0193(upp) CLC_1514(pyrR-1) CLC_2697(pyrR-2)
            CBF: CLI_0200(upp) CLI_1561(pyrR-1) CLI_2870(pyrR-2)
            CBE: Cbei_0408 Cbei_1596
            CKL: CKL_3702(upp)
            AMT: Amet_2795
            CHY: CHY_1503(pyrR)
            DSY: DSY2863 DSY4926
            DRM: Dred_1680
            SWO: Swol_1285
            CSC: Csac_1201 Csac_1929
            TTE: TTE0147(upp) TTE1536(pyrR)
            MTA: Moth_0878
            MGE: MG_030(upp)
            MPN: MPN033(upp)
            MPU: MYPU_3150(upp)
            MPE: MYPE10300(upp) MYPE7900(pyrR)
            MGA: MGA_1159(upp)
            MMY: MSC_0893(upp)
            MMO: MMOB5380(upp)
            MHY: mhp543(upp)
            MHJ: MHJ_0527(upp)
            MHP: MHP7448_0526(upp)
            MSY: MS53_0309(upp)
            MCP: MCAP_0076(upp)
            UUR: UU116(upp)
            MFL: Mfl107
            MTU: Rv1379(pyrR) Rv3309c(upp)
            MTC: MT1423(pyrR) MT3408(upp)
            MBO: Mb1414(pyrR) Mb3337c(upp)
            MBB: BCG_3374c(upp)
            MPA: MAP1114(pyrR) MAP3431c(upp)
            MAV: MAV_3394 MAV_4285
            MSM: MSMEG_1694(upp) MSMEG_3042 MSMEG_3473(upp)
            MVA: Mvan_2659
            MGI: Mflv_3748
            MMC: Mmcs_1240 Mmcs_2362 Mmcs_5192
            MKM: Mkms_2409
            MJL: Mjls_2403
            CGL: NCgl0654(cgl0684) NCgl1551(cgl1613)
            CGB: cg0786(upp) cg1817(pyrR)
            CEF: CE0704 CE1733
            CDI: DIP0642(upp) DIP1335(pyrR)
            CJK: jk1026(pyrR) jk1676(upp)
            NFA: nfa36240(pyrR) nfa9590(upp)
            RHA: RHA1_ro00256 RHA1_ro06255 RHA1_ro07147
            SCO: SCO1488(pyrR) SCO4041(2SCD60.07)
            SMA: SAV4178(uraP) SAV6862(pyrR)
            LXX: Lxx01650(upp) Lxx11050
            CMI: CMM_1787(pyrR)
            ART: Arth_2267
            AAU: AAur_0795(upp) AAur_2270(pyrR)
            PAC: PPA0995 PPA2184
            NCA: Noca_2427
            TFU: Tfu_1053
            FRA: Francci3_0689 Francci3_3203
            FAL: FRAAL1198(upp) FRAAL5239(pyrR)
            ACE: Acel_1302
            KRA: Krad_3006
            SEN: SACE_2078 SACE_6559(upp)
            BLO: BL1254(upp)
            BAD: BAD_0124(upp)
            RXY: Rxyl_1481 Rxyl_1648
            FNU: FN0418(pyrR) FN0483
            RBA: RB10188(upp)
            CMU: TC0833
            TPA: TP0448
            TDE: TDE1612
            SYN: sll0368(pyrR) sll1035(upp)
            SYW: SYNW0520(pyrR) SYNW1125
            SYC: syc0234_c syc2376_d(upp)
            SYF: Synpcc7942_1319 Synpcc7942_1715
            SYD: Syncc9605_1262 Syncc9605_2163
            SYE: Syncc9902_0514 Syncc9902_1220
            SYG: sync_1694(upp) sync_2275(pyrR)
            SYR: SynRCC307_1246(upp) SynRCC307_1856(pyrR)
            SYX: SynWH7803_1133(upp)
            CYA: CYA_0406(pyrR) CYA_1803(upp)
            CYB: CYB_1933(upp-1) CYB_2389(upp-2) CYB_2433(pyrR)
            TEL: tll2320 tlr1764
            GVI: gll0063 glr0827
            ANA: all2063 alr2083
            AVA: Ava_3111 Ava_3128
            PMA: Pro0849(upp) Pro1586(pyrR)
            PMM: PMM0776 PMM1433
            PMT: PMT0558 PMT1445
            PMN: PMN2A_0182
            PMI: PMT9312_0784 PMT9312_1526
            PMB: A9601_08381(upp) A9601_16351(pyrR)
            PMC: P9515_08071(upp) P9515_16111(pyrR)
            PMF: P9303_05091(pyrR) P9303_16941(upp)
            PMG: P9301_08361(upp) P9301_16231(pyrR)
            PMH: P9215_08701(upp)
            PME: NATL1_08141(upp)
            TER: Tery_1858 Tery_2191
            BTH: BT_2791
            BFR: BF4445
            BFS: BF4243
            PGI: PG0752
            SRU: SRU_1287(upp) SRU_1335 SRU_2693
            CHU: CHU_0083(pyrR) CHU_0488(pyrR)
            GFO: GFO_1565(upp)
            FPS: FP1442(pyrR2) FP1796(pyrR1) FP2471(upp)
            DET: DET1198(pyrR)
            DEH: cbdb_A1112(pyrR)
            RRS: RoseRS_2864
            RCA: Rcas_2433
            DRA: DR_1110(pyrR) DR_1563
            DGE: Dgeo_0504 Dgeo_1296
            TTH: TTC0428(pyrR) TTC0946
            TTJ: TTHA0783 TTHA1312
            AAE: aq_2163(uraP)
            TMA: TM0721
            TME: Tmel_1418
            MMP: MMP0680
            MTH: MTH1114
            MSI: Msm_0398
            HAL: VNG2305C
            HMA: rrnAC2577(upp)
            HWA: HQ1029A(upp)
            NPH: NP1408A(upp)
            PAB: PAB1839
            PFU: PF1241
            TKO: TK1287
            APE: APE_0545.1
            SSO: SSO0231(upp)
            STO: ST0281
            SAI: Saci_0699
            PAI: PAE1598
STRUCTURES  PDB: 1BD3  1BD4  1I5E  1JLR  1JLS  1NON  1O5O  1UPF  1UPU  1V9S  
                 1W30  1XTT  1XTU  1XTV  1XZ8  1XZN  2IGB  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.9
            ExPASy - ENZYME nomenclature database: 2.4.2.9
            ExplorEnz - The Enzyme Database: 2.4.2.9
            ERGO genome analysis and discovery system: 2.4.2.9
            BRENDA, the Enzyme Database: 2.4.2.9
            CAS: 9030-24-4
///
ENTRY       EC 2.4.2.10                 Enzyme
NAME        orotate phosphoribosyltransferase;
            orotidylic acid phosphorylase;
            orotidine-5'-phosphate pyrophosphorylase;
            OPRTase;
            orotate phosphoribosyl pyrophosphate transferase;
            orotic acid phosphoribosyltransferase;
            orotidine 5'-monophosphate pyrophosphorylase;
            orotidine monophosphate pyrophosphorylase;
            orotidine phosphoribosyltransferase;
            orotidylate phosphoribosyltransferase;
            orotidylate pyrophosphorylase;
            orotidylic acid pyrophosphorylase;
            orotidylic phosphorylase;
            orotidylic pyrophosphorylase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     orotidine-5'-phosphate:diphosphate
            phospho-alpha-D-ribosyl-transferase
REACTION    orotidine 5'-phosphate + diphosphate = orotate +
            5-phospho-alpha-D-ribose 1-diphosphate [RN:R01870]
ALL_REAC    R01870
SUBSTRATE   orotidine 5'-phosphate [CPD:C01103];
            diphosphate [CPD:C00013]
PRODUCT     orotate [CPD:C00295];
            5-phospho-alpha-D-ribose 1-diphosphate [CPD:C00119]
COMMENT     The enzyme from higher eukaryotes also catalyses the reaction listed
            as EC 4.1.1.23, orotidine-5'-phosphate decarboxylase.
REFERENCE   1  [PMID:692383]
  AUTHORS   Jones ME, Kavipurapu PR, Traut TW.
  TITLE     Orotate phosphoribosyltransferase: orotidylate decarboxylase
            (Ehrlich ascites cell).
  JOURNAL   Methods. Enzymol. 51 (1978) 155-67.
REFERENCE   2  [PMID:14392174]
  AUTHORS   LIEBERMAN I, KORNBERG A, SIMMS ES.
  TITLE     Enzymatic synthesis of pyrimidine nucleotides;
            orotidine-5'-phosphate and uridine-5'-phosphate.
  JOURNAL   J. Biol. Chem. 215 (1955) 403-51.
REFERENCE   3  [PMID:6893554]
  AUTHORS   McClard RW, Black MJ, Livingstone LR, Jones ME.
  TITLE     Isolation and initial characterization of the single polypeptide
            that synthesizes uridine 5'-monophosphate from orotate in Ehrlich
            ascites carcinoma. Purification by tandem affinity chromatography of
            uridine-5'-monophosphate synthase.
  JOURNAL   Biochemistry. 19 (1980) 4699-706.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K00762  orotate phosphoribosyltransferase
GENES       HSA: 7372(UMPS)
            MMU: 22247(Umps)
            RNO: 288051(Umps)
            CFA: 478593(UMPS)
            BTA: 281568(UMPS)
            GGA: 424256(RCJMB04_1g10)
            XLA: 494728(LOC494728)
            DME: Dmel_CG3593(r-l)
            CEL: R12E2.11 T07C4.1
            ATH: AT3G54470
            OSA: 4325739 4325740
            CME: CMK046C
            SCE: YML106W(URA5) YMR271C(URA10)
            AGO: AGOS_AER290C
            PIC: PICST_90848(URA5)
            CGR: CAGL0J06600g
            SPO: SPBC725.15
            ANI: AN5884.2
            AFM: AFUA_2G11290
            AOR: AO090026000521
            CNE: CNG03730
            DDI: DDB_0214958(pyr56)
            PFA: PFE0630c
            TAN: TA19940
            TPV: TP01_0073
            TBR: Tb927.5.3810
            TCR: 507059.60 509899.110
            LMA: LmjF16.0550
            ECO: b3642(pyrE)
            ECJ: JW3617(pyrE)
            ECE: Z5066(pyrE)
            ECS: ECs4517
            ECC: c4466(pyrE)
            ECI: UTI89_C4186(pyrE)
            ECP: ECP_3740
            ECV: APECO1_2819(pyrE)
            ECW: EcE24377A_4143(pyrE)
            ECX: EcHS_A3851
            STY: STY4061(pyrE)
            STT: t3785(pyrE)
            SPT: SPA3585(pyrE)
            SEC: SC3656(pyrE)
            STM: STM3733(pyrE)
            YPE: YPO0045(pyrE)
            YPK: y0096(pyrE)
            YPM: YP_0046(pyrE)
            YPA: YPA_3497
            YPN: YPN_3805
            YPP: YPDSF_3860
            YPS: YPTB0042(pyrE)
            YPI: YpsIP31758_0057(pyrE)
            YEN: YE0059(pyrE)
            SFL: SF3681(pyrE)
            SFX: S4087(pyrE)
            SFV: SFV_3888(pyrE)
            SSN: SSON_3764(pyrE)
            SBO: SBO_3644(pyrE)
            SDY: SDY_4073(pyrE)
            ECA: ECA0141(pyrE)
            PLU: plu4869(pyrE)
            BUC: BU559(pyrE)
            BAB: bbp506(pyrE)
            WBR: WGLp400(pyrE)
            SGL: SG2212
            ENT: Ent638_0097
            SPE: Spro_4846
            HIN: HI0272(pyrE)
            HIT: NTHI0380(pyrE)
            HIP: CGSHiEE_01690(pyrE)
            HDU: HD1759(pryE)
            PMU: PM1877(pyrE)
            MSU: MS0251(pyrE)
            APL: APL_0318(pryE)
            ASU: Asuc_0421
            XFA: XF0153
            XFT: PD0122(pyrE)
            XCC: XCC3847(pyrE)
            XCB: XC_3931
            XCV: XCV4016(pyrE)
            XAC: XAC3903(pyrE)
            XOO: XOO0508(pyrE)
            XOM: XOO_0474(XOO0474)
            VCH: VC0211
            VCO: VC0395_A2590(pyrE)
            VVU: VV1_0831
            VVY: VV0280
            VPA: VP0178
            VFI: VF0112(pyrE)
            PPR: PBPRA0199
            PAE: PA5331(pyrE)
            PAU: PA14_70370(pyrE)
            PPU: PP_5291(pyrE)
            PPF: Pput_5199
            PST: PSPTO_0080(pyrE)
            PSB: Psyr_0216(pyrE)
            PSP: PSPPH_0204(pyrE)
            PFL: PFL_6056(pyrE)
            PFO: Pfl_5544(pyrE)
            PEN: PSEEN5436(pyrE)
            PMY: Pmen_4383
            PAR: Psyc_1753(pyrE)
            PCR: Pcryo_2034
            PRW: PsycPRwf_0521
            ACI: ACIAD3525(pyrE)
            ACB: A1S_3340
            SON: SO_4255(pyrE)
            SDN: Sden_0320
            SFR: Sfri_3835
            SAZ: Sama_0321
            SBL: Sbal_0371
            SBM: Shew185_0370
            SLO: Shew_3487
            SPC: Sputcn32_0457
            SSE: Ssed_0379
            SPL: Spea_3843
            SHE: Shewmr4_3603
            SHM: Shewmr7_0353
            SHN: Shewana3_3776
            SHW: Sputw3181_0333
            ILO: IL2426(pyrE)
            CPS: CPS_0113(pyrE)
            PHA: PSHAa2787(pyrE)
            PAT: Patl_4281
            SDE: Sde_3672
            PIN: Ping_3478
            MAQ: Maqu_0546
            CBU: CBU_0296(pyrE)
            CBD: COXBU7E912_1785(pyrE)
            LPN: lpg1204(pyrE)
            LPF: lpl1212(pyrE)
            LPP: lpp1206(pyrE)
            MCA: MCA2740(pyrE)
            FTU: FTT0437c(pyrE)
            FTF: FTF0437c(pyrE)
            FTW: FTW_1636(pyrE)
            FTL: FTL_0507
            FTH: FTH_0504(pyrE)
            FTA: FTA_0535(pyrE)
            FTN: FTN_0529(pyrE)
            TCX: Tcr_1895
            NOC: Noc_2998
            AEH: Mlg_0260
            HHA: Hhal_2292
            HCH: HCH_06340(pyrE)
            CSA: Csal_3204
            ABO: ABO_0207(pyrE)
            MMW: Mmwyl1_0619
            AHA: AHA_4223(pyrE)
            DNO: DNO_0919(pyrE)
            BCI: BCI_0181(pyrE)
            RMA: Rmag_0995
            VOK: COSY_0891(pyrE)
            NME: NMB1874
            NMA: NMA0582(pyrE)
            NMC: NMC0345(pyrE)
            NGO: NGO0029(pyrE)
            CVI: CV_4248(pyrE)
            RSO: RSc0139(pyrE)
            REU: Reut_A0195(pyrE)
            REH: H16_A0224(pyrE)
            RME: Rmet_0150
            BMA: BMA2587(pyrE)
            BMV: BMASAVP1_A3125(pyrE-1) BMASAVP1_A3531(pyrE-2)
            BML: BMA10299_A1968(pyrE)
            BMN: BMA10247_3522(pyrE)
            BXE: Bxe_A0281
            BVI: Bcep1808_0299
            BUR: Bcep18194_A3416(pyrE)
            BCN: Bcen_2789
            BCH: Bcen2424_0317
            BAM: Bamb_0236
            BPS: BPSL3243(pyrE)
            BPM: BURPS1710b_0020(pyrE)
            BPL: BURPS1106A_3851(pyrE)
            BPD: BURPS668_3789(pyrE)
            BTE: BTH_I3111
            PNU: Pnuc_2007
            BPE: BP0370(pyrE)
            BPA: BPP4060(pyrE)
            BBR: BB4533(pyrE)
            RFR: Rfer_3928
            POL: Bpro_0217
            PNA: Pnap_0168
            AAV: Aave_0289
            AJS: Ajs_0234
            VEI: Veis_1618
            MPT: Mpe_A0088
            HAR: HEAR0162(pyrE)
            MMS: mma_0191
            NEU: NE1734(pyrE)
            NET: Neut_2050
            NMU: Nmul_A0225
            EBA: ebA3324(pyrE)
            AZO: azo3663(pyrE)
            DAR: Daro_0122
            TBD: Tbd_0255
            MFA: Mfla_2485
            HPY: HP1257(pyrE)
            HPA: HPAG1_1201
            HHE: HH1355(pyrE)
            HAC: Hac_0228(pyrE)
            WSU: WS0315(pyrE)
            TDN: Tmden_2068
            CJE: Cj0233c(pyrE)
            CJR: CJE0284(pyrE)
            CJJ: CJJ81176_0258(pyrE)
            CJU: C8J_0211(pyrE)
            CJD: JJD26997_0231(pyrE)
            CFF: CFF8240_1780(pyrE)
            CCV: CCV52592_2073 CCV52592_2109(pyrE)
            CHA: CHAB381_0211(pyrE)
            CCO: CCC13826_1866(pyrE) CCC13826_2089
            ABU: Abu_2278(pyrE)
            NIS: NIS_1844
            SUN: SUN_0035
            GSU: GSU1637(pyrE)
            GME: Gmet_1938
            GUR: Gura_2069
            PCA: Pcar_1325
            PPD: Ppro_1154
            DVU: DVU2943(pyrE)
            DVL: Dvul_0425
            DDE: Dde_3012
            LIP: LI0998(pyrE)
            BBA: Bd0896 Bd0979(pyrE)
            DPS: DP2916
            ADE: Adeh_3568
            MXA: MXAN_4633(pyrE)
            SAT: SYN_02702
            WOL: WD0228(pyrE)
            WBM: Wbm0790
            AMA: AM087(pyrE)
            APH: APH_1173(pyrE)
            ERU: Erum8490(pyrE)
            ERW: ERWE_CDS_09000(pyrE)
            ERG: ERGA_CDS_08900(pyrE)
            ECN: Ecaj_0886(pyrE)
            ECH: ECH_1108(pyrE)
            NSE: NSE_0538(pyrE)
            PUB: SAR11_1057(pyrE)
            MLO: mll5916 mlr7756
            MES: Meso_1476
            SME: SMc02165(pyrE)
            SMD: Smed_0107
            ATU: Atu0400(pyrE)
            ATC: AGR_C_704
            RET: RHE_CH00474(pyrE)
            BME: BMEI1295
            BMF: BAB1_0673(pyrE)
            BMS: BR0653(pyrE)
            BMB: BruAb1_0670(pyrE)
            BOV: BOV_0646(pyrE)
            BJA: blr8134(pyrE)
            BRA: BRADO0748(pyrE)
            BBT: BBta_7360(pyrE)
            RPA: RPA4724(pyrE)
            RPB: RPB_0847
            RPC: RPC_4858
            RPD: RPD_0955
            RPE: RPE_4822
            NWI: Nwi_0153(pyrE)
            NHA: Nham_0451
            BHE: BH05050(pyrE)
            BQU: BQ04240(pyrE)
            BBK: BARBAKC583_0469(pyrE)
            XAU: Xaut_0057
            CCR: CC_1555
            SIL: SPO2654(pyrE)
            SIT: TM1040_1777
            RSP: RSP_1929(pyrE)
            RSH: Rsph17029_0580
            RSQ: Rsph17025_0324
            JAN: Jann_1741
            RDE: RD1_3236(pyrE)
            PDE: Pden_4468
            MMR: Mmar10_1574
            HNE: HNE_0874(pyrE)
            ZMO: ZMO1707(pyrE)
            NAR: Saro_0912
            SAL: Sala_1406
            ELI: ELI_02720
            GOX: GOX1998(pyrE)
            GBE: GbCGDNIH1_0893
            ACR: Acry_0566
            RRU: Rru_A2507
            MAG: amb1314
            MGM: Mmc1_3732
            ABA: Acid345_1176
            BSU: BG10720(pyrE)
            BHA: BH2532(pyrE)
            BAN: BA4021(pyrE)
            BAR: GBAA4021(pyrE)
            BAA: BA_4492
            BAT: BAS3733
            BCE: BC3882(pyrE)
            BCA: BCE_0690 BCE_3927(pyrE)
            BCZ: BCZK0532(pyrE) BCZK3641(pyrE)
            BTK: BT9727_0532(pyrE) BT9727_3624(pyrE)
            BLI: BL02280(pyrE)
            BLD: BLi01776(pyrE)
            BCL: ABC2329(pyrE)
            BAY: RBAM_015390
            BPU: BPUM_1455
            OIH: OB1495(pyrE)
            GKA: GK1157(pyrE)
            SAU: SA1048(pyrE)
            SAV: SAV1205(pyrE)
            SAM: MW1088(pyrE)
            SAR: SAR1181(pyrE)
            SAS: SAS1139
            SAC: SACOL1217(pyrE)
            SAB: SAB1069(pyrE)
            SAA: SAUSA300_1098(pyrE)
            SAO: SAOUHSC_01172
            SAJ: SaurJH9_1264
            SAH: SaurJH1_1289
            SEP: SE0881
            SER: SERP0771(pyrE)
            SHA: SH1709(pyrE)
            SSP: SSP1567
            LMO: lmo1831(pyrE)
            LMF: LMOf2365_1859(pyrE)
            LIN: lin1945(pyrE)
            LWE: lwe1850(pyrE)
            LLA: L80411(pyrE)
            LLC: LACR_1159
            LLM: llmg_1509(pyrE)
            SPY: SPy_0901(pyrE)
            SPZ: M5005_Spy_0704(pyrE)
            SPM: spyM18_0960(pyrE)
            SPG: SpyM3_0617(pyrE)
            SPS: SPs1236
            SPH: MGAS10270_Spy0762(pyrE)
            SPI: MGAS10750_Spy0796(pyrE)
            SPJ: MGAS2096_Spy0776(pyrE)
            SPK: MGAS9429_Spy0760(pyrE)
            SPF: SpyM51104(pyrE)
            SPA: M6_Spy0721(pyrE)
            SPB: M28_Spy0684(pyrE)
            SPN: SP_0702
            SPR: spr0614(pyrE)
            SPD: SPD_0609(pyrE)
            SAG: SAG1046(pyrE)
            SAN: gbs1081(pyrE)
            SAK: SAK_1136(pyrE)
            SMU: SMU.1221(pyrE)
            STC: str0968(pyrE)
            STL: stu0968(pyrE)
            SSA: SSA_1240(pyrE)
            SGO: SGO_1253(pyrE)
            LPL: lp_2697(pyrE)
            LJO: LJ1283
            LAC: LBA1387(pyrE)
            LSA: LSA0959(pyrE)
            LSL: LSL_0831(pyrE)
            LDB: Ldb1532(pyrE)
            LBU: LBUL_1423
            LBR: LVIS_2228
            LCA: LSEI_1449
            EFA: EF1712(pyrE)
            OOE: OEOE_0263
            STH: STH1261
            CAC: CAC0027(pyrE)
            CPE: CPE1177(pyrE)
            CPF: CPF_1381(pyrE)
            CPR: CPR_1196(pyrE)
            CTC: CTC02378(pyrE)
            CNO: NT01CX_0390(pyrE)
            CDF: CD0187(pyrE)
            CBO: CBO3235(pyrE)
            CBA: CLB_3272(pyrE)
            CBH: CLC_3146(pyrE)
            CBF: CLI_3374(pyrE)
            CBE: Cbei_1006
            CKL: CKL_3355(pyrE)
            AMT: Amet_4207
            CHY: CHY_1495(pyrE)
            DSY: DSY2855
            SWO: Swol_1277
            TTE: TTE1529(pyrE)
            MTA: Moth_2126
            MPE: MYPE7840(pyrE)
            MTU: Rv0382c(pyrE)
            MTC: MT0395(pyrE)
            MBO: Mb0389c(pyrE)
            MBB: BCG_0420c(pyrE)
            MLE: ML2487
            MPA: MAP3857(umpA)
            MAV: MAV_4790(pyrE)
            MSM: MSMEG_6520
            MMC: Mmcs_5123
            CGL: NCgl2676(pyrE)
            CGB: cg3071(pyrE)
            CEF: CE2604
            CDI: DIP2097(pyrE)
            CJK: jk0213(pyrE)
            NFA: nfa53980(pyrE)
            RHA: RHA1_ro05518
            SCO: SCO3650(pyrE)
            SMA: SAV4522(pyrE)
            TWH: TWT743(pyrE)
            TWS: TW755(pyrE)
            LXX: Lxx23400(pyrE)
            ART: Arth_0512
            AAU: AAur_0535(pyrE)
            PAC: PPA1004
            TFU: Tfu_3008(pyrE)
            FRA: Francci3_0559
            FAL: FRAAL1055(pyrE)
            KRA: Krad_4186
            SEN: SACE_3691(pyrE) SACE_7189(pyrE)
            BLO: BL0788(pyrE)
            BAD: BAD_0765(pyrE)
            RXY: Rxyl_2302
            FNU: FN0427
            RBA: RB328(pyrE)
            CPN: CPn0608
            CPA: CP0139
            CPJ: CPj0608
            CPT: CpB0632
            CCA: CCA00132(pyrE)
            CAB: CAB131(pyrE)
            CFE: CF0874(pyrF)
            TDE: TDE1001(pyrE)
            LIL: LA1539 LA2988(pyrE)
            LIC: LIC11076(pyrE) LIC12227
            LBJ: LBJ_2101(pyrE)
            LBL: LBL_0950(pyrE)
            SYN: slr0185(umpS)
            SYW: SYNW0238(pyrE)
            SYC: syc1518_d(umpS)
            SYF: Synpcc7942_2592
            SYD: Syncc9605_0231
            SYE: Syncc9902_0260
            SYG: sync_0276(pyrE) sync_0364 sync_2377
            SYR: SynRCC307_2302(pyrE)
            SYX: SynWH7803_0281(pyrE)
            CYA: CYA_2438(pyrE)
            CYB: CYB_1487(pyrE)
            TEL: tlr1828
            GVI: gll4276 glr1079
            ANA: alr2945 alr5099
            AVA: Ava_0957 Ava_2358(pyrE)
            PMA: Pro0307(pyrE)
            PMM: PMM0275(pyrE)
            PMT: PMT1868(pyrE)
            PMN: PMN2A_1641
            PMI: PMT9312_0277
            PMB: A9601_02981(pyrE)
            PMC: P9515_03081(pyrE)
            PMF: P9303_24961(pyrE)
            PMG: P9301_02991(pyrE)
            PMH: P9215_03001
            PME: NATL1_03551(pyrE)
            TER: Tery_0376 Tery_2462
            BTH: BT_3731
            BFR: BF0510
            BFS: BF0455(pyrE)
            PGI: PG1353(pyrE)
            SRU: SRU_1302(pyrE)
            CHU: CHU_2669(pyrE)
            GFO: GFO_2690(pyrE)
            FPS: FP0663(pyrE)
            CTE: CT0083(pyrE)
            CCH: Cag_0017(pyrE)
            PLT: Plut_2048(pyrE)
            DET: DET1193(pyrE)
            DEH: cbdb_A1108(pyrE)
            RRS: RoseRS_1721
            RCA: Rcas_1987
            DRA: DR_0447
            DGE: Dgeo_0138
            TTH: TTC1380(pyrE)
            TTJ: TTHA1742
            AAE: aq_1907
            TMA: TM0331
            MJA: MJ1646
            MMP: MMP0079 MMP1492(pyrE)
            MAE: Maeo_0561
            MVN: Mevan_0801
            MAC: MA0919 MA2520(pyrE) MA3307(pyrE)
            MBA: Mbar_A0547 Mbar_A3471 Mbar_A3515
            MMA: MM_0142 MM_2035
            MBU: Mbur_1052 Mbur_1806
            MTP: Mthe_1305
            MHU: Mhun_0973 Mhun_1108
            MEM: Memar_1001
            MTH: MTH1860 MTH876
            MST: Msp_1036(pyrE) Msp_1334
            MSI: Msm_0821 Msm_0883
            MKA: MK1072(pyrE)
            AFU: AF0386
            HAL: VNG0448G(pyrE1) VNG2118G(pyrE2)
            HMA: rrnAC0927(pyrE2) rrnAC2521(pyrE1) rrnAC2670(ort)
            HWA: HQ1664A(pyrE) HQ3229A(pyrE)
            NPH: NP1256A(pyrE)
            TAC: Ta0056 Ta1164
            TVO: TVN0012 TVN1218
            PTO: PTO0208(pyrE) PTO0465
            PHO: PH1128
            PAB: PAB2430(pyrE)
            PFU: PF1034
            TKO: TK2138
            RCI: RCIX2284(pyrE-2) RCIX518(pyrE-1)
            APE: APE_2349.1
            HBU: Hbut_0111
            SSO: SSO0615(pyrE)
            STO: ST1481
            SAI: Saci_1597(pyrE)
            PAI: PAE3264(pyrE)
            PAS: Pars_1693
STRUCTURES  PDB: 1LH0  1OPR  1ORO  1STO  2AEE  2EAW  2P1Z  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.10
            ExPASy - ENZYME nomenclature database: 2.4.2.10
            ExplorEnz - The Enzyme Database: 2.4.2.10
            ERGO genome analysis and discovery system: 2.4.2.10
            BRENDA, the Enzyme Database: 2.4.2.10
            CAS: 9030-25-5
///
ENTRY       EC 2.4.2.11                 Enzyme
NAME        nicotinate phosphoribosyltransferase;
            niacin ribonucleotidase;
            nicotinic acid mononucleotide glycohydrolase;
            nicotinic acid mononucleotide pyrophosphorylase;
            nicotinic acid phosphoribosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     nicotinate-nucleotide:diphosphate phospho-alpha-D-ribosyltransferase
REACTION    nicotinate D-ribonucleotide + diphosphate = nicotinate +
            5-phospho-alpha-D-ribose 1-diphosphate [RN:R01724]
ALL_REAC    R01724
SUBSTRATE   nicotinate D-ribonucleotide [CPD:C01185];
            diphosphate [CPD:C00013]
PRODUCT     nicotinate [CPD:C00253];
            5-phospho-alpha-D-ribose 1-diphosphate [CPD:C00119]
REFERENCE   1  [PMID:13717628]
  AUTHORS   IMSANDE J.
  TITLE     Pathway of diphosphopyridine nucleotide biosynthesis in Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 236 (1961) 1494-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:13717627]
  AUTHORS   IMSANDE J, HANDLER P.
  TITLE     Biosynthesis of diphosphopyridine nucleotide. III. Nicotinic acid
            mononucleotide pyrophos-phorylase.
  JOURNAL   J. Biol. Chem. 236 (1961) 525-30.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:4324895]
  AUTHORS   Kosaka A, Spivey HO, Gholson RK.
  TITLE     Nicotinate phosphoribosyltransferase of yeast. Purification and
            properties.
  JOURNAL   J. Biol. Chem. 246 (1971) 3277-83.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], human [GN:hsa], cow [GN:bta],
            Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K00763  nicotinate phosphoribosyltransferase
GENES       SCE: YOR209C(NPT1)
            AGO: AGOS_ACR160C
            PIC: PICST_87669(NPT1)
            CAL: CaO19.7176(NPT1)
            CGR: CAGL0L02805g
            SPO: SPAC1486.06
            ANI: AN9116.2
            AFM: AFUA_7G01880
            AOR: AO090038000565
            CNE: CNL05000
            TBR: Tb10.26.0320
            TCR: 509647.180
            LMA: LmjF33.0960
            EHI: 25.t00031
            ECO: b0931(pncB)
            ECJ: JW0914(pncB)
            ECE: Z1279(pncB)
            ECS: ECs1014
            ECC: c1073(pncB)
            ECI: UTI89_C1003(pncB)
            ECV: APECO1_43(pncB)
            ECW: EcE24377A_1031(pncB)
            ECX: EcHS_A1039
            STY: STY1010(pncB)
            STT: t1930(pncB)
            SPT: SPA1794(pncB)
            SEC: SC0962(pncB)
            STM: STM1004(pncB)
            YPE: YPO1413(pncB)
            YPK: y2757(pncB)
            YPM: YP_1180(pncB)
            YPA: YPA_0708
            YPN: YPN_2564
            YPP: YPDSF_2282
            YPS: YPTB1437(pncB)
            YPI: YpsIP31758_2557(pncB)
            YEN: YE1565(pncB)
            SFL: SF0928(pncB)
            SFX: S0992(pncB)
            SFV: SFV_0933(pncB)
            SSN: SSON_0934(pncB)
            SBO: SBO_2222(pncB)
            SDY: SDY_2326(pncB)
            ECA: ECA2540(pncB)
            PLU: plu1754(pcnB)
            BUC: BU361(pncB)
            BAS: BUsg349(pncB)
            SGL: SG1016
            ENT: Ent638_1450
            SPE: Spro_1732
            HSO: HS_0002(pncB)
            MSU: MS1889(pncB)
            XFA: XF1097
            XFT: PD0393(pncB)
            XCC: XCC0681(pncB) XCC3445(pbeF)
            XCB: XC_0719 XC_3552
            XCV: XCV0735 XCV3647(pncB)
            XAC: XAC0674(pbeF) XAC3521(pncB)
            XOO: XOO3947(pbeF)
            XOM: XOO_3724(XOO3724)
            VCH: VCA0098
            VCO: VC0395_0041(pncB)
            VVU: VV1_2372
            VVY: VV1969
            VPA: VPA0309
            PPR: PBPRA1763
            PAE: PA4376(pncB2) PA4919(pncB1)
            PAU: PA14_56900(pncB2) PA14_64960(pncB1)
            PAP: PSPA7_4945(pncB2) PSPA7_5645(pncB1)
            PPU: PP_4868(pncB)
            PPF: Pput_4746
            PST: PSPTO_4921(pncB)
            PSB: Psyr_0595
            PSP: PSPPH_0588(pncB)
            PFL: PFL_0594(pncB) PFL_2467(pncB)
            PFO: Pfl_0548
            PEN: PSEEN2058(pncB-2) PSEEN4919(pncB-1)
            PMY: Pmen_1411
            PAR: Psyc_1293(pncB)
            PCR: Pcryo_1089 Pcryo_2205
            PRW: PsycPRwf_0581
            ACI: ACIAD3562(pncB)
            ILO: IL0103(pncB)
            PIN: Ping_1730
            CBU: CBU_1035
            LPN: lpg0270
            LPF: lpl0322(pncB)
            LPP: lpp0344(pncB)
            MCA: MCA2760
            FTU: FTT1534c
            FTF: FTF1534c
            FTL: FTL_0579
            FTH: FTH_0579(pncB)
            FTN: FTN_1443
            NOC: Noc_1009
            AEH: Mlg_1985
            CSA: Csal_0941
            AHA: AHA_4212(pncB)
            DNO: DNO_0196(pncB)
            NME: NMB1505
            NMA: NMA1706(pncB)
            NMC: NMC1435(pncB)
            NGO: NGO0962
            CVI: CV_3422(pncB)
            RSO: RS05359(RSp0836) RSc1031(pncB)
            REU: Reut_A2284
            REH: H16_A2589(pncB)
            RME: Rmet_2449 Rmet_5105
            BMA: BMA0510(pncB)
            BMV: BMASAVP1_A2501(pncB)
            BML: BMA10299_A2781(pncB)
            BMN: BMA10247_1824(pncB)
            BXE: Bxe_A1052 Bxe_B1188
            BVI: Bcep1808_1020
            BUR: Bcep18194_A4213 Bcep18194_B0826
            BCN: Bcen_0621 Bcen_3480
            BCH: Bcen2424_1100 Bcen2424_4886
            BAM: Bamb_0976
            BPS: BPSL0717 BPSL2462
            BPM: BURPS1710b_0939(pncB) BURPS1710b_2931(pncB)
            BPL: BURPS1106A_0775(pncB) BURPS1106A_2873(pncB)
            BPD: BURPS668_0763(pncB) BURPS668_2812(pncB)
            BTE: BTH_I0625 BTH_I1697(pncB)
            BPE: BP3583(pncB)
            BPA: BPP3329(pncB)
            BBR: BB3780(pncB)
            RFR: Rfer_0827
            POL: Bpro_3080
            PNA: Pnap_1620 Pnap_3719
            AAV: Aave_0976 Aave_3306
            AJS: Ajs_2492
            VEI: Veis_2067
            HAR: HEAR0018(pncB)
            MMS: mma_0027
            NMU: Nmul_A0907
            CJE: Cj0230c
            CJR: CJE0281
            CJU: C8J_0208
            CCV: CCV52592_0508(pncB)
            CHA: CHAB381_0113(pncB)
            CCO: CCC13826_1903(pncB)
            NIS: NIS_1072(pncB)
            GSU: GSU2289
            GME: Gmet_2373
            PCA: Pcar_0167 Pcar_1071
            ADE: Adeh_3664
            MXA: MXAN_7166
            SFU: Sfum_2602
            MLO: mll4892
            MES: Meso_1739
            SME: SMc02276(pncB)
            SMD: Smed_0200
            ATU: Atu0213(pncB)
            ATC: AGR_C_367
            RET: RHE_CH00181(pncB)
            RLE: RL0191
            BME: BMEI1836
            BMF: BAB1_0109(pncB)
            BMS: BR0112(pncB)
            BMB: BruAb1_0109(pncB)
            BOV: BOV_0109(pncB)
            OAN: Oant_0125
            BJA: bll2327(pncB)
            BRA: BRADO0323(pncB)
            BBT: BBta_0308(pncB)
            RPB: RPB_2592
            NHA: Nham_3403
            BHE: BH00910(pncB)
            BQU: BQ00840(pncB)
            BBK: BARBAKC583_1307(pncB)
            XAU: Xaut_2365
            SIL: SPO0095(pncB)
            SIT: TM1040_3432
            RSP: RSP_1367
            RSH: Rsph17029_0035
            RSQ: Rsph17025_0025
            JAN: Jann_0022
            RDE: RD1_0586(pncB)
            PDE: Pden_0852
            GBE: GbCGDNIH1_1419
            MAG: amb2738
            MGM: Mmc1_1212
            BSU: BG13966(yueK)
            BAN: BA0596
            BAR: GBAA0596
            BAA: BA_1178
            BAT: BAS0565
            BCE: BC0597 BC4685
            BCA: BCE_0664
            BCZ: BCZK0509(pncB) BCZK4439(pncB)
            BTK: BT9727_0507(pncB) BT9727_4421(pncB)
            BTL: BALH_0537(pncB) BALH_4263(pncB)
            BLI: BL02611
            BLD: BLi03363(yueK)
            BCL: ABC3966
            BPU: BPUM_2844
            OIH: OB0386
            GKA: GK1819
            SAU: SA1729
            SAV: SAV1913
            SAM: MW1854
            SAR: SAR2006
            SAS: SAS1837
            SAC: SACOL1975
            SAB: SAB1850c
            SAA: SAUSA300_1894
            SAO: SAOUHSC_02133
            SEP: SE1597
            SER: SERP1450
            SHA: SH1039
            SSP: SSP0878
            LMO: lmo1092
            LMF: LMOf2365_1106
            LIN: lin1077
            LWE: lwe1067(pncB)
            LLA: L107468(ylaF)
            LLC: LACR_1202
            LLM: llmg_1472(pncB)
            SPY: SPy_1653
            SPZ: M5005_Spy_1358(nadE)
            SPM: spyM18_1664
            SPG: SpyM3_1393
            SPS: SPs0469
            SPH: MGAS10270_Spy1475(nadE)
            SPI: MGAS10750_Spy1467(nadE)
            SPJ: MGAS2096_Spy1380(nadE)
            SPK: MGAS9429_Spy1354(nadE)
            SPA: M6_Spy1404
            SPB: M28_Spy1399(nadE)
            SPN: SP_1421
            SPR: spr1277
            SPD: SPD_1251(pncB)
            SAG: SAG0295
            SAN: gbs0285
            SAK: SAK_0367
            SMU: SMU.464
            STC: str0226(pncB)
            STL: stu0226(pncB)
            SSA: SSA_1864(pncB)
            SGO: SGO_0582
            LPL: lp_0565(nadC1) lp_2771(natC2)
            LJO: LJ1734
            LAC: LBA0521(nadC)
            LSA: LSA1570(nadC)
            LSL: LSL_1261(pncB) pSF118-44_01
            LDB: Ldb0319(pncB)
            LBU: LBUL_0276
            LBR: LVIS_0543
            LCA: LSEI_1806 LSEI_2766
            EFA: EF2626
            OOE: OEOE_0890
            STH: STH2605
            CAC: CAC1002 CAC1780
            CPE: CPE1207
            CPF: CPF_1417
            CPR: CPR_1227(pncB)
            CTC: CTC00983
            CNO: NT01CX_1626
            CBA: CLB_1435
            CBH: CLC_1447
            CBF: CLI_1508
            CKL: CKL_1467
            DSY: DSY0787(pncB)
            MGE: MG_037
            MMY: MSC_0687(pncB)
            MMO: MMOB3120(pncB)
            MHP: MHP7448_0394
            MTU: Rv0573c
            MTC: MT0601
            MBO: Mb0588c
            MAV: MAV_1550(pncB)
            MSM: MSMEG_4911(pncB)
            MMC: Mmcs_3854
            CJK: jk0492
            RHA: RHA1_ro01442
            SCO: SCO0171(SCJ1.20)
            CMI: CMM_1292(pncB)
            PAC: PPA1681
            FRA: Francci3_0860
            FAL: FRAAL1493
            SEN: SACE_2423(pncB)
            FNU: FN0348
            BBU: BB0635
            BGA: BG0657
            TPA: TP0628
            TDE: TDE0174
            CYA: CYA_1521
            CYB: CYB_1096
            TEL: tlr1177
            ANA: alr2482
            AVA: Ava_0414
            TER: Tery_0318
            BTH: BT_1913
            BFR: BF3524
            BFS: BF3334(pncB)
            PGI: PG0057(pncB)
            SRU: SRU_0348(pncB)
            CHU: CHU_2424(nadV)
            GFO: GFO_3189
            FJO: Fjoh_2472
            DEH: cbdb_A1382(pncB)
            DRA: DR_A0272
            DGE: Dgeo_1325
            TTH: TTC0252
            TTJ: TTHA0617
            AAE: aq_1056
            MAC: MA2533(pncB)
            MBA: Mbar_A3022
            MMA: MM_3086
            MBU: Mbur_0321
            MHU: Mhun_2593
            HWA: HQ1058A(pncB) HQ1979A(pncB)
            NPH: NP1174A(pncB)
            PTO: PTO1004
STRUCTURES  PDB: 1VLP  1YBE  1YIR  1YTD  1YTE  1YTK  2F7F  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.11
            ExPASy - ENZYME nomenclature database: 2.4.2.11
            ExplorEnz - The Enzyme Database: 2.4.2.11
            ERGO genome analysis and discovery system: 2.4.2.11
            BRENDA, the Enzyme Database: 2.4.2.11
            CAS: 9030-26-6
///
ENTRY       EC 2.4.2.12                 Enzyme
NAME        nicotinamide phosphoribosyltransferase;
            NMN pyrophosphorylase;
            nicotinamide mononucleotide pyrophosphorylase;
            nicotinamide mononucleotide synthetase;
            NMN synthetase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     nicotinamide-nucleotide:diphosphate
            phospho-alpha-D-ribosyltransferase
REACTION    nicotinamide D-ribonucleotide + diphosphate = nicotinamide +
            5-phospho-alpha-D-ribose 1-diphosphate [RN:R01271]
ALL_REAC    R01271
SUBSTRATE   nicotinamide D-ribonucleotide [CPD:C00455];
            diphosphate [CPD:C00013]
PRODUCT     nicotinamide [CPD:C00153];
            5-phospho-alpha-D-ribose 1-diphosphate [CPD:C00119]
REFERENCE   1
  AUTHORS   Preiss, J. and Handler, P.
  TITLE     Enzymatic synthesis of nicotinamide mononucleotide.
  JOURNAL   J. Biol. Chem. 225 (1957) 759-770.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K03462  nicotinamide phosphoribosyltransferase
GENES       HSA: 10135(PBEF1)
            PTR: 463648(PBEF1)
            MMU: 59027(Pbef1)
            RNO: 297508(Pbef1)
            CFA: 483267(PBEF1)
            GGA: 417707(RCJMB04_6p13)
            SPU: 577046(LOC577046)
            PRW: PsycPRwf_1852
            FTW: FTW_0395
            CFF: CFF8240_0022
            CBE: Cbei_2078
            FJO: Fjoh_0745
            MSI: Msm_1792
STRUCTURES  PDB: 2G95  2G96  2G97  2GVG  2GVJ  2GVL  2H3B  2H3D  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.12
            ExPASy - ENZYME nomenclature database: 2.4.2.12
            ExplorEnz - The Enzyme Database: 2.4.2.12
            ERGO genome analysis and discovery system: 2.4.2.12
            BRENDA, the Enzyme Database: 2.4.2.12
            CAS: 9030-27-7
///
ENTRY       EC 2.4.2.13       Obsolete  Enzyme
NAME        Transferred to 2.5.1.6
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
COMMENT     Transferred entry: now EC 2.5.1.6 methionine adenosyltransferase (EC
            2.4.2.13 created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.13
            ExPASy - ENZYME nomenclature database: 2.4.2.13
            ExplorEnz - The Enzyme Database: 2.4.2.13
            ERGO genome analysis and discovery system: 2.4.2.13
            BRENDA, the Enzyme Database: 2.4.2.13
///
ENTRY       EC 2.4.2.14                 Enzyme
NAME        amidophosphoribosyltransferase;
            phosphoribosyldiphosphate 5-amidotransferase;
            glutamine phosphoribosyldiphosphate amidotransferase;
            alpha-5-phosphoribosyl-1-pyrophosphate amidotransferase;
            5'-phosphoribosylpyrophosphate amidotransferase;
            5-phosphoribosyl-1-pyrophosphate amidotransferase;
            5-phosphororibosyl-1-pyrophosphate amidotransferase;
            glutamine 5-phosphoribosylpyrophosphate amidotransferase;
            glutamine ribosylpyrophosphate 5-phosphate amidotransferase;
            phosphoribose pyrophosphate amidotransferase;
            phosphoribosyl pyrophosphate amidotransferase;
            phosphoribosylpyrophosphate glutamyl amidotransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     5-phosphoribosylamine:diphosphate phospho-alpha-D-ribosyltransferase
            (glutamate-amidating)
REACTION    5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate =
            L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
            [RN:R01072]
ALL_REAC    R01072
SUBSTRATE   5-phospho-beta-D-ribosylamine [CPD:C03090];
            diphosphate [CPD:C00013];
            L-glutamate [CPD:C00025]
PRODUCT     L-glutamine [CPD:C00064];
            5-phospho-alpha-D-ribose 1-diphosphate [CPD:C00119];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:14235537]
  AUTHORS   CASKEY CT, ASHTON DM, WYNGAARDEN JB.
  TITLE     THE ENZYMOLOGY OF FEEDBACK INHIBITION OF GLUTAMINE
            PHOSPHORIBOSYLPYROPHOSPHATE AMIDOTRANSFERASE BY PURINE
            RIBONUCLEOTIDES.
  JOURNAL   J. Biol. Chem. 239 (1964) 2570-9.
  ORGANISM  pigeon
REFERENCE   2  [PMID:13563519]
  AUTHORS   HARTMAN SC, BUCHANAN JM.
  TITLE     Biosynthesis of the purines. XXI. 5-Phosphoribosylpyrophosphate
            amidotransferase.
  JOURNAL   J. Biol. Chem. 233 (1958) 451-5.
  ORGANISM  pigeon
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00251  Glutamate metabolism
ORTHOLOGY   KO: K00764  amidophosphoribosyltransferase
GENES       HSA: 5471(PPAT)
            MMU: 231327(Ppat)
            RNO: 117544(Ppat)
            CFA: 611407(PPAT)
            GGA: 422743(PPAT)
            XLA: 398956(MGC68694)
            XTR: 394937(MGC76221)
            DME: Dmel_CG10078(Prat2) Dmel_CG2867(Prat)
            CEL: T04A8.5(Amidophosphoribosyltransferase)
            ATH: AT2G16570(ATASE) AT4G34740(ATASE2/ATD2) AT4G38880(ATASE3)
            OSA: 4338879
            CME: CMR240C
            SCE: YMR300C(ADE4)
            AGO: AGOS_AGL334W
            PIC: PICST_78788(ADE4)
            CGR: CAGL0M13717g
            SPO: SPAC4D7.08c(ade4)
            ANI: AN6637.2
            AFM: AFUA_6G03750
            AOR: AO090701000173
            CNE: CNC04700
            DDI: DDB_0230083(purF)
            ECO: b2312(purF)
            ECJ: JW2309(purF)
            ECE: Z3574(purF)
            ECS: ECs3196
            ECC: c2856(purF)
            ECI: UTI89_C2596(purF)
            ECP: ECP_2351
            ECV: APECO1_4252(purF)
            ECW: EcE24377A_2606(purF)
            ECX: EcHS_A2463
            STY: STY2592(purF)
            STT: t0502(purF)
            SPT: SPA0502(purF)
            SEC: SC2364(purF)
            STM: STM2362(purF)
            YPE: YPO2772(purF)
            YPK: y1605(purF)
            YPM: YP_2392(purF)
            YPA: YPA_2072
            YPN: YPN_2175
            YPP: YPDSF_1989
            YPS: YPTB2612(purF)
            YPI: YpsIP31758_1426(purF)
            YEN: YE1315(purF)
            SFL: SF2388(purF)
            SFX: S2523(purF)
            SFV: SFV_2381(purF)
            SSN: SSON_2370(purF)
            SBO: SBO_2349(purF)
            SDY: SDY_2511(purF)
            ECA: ECA3052(purF)
            PLU: plu3167(purF)
            WBR: WGLp313(purF)
            SGL: SG1613
            ENT: Ent638_2861
            KPN: KPN_02702(purF)
            HIN: HI1207(purF)
            HIT: NTHI1378(purF)
            HIQ: CGSHiGG_09765
            HSO: HS_0916(purF)
            PMU: PM0701(purF)
            MSU: MS1003(purF)
            APL: APL_0425(purF)
            XFA: XF1949
            XFT: PD0851(purF)
            XCC: XCC0953(purF)
            XCB: XC_3282
            XCV: XCV1061(purF)
            XAC: XAC1032(purF)
            XOO: XOO3675(purF)
            XOM: XOO_3472(XOO3472)
            VCH: VC1004
            VCO: VC0395_A0525(purF)
            VVU: VV1_1997
            VVY: VV2419
            VPA: VP2185
            VFI: VF1691
            PPR: PBPRA2648
            PAE: PA3108(purF)
            PAU: PA14_23920(purF)
            PAP: PSPA7_2025(purF)
            PPU: PP_2000(purF)
            PST: PSPTO_3811(purF)
            PSB: Psyr_1668
            PSP: PSPPH_1662(purF) PSPPH_2915
            PFL: PFL_2077(purF)
            PFO: Pfl_1902
            PEN: PSEEN1695(purF)
            PMY: Pmen_2711
            PAR: Psyc_1282(purF)
            PCR: Pcryo_1103
            ACI: ACIAD1323(purF) ACIAD2527
            ACB: A1S_2251
            SON: SO_3064(purF)
            SDN: Sden_1490
            SFR: Sfri_1399
            SAZ: Sama_2146
            SBL: Sbal_2738
            SLO: Shew_2302
            SPC: Sputcn32_2437
            SHE: Shewmr4_1430
            SHM: Shewmr7_1495
            SHN: Shewana3_1483
            SHW: Sputw3181_1571
            ILO: IL1012(purF)
            CPS: CPS_3798(purF)
            PHA: PSHAa2070(purF)
            PAT: Patl_1609
            SDE: Sde_2072
            PIN: Ping_1965
            MAQ: Maqu_1552
            CBU: CBU_0897(purF)
            CBD: COXBU7E912_0961(purF)
            LPN: lpg1674(purF)
            LPF: lpl1639(purF)
            LPP: lpp1646(purF)
            MCA: MCA2489(purF)
            FTU: FTT1721c(purF)
            FTF: FTF1721c(purF)
            FTW: FTW_0077(purF)
            FTL: FTL_1861
            FTH: FTH_0402 FTH_1790(purF)
            FTA: FTA_1967(purF)
            FTN: FTN_1700(purF)
            TCX: Tcr_0808 Tcr_1346
            NOC: Noc_1671
            AEH: Mlg_1242
            HHA: Hhal_1798
            HCH: HCH_02442(purF)
            CSA: Csal_1267
            ABO: ABO_1455(purF)
            AHA: AHA_1870(purF)
            DNO: DNO_0088(purF)
            BCI: BCI_0368(purF)
            RMA: Rmag_1001
            VOK: COSY_0897(purF)
            NME: NMB0690
            NMA: NMA0892(purF)
            NMC: NMC0641(purF)
            NGO: NGO0263
            CVI: CV_2023 CV_2515(purF)
            RSO: RSc1976(purF)
            REU: Reut_A2299
            REH: H16_A2607(purF)
            RME: Rmet_2460
            BMA: BMAA1714(purF)
            BMV: BMASAVP1_1656(purF)
            BML: BMA10299_1865(purF)
            BMN: BMA10247_A0536(purF)
            BXE: Bxe_B2874
            BUR: Bcep18194_B2118
            BCN: Bcen_4402
            BCH: Bcen2424_3965
            BAM: Bamb_3355
            BPS: BPSS1692(purF)
            BPM: BURPS1710b_A0762(purF)
            BPL: BURPS1106A_A2300(purF)
            BPD: BURPS668_A2438(purF)
            BTE: BTH_II0686(purF)
            BPE: BP1415(purF)
            BPA: BPP1522(purF)
            BBR: BB2600(purF)
            RFR: Rfer_2683
            POL: Bpro_1607
            MPT: Mpe_A2151
            HAR: HEAR1229(purF)
            MMS: mma_2158
            NEU: NE0699(purF)
            NET: Neut_1158
            NMU: Nmul_A1906
            EBA: ebA1295(hisH) ebA4783(purF)
            AZO: azo1053(purF) azo3011(glxB)
            DAR: Daro_0876
            TBD: Tbd_1908
            MFA: Mfla_1692
            HHE: HH0488(purF)
            WSU: WS0456(purF)
            TDN: Tmden_1871
            CJE: Cj0196c(purF)
            CJR: CJE0189(purF)
            CJJ: CJJ81176_0227(purF)
            CJU: C8J_0185(purF)
            CJD: JJD26997_0206(purF)
            CFF: CFF8240_0299(purF)
            CCV: CCV52592_0845(purF)
            CHA: CHAB381_1359(purF)
            CCO: CCC13826_1137(purF)
            ABU: Abu_2088(purF)
            NIS: NIS_1547(purF)
            SUN: SUN_0236(purF)
            GSU: GSU1636(purF)
            GME: Gmet_1939
            PCA: Pcar_1326
            DVU: DVU0161(purF)
            DDE: Dde_0334
            LIP: LI0938(purF)
            BBA: Bd3009(purF)
            DPS: DP0259
            ADE: Adeh_4206
            MXA: MXAN_1103(purF)
            SAT: SYN_00907 SYN_01624
            SFU: Sfum_0268
            WOL: WD1109(purF)
            WBM: Wbm0255
            AMA: AM1338(purF)
            APH: APH_1300(purF)
            ERU: Erum0900(purF)
            ERW: ERWE_CDS_00860(purF)
            ERG: ERGA_CDS_00830(purF)
            ECN: Ecaj_0090
            ECH: ECH_0139(purF)
            NSE: NSE_0194(purF)
            PUB: SAR11_0699(purF)
            MLO: mll7833
            MES: Meso_0983
            SME: SMc00554(purF)
            ATU: Atu1075(purF)
            ATC: AGR_C_1986
            RET: RHE_CH01428(purF) RHE_PE00421(glxB)
            RLE: RL1546(purF) pRL110557(glxB)
            BME: BMEI1488
            BMF: BAB1_0472(purF)
            BMS: BR0446(purF)
            BMB: BruAb1_0468(purF)
            BOV: BOV_0453(purF)
            BJA: bll4060(purF)
            BRA: BRADO3280(purF)
            BBT: BBta_3787(purF)
            RPA: RPA3091(purF)
            RPB: RPB_2452
            RPC: RPC_2282
            RPD: RPD_2997
            RPE: RPE_3340
            NWI: Nwi_2017
            NHA: Nham_2293
            BHE: BH05240(purF)
            BQU: BQ04430(purF)
            BBK: BARBAKC583_0486(cvpA1)
            CCR: CC_1658
            SIL: SPO2677(purF)
            SIT: TM1040_1787
            RSP: RSP_2454(purF)
            JAN: Jann_1707
            RDE: RD1_3247 RD1_4253
            MMR: Mmar10_1205
            HNE: HNE_0717(purF)
            ZMO: ZMO1557(purF)
            NAR: Saro_1763
            SAL: Sala_1541
            ELI: ELI_07015
            GOX: GOX1640
            GBE: GbCGDNIH1_0470 GbCGDNIH1_2113
            RRU: Rru_A0404
            MAG: amb2089
            MGM: Mmc1_0265
            ABA: Acid345_4621
            BSU: BG10707(purF)
            BHA: BH0630(purF)
            BAN: BA0295(purF)
            BAR: GBAA0295(purF)
            BAA: BA_0867
            BAT: BAS0282
            BCE: BC0330
            BCA: BCE_0324(purF)
            BCZ: BCZK0270(purF)
            BTK: BT9727_0267(purF)
            BTL: BALH_0289(purF)
            BLI: BL01483(purF)
            BLD: BLi00700(purF)
            BCL: ABC1031(purF)
            BAY: RBAM_006910
            BPU: BPUM_0603
            OIH: OB0746(purF)
            GKA: GK0264
            SAU: SA0922(purF)
            SAV: SAV1070(purF)
            SAM: MW0953(purF)
            SAR: SAR1044(purF)
            SAS: SAS1006
            SAC: SACOL1079(purF)
            SAB: SAB0937(purF)
            SAA: SAUSA300_0972(purF)
            SAO: SAOUHSC_01014
            SEP: SE0768
            SER: SERP0655(purF)
            SHA: SH1887(purF)
            SSP: SSP1720
            LMO: lmo1768(purF)
            LMF: LMOf2365_1793(purF)
            LIN: lin1880(purF)
            LWE: lwe1786(purF)
            LLA: L171350(purF)
            LLC: LACR_1618
            LLM: llmg_0977(purF)
            SPY: SPy_0026(purF)
            SPZ: M5005_Spy_0024(purF)
            SPM: spyM18_0027(purF)
            SPG: SpyM3_0021(purF)
            SPS: SPs0022
            SPH: MGAS10270_Spy0025(purF)
            SPI: MGAS10750_Spy0024(purF)
            SPJ: MGAS2096_Spy0025(purF)
            SPK: MGAS9429_Spy0024(purF)
            SPF: SpyM50023(purF)
            SPA: M6_Spy0073
            SPB: M28_Spy0024(purF)
            SPN: SP_0046
            SPR: spr0047(purF)
            SPD: SPD_0053(purF)
            SAG: SAG0026(purF)
            SAN: gbs0025
            SAK: SAK_0059(purF)
            SMU: SMU.32(purF)
            STC: str0032(purF)
            STL: stu0032(purF)
            SSA: SSA_0031(purF)
            SGO: SGO_0036(purF)
            LPL: lp_2723(purF)
            LAC: LBA1555(purL)
            LSA: LSA0659(purF)
            LSL: LSL_0667(purF)
            LDB: Ldb1439(purF)
            LBU: LBUL_1334
            LCA: LSEI_1750
            EFA: EF1781(purF)
            STH: STH2854
            CAC: CAC1392(purF)
            CPE: CPE0683(purF)
            CPF: CPF_0674(purF)
            CPR: CPR_0672(purF)
            CTC: CTC01965
            CNO: NT01CX_2422(purF)
            CDF: CD0220(purF)
            CBO: CBO2876(purF) CBO2913(purF)
            CBA: CLB_2841(purF-1) CLB_2875(purF-2)
            CBH: CLC_2774(purF-1) CLC_2808(purF-2)
            CBF: CLI_2934(purF-1) CLI_2968(purF-2)
            CBE: Cbei_1056
            CKL: CKL_2687(purF)
            CHY: CHY_1075(purF)
            DSY: DSY3930
            SWO: Swol_1778
            TTE: TTE0812(purF)
            MTA: Moth_2047
            MTU: Rv0808(purF)
            MTC: MT0829(purF)
            MBO: Mb0831(purF)
            MBB: BCG_0860(purF)
            MLE: ML2206(purF)
            MPA: MAP0638(purF)
            MAV: MAV_0747(purF)
            MSM: MSMEG_5800(purF) MSMEG_6261
            MMC: Mmcs_4541
            CGL: NCgl2495(cgl2584)
            CGB: cg2857(purF)
            CEF: CE2476(purF)
            CDI: DIP1920(purF)
            CJK: jk0358(purF)
            NFA: nfa5790(purF)
            RHA: RHA1_ro04840(purF)
            SCO: SCO4086(purF)
            SMA: SAV4135(purF)
            TWH: TWT723(purF)
            TWS: TW737(purF)
            LXX: Lxx22760(purF)
            CMI: CMM_0757(purF)
            AAU: AAur_3525(purF)
            PAC: PPA1970
            TFU: Tfu_2747
            FRA: Francci3_0094
            FAL: FRAAL0128(purC)
            SEN: SACE_7125(purF)
            BLO: BL1121(purF)
            BAD: BAD_0521(purF)
            RXY: Rxyl_0997
            FNU: FN0987
            RBA: RB5050
            TDE: TDE2407(purF)
            LIL: LA4092(purF)
            LIC: LIC13262(purF)
            LBJ: LBJ_0194(purF)
            LBL: LBL_2889(purF)
            SYN: sll0757(purF)
            SYW: SYNW0004(purF)
            SYC: syc1493_c(purF)
            SYF: Synpcc7942_0004
            SYD: Syncc9605_0004
            SYE: Syncc9902_0004
            SYG: sync_0004(purF)
            SYR: SynRCC307_0004(purF)
            SYX: SynWH7803_0004(purF)
            CYA: CYA_0277(purF)
            CYB: CYB_2131(purF)
            TEL: tlr1684(purF)
            GVI: glr2114(purF)
            ANA: all3651
            AVA: Ava_3637
            PMA: Pro0004(purF)
            PMM: PMM0004(purF)
            PMT: PMT0004(purF)
            PMN: PMN2A_1331
            PMI: PMT9312_0004
            PMB: A9601_00031(purF)
            PMC: P9515_00031(purF)
            PMF: P9303_00031(purF)
            PMG: P9301_00031(purF)
            PMH: P9215_00031
            PME: NATL1_00031(purF)
            BTH: BT_4582
            BFR: BF1301
            BFS: BF1288(purF)
            SRU: SRU_0897(purF)
            CHU: CHU_2612(purF) CHU_3495(purF)
            GFO: GFO_3378(purF)
            FJO: Fjoh_1130
            FPS: FP0196(purF)
            CTE: CT0313(purF)
            CCH: Cag_0525
            PLT: Plut_0425
            DET: DET1415(purF)
            DEH: cbdb_A1377(purF)
            DRA: DR_0220
            DGE: Dgeo_0063
            TTH: TTC1156
            TTJ: TTHA1520
            AAE: aq_1175(purF)
            TMA: TM1247
            MMP: MMP1146(purF)
            MMQ: MmarC5_0439
            MAC: MA3193(purF)
            MBA: Mbar_A3498
            MMA: MM_0341
            MBU: Mbur_2179
            MHU: Mhun_3061
            MST: Msp_1122(purF)
            MSI: Msm_1704
            MKA: MK1063(gltB_2) MK1649(purF)
            HAL: VNG1493G(purF)
            HMA: rrnAC0797(purF)
            HWA: HQ2893A(purF)
            NPH: NP4312A(purF)
            TAC: Ta1242
            TVO: TVN0354
            PTO: PTO0669
            PAB: PAB0151(purF)
            PFU: PF0154
            TKO: TK0211
            RCI: LRC233(purF)
            IHO: Igni_0600
            SSO: SSO0632(purF-1) SSO0633(purF-2)
            STO: ST1496 ST1497
            SAI: Saci_1611(purF-1) Saci_1612(purF-2)
            MSE: Msed_1982
            PAI: PAE0218(purF) PAE0226(purF)
            PIS: Pisl_0102 Pisl_0109
            PCL: Pcal_1884 Pcal_1893
            PAS: Pars_2177 Pars_2190
STRUCTURES  PDB: 1AO0  1ECB  1ECC  1ECF  1ECG  1ECJ  1GPH  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.14
            ExPASy - ENZYME nomenclature database: 2.4.2.14
            ExplorEnz - The Enzyme Database: 2.4.2.14
            ERGO genome analysis and discovery system: 2.4.2.14
            BRENDA, the Enzyme Database: 2.4.2.14
            CAS: 9031-82-7
///
ENTRY       EC 2.4.2.15                 Enzyme
NAME        guanosine phosphorylase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     guanosine:phosphate alpha-D-ribosyltransferase
REACTION    guanosine + phosphate = guanine + alpha-D-ribose 1-phosphate
            [RN:R02147]
ALL_REAC    R02147;
            (other) R01863
SUBSTRATE   guanosine [CPD:C00387];
            phosphate [CPD:C00009]
PRODUCT     guanine [CPD:C00242];
            alpha-D-ribose 1-phosphate [CPD:C00620]
COMMENT     Also acts on deoxyguanosine.
REFERENCE   1
  AUTHORS   Yamada, E.W.
  TITLE     The phosphorolysis of nucleosides by rabbit bone marrow.
  JOURNAL   J. Biol. Chem. 236 (1961) 3043-3046.
  ORGANISM  rabbit
PATHWAY     PATH: map00230  Purine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.15
            ExPASy - ENZYME nomenclature database: 2.4.2.15
            ExplorEnz - The Enzyme Database: 2.4.2.15
            ERGO genome analysis and discovery system: 2.4.2.15
            BRENDA, the Enzyme Database: 2.4.2.15
            CAS: 9030-28-8
///
ENTRY       EC 2.4.2.16                 Enzyme
NAME        urate-ribonucleotide phosphorylase;
            UAR phosphorylase;
            urate-ribonucleotide:phosphate D-ribosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     urate-ribonucleotide:phosphate alpha-D-ribosyltransferase
REACTION    urate D-ribonucleotide + phosphate = urate + alpha-D-ribose
            1-phosphate [RN:R02645]
ALL_REAC    R02645;
            (other) R02646
SUBSTRATE   urate D-ribonucleotide [CPD:C03312];
            phosphate [CPD:C00009]
PRODUCT     urate [CPD:C00366];
            alpha-D-ribose 1-phosphate [CPD:C00620]
REFERENCE   1
  AUTHORS   Laster, L. and Blair, A.
  TITLE     An intestinal phosphorylase for uric acid ribonucleoside.
  JOURNAL   J. Biol. Chem. 238 (1963) 3348-3357.
  ORGANISM  rat [GN:rno], pigeon, guinea pig, dog [GN:cfa]
PATHWAY     PATH: map00230  Purine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.16
            ExPASy - ENZYME nomenclature database: 2.4.2.16
            ExplorEnz - The Enzyme Database: 2.4.2.16
            ERGO genome analysis and discovery system: 2.4.2.16
            BRENDA, the Enzyme Database: 2.4.2.16
            CAS: 9030-29-9
///
ENTRY       EC 2.4.2.17                 Enzyme
NAME        ATP phosphoribosyltransferase;
            phosphoribosyl-ATP pyrophosphorylase;
            adenosine triphosphate phosphoribosyltransferase;
            phosphoribosyladenosine triphosphate:pyrophosphate
            phosphoribosyltransferase;
            phosphoribosyl ATP synthetase;
            phosphoribosyl ATP:pyrophosphate phosphoribosyltransferase;
            phosphoribosyl-ATP:pyrophosphate-phosphoribosyl phosphotransferase;
            phosphoribosyladenosine triphosphate pyrophosphorylase;
            phosphoribosyladenosine triphosphate synthetase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     1-(5-phospho-D-ribosyl)-ATP:diphosphate
            phospho-alpha-D-ribosyl-transferase
REACTION    1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP +
            5-phospho-alpha-D-ribose 1-diphosphate [RN:R01071]
ALL_REAC    R01071
SUBSTRATE   1-(5-phospho-D-ribosyl)-ATP;
            diphosphate [CPD:C00013]
PRODUCT     ATP [CPD:C00002];
            5-phospho-alpha-D-ribose 1-diphosphate [CPD:C00119]
REFERENCE   1  [PMID:13682989]
  AUTHORS   AMES BN, MARTIN RG, GARRY BJ.
  TITLE     The first step of histidine biosynthesis.
  JOURNAL   J. Biol. Chem. 236 (1961) 2019-26.
  ORGANISM  Salmonella typhimurium
REFERENCE   2
  AUTHORS   Martin, R.G.
  TITLE     The phosphorolysis of nucleosides by rabbit bone marrow: The nature
            of feedback inhibition by histidine.
  JOURNAL   J. Biol. Chem. 238 (1963) 257-268.
  ORGANISM  Salmonella typhimurium
REFERENCE   3  [PMID:5337591]
  AUTHORS   Voll MJ, Appella E, Martin RG.
  TITLE     Purification and composition studies of phosphoribosyladenosine
            triphosphate:pyrophosphate phosphoribosyltransferase, the first
            enzyme of histidine biosynthesis.
  JOURNAL   J. Biol. Chem. 242 (1967) 1760-7.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00340  Histidine metabolism
ORTHOLOGY   KO: K00765  ATP phosphoribosyltransferase
GENES       HSA: 5631(PRPS1) 5634(PRPS2)
            OSA: 4331530
            SCE: YER055C(HIS1)
            AGO: AGOS_ADL081C
            PIC: PICST_67165(HIS1)
            CGR: CAGL0L00759g
            YLI: YALI0C05170g(HIS1)
            SPO: SPAC25G10.05c(his1)
            ANI: AN3748.2
            AFM: AFUA_7G04500
            AOR: AO090005000135
            CNE: CND01510
            UMA: UM06017.1
            ECO: b2019(hisG)
            ECJ: JW2001(hisG)
            ECE: Z3181(hisG)
            ECS: ECs2820
            ECC: c2546(hisG)
            ECI: UTI89_C2292(hisG)
            ECP: ECP_2062
            ECV: APECO1_1116(hisG)
            ECW: EcE24377A_2310(hisG)
            ECX: EcHS_A2158(hisG)
            STY: STY2280(hisG)
            STT: t0802(hisG)
            SPT: SPA0800(hisG)
            SEC: SC2081(hisG)
            STM: STM2071(hisG)
            YPE: YPO1549(hisG)
            YPK: y2620(hisG)
            YPM: YP_1438(hisG)
            YPA: YPA_0845
            YPN: YPN_2430
            YPP: YPDSF_1427
            YPS: YPTB1562(hisG)
            YPI: YpsIP31758_2428(hisG)
            SFL: SF2081(hisG)
            SFX: S2202(hisG)
            SFV: SFV_2079(hisG)
            SSN: SSON_2090(hisG)
            SBO: SBO_0845(hisG)
            SDY: SDY_2222(hisG)
            ECA: ECA2582(hisG)
            PLU: plu1570(hisG)
            BUC: BU099(hisG)
            BAS: BUsg092(hisG)
            BAB: bbp093(hisG)
            BCC: BCc_063(hisG)
            SGL: SG1130
            ENT: Ent638_2631
            SPE: Spro_1616
            BFL: Bfl462(hisG)
            BPN: BPEN_477(hisG)
            HIT: NTHI0599(hisG)
            HIP: CGSHiEE_00650(hisG)
            HIQ: CGSHiGG_05585(hisG)
            PMU: PM1195(hisG)
            MSU: MS1893(hisG)
            APL: APL_2019(hisG)
            ASU: Asuc_0630
            XFA: XF2220
            XFT: PD1268(hisG)
            XCC: XCC1808(hisG)
            XCB: XC_2381
            XCV: XCV1874(hisG)
            XAC: XAC1828(hisG)
            XOO: XOO2255(hisG)
            XOM: XOO_2118(XOO2118)
            VCH: VC1132
            VCO: VC0395_A0702(hisG)
            VVU: VV1_2920
            VVY: VV1350
            VPA: VP1137
            VFI: VF1012(hisG)
            PPR: PBPRA1092(hisG)
            PAE: PA4449(hisG)
            PAU: PA14_57800(hisG)
            PAP: PSPA7_5021(hisG)
            PPU: PP_0965(hisG)
            PPF: Pput_1004
            PST: PSPTO_4439(hisG)
            PSB: Psyr_4134(hisG)
            PSP: PSPPH_4138(hisG)
            PFL: PFL_0928(hisG)
            PFO: Pfl_0870
            PEN: PSEEN1106(hisG)
            PMY: Pmen_0883
            PAR: Psyc_1903(hisG)
            PCR: Pcryo_2193
            PRW: PsycPRwf_0502
            ACI: ACIAD0661(hisG) ACIAD1257(hisZ)
            SON: SO_2074(hisG)
            SDN: Sden_1618
            SFR: Sfri_1720
            SAZ: Sama_1941
            SBL: Sbal_2425
            SBM: Shew185_2418
            SLO: Shew_2197
            SPC: Sputcn32_2178
            SSE: Ssed_2541
            SPL: Spea_2456
            SHE: Shewmr4_1800
            SHM: Shewmr7_2177
            SHN: Shewana3_1854
            SHW: Sputw3181_1831
            ILO: IL1834(hisG)
            CPS: CPS_3889(hisG)
            PHA: PSHAb0494(hisG)
            PAT: Patl_2880
            SDE: Sde_3169
            PIN: Ping_1657
            MAQ: Maqu_2702
            LPN: lpg1200(hisG)
            LPF: lpl1208(hisG)
            LPP: lpp1202(hisG)
            MCA: MCA1964(hisG)
            TCX: Tcr_0988
            NOC: Noc_2779
            AEH: Mlg_2216
            HHA: Hhal_2113
            HCH: HCH_05306(hisG)
            CSA: Csal_2213
            ABO: ABO_0561
            MMW: Mmwyl1_2407
            AHA: AHA_2196(hisG)
            BCI: BCI_0405(hisG)
            RMA: Rmag_0601
            VOK: COSY_0555(hisG)
            NME: NMB1579
            NMA: NMA1768(hisG)
            NMC: NMC1499(hisG)
            NGO: NGO1238(hisG)
            CVI: CV_0610(hisG)
            REU: Reut_A3112(hisG)
            REH: H16_A3417(hisG)
            RME: Rmet_3249
            BMA: BMA2715(hisG)
            BMV: BMASAVP1_A3238(hisG)
            BML: BMA10299_A1787(hisG)
            BMN: BMA10247_2766(hisG)
            BXE: Bxe_A0397
            BVI: Bcep1808_0403
            BUR: Bcep18194_A3522(hisG)
            BCN: Bcen_2683
            BCH: Bcen2424_0424
            BAM: Bamb_0342
            BPS: BPSL3140(hisG)
            BPM: BURPS1710b_2345(hisZ) BURPS1710b_3694(hisG)
            BPL: BURPS1106A_3725(hisG)
            BPD: BURPS668_3667(hisG)
            BTE: BTH_I2994(hisG)
            PNU: Pnuc_0106
            BPE: BP3767(hisG)
            BPA: BPP4266(hisG)
            BBR: BB4853(hisG)
            RFR: Rfer_2945
            POL: Bpro_0803
            PNA: Pnap_0695
            AAV: Aave_1023
            AJS: Ajs_0759
            VEI: Veis_4452
            MPT: Mpe_A0830
            HAR: HEAR3070(hisG)
            MMS: mma_3289(hisG)
            NEU: NE0871(hisG)
            NET: Neut_1205
            NMU: Nmul_A0820
            EBA: ebA1300(hisG)
            AZO: azo0817(hisG)
            DAR: Daro_3388
            TBD: Tbd_1890(hisG)
            MFA: Mfla_0247
            HHE: HH0149(hisG)
            WSU: WS0804(hisG)
            TDN: Tmden_0889
            CJE: Cj1597(hisG)
            CJR: CJE1769(hisG)
            CJJ: CJJ81176_1584(hisG)
            CJU: C8J_1499(hisG)
            CJD: JJD26997_1950(hisG)
            CFF: CFF8240_1151(hisG)
            CCV: CCV52592_0991(hisG)
            CHA: CHAB381_1637(hisG)
            CCO: CCC13826_0216(hisG) CCC13826_0608
            ABU: Abu_0322(hisG)
            NIS: NIS_1169(hisG)
            SUN: SUN_0424
            GSU: GSU1530(hisG) GSU3101(hisG-2)
            GME: Gmet_0383 Gmet_1898(hisG)
            GUR: Gura_3242 Gura_4058
            PCA: Pcar_2689
            PPD: Ppro_2945 Ppro_3043
            DVU: DVU0114(hisG)
            DVL: Dvul_2849
            DDE: Dde_3566
            DPS: DP2638
            ADE: Adeh_0363
            AFW: Anae109_4216
            MXA: MXAN_4230(hisG)
            SAT: SYN_03109 SYN_03698
            SFU: Sfum_4055
            PUB: SAR11_0480(hisG)
            MLO: mlr6931
            MES: Meso_0419
            PLA: Plav_0600
            SME: SMc00917(hisG)
            SMD: Smed_0405
            ATU: Atu0679(hisG)
            ATC: AGR_C_1215
            RET: RHE_CH00823(hisG)
            RLE: RL0879(hisG)
            BME: BMEII1054
            BMF: BAB2_0183
            BMS: BRA0189
            BMB: BruAb2_0184(hisG)
            OAN: Oant_3019
            BJA: blr7525(hisG)
            BRA: BRADO6107(hisG)
            BBT: BBta_1680(hisG)
            RPA: RPA1149(hisG)
            RPB: RPB_1845
            RPC: RPC_4718
            RPD: RPD_4118
            RPE: RPE_0871
            NWI: Nwi_2566(hisG)
            NHA: Nham_3188
            XAU: Xaut_4747
            CCR: CC_3511
            SIL: SPO0669
            SIT: TM1040_0505
            RSP: RSP_3549(hisG)
            RSH: Rsph17029_3232
            RSQ: Rsph17025_3952
            JAN: Jann_0947
            RDE: RD1_4063(hisG)
            PDE: Pden_1923
            MMR: Mmar10_1615
            HNE: HNE_0579(hisG)
            ZMO: ZMO1550(hisG) ZMO1686(hisG)
            NAR: Saro_2919
            SAL: Sala_2027
            SWI: Swit_2777
            ELI: ELI_02600
            GOX: GOX0990
            GBE: GbCGDNIH1_1032
            ACR: Acry_2694
            RRU: Rru_A2772
            MAG: amb3343
            MGM: Mmc1_3194
            ABA: Acid345_3682
            SUS: Acid_3856
            BSU: BG12601(hisG)
            BHA: BH3583(hisG)
            BAN: BA1425(hisG)
            BAR: GBAA1425(hisG)
            BAA: BA_1945(hisG)
            BAT: BAS1316
            BCE: BC1405(hisG)
            BCA: BCE_1525(hisG)
            BCZ: BCZK1290(hisG)
            BCY: Bcer98_1128
            BTK: BT9727_1289(hisG)
            BTL: BALH_1260
            BLI: BL03407(hisG)
            BLD: BLi03737(hisG)
            BCL: ABC3049(hisG)
            BAY: RBAM_032130(hisG)
            BPU: BPUM_3127(hisG)
            OIH: OB0552
            GKA: GK3076(hisG)
            SAU: SA2471(hisG)
            SAV: SAV2679(hisG)
            SAM: MW2598(hisG)
            SAR: SAR2761(hisG)
            SAS: SAS2564
            SAC: SACOL2703(hisG)
            SAB: SAB2555c(hisG)
            SAA: SAUSA300_2612(hisG)
            SAO: SAOUHSC_03014
            SAJ: SaurJH9_2703
            SAH: SaurJH1_2760
            SEP: SE0271
            SER: SERP2306(hisG)
            SSP: SSP0430
            LMO: lmo0568(hisG)
            LMF: LMOf2365_0597(hisG)
            LIN: lin0577(hisG)
            LWE: lwe0534(hisG)
            LLA: L0066(hisG)
            LLM: llmg_1296(hisG)
            SMU: SMU.1271(hisG)
            SSA: SSA_1447(hisG)
            SGO: SGO_1409(hisG)
            LPL: lp_2560(hisG)
            LCA: LSEI_1434
            STH: STH2838(hisG)
            CAC: CAC0936(hisG)
            CNO: NT01CX_1061(hisG)
            CTH: Cthe_2881
            CDF: CD1548(hisG)
            CBA: CLB_1586(hisG)
            CBH: CLC_1597(hisG)
            CBF: CLI_1648(hisG)
            CBE: Cbei_1316
            CKL: CKL_1294(hisG)
            AMT: Amet_0571
            CHY: CHY_1084(hisG)
            DSY: DSY3914
            DRM: Dred_2356
            SWO: Swol_1769
            CSC: Csac_2026
            TTE: TTE2139(hisG)
            MTA: Moth_2036
            MTU: Rv2121c(hisG)
            MTC: MT2181(hisG)
            MBO: Mb2145c(hisG)
            MBB: BCG_2138c(hisG)
            MLE: ML1310(hisG)
            MPA: MAP1846c(hisG)
            MAV: MAV_2393(hisG)
            MSM: MSMEG_4180(hisG)
            MVA: Mvan_3470
            MGI: Mflv_3057
            MMC: Mmcs_3145
            MKM: Mkms_3207
            MJL: Mjls_3157
            CGL: NCgl1447(hisG)
            CGB: cg1698(hisG)
            CEF: CE1634(hisG)
            CDI: DIP1256(hisG)
            CJK: jk0952(hisG)
            NFA: nfa31850(hisG)
            RHA: RHA1_ro00854(hisG)
            SCO: SCO1438(hisG)
            SMA: SAV6907(hisG)
            LXX: Lxx11220(hisG)
            ART: Arth_1680
            AAU: AAur_1831(hisG)
            PAC: PPA1417(hisG)
            NCA: Noca_2452
            TFU: Tfu_0174(hisG)
            FRA: Francci3_4316
            FAL: FRAAL6590(hisG)
            ACE: Acel_1270
            KRA: Krad_2975
            SEN: SACE_2238(hisG)
            STP: Strop_1880
            BLO: BL0751(hisG)
            BAD: BAD_0795(hisG)
            RXY: Rxyl_1101
            RBA: RB5603(hisG)
            LIL: LA1262(hisG)
            LIC: LIC12445(hisG)
            LBJ: LBJ_0938(hisG)
            LBL: LBL_2095(hisG)
            SYN: sll0900(hisG)
            SYW: SYNW1542(hisG)
            SYC: syc0754_d(hisG)
            SYF: Synpcc7942_0783
            SYD: Syncc9605_0967(hisG)
            SYE: Syncc9902_0880(hisG)
            SYG: sync_1940(hisG)
            SYR: SynRCC307_0838(hisG)
            SYX: SynWH7803_0695(hisG)
            CYA: CYA_1232(hisG)
            CYB: CYB_1550(hisG)
            TEL: tll0180(hisG)
            GVI: glr3383(hisG)
            ANA: alr1965
            AVA: Ava_4346(hisG)
            PMA: Pro0562(hisG)
            PMM: PMM0560(hisG)
            PMT: PMT1193(hisG)
            PMN: PMN2A_1890(hisG)
            PMI: PMT9312_0560
            PMB: A9601_06161(hisG)
            PMC: P9515_06241(hisG)
            PMF: P9303_08231(hisG)
            PMG: P9301_05861(hisG)
            PME: NATL1_06151(hisG)
            TER: Tery_0578
            BTH: BT_0200
            BFR: BF3190
            BFS: BF3030(hisG)
            SRU: SRU_0727(hisG)
            CHU: CHU_1862(hisG)
            GFO: GFO_1764(hisG)
            FJO: Fjoh_2878
            FPS: FP0960(hisG)
            CTE: CT1988(hisG)
            CCH: Cag_0211(hisG)
            CPH: Cpha266_2357
            PVI: Cvib_0307
            PLT: Plut_0241(hisG)
            DEH: cbdb_A828
            RRS: RoseRS_3180
            RCA: Rcas_2907
            DRA: DR_1445
            DGE: Dgeo_0782
            TTH: TTC1866
            TTJ: TTHA0128
            AAE: aq_1613(hisG)
            TMA: TM1042
            TPT: Tpet_1708
            MMP: MMP0947(hisG)
            MMQ: MmarC5_0754
            MMZ: MmarC7_0194
            MAE: Maeo_0137
            MVN: Mevan_0242
            MAC: MA0217(hisG)
            MBA: Mbar_A1312
            MMA: MM_1503
            MBU: Mbur_1331
            MTP: Mthe_0080
            MHU: Mhun_0922 Mhun_2050
            MEM: Memar_0837 Memar_2370
            MBN: Mboo_0134 Mboo_1065
            MST: Msp_0178(hisG)
            MSI: Msm_1261
            MKA: MK0365(hisG)
            AFU: AF0590(hisG)
            HAL: VNG2247G(hisG)
            HMA: rrnAC2835(hisG)
            HWA: HQ3412A(hisG)
            NPH: NP1062A(hisG)
            PTO: PTO1337
            PFU: PF1658
            TKO: TK0243
            RCI: RCIX583(hisG)
            IHO: Igni_0754
            SSO: SSO0593(hisG)
            STO: ST1459
            SAI: Saci_1575(hisG)
            MSE: Msed_1943
            PAI: PAE0961(hisG)
            PIS: Pisl_1213
            PCL: Pcal_0134
            PAS: Pars_0160
STRUCTURES  PDB: 1H3D  1NH7  1NH8  1O63  1O64  1Q1K  1USY  1VE4  1Z7M  1Z7N  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.17
            ExPASy - ENZYME nomenclature database: 2.4.2.17
            ExplorEnz - The Enzyme Database: 2.4.2.17
            ERGO genome analysis and discovery system: 2.4.2.17
            BRENDA, the Enzyme Database: 2.4.2.17
            CAS: 9031-46-3
///
ENTRY       EC 2.4.2.18                 Enzyme
NAME        anthranilate phosphoribosyltransferase;
            phosphoribosyl-anthranilate pyrophosphorylase;
            PRT;
            anthranilate 5-phosphoribosylpyrophosphate
            phosphoribosyltransferase;
            anthranilate phosphoribosylpyrophosphate phosphoribosyltransferase;
            phosphoribosylanthranilate pyrophosphorylase;
            phosphoribosylanthranilate transferase;
            anthranilate-PP-ribose-P phosphoribosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     N-(5-phospho-D-ribosyl)-anthranilate:diphosphate
            phospho-alpha-D-ribosyltransferase
REACTION    N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate +
            5-phospho-alpha-D-ribose 1-diphosphate [RN:R01073]
ALL_REAC    R01073
SUBSTRATE   N-(5-phospho-D-ribosyl)-anthranilate;
            diphosphate [CPD:C00013]
PRODUCT     anthranilate [CPD:C00108];
            5-phospho-alpha-D-ribose 1-diphosphate [CPD:C00119]
COMMENT     In some organisms, this enzyme is part of a multifunctional protein
            together with one or more other components of the system for
            biosynthesis of tryptophan [EC 4.1.1.48 (indole-3-glycerol-phosphate
            synthase), EC 4.1.3.27 (anthranilate synthase), EC 4.2.1.20
            (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate
            isomerase)].
REFERENCE   1
  AUTHORS   Creighton, T.E. and Yanofsky, C.
  TITLE     Chorismate to tryptophan (Escherichia coli) - Anthranilate
            synthetase, PR transferase, PRA isomerase, InGP synthetase,
            tryptophan synthetase.
  JOURNAL   Methods Enzymol. 17A (1970) 365-380.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:16526091]
  AUTHORS   Kung CC, Huang WN, Huang YC, Yeh KC.
  TITLE     Proteomic survey of copper-binding proteins in Arabidopsis roots by
            immobilized metal affinity chromatography and mass spectrometry.
  JOURNAL   Proteomics. 6 (2006) 2746-58.
REFERENCE   3  [PMID:4886290]
  AUTHORS   Ito J, Yanofsky C.
  TITLE     Anthranilate synthetase, an enzyme specified by the tryptophan
            operon of Escherichia coli: Comparative studies on the complex and
            the subunits.
  JOURNAL   J. Bacteriol. 97 (1969) 734-42.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:5842052]
  AUTHORS   Wegman J, DeMoss JA.
  TITLE     The enzymatic conversion of anthranilate to indolylglycerol
            phosphate in Neurospora crassa.
  JOURNAL   J. Biol. Chem. 240 (1965) 3781-8.
  ORGANISM  Neurospora crassa [GN:dncr]
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
            PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K00766  anthranilate phosphoribosyltransferase
GENES       ATH: AT5G17990(TRP1)
            OSA: 4331468
            CME: CMC098C
            SCE: YDR354W(TRP4)
            AGO: AGOS_AER239W
            PIC: PICST_34016(TRP4)
            CGR: CAGL0A02574g
            SPO: SPBC16G5.08
            ANI: AN3634.2
            AFM: AFUA_4G11980
            AOR: AO090003001011
            CNE: CNA07880
            UMA: UM00518.1
            ECO: b1263(trpD)
            ECJ: JW1255(trpD)
            ECE: Z2548(trpD)
            ECS: ECs1835
            ECC: c1729(trpD)
            ECI: UTI89_C1532(trpD)
            ECP: ECP_1311
            ECV: APECO1_424(trpD)
            STY: STY1327(trpD)
            STT: t1636(trpD)
            SPT: SPA1153(trpD)
            SEC: SC1720(trpD)
            STM: STM1724(trpD)
            YPE: YPO2206(trpD)
            YPM: YP_2004(trpD1)
            YPA: YPA_1566
            YPN: YPN_1675
            YPP: YPDSF_0927
            YPS: YPTB2128(trpD)
            YPI: YpsIP31758_1934(trpD)
            SFL: SF1266(trpD)
            SFX: S1352(trpD)
            SFV: SFV_1277(trpD)
            SSN: SSON_1880(trpD)
            SBO: SBO_1803(trpD)
            SDY: SDY_1331(trpD)
            ECA: ECA2298(trpD)
            PLU: plu2464(trpD)
            BUC: BU280(trpD)
            BAS: BUsg269(trpD)
            BAB: bbp260(trpD)
            SGL: SG1400
            SPE: Spro_2669
            BFL: Bfl428(trpD)
            BPN: BPEN_440(trpD)
            HIT: NTHI1764(trpD)
            HIP: CGSHiEE_04510(trpD)
            HIQ: CGSHiGG_00710(trpD)
            PMU: PM0581(trpD)
            MSU: MS1151(trpD)
            APL: APL_1165(trpD)
            ASU: Asuc_1270
            XFA: XF0212
            XFT: PD0172(trpD)
            XCC: XCC0469(trpD)
            XCB: XC_0483
            XCV: XCV0516(trpD)
            XAC: XAC0480(trpD)
            XOO: XOO4161(trpD)
            XOM: XOO_3936(XOO3936)
            VCH: VC1172
            VCO: VC0395_A0794(trpD)
            VVU: VV1_3066
            VVY: VV1219
            VPA: VP1958
            VFI: VF1030 VF1031 VFA0741
            PPR: PBPRA2488
            PAE: PA0650(trpD)
            PAU: PA14_08350(trpD)
            PPU: PP_0421(trpD)
            PPF: Pput_0454
            PST: PSPTO_0593(trpD)
            PSB: Psyr_4580
            PSP: PSPPH_0673(trpD)
            PFL: PFL_5622(trpD)
            PFO: Pfl_5114
            PEN: PSEEN0448(trpD)
            PAR: Psyc_0973(trpD)
            PCR: Pcryo_1442
            PRW: PsycPRwf_1647
            ACI: ACIAD2462(trpD)
            ACB: A1S_2359
            SON: SO_3021(trpD)
            SDN: Sden_2452
            SFR: Sfri_1427
            SAZ: Sama_2131
            SBL: Sbal_2703
            SBM: Shew185_2724
            SLO: Shew_2253
            SPC: Sputcn32_2405
            SSE: Ssed_1684
            SPL: Spea_1588
            SHE: Shewmr4_1460
            SHM: Shewmr7_1526
            SHN: Shewana3_1518
            SHW: Sputw3181_1603
            ILO: IL1753(trpD)
            CPS: CPS_3524(trpD)
            PHA: PSHAa1291(trpD)
            PAT: Patl_2831
            SDE: Sde_0753
            PIN: Ping_1058
            MAQ: Maqu_3519
            CBD: COXBU7E912_1251(trpD)
            LPN: lpg0834(trpD)
            LPF: lpl0865(trpD)
            LPP: lpp0896(trpD)
            MCA: MCA2586(trpD)
            FTW: FTW_2023(trpD)
            FTH: FTH_1881(trpD)
            FTA: FTA_2078(trpD) FTA_2079
            FTN: FTN_1776(trpD)
            TCX: Tcr_0268
            NOC: Noc_2496
            AEH: Mlg_2248
            HHA: Hhal_0086 Hhal_2080
            HCH: HCH_06127
            CSA: Csal_2320
            ABO: ABO_2025(trpD)
            AHA: AHA_2925(trpD)
            VOK: COSY_0117
            NME: NMB0967
            NMA: NMA1164(trpD)
            NMC: NMC0948(trpD)
            NGO: NGO1203
            CVI: CV_2173(trpD)
            RSO: RSc0378(trpD3) RSc2884(trpD1) RSp0681(trpD2)
            REU: Reut_A3025
            REH: H16_A0356(trpD2) H16_A3321(trpD1)
            RME: Rmet_3180
            BMA: BMAA0531(trpD)
            BMV: BMASAVP1_0646(trpD)
            BML: BMA10299_0942(trpD)
            BMN: BMA10247_A1912(trpD)
            BXE: Bxe_A0459
            BVI: Bcep1808_0509
            BUR: Bcep18194_A3619 Bcep18194_A6141
            BCN: Bcen_2573
            BCH: Bcen2424_0532
            BAM: Bamb_0437
            BPS: BPSL3052(trpD)
            BPM: BURPS1710b_3577(trpD)
            BPL: BURPS1106A_3585(trpD)
            BPD: BURPS668_3558(trpD)
            BTE: BTH_I2911(trpD)
            BPE: BP3262(trpD)
            BPA: BPP4158(trpD)
            BBR: BB4628(trpD)
            RFR: Rfer_3602
            POL: Bpro_4452
            PNA: Pnap_3650
            AJS: Ajs_0369
            VEI: Veis_1210
            MPT: Mpe_A3461
            HAR: HEAR0198(trpD) HEAR0436
            MMS: mma_0233(trpD1) mma_0486(trpD2)
            NEU: NE0013(trpD)
            NET: Neut_0134
            NMU: Nmul_A2563
            EBA: ebA4200(trpD)
            AZO: azo3323(trpD)
            DAR: Daro_3476
            TBD: Tbd_2223
            MFA: Mfla_2467
            HPY: HP1280(trpD)
            HPJ: jhp1201(trpD)
            HPA: HPAG1_1232
            HHE: HH0314(trpD)
            HAC: Hac_0016(trpD)
            WSU: WS2097
            TDN: Tmden_1151
            CJE: Cj0346(trpD)
            CJR: CJE0395(trpD)
            CJU: C8J_0323(trpD)
            CFF: CFF8240_0351
            CCV: CCV52592_1684 CCV52592_1709
            CCO: CCC13826_0023
            ABU: Abu_0368 Abu_1276(trpD)
            NIS: NIS_0849(trpD)
            SUN: SUN_1586
            GSU: GSU2381(trpD)
            GME: Gmet_2495
            PCA: Pcar_0732
            DVU: DVU0467(trpD)
            DVL: Dvul_2470
            DDE: Dde_3482
            LIP: LI0414(trpD)
            DPS: DP1621
            ADE: Adeh_4054
            MXA: MXAN_6062(trpD)
            SAT: SYN_01945 SYN_02590
            SFU: Sfum_0769 Sfum_1774
            PUB: SAR11_0923(trpD)
            MLO: mlr0614
            MES: Meso_1638
            PLA: Plav_3172
            SME: SMc00235(trpD)
            SMD: Smed_1408
            ATU: Atu1687(trpD)
            ATC: AGR_C_3100
            RET: RHE_CH02174(trpD)
            RLE: RL2493(trpD)
            BME: BMEI0844
            BMF: BAB1_1163
            BMS: BR1140(trpD)
            BMB: BruAb1_1146(trpD)
            BOV: BOV_1099(trpD)
            OAN: Oant_2049
            BJA: bll2049(trpD) blr4809(trpD)
            BRA: BRADO4109(trpD)
            BBT: BBta_4482(trpD)
            RPA: RPA2890(trpD)
            RPB: RPB_2797
            RPC: RPC_2467
            RPD: RPD_2828
            RPE: RPE_2591
            NWI: Nwi_1837
            NHA: Nham_1734
            XAU: Xaut_4376
            CCR: CC_1898
            SIL: SPO2150(trpD)
            SIT: TM1040_1140
            RSP: RSP_2001(trpD)
            RSH: Rsph17029_0711
            RSQ: Rsph17025_3098
            JAN: Jann_1879
            RDE: RD1_3210(trpD)
            PDE: Pden_2137
            MMR: Mmar10_1400
            HNE: HNE_1788(trpD)
            ZMO: ZMO0200(trpD)
            NAR: Saro_2023
            SAL: Sala_0836
            SWI: Swit_3226
            ELI: ELI_06510
            GOX: GOX2287
            GBE: GbCGDNIH1_0820
            RRU: Rru_A1896
            MAG: amb2862
            MGM: Mmc1_1120
            ABA: Acid345_3885
            SUS: Acid_3379
            BSU: BG10288(trpD)
            BHA: BH1660(trpD)
            BAN: BA1250(trpD)
            BAR: GBAA1250(trpD)
            BAA: BA_1783
            BAT: BAS1158
            BCE: BC1234
            BCA: BCE_1358(trpD)
            BCZ: BCZK1132(trpD)
            BTK: BT9727_1138(trpD)
            BLI: BL02774(trpD)
            BLD: BLi02402(trpD)
            BCL: ABC1896(trpD)
            BAY: RBAM_020830(trpD)
            BPU: BPUM_1998(trpD)
            OIH: OB0525
            GKA: GK2203(trpD)
            SAU: SA1201(trpD)
            SAV: SAV1369(trpD)
            SAM: MW1256(trpD)
            SAS: SAS1309
            SAC: SACOL1405(trpD)
            SAB: SAB1224(trpD)
            SAA: SAUSA300_1264(trpD)
            SAO: SAOUHSC_01368
            SAJ: SaurJH9_1430
            SAH: SaurJH1_1459
            SEP: SE1050
            SER: SERP0939(trpD)
            SHA: SH1540(trpD)
            SSP: SSP1377
            LMO: lmo1631(trpD)
            LMF: LMOf2365_1653(trpD)
            LIN: lin1672(trpD)
            LWE: lwe1647(trpD)
            LLA: L0052(trpD)
            LLC: LACR_1558
            LLM: llmg_1032(trpD)
            SPN: SP_1815
            SPR: spr1635(trpD)
            SPD: SPD_1600(trpD)
            SMU: SMU.534(trpD)
            STC: str1591(trpD)
            STL: stu1591(trpD)
            SSA: SSA_0634(trpD)
            SGO: SGO_0659(trpD)
            LPL: lp_1654(trpD)
            LCA: LSEI_0078
            STH: STH1409
            CAC: CAC3161(trpD)
            CKL: CKL_1276(trpD)
            CHY: CHY_1585(trpD)
            DSY: DSY3199
            SWO: Swol_0358
            CSC: Csac_2234
            TTE: TTE1581(trpD)
            MTA: Moth_1340
            MTU: Rv2192c(trpD)
            MTC: MT2248(trpD)
            MBO: Mb2215c(trpD)
            MBB: BCG_2208c(trpD)
            MLE: ML0883(trpD)
            MPA: MAP1931c(trpD)
            MAV: MAV_2301(trpD)
            MSM: MSMEG_4258(trpD)
            MVA: Mvan_3556
            MGI: Mflv_2957
            MMC: Mmcs_3290
            MKM: Mkms_3352
            MJL: Mjls_3301
            CGL: NCgl2929(trpD)
            CGB: cg3361(trpD)
            CEF: CE2870(trpD)
            CDI: DIP2354(trpD)
            CJK: jk0718(trpD)
            NFA: nfa17240(trpD)
            RHA: RHA1_ro01128(trpD)
            SCO: SCO2147(SC6G10.20c) SCO3212(SCE8.05c)
            SMA: SAV6056(trpD)
            LXX: Lxx09860(trpD)
            CMI: CMM_1833(trpD)
            ART: Arth_2208
            AAU: AAur_2206(trpD)
            NCA: Noca_3131
            TFU: Tfu_1024
            FRA: Francci3_3114
            FAL: FRAAL5120(trpD)
            ACE: Acel_0966
            KRA: Krad_3249
            SEN: SACE_1681(trpD)
            STP: Strop_3298
            BLO: BL1422(trpD)
            BAD: BAD_1019(trpD)
            RXY: Rxyl_2095
            RBA: RB410(trpD)
            CCA: CCA00563(trpD)
            CFE: CF0439(trpD)
            LIL: LA1140(trpD)
            LIC: LIC12541(trpD)
            LBJ: LBJ_2157(trpD)
            LBL: LBL_2151(trpD)
            SYN: slr1867(trpD)
            SYW: SYNW1025(trpD) SYNW2492
            SYC: syc1969_d(trpD)
            SYF: Synpcc7942_2123
            SYD: Syncc9605_1151
            SYE: Syncc9902_1308
            SYG: sync_1637(trpD)
            SYR: SynRCC307_1332(trpD)
            SYX: SynWH7803_1060(trpD) SynWH7803_2497(trpD)
            CYA: CYA_0630(trpD)
            CYB: CYB_0050(trpD)
            TEL: tll1714(trpD)
            GVI: gll2795(trpD)
            ANA: all0409(trpD) alr1153(trpD)
            AVA: Ava_4408 Ava_4534
            PMA: Pro0744(trpD)
            PMM: PMM0952(trpD)
            PMT: PMT0654(trpD)
            PMN: PMN2A_0258
            PMI: PMT9312_0847
            PMB: A9601_09081
            PMC: P9515_10351
            PMF: P9303_15761 P9303_29911
            PMG: P9301_09061
            PME: NATL1_09271 NATL1_21741
            TER: Tery_2308
            BTH: BT_0530
            BFR: BF2653
            SRU: SRU_1666(trpD)
            CHU: CHU_3292(trpD)
            GFO: GFO_2670(trpD)
            FJO: Fjoh_4893
            FPS: FP0511(trpD)
            CTE: CT1609(trpD)
            CCH: Cag_1741
            CPH: Cpha266_0584
            PVI: Cvib_0811 Cvib_1394
            PLT: Plut_1143 Plut_1604
            DET: DET0126(trpD-1) DET1483(trpD-2)
            DEH: cbdb_A1444(trpD) cbdb_A146(trpD)
            RRS: RoseRS_1452
            RCA: Rcas_2153
            DRA: DR_1767
            DGE: Dgeo_0986
            TTH: TTC1491
            TTJ: TTHA1842
            AAE: aq_196(trpD1) aq_209(trpD2)
            TMA: TM0141
            MMP: MMP1007(trpD)
            MMQ: MmarC5_0587
            MMZ: MmarC7_0249
            MAE: Maeo_1116
            MVN: Mevan_0332
            MAC: MA2989(trpD)
            MBA: Mbar_A3624
            MMA: MM_2820
            MBU: Mbur_2363
            MHU: Mhun_1787
            MST: Msp_1076(trpD)
            MSI: Msm_1144
            MKA: MK0678(trpD)
            AFU: AF1604(trpD)
            HAL: VNG1649G(trpD1)
            HMA: rrnAC1520(trpD3) rrnAC3306(trpD1)
            HWA: HQ3122A(trpD) HQ3169A(trpD)
            NPH: NP0532A(trpD_2) NP3062A(trpD_3) NP3338A(trpD)
            TAC: Ta0804
            TVO: TVN1026
            PTO: PTO0344
            PAB: PAB2044(trpD)
            PFU: PF1710
            TKO: TK0253
            APE: APE_2551
            SSO: SSO0890(trpD)
            STO: ST1231
            SAI: Saci_1423(trpD)
            MSE: Msed_1689
            PAI: PAE2461
            PIS: Pisl_1915
            PCL: Pcal_1208
STRUCTURES  PDB: 1GXB  1KGZ  1KHD  1O17  1V8G  1VQU  1ZVW  1ZXY  1ZYK  2BPQ  
                 2ELC  2GVQ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.18
            ExPASy - ENZYME nomenclature database: 2.4.2.18
            ExplorEnz - The Enzyme Database: 2.4.2.18
            ERGO genome analysis and discovery system: 2.4.2.18
            BRENDA, the Enzyme Database: 2.4.2.18
            CAS: 9059-35-2
///
ENTRY       EC 2.4.2.19                 Enzyme
NAME        nicotinate-nucleotide diphosphorylase (carboxylating);
            quinolinate phosphoribosyltransferase (decarboxylating);
            quinolinic acid phosphoribosyltransferase;
            QAPRTase;
            NAD+ pyrophosphorylase;
            nicotinate mononucleotide pyrophosphorylase (carboxylating);
            quinolinic phosphoribosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     nicotinate-nucleotide:diphosphate phospho-alpha-D-ribosyltransferase
            (carboxylating)
REACTION    nicotinate D-ribonucleotide + diphosphate + CO2 =
            pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate
            [RN:R03348]
ALL_REAC    R03348
SUBSTRATE   nicotinate D-ribonucleotide [CPD:C01185];
            diphosphate [CPD:C00013];
            CO2 [CPD:C00011]
PRODUCT     pyridine-2,3-dicarboxylate [CPD:C03722];
            5-phospho-alpha-D-ribose 1-diphosphate [CPD:C00119]
REFERENCE   1  [PMID:14165928]
  AUTHORS   GHOLSON RK, UEDA I, OGASAWARA N, HENDERSON LM.
  TITLE     THE ENZYMATIC CONVERSION OF QUINOLINATE TO NICOTINIC ACID
            MONONUCLEOTIDE IN MAMMALIAN LIVER.
  JOURNAL   J. Biol. Chem. 239 (1964) 1208-14.
  ORGANISM  cow [GN:bta], rat [GN:rno]
REFERENCE   2  [PMID:5320648]
  AUTHORS   Packman PM, Jakoby WB.
  TITLE     Crystalline quinolinate phosphoribosyltransferase.
  JOURNAL   J. Biol. Chem. 240 (1965) 4107-8.
  ORGANISM  cow [GN:bta], rat [GN:rno], Escherichia coli [GN:eco]
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K00767  nicotinate-nucleotide pyrophosphorylase (carboxylating)
GENES       HSA: 23475(QPRT)
            MMU: 67375(Qprt)
            CFA: 607664(QPRT)
            XLA: 446628(qprt)
            SPU: 759072(LOC759072)
            ATH: AT2G01350(QPT)
            OSA: 4347802
            CME: CMO013C
            SCE: YFR047C(BNA6)
            AGO: AGOS_AFR271W
            PIC: PICST_36541(BNA6)
            ANI: AN3431.2
            AFM: AFUA_3G05730
            AOR: AO090020000041
            CNE: CNC03970
            DDI: DDB_0231362
            ECO: b0109(nadC)
            ECJ: JW0105(nadC)
            ECE: Z0119(nadC)
            ECS: ECs0113
            ECC: c0128(nadC)
            ECI: UTI89_C0117(nadC)
            ECP: ECP_0109
            ECV: APECO1_1880(nadC)
            ECW: EcE24377A_0111(nadC)
            ECX: EcHS_A0113
            STY: STY0167(nadC)
            STT: t0151(nadC)
            SPT: SPA0149(nadC)
            SEC: SC0144(nadC)
            STM: STM0145(nadC)
            YPE: YPO3424(nadC)
            YPK: y0762(nadC)
            YPM: YP_0260(nadC)
            YPA: YPA_2926
            YPN: YPN_0664
            YPP: YPDSF_2930
            YPS: YPTB0708(nadC)
            YPI: YpsIP31758_3369(nadC)
            SFL: SF0106(nadC)
            SFX: S0108(nadC)
            SFV: SFV_0100(nadC)
            SSN: SSON_0117(nadC)
            SBO: SBO_0098(nadC)
            SDY: SDY_0139(nadC)
            ECA: ECA3797(nadC)
            PLU: plu3637(nadC)
            WBR: WGLp324(nadC)
            SGL: SG0464
            ENT: Ent638_0653
            KPN: KPN_00111(nadC)
            SPE: Spro_0779
            XFA: XF1925
            XFT: PD0867(nadC)
            XCC: XCC2505(nadC)
            XCB: XC_1611
            XCV: XCV2831(nadC)
            XAC: XAC2681(nadC)
            XOO: XOO3212(nadC)
            XOM: XOO_3045(XOO3045)
            VCH: VC2422
            VCO: VC0395_A1998(nadC)
            VVU: VV1_1627
            VVY: VV2777
            VPA: VP2522
            VFI: VF2184
            PPR: PBPRA3199
            PAE: PA4524(nadC)
            PAU: PA14_58700(nadC)
            PAP: PSPA7_5142(nadC)
            PPU: PP_0787(nadC)
            PPF: Pput_0810
            PST: PSPTO_0948(nadC)
            PSB: Psyr_0815
            PSP: PSPPH_0841(nadC)
            PFL: PFL_0851(nadC)
            PFO: Pfl_0785
            PEN: PSEEN0925(nadC)
            PMY: Pmen_0778
            PAR: Psyc_0634(nadC)
            PCR: Pcryo_0602
            PRW: PsycPRwf_1962
            ACI: ACIAD0062(nadC)
            ACB: A1S_0044
            SDN: Sden_3387
            SFR: Sfri_3781
            SAZ: Sama_0371
            SBL: Sbal_3917
            SBM: Shew185_3939
            SLO: Shew_3435
            SPC: Sputcn32_3421
            SSE: Ssed_0427
            SPL: Spea_0415
            SHE: Shewmr4_0424
            SHM: Shewmr7_3603
            SHN: Shewana3_0422
            SHW: Sputw3181_0522
            ILO: IL0454(nadC)
            CPS: CPS_4813(nadC)
            PHA: PSHAa0386(nadC)
            PAT: Patl_3345
            SDE: Sde_0874
            PIN: Ping_1158
            MAQ: Maqu_0952
            CBU: CBU_0098(nadC)
            CBD: COXBU7E912_2010(nadC)
            LPN: lpg0807(nadC)
            LPF: lpl0840(nadC)
            LPP: lpp0869(nadC)
            MCA: MCA3101(nadC)
            FTU: FTT1468c(nadC)
            FTF: FTF1468c(nadC)
            FTW: FTW_0630(nadC)
            FTL: FTL_1389
            FTH: FTH_1351(nadC)
            FTA: FTA_1476(nadC)
            FTN: FTN_0693(nadC)
            TCX: Tcr_1367
            NOC: Noc_0865
            AEH: Mlg_2097
            HHA: Hhal_2042
            HCH: HCH_01917(nadC)
            CSA: Csal_0853
            ABO: ABO_0617(nadC)
            MMW: Mmwyl1_2308
            AHA: AHA_3867(nadC)
            BCI: BCI_0513(nadC)
            RMA: Rmag_0106
            VOK: COSY_0109(nadC)
            NME: NMB0396
            NMA: NMA2088(nadC)
            NMC: NMC1770(nadC)
            NGO: NGO1565
            CVI: CV_1588(nadC)
            RSO: RSc2448(nadC)
            REU: Reut_A2736 Reut_B3748
            REH: H16_A3037(nadC) H16_B0560
            RME: Rmet_2873
            BMA: BMA2235(nadC)
            BMV: BMASAVP1_A2650(nadC)
            BML: BMA10299_A1025(nadC)
            BMN: BMA10247_2104(nadC)
            BXE: Bxe_A0814
            BVI: Bcep1808_2583 Bcep1808_4270
            BUR: Bcep18194_A5837
            BCN: Bcen_1894
            BCH: Bcen2424_2505
            BAM: Bamb_2552
            BPS: BPSL0913(nadC)
            BPM: BURPS1710b_1132(nadC)
            BPL: BURPS1106A_0979(nadC)
            BPD: BURPS668_0975(nadC)
            BTE: BTH_I0777(nadC)
            PNU: Pnuc_1104
            BPE: BP3725(nadC)
            BPA: BPP3842(nadC)
            BBR: BB4286(nadC)
            RFR: Rfer_1318
            POL: Bpro_0902
            PNA: Pnap_0937 Pnap_4632
            AAV: Aave_3851
            AJS: Ajs_3498
            MPT: Mpe_A1553
            HAR: HEAR1090(nadC)
            MMS: mma_1999
            NEU: NE2122(nadC)
            NMU: Nmul_A1543
            EBA: ebA4956(nadC)
            AZO: azo2079(nadC)
            DAR: Daro_2380
            TBD: Tbd_0814
            MFA: Mfla_2117
            HPY: HP1355
            HPA: HPAG1_1302
            HHE: HH1833(nadC)
            HAC: Hac_0200(nadC)
            WSU: WS1273(nadC)
            TDN: Tmden_0668
            CFF: CFF8240_0821(nadC)
            ABU: Abu_2036(nadC)
            NIS: NIS_0415(nadC)
            SUN: SUN_1979(nadC)
            GSU: GSU1936(nadC)
            GME: Gmet_1988
            GUR: Gura_2818
            PCA: Pcar_1972
            PPD: Ppro_0653
            DVU: DVU1807(nadC)
            DVL: Dvul_1353
            DDE: Dde_1831
            LIP: LI0360(nadC)
            BBA: Bd2762(nadC)
            DPS: DP1795
            ADE: Adeh_2389
            MXA: MXAN_4459(nadC)
            SAT: SYN_02885
            SFU: Sfum_0193
            AMA: AM1297(nadC)
            APH: APH_0016(nadC)
            ERU: Erum0140(nadC)
            ERW: ERWE_CDS_00010(nadC)
            ERG: ERGA_CDS_00010(nadC)
            ECN: Ecaj_0006
            ECH: ECH_0026(nadC)
            NSE: NSE_0122(nadC)
            PUB: SAR11_0619(nadC)
            MLO: mll5833 mll6272 mll9102
            MES: Meso_2555
            PLA: Plav_0732
            SME: SMc02598(nadC)
            SMD: Smed_0701
            ATU: Atu4096(nadC)
            ATC: AGR_L_1516
            RET: RHE_PE00439(nadC)
            RLE: pRL110615(nadC)
            OAN: Oant_0431
            BJA: bll2540(nadC)
            BRA: BRADO4529(nadC)
            BBT: BBta_4755(nadC)
            RPA: RPA1053(nadC)
            RPB: RPB_1105
            RPC: RPC_4340
            RPD: RPD_1227
            RPE: RPE_4402
            NWI: Nwi_2426
            NHA: Nham_2821
            XAU: Xaut_0148 Xaut_1181
            CCR: CC_2915
            SIL: SPO3245(nadC)
            SIT: TM1040_2248
            RSH: Rsph17029_4167
            RDE: RD1_1527(nadC)
            PDE: Pden_4430
            MMR: Mmar10_0789
            HNE: HNE_0689(nadC)
            ZMO: ZMO1870(nadC)
            NAR: Saro_0226
            SAL: Sala_1150
            SWI: Swit_4716
            ELI: ELI_12670
            GBE: GbCGDNIH1_0642
            RRU: Rru_A1432
            MAG: amb2953 amb3885
            MGM: Mmc1_1475
            ABA: Acid345_0133
            SUS: Acid_7560
            BSU: BG10868(nadC)
            BHA: BH1219(nadC)
            BAN: BA4661(nadC)
            BAR: GBAA4661(nadC)
            BAA: BA_5100
            BAT: BAS4326
            BCE: BC4422
            BCA: BCE_4514(nadC)
            BCZ: BCZK4174(nadC)
            BCY: Bcer98_3144
            BTK: BT9727_4163(nadC)
            BTL: BALH_4010(nadC)
            BLI: BL01154(nadC)
            BLD: BLi02913(nadC)
            BCL: ABC1548(nadC)
            BAY: RBAM_024910
            BPU: BPUM_2426
            GKA: GK2600
            LMO: lmo2024(nadC)
            LMF: LMOf2365_2049(nadC)
            LIN: lin2132(nadC)
            SPY: SPy_0197(nadC)
            SPZ: M5005_Spy_0170(nadC)
            SPM: spyM18_1346
            SPG: SpyM3_1013(nadC)
            SPS: SPs0845
            SPH: MGAS10270_Spy0173(nadC)
            SPI: MGAS10750_Spy1186(nadC)
            SPJ: MGAS2096_Spy0181(nadC)
            SPK: MGAS9429_Spy0172(nadC)
            SPF: SpyM50773(nadC)
            SPA: M6_Spy1061
            SPB: M28_Spy0168(nadC)
            SPN: SP_2016
            SPR: spr1829(nadC)
            SPD: SPD_1826(nadC)
            CAC: CAC1023(nadC)
            CPE: CPE0396(nadC)
            CPF: CPF_0384(nadC)
            CPR: CPR_0378(nadC)
            CNO: NT01CX_0088(nadC)
            CTH: Cthe_2354
            CDF: CD2370(nadC)
            CBO: CBO1447(nadC)
            CBA: CLB_1472(nadC)
            CBH: CLC_1484(nadC)
            CBF: CLI_1531(nadC)
            CBE: Cbei_0794
            CKL: CKL_0750(nadC) CKL_3642
            AMT: Amet_0019
            CHY: CHY_2372(nadC)
            DSY: DSY0214(nadC)
            DRM: Dred_0165
            SWO: Swol_0107
            CSC: Csac_1779
            MTU: Rv1596(nadC)
            MTC: MT1632(nadC)
            MBO: Mb1622(nadC)
            MBB: BCG_1634(nadC)
            MLE: ML1227(nadC)
            MPA: MAP1291(nadC)
            MAV: MAV_3189(nadC)
            MSM: MSMEG_3201(nadC)
            MVA: Mvan_2800
            MGI: Mflv_3617
            MMC: Mmcs_3066
            MKM: Mkms_3126
            MJL: Mjls_3083
            CGL: NCgl1023(cgl1068)
            CGB: cg1215(nadC)
            CEF: CE1115
            CDI: DIP2259(nadC)
            CJK: jk0784(nadC)
            NFA: nfa18390(nadC)
            RHA: RHA1_ro01036(nadC)
            SCO: SCO3381(nadC)
            SMA: SAV4689(nadC)
            LXX: Lxx16510(nadC)
            ART: Arth_2558
            AAU: AAur_2532(nadC)
            NCA: Noca_0463
            TFU: Tfu_2883
            FRA: Francci3_4378
            FAL: FRAAL6673(nadC)
            ACE: Acel_0214
            KRA: Krad_3559
            SEN: SACE_5801(nadC)
            BLO: BL1376(nadC)
            RXY: Rxyl_0106
            FNU: FN0010
            RBA: RB6623(nadC)
            LIL: LA3086(nadC)
            LIC: LIC11011(nadC)
            LBJ: LBJ_0841(nadC)
            LBL: LBL_2241(nadC)
            SYN: slr0936(nadC)
            SYW: SYNW2320(nadC)
            SYC: syc0591_c(nadC)
            SYF: Synpcc7942_0951
            SYD: Syncc9605_2452
            SYE: Syncc9902_2135
            SYG: sync_2692(nadC)
            SYR: SynRCC307_2240(nadC)
            SYX: SynWH7803_2337(nadC)
            CYA: CYA_0945(nadC)
            CYB: CYB_2483(nadC)
            TEL: tll1713(nadC)
            GVI: gll0888(nadC)
            ANA: all2091
            AVA: Ava_3136
            PMA: Pro0213(nadC)
            PMM: PMM0188(nadC)
            PMT: PMT2073(nadC)
            PMN: PMN2A_1555
            PMI: PMT9312_0190
            PMB: A9601_02061(nadC)
            PMC: P9515_02171(nadC)
            PMF: P9303_27531(nadC)
            PMG: P9301_02081(nadC)
            PMH: P9215_02061
            PME: NATL1_02631(nadC)
            TER: Tery_4352
            BTH: BT_1560
            BFR: BF1469
            BFS: BF1400(nadC)
            PGI: PG1577(nadC)
            SRU: SRU_1913(nadC)
            CHU: CHU_3729(nadC)
            GFO: GFO_1102(nadC)
            FJO: Fjoh_3488
            FPS: FP1856(nadC)
            CTE: CT1936(nadC)
            CCH: Cag_0234
            CPH: Cpha266_0455 Cpha266_2293
            PVI: Cvib_0108 Cvib_0335 Cvib_1491
            PLT: Plut_0270
            DET: DET1382(nadC)
            DEH: cbdb_A1336(nadC)
            DEB: DehaBAV1_1192
            RRS: RoseRS_0439
            RCA: Rcas_1005
            DGE: Dgeo_1163
            TTH: TTC0621
            TTJ: TTHA0985
            AAE: aq_869(nadC)
            TMA: TM1645
            TPT: Tpet_1146
            TME: Tmel_1584
            MMP: MMP0877(nadC)
            MMQ: MmarC5_0685
            MAE: Maeo_0914
            MVN: Mevan_0043
            MAC: MA0322(nadC) MA0955(nadC)
            MBA: Mbar_A1304 Mbar_A1867
            MMA: MM_1577 MM_2070
            MBU: Mbur_0259 Mbur_1682
            MTP: Mthe_0241
            MHU: Mhun_2352
            MEM: Memar_0821
            MBN: Mboo_0499
            MST: Msp_0410(nadC)
            MSI: Msm_0491
            MKA: MK0446(nadC)
            HAL: VNG1884G(nadC)
            HMA: rrnAC2241 rrnAC3408(nadC1)
            NPH: NP2414A(nadC)
            PAB: PAB2347(nadC)
            PFU: PF1978
            TKO: TK0218
            RCI: RCIX225(nadC)
            IHO: Igni_1350
            HBU: Hbut_0679
            SSO: SSO0996
            STO: ST1198
            SAI: Saci_0547
            PAI: PAE3114
            PIS: Pisl_0060
STRUCTURES  PDB: 1QAP  1QPN  1QPO  1QPQ  1QPR  1X1O  2B7N  2B7P  2B7Q  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.19
            ExPASy - ENZYME nomenclature database: 2.4.2.19
            ExplorEnz - The Enzyme Database: 2.4.2.19
            ERGO genome analysis and discovery system: 2.4.2.19
            BRENDA, the Enzyme Database: 2.4.2.19
            CAS: 37277-74-0
///
ENTRY       EC 2.4.2.20                 Enzyme
NAME        dioxotetrahydropyrimidine phosphoribosyltransferase;
            dioxotetrahydropyrimidine-ribonucleotide pyrophosphorylase;
            dioxotetrahydropyrimidine phosphoribosyl transferase;
            dioxotetrahydropyrimidine ribonucleotide pyrophosphorylase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     2,4-dioxotetrahydropyrimidine-nucleotide:diphosphate
            phospho-alpha-D-ribosyltransferase
REACTION    a 2,4-dioxotetrahydropyrimidine D-ribonucleotide + diphosphate = a
            2,4-dioxotetrahydropyrimidine + 5-phospho-alpha-D-ribose
            1-diphosphate [RN:R04346]
ALL_REAC    R04346
SUBSTRATE   2,4-dioxotetrahydropyrimidine D-ribonucleotide [CPD:C04639];
            diphosphate [CPD:C00013]
PRODUCT     2,4-dioxotetrahydropyrimidine [CPD:C03919];
            5-phospho-alpha-D-ribose 1-diphosphate [CPD:C00119]
COMMENT     Acts (in the reverse direction) on uracil and other pyrimidines and
            pteridines containing a 2,4-diketo structure.
REFERENCE   1  [PMID:14235538]
  AUTHORS   HATFIELD D, WYNGAARDEN JB.
  TITLE     3-RIBOSYLPURINES. I. SYNTHESIS OF (3-RIBOSYLURIC ACID) 5'-PHOSPHATE
            AND (3-RIBOSYLXANTHINE) 5'-PHOSPHATE BY A PYRIMIDINE RIBONUCLEOTIDE
            PYROPHOSPHORYLASE OF BEEF ERYTHROCYTES.
  JOURNAL   J. Biol. Chem. 239 (1964) 2580-6.
  ORGANISM  cow [GN:bta]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.20
            ExPASy - ENZYME nomenclature database: 2.4.2.20
            ExplorEnz - The Enzyme Database: 2.4.2.20
            ERGO genome analysis and discovery system: 2.4.2.20
            BRENDA, the Enzyme Database: 2.4.2.20
            CAS: 37277-75-1
///
ENTRY       EC 2.4.2.21                 Enzyme
NAME        nicotinate-nucleotide---dimethylbenzimidazole
            phosphoribosyltransferase;
            nicotinate mononucleotide-dimethylbenzimidazole
            phosphoribosyltransferase;
            nicotinate ribonucleotide:benzimidazole (adenine)
            phosphoribosyltransferase;
            nicotinate-nucleotide:dimethylbenzimidazole
            phospho-D-ribosyltransferase;
            CobT;
            nicotinate mononucleotide (NaMN):5,6-dimethylbenzimidazole
            phosphoribosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     nicotinate-nucleotide:5,6-dimethylbenzimidazole
            phospho-D-ribosyltransferase
REACTION    beta-nicotinate D-ribonucleotide + 5,6-dimethylbenzimidazole =
            nicotinate + alpha-ribazole 5'-phosphate [RN:R04148]
ALL_REAC    R04148
SUBSTRATE   beta-nicotinate D-ribonucleotide [CPD:C01185];
            5,6-dimethylbenzimidazole [CPD:C03114]
PRODUCT     nicotinate [CPD:C00253];
            alpha-ribazole 5'-phosphate [CPD:C04778]
COMMENT     Also acts on benzimidazole, and the clostridial enzyme acts on
            adenine to form 7-alpha-D-ribosyladenine 5'-phosphate. The product
            of the reaction, alpha-ribazole 5'-phosphate, forms part of the
            corrin-biosynthesis pathway and is a substrate for EC 2.7.8.26,
            adenosylcobinamide-GDP ribazoletransferase [4]. It can also be
            dephosphorylated to form alpha-ribazole by the action of EC
            3.1.3.73, alpha-ribazole phosphatase.
REFERENCE   1  [PMID:14253445]
  AUTHORS   FRIEDMANN HC.
  TITLE     PARTIAL PURIFICATION AND PROPERTIES OF A SINGLE DISPLACEMENT
            TRANS-N-GLYCOSIDASE.
  JOURNAL   J. Biol. Chem. 240 (1965) 413-8.
  ORGANISM  Propionibacterium shermanii
REFERENCE   2  [PMID:5780835]
  AUTHORS   Friedmann HC, Fyfe JA.
  TITLE     Pseudovitamin B 12 biosynthesis. Enzymatic formation of a new
            adenylic acid, 7-alpha-D-ribofuranosyladenine 5'-phosphate.
  JOURNAL   J. Biol. Chem. 244 (1969) 1667-71.
  ORGANISM  Clostridium sticklandii
REFERENCE   3  [PMID:4238408]
  AUTHORS   Fyfe JA, Friedmann HC.
  TITLE     Vitamin B 12 biosynthesis. Enzyme studies on the formation of the
            alpha-glycosidic nucleotide precursor.
  JOURNAL   J. Biol. Chem. 244 (1969) 1659-66.
  ORGANISM  Propionibacterium shermanii, Clostridium sticklandii
REFERENCE   4  [PMID:1917841]
  AUTHORS   Cameron B, Blanche F, Rouyez MC, Bisch D, Famechon A, Couder M,
            Cauchois L, Thibaut D, Debussche L, Crouzet J.
  TITLE     Genetic analysis, nucleotide sequence, and products of two
            Pseudomonas denitrificans cob genes encoding nicotinate-nucleotide:
            dimethylbenzimidazole phosphoribosyltransferase and cobalamin
            (5'-phosphate) synthase.
  JOURNAL   J. Bacteriol. 173 (1991) 6066-73.
  ORGANISM  Pseudomonas denitrificans
REFERENCE   5  [PMID:11441022]
  AUTHORS   Cheong CG, Escalante-Semerena JC, Rayment I.
  TITLE     Structural investigation of the biosynthesis of alternative lower
            ligands for cobamides by nicotinate mononucleotide:
            5,6-dimethylbenzimidazole phosphoribosyltransferase from Salmonella
            enterica.
  JOURNAL   J. Biol. Chem. 276 (2001) 37612-20.
  ORGANISM  Salmonella enterica
REFERENCE   6  [PMID:12101181]
  AUTHORS   Cheong CG, Escalante-Semerena JC, Rayment I.
  TITLE     Capture of a labile substrate by expulsion of water molecules from
            the active site of nicotinate
            mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase
            (CobT) from Salmonella enterica.
  JOURNAL   J. Biol. Chem. 277 (2002) 41120-7.
  ORGANISM  Salmonella enterica
PATHWAY     PATH: map00740  Riboflavin metabolism
            PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K00768  nicotinate-nucleotide--dimethylbenzimidazole
                        phosphoribosyltransferase
GENES       PIC: PICST_32025(HST2)
            ECO: b1991(cobT)
            ECJ: JW1107(ycfZ) JW1969(cobT)
            ECE: Z3151(cobT)
            ECS: ECs2786
            ECC: c1396(ycfZ) c2477(cobT)
            ECI: UTI89_C2229(cobT)
            ECP: ECP_1989
            ECV: APECO1_1072(cobT) APECO1_202(ycfZ)
            ECW: EcE24377A_2273(cobT)
            ECX: EcHS_A2114(cobT)
            STY: STY2219(cobT)
            STT: t0858(cobT)
            SPT: SPA0855(cobT)
            SEC: SC2024(cobT)
            STM: STM2016(cobT)
            YEN: YE2707(cobT)
            SFL: SF2059(cobT)
            SFX: S2169(cobT)
            SFV: SFV_2063(cobT)
            SSN: SSON_2052(cobT)
            SBO: SBO_1212(cobT)
            SDY: SDY_2242(cobT)
            PLU: plu2980(cobT)
            XCC: XCC3059(cobT)
            XCB: XC_1099
            XCV: XCV3315(cobT)
            XAC: XAC3186(cobT)
            XOO: XOO1351(cobT)
            XOM: XOO_1241(XOO1241)
            VCH: VC1237
            VCO: VC0395_A0859(cobT)
            VVU: VV1_2788
            VVY: VV1474
            VPA: VP1304
            PPR: PBPRA1182
            PAE: PA1279(cobU)
            PAU: PA14_47670(cobU)
            PAP: PSPA7_4111(cobT)
            PPU: PP_1679(cobT)
            PPF: Pput_4040
            PST: PSPTO_1715(cobT)
            PSB: Psyr_3674
            PSP: PSPPH_3695(cobT)
            PFL: PFL_4424(cobT)
            PFO: Pfl_1648
            PEN: PSEEN1385
            PMY: Pmen_1757
            PCR: Pcryo_1026
            PRW: PsycPRwf_0843
            SON: SO_1035(cobT)
            SFR: Sfri_0876
            SAZ: Sama_0762
            SBL: Sbal_3364
            SBM: Shew185_0977
            SLO: Shew_0714
            SPC: Sputcn32_2961
            SSE: Ssed_3734
            SPL: Spea_3380
            SHE: Shewmr4_0842
            SHM: Shewmr7_3180
            SHN: Shewana3_3278
            SHW: Sputw3181_0986
            CPS: CPS_3659
            PHA: PSHAa2999(cobT)
            PAT: Patl_1139
            SDE: Sde_0630
            MAQ: Maqu_0270
            MCA: MCA0463(cobT)
            AEH: Mlg_2823
            HHA: Hhal_1854
            HCH: HCH_00964(cobT)
            ABO: ABO_2378(cobT)
            MMW: Mmwyl1_1409
            CVI: CV_0493(cobT)
            RSO: RSc2397(cobU)
            REU: Reut_A0658
            REH: H16_A2968(cobT1)
            RME: Rmet_2785
            BMA: BMA0688(cobT)
            BMV: BMASAVP1_A2324(cobT)
            BML: BMA10299_A2962(cobT)
            BMN: BMA10247_1636(cobT)
            BXE: Bxe_A3499
            BVI: Bcep1808_2537
            BUR: Bcep18194_A5784
            BCN: Bcen_1842
            BCH: Bcen2424_2453
            BAM: Bamb_2501
            BPS: BPSL0979
            BPM: BURPS1710b_1191(cobT)
            BPD: BURPS668_1031(cobT)
            BTE: BTH_I0837
            RFR: Rfer_2611
            POL: Bpro_0741
            PNA: Pnap_0642
            AAV: Aave_1553
            AJS: Ajs_3176
            MPT: Mpe_A2303 Mpe_A3126 Mpe_B0519(cobT)
            HAR: HEAR0954(cobT)
            MMS: mma_1087(cobT)
            EBA: ebA4008(cobT)
            AZO: azo3560(cobT)
            DAR: Daro_0148
            TBD: Tbd_2712
            MFA: Mfla_0098
            GSU: GSU3009(cobT)
            GME: Gmet_0467
            GUR: Gura_4187
            PCA: Pcar_0486(cobT)
            PPD: Ppro_2806
            DVU: DVU3279(cobT)
            DVL: Dvul_0111
            DDE: Dde_3777
            DPS: DP1952(cobT)
            SFU: Sfum_0323
            MLO: mll0563 mlr1389
            MES: Meso_1552
            PLA: Plav_1058
            SME: SMc04214(cobU)
            SMD: Smed_1603
            ATU: Atu1890(cobT)
            ATC: AGR_C_3467
            RET: RHE_CH02443(cobU)
            RLE: RL2781(cobT)
            BME: BMEI1099
            BMF: BAB1_0886(cobT)
            BMS: BR0867(cobT)
            BMB: BruAb1_0879(cobT)
            BOV: BOV_0859(cobT-2)
            OAN: Oant_2360
            BJA: blr3276(cobU)
            BRA: BRADO4918
            BBT: BBta_3133
            RPA: RPA0712(cobT) RPA2094(cobT1)
            RPB: RPB_0742 RPB_3282
            RPC: RPC_3748
            RPD: RPD_0640 RPD_2324
            RPE: RPE_2229 RPE_3845
            BHE: BH08100(cobT1)
            BBK: BARBAKC583_0851
            XAU: Xaut_3321
            CCR: CC_1309
            SIL: SPO1423(cobU)
            SIT: TM1040_0578
            RSP: RSP_2428(cobT)
            RSH: Rsph17029_1091
            RSQ: Rsph17025_1056
            JAN: Jann_3305
            RDE: RD1_1827(cobU)
            PDE: Pden_1567
            HNE: HNE_1510 HNE_2095
            NAR: Saro_0328
            GBE: GbCGDNIH1_0669
            RRU: Rru_A0667
            MAG: amb0542
            MGM: Mmc1_3279
            BHA: BH0284
            GKA: GK1793
            SSA: SSA_0512
            LRE: Lreu_1695
            CAC: CAC1372(cobT)
            CPE: CPE1034(cobT)
            CPF: CPF_1289(cobT)
            CPR: CPR_1108(cobT)
            CTC: CTC02290(cobT)
            CNO: NT01CX_2077
            CTH: Cthe_1297
            CDF: CD3439(cobT)
            CBE: Cbei_1262
            CKL: CKL_2908(cobT)
            AMT: Amet_0464
            CHY: CHY_0480(cobT)
            DSY: DSY2114(cobT)
            DRM: Dred_2728
            SWO: Swol_1405
            MTA: Moth_1101 Moth_1721
            MTU: Rv2207(cobT)
            MTC: MT2263(cobT)
            MBO: Mb2230(cobT)
            MBB: BCG_2223(cobT)
            MLE: ML0868(cobT)
            MPA: MAP1948(cobT)
            MAV: MAV_2283
            MSM: MSMEG_4275
            MVA: Mvan_3571
            MGI: Mflv_2942
            MMC: Mmcs_3305
            MKM: Mkms_3367
            MJL: Mjls_3316
            CGL: NCgl2120(cgl2200)
            CGB: cg2414(cobT)
            CEF: CE2092
            CDI: DIP1634(cobT)
            CJK: jk0711(cobT)
            NFA: nfa17000(cobT)
            RHA: RHA1_ro01145(cobT)
            SCO: SCO2175(SC5F7.26)
            SMA: SAV6030(cobT1)
            PAC: PPA0441
            NCA: Noca_2512 Noca_2886
            FRA: Francci3_3130
            FAL: FRAAL5141(cobT)
            ACE: Acel_0940
            KRA: Krad_3274
            SEN: SACE_1650(cobT)
            STP: Strop_3546
            RXY: Rxyl_0647
            FNU: FN0910
            RBA: RB8404(cobT)
            TDE: TDE0880(cobT)
            LIL: LA4204
            LIC: LIC13356(cobT)
            LBJ: LBJ_2826(cobT)
            LBL: LBL_0245(cobT)
            BFR: BF2486
            BFS: BF2519
            PGI: PG0702
            FPS: FP1460(bluB)
            CTE: CT0946(cobT)
            CCH: Cag_1058
            CPH: Cpha266_0999
            PVI: Cvib_0822
            PLT: Plut_1132
            DET: DET0657(cobT-1) DET0691(cobT-2)
            DEH: cbdb_A641(cobT)
            DEB: DehaBAV1_0626
            RRS: RoseRS_0559
            RCA: Rcas_0647
            DRA: DR_A0240
            DGE: Dgeo_2872
            TTH: TT_P0005
            TTJ: TTHB048
            TME: Tmel_0695 Tmel_0854
            FNO: Fnod_1365
            HWA: HQ1408A(cobT)
            NPH: NP0736A(cobT)
            PTO: PTO0212
STRUCTURES  PDB: 1D0S  1D0V  1JH8  1JHA  1JHM  1JHP  1JHQ  1JHR  1JHU  1JHV  
                 1JHX  1JHY  1L4B  1L4E  1L4F  1L4G  1L4H  1L4K  1L4L  1L4M  
                 1L4N  1L5F  1L5K  1L5L  1L5M  1L5N  1L5O  1WX1  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.21
            ExPASy - ENZYME nomenclature database: 2.4.2.21
            ExplorEnz - The Enzyme Database: 2.4.2.21
            ERGO genome analysis and discovery system: 2.4.2.21
            BRENDA, the Enzyme Database: 2.4.2.21
            CAS: 37277-76-2
///
ENTRY       EC 2.4.2.22                 Enzyme
NAME        xanthine phosphoribosyltransferase;
            Xan phosphoribosyltransferase;
            xanthosine 5'-phosphate pyrophosphorylase;
            xanthylate pyrophosphorylase;
            xanthylic pyrophosphorylase;
            XMP pyrophosphorylase;
            5-phospho-alpha-D-ribose-1-diphosphate:xanthine
            phospho-D-ribosyltransferase;
            9-(5-phospho-beta-D-ribosyl)xanthine:diphosphate
            5-phospho-alpha-D-ribosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     XMP:diphosphate 5-phospho-alpha-D-ribosyltransferase
REACTION    XMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate +
            xanthine [RN:R02142]
ALL_REAC    R02142;
            (other) R01229
SUBSTRATE   XMP [CPD:C00655];
            diphosphate [CPD:C00013]
PRODUCT     5-phospho-alpha-D-ribose 1-diphosphate [CPD:C00119];
            xanthine [CPD:C00385]
REFERENCE   1  [PMID:4910918]
  AUTHORS   Krenitsky TA, Neil SM, Miller RL.
  TITLE     Guanine and xanthine phosphoribosyltransfer activities of
            Lactobacillus casei and Escherichia coli. Their relationship to
            hypoxanthine and adenine phosphoribosyltransfer activities.
  JOURNAL   J. Biol. Chem. 245 (1970) 2605-11.
  ORGANISM  Lactobacillus casei [GN:lca], Escherichia coli [GN:eco]
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K00769  xanthine phosphoribosyltransferase
GENES       ECO: b0238(gpt)
            ECJ: JW0228(gpt)
            ECE: Z0299(gpt)
            ECS: ECs0265
            ECC: c0384(gpt)
            ECI: UTI89_C0278(gpt)
            ECP: ECP_0267
            ECV: APECO1_1731(gpt)
            ECW: EcE24377A_0270(gpt)
            ECX: EcHS_A0265(gpt)
            STY: STY0362(gpt)
            STT: t2533(gpt)
            SPT: SPA2438(gpt)
            SEC: SC0318(gpt)
            STM: STM0317(gpt)
            YPE: YPO3225(gpt)
            YPK: y0963(gpt)
            YPM: YP_0708(gpt)
            YPA: YPA_2717
            YPN: YPN_0868
            YPP: YPDSF_2854
            YPS: YPTB0901(gpt)
            YPI: YpsIP31758_3153(gpt)
            SFL: SF0286(gpt)
            SFX: S0307(gpt)
            SFV: SFV_0292(gpt)
            SSN: SSON_0280(gpt)
            SBO: SBO_0244(gpt)
            SDY: SDY_0479(gpt)
            ECA: ECA3466(gpt)
            PLU: plu1241(gpt)
            BUC: BU251(gpt)
            BAS: BUsg242(gpt)
            BAB: bbp232(gpt)
            SGL: SG0598
            ENT: Ent638_0764
            SPE: Spro_0964
            HIT: NTHI0796(gpt) NTHI0814(gpt2)
            HIP: CGSHiEE_08725 CGSHiEE_08800
            HIQ: CGSHiGG_06655 CGSHiGG_06750
            HDU: HD1831(gpt)
            HSO: HS_0003(gptA)
            PMU: PM1369(gpt)
            MSU: MS2117(apt)
            APL: APL_0255(gpt)
            ASU: Asuc_0179
            VCH: VC2277
            VCO: VC0395_A1867(gpt)
            VVU: VV1_0329
            VVY: VV0855
            VPA: VP0673
            VFI: VF0738
            PPR: PBPRA0836
            PAP: PSPA7_6072(xpt)
            ACI: ACIAD3164(xpt)
            SPL: Spea_2433
            ILO: IL0887(gpt)
            HCH: HCH_01089
            CSA: Csal_2097
            MMW: Mmwyl1_3674
            AHA: AHA_3424(gpt)
            HPY: HP0735(gpt)
            HPA: HPAG1_0719
            HAC: Hac_0684(gpt)
            WSU: WS2175
            TDN: Tmden_0395
            CJE: Cj1370
            CJR: CJE1562
            CJU: C8J_1289
            NIS: NIS_0649
            SUN: SUN_1505
            DVU: DVU1066(gpt)
            DVL: Dvul_1928
            DDE: Dde_1506
            DPS: DP0680
            ADE: Adeh_1006
            AFW: Anae109_3172
            SAT: SYN_03353
            MLO: mll0141
            MES: Meso_1335
            SME: SMc00945(gpt)
            SMD: Smed_1386
            ATU: Atu1731(gpt)
            ATC: AGR_C_3180(gpt)
            RET: RHE_CH01754(gpt)
            RLE: RL1948(gpt)
            BME: BMEI0940
            BMF: BAB1_1066
            BMS: BR1046
            OAN: Oant_2133
            BJA: bll5610(gpt)
            BRA: BRADO2909(gpt)
            BBT: BBta_5270(gpt)
            RPA: RPA2179
            RPB: RPB_3213
            RPC: RPC_3155
            RPD: RPD_2243
            RPE: RPE_2299
            NWI: Nwi_2188
            NHA: Nham_2590
            SIL: SPO2143(gpt)
            SIT: TM1040_1146
            RSP: RSP_2342(gpt)
            RSH: Rsph17029_1017
            RSQ: Rsph17025_1049
            JAN: Jann_2477
            RDE: RD1_3201(gpt)
            PDE: Pden_0855
            ZMO: ZMO0656(gpt)
            GOX: GOX0174
            GBE: GbCGDNIH1_1116
            ACR: Acry_2747
            RRU: Rru_A3319
            MAG: amb4308
            BPU: BPUM_1944(xpt)
            SPD: SPD_1628(xpt)
            CPF: CPF_1498(xpt)
            CBA: CLB_0360(xpt-1) CLB_1176(xpt-2)
            CBH: CLC_0375(xpt-1) CLC_1188(xpt-2)
            CBF: CLI_0387(xpt-1) CLI_1225(xpt-2)
            SYG: sync_1158
            MMA: MM_0078 MM_1262
            HWA: HQ1672A(apt) HQ2050A(apt) HQ3228A(apt)
            NPH: NP1254A(apt_2) NP1426A(apt_1)
            PTO: PTO0589
STRUCTURES  PDB: 1A95  1A96  1A97  1A98  1NUL  2FXV  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.22
            ExPASy - ENZYME nomenclature database: 2.4.2.22
            ExplorEnz - The Enzyme Database: 2.4.2.22
            ERGO genome analysis and discovery system: 2.4.2.22
            BRENDA, the Enzyme Database: 2.4.2.22
            CAS: 9023-10-3
///
ENTRY       EC 2.4.2.23                 Enzyme
NAME        deoxyuridine phosphorylase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     2'-deoxyuridine:phosphate 2-deoxy-alpha-D-ribosyltransferase
REACTION    2'-deoxyuridine + phosphate = uracil + 2-deoxy-alpha-D-ribose
            1-phosphate [RN:R02484]
ALL_REAC    R02484
SUBSTRATE   2'-deoxyuridine [CPD:C00526];
            phosphate [CPD:C00009]
PRODUCT     uracil [CPD:C00106];
            2-deoxy-alpha-D-ribose 1-phosphate [CPD:C00672]
REFERENCE   1  [PMID:16495004]
  AUTHORS   Soukhova-O'Hare GK, Roberts AM, Gozal D.
  TITLE     Impaired control of renal sympathetic nerve activity following
            neonatal intermittent hypoxia in rats.
  JOURNAL   Neurosci. Lett. 399 (2006) 181-5.
REFERENCE   2
  AUTHORS   Yamada, E.W.
  TITLE     The effect of cortisol administration on the activities of uridine
            and deoxyuridine phosphorylases of normal and regenerating rat
            liver.
  JOURNAL   Can. J. Biochem. 42 (1964) 317-325.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00240  Pyrimidine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.23
            ExPASy - ENZYME nomenclature database: 2.4.2.23
            ExplorEnz - The Enzyme Database: 2.4.2.23
            ERGO genome analysis and discovery system: 2.4.2.23
            BRENDA, the Enzyme Database: 2.4.2.23
            CAS: 37277-77-3
///
ENTRY       EC 2.4.2.24                 Enzyme
NAME        1,4-beta-D-xylan synthase;
            uridine diphosphoxylose-1,4-beta-xylan xylosyltransferase;
            1,4-beta-xylan synthase;
            xylan synthase;
            xylan synthetase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     UDP-D-xylose:1,4-beta-D-xylan 4-beta-D-xylosyltransferase
REACTION    UDP-D-xylose + (1,4-beta-D-xylan)n = UDP + (1,4-beta-D-xylan)n+1
            [RN:R03928 R06083]
ALL_REAC    R03928 R06083(G)
SUBSTRATE   UDP-D-xylose [CPD:C00190];
            (1,4-beta-D-xylan)n [CPD:C02352]
PRODUCT     UDP [CPD:C00015];
            (1,4-beta-D-xylan)n+1 [CPD:C02352]
REFERENCE   1
  AUTHORS   Bailey, R.W. and Hassid, W.Z.
  TITLE     Xylan synthesis from uridine-diphosphate-D-xylose by particulate
            preparations from immature corncobs.
  JOURNAL   Proc. Natl. Acad. Sci. USA 56 (1966) 1586-1593.
  ORGANISM  Zea mays [GN:ezma]
PATHWAY     PATH: map00500  Starch and sucrose metabolism
            PATH: map00520  Nucleotide sugars metabolism
ORTHOLOGY   KO: K00770  1,4-beta-D-xylan synthase
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.24
            ExPASy - ENZYME nomenclature database: 2.4.2.24
            ExplorEnz - The Enzyme Database: 2.4.2.24
            ERGO genome analysis and discovery system: 2.4.2.24
            BRENDA, the Enzyme Database: 2.4.2.24
            CAS: 37277-73-9
///
ENTRY       EC 2.4.2.25                 Enzyme
NAME        flavone apiosyltransferase;
            uridine diphosphoapiose-flavone apiosyltransferase;
            UDP-apiose:7-O-(beta-D-glucosyl)-flavone apiosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     UDP-apiose:5,4'-dihydroxyflavone 7-O-beta-D-glucoside
            2''-O-beta-D-apiofuranosyltransferase
REACTION    UDP-apiose + 5,7,4'-trihydroxyflavone 7-O-beta-D-glucoside = UDP +
            5,7,4'-trihydroxyflavone
            7-O-[beta-D-apiosyl-(1->2)-beta-D-glucoside] [RN:R04526]
ALL_REAC    R04526
SUBSTRATE   UDP-apiose [CPD:C01623];
            5,7,4'-trihydroxyflavone 7-O-beta-D-glucoside
PRODUCT     UDP [CPD:C00015];
            5,7,4'-trihydroxyflavone
            7-O-[beta-D-apiosyl-(1->2)-beta-D-glucoside]
COMMENT     7-O-beta-D-Glucosides of a number of flavonoids and of 4-substituted
            phenols can act as acceptors.
REFERENCE   1  [PMID:4650134]
  AUTHORS   Ortmann R, Sutter A, Grisebach H.
  TITLE     Purification and properties of udpapiose: 7-O-( -D-glucosyl)-flavone
            apiosyltransferase from cell suspension cultures of parsley.
  JOURNAL   Biochim. Biophys. Acta. 289 (1972) 293-302.
  ORGANISM  parsley
PATHWAY     PATH: map00941  Flavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.25
            ExPASy - ENZYME nomenclature database: 2.4.2.25
            ExplorEnz - The Enzyme Database: 2.4.2.25
            ERGO genome analysis and discovery system: 2.4.2.25
            BRENDA, the Enzyme Database: 2.4.2.25
            CAS: 37332-49-3
///
ENTRY       EC 2.4.2.26                 Enzyme
NAME        protein xylosyltransferase;
            UDP-D-xylose:core protein beta-D-xylosyltransferase;
            UDP-D-xylose:core protein xylosyltransferase;
            UDP-D-xylose:proteoglycan core protein beta-D-xylosyltransferase;
            UDP-xylose-core protein beta-D-xylosyltransferase;
            uridine diphosphoxylose-core protein beta-xylosyltransferase;
            uridine diphosphoxylose-protein xylosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     UDP-D-xylose:protein beta-D-xylosyltransferase
REACTION    Transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine
            hydroxy group of an acceptor protein substrate [RN:R05925]
ALL_REAC    R05925(G)
COMMENT     Involved in the biosynthesis of the linkage region of
            glycosaminoglycan chains as part of proteoglycan biosynthesis
            (chondroitin, dermatan and heparan sulfates).
REFERENCE   1  [PMID:5030630]
  AUTHORS   Stoolmiller AC, Horwitz AL, Dorfman A.
  TITLE     Biosynthesis of the chondroitin sulfate proteoglycan. Purification
            and properties of xylosyltransferase.
  JOURNAL   J. Biol. Chem. 247 (1972) 3525-32.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:11099377]
  AUTHORS   Gotting C, Kuhn J, Zahn R, Brinkmann T, Kleesiek K.
  TITLE     Molecular cloning and expression of human UDP-d-Xylose:proteoglycan
            core protein beta-d-xylosyltransferase and its first isoform XT-II.
  JOURNAL   J. Mol. Biol. 304 (2000) 517-28.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00532  Chondroitin sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00771  protein xylosyltransferase
GENES       HSA: 64131(XYLT1) 64132(XYLT2)
            PTR: 453955(XYLT1) 455118(XYLT2)
            MMU: 217119(Xylt2) 233781(Xylt1)
            RNO: 64133(Xylt1) 64134(Xylt2)
            CFA: 493990(XYLT2) 494008(XYLT1)
            BTA: 493989(XYLT2)
            GGA: 414780(XYLT2) 414781(XYLT1)
            XLA: 444363(MGC82842)
            XTR: 448400(xylt2)
            SPU: 585774(LOC585774)
            DME: Dmel_CG32300(oxt)
            CEL: Y50D4C.4(sqv-6)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.26
            ExPASy - ENZYME nomenclature database: 2.4.2.26
            ExplorEnz - The Enzyme Database: 2.4.2.26
            ERGO genome analysis and discovery system: 2.4.2.26
            BRENDA, the Enzyme Database: 2.4.2.26
            CAS: 55576-38-0
///
ENTRY       EC 2.4.2.27                 Enzyme
NAME        dTDP-dihydrostreptose---streptidine-6-phosphate
            dihydrostreptosyltransferase;
            thymidine diphosphodihydrostreptose-streptidine 6-phosphate
            dihydrostreptosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     dTDP-L-dihydrostreptose:streptidine-6-phosphate
            dihydrostreptosyltransferase
REACTION    dTDP-L-dihydrostreptose + streptidine 6-phosphate = dTDP +
            O-1,4-alpha-L-dihydrostreptosyl-streptidine 6-phosphate [RN:R04222]
ALL_REAC    R04222
SUBSTRATE   dTDP-L-dihydrostreptose [CPD:C03442];
            streptidine 6-phosphate [CPD:C01121]
PRODUCT     dTDP [CPD:C00363];
            O-1,4-alpha-L-dihydrostreptosyl-streptidine 6-phosphate [CPD:C04767]
REFERENCE   1  [PMID:6768553]
  AUTHORS   Kniep B, Grisebach H.
  TITLE     Biosynthesis of streptomycin. Purification and properties of a
            dTDP-L-dihydrostreptose: streptidine-6-phosphate
            dihydrostreptosyltransferase from Streptomyces griseus.
  JOURNAL   Eur. J. Biochem. 105 (1980) 139-44.
  ORGANISM  Streptomyces griseus
PATHWAY     PATH: map00521  Streptomycin biosynthesis
ORTHOLOGY   KO: K04341  dTDP-dihydrostreptose-streptidine-6-phosphate
                        dihydrostreptosyltransferase
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.27
            ExPASy - ENZYME nomenclature database: 2.4.2.27
            ExplorEnz - The Enzyme Database: 2.4.2.27
            ERGO genome analysis and discovery system: 2.4.2.27
            BRENDA, the Enzyme Database: 2.4.2.27
            CAS: 73699-20-4
///
ENTRY       EC 2.4.2.28                 Enzyme
NAME        S-methyl-5'-thioadenosine phosphorylase;
            5'-methylthioadenosine nucleosidase;
            5'-deoxy-5'-methylthioadenosine phosphorylase;
            MTA phosphorylase;
            MeSAdo phosphorylase;
            MeSAdo/Ado phosphorylase;
            methylthioadenosine phosphorylase;
            methylthioadenosine nucleoside phosphorylase;
            5'-methylthioadenosine:phosphate methylthio-D-ribosyl-transferase;
            S-methyl-5-thioadenosine phosphorylase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     S-methyl-5-thioadenosine:phosphate
            S-methyl-5-thio-alpha-D-ribosyl-transferase
REACTION    S-methyl-5'-thioadenosine + phosphate = adenine +
            S-methyl-5-thio-alpha-D-ribose 1-phosphate [RN:R01402]
ALL_REAC    R01402
SUBSTRATE   S-methyl-5'-thioadenosine [CPD:C00170];
            phosphate [CPD:C00009]
PRODUCT     adenine [CPD:C00147];
            S-methyl-5-thio-alpha-D-ribose 1-phosphate [CPD:C04188]
COMMENT     Also acts on 5'-deoxyadenosine and other analogues having 5'-deoxy
            groups.
REFERENCE   1  [PMID:118001]
  AUTHORS   Carteni'-Farina M, Oliva A, Romeo G, Napolitano G, De Rosa M,
            Gambacorta A, Zappia V.
  TITLE     5'-Methylthioadenosine phosphorylase from Caldariella acidophila.
            Purification and properties.
  JOURNAL   Eur. J. Biochem. 101 (1979) 317-24.
  ORGANISM  Caldariella acidophila
REFERENCE   2  [PMID:415762]
  AUTHORS   Garbers DL.
  TITLE     Demonstration of 5'-methylthioadenosine phosphorylase activity in
            various rat tissues. Some properties of the enzyme from rat lung.
  JOURNAL   Biochim. Biophys. Acta. 523 (1978) 82-93.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:5378381]
  AUTHORS   Pegg AE, Williams-Ashman HG.
  TITLE     Phosphate-stimulated breakdown of 5'-methylthioadenosine by rat
            ventral prostate.
  JOURNAL   Biochem. J. 115 (1969) 241-7.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K00772  5'-methylthioadenosine phosphorylase
GENES       HSA: 4507(MTAP)
            MMU: 66902(Mtap)
            CFA: 474729(MTAP)
            GGA: 431261(RCJMB04_34g8)
            XTR: 496996(mtap)
            DRE: 393526(mtap)
            SPU: 580214(LOC580214)
            DME: Dmel_CG4802
            CEL: B0228.7
            SPO: SPAC16C9.02c
            ANI: AN1735.2
            AFM: AFUA_6G08720
            AOR: AO090001000546
            CNE: CNA01530
            UMA: UM00570.1
            TBR: Tb927.7.7040
            TCR: 506789.280 508387.20
            LMA: LmjF05.0830
            XFA: XF2353
            XFT: PD1381(deoD)
            XCC: XCC1285(deoD)
            XCB: XC_2956
            XAC: XAC1336(deoD)
            XOO: XOO1869(deoD)
            XOM: XOO_1764(XOO1764)
            PAE: PA3004
            PAP: PSPA7_2155(mtnP)
            PST: PSPTO_3506
            PSB: Psyr_3280
            PSP: PSPPH_3200(mtaP)
            PFO: Pfl_3869
            PMY: Pmen_1591
            PAR: Psyc_1155(deoD)
            SDE: Sde_1793
            MCA: MCA1986
            NOC: Noc_0457
            HCH: HCH_02681(mtaP)
            ABO: ABO_1021(deoD)
            CVI: CV_1400 CV_3894
            RFR: Rfer_3751
            NEU: NE1754
            NMU: Nmul_A0650
            EBA: ebA6375
            DAR: Daro_1738
            TBD: Tbd_0778
            MFA: Mfla_1467
            GSU: GSU1112(mtaP)
            GME: Gmet_2684
            GUR: Gura_1582
            PCA: Pcar_2021
            PPD: Ppro_0431
            ADE: Adeh_1180
            AFW: Anae109_3381
            MXA: MXAN_6386(mtaP)
            PLA: Plav_2245
            BJA: blr0960
            BRA: BRADO6904
            BBT: BBta_0647(mtaP)
            RPA: RPA4821
            RPB: RPB_4698
            RPC: RPC_4937
            RPD: RPD_4408
            RPE: RPE_4907
            SIL: SPO3060(mtaP)
            SIT: TM1040_2324
            RSP: RSP_1837
            RSH: Rsph17029_0486
            JAN: Jann_3207
            RDE: RD1_2150
            MMR: Mmar10_0739
            HNE: HNE_0354(mtaP)
            SWI: Swit_1393
            ELI: ELI_01490
            GOX: GOX1897
            GBE: GbCGDNIH1_1721
            RRU: Rru_A0361
            MAG: amb4121
            ABA: Acid345_2626
            SUS: Acid_7058
            STH: STH1696 STH814 STH815
            CHY: CHY_1441(mtaP)
            DSY: DSY2604
            SWO: Swol_0778
            TTE: TTE1587(pnp2)
            MTA: Moth_0705
            MTU: Rv0535(pnp)
            MTC: MT0559(mtaP)
            MBO: Mb0549(pnp)
            MBB: BCG_0579(pnp)
            MPA: MAP4030(pnp)
            MAV: MAV_4610(mtaP)
            MSM: MSMEG_0990(mtaP)
            MVA: Mvan_0881
            MMC: Mmcs_0703
            MKM: Mkms_0717
            MJL: Mjls_0697
            NFA: nfa8440
            RHA: RHA1_ro02578 RHA1_ro04261
            SCO: SCO3188(SCE22.05)
            SMA: SAV3679(mtaP)
            NCA: Noca_2340
            ACE: Acel_0158
            STP: Strop_0986
            LIL: LA4248
            LIC: LIC13399(mtaP)
            LBJ: LBJ_2920
            LBL: LBL_0143
            SYN: sll0135
            SYW: SYNW1265
            SYC: syc0619_d
            SYF: Synpcc7942_0923
            SYD: Syncc9605_1392
            SYE: Syncc9902_1096
            SYG: sync_1385(mtaP)
            SYR: SynRCC307_1356
            SYX: SynWH7803_1250
            TEL: tlr1281
            GVI: gll2424
            ANA: alr4054
            AVA: Ava_1653
            PMA: Pro0332(pnp)
            PMM: PMM0301
            PMT: PMT1900
            PMN: PMN2A_1666
            PMI: PMT9312_0303
            PMB: A9601_03241
            PMC: P9515_03341
            PMF: P9303_25331
            PMG: P9301_03251
            PME: NATL1_03801
            TER: Tery_3686
            SRU: SRU_2160(mtaP)
            DET: DET0517(mtaP)
            DEH: cbdb_A482(mtaP)
            DEB: DehaBAV1_0493
            RRS: RoseRS_3664
            RCA: Rcas_1474
            AAE: aq_568(deoD)
            MJA: MJ0060
            MMP: MMP0185(mtaP)
            MAC: MA1409
            MBA: Mbar_A3594
            MMA: MM_2379
            MBU: Mbur_0182
            MSI: Msm_0665
            MKA: MK0021(pnp)
            HAL: VNG0335a VNG0335b
            HWA: HQ1262A(mtaP)
            TAC: Ta0332
            TVO: TVN0438
            PTO: PTO0942
            PAB: PAB1659(mtaP) PAB2264(mtaP)
            PFU: PF0016 PF0853
            TKO: TK1482 TK1895
            APE: APE_1885
            SMR: Smar_0749
            HBU: Hbut_0022 Hbut_0922
            SSO: SSO2343(mtaP) SSO2706(mtaP)
            STO: ST0485 ST0975
            SAI: Saci_0997 Saci_1247(mtaP)
            MSE: Msed_0689
            PAI: PAE1476 PAE3338
            PCL: Pcal_0435
STRUCTURES  PDB: 1CB0  1CG6  1JDS  1JDT  1JDU  1JDV  1JDZ  1JE0  1JE1  1JP7  
                 1JPV  1K27  1ODI  1ODJ  1ODK  1SD1  1SD2  1V4N  1WTA  2A8Y  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.28
            ExPASy - ENZYME nomenclature database: 2.4.2.28
            ExplorEnz - The Enzyme Database: 2.4.2.28
            ERGO genome analysis and discovery system: 2.4.2.28
            BRENDA, the Enzyme Database: 2.4.2.28
            CAS: 61970-06-7
///
ENTRY       EC 2.4.2.29                 Enzyme
NAME        tRNA-guanine transglycosylase;
            guanine insertion enzyme;
            tRNA transglycosylase;
            Q-insertase;
            queuine transfer ribonucleate ribosyltransferase;
            transfer ribonucleate glycosyltransferase;
            tRNA guanine transglycosidase;
            guanine, queuine-tRNA transglycosylase;
            queuine tRNA-ribosyltransferase;
            TGT;
            [tRNA]-guanine:queuine tRNA-D-ribosyltransferase;
            transfer ribonucleic acid guanine transglycosylase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     tRNA-guanine:queuine tRNA-D-ribosyltransferase
REACTION    (1) [tRNA]-guanine + queuine = [tRNA]-queuine + guanine [RN:R03789];
            (2) [tRNA]-guanine + 7-aminomethyl-7-carbaguanine =
            [tRNA]-7-aminomethyl-7-carbaguanine + guanine
ALL_REAC    R03789
SUBSTRATE   [tRNA]-guanine;
            queuine [CPD:C01449];
            7-aminomethyl-7-carbaguanine
PRODUCT     [tRNA]-queuine;
            guanine [CPD:C00242];
            [tRNA]-7-aminomethyl-7-carbaguanine
COMMENT     In eukaryotes, queuine is incorporated into tRNA directly via a
            base-exchange reaction (replacing guanine) whereas in eubacteria,
            the queuine precursor preQ1 is incorporated and ultimately modified
            to queuine [4]. In eubacteria, preQ0 can also be incorporated into
            undermodified tRNATyr and tRNAAsn containing normal guanine instead
            of queuine in the first position of the anticodon [2]. This enzyme
            acts after EC 1.7.1.13, preQ1 synthase, in the queuine-biosynthesis
            pathway.
REFERENCE   1  [PMID:721832]
  AUTHORS   Howes NK, Farkas WR.
  TITLE     Studies with a homogeneous enzyme from rabbit erythrocytes
            catalyzing the insertion of guanine into tRNA.
  JOURNAL   J. Biol. Chem. 253 (1978) 9082-7.
  ORGANISM  rabbit
REFERENCE   2  [PMID:372186]
  AUTHORS   Okada N, Noguchi S, Kasai H, Shindo-Okada N, Ohgi T, Goto T,
            Nishimura S.
  TITLE     Novel mechanism of post-transcriptional modification of tRNA.
            Insertion of bases of Q precursors into tRNA by a specific tRNA
            transglycosylase reaction.
  JOURNAL   J. Biol. Chem. 254 (1979) 3067-73.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:6986171]
  AUTHORS   Shindo-Okada N, Okada N, Ohgi T, Goto T, Nishimura S.
  TITLE     Transfer ribonucleic acid guanine transglycosylase isolated from rat
            liver.
  JOURNAL   Biochemistry. 19 (1980) 395-400.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:16401090]
  AUTHORS   Todorov KA, Garcia GA.
  TITLE     Role of aspartate 143 in Escherichia coli tRNA-guanine
            transglycosylase: alteration of heterocyclic substrate specificity.
  JOURNAL   Biochemistry. 45 (2006) 617-25.
ORTHOLOGY   KO: K00773  queuine tRNA-ribosyltransferase
GENES       HSA: 81890(QTRT1)
            PTR: 455717(QTRT1)
            MMU: 60507(Qtrt1)
            RNO: 64016(Qtrt1)
            CFA: 476711(QTRT1)
            GGA: 418351(RCJMB04_2m13)
            XLA: 446424(qtrtd1)
            XTR: 394694(MGC76136)
            DRE: 393985(zgc:66378)
            SPU: 579235(LOC579235)
            DME: Dmel_CG4947(Tgt)
            CEL: ZK829.6(tgt-1)
            OSA: 4347331
            CME: CMM013C CMN182C
            PIC: PICST_37903(UBP6)
            SPO: SPAC1687.19c SPAC2F3.13c
            ANI: AN7028.2 AN8214.2
            AFM: AFUA_4G04260 AFUA_4G04270 AFUA_5G03470
            AOR: AO090102000556 AO090206000066 AO090206000067
            ECU: ECU06_0310
            DDI: DDBDRAFT_0167339 DDBDRAFT_0184073
            PFA: PF07_0071 PFL2030w
            CPV: cgd7_830
            CHO: Chro.70102
            TAN: TA16175 TA18520
            TPV: TP01_1072
            TET: TTHERM_00494100
            TBR: Tb927.5.3520 Tb927.6.3130
            TCR: 507023.200 511751.30
            LMA: LmjF30.1800
            EHI: 17.t00053
            ECO: b0406(tgt)
            ECJ: JW0396(tgt)
            ECE: Z0505(tgt)
            ECS: ECs0457
            ECC: c0516(tgt)
            ECI: UTI89_C0428(tgt)
            ECP: ECP_0465
            ECV: APECO1_1604(tgt)
            ECW: EcE24377A_0436(tgt)
            ECX: EcHS_A0476(tgt)
            STY: STY0443(tgt)
            STT: t2458(tgt)
            SPT: SPA2318(tgt)
            SEC: SC0447(tgt)
            STM: STM0405(tgt)
            YPE: YPO3191(tgt)
            YPK: y0991(tgt)
            YPM: YP_0740(tgt)
            YPA: YPA_2686
            YPN: YPN_0896
            YPP: YPDSF_2826
            YPS: YPTB0928(tgt)
            YPI: YpsIP31758_3123(tgt)
            SFL: SF0343(vacC)
            SFX: S0351(tgt)
            SFV: SFV_0371(tgt)
            SSN: SSON_0383(tgt)
            SBO: SBO_0300(tgt)
            SDY: SDY_0328(tgt)
            ECA: ECA1120(tgt)
            PLU: plu3904(tgt)
            BUC: BU133(tgt)
            BAS: BUsg125(tgt)
            SGL: SG0646
            ENT: Ent638_0875
            KPN: KPN_00357(tgt)
            SPE: Spro_1061
            BFL: Bfl230(tgt)
            BPN: BPEN_236(tgt)
            HIN: HI0244(tgt)
            HIT: NTHI0350(tgt)
            HIP: CGSHiEE_01865(tgt)
            HDU: HD1368(tgt)
            HSO: HS_1315(tgt)
            PMU: PM0229(tgt)
            MSU: MS1559(tgt)
            APL: APL_0723(tgt)
            ASU: Asuc_1056
            XFA: XF0223
            XFT: PD0180(tgt)
            XCC: XCC2378(tgt)
            XCB: XC_1736
            XCV: XCV2695(tgt)
            XAC: XAC2513(tgt)
            XOO: XOO2484(tgt)
            XOM: XOO_2352(XOO2352)
            VCH: VC0741
            VCO: VC0395_A0270(tgt)
            VVU: VV1_0445
            VVY: VV0746
            VPA: VP0588
            VFI: VF1969
            PPR: PBPRA0743(tgt)
            PAE: PA3823(tgt)
            PAU: PA14_14600(tgt)
            PAP: PSPA7_1290(tgt)
            PPU: PP_0833(tgt)
            PPF: Pput_0863
            PST: PSPTO_1413(tgt)
            PSB: Psyr_1228
            PSP: PSPPH_1300(tgt)
            PFL: PFL_4974(tgt)
            PFO: Pfl_4621
            PEN: PSEEN1000(tgt)
            PMY: Pmen_3520
            PAR: Psyc_1524(tgt)
            PCR: Pcryo_1703
            PRW: PsycPRwf_1927
            ACI: ACIAD0590(tgt)
            SON: SO_3113(tgt)
            SDN: Sden_1401
            SFR: Sfri_2702
            SAZ: Sama_2193
            SBL: Sbal_2787
            SBM: Shew185_2807
            SLO: Shew_2337
            SPC: Sputcn32_2484
            SSE: Ssed_2892
            SPL: Spea_1470
            SHE: Shewmr4_1382
            SHM: Shewmr7_1447
            SHN: Shewana3_1435
            SHW: Sputw3181_1524
            ILO: IL2205(tgt)
            CPS: CPS_1120(tgt)
            PHA: PSHAa0319(tgt)
            PAT: Patl_1228
            SDE: Sde_1406
            PIN: Ping_2214
            MAQ: Maqu_1114
            CBU: CBU_1072(tgt)
            CBD: COXBU7E912_1174(tgt)
            LPN: lpg2003(tgt) lpg2727(tgt)
            LPF: lpl1979 lpl2653(tgt)
            LPP: lpp1984 lpp2784(tgt)
            MCA: MCA0681(tgt)
            FTU: FTT1120c(tgt)
            FTF: FTF1120c(tgt)
            FTW: FTW_1153(tgt)
            FTL: FTL_0843
            FTH: FTH_0831(tgt)
            FTA: FTA_0893(tgt)
            FTN: FTN_1100(tgt)
            TCX: Tcr_1333
            NOC: Noc_2352
            AEH: Mlg_1215
            HHA: Hhal_1699
            HCH: HCH_04469(tgt)
            CSA: Csal_2833
            ABO: ABO_0501(tgt)
            MMW: Mmwyl1_2647
            AHA: AHA_1735(tgt)
            DNO: DNO_0319(tgt)
            BCI: BCI_0597(tgt)
            VOK: COSY_0724(tgt)
            NME: NMB0719
            NMA: NMA0928(tgt)
            NMC: NMC0671(tgt)
            NGO: NGO0294
            CVI: CV_1347(tgt)
            RSO: RSc2713(tgt)
            REU: Reut_A2808
            REH: H16_A3113(tgt)
            RME: Rmet_2944
            BMA: BMA2387(tgt)
            BMV: BMASAVP1_A0303(tgt)
            BML: BMA10299_A1165(tgt)
            BMN: BMA10247_2573(tgt)
            BXE: Bxe_A3990
            BVI: Bcep1808_0683
            BUR: Bcep18194_A3810
            BCN: Bcen_0238
            BCH: Bcen2424_0722
            BAM: Bamb_0612
            BPS: BPSL2869(tgt)
            BPM: BURPS1710b_3371(tgt)
            BPL: BURPS1106A_3361(tgt)
            BPD: BURPS668_3328(tgt)
            BTE: BTH_I1278(tgt)
            PNU: Pnuc_1789
            BPE: BP1049(tgt)
            BPA: BPP1146(tgt)
            BBR: BB1362(tgt)
            RFR: Rfer_0626
            POL: Bpro_0466
            PNA: Pnap_0320
            AAV: Aave_4479
            AJS: Ajs_3870
            VEI: Veis_0596
            MPT: Mpe_A3733
            HAR: HEAR0304(tgt)
            MMS: mma_0351(tgt)
            NEU: NE1141(tgt)
            NET: Neut_1431
            NMU: Nmul_A2429
            EBA: ebA1415(tgt)
            AZO: azo0907(tgt)
            DAR: Daro_3278
            TBD: Tbd_2075
            MFA: Mfla_0514
            HPY: HP0281
            HPJ: jhp0266(tgt)
            HPA: HPAG1_0283
            HHE: HH0841(tgt)
            HAC: Hac_0541(tgt)
            WSU: WS1519(TGT)
            TDN: Tmden_0907
            CJE: Cj1010(tgt)
            CJR: CJE1090(tgt)
            CJJ: CJJ81176_1028(tgt)
            CJU: C8J_0947(tgt)
            CJD: JJD26997_0779(tgt)
            CFF: CFF8240_0980(tgt)
            CCV: CCV52592_1432(tgt)
            CHA: CHAB381_1172(tgt)
            CCO: CCC13826_0093(tgt)
            ABU: Abu_0230(tgt)
            NIS: NIS_1085(tgt)
            SUN: SUN_1008(tgt)
            GSU: GSU1175(tgt-1) GSU2619(tgt-2)
            GME: Gmet_0852 Gmet_2398
            GUR: Gura_1716 Gura_3258
            PCA: Pcar_1228 Pcar_1894
            PPD: Ppro_1800 Ppro_2484
            DVU: DVU0726(tgt)
            DVL: Dvul_2243
            DDE: Dde_2844
            LIP: LI0928(tgt)
            BBA: Bd2236(tgt)
            DPS: DP0907 DP0908
            ADE: Adeh_1428 Adeh_2542
            AFW: Anae109_1321 Anae109_2402
            MXA: MXAN_4585(tgt) MXAN_4693(tgt)
            SAT: SYN_00038
            SFU: Sfum_0565
            RPR: RP721(tgt)
            RTY: RT0707(tgt)
            RCO: RC1097(tgt)
            RFE: RF_0191(tgt)
            RBE: RBE_1258(tgt)
            RAK: A1C_05610(tgt)
            RBO: A1I_00995(tgt)
            RCM: A1E_04725(tgt)
            RRI: A1G_06090(tgt)
            WOL: WD0735(tgt)
            WBM: Wbm0593
            AMA: AM871(tgt)
            APH: APH_0314(tgt)
            ERU: Erum5750(tgt)
            ERW: ERWE_CDS_06040(tgt)
            ERG: ERGA_CDS_05950(tgt)
            ECN: Ecaj_0577
            ECH: ECH_0445(tgt)
            NSE: NSE_0016(tgt)
            PUB: SAR11_0988(tgt)
            MLO: mll0721
            MES: Meso_1406
            PLA: Plav_3054
            SME: SMc01206(tgt)
            SMD: Smed_1268
            ATU: Atu1677(tgt)
            ATC: AGR_C_3085
            RET: RHE_CH02117(tgt)
            RLE: RL2407(tgt)
            BME: BMEI0890 BMEI1003
            BMF: BAB1_1115(tgt)
            BMS: BR1091(tgt)
            BMB: BruAb1_1097(tgt)
            BOV: BOV_1052(tgt)
            OAN: Oant_2176
            BJA: bll4683(tgt)
            BRA: BRADO3990(tgt) BRADO3993(queA)
            BBT: BBta_4363(tgt) BBta_4366(queA)
            RPA: RPA2606(tgt)
            RPB: RPB_2869
            RPC: RPC_2592
            RPD: RPD_2603
            RPE: RPE_2771
            NWI: Nwi_1795
            NHA: Nham_1771
            BHE: BH10080(tgt)
            BBK: BARBAKC583_0741(tgt)
            XAU: Xaut_4271
            CCR: CC_1588
            SIL: SPO2616(tgt)
            SIT: TM1040_0770
            RSP: RSP_2804(tgt)
            RSH: Rsph17029_1495
            RSQ: Rsph17025_1156
            JAN: Jann_2520
            RDE: RD1_2952(tgt)
            PDE: Pden_1891
            MMR: Mmar10_1866
            HNE: HNE_1130(tgt)
            ZMO: ZMO0363(tgt)
            NAR: Saro_2247
            SAL: Sala_2187
            SWI: Swit_0133
            ELI: ELI_05605
            GOX: GOX1439
            GBE: GbCGDNIH1_0290
            ACR: Acry_1340
            RRU: Rru_A0280
            MAG: amb0599
            MGM: Mmc1_0605
            ABA: Acid345_0144
            SUS: Acid_1276
            BSU: BG12686(tgt)
            BHA: BH1228(tgt)
            BAN: BA4647(tgt)
            BAR: GBAA4647(tgt)
            BAA: BA_5085
            BAT: BAS4312
            BCE: BC4411
            BCA: BCE_4502(tgt)
            BCZ: BCZK4161(tgt)
            BCY: Bcer98_3134
            BTK: BT9727_4150(tgt)
            BTL: BALH_3997(tgt)
            BLI: BL01140(tgt)
            BLD: BLi02897(tgt)
            BCL: ABC1558(tgt)
            BAY: RBAM_024820(tgt)
            BPU: BPUM_2412(tgt)
            OIH: OB2033(tgt)
            GKA: GK2587
            SAU: SA1465(tgt)
            SAV: SAV1639(tgt)
            SAM: MW1589(tgt)
            SAR: SAR1719(tgt)
            SAS: SAS1575
            SAC: SACOL1694(tgt)
            SAB: SAB1508c(tgt)
            SAA: SAUSA300_1595(tgt)
            SAO: SAOUHSC_01748
            SAJ: SaurJH9_1696
            SAH: SaurJH1_1729
            SEP: SE1322
            SER: SERP1203(tgt)
            SHA: SH1282(tgt)
            SSP: SSP1120
            LMO: lmo1530
            LMF: LMOf2365_1549(tgt)
            LIN: lin1565
            LWE: lwe1543(tgt)
            LLA: L0361(tgt)
            LLC: LACR_0159
            LLM: llmg_0164(tgt)
            SPY: SPy_0203(tgt)
            SPZ: M5005_Spy_0175(tgt)
            SPM: spyM18_0189(tgt)
            SPG: SpyM3_0149(tgt)
            SPS: SPs0154
            SPH: MGAS10270_Spy0178(tgt)
            SPI: MGAS10750_Spy0170(tgt)
            SPJ: MGAS2096_Spy0186(tgt)
            SPK: MGAS9429_Spy0177(tgt)
            SPF: SpyM50157(tgt)
            SPA: M6_Spy0210
            SPB: M28_Spy0173(tgt)
            SPN: SP_2058
            SPR: spr1869(tgt)
            SPD: SPD_1868(tgt)
            SAG: SAG0396(tgt)
            SAN: gbs0432(tgt)
            SAK: SAK_0470(tgt)
            SMU: SMU.300(tgt)
            STC: str1806(tgt)
            STL: stu1806(tgt)
            SSA: SSA_0104(tgt)
            SSU: SSU05_1374
            SSV: SSU98_1389
            SGO: SGO_0152(tgt)
            LPL: lp_2282(tgt)
            LSA: LSA0377(tgt)
            LSL: LSL_1123(tgt)
            LBR: LVIS_1228
            LCA: LSEI_0771
            LRE: Lreu_0529
            EFA: EF0896(tgt)
            OOE: OEOE_1289
            STH: STH1166
            CAC: CAC2282(tgt)
            CPE: CPE1945(tgt)
            CPF: CPF_2201(tgt)
            CPR: CPR_1912(tgt)
            CTC: CTC02209(tgt)
            CNO: NT01CX_1835
            CTH: Cthe_0958
            CDF: CD2802(tgt)
            CBO: CBO3068(tgt)
            CBA: CLB_3097(tgt)
            CBH: CLC_2970(tgt)
            CBF: CLI_3127(tgt)
            CBE: Cbei_1533
            CKL: CKL_3142(tgt)
            AMT: Amet_2342
            CHY: CHY_1515(tgt)
            DSY: DSY2463
            DRM: Dred_1666
            SWO: Swol_1428
            CSC: Csac_0257
            TTE: TTE1183(tgt)
            MTA: Moth_1694
            MSM: MSMEG_6313(tgt)
            MVA: Mvan_5580
            MGI: Mflv_1228
            MMC: Mmcs_4948
            MKM: Mkms_5036
            MJL: Mjls_5329
            CGL: NCgl0229(cgl0232)
            CGB: cg0285(tgt)
            CEF: CE0201
            CDI: DIP0251
            CJK: jk2020(tgt)
            NFA: nfa2650(tgt)
            RHA: RHA1_ro04173
            TWH: TWT152(tgt)
            TWS: TW620(tgt)
            ART: Arth_0599
            AAU: AAur_0736(tgt)
            PAC: PPA0924
            FRA: Francci3_3378
            BLO: BL0556(tgt)
            BAD: BAD_0056(tgt)
            RXY: Rxyl_1330
            FNU: FN1481
            RBA: RB1970(tgt)
            CTR: CT193(tgt)
            CTA: CTA_0211(tgt)
            CMU: TC0465
            CPN: CPn0219(tgt)
            CPA: CP0546
            CPJ: CPj0219(tgt)
            CPT: CpB0223
            CCA: CCA00581(tgt)
            CAB: CAB559
            CFE: CF0419(tgt)
            PCU: pc0794
            BBU: BB0809(tgt)
            BGA: BG0835(tgt)
            BAF: BAPKO_0862(tgt)
            TDE: TDE0438(tgt)
            LIL: LA3095
            LIC: LIC11005(tgt)
            LBJ: LBJ_0838(tgt)
            LBL: LBL_2244(tgt)
            SYN: slr0713(tgt)
            SYW: SYNW0244(tgt)
            SYC: syc1063_c(tgt)
            SYF: Synpcc7942_0455
            SYD: Syncc9605_0238
            SYE: Syncc9902_0267
            SYG: sync_0284(tgt)
            SYR: SynRCC307_2311(tgt)
            SYX: SynWH7803_0288(tgt)
            CYA: CYA_2841(tgt)
            CYB: CYB_0511(tgt)
            TEL: tll0080(tgt)
            GVI: glr0802
            ANA: alr1885
            AVA: Ava_3755
            PMA: Pro0303(tgt)
            PMM: PMM0271(tgt)
            PMT: PMT1862(tgt)
            PMN: PMN2A_1637
            PMI: PMT9312_0273
            PMB: A9601_02931(tgt)
            PMC: P9515_03041(tgt)
            PMF: P9303_24901(tgt)
            PMG: P9301_02941(tgt)
            PMH: P9215_02951(tgt)
            PME: NATL1_03501(tgt)
            TER: Tery_2456
            BTH: BT_0835
            BFR: BF2303
            BFS: BF2392(tgt)
            PGI: PG0500(tgt)
            CHU: CHU_1197(tgt)
            GFO: GFO_0596(tgt)
            FJO: Fjoh_0045
            FPS: FP0610(tgt)
            CTE: CT1397(tgt)
            CCH: Cag_0712
            CPH: Cpha266_1759
            PVI: Cvib_1223
            PLT: Plut_1404
            DET: DET0052(tgt)
            DEH: cbdb_A68(tgt)
            DEB: DehaBAV1_0049
            RRS: RoseRS_1302 RoseRS_1988
            RCA: Rcas_1658 Rcas_3266
            DRA: DR_2578
            DGE: Dgeo_0330
            TTH: TTC1676
            TTJ: TTHA0306
            AAE: aq_1308(tgt)
            TMA: TM1561
            TPT: Tpet_1231
            TME: Tmel_1416
            FNO: Fnod_0901
            MJA: MJ0436(tgtA)
            MMP: MMP0610(tgtA)
            MMQ: MmarC5_0996
            MMZ: MmarC7_1632
            MAE: Maeo_0878
            MVN: Mevan_1482
            MAC: MA4419(tgt)
            MBA: Mbar_A1088
            MMA: MM_1101
            MBU: Mbur_0941
            MTP: Mthe_0129 Mthe_1660
            MHU: Mhun_1120
            MEM: Memar_1287
            MBN: Mboo_1313
            MTH: MTH176
            MST: Msp_0520
            MSI: Msm_1557
            MKA: MK0188(tgt)
            AFU: AF0588(tgtA)
            HAL: VNG1959G(tgtA1)
            HMA: rrnAC3258(tgt)
            NPH: NP2508A(tgtA1)
            TAC: Ta1493
            TVO: TVN1497
            PTO: PTO0454
            PHO: PH1116
            PAB: PAB0740(tgtA)
            PFU: PF1046
            TKO: TK0760
            RCI: LRC280(tgt-1) RCIX2688(tgt-2)
            APE: APE_2017
            IHO: Igni_0478
            HBU: Hbut_0469
            SSO: SSO0274(tgtA)
            STO: ST0327
            SAI: Saci_0659
            PAI: PAE0777
            TPE: Tpen_0356
            NEQ: NEQ124
STRUCTURES  PDB: 1EFZ  1ENU  1F3E  1IQ8  1IT7  1IT8  1J2B  1K4G  1K4H  1N2V  
                 1OZM  1OZQ  1P0B  1P0D  1P0E  1PUD  1PXG  1Q2R  1Q2S  1Q4W  
                 1Q63  1Q65  1Q66  1R5Y  1S38  1S39  1WKD  1WKE  1WKF  1Y5V  
                 1Y5W  1Y5X  2ASH  2BBF  2QII  2QZR  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.29
            ExPASy - ENZYME nomenclature database: 2.4.2.29
            ExplorEnz - The Enzyme Database: 2.4.2.29
            ERGO genome analysis and discovery system: 2.4.2.29
            BRENDA, the Enzyme Database: 2.4.2.29
            CAS: 72162-89-1
///
ENTRY       EC 2.4.2.30                 Enzyme
NAME        NAD+ ADP-ribosyltransferase;
            poly(ADP-ribose) synthase;
            ADP-ribosyltransferase (polymerizing);
            NAD ADP-ribosyltransferase;
            PARP;
            PARP-1
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     NAD+:poly(adenine-diphosphate-D-ribosyl)-acceptor
            ADP-D-ribosyl-transferase
REACTION    NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide +
            (ADP-D-ribosyl)n+1-acceptor + H+ [RN:R04176]
ALL_REAC    R04176
SUBSTRATE   NAD+ [CPD:C00003];
            (ADP-D-ribosyl)n-acceptor [CPD:C03245]
PRODUCT     nicotinamide [CPD:C00153];
            (ADP-D-ribosyl)n+1-acceptor [CPD:C03245];
            H+ [CPD:C00080]
COMMENT     The ADP-D-ribosyl group of NAD+ is transferred to an acceptor
            carboxy group on a histone or the enzyme itself, and further
            ADP-ribosyl groups are transferred to the 2'-position of the
            terminal adenosine moiety, building up a polymer with an average
            chain length of 20-30 units.
REFERENCE   1  [PMID:3927821]
  AUTHORS   Ueda K, Hayaishi O.
  TITLE     ADP-ribosylation.
  JOURNAL   Annu. Rev. Biochem. 54 (1985) 73-100.
REFERENCE   2
  AUTHORS   Ueda, K., Kawaichi, M. and Hayaishi, O.
  TITLE     Poly(ADP-ribose) synthetase.
  JOURNAL   In: Hayaishi, O. and Ueda, K. (Eds.), ADP-Ribosylation Reactions:
            Biology and Medicine, Academic Press, London, 1982, p. 117-155.
REFERENCE   3  [PMID:2434482]
  AUTHORS   Ushiro H, Yokoyama Y, Shizuta Y.
  TITLE     Purification and characterization of poly (ADP-ribose) synthetase
            from human placenta.
  JOURNAL   J. Biol. Chem. 262 (1987) 2352-7.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K00774  NAD ADP-ribosyltransferase
GENES       HSA: 10038(PARP2) 10039(PARP3) 142(PARP1) 143(PARP4) 80351(TNKS2)
                 8658(TNKS)
            PTR: 463982(TNKS) 465197(PARP2)
            MMU: 11545(Parp1) 11546(Parp2) 235587(Parp3)
            RNO: 25591(Parp1) 300985(Parp3)
            CFA: 475392(PARP2) 475603(TNKS) 477767(TNKS2) 484745(PARP3)
                 490385(PARP1)
            BTA: 286764(ADPRT)
            GGA: 374253(TNKS2) 396199(PARP1)
            XLA: 446370(adprtl2) 496154(LOC496154)
            DRE: 335495(parp3)
            SPU: 581348(LOC581348)
            DME: Dmel_CG4719(tankyrase)
            CEL: E02H1.4(ADP-Ribosyltransferase)
            ATH: AT2G31320 AT4G02390(APP)
            OSA: 4326479 4343013
            ANI: AN3129.2
            AFM: AFUA_5G07320
            AOR: AO090003000350
            DDI: DDB_0185172(adprt2) DDB_0214818(adprt1A)
            TET: TTHERM_00030430 TTHERM_00726460 TTHERM_00726470
                 TTHERM_00823980 TTHERM_00865150
            TBR: Tb927.5.3050
            TCR: 509721.60 510173.90
            EHI: 113.t00020
            AZO: azo2985(tnkS)
            RPA: RPA2405(draT2)
STRUCTURES  PDB: 1A26  1EFY  1GS0  1PAX  1QS1  1QS2  1UK0  1UK1  1UZI  1V9X  
                 1WOK  2COK  2CR9  2CS2  2DMJ  2HW2  2PA9  2PAW  2PAX  2PQF  
                 2RF5  3PAX  4PAX  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.30
            ExPASy - ENZYME nomenclature database: 2.4.2.30
            ExplorEnz - The Enzyme Database: 2.4.2.30
            ERGO genome analysis and discovery system: 2.4.2.30
            BRENDA, the Enzyme Database: 2.4.2.30
            CAS: 58319-92-9
///
ENTRY       EC 2.4.2.31                 Enzyme
NAME        NAD(P)+---protein-arginine ADP-ribosyltransferase;
            ADP-ribosyltransferase;
            mono(ADP-ribosyl)transferase;
            NAD+:L-arginine ADP-D-ribosyltransferase;
            NAD(P)+-arginine ADP-ribosyltransferase;
            NAD(P)+-arginine ADP-ribosyltransferase;
            NAD(P)+:L-arginine ADP-D-ribosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     NAD(P)+:protein-L-arginine ADP-D-ribosyltransferase
REACTION    (1) NAD+ + protein L-arginine = nicotinamide +
            Nomega-(ADP-D-ribosyl)-protein-L-arginine [RN:R00555];
            (2) NADP+ + protein L-arginine = nicotinamide +
            Nomega-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine
ALL_REAC    R00555
SUBSTRATE   NAD+ [CPD:C00003];
            protein L-arginine;
            NADP+ [CPD:C00006]
PRODUCT     nicotinamide [CPD:C00153];
            Nomega-(ADP-D-ribosyl)-protein-L-arginine;
            Nomega-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine
COMMENT     Arginine residues in proteins act as acceptors. Free arginine,
            agmatine [(4-aminobutyl)guanidine], arginine methyl ester and
            guanidine can also do so. The enzyme catalyses the NAD+-dependent
            activation of EC 4.6.1.1, adenylate cyclase. Some bacterial
            enterotoxins possess similar enzymatic activities. (cf. EC 2.4.2.36
            NAD+---diphthamide ADP-ribosyltransferase).
REFERENCE   1  [PMID:225315]
  AUTHORS   Moss J, Stanley SJ, Oppenheimer NJ.
  TITLE     Substrate specificity and partial purification of a stereospecific
            NAD- and guanidine-dependent ADP-ribosyltransferase from avian
            erythrocytes.
  JOURNAL   J. Biol. Chem. 254 (1979) 8891-4.
  ORGANISM  avian
REFERENCE   2  [PMID:6247348]
  AUTHORS   Moss J, Stanley SJ, Watkins PA.
  TITLE     Isolation and properties of an NAD- and guanidine-dependent
            ADP-ribosyltransferase from turkey erythrocytes.
  JOURNAL   J. Biol. Chem. 255 (1980) 5838-40.
  ORGANISM  turkey
REFERENCE   3  [PMID:3927821]
  AUTHORS   Ueda K, Hayaishi O.
  TITLE     ADP-ribosylation.
  JOURNAL   Annu. Rev. Biochem. 54 (1985) 73-100.
ORTHOLOGY   KO: K00775  NAD(P)-arginine ADP-ribosyltransferase
            KO: K06716  ADP-ribosyltransferase 1
            KO: K06717  ADP-ribosyltransferase 4
GENES       HSA: 116969(ART5) 417(ART1) 419(ART3) 420(ART4) 51548(SIRT6)
            PTR: 450970(ART5) 466326(ART1) 473376(ART4)
            MMU: 109978(Art4) 109979(Art3) 11870(Art1) 11871(Art2a)
                 11872(Art2b) 11875(Art5) 50721(Sirt6)
            RNO: 293152(Art2b) 308873(Art1_predicted) 312806(Art4_predicted)
            CFA: 476821(ART1) 478434(ART3) 486668(ART4)
            BTA: 407146(ART4) 407147(ART3) 407148(art5) 539042(LOC539042)
            GGA: 427879(ART4) 428123(ART1) 429485(ART1)
            XTR: 780139(art1)
STRUCTURES  PDB: 1GXY  1GXZ  1GY0  1OG1  1OG3  1OG4  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.31
            ExPASy - ENZYME nomenclature database: 2.4.2.31
            ExplorEnz - The Enzyme Database: 2.4.2.31
            ERGO genome analysis and discovery system: 2.4.2.31
            BRENDA, the Enzyme Database: 2.4.2.31
            CAS: 81457-93-4
///
ENTRY       EC 2.4.2.32                 Enzyme
NAME        dolichyl-phosphate D-xylosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     UDP-D-xylose:dolichyl-phosphate D-xylosyltransferase
REACTION    UDP-D-xylose + dolichyl phosphate = UDP + dolichyl D-xylosyl
            phosphate [RN:R01472]
ALL_REAC    R01472
SUBSTRATE   UDP-D-xylose [CPD:C00190];
            dolichyl phosphate [CPD:C00110]
PRODUCT     UDP [CPD:C00015];
            dolichyl D-xylosyl phosphate [CPD:C01191]
REFERENCE   1  [PMID:4823870]
  AUTHORS   Waechter CJ, Lucas JJ, Lennarz WJ.
  TITLE     Evidence for xylosyl lipids as intermediates in xylosyl transfers in
            hen oviduct membranes.
  JOURNAL   Biochem. Biophys. Res. Commun. 56 (1974) 343-50.
  ORGANISM  chicken [GN:gga]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.32
            ExPASy - ENZYME nomenclature database: 2.4.2.32
            ExplorEnz - The Enzyme Database: 2.4.2.32
            ERGO genome analysis and discovery system: 2.4.2.32
            BRENDA, the Enzyme Database: 2.4.2.32
///
ENTRY       EC 2.4.2.33                 Enzyme
NAME        dolichyl-xylosyl-phosphate---protein xylosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     dolichyl-D-xylosyl-phosphate:protein D-xylosyltransferase
REACTION    dolichyl D-xylosyl phosphate + protein = dolichyl phosphate +
            D-xylosylprotein [RN:R03356]
ALL_REAC    R03356
SUBSTRATE   dolichyl D-xylosyl phosphate [CPD:C01191];
            protein [CPD:C00017]
PRODUCT     dolichyl phosphate [CPD:C00110];
            D-xylosylprotein [CPD:C02399]
REFERENCE   1  [PMID:4823870]
  AUTHORS   Waechter CJ, Lucas JJ, Lennarz WJ.
  TITLE     Evidence for xylosyl lipids as intermediates in xylosyl transfers in
            hen oviduct membranes.
  JOURNAL   Biochem. Biophys. Res. Commun. 56 (1974) 343-50.
  ORGANISM  chicken [GN:gga]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.33
            ExPASy - ENZYME nomenclature database: 2.4.2.33
            ExplorEnz - The Enzyme Database: 2.4.2.33
            ERGO genome analysis and discovery system: 2.4.2.33
            BRENDA, the Enzyme Database: 2.4.2.33
///
ENTRY       EC 2.4.2.34                 Enzyme
NAME        indolylacetylinositol arabinosyltransferase;
            arabinosylindolylacetylinositol synthase;
            UDP-L-arabinose:indol-3-ylacetyl-myo-inositol
            L-arabinosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     UDP-L-arabinose:(indol-3-yl)acetyl-myo-inositol
            L-arabinosyltransferase
REACTION    UDP-L-arabinose + (indol-3-yl)acetyl-1D-myo-inositol = UDP +
            (indol-3-yl)acetyl-myo-inositol 3-L-arabinoside [RN:R04335]
ALL_REAC    R04335
SUBSTRATE   UDP-L-arabinose [CPD:C00935];
            indol-3-ylacetyl-1D-myo-inositol [CPD:C03868]
PRODUCT     UDP [CPD:C00015];
            (indol-3-yl)acetyl-myo-inositol 3-L-arabinoside
COMMENT     The position of acylation is indeterminate because of the ease of
            acyl transfer between hydroxy groups. For a diagram showing the
            biosynthesis of UDP-L-arabinose, click here.
REFERENCE   1
  AUTHORS   Corcuera, L.J. and Bandurski, R.S.
  TITLE     Biosynthesis of indol-3-yl-acetyl-myo-inositol arabinoside in
            kernels of Zea mays L.
  JOURNAL   Plant Physiol. 70 (1982) 1664-1666.
  ORGANISM  Zea mays [GN:ezma]
ORTHOLOGY   KO: K05950  
GENES       MBO: Mb3822(embC) Mb3823(embA) Mb3824(embB)
            MBB: BCG_3855(embC) BCG_3856(embA) BCG_3857(embB)
            SEN: SACE_0179(embC)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.34
            ExPASy - ENZYME nomenclature database: 2.4.2.34
            ExplorEnz - The Enzyme Database: 2.4.2.34
            ERGO genome analysis and discovery system: 2.4.2.34
            BRENDA, the Enzyme Database: 2.4.2.34
            CAS: 84720-96-7
///
ENTRY       EC 2.4.2.35                 Enzyme
NAME        flavonol-3-O-glycoside xylosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     UDP-D-xylose:flavonol-3-O-glycoside 2''-O-beta-D-xylosyltransferase
REACTION    UDP-D-xylose + a flavonol 3-O-glycoside = UDP + a flavonol
            3-[-D-xylosyl-(1->2)-beta-D-glycoside] [RN:R03268]
ALL_REAC    R03268 > R06811 R06814
SUBSTRATE   UDP-D-xylose [CPD:C00190];
            flavonol 3-O-glycoside
PRODUCT     UDP [CPD:C00015];
            flavonol 3-[-D-xylosyl-(1->2)-beta-D-glycoside]
COMMENT     Flavonol 3-O-glucoside, flavonol 3-O-galactoside and, more slowly,
            rutin, can act as acceptors.
REFERENCE   1
  AUTHORS   Kleinehollenhorst, G., Behrens, H., Pegels, G., Srunk, N. and
            Wiermann, R.
  TITLE     Formation of flavonol 3-O-diglycosides and flavonol
            3-O-triglycosides by enzyme extracts from anthers of Tulipa cv
            apeldoorn - characterization and activity of 3 different
            O-glycosyltransferases during anther development.
  JOURNAL   Z. Natursforsch. C: Biosci. 37 (1982) 587-599.
REFERENCE   2
  AUTHORS   Ishikura, N. and Yang, Z.Q.
  TITLE     UDP-D-xylose: flavonol 3-O-xylosyltransferase from young leaves of
            Euonymus alatus f. ciliato-dentatus.
  JOURNAL   Z. Naturforsch. C: Biosci. 46 (1991) 1003-1010.
  ORGANISM  Euonymus alatus
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.35
            ExPASy - ENZYME nomenclature database: 2.4.2.35
            ExplorEnz - The Enzyme Database: 2.4.2.35
            ERGO genome analysis and discovery system: 2.4.2.35
            BRENDA, the Enzyme Database: 2.4.2.35
            CAS: 83380-90-9
///
ENTRY       EC 2.4.2.36                 Enzyme
NAME        NAD+---diphthamide ADP-ribosyltransferase;
            ADP-ribosyltransferase;
            mono(ADPribosyl)transferase;
            NAD---diphthamide ADP-ribosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     NAD+:peptide-diphthamide N-(ADP-D-ribosyl)transferase
REACTION    NAD+ + peptide diphthamide = nicotinamide + peptide
            N-(ADP-D-ribosyl)diphthamide [RN:R04074]
ALL_REAC    R04074
SUBSTRATE   NAD+ [CPD:C00003];
            peptide diphthamide [CPD:C02872]
PRODUCT     nicotinamide [CPD:C00153];
            peptide N-(ADP-D-ribosyl)diphthamide [CPD:C04339]
COMMENT     Diphtheria toxin and some other bacterial toxins catalyse this
            reaction. The acceptor is a diphthamide residue in elongation factor
            2. cf. EC 2.4.2.31 NAD(P)+---protein-arginine
            ADP-ribosyltransferase.
REFERENCE   1  [PMID:6326138]
  AUTHORS   Lee H, Iglewski WJ.
  TITLE     Cellular ADP-ribosyltransferase with the same mechanism of action as
            diphtheria toxin and Pseudomonas toxin A.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 2703-7.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   2  [PMID:3927821]
  AUTHORS   Ueda K, Hayaishi O.
  TITLE     ADP-ribosylation.
  JOURNAL   Annu. Rev. Biochem. 54 (1985) 73-100.
ORTHOLOGY   KO: K00776  NAD-diphthamide ADP-ribosyltransferase
GENES       VCH: VC1457
            VCO: VC0395_0512(ctxA) VC0395_A1060(ctxA)
            BXE: Bxe_A0732 Bxe_A2168 Bxe_B1766 Bxe_B1851
            CDI: DIP0222(tox)
STRUCTURES  PDB: 1S5B  1S5C  1S5D  1S5E  1S5F  1SGK  1TOX  1XDT  1XK9  1ZM3  
                 1ZM4  1ZM9  2A5D  2A5F  2A5G  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.36
            ExPASy - ENZYME nomenclature database: 2.4.2.36
            ExplorEnz - The Enzyme Database: 2.4.2.36
            ERGO genome analysis and discovery system: 2.4.2.36
            BRENDA, the Enzyme Database: 2.4.2.36
            CAS: 52933-21-8
///
ENTRY       EC 2.4.2.37                 Enzyme
NAME        NAD+---dinitrogen-reductase ADP-D-ribosyltransferase;
            NAD---azoferredoxin (ADPribose)transferase;
            NAD---dinitrogen-reductase ADP-D-ribosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     NAD+:[dinitrogen reductase] (ADP-D-ribosyl)transferase
REACTION    NAD+ + [dinitrogen reductase] = nicotinamide +
            ADP-D-ribosyl-[dinitrogen reductase] [RN:R03447]
ALL_REAC    R03447
SUBSTRATE   NAD+ [CPD:C00003];
            [dinitrogen reductase] [CPD:C03315]
PRODUCT     nicotinamide [CPD:C00153];
            ADP-D-ribosyl-[dinitrogen reductase] [CPD:C01253]
COMMENT     Together with EC 3.2.2.24 (ADP-ribosyl-[dinitrogen reductase]
            hydrolase), controls the level of activity of EC 1.18.6.1
            nitrogenase.
REFERENCE   1  [PMID:2506427]
  AUTHORS   Fitzmaurice WP, Saari LL, Lowery RG, Ludden PW, Roberts GP.
  TITLE     Genes coding for the reversible ADP-ribosylation system of
            dinitrogenase reductase from Rhodospirillum rubrum.
  JOURNAL   Mol. Gen. Genet. 218 (1989) 340-7.
  ORGANISM  Rhodospirillum rubrum [GN:rru]
REFERENCE   2  [PMID:3141411]
  AUTHORS   Lowery RG, Ludden PW.
  TITLE     Purification and properties of dinitrogenase reductase
            ADP-ribosyltransferase from the photosynthetic bacterium
            Rhodospirillum rubrum.
  JOURNAL   J. Biol. Chem. 263 (1988) 16714-9.
  ORGANISM  Rhodospirillum rubrum [GN:rru]
ORTHOLOGY   KO: K05951  
GENES       AZO: azo0537(draT)
            GSU: GSU2802(dRAT)
            GUR: Gura_1205
            PCA: Pcar_2092
            PPD: Ppro_3487
            AFW: Anae109_3033
            RPB: RPB_3044
            RPC: RPC_0878
            RPD: RPD_2407
            RPE: RPE_0837 RPE_3888
            RRU: Rru_A1009 Rru_A1389
            MGM: Mmc1_1203
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.37
            ExPASy - ENZYME nomenclature database: 2.4.2.37
            ExplorEnz - The Enzyme Database: 2.4.2.37
            ERGO genome analysis and discovery system: 2.4.2.37
            BRENDA, the Enzyme Database: 2.4.2.37
            CAS: 117590-45-1
///
ENTRY       EC 2.4.2.38                 Enzyme
NAME        glycoprotein 2-beta-D-xylosyltransferase;
            beta1,2-xylosyltransferase;
            UDP-D-xylose:glycoprotein (D-xylose to the 3,6-disubstituted mannose
            of
            4-N-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-
            acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-
            mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-
            glucosaminyl}asparagine) 2-beta-D-xylosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     UDP-D-xylose:glycoprotein (D-xylose to the 3,6-disubstituted mannose
            of
            N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-a
            cetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-man
            nosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glu
            cosaminyl}asparagine) 2-beta-D-xylosyltransferase
REACTION    UDP-D-xylose +
            N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-
            acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-
            mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-
            glucosaminyl}asparagine = UDP +
            N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-
            acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-[beta-D-
            xylosyl-(1->2)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-
            (1->4)-N-acetyl-beta-D-glucosaminyl}asparagine [RN:R06016]
ALL_REAC    R06016(G)
SUBSTRATE   UDP-D-xylose [CPD:C00190];
            N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-
            acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-
            mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-
            glucosaminyl}asparagine
PRODUCT     UDP [CPD:C00015];
            N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-
            acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-[beta-D-
            xylosyl-(1->2)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-
            (1->4)-N-acetyl-beta-D-glucosaminyl}asparagine
COMMENT     Specific for N-linked oligosaccharides (N-glycans).
REFERENCE   1  [PMID:9395463]
  AUTHORS   Zeng Y, Bannon G, Thomas VH, Rice K, Drake R, Elbein A.
  TITLE     Purification and specificity of beta1,2-xylosyltransferase, an
            enzyme that contributes to the allergenicity of some plant proteins.
  JOURNAL   J. Biol. Chem. 272 (1997) 31340-7.
  ORGANISM  Glycine max [GN:egma]
REFERENCE   2  [PMID:10781814]
  AUTHORS   Strasser R, Mucha J, Mach L, Altmann F, Wilson IB, Glossl J,
            Steinkellner H.
  TITLE     Molecular cloning and functional expression of beta1,
            2-xylosyltransferase cDNA from Arabidopsis thaliana.
  JOURNAL   FEBS. Lett. 472 (2000) 105-8.
  ORGANISM  Arabidopsis thaliana [GN:ath]
PATHWAY     PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K03714  glycoprotein 2-beta-D-xylosyltransferase
GENES       ATH: AT5G55500(AtXylT)
            OSA: 4345969
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.38
            ExPASy - ENZYME nomenclature database: 2.4.2.38
            ExplorEnz - The Enzyme Database: 2.4.2.38
            ERGO genome analysis and discovery system: 2.4.2.38
            BRENDA, the Enzyme Database: 2.4.2.38
            CAS: 141256-56-6
///
ENTRY       EC 2.4.2.39                 Enzyme
NAME        xyloglucan 6-xylosyltransferase;
            uridine diphosphoxylose-xyloglucan 6alpha-xylosyltransferase;
            xyloglucan 6-alpha-D-xylosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     UDP-D-xylose:xyloglucan 1,6-alpha-D-xylosyltransferase
REACTION    Transfers an alpha-D-xylosyl residue from UDP-D-xylose to a glucose
            residue in xyloglucan, forming an alpha-1,6-D-xylosyl-D-glucose
            linkage
COMMENT     In association with EC 2.4.1.168 (xyloglucan 4-glucosyltransferase),
            this enzyme brings about the synthesis of xyloglucan; concurrent
            transfers of glucose and xylose are necessary for this synthesis.
REFERENCE   1  [PMID:6457048]
  AUTHORS   Hayashi T, Matsuda K.
  TITLE     Biosynthesis of xyloglucan in suspension-cultured soybean cells.
            Occurrence and some properties of xyloglucan
            4-beta-D-glucosyltransferase and 6-alpha-D-xylosyltransferase.
  JOURNAL   J. Biol. Chem. 256 (1981) 11117-22.
  ORGANISM  Glycine max [GN:egma]
REFERENCE   2
  AUTHORS   Hayashi, T. and Matsuda, K.
  TITLE     Biosynthesis of xyloglucan in suspension-cultured soybean cells -
            synthesis of xyloglucan from UDP-glucose and UDP-xylose in the
            cell-free system.
  JOURNAL   Plant Cell Physiol. 22 (1981) 517-523.
  ORGANISM  Glycine max [GN:egma]
ORTHOLOGY   KO: K08238  xyloglucan 6-xylosyltransferase
GENES       ATH: AT1G74380 AT3G62720(ATXT1) AT4G02500(ATXT2) AT5G07720
            OSA: 4332564
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.39
            ExPASy - ENZYME nomenclature database: 2.4.2.39
            ExplorEnz - The Enzyme Database: 2.4.2.39
            ERGO genome analysis and discovery system: 2.4.2.39
            BRENDA, the Enzyme Database: 2.4.2.39
            CAS: 80238-01-3
///
ENTRY       EC 2.4.2.40                 Enzyme
NAME        zeatin O-beta-D-xylosyltransferase;
            uridine diphosphoxylose-zeatin xylosyltransferase;
            zeatin O-xylosyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Pentosyltransferases
SYSNAME     UDP-D-xylose:zeatin O-beta-D-xylosyltransferase
REACTION    UDP-D-xylose + zeatin = UDP + O-beta-D-xylosylzeatin [RN:R02119]
ALL_REAC    R02119
SUBSTRATE   UDP-D-xylose [CPD:C00190];
            zeatin [CPD:C00371]
PRODUCT     UDP [CPD:C00015];
            O-beta-D-xylosylzeatin [CPD:C03300]
COMMENT     Does not act on UDP-glucose (cf. EC 2.4.1.103 alizarin
            2-beta-glucosyltransferase).
REFERENCE   1  [PMID:16593839]
  AUTHORS   Turner JE, Mok DW, Mok MC, Shaw G.
  TITLE     Isolation and partial purification of an enzyme catalyzing the
            formation of O-xylosylzeatin in Phaseolus vulgaris embryos.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 3714-3717.
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.2.40
            ExPASy - ENZYME nomenclature database: 2.4.2.40
            ExplorEnz - The Enzyme Database: 2.4.2.40
            ERGO genome analysis and discovery system: 2.4.2.40
            BRENDA, the Enzyme Database: 2.4.2.40
            CAS: 110541-22-5
///
ENTRY       EC 2.4.99.1                 Enzyme
NAME        beta-galactoside alpha-2,6-sialyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Transferring other glycosyl groups
SYSNAME     CMP-N-acetylneuraminate:beta-D-galactosyl-1,4-N-acetyl-beta-D-glucos
            amine alpha-2,6-N-acetylneuraminyltransferase
REACTION    CMP-N-acetylneuraminate +
            beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine = CMP +
            alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-
            glucosamine [RN:R04532 R06188]
ALL_REAC    R04532 R06188(G);
            (other) R05580 R05905(G) R05906(G) R05990(G)
SUBSTRATE   CMP-N-acetylneuraminate [CPD:C00128];
            beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine [CPD:C00611]
PRODUCT     CMP [CPD:C00055];
            alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-
            glucosamine [CPD:C04886]
COMMENT     The terminal beta-D-galactosyl residue of the oligosaccharide of
            glycoproteins, as well as lactose, can act as acceptor.
REFERENCE   1  [PMID:4723915]
  AUTHORS   Bartholomew BA, Jourdian GW, Roseman S.
  TITLE     The sialic acids. XV. Transfer of sialic acid to glycoproteins by a
            sialyltransferase from colostrum.
  JOURNAL   J. Biol. Chem. 248 (1973) 5751-62.
  ORGANISM  goat, cow [GN:bta], human [GN:hsa], rat [GN:rno]
REFERENCE   2  [PMID:4313609]
  AUTHORS   Hickman J, Ashwell G, Morell AG, van den Hamer CJ, Scheinberg IH.
  TITLE     Physical and chemical studies on ceruloplasmin. 8. Preparation of
            N-acetylneuraminic acid-1-14C-labeled ceruloplasmin.
  JOURNAL   J. Biol. Chem. 245 (1970) 759-66.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:849932]
  AUTHORS   Paulson JC, Beranek WE, Hill RL.
  TITLE     Purification of a sialyltransferase from bovine colostrum by
            affinity chromatography on CDP-agarose.
  JOURNAL   J. Biol. Chem. 252 (1977) 2356-62.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:6366476]
  AUTHORS   Schachter H, Narasimhan S, Gleeson P, Vella G.
  TITLE     Glycosyltransferases involved in elongation of N-glycosidically
            linked oligosaccharides of the complex or N-acetyllactosamine type.
  JOURNAL   Methods. Enzymol. 98 (1983) 98-134.
REFERENCE   5  [PMID:5726897]
  AUTHORS   Spiro MJ, Spiro RG.
  TITLE     Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid
            sialyltransferase.
  JOURNAL   J. Biol. Chem. 243 (1968) 6520-8.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K00778  beta-galactoside alpha-2,6-sialyltransferase
                        (sialyltransferase 1)
GENES       HSA: 6480(ST6GAL1)
            PTR: 460922(ST6GAL1)
            MMU: 20440(St6gal1)
            RNO: 25197(St6gal1)
            CFA: 478668(ST6GAL1)
            BTA: 282073(SIAT1)
            GGA: 396169(ST6GAL1)
            DRE: 445376(st6gal1)
            DME: Dmel_CG4871(ST6Gal)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.99.1
            ExPASy - ENZYME nomenclature database: 2.4.99.1
            ExplorEnz - The Enzyme Database: 2.4.99.1
            ERGO genome analysis and discovery system: 2.4.99.1
            BRENDA, the Enzyme Database: 2.4.99.1
            CAS: 9075-81-4
///
ENTRY       EC 2.4.99.2                 Enzyme
NAME        monosialoganglioside sialyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Transferring other glycosyl groups
SYSNAME     CMP-N-acetylneuraminate:D-galactosyl-N-acetyl-D-galactosaminyl-(N-ac
            etylneuraminyl)-D-galactosyl-D-glucosylceramide
            N-acetylneuraminyltransferase
REACTION    CMP-N-acetylneuraminate +
            D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-
            galactosyl-D-glucosylceramide = CMP +
            N-acetylneuraminyl-D-galactosyl-N-acetyl-D-galactosaminyl-(N-
            acetylneuraminyl)-D-galactosyl-D-glucosylceramide [RN:R04648 R05942]
ALL_REAC    R04648 R05942(G)
SUBSTRATE   CMP-N-acetylneuraminate [CPD:C00128];
            D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-
            galactosyl-D-glucosylceramide [CPD:C04911]
PRODUCT     CMP [CPD:C00055];
            N-acetylneuraminyl-D-galactosyl-N-acetyl-D-galactosaminyl-(N-
            acetylneuraminyl)-D-galactosyl-D-glucosylceramide [CPD:C04927]
COMMENT     May be identical with EC 2.4.99.4 beta-galactoside
            alpha-2,3-sialyltransferase.
REFERENCE   1  [PMID:438198]
  AUTHORS   Rearick JI, Sadler JE, Paulson JC, Hill RL.
  TITLE     Enzymatic characterization of beta D-galactoside alpha2 leads to 3
            sialyltransferase from porcine submaxillary gland.
  JOURNAL   J. Biol. Chem. 254 (1979) 4444-51.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:4351506]
  AUTHORS   Yip MC.
  TITLE     The enzymic synthesis of disialoganglioside: rat brain
            cytidine-5'-monophospho-N-acetylneuraminic acid:
            monosialoganglioside (G M1 ) sialyltransferase.
  JOURNAL   Biochim. Biophys. Acta. 306 (1973) 298-306.
  ORGANISM  rat [GN:rno]
GENES       HSA: 84620(ST6GAL2)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.99.2
            ExPASy - ENZYME nomenclature database: 2.4.99.2
            ExplorEnz - The Enzyme Database: 2.4.99.2
            ERGO genome analysis and discovery system: 2.4.99.2
            BRENDA, the Enzyme Database: 2.4.99.2
            CAS: 60202-12-2
///
ENTRY       EC 2.4.99.3                 Enzyme
NAME        alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Transferring other glycosyl groups
SYSNAME     CMP-N-acetylneuraminate:glycano-1,3-(N-acetyl-alpha-D-galactosaminyl
            )-glycoprotein alpha-2,6-N-acetylneuraminyltransferase
REACTION    CMP-N-acetylneuraminate +
            glycano-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein = CMP +
            glycano-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-
            glycoprotein [RN:R05911]
ALL_REAC    R05911(G) > R05914(G) R06273(G)
SUBSTRATE   CMP-N-acetylneuraminate [CPD:C00128];
            glycano-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein
            [CPD:C04788]
PRODUCT     CMP [CPD:C00055];
            glycano-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-
            glycoprotein
COMMENT     alpha-N-Acetylgalactosamine linked to threonine or serine is also an
            acceptor, when substituted at the 3-position.
REFERENCE   1  [PMID:447688]
  AUTHORS   Sadler JE, Rearick JI, Hill RL.
  TITLE     Purification to homogeneity and enzymatic characterization of an
            alpha-N-acetylgalactosaminide alpha 2 leads to 6 sialyltransferase
            from porcine submaxillary glands.
  JOURNAL   J. Biol. Chem. 254 (1979) 5934-41.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00512  O-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K03479  alpha-N-acetylgalactosaminide
                        alpha-2,6-sialyltransferase (sialyltransferase 7A)
GENES       HSA: 55808(ST6GALNAC1)
            PTR: 449516(ST6GALNAC1)
            MCC: 707339(LOC707339)
            MMU: 20445(St6galnac1)
            RNO: 287920(St6galnac1)
            CFA: 483334(ST6GALNAC1)
            BTA: 618655(LOC618655)
            GGA: 396168(ST6GALNAC1)
            DRE: 564336(si:ch211-51n14.1)
            SPU: 580149(LOC580149)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.99.3
            ExPASy - ENZYME nomenclature database: 2.4.99.3
            ExplorEnz - The Enzyme Database: 2.4.99.3
            ERGO genome analysis and discovery system: 2.4.99.3
            BRENDA, the Enzyme Database: 2.4.99.3
            CAS: 71124-50-0
///
ENTRY       EC 2.4.99.4                 Enzyme
NAME        beta-galactoside alpha-2,3-sialyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Transferring other glycosyl groups
SYSNAME     CMP-N-acetylneuraminate:beta-D-galactoside
            alpha-2,3-N-acetylneuraminyl-transferase
REACTION    CMP-N-acetylneuraminate +
            beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R = CMP +
            alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D-
            galactosaminyl-R [RN:R04590 R05913]
ALL_REAC    R04590 R05913(G);
            (other) R04648 R05116 R05942(G) R05949(G) R05957(G) R05967(G)
SUBSTRATE   CMP-N-acetylneuraminate [CPD:C00128];
            beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R [CPD:C04750]
PRODUCT     CMP [CPD:C00055];
            alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D-
            galactosaminyl-R [CPD:C04901]
COMMENT     The acceptor is Galbeta1,3GalNAc-R, where R is H, a threonine or
            serine residue in a glycoprotein, or a glycolipid. Lactose can also
            act as acceptor. May be identical with EC 2.4.99.2
            monosialoganglioside sialyltransferase.
REFERENCE   1  [PMID:438198]
  AUTHORS   Rearick JI, Sadler JE, Paulson JC, Hill RL.
  TITLE     Enzymatic characterization of beta D-galactoside alpha2 leads to 3
            sialyltransferase from porcine submaxillary gland.
  JOURNAL   J. Biol. Chem. 254 (1979) 4444-51.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:438196]
  AUTHORS   Sadler JE, Rearick JI, Paulson JC, Hill RL.
  TITLE     Purification to homogeneity of a beta-galactoside alpha2 leads to 3
            sialyltransferase and partial purification of an
            alpha-N-acetylgalactosaminide alpha2 leads to 6 sialyltransferase
            from porcine submaxillary glands.
  JOURNAL   J. Biol. Chem. 254 (1979) 4434-42.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00512  O-Glycan biosynthesis
            PATH: map00533  Keratan sulfate biosynthesis
            PATH: map00601  Glycosphingolipid biosynthesis - lactoseries
            PATH: map00603  Glycosphingolipid biosynthesis - globoseries
            PATH: map00604  Glycosphingolipid biosynthesis - ganglioseries
            PATH: map01030  Glycan structures - biosynthesis 1
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K00780  beta-galactoside alpha-2,3-sialyltransferase
                        (sialyltransferase 4A)
            KO: K03368  beta-galactoside alpha-2,3-sialyltransferase
                        (sialyltransferase 4B)
            KO: K03494  beta-galactoside alpha-2,3-sialyltransferase
                        (sialyltransferase 4C)
GENES       HSA: 6482(ST3GAL1) 6483(ST3GAL2) 6484(ST3GAL4)
            PTR: 450114(ST3GAL1) 454214(ST3GAL2) 466845(ST3GAL4)
            MMU: 20442(St3gal1) 20443(St3gal4) 20444(St3gal2)
            RNO: 362924(St3gal1) 363040(St3gal4) 64442(St3gal2)
            CFA: 482050(ST3GAL1) 489714(ST3GAL2) 607094(ST3GAL4)
            BTA: 282351(SIAT4A) 404163(ST3GAL-IV) 444879(SIAT4B)
            SSC: 396602(ST3GAL-IV) 445537(SIAT4A)
            GGA: 395139(ST3GAL2) 396140(ST3GAL1) 419718(ST3GAL4)
            XLA: 414465(MGC81265)
            XTR: 394493(st3Gal-II) 403093(siat4c)
            DRE: 445562(st3gal2) 504044(st3gal4)
            SPU: 590209(st)
STRUCTURES  PDB: 2EX0  2EX1  2IHJ  2IHK  2IHZ  2II6  2IIB  2IIQ  2ILV  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.99.4
            ExPASy - ENZYME nomenclature database: 2.4.99.4
            ExplorEnz - The Enzyme Database: 2.4.99.4
            ERGO genome analysis and discovery system: 2.4.99.4
            BRENDA, the Enzyme Database: 2.4.99.4
            CAS: 71124-51-1
///
ENTRY       EC 2.4.99.5                 Enzyme
NAME        galactosyldiacylglycerol alpha-2,3-sialyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Transferring other glycosyl groups
SYSNAME     CMP-N-acetylneuraminate:1,2-diacyl-3-beta-D-galactosyl-sn-glycerol
            N-acetylneuraminyltransferase
REACTION    CMP-N-acetylneuraminate + 1,2-diacyl-3-beta-D-galactosyl-sn-glycerol
            = CMP +
            1,2-diacyl-3-[3-(alpha-D-N-acetylneuraminyl)-beta-D-galactosyl]-sn-
            glycerol [RN:R03468]
ALL_REAC    R03468
SUBSTRATE   CMP-N-acetylneuraminate [CPD:C00128];
            1,2-diacyl-3-beta-D-galactosyl-sn-glycerol [CPD:C03692]
PRODUCT     CMP [CPD:C00055];
            1,2-diacyl-3-[3-(alpha-D-N-acetylneuraminyl)-beta-D-galactosyl]-sn-
            glycerol [CPD:C04872]
COMMENT     The beta-D-galactosyl residue of the oligosaccharide of
            glycoproteins may also act as acceptor.
REFERENCE   1  [PMID:7298658]
  AUTHORS   Pieringer J, Keech S, Pieringer RA.
  TITLE     Biosynthesis in vitro of sialosylgalactosyldiacylglycerol by mouse
            brain microsomes.
  JOURNAL   J. Biol. Chem. 256 (1981) 12306-9.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:7142179]
  AUTHORS   Weinstein J, de Souza-e-Silva U, Paulson JC.
  TITLE     Purification of a Gal beta 1 to 4GlcNAc alpha 2 to 6
            sialyltransferase and a Gal beta 1 to 3(4)GlcNAc alpha 2 to 3
            sialyltransferase to homogeneity from rat liver.
  JOURNAL   J. Biol. Chem. 257 (1982) 13835-44.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:7142180]
  AUTHORS   Weinstein J, de Souza-e-Silva U, Paulson JC.
  TITLE     Sialylation of glycoprotein oligosaccharides N-linked to asparagine.
            Enzymatic characterization of a Gal beta 1 to 3(4)GlcNAc alpha 2 to
            3 sialyltransferase and a Gal beta 1 to 4GlcNAc alpha 2 to 6
            sialyltransferase from rat liver.
  JOURNAL   J. Biol. Chem. 257 (1982) 13845-53.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00561  Glycerolipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.99.5
            ExPASy - ENZYME nomenclature database: 2.4.99.5
            ExplorEnz - The Enzyme Database: 2.4.99.5
            ERGO genome analysis and discovery system: 2.4.99.5
            BRENDA, the Enzyme Database: 2.4.99.5
            CAS: 80237-98-5
///
ENTRY       EC 2.4.99.6                 Enzyme
NAME        N-acetyllactosaminide alpha-2,3-sialyltransferase;
            sialyltransferase;
            cytidine
            monophosphoacetylneuraminate-beta-galactosyl(1-
            >4)acetylglucosaminide alpha2->3-sialyltransferase;
            alpha2->3 sialyltransferase;
            SiaT
CLASS       Transferases;
            Glycosyltransferases;
            Transferring other glycosyl groups
SYSNAME     CMP-N-acetylneuraminate:beta-D-galactosyl-1,4-N-acetyl-D-glucosaminy
            l-glycoprotein alpha-2,3-N-acetylneuraminyltransferase
REACTION    CMP-N-acetylneuraminate +
            beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein = CMP +
            alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-D-
            glucosaminyl-glycoprotein [RN:R04596]
ALL_REAC    R04596;
            (other) R06153(G)
SUBSTRATE   CMP-N-acetylneuraminate [CPD:C00128];
            beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein
            [CPD:C04791]
PRODUCT     CMP [CPD:C00055];
            alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-D-
            glucosaminyl-glycoprotein [CPD:C04907]
COMMENT     Acts on beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl termini on
            glycoprotein.
REFERENCE   1  [PMID:7204397]
  AUTHORS   Van den Eijnden DH, Schiphorst WE.
  TITLE     Detection of beta-galactosyl(1 leads to 4)N-acetylglucosaminide
            alpha(2 leads to 3)-sialyltransferase activity in fetal calf liver
            and other tissues.
  JOURNAL   J. Biol. Chem. 256 (1981) 3159-62.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00533  Keratan sulfate biosynthesis
            PATH: map00601  Glycosphingolipid biosynthesis - lactoseries
            PATH: map01030  Glycan structures - biosynthesis 1
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K00781  N-acetyllactosaminide alpha-2,3-sialyltransferase
                        (sialyltransferase 6)
GENES       HSA: 6487(ST3GAL3)
            PTR: 456832(ST3GAL3)
            MMU: 20441(St3gal3)
            RNO: 64445(St3gal3)
            CFA: 610736(ST3GAL3)
            BTA: 444859(SIAT6)
            SSC: 396619(ST3GAL-III)
            GGA: 424572(ST3GAL3)
            XTR: 402789(siat6)
            DRE: 407659(siat6l)
            SPU: 581680(LOC581680)
STRUCTURES  PDB: 2EX0  2EX1  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.99.6
            ExPASy - ENZYME nomenclature database: 2.4.99.6
            ExplorEnz - The Enzyme Database: 2.4.99.6
            ERGO genome analysis and discovery system: 2.4.99.6
            BRENDA, the Enzyme Database: 2.4.99.6
            CAS: 77537-85-0
///
ENTRY       EC 2.4.99.7                 Enzyme
NAME        alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3-N-
            acetylgalactosaminide 6-alpha-sialyltransferase;
            sialyltransferase;
            cytidine
            monophosphoacetylneuraminate-(alpha-N-acetylneuraminyl-2,3-beta-
            galactosyl-1,3)-N-acetylgalactosaminide-alpha-2,6-sialyltransferase;
            alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-
            galactosaminide alpha-2,6-sialyltransferase;
            SIAT7;
            ST6GALNAC;
            (alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetyl-
            galactosaminide 6-alpha-sialyltransferase;
            CMP-N-acetylneuraminate:(alpha-N-acetylneuraminyl-2,3-beta-D-
            galactosyl-1,3)-N-acetyl-D-galactosaminide
            alpha-2,6-N-acetylneuraminyl-transferase
CLASS       Transferases;
            Glycosyltransferases;
            Transferring other glycosyl groups
SYSNAME     CMP-N-acetylneuraminate:(alpha-N-acetylneuraminyl-2,3-beta-D-galacto
            syl-1,3)-N-acetyl-D-galactosaminide
            galactosamine-6-alpha-N-acetylneuraminyltransferase
REACTION    CMP-N-acetylneuraminate +
            N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-
            D-galactosaminyl-R = CMP +
            N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-[N-acetyl-
            alpha-neuraminyl-(2->6)]-N-acetyl-D-galactosaminyl-R [RN:R04635]
ALL_REAC    R04635
SUBSTRATE   CMP-N-acetylneuraminate [CPD:C00128];
            N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-
            D-galactosaminyl-R [CPD:C04885]
PRODUCT     CMP [CPD:C00055];
            N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-[N-acetyl-
            alpha-neuraminyl-(2->6)]-N-acetyl-D-galactosaminyl-R [CPD:C04926]
COMMENT     Attaches N-acetylneuraminic acid in alpha-2,6-linkage to
            N-acetyl-galactosamine only when present in the structure of
            alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosam
            inyl-R, where R may be protein or p-nitrophenol. Not identical with
            EC 2.4.99.3 alpha-N-acetylgalactosaminide
            alpha-2,6-sialyltransferase.
REFERENCE   1  [PMID:6190802]
  AUTHORS   Bergh ML, Hooghwinkel GJ, van den Eijnden DH.
  TITLE     Biosynthesis of the O-glycosidically linked oligosaccharide chains
            of fetuin. Indications for an alpha-N-acetylgalactosaminide alpha 2
            leads to 6 sialyltransferase with a narrow acceptor specificity in
            fetal calf liver.
  JOURNAL   J. Biol. Chem. 258 (1983) 7430-6.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00604  Glycosphingolipid biosynthesis - ganglioseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K03374  N-acetylgalactosaminide alpha-2,6-sialyltransferase
                        (sialyltransferase 7D)
GENES       HSA: 27090(ST6GALNAC4)
            PTR: 450108(ST6GALNAC4)
            MMU: 20448(St6galnac4)
            RNO: 407764(siat7D)
            CFA: 609133(ST6GALNAC4)
            BTA: 404124(SIAT7B)
            SSC: 396676(SIAT7B)
            GGA: 395182(ST6GALNAC4)
            SPU: 574822(LOC574822)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.99.7
            ExPASy - ENZYME nomenclature database: 2.4.99.7
            ExplorEnz - The Enzyme Database: 2.4.99.7
            ERGO genome analysis and discovery system: 2.4.99.7
            BRENDA, the Enzyme Database: 2.4.99.7
            CAS: 129924-24-9
///
ENTRY       EC 2.4.99.8                 Enzyme
NAME        alpha-N-acetylneuraminate alpha-2,8-sialyltransferase;
            cytidine monophosphoacetylneuraminate-ganglioside GM3;
            alpha-2,8-sialyltransferase;
            ganglioside GD3 synthase;
            ganglioside GD3 synthetase sialyltransferase;
            CMP-NeuAc:LM1(alpha2-8) sialyltranferase;
            GD3 synthase;
            SAT-2
CLASS       Transferases;
            Glycosyltransferases;
            Transferring other glycosyl groups
SYSNAME     CMP-N-acetylneuraminate:alpha-N-acetylneuraminyl-2,3-beta-D-galactos
            ide alpha-2,8-N-acetylneuraminyltransferase
REACTION    CMP-N-acetylneuraminate +
            alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-R = CMP +
            alpha-N-acetylneuraminyl-2,8-alpha-N-acetylneuraminyl-2,3-beta-D-
            galactosyl-R [RN:R04564]
ALL_REAC    R04564 > R04583 R05940(G) R06032(G);
            (other) R04632 R04649 R04661 R05113 R05995(G) R06000(G) R06005(G)
            R06009(G)
SUBSTRATE   CMP-N-acetylneuraminate [CPD:C00128];
            alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-R [CPD:C04683]
PRODUCT     CMP [CPD:C00055];
            alpha-N-acetylneuraminyl-2,8-alpha-N-acetylneuraminyl-2,3-beta-D-
            galactosyl-R [CPD:C04887]
COMMENT     Gangliosides act as acceptors.
REFERENCE   1  [PMID:7407217]
  AUTHORS   Eppler CM, Morre DJ, Keenan TW.
  TITLE     Ganglioside biosynthesis in rat liver: alteration of
            sialyltransferase activities by nucleotides.
  JOURNAL   Biochim. Biophys. Acta. 619 (1980) 332-43.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:3838172]
  AUTHORS   Higashi H, Basu M, Basu S.
  TITLE     Biosynthesis in vitro of disialosylneolactotetraosylceramide by a
            solubilized sialyltransferase from embryonic chicken brain.
  JOURNAL   J. Biol. Chem. 260 (1985) 824-8.
  ORGANISM  chicken [GN:gga]
REFERENCE   3  [PMID:4044605]
  AUTHORS   McCoy RD, Vimr ER, Troy FA.
  TITLE     CMP-NeuNAc:poly-alpha-2,8-sialosyl sialyltransferase and the
            biosynthesis of polysialosyl units in neural cell adhesion
            molecules.
  JOURNAL   J. Biol. Chem. 260 (1985) 12695-9.
  ORGANISM  rat [GN:rno], chicken [GN:gga]
REFERENCE   4  [PMID:6766128]
  AUTHORS   Yohe HC, Yu RK.
  TITLE     In vitro biosynthesis of an isomer of brain trisialoganglioside,
            GT1a.
  JOURNAL   J. Biol. Chem. 255 (1980) 608-13.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00602  Glycosphingolipid biosynthesis - neo-lactoseries
            PATH: map00603  Glycosphingolipid biosynthesis - globoseries
            PATH: map00604  Glycosphingolipid biosynthesis - ganglioseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K03371  alpha-N-acetyl-neuraminate alpha-2,8-sialyltransferase
                        (sialyltransferase 8A)
GENES       HSA: 6489(ST8SIA1)
            PTR: 465341(ST8SIA1)
            MMU: 20449(St8sia1)
            RNO: 25280(St8sia1)
            CFA: 477672(ST8SIA1)
            BTA: 282352(SIAT8A)
            GGA: 395860(ST8SIA1)
            XTR: 444887(st8siaI)
            DRE: 553210(st8sia1)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.99.8
            ExPASy - ENZYME nomenclature database: 2.4.99.8
            ExplorEnz - The Enzyme Database: 2.4.99.8
            ERGO genome analysis and discovery system: 2.4.99.8
            BRENDA, the Enzyme Database: 2.4.99.8
            CAS: 67339-00-8
///
ENTRY       EC 2.4.99.9                 Enzyme
NAME        lactosylceramide alpha-2,3-sialyltransferase;
            cytidine monophosphoacetylneuraminate-lactosylceramide alpha2,3-
            sialyltransferase;
            CMP-acetylneuraminate-lactosylceramide-sialyltransferase;
            CMP-acetylneuraminic acid:lactosylceramide sialyltransferase;
            CMP-sialic acid:lactosylceramide-sialyltransferase;
            cytidine monophosphoacetylneuraminate-lactosylceramide
            sialyltransferase;
            ganglioside GM3 synthetase;
            GM3 synthase;
            GM3 synthetase;
            SAT 1
CLASS       Transferases;
            Glycosyltransferases;
            Transferring other glycosyl groups
SYSNAME     CMP-N-acetylneuraminate:lactosylceramide
            alpha-2,3-N-acetylneuraminyltransferase
REACTION    CMP-N-acetylneuraminate +
            beta-D-galactosyl-1,4-beta-D-glucosylceramide = CMP +
            alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-beta-D-
            glucosylceramide [RN:R03488 R05937]
ALL_REAC    R03488 R05937(G);
            (other) R04630 R04647 R06003(G) R06007(G)
SUBSTRATE   CMP-N-acetylneuraminate [CPD:C00128];
            beta-D-galactosyl-1,4-beta-D-glucosylceramide [CPD:C01290]
PRODUCT     CMP [CPD:C00055];
            alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-beta-D-
            glucosylceramide [CPD:C04730]
COMMENT     Lactose cannot act as acceptor.
REFERENCE   1  [PMID:4631392]
  AUTHORS   Basu S, Kaufman B, Roseman S.
  TITLE     Enzymatic synthesis of glucocerebroside by a glucosyltransferase
            from embryonic chicken brain.
  JOURNAL   J. Biol. Chem. 248 (1973) 1388-94.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:4022]
  AUTHORS   Fishman PH, Bradley RM, Henneberry RC.
  TITLE     Butyrate-induced glycolipid biosynthesis in HeLa cells: properties
            of the induced sialyltransferase.
  JOURNAL   Arch. Biochem. Biophys. 172 (1976) 618-26.
  ORGANISM  rat [GN:rno], human [GN:hsa]
REFERENCE   3  [PMID:3838172]
  AUTHORS   Higashi H, Basu M, Basu S.
  TITLE     Biosynthesis in vitro of disialosylneolactotetraosylceramide by a
            solubilized sialyltransferase from embryonic chicken brain.
  JOURNAL   J. Biol. Chem. 260 (1985) 824-8.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00604  Glycosphingolipid biosynthesis - ganglioseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K03370  lactosylceramide alpha-2,3-sialyltransferase
                        (sialyltransferase 9)
GENES       HSA: 8869(ST3GAL5)
            PTR: 459371(ST3GAL5)
            MMU: 20454(St3gal5)
            RNO: 83505(St3gal5)
            CFA: 612022(ST3GAL5)
            BTA: 404164(ST3GAL-V)
            GGA: 407775(ST3GAL5)
            DRE: 394230(st3gal5)
STRUCTURES  PDB: 2EX0  2EX1  
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.99.9
            ExPASy - ENZYME nomenclature database: 2.4.99.9
            ExplorEnz - The Enzyme Database: 2.4.99.9
            ERGO genome analysis and discovery system: 2.4.99.9
            BRENDA, the Enzyme Database: 2.4.99.9
            CAS: 125752-90-1
///
ENTRY       EC 2.4.99.10                Enzyme
NAME        neolactotetraosylceramide alpha-2,3-sialyltransferase;
            sialyltransferase;
            cytidine monophosphoacetylneuraminate-neolactotetraosylceramide
            sialyltransferase;
            sialyltransferase 3;
            SAT-3
CLASS       Transferases;
            Glycosyltransferases;
            Transferring other glycosyl groups
SYSNAME     CMP-N-acetylneuraminate:neolactotetraosylceramide
            alpha-2,3-sialyltransferase
REACTION    CMP-N-acetylneuraminate +
            beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-
            galactosyl-1,4-D-glucosylceramide = CMP +
            alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-
            glucosaminyl-1,3-beta-D-galactosyl-1,4-D-glucosylceramide [RN:R04656
            R06026]
ALL_REAC    R04656 R06026(G);
            (other) R06037(G)
SUBSTRATE   CMP-N-acetylneuraminate [CPD:C00128];
            beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-
            galactosyl-1,4-D-glucosylceramide
PRODUCT     CMP [CPD:C00055];
            alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-
            glucosaminyl-1,3-beta-D-galactosyl-1,4-D-glucosylceramide
            [CPD:C04936]
REFERENCE   1  [PMID:7130178]
  AUTHORS   Basu M, Basu S, Stoffyn A, Stoffyn P.
  TITLE     Biosynthesis in vitro of sialyl(alpha 2-3)neolactotetraosylceramide
            by a sialyltransferase from embryonic chicken brain.
  JOURNAL   J. Biol. Chem. 257 (1982) 12765-9.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00602  Glycosphingolipid biosynthesis - neo-lactoseries
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K03792  beta-galactoside alpha-2,3-sialyltransferase
                        (sialyltransferase 10)
GENES       HSA: 10402(ST3GAL6)
            PTR: 460547(ST3GAL6)
            MMU: 54613(St3gal6)
            RNO: 304023(St3gal6)
            CFA: 478535(ST3GAL6)
            BTA: 444860(SIAT10)
            GGA: 395138(ST3GAL6)
            XLA: 398745(st3Gal-VI)
            XTR: 402790(3Gal-VI)
            SPU: 754196(LOC754196)
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.99.10
            ExPASy - ENZYME nomenclature database: 2.4.99.10
            ExplorEnz - The Enzyme Database: 2.4.99.10
            ERGO genome analysis and discovery system: 2.4.99.10
            BRENDA, the Enzyme Database: 2.4.99.10
            CAS: 83745-06-6
///
ENTRY       EC 2.4.99.11                Enzyme
NAME        lactosylceramide alpha-2,6-N-sialyltransferase;
            cytidine monophosphoacetylneuraminate-lactosylceramide
            sialyltransferase;
            CMP-acetylneuraminate-lactosylceramide-sialyltransferase;
            CMP-N-acetylneuraminic acid:lactosylceramide sialyltransferase;
            CMP-sialic acid:lactosylceramide sialyltransferase;
            cytidine monophosphoacetylneuraminate-lactosylceramide
            sialyltransferase
CLASS       Transferases;
            Glycosyltransferases;
            Transferring other glycosyl groups
SYSNAME     CMP-N-acetylneuraminate:lactosylceramide
            alpha-2,6-N-acetylneuraminyltransferase
REACTION    CMP-N-acetylneuraminate +
            beta-D-galactosyl-1,4-beta-D-glucosylceramide = CMP +
            alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-beta-D-
            glucosylceramide
ALL_REAC    (other) R03489 R06121(G)
SUBSTRATE   CMP-N-acetylneuraminate [CPD:C00128];
            beta-D-galactosyl-1,4-beta-D-glucosylceramide [CPD:C01290]
PRODUCT     CMP [CPD:C00055];
            alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-beta-D-
            glucosylceramide
REFERENCE   1  [PMID:2460092]
  AUTHORS   Albarracin I, Lassaga FE, Caputto R.
  TITLE     Purification and characterization of an endogenous inhibitor of the
            sialyltransferase CMP-N-acetylneuraminate: lactosylceramide alpha
            2,6-N-acetylneuraminyltransferase (EC 2.4.99.-).
  JOURNAL   Biochem. J. 254 (1988) 559-65.
  ORGANISM  chicken [GN:gga], cow [GN:bta]
REFERENCE   2  [PMID:606237]
  AUTHORS   Landa CA, Maccioni HJ, Arce A, Caputto R.
  TITLE     The biosynthesis of brain gangliosides. Separation of membranes with
            different ratios of ganglioside sialylating activity to
            gangliosides.
  JOURNAL   Biochem. J. 168 (1977) 325-32.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.4.99.11
            ExPASy - ENZYME nomenclature database: 2.4.99.11
            ExplorEnz - The Enzyme Database: 2.4.99.11
            ERGO genome analysis and discovery system: 2.4.99.11
            BRENDA, the Enzyme Database: 2.4.99.11
            CAS: 55071-95-9
///
ENTRY       EC 2.4.99.-                 Enzyme
CLASS       Transferases;
            Glycosyltransferases;
            Transferring other glycosyl groups
REACTION    (1) CMP-N-acetylneuraminate +
            N-Acetylneuraminyl-D-galactosyl-N-acetyl-D-galactosaminyl-(N-
            acetylneuraminyl)-D-galactosyl-D-glucosylceramide <=> CMP + GT1a
            [RN:R04660];
            (2) CMP-N-acetylneuraminate + GT1b <=> CMP + GQ1 [RN:R05114];
            (3) CMP-N-acetylneuraminate + Paragloboside <=> CMP +
            Sialyl-6-paragloboside [RN:R06215];
            (4) CMP-N-acetylneuraminate + nLc6Cer <=> CMP + VI6NeuAc-nLc6Cer
            [RN:R06216];
            (5) CMP-N-acetylneuraminate + V3Fuc-nLc6Cer <=> CMP + G00091
            [RN:R06232];
            (6) CMP-N-acetylneuraminate + G04461 <=> CMP + G04135 [RN:R06274]
SUBSTRATE   CMP-N-acetylneuraminate [CPD:C00128];
            N-Acetylneuraminyl-D-galactosyl-N-acetyl-D-galactosaminyl-(N-
            acetylneuraminyl)-D-galactosyl-D-glucosylceramide [CPD:C04927];
            GT1b [CPD:C06140];
            CMP-N-acetylneuraminate [GL:G10616];
            Paragloboside [GL:G00050];
            nLc6Cer [GL:G00067];
            V3Fuc-nLc6Cer [GL:G00089];
            [GL:G04461]
PRODUCT     CMP [CPD:C00055];
            GT1a [CPD:C06138];
            GQ1 [CPD:C06139];
            CMP [GL:G10621];
            Sialyl-6-paragloboside [GL:G00061];
            VI6NeuAc-nLc6Cer [GL:G00087];
            [GL:G00091];
            [GL:G04135]
///
ENTRY       EC 2.5.1.1                  Enzyme
NAME        dimethylallyltranstransferase;
            geranyl-diphosphate synthase;
            prenyltransferase;
            dimethylallyltransferase;
            DMAPP:IPP-dimethylallyltransferase;
            (2E,6E)-farnesyl diphosphate synthetase;
            diprenyltransferase;
            geranyl pyrophosphate synthase;
            geranyl pyrophosphate synthetase;
            trans-farnesyl pyrophosphate synthetase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     dimethylallyl-diphosphate:isopentenyl-diphosphate
            dimethylallyltranstransferase
REACTION    dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate +
            geranyl diphosphate [RN:R01658]
ALL_REAC    R01658;
            (other) R02003
SUBSTRATE   dimethylallyl diphosphate [CPD:C00235];
            isopentenyl diphosphate [CPD:C00129]
PRODUCT     diphosphate [CPD:C00013];
            geranyl diphosphate [CPD:C00341]
COMMENT     This enzyme will not accept larger prenyl diphosphates as efficient
            donors.
REFERENCE   1
  AUTHORS   Banthorpe, D.V., Bucknall, G.A., Doonan, H.J., Doonan, S. and Rowan,
            M.G.
  TITLE     Biosynthesis of geraniol and nerol in cell-free extracts of
            Tanacetum vulgare.
  JOURNAL   Phytochemistry 15 (1976) 91-100.
  ORGANISM  Tanacetum vulgare
REFERENCE   2  [PMID:736921]
  AUTHORS   Sagami H, Ogura K, Seto S, Kurokawa T.
  TITLE     A new prenyltransferase from Micrococcus lysodeikticus.
  JOURNAL   Biochem. Biophys. Res. Commun. 85 (1978) 572-8.
  ORGANISM  Micrococcus lysodeikticus
PATHWAY     PATH: map00100  Biosynthesis of steroids
            PATH: map00900  Terpenoid biosynthesis
ORTHOLOGY   KO: K00787  dimethylallyltranstransferase
GENES       HSA: 2224(FDPS) 9453(GGPS1)
            MMU: 110196(Fdps) 14593(Ggps1)
            RNO: 83791(Fdps)
            CFA: 479198(GGPS1) 480129(FDPS)
            BTA: 281156(FDPS) 780882(GGPS1)
            GGA: 427092(GGPS1)
            XLA: 414582(MGC83119)
            DRE: 336798(ggps1)
            SPU: 576515(LOC576515)
            DME: Dmel_CG12389(Fpps) Dmel_CG8593(qm)
            CEL: R06C1.2
            ATH: AT2G18620 AT3G14530 AT3G14550(GGPS3) AT3G20160 AT3G29430
                 AT3G32040 AT5G47770(FPS1)
            OSA: 4323892 4324245 4343721
            CME: CMK058C CMM269C
            SCE: YJL167W(ERG20) YPL069C(BTS1)
            AGO: AGOS_AEL122W AGOS_AEL238C
            PIC: PICST_46658(BTS1)
            CAL: CaO19.6674(bts1)
            CGR: CAGL0H05269g CAGL0L00319g
            SPO: SPAC6F12.13c SPBC36.06c
            AFM: AFUA_2G12660
            CNE: CNE04510 CNI00090
            UMA: UM04459.1
            ECU: ECU11_1810
            DDI: DDBDRAFT_0190001 DDBDRAFT_0206219 DDB_0215017(fps)
                 DDB_0233098
            PFA: PF11_0295
            CPV: cgd4_2550
            CHO: Chro.40285
            TAN: TA17400
            TPV: TP03_0857
            TBR: Tb927.7.3360
            TCR: 508323.9 511823.70
            LMA: LmjF22.1360
            VFI: VF0712
            FTU: FTT1562(ispA)
            FTF: FTF1562(ispA)
            ABO: ABO_1906(idsA) ABO_2165(ggpS)
            RMA: Rmag_0366
            CVI: CV_3954(idsA) CV_3958(ispA)
            AJS: Ajs_0840
            VEI: Veis_3918
            CHA: CHAB381_0895
            SAT: SYN_02457 SYN_03252
            BME: BMEI1532
            BRA: BRADO2023(ispB)
            BBT: BBta_2349(ispB)
            GOX: GOX0251 GOX1996
            GBE: GbCGDNIH1_0220
            SPH: MGAS10270_Spy1247(fps)
            SPI: MGAS10750_Spy1338(fps)
            SPJ: MGAS2096_Spy1249(fps)
            SPK: MGAS9429_Spy1225(fps)
            SPA: M6_Spy1251
            SSA: SSA_0676(ispA)
            LSL: LSL_1028
            MTU: Rv3398c(idsA1)
            MTC: MT3491 MT3506
            MBO: Mb3431c(idsA1)
            MBB: BCG_3468c(idsA1)
            MSM: MSMEG_1133
            CGL: NCgl2092(cgl2172)
            SCO: SCO5250(2SC7G11.12) SCO6763(SC6A5.12)
            SMA: SAV2997(ptlB) SAV3006(idsB)
            PAC: PPA0732
            FRA: Francci3_0822
            FAL: FRAAL1431(fppS) FRAAL2161(idsA)
            SEN: SACE_3979 SACE_4328 SACE_4646(ptlB) SACE_4909 SACE_5289
            FNU: FN1327
            CTA: CTA_0681(ispA)
            PMB: A9601_11751(ispA)
            PMC: P9515_11601(ispA)
            PMF: P9303_09331(ispA)
            PMG: P9301_11761(ispA)
            PME: NATL1_15151(ispA)
            BTH: BT_2058
            BFR: BF3745
            BFS: BF3533
            PGI: PG0784
            SRU: SRU_1874(idsA)
            CHU: CHU_0461(ispA)
            CTE: CT0256
            CCH: Cag_1446
            PVI: Cvib_0973
            PLT: Plut_1765
            DRA: DR_1395
            DGE: Dgeo_0496
            MMP: MMP0045(idsA)
            MMQ: MmarC5_1635
            MAC: MA0606(idsA)
            MBA: Mbar_A1417
            MMA: MM_1767
            MST: Msp_0854(idsA)
            MSI: Msm_1443
            MKA: MK0774(ispA)
            AFU: AF2286(idsA)
            HAL: VNG1150G(idsA)
            HMA: rrnAC0081(idsA)
            HWA: HQ2889A(idsA)
            NPH: NP3696A(idsA_3)
            PTO: PTO0848 PTO1199
            PHO: PH1072
            PAB: PAB2389(idsA)
            PFU: PF1102
            TKO: TK1468
            APE: APE_1764.1
            HBU: Hbut_0540
            SSO: SSO0061(gds-1)
            STO: ST2058
            SAI: Saci_0092(gds)
            PAI: PAE1013
STRUCTURES  PDB: 1R9C  1UBV  1UBW  1UBX  1UBY  2AZJ  2AZK  2F7M  2F89  2F8C  
                 2F8Z  2F92  2F94  2F9K  2OPN  2Q80  2QIS  2RAH  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.1
            ExPASy - ENZYME nomenclature database: 2.5.1.1
            ExplorEnz - The Enzyme Database: 2.5.1.1
            ERGO genome analysis and discovery system: 2.5.1.1
            BRENDA, the Enzyme Database: 2.5.1.1
            CAS: 9032-79-5
///
ENTRY       EC 2.5.1.2                  Enzyme
NAME        thiamine pyridinylase;
            pyrimidine transferase;
            thiaminase I;
            thiamin hydrolase;
            thiamin pyridinolase;
            thiaminase;
            thiamine pyridinolase;
            thiamin pyridinylase;
            thiamin:base 2-methyl-4-aminopyrimidine-5-methenyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     thiamine:base 2-methyl-4-aminopyrimidine-5-methenyltransferase
REACTION    thiamine + pyridine =
            1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyridinium +
            4-methyl-5-(2-hydroxyethyl)thiazole [RN:R02863]
ALL_REAC    R02863
SUBSTRATE   thiamine [CPD:C00378];
            pyridine [CPD:C00747]
PRODUCT     1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyridinium;
            4-methyl-5-(2-hydroxyethyl)thiazole
COMMENT     Various bases and thiol compounds can act instead of pyridine.
REFERENCE   1  [PMID:13158184]
  AUTHORS   FUJITA A.
  TITLE     Thiaminase.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 15 (1954) 389-421.
REFERENCE   2  [PMID:13471505]
  AUTHORS   KENTEN RH.
  TITLE     [Pteridium aquilinum (L.) Kuhn.]
  JOURNAL   Biochem. J. 67 (1957) 25-33.
  ORGANISM  Pteridium aquilinum
REFERENCE   3  [PMID:4966932]
  AUTHORS   Wittliff JL, Airth RL.
  TITLE     The extracellular thiaminase I of Bacillus thiaminolyticus. I.
            Purification and physicochemical properties.
  JOURNAL   Biochemistry. 7 (1968) 736-44.
  ORGANISM  Bacillus thiaminolyticus
PATHWAY     PATH: map00730  Thiamine metabolism
GENES       ECI: UTI89_C0447(thiJ)
            BPM: BURPS1710b_A0059
            BTE: BTH_II1306
            BCZ: BCZK3357(thiJ)
            SSA: SSA_2006
            CBO: CBO0770
            LIL: LA2252(thiJ)
            LIC: LIC11685
STRUCTURES  PDB: 2GM7  2GM8  2THI  3THI  4THI  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.2
            ExPASy - ENZYME nomenclature database: 2.5.1.2
            ExplorEnz - The Enzyme Database: 2.5.1.2
            ERGO genome analysis and discovery system: 2.5.1.2
            BRENDA, the Enzyme Database: 2.5.1.2
            CAS: 9030-35-7
///
ENTRY       EC 2.5.1.3                  Enzyme
NAME        thiamine-phosphate diphosphorylase;
            thiamine phosphate pyrophosphorylase;
            thiamine monophosphate pyrophosphorylase;
            TMP-PPase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     2-methyl-4-amino-5-hydroxymethylpyrimidine-diphosphate:4-methyl-5-(2
            -phosphoethyl)thiazole
            2-methyl-4-aminopyrimidine-5-methenyltransferase
REACTION    2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate +
            4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine
            phosphate [RN:R03223]
ALL_REAC    R03223
SUBSTRATE   2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate [CPD:C04752];
            4-methyl-5-(2-phosphono-oxyethyl)thiazole
PRODUCT     diphosphate [CPD:C00013];
            thiamine phosphate [CPD:C01081]
REFERENCE   1  [PMID:13807175]
  AUTHORS   CAMIENER GW, BROWN GM.
  TITLE     The biosynthesis of thiamine. 2. Fractionation of enzyme system and
            identification of thiazole monophosphate and thiamine monophosphate
            as intermediates.
  JOURNAL   J. Biol. Chem. 235 (1960) 2411-7.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2
  AUTHORS   Leder, I.G.
  TITLE     The enzymatic synthesis of thiamine monophosphate.
  JOURNAL   J. Biol. Chem. 236 (1961) 3066-3071.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00730  Thiamine metabolism
ORTHOLOGY   KO: K00788  thiamine-phosphate pyrophosphorylase
GENES       ATH: AT1G22940(TH1)
            CME: CMP214C
            SCE: YPL214C(THI6)
            AGO: AGOS_AFL110C
            CGR: CAGL0E05808g
            SPO: SPAC23H4.10c(thi4)
            CNE: CNI03710
            PFA: PFF0680c
            ECO: b3993(thiE)
            ECJ: JW3957(thiE)
            ECE: Z5568(thiE)
            ECS: ECs4916
            ECC: c4950(thiE)
            ECI: UTI89_C3826(thiE)
            ECP: ECP_4206
            ECV: APECO1_24812(thiE)
            ECW: EcE24377A_4535(thiE)
            ECX: EcHS_A4227(thiE)
            STY: STY3722(thiE)
            STT: t3468(thiE)
            SPT: SPA4000(thiE)
            SEC: SC4044(thiE)
            STM: STM4163(thiE)
            YPE: YPO3740(thiE)
            YPK: y0490(thiE)
            YPM: YP_3103(thiE)
            YPA: YPA_3612
            YPN: YPN_0226
            YPP: YPDSF_3737
            YPS: YPTB0289(thiE)
            YPI: YpsIP31758_3854(thiE)
            YEN: YE0292(thiE)
            SFL: SF4065(thiE)
            SFX: S3670(thiE)
            SFV: SFV_4065(thiE)
            SSN: SSON_4166(thiE)
            SBO: SBO_4014(thiE)
            SDY: SDY_3733(thiE)
            ECA: ECA0231(thiE)
            PLU: plu0485(thiE)
            WBR: WGLp506(thiE)
            ENT: Ent638_0206
            SPE: Spro_0283
            HIT: NTHI0542(thiE)
            HIP: CGSHiEE_00910(thiE)
            HIQ: CGSHiGG_05315(thiE)
            HSO: HS_0090(thiE)
            PMU: PM1260(thiE)
            MSU: MS0676(thiE)
            APL: APL_0540(thiE)
            ASU: Asuc_1508
            XFA: XF0378 XF1120
            XFT: PD0412(mutT) PD1687(thiE)
            XCC: XCC0736 XCC3269(thiE)
            XCB: XC_0895 XC_3499
            XCV: XCV0840 XCV3532(thiE)
            XAC: XAC0789 XAC3415(thiE)
            XOO: XOO1123(thiE) XOO3816
            XOM: XOO_1019(XOO1019) XOO_3593(XOO3593)
            VCH: VC0062
            VCO: VC0395_A2451(thiE)
            VVU: VV1_0963(thiE)
            VVY: VV3206(thiE)
            VPA: VP3026 VPA0130
            VFI: VF0033 VFA0322
            PPR: PBPRA0107
            PAE: PA3976(thiE) PA4400
            PAU: PA14_12400(thiE) PA14_57190(mutT)
            PPU: PP_1348 PP_4783(thiE)
            PPF: Pput_4659
            PST: PSPTO_4397 PSPTO_4799(thiE)
            PSB: Psyr_4091(mutT) Psyr_4341(thiE)
            PSP: PSPPH_4097 PSPPH_4383(thiE)
            PFL: PFL_4779 PFL_5428(thiE)
            PFO: Pfl_4425(mutT) Pfl_4946
            PEN: PSEEN4474 PSEEN4803(thiE)
            PMY: Pmen_3773
            PAR: Psyc_0705(thiE) Psyc_1507
            PCR: Pcryo_0679
            PRW: PsycPRwf_0829
            ACI: ACIAD1200 ACIAD2236
            ACB: A1S_2465
            SON: SO_2444(thiDE)
            SDN: Sden_1771
            SFR: Sfri_2200
            SAZ: Sama_1859
            SBL: Sbal_2023
            SBM: Shew185_2322
            SLO: Shew_2095
            SPC: Sputcn32_1923
            SSE: Ssed_2014
            SPL: Spea_2382
            SHE: Shewmr4_1882
            SHM: Shewmr7_2096
            SHN: Shewana3_1937
            SHW: Sputw3181_2085
            ILO: IL0766(thiE)
            CPS: CPS_0254(thiDE)
            PHA: PSHAa0484(thiDE)
            PAT: Patl_1935
            SDE: Sde_0828
            PIN: Ping_0361 Ping_2372
            MAQ: Maqu_0687
            CBU: CBU_0334(thiDE)
            CBD: COXBU7E912_1745(thiDE)
            LPN: lpg1568(thiDE)
            LPF: lpl1457(thiDE)
            LPP: lpp1526(thiDE)
            MCA: MCA1678 MCA2999(thiE)
            TCX: Tcr_0144 Tcr_0592
            NOC: Noc_0306(mutT) Noc_0604
            AEH: Mlg_2067 Mlg_2084
            HHA: Hhal_2012
            HCH: HCH_00141(thiE) HCH_05871
            CSA: Csal_3303
            ABO: ABO_0355(thiE) ABO_0609
            MMW: Mmwyl1_2391
            BCI: BCI_0042(thiE)
            RMA: Rmag_0082
            VOK: COSY_0087(thiE)
            NME: NMB2069
            NMA: NMA0363(thiE)
            NMC: NMC2050(thiE)
            NGO: NGO2007
            CVI: CV_0150 CV_3611
            RSO: RSc0108(thiE1) RSp0984(thiE2)
            REU: Reut_A0209
            REH: H16_A0239(thiE)
            RME: Rmet_0166
            BMA: BMA2727(thiE) BMAA0287
            BMV: BMASAVP1_A3227(thiE)
            BML: BMA10299_A1776(thiE)
            BMN: BMA10247_2777(thiE)
            BXE: Bxe_A0386
            BVI: Bcep1808_0392
            BUR: Bcep18194_A3511 Bcep18194_B2246
            BCN: Bcen_2694 Bcen_4514
            BCH: Bcen2424_0413 Bcen2424_3850
            BAM: Bamb_0331
            BPS: BPSL3151(thiE) BPSS1216 BPSS1796
            BPM: BURPS1710b_3705(thiE) BURPS1710b_A0210(thiE2)
                 BURPS1710b_A0878(thiE2)
            BPL: BURPS1106A_3736(thiE)
            BPD: BURPS668_3678(thiE)
            BTE: BTH_I3005 BTH_II0583
            PNU: Pnuc_0892
            BPE: BP0316(thiE) BP3809
            BPA: BPP3935(thiE) BPP3955
            BBR: BB4408(thiE) BB4428
            RFR: Rfer_2467 Rfer_2471
            POL: Bpro_0041
            PNA: Pnap_0023
            AAV: Aave_3071
            AJS: Ajs_1783
            VEI: Veis_4311
            HAR: HEAR0264
            MMS: mma_0318(thiE)
            NEU: NE1424 NE2215
            NET: Neut_0653 Neut_1538
            NMU: Nmul_A1007 Nmul_A2628
            EBA: ebA4102 ebB48(thiE)
            AZO: azo3450(thiE)
            DAR: Daro_3706 Daro_3901
            TBD: Tbd_0027 Tbd_2556
            MFA: Mfla_2230 Mfla_2663
            HPY: HP0843(thiB)
            HPJ: jhp0781(thiE)
            HPA: HPAG1_0828
            HHE: HH1828(thiE)
            WSU: WS0788
            TDN: Tmden_1173
            CJE: Cj1081c(thiE)
            CJR: CJE1224(thiE)
            CJJ: CJJ81176_1099(thiE)
            CJU: C8J_1022(thiE)
            CFF: CFF8240_1234
            CCV: CCV52592_0497(thiE) CCV52592_2068 CCV52592_2114
            CHA: CHAB381_0436(thiE)
            CCO: CCC13826_0338 CCC13826_0400(thiE) CCC13826_0951
            ABU: Abu_0447(thiE) Abu_2274
            NIS: NIS_0854 NIS_1197
            SUN: SUN_0530(thiE)
            GSU: GSU0587(thiE) GSU0605
            GME: Gmet_2909 Gmet_2935
            GUR: Gura_3660
            PCA: Pcar_0342 Pcar_0607 Pcar_2235
            PPD: Ppro_3476
            DVU: DVU2091(thiE-1) DVU2362(thiE-2)
            DVL: Dvul_0900 Dvul_1139
            DDE: Dde_1379 Dde_1558
            LIP: LI0324(thiE)
            DPS: DP1089(thiE)
            ADE: Adeh_0075 Adeh_2516
            AFW: Anae109_0075 Anae109_1348
            MXA: MXAN_3267 MXAN_5087(thiE)
            SAT: SYN_00302 SYN_00442
            SFU: Sfum_1824 Sfum_3508
            AMA: AM318(thiE)
            APH: APH_0960(thiE)
            ERU: Erum2060(thiE)
            ERW: ERWE_CDS_02080(thiE)
            ERG: ERGA_CDS_02030(thiE)
            ECN: Ecaj_0208
            ECH: ECH_0893(thiE)
            NSE: NSE_0220
            PUB: SAR11_0583(thiE)
            MLO: mll5789 mlr3913
            MES: Meso_2565 Meso_3182
            PLA: Plav_2104
            SME: SMb20618(thiE) SMc03996(thiE2)
            SMD: Smed_4170
            ATU: Atu3289 Atu3750(thiE)
            ATC: AGR_L_2166 AGR_L_3059
            RET: RHE_CH03527(thiEch) RHE_PB00079(thiEb) RHE_PE00336(thiEe)
            RLE: RL4040(thiE) pRL110442(thiE)
            BME: BMEI0329 BMEI1736
            BMF: BAB1_0215 BAB1_1719
            BMS: BR0214 BR1707
            BMB: BruAb1_0209 BruAb1_1692
            OAN: Oant_0281
            BJA: bll1519 blr6658(thiE)
            BRA: BRADO0790 BRADO0791 BRADO1119 BRADO5712(thiE)
            BBT: BBta_6225(thiE) BBta_6930
            RPA: RPA0939 RPA3576(thiE)
            RPB: RPB_1955 RPB_4472
            RPC: RPC_2163 RPC_4774
            RPD: RPD_3431 RPD_4318
            RPE: RPE_2070 RPE_4721
            NWI: Nwi_2467 Nwi_2738
            NHA: Nham_2894 Nham_3535
            BHE: BH04870(thiE1) BH14940(thiE2)
            BQU: BQ04070(thiE1) BQ11920(thiE2)
            BBK: BARBAKC583_0442(thiE)
            XAU: Xaut_1867
            CCR: CC_3264
            SIL: SPO0048(thiE) SPO2056
            SIT: TM1040_1337 TM1040_3653
            RSP: RSP_0648(thiE) RSP_3828
            RSH: Rsph17029_2301
            RSQ: Rsph17025_0584
            JAN: Jann_2434
            RDE: RD1_0750(thiE) RD1_2730(thiE) RD1_3611(thiDE)
            PDE: Pden_0038
            MMR: Mmar10_2591
            HNE: HNE_3185(thiE) HNE_3553
            ZMO: ZMO0332(thiE) ZMO1425(thiE)
            NAR: Saro_1962
            SAL: Sala_1315
            SWI: Swit_3151
            ELI: ELI_05245
            GOX: GOX0009 GOX2228
            GBE: GbCGDNIH1_1089
            ACR: Acry_0381
            RRU: Rru_A1080
            MAG: amb2858
            MGM: Mmc1_0633 Mmc1_3286
            ABA: Acid345_3286 Acid345_4410
            SUS: Acid_4942 Acid_6375
            BSU: BG10572(thiC)
            BHA: BH1431
            BAN: BA0377(thiE)
            BAR: GBAA0377(thiE)
            BAA: BA_0953
            BAT: BAS0363
            BCE: BC0420(thiE)
            BCA: BCE_0487(thiE)
            BCZ: BCZK0349(thiE) BCZK0639(thiE)
            BCY: Bcer98_0364
            BTK: BT9727_0353(thiE)
            BTL: BALH_0375(thiE) BALH_0666
            BLI: BL03866(thiE)
            BLD: BLi04051(thiE)
            BCL: ABC1733(thiC)
            BAY: RBAM_035550(thiE)
            BPU: BPUM_1095(tenI) BPUM_3483(thiE)
            OIH: OB0472
            GKA: GK1511(thiE)
            SAU: SA1894(thiE)
            SAV: SAV2091(thiE)
            SAM: MW2014(thiE)
            SAR: SAR2180(thiE)
            SAS: SAS1995
            SAC: SACOL2083(thiE)
            SAB: SAB1975c(thiE)
            SAA: SAUSA300_2047(thiE)
            SAO: SAOUHSC_02328
            SAJ: SaurJH9_2128
            SAH: SaurJH1_2166
            SEP: SE1690
            SER: SERP1698(thiE)
            SHA: SH0943(thiE)
            SSP: SSP0792
            LMO: lmo0318
            LMF: LMOf2365_0336(thiE)
            LIN: lin0343
            LWE: lwe0289(thiE)
            LLA: L0201(thiE)
            LLC: LACR_1375
            LLM: llmg_1218(thiE)
            SPN: SP_0718 SP_0725
            SPR: spr0630(thiE) spr0637(thiE)
            SPD: SPD_0624(thiE-1) SPD_0631(thiE-2)
            SAG: SAG0842(thiE)
            SAN: gbs0860
            SAK: SAK_0965(thiE)
            LPL: lp_0115(thiE)
            LSA: LSA0057(thiE)
            LBR: LVIS_2097
            LCA: LSEI_0300
            LRE: Lreu_1015
            EFA: EF2776(thiE)
            CAC: CAC0495(thiC) CAC2920(tenI)
            CPE: CPE1336(thiE) CPE1599(thiE)
            CPF: CPF_1543(thiE) CPF_1852
            CPR: CPR_1336(thiE) CPR_1569
            CTC: CTC01746(tenI) CTC01751
            CNO: NT01CX_0248(thiE) NT01CX_1504
            CTH: Cthe_0601
            CDF: CD1601(thiE1)
            CBO: CBO0449(thiC)
            CBA: CLB_0490(thiE)
            CBH: CLC_0523(thiE)
            CBF: CLI_0534(thiE)
            CBE: Cbei_4487
            CKL: CKL_1635(thiE1) CKL_2917(thiE2)
            AMT: Amet_1247 Amet_4232
            CHY: CHY_0746 CHY_1265(thiE)
            DSY: DSY1403
            DRM: Dred_0076 Dred_0593
            SWO: Swol_0641
            CSC: Csac_0254
            TTE: TTE2233(thiE)
            MTA: Moth_0547 Moth_2162
            MTU: Rv0414c(thiE)
            MTC: MT0427(thiE)
            MBO: Mb0422c(thiE)
            MBB: BCG_0453c(thiE)
            MLE: ML0300(thiE)
            MPA: MAP3897c(thiE)
            MAV: MAV_4748(thiE)
            MSM: MSMEG_0789(thiE)
            MVA: Mvan_0707
            MGI: Mflv_0198
            MMC: Mmcs_0544
            MKM: Mkms_0556
            MJL: Mjls_0534
            CGL: NCgl1961(cgl2038)
            CGB: cg1654(thiD1) cg2236(thiE)
            CEF: CE1591 CE1933
            CDI: DIP0030(thiE)
            CJK: jk0854(thiE)
            NFA: nfa53400(thiE)
            RHA: RHA1_ro02191(thiE)
            SCO: SCO2104(SC4A10.37c)
            SMA: SAV6099(thiE)
            CMI: CMM_2116(thiED)
            ART: Arth_2782
            AAU: AAur_2765(thiE)
            PAC: PPA0112 PPA0886
            NCA: Noca_3406
            TFU: Tfu_1046
            FRA: Francci3_3070
            FAL: FRAAL5075(thiE)
            ACE: Acel_0990
            KRA: Krad_0853
            SEN: SACE_0505(thiE)
            STP: Strop_3889
            RXY: Rxyl_2395 Rxyl_2788
            FNU: FN1758
            RBA: RB6331(thiE)
            CCA: CCA00203(thiE)
            CAB: CAB198(thiE)
            CFE: CF0804(thiE)
            LIL: LA1991(thiE)
            LIC: LIC11915(thiE)
            LBJ: LBJ_1526(thiE)
            LBL: LBL_1750(thiE)
            SYN: sll0635(thiE)
            SYW: SYNW1604(thiE)
            SYC: syc0491_c(thiE)
            SYF: Synpcc7942_1057
            SYD: Syncc9605_0896
            SYE: Syncc9902_1502
            SYG: sync_0791(thiE)
            SYR: SynRCC307_1737(thiE)
            SYX: SynWH7803_1716(thiE)
            CYA: CYA_1569(thiE)
            CYB: CYB_1815(thiE)
            TEL: tlr1947(thiE)
            GVI: gll0403(thiE)
            ANA: alr1343
            AVA: Ava_5047
            PMA: Pro1348(thiE)
            PMM: PMM1274(thiE)
            PMT: PMT0363(thiE)
            PMN: PMN2A_0840
            PMI: PMT9312_1368
            PMB: A9601_14731(thiE)
            PMC: P9515_14351(thiE)
            PMF: P9303_19391(thiE)
            PMG: P9301_14591(thiE)
            PME: NATL1_16941(thiE)
            TER: Tery_2583
            BTH: BT_0652
            BFR: BF2529
            BFS: BF2558
            SRU: SRU_1552(thiE)
            CHU: CHU_0242(thiE) CHU_0246(thiE)
            FJO: Fjoh_1600
            FPS: FP0429(thiE1) FP0431(thiE2)
            CTE: CT1174 CT1175(thiE)
            CCH: Cag_0815 Cag_0816
            CPH: Cpha266_1532
            PVI: Cvib_0943
            PLT: Plut_0958 Plut_0959
            DET: DET0782
            DEH: cbdb_A758(thiE)
            DEB: DehaBAV1_0708
            RRS: RoseRS_1927
            RCA: Rcas_4121
            DRA: DR_A0174
            DGE: Dgeo_1923
            TTH: TTC0315
            TTJ: TTHA0674
            AAE: aq_1366(thiE1) aq_558(thiE2)
            MMP: MMP1139(thiE)
            MMQ: MmarC5_0446
            MMZ: MmarC7_0390
            MVN: Mevan_0461
            MAC: MA2722(thiE)
            MBA: Mbar_A3318
            MMA: MM_3235
            MHU: Mhun_1934
            MEM: Memar_0261
            MBN: Mboo_2056
            MST: Msp_0683
            MSI: Msm_0917
            HMA: rrnAC2143(thiE)
            HWA: HQ2655A(thiE)
            NPH: NP4054A(thiE)
            TAC: Ta1277
            TVO: TVN0508
            PTO: PTO1288
            PAB: PAB1645(thiE)
            PFU: PF1334
            RCI: RCIX2678(thiE)
STRUCTURES  PDB: 1G4E  1G4P  1G4S  1G4T  1G67  1G69  1G6C  1XI3  2TPS  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.3
            ExPASy - ENZYME nomenclature database: 2.5.1.3
            ExplorEnz - The Enzyme Database: 2.5.1.3
            ERGO genome analysis and discovery system: 2.5.1.3
            BRENDA, the Enzyme Database: 2.5.1.3
            CAS: 9030-30-2
///
ENTRY       EC 2.5.1.4                  Enzyme
NAME        adenosylmethionine cyclotransferase;
            adenosylmethioninase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     S-adenosyl-L-methionine alkyltransferase (cyclizing)
REACTION    S-adenosyl-L-methionine = 5'-methylthioadenosine +
            2-aminobutan-4-olide [RN:R00180]
ALL_REAC    R00180
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019]
PRODUCT     5'-methylthioadenosine [CPD:C00170];
            2-aminobutan-4-olide [CPD:C02926]
REFERENCE   1
  AUTHORS   Mudd, S.H.
  TITLE     Enzymatic cleavage of S-adenosylmethionine.
  JOURNAL   J. Biol. Chem. 234 (1959) 87-92.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2
  AUTHORS   Mudd, S.H.
  TITLE     The mechanism of the enzymatic cleavage of S-adenosylmethionine to
            alpha-amino-gamma-butyrolactone.
  JOURNAL   J. Biol. Chem. 234 (1959) 1784-1786.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.4
            ExPASy - ENZYME nomenclature database: 2.5.1.4
            ExplorEnz - The Enzyme Database: 2.5.1.4
            ERGO genome analysis and discovery system: 2.5.1.4
            BRENDA, the Enzyme Database: 2.5.1.4
            CAS: 9030-34-6
///
ENTRY       EC 2.5.1.5                  Enzyme
NAME        galactose-6-sulfurylase;
            porphyran sulfatase;
            galactose-6-sulfatase;
            galactose 6-sulfatase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     D-galactose-6-sulfate:alkyltransferase (cyclizing)
REACTION    Eliminates sulfate from the D-galactose 6-sulfate residues of
            porphyran, producing 3,6-anhydrogalactose residues
REFERENCE   1
  AUTHORS   Rees, D.A.
  TITLE     Enzymic desulphation of porphyran.
  JOURNAL   Biochem. J. 80 (1961) 449-453.
  ORGANISM  Porphyra umbilicalis
REFERENCE   2
  AUTHORS   Rees, D.A.
  TITLE     Enzymic synthesis of 3:6-anhydro-L-galactose within porphyran from
            L-galactose 6-sulphate units.
  JOURNAL   Biochem. J. 81 (1961) 347-352.
  ORGANISM  Porphyra umbilicalis
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.5
            ExPASy - ENZYME nomenclature database: 2.5.1.5
            ExplorEnz - The Enzyme Database: 2.5.1.5
            ERGO genome analysis and discovery system: 2.5.1.5
            BRENDA, the Enzyme Database: 2.5.1.5
            CAS: 9030-36-8
///
ENTRY       EC 2.5.1.6                  Enzyme
NAME        methionine adenosyltransferase;
            adenosylmethionine synthetase;
            ATP-methionine adenosyltransferase;
            methionine S-adenosyltransferase;
            methionine-activating enzyme;
            S-adenosyl-L-methionine synthetase;
            S-adenosylmethionine synthase;
            S-adenosylmethionine synthetase;
            AdoMet synthetase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     ATP:L-methionine S-adenosyltransferase
REACTION    ATP + L-methionine + H2O = phosphate + diphosphate +
            S-adenosyl-L-methionine [RN:R00177]
ALL_REAC    R00177;
            (other) R04771
SUBSTRATE   ATP [CPD:C00002];
            L-methionine [CPD:C00073];
            H2O [CPD:C00001]
PRODUCT     phosphate [CPD:C00009];
            diphosphate [CPD:C00013];
            S-adenosyl-L-methionine [CPD:C00019]
REFERENCE   1
  AUTHORS   Cantoni, G.L.
  TITLE     S-Adenosylmethionine: A new intermediate formed enzymatically from
            L-methionine and adenosinetriphosphate.
  JOURNAL   J. Biol. Chem. 204 (1953) 403-416.
  ORGANISM  rabbit, rat [GN:rno], pig [GN:ssc]
REFERENCE   2  [PMID:13416303]
  AUTHORS   CANTONI GL, DURELL J.
  TITLE     Activation of methionine for transmethylation.  II.  The
            methionine-activating enzyme; studies on the mechanism of the
            reaction.
  JOURNAL   J. Biol. Chem. 225 (1957) 1033-48.
  ORGANISM  rabbit, rat [GN:rno]
REFERENCE   3  [PMID:13538985]
  AUTHORS   MUDD SH, CANTONI GL.
  TITLE     Activation of methionine for transmethylation. III. The
            methionine-activating enzyme of Bakers' yeast.
  JOURNAL   J. Biol. Chem. 231 (1958) 481-92.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00271  Methionine metabolism
            PATH: map00450  Selenoamino acid metabolism
ORTHOLOGY   KO: K00789  S-adenosylmethionine synthetase
GENES       HSA: 27430(MAT2B) 4143(MAT1A)
            PTR: 450555(MAT1A)
            MMU: 11720(Mat1a) 232087(Mat2a)
            RNO: 171347(Mat2a) 25331(Mat1a)
            CFA: 475770(MAT2A)
            GGA: 423628(MAT1A)
            XLA: 379867(m(2)21ab)
            XTR: 395032(TEgg043h19.1)
            DRE: 334195(mat1a)
            SPU: 548618(LOC548618)
            DME: Dmel_CG2674(M(2)21AB)
            CEL: C06E7.1 C06E7.3 C49F5.1(sams-1) T13A10.11(tag-32)
            ATH: AT2G36880(MAT3) AT3G17390(MTO3)
            OSA: 4325163 4337733
            CME: CMN227C
            SCE: YDR502C(SAM2) YLR180W(SAM1)
            AGO: AGOS_AFR692C
            PIC: PICST_65158(SAM2)
            CGR: CAGL0B01122g CAGL0J08415g
            SPO: SPBC14F5.05c(sam1)
            ANI: AN1222.2
            AFM: AFUA_1G10630
            AOR: AO090038000357
            CNE: CNA04060
            DDI: DDB_0230070
            PFA: PFI1090w
            CPV: cgd7_2650
            CHO: Chro.70301
            TAN: TA11070
            TPV: TP04_0893
            TET: TTHERM_00444470
            TBR: Tb927.6.4840 Tb927.6.4850 Tb927.6.4860 Tb927.6.4870
                 Tb927.6.4880 Tb927.6.4890 Tb927.6.4900 Tb927.6.4910
                 Tb927.6.4920
            TCR: 506945.160 510445.50
            LMA: LmjF30.3500 LmjF30.3520
            EHI: 103.t00003 116.t00023 203.t00005 376.t00007 70.t00021
                 70.t00027
            ECO: b2942(metK)
            ECJ: JW2909(metK)
            ECE: Z4287(metK)
            ECS: ECs3818
            ECC: c3528(metK) c4547
            ECI: UTI89_C3331(metK)
            ECP: ECP_2935
            ECV: APECO1_2302 APECO1_3589(metK)
            ECW: EcE24377A_3284(metK)
            ECX: EcHS_A3099
            STY: STY3243(metK)
            STT: t3002(metK)
            SPT: SPA2953(metK)
            SEC: SC3030(metK)
            STM: STM3090(metK)
            YPE: YPO0931(metK)
            YPK: y3314(metK)
            YPM: YP_3512(metK)
            YPA: YPA_0335
            YPN: YPN_3127
            YPP: YPDSF_0585
            YPS: YPTB3203(metK)
            YPI: YpsIP31758_0841(metK)
            SFL: SF2933(metK)
            SFX: S3137(metK)
            SFV: SFV_2996(metK)
            SSN: SSON_3096(metK)
            SBO: SBO_3048(metK)
            SDY: SDY_3130(metK)
            ECA: ECA3920(metK)
            PLU: plu3683(metK)
            BUC: BU408(metK)
            BAS: BUsg393(metK)
            WBR: WGLp316(metK)
            SGL: SG2019
            ENT: Ent638_3346
            SPE: Spro_3974
            BFL: Bfl252(metK)
            BPN: BPEN_259(metK)
            HIN: HI1172(metX)
            HIT: NTHI1340(metK)
            HIP: CGSHiEE_06180
            HIQ: CGSHiGG_09560
            HDU: HD0569(metK)
            HSO: HS_1623(metK)
            PMU: PM1027(metX)
            MSU: MS0669(metK)
            APL: APL_1080(metK)
            ASU: Asuc_0835
            XFA: XF0392
            XFT: PD1677(metK)
            XCC: XCC0761(metK)
            XCB: XC_3471
            XCV: XCV0865(metK)
            XAC: XAC0813(metK)
            XOO: XOO3791(metK)
            XOM: XOO_3571(XOO3571)
            VCH: VC0472
            VCO: VC0395_A0024(metK)
            VVU: VV1_1536
            VVY: VV2863
            VPA: VP2606
            VFI: VF0439
            PPR: PBPRA3134
            PAE: PA0546(metK)
            PAU: PA14_07090(metK)
            PAP: PSPA7_0649(metK)
            PPU: PP_4967(metK)
            PPF: Pput_4840
            PST: PSPTO_0383(metK)
            PSB: Psyr_4794
            PSP: PSPPH_4823(metK)
            PFL: PFL_5788(metK)
            PFO: Pfl_5269
            PEN: PSEEN5026(metK)
            PMY: Pmen_0454
            PAR: Psyc_0828(metK)
            PCR: Pcryo_0850
            PRW: PsycPRwf_0879
            ACI: ACIAD2037(metK)
            SON: SO_0929(metK)
            SDN: Sden_1082
            SFR: Sfri_0646
            SAZ: Sama_2760
            SBL: Sbal_0826
            SBM: Shew185_3541
            SLO: Shew_0751
            SPC: Sputcn32_0871
            SSE: Ssed_0873
            SPL: Spea_0787
            SHE: Shewmr4_0772
            SHM: Shewmr7_3251
            SHN: Shewana3_3354
            SHW: Sputw3181_3302
            ILO: IL2215(metK)
            CPS: CPS_1256(metK)
            PHA: PSHAa0670(metK)
            PAT: Patl_3331
            SDE: Sde_0470
            PIN: Ping_3227
            MAQ: Maqu_3042
            CBU: CBU_2030(metK)
            CBD: COXBU7E912_2131(metK)
            LPN: lpg2022(metK)
            LPF: lpl1999(metK)
            LPP: lpp2004(metK)
            MCA: MCA0139(metK-1) MCA0450(metK-2)
            FTU: FTT0149c(metK)
            FTF: FTF0149c(metK)
            FTW: FTW_0239(metK)
            FTL: FTL_1739
            FTH: FTH_1678(metK)
            FTA: FTA_1842(metK)
            FTN: FTN_1563(metK)
            TCX: Tcr_1821
            NOC: Noc_2678
            AEH: Mlg_2262
            HHA: Hhal_0919 Hhal_1676
            HCH: HCH_01533(metK)
            CSA: Csal_0385
            ABO: ABO_2617(metK)
            MMW: Mmwyl1_4320
            AHA: AHA_3124(metK)
            DNO: DNO_0971(metK)
            BCI: BCI_0015(metK)
            RMA: Rmag_0738
            VOK: COSY_0683(metK)
            NME: NMB1799
            NMA: NMA0663(metK)
            NMC: NMC0422(metK)
            NGO: NGO0106
            CVI: CV_0963(metK)
            RSO: RSc0134(metK)
            REU: Reut_A0201 Reut_C6197
            REH: H16_A0230(metK1) H16_A1975(metK2)
            RME: Rmet_0156
            BMA: BMA3262(metK)
            BMV: BMASAVP1_A2924(metK)
            BML: BMA10299_A2165(metK)
            BMN: BMA10247_3424(metK)
            BXE: Bxe_A4371
            BVI: Bcep1808_3166 Bcep1808_7266
            BUR: Bcep18194_A6431
            BCN: Bcen_2467
            BCH: Bcen2424_3081
            BAM: Bamb_3129
            BPS: BPSL0212(metK)
            BPM: BURPS1710b_0395(metK)
            BPL: BURPS1106A_0211(metK)
            BPD: BURPS668_0199(metK)
            BTE: BTH_I0174(metK)
            PNU: Pnuc_2003
            BPE: BP3071(metK)
            BPA: BPP0192(metK)
            BBR: BB0195(metK)
            RFR: Rfer_3880
            POL: Bpro_0767
            PNA: Pnap_0660
            AAV: Aave_0979
            AJS: Ajs_0705
            VEI: Veis_4844
            MPT: Mpe_A3252
            HAR: HEAR2952(metK)
            MMS: mma_3198
            NEU: NE0659(metK)
            NET: Neut_1893
            NMU: Nmul_A0036 Nmul_A2541
            EBA: ebA3942(metK)
            AZO: azo0589(metK)
            DAR: Daro_0188
            TBD: Tbd_2521
            MFA: Mfla_0194
            HPY: HP0197
            HPJ: jhp0183(metK)
            HPA: HPAG1_0191
            HHE: HH1540(metK)
            HAC: Hac_0382(metK)
            WSU: WS1994(metX)
            TDN: Tmden_1476 Tmden_1777
            CJE: Cj1096c(metK)
            CJR: CJE1239(metK)
            CJJ: CJJ81176_1114(metK)
            CJU: C8J_1037(metK)
            CJD: JJD26997_0626(metK)
            CFF: CFF8240_0721(metK)
            CCV: CCV52592_0703(metK) CCV52592_1319
            CHA: CHAB381_1103(metK)
            CCO: CCC13826_0068(metK) CCC13826_1787
            ABU: Abu_0445(metK)
            NIS: NIS_0393(metK) NIS_1074
            SUN: SUN_1452 SUN_2054(metK)
            GSU: GSU0918 GSU1880(metK)
            GME: Gmet_1290 Gmet_2549
            GUR: Gura_1332 Gura_1448
            PCA: Pcar_1928
            PPD: Ppro_0044 Ppro_2839
            DVU: DVU2449(metK)
            DVL: Dvul_0786
            DDE: Dde_1496
            LIP: LI0726(metK)
            BBA: Bd0850(metK)
            DPS: DP0801
            ADE: Adeh_0154
            AFW: Anae109_0159
            MXA: MXAN_6517(metK)
            SAT: SYN_00253 SYN_00417
            SFU: Sfum_0367
            RTY: RT0764(metK)
            RFE: RF_1241(metK) RF_1242(metK)
            RRI: A1G_06605
            WOL: WD0136(metK)
            WBM: Wbm0699
            AMA: AM1288(metK)
            APH: APH_0007(metK) APH_0058
            ERU: Erum0070(metK)
            ERW: ERWE_CDS_09520(metK)
            ERG: ERGA_CDS_09440(metK)
            ECN: Ecaj_0945
            ECH: ECH_0018(metK)
            NSE: NSE_0488(metK)
            PUB: SAR11_0387(metK)
            MLO: mlr5545 mlr6115
            MES: Meso_3924
            PLA: Plav_3623
            SME: SMc01109(metK)
            SMD: Smed_0046
            ATU: Atu0362(metK)
            ATC: AGR_C_632
            RET: RHE_CH00370(metK)
            RLE: RL0389(metK)
            BME: BMEI1970
            BMF: BAB1_2160
            BMS: BR2160(metK)
            BMB: BruAb1_2133(metK)
            BOV: BOV_2072(metK)
            OAN: Oant_0752
            BJA: bll5945(metK) bll7989(mat)
            BRA: BRADO5239(metK)
            BBT: BBta_5699(metK)
            RPA: RPA4016(metK)
            RPB: RPB_1588
            RPC: RPC_1177 RPC_4154
            RPD: RPD_1596
            RPE: RPE_4204
            NWI: Nwi_2378
            NHA: Nham_2753
            BHE: BH02200(metK)
            BQU: BQ02080(metK)
            BBK: BARBAKC583_1249(metK)
            XAU: Xaut_1816
            CCR: CC_0050
            SIL: SPOA0011(metK)
            SIT: TM1040_0193
            RSP: RSP_3595(metK)
            RSH: Rsph17029_3280
            JAN: Jann_0706
            RDE: RD1_3916(metK)
            PDE: Pden_1873
            MMR: Mmar10_2439
            HNE: HNE_0786(metK)
            ZMO: ZMO0273(metK)
            NAR: Saro_0284
            SAL: Sala_3139
            SWI: Swit_3373
            ELI: ELI_14285
            GOX: GOX0866
            GBE: GbCGDNIH1_2399
            ACR: Acry_1054
            RRU: Rru_A0917 Rru_A3776
            MAG: amb4469
            MGM: Mmc1_3332
            ABA: Acid345_3661 Acid345_4566
            SUS: Acid_1686 Acid_5274
            BSU: BG11840(metK)
            BHA: BH3300(metK)
            BAN: BA5017(metK)
            BAR: GBAA5017(metK)
            BAA: BA_5437
            BAT: BAS4660
            BCE: BC4761
            BCA: BCE_0391(metK) BCE_4914(metK)
            BCZ: BCZK4517(metK)
            BCY: Bcer98_3437
            BTK: BT9727_4500(metK)
            BTL: BALH_4340(metK)
            BLI: BL02632(metK)
            BLD: BLi03196(metK)
            BCL: ABC2878(metK)
            BAY: RBAM_027570
            BPU: BPUM_2686
            OIH: OB2314(metK)
            GKA: GK2849
            GTN: GTNG_2750
            SAU: SA1608(metK)
            SAV: SAV1790(metK)
            SAM: MW1728(metK)
            SAR: SAR1870
            SAS: SAS1711
            SAC: SACOL1837(metK)
            SAB: SAB1645c
            SAA: SAUSA300_1730(metK)
            SAO: SAOUHSC_01909
            SAJ: SaurJH9_1841
            SAH: SaurJH1_1877
            SEP: SE1458
            SER: SERP1352(metK)
            SHA: SH1139(metK)
            SSP: SSP0976
            LMO: lmo1664(metK)
            LMF: LMOf2365_1688(metK)
            LIN: lin1773(metK)
            LWE: lwe1683(metK)
            LLA: L153408(metK)
            LLC: LACR_2161
            LLM: llmg_2160(metK)
            SPY: SPy_0538 SPy_1359(metK)
            SPZ: M5005_Spy_0445(metK1) M5005_Spy_1108(metK2)
            SPM: spyM18_0604 spyM18_1372(metK)
            SPG: SpyM3_0382 SpyM3_1034(metK)
            SPS: SPs0826 SPs1471
            SPH: MGAS10270_Spy0446(metK1) MGAS10270_Spy1178(metK2)
            SPI: MGAS10750_Spy0465(metK1) MGAS10750_Spy1207(metK2)
            SPJ: MGAS2096_Spy0464(metK1) MGAS2096_Spy1170(metK2)
            SPK: MGAS9429_Spy0444(metK1) MGAS9429_Spy1152(metK2)
            SPF: SpyM50751(metK)
            SPA: M6_Spy0479 M6_Spy1082 M6_Spy1147
            SPB: M28_Spy0433(metK1) M28_Spy1100(metK2)
            SPN: SP_0762
            SPR: spr0671(metK)
            SPD: SPD_0664(metK)
            SAG: SAG0831(metK)
            SAN: gbs0849(metK)
            SAK: SAK_0736(metK) SAK_0954(metK)
            SMU: SMU.1573(metK)
            STC: str1172(metK)
            STL: stu1172(metK)
            STE: STER_1135
            SSA: SSA_1495(metK)
            SSU: SSU05_1621
            SSV: SSU98_1632
            SGO: SGO_0987(metK)
            LPL: lp_1301(metK)
            LJO: LJ0677
            LAC: LBA1622(metK)
            LSA: LSA0468(metK)
            LSL: LSL_0441(metK)
            LDB: Ldb1575(metK)
            LBU: LBUL_1455
            LBR: LVIS_1523
            LCA: LSEI_0877
            LGA: LGAS_0456
            LRE: Lreu_1296
            PPE: PEPE_0641
            EFA: EF0784(metK)
            OOE: OEOE_0838
            STH: STH118
            CAC: CAC2856(metK)
            CPE: CPE2177(metK)
            CPF: CPF_2435(metK)
            CPR: CPR_2145(metK)
            CTC: CTC00321
            CNO: NT01CX_0516(metK)
            CTH: Cthe_2251
            CDF: CD0130(metE)
            CBO: CBO0168(metE)
            CBA: CLB_0208(metK)
            CBH: CLC_0222(metK)
            CBF: CLI_0231(metK)
            CBE: Cbei_0428 Cbei_4050
            CKL: CKL_1633(metK1) CKL_2650(metK2) CKL_3674(metK3)
            AMT: Amet_0716 Amet_4040
            CHY: CHY_0138(metK)
            DSY: DSY2726
            DRM: Dred_3096
            PTH: PTH_2759(metK)
            SWO: Swol_1234
            CSC: Csac_0857
            TTE: TTE0488(metK)
            MTA: Moth_0894
            MGE: MG_047(metX)
            MPN: MPN060(metX)
            MPU: MYPU_7020(metK)
            MPE: MYPE940(metK)
            MGA: MGA_0128(metK)
            MMY: MSC_0492(metK)
            MMO: MMOB3090(metK)
            MHY: mhp450(metK)
            MHJ: MHJ_0448(metK)
            MHP: MHP7448_0451(metK)
            MSY: MS53_0610(metK)
            MCP: MCAP_0478(metK)
            UUR: UU412(metK)
            MFL: Mfl240
            MTU: Rv1392(metK)
            MTC: MT1437(metK)
            MBO: Mb1427(metK)
            MBB: BCG_1453(metK)
            MLE: ML0544(metK)
            MPA: MAP1126(metK)
            MAV: MAV_3382(metK)
            MSM: MSMEG_3055(metK)
            MVA: Mvan_2670
            MGI: Mflv_3737
            MMC: Mmcs_2373
            MKM: Mkms_2420
            MJL: Mjls_2414
            CGL: NCgl1541(cgl1603)
            CGB: cg1806(metK)
            CEF: CE1723(metK)
            CDI: DIP1325(metK)
            CJK: jk1016(metK)
            NFA: nfa36130(metK)
            RHA: RHA1_ro07158(metK)
            SCO: SCO1476(metK)
            SMA: SAV6874(metK)
            TWH: TWT360(metK)
            TWS: TW409(metK)
            LXX: Lxx11150(metK)
            ART: Arth_2256
            AAU: AAur_2259(metK)
            PAC: PPA1193 PPA1587
            NCA: Noca_2439
            TFU: Tfu_1065
            FRA: Francci3_2993 Francci3_3192
            FAL: FRAAL4932(metK) FRAAL5227(metK)
            ACE: Acel_1290
            KRA: Krad_2989
            SEN: SACE_2103(metK) SACE_3900(metK)
            STP: Strop_1136 Strop_1864
            BLO: BL1786(metK)
            BAD: BAD_0541(metK)
            RXY: Rxyl_1470
            FNU: FN0355
            RBA: RB5444(metK)
            BGA: BG0375(metK)
            BAF: BAPKO_0385(metK)
            TPA: TP0794
            TDE: TDE2470(metK)
            LIL: LA2633(metK)
            LIC: LIC11354(metK)
            LBJ: LBJ_1645(metK)
            LBL: LBL_1864(metK)
            SYN: sll0927(metX)
            SYW: SYNW1987(metK)
            SYC: syc1641_d(metX)
            SYF: Synpcc7942_2463
            SYD: Syncc9605_0466
            SYE: Syncc9902_1869
            SYG: sync_0529(metK)
            SYR: SynRCC307_0413(metK)
            SYX: SynWH7803_0513(metK)
            CYA: CYA_1186(metK)
            CYB: CYB_2590(metK)
            TEL: tll0978
            GVI: gll2577
            ANA: all3244 alr4124
            AVA: Ava_0780 Ava_4899
            PMA: Pro0349(metK)
            PMM: PMM0311(metK)
            PMT: PMT1670(metK)
            PMN: PMN2A_1687
            PMI: PMT9312_0317
            PMB: A9601_03351(metK)
            PMC: P9515_03441(metK)
            PMF: P9303_22181(metK)
            PMG: P9301_03361(metK)
            PMH: P9215_03361
            PME: NATL1_04001(metK)
            TER: Tery_4661
            BTH: BT_3219
            BFR: BF0061
            BFS: BF0072(metK)
            PGI: PG1896(metK)
            SRU: SRU_2755(metK)
            CHU: CHU_3400(metK)
            GFO: GFO_0314(metK)
            FJO: Fjoh_1489
            FPS: FP0268(metK)
            CTE: CT0540(metK) CT0722(metK)
            CCH: Cag_1547
            CPH: Cpha266_0746 Cpha266_0922
            PVI: Cvib_1121
            PLT: Plut_0551 Plut_0672
            DET: DET0067(metK-1) DET0512(metK-2)
            DEH: cbdb_A476(metK)
            DEB: DehaBAV1_0488
            RRS: RoseRS_0489 RoseRS_0919
            RCA: Rcas_0160 Rcas_1562
            DRA: DR_0640
            DGE: Dgeo_0287
            TTH: TTC1279
            TTJ: TTHA1642
            AAE: aq_1154(metK) aq_1226
            TMA: TM1658
            TPT: Tpet_1133
            TME: Tmel_1756
            FNO: Fnod_0125
            MJA: MJ1208
            MMP: MMP1640
            MMQ: MmarC5_1768
            MMZ: MmarC7_0913
            MAE: Maeo_0461
            MVN: Mevan_0945
            MAC: MA0216(mat) MA0962(mat)
            MBA: Mbar_A1313 Mbar_A1862
            MMA: MM_1502 MM_2076
            MBU: Mbur_1330
            MTP: Mthe_0726 Mthe_1403
            MHU: Mhun_0923
            MEM: Memar_0838
            MBN: Mboo_1064
            MTH: MTH1376
            MST: Msp_1470(mat)
            MSI: Msm_1340
            MKA: MK1508
            AFU: AF0050
            HAL: VNG1297C
            HMA: rrnAC1233(metK)
            HWA: HQ2584A(metK)
            NPH: NP3100A(mat)
            TAC: Ta0059
            TVO: TVN0015
            PTO: PTO0744
            PHO: PH1824
            PAB: PAB2094
            PFU: PF1866
            TKO: TK0545
            RCI: RCIX2255(mat) RRC334(metK)
            APE: APE_1596
            SMR: Smar_1298
            IHO: Igni_0158
            HBU: Hbut_0083
            SSO: SSO0199(mat)
            STO: ST0235
            SAI: Saci_0798(matT)
            MSE: Msed_0231
            PAI: PAE0677
            PIS: Pisl_0691
            PCL: Pcal_2103
            PAS: Pars_2333
            TPE: Tpen_0737
STRUCTURES  PDB: 1FUG  1MXA  1MXB  1MXC  1O90  1O92  1O93  1O9T  1P7L  1QM4  
                 1RG9  1XRA  1XRB  1XRC  2OBV  2P02  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.6
            ExPASy - ENZYME nomenclature database: 2.5.1.6
            ExplorEnz - The Enzyme Database: 2.5.1.6
            ERGO genome analysis and discovery system: 2.5.1.6
            BRENDA, the Enzyme Database: 2.5.1.6
            CAS: 9012-52-6
///
ENTRY       EC 2.5.1.7                  Enzyme
NAME        UDP-N-acetylglucosamine 1-carboxyvinyltransferase;
            MurA transferase;
            UDP-N-acetylglucosamine 1-carboxyvinyl-transferase;
            UDP-N-acetylglucosamine enoylpyruvyltransferase;
            enoylpyruvate transferase;
            phosphoenolpyruvate-UDP-acetylglucosamine-3-enolpyruvyltransferase;
            phosphoenolpyruvate:UDP-2-acetamido-2-deoxy-D-glucose
            2-enoyl-1-carboxyethyltransferase;
            phosphoenolpyruvate:uridine diphosphate N-acetylglucosamine
            enolpyruvyltransferase;
            phosphoenolpyruvate:uridine-5'-diphospho-N-acetyl-2-amino-2-
            deoxyglucose 3-enolpyruvyltransferase;
            phosphopyruvate-uridine diphosphoacetylglucosamine
            pyruvatetransferase;
            pyruvate-UDP-acetylglucosamine transferase;
            pyruvate-uridine diphospho-N-acetylglucosamine transferase;
            pyruvate-uridine diphospho-N-acetyl-glucosamine transferase;
            pyruvic-uridine diphospho-N-acetylglucosaminyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     phosphoenolpyruvate:UDP-N-acetyl-D-glucosamine
            1-carboxyvinyltransferase
REACTION    phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate +
            UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine [RN:R00660]
ALL_REAC    R00660
SUBSTRATE   phosphoenolpyruvate [CPD:C00074];
            UDP-N-acetyl-D-glucosamine [CPD:C00043]
PRODUCT     phosphate [CPD:C00009];
            UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine [CPD:C04631]
REFERENCE   1  [PMID:5699062]
  AUTHORS   Gunetileke KG, Anwar RA.
  TITLE     Biosynthesis of uridine diphospho-N-acetylmuramic acid. II.
            Purification and properties of pyruvate-uridine
            diphospho-N-acetylglucosamine transferase and characterization of
            uridine diphospho-N-acetylenopyruvylglucosamine.
  JOURNAL   J. Biol. Chem. 243 (1968) 5770-8.
  ORGANISM  Enterobacter cloacae
REFERENCE   2  [PMID:1123336]
  AUTHORS   Zemell RI, Anwar RA.
  TITLE     Pyruvate-uridine diphospho-N-acetylglucosamine transferase.
            Purification to homogeneity and feedback inhibition.
  JOURNAL   J. Biol. Chem. 250 (1975) 3185-92.
  ORGANISM  Enterobacter cloacae
REFERENCE   3  [PMID:11699883]
  AUTHORS   van Heijenoort J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit.
  JOURNAL   Nat. Prod. Rep. 18 (2001) 503-19.
  ORGANISM  Enterobacter cloacae, Escherichia coli [GN:eco]
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K00790  UDP-N-acetylglucosamine 1-carboxyvinyltransferase
GENES       AFM: AFUA_2G09590
            ECO: b3189(murA)
            ECJ: JW3156(murA)
            ECE: Z4552(murA)
            ECS: ECs4068
            ECC: c3947(murA)
            ECI: UTI89_C3623(murA)
            ECP: ECP_3276
            ECV: APECO1_3245(murA)
            ECW: EcE24377A_3675(murA)
            ECX: EcHS_A3382
            STY: STY3486(murA)
            STT: t3224(murA)
            SPT: SPA3174(murA)
            SEC: SC3245(murA)
            STM: STM3307(murA)
            YPE: YPO3569(murA)
            YPK: y0140(murA)
            YPM: YP_3824(murA)
            YPA: YPA_3734
            YPN: YPN_3451
            YPS: YPTB3513(murA)
            YPI: YpsIP31758_0454(murA)
            SFL: SF3229(murA)
            SFX: S3447(murA)
            SFV: SFV_3219(murA)
            SSN: SSON_3337(murA)
            SBO: SBO_3193(murA)
            SDY: SDY_3370(murA)
            ECA: ECA0301(murA)
            PLU: plu4028(murA)
            BUC: BU386(murA)
            BAS: BUsg373(murA)
            BAB: bbp349(murA)
            WBR: WGLp329(murA)
            SGL: SG0211
            BFL: Bfl046(murA)
            BPN: BPEN_047(murA)
            HIT: NTHI1244(murA)
            HIP: CGSHiEE_06685
            HIQ: CGSHiGG_09145
            HDU: HD0253(murA)
            HSO: HS_1167(murZ)
            PMU: PM0180(murZ)
            MSU: MS1707(murA)
            APL: APL_1286(murA)
            XFA: XF1415
            XFT: PD0644(murA)
            XCC: XCC2795(murA)
            XCB: XC_1318
            XCV: XCV3110(murA)
            XAC: XAC2965(murA)
            XOO: XOO1290(murA)
            XOM: XOO_1190(XOO1190)
            VCH: VC2514
            VCO: VC0395_A2096(murA)
            VVU: VV1_0679
            VVY: VV0461
            VPA: VP2658
            VFI: VF0401
            PPR: PBPRA3242
            PAE: PA4450(murA)
            PAU: PA14_57810(murA)
            PAP: PSPA7_5022(murA)
            PPU: PP_0964(murA)
            PST: PSPTO_4441(murA)
            PSB: Psyr_4135
            PSP: PSPPH_4139(murA)
            PFL: PFL_0927(murA)
            PFO: Pfl_0869
            PEN: PSEEN1105(murA)
            PAR: Psyc_1904(murA)
            PCR: Pcryo_2194
            ACI: ACIAD0660(murA)
            SON: SO_3948(murA)
            SDN: Sden_0502
            SFR: Sfri_3364
            SAZ: Sama_3075
            SLO: Shew_3298
            SHE: Shewmr4_0685
            SHM: Shewmr7_3337
            SHN: Shewana3_0684
            SHW: Sputw3181_3446
            ILO: IL0409(murA)
            CPS: CPS_4530(murA)
            PHA: PSHAa2538(murA)
            PAT: Patl_0555
            SDE: Sde_3170
            MAQ: Maqu_2703
            CBU: CBU_0751(murA)
            CBD: COXBU7E912_0764(murA)
            LPN: lpg0847(murA)
            LPF: lpl0612 lpl0878(murA)
            LPP: lpp0909(murA)
            MCA: MCA1965(murA)
            FTU: FTT1305c(murA)
            FTF: FTF1305c(murA)
            FTW: FTW_0741(murA)
            FTL: FTL_0413
            FTH: FTH_0406(murA)
            FTN: FTN_0447(murA)
            TCX: Tcr_0987
            NOC: Noc_2780
            AEH: Mlg_2217
            HCH: HCH_05307(murA)
            CSA: Csal_2214
            ABO: ABO_0560(murA)
            AHA: AHA_3935(murA)
            DNO: DNO_0853(murA)
            BCI: BCI_0028(murA)
            VOK: COSY_0554(murA)
            NME: NMB0011
            NMA: NMA0258(murA)
            NMC: NMC2149(murA)
            NGO: NGO1918
            CVI: CV_0440(murA)
            RSO: RSc2953(murA)
            REU: Reut_A3113
            REH: H16_A3418(murA)
            RME: Rmet_3250
            BMA: BMA2716(murA) BMAA1237
            BMV: BMASAVP1_A3237(murA)
            BML: BMA10299_A1786(murA)
            BMN: BMA10247_2767(murA)
            BXE: Bxe_A0396
            BUR: Bcep18194_A3521 Bcep18194_B1627
            BCN: Bcen_2684 Bcen_3974
            BCH: Bcen2424_0423 Bcen2424_4393
            BAM: Bamb_0341
            BPS: BPSL3141(murA) BPSS0984
            BPM: BURPS1710b_3695(murA) BURPS1710b_A2596
            BPL: BURPS1106A_3726(murA)
            BPD: BURPS668_3668(murA)
            BTE: BTH_I2995(murA) BTH_II1407
            BPE: BP3766(murA)
            BPA: BPP2157 BPP4265(murA)
            BBR: BB1554 BB4852(murA)
            RFR: Rfer_2944
            POL: Bpro_0802
            AJS: Ajs_0352
            MPT: Mpe_A0829
            HAR: HEAR3071(murA)
            MMS: mma_3290
            NEU: NE1852(murA)
            NET: Neut_1556
            NMU: Nmul_A0886
            EBA: ebA1302(murA)
            AZO: azo0815(murA)
            DAR: Daro_3393
            TBD: Tbd_1891
            MFA: Mfla_0246
            HPY: HP0648
            HPJ: jhp0593(murA)
            HPA: HPAG1_0633
            HHE: HH0576(murA)
            HAC: Hac_1066(mur)
            WSU: WS0342(murA)
            TDN: Tmden_0556
            CJE: Cj0858c(murA)
            CJR: CJE0945(murA)
            CJJ: CJJ81176_0874(murA)
            CJU: C8J_0805(murA)
            CJD: JJD26997_1007(murA)
            CFF: CFF8240_0888(murA)
            CCV: CCV52592_1092(murA)
            CHA: CHAB381_0919(murA)
            CCO: CCC13826_0064 CCC13826_1265(murA)
            ABU: Abu_1843(murA)
            NIS: NIS_0957(murA)
            SUN: SUN_1190(murA)
            GSU: GSU3102(murA)
            GME: Gmet_0382
            PCA: Pcar_2690
            PPD: Ppro_3044
            DVU: DVU3258(murA)
            DDE: Dde_0546
            LIP: LI0838(murA)
            BBA: Bd0071(murA)
            DPS: DP2724
            ADE: Adeh_0364
            MXA: MXAN_4909(murA)
            SAT: SYN_01793
            SFU: Sfum_1715
            RPR: RP579
            RTY: RT0568(murA)
            RCO: RC0883(murA)
            RFE: RF_0945(murA)
            RBE: RBE_0994(murA)
            RAK: A1C_04505
            RBO: A1I_03685
            RRI: A1G_04875
            OTS: OTBS_1615(murA)
            WOL: WD1197(murA)
            WBM: Wbm0740
            AMA: AM145(murA)
            PUB: SAR11_0473(murA)
            MLO: mll6459 mll7251
            MES: Meso_0192
            SME: SMc02305(murA)
            ATU: Atu0539(murA)
            ATC: AGR_C_953
            RET: RHE_CH00579(murA)
            RLE: RL0611(murA)
            BME: BMEI1666
            BMF: BAB1_0287(murA)
            BMS: BR0254(murA)
            BMB: BruAb1_0282(murA)
            BOV: BOV_0272(murA)
            BJA: bll0822(murA)
            BRA: BRADO0005(murA) BRADO6639(murA)
            BBT: BBta_0011(murA) BBta_0895(murA)
            RPA: RPA4533(murA)
            RPB: RPB_4352
            RPC: RPC_4418
            RPD: RPD_4281
            RPE: RPE_4488
            NWI: Nwi_0246
            NHA: Nham_0285
            BHE: BH14420(murA)
            BQU: BQ11390(murA)
            BBK: BARBAKC583_0201(murA)
            CCR: CC_2350
            SIL: SPOA0137(murA)
            SIT: TM1040_3565
            RSP: RSP_0633
            JAN: Jann_2886
            RDE: RD1_1065(murA)
            MMR: Mmar10_1126
            HNE: HNE_1344(murA)
            ZMO: ZMO1724(murA)
            NAR: Saro_0449
            SAL: Sala_0499
            ELI: ELI_12305
            GOX: GOX0850
            GBE: GbCGDNIH1_1036
            RRU: Rru_A2931
            MAG: amb1982
            MGM: Mmc1_1221
            ABA: Acid345_2108
            BSU: BG10414(murZ) BG11955(murA)
            BHA: BH3749(murA) BH3784(murZ)
            BAN: BA5529(murA1) BA5578(murA2)
            BAR: GBAA5529(murA1) GBAA5578(murA2)
            BAA: BA_0383 BA_0435
            BAT: BAS5137 BAS5183
            BCE: BC5288 BC5334
            BCA: BCE_5412(murA1) BCE_5463(murA2)
            BCZ: BCZK4987(murA) BCZK5034(murA2)
            BTK: BT9727_4969(murA) BT9727_5018(murA2)
            BTL: BALH_4792(murA) BALH_4832(murA)
            BLI: BL03971(murAB) BL04004(murAA)
            BLD: BLi03922(murAA) BLi03958(murAB)
            BCL: ABC3847(murA) ABC3881(murZ)
            BAY: RBAM_033920 RBAM_034260
            BPU: BPUM_3321 BPUM_3354
            OIH: OB2972(murA) OB3003(murZ)
            GKA: GK3341 GK3384
            GTN: GTNG_3329
            SAU: SA1902(murA) SA1926(murZ)
            SAV: SAV2099(murA) SAV2124(murZ)
            SAM: MW2024(murA) MW2048(murZ)
            SAR: SAR2188(murA1) SAR2212(murA2)
            SAS: SAS2003 SAS2027
            SAC: SACOL2092(murAA) SACOL2116(murAB)
            SAB: SAB1984c(murA1) SAB2008c(murA2)
            SAA: SAUSA300_2055(murA) SAUSA300_2078(murA)
            SAO: SAOUHSC_02337 SAOUHSC_02365
            SEP: SE1698 SE1722
            SER: SERP1706(murAA) SERP1731(murAB)
            SHA: SH0911(murZ) SH0935(murA)
            SSP: SSP0760 SSP0784
            LMO: lmo2526(murA) lmo2552(murZ)
            LMF: LMOf2365_2499(murA-1) LMOf2365_2524(murA-2)
            LIN: lin2670(murA) lin2697(murZ)
            LWE: lwe2474(murA-1) lwe2502(murA-2)
            LLA: L113067(murA1) L134243(murA2)
            LLC: LACR_0348 LACR_0548
            LLM: llmg_0326(murA1) llmg_0517(murA2)
            SPY: SPy_0763 SPy_1358(murZ)
            SPZ: M5005_Spy_0584(murA) M5005_Spy_1107(murZ)
            SPM: spyM18_0821(murA) spyM18_1371(murA)
            SPG: SpyM3_0502(murA) SpyM3_1033(murZ)
            SPS: SPs0827 SPs1352
            SPH: MGAS10270_Spy0639(murA) MGAS10270_Spy1177(murZ)
            SPI: MGAS10750_Spy0668(murA) MGAS10750_Spy1206(murZ)
            SPJ: MGAS2096_Spy0646(murA) MGAS2096_Spy1169(murZ)
            SPK: MGAS9429_Spy0638(murA) MGAS9429_Spy1151(murZ)
            SPF: SpyM50752(murA2) SpyM51224(murA1)
            SPA: M6_Spy0601 M6_Spy1081
            SPB: M28_Spy0562(murA) M28_Spy1099(murZ)
            SPN: SP_1081 SP_1966
            SPR: spr0989(murZ) spr1781(murA)
            SPD: SPD_0967(murA-1) SPD_1764(murA-2)
            SAG: SAG0843(murA-1) SAG0866(murA-2)
            SAN: gbs0861 gbs0883(murA)
            SAK: SAK_0966(murA) SAK_0989(murA)
            SMU: SMU.1525(murA) SMU.1572(murZ)
            STC: str1167(murA) str1560(murZ)
            STL: stu1167(murA) stu1560(murZ)
            STE: STER_1519
            SSA: SSA_0791(murA) SSA_1494(murZ)
            SSU: SSU05_1619
            SSV: SSU98_1630
            SGO: SGO_0763(murA-1) SGO_1400(murA-2)
            LPL: lp_0510(murA1) lp_2361(murA2)
            LJO: LJ0225
            LAC: LBA0234
            LSA: LSA1123(murA1) LSA1628(murA2)
            LSL: LSL_0345(murA) LSL_0603(murA)
            LDB: Ldb0355(murA)
            LBU: LBUL_0310
            LBR: LVIS_0494 LVIS_1276
            LCA: LSEI_2570
            LGA: LGAS_0227
            PPE: PEPE_1570
            EFA: EF1169(murAB) EF2605(murAA)
            OOE: OEOE_1785
            LME: LEUM_0449
            STH: STH1212 STH2915 STH3304
            CAC: CAC2862(murA) CAC3539(murA)
            CPE: CPE2184(murA) CPE2606(murA)
            CPF: CPF_2449(murA) CPF_2933(murA)
            CPR: CPR_2159(murA) CPR_2616(murA)
            CTC: CTC00169 CTC00314
            CNO: NT01CX_0527(murA) NT01CX_0948(murA)
            CTH: Cthe_0441 Cthe_0973 Cthe_2328 Cthe_2615
            CDF: CD0123(murA)
            CBO: CBO0159(murA) CBO3566(murA)
            CBA: CLB_3647(murA)
            CBH: CLC_0207(murA-1) CLC_3545(murA-2)
            CBF: CLI_0214(murA-1) CLI_3787(murA-2)
            CKL: CKL_0127(murA1) CKL_3685(murA2)
            CHY: CHY_2066(murAB) CHY_2542(murA)
            DSY: DSY2905 DSY4909
            DRM: Dred_3148
            PTH: PTH_2858(murA)
            SWO: Swol_0828 Swol_2377 Swol_2469
            CSC: Csac_1198
            TTE: TTE0158(murA) TTE2684(murA3)
            MTA: Moth_0846 Moth_2375
            MTU: Rv1315(murA)
            MTC: MT1355(murA)
            MBO: Mb1348(murA)
            MBB: BCG_1376(murA)
            MLE: ML1150(murA)
            MPA: MAP2447c(murA)
            MAV: MAV_1531(murA)
            MSM: MSMEG_4932(murA)
            MMC: Mmcs_3872
            CGL: NCgl0345(cgl0352) NCgl2470(cgl2558)
            CGB: cg0422(murA) cg2829(murA2)
            CEF: CE2443
            CDI: DIP1887(murA)
            CJK: jk0398(murA)
            NFA: nfa10690(murA)
            RHA: RHA1_ro01468
            SCO: SCO2949(murA) SCO5998(murA2)
            SMA: SAV2260(murA1) SAV5128(murA2)
            TWH: TWT508(murA)
            TWS: TW254(murA)
            LXX: Lxx09670(murA)
            CMI: CMM_1343(murA)
            AAU: AAur_2484(murA)
            PAC: PPA1226
            TFU: Tfu_3016
            FRA: Francci3_3613 Francci3_3700
            FAL: FRAAL5820(murA) FRAAL5925(murA)
            ACE: Acel_0368 Acel_0657
            SEN: SACE_6270(murA)
            BLO: BL1267(murA)
            BAD: BAD_0183(murA)
            RXY: Rxyl_1636
            FNU: FN1520
            CTR: CT455(murA)
            CTA: CTA_0497(murA)
            CMU: TC0740
            CPN: CPn0571(murA)
            CPA: CP0178
            CPJ: CPj0571(murA)
            CPT: CpB0592
            CCA: CCA00171(murA)
            CAB: CAB168
            CFE: CF0836(murA)
            PCU: pc0229(murA)
            BGA: BG0484(murA)
            BAF: BAPKO_0501(murA)
            TPA: TP0029
            TDE: TDE0641(murA)
            LIL: LA4079(murA)
            LIC: LIC13251(murA)
            LBJ: LBJ_0205(murA)
            LBL: LBL_2877(murA)
            SYN: slr0017(murA)
            SYW: SYNW1633(murA)
            SYC: syc0815_c(murZ)
            SYF: Synpcc7942_0715
            SYD: Syncc9605_0866
            SYE: Syncc9902_1533
            SYG: sync_0746(murA)
            SYR: SynRCC307_0612(murA)
            SYX: SynWH7803_1746(murA)
            CYA: CYA_1988(murA)
            CYB: CYB_0095(murA)
            TEL: tll0780(murZ)
            GVI: glr3125
            ANA: all0174
            AVA: Ava_1435
            PMA: Pro1374(murA) Pro1539(murA)
            PMM: PMM1300(murA)
            PMT: PMT0332(murA)
            PMN: PMN2A_0866
            PMI: PMT9312_1396
            PMB: A9601_14991(murA)
            PMC: P9515_14611(murA)
            PMG: P9301_14851(murA)
            PMH: P9215_15281
            PME: NATL1_17201(murA)
            TER: Tery_3177
            BTH: BT_2005
            BFR: BF3702
            BFS: BF3495
            PGI: PG1366(murA)
            SRU: SRU_1859(murA)
            CHU: CHU_1552(murA)
            GFO: GFO_1448(murA)
            FPS: FP2014(murA)
            CTE: CT0555(murA)
            CCH: Cag_1282
            PLT: Plut_0561
            DRA: DR_1123
            DGE: Dgeo_1386
            TTH: TTC1854
            TTJ: TTHA0140
            AAE: aq_1281(murA)
            TMA: TM0108
            MBA: Mbar_A0022
STRUCTURES  PDB: 1A2N  1DLG  1EJC  1EJD  1EYN  1NAW  1Q3G  1RYW  1UAE  1YBG  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.7
            ExPASy - ENZYME nomenclature database: 2.5.1.7
            ExplorEnz - The Enzyme Database: 2.5.1.7
            ERGO genome analysis and discovery system: 2.5.1.7
            BRENDA, the Enzyme Database: 2.5.1.7
            CAS: 9023-27-2
///
ENTRY       EC 2.5.1.8                  Enzyme
NAME        tRNA isopentenyltransferase;
            transfer ribonucleate isopentenyltransferase;
            Delta2-isopentenyl pyrophosphate:tRNA-Delta2-isopentenyl
            transferase;
            Delta2-isopentenyl pyrophosphate:transfer ribonucleic acid
            Delta2-isopentenyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     isopentenyl-diphosphate:tRNA isopentenyltransferase
REACTION    isopentenyl diphosphate + tRNA = diphosphate + tRNA containing
            6-isopentenyladenosine [RN:R01122]
ALL_REAC    R01122
SUBSTRATE   isopentenyl diphosphate [CPD:C00129];
            tRNA [CPD:C00066]
PRODUCT     diphosphate [CPD:C00013];
            tRNA containing 6-isopentenyladenosine [CPD:C04432]
REFERENCE   1  [PMID:4311031]
  AUTHORS   Kline LK, Fittler F, Hall RH.
  TITLE     N6-(delta-2-isopentenyl) adenosine. Biosynthesis in transfer
            ribonucleic acid in vitro.
  JOURNAL   Biochemistry. 8 (1969) 4361-71.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4341485]
  AUTHORS   Rosenbaum N, Gefter ML.
  TITLE     Delta 2 -isopentenylpyrophosphate: transfer ribonucleic acid   2
            -isopentenyltransferase from Escherichia coli. Purification and
            properties of the enzyme.
  JOURNAL   J. Biol. Chem. 247 (1972) 5675-80.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K00791  tRNA delta(2)-isopentenylpyrophosphate transferase
GENES       HSA: 54802(TRIT1)
            MMU: 66966(Trit1)
            CFA: 475320(TRIT1)
            XTR: 496761(trit1)
            DME: Dmel_CG31381
            CEL: ZC395.6(gro-1)
            ATH: AT2G27760(ATIPT2)
            OSA: 4323831
            SCE: YOR274W(MOD5)
            AGO: AGOS_AER341W
            PIC: PICST_40644
            CGR: CAGL0L10934g
            SPO: SPAC343.15
            ANI: AN6513.2
            AFM: AFUA_6G05070
            AOR: AO090701000031
            CNE: CNA03460
            DDI: DDBDRAFT_0183953 DDBDRAFT_0217421
            PFA: PFL0380c
            CHO: Chro.60293
            TAN: TA20750
            TPV: TP01_0445
            TET: TTHERM_00255600
            TBR: Tb927.3.4900
            TCR: 507951.250
            EHI: 23.t00020
            ECO: b4171(miaA)
            ECJ: JW4129(miaA)
            ECE: Z5778(miaA)
            ECS: ECs5147
            ECC: c5255(miaA)
            ECI: UTI89_C4771(miaA)
            ECP: ECP_4416
            ECV: APECO1_2220(miaA)
            ECW: EcE24377A_4729(miaA)
            ECX: EcHS_A4413
            STY: STY4717(miaA)
            STT: t4411(miaA)
            SPT: SPA4177(miaA)
            SEC: SC4236(miaA)
            STM: STM4360(miaA)
            YPE: YPO0372(miaA)
            YPK: y0629(miaA)
            YPM: YP_0528(miaA)
            YPA: YPA_3912
            YPN: YPN_3299
            YPP: YPDSF_3602
            YPS: YPTB0424(miaA)
            YPI: YpsIP31758_3654(miaA)
            YEN: YE0376(b4171)
            SFL: SF4326(miaA)
            SFX: S4594(miaA)
            SFV: SFV_4329(miaA)
            SSN: SSON_4356(miaA)
            SBO: SBO_4285(miaA)
            SDY: SDY_4418(miaA)
            ECA: ECA3935(miaA)
            PLU: plu4582(miaA)
            BUC: BU569(miaA)
            BAB: bbp514(miaA)
            BCC: BCc_371(miaA)
            WBR: WGLp183(miaA)
            SGL: SG0336
            ENT: Ent638_0354
            KPN: KPN_04569(miaA)
            SPE: Spro_0430
            BFL: Bfl079(miaA)
            BPN: BPEN_081(miaA)
            HIN: HI0068(trpX)
            HIT: NTHI0081(miaA)
            HIP: CGSHiEE_02955(miaA)
            HDU: HD0742(miaA)
            HSO: HS_1084(miaA)
            PMU: PM0905(trpX)
            MSU: MS1517(miaA)
            APL: APL_1960(miaA)
            ASU: Asuc_0988
            XFA: XF0090
            XFT: PD0067(miaA)
            XCC: XCC1715(miaA)
            XCB: XC_2516
            XCV: XCV1767(miaA)
            XAC: XAC1734(miaA)
            XOO: XOO2947(miaA)
            XOM: XOO_2799(XOO2799)
            VCH: VC0346
            VCO: VC0395_A2757(miaA)
            VVU: VV1_1293
            VVY: VV3072
            VPA: VP2818
            VFI: VF2324
            PPR: PBPRA3351
            PAE: PA4945(miaA)
            PAU: PA14_65320(miaA)
            PAP: PSPA7_5674(miaA)
            PPU: PP_4895(miaA)
            PPF: Pput_4771
            PST: PSPTO_4943(miaA)
            PSB: Psyr_0571(miaA)
            PSP: PSPPH_0564(miaA)
            PFL: PFL_0565(miaA)
            PFO: Pfl_0522
            PEN: PSEEN4944(miaA)
            PMY: Pmen_0634
            PAR: Psyc_0920(miaA)
            PCR: Pcryo_1494
            PRW: PsycPRwf_0820
            ACI: ACIAD2374(miaA)
            SON: SO_0602(miaA)
            SDN: Sden_3206
            SFR: Sfri_3312
            SAZ: Sama_3026
            SBL: Sbal_0557
            SBM: Shew185_3768
            SLO: Shew_0565
            SPC: Sputcn32_3281
            SSE: Ssed_0796 Ssed_3611
            SPL: Spea_3541
            SHE: Shewmr4_0597
            SHM: Shewmr7_3433
            SHN: Shewana3_0596
            SHW: Sputw3181_0660
            ILO: IL0332(miaA)
            CPS: CPS_0324(miaA)
            PHA: PSHAa0270(miaA)
            PAT: Patl_3977
            SDE: Sde_2668
            PIN: Ping_3239
            MAQ: Maqu_2770
            CBU: CBU_1082(miaA)
            CBD: COXBU7E912_1185(miaA)
            LPN: lpg2696(miaA)
            LPF: lpl2624(miaA)
            LPP: lpp2751(miaA)
            MCA: MCA1691(miaA)
            FTU: FTT0629(miaA)
            FTF: FTF0629(miaA)
            FTW: FTW_1100(miaA)
            FTL: FTL_0897
            FTH: FTH_0882(miaA)
            FTA: FTA_0948(miaA)
            FTN: FTN_1052(miaA)
            TCX: Tcr_1085
            NOC: Noc_2591
            AEH: Mlg_0572
            HHA: Hhal_0667
            HCH: HCH_02227(miaA1) HCH_05384(miaA2)
            CSA: Csal_1276
            ABO: ABO_2204(miaA)
            MMW: Mmwyl1_2633
            AHA: AHA_0923(miaA)
            DNO: DNO_1117(miaA)
            BCI: BCI_0583(miaA)
            RMA: Rmag_0765
            VOK: COSY_0703(miaA)
            NME: NMB0935
            NMA: NMA1130(miaA)
            NMC: NMC0912(miaA)
            NGO: NGO0940
            CVI: CV_3389(miaA)
            RSO: RSc2564(miaA)
            REU: Reut_A2770
            REH: H16_A3070(miaA)
            RME: Rmet_2909
            BMA: BMA2315(miaA)
            BMV: BMASAVP1_A0513(miaA)
            BML: BMA10299_A1086(miaA)
            BMN: BMA10247_2193(miaA)
            BXE: Bxe_A3935
            BVI: Bcep1808_0723
            BUR: Bcep18194_A3852
            BCN: Bcen_0280
            BCH: Bcen2424_0764
            BAM: Bamb_0659
            BPS: BPSL2815(miaA)
            BPM: BURPS1710b_3309(miaA)
            BPL: BURPS1106A_3298(miaA)
            BPD: BURPS668_3265(miaA)
            BTE: BTH_I1319(miaA)
            PNU: Pnuc_1760
            BPE: BP0243(miaA)
            BPA: BPP3624(miaA)
            BBR: BB4059(miaA)
            RFR: Rfer_1535
            POL: Bpro_3212
            PNA: Pnap_1155
            AAV: Aave_1294
            AJS: Ajs_3111
            VEI: Veis_4227
            MPT: Mpe_A2034
            HAR: HEAR0405(miaA)
            MMS: mma_0461
            NEU: NE1976(miaA)
            NET: Neut_0386
            NMU: Nmul_A0092
            EBA: ebA7097(miaA)
            AZO: azo3131(miaA)
            DAR: Daro_3171
            TBD: Tbd_1512
            MFA: Mfla_1385
            HPY: HP1415
            HPJ: jhp1310(miaA)
            HPA: HPAG1_1341
            HHE: HH0910(miaA)
            HAC: Hac_0022(miaA)
            WSU: WS1976(miaA)
            TDN: Tmden_1812
            CJE: Cj0166(miaA)
            CJR: CJE0161(miaA)
            CJJ: CJJ81176_0201(miaA)
            CJU: C8J_0162(miaA)
            CJD: JJD26997_0181(miaA)
            CFF: CFF8240_0216(miaA)
            CCV: CCV52592_0816(miaA)
            CHA: CHAB381_1775(miaA)
            CCO: CCC13826_1161(miaA)
            ABU: Abu_0152(miaA)
            NIS: NIS_0303(miaA)
            SUN: SUN_2217(miaA)
            GSU: GSU2000(miaA)
            GME: Gmet_2052
            GUR: Gura_1499 Gura_1771
            PCA: Pcar_1305 Pcar_3100
            PPD: Ppro_2963 Ppro_3245
            DVU: DVU1533(miaA)
            DVL: Dvul_1598
            DDE: Dde_1784
            LIP: LI0281(miaA)
            BBA: Bd1565(miaA)
            DPS: DP1930(trpX)
            ADE: Adeh_1512
            AFW: Anae109_2312
            MXA: MXAN_3731(miaA)
            SAT: SYN_01969 SYN_02888
            SFU: Sfum_1920
            RPR: RP510(miaA)
            RTY: RT0495(miaA)
            RCO: RC0656(miaA)
            RFE: RF_0714(miaA)
            RBE: RBE_0779(miaA)
            RAK: A1C_03530(miaA)
            RBO: A1I_05010(miaA)
            RCM: A1E_02960(miaA)
            RRI: A1G_03725(miaA)
            OTS: OTBS_0858(miaA)
            WOL: WD0822(miaA)
            WBM: Wbm0636
            AMA: AM755(miaA)
            APH: APH_0431(miaA)
            ERU: Erum4370(miaA)
            ERW: ERWE_CDS_04560(miaA)
            ERG: ERGA_CDS_04490(miaA)
            ECN: Ecaj_0457
            ECH: ECH_0588(miaA)
            NSE: NSE_0570(miaA)
            PUB: SAR11_0004(miaA)
            MLO: mll1448
            MES: Meso_1743
            PLA: Plav_2463
            SME: SMc01435(miaA)
            SMD: Smed_2011
            ATU: Atu2039(miaA)
            ATC: AGR_C_3695(ippT)
            RET: RHE_CH02793(miaA)
            RLE: RL3249(miaA)
            BME: BMEI0616
            BMF: BAB1_1409
            BMS: BR1390(miaA)
            BMB: BruAb1_1386(miaA)
            BOV: BOV_1347(miaA)
            OAN: Oant_1801
            BJA: bll6504
            BRA: BRADO5567(miaA)
            BBT: BBta_6088(miaA)
            RPA: RPA2030(miaA)
            RPB: RPB_3346
            RPC: RPC_3256
            RPD: RPD_2097
            RPE: RPE_2186
            NWI: Nwi_2344
            NHA: Nham_2723
            BHE: BH10930(miaA)
            BQU: BQ08580(miaA)
            XAU: Xaut_1659
            CCR: CC_2098
            SIL: SPO1661(miaA)
            SIT: TM1040_1415
            RSP: RSP_2704(miaA)
            RSH: Rsph17029_1361
            RSQ: Rsph17025_2154
            JAN: Jann_2461
            RDE: RD1_2584(miaA)
            PDE: Pden_3992
            MMR: Mmar10_2021
            HNE: HNE_0452(miaA)
            ZMO: ZMO1138(miaA)
            NAR: Saro_2260
            SAL: Sala_1469
            SWI: Swit_0608
            ELI: ELI_05520
            GOX: GOX1086
            GBE: GbCGDNIH1_1482
            ACR: Acry_2834
            RRU: Rru_A0466
            MAG: amb3506
            MGM: Mmc1_0276
            ABA: Acid345_4559
            SUS: Acid_1297
            BSU: BG12617(miaA)
            BHA: BH2366(miaA)
            BAN: BA3843(miaA)
            BAR: GBAA3843(miaA)
            BAA: BA_4316
            BAT: BAS3560
            BCE: BC3714
            BCA: BCE_3741(miaA)
            BCZ: BCZK3473(miaA)
            BCY: Bcer98_2391
            BTK: BT9727_3459(miaA)
            BLI: BL05174(miaA)
            BLD: BLi01961(miaA)
            BCL: ABC2184(miaA)
            BAY: RBAM_017130
            BPU: BPUM_1624
            OIH: OB1634(miaA)
            GKA: GK1312
            SAU: SA1144(miaA)
            SAV: SAV1304(miaA)
            SAM: MW1186(miaA)
            SAR: SAR1278(miaA)
            SAS: SAS1236
            SAC: SACOL1323(miaA)
            SAB: SAB1164
            SAA: SAUSA300_1195(miaA)
            SAO: SAOUHSC_01280
            SAJ: SaurJH9_1362
            SAH: SaurJH1_1388
            SEP: SE0981
            SER: SERP0870(miaA)
            SHA: SH1606(miaA)
            SSP: SSP1457
            LMO: lmo1294(miaA)
            LMF: LMOf2365_1311(miaA)
            LIN: lin1332(miaA)
            LWE: lwe1309(miaA)
            LLA: L15012(miaA)
            LLC: LACR_0647
            LLM: llmg_0591(miaA)
            SPY: SPy_0921(miaA)
            SPZ: M5005_Spy_0722(miaA)
            SPM: spyM18_0978(miaA)
            SPG: SpyM3_0634(miaA)
            SPS: SPs1218
            SPH: MGAS10270_Spy0781(miaA)
            SPI: MGAS10750_Spy0816(miaA)
            SPJ: MGAS2096_Spy0794(miaA)
            SPK: MGAS9429_Spy0779(miaA)
            SPF: SpyM51085(miaA)
            SPA: M6_Spy0748
            SPB: M28_Spy0702(miaA)
            SPN: SP_0671
            SPR: spr0588(miaA)
            SPD: SPD_0583(miaA)
            SAG: SAG1213(miaA)
            SAN: gbs1285
            SAK: SAK_1299(miaA)
            SMU: SMU.1477(miaA)
            STL: stu1177(miaA)
            SSA: SSA_1433(miaA)
            SGO: SGO_0992(miaA)
            LPL: lp_1579(miaA)
            LJO: LJ1615
            LAC: LBA1503(miaA)
            LSA: LSA1326(miaA)
            LSL: LSL_0555(miaA)
            LDB: Ldb1476(miaA)
            LBU: LBUL_1371
            LBR: LVIS_0992
            LCA: LSEI_1656
            LRE: Lreu_1203
            EFA: EF2162(miaA)
            OOE: OEOE_0950
            STH: STH1747
            CAC: CAC1835(miaA)
            CPE: CPE1157(miaA)
            CPF: CPF_1360(miaA)
            CPR: CPR_1173(miaA)
            CTC: CTC01300(miaA)
            CNO: NT01CX_2107(miaA)
            CTH: Cthe_0775
            CDF: CD1975(miaA)
            CBO: CBO1798(miaA)
            CBA: CLB_1733(miaA)
            CBH: CLC_1740(miaA)
            CBF: CLI_1793(miaA)
            CBE: Cbei_2564
            CKL: CKL_1576(miaA)
            AMT: Amet_2542
            CHY: CHY_1394(miaA)
            DSY: DSY1587
            DRM: Dred_1882
            SWO: Swol_0979
            CSC: Csac_2045
            TTE: TTE1359(miaA)
            MTA: Moth_1115
            MPE: MYPE5020(miaA)
            MGA: MGA_0914(miaA)
            POY: PAM275(miaA)
            AYW: AYWB_446(miaA)
            MTU: Rv2727c(miaA)
            MTC: MT2799(miaA)
            MBO: Mb2746c(miaA)
            MBB: BCG_2740c(miaA)
            MLE: ML0995(miaA)
            MPA: MAP2841c(miaA)
            MAV: MAV_3620(miaA)
            MSM: MSMEG_2734(miaA)
            MVA: Mvan_2434
            MGI: Mflv_3962
            MMC: Mmcs_2162
            MKM: Mkms_2208
            MJL: Mjls_2149
            CGL: NCgl1869(cgl1944)
            CGB: cg2130(miaA)
            CEF: CE1838
            CDI: DIP1443(miaA)
            CJK: jk1111(miaA)
            NFA: nfa38310(miaA)
            RHA: RHA1_ro06775
            SCO: SCO5791(miaA)
            SMA: SAV2475(miaA)
            TWH: TWT609(miaA)
            TWS: TW626(miaA)
            LXX: Lxx15980(miaA)
            ART: Arth_1463
            AAU: AAur_1597(miaA)
            PAC: PPA1019
            NCA: Noca_3843
            TFU: Tfu_0815
            FRA: Francci3_3516
            FAL: FRAAL5709(miaA)
            ACE: Acel_1484
            KRA: Krad_1500
            SEN: SACE_1752(miaA)
            STP: Strop_1445
            BLO: BL1409(miaA)
            BAD: BAD_1031(miaA)
            FNU: FN1917
            RBA: RB1507(miaA)
            CTR: CT766(miaA)
            CTA: CTA_0836(miaA)
            CMU: TC0147
            CPN: CPn0910(miaA)
            CPA: CP0956
            CPJ: CPj0910(miaA)
            CPT: CpB0943
            CCA: CCA00858(miaA)
            CAB: CAB823
            CFE: CF0158(miaA)
            PCU: pc1243(miaA)
            BGA: BG0846(miaA)
            BAF: BAPKO_0874(miaA)
            TPA: TP0637
            TDE: TDE0057(miaA-1) TDE1447(miaA-2)
            LIL: LA1516(miaA)
            LIC: LIC12246(miaA)
            LBJ: LBJ_1703(miaA)
            LBL: LBL_1922(miaA)
            SYN: sll0817(miaA)
            SYW: SYNW0094(miaA)
            SYC: syc1616_d(miaA)
            SYF: Synpcc7942_2490
            SYD: Syncc9605_0086
            SYE: Syncc9902_0132
            SYG: sync_0091(miaA)
            SYR: SynRCC307_0091(miaA)
            SYX: SynWH7803_0146(miaA)
            CYA: CYA_0081(miaA)
            CYB: CYB_2044(miaA)
            TEL: tlr0648
            GVI: gll3248
            ANA: alr5266
            AVA: Ava_2518
            PMA: Pro1797(miaA)
            PMM: PMM1635(miaA)
            PMT: PMT0120(miaA)
            PMN: PMN2A_1214
            PMI: PMT9312_1728
            PMB: A9601_18451(miaA)
            PMC: P9515_18241(miaA)
            PMF: P9303_01561(miaA)
            PMG: P9301_18261(miaA)
            PMH: P9215_19091
            PME: NATL1_20891(miaA)
            TER: Tery_3962
            BTH: BT_4203 BT_4323
            BFR: BF0903 BF1021
            BFS: BF0825(miaA) BF0938
            PGI: PG0335(miaA-1) PG0522(miaA-2)
            SRU: SRU_1498(miaA)
            CHU: CHU_2776(miaA)
            GFO: GFO_0660(miaA)
            FJO: Fjoh_3453
            FPS: FP1916(miaA)
            CTE: CT0973(miaA)
            CCH: Cag_1394
            CPH: Cpha266_1081
            PVI: Cvib_0776
            PLT: Plut_1180
            DET: DET0741(miaA)
            DEH: cbdb_A716(miaA)
            DEB: DehaBAV1_0671
            RRS: RoseRS_3334
            RCA: Rcas_4310
            DRA: DR_1690
            DGE: Dgeo_0860
            TTH: TTC0204
            TTJ: TTHA0572
            AAE: aq_1067(miaA)
            TMA: TM0525
            TPT: Tpet_0396
            TME: Tmel_1398
            FNO: Fnod_0276
STRUCTURES  PDB: 2QGN  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.8
            ExPASy - ENZYME nomenclature database: 2.5.1.8
            ExplorEnz - The Enzyme Database: 2.5.1.8
            ERGO genome analysis and discovery system: 2.5.1.8
            BRENDA, the Enzyme Database: 2.5.1.8
            CAS: 37277-78-4
///
ENTRY       EC 2.5.1.9                  Enzyme
NAME        riboflavin synthase;
            heavy riboflavin synthase;
            light riboflavin synthase;
            riboflavin synthetase;
            riboflavine synthase;
            riboflavine synthetase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     6,7-dimethyl-8-(1-D-ribityl)lumazine:6,7-dimethyl-8-(1-D-ribityl)lum
            azine 2,3-butanediyltransferase
REACTION    2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin +
            4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine [RN:R00066]
ALL_REAC    R00066
SUBSTRATE   6,7-dimethyl-8-(1-D-ribityl)lumazine [CPD:C04332]
PRODUCT     riboflavin [CPD:C00255];
            4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine [CPD:C04732]
COFACTOR    Riboflavin [CPD:C00255]
COMMENT     A flavoprotein (riboflavin).
REFERENCE   1
  AUTHORS   Plaut, G.W.E.
  TITLE     Studies on the nature of the enzymic conversion of
            6,7-dimethyl-8-ribityllumazine to riboflavin.
  JOURNAL   J. Biol. Chem. 238 (1963) 2225-2243.
  ORGANISM  Ashbya gossypii [GN:ago], Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Plaut, G.W.E. and Harvey, R.A.
  TITLE     Riboflavin synthetase.
  JOURNAL   Methods Enzymol. 18B (1971) 527-538.
  ORGANISM  Ashbya gossypii [GN:ago], Escherichia coli [GN:eco], Saccharomyces
            cerevisiae [GN:sce], Aerobacter aerogenes , Pseudomonas sp. ,
            Bacillus subtilis [GN:bsu], Neurospora crassa [GN:dncr],
            Lactobacillus casei , Lactobacillus plantarum [GN:lpl]
REFERENCE   3
  AUTHORS   Wacker, H., Harvey, R.A., Winestock, C.H. and Plaut, G.W.E.
  TITLE     4-(1'-D-Ribitylamino)-5-amino-2,6-dihydroxypyrimidine, the second
            product of the riboflavin synthetase reaction.
  JOURNAL   J. Biol. Chem. 239 (1964) 3493-3497.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00740  Riboflavin metabolism
ORTHOLOGY   KO: K00792  riboflavin synthase
            KO: K00793  riboflavin synthase alpha chain
GENES       ATH: AT2G20690 AT2G44050(COS1)
            OSA: 4336286 4352436
            CME: CML247C
            SCE: YBR256C(RIB5)
            AGO: AGOS_AGR241W
            PIC: PICST_40556(RIB5) PICST_51333(RIB4)
            CGR: CAGL0D05302g
            SPO: SPCC1450.13c
            ANI: AN4231.2
            AFM: AFUA_1G06240
            AOR: AO090001000426
            CNE: CNC06150
            ECO: b1662(ribC)
            ECJ: JW1654(ribC)
            ECE: Z2688(ribE)
            ECS: ECs2371
            ECC: c2056(ribE)
            ECI: UTI89_C1853(ribC)
            ECP: ECP_1609
            ECV: APECO1_742(ribE)
            ECW: EcE24377A_1876(ribE)
            ECX: EcHS_A1742(ribE)
            STY: STY1696(ribE)
            STT: t1294(ribE)
            SPT: SPA1427(ribE)
            SEC: SC1445(ribE)
            STM: STM1426(ribE)
            YPE: YPO2391(ribE)
            YPK: y1946(ribE)
            YPM: YP_2177(ribE)
            YPA: YPA_1736
            YPN: YPN_1845
            YPP: YPDSF_2817
            YPS: YPTB2304(ribE)
            YPI: YpsIP31758_1751(ribE)
            SFL: SF1690(ribC)
            SFX: S1822(ribE)
            SFV: SFV_1684(ribE)
            SSN: SSON_1494(ribE)
            SBO: SBO_1469(ribE)
            SDY: SDY_1888(ribE)
            ECA: ECA1923
            PLU: plu2610(ribE)
            BUC: BU112(ribE)
            BAS: BUsg104(ribE)
            BAB: bbp107(ribE)
            WBR: WGLp333(ribE)
            SGL: SG1439
            ENT: Ent638_0883
            SPE: Spro_1073
            BFL: Bfl366(ribE)
            BPN: BPEN_377(ribE)
            HIN: HI1613(ribE)
            HIT: NTHI1429(ribE)
            HIP: CGSHiEE_05740
            HIQ: CGSHiGG_10055
            HDU: HD1162(ribE)
            HSO: HS_0812(ribE)
            PMU: PM0650(ribE)
            MSU: MS1313(ribC)
            APL: APL_0383(ribE)
            ASU: Asuc_1488
            XFA: XF0952
            XFT: PD1746(ribC)
            XCC: XCC0695(ribE)
            XCB: XC_3539
            XCV: XCV0800(ribE)
            XAC: XAC0748(ribE)
            XOO: XOO3854(ribE)
            XOM: XOO_3633(XOO3633)
            VCH: VC2270
            VCO: VC0395_A1860(ribE)
            VVU: VV1_0322 VV1_2560
            VVY: VV0862 VV1729
            VPA: VP0680 VP1480
            VFI: VF0701 VF1414
            PPR: PBPRA0798 PBPRA2176(ribE)
            PAE: PA4055(ribC)
            PAU: PA14_11410(ribC)
            PAP: PSPA7_1046(ribE)
            PPU: PP_0515(ribE-1) PP_2916(ribE-2)
            PPF: Pput_0552
            PST: PSPTO_0691(ribE)
            PSB: Psyr_4461
            PSP: PSPPH_4506(ribE)
            PFL: PFL_5521(ribE)
            PFO: Pfl_5018
            PEN: PSEEN0589(ribC) PSEEN0591(ribH)
            PMY: Pmen_3854
            PAR: Psyc_2140(ribE)
            PCR: Pcryo_2469
            PRW: PsycPRwf_2285
            ACI: ACIAD0249(ribC)
            SON: SO_2296(ribE-1) SO_3468(ribE-2)
            SDN: Sden_1145 Sden_1703
            SFR: Sfri_1036 Sfri_2030
            SAZ: Sama_1019
            SBM: Shew185_3155
            SSE: Ssed_1276
            SPL: Spea_1165
            SHE: Shewmr4_1097 Shewmr4_1952
            SHM: Shewmr7_1163 Shewmr7_2024
            SHN: Shewana3_1097 Shewana3_2040
            ILO: IL1402(ribC)
            CPS: CPS_0731(ribE1)
            PHA: PSHAa1734(ribC) PSHAa2373(ribE)
            PAT: Patl_1312
            PIN: Ping_1441
            MAQ: Maqu_0845
            CBU: CBU_0646(ribE)
            CBD: COXBU7E912_0657(ribE)
            LPN: lpg1178(ribE)
            LPF: lpl1187(ribE)
            LPP: lpp1181(ribE)
            MCA: MCA1657(ribE-1) MCA1865(ribE-2)
            FTU: FTT1672(ribB)
            FTF: FTF1672(ribB)
            FTW: FTW_1945(ribE)
            FTL: FTL_0077
            FTH: FTH_0073(ribB)
            FTA: FTA_0085(ribE)
            FTN: FTN_0113(ribC)
            TCX: Tcr_1399
            NOC: Noc_2024
            AEH: Mlg_0376 Mlg_0378
            HHA: Hhal_0897
            HCH: HCH_02673(ribE1) HCH_05956(ribE2)
            CSA: Csal_2099
            ABO: ABO_2173(ribE)
            AHA: AHA_2116(ribE-1) AHA_3332(ribE-3)
            DNO: DNO_0471(ribH) DNO_0473(ribE)
            BCI: BCI_0087(ribE)
            RMA: Rmag_0506
            VOK: COSY_0462 COSY_0464(ribH)
            NME: NMB1247
            NMA: NMA1416(ribC)
            NMC: NMC0635(ribE) NMC1148(ribC)
            NGO: NGO0755
            CVI: CV_2387(ribE) CV_4217
            RSO: RSc0714(ribE)
            REU: Reut_A0775
            REH: H16_A2849(ribC) H16_A2855(ribH)
            RME: Rmet_2689
            BMA: BMA2144(ribE)
            BMV: BMASAVP1_A0766(ribE)
            BML: BMA10299_A2599(ribE)
            BMN: BMA10247_2014(ribE)
            BXE: Bxe_A0894
            BVI: Bcep1808_0873
            BUR: Bcep18194_A4063 Bcep18194_B2300
            BCN: Bcen_0480 Bcen_4568
            BCH: Bcen2424_0956 Bcen2424_0959 Bcen2424_3795
            BAM: Bamb_0817 Bamb_0820
            BPS: BPSL2625(ribE)
            BPM: BURPS1710b_3101(ribE)
            BPL: BURPS1106A_3066(ribE)
            BPD: BURPS668_3013(ribE)
            BTE: BTH_I1541(ribE)
            PNU: Pnuc_0265
            BPE: BP2874(ribE)
            BPA: BPP0955(ribE)
            BBR: BB1167(ribE)
            RFR: Rfer_2667
            POL: Bpro_2884
            PNA: Pnap_2918
            AAV: Aave_2231
            AJS: Ajs_2767
            VEI: Veis_4792
            MPT: Mpe_A2946 Mpe_A2948
            HAR: HEAR1037(ribE) HEAR2090(ribH)
            MMS: mma_1345(ribH1) mma_2339(ribH2) mma_2433(ribE)
            NEU: NE2555
            NET: Neut_2515 Neut_2517
            NMU: Nmul_A0009
            EBA: ebA3569(ribE)
            AZO: azo0318(ribH) azo0320(ribE)
            DAR: Daro_4095
            TBD: Tbd_2189
            MFA: Mfla_2097
            HPY: HP1574(ribC)
            HPJ: jhp1482(ribC)
            HPA: HPAG1_0002 HPAG1_1523
            HHE: HH1321(ribC)
            HAC: Hac_1681(ribC)
            WSU: WS2075(ribA)
            TDN: Tmden_1930
            CJE: Cj1218c(ribA)
            CJR: CJE1353(ribE)
            CJJ: CJJ81176_1231(ribE)
            CJU: C8J_1161(ribE)
            CJD: JJD26997_0512(ribE)
            CFF: CFF8240_1445(ribE)
            CCV: CCV52592_1908(ribE)
            CHA: CHAB381_0712(ribE)
            CCO: CCC13826_0555(ribE) CCC13826_0661
            ABU: Abu_1846(ribH) Abu_2211(ribE)
            NIS: NIS_1361(ribE) NIS_1588
            SUN: SUN_0205 SUN_1919(ribE)
            GSU: GSU1689(ribE)
            GME: Gmet_1625
            GUR: Gura_2180
            PCA: Pcar_1446
            PPD: Ppro_1595
            DVU: DVU1200(ribE)
            DVL: Dvul_1859
            DDE: Dde_2435
            LIP: LI0156(ribE)
            BBA: Bd3039(ribB)
            DPS: DP1099
            ADE: Adeh_2741
            AFW: Anae109_2728
            MXA: MXAN_4763(ribE)
            SAT: SYN_02370
            SFU: Sfum_1379 Sfum_1381
            WOL: WD0130(ribE)
            WBM: Wbm0083
            AMA: AM120(ribA)
            APH: APH_0106(ribE)
            ERU: Erum7390(ribE)
            ERW: ERWE_CDS_07790(ribE)
            ERG: ERGA_CDS_07700(ribE)
            ECN: Ecaj_0773
            ECH: ECH_0239(ribE-1)
            NSE: NSE_0853(ribE-2)
            PUB: SAR11_1045(ribB)
            MLO: mlr8407
            MES: Meso_1137
            SME: SMc01773(ribE)
            SMD: Smed_0821
            ATU: Atu1169(ribc)
            ATC: AGR_C_2161
            RET: RHE_CH01511(ribE)
            RLE: RL1622(ribC) RL1632(ribH) RL3153(ribH)
            BME: BMEI1188
            BMF: BAB1_0790
            BMS: BR0768(ribE)
            BMB: BruAb1_0784(ribE)
            BOV: BOV_0761(ribE) BOV_A0649(ribH-2)
            OAN: Oant_2526
            BJA: bll5030(ribE)
            BRA: BRADO4426(ribH) BRADO4427(ribC) BRADO6033
            BBT: BBta_1745 BBta_4645(ribH) BBta_4646(ribC)
            RPA: RPA2727(ribC)
            RPB: RPB_2637
            RPC: RPC_2662
            RPD: RPD_2674
            RPE: RPE_2811 RPE_2812
            NWI: Nwi_1724
            NHA: Nham_1817
            BHE: BH07570(ribE)
            BQU: BQ05420(ribE)
            BBK: BARBAKC583_0632(ribE)
            XAU: Xaut_4280
            CCR: CC_0886
            SIL: SPO1759(ribE)
            SIT: TM1040_2131
            RSP: RSP_0758
            JAN: Jann_3417
            RDE: RD1_0560(ribH) RD1_1800(ribE) RD1_1803(ribH)
            MMR: Mmar10_1532 Mmar10_1534
            HNE: HNE_2057(ribE)
            ZMO: ZMO0475(ribC)
            NAR: Saro_2858
            SAL: Sala_2990
            SWI: Swit_2446
            ELI: ELI_00145
            GOX: GOX0979
            GBE: GbCGDNIH1_1004 GbCGDNIH1_1006
            RRU: Rru_A1824
            MAG: amb2342 amb2343
            MGM: Mmc1_0165 Mmc1_0167
            ABA: Acid345_2883
            SUS: Acid_4223 Acid_6223
            BSU: BG10519(ribB)
            BHA: BH1555(ribB)
            BAN: BA4332(ribE)
            BAR: GBAA4332(ribE)
            BAA: BA_4790
            BAT: BAS4019
            BCE: BC4110
            BCA: BCE_4180(ribE)
            BCZ: BCZK3866(ribE)
            BCY: Bcer98_2811
            BTK: BT9727_3852(ribE)
            BTL: BALH_3726
            BLI: BL01890(ribE)
            BLD: BLi02474(ribE)
            BCL: ABC1811(ribB)
            BAY: RBAM_021390(ribH) RBAM_021410(ribE)
            BPU: BPUM_2059(ribH) BPUM_2061(ribE)
            OIH: OB3215
            GKA: GK2296
            GTN: GTNG_2224
            SAU: SA1588(ribB)
            SAV: SAV1770(ribB)
            SAM: MW1710(ribB)
            SAR: SAR1852(ribE)
            SAS: SAS1693
            SAC: SACOL1819(ribE)
            SAB: SAB1627c(ribE)
            SAA: SAUSA300_1714(ribE)
            SAO: SAOUHSC_01888
            SAJ: SaurJH9_1820
            SAH: SaurJH1_1855
            SEP: SE1440
            SER: SERP1327(ribE)
            SHA: SH1154(ribB)
            SSP: SSP0996
            LLA: L0164(ribB)
            LLC: LACR_1073
            LLM: llmg_1531(ribB)
            SPN: SP_0177
            SPR: spr0163(ribC)
            SPD: SPD_0168(ribE)
            SAG: SAG0747(ribE)
            SAN: gbs0768
            SAK: SAK_0873(ribE)
            LBR: LVIS_1652
            LRE: Lreu_0881
            CAC: CAC0591(ribB)
            CPE: CPE0567(risA)
            CPF: CPF_0547(ribE)
            CPR: CPR_0531(ribE)
            CTC: CTC00672
            CNO: NT01CX_0714(ribE)
            CTH: Cthe_0105 Cthe_0107
            CDF: CD1699(ribB)
            CBO: CBO2863(ribE) CBO2865(ribB)
            CBA: CLB_2831(ribE)
            CBH: CLC_2764(ribE)
            CBF: CLI_2921(ribE)
            CBE: Cbei_1227
            CKL: CKL_2166(ribH) CKL_2168(ribE)
            AMT: Amet_1021
            CHY: CHY_1474(ribE)
            DSY: DSY1663(ribE)
            DRM: Dred_2092
            PTH: PTH_1760(ribC)
            SWO: Swol_1219 Swol_1221
            CSC: Csac_0793
            MTA: Moth_0916
            MTU: Rv1412(ribC)
            MTC: MT1456(ribE)
            MBO: Mb1447(ribC)
            MBB: BCG_1473(ribC) BCG_1477(ribH)
            MLE: ML0558(ribC)
            MPA: MAP1139(ribC)
            MAV: MAV_3366(ribE)
            MSM: MSMEG_3071(ribE) MSMEG_3073(ribE)
            MVA: Mvan_2695
            MGI: Mflv_3718
            MMC: Mmcs_2389
            MKM: Mkms_2438
            MJL: Mjls_2432
            CGL: NCgl1534(cgl1596)
            CGB: cg1799(ribC)
            CEF: CE1715
            CDI: DIP1318(ribE)
            CJK: jk1009(ribC)
            NFA: nfa36010(ribE)
            RHA: RHA1_ro07169(ribE) RHA1_ro07171(ribH)
            SCO: SCO1443(SC6D7A.06c)
            SMA: SAV6902(ribC)
            TWH: TWT688(ribC)
            TWS: TW707(ribE)
            LXX: Lxx04360(ribC)
            CMI: CMM_0960(ribH)
            ART: Arth_1678
            AAU: AAur_1827(ribE) AAur_1829(ribH)
            PAC: PPA1751
            NCA: Noca_2450
            TFU: Tfu_1078
            FRA: Francci3_3187
            FAL: FRAAL5221(ribC)
            ACE: Acel_1271
            KRA: Krad_2977
            SEN: SACE_2122(ribC)
            RXY: Rxyl_1365
            FNU: FN1507
            RBA: RB12379(ribE)
            CTR: CT405(ribC)
            CTA: CTA_0440(ribC)
            CMU: TC0685
            CPN: CPn0532(ribC)
            CPA: CP0220
            CPJ: CPj0532(ribC)
            CPT: CpB0553
            CCA: CCA00213(ribE)
            CAB: CAB208(ribC)
            CFE: CF0794(ribC)
            PCU: pc0891(ribC)
            LIL: LA1145(ribE)
            LIC: LIC12535(risA)
            LBJ: LBJ_2151(ribC)
            LBL: LBL_2145(ribC)
            SYN: sll0300(ribC)
            SYW: SYNW1865(ribE)
            SYC: syc0082_c(ribC)
            SYF: Synpcc7942_1624
            SYD: Syncc9605_0604
            SYE: Syncc9902_1758
            SYG: sync_2122(ribE)
            SYR: SynRCC307_0080(ribH) SynRCC307_0667(ribE)
            SYX: SynWH7803_0088(ribH) SynWH7803_1876(ribE)
            CYA: CYA_2645(ribE)
            CYB: CYB_1738(ribE)
            TEL: tlr1686(ribC)
            GVI: glr3604(ribC)
            ANA: all5258
            AVA: Ava_1416
            PMA: Pro0438(ribC)
            PMM: PMM0442(ribE)
            PMT: PMT1346(ribE)
            PMN: PMN2A_1773
            PMI: PMT9312_0441
            PMB: A9601_04971(ribE) A9601_18521(ribH)
            PMC: P9515_05041(ribE) P9515_18331(ribH)
            PMF: P9303_00901(ribH) P9303_06371(ribE)
            PMG: P9301_04661(ribE) P9301_18331(ribH)
            PMH: P9215_05211(ribC)
            PME: NATL1_04961(ribE) NATL1_21111(ribH)
            TER: Tery_2569
            BTH: BT_1317
            BFR: BF2752
            BFS: BF2767(ribE)
            PGI: PG0733(ribE)
            SRU: SRU_2303(ribE)
            CHU: CHU_1926(ribE)
            GFO: GFO_0795(ribH) GFO_3338(ribE)
            FJO: Fjoh_0212 Fjoh_0650
            FPS: FP2003(ribH) FP2383(ribE)
            CTE: CT0756(ribE)
            CCH: Cag_0625
            CPH: Cpha266_2548
            PVI: Cvib_1632
            PLT: Plut_0731
            DET: DET1189(ribE)
            DEH: cbdb_A1104(ribE)
            DEB: DehaBAV1_0998
            RRS: RoseRS_0970
            DRA: DR_0154
            DGE: Dgeo_0301
            TTH: TTC0698
            TTJ: TTHA1063
            AAE: aq_1707(ribC)
            TMA: TM1827
            TPT: Tpet_1110
            TME: Tmel_0042
            FNO: Fnod_1418
            MLA: Mlab_0397
            HAL: VNG2624G(ribC)
            HMA: rrnAC2367(ribC)
            HWA: HQ1396A(ribC) HQ1633A(ribE)
            NPH: NP1356A(ribC)
            PFU: PF0061
            TKO: TK0425
            RCI: RRC56(ribC) RRC57(ribH)
            IHO: Igni_0936
            HBU: Hbut_0559 Hbut_0560
STRUCTURES  PDB: 1C2Y  1C41  1EJB  1EPS  1HQK  1HZE  1I18  1I8D  1KYV  1KYX  
                 1KYY  1KZ1  1KZ4  1KZ6  1KZ9  1KZL  1NQU  1NQV  1NQW  1NQX  
                 1PKV  1T13  1W19  1W29  1XN1  1ZIS  2A57  2A58  2A59  2B98  
                 2B99  2C92  2C94  2C97  2C9B  2C9D  2F59  2I0F  2JFB  2O6H  
                 2OBX  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.9
            ExPASy - ENZYME nomenclature database: 2.5.1.9
            ExplorEnz - The Enzyme Database: 2.5.1.9
            ERGO genome analysis and discovery system: 2.5.1.9
            BRENDA, the Enzyme Database: 2.5.1.9
            CAS: 9075-82-5
///
ENTRY       EC 2.5.1.10                 Enzyme
NAME        geranyltranstransferase;
            farnesyl-diphosphate synthase;
            geranyl transferase I;
            prenyltransferase;
            farnesyl pyrophosphate synthetase;
            farnesylpyrophosphate synthetase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     geranyl-diphosphate:isopentenyl-diphosphate geranyltranstransferase
REACTION    geranyl diphosphate + isopentenyl diphosphate = diphosphate +
            trans,trans-farnesyl diphosphate [RN:R02003]
ALL_REAC    R02003;
            (other) R01658
SUBSTRATE   geranyl diphosphate [CPD:C00341];
            isopentenyl diphosphate [CPD:C00129]
PRODUCT     diphosphate [CPD:C00013];
            trans,trans-farnesyl diphosphate [CPD:C00448]
COMMENT     Some forms of this enzyme will also use dimethylallyl diphosphate as
            a substrate. The enzyme will not accept larger prenyl diphosphates
            as efficient donors.
REFERENCE   1
  AUTHORS   Lynen, F., Agranoff, B.W., Eggerer, H., Henning, V. and Moslein,
            E.M.
  TITLE     Zur Biosynthese der Terpene. VI.
            gamma,gamma-Dimethyl-allyl-pyrophosphat und Geranyl-pyrophosphat,
            biologische Vorstufen des Squalens.
  JOURNAL   Angew. Chem. 71 (1959) 657-663.
  ORGANISM  pumpkin
REFERENCE   2  [PMID:4303505]
  AUTHORS   Ogura K, Nishino T, Seto S.
  TITLE     The purification of prenyltransferase and isopentenyl pyrophosphate
            isomerase of pumpkin fruit and their some properties.
  JOURNAL   J. Biochem. (Tokyo). 64 (1968) 197-203.
  ORGANISM  pumpkin, rat [GN:rno]
REFERENCE   3  [PMID:1109590]
  AUTHORS   Reed BC, Rilling HC.
  TITLE     Crystallization and partial characterization of prenyltransferase
            from avian liver.
  JOURNAL   Biochemistry. 14 (1975) 50-4.
  ORGANISM  chicken [GN:gga], pig [GN:ssc]
REFERENCE   4  [PMID:6792191]
  AUTHORS   Takahashi I, Ogura K.
  TITLE     Farnesyl pyrophosphate synthetase from Bacillus subtilis.
  JOURNAL   J. Biochem. (Tokyo). 89 (1981) 1581-7.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   5  [PMID:6818223]
  AUTHORS   Takahashi I, Ogura K.
  TITLE     Prenyltransferases of Bacillus subtilis: undecaprenyl pyrophosphate
            synthetase and geranylgeranyl pyrophosphate synthetase.
  JOURNAL   J. Biochem. (Tokyo). 92 (1982) 1527-37.
  ORGANISM  Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00100  Biosynthesis of steroids
            PATH: map00900  Terpenoid biosynthesis
ORTHOLOGY   KO: K00795  geranyltranstransferase
GENES       HSA: 2224(FDPS) 9453(GGPS1)
            MMU: 110196(Fdps) 14593(Ggps1)
            RNO: 83791(Fdps)
            CFA: 479198(GGPS1) 480129(FDPS)
            BTA: 281156(FDPS) 780882(GGPS1)
            GGA: 427092(GGPS1)
            XLA: 414582(MGC83119)
            DRE: 336798(ggps1)
            SPU: 576515(LOC576515)
            DME: Dmel_CG12389(Fpps) Dmel_CG8593(qm)
            CEL: R06C1.2
            ATH: AT2G18620 AT3G14530 AT3G14550(GGPS3) AT3G20160 AT3G29430
                 AT3G32040 AT5G47770(FPS1)
            OSA: 4323892 4324245 4343721
            CME: CMK058C CMM269C
            SCE: YJL167W(ERG20) YPL069C(BTS1)
            AGO: AGOS_AEL122W AGOS_AEL238C
            PIC: PICST_46658(BTS1) PICST_89338(ERG20)
            CAL: CaO19.6674(bts1)
            CGR: CAGL0H05269g CAGL0L00319g
            SPO: SPAC6F12.13c SPBC36.06c
            CNE: CNE04510 CNI00090
            UMA: UM04459.1
            ECU: ECU11_1810
            DDI: DDBDRAFT_0190001 DDBDRAFT_0206219 DDB_0215017(fps)
                 DDB_0233098
            PFA: PF11_0295
            CPV: cgd4_2550
            CHO: Chro.40285
            TBR: Tb927.7.3360
            TCR: 508323.9 511823.70
            LMA: LmjF22.1360
            ECO: b0421(ispA)
            ECJ: JW0411(ispA)
            ECE: Z0524(ispA)
            ECS: ECs0475
            ECC: c0532(ispA)
            ECI: UTI89_C0444(ispA)
            ECP: ECP_0480
            ECV: APECO1_1589(ispA)
            ECW: EcE24377A_0452(ispA)
            ECX: EcHS_A0492
            STY: STY0462(ispA)
            STT: t2440(ispA)
            SPT: SPA2300(ispA)
            SEC: SC0464(ispA)
            STM: STM0423(ispA)
            YPE: YPO3176(ispA)
            YPK: y1009(ispA)
            YPM: YP_0755(ispA)
            YPA: YPA_2670
            YPN: YPN_0912
            YPS: YPTB0940(ispA)
            YPI: YpsIP31758_3111(ispA)
            SFL: SF0358(ispA)
            SFX: S0366(ispA)
            SFV: SFV_0386(ispA)
            SSN: SSON_0398(ispA)
            SBO: SBO_0315(ispA)
            SDY: SDY_0309(ispA)
            ECA: ECA1132(ispA)
            PLU: plu3886(ispA)
            BUC: BU465(ispA)
            BAS: BUsg449(ispA)
            WBR: WGLp145(ispA)
            SGL: SG0657
            BPN: BPEN_245(ispA)
            HIT: NTHI1692(ispA)
            HDU: HD1322(ispA)
            HSO: HS_0904(ispA)
            PMU: PM0533(ispA)
            MSU: MS1060(ispA)
            APL: APL_0807(ispA)
            XFA: XF0661
            XFT: PD1512(ispA)
            XCC: XCC2600(ispA)
            XCB: XC_1516
            XCV: XCV2916(ispA)
            XAC: XAC2762(ispA)
            XOO: XOO3299(ispA)
            XOM: XOO_3122(XOO3122)
            VCH: VC0890
            VCO: VC0395_A0413(ispA)
            VVU: VV1_0314
            VVY: VV0869
            VPA: VP0687
            VFI: VF0712
            PPR: PBPRA0806
            PAE: PA4043(is)
            PAU: PA14_11560(ispA)
            PPU: PP_0528(ispA)
            PST: PSPTO_0699(ispA)
            PSB: Psyr_0605
            PSP: PSPPH_0600(ispA)
            PFL: PFL_5509
            PFO: Pfl_5006
            PEN: PSEEN0601(ispA)
            PAR: Psyc_1935(ispA)
            ACI: ACIAD2968(ispA)
            SON: SO_1526(ispA)
            SDN: Sden_2570
            SHN: Shewana3_2900
            ILO: IL2137(ispA_2)
            CPS: CPS_1089(ispA)
            PHA: PSHAa2365(ispA)
            MAQ: Maqu_2437
            CBU: CBU_1255
            LPN: lpg2330(ispA)
            LPF: lpl2250
            LPP: lpp2278
            MCA: MCA0818(ispA)
            FTU: FTT1562(ispA)
            FTF: FTF1562(ispA)
            FTL: FTL_0546
            FTH: FTH_0548(ispA)
            FTA: FTA_0579
            TCX: Tcr_1388
            NOC: Noc_2037
            AEH: Mlg_0945
            HHA: Hhal_1985
            HCH: HCH_05865(ispA)
            CSA: Csal_0098
            AHA: AHA_3320
            DNO: DNO_0648(ispA)
            BCI: BCI_0274(ispA)
            VOK: COSY_0445(ispA)
            NME: NMB0261
            NMA: NMA2226(ispA)
            NMC: NMC0255(ispA)
            NGO: NGO1735
            CVI: CV_2691(ispA)
            RSO: RSc2222(ispA)
            REU: Reut_A0881
            REH: H16_A2733(ispA)
            RME: Rmet_2616
            BMA: BMAA0329(ispA)
            BMV: BMASAVP1_1511(ispA)
            BML: BMA10299_1705(ispA)
            BMN: BMA10247_A0363(ispA)
            BXE: Bxe_B2828
            BUR: Bcep18194_B2212
            BCN: Bcen_4487
            BCH: Bcen2424_3878
            BAM: Bamb_3249
            BPS: BPSS1763(ispA)
            BPM: BURPS1710b_A0218(ispA) BURPS1710b_A0843(ispA)
            BPL: BURPS1106A_A2393(ispA)
            BPD: BURPS668_A2535(ispA)
            BTE: BTH_II0613
            BPE: BP2799
            BPA: BPP2463
            BBR: BB1911
            RFR: Rfer_2876
            POL: Bpro_1746
            MPT: Mpe_A2632
            HAR: HEAR0278(ispA)
            MMS: mma_0330
            NEU: NE1160(ispA)
            NET: Neut_1500
            NMU: Nmul_A0235
            EBA: ebA4440(ispA)
            AZO: azo1199(ispA)
            DAR: Daro_3060
            TBD: Tbd_0880
            MFA: Mfla_2132
            HPY: HP0929(ispA)
            HPA: HPAG1_0910
            HHE: HH0334(ispA)
            HAC: Hac_1086(ispA)
            WSU: WS1679(ispA)
            TDN: Tmden_0337
            CJE: Cj1644(ispA)
            CJR: CJE1816(ispA)
            CJJ: CJJ81176_1635(ispA)
            CJU: C8J_1546(ispA)
            CJD: JJD26997_2004(ispA)
            CFF: CFF8240_0068
            CCV: CCV52592_0071
            CHA: CHAB381_0201 CHAB381_0895
            CCO: CCC13826_1736
            ABU: Abu_0430(ispA)
            NIS: NIS_0257(ispA)
            SUN: SUN_0165(ispA) SUN_0639
            GSU: GSU1765
            PCA: Pcar_1668
            DVU: DVU1349
            DDE: Dde_2201
            BBA: Bd0199(yqiD)
            SAT: SYN_02457 SYN_03252
            WOL: WD1192(ispA)
            WBM: Wbm0737
            AMA: AM861(ispA)
            APH: APH_0329(ispA)
            ERU: Erum5660(ispA)
            ERW: ERWE_CDS_05930(ispA)
            ERG: ERGA_CDS_05840(ispA)
            ECN: Ecaj_0567
            ECH: ECH_0455
            NSE: NSE_0694
            PUB: SAR11_0610(ispA)
            MLO: mlr3784 mlr6368
            SME: SMc03884(ispA)
            ATU: Atu2721(ispA)
            ATC: AGR_C_4933
            RET: RHE_CH04011(ispA)
            RLE: RL4628(ispA)
            BME: BMEI0270 BMEI1532
            BMF: BAB1_1787
            BMS: BR1777(ispA)
            BMB: BruAb1_1760(ispA)
            BOV: BOV_1712(ispA)
            BJA: bll0946(ispA) blr2148(fppS)
            BRA: BRADO0555
            BBT: BBta_7621
            RPA: RPA0524
            RPB: RPB_0516
            RPC: RPC_0497
            RPD: RPD_0313
            RPE: RPE_0176
            NWI: Nwi_0495
            BHE: BH15260(ispA)
            BQU: BQ12170(ispA)
            CCR: CC_2069
            SIL: SPO0248(ispA)
            SIT: TM1040_2921
            RSP: RSP_0265(crtE) RSP_1135(ispA)
            RDE: RD1_0549(ispA)
            MMR: Mmar10_0848
            HNE: HNE_1839(ispA)
            ZMO: ZMO0855(ispA)
            GOX: GOX0251
            GBE: GbCGDNIH1_0220
            RRU: Rru_A2618
            MAG: amb2903
            MGM: Mmc1_1049
            SUS: Acid_3351
            BSU: BG11714(yqiD)
            BHA: BH2781
            BAN: BA4402(ispA)
            BAR: GBAA4402(ispA)
            BAA: BA_4854
            BAT: BAS4082
            BCE: BC4177
            BCA: BCE_4251(ispA)
            BCZ: BCZK3931(ispA)
            BTK: BT9727_3920(ispA)
            BTL: BALH_3786(ispA)
            BLI: BL01524(ispAB)
            BLD: BLi02599(yqiD)
            BCL: ABC2463(ispA)
            BAY: RBAM_022610(yqiD)
            BPU: BPUM_2160(yqiD)
            OIH: OB1877
            GKA: GK2393
            SAU: SA1352(ispA)
            SAV: SAV1521(ispA)
            SAM: MW1474(ispA)
            SAR: SAR1599
            SAS: SAS1460
            SAC: SACOL1566(ispA)
            SAB: SAB1394c
            SAA: SAUSA300_1470
            SAO: SAOUHSC_01618
            SEP: SE1202
            SER: SERP1082(ispA)
            SHA: SH1394(ispA)
            SSP: SSP1233
            LMO: lmo1363
            LMF: LMOf2365_1380
            LIN: lin1400
            LWE: lwe1378(ispA)
            LLA: L80459(ispA)
            LLC: LACR_0926
            LLM: llmg_1689(ispA)
            SPY: SPy_1498(fps)
            SPZ: M5005_Spy_1231(fps)
            SPM: spyM18_1516(ispA)
            SPG: SpyM3_1154(fps)
            SPS: SPs0708
            SPH: MGAS10270_Spy1247(fps)
            SPI: MGAS10750_Spy1338(fps)
            SPJ: MGAS2096_Spy1249(fps)
            SPK: MGAS9429_Spy1225(fps)
            SPF: SpyM50622(fps)
            SPA: M6_Spy1251
            SPB: M28_Spy1170(fps)
            SPN: SP_1205
            SPR: spr1087(ispA)
            SPD: SPD_1065(ispA)
            SAG: SAG0498
            SAN: gbs0544
            SAK: SAK_0599
            SMU: SMU.582
            STC: str1216(ispA)
            STL: stu1216(ispA)
            SSA: SSA_0676(ispA)
            SGO: SGO_0695
            LPL: lp_1602(ispA)
            LJO: LJ1547
            LAC: LBA1329
            LSA: LSA0679(ispA)
            LSL: LSL_0536(ispA) LSL_1028
            LBR: LVIS_0975
            LCA: LSEI_1636
            LGA: LGAS_0754
            EFA: EF0981(ispA)
            OOE: OEOE_1235
            CAC: CAC2080
            CPE: CPE1820
            CPF: CPF_2074(ispA)
            CPR: CPR_1788(ispA)
            CTC: CTC01577
            CNO: NT01CX_1982
            CDF: CD1205(ispA)
            CBO: CBO1883(ispA)
            CBH: CLC_1827(ispA)
            CBF: CLI_1947(ispA)
            CKL: CKL_1230(fps)
            CHY: CHY_1988
            MTU: Rv3398c(idsA1)
            MTC: MT3491 MT3506
            MBO: Mb3431c(idsA1)
            MBB: BCG_1144 BCG_3468c(idsA1)
            MSM: MSMEG_1133
            CGB: cg0723(crtE)
            SCO: SCO5250(2SC7G11.12) SCO6763(SC6A5.12)
            SMA: SAV2997(ptlB) SAV3006(idsB)
            FRA: Francci3_0822
            FAL: FRAAL1431(fppS)
            SEN: SACE_3979 SACE_4328 SACE_4646(ptlB) SACE_4909 SACE_5289
            FNU: FN1327
            RBA: RB2144(ggpP)
            CTR: CT628(ispA)
            CTA: CTA_0681(ispA)
            CMU: TC0917
            CPN: CPn0748(ispA)
            CPA: CP1125
            CPJ: CPj0748(ispA)
            CPT: CpB0776
            CCA: CCA01009(ispA)
            CAB: CAB979(ispA)
            CFE: CF0003(ispA)
            PCU: pc1996(ispA)
            LIL: LA0326(ispA)
            LIC: LIC10283(ispA)
            LBJ: LBJ_2397(ispA-1)
            LBL: LBL_0711(ispA-1)
            PMB: A9601_11751(ispA)
            PMC: P9515_11601(ispA)
            PMF: P9303_09331(ispA)
            PMG: P9301_11761(ispA)
            PMH: P9215_12051
            PME: NATL1_15151(ispA)
            BTH: BT_2058
            BFR: BF3745
            BFS: BF3533
            PGI: PG0784
            SRU: SRU_1874(idsA)
            CHU: CHU_0461(ispA)
            CTE: CT0256
            CCH: Cag_1446
            PVI: Cvib_1546
            PLT: Plut_1765
            DRA: DR_1395
            AAE: aq_748(ispA)
            TMA: TM0161
            MMP: MMP0045(idsA)
            MAC: MA0606(idsA)
            MBA: Mbar_A1417
            MMA: MM_1767
            MEM: Memar_1816
            MST: Msp_0854(idsA)
            MKA: MK0774(ispA)
            AFU: AF2286(idsA)
            HAL: VNG1150G(idsA)
            HMA: rrnAC0081(idsA)
            HWA: HQ2889A(idsA)
            NPH: NP3696A(idsA_3)
            PTO: PTO1199
            PHO: PH1072
            PAB: PAB2389(idsA)
            PFU: PF1102
            TKO: TK1468
            APE: APE_1764.1
            SSO: SSO0061(gds-1)
            STO: ST2058
            SAI: Saci_0092(gds)
            MSE: Msed_2135
            PAI: PAE1013
            TPE: Tpen_0606
STRUCTURES  PDB: 1FPS  1RQI  1RQJ  1YHK  1YHM  1YQ7  1YV5  1ZW5  2EWG  2F7M  
                 2F89  2F8C  2F8Z  2F92  2F94  2F9K  2FOR  2FTZ  2H8O  2I19  
                 2OGD  2OPN  2Q80  2QIS  2RAH  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.10
            ExPASy - ENZYME nomenclature database: 2.5.1.10
            ExplorEnz - The Enzyme Database: 2.5.1.10
            ERGO genome analysis and discovery system: 2.5.1.10
            BRENDA, the Enzyme Database: 2.5.1.10
            CAS: 37277-79-5
///
ENTRY       EC 2.5.1.11                 Enzyme
NAME        trans-octaprenyltranstransferase;
            all-trans-nonaprenyl-diphosphate synthase;
            solanesyl-diphosphate synthase;
            solanesyl pyrophosphate synthetase;
            SPP synthase;
            nonaprenyl pyrophosphate synthetase;
            polyprenylpyrophosphate synthetase;
            terpenoidallyltransferase;
            terpenyl pyrophosphate synthetase;
            trans-octaprenyltranstransferase;
            trans-prenyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     (E)-octaprenyl-diphosphate:isopentenyl-diphosphate
            octaprenyltranstransferase
REACTION    all-trans-octaprenyl diphosphate + isopentenyl diphosphate =
            diphosphate + all-trans-nonaprenyl diphosphate [RN:R07267]
ALL_REAC    R07267;
            (other) R05611
SUBSTRATE   all-trans-octaprenyl diphosphate [CPD:C04146];
            isopentenyl diphosphate [CPD:C00129]
PRODUCT     diphosphate [CPD:C00013];
            all-trans-nonaprenyl diphosphate [CPD:C04145]
COMMENT     This enzyme will also use geranyl diphosphate and all-trans-prenyl
            diphosphates of intermediate size as donors, but not dimethylallyl
            diphosphate.
REFERENCE   1  [PMID:7447947]
  AUTHORS   Fujii H, Sagami H, Koyama T, Ogura K, Seto S, Baba T, Allen CM.
  TITLE     Variable product specificity of solanesyl pyrophosphate synthetase.
  JOURNAL   Biochem. Biophys. Res. Commun. 96 (1980) 1648-53.
  ORGANISM  Micrococcus luteus
REFERENCE   2
  AUTHORS   Sagami, H., Ogura, K. and Seto, S.
  TITLE     Solanesyl pyrophosphate synthetase from Micrococcus lysodeikticus.
  JOURNAL   Biochemistry 16 (1978) 4616-4622.
  ORGANISM  Micrococcus lysodeikticus
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K05356  trans-octaprenyltranstransferase
GENES       PUB: SAR11_0614(ispB)
            SYW: SYNW1011(sds)
            SYG: sync_1551
            CYA: CYA_2276(sds)
            CYB: CYB_0451(sds)
            PMM: PMM0618(sds)
            PMT: PMT0392(sds)
            PMB: A9601_06741(sds)
            PMC: P9515_06831(sds)
            PMF: P9303_18951(sds)
            PMG: P9301_06441(sds)
            PME: NATL1_06761(sds)
STRUCTURES  PDB: 1V4E  1V4H  1V4I  1V4J  1V4K  1VG2  1VG3  1VG4  1VG6  1VG7  
                 1WKZ  1WL0  1WL1  1WL2  1WL3  2AZL  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.11
            ExPASy - ENZYME nomenclature database: 2.5.1.11
            ExplorEnz - The Enzyme Database: 2.5.1.11
            ERGO genome analysis and discovery system: 2.5.1.11
            BRENDA, the Enzyme Database: 2.5.1.11
            CAS: 64763-52-6
///
ENTRY       EC 2.5.1.12       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
COMMENT     Deleted entry: glutathione S-alkyltransferase. Now included with EC
            2.5.1.18 glutathione transferase (EC 2.5.1.12 created 1972, deleted
            1976)
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.12
            ExPASy - ENZYME nomenclature database: 2.5.1.12
            ExplorEnz - The Enzyme Database: 2.5.1.12
            ERGO genome analysis and discovery system: 2.5.1.12
            BRENDA, the Enzyme Database: 2.5.1.12
///
ENTRY       EC 2.5.1.13       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
COMMENT     Deleted entry: glutathione S-aryltransferase. Now included with EC
            2.5.1.18 glutathione transferase (EC 2.5.1.13 created 1972, deleted
            1976)
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.13
            ExPASy - ENZYME nomenclature database: 2.5.1.13
            ExplorEnz - The Enzyme Database: 2.5.1.13
            ERGO genome analysis and discovery system: 2.5.1.13
            BRENDA, the Enzyme Database: 2.5.1.13
///
ENTRY       EC 2.5.1.14       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
COMMENT     Deleted entry: glutathione S-aralkyltransferase. Now included with
            EC 2.5.1.18 glutathione transferase (EC 2.5.1.14 created 1972,
            deleted 1976)
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.14
            ExPASy - ENZYME nomenclature database: 2.5.1.14
            ExplorEnz - The Enzyme Database: 2.5.1.14
            ERGO genome analysis and discovery system: 2.5.1.14
            BRENDA, the Enzyme Database: 2.5.1.14
///
ENTRY       EC 2.5.1.15                 Enzyme
NAME        dihydropteroate synthase;
            dihydropteroate pyrophosphorylase;
            DHPS;
            7,8-dihydropteroate synthase;
            7,8-dihydropteroate synthetase;
            7,8-dihydropteroic acid synthetase;
            dihydropteroate synthetase;
            dihydropteroic synthetase;
            2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-
            diphosphate:4-aminobenzoate
            2-amino-4-hydroxydihydropteridine-6-methenyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl-diphosphate:4-ami
            nobenzoate 2-amino-4-hydroxydihydropteridine-6-methenyltransferase
REACTION    (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate +
            4-aminobenzoate = diphosphate + 7,8-dihydropteroate [RN:R03067]
ALL_REAC    R03067;
            (other) R03066
SUBSTRATE   (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate;
            4-aminobenzoate [CPD:C00568]
PRODUCT     diphosphate [CPD:C00013];
            7,8-dihydropteroate [CPD:C00921]
REFERENCE   1  [PMID:4304228]
  AUTHORS   Richey DP, Brown GM.
  TITLE     The biosynthesis of folic acid. IX. Purification and properties of
            the enzymes required for the formation of dihydropteroic acid.
  JOURNAL   J. Biol. Chem. 244 (1969) 1582-92.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4312465]
  AUTHORS   Shiota T, Baugh CM, Jackson R, Dillard R.
  TITLE     The enzymatic synthesis of hydroxymethyldihydropteridine
            pyrophosphate and dihydrofolate.
  JOURNAL   Biochemistry. 8 (1969) 5022-8.
  ORGANISM  Escherichia coli [GN:eco], Lactobacillus plantarum [GN:lpl]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K00796  dihydropteroate synthase
GENES       SCE: YNL256W(FOL1)
            AGO: AGOS_AFR647C
            PIC: PICST_66087
            CGR: CAGL0J07920g
            SPO: SPBC1734.03
            AFM: AFUA_2G09840
            CNE: CNC04040
            DDI: DDB_0230139
            PFA: PF08_0095
            ECO: b3177(folP)
            ECJ: JW3144(folP)
            ECE: Z4539(folP)
            ECS: ECs4056
            ECC: c3933(folP)
            ECI: UTI89_C3609(folP)
            ECP: ECP_3264
            ECV: APECO1_3255(folP)
            ECW: EcE24377A_3662(folP1) EcE24377A_B0005(folP2)
            ECX: EcHS_A3369(folP)
            STY: HCM1.222 STY3473(folP)
            STT: t3212(folP)
            SPT: SPA3162(folP)
            SEC: SC034(sulI)
            STM: STM3295(folP)
            YPE: YPO3501(folP)
            YPK: y0683(folP)
            YPM: YP_0582(folP)
            YPA: YPA_0051
            YPN: YPN_3245
            YPP: YPDSF_3550
            YPS: YPTB0475(folP)
            YPI: YpsIP31758_3601(folP)
            YEN: YE0429(dhpS)
            SFL: SF3217(folP)
            SFX: S2703 S3435(folP)
            SFV: SFV_3207(folP)
            SSN: SSON_3325(folP)
            SBO: SBO_3205(folP)
            SDY: SDY_3358(folP)
            ECA: ECA0699(dhpS)
            PLU: plu4534(folP)
            WBR: WGLp230(folP)
            SGL: SG0372
            ENT: Ent638_3611
            SPE: Spro_0484
            BFL: Bfl099(folP)
            BPN: BPEN_102(folP)
            HIT: NTHI1663(folP)
            HDU: HD0644(folP)
            HSO: HS_0729(folP)
            PMU: PM0439(folP)
            MSU: MS0966(folP)
            APL: APL_1876(folP)
            ASU: Asuc_1423
            XFA: XF0091
            XFT: PD0068(folP)
            XCC: XCC1714(folP)
            XCB: XC_2517
            XCV: XCV1766(folP)
            XAC: XAC1733(folP)
            XOM: XOO_2800(XOO2800)
            VCH: VC0638
            VCO: VC0395_A0167(folP)
            VVU: VV1_1691
            VVY: VV2714
            VPA: VP2462
            VFI: VF0480
            PPR: PBPRA0605
            PAE: PA4750(folP)
            PAU: PA14_62850(folP)
            PAP: PSPA7_5470(folP)
            PPU: PP_4717(folP)
            PPF: Pput_4583
            PST: PSPTO_4496(folP)
            PSB: Psyr_4186
            PSP: PSPPH_4197(folP)
            PFL: PFL_0837(folP)
            PFO: Pfl_0773
            PEN: PSEEN0788(folP)
            PMY: Pmen_3614
            PAR: Psyc_1737(folP)
            PCR: Pcryo_2019
            PRW: PsycPRwf_0536
            ACI: ACIAD2852(folP)
            SON: SO_1198(folP)
            SDN: Sden_1001
            SFR: Sfri_0984
            SAZ: Sama_0955
            SBL: Sbal_3245
            SBM: Shew185_3286
            SLO: Shew_2833
            SPC: Sputcn32_2840
            SSE: Ssed_3395
            SPL: Spea_3066
            SHE: Shewmr4_1020
            SHM: Shewmr7_1085
            SHN: Shewana3_1024
            SHW: Sputw3181_1064
            ILO: IL0974(folP)
            CPS: CPS_3451(folP)
            PHA: PSHAa0871(folP)
            PAT: Patl_1572
            SDE: Sde_2719
            PIN: Ping_0812
            MAQ: Maqu_3354
            CBU: CBU_1351(folP)
            CBD: COXBU7E912_1439(folP)
            LPN: lpg2795
            LPF: lpl2710(folP)
            LPP: lpp2841(folP)
            MCA: MCA2317(folP)
            FTU: FTT0942c(folK)
            FTF: FTF0942c(folK)
            FTW: FTW_0836
            FTL: FTL_1265
            FTH: FTH_1240(folK)
            FTN: FTN_0819
            TCX: Tcr_0813
            NOC: Noc_2568
            AEH: Mlg_1974
            HHA: Hhal_1769
            HCH: HCH_01233(folP)
            CSA: Csal_3080
            ABO: ABO_0323(folP)
            MMW: Mmwyl1_1021
            AHA: AHA_3311(folP)
            DNO: DNO_1237(folP)
            BCI: BCI_0637(folP)
            RMA: Rmag_0137
            VOK: COSY_0139(folP)
            NME: NMB1691
            NMA: NMA1950(dhpS)
            NMC: NMC1609(dhpS)
            NGO: NGO1342
            CVI: CV_3796(folP)
            RSO: RSc1527(folP)
            REU: Reut_A2169
            REH: H16_A2446(folP)
            RME: Rmet_2187
            BMA: BMA0778(folP)
            BMV: BMASAVP1_A1289(folP)
            BML: BMA10299_A0579(folP)
            BMN: BMA10247_0572(folP)
            BXE: Bxe_A1263
            BVI: Bcep1808_1251
            BUR: Bcep18194_A4440
            BCN: Bcen_0817
            BCH: Bcen2424_1298
            BAM: Bamb_1175
            BPS: BPSL1357(folP)
            BPM: BURPS1710b_1616(folP)
            BPL: BURPS1106A_1513(folP)
            BPD: BURPS668_1483(folP)
            BTE: BTH_I2775
            PNU: Pnuc_1012
            BPE: BP1076(folP)
            BPA: BPP2068(folP)
            BBR: BB1461(folP)
            RFR: Rfer_2012
            POL: Bpro_2851
            PNA: Pnap_2610
            AAV: Aave_2618
            AJS: Ajs_2382
            VEI: Veis_0210
            MPT: Mpe_A1269
            HAR: HEAR1171(folP)
            MMS: mma_2236(folP)
            NEU: NE0529(folP)
            NET: Neut_0999
            NMU: Nmul_A0484
            EBA: ebA4824(dhpS)
            AZO: azo1388(folP)
            DAR: Daro_0945
            TBD: Tbd_1134
            MFA: Mfla_0784
            HPY: HP1232(folP)
            HPA: HPAG1_1174
            HHE: HH0621(folP)
            HAC: Hac_1643(folP)
            WSU: WS1732(folP)
            TDN: Tmden_1647
            CJE: Cj0585(folP)
            CJR: CJE0688(folP)
            CJJ: CJJ81176_0613(folP)
            CJU: C8J_0547(folP)
            CJD: JJD26997_1084(folP)
            CCO: CCC13826_2021
            ABU: Abu_1202(folP)
            NIS: NIS_1137
            SUN: SUN_0459
            GSU: GSU1808(folP)
            GME: Gmet_1889
            GUR: Gura_2733
            PCA: Pcar_0998
            PPD: Ppro_2253
            DVU: DVU1279(folP)
            DVL: Dvul_1786
            DDE: Dde_1514
            LIP: LI0189(folP)
            DPS: DP3098
            ADE: Adeh_1496
            AFW: Anae109_2337
            MXA: MXAN_4353(folP)
            SAT: SYN_02578 SYN_02778
            SFU: Sfum_0550
            RFE: RF_0039(folKP)
            RBE: RBE_0032(folKP)
            AMA: AM931(folP)
            APH: APH_0254(folP)
            ERU: Erum6280(folP1) Erum6290(folP2)
            ERW: ERWE_CDS_06590(folP) ERWE_CDS_06600(folP)
            ERG: ERGA_CDS_06500(folP) ERGA_CDS_06510(folP)
            ECN: Ecaj_0633
            ECH: ECH_0381(folP)
            NSE: NSE_0485(folP)
            PUB: SAR11_0602(folP)
            MLO: mll0788
            MES: Meso_1412
            PLA: Plav_2130
            SME: SMc00462(folP)
            SMD: Smed_1534
            ATU: Atu1352(folP)
            ATC: AGR_C_2497
            RET: RHE_CH02336(folP)
            RLE: RL2650(folC)
            BME: BMEI0956
            BMF: BAB1_1049
            BMS: BR1029(folP)
            BMB: BruAb1_1034(folP)
            BOV: BOV_0995(folP)
            OAN: Oant_2115
            BJA: bll3059
            BRA: BRADO2685(folP)
            BBT: BBta_3026(folP)
            RPA: RPA1840(folP)
            RPB: RPB_3533
            RPC: RPC_1765
            RPD: RPD_1932
            RPE: RPE_1857
            NWI: Nwi_2233
            NHA: Nham_2633
            XAU: Xaut_2493
            CCR: CC_3224
            SIL: SPO1363(folP)
            SIT: TM1040_2306
            RSP: RSP_1862
            RSH: Rsph17029_0511
            RSQ: Rsph17025_0648
            JAN: Jann_2726
            RDE: RD1_1951(folP)
            PDE: Pden_0544
            MMR: Mmar10_2410
            HNE: HNE_2366(folP)
            ZMO: ZMO1006(sul)
            NAR: Saro_1841
            SAL: Sala_0966
            SWI: Swit_4577
            ELI: ELI_02305
            GOX: GOX1535
            GBE: GbCGDNIH1_0765 GbCGDNIH1_1111
            ACR: Acry_0816
            RRU: Rru_A1099
            MAG: amb3205
            MGM: Mmc1_0439
            ABA: Acid345_4496
            SUS: Acid_6708
            BSU: BG10140(sul)
            BHA: BH0093(sul)
            BAN: BA0071(folP)
            BAR: GBAA0071(folP)
            BAA: BA_0661
            BAT: BAS0071
            BCE: BC0079
            BCA: BCE_0070(folP)
            BCZ: BCZK0067(sul)
            BCY: Bcer98_0067
            BTK: BT9727_0067(sul)
            BTL: BALH_0070(folP)
            BLI: BL00861(sul)
            BLD: BLi00093(sul)
            BCL: ABC0113(sul)
            BAY: RBAM_000880(sul)
            BPU: BPUM_0061(sul)
            OIH: OB0085
            GKA: GK0069
            SAU: SA0472(folP)
            SAV: SAV0514(folP)
            SAM: MW0469(folP)
            SAR: SAR0515(folP)
            SAS: SAS0471
            SAC: SACOL0558(folP)
            SAB: SAB0463(folP)
            SAA: SAUSA300_0492(folP)
            SAO: SAOUHSC_00489
            SAJ: SaurJH9_0536
            SAH: SaurJH1_0549
            SEP: SE2269
            SER: SERP0153(folP)
            SHA: SH2496(folP)
            SSP: SSP2242
            LMO: lmo0224(sul)
            LMF: LMOf2365_0236(folP)
            LIN: lin0256(sul)
            LWE: lwe0188(folP)
            LLA: L0176(folP)
            LLC: LACR_1276
            LLM: llmg_1336(folP)
            SPY: SPy_1098(folP)
            SPZ: M5005_Spy_0822(folP)
            SPM: spyM18_1060(folP)
            SPG: SpyM3_0760(folP)
            SPS: SPs0960
            SPH: MGAS10270_Spy0938(folP)
            SPI: MGAS10750_Spy0973(folP)
            SPJ: MGAS2096_Spy0896(folP)
            SPK: MGAS9429_Spy0941(folP)
            SPF: SpyM50966(folP)
            SPA: M6_Spy0820
            SPB: M28_Spy0799(folP)
            SPN: SP_0289
            SPR: spr0266(sulA)
            SPD: SPD_0269(folP)
            SAG: SAG1115(folP)
            SAN: gbs1182
            SAK: SAK_1200(folP)
            SMU: SMU.969(folP)
            STC: str1543(folP)
            STL: stu1543(folP)
            SSA: SSA_0197(folP)
            SGO: SGO_1914(folP)
            LPL: lp_3294(folP)
            LSA: LSA1098(folP)
            LDB: Ldb0249(folP)
            LBU: LBUL_0211
            LRE: Lreu_1275
            EFA: EF3265(folP)
            STH: STH3188
            CAC: CAC2926(sul)
            CPE: CPE1021(folP)
            CPF: CPF_1276(folP)
            CPR: CPR_1098(folP)
            CNO: NT01CX_0375(folP)
            CTH: Cthe_2581
            CDF: CD1450(folP)
            CBO: CBO0828(dhpS)
            CBA: CLB_0869(folP)
            CBH: CLC_0883(folP)
            CBF: CLI_0910(folP)
            CBE: Cbei_0206
            CKL: CKL_0957(folP)
            AMT: Amet_2161
            CHY: CHY_2383(folP)
            DSY: DSY0207
            DRM: Dred_0154
            SWO: Swol_0097
            CSC: Csac_0110
            TTE: TTE2370(folP)
            MTA: Moth_0110
            POY: PAM581(folP)
            AYW: AYWB_246
            MTU: Rv1207(folP2) Rv3608c(folP1)
            MTC: MT1245(folP-1) MT3712(folP-2)
            MBO: Mb1239(folP2) Mb3638c(folP1)
            MBB: BCG_1267(folP2) BCG_3672c(folP1)
            MLE: ML0224(folP) ML1063(folP2)
            MPA: MAP0450(folP) MAP2570c(folP2)
            MAV: MAV_0544(folP) MAV_1352(folP)
            MSM: MSMEG_5085(folP) MSMEG_6103(folP)
            MVA: Mvan_4509 Mvan_5370
            MGI: Mflv_1418 Mflv_2186
            MMC: Mmcs_4006 Mmcs_4768
            MKM: Mkms_4080 Mkms_4854
            MJL: Mjls_4236 Mjls_5154
            CGL: NCgl1066(cgl1111) NCgl2601(cgl2694)
            CGB: cg1262(folP2) cg2982(folP1)
            CEF: CE1168 CE2540
            CDI: DIP0984(folP) DIP1948 DIP1999
            CJK: jk0280(folP)
            NFA: nfa4000(folP) nfa47370(folP2)
            RHA: RHA1_ro01825 RHA1_ro04409 RHA1_ro05968
            SCO: SCO3398(folP) SCO5141(folP)
            SMA: SAV3123(folP1) SAV4672(folP2)
            TWH: TWT586(folPXK)
            TWS: TW175(folP)
            LXX: Lxx17980(folP) Lxx21480(folP)
            CMI: CMM_0846(folP)
            ART: Arth_0153
            AAU: AAur_0140(folP)
            PAC: PPA0271
            NCA: Noca_0446 Noca_0638 Noca_4156
            TFU: Tfu_1314 Tfu_2893
            FRA: Francci3_3839 Francci3_4407
            FAL: FRAAL6098(folP) FRAAL6710(folP)
            ACE: Acel_0207 Acel_1839
            KRA: Krad_0540
            SEN: SACE_0398(folP) SACE_1023(folP) SACE_4499(folP)
            STP: Strop_0702 Strop_4297
            BLO: BL1684(folP)
            BAD: BAD_0411(folP)
            RXY: Rxyl_2184
            FNU: FN0073
            RBA: RB6484(folP)
            CTR: CT613(folP)
            CTA: CTA_0666(folP)
            CMU: TC0903
            CPN: CPn0758(folP)
            CPA: CP1114
            CPJ: CPj0758(folP)
            CPT: CpB0786
            CCA: CCA00999(folKP)
            CAB: CAB969(folKP)
            CFE: CF0014(folP)
            PCU: pc1632(folP)
            LIL: LA0057(folP)
            LIC: LIC10051(folP)
            LBJ: LBJ_0045(folP)
            LBL: LBL_2999(folP)
            SYN: slr2026(folP)
            SYW: SYNW0822(folP)
            SYC: syc1798_c(folP)
            SYF: Synpcc7942_2303
            SYD: Syncc9605_1826
            SYE: Syncc9902_0829
            SYG: sync_1211(folP)
            SYR: SynRCC307_0973
            SYX: SynWH7803_1436(folP)
            CYA: CYA_0022(folP)
            CYB: CYB_2922(folP)
            TEL: tlr1522(folP)
            GVI: glr0540(folP)
            ANA: alr4386
            AVA: Ava_3289
            PMA: Pro0902(folP)
            PMM: PMM0830(folP)
            PMT: PMT0816(folP)
            PMN: PMN2A_0381
            PMI: PMT9312_0970
            PMB: A9601_10401(folP)
            PMC: P9515_09051(folP)
            PMG: P9301_10401(folP)
            PMH: P9215_10721(folP)
            PME: NATL1_10631(folP)
            TER: Tery_1381
            BTH: BT_3646
            BFR: BF0457
            BFS: BF0396(folP)
            PGI: PG1589(folP)
            SRU: SRU_1947(folP)
            CHU: CHU_3223(folP)
            GFO: GFO_0429(folP)
            FJO: Fjoh_3497
            FPS: FP1425(folP)
            CTE: CT1706(folP)
            CCH: Cag_0420
            CPH: Cpha266_0505
            PVI: Cvib_1461
            PLT: Plut_1676
            DET: DET1603(folP)
            DEH: cbdb_A1696(folP)
            DEB: DehaBAV1_1349
            DRA: DR_0168
            DGE: Dgeo_0396
            TTH: TTC1795
            TTJ: TTHA0191
            AAE: aq_1468(folP)
            TMA: TM0040
            TPT: Tpet_0883
            TME: Tmel_0868
            FNO: Fnod_0098
            MBA: Mbar_A2314
            MMA: MM_0440 MM_0698
            MBU: Mbur_1815
            MTP: Mthe_1468
            MHU: Mhun_0021
            MEM: Memar_1835
            MBN: Mboo_2189
            HAL: VNG0412G(folP)
            HMA: pNG7379(folP2) rrnAC0184(folP) rrnAC0246(folP3)
            HWA: HQ1767A(folCP) HQ2465A(folP)
            NPH: NP1478A(folCP) NP3770A(folP_2)
            TAC: Ta0079
            TVO: TVN0153
            PTO: PTO0551
            PFU: PF1296
            TKO: TK1161
            PAI: PAE2937
            PIS: Pisl_0343
            PCL: Pcal_1162
            PAS: Pars_1313
STRUCTURES  PDB: 1AD1  1AD4  1AJ0  1AJ2  1AJZ  1EYE  1TWS  1TWW  1TWZ  1TX0  
                 1TX2  2DQW  2DZA  2DZB  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.15
            ExPASy - ENZYME nomenclature database: 2.5.1.15
            ExplorEnz - The Enzyme Database: 2.5.1.15
            ERGO genome analysis and discovery system: 2.5.1.15
            BRENDA, the Enzyme Database: 2.5.1.15
            CAS: 9055-61-2
///
ENTRY       EC 2.5.1.16                 Enzyme
NAME        spermidine synthase;
            aminopropyltransferase;
            putrescine aminopropyltransferase;
            spermidine synthetase;
            SpeE
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     S-adenosylmethioninamine:putrescine 3-aminopropyltransferase
REACTION    S-adenosylmethioninamine + putrescine = 5'-S-methyl-5'-thioadenosine
            + spermidine [RN:R01920]
ALL_REAC    R01920;
            (other) R02869
SUBSTRATE   S-adenosylmethioninamine [CPD:C01137];
            putrescine [CPD:C00134]
PRODUCT     5'-S-methyl-5'-thioadenosine;
            spermidine [CPD:C00315]
COMMENT     This enzyme is not identical with EC 2.5.1.22, spermine synthase.
            The mammalian enzyme is highly specific but the bacterial enzyme can
            use other acceptors and can synthesize spermine.
REFERENCE   1  [PMID:4564056]
  AUTHORS   Hannonen P, Janne J, Raina A.
  TITLE     Partial purification and characterization of spermine synthase from
            rat brain.
  JOURNAL   Biochim. Biophys. Acta. 289 (1972) 225-31.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6798961]
  AUTHORS   Pegg AE, Shuttleworth K, Hibasami H.
  TITLE     Specificity of mammalian spermidine synthase and spermine synthase.
  JOURNAL   Biochem. J. 197 (1981) 315-20.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Tabor, C.W.
  TITLE     Propylamine transferase (spermidine synthesis).
  JOURNAL   Methods Enzymol. 5 (1962) 761-765.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:4628436]
  AUTHORS   Tabor H, Tabor CW.
  TITLE     Biosynthesis and metabolism of 1,4-diaminobutane, spermidine,
            spermine, and related amines.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 36 (1972) 203-68.
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00271  Methionine metabolism
            PATH: map00410  beta-Alanine metabolism
ORTHOLOGY   KO: K00797  spermidine synthase
GENES       HSA: 6723(SRM)
            PTR: 457943(SRM)
            MMU: 20810(Srm)
            RNO: 84596(Srm)
            CFA: 608702(LOC608702)
            GGA: 771447(SRM)
            XLA: 431924(MGC83147)
            DRE: 394009(zgc:63600)
            SPU: 591935(LOC591935)
            DME: Dmel_CG8327(SpdS)
            CEL: Y46G5A.19
            ATH: AT1G23820(SPDS1) AT1G70310(SPDS2)
            OSA: 4328835 4341195 4342996
            CME: CMP329C CMR256C
            SCE: YPR069C(SPE3)
            AGO: AGOS_ADL340W
            PIC: PICST_84352
            CGR: CAGL0D01408g
            SPO: SPBC12C2.07c
            ANI: AN0687.2
            AFM: AFUA_1G13490
            AOR: AO090012000528
            CNE: CNG01150
            UMA: UM05818.1
            DDI: DDB_0191167(spsA)
            PFA: PF11_0301
            TET: TTHERM_00419690
            TBR: Tb09.v1.0380
            TCR: 503855.20 504033.130 510337.40 510339.50
            LMA: LmjF04.0580
            ECO: b0121(speE)
            ECJ: JW0117(speE)
            ECE: Z0131(speE)
            ECS: ECs0125
            ECC: c0150(speE)
            ECI: UTI89_C0134(speE)
            ECP: ECP_0128
            ECV: APECO1_1864(speE)
            ECW: EcE24377A_0123(speE)
            ECX: EcHS_A0125(speE)
            STY: STY0188(speE)
            STT: t0171(speE)
            SPT: SPA0169(speE)
            SEC: SC0166(speE)
            STM: STM0166(speE)
            YPE: YPO3411(speE)
            YPK: y0775(speE)
            YPM: YP_0274(speE)
            YPA: YPA_2913
            YPN: YPN_0677
            YPP: YPDSF_2944
            YPS: YPTB0720(speE)
            YPI: YpsIP31758_3354(speE)
            YEN: YE0710(speE)
            SFL: SF0118(speE)
            SFX: S0120(speE)
            SFV: SFV_0112(speE)
            SSN: SSON_0129(speE)
            SBO: SBO_0110(speE)
            SDY: SDY_0028(speE)
            ECA: ECA3333(speE)
            PLU: plu0843(speE)
            BUC: BU209(speE)
            BAS: BUsg203(speE)
            SGL: SG0479
            XFA: XF0143
            XFT: PD0112(speE)
            XCC: XCC3869(speE)
            XCB: XC_3954
            XCV: XCV4039(speE)
            XAC: XAC3924(speE)
            XOO: XOO0219(speE)
            XOM: XOO_0194(XOO0194)
            VVU: VV2_1635
            VVY: VVA0446
            PAE: PA1687(speE) PA4774
            PAU: PA14_42690(speE) PA14_63120
            PAP: PSPA7_3584(speE)
            PST: PSPTO_2055(speE)
            PSB: Psyr_1864
            PSP: PSPPH_1824(speE)
            PFO: Pfl_1732
            SON: SO_3763
            SDN: Sden_0699
            SFR: Sfri_3264
            SAZ: Sama_1964 Sama_2666
            SBL: Sbal_3448
            SBM: Shew185_0890
            SLO: Shew_0625
            SPC: Sputcn32_3089
            SSE: Ssed_3836
            SPL: Spea_3480
            SHE: Shewmr4_3112
            SHM: Shewmr7_0860
            SHN: Shewana3_0829
            SHW: Sputw3181_0855
            CPS: CPS_4189 CPS_4320
            PHA: PSHAa0040 PSHAa2847(speE) PSHAb0034
            SDE: Sde_1222
            MCA: MCA2046(speE)
            FTU: FTT0431(speE)
            FTF: FTF0431(speE)
            FTW: FTW_1643(speE)
            FTL: FTL_0500
            FTH: FTH_0498(speE)
            FTA: FTA_0525(speE)
            TCX: Tcr_0273
            NOC: Noc_0558
            AEH: Mlg_0073
            HCH: HCH_06404(speE)
            CSA: Csal_0119
            ABO: ABO_2399(speE)
            NME: NMB0869
            NMA: NMA1087
            CVI: CV_4130
            RSO: RS05370(RSp0825) RSp1306(speE2) RSp1337(speE1)
            REU: Reut_A3304 Reut_B5699
            REH: H16_A1603 H16_A2204 H16_A2643 H16_A2647(speE)
            RME: Rmet_2981 Rmet_3461 Rmet_4663
            BMA: BMA2470
            BXE: Bxe_A0564 Bxe_B0334 Bxe_B0336 Bxe_C0180
            BUR: Bcep18194_A3721(speE) Bcep18194_B0816 Bcep18194_C7063
            BCN: Bcen_0154 Bcen_1274 Bcen_3473
            BCH: Bcen2424_0637 Bcen2424_4893 Bcen2424_6557
            BAM: Bamb_0537
            BPS: BPSL2954 BPSS1151
            BPM: BURPS1710b_3468(speE) BURPS1710b_A0114
            BPL: BURPS1106A_3470(speE)
            BPD: BURPS668_3433(speE)
            BTE: BTH_I1194 BTH_II1257
            RFR: Rfer_2633
            POL: Bpro_0913
            AJS: Ajs_0746
            MPT: Mpe_A0249
            HAR: HEAR0760 HEAR2543
            NEU: NE0347(speE)
            NET: Neut_2464
            NMU: Nmul_A0102
            EBA: ebA2152(speE)
            AZO: azo2053(speE1) azo3986(speE2)
            DAR: Daro_0026 Daro_3735
            TBD: Tbd_2111
            MFA: Mfla_1235
            HPY: HP0832(speE)
            HPJ: jhp0771(speE)
            HPA: HPAG1_0818
            HHE: HH1699(speE)
            HAC: Hac_1202(speE)
            WSU: WS2148
            TDN: Tmden_2048
            ABU: Abu_0142(speE)
            NIS: NIS_0100(speE)
            BBA: Bd3616
            MXA: MXAN_1183
            SAT: SYN_01347
            SFU: Sfum_1994
            PUB: SAR11_1211(speE)
            RLE: pRL110433
            BRA: BRADO0662 BRADO4719 BRADO6330
            BBT: BBta_1296 BBta_3479 BBta_7524
            RPE: RPE_2992
            SIT: TM1040_1389
            JAN: Jann_0855
            GOX: GOX1091
            GBE: GbCGDNIH1_1386
            RRU: Rru_A1691
            MGM: Mmc1_3170
            ABA: Acid345_0111
            BSU: BG12460(speE)
            BHA: BH3811
            BAN: BA5445 BA5619(speE)
            BAR: GBAA5445 GBAA5619(speE)
            BAA: BA_0298 BA_0474
            BAT: BAS5060 BAS5219
            BCE: BC5213(speE) BC5371
            BCA: BCE_5500(speE)
            BCZ: BCZK4905(speE) BCZK5067(speE)
            BTK: BT9727_4890(speE) BT9727_5051(speE)
            BTL: BALH_4705(speE) BALH_4867(speE)
            BLI: BL03920(speE)
            BLD: BLi03974(speE)
            BCL: ABC3898(speE)
            BAY: RBAM_034620(speE)
            BPU: BPUM_3387(speE)
            OIH: OB0943
            GKA: GK1740 GK3405
            SPN: SP_0918
            SPR: spr0819(speE)
            SPD: SPD_0811(speE)
            STH: STH1613 STH17
            CAC: CAC2602
            CPE: CPE0550(speE)
            CPF: CPF_0529(speE)
            CPR: CPR_0515(speE)
            CTC: CTC02249
            CTH: Cthe_0694
            CDF: CD0890(speE)
            CKL: CKL_3157(speE)
            CHY: CHY_1240(speE1) CHY_1621(speE2)
            DSY: DSY0237 DSY4248
            SWO: Swol_0668 Swol_1199
            TTE: TTE1334(speE)
            MTA: Moth_1816
            MTU: Rv2601(speE)
            MTC: MT2675(speE)
            MBO: Mb2632(speE)
            MBB: BCG_2625(speE)
            MPA: MAP1031c(speE)
            MMC: Mmcs_1882
            CGL: NCgl2608(cgl2702)
            CGB: cg2990(speE)
            CEF: CE2547
            NFA: nfa34940
            RHA: RHA1_ro02313 RHA1_ro02466
            SCO: SCO2455(SCC24.26c)
            SMA: SAV4519(speE)
            TFU: Tfu_2234
            SEN: SACE_0456(speE)
            RBA: RB2115(speE)
            LIL: LA3811(speE1) LB311(speE2)
            LIC: LIC10437
            LBJ: LBJ_2595(speE) LBJ_4228(speE)
            LBL: LBL_0517(speE) LBL_4242(speE)
            SYW: SYNW2421(speE)
            SYC: syc0896_c
            SYF: Synpcc7942_0628
            SYD: Syncc9605_2590
            SYE: Syncc9902_2229
            SYG: sync_2850(speE)
            SYR: SynRCC307_2434(speE)
            SYX: SynWH7803_1192(speE) SynWH7803_2453(speE)
            CYA: CYA_0575(speE)
            CYB: CYB_0058(speE)
            PMA: Pro1848(speE)
            PMM: PMM1685(speE)
            PMT: PMT2213(speE)
            PMN: PMN2A_1286
            PMI: PMT9312_1778
            PMB: A9601_18951(speE)
            PMC: P9515_18761(speE)
            PMF: P9303_29501(speE)
            PMG: P9301_18761(speE)
            PMH: P9215_19581(speE)
            PME: NATL1_21581(speE)
            TER: Tery_0248 Tery_0886
            TTH: TTC0472
            TTJ: TTHA0824
            AAE: aq_062(speE) aq_1350
            TMA: TM0654
            MMP: MMP1584
            MHU: Mhun_2884
            MKA: MK0961(speE)
            HMA: rrnB0070(speE)
            HWA: HQ1919A(speE)
            TAC: Ta0355
            TVO: TVN0417
            PTO: PTO0613
            PAB: PAB2221(speE)
            PFU: PF0127
            TKO: TK0147
            APE: APE_0767.1
            HBU: Hbut_0057 Hbut_0383
            SSO: SSO0757
            STO: ST0346
            SAI: Saci_0643
            PAI: PAE1203
STRUCTURES  PDB: 1INL  1IY9  1JQ3  1MJF  1UIR  1XJ5  2B2C  2CMG  2CMH  2E5W  
                 2HTE  2I7C  2O05  2O06  2O07  2O0L  2PWP  2Q41  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.16
            ExPASy - ENZYME nomenclature database: 2.5.1.16
            ExplorEnz - The Enzyme Database: 2.5.1.16
            ERGO genome analysis and discovery system: 2.5.1.16
            BRENDA, the Enzyme Database: 2.5.1.16
            CAS: 37277-82-0
///
ENTRY       EC 2.5.1.17                 Enzyme
NAME        cob(I)yrinic acid a,c-diamide adenosyltransferase;
            CobA;
            CobO;
            ATP:corrinoid adenosyltransferase;
            cob(I)alamin adenosyltransferase;
            aquacob(I)alamin adenosyltransferase;
            aquocob(I)alamin vitamin B12s adenosyltransferase;
            ATP:cob(I)alamin Cobeta-adenosyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     ATP:cob(I)yrinic acid-a,c-diamide Cobeta-adenosyltransferase
REACTION    (1) ATP + cob(I)yrinic acid a,c-diamide = triphosphate +
            adenosylcob(III)yrinic acid a,c-diamide [RN:R05220];
            (2) ATP + cobinamide = triphosphate + adenosylcobinamide [RN:R07268]
ALL_REAC    R05220 R07268;
            (other) R01492
SUBSTRATE   ATP [CPD:C00002];
            cob(I)yrinic acid a,c-diamide [CPD:C06505];
            cobinamide [CPD:C05774]
PRODUCT     triphosphate [CPD:C00536];
            adenosylcob(III)yrinic acid a,c-diamide [CPD:C06506];
            adenosylcobinamide
COFACTOR    Manganese [CPD:C00034]
COMMENT     The corrinoid adenosylation pathway comprises three steps: (i)
            reduction of Co(III) to Co(II) by a one-electron transfer. This can
            be carried out by EC 1.16.1.3, aquacobalamin reductase or
            non-enzymically in the presence of dihydroflavin nucleotides [2].
            (ii) Co(II) is reduced to Co(I) in a second single-electron transfer
            by EC 1.16.1.4, cob(II)alamin reductase and (iii) the Co(I) conducts
            a nucleophilic attack on the adenosyl moiety of ATP to leave the
            cobalt atom in a Co(III) state (EC 2.5.1.17). The enzyme responsible
            for the adenosylation reaction is the product of the gene cobO in
            the aerobic bacterium Pseudomonas denitrificans and of the gene cobA
            in the anaerobic bacterium Salmonella typhimurium. In P.
            denitrificans, the enzyme shows specificity for cobyrinic acid
            a,c-diamide and the corrinoids that occur later in the biosynthetic
            pathway whereas CobA seems to have broader specificity [3]. While
            CobA has a preference for ATP and Mn2+, it is able to transfer a
            variety of nucleosides to the cobalt, including CTP, UTP and GTP, in
            decreasing order of preference [4] and to use Mg2+ instead of Mn2+.
REFERENCE   1  [PMID:5946606]
  AUTHORS   Vitols E, Walker GA, Huennekens FM.
  TITLE     Enzymatic conversion of vitamin B-12s to a cobamide coenzyme,
            alpha-(5,6-dimethylbenzimidazolyl)deoxyadenosylcobamide
            (adenosyl-B-12).
  JOURNAL   J. Biol. Chem. 241 (1966) 1455-61.
  ORGANISM  Clostridium tetanomorphum
REFERENCE   2  [PMID:11148030]
  AUTHORS   Bauer CB, Fonseca MV, Holden HM, Thoden JB, Thompson TB,
            Escalante-Semerena JC, Rayment I.
  TITLE     Three-dimensional structure of ATP:corrinoid adenosyltransferase
            from Salmonella typhimurium in its free state, complexed with MgATP,
            or complexed with hydroxycobalamin and MgATP.
  JOURNAL   Biochemistry. 40 (2001) 361-74.
  ORGANISM  Salmonella typhimurium
REFERENCE   3  [PMID:11408479]
  AUTHORS   Fonseca MV, Escalante-Semerena JC.
  TITLE     An in vitro reducing system for the enzymic conversion of cobalamin
            to adenosylcobalamin.
  JOURNAL   J. Biol. Chem. 276 (2001) 32101-8.
  ORGANISM  Salmonella enterica
REFERENCE   4  [PMID:7860601]
  AUTHORS   Suh S, Escalante-Semerena JC.
  TITLE     Purification and initial characterization of the ATP:corrinoid
            adenosyltransferase encoded by the cobA gene of Salmonella
            typhimurium.
  JOURNAL   J. Bacteriol. 177 (1995) 921-5.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K00798  cob(I)alamin adenosyltransferase
            KO: K04032  ethanolamine utilization cobalamin adenosyltransferase
GENES       HSA: 326625(MMAB)
            PTR: 452403(MMAB)
            MMU: 77697(Mmab)
            CFA: 486310(MMAB)
            SPU: 579282(LOC579282)
            DDI: DDBDRAFT_0204262 DDBDRAFT_0218202
            ECO: b1270(btuR) b2459(eutT)
            ECJ: JW1262(btuR) JW2443(eutT)
            ECE: Z0886 Z2540(btuR) Z3715
            ECS: ECs0756 ECs1842 ECs3321
            ECC: c1735(btuR) c2984
            ECI: UTI89_C1538(btuR) UTI89_C2783(eutT)
            ECP: ECP_1319 ECP_2471
            ECV: APECO1_4098(eutT) APECO1_430(btuR)
            ECW: EcE24377A_1468(btuR) EcE24377A_2736(eutT)
            ECX: EcHS_A1379(btuR) EcHS_A2588(eutT)
            STY: STY1332(btuR) STY2703
            STT: t0392 t1631(btuR)
            SPT: SPA0401(eutT) SPA1158(btuR)
            SEC: SC1715(btuR) SC2463(eutT)
            STM: STM1718(btuR) STM2467(eutT)
            YPE: YPO2214(btuR)
            YPK: y2055(btuR)
            YPM: YP_2011(btuR)
            YPA: YPA_1572
            YPN: YPN_1681
            YPP: YPDSF_0921
            YPS: YPTB2136(btuR)
            YPI: YpsIP31758_1927(cobO)
            YEN: YE4035(btuR)
            SFL: SF1272(btuR)
            SFX: S1357(btuR)
            SFV: SFV_1282(btuR)
            SSN: SSON_1873(btuR) SSON_2539
            SBO: SBO_1796(btuR) SBO_2474
            SDY: SDY_1340(btuR)
            ECA: ECA2290(btuR)
            PLU: plu2451(btuR) plu2964
            ENT: Ent638_2200
            SPE: Spro_2661
            XCC: XCC3064(btuR)
            XCB: XC_1094
            XCV: XCV3320(cobA)
            XAC: XAC3191(btuR)
            XOO: XOO1349(btuR)
            XOM: XOO_1239(XOO1239)
            VCH: VC1040
            VCO: VC0395_A0558(cobA)
            VVU: VV1_3022
            VVY: VV1263
            VPA: VP2065
            VFI: VF1750
            PPR: PBPRA1180
            PAE: PA1272(cobO)
            PAU: PA14_47790(cobO) PA14_57180
            PAP: PSPA7_4118(cobO)
            PPU: PP_1672(cobO)
            PPF: Pput_4047
            PST: PSPTO_1708(cobO)
            PSB: Psyr_3681
            PSP: PSPPH_3702(cobO)
            PFL: PFL_4431(cobO)
            PFO: Pfl_1641
            PEN: PSEEN1378 PSEEN4473
            PMY: Pmen_1750
            SON: SO_1039(cobO)
            SDN: Sden_1119
            SFR: Sfri_0880
            SAZ: Sama_0766
            SBL: Sbal_3360
            SBM: Shew185_0981
            SLO: Shew_0718
            SPC: Sputcn32_2957
            SSE: Ssed_2154 Ssed_3730
            SPL: Spea_3376
            SHE: Shewmr4_0846
            SHM: Shewmr7_3176
            SHN: Shewana3_3274
            SHW: Sputw3181_0990
            CPS: CPS_1148(cobO1) CPS_1164(cobO2)
            PHA: PSHAa2563(btuR)
            PAT: Patl_1134
            SDE: Sde_0629
            PIN: Ping_0213
            MAQ: Maqu_0278
            MCA: MCA2291(cobA)
            TCX: Tcr_1380
            NOC: Noc_0867
            AEH: Mlg_2814
            HHA: Hhal_1908
            HCH: HCH_06467(cobO)
            CSA: Csal_1493
            ABO: ABO_2366(cobO)
            MMW: Mmwyl1_1413 Mmwyl1_2170
            VOK: COSY_0583(cobO)
            CVI: CV_1557(btuR)
            RSO: RSp0616(cobA)
            REU: Reut_A0657
            REH: H16_A2969(btuR)
            RME: Rmet_2786
            BMA: BMA1175(cobO) BMA2416
            BMV: BMASAVP1_A1619(cobO)
            BML: BMA10299_A0281(cobO)
            BMN: BMA10247_0879(cobO)
            BXE: Bxe_B1655
            BVI: Bcep1808_1597
            BUR: Bcep18194_A3822 Bcep18194_A4800
            BCN: Bcen_1172
            BCH: Bcen2424_1652
            BAM: Bamb_1552
            BPS: BPSL1772(cobO) BPSL2841
            BPM: BURPS1710b_2094(cobO) BURPS1710b_3339
            BTE: BTH_I1293 BTH_I2411(cobO)
            RFR: Rfer_2618
            POL: Bpro_2764
            PNA: Pnap_2150
            AAV: Aave_1543
            AJS: Ajs_1102
            VEI: Veis_4777
            MPT: Mpe_B0515(btuR)
            HAR: HEAR0281 HEAR0964(btuR)
            MMS: mma_1095(cobO)
            NEU: NE0634(cobO)
            NET: Neut_1918
            EBA: ebA4023(cobO)
            AZO: azo3552(cobO)
            DAR: Daro_4033
            TBD: Tbd_2718
            MFA: Mfla_0120
            GSU: GSU1577(cobO)
            GME: Gmet_1573
            PCA: Pcar_0482 Pcar_3106
            DVU: DVU1403(cobO)
            DDE: Dde_1669
            DPS: DP2168(cobO)
            SAT: SYN_01073
            SFU: Sfum_1039
            MLO: mll1306
            SME: SMc04302(cobO)
            SMD: Smed_1758
            ATU: Atu2807(cobO)
            ATC: AGR_C_5090
            RET: RHE_CH02488(cobO)
            RLE: RL2829(cobO)
            BME: BMEI0696
            BMF: BAB1_1325(cobO)
            BMS: BR1305(cobO)
            BMB: BruAb1_1306(cobO)
            BOV: BOV_1268(cobO)
            OAN: Oant_1878
            BJA: bll3260(cobO)
            BRA: BRADO4912(cobO) BRADO6493
            BBT: BBta_1139 BBta_3139(cobO)
            RPA: RPA0717(cobO)
            RPB: RPB_0737
            RPC: RPC_3746
            RPD: RPD_0635
            RPE: RPE_2237 RPE_4850
            NWI: Nwi_0752
            XAU: Xaut_3777
            SIL: SPO0262(cobO)
            SIT: TM1040_2207
            RSP: RSP_2831(cobO)
            RSH: Rsph17029_1464
            RSQ: Rsph17025_1514
            JAN: Jann_2935
            RDE: RD1_2181(cobO)
            PDE: Pden_2529
            HNE: HNE_1513(cobO)
            NAR: Saro_0331
            GBE: GbCGDNIH1_0655
            RRU: Rru_A3076 Rru_A3367
            MAG: amb4475
            MGM: Mmc1_0537
            ABA: Acid345_4702
            BPU: BPUM_2969
            GKA: GK1791
            LMO: lmo1181
            LMF: LMOf2365_1191
            LIN: lin1145
            LWE: lwe1139
            CPE: CPE0904(eutT) CPE1908
            CPF: CPF_0897(eutT) CPF_2164
            CPR: CPR_1875
            CTC: CTC00744 CTC00746 CTC02171
            CNO: NT01CX_0356(cobO)
            CDF: CD1919(eutT)
            CBO: CBO0954(btuR)
            CBA: CLB_0996(cobO)
            CBH: CLC_1010(cobO)
            CBF: CLI_1044(cobO)
            CKL: CKL_0715(cobO)
            CHY: CHY_0571 CHY_2619(cobO)
            DSY: DSY1561(cobA) DSY1853(cobA) DSY3879(cobA) DSY4964
            SWO: Swol_0356
            TTE: TTE0370(btuR) TTE0526(btuR2)
            MTA: Moth_1351
            MMO: MMOB0170(btuR)
            MTU: Rv2849c(cobO)
            MTC: MT2915(cobA)
            MBO: Mb2874c(cobO)
            MBB: BCG_2869c(cobO)
            MPA: MAP2918c(cobA)
            MAV: MAV_1529 MAV_3705(cobO)
            MSM: MSMEG_2616(cobO) MSMEG_4934
            MMC: Mmcs_2072
            MKM: Mkms_2118
            MJL: Mjls_2055
            CDI: DIP1489
            NFA: nfa40820(btuR)
            RHA: RHA1_ro06615
            SCO: SCO1851(cobO)
            SMA: SAV6413(cobA)
            PAC: PPA0437
            TFU: Tfu_0312
            FRA: Francci3_2298
            FAL: FRAAL3728(cobO)
            SEN: SACE_5964
            RXY: Rxyl_0637
            FNU: FN0085 FN1790
            TDE: TDE0210(cobO)
            LIL: LB155(cobA)
            LIC: LIC20125(cobO)
            LBJ: LBJ_4187(cobA)
            LBL: LBL_4202(cobA)
            SYN: slr0260(cobO)
            SYW: SYNW0277 SYNW1750(cobO) SYNW2052
            SYC: syc0169_d syc0477_d(cobO) syc0585_c(cobO)
            SYF: Synpcc7942_0957 Synpcc7942_1072 Synpcc7942_1386
            SYD: Syncc9605_0271 Syncc9605_0391 Syncc9605_0713
            SYE: Syncc9902_1646 Syncc9902_1938 Syncc9902_2073
            SYG: sync_0318 sync_0453(cobO-1) sync_2003(cobO-2)
            SYR: SynRCC307_0857(cobO) SynRCC307_2345(cobA)
            SYX: SynWH7803_0321(cobA) SynWH7803_0449 SynWH7803_0641(cobO)
            CYA: CYA_1188(cobO-1) CYA_1205(cobO-2) CYA_1473
            CYB: CYB_1671 CYB_2316(cobO-1) CYB_2588(cobO-2)
            TEL: tlr0265(cobO) tlr0917 tlr2245
            GVI: gll3511 glr0385(cobO) glr4320
            ANA: all0067 all2391 all3802
            AVA: Ava_0207 Ava_1898 Ava_2669
            PMA: Pro0275(ctuR) Pro0523(ctuR) Pro1725(ctuR)
            PMM: PMM0245 PMM0523(cobO) PMM1570
            PMT: PMT1243(cobO) PMT1718 PMT1829
            PMN: PMN2A_1142 PMN2A_1611 PMN2A_1855
            PMI: PMT9312_0247 PMT9312_0523 PMT9312_1662
            PMB: A9601_02671 A9601_05791(cobO)
            PMC: P9515_02781 P9515_05871(cobO)
            PMF: P9303_07631(cobO) P9303_24541
            PMG: P9301_02681 P9301_05491(cobO)
            PMH: P9215_06041(btuR)
            PME: NATL1_03231 NATL1_05801(cobO)
            TER: Tery_0786 Tery_2088 Tery_4685
            CTE: CT0941(btuR)
            CCH: Cag_0753
            PLT: Plut_1137
            DET: DET0245(cobA-1) DET1139(cobA-2) DET1224(cobA-3)
            DEH: cbdb_A1069(cobA) cbdb_A1141(cobA) cbdb_A253(cobA)
            RRS: RoseRS_0557
            RCA: Rcas_0649
            DRA: DR_B0008
            DGE: Dgeo_2362
            TTH: TT_P0002
            TTJ: TTHB044
            TMA: TM1465
            MAC: MA2084
            MBA: Mbar_A1365
            MMA: MM_3138
            MHU: Mhun_0284
            HAL: VNG1574G(cobI)
            HMA: rrnAC1936(cobI)
            HWA: HQ1405A(cobO)
            NPH: NP4974A(cobO)
            TAC: Ta1121
            TVO: TVN1190
            PHO: PH0075
            PAB: PAB2289
            PFU: PF2038
            TKO: TK2130
            APE: APE_0166.1
            PAI: PAE0370
STRUCTURES  PDB: 1G5R  1G5T  1G64  2G2D  2IDX  2NT8  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.17
            ExPASy - ENZYME nomenclature database: 2.5.1.17
            ExplorEnz - The Enzyme Database: 2.5.1.17
            ERGO genome analysis and discovery system: 2.5.1.17
            BRENDA, the Enzyme Database: 2.5.1.17
            CAS: 37277-84-2
///
ENTRY       EC 2.5.1.18                 Enzyme
NAME        glutathione transferase;
            glutathione S-transferase;
            glutathione S-alkyltransferase;
            glutathione S-aryltransferase;
            S-(hydroxyalkyl)glutathione lyase;
            glutathione S-aralkyltransferase;
            glutathione S-alkyl transferase;
            GST
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     RX:glutathione R-transferase
REACTION    RX + glutathione = HX + R-S-glutathione [RN:R03522]
ALL_REAC    R03522 > R07084 R07092 R07093 R07094 R07100 R07116;
            (other) R07002 R07003 R07004 R07023 R07024 R07025 R07026 R07069
            R07070 R07083 R07091 R07113
SUBSTRATE   RX [CPD:C01322];
            glutathione [CPD:C00051]
PRODUCT     HX [CPD:C01318];
            R-S-glutathione [CPD:C02320]
INHIBITOR   S-Hexyl-glutathione [CPD:C02886]
COMMENT     A group of enzymes of broad specificity. R may be an aliphatic,
            aromatic or heterocyclic group; X may be a sulfate, nitrile or
            halide group. Also catalyses the addition of aliphatic epoxides and
            arene oxides to glutathione, the reduction of polyol nitrate by
            glutathione to polyol and nitrile, certain isomerization reactions
            and disulfide interchange.
REFERENCE   1  [PMID:4436300]
  AUTHORS   Habig WH, Pabst MJ, Jakoby WB.
  TITLE     Glutathione S-transferases. The first enzymatic step in mercapturic
            acid formation.
  JOURNAL   J. Biol. Chem. 249 (1974) 7130-9.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:345769]
  AUTHORS   Jakoby WB.
  TITLE     The glutathione S-transferases: a group of multifunctional
            detoxification proteins.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 46 (1978) 383-414.
REFERENCE   3  [PMID:4088070]
  AUTHORS   Jakoby WB.
  TITLE     Glutathione transferases: an overview.
  JOURNAL   Methods. Enzymol. 113 (1985) 495-9.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:670218]
  AUTHORS   Keen JH, Jakoby WB.
  TITLE     Glutathione transferases. Catalysis of nucleophilic reactions of
            glutathione.
  JOURNAL   J. Biol. Chem. 253 (1978) 5654-7.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:11695986]
  AUTHORS   Sheehan D, Meade G, Foley VM, Dowd CA.
  TITLE     Structure, function and evolution of glutathione transferases:
            implications for classification of non-mammalian members of an
            ancient enzyme superfamily.
  JOURNAL   Biochem. J. 360 (2001) 1-16.
  ORGANISM  mouse [GN:mmu], human [GN:hsa]
PATHWAY     PATH: map00480  Glutathione metabolism
            PATH: map00980  Metabolism of xenobiotics by cytochrome P450
ORTHOLOGY   KO: K00799  glutathione S-transferase
GENES       HSA: 119391(GSTO2) 221357(GSTA5) 2938(GSTA1) 2939(GSTA2)
                 2940(GSTA3) 2941(GSTA4) 2944(GSTM1) 2946(GSTM2) 2947(GSTM3)
                 2948(GSTM4) 2949(GSTM5) 2950(GSTP1) 2952(GSTT1) 2953(GSTT2)
                 2954(GSTZ1) 373156(GSTK1) 4257(MGST1) 4258(MGST2) 4259(MGST3)
            PTR: 462769(GSTA2) 462770(GSTA3) 462771(GSTA4) 463802(GSTK1)
                 470264(GSTT1) 473380(MGST1)
            MMU: 14857(Gsta1) 14858(Gsta2) 14859(Gsta3) 14860(Gsta4)
                 14862(Gstm1) 14863(Gstm2) 14864(Gstm3) 14865(Gstm4)
                 14866(Gstm5) 14867(Gstm6) 14869(Gstp2) 14870(Gstp1)
                 14871(Gstt1) 14872(Gstt2) 14873(Gsto1) 14874(Gstz1)
                 56615(Mgst1) 66447(Mgst3) 68214(Gsto2) 68312(Gstm7)
                 76263(Gstk1)
            RNO: 171341(Mgst1) 24421(Gsta3) 24422(Gsta2) 24424(Gstm2)
                 24426(Gstp1) 25260(Gstt1) 29487(Gstt2) 295037(Mgst2_predicted)
                 297029(Gstk1) 57298(Gstm4) 64352(Gstm5) 81869(Gstm3)
            CFA: 474938(GSTA3) 474939(LOC474939) 475518(GSTK1)
                 476005(LOC476005) 476006(LOC476006) 476078(MGST2)
                 477556(GSTT1) 477558(LOC477558) 477683(MGST1)
                 478990(LOC478990) 479911(GSTM3) 479912(GSTM1)
                 480657(LOC480657) 480844(LOC480844) 487023(LOC487023)
                 610304(LOC610304) 611366(LOC611366)
            BTA: 281805(GSTA2) 281806(GSTP1) 327709(GSTM1) 493719(MGST1)
            SSC: 396850(LOC396850) 397117(GSTO1) 397567(MGST1) 397682(GSTA2)
            GGA: 395612(GSTA3) 395976(LOC395976) 396322(GSTT1) 414895(GSTA)
                 414896(GSTA1) 418178(MGST1) 418302(GSTK1) 423374(GSTZ1)
                 424404(MGST3) 770916(MGST2)
            XLA: 379895(gst13-13) 380534(gstm2) 414684(MGC82293)
                 444764(MGC81800)
            XTR: 448387(MGC89299) 448730(mgst3) 496688(gstk1)
                 496690(LOC496690)
            DRE: 324366(gstm) 449784(zgc:101898) 79381(gstp1)
            SPU: 574614(LOC574614) 574739(LOC574739) 579110(LOC579110)
                 579788(LOC579788) 581106(LOC581106) 583081(LOC583081)
                 584003(LOC584003) 588493(LOC588493) 588496(LOC588496)
                 589077(LOC589077) 754063(LOC754063)
            DME: Dmel_CG10045(GstD1) Dmel_CG10091(GstD9) Dmel_CG11512(GstD4)
                 Dmel_CG12242(GstD5) Dmel_CG1742(Mgstl) Dmel_CG17522(GstE10)
                 Dmel_CG17523(GstE2) Dmel_CG17524(GstE3) Dmel_CG17525(GstE4)
                 Dmel_CG17527(GstE5) Dmel_CG17530(GstE6) Dmel_CG17531(GstE7)
                 Dmel_CG17534(GstE9) Dmel_CG18548(GstD10) Dmel_CG33546(gfzf)
                 Dmel_CG4181(GstD2) Dmel_CG4371(GstD7) Dmel_CG4381(GstD3)
                 Dmel_CG4423(GstD6) Dmel_CG5164(GstE1) Dmel_CG8938(GstS1)
                 Dmel_CG9362
            CEL: F11G11.1(gst-8) F11G11.2(gst-7) F11G11.3(gst-6)
                 F35E8.8(gst-38) K08F4.11(gst-3) K08F4.6(gst-2) K08F4.7(gst-4)
                 R03D7.6(gst-5) R07B1.4(gst-36) R107.7(gst-1) Y45G12C.2(gst-10)
                 ZK546.11(gst-30)
            ATH: AT1G02920(ATGSTF7) AT1G02940(ATGSTF5) AT1G02950(ATGSTF4)
                 AT1G65820 AT2G02930(ATGSTF3) AT2G29440(ATGSTU6)
                 AT2G29460(ATGSTU4) AT2G29480(ATGSTU2) AT2G29490(ATGSTU1)
                 AT2G30860(ATGSTF9) AT2G47730(ATGSTF8) AT3G03190(ATGSTF11)
                 AT3G43800(ATGSTU27)
            OSA: 4326828 4332456 4333870 4343183 4349207
            CME: CMQ168C CMS309C CMT103C
            PIC: PICST_28613(GST2) PICST_43969(ECM4) PICST_46914(URE2)
                 PICST_88081(TEF4)
            ANI: AN4905.2 AN6158.2
            AFM: AFUA_1G01370 AFUA_1G17010 AFUA_2G00590 AFUA_3G10830
                 AFUA_6G00760 AFUA_6G03390 AFUA_6G09690 AFUA_7G05500
                 AFUA_7G06460
            AOR: AO090003000212 AO090003000631 AO090005000973 AO090012000378
                 AO090023000149 AO090103000134
            CNE: CNK02140
            UMA: UM01870.1 UM05561.1
            DDI: DDBDRAFT_0167587 DDBDRAFT_0229820 DDB_0231408 DDB_0231430
                 DDB_0231433 DDB_0231516
            PFA: PF13_0214 PF14_0187
            TET: TTHERM_00161470 TTHERM_00316210 TTHERM_00332090
                 TTHERM_00400730 TTHERM_00463010 TTHERM_00518470
                 TTHERM_00569160 TTHERM_00569210 TTHERM_00575360
                 TTHERM_00575390 TTHERM_00630450 TTHERM_00661640
                 TTHERM_00661650 TTHERM_00661660 TTHERM_00924320
            ECO: b1454(yncG) b1635(gst)
            ECJ: JW1449(yncG) JW1627(gst)
            ECE: Z2265 Z2647(gst)
            ECS: ECs2058 ECs2344
            ECC: c1880 c2027(gst)
            ECI: UTI89_C0841(yliJ) UTI89_C1189(grxB) UTI89_C1826(gst)
                 UTI89_C2586(yfcG) UTI89_C3411(yghU) UTI89_C3540(yqjG)
                 UTI89_C3658(sspA) UTI89_C4134(yibF)
            ECP: ECP_1455 ECP_1456 ECP_1580 ECP_2341
            ECV: APECO1_4262(yfcG) APECO1_594 APECO1_718(gst)
            ECW: EcE24377A_1845 EcE24377A_2596 EcE24377A_3456 EcE24377A_4090
            ECX: EcHS_A1711 EcHS_A2452 EcHS_A3169 EcHS_A3798
            STY: STY1671(gst)
            STT: t1319(gst)
            SPT: SPA1402(gst)
            SEC: SC1469(gst)
            STM: STM1451(gst)
            YPE: YPO2367(gst)
            YPK: y1968(gst)
            YPM: YP_2153(gst2)
            YPA: YPA_1713
            YPN: YPN_1824
            YPS: YPTB2281(gst)
            YPI: YpsIP31758_0370 YpsIP31758_1775
            SFL: SF1660(gst)
            SFX: S1792(gst)
            SFV: SFV_1652(gst)
            SSN: SSON_1679
            SBO: SBO_1499(gst) SBO_1593
            SDY: SDY_1858(gst) SDY_1951
            ECA: ECA1587 ECA1938(gst)
            PLU: plu2594(gst)
            SPE: Spro_3136
            HIT: NTHI0201(gst)
            MSU: MS2085(gst)
            APL: APL_1524(gst)
            XFA: XF1210
            XFT: PD0491(gst)
            XCC: XCC0929(gst) XCC1418(gst) XCC1431(gst) XCC2286(gstA)
                 XCC2327(gstA) XCC3073 XCC3766(gst) XCC3962(gst)
            XCB: XC_1085 XC_1789 XC_1829 XC_2807 XC_2820 XC_3306 XC_3837
                 XC_4052
            XCV: XCV0637 XCV0931(gst1) XCV1035(gst2) XCV1348(gst3)
                 XCV1518(gst4) XCV1532(gst5) XCV2591(gst6) XCV2637(gst) XCV3327
                 XCV3944 XCV4137(gst7) XCV4464(gst8)
            XAC: XAC1007(gst) XAC1299(gstA) XAC1461(gst) XAC1474(gst)
                 XAC2230(gst) XAC2394(gstA) XAC2460(gstA) XAC3203 XAC3819(gst)
                 XAC4047(gst) XAC4352(gst)
            XOO: XOO0397(gst) XOO0970(gst) XOO1335 XOO1521(gst) XOO2335(gst)
                 XOO2720(gstA) XOO2765(gstA)
            XOM: XOO_0360(XOO0360) XOO_0885(XOO0885) XOO_1227(XOO1227)
                 XOO_1411(XOO1411) XOO_2215(XOO2215) XOO_2565(XOO2565)
                 XOO_2605(XOO2605)
            VCH: VCA0584
            VVY: VV1856
            VFI: VF1082 VF1083 VFA0821 VFA0849
            PPR: PBPRB0252 PBPRB0681
            PAE: PA1466 PA1623 PA1655 PA1890 PA2813 PA3035
            PAU: PA14_14170 PA14_22530 PA14_24830 PA14_40070 PA14_43110
                 PA14_43530 PA14_45470 PA14_50970(yfcG)
            PPU: PP_1162 PP_1821 PP_2536 PP_4104
            PST: PSPTO_0929(gsT) PSPTO_2032 PSPTO_4777
            PSB: Psyr_1842 Psyr_2499 Psyr_3061
            PSP: PSPPH_1249 PSPPH_1739 PSPPH_1802 PSPPH_2172
            PFL: PFL_1269 PFL_1748 PFL_1771 PFL_2287 PFL_2309 PFL_4361
                 PFL_4586 PFL_4592 PFL_6206
            PFO: Pfl_1214 Pfl_2442 Pfl_3736 Pfl_3752 Pfl_4182 Pfl_5690
            PEN: PSEEN1321 PSEEN1519 PSEEN1595 PSEEN1720 PSEEN2011
                 PSEEN2250(fosA) PSEEN3019 PSEEN3467 PSEEN5149 PSEEN5356
            PAR: Psyc_0418(gst)
            PCR: Pcryo_0668 Pcryo_0878 Pcryo_1254 Pcryo_1722
            ACI: ACIAD0017 ACIAD0159 ACIAD0201 ACIAD0445 ACIAD1305 ACIAD1548
                 ACIAD3051 ACIAD3130
            ACB: A1S_3460
            SON: SO_1576 SO_4697(gst)
            SDN: Sden_0635 Sden_0739 Sden_0764 Sden_3511
            SFR: Sfri_0838 Sfri_1471 Sfri_1613 Sfri_2143 Sfri_2158 Sfri_2771
            SHE: Shewmr4_2696 Shewmr4_3183 Shewmr4_3349 Shewmr4_3840
            SHM: Shewmr7_0604 Shewmr7_0783 Shewmr7_2764 Shewmr7_3933
            SHN: Shewana3_0755 Shewana3_2866 Shewana3_3519 Shewana3_4049
            ILO: IL0046(gst) IL0623
            CPS: CPS_2495 CPS_2673 CPS_2749
            PHA: PSHAa0526 PSHAa2192 PSHAa2489 PSHAb0017 PSHAb0337(maiA)
            PAT: Patl_0196 Patl_0872 Patl_1128 Patl_3957 Patl_3983
            SDE: Sde_0362 Sde_2979 Sde_3206 Sde_3430 Sde_3433 Sde_3528
                 Sde_3827
            LPN: lpg1908(gst) lpg1970
            LPF: lpl1872(gst) lpl1948
            LPP: lpp1883(gst) lpp1953
            MCA: MCA0074(gst) MCA1303(gstB)
            TCX: Tcr_1309
            NOC: Noc_2217
            AEH: Mlg_1459 Mlg_1935
            HCH: HCH_01621(gst) HCH_03323 HCH_03794 HCH_06415 HCH_06491
                 HCH_06725
            CSA: Csal_1012 Csal_2125
            ABO: ABO_0230
            AHA: AHA_0505 AHA_1409 AHA_1712 AHA_2226 AHA_2231 AHA_2308
                 AHA_2659
            DNO: DNO_0086 DNO_0851
            VOK: COSY_0306(gst)
            CVI: CV_0194 CV_0289(gst2) CV_0905 CV_1164(gst1) CV_1775(gst3)
                 CV_2424(gstA) CV_2745 CV_3024 CV_3306 CV_4373
            RSO: RSc0607(RS04835) RSc0817(gst1) RSc0984(RS04308)
                 RSc2021(RS03589) RSc2594(RS00842) RSc2721(RS00001)
                 RSc3070(RS00514) RSc3309(gst2)
            REU: Reut_A1001 Reut_A1486 Reut_A2820 Reut_B3491 Reut_B3493
                 Reut_B4729
            REH: H16_A0066 H16_A0176 H16_A0252 H16_A1090 H16_A1103 H16_A1535
                 H16_A1648 H16_A1801 H16_A2663 H16_A2861 H16_A3125 H16_B0451
                 H16_B0464 H16_B0522 H16_B0571 H16_B0764 H16_B2514
            RME: Rmet_0967 Rmet_0975 Rmet_2514 Rmet_2957 Rmet_4051 Rmet_4929
            BMA: BMA0597 BMA1151 BMA2345 BMA2361(gst-1) BMAA0014
                 BMAA0107(gst-2) BMAA0827
            BMV: BMASAVP1_1164 BMASAVP1_1267(gst-2) BMASAVP1_A0276(gst-1)
                 BMASAVP1_A1591
            BML: BMA10299_1443 BMA10299_A0251 BMA10299_A1137(gst-1)
            BMN: BMA10247_0909 BMA10247_2542(gst-1) BMA10247_A0018
                 BMA10247_A0125(gst-2)
            BXE: Bxe_A0624 Bxe_A1834 Bxe_A1976 Bxe_A2053 Bxe_A2200 Bxe_A2423
                 Bxe_A2900 Bxe_A3350 Bxe_A3446 Bxe_B0273 Bxe_B0925 Bxe_B1268
                 Bxe_C1190(bphK)
            BUR: Bcep18194_A3782 Bcep18194_A4836 Bcep18194_A4988
                 Bcep18194_A5556 Bcep18194_A6295 Bcep18194_A6303
                 Bcep18194_A6379 Bcep18194_B0039 Bcep18194_B0183
                 Bcep18194_B0203 Bcep18194_B1010 Bcep18194_B2137
                 Bcep18194_B2249 Bcep18194_B2348 Bcep18194_B2439
                 Bcep18194_B2557 Bcep18194_B2771 Bcep18194_C7338
                 Bcep18194_C7480 Bcep18194_C7686
            BCN: Bcen_0212 Bcen_1203 Bcen_1616 Bcen_2329 Bcen_2337 Bcen_2808
                 Bcen_4421 Bcen_4517 Bcen_4693 Bcen_4769 Bcen_5390 Bcen_5413
                 Bcen_5777
            BCH: Bcen2424_0298 Bcen2424_0696 Bcen2424_1682 Bcen2424_2226
                 Bcen2424_2228 Bcen2424_2943 Bcen2424_2951 Bcen2424_3398
                 Bcen2424_3670 Bcen2424_3847 Bcen2424_3946 Bcen2424_4742
                 Bcen2424_5448 Bcen2424_5471 Bcen2424_6142
            BAM: Bamb_0589 Bamb_1581 Bamb_2266 Bamb_2990 Bamb_2997 Bamb_3323
                 Bamb_4793 Bamb_5691
            BPS: BPSL1749 BPSL2891 BPSL2906 BPSL2907 BPSS0014 BPSS0640
                 BPSS1374 BPSS1965
            BPM: BURPS1710b_1464 BURPS1710b_2123 BURPS1710b_2840
                 BURPS1710b_3398(gst-1) BURPS1710b_3416 BURPS1710b_3417
                 BURPS1710b_A0400(gst12) BURPS1710b_A1071 BURPS1710b_A1521
                 BURPS1710b_A2204(gst10)
            BPL: BURPS1106A_1980 BURPS1106A_3392 BURPS1106A_A0017
                 BURPS1106A_A1868
            BPD: BURPS668_1961 BURPS668_3356 BURPS668_A0019
                 BURPS668_A1960(gst)
            BTE: BTH_I1237 BTH_I1238 BTH_I1255 BTH_I1781 BTH_I2390 BTH_II0016
                 BTH_II0407 BTH_II0987 BTH_II1768
            BPE: BP1270 BP1300 BP1664(gst)
            BPA: BPP0666(gst) BPP1273 BPP2742(gst) BPP2918 BPP2933
                 BPP2935(gst)
            BBR: BB0673(gst) BB2427 BB2744(gst) BB2888 BB2901 BB2903(gst)
            RFR: Rfer_0047 Rfer_2631 Rfer_3112 Rfer_3730 Rfer_4017 Rfer_4050
            POL: Bpro_0079 Bpro_0243 Bpro_0387 Bpro_0645 Bpro_1375 Bpro_2015
                 Bpro_2962 Bpro_3007 Bpro_4176 Bpro_4241 Bpro_4661 Bpro_5178
                 Bpro_5179
            PNA: Pnap_3984
            AAV: Aave_0798
            AJS: Ajs_3976
            MPT: Mpe_A1954
            HAR: HEAR0313 HEAR1956 HEAR2945
            MMS: mma_0970(gst3) mma_1380(gst4) mma_1676(gst6) mma_3676(gst9)
            NET: Neut_0409 Neut_1354
            NMU: Nmul_A0891 Nmul_A2242
            EBA: ebA1984 ebA3377 ebA3583 ebA5076(gst) ebA6536(gst)
            AZO: azo0113(gstA) azo0361 azo0491(isoJ) azo1541(gst)
                 azo2267(gstB) azo3542
            MFA: Mfla_2116
            BBA: Bd2066 Bd3237(gst) Bd3594(gst)
            ADE: Adeh_3832
            MXA: MXAN_0089 MXAN_0548 MXAN_0864 MXAN_1427 MXAN_4035 MXAN_5252
                 MXAN_5471 MXAN_6122(gst)
            RPR: RP490
            RTY: RT0476
            RCO: RC0782
            RFE: RF_0736
            RBE: RBE_1204
            OTS: OTBS_1589(gst)
            WOL: WD1058
            WBM: Wbm0435
            AMA: AM390(gst)
            ERU: Erum2530
            ERW: ERWE_CDS_02570
            ERG: ERGA_CDS_02530
            ECN: Ecaj_0241
            ECH: ECH_0847
            PUB: SAR11_0628(yfcG)
            MLO: mll2536 mll3731 mll3775 mll4614 mlr0981 mlr1410 mlr2031
                 mlr3345 mlr4635 mlr4954
            MES: Meso_1469 Meso_1689 Meso_2547 Meso_3599
            SME: SMa2319(gst14) SMb20005(gst15) SMb20420 SMb21449(gst12)
                 SMc00036(gst1) SMc00097(gst2) SMc00383(gst3) SMc00407(gst4)
                 SMc00916(gst11) SMc01443(gst6) SMc02390(gst7) SMc04321(gst10)
            ATU: Atu0293 Atu0835(gst) Atu0836(gst) Atu1871(gst) Atu3585
                 Atu3701 Atu5150(attY) Atu5272
            ATC: AGR_C_1527 AGR_C_1530 AGR_C_3433 AGR_C_503 AGR_L_2272
                 AGR_pAT_209 AGR_pAT_394
            RET: RHE_CH00281(gstch1) RHE_CH00309(gstch2) RHE_CH00825(gstch3)
                 RHE_CH01001(gstch4) RHE_CH01147(gstch6) RHE_CH01196(ypch00398)
                 RHE_CH01216 RHE_CH01278(gstA) RHE_CH01482(gstch7)
                 RHE_CH02320(gstch8) RHE_CH02424(gstch9) RHE_PB00095
                 RHE_PE00210(gstE)
            RLE: RL0287 RL0327 RL0349 RL0881 RL1212 RL1284(gstB) RL1288(gst2b)
                 RL1333(gst) RL1348(gstA) RL1425 RL1444 RL1579 RL1590 RL2005
                 RL2633(gstA) RL2759 RL2993(gstA) RL3122(gst) pRL110307
                 pRL90186
            BME: BMEI0517 BMEI1023 BMEI1248 BMEI1316 BMEII0256 BMEII0294
            BMF: BAB1_0649 BAB1_1513 BAB1_1578 BAB2_0230 BAB2_1005
            BMS: BR0626 BR1493 BRA1002 BRA1044
            BMB: BruAb1_0645 BruAb1_0721 BruAb1_1487 BruAb2_0232 BruAb2_0984
            BJA: bll0715 bll1162(attY) bll2508 bll5607 bll5800 bll7404 bll7859
                 bll8133 blr2503(gst) blr4031 blr4332 blr5350 blr6664
            BRA: BRADO0024 BRADO0130 BRADO0334 BRADO0684(maiA) BRADO0749
                 BRADO0990 BRADO1131 BRADO1151 BRADO1164 BRADO1419(gst1)
                 BRADO1844 BRADO2006(gst) BRADO2912 BRADO2929 BRADO3534
                 BRADO3663 BRADO4454 BRADO4559 BRADO4806 BRADO4939 BRADO5020
                 BRADO5718 BRADO5975 BRADO5989 BRADO6428 BRADO6720(gst)
                 BRADO6879
            BBT: BBta_0029 BBta_0222 BBta_0318 BBta_0613 BBta_0670
                 BBta_0818(gst) BBta_1206 BBta_1609 BBta_1788 BBta_1799
                 BBta_1820 BBta_2166 BBta_2328(gst) BBta_2913 BBta_3119
                 BBta_3962 BBta_4031 BBta_4673 BBta_4787 BBta_5247 BBta_5265
                 BBta_5488 BBta_6230 BBta_6685(gst1) BBta_6889 BBta_6902
                 BBta_6917 BBta_7065 BBta_7359 BBta_7500(maiA)
            RPA: RPA0043 RPA0820(gst2) RPA2182 RPA2266(gst1) RPA3880 RPA4103
                 RPA4314(gstA2) RPA4332(gstA1)
            RPB: RPB_0662 RPB_1296 RPB_1311 RPB_2631 RPB_3209 RPB_3767
                 RPB_4144 RPB_4603
            RPC: RPC_0439 RPC_0734 RPC_1528 RPC_3152 RPC_3593 RPC_4124
                 RPC_4135
            RPD: RPD_0171 RPD_0808 RPD_1703 RPD_2246 RPD_3910 RPD_3927
            RPE: RPE_0022 RPE_0254 RPE_0503 RPE_0518 RPE_0675 RPE_1562
                 RPE_2250 RPE_2302 RPE_4164 RPE_4177 RPE_4186 RPE_4187 RPE_4327
            NWI: Nwi_0031 Nwi_0090 Nwi_0164 Nwi_0721 Nwi_2604 Nwi_2981
            NHA: Nham_0039 Nham_0097 Nham_0185 Nham_1101 Nham_2099 Nham_3226
            BHE: BH12430
            BQU: BQ09800
            BBK: BARBAKC583_1050
            CCR: CC_0259 CC_1124 CC_1316 CC_1533 CC_2309 CC_2434 CC_2973
                 CC_3639
            SIL: SPO1191(gst) SPO1324 SPO2163 SPO3261 SPO3306 SPO3494 SPO3764
            SIT: TM1040_0108 TM1040_0209 TM1040_1560 TM1040_1931 TM1040_1961
                 TM1040_2245 TM1040_2825
            RSP: RSP_0897 RSP_1144(gst) RSP_3110 RSP_3111 RSP_3122 RSP_3730
            JAN: Jann_0275 Jann_0322 Jann_0408 Jann_0456 Jann_1148 Jann_2420
                 Jann_2946 Jann_2973
            RDE: RD1_0053 RD1_0058 RD1_0562 RD1_0699(gst) RD1_1133(gst)
                 RD1_1937(gst) RD1_3296(gst) RD1_3971(gst)
            MMR: Mmar10_0117 Mmar10_1107 Mmar10_1112 Mmar10_1322 Mmar10_1820
                 Mmar10_1985 Mmar10_2409
            HNE: HNE_0050 HNE_0132 HNE_0315 HNE_0324 HNE_1014 HNE_1223
                 HNE_2391 HNE_2566 HNE_2762 HNE_2815 HNE_2960 HNE_3104 HNE_3110
                 HNE_3237
            ZMO: ZMO0935(gstA) ZMO1118
            NAR: Saro_2762
            ELI: ELI_00340
            GOX: GOX0399 GOX1372 GOX1932
            GBE: GbCGDNIH1_0168 GbCGDNIH1_0452 GbCGDNIH1_0705 GbCGDNIH1_0799
                 GbCGDNIH1_1353
            RRU: Rru_A0022 Rru_A0332 Rru_A3675
            MAG: amb1272 amb2655 amb3942 amb4311
            MGM: Mmc1_1076
            BCA: BCE_2111(fosB) BCE_2765
            BTL: BALH_2456(fosB)
            BCL: ABC2796(fosB)
            BAY: RBAM_011160(fosB)
            BPU: BPUM_1669
            OIH: OB0825
            SAR: SAR0971
            SAS: SAS0873
            SAA: SAUSA300_2280(fosB)
            SPZ: M5005_Spy_0719
            SPH: MGAS10270_Spy0778
            SPI: MGAS10750_Spy0813
            SPJ: MGAS2096_Spy0791
            SPK: MGAS9429_Spy0775
            SPA: M6_Spy0745
            SPB: M28_Spy0699
            SGO: SGO_1004
            AMT: Amet_2120
            CGB: cg1426
            SEN: SACE_1603 SACE_2873
            RXY: Rxyl_0239 Rxyl_0300
            LIL: LA0595 LA2623 LA3356
            LIC: LIC10807(gst) LIC11363 LIC12981
            SYN: sll0067(gst) sll1147 sll1545(gst1) sll1902
            SYW: SYNW0857 SYNW0931 SYNW1534 SYNW2205
            SYC: syc0295_c(gst) syc0749_d(gst1) syc0765_d syc1953_c
            SYF: Synpcc7942_0771 Synpcc7942_0788 Synpcc7942_1256
                 Synpcc7942_2139
            SYD: Syncc9605_1636 Syncc9605_1783 Syncc9605_2348
            SYE: Syncc9902_0343 Syncc9902_0862 Syncc9902_1396
            SYG: sync_1035 sync_1161 sync_1172 sync_2390 sync_2560
            SYR: SynRCC307_0283(gst) SynRCC307_2304(gst)
            SYX: SynWH7803_2216(gst)
            CYA: CYA_1219
            CYB: CYB_1266
            TEL: tlr0207
            GVI: gll1702 gll1892 gll3020 glr2697 glr3057 glr4372
            ANA: all1124 all1745 all4902 alr3195 alr3798 alr4570 alr4661
            AVA: Ava_0291 Ava_1907 Ava_2002 Ava_2483 Ava_3893 Ava_4693
                 Ava_4998 Ava_5006 Ava_5011
            PMA: Pro0130(gst) Pro0568(gst)
            PMM: PMM0110 PMM0566 PMM0630(GSTTLp28)
            PMT: PMT0471 PMT1025 PMT1961 PMT2104(GSTTLp28)
            PMN: PMN2A_0002 PMN2A_1478
            PMI: PMT9312_0113 PMT9312_0630
            PMB: A9601_01271 A9601_06861
            PMC: P9515_01231 P9515_06961
            PMF: P9303_10551 P9303_26121 P9303_27941
            PMG: P9301_01261 P9301_06571
            PME: NATL1_00391 NATL1_01821 NATL1_06911
            TER: Tery_0356 Tery_2440
STRUCTURES  PDB: 10GS  11GS  12GS  13GS  14GS  16GS  17GS  18GS  19GS  1A0F  
                 1AGS  1AQV  1AQW  1AQX  1AW9  1AXD  1B48  1B4P  1BAY  1C72  
                 1DUG  1E6B  1EOG  1EOH  1EV4  1EV9  1F2E  1F3A  1F3B  1FHE  
                 1FW1  1GLP  1GLQ  1GNE  1GNW  1GSB  1GSC  1GSD  1GSE  1GSF  
                 1GSQ  1GSS  1GSU  1GSY  1GTA  1GTB  1GTI  1GTU  1GUH  1GUK  
                 1GUL  1GUM  1GWC  1HNA  1HNB  1HNC  1JLV  1JLW  1K3L  1K3O  
                 1K3Y  1KBN  1LBK  1LJR  1LQK  1LQO  1LQP  1M0U  1M99  1M9A  
                 1M9B  1MD3  1MD4  1ML6  1MTC  1N2A  1NKI  1NNR  1OE7  1OE8  
                 1OKT  1OYJ  1PGT  1PKW  1PKZ  1PL1  1PL2  1PMT  1PN9  1PX6  
                 1PX7  1R4W  1R5A  1TDI  1TU7  1TU8  1U3I  1U87  1U88  1UA5  
                 1USB  1V2A  1VF1  1VF2  1VF3  1VF4  1XW5  1XW6  1XWG  1XWK  
                 1Y6E  1YDK  1YJ6  1YKC  1YQ1  1YZX  1ZGN  1ZL9  20GS  21GS  
                 22GS  2A2R  2A2S  2AAW  2AB6  2C3N  2C3Q  2C3T  2C4J  2C80  
                 2C8U  2CA8  2CAI  2CAQ  2CZ2  2CZ3  2DC5  2DSA  2F3M  2F8F  
                 2FHE  2GDR  2GLR  2GSQ  2GSR  2GSS  2GST  2GTU  2H8A  2HNL  
                 2IL3  2IMD  2IME  2IMF  2IMI  2IMK  2J9H  2LJR  2NTO  2OA7  
                 2OAC  2OAD  2PGT  2PMT  3FYG  3GSS  3GST  3GTU  3LJR  3PGT  
                 4GSS  4GST  4GTU  4PGT  5FWG  5GSS  5GST  6GSS  6GST  6GSU  
                 6GSV  6GSW  6GSX  6GSY  7GSS  8GSS  9GSS  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.18
            ExPASy - ENZYME nomenclature database: 2.5.1.18
            ExplorEnz - The Enzyme Database: 2.5.1.18
            ERGO genome analysis and discovery system: 2.5.1.18
            BRENDA, the Enzyme Database: 2.5.1.18
            CAS: 50812-37-8
///
ENTRY       EC 2.5.1.19                 Enzyme
NAME        3-phosphoshikimate 1-carboxyvinyltransferase;
            5-enolpyruvylshikimate-3-phosphate synthase;
            3-enolpyruvylshikimate 5-phosphate synthase;
            3-enolpyruvylshikimic acid-5-phosphate synthetase;
            5'-enolpyruvylshikimate-3-phosphate synthase;
            5-enolpyruvyl-3-phosphoshikimate synthase;
            5-enolpyruvylshikimate-3-phosphate synthetase;
            5-enolpyruvylshikimate-3-phosphoric acid synthase;
            enolpyruvylshikimate phosphate synthase;
            EPSP synthase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     phosphoenolpyruvate:3-phosphoshikimate
            5-O-(1-carboxyvinyl)-transferase
REACTION    phosphoenolpyruvate + 3-phosphoshikimate = phosphate +
            5-O-(1-carboxyvinyl)-3-phosphoshikimate [RN:R03460]
ALL_REAC    R03460
SUBSTRATE   phosphoenolpyruvate [CPD:C00074];
            3-phosphoshikimate
PRODUCT     phosphate [CPD:C00009];
            5-O-(1-carboxyvinyl)-3-phosphoshikimate [CPD:C01269]
INHIBITOR   Glyphosate [CPD:C01705]
REFERENCE   1  [PMID:4289188]
  AUTHORS   Morell H, Clark MJ, Knowles PF, Sprinson DB.
  TITLE     The enzymic synthesis of chorismic and prephenic acids from
            3-enolpyruvylshikimic acid 5-phosphate.
  JOURNAL   J. Biol. Chem. 242 (1967) 82-90.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K00800  3-phosphoshikimate 1-carboxyvinyltransferase
GENES       ATH: AT1G48860
            OSA: 4340026
            CME: CMA048C
            SCE: YDR127W(ARO1)
            AGO: AGOS_AGR066W
            CAL: CaO19_4704(CaO19.4704)
            CGR: CAGL0M11484g
            SPO: SPAC1834.02(aro1)
            AFM: AFUA_1G13740
            AOR: AO090012000502
            CNE: CNB01990
            UMA: UM03607.1
            ECO: b0908(aroA)
            ECJ: JW0891(aroA)
            ECE: Z1254(aroA)
            ECS: ECs0991
            ECC: c1046(aroA)
            ECI: UTI89_C0979(aroA)
            ECP: ECP_0919
            ECV: APECO1_20(aroA)
            ECW: EcE24377A_1005(aroA)
            ECX: EcHS_A1014
            STY: STY0978(aroA)
            STT: t1956(aroA)
            SPT: SPA1820(aroA)
            SEC: SC0932(aroA)
            STM: STM0978(aroA)
            YPE: YPO1390(aroA)
            YPK: y2783(aroA)
            YPM: YP_1203(aroA)
            YPA: YPA_0681
            YPN: YPN_2587
            YPP: YPDSF_2305
            YPS: YPTB1415(aroA)
            YPI: YpsIP31758_2582(aroA)
            YEN: YE1538(aroA)
            SFL: SF0903(aroA)
            SFX: S0967(aroA)
            SFV: SFV_0908(aroA)
            SSN: SSON_0909(aroA)
            SBO: SBO_2194(aroA)
            SDY: SDY_2353(aroA)
            ECA: ECA2593(aroA)
            PLU: plu1620(aroA) plu2769
            BUC: BU311(aroA)
            BAS: BUsg301(aroA)
            BAB: bbp288(aroA)
            BCC: BCc_191(aroA)
            SGL: SG0991
            KPN: KPN_00936(aroA)
            BFL: Bfl382(aroA)
            BPN: BPEN_393(aroA)
            HIN: HI1589(aroA)
            HIT: NTHI1462(aroA)
            HIP: CGSHiEE_05570
            HIQ: CGSHiGG_10170
            HDU: HD1383(aroA)
            HSO: HS_0613(aroA)
            PMU: PM0839(aroA)
            MSU: MS1575(aroA)
            APL: APL_0699(aroA)
            XFA: XF2324
            XFT: PD1356(aroA)
            XCC: XCC1591(aroA)
            XCB: XC_2643
            XCV: XCV1691(aroA)
            XAC: XAC1650(aroA)
            XOO: XOO2386(aroA)
            XOM: XOO_2266(XOO2266)
            VCH: VC1732
            VCO: VC0395_A1334(aroA)
            VVU: VV1_2126 VV1_2127
            VVY: VV2318
            VPA: VP1020
            VFI: VF1761
            PPR: PBPRA2452
            PAE: PA3164
            PPU: PP_1770
            PST: PSPTO_1041(aroA) PSPTO_1748
            PSB: Psyr_0888 Psyr_3644
            PSP: PSPPH_0925(aroA) PSPPH_3664
            PFL: PFL_4310 PFL_4652
            PFO: Pfl_4074
            PEN: PSEEN1490
            PAR: Psyc_1184
            PCR: Pcryo_1206
            ACI: ACIAD2222
            SON: SO_2404(aroA)
            SDN: Sden_1751
            SFR: Sfri_2125
            SAZ: Sama_1734
            SBL: Sbal_2068
            SLO: Shew_1952
            SHE: Shewmr4_1922
            SHM: Shewmr7_2056
            SHN: Shewana3_1975
            SHW: Sputw3181_1969
            ILO: IL1357(aroA)
            CPS: CPS_2333(aroA)
            PHA: PSHAa1423(aroA)
            PAT: Patl_2468
            PIN: Ping_1117
            MAQ: Maqu_1025
            CBU: CBU_0526(aroA)
            CBD: COXBU7E912_1537(aroA)
            LPN: lpg1419
            LPF: lpl1370(aroA)
            LPP: lpp1374(aroA)
            MCA: MCA1415(aroA)
            FTU: FTT0588(aroA)
            FTF: FTF0588(aroA)
            FTW: FTW_1141(aroA)
            FTL: FTL_0852
            FTH: FTH_0841(aroA)
            FTA: FTA_0904(aroA)
            FTN: FTN_1091(aroA)
            TCX: Tcr_1196
            NOC: Noc_0177
            AEH: Mlg_0929
            HHA: Hhal_0565
            HCH: HCH_04980(aroA)
            CSA: Csal_2165
            MMW: Mmwyl1_2857
            AHA: AHA_1979(aroA)
            DNO: DNO_0111(aroA)
            BCI: BCI_0253(aroA)
            CRP: CRP_049
            VOK: COSY_0576(aroA)
            NME: NMB1432
            NMA: NMA1644(aroA)
            NMC: NMC1366(aroA)
            NGO: NGO0900
            CVI: CV_3048(aroA)
            RSO: RSc0907(aroA)
            REU: Reut_A2572
            REH: H16_A0795(aroA)
            RME: Rmet_0719
            BMA: BMA0235 BMA0430
            BMV: BMASAVP1_A2574 BMASAVP1_A2711(aroA)
            BML: BMA10299_A0949 BMA10299_A2367(aroA)
            BMN: BMA10247_0199 BMA10247_2447(aroA)
            BXE: Bxe_A0980
            BVI: Bcep1808_0966 Bcep1808_4934
            BUR: Bcep18194_A4158
            BCN: Bcen_0566
            BCH: Bcen2424_1045
            BAM: Bamb_0921
            BPS: BPSL0683 BPSL0684 BPSL2517(aroA)
            BPM: BURPS1710b_0902(aroA) BURPS1710b_0903 BURPS1710b_2996(aroA)
            BPL: BURPS1106A_0734(aroA) BURPS1106A_0735(aroA)
                 BURPS1106A_2947(aroA)
            BPD: BURPS668_0720(aroA) BURPS668_0721(aroA) BURPS668_2884(aroA)
            BTE: BTH_I1636
            PNU: Pnuc_0498
            BPE: BP0948(aroA)
            BPA: BPP3130(aroA)
            BBR: BB3469(aroA)
            RFR: Rfer_1567
            POL: Bpro_1790
            PNA: Pnap_2795
            AAV: Aave_3284
            AJS: Ajs_2468
            VEI: Veis_3123
            MPT: Mpe_A2243
            HAR: HEAR2576(aroA)
            MMS: mma_2670
            NEU: NE1964(aroA)
            NET: Neut_0398
            NMU: Nmul_A2071
            EBA: ebA904(aroO)
            AZO: azo1071(aroA)
            DAR: Daro_1279
            TBD: Tbd_0954
            MFA: Mfla_0929 Mfla_1073
            HPY: HP0401
            HPJ: jhp0980(aroA)
            HPA: HPAG1_0991
            HHE: HH0139(aroA)
            HAC: Hac_0459(aroA)
            WSU: WS1309
            TDN: Tmden_0871
            CJE: Cj0895c(aroA)
            CJR: CJE0974(aroA)
            CJJ: CJJ81176_0904(aroA)
            CJU: C8J_0832(aroA)
            CJD: JJD26997_0918(aroA)
            CFF: CFF8240_1252(aroA)
            CCV: CCV52592_0516(aroA) CCV52592_0971
            CHA: CHAB381_0484(aroA)
            CCO: CCC13826_0485
            ABU: Abu_2051(aroA)
            NIS: NIS_0661(aroA)
            SUN: SUN_0549(aroA)
            GSU: GSU2606(aroA)
            GME: Gmet_0864
            PCA: Pcar_1885
            PPD: Ppro_1347
            DVU: DVU0463(aroA)
            DVL: Dvul_2474
            DDE: Dde_3486
            LIP: LI0781
            BBA: Bd3495(aroA)
            DPS: DP3011
            ADE: Adeh_0184
            MXA: MXAN_3520
            SAT: SYN_01936
            SFU: Sfum_2720 Sfum_2757
            AMA: AM289(rrs)
            APH: APH_1001
            ERU: Erum1880(aroE)
            ERW: ERWE_CDS_01880(aroA)
            ERG: ERGA_CDS_01830(aroA)
            ECN: Ecaj_0188
            ECH: ECH_0920
            NSE: NSE_0180
            PUB: SAR11_0494(aroA)
            MLO: mll5213
            MES: Meso_3609
            SME: SMc00333(aroA)
            SMD: Smed_3456
            ATU: Atu0642(aroA)
            ATC: AGR_C_1140
            RET: RHE_CH00884(aroA)
            RLE: RL0108(aroA) RL0945(aroA)
            BME: BMEI1917
            BMF: BAB1_0023(aroA)
            BMS: BR0025(aroA)
            BMB: BruAb1_0025(aroA)
            BOV: BOV_0024(aroA)
            OAN: Oant_0031
            BJA: blr0738(aroA)
            BRA: BRADO0098(aroA)
            BBT: BBta_0105(aroA) BBta_3803(aroA)
            RPA: RPA0061(aroA)
            RPB: RPB_0643
            RPC: RPC_0400
            RPD: RPD_0189
            RPE: RPE_0444
            NWI: Nwi_0209
            NHA: Nham_0165
            BHE: BH00950(aroA)
            BQU: BQ00880(aroA)
            BBK: BARBAKC583_1303(aroA)
            CCR: CC_3589
            SIL: SPOA0015(aroA)
            SIT: TM1040_0199
            RSP: RSP_3592(aroA)
            RSH: Rsph17029_3277
            JAN: Jann_0708
            RDE: RD1_3914(aroA)
            PDE: Pden_2226
            MMR: Mmar10_0100
            HNE: HNE_0195(aroA)
            ZMO: ZMO1796(aroA)
            NAR: Saro_1326
            SAL: Sala_1493
            SWI: Swit_2458
            ELI: ELI_07490
            GOX: GOX0598
            GBE: GbCGDNIH1_2025
            RRU: Rru_A0295
            MAG: amb4263
            MGM: Mmc1_0174
            ABA: Acid345_3614
            SUS: Acid_7333
            BSU: BG10294(aroE)
            BHA: BH1667(aroE) BH2713
            BAN: BA2953(aroA)
            BAR: GBAA2953(aroA)
            BAA: BA_3462
            BAT: BAS2744
            BCE: BC2938
            BCA: BCE_2994(aroA)
            BCZ: BCZK2673(aroA)
            BTK: BT9727_2694(aroA)
            BTL: BALH_2641(aroA)
            BLI: BL02766(aroEA)
            BLD: BLi02395(aroE)
            BCL: ABC1221 ABC1903(aroE)
            BAY: RBAM_020760
            BPU: BPUM_1991
            OIH: OB1780(aroE)
            GKA: GK2196
            SAU: SA1297(aroA)
            SAV: SAV1464(aroA)
            SAM: MW1354(aroA)
            SAR: SAR1475(aroA)
            SAS: SAS1407
            SAC: SACOL1504(aroA)
            SAB: SAB1328c(aroA)
            SAA: SAUSA300_1355(aroA)
            SAO: SAOUHSC_01481
            SEP: SE1153
            SER: SERP1034(aroA)
            SHA: SH1448(aroA)
            SSP: SSP1280
            LMO: lmo1923(aroE)
            LMF: LMOf2365_1952(aroA)
            LIN: lin2037(aroE)
            LWE: lwe1949(aroA)
            LLA: L0057(aroA)
            LLC: LACR_1907
            LLM: llmg_1926(aroA)
            SPY: SPy_1352(aroA)
            SPZ: M5005_Spy_1101
            SPM: spyM18_1364(aroA)
            SPG: SpyM3_1027(aroA.1)
            SPS: SPs0833
            SPH: MGAS10270_Spy1158
            SPI: MGAS10750_Spy1200
            SPJ: MGAS2096_Spy1163
            SPK: MGAS9429_Spy1145
            SPF: SpyM50758(aroA)
            SPA: M6_Spy1073
            SPB: M28_Spy1093
            SPN: SP_1371
            SPR: spr1229(aroA)
            SPD: SPD_1205(aroA)
            SAG: SAG0630(aroA)
            SAN: gbs0610(aroA)
            SAK: SAK_0715(aroA)
            SMU: SMU.784(aroA)
            STC: str0645(aroA)
            STL: stu0645(aroA)
            SSA: SSA_1464(aroA)
            SGO: SGO_1368(aroA)
            LPL: lp_2035(aroE)
            EFA: EF1566(aroA)
            OOE: OEOE_0152
            STH: STH1419
            CAC: CAC0895(aroA)
            CPE: CPE0696(aroA)
            CPF: CPF_0689(aroA)
            CPR: CPR_0690(aroA)
            CTC: CTC01617
            CNO: NT01CX_0624(aroA)
            CDF: CD1834(aroA)
            CBO: CBO1473(aroA)
            CBA: CLB_1498(aroA)
            CBH: CLC_1510(aroA)
            CBF: CLI_1557(aroA)
            CKL: CKL_0787(aroA)
            CHY: CHY_1928(aroA)
            DSY: DSY2262
            SWO: Swol_1347
            TTE: TTE1015(aroA2)
            MTA: Moth_1332
            MTU: Rv3227(aroA)
            MTC: MT3324(aroA)
            MBO: Mb3256(aroA)
            MBB: BCG_3257(aroA_1) BCG_3350(aroA_2)
            MLE: ML0792(aroA)
            MPA: MAP3334(aroA)
            MAV: MAV_4182(aroA)
            MSM: MSMEG_1890(aroA)
            MVA: Mvan_1771
            MGI: Mflv_4695
            MMC: Mmcs_1362
            MKM: Mkms_1380
            MJL: Mjls_1396
            CGL: NCgl0730(cgl0764)
            CGB: cg0873(aroA)
            CEF: CE0779(aroA)
            CDI: DIP0706(aroA)
            CJK: jk1625(aroA)
            NFA: nfa45890(aroA)
            RHA: RHA1_ro06338(aroA)
            SCO: SCO5212(aroA2) SCO6819(aroA)
            SMA: SAV3042(aroA)
            TWH: TWT567(aroA)
            TWS: TW194(aroA)
            LXX: Lxx19180(aroA)
            CMI: CMM_1318(aroA)
            ART: Arth_2653
            AAU: AAur_2643(aroA)
            PAC: PPA1268
            NCA: Noca_1700
            TFU: Tfu_0544
            FRA: Francci3_3771
            FAL: FRAAL6014(aroA)
            ACE: Acel_0535
            KRA: Krad_1209
            SEN: SACE_6435(aroA)
            STP: Strop_2986 Strop_3718
            BLO: BL0970
            BAD: BAD_0685
            RXY: Rxyl_1441
            FNU: FN0933
            RBA: RB2278
            CTR: CT366(aroA)
            CTA: CTA_0398(aroA)
            CMU: TC0645
            CPN: CPn1039(aroA)
            CPA: CP0813
            CPJ: CPj1039(aroA)
            CPT: CpB1079
            CCA: CCA00723(aroA)
            CAB: CAB690(aroA)
            CFE: CF0293(aroA)
            TDE: TDE1686(aroA)
            LIL: LA1258(aroA)
            LIC: LIC12449(aroA)
            LBJ: LBJ_0934(aroA)
            LBL: LBL_2099(aroA)
            SYN: slr0444(aroA)
            SYW: SYNW1005(aroA)
            SYC: syc1281_d(aroA)
            SYF: Synpcc7942_0232
            SYD: Syncc9605_1131
            SYE: Syncc9902_1326
            SYG: sync_1537(aroA)
            SYR: SynRCC307_1150(aroA)
            SYX: SynWH7803_1032(aroA)
            CYA: CYA_2296(aroA)
            CYB: CYB_1326(aroA)
            TEL: tlr0343(aroA)
            GVI: gll1038(aroA)
            ANA: all5019(aroA)
            AVA: Ava_2259
            PMA: Pro1048(aroA)
            PMM: PMM0613(aroA)
            PMT: PMT0398(aroA)
            PMN: PMN2A_0049
            PMI: PMT9312_0613
            PMB: A9601_06691(aroA)
            PMC: P9515_06781(aroA)
            PMF: P9303_18891(aroA)
            PMG: P9301_06391(aroA)
            PMH: P9215_06951
            PME: NATL1_06701(aroA)
            TER: Tery_4895
            BTH: BT_2186
            BFR: BF0737
            BFS: BF0666(aroA)
            PGI: PG1944(aroA)
            SRU: SRU_0674(aroA)
            CHU: CHU_0717(aroA)
            GFO: GFO_0351(aroA)
            FJO: Fjoh_0508
            FPS: FP0241(aroA)
            CTE: CT1918(aroA)
            CCH: Cag_1631
            CPH: Cpha266_2277
            PVI: Cvib_0349
            PLT: Plut_0284
            DET: DET0463(aroA)
            DEH: cbdb_A427(aroA)
            DRA: DR_1096
            DGE: Dgeo_1001
            TTH: TTC0088
            TTJ: TTHA0457
            AAE: aq_1536(aroA)
            TMA: TM0345
            TPT: Tpet_0575
            MMP: MMP1205(aroA)
            MAC: MA4544(aroA)
            MBA: Mbar_A0891
            MMA: MM_1238
            MBU: Mbur_1078
            MHU: Mhun_1031
            MBN: Mboo_1562
            MST: Msp_0498(aroA)
            MSI: Msm_0273
            MKA: MK0628(aroA)
            HAL: VNG1232G(psc)
            HMA: rrnAC0127(aroA)
            HWA: HQ3358A(aroA)
            NPH: NP3078A(aroA)
            TAC: Ta0282
            TVO: TVN1319
            PTO: PTO0602
            PAB: PAB0306(aroA)
            PFU: PF1699
            TKO: TK0263
            RCI: RCIX508(aroA)
            APE: APE_0569 APE_1404.1
            IHO: Igni_1288
            SSO: SSO0309(aroA)
            STO: ST2277
            SAI: Saci_0188(aroA)
            MSE: Msed_1871
            PAI: PAE1924(aroA)
            PIS: Pisl_1773
            PCL: Pcal_0896
            PAS: Pars_2112
STRUCTURES  PDB: 1G6S  1G6T  1MI4  1P88  1P89  1Q36  1RF4  1RF5  1RF6  1X8R  
                 1X8T  2AA9  2AAY  2BJB  2GG4  2GG6  2GGA  2GGD  2QFQ  2QFS  
                 2QFT  2QFU  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.19
            ExPASy - ENZYME nomenclature database: 2.5.1.19
            ExplorEnz - The Enzyme Database: 2.5.1.19
            ERGO genome analysis and discovery system: 2.5.1.19
            BRENDA, the Enzyme Database: 2.5.1.19
            CAS: 9068-73-9
///
ENTRY       EC 2.5.1.20                 Enzyme
NAME        rubber cis-polyprenylcistransferase;
            rubber allyltransferase;
            rubber transferase;
            isopentenyl pyrophosphate cis-1,4-polyisoprenyl transferase;
            cis-prenyl transferase;
            rubber polymerase;
            rubber prenyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     poly-cis-polyprenyl-diphosphate:isopentenyl-diphosphate
            polyprenylcistransferase
REACTION    poly-cis-polyprenyl diphosphate + isopentenyl diphosphate =
            diphosphate + a poly-cis-polyprenyl diphosphate longer by one C5
            unit [RN:R03917]
ALL_REAC    R03917
SUBSTRATE   poly-cis-polyprenyl diphosphate [CPD:C04093];
            isopentenyl diphosphate [CPD:C00129]
PRODUCT     diphosphate [CPD:C00013];
            poly-cis-polyprenyl diphosphate longer by one C5 unit [CPD:C02321]
COMMENT     Rubber particles act as acceptor.
REFERENCE   1
  AUTHORS   Archer, B.L. and Cockbain, E.G.
  TITLE     Rubber transferase from Hevea brasiliensis latex.
  JOURNAL   Methods Enzymol. 15 (1969) 476-480.
  ORGANISM  Hevea brasiliensis
REFERENCE   2
  AUTHORS   McMullen, A.I. and McSweeney, G.P.
  TITLE     The biosynthesis of rubber. Incorporation of isopentenyl
            pyrophosphate into purified rubber particles by a soluble
            latex-serum enzyme.
  JOURNAL   Biochem. J. 101 (1966) 42-47.
  ORGANISM  Hevea brasiliensis
PATHWAY     PATH: map00100  Biosynthesis of steroids
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.20
            ExPASy - ENZYME nomenclature database: 2.5.1.20
            ExplorEnz - The Enzyme Database: 2.5.1.20
            ERGO genome analysis and discovery system: 2.5.1.20
            BRENDA, the Enzyme Database: 2.5.1.20
            CAS: 62213-41-6
///
ENTRY       EC 2.5.1.21                 Enzyme
NAME        squalene synthase;
            farnesyltransferase;
            presqualene-diphosphate synthase;
            presqualene synthase;
            squalene synthetase;
            farnesyl-diphosphate farnesyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     farnesyl-diphosphate:farnesyl-diphosphate farnesyltransferase
REACTION    (1) 2 farnesyl diphosphate = diphosphate + presqualene diphosphate
            [RN:R00702];
            (2) presqualene diphosphate + NAD(P)H + H+ = squalene + diphosphate
            + NAD(P)+ [RN:R02872]
ALL_REAC    R00702 R02872;
            (other) R06223
SUBSTRATE   farnesyl diphosphate [CPD:C00448];
            presqualene diphosphate [CPD:C03428];
            NADH [CPD:C00004];
            NADPH [CPD:C00005];
            H+ [CPD:C00080]
PRODUCT     diphosphate [CPD:C00013];
            presqualene diphosphate [CPD:C03428];
            squalene [CPD:C00751];
            NAD+ [CPD:C00003];
            NADP+ [CPD:C00006]
INHIBITOR   alpha-Phosphono sulfonate triacid [CPD:C05355]
COMMENT     The enzyme from yeast requires either Mg2+ or Mn2+ for activity. In
            the absence of NAD(P)H, presqualene diphosphate is accumulated.
REFERENCE   1  [PMID:3805037]
  AUTHORS   Kuswik-Rabiega G, Rilling HC.
  TITLE     Squalene synthetase. Solubilization and partial purification of
            squalene synthetase, copurification of presqualene pyrophosphate and
            squalene synthetase activities.
  JOURNAL   J. Biol. Chem. 262 (1987) 1505-9.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:1527001]
  AUTHORS   Ericsson J, Appelkvist EL, Thelin A, Chojnacki T, Dallner G.
  TITLE     Isoprenoid biosynthesis in rat liver peroxisomes. Characterization
            of cis-prenyltransferase and squalene synthetase.
  JOURNAL   J. Biol. Chem. 267 (1992) 18708-14.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:11111077]
  AUTHORS   Tansey TR, Shechter I.
  TITLE     Structure and regulation of mammalian squalene synthase.
  JOURNAL   Biochim. Biophys. Acta. 1529 (2000) 49-62.
  ORGANISM  rat [GN:rno], human [GN:hsa], Arabidopsis thaliana [GN:ath],
            Saccharomyces cerevisiae [GN:sce], Neurospora crassa [GN:dncr]
REFERENCE   4  [PMID:8239656]
  AUTHORS   LoGrasso PV, Soltis DA, Boettcher BR.
  TITLE     Overexpression, purification, and kinetic characterization of a
            carboxyl-terminal-truncated yeast squalene synthetase.
  JOURNAL   Arch. Biochem. Biophys. 307 (1993) 193-9.
  ORGANISM  mammalian, Saccharomyces cerevisiae [GN:sce]
REFERENCE   5  [PMID:1569107]
  AUTHORS   Shechter I, Klinger E, Rucker ML, Engstrom RG, Spirito JA, Islam MA,
            Boettcher BR, Weinstein DB.
  TITLE     Solubilization, purification, and characterization of a truncated
            form of rat hepatic squalene synthetase.
  JOURNAL   J. Biol. Chem. 267 (1992) 8628-35.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00100  Biosynthesis of steroids
            PATH: map00900  Terpenoid biosynthesis
ORTHOLOGY   KO: K00801  farnesyl-diphosphate farnesyltransferase
GENES       HSA: 2222(FDFT1)
            MMU: 14137(Fdft1)
            RNO: 29580(Fdft1)
            CFA: 477362(FDFT1)
            BTA: 281767(FDFT1)
            GGA: 422038(RCJMB04_8p18)
            SPU: 586013(LOC586013)
            ATH: AT4G34650(SQS2)
            OSA: 4334492 4342663
            CME: CMG178C
            SCE: YHR190W(ERG9)
            AGO: AGOS_AFR444C
            PIC: PICST_83429(ERG9)
            CGR: CAGL0M07095g
            SPO: SPBC646.05c(erg9)
            AFM: AFUA_7G01220
            AOR: AO090010000204
            CNE: CNC05660
            UMA: UM04374.1
            DDI: DDB_0231376(fdfT)
            TET: TTHERM_00382150
            TBR: Tb927.8.7120
            TCR: 507897.20 508369.20
            LMA: LmjF31.2940
            NOC: Noc_1321
            CVI: CV_3992(cyoE)
            REH: H16_B0208
            BPM: BURPS1710b_A1762(sqs)
            GBE: GbCGDNIH1_1980
            SYN: sll0513
            ANA: alr1805
            AVA: Ava_4808
            HMA: rrnAC1477(fdfT) rrnAC2069(crtB)
            HWA: HQ2353A(fdfT)
STRUCTURES  PDB: 1D8D  1D8E  1EZF  1KZO  1KZP  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.21
            ExPASy - ENZYME nomenclature database: 2.5.1.21
            ExplorEnz - The Enzyme Database: 2.5.1.21
            ERGO genome analysis and discovery system: 2.5.1.21
            BRENDA, the Enzyme Database: 2.5.1.21
            CAS: 9077-14-9
///
ENTRY       EC 2.5.1.22                 Enzyme
NAME        spermine synthase;
            spermidine aminopropyltransferase;
            spermine synthetase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     S-adenosylmethioninamine:spermidine 3-aminopropyltransferase
REACTION    S-adenosylmethioninamine + spermidine = 5'-methylthioadenosine +
            spermine [RN:R02869]
ALL_REAC    R02869
SUBSTRATE   S-adenosylmethioninamine [CPD:C01137];
            spermidine [CPD:C00315]
PRODUCT     5'-methylthioadenosine [CPD:C00170];
            spermine [CPD:C00750]
COMMENT     This enzyme is not identical with EC 2.5.1.16 (spermidine synthase)
            or EC 2.5.1.23 (sym-norspermidine synthase).
REFERENCE   1  [PMID:7396856]
  AUTHORS   Hibasami H, Borchardt RT, Chen SY, Coward JK, Pegg AE.
  TITLE     Studies of inhibition of rat spermidine synthase and spermine
            synthase.
  JOURNAL   Biochem. J. 187 (1980) 419-28.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:520313]
  AUTHORS   Pajula RL, Raina A, Eloranta T.
  TITLE     Polyamine synthesis in mammalian tissues. Isolation and
            characterization of spermine synthase from bovine brain.
  JOURNAL   Eur. J. Biochem. 101 (1979) 619-26.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00410  beta-Alanine metabolism
ORTHOLOGY   KO: K00802  spermine synthase
GENES       HSA: 6611(SMS)
            PTR: 472307(LOC472307)
            MMU: 20603(Sms)
            RNO: 683008(LOC683008)
            CFA: 480861(SMS)
            BTA: 615950(SMS)
            GGA: 418602(RCJMB04_4b7)
            DRE: 80872(sms)
            SPU: 584264(LOC584264)
            DME: Dmel_CG4300
            SCE: YLR146C(SPE4)
            CGR: CAGL0M04609g
STRUCTURES  PDB: 1UIR  2QFM  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.22
            ExPASy - ENZYME nomenclature database: 2.5.1.22
            ExplorEnz - The Enzyme Database: 2.5.1.22
            ERGO genome analysis and discovery system: 2.5.1.22
            BRENDA, the Enzyme Database: 2.5.1.22
            CAS: 74812-43-4
///
ENTRY       EC 2.5.1.23                 Enzyme
NAME        sym-norspermidine synthase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     S-adenosylmethioninamine:propane-1,3-diamine
            3-aminopropyltransferase
REACTION    S-adenosylmethioninamine + propane-1,3-diamine =
            5'-methylthioadenosine + bis(3-aminopropyl)amine [RN:R03271]
ALL_REAC    R03271
SUBSTRATE   S-adenosylmethioninamine [CPD:C01137];
            propane-1,3-diamine [CPD:C00986]
PRODUCT     5'-methylthioadenosine [CPD:C00170];
            bis(3-aminopropyl)amine [CPD:C03375]
COMMENT     This enzyme is not identical with EC 2.5.1.16 (spermidine synthase)
            or EC 2.5.1.22 (spermine synthase).
REFERENCE   1  [PMID:116684]
  AUTHORS   Aleksijevic A, Grove J, Schuber F.
  TITLE     Studies on polyamine biosynthesis in Euglena gracilis.
  JOURNAL   Biochim. Biophys. Acta. 565 (1979) 199-207.
  ORGANISM  Euglena gracilis
REFERENCE   2
  AUTHORS   Villanueva, V.R., Adlakha, R.C. and Calbayrac, R.
  TITLE     Biosynthesis of polyamines in Euglena gracilis.
  JOURNAL   Phytochemistry 19 (1980) 787-790.
  ORGANISM  Euglena gracilis
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.23
            ExPASy - ENZYME nomenclature database: 2.5.1.23
            ExplorEnz - The Enzyme Database: 2.5.1.23
            ERGO genome analysis and discovery system: 2.5.1.23
            BRENDA, the Enzyme Database: 2.5.1.23
///
ENTRY       EC 2.5.1.24                 Enzyme
NAME        discadenine synthase;
            discadenine synthetase;
            S-adenosyl-L-methionine:6-N-(Delta2-isopentenyl)-adenine
            3-(3-amino-3-carboxypropyl)-transferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     S-adenosyl-L-methionine:N6-(Delta2-isopentenyl)-adenine
            3-(3-amino-3-carboxypropyl)-transferase
REACTION    S-adenosyl-L-methionine + N6-(Delta2-isopentenyl)-adenine =
            5'-methylthioadenosine + discadenine [RN:R03726]
ALL_REAC    R03726
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            N6-(Delta2-isopentenyl)-adenine [CPD:C04083]
PRODUCT     5'-methylthioadenosine [CPD:C00170];
            discadenine [CPD:C01804]
REFERENCE   1  [PMID:566219]
  AUTHORS   Taya Y, Tanaka Y, Nishimura S.
  TITLE     Cell-free biosynthesis of discadenine, a spore germination inhibitor
            of Dictyostelium discoideum.
  JOURNAL   FEBS. Lett. 89 (1978) 326-8.
  ORGANISM  Dictyostelium discoideum [GN:ddi]
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.24
            ExPASy - ENZYME nomenclature database: 2.5.1.24
            ExplorEnz - The Enzyme Database: 2.5.1.24
            ERGO genome analysis and discovery system: 2.5.1.24
            BRENDA, the Enzyme Database: 2.5.1.24
            CAS: 74082-52-3
///
ENTRY       EC 2.5.1.25                 Enzyme
NAME        tRNA-uridine aminocarboxypropyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     S-adenosyl-L-methionine:tRNA-uridine
            3-(3-amino-3-carboxypropyl)transferase
REACTION    S-adenosyl-L-methionine + tRNA uridine = 5'-methylthioadenosine +
            tRNA 3-(3-amino-3-carboxypropyl)-uridine [RN:R03019]
ALL_REAC    R03019
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            tRNA uridine [CPD:C00868]
PRODUCT     5'-methylthioadenosine [CPD:C00170];
            tRNA 3-(3-amino-3-carboxypropyl)-uridine [CPD:C04510]
REFERENCE   1  [PMID:4597321]
  AUTHORS   Nishimura S, Taya Y, Kuchino Y, Oashi Z.
  TITLE     Enzymatic synthesis of 3-(3-amino-3-carboxypropyl)uridine in
            Escherichia coli phenylalanine transfer RNA: transfer of the
            3-amino-acid-3-carboxypropyl group from S-adenosylmethionine.
  JOURNAL   Biochem. Biophys. Res. Commun. 57 (1974) 702-8.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.25
            ExPASy - ENZYME nomenclature database: 2.5.1.25
            ExplorEnz - The Enzyme Database: 2.5.1.25
            ERGO genome analysis and discovery system: 2.5.1.25
            BRENDA, the Enzyme Database: 2.5.1.25
///
ENTRY       EC 2.5.1.26                 Enzyme
NAME        alkylglycerone-phosphate synthase;
            alkyldihydroxyacetonephosphate synthase;
            alkyldihydroxyacetone phosphate synthetase;
            alkyl DHAP synthetase;
            alkyl-DHAP;
            dihydroxyacetone-phosphate acyltransferase;
            DHAP-AT
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     1-acyl-glycerone-3-phosphate:long-chain-alcohol
            O-3-phospho-2-oxopropanyltransferase
REACTION    1-acyl-glycerone 3-phosphate + a long-chain alcohol = an
            alkyl-glycerone 3-phosphate + a long-chain acid anion [RN:R04311]
ALL_REAC    R04311
SUBSTRATE   1-acyl-glycerone 3-phosphate [CPD:C03372];
            long-chain alcohol [CPD:C00339]
PRODUCT     alkyl-glycerone 3-phosphate [CPD:C03715];
            long-chain acid anion [CPD:C03129]
COMMENT     The ester-linked fatty acid of the substrate is cleaved and replaced
            by a long-chain alcohol in an ether linkage.
REFERENCE   1  [PMID:7096336]
  AUTHORS   Brown AJ, Snyder F.
  TITLE     Alkyldihydroxyacetone-P synthase. Solubilization, partial
            purification, new assay method, and evidence for a ping-pong
            mechanism.
  JOURNAL   J. Biol. Chem. 257 (1982) 8835-9.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:4401994]
  AUTHORS   Wykle RL, Plantadosi C, Snyder F.
  TITLE     The role of acyldihydroxyacetone phosphate, reduced nicotinamide
            adenine dinucleotide, and reduced nicotinamide adenine dinucleotide
            phosphate in the biosynthesis of O-alkyl glycerolipids by microsomal
            enzymes of Ehrlich ascites tumor.
  JOURNAL   J. Biol. Chem. 247 (1972) 2944-8.
  ORGANISM  mouse [GN:mmu], guinea pig, rat [GN:rno]
PATHWAY     PATH: map00565  Ether lipid metabolism
ORTHOLOGY   KO: K00803  alkyldihydroxyacetonephosphate synthase
GENES       HSA: 8540(AGPS)
            MMU: 228061(Agps)
            RNO: 84114(Agps)
            CFA: 488421(AGPS)
            GGA: 424135(AGPS)
            XLA: 446408(agps)
            DRE: 386801(agps)
            SPU: 585499(LOC585499)
            DME: Dmel_CG10253
            CEL: Y50D7A.7(ads-1)
            DDI: DDB_0191146(eapA)
            TBR: Tb927.6.1500
            TCR: 503815.10 505807.110
            LMA: LmjF30.0120
            SPE: Spro_2461
            PFL: PFL_2767
            ABO: ABO_1409
            REH: H16_B1197
            RME: Rmet_5443
            BUR: Bcep18194_B2080
            RFR: Rfer_2332
            POL: Bpro_5107
            PLA: Plav_1669
            RPD: RPD_1036
            MTU: Rv2250A Rv2251 Rv3107c(agpS)
            MTC: MT2311 MT3190
            MBO: Mb2275 Mb3134c(agpS)
            MBB: BCG_3132c(agpS)
            MPA: MAP2004
            MVA: Mvan_3761
            MGI: Mflv_2772
            MMC: Mmcs_3374
            MKM: Mkms_3436
            MJL: Mjls_3385
            NFA: nfa13450
            RHA: RHA1_ro05090
            SCO: SCO0668(SCF91.28c)
            FRA: Francci3_0943 Francci3_2658
            FAL: FRAAL1575
            SEN: SACE_0660 SACE_3960
            STP: Strop_2577
            TDE: TDE0138
            LIL: LA2262(adaS)
            LIC: LIC11674
            APE: APE_0308.1
            SSO: SSO1531
            SAI: Saci_1188
            TPE: Tpen_1372
STRUCTURES  PDB: 2UUU  2UUV  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.26
            ExPASy - ENZYME nomenclature database: 2.5.1.26
            ExplorEnz - The Enzyme Database: 2.5.1.26
            ERGO genome analysis and discovery system: 2.5.1.26
            BRENDA, the Enzyme Database: 2.5.1.26
            CAS: 102484-74-2
///
ENTRY       EC 2.5.1.27                 Enzyme
NAME        adenylate dimethylallyltransferase;
            cytokinin synthase;
            isopentenyltransferase;
            2-isopentenyl-diphosphate:AMP Delta2-isopentenyltransferase;
            adenylate isopentenyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     dimethylallyl-diphosphate:AMP dimethylallyltransferase
REACTION    dimethylallyl diphosphate + AMP = diphosphate +
            N6-(dimethylallyl)adenosine 5'-phosphate [RN:R04038]
ALL_REAC    R04038
SUBSTRATE   dimethylallyl diphosphate [CPD:C00235];
            AMP [CPD:C00020]
PRODUCT     diphosphate [CPD:C00013];
            N6-(dimethylallyl)adenosine 5'-phosphate [CPD:C04713]
REFERENCE   1  [PMID:499537]
  AUTHORS   Chen CM, Melitz DK.
  TITLE     Cytokinin biosynthesis in a cell-free system from
            cytokinin-autotrophic tobacco tissue cultures.
  JOURNAL   FEBS. Lett. 107 (1979) 15-20.
  ORGANISM  Nicotiana tabacum
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.27
            ExPASy - ENZYME nomenclature database: 2.5.1.27
            ExplorEnz - The Enzyme Database: 2.5.1.27
            ERGO genome analysis and discovery system: 2.5.1.27
            BRENDA, the Enzyme Database: 2.5.1.27
            CAS: 72840-95-0
///
ENTRY       EC 2.5.1.28                 Enzyme
NAME        dimethylallylcistransferase;
            neryl-diphosphate synthase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     dimethylallyl-diphosphate:isopentenyl-diphosphate
            dimethylallylcistransferase
REACTION    dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate +
            neryl diphosphate [RN:R01659]
ALL_REAC    R01659
SUBSTRATE   dimethylallyl diphosphate [CPD:C00235];
            isopentenyl diphosphate [CPD:C00129]
PRODUCT     diphosphate [CPD:C00013];
            neryl diphosphate [CPD:C02569]
COMMENT     This enzyme will not use larger prenyl diphosphates as efficient
            donors.
REFERENCE   1
  AUTHORS   Banthorpe, D.V., Bucknall, G.A., Doonan, H.J., Doonan, S. and Rowan,
            M.G.
  TITLE     Biosynthesis of geraniol and nerol in cell-free extracts of
            Tanacetum vulgare.
  JOURNAL   Phytochemistry 15 (1976) 91-100.
  ORGANISM  Tanacetum vulgare
REFERENCE   2  [PMID:11633027]
  AUTHORS   Beyt JP.
  TITLE     [Not Available.]
  JOURNAL   Rev. Nord. 65 (1983) 683-9.
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.28
            ExPASy - ENZYME nomenclature database: 2.5.1.28
            ExplorEnz - The Enzyme Database: 2.5.1.28
            ERGO genome analysis and discovery system: 2.5.1.28
            BRENDA, the Enzyme Database: 2.5.1.28
            CAS: 9032-79-5
///
ENTRY       EC 2.5.1.29                 Enzyme
NAME        farnesyltranstransferase;
            geranylgeranyl-diphosphate synthase;
            geranylgeranyl pyrophosphate synthetase;
            geranylgeranyl-PP synthetase;
            farnesyltransferase;
            geranylgeranyl pyrophosphate synthase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     trans,trans-farnesyl-diphosphate:isopentenyl-diphosphate
            farnesyltranstransferase
REACTION    trans,trans-farnesyl diphosphate + isopentenyl diphosphate =
            diphosphate + geranylgeranyl diphosphate [RN:R02061]
ALL_REAC    R02061;
            (other) R01658 R02003
SUBSTRATE   trans,trans-farnesyl diphosphate [CPD:C00448];
            isopentenyl diphosphate [CPD:C00129]
PRODUCT     diphosphate [CPD:C00013];
            geranylgeranyl diphosphate [CPD:C00353]
COMMENT     Some forms of this enzyme will also use geranyl diphosphate and
            dimethylallyl diphosphate as donors; it will not use larger prenyl
            diphosphates as efficient donors.
REFERENCE   1
  AUTHORS   Sagami, H., Ishi, K. and Ogura, K.
  TITLE     Occurrence and unusual properties of geranylgeranyl pyrophosphate
            synthetase of pig liver.
  JOURNAL   Biochem. Int. 3 (1981) 669-675.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00100  Biosynthesis of steroids
            PATH: map00900  Terpenoid biosynthesis
ORTHOLOGY   KO: K00804  geranylgeranyl pyrophosphate synthetase
GENES       HSA: 9453(GGPS1)
            MMU: 14593(Ggps1)
            CFA: 479198(GGPS1)
            BTA: 780882(GGPS1)
            GGA: 427092(GGPS1)
            DRE: 336798(ggps1)
            DME: Dmel_CG8593(qm)
            ATH: AT2G18620 AT3G14530 AT3G14550(GGPS3) AT3G20160 AT3G29430
                 AT3G32040
            OSA: 4343721
            CME: CMK058C
            SCE: YPL069C(BTS1)
            AGO: AGOS_AEL238C
            PIC: PICST_32799(BET4) PICST_46658(BTS1) PICST_55783(RAM2)
            CAL: CaO19.6674(bts1)
            CGR: CAGL0H05269g
            CNE: CNI00090
            UMA: UM04459.1
            DDI: DDB_0233098
            VFI: VF0712
            MAQ: Maqu_0854
            NOC: Noc_2231
            PNU: Pnuc_0193
            RFR: Rfer_1267
            NET: Neut_0825
            NMU: Nmul_A1814
            DPS: DP2699
            ADE: Adeh_0378
            SAT: SYN_02457 SYN_03252
            RET: RHE_PD00244(ctrE)
            BRA: BRADO1615(crtE) BRADO6509(crtE)
            BBT: BBta_6440(crtE)
            RPA: RPA1519(crtE)
            RPB: RPB_4004
            RPC: RPC_1290
            RPD: RPD_3759
            RPE: RPE_1324
            NWI: Nwi_2592
            NHA: Nham_3215
            RDE: RD1_0114(crtE)
            RRU: Rru_A2983
            ABA: Acid345_3432
            LSL: LSL_1028
            LDB: Ldb1422(crtE)
            STH: STH1844
            CTC: CTC01577
            TTE: TTE1296(ispA)
            MTU: Rv3398c(idsA1)
            MTC: MT3506
            MBO: Mb3431c(idsA1)
            MBB: BCG_3468c(idsA1)
            SCO: SCO6763(SC6A5.12)
            SMA: SAV2997(ptlB)
            FRA: Francci3_0822
            FAL: FRAAL1431(fppS)
            SEN: SACE_3979 SACE_4328 SACE_4646(ptlB) SACE_4909 SACE_5289
            CTA: CTA_0681(ispA)
            PCU: pc1696(crtE)
            SYN: slr0739(crtE)
            SYW: SYNW0742(crtE)
            SYC: syc0760_d(crtE)
            SYF: Synpcc7942_0776
            SYD: Syncc9605_1926
            SYE: Syncc9902_0739
            SYG: sync_0991(crtE)
            SYR: SynRCC307_0751(crtE)
            SYX: SynWH7803_1569(crtE)
            CYA: CYA_0377(crtE)
            CYB: CYB_1859(crtE)
            TEL: tll0020(crtE)
            GVI: gll0416(crtE)
            ANA: alr0213(crtE)
            AVA: Ava_2704
            PMA: Pro1042(crtE) Pro1129(ispA)
            PMM: PMM1070(crtE)
            PMT: PMT1109(crtE)
            PMN: PMN2A_0681
            PMB: A9601_06741(sds) A9601_11751(ispA)
            PMC: P9515_06831(sds) P9515_11601(ispA)
            PMF: P9303_09331(ispA) P9303_18951(sds)
            PMG: P9301_06441(sds) P9301_11761(ispA)
            PME: NATL1_06761(sds) NATL1_15151(ispA)
            TER: Tery_4173
            MBU: Mbur_2399
            MTP: Mthe_0472
            MHU: Mhun_2886
            MBN: Mboo_2209
            HWA: HQ2889A(idsA)
            NPH: NP3696A(idsA_3)
            PTO: PTO1199
            RCI: RCIX2437(crtE)
            SSO: SSO0061(gds-1)
            STO: ST2058
            SAI: Saci_0092(gds)
STRUCTURES  PDB: 2DH4  2Q80  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.29
            ExPASy - ENZYME nomenclature database: 2.5.1.29
            ExplorEnz - The Enzyme Database: 2.5.1.29
            ERGO genome analysis and discovery system: 2.5.1.29
            BRENDA, the Enzyme Database: 2.5.1.29
            CAS: 9032-58-0
///
ENTRY       EC 2.5.1.30                 Enzyme
NAME        trans-hexaprenyltranstransferase;
            all-trans-heptaprenyl-diphosphate synthase;
            heptaprenyl pyrophosphate synthase;
            heptaprenyl diphosphate synthase;
            heptaprenyl pyrophosphate synthetase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     all-trans-hexaprenyl-diphosphate:isopentenyl-diphosphate
            hexaprenyltranstransferase
REACTION    all-trans-hexaprenyl diphosphate + isopentenyl diphosphate =
            diphosphate + all-trans-heptaprenyl diphosphate [RN:R05612]
ALL_REAC    R05612
SUBSTRATE   all-trans-hexaprenyl diphosphate [CPD:C01230];
            isopentenyl diphosphate [CPD:C00129]
PRODUCT     diphosphate [CPD:C00013];
            all-trans-heptaprenyl diphosphate [CPD:C04216]
COMMENT     This enzyme will also use trans-trans-farnesyl diphosphate and
            all-trans-prenyl diphosphates of intermediate size as donors, but
            not dimethylallyl diphosphate.
REFERENCE   1  [PMID:6768722]
  AUTHORS   Takahashi I, Ogura K, Seto S.
  TITLE     Heptaprenyl pyrophosphate synthetase from Bacillus subtilis.
  JOURNAL   J. Biol. Chem. 255 (1980) 4539-43.
  ORGANISM  Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K00805  trans-hexaprenyltranstransferase
GENES       YPP: YPDSF_3562
            ENT: Ent638_3623
            PCR: Pcryo_1756
            SFR: Sfri_3090
            SAZ: Sama_2830
            SBL: Sbal_0966
            SLO: Shew_0868
            SPC: Sputcn32_0978
            SHE: Shewmr4_0894
            SHM: Shewmr7_3126
            SHW: Sputw3181_3189
            PAT: Patl_3739
            SDE: Sde_1007
            PIN: Ping_0524
            TCX: Tcr_0340
            NOC: Noc_3032
            AEH: Mlg_0833
            HHA: Hhal_1849
            CSA: Csal_0473
            VOK: COSY_0337(ispB)
            REU: Reut_A2959
            REH: H16_A3253(grcC)
            BVI: Bcep1808_0556
            BUR: Bcep18194_A3665
            BCH: Bcen2424_0580
            BAM: Bamb_0483
            POL: Bpro_0840
            PNA: Pnap_0752
            AAV: Aave_3676
            HAR: HEAR2788(ispB)
            AZO: azo0401
            MFA: Mfla_2220
            PPD: Ppro_2007
            DVL: Dvul_0208
            DDE: Dde_3189
            SFU: Sfum_1586
            RSH: Rsph17029_2406
            JAN: Jann_0487
            RDE: RD1_3401(ispB)
            PDE: Pden_2031
            MMR: Mmar10_2184
            MGM: Mmc1_3354
            ABA: Acid345_2027
            BSU: BG10279(hepB) BG10281(hepA)
            BHA: BH1648(gerCA) BH1653(gerCC)
            BAN: BA1533 BA1535(hepT)
            BAR: GBAA1533 GBAA1535(hepT)
            BAA: BA_2053 BA_2055
            BAT: BAS1422 BAS1424
            BCE: BC1512 BC1514
            BCA: BCE_1639 BCE_1641(hepT)
            BCZ: BCZK1394(hepS) BCZK1396(hepT)
            BTK: BT9727_1394(hepS) BT9727_1396(hepT)
            BTL: BALH_1368(hepT)
            BLI: BL02782(hepT) BL02784(hepS)
            BLD: BLi02409(hepT) BLi02411(hepS)
            BCL: ABC1885 ABC1889(hepA)
            BAY: RBAM_020900(hepT) RBAM_020920(hepS)
            BPU: BPUM_2005(hepT) BPUM_2007(hepS)
            OIH: OB1788(gerCC) OB1790(gerCA)
            GKA: GK2210(gerCC) GK2212(gerCA)
            SAU: SA1302(gerCC)
            SAV: SAV1470(gerCC)
            SAM: MW1359(gerCC)
            SAR: SAR1479
            SAS: SAS1411
            SAC: SACOL1510
            SAB: SAB1332c
            SAA: SAUSA300_1359
            SAO: SAOUHSC_01486
            SEP: SE1157
            SER: SERP1038
            SHA: SH1444(gerCC)
            SSP: SSP1276
            LMO: lmo1930
            LMF: LMOf2365_1959(hepB)
            LIN: lin2044
            LWE: lwe1956(hepB) lwe1958(hepS) lwe2591
            LLC: LACR_0190
            LLM: llmg_0196 llmg_1110(ispB) llmg_1111(gerCA)
            LPL: lp_1066(hepB1) lp_1134(hepB2)
            LSL: LSL_1028
            LCA: LSEI_2300
            STH: STH190
            CTC: CTC01025
            CTH: Cthe_0564
            CHY: CHY_1206(hepT)
            DSY: DSY2232
            DRM: Dred_2166
            SWO: Swol_0680
            MTA: Moth_1252
            MTC: MT0588 MT1018
            MBO: Mb0577(grcC1) Mb1016c(grcC2)
            MLE: ML2277
            MPA: MAP4058(grcC1)
            MVA: Mvan_0992
            MGI: Mflv_5253
            MMC: Mmcs_0771
            MKM: Mkms_0785
            MJL: Mjls_0766
            CGL: NCgl0456(cgl0473)
            CGB: cg0559(ispB) cg2384(idsA)
            CEF: CE0483
            CDI: DIP0429
            CJK: jk1863
            NFA: nfa51220
            RHA: RHA1_ro01991
            SCO: SCO4583(SCD20.01)
            SMA: SAV4864(grcC)
            TWH: TWT054(grcC)
            TWS: TW064
            LXX: Lxx01830(hepB)
            ART: Arth_3130
            AAU: AAur_3100
            PAC: PPA1921
            NCA: Noca_0534
            TFU: Tfu_2681
            FRA: Francci3_0552
            FAL: FRAAL1046
            ACE: Acel_0281
            SEN: SACE_6888
            RXY: Rxyl_1972
            FNU: FN1541
            SYF: Synpcc7942_2362
            SYD: Syncc9605_1137
            SYE: Syncc9902_1320
            AVA: Ava_1469
            PMN: PMN2A_0055
            PMI: PMT9312_0618
            PMB: A9601_06741(sds)
            PMC: P9515_06831(sds)
            PMF: P9303_18951(sds)
            PMG: P9301_06441(sds)
            PME: NATL1_06761(sds)
            TER: Tery_0157
            CCH: Cag_0963
            CPH: Cpha266_0988
            PLT: Plut_1219
            DET: DET0389(hepT)
            DEH: cbdb_A335(hepT)
STRUCTURES  PDB: 2E8T  2E8U  2E8V  2E8W  2E8X  2E90  2E91  2E92  2E93  2E94  
                 2E95  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.30
            ExPASy - ENZYME nomenclature database: 2.5.1.30
            ExplorEnz - The Enzyme Database: 2.5.1.30
            ERGO genome analysis and discovery system: 2.5.1.30
            BRENDA, the Enzyme Database: 2.5.1.30
            CAS: 74506-59-5
///
ENTRY       EC 2.5.1.31                 Enzyme
NAME        di-trans,poly-cis-decaprenylcistransferase;
            di-trans,poly-cis-undecaprenyl-diphosphate synthase;
            undecaprenyl-diphosphate synthase;
            bactoprenyl-diphosphate synthase;
            UPP synthetase;
            undecaprenyl diphosphate synthetase;
            undecaprenyl pyrophosphate synthetase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     di-trans,poly-cis-decaprenyl-diphosphate:isopentenyl-diphosphate
            undecaprenylcistransferase
REACTION    di-trans,poly-cis-decaprenyl diphosphate + isopentenyl diphosphate =
            diphosphate + di-trans,poly-cis-undecaprenyl diphosphate [RN:R07269]
ALL_REAC    R07269;
            (other) R06447
SUBSTRATE   di-trans,poly-cis-decaprenyl diphosphate [CPD:C04509];
            isopentenyl diphosphate [CPD:C00129]
PRODUCT     diphosphate [CPD:C00013];
            di-trans,poly-cis-undecaprenyl diphosphate [CPD:C04574]
COMMENT     This enzyme will also use trans,trans-farnesyl diphosphate and
            di-trans,poly-cis-prenyl diphosphates of intermediate size as
            donors. The two trans- bonds in the substrate and product are those
            furthest from the diphosphate group.
REFERENCE   1  [PMID:6712246]
  AUTHORS   Muth JD, Allen CM.
  TITLE     Undecaprenyl pyrophosphate synthetase from Lactobacillus plantarum:
            a dimeric protein.
  JOURNAL   Arch. Biochem. Biophys. 230 (1984) 49-60.
  ORGANISM  Lactobacillus plantarum [GN:lpl]
REFERENCE   2  [PMID:6818223]
  AUTHORS   Takahashi I, Ogura K.
  TITLE     Prenyltransferases of Bacillus subtilis: undecaprenyl pyrophosphate
            synthetase and geranylgeranyl pyrophosphate synthetase.
  JOURNAL   J. Biochem. (Tokyo). 92 (1982) 1527-37.
  ORGANISM  Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00900  Terpenoid biosynthesis
ORTHOLOGY   KO: K00806  undecaprenyl pyrophosphate synthetase
GENES       ATH: AT2G23410(ACPT) AT5G58770
            OSA: 4324755
            PIC: PICST_29164(SRT1)
            AFM: AFUA_4G11350
            UMA: UM01380.1
            CPV: cgd4_1510
            TPV: TP03_0421
            TET: TTHERM_00243950
            TBR: Tb927.7.5880
            TCR: 508173.60
            LMA: LmjF13.0020
            ECO: b0174(uppS)
            ECJ: JW0169(ispU)
            ECE: Z0185(yaeS)
            ECS: ECs0176
            ECC: c0211(yaeS)
            ECI: UTI89_C0189(uppS)
            ECP: ECP_0182
            ECV: APECO1_1813
            ECW: EcE24377A_0178(uppS)
            ECX: EcHS_A0176(uppS)
            STY: STY0244
            STT: t0222
            SPT: SPA0228(uppS)
            SEC: SC0221(uppS)
            STM: STM0221(uppS)
            YPE: YPO1049(uppS)
            YPK: y3130
            YPM: YP_2801(uppS)
            YPA: YPA_0525
            YPN: YPN_2951
            YPP: YPDSF_1663
            YPS: YPTB2998(uppS)
            YPI: YpsIP31758_1018(uppS)
            SFL: SF0164(yaeS)
            SFX: S0167(yaeS)
            SFV: SFV_0157(yaeS)
            SSN: SSON_0186(yaeS)
            SBO: SBO_0162(yaeS)
            SDY: SDY_0190(yaeS)
            ECA: ECA1036(uppS)
            PLU: plu0677(uppS)
            BUC: BU236(uppS)
            BAS: BUsg230(uppS)
            BAB: bbp218(uppS)
            WBR: WGLp387(yaeS)
            SGL: SG1938
            ENT: Ent638_0712
            SPE: Spro_3785
            BFL: Bfl276(uppS)
            BPN: BPEN_284(uppS)
            HIN: HI0920
            HIT: NTHI1088(uppS)
            HDU: HD1196(uppS)
            HSO: HS_0983(uppS)
            PMU: PM1989
            MSU: MS1927(uppS)
            APL: APL_0414(uppS)
            ASU: Asuc_1967
            XFA: XF1050
            XFT: PD0330(uppS)
            XCC: XCC1369(uppS)
            XCB: XC_2869
            XCV: XCV1474(uppS)
            XAC: XAC1417(uppS)
            XOO: XOO1972(uppS)
            XOM: XOO_1862(XOO1862)
            VCH: VC2256
            VCO: VC0395_A1847(uppS)
            VVU: VV1_1864
            VVY: VV2553
            VPA: VP2314
            VFI: VF1958
            PPR: PBPRA2964
            PAE: PA3652(uppS)
            PAU: PA14_17110(uppS)
            PAP: PSPA7_1487(uppS)
            PPU: PP_1595(uppS)
            PPF: Pput_4182
            PST: PSPTO_1538(uppS)
            PSB: Psyr_1347
            PSP: PSPPH_3836(uppS)
            PFL: PFL_1180(uppS)
            PFO: Pfl_1105
            PEN: PSEEN4216(uppS)
            PMY: Pmen_3049
            PAR: Psyc_1533(uppS)
            PCR: Pcryo_1712
            PRW: PsycPRwf_1800
            ACI: ACIAD1374(ispU)
            SON: SO_1633(uppS)
            SDN: Sden_1558
            SFR: Sfri_1274
            SAZ: Sama_1143
            SBL: Sbal_1454
            SBM: Shew185_1449
            SLO: Shew_2631
            SPC: Sputcn32_1352
            SSE: Ssed_3157
            SPL: Spea_2881
            SHE: Shewmr4_2637
            SHM: Shewmr7_2704
            SHN: Shewana3_2811
            SHW: Sputw3181_2751
            ILO: IL0841(uppS)
            CPS: CPS_1557(uppS)
            PHA: PSHAa2032(ispU)
            PAT: Patl_1253
            SDE: Sde_2593
            PIN: Ping_2972
            MAQ: Maqu_2544
            CBU: CBU_1382(uppS)
            CBD: COXBU7E912_0612(uppS)
            LPN: lpg0503(uppS)
            LPF: lpl0542(uppS)
            LPP: lpp0566(uppS)
            MCA: MCA0571(uppS)
            FTU: FTT0317(uppS)
            FTF: FTF0317(uppS)
            FTW: FTW_1765(uppS)
            FTL: FTL_0228
            FTH: FTH_0223(uppS)
            FTA: FTA_0244(uppS)
            FTN: FTN_0231(uppS)
            TCX: Tcr_1281
            NOC: Noc_0812
            AEH: Mlg_1859
            HHA: Hhal_1462
            HCH: HCH_05248(uppS)
            CSA: Csal_0567
            ABO: ABO_1147(uppS)
            MMW: Mmwyl1_1276
            AHA: AHA_1177(uppS)
            DNO: DNO_0719(uppS)
            BCI: BCI_0532(uppS)
            RMA: Rmag_0027
            VOK: COSY_0027(uppS)
            NME: NMB0186
            NMA: NMA0081(uppS)
            NMC: NMC0177(uppS)
            NGO: NGO1797
            CVI: CV_2200(uppS)
            RSO: RSc1408(uppS)
            REU: Reut_A1877
            REH: H16_A2051(uppS)
            RME: Rmet_1439
            BMA: BMA1551(uppS)
            BMV: BMASAVP1_A2052(uppS)
            BML: BMA10299_A3259(uppS)
            BMN: BMA10247_1324(uppS)
            BXE: Bxe_A1686
            BVI: Bcep1808_1921
            BUR: Bcep18194_A5325
            BCN: Bcen_6062
            BCH: Bcen2424_2015
            BAM: Bamb_2048
            BPS: BPSL2155(uppS)
            BPM: BURPS1710b_2579(uppS)
            BPL: BURPS1106A_2489(uppS)
            BPD: BURPS668_2433(uppS)
            BTE: BTH_I2031(uppS)
            PNU: Pnuc_1447
            BPE: BP1423(uppS)
            BPA: BPP1531(uppS)
            BBR: BB2609(uppS)
            RFR: Rfer_2675
            POL: Bpro_2691
            PNA: Pnap_1762 Pnap_3193
            AAV: Aave_1827
            AJS: Ajs_2581
            VEI: Veis_1442
            MPT: Mpe_A1975
            HAR: HEAR1339(ispU)
            MMS: mma_2054(uppS)
            NEU: NE1714
            NET: Neut_2031
            NMU: Nmul_A0661
            EBA: ebA5991(uppS)
            AZO: azo1905(uppS)
            DAR: Daro_1746
            TBD: Tbd_0789
            MFA: Mfla_1526
            HPY: HP1221
            HPJ: jhp1142
            HPA: HPAG1_1163
            HHE: HH1093
            HAC: Hac_1597(uppS)
            WSU: WS2058(uppS)
            TDN: Tmden_0997
            CJE: Cj0824(uppS)
            CJR: CJE0911(uppS)
            CJJ: CJJ81176_0841(uppS)
            CJU: C8J_0771(uppS)
            CJD: JJD26997_1190(uppS)
            CFF: CFF8240_0750(uppS)
            CHA: CHAB381_0970(uppS)
            CCO: CCC13826_0695(uppS)
            ABU: Abu_2202(uppS)
            NIS: NIS_1105(uppS)
            SUN: SUN_1838(uppS)
            GSU: GSU1917(uppS)
            GME: Gmet_1254
            GUR: Gura_3729
            PCA: Pcar_1917
            PPD: Ppro_2048
            DVU: DVU0869(uppS)
            DVL: Dvul_2113
            DDE: Dde_1126
            LIP: LI0384(yaeS)
            BBA: Bd3785(uppS)
            DPS: DP1158
            ADE: Adeh_3585
            AFW: Anae109_3706
            MXA: MXAN_2555(uppS)
            SAT: SYN_00918
            SFU: Sfum_1782
            RPR: RP425
            RTY: RT0411(uppS)
            RCO: RC0590
            RFE: RF_0656(uppS)
            RBE: RBE_0745(uppS)
            RCM: A1E_03230
            OTS: OTBS_0268(uppS)
            WOL: WD0527(uppS)
            WBM: Wbm0804
            AMA: AM131(uppS)
            NSE: NSE_0944(uppS)
            PUB: SAR11_0910
            MLO: mll0640
            MES: Meso_1385
            PLA: Plav_3192
            SME: SMc02097(uppS)
            SMD: Smed_1135
            ATU: Atu1378(uppS)
            ATC: AGR_C_2550
            RET: RHE_CH01917(uppS)
            RLE: RL2225(uppS)
            BME: BMEI0827
            BMF: BAB1_1180
            BMS: BR1158(uppS)
            BMB: BruAb1_1164(uppS)
            BOV: BOV_1115(uppS)
            OAN: Oant_2033
            BJA: bll4857(uppS) blr0852(uppS)
            BRA: BRADO4136(ispU) BRADO7124(uppS)
            BBT: BBta_4513(ispU) BBta_7856(uppS)
            RPA: RPA2918(uppS)
            RPB: RPB_2688 RPB_2824
            RPC: RPC_2440
            RPD: RPD_0061 RPD_2853
            RPE: RPE_2557
            NWI: Nwi_1855
            NHA: Nham_1698
            XAU: Xaut_4435
            CCR: CC_1919
            SIL: SPO0319(ddsA) SPO1665(uppS)
            SIT: TM1040_1412
            RSP: RSP_2707(uppS)
            RSH: Rsph17029_1364
            RSQ: Rsph17025_2151
            JAN: Jann_2457
            RDE: RD1_2587(uppS)
            PDE: Pden_3995
            MMR: Mmar10_1384
            HNE: HNE_1772(uppS)
            ZMO: ZMO1152(uppS)
            NAR: Saro_1373
            SAL: Sala_1956
            SWI: Swit_0464
            ELI: ELI_03795
            GOX: GOX1814
            GBE: GbCGDNIH1_0936
            ACR: Acry_2555
            RRU: Rru_A1590
            MAG: amb2494
            MGM: Mmc1_1844
            ABA: Acid345_1417 Acid345_3136
            SUS: Acid_3241 Acid_6294
            BSU: BG13408(uppS)
            BHA: BH2423(uppS)
            BAN: BA3961(uppS)
            BAR: GBAA3961(uppS)
            BAA: BA_4431
            BAT: BAS3674
            BCE: BC3821
            BCA: BCE_3864(uppS)
            BCZ: BCZK3582(uppS)
            BCY: Bcer98_2475
            BTK: BT9727_3564(uppS)
            BLI: BL01239(uppS)
            BLD: BLi01874(uppS)
            BCL: ABC2238(uppS)
            BAY: RBAM_016370(uppS)
            BPU: BPUM_1552(uppS)
            OIH: OB1590(uppS)
            GKA: GK1253
            GTN: GTNG_1107
            SAU: SA1103(uppS)
            SAV: SAV1260(uppS)
            SAM: MW1143(uppS)
            SAR: SAR1236(uppS)
            SAS: SAS1194
            SAC: SACOL1279(uppS)
            SAB: SAB1122(uppS)
            SAA: SAUSA300_1153(uppS)
            SAO: SAOUHSC_01237
            SAJ: SaurJH9_1320
            SAH: SaurJH1_1346
            SEP: SE0936
            SER: SERP0827(uppS)
            SHA: SH1654(uppS)
            SSP: SSP1508
            LMO: lmo1315
            LMF: LMOf2365_1332(uppS)
            LIN: lin1352
            LWE: lwe1330(uppS)
            LLA: L183602(uppS)
            LLC: LACR_2435
            LLM: llmg_2415(uppS)
            SPY: SPy_1965(uppS)
            SPZ: M5005_Spy_1676(uppS)
            SPM: spyM18_2033(uppS)
            SPG: SpyM3_1691(uppS)
            SPS: SPs1693
            SPH: MGAS10270_Spy1744(uppS)
            SPI: MGAS10750_Spy1770(uppS)
            SPJ: MGAS2096_Spy1699(uppS)
            SPK: MGAS9429_Spy1677(uppS)
            SPF: SpyM51648(uppS)
            SPA: M6_Spy1684
            SPB: M28_Spy1664(uppS)
            SPN: SP_0261
            SPR: spr0240(uppS)
            SPD: SPD_0243(uppS)
            SAG: SAG1916(uppS)
            SAN: gbs1903
            SAK: SAK_1874(uppS)
            SMU: SMU.1786(uppS)
            STC: str0197(uppS)
            STL: stu0197(uppS)
            STE: STER_0244
            SSA: SSA_2073(uppS)
            SGO: SGO_1854(uppS)
            LPL: lp_2051(uppS)
            LJO: LJ1496
            LAC: LBA1266
            LSA: LSA1260(uppS)
            LSL: LSL_0563(uppS)
            LDB: Ldb1341(uppS)
            LBU: LBUL_1250
            LBR: LVIS_1345
            LCA: LSEI_1582
            LGA: LGAS_0805
            LRE: Lreu_0690
            EFA: EF2495(uppS)
            OOE: OEOE_0979
            STH: STH1496
            CAC: CAC1432 CAC1791
            CPE: CPE1558 CPE1696(uppS)
            CPF: CPF_1950(uppS)
            CPR: CPR_1668(uppS)
            CTC: CTC01265 CTC01360
            CNO: NT01CX_2145(uppS)
            CTH: Cthe_1001
            CDF: CD2136(uppS) CD2762(uppS)
            CBO: CBO2431(uppS)
            CBA: CLB_2295(uppS)
            CBH: CLC_2278(uppS)
            CBF: CLI_2487(uppS)
            CBE: Cbei_1192
            CKL: CKL_1421(uppS1) CKL_3336(uppS2)
            AMT: Amet_2684
            CHY: CHY_0237 CHY_1781(uppS)
            DSY: DSY2542
            DRM: Dred_1450 Dred_1973
            SWO: Swol_0886
            CSC: Csac_2355
            TTE: TTE1404(uppS)
            MTA: Moth_1038
            MPE: MYPE9550
            MTU: Rv1086 Rv2361c
            MTC: MT1118(uppS-1) MT2430(uppS-2)
            MBO: Mb1115 Mb2382c
            MLE: ML0634 ML2467
            MPA: MAP2141c MAP2703c
            MAV: MAV_2034(uppS)
            MSM: MSMEG_4490(uppS) MSMEG_5256(uppS)
            MVA: Mvan_3822 Mvan_4662
            MGI: Mflv_2055 Mflv_2714
            MMC: Mmcs_3449 Mmcs_4137
            MKM: Mkms_3512 Mkms_4212
            MJL: Mjls_3460 Mjls_4368
            CGL: NCgl0951(cgl0991) NCgl2203(cgl2283)
            CGB: cg1130(uppS1) cg2508(uppS2)
            CEF: CE1055 CE2182
            CDI: DIP0929 DIP1712
            CJK: jk0610(uppS2) jk1467(uppS1)
            NFA: nfa14530 nfa48180
            RHA: RHA1_ro01224 RHA1_ro05856
            SCO: SCO2509(SCC121.12c) SCO3858(SCH69.28c) SCP1.212
            SMA: SAV3237(uppS1) SAV5629(uppS2)
            TWH: TWT286(uppS) TWT331
            TWS: TW440(uppS1) TW486(uppS2)
            LXX: Lxx14460(uppS) Lxx16850(uppS)
            CMI: CMM_1579(uppS1) CMM_2236(uppS2)
            ART: Arth_1173 Arth_2224
            AAU: AAur_1291(uppS) AAur_2223(uppS)
            PAC: PPA0564 PPA0942
            NCA: Noca_1056 Noca_1932
            TFU: Tfu_0456 Tfu_0853
            FRA: Francci3_1273 Francci3_2214
            FAL: FRAAL2017(ispU) FRAAL3564(uppS)
            ACE: Acel_0796 Acel_1881
            KRA: Krad_1106 Krad_3373
            SEN: SACE_0919(uppS1) SACE_1494(uppS-2)
            STP: Strop_3446
            BLO: BL0101(uppS)
            BAD: BAD_1154(uppS)
            RXY: Rxyl_1402
            FNU: FN1326
            RBA: RB10335(uppS)
            CTR: CT450(yaeS)
            CTA: CTA_0492(uppS)
            CMU: TC0735
            CPN: CPn0566(yaeS)
            CPA: CP0183
            CPJ: CPj0566(yaeS)
            CPT: CpB0588
            CCA: CCA00176(uppS)
            CAB: CAB173
            CFE: CF0831(yaeS)
            PCU: pc0321(uppS)
            BBU: BB0120
            BGA: BG0121
            BAF: BAPKO_0121
            TPA: TP0603
            TDE: TDE2344(uppS)
            LIL: LA3294(uppS)
            LIC: LIC10854(uppS)
            LBJ: LBJ_0908(uppS)
            LBL: LBL_0923(uppS)
            SYN: sll0506
            SYW: SYNW0934(uppS)
            SYC: syc1249_c(uppS)
            SYF: Synpcc7942_0264
            SYD: Syncc9605_1631
            SYE: Syncc9902_1393
            SYG: sync_1031(uppS)
            SYR: SynRCC307_0792(uppS)
            SYX: SynWH7803_1531(uppS)
            CYA: CYA_2893(uppS)
            CYB: CYB_1646(uppS)
            TEL: tlr1763
            GVI: gll0108
            ANA: all2995 all3432
            AVA: Ava_0914 Ava_3455
            PMA: Pro1103(uppS)
            PMM: PMM1092(uppS)
            PMT: PMT1057(uppS)
            PMN: PMN2A_0656
            PMI: PMT9312_1103
            PMB: A9601_11981(uppS)
            PMC: P9515_11831(uppS)
            PMF: P9303_09951(uppS)
            PMG: P9301_11991(uppS)
            PMH: P9215_12281(uppS)
            PME: NATL1_14881(uppS)
            TER: Tery_2432
            BTH: BT_3726
            BFR: BF0505
            BFS: BF0450(uppS)
            PGI: PG0190(uppS)
            SRU: SRU_1847(uppS)
            CHU: CHU_3411(uppS)
            GFO: GFO_0213(uppS)
            FJO: Fjoh_1691
            FPS: FP2095(uppS)
            CTE: CT0267(uppS)
            CCH: Cag_0464
            CPH: Cpha266_0398
            PVI: Cvib_1531
            PLT: Plut_1750
            DET: DET0373(uppS)
            DEH: cbdb_A316(uppS)
            DEB: DehaBAV1_0355
            RRS: RoseRS_2015
            RCA: Rcas_3929
            DRA: DR_2447
            DGE: Dgeo_0020
            TTH: TTC1551
            TTJ: TTHA1915
            AAE: aq_1248
            TMA: TM1398
            TPT: Tpet_1385
            TME: Tmel_1279
            FNO: Fnod_1501
            MJA: MJ1372
            MMP: MMP1345
            MMQ: MmarC5_0233
            MMZ: MmarC7_0590
            MAE: Maeo_1136
            MVN: Mevan_0656
            MAC: MA1831(uppS) MA3723(uppS) MA4402
            MBA: Mbar_A0263 Mbar_A1074 Mbar_A2346
            MMA: MM_0014 MM_0618 MM_1083
            MBU: Mbur_0041
            MTP: Mthe_0589 Mthe_1499
            MHU: Mhun_0785
            MLA: Mlab_0463
            MEM: Memar_1788
            MBN: Mboo_2063
            MTH: MTH232
            MST: Msp_1182(uppS)
            MSI: Msm_0096
            MKA: MK0767(uppS)
            AFU: AF1219
            HAL: VNG1779C
            HMA: rrnAC1716(uppS)
            HWA: HQ3331A(uppS) HQ3332A(uppS)
            NPH: NP4544A(uppS_2) NP4550A(uppS_1)
            TAC: Ta0546
            TVO: TVN0600
            PTO: PTO1378
            PHO: PH1590
            PAB: PAB0394(hypoth)
            PFU: PF1599
            TKO: TK1173
            RCI: RCIX889(uppS-1) RRC441(uppS-2)
            APE: APE_1385
            SMR: Smar_1245
            IHO: Igni_0586
            HBU: Hbut_1087
            SSO: SSO0163
            STO: ST0189
            SAI: Saci_0757
            MSE: Msed_0171
            PAI: PAE2942
            PIS: Pisl_0348
            PCL: Pcal_1157
            PAS: Pars_1319
            TPE: Tpen_0762
STRUCTURES  PDB: 1F75  1JP3  1UEH  1V7U  1X06  1X07  1X08  1X09  2D2R  2DTN  
                 2E98  2E99  2E9A  2E9C  2E9D  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.31
            ExPASy - ENZYME nomenclature database: 2.5.1.31
            ExplorEnz - The Enzyme Database: 2.5.1.31
            ERGO genome analysis and discovery system: 2.5.1.31
            BRENDA, the Enzyme Database: 2.5.1.31
            CAS: 52350-87-5
///
ENTRY       EC 2.5.1.32                 Enzyme
NAME        phytoene synthase;
            prephytoene-diphosphate synthase;
            phytoene synthetase;
            PSase;
            geranylgeranyl-diphosphate geranylgeranyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     geranylgeranyl-diphosphate:geranylgeranyl-diphosphate
            geranylgeranyltransferase
REACTION    (1) 2 geranylgeranyl diphosphate = diphosphate + prephytoene
            diphosphate [RN:R02065];
            (2) prephytoene diphosphate = phytoene + diphosphate [RN:R07270]
ALL_REAC    R07270 > R04218;
            R02065;
            (other) R07916
SUBSTRATE   geranylgeranyl diphosphate [CPD:C00353];
            prephytoene diphosphate [CPD:C03427]
PRODUCT     diphosphate [CPD:C00013];
            prephytoene diphosphate [CPD:C03427];
            phytoene [CPD:C05413]
COMMENT     Requires Mn2+ for activity. The enzyme appears to be stereospecific,
            normally producing 15-cis-phytoene. However, in Erwinia herbicola,
            the product is the 15-trans isomer [2].
REFERENCE   1  [PMID:4819767]
  AUTHORS   Gregonis DE, Rilling HC.
  TITLE     The stereochemistry of trans-phytoene synthesis. Some observations
            on lycopersene as a carotene precursor and a mechanism for the
            synthesis of cis- and trans-phytoene.
  JOURNAL   Biochemistry. 13 (1974) 1538-42.
  ORGANISM  Mycobacterium sp.
REFERENCE   2  [PMID:12641468]
  AUTHORS   Iwata-Reuyl D, Math SK, Desai SB, Poulter CD.
  TITLE     Bacterial phytoene synthase: molecular cloning, expression, and
            characterization of Erwinia herbicola phytoene synthase.
  JOURNAL   Biochemistry. 42 (2003) 3359-65.
  ORGANISM  Erwinia herbicola
REFERENCE   3  [PMID:7896759]
  AUTHORS   Misawa N, Truesdale MR, Sandmann G, Fraser PD, Bird C, Schuch W,
            Bramley PM.
  TITLE     Expression of a tomato cDNA coding for phytoene synthase in
            Escherichia coli, phytoene formation in vivo and in vitro, and
            functional analysis of the various truncated gene products.
  JOURNAL   J. Biochem. (Tokyo). 116 (1994) 980-5.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00906  Carotenoid biosynthesis - General
ORTHOLOGY   KO: K02291  phytoene synthase
GENES       ATH: AT5G17230(PSY)
            OSA: 4342137
            CME: CMM166C
            PIC: PICST_79863(CDC43)
            PLU: plu4343(crtB)
            NOC: Noc_1042
            AEH: Mlg_0906
            HHA: Hhal_1618
            NME: NMB1130 NMB1168
            NMA: NMA1339
            NGO: NGO0830
            CVI: CV_2978
            RSO: RSc1652(crtB)
            REU: Reut_A1371 Reut_B4953
            REH: H16_A1466
            RME: Rmet_1944 Rmet_4149
            BMA: BMA1482 BMAA2102
            BXE: Bxe_A2303 Bxe_B0010
            BUR: Bcep18194_A5245 Bcep18194_B0017
            BCN: Bcen_5178 Bcen_6145
            BCH: Bcen2424_1934 Bcen2424_5681
            BAM: Bamb_1922
            BPS: BPSL2090 BPSS2340
            BPM: BURPS1710b_2502 BURPS1710b_A1491
            BTE: BTH_I2098 BTH_II2361
            BPE: BP1219
            BPA: BPP1833
            BBR: BB3273
            RFR: Rfer_1549
            POL: Bpro_2017
            MPT: Mpe_A1287
            MMS: mma_1528(crtB)
            NMU: Nmul_A2343
            EBA: ebA6810
            AZO: azo1883(crtB1) azo1884(crtB2)
            DAR: Daro_2706
            TBD: Tbd_1697
            MFA: Mfla_1469
            BBA: Bd1725(pys)
            MXA: MXAN_0896(crtB)
            PUB: SAR11_0121(crtB)
            MLO: mll1068
            MES: Meso_1794
            SME: SMc02055(crtB)
            ATU: Atu1560(crtB)
            ATC: AGR_C_2873(crtB)
            RET: RHE_CH01834(crtB)
            RLE: RL2057
            BME: BMEI1074
            BMF: BAB1_0912
            BMS: BR0893
            BMB: BruAb1_0905
            BJA: bll4732 blr3002
            BRA: BRADO1611(crtB)
            BBT: BBta_6444(crtB)
            RPA: RPA1513(crtB) RPA2828
            RPB: RPB_2729 RPB_4010
            RPC: RPC_1262 RPC_2773
            RPD: RPD_2774 RPD_3765
            RPE: RPE_1316 RPE_1812 RPE_2904
            NWI: Nwi_1766 Nwi_2271
            BHE: BH05660
            BQU: BQ04820
            RSP: RSP_0270(crtB)
            RSH: Rsph17029_1913
            JAN: Jann_0142
            RDE: RD1_0119(crtB) RD1_3180
            ZMO: ZMO0870
            NAR: Saro_1814
            SAL: Sala_3132
            ELI: ELI_09895
            GOX: GOX2258
            GBE: GbCGDNIH1_1981
            RRU: Rru_A0494
            MAG: amb1366 amb2508
            MGM: Mmc1_0306
            ABA: Acid345_1746
            BSU: BG12241(yisP)
            BPU: BPUM_1012(yisP)
            OOE: OEOE_0064
            MTU: Rv3397c(phyA)
            MTC: MT3505(crtB)
            MBO: Mb3430c(phyA)
            MPA: MAP3071
            SCO: SCO6760(SC6A5.09)
            SMA: SAV1024(crtB) SAV1653(hopD)
            TFU: Tfu_3076
            FRA: Francci3_0820 Francci3_1383
            FAL: FRAAL1429
            SEN: SACE_3269(crtB) SACE_3539(crtB) SACE_4330(hopD)
            RXY: Rxyl_0844
            RBA: RB9283(crtB)
            SYN: slr1255(crtB)
            SYW: SYNW2256(crtB)
            SYC: syc2112_c(pys)
            SYF: Synpcc7942_1984
            SYD: Syncc9605_2394
            SYE: Syncc9902_0299
            SYG: sync_2607(crtB)
            SYR: SynRCC307_0239(crtB)
            SYX: SynWH7803_2269(crtB)
            CYA: CYA_0317(crtB)
            CYB: CYB_1695(crtB)
            TEL: tll1560(pys)
            GVI: glr1744(pys)
            ANA: alr1833(pys)
            AVA: Ava_4794
            PMA: Pro0166(crtB)
            PMM: PMM0143(crtB)
            PMT: PMT2003(crtB)
            PMN: PMN2A_1509(crtB)
            PMI: PMT9312_0145
            PMB: A9601_01601(crtB)
            PMC: P9515_01711(crtB)
            PMF: P9303_26641(crtB)
            PMG: P9301_01621(crtB)
            PME: NATL1_02151(crtB)
            TER: Tery_4010
            SRU: SRU_1430(crtB)
            FPS: FP1450(crtB)
            CTE: CT1386
            CCH: Cag_1175
            CPH: Cpha266_1738
            PVI: Cvib_0699
            PLT: Plut_1356
            DRA: DR_0862
            DGE: Dgeo_0523
            TTH: TT_P0057
            TTJ: TTHB101
            MTH: MTH1808
            HAL: VNG1458G(crtB1) VNG1680G(crtB2)
            HMA: rrnAC2069(crtB)
            HWA: HQ2860A(crtB)
            NPH: NP4770A(crtB)
            PTO: PTO1535
            SSO: SSO2905(crtB)
            SAI: Saci_1734
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.32
            ExPASy - ENZYME nomenclature database: 2.5.1.32
            ExplorEnz - The Enzyme Database: 2.5.1.32
            ERGO genome analysis and discovery system: 2.5.1.32
            BRENDA, the Enzyme Database: 2.5.1.32
            CAS: 57219-66-6
///
ENTRY       EC 2.5.1.33                 Enzyme
NAME        trans-pentaprenyltranstransferase;
            all-trans-hexaprenyl-diphosphate synthase;
            hexaprenyl diphosphate synthase;
            hexaprenyl pyrophosphate synthetase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     all-trans-pentaprenyl-diphosphate:isopentenyl-diphosphate
            pentaprenyltranstransferase
REACTION    all-trans-pentaprenyl diphosphate + isopentenyl diphosphate =
            diphosphate + all-trans-hexaprenyl diphosphate [RN:R05613]
ALL_REAC    R05613
SUBSTRATE   all-trans-pentaprenyl diphosphate [CPD:C04217];
            isopentenyl diphosphate [CPD:C00129]
PRODUCT     diphosphate [CPD:C00013];
            all-trans-hexaprenyl diphosphate [CPD:C01230]
COMMENT     This enzyme will also use trans,trans-farnesyl diphosphate and
            all-trans-geranylgeranyl diphosphate as donors.
REFERENCE   1  [PMID:7174655]
  AUTHORS   Fujii H, Koyama T, Ogura K.
  TITLE     Hexaprenyl pyrophosphate synthetase from Micrococcus luteus B-P 26.
            Separation of two essential components.
  JOURNAL   J. Biol. Chem. 257 (1982) 14610-2.
  ORGANISM  Micrococcus luteus
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K05355  trans-pentaprenyltranstransferase
GENES       PTO: PTO1199
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.33
            ExPASy - ENZYME nomenclature database: 2.5.1.33
            ExplorEnz - The Enzyme Database: 2.5.1.33
            ERGO genome analysis and discovery system: 2.5.1.33
            BRENDA, the Enzyme Database: 2.5.1.33
            CAS: 83745-07-7
///
ENTRY       EC 2.5.1.34                 Enzyme
NAME        tryptophan dimethylallyltransferase;
            dimethylallylpyrophosphate:L-tryptophan dimethylallyltransferase;
            dimethylallyltryptophan synthetase;
            dimethylallylpyrophosphate:tryptophan dimethylallyl transferase;
            DMAT synthetase;
            4-(gamma,gamma-dimethylallyl)tryptophan synthase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     dimethylallyl-diphosphate:L-tryptophan dimethylallyltransferase
REACTION    dimethylallyl diphosphate + L-tryptophan = diphosphate +
            4-(3-methylbut-2-enyl)-L-tryptophan [RN:R01657]
ALL_REAC    R01657
SUBSTRATE   dimethylallyl diphosphate [CPD:C00235];
            L-tryptophan [CPD:C00078]
PRODUCT     diphosphate [CPD:C00013];
            4-(3-methylbut-2-enyl)-L-tryptophan [CPD:C04290]
REFERENCE   1  [PMID:999297]
  AUTHORS   Lee SL, Floss HG, Heinstein P.
  TITLE     Purification and properties of
            dimethylallylpyrophosphate:tryptopharm dimethylallyl transferase,
            the first enzyme of ergot alkaloid biosynthesis in Claviceps. sp. SD
            58.
  JOURNAL   Arch. Biochem. Biophys. 177 (1976) 84-94.
  ORGANISM  Claviceps. sp.
GENES       AFM: AFUA_2G18040 AFUA_3G12930
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.34
            ExPASy - ENZYME nomenclature database: 2.5.1.34
            ExplorEnz - The Enzyme Database: 2.5.1.34
            ERGO genome analysis and discovery system: 2.5.1.34
            BRENDA, the Enzyme Database: 2.5.1.34
            CAS: 55127-01-0
///
ENTRY       EC 2.5.1.35                 Enzyme
NAME        aspulvinone dimethylallyltransferase;
            dimethylallyl pyrophosphate:aspulvinone dimethylallyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     dimethylallyl-diphosphate:aspulvinone-E dimethylallyltransferase
REACTION    2 dimethylallyl diphosphate + aspulvinone E = 2 diphosphate +
            aspulvinone H [RN:R03799]
ALL_REAC    R03799
SUBSTRATE   dimethylallyl diphosphate [CPD:C00235];
            aspulvinone E [CPD:C02006]
PRODUCT     diphosphate [CPD:C00013];
            aspulvinone H [CPD:C02008]
COMMENT     This enzyme will also use as acceptor aspulvinone G, a hydroxylated
            derivative of the complex phenolic pigment aspulvinone E.
REFERENCE   1  [PMID:678538]
  AUTHORS   Takahashi I, Ojima N, Ogura K, Seto S.
  TITLE     Purification and characterization of dimethylallyl pyrophosphate:
            aspulvinone dimethylallyltransferase from Aspergillus terreus.
  JOURNAL   Biochemistry. 17 (1978) 2696-702.
  ORGANISM  Aspergillus terreus
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.35
            ExPASy - ENZYME nomenclature database: 2.5.1.35
            ExplorEnz - The Enzyme Database: 2.5.1.35
            ERGO genome analysis and discovery system: 2.5.1.35
            BRENDA, the Enzyme Database: 2.5.1.35
            CAS: 67584-68-3
///
ENTRY       EC 2.5.1.36                 Enzyme
NAME        trihydroxypterocarpan dimethylallyltransferase;
            glyceollin synthase;
            dimethylallylpyrophosphate:3,6a,9-trihydroxypterocarpan
            dimethylallyltransferase;
            dimethylallylpyrophosphate:trihydroxypterocarpan dimethylallyl
            transferase;
            dimethylallyl-diphosphate:(6aS,11aS)-3,6a,9-trihydroxypterocarpan
            dimethyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     dimethylallyl-diphosphate:(6aS,11aS)-3,6a,9-trihydroxypterocarpan
            dimethylallyltransferase
REACTION    (1) dimethylallyl diphosphate +
            (6aS,11aS)-3,6a,9-trihydroxypterocarpan = diphosphate +
            2-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan [RN:R07271];
            (2) dimethylallyl diphosphate +
            (6aS,11aS)-3,6a,9-trihydroxypterocarpan = diphosphate +
            4-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan [RN:R07272]
ALL_REAC    R07271 R07272
SUBSTRATE   dimethylallyl diphosphate [CPD:C00235];
            (6aS,11aS)-3,6a,9-trihydroxypterocarpan [CPD:C01263]
PRODUCT     diphosphate [CPD:C00013];
            2-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan
            [CPD:C15509];
            4-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan [CPD:C15510]
COMMENT     Part of the glyceollin biosynthesis system in soy bean.
REFERENCE   1
  AUTHORS   Leube, J. and Grisebach, H.
  TITLE     Further studies on induction of enzymes of phytoalexin synthesis in
            soybean and cultured soybean cells.
  JOURNAL   Z. Naturforsch. C: Biosci. 38 (1983) 730-735.
  ORGANISM  Glycine max [GN:egma]
REFERENCE   2
  AUTHORS   Zahringer, U., Schaller, E. and Grisebach, H.
  TITLE     Induction of phytoalexin synthesis in soybean. Structure and
            reactions of naturally occurring and enzymatically prepared
            prenylated pterocarpans from elicitor-treated cotyledons and cell
            cultures of soybean.
  JOURNAL   Z. Natursforsch. C: Biosci. 36 (1981) 234-241.
  ORGANISM  Glycine max [GN:egma]
PATHWAY     PATH: map00943  Isoflavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.36
            ExPASy - ENZYME nomenclature database: 2.5.1.36
            ExplorEnz - The Enzyme Database: 2.5.1.36
            ERGO genome analysis and discovery system: 2.5.1.36
            BRENDA, the Enzyme Database: 2.5.1.36
            CAS: 70851-94-4
///
ENTRY       EC 2.5.1.37       Obsolete  Enzyme
NAME        Transferred to 4.4.1.20
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
COMMENT     Transferred entry: now EC 4.4.1.20 leukotriene-C4 synthase. The
            enzyme was incorrectly classified as a transferase. (EC 2.5.1.37
            created 1989, deleted 2004)
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.37
            ExPASy - ENZYME nomenclature database: 2.5.1.37
            ExplorEnz - The Enzyme Database: 2.5.1.37
            ERGO genome analysis and discovery system: 2.5.1.37
            BRENDA, the Enzyme Database: 2.5.1.37
///
ENTRY       EC 2.5.1.38                 Enzyme
NAME        isonocardicin synthase;
            nocardicin aminocarboxypropyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     S-adenosyl-L-methionine:nocardicin-E
            3-amino-3-carboxypropyltransferase
REACTION    S-adenosyl-L-methionine + nocardicin E = 5'-methylthioadenosine +
            isonocardicin A [RN:R03072]
ALL_REAC    R03072
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            nocardicin E [CPD:C01739]
PRODUCT     5'-methylthioadenosine [CPD:C00170];
            isonocardicin A [CPD:C00927]
COMMENT     Involved in the biosynthesis of the beta-lactam antibiotic
            nocardicin A.
REFERENCE   1
  AUTHORS   Wilson, B.A., Bantia, S., Salituro, G.M., Reeve, A.M. and Townsend,
            C.A.
  TITLE     Cell-free biosynthesis of nocardicin A from nocardicin E and
            S-adenosylmethionine.
  JOURNAL   J. Am. Chem. Soc. 110 (1988) 8238-8239.
  ORGANISM  Nocardia uniformis
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.38
            ExPASy - ENZYME nomenclature database: 2.5.1.38
            ExplorEnz - The Enzyme Database: 2.5.1.38
            ERGO genome analysis and discovery system: 2.5.1.38
            BRENDA, the Enzyme Database: 2.5.1.38
            CAS: 118246-74-5
///
ENTRY       EC 2.5.1.39                 Enzyme
NAME        4-hydroxybenzoate nonaprenyltransferase;
            nonaprenyl-4-hydroxybenzoate transferase;
            4-hydroxybenzoate transferase;
            p-hydroxybenzoate dimethylallyltransferase;
            p-hydroxybenzoate polyprenyltransferase;
            p-hydroxybenzoic acid-polyprenyl transferase;
            p-hydroxybenzoic-polyprenyl transferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     solanesyl-diphosphate:4-hydroxybenzoate nonaprenyltransferase
REACTION    solanesyl diphosphate + 4-hydroxybenzoate = diphosphate +
            nonaprenyl-4-hydroxybenzoate [RN:R07273]
ALL_REAC    R07273;
            (other) R05000
SUBSTRATE   solanesyl diphosphate [CPD:C04145];
            4-hydroxybenzoate [CPD:C00156]
PRODUCT     diphosphate [CPD:C00013];
            nonaprenyl-4-hydroxybenzoate [CPD:C03885]
COMMENT     Involved in the biosynthesis of ubiquinone.
REFERENCE   1  [PMID:2295606]
  AUTHORS   Kalen A, Appelkvist EL, Chojnacki T, Dallner G.
  TITLE     Nonaprenyl-4-hydroxybenzoate transferase, an enzyme involved in
            ubiquinone biosynthesis, in the endoplasmic reticulum-Golgi system
            of rat liver.
  JOURNAL   J. Biol. Chem. 265 (1990) 1158-64.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00130  Ubiquinone biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.39
            ExPASy - ENZYME nomenclature database: 2.5.1.39
            ExplorEnz - The Enzyme Database: 2.5.1.39
            ERGO genome analysis and discovery system: 2.5.1.39
            BRENDA, the Enzyme Database: 2.5.1.39
            CAS: 9030-77-7
///
ENTRY       EC 2.5.1.40       Obsolete  Enzyme
NAME        Transferred to 4.2.3.9
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
COMMENT     Transferred entry: now EC 4.2.3.9 aristolochene synthase (EC
            2.5.1.40 created 1992, deleted 1999)
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.40
            ExPASy - ENZYME nomenclature database: 2.5.1.40
            ExplorEnz - The Enzyme Database: 2.5.1.40
            ERGO genome analysis and discovery system: 2.5.1.40
            BRENDA, the Enzyme Database: 2.5.1.40
///
ENTRY       EC 2.5.1.41                 Enzyme
NAME        phosphoglycerol geranylgeranyltransferase;
            glycerol phosphate geranylgeranyltransferase;
            geranylgeranyl-transferase;
            prenyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     geranylgeranyl diphosphate:sn-glyceryl phosphate
            geranylgeranyltransferase
REACTION    geranylgeranyl diphosphate + sn-glyceryl phosphate = diphosphate +
            sn-3-O-(geranylgeranyl)glyceryl 1-phosphate [RN:R04158]
ALL_REAC    R04158
SUBSTRATE   geranylgeranyl diphosphate [CPD:C00353];
            sn-glyceryl phosphate [CPD:C03189]
PRODUCT     diphosphate [CPD:C00013];
            sn-3-O-(geranylgeranyl)glyceryl 1-phosphate
REFERENCE   1
  AUTHORS   Zhang, D.-L., Daniels, L. and Poulter, C.D.
  TITLE     Biosynthesis of archaebacterial membranes. Formation of isoprene
            ethers by a prenyl transfer reaction.
  JOURNAL   J. Am. Chem. Soc. 112 (1990) 1264-1265.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.41
            ExPASy - ENZYME nomenclature database: 2.5.1.41
            ExplorEnz - The Enzyme Database: 2.5.1.41
            ERGO genome analysis and discovery system: 2.5.1.41
            BRENDA, the Enzyme Database: 2.5.1.41
            CAS: 124650-69-7
///
ENTRY       EC 2.5.1.42                 Enzyme
NAME        geranylgeranylglycerol-phosphate geranylgeranyltransferase;
            geranylgeranyloxyglycerol phosphate geranylgeranyltransferase;
            geranylgeranyltransferase II
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     geranylgeranyl diphosphate:sn-3-O-(geranylgeranyl)glycerol
            1-phosphate geranylgeranyltransferase
REACTION    geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol
            1-phosphate = diphosphate + 2,3-bis-O-(geranylgeranyl)glycerol
            1-phosphate [RN:R04520]
ALL_REAC    R04520
SUBSTRATE   geranylgeranyl diphosphate [CPD:C00353];
            sn-3-O-(geranylgeranyl)glycerol 1-phosphate [CPD:C04590]
PRODUCT     diphosphate [CPD:C00013];
            2,3-bis-O-(geranylgeranyl)glycerol 1-phosphate [CPD:C04638]
REFERENCE   1
  AUTHORS   Zhang, D.-L., Daniels, L. and Poulter, C.D.
  TITLE     Biosynthesis of archaebacterial membranes. Formation of isoprene
            ethers by a prenyl transfer reaction.
  JOURNAL   J. Am. Chem. Soc. 112 (1990) 1264-1265.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
STRUCTURES  PDB: 2F6U  2F6X  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.42
            ExPASy - ENZYME nomenclature database: 2.5.1.42
            ExplorEnz - The Enzyme Database: 2.5.1.42
            ERGO genome analysis and discovery system: 2.5.1.42
            BRENDA, the Enzyme Database: 2.5.1.42
            CAS: 124650-68-6
///
ENTRY       EC 2.5.1.43                 Enzyme
NAME        nicotianamine synthase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     S-adenosyl-L-methionine:S-adenosyl-L-methionine:S-adenosyl-Lmethioni
            ne 3-amino-3-carboxypropyltransferase
REACTION    3 S-adenosyl-L-methionine = 3 S-methyl-5'-thioadenosine +
            nicotianamine [RN:R00075]
ALL_REAC    R00075
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019]
PRODUCT     S-methyl-5'-thioadenosine [CPD:C00170];
            nicotianamine [CPD:C05324]
REFERENCE   1
  AUTHORS   Higuchi, K., Kanazawa, K., Nishizawa, N.-K., Chino, M., Mori, S.
  TITLE     Purification and characterization of nicotianamine synthase from
            Fe-deficient barley root.
  JOURNAL   Plant Soil 165 (1994) 173-179.
  ORGANISM  Hordeum vulgare [GN:ehvu]
ORTHOLOGY   KO: K05953  
GENES       ATH: AT1G09240 AT1G56430 AT5G04950 AT5G56080
            OSA: 4344361
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.43
            ExPASy - ENZYME nomenclature database: 2.5.1.43
            ExplorEnz - The Enzyme Database: 2.5.1.43
            ERGO genome analysis and discovery system: 2.5.1.43
            BRENDA, the Enzyme Database: 2.5.1.43
            CAS: 161515-44-2
///
ENTRY       EC 2.5.1.44                 Enzyme
NAME        homospermidine synthase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     putrescine:putrescine 4-aminobutyltransferase (ammonia-forming)
REACTION    (1) 2 putrescine = sym-homospermidine + NH3 + H+ [RN:R00018];
            (2) putrescine + spermidine = sym-homospermidine + propane
            1,3-diamine
ALL_REAC    R00018
SUBSTRATE   putrescine [CPD:C00134];
            spermidine [CPD:C00315]
PRODUCT     sym-homospermidine [CPD:C06366];
            NH3 [CPD:C00014];
            H+ [CPD:C00080];
            propane 1,3-diamine
COFACTOR    NAD+ [CPD:C00003]
COMMENT     The reaction of this enzyme occurs in three steps, with some of the
            intermediates presumably remaining enzyme-bound: NAD+-dependent
            dehydrogenation of putrescine, transfer of the 4-aminobutylidene
            group from dehydroputrescine to a second molecule of putrescine and
            reduction of the imine intermediate to form homospermidine. Hence
            the overall reaction is transfer of a 4-aminobutyl group. Differs
            from EC 2.5.1.45, homospermidine synthase (spermidine-specific),
            which cannot use putrescine as donor of the aminobutyl group.
REFERENCE   1  [PMID:437275]
  AUTHORS   Tait GH.
  TITLE     The formation of homospermidine by an enzyme from Rhodopseudomonas
            viridis [proceedings]
  JOURNAL   Biochem. Soc. Trans. 7 (1979) 199-201.
  ORGANISM  Rhodopseudomonas viridis
REFERENCE   2  [PMID:16526057]
  AUTHORS   Ostrovsky AN, Grischenko AV, Taylor PD, Bock P, Mawatari SF.
  TITLE     Comparative anatomical study of internal brooding in three anascan
            bryozoans (Cheilostomata) and its taxonomic and evolutionary
            implications.
  JOURNAL   J. Morphol. 267 (2006) 739-49.
REFERENCE   3  [PMID:8407874]
  AUTHORS   Yamamoto S, Nagata S, Kusaba K.
  TITLE     Purification and characterization of homospermidine synthase in
            Acinetobacter tartarogenes ATCC 31105.
  JOURNAL   J. Biochem. (Tokyo). 114 (1993) 45-9.
  ORGANISM  Acinetobacter tartarogenes
REFERENCE   4  [PMID:7470060]
  AUTHORS   Srivenugopal KS, Adiga PR.
  TITLE     Enzymic synthesis of sym-homospermidine in Lathyrus sativus (grass
            pea) seedlings.
  JOURNAL   Biochem. J. 190 (1980) 461-4.
  ORGANISM  Lathyrus sativus
REFERENCE   5
  AUTHORS   Ober, D., Tholl, D., Martin, W. and Hartmann, T.
  TITLE     Homospermidine synthase of Rhodopseudomonas viridis: Substrate
            specificity and effects of the heterologously expressed enzyme on
            polyamine metabolism of Escherichia coli.
  JOURNAL   J. Gen. Appl. Microbiol. 42 (1996) 411-419.
  ORGANISM  Rhodopseudomonas viridis
REFERENCE   6  [PMID:10611289]
  AUTHORS   Ober D, Hartmann T.
  TITLE     Homospermidine synthase, the first pathway-specific enzyme of
            pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine
            synthase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 14777-82.
  ORGANISM  Senecio vernalis
PATHWAY     PATH: map00960  Alkaloid biosynthesis II
ORTHOLOGY   KO: K00808  homospermidine synthase
GENES       PAU: PA14_35790
            PAP: PSPA7_3061
            PST: PSPTO_1868(hss)
            SAZ: Sama_3337
            LPN: lpg2495(hss)
            LPF: lpl2416
            LPP: lpp2562
            REH: H16_A0043(hss)
            NEU: NE1498(hss)
            NMU: Nmul_A1700
            MLO: mlr3014
            MES: Meso_2727
            PLA: Plav_1354
            SME: SMc04016(hss)
            SMD: Smed_2688
            ATU: Atu3768
            ATC: AGR_L_2136
            RET: RHE_CH03553(hss)
            RLE: RL4073(hss)
            BME: BMEII0015 BMEII0016
            BMF: BAB2_0077
            BMS: BRA0078
            BMB: BruAb2_0078
            OAN: Oant_4263
            BJA: blr7762
            BRA: BRADO6264(hss)
            BBT: BBta_1345(hss)
            RPA: RPA0865
            RPB: RPB_4552
            RPC: RPC_4834
            RPD: RPD_0850
            RPE: RPE_4799
            NWI: Nwi_0921
            NHA: Nham_3423
            XAU: Xaut_2138
            JAN: Jann_0956
            GBE: GbCGDNIH1_0521
            MAG: amb2266
            MAC: MA1636
            MBA: Mbar_A2685
            MMA: MM_0166
            MBN: Mboo_1047
STRUCTURES  PDB: 2PH5  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.44
            ExPASy - ENZYME nomenclature database: 2.5.1.44
            ExplorEnz - The Enzyme Database: 2.5.1.44
            ERGO genome analysis and discovery system: 2.5.1.44
            BRENDA, the Enzyme Database: 2.5.1.44
            CAS: 76106-84-8
///
ENTRY       EC 2.5.1.45                 Enzyme
NAME        homospermidine synthase (spermidine-specific)
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     spermidine:putrescine 4-aminobutyltransferase
            (propane-1,3-diamine-forming)
REACTION    spermidine + putrescine = sym-homospermidine + propane-1,3-diamine
            [RN:R01919]
ALL_REAC    R01919
SUBSTRATE   spermidine [CPD:C00315];
            putrescine [CPD:C00134]
PRODUCT     sym-homospermidine [CPD:C06366];
            propane-1,3-diamine [CPD:C00986]
COMMENT     The reaction of this enzyme occurs in three steps, with some of the
            intermediates presumably remaining enzyme-bound: (a) NAD+-dependent
            dehydrogenation of spermidine, (b) transfer of the 4-aminobutylidene
            group from dehydrospermidine to putrescine and (c) reduction of the
            imine intermediate to form homospermidine. This enzyme is more
            specific than EC 2.5.1.44, homospermidine synthase, which is found
            in bacteria, as it cannot use putrescine as donor of the
            4-aminobutyl group. Forms part of the biosynthetic pathway of the
            poisonous pyrrolizidine alkaloids of the ragworts (Senecio).
REFERENCE   1  [PMID:16526057]
  AUTHORS   Ostrovsky AN, Grischenko AV, Taylor PD, Bock P, Mawatari SF.
  TITLE     Comparative anatomical study of internal brooding in three anascan
            bryozoans (Cheilostomata) and its taxonomic and evolutionary
            implications.
  JOURNAL   J. Morphol. 267 (2006) 739-49.
REFERENCE   2  [PMID:10611289]
  AUTHORS   Ober D, Hartmann T.
  TITLE     Homospermidine synthase, the first pathway-specific enzyme of
            pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine
            synthase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 14777-82.
  ORGANISM  Senecio vulgaris
REFERENCE   3
  AUTHORS   Ober, D., Harms, R. and Hartmann, T.
  TITLE     Cloning and expression of homospermidine synthase from Senecio
            vulgaris: a revision.
  JOURNAL   Phytochemistry 55 (2000) 311-316.
  ORGANISM  Senecio vulgaris
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.45
            ExPASy - ENZYME nomenclature database: 2.5.1.45
            ExplorEnz - The Enzyme Database: 2.5.1.45
            ERGO genome analysis and discovery system: 2.5.1.45
            BRENDA, the Enzyme Database: 2.5.1.45
///
ENTRY       EC 2.5.1.46                 Enzyme
NAME        deoxyhypusine synthase;
            spermidine:eIF5A-lysine 4-aminobutyltransferase
            (propane-1,3-diamine-forming)
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     [eIF5A-precursor]-lysine:spermidine 4-aminobutyltransferase
            (propane-1,3-diamine-forming)
REACTION    (1) [eIF5A-precursor]-lysine + spermidine =
            [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine [RN:R05329];
            (2) (1a) spermidine + NAD+ = dehydrospermidine + NADH;
            (3) (1b) dehydrospermidine + [enzyme]-lysine =
            N-(4-aminobutylidene)-[enzyme]-lysine + propane-1,3-diamine;
            (4) (1c) N-(4-aminobutylidene)-[enzyme]-lysine +
            [eIF5A-precursor]-lysine =
            N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + [enzyme]-lysine;
            (5) (1d) N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + NADH + H+
            = [eIF5A-precursor]-deoxyhypusine + NAD+
ALL_REAC    R05329;
            (other) R07477 R07478 R07479 R07480
SUBSTRATE   [eIF5A-precursor]-lysine [CPD:C07281];
            spermidine [CPD:C00315];
            NAD+ [CPD:C00003];
            dehydrospermidine [CPD:C15853];
            [enzyme]-lysine [CPD:C07281];
            N-(4-aminobutylidene)-[enzyme]-lysine [CPD:C15854];
            N-(4-aminobutylidene)-[eIF5A-precursor]-lysine [CPD:C15854];
            NADH [CPD:C00004];
            H+ [CPD:C00080]
PRODUCT     [eIF5A-precursor]-deoxyhypusine [CPD:C07282];
            propane-1,3-diamine [CPD:C00986];
            dehydrospermidine [CPD:C15853];
            NADH [CPD:C00004];
            N-(4-aminobutylidene)-[enzyme]-lysine [CPD:C15854];
            N-(4-aminobutylidene)-[eIF5A-precursor]-lysine [CPD:C15854];
            [enzyme]-lysine [CPD:C07281];
            NAD+ [CPD:C00003]
COMMENT     The eukaryotic initiation factor eIF5A contains a hypusine residue
            that is essential for activity. This enzyme catalyses the first
            reaction of hypusine formation from one specific lysine residue of
            the eIF5A precursor. The reaction occurs in four steps:
            NAD+-dependent dehydrogenation of spermidine (1a), formation of an
            enzyme-imine intermediate by transfer of the 4-aminobutylidene group
            from dehydrospermidine to the active site lysine residue (Lys329 for
            the human enzyme; 1b), transfer of the same 4-aminobutylidene group
            from the enzyme intermediate to the e1F5A precursor (1c), reduction
            of the e1F5A-imine intermediate to form a deoxyhypusine residue
            (1d). Hence the overall reaction is transfer of a 4-aminobutyl
            group. For the plant enzyme, homospermidine can substitute for
            spermidine and putrescine can substitute for the lysine residue of
            the eIF5A precursor. Hypusine is formed from deoxyhypusine by the
            action of EC 1.14.99.29, deoxyhypusine monooxygenase.
REFERENCE   1  [PMID:1690726]
  AUTHORS   Yoshioka H, Ramirez F.
  TITLE     Pro-alpha 1(XI) collagen. Structure of the amino-terminal propeptide
            and expression of the gene in tumor cell lines.
  JOURNAL   J. Biol. Chem. 265 (1990) 6423-6.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:9188485]
  AUTHORS   Wolff EC, Folk JE, Park MH.
  TITLE     Enzyme-substrate intermediate formation at lysine 329 of human
            deoxyhypusine synthase.
  JOURNAL   J. Biol. Chem. 272 (1997) 15865-71.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:9285092]
  AUTHORS   Chen KY, Liu AY.
  TITLE     Biochemistry and function of hypusine formation on eukaryotic
            initiation factor 5A.
  JOURNAL   Biol. Signals. 6 (1997) 105-9.
  ORGANISM  human [GN:hsa], Neurospora crassa [GN:dncr]
REFERENCE   4  [PMID:10542236]
  AUTHORS   Ober D, Hartmann T.
  TITLE     Deoxyhypusine synthase from tobacco. cDNA isolation,
            characterization, and bacterial expression of an enzyme with
            extended substrate specificity.
  JOURNAL   J. Biol. Chem. 274 (1999) 32040-7.
  ORGANISM  Nicotiana tabacum
REFERENCE   5  [PMID:10611289]
  AUTHORS   Ober D, Hartmann T.
  TITLE     Homospermidine synthase, the first pathway-specific enzyme of
            pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine
            synthase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 14777-82.
  ORGANISM  Senecio vernalis
REFERENCE   6  [PMID:10028184]
  AUTHORS   Wolff EC, Park MH.
  TITLE     Identification of lysine350 of yeast deoxyhypusine synthase as the
            site of enzyme intermediate formation.
  JOURNAL   Yeast. 15 (1999) 43-50.
  ORGANISM  human [GN:hsa], Saccharomyces cerevisiae [GN:sce]
REFERENCE   7  [PMID:10734052]
  AUTHORS   Wolff EC, Wolff J, Park MH.
  TITLE     Deoxyhypusine synthase generates and uses bound NADH in a transient
            hydride transfer mechanism.
  JOURNAL   J. Biol. Chem. 275 (2000) 9170-7.
  ORGANISM  human [GN:hsa]
REFERENCE   8  [PMID:7673224]
  AUTHORS   Joe YA, Wolff EC, Park MH.
  TITLE     Cloning and expression of human deoxyhypusine synthase cDNA.
            Structure-function studies with the recombinant enzyme and mutant
            proteins.
  JOURNAL   J. Biol. Chem. 270 (1995) 22386-92.
  ORGANISM  Neurospora crassa [GN:dncr], rat [GN:rno]
REFERENCE   9  [PMID:7592594]
  AUTHORS   Tao Y, Chen KY.
  TITLE     Molecular cloning and functional expression of Neurospora
            deoxyhypusine synthase cDNA and identification of yeast
            deoxyhypusine synthase cDNA.
  JOURNAL   J. Biol. Chem. 270 (1995) 23984-7.
  ORGANISM  Neurospora crassa [GN:dncr]
ORTHOLOGY   KO: K00809  deoxyhypusine synthase
GENES       HSA: 1725(DHPS)
            PTR: 455746(DHPS)
            MMU: 330817(Dhps)
            CFA: 476702(DHPS)
            BTA: 444988(DHPS)
            XLA: 431985(MGC82178)
            XTR: 394501(dhps)
            SPU: 579530(LOC579530) 582547(LOC582547)
            CEL: Y17G7B.4
            OSA: 4334056
            CME: CMA098C
            SCE: YHR068W(DYS1)
            AGO: AGOS_AAL036W
            PIC: PICST_88952
            CGR: CAGL0H07249g
            SPO: SPBC1271.04c
            ANI: AN8075.2
            AFM: AFUA_5G01740
            AOR: AO090003001350
            CNE: CNJ02480
            UMA: UM00071.1
            ECU: ECU09_0910
            DDI: DDBDRAFT_0186679
            PFA: PF14_0125
            CHO: Chro.20420
            TAN: TA13570
            TPV: TP02_0058
            TET: TTHERM_00819550
            TBR: Tb927.1.870
            TCR: 511421.60
            LMA: LmjF20.0250
            EHI: 77.t00015 83.t00016
            CBU: CBU_0721
            CBD: COXBU7E912_0732
            BBA: Bd2349(dys)
            ADE: Adeh_3097
            MXA: MXAN_2140
            SAT: SYN_02461
            SFU: Sfum_3135
            CCR: CC_0359
            MMR: Mmar10_0376
            ZMO: ZMO1019(dys)
            ABA: Acid345_1942
            SUS: Acid_1177
            RBA: RB1381(dys1)
            CYA: CYA_2657
            CYB: CYB_2420
            TEL: tlr0818
            GVI: glr1045
            ANA: alr3804
            AVA: Ava_1896 Ava_B0166
            CHU: CHU_1939
            GFO: GFO_3623
            CTE: CT0011
            CCH: Cag_0073
            PLT: Plut_2089
            TTH: TTC1205
            TTJ: TTHA1570
            MJA: MJ0814
            MMP: MMP0137(dys)
            MMQ: MmarC5_1539
            MMZ: MmarC7_1136
            MAE: Maeo_1473
            MVN: Mevan_1142
            MAC: MA0968 MA3013(dys)
            MBA: Mbar_A0061 Mbar_A2038
            MMA: MM_0287 MM_2082
            MBU: Mbur_1868
            MTP: Mthe_1200
            MHU: Mhun_2546 Mhun_2903
            MTH: MTH127
            MST: Msp_0395(dys)
            MSI: Msm_1615
            MKA: MK0737(dYS1)
            AFU: AF2195(dys1-1) AF2300(dys1-2)
            HAL: VNG1432G(dhs)
            HMA: rrnAC1918(dhs)
            HWA: HQ2852A(dhs)
            NPH: NP4578A(dhs)
            TAC: Ta0356
            TVO: TVN0418
            PTO: PTO1252
            PHO: PH1397
            PAB: PAB0511(dys1)
            PFU: PF0292
            TKO: TK0671
            RCI: RCIX304(dys-1) RRC163(dys-2)
            APE: APE_0698.1
            SMR: Smar_1363
            IHO: Igni_0631
            SSO: SSO0967
            STO: ST1293
            SAI: Saci_1316
            MSE: Msed_1753
            PAI: PAE3487
            PIS: Pisl_0783
            PCL: Pcal_1171
            PAS: Pars_1970
            TPE: Tpen_0413
            NEQ: NEQ402
STRUCTURES  PDB: 1RLZ  1ROZ  1RQD  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.46
            ExPASy - ENZYME nomenclature database: 2.5.1.46
            ExplorEnz - The Enzyme Database: 2.5.1.46
            ERGO genome analysis and discovery system: 2.5.1.46
            BRENDA, the Enzyme Database: 2.5.1.46
///
ENTRY       EC 2.5.1.47                 Enzyme
NAME        cysteine synthase;
            O-acetyl-L-serine sulfhydrylase;
            O-acetyl-L-serine sulfohydrolase;
            O-acetylserine (thiol)-lyase;
            O-acetylserine (thiol)-lyase A;
            O-acetylserine sulfhydrylase;
            O3-acetyl-L-serine acetate-lyase (adding hydrogen-sulfide);
            acetylserine sulfhydrylase;
            cysteine synthetase;
            S-sulfocysteine synthase;
            3-O-acetyl-L-serine:hydrogen-sulfide
            2-amino-2-carboxyethyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     O3-acetyl-L-serine:hydrogen-sulfide
            2-amino-2-carboxyethyltransferase
REACTION    O3-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
            [RN:R00897]
ALL_REAC    R00897;
            (other) R03132 R03601 R04859
SUBSTRATE   O3-acetyl-L-serine [CPD:C00979];
            hydrogen sulfide [CPD:C00283]
PRODUCT     L-cysteine [CPD:C00097];
            acetate [CPD:C00033]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Some alkyl thiols, cyanide, pyrazole
            and some other heterocyclic compounds can act as acceptors. Not
            identical with EC 2.5.1.51 (beta-pyrazolylalanine synthase), EC
            2.5.1.52 (L-mimosine synthase) and EC 2.5.1.53 (uracilylalanine
            synthase).
REFERENCE   1  [PMID:4891157]
  AUTHORS   Becker MA, Kredich NM, Tomkins GM.
  TITLE     The purification and characterization of O-acetylserine
            sulfhydrylase-A from Salmonella typhimurium.
  JOURNAL   J. Biol. Chem. 244 (1969) 2418-27.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:2152186]
  AUTHORS   Hara S, Payne MA, Schnackerz KD, Cook PF.
  TITLE     A rapid purification procedure and computer-assisted sulfide ion
            selective electrode assay for O-acetylserine sulfhydrylase from
            Salmonella typhimurium.
  JOURNAL   Protein. Expr. Purif. 1 (1990) 70-6.
  ORGANISM  Salmonella typhimurium
REFERENCE   3
  AUTHORS   Ikegami, F., Kaneko, M., Lambein, F., Kuo, Y.-H. and Murakoshi, I.
  TITLE     Difference between uracilylalanine synthases and cysteine synthases
            in Pisum sativum.
  JOURNAL   Phytochemistry 26 (1987) 2699-2704.
  ORGANISM  Pisum sativum
REFERENCE   4
  AUTHORS   Murakoshi, I., Kaneko, M., Koide, C. and Ikegami, F.
  TITLE     Enzymatic-synthesis of the neuroexcitatory amino-acid quisqualic by
            cysteine synthase.
  JOURNAL   Phytochemistry 25 (1986) 2759-2763.
  ORGANISM  Quisqualis indica
REFERENCE   5  [PMID:11412097]
  AUTHORS   Tai CH, Burkhard P, Gani D, Jenn T, Johnson C, Cook PF.
  TITLE     Characterization of the allosteric anion-binding site of
            O-acetylserine sulfhydrylase.
  JOURNAL   Biochemistry. 40 (2001) 7446-52.
  ORGANISM  Salmonella typhimurium, Escherichia coli [GN:eco]
REFERENCE   6  [PMID:10995767]
  AUTHORS   Bettati S, Benci S, Campanini B, Raboni S, Chirico G, Beretta S,
            Schnackerz KD, Hazlett TL, Gratton E, Mozzarelli A.
  TITLE     Role of pyridoxal 5'-phosphate in the structural stabilization of
            O-acetylserine sulfhydrylase.
  JOURNAL   J. Biol. Chem. 275 (2000) 40244-51.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00272  Cysteine metabolism
            PATH: map00450  Selenoamino acid metabolism
            PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K01738  cysteine synthase
GENES       CEL: C17G1.7 F59A7.9 K10H10.2(beta-synthase)
            ATH: AT1G55880 AT2G43750(OASB) AT3G03630(CS26) AT3G04940(ATCYSD1)
                 AT3G22460 AT3G61440(ATCYSC1) AT5G28030
            OSA: 4327479 4327819 4332062 4334101 4335048 4352839
            CME: CMH036C CMT313C
            SCE: YGR012W YLR303W(MET17)
            AGO: AGOS_ADL031W AGOS_AEL161W AGOS_AGR021C
            PIC: PICST_30734(CYK2) PICST_31162 PICST_59891(CYK1)
            CAL: CaO19.7152(CYS4) CaO19_5574(CaO19.5574)
            CGR: CAGL0F08789g
            SPO: SPAC3A12.17c SPBC36.04
            ANI: AN1513.2 AN8057.2
            AFM: AFUA_4G03930 AFUA_5G02180 AFUA_8G05200
            AOR: AO090005000626 AO090102000276
            CNE: CNH02520 CNL05880
            UMA: UM06345.1
            DDI: DDB_0230066
            TET: TTHERM_00189320 TTHERM_00239430
            TCR: 507165.50 507793.20
            LMA: LmjF36.3590
            EHI: 124.t00003 189.t00001 328.t00005 487.t00002 89.t00017
            ECO: b2414(cysK) b2421(cysM)
            ECJ: JW2407(cysK) JW2414(cysM)
            ECE: Z3680(cysK) Z3686(cysM)
            ECS: ECs3286 ECs3292
            ECC: c2948(cysK) c2955(cysM)
            ECI: UTI89_C2747(cysK) UTI89_C2754(cysM)
            ECP: ECP_2438 ECP_2444
            ECV: APECO1_4125(cysM) APECO1_4131(cysK)
            ECW: EcE24377A_2701(cysK) EcE24377A_2707(cysM)
            ECX: EcHS_A2549(cysK) EcHS_A2557(cysM) EcHS_A2665(hisS)
            STY: STY0501 STY2666(cysK) STY2677(cysM)
            STT: t0418(cysM) t0427(cysK) t2401
            SPT: SPA0426(cysM) SPA0435(cysK) SPA2264
            SEC: SC0500 SC2428(cysK) SC2439(cysM)
            STM: STM0458 STM2430(cysK) STM2440(cysM)
            YPE: YPO2992(cysK) YPO3011(cysM) YPO3147 YPO4018(cysM)
            YPK: y1037 y1470(cysM) y1489(cysK) y4039(cysK)
            YPM: YP_0784(cysK1) YP_2617(cysK2) YP_2635(cysM1) YP_3381(cysM2)
            YPA: YPA_2182 YPA_2200 YPA_2642 YPA_4106
            YPN: YPN_0943 YPN_1372 YPN_1390 YPN_3666
            YPP: YPDSF_2100 YPDSF_2118
            YPS: YPTB0969 YPTB2714(cysK) YPTB2731(cysM)
            YPI: YpsIP31758_1303(cysM) YpsIP31758_1318(cysK)
            YEN: YE1198(cysM) YE1208(cysK)
            SFL: SF2469(cysK) SF2476(cysM)
            SFX: S2615(cysK) S2622(cysM)
            SFV: SFV_2466(cysK) SFV_2474(cysM)
            SSN: SSON_2503(cysK) SSON_2510(cysM)
            SBO: SBO_2438(cysK) SBO_2446(cysM)
            SDY: SDY_2611(cysK) SDY_2617(cysM)
            ECA: ECA0886(cysM) ECA0894(cysK) ECA1156
            PLU: plu1391(cysM) plu1395(cysK) plu3861
            BUC: BU066(cysK)
            BAS: BUsg063(cysK)
            SGL: SG1700 SG1705
            BFL: Bfl508(cysK)
            BPN: BPEN_525(cysK)
            HIN: HI1103(cysK)
            HIT: NTHI1269(cysK)
            HDU: HD0896(cysK)
            HSO: HS_0369(cysK)
            PMU: PM1693(cysK)
            MSU: MS1770(cysK)
            APL: APL_0248(cysK)
            XFA: XF0128 XF0831
            XFT: PD0098(cysK) PD1841(cysK)
            XCC: XCC0578(cysM) XCC3182(cysK)
            XCB: XC_0982 XC_3655
            XCV: XCV3459(cysK) XCV3745
            XAC: XAC3341(cysK) XAC3628(cysM)
            XOO: XOO0758(cysM) XOO3409(cysK)
            XOM: XOO_0688(XOO0688) XOO_3209(XOO3209)
            VCH: VC0537 VC0968 VC1061
            VCO: VC0395_A0064(cysM) VC0395_A0489(cysK)
            VVU: VV1_0209 VV1_3153
            VVY: VV0979 VV1133
            VPA: VP0797 VP0946
            VFI: VF1579 VF1893
            PPR: PBPRA0864 PBPRA0969(cysK)
            PAE: PA0932(cysM) PA1061 PA2104 PA2709(cysK)
            PAU: PA14_29110(cysK) PA14_50660 PA14_52210(cysM)
            PAP: PSPA7_3986(cysK) PSPA7_4578(cysM)
            PPU: PP_1654(cysM) PP_4571(cysK)
            PST: PSPTO_1692(cysM) PSPTO_3902(cysK)
            PSB: Psyr_1583 Psyr_3697
            PSP: PSPPH_1566(cysK) PSPPH_3718(cysM)
            PFL: PFL_1287 PFL_1519(cysK) PFL_4448(cysM)
            PFO: Pfl_1235 Pfl_1413 Pfl_3248 Pfl_4219
            PEN: PSEEN1362(cysM) PSEEN2152 PSEEN4013(cysK)
            PAR: Psyc_0346(cysM)
            PCR: Pcryo_0380
            ACI: ACIAD1662(cysK) ACIAD3071(cysM)
            SON: SO_2903(cysK) SO_3598(cysM)
            SDN: Sden_0590 Sden_2013 Sden_2520
            SFR: Sfri_1878 Sfri_2468
            SAZ: Sama_1508
            SBL: Sbal_0998 Sbal_2663
            SLO: Shew_2382
            SHE: Shewmr4_1500 Shewmr4_3011
            SHM: Shewmr7_1567 Shewmr7_3091
            SHN: Shewana3_1561 Shewana3_3188
            SHW: Sputw3181_1639 Sputw3181_3159
            ILO: IL2163(cysK)
            CPS: CPS_2251(cysK)
            PHA: PSHAa1918(cysK)
            PAT: Patl_0400 Patl_2517
            SDE: Sde_2239 Sde_2901
            PIN: Ping_2438
            MAQ: Maqu_2240 Maqu_3690
            CBU: CBU_2024
            LPN: lpg2951
            LPF: lpl2880(cysK)
            LPP: lpp3022(cysK)
            MCA: MCA1022(cysK) MCA1899(cysM)
            TCX: Tcr_1306
            NOC: Noc_0797 Noc_2604
            AEH: Mlg_1352
            HHA: Hhal_0556
            HCH: HCH_01805(cysM) HCH_02622(cysK) HCH_06702
            CSA: Csal_1086 Csal_1467 Csal_1636
            ABO: ABO_1023(cysK) ABO_1626(cysM)
            AHA: AHA_1504(cysM) AHA_3038(cysK)
            BCI: BCI_0068(cysK)
            RMA: Rmag_0772
            VOK: COSY_0708(cysK)
            NME: NMB0763
            NMA: NMA0974(cysK)
            NMC: NMC0715(cysK)
            NGO: NGO0340
            CVI: CV_3025(cysM) CV_3561(cysK) CV_3597
            RSO: RSc0917(cysM) RSp0276(cysK1) RSp0417(cysK2)
            REU: Reut_A1804 Reut_A2337 Reut_A2560 Reut_B4743
            REH: H16_A0807(cysK1) H16_A1903(cysK2) H16_B2378(cysK4)
            RME: Rmet_0731 Rmet_1117 Rmet_3819
            BMA: BMA0418(cysM) BMA1621
            BMV: BMASAVP1_A2562(cysM)
            BML: BMA10299_A0938(cysM)
            BMN: BMA10247_0211(cysM)
            BXE: Bxe_A0990 Bxe_C0241
            BUR: Bcep18194_A4168 Bcep18194_A5010
            BCN: Bcen_0576 Bcen_5540
            BCH: Bcen2424_1055 Bcen2424_5905
            BAM: Bamb_0931
            BPS: BPSL1716 BPSL2215 BPSL2507(cysM)
            BPM: BURPS1710b_2157 BURPS1710b_2647 BURPS1710b_2984(cysM)
            BPL: BURPS1106A_2021 BURPS1106A_2937(cysM)
            BPD: BURPS668_2001 BURPS668_2874(cysM)
            BTE: BTH_I1646(cysM) BTH_I1970
            BPE: BP0958(cysM)
            BPA: BPP3120(cysM)
            BBR: BB3460(cysM)
            RFR: Rfer_1520 Rfer_2378 Rfer_3460
            POL: Bpro_3360 Bpro_3726
            PNA: Pnap_0562 Pnap_3172 Pnap_3445
            AAV: Aave_1987
            AJS: Ajs_2900
            VEI: Veis_1026 Veis_1207
            MPT: Mpe_A0450 Mpe_A1132(cysM)
            HAR: HEAR2568(cysM)
            MMS: mma_2663(cysK)
            NEU: NE1443(cysM)
            NET: Neut_2071
            NMU: Nmul_A2072 Nmul_A2221
            EBA: ebA4678(cysK) ebA896(cysM)
            AZO: azo1077(cysM) azo2399(cysK)
            DAR: Daro_1287 Daro_2138 Daro_4128
            TBD: Tbd_0964
            MFA: Mfla_1861
            HPY: HP0107(cysK)
            HPJ: jhp0099(cysK)
            HPA: HPAG1_0107
            HHE: HH0063(cysK_1) HH0849(cysK_2)
            HAC: Hac_1465(cysK)
            WSU: WS1188
            TDN: Tmden_0154 Tmden_0433 Tmden_0765
            CJE: Cj0912c(cysM)
            CJR: CJE0990(cysK)
            CJJ: CJJ81176_0920(cysK)
            CJU: C8J_0848(cysM)
            CJD: JJD26997_0902(cysK)
            CFF: CFF8240_0922(cysK)
            CCV: CCV52592_0717(cysK)
            CHA: CHAB381_0889(cysK)
            CCO: CCC13826_0081(cysK) CCC13826_1774(cysK)
            ABU: Abu_2171(cysK1) Abu_2299(cysK2)
            NIS: NIS_1469(cysK)
            SUN: SUN_0388
            GSU: GSU0535(cysK) GSU3158(cysM)
            GME: Gmet_0264 Gmet_1558 Gmet_2988
            PCA: Pcar_1534 Pcar_1718 Pcar_2430 Pcar_3005
            PPD: Ppro_1832
            DVU: DVU0663(cysK)
            DDE: Dde_3080
            BBA: Bd1710 Bd1744(cysM)
            DPS: DP1240
            ADE: Adeh_1280 Adeh_2316 Adeh_2668
            MXA: MXAN_0992 MXAN_1571(cysK) MXAN_4171
            SAT: SYN_00446 SYN_01253
            SFU: Sfum_2681
            PUB: SAR11_0789(cysK)
            MLO: mll4616 mlr0353 mlr4651
            MES: Meso_1424
            SME: SMc00421(cysK1) SMc01174(cysK2)
            ATU: Atu0312(cysK) Atu1217(cysK)
            ATC: AGR_C_2247 AGR_C_543
            RET: RHE_CH00325(cysK1) RHE_CH01775(cysK2)
            RLE: RL0340(cysK) RL1979(cysB)
            BME: BMEI0101 BMEI0933 BMEI1166
            BMF: BAB1_0813 BAB1_1073 BAB1_1968
            BMS: BR0793 BR1053
            BMB: BruAb1_0807 BruAb1_1058
            BOV: BOV_1018 BOV_1893(cysK)
            BJA: bll0236 bll4453(cysK) bll4682(cysK)
            BRA: BRADO3909(cysB) BRADO3987(cysK)
            BBT: BBta_0633 BBta_3927(cysB) BBta_4022 BBta_4360(cysK)
            RPA: RPA0557(cysK) RPA2565 RPA2568
            RPB: RPB_0477 RPB_2907 RPB_3087
            RPC: RPC_2553 RPC_2594 RPC_3639
            RPD: RPD_0343 RPD_2564 RPD_4194
            RPE: RPE_2734 RPE_2774 RPE_3624
            NWI: Nwi_1525 Nwi_1794
            NHA: Nham_1773 Nham_2067
            CCR: CC_1426 CC_3625
            SIL: SPO1921 SPO2246(cysK)
            RSP: RSP_1109(cysK) RSP_2147(cysK)
            RDE: RD1_2299(cysB) RD1_2941(cysK) RD1_3674
            MMR: Mmar10_1493 Mmar10_3067
            HNE: HNE_0049(cysK) HNE_0181 HNE_1420
            ZMO: ZMO0748(cysK) ZMO0821(cysZ)
            NAR: Saro_2103
            SAL: Sala_1045
            ELI: ELI_05900
            GOX: GOX0660 GOX1601
            GBE: GbCGDNIH1_0510 GbCGDNIH1_0906 GbCGDNIH1_1397
            RRU: Rru_A0787 Rru_A1616 Rru_A3794
            MAG: amb0199 amb1300
            MGM: Mmc1_2102 Mmc1_3416
            ABA: Acid345_2096 Acid345_2500
            SUS: Acid_0758 Acid_5884
            BSU: BG10136(cysK) BG12290(yrhA) BG13872(ytkP)
            BHA: BH0088(cysK) BH3271
            BAN: BA0067(cysK-1) BA1831(cysK-2) BA4601(cysM)
            BAR: GBAA0067(cysK-1) GBAA1831(cysK-2) GBAA4601(cysM)
            BAA: BA_0657 BA_2337 BA_5042
            BAT: BAS0067 BAS1697 BAS4269
            BCE: BC0075 BC1763 BC4367
            BCA: BCE_0066(cysK) BCE_1919(cysK) BCE_4455(cysM)
            BCZ: BCZK0063(cysK) BCZK1653(cysK) BCZK4117(cysM)
            BCY: Bcer98_3925
            BTK: BT9727_0063(cysK) BT9727_1678(cysK) BT9727_4106(cysM)
            BTL: BALH_0066(cysK) BALH_1608(cysK) BALH_3958(cysM)
            BLI: BL00857(cysK) BL02019(yrhA)
            BLD: BLi00089(cysK) BLi02854(yrhA) BLi03148(ytkP)
            BCL: ABC0109(cysK) ABC1944 ABC2792
            BAY: RBAM_000840(cysK) RBAM_027070(ytkP)
            BPU: BPUM_0057(cysK) BPUM_2361(yrhA) BPUM_2643(ytkP)
            OIH: OB0084 OB1108(cysK) OB1703
            GKA: GK0065 GK1525 GK2541
            SAU: SA0418(cysM) SA0471(cysK)
            SAV: SAV0459(cysM) SAV0513(cysK)
            SAM: MW0414(cysM) MW0468(cysK)
            SAR: SAR0459 SAR0514
            SAS: SAS0417 SAS0470
            SAC: SACOL0502 SACOL0557(cysK)
            SAB: SAB0055 SAB0409 SAB0462
            SAA: SAUSA300_0433(cysM) SAUSA300_0491(cysK)
            SAO: SAOUHSC_00421 SAOUHSC_00488
            SEP: SE2270 SE2324
            SER: SERP0094 SERP0152(cysK)
            SHA: SH2497(cysK) SH2549(cysM)
            SSP: SSP0252 SSP2243
            LMO: lmo0223(cysK)
            LMF: LMOf2365_0234(cysK)
            LIN: lin0255(cysK)
            LWE: lwe0186(cysK)
            LLA: L0088(cysM) L0089(cysK)
            LLC: LACR_0537 LACR_0832
            LLM: llmg_0508 llmg_1775(cysK)
            SPY: SPy_1618(cysM)
            SPZ: M5005_Spy_1329(cysM)
            SPM: spyM18_1627(cysK)
            SPG: SpyM3_1363(cysM)
            SPS: SPs0499
            SPH: MGAS10270_Spy1445(cysM)
            SPI: MGAS10750_Spy1438(cysM)
            SPJ: MGAS2096_Spy1350(cysM)
            SPK: MGAS9429_Spy1324(cysM)
            SPF: SpyM50462(cysM)
            SPA: M6_Spy1375
            SPB: M28_Spy1370(cysM)
            SPN: SP_2210
            SPR: spr2015(cycK)
            SPD: SPD_2037(cysK)
            SAG: SAG0334(cysK)
            SAN: gbs0322(cysK)
            SAK: SAK_0404
            SMU: SMU.496(cysK)
            STC: str0366(cysM1) str0846(cysM2)
            STL: stu0366(cysM1) stu0846(cysM2)
            SSA: SSA_1839(cysK)
            SGO: SGO_0606(cysK)
            LPL: lp_0256(cysK)
            LAC: LBA1087 LBA1088 LBA1238
            LSL: LSL_0026(cysK) LSL_1718(cysK)
            LDB: Ldb1325(cysK2) Ldb1458(cysK1)
            LBU: LBUL_1235 LBUL_1354
            LCA: LSEI_0480
            EFA: EF0289 EF1584(cysK)
            OOE: OEOE_1759
            STH: STH1137
            CAC: CAC0931 CAC2235(cysK)
            CPE: CPE0177(cysK) CPE1322(cysK)
            CPF: CPF_0170 CPF_1529(cysK)
            CPR: CPR_0166 CPR_1322(cysK)
            CTC: CTC01153 CTC01343
            CNO: NT01CX_0572(cysK)
            CDF: CD1665(cysK)
            CBO: CBO0205(cysK1) CBO0724(cysK) CBO1179(cysK2)
            CBA: CLB_0246(cysK-1) CLB_1210(cysK-2)
            CBH: CLC_0261(cysK-1) CLC_1222(cysK-2)
            CBF: CLI_0270(cysK-1) CLI_1261(cysK-2)
            CBE: Cbei_0622
            CKL: CKL_1003(cysK)
            AMT: Amet_0057
            CHY: CHY_0808(cysK)
            DSY: DSY1356 DSY4189
            SWO: Swol_1438
            TTE: TTE1134(cysK) TTE2478(cysK2)
            MTA: Moth_1706 Moth_1971
            MTU: Rv0848(cysK2) Rv1336(cysM) Rv2334(cysK1) Rv3684
            MTC: MT1377(cysM) MT2397(cysK) MT3786
            MBO: Mb0871(cysK2) Mb1371(cysM) Mb2362(cysK1)
            MBB: BCG_0900(cysK2) BCG_1398(cysM) BCG_2356(cysK1)
            MLE: ML0839(cysK)
            MPA: MAP0390c MAP2123(cysK)
            MAV: MAV_2052(cysK)
            MSM: MSMEG_4905(cysM) MSMEG_6203
            MVA: Mvan_4291 Mvan_4674
            MGI: Mflv_2043 Mflv_2354
            MMC: Mmcs_3848 Mmcs_4149 Mmcs_4197 Mmcs_4827
            MKM: Mkms_3922 Mkms_4224
            MJL: Mjls_3834 Mjls_4380
            CGL: NCgl2055(cgl2136) NCgl2473(cgl2562)
            CGB: cg2833(cysK)
            CEF: CE1418 CE2446
            CDI: DIP1890
            CJK: jk0394(cysK)
            NFA: nfa10910(cysM) nfa51510 pnf1800
            RHA: RHA1_ro01436(cysM) RHA1_ro02027 RHA1_ro10436
            SCO: SCO1028(SCG20A.08c) SCO2910(SCE19A.10c)
            SMA: SAV1435(cysK1) SAV5164(cysM2) SAV7162(cysK3)
            AAU: AAur_2416(cysK)
            PAC: PPA0963
            NCA: Noca_0939 Noca_1312
            TFU: Tfu_2368
            FRA: Francci3_0868 Francci3_2427 Francci3_3460
            FAL: FRAAL1500(cysM) FRAAL3176 FRAAL3350(cysK)
            KRA: Krad_1082
            SEN: SACE_1206(cysM) SACE_1726 SACE_2893(cysK) SACE_3013(cysK3)
                 SACE_4282(cysK3) SACE_6328 SACE_6924
            RXY: Rxyl_0746
            FNU: FN1055 FN1220
            RBA: RB10170(cysM) RB10894(thrC) RB4386 RB6932(cysK)
            LIL: LA1719(cysK) LA2097(cysM)
            LIC: LIC11820 LIC12082(cysK)
            LBJ: LBJ_1097(cysK-1) LBJ_1227(cysK-2) LBJ_1911(cysK-3)
            LBL: LBL_1148(cysK-1) LBL_1278(cysK-2) LBL_1373(cysK-3)
            SYN: sll0712(cysM) slr1842(cysK)
            SYW: SYNW0673(cysK1) SYNW2222(cysK2)
            SYC: syc1337_c(cysM) syc2453_d(cysM)
            SYF: Synpcc7942_0171 Synpcc7942_1466 Synpcc7942_B2623
                 Synpcc7942_B2664
            SYD: Syncc9605_1996 Syncc9605_2365
            SYE: Syncc9902_0325 Syncc9902_0664
            SYG: sync_0620(cysK-1) sync_2577(cysK-2)
            SYR: SynRCC307_0121(cysK) SynRCC307_0267(cysK)
            SYX: SynWH7803_0585(cysK) SynWH7803_2234(cysK)
            CYA: CYA_1206 CYA_1702(cysK)
            CYB: CYB_1982(cysK) CYB_2315
            TEL: tll2311(cysM) tlr0504(cysK)
            GVI: gll0765 glr0798(cysK)
            ANA: all1169 all2521 alr4416 alr4552
            AVA: Ava_0452 Ava_1347 Ava_2508 Ava_5019
            PMA: Pro0143(cysK) Pro0403(cysK)
            PMM: PMM0123(cysK2) PMM0407(cysK1)
            PMT: PMT0224(cysK1) PMT1978(cysK2)
            PMN: PMN2A_1490 PMN2A_1741
            PMI: PMT9312_0126 PMT9312_0402
            PMB: A9601_01411 A9601_04571
            PMC: P9515_01371 P9515_04681
            PMF: P9303_21201 P9303_26311
            PMG: P9301_01401 P9301_04261
            PMH: P9215_04831(cysK)
            PME: NATL1_01951 NATL1_04581
            TER: Tery_1235 Tery_4742
            BTH: BT_1852 BT_3080
            BFR: BF3430 BF4576
            BFS: BF3251 BF4362(cysK)
            SRU: SRU_2039 SRU_2787
            CHU: CHU_0684(cysM)
            GFO: GFO_1532(cysKM)
            FJO: Fjoh_1491
            CTE: CT0700(cysK)
            CCH: Cag_1258
            CPH: Cpha266_2280
            PVI: Cvib_0346
            PLT: Plut_0234 Plut_1551
            DET: DET1135(cysK)
            DEH: cbdb_A1063(cysK)
            DRA: DR_0789
            DGE: Dgeo_1657
            TTH: TTC1636
            TTJ: TTHA0347
            AAE: aq_1556(cysM)
            TMA: TM0665
            MAC: MA2720(cysK)
            MBA: Mbar_A2422
            MBU: Mbur_0413
            MHU: Mhun_2182
            MST: Msp_0449
            MSI: Msm_0271
            HAL: VNG0606G(yrhA) VNG1301G(cysK)
            HMA: rrnAC0137(cysK2) rrnAC1236(cysK1)
            HWA: HQ2556A(cysK)
            NPH: NP3116A(cysK_2) NP4748A(cysK_1)
            TAC: Ta0535
            TVO: TVN0589
            PTO: PTO0151 PTO0953
            PAB: PAB0250
            PFU: PF1858
            TKO: TK1687
            APE: APE_1586
            SSO: SSO0360(cysM)
            STO: ST1380
            SAI: Saci_1475(cysM)
            PAI: PAE1051
STRUCTURES  PDB: 1O58  1VE1  1Y7L  1Z7W  1Z7Y  2BHS  2BHT  2EGU  2ISQ  2Q3B  
                 2Q3C  2Q3D  2V03  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.47
            ExPASy - ENZYME nomenclature database: 2.5.1.47
            ExplorEnz - The Enzyme Database: 2.5.1.47
            ERGO genome analysis and discovery system: 2.5.1.47
            BRENDA, the Enzyme Database: 2.5.1.47
            CAS: 37290-89-4
///
ENTRY       EC 2.5.1.48                 Enzyme
NAME        cystathionine gamma-synthase;
            O-succinyl-L-homoserine succinate-lyase (adding cysteine);
            O-succinylhomoserine (thiol)-lyase;
            homoserine O-transsuccinylase;
            O-succinylhomoserine synthase;
            O-succinylhomoserine synthetase;
            cystathionine synthase;
            cystathionine synthetase;
            homoserine transsuccinylase;
            4-O-succinyl-L-homoserine:L-cysteine
            S-(3-amino-3-carboxypropyl)transferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     O4-succinyl-L-homoserine:L-cysteine
            S-(3-amino-3-carboxypropyl)transferase
REACTION    O4-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate
            [RN:R03260]
ALL_REAC    R03260;
            (other) R00999 R01288 R02508 R03132 R04944 R04945 R04946
SUBSTRATE   O4-succinyl-L-homoserine;
            L-cysteine [CPD:C00097]
PRODUCT     L-cystathionine [CPD:C02291];
            succinate [CPD:C00042]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also reacts with hydrogen sulfide and
            methanethiol as replacing agents, producing homocysteine and
            methionine, respectively. In the absence of thiol, can also catalyse
            beta,gamma-elimination to form 2-oxobutanoate, succinate and
            ammonia.
REFERENCE   1  [PMID:5340123]
  AUTHORS   Flavin M, Slaughter C.
  TITLE     Enzymatic synthesis of homocysteine or methionine directly from
            O-succinyl-homoserine.
  JOURNAL   Biochim. Biophys. Acta. 132 (1967) 400-5.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:5922970]
  AUTHORS   Kaplan MM, Flavin M.
  TITLE     Cystathionine gamma-synthetase of Salmonella. Catalytic properties
            of a new enzyme in bacterial methionine biosynthesis.
  JOURNAL   J. Biol. Chem. 241 (1966) 4463-71.
  ORGANISM  Salmonella typhimurium, Escherichia coli [GN:eco]
REFERENCE   3  [PMID:6016326]
  AUTHORS   Wiebers JL, Garner HR.
  TITLE     Homocysteine and cysteine synthetases of Neurospora crassa.
            Purification, properties, and feedback control of activity.
  JOURNAL   J. Biol. Chem. 242 (1967) 12-23.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   4  [PMID:12325384]
  AUTHORS   Wiebers JL, Garner HR.
  TITLE     Acyl derivatives of homoserine as substrates for homocysteine
            synthesis in Neurospora crassa, yeast, and Escherichia coli.
  JOURNAL   J. Biol. Chem. 242 (1967) 5644-9.
  ORGANISM  Escherichia coli [GN:eco], Neurospora crassa [GN:dncr]
REFERENCE   5  [PMID:9843488]
  AUTHORS   Clausen T, Huber R, Prade L, Wahl MC, Messerschmidt A.
  TITLE     Crystal structure of Escherichia coli cystathionine gamma-synthase
            at 1.5 A resolution.
  JOURNAL   EMBO. J. 17 (1998) 6827-38.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:9531508]
  AUTHORS   Ravanel S, Gakiere B, Job D, Douce R.
  TITLE     Cystathionine gamma-synthase from Arabidopsis thaliana: purification
            and biochemical characterization of the recombinant enzyme
            overexpressed in Escherichia coli.
  JOURNAL   Biochem. J. 331 ( Pt 2) (1998) 639-48.
  ORGANISM  Escherichia coli [GN:eco], Arabidopsis thaliana [GN:ath]
PATHWAY     PATH: map00271  Methionine metabolism
            PATH: map00272  Cysteine metabolism
            PATH: map00450  Selenoamino acid metabolism
            PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K01739  cystathionine gamma-synthase
GENES       XLA: 494673(LOC494673)
            XTR: 394634(MGC75946)
            ATH: AT3G01120(MTO1)
            OSA: 4332956
            CME: CMF156C
            SCE: YJR130C(STR2) YML082W
            AGO: AGOS_AER164C
            PIC: PICST_36608 PICST_59680
            CAL: CaO19.1033 CaO19_7297(CaO19.7297)
            CGR: CAGL0I01276g CAGL0M00550g
            SPO: SPAC23A1.14c SPBC15D4.09c
            ANI: AN3456.2
            AFM: AFUA_3G05480
            AOR: AO090003001113 AO090020000019
            CNE: CNC01220
            UMA: UM04053.1
            LMA: LmjF35.3230
            EHI: 132.t00018 389.t00003 395.t00003
            ECO: b3939(metB)
            ECJ: JW3910(metB)
            ECE: Z5494(metB)
            ECS: ECs4868
            ECC: c4892(metB)
            ECI: UTI89_C4524(metB)
            ECP: ECP_4148
            ECV: APECO1_2532(metB)
            ECW: EcE24377A_4479(metB)
            ECX: EcHS_A4172
            STY: STY3769(metB)
            STT: t3518(metB)
            SPT: SPA3943(metB)
            SEC: SC3991(metB)
            STM: STM4100(metB)
            YPE: YPO0115(metB)
            YPM: YP_0117(metC1)
            YPA: YPA_0264
            YPN: YPN_3739
            YPS: YPTB0105(metB)
            YPI: YpsIP31758_0121(metB)
            YEN: YE1469(metB)
            SFL: SF4017(metB)
            SFX: S3730(metB)
            SFV: SFV_4009(metB)
            SSN: SSON_4113(metB)
            SBO: SBO_3959(metB)
            SDY: SDY_3774(metB)
            ECA: ECA4252(metB)
            PLU: plu4756(metB)
            SGL: SG2163
            ENT: Ent638_1769 Ent638_4035
            SPE: Spro_1626 Spro_4786
            BFL: Bfl598(metB)
            BPN: BPEN_620(metB)
            HIN: HI0086(metB)
            HIT: NTHI0100(metB)
            HSO: HS_1345(metB)
            PMU: PM0995(metB)
            MSU: MS1627(metC)
            APL: APL_0683(metB)
            ASU: Asuc_1846
            XFA: XF0864
            XFT: PD1812(metB)
            XCC: XCC2856(metB)
            XCB: XC_1252
            XCV: XCV3176(metB)
            XAC: XAC3039(metB)
            XOO: XOO1818(metB)
            XOM: XOO_1717(XOO1717)
            VCH: VC2683
            VCO: VC0395_A2256(metB)
            VVU: VV1_1364
            VVY: VV3008
            VPA: VP2765
            VFI: VF2267
            PPR: PBPRA0261
            PPU: PP_0659(metB)
            PPF: Pput_0693 Pput_3760
            PSB: Psyr_1669
            PFO: Pfl_3249
            PEN: PSEEN4039
            PMY: Pmen_2710
            PAR: Psyc_0792(metZ)
            PCR: Pcryo_0798
            PRW: PsycPRwf_1730
            SON: SO_4056(metB)
            SDN: Sden_0615
            SFR: Sfri_3551
            SAZ: Sama_3171
            SBL: Sbal_3776
            SBM: Shew185_0536
            SLO: Shew_0520
            SPC: Sputcn32_0616
            SSE: Ssed_4041
            SPL: Spea_0560 Spea_2664
            SHE: Shewmr4_3439
            SHM: Shewmr7_0512
            SHN: Shewana3_3614
            SHW: Sputw3181_3554
            CPS: CPS_0455(metB)
            PHA: PSHAa2723(metB)
            PAT: Patl_4021
            SDE: Sde_2071
            PIN: Ping_0757
            MAQ: Maqu_1551 Maqu_1897
            TCX: Tcr_0809
            NOC: Noc_0842 Noc_1151
            AEH: Mlg_1615
            HHA: Hhal_1797
            CSA: Csal_1268
            MMW: Mmwyl1_3697
            AHA: AHA_0589(metB)
            BCI: BCI_0163(metB)
            RMA: Rmag_1002
            NME: NMB0802
            NMA: NMA1012
            CVI: CV_1934(metY) CV_2725(metZ) CV_3394 CV_4049(metB)
            RSO: RSp0781(metB)
            REU: Reut_A2298
            REH: H16_A2606(metB)
            RME: Rmet_2459
            BVI: Bcep1808_4470
            BUR: Bcep18194_B2117 Bcep18194_B2807
            BCN: Bcen_4401
            BCH: Bcen2424_3966
            BAM: Bamb_3356 Bamb_4283 Bamb_6437
            BPM: BURPS1710b_A2511
            BTE: BTH_II1484
            PNU: Pnuc_0779
            RFR: Rfer_2682
            POL: Bpro_1608 Bpro_2831
            PNA: Pnap_1093
            AAV: Aave_1864
            AJS: Ajs_2735
            VEI: Veis_0265
            NET: Neut_1159
            NMU: Nmul_A1905
            DAR: Daro_0877
            TBD: Tbd_1907
            MFA: Mfla_1691
            HPY: HP0106(metB)
            HPJ: jhp0098(metB)
            HPA: HPAG1_0106
            HHE: HH0062(metB)
            HAC: Hac_1464(metB)
            ABU: Abu_1723(metC1) Abu_1724(metC2)
            GUR: Gura_3857 Gura_3858
            PPD: Ppro_1830 Ppro_1831
            ADE: Adeh_3143 Adeh_3707
            AFW: Anae109_3196
            SFU: Sfum_2670
            PLA: Plav_0409
            SME: SMc02595(metB)
            SMD: Smed_0133 Smed_2201 Smed_4014
            RET: RHE_PE00244(mdeAe) RHE_PF00019(mdeAf) RHE_PF00461(vbsL)
            RLE: pRL110363 pRL120373
            BME: BMEI0103
            BMF: BAB1_1966
            OAN: Oant_0355 Oant_1017 Oant_4374
            RPC: RPC_4904
            RPD: RPD_0903
            RPE: RPE_4877
            NWI: Nwi_0139 Nwi_0592
            NHA: Nham_0219 Nham_0684
            XAU: Xaut_0471
            SIT: TM1040_1264 TM1040_1938
            RSP: RSP_1851(metZ) RSP_2917
            RSH: Rsph17029_0500
            RSQ: Rsph17025_0638 Rsph17025_0780
            JAN: Jann_2286
            PDE: Pden_5069
            MMR: Mmar10_1549 Mmar10_1859 Mmar10_2620
            NAR: Saro_2665
            SAL: Sala_1086
            SWI: Swit_0856 Swit_3154
            ACR: Acry_2070
            RRU: Rru_A0098 Rru_A0786 Rru_A3214
            MGM: Mmc1_1942
            ABA: Acid345_1913 Acid345_1981 Acid345_1982 Acid345_2499
            SUS: Acid_3250 Acid_4794 Acid_5643
            BSU: BG13162(yjcI)
            BHA: BH0542 BH1627(metB)
            BCE: BC4253
            BCY: Bcer98_2985 Bcer98_2986 Bcer98_3084
            BLI: BL02660
            BLD: BLi01289(yjcI)
            BCL: ABC0021 ABC1867(metI) ABC1945
            OIH: OB2949
            GKA: GK0866
            SAU: SA0347 SA0419(metB)
            SAV: SAV0359 SAV0460(yrhB)
            SAM: MW0335 MW0415(metB)
            SAR: SAR0356 SAR0460
            SAS: SAS0335 SAS0418
            SAC: SACOL0431 SACOL0503
            SAB: SAB0309c SAB0410
            SAJ: SaurJH9_0406 SaurJH9_0407 SaurJH9_0482
            SAH: SaurJH1_0416 SaurJH1_0417 SaurJH1_0495
            SEP: SE2323 SE2379
            SER: SERP0037 SERP0095
            SHA: SH2548(metB) SH2635
            SSP: SSP0253 SSP2413
            LMO: lmo1680
            LIN: lin1788
            LWE: lwe1698
            LLA: L0102(metB1)
            LLM: llmg_2181(metB1)
            SPZ: M5005_Spy_0146(metB)
            SPN: SP_1525
            SPR: spr1377(metB)
            SMU: SMU.1675(metB)
            STC: str0352(metB1)
            STL: stu0352(metB1)
            SSA: SSA_1737(metB)
            SGO: SGO_1159(guaC) SGO_1636
            LPL: lp_2634(metB)
            LRE: Lreu_0293
            STH: STH2363
            CAC: CAC0390 CAC0930(metB)
            CPE: CPE0176(metB)
            CTH: Cthe_1559 Cthe_2799
            CBE: Cbei_0239 Cbei_0240 Cbei_0629
            CKL: CKL_1002(metB1) CKL_1632(metB2)
            AMT: Amet_3706 Amet_3707
            DSY: DSY3983
            TTE: TTE1574(metC2)
            MTA: Moth_1989 Moth_1990
            MTU: Rv0391(metZ) Rv1079(metB)
            MTC: MT0402(metZ) MT1110(metB)
            MBO: Mb1108(metB)
            MBB: BCG_1137(metB)
            MLE: ML2394(metB)
            MPA: MAP1026(metB) MAP3873(metZ)
            MSM: MSMEG_0769(metZ) MSMEG_2394 MSMEG_5265
            MVA: Mvan_0688 Mvan_4670
            MGI: Mflv_0219 Mflv_2046
            MMC: Mmcs_0526 Mmcs_4146
            MKM: Mkms_0538 Mkms_4221
            MJL: Mjls_0516 Mjls_4377
            CGL: NCgl2360(cgl2446)
            CGB: cg2687(metB)
            CEF: CE2343(metB)
            CJK: jk0055(metB)
            NFA: nfa48270(metB)
            RHA: RHA1_ro05845(metB)
            SCO: SCO4958(2SCK31.18)
            SMA: SAV3305(metB)
            LXX: Lxx03230(metB)
            ART: Arth_2849 Arth_3061 Arth_3860
            AAU: AAur_0889(metB) AAur_3037(metB) AAur_3664(metB)
            NCA: Noca_0976
            TFU: Tfu_0440 Tfu_0632
            FRA: Francci3_0374 Francci3_1998
            FAL: FRAAL0783(metB)
            KRA: Krad_1092
            SEN: SACE_0902(metB)
            STP: Strop_0920
            BLO: BL1155(metB)
            BAD: BAD_0491(metB)
            RXY: Rxyl_2537
            FNU: FN1745
            RBA: RB6442(metB)
            LIL: LA0113(metC)
            LIC: LIC10101(met-7)
            LBJ: LBJ_0092
            LBL: LBL_0043
            SYW: SYNW0674 SYNW0675(metB) SYNW0851(cysD)
            SYD: Syncc9605_1994 Syncc9605_1995
            SYE: Syncc9902_0665 Syncc9902_0666
            SYG: sync_0622 sync_0623(metB)
            AVA: Ava_4155
            PMA: Pro0404(metC) Pro0405(metC)
            PMM: PMM0408 PMM0409(metB)
            PMT: PMT0225 PMT0226(metB)
            PMN: PMN2A_1742
            PMI: PMT9312_0403
            PMB: A9601_04581 A9601_04591(metB)
            PMC: P9515_04691 P9515_04701(metB)
            PMF: P9303_21181(metB) P9303_21191
            PMG: P9301_04271 P9301_04281(metB)
            PMH: P9215_04851
            PME: NATL1_04591 NATL1_04601(metB)
            SRU: SRU_1161
            FJO: Fjoh_2131
            CCH: Cag_1264
            CPH: Cpha266_0732
            PVI: Cvib_1358
            PLT: Plut_1548 Plut_1563
            RRS: RoseRS_1055 RoseRS_4038 RoseRS_4472
            RCA: Rcas_0823 Rcas_3473
            DGE: Dgeo_1004
            TMA: TM1270
            HAL: VNG1172G(metB)
            HMA: rrnAC2414(metB)
            NPH: NP4746A(metB)
            TAC: Ta0531
            TVO: TVN1007
            PTO: PTO1102
            PAB: PAB0605(metB)
            TKO: TK1449
            APE: APE_2068
            IHO: Igni_1102
            SSO: SSO2368(metB)
            STO: ST0506
            SAI: Saci_0971
            MSE: Msed_0673
            PAI: PAE2420
            PIS: Pisl_0881
            PCL: Pcal_0316
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.48
            ExPASy - ENZYME nomenclature database: 2.5.1.48
            ExplorEnz - The Enzyme Database: 2.5.1.48
            ERGO genome analysis and discovery system: 2.5.1.48
            BRENDA, the Enzyme Database: 2.5.1.48
            CAS: 9030-70-0
///
ENTRY       EC 2.5.1.49                 Enzyme
NAME        O-acetylhomoserine aminocarboxypropyltransferase;
            O-acetyl-L-homoserine acetate-lyase (adding methanethiol);
            O-acetyl-L-homoserine sulfhydrolase;
            O-acetylhomoserine (thiol)-lyase;
            O-acetylhomoserine sulfhydrolase;
            methionine synthase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     O-acetyl-L-homoserine:methanethiol
            3-amino-3-carboxypropyltransferase
REACTION    O-acetyl-L-homoserine + methanethiol = L-methionine + acetate
            [RN:R00651]
ALL_REAC    R00651;
            (other) R01287 R02026 R03217 R04859
SUBSTRATE   O-acetyl-L-homoserine [CPD:C01077];
            methanethiol [CPD:C00409]
PRODUCT     L-methionine [CPD:C00073];
            acetate [CPD:C00033]
COMMENT     Also reacts with other thiols and H2S, producing homocysteine or
            thioethers. The name methionine synthase is more commonly applied to
            EC 2.1.1.13, methionine synthase. The enzyme from baker's yeast also
            catalyses the reaction of EC 2.5.1.47 cysteine synthase, but more
            slowly.
REFERENCE   1
  AUTHORS   Kerr, D.
  TITLE     O-Acetylhomoserine sulfhydrylase (Neurospora).
  JOURNAL   Methods Enzymol. 17B (1971) 446-450.
  ORGANISM  Neurospora sp.
REFERENCE   2  [PMID:5791104]
  AUTHORS   Smith IK, Thompson JF.
  TITLE     Utilization of S-methylcysteine and methylmercaptan by
            methionineless mutants of Neurospora and the pathway of their
            conversion to methionine. II. Enzyme studies.
  JOURNAL   Biochim. Biophys. Acta. 184 (1969) 130-8.
  ORGANISM  Neurospora sp.
REFERENCE   3  [PMID:795806]
  AUTHORS   Yamagata S, Takeshima K.
  TITLE     O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast.
            Further purification and characterization as a pyridoxal enzyme.
  JOURNAL   J. Biochem. (Tokyo). 80 (1976) 777-85.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4  [PMID:795807]
  AUTHORS   Yamagata S.
  TITLE     O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast.
            Subunit structure.
  JOURNAL   J. Biochem. (Tokyo). 80 (1976) 787-97.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   5  [PMID:4609980]
  AUTHORS   Yamagata S, Takeshima K, Naiki N.
  TITLE     Evidence for the identity of O-acetylserine sulfhydrylase with
            O-acetylhomoserine sulfhydrylase in yeast.
  JOURNAL   J. Biochem. (Tokyo). 75 (1974) 1221-9.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   6  [PMID:2517474]
  AUTHORS   Yamagata S.
  TITLE     Roles of O-acetyl-L-homoserine sulfhydrylases in micro-organisms.
  JOURNAL   Biochimie. 71 (1989) 1125-43.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   7  [PMID:11566369]
  AUTHORS   Shimizu H, Yamagata S, Masui R, Inoue Y, Shibata T, Yokoyama S,
            Kuramitsu S, Iwama T.
  TITLE     Cloning and overexpression of the oah1 gene encoding
            O-acetyl-L-homoserine sulfhydrylase of Thermus thermophilus HB8 and
            characterization of the gene product.
  JOURNAL   Biochim. Biophys. Acta. 1549 (2001) 61-72.
  ORGANISM  Thermus thermophilus
PATHWAY     PATH: map00271  Methionine metabolism
            PATH: map00272  Cysteine metabolism
ORTHOLOGY   KO: K01740  O-acetylhomoserine (thiol)-lyase
GENES       SCE: YLR303W(MET17)
            AGO: AGOS_ADL031W
            PIC: PICST_31162
            SPO: SPBC428.11
            ANI: AN8277.2
            AFM: AFUA_5G04250
            AOR: AO090102000630
            UMA: UM05581.1
            ECA: ECA0820
            PLU: plu3517
            ASU: Asuc_1623
            XCC: XCC3068(metB)
            XCB: XC_1090
            XOO: XOO1390(rtxA)
            XOM: XOO_1278(XOO1278)
            VPA: VP0629
            PPR: PBPRB1415
            PAE: PA5025(metY)
            PAU: PA14_66440(metY)
            PPU: PP_2528(metY)
            PPF: Pput_3191
            PFL: PFL_0498(cysD)
            PEN: PSEEN2118(metY)
            PCR: Pcryo_2201
            PRW: PsycPRwf_1846
            ACI: ACIAD3382(metY)
            SON: SO_1095
            SDN: Sden_0823
            SFR: Sfri_3160
            SBL: Sbal_0916
            SBM: Shew185_3447
            SLO: Shew_2710
            SPC: Sputcn32_0932
            SSE: Ssed_3283
            SHE: Shewmr4_0928
            SHM: Shewmr7_0966
            SHN: Shewana3_0930
            SHW: Sputw3181_3244
            ILO: IL2014
            CPS: CPS_2546
            PHA: PSHAb0477
            PAT: Patl_3406
            PIN: Ping_3644
            MAQ: Maqu_2372
            NOC: Noc_2714
            AEH: Mlg_2101
            HHA: Hhal_2153
            HCH: HCH_04407
            ABO: ABO_2555(metY)
            MMW: Mmwyl1_1496
            AHA: AHA_0506
            CVI: CV_1934(metY)
            RSO: RSc1562(RS05249)
            REU: Reut_A1253 Reut_B4968
            REH: H16_A1313(metY1) H16_B2229(metY2)
            RME: Rmet_1134 Rmet_4606
            BMA: BMAA1890
            BXE: Bxe_A1357
            BVI: Bcep1808_4104
            BUR: Bcep18194_B2422
            BCN: Bcen_4675
            BCH: Bcen2424_3688
            BAM: Bamb_5428
            BPS: BPSS0190
            BPM: BURPS1710b_A1713(metY)
            BTE: BTH_II2196
            BBR: BB1055(metY)
            RFR: Rfer_1327 Rfer_3160
            POL: Bpro_1836
            PNA: Pnap_0219 Pnap_2758
            AAV: Aave_2997 Aave_3089
            AJS: Ajs_1656 Ajs_2286 Ajs_3858
            VEI: Veis_3780
            MPT: Mpe_A0028
            HAR: HEAR1230 HEAR1790
            MMS: mma_2157
            NEU: NE1697(metY)
            NET: Neut_0424
            NMU: Nmul_A1497
            EBA: ebA4861(metB) ebA6307(metY)
            AZO: azo0472 azo1422 azo2193
            DAR: Daro_2851
            HHE: HH0636(metY)
            WSU: WS1015 WS1894(metY)
            TDN: Tmden_0459
            CJE: Cj1727c(metY)
            CCV: CCV52592_1597
            CCO: CCC13826_1282
            ABU: Abu_2169(metY)
            NIS: NIS_1278 NIS_1279
            SUN: SUN_1791
            GSU: GSU1183 GSU2425
            GME: Gmet_0819 Gmet_1566 Gmet_2390
            GUR: Gura_3249 Gura_3945
            PCA: Pcar_1453 Pcar_1719
            PPD: Ppro_1787
            DPS: DP1700 DP2506
            ADE: Adeh_0924
            AFW: Anae109_0967
            SAT: SYN_01255
            PUB: SAR11_1030(metY) SAR11_1259(met17)
            MLO: mlr8465
            MES: Meso_1167
            PLA: Plav_2933
            SME: SMc01809
            SMD: Smed_0867
            ATU: Atu1251(cysD)
            ATC: AGR_C_2311
            RET: RHE_CH01577(ypch00547)
            RLE: RL1679(cysD)
            BME: BMEI1166
            BMF: BAB1_0813
            BMS: BR0793
            BMB: BruAb1_0807
            OAN: Oant_2492
            BJA: bll0245(cysD) bll1235(cysD) bll6281(cysD) blr2078 blr2079
                 blr4967(cysD)
            BRA: BRADO4221(metC) BRADO4873(metC) BRADO6912(metY)
            BBT: BBta_2509(oahS) BBta_3176(metC) BBta_4596(metC)
            RPA: RPA1569 RPA2349(metY) RPA2350(metC) RPA2362 RPA2763
                 RPA4251(oahS) RPA4591(metY)
            RPB: RPB_1001 RPB_1360 RPB_2667 RPB_3960
            RPC: RPC_1331 RPC_2691 RPC_4056
            RPD: RPD_1104 RPD_1339 RPD_2703 RPD_3718
            RPE: RPE_1365 RPE_1723 RPE_2853
            NWI: Nwi_1420
            NHA: Nham_2458
            XAU: Xaut_4332
            SIL: SPO1431
            SIT: TM1040_0585
            RSP: RSP_4161
            RSH: Rsph17029_1095
            RSQ: Rsph17025_0776 Rsph17025_1060
            JAN: Jann_2721
            RDE: RD1_1834(metB)
            PDE: Pden_1933
            HNE: HNE_2885
            NAR: Saro_0813
            SWI: Swit_1278
            GBE: GbCGDNIH1_0510
            ACR: Acry_2103
            RRU: Rru_A0774 Rru_A0784 Rru_A1836 Rru_A2075
            MAG: amb2562
            MGM: Mmc1_1822
            ABA: Acid345_4499
            SUS: Acid_5487
            BHA: BH2603
            BAN: BA5656
            BAR: GBAA5656
            BAA: BA_0514
            BAT: BAS5258
            BCE: BC5406
            BCA: BCE_5535
            BCZ: BCZK5104(cysD)
            BTK: BT9727_5087(cysD)
            BTL: BALH_4907(cysD)
            BCL: ABC0432
            BPU: BPUM_0854
            OIH: OB2639 OB3048
            GKA: GK0284
            SHA: SH0593(cysD)
            SSP: SSP0251
            LMO: lmo0595
            LMF: LMOf2365_0624
            LIN: lin0604
            LWE: lwe0562(cysD)
            LLA: L75975(cysD)
            LLC: LACR_0068
            LLM: llmg_0091(cysD)
            SPR: spr1095 spr1096
            SMU: SMU.1173(cysD)
            STC: str0987(cysD)
            STL: stu0987(cysD)
            STE: STER_0995
            SSA: SSA_0855(cysD)
            SGO: SGO_1334(cysD)
            LPL: lp_2536(metY)
            OOE: OEOE_0239
            LME: LEUM_1799
            STH: STH2681 STH2782
            CAC: CAC0102 CAC2783(cysD)
            CTC: CTC01153
            CTH: Cthe_1569 Cthe_1842
            CDF: CD1825(cysD)
            CBO: CBO1876(cysD)
            CBE: Cbei_0609 Cbei_0766 Cbei_3543
            CKL: CKL_1808
            AMT: Amet_3376
            CHY: CHY_1904
            DSY: DSY4192
            CSC: Csac_1574 Csac_1639
            TTE: TTE2151(mET17)
            MTA: Moth_1309
            MTU: Rv3340(metC)
            MBO: Mb3372(metC)
            MBB: BCG_3410(metC)
            MSM: MSMEG_0239 MSMEG_1652
            MVA: Mvan_1554
            MGI: Mflv_4875
            MMC: Mmcs_1208
            MKM: Mkms_1225
            MJL: Mjls_1235
            CGL: NCgl0625(cgl0653)
            CGB: cg0755(metY)
            CEF: CE0679(metY)
            CDI: DIP0630
            CJK: jk1694(metY)
            RHA: RHA1_ro01767 RHA1_ro05069 RHA1_ro06237
            CMI: CMM_0185(metC) CMM_1336(metY) CMM_2400
            ART: Arth_0531 Arth_1317
            AAU: AAur_1474
            NCA: Noca_3629
            TFU: Tfu_2823
            FRA: Francci3_2830
            FAL: FRAAL4842(metY)
            KRA: Krad_0513 Krad_1344 Krad_3362
            BLO: BL0933(cysD)
            BAD: BAD_0421 BAD_0598(cysD)
            RBA: RB8221
            LIL: LA2062(metY)
            LIC: LIC11852
            SYC: syc1143_c(metY)
            SYF: Synpcc7942_0370
            SYD: Syncc9605_1799
            SYE: Syncc9902_0856
            SYG: sync_1180(thiol)
            SYR: SynRCC307_0795(cysD)
            SYX: SynWH7803_1407(cysD)
            AVA: Ava_4077
            PMA: Pro0800(MET17)
            PMM: PMM0642(cysD)
            PMT: PMT0875(cysD)
            PMN: PMN2A_0083
            PMI: PMT9312_0642
            PMB: A9601_06981(met17)
            PMC: P9515_07081(met17)
            PMF: P9303_13191(met17)
            PMG: P9301_06691(met17)
            PME: NATL1_07071(met17)
            BTH: BT_1923 BT_2387
            BFR: BF1406 BF3545
            BFS: BF1342(metY) BF3351
            SRU: SRU_0479(cysD)
            CHU: CHU_0274(metC) CHU_1812(oahS)
            FPS: FP0257(metY)
            CTE: CT0604(cysD)
            CCH: Cag_1257
            CPH: Cpha266_1767
            PVI: Cvib_1184
            PLT: Plut_0592 Plut_1549
            RRS: RoseRS_1758
            RCA: Rcas_2040
            DRA: DR_0873 DR_2186
            DGE: Dgeo_0225 Dgeo_0518
            TTH: TTC0408 TTC0792
            TTJ: TTHA0760 TTHA1156
            TMA: TM0882
            TPT: Tpet_0045
            MVN: Mevan_0171
            MAC: MA2715(metY)
            MBA: Mbar_A2427
            MBU: Mbur_0797
            MHU: Mhun_2181
            MBN: Mboo_1994 Mboo_2044
            MST: Msp_0677
            MSI: Msm_0174 Msm_0265
            HAL: VNG2421G(hal)
            HMA: rrnAC2716(cysD) rrnAC3063(metY)
            HWA: HQ3454A(metY) HQ3699A(metY)
            NPH: NP0280A(metY_2) NP0284A(metY_1)
            RCI: RCIX1554(metY)
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.49
            ExPASy - ENZYME nomenclature database: 2.5.1.49
            ExplorEnz - The Enzyme Database: 2.5.1.49
            ERGO genome analysis and discovery system: 2.5.1.49
            BRENDA, the Enzyme Database: 2.5.1.49
            CAS: 37290-90-7
///
ENTRY       EC 2.5.1.50                 Enzyme
NAME        zeatin 9-aminocarboxyethyltransferase;
            beta-(9-cytokinin)-alanine synthase;
            beta-(9-cytokinin)alanine synthase;
            O-acetyl-L-serine acetate-lyase (adding N6-substituted adenine);
            lupinate synthetase;
            lupinic acid synthase;
            lupinic acid synthetase;
            3-O-acetyl-L-serine:zeatin 2-amino-2-carboxyethyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     O3-acetyl-L-serine:zeatin 2-amino-2-carboxyethyltransferase
REACTION    O-acetyl-L-serine + zeatin = lupinate + acetate [RN:R03133]
ALL_REAC    R03133
SUBSTRATE   O-acetyl-L-serine [CPD:C00979];
            zeatin [CPD:C00371]
PRODUCT     lupinate [CPD:C01513];
            acetate [CPD:C00033]
COMMENT     The enzyme acts not only on zeatin but also on other N6-substituted
            adenines. The reaction destroys their cytokinin activity and forms
            the corresponding 3-(adenin-9-yl)-L-alanine.
REFERENCE   1
  AUTHORS   Entsch, B., Parker, C.W. and Letham, D.S.
  TITLE     An enzyme from lupin seeds forming alanine derivatives of
            cytokinins.
  JOURNAL   Phytochemistry 22 (1983) 375-381.
  ORGANISM  lupin
REFERENCE   2
  AUTHORS   Mok, D.W.S. and Mok, M.C.
  TITLE     Cytokinin metabolism and action.
  JOURNAL   Ann. Rev. Plant Physiol. Plant Mol. Biol. 52 (2001) 89-118.
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.50
            ExPASy - ENZYME nomenclature database: 2.5.1.50
            ExplorEnz - The Enzyme Database: 2.5.1.50
            ERGO genome analysis and discovery system: 2.5.1.50
            BRENDA, the Enzyme Database: 2.5.1.50
            CAS: 62683-23-2
///
ENTRY       EC 2.5.1.51                 Enzyme
NAME        beta-pyrazolylalanine synthase;
            beta-(1-pyrazolyl)alanine synthase;
            beta-pyrazolealanine synthase;
            beta-pyrazolylalanine synthase (acetylserine);
            O3-acetyl-L-serine acetate-lyase (adding pyrazole);
            BPA-synthase;
            pyrazolealanine synthase;
            pyrazolylalaninase;
            3-O-acetyl-L-serine:pyrazole 1-(2-amino-2-carboxyethyl)transferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     O3-acetyl-L-serine:pyrazole 1-(2-amino-2-carboxyethyl)transferase
REACTION    O3-acetyl-L-serine + pyrazole = 3-(pyrazol-1-yl)-L-alanine + acetate
            [RN:R03134]
ALL_REAC    R03134
SUBSTRATE   O3-acetyl-L-serine [CPD:C00979];
            pyrazole [CPD:C00481]
PRODUCT     3-(pyrazol-1-yl)-L-alanine [CPD:C01162];
            acetate [CPD:C00033]
COMMENT     The enzyme is highly specific for acetylserine and pyrazole. Not
            identical with EC 2.5.1.52 L-mimosine synthase.
REFERENCE   1
  AUTHORS   Murakoshi, I., Ikegami, F., Hinuma, Y. and Hanma, Y.
  TITLE     Purification and characterization of beta-(pyrazol-1-yl)-L-alanine
            synthase from Citrullus vulgaris.
  JOURNAL   Phytochemistry 23 (1984) 973-977.
  ORGANISM  Citrullus vulgaris
REFERENCE   2
  AUTHORS   Murakoshi, I., Ikegami, F., Hinuma, Y. and Hanma, Y.
  TITLE     Purification and characterization of L-mimosine synthase from
            Leucaena leucocephala.
  JOURNAL   Phytochemistry 23 (1984) 1905-1908.
  ORGANISM  Citrullus vulgaris
REFERENCE   3
  AUTHORS   Murakoshi, I., Kuramoto, H. and Haginiwa, J.
  TITLE     The enzymic synthesis of beta-substituted alanines.
  JOURNAL   Phytochemistry 11 (1972) 177-182.
  ORGANISM  Citrullus vulgaris
REFERENCE   4  [PMID:8280125]
  AUTHORS   Noji M, Murakoshi I, Saito K.
  TITLE     Evidence for identity of beta-pyrazolealanine synthase with cysteine
            synthase in watermelon: formation of beta-pyrazole-alanine by cloned
            cysteine synthase in vitro and in vivo.
  JOURNAL   Biochem. Biophys. Res. Commun. 197 (1993) 1111-7.
  ORGANISM  Citrullus vulgaris
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.51
            ExPASy - ENZYME nomenclature database: 2.5.1.51
            ExplorEnz - The Enzyme Database: 2.5.1.51
            ERGO genome analysis and discovery system: 2.5.1.51
            BRENDA, the Enzyme Database: 2.5.1.51
            CAS: 37290-81-6
///
ENTRY       EC 2.5.1.52                 Enzyme
NAME        L-mimosine synthase;
            O3-acetyl-L-serine acetate-lyase (adding 3,4-dihydroxypyridin-1-yl);
            3-O-acetyl-L-serine:3,4-dihydroxypyridine
            1-(2-amino-2-carboxyethyl)transferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     O3-acetyl-L-serine:3,4-dihydroxypyridine
            1-(2-amino-2-carboxyethyl)transferase
REACTION    O3-acetyl-L-serine + 3,4-dihydroxypyridine =
            3-(3,4-dihydroxypyridin-1-yl)-L-alanine + acetate [RN:R04091]
ALL_REAC    R04091
SUBSTRATE   O3-acetyl-L-serine [CPD:C00979];
            3,4-dihydroxypyridine [CPD:C02932]
PRODUCT     3-(3,4-dihydroxypyridin-1-yl)-L-alanine [CPD:C04446];
            acetate [CPD:C00033]
REFERENCE   1
  AUTHORS   Murakoshi, I., Ikegami, F., Hinuma, Y. and Hanma, Y.
  TITLE     Purification and characterization of L-mimosine synthase from
            Leucaena leucocephala.
  JOURNAL   Phytochemistry 23 (1984) 1905-1908.
  ORGANISM  Leucaena leucocephala
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.52
            ExPASy - ENZYME nomenclature database: 2.5.1.52
            ExplorEnz - The Enzyme Database: 2.5.1.52
            ERGO genome analysis and discovery system: 2.5.1.52
            BRENDA, the Enzyme Database: 2.5.1.52
            CAS: 93229-75-5
///
ENTRY       EC 2.5.1.53                 Enzyme
NAME        uracilylalanine synthase;
            O3-acetyl-L-serine acetate-lyase (adding uracil);
            isowillardiine synthase;
            willardiine synthase;
            3-O-acetyl-L-serine:uracil 1-(2-amino-2-carboxyethyl)transferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     O3-acetyl-L-serine:uracil 1-(2-amino-2-carboxyethyl)transferase
REACTION    O3-acetyl-L-serine + uracil = 3-(uracil-1-yl)-L-alanine + acetate
            [RN:R03131]
ALL_REAC    R03131
SUBSTRATE   O3-acetyl-L-serine [CPD:C00979];
            uracil [CPD:C00106]
PRODUCT     3-(uracil-1-yl)-L-alanine [CPD:C03584];
            acetate [CPD:C00033]
COMMENT     Both L-willardiine and L-isowillardiine are produced in the
            reaction. Not identical with EC 2.5.1.47 cysteine synthase.
REFERENCE   1
  AUTHORS   Ahmmad, M.A.S., Maskall, C.S. and Brown, E.G.
  TITLE     Partial-purification and properties of willardiine and synthase
            activity from Pisum sativum.
  JOURNAL   Phytochemistry 23 (1984) 265-270.
  ORGANISM  Pisum sativum
REFERENCE   2
  AUTHORS   Ikegami, F., Kaneko, M., Lambein, F., Kuo, Y.-H. and Murakoshi, I.
  TITLE     Difference between uracilylalanine synthases and cysteine synthases
            in Pisum sativum.
  JOURNAL   Phytochemistry 26 (1987) 2699-2704.
  ORGANISM  Pisum sativum
REFERENCE   3
  AUTHORS   Murakoshi, I., Ikegami, F., Ookawa, N., Ariki, T., Haginiwa, J.,
            Kuo, Y.-H. and Lambein, F.
  TITLE     Biosynthesis of the uracilylalanines willardiine and isowillardiine
            in higher plants.
  JOURNAL   Phytochemistry 17 (1978) 1571-1576.
  ORGANISM  Lathyrus odoratus, Albizia julibrimin, Leucaena leucocephalu, Fagus
            crenata
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.53
            ExPASy - ENZYME nomenclature database: 2.5.1.53
            ExplorEnz - The Enzyme Database: 2.5.1.53
            ERGO genome analysis and discovery system: 2.5.1.53
            BRENDA, the Enzyme Database: 2.5.1.53
            CAS: 113573-73-2
///
ENTRY       EC 2.5.1.54                 Enzyme
NAME        3-deoxy-7-phosphoheptulonate synthase;
            2-dehydro-3-deoxy-phosphoheptonate aldolase;
            2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase;
            3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase;
            3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase;
            3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase;
            7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate
            lyase (pyruvate-phosphorylating);
            7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate
            D-erythrose-4-phosphate lyase (pyruvate-phosphorylating);
            D-erythrose-4-phosphate-lyase;
            D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating);
            DAH7-P synthase;
            DAHP synthase;
            DS-Co;
            DS-Mn;
            KDPH synthase;
            KDPH synthetase;
            deoxy-D-arabino-heptulosonate-7-phosphate synthetase;
            phospho-2-dehydro-3-deoxyheptonate aldolase;
            phospho-2-keto-3-deoxyheptanoate aldolase;
            phospho-2-keto-3-deoxyheptonate aldolase;
            phospho-2-keto-3-deoxyheptonic aldolase;
            phospho-2-oxo-3-deoxyheptonate aldolase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     phosphoenolpyruvate:D-erythrose-4-phosphate
            C-(1-carboxyvinyl)transferase (phosphate-hydrolysing,
            2-carboxy-2-oxoethyl-forming)
REACTION    phosphoenolpyruvate + D-erythrose 4-phosphate + H2O =
            3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
            [RN:R01826]
ALL_REAC    R01826
SUBSTRATE   phosphoenolpyruvate [CPD:C00074];
            D-erythrose 4-phosphate [CPD:C00279];
            H2O [CPD:C00001]
PRODUCT     3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate [CPD:C04691];
            phosphate [CPD:C00009]
COFACTOR    Cadmium [CPD:C01413]
REFERENCE   1
  AUTHORS   Srinivasan, P.R. and Sprinson, D.B.
  TITLE     2-Keto-3-deoxy-D-arabo-heptonic acid 7-phosphate synthetase.
  JOURNAL   J. Biol. Chem. 234 (1959) 716-722.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:11506923]
  AUTHORS   Jossek R, Bongaerts J, Sprenger GA.
  TITLE     Characterization of a new feedback-resistant
            3-deoxy-D-arabino-heptulosonate 7-phosphate synthase AroF of
            Escherichia coli.
  JOURNAL   FEMS. Microbiol. Lett. 202 (2001) 145-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:10489454]
  AUTHORS   Schneider TR, Hartmann M, Braus GH.
  TITLE     Crystallization and preliminary X-ray analysis of
            3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (tyrosine
            inhibitable) from Saccharomyces cerevisiae.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 55 ( Pt 9) (1999) 1586-8.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K01626  3-deoxy-7-phosphoheptulonate synthase
            KO: K03856  3-deoxy-7-phosphoheptulonate synthase
GENES       ATH: AT1G22410 AT4G33510(DHS2) AT4G39980(DHS1)
            OSA: 4333014 4343946 4345872
            CME: CMQ120C CMT165C
            SCE: YBR249C(ARO4) YDR035W(ARO3)
            AGO: AGOS_ABL102C AGOS_AFL047W
            PIC: PICST_80434(ARO4) PICST_83093(ARO3)
            CGR: CAGL0C01573g CAGL0H10142g
            SPO: SPAC24H6.10c SPAP8A3.07c
            ANI: AN0354.2 AN1673.2 AN5701.2
            AFM: AFUA_1G02110 AFUA_4G01450 AFUA_4G08760 AFUA_7G04070
            AOR: AO090005000086 AO090005000886 AO090023000682
            CNE: CND05120 CNL06640
            UMA: UM02010.1 UM02385.1
            TET: TTHERM_00518500
            ECO: b0754(aroG) b1704(aroH) b2601(aroF)
            ECJ: JW0737(aroG) JW1694(aroH) JW2582(aroF)
            ECE: Z0924(aroG) Z2733(aroH) Z3893(aroF)
            ECS: ECs0782 ECs2411 ECs3464
            ECC: c0830(aroG) c1220 c2100(aroH) c3122(aroF)
            ECI: UTI89_C0751(aroG) UTI89_C1897(aroH) UTI89_C2934(aroF)
            ECP: ECP_0281 ECP_0765 ECP_1652 ECP_2602
            ECV: APECO1_1334(aroG) APECO1_3932(aroF) APECO1_780(aroH)
            ECW: EcE24377A_0781(aroG) EcE24377A_1922(aroH)
                 EcE24377A_2885(aroF)
            ECX: EcHS_A0808 EcHS_A1784 EcHS_A2758
            STY: STY0801(aroG) STY1763(aroH) STY2857(aroF)
            STT: t1228(aroH) t2118(aroG) t2625(aroF)
            SPT: SPA1496(aroH) SPA1983(aroG) SPA2529(aroF)
            SEC: SC0759(aroG) SC1366(aroH) SC2672(aroF)
            STM: STM0760(aroG) STM1347(aroH) STM2670(aroF)
            YPE: YPO1130(aroG) YPO2411(aroH) YPO3286(aroF)
            YPK: y0903(aroF) y1928(aroH) y3049(aroG)
            YPM: YP_0398(aroF) YP_1026(aroG) YP_2198(aroH)
            YPA: YPA_1755 YPA_2859
            YPN: YPN_0813 YPN_1865
            YPP: YPDSF_0738 YPDSF_3074
            YPS: YPTB0841(aroF) YPTB1165(aroG) YPTB2320(aroH)
            YPI: YpsIP31758_1735(aroH) YpsIP31758_3220(aroF)
            SFL: SF0550(aroG) SF1526(aroH) SF2661(aroF)
            SFX: S0558(aroG) S1644(aroH) S2838(aroF)
            SFV: SFV_0586(aroG) SFV_1520(aroH) SFV_2870(aroF)
            SSN: SSON_0706(aroG) SSON_1455(aroH) SSON_2752(aroF)
            SBO: SBO_0609(aroG) SBO_1424(aroH) SBO_2639(aroF)
            SDY: SDY_0701(aroG) SDY_1798(aroH) SDY_2765(aroF)
            ECA: ECA1381(aroG) ECA1851(aroH) ECA3352(aroF)
            PLU: plu1262(aroF) plu1470(aroG) plu2630(aroH)
            BUC: BU124(aroH)
            BAS: BUsg116(aroH)
            BAB: bbp118(aroH)
            BCC: BCc_077(aroH)
            WBR: WGLp236(aroF)
            SGL: SG0578 SG0893 SG1427
            ENT: Ent638_1245 Ent638_1743 Ent638_3080
            KPN: KPN_00758(aroG)
            SPE: Spro_0879 Spro_1287 Spro_2172
            BFL: Bfl177(aroF)
            BPN: BPEN_183(aroF)
            HIN: HI1547(aroG)
            HIT: NTHI1587(aroG)
            HIP: CGSHiEE_05315
            HIQ: CGSHiGG_00280
            HDU: HD0444(aroF) HD1475(aroG)
            HSO: HS_0941(aroG)
            PMU: PM0563(aroG) PM0665(aroF)
            MSU: MS1104(aroG) MS1184(aroG)
            APL: APL_0185(aroF) APL_0620(aroG)
            ASU: Asuc_1428 Asuc_1570
            XFA: XF0026
            XFT: PD0018(aroG)
            XCC: XCC0922(dhs1) XCC3587(aroG)
            XCB: XC_0548 XC_3313
            XCV: XCV0574(aroG) XCV1028
            XAC: XAC0545(aroG) XAC1000(dhs1)
            XOO: XOO0977(dhs1) XOO4284(aroG)
            XOM: XOO_0892(XOO0892) XOO_4039(XOO4039)
            VCH: VC0695 VC1507
            VCO: VC0395_0205(aroG) VC0395_A0226(aroF) VC0395_A1114(aroH)
            VVU: VV1_0495 VV1_2654 VV2_0558 VV2_0833
            VVY: VV0701 VV1637 VVA1106 VVA1298
            VPA: VP0546 VP1616 VPA1185
            VFI: VF0553 VF1241 VFA0394
            PPR: PBPRA2023 PBPRA2485 PBPRA3026(aroF) PBPRB1262 PBPRB1813
            PAE: PA1750 PA1901 PA2843 PA2943 PA4212
            PAU: PA14_25980(aroF) PA14_27330(dhs) PA14_41920(aroF-1)
            PAP: PSPA7_2220 PSPA7_2312 PSPA7_3558
            PPU: PP_1866 PP_2324(aroF-1) PP_3080(aroF-2)
            PPF: Pput_2644 Pput_3446 Pput_3849
            PST: PSPTO_1772 PSPTO_2275(aroF-1) PSPTO_3027(aroF-2)
            PSB: Psyr_2073 Psyr_2900 Psyr_3622
            PSP: PSPPH_2044 PSPPH_2325 PSPPH_3636
            PFL: PFL_3568(aroF) PFL_4254 PFL_4274(aroF)
            PFO: Pfl_3069 Pfl_3990 Pfl_4009
            PEN: PSEEN1570 PSEEN1891(aro) PSEEN3146(aroF-2)
            PMY: Pmen_2140 Pmen_2552 Pmen_2961
            PAR: Psyc_0910(aroF)
            PCR: Pcryo_1507
            PRW: PsycPRwf_0921
            ACI: ACIAD1878(aro) ACIAD2330(aro)
            ACB: A1S_1664
            SON: SO_0756(aroG) SO_1361(aroF) SO_1367(pheA) SO_2646(aroH)
            SDN: Sden_0622 Sden_2011 Sden_2747 Sden_2750 Sden_2901
            SFR: Sfri_0628 Sfri_2299 Sfri_2916
            SAZ: Sama_0657 Sama_0893 Sama_2074
            SBL: Sbal_0801 Sbal_1214 Sbal_2490
            SBM: Shew185_1258 Shew185_2483 Shew185_3704
            SLO: Shew_0851 Shew_1067 Shew_1547
            SPC: Sputcn32_1172 Sputcn32_2245 Sputcn32_3238
            SSE: Ssed_0937 Ssed_1163 Ssed_1869
            SPL: Spea_0837 Spea_1053 Spea_2551
            SHE: Shewmr4_1590 Shewmr4_2834 Shewmr4_3358
            SHM: Shewmr7_0595 Shewmr7_1665 Shewmr7_2916
            SHN: Shewana3_1734 Shewana3_3007 Shewana3_3013 Shewana3_3528
            SHW: Sputw3181_0703 Sputw3181_1763 Sputw3181_2992
            ILO: IL1319(aroG)
            CPS: CPS_2779(aroG) CPS_3014(aroH) CPS_3954(aroF)
            PHA: PSHAb0559(aroH)
            PAT: Patl_1587 Patl_1707
            SDE: Sde_2007
            PIN: Ping_0286 Ping_1478 Ping_1726
            MAQ: Maqu_1545 Maqu_1921 Maqu_3489
            CBU: CBU_0982
            CBD: COXBU7E912_1066
            LPN: lpg2027(dhs1) lpg2530(aroF)
            LPF: lpl2004 lpl2451(aroF)
            LPP: lpp2009 lpp2595(aroF)
            MCA: MCA1076
            FTU: FTT0963c(aroG)
            FTF: FTF0963c(aroG)
            FTW: FTW_0862(aroG)
            FTL: FTL_1240
            FTH: FTH_1217(aroG)
            FTA: FTA_1312
            FTN: FTN_0842(aroG)
            TCX: Tcr_1393
            NOC: Noc_1491 Noc_1622
            AEH: Mlg_0275
            HHA: Hhal_0996
            HCH: HCH_02512 HCH_02697 HCH_06088
            CSA: Csal_0588 Csal_1625
            ABO: ABO_0953(aroF-2) ABO_1092(aroF-1)
            MMW: Mmwyl1_2343 Mmwyl1_2600
            AHA: AHA_1654 AHA_1980 AHA_2733 AHA_2993
            DNO: DNO_1003
            BCI: BCI_0191(aroH)
            CRP: CRP_094
            RMA: Rmag_0305
            VOK: COSY_0287(aroG)
            NME: NMB0307
            NMA: NMA2180(aroG)
            NMC: NMC1874(aroG)
            NGO: NGO1695(aroG)
            CVI: CV_0173(aroG) CV_1481(aroF) CV_2358
            RSO: RSc0743(aroG2) RSc2660(aroG1)
            REU: Reut_A1026 Reut_B4281
            REH: H16_A1122(aroG1) H16_B1076(aroG2)
            RME: Rmet_0989 Rmet_1681
            BMA: BMA2339 BMAA0987
            BMV: BMASAVP1_0386 BMASAVP1_A0486(aroG)
            BML: BMA10299_0255 BMA10299_A1113(aroG)
            BMN: BMA10247_2220(aroG) BMA10247_A1341
            BXE: Bxe_A3973 Bxe_B0957
            BVI: Bcep1808_0699 Bcep1808_3726
            BUR: Bcep18194_A3826 Bcep18194_B0086 Bcep18194_B1575
            BCN: Bcen_0254 Bcen_5252
            BCH: Bcen2424_0738 Bcen2424_5607
            BAM: Bamb_0630 Bamb_4886
            BPS: BPSL2839(aroG) BPSS1295(aroG)
            BPM: BURPS1710b_3336 BURPS1710b_A0312
            BPL: BURPS1106A_3325(aroG) BURPS1106A_A1752(aroG)
            BPD: BURPS668_3292(aroG) BURPS668_A1837(aroG)
            BTE: BTH_I1295 BTH_II1124
            PNU: Pnuc_1779
            BPE: BP2123(aroG) BP2908(aroG)
            BPA: BPP1356(aroG) BPP2488(aroG)
            BBR: BB1935(aroG) BB2422(aroG)
            RFR: Rfer_0482 Rfer_3367
            POL: Bpro_1094 Bpro_2057
            PNA: Pnap_3398 Pnap_4121 Pnap_4700
            AAV: Aave_0021 Aave_0852
            AJS: Ajs_0002 Ajs_3644
            VEI: Veis_2189
            MPT: Mpe_A3771
            HAR: HEAR0863(aro)
            MMS: mma_0838
            NEU: NE0831
            NET: Neut_1338
            NMU: Nmul_A0091 Nmul_A2194
            EBA: ebA1026(aroG) ebA6035(aroA)
            AZO: azo1669(aroF) azo2788(aroG)
            DAR: Daro_1964 Daro_3324
            TBD: Tbd_0514
            MFA: Mfla_0525
            HPY: HP0134(dhs1)
            HPJ: jhp0122(aroF)
            HPA: HPAG1_0132
            HHE: HH1557(aroF)
            HAC: Hac_0314(aroAII)
            WSU: WS1452
            TDN: Tmden_1269
            CJE: Cj0716
            CJR: CJE0816
            CJJ: CJJ81176_0739
            CJU: C8J_0683
            CJD: JJD26997_1290
            CFF: CFF8240_0633
            CHA: CHAB381_0852
            CCO: CCC13826_0150
            ABU: Abu_0223(dhs)
            NIS: NIS_1184
            SUN: SUN_0466
            GSU: GSU2291 GSU3142 GSU3333
            GME: Gmet_0024 Gmet_0346 Gmet_2375
            GUR: Gura_0027 Gura_1738
            PCA: Pcar_0614 Pcar_0762 Pcar_3113
            PPD: Ppro_0829 Ppro_2550
            BBA: Bd3486(aroAG)
            DPS: DP0754
            ADE: Adeh_2108 Adeh_2954 Adeh_4059
            AFW: Anae109_0202 Anae109_1710 Anae109_3094
            MXA: MXAN_3526(aroF) MXAN_3642 MXAN_6061(aroF)
            SAT: SYN_01940 SYN_02256
            SFU: Sfum_1777 Sfum_3766
            PUB: SAR11_1150(dhs)
            MLO: mll0826 mll4988
            MES: Meso_1462
            PLA: Plav_1096
            SME: SMc00155(aroF)
            SMD: Smed_1570
            ATU: Atu1610(dhs)
            ATC: AGR_C_2964
            RET: RHE_CH02369(aroG) RHE_CH02375(aroF)
            RLE: RL2686(aroG) RL2692
            BME: BMEI0971
            BMF: BAB1_1031
            BMS: BR1013(dhs)
            BMB: BruAb1_1018(dhs)
            BOV: BOV_0979
            OAN: Oant_2095
            BJA: bll4389(aroG) blr3778
            BRA: BRADO3590(aroG) BRADO4704(aroF)
            BBT: BBta_3493(aroF) BBta_4018(aroG)
            RPA: RPA0027(aroG1) RPA1984(aroG2)
            RPB: RPB_3383
            RPC: RPC_2080
            RPD: RPD_0720 RPD_2058
            RPE: RPE_1991
            NWI: Nwi_1224
            NHA: Nham_1483
            BHE: BH06440
            BQU: BQ06790
            BBK: BARBAKC583_0605
            XAU: Xaut_3227
            CCR: CC_1397 CC_2300
            SIL: SPO1942
            SIT: TM1040_0286 TM1040_1269
            RSP: RSP_2921
            RSH: Rsph17029_1566
            RSQ: Rsph17025_1101
            JAN: Jann_2443
            RDE: RD1_2635
            PDE: Pden_3934 Pden_4791
            MMR: Mmar10_0974
            HNE: HNE_0709
            ZMO: ZMO0187(aroH)
            NAR: Saro_0991
            SAL: Sala_2212
            SWI: Swit_0388
            ELI: ELI_08450
            GOX: GOX1769
            GBE: GbCGDNIH1_1420
            ACR: Acry_1982
            RRU: Rru_A0683
            MAG: amb1219
            MGM: Mmc1_1410
            ABA: Acid345_0281 Acid345_1883 Acid345_3110
            SUS: Acid_5467 Acid_7885
            BSU: BG10375(aroA)
            BHA: BH3242(aroA)
            BAN: BA2958
            BAR: GBAA2958
            BAA: BA_3466
            BAT: BAS2748
            BCE: BC2942 BC4674
            BCA: BCE_2998
            BCZ: BCZK2677(aroA)
            BTK: BT9727_2698(aroA)
            BLI: BL00056(aroA)
            BLD: BLi03126(aroA)
            BCL: ABC2765(aroA)
            BPU: BPUM_2621
            OIH: OB2227(aroG)
            GKA: GK2811
            SAU: SA1558
            SAV: SAV1737
            SAM: MW1680
            SAR: SAR1815
            SAS: SAS1663
            SAC: SACOL1787
            SAB: SAB1597c(aroA)
            SAA: SAUSA300_1683
            SAO: SAOUHSC_01852
            SEP: SE1410
            SER: SERP1297
            SHA: SH1185(aroA)
            SSP: SSP1026
            LMO: lmo1600(aroA)
            LMF: LMOf2365_1621
            LIN: lin1641(aroA)
            LWE: lwe1614
            LLA: L0063(aroF) L0064(aroH)
            LLC: LACR_0102
            LLM: llmg_0125(aroF) llmg_1227(aroH)
            SPY: SPy_1576
            SPZ: M5005_Spy_1297
            SPM: spyM18_1585(aroA)
            SPG: SpyM3_1279(aroA.2)
            SPS: SPs0583
            SPH: MGAS10270_Spy1412
            SPI: MGAS10750_Spy1406
            SPJ: MGAS2096_Spy1316
            SPK: MGAS9429_Spy1291
            SPA: M6_Spy1315
            SPB: M28_Spy1338
            SPN: SP_1700 SP_1701
            SPR: spr1542(aroF) spr1543(aroG)
            SPD: SPD_1510 SPD_1511
            SAG: SAG1686
            SAN: gbs1730
            SAK: SAK_1698
            SMU: SMU.1836(aroG) SMU.1837(aroH)
            STC: str1728(aroG)
            STL: stu1728(aroG1) stu1729(aroG2)
            STE: STER_1704
            SSA: SSA_0544(aroG) SSA_0546(aro)
            SSU: SSU05_1249
            SSV: SSU98_1264
            SGO: SGO_0416
            LPL: lp_1085(aroA)
            LSA: LSA0893(aroH)
            EFA: EF1562
            STH: STH1417 STH2349
            CAC: CAC0892
            CPE: CPE0694
            CPF: CPF_0687(aroF)
            CPR: CPR_0688(aroF)
            CTC: CTC01618
            CDF: CD1453 CD1832
            CBA: CLB_1497(aroF)
            CBH: CLC_1509(aroF)
            CBF: CLI_1556(aroF)
            CBE: Cbei_0692 Cbei_2438 Cbei_4569 Cbei_4577
            CKL: CKL_0784(aroF) CKL_2916(aroH)
            CHY: CHY_0475(aroF1) CHY_1037(aroF2) CHY_1588(aroF3)
                 CHY_1930(aroF4)
            DSY: DSY1400 DSY2264 DSY4186
            DRM: Dred_1149
            SWO: Swol_0363 Swol_1348 Swol_1388
            CSC: Csac_2698
            TTE: TTE1013(aroA) TTE1576(aroA3)
            MTA: Moth_1335 Moth_2412
            MTU: Rv2178c
            MTC: MT2234
            MBO: Mb2200c(aroG)
            MBB: BCG_2193c(aroG)
            MLE: ML0896(aroG)
            MPA: MAP1916c(aroG)
            MAV: MAV_2007 MAV_2317
            MSM: MSMEG_2799 MSMEG_4244
            MVA: Mvan_1501 Mvan_3540
            MGI: Mflv_2971 Mflv_4919
            MMC: Mmcs_1161 Mmcs_3273
            MKM: Mkms_1178 Mkms_3335
            MJL: Mjls_1188 Mjls_3284
            CGL: NCgl0950(cgl0990) NCgl2098(cgl2178)
            CGB: cg1129(aroF) cg2391(aroG)
            CEF: CE1054(aroG) CE2073
            CDI: DIP1616(aroH)
            CJK: jk0732(aroG)
            NFA: nfa17320(aroG2) nfa6230(aroG1)
            RHA: RHA1_ro01112(aroG) RHA1_ro04931
            SCO: SCO2115(aroH) SCO3210(SCE8.03c)
            SMA: SAV6086(aroG)
            TWH: TWT215
            TWS: TW556(aroH)
            LXX: Lxx15410(aro)
            CMI: CMM_1874(aroG)
            ART: Arth_1553 Arth_3302
            AAU: AAur_1693 AAur_3302
            PAC: PPA0726
            NCA: Noca_3096
            TFU: Tfu_1039 Tfu_2350
            FRA: Francci3_3084
            FAL: FRAAL5083(aroF)
            ACE: Acel_0984
            KRA: Krad_3233
            SEN: SACE_1708(aroG) SACE_2874(aroH) SACE_4114(aroH)
                 SACE_5545(aroH) SACE_6347
            STP: Strop_1036 Strop_3256 Strop_3571
            BLO: BL0319(aroG) BL0320(aroG2)
            BAD: BAD_0273(aroG2) BAD_0274(aroG)
            RXY: Rxyl_0960
            FNU: FN1562
            RBA: RB12510(aroG) RB7096(aroA)
            CTR: CT382(aroG)
            CTA: CTA_0416(aroG)
            CMU: TC0661
            CPN: CPn0484(aroG)
            CPA: CP0270
            CPJ: CPj0484(aroG)
            CPT: CpB0504
            CCA: CCA00260(aroG)
            CFE: CF0748(aroG1)
            PCU: pc1658(aroF)
            TDE: TDE2569(aroF)
            LIL: LA3957(aroF)
            LIC: LIC13162(aroA(G))
            LBJ: LBJ_0348(aroF)
            LBL: LBL_2728(aroF)
            SYN: sll0934(ccmA)
            SYW: SYNW2499(aroF)
            SYC: syc1605_c(aroF)
            SYF: Synpcc7942_2501
            SYD: Syncc9605_2666
            SYE: Syncc9902_2295
            SYG: sync_2909
            SYR: SynRCC307_2507(aroF)
            SYX: SynWH7803_2504(aroF)
            CYA: CYA_2186
            CYB: CYB_1407
            TEL: tll0358(ccmA) tll1569
            GVI: glr0193 glr0734 glr1741(ccmA)
            ANA: all0408(ccmA) all0574(aroF) all0747(ccmA) alr3050
            AVA: Ava_0334 Ava_0861 Ava_3980 Ava_4649
            PMA: Pro1865(aroG)
            PMM: PMM1699(aroF)
            PMT: PMT2248(aroF)
            PMN: PMN2A_1307
            PMI: PMT9312_1792
            PMB: A9601_19091(aroG)
            PMC: P9515_18901(aroG)
            PMF: P9303_29971(aroG)
            PMG: P9301_18901(aroG)
            PMH: P9215_19721
            PME: NATL1_21801(aroG)
            TER: Tery_0171 Tery_4537
            BTH: BT_3934
            BFR: BF3944
            BFS: BF3717
            PGI: PG0885
            SRU: SRU_2489
            CHU: CHU_0719(pheB)
            GFO: GFO_0343(aroA)
            CTE: CT0981(aroF)
            CCH: Cag_1376
            CPH: Cpha266_1090
            PVI: Cvib_0784
            PLT: Plut_1169
            DET: DET0468 DET1486
            DEH: cbdb_A1449(aroA) cbdb_A432(aroF)
            DEB: DehaBAV1_1276
            RRS: RoseRS_2359 RoseRS_2785
            RCA: Rcas_2565 Rcas_3120
            DRA: DR_1001 DR_1817
            DGE: Dgeo_1572 Dgeo_1821
            TTH: TTC0020 TTC0448
            TTJ: TTHA0388 TTHA0800
            TMA: TM0343
            TPT: Tpet_0577
            MMA: MM_1271
            TAC: Ta0247
            TVO: TVN1351
            PTO: PTO0339
            PAB: PAB0297(aroG)
            PFU: PF1690
            TKO: TK0268
            RCI: RRC153(aroF)
            APE: APE_0581.1
            SSO: SSO0304(aroG)
            STO: ST2271
            PAI: PAE1932
STRUCTURES  PDB: 1RZM  1VR6  1VS1  2B7O  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.54
            ExPASy - ENZYME nomenclature database: 2.5.1.54
            ExplorEnz - The Enzyme Database: 2.5.1.54
            ERGO genome analysis and discovery system: 2.5.1.54
            BRENDA, the Enzyme Database: 2.5.1.54
            CAS: 9026-94-2
///
ENTRY       EC 2.5.1.55                 Enzyme
NAME        3-deoxy-8-phosphooctulonate synthase;
            2-dehydro-3-deoxy-D-octonate-8-phosphate
            D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating);
            2-dehydro-3-deoxy-phosphooctonate aldolase;
            2-keto-3-deoxy-8-phosphooctonic synthetase;
            3-deoxy-D-manno-octulosonate-8-phosphate synthase;
            3-deoxy-D-mannooctulosonate-8-phosphate synthetase;
            3-deoxyoctulosonic 8-phosphate synthetase;
            KDOP synthase;
            phospho-2-keto-3-deoxyoctonate aldolase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     phosphoenolpyruvate:D-arabinose-5-phosphate
            C-(1-carboxyvinyl)transferase (phosphate-hydrolysing,
            2-carboxy-2-oxoethyl-forming)
REACTION    phosphoenolpyruvate + D-arabinose 5-phosphate + H2O =
            2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate [RN:R03254]
ALL_REAC    R03254
SUBSTRATE   phosphoenolpyruvate [CPD:C00074];
            D-arabinose 5-phosphate [CPD:C01112];
            H2O [CPD:C00001]
PRODUCT     2-dehydro-3-deoxy-D-octonate 8-phosphate [CPD:C04478];
            phosphate [CPD:C00009]
REFERENCE   1  [PMID:14416200]
  AUTHORS   LEVIN DH, RACKER E.
  TITLE     Condensation of arabinose 5-phosphate and phosphorylenol pyruvate by
            2-keto-3-deoxy-8-phosphooctonic acid synthetase.
  JOURNAL   J. Biol. Chem. 234 (1959) 2532-9.
REFERENCE   2  [PMID:11904225]
  AUTHORS   Krosky DJ, Alm R, Berg M, Carmel G, Tummino PJ, Xu B, Yang W.
  TITLE     Helicobacter pylori 3-deoxy-D-manno-octulosonate-8-phosphate
            (KDO-8-P) synthase is a zinc-metalloenzyme.
  JOURNAL   Biochim. Biophys. Acta. 1594 (2002) 297-306.
  ORGANISM  Helicobacter pylori
REFERENCE   3  [PMID:11371194]
  AUTHORS   Asojo O, Friedman J, Adir N, Belakhov V, Shoham Y, Baasov T.
  TITLE     Crystal structures of KDOP synthase in its binary complexes with the
            substrate phosphoenolpyruvate and with a mechanism-based inhibitor.
  JOURNAL   Biochemistry. 40 (2001) 6326-34.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00540  Lipopolysaccharide biosynthesis
ORTHOLOGY   KO: K01627  2-dehydro-3-deoxyphosphooctonate aldolase (KDO 8-P
                        synthase)
GENES       ATH: AT1G16340(ATKDSA2/ATKSDA)
            OSA: 4351779
            ECO: b1215(kdsA)
            ECJ: JW1206(kdsA)
            ECE: Z1986(kdsA)
            ECS: ECs1720
            ECC: c1674(kdsA)
            ECI: UTI89_C1409(kdsA)
            ECP: ECP_1263
            ECV: APECO1_332
            ECW: EcE24377A_1363(kdsA)
            ECX: EcHS_A1320(kdsA)
            STY: STY1897(kdsA)
            STT: t1104(kdsA)
            SPT: SPA1101(kdsA)
            SEC: SC1766(kdsA)
            STM: STM1772(kdsA)
            YPE: YPO2021(kdsA)
            YPK: y2286(kdsA)
            YPM: YP_1869(kdsA)
            YPA: YPA_1405
            YPN: YPN_1503
            YPS: YPTB2009(kdsA)
            YPI: YpsIP31758_2062(kdsA)
            SFL: SF1218(kdsA)
            SFX: S1302(kdsA)
            SFV: SFV_1229(kdsA)
            SSN: SSON_1963(kdsA)
            SBO: SBO_1852(kdsA)
            SDY: SDY_1264(kdsA)
            ECA: ECA2194(kdsA)
            PLU: plu2073(kdsA)
            WBR: WGLp343(kdsA)
            SGL: SG1873
            BFL: Bfl350(kdsA)
            BPN: BPEN_361(kdsA)
            HIN: HI1557(kdsA)
            HIT: NTHI1576(kdsA)
            HIP: CGSHiEE_05380
            HIQ: CGSHiGG_00170
            HDU: HD0857(kdsA)
            HSO: HS_0946(kdsA)
            PMU: PM0558(kdsA)
            MSU: MS1189(kdsA)
            APL: APL_1578(kdsA) APL_2040(kdsA)
            XFA: XF1289
            XFT: PD0542(kdsA)
            XCC: XCC1698(kdsA)
            XCB: XC_2533
            XCV: XCV1750
            XAC: XAC1717(kdsA)
            XOO: XOO2966(kdsA)
            XOM: XOO_2816(XOO2816)
            VCH: VC2175
            VCO: VC0395_A1752(kdsA)
            VVU: VV1_0249
            VVY: VV0935
            VPA: VP0747
            VFI: VF0176 VF0772
            PPR: PBPRA2841
            PAE: PA3636(kdsA)
            PAU: PA14_17310(kdsA)
            PAP: PSPA7_1503(kdsA)
            PPU: PP_1611(kdsA-1) PP_1807(kdsA-2)
            PST: PSPTO_1553(kdsA)
            PSB: Psyr_1362
            PSP: PSPPH_3821(kdsA)
            PFL: PFL_1195(kdsA)
            PFO: Pfl_1120
            PEN: PSEEN4201(kdsA)
            PAR: Psyc_1640(kdsA)
            PCR: Pcryo_1874
            ACI: ACIAD2002(kdsA)
            ACB: A1S_1899
            SON: SO_3827(kdsA)
            SDN: Sden_0925
            SFR: Sfri_0728
            SAZ: Sama_2561
            SBL: Sbal_0703
            SLO: Shew_2904
            SHE: Shewmr4_3163
            SHM: Shewmr7_0803
            SHN: Shewana3_0775
            SHW: Sputw3181_3365
            ILO: IL0920(kdsA)
            CPS: CPS_3547(kdsA)
            PHA: PSHAa1063(kdsA)
            PAT: Patl_2205
            SDE: Sde_1244
            PIN: Ping_1611
            MAQ: Maqu_0920
            CBU: CBU_1675(kdsA)
            CBD: COXBU7E912_0326(kdsA)
            LPN: lpg1182(kdsA)
            LPF: lpl1191(kdsA)
            LPP: lpp1185(kdsA)
            MCA: MCA2514(kdsA)
            FTU: FTT0701(kdsA)
            FTF: FTF0701(kdsA)
            FTW: FTW_1542(kdsA)
            FTL: FTL_1535
            FTH: FTH_1485(kdsA)
            FTA: FTA_1619(kdsA)
            TCX: Tcr_1261
            NOC: Noc_0851
            AEH: Mlg_1840
            HCH: HCH_01866(kdsA)
            CSA: Csal_0618
            ABO: ABO_1163(kdsA-1)
            AHA: AHA_3145(kdsA)
            DNO: DNO_0361(kdsA)
            VOK: COSY_0755(kdsA)
            NME: NMB1283
            NMA: NMA1493(kdsA)
            NMC: NMC1218(kdsA)
            NGO: NGO0619
            CVI: CV_2747(kdsA)
            RSO: RSc1127(kdsA)
            REU: Reut_A1089
            REH: H16_A1186(kdsA)
            RME: Rmet_1053 Rmet_5733
            BMA: BMA1690(kdsA)
            BMV: BMASAVP1_A2194(kdsA)
            BML: BMA10299_A3124(kdsA)
            BMN: BMA10247_1467(kdsA)
            BXE: Bxe_A1572
            BUR: Bcep18194_A5414 Bcep18194_C7392
            BCN: Bcen_5969
            BCH: Bcen2424_2108
            BAM: Bamb_2145 Bamb_6182
            BPS: BPSL2271 BPSL2772(kdsA)
            BPM: BURPS1710b_2712(kdsA) BURPS1710b_3264(kdsA)
            BPL: BURPS1106A_2632(kdsA) BURPS1106A_3251(kdsA)
            BPD: BURPS668_2578(kdsA) BURPS668_3213(kdsA)
            BTE: BTH_I1360(kdsA-1) BTH_I1893(kdsA-2)
            BPE: BP2388(kdsA)
            BPA: BPP3254(kdsA)
            BBR: BB3705(kdsA)
            RFR: Rfer_2649
            POL: Bpro_3182
            MPT: Mpe_A2846
            HAR: HEAR0454(kdsA)
            MMS: mma_0532(kdsA)
            EBA: ebA6160(kdsA)
            AZO: azo2145(kdsA)
            DAR: Daro_2365
            TBD: Tbd_0620
            MFA: Mfla_1910
            HPY: HP0003(kdsA)
            HPJ: jhp0003(kdsA)
            HPA: HPAG1_0003
            HHE: HH0039(kdsA)
            HAC: Hac_0256(kdsA)
            WSU: WS0294(kdsA)
            TDN: Tmden_0401
            CJE: Cj0384c(kdsA)
            CJR: CJE0433(kdsA)
            CJJ: CJJ81176_0407(kdsA)
            CJU: C8J_0359(kdsA)
            CJD: JJD26997_1574(kdsA)
            CFF: CFF8240_1337(kdsA)
            CCV: CCV52592_1184(kdsA)
            CHA: CHAB381_0055(kdsA)
            CCO: CCC13826_0665 CCC13826_0779(kdsA)
            ABU: Abu_1845(kdsA)
            NIS: NIS_1364(kdsA)
            SUN: SUN_1920(kdsA)
            GSU: GSU1894(kdsA)
            GME: Gmet_1277
            PCA: Pcar_1944
            DVU: DVU1624(kdsA)
            DDE: Dde_1766
            LIP: LI0452(kdsA)
            BBA: Bd2255
            DPS: DP0765
            ADE: Adeh_4173
            MXA: MXAN_1095(kdsA)
            SAT: SYN_00950
            SFU: Sfum_2074
            RPR: RP062(kdsA)
            RTY: RT0070(kdsA)
            RCO: RC0090(kdsA)
            RFE: RF_0113(kdsA)
            RBE: RBE_1345(kdsA)
            RAK: A1C_00485
            RBO: A1I_00825
            RCM: A1E_00300
            RRI: A1G_00560
            PUB: SAR11_0938(kdsA)
            MLO: mlr0374
            MES: Meso_1633
            SME: SMc01027(kdsA)
            ATU: Atu1424(kdsA)
            ATC: AGR_C_2628
            RET: RHE_CH01930(kdsA)
            RLE: RL2238(kdsA)
            BME: BMEI0850
            BMF: BAB1_1156
            BMS: BR1133(kdsA)
            BMB: BruAb1_1139(kdsA)
            BOV: BOV_1093(kdsA)
            BJA: bll4800(kdsA)
            BRA: BRADO4101(kdsA)
            BBT: BBta_4474(kdsA)
            RPA: RPA2879(kdsA)
            RPB: RPB_2784
            RPC: RPC_2477
            RPD: RPD_2820
            RPE: RPE_2601
            NWI: Nwi_1831
            NHA: Nham_1739
            BHE: BH05710(kdsA)
            BQU: BQ04870(kdsA)
            BBK: BARBAKC583_0531(kdsA)
            CCR: CC_1429
            SIL: SPO0947(kdsA)
            SIT: TM1040_0653
            RSP: RSP_3849
            JAN: Jann_3658
            RDE: RD1_1661(kdsA)
            MMR: Mmar10_1490
            HNE: HNE_0806(kdsA)
            ZMO: ZMO1488(kdsA)
            NAR: Saro_0726
            GOX: GOX2281
            GBE: GbCGDNIH1_0829
            RRU: Rru_A1886
            MAG: amb1822
            MGM: Mmc1_1558
            ABA: Acid345_3669
            OOE: OEOE_1332
            CBO: CBO1472
            FNU: FN1224
            RBA: RB6563(kdsA)
            CTR: CT655(kdsA)
            CTA: CTA_0711(kdsA)
            CMU: TC0025
            CPN: CPn0721(kdsA)
            CPA: CP0025
            CPJ: CPj0721(kdsA)
            CPT: CpB0749
            CCA: CCA00021(kdsA)
            CAB: CAB021(kdsA)
            CFE: CF0985(aroG2)
            PCU: pc0362(kdsA)
            LIL: LA2408(kdsA)
            LIC: LIC11541(kdsA)
            LBJ: LBJ_1450(kdsA)
            LBL: LBL_1674(kdsA)
            SYW: SYNW0180(kdsA)
            SYC: syc1811_d(ccmA)
            SYF: Synpcc7942_2289
            SYD: Syncc9605_0139 Syncc9605_0175
            SYE: Syncc9902_0206
            SYR: SynRCC307_0285(kdsA)
            SYX: SynWH7803_0231(kdsA)
            PMT: PMT1925(kdsA)
            PMF: P9303_25561(kdsA)
            BTH: BT_4321
            BFR: BF1019
            BFS: BF0936(kdsA)
            PGI: PG1743(kdsA)
            CHU: CHU_2589(kdsA)
            GFO: GFO_2550(kdsA)
            FPS: FP0501(kdsA)
            CTE: CT0088(kdsA)
            CCH: Cag_1974
            CPH: Cpha266_2576
            PLT: Plut_2053
            AAE: aq_085(kdsA)
            SAI: Saci_0183(aroA)
STRUCTURES  PDB: 1O60  1PHQ  1PHW  1PL9  1Q3N  1T8X  1T96  1T99  1X6U  1X8F  
                 1ZHA  1ZJI  2A21  2A2I  2EF9  2NWR  2NWS  2NX1  2NX3  2NXG  
                 2NXH  2NXI  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.55
            ExPASy - ENZYME nomenclature database: 2.5.1.55
            ExplorEnz - The Enzyme Database: 2.5.1.55
            ERGO genome analysis and discovery system: 2.5.1.55
            BRENDA, the Enzyme Database: 2.5.1.55
            CAS: 9026-96-4
///
ENTRY       EC 2.5.1.56                 Enzyme
NAME        N-acetylneuraminate synthase;
            (NANA)condensing enzyme;
            N-acetylneuraminate pyruvate-lyase (pyruvate-phosphorylating);
            NeuAc synthase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     phosphoenolpyruvate:N-acetyl-D-mannosamine
            C-(1-carboxyvinyl)transferase (phosphate-hydrolysing,
            2-carboxy-2-oxoethyl-forming)
REACTION    phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O = phosphate +
            N-acetylneuraminate [RN:R01804]
ALL_REAC    R01804;
            (other) R04435
SUBSTRATE   phosphoenolpyruvate [CPD:C00074];
            N-acetyl-D-mannosamine [CPD:C00645];
            H2O [CPD:C00001]
PRODUCT     phosphate [CPD:C00009];
            N-acetylneuraminate [CPD:C00270]
REFERENCE   1  [PMID:13971393]
  AUTHORS   BLACKLOW RS, WARREN L.
  TITLE     Biosynthesis of sialic acids by Neisseria meningitidis.
  JOURNAL   J. Biol. Chem. 237 (1962) 3520-6.
  ORGANISM  Neisseria meningitidis
REFERENCE   2  [PMID:9438985]
  AUTHORS   Komaki E, Ohta Y, Tsukada Y.
  TITLE     Purification and characterization of N-acetylneuraminate synthase
            from Escherichia coli K1-M12.
  JOURNAL   Biosci. Biotechnol. Biochem. 61 (1997) 2046-50.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K01654  N-acetylneuraminate synthase
GENES       HSA: 54187(NANS)
            MMU: 94181(Nans)
            RNO: 298071(Nans_predicted)
            CFA: 481624(NANS)
            GGA: 427283(NANS)
            XLA: 432051(MGC83164) 447417(MGC84329)
            DRE: 322780(zgc:77126)
            ECI: UTI89_C3372(neuB)
            ECV: APECO1_3471(neuB)
            VVU: VV1_0808
            VVY: VV0312
            VPA: VP0200
            VFI: VF0143
            ILO: IL0519(siaC) IL0551
            LPN: lpg0752(neuB)
            LPF: lpl0789(neuB)
            LPP: lpp0818(neuB)
            HCH: HCH_04835
            AHA: AHA_4180(nueB)
            NME: NMB0068(siaC)
            CVI: CV_4031(neuB)
            NEU: NE1570
            HPA: HPAG1_0175
            HAC: Hac_0364 Hac_1271(neuB)
            TDN: Tmden_0595
            CJE: Cj1141(neuB1) Cj1317(neuB3) Cj1327(neuB2)
            CJR: CJE1512(neuB) CJE1516(ptmC)
            CJU: C8J_1251(neuB)
            GSU: GSU1970
            GUR: Gura_4086
            PCA: Pcar_1277
            BBA: Bd1683(neuB)
            BJA: blr5992
            RPB: RPB_1534
            RPE: RPE_4236
            NWI: Nwi_2396
            MMR: Mmar10_1969 Mmar10_1974
            ABA: Acid345_2841
            GKA: GK3123
            SAG: SAG1161(neuB)
            SAN: gbs1236(neuB)
            SAK: SAK_1250(neuB)
            CTC: CTC01711
            CTH: Cthe_2229
            FNU: FN1684
            LIL: LA1609(nnaB1)
            LIC: LIC12173(neuB)
            SYW: SYNW0448(neuB)
            PMB: A9601_14241(spsE)
            PMF: P9303_01101(spsE)
            PMG: P9301_14081(spsE)
            SRU: SRU_0605(spsE)
            MAE: Maeo_0420
            HWA: HQ3519A(neuB)
STRUCTURES  PDB: 1WVO  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.56
            ExPASy - ENZYME nomenclature database: 2.5.1.56
            ExplorEnz - The Enzyme Database: 2.5.1.56
            ERGO genome analysis and discovery system: 2.5.1.56
            BRENDA, the Enzyme Database: 2.5.1.56
            CAS: 37290-66-7
///
ENTRY       EC 2.5.1.57                 Enzyme
NAME        N-acylneuraminate-9-phosphate synthase;
            N-acetylneuraminate 9-phosphate lyase;
            N-acetylneuraminate 9-phosphate sialic acid 9-phosphate synthase;
            N-acetylneuraminate 9-phosphate synthetase;
            N-acylneuraminate-9-phosphate pyruvate-lyase
            (pyruvate-phosphorylating);
            sialic acid 9-phosphate synthetase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     phosphoenolpyruvate:N-acyl-D-mannosamine-6-phosphate
            1-(2-carboxy-2-oxoethyl)transferase
REACTION    phosphoenolpyruvate + N-acyl-D-mannosamine 6-phosphate + H2O =
            N-acylneuraminate 9-phosphate + phosphate [RN:R02769]
ALL_REAC    R02769 > R04435
SUBSTRATE   phosphoenolpyruvate [CPD:C00074];
            N-acyl-D-mannosamine 6-phosphate [CPD:C00686];
            H2O [CPD:C00001]
PRODUCT     N-acylneuraminate 9-phosphate [CPD:C01200];
            phosphate [CPD:C00009]
COMMENT     Acts on N-glycoloyl and N-acetyl-derivatives.
REFERENCE   1
  AUTHORS   Roseman, S., Jourdian, G.W., Watson, D. and Rood, R.
  TITLE     Enzymatic synthesis of sialic acid 9-phosphates.
  JOURNAL   Proc. Natl. Acad. Sci. USA 47 (1961) 958-961.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:5928202]
  AUTHORS   Watson DR, Jourdian GW, Roseman S.
  TITLE     The sialic acids. 8. Sialic acid 9-phosphate synthetase.
  JOURNAL   J. Biol. Chem. 241 (1966) 5627-36.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:10873658]
  AUTHORS   Nakata D, Close BE, Colley KJ, Matsuda T, Kitajima K.
  TITLE     Molecular cloning and expression of the mouse N-acetylneuraminic
            acid 9-phosphate synthase which does not have deaminoneuraminic acid
            (KDN) 9-phosphate synthase activity.
  JOURNAL   Biochem. Biophys. Res. Commun. 273 (2000) 642-8.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K05304  N-acylneuraminate-9-phosphate synthase activity
GENES       HSA: 54187(NANS)
            MMU: 94181(Nans)
            RNO: 298071(Nans_predicted)
            CFA: 481624(NANS)
            GGA: 427283(NANS)
            XLA: 432051(MGC83164) 447417(MGC84329)
            DRE: 322780(zgc:77126)
            SDN: Sden_1289 Sden_3113
            SAZ: Sama_2331
            SBM: Shew185_2977
            SLO: Shew_1329
            SPC: Sputcn32_2625
            SSE: Ssed_3100
            SPL: Spea_0049
            SHM: Shewmr7_1391
            SHW: Sputw3181_1382
            PAT: Patl_3076
            TCX: Tcr_1458
            AEH: Mlg_2327 Mlg_2369
            MMW: Mmwyl1_3564
            VEI: Veis_4853
            HAR: HEAR1126
            NET: Neut_1549
            NMU: Nmul_A0408
            DVL: Dvul_2590 Dvul_2635
            DDE: Dde_3256 Dde_3681
            NHA: Nham_1196
            RDE: RD1_4205
            PDE: Pden_3556
            SAL: Sala_1576 Sala_1580
            MAG: amb0080
            MGM: Mmc1_0562
            SUS: Acid_2246
            CTH: Cthe_2641
            CBE: Cbei_4278
            SWO: Swol_0210
            MTA: Moth_0756
            SYD: Syncc9605_2221
            SYE: Syncc9902_0084 Syncc9902_0458
            PMI: PMT9312_1346
            PMG: P9301_14081(spsE)
            CCH: Cag_1072
            CPH: Cpha266_1187
            PVI: Cvib_1025
            PLT: Plut_1274
            RCA: Rcas_0774
            MMQ: MmarC5_0506
            MBU: Mbur_1586
            MHU: Mhun_3098
            HWA: HQ3519A(neuB)
STRUCTURES  PDB: 1WVO  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.57
            ExPASy - ENZYME nomenclature database: 2.5.1.57
            ExplorEnz - The Enzyme Database: 2.5.1.57
            ERGO genome analysis and discovery system: 2.5.1.57
            BRENDA, the Enzyme Database: 2.5.1.57
            CAS: 9031-58-7
///
ENTRY       EC 2.5.1.58                 Enzyme
NAME        protein farnesyltransferase;
            FTase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     farnesyl-diphosphate:protein-cysteine farnesyltransferase
REACTION    farnesyl diphosphate + protein-cysteine = S-farnesyl protein +
            diphosphate
SUBSTRATE   farnesyl diphosphate [CPD:C00448];
            protein-cysteine
PRODUCT     S-farnesyl protein;
            diphosphate [CPD:C00013]
COMMENT     This enzyme, along with protein geranylgeranyltransferase types I
            (EC 2.5.1.59) and II (EC 2.5.1.60), constitutes the protein
            prenyltransferase family of enzymes. Catalyses the formation of a
            thioether linkage between the C-1 of an isoprenyl group and a
            cysteine residue fourth from the C-terminus of the protein. These
            protein acceptors have the C-terminal sequence CA1A2X, where the
            terminal residue, X, is preferably serine, methionine, alanine or
            glutamine; leucine makes the protein a substrate for EC 2.5.1.59.
            The enzymes are relaxed in specificity for A1, but cannot act if A2
            is aromatic. Substrates of the prenyltransferases include Ras, Rho,
            Rab, other Ras-related small GTP-binding proteins, gamma-subunits of
            heterotrimeric G-proteins, nuclear lamins, centromeric proteins and
            many proteins involved in visual signal transduction. A zinc
            metalloenzyme that requires Mg2+ for activity.
REFERENCE   1  [PMID:7756316]
  AUTHORS   Furfine ES, Leban JJ, Landavazo A, Moomaw JF, Casey PJ.
  TITLE     Protein farnesyltransferase: kinetics of farnesyl pyrophosphate
            binding and product release.
  JOURNAL   Biochemistry. 34 (1995) 6857-62.
  ORGANISM  rat [GN:rno], cow [GN:bta]
REFERENCE   2  [PMID:8621375]
  AUTHORS   Casey PJ, Seabra MC.
  TITLE     Protein prenyltransferases.
  JOURNAL   J. Biol. Chem. 271 (1996) 5289-92.
  ORGANISM  human [GN:hsa], rat [GN:rno], Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:9657673]
  AUTHORS   Long SB, Casey PJ, Beese LS.
  TITLE     Cocrystal structure of protein farnesyltransferase complexed with a
            farnesyl diphosphate substrate.
  JOURNAL   Biochemistry. 37 (1998) 9612-8.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:11591144]
  AUTHORS   Micali E, Chehade KA, Isaacs RJ, Andres DA, Spielmann HP.
  TITLE     Protein farnesyltransferase isoprenoid substrate discrimination is
            dependent on isoprene double bonds and branched methyl groups.
  JOURNAL   Biochemistry. 40 (2001) 12254-65.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:12374986]
  AUTHORS   Long SB, Casey PJ, Beese LS.
  TITLE     Reaction path of protein farnesyltransferase at atomic resolution.
  JOURNAL   Nature. 419 (2002) 645-50.
  ORGANISM  human [GN:hsa]
REFERENCE   6
  AUTHORS   Gibbs, R.A.
  TITLE     Prenyl transfer and the enzymes of terpenoid and steroid
            biosynthesis.
  JOURNAL   In: Sinnott, M. (Ed.), Comprehensive Biological Catalysis. A
            Mechanistic Reference, vol. 1, Academic Press, San Diego, CA, 1998,
            p. 31-118.
ORTHOLOGY   KO: K05954  
GENES       HSA: 2339(FNTA) 2342(FNTB)
            PTR: 452971(FNTB) 472929(FNTA)
            MMU: 110606(Fntb) 14272(Fnta)
            RNO: 25318(Fnta) 64511(Fntb)
            CFA: 490735(FNTB)
            BTA: 281169(FNTA) 327686(FNTB)
            XLA: 447605(MGC85220)
            XTR: 550012(fntb)
            DRE: 323500(fntb)
            DME: Dmel_CG2976
            CEL: F23B12.6(tag-114) R02D3.5
            ATH: AT3G59380(FTA) AT5G40280(ERA1)
            OSA: 4327880 4347566
            CME: CMS122C
            SCE: YDL090C(RAM1) YKL019W(RAM2)
            AGO: AGOS_ACR094C AGOS_ADR275W
            CGR: CAGL0L07106g
            SPO: SPAC17G6.04c SPAPB1A10.04c(cwp1)
            ANI: AN2002.2 AN3867.2
            AFM: AFUA_4G07800 AFUA_4G10330
            AOR: AO090003001188 AO090023000791
            CNE: CNE03110 CNF02370
            UMA: UM01488.1 UM05348.1
            DDI: DDBDRAFT_0216701 DDBDRAFT_0218423
            PFA: PF11_0483
            CPV: cgd6_2510
            CHO: Chro.60290
            TAN: TA15255 TA17870
            TPV: TP02_0810
            TET: TTHERM_00248530 TTHERM_00532030
            TBR: Tb927.3.4490 Tb927.7.460
            TCR: 507257.70 510329.280
            LMA: LmjF29.1950
            EHI: 288.t00007 83.t00031
STRUCTURES  PDB: 1S63  1S64  1SA4  1SA5  1TN6  1TN7  1TN8  1X81  2BED  2F0Y  
                 2H6F  2H6G  2H6H  2H6I  2IEJ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.58
            ExPASy - ENZYME nomenclature database: 2.5.1.58
            ExplorEnz - The Enzyme Database: 2.5.1.58
            ERGO genome analysis and discovery system: 2.5.1.58
            BRENDA, the Enzyme Database: 2.5.1.58
///
ENTRY       EC 2.5.1.59                 Enzyme
NAME        protein geranylgeranyltransferase type I;
            GGTase-I;
            GGTaseI
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     geranylgeranyl-diphosphate:protein-cysteine geranyltransferase
REACTION    geranylgeranyl diphosphate + protein-cysteine =
            S-geranylgeranyl-protein + diphosphate
SUBSTRATE   geranylgeranyl diphosphate [CPD:C00353];
            protein-cysteine
PRODUCT     S-geranylgeranyl-protein;
            diphosphate [CPD:C00013]
COMMENT     This enzyme, along with protein farnesyltransferase (EC 2.5.1.58)
            and protein geranylgeranyltransferase type II (EC 2.5.1.60),
            constitutes the protein prenyltransferase family of enzymes.
            Catalyses the formation of a thioether linkage between the C-1 atom
            of the geranylgeranyl group and a cysteine residue fourth from the
            C-terminus of the protein. These protein acceptors have the
            C-terminal sequence CA1A2X, where the terminal residue, X, is
            preferably leucine; serine, methionine, alanine or glutamine makes
            the protein a substrate for EC 2.5.1.58. The enzymes are relaxed in
            specificity for A1, but cannot act if A2 is aromatic. Known targets
            of this enzyme include most gamma-subunits of heterotrimeric G
            proteins and Ras-related GTPases such as members of the Ras and
            Rac/Rho families. A zinc metalloenzyme. The Zn2+ is required for
            peptide, but not for isoprenoid, substrate binding.
REFERENCE   1  [PMID:8621375]
  AUTHORS   Casey PJ, Seabra MC.
  TITLE     Protein prenyltransferases.
  JOURNAL   J. Biol. Chem. 271 (1996) 5289-92.
  ORGANISM  human [GN:hsa], rat [GN:rno], Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:9003382]
  AUTHORS   Zhang FL, Casey PJ.
  TITLE     Influence of metal ions on substrate binding and catalytic activity
            of mammalian protein geranylgeranyltransferase type-I.
  JOURNAL   Biochem. J. 320 ( Pt 3) (1996) 925-32.
  ORGANISM  human [GN:hsa], rat [GN:rno]
REFERENCE   3
  AUTHORS   Gibbs, R.A.
  TITLE     Prenyl transfer and the enzymes of terpenoid and steroid
            biosynthesis.
  JOURNAL   In: Sinnott, M. (Ed.), Comprehensive Biological Catalysis. A
            Mechanistic Reference, vol. 1, Academic Press, San Diego, CA, 1998,
            p. 31-118.
ORTHOLOGY   KO: K05955  
GENES       HSA: 2339(FNTA) 5229(PGGT1B)
            PTR: 471600(PGGT1B) 472929(FNTA)
            MMU: 14272(Fnta) 225467(Pggt1b)
            RNO: 25318(Fnta) 81746(Pggt1b)
            CFA: 481440(PGGT1B)
            BTA: 281169(FNTA)
            XLA: 414563(MGC81402)
            XTR: 493499(MGC89595)
            SPU: 581220(LOC581220)
            DME: Dmel_CG2976 Dmel_CG3469(betaggt-I)
            CEL: R02D3.5 Y48E1B.3
            ATH: AT2G39550(ATGGT-IB) AT3G59380(FTA)
            OSA: 4347566
            SCE: YGL155W(CDC43) YKL019W(RAM2)
            AGO: AGOS_ACR094C AGOS_AGR384C
            CAL: CaO19.1803
            CGR: CAGL0E05126g
            SPO: SPAC2E1P5.04c(cwg2) SPAPB1A10.04c(cwp1)
            ANI: AN3867.2 AN5760.2
            AFM: AFUA_4G07800
            AOR: AO090003000047 AO090023000791
            CNE: CNE03110
            UMA: UM01488.1 UM04373.1
            DDI: DDBDRAFT_0190505 DDBDRAFT_0218423
            CPV: cgd6_2510
            CHO: Chro.60290
            TAN: TA17870
            TET: TTHERM_00532030 TTHERM_00770790
            EHI: 288.t00007 40.t00014
STRUCTURES  PDB: 1S63  1S64  1SA4  1SA5  1TNB  1TNO  1TNU  1TNY  1TNZ  1X81  
                 2BED  2F0Y  2H6F  2H6G  2H6H  2H6I  2IEJ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.59
            ExPASy - ENZYME nomenclature database: 2.5.1.59
            ExplorEnz - The Enzyme Database: 2.5.1.59
            ERGO genome analysis and discovery system: 2.5.1.59
            BRENDA, the Enzyme Database: 2.5.1.59
///
ENTRY       EC 2.5.1.60                 Enzyme
NAME        protein geranylgeranyltransferase type II;
            GGTaseII;
            Rab geranylgeranyltransferase;
            RabGGTase;
            geranylgeranyl-diphosphate,geranylgeranyl-diphosphate:protein-
            cysteine geranyltransferase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     geranylgeranyl-diphosphate:protein-cysteine geranyltransferase
REACTION    geranylgeranyl diphosphate + protein-cysteine =
            S-geranylgeranyl-protein + diphosphate
SUBSTRATE   geranylgeranyl diphosphate [CPD:C00353];
            protein-cysteine
PRODUCT     S-geranylgeranyl-protein;
            diphosphate [CPD:C00013]
COMMENT     This enzyme, along with protein farnesyltransferase (EC 2.5.1.58)
            and protein geranylgeranyltransferase type I (EC 2.5.1.59),
            constitutes the protein prenyltransferase family of enzymes.
            Attaches geranylgeranyl groups to two C-terminal cysteines in
            Ras-related GTPases of a single family, the Rab family (Ypt/Sec4 in
            lower eukaryotes) that terminate in XXCC, XCXC and CCXX motifs.
            Reaction is entirely dependent on the Rab substrate being bound to
            Rab escort protein (REP). Post-translational modification with the
            geranylgeranyl moiety is essential for Rab GTPases to be able to
            control the processes of membrane docking and fusion [5].
REFERENCE   1  [PMID:8621375]
  AUTHORS   Casey PJ, Seabra MC.
  TITLE     Protein prenyltransferases.
  JOURNAL   J. Biol. Chem. 271 (1996) 5289-92.
  ORGANISM  human [GN:hsa], rat [GN:rno], Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:9677305]
  AUTHORS   Wilson AL, Erdman RA, Castellano F, Maltese WA.
  TITLE     Prenylation of Rab8 GTPase by type I and type II geranylgeranyl
            transferases.
  JOURNAL   Biochem. J. 333 ( Pt 3) (1998) 497-504.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:10745007]
  AUTHORS   Zhang H, Seabra MC, Deisenhofer J.
  TITLE     Crystal structure of Rab geranylgeranyltransferase at 2.0 A
            resolution.
  JOURNAL   Structure. Fold. Des. 8 (2000) 241-51.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:11591706]
  AUTHORS   Thoma NH, Niculae A, Goody RS, Alexandrov K.
  TITLE     Double prenylation by RabGGTase can proceed without dissociation of
            the mono-prenylated intermediate.
  JOURNAL   J. Biol. Chem. 276 (2001) 48631-6.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:12071695]
  AUTHORS   Rak A, Niculae A, Kalinin A, Thoma NH, Sidorovitch V, Goody RS,
            Alexandrov K.
  TITLE     In vitro assembly, purification, and crystallization of the rab
            geranylgeranyl transferase:substrate complex.
  JOURNAL   Protein. Expr. Purif. 25 (2002) 23-30.
  ORGANISM  human [GN:hsa]
REFERENCE   6
  AUTHORS   Gibbs, R.A.
  TITLE     Prenyl transfer and the enzymes of terpenoid and steroid
            biosynthesis.
  JOURNAL   In: Sinnott, M. (Ed.), Comprehensive Biological Catalysis. A
            Mechanistic Reference, vol. 1, Academic Press, San Diego, CA, 1998,
            p. 31-118.
ORTHOLOGY   KO: K05956  
GENES       HSA: 5875(RABGGTA) 5876(RABGGTB)
            PTR: 469356(ACADM)
            MMU: 19352(Rabggtb) 56187(Rabggta)
            RNO: 25533(Rabggtb) 58983(Rabggta)
            CFA: 492055(LOC492055) 608407(RABGGTA) 612683(RABGGTB)
            SPU: 588843(LOC588843)
            DME: Dmel_CG3073(l(1)G0144)
            ATH: AT5G12210
            OSA: 4346013
            CME: CMT217C
            SCE: YJL031C(BET4) YPR176C(BET2)
            AGO: AGOS_AEL268W
            PIC: PICST_37880(BET2.2)
            CAL: CaO19_7563(CaO19.7563)
            CGR: CAGL0G09823g CAGL0J01067g
            SPO: SPAC167.02(ptb1)
            ANI: AN1981.2 AN3747.2
            AFM: AFUA_4G10580 AFUA_7G04460
            AOR: AO090003001153 AO090005000132
            CNE: CND01670
            ECU: ECU08_1290
            DDI: DDBDRAFT_0219584
            CPV: cgd6_1750
            CHO: Chro.60212
            TAN: TA04900 TA11140
            TPV: TP03_0500
            TET: TTHERM_00630460
            TBR: Tb927.4.690
            TCR: 507053.70
            LMA: LmjF34.4030
            EHI: 25.t00001 505.t00003
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.60
            ExPASy - ENZYME nomenclature database: 2.5.1.60
            ExplorEnz - The Enzyme Database: 2.5.1.60
            ERGO genome analysis and discovery system: 2.5.1.60
            BRENDA, the Enzyme Database: 2.5.1.60
///
ENTRY       EC 2.5.1.61                 Enzyme
NAME        hydroxymethylbilane synthase;
            HMB-synthase;
            porphobilinogen deaminase;
            pre-uroporphyrinogen synthase;
            uroporphyrinogen I synthase;
            uroporphyrinogen I synthetase;
            uroporphyrinogen synthase;
            uroporphyrinogen synthetase;
            porphobilinogen ammonia-lyase (polymerizing);
            (4-[2-carboxyethyl]-3-[carboxymethyl]pyrrol-2-yl)methyltransferase
            (hydrolysing)
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     porphobilinogen:(4-[2-carboxyethyl]-3-[carboxymethyl]pyrrol-2-yl)met
            hyltransferase (hydrolysing)
REACTION    4 porphobilinogen + H2O = hydroxymethylbilane + 4 NH3 [RN:R00084]
ALL_REAC    R00084
SUBSTRATE   porphobilinogen [CPD:C00931];
            H2O [CPD:C00001]
PRODUCT     hydroxymethylbilane [CPD:C01024];
            NH3 [CPD:C00014]
COMMENT     The enzyme works by stepwise addition of pyrrolylmethyl groups until
            a hexapyrrole is present at the active centre. The terminal
            tetrapyrrole is then hydrolysed to yield the product, leaving a
            cysteine-bound dipyrrole on which assembly continues. In the
            presence of a second enzyme, EC 4.2.1.75 uroporphyrinogen-III
            synthase, which is often called cosynthase, the product is cyclized
            to form uroporphyrinogen-III. If EC 4.2.1.75 is absent, the
            hydroxymethylbilane cyclizes spontaneously to form uroporphyrinogen
            I.
REFERENCE   1  [PMID:6769048]
  AUTHORS   Battersby AR, Fookes CJ, Matcham GW, McDonald E.
  TITLE     Biosynthesis of the pigments of life: formation of the macrocycle.
  JOURNAL   Nature. 285 (1980) 17-21.
REFERENCE   2  [PMID:4847568]
  AUTHORS   Frydman RB, Feinstein G.
  TITLE     Studies on porphobilinogen deaminase and uroporphyrinogen 3
            cosynthase from human erythrocytes.
  JOURNAL   Biochim. Biophys. Acta. 350 (1974) 358-73.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:6061709]
  AUTHORS   Levin EY, Coleman DL.
  TITLE     The enzymatic conversion of porphobilinogen to uroporphyrinogen
            catalyzed by extracts of hematopoietic mouse spleen.
  JOURNAL   J. Biol. Chem. 242 (1967) 4247-53.
  ORGANISM  mouse [GN:mmu]
REFERENCE   4  [PMID:3069132]
  AUTHORS   Warren MJ, Jordan PM.
  TITLE     Investigation into the nature of substrate binding to the
            dipyrromethane cofactor of Escherichia coli porphobilinogen
            deaminase.
  JOURNAL   Biochemistry. 27 (1988) 9020-30.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:3196304]
  AUTHORS   Miller AD, Hart GJ, Packman LC, Battersby AR.
  TITLE     Evidence that the pyrromethane cofactor of hydroxymethylbilane
            synthase (porphobilinogen deaminase) is bound to the protein through
            the sulphur atom of cysteine-242.
  JOURNAL   Biochem. J. 254 (1988) 915-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:11152419]
  AUTHORS   Battersby AR.
  TITLE     Tetrapyrroles: the pigments of life.
  JOURNAL   Nat. Prod. Rep. 17 (2000) 507-26.
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K01749  hydroxymethylbilane synthase
GENES       HSA: 3145(HMBS)
            MMU: 15288(Hmbs)
            RNO: 25709(Hmbs)
            CFA: 489373(HMBS)
            GGA: 419701(HMBS)
            XLA: 495094(LOC495094)
            XTR: 448096(hmbs)
            DRE: 394129(hmbs)
            SPU: 575537(LOC575537)
            DME: Dmel_CG9165(l(3)02640)
            ATH: AT5G08280(HEMC)
            OSA: 4328432
            SCE: YDL205C(HEM3)
            AGO: AGOS_ABL107C
            PIC: PICST_47071
            CAL: CaO19.1742
            CGR: CAGL0J09680g
            SPO: SPAC24B11.13(hem3)
            ANI: AN0121.2
            AFM: AFUA_3G13120 AFUA_5G11760
            AOR: AO090012000205 AO090103000151 AO090120000294
            DDI: DDB_0231417(hemC)
            PFA: PFL0480w
            TET: TTHERM_00317210
            ECO: b3805(hemC)
            ECJ: JW5932(hemC)
            ECE: Z5319(hemC)
            ECS: ECs4735
            ECC: c4724(hemC)
            ECI: UTI89_C4364(hemC)
            ECP: ECP_3997
            ECV: APECO1_2673(hemC)
            ECW: EcE24377A_4320(hemC)
            ECX: EcHS_A4025(hemC)
            STY: STY3621(hemC)
            STT: t3359(hemC)
            SPT: SPA3779(hemC)
            SEC: SC3839(hemC)
            STM: STM3938(hemC)
            YPE: YPO3849(hemC)
            YPK: y0381(hemC)
            YPM: YP_3197(hemC)
            YPA: YPA_0172
            YPN: YPN_0114
            YPP: YPDSF_3467
            YPS: YPTB0184(hemC)
            YPI: YpsIP31758_0198(hemC)
            YEN: YE0187(hemC)
            SFL: SF3877(hemC)
            SFX: S3879(hemC)
            SFV: SFV_3697(hemC)
            SSN: SSON_3977(hemC)
            SBO: SBO_3816(hemC)
            SDY: SDY_3941(hemC)
            ECA: ECA4188(hemC)
            PLU: plu4644(hemC)
            BUC: BU591(hemC)
            WBR: WGLp240(hemC)
            SGL: SG2366
            ENT: Ent638_3987
            SPE: Spro_0178
            BFL: Bfl580(hemC)
            BPN: BPEN_601(hemC)
            HSO: HS_0044(hemC)
            PMU: PM1812(pbg)
            MSU: MS0276(hemC)
            APL: APL_1010(hemC)
            ASU: Asuc_0356
            XFA: XF1627
            XFT: PD1152(hemC)
            XCC: XCC3511(hemC)
            XCB: XC_0649
            XCV: XCV0679(hemC)
            XAC: XAC0622(hemC)
            XOO: XOO4007(hemC)
            XOM: XOO_3778(XOO3778)
            VCH: VC0120
            VCO: VC0395_A2398(hemC)
            VVU: VV1_1122
            VVY: VV0081
            VPA: VP2988
            VFI: VF0066
            PPR: PBPRA3527(hemC) PBPRA3528
            PAE: PA5260(hemC)
            PAU: PA14_69450(hemC)
            PAP: PSPA7_6006(hemC)
            PPU: PP_0186(hemC)
            PPF: Pput_0208
            PST: PSPTO_0128(hemC)
            PSB: Psyr_0062
            PSP: PSPPH_0067(hemC)
            PFL: PFL_6002(hemC)
            PFO: Pfl_5487
            PEN: PSEEN5353(hemC)
            PMY: Pmen_0280
            PAR: Psyc_0089(hemC)
            PCR: Pcryo_0098
            PRW: PsycPRwf_2263
            ACI: ACIAD0286(hemC)
            SON: SO_4313(hemC)
            SDN: Sden_0388
            SFR: Sfri_0440
            SAZ: Sama_3254
            SBL: Sbal_4000
            SBM: Shew185_3978
            SLO: Shew_0318
            SPC: Sputcn32_3587
            SSE: Ssed_4133
            SPL: Spea_0373
            SHE: Shewmr4_0388
            SHM: Shewmr7_3638
            SHN: Shewana3_0386
            SHW: Sputw3181_3726
            ILO: IL2558(hemC)
            CPS: CPS_0074(hemC)
            PHA: PSHAa0098(hemC)
            PAT: Patl_0342
            SDE: Sde_3667
            PIN: Ping_3642
            MAQ: Maqu_0487
            CBU: CBU_2074(hemC)
            CBD: COXBU7E912_2170(hemC)
            LPN: lpg2735
            LPF: lpl2660(hemC)
            LPP: lpp2791(hemC)
            MCA: MCA3060(hemC)
            FTU: FTT0259(hemC)
            FTF: FTF0259(hemC)
            FTW: FTW_1818(hemC)
            FTL: FTL_0140
            FTH: FTH_0132(hemC)
            FTA: FTA_0152(hemC)
            FTN: FTN_0135(hemC)
            TCX: Tcr_0112
            NOC: Noc_0502
            AEH: Mlg_2670
            HHA: Hhal_1025
            HCH: HCH_00291(hemC)
            CSA: Csal_3109
            ABO: ABO_2322(hemC)
            MMW: Mmwyl1_3591
            AHA: AHA_0469(hemC)
            DNO: DNO_0299(hemC)
            BCI: BCI_0061(hemC)
            RMA: Rmag_0783
            VOK: COSY_0712(hemC)
            NME: NMB0539
            NMA: NMA0718(hemC)
            NMC: NMC0478(hemC)
            NGO: NGO0146
            CVI: CV_0054(hemC)
            RSO: RSc2357(hemC)
            REU: Reut_A0700
            REH: H16_A2920(hemC)
            RME: Rmet_2749
            BMA: BMA0730(hemC)
            BMV: BMASAVP1_A2284(hemC)
            BML: BMA10299_A3000(hemC)
            BMN: BMA10247_1597(hemC)
            BXE: Bxe_A3411
            BVI: Bcep1808_2509
            BUR: Bcep18194_A5752
            BCN: Bcen_1813
            BCH: Bcen2424_2425
            BAM: Bamb_2468
            BPS: BPSL1015(hemC)
            BPM: BURPS1710b_1229(hemC)
            BPL: BURPS1106A_1077(hemC)
            BPD: BURPS668_1071(hemC)
            BTE: BTH_I0872
            PNU: Pnuc_0656
            BPE: BP2537(hemC)
            BPA: BPP2642(hemC)
            BBR: BB2085(HemC)
            RFR: Rfer_1715
            POL: Bpro_3664
            PNA: Pnap_3090
            AAV: Aave_1999
            AJS: Ajs_2890
            VEI: Veis_1040
            MPT: Mpe_A3002
            HAR: HEAR1007(hemC)
            MMS: mma_1142(hemC)
            NEU: NE0590(hemC)
            NET: Neut_1037
            NMU: Nmul_A2690
            EBA: ebA1166(hemC)
            AZO: azo0993(hemC)
            DAR: Daro_3674
            TBD: Tbd_2568
            MFA: Mfla_0035
            HPY: HP0237(hemC)
            HPJ: jhp0222(hemC)
            HPA: HPAG1_0240
            HHE: HH1727(hemC)
            HAC: Hac_1381(hemC)
            WSU: WS1578(hemC)
            TDN: Tmden_0863
            CJE: Cj0545(hemC)
            CJR: CJE0649(hemC)
            CJJ: CJJ81176_0570(hemC)
            CJU: C8J_0506(hemC)
            CJD: JJD26997_1385(hemC)
            CFF: CFF8240_0691(hemC)
            CCV: CCV52592_0767(hemC) CCV52592_1588
            CHA: CHAB381_0899(hemC)
            CCO: CCC13826_1048(hemC)
            ABU: Abu_0283(hemC)
            NIS: NIS_1020(hemC)
            SUN: SUN_0634(hemC)
            GSU: GSU3285(hemC)
            GME: Gmet_3234
            GUR: Gura_0359
            PCA: Pcar_3063
            PPD: Ppro_3375
            DVU: DVU1890(hemC)
            DVL: Dvul_1273
            DDE: Dde_2621
            LIP: LI1011(hemC)
            BBA: Bd3447(hemC)
            DPS: DP0602
            ADE: Adeh_2492
            AFW: Anae109_1375
            MXA: MXAN_2656(hemC)
            SAT: SYN_02273
            SFU: Sfum_3202
            RPR: RP466(hemC)
            RTY: RT0453(hemC)
            RCO: RC0706(hemC)
            RFE: RF_0817(hemC)
            RBE: RBE_0346(hemC)
            RAK: A1C_03825(hemC)
            RBO: A1I_06040(hemC)
            RCM: A1E_02485(hemC)
            RRI: A1G_04275(hemC)
            OTS: OTBS_0843(hemC)
            WOL: WD0542(hemC)
            WBM: Wbm0777
            AMA: AM700(hemC)
            APH: APH_0746(hemC)
            ERU: Erum3690(hemC)
            ERW: ERWE_CDS_03800(hemC)
            ERG: ERGA_CDS_03750(hemC)
            ECN: Ecaj_0354
            ECH: ECH_0701(hemC)
            NSE: NSE_0385
            PUB: SAR11_0310(hemC)
            MLO: mll4223
            MES: Meso_3202
            PLA: Plav_1349
            SME: SMc03231(hemC)
            SMD: Smed_2966
            ATU: Atu2652(hemC)
            ATC: AGR_C_4808
            RET: RHE_CH03904(hemC)
            RLE: RL4495(hemC)
            BME: BMEI0176
            BMF: BAB1_1887
            BMS: BR1887(hemC)
            BMB: BruAb1_1864(hemC)
            BOV: BOV_1815(hemC)
            OAN: Oant_0975
            BJA: blr2398(hemC)
            BRA: BRADO1874(hemC)
            BBT: BBta_2191(hemC)
            RPA: RPA1505
            RPB: RPB_4018
            RPC: RPC_1249
            RPD: RPD_3772
            RPE: RPE_1305
            NWI: Nwi_0471
            NHA: Nham_0562
            XAU: Xaut_1158
            CCR: CC_0072
            SIL: SPO3649(hemC)
            SIT: TM1040_2529
            RSP: RSP_0679(hemC)
            RSH: Rsph17029_2334
            RSQ: Rsph17025_0551
            JAN: Jann_3845
            RDE: RD1_1283(hemC)
            PDE: Pden_3630
            MMR: Mmar10_0040
            HNE: HNE_3227(hemC)
            ZMO: ZMO1903(hemC)
            NAR: Saro_2786
            SAL: Sala_2876
            SWI: Swit_1936
            ELI: ELI_09155
            GOX: GOX1883
            GBE: GbCGDNIH1_2424
            ACR: Acry_0128
            RRU: Rru_A3568
            MAG: amb4420
            MGM: Mmc1_0737
            ABA: Acid345_2563
            SUS: Acid_3179
            BSU: BG10342(hemC)
            BHA: BH3046(hemC)
            BAN: BA4696(hemC)
            BAR: GBAA4696(hemC)
            BAA: BA_5135
            BAT: BAS4361
            BCE: BC4471
            BCA: BCE_4555(hemC)
            BCZ: BCZK4208(hemC)
            BCY: Bcer98_3180
            BTK: BT9727_4197(hemC)
            BTL: BALH_4057(hemC)
            BLI: BL00625(hemC)
            BLD: BLi02945(hemC)
            BCL: ABC2630(hemC)
            BPU: BPUM_2456(hemC)
            OIH: OB2068(hemC)
            GKA: GK2645
            SAU: SA1494(hemC)
            SAV: SAV1670(hemC)
            SAM: MW1614(hemC)
            SAR: SAR1750(hemC)
            SAS: SAS1599
            SAC: SACOL1717(hemC)
            SAB: SAB1530c(hemC)
            SAA: SAUSA300_1617(hemC)
            SAO: SAOUHSC_01774
            SAJ: SaurJH9_1728
            SAH: SaurJH1_1762
            SEP: SE1345
            SER: SERP1234(hemC)
            SHA: SH1257(hemC)
            SSP: SSP1094
            LMO: lmo1556(hemC)
            LMF: LMOf2365_1577(hemC)
            LIN: lin1591(hemC)
            LWE: lwe1569(hemC)
            SSA: SSA_0485
            LRE: Lreu_1702
            CAC: CAC0097(hemC)
            CPE: CPE1435(hemD)
            CPF: CPF_1688(hemC)
            CPR: CPR_1422(hemC)
            CTC: CTC00727
            CNO: NT01CX_0262(hemC)
            CTH: Cthe_2527
            CDF: CD3421(hemC)
            CBO: CBO0920(hemC)
            CBA: CLB_0961(hemC)
            CBH: CLC_0975(hemC)
            CBF: CLI_1007(hemC)
            CBE: Cbei_1285
            CKL: CKL_0718(hemC)
            AMT: Amet_0060
            CHY: CHY_1208(hemC)
            DSY: DSY2225
            DRM: Dred_2163
            SWO: Swol_0685
            CSC: Csac_1651
            MTA: Moth_1249
            MTU: Rv0510(hemC)
            MTC: MT0531(hemC)
            MBO: Mb0523(hemC)
            MBB: BCG_0553(hemC)
            MLE: ML2421(hemC)
            MPA: MAP4003(hemC)
            MAV: MAV_4639(hemC)
            MSM: MSMEG_0953(hemC)
            MVA: Mvan_0845
            MGI: Mflv_0066
            MMC: Mmcs_0677
            MKM: Mkms_0690
            MJL: Mjls_0670
            CGL: NCgl0403(cgl0418)
            CGB: cg0498(hemC)
            CEF: CE0436
            CDI: DIP0401(hemC)
            CJK: jk1901(hemC)
            NFA: nfa51690(hemC)
            RHA: RHA1_ro02052
            SCO: SCO3318(hemC) SCO7343(hemC)
            SMA: SAV1038(hemC2) SAV4740(hemC1)
            TWH: TWT732(hemC)
            TWS: TW746(hemC)
            LXX: Lxx01100(hemC)
            ART: Arth_2767
            AAU: AAur_2751(hemC)
            PAC: PPA0304
            NCA: Noca_0495
            TFU: Tfu_2732
            FRA: Francci3_0486
            FAL: FRAAL0984(hemC)
            ACE: Acel_0237
            KRA: Krad_0618
            SEN: SACE_6945(hemC)
            STP: Strop_0357
            RXY: Rxyl_1978
            FNU: FN0645
            RBA: RB6828(hemC)
            CTR: CT299(hemC)
            CTA: CTA_0321(hemC)
            CMU: TC0572
            CPN: CPn0052(hemC)
            CPA: CP0723
            CPJ: CPj0052(hemC)
            CPT: CpB0053
            CCA: CCA00340
            CAB: CAB332
            CFE: CF0666(hemC)
            LIL: LB011(hemC)
            LIC: LIC20009(hemC)
            LBJ: LBJ_4009(hemCD)
            LBL: LBL_4009(hemCD)
            SYN: slr1887(hemC)
            SYW: SYNW1785(hemC)
            SYC: syc0575_c(hemC)
            SYF: Synpcc7942_0967
            SYD: Syncc9605_0679
            SYE: Syncc9902_1680
            SYG: sync_2036(hemC)
            SYR: SynRCC307_0896(hemC)
            SYX: SynWH7803_0609(hemC)
            CYA: CYA_0243(hemC)
            CYB: CYB_1786(hemC)
            TEL: tll1646(hemC)
            GVI: glr3212(hemC)
            ANA: alr1878(hemC)
            AVA: Ava_4774
            PMA: Pro0494(hemC)
            PMM: PMM0495(hemC)
            PMT: PMT1273(hemC)
            PMN: PMN2A_1828
            PMI: PMT9312_0496
            PMB: A9601_05521(hemC)
            PMC: P9515_05591(hemC)
            PMF: P9303_07271(hemC)
            PMG: P9301_05221(hemC)
            PMH: P9215_05771(hemC)
            PME: NATL1_05521(hemC)
            TER: Tery_4621
            SRU: SRU_1554(hemC)
            CHU: CHU_0492(hemC)
            GFO: GFO_3224(hemC)
            FJO: Fjoh_0944
            FPS: FP0043(hemC)
            CTE: CT1427(hemC)
            CCH: Cag_1515
            CPH: Cpha266_1796
            PVI: Cvib_1245
            PLT: Plut_1427
            RRS: RoseRS_1750
            RCA: Rcas_2030
            DRA: DR_2352
            DGE: Dgeo_0093
            TTH: TTC1638
            TTJ: TTHA0345
            AAE: aq_263(hemC)
            TME: Tmel_0707
            MJA: MJ0569(hemC)
            MMP: MMP0872(hemC)
            MMQ: MmarC5_0680
            MMZ: MmarC7_0120
            MAE: Maeo_1324
            MVN: Mevan_0048
            MAC: MA0582(hemC)
            MBA: Mbar_A1465
            MMA: MM_1744
            MBU: Mbur_1226
            MTP: Mthe_1125
            MHU: Mhun_2559
            MEM: Memar_0983
            MBN: Mboo_1234
            MTH: MTH874
            MST: Msp_1332(hemC)
            MSI: Msm_0881
            MKA: MK0746(hemC)
            AFU: AF1242(hemC)
            HAL: VNG2330G(hem3)
            HMA: rrnAC3086(hemC)
            HWA: HQ3450A(hemC)
            NPH: NP1326A(hemC)
            TAC: Ta0572
            TVO: TVN0634
            PTO: PTO0249
            RCI: RCIX914(hemC)
            APE: APE_2298.1
            IHO: Igni_0684
            HBU: Hbut_0836
            SSO: SSO0183
            STO: ST0217
            SAI: Saci_0780(pbg)
            MSE: Msed_0217
            PAI: PAE0580(hemC)
            PIS: Pisl_0050
            PCL: Pcal_1707
            PAS: Pars_2245
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.61
            ExPASy - ENZYME nomenclature database: 2.5.1.61
            ExplorEnz - The Enzyme Database: 2.5.1.61
            ERGO genome analysis and discovery system: 2.5.1.61
            BRENDA, the Enzyme Database: 2.5.1.61
            CAS: 9074-91-3
///
ENTRY       EC 2.5.1.62                 Enzyme
NAME        chlorophyll synthase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     chlorophyllide-a:phytyl-diphosphate phytyltransferase
REACTION    chlorophyllide a + phytyl diphosphate = chlorophyll a + diphosphate
            [RN:R06284]
ALL_REAC    R06284
SUBSTRATE   chlorophyllide a [CPD:C02139];
            phytyl diphosphate [CPD:C05427]
PRODUCT     chlorophyll a [CPD:C05306];
            diphosphate [CPD:C00013]
COMMENT     Requires Mg2+. The enzyme is modified by binding of the first
            substrate, phytyl diphosphate, before reaction of the modified
            enzyme with the second substrate, chlorophyllide a, can occur. The
            reaction also occurs when phytyl diphosphate is replaced by
            geranylgeranyl diphosphate.
REFERENCE   1  [PMID:12530542]
  AUTHORS   Schmid HC, Rassadina V, Oster U, Schoch S, Rudiger W.
  TITLE     Pre-loading of chlorophyll synthase with tetraprenyl diphosphate is
            an obligatory step in chlorophyll biosynthesis.
  JOURNAL   Biol. Chem. 383 (2002) 1769-78.
  ORGANISM  Avena sativa
REFERENCE   2  [PMID:9092496]
  AUTHORS   Oster U, Bauer CE, Rudiger W.
  TITLE     Characterization of chlorophyll a and bacteriochlorophyll a
            synthases by heterologous expression in Escherichia coli.
  JOURNAL   J. Biol. Chem. 272 (1997) 9671-6.
  ORGANISM  Synechocystis sp.
REFERENCE   3  [PMID:7408876]
  AUTHORS   Rudiger W, Benz J, Guthoff C.
  TITLE     Detection and partial characterization of activity of chlorophyll
            synthetase in etioplast membranes.
  JOURNAL   Eur. J. Biochem. 109 (1980) 193-200.
  ORGANISM  Avena sativa
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K04040  Chlorophyll synthase
GENES       ATH: AT3G51820(ATG4/CHLG/G4)
            OSA: 4338498
            CME: CMT220C
            RPA: RPA1530(bchG)
            RPB: RPB_3992
            RPC: RPC_1302
            RPD: RPD_3747
            RPE: RPE_1336
            RSP: RSP_0279(bchG)
            JAN: Jann_0165
            RDE: RD1_0144(bchG)
            RRU: Rru_A0627
            SYN: slr0056(chlG)
            SYW: SYNW1677(chlG)
            SYC: syc2009_d(chlG)
            SYF: Synpcc7942_2084
            SYD: Syncc9605_0806
            SYE: Syncc9902_1573
            SYG: sync_0696(chlG)
            SYR: SynRCC307_0577(chlG)
            SYX: SynWH7803_1776(chlG)
            CYA: CYA_2138(chlG)
            CYB: CYB_0533(chlG)
            TEL: tll1539(chlG)
            GVI: glr1809(chlG)
            ANA: all4480(chlG)
            AVA: Ava_3341
            PMA: Pro0424(chlG)
            PMM: PMM0428(chlG)
            PMT: PMT0272(chlG)
            PMN: PMN2A_1759(chlG)
            PMI: PMT9312_0427
            PMB: A9601_04831(chlG)
            PMC: P9515_04901(chlG)
            PMF: P9303_20661(chlG)
            PMG: P9301_04521(chlG)
            PME: NATL1_04811(chlG)
            TER: Tery_0876
            CTE: CT1270(chlG) CT1610(bchG)
            CCH: Cag_1105 Cag_1742
            PLT: Plut_0911 Plut_1605
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.62
            ExPASy - ENZYME nomenclature database: 2.5.1.62
            ExplorEnz - The Enzyme Database: 2.5.1.62
            ERGO genome analysis and discovery system: 2.5.1.62
            BRENDA, the Enzyme Database: 2.5.1.62
///
ENTRY       EC 2.5.1.63                 Enzyme
NAME        adenosyl-fluoride synthase;
            fluorinase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     S-adenosyl-L-methionine:fluoride adenosyltransferase
REACTION    S-adenosyl-L-methionine + fluoride = 5'-deoxy-5'-fluoroadenosine +
            L-methionine
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            fluoride [CPD:C00742]
PRODUCT     5'-deoxy-5'-fluoroadenosine;
            L-methionine [CPD:C00073]
REFERENCE   1  [PMID:11907567]
  AUTHORS   O'Hagan D, Schaffrath C, Cobb SL, Hamilton JT, Murphy CD.
  TITLE     Biochemistry: biosynthesis of an organofluorine molecule.
  JOURNAL   Nature. 416 (2002) 279.
  ORGANISM  Streptomyces cattleya
REFERENCE   2  [PMID:14765200]
  AUTHORS   Dong C, Huang F, Deng H, Schaffrath C, Spencer JB, O'Hagan D,
            Naismith JH.
  TITLE     Crystal structure and mechanism of a bacterial fluorinating enzyme.
  JOURNAL   Nature. 427 (2004) 561-5.
  ORGANISM  Streptomyces cattleya
STRUCTURES  PDB: 1RQP  1RQR  2C2W  2C4T  2C4U  2C5B  2C5H  2CBX  2CC2  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.63
            ExPASy - ENZYME nomenclature database: 2.5.1.63
            ExplorEnz - The Enzyme Database: 2.5.1.63
            ERGO genome analysis and discovery system: 2.5.1.63
            BRENDA, the Enzyme Database: 2.5.1.63
///
ENTRY       EC 2.5.1.64                 Enzyme
NAME        2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase;
            2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate
            synthase---alpha-ketoglutarate decarboxylase;
            2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid synthase;
            6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate synthase;
            SHCHC synthase;
            2-oxoglutarate decarboxylase/SHCHC synthase;
            (1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate
            synthase;
            MenD
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     isochorismate:2-oxoglutarate:cyclodienyltransferase
            (decarboxylating, pyruvate-forming)
REACTION    2-oxoglutarate + isochorismate =
            (1S,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate +
            pyruvate + CO2 [RN:R06860]
ALL_REAC    R06860
SUBSTRATE   2-oxoglutarate [CPD:C00026];
            isochorismate [CPD:C00885]
PRODUCT     (1S,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
            [CPD:C05817];
            pyruvate [CPD:C00022];
            CO2 [CPD:C00011]
COMMENT     In the first step of the reaction, the oxoglutarate is
            decarboxylated and an adduct of the succinic semialdehyde is formed
            with thiamine diphosphate of the enzyme, as in both E1 of the
            2-oxoglutarate dehydrogenase complex [EC 1.2.4.2, oxoglutarate
            dehydrogenase (succinyl-transferring)] and in the reaction of
            2-oxoglutarate decarboxylase (EC 4.1.1.71), which liberates free
            succinic semialdehyde.
REFERENCE   1  [PMID:1459959]
  AUTHORS   Palaniappan C, Sharma V, Hudspeth ME, Meganathan R.
  TITLE     Menaquinone (vitamin K2) biosynthesis: evidence that the Escherichia
            coli menD gene encodes both
            2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid synthase
            and alpha-ketoglutarate decarboxylase activities.
  JOURNAL   J. Bacteriol. 174 (1992) 8111-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:8169214]
  AUTHORS   Palaniappan C, Taber H, Meganathan R.
  TITLE     Biosynthesis of o-succinylbenzoic acid in Bacillus subtilis:
            identification of menD mutants and evidence against the involvement
            of the alpha-ketoglutarate dehydrogenase complex.
  JOURNAL   J. Bacteriol. 176 (1994) 2648-53.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   3  [PMID:14621995]
  AUTHORS   Bhasin M, Billinsky JL, Palmer DR.
  TITLE     Steady-state kinetics and molecular evolution of Escherichia coli
            MenD [(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate
            synthase], an anomalous thiamin diphosphate-dependent
            decarboxylase-carboligase.
  JOURNAL   Biochemistry. 42 (2003) 13496-504.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:3902015]
  AUTHORS   Emmons GT, Campbell IM, Bentley R.
  TITLE     Vitamin K (menaquinone) biosynthesis in bacteria: purification and
            probable structure of an intermediate prior to o-succinylbenzoate.
  JOURNAL   Biochem. Biophys. Res. Commun. 131 (1985) 956-60.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00130  Ubiquinone biosynthesis
ORTHOLOGY   KO: K02551  2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate
                        synthase
GENES       ATH: AT1G68890
            ECO: b2264(menD)
            ECJ: JW5374(menD)
            ECE: Z3524(menD)
            ECS: ECs3152
            ECC: c2808(menD)
            ECI: UTI89_C2548(menD)
            ECP: ECP_2308
            STY: STY2540(menD)
            STT: t0554(menD)
            SPT: SPA0554(menD)
            SEC: SC2309(menD)
            STM: STM2309(menD)
            YPE: YPO2527(menD)
            YPK: y1660(menD)
            YPM: YP_2338(menD)
            YPA: YPA_2019
            YPN: YPN_2122
            YPP: YPDSF_1937
            YPS: YPTB2560(menD)
            SFL: SF2343(menD)
            SFX: S2477(menD)
            SFV: SFV_2335(menD)
            SSN: SSON_2325(menD)
            SBO: SBO_2301(menD)
            SDY: SDY_2460(menD)
            ECA: ECA1211(menD)
            PLU: plu3073(menD)
            HIN: HI0283(menD)
            HIT: NTHI0392(menD)
            HIP: CGSHiEE_01640
            HDU: HD1853(menD)
            HSO: HS_0617(menD)
            PMU: PM0054(menD)
            MSU: MS1794(menD)
            APL: APL_1750(menD)
            ASU: Asuc_0785
            VCH: VC1975
            VVU: VV1_3172
            VVY: VV1116
            VPA: VP0929
            VFI: VF1671
            PPR: PBPRA2624
            SON: SO_4573(menD)
            SFR: Sfri_0282
            SPL: Spea_3971
            SHE: Shewmr4_3767
            SHM: Shewmr7_3840
            SHN: Shewana3_3965
            DAR: Daro_2345
            BBA: Bd3484(menD)
            DPS: DP0253(menD)
            MXA: MXAN_3528(menD)
            SAT: SYN_02399
            BSU: BG10683(menD)
            BAN: BA5111(menD)
            BAR: GBAA5111(menD)
            BAA: BA_5529
            BAT: BAS4750
            BCE: BC4855
            BCA: BCE_5015(menD)
            BCZ: BCZK4610(menD)
            BTK: BT9727_4588(menD)
            BTL: BALH_4421(menD)
            BLI: BL02408(menD)
            BLD: BLi03222(menD)
            OIH: OB2325(menD)
            GKA: GK2875
            SAU: SA0896(menD)
            SAV: SAV1043(menD)
            SAM: MW0927(menD)
            SAR: SAR1017
            SAS: SAS0979
            SAJ: SaurJH9_1102
            SAH: SaurJH1_1125
            SEP: SE0744
            SER: SERP0630(menD)
            SHA: SH1919(menD)
            SSP: SSP1748
            LMO: lmo1675(menD)
            LMF: LMOf2365_1699(menD)
            LIN: lin1783(menD)
            LLA: L0169(menD)
            LLC: LACR_0773
            EFA: EF0448(menD)
            DSY: DSY0518(menD)
            MTU: Rv0555(menD)
            MTC: MT0581(menD)
            MBO: Mb0570(menD)
            MLE: ML2270(menD)
            MPA: MAP4052(menD)
            MGI: Mflv_5263
            CGL: NCgl0450(cgl0467)
            CEF: CE0478
            CDI: DIP0423
            NFA: nfa51330(menD)
            RHA: RHA1_ro01997(menD)
            TWH: TWT068(menD)
            TWS: TW078(menD)
            LXX: Lxx01490(menD)
            PAC: PPA0903
            TFU: Tfu_1411
            KRA: Krad_0646
            SEN: SACE_6913(menD)
            BLO: BL0231
            PCU: pc1068(menD)
            SYN: sll0603(menD)
            SYW: SYNW0997(menD)
            SYC: syc0121_d(menD)
            SYF: Synpcc7942_1435
            SYD: Syncc9605_1122
            SYE: Syncc9902_1334
            SYG: sync_1526(menD)
            SYR: SynRCC307_1140(menD)
            SYX: SynWH7803_1021(menD)
            TEL: tll0130(menD)
            ANA: alr0312(menD)
            PMA: Pro1054(menD)
            PMM: PMM0607(menD)
            PMT: PMT0406(menD)
            PMI: PMT9312_0607
            PMB: A9601_06631(menD)
            PMC: P9515_06721(menD)
            PMF: P9303_18801(menD)
            PMG: P9301_06331(menD)
            PMH: P9215_06891
            PME: NATL1_06631(menD)
            BTH: BT_4701
            BFR: BF1316
            BFS: BF1301(menD)
            PGI: PG1524(menD)
            CHU: CHU_1759(menD)
            GFO: GFO_2075(menD)
            FPS: FP1676(menD)
            CTE: CT1839(menD)
            PVI: Cvib_0397
            HAL: VNG1081G(menD)
            HMA: rrnAC0838(menD)
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.64
            ExPASy - ENZYME nomenclature database: 2.5.1.64
            ExplorEnz - The Enzyme Database: 2.5.1.64
            ERGO genome analysis and discovery system: 2.5.1.64
            BRENDA, the Enzyme Database: 2.5.1.64
///
ENTRY       EC 2.5.1.65                 Enzyme
NAME        O-phosphoserine sulfhydrylase;
            O-phosphoserine(thiol)-lyase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     O-phospho-L-serine:hydrogen-sulfide
            2-amino-2-carboxyethyltransferase
REACTION    O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
            [RN:R07274]
ALL_REAC    R07274;
            (other) R00897
SUBSTRATE   O-phospho-L-serine [CPD:C01005];
            hydrogen sulfide [CPD:C00283]
PRODUCT     L-cysteine [CPD:C00097];
            phosphate [CPD:C00009]
COMMENT     A pyridoxal-phosphate protein. The enzyme from Aeropyrum pernix acts
            on both O-phospho-L-serine and O3-acetyl-L-serine, in contrast with
            EC 2.5.1.47, cysteine synthase, which acts only on
            O3-acetyl-L-serine.
REFERENCE   1  [PMID:12965218]
  AUTHORS   Mino K, Ishikawa K.
  TITLE     A novel O-phospho-L-serine sulfhydrylation reaction catalyzed by
            O-acetylserine sulfhydrylase from Aeropyrum pernix K1.
  JOURNAL   FEBS. Lett. 551 (2003) 133-8.
  ORGANISM  Aeropyrum pernix [GN:ape]
REFERENCE   2  [PMID:12644499]
  AUTHORS   Mino K, Ishikawa K.
  TITLE     Characterization of a novel thermostable O-acetylserine
            sulfhydrylase from Aeropyrum pernix K1.
  JOURNAL   J. Bacteriol. 185 (2003) 2277-84.
  ORGANISM  Aeropyrum pernix [GN:ape]
REFERENCE   3  [PMID:12554945]
  AUTHORS   Mino K, Oda Y, Ataka M, Ishikawa K.
  TITLE     Crystallization and preliminary X-ray diffraction analysis of
            O-acetylserine sulfhydrylase from Aeropyrum pernix K1.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 59 (2003) 338-40.
  ORGANISM  Aeropyrum pernix [GN:ape]
PATHWAY     PATH: map00272  Cysteine metabolism
            PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K10150  O-phosphoserine sulfhydrylase
GENES       APE: APE_1586
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.65
            ExPASy - ENZYME nomenclature database: 2.5.1.65
            ExplorEnz - The Enzyme Database: 2.5.1.65
            ERGO genome analysis and discovery system: 2.5.1.65
            BRENDA, the Enzyme Database: 2.5.1.65
///
ENTRY       EC 2.5.1.66                 Enzyme
NAME        N2-(2-carboxyethyl)arginine synthase;
            CEAS;
            N2-(2-carboxyethyl)arginine synthetase;
            CEA synthetase;
            glyceraldehyde-3-phosphate:L-arginine 2-N-(2-hydroxy-3-oxopropyl)
            transferase (2-carboxyethyl-forming)
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     glyceraldehyde-3-phosphate:L-arginine N2-(2-hydroxy-3-oxopropyl)
            transferase (2-carboxyethyl-forming)
REACTION    D-glyceraldehyde 3-phosphate + L-arginine =
            N2-(2-carboxyethyl)-L-arginine + phosphate
ALL_REAC    (other) R05465
SUBSTRATE   D-glyceraldehyde 3-phosphate [CPD:C00118];
            L-arginine [CPD:C00062]
PRODUCT     N2-(2-carboxyethyl)-L-arginine;
            phosphate [CPD:C00009]
COMMENT     The enzyme requires thiamine diphosphate and catalyses the first
            step in the clavulanic-acid-biosynthesis pathway. The
            2-hydroxy-3-oxo group transferred from glyceraldehyde 3-phosphate is
            isomerized during transfer to form the 2-carboxyethyl group.
REFERENCE   1  [PMID:14623876]
  AUTHORS   Caines ME, Elkins JM, Hewitson KS, Schofield CJ.
  TITLE     Crystal structure and mechanistic implications of
            N2-(2-carboxyethyl)arginine synthase, the first enzyme in the
            clavulanic acid biosynthesis pathway.
  JOURNAL   J. Biol. Chem. 279 (2004) 5685-92.
  ORGANISM  Streptomyces clavuligerus
REFERENCE   2
  AUTHORS   Khaleeli, N., Li, R. and Townsend, C.A.
  TITLE     Origin of the beta-lactam carbons in clavulanic acid from an unusual
            thiamine pyrophosphate-mediated reaction.
  JOURNAL   J. Am. Chem. Soc. 121 (1999) 9223-9224.
  ORGANISM  Streptomyces clavuligerus
PATHWAY     PATH: map00331  Clavulanic acid biosynthesis
STRUCTURES  PDB: 2IHT  2IHV  
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.66
            ExPASy - ENZYME nomenclature database: 2.5.1.66
            ExplorEnz - The Enzyme Database: 2.5.1.66
            ERGO genome analysis and discovery system: 2.5.1.66
            BRENDA, the Enzyme Database: 2.5.1.66
///
ENTRY       EC 2.5.1.67                 Enzyme
NAME        chrysanthemyl diphosphate synthase;
            CPPase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     dimethylallyl-diphosphate:dimethylallyl-diphosphate
            dimethylallyltransferase (chrysanthemyl-diphosphate-forming)
REACTION    2 dimethylallyl diphosphate = diphosphate + chrysanthemyl
            diphosphate
SUBSTRATE   dimethylallyl diphosphate [CPD:C00235]
PRODUCT     diphosphate [CPD:C00013];
            chrysanthemyl diphosphate
COMMENT     Requires a divalent metal ion for activity, with Mg2+ being better
            than Mn2+ [1]. Chrysanthemyl diphosphate is a monoterpene with a
            non-head-to-tail linkage. It is unlike most monoterpenoids, which
            are derived from geranyl diphosphate and have isoprene units that
            are linked head-to-tail. The mechanism of its formation is similar
            to that of the early steps of squalene and phytoene biosynthesis.
            Chrysanthemyl diphosphate is the precursor of chrysanthemic acid,
            the acid half of the pyrethroid insecticides found in
            chrysanthemums.
REFERENCE   1  [PMID:11287653]
  AUTHORS   Rivera SB, Swedlund BD, King GJ, Bell RN, Hussey CE Jr,
            Shattuck-Eidens DM, Wrobel WM, Peiser GD, Poulter CD.
  TITLE     Chrysanthemyl diphosphate synthase: isolation of the gene and
            characterization of the recombinant non-head-to-tail monoterpene
            synthase from Chrysanthemum cinerariaefolium.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 4373-8.
REFERENCE   2  [PMID:12783539]
  AUTHORS   Erickson HK, Poulter CD.
  TITLE     Chrysanthemyl diphosphate synthase. The relationship among chain
            elongation, branching, and cyclopropanation reactions in the
            isoprenoid biosynthetic pathway.
  JOURNAL   J. Am. Chem. Soc. 125 (2003) 6886-8.
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.67
            ExPASy - ENZYME nomenclature database: 2.5.1.67
            ExplorEnz - The Enzyme Database: 2.5.1.67
            ERGO genome analysis and discovery system: 2.5.1.67
            BRENDA, the Enzyme Database: 2.5.1.67
///
ENTRY       EC 2.5.1.68                 Enzyme
NAME        Z-farnesyl diphosphate synthase;
            (Z)-farnesyl diphosphate synthase
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     geranyl-diphosphate:isopentenyl-diphosphate geranylcistransferase
REACTION    geranyl diphosphate + isopentenyl diphosphate = diphosphate +
            (2Z,6E)-farnesyl diphosphate
SUBSTRATE   geranyl diphosphate [CPD:C00341];
            isopentenyl diphosphate [CPD:C00129]
PRODUCT     diphosphate [CPD:C00013];
            (2Z,6E)-farnesyl diphosphate
COMMENT     Requires Mg2+ or Mn2+ for activity. The product of this reaction is
            an intermediate in the synthesis of decaprenyl phosphate, which
            plays a central role in the biosynthesis of most features of the
            mycobacterial cell wall, including peptidoglycan, linker unit
            galactan and arabinan. Neryl diphosphate can also act as substrate.
REFERENCE   1  [PMID:11152452]
  AUTHORS   Schulbach MC, Mahapatra S, Macchia M, Barontini S, Papi C, Minutolo
            F, Bertini S, Brennan PJ, Crick DC.
  TITLE     Purification, enzymatic characterization, and inhibition of the
            Z-farnesyl diphosphate synthase from Mycobacterium tuberculosis.
  JOURNAL   J. Biol. Chem. 276 (2001) 11624-30.
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.68
            ExPASy - ENZYME nomenclature database: 2.5.1.68
            ExplorEnz - The Enzyme Database: 2.5.1.68
            ERGO genome analysis and discovery system: 2.5.1.68
            BRENDA, the Enzyme Database: 2.5.1.68
///
ENTRY       EC 2.5.1.69                 Enzyme
NAME        lavandulyl diphosphate synthase;
            FDS-5
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     dimethylallyl-diphosphate:dimethylallyl-diphosphate
            dimethylallyltransferase (lavandulyl-diphosphate-forming)
REACTION    2 dimethylallyl diphosphate = diphosphate + lavandulyl diphosphate
SUBSTRATE   dimethylallyl diphosphate [CPD:C00235]
PRODUCT     diphosphate [CPD:C00013];
            lavandulyl diphosphate
COMMENT     Lavandulyl diphosphate is a monoterpene with a non-head-to-tail
            linkage. It is unlike most monoterpenoids, which are derived from
            geranyl diphosphate and have isoprene units that are linked
            head-to-tail. When this enzyme is incubated with dimethylallyl
            diphosphate and isopentenyl diphosphate, it also forms the regular
            monoterpene geranyl diphosphate [2]. The enzyme from Artemisia
            tridentata (big sagebrush) forms both lavandulyl diphosphate and
            chrysanthemyl diphosphate (see EC 2.5.1.67, chrysanthemyl
            diphosphate synthase) when dimethylally diphosphate is the sole
            substrate.
REFERENCE   1  [PMID:12783539]
  AUTHORS   Erickson HK, Poulter CD.
  TITLE     Chrysanthemyl diphosphate synthase. The relationship among chain
            elongation, branching, and cyclopropanation reactions in the
            isoprenoid biosynthetic pathway.
  JOURNAL   J. Am. Chem. Soc. 125 (2003) 6886-8.
REFERENCE   2  [PMID:12782626]
  AUTHORS   Hemmerlin A, Rivera SB, Erickson HK, Poulter CD.
  TITLE     Enzymes encoded by the farnesyl diphosphate synthase gene family in
            the Big Sagebrush Artemisia tridentata ssp. spiciformis.
  JOURNAL   J. Biol. Chem. 278 (2003) 32132-40.
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.69
            ExPASy - ENZYME nomenclature database: 2.5.1.69
            ExplorEnz - The Enzyme Database: 2.5.1.69
            ERGO genome analysis and discovery system: 2.5.1.69
            BRENDA, the Enzyme Database: 2.5.1.69
///
ENTRY       EC 2.5.1.70                 Enzyme
NAME        naringenin 8-dimethylallyltransferase;
            N8DT
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     dimethylallyl-diphosphate:naringenin 8-dimethylallyltransferase
REACTION    dimethylallyl diphosphate + (-)-(2S)-naringenin = diphosphate +
            sophoraflavanone B
SUBSTRATE   dimethylallyl diphosphate [CPD:C00235];
            (-)-(2S)-naringenin
PRODUCT     diphosphate [CPD:C00013];
            sophoraflavanone B
COMMENT     Requires Mg2+. This membrane-bound protein is located in the
            plastids [2]. In addition to naringenin, the enzyme can prenylate
            several other flavanones at the C-8 position, but more slowly. Along
            with EC 1.14.13.103 (8-dimethylallylnaringenin 2'-hydroxylase) and
            EC 2.5.1.71 (leachianone G 2''-dimethylallyltransferase), this
            enzyme forms part of the sophoraflavanone-G-biosynthesis pathway.
REFERENCE   1  [PMID:10975499]
  AUTHORS   Yamamoto H, Senda M, Inoue K.
  TITLE     Flavanone 8-dimethylallyltransferase in Sophora flavescens cell
            suspension cultures.
  JOURNAL   Phytochemistry. 54 (2000) 649-55.
REFERENCE   2  [PMID:14551337]
  AUTHORS   Zhao P, Inoue K, Kouno I, Yamamoto H.
  TITLE     Characterization of leachianone G 2"-dimethylallyltransferase, a
            novel prenyl side-chain elongation enzyme for the formation of the
            lavandulyl group of sophoraflavanone G in Sophora flavescens Ait.
            cell suspension cultures.
  JOURNAL   Plant. Physiol. 133 (2003) 1306-13.
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.70
            ExPASy - ENZYME nomenclature database: 2.5.1.70
            ExplorEnz - The Enzyme Database: 2.5.1.70
            ERGO genome analysis and discovery system: 2.5.1.70
            BRENDA, the Enzyme Database: 2.5.1.70
///
ENTRY       EC 2.5.1.71                 Enzyme
NAME        leachianone-G 2''-dimethylallyltransferase;
            LG 2''-dimethylallyltransferase;
            leachianone G 2''-dimethylallyltransferase;
            LGDT
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups (only
            sub-subclass identified to date)
SYSNAME     dimethylallyl-diphosphate:leachianone-G 2''-dimethylallyltransferase
REACTION    dimethylallyl diphosphate + leachianone G = diphosphate +
            sophoraflavanone G
SUBSTRATE   dimethylallyl diphosphate [CPD:C00235];
            leachianone G
PRODUCT     diphosphate [CPD:C00013];
            sophoraflavanone G
COMMENT     This membrane-bound enzyme is located in the plastids and requires
            Mg2+ for activity. The reaction forms the lavandulyl sidechain of
            sophoraflavanone G by transferring a dimethylallyl group to the 2''
            position of another dimethylallyl group attached at postiion 8 of
            leachianone G. The enzyme is specific for dimethylallyl diphosphate
            as the prenyl donor, as it cannot be replaced by isopentenyl
            diphosphate or geranyl diphosphate. Euchrenone a7 (a 5-deoxy
            derivative of leachianone G) and kenusanone I (a 7-methoxy
            derivative of leachianone G) can also act as substrates, but more
            slowly. Along with EC 1.14.13.103 (8-dimethylallylnaringenin
            2'-hydroxylase) and EC 2.5.1.70 (naringenin
            8-dimethylallyltransferase), this enzyme forms part of the
            sophoraflavanone-G-biosynthesis pathway.
REFERENCE   1  [PMID:14551337]
  AUTHORS   Zhao P, Inoue K, Kouno I, Yamamoto H.
  TITLE     Characterization of leachianone G 2"-dimethylallyltransferase, a
            novel prenyl side-chain elongation enzyme for the formation of the
            lavandulyl group of sophoraflavanone G in Sophora flavescens Ait.
            cell suspension cultures.
  JOURNAL   Plant. Physiol. 133 (2003) 1306-13.
DBLINKS     IUBMB Enzyme Nomenclature: 2.5.1.71
            ExPASy - ENZYME nomenclature database: 2.5.1.71
            ExplorEnz - The Enzyme Database: 2.5.1.71
            ERGO genome analysis and discovery system: 2.5.1.71
            BRENDA, the Enzyme Database: 2.5.1.71
///
ENTRY       EC 2.5.1.-                  Enzyme
CLASS       Transferases;
            Transferring alkyl or aryl groups, other than methyl groups;
            Transferring alkyl or aryl groups, other than methyl groups
REACTION    (1) trans,trans-Farnesyl diphosphate + Isopentenyl diphosphate <=>
            trans,trans,cis-Geranylgeranyl diphosphate + Pyrophosphate
            [RN:R05555];
            (2) trans,trans,cis-Geranylgeranyl diphosphate + Isopentenyl
            diphosphate <=> Dehydrodolichol diphosphate + Pyrophosphate
            [RN:R05556];
            (3) all-trans-Octaprenyl diphosphate + 4-Hydroxybenzoate <=>
            3-Octaprenyl-4-hydroxybenzoate + Pyrophosphate [RN:R05615];
            (4) all-trans-Hexaprenyl diphosphate + 4-Hydroxybenzoate <=>
            3-Hexaprenyl-4-hydroxybenzoate + Pyrophosphate [RN:R05616];
            (5) 1,4-Dihydroxy-2-naphthoate + all-trans-Octaprenyl diphosphate
            <=> 2-Demethylmenaquinone + Pyrophosphate + CO2 [RN:R05617];
            (6) 1,4-Dihydroxy-2-naphthoate + Phytyl diphosphate <=>
            2-Phytyl-1,4-naphthoquinone + CO2 + Pyrophosphate [RN:R06858];
            (7) Heme <=> Heme O [RN:R07411];
            (8) trans,trans-Farnesyl diphosphate <=> Dehydrosqualene [RN:R07652]
SUBSTRATE   trans,trans-Farnesyl diphosphate [CPD:C00448];
            Isopentenyl diphosphate [CPD:C00129];
            trans,trans,cis-Geranylgeranyl diphosphate [CPD:C11356];
            all-trans-Octaprenyl diphosphate [CPD:C04146];
            4-Hydroxybenzoate [CPD:C00156];
            all-trans-Hexaprenyl diphosphate [CPD:C01230];
            1,4-Dihydroxy-2-naphthoate [CPD:C03657];
            Phytyl diphosphate [CPD:C05427];
            Heme [CPD:C00032]
PRODUCT     trans,trans,cis-Geranylgeranyl diphosphate [CPD:C11356];
            Pyrophosphate [CPD:C00013];
            Dehydrodolichol diphosphate [CPD:C05859];
            3-Octaprenyl-4-hydroxybenzoate [CPD:C05809];
            3-Hexaprenyl-4-hydroxybenzoate [CPD:C13425];
            2-Demethylmenaquinone [CPD:C05818];
            CO2 [CPD:C00011];
            2-Phytyl-1,4-naphthoquinone [CPD:C13309];
            Heme O [CPD:C15672]
///
ENTRY       EC 2.6.1.1                  Enzyme
NAME        aspartate transaminase;
            glutamic-oxaloacetic transaminase;
            glutamic-aspartic transaminase;
            transaminase A;
            AAT;
            AspT;
            2-oxoglutarate-glutamate aminotransferase;
            aspartate alpha-ketoglutarate transaminase;
            aspartate aminotransferase;
            aspartate-2-oxoglutarate transaminase;
            aspartic acid aminotransferase;
            aspartic aminotransferase;
            aspartyl aminotransferase;
            AST;
            glutamate-oxalacetate aminotransferase;
            glutamate-oxalate transaminase;
            glutamic-aspartic aminotransferase;
            glutamic-oxalacetic transaminase;
            glutamic oxalic transaminase;
            GOT (enzyme);
            L-aspartate transaminase;
            L-aspartate-alpha-ketoglutarate transaminase;
            L-aspartate-2-ketoglutarate aminotransferase;
            L-aspartate-2-oxoglutarate aminotransferase;
            L-aspartate-2-oxoglutarate-transaminase;
            L-aspartic aminotransferase;
            oxaloacetate-aspartate aminotransferase;
            oxaloacetate transferase;
            aspartate:2-oxoglutarate aminotransferase;
            glutamate oxaloacetate transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-aspartate:2-oxoglutarate aminotransferase
REACTION    L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
            [RN:R00355]
ALL_REAC    R00355;
            (other) R00694 R00734 R00896 R02433 R02619 R05052
SUBSTRATE   L-aspartate [CPD:C00049];
            2-oxoglutarate [CPD:C00026]
PRODUCT     oxaloacetate [CPD:C00036];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also acts on L-tyrosine,
            L-phenylalanine and L-tryptophan. Aspartate transaminase activity
            can be formed from the aromatic-amino-acid transaminase (EC
            2.6.1.57) of Escherichia coli by controlled proteolysis [7], some EC
            2.6.1.57 activity can be found in this enzyme from other sources
            [8]; indeed the enzymes are identical in Trichomonas vaginalis [6].
REFERENCE   1
  AUTHORS   Banks, B.E.C. and Vernon, C.A.
  TITLE     Transamination. Part I. The isolation of the apoenzyme of
            glutamic-aspartic transaminase from pig heart muscle.
  JOURNAL   J. Chem. Soc. (Lond.) (1961) 1698-1705.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:5758538]
  AUTHORS   Bertland LH, Kaplan NO.
  TITLE     Chicken heart soluble aspartate aminotransferase. Purification and
            properties.
  JOURNAL   Biochemistry. 7 (1968) 134-42.
  ORGANISM  chicken [GN:gga]
REFERENCE   3
  AUTHORS   Forest, J.C. and Wightman, F.
  TITLE     Amino acid metabolism in plants. III. Purification and some
            properties of a multispecific aminotransferase isolated from
            bushbean seedlings (Phaseolus vulgaris L.).
  JOURNAL   Can. J. Biochem. 50 (1973) 813-829.
  ORGANISM  Phaseolus vulgaris
REFERENCE   4  [PMID:14155095]
  AUTHORS   HENSON CP, CLELAND WW.
  TITLE     KINETIC STUDIES OF GLUTAMIC OXALOACETIC TRANSAMINASE ISOZYMES.
  JOURNAL   Biochemistry. 3 (1964) 338-45.
  ORGANISM  pig [GN:ssc]
REFERENCE   5  [PMID:13610891]
  AUTHORS   JENKINS WT, YPHANTIS DA, SIZER IW.
  TITLE     Glutamic aspartic transaminase. I. Assay, purification, and general
            properties.
  JOURNAL   J. Biol. Chem. 234 (1959) 51-7.
  ORGANISM  pig [GN:ssc]
REFERENCE   6  [PMID:3879173]
  AUTHORS   Lowe PN, Rowe AF.
  TITLE     Aspartate: 2-oxoglutarate aminotransferase from trichomonas
            vaginalis. Identity of aspartate aminotransferase and aromatic amino
            acid aminotransferase.
  JOURNAL   Biochem. J. 232 (1985) 689-95.
  ORGANISM  Trichomonas vaginalis
REFERENCE   7  [PMID:236311]
  AUTHORS   Mavrides C, Orr W.
  TITLE     Multispecific aspartate and aromatic amino acid aminotransferases in
            Escherichia coli.
  JOURNAL   J. Biol. Chem. 250 (1975) 4128-33.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   8
  AUTHORS   Schreiber, G., Eckstein, M., Oeser, A. and Holzer, H.
  TITLE     [The concentration of aspartate aminotransferase from brewers'
            yeast].
  JOURNAL   Biochem. Z. 340 (1964) 13-20.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   9  [PMID:4623131]
  AUTHORS   Shrawder E, Martinez-Carrion M.
  TITLE     Evidence of phenylalanine transaminase activity in the isoenzymes of
            aspartate transaminase.
  JOURNAL   J. Biol. Chem. 247 (1972) 2486-92.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00252  Alanine and aspartate metabolism
            PATH: map00272  Cysteine metabolism
            PATH: map00330  Arginine and proline metabolism
            PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
            PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
            PATH: map00401  Novobiocin biosynthesis
            PATH: map00710  Carbon fixation
            PATH: map00950  Alkaloid biosynthesis I
ORTHOLOGY   KO: K00811  aspartate aminotransferase
            KO: K00812  aspartate aminotransferase
            KO: K00813  aspartate aminotransferase
GENES       HSA: 2805(GOT1) 2806(GOT2)
            PTR: 467989(GOT2)
            MMU: 14718(Got1) 14719(Got2)
            RNO: 24401(Got1) 25721(Got2)
            CFA: 486834(GOT1)
            BTA: 281206(GOT1) 286886(GOT2)
            SSC: 396967(CASPAT) 396968(GOT2)
            GGA: 396261(GOT1)
            XLA: 379947(got2) 380235(xr406)
            XTR: 407943(406)
            DRE: 406330(got1) 406688(got2a)
            SPU: 589279(LOC589279) 592180(LOC592180)
            DME: Dmel_CG4233(Got2) Dmel_CG8430(Got1)
            CEL: C14E2.2 C44E4.3(aminotransferase) T01C8.4(aminotransferase)
                 T01C8.5(aminotransferase)
            ATH: AT1G62800(ASP4) AT2G13810(ALD1) AT2G22250(AAT/ATAAT/MEE17)
                 AT2G30970(ASP1) AT5G11520(ASP3) AT5G19550(ASP2)
            OSA: 4324941 4325621 4328828 4331017 4331850 4331930 4341252
            CME: CMA077C CMC148C
            SCE: YKL106W(AAT1) YLR027C(AAT2)
            AGO: AGOS_ABL038W AGOS_AFR211C
            PIC: PICST_51039(AAT22) PICST_66059(AAT2)
            CAL: CaO19.3554 CaO19.6287(aat2)
            CGR: CAGL0D01892g CAGL0J04554g CAGL0K08580g
            SPO: SPAC10F6.13c SPBC725.01
            ANI: AN1993.2 AN6048.2
            AFM: AFUA_1G04160 AFUA_2G09650 AFUA_4G10410 AFUA_6G00290
                 AFUA_6G02490
            AOR: AO090003001171 AO090011000679
            CNE: CNM00360 CNM00950
            UMA: UM00595.1 UM04562.1
            DDI: DDB_0230092(aatA) DDB_0230093(aatB)
            PFA: PFB0200c
            TAN: TA12970
            TPV: TP02_0046
            TET: TTHERM_00192090 TTHERM_00673400 TTHERM_01369760
            TBR: Tb10.70.3710 Tb11.02.2740
            TCR: 503679.10 503841.70 510945.70
            LMA: LmjF24.0370 LmjF35.0820
            EHI: 83.t00021
            ECO: b0600(ybdL) b0928(aspC) b2290(yfbQ)
            ECJ: JW0593(ybdL) JW0911(aspC) JW2287(yfbQ)
            ECE: Z0743(ybdL) Z1275(aspC) Z3551
            ECS: ECs0639 ECs1011 ECs3174
            ECC: c0688(ybdL) c1070(aspC) c2831
            ECI: UTI89_C0603(ybdL) UTI89_C1000(aspC) UTI89_C2572
            ECP: ECP_0633 ECP_0939 ECP_2329
            ECV: APECO1_1449(ybdL) APECO1_40(aspC) APECO1_4274(yfbQ)
            ECW: EcE24377A_1027(aspC)
            ECX: EcHS_A1036
            STY: STY0647 STY1000(aspC) STY2561
            STT: t0533 t1936(aspC) t2265
            SPT: SPA0533(yfbQ) SPA1800(aspC) SPA2131(ybdL)
            SEC: SC0634(ybdL) SC0955(aspC) SC2332(yfbQ)
            STM: STM0603(ybdL) STM0998(aspC) STM2331(yfbQ)
            YPE: YPO0623 YPO1410(aspC) YPO2558(aat)
            YPK: y1628 y2760(aspC) y3555
            YPM: YP_1183(aspC) YP_2369(aat2) YP_2940(avtA2)
            YPA: YPA_0704 YPA_2049 YPA_3168
            YPN: YPN_0485 YPN_2152 YPN_2567
            YPP: YPDSF_2285
            YPS: YPTB0873(ybdL) YPTB1434(aspC) YPTB2589(aat) YPTB3432
            SFL: SF0515(ybdL) SF0925(aspC) SF2366(yfbQ)
            SFX: S0520(ybdL) S0989(aspC) S2501
            SFV: SFV_0549(ybdL) SFV_0930(aspC) SFV_2357
            SSN: SSON_0552(ybdL) SSON_0931(aspC) SSON_2347
            SBO: SBO_2219(aspC) SBO_2323
            SDY: SDY_0532(ybdL) SDY_2329(aspC) SDY_2486
            ECA: ECA2543(aspC) ECA3033 ECA3488 ECA4485(aatA)
            PLU: plu1750(aspC) plu3091
            WBR: WGLp124(aspC)
            SGL: SG1006 SG1602
            ENT: Ent638_1447
            SPE: Spro_1729 Spro_3088
            BFL: Bfl422(aspC)
            BPN: BPEN_434(aspC)
            HIN: HI0286(aspC) HI1617(aspC)
            HIT: NTHI0395(aspC3) NTHI1423(aspC)
            HIP: CGSHiEE_01635
            HDU: HD1419(aspC)
            HSO: HS_0619 HS_0838(aspC)
            PMU: PM0052 PM0621(aspC)
            MSU: MS1031(tyrB) MS1248(avtA) MS1797(avtA)
            APL: APL_0662(aspC) APL_1043
            ASU: Asuc_1574
            XFA: XF2396
            XFT: PD1411(aspC)
            XCC: XCC3364(aspC) XCC3503(aspC)
            XCB: XC_0658 XC_0800
            XCV: XCV0101 XCV0686(aspC) XCV3622
            XAC: XAC0630(aspC) XAC3494(aspC)
            XOO: XOO1094(aspC) XOO4000(aspC)
            XOM: XOO_0992(XOO0992) XOO_3771(XOO3771)
            VCH: VC1293 VC1977 VCA0513
            VCO: VC0395_A0911(aspC) VC0395_A2195(argD)
            VVU: VV1_2248 VV1_3174 VV2_0334
            VVY: VV1114 VV2096 VVA0892
            VPA: VP0927 VP1900 VPA0936
            VFI: VF1488 VF1673
            PPR: PBPRA2341 PBPRA2626(aat) PBPRB0692(aspC-1)
            PAE: PA2828 PA3798 PA4722 PA4976(aspC)
            PAU: PA14_14940(ybdL) PA14_62480(aspC) PA14_65770(aspC)
            PPU: PP_0858 PP_1872 PP_3721(aspC) PP_4692
            PPF: Pput_3787
            PST: PSPTO_0970 PSPTO_1440 PSPTO_1779 PSPTO_2925(aspB)
            PSB: Psyr_0836 Psyr_1253 Psyr_3615
            PSP: PSPPH_0862 PSPPH_1325 PSPPH_2453(aspB) PSPPH_3521(argD2)
                 PSPPH_3631
            PFL: PFL_2138(aspC) PFL_2715(aspC) PFL_3354(aspC) PFL_4247
                 PFL_4949 PFL_5024(aspB-3) PFL_5269
            PFO: Pfl_1874 Pfl_2905 Pfl_3983 Pfl_4596 Pfl_4803
            PEN: PSEEN1026 PSEEN1583 PSEEN3003(aspC) PSEEN3954 PSEEN4725
            PMY: Pmen_2738
            PAR: Psyc_0717
            PCR: Pcryo_0692 Pcryo_1557
            ACI: ACIAD2032 ACIAD2087 ACIAD2574(aspC) ACIAD3553
            ACB: A1S_2508
            SON: SO_2350(aspC-1) SO_2406(aspC-2) SO_2483
            SDN: Sden_1668 Sden_1750 Sden_1993
            SFR: Sfri_1907 Sfri_2024 Sfri_2126
            SAZ: Sama_1733 Sama_1805
            SBL: Sbal_2067 Sbal_2215
            SBM: Shew185_2156 Shew185_2282
            SLO: Shew_1951 Shew_1999
            SPC: Sputcn32_1945 Sputcn32_2045
            SSE: Ssed_2225 Ssed_2301
            SPL: Spea_2070 Spea_2228
            SHE: Shewmr4_1921 Shewmr4_2020 Shewmr4_2040
            SHM: Shewmr7_1935 Shewmr7_1955 Shewmr7_2057
            SHN: Shewana3_1974 Shewana3_2121 Shewana3_2145
            SHW: Sputw3181_1967 Sputw3181_2060
            ILO: IL1791
            CPS: CPS_3232 CPS_4970(aspC)
            PHA: PSHAa0956(aspC) PSHAa1323(yfbQ)
            PAT: Patl_1485 Patl_2034 Patl_4016
            SDE: Sde_1232
            PIN: Ping_1976
            MAQ: Maqu_1032
            CBU: CBU_0517(aspB)
            CBD: COXBU7E912_1545(aspC)
            LPN: lpg0070(aatA) lpg2532
            LPF: lpl0073 lpl2454(aspB)
            LPP: lpp0085 lpp2598(aspB)
            MCA: MCA2053 MCA2202
            FTU: FTT0884c(aspC1) FTT1165c(aspC2) FTT1413
            FTF: FTF0884c(aspC1) FTF1165c(aspC2) FTF1413
            FTW: FTW_1208
            FTL: FTL_0387 FTL_0648 FTL_0649 FTL_0789
            FTH: FTH_0378 FTH_0783(aat)
            FTN: FTN_0410 FTN_1146 FTN_1725(aspC)
            TCX: Tcr_1755 Tcr_1903
            NOC: Noc_0881 Noc_1138 Noc_2455
            AEH: Mlg_1087
            HHA: Hhal_0543
            HCH: HCH_02301 HCH_02799 HCH_04972
            CSA: Csal_0536 Csal_1320
            ABO: ABO_0346 ABO_0944(aspC) ABO_1183
            MMW: Mmwyl1_3552 Mmwyl1_4445
            AHA: AHA_2627 AHA_2783(aspC)
            BCI: BCI_0407(aspC)
            RMA: Rmag_0425
            VOK: COSY_0396(aspB)
            NME: NMB0540 NMB1473
            NMA: NMA0719(aspC) NMA1684
            NMC: NMC0479(aspC)
            NGO: NGO1047 NGO1452
            CVI: CV_0995
            RSO: RSc0710(RS05143) RSc1096(aspC) RSc1326(RS02848)
                 RSc2011(RS03579) RSp0943(aatA2) RSp1232(aatA1)
            REU: Reut_A0405 Reut_A0767 Reut_A1012 Reut_A1050 Reut_A1994
                 Reut_B4503
            RME: Rmet_0346 Rmet_0976 Rmet_1967 Rmet_2696
            BMA: BMA1801 BMA2148(aspB)
            BMV: BMASAVP1_A0761(aspB)
            BML: BMA10299_A2594(aspB)
            BMN: BMA10247_2019(aspB)
            BXE: Bxe_A0890 Bxe_A2382 Bxe_A2825 Bxe_A3182 Bxe_A4435 Bxe_B1173
            BVI: Bcep1808_2296 Bcep1808_4882
            BUR: Bcep18194_A3299 Bcep18194_A4055 Bcep18194_A4479
                 Bcep18194_A4480 Bcep18194_A5156 Bcep18194_A5338
                 Bcep18194_A5539 Bcep18194_A5553 Bcep18194_A5687
                 Bcep18194_B0395 Bcep18194_B0568 Bcep18194_B0828
                 Bcep18194_B1356 Bcep18194_B1670 Bcep18194_B1766
                 Bcep18194_B2171 Bcep18194_C6954
            BCN: Bcen_1613 Bcen_4017 Bcen_5866
            BCH: Bcen2424_0954 Bcen2424_1495 Bcen2424_1855 Bcen2424_2211
                 Bcen2424_2225 Bcen2424_4350
            BAM: Bamb_0815 Bamb_1377 Bamb_1793 Bamb_2249 Bamb_2263 Bamb_3759
            BPS: BPSL1239 BPSL1476 BPSL2629
            BPM: BURPS1710b_1465 BURPS1710b_2397 BURPS1710b_3104(aspB)
            BTE: BTH_I1088 BTH_I1528
            PNU: Pnuc_1496
            BPE: BP1062 BP1185(aspC)
            BPA: BPP0680(aatB) BPP1158 BPP1801(aspC) BPP2131 BPP3169
            BBR: BB0687(aatB) BB1045(aatB) BB1374 BB1528 BB3306(aspC) BB3570
                 BB4722(aatA) BB4736 BB5012
            RFR: Rfer_0881 Rfer_1911 Rfer_2111 Rfer_2174 Rfer_2671
            POL: Bpro_2175 Bpro_2189 Bpro_2403 Bpro_2888 Bpro_3262
            PNA: Pnap_1562
            AAV: Aave_2440 Aave_3888
            AJS: Ajs_2151
            VEI: Veis_2370
            MPT: Mpe_A1540 Mpe_A1947 Mpe_A2950
            HAR: HEAR1039 HEAR1325 HEAR2151(yfbQ) HEAR2244(tyrB) HEAR2824
            MMS: mma_1311 mma_1383 mma_2337
            NEU: NE0786(aatA) NE2362 NE2368
            NET: Neut_0866 Neut_1083
            NMU: Nmul_A1360 Nmul_A1552
            EBA: ebA4951
            AZO: azo0819(aspC) azo2082(yfbQ)
            DAR: Daro_0664 Daro_2387 Daro_3334
            TBD: Tbd_0768 Tbd_0842 Tbd_1569
            MFA: Mfla_0903 Mfla_1047 Mfla_1319
            HPY: HP0672(aspB)
            HPJ: jhp0615(aspB)
            HPA: HPAG1_0655
            HHE: HH1671
            HAC: Hac_0856(aspB)
            WSU: WS0310(aspB)
            TDN: Tmden_1134
            CJE: Cj0762c(aspB)
            CJR: CJE0853(aspC)
            CJJ: CJJ81176_0783(aspC)
            CJU: C8J_0713(aspB)
            CJD: JJD26997_1250
            CFF: CFF8240_0897
            CCV: CCV52592_1379
            CHA: CHAB381_0928
            CCO: CCC13826_1274
            ABU: Abu_0925(aspB3)
            NIS: NIS_0815 NIS_1554
            SUN: SUN_0224 SUN_1362
            GSU: GSU0117 GSU0162 GSU1061 GSU1242
            GME: Gmet_0213 Gmet_0732 Gmet_3325
            PCA: Pcar_0011 Pcar_0680 Pcar_1888 Pcar_2423
            PPD: Ppro_2189
            DVU: DVU0392 DVU0841 DVU3223(aspB)
            DDE: Dde_0513 Dde_1103 Dde_1970 Dde_2192 Dde_2730 Dde_3596
            LIP: LI0435(aspC)
            BBA: Bd0624(aspC)
            DPS: DP0617 DP1447 DP2165 DP2938
            ADE: Adeh_0533 Adeh_1731
            MXA: MXAN_3386
            SAT: SYN_00908 SYN_02699 SYN_02937
            SFU: Sfum_1171 Sfum_1665
            RPR: RP091(aatA)
            RTY: RT0046(aatA)
            RCO: RC0120(aatA)
            RFE: RF_0074(aatA)
            RBE: RBE_1333(aatA)
            RAK: A1C_00650
            RBO: A1I_00880
            RCM: A1E_00450
            RRI: A1G_00710
            OTS: OTBS_1766(aatA)
            WOL: WD1029(aspC)
            WBM: Wbm0002
            AMA: AM514(aatA) AM515(aatA)
            APH: APH_0660(aspC)
            ERU: Erum3490(aatA)
            ERW: ERWE_CDS_03560(aatA)
            ERG: ERGA_CDS_03520(aatA)
            ECN: Ecaj_0333
            ECH: ECH_0732
            NSE: NSE_0758
            PUB: SAR11_0080(aatA)
            MLO: mlr0210 mlr1282 mlr2541 mlr2987 mlr4213 mlr5693 mlr5883
                 mlr9116 mlr9118
            MES: Meso_1479 Meso_2107 Meso_2719
            SME: SMc01340 SMc01578(aatA) SMc02251 SMc02262 SMc04386(aatB)
            ATU: Atu0529(aspB) Atu1334(aspB) Atu2196(aatA) Atu4278(aatA)
            ATC: AGR_C_2460(aspB) AGR_C_3991 AGR_C_935 AGR_L_1171
            RET: RHE_CH00568(aspB1) RHE_CH01873(aspB2) RHE_CH02998(aatAch)
                 RHE_PC00186(aatAc) RHE_PF00273(ypf00130)
            RLE: RL0603 RL2092(aspB) RL3118 RL3443 RL4471(aspC) pRL100056
                 pRL100431(aatA) pRL120409(aatA) pRL90152
            BME: BMEI0516 BMEI1058
            BMF: BAB1_0929 BAB1_1514(aspC)
            BMS: BR0911 BR1495(aspC)
            BMB: BruAb1_0922 BruAb1_1488(aspC)
            BOV: BOV_1448(aspC)
            BJA: bll7416(aatA) blr3619(aatB) blr3627(aatA) blr4296(aspB)
            BRA: BRADO3492 BRADO3509 BRADO3571 BRADO5973(aatA)
            BBT: BBta_1248(aatB) BBta_1801(aatA) BBta_3995 BBta_4206 BBta_4224
            RPA: RPA2446 RPA4331(aatA)
            RPB: RPB_1297 RPB_3012
            RPC: RPC_2860 RPC_4122
            RPD: RPD_2440 RPD_3925
            RPE: RPE_2980 RPE_4176
            NWI: Nwi_0082 Nwi_1648 Nwi_1748 Nwi_2980
            NHA: Nham_1103 Nham_2183
            BHE: BH11640(aatA)
            BQU: BQ09260(aatA)
            BBK: BARBAKC583_0979(aatA)
            CCR: CC_1534 CC_2455
            SIL: SPO0584(aspC-1) SPO1264(aspC-2) SPO2132(aspC-3) SPO2589
                 SPOA0066
            SIT: TM1040_0865 TM1040_1734 TM1040_3605
            RSP: RSP_0763(aatA) RSP_2980(aspAT) RSP_3437 RSP_3439
            RSH: Rsph17029_2422
            JAN: Jann_2537 Jann_2654
            RDE: RD1_1835 RD1_2822(aspB) RD1_3185(aspC) RD1_3202(aspC)
                 RD1_3892(aatA)
            PDE: Pden_0938
            MMR: Mmar10_2149
            HNE: HNE_0889 HNE_2968(aatA)
            ZMO: ZMO0342(aatA) ZMO1950
            SAL: Sala_0172
            SWI: Swit_0763 Swit_4192
            GOX: GOX0189 GOX0190
            GBE: GbCGDNIH1_0380 GbCGDNIH1_0715 GbCGDNIH1_0716 GbCGDNIH1_0960
            RRU: Rru_A0776 Rru_A1135 Rru_A2084 Rru_A2411 Rru_A2423 Rru_A3706
            MAG: amb0555 amb1390
            MGM: Mmc1_0698 Mmc1_3276
            ABA: Acid345_0568 Acid345_1458 Acid345_2243 Acid345_2793
            BSU: BG10631(ywfG) BG11513(aspB) BG13024(yhdR)
            BHA: BH1695(aspB) BH2195
            BAN: BA1568(aspB)
            BAA: BA_2087
            BAT: BAS1454
            BCE: BC1546
            BCA: BCE_1674(aspB) BCE_4200(argD)
            BCZ: BCZK1427(aspB) BCZK2627(aspB)
            BTK: BT9727_1426(aspB) BT9727_2650(aspB)
            BTL: BALH_1397(aspB) BALH_4442(aspC)
            BLI: BL02746(aspB)
            BLD: BLi02372(aspB)
            BCL: ABC1492(mtnV) ABC2913(alaT)
            BAY: RBAM_013360 RBAM_020520
            BPU: BPUM_3424(ywfG)
            OIH: OB1760(aspB)
            GKA: GK2172 GK2928
            SAB: SAB1872
            SHA: SH1916(hisC)
            LMO: lmo1897(aspB) lmo2252
            LMF: LMOf2365_1926 LMOf2365_2285(aspB)
            LIN: lin2011(aspB) lin2354
            LWE: lwe1916(aspB) lwe2268
            LLA: L0098(aspB) L162604(aspC)
            LLC: LACR_0167 LACR_2022 LACR_2317
            LLM: llmg_0171(aspC) llmg_2019(aspB) llmg_2308(arcT)
            SPY: SPy_0650(aspC) SPy_1779
            SPZ: M5005_Spy_0537(aspC) M5005_Spy_1513
            SPM: spyM18_0711(aspC) spyM18_1849
            SPG: SpyM3_0460(aspC) SpyM3_1545
            SPS: SPs0321 SPs1395
            SPH: MGAS10270_Spy0531(aspC) MGAS10270_Spy1581
            SPI: MGAS10750_Spy0555(aspC) MGAS10750_Spy1573
            SPJ: MGAS2096_Spy0548(aspC) MGAS2096_Spy1540
            SPK: MGAS9429_Spy0527(aspC) MGAS9429_Spy1514
            SPF: SpyM51327(aspC)
            SPA: M6_Spy0557 M6_Spy1506
            SPB: M28_Spy0515(aspC) M28_Spy1502
            SPN: SP_1544 SP_1994
            SPR: spr1399(aspB) spr1808(aspC)
            SPD: SPD_1373(aspC)
            SAG: SAG0525(aspC) SAG1676
            SAN: gbs0571 gbs1720
            SAK: SAK_0676 SAK_1688
            SMU: SMU.1312(aspB) SMU.1826(yfbQ)
            STC: str0817(aspC1) str1636(aspC2)
            STL: stu0817(aspC1) stu1636(aspC2)
            SSA: SSA_0564 SSA_1383(aspB)
            SGO: SGO_0030(aspB) SGO_1297(aspC)
            LPL: lp_1739(aspB)
            LSL: LSL_0688
            LBR: LVIS_0855
            LCA: LSEI_1486
            EFA: EF0891 EF1314 EF2372(aspB)
            STH: STH1030
            CAC: CAC1001 CAC1819(aspB) CAC2832
            CPE: CPE1670(aspC)
            CPF: CPF_1924(aspB)
            CPR: CPR_0701 CPR_1642(aspB) CPR_1874
            CTC: CTC01294 CTC01309
            CNO: NT01CX_0284 NT01CX_2120 NT01CX_2121
            CDF: CD0107(aspC) CD1339
            CBO: CBO1804(aspC) CBO2015 CBO2399(aspC)
            CBA: CLB_1114 CLB_1739(aspB-1) CLB_1955(aspB-2) CLB_2262(aspB-3)
            CBH: CLC_1126 CLC_1746(aspB-1) CLC_1961(aspB-2) CLC_2245(aspB-3)
            CBF: CLI_1165 CLI_1799(aspB-1) CLI_2081(aspB-2) CLI_2454(aspB-3)
            CKL: CKL_0889(aspC1) CKL_1451(aspC2) CKL_1570(aspC3)
            CHY: CHY_1491(aspC)
            DSY: DSY1222 DSY3335 DSY3402 DSY4778
            SWO: Swol_2093
            CSC: Csac_1578
            TTE: TTE1206(avtA2) TTE1368(avtA3)
            MTA: Moth_1490 Moth_1955
            MTU: Rv0337c(aspC) Rv1178 Rv3565(aspB)
            MTC: MT0351(aspC) MT1215
            MBO: Mb0344c(aspC) Mb1211 Mb3595(aspB)
            MBB: BCG_0376c(aspC) BCG_3629(aspB)
            MLE: ML1488 ML2502
            MPA: MAP0502c(aspB) MAP2606c MAP3830c(aspC)
            MSM: MSMEG_0688 MSMEG_6017 MSMEG_6286
            MMC: Mmcs_0441 Mmcs_4029 Mmcs_4698
            CGL: NCgl0237(cgl0240) NCgl1058(cgl1103) NCgl2510(cgl2599)
                 NCgl2747(cgl2844)
            CGB: cg0294(aspB) cg3149
            CEF: CE1161 CE2489 CE2661
            CDI: DIP0974 DIP1929 DIP2136
            CJK: jk0175(aspC) jk1394(dapC)
            NFA: nfa47500 nfa54270 nfa5570
            RHA: RHA1_ro03290(aspC) RHA1_ro04781 RHA1_ro05465 RHA1_ro05947
            SCO: SCO4645(aspC) SCO4984(2SCK36.07c) SCO5136(SC9E12.21)
                 SCO6222(SC2H4.04c)
            SMA: SAV2008(aspB1) SAV3128(aspB2) SAV3285(aspB3) SAV4907(aspC1)
            TWH: TWT717(aspC)
            TWS: TW733(aspC)
            LXX: Lxx16230
            CMI: CMM_2790(aspC)
            AAU: AAur_1564(aspC) AAur_1949 AAur_2969 AAur_3909
            PAC: PPA0628 PPA1893
            TFU: Tfu_0492 Tfu_2661
            FRA: Francci3_0064 Francci3_0566 Francci3_3857
            FAL: FRAAL0078 FRAAL1062(aspC)
            ACE: Acel_0292
            SEN: SACE_1011(dapC) SACE_4319(aspB) SACE_6874(aspC)
                 SACE_7165(aspB)
            BLO: BL0628 BL0712 BL0783 BL1286(aspC) BL1564 BL1741
            BAD: BAD_0196 BAD_0244(aspC) BAD_0297 BAD_0831 BAD_1224
            FNU: FN0605 FN0625 FN1152
            RBA: RB12864(aspC) RB6821(aspC) RB8219(aspC)
            CTR: CT390(aspC) CT637(tyrB)
            CTA: CTA_0425(aspC)
            CMU: TC0005 TC0669
            CPN: CPn0495(aspC) CPn0740(tyrB)
            CPA: CP0005 CP0259
            CPJ: CPj0495(aspC) CPj0740(tyrB)
            CPT: CpB0515 CpB0768
            CCA: CCA00005 CCA00249
            CAB: CAB005 CAB245
            CFE: CF0757(aspC) CF1001(tyrB)
            PCU: pc0069(aspC) pc0685(aspC)
            TPA: TP0223
            LIL: LA0776 LA1293 LA2130 LA3052
            LIC: LIC11038 LIC11790(aspC) LIC12422(aspB) LIC12841(ywfG)
            LBJ: LBJ_0733 LBJ_1031 LBJ_1882 LBJ_2293
            LBL: LBL_0814 LBL_1402 LBL_2003 LBL_2347
            SYN: sll0402(aspC) slr0036(aspC)
            SYW: SYNW1171(aspC)
            SYC: syc1565_c(aspC)
            SYF: Synpcc7942_2545
            SYD: Syncc9605_1295
            SYE: Syncc9902_1182
            SYG: sync_1671(aspC)
            SYR: SynRCC307_1458(aspC)
            SYX: SynWH7803_1472(aspC)
            CYA: CYA_0815(aspC)
            CYB: CYB_1878(aspC)
            TEL: tll2357(aspC)
            GVI: glr2600
            ANA: alr1039 alr4853
            AVA: Ava_0017 Ava_0159 Ava_0899 Ava_1277 Ava_2127 Ava_3695
                 Ava_4157
            PMA: Pro1018
            PMM: PMM0674(aspC)
            PMT: PMT0779(aspC) PMT1029(aspC)
            PMN: PMN2A_0106
            PMI: PMT9312_0674
            PMB: A9601_07291(aspC)
            PMC: P9515_07471(aspC)
            PMF: P9303_10411 P9303_14321(aspC)
            PMG: P9301_07271(aspC)
            PMH: P9215_07591
            PME: NATL1_07311(aspC)
            TER: Tery_0293 Tery_2717
            BTH: BT_0547 BT_1476 BT_2415 BT_3720
            BFR: BF0595 BF1588 BF2643
            BFS: BF0545(aspC1) BF1601 BF2666 BF3859(aspC2)
            SRU: SRU_0938
            CHU: CHU_0694(ybdL) CHU_0784(aspB) CHU_0991 CHU_2704(aspB)
            GFO: GFO_0391(aatA) GFO_2931(aspB)
            FJO: Fjoh_1747
            FPS: FP0250(aspC3) FP0412(aspC1) FP1696(aspC2)
            CTE: CT0966 CT1381(aspC-2)
            CCH: Cag_0798 Cag_1027 Cag_1440
            PLT: Plut_1189 Plut_1353
            DET: DET1342(aspC)
            DEH: cbdb_A1292(aspC) cbdb_A714
            DRA: DR_0623
            DGE: Dgeo_1627
            TTH: TTC1641 TTC1960
            TTJ: TTHA0046 TTHA0342
            AAE: aq_1969(aspC1) aq_421(aspC3)
            TMA: TM1255 TM1698
            MJA: MJ0001 MJ0684(aspB2) MJ1391 MJ1479
            MMP: MMP1072 MMP1396
            MAC: MA0636(aspC) MA0925(tyrB) MA1385 MA1819(aspB)
            MBA: Mbar_A1546 Mbar_A2083 Mbar_A3133 Mbar_A3463
            MMA: MM_0243 MM_1802 MM_2041 MM_2368
            MBU: Mbur_0428 Mbur_1888 Mbur_2099
            MHU: Mhun_2478
            MTH: MTH1694 MTH1894 MTH52
            MST: Msp_0370 Msp_0510 Msp_0662 Msp_0924
            MSI: Msm_0788 Msm_1455
            MKA: MK1024
            AFU: AF1623(aspB-3) AF2129(aspB-2) AF2366(aspB-1)
            HAL: VNG0502G(aspB1) VNG0629G(aspB2) VNG1121G(aspC2)
            HMA: rrnAC0691(aspC4) rrnAC1251(aspB1) rrnAC1434(aspC3)
                 rrnAC3495(aspB2) rrnB0206(aspC1)
            HWA: HQ1237A(aspC) HQ1632A(aspC) HQ1812A(aspC) HQ2629A(aspC)
            NPH: NP0824A(aspC_4) NP1666A(aspC_2) NP4024A(aspC_1)
                 NP4410A(aspC_3)
            TAC: Ta0529m Ta0765
            TVO: TVN0848 TVN1005
            PTO: PTO1109
            PHO: PH0771 PH1322 PH1371
            PAB: PAB0525(aspC) PAB1523(aspB-2) PAB1810(aspB-like2)
            PFU: PF0522 PF1253 PF1497 PF1702
            TKO: TK0260 TK0548 TK1094 TK2268
            RCI: LRC221(aat-1) RCIX1738(aat-2) RCIX1962(aat-3) RRC55(aat-4)
                 RRC58(aat-5)
            APE: APE_0674.1 APE_2248.1 APE_2575
            IHO: Igni_0946
            HBU: Hbut_1044
            SSO: SSO0897(aspB-2) SSO1177(aspB-3) SSO3245(aspB-4)
            STO: ST1225 ST2333
            SAI: Saci_1014 Saci_1428(aspB) Saci_1837
            PAI: PAE1964(aspC) PAE2251
STRUCTURES  PDB: 1AAM  1AAT  1AAW  1AHE  1AHF  1AHG  1AHX  1AHY  1AIA  1AIB  
                 1AIC  1AJR  1AJS  1AKA  1AKB  1AKC  1AMA  1AMQ  1AMR  1AMS  
                 1ARG  1ARH  1ARI  1ARS  1ART  1ASA  1ASB  1ASC  1ASD  1ASE  
                 1ASF  1ASG  1ASL  1ASM  1ASN  1B4X  1B5O  1B5P  1BJW  1BKG  
                 1BQA  1BQD  1C9C  1CQ6  1CQ7  1CQ8  1CZC  1CZE  1G4V  1G4X  
                 1G7W  1G7X  1GC3  1GC4  1GCK  1IVR  1IX6  1IX7  1IX8  1J32  
                 1MAP  1MAQ  1O4S  1OXO  1OXP  1QIR  1QIS  1QIT  1SPA  1TAR  
                 1TAS  1TAT  1TOE  1TOG  1TOI  1TOJ  1TOK  1X28  1X29  1X2A  
                 1YAA  1YOO  2AAT  2CST  2D5Y  2D61  2D63  2D64  2D65  2D66  
                 2D7Y  2D7Z  2O1B  2Q7W  2QBT  3AAT  5BJ3  5BJ4  5EAA  7AAT  
                 8AAT  9AAT  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.1
            ExPASy - ENZYME nomenclature database: 2.6.1.1
            ExplorEnz - The Enzyme Database: 2.6.1.1
            ERGO genome analysis and discovery system: 2.6.1.1
            BRENDA, the Enzyme Database: 2.6.1.1
            CAS: 9000-97-9
///
ENTRY       EC 2.6.1.2                  Enzyme
NAME        alanine transaminase;
            glutamic-pyruvic transaminase;
            glutamic-alanine transaminase;
            GPT;
            beta-alanine aminotransferase;
            alanine aminotransferase;
            alanine-alpha-ketoglutarate aminotransferase;
            alanine-pyruvate aminotransferase;
            ALT;
            glutamic acid-pyruvic acid transaminase;
            glutamic-pyruvic aminotransferase;
            L-alanine aminotransferase;
            L-alanine transaminase;
            L-alanine-alpha-ketoglutarate aminotransferase;
            pyruvate transaminase;
            pyruvate-alanine aminotransferase;
            pyruvate-glutamate transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-alanine:2-oxoglutarate aminotransferase
REACTION    L-alanine + 2-oxoglutarate = pyruvate + L-glutamate [RN:R00258]
ALL_REAC    R00258
SUBSTRATE   L-alanine [CPD:C00041];
            2-oxoglutarate [CPD:C00026]
PRODUCT     pyruvate [CPD:C00022];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. 2-Aminobutanoate can act slowly
            instead of alanine.
REFERENCE   1  [PMID:5452003]
  AUTHORS   Dumitru IF, Iordachescu D, Niculescu S.
  TITLE     Chromatographic purification, crystallization and study of vegetable
            L-alanine: 2-oxoglutarate-aminotransferase properties.
  JOURNAL   Experientia. 26 (1970) 837-8.
  ORGANISM  Glycine hispida
REFERENCE   2
  AUTHORS   Dumitru, I.F., Iordachescu, D. and Niculescu, S.
  TITLE     L-Alanine: 2-oxoglutarate-aminotransferase chromatographic
            purification and crystallization of the enzyme from seeds of Glycine
            hispida var Cheepeura.
  JOURNAL   Rev. Roum. Biochim. 7 (1970) 31-44.
  ORGANISM  Glycine hispida
REFERENCE   3
  AUTHORS   Green, D.E., Leloir, L.F. and Nocito, W.
  TITLE     Transaminases.
  JOURNAL   J. Biol. Chem. 161 (1945) 559-582.
  ORGANISM  pig [GN:ssc]
REFERENCE   4
  AUTHORS   Iordachescu, D., Dumitru, I.F. and Corniciuc, M.-T.
  TITLE     Comparative biochemical studies concerning L-alanine:
            2-oxoglutarate-aminotransferase from the liver and the bile of
            swines.
  JOURNAL   Rev. Roum. Biochim. 20 (1983) 173-179.
  ORGANISM  pig [GN:ssc]
REFERENCE   5
  AUTHORS   Wilson, D.G., King, K.W. and Burris, R.H.
  TITLE     Transaminase reactions in plants.
  JOURNAL   J. Biol. Chem. 208 (1954) 863-874.
  ORGANISM  white lupine, Hordeum vulgare [GN:ehvu]
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00252  Alanine and aspartate metabolism
            PATH: map00710  Carbon fixation
ORTHOLOGY   KO: K00814  alanine transaminase
GENES       HSA: 2875(GPT) 84706(GPT2)
            MMU: 108682(Gpt2) 76282(Gpt1)
            RNO: 81670(Gpt1)
            CFA: 609510(LOC609510)
            GGA: 415746(GPT2)
            XLA: 444533(gpt2)
            DME: Dmel_CG1640
            CEL: C32F10.8
            OSA: 4342210 4348524
            CME: CMM066C
            SCE: YDR111C(ALT2) YLR089C(ALT1)
            AGO: AGOS_AGR085W
            PIC: PICST_70108(ALA2)
            CGR: CAGL0L12254g
            SPO: SPBC582.08
            ANI: AN1923.2
            AFM: AFUA_6G07770
            AOR: AO090003000164
            CNE: CNG01490
            DDI: DDB_0232139
            TET: TTHERM_00302100
            TBR: Tb927.1.3950
            TCR: 506529.420 506529.430 510889.120 510889.140
            LMA: LmjF12.0630
            EHI: 233.t00009 24.t00016
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.2
            ExPASy - ENZYME nomenclature database: 2.6.1.2
            ExplorEnz - The Enzyme Database: 2.6.1.2
            ERGO genome analysis and discovery system: 2.6.1.2
            BRENDA, the Enzyme Database: 2.6.1.2
            CAS: 9000-86-6
///
ENTRY       EC 2.6.1.3                  Enzyme
NAME        cysteine transaminase;
            cysteine aminotransferase;
            L-cysteine aminotransferase;
            CGT
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-cysteine:2-oxoglutarate aminotransferase
REACTION    L-cysteine + 2-oxoglutarate = mercaptopyruvate + L-glutamate
            [RN:R00895]
ALL_REAC    R00895
SUBSTRATE   L-cysteine [CPD:C00097];
            2-oxoglutarate [CPD:C00026]
PRODUCT     mercaptopyruvate [CPD:C00957];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:13342749]
  AUTHORS   CHATAGNER F, SAURET-IGNAZI G.
  TITLE     [Role of transamination and pyridoxal phosphate in the enzymatic
            formation of hydrogen sulfide from cysteine by the rat liver under
            anaerobiosis.]
  JOURNAL   Bull. Soc. Chim. Biol. (Paris). 38 (1956) 415-28.
PATHWAY     PATH: map00272  Cysteine metabolism
GENES       REH: H16_B1170
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.3
            ExPASy - ENZYME nomenclature database: 2.6.1.3
            ExplorEnz - The Enzyme Database: 2.6.1.3
            ERGO genome analysis and discovery system: 2.6.1.3
            BRENDA, the Enzyme Database: 2.6.1.3
            CAS: 9030-32-4
///
ENTRY       EC 2.6.1.4                  Enzyme
NAME        glycine transaminase;
            glutamic-glyoxylic transaminase;
            glycine aminotransferase;
            glyoxylate-glutamic transaminase;
            L-glutamate:glyoxylate aminotransferase;
            glyoxylate-glutamate aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     glycine:2-oxoglutarate aminotransferase
REACTION    glycine + 2-oxoglutarate = glyoxylate + L-glutamate [RN:R00372]
ALL_REAC    R00372
SUBSTRATE   glycine [CPD:C00037];
            2-oxoglutarate [CPD:C00026]
PRODUCT     glyoxylate [CPD:C00048];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1
  AUTHORS   Nakada, H.I.
  TITLE     Glutamic-glycine transaminase from rat liver.
  JOURNAL   J. Biol. Chem. 239 (1964) 468-471.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Thompson, J.S. and Richardson, K.E.
  TITLE     Isolation and chracterization of a glutamate-glycine transaminase
            from human liver.
  JOURNAL   Arch. Biochem. Biophys. 117 (1966) 599-603.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.4
            ExPASy - ENZYME nomenclature database: 2.6.1.4
            ExplorEnz - The Enzyme Database: 2.6.1.4
            ERGO genome analysis and discovery system: 2.6.1.4
            BRENDA, the Enzyme Database: 2.6.1.4
            CAS: 9032-99-9
///
ENTRY       EC 2.6.1.5                  Enzyme
NAME        tyrosine transaminase;
            tyrosine aminotransferase;
            glutamic-hydroxyphenylpyruvic transaminase;
            glutamic phenylpyruvic aminotransferase;
            L-phenylalanine 2-oxoglutarate aminotransferase;
            L-tyrosine aminotransferase;
            phenylalanine aminotransferase;
            phenylalanine transaminase;
            phenylalanine-alpha-ketoglutarate transaminase;
            phenylpyruvate transaminase;
            phenylpyruvic acid transaminase;
            tyrosine-alpha-ketoglutarate aminotransferase;
            tyrosine-alpha-ketoglutarate transaminase;
            tyrosine-2-ketoglutarate aminotransferase;
            TyrAT
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-tyrosine:2-oxoglutarate aminotransferase
REACTION    L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate
            [RN:R00734]
ALL_REAC    R00734;
            (other) R00694 R07396
SUBSTRATE   L-tyrosine [CPD:C00082];
            2-oxoglutarate [CPD:C00026]
PRODUCT     4-hydroxyphenylpyruvate [CPD:C01179];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. L-Phenylalanine can act instead of
            L-tyrosine. The mitochondrial enzyme may be identical with EC
            2.6.1.1 (aspartate transaminase). The three isoenzymic forms are
            interconverted by EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33
            (fruit bromelain). The enzyme can also catalyse the final step in
            the methionine-salvage pathway of Klebsiella pneumoniae [8].
REFERENCE   1  [PMID:13366978]
  AUTHORS   CANELLAKIS ZN, COHEN PP.
  TITLE     Purification studies of tyrosine-alpha-ketoglutaric acid
            transaminase.
  JOURNAL   J. Biol. Chem. 222 (1956) 53-62.
  ORGANISM  dog [GN:cfa]
REFERENCE   2  [PMID:13366979]
  AUTHORS   CANELLAKIS ZN, COHEN PP.
  TITLE     Kinetic and substrate specificity study of
            tyrosine-alpha-ketoglutaric acid transaminase.
  JOURNAL   J. Biol. Chem. 222 (1956) 63-71.
  ORGANISM  dog [GN:cfa]
REFERENCE   3  [PMID:14171223]
  AUTHORS   JACOBY GA, LADU BN.
  TITLE     STUDIES ON THE SPECIFICITY OF TYROSINE-ALPHA-KETOGLUTARATE
            TRANSAMINASE.
  JOURNAL   J. Biol. Chem. 239 (1964) 419-24.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:14408534]
  AUTHORS   KENNEY FT.
  TITLE     Properties of partially purified tyrosine-alpha-ketoglutarate
            transaminase from rat liver.
  JOURNAL   J. Biol. Chem. 234 (1959) 2707-12.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:4396841]
  AUTHORS   Miller JE, Litwack G.
  TITLE     Purification, properties, and identity of liver mitochondrial
            tyrosine aminotransferase.
  JOURNAL   J. Biol. Chem. 246 (1971) 3234-40.
  ORGANISM  rat [GN:rno]
REFERENCE   6  [PMID:13363833]
  AUTHORS   ROWSELL EV.
  TITLE     Transaminations with L-glutamate and alpha-oxoglutarate in fresh
            extracts of animal tissues.
  JOURNAL   Biochem. J. 64 (1956) 235-45.
  ORGANISM  pig [GN:ssc]
REFERENCE   7
  AUTHORS   SentheShanmuganathan, S.
  TITLE     The purification and properties of the tyrosine-2-oxoglutarate
            transaminase of Saccharomyces cerevisiae.
  JOURNAL   Biochem. J. 77 (1960) 619-625.
  ORGANISM  dog [GN:cfa], Saccharomyces cerevisiae [GN:sce]
REFERENCE   8  [PMID:10074065]
  AUTHORS   Heilbronn J, Wilson J, Berger BJ.
  TITLE     Tyrosine aminotransferase catalyzes the final step of methionine
            recycling in Klebsiella pneumoniae.
  JOURNAL   J. Bacteriol. 181 (1999) 1739-47.
  ORGANISM  Klebsiella pneumoniae
PATHWAY     PATH: map00271  Methionine metabolism
            PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
            PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
            PATH: map00401  Novobiocin biosynthesis
            PATH: map00950  Alkaloid biosynthesis I
ORTHOLOGY   KO: K00815  tyrosine aminotransferase
GENES       HSA: 6898(TAT)
            PTR: 454227(TAT)
            MMU: 234724(Tat)
            RNO: 24813(Tat)
            CFA: 479665(TAT)
            GGA: 415884(TAT)
            XTR: 448486(tat)
            SPU: 592114(LOC592114)
            DME: Dmel_CG1461
            CEL: F42D1.2
            OSA: 4329098 4329101
            CME: CMT533C
            DDI: DDB_0230996(tat)
            TET: TTHERM_00046180 TTHERM_00554320 TTHERM_00683360
            TCR: 508535.50 510187.20 510187.30 510187.40 510187.50 510187.70
                 510795.10 511461.20
            LMA: LmjF36.2360
            SME: SMc00387(tatA)
            SMD: Smed_3509
            BRA: BRADO3492
            BBT: BBta_4224
            NAR: Saro_0792
            SWI: Swit_2700
            ELI: ELI_00130
            BPU: BPUM_1993(hisC)
            SGO: SGO_0963
STRUCTURES  PDB: 1BW0  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.5
            ExPASy - ENZYME nomenclature database: 2.6.1.5
            ExplorEnz - The Enzyme Database: 2.6.1.5
            ERGO genome analysis and discovery system: 2.6.1.5
            UM-BBD (Biocatalysis/Biodegradation Database): 2.6.1.5
            BRENDA, the Enzyme Database: 2.6.1.5
            CAS: 9014-55-5
///
ENTRY       EC 2.6.1.6                  Enzyme
NAME        leucine transaminase;
            L-leucine aminotransferase;
            leucine 2-oxoglutarate transaminase;
            leucine aminotransferase;
            leucine-alpha-ketoglutarate transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-leucine:2-oxoglutarate aminotransferase
REACTION    L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
            [RN:R01090]
ALL_REAC    R01090;
            (other) R01214
SUBSTRATE   L-leucine [CPD:C00123];
            2-oxoglutarate [CPD:C00026]
PRODUCT     4-methyl-2-oxopentanoate [CPD:C00233];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. This enzyme differs from EC 2.6.1.42,
            branched-chain-amino-acid transaminase, in that it does not act on
            L-valine or L-isoleucine, although it does act on L-methionine. The
            mitochondrial form from rat liver differs in physical
            characteristics from the cytoplasmic form.
REFERENCE   1  [PMID:4968655]
  AUTHORS   Aki K, Ogawa K, Ichihara A.
  TITLE     Transaminases of branched chain amino acids. IV. Purification and
            properties of two enzymes from rat liver.
  JOURNAL   Biochim. Biophys. Acta. 159 (1968) 276-84.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:974100]
  AUTHORS   Ikeda T, Konishi Y, Ichihara A.
  TITLE     Transaminase of branched chain amino acids. XI. Leucine (methionine)
            transaminase of rat liver mitochondria.
  JOURNAL   Biochim. Biophys. Acta. 445 (1976) 622-31.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00290  Valine, leucine and isoleucine biosynthesis
            PATH: map00770  Pantothenate and CoA biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.6
            ExPASy - ENZYME nomenclature database: 2.6.1.6
            ExplorEnz - The Enzyme Database: 2.6.1.6
            ERGO genome analysis and discovery system: 2.6.1.6
            BRENDA, the Enzyme Database: 2.6.1.6
            CAS: 9030-37-9
///
ENTRY       EC 2.6.1.7                  Enzyme
NAME        kynurenine---oxoglutarate transaminase;
            kynurenine transaminase (cyclizing);
            kynurenine 2-oxoglutarate transaminase;
            kynurenine aminotransferase;
            L-kynurenine aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-kynurenine:2-oxoglutarate aminotransferase
REACTION    L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate
            + L-glutamate [RN:R01956]
ALL_REAC    R01956;
            (other) R04171
SUBSTRATE   L-kynurenine [CPD:C00328];
            2-oxoglutarate [CPD:C00026]
PRODUCT     4-(2-aminophenyl)-2,4-dioxobutanoate [CPD:C01252];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also acts on 3-hydroxykynurenine. The
            product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into
            kynurenate by a spontaneous reaction.
REFERENCE   1  [PMID:13357462]
  AUTHORS   BONNER DM, JAKOBY WB.
  TITLE     Kynurenine transaminase from neurospora.
  JOURNAL   J. Biol. Chem. 221 (1956) 689-95.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2  [PMID:13449053]
  AUTHORS   MASON M.
  TITLE     Kynurenine transaminase of rat kidney; a study of coenzyme
            dissociation.
  JOURNAL   J. Biol. Chem. 227 (1957) 61-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00380  Tryptophan metabolism
ORTHOLOGY   KO: K00816  kynurenine-oxoglutarate transaminase
GENES       HSA: 51166(AADAT)
            PTR: 461601(AADAT)
            MMU: 23923(Aadat) 70266(Ccbl1)
            RNO: 311844(Ccbl1)
            CFA: 491310(CCBL1)
            XLA: 398787(MGC68542)
            XTR: 496662(LOC496662)
            UMA: UM01804.1 UM03538.1
            DDI: DDBDRAFT_0187583
STRUCTURES  PDB: 1X0M  1YIY  1YIZ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.7
            ExPASy - ENZYME nomenclature database: 2.6.1.7
            ExplorEnz - The Enzyme Database: 2.6.1.7
            ERGO genome analysis and discovery system: 2.6.1.7
            BRENDA, the Enzyme Database: 2.6.1.7
            CAS: 9030-38-0
///
ENTRY       EC 2.6.1.8                  Enzyme
NAME        2,5-diaminovalerate transaminase;
            diamino-acid transaminase;
            diamino acid aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     2,5-diaminopentanoate:2-oxoglutarate aminotransferase
REACTION    2,5-diaminopentanoate + 2-oxoglutarate = 5-amino-2-oxopentanoate +
            L-glutamate [RN:R03248]
ALL_REAC    R03248
SUBSTRATE   2,5-diaminopentanoate [CPD:C01602];
            2-oxoglutarate [CPD:C00026]
PRODUCT     5-amino-2-oxopentanoate [CPD:C01110];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. 2,5-Diaminoglutarate can act instead
            of diaminopentanoate.
REFERENCE   1  [PMID:13125615]
  AUTHORS   ROBERTS E.
  TITLE     Studies of transamination.
  JOURNAL   Arch. Biochem. Biophys. 48 (1954) 395-401.
  ORGANISM  mouse [GN:mmu], Escherichia coli [GN:eco], Aspergillus fumigatus
            [GN:afm]
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.8
            ExPASy - ENZYME nomenclature database: 2.6.1.8
            ExplorEnz - The Enzyme Database: 2.6.1.8
            ERGO genome analysis and discovery system: 2.6.1.8
            BRENDA, the Enzyme Database: 2.6.1.8
            CAS: 9030-39-1
///
ENTRY       EC 2.6.1.9                  Enzyme
NAME        histidinol-phosphate transaminase;
            imidazolylacetolphosphate transaminase;
            glutamic-imidazoleacetol phosphate transaminase;
            histidinol phosphate aminotransferase;
            imidazoleacetol phosphate transaminase;
            L-histidinol phosphate aminotransferase;
            histidine:imidazoleacetol phosphate transaminase;
            IAP transaminase;
            imidazolylacetolphosphate aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-histidinol-phosphate:2-oxoglutarate aminotransferase
REACTION    L-histidinol phosphate + 2-oxoglutarate =
            3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate [RN:R03243]
ALL_REAC    R03243;
            (other) R00694 R00734
SUBSTRATE   L-histidinol phosphate [CPD:C01100];
            2-oxoglutarate [CPD:C00026]
PRODUCT     3-(imidazol-4-yl)-2-oxopropyl phosphate [CPD:C01267];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:13319331]
  AUTHORS   AMES BN, HORECKER BL.
  TITLE     The biosynthesis of histidine:  imidazoleacetol phosphate
            transaminase.
  JOURNAL   J. Biol. Chem. 220 (1956) 113-28.
  ORGANISM  Neurospora crassa [GN:dncr], Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Martin, R.G. and Goldberger, R.F.
  TITLE     Imidazolylacetolphosphate:L-glutamate aminotransferase. Purification
            and properties.
  JOURNAL   J. Biol. Chem. 242 (1963) 1168-1174.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00340  Histidine metabolism
            PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
            PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
            PATH: map00401  Novobiocin biosynthesis
ORTHOLOGY   KO: K00817  histidinol-phosphate aminotransferase
GENES       OSA: 4330482
            CME: CMT439C
            SCE: YIL116W(HIS5)
            AGO: AGOS_ADL249W
            PIC: PICST_44612(HIS5)
            CGR: CAGL0C01243g
            SPO: SPBC11B10.02c(his3)
            ANI: AN0717.2
            AFM: AFUA_1G14090
            AOR: AO090012000450
            CNE: CNB03030
            UMA: UM04429.1
            ECO: b2021(hisC)
            ECJ: JW2003(hisC)
            ECE: Z3183(hisC)
            ECS: ECs2822
            ECC: c2548(hisC)
            ECI: UTI89_C2294(hisC)
            ECP: ECP_2064
            ECV: APECO1_1118(hisC)
            ECW: EcE24377A_2312(hisC)
            ECX: EcHS_A2160(hisC)
            STY: STY2282(hisC)
            STT: t0800(hisC)
            SPT: SPA0798(hisC)
            SEC: SC2083(hisC)
            STM: STM2073(hisC)
            YPE: YPO1547(hisC)
            YPK: y2622(hisC)
            YPM: YP_1436(hisC)
            YPA: YPA_0843
            YPN: YPN_2432
            YPS: YPTB1560(hisC)
            YPI: YpsIP31758_2430(hisC)
            SFL: SF2083(hisC)
            SFX: S2204(hisC)
            SFV: SFV_2081(hisC)
            SSN: SSON_2092(hisC)
            SBO: SBO_0847(hisC)
            SDY: SDY_2220(hisC)
            ECA: ECA2250 ECA2584(hisC)
            PLU: plu1569(hisD)
            BUC: BU101(hisC)
            BAS: BUsg094(hisC)
            BAB: bbp095(hisC)
            BCC: BCc_065(hisC)
            SGL: SG1128
            BFL: Bfl464(hisC)
            BPN: BPEN_479(hisC)
            HIN: HI1166(hisH)
            HIT: NTHI0601(hisC) NTHI1334
            HIP: CGSHiEE_00640
            HIQ: CGSHiGG_05595
            HSO: HS_0612(hisC)
            PMU: PM0838(hisH_1) PM1199(hisC)
            MSU: MS1574(hisC) MS1891(hisC)
            APL: APL_0700(hisC) APL_2021(hisC)
            XFA: XF2218
            XFT: PD1266(hisC)
            XCC: XCC1569(hisC) XCC1810(hisC) XCC3061 XCC3275(hisC)
            XCB: XC_0889 XC_1097 XC_2379 XC_2665
            XCV: XCV1667(hisC) XCV1876(hisC2) XCV3538(hisC3)
            XAC: XAC1626(hisC) XAC1830(hisC) XAC3423(hisC)
            XOO: XOO2257(hisC)
            XOM: XOO_1122(XOO1122) XOO_2120(XOO2120)
            VCH: VC1134
            VCO: VC0395_A0704(hisC)
            VVU: VV1_2918
            VVY: VV1352
            VPA: VP1139
            VFI: VF1014
            PPR: PBPRA1090 PBPRB1129(hisC)
            PAE: PA2531 PA3165(hisC2) PA4447(hisC1)
            PAU: PA14_23290(hisC2) PA14_31820(hisC) PA14_57770(hisC1)
            PAP: PSPA7_1964(hisC2) PSPA7_5019(hisC1)
            PPU: PP_0967(hisC)
            PST: PSPTO_4437(hisC)
            PSB: Psyr_4132
            PSP: PSPPH_4136(hisC)
            PFL: PFL_0930(hisC) PFL_4311(hisC)
            PFO: Pfl_0872 Pfl_4075
            PEN: PSEEN1108(hisC)
            PAR: Psyc_1185(hisC) Psyc_1901
            PCR: Pcryo_1205 Pcryo_2191
            ACI: ACIAD0664(hisC)
            SON: SO_2072(hisC)
            SDN: Sden_1616
            SFR: Sfri_1718
            SHE: Shewmr4_1798
            SHM: Shewmr7_2179
            SHN: Shewana3_1852
            ILO: IL1358 IL1836(hisC)
            CPS: CPS_3891(hisC)
            PHA: PSHAb0492(hisC)
            PAT: Patl_2882
            SDE: Sde_1012
            MAQ: Maqu_2700
            LPN: lpg1198(hisC) lpg1998(hisC2)
            LPF: lpl1206(hisC) lpl1974(hisC)
            LPP: lpp1200(hisC) lpp1979(hisC)
            MCA: MCA1113(hisC-1) MCA1417(hisC-2)
            TCX: Tcr_0591 Tcr_1194
            NOC: Noc_0175 Noc_2777
            AEH: Mlg_0927 Mlg_2214
            HCH: HCH_05304(hisC)
            CSA: Csal_0507 Csal_3157
            ABO: ABO_0563(hisC-1) ABO_1748(hisC-2)
            AHA: AHA_2194(hisC)
            BCI: BCI_0403(hisC)
            VOK: COSY_0853(hisC)
            NME: NMB1582
            NMA: NMA1771(hisC)
            NMC: NMC1502(hisC)
            NGO: NGO1241
            CVI: CV_0038 CV_0613(hisC)
            RSO: RSc0905(hisC2) RSc2951(hisC1)
            REU: Reut_A2574 Reut_A3110
            REH: H16_A0793(hisC1) H16_A3415(hisC2)
            RME: Rmet_0717 Rmet_3247
            BMA: BMA2713(hisC-1) BMA3123(hisC-2)
            BMV: BMASAVP1_A0091(hisC-2) BMASAVP1_A3240(hisC-1)
            BML: BMA10299_A1499(hisC-2) BMA10299_A1789(hisC-1)
            BMN: BMA10247_2764(hisC-1) BMA10247_2927(hisC-2)
            BXE: Bxe_A0399 Bxe_A0978 Bxe_A4136
            BUR: Bcep18194_A3524 Bcep18194_A6135 Bcep18194_C7445
            BCN: Bcen_2191 Bcen_2681
            BCH: Bcen2424_0426 Bcen2424_2805
            BAM: Bamb_0344 Bamb_2865
            BPS: BPSL0518 BPSL1724 BPSL3138(hisC)
            BPM: BURPS1710b_0750(hisC) BURPS1710b_2149(hisC)
                 BURPS1710b_3692(hisC)
            BPL: BURPS1106A_0582(hisC) BURPS1106A_3723(hisC)
            BPD: BURPS668_0566(hisC) BURPS668_3665(hisC)
            BTE: BTH_I0471(hisC-1) BTH_I2992(hisC-2)
            BPE: BP2194(his1) BP3769(hisC)
            BPA: BPP2850(his1) BPP4268(hisC)
            BBR: BB3171(hisC) BB4855(hisC)
            RFR: Rfer_1408 Rfer_2615 Rfer_2947
            POL: Bpro_0805 Bpro_1696 Bpro_2761
            MPT: Mpe_A0832 Mpe_B0517(hisC)
            HAR: HEAR1698(hisC) HEAR2578
            MMS: mma_1951(hisC1) mma_2672(hisC2)
            NEU: NE0336(hisC2) NE0647(hisC1)
            NET: Neut_1569 Neut_1905
            NMU: Nmul_A0818 Nmul_A2193
            EBA: ebA1297(hisC)
            AZO: azo1069(hisC1) azo3348(hisC2)
            DAR: Daro_1233 Daro_3383
            TBD: Tbd_0952 Tbd_1712
            MFA: Mfla_0249 Mfla_1684
            HHE: HH0612(hisC)
            WSU: WS2000(hisC)
            TDN: Tmden_0471
            CJE: Cj0317(hisC) Cj1437c
            CJR: CJE0362(hisC)
            CJJ: CJJ81176_0339(hisC)
            CJU: C8J_0294(hisC)
            CJD: JJD26997_1646(hisC)
            CFF: CFF8240_0268(hisC)
            CCV: CCV52592_1667(hisC)
            CHA: CHAB381_1298(hisC)
            CCO: CCC13826_0511 CCC13826_1590(hisC)
            ABU: Abu_2138(hisC)
            NIS: NIS_0390(hisC)
            SUN: SUN_2056(hisC)
            GSU: GSU3099(hisC)
            GME: Gmet_0385
            PCA: Pcar_0321 Pcar_0484(cobD)
            DVU: DVU1029(hisC)
            DDE: Dde_1453
            BBA: Bd1061(hisC)
            DPS: DP0642 DP1950(cobD)
            ADE: Adeh_4103
            MXA: MXAN_4038(hisC) MXAN_4228(hisC)
            SAT: SYN_01164 SYN_01517
            SFU: Sfum_2116
            PUB: SAR11_0216(hisC)
            MLO: mll3536 mll7105 mll7737 mlr5786
            MES: Meso_0933 Meso_3084
            SME: SMa0387(hisC3) SMc00710(hisC1) SMc02393 SMc03885(hisC2)
            ATU: Atu1011(hisC) Atu3612(hisC)
            ATC: AGR_C_1866 AGR_L_2426
            RET: RHE_CH01331(hisCch1) RHE_CH03810(hisCch2)
                 RHE_CH04010(hisCch3) RHE_PD00233(hisCd)
            RLE: RL1482(hisC) RL4338(hisC) RL4629(hisC)
            BME: BMEI0080 BMEI1308 BMEI1309
            BMF: BAB1_0657 BAB1_1988(hisC)
            BMS: BR0635 BR1987(hisC)
            BMB: BruAb1_0653 BruAb1_1963(hisC)
            BOV: BOV_1912(hisC)
            BJA: bll1397(hisC) blr6225(hisC)
            BRA: BRADO0818(hisC) BRADO4744 BRADO6463(hisC)
            BBT: BBta_1183(hisC) BBta_3457 BBta_7238(hisC)
            RPA: RPA4439(hisC)
            RPB: RPB_4254
            RPC: RPC_4283
            RPD: RPD_4101
            RPE: RPE_4342
            NWI: Nwi_0583
            NHA: Nham_0674
            CCR: CC_1071 CC_2223 CC_2534
            SIL: SPO1468 SPO3027 SPO3177(hisC)
            SIT: TM1040_1981 TM1040_2101
            RSP: RSP_1984 RSP_2284
            JAN: Jann_1034
            RDE: RD1_1752 RD1_3388(hisC)
            MMR: Mmar10_2379
            HNE: HNE_1125(hisC)
            ZMO: ZMO0002(hisC) ZMO0421(hisC) ZMO0560(hisC) ZMO0562(hisC)
            NAR: Saro_0695
            SAL: Sala_2887
            ELI: ELI_11415
            GOX: GOX1171 GOX1700 GOX2256
            GBE: GbCGDNIH1_0140
            RRU: Rru_A3264
            MAG: amb3974
            MGM: Mmc1_3594
            ABA: Acid345_3031 Acid345_3684 Acid345_3864
            SUS: Acid_4459
            BSU: BG10292(hisC)
            BHA: BH1665(hisC)
            BAN: BA1539(hisC-1) BA2955(hisC-2)
            BAR: GBAA1539(hisC-1) GBAA2955(hisC-2)
            BAA: BA_2059 BA_3464
            BAT: BAS1428 BAS2746
            BCE: BC1518 BC2940
            BCA: BCE_1645(hisC) BCE_2996(hisC)
            BCZ: BCZK1400(hisC) BCZK2675(hisC)
            BTK: BT9727_1400(hisC) BT9727_2696(hisC)
            BLI: BL02769(hisC)
            BLD: BLi02397(hisC)
            BCL: ABC1901(hisC)
            BAY: RBAM_020780(hisC)
            BPU: BPUM_1993(hisC)
            OIH: OB0545 OB1782(hisC)
            GKA: GK2198(hisC)
            SAU: SA0679 SA2469
            SAV: SAV0724 SAV2677
            SAM: MW0686 MW2596
            SAR: SAR0777 SAR2759
            SAS: SAS0689 SAS2562
            SAC: SACOL0784(hisC) SACOL2701
            SAB: SAB0673
            SAA: SAUSA300_0708(hisC) SAUSA300_2610(hisC)
            SAO: SAOUHSC_00733 SAOUHSC_03012
            SEP: SE0504
            SER: SERP0387(hisC)
            SHA: SH2169
            SSP: SSP0428 SSP1995
            LMO: lmo1925(hisC)
            LMF: LMOf2365_1177 LMOf2365_1954(hisC)
            LIN: lin2039(hisC)
            LWE: lwe1127(cobD) lwe1951(hisC)
            LLA: L0065(hisC)
            LLC: LACR_1336
            LLM: llmg_1298(hisC)
            SMU: SMU.1273(hisC)
            SSA: SSA_0510 SSA_1449(hisC)
            SGO: SGO_1411(hisC)
            LPL: lp_2551(hisC)
            LCA: LSEI_1426 LSEI_1436
            STH: STH2831(hisC)
            CAC: CAC1369(hisC) CAC3031(hisC)
            CPE: CPE1040 CPE1373(hisC)
            CPF: CPF_1295 CPF_1623
            CPR: CPR_1365
            CTC: CTC00722(cobD)
            CNO: NT01CX_1063(hisC)
            CDF: CD1549(hisC)
            CBO: CBO1571(hisC)
            CBA: CLB_1591(hisC)
            CBH: CLC_1602(hisC)
            CBF: CLI_1653(hisC)
            CKL: CKL_1296(hisC)
            CHY: CHY_1086(hisC1) CHY_1929(hisC2)
            DSY: DSY3912 DSY4057
            SWO: Swol_1198
            TTE: TTE0380(hisC) TTE2137(hisC2)
            MTA: Moth_0515
            MTU: Rv1600(hisC1) Rv2231c(cobC) Rv2589(gabT) Rv3772(hisC2)
            MTC: MT1636(hisC-1) MT2290(hisC-2) MT3881(hisC-3)
            MBO: Mb1626(hisC1) Mb2256c(cobC) Mb2620(gabT) Mb3800(hisC2)
            MBB: BCG_1638(hisC1) BCG_2612(gabT) BCG_3833(hisC2)
            MLE: ML1258(hisC)
            MPA: MAP0252c(hisC2) MAP1294(hisC) MAP1983c(cobC)
            MAV: MAV_0250(hisC) MAV_3186(hisC)
            MSM: MSMEG_1491 MSMEG_3206(hisC) MSMEG_6351(hisC)
            MMC: Mmcs_2935 Mmcs_3062 Mmcs_3345 Mmcs_4982
            CGL: NCgl0215(cgl0218) NCgl2020(cgl2101)
            CGB: cg0267(pat) cg2304(hisC)
            CEF: CE0193 CE2002(hisC) CE2136
            CDI: DIP0178 DIP1565(hisC) DIP1681
            CJK: jk0787(hisC) jk2030(pat)
            NFA: nfa16320 nfa18460(hisC) nfa2290(hisC2)
            RHA: RHA1_ro01030(hisC1) RHA1_ro01184 RHA1_ro01256(hisC2)
                 RHA1_ro04128(hisC3)
            SCO: SCO1859(SCI39.06) SCO2053(hisC1) SCO3944(hisC2)
            SMA: SAV1375(hisC3) SAV4261(hisC2) SAV6154(hisC1) SAV6404(cobC)
            LXX: Lxx15860(hisC1) Lxx25080(hisC2)
            CMI: CMM_1509(hisC1)
            AAU: AAur_1604(hisC)
            PAC: PPA0034 PPA1153
            TFU: Tfu_1151 Tfu_2223 Tfu_3018
            FRA: Francci3_1862 Francci3_3026
            FAL: FRAAL5003(hisC)
            ACE: Acel_0035
            SEN: SACE_0217(hisC2) SACE_1581(cobC) SACE_4645(hisC2)
                 SACE_5777(hisC-1)
            BLO: BL1296(hisC)
            BAD: BAD_1128(hisC)
            RXY: Rxyl_0726
            FNU: FN0973
            RBA: RB7661(hisC)
            TDE: TDE2687
            LIL: LA1182(hisC)
            LIC: LIC12508(hisC) LIC20121(cbiP)
            LBJ: LBJ_2219(hisC) LBJ_4191(cobQ)
            LBL: LBL_2212(hisC) LBL_4206(cobQ)
            SYN: sll1958(hisC)
            SYW: SYNW2318(hisC) SYNW2334(hisC)
            SYC: syc0516_c(hisC)
            SYF: Synpcc7942_1030
            SYD: Syncc9605_2450 Syncc9605_2464
            SYE: Syncc9902_2133
            SYG: sync_2666(hisC)
            SYR: SynRCC307_2242(hisC)
            SYX: SynWH7803_2331(hisC)
            CYA: CYA_1885(hisC)
            CYB: CYB_0260(hisC)
            TEL: tlr0281
            GVI: gll1323(hisC) gll2475(hisC)
            ANA: all4966(hisC) alr2092(hisC)
            AVA: Ava_2242 Ava_4334
            PMA: Pro0211(hisC) Pro0224(hisC)
            PMM: PMM0186(hisC) PMM0198(hisC)
            PMT: PMT2069(hisC) PMT2100(hisC)
            PMN: PMN2A_1553 PMN2A_1565
            PMI: PMT9312_0188 PMT9312_0200
            PMB: A9601_02041 A9601_02161
            PMC: P9515_02151 P9515_02271
            PMF: P9303_27461 P9303_27901
            PMG: P9301_02061 P9301_02181
            PMH: P9215_02041(hisC)
            PME: NATL1_02611 NATL1_02741
            TER: Tery_4690
            BTH: BT_0202
            BFR: BF2490(cobC) BF3188
            BFS: BF2523 BF3028
            PGI: PG0012 PG1160
            SRU: SRU_2128(hisC)
            CHU: CHU_1269(hisC)
            GFO: GFO_1762(hisC)
            FPS: FP0958(hisC)
            CTE: CT0939 CT1256(hisC)
            CCH: Cag_1086
            PLT: Plut_1206
            DET: DET0655 DET0689 DET0843(hisC)
            DEH: cbdb_A639(cobD) cbdb_A825(hisC)
            DRA: DR_2461 DR_B0011
            DGE: Dgeo_0118 Dgeo_2875
            TTH: TTC0060 TT_P0022
            TTJ: TTHA0428 TTHB065
            AAE: aq_2084(hisC)
            TMA: TM1040
            MMP: MMP1216(hisC)
            MAC: MA0118(hisC) MA0942(hisC)
            MBA: Mbar_A0872 Mbar_A3453
            MMA: MM_1405 MM_2060
            MBU: Mbur_2087 Mbur_2203
            MHU: Mhun_2525
            MST: Msp_1326(hisC)
            MSI: Msm_0653
            MKA: MK1426(hisC)
            AFU: AF2002(hisC-1) AF2024(hisC-2)
            HAL: VNG1033G(hisC1) VNG1582G(hisC2)
            HMA: rrnAC0529(hisC2) rrnAC1934(hisC1)
            HWA: HQ3364A(hisC)
            NPH: NP2140A(hisC) NP5302A(cobD)
            TAC: Ta0021m
            TVO: TVN0078
            PTO: PTO0813 PTO1297
            PHO: PH0377
            PAB: PAB0026(hisC)
            PFU: PF0293 PF1665
            TKO: TK0250 TK0864
            RCI: RCIX2460(hisC)
            APE: APE_2035.1
            HBU: Hbut_0488
            SSO: SSO0448(hisC-like) SSO0592(hisC)
            STO: ST0165 ST1458
            SAI: Saci_0454 Saci_1574(hisC)
            PAI: PAE0377 PAE0918(hisC) PAE0958(hisC)
STRUCTURES  PDB: 1FG3  1FG7  1GEW  1GEX  1GEY  1H1C  1IJI  1UU0  1UU1  1UU2  
                 2F8J  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.9
            ExPASy - ENZYME nomenclature database: 2.6.1.9
            ExplorEnz - The Enzyme Database: 2.6.1.9
            ERGO genome analysis and discovery system: 2.6.1.9
            BRENDA, the Enzyme Database: 2.6.1.9
            CAS: 9032-98-8
///
ENTRY       EC 2.6.1.10       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
COMMENT     Deleted entry: D-aspartate transaminase. Now included with EC
            2.6.1.21, D-amino-acid transaminase (EC 2.6.1.10 created 1961,
            deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.10
            ExPASy - ENZYME nomenclature database: 2.6.1.10
            ExplorEnz - The Enzyme Database: 2.6.1.10
            ERGO genome analysis and discovery system: 2.6.1.10
            BRENDA, the Enzyme Database: 2.6.1.10
///
ENTRY       EC 2.6.1.11                 Enzyme
NAME        acetylornithine transaminase;
            acetylornithine delta-transaminase;
            ACOAT;
            acetylornithine 5-aminotransferase;
            acetylornithine aminotransferase;
            N-acetylornithine aminotransferase;
            N-acetylornithine-delta-transaminase;
            N2-acetylornithine 5-transaminase;
            N2-acetyl-L-ornithine:2-oxoglutarate aminotransferase;
            succinylornithine aminotransferase;
            2-N-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase
REACTION    N2-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate
            5-semialdehyde + L-glutamate [RN:R02283]
ALL_REAC    R02283
SUBSTRATE   N2-acetyl-L-ornithine [CPD:C00437];
            2-oxoglutarate [CPD:C00026]
PRODUCT     N-acetyl-L-glutamate 5-semialdehyde [CPD:C01250];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also acts on L-ornithine and
            N2-succinyl-L-ornithine.
REFERENCE   1  [PMID:14213368]
  AUTHORS   ALBRECHT AM, VOGEL HJ.
  TITLE     ACETYLORNITHINE DELTA-TRANSAMINASE. PARTIAL PURIFICATION AND
            REPRESSION BEHAVIOR.
  JOURNAL   J. Biol. Chem. 239 (1964) 1872-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:16589307]
  AUTHORS   Vogel HJ.
  TITLE     Path of Ornithine Synthesis in Escherichia Coli.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 39 (1953) 578-83.
REFERENCE   3  [PMID:238949]
  AUTHORS   Voellmy R, Leisinger T.
  TITLE     Dual role for N-2-acetylornithine 5-aminotransferase from
            Pseudomonas aeruginosa in arginine biosynthesis and arginine
            catabolism.
  JOURNAL   J. Bacteriol. 122 (1975) 799-809.
  ORGANISM  Pseudomonas aeruginosa
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K00818  acetylornithine aminotransferase
GENES       OSA: 4337697
            CME: CMQ064C
            SCE: YOL140W(ARG8)
            AGO: AGOS_ADL191W
            PIC: PICST_52948(ARG8)
            CGR: CAGL0B01507g
            SPO: SPCC777.09k
            ANI: AN1150.2
            AFM: AFUA_2G12470 AFUA_8G02150
            AOR: AO090026000394
            CNE: CNA06020
            DDI: DDB_0231481(argD)
            TET: TTHERM_00787240
            ECO: b3359(argD)
            ECJ: JW3322(argD)
            ECE: Z4720(argD)
            ECS: ECs4210
            ECC: c4134(argD)
            ECI: UTI89_C3862(argD)
            ECP: ECP_3450
            ECV: APECO1_3096(argD)
            ECW: EcE24377A_3829(argD)
            ECX: EcHS_A3556
            STY: STY4328(argD)
            STT: t4037(argD)
            SPT: SPA3334(argD)
            SEC: SC3402(argD)
            STM: STM3468(argD)
            YPK: y3954(argD)
            YPM: YP_0172(argD)
            YPA: YPA_3299
            YPN: YPN_3894
            YPS: YPTB3731
            YPI: YpsIP31758_3947(argD)
            SFL: SF3378(argD)
            SFX: S4385(argD)
            SFV: SFV_3365(argD)
            SSN: SSON_3490(argD)
            SBO: SBO_3341(argD)
            SDY: SDY_3521(argD)
            ECA: ECA4065(argD)
            PLU: plu0394(argD)
            BUC: BU534(argD)
            BAS: BUsg515(argD)
            HDU: HD0892(argD)
            PMU: PM0344(argD)
            MSU: MS0782(argD)
            APL: APL_0244(argD)
            XFA: XF1427
            XFT: PD0654(argD)
            XCC: XCC3282(argD)
            XCB: XC_0882
            XCV: XCV2698 XCV3544(argD)
            XAC: XAC3429(argD)
            XOO: XOO1219(argD)
            XOM: XOO_1115(XOO1115)
            VCH: VC2618
            VVU: VV1_1313
            VVY: VV3054
            VPA: VP2797
            VFI: VF2284
            PPR: PBPRA0289
            PAE: PA0530
            PAU: PA14_06920(argD)
            PPU: PP_0372 PP_4481(argD)
            PST: PSPTO_1832(argD-1) PSPTO_2618(argD-2)
            PSB: Psyr_2358 Psyr_3565
            PSP: PSPPH_2492(argD1) PSPPH_2707 PSPPH_4313(argD)
            PFL: PFL_2461 PFL_4515(argD) PFL_5681
            PFO: Pfl_4285 Pfl_4636 Pfl_5164
            PEN: PSEEN3882(aruC) PSEEN5110
            PAR: Psyc_1057(argD)
            PCR: Pcryo_1405
            ACI: ACIAD1231(argD)
            SON: SO_0617(argD)
            SDN: Sden_1054 Sden_3193
            SFR: Sfri_3299
            SHE: Shewmr4_0611
            SHM: Shewmr7_3419
            SHN: Shewana3_0610
            ILO: IL2318(argD)
            PHA: PSHAa0194(argD)
            PAT: Patl_0163 Patl_0651
            SDE: Sde_2440
            MAQ: Maqu_2210
            LPN: lpg2968(argD)
            LPF: lpl2898(argD)
            LPP: lpp3040(argD)
            MCA: MCA2079(argD)
            TCX: Tcr_0533
            NOC: Noc_2429
            AEH: Mlg_0491 Mlg_1102
            HCH: HCH_01763(argD) HCH_01947(aruC)
            CSA: Csal_2808
            ABO: ABO_0719(argD)
            AHA: AHA_1939 AHA_3180
            VOK: COSY_0419(argD)
            NME: NMB1371(argD)
            NMA: NMA1584(argD)
            NMC: NMC1306(argD)
            NGO: NGO0646
            CVI: CV_1496(aruC) CV_2256(argD)
            RSO: RSc2435(argM)
            REU: Reut_A2723
            REH: H16_A3025(argD)
            RME: Rmet_2862
            BMA: BMA1967(argD)
            BMV: BMASAVP1_A0946(argD)
            BML: BMA10299_A0879(argD)
            BMN: BMA10247_0269(argD)
            BXE: Bxe_A2923
            BUR: Bcep18194_A4291(argD) Bcep18194_A5823(argD) Bcep18194_B1957
                 Bcep18194_C7547
            BCH: Bcen2424_2491 Bcen2424_4086
            BAM: Bamb_2538
            BPS: BPSL0926
            BPM: BURPS1710b_1150(argD)
            BTE: BTH_I0791
            BPE: BP0451(argM) BP3539(argD)
            BPA: BPP2543(argD) BPP4365(argM)
            BBR: BB1988(argD) BB4951(argM)
            RFR: Rfer_2121
            POL: Bpro_3572
            AAV: Aave_1164
            MPT: Mpe_A3029
            HAR: HEAR0754(argM)
            MMS: mma_0683
            NEU: NE1439(argD)
            NET: Neut_2067
            NMU: Nmul_A1041
            EBA: ebA5095(argD)
            AZO: azo1195(argM) azo2188(argD)
            DAR: Daro_1679 Daro_3033
            TBD: Tbd_1851
            MFA: Mfla_1710
            HHE: HH0969(argD)
            WSU: WS0302(argD)
            TDN: Tmden_1254
            CJE: Cj0227(argD)
            CJR: CJE0278(argD)
            CJJ: CJJ81176_0252(argD)
            CJU: C8J_0205(argD)
            CJD: JJD26997_0225(argD)
            CFF: CFF8240_0925
            CHA: CHAB381_0717
            ABU: Abu_0259(argD1) Abu_1468(argD2)
            GSU: GSU0151(argD)
            GME: Gmet_0204
            PCA: Pcar_2414
            PPD: Ppro_0566
            DVU: DVU2347(argD)
            DDE: Dde_1426
            LIP: LI0087(argD)
            DPS: DP0438
            ADE: Adeh_2692
            MXA: MXAN_3014(argD)
            SAT: SYN_00570 SYN_02155
            SFU: Sfum_0063
            WOL: WD0559(argD) WD1283
            WBM: Wbm0129
            AMA: AM326(argD)
            APH: APH_0945(argD)
            ERU: Erum2110(argD)
            ERW: ERWE_CDS_02130(argD)
            ERG: ERGA_CDS_02080(argD)
            ECN: Ecaj_0214
            ECH: ECH_0886(argD)
            NSE: NSE_0850(argD)
            MLO: mlr5646
            MES: Meso_0009
            SME: SMc02138(argD)
            SMD: Smed_0127
            ATU: Atu0428(argD)
            ATC: AGR_C_752
            RET: RHE_CH00516(argD1)
            RLE: RL0549
            BME: BMEI1621
            BMF: BAB1_0331
            BMS: BR0301
            BMB: BruAb1_0327(argD)
            BJA: blr1098(argD) blr4582(argD)
            BRA: BRADO3787(argM) BRADO6779(argD)
            BBT: BBta_0759(argD) BBta_4143(argM)
            RPA: RPA3732(argD1) RPA4773(argD2)
            RPB: RPB_0783
            RPC: RPC_4916
            RPD: RPD_0895 RPD_2300
            RPE: RPE_4884
            NWI: Nwi_0513(argD)
            NHA: Nham_0642
            BHE: BH01090(argD)
            BQU: BQ01010(argD)
            BBK: BARBAKC583_1290(argD)
            CCR: CC_2243
            SIL: SPO0962(argD)
            SIT: TM1040_0665
            RSP: RSP_2008(argD)
            JAN: Jann_1024
            RDE: RD1_1676(argD)
            MMR: Mmar10_0487
            HNE: HNE_0580(argD)
            ZMO: ZMO0408(argD)
            NAR: Saro_3141
            SAL: Sala_1359
            ELI: ELI_13915
            GOX: GOX1237
            GBE: GbCGDNIH1_2274
            RRU: Rru_A0176 Rru_A1147 Rru_A3277
            MAG: amb0316 amb0812
            MGM: Mmc1_3744
            ABA: Acid345_0626
            BSU: BG10194(argD)
            BHA: BH2897(argD)
            BAN: BA3029 BA4352(argD)
            BAR: GBAA3029 GBAA4352(argD)
            BAA: BA_3538 BA_4809
            BAT: BAS2815 BAS4037
            BCE: BC3007 BC4127(argD)
            BCA: BCE_3057(argD)
            BCZ: BCZK2746(argD) BCZK3884(argD)
            BTK: BT9727_2763(argD) BT9727_3876(argD)
            BTL: BALH_2709(argD) BALH_3744(argD)
            BLI: BL03244(argD)
            BLD: BLi01209(argD)
            BCL: ABC2432 ABC2555(argD)
            BAY: RBAM_011220
            BPU: BPUM_1045
            OIH: OB1078(argD)
            GKA: GK0793(argD)
            SAU: SA0179 SA0818(rocD)
            SAV: SAV0185 SAV0957(rocD)
            SAM: MW0159 MW0839(rocD)
            SAR: SAR0186 SAR0919(rocD)
            SAS: SAS0160 SAS0827(rocD)
            SAC: SACOL0170(rocD1) SACOL0960(rocD)
            SAB: SAB0125c SAB0824(rocD)
            SAA: SAUSA300_0187(rocD) SAUSA300_0860(rocD)
            SAO: SAOUHSC_00150 SAOUHSC_00894
            SEP: SE0653 SE1209
            SER: SERP0545(rocD) SERP1089(argD)
            SHA: SH1993(rocD)
            SSP: SSP0220 SSP1818
            LMO: lmo1588(argD)
            LMF: LMOf2365_1610(argD)
            LIN: lin1630(argD)
            LWE: lwe1601(argD)
            LLA: L0106(argD)
            LLC: LACR_0858
            LLM: llmg_1756(argD)
            SMU: SMU.666(argD)
            STC: str0467(argD)
            STL: stu0467(argD)
            SSA: SSA_0760
            SGO: SGO_1566(argD)
            LPL: lp_0531(argD)
            STH: STH2881
            CAC: CAC2388(argD)
            CNO: NT01CX_2381(argD)
            CKL: CKL_1556(argD)
            CHY: CHY_2262(argD)
            DSY: DSY0763
            SWO: Swol_2288
            TTE: TTE2495(argD2)
            MTA: Moth_2287
            MTU: Rv1655(argD)
            MTC: MT1693(argD)
            MBO: Mb1683(argD)
            MBB: BCG_1694(argD)
            MLE: ML1409(argD)
            MPA: MAP1364(argD)
            MAV: MAV_3115(argD)
            MSM: MSMEG_3773(argD)
            MMC: Mmcs_2969
            CGL: NCgl1343(argD) NCgl2355(cgl2441)
            CGB: cg1583(argD)
            CEF: CE1529(argD)
            CDI: DIP1170(argD)
            CJK: jk0844(argD)
            NFA: nfa19390(argD)
            RHA: RHA1_ro00953(argD) RHA1_ro03546 RHA1_ro05386 RHA1_ro10420
            SCO: SCO1577(argD)
            SMA: SAV6766(argD)
            LXX: Lxx06060(argD)
            CMI: CMM_1998(argD)
            AAU: AAur_1634(argD)
            PAC: PPA1347
            TFU: Tfu_2054
            FRA: Francci3_3172
            FAL: FRAAL5205(argD)
            SEN: SACE_4673 SACE_5259(argD) SACE_5670
            BLO: BL1061(argD)
            BAD: BAD_0922(argD)
            RXY: Rxyl_2888
            RBA: RB5984 RB8633(argD)
            LIL: LA2153(argD)
            LIC: LIC11767(argD)
            LBJ: LBJ_1862(argD)
            LBL: LBL_1422(argD)
            SYN: slr1022(argD)
            SYW: SYNW1634(argD)
            SYC: syc0599_c(argD)
            SYF: Synpcc7942_0943
            SYD: Syncc9605_0858
            SYE: Syncc9902_1534
            SYG: sync_0744
            SYR: SynRCC307_0611(argD)
            SYX: SynWH7803_1747(argD)
            CYA: CYA_1537(argD)
            CYB: CYB_1419(argD)
            TEL: tlr1328(argD)
            GVI: glr0547(argD)
            ANA: alr1080(argD)
            AVA: Ava_3730
            PMA: Pro1375(argD)
            PMM: PMM1301(argD)
            PMT: PMT0331(argD)
            PMN: PMN2A_0867
            PMI: PMT9312_1397
            PMB: A9601_15001(argD)
            PMC: P9515_14621(argD)
            PMF: P9303_19841(argD)
            PMG: P9301_14871(argD)
            PME: NATL1_17211(argD)
            TER: Tery_2649
            BTH: BT_3758
            BFR: BF0531
            BFS: BF0479(argD)
            SRU: SRU_2217
            CHU: CHU_1633(argD) CHU_3083(astC)
            GFO: GFO_0771(argD) GFO_2104(argD)
            FPS: FP1771(argD)
            CTE: CT0367(argD)
            CCH: Cag_0503
            PLT: Plut_1583
            DET: DET1258(argD)
            DEH: cbdb_A1181(argD)
            DRA: DR_0794
            DGE: Dgeo_1416
            TTH: TTC1393
            TTJ: TTHA1755
            AAE: aq_023(argD)
            TMA: TM1785(argD)
            TPT: Tpet_1072
            MJA: MJ0721(argD)
            MMP: MMP1101
            MAC: MA0119(argD)
            MBA: Mbar_A0871
            MMA: MM_1406
            MBU: Mbur_2204
            MHU: Mhun_2526
            MTH: MTH1337
            MST: Msp_0037(argD)
            MSI: Msm_1368
            MKA: MK1606(argD)
            AFU: AF0080(argD-1) AF1815(argD-2)
            HMA: rrnAC2675(argD)
            HWA: HQ3717A(argD)
            NPH: NP5264A(argD)
            PTO: PTO1470
            PHO: PH1716
            PAB: PAB2440(argD)
            PFU: PF1685
            TKO: TK0275
            RCI: RCIX1575(argD)
            APE: APE_1464
            HBU: Hbut_0873
            SSO: SSO0160(argD)
            STO: ST0191
            SAI: Saci_0755(argD)
            PAI: PAE2515(argD)
            TPE: Tpen_0539
STRUCTURES  PDB: 1VEF  1WKG  1WKH  2E54  2EH6  2ORD  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.11
            ExPASy - ENZYME nomenclature database: 2.6.1.11
            ExplorEnz - The Enzyme Database: 2.6.1.11
            ERGO genome analysis and discovery system: 2.6.1.11
            BRENDA, the Enzyme Database: 2.6.1.11
            CAS: 9030-40-4
///
ENTRY       EC 2.6.1.12                 Enzyme
NAME        alanine---oxo-acid transaminase;
            L-alanine-alpha-keto acid aminotransferase;
            leucine-alanine transaminase;
            alanine-keto acid aminotransferase;
            alanine-oxo acid aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-alanine:2-oxo-acid aminotransferase
REACTION    L-alanine + a 2-oxo acid = pyruvate + an L-amino acid [RN:R01261]
ALL_REAC    R01261 > R00400
SUBSTRATE   L-alanine [CPD:C00041];
            2-oxo acid [CPD:C00161]
PRODUCT     pyruvate [CPD:C00022];
            L-amino acid [CPD:C00151]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:13084587]
  AUTHORS   ALTENBERN RA, HOUSEWRIGHT RD.
  TITLE     Transaminases in smooth Brucella abortus, strain 19.
  JOURNAL   J. Biol. Chem. 204 (1953) 159-67.
  ORGANISM  Brucella abortus [GN:bmb]
REFERENCE   2
  AUTHORS   Rowsell, E.V.
  TITLE     Transaminations with pyruvate and other alpha-keto acids.
  JOURNAL   Biochem. J. 64 (1956) 246-252.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Sallach, H.J.
  TITLE     Formation of serine from hydroxypyruvate and L-alanine.
  JOURNAL   J. Biol. Chem. 223 (1956) 1101-1108.
  ORGANISM  dog [GN:cfa]
REFERENCE   4
  AUTHORS   Wilson, D.G., King, K.W. and Burris, R.H.
  TITLE     Transaminase reactions in plants.
  JOURNAL   J. Biol. Chem. 208 (1954) 863-874.
  ORGANISM  white lupine, Hordeum vulgare [GN:ehvu]
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.12
            ExPASy - ENZYME nomenclature database: 2.6.1.12
            ExplorEnz - The Enzyme Database: 2.6.1.12
            ERGO genome analysis and discovery system: 2.6.1.12
            BRENDA, the Enzyme Database: 2.6.1.12
            CAS: 9030-41-5
///
ENTRY       EC 2.6.1.13                 Enzyme
NAME        ornithine aminotransferase;
            ornithine delta-transaminase;
            L-ornithine:alpha-ketoglutarate delta-aminotransferase;
            OAT;
            L-ornithine 5-aminotransferase;
            L-ornithine aminotransferase;
            ornithine 5-aminotransferase;
            ornithine transaminase;
            ornithine-alpha-ketoglutarate aminotransferase;
            ornithine-2-oxoacid aminotransferase;
            ornithine-keto acid aminotransferase;
            ornithine-keto acid transaminase;
            ornithine-ketoglutarate aminotransferase;
            ornithine-oxo acid aminotransferase;
            ornithine:alpha-oxoglutarate transaminase;
            ornithine---oxo-acid transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-ornithine:2-oxo-acid aminotransferase
REACTION    L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino
            acid [RN:R01343]
ALL_REAC    R01343 > R00667
SUBSTRATE   L-ornithine [CPD:C00077];
            2-oxo acid [CPD:C00161]
PRODUCT     L-glutamate 5-semialdehyde [CPD:C01165];
            L-amino acid [CPD:C00151]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1
  AUTHORS   Fincham, J.R.S.
  TITLE     Ornithine transaminase in Neurospora and its relation to the
            biosynthesis of proline.
  JOURNAL   Biochem. J. 53 (1953) 313-320.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2
  AUTHORS   Katunuma, N., Matsuda, Y. and Tomino, I.
  TITLE     Studies on ornithine-ketoacid transaminase. I. Purification and
            properties.
  JOURNAL   J. Biochem. (Tokyo) 56 (1964) 499-503.
  ORGANISM  Neurospora crassa [GN:dncr], Escherichia coli [GN:eco], rat [GN:rno]
REFERENCE   3  [PMID:13143017]
  AUTHORS   MEISTER A.
  TITLE     Enzymatic transamination reactions involving arginine and ornithine.
  JOURNAL   J. Biol. Chem. 206 (1954) 587-96.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   4  [PMID:5783831]
  AUTHORS   Peraino C, Bunville LG, Tahmisian TN.
  TITLE     Chemical, physical, and morphological properties of ornithine
            Aminotransferase from rat liver.
  JOURNAL   J. Biol. Chem. 244 (1969) 2241-9.
  ORGANISM  rat [GN:rno]
REFERENCE   5
  AUTHORS   Quastel, J.H. and Witty, R.
  TITLE     Ornithine transaminase.
  JOURNAL   Nature 167 (1951) 556.
REFERENCE   6
  AUTHORS   Strecker, H.J.
  TITLE     Purification and properties of rat liver ornithine
            delta-transaminase.
  JOURNAL   J. Biol. Chem. 240 (1965) 1225-1230.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K00819  ornithine--oxo-acid transaminase
GENES       HSA: 4942(OAT)
            MMU: 18242(Oat)
            RNO: 64313(Oat)
            CFA: 477858(OAT)
            GGA: 426430(OAT)
            XLA: 379754(oat) 446525(oat)
            DME: Dmel_CG8782(Oat)
            CEL: C16A3.10
            OSA: 4333554
            CME: CML323C
            SCE: YLR438W(CAR2)
            AGO: AGOS_AER123W
            PIC: PICST_77538(CAR2)
            CGR: CAGL0M00880g
            SPO: SPAC27F1.05c SPBC21C3.08c
            ANI: AN1810.2
            AFM: AFUA_4G09140
            AOR: AO090023000628
            CNE: CNL04880
            UMA: UM03169.1
            DDI: DDB_0231478(oatA)
            PFA: PFF0435w
            TET: TTHERM_01049320
            ECW: EcE24377A_3540(rocD)
            ENT: Ent638_3528
            NOC: Noc_1711
            RSO: RSc0159(RS01029)
            BPE: BP0539(rocD)
            BPA: BPP0748(rocD)
            BBR: BB0834(rocD)
            MPT: Mpe_A2115
            HAR: HEAR0122(rocD)
            MMS: mma_0147(rocD)
            NEU: NE0142
            EBA: ebA3609(rocD)
            MXA: MXAN_7377(rocD)
            MLO: mll1261
            RET: RHE_CH03852(rocD)
            RLE: RL4385(rocD)
            BME: BMEII0441
            BMF: BAB2_0385
            BMS: BRA0851
            BMB: BruAb2_0380
            BJA: bll2855(rocD) blr3010
            BRA: BRADO2635
            BBT: BBta_2975
            NWI: Nwi_2516
            NHA: Nham_3111
            GBE: GbCGDNIH1_1948
            RRU: Rru_A3466
            ABA: Acid345_1822
            BSU: BG10722(rocD)
            BHA: BH3943(rocD)
            BAN: BA1154(rocD)
            BAR: GBAA1154(rocD)
            BAA: BA_1699
            BAT: BAS1071
            BCE: BC1149(rocD)
            BCA: BCE_1256(rocD)
            BCZ: BCZK1050(rocD)
            BTK: BT9727_1052(rocD)
            BTL: BALH_1015(rocD)
            BLI: BL01737(rocD)
            BLD: BLi00422(rocD)
            BCL: ABC0017(rocD)
            BAY: RBAM_037250(rocD)
            BPU: BPUM_3060(rocD)
            OIH: OB2287(rocD)
            GKA: GK0188(rocD)
            MTU: Rv2321c(rocD2) Rv2322c(rocD1)
            MBO: Mb2348c(rocD2) Mb2349c(rocD1)
            MBB: BCG_2342c(rocD2) BCG_2343c(rocD1)
            MPA: MAP2094c(rocD1)
            MAV: MAV_2086(rocD)
            MSM: MSMEG_1413(rocD)
            RHA: RHA1_ro06169(rocD)
            SCO: SCO1223(2SCG58.23) SCO1284(2SCG18.31c)
            SMA: SAV2285(rocD3) SAV3420(rocD1) SAV7112(rocD2)
            CMI: CMM_0630(rocD)
            TFU: Tfu_2247
            ACE: Acel_0454
            SEN: SACE_1875(rocD)
            AVA: Ava_B0165
            PGI: PG1271
            CHU: CHU_0647(hemL)
            GFO: GFO_1886(oat)
            FPS: FP0739(rocD)
            DRA: DR_1415
            DGE: Dgeo_1219
            TTH: TTC0553
            TTJ: TTHA0909
STRUCTURES  PDB: 1GBN  1OAT  1Z7D  2BYJ  2BYL  2CAN  2OAT  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.13
            ExPASy - ENZYME nomenclature database: 2.6.1.13
            ExplorEnz - The Enzyme Database: 2.6.1.13
            ERGO genome analysis and discovery system: 2.6.1.13
            BRENDA, the Enzyme Database: 2.6.1.13
            CAS: 9030-42-6
///
ENTRY       EC 2.6.1.14                 Enzyme
NAME        asparagine---oxo-acid transaminase;
            asparagine-keto acid aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-asparagine:2-oxo-acid aminotransferase
REACTION    L-asparagine + a 2-oxo acid = 2-oxosuccinamate + an amino acid
            [RN:R01345]
ALL_REAC    R01345 > R01346
SUBSTRATE   L-asparagine [CPD:C00152];
            2-oxo acid [CPD:C00161]
PRODUCT     2-oxosuccinamate [CPD:C02362];
            amino acid [CPD:C00045]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:13201567]
  AUTHORS   MEISTER A, FRASER PE.
  TITLE     Enzymatic formation of L-asparagine by transamination.
  JOURNAL   J. Biol. Chem. 210 (1954) 37-43.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
            PATH: map00253  Tetracycline biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.14
            ExPASy - ENZYME nomenclature database: 2.6.1.14
            ExplorEnz - The Enzyme Database: 2.6.1.14
            ERGO genome analysis and discovery system: 2.6.1.14
            BRENDA, the Enzyme Database: 2.6.1.14
            CAS: 9030-43-7
///
ENTRY       EC 2.6.1.15                 Enzyme
NAME        glutamine---pyruvate transaminase;
            glutaminase II;
            L-glutamine transaminase L;
            glutamine-oxo-acid transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-glutamine:pyruvate aminotransferase
REACTION    L-glutamine + pyruvate = 2-oxoglutaramate + L-alanine [RN:R00576]
ALL_REAC    R00576
SUBSTRATE   L-glutamine [CPD:C00064];
            pyruvate [CPD:C00022]
PRODUCT     2-oxoglutaramate [CPD:C00940];
            L-alanine [CPD:C00041]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. L-Methionine can act as donor;
            glyoxylate can act as acceptor.
REFERENCE   1  [PMID:5059882]
  AUTHORS   Cooper JL, Meister A.
  TITLE     Isolation and properties of highly purified glutamine transaminase.
  JOURNAL   Biochemistry. 11 (1972) 661-71.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:13201566]
  AUTHORS   MEISTER A.
  TITLE     Studies on the mechanism and specificity of the glutamine-alpha-keto
            acid transamination-deamidation reaction.
  JOURNAL   J. Biol. Chem. 210 (1954) 17-35.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00251  Glutamate metabolism
STRUCTURES  PDB: 1V2D  1V2E  1V2F  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.15
            ExPASy - ENZYME nomenclature database: 2.6.1.15
            ExplorEnz - The Enzyme Database: 2.6.1.15
            ERGO genome analysis and discovery system: 2.6.1.15
            BRENDA, the Enzyme Database: 2.6.1.15
            CAS: 9030-44-8
///
ENTRY       EC 2.6.1.16                 Enzyme
NAME        glutamine---fructose-6-phosphate transaminase (isomerizing);
            hexosephosphate aminotransferase;
            glucosamine-6-phosphate isomerase (glutamine-forming);
            glutamine-fructose-6-phosphate transaminase (isomerizing);
            D-fructose-6-phosphate amidotransferase;
            glucosaminephosphate isomerase;
            glucosamine 6-phosphate synthase;
            GlcN6P synthase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-glutamine:D-fructose-6-phosphate isomerase (deaminating)
REACTION    L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine
            6-phosphate [RN:R00768]
ALL_REAC    R00768
SUBSTRATE   L-glutamine [CPD:C00064];
            D-fructose 6-phosphate [CPD:C00085]
PRODUCT     L-glutamate [CPD:C00025];
            D-glucosamine 6-phosphate [CPD:C00352]
COMMENT     Although the overall reaction is that of a transferase, the
            mechanism involves the formation of ketimine between fructose
            6-phosphate and a 6-amino group from a lysine residue at the active
            site, which is subsequently displaced by ammonia (transamidination).
REFERENCE   1
  AUTHORS   Ghosh, S., Blumenthal, H.J., Davidson, E. and Roseman, S.
  TITLE     Glucosamine metabolism. V. Enzymatic synthesis of glucosamine
            6-phosphate.
  JOURNAL   J. Biol. Chem. 235 (1960) 1265-1273.
  ORGANISM  rat [GN:rno], Neurospora crassa [GN:dncr]
REFERENCE   2  [PMID:13829889]
  AUTHORS   GRYDER RM, POGELL BM.
  TITLE     Further studies on glucosamine 6-phosphate synthesis by rat liver
            enzymes.
  JOURNAL   J. Biol. Chem. 235 (1960) 558-62.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:13115409]
  AUTHORS   LELOIR LF, CARDINI CE.
  TITLE     The biosynthesis of glucosamine.
  JOURNAL   Biochim. Biophys. Acta. 12 (1953) 15-22.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   4  [PMID:10091662]
  AUTHORS   Teplyakov A, Obmolova G, Badet-Denisot MA, Badet B.
  TITLE     The mechanism of sugar phosphate isomerization by glucosamine
            6-phosphate synthase.
  JOURNAL   Protein. Sci. 8 (1999) 596-602.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K00820  glucosamine--fructose-6-phosphate aminotransferase
                        (isomerizing)
GENES       HSA: 2673(GFPT1)
            PTR: 462337(GFPT2)
            MMU: 14583(Gfpt1) 14584(Gfpt2)
            CFA: 474624(GFPT1) 474653(GFPT2)
            BTA: 281779(GFPT1)
            GGA: 419514(RCJMB04_26h2)
            XLA: 380175(gfpt1) 414702(MGC83201)
            DME: Dmel_CG1345(Gfat2)
            CEL: F22B3.4
            CME: CMK166C
            SCE: YKL104C(GFA1)
            AGO: AGOS_ABL036C
            PIC: PICST_67692(GFA1)
            CGR: CAGL0K08558g
            SPO: SPBC21D10.02
            ANI: AN5794.2
            AFM: AFUA_6G06340
            AOR: AO090003000003 AO090003001475
            CNE: CND02900
            UMA: UM03199.1
            ECU: ECU07_1280
            DDI: DDBDRAFT_0187034
            PFA: PF10_0245
            CPV: cgd1_3730
            CHO: Chro.10420
            TAN: TA15930
            TPV: TP02_0935
            TET: TTHERM_01005220
            TBR: Tb927.7.5560
            TCR: 510303.200
            LMA: LmjF06.0950
            EHI: 248.t00008
            ECO: b3729(glmS)
            ECJ: JW3707(glmS)
            ECE: Z5227(glmS)
            ECS: ECs4671
            ECC: c4654(glmS)
            ECI: UTI89_C4281(glmS)
            ECP: ECP_3928
            ECV: APECO1_2732(glmS)
            ECW: EcE24377A_4244(glmS)
            ECX: EcHS_A3944(glmS)
            STY: STY3917(glmS)
            STT: t3658(glmS)
            SPT: SPA3700(glmS)
            SEC: SC3774(glmS)
            STM: STM3861(glmS)
            YPE: YPO4118(glmS)
            YPK: y4132(glmS)
            YPM: YP_4025(glmS)
            YPA: YPA_4163
            YPN: YPN_3975
            YPP: YPDSF_3917
            YPS: YPTB3964(glmS)
            YPI: YpsIP31758_4173(glmS)
            SFL: SF3809(glmS)
            SFX: S3959(glmS)
            SFV: SFV_3755(glmS)
            SSN: SSON_3890(glmS)
            SBO: SBO_3758(glmS)
            SDY: SDY_4019(glmS)
            ECA: ECA4508(glmS)
            PLU: plu0037(glmS)
            BUC: BU026(glmS)
            BAS: BUsg027(glmS)
            BAB: bbp028(glmS)
            WBR: WGLp011(glmS)
            SGL: SG2417
            HIN: HI0429(glmS)
            HIT: NTHI0553(glmS)
            HIP: CGSHiEE_00845
            HIQ: CGSHiGG_05375
            HDU: HD1894(glmS)
            HSO: HS_1536(glmS)
            PMU: PM1731(glmS)
            MSU: MS0189(glmS)
            APL: APL_1631(glmS)
            XFA: XF0141
            XFT: PD0110(glmS)
            XCC: XCC0569(glmS)
            XCB: XC_3663
            XCV: XCV3754(glmS)
            XAC: XAC3637(glmS)
            XOO: XOO0746(glmS)
            XOM: XOO_0678(XOO0678)
            VCH: VC0487
            VCO: VC0395_A0039(glmS)
            VVU: VV1_0641
            VVY: VV0502
            VPA: VP0359
            VFI: VF2372
            PPR: PBPRA3599
            PAE: PA5549(glmS)
            PAU: PA14_73170(glmS)
            PAP: PSPA7_6350(glmS)
            PPU: PP_5409(glmS)
            PST: PSPTO_5595(glmS)
            PSB: Psyr_5117
            PSP: PSPPH_5203(glmS)
            PFL: PFL_6212(glmS)
            PFO: Pfl_5726
            PEN: PSEEN4381 PSEEN5537(glmS)
            PAR: Psyc_2074(glmS)
            PCR: Pcryo_2397
            ACI: ACIAD3576(glmS)
            SON: SO_4741(glmS)
            SDN: Sden_2705 Sden_3743
            SFR: Sfri_4040
            SAZ: Sama_0945 Sama_3639
            SBL: Sbal_1085 Sbal_4361
            SBM: Shew185_1145
            SLO: Shew_3839
            SPC: Sputcn32_1077
            SHE: Shewmr4_2934 Shewmr4_3920
            SHM: Shewmr7_3016 Shewmr7_4012
            SHN: Shewana3_3113 Shewana3_4125
            SHW: Sputw3181_3088 Sputw3181_4048
            ILO: IL2616(glmS)
            CPS: CPS_4942(glmS)
            PHA: PSHAa2994(glmS)
            PAT: Patl_0131 Patl_3881 Patl_4173
            SDE: Sde_3041 Sde_3948
            PIN: Ping_0085
            MAQ: Maqu_3872
            CBU: CBU_1787(glmS)
            CBD: COXBU7E912_0013(glmS)
            LPN: lpg2836(glmS)
            LPF: lpl2748(glmS)
            LPP: lpp2893(glmS)
            MCA: MCA0015(glmS)
            FTU: FTT0388(glmS)
            FTF: FTF0388(glmS)
            FTW: FTW_1686(glmS)
            FTL: FTL_0454 FTL_0864
            FTH: FTH_0451(glmS)
            FTA: FTA_0481(glmS)
            FTN: FTN_0485(glmS)
            TCX: Tcr_1692
            NOC: Noc_3071
            AEH: Mlg_2865
            HHA: Hhal_2426
            HCH: HCH_07068(glmS)
            CSA: Csal_3280
            ABO: ABO_2723(glmS)
            AHA: AHA_4254(glmS)
            DNO: DNO_0528(glmS)
            BCI: BCI_0138(glmS)
            RMA: Rmag_0883
            VOK: COSY_0809(glmS)
            NME: NMB0031
            NMA: NMA0276(glmS)
            NMC: NMC0008(glmS)
            NGO: NGO2045
            CVI: CV_0677(glmS)
            RSO: RSc0178(glmS)
            REU: Reut_A0230
            REH: H16_A0263(glmS)
            RME: Rmet_0187
            BMA: BMA3059(glmS-1) BMA3379(glmS-2)
            BMV: BMASAVP1_A1232(glmS-1) BMASAVP1_A3050(glmS-2)
            BML: BMA10299_A0636(glmS-1) BMA10299_A2042(glmS-2)
            BMN: BMA10247_0517(glmS-1) BMA10247_2242(glmS-2)
            BXE: Bxe_A0208
            BVI: Bcep1808_2927
            BUR: Bcep18194_A4463 Bcep18194_A6153 Bcep18194_A6331
                 Bcep18194_B1944 Bcep18194_B2724
            BCN: Bcen_0846 Bcen_2210 Bcen_2368 Bcen_4266
            BCH: Bcen2424_1327 Bcen2424_2823 Bcen2424_2982 Bcen2424_3445
                 Bcen2424_4100
            BAM: Bamb_2883 Bamb_3029
            BPS: BPSL0312(glmS1) BPSL1312(glmS2) BPSS2009(glmS3)
            BPM: BURPS1710b_0517(glmS) BURPS1710b_1560(glmS)
                 BURPS1710b_A1120(glmS)
            BPL: BURPS1106A_0336(glmS) BURPS1106A_1458(glmS)
                 BURPS1106A_A2740(glmS)
            BPD: BURPS668_0323(glmS) BURPS668_1427(glmS) BURPS668_A2892(glmS)
            BTE: BTH_I0288(glmS-1) BTH_II0348(glmS-2)
            BPE: BP0666(glmS)
            BPA: BPP4214(glmS)
            BBR: BB4802(glmS)
            RFR: Rfer_1074
            POL: Bpro_0675
            MPT: Mpe_A0560
            HAR: HEAR3199(glmS)
            MMS: mma_3443(glmS)
            NEU: NE0209(glmS)
            NET: Neut_0280
            NMU: Nmul_A0313
            EBA: ebA2244(glmS)
            AZO: azo3636(glmS)
            DAR: Daro_3931
            TBD: Tbd_2793
            MFA: Mfla_2741
            HPY: HP1532
            HPJ: jhp1420(glmS)
            HPA: HPAG1_1384
            HHE: HH0854(glmS)
            HAC: Hac_1787(glmS)
            WSU: WS0022(glmS)
            TDN: Tmden_1483
            CJE: Cj1366c(glmS)
            CJR: CJE1558(glmS)
            CJJ: CJJ81176_1368(glmS)
            CJU: C8J_1283(glmS)
            CJD: JJD26997_0284(glmS)
            CFF: CFF8240_0586(glmS)
            CCV: CCV52592_0218(glmS)
            CHA: CHAB381_0830(glmS)
            ABU: Abu_0444(glmS)
            NIS: NIS_0647(glmS)
            SUN: SUN_0536(glmS)
            GSU: GSU0270(glmS)
            GME: Gmet_0104 Gmet_1487
            PCA: Pcar_1805 Pcar_2933
            DVU: DVU3156(glmS)
            DDE: Dde_0502 Dde_0958
            LIP: LI0661(glmS)
            BBA: Bd3424(glmS)
            DPS: DP2915
            ADE: Adeh_3959
            MXA: MXAN_0501(glmS) MXAN_1386(glmS)
            SAT: SYN_02923
            SFU: Sfum_2580
            WOL: WD0535(glmS)
            WBM: Wbm0223
            AMA: AM1013(glmS)
            PUB: SAR11_1151(glmS)
            MLO: mll0833 mlr6386 mlr6774
            MES: Meso_1706
            SME: SMa0878(nodM) SMc00231(glmS)
            SMD: Smed_3409
            ATU: Atu1786(glmS)
            ATC: AGR_C_3284
            RET: RHE_CH02091(glmS1) RHE_CH04036(glmS2)
            RLE: RL2382(glmS) pRL100180(nodM) pRL120250
            BME: BMEII0685
            BMF: BAB2_0658
            BMS: BRA0582(glmS)
            BMB: BruAb2_0642(glmS)
            BOV: BOV_A0547(glmS)
            OAN: Oant_1455
            BJA: bll4607(glmS) blr1632(nodM)
            BRA: BRADO3763(glmS)
            BBT: BBta_4166(glmS)
            RPA: RPA2660(glmS)
            RPB: RPB_2854
            RPC: RPC_2606
            RPD: RPD_2618
            RPE: RPE_2786
            NWI: Nwi_1517
            NHA: Nham_2057
            BHE: BH09920(glmS)
            BQU: BQ07640(glmS)
            BBK: BARBAKC583_0755(glmS)
            CCR: CC_0118
            SIL: SPOA0140(glmS)
            SIT: TM1040_0727 TM1040_3149
            RSP: RSP_1447 RSP_2502(glmS)
            JAN: Jann_1360 Jann_3186
            RDE: RD1_3305(glmS)
            PDE: Pden_2476
            MMR: Mmar10_2453
            HNE: HNE_0778(glmS)
            ZMO: ZMO0056(glmS)
            NAR: Saro_1202 Saro_2415
            SAL: Sala_1366
            ELI: ELI_02430
            GOX: GOX0007
            GBE: GbCGDNIH1_1238
            RRU: Rru_A3029
            MAG: amb1279
            MGM: Mmc1_3455
            ABA: Acid345_0004 Acid345_0997 Acid345_2961
            SUS: Acid_1598
            BSU: BG10948(glmS) BG12712(ybcM)
            BHA: BH0268(glmS)
            BAN: BA0159(glmS)
            BAR: GBAA0159(glmS)
            BAA: BA_0740
            BAT: BAS0160
            BCE: BC0190
            BCA: BCE_0158(glmS)
            BCZ: BCZK0152(glmS)
            BTK: BT9727_0153(glmS)
            BTL: BALH_0155(glmS)
            BLI: BL02704(glmS)
            BLD: BLi00204(glmS)
            BCL: ABC0245(glmS)
            BAY: RBAM_002320(glmS)
            BPU: BPUM_0165(glmS)
            OIH: OB0235
            GKA: GK0155
            SAU: SA1959(glmS)
            SAV: SAV2154(glmS)
            SAM: MW2080(glmS)
            SAR: SAR2242(glmS)
            SAS: SAS2055
            SAC: SACOL2145(glmS)
            SAB: SAB2034c(glmS)
            SAA: SAUSA300_2104(glmS)
            SAO: SAOUHSC_02399
            SEP: SE1751
            SER: SERP1760(glmS)
            SHA: SH0880(glmS)
            SSP: SSP0729
            LMO: lmo0727
            LMF: LMOf2365_0762(glmS)
            LIN: lin0734
            LWE: lwe0695(glmS) lwe2019
            LLA: L33556(glmS)
            LLC: LACR_1094
            LLM: llmg_1516(glmS)
            SPY: SPy_1280(glmS)
            SPZ: M5005_Spy_0986(glmS)
            SPM: spyM18_1228(glmS)
            SPG: SpyM3_0910(glmS)
            SPS: SPs1109
            SPH: MGAS10270_Spy1100(glmS)
            SPI: MGAS10750_Spy1136(glmS)
            SPJ: MGAS2096_Spy1046(glmS)
            SPK: MGAS9429_Spy1090(glmS)
            SPF: SpyM50815(gcaA)
            SPA: M6_Spy0972
            SPB: M28_Spy0958(glmS)
            SPN: SP_0266
            SPR: spr0245(glmS)
            SPD: SPD_0248(glmS)
            SAG: SAG0944(glmS)
            SAN: gbs0933
            SAK: SAK_1040(glmS)
            SMU: SMU.1187(glmS)
            STC: str0873(glmS)
            STL: stu0873(glmS)
            SSA: SSA_2107(glmS)
            SGO: SGO_1757(glmS)
            LPL: lp_0822(glmS1)
            LJO: LJ1581
            LAC: LBA0462(glmS)
            LSA: LSA1355(glmS)
            LSL: LSL_1627(glmS)
            LDB: Ldb0494(glmS)
            LBU: LBUL_0440
            LBR: LVIS_0687
            LCA: LSEI_1019
            LGA: LGAS_0719
            EFA: EF2151(glmS)
            OOE: OEOE_0635
            STH: STH196
            CAC: CAC0158(glmS)
            CPE: CPE2327(glmS)
            CPF: CPF_2636(glmS)
            CPR: CPR_2322(glmS)
            CTC: CTC02543
            CNO: NT01CX_1166(glmS)
            CDF: CD0120(glmS)
            CBO: CBO3410(glmS)
            CBA: CLB_3467(glmS)
            CBH: CLC_3355(glmS)
            CBF: CLI_3593(glmS)
            CKL: CKL_0317(glmS)
            CHY: CHY_2010(glmS)
            DSY: DSY4485
            SWO: Swol_2099
            TTE: TTE2190(glmS)
            MTA: Moth_2245
            MTU: Rv3436c(glmS)
            MTC: MT3542(glmS)
            MBO: Mb3466c(glmS)
            MBB: BCG_3502c(glmS)
            MLE: ML0371(glmS)
            MPA: MAP4253(glmS)
            MAV: MAV_4377(glmS)
            MSM: MSMEG_0474 MSMEG_1568(glmS) MSMEG_5986(glmS)
            MMC: Mmcs_1139 Mmcs_3352
            CGL: NCgl2191(cgl2271)
            CGB: cg2492(glmS)
            CEF: CE2172
            CDI: DIP1700(glmS)
            CJK: jk1735(glmS)
            NFA: nfa8760(glmS)
            RHA: RHA1_ro06177(glmS)
            SCO: SCO2789(glmS2) SCO4740(glmS1)
            SMA: SAV4963(glmS1) SAV5265(glmS2)
            TWH: TWT606(glmS)
            TWS: TW158(glmS)
            LXX: Lxx19980(glmS)
            CMI: CMM_2576(glmS)
            AAU: AAur_2900(glmS)
            PAC: PPA1794
            TFU: Tfu_2611
            FRA: Francci3_0617
            FAL: FRAAL1117(glmS)
            ACE: Acel_0344 Acel_0556
            KRA: Krad_0771
            SEN: SACE_6768(glmS)
            STP: Strop_3707
            BLO: BL1175(glmS)
            BAD: BAD_0473(glmS)
            RXY: Rxyl_0137 Rxyl_0799
            FNU: FN0452
            RBA: RB12652(glmS)
            CTR: CT816(glmS)
            CTA: CTA_0889(glmS)
            CMU: TC0203
            CPN: CPn0968(glmS)
            CPA: CP0892
            CPJ: CPj0968(glmS)
            CPT: CpB1005
            CCA: CCA00788(glmS)
            CAB: CAB756(glmS)
            CFE: CF0225(glmS)
            PCU: pc1306(glmS)
            TPA: TP0861
            LIL: LA3801(glmS)
            LIC: LIC10445(glmS)
            LBJ: LBJ_0368(glmS)
            LBL: LBL_2709(glmS)
            SYN: sll0220(glmS)
            SYW: SYNW0145(glmS)
            SYC: syc0987_d(glmS)
            SYF: Synpcc7942_0534
            SYD: Syncc9605_0128
            SYE: Syncc9902_0172
            SYG: sync_0134(glmS)
            SYR: SynRCC307_0134(glmS)
            SYX: SynWH7803_0199(glmS)
            CYA: CYA_1543(glmS)
            CYB: CYB_1089(glmS)
            TEL: tll1237(glmS)
            GVI: gll2215
            ANA: alr3464(nodM)
            AVA: Ava_3485
            PMA: Pro1766(glmS)
            PMM: PMM1606(glmS)
            PMT: PMT1953(glmS)
            PMN: PMN2A_1183
            PMI: PMT9312_1699
            PMB: A9601_18161(glmS)
            PMC: P9515_17941(glmS)
            PMF: P9303_26041(glmS)
            PMG: P9301_17991(glmS)
            PMH: P9215_18801(glmS)
            PME: NATL1_20581(glmS)
            TER: Tery_0455
            BTH: BT_0554
            BFR: BF2638
            SRU: SRU_1363(glmS)
            CHU: CHU_3838(glmS)
            GFO: GFO_3547(glmS)
            FPS: FP0111(glmS)
            CTE: CT0130(glmS)
            CCH: Cag_0005
            PLT: Plut_0080
            DET: DET0531(glmS)
            DEH: cbdb_A503(glmS)
            RRS: RoseRS_2367
            RCA: Rcas_3111
            DRA: DR_0302
            DGE: Dgeo_0010 Dgeo_2624
            TTH: TTC1533
            TTJ: TTHA1896
            AAE: aq_301(glmS)
            TMA: TM0148
            TPT: Tpet_0115
            MJA: MJ1420
            MMP: MMP1680(glmS)
            MAC: MA3023(glmS)
            MBA: Mbar_A2022
            MMA: MM_0300
            MBU: Mbur_2343
            MHU: Mhun_2855
            MST: Msp_1054 Msp_1196(glmS)
            MSI: Msm_1551
            MKA: MK0127(glmS)
            HAL: VNG0006G(glmS)
            HMA: rrnAC1587(glmS1) rrnAC3235(glmS2)
            HWA: HQ2990A(glmS)
            NPH: NP2384A(glmS_2) NP4654A(glmS_1)
            PTO: PTO0012 PTO1138
            PAB: PAB2201
            PFU: PF0157
            TKO: TK0809
            RCI: RCIX1436(glmS)
            APE: APE_1205.1
            SSO: SSO0382(glmS-1) SSO1268(glmS-2)
            STO: ST2186 ST2545
            SAI: Saci_2364(glmS)
            PAI: PAE3025
STRUCTURES  PDB: 1JXA  1MOQ  1MOR  1MOS  1XFF  1XFG  2BPL  2J6H  2POC  2PUT  
                 2PUV  2PUW  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.16
            ExPASy - ENZYME nomenclature database: 2.6.1.16
            ExplorEnz - The Enzyme Database: 2.6.1.16
            ERGO genome analysis and discovery system: 2.6.1.16
            BRENDA, the Enzyme Database: 2.6.1.16
            CAS: 9030-45-9
///
ENTRY       EC 2.6.1.17                 Enzyme
NAME        succinyldiaminopimelate transaminase;
            succinyldiaminopimelate aminotransferase;
            N-succinyl-L-diaminopimelic glutamic transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     N-succinyl-L-2,6-diaminoheptanedioate:2-oxoglutarate
            aminotransferase
REACTION    N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate =
            N-succinyl-L-2-amino-6-oxoheptanedioate + L-glutamate [RN:R04475]
ALL_REAC    R04475
SUBSTRATE   N-succinyl-L-2,6-diaminoheptanedioate [CPD:C04421];
            2-oxoglutarate [CPD:C00026]
PRODUCT     N-succinyl-L-2-amino-6-oxoheptanedioate [CPD:C04462];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1
  AUTHORS   Peterkofsky, B. and Gilvarg, C.
  TITLE     N-Succinyl-L-diaminopimelic-glutamic transaminase.
  JOURNAL   J. Biol. Chem. 236 (1961) 1432-1438.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K00821  N-succinyldiaminopimelate aminotransferase
GENES       ECO: b3359(argD)
            ECJ: JW3322(argD)
            ECE: Z4720(argD)
            ECS: ECs4210
            ECC: c4134(argD)
            ECI: UTI89_C3862(argD)
            ECP: ECP_3450
            ECV: APECO1_3096(argD)
            ECW: EcE24377A_3829(argD)
            ECX: EcHS_A3556
            STY: STY4328(argD)
            STT: t4037(argD)
            SPT: SPA3334(argD)
            SEC: SC3402(argD)
            STM: STM3468(argD)
            YPK: y1507 y3954(argD)
            YPM: YP_0172(argD)
            YPA: YPA_3299
            YPN: YPN_3894
            YPS: YPTB3731
            YPI: YpsIP31758_3947(argD)
            SFL: SF3378(argD)
            SFX: S4385(argD)
            SFV: SFV_3365(argD)
            SSN: SSON_3490(argD)
            SBO: SBO_3341(argD)
            SDY: SDY_3521(argD)
            ECA: ECA4065(argD)
            PLU: plu0394(argD)
            BUC: BU534(argD)
            BAS: BUsg515(argD)
            XFT: PD1474(aspC)
            XCC: XCC2218(ybdL)
            XCB: XC_1899
            XCV: XCV2521
            XAC: XAC2322(ybdL)
            XOO: XOO2156(ybdL)
            XOM: XOO_2025(XOO2025)
            PAE: PA3659
            PPU: PP_1588
            PST: PSPTO_1531
            PSB: Psyr_1340
            PSP: PSPPH_3843(dapC)
            PFL: PFL_1173(aspB-4)
            PFO: Pfl_1098
            PEN: PSEEN4223
            PAR: Psyc_0393
            PCR: Pcryo_0439
            ACI: ACIAD2080
            CPS: CPS_0636(argD)
            MCA: MCA1491
            NOC: Noc_2124
            HCH: HCH_05257
            ABO: ABO_1140
            AHA: AHA_3180
            NME: NMB0894
            NMA: NMA1113
            NGO: NGO0460
            CVI: CV_0451(dapC)
            RSO: RSc1394(dapC)
            REU: Reut_A1891
            RME: Rmet_1424
            BMA: BMA1565
            BXE: Bxe_A1671
            BPS: BPSL2168
            BTE: BTH_I2017
            BPE: BP1765(dapC)
            BPA: BPP1996(dapC)
            RFR: Rfer_2047
            POL: Bpro_1997
            MPT: Mpe_A1807
            MMS: mma_2068
            NEU: NE2463(dapC)
            NET: Neut_0228
            NMU: Nmul_A1850
            AZO: azo2004(dapC)
            DAR: Daro_1727
            TBD: Tbd_1221
            MFA: Mfla_1386
            HPY: HP0624(aspB)
            HPJ: jhp0568
            HPA: HPAG1_0607
            HHE: HH0372
            HAC: Hac_0736(aspB)
            WSU: WS1483
            TDN: Tmden_0759
            ABU: Abu_0232(aspB2)
            DVU: DVU1655
            BBA: Bd0127(argD)
            SAT: SYN_00570
            APH: APH_0945(argD)
            ERU: Erum2110(argD)
            ECN: Ecaj_0214
            ECH: ECH_0886(argD)
            PUB: SAR11_0502(argD)
            RET: RHE_CH01877(aatCch) RHE_PD00118(aatCd)
            RLE: RL2096
            BMF: BAB1_1294
            BJA: blr0615
            BRA: BRADO6779(argD)
            BBT: BBta_0759(argD)
            RPA: RPA0278
            RPE: RPE_0399
            SIL: SPO3417
            SIT: TM1040_0059
            RSP: RSP_1494
            JAN: Jann_0427
            RDE: RD1_0034
            GBE: GbCGDNIH1_2274
            MGM: Mmc1_0044
            BSU: BG12362(yugH)
            BHA: BH0936 BH3350
            BAN: BA2899 BA5133
            BAR: GBAA2899 GBAA5133
            BAA: BA_0007 BA_3415
            BAT: BAS2700 BAS4771
            BCE: BC4901
            BCA: BCE_5040
            BLI: BL02594(alaT)
            BLD: BLi03320(alaT)
            CAC: CAC2380
            CPE: CPE1907(patA)
            TTE: TTE2440(avtA4)
            MTU: Rv0858c
            MTC: MT0881
            MBO: Mb0881c
            MPA: MAP0788c
            MMC: Mmcs_4497
            CGL: NCgl0780(cgl0814)
            CGB: cg0931 cg1253(dapC)
            CEF: CE0889
            NFA: nfa6260
            RHA: RHA1_ro00953(argD) RHA1_ro04939
            SCO: SCO3658(SCH10.36)
            SMA: SAV4517(dapC)
            TFU: Tfu_0568
            FAL: FRAAL6125(dapC)
            SEN: SACE_6995
            SYN: sll0938
            SYG: sync_2108
            CYA: CYA_0589
            CYB: CYB_0071
            TEL: tlr0930
            GVI: glr3468
            ANA: all2340 all4327
            FPS: FP1771(argD)
            DET: DET0739
            AAE: aq_273(aspC4)
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.17
            ExPASy - ENZYME nomenclature database: 2.6.1.17
            ExplorEnz - The Enzyme Database: 2.6.1.17
            ERGO genome analysis and discovery system: 2.6.1.17
            BRENDA, the Enzyme Database: 2.6.1.17
            CAS: 9030-46-0
///
ENTRY       EC 2.6.1.18                 Enzyme
NAME        beta-alanine---pyruvate transaminase;
            beta-alanine-pyruvate aminotransferase;
            beta-alanine-alpha-alanine transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-alanine:3-oxopropanoate aminotransferase
REACTION    L-alanine + 3-oxopropanoate = pyruvate + beta-alanine [RN:R00907]
ALL_REAC    R00907;
            (other) R04187
SUBSTRATE   L-alanine [CPD:C00041];
            3-oxopropanoate [CPD:C00222]
PRODUCT     pyruvate [CPD:C00022];
            beta-alanine [CPD:C00099]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:13712439]
  AUTHORS   HAYAISHI O, NISHIZUKA Y, TATIBANA M, TAKESHITA M, KUNO S.
  TITLE     Enzymatic studies on the metabolism of beta-alanine.
  JOURNAL   J. Biol. Chem. 236 (1961) 781-90.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   2  [PMID:5762452]
  AUTHORS   Stinson RA, Spencer MS.
  TITLE     Beta alanine aminotransferase (s) from a plant source.
  JOURNAL   Biochem. Biophys. Res. Commun. 34 (1969) 120-7.
  ORGANISM  Phaseolus vulgaris
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
            PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00410  beta-Alanine metabolism
            PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K00822  beta-alanine--pyruvate transaminase
GENES       PLU: plu2260
            XCC: XCC2357
            XCB: XC_1759
            XCV: XCV2668
            XAC: XAC2489
            XOO: XOO2793
            XOM: XOO_2635(XOO2635)
            PAE: PA0132 PA5313
            PAU: PA14_01620(aptA) PA14_70160(bioA)
            PPU: PP_0596
            PST: PSPTO_0774
            PSB: Psyr_0678
            PSP: PSPPH_4619
            PFL: PFL_0733
            PFO: Pfl_0685
            PEN: PSEEN0681
            SON: SO_3497
            SFR: Sfri_3022
            SSE: Ssed_1044
            SHE: Shewmr4_2927
            SHN: Shewana3_3106
            CPS: CPS_0099 CPS_4059
            CSA: Csal_1125
            AHA: AHA_0245
            CVI: CV_1436
            RSO: RS02393(RSp1056)
            REU: Reut_A0248 Reut_C6274
            REH: H16_A0272(aptA)
            RME: Rmet_0205
            BMA: BMA2175 BMAA1380
            BMV: BMASAVP1_0494 BMASAVP1_A0734(aptA)
            BML: BMA10299_0156 BMA10299_A2567(aptA)
            BMN: BMA10247_2046(aptA) BMA10247_A1454
            BXE: Bxe_B0670
            BUR: Bcep18194_B1698
            BCN: Bcen_4053
            BCH: Bcen2424_4313
            BPS: BPSL2650 BPSS0742
            BPM: BURPS1710b_3126(aptA) BURPS1710b_A2318 BURPS1710b_A2467
            BPL: BURPS1106A_3101(aptA) BURPS1106A_A1009
            BPD: BURPS668_3065(aptA) BURPS668_A1096
            BTE: BTH_I1505 BTH_II1658
            BPE: BP3157
            BPA: BPP0784
            BBR: BB0869
            RFR: Rfer_0373
            POL: Bpro_4286
            MPT: Mpe_A1898
            HAR: HEAR2429
            MMS: mma_2491
            AZO: azo2100
            MLO: mll1632
            SME: SMc01534 SMc04388
            ATU: Atu3329(bioA)
            ATC: AGR_L_2984
            RET: RHE_PF00434(ypf00232)
            RLE: RL3538 pRL120419(aptA)
            BME: BMEII0371
            BMF: BAB2_0309
            BMS: BRA0926
            BMB: BruAb2_0307
            BJA: blr2221(bioA)
            BBT: BBta_7631
            RPA: RPA1179
            RPB: RPB_1184
            RPC: RPC_0894
            RPD: RPD_1288
            RPE: RPE_0915
            NWI: Nwi_2537
            NHA: Nham_3157
            CCR: CC_3143
            RRU: Rru_A1541
            CYA: CYA_0689
            CYB: CYB_2128
            TEL: tlr0408
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.18
            ExPASy - ENZYME nomenclature database: 2.6.1.18
            ExplorEnz - The Enzyme Database: 2.6.1.18
            ERGO genome analysis and discovery system: 2.6.1.18
            BRENDA, the Enzyme Database: 2.6.1.18
            CAS: 9030-47-1
///
ENTRY       EC 2.6.1.19                 Enzyme
NAME        4-aminobutyrate transaminase;
            beta-alanine-oxoglutarate transaminase;
            aminobutyrate aminotransferase;
            beta-alanine aminotransferase;
            beta-alanine-oxoglutarate aminotransferase;
            gamma-aminobutyrate aminotransaminase;
            gamma-aminobutyrate transaminase;
            gamma-aminobutyrate-alpha-ketoglutarate aminotransferase;
            gamma-aminobutyrate-alpha-ketoglutarate transaminase;
            gamma-aminobutyrate:alpha-oxoglutarate aminotransferase;
            gamma-aminobutyric acid aminotransferase;
            gamma-aminobutyric acid pyruvate transaminase;
            gamma-aminobutyric acid transaminase;
            gamma-aminobutyric acid-alpha-ketoglutarate transaminase;
            gamma-aminobutyric acid-alpha-ketoglutaric acid aminotransferase;
            gamma-aminobutyric acid-2-oxoglutarate transaminase;
            gamma-aminobutyric transaminase;
            4-aminobutyrate aminotransferase;
            4-aminobutyrate-2-ketoglutarate aminotransferase;
            4-aminobutyrate-2-oxoglutarate aminotransferase;
            4-aminobutyrate-2-oxoglutarate transaminase;
            4-aminobutyric acid 2-ketoglutaric acid aminotransferase;
            4-aminobutyric acid aminotransferase;
            aminobutyrate aminotransferase;
            aminobutyrate transaminase;
            GABA aminotransferase;
            GABA transaminase;
            GABA transferase;
            GABA-alpha-ketoglutarate aminotransferase;
            GABA-alpha-ketoglutarate transaminase;
            GABA-alpha-ketoglutaric acid transaminase;
            GABA-alpha-oxoglutarate aminotransferase;
            GABA-2-oxoglutarate aminotransferase;
            GABA-2-oxoglutarate transaminase;
            GABA-oxoglutarate aminotransferase;
            GABA-oxoglutarate transaminase;
            glutamate-succinic semialdehyde transaminase;
            GabT
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     4-aminobutanoate:2-oxoglutarate aminotransferase
REACTION    4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde +
            L-glutamate [RN:R01648]
ALL_REAC    R01648;
            (other) R00908
SUBSTRATE   4-aminobutanoate [CPD:C00334];
            2-oxoglutarate [CPD:C00026]
PRODUCT     succinate semialdehyde [CPD:C00232];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     Some preparations also act on beta-alanine, 5-aminopentanoate and
            (R,S)-3-amino-2-methylpropanoate.
REFERENCE   1
  AUTHORS   Aurich, H.
  TITLE     Uber die beta-Alanin-alpha-Ketoglutarat-Transaminase aus Neurospora
            crassa.
  JOURNAL   Hoppe-Seyler's Z. Physiol. Chem. 326 (1961) 25-33.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2  [PMID:4719123]
  AUTHORS   Schousboe A, Wu JY, Roberts E.
  TITLE     Purification and characterization of the
            4-aminobutyrate--2,ketoglutarate transaminase from mouse brain.
  JOURNAL   Biochemistry. 12 (1973) 2868-73.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:13654294]
  AUTHORS   SCOTT EM, JAKOBY WB.
  TITLE     Soluble gamma-aminobutyric-glutamic transaminase from Pseudomonas
            fluorescens.
  JOURNAL   J. Biol. Chem. 234 (1959) 932-6.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00252  Alanine and aspartate metabolism
            PATH: map00410  beta-Alanine metabolism
            PATH: map00640  Propanoate metabolism
            PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K00823  4-aminobutyrate aminotransferase
GENES       HSA: 18(ABAT)
            MMU: 268860(Abat)
            RNO: 81632(Abat)
            BTA: 280969(ABAT)
            SSC: 397500(ABAT)
            GGA: 416642(ABAT)
            XLA: 399028(MGC68458)
            DRE: 378968(abat)
            SPU: 577656(LOC577656)
            DME: Dmel_CG7433
            CEL: K04D7.3(gta-1)
            CME: CMR117C
            SCE: YGR019W(UGA1)
            AGO: AGOS_AGL050C
            PIC: PICST_46781(UGA1.2) PICST_54153(UGA1.1)
            CGR: CAGL0D04026g
            SPO: SPAC19D5.07
            ANI: AN2248.2
            AFM: AFUA_5G06680
            AOR: AO090701000206
            CNE: CNC04690 CND02040 CNE01830 CNI00880
            UMA: UM01040.1 UM01080.1
            DDI: DDB_0231448(gabT)
            ECO: b1302(goaG) b2662(gabT)
            ECJ: JW1295(puuE) JW2637(gabT)
            ECE: Z2486(goaG) Z3960(gabT)
            ECS: ECs1879 ECs3523
            ECC: c3210(gabT)
            ECI: UTI89_C3017(gabT)
            ECP: ECP_2625
            ECV: APECO1_3858(gabT)
            ECW: EcE24377A_1512(gabT1) EcE24377A_2942(gabT2)
            ECX: EcHS_A1417(gabT1) EcHS_A2797(gabT2)
            STY: STY2912(gabT)
            STT: t2687(gabT)
            SPT: SPA2649(gabT)
            SEC: SC2724(gabT)
            STM: STM2792(gabT)
            YPE: YPO2844(goaG)
            YPK: y1390(goaG)
            YPM: YP_2711(goaG)
            YPA: YPA_2283
            YPN: YPN_1294
            YPS: YPTB2810(goaG)
            YPI: YpsIP31758_1218(gabT)
            SFL: SF1307(goaG) SF2689(gabT)
            SFX: S1389(goaG) S2874(gabT)
            SFV: SFV_1316(goaG) SFV_2841(gabT)
            SSN: SSON_2806(gabT)
            SBO: SBO_1760(goaG)
            ECA: ECA2053(gabT)
            PLU: plu2347(goaG)
            VCH: VCA0605
            VVU: VV2_1663
            VVY: VVA0475
            VPA: VP1771 VPA0234
            PAE: PA0266(gabT)
            PAU: PA14_03450(gabT)
            PAP: PSPA7_0344(gabT)
            PPU: PP_0214(gabT)
            PST: PSPTO_0259(gabT-1) PSPTO_0301(gabT-2)
            PSB: Psyr_0090 Psyr_0146
            PSP: PSPPH_0095(gabT1) PSPPH_5040(gabT3)
            PFL: PFL_0186(gabT)
            PFO: Pfl_0188
            PEN: PSEEN0191(gabT)
            PAR: Psyc_0809(gabT)
            PCR: Pcryo_0819
            ACI: ACIAD3446(gabT)
            SON: SO_1276(gabT)
            SDN: Sden_0910
            SFR: Sfri_3003
            SHE: Shewmr4_2912
            SHM: Shewmr7_2994
            SHN: Shewana3_3091
            CPS: CPS_4664(gabT)
            LPN: lpg0239(gabT)
            LPF: lpl0293(gabT)
            LPP: lpp0309(gabT)
            AHA: AHA_3002(gabT)
            CVI: CV_3926(goaG)
            RSO: RSc0029(goaG)
            REU: Reut_B5663
            REH: H16_B0981(gabT)
            RME: Rmet_1618
            BMA: BMAA1480(gabT)
            BML: BMA10299_2127(gabT)
            BMN: BMA10247_A0810(gabT)
            BXE: Bxe_B0834 Bxe_B1978
            BUR: Bcep18194_B0280
            BCN: Bcen_3005
            BCH: Bcen2424_5361
            BPS: BPSS0281(gabT)
            BPM: BURPS1710b_A1822(gabT)
            BPL: BURPS1106A_A0396(gabT)
            BPD: BURPS668_A0494(gabT)
            BTE: BTH_II2119(gabT)
            BPE: BP1977(goaG) BP2298
            BPA: BPP2357(goaG) BPP2431
            BBR: BB1807(goaG) BB1880
            RFR: Rfer_0592
            POL: Bpro_2912
            MPT: Mpe_A1910
            DDE: Dde_0417
            SAT: SYN_01215
            MLO: mlr5521
            SME: SMb21186(gabT)
            RET: RHE_CH00093(gabT)
            BRA: BRADO3420(gabT)
            BBT: BBta_4286(gabT)
            RPA: RPA2323(goaT)
            RPB: RPB_3137
            RPC: RPC_3494
            SIL: SPOA0274(gabT)
            SIT: TM1040_3262
            RSP: RSP_2176C(gabT) RSP_2176N(gabT)
            JAN: Jann_3070
            RDE: RD1_0839(gabT)
            PDE: Pden_2338
            NAR: Saro_2602
            ABA: Acid345_1534
            BSU: BG12043(gabT)
            BHA: BH0991
            BAN: BA0325(gabT)
            BAR: GBAA0325(gabT)
            BAA: BA_0895
            BAT: BAS0310
            BCE: BC0355
            BCA: BCE_0354(gabT)
            BCZ: BCZK0297(gabT)
            BTK: BT9727_0293(gabT)
            BTL: BALH_0317(gabT)
            BLI: BL01762(gabT)
            BLD: BLi00474(gabT)
            BCL: ABC2997(gabT)
            BAY: RBAM_002040(gabT1) RBAM_004150(gabT)
            BPU: BPUM_0362(gabT)
            OIH: OB1261
            SAU: SA2397
            SAV: SAV2604
            SAM: MW2523
            SAR: SAR2682
            SAS: SAS2489
            SAC: SACOL2620
            SAA: SAUSA300_2539
            SAO: SAOUHSC_02924
            SEP: SE2148
            SER: SERP2159
            SHA: SH0459(argD)
            SSP: SSP0187 SSP0353
            LPL: lp_1721
            OOE: OEOE_0387
            STH: STH616
            CAC: CAC0368 CAC1427(gabT)
            CDF: CD2158(gabT)
            CKL: CKL_3119(gabT)
            MTC: MT2666(gabT)
            MLE: ML0485(gabT)
            MPA: MAP1041c(gabT)
            MAV: MAV_3470(gabT)
            MSM: MSMEG_0581(gabT) MSMEG_2487 MSMEG_2959(gabT) MSMEG_6685(gabT)
            MMC: Mmcs_2274
            CGL: NCgl0462(cgl0479)
            CGB: cg0566(gabT)
            RHA: RHA1_ro04469(gabT1) RHA1_ro04544(gabT2) RHA1_ro05598(gabT3)
                 RHA1_ro08620 RHA1_ro08787(gabT4)
            SCO: SCO5676(gabT) SCO7034(SC1H10.23)
            SMA: SAV2583(gabT) SAV7160
            TWH: TWT633(gabT)
            TWS: TW652(gabT)
            LXX: Lxx12130(goaG) Lxx12170(gabT)
            CMI: CMM_2163(gabT)
            AAU: AAur_3069(gabT)
            TFU: Tfu_0690
            FRA: Francci3_3824
            FAL: FRAAL6081(gabT)
            SEN: SACE_3418 SACE_3766(gabT2) SACE_6022(gabT)
            RXY: Rxyl_2903
            GVI: glr3849
            ANA: alr2398
            AVA: Ava_0214
            GFO: GFO_2173(gabT)
            DRA: DR_A0029
            DGE: Dgeo_0989
            TTH: TTC0510
            TTJ: TTHA0862
            MAC: MA2859(argD)
            MBA: Mbar_A2386
            MMA: MM_0047
            HAL: VNG1524C
            HMA: rrnAC0382(gabT)
            NPH: NP6188A(gabT)
            TAC: Ta0068
            TVO: TVN0024
            PTO: PTO0791
            PHO: PH0782 PH1501
            PAB: PAB0086 PAB0501(gabT) PAB1921 PAB2386
            PFU: PF0513 PF1232 PF1421
            TKO: TK1211 TK2101
            APE: APE_0457
            SSO: SSO2727(gabT-1) SSO3211(gabT-2)
            STO: ST0735
            SAI: Saci_1028
            PAI: PAE1799
STRUCTURES  PDB: 1OHV  1OHW  1OHY  1SF2  1SFF  1SZK  1SZS  1SZU  2EO5  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.19
            ExPASy - ENZYME nomenclature database: 2.6.1.19
            ExplorEnz - The Enzyme Database: 2.6.1.19
            ERGO genome analysis and discovery system: 2.6.1.19
            BRENDA, the Enzyme Database: 2.6.1.19
            CAS: 9037-67-6
///
ENTRY       EC 2.6.1.20       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
COMMENT     Deleted entry: tyrosine-pyruvate transaminase (EC 2.6.1.20 created
            1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.20
            ExPASy - ENZYME nomenclature database: 2.6.1.20
            ExplorEnz - The Enzyme Database: 2.6.1.20
            ERGO genome analysis and discovery system: 2.6.1.20
            BRENDA, the Enzyme Database: 2.6.1.20
///
ENTRY       EC 2.6.1.21                 Enzyme
NAME        D-amino-acid transaminase;
            D-aspartate transaminase;
            D-alanine aminotransferase;
            D-aspartic aminotransferase;
            D-alanine-D-glutamate transaminase;
            D-alanine transaminase;
            D-amino acid aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     D-alanine:2-oxoglutarate aminotransferase
REACTION    D-alanine + 2-oxoglutarate = pyruvate + D-glutamate [RN:R01148]
ALL_REAC    R01148;
            (other) R01582 R02459 R02851 R02924 R03041 R05053
SUBSTRATE   D-alanine [CPD:C00133];
            2-oxoglutarate [CPD:C00026]
PRODUCT     pyruvate [CPD:C00022];
            D-glutamate [CPD:C00217]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. The enzyme from thermophilic Bacillus
            species acts on many D-amino acids with D-alanine and
            D-2-aminobutyrate as the best amino donors. It can similarly use any
            of several 2-oxo acids as amino acceptor, with 2-oxoglutarate and
            2-oxobutyrate among the best. The enzyme from some other sources has
            a broader specificity [6].
REFERENCE   1  [PMID:14367287]
  AUTHORS   THORNE CB, GOMEZ CG, HOUSEWRIGHT RD.
  TITLE     Transamination of D-amino acids by Bacillus subtilis.
  JOURNAL   J. Bacteriol. 69 (1955) 357-62.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   2  [PMID:13263311]
  AUTHORS   THORNE CB, MOLNAR DM.
  TITLE     D-Amino acid transamination in bacillus anthracis.
  JOURNAL   J. Bacteriol. 70 (1955) 420-6.
  ORGANISM  Bacillus anthracis
REFERENCE   3  [PMID:4953710]
  AUTHORS   Martinez-Carrion M, Jenkins WT.
  TITLE     D-Alanine-D-glutamate transaminase. I. Purification and
            characterization.
  JOURNAL   J. Biol. Chem. 240 (1965) 3538-46.
  ORGANISM  Bacillus subtilis [GN:bsu], Bacillus anthracis
REFERENCE   4  [PMID:4710577]
  AUTHORS   Ogawa T, Fukuda M, Sasaoka K.
  TITLE     Occurrence of D-amino acid aminotransferase in pea seedlings.
  JOURNAL   Biochem. Biophys. Res. Commun. 52 (1973) 998-1002.
  ORGANISM  Pisum sativum
REFERENCE   5  [PMID:1158891]
  AUTHORS   Yonaha K, Misono H, Yamamoto T, Soda K.
  TITLE     D-amino acid aminotransferase of Bacillus sphaericus. Enzymologic
            and spectrometric properties.
  JOURNAL   J. Biol. Chem. 250 (1975) 6983-9.
  ORGANISM  Bacillus sphaericus
REFERENCE   6  [PMID:2914916]
  AUTHORS   Tanizawa K, Masu Y, Asano S, Tanaka H, Soda K.
  TITLE     Thermostable D-amino acid aminotransferase from a thermophilic
            Bacillus species. Purification, characterization, and active site
            sequence determination.
  JOURNAL   J. Biol. Chem. 264 (1989) 2445-9.
  ORGANISM  Bacillus sphaericus, Bacillus sp.
REFERENCE   7  [PMID:9696787]
  AUTHORS   Fotheringham IG, Bledig SA, Taylor PP.
  TITLE     Characterization of the genes encoding D-amino acid transaminase and
            glutamate racemase, two D-glutamate biosynthetic enzymes of Bacillus
            sphaericus ATCC 10208.
  JOURNAL   J. Bacteriol. 180 (1998) 4319-23.
  ORGANISM  Bacillus sphaericus
REFERENCE   8  [PMID:9485439]
  AUTHORS   van Ophem PW, Erickson SD, Martinez del Pozo A, Haller I, Chait BT,
            Yoshimura T, Soda K, Ringe D, Petsko G, Manning JM.
  TITLE     Substrate inhibition of D-amino acid transaminase and protection by
            salts and by reduced nicotinamide adenine dinucleotide: isolation
            and initial characterization of a pyridoxo intermediate related to
            inactivation.
  JOURNAL   Biochemistry. 37 (1998) 2879-88.
REFERENCE   9  [PMID:7626635]
  AUTHORS   Sugio S, Petsko GA, Manning JM, Soda K, Ringe D.
  TITLE     Crystal structure of a D-amino acid aminotransferase: how the
            protein controls stereoselectivity.
  JOURNAL   Biochemistry. 34 (1995) 9661-9.
  ORGANISM  Bacillus sphaericus, Bacillus sp.
PATHWAY     PATH: map00310  Lysine degradation
            PATH: map00330  Arginine and proline metabolism
            PATH: map00360  Phenylalanine metabolism
            PATH: map00472  D-Arginine and D-ornithine metabolism
            PATH: map00473  D-Alanine metabolism
            PATH: map00550  Peptidoglycan biosynthesis
ORTHOLOGY   KO: K00824  D-alanine transaminase
GENES       ECA: ECA2971 ECA3117(dat)
            PAT: Patl_4024
            LPN: lpg1510
            LPF: lpl1516(ala)
            LPP: lpp1467(ala)
            MCA: MCA0106
            TCX: Tcr_1636
            NOC: Noc_2631
            AEH: Mlg_0177
            HHA: Hhal_1013
            ABO: ABO_1960(dat)
            VOK: COSY_0432
            RSO: RS01735(RSp0714)
            REU: Reut_A2225
            REH: H16_A2521(dat)
            RME: Rmet_2249
            BMA: BMA0057
            BXE: Bxe_A4217
            BUR: Bcep18194_A6235 Bcep18194_C6784
            BAM: Bamb_2942
            BPS: BPSL0409
            BPM: BURPS1710b_0621
            BTE: BTH_I0381
            BPE: BP0103 BP0769
            BPA: BPP0167 BPP0330
            BBR: BB0169 BB0333
            RFR: Rfer_1037 Rfer_1546
            POL: Bpro_0317
            MPT: Mpe_A0312
            HAR: HEAR3000(dat)
            MMS: mma_3249
            NEU: NE1486
            NET: Neut_0760
            NMU: Nmul_A1990
            EBA: ebA3046
            AZO: azo0181(daaA)
            DAR: Daro_0290
            TBD: Tbd_0267
            MFA: Mfla_2498
            CFF: CFF8240_0563
            CCV: CCV52592_1852
            CHA: CHAB381_1083
            ADE: Adeh_2654
            MLO: mlr0401
            MES: Meso_1614
            SME: SMa0093 SMc01047
            ATU: Atu2511(dat) Atu5473(dat)
            ATC: AGR_C_4563 AGR_pAT_698
            RET: RHE_CH01953(ypch00632)
            RLE: RL2283
            BME: BMEII0363
            BMF: BAB2_0301
            BMS: BRA0934
            BMB: BruAb2_0299
            BJA: bll7596
            BRA: BRADO6144
            BBT: BBta_1647
            RPA: RPA2596
            RPE: RPE_2761
            NWI: Nwi_1448
            CCR: CC_1744
            SIL: SPO3604
            SIT: TM1040_3168
            RSP: RSP_1768 RSP_3455
            JAN: Jann_0363
            RDE: RD1_1004(dat)
            HNE: HNE_3117
            GBE: GbCGDNIH1_1121
            RRU: Rru_A1682
            BSU: BG13045(dat)
            BHA: BH2811
            BAN: BA2256(dat-1) BA5472(dat-2)
            BAR: GBAA2256(dat-1) GBAA5472(dat-2)
            BAA: BA_2758
            BAT: BAS2100 BAS5082
            BCE: BC2209 BC5233
            BCA: BCE_2285(dat) BCE_5351(dat)
            BCZ: BCZK2037(daaA) BCZK4929(dat)
            BCY: Bcer98_1655
            BTK: BT9727_2039(daaA) BT9727_4914(dat)
            BTL: BALH_2017(daaA) BALH_4731(dat)
            BLI: BL02875(dat)
            BLD: BLi01040(dat)
            BCL: ABC2489(dat)
            BAY: RBAM_009900
            BPU: BPUM_0916
            OIH: OB1083(daaA)
            GKA: GK0672
            SAU: SA1571
            SAV: SAV1750
            SAM: MW1693
            SAR: SAR1835(dat)
            SAS: SAS1676
            SAC: SACOL1800(dat)
            SAB: SAB1610c(dat)
            SAA: SAUSA300_1696(dat)
            SAO: SAOUHSC_01867
            SEP: SE1423
            SER: SERP1309(dat)
            SHA: SH1172(dat)
            SSP: SSP1013
            LMO: lmo1619(daaA)
            LMF: LMOf2365_1641(dat)
            LIN: lin1660(daaA)
            LWE: lwe1635(dat)
            LSL: LSL_1670
            STH: STH1330
            CAC: CAC0792
            DSY: DSY3261
            CSC: Csac_0835
            SRU: SRU_0542
STRUCTURES  PDB: 1A0G  1DAA  1G2W  2DAA  2DAB  3DAA  4DAA  5DAA  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.21
            ExPASy - ENZYME nomenclature database: 2.6.1.21
            ExplorEnz - The Enzyme Database: 2.6.1.21
            ERGO genome analysis and discovery system: 2.6.1.21
            BRENDA, the Enzyme Database: 2.6.1.21
            CAS: 37277-85-3
///
ENTRY       EC 2.6.1.22                 Enzyme
NAME        (S)-3-amino-2-methylpropionate transaminase;
            L-3-aminoisobutyrate transaminase;
            beta-aminobutyric transaminase;
            L-3-aminoisobutyric aminotransferase;
            beta-aminoisobutyrate-alpha-ketoglutarate transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     (S)-3-amino-2-methylpropanoate:2-oxoglutarate aminotransferase
REACTION    (S)-3-amino-2-methylpropanoate + 2-oxoglutarate =
            2-methyl-3-oxopropanoate + L-glutamate
ALL_REAC    (other) R04188
SUBSTRATE   (S)-3-amino-2-methylpropanoate [CPD:C03284];
            2-oxoglutarate [CPD:C00026]
PRODUCT     2-methyl-3-oxopropanoate [CPD:C00349];
            L-glutamate [CPD:C00025]
COMMENT     Also acts on beta-alanine and other omega-amino acids having carbon
            chains between 2 and 5. The two enantiomers of the
            2-methyl-3-oxopropanoate formed by the enzyme interconvert by
            enolization, so that this enzyme, together with EC 2.6.1.40,
            (R)-3-amino-2-methylpropionate---pyruvate transaminase, provide a
            route for interconversion of the enantiomers of
            3-amino-2-methylpropanoate.
REFERENCE   1  [PMID:5641913]
  AUTHORS   Kakimoto Y, Kanazawa A, Taniguchi K, Sano I.
  TITLE     Beta-aminoisobutyrate-alpha-ketoglutarate transaminase in relation
            to beta-aminoisobutyric aciduria.
  JOURNAL   Biochim. Biophys. Acta. 156 (1968) 374-80.
  ORGANISM  pig [GN:ssc], human [GN:hsa]
REFERENCE   2  [PMID:10989446]
  AUTHORS   Tamaki N, Sakata SF, Matsuda K.
  TITLE     Purification, properties, and sequencing of aminoisobutyrate
            aminotransferases from rat liver.
  JOURNAL   Methods. Enzymol. 324 (2000) 376-89.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
ORTHOLOGY   KO: K07250  (S)-3-amino-2-methylpropionate transaminase
GENES       HSA: 18(ABAT)
            BTA: 280969(ABAT)
            ECO: b2662(gabT)
            ECJ: JW2637(gabT)
            ECE: Z3960(gabT)
            ECS: ECs3523
            ECC: c3210(gabT)
            ECI: UTI89_C3017(gabT)
            ECV: APECO1_3858(gabT)
            STY: STY2912(gabT)
            STT: t2687(gabT)
            SPT: SPA2649(gabT)
            SEC: SC2724(gabT)
            STM: STM2792(gabT)
            YPE: YPO2844(goaG)
            YPK: y1390(goaG)
            YPM: YP_2711(goaG)
            YPA: YPA_2283
            YPN: YPN_1294
            YPS: YPTB2810(goaG)
            SFL: SF2689(gabT)
            SFX: S2874(gabT)
            SFV: SFV_2841(gabT)
            SSN: SSON_2806(gabT)
            ECA: ECA2053(gabT)
            PLU: plu2347(goaG)
            VPA: VP1771
            PAE: PA0266(gabT)
            PAU: PA14_03450(gabT)
            PPU: PP_0214(gabT)
            PST: PSPTO_0259(gabT-1) PSPTO_0301(gabT-2)
            PSB: Psyr_0090 Psyr_0146
            PSP: PSPPH_0095(gabT1) PSPPH_5040(gabT3)
            PFL: PFL_0186(gabT)
            PFO: Pfl_0188
            PEN: PSEEN0191(gabT)
            PAR: Psyc_0809(gabT)
            PCR: Pcryo_0819
            ACI: ACIAD3446(gabT)
            SON: SO_1276(gabT)
            SDN: Sden_0910
            SFR: Sfri_3003
            SLO: Shew_3172
            SSE: Ssed_3928
            SHE: Shewmr4_2912
            SHM: Shewmr7_2994
            SHN: Shewana3_3091
            CPS: CPS_4664(gabT)
            PIN: Ping_1889
            AHA: AHA_3002(gabT)
            CVI: CV_3926(goaG)
            RSO: RSc0029(goaG)
            REU: Reut_B5663
            RME: Rmet_1618
            BMA: BMAA1480(gabT)
            BPS: BPSS0281(gabT)
            BPM: BURPS1710b_A1822(gabT)
            BTE: BTH_II2119(gabT)
            BPE: BP2298
            BPA: BPP2431
            BBR: BB1880
            RFR: Rfer_0592
            POL: Bpro_2912
            DDE: Dde_0417
            MLO: mlr5521
            SME: SMb21186(gabT)
            BRA: BRADO3420(gabT)
            BBT: BBta_4286(gabT)
            RPA: RPA2323(goaT)
            RPB: RPB_3137
            RPC: RPC_3494
            SIL: SPOA0274(gabT)
            SIT: TM1040_3262
            RDE: RD1_0839(gabT)
            BAN: BA0325(gabT)
            BAR: GBAA0325(gabT)
            BAA: BA_0895
            BAT: BAS0310
            BCA: BCE_0354(gabT)
            BCZ: BCZK0297(gabT)
            BTL: BALH_0317(gabT)
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.22
            ExPASy - ENZYME nomenclature database: 2.6.1.22
            ExplorEnz - The Enzyme Database: 2.6.1.22
            ERGO genome analysis and discovery system: 2.6.1.22
            BRENDA, the Enzyme Database: 2.6.1.22
            CAS: 9031-95-2
///
ENTRY       EC 2.6.1.23                 Enzyme
NAME        4-hydroxyglutamate transaminase;
            4-hydroxyglutamate aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     4-hydroxy-L-glutamate:2-oxoglutarate aminotransferase
REACTION    4-hydroxy-L-glutamate + 2-oxoglutarate = 4-hydroxy-2-oxoglutarate +
            L-glutamate [RN:R03266]
ALL_REAC    R03266 > R05052
SUBSTRATE   4-hydroxy-L-glutamate [CPD:C03079];
            2-oxoglutarate [CPD:C00026]
PRODUCT     4-hydroxy-2-oxoglutarate [CPD:C01127];
            L-glutamate [CPD:C00025]
COMMENT     Oxaloacetate can replace 2-oxoglutarate. This enzyme may be
            identical with EC 2.6.1.1 aspartate transaminase.
REFERENCE   1  [PMID:13948827]
  AUTHORS   GOLDSTONE A, ADAMS E.
  TITLE     Metabolism of gamma-hydroxyglutamic acid. I. Conversion to
            alpha-hydroxy-gamma-ketoglutarate by purified glutamic-aspartic
            transaminase to rat liver.
  JOURNAL   J. Biol. Chem. 237 (1962) 3476-85.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:14089443]
  AUTHORS   KURATOMI K, FUKUNAGA K, KOBAYASHI Y.
  TITLE     THE METABOLISM OF GAMMA-HYDROXYGLUTAMATE IN RAT  LIVER. II. A
            TRANSAMINASE CONCERNED IN GAMMA-HYDROXYGLUTAMATE METABOLISM.
  JOURNAL   Biochim. Biophys. Acta. 78 (1963) 629-36.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00330  Arginine and proline metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.23
            ExPASy - ENZYME nomenclature database: 2.6.1.23
            ExplorEnz - The Enzyme Database: 2.6.1.23
            ERGO genome analysis and discovery system: 2.6.1.23
            BRENDA, the Enzyme Database: 2.6.1.23
            CAS: 37277-86-4
///
ENTRY       EC 2.6.1.24                 Enzyme
NAME        diiodotyrosine transaminase;
            diiodotyrosine aminotransferase;
            halogenated tyrosine aminotransferase;
            halogenated tyrosine transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     3,5-diiodo-L-tyrosine:2-oxoglutarate aminotransferase
REACTION    3,5-diiodo-L-tyrosine + 2-oxoglutarate =
            4-hydroxy-3,5-diiodophenylpyruvate + L-glutamate [RN:R03207]
ALL_REAC    R03207
SUBSTRATE   3,5-diiodo-L-tyrosine [CPD:C01060];
            2-oxoglutarate [CPD:C00026]
PRODUCT     4-hydroxy-3,5-diiodophenylpyruvate;
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also acts on 3,5-dichloro-,
            3,5-dibromo- and 3-iodo-L-tyrosine, thyroxine and triiodothyronine.
REFERENCE   1  [PMID:4381052]
  AUTHORS   Nakano M.
  TITLE     Purification and properties of halogenated tyrosine and thyroid
            hormone transaminase from rat kidney mitochondria.
  JOURNAL   J. Biol. Chem. 242 (1967) 73-81.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Nakano, M. and Danowski, T.S.
  TITLE     Thyroid-hormone transaminase and oxidase in rat-kidney mitochondria.
  JOURNAL   Biochim. Biophys. Acta 85 (1964) 18-28.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.24
            ExPASy - ENZYME nomenclature database: 2.6.1.24
            ExplorEnz - The Enzyme Database: 2.6.1.24
            ERGO genome analysis and discovery system: 2.6.1.24
            BRENDA, the Enzyme Database: 2.6.1.24
            CAS: 9033-18-5
///
ENTRY       EC 2.6.1.25       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
COMMENT     Deleted entry: thyroxine transaminase. Now included with EC 2.6.1.24
            diiodotyrosine transaminase (EC 2.6.1.25 created 1972, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.25
            ExPASy - ENZYME nomenclature database: 2.6.1.25
            ExplorEnz - The Enzyme Database: 2.6.1.25
            ERGO genome analysis and discovery system: 2.6.1.25
            BRENDA, the Enzyme Database: 2.6.1.25
///
ENTRY       EC 2.6.1.26                 Enzyme
NAME        thyroid-hormone transaminase;
            3,5-dinitrotyrosine transaminase;
            thyroid hormone aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-3,5,3'-triiodothyronine:2-oxoglutarate aminotransferase
REACTION    L-3,5,3'-triiodothyronine + 2-oxoglutarate =
            3-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]-2-oxopropanoate +
            L-glutamate [RN:R03952]
ALL_REAC    R03952
SUBSTRATE   L-3,5,3'-triiodothyronine [CPD:C02465];
            2-oxoglutarate [CPD:C00026]
PRODUCT     3-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]-2-oxopropanoate
            [CPD:C03832];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Acts on monoiodotyrosine,
            diiodotyrosine, triiodothyronine, thyroxine and dinitrotyrosine
            (unlike EC 2.6.1.24 diiodotyrosine transaminase, which does not act
            on dinitrotyrosine). Pyruvate or oxaloacetate can act as acceptors.
REFERENCE   1  [PMID:4686924]
  AUTHORS   Soffer RL, Hechtman P, Savage M.
  TITLE     L-Triiodothyronine aminotransferase.
  JOURNAL   J. Biol. Chem. 248 (1973) 1224-30.
  ORGANISM  rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.26
            ExPASy - ENZYME nomenclature database: 2.6.1.26
            ExplorEnz - The Enzyme Database: 2.6.1.26
            ERGO genome analysis and discovery system: 2.6.1.26
            BRENDA, the Enzyme Database: 2.6.1.26
            CAS: 51004-29-6
///
ENTRY       EC 2.6.1.27                 Enzyme
NAME        tryptophan transaminase;
            L-phenylalanine-2-oxoglutarate aminotransferase;
            tryptophan aminotransferase;
            5-hydroxytryptophan-ketoglutaric transaminase;
            hydroxytryptophan aminotransferase;
            L-tryptophan aminotransferase;
            L-tryptophan transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-tryptophan:2-oxoglutarate aminotransferase
REACTION    L-tryptophan + 2-oxoglutarate = (indol-3-yl)pyruvate + L-glutamate
            [RN:R00684]
ALL_REAC    R00684;
            (other) R02700 R04913
SUBSTRATE   L-tryptophan [CPD:C00078];
            2-oxoglutarate [CPD:C00026]
PRODUCT     (indol-3-yl)pyruvate [CPD:C00331];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also acts on 5-hydroxytryptophan and,
            to a lesser extent, on the phenyl amino acids.
REFERENCE   1  [PMID:5722279]
  AUTHORS   George H, Gabay S.
  TITLE     Brain aromatic aminotransferase. I. Purification and some properties
            of pig brain L-phenylalanine-2-oxoglutarate aminotransferase.
  JOURNAL   Biochim. Biophys. Acta. 167 (1968) 555-66.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:5697992]
  AUTHORS   O'Neil SR, DeMoss RD.
  TITLE     Tryptophan transaminase from Clostridium sporogenes.
  JOURNAL   Arch. Biochem. Biophys. 127 (1968) 361-9.
  ORGANISM  Clostridium sporogenes
REFERENCE   3
  AUTHORS   Tangen, O., Fonnum, F. and Haavaldsen, R.
  TITLE     Separation and purification of aromatic amino acid transaminases
            from rat brain.
  JOURNAL   Biochim. Biophys. Acta 96 (1965) 82-90.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00380  Tryptophan metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.27
            ExPASy - ENZYME nomenclature database: 2.6.1.27
            ExplorEnz - The Enzyme Database: 2.6.1.27
            ERGO genome analysis and discovery system: 2.6.1.27
            BRENDA, the Enzyme Database: 2.6.1.27
            CAS: 9022-98-4
///
ENTRY       EC 2.6.1.28                 Enzyme
NAME        tryptophan---phenylpyruvate transaminase;
            L-tryptophan-alpha-ketoisocaproate aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-tryptophan:phenylpyruvate aminotransferase
REACTION    L-tryptophan + phenylpyruvate = (indol-3-yl)pyruvate +
            L-phenylalanine [RN:R01376]
ALL_REAC    R01376
SUBSTRATE   L-tryptophan [CPD:C00078];
            phenylpyruvate [CPD:C00166]
PRODUCT     (indol-3-yl)pyruvate [CPD:C00331];
            L-phenylalanine [CPD:C00079]
COMMENT     Valine, leucine and isoleucine can replace tryptophan as amino
            donor.
REFERENCE   1
  AUTHORS   Koide, Y., Honma, M. and Shimomura, T.
  TITLE     L-Tryptophan-alpha-ketoisocaproate aminotransferase from Pseudomonas
            sp.
  JOURNAL   Agric. Biol. Chem. 44 (1980) 2013-2019.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:5837443]
  AUTHORS   Sukanya NK, Vaidyanathan CS.
  TITLE     Aminotransferases of Agrobacterium tumefaciens. Transamination
            between tryptophan and phenylpyruvate.
  JOURNAL   Biochem. J. 92 (1964) 594-8.
  ORGANISM  Agrobacterium tumefaciens
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.28
            ExPASy - ENZYME nomenclature database: 2.6.1.28
            ExplorEnz - The Enzyme Database: 2.6.1.28
            ERGO genome analysis and discovery system: 2.6.1.28
            BRENDA, the Enzyme Database: 2.6.1.28
            CAS: 37277-87-5
///
ENTRY       EC 2.6.1.29                 Enzyme
NAME        diamine transaminase;
            amine transaminase;
            amine-ketoacid transaminase;
            diamine aminotransferase;
            diamine-ketoglutaric transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     diamine:2-oxoglutarate aminotransferase
REACTION    an alpha,omega-diamine + 2-oxoglutarate = an omega-aminoaldehyde +
            L-glutamate [RN:R07275]
ALL_REAC    R07275 > R01155
SUBSTRATE   alpha,omega-diamine [CPD:C02896];
            2-oxoglutarate [CPD:C00026]
PRODUCT     omega-aminoaldehyde [CPD:C02903];
            L-glutamate [CPD:C00025]
REFERENCE   1
  AUTHORS   Kim, K.
  TITLE     Purification and properties of a diamine alpha-ketoglutarate
            transaminase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 239 (1964) 783-786.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.29
            ExPASy - ENZYME nomenclature database: 2.6.1.29
            ExplorEnz - The Enzyme Database: 2.6.1.29
            ERGO genome analysis and discovery system: 2.6.1.29
            BRENDA, the Enzyme Database: 2.6.1.29
            CAS: 9031-83-8
///
ENTRY       EC 2.6.1.30                 Enzyme
NAME        pyridoxamine---pyruvate transaminase;
            pyridoxamine-pyruvic transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     pyridoxamine:pyruvate aminotransferase
REACTION    pyridoxamine + pyruvate = pyridoxal + L-alanine [RN:R01712]
ALL_REAC    R01712
SUBSTRATE   pyridoxamine [CPD:C00534];
            pyruvate [CPD:C00022]
PRODUCT     pyridoxal [CPD:C00250];
            L-alanine [CPD:C00041]
REFERENCE   1
  AUTHORS   Wada, H. and Snell, E.E.
  TITLE     Enzymatic transamination of pyridoxamine. II. Crystalline
            pyridoxamine-pyruvate transaminase.
  JOURNAL   J. Biol. Chem. 237 (1962) 133-137.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00750  Vitamin B6 metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.30
            ExPASy - ENZYME nomenclature database: 2.6.1.30
            ExplorEnz - The Enzyme Database: 2.6.1.30
            ERGO genome analysis and discovery system: 2.6.1.30
            BRENDA, the Enzyme Database: 2.6.1.30
            CAS: 9023-38-5
///
ENTRY       EC 2.6.1.31                 Enzyme
NAME        pyridoxamine---oxaloacetate transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     pyridoxamine:oxaloacetate aminotransferase
REACTION    pyridoxamine + oxaloacetate = pyridoxal + L-aspartate [RN:R01713]
ALL_REAC    R01713
SUBSTRATE   pyridoxamine [CPD:C00534];
            oxaloacetate [CPD:C00036]
PRODUCT     pyridoxal [CPD:C00250];
            L-aspartate [CPD:C00049]
REFERENCE   1
  AUTHORS   Wada, H. and Snell, E.E.
  TITLE     Enzymatic transamination of pyridoxamine. I. With oxaloacetate and
            alpha-ketoglutarate.
  JOURNAL   J. Biol. Chem. 237 (1962) 127-132.
  ORGANISM  rabbit, Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Wu, H.L.C. and Mason, M.
  TITLE     Pyridoxamine-oxaloacetic transaminase of rat kidney.
  JOURNAL   J. Biol. Chem. 239 (1964) 1492-1497.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00750  Vitamin B6 metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.31
            ExPASy - ENZYME nomenclature database: 2.6.1.31
            ExplorEnz - The Enzyme Database: 2.6.1.31
            ERGO genome analysis and discovery system: 2.6.1.31
            BRENDA, the Enzyme Database: 2.6.1.31
            CAS: 37277-88-6
///
ENTRY       EC 2.6.1.32                 Enzyme
NAME        valine---3-methyl-2-oxovalerate transaminase;
            valine---isoleucine transaminase;
            valine-3-methyl-2-oxovalerate aminotransferase;
            alanine-valine transaminase;
            valine-2-keto-methylvalerate aminotransferase;
            valine-isoleucine aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-valine:(S)-3-methyl-2-oxopentanoate aminotransferase
REACTION    L-valine + (S)-3-methyl-2-oxopentanoate = 3-methyl-2-oxobutanoate +
            L-isoleucine [RN:R02200]
ALL_REAC    R02200
SUBSTRATE   L-valine [CPD:C00183];
            (S)-3-methyl-2-oxopentanoate [CPD:C00671]
PRODUCT     3-methyl-2-oxobutanoate [CPD:C00141];
            L-isoleucine [CPD:C00407]
REFERENCE   1
  AUTHORS   Kagan, Z.S., Dronov, A.S. and Kretovich, V.L.
  TITLE     [Some properties of valine-isoleucine- and
            valine-glutamate-aminotransferases of pea sprouts.].
  JOURNAL   Dokl. Akad. Nauk S.S.S.R. 179 (1968) 1236-1239.
  ORGANISM  Pisum sativum
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.32
            ExPASy - ENZYME nomenclature database: 2.6.1.32
            ExplorEnz - The Enzyme Database: 2.6.1.32
            ERGO genome analysis and discovery system: 2.6.1.32
            BRENDA, the Enzyme Database: 2.6.1.32
            CAS: 9023-14-7
///
ENTRY       EC 2.6.1.33                 Enzyme
NAME        dTDP-4-amino-4,6-dideoxy-D-glucose transaminase;
            thymidine diphospho-4-amino-4,6-dideoxyglucose aminotransferase;
            thymidine diphospho-4-amino-6-deoxyglucose aminotransferase;
            thymidine diphospho-4-keto-6-deoxy-D-glucose transaminase;
            thymidine diphospho-4-keto-6-deoxy-D-glucose-glutamic transaminase;
            TDP-4-keto-6-deoxy-D-glucose transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     dTDP-4-amino-4,6-dideoxy-D-glucose:2-oxoglutarate aminotransferase
REACTION    dTDP-4-amino-4,6-dideoxy-D-glucose + 2-oxoglutarate =
            dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate [RN:R02773]
ALL_REAC    R02773;
            (other) R02772
SUBSTRATE   dTDP-4-amino-4,6-dideoxy-D-glucose [CPD:C04268];
            2-oxoglutarate [CPD:C00026]
PRODUCT     dTDP-4-dehydro-6-deoxy-D-glucose [CPD:C11907];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:5332731]
  AUTHORS   Matsuhashi M, Strominger JL.
  TITLE     Thymidine diphosphate 4-acetamido-2,6-dideoxyhexoses. 3.
            Purification and properties of thymidine diphosphate
            4-keto-6-deoxy-D-glucose transaminase from Escherichia coli strain
            B.
  JOURNAL   J. Biol. Chem. 241 (1966) 4738-44.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.33
            ExPASy - ENZYME nomenclature database: 2.6.1.33
            ExplorEnz - The Enzyme Database: 2.6.1.33
            ERGO genome analysis and discovery system: 2.6.1.33
            BRENDA, the Enzyme Database: 2.6.1.33
            CAS: 9023-19-2
///
ENTRY       EC 2.6.1.34                 Enzyme
NAME        UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose transaminase;
            uridine diphospho-4-amino-2-acetamido-2,4,6-trideoxyglucose
            aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose:2-oxoglutarate
            aminotransferase
REACTION    UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose + 2-oxoglutarate =
            UDP-2-acetamido-4-dehydro-2,6-dideoxyglucose + L-glutamate
            [RN:R04529]
ALL_REAC    R04529
SUBSTRATE   UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose [CPD:C04630];
            2-oxoglutarate [CPD:C00026]
PRODUCT     UDP-2-acetamido-4-dehydro-2,6-dideoxyglucose [CPD:C04613];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:4381351]
  AUTHORS   Distler J, Kaufman B, Roseman S.
  TITLE     Enzymic synthesis of a diamino sugar nucleotide by extracts of type
            XIV Diplococcus pneumoniae.
  JOURNAL   Arch. Biochem. Biophys. 116 (1966) 466-78.
  ORGANISM  Diplococcus pneumoniae
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.34
            ExPASy - ENZYME nomenclature database: 2.6.1.34
            ExplorEnz - The Enzyme Database: 2.6.1.34
            ERGO genome analysis and discovery system: 2.6.1.34
            BRENDA, the Enzyme Database: 2.6.1.34
            CAS: 37277-89-7
///
ENTRY       EC 2.6.1.35                 Enzyme
NAME        glycine---oxaloacetate transaminase;
            glycine-oxalacetate aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     glycine:oxaloacetate aminotransferase
REACTION    glycine + oxaloacetate = glyoxylate + L-aspartate [RN:R00373]
ALL_REAC    R00373
SUBSTRATE   glycine [CPD:C00037];
            oxaloacetate [CPD:C00036]
PRODUCT     glyoxylate [CPD:C00048];
            L-aspartate [CPD:C00049]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1
  AUTHORS   Gibbs, R.G. and Morris, J.G.
  TITLE     Formation of glycine from glyoxylate in Micrococcus denitrificans.
  JOURNAL   Biochem. J. 99 (1966) 27.
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.35
            ExPASy - ENZYME nomenclature database: 2.6.1.35
            ExplorEnz - The Enzyme Database: 2.6.1.35
            ERGO genome analysis and discovery system: 2.6.1.35
            BRENDA, the Enzyme Database: 2.6.1.35
            CAS: 37277-90-0
///
ENTRY       EC 2.6.1.36                 Enzyme
NAME        L-lysine 6-transaminase;
            lysine 6-aminotransferase;
            lysine epsilon-aminotransferase;
            lysine epsilon-transaminase;
            lysine:2-ketoglutarate 6-aminotransferase;
            L-lysine-alpha-ketoglutarate aminotransferase;
            L-lysine-alpha-ketoglutarate 6-aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-lysine:2-oxoglutarate 6-aminotransferase
REACTION    L-lysine + 2-oxoglutarate = 2-aminoadipate 6-semialdehyde +
            L-glutamate [RN:R00457]
ALL_REAC    R00457
SUBSTRATE   L-lysine [CPD:C00047];
            2-oxoglutarate [CPD:C00026]
PRODUCT     2-aminoadipate 6-semialdehyde [CPD:C04076];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. The product (allysine) is converted
            into the intramolecularly dehydrated form, 1-piperideine
            6-carboxylate.
REFERENCE   1  [PMID:5722275]
  AUTHORS   Soda K, Misono H, Yamamoto T.
  TITLE     L-Lysine:alpha-ketoglutarate aminotransferase. I. Identification of
            a product, delta-1-piperideine-6-carboxylic acid.
  JOURNAL   Biochemistry. 7 (1968) 4102-9.
  ORGANISM  Flavobacterium fuscum
REFERENCE   2  [PMID:5722276]
  AUTHORS   Soda K, Misono H.
  TITLE     L-Lysine:alpha-ketoglutarate aminotransferase. II. Purification,
            crystallization, and properties.
  JOURNAL   Biochemistry. 7 (1968) 4110-9.
  ORGANISM  Flavobacterium fuscum, Achrornobacter liquidurn, Flavobacterium
            flavescens
PATHWAY     PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K03918  L-lysine 6-transaminase
GENES       PCA: Pcar_2442
            DPS: DP2333
            MTU: Rv3290c(lat)
            MTC: MT3389(lat)
            MBO: Mb3318c(lat)
            MBB: BCG_3319c(lat) BCG_3354c(lat')
            MPA: MAP3410c(lat)
            MAV: MAV_4262
            MSM: MSMEG_1764
            NFA: nfa9840
            RHA: RHA1_ro06277(lat)
            FRA: Francci3_2873
            FAL: FRAAL4414(lat)
            SEN: SACE_0784(lat)
            SRU: SRU_0799
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.36
            ExPASy - ENZYME nomenclature database: 2.6.1.36
            ExplorEnz - The Enzyme Database: 2.6.1.36
            ERGO genome analysis and discovery system: 2.6.1.36
            BRENDA, the Enzyme Database: 2.6.1.36
            CAS: 9054-68-6
///
ENTRY       EC 2.6.1.37                 Enzyme
NAME        2-aminoethylphosphonate---pyruvate transaminase;
            (2-aminoethyl)phosphonate transaminase;
            (2-aminoethyl)phosphonate aminotransferase;
            (2-aminoethyl)phosphonic acid aminotransferase;
            2-aminoethylphosphonate-pyruvate aminotransferase;
            2-aminoethylphosphonate aminotransferase;
            2-aminoethylphosphonate transaminase;
            AEP transaminase;
            AEPT
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     (2-aminoethyl)phosphonate:pyruvate aminotransferase
REACTION    (2-aminoethyl)phosphonate + pyruvate = 2-phosphonoacetaldehyde +
            L-alanine [RN:R04152]
ALL_REAC    R04152
SUBSTRATE   (2-aminoethyl)phosphonate [CPD:C03557];
            pyruvate [CPD:C00022]
PRODUCT     2-phosphonoacetaldehyde [CPD:C03167];
            L-alanine [CPD:C00041]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. 2-Aminoethylarsonate can replace
            2-aminoethylphosphonate as a substrate.
REFERENCE   1  [PMID:4982500]
  AUTHORS   La Nauze JM, Rosenberg H.
  TITLE     The identification of 2-phosphonoacetaldehyde as an intermediate in
            the degradation of 2-aminoethylphosphonate by Bacillus cereus.
  JOURNAL   Biochim. Biophys. Acta. 165 (1968) 438-47.
  ORGANISM  Bacillus cereus
REFERENCE   2  [PMID:6406228]
  AUTHORS   Dumora C, Lacoste AM, Cassaigne A.
  TITLE     Purification and properties of 2-aminoethylphosphonate:pyruvate
            aminotransferase from Pseudomonas aeruginosa.
  JOURNAL   Eur. J. Biochem. 133 (1983) 119-25.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   3  [PMID:8394813]
  AUTHORS   Lacoste AM, Dumora C, Balas L, Hammerschmidt F, Vercauteren J.
  TITLE     Stereochemistry of the reaction catalysed by 2-aminoethylphosphonate
            aminotransferase. A 1H-NMR study.
  JOURNAL   Eur. J. Biochem. 215 (1993) 841-4.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   4  [PMID:1527499]
  AUTHORS   Lacoste AM, Dumora C, Ali BR, Neuzil E, Dixon HB.
  TITLE     Utilization of 2-aminoethylarsonic acid in Pseudomonas aeruginosa.
  JOURNAL   J. Gen. Microbiol. 138 (1992) 1283-7.
  ORGANISM  Pseudomonas aeruginosa
PATHWAY     PATH: map00440  Aminophosphonate metabolism
ORTHOLOGY   KO: K03430  2-aminoethylphosphonate-pyruvate transaminase
            KO: K09469  2-aminoethylphosphonate-pyruvate transaminase
GENES       STY: STY0470(phnW)
            STT: t2432(phnW)
            SPT: SPA2292(phnW)
            STM: STM0431(phnW)
            XOO: XOO1391
            XOM: XOO_1279(XOO1279)
            VCH: VCA0604
            VVU: VV2_1664
            VVY: VVA0476
            VPA: VPA0235
            PAE: PA1310(phnW)
            PAU: PA14_47300(phnW)
            PAP: PSPA7_4081(phnW)
            PPU: PP_2209(phnW)
            PFL: PFL_3965(phnW)
            PFO: Pfl_3683
            PEN: PSEEN3553(phnW)
            SDN: Sden_1165
            NOC: Noc_1315
            HCH: HCH_03085
            AHA: AHA_1938(phnW)
            REU: Reut_B3718 Reut_B5871
            RME: Rmet_1810
            BMA: BMAA0852 BMAA1770(phnW)
            BMV: BMASAVP1_0760(phnW)
            BML: BMA10299_1053(phnW)
            BMN: BMA10247_A2028(phnW)
            BCN: Bcen_3066
            BCH: Bcen2424_5301
            BAM: Bamb_4662
            BPS: BPSS0343 BPSS0507
            BPM: BURPS1710b_A1899(phnW) BURPS1710b_A2063(phnW)
            BPL: BURPS1106A_A0485(phnW) BURPS1106A_A0689(phnW)
            BPD: BURPS668_A0582(phnW) BURPS668_A0778(phnW)
            BTE: BTH_II1910 BTH_II2055(phnW)
            POL: Bpro_3216 Bpro_4697
            SFU: Sfum_2895
            SME: SMb21537
            BJA: blr2077
            BAN: BA1341
            BAA: BA_1866
            BAT: BAS1240
            BCE: BC1327
            BCA: BCE_1440
            BCZ: BCZK1218(phnW)
            BTK: BT9727_1216(phnW)
            BTL: BALH_1190(phnW)
            LPL: lp_0710(phnW)
            CTC: CTC01700
            BTH: BT_1718
            BFR: BF1834 BF3695
            BFS: BF1899(aepZ) BF3487
STRUCTURES  PDB: 1M32  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.37
            ExPASy - ENZYME nomenclature database: 2.6.1.37
            ExplorEnz - The Enzyme Database: 2.6.1.37
            ERGO genome analysis and discovery system: 2.6.1.37
            BRENDA, the Enzyme Database: 2.6.1.37
            CAS: 37277-91-1
///
ENTRY       EC 2.6.1.38                 Enzyme
NAME        histidine transaminase;
            histidine aminotransferase;
            histidine-2-oxoglutarate aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-histidine:2-oxoglutarate aminotransferase
REACTION    L-histidine + 2-oxoglutarate = (imidazol-5-yl)pyruvate + L-glutamate
            [RN:R01161]
ALL_REAC    R01161
SUBSTRATE   L-histidine [CPD:C00135];
            2-oxoglutarate [CPD:C00026]
PRODUCT     (imidazol-5-yl)pyruvate;
            L-glutamate [CPD:C00025]
REFERENCE   1  [PMID:4303364]
  AUTHORS   Coote JG, Hassall H.
  TITLE     The role of imidazol-5-yl-lactate-nicotinamide-adenine dinucleotide
            phosphate oxidoreductase and histidine-2-oxoglutarate
            aminotransferase in the degradation of imidazol-5-yl-lactate by
            Pseudomonas acidovorans.
  JOURNAL   Biochem. J. 111 (1969) 237-9.
  ORGANISM  Pseudomonas acidovorans
REFERENCE   2
  AUTHORS   Wickremasinghe, R., Hedegaard, J. and Roche, J.
  TITLE     Degradation de la L-histidine chez Escherichia coli B: formation de
            l'acide imidazolepyruvique par une histidine-transaminase.
  JOURNAL   C.R. Soc. Biol. 161 (1967) 1891-1896.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00340  Histidine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.38
            ExPASy - ENZYME nomenclature database: 2.6.1.38
            ExplorEnz - The Enzyme Database: 2.6.1.38
            ERGO genome analysis and discovery system: 2.6.1.38
            BRENDA, the Enzyme Database: 2.6.1.38
            CAS: 37277-92-2
///
ENTRY       EC 2.6.1.39                 Enzyme
NAME        2-aminoadipate transaminase;
            alpha-aminoadipate aminotransferase;
            2-aminoadipate aminotransferase;
            2-aminoadipic aminotransferase;
            glutamic-ketoadipic transaminase;
            glutamate-alpha-ketoadipate transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-2-aminoadipate:2-oxoglutarate aminotransferase
REACTION    L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate
            [RN:R01939]
ALL_REAC    R01939;
            (other) R04029
SUBSTRATE   L-2-aminoadipate [CPD:C00956];
            2-oxoglutarate [CPD:C00026]
PRODUCT     2-oxoadipate [CPD:C00322];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:5792664]
  AUTHORS   Matsuda M, Ogur M.
  TITLE     Separation and specificity of the yeast glutamate-alpha-ketoadipate
            transaminase.
  JOURNAL   J. Biol. Chem. 244 (1969) 3352-8.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00300  Lysine biosynthesis
            PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K00825  2-aminoadipate transaminase
GENES       HSA: 51166(AADAT)
            PTR: 461601(AADAT)
            MMU: 23923(Aadat)
            XLA: 398787(MGC68542)
            XTR: 496662(LOC496662)
            UMA: UM01804.1 UM03538.1
            DDI: DDBDRAFT_0187583
            BUR: Bcep18194_A5690 Bcep18194_B0281 Bcep18194_B1266
                 Bcep18194_B1330 Bcep18194_B1740 Bcep18194_B1880
                 Bcep18194_B1990 Bcep18194_B2202 Bcep18194_B2654
                 Bcep18194_B3074 Bcep18194_C7006 Bcep18194_C7710
            BAM: Bamb_2387
            RLE: RL1422
            BRA: BRADO2132
            BBT: BBta_2449
            NWI: Nwi_0881
            RRU: Rru_A1143 Rru_A1925 Rru_A3004
            SEN: SACE_6850
            AVA: Ava_1933
STRUCTURES  PDB: 2DTV  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.39
            ExPASy - ENZYME nomenclature database: 2.6.1.39
            ExplorEnz - The Enzyme Database: 2.6.1.39
            ERGO genome analysis and discovery system: 2.6.1.39
            BRENDA, the Enzyme Database: 2.6.1.39
            CAS: 9033-00-5
///
ENTRY       EC 2.6.1.40                 Enzyme
NAME        (R)-3-amino-2-methylpropionate---pyruvate transaminase;
            D-3-aminoisobutyrate---pyruvate transaminase;
            beta-aminoisobutyrate-pyruvate aminotransferase;
            D-3-aminoisobutyrate-pyruvate aminotransferase;
            D-3-aminoisobutyrate-pyruvate transaminase;
            (R)-3-amino-2-methylpropionate transaminase;
            D-beta-aminoisobutyrate:pyruvate aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     (R)-3-amino-2-methylpropanoate:pyruvate aminotransferase
REACTION    (R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-oxopropanoate
            + L-alanine [RN:R02050]
ALL_REAC    R02050;
            (other) R02048
SUBSTRATE   (R)-3-amino-2-methylpropanoate [CPD:C01205];
            pyruvate [CPD:C00022]
PRODUCT     2-methyl-3-oxopropanoate [CPD:C00349];
            L-alanine [CPD:C00041]
COMMENT     The two enantiomers of the 2-methyl-3-oxopropanoate formed by the
            enzyme interconvert by enolization, so that this enzyme, together
            with EC 2.6.1.22, (S)-3-amino-2-methylpropionate transaminase,
            provide a route for interconversion of the enantiomers of
            3-amino-2-methylpropanoate.
REFERENCE   1  [PMID:5773299]
  AUTHORS   Kakimoto Y, Taniguchi K, Sano I.
  TITLE     D-beta-aminoisobutyrate:pyruvate aminotransferase in mammalian liver
            and excretion of beta-aminoisobutyrate by man.
  JOURNAL   J. Biol. Chem. 244 (1969) 335-40.
  ORGANISM  rat [GN:rno], guinea pig, pig [GN:ssc], human [GN:hsa]
REFERENCE   2  [PMID:10989446]
  AUTHORS   Tamaki N, Sakata SF, Matsuda K.
  TITLE     Purification, properties, and sequencing of aminoisobutyrate
            aminotransferases from rat liver.
  JOURNAL   Methods. Enzymol. 324 (2000) 376-89.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K08072  (R)-3-amino-2-methylpropionate-pyruvate transaminase
GENES       HSA: 64902(AGXT2)
            PTR: 471573(AGXT2)
            MMU: 268782(Agxt2)
            RNO: 83784(Agxt2)
            CFA: 612589(AGXT2)
            GGA: 431666(AGXT2)
            SPU: 594821(LOC594821)
            DME: Dmel_CG11241
            CEL: T09B4.8(aminotransferase)
            ATH: AT4G39660(AGT2)
            OSA: 4331779
            RRU: Rru_A3009
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.40
            ExPASy - ENZYME nomenclature database: 2.6.1.40
            ExplorEnz - The Enzyme Database: 2.6.1.40
            ERGO genome analysis and discovery system: 2.6.1.40
            BRENDA, the Enzyme Database: 2.6.1.40
            CAS: 37279-00-8
///
ENTRY       EC 2.6.1.41                 Enzyme
NAME        D-methionine---pyruvate transaminase;
            D-methionine transaminase;
            D-methionine aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     D-methionine:pyruvate aminotransferase
REACTION    D-methionine + pyruvate = 4-methylthio-2-oxobutanoate + L-alanine
            [RN:R03001]
ALL_REAC    R03001;
            (other) R01344
SUBSTRATE   D-methionine [CPD:C00855];
            pyruvate [CPD:C00022]
PRODUCT     4-methylthio-2-oxobutanoate [CPD:C01180];
            L-alanine [CPD:C00041]
COMMENT     Oxaloacetate can replace pyruvate.
REFERENCE   1  [PMID:5357015]
  AUTHORS   Mapson LW, March JF, Wardale DA.
  TITLE     Biosynthesis of ethylene. 4-methylmercapto-2-oxobutyric acid: an
            intermediate in the formation from methionine.
  JOURNAL   Biochem. J. 115 (1969) 653-61.
  ORGANISM  cauliflower
PATHWAY     PATH: map00473  D-Alanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.41
            ExPASy - ENZYME nomenclature database: 2.6.1.41
            ExplorEnz - The Enzyme Database: 2.6.1.41
            ERGO genome analysis and discovery system: 2.6.1.41
            BRENDA, the Enzyme Database: 2.6.1.41
            CAS: 37277-93-3
///
ENTRY       EC 2.6.1.42                 Enzyme
NAME        branched-chain-amino-acid transaminase;
            transaminase B;
            branched-chain amino acid aminotransferase;
            branched-chain amino acid-glutamate transaminase;
            branched-chain aminotransferase;
            L-branched chain amino acid aminotransferase;
            glutamate-branched-chain amino acid transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     branched-chain-amino-acid:2-oxoglutarate aminotransferase
REACTION    L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
            [RN:R01090]
ALL_REAC    R01090;
            (other) R01214 R02199
SUBSTRATE   L-leucine [CPD:C00123];
            2-oxoglutarate [CPD:C00026]
PRODUCT     4-methyl-2-oxopentanoate [CPD:C00233];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     Also acts on L-isoleucine and L-valine, and thereby differs from EC
            2.6.1.6, leucine transaminase, which does not. It also differs from
            EC 2.6.1.66, valine---pyruvate transaminase.
REFERENCE   1  [PMID:4968655]
  AUTHORS   Aki K, Ogawa K, Ichihara A.
  TITLE     Transaminases of branched chain amino acids. IV. Purification and
            properties of two enzymes from rat liver.
  JOURNAL   Biochim. Biophys. Acta. 159 (1968) 276-84.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4979711]
  AUTHORS   Aki K, Yokojima A, Ichihara A.
  TITLE     Transaminase of branched chain amino acids. VI. Purification and
            properties of the hog brain enzyme.
  JOURNAL   J. Biochem. (Tokyo). 65 (1969) 539-44.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:5943594]
  AUTHORS   Ichihara A, Koyama E.
  TITLE     Transaminase of branched chain amino acids. I. Branched chain amino
            acids-alpha-ketoglutarate transaminase.
  JOURNAL   J. Biochem. (Tokyo). 59 (1966) 160-9.
  ORGANISM  rat [GN:rno], pig [GN:ssc]
REFERENCE   4  [PMID:5922965]
  AUTHORS   Taylor RT, Jenkins WT.
  TITLE     Leucine aminotransferase. II. Purification and characterization.
  JOURNAL   J. Biol. Chem. 241 (1966) 4396-405.
  ORGANISM  pig [GN:ssc]
REFERENCE   5  [PMID:13034817]
  AUTHORS   RUDMAN D, MEISTER A.
  TITLE     Transamination in Escherichia coli.
  JOURNAL   J. Biol. Chem. 200 (1953) 591-604.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00290  Valine, leucine and isoleucine biosynthesis
            PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K00826  branched-chain amino acid aminotransferase
GENES       HSA: 586(BCAT1) 587(BCAT2)
            MMU: 12035(Bcat1) 12036(Bcat2)
            RNO: 29592(Bcat1) 64203(Bcat2)
            CFA: 484394(BCAT2) 486633(BCAT1)
            BTA: 281643(BCAT2)
            GGA: 418193(BCAT1)
            XLA: 494683(LOC494683)
            XTR: 448409(bcat1)
            DRE: 337412(bcat1)
            DME: Dmel_CG1673
            CEL: K02A4.1(bcat-1) Y44A6D.5
            ATH: AT1G10070(ATBCAT-2) AT1G50090 AT1G50110 AT3G19710(BCAT4)
                 AT3G49680(ATBCAT-3)
            OSA: 4331322 4332151 4332881 4338203 4339583
            CME: CMN181C CMO144C
            SCE: YHR208W(BAT1) YJR148W(BAT2)
            AGO: AGOS_ADL384W
            PIC: PICST_84005(BAT2)
            CGR: CAGL0M00176g
            SPO: SPBC428.02c(eca39)
            ANI: AN0385.2 AN4323.2 AN7876.2
            AFM: AFUA_1G01680 AFUA_2G10420 AFUA_4G06160
            AOR: AO090005000936 AO090011000044 AO090023000977
            CNE: CNN00980
            UMA: UM00115.1 UM02783.1
            DDI: DDB_0230183(bcaA)
            TET: TTHERM_00765280
            TBR: Tb927.2.4590
            LMA: LmjF27.2030
            EHI: 6.t00097
            ECO: b3770(ilvE)
            ECJ: JW5606(ilvE)
            ECE: Z5281(ilvE)
            ECS: ECs4704
            ECC: c4692(ilvE)
            ECI: UTI89_C4326(ilvE)
            ECP: ECP_3963
            ECV: APECO1_2701(ilvE)
            ECW: EcE24377A_4281(ilvE)
            ECX: EcHS_A3987
            STY: STY3654(ilvE)
            STT: t3395(ilvE)
            SPT: SPA3742(ilvE)
            SEC: SC3808(ilvE)
            STM: STM3903(ilvE)
            YPE: YPO3899(ilvE)
            YPK: y0337(ilvE)
            YPM: YP_3149(ilvE)
            YPA: YPA_0123
            YPN: YPN_0068
            YPP: YPDSF_3511
            YPS: YPTB0136(ilvE)
            YPI: YpsIP31758_0156(ilvE)
            YEN: YE0150(ilvE)
            SFL: SF3845(ilvE)
            SFX: S3914(ilvE)
            SFV: SFV_3732(ilvE)
            SSN: SSON_3941(ilvE)
            SBO: SBO_3781(ilvE)
            SDY: SDY_3978(ilvE)
            ECA: ECA4227(ilvE)
            PLU: plu4683(ilvE)
            SGL: SG2395
            BFL: Bfl591(ilvE)
            BPN: BPEN_612(ilvE)
            HIN: HI1193(ilvE)
            HIT: NTHI1364(ilvE)
            HIP: CGSHiEE_06100
            HIQ: CGSHiGG_09680
            HSO: HS_0494(ilvE)
            PMU: PM0566(ivlE)
            MSU: MS0896(ilvE)
            APL: APL_0072(ilvE)
            ASU: Asuc_1698
            XFA: XF1999
            XFT: PD0810(ilvE)
            XCC: XCC0850(ilvE)
            XCB: XC_3380
            XCV: XCV0958(ilvE)
            XAC: XAC0927(ilvE)
            XOO: XOO3624(ilvE)
            XOM: XOO_3425(XOO3425)
            VCH: VC0029
            VCO: VC0395_A2490(ilvE)
            VVU: VV1_1030
            VVY: VV3242
            VPA: VP3060
            VFI: VF2558
            PPR: PBPRA3594
            PAE: PA5013(ilvE)
            PAU: PA14_66260(ilvE)
            PAP: PSPA7_5748(ilvE)
            PPU: PP_3511(ilvE)
            PPF: Pput_2264
            PST: PSPTO_1332(ilvE)
            PSB: Psyr_1148
            PSP: PSPPH_1218(ilvE)
            PFL: PFL_2530(ilvE)
            PFO: Pfl_3467
            PEN: PSEEN2090(ilvE)
            PAR: Psyc_1216(ilvE)
            PCR: Pcryo_1176
            ACI: ACIAD0597(ilvE)
            SON: SO_0340(ilvE)
            SDN: Sden_0289
            SFR: Sfri_0414
            SAZ: Sama_3299
            SBL: Sbal_4053
            SBM: Shew185_4027
            SLO: Shew_0278 Shew_0291
            SPC: Sputcn32_3649
            SSE: Ssed_4176
            SPL: Spea_0327
            SHE: Shewmr4_3634
            SHM: Shewmr7_0310
            SHN: Shewana3_3830
            SHW: Sputw3181_3790
            ILO: IL1556(ilvE)
            CPS: CPS_4845(ilvE)
            PHA: PSHAa1270(ilvE)
            PAT: Patl_2886
            SDE: Sde_0388 Sde_3057
            PIN: Ping_2596
            MAQ: Maqu_0777
            MCA: MCA2344(ilvE)
            FTU: FTT0251(ilvE)
            FTF: FTF0251(ilvE)
            FTW: FTW_1868(ilvE)
            FTL: FTL_0131
            FTH: FTH_0122(ilvE)
            FTA: FTA_0142(ilvE)
            FTN: FTN_0063(ilvE)
            TCX: Tcr_0534
            NOC: Noc_0136
            AEH: Mlg_2699
            HCH: HCH_01045(ilvE1) HCH_06836(ilvE2)
            CSA: Csal_2919
            ABO: ABO_2301(ilvE)
            MMW: Mmwyl1_1558
            AHA: AHA_4203(ilvE)
            CRP: CRP_172
            RMA: Rmag_0584
            VOK: COSY_0539(ilvE)
            NME: NMB0337
            NMA: NMA2151(ilvE)
            NGO: NGO1665
            CVI: CV_2094(ilvE)
            RSO: RSc0567(ilvE1) RSp1327(ilvE3) RSp1358(ilvE2)
            REU: Reut_B4282
            REH: H16_A0561
            RME: Rmet_0493
            BMA: BMA0293(ilvE)
            BMV: BMASAVP1_A0588(ilvE)
            BML: BMA10299_A2421(ilvE)
            BMN: BMA10247_0034(ilvE)
            BXE: Bxe_A0686 Bxe_B0360
            BUR: Bcep18194_A3841 Bcep18194_A5962
            BCN: Bcen_2020 Bcen_3725
            BCH: Bcen2424_2631 Bcen2424_4643
            BAM: Bamb_2678 Bamb_6410
            BPS: BPSL0793(ilvE) BPSS1810(ilvE)
            BPM: BURPS1710b_0992(ilvE) BURPS1710b_A0893(ilvE)
            BPL: BURPS1106A_0834(ilvE) BURPS1106A_A2457(ilvE)
            BPD: BURPS668_0830(ilvE) BURPS668_A2593(ilvE)
            BTE: BTH_I0660(ilvE-1) BTH_II0567(ilvE-2)
            PNU: Pnuc_1818
            BPE: BP3398(ilvE) BP3571
            BPA: BPP3341 BPP3551(ilvE)
            BBR: BB3792 BB3986(ilvE)
            RFR: Rfer_0506
            POL: Bpro_0203
            AAV: Aave_0264
            AJS: Ajs_0182
            VEI: Veis_2475
            MPT: Mpe_A3552
            HAR: HEAR2611(ilvE)
            MMS: mma_2848
            NEU: NE1893(ilvE)
            NET: Neut_2005
            NMU: Nmul_A1060
            EBA: ebA993(ilvE)
            AZO: azo0133(ilvE1) azo2775(ilvE2)
            DAR: Daro_3294 Daro_4078
            TBD: Tbd_2134
            MFA: Mfla_0626
            HPY: HP1468
            HPJ: jhp1361(ilvE)
            HPA: HPAG1_1447
            HHE: HH0451(ilvE)
            HAC: Hac_1717(ilvE)
            WSU: WS0092(ilvE)
            TDN: Tmden_1877
            CJE: Cj0269c(ilvE)
            CJR: CJE0318(ilvE)
            CJJ: CJJ81176_0296(ilvE)
            CJU: C8J_0246(ilvE)
            CJD: JJD26997_1707(ilvE)
            CFF: CFF8240_0304(ilvE)
            CCV: CCV52592_0855(ilvE)
            CHA: CHAB381_1449(ilvE)
            CCO: CCC13826_2109(ilvE)
            ABU: Abu_0118(ilvE)
            NIS: NIS_1542(ilvE)
            SUN: SUN_0239(ilvE)
            GSU: GSU0656(ilvE)
            GME: Gmet_2853
            GUR: Gura_3951
            PCA: Pcar_0976 Pcar_2588
            PPD: Ppro_1335
            DVU: DVU3047 DVU3197(ilvE)
            DVL: Dvul_0190
            DDE: Dde_0065 Dde_0255
            LIP: LI0915(livE) LI0950
            BBA: Bd1131(ilvE) Bd1736(ilvE)
            DPS: DP0085 DP0192
            ADE: Adeh_1052 Adeh_3428
            MXA: MXAN_2987(ilvE)
            SAT: SYN_03154 SYN_03155
            SFU: Sfum_3098 Sfum_3207
            RPR: RP428
            RTY: RT0414(ilvE)
            RCO: RC0594(ilvE)
            RFE: RF_0659(ilvE)
            RBE: RBE_0741(ilvE)
            RAK: A1C_03195
            RBO: A1I_04810
            RRI: A1G_03340
            OTS: OTBS_0394(ilvE)
            PUB: SAR11_0086(ilvE)
            MLO: mll2664 mll9205 mlr1594 mlr7635
            MES: Meso_2140
            SME: SMc00042(ilvE2) SMc02896(ilvE1)
            ATU: Atu0871(ilvE)
            ATC: AGR_C_1592
            RET: RHE_CH01190(ilvE1) RHE_CH02730(ilvE2)
            RLE: RL1326(ilvE) RL3200(ilvE)
            BME: BMEII0612 BMEII0613
            BMF: BAB2_0572
            BMB: BruAb2_0559
            BJA: bll0229(ilvE) bll7459
            BRA: BRADO6039 BRADO6909
            BBT: BBta_0618 BBta_1739
            RPA: RPA4370(ilvE) RPA4593
            RPB: RPB_0999 RPB_4175
            RPC: RPC_1388
            RPD: RPD_1102 RPD_3886
            RPE: RPE_1423
            NWI: Nwi_2520
            NHA: Nham_3139
            BHE: BH10010(ilvE)
            BQU: BQ07730(ilvE)
            BBK: BARBAKC583_0747(ilvE)
            CCR: CC_2929
            SIL: SPO0253(ilvE) SPO0388 SPOA0291
            SIT: TM1040_2926 TM1040_3729
            RSP: RSP_1140(ilvE) RSP_1215(ilvE) RSP_2216(ilvE)
            JAN: Jann_0094
            RDE: RD1_0553(ilvE) RD1_0990 RD1_1654(ilvE)
            MMR: Mmar10_0286
            HNE: HNE_3091(ilvE)
            ZMO: ZMO0913(ilvE)
            NAR: Saro_2671
            SAL: Sala_0047
            SWI: Swit_0778
            ELI: ELI_08370
            GOX: GOX0450
            GBE: GbCGDNIH1_0739
            RRU: Rru_A0300 Rru_A0508 Rru_A2223
            MAG: amb0551
            MGM: Mmc1_1863
            ABA: Acid345_0712
            SUS: Acid_5573
            BSU: BG10546(ywaA) BG12749(ybgE)
            BHA: BH2156(bcaT)
            BAN: BA1416(ilvE-1) BA1849(ilvE-2)
            BAR: GBAA1416(ilvE-1) GBAA1849(ilvE-2)
            BAA: BA_1936 BA_2352
            BAT: BAS1307 BAS1713
            BCE: BC1396 BC1776
            BCA: BCE_1516(ilvE) BCE_1933(ilvE)
            BCZ: BCZK1281(ilvE) BCZK1665(ilvE)
            BCY: Bcer98_1444
            BTK: BT9727_1280(ilvE) BT9727_1690(ilvE)
            BTL: BALH_1251(ilvE) BALH_1623(ilvE)
            BLI: BL00607 BL03930(ywaA)
            BLD: BLi02962 BLi04084(ywaA)
            BCL: ABC1931
            OIH: OB2628
            GKA: GK2662
            SAU: SA0512(ilvE)
            SAV: SAV0554(ilvE)
            SAM: MW0509(ilvE)
            SAR: SAR0559
            SAS: SAS0512
            SAC: SACOL0600(ilvE)
            SAB: SAB0505
            SAA: SAUSA300_0539(ilvE)
            SAO: SAOUHSC_00536
            SEP: SE0318
            SER: SERP0195(ilvE)
            SHA: SH2449(ilvE)
            SSP: SSP2163
            LMO: lmo0978
            LMF: LMOf2365_0999(ilvE)
            LIN: lin0977
            LWE: lwe0961(ilvE)
            LLA: L0086(bcaT)
            LLC: LACR_1409
            LLM: llmg_1181(ilvE)
            SPY: SPy_0911(bcaT)
            SPZ: M5005_Spy_0713(bcaT)
            SPM: spyM18_0969(ilvE)
            SPG: SpyM3_0626(bcaT)
            SPS: SPs1227
            SPH: MGAS10270_Spy0772(bcaT)
            SPI: MGAS10750_Spy0805(bcaT)
            SPJ: MGAS2096_Spy0785(bcaT)
            SPK: MGAS9429_Spy0769(bcaT)
            SPF: SpyM51094
            SPA: M6_Spy0730
            SPB: M28_Spy0693(bcaT)
            SPN: SP_0856
            SPR: spr0758(ilvE)
            SPD: SPD_0749(ilvE)
            SAG: SAG1152(ilvE)
            SAN: gbs1227
            SAK: SAK_1241(ilvE)
            SMU: SMU.1203(ilvE)
            STC: str0590(bcaT)
            STL: stu0590(bcaT)
            SSA: SSA_1225(ilvE)
            SGO: SGO_1238(ilvE)
            LPL: lp_2390(bcaT)
            LAC: LBA1341(ilvE)
            LSL: LSL_0063(ilvE)
            LDB: Ldb1305(ilvE)
            LBU: LBUL_1219
            LCA: LSEI_2041
            EFA: EF1793(ilvE)
            STH: STH2686
            CAC: CAC1479(ilvE)
            CPE: CPE1520(ilvE)
            CPF: CPF_1772(ilvE)
            CPR: CPR_1501(ilvE)
            CTC: CTC01738
            CNO: NT01CX_0183(ilvE) NT01CX_1857 NT01CX_2030(ilvE)
            CTH: Cthe_0856
            CBE: Cbei_1043
            CKL: CKL_2135(ilvE2) CKL_3620(ilvE3)
            AMT: Amet_3334
            CHY: CHY_0515(ilvE)
            DSY: DSY1364
            DRM: Dred_2144
            SWO: Swol_2148
            TTE: TTE0933(ilvE)
            MTA: Moth_2109 Moth_2260
            MTU: Rv2210c(ilvE)
            MTC: MT2266(ilvE)
            MBO: Mb2233c(ilvE)
            MBB: BCG_2226c(ilvE)
            MLE: ML0866(ilvE)
            MPA: MAP1950c(ilvE)
            MAV: MAV_2281(ilvE)
            MSM: MSMEG_4276(ilvE)
            MVA: Mvan_3573
            MGI: Mflv_2940
            MMC: Mmcs_3308
            MKM: Mkms_3370
            MJL: Mjls_3319
            CGL: NCgl2123(cgl2204)
            CGB: cg2418(ilvE)
            CEF: CE2095(ilvE)
            CDI: DIP1636(ilvE)
            CJK: jk0710(ilvE)
            NFA: nfa16970 nfa3220
            RHA: RHA1_ro01147(ilvE1) RHA1_ro02970(ilvE2) RHA1_ro04442(ilvE3)
            SCO: SCO1546(SCL11.02c) SCO5523(ilvE)
            SMA: SAV2717(ilvE) SAV6804 SAV842
            TWH: TWT208(ilvE)
            TWS: TW564(ilvE)
            LXX: Lxx13120(ilvE)
            CMI: CMM_1105(ilvE)
            AAU: AAur_2497(ilvE)
            PAC: PPA1368
            NCA: Noca_3367
            TFU: Tfu_0616 Tfu_2112
            FRA: Francci3_3631
            FAL: FRAAL4661 FRAAL5842(ilvE)
            ACE: Acel_0711
            KRA: Krad_1353
            SEN: SACE_1646 SACE_2128
            STP: Strop_1240
            BLO: BL0852(ilvE)
            BAD: BAD_0743(ilvE)
            RXY: Rxyl_3128
            RBA: RB5738(ilvE) RB8126(ilvE)
            LIL: LA4360(ilvE)
            LIC: LIC13496(ilvE)
            LBJ: LBJ_0002(ilvE)
            LBL: LBL_0002(ilvE)
            SYN: slr0032(ilvE)
            SYW: SYNW1239(ilvE)
            SYC: syc0517_c(livE)
            SYF: Synpcc7942_1029
            SYD: Syncc9605_1356
            SYE: Syncc9902_1122
            SYG: sync_1354(ilvE)
            SYR: SynRCC307_1208(ilvE)
            SYX: SynWH7803_1276(ilvE)
            CYA: CYA_1005(ilvE)
            CYB: CYB_0479(ilvE)
            TEL: tll1462 tll2043
            GVI: gll1225 gll2582(ilvE)
            PMA: Pro0958(ilvE)
            PMM: PMM0878(ilvE)
            PMT: PMT0728(ilvE)
            PMN: PMN2A_0332
            PMI: PMT9312_0922
            PMB: A9601_09831(ilvE)
            PMC: P9515_09601(ilvE)
            PMF: P9303_14901(ilvE)
            PMG: P9301_09811(ilvE)
            PMH: P9215_10141
            PME: NATL1_10051(ilvE)
            TER: Tery_0889
            BTH: BT_3892
            BFR: BF3997
            BFS: BF3772
            PGI: PG1290(ilvE)
            SRU: SRU_2317(ilvE)
            CHU: CHU_2817(ilvE)
            GFO: GFO_0499 GFO_1441(ilvE)
            FJO: Fjoh_4770
            FPS: FP0450(ilvE) FP1741 FP2006
            CTE: CT1605(ilvE)
            CCH: Cag_1779
            CPH: Cpha266_0588
            PLT: Plut_1601
            DET: DET0009(ilvE)
            DEH: cbdb_A11(ilvE)
            DRA: DR_1626
            DGE: Dgeo_2743
            TTH: TTC1870
            TTJ: TTHA0124
            AAE: aq_1893(ilvE)
            TMA: TM0831
            MMP: MMP0132
            MMQ: MmarC5_1546
            MMZ: MmarC7_1131
            MAE: Maeo_1195
            MVN: Mevan_1137
            MAC: MA4349(ilvE)
            MBA: Mbar_A0576
            MMA: MM_1045
            MBU: Mbur_1543
            MTP: Mthe_1306
            MHU: Mhun_0672
            MEM: Memar_1735
            MBN: Mboo_1421
            MST: Msp_0015(ilvE)
            MSI: Msm_1202
            MKA: MK1627(ilvE)
            HAL: VNG0387G(ilvE1) VNG2122G(ilvE2)
            HMA: rrnAC0711(ilvE2) rrnAC3071(ilvE1)
            HWA: HQ1247A(ilvE) HQ3234A(ilvE)
            NPH: NP0798A(ilvE_2) NP5036A(ilvE_1)
            RCI: RCIX558(ilvE)
            PAI: PAE3297(ilvE)
            NEQ: NEQ190
STRUCTURES  PDB: 1A3G  1EKF  1EKP  1EKV  1I1K  1I1L  1I1M  1IYD  1IYE  1KT8  
                 1KTA  1WRV  2A1H  2ABJ  2COG  2COI  2COJ  2HDK  2HG8  2HGW  
                 2HGX  2HHF  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.42
            ExPASy - ENZYME nomenclature database: 2.6.1.42
            ExplorEnz - The Enzyme Database: 2.6.1.42
            ERGO genome analysis and discovery system: 2.6.1.42
            BRENDA, the Enzyme Database: 2.6.1.42
            CAS: 9054-65-3
///
ENTRY       EC 2.6.1.43                 Enzyme
NAME        aminolevulinate transaminase;
            aminolevulinate aminotransferase, gamma,delta-dioxovalerate
            aminotransferase;
            gamma,delta-dioxovaleric acid transaminase;
            4,5-dioxovalerate aminotransferase;
            4,5-dioxovaleric acid transaminase;
            4,5-dioxovaleric transaminase;
            5-aminolevulinic acid transaminase;
            alanine-gamma,delta-dioxovalerate aminotransferase;
            alanine-dioxovalerate aminotransferase;
            alanine:4,5-dioxovalerate aminotransferase;
            aminolevulinic acid transaminase;
            dioxovalerate transaminase;
            L-alanine-4,5-dioxovalerate aminotransferase;
            L-alanine:4,5-dioxovaleric acid transaminase;
            L-alanine:dioxovalerate transaminase;
            DOVA transaminase;
            4,5-dioxovaleric acid aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     5-aminolevulinate:pyruvate aminotransferase
REACTION    5-aminolevulinate + pyruvate = 4,5-dioxopentanoate + L-alanine
            [RN:R02271]
ALL_REAC    R02271
SUBSTRATE   5-aminolevulinate [CPD:C00430];
            pyruvate [CPD:C00022]
PRODUCT     4,5-dioxopentanoate [CPD:C02800];
            L-alanine [CPD:C00041]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1
  AUTHORS   Gibson, K.D., Matthew, M. and Neuberger, A.
  TITLE     Biosynthesis of porphyrins and chlorophylls.
  JOURNAL   Nature 192 (1961) 204-208.
REFERENCE   2  [PMID:13938132]
  AUTHORS   NEUBERGER A, TURNER JM.
  TITLE     gamma,delta-Dioxovalerate aminotransferase activity in
            Rhodopseudomonas spheroides.
  JOURNAL   Biochim. Biophys. Acta. 67 (1963) 342-5.
  ORGANISM  Rhodopseudomonas spheroides
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.43
            ExPASy - ENZYME nomenclature database: 2.6.1.43
            ExplorEnz - The Enzyme Database: 2.6.1.43
            ERGO genome analysis and discovery system: 2.6.1.43
            BRENDA, the Enzyme Database: 2.6.1.43
            CAS: 9012-46-8
///
ENTRY       EC 2.6.1.44                 Enzyme
NAME        alanine---glyoxylate transaminase;
            AGT;
            alanine-glyoxylate aminotransferase;
            alanine-glyoxylic aminotransferase;
            L-alanine-glycine transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-alanine:glyoxylate aminotransferase
REACTION    L-alanine + glyoxylate = pyruvate + glycine [RN:R00369]
ALL_REAC    R00369
SUBSTRATE   L-alanine [CPD:C00041];
            glyoxylate [CPD:C00048]
PRODUCT     pyruvate [CPD:C00022];
            glycine [CPD:C00037]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. With one component of the animal
            enzyme, 2-oxobutanoate can replace glyoxylate. A second component
            also catalyses the reaction of EC 2.6.1.51 serine---pyruvate
            transaminase.
REFERENCE   1  [PMID:629740]
  AUTHORS   Noguchi T, Okuno E, Takada Y, Minatogawa Y, Okai K, Kido R.
  TITLE     Characteristics of hepatic alanine-glyoxylate aminotransferase in
            different mammalian species.
  JOURNAL   Biochem. J. 169 (1978) 113-22.
  ORGANISM  dog [GN:cfa], cat, rat [GN:rno], mouse [GN:mmu]
REFERENCE   2  [PMID:6803844]
  AUTHORS   Okuno E, Minatogawa Y, Kido R.
  TITLE     Co-purification of alanine-glyoxylate aminotransferase with
            2-aminobutyrate aminotransferase in rat kidney.
  JOURNAL   Biochim. Biophys. Acta. 715 (1982) 97-104.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:6038488]
  AUTHORS   Thompson JS, Richardson KE.
  TITLE     Isolation and characterization of an L-alanine: glyoxylate
            aminotransferase from human liver.
  JOURNAL   J. Biol. Chem. 242 (1967) 3614-9.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
            PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K00827  alanine--glyoxylate transaminase
GENES       HSA: 189(AGXT) 64902(AGXT2)
            MMU: 11611(Agxt) 268782(Agxt2)
            RNO: 24792(Agxt) 83784(Agxt2)
            CFA: 607355(AGXT) 612589(AGXT2)
            GGA: 431666(AGXT2)
            XLA: 398137(agt)
            XTR: 448338(agxt)
            SPU: 575497(LOC575497) 594821(LOC594821)
            DME: Dmel_CG11241 Dmel_CG3926(Spat)
            CEL: T09B4.8(aminotransferase) T14D7.1
            ATH: AT4G39660(AGT2)
            OSA: 4331779
            CNE: CNL05470
            DDI: DDBDRAFT_0188646
            TET: TTHERM_00102730
            SFR: Sfri_0426
            SBL: Sbal_4027
            SLO: Shew_0294
            SPC: Sputcn32_3610
            RMA: Rmag_0312
            BUR: Bcep18194_A3920 Bcep18194_B0347
            BPM: BURPS1710b_3219
            BPE: BP3685
            BPA: BPP0101
            BBR: BB0100
            HAR: HEAR0887
            NET: Neut_0200
            GUR: Gura_0866
            RDE: RD1_1161
            ABA: Acid345_0127
            SUS: Acid_2515
            AMT: Amet_3605
            NCA: Noca_3274
            SYW: SYNW1075(spt)
            SYC: syc1934_c(spt)
            SYF: Synpcc7942_2160
            SYD: Syncc9605_1207
            SYE: Syncc9902_1263
            SYG: sync_1566
            SYR: SynRCC307_1294(spt)
            SYX: SynWH7803_1345(spt)
            ANA: alr1004
            AVA: Ava_5058
            PMA: Pro1037
            PMM: PMM0919(spt)
            PMT: PMT0600(spt)
            PMN: PMN2A_0142
            PMI: PMT9312_0881
            PMB: A9601_09411(spt)
            PMC: P9515_10021(spt)
            PMF: P9303_16451(spt)
            PMG: P9301_09401(spt)
            PME: NATL1_07741(spt)
            MMZ: MmarC7_1389
            MAE: Maeo_1323
            HMA: rrnAC1999(spaT)
            HWA: HQ2919A(agxT)
            NPH: NP2578A(agt_1)
STRUCTURES  PDB: 1H0C  1J04  1VJO  2BKW  2HUF  2HUI  2HUU  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.44
            ExPASy - ENZYME nomenclature database: 2.6.1.44
            ExplorEnz - The Enzyme Database: 2.6.1.44
            ERGO genome analysis and discovery system: 2.6.1.44
            BRENDA, the Enzyme Database: 2.6.1.44
            CAS: 9015-67-2
///
ENTRY       EC 2.6.1.45                 Enzyme
NAME        serine---glyoxylate transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-serine:glyoxylate aminotransferase
REACTION    L-serine + glyoxylate = 3-hydroxypyruvate + glycine [RN:R00588]
ALL_REAC    R00588
SUBSTRATE   L-serine [CPD:C00065];
            glyoxylate [CPD:C00048]
PRODUCT     3-hydroxypyruvate [CPD:C00168];
            glycine [CPD:C00037]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:6407397]
  AUTHORS   Ireland RJ, Joy KW.
  TITLE     Purification and properties of an asparagine aminotransferase from
            Pisum sativum leaves.
  JOURNAL   Arch. Biochem. Biophys. 223 (1983) 291-6.
  ORGANISM  Pisum sativum
REFERENCE   2  [PMID:5672858]
  AUTHORS   King J, Waygood ER.
  TITLE     Glyoxylate aminotranferases from wheat leaves.
  JOURNAL   Can. J. Biochem. 46 (1968) 771-9.
  ORGANISM  Triticum aestivum [GN:etae]
REFERENCE   3  [PMID:4750762]
  AUTHORS   Smith IK.
  TITLE     Purification and characterization of serine:glyoxylate
            aminotransferase from kidney bean (Phaseolus vulgaris).
  JOURNAL   Biochim. Biophys. Acta. 321 (1973) 156-64.
  ORGANISM  Phaseolus vulgaris
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K00828  serine--glyoxylate transaminase
GENES       OSA: 4345962
            CME: CMS429C
            PAR: Psyc_1388(sgaA)
            MCA: MCA1406(sgaA)
            RME: Rmet_5630
            BXE: Bxe_B3001
            BUR: Bcep18194_A6497 Bcep18194_B2675 Bcep18194_B3022
            PNU: Pnuc_0602
            BPA: BPP4201
            BBR: BB4671
            POL: Bpro_0548
            MPT: Mpe_A3261
            HAR: HEAR2731(sgaA)
            MMS: mma_0436
            DVL: Dvul_2447
            MLO: mlr1322
            SME: SMa2139(sgaA)
            BJA: bll6039
            BRA: BRADO5277 BRADO5278 BRADO6985
            BBT: BBta_0544 BBta_5728 BBta_5729
            RPA: RPA0789
            RPB: RPB_4629
            RPC: RPC_4689
            RPD: RPD_0780
            RPE: RPE_0897
            NWI: Nwi_2413
            NHA: Nham_2804
            SIL: SPO3029 SPOA0144
            SIT: TM1040_1983 TM1040_2699
            RSP: RSP_0245
            RSQ: Rsph17025_2018
            RDE: RD1_1750(sgaA) RD1_2892(sgaA)
            PDE: Pden_3921
            GBE: GbCGDNIH1_0048
            ACR: Acry_1369 Acry_3418
            CDF: CD0994
            CBO: CBO1126
            SEN: SACE_3639
            RXY: Rxyl_0836
            SYF: Synpcc7942_0191
            PMI: PMT9312_0035
            TER: Tery_3167
            CPH: Cpha266_2460
            MMQ: MmarC5_1247
            MHU: Mhun_2475
            PCL: Pcal_1612
            PAS: Pars_1870
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.45
            ExPASy - ENZYME nomenclature database: 2.6.1.45
            ExplorEnz - The Enzyme Database: 2.6.1.45
            ERGO genome analysis and discovery system: 2.6.1.45
            BRENDA, the Enzyme Database: 2.6.1.45
            CAS: 37259-57-7
///
ENTRY       EC 2.6.1.46                 Enzyme
NAME        diaminobutyrate---pyruvate transaminase;
            diaminobutyrate-pyruvate aminotransferase;
            L-diaminobutyric acid transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-2,4-diaminobutanoate:pyruvate aminotransferase
REACTION    L-2,4-diaminobutanoate + pyruvate = L-aspartate 4-semialdehyde +
            L-alanine [RN:R02293]
ALL_REAC    R02293
SUBSTRATE   L-2,4-diaminobutanoate [CPD:C03283];
            pyruvate [CPD:C00022]
PRODUCT     L-aspartate 4-semialdehyde [CPD:C00441];
            L-alanine [CPD:C00041]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:4390206]
  AUTHORS   Rao DR, Hariharan K, Vijayalakshmi KR.
  TITLE     A study of the metabolism of L-alpha gamma-diaminobutyric acid in a
            Xanthomonas species.
  JOURNAL   Biochem. J. 114 (1969) 107-15.
  ORGANISM  Xanthomonas sp.
ORTHOLOGY   KO: K00829  diaminobutyrate-pyruvate transaminase
GENES       HIT: NTHI1122(dat)
            VCO: VC0395_0410(ectB)
            SDE: Sde_1190
            NOC: Noc_1561
            HCH: HCH_01509(gabT)
            ABO: ABO_2151(ectB)
            MMS: mma_3600(ectB)
            RET: RHE_CH01979(argD2)
            NFA: nfa27170(ectB)
            RHA: RHA1_ro01306
            SCO: SCO5799(SC4H2.20)
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.46
            ExPASy - ENZYME nomenclature database: 2.6.1.46
            ExplorEnz - The Enzyme Database: 2.6.1.46
            ERGO genome analysis and discovery system: 2.6.1.46
            BRENDA, the Enzyme Database: 2.6.1.46
            CAS: 37277-95-5
///
ENTRY       EC 2.6.1.47                 Enzyme
NAME        alanine---oxomalonate transaminase;
            alanine-oxomalonate aminotransferase;
            L-alanine-ketomalonate transaminase;
            alanine-ketomalonate (mesoxalate) transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-alanine:oxomalonate aminotransferase
REACTION    L-alanine + oxomalonate = pyruvate + aminomalonate [RN:R02970]
ALL_REAC    R02970
SUBSTRATE   L-alanine [CPD:C00041];
            oxomalonate [CPD:C00830]
PRODUCT     pyruvate [CPD:C00022];
            aminomalonate [CPD:C00872]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1
  AUTHORS   Nagayama, H., Muramatsu, M. and Shimura, K.
  TITLE     Enzymatic formation of aminomalonic acid from ketomalonic acid.
  JOURNAL   Nature 181 (1958) 417-418.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.47
            ExPASy - ENZYME nomenclature database: 2.6.1.47
            ExplorEnz - The Enzyme Database: 2.6.1.47
            ERGO genome analysis and discovery system: 2.6.1.47
            BRENDA, the Enzyme Database: 2.6.1.47
            CAS: 37277-96-6
///
ENTRY       EC 2.6.1.48                 Enzyme
NAME        5-aminovalerate transaminase;
            5-aminovalerate aminotransferase;
            delta-aminovalerate aminotransferase;
            delta-aminovalerate transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     5-aminopentanoate:2-oxoglutarate aminotransferase
REACTION    5-aminopentanoate + 2-oxoglutarate = 5-oxopentanoate + L-glutamate
            [RN:R02274]
ALL_REAC    R02274
SUBSTRATE   5-aminopentanoate [CPD:C00431];
            2-oxoglutarate [CPD:C00026]
PRODUCT     5-oxopentanoate [CPD:C03273];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1
  AUTHORS   Ichihara, A., Ichihara, E.A. and Suda, M.
  TITLE     Metabolism of L-lysine by bacterial enzymes. IV. delta-Aminovaleric
            acid-glutamic acid transaminase.
  JOURNAL   J. Biochem. (Tokyo) 48 (1960) 412-420.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.48
            ExPASy - ENZYME nomenclature database: 2.6.1.48
            ExplorEnz - The Enzyme Database: 2.6.1.48
            ERGO genome analysis and discovery system: 2.6.1.48
            BRENDA, the Enzyme Database: 2.6.1.48
            CAS: 37277-97-7
///
ENTRY       EC 2.6.1.49                 Enzyme
NAME        dihydroxyphenylalanine transaminase;
            dopa transaminase;
            dihydroxyphenylalanine aminotransferase;
            aspartate-DOPP transaminase (ADT);
            L-dopa transaminase;
            dopa aminotransferase;
            glutamate-DOPP transaminase (GDT);
            phenylalanine-DOPP transaminase (PDT);
            DOPA 2-oxoglutarate aminotransferase;
            DOPAATS
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     3,4-dihydroxy-L-phenylalanine:2-oxoglutarate aminotransferase
REACTION    3,4-dihydroxy-L-phenylalanine + 2-oxoglutarate =
            3,4-dihydroxyphenylpyruvate + L-glutamate [RN:R02077]
ALL_REAC    R02077
SUBSTRATE   3,4-dihydroxy-L-phenylalanine [CPD:C00355];
            2-oxoglutarate [CPD:C00026]
PRODUCT     3,4-dihydroxyphenylpyruvate;
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:5829872]
  AUTHORS   Fonnum F, Larsen K.
  TITLE     Purification and properties of dihydroxyphenylalanine transaminase
            from guinea pig brain.
  JOURNAL   J. Neurochem. 12 (1965) 589-98.
  ORGANISM  guinea pig
PATHWAY     PATH: map00350  Tyrosine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.49
            ExPASy - ENZYME nomenclature database: 2.6.1.49
            ExplorEnz - The Enzyme Database: 2.6.1.49
            ERGO genome analysis and discovery system: 2.6.1.49
            BRENDA, the Enzyme Database: 2.6.1.49
            CAS: 37277-98-8
///
ENTRY       EC 2.6.1.50                 Enzyme
NAME        glutamine---scyllo-inositol transaminase;
            glutamine scyllo-inosose aminotransferase;
            L-glutamine-keto-scyllo-inositol aminotransferase;
            glutamine-scyllo-inosose transaminase;
            L-glutamine-scyllo-inosose transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-glutamine:2,4,6/3,5-pentahydroxycyclohexanone aminotransferase
REACTION    L-glutamine + 2,4,6/3,5-pentahydroxycyclohexanone = 2-oxoglutaramate
            + 1-amino-1-deoxy-scyllo-inositol [RN:R02781]
ALL_REAC    R02781
SUBSTRATE   L-glutamine [CPD:C00064];
            2,4,6/3,5-pentahydroxycyclohexanone [CPD:C00691]
PRODUCT     2-oxoglutaramate [CPD:C00940];
            1-amino-1-deoxy-scyllo-inositol [CPD:C01214]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:5781017]
  AUTHORS   Walker JB, Walker MS.
  TITLE     Streptomycin biosynthesis. Transamination reactions involving
            inosamines and inosadiamines.
  JOURNAL   Biochemistry. 8 (1969) 763-70.
  ORGANISM  Streptomyces bikiniensis
ORTHOLOGY   KO: K05957  
GENES       ASU: Asuc_0108
            SBM: Shew185_2361
            CVI: CV_0750
            HPA: HPAG1_1028
            GUR: Gura_1701 Gura_3190 Gura_4276
            SMD: Smed_4806 Smed_4809
            CBE: Cbei_4711 Cbei_4882
            CSC: Csac_1802
            STP: Strop_1688
            RRS: RoseRS_3868 RoseRS_4428
            RCA: Rcas_0204 Rcas_0781 Rcas_1361 Rcas_3628 Rcas_3813
            MAE: Maeo_0427
            MVN: Mevan_0205
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.50
            ExPASy - ENZYME nomenclature database: 2.6.1.50
            ExplorEnz - The Enzyme Database: 2.6.1.50
            ERGO genome analysis and discovery system: 2.6.1.50
            BRENDA, the Enzyme Database: 2.6.1.50
            CAS: 9033-03-8
///
ENTRY       EC 2.6.1.51                 Enzyme
NAME        serine---pyruvate transaminase;
            SPT;
            hydroxypyruvate:L-alanine transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-serine:pyruvate aminotransferase
REACTION    L-serine + pyruvate = 3-hydroxypyruvate + L-alanine [RN:R00585]
ALL_REAC    R00585
SUBSTRATE   L-serine [CPD:C00065];
            pyruvate [CPD:C00022]
PRODUCT     3-hydroxypyruvate [CPD:C00168];
            L-alanine [CPD:C00041]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. The liver enzyme may be identical
            with EC 2.6.1.44 alanine-glyoxylate transaminase.
REFERENCE   1  [PMID:5699148]
  AUTHORS   Cheung GP, Rosenblum IY, Sallach HJ.
  TITLE     Comparative studies of enzymes related to serine metabolism in
            higher plants.
  JOURNAL   Plant. Physiol. 43 (1968) 1813-20.
  ORGANISM  Pisum sativum
REFERENCE   2
  AUTHORS   Kretovich, V.L. and Stepanovich, K.M.
  TITLE     [The synthesis of serine from hydroxypyruvate in plants.].
  JOURNAL   Dokl. Akad. Nauk S.S.S.R. 139 (1961) 488-490.
REFERENCE   3
  AUTHORS   Sallach, H.J.
  TITLE     Formation of serine from hydroxypyruvate and L-alanine.
  JOURNAL   J. Biol. Chem. 223 (1956) 1101-1108.
  ORGANISM  dog [GN:cfa]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K00830  serine--pyruvate aminotransferase
GENES       HSA: 189(AGXT)
            MMU: 11611(Agxt)
            RNO: 24792(Agxt)
            CFA: 607355(AGXT)
            XLA: 398137(agt)
            XTR: 448338(agxt)
            SPU: 575497(LOC575497)
            CEL: T14D7.1
            DDI: DDBDRAFT_0188646
            PEN: PSEEN2741
            SDN: Sden_0404
            SAZ: Sama_3277
            SBM: Shew185_4005
            SSE: Ssed_4160
            SPL: Spea_0350
            SHE: Shewmr4_0366
            SHM: Shewmr7_3660
            SHN: Shewana3_0360
            SHW: Sputw3181_3750
            PAT: Patl_2043
            PIN: Ping_2424
            ABO: ABO_1608
            BUR: Bcep18194_B1916
            MMS: mma_0747
            NMU: Nmul_A2538
            DVL: Dvul_0262 Dvul_2203
            SMD: Smed_5312
            RDE: RD1_1957
            RRU: Rru_A2010
            BCE: BC2399
            BCZ: BCZK2217
            BTK: BT9727_2259
            BCL: ABC3292
            CBE: Cbei_0759
            DSY: DSY1288
            KRA: Krad_2078
            DGE: Dgeo_1114
            TTH: TTC1813
            MVN: Mevan_1378
            HWA: HQ2919A(agxT)
            NPH: NP2578A(agt_1)
            PTO: PTO0371 PTO1431
            SSO: SSO2597(agxT)
            STO: ST0602
            SAI: Saci_0249
STRUCTURES  PDB: 1J04  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.51
            ExPASy - ENZYME nomenclature database: 2.6.1.51
            ExplorEnz - The Enzyme Database: 2.6.1.51
            ERGO genome analysis and discovery system: 2.6.1.51
            BRENDA, the Enzyme Database: 2.6.1.51
            CAS: 9030-88-0
///
ENTRY       EC 2.6.1.52                 Enzyme
NAME        phosphoserine transaminase;
            PSAT;
            phosphoserine aminotransferase;
            3-phosphoserine aminotransferase;
            hydroxypyruvic phosphate-glutamic transaminase;
            L-phosphoserine aminotransferase;
            phosphohydroxypyruvate transaminase;
            phosphohydroxypyruvic-glutamic transaminase;
            3-O-phospho-L-serine:2-oxoglutarate aminotransferase;
            SerC;
            PdxC;
            3PHP transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     O-phospho-L-serine:2-oxoglutarate aminotransferase
REACTION    (1) O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate +
            L-glutamate [RN:R04173];
            (2) 4-phosphonooxy-L-threonine + 2-oxoglutarate =
            (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate
ALL_REAC    R04173;
            (other) R05085
SUBSTRATE   O-phospho-L-serine [CPD:C01005];
            2-oxoglutarate [CPD:C00026];
            4-phosphonooxy-L-threonine
PRODUCT     3-phosphonooxypyruvate [CPD:C03232];
            L-glutamate [CPD:C00025];
            (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate [CPD:C06054]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. This enzyme catalyses the second step
            in the phosphorylated pathway of serine biosynthesis in Escherichia
            coli [2,3]. It also catalyses the third step in the biosynthesis of
            the coenzyme pyridoxal 5'-phosphate in Escherichia coli (using
            Reaction 2 above) [3]. In Escherichia coli, pyridoxal 5'-phosphate
            is synthesized de novo by a pathway that involves EC 1.2.1.72
            (erythrose-4-phosphate dehydrogenase), EC 1.1.1.290
            (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine
            transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate
            dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and
            EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate). Pyridoxal
            phosphate is the cofactor for both activities and therefore seems to
            be involved in its own biosynthesis [4]. Non-phosphorylated forms of
            serine and threonine are not substrates [4].
REFERENCE   1  [PMID:6022873]
  AUTHORS   Hirsch H, Greenberg DM.
  TITLE     Studies on phosphoserine aminotransferase of sheep brain.
  JOURNAL   J. Biol. Chem. 242 (1967) 2283-7.
  ORGANISM  sheep
REFERENCE   2  [PMID:14086727]
  AUTHORS   PIZER LI.
  TITLE     THE PATHWAY AND CONTROL OF SERINE BIOSYNTHESIS IN ESCHERICHIA COLI.
  JOURNAL   J. Biol. Chem. 238 (1963) 3934-44.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:8550422]
  AUTHORS   Zhao G, Winkler ME.
  TITLE     A novel alpha-ketoglutarate reductase activity of the serA-encoded
            3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its
            possible implications for human 2-hydroxyglutaric aciduria.
  JOURNAL   J. Bacteriol. 178 (1996) 232-9.
  ORGANISM  Escherichia coli [GN:eco], human [GN:hsa]
REFERENCE   4  [PMID:8706854]
  AUTHORS   Drewke C, Klein M, Clade D, Arenz A, Muller R, Leistner E.
  TITLE     4-O-phosphoryl-L-threonine, a substrate of the pdxC(serC) gene
            product involved in vitamin B6 biosynthesis.
  JOURNAL   FEBS. Lett. 390 (1996) 179-82.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:8595869]
  AUTHORS   Zhao G, Winkler ME.
  TITLE     4-Phospho-hydroxy-L-threonine is an obligatory intermediate in
            pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli
            K-12.
  JOURNAL   FEMS. Microbiol. Lett. 135 (1996) 275-80.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00750  Vitamin B6 metabolism
ORTHOLOGY   KO: K00831  phosphoserine aminotransferase
GENES       HSA: 29968(PSAT1)
            PTR: 464542(PSAT1)
            MMU: 107272(Psat1)
            RNO: 293820(Psat1)
            CFA: 476318(PSAT1)
            GGA: 427263(PSAT1)
            XLA: 494700(LOC494700)
            DRE: 327512(psat1)
            SPU: 580016(LOC580016)
            DME: Dmel_CG11899
            CEL: F26H9.5
            OSA: 4331678
            CME: CMT252C
            SCE: YOR184W(SER1)
            AGO: AGOS_AGR288W
            PIC: PICST_36392(SER1)
            CGR: CAGL0G09691g
            SPO: SPAC1F12.07
            ANI: AN2409.2
            AFM: AFUA_6G04970
            AOR: AO090023000099
            CNE: CNH00670
            DDI: DDB_0230053(serC)
            TET: TTHERM_00418290 TTHERM_00678170
            EHI: 253.t00001 30.t00047
            ECO: b0907(serC)
            ECJ: JW0890(serC)
            ECE: Z1253(serC)
            ECS: ECs0990
            ECC: c1045(serC)
            ECI: UTI89_C0978(serC)
            ECP: ECP_0918
            ECV: APECO1_19(serC)
            ECW: EcE24377A_1004(serC)
            ECX: EcHS_A0989 EcHS_A1013(serC)
            STY: STY0977(serC)
            STT: t1957(serC)
            SPT: SPA1821(serC)
            SEC: SC0931(serC)
            STM: STM0977(serC)
            YPE: YPO1389(serC)
            YPK: y2784(serC)
            YPM: YP_1204(serC)
            YPA: YPA_0680
            YPN: YPN_2588
            YPP: YPDSF_2306
            YPS: YPTB1414(serC)
            YPI: YpsIP31758_2583(serC)
            YEN: YE1537(serC)
            SFL: SF0902(serC)
            SFX: S0966(serC)
            SFV: SFV_0907(serC)
            SSN: SSON_0908(serC)
            SBO: SBO_2193(serC)
            SDY: SDY_2354(serC)
            ECA: ECA2594(serC)
            PLU: plu1619(serC)
            BUC: BU312(serC)
            BAS: BUsg302(serC)
            BAB: bbp289(serC)
            BCC: BCc_192(serC)
            WBR: WGLp486(serC)
            SGL: SG0990
            ENT: Ent638_1427
            SPE: Spro_1706
            BFL: Bfl383(serC)
            BPN: BPEN_394(serC)
            HIN: HI1167(serC)
            HIT: NTHI1335(serC)
            HDU: HD1382(serC)
            HSO: HS_0611(serC)
            PMU: PM0837(serC)
            MSU: MS1573(serC)
            APL: APL_0702(serC)
            ASU: Asuc_0922
            XFA: XF2326
            XFT: PD1358(serC)
            XCC: XCC1589(serC)
            XCB: XC_2645
            XCV: XCV1689(serC)
            XAC: XAC1648(serC)
            XOO: XOO2388(serC)
            XOM: XOO_2268(XOO2268)
            VCH: VC1159
            VCO: VC0395_A0728(serC)
            VVU: VV1_2813
            VVY: VV1451
            VPA: VP1247
            VFI: VF0899
            PPR: PBPRA2455
            PAE: PA3167(serC)
            PAU: PA14_23270(serC)
            PAP: PSPA7_1962(serC)
            PPU: PP_1768(serC)
            PPF: Pput_3946
            PST: PSPTO_1746(serC)
            PSB: Psyr_3646
            PSP: PSPPH_3666(serC)
            PFL: PFL_4313(serC)
            PFO: Pfl_4077
            PEN: PSEEN1488(serC)
            PMY: Pmen_1849
            PAR: Psyc_1036(serC)
            PCR: Pcryo_1434
            PRW: PsycPRwf_1413
            ACI: ACIAD2647(serC)
            SON: SO_2410(serC)
            SDN: Sden_1947
            SFR: Sfri_2129
            SAZ: Sama_1732
            SBL: Sbal_2063
            SBM: Shew185_2286
            SLO: Shew_1950
            SPC: Sputcn32_2069
            SSE: Ssed_2302
            SPL: Spea_2069
            SHE: Shewmr4_1920
            SHM: Shewmr7_2058
            SHN: Shewana3_1973
            SHW: Sputw3181_1943
            ILO: IL1359(serC)
            CPS: CPS_2332(serC)
            PHA: PSHAa1422(serC)
            PAT: Patl_2469
            SDE: Sde_1332
            PIN: Ping_0508 Ping_1115
            MAQ: Maqu_1022
            CBU: CBU_0525(serC)
            CBD: COXBU7E912_1538(serC)
            LPN: lpg1418(serC)
            LPF: lpl1369(serC)
            LPP: lpp1373(serC)
            MCA: MCA1420(serC)
            FTU: FTT0560c(serC)
            FTF: FTF0560c(serC)
            FTW: FTW_0980(serC)
            FTL: FTL_1018
            FTH: FTH_0993(serC)
            FTN: FTN_0955(serC)
            TCX: Tcr_1192
            NOC: Noc_0172
            AEH: Mlg_0924
            HHA: Hhal_0570
            HCH: HCH_04982(serC)
            CSA: Csal_2167
            ABO: ABO_1750(serC)
            MMW: Mmwyl1_2859
            AHA: AHA_1978(serC)
            DNO: DNO_0670
            BCI: BCI_0252(serC)
            RMA: Rmag_0628
            VOK: COSY_0581(serC)
            NME: NMB1640
            NMA: NMA1894(serC)
            NMC: NMC1554(serC)
            NGO: NGO1283
            CVI: CV_2301(serC)
            RSO: RSc0903(serC)
            REU: Reut_A2576
            REH: H16_A0791(serC)
            RME: Rmet_0715
            BMA: BMA0433(serC-1) BMA1625(serC-2)
            BMV: BMASAVP1_A2127(serC-2) BMASAVP1_A2576(serC-1)
            BML: BMA10299_A0951(serC-1) BMA10299_A3187(serC-2)
            BMN: BMA10247_0197(serC-1) BMA10247_1401(serC-2)
            BXE: Bxe_A0976
            BVI: Bcep1808_0963
            BUR: Bcep18194_A4155
            BCN: Bcen_0563
            BCH: Bcen2424_1042
            BAM: Bamb_0918
            BPS: BPSL2219 BPSL2519(serC)
            BPM: BURPS1710b_2651(serC-2) BURPS1710b_2998(serC)
            BPL: BURPS1106A_2565(serC-2) BURPS1106A_2949(serC)
            BPD: BURPS668_2512 BURPS668_2886(serC)
            BTE: BTH_I1634(serC) BTH_I1966
            PNU: Pnuc_0494
            BPE: BP0945(serC)
            BPA: BPP3133(serC)
            BBR: BB3472(serC)
            RFR: Rfer_1570
            POL: Bpro_1793
            PNA: Pnap_2792
            AAV: Aave_3281
            AJS: Ajs_2465
            VEI: Veis_3120
            MPT: Mpe_A2240
            HAR: HEAR2580(serC)
            MMS: mma_2674(serC)
            NEU: NE0333(serC)
            NET: Neut_1572
            NMU: Nmul_A2190
            EBA: ebA907(serC)
            AZO: azo1067(serC)
            DAR: Daro_0984 Daro_1231
            TBD: Tbd_0949
            MFA: Mfla_1687
            CJE: Cj0326(serC)
            CJR: CJE0371(serC)
            CJJ: CJJ81176_0348(serC)
            CJU: C8J_0303(serC)
            CJD: JJD26997_1632(serC)
            CFF: CFF8240_0254(serC)
            CCV: CCV52592_1676(serC)
            CHA: CHAB381_1292(serC)
            CCO: CCC13826_0520 CCC13826_1599(serC)
            PPD: Ppro_0735
            DPS: DP1933
            ADE: Adeh_2622
            AFW: Anae109_1719
            MXA: MXAN_4948(serC)
            SAT: SYN_00124
            SFU: Sfum_2083
            MLO: mll3876(psaT)
            MES: Meso_3162
            PLA: Plav_2137
            SME: SMc00640(serC)
            SMD: Smed_2619
            ATU: Atu3707(serC)
            ATC: AGR_L_2260(psaT)
            RET: RHE_CH03455(serC)
            RLE: RL3961(serC)
            BME: BMEI0347
            BMF: BAB1_1699(serC)
            BMS: BR1687(serC)
            BMB: BruAb1_1672(serC)
            BOV: BOV_1631
            OAN: Oant_1228
            BJA: bll7402(serC)
            BRA: BRADO5949(serC)
            BBT: BBta_1825(serC)
            RPA: RPA4309(serC)
            RPB: RPB_1314
            RPC: RPC_4107
            RPD: RPD_3906
            RPE: RPE_4161
            NWI: Nwi_2969
            NHA: Nham_1118
            BHE: BH03780(serC)
            BQU: BQ02790(serC)
            BBK: BARBAKC583_0271
            XAU: Xaut_1203
            CCR: CC_3216
            SIL: SPO3354
            SIT: TM1040_3020
            RSP: RSP_1351(serC)
            RSH: Rsph17029_0019
            RSQ: Rsph17025_0009
            JAN: Jann_0260
            RDE: RD1_0196(serC)
            PDE: Pden_0813
            MMR: Mmar10_0555
            HNE: HNE_3128
            ZMO: ZMO1684(serC)
            NAR: Saro_2679
            SAL: Sala_0617
            SWI: Swit_4686
            ELI: ELI_01955
            GOX: GOX1446
            GBE: GbCGDNIH1_0840
            ACR: Acry_2651
            RRU: Rru_A1104
            MAG: amb3194
            MGM: Mmc1_1422
            BSU: BG12673(serC)
            BHA: BH1188(serC)
            BAN: BA3321(serC)
            BAR: GBAA3321(serC)
            BAA: BA_3823
            BAT: BAS3079
            BCE: BC3249
            BCA: BCE_3285(serC)
            BCZ: BCZK2969(serC)
            BCY: Bcer98_2086
            BTK: BT9727_3023(serC)
            BTL: BALH_2946
            BLI: BL05093(serC)
            BLD: BLi01082(serC)
            BCL: ABC1531(serC)
            BAY: RBAM_010260(serC)
            BPU: BPUM_0948(serC)
            GKA: GK0649
            GTN: GTNG_0559
            LMO: lmo2825(serC)
            LMF: LMOf2365_2816(serC)
            LIN: lin2957(serC)
            LWE: lwe2755(serC)
            LLA: L0083(serC)
            LLC: LACR_0619
            LLM: llmg_0565(serC)
            SAN: gbs1621(serC)
            SMU: SMU.1656(serC)
            STC: str1529(serC)
            STL: stu1529(serC)
            SSA: SSA_1715(serC)
            LPL: lp_0204(serC)
            LSL: LSL_0091(serC)
            CTH: Cthe_0295
            CBE: Cbei_0075
            DSY: DSY4684
            MTU: Rv0884c(serC)
            MTC: MT0907
            MBO: Mb0908c(serC)
            MBB: BCG_0936c(serC)
            MLE: ML2136(serC)
            MPA: MAP0823c(serC)
            MAV: MAV_1012
            MSM: MSMEG_5684
            MVA: Mvan_5033
            MGI: Mflv_1718
            MMC: Mmcs_4464
            MKM: Mkms_4551
            MJL: Mjls_4847
            CGL: NCgl0794(cgl0828)
            CGB: cg0948(serC)
            CEF: CE0903
            CDI: DIP0784
            CJK: jk0425(serC)
            NFA: nfa6550(serC)
            RHA: RHA1_ro04992(serC)
            SCO: SCO4366(SCD19.21c)
            SMA: SAV3883(serC)
            LXX: Lxx17890(serC)
            ART: Arth_0793
            AAU: AAur_1016
            PAC: PPA0483
            NCA: Noca_0730
            TFU: Tfu_0246
            FRA: Francci3_0082
            FAL: FRAAL0110(serC)
            ACE: Acel_0114
            SEN: SACE_0630(serC)
            BLO: BL1660(serC)
            BAD: BAD_0383(serC)
            RBA: RB6246(serC)
            LIL: LA0366(serC)
            LBJ: LBJ_2753(serC)
            LBL: LBL_0318(serC)
            ANA: all1683
            AVA: Ava_1171
            BTH: BT_1153
            BFR: BF2018
            BFS: BF2072(serC)
            PGI: PG1278(serC)
            SRU: SRU_2207(serC)
            CHU: CHU_0995(serC)
            GFO: GFO_1470(serC)
            FJO: Fjoh_2462
            FPS: FP0640(serC)
            RRS: RoseRS_2214
            RCA: Rcas_3363
            MAC: MA2304(serC)
            MBA: Mbar_A1294
            MMA: MM_2911
STRUCTURES  PDB: 1BJN  1BJO  1BT4  1W23  1W3U  2BHX  2BI1  2BI2  2BI3  2BI5  
                 2BI9  2BIA  2BIE  2BIG  2C0R  2FYF  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.52
            ExPASy - ENZYME nomenclature database: 2.6.1.52
            ExplorEnz - The Enzyme Database: 2.6.1.52
            ERGO genome analysis and discovery system: 2.6.1.52
            BRENDA, the Enzyme Database: 2.6.1.52
            CAS: 9030-90-4
///
ENTRY       EC 2.6.1.53       Obsolete  Enzyme
NAME        Transferred to 1.4.1.13
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
COMMENT     Transferred entry: now EC 1.4.1.13, glutamate synthase (NADPH) (EC
            2.6.1.53 created 1972, deleted 1976)
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.53
            ExPASy - ENZYME nomenclature database: 2.6.1.53
            ExplorEnz - The Enzyme Database: 2.6.1.53
            ERGO genome analysis and discovery system: 2.6.1.53
            BRENDA, the Enzyme Database: 2.6.1.53
///
ENTRY       EC 2.6.1.54                 Enzyme
NAME        pyridoxamine-phosphate transaminase;
            pyridoxamine phosphate aminotransferase;
            pyridoxamine 5'-phosphate-alpha-ketoglutarate transaminase;
            pyridoxamine 5'-phosphate transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     pyridoxamine-5'-phosphate:2-oxoglutarate aminotransferase
            (D-glutamate-forming)
REACTION    pyridoxamine 5'-phosphate + 2-oxoglutarate = pyridoxal 5'-phosphate
            + D-glutamate [RN:R01580]
ALL_REAC    R01580;
            (other) R01147 R05839
SUBSTRATE   pyridoxamine 5'-phosphate [CPD:C00647];
            2-oxoglutarate [CPD:C00026]
PRODUCT     pyridoxal 5'-phosphate [CPD:C00018];
            D-glutamate [CPD:C00217]
COMMENT     Also acts, more slowly, on pyridoxamine.
REFERENCE   1
  AUTHORS   Tani, Y., Ukita, M. and Ogata, K.
  TITLE     Studies on vitamin B6 metabolism in microorganisms. Part X. Further
            purification and characterization of pyridoxamine
            5'-phosphate-alpha-ketoglutarate transaminase from Clostridium
            kainantoi.
  JOURNAL   Agric. Biol. Chem. 36 (1972) 181-188.
  ORGANISM  Clostridium kainantoi
PATHWAY     PATH: map00750  Vitamin B6 metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.54
            ExPASy - ENZYME nomenclature database: 2.6.1.54
            ExplorEnz - The Enzyme Database: 2.6.1.54
            ERGO genome analysis and discovery system: 2.6.1.54
            BRENDA, the Enzyme Database: 2.6.1.54
            CAS: 9074-84-4
///
ENTRY       EC 2.6.1.55                 Enzyme
NAME        taurine---2-oxoglutarate transaminase;
            taurine aminotransferase;
            taurine transaminase;
            taurine---alpha-ketoglutarate aminotransferase;
            taurine---glutamate transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     taurine:2-oxoglutarate aminotransferase
REACTION    taurine + 2-oxoglutarate = sulfoacetaldehyde + L-glutamate
            [RN:R01684]
ALL_REAC    R01684;
            (other) R00908
SUBSTRATE   taurine [CPD:C00245];
            2-oxoglutarate [CPD:C00026]
PRODUCT     sulfoacetaldehyde [CPD:C00593];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also acts on
            D,L-3-amino-isobutanoate, beta-alanine and 3-aminopropanesulfonate.
            Involved in the microbial utilization of beta-alanine.
REFERENCE   1  [PMID:5012173]
  AUTHORS   Toyama S, Misono H, Soda K.
  TITLE     Crystalline taurine: -ketoglutarate aminotransferase from
            Achromobacter superficialis.
  JOURNAL   Biochem. Biophys. Res. Commun. 46 (1972) 1374-9.
  ORGANISM  Achromobacter superficialis
REFERENCE   2  [PMID:12471498]
  AUTHORS   Cook AM, Denger K.
  TITLE     Dissimilation of the C2 sulfonates.
  JOURNAL   Arch. Microbiol. 179 (2002) 1-6.
  ORGANISM  Achromobacter superficialis
PATHWAY     PATH: map00410  beta-Alanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.55
            ExPASy - ENZYME nomenclature database: 2.6.1.55
            ExplorEnz - The Enzyme Database: 2.6.1.55
            ERGO genome analysis and discovery system: 2.6.1.55
            BRENDA, the Enzyme Database: 2.6.1.55
            CAS: 9076-52-2
///
ENTRY       EC 2.6.1.56                 Enzyme
NAME        1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol transaminase;
            guanidinoaminodideoxy-scyllo-inositol-pyruvate aminotransferase;
            L-alanine-N-amidino-3-(or 5-)keto-scyllo-inosamine transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol:pyruvate
            aminotransferase
REACTION    1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol + pyruvate =
            1D-1-guanidino-1-deoxy-3-dehydro-scyllo-inositol + L-alanine
            [RN:R03502]
ALL_REAC    R03502
SUBSTRATE   1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol [CPD:C01298];
            pyruvate [CPD:C00022]
PRODUCT     1D-1-guanidino-1-deoxy-3-dehydro-scyllo-inositol [CPD:C04673];
            L-alanine [CPD:C00041]
COMMENT     L-Glutamate and L-glutamine can also act as amino donors.
REFERENCE   1  [PMID:4376579]
  AUTHORS   Walker JB.
  TITLE     Enzymatic reactions involved in streptomycin biosynthesis and
            metabolism.
  JOURNAL   Lloydia. 34 (1971) 363-71.
  ORGANISM  Streptomyces bikiniensis, Streptomyces griseus
REFERENCE   2  [PMID:5781017]
  AUTHORS   Walker JB, Walker MS.
  TITLE     Streptomycin biosynthesis. Transamination reactions involving
            inosamines and inosadiamines.
  JOURNAL   Biochemistry. 8 (1969) 763-70.
  ORGANISM  Streptomyces bikiniensis
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.56
            ExPASy - ENZYME nomenclature database: 2.6.1.56
            ExplorEnz - The Enzyme Database: 2.6.1.56
            ERGO genome analysis and discovery system: 2.6.1.56
            BRENDA, the Enzyme Database: 2.6.1.56
            CAS: 57127-19-2
///
ENTRY       EC 2.6.1.57                 Enzyme
NAME        aromatic-amino-acid transaminase;
            aromatic amino acid aminotransferase;
            aromatic aminotransferase;
            ArAT
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     aromatic-amino-acid:2-oxoglutarate aminotransferase
REACTION    an aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid +
            L-glutamate [RN:R03120]
ALL_REAC    R03120 > R00694 R00734;
            (other) R01731 R07396
SUBSTRATE   aromatic amino acid [CPD:C01021];
            2-oxoglutarate [CPD:C00026]
PRODUCT     aromatic oxo acid [CPD:C00972];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. L-Methionine can also act as donor,
            but more slowly; oxaloacetate can act as acceptor. Controlled
            proteolysis converts the enzyme into EC 2.6.1.1 aspartate
            transaminase.
REFERENCE   1  [PMID:236311]
  AUTHORS   Mavrides C, Orr W.
  TITLE     Multispecific aspartate and aromatic amino acid aminotransferases in
            Escherichia coli.
  JOURNAL   J. Biol. Chem. 250 (1975) 4128-33.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00271  Methionine metabolism
            PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
            PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
            PATH: map00401  Novobiocin biosynthesis
            PATH: map00950  Alkaloid biosynthesis I
ORTHOLOGY   KO: K00832  aromatic-amino-acid transaminase
GENES       ECO: b4054(tyrB)
            ECJ: JW4014(tyrB)
            ECE: Z5652(tyrB)
            ECS: ECs5036
            ECC: c5031(tyrB)
            ECI: UTI89_C4629(tyrB)
            ECP: ECP_4273
            ECV: APECO1_2411(tyrB)
            ECW: EcE24377A_4606(tyrB)
            ECX: EcHS_A4294(tyrB)
            STY: STY4444(tyrB)
            STT: t4154(tyrB)
            SPT: SPA4065(tyrB)
            SEC: SC4127(tyrB)
            STM: STM4248(tyrB)
            YPE: YPO0322(tyrB)
            YPK: y0579(tyrB)
            YPM: YP_0477(tyrB)
            YPA: YPA_3963
            YPN: YPN_3348
            YPP: YPDSF_3650
            YPS: YPTB0377(tyrB)
            YPI: YpsIP31758_3763(tyrB)
            SFL: SF4151(tyrB)
            SFX: S3579(tyrB)
            SFV: SFV_4159(tyrB)
            SSN: SSON_4234(tyrB)
            SBO: SBO_4063(tyrB)
            SDY: SDY_4520(tyrB)
            ECA: ECA3670(tyrB)
            PLU: plu4357(tyrB)
            SGL: SG2131
            ENT: Ent638_0258
            SPE: Spro_4445
            HIP: CGSHiEE_05760
            HIQ: CGSHiGG_10005
            XFA: XF0036
            XFT: PD0026(tyrB)
            XCC: XCC0097(tyrB)
            XCB: XC_0100
            XCV: XCV0101
            XAC: XAC0125(tyrB)
            XOO: XOO0016(tyrB)
            XOM: XOO_0017(XOO0017)
            VFI: VFA0283
            PAE: PA0870(phhC) PA3139
            PAU: PA14_53010(phhC)
            PPU: PP_1972(tyrB-1) PP_3590(tyrB-2)
            PPF: Pput_2182
            PST: PSPTO_2163(aspC) PSPTO_5339(tyrB)
            PSB: Psyr_1973 Psyr_4898
            PSP: PSPPH_1939(aspC) PSPPH_4927(tyrB)
            PFL: PFL_2045(tyrB)
            PEN: PSEEN1635(tyrB) PSEEN2670(tyrB-2) PSEEN3894(phhC)
            PMY: Pmen_3114
            PAR: Psyc_1403(tyrB)
            PRW: PsycPRwf_0225
            ACI: ACIAD0112(tyrB)
            AHA: AHA_0624
            NME: NMB1678
            NMA: NMA1937(tyrB)
            NMC: NMC1596(tyrB)
            NGO: NGO1329
            CVI: CV_0331(tyrB2) CV_2382(tyrB1)
            RSO: RSc1010(tyrB)
            REH: H16_A1151(tyrB1) H16_B1081(tyrB2)
            RME: Rmet_1018 Rmet_4927
            BMA: BMAA0667(tyrB-1) BMAA0879(tyrB-2)
            BMV: BMASAVP1_1738(tyrB-2)
            BML: BMA10299_0016(tyrB-2) BMA10299_0798(tyrB-1)
            BMN: BMA10247_A0916(tyrB-2) BMA10247_A1762(tyrB-1)
            BXE: Bxe_A3154 Bxe_B1222
            BPS: BPSS0355(tyrB) BPSS0808(tyrB1) BPSS2200(tyrB2)
            BPM: BURPS1710b_A1321(tyrB2) BURPS1710b_A1919(tyrB)
                 BURPS1710b_A2395(tyrB1)
            BPL: BURPS1106A_A0506(tyrB-2) BURPS1106A_A1111(tyrB)
                 BURPS1106A_A2971(tyrB)
            BPD: BURPS668_A0603(tyrB-2) BURPS668_A1187(tyrB)
                 BURPS668_A3097(tyrB)
            BTE: BTH_II1593 BTH_II2037 BTH_II2280
            BPE: BP1795(tyrB) BP2858(tyrB)
            BPA: BPP0970(tyrB) BPP2024(tyrB)
            BBR: BB1182(tyrB) BB2272(tyrB)
            MPT: Mpe_A2293 Mpe_A3682
            HAR: HEAR2244(tyrB)
            MMS: mma_1247(tyrB)
            EBA: ebA5437(tyrB) ebA596(pat)
            AZO: azo1610(tyrB)
            DAR: Daro_2002
            BRA: BRADO3492
            BBT: BBta_0622(tyrB) BBta_4224
            SIL: SPO3720(tyrB)
            SIT: TM1040_2635
            RSP: RSP_0886(tyrB)
            RSH: Rsph17029_2545
            RSQ: Rsph17025_0121
            JAN: Jann_0028
            RDE: RD1_0935(tyrB)
            PDE: Pden_0630
            SPD: SPD_0041(araT)
            LSL: LSL_0307(araT) LSL_0835(araT)
            LDB: Ldb0441
            LCA: LSEI_2157
            CTA: CTA_0692(tyrB)
            PMB: A9601_09831(ilvE)
            PMC: P9515_09601(ilvE)
            PMF: P9303_14901(ilvE)
            PMG: P9301_09811(ilvE)
            PME: NATL1_10051(ilvE)
STRUCTURES  PDB: 1AY4  1AY5  1AY8  2AY1  2AY2  2AY3  2AY4  2AY5  2AY6  2AY7  
                 2AY8  2AY9  3TAT  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.57
            ExPASy - ENZYME nomenclature database: 2.6.1.57
            ExplorEnz - The Enzyme Database: 2.6.1.57
            ERGO genome analysis and discovery system: 2.6.1.57
            BRENDA, the Enzyme Database: 2.6.1.57
            CAS: 37332-38-0
///
ENTRY       EC 2.6.1.58                 Enzyme
NAME        phenylalanine(histidine) transaminase;
            phenylalanine (histidine) aminotransferase;
            phenylalanine(histidine):pyruvate aminotransferase;
            histidine:pyruvate aminotransferase;
            L-phenylalanine(L-histidine):pyruvate aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-phenylalanine:pyruvate aminotransferase
REACTION    L-phenylalanine + pyruvate = phenylpyruvate + L-alanine [RN:R00692]
ALL_REAC    R00692
SUBSTRATE   L-phenylalanine [CPD:C00079];
            pyruvate [CPD:C00022]
PRODUCT     phenylpyruvate [CPD:C00166];
            L-alanine [CPD:C00041]
COMMENT     L-Histidine and L-tyrosine can act instead of L-phenylalanine; in
            the reverse reaction, L-methionine, L-serine and L-glutamine can
            replace L-alanine.
REFERENCE   1  [PMID:14070]
  AUTHORS   Minatogawa Y, Noguchi T, Kido R.
  TITLE     Species distribution and properties of hepatic phenylalanine
            (histidine):pyruvate aminotransferase.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 358 (1977) 59-67.
  ORGANISM  rat [GN:rno], mouse [GN:mmu], human [GN:hsa], guinea pig, rabbit,
            pig [GN:ssc], dog [GN:cfa], chicken [GN:gga]
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.58
            ExPASy - ENZYME nomenclature database: 2.6.1.58
            ExplorEnz - The Enzyme Database: 2.6.1.58
            ERGO genome analysis and discovery system: 2.6.1.58
            BRENDA, the Enzyme Database: 2.6.1.58
            CAS: 72560-98-6
///
ENTRY       EC 2.6.1.59                 Enzyme
NAME        dTDP-4-amino-4,6-dideoxygalactose transaminase;
            thymidine diphosphoaminodideoxygalactose aminotransferase;
            thymidine diphosphate 4-keto-6-deoxy-D-glucose transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     dTDP-4,6-dideoxy-D-galactose:2-oxoglutarate aminotransferase
REACTION    dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutarate =
            dTDP-4-dehydro-6-deoxy-D-galactose + L-glutamate [RN:R04438]
ALL_REAC    R04438
SUBSTRATE   dTDP-4-amino-4,6-dideoxy-D-galactose [CPD:C04346];
            2-oxoglutarate [CPD:C00026]
PRODUCT     dTDP-4-dehydro-6-deoxy-D-galactose [CPD:C04269];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:4928644]
  AUTHORS   Oashi H, Matsuhashi M, Matsuhashi S.
  TITLE     Thymidine diphosphate 4-acetamido-4,6-dideoxyhexoses. IV.
            Purification and properties of thymidine diphosphate
            4-keto-6-deoxy-D-glucose transaminase from Pasteurella
            pseudotuberculosis.
  JOURNAL   J. Biol. Chem. 246 (1971) 2325-30.
  ORGANISM  Pasteurella pseudotuberculosis
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.59
            ExPASy - ENZYME nomenclature database: 2.6.1.59
            ExplorEnz - The Enzyme Database: 2.6.1.59
            ERGO genome analysis and discovery system: 2.6.1.59
            BRENDA, the Enzyme Database: 2.6.1.59
            CAS: 72560-97-5
///
ENTRY       EC 2.6.1.60                 Enzyme
NAME        aromatic-amino-acid---glyoxylate transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     aromatic-amino-acid:glyoxylate aminotransferase
REACTION    an aromatic amino acid + glyoxylate = an aromatic oxo acid + glycine
            [RN:R03121]
ALL_REAC    R03121
SUBSTRATE   aromatic amino acid [CPD:C01021];
            glyoxylate [CPD:C00048]
PRODUCT     aromatic oxo acid [CPD:C00972];
            glycine [CPD:C00037]
COMMENT     Phenylalanine, kynurenine, tyrosine and histidine can act as amino
            donors; glyoxylate, pyruvate and hydroxypyruvate can act as amino
            acceptors.
REFERENCE   1  [PMID:25837]
  AUTHORS   Harada I, Noguchi T, Kido R.
  TITLE     Purification and characterization of aromatic-amino-acid-glyoxylate
            aminotransferase from monkey and rat liver.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 359 (1978) 481-8.
  ORGANISM  rat [GN:rno], monkey
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.60
            ExPASy - ENZYME nomenclature database: 2.6.1.60
            ExplorEnz - The Enzyme Database: 2.6.1.60
            ERGO genome analysis and discovery system: 2.6.1.60
            BRENDA, the Enzyme Database: 2.6.1.60
            CAS: 67185-76-6
///
ENTRY       EC 2.6.1.61       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
COMMENT     Deleted entry: (R)-3-amino-2-methylpropionate transaminase. Enzyme
            is identical to EC 2.6.1.40, (R)-3-amino-2-methylpropionate-pyruvate
            transaminase (EC 2.6.1.61 created 1982, deleted 2004)
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.61
            ExPASy - ENZYME nomenclature database: 2.6.1.61
            ExplorEnz - The Enzyme Database: 2.6.1.61
            ERGO genome analysis and discovery system: 2.6.1.61
            BRENDA, the Enzyme Database: 2.6.1.61
///
ENTRY       EC 2.6.1.62                 Enzyme
NAME        adenosylmethionine---8-amino-7-oxononanoate transaminase;
            7,8-diaminonanoate transaminase;
            7,8-diaminononanoate transaminase;
            DAPA transaminase;
            7,8-diaminopelargonic acid aminotransferase;
            DAPA aminotransferase;
            7-keto-8-aminopelargonic acid;
            diaminopelargonate synthase;
            7-keto-8-aminopelargonic acid aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     S-adenosyl-L-methionine:8-amino-7-oxononanoate aminotransferase
REACTION    S-adenosyl-L-methionine + 8-amino-7-oxononanoate =
            S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
            [RN:R03231]
ALL_REAC    R03231
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            8-amino-7-oxononanoate [CPD:C01092]
PRODUCT     S-adenosyl-4-methylthio-2-oxobutanoate [CPD:C04425];
            7,8-diaminononanoate [CPD:C01037]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     S-adenosylhomocysteine can also act as donor.
REFERENCE   1
  AUTHORS   Izumi, Y., Sato, K., Tani, Y. and Ogata, K.
  TITLE     Purification of 7-keto-8-aminopelargonic acid-7,8-diaminopelargonic
            acid aminotransferase, an enzyme involved in biotin synthesis, from
            Brevibacterium divaricatum.
  JOURNAL   Agric. Biol. Chem. 37 (1973) 2683-2684.
  ORGANISM  Brevibacterium divaricatum
REFERENCE   2
  AUTHORS   Izumi, Y., Sato, K., Tani, Y. and Ogata, K.
  TITLE     7,8-Diaminopelargonic acid aminotransferase, an enzyme involved in
            biotin synthesis by microorganisms.
  JOURNAL   Agric. Biol. Chem. 39 (1975) 175-181.
  ORGANISM  Brevibacterium divaricatum
REFERENCE   3
  AUTHORS   Stoner, G.L. and Eisenberg, M.A.
  TITLE     Purification and properties of 7,8-diaminopelargonic acid
            aminotransferase. An enzyme in the biotin biosynthetic pathway.
  JOURNAL   J. Biol. Chem. 250 (1973) 4029-4036.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00780  Biotin metabolism
ORTHOLOGY   KO: K00833  adenosylmethionine-8-amino-7-oxononanoate
                        aminotransferase
GENES       ATH: AT5G57590(BIO1)
            CME: CMG023C
            SCE: YNR058W(BIO3)
            PIC: PICST_38281(YOD2) PICST_38592(BIO3)
            ANI: AN6644.2
            AFM: AFUA_6G03660
            AOR: AO090009000590
            CNE: CNB00630
            UMA: UM02915.1
            ECO: b0774(bioA)
            ECJ: JW0757(bioA)
            ECE: Z0993(bioA)
            ECS: ECs0852
            ECC: c0853(bioA)
            ECI: UTI89_C0772(bioA)
            ECP: ECP_0788
            ECV: APECO1_1315(bioA)
            ECW: EcE24377A_0837(bioA)
            ECX: EcHS_A0829(bioA)
            STY: STY0826(bioA)
            STT: t2094(bioA)
            SPT: SPA1959(bioA)
            SEC: SC0791(bioA)
            STM: STM0793(bioA)
            YPE: YPO1150(bioA)
            YPK: y3032(bioA)
            YPM: YP_1010(bioA)
            YPA: YPA_1057
            YPN: YPN_2851
            YPS: YPTB1181(bioA)
            YPI: YpsIP31758_2845(bioA)
            SFL: SF0725(bioA)
            SFX: S0765(bioA)
            SFV: SFV_0758(bioA)
            SSN: SSON_0753(bioA)
            SBO: SBO_0661(bioA)
            SDY: SDY_0832(bioA)
            ECA: ECA2826(bioA)
            PLU: plu1484(bioA)
            BUC: BU292(bioA)
            BAS: BUsg281(bioA)
            BAB: bbp273(bioA)
            WBR: WGLp452(bioA)
            SGL: SG0902
            HIT: NTHI1579(bioA)
            HIP: CGSHiEE_05355
            HIQ: CGSHiGG_00185
            HDU: HD1685(bioA)
            PMU: PM1900(bioA)
            APL: APL_0942(bioA)
            XFA: XF0189
            XFT: PD0155(bioA)
            XCC: XCC2345(bioA) XCC2884(bioA)
            XCB: XC_1225 XC_1771
            XCV: XCV2655 XCV3202
            XAC: XAC2477(bioA) XAC3068(bioA)
            XOO: XOO1787(bioA)
            XOM: XOO_1690(XOO1690)
            VCH: VC1111
            VCO: VC0395_A0629(bioA)
            VVU: VV1_2944 VV1_2945
            VVY: VV1326
            VPA: VP1112
            VFI: VFA0748
            PPR: PBPRA2330
            PAE: PA0420(bioA)
            PAU: PA14_03900(spuC) PA14_05460(bioA)
            PAP: PSPA7_0520(bioA)
            PPU: PP_4984(bioA)
            PST: PSPTO_5075(bioA)
            PSB: Psyr_0454
            PSP: PSPPH_0445(bioA1)
            PFL: PFL_5804(bioA)
            PFO: Pfl_5287
            PEN: PSEEN2885 PSEEN5047(bioA) PSEEN5296
            PMY: Pmen_0413
            PAR: Psyc_0328(bioA)
            PCR: Pcryo_0361
            ACI: ACIAD0856(bioA)
            SON: SO_2741(bioA)
            SDN: Sden_1657
            SFR: Sfri_1474
            SHE: Shewmr4_2360
            SHM: Shewmr7_2432
            SHN: Shewana3_2520
            ILO: IL1325(bioA)
            CPS: CPS_2593(bioA)
            PHA: PSHAa1610(bioA)
            PAT: Patl_2558
            SDE: Sde_2227
            MAQ: Maqu_3049
            CBU: CBU_1008(bioA)
            CBD: COXBU7E912_1039(bioA)
            LPN: lpg1471(bioA)
            LPF: lpl1557(bioA)
            LPP: lpp1427(bioA)
            MCA: MCA0017(bioA)
            FTU: FTT0938(bioA)
            FTF: FTF0938(bioA)
            FTL: FTL_1271
            FTH: FTH_1244(bioA)
            FTN: FTN_0816(bioA)
            TCX: Tcr_0277
            NOC: Noc_0122
            AEH: Mlg_0362
            HHA: Hhal_0932
            HCH: HCH_01529(bioA)
            CSA: Csal_1162
            ABO: ABO_0256(bioA)
            AHA: AHA_1488(bioA)
            BCI: BCI_0245(bioA)
            VOK: COSY_0123(bioA)
            NME: NMB0732
            NMA: NMA0942(bioA)
            NMC: NMC0685(bioA)
            NGO: NGO0308
            CVI: CV_2025 CV_4210(bioA)
            RSO: RSc1477(bioA)
            REU: Reut_A0147
            REH: H16_A0180(bioA) H16_B2123
            RME: Rmet_0114
            BMA: BMA0100(bioA)
            BMV: BMASAVP1_A3080(bioA)
            BML: BMA10299_A2014(bioA)
            BMN: BMA10247_2272(bioA)
            BXE: Bxe_A4263 Bxe_B0941
            BVI: Bcep1808_3026
            BUR: Bcep18194_A5472 Bcep18194_A6275 Bcep18194_A6344
                 Bcep18194_B0934 Bcep18194_C6646
            BCN: Bcen_2317
            BCH: Bcen2424_2931 Bcen2424_2995 Bcen2424_4780
            BAM: Bamb_2980 Bamb_3042
            BPS: BPSL0367(bioA) BPSL2335
            BPM: BURPS1710b_0574(bioA) BURPS1710b_2787 BURPS1710b_A2021
            BPL: BURPS1106A_0412(bioA)
            BPD: BURPS668_0391(bioA)
            BTE: BTH_I0340(bioA) BTH_I1829 BTH_II1947
            PNU: Pnuc_0155
            BPE: BP2165(bioA)
            BPA: BPP1776(bioA)
            BBR: BB3332(bioA)
            POL: Bpro_0900
            AAV: Aave_3841
            MPT: Mpe_A0528
            HAR: HEAR0100(bioA)
            MMS: mma_0120(bioA)
            NEU: NE0026(bioA)
            NET: Neut_0208
            NMU: Nmul_A2364
            EBA: ebA6019(bioA)
            AZO: azo1888(bioA)
            DAR: Daro_2895
            TBD: Tbd_0093
            MFA: Mfla_0377
            HPY: HP0976
            HPJ: jhp0910(bioA)
            HPA: HPAG1_0957
            HHE: HH1210(bioA)
            HAC: Hac_0635(bioA)
            WSU: WS0234(bioA)
            TDN: Tmden_1290
            CJE: Cj0307(bioA)
            CJR: CJE0352(bioA)
            CJJ: CJJ81176_0329(bioA)
            CJU: C8J_0284(bioA)
            CJD: JJD26997_1657(bioA)
            CFF: CFF8240_0513(bioA)
            CHA: CHAB381_0700
            ABU: Abu_1636(bioA)
            NIS: NIS_1030(bioA)
            SUN: SUN_0618(bioA)
            GSU: GSU1582(bioA)
            GME: Gmet_1580
            PCA: Pcar_1460
            DVU: DVU2559(bioA)
            DDE: Dde_2656
            LIP: LI0426(bioA)
            DPS: DP2548(bioA)
            ADE: Adeh_0069
            MXA: MXAN_0318
            SAT: SYN_02563
            SFU: Sfum_3719
            AMA: AM556(bioA)
            APH: APH_0482(bioA)
            ERU: Erum3870(bioA)
            ERW: ERWE_CDS_03990(bioA)
            ERG: ERGA_CDS_03950(bioA)
            ECN: Ecaj_0376
            ECH: ECH_0666(bioA)
            NSE: NSE_0618(bioA)
            PUB: SAR11_0808(bioA)
            MLO: mll5828 mll6003 mll9097
            ATU: Atu4000(bioA)
            ATC: AGR_L_1704(bioA)
            RET: RHE_CH01316(bioA) RHE_CH02145(ypch00704)
                 RHE_CH03090(ypch01076) RHE_PF00202 RHE_PF00349(ypf00179)
            RLE: RL1467 pRL120043 pRL120612
            BME: BMEII0778
            BMF: BAB2_0747(bioA)
            BMS: BRA0489(bioA)
            BMB: BruAb2_0733(bioA)
            BOV: BOV_A0427(bioA)
            BJA: blr2099(bioA)
            BBT: BBta_1920 BBta_2779(bioA)
            RPA: RPA2970(bioA)
            RPB: RPB_4342
            RPC: RPC_2097
            RPD: RPD_4238
            RPE: RPE_3402
            NWI: Nwi_2419
            NHA: Nham_2814
            CCR: CC_1577
            RSP: RSP_0943(yhxA) RSP_3261(bioA)
            RDE: RD1_0172 RD1_2337
            MMR: Mmar10_1347
            HNE: HNE_1247(bioA)
            ZMO: ZMO1918(bioA)
            NAR: Saro_1343
            SAL: Sala_1475
            GOX: GOX0719
            GBE: GbCGDNIH1_0500
            RRU: Rru_A1254 Rru_A2041
            MAG: amb2763
            MGM: Mmc1_0037
            BSU: BG11524(bioA)
            BHA: BH0782
            BAN: BA1636 BA4341(bioA)
            BAR: GBAA1636 GBAA4341(bioA)
            BAA: BA_2152 BA_4800
            BAT: BAS1519 BAS4028
            BCE: BC1610 BC4119
            BCA: BCE_1727 BCE_4189(bioA)
            BCZ: BCZK1481(bioA) BCZK3875(bioA)
            BTK: BT9727_1491(bioA) BT9727_3861(bioA)
            BTL: BALH_1122(bioA) BALH_1448(bioA) BALH_3735(bioA)
            BLI: BL00953(bioA)
            BLD: BLi00767(bioA)
            BCL: ABC3786
            BAY: RBAM_018280(bioA)
            BPU: BPUM_0880(bioA)
            GKA: GK1427 GK3016
            SAU: SA2214(bioA)
            SAV: SAV2426(bioA)
            SAM: MW2349(bioA)
            SAR: SAR2516(bioA)
            SAS: SAS2317
            SAC: SACOL2427(bioA)
            SAB: SAB2307c(bioA)
            SAA: SAUSA300_2372(bioA)
            SAO: SAOUHSC_02715
            SEP: SE0180
            SER: SERP2395(bioA)
            CAC: CAC1362(bioA)
            CNO: NT01CX_1469(bioA)
            CTH: Cthe_0025
            CKL: CKL_0938(bioA)
            CSC: Csac_0306
            MTU: Rv1568(bioA)
            MTC: MT1619(bioA)
            MBO: Mb1595(bioA)
            MBB: BCG_1621(bioA)
            MLE: ML1216(bioA)
            MPA: MAP1274(bioA)
            MAV: MAV_3206(bioA)
            MSM: MSMEG_3188(bioA)
            MMC: Mmcs_3078
            CGL: NCgl2515(cgl2604)
            CGB: cg2885(bioA)
            CEF: CE1421(bioA)
            CDI: DIP1191(bioA)
            NFA: nfa18180(bioA)
            RHA: RHA1_ro01055(bioA1) RHA1_ro06796(bioA2)
            SCO: SCO1245(2SCG1.20)
            SMA: SAV7092(bioA)
            AAU: AAur_1089(bioA)
            PAC: PPA0967
            FRA: Francci3_1490
            FAL: FRAAL2296(bioA)
            SEN: SACE_3329(bioA2) SACE_4684(bioA)
            FNU: FN1002
            RBA: RB3292(bioA)
            CPN: CPn1041(bioA)
            CPA: CP0811
            CPJ: CPj1041(bioA)
            CPT: CpB1081
            CAB: CAB688(bioA)
            CFE: CF0295(bioA)
            LIL: LA2142(bioA)
            LIC: LIC11778(bioA)
            LBJ: LBJ_1871(bioA)
            LBL: LBL_1413(bioA)
            SYW: SYNW0629(bioA)
            SYC: syc1466_c(bioA)
            SYF: Synpcc7942_0031 Synpcc7942_0034
            SYD: Syncc9605_2052
            SYE: Syncc9902_0620
            SYG: sync_2343(bioA)
            SYR: SynRCC307_1941(bioA)
            SYX: SynWH7803_2048(bioA)
            TEL: tll1935
            PMA: Pro1626(cioA)
            PMM: PMM1472(bioA)
            PMT: PMT1493(bioA)
            PMN: PMN2A_1003
            PMI: PMT9312_1565
            PMB: A9601_16741(bioA)
            PMC: P9515_16521(bioA)
            PMF: P9303_04531(bioA)
            PMG: P9301_16621(bioA)
            PMH: P9215_17401(bioA)
            PME: NATL1_18721(bioA)
            BTH: BT_1442
            BFR: BF1603
            BFS: BF1617(bioA)
            PGI: PG2080(bioA)
            CHU: CHU_2976(bioA)
            GFO: GFO_3563(bioA)
            FPS: FP2328(bioA)
            CTE: CT0047(bioA)
            CCH: Cag_0083
            PLT: Plut_2065
            AAE: aq_170(bioA)
            MMP: MMP0865
STRUCTURES  PDB: 1DTY  1MGV  1MLY  1MLZ  1QJ3  1QJ5  1S06  1S07  1S08  1S09  
                 1S0A  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.62
            ExPASy - ENZYME nomenclature database: 2.6.1.62
            ExplorEnz - The Enzyme Database: 2.6.1.62
            ERGO genome analysis and discovery system: 2.6.1.62
            BRENDA, the Enzyme Database: 2.6.1.62
            CAS: 37259-71-5
///
ENTRY       EC 2.6.1.63                 Enzyme
NAME        kynurenine---glyoxylate transaminase;
            kynurenine-glyoxylate aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-kynurenine:glyoxylate aminotransferase (cyclizing)
REACTION    L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate +
            glycine [RN:R01957]
ALL_REAC    R01957
SUBSTRATE   L-kynurenine [CPD:C00328];
            glyoxylate [CPD:C00048]
PRODUCT     4-(2-aminophenyl)-2,4-dioxobutanoate [CPD:C01252];
            glycine [CPD:C00037]
COMMENT     Acts, more slowly, on L-phenylalanine, L-histidine and L-tyrosine.
REFERENCE   1
  AUTHORS   Harada, I.
  TITLE     [Glucagen inducible kynurenine aminotransferase.].
  JOURNAL   Wakayama Igaku 31 (1980) 61-68.
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.63
            ExPASy - ENZYME nomenclature database: 2.6.1.63
            ExplorEnz - The Enzyme Database: 2.6.1.63
            ERGO genome analysis and discovery system: 2.6.1.63
            BRENDA, the Enzyme Database: 2.6.1.63
            CAS: 74506-33-5
///
ENTRY       EC 2.6.1.64                 Enzyme
NAME        glutamine---phenylpyruvate transaminase;
            glutamine transaminase K;
            glutamine-phenylpyruvate aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-glutamine:phenylpyruvate aminotransferase
REACTION    L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine
            [RN:R01375]
ALL_REAC    R01375
SUBSTRATE   L-glutamine [CPD:C00064];
            phenylpyruvate [CPD:C00166]
PRODUCT     2-oxoglutaramate [CPD:C00940];
            L-phenylalanine [CPD:C00079]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. L-Methionine, L-histidine and
            L-tyrosine can act as donors. The enzyme has little activity on
            pyruvate and glyoxylate (cf. EC 2.6.1.15 glutamine---pyruvate
            transaminase).
REFERENCE   1  [PMID:727444]
  AUTHORS   Cooper AJ.
  TITLE     Purification of soluble and mitochondrial glutamine transaminase K
            from rat kidney. Use of a sensitive assay involving transamination
            between L-phenylalanine and alpha-keto-gamma-methiolbutyrate.
  JOURNAL   Anal. Biochem. 89 (1978) 451-60.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4822504]
  AUTHORS   Cooper AJ, Meister A.
  TITLE     Isolation and properties of a new glutamine transaminase from rat
            kidney.
  JOURNAL   J. Biol. Chem. 249 (1974) 2554-61.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K00834  glutamine-phenylpyruvate transaminase
GENES       HSA: 883(CCBL1)
            MMU: 70266(Ccbl1)
            RNO: 311844(Ccbl1)
            CFA: 491310(CCBL1)
            TET: TTHERM_00313800
STRUCTURES  PDB: 1YIY  1YIZ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.64
            ExPASy - ENZYME nomenclature database: 2.6.1.64
            ExplorEnz - The Enzyme Database: 2.6.1.64
            ERGO genome analysis and discovery system: 2.6.1.64
            BRENDA, the Enzyme Database: 2.6.1.64
            CAS: 68518-06-9
///
ENTRY       EC 2.6.1.65                 Enzyme
NAME        N6-acetyl-beta-lysine transaminase;
            epsilon-acetyl-beta-lysine aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     6-acetamido-3-aminohexanoate:2-oxoglutarate aminotransferase
REACTION    6-acetamido-3-aminohexanoate + 2-oxoglutarate =
            6-acetamido-3-oxohexanoate + L-glutamate [RN:R04028]
ALL_REAC    R04028;
            (other) R04029
SUBSTRATE   6-acetamido-3-aminohexanoate [CPD:C03846];
            2-oxoglutarate [CPD:C00026]
PRODUCT     6-acetamido-3-oxohexanoate [CPD:C03682];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:44448]
  AUTHORS   Bozler G, Robertson JM, Ohsugi M, Hensley C, Barker HA.
  TITLE     Metabolism of L-beta-lysine in a Pseudomonas: conversion of
            6-N-acetyl-L-beta-lysine to 3-keto-6-acetamidohexanoate and of
            4-aminobutyrate to succinic semialdehyde by different transaminases.
  JOURNAL   Arch. Biochem. Biophys. 197 (1979) 226-35.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.65
            ExPASy - ENZYME nomenclature database: 2.6.1.65
            ExplorEnz - The Enzyme Database: 2.6.1.65
            ERGO genome analysis and discovery system: 2.6.1.65
            BRENDA, the Enzyme Database: 2.6.1.65
            CAS: 71768-10-0
///
ENTRY       EC 2.6.1.66                 Enzyme
NAME        valine---pyruvate transaminase;
            transaminase C;
            valine-pyruvate aminotransferase;
            alanine-oxoisovalerate aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-valine:pyruvate aminotransferase
REACTION    L-valine + pyruvate = 3-methyl-2-oxobutanoate + L-alanine
            [RN:R01215]
ALL_REAC    R01215
SUBSTRATE   L-valine [CPD:C00183];
            pyruvate [CPD:C00022]
PRODUCT     3-methyl-2-oxobutanoate [CPD:C00141];
            L-alanine [CPD:C00041]
COMMENT     Different from EC 2.6.1.42, branched-chain-amino-acid-transaminase.
REFERENCE   1  [PMID:396446]
  AUTHORS   Falkinham JO 3rd.
  TITLE     Identification of a mutation affecting an
            alanine-alpha-ketoisovalerate transaminase activity in Escherichia
            coli K-12.
  JOURNAL   Mol. Gen. Genet. 176 (1979) 147-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:13034817]
  AUTHORS   RUDMAN D, MEISTER A.
  TITLE     Transamination in Escherichia coli.
  JOURNAL   J. Biol. Chem. 200 (1953) 591-604.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00290  Valine, leucine and isoleucine biosynthesis
ORTHOLOGY   KO: K00835  valine--pyruvate aminotransferase
GENES       CME: CML079C
            PIC: PICST_28702(ARO9.2) PICST_89470(YEY2)
            CGR: CAGL0I06578g
            ECO: b3572(avtA)
            ECJ: JW5652(avtA)
            ECE: Z4997(avtA)
            ECS: ECs4455
            ECC: c4393(avtA)
            ECI: UTI89_C4114(avtA)
            ECP: ECP_3676
            ECV: APECO1_2878(avtA)
            STY: STY4133(avtA)
            STT: t3854(avtA)
            SPT: SPA3516(avtA)
            STM: STM3665(avtA)
            YPE: YPO4082(avtA)
            YPK: y4099(avtA)
            YPM: YP_3991(avtA3)
            YPA: YPA_3003
            YPN: YPN_3726
            YPS: YPTB3907(avtA)
            SFL: SF3616(avtA)
            SFX: S4153(avtA)
            SFV: SFV_3968(avtA)
            SBO: SBO_3580(avtA)
            SDY: SDY_3707(avtA)
            ECA: ECA4386(avtA)
            PLU: plu0291(avtA)
            SGL: SG0009
            XCC: XCC1838(avtA)
            XCB: XC_2351
            XCV: XCV1904
            XAC: XAC1858(avtA)
            XOO: XOO2895(avtA)
            XOM: XOO_2745(XOO2745)
            VCH: VC0019(avtA)
            VCO: VC0395_A2500(avtA)
            VVU: VV1_0992
            VVY: VV0018
            VPA: VP0019
            VFI: VF0014(avtA)
            PPR: PBPRA0054
            PAR: Psyc_2118(avtA)
            PCR: Pcryo_2440
            PHA: PSHAa1703(avtA)
            SDE: Sde_0903
            HCH: HCH_01903(avtA)
            AHA: AHA_0009
            NME: NMB1823
            NMA: NMA0636(avtA)
            NMC: NMC0395(avtA)
            NGO: NGO0082(avtA)
            BPM: BURPS1710b_A0496
            BLI: BL00232(alaTA)
            BLD: BLi04237(ywfG)
            SEN: SACE_4564(avtA)
            LIL: LA0171
            LIC: LIC10150(avtA)
            SYC: syc1840_c
            SYF: Synpcc7942_2258
            TEL: tll1742
            ANA: alr2811
            AVA: Ava_1090(avtA)
            DGE: Dgeo_2084
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.66
            ExPASy - ENZYME nomenclature database: 2.6.1.66
            ExplorEnz - The Enzyme Database: 2.6.1.66
            ERGO genome analysis and discovery system: 2.6.1.66
            BRENDA, the Enzyme Database: 2.6.1.66
            CAS: 132421-38-6
///
ENTRY       EC 2.6.1.67                 Enzyme
NAME        2-aminohexanoate transaminase;
            norleucine transaminase;
            norleucine (leucine) aminotransferase;
            leucine L-norleucine: 2-oxoglutarate aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-2-aminohexanoate:2-oxoglutarate aminotransferase
REACTION    L-2-aminohexanoate + 2-oxoglutarate = 2-oxohexanoate + L-glutamate
            [RN:R03053]
ALL_REAC    R03053
SUBSTRATE   L-2-aminohexanoate [CPD:C01933];
            2-oxoglutarate [CPD:C00026]
PRODUCT     2-oxohexanoate [CPD:C00902];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also acts on L-leucine and, more
            slowly, on L-isoleucine, L-2-aminopentanoate and L-aspartate.
REFERENCE   1  [PMID:3622507]
  AUTHORS   Der Garabedian PA, Vermeersch JJ.
  TITLE     Candida L-norleucine,leucine:2-oxoglutarate aminotransferase.
            Purification and properties.
  JOURNAL   Eur. J. Biochem. 167 (1987) 141-7.
  ORGANISM  Candida guilliermondii
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.67
            ExPASy - ENZYME nomenclature database: 2.6.1.67
            ExplorEnz - The Enzyme Database: 2.6.1.67
            ERGO genome analysis and discovery system: 2.6.1.67
            BRENDA, the Enzyme Database: 2.6.1.67
            CAS: 111310-35-1
///
ENTRY       EC 2.6.1.68                 Enzyme
NAME        ornithine(lysine) transaminase;
            ornithine(lysine) aminotransferase;
            lysine/ornithine:2-oxoglutarate aminotransferase;
            L-ornithine(L-lysine):2-oxoglutarate-aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-ornithine:2-oxoglutarate-aminotransferase
REACTION    L-ornithine + 2-oxoglutarate = 3,4-dihydro-2H-pyrrole-2-carboxylate
            + L-glutamate + H2O [RN:R00668]
ALL_REAC    R00668
SUBSTRATE   L-ornithine [CPD:C00077];
            2-oxoglutarate [CPD:C00026]
PRODUCT     3,4-dihydro-2H-pyrrole-2-carboxylate [CPD:C04322];
            L-glutamate [CPD:C00025];
            H2O [CPD:C00001]
COMMENT     The enzyme from Trichomonas vaginalis also acts on L-lysine,
            producing 2,3,4,5-tetrahydropyridine-2-carboxylate.
REFERENCE   1  [PMID:3095639]
  AUTHORS   Lowe PN, Rowe AF.
  TITLE     Aminotransferase activities in Trichomonas vaginalis.
  JOURNAL   Mol. Biochem. Parasitol. 21 (1986) 65-74.
  ORGANISM  Trichomonas vaginalis
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.68
            ExPASy - ENZYME nomenclature database: 2.6.1.68
            ExplorEnz - The Enzyme Database: 2.6.1.68
            ERGO genome analysis and discovery system: 2.6.1.68
            BRENDA, the Enzyme Database: 2.6.1.68
            CAS: 105542-39-0
///
ENTRY       EC 2.6.1.69       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
COMMENT     Deleted entry: N2-acetylornithine 5-transaminase. Enzyme is
            identical to EC 2.6.1.11, acetylornithine transaminase (EC 2.6.1.69
            created 1989, deleted 2004)
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.69
            ExPASy - ENZYME nomenclature database: 2.6.1.69
            ExplorEnz - The Enzyme Database: 2.6.1.69
            ERGO genome analysis and discovery system: 2.6.1.69
            BRENDA, the Enzyme Database: 2.6.1.69
///
ENTRY       EC 2.6.1.70                 Enzyme
NAME        aspartate---phenylpyruvate transaminase;
            aspartate-phenylpyruvate aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-aspartate:phenylpyruvate aminotransferase
REACTION    L-aspartate + phenylpyruvate = oxaloacetate + L-phenylalanine
            [RN:R00695]
ALL_REAC    R00695
SUBSTRATE   L-aspartate [CPD:C00049];
            phenylpyruvate [CPD:C00166]
PRODUCT     oxaloacetate [CPD:C00036];
            L-phenylalanine [CPD:C00079]
COMMENT     The enzyme from Pseudomonas putida also acts on
            4-hydroxy-phenylpyruvate and, more slowly, on L-glutamate and
            L-histidine.
REFERENCE   1
  AUTHORS   Holger, Z. and Kula, M.-R.
  TITLE     Isolation and characterization of a highly inducible
            L-aspartate-phenylpyruvate transaminase from Pseudomonas putida.
  JOURNAL   J. Biotechnol. 3 (1985) 19-31.
  ORGANISM  Pseudomonas putida [GN:ppu]
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.70
            ExPASy - ENZYME nomenclature database: 2.6.1.70
            ExplorEnz - The Enzyme Database: 2.6.1.70
            ERGO genome analysis and discovery system: 2.6.1.70
            BRENDA, the Enzyme Database: 2.6.1.70
            CAS: 99533-45-6
///
ENTRY       EC 2.6.1.71                 Enzyme
NAME        lysine---pyruvate 6-transaminase;
            lysine-pyruvate aminotransferase;
            Lys-AT
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-lysine:pyruvate aminotransferase
REACTION    L-lysine + pyruvate = L-2-aminoadipate 6-semialdehyde + L-alanine
            [RN:R00453]
ALL_REAC    R00453
SUBSTRATE   L-lysine [CPD:C00047];
            pyruvate [CPD:C00022]
PRODUCT     L-2-aminoadipate 6-semialdehyde [CPD:C04076];
            L-alanine [CPD:C00041]
REFERENCE   1
  AUTHORS   Schmidt, H., Bode, R. and Birnbaum, D.
  TITLE     A novel enzyme, L-lysine : pyruvate aminotransferase, catalyses the
            first step of lysine catabolism in Pichia guilliermondii.
  JOURNAL   FEMS Microbiol. Lett. 49 (1988) 203-206.
  ORGANISM  Pichia guilliermondii
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.71
            ExPASy - ENZYME nomenclature database: 2.6.1.71
            ExplorEnz - The Enzyme Database: 2.6.1.71
            ERGO genome analysis and discovery system: 2.6.1.71
            BRENDA, the Enzyme Database: 2.6.1.71
            CAS: 114189-79-6
///
ENTRY       EC 2.6.1.72                 Enzyme
NAME        D-4-hydroxyphenylglycine transaminase;
            D-hydroxyphenylglycine aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     D-4-hydroxyphenylglycine:2-oxoglutarate aminotransferase
REACTION    D-4-hydroxyphenylglycine + 2-oxoglutarate =
            4-hydroxyphenylglyoxylate + L-glutamate [RN:R04234]
ALL_REAC    R04234
SUBSTRATE   D-4-hydroxyphenylglycine [CPD:C03493];
            2-oxoglutarate [CPD:C00026]
PRODUCT     4-hydroxyphenylglyoxylate [CPD:C03590];
            L-glutamate [CPD:C00025]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:16525953]
  AUTHORS   Hildebrand F, van Griensven M, Giannoudis P, Schreiber T, Frink M,
            Probst C, Grotz M, Krettek C, Pape HC.
  TITLE     Impact of hypothermia on the immunologic response after trauma and
            elective surgery.
  JOURNAL   Surg. Technol. Int. 14 (2005) 41-50.
REFERENCE   2  [PMID:16525953]
  AUTHORS   Hildebrand F, van Griensven M, Giannoudis P, Schreiber T, Frink M,
            Probst C, Grotz M, Krettek C, Pape HC.
  TITLE     Impact of hypothermia on the immunologic response after trauma and
            elective surgery.
  JOURNAL   Surg. Technol. Int. 14 (2005) 41-50.
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.72
            ExPASy - ENZYME nomenclature database: 2.6.1.72
            ExplorEnz - The Enzyme Database: 2.6.1.72
            ERGO genome analysis and discovery system: 2.6.1.72
            BRENDA, the Enzyme Database: 2.6.1.72
            CAS: 117444-05-0
///
ENTRY       EC 2.6.1.73                 Enzyme
NAME        methionine---glyoxylate transaminase;
            methionine-glyoxylate aminotransferase;
            MGAT
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-methionine:glyoxylate aminotransferase
REACTION    L-methionine + glyoxylate = 4-methylthio-2-oxobutanoate + glycine
            [RN:R00652]
ALL_REAC    R00652
SUBSTRATE   L-methionine [CPD:C00073];
            glyoxylate [CPD:C00048]
PRODUCT     4-methylthio-2-oxobutanoate [CPD:C01180];
            glycine [CPD:C00037]
COMMENT     L-Glutamate can also act as donor.
REFERENCE   1
  AUTHORS   Glover, J.R., Chapple, C.C.S., Rothwell, S., Tober, I. and Ellis,
            B.E.
  TITLE     Allylglucosinolate biosynthesis in Brassica carinata.
  JOURNAL   Phytochemistry 27 (1988) 1345-1348.
  ORGANISM  Brassica carinata
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.73
            ExPASy - ENZYME nomenclature database: 2.6.1.73
            ExplorEnz - The Enzyme Database: 2.6.1.73
            ERGO genome analysis and discovery system: 2.6.1.73
            BRENDA, the Enzyme Database: 2.6.1.73
            CAS: 116155-75-0
///
ENTRY       EC 2.6.1.74                 Enzyme
NAME        cephalosporin-C transaminase;
            cephalosporin C aminotransferase;
            L-alanine:cephalosporin-C aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     cephalosporin-C:2-oxoglutarate aminotransferase
REACTION    (7R)-7-(5-carboxy-5-oxopentanoyl)aminocephalosporinate + D-glutamate
            = cephalosporin C + 2-oxoglutarate [RN:R03063]
ALL_REAC    R03063
SUBSTRATE   (7R)-7-(5-carboxy-5-oxopentanoyl)aminocephalosporinate [CPD:C04712];
            D-glutamate [CPD:C00217]
PRODUCT     cephalosporin C [CPD:C00916];
            2-oxoglutarate [CPD:C00026]
COMMENT     A number of D-amino acids, including D-alanine, D-aspartate and
            D-methionine can also act as amino-group donors. Although this
            enzyme acts on several free D-amino acids, it differs from EC
            2.6.1.21, D-alanine transaminase, in that it can use cephalosporin C
            as an amino donor.
REFERENCE   1  [PMID:3228235]
  AUTHORS   Aretz W, Sauber K.
  TITLE     Novel D-amino acid transaminase.
  JOURNAL   Ann. N. Y. Acad. Sci. 542 (1988) 366-70.
PATHWAY     PATH: map00311  Penicillin and cephalosporin biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.74
            ExPASy - ENZYME nomenclature database: 2.6.1.74
            ExplorEnz - The Enzyme Database: 2.6.1.74
            ERGO genome analysis and discovery system: 2.6.1.74
            BRENDA, the Enzyme Database: 2.6.1.74
            CAS: 122096-91-7
///
ENTRY       EC 2.6.1.75                 Enzyme
NAME        cysteine-conjugate transaminase;
            cysteine conjugate aminotransferase;
            cysteine-conjugate alpha-ketoglutarate transaminase (CAT-1)
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     S-(4-bromophenyl)-L-cysteine:2-oxoglutarate aminotransferase
REACTION    S-(4-bromophenyl)-L-cysteine + 2-oxoglutarate =
            S-(4-bromophenyl)mercaptopyruvate + L-glutamate [RN:R04338]
ALL_REAC    R04338
SUBSTRATE   S-(4-bromophenyl)-L-cysteine [CPD:C03900];
            2-oxoglutarate [CPD:C00026]
PRODUCT     S-(4-bromophenyl)mercaptopyruvate;
            L-glutamate [CPD:C00025]
COMMENT     A number of cysteine conjugates can also act.
REFERENCE   1  [PMID:2852419]
  AUTHORS   Tomisawa H, Ichimoto N, Takanohashi Y, Ichihara S, Fukazawa H,
            Tateishi M.
  TITLE     Purification and characterization of cysteine conjugate
            transaminases from rat liver.
  JOURNAL   Xenobiotica. 18 (1988) 1015-28.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.75
            ExPASy - ENZYME nomenclature database: 2.6.1.75
            ExplorEnz - The Enzyme Database: 2.6.1.75
            ERGO genome analysis and discovery system: 2.6.1.75
            BRENDA, the Enzyme Database: 2.6.1.75
            CAS: 117698-05-2
///
ENTRY       EC 2.6.1.76                 Enzyme
NAME        diaminobutyrate---2-oxoglutarate transaminase;
            L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase;
            2,4-diaminobutyrate 4-aminotransferase;
            diaminobutyrate aminotransferase;
            DABA aminotransferase;
            DAB aminotransferase;
            EctB;
            diaminibutyric acid aminotransferase;
            L-2,4-diaminobutyrate:2-oxoglutarate 4-aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-2,4-diaminobutanoate:2-oxoglutarate 4-aminotransferase
REACTION    L-2,4-diaminobutanoate + 2-oxoglutarate = L-aspartate 4-semialdehyde
            + L-glutamate [RN:R06977]
ALL_REAC    R06977
SUBSTRATE   L-2,4-diaminobutanoate [CPD:C03283];
            2-oxoglutarate [CPD:C00026]
PRODUCT     L-aspartate 4-semialdehyde [CPD:C00441];
            L-glutamate [CPD:C00025]
COMMENT     A pyridoxal-phosphate protein that requires potassium for activity
            [4]. In the proteobacterium Acinetobacter baumannii, this enzyme is
            cotranscribed with the neighbouring ddc gene that also encodes EC
            4.1.1.86, diaminobutyrate decarboxylase. Differs from EC 2.6.1.46,
            diaminobutyrate---pyruvate transaminase, which has pyruvate as the
            amino-group acceptor. This is the first enzyme in the
            ectoine-biosynthesis pathway, the other enzymes involved being EC
            2.3.1.178, diaminobutyrate acetyltransferase and EC 4.2.1.108,
            ectoine synthase [3,4].
REFERENCE   1  [PMID:9260954]
  AUTHORS   Ikai H, Yamamoto S.
  TITLE     Identification and analysis of a gene encoding
            L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase involved in
            the 1,3-diaminopropane production pathway in Acinetobacter
            baumannii.
  JOURNAL   J. Bacteriol. 179 (1997) 5118-25.
  ORGANISM  Acinetobacter baumannii [GN:acb]
REFERENCE   2  [PMID:9514614]
  AUTHORS   Ikai H, Yamamoto S.
  TITLE     Two genes involved in the 1,3-diaminopropane production pathway in
            Haemophilus influenzae.
  JOURNAL   Biol. Pharm. Bull. 21 (1998) 170-3.
  ORGANISM  Haemophilus influenzae
REFERENCE   3
  AUTHORS   Peters, P., Galinski, E.A. and Truper, H.G.
  TITLE     The biosynthesis of ectoine.
  JOURNAL   FEMS Microbiol. Lett. 71 (1990) 157-162.
  ORGANISM  Ectothiorhodospira halochloris, Halomonas elongata
REFERENCE   4  [PMID:9864317]
  AUTHORS   Ono H, Sawada K, Khunajakr N, Tao T, Yamamoto M, Hiramoto M, Shinmyo
            A, Takano M, Murooka Y.
  TITLE     Characterization of biosynthetic enzymes for ectoine as a compatible
            solute in a moderately halophilic eubacterium, Halomonas elongata.
  JOURNAL   J. Bacteriol. 181 (1999) 91-9.
  ORGANISM  Halomonas elongata
REFERENCE   5  [PMID:11823218]
  AUTHORS   Kuhlmann AU, Bremer E.
  TITLE     Osmotically regulated synthesis of the compatible solute ectoine in
            Bacillus pasteurii and related Bacillus spp.
  JOURNAL   Appl. Environ. Microbiol. 68 (2002) 772-83.
  ORGANISM  Bacillus pasteurii
REFERENCE   6  [PMID:9141677]
  AUTHORS   Louis P, Galinski EA.
  TITLE     Characterization of genes for the biosynthesis of the compatible
            solute ectoine from Marinococcus halophilus and osmoregulated
            expression in Escherichia coli.
  JOURNAL   Microbiology. 143 ( Pt 4) (1997) 1141-9.
  ORGANISM  Marinococcus halophilus
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K00836  diaminobutyrate-2-oxoglutarate transaminase
GENES       ECA: ECA2243(dat)
            PLU: plu2191 plu3538 plu4263
            SGL: SGP1_0046
            HIN: HI0949
            HIP: CGSHiEE_07230
            HIQ: CGSHiGG_08315
            HDU: HD0729(dat)
            HSO: HS_0926(dat)
            MSU: MS0829(argD)
            APL: APL_1974(argD)
            VCH: VCA0824
            VVU: VV1_3050
            VVY: VV1236
            VPA: VP1721 VP1942
            VFI: VFA1123
            PPR: PBPRA2230
            PAE: PA2413
            PAU: PA14_33500(pvdH)
            PPU: PP_2800 PP_4223
            PST: PSPTO_2136(daT)
            PSB: Psyr_1925 Psyr_1946 Psyr_2583 Psyr_2619
            PSP: PSPPH_1912 PSPPH_2750 PSPPH_3754
            PFL: PFL_4179 PFL_4988(ectB)
            PFO: Pfl_3932
            PEN: PSEEN3669(dat)
            ACI: ACIAD1210(dat)
            ACB: A1S_2454
            TCX: Tcr_0220 Tcr_0519
            AEH: Mlg_1191
            CVI: CV_2804
            RSO: RSp1424(ectB)
            REH: H16_B1692
            BMA: BMA3149 BMAA1647
            BMV: BMASAVP1_A0119
            BML: BMA10299_A1469
            BMN: BMA10247_2897
            BPS: BPSL0476 BPSS1635
            BPM: BURPS1710b_0696(rhbA) BURPS1710b_A0697
            BPA: BPP1889(ectB)
            BBR: BB3219(ectB)
            AAV: Aave_4220
            HAR: HEAR3379(ectB)
            WSU: WS0855
            MLO: mlr5943
            SME: SMa2400(rhbA)
            SIT: TM1040_0552
            HNE: HNE_1640(ectB)
            SAL: Sala_2950
            BHA: BH0919 BH2624
            BAN: BA3312
            BAR: GBAA3312
            BAA: BA_3812
            BAT: BAS3069
            BTL: BALH_2936(ectB)
            BLI: BL01336
            BLD: BLi01183
            BCL: ABC0335(ectB)
            BPU: BPUM_1019
            OIH: OB0518
            MSM: MSMEG_3900(ectB)
            MMC: Mmcs_4191
            NFA: nfa12990
            SCO: SCO1865(SCI39.12)
            SMA: SAV2467 SAV6397(ectB)
            TFU: Tfu_0301
            FRA: Francci3_4054
            FAL: FRAAL6421
            SEN: SACE_0484(ectB)
            RXY: Rxyl_0412
            RBA: RB7275(ectB)
            GVI: gll2223
            ANA: all0396
            AVA: Ava_2839
            HAL: VNG6210G(gabT)
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.76
            ExPASy - ENZYME nomenclature database: 2.6.1.76
            ExplorEnz - The Enzyme Database: 2.6.1.76
            ERGO genome analysis and discovery system: 2.6.1.76
            BRENDA, the Enzyme Database: 2.6.1.76
            CAS: 196622-96-5
///
ENTRY       EC 2.6.1.77                 Enzyme
NAME        taurine---pyruvate aminotransferase;
            Tpa
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     taurine:pyruvate aminotransferase
REACTION    taurine + pyruvate = L-alanine + 2-sulfoacetaldehyde [RN:R05652]
ALL_REAC    R05652
SUBSTRATE   taurine [CPD:C00245];
            pyruvate [CPD:C00022]
PRODUCT     L-alanine [CPD:C00041];
            2-sulfoacetaldehyde [CPD:C00593]
COMMENT     The enzyme from Bilophila wadsworthia requires pyridoxal
            5'-phosphate as a cofactor, is reversible, and catalyses the first
            step of anaerobic taurine degradation. Hypotaurine (i.e.
            2-aminoethanesulfinate) and beta-alanine are also significant donors
            of an amino group. Unlike, EC 2.6.1.55, taurine---2-oxoglutarate
            transaminase, 2-oxoglutarate is not an acceptor of amino groups.
REFERENCE   1  [PMID:11082195]
  AUTHORS   Laue H, Cook AM.
  TITLE     Biochemical and molecular characterization of taurine:pyruvate
            aminotransferase from the anaerobe Bilophila wadsworthia.
  JOURNAL   Eur. J. Biochem. 267 (2000) 6841-8.
  ORGANISM  Bilophila wadsworthia
REFERENCE   2  [PMID:12471498]
  AUTHORS   Cook AM, Denger K.
  TITLE     Dissimilation of the C2 sulfonates.
  JOURNAL   Arch. Microbiol. 179 (2002) 1-6.
  ORGANISM  Pseudomonas aeruginosa, Desulfonispora thiosulfatigenes, Bilophila
            wadsworthia, Alcaligenes defragrans
REFERENCE   3  [PMID:11728723]
  AUTHORS   Masepohl B, Fuhrer F, Klipp W.
  TITLE     Genetic analysis of a Rhodobacter capsulatus gene region involved in
            utilization of taurine as a sulfur source.
  JOURNAL   FEMS. Microbiol. Lett. 205 (2001) 105-11.
  ORGANISM  Rhodobacter capsulatus
PATHWAY     PATH: map00430  Taurine and hypotaurine metabolism
ORTHOLOGY   KO: K03851  taurine-pyruvate aminotransferase
GENES       SIL: SPO0673(tpa)
            RDE: RD1_0981(tpa)
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.77
            ExPASy - ENZYME nomenclature database: 2.6.1.77
            ExplorEnz - The Enzyme Database: 2.6.1.77
            ERGO genome analysis and discovery system: 2.6.1.77
            BRENDA, the Enzyme Database: 2.6.1.77
///
ENTRY       EC 2.6.1.78                 Enzyme
NAME        aspartate---prephenate aminotransferase;
            prephenate transaminase (ambiguous);
            PAT (ambiguous);
            prephenate aspartate aminotransferase;
            L-aspartate:prephenate aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-arogenate:oxaloacetate aminotransferase
REACTION    L-arogenate + oxaloacetate = prephenate + L-aspartate [RN:R01731]
ALL_REAC    R01731
SUBSTRATE   L-arogenate [CPD:C00826];
            oxaloacetate [CPD:C00036]
PRODUCT     prephenate [CPD:C00254];
            L-aspartate [CPD:C00049]
COMMENT     A pyridoxal-phosphate protein. Glutamate can also act as the amino
            donor, but more slowly (cf. EC 2.6.1.79, glutamate---prephenate
            aminotransferase).
REFERENCE   1  [PMID:3196038]
  AUTHORS   De-Eknamkul W, Ellis BE.
  TITLE     Purification and characterization of prephenate aminotransferase
            from Anchusa officinalis cell cultures.
  JOURNAL   Arch. Biochem. Biophys. 267 (1988) 87-94.
  ORGANISM  Anchusa officinalis
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.78
            ExPASy - ENZYME nomenclature database: 2.6.1.78
            ExplorEnz - The Enzyme Database: 2.6.1.78
            ERGO genome analysis and discovery system: 2.6.1.78
            BRENDA, the Enzyme Database: 2.6.1.78
///
ENTRY       EC 2.6.1.79                 Enzyme
NAME        glutamate---prephenate aminotransferase;
            prephenate transaminase (ambiguous);
            PAT (ambiguous);
            L-glutamate:prephenate aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-arogenate:2-oxoglutarate aminotransferase
REACTION    L-arogenate + 2-oxoglutarate = prephenate + L-glutamate [RN:R07276]
ALL_REAC    R07276
SUBSTRATE   L-arogenate [CPD:C00826];
            2-oxoglutarate [CPD:C00026]
PRODUCT     prephenate [CPD:C00254];
            L-glutamate [CPD:C00025]
COMMENT     A pyridoxal-phosphate protein. Aspartate can also act as the amino
            donor, but more slowly (cf. EC 2.6.1.78, aspartate---prephenate
            aminotransferase). The enzyme from higher plants shows a marked
            preference for prephenate as substrate compared to pyruvate,
            phenylpyruvate or 4-hydroxyphenylpyruvate [1].
REFERENCE   1  [PMID:3985619]
  AUTHORS   Bonner CA, Jensen RA.
  TITLE     Novel features of prephenate aminotransferase from cell cultures of
            Nicotiana silvestris.
  JOURNAL   Arch. Biochem. Biophys. 238 (1985) 237-46.
  ORGANISM  Nicotiana silvestris
REFERENCE   2  [PMID:2939644]
  AUTHORS   Siehl DL, Connelly JA, Conn EE.
  TITLE     Tyrosine biosynthesis in Sorghum bicolor: characteristics of
            prephenate aminotransferase.
  JOURNAL   Z. Naturforsch. [C]. 41 (1986) 79-86.
  ORGANISM  Sorghum bicolor [GN:esbi]
REFERENCE   3  [PMID:3298985]
  AUTHORS   Bonner C, Jensen R.
  TITLE     Prephenate aminotransferase.
  JOURNAL   Methods. Enzymol. 142 (1987) 479-87.
  ORGANISM  Nicotiana silvestris, Brevibacterium flavum , Corynebacterium
            glutamicum
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.79
            ExPASy - ENZYME nomenclature database: 2.6.1.79
            ExplorEnz - The Enzyme Database: 2.6.1.79
            ERGO genome analysis and discovery system: 2.6.1.79
            BRENDA, the Enzyme Database: 2.6.1.79
///
ENTRY       EC 2.6.1.80                 Enzyme
NAME        nicotianamine aminotransferase;
            NAAT;
            NAAT-I;
            NAAT-II;
            NAAT-III
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     nicotianamine:2-oxoglutarate aminotransferase; nicotianamine
            transaminase
REACTION    nicotianamine + 2-oxoglutarate = 3"-deamino-3"-oxonicotianamine +
            L-glutamate [RN:R07277]
ALL_REAC    R07277
SUBSTRATE   nicotianamine [CPD:C05324];
            2-oxoglutarate [CPD:C00026]
PRODUCT     3''-deamino-3''-oxonicotianamine [CPD:C15486];
            L-glutamate [CPD:C00025]
COMMENT     A pyridoxal-phosphate protein. This enzyme is produced by grasses.
            They secrete both the nicotianamine and the transaminated product
            into the soil around them. Both compounds chelate iron(II) and
            iron(III); these chelators, called mugineic acid family
            phytosiderophores, are taken up by the grass, which is thereby
            supplied with iron.
REFERENCE   1
  AUTHORS   Kanazawa, K., Higuchi, K., Nishizawa, N.-K., Fushiya, S., Chino, M.
            and Mori, S.
  TITLE     Nicotianamine aminotransferase activities are correlated with the
            phytosiderophore secretions under Fe-deficient conditions in
            Gramineae.
  JOURNAL   J. Exp. Bot. 45 (1994) 1903-1906.
  ORGANISM  Hordeum vulgare [GN:ehvu], oat, Triticum aestivum [GN:etae], Zea
            mays [GN:ezma], Sorghum bicolor [GN:esbi], Oryza sativa [GN:eosa]
REFERENCE   2  [PMID:10557244]
  AUTHORS   Takahashi M, Yamaguchi H, Nakanishi H, Shioiri T, Nishizawa NK, Mori
            S.
  TITLE     Cloning two genes for nicotianamine aminotransferase, a critical
            enzyme in iron acquisition (Strategy II) in graminaceous plants.
  JOURNAL   Plant. Physiol. 121 (1999) 947-56.
  ORGANISM  Hordeum vulgare [GN:ehvu]
REFERENCE   3  [PMID:14699112]
  AUTHORS   Schaaf G, Ludewig U, Erenoglu BE, Mori S, Kitahara T, von Wiren N.
  TITLE     ZmYS1 functions as a proton-coupled symporter for phytosiderophore-
            and nicotianamine-chelated metals.
  JOURNAL   J. Biol. Chem. 279 (2004) 9091-6.
  ORGANISM  Zea mays [GN:ezma]
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.80
            ExPASy - ENZYME nomenclature database: 2.6.1.80
            ExplorEnz - The Enzyme Database: 2.6.1.80
            ERGO genome analysis and discovery system: 2.6.1.80
            BRENDA, the Enzyme Database: 2.6.1.80
///
ENTRY       EC 2.6.1.81                 Enzyme
NAME        succinylornithine transaminase;
            succinylornithine aminotransferase;
            N2-succinylornithine 5-aminotransferase;
            AstC;
            SOAT;
            2-N-succinyl-L-ornithine:2-oxoglutarate 5-aminotransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     N2-succinyl-L-ornithine:2-oxoglutarate 5-aminotransferase
REACTION    N2-succinyl-L-ornithine + 2-oxoglutarate = N-succinyl-L-glutamate
            5-semialdehyde + L-glutamate [RN:R04217]
ALL_REAC    R04217
SUBSTRATE   N2-succinyl-L-ornithine [CPD:C03415];
            2-oxoglutarate [CPD:C00026]
PRODUCT     N-succinyl-L-glutamate 5-semialdehyde [CPD:C05932];
            L-glutamate [CPD:C00025]
COMMENT     A pyridoxal-phosphate protein. Also acts on N2-acetyl-L-ornithine
            and L-ornithine, but more slowly [3]. In Pseudomonas aeruginosa, the
            arginine-inducible succinylornithine transaminase, acetylornithine
            transaminase (EC 2.6.1.11) and ornithine aminotransferase (EC
            2.6.1.13) activities are catalysed by the same enzyme, but this is
            not the case in all species [5]. This is the third enzyme in the
            arginine succinyltransferase (AST) pathway for the catabolism of
            arginine [1]. This pathway converts the carbon skeleton of arginine
            into glutamate, with the concomitant production of ammonia and
            conversion of succinyl-CoA into succinate and CoA. The five enzymes
            involved in this pathway are EC 2.3.1.109 (arginine
            N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine
            dihydrolase), EC 2.6.1.81 (succinylornithine transaminase), EC
            1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC
            3.5.1.96 (succinylglutamate desuccinylase) [3, 6].
REFERENCE   1  [PMID:2865249]
  AUTHORS   Vander Wauven C, Stalon V.
  TITLE     Occurrence of succinyl derivatives in the catabolism of arginine in
            Pseudomonas cepacia.
  JOURNAL   J. Bacteriol. 164 (1985) 882-6.
  ORGANISM  Pseudomonas cepacia
REFERENCE   2  [PMID:9696779]
  AUTHORS   Schneider BL, Kiupakis AK, Reitzer LJ.
  TITLE     Arginine catabolism and the arginine succinyltransferase pathway in
            Escherichia coli.
  JOURNAL   J. Bacteriol. 180 (1998) 4278-86.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:3534538]
  AUTHORS   Cunin R, Glansdorff N, Pierard A, Stalon V.
  TITLE     Biosynthesis and metabolism of arginine in bacteria.
  JOURNAL   Microbiol. Rev. 50 (1986) 314-52.
  ORGANISM  Pseudomonas spp.
REFERENCE   4  [PMID:9393691]
  AUTHORS   Itoh Y.
  TITLE     Cloning and characterization of the aru genes encoding enzymes of
            the catabolic arginine succinyltransferase pathway in Pseudomonas
            aeruginosa.
  JOURNAL   J. Bacteriol. 179 (1997) 7280-90.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   5  [PMID:3129535]
  AUTHORS   Stalon V, Vander Wauven C, Momin P, Legrain C.
  TITLE     Catabolism of arginine, citrulline and ornithine by Pseudomonas and
            related bacteria.
  JOURNAL   J. Gen. Microbiol. 133 (1987) 2487-95.
  ORGANISM  Pseudomonas cepacia, Pseudomonas putida [GN:ppu], Pseudomonas
            indigofera
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K00840  succinylornithine aminotransferase
GENES       ECO: b1748(astC)
            ECJ: JW1737(astC)
            ECE: Z2780(cstC)
            ECS: ECs2454
            ECC: c2148(cstC)
            ECI: UTI89_C1943(astC)
            ECP: ECP_1694
            ECV: APECO1_817(cstC)
            ECW: EcE24377A_1970(astC)
            ECX: EcHS_A1831
            STY: STY1811(astC)
            STT: t1182(astC)
            SPT: SPA1541(astC)
            SEC: SC1326(astC)
            STM: STM1303(astC)
            YPE: YPO1962(astC)
            YPK: y2349(cstC)
            YPM: YP_1707(cstC)
            YPA: YPA_1344
            YPS: YPTB1959(astC)
            SSN: SSON_1409(cstC)
            SBO: SBO_1342(cstC)
            PAE: PA0895(aruC)
            ACI: ACIAD1284(astC)
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.81
            ExPASy - ENZYME nomenclature database: 2.6.1.81
            ExplorEnz - The Enzyme Database: 2.6.1.81
            ERGO genome analysis and discovery system: 2.6.1.81
            BRENDA, the Enzyme Database: 2.6.1.81
///
ENTRY       EC 2.6.1.82                 Enzyme
NAME        putrescine aminotransferase;
            putrescine-alpha-ketoglutarate transaminase;
            YgjG;
            putrescine:alpha-ketoglutarate aminotransferase;
            PAT;
            putrescine:2-oxoglutarate aminotransferase;
            putrescine transaminase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     butane-1,4-diamine:2-oxoglutarate aminotransferase
REACTION    (1) (1a) putrescine + 2-oxoglutarate = 4-aminobutanal + L-glutamate
            [RN:R01155];
            (2) (1b) 4-aminobutanal = 1-pyrroline (spontaneous) [RN:R07408]
ALL_REAC    R01155 R07408
SUBSTRATE   putrescine [CPD:C00134];
            2-oxoglutarate [CPD:C00026];
            4-aminobutanal [CPD:C00555]
PRODUCT     4-aminobutanal [CPD:C00555];
            L-glutamate [CPD:C00025];
            1-pyrroline [CPD:C15668]
COMMENT     A pyridoxal-phosphate protein [3]. The product, 4-aminobutanal,
            spontaneously cyclizes to form 1-pyrroline, which is a substrate for
            EC 1.5.1.35, 1-pyrroline dehydrogenase. Cadaverine and spermidine
            can also act as substrates [3]. Forms part of the
            arginine-catabolism pathway [2].
REFERENCE   1  [PMID:3510672]
  AUTHORS   Prieto-Santos MI, Martin-Checa J, Balana-Fouce R, Garrido-Pertierra
            A.
  TITLE     A pathway for putrescine catabolism in Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 880 (1986) 242-4.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:16023116]
  AUTHORS   Samsonova NN, Smirnov SV, Novikova AE, Ptitsyn LR.
  TITLE     Identification of Escherichia coli K12 YdcW protein as a
            gamma-aminobutyraldehyde dehydrogenase.
  JOURNAL   FEBS. Lett. 579 (2005) 4107-12.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:12617754]
  AUTHORS   Samsonova NN, Smirnov SV, Altman IB, Ptitsyn LR.
  TITLE     Molecular cloning and characterization of Escherichia coli K12 ygjG
            gene.
  JOURNAL   BMC. Microbiol. 3 (2003) 2.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K09251  putrescine aminotransferase
GENES       ECO: b3073(ygjG)
            ECJ: JW5510(ygjG)
            ECE: Z4426(ygjG)
            ECS: ECs3955
            ECC: c3828(ygjG)
            ECI: UTI89_C3511(ygjG)
            ECP: ECP_3163
            ECV: APECO1_3343(ygjG)
            STY: STY3396
            STT: t3138
            SPT: SPA3086(oat)
            SEC: SC3165(oat)
            STM: STM3218(oat)
            SFL: SF3114(ygjG)
            SFX: S3320(ygjG)
            SFV: SFV_3114(ygjG)
            SSN: SSON_3211(ygjG)
            SBO: SBO_2932(ygjG)
            ECA: ECA1543
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.82
            ExPASy - ENZYME nomenclature database: 2.6.1.82
            ExplorEnz - The Enzyme Database: 2.6.1.82
            ERGO genome analysis and discovery system: 2.6.1.82
            BRENDA, the Enzyme Database: 2.6.1.82
///
ENTRY       EC 2.6.1.83                 Enzyme
NAME        LL-diaminopimelate aminotransferase;
            LL-diaminopimelate transaminase;
            LL-DAP aminotransferase;
            LL-DAP-AT
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     LL-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase
REACTION    LL-2,6-diaminoheptanedioate + 2-oxoglutarate =
            (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O
            [RN:R07613]
ALL_REAC    R07613
SUBSTRATE   LL-2,6-diaminoheptanedioate [CPD:C00666];
            2-oxoglutarate [CPD:C00026]
PRODUCT     (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate [CPD:C03972];
            L-glutamate [CPD:C00025];
            H2O [CPD:C00001]
COMMENT     A pyridoxal-phosphate enzyme. In vivo, the reaction occurs in the
            opposite direction to that shown above. This is one of the final
            steps in the lysine-biosynthesis pathway of plants (ranging from
            mosses to flowering plants). meso-Diaminoheptanedioate, an isomer of
            LL-2,6-diaminoheptanedioate, and the structurally related compounds
            lysine and ornithine are not substrates. 2-Oxoglutarate cannot be
            replaced by oxaloacetate or pyruvate. It is not yet known if the
            substrate of the biosynthetic reaction is the cyclic or acyclic form
            of tetrahydropyridine-2,6-dicarboxylate.
REFERENCE   1  [PMID:16361515]
  AUTHORS   Hudson AO, Singh BK, Leustek T, Gilvarg C.
  TITLE     An LL-diaminopimelate aminotransferase defines a novel variant of
            the lysine biosynthesis pathway in plants.
  JOURNAL   Plant. Physiol. 140 (2006) 292-301.
  ORGANISM  Arabidopsis thaliana [GN:ath]
PATHWAY     PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K10206  LL-diaminopimelate aminotransferase
GENES       ATH: AT4G33680(AGD2)
            OSA: 4332563
            CME: CMN323C
            SYN: sll0480
            SYW: SYNW2147
            SYC: syc0687_c(aspB)
            SYF: Synpcc7942_0853
            SYD: Syncc9605_0311
            SYE: Syncc9902_2031
            SYG: sync_0372(aspB)
            CYA: CYA_2460
            CYB: CYB_1421(aspB)
            TEL: tll2102
            ANA: alr5103
            AVA: Ava_2354
            PMA: Pro1655
            PMM: PMM1500
            PMT: PMT1791
            PMN: PMN2A_1066
            PMI: PMT9312_1592
            PMB: A9601_17031
            PMC: P9515_16801
            PMF: P9303_23741
            PMG: P9301_16911
            PME: NATL1_19411
            TER: Tery_3293
STRUCTURES  PDB: 2Z1Z  2Z20  
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.83
            ExPASy - ENZYME nomenclature database: 2.6.1.83
            ExplorEnz - The Enzyme Database: 2.6.1.83
            ERGO genome analysis and discovery system: 2.6.1.83
            BRENDA, the Enzyme Database: 2.6.1.83
///
ENTRY       EC 2.6.1.84                 Enzyme
NAME        arginine---pyruvate transaminase;
            arginine:pyruvate transaminase;
            AruH
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     L-arginine:pyruvate aminotransferase
REACTION    L-arginine + pyruvate = 5-guanidino-2-oxopentanoate + L-alanine
SUBSTRATE   L-arginine [CPD:C00062];
            pyruvate [CPD:C00022]
PRODUCT     5-guanidino-2-oxopentanoate [CPD:C03771];
            L-alanine [CPD:C00041]
COMMENT     A pyridoxal-phosphate protein. While L-arginine is the best
            substrate, the enzyme exhibits broad substrate specificity, with
            L-lysine, L-methionine, L-leucine, ornithine and L-glutamine also
            able to act as substrates, but more slowly. Pyruvate cannot be
            replaced by 2-oxoglutarate as amino-group acceptor. This is the
            first catalytic enzyme of the arginine transaminase pathway for
            L-arginine utilization in Pseudomonas aeruginosa. This pathway is
            only used when the major route of arginine catabolism, i.e. the
            arginine succinyltransferase pathway, is blocked.
REFERENCE   1  [PMID:17416668]
  AUTHORS   Yang Z, Lu CD.
  TITLE     Characterization of an arginine:pyruvate transaminase in arginine
            catabolism of Pseudomonas aeruginosa PAO1.
  JOURNAL   J. Bacteriol. 189 (2007) 3954-9.
REFERENCE   2  [PMID:17416670]
  AUTHORS   Yang Z, Lu CD.
  TITLE     Functional genomics enables identification of genes of the arginine
            transaminase pathway in Pseudomonas aeruginosa.
  JOURNAL   J. Bacteriol. 189 (2007) 3945-53.
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.84
            ExPASy - ENZYME nomenclature database: 2.6.1.84
            ExplorEnz - The Enzyme Database: 2.6.1.84
            ERGO genome analysis and discovery system: 2.6.1.84
            BRENDA, the Enzyme Database: 2.6.1.84
///
ENTRY       EC 2.6.1.85                 Enzyme
NAME        aminodeoxychorismate synthase;
            ADC synthase;
            4-amino-4-deoxychorismate synthase;
            PabB;
            chorismate:L-glutamine amido-ligase (incorrect)
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
SYSNAME     chorismate:L-glutamine aminotransferase
REACTION    chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
SUBSTRATE   chorismate [CPD:C00251];
            L-glutamine [CPD:C00064]
PRODUCT     4-amino-4-deoxychorismate [CPD:C11355];
            L-glutamate [CPD:C00025]
COMMENT     The enzyme is composed of two parts, PabA and PabB. In the absence
            of PabA and glutamine, PabB converts ammonia and chorismate into
            4-amino-4-deoxychorismate (in the presence of Mg2+). PabA converts
            glutamine into glutamate only in the presence of stoichiometric
            amounts of PabB. This enzyme is coupled with EC 4.1.3.38,
            aminodeoxychorismate lyase, to form 4-aminobenzoate.
REFERENCE   1  [PMID:2251281]
  AUTHORS   Ye QZ, Liu J, Walsh CT.
  TITLE     p-Aminobenzoate synthesis in Escherichia coli: purification and
            characterization of PabB as aminodeoxychorismate synthase and enzyme
            X as aminodeoxychorismate lyase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 9391-5.
REFERENCE   2  [PMID:7592344]
  AUTHORS   Viswanathan VK, Green JM, Nichols BP.
  TITLE     Kinetic characterization of 4-amino 4-deoxychorismate synthase from
            Escherichia coli.
  JOURNAL   J. Bacteriol. 177 (1995) 5918-23.
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K01664  para-aminobenzoate synthetase component II
            KO: K01665  para-aminobenzoate synthetase component I
            KO: K03342  para-aminobenzoate synthetase
GENES       SCE: YNR033W(ABZ1)
            AGO: AGOS_AER267W
            CGR: CAGL0M10934g
            AFM: AFUA_6G04820
            ECO: b1812(pabB) b3360(pabA)
            ECJ: JW1801(pabB) JW3323(pabA)
            ECE: Z2855(pabB) Z4721(pabA)
            ECS: ECs2521 ECs4211
            ECC: c2217(pabB) c4135(pabA)
            ECI: UTI89_C2008(pabB) UTI89_C3863(pabA)
            ECP: ECP_1755 ECP_3451
            ECV: APECO1_3095(pabA) APECO1_869(pabB)
            ECW: EcE24377A_2040(pabB) EcE24377A_3830(pabA)
            ECX: EcHS_A1902 EcHS_A3557 EcHS_A3634
            STY: STY1954(pabB) STY4327(pabA)
            STT: t1053(pabB) t4036(pabA)
            SPT: SPA1049(pabB) SPA3335(pabA)
            SEC: SC1818(pabB) SC3403(pabA)
            STM: STM1824(pabB) STM3469(pabA)
            YPE: YPO0169(pabA) YPO1773(pabB)
            YPK: y2535(pabB) y3953(pabA)
            YPM: YP_0171(pabA) YP_1620(pabB)
            YPA: YPA_1145 YPA_3300
            YPN: YPN_2350 YPN_3895
            YPP: YPDSF_0097 YPDSF_1350
            YPS: YPTB1649(pabB) YPTB3732(pabA)
            YPI: YpsIP31758_3948(pabA)
            YEN: YE1781(pabB) YE3958(pabA)
            SFL: SF1416(pabB) SF3379(pabA)
            SFX: S1531(pabB) S4384(pabA)
            SFV: SFV_1417(pabB) SFV_3366(pabA)
            SSN: SSON_1348(pabB) SSON_3491(pabA)
            SBO: SBO_1272(pabB) SBO_3342(pabA)
            SDY: SDY_1718(pabB) SDY_3522(pabA)
            ECA: ECA2378(pabB) ECA4066
            PLU: plu0393(pabA) plu2694(pabB) plu3563
            SGL: SG1329 SG2302
            ENT: Ent638_2381 Ent638_3787
            KPN: KPN_02328(pabB) KPN_03746(pabA)
            BFL: Bfl443(pabB) Bfl568(pabA)
            BPN: BPEN_457(pabB) BPEN_588(pabA)
            HIT: NTHI1338
            HIP: CGSHiEE_06185 CGSHiEE_06190
            HIQ: CGSHiGG_09550 CGSHiGG_09555
            HDU: HD0408(pabB)
            HSO: HS_0129(pabB)
            PMU: PM1464(pabB)
            MSU: MS2193(trpE)
            APL: APL_1145(pabB)
            VCH: VC1303 VC2619
            VCO: VC0395_A0921(pabB) VC0395_A2196(pabA)
            VVU: VV1_1311 VV1_1312 VV1_2265
            VVY: VV2080 VV3055
            VPA: VP1875 VP2798
            VFI: VF1179
            PPR: PBPRA0288 PBPRA2410
            PAE: PA1758
            PAU: PA14_41820(pabB)
            PPU: PP_2329(pabB)
            PPF: Pput_3441
            PST: PSPTO_2282(pabB)
            PSB: Psyr_2080
            PSP: PSPPH_2051(pabB)
            PFL: PFL_1856
            PFO: Pfl_1759
            PEN: PSEEN1897
            PMY: Pmen_2540
            PSA: PST_2029(pabB)
            PAR: Psyc_1900(pabB)
            ACI: ACIAD0665(pabB)
            SON: SO_0613(pabA) SO_2221(pabB)
            SDN: Sden_1913 Sden_3196
            SFR: Sfri_2157
            SAZ: Sama_1687
            SBL: Sbal_1917
            SLO: Shew_1903
            SPC: Sputcn32_1806
            SHE: Shewmr4_0607 Shewmr4_2125
            SHM: Shewmr7_2201
            SHN: Shewana3_0606 Shewana3_2303
            SHW: Sputw3181_2219
            ILO: IL1706(pabB) IL2321(pabA)
            CPS: CPS_3614(pabB)
            PHA: PSHAa1165(pabB)
            PAT: Patl_0653 Patl_1627
            SDE: Sde_1671
            PIN: Ping_1978
            MAQ: Maqu_1580
            CBU: CBU_1373(pabB) CBU_1871(pabA)
            CBD: COXBU7E912_0101(pabA)
            LPN: lpg1557
            LPF: lpl1469(pabB)
            LPP: lpp1514(pabB)
            LPC: LPC_0979(pabB)
            MCA: MCA2870(pabB)
            FTU: FTT0945
            FTF: FTF0945
            FTW: FTW_0839
            NOC: Noc_0255
            AEH: Mlg_2489
            HHA: Hhal_2208
            HCH: HCH_02662(pabB)
            CSA: Csal_2424
            MMW: Mmwyl1_2967
            AHA: AHA_2435(pabB) AHA_3181
            ASA: ASA_2293(pabB)
            DNO: DNO_1127
            BCI: BCI_0453(pabB) BCI_0549(pabA)
            VOK: COSY_0476 COSY_0734 COSY_0837
            NME: NMB1970
            NMA: NMA0477
            NGO: NGO2112
            RSO: RSc2633(pabB)
            RME: Rmet_2920
            BMA: BMA2324
            BXE: Bxe_A3959
            BPS: BPSL2825
            BPM: BURPS1710b_3318(pabB)
            BTE: BTH_I1310
            BPE: BP3241
            BPA: BPP3598
            BBR: BB4033
            RFR: Rfer_3314
            POL: Bpro_0904
            MPT: Mpe_A2628
            MMS: mma_3230
            EBA: ebA6309(pabB)
            DAR: Daro_3087
            MFA: Mfla_1648
            HPY: HP0293(pabB)
            HPJ: jhp0278(pabB)
            HPA: HPAG1_0295
            HHE: HH0304(trpE_1)
            HAC: Hac_0553(pabB)
            WSU: WS0689
            TDN: Tmden_0462
            CJE: Cj0861c(pabA) Cj0862c(pabB)
            ABU: Abu_0262(pabB)
            NIS: NIS_0375 NIS_0650(pabA)
            SUN: SUN_0539(pabA) SUN_2069
            GSU: GSU0523(pabB)
            GME: Gmet_3010
            PCA: Pcar_0977
            DVU: DVU0363(pabB)
            DPS: DP0876
            PUB: SAR11_0831(pabB)
            MLO: mlr3005
            MES: Meso_2729
            PLA: Plav_1564
            SME: SMc04013(pabB)
            ATU: Atu1676(pabB)
            ATC: AGR_C_3082
            RET: RHE_CH03550(pabB)
            RLE: RL4069(pabB)
            BME: BMEII0013
            BMS: BRA0080
            BMB: BruAb2_0080
            BJA: bll2091(pabA) bll2092(pabB)
            CCR: CC_2953
            SIL: SPO0924(pabB)
            SIT: TM1040_0633
            RSP: RSP_0817
            RDE: RD1_3657(pabB)
            MMR: Mmar10_0411
            HNE: HNE_2368(pabA) HNE_2369(pabB)
            ZMO: ZMO0113(pabB)
            GBE: GbCGDNIH1_0760
            BSU: BG10137(pabB)
            BHA: BH0090(pabB)
            BAN: BA0068(pabB)
            BAR: GBAA0068(pabB)
            BAA: BA_0658
            BAT: BAS0068
            BCE: BC0076
            BCA: BCE_0067(pabB)
            BCZ: BCZK0064(pabB)
            BTK: BT9727_0064(pabB)
            BTL: BALH_0067(pabB)
            BLI: BL00858(pabB)
            BLD: BLi00090(pabB)
            BCL: ABC0110(pabB)
            OIH: OB0701 OB0702
            GKA: GK0066
            SAU: SA0669
            SAV: SAV0714
            SAM: MW0676
            SAR: SAR0767
            SAS: SAS0679
            SAA: SAUSA300_0699
            SAO: SAOUHSC_00723
            SEP: SE0489
            SHA: SH2184
            SSP: SSP2006
            LMO: lmo2750
            LMF: LMOf2365_2737(pabB)
            LIN: lin2893
            LWE: lwe2698(pabB)
            LLA: L0178(pabA) L0179(pabB)
            LLC: LACR_C07
            LLM: llmg_1153(pabA) llmg_1154(pabB)
            SPM: spyM18_2056
            SPG: SpyM3_1712(pabP)
            SPS: SPs1712
            SPH: MGAS10270_Spy1765
            SPI: MGAS10750_Spy1789
            SPJ: MGAS2096_Spy1724
            SPK: MGAS9429_Spy1702
            SPA: M6_Spy1703
            SPB: M28_Spy1682
            SPN: SP_0665
            SPR: spr0582(pabB)
            SAG: SAG1528
            SAN: gbs1584
            SAK: SAK_1551(pabB)
            STC: str0771(pabB)
            STL: stu0771(pabB)
            CPE: CPE1017(pabB)
            CPF: CPF_1272(pabB)
            CPR: CPR_1094(pabB)
            CDF: CD1445(pabA) CD1446(pabB)
            CHY: CHY_1046(pabB)
            MSM: MSMEG_5446(pabB)
            SEN: SACE_0040(pabA) SACE_0793(pabB)
            RXY: Rxyl_0761
            LIL: LA0110
            LIC: LIC10098(pabB)
            LBJ: LBJ_0090
            LBL: LBL_0046
            SYF: Synpcc7942_1334
            SYG: sync_2865
            SYR: SynRCC307_2244(pabA) SynRCC307_2445
            SYX: SynWH7803_2329(pabA)
            PMB: A9601_19021
            PMC: P9515_18831
            PMF: P9303_29681
            PMG: P9301_18831
            PMH: P9215_02021
            PME: NATL1_21661
            FPS: FP1625(pabB)
            CTE: CT1712
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.1.85
            ExPASy - ENZYME nomenclature database: 2.6.1.85
            ExplorEnz - The Enzyme Database: 2.6.1.85
            ERGO genome analysis and discovery system: 2.6.1.85
            BRENDA, the Enzyme Database: 2.6.1.85
///
ENTRY       EC 2.6.1.-                  Enzyme
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transaminases
REACTION    (1) 3-Phosphonopyruvate + L-Glutamate <=>
            2-Amino-3-phosphonopropanoate + 2-Oxoglutarate [RN:R04051];
            (2) N6-Acetyl-LL-2,6-diaminoheptanedioate + 2-Oxoglutarate <=>
            N-Acetyl-L-2-amino-6-oxopimelate + L-Glutamate [RN:R04467];
            (3) D-erythro-1-(Imidazol-4-yl)glycerol 3-phosphate + L-Glutamate
            <=> 5'-Phospho-D-1-ribulosylformimine + L-Glutamine [RN:R04554];
            (4) 6-Aminohexanoate + 2-Oxoglutarate <=> Adipate semialdehyde +
            Glutamate [RN:R05507];
            (5) N2-Acetyl-L-aminoadipate semialdehyde + L-Glutamate <=>
            N2-Acetyl-L-lysine + 2-Oxoglutarate [RN:R06844];
            (6) UDP-L-Ara4O + L-Glutamate <=> UDP-L-Ara4N + 2-Oxoglutarate
            [RN:R07659]
SUBSTRATE   3-Phosphonopyruvate [CPD:C02798];
            L-Glutamate [CPD:C00025];
            N6-Acetyl-LL-2,6-diaminoheptanedioate [CPD:C04390];
            2-Oxoglutarate [CPD:C00026];
            D-erythro-1-(Imidazol-4-yl)glycerol 3-phosphate [CPD:C04666];
            6-Aminohexanoate [CPD:C02378];
            N2-Acetyl-L-aminoadipate semialdehyde [CPD:C12988]
PRODUCT     2-Amino-3-phosphonopropanoate [CPD:C05672];
            2-Oxoglutarate [CPD:C00026];
            N-Acetyl-L-2-amino-6-oxopimelate [CPD:C05539];
            L-Glutamate [CPD:C00025];
            5'-Phospho-D-1-ribulosylformimine [CPD:C05569];
            L-Glutamine [CPD:C00064];
            Adipate semialdehyde [CPD:C06102];
            Glutamate [CPD:C00302];
            N2-Acetyl-L-lysine [CPD:C12989]
///
ENTRY       EC 2.6.2.1        Obsolete  Enzyme
NAME        Transferred to 2.1.4.1
CLASS       Transferases;
            Transferring nitrogenous groups;
            Amidinotransferases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 2.1.4.1 glycine amidinotransferase (EC
            2.6.2.1 created 1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.2.1
            ExPASy - ENZYME nomenclature database: 2.6.2.1
            ExplorEnz - The Enzyme Database: 2.6.2.1
            ERGO genome analysis and discovery system: 2.6.2.1
            BRENDA, the Enzyme Database: 2.6.2.1
///
ENTRY       EC 2.6.3.1                  Enzyme
NAME        oximinotransferase;
            transoximinase;
            oximase;
            pyruvate-acetone oximinotransferase;
            transoximase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Oximinotransferases
SYSNAME     pyruvate-oxime:acetone oximinotransferase
REACTION    pyruvate oxime + acetone = pyruvate + acetone oxime [RN:R03796]
ALL_REAC    R03796
SUBSTRATE   pyruvate oxime [CPD:C02193];
            acetone [CPD:C00207]
PRODUCT     pyruvate [CPD:C00022];
            acetone oxime [CPD:C01995]
COMMENT     Acetaldehyde can act instead of acetone; D-glucose oxime can act
            instead of pyruvate oxime.
REFERENCE   1
  AUTHORS   Yamafuji, K. and Eto, M.
  TITLE     Chromatographic study of transoximase.
  JOURNAL   Enzymologia 16 (1954) 247-255.
  ORGANISM  Bombyx mori [GN:dbmo]
REFERENCE   2
  AUTHORS   Yamafuji, K., Omura, H. and Miura, K.
  TITLE     On the transoximase.
  JOURNAL   Enzymologia 16 (1953) 75-80.
  ORGANISM  Bombyx mori [GN:dbmo]
REFERENCE   3
  AUTHORS   Yamafuji, K., Shimamura, M. and Omura, H.
  TITLE     Measurement of transoximase action.
  JOURNAL   Enzymologia 17 (1956) 359-362.
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.3.1
            ExPASy - ENZYME nomenclature database: 2.6.3.1
            ExplorEnz - The Enzyme Database: 2.6.3.1
            ERGO genome analysis and discovery system: 2.6.3.1
            BRENDA, the Enzyme Database: 2.6.3.1
            CAS: 9030-49-3
///
ENTRY       EC 2.6.99.1                 Enzyme
NAME        dATP(dGTP)---DNA purinetransferase
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transferring other nitrogenous groups
SYSNAME     dATP(dGTP):depurinated-DNA purine transferase
REACTION    (1) dATP + depurinated DNA = deoxyribose triphosphate + DNA
            [RN:R03904 R07278];
            (2) dGTP + depurinated DNA = deoxyribose triphosphate + DNA
ALL_REAC    R03904 R07278
SUBSTRATE   dATP [CPD:C00131];
            depurinated DNA [CPD:C02270];
            dGTP [CPD:C00286]
PRODUCT     deoxyribose triphosphate [CPD:C12347];
            DNA [CPD:C00039]
COMMENT     The purine residue is transferred on to the apurinic site forming a
            normal glycosylic bond. dATP reacts at sites of the double-stranded
            depurinated DNA that lack adenine, and dGTP at sites that lack
            guanine.
REFERENCE   1  [PMID:218192]
  AUTHORS   Deutsch WA, Linn S.
  TITLE     DNA binding activity from cultured human fibrolasts that is specific
            for partially depurinated DNA and that inserts purines into apurinic
            sites.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 141-4.
REFERENCE   2  [PMID:375225]
  AUTHORS   Livneh Z, Elad D, Sperling J.
  TITLE     Enzymatic insertion of purine bases into depurinated DNA in vitro.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 1089-93.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.99.1
            ExPASy - ENZYME nomenclature database: 2.6.99.1
            ExplorEnz - The Enzyme Database: 2.6.99.1
            ERGO genome analysis and discovery system: 2.6.99.1
            BRENDA, the Enzyme Database: 2.6.99.1
///
ENTRY       EC 2.6.99.2                 Enzyme
NAME        pyridoxine 5'-phosphate synthase;
            pyridoxine 5-phosphate phospho lyase;
            PNP synthase;
            PdxJ
CLASS       Transferases;
            Transferring nitrogenous groups;
            Transferring other nitrogenous groups
SYSNAME     1-deoxy-D-xylulose-5-phosphate:3-amino-2-oxopropyl phosphate
            3-amino-2-oxopropyltransferase (phosphate-hydrolysing; cyclizing)
REACTION    1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate =
            pyridoxine 5'-phosphate + phosphate + 2 H2O [RN:R05838]
ALL_REAC    R05838
SUBSTRATE   1-deoxy-D-xylulose 5-phosphate [CPD:C11437];
            3-amino-2-oxopropyl phosphate [CPD:C11638]
PRODUCT     pyridoxine 5'-phosphate [CPD:C00627];
            phosphate [CPD:C00009];
            H2O [CPD:C00001]
COMMENT     In Escherichia coli, the coenzyme pyridoxal 5'-phosphate is
            synthesized de novo by a pathway that involves EC 1.2.1.72
            (erythrose-4-phosphate dehydrogenase), EC 1.1.1.290
            (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine
            transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate
            dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and
            EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate).
            1-Deoxy-D-xylulose cannot replace 1-deoxy-D-xylulose 5-phosphate as
            a substrate [3].
REFERENCE   1  [PMID:12686115]
  AUTHORS   Garrido-Franco M.
  TITLE     Pyridoxine 5'-phosphate synthase: de novo synthesis of vitamin B6
            and beyond.
  JOURNAL   Biochim. Biophys. Acta. 1647 (2003) 92-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:12206776]
  AUTHORS   Garrido-Franco M, Laber B, Huber R, Clausen T.
  TITLE     Enzyme-ligand complexes of pyridoxine 5'-phosphate synthase:
            implications for substrate binding and catalysis.
  JOURNAL   J. Mol. Biol. 321 (2002) 601-12.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:10225425]
  AUTHORS   Laber B, Maurer W, Scharf S, Stepusin K, Schmidt FS.
  TITLE     Vitamin B6 biosynthesis: formation of pyridoxine 5'-phosphate from
            4-(phosphohydroxy)-L-threonine and 1-deoxy-D-xylulose-5-phosphate by
            PdxA and PdxJ protein.
  JOURNAL   FEBS. Lett. 449 (1999) 45-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:11286891]
  AUTHORS   Franco MG, Laber B, Huber R, Clausen T.
  TITLE     Structural basis for the function of pyridoxine 5'-phosphate
            synthase.
  JOURNAL   Structure. 9 (2001) 245-53.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00750  Vitamin B6 metabolism
ORTHOLOGY   KO: K03474  pyridoxine 5-phosphate synthase
GENES       ECO: b2564(pdxJ)
            ECJ: JW2548(pdxJ)
            ECE: Z3845(pdxJ)
            ECS: ECs3430
            ECC: c3088(pdxJ)
            ECI: UTI89_C2885(pdxJ)
            ECP: ECP_2566
            ECV: APECO1_3967(pdxJ)
            ECW: EcE24377A_2850(pdxJ)
            ECX: EcHS_A2719
            STY: STY2824(pdxJ)
            STT: t0279(pdxJ)
            SPT: SPA0287(pdxJ)
            SEC: SC2573(pdxJ)
            STM: STM2578(pdxJ)
            YPE: YPO2930(pdxJ)
            YPK: y1300(pdxJ)
            YPM: YP_2525(pdxJ)
            YPA: YPA_2369
            YPN: YPN_1209
            YPS: YPTB2887(pdxJ)
            SFL: SF2626(pdxJ)
            SFX: S2799(pdxJ)
            SFV: SFV_2627(pdxJ)
            SSN: SSON_2688(pdxJ)
            SBO: SBO_2592(pdxJ)
            SDY: SDY_2805(pdxJ)
            ECA: ECA3275(pdxJ)
            PLU: plu3337(pdxJ)
            WBR: WGLp197(pdxJ)
            SGL: SG1784
            BFL: Bfl539(pdxJ)
            BPN: BPEN_559(pdxJ)
            XFA: XF0060
            XFT: PD0040(pdxJ)
            XCC: XCC0012(pdxJ)
            XCB: XC_0012
            XCV: XCV0013(pdxJ)
            XAC: XAC0012(pdxJ)
            XOO: XOO0012(pdxJ)
            XOM: XOO_0012(XOO0012)
            VCH: VC2458(pdxJ)
            VVU: VV1_1568
            VVY: VV2828
            VPA: VP2569(pdxJ)
            VFI: VF2084(pdxJ)
            PPR: PBPRA3086(pdxJ)
            PAE: PA0773(pdxJ)
            PAU: PA14_54290(pdxJ)
            PAP: PSPA7_4746(pdxJ)
            PPU: PP_1436(pdxJ)
            PST: PSPTO_4214(pdxJ)
            PSB: Psyr_3948(pdxJ)
            PSP: PSPPH_3945(pdxJ)
            PFL: PFL_1074(pdxJ)
            PFO: Pfl_0997(pdxJ)
            PEN: PSEEN4287(pdxJ)
            PAR: Psyc_0336(pdxJ)
            PCR: Pcryo_0370
            ACI: ACIAD2577(pdxJ)
            SON: SO_1351(pdxJ)
            SDN: Sden_2763
            SFR: Sfri_2926
            SHE: Shewmr4_2845
            SHM: Shewmr7_2927
            SHN: Shewana3_3023
            ILO: IL0807(pdxJ)
            CPS: CPS_4119(pdxJ)
            PHA: PSHAa0735(pdxJ)
            PAT: Patl_3709
            SDE: Sde_1713
            CBU: CBU_1494(pdxJ)
            CBD: COXBU7E912_0488(pdxJ)
            LPN: lpg0946(pdxJ)
            LPF: lpl0975(pdxJ)
            LPP: lpp1008(pdxJ)
            MCA: MCA1667(pdxJ)
            TCX: Tcr_0737
            NOC: Noc_0795(pdxJ)
            AEH: Mlg_1350
            HCH: HCH_00130(pdxJ)
            CSA: Csal_1634
            ABO: ABO_1628(pdxJ)
            AHA: AHA_0803(pdxJ)
            BCI: BCI_0279(pdxJ)
            NME: NMB0448(pdxJ)
            NMA: NMA2037(pdxJ)
            NGO: NGO1508(pdxJ)
            CVI: CV_2070(pdxJ)
            RSO: RSc1066(pdxJ)
            REU: Reut_A2249(pdxJ)
            RME: Rmet_2415
            BMA: BMA0546(pdxJ)
            BXE: Bxe_A1088
            BUR: Bcep18194_A4249(pdxJ)
            BCN: Bcen_0657
            BCH: Bcen2424_1137
            BAM: Bamb_1013
            BPS: BPSL2426(pdxJ)
            BPM: BURPS1710b_2892(pdxJ)
            BTE: BTH_I1733(pdxJ)
            BPE: BP2078(pdxJ)
            BPA: BPP1762(pdxJ)
            BBR: BB3346(pdxJ)
            RFR: Rfer_1752
            POL: Bpro_3632
            NEU: NE2322(pdxJ)
            NET: Neut_1776
            NMU: Nmul_A1759(pdxJ)
            EBA: ebA5544(pdxJ)
            DAR: Daro_2032(pdxJ)
            TBD: Tbd_2083(pdxJ)
            MFA: Mfla_0867 Mfla_1011
            HPY: HP1582(pdxJ)
            HPJ: jhp1489(pdxJ)
            HPA: HPAG1_1530
            HHE: HH0862(pdxJ)
            HAC: Hac_0031(pdxJ)
            WSU: WS0105(pdxJ)
            TDN: Tmden_0896
            CJE: Cj1238(pdxJ)
            CJR: CJE1373(pdxJ)
            CHA: CHAB381_1714(pdxJ)
            GSU: GSU1804(pdxJ)
            GME: Gmet_1885
            PCA: Pcar_1002
            DVU: DVU1908(pdxJ)
            DDE: Dde_2043(pdxJ)
            BBA: Bd1932(pdxJ)
            DPS: DP1605
            ADE: Adeh_1500
            MXA: MXAN_4351(pdxJ)
            SAT: SYN_01378
            SFU: Sfum_2166
            WOL: WD0064(pdxJ)
            AMA: AM434(pdxJ)
            APH: APH_0790(pdxJ)
            ERU: Erum2920(pdxJ)
            ERW: ERWE_CDS_02980(pdxJ)
            ERG: ERGA_CDS_02920(pdxJ)
            ECN: Ecaj_0273(pdxJ)
            ECH: ECH_0805(pdxJ)
            NSE: NSE_0320(pdxJ)
            PUB: SAR11_1056(pdxJ)
            MLO: mll1418
            MES: Meso_1493
            SME: SMc01407(pdxJ)
            ATU: Atu2024(pdxJ)
            ATC: AGR_C_3668(pdxJ)
            RET: RHE_CH02769(pdxJ)
            RLE: RL3222(pdxJ)
            BME: BMEI0621
            BMF: BAB1_1404
            BMS: BR1385
            BMB: BruAb1_1381
            BJA: bll5064(pdxJ)
            RPA: RPA2694(pdxJ)
            RPB: RPB_2609(pdxJ)
            RPC: RPC_2637
            RPD: RPD_2648
            RPE: RPE_3025
            NWI: Nwi_1921
            NHA: Nham_2254
            BHE: BH10900(pdxJ)
            BQU: BQ08550(pdxJ)
            CCR: CC_1557(pdxJ)
            SIL: SPO3201(pdxJ)
            SIT: TM1040_2563
            RSP: RSP_1672(pdxJ)
            JAN: Jann_0516
            RDE: RD1_1362(pdxJ)
            MMR: Mmar10_1573
            HNE: HNE_0875(pdxJ)
            ZMO: ZMO1708
            NAR: Saro_0911
            SAL: Sala_1407
            ELI: ELI_02715
            GOX: GOX2241(pdxJ)
            GBE: GbCGDNIH1_2064
            RRU: Rru_A1854
            MAG: amb2254
            MGM: Mmc1_1860
            RBA: RB536(pdxJ)
            LIL: LA1514(pdxJ)
            LIC: LIC12248(pdxJ)
            LBJ: LBJ_1705(pdxJ)
            LBL: LBL_1924(pdxJ)
            SYN: slr1779(pdxJ)
            SYW: SYNW0910(pdxJ)
            SYC: syc0356_c(pdxJ)
            SYF: Synpcc7942_1194
            SYD: Syncc9605_1657
            SYE: Syncc9902_1414
            SYG: sync_1151(pdxJ)
            CYA: CYA_2272(pdxJ)
            CYB: CYB_0455(pdxJ)
            TEL: tlr0838(pdxJ)
            GVI: gll0103(pdxJ)
            ANA: all0218(pdxJ)
            AVA: Ava_2709
            PMA: Pro1089(pdxJ)
            PMM: PMM1107(pdxJ)
            PMT: PMT1091(pdxJ)
            PMN: PMN2A_0642(pdxJ)
            PMI: PMT9312_1118
            TER: Tery_4177
            BTH: BT_3918(pdxJ)
            BFR: BF3967(pdxJ)
            BFS: BF3740
            PGI: PG0630(pdxJ)
            SRU: SRU_2080(pdxJ)
            CHU: CHU_3403(pdxJ)
            CTE: CT0331(pdxJ)
            CCH: Cag_0484
            PLT: Plut_0446
            AAE: aq_1423(pdxJ)
DBLINKS     IUBMB Enzyme Nomenclature: 2.6.99.2
            ExPASy - ENZYME nomenclature database: 2.6.99.2
            ExplorEnz - The Enzyme Database: 2.6.99.2
            ERGO genome analysis and discovery system: 2.6.99.2
            BRENDA, the Enzyme Database: 2.6.99.2
///
ENTRY       EC 2.6.-.-                  Enzyme
CLASS       Transferases;
            Transferring nitrogenous groups
REACTION    O-1-Alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine + Choline <=>
            Plasmenylcholine + Ethanolamine [RN:R07386]
SUBSTRATE   O-1-Alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine [CPD:C04756];
            Choline [CPD:C00114]
PRODUCT     Plasmenylcholine [CPD:C00958];
            Ethanolamine [CPD:C00189]
///
ENTRY       EC 2.7.1.1                  Enzyme
NAME        hexokinase;
            hexokinase type IV glucokinase;
            hexokinase D;
            hexokinase type IV;
            hexokinase (phosphorylating);
            ATP-dependent hexokinase;
            glucose ATP phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-hexose 6-phosphotransferase
REACTION    ATP + D-hexose = ADP + D-hexose 6-phosphate [RN:R02848]
ALL_REAC    R02848 > R00299 R00760 R00867 R01326 R01600 R01786 R01961 R02865
            R03920;
            (other) R00725 R00876 R01139 R01140 R01327 R01330 R01964 R01965
            R02849 R02850 R02867 R02868
SUBSTRATE   ATP [CPD:C00002];
            D-hexose [CPD:C00738]
PRODUCT     ADP [CPD:C00008];
            D-hexose 6-phosphate [CPD:C02965]
COMMENT     D-Glucose, D-mannose, D-fructose, sorbitol and D-glucosamine can act
            as acceptors; ITP and dATP can act as donors. The liver isoenzyme
            has sometimes been called glucokinase.
REFERENCE   1
  AUTHORS   Bailey, K. and Webb, E.C.
  TITLE     Purification of yeast hexokinase and its reaction with
            betabeta'-dichlorodiethyl sulphide.
  JOURNAL   Biochem. J. 42 (1948) 60-68.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2
  AUTHORS   Berger, L., Slein, M.W., Colowick, S.P. and Cori, C.F.
  TITLE     Isolation of hexokinase from baker's yeast.
  JOURNAL   J. Gen. Physiol. 29 (1946) 379-391.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Kunitz, M. and McDonald, M.R.
  TITLE     Crystalline hexokinase (heterophosphatase). Method of isolation and
            properties.
  JOURNAL   J. Gen. Physiol. 29 (1946) 393-412.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4  [PMID:7048063]
  AUTHORS   Pollard-Knight D, Cornish-Bowden A.
  TITLE     Mechanism of liver glucokinase.
  JOURNAL   Mol. Cell. Biochem. 44 (1982) 71-80.
  ORGANISM  rat [GN:rno], cow [GN:bta]
REFERENCE   5  [PMID:233226]
  AUTHORS   Ureta T, Radojkovic J, Lagos R, Guixe V, Nunez L.
  TITLE     Phylogenetic and ontogenetic studies of glucose phosphorylating
            isozymes of vertebrates.
  JOURNAL   Arch. Biol. Med. Exp. (Santiago). 12 (1979) 587-604.
REFERENCE   6  [PMID:6477520]
  AUTHORS   Cardenas ML, Rabajille E, Niemeyer H.
  TITLE     Fructose is a good substrate for rat liver 'glucokinase' (hexokinase
            D).
  JOURNAL   Biochem. J. 222 (1984) 363-70.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00051  Fructose and mannose metabolism
            PATH: map00052  Galactose metabolism
            PATH: map00500  Starch and sucrose metabolism
            PATH: map00521  Streptomycin biosynthesis
            PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K00844  hexokinase
GENES       HSA: 3098(HK1) 3099(HK2) 3101(HK3)
            PTR: 462298(HK3)
            MCC: 710479(LOC710479)
            MMU: 15277(Hk2) 212032(Hk3)
            RNO: 25058(Hk1) 25059(Hk2) 25060(Hk3)
            CFA: 475781(HK2) 479234(HK1) 489096(HK3)
            BTA: 280817(HK1) 281771(FRAP1)
            GGA: 373889(HK1) 374044(HK2)
            DRE: 406339(hk2)
            SPU: 594105(LOC594105)
            DME: Dmel_CG3001(Hex-A) Dmel_CG32849(Hex-t2) Dmel_CG33102(Hex-t1)
                 Dmel_CG8094(Hex-C)
            CEL: F14B4.2(hexokinase)
            ATH: AT1G47840 AT2G19860(ATHXK2) AT4G37840
            OSA: 4326547 4326776 4339361 4339420 4342654 4343113
            SCE: YFR053C(HXK1) YGL253W(HXK2)
            AGO: AGOS_AFR279C
            PIC: PICST_32526(NAG5) PICST_85453(HXK1)
            CAL: CaO19_542(CaO19.542)
            CGR: CAGL0A04829g CAGL0H07579g
            SPO: SPAC24H6.04 SPAC4F8.07c(hxk2)
            ANI: AN7459.2
            AFM: AFUA_2G00450 AFUA_2G05910 AFUA_6G03980 AFUA_7G04040
            AOR: AO090001000710
            ANG: An02g14380(hxk)
            CNE: CNH01400
            UMA: UM03093.1
            PFA: PFF1155w
            CPV: cgd6_3800
            CHO: Chro.60435
            TAN: TA19800 TA19810
            TPV: TP01_0043 TP01_0045
            TBR: Tb10.70.5800 Tb10.70.5820
            TCR: 508951.20 510121.20
            LMA: LmjF21.0240 LmjF21.0250
            EHI: 19.t00020 77.t00021
            DRM: Dred_1810
            TPA: TP0505
            TDE: TDE2469
STRUCTURES  PDB: 1BDG  1BG3  1CZA  1DGK  1HKB  1HKC  1HKG  1IG8  1QHA  1V4S  
                 1V4T  2E2N  2E2O  2E2P  2E2Q  2NZT  2YHX  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.1
            ExPASy - ENZYME nomenclature database: 2.7.1.1
            ExplorEnz - The Enzyme Database: 2.7.1.1
            ERGO genome analysis and discovery system: 2.7.1.1
            BRENDA, the Enzyme Database: 2.7.1.1
            CAS: 9001-51-8
///
ENTRY       EC 2.7.1.2                  Enzyme
NAME        glucokinase;
            glucokinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-glucose 6-phosphotransferase
REACTION    ATP + D-glucose = ADP + D-glucose 6-phosphate [RN:R00299]
ALL_REAC    R00299 > R01600 R01786
SUBSTRATE   ATP [CPD:C00002];
            D-glucose [CPD:C00031]
PRODUCT     ADP [CPD:C00008];
            D-glucose 6-phosphate [CPD:C00092]
COMMENT     A group of enzymes found in invertebrates and microorganisms that
            are highly specific for glucose.
REFERENCE   1  [PMID:4312464]
  AUTHORS   Baumann P.
  TITLE     Glucokinase of Dictyostelium discoideum.
  JOURNAL   Biochemistry. 8 (1969) 5011-5.
  ORGANISM  Dictyostelium discoideum [GN:ddi]
REFERENCE   2  [PMID:13242546]
  AUTHORS   BUEDING E, MACKINNON JA.
  TITLE     Hexokinases of Schistosoma mansoni.
  JOURNAL   J. Biol. Chem. 215 (1955) 495-506.
  ORGANISM  Schistosoma mansoni
REFERENCE   3  [PMID:7150605]
  AUTHORS   Porter EV, Chassy BM, Holmlund CE.
  TITLE     Purification and kinetic characterization of a specific glucokinase
            from Streptococcus mutans OMZ70 cells.
  JOURNAL   Biochim. Biophys. Acta. 709 (1982) 178-86.
  ORGANISM  Streptococcus mutans [GN:smu]
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00052  Galactose metabolism
            PATH: map00500  Starch and sucrose metabolism
            PATH: map00521  Streptomycin biosynthesis
            PATH: map04910  Insulin signaling pathway
            PATH: map04930  Type II diabetes mellitus
            PATH: map04950  Maturity onset diabetes of the young
ORTHOLOGY   KO: K00845  glucokinase
GENES       HSA: 2645(GCK)
            MMU: 103988(Gck)
            RNO: 24385(Gck)
            CME: CMO276C
            SCE: YCL040W(GLK1)
            AGO: AGOS_AFR716C
            PIC: PICST_73701(GLK1)
            CGR: CAGL0F00605g
            ANI: AN8689.2
            AFM: AFUA_2G16330 AFUA_6G02230
            AOR: AO090120000109
            ANG: An12g08610(GlkA)
            CNE: CNB02660
            UMA: UM02173.1
            TET: TTHERM_00388400 TTHERM_00574250 TTHERM_00592990
                 TTHERM_00593010 TTHERM_00593020
            TCR: 510187.100
            LMA: LmjF36.2320
            ECO: b2388(glk)
            ECJ: JW2385(glk)
            ECE: Z3654(glk)
            ECS: ECs3268
            ECC: c2927(glk)
            ECI: UTI89_C0670(nagC) UTI89_C1781(mlc) UTI89_C2720(glk)
            ECP: ECP_2414
            ECV: APECO1_4149(glk)
            ECW: EcE24377A_2678(glk)
            ECX: EcHS_A2525(glk)
            STY: STY2644(glk)
            STT: t0454(glk)
            SPT: SPA0457(glk)
            SEC: SC2406(glk)
            STM: STM2403(glk)
            YPE: YPO2977(glk)
            YPK: y1505(glk)
            YPM: YP_2602(glk)
            YPA: YPA_2166
            YPN: YPN_1405
            YPP: YPDSF_2084
            YPS: YPTB2700(glk)
            YPI: YpsIP31758_1332(glk)
            SFL: SF2454(glk)
            SFX: S2593(glk)
            SFV: SFV_2446(glk)
            SSN: SSON_2480(glk)
            SBO: SBO_2414(glk)
            SDY: SDY_2587(glk)
            ECA: ECA1401(glk)
            PLU: plu1405(glk)
            ENT: Ent638_2921
            SPE: Spro_3407
            XFA: XF1064 XF1460
            XFT: PD0345(glk) PD0680(glk)
            XCC: XCC2137(glk) XCC2886(glk) XCC2943(glk)
            XCB: XC_1166 XC_1223 XC_1976
            XCV: XCV2236(glk) XCV3204(glk2) XCV3251(glk3)
            XAC: XAC2070(glk) XAC3070(glk) XAC3120(glk)
            XOO: XOO1785(glk) XOO2315(glk)
            XOM: XOO_1626(XOO1626) XOO_1627(XOO1627) XOO_1628(XOO1628)
                 XOO_1688(XOO1688) XOO_2192(XOO2192)
            VFI: VF0606
            PAE: PA3193(glk)
            PAU: PA14_22930(glk)
            PAP: PSPA7_1935(glk)
            PPU: PP_1011(glk)
            PPF: Pput_1049
            PST: PSPTO_1289(glk)
            PSB: Psyr_1110(glk)
            PSP: PSPPH_1178(glk)
            PFL: PFL_4621(glk)
            PFO: Pfl_4374
            PEN: PSEEN4416(glk)
            PMY: Pmen_1147
            CPS: CPS_0247(glk1) CPS_0976(glk2) CPS_0982(glk3) CPS_2390(glk4)
                 CPS_3710(glk5)
            PHA: PSHAa1364
            PAT: Patl_0973
            SDE: Sde_1018
            PIN: Ping_2359 Ping_2382
            MAQ: Maqu_1829
            LPN: lpg0419(glk)
            LPF: lpl0462(glk)
            LPP: lpp0486(glk)
            MCA: MCA0561(glk)
            FTU: FTT1295c(glk)
            FTF: FTF1295c(glk1)
            FTW: FTW_0752(glk)
            FTL: FTL_0404
            FTH: FTH_0396(glk)
            FTA: FTA_0426(glk)
            FTN: FTN_0462(glk)
            TCX: Tcr_0507
            NOC: Noc_1347
            AEH: Mlg_0008
            HHA: Hhal_1119
            HCH: HCH_00434(glk)
            CSA: Csal_0935
            MMW: Mmwyl1_1037
            AHA: AHA_1351(glk)
            NME: NMB1390
            NMA: NMA1607(glk)
            NMC: NMC1329(glk)
            NGO: NGO0717
            CVI: CV_0147(glk)
            RSO: RSp1557(glk)
            REU: Reut_B5327
            REH: H16_B2564(glk)
            RME: Rmet_5799
            BMA: BMA2132
            BXE: Bxe_A3454
            BVI: Bcep1808_0881
            BUR: Bcep18194_A4068
            BCN: Bcen_0486
            BCH: Bcen2424_0965
            BAM: Bamb_0825
            BPS: BPSL2614(glk)
            BPM: BURPS1710b_3090(glk)
            BPL: BURPS1106A_3055(glk)
            BPD: BURPS668_3001(glk)
            BTE: BTH_I1550
            PNA: Pnap_3695
            VEI: Veis_1783
            NEU: NE1694
            NET: Neut_0427
            NMU: Nmul_A1872
            EBA: ebA584(glk)
            AZO: azo1800(glk1) azo2313(glk2)
            DAR: Daro_0592
            TBD: Tbd_2062
            MFA: Mfla_1371
            HPY: HP1103(glk)
            HPJ: jhp1029(glk)
            HPA: HPAG1_1041
            HAC: Hac_0439(glk)
            CJD: JJD26997_1268(glk)
            GSU: GSU1702
            GME: Gmet_1639
            PCA: Pcar_1507
            DVU: DVU1035
            DVL: Dvul_1958
            DDE: Dde_1461
            LIP: LI1076(glk)
            BBA: Bd1223(glk)
            DPS: DP1060
            ADE: Adeh_0161
            MXA: MXAN_1039(glkA) MXAN_6497(glcK)
            SAT: SYN_02951
            SFU: Sfum_1913 Sfum_1953
            MLO: mlr3412 mlr4640(glk) mlr7234
            MES: Meso_3594
            PLA: Plav_0309
            SME: SMc02835(glk)
            SMD: Smed_3369
            ATU: Atu0184(glk)
            ATC: AGR_C_310
            RET: RHE_CH00172(glk)
            RLE: RL0182(glk) pRL120034
            BME: BMEII0251
            BMF: BAB2_1010(glk)
            BMS: BRA1049(glk)
            BMB: BruAb2_0989(glk)
            BOV: BOV_A0987(glk)
            OAN: Oant_1332
            BJA: blr4550 blr4658(glk)
            BRA: BRADO1576(glk)
            BBT: BBta_6478(glk)
            RPC: RPC_4623
            RPE: RPE_4618
            NWI: Nwi_1025
            NHA: Nham_4371
            XAU: Xaut_2047 Xaut_4319
            CCR: CC_2054 CC_3167
            SIL: SPO0864
            SIT: TM1040_0363
            RSP: RSP_2875(glk)
            RSH: Rsph17029_1521
            RSQ: Rsph17025_1145
            JAN: Jann_1943
            RDE: RD1_3776(glk)
            PDE: Pden_2680
            MMR: Mmar10_2672
            HNE: HNE_1741(glk)
            ZMO: ZMO0369(glk)
            NAR: Saro_1896
            SAL: Sala_1110
            SWI: Swit_1625
            ELI: ELI_00535
            GOX: GOX1182 GOX2419
            GBE: GbCGDNIH1_0980
            RRU: Rru_A2486
            MAG: amb2112
            ABA: Acid345_0003
            BSU: BG11685(glcK)
            BHA: BH0797 BH1425(glk)
            BAN: BA4487(glcK)
            BAR: GBAA4487(glcK)
            BAA: BA_4934
            BAT: BAS4165
            BCE: BC0441 BC4260
            BCA: BCE_1908 BCE_4343(glcK)
            BCZ: BCZK1643(glcK) BCZK4014(glcK)
            BTK: BT9727_4004(glcK)
            BTL: BALH_0398 BALH_3025 BALH_3857(glcK)
            BLD: BLi02660(glcK)
            BCL: ABC1731(glcK)
            BAY: RBAM_023170(glcK)
            BPU: BPUM_2215(glcK)
            OIH: OB1919
            GKA: GK2442(glcK)
            SAU: SA1377(glcK)
            SAV: SAV1547(glcK)
            SAM: MW1499(glcK)
            SAR: SAR1624(glkA)
            SAS: SAS1485
            SAC: SACOL1604(glk)
            SAB: SAB1419c(glkA)
            SAA: SAUSA300_1507(glk)
            SAO: SAOUHSC_01646
            SEP: SE1233
            SER: SERP1112(glk)
            SHA: SH1369(glcK)
            SSP: SSP1209
            LMO: lmo1339
            LMF: LMOf2365_1356(glcK)
            LIN: lin1376
            LWE: lwe1354(glcK)
            LLA: L84096(glk)
            LLC: LACR_2309
            LLM: llmg_2299(glk)
            SPY: SPy_1529(glcK)
            SPZ: M5005_Spy_1257(glcK) M5005_Spy_1311
            SPM: spyM18_1546
            SPG: SpyM3_1180(glcK)
            SPS: SPs0682
            SPH: MGAS10270_Spy1273(glcK) MGAS10270_Spy1427
            SPI: MGAS10750_Spy1365(glcK) MGAS10750_Spy1420
            SPJ: MGAS2096_Spy1277(glcK) MGAS2096_Spy1331
            SPK: MGAS9429_Spy1252(glcK) MGAS9429_Spy1305
            SPF: SpyM50595(glkA)
            SPA: M6_Spy1278 M6_Spy1329
            SPB: M28_Spy1196(glcK) M28_Spy1352
            SPN: SP_0668
            SPR: spr0584(glcK)
            SPD: SPD_0580(gki)
            SAG: SAG0471(glk)
            SAN: gbs0518
            SAK: SAK_0573
            SMU: SMU.542(glk)
            STC: str0728(glcK)
            STL: stu0728(glcK)
            SSA: SSA_1090(glcK)
            SGO: SGO_1144(glcK)
            LPL: lp_1573(glk)
            LJO: LJ0195
            LAC: LBA0886
            LSA: LSA0123 LSA1329(glk)
            LSL: LSL_0552 LSL_1937(nagC)
            LDB: Ldb0119(glcK)
            LBU: LBUL_0099
            LBR: LVIS_0996
            LCA: LSEI_1659
            LGA: LGAS_0197
            EFA: EF2788(glcK)
            STH: STH602
            CAC: CAC2613(glcK)
            CPE: CPE0081(glcK)
            CPF: CPF_0076
            CPR: CPR_0098
            CTC: CTC00230
            CNO: NT01CX_2039
            CDF: CD2459(glcK)
            CBO: CBO1602(glcK)
            CHY: CHY_0270(glcK)
            DSY: DSY2007
            CSC: Csac_0778
            TTE: TTE0090(nagC) TTE1961(nagC4) TTE2418(nagC5)
            MTA: Moth_0832
            MPU: MYPU_2280(glcK)
            MMY: MSC_0863(glk) MSC_0875(glk)
            MMO: MMOB2030(glcK)
            MHY: mhp515(glcK)
            MHJ: MHJ_0515(glcK)
            MHP: MHP7448_0517(glcK)
            MFL: Mfl497
            MTU: Rv0650
            MTC: MT0679
            MBO: Mb0669
            MPA: MAP4123
            MSM: MSMEG_1363
            MMC: Mmcs_0965
            MKM: Mkms_0983
            MJL: Mjls_0993
            CGL: NCgl2105(cgl2185) NCgl2558(cgl2647)
            CGB: cg2399(glk)
            CEF: CE2078(glk)
            CDI: DIP1619(glk)
            CJK: jk0728(glk)
            NFA: nfa17130 nfa51900
            RHA: RHA1_ro01116 RHA1_ro01359 RHA1_ro04278 RHA1_ro05185
            SCO: SCO1077(SCG22.23c) SCO2126(glk) SCO6260(SCAH10.25)
            SMA: SAV1476 SAV1980 SAV6074(glkA1)
            TWH: TWT213(glkA)
            TWS: TW558(glk)
            LXX: Lxx15430(glkA)
            CMI: CMM_1876(glkA) CMM_2137
            ART: Arth_1710
            AAU: AAur_1467(glk) AAur_1688(glk)
            PAC: PPA0722
            NCA: Noca_3109
            TFU: Tfu_0273 Tfu_1033
            FRA: Francci3_3092 Francci3_3653
            FAL: FRAAL0917 FRAAL5091
            ACE: Acel_0979
            SEN: SACE_1700(glk) SACE_2869(rifN) SACE_7183(nagC4)
            STP: Strop_3274
            BLO: BL1691(glkA)
            FNU: FN1164
            RBA: RB1321 RB1629(glcK) RB3555(glcK)
            PCU: pc0935(glk)
            LIL: LA1437
            LIC: LIC12312(glcK)
            LBJ: LBJ_2173
            LBL: LBL_2167
            SYN: sll0593(glk) slr0329(xylR)
            SYW: SYNW1480 SYNW1487
            SYC: syc1291_c(glk) syc1981_c(xylR)
            SYF: Synpcc7942_0221 Synpcc7942_2111
            SYD: Syncc9605_1025 Syncc9605_1032
            SYE: Syncc9902_0926 Syncc9902_0933
            SYG: sync_1868(glk) sync_1879
            SYR: SynRCC307_0944(glk)
            SYX: SynWH7803_0774(glk)
            CYA: CYA_2134(glk)
            CYB: CYB_0974(glk)
            TEL: tll1495 tlr2355
            GVI: gll1169 gll3630
            ANA: all5002 alr1982 alr2973
            AVA: Ava_0933(glk) Ava_2265 Ava_4339
            PMA: Pro1065(glk)
            PMM: PMM0596
            PMT: PMT0425 PMT0437
            PMN: PMN2A_0032
            PMI: PMT9312_0596
            PMB: A9601_06521(glk)
            PMC: P9515_06611(glk)
            PMF: P9303_18441 P9303_18591(glk)
            PMG: P9301_06221(glk)
            PMH: P9215_06781(glk)
            PME: NATL1_06521(glk)
            TER: Tery_0774
            BTH: BT_2493 BT_3600 BT_4654
            BFR: BF0562
            BFS: BF0512
            SRU: SRU_0785
            CHU: CHU_1875(glk)
            CTE: CT2007
            CCH: Cag_0199
            PLT: Plut_0225
            DEH: cbdb_A63
            DRA: DR_2296
            DGE: Dgeo_0242
            TTH: TTC1688
            TTJ: TTHA0299
            TMA: TM1469
            MHU: Mhun_2804
            HAL: VNG2629G(glcK)
            HMA: rrnAC0547(glcK)
            HWA: HQ3108A(glcK)
            TAC: Ta0825
            TVO: TVN0728
            PTO: PTO1216
            APE: APE_2091.1
            PAI: PAE3437
STRUCTURES  PDB: 1L2L  1Q18  1SZ2  1UA4  2IU4  2IU6  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.2
            ExPASy - ENZYME nomenclature database: 2.7.1.2
            ExplorEnz - The Enzyme Database: 2.7.1.2
            ERGO genome analysis and discovery system: 2.7.1.2
            BRENDA, the Enzyme Database: 2.7.1.2
            CAS: 9001-36-9
///
ENTRY       EC 2.7.1.3                  Enzyme
NAME        ketohexokinase;
            ketohexokinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-fructose 1-phosphotransferase
REACTION    ATP + D-fructose = ADP + D-fructose 1-phosphate [RN:R00866]
ALL_REAC    R00866
SUBSTRATE   ATP [CPD:C00002];
            D-fructose [CPD:C00095]
PRODUCT     ADP [CPD:C00008];
            D-fructose 1-phosphate [CPD:C01094]
COMMENT     D-Sorbose, D-tagatose and 5-dehydro-D-fructose and a number of other
            ketoses and their analogues can also act as substrates [4].
REFERENCE   1  [PMID:14858418]
  AUTHORS   CORI GT, OCHOA S, SLEIN MW, CORI CF.
  TITLE     The metabolism of fructose in liver; isolation of
            fructose-I-phosphate and inorganic pyrophosphate.
  JOURNAL   Biochim. Biophys. Acta. 7 (1951) 304-17.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:13208667]
  AUTHORS   HERS HG.
  TITLE     [Liver fructokinase.]
  JOURNAL   Biochim. Biophys. Acta. 8 (1952) 416-23.
  ORGANISM  cow [GN:bta]
REFERENCE   3
  AUTHORS   Parks, R.E., Ben-Gershom, E. and Lardy, H.A.
  TITLE     Liver fructokinase.
  JOURNAL   J. Biol. Chem. 227 (1957) 231-242.
  ORGANISM  cow [GN:bta], rat [GN:rno]
REFERENCE   4  [PMID:193556]
  AUTHORS   Raushel FM, Cleland WW.
  TITLE     Bovine liver fructokinase: purification and kinetic properties.
  JOURNAL   Biochemistry. 16 (1977) 2169-75.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K00846  ketohexokinase
GENES       HSA: 3795(KHK)
            MMU: 16548(Khk)
            RNO: 25659(Khk)
            XLA: 447317(MGC81863)
            SPU: 588197(LOC588197)
            DME: Dmel_CG7328
            ECI: UTI89_C4462(yihV)
            NOC: Noc_2848
            HHA: Hhal_0921
            NPH: NP3184A(suk)
STRUCTURES  PDB: 2HLZ  2HQQ  2HW1  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.3
            ExPASy - ENZYME nomenclature database: 2.7.1.3
            ExplorEnz - The Enzyme Database: 2.7.1.3
            ERGO genome analysis and discovery system: 2.7.1.3
            BRENDA, the Enzyme Database: 2.7.1.3
            CAS: 9030-50-6
///
ENTRY       EC 2.7.1.4                  Enzyme
NAME        fructokinase;
            fructokinase (phosphorylating);
            D-fructokinase;
            D-fructose(D-mannose)kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-fructose 6-phosphotransferase
REACTION    ATP + D-fructose = ADP + D-fructose 6-phosphate [RN:R00760]
ALL_REAC    R00760 > R00867 R03920
SUBSTRATE   ATP [CPD:C00002];
            D-fructose [CPD:C00095]
PRODUCT     ADP [CPD:C00008];
            D-fructose 6-phosphate [CPD:C00085]
REFERENCE   1  [PMID:13242546]
  AUTHORS   BUEDING E, MACKINNON JA.
  TITLE     Hexokinases of Schistosoma mansoni.
  JOURNAL   J. Biol. Chem. 215 (1955) 495-506.
  ORGANISM  Schistosoma mansoni
REFERENCE   2
  AUTHORS   Medina, A. and Sols, A.
  TITLE     A specific fructokinase in peas.
  JOURNAL   Biochim. Biophys. Acta 19 (1956) 378-379.
  ORGANISM  Pisum sativum
PATHWAY     PATH: map00051  Fructose and mannose metabolism
            PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K00847  fructokinase
GENES       ATH: AT1G06030 AT1G66430 AT2G31390 AT3G59480 AT4G10260 AT5G51830
            OSA: 4324962 4340579 4344497
            CME: CMG166C
            DDI: DDBDRAFT_0204621
            TET: TTHERM_00052020
            EHI: 133.t00007
            TVA: TVAG_099490
            ECE: Z3624
            ECS: ECs3242
            ECP: ECP_2387 ECP_2750
            ECV: APECO1_31822 APECO1_3188
            ECW: EcE24377A_2647(cscK)
            STY: STY3804
            STT: t3552
            SPT: SPA3909
            SEC: SC3957(scrK)
            STM: STM4066
            YEN: YE0554(scrK)
            SFV: SFV_2420
            ECA: ECA0364(scrK)
            PMU: PM1849
            MSU: MS1233(rbsK)
            APL: APL_2034(scrK)
            XFA: XF1610
            XFT: PD1163
            XCC: XCC1509(scrK)
            XCB: XC_2727
            XCV: XCV1600
            XAC: XAC1557(scrK)
            XOO: XOO2071(scrK)
            XOM: XOO_1952(XOO1952)
            VCH: VCA0656
            VCO: VC0395_0600(cscK)
            PAE: PA2344(mtlZ)
            PAU: PA14_34340(mtlZ)
            PST: PSPTO_2701
            PSB: Psyr_2434(pfkB)
            PSP: PSPPH_2592(mtlZ)
            PFL: PFL_3076(mtlZ)
            PFO: Pfl_2634(pfkB)
            PEN: PSEEN1987(mtlZ)
            SFR: Sfri_3987
            SHE: Shewmr4_0067
            SHM: Shewmr7_0065
            SHN: Shewana3_0069
            CPS: CPS_2648
            PAT: Patl_4122
            FTU: FTT1331(cscK)
            FTF: FTF1331(cscK)
            FTW: FTW_1497
            FTL: FTL_1492
            FTH: FTH_1446
            FTA: FTA_1577
            FTN: FTN_0646(cscK)
            TCX: Tcr_1796
            NOC: Noc_3070
            HCH: HCH_06077
            CSA: Csal_0931
            ABO: ABO_0350(pfkB)
            AHA: AHA_2980
            CVI: CV_1424(pfkB)
            RSO: RS05325(RSp1280) RSc2146(cscK)
            REU: Reut_A1648
            REH: H16_B1503(frcK)
            BMA: BMA0331 BMA3386
            BXE: Bxe_A4286
            BUR: Bcep18194_A4680 Bcep18194_A5081 Bcep18194_A5928
                 Bcep18194_A6323
            BCN: Bcen_1060
            BCH: Bcen2424_1540 Bcen2424_2597 Bcen2424_2974
            BAM: Bamb_1422
            BPS: BPSL0320 BPSL0827(scrK)
            BPM: BURPS1710b_0526(cscK) BURPS1710b_1032(scrK)
            BTE: BTH_I0298 BTH_I0693
            RFR: Rfer_1904
            POL: Bpro_3202
            NEU: NE1212
            NMU: Nmul_A2268(pfkB)
            MFA: Mfla_2609
            DDE: Dde_2522
            ADE: Adeh_1304
            MXA: MXAN_3087(cscK)
            PUB: SAR11_0364(frk)
            MLO: mll7216 mll7580
            MES: Meso_0836
            SME: SMc02164(frk)
            ATU: Atu0401(scrK)
            ATC: AGR_C_706
            RET: RHE_CH00135 RHE_CH00475(frk)
            RLE: RL0143 RL0502(frk) RL0642 pRL80080
            BME: BMEI1779 BMEI1833
            BMF: BAB1_0112(cscK)
            BMS: BR0115(cscK)
            BMB: BruAb1_0112(cscK)
            BOV: BOV_0112(cscK)
            BJA: blr3227
            BRA: BRADO6614
            BBT: BBta_0921
            CCR: CC_1134
            SIL: SPOA0276(cscK)
            SIT: TM1040_3042
            RSP: RSP_2257
            RSH: Rsph17029_0931
            JAN: Jann_2674
            RDE: RD1_2877(frk)
            PDE: Pden_2946
            ZMO: ZMO1719(frk)
            NAR: Saro_1885
            ELI: ELI_04230
            GOX: GOX0612
            GBE: GbCGDNIH1_0400
            BSU: BG12195(ydhR) BG12796(ydjE)
            BHA: BH1857
            BAN: BA0752(scrK)
            BAR: GBAA0752(scrK)
            BAA: BA_1336(pfkB)
            BAT: BAS0716
            BCE: BC0773
            BTK: BT9727_0666(scrK)
            BLI: BL00700
            BLD: BLi03529(ydhR)
            BCL: ABC3225
            BPU: BPUM_0215(ydhR)
            OIH: OB2757
            GKA: GK3204
            GTN: GTNG_3123
            SAU: SA1845
            SAV: SAV2040
            SAM: MW1964
            SAR: SAR2127
            SAS: SAS1945
            SAC: SACOL2028
            SAB: SAB1924c
            SAA: SAUSA300_1993
            SAO: SAOUHSC_02267
            SEP: SE1639
            SER: SERP1494
            SHA: SH0992
            SSP: SSP0838
            LMO: lmo0813
            LMF: LMOf2365_0829(scrK)
            LIN: lin0809
            LWE: lwe0808(scrK)
            LLA: L117718(scrK)
            LLC: LACR_1584
            LLM: llmg_1006(scrK)
            SPY: SPy_1811(scrK)
            SPZ: M5005_Spy_1539(scrK)
            SPM: spyM18_1877
            SPG: SpyM3_1567(scrK)
            SPS: SPs0300
            SPH: MGAS10270_Spy1606(scrK)
            SPI: MGAS10750_Spy1598(scrK)
            SPJ: MGAS2096_Spy1564(scrK)
            SPK: MGAS9429_Spy1543(scrK)
            SPF: SpyM50310(scrK)
            SPA: M6_Spy1529
            SPB: M28_Spy1526(scrK)
            SPN: SP_1721
            SPR: spr1565(scrK)
            SPD: SPD_1531(scrK)
            SAG: SAG1689(scrK)
            SAN: gbs1733
            SAK: SAK_1701(scrK)
            SMU: SMU.1840(scrK)
            STC: str1733(scrK)
            STL: stu1733(scrK)
            STE: STER_1709
            SSA: SSA_0457(scrK)
            SSU: SSU05_1816
            SSV: SSU98_1820
            SGO: SGO_1755(scrK)
            LPL: lp_0184(sacK1) lp_3637(sacK2)
            LJO: LJ0013
            LAC: LBA0016
            LSA: LSA1790(scrK)
            LSL: LSL_1461
            LBR: LVIS_2163
            LGA: LGAS_0014
            PPE: PEPE_0516
            EFA: EF1179(cscK)
            OOE: OEOE_1708
            LME: LEUM_0290
            CAC: CAC0424 CAC1523
            CPE: CPE1531
            CPF: CPF_0734(scrK) CPF_1782
            CPR: CPR_0909 CPR_1510
            MFL: Mfl514
            MPA: MAP0876c
            MSM: MSMEG_5577
            RHA: RHA1_ro02811
            SCO: SCO1957(SCC54.17)
            SMA: SAV5705(scrK1) SAV6287(scrK2)
            LXX: Lxx01600(scrK)
            AAU: AAur_0061 AAur_0414 AAur_0694 AAur_1960 AAur_pTC20246
            TFU: Tfu_0928
            ACE: Acel_2120
            SEN: SACE_0647(cscK) SACE_5189(iolC)
            BLO: BL1339
            BAD: BAD_1096
            RBA: RB5198(scrK)
            SYN: slr1448(cscK)
            SYW: SYNW0117
            SYC: syc1388_c(cscK)
            SYF: Synpcc7942_0116
            SYD: Syncc9605_0100
            SYE: Syncc9902_0144
            SYG: sync_0103 sync_2024
            SYR: SynRCC307_0104(cscK)
            SYX: SynWH7803_0165(cscK)
            CYA: CYA_0402
            CYB: CYB_2162
            TEL: tll1428
            GVI: gll0502
            ANA: alr0517
            AVA: Ava_2919
            PMA: Pro1788(rbsK)
            PMM: PMM1627
            PMT: PMT0136
            PMN: PMN2A_1204
            PMI: PMT9312_1720
            PMB: A9601_18371
            PMC: P9515_18161
            PMF: P9303_01731
            PMG: P9301_18191
            PME: NATL1_20791
            TER: Tery_2734
            BTH: BT_1757 BT_3305
            BFR: BF0171 BF3340
            BFS: BF0136(frk) BF3175
            DRA: DR_0728
            DGE: Dgeo_1421
            TTH: TTC0630
            TTJ: TTHA0992
            TMA: TM0296
            MAC: MA1840
            MBA: Mbar_A2838
            MMA: MM_3131
            NPH: NP3184A(suk)
            PHO: PH1459
            PAB: PAB0482(scrK)
            PFU: PF1458 PF1738
            SSO: SSO3195
            STO: ST2478
            SAI: Saci_0226(kdgK)
STRUCTURES  PDB: 1TYY  1TZ3  1TZ6  1XC3  2V78  2VAR  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.4
            ExPASy - ENZYME nomenclature database: 2.7.1.4
            ExplorEnz - The Enzyme Database: 2.7.1.4
            ERGO genome analysis and discovery system: 2.7.1.4
            BRENDA, the Enzyme Database: 2.7.1.4
            CAS: 9030-51-7
///
ENTRY       EC 2.7.1.5                  Enzyme
NAME        rhamnulokinase;
            RhuK;
            rhamnulokinase (phosphorylating);
            L-rhamnulokinase;
            L-rhamnulose kinase;
            rhamnulose kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:L-rhamnulose 1-phosphotransferase
REACTION    ATP + L-rhamnulose = ADP + L-rhamnulose 1-phosphate [RN:R03014]
ALL_REAC    R03014;
            (other) R01902
SUBSTRATE   ATP [CPD:C00002];
            L-rhamnulose [CPD:C00861]
PRODUCT     ADP [CPD:C00008];
            L-rhamnulose 1-phosphate [CPD:C01131]
REFERENCE   1
  AUTHORS   Wilson, D.M. and Ajl, S.
  TITLE     Metabolism of L-rhamnose by Escherichia coli. II. The
            phosphorylation of L-rhamnulose.
  JOURNAL   J. Bacteriol. 73 (1957) 415-420.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K00848  rhamnulokinase
GENES       ECO: b3904(rhaB)
            ECJ: JW3875(rhaB)
            ECE: Z5448(rhaB)
            ECS: ECs4831
            ECC: c4853(rhaB)
            ECI: UTI89_C4487(rhaB)
            ECP: ECP_4114
            ECV: APECO1_2564(rhaB)
            ECW: EcE24377A_4435(rhaB)
            ECX: EcHS_A4133(rhaB)
            STY: STY3826(rhaB)
            STT: t3572(rhaB)
            SPT: SPA3890(rhaB)
            SEC: SC3937(rhaB)
            STM: STM4047(rhaB)
            YPE: YPO0330(rhaB)
            YPK: y0587(rhaB)
            YPM: YP_0485(rhaB)
            YPA: YPA_3952
            YPN: YPN_3340
            YPS: YPTB0385(rhaB)
            YPI: YpsIP31758_3755(rhaB)
            SFL: SF3981(rhaB)
            SFX: S3767(rhaB)
            SFV: SFV_3591(rhaB)
            SSN: SSON_4074(rhaB)
            SBO: SBO_3922(rhaB)
            SDY: SDY_3842(rhaB)
            ECA: ECA0440(rhaB)
            MSU: MS2329(xylB)
            BSU: BG12385(yulC)
            BHA: BH1551
            BLI: BL00812(yulC)
            BLD: BLi03558(yulC)
            BCL: ABC0374
            OIH: OB0495
            LMO: lmo2849
            LMF: LMOf2365_2839(rhaB)
            LIN: lin2981
            LPL: lp_3595(rhaB)
            LSL: LSL_1752(rhaB)
            EFA: EF0433
            MSM: MSMEG_0591(rhaB)
            NFA: nfa32950
            RHA: RHA1_ro04093
            SCO: SCO0814(SCF43A.04)
            SMA: SAV7413(rhaB)
            AAU: AAur_3717(rhaB)
            SEN: SACE_4103(rhaB)
            RBA: RB5406
            BTH: BT_3763
            BFR: BF0256
            BFS: BF0214(fucK)
            DGE: Dgeo_2453
            TMA: TM1073
            HMA: pNG7029(rhaB)
STRUCTURES  PDB: 2CGJ  2CGK  2CGL  2UYT  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.5
            ExPASy - ENZYME nomenclature database: 2.7.1.5
            ExplorEnz - The Enzyme Database: 2.7.1.5
            ERGO genome analysis and discovery system: 2.7.1.5
            BRENDA, the Enzyme Database: 2.7.1.5
            CAS: 9030-52-8
///
ENTRY       EC 2.7.1.6                  Enzyme
NAME        galactokinase;
            galactokinase (phosphorylating);
            ATP:D-galactose-1-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-galactose 1-phosphotransferase
REACTION    ATP + D-galactose = ADP + alpha-D-galactose 1-phosphate [RN:R01092]
ALL_REAC    R01092
SUBSTRATE   ATP [CPD:C00002];
            D-galactose [CPD:C00124]
PRODUCT     ADP [CPD:C00008];
            alpha-D-galactose 1-phosphate [CPD:C00446]
COMMENT     D-Galactosamine can also act as acceptor.
REFERENCE   1  [PMID:13058412]
  AUTHORS   CARDINI CE, LELOIR LF.
  TITLE     Enzymic phosphorylation of galactosamine and galactose.
  JOURNAL   Arch. Biochem. Biophys. 45 (1953) 55-64.
  ORGANISM  Saccharomyces fragilis
REFERENCE   2
  AUTHORS   Neufeld, E.F., Feingold, D.S. and Hassid, W.Z.
  TITLE     Phosphorylation of D-galactose and L-arabinose by extracts from
            Phaseolus aureus seedlings.
  JOURNAL   J. Biol. Chem. 235 (1960) 906-909.
  ORGANISM  Phaseolus aureus
REFERENCE   3
  AUTHORS   Wilkinson, J.F.
  TITLE     The pathway of the adaptive fermentation of galactose by yeast.
  JOURNAL   Biochem. J. 44 (1949) 460-467.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00052  Galactose metabolism
ORTHOLOGY   KO: K00849  galactokinase
GENES       HSA: 2584(GALK1) 2585(GALK2)
            MMU: 14635(Galk1) 69976(Galk2)
            CFA: 403694(GALK1)
            GGA: 415596(RCJMB04_1i18) 417373(GALK1) 770230(LOC770230)
            XLA: 380379(galk2) 444349(MGC82807)
            XTR: 448280(galk2)
            SPU: 591788(LOC591788) 593554(LOC593554)
            DME: Dmel_CG5288
            CEL: M01D7.4(galactokinase)
            ATH: AT3G06580(GAL1) AT3G10700
            OSA: 4334679 4336928
            CME: CMN198C
            SCE: YBR020W(GAL1) YDR009W(GAL3)
            PIC: PICST_82625(GAL1)
            SPO: SPBPB2B2.13
            ANI: AN4957.2
            AFM: AFUA_3G10300
            AOR: AO090003000570
            CNE: CNB04330 CNM00610
            DDI: DDB_0231667(galK)
            TET: TTHERM_00145260 TTHERM_00703700
            TCR: 507001.110 507009.40 508465.90 510667.120
            LMA: LmjF35.2740
            EHI: 349.t00010
            ECO: b0757(galK)
            ECJ: JW0740(galK)
            ECE: Z0927(galK)
            ECS: ECs0785
            ECC: c0833(galK)
            ECI: UTI89_C0754(galK)
            ECP: ECP_0768
            ECV: APECO1_1331(galK)
            ECW: EcE24377A_0784(galK)
            ECX: EcHS_A0811(galK)
            STY: STY0807(galK)
            STT: t2113(galK)
            SPT: SPA1978(galK)
            SEC: SC0772(galK)
            STM: STM0774(galK)
            YPE: YPO1137(galK)
            YPK: y3045(galK)
            YPM: YP_1022(galK)
            YPA: YPA_1045
            YPN: YPN_2863
            YPP: YPDSF_2560
            YPS: YPTB1169(galK)
            YPI: YpsIP31758_2857(galK)
            SFL: SF0547(galK)
            SFX: S0555(galK)
            SFV: SFV_0583(galK)
            SSN: SSON_0709(galK)
            SBO: SBO_0612(galK) SBO_0872(wcaK)
            SDY: SDY_0704(galK)
            ECA: ECA3170(galK)
            PLU: plu0576(galK)
            SGL: SG0895
            ENT: Ent638_1248
            KPN: KPN_00771(galK)
            HIN: HI0819(galK)
            HIT: NTHI0983(galK)
            HIP: CGSHiEE_07965
            HIQ: CGSHiGG_07595
            HSO: HS_0235(galK)
            PMU: PM1035(galK)
            MSU: MS0648(galK)
            APL: APL_0995(galK)
            VCH: VC1595
            VCO: VC0395_A1197(galK)
            VVU: VV1_1772
            VVY: VV2637
            VPA: VP2398
            VFI: VFA0355
            PPR: PBPRA2080(galK)
            SON: SO_0694(galK)
            SDN: Sden_0414
            SFR: Sfri_3668
            SAZ: Sama_0536
            SBL: Sbal_3728
            SLO: Shew_3271
            SPC: Sputcn32_3249
            SHE: Shewmr4_3408
            SHM: Shewmr7_0544
            SHN: Shewana3_3578
            SHW: Sputw3181_0692
            PHA: PSHAa1769(galK)
            PAT: Patl_0647
            SDE: Sde_1097
            PIN: Ping_2017
            FTU: FTT1476(galK)
            FTF: FTF1476(galK)
            FTW: FTW_0622(galK)
            FTL: FTL_1397
            FTH: FTH_1359(galK)
            FTA: FTA_1485(galK)
            FTN: FTN_0685(galK)
            AHA: AHA_4105(galK)
            NMU: Nmul_A1938
            DDE: Dde_3653
            NAR: Saro_0544
            ELI: ELI_03500
            ABA: Acid345_1701
            BSU: BG10581(galK)
            BHA: BH1107(galK)
            BCZ: pE33L466_0355(galK)
            BLI: BL00191(galK)
            BLD: BLi04282(galK)
            BCL: ABC3219(galK)
            BAY: RBAM_012150(galK1) RBAM_035460(galK)
            BPU: BPUM_3468(galK)
            GKA: GK2150
            GTN: GTNG_2086(galK)
            SSP: SSP0629
            LLA: L0028(galK)
            LLC: LACR_2244
            LLM: llmg_2235(galK)
            SPN: SP_1853
            SPR: spr1668(galK)
            SPD: SPD_1634(galK)
            SMU: SMU.886(galK)
            STC: str1402(galK)
            STL: stu1402(galK)
            SSA: SSA_1008(galK)
            SSU: SSU05_0360
            SSV: SSU98_0351
            SGO: SGO_0932(galK)
            LPL: lp_3482(galK)
            LJO: LJ0859
            LAC: LBA1459(galK)
            LSA: LSA0764(galK)
            LSL: LSL_0381(galK)
            LBR: LVIS_1904
            LCA: LSEI_0664
            LGA: LGAS_1322
            PPE: PEPE_0206
            EFA: EF1069(galK)
            OOE: OEOE_0304
            LME: LEUM_1313
            CAC: CAC2959(galK)
            CPE: CPE1345(galK)
            CPF: CPF_1552(galK)
            CPR: CPR_1345(galK)
            CTC: CTC00865
            CSC: Csac_1511
            TTE: TTE1928(galK)
            MTU: Rv0620(galK)
            MTC: MT0648(galK)
            MBO: Mb0636(galK)
            MBB: BCG_0666(galK)
            MPA: MAP4072(galK)
            MAV: MAV_4564(galK)
            MSM: MSMEG_3692(galK)
            CGL: NCgl2152(cgl2233)
            CGB: cg2452
            CEF: CE2131
            CDI: DIP1015(galK) DIP1674
            CJK: jk0291(galK)
            NFA: nfa45050(galK)
            RHA: RHA1_ro05490(galK)
            SCO: SCO3136(galK)
            SMA: SAV3574(galK)
            AAU: AAur_1279(galK)
            PAC: PPA2192 PPA2287
            TFU: Tfu_2566
            FRA: Francci3_3451
            FAL: FRAAL5626(galK)
            SEN: SACE_1775(galK)
            BLO: BL1210(galK)
            BAD: BAD_1331(galK)
            FNU: FN2107
            TPA: TP0418
            TDE: TDE0455 TDE2212(galK) TDE2298
            LIL: LA3885(galK)
            LIC: LIC13104(galK)
            LBJ: LBJ_0599(galK)
            BTH: BT_0370
            BFR: BF1653
            BFS: BF1661(galK)
            PGI: PG1633(galK)
            CHU: CHU_0657(galK)
            GFO: GFO_2146(galK)
            DGE: Dgeo_2481
            TTH: TTC0226
            TTJ: TTHA0595
            TMA: TM1190
            PHO: PH0369
            PFU: PF0445
            TKO: TK1831
            PAI: PAE1185
STRUCTURES  PDB: 1PIE  1S4E  1WUU  2AJ4  2CZ9  2DEI  2DEJ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.6
            ExPASy - ENZYME nomenclature database: 2.7.1.6
            ExplorEnz - The Enzyme Database: 2.7.1.6
            ERGO genome analysis and discovery system: 2.7.1.6
            BRENDA, the Enzyme Database: 2.7.1.6
            CAS: 9030-53-9
///
ENTRY       EC 2.7.1.7                  Enzyme
NAME        mannokinase;
            mannokinase (phosphorylating);
            D-fructose (D-mannose) kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-mannose 6-phosphotransferase
REACTION    ATP + D-mannose = ADP + D-mannose 6-phosphate [RN:R01326]
ALL_REAC    R01326
SUBSTRATE   ATP [CPD:C00002];
            D-mannose [CPD:C00159]
PRODUCT     ADP [CPD:C00008];
            D-mannose 6-phosphate [CPD:C00275]
REFERENCE   1  [PMID:13242546]
  AUTHORS   BUEDING E, MACKINNON JA.
  TITLE     Hexokinases of Schistosoma mansoni.
  JOURNAL   J. Biol. Chem. 215 (1955) 495-506.
  ORGANISM  Schistosoma mansoni
PATHWAY     PATH: map00051  Fructose and mannose metabolism
GENES       GBE: GbCGDNIH1_0217
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.7
            ExPASy - ENZYME nomenclature database: 2.7.1.7
            ExplorEnz - The Enzyme Database: 2.7.1.7
            ERGO genome analysis and discovery system: 2.7.1.7
            BRENDA, the Enzyme Database: 2.7.1.7
            CAS: 9030-54-0
///
ENTRY       EC 2.7.1.8                  Enzyme
NAME        glucosamine kinase;
            glucosamine kinase (phosphorylating);
            ATP:2-amino-2-deoxy-D-glucose-6-phosphotransferase;
            aminodeoxyglucose kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-glucosamine phosphotransferase
REACTION    ATP + D-glucosamine = ADP + D-glucosamine phosphate [RN:R01961]
ALL_REAC    R01961
SUBSTRATE   ATP [CPD:C00002];
            D-glucosamine [CPD:C00329]
PRODUCT     ADP [CPD:C00008];
            D-glucosamine phosphate [CPD:C00352]
REFERENCE   1  [PMID:13242546]
  AUTHORS   BUEDING E, MACKINNON JA.
  TITLE     Hexokinases of Schistosoma mansoni.
  JOURNAL   J. Biol. Chem. 215 (1955) 495-506.
  ORGANISM  Schistosoma mansoni
PATHWAY     PATH: map00530  Aminosugars metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.8
            ExPASy - ENZYME nomenclature database: 2.7.1.8
            ExplorEnz - The Enzyme Database: 2.7.1.8
            ERGO genome analysis and discovery system: 2.7.1.8
            BRENDA, the Enzyme Database: 2.7.1.8
            CAS: 9031-90-7
///
ENTRY       EC 2.7.1.9        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Deleted entry: acetylaminodeoxyglucose kinase (EC 2.7.1.9 created
            1961, deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.9
            ExPASy - ENZYME nomenclature database: 2.7.1.9
            ExplorEnz - The Enzyme Database: 2.7.1.9
            ERGO genome analysis and discovery system: 2.7.1.9
            BRENDA, the Enzyme Database: 2.7.1.9
///
ENTRY       EC 2.7.1.10                 Enzyme
NAME        phosphoglucokinase;
            glucose-phosphate kinase;
            phosphoglucokinase (phosphorylating);
            ATP:D-glucose-1-phosphate 6-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:alpha-D-glucose-1-phosphate 6-phosphotransferase
REACTION    ATP + alpha-D-glucose 1-phosphate = ADP + alpha-D-glucose
            1,6-bisphosphate [RN:R00949]
ALL_REAC    R00949
SUBSTRATE   ATP [CPD:C00002];
            alpha-D-glucose 1-phosphate [CPD:C00103]
PRODUCT     ADP [CPD:C00008];
            alpha-D-glucose 1,6-bisphosphate [CPD:C01231]
REFERENCE   1
  AUTHORS   Paladini, A.C., Caputto, R., Leloir, L.F., Trucco, R.E. and Cardini,
            C.E.
  TITLE     The enzymatic synthesis of glucose-1,6-diphosphate.
  JOURNAL   Arch. Biochem. 23 (1949) 55-66.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.10
            ExPASy - ENZYME nomenclature database: 2.7.1.10
            ExplorEnz - The Enzyme Database: 2.7.1.10
            ERGO genome analysis and discovery system: 2.7.1.10
            BRENDA, the Enzyme Database: 2.7.1.10
            CAS: 9032-96-6
///
ENTRY       EC 2.7.1.11                 Enzyme
NAME        6-phosphofructokinase;
            phosphohexokinase;
            phosphofructokinase I;
            phosphofructokinase (phosphorylating);
            6-phosphofructose 1-kinase;
            ATP-dependent phosphofructokinase;
            D-fructose-6-phosphate 1-phosphotransferase;
            fructose 6-phosphate kinase;
            fructose 6-phosphokinase;
            nucleotide triphosphate-dependent phosphofructokinase;
            phospho-1,6-fructokinase;
            PFK
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-fructose-6-phosphate 1-phosphotransferase
REACTION    ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
            [RN:R00756]
ALL_REAC    R00756 > R04779;
            (other) R00767 R00769 R00770 R01843 R01846 R01847 R01848 R03236
            R03237 R03238 R03239
SUBSTRATE   ATP [CPD:C00002];
            D-fructose 6-phosphate [CPD:C00085]
PRODUCT     ADP [CPD:C00008];
            D-fructose 1,6-bisphosphate [CPD:C00354]
EFFECTOR    ADP [CPD:C00008];
            GDP [CPD:C00035];
            Phosphoenolpyruvate [CPD:C00074]
COMMENT     D-Tagatose 6-phosphate and sedoheptulose 7-phosphate can act as
            acceptors. UTP, CTP and ITP can act as donors. Not identical with EC
            2.7.1.105 6-phosphofructo-2-kinase.
REFERENCE   1
  AUTHORS   Axelrod, B., Saltman, P., Bandurski, R.S. and Baker, R.S.
  TITLE     Hexokinase in higher plants.
  JOURNAL   J. Biol. Chem. 197 (1952) 89-96.
  ORGANISM  Pisum sativum
REFERENCE   2
  AUTHORS   Ling, K.H., Pastkau, V., Marcus, F. and Lardy, H.A.
  TITLE     Phosphofructokinase. I. Skeletal muscle.
  JOURNAL   Methods Enzymol. 9 (1966) 425-429.
REFERENCE   3
  AUTHORS   Mansour, T.E.
  TITLE     Phosphofructokinase. II. Heart muscle.
  JOURNAL   Methods Enzymol. 9 (1966) 430-436.
  ORGANISM  sheep
REFERENCE   4  [PMID:4237772]
  AUTHORS   Odeide R, Guilloton M, Dupuis B, Ravon D, Rosenberg AJ.
  TITLE     [Study of an enzyme allosteric to 2 substrates: phosphofructokinase
            of rat muscle. I. Preparation and crystallization of the enzyme]
  JOURNAL   Bull. Soc. Chim. Biol. (Paris). 50 (1968) 2023-33.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:4224472]
  AUTHORS   Parmeggiani A, Luft JH, Love DS, Krebs EG.
  TITLE     Crystallization and properties of rabbit skeletal muscle
            phosphofructokinase.
  JOURNAL   J. Biol. Chem. 241 (1966) 4625-37.
  ORGANISM  rabbit
REFERENCE   6
  AUTHORS   Racker, E.
  TITLE     Spectrophotometric measurement of hexokinase and phosphohexokinase
            activity.
  JOURNAL   J. Biol. Chem. 167 (1947) 843-854.
  ORGANISM  rabbit
REFERENCE   7
  AUTHORS   Sols, A. and Salas, M.L.
  TITLE     Phosphofructokinase. III. Yeast.
  JOURNAL   Methods Enzymol. 9 (1966) 436-442.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   8  [PMID:4248230]
  AUTHORS   Uyeda K, Kurooka S.
  TITLE     Crystallization and properties of phosphofructokinase from
            Clostridium pasteurianum.
  JOURNAL   J. Biol. Chem. 245 (1970) 3315-24.
  ORGANISM  Clostridium pasteurianum
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00030  Pentose phosphate pathway
            PATH: map00051  Fructose and mannose metabolism
            PATH: map00052  Galactose metabolism
            PATH: map04910  Insulin signaling pathway
ORTHOLOGY   KO: K00850  6-phosphofructokinase
GENES       HSA: 5211(PFKL) 5213(PFKM) 5214(PFKP)
            PTR: 450266(PFKP) 451863(PFKM)
            MMU: 18641(Pfkl) 18642(Pfkm) 56421(Pfkp)
            RNO: 25741(Pfkl) 65152(Pfkm)
            CFA: 403849(PFKM) 478019(PFKP) 487797(PFKL)
            GGA: 374064(PFKM) 769850(PFKL)
            XLA: 379632(MGC68847) 446756(MGC79063)
            XTR: 394825(pfkp)
            SPU: 548617(LOC548617)
            DME: Dmel_CG4001(Pfk)
            CEL: C50F4.2(6-phosphofructokinase) Y71H10A.1(phosphofructokinase)
            SCE: YGR240C(PFK1) YMR205C(PFK2)
            AGO: AGOS_AEL208W AGOS_AFL185W
            PIC: PICST_66973(PFK2) PICST_70563(PFK1)
            CGR: CAGL0F08041g CAGL0I05698g CAGL0L10758g
            SPO: SPBC16H5.02
            ANI: AN3223.2
            AFM: AFUA_4G00960
            AOR: AO090003001390 AO090010000444
            ANG: An18g01670(pfkA)
            CNE: CNJ01080
            UMA: UM02512.1
            ECU: ECU03_0680
            DDI: DDB_0191364(pfkA)
            PFA: PF11_0294 PFI0755c
            CPV: cgd2_2130
            TBR: Tb927.3.3270
            TCR: 508153.340
            LMA: LmjF29.2510
            EHI: 12.t00038 74.t00023 85.t00007
            ECO: b1723(pfkB) b3916(pfkA)
            ECJ: JW3887(pfkA) JW5280(pfkB)
            ECE: Z2752(pfkB) Z5460(pfkA)
            ECS: ECs2429 ECs4841
            ECC: c2121(pfkB) c4867(pfkA)
            ECI: UTI89_C1916(pfkB) UTI89_C4499(pfkA)
            ECP: ECP_1670 ECP_4125
            ECV: APECO1_2553(pfkA) APECO1_793(pfkB)
            ECW: EcE24377A_1943(pfkB) EcE24377A_4449(pfkA)
            ECX: EcHS_A1804 EcHS_A4146
            STY: STY1785(pfkB) STY3809(pfkA)
            STT: t1206(pfkB) t3557(pfkA)
            SPT: SPA1518(pfkB) SPA3905(pfkA)
            SEC: SC1347(pfkB) SC3953(pfkA)
            STM: STM1326(pfkB) STM4062(pfkA)
            YPE: YPO0078(pfkA)
            YPK: y0059(pfkA)
            YPM: YP_0080(pfkA)
            YPA: YPA_3463
            YPN: YPN_3770
            YPP: YPDSF_3826
            YPS: YPTB0074(pfkA)
            YPI: YpsIP31758_0089(pfkA)
            SFL: SF1507(pfkB) SF3994(pfkA)
            SFX: S1624(pfkB) S3753(pfkA)
            SFV: SFV_1498(pfkB) SFV_3578(pfkA)
            SSN: SSON_1434(pfkB) SSON_4085(pfkA)
            SBO: SBO_1367(pfkB) SBO_3933(pfkA)
            SDY: SDY_1816(pfkB) SDY_3831(pfkA)
            ECA: ECA2352 ECA4307(pfkA)
            PLU: plu4774(pfkA)
            BUC: BU305(pfkA)
            BAS: BUsg295(pfkA)
            BAB: bbp284(pfkA)
            BCC: BCc_187(pfkA)
            SGL: SG2178
            ENT: Ent638_4056
            SPE: Spro_4807
            BFL: Bfl602(pfkA)
            BPN: BPEN_624(pfkA)
            HIT: NTHI1154(pfkA)
            HIP: CGSHiEE_07055
            HIQ: CGSHiGG_08490
            HDU: HD0465(pfkA)
            HSO: HS_0485(pfkA)
            PMU: PM0069(pfkA)
            MSU: MS0377(pfkA)
            APL: APL_1124(pfkA)
            ASU: Asuc_0687
            XFA: XF0274
            XFT: PD0221(pfkA)
            XCC: XCC3292(pfkA)
            XCB: XC_0872
            XCV: XCV3554(pfkA)
            XAC: XAC3438(pfkA)
            XOO: XOO0962(pfkA)
            XOM: XOO_0878(XOO0878)
            VCH: VC2689
            VCO: VC0395_A2261(pfkA)
            VVU: VV1_1257
            VVY: VV3110
            VPA: VP2855
            VFI: VF2340(pfkA)
            PPR: PBPRA0234(pfkA)
            ILO: IL1211(pfkA)
            CPS: CPS_0649(pfkA)
            PAT: Patl_2087 Patl_2592
            SDE: Sde_0935
            PIN: Ping_0591 Ping_1316
            CBU: CBU_0341(pfkA) CBU_1273
            CBD: COXBU7E912_1738(pfkA)
            LPN: lpg1913
            LPF: lpl1877(pfp)
            LPP: lpp1888(pfp)
            MCA: MCA1251
            TCX: Tcr_1583
            NOC: Noc_2846
            HCH: HCH_05798(pfkA)
            CSA: Csal_1534
            ABO: ABO_1989(pfkA)
            AHA: AHA_2383(pfkA)
            BCI: BCI_0171(pfkA)
            VOK: COSY_0098(pfkA)
            CVI: CV_1745(pfkA)
            BMA: BMAA0117(pfk)
            BMV: BMASAVP1_1282(pfk)
            BMN: BMA10247_A0142(pfk)
            BPS: BPSS1957
            BPM: BURPS1710b_A1061(pfk)
            BPD: BURPS668_A2801(pfk)
            BTE: BTH_II0415
            RFR: Rfer_0362 Rfer_1479
            POL: Bpro_2756
            AJS: Ajs_3260
            MPT: Mpe_A2776
            NEU: NE1934
            NET: Neut_0787
            NMU: Nmul_A0740
            EBA: ebA5088(pfkA)
            AZO: azo1474(pfkA)
            DAR: Daro_3204
            TBD: Tbd_1502
            WSU: WS1028(ftsI)
            TDN: Tmden_0549
            NIS: NIS_0897(pfkA)
            SUN: SUN_1472(pfkA)
            GSU: GSU1703(pfk) GSU2068
            GME: Gmet_0938 Gmet_1640
            GUR: Gura_1703 Gura_2076
            PCA: Pcar_1508 Pcar_1542
            DVU: DVU2061(pfkA)
            DVL: Dvul_1167
            BBA: Bd3384
            DPS: DP1909
            MXA: MXAN_2372(pfkB) MXAN_4016(pfkA) MXAN_6373(pfkA)
            SAT: SYN_00886
            SFU: Sfum_3671
            MLO: mll5025
            PLA: Plav_0616
            BJA: bll2850 blr4659
            BRA: BRADO1575
            BBT: BBta_6479
            RPA: RPA0379(pfkB)
            RPB: RPB_0444(pfkB)
            RPC: RPC_0700
            RPD: RPD_0347
            RPE: RPE_0769
            NHA: Nham_0911
            RSP: RSP_2334(pfkB)
            SWI: Swit_3015
            RRU: Rru_A1047
            MAG: amb2301 amb4075
            MGM: Mmc1_1917 Mmc1_3024
            ABA: Acid345_1623 Acid345_3032 Acid345_4086
            BSU: BG12644(pfk)
            BHA: BH3164(pfkA)
            BAN: BA4844(pfk)
            BAR: GBAA4844(pfk)
            BAA: BA_5267
            BAT: BAS4493
            BCE: BC4600(pfkA)
            BCA: BCE_4730(pfk)
            BCZ: BCZK4340(pfkA)
            BCY: Bcer98_3283
            BTK: BT9727_4328(pfkA)
            BTL: BALH_4182(pfk)
            BLI: BL00403(pfkA)
            BLD: BLi03068(pfkA)
            BCL: ABC2719(pfkA) ABC3502
            BAY: RBAM_026240
            BPU: BPUM_2562
            OIH: OB2172(pfkA)
            GKA: GK2740(pfkA)
            GTN: GTNG_2664
            SAU: SA1521(pfk)
            SAV: SAV1698(pfk)
            SAM: MW1642(pfk)
            SAR: SAR1777(pfkA)
            SAS: SAS1626(pfkA)
            SAC: SACOL1746(pfkA)
            SAB: SAB1557c(pfkA)
            SAA: SAUSA300_1645(pfkA)
            SAO: SAOUHSC_01807
            SAJ: SaurJH9_1755
            SAH: SaurJH1_1789
            SEP: SE1374
            SER: SERP1262(pfkA)
            SHA: SH1226(pfk)
            SSP: SSP1068
            LMO: lmo1571(pfk)
            LMF: LMOf2365_1593(pfkA)
            LIN: lin1606
            LWE: lwe1584(pfk)
            LLA: L0002(pfk)
            LLC: LACR_1457
            LLM: llmg_1118(pfk)
            SPY: SPy_1283(pfk)
            SPZ: M5005_Spy_0989(pfkA)
            SPM: spyM18_1231(pfk)
            SPG: SpyM3_0913(pfk)
            SPS: SPs1112
            SPH: MGAS10270_Spy1103(pfk)
            SPI: MGAS10750_Spy1139(pfk)
            SPJ: MGAS2096_Spy1049(pfk)
            SPK: MGAS9429_Spy1093(pfk)
            SPF: SpyM50812(pfk)
            SPA: M6_Spy0976(pfkA)
            SPB: M28_Spy0961(pfkA)
            SPN: SP_0896
            SPR: spr0796(pfkA)
            SPD: SPD_0789(pfkA)
            SAG: SAG0940(pfk)
            SAN: gbs0930(pfk)
            SAK: SAK_1036(pfkA)
            SMU: SMU.1191(pfkA)
            STC: str1197(pfk)
            STL: stu1197(pfk)
            SSA: SSA_0847(pfk)
            LPL: lp_1898(pfkA)
            LJO: LJ1079
            LAC: LBA0956
            LSA: LSA1033(pfk)
            LSL: LSL_0866(pfkA)
            LDB: Ldb0838(pfk1) Ldb1772(pfk2)
            LBU: LBUL_0761 LBUL_1642
            LCA: LSEI_1364
            EFA: EF1045(pfk)
            STH: STH837
            CAC: CAC0517(pfk)
            CPE: CPE0361(pfk) CPE1185(pfk) CPE1467(pfk)
            CPF: CPF_0350(pfkA) CPF_1389 CPF_1718
            CPR: CPR_0341(pfkA) CPR_1203 CPR_1446
            CTC: CTC02490(pfkA)
            CNO: NT01CX_1297
            CTH: Cthe_1261
            CDF: CD3395(pfkA)
            CBO: CBO3373(pfkA)
            CBA: CLB_3429(pfkA)
            CBH: CLC_3316(pfkA)
            CBF: CLI_3557(pfkA)
            CBE: Cbei_0998 Cbei_4852
            CKL: CKL_3559(pfk1)
            AMT: Amet_4069
            CHY: CHY_1143(pfkA) CHY_1349
            DSY: DSY1413 DSY1501 DSY1839
            DRM: Dred_1798 Dred_2313
            SWO: Swol_1170 Swol_2041
            CSC: Csac_1830
            TTE: TTE1816(pfkA)
            MTA: Moth_1234 Moth_1738 Moth_1868
            MGE: MG_215(pfkA)
            MPN: MPN302(pfkA)
            MPU: MYPU_6010(pfk)
            MPE: MYPE5920(pfk)
            MGA: MGA_0157(pfkA)
            MMY: MSC_0260(pfk)
            MMO: MMOB3200(pfkA)
            MHY: mhp269(pfkA)
            MHJ: MHJ_0107(pfkA)
            MHP: MHP7448_0111(pfkA)
            MSY: MS53_0296(pfk)
            MCP: MCAP_0220(pfkA)
            UUR: UU185(pfkA)
            POY: PAM281(pfkA)
            AYW: AYWB_440(pfkA)
            MFL: Mfl174
            MTU: Rv2029c(pfkB) Rv3010c(pfkA)
            MTC: MT2088 MT3090(pfkA)
            MBO: Mb2054c(pfkB) Mb3035c(pfkA)
            MBB: BCG_3032c(pfkA)
            MLE: ML1701(pfkA)
            MPA: MAP3044c(pfkA)
            MAV: MAV_3858
            MSM: MSMEG_3947
            MVA: Mvan_2116
            MGI: Mflv_4245
            MMC: Mmcs_1892
            MKM: Mkms_1938
            MJL: Mjls_1872
            CGL: NCgl1202(cgl1250) NCgl1860(cgl1935)
            CGB: cg1409(pfkA)
            CEF: CE1348
            CDI: DIP1088(pfkA)
            CJK: jk1308
            NFA: nfa42410(pfkA)
            RHA: RHA1_ro06479(pfkA)
            SCO: SCO1214(2SCG58.14) SCO2119(pfkA) SCO5426(pfkA2)
            SMA: SAV2822(pfkA1) SAV6083(pfkA2) SAV7123(pfkA3)
            LXX: Lxx07530(pfkA)
            ART: Arth_3003
            AAU: AAur_2976(pfkA)
            PAC: PPA0090(pfkA) PPA0143 PPA2267
            TFU: Tfu_1037
            FRA: Francci3_2843 Francci3_3085
            FAL: FRAAL4376 FRAAL5084(pfkA)
            ACE: Acel_0983
            KRA: Krad_3234 Krad_4274
            SEN: SACE_1704(pfkA)
            RXY: Rxyl_2082 Rxyl_2588
            FNU: FN0410
            RBA: RB7572(pfkA)
            TDE: TDE0064(pfk)
            LIL: LB111
            SYN: sll0745(pfkA) sll1196(pfkA)
            SYC: syc0931_d(pfkA)
            SYF: Synpcc7942_0592
            CYB: CYB_2199
            TEL: tll1316
            ANA: all7335 alr1913
            AVA: Ava_3044(pfkA)
            BTH: BT_1102 BT_2062 BT_3356
            BFR: BF0217 BF3749
            BFS: BF0176(pfkA) BF3537(pfkA)
            SRU: SRU_0825(pfkA) SRU_2111
            CHU: CHU_1600(pfkB) CHU_2773(pfkA)
            GFO: GFO_1643(pfkA) GFO_2131(pfkA)
            FJO: Fjoh_4591
            FPS: FP1614(pfkA)
            CTE: CT0250(pfk-2) CT1603(pfk-1)
            CCH: Cag_0879(pfkA) Cag_1780
            CPH: Cpha266_2597
            PVI: Cvib_1665
            PLT: Plut_1600 Plut_2022(pfkA)
            RRS: RoseRS_1829 RoseRS_1831 RoseRS_2734
            RCA: Rcas_1875 Rcas_2513 Rcas_2515
            DRA: DR_0635
            DGE: Dgeo_1637
            TTH: TTC1597(pfkA)
            TTJ: TTHA1962
            AAE: aq_1708(pfkA)
            TMA: TM0209 TM0289
            TPT: Tpet_0623 Tpet_0715
            TME: Tmel_1595 Tmel_1902
            FNO: Fnod_1343 Fnod_1661
            MHU: Mhun_0556 Mhun_1465
            MEM: Memar_0927 Memar_1368
            MBN: Mboo_1941
            HMA: rrnAC0249(pfk3) rrnAC0342(pfk4) rrnAC0545(pfk1)
            PTO: PTO1237
            RCI: RRC499(pfkA)
STRUCTURES  PDB: 1MTO  1PFK  1ZXX  2HIG  2PFK  3PFK  4PFK  6PFK  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.11
            ExPASy - ENZYME nomenclature database: 2.7.1.11
            ExplorEnz - The Enzyme Database: 2.7.1.11
            ERGO genome analysis and discovery system: 2.7.1.11
            BRENDA, the Enzyme Database: 2.7.1.11
            CAS: 9001-80-3
///
ENTRY       EC 2.7.1.12                 Enzyme
NAME        gluconokinase;
            gluconokinase (phosphorylating);
            gluconate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-gluconate 6-phosphotransferase
REACTION    ATP + D-gluconate = ADP + 6-phospho-D-gluconate [RN:R01737]
ALL_REAC    R01737
SUBSTRATE   ATP [CPD:C00002];
            D-gluconate [CPD:C00257]
PRODUCT     ADP [CPD:C00008];
            6-phospho-D-gluconate [CPD:C00345]
REFERENCE   1  [PMID:14832279]
  AUTHORS   COHEN SS.
  TITLE     Gluconokinase and the oxidative path of glucose-6-phosphate
            utilization.
  JOURNAL   J. Biol. Chem. 189 (1951) 617-28.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:13416223]
  AUTHORS   LEDER IG.
  TITLE     Hog kidney gluconokinase.
  JOURNAL   J. Biol. Chem. 225 (1957) 125-36.
  ORGANISM  pig [GN:ssc]
REFERENCE   3
  AUTHORS   Narrod, S.A. and Wood, W.A.
  TITLE     Carbohydrate oxidation by Pseudomonas fluorescens. V. Evidence for
            gluconokinase and 2-ketogluconokinase.
  JOURNAL   J. Biol. Chem. 220 (1956) 45-55.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   4  [PMID:12980980]
  AUTHORS   SABLE HZ, GUARINO AJ.
  TITLE     Phosphorylation of gluconate in yeast extracts.
  JOURNAL   J. Biol. Chem. 196 (1952) 395-402.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00030  Pentose phosphate pathway
ORTHOLOGY   KO: K00851  gluconokinase
GENES       CEL: F26D11.1(gluconokinase)
            ATH: AT2G16790
            SCE: YDR248C
            AGO: AGOS_ADR164C
            PIC: PICST_83065(GLK2)
            CGR: CAGL0K11297g
            SPO: SPAC4G9.12
            ANI: AN3641.2
            AFM: AFUA_1G00530 AFUA_4G12050
            AOR: AO090003001003
            CNE: CNC00400
            DDI: DDB_0231437
            TCR: 508177.20 511693.60
            ECO: b3437(gntK) b4268(idnK)
            ECJ: JW3400(gntK) JW4225(idnK)
            ECE: Z4805(gntK)
            ECS: ECs4286
            ECC: c4225(gntK) c5369(idnK)
            ECI: UTI89_C3945(gntK) UTI89_C4003 UTI89_C4875(idnK)
            ECP: ECP_3532
            ECV: APECO1_2126(idnK) APECO1_3021(gntK)
            ECW: EcE24377A_3915(gntK)
            ECX: EcHS_A3636(gntK) EcHS_A4524
            STY: STY4269(gntK)
            STT: t3980(gntK)
            SPT: SPA3393(gntK) SPA4285(idnK)
            SEC: SC3472(gntK) SC4341(idnK)
            STM: STM3542(gntK) STM4485(idnK)
            YPE: YPO2540(idnK) YPO3953
            YPK: y1646(gntV) y3876(gntV)
            YPM: YP_2351(idnK) YP_3315(gntV)
            YPA: YPA_2032 YPA_3782
            YPN: YPN_2135 YPN_3602
            YPP: YPDSF_1950 YPDSF_3318
            YPS: YPTB2572(idnK) YPTB3796
            YPI: YpsIP31758_1469(idnK) YpsIP31758_4020(gntK)
            SFL: SF3459(gntK)
            SFX: S4303(gntK)
            SFV: SFV_3445(gntK)
            SSN: SSON_3679(gntK) SSON_4453(idnK)
            SBO: SBO_3434(gntK)
            SDY: SDY_3588(gntK)
            ECA: ECA1839(gntV) ECA4159
            PLU: plu0497(gntK)
            SGL: SG2151
            ENT: Ent638_3845
            SPE: Spro_4497 Spro_4650
            HSO: HS_0379(glk)
            PMU: PM0792(glk)
            MSU: MS0957(gntK)
            APL: APL_1666(gntK)
            ASU: Asuc_1154
            XCC: XCC4079(idnK)
            XCB: XC_4170
            XCV: XCV4297(idnK)
            XAC: XAC4197(idnK)
            XOO: XOO0332(idnK)
            XOM: XOO_0304(XOO0304)
            VCH: VC0287
            VCO: VC0395_A2665(gntV)
            VVU: VV1_1100
            VVY: VV0060
            VPA: VP0063
            PAE: PA2321
            PAU: PA14_34640(gnuK)
            PPU: PP_3416(gnuK)
            PPF: Pput_2346
            PST: PSPTO_3564(gntV)
            PSB: Psyr_3337
            PSP: PSPPH_3258
            PFL: PFL_4580
            PFO: Pfl_4336
            PEN: PSEEN2421
            PMY: Pmen_2569
            ACI: ACIAD0545(gntK)
            SBL: Sbal_4087
            SBM: Shew185_4056
            CPS: CPS_3695
            PHA: PSHAb0480(idnK)
            PAT: Patl_3644
            SDE: Sde_0904
            PIN: Ping_2932 Ping_2936
            HCH: HCH_03543
            CSA: Csal_0926
            NME: NMB2028
            NMA: NMA0412
            NMC: NMC2007
            NGO: NGO2076
            CVI: CV_2957(gntV)
            RSO: RS05387(RSp0946) RSc0441(gntK)
            REU: Reut_A1082
            REH: H16_A1179(gntK)
            RME: Rmet_1046
            BMA: BMA1194 BMA2443(gntK)
            BMV: BMASAVP1_A0359(gntK)
            BML: BMA10299_A1217(gntK)
            BMN: BMA10247_2628(gntK)
            BXE: Bxe_A0592
            BVI: Bcep1808_0631
            BUR: Bcep18194_A3749
            BCN: Bcen_0180
            BCH: Bcen2424_0663
            BAM: Bamb_0558
            BPS: BPSL2929
            BPM: BURPS1710b_2073
            BTE: BTH_I1220 BTH_I2431
            RFR: Rfer_0956
            POL: Bpro_3525
            PNA: Pnap_0046
            AAV: Aave_2797
            AJS: Ajs_2053
            AFW: Anae109_0595
            MXA: MXAN_0616(idnK)
            MLO: mll1676
            MES: Meso_0316
            SME: SMa0514(idnK) SMb21119(gntK)
            SMD: Smed_4531
            ATU: Atu0195(gntK)
            ATC: AGR_C_329
            RET: RHE_CH00741(gntK) RHE_PC00145(idnK)
            RLE: RL0783(idnK) pRL100392(idnK)
            OAN: Oant_3755
            BJA: blr6762
            BRA: BRADO5812
            BBT: BBta_6318
            RPA: RPA3638
            RPB: RPB_1888
            RPC: RPC_3674
            RPD: RPD_3478
            RPE: RPE_3712
            NWI: Nwi_2645
            NHA: Nham_3273
            XAU: Xaut_1235
            PDE: Pden_2932
            MMR: Mmar10_2730
            ZMO: ZMO1757(gntK)
            GOX: GOX1709
            GBE: GbCGDNIH1_0859
            ACR: Acry_1272
            ABA: Acid345_0242
            BSU: BG10649(gntK)
            BHA: BH2676(gntK)
            BAN: BA3428(gntK)
            BAR: GBAA3428(gntK)
            BAA: BA_0743 BA_0744 BA_3926
            BAT: BAS0163 BAS0164 BAS3177
            BCE: BC2223 BC3369
            BCA: BCE_2302(gntK) BCE_3017 BCE_3407(gntK)
            BCZ: BCZK0155(gntK) BCZK3078(gntK)
            BTK: BT9727_0157(gntK) BT9727_2056(gntK) BT9727_2057(gntK)
                 BT9727_3161(gntK)
            BTL: BALH_0159(gntK) BALH_2034(gntK)
            BLI: BL00195(gntK)
            BLD: BLi04287(gntK)
            BCL: ABC2000(gntK)
            BAY: RBAM_031430(gntK)
            BPU: BPUM_3602(gntK)
            OIH: OB3189(gntK)
            GKA: GK1941
            SAU: SA2294(gntK)
            SAV: SAV2506(gntK)
            SAM: MW2424(gntK)
            SAR: SAR2583(gntK)
            SAS: SAS2391
            SAC: SACOL2515(gntK)
            SAB: SAB2378c(gntK)
            SAA: SAUSA300_2443(gntK)
            SAO: SAOUHSC_02808
            SEP: SE2045
            SER: SERP2058(gntK)
            SHA: SH0575(gntK)
            SSP: SSP0411
            LMO: lmo2712
            LMF: LMOf2365_2692
            LIN: lin2860
            LWE: lwe2664
            LLA: L52019(gntK)
            LLC: LACR_2496
            LLM: llmg_2468(gntK)
            LPL: lp_1250(gntK)
            LJO: LJ0405
            LAC: LBA0354
            LSA: LSA0298(gntK)
            LBR: LVIS_0143 LVIS_1585
            LCA: LSEI_0228
            LGA: LGAS_0347
            PPE: PEPE_1361
            EFA: EF3235
            OOE: OEOE_1421
            LME: LEUM_0552
            MPA: MAP1778c
            MVA: Mvan_5911
            MGI: Mflv_0502
            MMC: Mmcs_5328
            MKM: Mkms_5417
            MJL: Mjls_5707
            CGL: NCgl2399(cgl2485) NCgl2905(cgl3008)
            CGB: cg2732(gntV) cg3336(gntK)
            CEF: CE2384 CE2840
            CDI: DIP0254
            CJK: jk0381(gntK)
            NFA: nfa23660
            RHA: RHA1_ro02362 RHA1_ro03300
            SCO: SCO1679(SCI52.21)
            SMA: SAV1925(gntK1) SAV6629(gntK2)
            CMI: CMM_2907(gntK)
            PAC: PPA0739
            NCA: Noca_3722
            TFU: Tfu_2114
            KRA: Krad_0597
            SEN: SACE_3356
            BLO: BL0620(gntK)
            BAD: BAD_0199
            GVI: gll2818
            ANA: alr3086
            AVA: Ava_4858
            TER: Tery_2732
            DRA: DR_1910
            AAE: aq_1484 aq_288
            TMA: TM0443
STRUCTURES  PDB: 1KNQ  1KO1  1KO4  1KO5  1KO8  1KOF  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.12
            ExPASy - ENZYME nomenclature database: 2.7.1.12
            ExplorEnz - The Enzyme Database: 2.7.1.12
            ERGO genome analysis and discovery system: 2.7.1.12
            BRENDA, the Enzyme Database: 2.7.1.12
            CAS: 9030-55-1
///
ENTRY       EC 2.7.1.13                 Enzyme
NAME        dehydrogluconokinase;
            ketogluconokinase;
            2-ketogluconate kinase;
            ketogluconokinase (phosphorylating);
            2-ketogluconokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:2-dehydro-D-gluconate 6-phosphotransferase
REACTION    ATP + 2-dehydro-D-gluconate = ADP + 6-phospho-2-dehydro-D-gluconate
            [RN:R02658]
ALL_REAC    R02658;
            (other) R00162
SUBSTRATE   ATP [CPD:C00002];
            2-dehydro-D-gluconate [CPD:C00629]
PRODUCT     ADP [CPD:C00008];
            6-phospho-2-dehydro-D-gluconate [CPD:C01218]
REFERENCE   1  [PMID:13894459]
  AUTHORS   FRAMPTON EW, WOOD WA.
  TITLE     Purification and properties of 2-ketogluconokinase from Aerobacter
            aerogenes.
  JOURNAL   J. Biol. Chem. 236 (1961) 2578-80.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00030  Pentose phosphate pathway
GENES       REH: H16_B1812(kguK)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.13
            ExPASy - ENZYME nomenclature database: 2.7.1.13
            ExplorEnz - The Enzyme Database: 2.7.1.13
            ERGO genome analysis and discovery system: 2.7.1.13
            BRENDA, the Enzyme Database: 2.7.1.13
            CAS: 9030-56-2
///
ENTRY       EC 2.7.1.14                 Enzyme
NAME        sedoheptulokinase;
            heptulokinase;
            sedoheptulokinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:sedoheptulose 7-phosphotransferase
REACTION    ATP + sedoheptulose = ADP + sedoheptulose 7-phosphate [RN:R01844]
ALL_REAC    R01844;
            (other) R03819
SUBSTRATE   ATP [CPD:C00002];
            sedoheptulose [CPD:C02076]
PRODUCT     ADP [CPD:C00008];
            sedoheptulose 7-phosphate [CPD:C00281]
REFERENCE   1
  AUTHORS   Ebata, M., Sato, R. and Bak, T.
  TITLE     The enzymic phosphorylation of sedoheptulose.
  JOURNAL   J. Biochem. (Tokyo) 42 (1955) 715-725.
  ORGANISM  Bacillus sp.
PATHWAY     PATH: map00710  Carbon fixation
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.14
            ExPASy - ENZYME nomenclature database: 2.7.1.14
            ExplorEnz - The Enzyme Database: 2.7.1.14
            ERGO genome analysis and discovery system: 2.7.1.14
            BRENDA, the Enzyme Database: 2.7.1.14
            CAS: 9030-63-1
///
ENTRY       EC 2.7.1.15                 Enzyme
NAME        ribokinase;
            deoxyribokinase;
            ribokinase (phosphorylating);
            D-ribokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-ribose 5-phosphotransferase
REACTION    ATP + D-ribose = ADP + D-ribose 5-phosphate [RN:R01051]
ALL_REAC    R01051;
            (other) R02750
SUBSTRATE   ATP [CPD:C00002];
            D-ribose [CPD:C00121]
PRODUCT     ADP [CPD:C00008];
            D-ribose 5-phosphate [CPD:C00117]
COMMENT     2-Deoxy-D-ribose can also act as acceptor.
REFERENCE   1
  AUTHORS   Agranoff, B.W. and Brady, R.O.
  TITLE     Purification and properties of calf liver ribokinase.
  JOURNAL   J. Biol.Chem. 219 (1956) 221-229.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:13641245]
  AUTHORS   GINSBURG A.
  TITLE     A deoxyribokinase from Lactobacillus plantarum.
  JOURNAL   J. Biol. Chem. 234 (1959) 481-7.
  ORGANISM  Lactobacillus plantarum [GN:lpl]
PATHWAY     PATH: map00030  Pentose phosphate pathway
ORTHOLOGY   KO: K00852  ribokinase
GENES       HSA: 64080(RBKS)
            MMU: 71336(Rbks)
            RNO: 362706(Rbks_predicted)
            CFA: 475710(RBKS)
            GGA: 421418(RBKS)
            XTR: 496800(LOC496800)
            DRE: 415207(zgc:86813)
            SPU: 761807(LOC761807)
            DME: Dmel_CG13369
            CEL: F07A11.5(ribokinase)
            ATH: AT1G17160
            OSA: 4326855
            CME: CMI123C
            SCE: YCR036W(RBK1)
            AGO: AGOS_AFR626W
            PIC: PICST_75489(RBK1)
            CGR: CAGL0L08228g
            SPO: SPBC16G5.02c
            ANI: AN7995.2
            AFM: AFUA_4G14650 AFUA_5G02530
            AOR: AO090038000092 AO090102000368
            UMA: UM04561.1
            DDI: DDB_0231353(rbsK)
            TET: TTHERM_00312950
            TBR: Tb11.03.0090
            TCR: 506925.480
            LMA: LmjF27.0420
            EHI: 20.t00015
            ECO: b3752(rbsK)
            ECJ: JW3731(rbsK)
            ECE: Z5253(rbsK)
            ECS: ECs4694
            ECC: c0331 c4680(rbsK)
            ECI: UTI89_C2435(yeiI) UTI89_C4307(rbsK)
            ECP: ECP_2983 ECP_3952
            ECV: APECO1_2711(rbsK)
            ECW: EcE24377A_4268(rbsK)
            ECX: EcHS_A3968(rbsK)
            STY: STY3892(rbsK) STY3989
            STT: t3634(rbsK) t3725
            SPT: SPA3643 SPA3724(rbsK)
            SEC: SC3713(rbsK) SC3798(rbsK)
            STM: STM3793 STM3885(rbsK)
            YPE: YPO0008(rbsK) YPO3621
            YPK: y0008(rbsK) y0248
            YPM: YP_0008(rbsK1) YP_3926(rbsK5)
            YPA: YPA_0011 YPA_3634
            YPN: YPN_0008 YPN_3549
            YPS: YPTB0008 YPTB3608
            YPI: YpsIP31758_0008(rbsK)
            YEN: YE0012(rbsK)
            SFL: SF3835(rbsK)
            SFX: S3932(rbsK)
            SFV: SFV_3747(rbsK)
            SSN: SSON_3922(rbsK)
            SBO: SBO_3766(rbsK)
            SDY: SDY_3995(rbsK)
            ECA: ECA0014(rbsK)
            PLU: plu0059(rbsK)
            ENT: Ent638_4112
            KPN: KPN_04157(rbsK)
            HIN: HI0505(rbsK)
            HIT: NTHI0633(rbsK)
            HIP: CGSHiEE_00465
            HIQ: CGSHiGG_05790
            HSO: HS_0225(rbsK) HS_0749(rbsK)
            PMU: PM0152(rbsK)
            MSU: MS0283(rbsK)
            APL: APL_1673(rbsK)
            XFA: XF0366
            XFT: PD1698(rbsK)
            XCC: XCC0764(rbsK)
            XCB: XC_3468
            XCV: XCV0870(rbsK)
            XAC: XAC0818(rbsK)
            XOO: XOO3785(rbsK)
            XOM: XOO_3565(XOO3565)
            VCH: VCA0131
            VCO: VC0395_0007(rbsK)
            VVU: VV2_0065
            VVY: VV0528 VVA0572
            VPA: VPA1083
            VFI: VF1448
            PPR: PBPRB1560
            PAE: PA1950(rbsK)
            PAU: PA14_39280(rbsK)
            PAP: PSPA7_3342(rbsK)
            PPU: PP_2458(rbsK)
            PST: PSPTO_2371(rbsK)
            PSB: Psyr_2155(pfkB) Psyr_4487(pfkB)
            PSP: PSPPH_2129(rbsK)
            PFL: PFL_2105(rbsK)
            PFO: Pfl_1923
            PEN: PSEEN1956
            PAR: Psyc_1910(pfkB)
            ACI: ACIAD2392(rbsK)
            SON: SO_0810(rbsK)
            SDN: Sden_0939
            SBL: Sbal_0659
            SLO: Shew_0696
            SPC: Sputcn32_3179
            SHE: Shewmr4_3307
            SHM: Shewmr7_0646
            SHN: Shewana3_3477
            SHW: Sputw3181_0764
            PAT: Patl_3505
            PIN: Ping_0344
            FTN: FTN_1767(rbsK)
            HCH: HCH_02313
            AHA: AHA_2313(rbsK)
            ASA: ASA_1967(rbsK)
            CVI: CV_3020(rbsK) CV_4278
            RSO: RSc1013(RS04269)
            BXE: Bxe_B0576 Bxe_B1401 Bxe_C1272 Bxe_C1282
            BUR: Bcep18194_A4749 Bcep18194_C6906 Bcep18194_C7623
            BCN: Bcen_1130 Bcen_1539 Bcen_5761
            BCH: Bcen2424_1610 Bcen2424_6126 Bcen2424_6290
            BAM: Bamb_1343 Bamb_1507
            BPS: BPSL1830 BPSS0853
            BPM: BURPS1710b_2023(rbsK) BURPS1710b_A2451(rbsK)
            BPL: BURPS1106A_1871(rbsK) BURPS1106A_A1183(rbsK)
            BPD: BURPS668_1858(rbsK) BURPS668_A1257(rbsK)
            BTE: BTH_I2471(rbsK) BTH_II1554
            AAV: Aave_4200
            DPS: DP1974
            ADE: Adeh_0498
            SAT: SYN_02874
            MLO: mll7662 mlr3185 mlr8492
            MES: Meso_3570
            SME: SMc01103(rbsK)
            ATU: Atu0364(rbsK) Atu3068 Atu4847(rbsk)
            ATC: AGR_C_637(rbsK) AGR_L_78 AGR_L_858GM
            RET: RHE_CH00409(rbsK) RHE_PC00098(ypc00049)
            RLE: RL0427(rbsK) RL2638(rbsK) RL2747(rbsK) pRL120009(rbsK)
                 pRL90218
            BME: BMEII0089
            BMF: BAB2_0004
            BMS: BRA0005
            BMB: BruAb2_0005
            BJA: bll2832(rbsK) blr1892(rbsK)
            BRA: BRADO2492
            BBT: BBta_2837 BBta_7825
            CCR: CC_0950
            SIL: SPO0013(rbsK)
            SIT: TM1040_2878
            RSP: RSP_1216(rbsK) RSP_3692 RSP_3738
            JAN: Jann_2121
            RDE: RD1_0420(rbsK) RD1_2419(rbsK) RD1_3737(rbsK) RD1_3764(rbsK)
            PDE: Pden_2308
            HNE: HNE_0207(rbsK)
            GOX: GOX2084
            GBE: GbCGDNIH1_1810
            RRU: Rru_A2297
            BSU: BG10877(rbsK)
            BHA: BH3728(rbsK)
            BAN: BA0665(rbsK)
            BAR: GBAA0665(rbsK)
            BAA: BA_1253(pfkB)
            BAT: BAS0632
            BCE: BC0660
            BCA: BCE_0733(rbsK)
            BCZ: BCZK0575(rbsK)
            BTK: BT9727_0576(rbsK)
            BTL: BALH_0607(rbsK)
            BLI: BL02439(rbsK)
            BLD: BLi03841(rbsK)
            BCL: ABC3548(rbsK) ABC3603 ABC3643
            BAY: RBAM_033090(rbsK)
            BPU: BPUM_3264(rbsK)
            OIH: OB2576(rbsK)
            GKA: GK3230
            SAU: SA0258(rbsK)
            SAV: SAV0268(rbsK)
            SAM: MW0244(rbsK)
            SAR: SAR0266
            SAS: SAS0245
            SAC: SACOL0253(rbsK)
            SAB: SAB0208c
            SAA: SAUSA300_0262(rbsK)
            SAO: SAOUHSC_00239
            SAJ: SaurJH9_0253
            SEP: SE2086
            SER: SERP2100(rbsK)
            SHA: SH0175(rbsK)
            SSP: SSP0744
            LLA: L86157(rbsK)
            LLC: LACR_1802
            LLM: llmg_0785(rbsK)
            SPD: SPD_1995(fucK)
            SAG: SAG0118(rbsK)
            SAN: gbs0117
            SAK: SAK_0170(rbsK)
            LPL: lp_0500(rbsK1) lp_2251(rbsK2) lp_3660(rbsK3)
            LJO: LJ0797
            LAC: LBA0587(rbsK) LBA1485(rbsK)
            LSA: LSA0202(rbsK)
            LSL: LSL_0423(rbsK)
            LDB: Ldb0529(rbsK)
            LBU: LBUL_0470
            LBR: LVIS_1421
            LCA: LSEI_0312
            LGA: LGAS_0556
            LRE: Lreu_1285
            PPE: PEPE_1239
            EFA: EF1922 EF2961(rbsK)
            OOE: OEOE_1612
            LME: LEUM_0691
            STH: STH771
            CPE: CPE1632(rbsK)
            CPF: CPF_1884(rbsK)
            CPR: CPR_1603(rbsK)
            CTC: CTC00909 CTC02352
            CNO: NT01CX_0166(rbsK)
            CDF: CD0299(rbsK)
            CBA: CLB_1584(rbsK)
            CBH: CLC_1595(rbsK)
            CBF: CLI_1646(rbsK)
            TTE: TTE0202(rbsK)
            MFL: Mfl642
            MTU: Rv2436(rbsK)
            MTC: MT2511(rbsK)
            MBO: Mb2462(rbsK)
            MBB: BCG_2455(rbsK)
            MPA: MAP2251(rbsK)
            MSM: MSMEG_4585(rbsK)
            MVA: Mvan_3935
            MGI: Mflv_2643
            MMC: Mmcs_3539
            CGL: NCgl1311(cgl1366) NCgl2243(cgl2325)
            CGB: cg1546(rbsK1) cg2554(rbsK2)
            CEF: CE1484
            CDI: DIP0655
            CJK: jk2077(rbsK)
            NFA: nfa13700
            RHA: RHA1_ro01303(rbsK)
            SCO: SCO2748(SCC57A.19)
            SMA: SAV5317(rbsK)
            LXX: Lxx17050(rbsK)
            AAU: AAur_1121(rbsK) AAur_3648(rbsK)
            PAC: PPA0018 PPA1211
            TFU: Tfu_0259
            FAL: FRAAL0770 FRAAL3962(rbsK)
            ACE: Acel_0624
            SEN: SACE_1230 SACE_1271(rbsK) SACE_3234(rbsK)
            BLO: BL1431 BL1772(rbsK)
            BAD: BAD_1485(rbsK)
            RBA: RB3499(rbsK)
            LIL: LA1392(pfkB)
            SYW: SYNW1551
            SYD: Syncc9605_1746
            SYE: Syncc9902_1813
            SYR: SynRCC307_1169(rbsK)
            SYX: SynWH7803_0794(rbsK)
            CYA: CYA_2257(rbsK)
            CYB: CYB_1353(rbsK)
            GVI: gll2315
            ANA: all1784
            AVA: Ava_0252
            PMA: Pro1157(rbsK)
            PMM: PMM1044(rbsK)
            PMT: PMT0910
            PMN: PMN2A_0709
            PMI: PMT9312_1055
            PMB: A9601_11491
            PMC: P9515_11351
            PMF: P9303_12381
            PMG: P9301_11501
            PME: NATL1_15431
            TER: Tery_0865
            BTH: BT_2803 BT_2804
            DET: DET0711
            DEH: cbdb_A667
            DRA: DR_1525 DR_A0055
            DGE: Dgeo_1072 Dgeo_1142
            TTH: TTC0063
            TTJ: TTHA0431
            TMA: TM0960
            MMP: MMP0418
            MAC: MA1373
            MBA: Mbar_A2903
            MMA: MM_2358
            MBU: Mbur_0967
            MHU: Mhun_0077
            MST: Msp_0071 Msp_0252
            MSI: Msm_0307 Msm_1389
            MKA: MK0817
            AFU: AF0356 AF0401
            HAL: VNG1851G(suk)
            HWA: HQ1474A(rbsK)
            NPH: NP3184A(suk)
            TAC: Ta0880
            TVO: TVN0979
            PAB: PAB0280(rbsK)
            PFU: PF1886
            TKO: TK2029
            RCI: RCIX2237(pfkB-1) RCIX2669(pfkB-2) RRC45(pfkB-3)
            APE: APE_0012 APE_2106.1
            SSO: SSO0004(rbsK-1) SSO2449(rbsK-2)
            STO: ST0574 ST2328
            SAI: Saci_0272(rbsK) Saci_0553
            PAI: PAE0835
STRUCTURES  PDB: 1GQT  1RK2  1RKA  1RKD  1RKS  1VM7  2FV7  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.15
            ExPASy - ENZYME nomenclature database: 2.7.1.15
            ExplorEnz - The Enzyme Database: 2.7.1.15
            ERGO genome analysis and discovery system: 2.7.1.15
            BRENDA, the Enzyme Database: 2.7.1.15
            CAS: 9026-84-0
///
ENTRY       EC 2.7.1.16                 Enzyme
NAME        ribulokinase;
            ribulokinase (phosphorylating);
            L-ribulokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:L(or D)-ribulose 5-phosphotransferase
REACTION    ATP + L(or D)-ribulose = ADP + L(or D)-ribulose 5-phosphate
            [RN:R01526 R02439]
ALL_REAC    R01526 R02439
SUBSTRATE   ATP [CPD:C00002];
            L-ribulose [CPD:C00508];
            D-ribulose [CPD:C00309]
PRODUCT     ADP [CPD:C00008];
            L-ribulose 5-phosphate [CPD:C01101];
            D-ribulose 5-phosphate [CPD:C00199]
COMMENT     Ribitol and L-arabinitol can also act as acceptors.
REFERENCE   1  [PMID:13539035]
  AUTHORS   BURMA DP, HORECKER BL.
  TITLE     Pentose fermentation by Lactobacillus plantarum. III. Ribulokinase.
  JOURNAL   J. Biol. Chem. 231 (1958) 1039-51.
  ORGANISM  Lactobacillus plantarum [GN:lpl]
REFERENCE   2  [PMID:5336963]
  AUTHORS   Lee N, Bendet I.
  TITLE     Crystalline L-ribulokinase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 242 (1967) 2043-50.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Simpson, F.J., Wolin, M.J. and Wood, W.A.
  TITLE     Degradation of L-arabinose by Aerobacter aerogenes. I. A pathway
            involving phosphorylated intermediates.
  JOURNAL   J. Biol. Chem. 230 (1958) 457-472.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K00853  L-ribulokinase
GENES       TCR: 508625.150 509757.49 509759.10
            LMA: LmjF36.0060
            ECO: b0063(araB)
            ECJ: JW0062(araB)
            ECE: Z0072(araB)
            ECS: ECs0067
            ECC: c0075(araB)
            ECI: UTI89_C0068(araB)
            ECP: ECP_0064
            ECV: APECO1_1921(araB)
            ECW: EcE24377A_0065(araB)
            ECX: EcHS_A0067
            STY: STY0120(araB)
            STT: t0107(araB)
            SPT: SPA0105(araB)
            STM: STM0103(araB)
            YPE: YPO2254(araB)
            YPK: y2095(araB)
            YPM: YP_2050(araB1)
            YPA: YPA_1614
            YPN: YPN_1723
            YPS: YPTB2173(araB)
            YPI: YpsIP31758_1886(araB)
            SFL: SF0058(araB)
            SFX: S0060(araB)
            SFV: SFV_0055(araB)
            SSN: SSON_0069(araB)
            SBO: SBO_0050(araB)
            SDY: SDY_0090(araB)
            ECA: ECA2274(araB)
            VPA: VPA1674
            SHE: Shewmr4_1977
            SHM: Shewmr7_1997
            SHN: Shewana3_2064
            SDE: Sde_0772
            AHA: AHA_1902(araB)
            RET: RHE_CH02747(rtlK) RHE_CH03676(ypch01311)
            RLE: RL4212(araB)
            BRA: BRADO6615
            BBT: BBta_0920
            RRU: Rru_A1346
            ABA: Acid345_0322
            BSU: BG11905(araB)
            BHA: BH1872(araB)
            BLI: BL00351(araB)
            BLD: BLi03027(araB)
            BCL: ABC0407(araB)
            BAY: RBAM_025850
            GKA: GK1905(araB)
            SAU: SA0510(araB)
            SAV: SAV0552(araB)
            SAM: MW0507(araB)
            SAR: SAR0557
            SAS: SAS0510
            SAC: SACOL0598
            SAB: SAB0503
            SAA: SAUSA300_0537
            SAO: SAOUHSC_00534
            SEP: SE1914
            SER: SERP1927
            SSP: SSP0563 SSP2178
            LPL: lp_3556(araB)
            LSA: LSA1859(araB)
            LBR: LVIS_1742
            MSM: MSMEG_1713(araB)
            CMI: CMM_0876(araB)
            AAU: AAur_3709(araB)
            PAC: PPA2319
            ACE: Acel_0871
            RBA: RB8788(araB)
            GFO: GFO_0697(araB)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.16
            ExPASy - ENZYME nomenclature database: 2.7.1.16
            ExplorEnz - The Enzyme Database: 2.7.1.16
            ERGO genome analysis and discovery system: 2.7.1.16
            BRENDA, the Enzyme Database: 2.7.1.16
            CAS: 9030-57-3
///
ENTRY       EC 2.7.1.17                 Enzyme
NAME        xylulokinase;
            xylulokinase (phosphorylating);
            D-xylulokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-xylulose 5-phosphotransferase
REACTION    ATP + D-xylulose = ADP + D-xylulose 5-phosphate [RN:R01639]
ALL_REAC    R01639
SUBSTRATE   ATP [CPD:C00002];
            D-xylulose [CPD:C00310]
PRODUCT     ADP [CPD:C00008];
            D-xylulose 5-phosphate [CPD:C00231]
REFERENCE   1
  AUTHORS   Hickman, J. and Ashwell, G.
  TITLE     Purification and properties of D-xylulokinase in liver.
  JOURNAL   J. Biol. Chem. 232 (1958) 737-748.
  ORGANISM  human [GN:hsa]
REFERENCE   2
  AUTHORS   Simpson, F.J.
  TITLE     D-Xylulokinase.
  JOURNAL   Methods Enzymol. 9 (1966) 454-458.
  ORGANISM  cow [GN:bta], Aerobacter aerogenes, Lactobacillus pentosus
REFERENCE   3
  AUTHORS   Slein, M.W.
  TITLE     Xylose isomerase from Pasteurella pestis, strain A-1122.
  JOURNAL   J. Am. Chem. Soc. 77 (1955) 1663-1667.
  ORGANISM  Pasteurella pestis
REFERENCE   4
  AUTHORS   Stumpf, P.K. and Horecker, B.L.
  TITLE     The roole of xylulose 5-phosphate in xylose metabolism of
            Lactobacillus pentosus.
  JOURNAL   J. Biol. Chem. 218 (1956) 753-768.
  ORGANISM  Lactobacillus pentosus
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K00854  xylulokinase
GENES       GGA: 420432(XYLB)
            SCE: YGR194C(XKS1)
            AGO: AGOS_AGR324C
            PIC: PICST_68734(XKS1)
            CAL: CaO19.1290(xks2)
            CGR: CAGL0G09339g
            SPO: SPCPJ732.02c
            ANI: AN8790.2
            AFM: AFUA_5G09840
            AOR: AO090020000603
            CNE: CNH03870
            UMA: UM01921.1
            LMA: LmjF36.0260
            EHI: 16.t00018
            ECO: b3564(xylB)
            ECJ: JW3536(xylB)
            ECE: Z4989(xylB)
            ECS: ECs4447
            ECC: c4384(xylB)
            ECI: UTI89_C4105(xylB)
            ECP: ECP_3667
            ECV: APECO1_2885(xylB)
            ECW: EcE24377A_4060(xylB)
            ECX: EcHS_A3767(xylB)
            STY: STY4138(xylB)
            STT: t3859(xylB)
            SPT: SPA3511(xylB)
            SEC: SC3595(xylB)
            STM: STM3660(xylB)
            YPE: YPO1291 YPO4039(xylB)
            YPK: y2893 y4058(xylB)
            YPM: YP_1300(xylB1) YP_3401(xylB2)
            YPA: YPA_1009 YPA_4129
            YPN: YPN_2687 YPN_3686
            YPS: YPTB1323 YPTB3892(xylB)
            YPI: YpsIP31758_4103(xylB)
            SFL: SF3608(xylB)
            SFX: S4161(xylB)
            SFV: SFV_3976(xylB)
            SSN: SSON_3821(xylB)
            SBO: SBO_3572(xylB)
            ECA: ECA0096(xylB)
            PLU: plu1959(xylB)
            SGL: SG0611
            HIN: HI1113
            HIT: NTHI1277(xylB)
            HSO: HS_0588(xylB)
            PMU: PM1371
            MSU: MS2372(xylB)
            APL: APL_1907(xylB)
            XCC: XCC1757
            XCB: XC_2478
            XCV: XCV1807 XCV4350(xylB4)
            XAC: XAC1775 XAC4244(xylB)
            XOO: XOO2911
            XOM: XOO_2762(XOO2762)
            PPR: PBPRA0467
            PAE: PA2343(mtlY)
            PAU: PA14_34350(mtlY)
            PAP: PSPA7_2920(xylB)
            PST: PSPTO_2702(xylB)
            PSB: Psyr_2435
            PSP: PSPPH_2593(uxuB) PSPPH_2736
            PFL: PFL_3075(xylB)
            PFO: Pfl_2635
            PEN: PSEEN1988(mtlY)
            PAT: Patl_3725
            CBU: CBU_0346(xylB)
            CBD: COXBU7E912_1732(xylB)
            TCX: Tcr_1241
            NOC: Noc_1697
            HCH: HCH_03095(xylB)
            CSA: Csal_0644
            CVI: CV_1862(xylB)
            RSO: RSc2128(dalK)
            BMA: BMA0343(xylB-1) BMAA1079(xylB-2)
            BMV: BMASAVP1_0071(xylB-2) BMASAVP1_A0642(xylB-1)
            BML: BMA10299_0348(xylB-2) BMA10299_A2477(xylB-1)
            BMN: BMA10247_0090(xylB-1) BMA10247_A1238(xylB-2)
            BXE: Bxe_A0232 Bxe_A0729
            BUR: Bcep18194_A5917 Bcep18194_A5936 Bcep18194_B0888
                 Bcep18194_B3071
            BCN: Bcen_1976 Bcen_3551 Bcen_5066 Bcen_6505
            BCH: Bcen2424_2586 Bcen2424_2605 Bcen2424_4816 Bcen2424_5794
                 Bcen2424_6739
            BAM: Bamb_2634 Bamb_2652 Bamb_4197
            BPS: BPSL0839(dalK) BPSS1238 BPSS2026
            BPM: BURPS1710b_1022 BURPS1710b_1046(xylB) BURPS1710b_A0237(xylB)
                 BURPS1710b_A1144
            BPL: BURPS1106A_0887(xylB) BURPS1106A_A1656(xylB)
            BPD: BURPS668_0884(xylB) BURPS668_A1745(xylB)
            BTE: BTH_I0684 BTH_I0702(xylB-1) BTH_II0307 BTH_II1173(xylB-2)
            MXA: MXAN_2879
            MLO: mlr5033
            MES: Meso_2819
            SME: SMc03164(xylB)
            ATU: Atu4482(xylB)
            ATC: AGR_L_776
            RET: RHE_CH03649(xylBch) RHE_PA00020(xylBa)
            RLE: RL4177(xylB)
            BME: BMEI1386
            BMF: BAB1_0571(xylB)
            BMS: BR0548(xylB)
            BMB: BruAb1_0570(xylB)
            BOV: BOV_0550(xylB)
            BJA: bll5785 blr1119(xylB)
            BRA: BRADO1395(xylB) BRADO2359(xylB)
            BBT: BBta_2713(xylB) BBta_6709(xylB)
            SIL: SPO0855(xylB)
            SIT: TM1040_0028
            RSP: RSP_1177(xylB)
            JAN: Jann_3259
            RDE: RD1_3617(xylB) RD1_3629(xylB) RD1_3704(xylB) RD1_3760(xylB)
            NAR: Saro_0756
            RRU: Rru_A0250 Rru_A1267
            ABA: Acid345_0904
            BSU: BG10807(xylB)
            BHA: BH2756(xylB)
            BCA: BCE_2211(xylB)
            BLI: BL03869(xylB)
            BLD: BLi04047(xylB)
            BCL: ABC0573(xylB)
            BAY: RBAM_017360(xylB)
            BPU: BPUM_1828(xylB) BPUM_2329
            OIH: OB3118
            GKA: GK1874
            SEP: SE2085
            SHA: SH0536(xylB)
            SSP: SSP0365 SSPP137
            LWE: lwe0244(xylB)
            LLA: L0231(xylB)
            LBR: LVIS_0184
            EFA: EF0557(xylB)
            STH: STH1273
            CAC: CAC2612(xylB)
            CDF: CD3065(xylB)
            MTA: Moth_2025
            MTU: Rv0729(xylB)
            MTC: MT0754
            MBO: Mb0750(xylB)
            MBB: BCG_0779(xylB)
            MPA: MAP4195(xylB)
            MSM: MSMEG_3113 MSMEG_3257(xylB) MSMEG_3263
            MMC: Mmcs_2519 Mmcs_2529
            CGL: NCgl0111(cgl0112)
            CGB: cg0147(xylB)
            CDI: DIP1746
            RHA: RHA1_ro02812 RHA1_ro02901
            SCO: SCO1170(2SCG11.04) SCO2462(SC7A8.01)
            SMA: SAV1126(xylB2) SAV5682 SAV5683(xylB3) SAV7181(xylB1)
            LXX: Lxx03360(xylB)
            CMI: CMM_1299
            AAU: AAur_3707(xylB)
            TFU: Tfu_1575 Tfu_1604
            SEN: SACE_0929(xylB) SACE_6529
            BLO: BL1293 BL1709(xylB)
            BAD: BAD_0432(xylB)
            RXY: Rxyl_0402 Rxyl_0833
            RBA: RB12012(xylB)
            SYX: SynWH7803_0166(xylB)
            AVA: Ava_2006
            PMF: P9303_22191(xylB)
            BTH: BT_0792 BT_4423
            BFR: BF2261
            BFS: BF2355
            SRU: SRU_0981
            DGE: Dgeo_2691 Dgeo_2863
            TMA: TM0116 TM0284
            AFU: AF1324
            APE: APE_0017.1
            SAI: Saci_1058
STRUCTURES  PDB: 2ITM  2NLX  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.17
            ExPASy - ENZYME nomenclature database: 2.7.1.17
            ExplorEnz - The Enzyme Database: 2.7.1.17
            ERGO genome analysis and discovery system: 2.7.1.17
            BRENDA, the Enzyme Database: 2.7.1.17
            CAS: 9030-58-4
///
ENTRY       EC 2.7.1.18                 Enzyme
NAME        phosphoribokinase;
            phosphoribokinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-ribose-5-phosphate 1-phosphotransferase
REACTION    ATP + D-ribose 5-phosphate = ADP + D-ribose 1,5-bisphosphate
            [RN:R01050]
ALL_REAC    R01050
SUBSTRATE   ATP [CPD:C00002];
            D-ribose 5-phosphate [CPD:C00117]
PRODUCT     ADP [CPD:C00008];
            D-ribose 1,5-bisphosphate [CPD:C01151]
REFERENCE   1
  AUTHORS   Krebs, E.G.
  TITLE     Phosphorylase b kinase from rabbit muscle.
  JOURNAL   Methods Enzymol. 8 (1966) 543-546.
  ORGANISM  rabbit
REFERENCE   2
  AUTHORS   Scarano, E.
  TITLE     Quoted by H.M. Kalckar The role of phosphoglycosyl compounds in the
            biosynthesis of nucleosides and nucleotides.
  JOURNAL   Biochim. Biophys. Acta 12 (1953) 250-264.
  ORGANISM  pigeon
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.18
            ExPASy - ENZYME nomenclature database: 2.7.1.18
            ExplorEnz - The Enzyme Database: 2.7.1.18
            ERGO genome analysis and discovery system: 2.7.1.18
            BRENDA, the Enzyme Database: 2.7.1.18
            CAS: 9030-59-5
///
ENTRY       EC 2.7.1.19                 Enzyme
NAME        phosphoribulokinase;
            phosphopentokinase;
            ribulose-5-phosphate kinase;
            phosphopentokinase;
            phosphoribulokinase (phosphorylating);
            5-phosphoribulose kinase;
            ribulose phosphate kinase;
            PKK;
            PRuK;
            PRK
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-ribulose-5-phosphate 1-phosphotransferase
REACTION    ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate
            [RN:R01523]
ALL_REAC    R01523
SUBSTRATE   ATP [CPD:C00002];
            D-ribulose 5-phosphate [CPD:C00199]
PRODUCT     ADP [CPD:C00008];
            D-ribulose 1,5-bisphosphate [CPD:C01182]
REFERENCE   1  [PMID:13295229]
  AUTHORS   HURWITZ J, WEISSBACH A, HORECKER BL, SMYRNIOTIS PZ.
  TITLE     Spinach phosphoribulokinase.
  JOURNAL   J. Biol. Chem. 218 (1956) 769-83.
  ORGANISM  spinach
REFERENCE   2  [PMID:13295232]
  AUTHORS   JAKOBY WB, BRUMMOND DO, OCHOA S.
  TITLE     Formation of 3-phosphoglyceric acid by carbon dioxide fixation with
            spinach leaf enzymes.
  JOURNAL   J. Biol. Chem. 218 (1956) 811-22.
  ORGANISM  spinach
PATHWAY     PATH: map00710  Carbon fixation
ORTHOLOGY   KO: K00855  phosphoribulokinase
GENES       ATH: AT1G32060(PRK)
            OSA: 4330413
            CME: CMF117C
            ECO: b3355(prkB)
            ECJ: JW3318(prkB)
            ECE: Z4716(prkB)
            ECS: ECs4206
            ECC: c4130(prkB)
            ECI: UTI89_C3858(prkB)
            ECP: ECP_3446
            ECV: APECO1_3100(prkB)
            STY: STY4333(prkB)
            STT: t4041(prkB)
            SPT: SPA3330(prkB)
            SEC: SC3398(prkB)
            STM: STM3464(prkB)
            YPE: YPO0178(prk)
            YPK: y3959(prkB)
            YPM: YP_0177(prk)
            YPA: YPA_3294
            YPN: YPN_3889
            YPP: YPDSF_0103
            YPS: YPTB3726(prk)
            SFL: SF3374(prkB)
            SFX: S4389(prkB)
            SFV: SFV_3361(prkB)
            SSN: SSON_3486(prkB)
            SBO: SBO_3335(prkB)
            ECA: ECA4062(prkB)
            PLU: plu0397(prkB)
            SGL: SG2299
            ENT: Ent638_3782
            SPE: Spro_4578
            VCH: VC2613
            VCO: VC0395_A2190(prkB)
            VVU: VV1_1319
            VVY: VV3049
            VPA: VP2792
            VFI: VF0213 VF0214
            PPR: PBPRA0295
            SON: SO_0878(prkB)
            SDN: Sden_3188
            SFR: Sfri_3290
            SAZ: Sama_3002
            SBL: Sbal_3486
            SBM: Shew185_0853
            SLO: Shew_0587
            SPC: Sputcn32_3124
            SSE: Ssed_3867
            SPL: Spea_3507
            SHE: Shewmr4_0734
            SHM: Shewmr7_3288
            SHN: Shewana3_3400
            SHW: Sputw3181_0819
            ILO: IL2312(prkB)
            CPS: CPS_0628(prkB)
            PHA: PSHAa2495(prkB)
            PAT: Patl_0224
            MAQ: Maqu_3554
            MCA: MCA3051(cbbP)
            TCX: Tcr_0013
            NOC: Noc_2826
            AEH: Mlg_2833
            HHA: Hhal_1049
            HCH: HCH_06138
            CSA: Csal_0910
            AHA: AHA_0985
            RMA: Rmag_0004
            VOK: COSY_0004(prkB)
            REH: H16_B1389(cbbP2)
            RME: Rmet_1512
            BXE: Bxe_B2449
            RFR: Rfer_1392
            PNA: Pnap_1983
            MPT: Mpe_A1482(cbbP) Mpe_A2789(cbbP)
            NEU: NE1474(cbbP)
            NET: Neut_0772
            NMU: Nmul_A0562
            EBA: ebA1099(prk)
            AZO: azo2835(prkB)
            DAR: Daro_3627
            TBD: Tbd_2447(cbbP)
            SME: SMb20201(cbbP)
            SMD: Smed_3921
            BJA: blr2582(cbbP)
            BRA: BRADO1656(cbbP)
            BBT: BBta_0446(cbbP) BBta_6400(cbbP)
            RPA: RPA4644(cbbP)
            RPB: RPB_0948
            RPC: RPC_2898
            RPD: RPD_1051
            RPE: RPE_2683
            NWI: Nwi_2693
            NHA: Nham_3753
            XAU: Xaut_1914
            RSP: RSP_1284(prkA) RSP_3267(prkB)
            RSH: Rsph17029_2943 Rsph17029_4000
            RSQ: Rsph17025_2714
            PDE: Pden_1696
            GBE: GbCGDNIH1_2139
            ACR: Acry_0822
            RRU: Rru_A2404
            MAG: amb2695
            SYN: sll1525(prk)
            SYW: SYNW0785(prk)
            SYC: syc0567_d(prk)
            SYF: Synpcc7942_0977
            SYD: Syncc9605_1864
            SYE: Syncc9902_0789
            SYG: sync_1711
            SYR: SynRCC307_0996(prk)
            SYX: SynWH7803_1151(prk)
            CYA: CYA_1258(prk)
            CYB: CYB_0441 CYB_2883(prk)
            TEL: tll1914(prk)
            GVI: gll2122(prk) glr2296(prk) glr4424(prk)
            ANA: alr2350 alr4123(prk)
            AVA: Ava_0169 Ava_0781
            PMA: Pro0861(prk)
            PMM: PMM0785(prk)
            PMT: PMT0532(prk)
            PMN: PMN2A_0193
            PMI: PMT9312_0793
            PMB: A9601_08491(prkB) A9601_16771(gidB)
            PMC: P9515_07961(prkB) P9515_16551(gidB)
            PMF: P9303_04501(gidB) P9303_17331(prkB)
            PMG: P9301_08461(prkB) P9301_16651(gidB)
            PMH: P9215_08801
            PME: NATL1_08251(prkB) NATL1_18741(gidB)
            TER: Tery_1845 Tery_3654
            MHU: Mhun_0794
STRUCTURES  PDB: 1A7J  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.19
            ExPASy - ENZYME nomenclature database: 2.7.1.19
            ExplorEnz - The Enzyme Database: 2.7.1.19
            ERGO genome analysis and discovery system: 2.7.1.19
            BRENDA, the Enzyme Database: 2.7.1.19
            CAS: 9030-60-8
///
ENTRY       EC 2.7.1.20                 Enzyme
NAME        adenosine kinase;
            adenosine kinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:adenosine 5'-phosphotransferase
REACTION    ATP + adenosine = ADP + AMP [RN:R00185]
ALL_REAC    R00185
SUBSTRATE   ATP [CPD:C00002];
            adenosine [CPD:C00212]
PRODUCT     ADP [CPD:C00008];
            AMP [CPD:C00020]
COMMENT     2-Aminoadenosine can also act as acceptor.
REFERENCE   1  [PMID:4290214]
  AUTHORS   Lindberg B, Klenow H, Hansen K.
  TITLE     Some properties of partially purified mammalian adenosine kinase.
  JOURNAL   J. Biol. Chem. 242 (1967) 350-6.
  ORGANISM  rabbit
REFERENCE   2  [PMID:14832298]
  AUTHORS   CAPUTTO R.
  TITLE     The enzymatic synthesis of adenylic acid; adenosinekinase.
  JOURNAL   J. Biol. Chem. 189 (1951) 801-14.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Kornberg, A. and Pricer, W.E.
  TITLE     Enzymatic phosphorylation of adenosine and 2,6-diaminopurine
            riboside.
  JOURNAL   J. Biol. Chem. 193 (1951) 481-495.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K00856  adenosine kinase
GENES       HSA: 132(ADK)
            MMU: 11534(Adk)
            RNO: 25368(Adk)
            GGA: 423735(ADK)
            XLA: 444786(MGC82032)
            XTR: 549452(adk)
            DRE: 368220(adka)
            SPU: 580959(LOC580959)
            DME: Dmel_CG11255 Dmel_CG1851
            CEL: R07H5.8
            ATH: AT3G09820(ADK1) AT5G03300(ADK2)
            OSA: 4330032 4336412
            CME: CMK016C
            SCE: YJR105W(ADO1)
            AGO: AGOS_ABR161C
            PIC: PICST_57331(ADO1)
            CGR: CAGL0C04983g
            SPO: SPCC338.14
            ANI: AN2272.2
            AFM: AFUA_5G06390
            AOR: AO090009000617
            CNE: CNN02130
            UMA: UM00797.1
            CPV: cgd8_2370
            TBR: Tb927.6.2300 Tb927.6.2360
            TCR: 509051.40 509965.370
            LMA: LmjF30.0880 LmjF30.0890
            NOC: Noc_2548
            BVI: Bcep1808_0575
            BUR: Bcep18194_A3683
            BCN: Bcen_0117
            BCH: Bcen2424_0600
            BAM: Bamb_0502
            HAR: HEAR2766(adoK)
            BRA: BRADO0031
            BBT: BBta_0036
            RDE: RD1_0962
            RRU: Rru_A0149
            MBB: BCG_2218c(adoK)
            MAV: MAV_2289
            MSM: MSMEG_4270
            MVA: Mvan_3566
            MGI: Mflv_2947
            MMC: Mmcs_3300
            MKM: Mkms_3362
            MJL: Mjls_3311
            RHA: RHA1_ro01139
            FRA: Francci3_3120
            FAL: FRAAL5126(adoK)
            ACE: Acel_0955
            SEN: SACE_1656(adoK) SACE_3899(adoK)
            CCH: Cag_1382
STRUCTURES  PDB: 1BX4  1DGM  1LII  1LIJ  1LIK  1LIO  2A9Y  2A9Z  2AA0  2AB8  
                 2ABS  2GL0  2PKF  2PKK  2PKM  2PKN  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.20
            ExPASy - ENZYME nomenclature database: 2.7.1.20
            ExplorEnz - The Enzyme Database: 2.7.1.20
            ERGO genome analysis and discovery system: 2.7.1.20
            BRENDA, the Enzyme Database: 2.7.1.20
            CAS: 9027-72-9
///
ENTRY       EC 2.7.1.21                 Enzyme
NAME        thymidine kinase;
            thymidine kinase (phosphorylating);
            2'-deoxythymidine kinase;
            deoxythymidine kinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:thymidine 5'-phosphotransferase
REACTION    ATP + thymidine = ADP + thymidine 5'-phosphate [RN:R01567]
ALL_REAC    R01567;
            (other) R02099
SUBSTRATE   ATP [CPD:C00002];
            thymidine [CPD:C00214]
PRODUCT     ADP [CPD:C00008];
            thymidine 5'-phosphate [CPD:C00364]
COMMENT     Deoxyuridine can also act as acceptor, and dGTP can act as a donor.
            The deoxypyrimidine kinase complex induced by Herpes simplex virus
            catalyses this reaction as well as those of EC 2.7.1.114
            (AMP---thymidine kinase), EC 2.7.1.118 (ADP---thymidine kinase) and
            EC 2.7.4.9 (dTMP-kinase).
REFERENCE   1  [PMID:6293576]
  AUTHORS   Falke D, Labenz J, Brauer D, Muller WE.
  TITLE     Adenosine diphosphate: thymidine 5'-phosphotransferase, a new enzyme
            activity, associated with the Herpes simplex virus-induced
            deoxypyrimidine kinase.
  JOURNAL   Biochim. Biophys. Acta. 708 (1982) 99-103.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:4407348]
  AUTHORS   Kizer DE, Holman L.
  TITLE     Purification and properties of thymidine kinase from regenerating
            rat liver.
  JOURNAL   Biochim. Biophys. Acta. 350 (1974) 193-200.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Okazaki, R. and Kornberg, A.
  TITLE     Deoxythymidine kinase of Escherichia coli. I. Purification and some
            properties of the enzyme.
  JOURNAL   J. Biol. Chem. 239 (1964) 269-274.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K00857  thymidine kinase
GENES       HSA: 7083(TK1) 7084(TK2)
            PTR: 454144(TK2)
            MMU: 21877(Tk1) 57813(Tk2)
            CFA: 483343(TK1) 611387(TK2)
            GGA: 395719(TK1) 427551(RCJMB04_31e21)
            XTR: 496942(LOC496942)
            DRE: 327590(tk1)
            SPU: 579588(LOC579588)
            CEL: Y43C5A.5(thk-1)
            ATH: AT3G07800 AT5G23070
            OSA: 4331376
            ECU: ECU01_0740i
            DDI: DDB_0191436(thyB)
            CPV: cgd5_4440
            CHO: Chro.50398
            TET: TTHERM_00487030
            TBR: Tb10.70.7270
            TCR: 506855.260 511133.20
            LMA: LmjF21.1210
            EHI: 20.t00034
            ECO: b1238(tdk)
            ECJ: JW1226(tdk)
            ECE: Z2015(tdk)
            ECS: ECs1740
            ECC: c1703(tdk)
            ECI: UTI89_C1436(tdk)
            ECP: ECP_1285
            ECV: APECO1_352(tdk)
            ECW: EcE24377A_1387(tdk)
            ECX: EcHS_A1347(tdk)
            STY: STY1301(tdk)
            STT: t1661(tdk)
            SPT: SPA1128(tdk)
            SEC: SC1745(tdk)
            STM: STM1750(tdk)
            YPE: YPO2176(tdk)
            YPK: y2145(tdk)
            YPM: YP_1975(tdk)
            YPA: YPA_1534
            YPN: YPN_1643
            YPP: YPDSF_0957
            YPS: YPTB2102(tdk)
            YPI: YpsIP31758_1964(tdk)
            SFL: SF1238(tdk)
            SFX: S1324(tdk)
            SFV: SFV_1251(tdk)
            SSN: SSON_1941(tdk)
            SBO: SBO_1831(tdk)
            SDY: SDY_1290(tdk)
            ECA: ECA2327(tdk)
            PLU: plu2497(tdk)
            SGL: SG1371
            ENT: Ent638_2305
            SPE: Spro_2705
            BFL: Bfl434(tdk)
            BPN: BPEN_447(tdk)
            HIN: HI0529(tdk)
            HIT: NTHI0655(tdk)
            HIP: CGSHiEE_00360
            HIQ: CGSHiGG_05895
            HDU: HD1473(tdk)
            HSO: HS_0410(tdk)
            PMU: PM1236(tdk)
            MSU: MS1764(tdk)
            APL: APL_0622(tdk)
            ASU: Asuc_2065
            XCC: XCC4143(tdk)
            XCB: XC_4235
            XCV: XCV4384(tdk)
            XAC: XAC4282(tdk)
            XOO: XOO0241(tdk)
            XOM: XOO_0220(XOO0220)
            VCH: VC1167
            VCO: VC0395_A0736(tdk)
            VVU: VV1_2907
            VVY: VV1363
            VPA: VP1151
            VFI: VF1599
            PPR: PBPRA1084
            SON: SO_3140
            SDN: Sden_2536
            SFR: Sfri_2745
            SAZ: Sama_1173
            SBL: Sbal_2842
            SBM: Shew185_2861
            SLO: Shew_2579
            SPC: Sputcn32_2506
            SSE: Ssed_1449
            SPL: Spea_2851
            SHE: Shewmr4_1357
            SHM: Shewmr7_1422
            SHN: Shewana3_1410
            SHW: Sputw3181_1502
            ILO: IL0361(tdk)
            CPS: CPS_1971(tdk)
            PHA: PSHAb0294(tdk)
            PAT: Patl_0626
            PIN: Ping_0685
            CBU: CBU_2069
            CBD: COXBU7E912_2162(tdk)
            LPN: lpg0636(tdk)
            LPF: lpl0673(tdk)
            LPP: lpp0690(tdk)
            FTU: FTT0621(tdk)
            FTF: FTF0621(tdk)
            FTW: FTW_1107(tdk)
            FTL: FTL_0890
            FTH: FTH_0875(tdk)
            FTA: FTA_0941(tdk)
            FTN: FTN_1060(tdk)
            MMW: Mmwyl1_2887
            AHA: AHA_1822(tdk)
            CVI: CV_2342(tdk)
            RFR: Rfer_4385
            CJD: JJD26997_0856(tdk)
            BBA: Bd3420
            MXA: MXAN_5072(tdk)
            MLO: mlr2747
            SME: SMc02736(tdk)
            ATU: Atu2282(tdk)
            ATC: AGR_C_4147(tdk)
            RET: RHE_CH03084(tdk)
            RLE: RL3532(tdk)
            SIL: SPO0914(tdk)
            SIT: TM1040_0626
            JAN: Jann_3324
            RDE: RD1_3494(tdk)
            PDE: Pden_1744
            MMR: Mmar10_2037
            HNE: HNE_3149(tdk)
            ZMO: ZMO0552(tdk)
            NAR: Saro_2487
            SAL: Sala_0538
            SWI: Swit_3814
            ELI: ELI_03490
            GOX: GOX0257
            SUS: Acid_3198
            BSU: BG10419(tdk)
            BHA: BH3779(tdk)
            BAN: BA5573(tdk)
            BAR: GBAA5573(tdk)
            BAA: BA_0429
            BAT: BAS5179
            BCE: BC5330
            BCA: BCE_5457(tdk)
            BCZ: BCZK5030(tdk)
            BCY: Bcer98_3851
            BTK: BT9727_5014(tdk)
            BTL: BALH_4829(tdk)
            BLI: BL03975(tdk)
            BLD: BLi03954(tdk)
            BCL: ABC3877(tdk)
            BAY: RBAM_034220(tdk)
            BPU: BPUM_3349(tdk)
            OIH: OB2999(tdk)
            GKA: GK3380
            SAU: SA1921(tdk)
            SAV: SAV2119(tdk)
            SAM: MW2043(tdk)
            SAR: SAR2207
            SAS: SAS2022
            SAC: SACOL2111(tdk)
            SAB: SAB2003c
            SAA: SAUSA300_2073(tdk)
            SAO: SAOUHSC_02360
            SAJ: SaurJH9_2155
            SAH: SaurJH1_2193
            SEP: SE1717
            SER: SERP1726(tdk)
            SHA: SH0916(tdk)
            SSP: SSP0765
            LMO: lmo2544
            LMF: LMOf2365_2517
            LIN: lin2688
            LWE: lwe2493(tdk)
            LLA: L184871(yfiG)
            LLC: LACR_0608
            LLM: llmg_0555(tdk)
            SPY: SPy_1140(tdk2)
            SPZ: M5005_Spy_0862(tdk2)
            SPM: spyM18_1100(tdk)
            SPG: SpyM3_0798(tdk)
            SPS: SPs0997
            SPH: MGAS10270_Spy0976(tdk2)
            SPI: MGAS10750_Spy1011(tdk2)
            SPJ: MGAS2096_Spy0936(tdk2)
            SPK: MGAS9429_Spy0979(tdk2)
            SPF: SpyM50928(tdk)
            SPA: M6_Spy0858
            SPB: M28_Spy0836(tdk2)
            SPN: SP_1018
            SPR: spr0922(tdk)
            SPD: SPD_0904(tdk)
            SAG: SAG1078(tdk)
            SAN: gbs1110
            SAK: SAK_1164(tdk)
            SMU: SMU.1086(kitH)
            STC: str0751(tdk)
            STL: stu0751(tdk)
            STE: STER_0792
            SSA: SSA_1151(tdk)
            LPL: lp_2379(tdk)
            LJO: LJ0929
            LAC: LBA0766
            LSA: LSA1138(tdk)
            LSL: LSL_0589(tdk)
            LDB: Ldb0700(tdk)
            LBU: LBUL_0632
            LBR: LVIS_1291
            LRE: Lreu_0451
            EFA: EF2555(tdK)
            OOE: OEOE_1598
            CAC: CAC2887(tdk)
            CPE: CPE2204(tdk)
            CPF: CPF_2468(tdk)
            CPR: CPR_2178(tdk)
            CTC: CTC00298
            CNO: NT01CX_0551
            CBO: CBO0136(tdk)
            CBA: CLB_0172(tdk)
            CBH: CLC_0184(tdk)
            CBF: CLI_0191(tdk)
            CBE: Cbei_0402
            AMT: Amet_0325
            CHY: CHY_0585(tdk)
            SWO: Swol_1112
            TTE: TTE0140(tdk)
            MGE: MG_034(tdk)
            MPN: MPN044(tdk)
            MPU: MYPU_1450(tdk)
            MPE: MYPE10320(tdk)
            MGA: MGA_0502(tdk)
            MMY: MSC_0149(tdk)
            MMO: MMOB6150(tdk)
            MHY: mhp627(tdk)
            MHJ: MHJ_0610(tdk)
            MHP: MHP7448_0608(tdk)
            MSY: MS53_0521(tdk)
            MCP: MCAP_0143(tdk)
            UUR: UU594(tdk)
            POY: PAM104(tdk)
            AYW: AYWB_605(tdk)
            MFL: Mfl635
            SCO: SCO5845(SC9B10.12)
            SMA: SAV2414(tdk)
            LXX: Lxx03510(tdk)
            ART: Arth_1631
            AAU: AAur_1778(tdk)
            PAC: PPA1049
            NCA: Noca_2919
            KRA: Krad_4250
            STP: Strop_2343
            RXY: Rxyl_2828
            RBA: RB8399(tdk)
            BGA: BG0816(tdk)
            BAF: BAPKO_0843(tdk)
            BTH: BT_2275
            BFR: BF0659
            BFS: BF0583(tdk)
            PGI: PG0925(tmk)
            SRU: SRU_2559(tdk)
            GFO: GFO_3354(tdk)
            FJO: Fjoh_0586
            FPS: FP1063(tdk)
            RRS: RoseRS_3804
            RCA: Rcas_1079
            DRA: DR_1984
            DGE: Dgeo_0578
            TMA: TM0401
            TPT: Tpet_0519
            TME: Tmel_1206
            FNO: Fnod_0798
            HAL: VNG1515G(tdk)
            HWA: HQ1795A(tdk)
            TAC: Ta1214
            TKO: TK1318
            PAI: PAE2453
            PAS: Pars_1427
STRUCTURES  PDB: 1E2H  1E2I  1E2J  1E2K  1E2L  1E2M  1E2N  1E2P  1KI2  1KI3  
                 1KI4  1KI6  1KI7  1KI8  1KIM  1OF1  1OSN  1P6X  1P72  1P73  
                 1P75  1P7C  1QHI  1VTK  1W4R  1XBT  1XX6  2B8T  2J87  2J9R  
                 2JA1  2KI5  2ORV  2ORW  2UZ3  2VTK  3VTK  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.21
            ExPASy - ENZYME nomenclature database: 2.7.1.21
            ExplorEnz - The Enzyme Database: 2.7.1.21
            ERGO genome analysis and discovery system: 2.7.1.21
            BRENDA, the Enzyme Database: 2.7.1.21
            CAS: 9002-06-6
///
ENTRY       EC 2.7.1.22                 Enzyme
NAME        ribosylnicotinamide kinase;
            ribosylnicotinamide kinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:N-ribosylnicotinamide 5'-phosphotransferase
REACTION    ATP + N-ribosylnicotinamide = ADP + nicotinamide ribonucleotide
            [RN:R02324]
ALL_REAC    R02324
SUBSTRATE   ATP [CPD:C00002];
            N-ribosylnicotinamide [CPD:C03150]
PRODUCT     ADP [CPD:C00008];
            nicotinamide ribonucleotide [CPD:C00455]
REFERENCE   1  [PMID:14907738]
  AUTHORS   ROWEN JW, KORNBERG A.
  TITLE     The phosphorolysis of nicotinamide riboside.
  JOURNAL   J. Biol. Chem. 193 (1951) 497-507.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.22
            ExPASy - ENZYME nomenclature database: 2.7.1.22
            ExplorEnz - The Enzyme Database: 2.7.1.22
            ERGO genome analysis and discovery system: 2.7.1.22
            BRENDA, the Enzyme Database: 2.7.1.22
            CAS: 9030-61-9
///
ENTRY       EC 2.7.1.23                 Enzyme
NAME        NAD+ kinase;
            DPN kinase;
            nicotinamide adenine dinucleotide kinase (phosphorylating);
            nicotinamide adenine dinucleotide kinase;
            NAD+ kinase;
            NAD+K
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:NAD+ 2'-phosphotransferase
REACTION    ATP + NAD+ = ADP + NADP+ [RN:R00104]
ALL_REAC    R00104
SUBSTRATE   ATP [CPD:C00002];
            NAD+ [CPD:C00003]
PRODUCT     ADP [CPD:C00008];
            NADP+ [CPD:C00006]
REFERENCE   1  [PMID:6290285]
  AUTHORS   Butler JR, McGuinness ET.
  TITLE     Candida utilis NAD+ kinase: purification, properties and affinity
            gel studies.
  JOURNAL   Int. J. Biochem. 14 (1982) 839-44.
  ORGANISM  Candida utilis
REFERENCE   2  [PMID:4290316]
  AUTHORS   Chung AE.
  TITLE     Nicotinamide adenine dinucleotide kinase from Azotobacter
            vinelandii. I. Purification and properties of the enzyme.
  JOURNAL   J. Biol. Chem. 242 (1967) 1182-6.
  ORGANISM  Azotobacter vinelandii
REFERENCE   3
  AUTHORS   Kornberg, A.
  TITLE     Enzymatic synthesis of triphosphopyridine nucleotide.
  JOURNAL   J. Biol. Chem. 182 (1950) 805-813.
  ORGANISM  pigeon
REFERENCE   4
  AUTHORS   Wang, T.P. and Kaplan, N.O.
  TITLE     Kinases for the synthesis of coenzyme A and triphosphopyridine
            nucleotide.
  JOURNAL   J. Biol. Chem. 206 (1954) 311-325.
  ORGANISM  pigeon
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K00858  NAD+ kinase
GENES       HSA: 65220(NADK)
            MMU: 192185(Nadk)
            GGA: 419403(RCJMB04_9i6)
            XLA: 379705(MGC68997)
            XTR: 448246(MGC88972)
            SPU: 584340(LOC584340)
            OSA: 4325416
            PIC: PICST_53028(POS5) PICST_87580(UTR1)
            CGR: CAGL0L01265g
            SPO: SPCC24B10.02c
            AFM: AFUA_2G01350 AFUA_5G05890
            DDI: DDB_0231370 DDB_0231371
            CPV: cgd8_1970
            CHO: Chro.80231
            TAN: TA04160
            TPV: TP03_0366
            TET: TTHERM_00013470 TTHERM_00048990
            TBR: Tb927.7.5080
            TCR: 508175.260 509151.40
            LMA: LmjF06.0460
            EHI: 2.t00078
            ECO: b2615(yfjB)
            ECJ: JW2596(yfjB)
            ECE: Z3908(yfjB)
            ECS: ECs3477
            ECC: c3137(ppnK)
            ECI: UTI89_C2949(yfjB)
            ECP: ECP_2615
            ECV: APECO1_3919(yfjB)
            ECW: EcE24377A_2899(ppnK)
            ECX: EcHS_A2773
            STY: STY2869(yfjB)
            STT: t2637(yfjB)
            SPT: SPA2542(yfjB)
            SEC: SC2682(yfjB)
            STM: STM2683(yfjB)
            YPE: YPO1106
            YPK: y3074
            YPM: YP_1050
            YPP: YPDSF_2591
            YPS: YPTB1140(ppnK)
            YEN: YE0999
            SFL: SF2674(yfjB)
            SFX: S2852(yfjB)
            SFV: SFV_2856(yfjB)
            SSN: SSON_2771(yfjB)
            SBO: SBO_2750(yfjB)
            SDY: SDY_2788(yfjB)
            ECA: ECA0841(ppnK)
            PLU: plu3373(ppnK)
            BUC: BU185(yfjB)
            BAS: BUsg179(yfjB)
            BAB: bbp174(ppnK)
            WBR: WGLp110(yfjB)
            SGL: SG1799
            ENT: Ent638_3095
            BFL: Bfl545(yfjB)
            BPN: BPEN_565(yfjB)
            HIN: HI0072
            HIT: NTHI0084(ppnK)
            HIQ: CGSHiGG_02900(ppnK)
            HDU: HD1804(pnnK)
            HSO: HS_0650(ppnK)
            PMU: PM0333
            MSU: MS0742
            APL: APL_0212(pnnK)
            XFA: XF2090
            XFT: PD0786(ppk)
            XCC: XCC1546
            XCB: XC_2688
            XCV: XCV1636(ppnK)
            XAC: XAC1595
            XOO: XOO2435
            XOM: XOO_2312(XOO2312)
            VCH: VC0853
            VVU: VV1_0366
            VVY: VV0824
            VPA: VP0650
            VFI: VF1997(ppnK)
            PPR: PBPRA0695(ppnK)
            PAE: PA3088
            PAU: PA14_24220
            PPU: PP_2012
            PST: PSPTO_3793(ppnK)
            PSB: Psyr_1685(ppnK)
            PSP: PSPPH_3600(ppnK)
            PFL: PFL_3286(ppnK)
            PFO: Pfl_2195(ppnK)
            PEN: PSEEN1708
            PAR: Psyc_1465(ppnK)
            PCR: Pcryo_1643
            ACI: ACIAD2231(ppnK)
            SON: SO_1523
            SDN: Sden_2573
            SFR: Sfri_2792
            SAZ: Sama_2438
            SBL: Sbal_1355
            SLO: Shew_2773
            SPC: Sputcn32_1273
            SHE: Shewmr4_2733
            SHM: Shewmr7_2806
            SHN: Shewana3_2903
            SHW: Sputw3181_2833
            ILO: IL0988(nadF)
            CPS: CPS_3824(ppnK)
            PHA: PSHAa1220(nadK)
            PAT: Patl_1715
            SDE: Sde_1733
            PIN: Ping_0915
            MAQ: Maqu_2072
            CBU: CBU_1296
            LPN: lpg2823
            LPF: lpl2738
            LPP: lpp2876
            MCA: MCA1859
            FTU: FTT1432c(ppnK)
            FTF: FTF1432c(ppnK)
            FTW: FTW_0434
            FTL: FTL_0626
            FTH: FTH_0629(ppnK)
            FTN: FTN_1402(ppnK)
            TCX: Tcr_0867
            NOC: Noc_1190
            AEH: Mlg_1903
            HHA: Hhal_1479
            HCH: HCH_04592
            CSA: Csal_1307
            ABO: ABO_0995(yfjB)
            AHA: AHA_2985
            DNO: DNO_1062
            BCI: BCI_0611(nadK)
            RMA: Rmag_1054
            VOK: COSY_0954
            NME: NMB0807
            NMA: NMA1017
            NGO: NGO0390
            CVI: CV_2322(ppnK)
            RSO: RSc2650(RS04566)
            REU: Reut_A1035(ppnK)
            REH: H16_A1132 H16_B0143(acoX)
            RME: Rmet_0999
            BMA: BMA2332(ppnK)
            BMV: BMASAVP1_A0493(ppnK)
            BML: BMA10299_A1106(ppnK)
            BMN: BMA10247_2213(ppnK)
            BXE: Bxe_A3967
            BVI: Bcep1808_0705
            BUR: Bcep18194_A3832(ppnK)
            BCN: Bcen_0260
            BCH: Bcen2424_0744
            BAM: Bamb_0638
            BPS: BPSL2833
            BPM: BURPS1710b_3328(ppnK)
            BTE: BTH_I1301
            PNU: Pnuc_1773
            BPE: BP2505(ppnK)
            BPA: BPP3491(ppnK)
            BBR: BB3940(ppnK)
            RFR: Rfer_1651
            POL: Bpro_1302
            PNA: Pnap_0908
            AAV: Aave_3601
            AJS: Ajs_0904
            VEI: Veis_1051
            MPT: Mpe_A3334
            HAR: HEAR2652(nadK)
            MMS: mma_2887
            NEU: NE1478
            NET: Neut_0768
            NMU: Nmul_A2422
            EBA: ebA4805(ppnK)
            AZO: azo2580(ppnK)
            DAR: Daro_0931
            TBD: Tbd_2031
            MFA: Mfla_0774
            HPY: HP1394
            HPJ: jhp1433
            HPA: HPAG1_1476
            HHE: HH1296
            HAC: Hac_1771(ppnK)
            WSU: WS1623
            TDN: Tmden_1085
            CJE: Cj0641
            CJR: CJE0744
            CJU: C8J_0600
            CFF: CFF8240_1195
            CCV: CCV52592_0464
            CHA: CHAB381_0297
            ABU: Abu_1986
            NIS: NIS_0772
            SUN: SUN_1233
            GSU: GSU2065(ppnK)
            GME: Gmet_0941
            PCA: Pcar_2327
            PPD: Ppro_1579
            DVU: DVU1888
            DVL: Dvul_1276
            DDE: Dde_2618
            LIP: LI1009(yfjB)
            BBA: Bd3172(ppnK)
            DPS: DP2234
            ADE: Adeh_0731
            MXA: MXAN_5363
            SAT: SYN_02863
            SFU: Sfum_0718
            RPR: RP440
            RTY: RT0427(ppnK)
            RCO: RC0612(ppnK)
            RFE: RF_0675(ppnK)
            RBE: RBE_1250 RBE_1251
            RAK: A1C_03295(ppnK)
            RBO: A1I_01030(ppnK)
            RCM: A1E_03915(ppnK)
            RRI: A1G_03460(ppnK)
            OTS: OTBS_1220(ppnK)
            WOL: WD0871(ppnK)
            WBM: Wbm0400
            AMA: AM106
            APH: APH_0089(ppnK)
            ERU: Erum7490(ppnK)
            ERW: ERWE_CDS_07890(ppnK)
            ERG: ERGA_CDS_07800(ppnK)
            ECN: Ecaj_0783
            ECH: ECH_0225
            NSE: NSE_0310
            PUB: SAR11_1132(ppnK)
            MLO: mll0225
            MES: Meso_1772
            PLA: Plav_2701
            SME: SMc01331
            SMD: Smed_0963
            ATU: Atu1345
            ATC: AGR_C_2483
            RET: RHE_CH01651(ypch00563)
            RLE: RL1755(ppnK)
            BME: BMEI1036
            BMF: BAB1_0954
            BMS: BR0937
            BMB: BruAb1_0946
            OAN: Oant_2250
            BRA: BRADO2990
            BBT: BBta_5177
            RPA: RPA3374
            RPB: RPB_2196
            RPC: RPC_3106
            RPD: RPD_3237
            RPE: RPE_2359
            NWI: Nwi_1335
            NHA: Nham_1663
            BHE: BH06480
            BQU: BQ06750
            XAU: Xaut_1643
            CCR: CC_1221
            SIL: SPO2939
            SIT: TM1040_1578
            RSP: RSP_0825(ppnK)
            RSH: Rsph17029_2482
            RSQ: Rsph17025_0353
            JAN: Jann_2990
            RDE: RD1_3989(ppnK)
            PDE: Pden_0921
            MMR: Mmar10_1840
            HNE: HNE_2064(ppnK)
            ZMO: ZMO1329
            NAR: Saro_1984
            SAL: Sala_1656
            SWI: Swit_1521
            ELI: ELI_05105
            GOX: GOX0418
            GBE: GbCGDNIH1_0329
            ACR: Acry_3061
            RRU: Rru_A0517
            MAG: amb0162
            MGM: Mmc1_1764
            ABA: Acid345_1046
            SUS: Acid_1116
            BSU: BG13143(yjbN) BG13837(ytdI)
            BHA: BH2848 BH3199
            BAN: BA1213 BA4893
            BAR: GBAA1213 GBAA4893
            BAA: BA_1748 BA_5314
            BAT: BAS1120 BAS4540
            BCE: BC1199(ppnK) BC4642(ppnK)
            BCA: BCE_1321 BCE_4778
            BCZ: BCZK1096(ppnK) BCZK4386(ppnK)
            BCY: Bcer98_0915 Bcer98_3315
            BTK: BT9727_1102(ppnK) BT9727_4376(ppnK)
            BTL: BALH_1061(ppnK) BALH_4220(ppnK)
            BLI: BL00367(ppnK2) BL05111(ppnK1)
            BLD: BLi01255(yjbN) BLi03093(ytdI)
            BCL: ABC2519(ppnK)
            BAY: RBAM_011620(yjbN)
            BPU: BPUM_1090 BPUM_2586
            OIH: OB1221(ppnK) OB2196
            GKA: GK0830(ppnK) GK2792
            SAU: SA0865
            SAV: SAV1007
            SAM: MW0888
            SAR: SAR0974
            SAS: SAS0876
            SAC: SACOL1011
            SAB: SAB0873
            SAA: SAUSA300_0908
            SAO: SAOUHSC_00943
            SAJ: SaurJH9_1005
            SAH: SaurJH1_1024
            SEP: SE0696
            SER: SERP0587
            SHA: SH1951
            SSP: SSP1778
            LMO: lmo0968 lmo1586
            LMF: LMOf2365_0988(ppnK) LMOf2365_1608
            LIN: lin0967 lin1628
            LWE: lwe0950 lwe1599
            LLA: L166614(ydgJ)
            LLC: LACR_0409
            LLM: llmg_0383(ppnK)
            SPY: SPy_1126
            SPZ: M5005_Spy_0848(ppnK)
            SPM: spyM18_1087
            SPG: SpyM3_0785
            SPS: SPs0986
            SPH: MGAS10270_Spy0964
            SPI: MGAS10750_Spy0999
            SPJ: MGAS2096_Spy0924
            SPK: MGAS9429_Spy0967
            SPF: SpyM50940(ppnK)
            SPA: M6_Spy0846(ppnK)
            SPB: M28_Spy0824(ppnK)
            SPN: SP_1098
            SPR: spr1005
            SPD: SPD_0983
            SAG: SAG1094
            SAN: gbs1161
            SAK: SAK_1179(ppnK)
            SMU: SMU.1045c
            STC: str1457(ppnK)
            STL: stu1457(ppnK)
            SSA: SSA_1209(ppnK)
            SGO: SGO_1221(ppnK)
            LPL: lp_2222(ppnK)
            LJO: LJ0824
            LAC: LBA0647(ppnK)
            LSA: LSA1443
            LSL: LSL_1304
            LDB: Ldb0585(ppnK)
            LBU: LBUL_0520
            LBR: LVIS_1472
            LCA: LSEI_0902
            LRE: Lreu_0573
            EFA: EF2670
            OOE: OEOE_1159
            STH: STH1837
            CAC: CAC2075
            CPE: CPE1817
            CPF: CPF_2071
            CPR: CPR_1785
            CTC: CTC01573
            CNO: NT01CX_1985
            CTH: Cthe_0816
            CBA: CLB_1816(ppnK)
            CBH: CLC_1823(ppnK)
            CBF: CLI_1943(ppnK)
            CKL: CKL_1233(ppnK)
            AMT: Amet_3174
            CHY: CHY_1983(ppnK)
            DSY: DSY2346
            DRM: Dred_1081
            SWO: Swol_0584
            TTE: TTE1300
            MTA: Moth_1509
            MGE: MG_128
            MPN: MPN267(A65_orf259)
            MPE: MYPE4600
            MGA: MGA_0291
            MMY: MSC_0302
            MCP: MCAP_0257
            UUR: UU177
            MFL: Mfl193
            MTU: Rv1695(ppnK)
            MTC: MT1734
            MBO: Mb1721(ppnK)
            MBB: BCG_1733(ppnK)
            MLE: ML1359
            MPA: MAP1402
            MAV: MAV_3076
            MSM: MSMEG_3750
            MVA: Mvan_3289
            MGI: Mflv_3508
            MMC: Mmcs_2950
            MKM: Mkms_2994
            MJL: Mjls_2965
            CGL: NCgl1358(ppnK)
            CGB: cg1601(ppnK)
            CEF: CE1547
            CDI: DIP1181(ppnK)
            CJK: jk0865(ppnK)
            NFA: nfa19970
            RHA: RHA1_ro00935
            SCO: SCO1781(ppnK)
            SMA: SAV1035 SAV6497
            TWH: TWT103
            TWS: TW112
            LXX: Lxx05620
            CMI: CMM_1985(ppnK)
            ART: Arth_1517
            AAU: AAur_1653(ppnK)
            PAC: PPA1395(ppnK)
            NCA: Noca_2481
            TFU: Tfu_2033(ppnK)
            FRA: Francci3_3159
            FAL: FRAAL3438 FRAAL5182
            ACE: Acel_1246
            KRA: Krad_1238
            SEN: SACE_5249
            STP: Strop_1702 Strop_1912
            BAD: BAD_0908(ppnK)
            RXY: Rxyl_1454
            FNU: FN0267
            RBA: RB2142
            PCU: pc0618
            BBU: BB0311
            BGA: BG0314
            BAF: BAPKO_0321
            TPA: TP0441
            TDE: TDE1591
            SYN: sll1415 slr0400
            SYW: SYNW1599 SYNW2270(ppnK)
            SYC: syc1797_c syc2229_c
            SYF: Synpcc7942_1865 Synpcc7942_2304
            SYD: Syncc9605_0914(ppnK) Syncc9605_2408(ppnK)
            SYE: Syncc9902_0284(ppnK) Syncc9902_1495(ppnK)
            SYG: sync_0806(ppnK) sync_2621
            SYR: SynRCC307_1743(ppnK) SynRCC307_2281(ppnK)
            SYX: SynWH7803_1710(ppnK) SynWH7803_2287(ppnK)
            CYA: CYA_2264
            CYB: CYB_0465
            TEL: tll0858 tlr0484
            GVI: gll0473 gll3525
            ANA: all4751 alr0227
            AVA: Ava_1921(ppnK) Ava_2718(ppnK)
            PMA: Pro0180 Pro1343
            PMM: PMM0156(ppnK) PMM1269
            PMT: PMT0368 PMT2016(ppnK)
            PMN: PMN2A_0835(ppnK) PMN2A_1523(ppnK)
            PMI: PMT9312_0158 PMT9312_1363
            PMB: A9601_01741 A9601_14681
            PMC: P9515_01851 P9515_14301
            PMF: P9303_19331 P9303_26861
            PMG: P9301_01761 P9301_14541
            PME: NATL1_02291 NATL1_16881
            TER: Tery_1770 Tery_3163
            BTH: BT_3917
            BFR: BF3968
            BFS: BF3741
            PGI: PG0629(ppnK)
            SRU: SRU_1609
            CHU: CHU_3408(ppnK)
            GFO: GFO_0215(ppnK)
            FPS: FP2093(ppnK)
            CTE: CT0085
            CCH: Cag_0019
            CPH: Cpha266_2573
            PVI: Cvib_1693
            PLT: Plut_2050
            DET: DET0458
            DEH: cbdb_A419
            AAE: aq_909
            TMA: TM1733
            TME: Tmel_1541
            FNO: Fnod_0155
            MJA: MJ0917
            MMP: MMP1489
            MMQ: MmarC5_0088
            MAC: MA3343
            MBA: Mbar_A2191
            MMA: MM_2784
            MBU: Mbur_0853
            MTP: Mthe_0840
            MHU: Mhun_0902
            MEM: Memar_0968
            MBN: Mboo_1352
            MTH: MTH872
            MST: Msp_1330(ppnK)
            MSI: Msm_0879
            MKA: MK0742
            AFU: AF2373
            HAL: VNG1900C
            HMA: rrnAC0727 rrnAC0821 rrnAC3391(ppnK)
            NPH: NP2512A(ppnK_1) NP4558A(ppnK_2)
            TAC: Ta0622
            TVO: TVN1034
            PTO: PTO0193(ppnK)
            PHO: PH1074
            PAB: PAB1756
            PFU: PF1103
            TKO: TK2124
            RCI: LRC51(ppnK)
            APE: APE_1104.1
            IHO: Igni_0536
            SSO: SSO2219
            STO: ST2136
            SAI: Saci_0027
            MSE: Msed_0740 Msed_1268
            PAI: PAE0624
            TPE: Tpen_0523
STRUCTURES  PDB: 1SUW  1U0R  1U0T  1Y3H  1Y3I  1YT5  1Z0S  1Z0U  1Z0Z  2AN1  
                 2I1W  2I29  2I2A  2I2B  2I2C  2I2D  2I2E  2I2F  2Q5F  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.23
            ExPASy - ENZYME nomenclature database: 2.7.1.23
            ExplorEnz - The Enzyme Database: 2.7.1.23
            ERGO genome analysis and discovery system: 2.7.1.23
            BRENDA, the Enzyme Database: 2.7.1.23
            CAS: 9032-66-0
///
ENTRY       EC 2.7.1.24                 Enzyme
NAME        dephospho-CoA kinase;
            dephosphocoenzyme A kinase (phosphorylating);
            3'-dephospho-CoA kinase;
            dephosphocoenzyme A kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:dephospho-CoA 3'-phosphotransferase
REACTION    ATP + dephospho-CoA = ADP + CoA [RN:R00130]
ALL_REAC    R00130
SUBSTRATE   ATP [CPD:C00002];
            dephospho-CoA [CPD:C00882]
PRODUCT     ADP [CPD:C00008];
            CoA [CPD:C00010]
REFERENCE   1
  AUTHORS   Abiko, Y.
  TITLE     Pantothenic acid and coenzyme A:dephospho-CoA pyrophosphorylase and
            dephospho-CoA kinase as a possible bifunctional enzyme complex
            (ATP:pantetheine-4'-phosphate adenylyltransferase, EC 2.7.7.3 and
            ATP:dephospho-CoA-3'-phosphotransferase EC 2.7.1.24).
  JOURNAL   Methods Enzymol. 18A (1970) 358-364.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:13163064]
  AUTHORS   HOAGLAND MB, NOVELLI GD.
  TITLE     Biosynthesis of coenzyme A from phospho-pantetheine and of
            pantetheine from pantothenate.
  JOURNAL   J. Biol. Chem. 207 (1954) 767-73.
  ORGANISM  pigeon, rat [GN:rno], pig [GN:ssc]
REFERENCE   3
  AUTHORS   Wang, T.P. and Kaplan, N.O.
  TITLE     Kinases for the synthesis of coenzyme A and triphosphopyridine
            nucleotide.
  JOURNAL   J. Biol. Chem. 206 (1954) 311-325.
  ORGANISM  pigeon, duck
PATHWAY     PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K00859  dephospho-CoA kinase
GENES       HSA: 80347(COASY)
            MMU: 71743(Coasy)
            SSC: 396688(PPAT/DPCK)
            CEL: T05G5.5
            OSA: 4326028
            PIC: PICST_41000(COA5)
            CAL: CaO19_4005(CaO19.4005)
            AFM: AFUA_5G02060
            AOR: AO090003001319
            ECU: ECU11_0300
            DDI: DDB_0231517
            PFA: PF14_0415
            CHO: Chro.20045
            TPV: TP01_0811
            TET: TTHERM_00523030
            TBR: Tb927.6.710
            TCR: 511825.210
            LMA: LmjF22.1530
            EHI: 23.t00005 361.t00011
            ECO: b0103(yacE)
            ECJ: JW0100(coaE)
            ECE: Z0113(yacE)
            ECS: ECs0107
            ECC: c0123(coaE)
            ECI: UTI89_C0111(coaE)
            ECP: ECP_0104
            ECV: APECO1_1885(coaC)
            ECW: EcE24377A_0105(coaE)
            ECX: EcHS_A0108(coaE)
            STY: STY0162(yacE)
            STT: t0146(yacE)
            SPT: SPA0144(yacE)
            SEC: SC0139(yacE)
            STM: STM0140(yacE)
            YPE: YPO3430
            YPK: y0757
            YPM: YP_0254(coaE)
            YPP: YPDSF_2925
            YPS: YPTB0702(coaE)
            YPI: YpsIP31758_3374(coaE)
            SFL: SF0100(yacE)
            SFX: S0102(yacE)
            SFV: SFV_0095(yacE)
            SSN: SSON_0111(yacE)
            SBO: SBO_0091(yacE)
            SDY: SDY_0133(yacE)
            ECA: ECA3802(coaE)
            PLU: plu3641(coaE)
            BUC: BU203(yacE)
            BAS: BUsg197(yacE)
            WBR: WGLp193(yacE)
            SGL: SG0461
            ENT: Ent638_0648
            SPE: Spro_0774
            BPN: BPEN_153(coaE)
            HIN: HI0890m(coaE)
            HIT: NTHI1055(coaE)
            HIP: CGSHiEE_07575(coaE)
            HDU: HD1127(coaE)
            HSO: HS_0459(coaE)
            PMU: PM0088
            MSU: MS0359(coaE)
            APL: APL_0876(coaE)
            ASU: Asuc_0609
            XFA: XF2536
            XFT: PD1921(coaE)
            XCC: XCC3102
            XCB: XC_1055
            XCV: XCV3356(coaE)
            XAC: XAC3244
            XOO: XOO1583
            XOM: XOO_1465(XOO1465)
            VCH: VC2427
            VVU: VV1_1621 VV1_1622
            VVY: VV2782
            VPA: VP2527
            VFI: VF2189
            PPR: PBPRA3204
            PAE: PA4529
            PAU: PA14_58780(coaE)
            PAP: PSPA7_5165(coaE)
            PPU: PP_0631
            PPF: Pput_0672
            PST: PSPTO_0923(coaE)
            PSB: Psyr_0795(coaE)
            PSP: PSPPH_0817(coaE)
            PFL: PFL_5290(coaE)
            PFO: Pfl_4823(coaE)
            PEN: PSEEN4669(coaE)
            PMY: Pmen_0772
            PAR: Psyc_0061(coaE)
            PCR: Pcryo_0066
            PRW: PsycPRwf_0148
            ACI: ACIAD0359(coaE)
            SON: SO_0413
            SDN: Sden_3392
            SFR: Sfri_3786
            SAZ: Sama_0366
            SBL: Sbal_3922
            SBM: Shew185_3945
            SLO: Shew_3441
            SPC: Sputcn32_3426
            SSE: Ssed_0422
            SPL: Spea_0410
            SHE: Shewmr4_0417
            SHM: Shewmr7_3608
            SHN: Shewana3_0416
            SHW: Sputw3181_0513
            ILO: IL0449(coaE)
            CPS: CPS_4450(coaE)
            PHA: PSHAa0379(coaE)
            PAT: Patl_3341
            SDE: Sde_0860
            PIN: Ping_1159
            MAQ: Maqu_2684
            CBU: CBU_0152(coaE)
            CBD: COXBU7E912_1954(coaE)
            LPN: lpg1467
            LPF: lpl1561
            LPP: lpp1423
            MCA: MCA2093(coaE)
            FTU: FTT1487(coaE)
            FTF: FTF1487(coaE)
            FTW: FTW_0806(coaE)
            FTL: FTL_0307
            FTH: FTH_0308(coaE)
            FTA: FTA_0326(coaE)
            FTN: FTN_1496(coaE)
            TCX: Tcr_0594
            NOC: Noc_0309
            AEH: Mlg_2082
            HHA: Hhal_2023
            HCH: HCH_05281(coaE)
            CSA: Csal_2177
            ABO: ABO_0611(coaE)
            MMW: Mmwyl1_2316
            AHA: AHA_3872(coaE)
            DNO: DNO_1122(coaE)
            BCI: BCI_0514(coaE)
            RMA: Rmag_0061
            VOK: COSY_0065(coaE)
            NME: NMB0331
            NMA: NMA2157
            NGO: NGO1671
            CVI: CV_3825
            RSO: RSc2828(RS00277)
            REU: Reut_A2963
            REH: H16_A3258(coaE)
            RME: Rmet_3111
            BMA: BMA2534
            BMV: BMASAVP1_A0456
            BML: BMA10299_A1314
            BMN: BMA10247_3248
            BXE: Bxe_A0501
            BVI: Bcep1808_0550
            BUR: Bcep18194_A3660
            BCN: Bcen_0093
            BCH: Bcen2424_0575
            BAM: Bamb_0478
            BPS: BPSL3011(coaE)
            BPM: BURPS1710b_3530(coaE)
            BPL: BURPS1106A_3534(coaE)
            BPD: BURPS668_3509(coaE)
            BTE: BTH_I1133(coaE)
            PNU: Pnuc_0183
            BPE: BP3817(coaE)
            BPA: BPP3961(coaE)
            BBR: BB4434(coaE)
            RFR: Rfer_2905
            POL: Bpro_0844
            PNA: Pnap_0769
            AAV: Aave_3683
            AJS: Ajs_0802
            VEI: Veis_3922
            MPT: Mpe_A0506
            HAR: HEAR2792(coaE)
            MMS: mma_2999(coaE)
            NEU: NE0598
            NET: Neut_1045
            NMU: Nmul_A2130
            EBA: ebA4105(coaE)
            AZO: azo0731(coaE)
            DAR: Daro_3709
            TBD: Tbd_2367
            MFA: Mfla_2226
            HPY: HP0831
            HPJ: jhp0770
            HPA: HPAG1_0817
            HHE: HH1700
            HAC: Hac_1201
            WSU: WS2149
            TDN: Tmden_2047
            CJE: Cj1530
            CJR: CJE1701
            CJJ: CJJ81176_1515
            CJU: C8J_1429
            CJD: JJD26997_1882
            CFF: CFF8240_1772(coaE)
            CCV: CCV52592_0349(coaE)
            CHA: CHAB381_0108(coaE)
            CCO: CCC13826_1842(coaE)
            ABU: Abu_0143(coaE)
            NIS: NIS_0101
            SUN: SUN_2409
            GSU: GSU0513
            GME: Gmet_3026
            GUR: Gura_3643
            PCA: Pcar_0757
            PPD: Ppro_2356
            DVL: Dvul_1969
            BBA: Bd3147(coaE)
            DPS: DP2729
            ADE: Adeh_2684
            AFW: Anae109_2675
            MXA: MXAN_3021(coaE)
            SAT: SYN_02876
            SFU: Sfum_0161
            RPR: RP731
            RTY: RT0717(coaE)
            RCO: RC1111(coaE)
            RFE: RF_0177(coaE)
            RBE: RBE_0363(coaE)
            RAK: A1C_05865(coaE)
            RBO: A1I_05960(coaE)
            RCM: A1E_01120(coaE)
            RRI: A1G_06160(coaE)
            WOL: WD0185
            WBM: Wbm0259
            AMA: AM438(coaE)
            APH: APH_0780(coaE)
            ERU: Erum2960(coaE)
            ERW: ERWE_CDS_03020(coaE)
            ERG: ERGA_CDS_02960(coaE)
            ECN: Ecaj_0277
            ECH: ECH_0801(coaE)
            NSE: NSE_0309(coaE)
            PUB: SAR11_0340(coaE)
            MLO: mlr4493
            MES: Meso_3481
            PLA: Plav_1253
            SME: SMc02790
            SMD: Smed_3212
            ATU: Atu0004(coaE)
            ATC: AGR_C_5
            RET: RHE_CH00004(coaE)
            RLE: RL0004
            BME: BMEI2057
            BMF: BAB1_2071
            BMS: BR2070
            BMB: BruAb1_2045(coaE)
            BOV: BOV_1990(coaE)
            OAN: Oant_0850
            BJA: blr0639(coaE)
            BRA: BRADO0201(coaE)
            BBT: BBta_0159(coaE)
            RPA: RPA0300(coaE)
            RPB: RPB_0397
            RPC: RPC_0296
            RPD: RPD_0424
            RPE: RPE_0378
            NWI: Nwi_0104(coaE)
            NHA: Nham_0114
            BHE: BH00040(coaE)
            BQU: BQ00040(coaE)
            BBK: BARBAKC583_0005(coaE)
            XAU: Xaut_1830
            CCR: CC_0004
            SIL: SPO3890(coaE)
            SIT: TM1040_2859
            RSP: RSP_1235(coaE)
            RSH: Rsph17029_2896
            RSQ: Rsph17025_2672
            JAN: Jann_0195
            RDE: RD1_0439(coaE)
            PDE: Pden_2814
            MMR: Mmar10_2977
            HNE: HNE_0004(coaE)
            ZMO: ZMO0040(coaE)
            NAR: Saro_0114
            SAL: Sala_2839
            SWI: Swit_2829
            ELI: ELI_12985
            GOX: GOX1960
            GBE: GbCGDNIH1_2143
            ACR: Acry_2760
            RRU: Rru_A3612
            MAG: amb4546
            MGM: Mmc1_0020
            ABA: Acid345_4423
            SUS: Acid_4781
            BSU: BG13824(coaE)
            BHA: BH3150
            BAN: BA4828
            BAR: GBAA4828
            BAA: BA_5252(coaE)
            BAT: BAS4479
            BCE: BC4584
            BCA: BCE_4715
            BCZ: BCZK4325(coaE)
            BCY: Bcer98_3269
            BTK: BT9727_4314(coaE)
            BTL: BALH_4167(coaE)
            BLI: BL00391(coaE)
            BLD: BLi03054(ytaG)
            BCL: ABC2706(coaE)
            BPU: BPUM_2548(coaE)
            OIH: OB2161
            GKA: GK2727
            SAU: SA1511
            SAV: SAV1688
            SAM: MW1631
            SAR: SAR1767(coaE)
            SAS: SAS1616
            SAC: SACOL1735(coaE)
            SAB: SAB1547c(coaE)
            SAA: SAUSA300_1634(coaE)
            SAO: SAOUHSC_01795
            SAJ: SaurJH9_1745
            SAH: SaurJH1_1779
            SEP: SE1365
            SER: SERP1252(coaE)
            SHA: SH1236
            SSP: SSP1077
            LMO: lmo1563
            LMF: LMOf2365_1585(coaE)
            LIN: lin1598
            LWE: lwe1576(coaE)
            LLA: L59930(yggA)
            LLC: LACR_0692
            LLM: llmg_0630(coaE)
            SPY: SPy_0498
            SPZ: M5005_Spy_0409(coaE)
            SPM: spyM18_0556
            SPG: SpyM3_0348
            SPS: SPs1506
            SPH: MGAS10270_Spy0410
            SPI: MGAS10750_Spy0422
            SPJ: MGAS2096_Spy0428
            SPK: MGAS9429_Spy0408
            SPF: SpyM51460(coaE)
            SPA: M6_Spy0435(coaE)
            SPB: M28_Spy0397(coaE)
            SPN: SP_0971
            SPR: spr0873
            SPD: SPD_0859(coaE)
            SAG: SAG1488
            SAN: gbs1553
            SAK: SAK_1518(coaE)
            SMU: SMU.1613c
            STC: str0621(coaE)
            STL: stu0621(coaE)
            SSA: SSA_1606(coaE)
            SGO: SGO_0716(coaE)
            LPL: lp_1510(coaE)
            LJO: LJ1649
            LAC: LBA1548(coaE)
            LSA: LSA1404(coaE)
            LSL: LSL_0490(coaE)
            LDB: Ldb1510(coaE)
            LBU: LBUL_1405
            LBR: LVIS_1040
            LCA: LSEI_1707
            LGA: LGAS_1419
            LRE: Lreu_1245
            EFA: EF0880
            OOE: OEOE_0676
            STH: STH851
            CAC: CAC1099
            CPE: CPE1993
            CPF: CPF_2249(coaE)
            CPR: CPR_1961(coaE)
            CTC: CTC02101(coaE)
            CNO: NT01CX_1678(coaE)
            CTH: Cthe_0885
            CDF: CD1129(coaE)
            CBO: CBO3013(coaE)
            CBA: CLB_3038(coaE)
            CBH: CLC_2910(coaE)
            CBF: CLI_3067(coaE)
            CBE: Cbei_0802
            CKL: CKL_0670(coaE)
            AMT: Amet_3124
            CHY: CHY_1647(coaE)
            DSY: DSY1345
            DRM: Dred_1596
            SWO: Swol_2014
            CSC: Csac_1987
            TTE: TTE0875(coaE)
            MTA: Moth_1838
            MGE: MG_264
            MPN: MPN382(A19_orf200)
            MPU: MYPU_7210
            MGA: MGA_1054n(coaE)
            MMY: MSC_0096(coaE)
            MMO: MMOB5770(coaE)
            MCP: MCAP_0054
            MFL: Mfl281
            MTU: Rv1631(coaE)
            MTC: MT1667
            MBO: Mb1657(coaE)
            MBB: BCG_1669(coaE)
            MLE: ML1383
            MPA: MAP1326
            MAV: MAV_3151
            MVA: Mvan_3353
            MGI: Mflv_3559
            MMC: Mmcs_3004
            MKM: Mkms_3050
            MJL: Mjls_3019
            CGL: NCgl1306(cgl1361)
            CGB: cg1538
            CEF: CE1459
            CDI: DIP1152(coaE)
            CJK: jk0825(coaE)
            NFA: nfa18990
            RHA: RHA1_ro00978
            SCO: SCO1996(coaE)
            SMA: SAV6235(coaE)
            TWH: TWT294(coaE)
            TWS: TW478(coaE)
            LXX: Lxx11440
            ART: Arth_2069
            AAU: AAur_2070(coaE)
            PAC: PPA0785
            NCA: Noca_2981
            TFU: Tfu_1192
            FRA: Francci3_1625
            FAL: FRAAL4608(coaE)
            ACE: Acel_1091
            KRA: Krad_2943
            SEN: SACE_5429(coaE)
            STP: Strop_3139
            BLO: BL0991
            BAD: BAD_0675
            RXY: Rxyl_2023
            FNU: FN1932
            RBA: RB6607
            CTR: CT492(yacE)
            CTA: CTA_0539(coaE)
            CMU: TC0779
            CPN: CPn0611(yacE)
            CPA: CP0136
            CPJ: CPj0611(yacE)
            CPT: CpB0635
            CCA: CCA00129
            CAB: CAB128
            CFE: CF0877(yacE)
            PCU: pc0222(yacE)
            BBU: BB0547
            BGA: BG0557
            BAF: BAPKO_0576
            TPA: TP0296
            TDE: TDE1638
            LIL: LA3863(coaE)
            LIC: LIC13085(coaE)
            LBJ: LBJ_0653(coaE)
            LBL: LBL_2426(coaE)
            SYN: slr0553
            SYW: SYNW2354(coaE)
            SYC: syc1240_c
            SYF: Synpcc7942_0273
            SYD: Syncc9605_2490
            SYE: Syncc9902_2167
            SYG: sync_2737(coaE)
            SYR: SynRCC307_2374(coaE)
            SYX: SynWH7803_2384(coaE)
            CYA: CYA_0565(coaE)
            CYB: CYB_1306(coaE)
            TEL: tlr0898
            GVI: glr2134
            ANA: all1754
            AVA: Ava_0282
            PMA: Pro0053(coaE)
            PMM: PMM0049(coaE)
            PMT: PMT2136(coaE)
            PMN: PMN2A_1382
            PMI: PMT9312_0050
            PMB: A9601_00501(coaE)
            PMC: P9515_00561(coaE)
            PMF: P9303_28241(coaE)
            PMG: P9301_00521(coaE)
            PMH: P9215_00591(coaE)
            PME: NATL1_00631(coaE)
            TER: Tery_0362
            BTH: BT_4594
            BFR: BF1202
            BFS: BF1169
            PGI: PG0483
            SRU: SRU_2791(coaE)
            CHU: CHU_2441(coaE)
            GFO: GFO_0656(coaE)
            FJO: Fjoh_3462
            FPS: FP1828(coaE)
            CTE: CT1209
            CCH: Cag_0965
            CPH: Cpha266_0985
            PVI: Cvib_0976
            PLT: Plut_1222
            DET: DET1323(coaE)
            DEH: cbdb_A1268(coaE)
            DEB: DehaBAV1_1134
            RRS: RoseRS_4316
            RCA: Rcas_4180
            DRA: DR_1892
            DGE: Dgeo_0828
            TTH: TTC0557
            TTJ: TTHA0926
            AAE: aq_1985
            TMA: TM1387
            TPT: Tpet_1396
            HWA: HQ3047A(coaE)
            NPH: NP0870A(coaE)
STRUCTURES  PDB: 1JJV  1N3B  1T3H  1VHL  1VHT  1VIY  2GRJ  2IF2  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.24
            ExPASy - ENZYME nomenclature database: 2.7.1.24
            ExplorEnz - The Enzyme Database: 2.7.1.24
            ERGO genome analysis and discovery system: 2.7.1.24
            BRENDA, the Enzyme Database: 2.7.1.24
            CAS: 9026-83-9
///
ENTRY       EC 2.7.1.25                 Enzyme
NAME        adenylyl-sulfate kinase;
            adenylylsulfate kinase (phosphorylating);
            5'-phosphoadenosine sulfate kinase;
            adenosine 5'-phosphosulfate kinase;
            adenosine phosphosulfate kinase;
            adenosine phosphosulfokinase;
            adenosine-5'-phosphosulfate-3'-phosphokinase;
            APS kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:adenylyl-sulfate 3'-phosphotransferase
REACTION    ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
            [RN:R00509]
ALL_REAC    R00509;
            (other) R04928
SUBSTRATE   ATP [CPD:C00002];
            adenylyl sulfate [CPD:C00224]
PRODUCT     ADP [CPD:C00008];
            3'-phosphoadenylyl sulfate [CPD:C00053]
COMMENT     The human phosphoadenosine-phosphosulfate synthase (PAPS) system is
            a bifunctional enzyme (fusion product of two catalytic activities).
            In a first step, sulfate adenylyltransferase catalyses the formation
            of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate.
            The second step is catalysed by the adenylylsulfate kinase portion
            of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which
            involves the formation of PAPS from enzyme-bound APS and ATP. In
            contrast, in bacteria, yeast, fungi and plants, the formation of
            PAPS is carried out by two individual polypeptides, sulfate
            adenylyltransferase (EC 2.7.7.4) and adenylyl-sulfate kinase (EC
            2.7.1.25).
REFERENCE   1
  AUTHORS   Bandurski, R.S., Wilson, L.G., Squires, C.L.
  TITLE     The mechanism of "active sulfate" formation.
  JOURNAL   J. Am. Chem. Soc. 78 (1956) 6408-6409.
REFERENCE   2  [PMID:13502346]
  AUTHORS   ROBBINS PW, LIPMANN F.
  TITLE     Isolation and identification of active sulfate.
  JOURNAL   J. Biol. Chem. 229 (1957) 837-51.
REFERENCE   3  [PMID:9668121]
  AUTHORS   Venkatachalam KV, Akita H, Strott CA.
  TITLE     Molecular cloning, expression, and characterization of human
            bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its
            functional domains.
  JOURNAL   J. Biol. Chem. 273 (1998) 19311-20.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00450  Selenoamino acid metabolism
            PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K00860  adenylylsulfate kinase
GENES       HSA: 9060(PAPSS2)
            PTR: 461422(PAPSS1)
            MMU: 23971(Papss1) 23972(Papss2)
            CFA: 478504(PAPSS1) 486463(PAPSS2)
            GGA: 422530(PAPSS1)
            XLA: 398910(MGC68677) 446649(papss1)
            XTR: 448413(papss1)
            SPU: 576349(LOC576349)
            CEL: T14G10.1(pps-1)
            ATH: AT5G67520
            CME: CMB151C
            SCE: YKL001C(MET14)
            AGO: AGOS_ABR001W
            PIC: PICST_90976(KAP1)
            CGR: CAGL0L02321g
            SPO: SPAC1782.11
            ANI: AN1194.2
            AFM: AFUA_1G10820
            AOR: AO090038000333
            CNE: CNE03380
            EHI: 15.t00012
            ECO: b2750(cysC)
            ECJ: JW2720(cysC)
            ECE: Z4058(cysC)
            ECS: ECs3604
            ECC: c3317(cysC)
            ECI: UTI89_C3121(cysC)
            ECP: ECP_2732
            ECV: APECO1_37732(cysC)
            ECW: EcE24377A_3051(cysC)
            ECX: EcHS_A2888(cysC)
            STY: STY3058(cysC)
            STT: t2834(cysC)
            SPT: SPA2789(cysC)
            SEC: SC2865(cysC)
            STM: STM2933(cysC)
            YPE: YPO3364(cysC)
            YPK: y0825(cysC)
            YPM: YP_0323(cysC)
            YPA: YPA_2779
            YPN: YPN_0729
            YPP: YPDSF_2996
            YPS: YPTB0767(cysC)
            YPI: YpsIP31758_3302(cysC)
            YEN: YE0764(cysC)
            SFL: SF2773(cysC)
            SFX: S2966(cysC)
            SFV: SFV_2748(cysC)
            SSN: SSON_2898(cysC)
            SBO: SBO_2770(cysC)
            SDY: SDY_2949(cysC)
            ECA: ECA3541(cysC)
            PLU: plu0711(cysC)
            BUC: BU422(cysC)
            BAS: BUsg407(cysC)
            SGL: SG0523
            ENT: Ent638_3221
            SPE: Spro_0820
            BFL: Bfl164(cysC)
            BPN: BPEN_169(cysC)
            XFA: XF1501
            XFT: PD0718(nodQ)
            XCC: XCC3171(nodQ)
            XCB: XC_0994
            XCV: XCV3445(cysN)
            XAC: XAC3328(nodQ)
            XOO: XOO3396(nodQ)
            XOM: XOO_3197(XOO3197)
            VCH: VC2558
            VCO: VC0395_A2135(cysC)
            VVU: VV1_0723
            VVY: VV0414
            VPA: VP0296
            VFI: VF0323
            PPR: PBPRA3308
            PAE: PA1393(cysC) PA4442(cysN)
            PPU: PP_1304(cysNC)
            PST: PSPTO_4432(cysN/C) PSPTO_5557(cysC)
            PSB: Psyr_4126
            PSP: PSPPH_4301(cysC1) PSPPH_5179(cysC2)
            PFL: PFL_0529(cysC) PFL_0936(cysN) PFL_5482(cysNC)
            PFO: Pfl_0162 Pfl_0483 Pfl_0878
            PEN: PSEEN0748(cycC-2) PSEEN4517(cysNC) PSEEN5524(cycC)
            PMY: Pmen_1862
            SON: SO_3723(cysC)
            SDN: Sden_0962
            SFR: Sfri_3184
            SAZ: Sama_2888
            SBL: Sbal_3405
            SBM: Shew185_0931
            SLO: Shew_1425
            SPC: Sputcn32_3040
            SSE: Ssed_2957 Ssed_2985
            SPL: Spea_0666
            SHE: Shewmr4_3069
            SHM: Shewmr7_0903
            SHN: Shewana3_0866
            SHW: Sputw3181_0905
            CPS: CPS_2145(cysC)
            PHA: PSHAa0209(cysC)
            PAT: Patl_1650
            SDE: Sde_2136
            PIN: Ping_0800
            MAQ: Maqu_2622
            CBU: CBU_0700
            CBD: COXBU7E912_0714(sat)
            MCA: MCA2204(cysC) MCA2628
            FTW: FTW_0958(cysC)
            FTL: FTL_1036
            FTA: FTA_1096(cysC)
            FTN: FTN_0926(cysC)
            NOC: Noc_2482
            AEH: Mlg_2345
            HHA: Hhal_2350 Hhal_2354
            HCH: HCH_02737 HCH_05344 HCH_06167
            CSA: Csal_1687
            ABO: ABO_0930(apsK)
            AHA: AHA_3564(cysC) AHA_4157
            BCI: BCI_0212(cysC)
            CVI: CV_2104(cysC)
            RSO: RSc3166(cysC1) RSp0166(cysC2)
            REU: Reut_A0739 Reut_A1530
            BMA: BMA0637(cysC-1) BMA1639 BMAA0153(cysC-2)
            BMV: BMASAVP1_1322(cysC-2) BMASAVP1_A2375(cysC-1)
            BML: BMA10299_A2912(cysC-1)
            BMN: BMA10247_1690(cysC-1) BMA10247_A0177(cysC-2)
            BXE: Bxe_A2481
            BVI: Bcep1808_0726 Bcep1808_3209
            BUR: Bcep18194_A5471 Bcep18194_A5496 Bcep18194_B1085
            BCN: Bcen_0303
            BCH: Bcen2424_0786
            BAM: Bamb_0664
            BPS: BPSL1668 BPSL2233 BPSS1926
            BPM: BURPS1710b_2668(cysN) BURPS1710b_2799(cysC)
                 BURPS1710b_A1028(cysC-2)
            BPL: BURPS1106A_2056(cysC) BURPS1106A_2580(cysC)
                 BURPS1106A_2733(cysC) BURPS1106A_A2619(cysC)
            BPD: BURPS668_2526(cysC) BURPS668_2676(cysC) BURPS668_A2763(cysC)
            BTE: BTH_I1816(cysC) BTH_I1952 BTH_II0450
            PNU: Pnuc_0334 Pnuc_1099
            AAV: Aave_4709
            MMS: mma_0523(cysC)
            NET: Neut_0164
            NMU: Nmul_A0299
            TBD: Tbd_0210
            HHE: HH1438(cysC)
            WSU: WS2182(cysC)
            CJE: Cj1415c(cysC)
            ABU: Abu_2175(cysNC)
            SUN: SUN_1719(cysC)
            GSU: GSU1718
            GUR: Gura_3831
            PCA: Pcar_1768
            PPD: Ppro_0064
            DVU: DVUA0079(cysC)
            DVL: Dvul_3030
            DPS: DP2110
            ADE: Adeh_0771 Adeh_1541
            AFW: Anae109_1642
            MXA: MXAN_3487(cysC) MXAN_4064
            SFU: Sfum_0774 Sfum_2338
            PUB: SAR11_1262(cysC)
            MLO: mlr7576
            MES: Meso_0834
            PLA: Plav_3064
            SME: SMa0857(nodQ1) SMb21224(nodQ2)
            SMD: Smed_4560 Smed_6191
            BME: BMEI1754
            BMF: BAB1_0194
            BMS: BR0194(cysNC)
            BMB: BruAb1_0189(cysNC)
            BOV: BOV_0186(cysNC)
            OAN: Oant_0201
            BJA: bll1475(nodQ)
            BRA: BRADO1063 BRADO5193
            BBT: BBta_0327 BBta_6984(cysNC)
            RPA: RPA0753(cysN)
            RPB: RPB_1042
            RPC: RPC_0064 RPC_4017
            RPD: RPD_1153
            RPE: RPE_0333 RPE_1761
            NWI: Nwi_2764
            NHA: Nham_3564
            XAU: Xaut_1400
            CCR: CC_1482
            SIL: SPO0900(sat)
            SIT: TM1040_0612
            RSP: RSP_1575(sopT)
            RSH: Rsph17029_0227
            RSQ: Rsph17025_0255
            JAN: Jann_3340
            RDE: RD1_B0030(sat)
            PDE: Pden_4396
            MMR: Mmar10_2450
            HNE: HNE_0776(cysNC)
            ZMO: ZMO0003(cysC)
            NAR: Saro_3253
            SAL: Sala_1526
            SWI: Swit_3342
            ELI: ELI_13670
            GOX: GOX0926
            GBE: GbCGDNIH1_2160
            ACR: Acry_1319
            RRU: Rru_A2290
            MAG: amb2212
            MGM: Mmc1_1018
            SUS: Acid_7933
            BSU: BG13105(yisZ) BG13379(cycC)
            BHA: BH1489 BH3385
            BAN: BA1442(cysC)
            BAR: GBAA1442(cysC)
            BAA: BA_1963
            BAT: BAS1332
            BCE: BC1423
            BCA: BCE_1546(cysC)
            BCZ: BCZK1306
            BCY: Bcer98_1145
            BTK: BT9727_1305
            BLI: BL02285(cysC)
            BLD: BLi01781(cysC)
            BCL: ABC0614
            BAY: RBAM_015430(cysC)
            BPU: BPUM_1459(cysC)
            OIH: OB1661
            GKA: GK0414
            SEP: SE2174
            SER: SERP2185(cysC)
            SHA: SH0420
            SSP: SSP2401
            LPL: lp_1379(cysC)
            CAC: CAC0103(cysC) CAC0110(cysN)
            CKL: CKL_1799(cysC)
            AMT: Amet_3496
            CHY: CHY_2693(cysC)
            DSY: DSY2951(cysN)
            MTU: Rv1286(cysN)
            MTC: MT1324(cysN)
            MBO: Mb1317(cysN)
            MBB: BCG_1345(cysN)
            MPA: MAP2484c(cysN) MAP2599c
            MAV: MAV_1325(cysC)
            MVA: Mvan_4422
            MGI: Mflv_2272
            MMC: Mmcs_0387 Mmcs_3918
            MKM: Mkms_0396 Mkms_3992
            MJL: Mjls_0375 Mjls_3933
            NFA: nfa24540(cysN2) nfa33920
            RHA: RHA1_ro01267(cysNC1) RHA1_ro01518(cysNC2)
            SCO: SCO6099(cysC)
            SMA: SAV2130(cysC1) SAV2312(cysC2)
            TFU: Tfu_0425
            FRA: Francci3_1339
            FAL: FRAAL2106(cysC) FRAAL2109(cysN)
            ACE: Acel_1619
            SEN: SACE_1473(cysN) SACE_3527 SACE_3531(cysN)
            RXY: Rxyl_0967 Rxyl_2355
            RBA: RB6049(cysC) RB7941(cysN)
            SYN: slr0676(cysC)
            SYW: SYNW2283(cysC)
            SYC: syc0603_c(cysC)
            SYF: Synpcc7942_0939
            SYD: Syncc9605_2420
            SYE: Syncc9902_2100
            SYG: sync_2636(cysC)
            SYR: SynRCC307_2267(cysC)
            SYX: SynWH7803_2302(cysC)
            CYA: CYA_1535(cysC)
            CYB: CYB_1417(cysC)
            TEL: tlr1341(cysC2) tlr2312(cysC1)
            GVI: gll0512(cysC)
            PMA: Pro0190(cysC)
            PMM: PMM0166(cysC)
            PMT: PMT2029(cysC)
            PMN: PMN2A_1533
            PMI: PMT9312_0168
            PMB: A9601_01841(cysC)
            PMC: P9515_01951(cysC)
            PMF: P9303_27091(cysC)
            PMG: P9301_01861(cysC)
            PMH: P9215_01841(cysC)
            PME: NATL1_02401(cysC)
            TER: Tery_1923 Tery_3968
            BTH: BT_0413
            BFR: BF1667
            BFS: BF1675(cysC)
            CHU: CHU_0637(cysC)
            CCH: Cag_0731
            PVI: Cvib_0631 Cvib_0635
            RRS: RoseRS_3336
            RCA: Rcas_4308
            DRA: DR_A0014
            DGE: Dgeo_1408
            AAE: aq_1081(cysD)
            PAB: PAB0781(cysC)
            RCI: RRC41(cysC)
            APE: APE_1195.1
            SMR: Smar_0339
            IHO: Igni_0968
            HBU: Hbut_1364
            PIS: Pisl_1509
            PAS: Pars_0345
STRUCTURES  PDB: 1D6J  1M7G  1M7H  1X6V  1XJQ  1XNJ  2AX4  2GKS  2OFW  2OFX  
                 2PEY  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.25
            ExPASy - ENZYME nomenclature database: 2.7.1.25
            ExplorEnz - The Enzyme Database: 2.7.1.25
            ERGO genome analysis and discovery system: 2.7.1.25
            BRENDA, the Enzyme Database: 2.7.1.25
            CAS: 9012-38-8
///
ENTRY       EC 2.7.1.26                 Enzyme
NAME        riboflavin kinase;
            flavokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:riboflavin 5'-phosphotransferase
REACTION    ATP + riboflavin = ADP + FMN [RN:R00549]
ALL_REAC    R00549
SUBSTRATE   ATP [CPD:C00002];
            riboflavin [CPD:C00255]
PRODUCT     ADP [CPD:C00008];
            FMN [CPD:C00061]
REFERENCE   1  [PMID:14284745]
  AUTHORS   CHASSY BM, ARSENIS C, MCCORMICK DB.
  TITLE     THE EFFECT OF THE LENGTH OF THE SIDE CHAIN OF FLAVINS ON REACTIVITY
            WITH FLAVOKINASE.
  JOURNAL   J. Biol. Chem. 240 (1965) 1338-40.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:13584303]
  AUTHORS   GIRI KV, KRISHNASWAMY PR, RAO NA.
  TITLE     Studies on plant flavokinase.
  JOURNAL   Biochem. J. 70 (1958) 66-71.
  ORGANISM  Phaseolus radiatus
REFERENCE   3  [PMID:14927668]
  AUTHORS   KEARNEY EB.
  TITLE     The interaction of yeast flavokinase with riboflavin analogues.
  JOURNAL   J. Biol. Chem. 194 (1952) 747-54.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4
  AUTHORS   McCormick, D.B. and Butler, R.C.
  TITLE     Substrate specificity of liver flavokinase.
  JOURNAL   Biochim. Biophys. Acta 65 (1962) 326-332.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:16183635]
  AUTHORS   Sandoval FJ, Roje S.
  TITLE     An FMN hydrolase is fused to a riboflavin kinase homolog in plants.
  JOURNAL   J. Biol. Chem. 280 (2005) 38337-45.
REFERENCE   6  [PMID:12693963]
  AUTHORS   Solovieva IM, Tarasov KV, Perumov DA.
  TITLE     Main physicochemical features of monofunctional flavokinase from
            Bacillus subtilis.
  JOURNAL   Biochemistry. (Mosc). 68 (2003) 177-81.
REFERENCE   7  [PMID:10206712]
  AUTHORS   Solovieva IM, Kreneva RA, Leak DJ, Perumov DA.
  TITLE     The ribR gene encodes a monofunctional riboflavin kinase which is
            involved in regulation of the Bacillus subtilis riboflavin operon.
  JOURNAL   Microbiology. 145 ( Pt 1) (1999) 67-73.
PATHWAY     PATH: map00740  Riboflavin metabolism
ORTHOLOGY   KO: K00861  riboflavin kinase
GENES       HSA: 55312(RFK)
            MMU: 54391(Rfk)
            CFA: 484159(RFK)
            GGA: 431449(RCJMB04_1k1)
            XLA: 379356(MGC52924) 447276(MGC86418)
            SPU: 584749(LOC584749)
            ATH: AT4G21470(ATFMN/FHY)
            CME: CMJ134C CMJ229C
            SCE: YDR236C(FMN1)
            AGO: AGOS_ABL109W
            PIC: PICST_50354(FMN1)
            SPO: SPCC18.16c
            ANI: AN7469.2
            AFM: AFUA_2G05820
            AOR: AO090001000701
            CNE: CNC05850
            UMA: UM04340.1
            PFA: MAL13P1.292
            TAN: TA20540
            TET: TTHERM_00171630
            TBR: Tb09.211.3420
            TCR: 510661.174 510741.80
            EHI: 193.t00007
            ECO: b0025(ribF)
            ECJ: JW0023(ribF)
            ECE: Z0029(ribF)
            ECS: ECs0028
            ECC: c0029(ribF)
            ECI: UTI89_C0027(ribF)
            ECP: ECP_0023
            ECV: APECO1_1958(ribF)
            ECW: EcE24377A_0025(ribF)
            ECX: EcHS_A0027(ribF)
            STY: STY0054(ribF)
            STT: t0047(ribF)
            SPT: SPA0046(ribF)
            SEC: SC0039(ribF)
            STM: STM0045(ribF)
            YPE: YPO0474(ribF)
            YPK: y3701(ribF)
            YPM: YP_3706(ribF)
            YPA: YPA_4067
            YPN: YPN_0346
            YPP: YPDSF_3158
            YPS: YPTB0616(ribF)
            YPI: YpsIP31758_3461(ribF)
            YEN: YE0615(b0025)
            SFL: SF0021(ribF)
            SFX: S0024(ribF)
            SFV: SFV_0019(ribF)
            SSN: SSON_0030(ribF)
            SBO: SBO_0024(ribF)
            SDY: SDY_0047(ribF)
            ECA: ECA3877(ribF)
            PLU: plu0590(ribF)
            BUC: BU150(ribF)
            BAS: BUsg143(ribF)
            WBR: WGLp295(ribF)
            SGL: SG0413
            ENT: Ent638_0583
            SPE: Spro_0697
            BFL: Bfl117(ribF)
            BPN: BPEN_121(ribF)
            HIN: HI0963(ribF)
            HIT: NTHI1136(ribF)
            HIP: CGSHiEE_07145
            HIQ: CGSHiGG_08395
            HDU: HD0273(ribF)
            HSO: HS_0188(ribF)
            PMU: PM1661(ribF)
            MSU: MS1752(ribF)
            APL: APL_0045(ribF)
            ASU: Asuc_1877
            XFA: XF2419
            XFT: PD1438(ribF)
            XCC: XCC1154(ribF)
            XCB: XC_3088
            XCV: XCV1289(ribF)
            XAC: XAC1253(ribF)
            XOO: XOO1625(ribF)
            XOM: XOO_1511(XOO1511)
            VCH: VC0681
            VCO: VC0395_A0213(ribF)
            VVU: VV1_0508
            VVY: VV0686
            VPA: VP0533
            VFI: VF0466
            PPR: PBPRA0590
            PAE: PA4561(ribF)
            PAU: PA14_60380(ribF)
            PAP: PSPA7_5201(ribF)
            PPU: PP_0602(ribF)
            PPF: Pput_0643
            PST: PSPTO_0805(ribF)
            PSB: Psyr_0709
            PSP: PSPPH_0720(ribF) PSPPH_4132(cysNC)
            PFL: PFL_5322(ribF)
            PFO: Pfl_4853
            PEN: PSEEN4693(ribF)
            PMY: Pmen_0952
            PAR: Psyc_1761(ribF)
            PCR: Pcryo_2042
            ACI: ACIAD0023(ribF)
            SON: SO_3533(ribF)
            SDN: Sden_2724
            SFR: Sfri_2891
            SAZ: Sama_0923
            SBL: Sbal_1053
            SLO: Shew_1098
            SPC: Sputcn32_1058
            SHE: Shewmr4_2958
            SHM: Shewmr7_3040
            SHN: Shewana3_3137
            SHW: Sputw3181_3107
            ILO: IL1129(ribF)
            CPS: CPS_1181(ribF)
            PHA: PSHAa0917(ribF)
            PAT: Patl_3179
            SDE: Sde_2567
            MAQ: Maqu_0861
            CBU: CBU_0391(ribF)
            CBD: COXBU7E912_1675(ribF)
            LPN: lpg0936(ribF)
            LPF: lpl0967(ribF)
            LPP: lpp0998(ribF)
            MCA: MCA2252(ribF)
            FTU: FTT0916c(ribF)
            FTF: FTF0916c(ribF)
            FTW: FTW_1263(ribF)
            FTL: FTL_0437
            FTH: FTH_0429(ribF)
            FTA: FTA_0459(ribF)
            FTN: FTN_0442(ribF)
            TCX: Tcr_0494
            NOC: Noc_2035
            AEH: Mlg_0851
            HHA: Hhal_1837
            HCH: HCH_05934(ribF)
            CSA: Csal_0480
            ABO: ABO_0458(ribF)
            MMW: Mmwyl1_4231
            AHA: AHA_0681(ribF)
            DNO: DNO_0082(ribF)
            BCI: BCI_0555(ribF)
            RMA: Rmag_0016
            VOK: COSY_0016(ribF)
            NME: NMB1834
            NMA: NMA0621(ribF)
            NMC: NMC0382(ribF)
            NGO: NGO0068
            CVI: CV_3570(ribF)
            RSO: RSc2457(ribF)
            REU: Reut_A2744
            RME: Rmet_2884
            BMA: BMA2241(ribF)
            BMV: BMASAVP1_A2657(ribF)
            BML: BMA10299_A1032(ribF)
            BMN: BMA10247_2111(ribF)
            BXE: Bxe_A0808
            BUR: Bcep18194_A5843
            BAM: Bamb_2558
            BPS: BPSL0907
            BPM: BURPS1710b_1124(ribF)
            BPL: BURPS1106A_0972(bimA)
            BPD: BURPS668_0968(bimA)
            BTE: BTH_I0771(ribF)
            PNU: Pnuc_1739
            BPE: BP1754(ribF)
            BPA: BPP1985(ribF)
            BBR: BB2173(ribF)
            RFR: Rfer_1433
            POL: Bpro_3848
            MPT: Mpe_A3045
            HAR: HEAR0846(ribF)
            MMS: mma_0829(ribF)
            NEU: NE1150(ribF)
            NET: Neut_1440
            NMU: Nmul_A2653(ribF)
            EBA: ebA4449(ribF)
            AZO: azo1206(ribF)
            DAR: Daro_3047
            TBD: Tbd_1856
            MFA: Mfla_2209
            HPY: HP1087(ribC)
            HPJ: jhp0338(ribF)
            HPA: HPAG1_0360
            HHE: HH0518(ribF)
            HAC: Hac_0795(ribC)
            WSU: WS0586(ribF)
            TDN: Tmden_1341
            CJE: Cj0589(ribF)
            CJR: CJE0692
            CJU: C8J_0551(ribF)
            CFF: CFF8240_1110(ribF)
            CCV: CCV52592_1563(ribF)
            CHA: CHAB381_1014(ribF)
            CCO: CCC13826_2025(ribF)
            ABU: Abu_1836(ribF)
            NIS: NIS_1131(ribF)
            SUN: SUN_0463(ribF)
            GSU: GSU1487(ribF)
            GME: Gmet_1388
            PCA: Pcar_2151(ribF)
            DVU: DVU0450(ribF)
            DDE: Dde_3505(ribF)
            LIP: LI0709(ribF)
            BBA: Bd1507(ribC)
            DPS: DP1094
            ADE: Adeh_0621
            SAT: SYN_01948
            SFU: Sfum_3182
            WOL: WD0759(ribF)
            WBM: Wbm0416
            AMA: AM1082(ribF)
            APH: APH_1161(ribF)
            ERU: Erum8130(ribF)
            ERW: ERWE_CDS_08610(ribF)
            ERG: ERGA_CDS_08520(ribF)
            ECN: Ecaj_0853
            ECH: ECH_1061(ribF)
            NSE: NSE_0040(ribF)
            PUB: SAR11_0159(ribF)
            MLO: mlr8243
            MES: Meso_0424
            SME: SMc00909(ribF)
            ATU: Atu0685(ribF)
            ATC: AGR_C_1228
            RET: RHE_CH00831(ribF)
            RLE: RL0886(ribF)
            BME: BMEII1044
            BMF: BAB2_0193
            BMS: BRA0201(ribF)
            BMB: BruAb2_0196(ribF)
            BOV: BOV_A0180(ribF)
            BJA: blr7480(ribF)
            BRA: BRADO6066(ribF)
            BBT: BBta_1717(ribF)
            RPA: RPA4379(ribF)
            RPB: RPB_4186(ribF)
            RPC: RPC_1399
            RPD: RPD_4040
            RPE: RPE_1410
            NWI: Nwi_2541
            NHA: Nham_3161
            BHE: BH13220(ribF)
            BQU: BQ10470(ribF)
            BBK: BARBAKC583_1163(ribF)
            CCR: CC_0703(ribF)
            SIL: SPO3154(ribF)
            SIT: TM1040_2071
            RSP: RSP_2304(ribF)
            JAN: Jann_3365
            RDE: RD1_3523(ribF)
            PDE: Pden_3662
            MMR: Mmar10_0612
            HNE: HNE_0844(ribF)
            ZMO: ZMO0322(ribF)
            NAR: Saro_3260
            SAL: Sala_2358
            ELI: ELI_13560
            GOX: GOX1245
            GBE: GbCGDNIH1_0467
            ACR: Acry_0583
            RRU: Rru_A2965
            MAG: amb0832
            MGM: Mmc1_2148
            ABA: Acid345_2631
            BSU: BG11495(ribC)
            BHA: BH2409(ribC)
            BAN: BA3946(ribC)
            BAR: GBAA3946(ribC)
            BAA: BA_4417
            BAT: BAS3660(ribC)
            BCE: BC3807
            BCA: BCE_2150 BCE_3847(ribC)
            BCZ: BCZK3568(ribC)
            BTK: BT9727_3550(ribC)
            BLI: BL01220(ribC)
            BLD: BLi01892(ribC)
            BCL: ABC2224(ribC)
            BAY: RBAM_016510(ribC)
            BPU: BPUM_1570(ribC)
            OIH: OB1602(ribC) OB2871
            GKA: GK1267
            SAU: SA1115(ribC)
            SAV: SAV1272(ribC)
            SAM: MW1155(ribC)
            SAR: SAR1248
            SAS: SAS1206
            SAC: SACOL1291(ribF)
            SAB: SAB1134(ribC)
            SAA: SAUSA300_1165(ribF)
            SAO: SAOUHSC_01249
            SEP: SE0949
            SER: SERP0839(ribF)
            SHA: SH1641(ribC)
            SSP: SSP1493
            LMO: lmo1329(ribC)
            LMF: LMOf2365_1346(ribF)
            LIN: lin1366(ribC)
            LWE: lwe1344(ribF)
            LLA: L0167(ribC)
            LLC: LACR_1238
            SPY: SPy_1250(mreA)
            SPZ: M5005_Spy_0960(mreA)
            SPM: spyM18_1199
            SPG: SpyM3_0886(mreA)
            SPS: SPs1086
            SPH: MGAS10270_Spy1075(mreA)
            SPI: MGAS10750_Spy1111(mreA)
            SPJ: MGAS2096_Spy1020(mreA)
            SPK: MGAS9429_Spy1064(mreA)
            SPF: SpyM50838(ribC)
            SPA: M6_Spy0950
            SPB: M28_Spy0933(mreA)
            SPN: SP_1110
            SPR: spr1017(mreA)
            SPD: SPD_0994(ribF)
            SAG: SAG0997(ribF)
            SAN: gbs1032
            SAK: SAK_1092(ribF)
            SMU: SMU.1143c
            STC: str0996(ribC)
            STL: stu0996(ribC)
            SSA: SSA_0936(mreA)
            LPL: lp_0850(ribC1) lp_2031(ribC2)
            LJO: LJ1484
            LAC: LBA1252(ribC)
            LSA: LSA1241
            LSL: LSL_0575(ribF)
            LDB: Ldb1316(ribC)
            LBU: LBUL_1230
            LBR: LVIS_1332
            LCA: LSEI_1569
            EFA: EF1295(ribF)
            OOE: OEOE_1312
            STH: STH1526
            CAC: CAC1806
            CPE: CPE1682(ribC)
            CPF: CPF_1936(ribF)
            CPR: CPR_1654(ribF)
            CTC: CTC01279
            CBA: CLB_2278(ribF)
            CBH: CLC_2261(ribF)
            CBF: CLI_2470(ribF)
            CHY: CHY_1762(ribF)
            DSY: DSY2513(ribF)
            SWO: Swol_0904
            TTE: TTE1389(ribF)
            MTA: Moth_1054(ribF)
            MGE: MG_145
            MPN: MPN158(yaaC)
            MPU: MYPU_5480(ribF)
            MPE: MYPE9310
            MMY: MSC_0106(ribC) MSC_0337(ribF)
            MMO: MMOB4680(ribF)
            MHY: mhp102(ribF)
            MHJ: MHJ_0270
            MHP: MHP7448_0278
            MSY: MS53_0563(ribF)
            MCP: MCAP_0061 MCAP_0327
            UUR: UU355(ribF)
            MFL: Mfl283 Mfl334
            MTU: Rv2786c(ribF)
            MTC: MT2856(ribF)
            MBO: Mb2809c(ribF)
            MBB: BCG_2804c(ribF)
            MLE: ML0852(ribF)
            MPA: MAP2893c(ribF)
            MAV: MAV_1437(cysNC) MAV_3678(ribF)
            MSM: MSMEG_2653(ribF) MSMEG_4978(cysNC)
            MMC: Mmcs_2098
            CGL: NCgl1903(cgl1978)
            CGB: cg2169(ribF)
            CEF: CE1871(ribF)
            CDI: DIP1470(ribF)
            CJK: jk1136(ribF)
            NFA: nfa38900(ribF)
            RHA: RHA1_ro06653(ribF)
            SCO: SCO5711(SC9F2.05c)
            SMA: SAV2546(ribF)
            TWH: TWT581(ribF)
            TWS: TW180(ribF)
            LXX: Lxx07280(ribF)
            PAC: PPA1474
            TFU: Tfu_0782
            FRA: Francci3_3557(ribF)
            FAL: FRAAL5755(ribF)
            SEN: SACE_5918(ribF)
            BLO: BL1619(ribF)
            BAD: BAD_0357(ribF)
            FNU: FN0707
            RBA: RB8286(ribF)
            CTR: CT093(ribF)
            CTA: CTA_0098(ribF)
            CMU: TC0368
            CPN: CPn0320(ribF)
            CPA: CP0437
            CPJ: CPj0320(ribF)
            CPT: CpB0331(ribC)
            CCA: CCA00462(ribF)
            CAB: CAB448(ribF)
            CFE: CF0545(ribF)
            PCU: pc0758(ribF)
            TPA: TP0888
            TDE: TDE0073
            LIL: LA3449(ribF)
            LIC: LIC10728(ribF)
            LBJ: LBJ_0645(ribF)
            LBL: LBL_2434(ribF)
            SYN: slr1882(ribF)
            SYW: SYNW1603(ribF)
            SYC: syc1028_d
            SYF: Synpcc7942_0492
            SYD: Syncc9605_0897
            SYE: Syncc9902_1501
            SYG: sync_0793(ribF)
            SYX: SynWH7803_1715(ribF)
            CYA: CYA_2407(ribF)
            CYB: CYB_2202(ribF)
            TEL: tll1556(ribF)
            GVI: gll0217(ribF)
            ANA: alr4848
            AVA: Ava_2118
            PMA: Pro1347(ribF)
            PMM: PMM1273(ribF)
            PMT: PMT0364(ribF)
            PMN: PMN2A_0839
            PMI: PMT9312_1367
            PMB: A9601_14721(ribF)
            PMC: P9515_14341(ribF)
            PMF: P9303_19371(ribF)
            PMG: P9301_14581(ribF)
            PMH: P9215_14981(ribF)
            PME: NATL1_16921(ribF)
            TER: Tery_1864
            BTH: BT_2543(ribF)
            BFR: BF4346
            BFS: BF4147(ribF)
            PGI: PG0957(ribF)
            SRU: SRU_1775(ribF)
            CHU: CHU_0947(ribF)
            GFO: GFO_3504(ribF)
            FPS: FP0233(ribF)
            CTE: CT0244(ribF)
            CCH: Cag_1459
            PLT: Plut_1776
            DET: DET0602(ribF)
            DEH: cbdb_A584(ribF)
            DRA: DR_1008
            DGE: Dgeo_1809
            TTH: TTC0159
            TTJ: TTHA0527
            AAE: aq_139(ribF)
            TMA: TM0857
STRUCTURES  PDB: 1N05  1N06  1N07  1N08  1NB0  1NB9  1P4M  1Q9S  2P3M  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.26
            ExPASy - ENZYME nomenclature database: 2.7.1.26
            ExplorEnz - The Enzyme Database: 2.7.1.26
            ERGO genome analysis and discovery system: 2.7.1.26
            BRENDA, the Enzyme Database: 2.7.1.26
            CAS: 9032-82-0
///
ENTRY       EC 2.7.1.27                 Enzyme
NAME        erythritol kinase;
            erythritol kinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:erythritol 4-phosphotransferase
REACTION    ATP + erythritol = ADP + D-erythritol 4-phosphate [RN:R02430]
ALL_REAC    R02430
SUBSTRATE   ATP [CPD:C00002];
            erythritol [CPD:C00503]
PRODUCT     ADP [CPD:C00008];
            D-erythritol 4-phosphate [CPD:C03494]
REFERENCE   1  [PMID:13908588]
  AUTHORS   HOLTEN D, FROMM HJ.
  TITLE     Purification and properties of erythritol kinase from
            Propionibacterium pentosaceum.
  JOURNAL   J. Biol. Chem. 236 (1961) 2581-4.
  ORGANISM  Propionibacterium pentosaceum
REFERENCE   2  [PMID:13908588]
  AUTHORS   HOLTEN D, FROMM HJ.
  TITLE     Purification and properties of erythritol kinase from
            Propionibacterium pentosaceum.
  JOURNAL   J. Biol. Chem. 236 (1961) 2581-4.
  ORGANISM  Propionibacterium pentosaceum
ORTHOLOGY   KO: K00862  erythritol kinase
GENES       SME: SMc01623(eriA)
            RLE: pRL120204(eryA)
            BME: BMEII0430
            BMF: BAB2_0372(eryA)
            BMB: BruAb2_0368(eryA)
            RDE: RD1_3634
            SEN: SACE_5218(eryA) SACE_6531(eryA)
STRUCTURES  PDB: 1V5S  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.27
            ExPASy - ENZYME nomenclature database: 2.7.1.27
            ExplorEnz - The Enzyme Database: 2.7.1.27
            ERGO genome analysis and discovery system: 2.7.1.27
            BRENDA, the Enzyme Database: 2.7.1.27
            CAS: 9030-64-2
///
ENTRY       EC 2.7.1.28                 Enzyme
NAME        triokinase;
            triose kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-glyceraldehyde 3-phosphotransferase
REACTION    ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate
            [RN:R01059]
ALL_REAC    R01059
SUBSTRATE   ATP [CPD:C00002];
            D-glyceraldehyde [CPD:C00577]
PRODUCT     ADP [CPD:C00008];
            D-glyceraldehyde 3-phosphate [CPD:C00118]
REFERENCE   1  [PMID:13093749]
  AUTHORS   HERS HG, KUSAKA T.
  TITLE     [The metabolism of fructose-1-phosphate in the liver.]
  JOURNAL   Biochim. Biophys. Acta. 11 (1953) 427-37.
REFERENCE   2  [PMID:5823111]
  AUTHORS   Sillero MA, Sillero A, Sols A.
  TITLE     Enzymes involved in fructose metabolism in lir and the
            glyceraldehyde metabolic crossroads.
  JOURNAL   Eur. J. Biochem. 10 (1969) 345-50.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.28
            ExPASy - ENZYME nomenclature database: 2.7.1.28
            ExplorEnz - The Enzyme Database: 2.7.1.28
            ERGO genome analysis and discovery system: 2.7.1.28
            BRENDA, the Enzyme Database: 2.7.1.28
            CAS: 9030-65-3
///
ENTRY       EC 2.7.1.29                 Enzyme
NAME        glycerone kinase;
            dihydroxyacetone kinase;
            acetol kinase;
            acetol kinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:glycerone phosphotransferase
REACTION    ATP + glycerone = ADP + glycerone phosphate [RN:R01011]
ALL_REAC    R01011
SUBSTRATE   ATP [CPD:C00002];
            glycerone [CPD:C00184]
PRODUCT     ADP [CPD:C00008];
            glycerone phosphate [CPD:C00111]
REFERENCE   1
  AUTHORS   Sellinger, O.Z. and Miller, O.N.
  TITLE     Phosphorylation of acetol by homogenates of rat liver.
  JOURNAL   Fed. Proc. 16 (1957) 245-246.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00561  Glycerolipid metabolism
ORTHOLOGY   KO: K00863  dihydroxyacetone kinase
GENES       HSA: 26007(DAK)
            PTR: 466626(DAK)
            MMU: 225913(Dak)
            RNO: 361730(RGD1311026)
            BTA: 512373(DAK)
            GGA: 426629(DAK)
            SCE: YFL053W(DAK2) YML070W(DAK1)
            AGO: AGOS_AER139C
            PIC: PICST_31117(DAK1.1) PICST_53027(DAK1.2) PICST_57462(DAK2)
            CGR: CAGL0L11374g
            SPO: SPAC22A12.11 SPAC977.16c(dak2)
            ANI: AN0034.2
            AFM: AFUA_5G12690
            AOR: AO090120000396
            UMA: UM00109.1
            TET: TTHERM_00038820
            LMA: LmjF10.0420
            YPP: YPDSF_3011
            ECA: ECA0866
            ENT: Ent638_3653
            SPE: Spro_4272
            ASU: Asuc_1441 Asuc_1586
            CSA: Csal_2326
            BMA: BMA1001(dak)
            BXE: Bxe_B2559
            BVI: Bcep1808_5455
            BUR: Bcep18194_C7717
            BCN: Bcen_5792
            BCH: Bcen2424_6157
            BAM: Bamb_6032
            BPS: BPSL1613
            BPM: BURPS1710b_2248(dak)
            BPL: BURPS1106A_A0365(dhaK) BURPS1106A_A0366(dhaL)
            BTE: BTH_I2329
            POL: Bpro_0697 Bpro_0706 Bpro_1459
            VEI: Veis_2047
            NET: Neut_1377
            NMU: Nmul_A2726
            DVL: Dvul_2009
            MXA: MXAN_0618
            MLO: mlr9018
            SME: SMb20767(dak)
            SMD: Smed_3823 Smed_3825 Smed_4228
            ATU: Atu3543(dhbK)
            ATC: AGR_L_2580
            RET: RHE_CH02988(dak) RHE_PA00021
            RLE: RL1752(dhaL2) RL2900(dhaK)
            BME: BMEI0399
            BMB: BruAb1_1613
            OAN: Oant_3102 Oant_4069 Oant_4071 Oant_4368
            BRA: BRADO4614(dhaL)
            RDE: RD1_3614 RD1_3702 RD1_3889
            GOX: GOX2222
            ACR: Acry_2616
            BHA: BH3393
            BAN: BA0963 BA0965
            BAR: GBAA0963 GBAA0965
            BAA: BA_1538(dak1) BA_1540(dak1)
            BAT: BAS0905 BAS0907
            BCE: BC0979 BC0981
            BCA: BCE_1052 BCE_1054
            BCZ: BCZK0868(dhaL) BCZK0870(dhaL) BCZK0873(dhaL) BCZK3615(dhaK)
            BCY: Bcer98_0787
            BTK: BT9727_0887(dhaL) BT9727_0889(dhaL)
            BTL: BALH_0870 BALH_0875
            SAJ: SaurJH9_0673
            SAH: SaurJH1_0688
            LWE: lwe1833
            LLC: LACR_0250
            LLM: llmg_0255(dhaK) llmg_0257(dhaM)
            SPZ: M5005_Spy_0431
            SPH: MGAS10270_Spy0432
            SPI: MGAS10750_Spy0445
            SPJ: MGAS2096_Spy0450
            SPK: MGAS9429_Spy0430
            SPA: M6_Spy0458 M6_Spy0459
            SPB: M28_Spy0419
            SSA: SSA_0049 SSA_0050
            LPL: lp_0166(dak1A)
            LSL: LSL_1634(dAK)
            CPE: CPE0100
            CPF: CPF_0095
            CPR: CPR_1160
            CBO: CBO0975(dhaK)
            CBA: CLB_1015(dhaKL)
            CBH: CLC_1029(dhaKL)
            CBF: CLI_1061(dhaKL)
            CBE: Cbei_2148
            AMT: Amet_4114
            MSM: MSMEG_3271
            MMC: Mmcs_2560 Mmcs_5133
            MKM: Mkms_2605 Mkms_5222
            MJL: Mjls_2599 Mjls_5514
            RHA: RHA1_ro01844
            SCO: SCO0580(SCF55.04c)
            CMI: CMM_0788(dakA)
            ART: Arth_0172 Arth_0884 Arth_3953
            AAU: AAur_0173(dhaK)
            PAC: PPA0622
            NCA: Noca_3316
            TFU: Tfu_1716
            KRA: Krad_1919 Krad_4000
            SEN: SACE_4765(dak) SACE_5217(dak) SACE_6248
            RXY: Rxyl_1064
            RRS: RoseRS_1766 RoseRS_3297
            RCA: Rcas_2044 Rcas_4109
STRUCTURES  PDB: 1OI2  1OI3  1UN8  1UN9  1UOD  1UOE  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.29
            ExPASy - ENZYME nomenclature database: 2.7.1.29
            ExplorEnz - The Enzyme Database: 2.7.1.29
            ERGO genome analysis and discovery system: 2.7.1.29
            BRENDA, the Enzyme Database: 2.7.1.29
            CAS: 9027-47-8
///
ENTRY       EC 2.7.1.30                 Enzyme
NAME        glycerol kinase;
            glycerokinase;
            GK;
            ATP:glycerol-3-phosphotransferase;
            glycerol kinase (phosphorylating);
            glyceric kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:glycerol 3-phosphotransferase
REACTION    ATP + glycerol = ADP + sn-glycerol 3-phosphate [RN:R00847]
ALL_REAC    R00847
SUBSTRATE   ATP [CPD:C00002];
            glycerol [CPD:C00116]
PRODUCT     ADP [CPD:C00008];
            sn-glycerol 3-phosphate [CPD:C00093]
COMMENT     Glycerone and L-glyceraldehyde can act as acceptors; UTP (and, in
            the case of the yeast enzyme, ITP and GTP) can act as donors.
REFERENCE   1
  AUTHORS   Bergmeyer, H.-U., Holz, G., Kauder, E.M., Mollering, H. and Wieland,
            O.
  TITLE     Kristallisierte Glycerokinase aus Candida mycoderma.
  JOURNAL   Biochem. Z. 333 (1961) 471-480.
  ORGANISM  Candida mycoderma
REFERENCE   2
  AUTHORS   Bublitz, C. and Kennedy, E.P.
  TITLE     Synthesis of phosphatides in isolated mitochondria. III. The
            enzymatic phosphorylation of glycerol.
  JOURNAL   J. Biol. Chem. 211 (1955) 951-961.
REFERENCE   3
  AUTHORS   Wieland, O. and Suyter, M.
  TITLE     Glycerokinase: Isolierung und Eigenschaften des Enzyms.
  JOURNAL   Biochem. Z. 329 (1957) 320-331.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00561  Glycerolipid metabolism
            PATH: map03320  PPAR signaling pathway
ORTHOLOGY   KO: K00864  glycerol kinase
GENES       HSA: 2710(GK) 2712(GK2)
            PTR: 471192(GK2)
            MMU: 14626(Gk2) 14933(Gyk)
            RNO: 79223(Gyk)
            CFA: 478448(GK2)
            BTA: 505987(GK) 538702(LOC538702)
            GGA: 418589(GK)
            XLA: 380332(gk2)
            SPU: 580504(LOC580504)
            DME: Dmel_CG1216(mri) Dmel_CG18374(Gyk) Dmel_CG7995
            CEL: R11F4.1
            OSA: 4337206
            CME: CMJ173C
            SCE: YHL032C(GUT1)
            AGO: AGOS_ACL069C
            PIC: PICST_66162(GUT1)
            CGR: CAGL0E03916g
            ANI: AN3916.2 AN5589.2
            AFM: AFUA_4G11540 AFUA_6G08470
            AOR: AO090001000509 AO090003001067
            CNE: CND02800
            UMA: UM04659.1
            DDI: DDBDRAFT_0218222
            PFA: PF13_0269
            TAN: TA14775
            TPV: TP02_0725
            TET: TTHERM_00224620
            TBR: Tb09.211.3540 Tb09.211.3550 Tb09.211.3560 Tb09.211.3570
                 Tb09.211.3590
            TCR: 510661.60
            LMA: LmjF35.3080
            EHI: 34.t00011
            ECO: b3926(glpK)
            ECJ: JW3897(glpK)
            ECE: Z5471(glpK)
            ECS: ECs4851
            ECC: c4878(glpK)
            ECI: UTI89_C4510(glpK)
            ECP: ECP_4135
            ECV: APECO1_2543(glpK)
            ECW: EcE24377A_4460(glpK)
            ECX: EcHS_A4157(glpK)
            STY: STY3784(glpK)
            STT: t3532(glpK)
            SPT: SPA3929(glpK)
            SEC: SC3975(glpK)
            STM: STM4086(glpK)
            YPE: YPO3312
            YPK: y0047(glpK) y0876(glpK)
            YPM: YP_0094(glpK1) YP_0374(glpK2)
            YPA: YPA_2832 YPA_3451
            YPN: YPN_0781 YPN_3758
            YPP: YPDSF_3813
            YPS: YPTB0086(glpK) YPTB0818
            YPI: YpsIP31758_0101(glpK)
            YEN: YE0099(glpK)
            SFL: SF4004(glpK)
            SFX: S3743(glpK)
            SFV: SFV_3997(glpK)
            SSN: SSON_4095(glpK)
            SBO: SBO_3943(glpK)
            SDY: SDY_3818(glpK)
            ECA: ECA1952 ECA4267(glpK)
            PLU: plu4768(glpK)
            SGL: SG2172
            ENT: Ent638_4047
            KPN: KPN_04011(glpK)
            HIN: HI0691(glpK)
            HIT: NTHI0813(glpK)
            HIQ: CGSHiGG_06745(glpK)
            PMU: PM1446(glpK)
            MSU: MS1988(glpK)
            APL: APL_0375(glpK)
            XFA: XF2268
            XFT: PD1304(glpK)
            XCC: XCC0358(glpK)
            XCB: XC_0370
            XCV: XCV0372(glpK)
            XAC: XAC0358(glpK)
            VCH: VCA0744
            VCO: VC0395_0682(gplK)
            VVU: VV1_1787
            VVY: VV2624
            VPA: VP2386
            VFI: VFA0236
            PPR: PBPRA0248
            PAE: PA1487 PA3579 PA3582(glpK)
            PAU: PA14_17960(glpK) PA14_18010(glpK) PA14_45190
            PAP: PSPA7_1561(glpK2) PSPA7_1564(glpK1)
            PPU: PP_1075(glpK)
            PST: PSPTO_2403 PSPTO_4168(glpK)
            PSB: Psyr_3905
            PSP: PSPPH_3899(glpK)
            PFL: PFL_0499 PFL_4868(glpK)
            PFO: Pfl_4532
            PEN: PSEEN1197(glpK)
            PAR: Psyc_1332
            PCR: Pcryo_1041
            ACI: ACIAD0930(glpK)
            SON: SO_4230(glpK)
            SDN: Sden_0342
            SFR: Sfri_3815
            SPC: Sputcn32_0476
            SHE: Shewmr4_3583
            SHM: Shewmr7_0373
            SHN: Shewana3_3756
            SHW: Sputw3181_0379
            PHA: PSHAa0190(glpK) PSHAb0551(glpK)
            PAT: Patl_3533
            SDE: Sde_1480
            PIN: Ping_3168
            CBU: CBU_0932(gplK)
            CBD: COXBU7E912_1141(glpK)
            LPN: lpg1414
            LPF: lpl1365(glpK)
            LPP: lpp1369(glpK)
            FTU: FTT0130(glpK)
            FTF: FTF0130(glpK)
            FTW: FTW_0219(glpK)
            FTL: FTL_1644
            FTH: FTH_1588(glpK)
            FTA: FTA_1739(glpK)
            FTN: FTN_1585(glpK)
            NOC: Noc_2698
            AEH: Mlg_1315
            HHA: Hhal_0078
            HCH: HCH_06965(glpK)
            CSA: Csal_2104
            ABO: ABO_0714(glpK)
            AHA: AHA_1648(glpK)
            DNO: DNO_0213(glpK)
            CVI: CV_0251(glpK)
            RSO: RSc3052(glpK)
            REU: Reut_A2213
            REH: H16_A2507 H16_B1199
            RME: Rmet_2238 Rmet_5445
            BMA: BMA0240(glpK)
            BMV: BMASAVP1_A2706(glpK)
            BML: BMA10299_A2371(glpK)
            BMN: BMA10247_2452(glpK)
            BXE: Bxe_A0638
            BUR: Bcep18194_A6006(glpK) Bcep18194_B2082
            BCN: Bcen_2067
            BCH: Bcen2424_2678
            BAM: Bamb_2731
            BPS: BPSL0687(glpK)
            BPM: BURPS1710b_0906(glpK)
            BPL: BURPS1106A_0739(glpK)
            BPD: BURPS668_0725(glpK)
            BTE: BTH_I0599(glpK)
            BPE: BP3825(glpK)
            BPA: BPP3969(glpK)
            BBR: BB4442(glpK)
            RFR: Rfer_3678
            POL: Bpro_0476
            MPT: Mpe_A3665
            HAR: HEAR0215(glpK)
            MMS: mma_0268(glpK)
            NEU: NE2128 NE2129
            NET: Neut_2080
            EBA: ebA4462(glpK)
            AZO: azo2751(glpK)
            DAR: Daro_1922
            GSU: GSU2762(glpK)
            GME: Gmet_1676
            DVU: DVU3134(glpK)
            DDE: Dde_0410
            BBA: Bd2718(glpK)
            ADE: Adeh_3457
            MXA: MXAN_6771(glpK)
            MLO: mll0700
            MES: Meso_1598
            SME: SMb21009(glpK)
            ATU: Atu1903(glpK) Atu3890(glpK)
            ATC: AGR_C_3493 AGR_L_1914
            RET: RHE_CH02396(glpKch1) RHE_CH03122(glpKch2) RHE_PB00026(glpKb)
            RLE: RL2717(glpK) RL3568(glpK) pRL90081(glpK)
            BME: BMEII0823 BMEII0824
            BMF: BAB2_0796(glpK) BAB2_0797
            BMS: BRA0443(glpK)
            BOV: BOV_A0386(glpK)
            BJA: blr1410(glpK)
            BRA: BRADO0987(glpK)
            BBT: BBta_7067(glpK)
            RPA: RPA3705(glpK)
            RPB: RPB_1763
            RPC: RPC_2231
            RPD: RPD_3544
            RPE: RPE_3774
            NWI: Nwi_0281
            NHA: Nham_0360
            CCR: CC_1223
            SIL: SPO0104(glpK)
            SIT: TM1040_3440
            RSP: RSP_2662(glpK)
            JAN: Jann_3683
            RDE: RD1_2883(glpK)
            MMR: Mmar10_2621
            HNE: HNE_1335(glpK)
            NAR: Saro_0084
            SAL: Sala_1948
            ELI: ELI_00480
            GOX: GOX2090
            RRU: Rru_A2009 Rru_A3461
            ABA: Acid345_2987
            BSU: BG10187(glpK)
            BHA: BH1093(glpK)
            BAN: BA1026(glpK)
            BAR: GBAA1026(glpK)
            BAA: BA_1586
            BAT: BAS0960
            BCE: BC1035
            BCA: BCE_1125(glpK)
            BCZ: BCZK0938(glpK)
            BTK: BT9727_0947(glpK)
            BTL: BALH_0918
            BLI: BL02903(glpK)
            BLD: BLi00995(glpK)
            BCL: ABC1256(glpK) ABC3384(glpK)
            BAY: RBAM_009550(glpK)
            BPU: BPUM_0883(glpK)
            OIH: OB2475
            GKA: GK1360
            GTN: GTNG_1216(glpK)
            SAU: SA1141(glpK)
            SAV: SAV1301(glpK)
            SAM: MW1183(glpK)
            SAR: SAR1275(glpK)
            SAS: SAS1233
            SAC: SACOL1320(glpK)
            SAB: SAB1161(glpK)
            SAA: SAUSA300_1192(glpK)
            SAO: SAOUHSC_01276
            SEP: SE0978
            SER: SERP0867(glpK)
            SHA: SH1609(glpD)
            SSP: SSP1460
            LMO: lmo1034 lmo1538
            LMF: LMOf2365_1055(glpK-1) LMOf2365_1557(glpK-2)
            LIN: lin1573
            LWE: lwe1551(glpK)
            LLA: L0014(glpK)
            LLC: LACR_1485
            LLM: llmg_1099(glpK)
            SPY: SPy_1684(glpK)
            SPZ: M5005_Spy_1381(glpK)
            SPM: spyM18_1696(glpK)
            SPG: SpyM3_1468(glpK)
            SPS: SPs0398
            SPH: MGAS10270_Spy1499(glpK)
            SPI: MGAS10750_Spy1492(glpK)
            SPJ: MGAS2096_Spy1404(glpK)
            SPK: MGAS9429_Spy1379(glpK)
            SPF: SpyM50409(glpK)
            SPA: M6_Spy1429
            SPB: M28_Spy1424(glpK)
            SPN: SP_2186
            SPR: spr1991(glpK)
            SPD: SPD_2013(glpK)
            SAG: SAG0273(glpK)
            SAN: gbs0263(glpK)
            SAK: SAK_0345(glpK)
            SSA: SSA_1826(glpK)
            SGO: SGO_0632(glpK)
            LPL: lp_0370(glpK1) lp_0834(glpK2)
            LJO: LJ1268
            LAC: LBA1492(glpK) LBA1878(glpK)
            LSA: LSA0649(glpK)
            LSL: LSL_0110(glpK)
            LBU: LBUL_1941
            LBR: LVIS_0238 LVIS_0897
            LCA: LSEI_0662 LSEI_2657
            EFA: EF1929(glpK)
            STH: STH1195
            CAC: CAC1321(glpK)
            CPE: CPE2552(glpK)
            CPF: CPF_2876(glpK)
            CPR: CPR_2559(glpK)
            CTC: CTC01758 CTC02462
            CNO: NT01CX_0605(glpK) NT01CX_0608(glpK)
            CDF: CD0741(glpK1) CD1382(glpK2)
            CBO: CBO2784(glpK)
            CBA: CLB_2727(glpK)
            CBH: CLC_2660(glpK)
            CBF: CLI_2834(glpK)
            CHY: CHY_1839(glpK)
            DSY: DSY4810
            DRM: Dred_2845
            TTE: TTE2002(glpK)
            MGE: MG_038(glpK)
            MPN: MPN050(glpK)
            MPU: MYPU_2210(glpK)
            MPE: MYPE6360(glpK)
            MGA: MGA_0644(glpK)
            MMY: MSC_0258(glpK)
            MMO: MMOB2940(glpK)
            MHY: mhp370(glpK)
            MHJ: MHJ_0355(glpK)
            MHP: MHP7448_0359(glpK)
            MCP: MCAP_0218(glpK)
            MTU: Rv3696c(glpK)
            MTC: MT3798(glpK)
            MBO: Mb3721c(glpKb) Mb3722c(glpKa)
            MBB: BCG_3755c(glpK)
            MLE: ML2314(glpK)
            MPA: MAP0353(glpK)
            MAV: MAV_0406(glpK)
            MSM: MSMEG_6229(glpK) MSMEG_6756(glpK) MSMEG_6759(glpK)
            MMC: Mmcs_4873
            CGL: NCgl2790(glpK)
            CGB: cg3198(glpK)
            CEF: CE2721
            CDI: DIP2235(glpK)
            CJK: jk1671(glpK)
            NFA: nfa9710(glpK)
            RHA: RHA1_ro06264
            SCO: SCO0509(glpK2) SCO1660(glpK)
            SMA: SAV6664(glpK1) SAV6963(glpK2) SAV7201(glpK3)
            LXX: Lxx04420(glpK)
            CMI: CMM_1831(glpK)
            AAU: AAur_2247(glpK)
            PAC: PPA2304
            TFU: Tfu_0787
            FRA: Francci3_1657
            FAL: FRAAL4566(glpK)
            SEN: SACE_6518(glpK)
            RXY: Rxyl_1063
            FNU: FN1839
            RBA: RB3762(glpK)
            BGA: BG0244(glpK)
            BAF: BAPKO_0250(glpK)
            TDE: TDE1916(glpK)
            LIL: LA2119(glpK1) LA3565(glpK2)
            LIC: LIC10629(glpK2) LIC11799(glpK)
            LBJ: LBJ_0524(glpK-2) LBJ_1891(glpK-1)
            LBL: LBL_1393(glpK-1) LBL_2555(glpK-2)
            SYN: slr1672(glpK)
            SYW: SYNW1953
            SYD: Syncc9605_0500
            SYE: Syncc9902_1835
            SYG: sync_0569(glpK)
            SYR: SynRCC307_1382(glpK)
            SYX: SynWH7803_0547(glpK)
            GVI: gll1751(glpK)
            ANA: all1811
            AVA: Ava_4817
            TER: Tery_3810
            SRU: SRU_1471(glpK)
            CTE: CT0185(glpK)
            PLT: Plut_1940
            DRA: DR_1928
            DGE: Dgeo_2522
            TTJ: TTHB142
            AAE: aq_434(glpK)
            TMA: TM0952 TM1430
            HAL: VNG1967G(glpK)
            HMA: rrnAC0550(glpK)
            HWA: HQ1733A(glpK)
            TAC: Ta1096
            TVO: TVN1141
            PTO: PTO1484
            PAB: PAB2406(glpK)
            PFU: PF2004
            TKO: TK1396
            APE: APE_0306.1
            SSO: SSO1600 SSO2133(glpK-2)
            SAI: Saci_1117 Saci_2033
            TPE: Tpen_0894
STRUCTURES  PDB: 1BO5  1BOT  1BU6  1BWF  1GLA  1GLB  1GLC  1GLD  1GLE  1GLF  
                 1GLJ  1GLL  1R59  1XUP  2D4W  2P3R  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.30
            ExPASy - ENZYME nomenclature database: 2.7.1.30
            ExplorEnz - The Enzyme Database: 2.7.1.30
            ERGO genome analysis and discovery system: 2.7.1.30
            BRENDA, the Enzyme Database: 2.7.1.30
            CAS: 9030-66-4
///
ENTRY       EC 2.7.1.31                 Enzyme
NAME        glycerate kinase;
            glycerate kinase (phosphorylating);
            D-glycerate 3-kinase;
            D-glycerate kinase;
            glycerate-3-kinase;
            GK;
            D-glyceric acid kinase;
            ATP:D-glycerate 2-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:(R)-glycerate 3-phosphotransferase
REACTION    ATP + (R)-glycerate = ADP + 3-phospho-(R)-glycerate [RN:R01514]
ALL_REAC    R01514
SUBSTRATE   ATP [CPD:C00002];
            (R)-glycerate [CPD:C00258]
PRODUCT     ADP [CPD:C00008];
            3-phospho-(R)-glycerate [CPD:C00197]
REFERENCE   1  [PMID:5325263]
  AUTHORS   Doughty CC, Hayashi JA, Guenther HL.
  TITLE     Purification and properties of D-glycerate 3-kinase from Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 241 (1966) 568-72.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:13416296]
  AUTHORS   ICHIHARA A, GREENBERG DM.
  TITLE     Studies on the purification and properties of D-glyceric acid kinase
            of liver.
  JOURNAL   J. Biol. Chem. 225 (1957) 949-58.
  ORGANISM  horse, rat [GN:rno]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00561  Glycerolipid metabolism
            PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K00865  glycerate kinase
GENES       ANI: AN6943.2
            TCR: 508741.170
            EHI: 250.t00007 92.t00002
            ECO: b0514(glxK) b3124(garK)
            ECJ: JW0502(glxK) JW3093(garK)
            ECE: Z0669(ybbZ) Z4476(yhaD)
            ECS: ECs0576 ECs4002
            ECC: c0628(ybbZ) c3879(yhaD)
            ECI: UTI89_C0542(ybbZ) UTI89_C3555(yhaD)
            ECP: ECP_0574 ECP_3214
            ECV: APECO1_1501(glxK) APECO1_3303(garK)
            ECW: EcE24377A_3602(garK)
            ECX: EcHS_A0587 EcHS_A3313(garK)
            STY: STY0573(glxK) STY2730 STY3097 STY3429
            STT: t0367 t2336(glxK) t2868 t3167
            SPT: SPA0377 SPA2198(glxK) SPA2824 SPA3116(garK)
            SEC: SC0564(glxK) SC2487(grk) SC2899(grk) SC3194(garK)
            STM: STM0525(glxK) STM2959 STM3247(garK)
            YPE: YPO3980(glxK)
            YPK: y3849
            YPM: YP_3343(glxK)
            YPA: YPA_3808
            YPN: YPN_3630
            YPP: YPDSF_3346
            YPS: YPTB3821(glxK)
            YPI: YpsIP31758_4052
            SFL: SF3161(yhaD)
            SFX: S3376(yhaD)
            SFV: SFV_3164(yhaD)
            SSN: SSON_3279(yhaD)
            SBO: SBO_2989(yhaD)
            SDY: SDY_3318(yhaD)
            ECA: ECA3572(garK)
            PLU: plu4100(garK)
            ENT: Ent638_3239 Ent638_3566
            SPE: Spro_1142
            HIN: HI0091
            HIT: NTHI0169(grk)
            HSO: HS_1524(glxK)
            PMU: PM1741
            MSU: MS0693
            APL: APL_0142(glxK)
            ASU: Asuc_1857
            XCC: XCC4226(glxK)
            XCB: XC_4315
            XCV: XCV4472(glxK)
            XAC: XAC4360(glxK)
            XOO: XOO4620(glxK)
            XOM: XOO_4357(XOO4357)
            VCH: VCA0903
            VVU: VV1_1654
            VVY: VV2752 VVA1391
            VPA: VPA0117
            VFI: VF2157
            PPR: PBPRA3190
            PAE: PA1052
            PAU: PA14_50760
            PPU: PP_3178
            PPF: Pput_2538
            PST: PSPTO_3280(glxK)
            PSB: Psyr_3115
            PSP: PSPPH_3026(garK)
            PFL: PFL_3378(glxK)
            PFO: Pfl_2908
            PEN: PSEEN2878
            PMY: Pmen_1439
            PAR: Psyc_1342
            PCR: Pcryo_1024
            PRW: PsycPRwf_1372
            ACI: ACIAD2850(glxK)
            ACB: A1S_2641
            SON: SO_1770
            SFR: Sfri_2642
            SAZ: Sama_3228
            SBL: Sbal_1575
            SBM: Shew185_1570
            SLO: Shew_2534
            SPC: Sputcn32_1470
            SSE: Ssed_2779
            SPL: Spea_2714
            SHE: Shewmr4_2519
            SHM: Shewmr7_2587
            SHN: Shewana3_1512 Shewana3_2685
            SHW: Sputw3181_2631
            PIN: Ping_0645
            MAQ: Maqu_2051
            FTA: FTA_1541 FTA_1543
            FTN: FTN_0674(glxK)
            TCX: Tcr_0775
            HCH: HCH_01301(garK)
            CSA: Csal_2952
            AHA: AHA_0642
            NME: NMB1268
            NMA: NMA1473
            REH: H16_B0612(glxK)
            BMA: BMA1468(glxK)
            BMV: BMASAVP1_A1961(glxK)
            BML: BMA10299_A3344(glxK)
            BMN: BMA10247_1235(glxK)
            BXE: Bxe_A2298
            BVI: Bcep1808_1857
            BUR: Bcep18194_A5226
            BCN: Bcen_6154
            BCH: Bcen2424_1925
            BAM: Bamb_1913
            BPS: BPSL1401 BPSS0127(glxK)
            BPM: BURPS1710b_2484(glxK) BURPS1710b_A1637(glxK)
            BPL: BURPS1106A_2368 BURPS1106A_A0173
            BPD: BURPS668_2327 BURPS668_A0262
            BTE: BTH_I2117 BTH_II0201
            BPE: BP3332(garK)
            BPA: BPP3664(garK)
            BBR: BB4099(garK)
            CCV: CCV52592_0612
            PCA: Pcar_1226
            PPD: Ppro_2915
            MXA: MXAN_5570
            PDE: Pden_4561
            ZMO: ZMO0059(glxK)
            BSU: BG11103(yxaA)
            BHA: BH0555
            BAN: BA2210
            BAR: GBAA2210
            BAA: BA_0734 BA_2712
            BAT: BAS0154 BAS2054
            BCE: BC0184
            BCA: BCE_0153
            BCZ: BCZK0146(garK)
            BCY: Bcer98_0146
            BTK: BT9727_0148(garK)
            BTL: BALH_0150(garK) BALH_1969
            BLI: BL02363(glxK)
            BCL: ABC0498 ABC0745
            BAY: RBAM_000170(glxK)
            BPU: BPUM_3630(glxK)
            OIH: OB0282 OB2786
            GKA: GK3465
            GTN: GTNG_3399
            SAU: SA2220
            SAV: SAV2432
            SAM: MW2356
            SAR: SAR2522
            SAS: SAS2324
            SAC: SACOL2435
            SAB: SAB0694 SAB2314
            SAA: SAUSA300_0726 SAUSA300_2377
            SAO: SAOUHSC_02723
            SAJ: SaurJH9_0766 SaurJH9_2458
            SAH: SaurJH1_0783 SaurJH1_2507
            SEP: SE1999
            SER: SERP2012(garK)
            SHA: SH0631
            SSP: SSP0178
            LMO: lmo2736 lmo2832
            LMF: LMOf2365_2723(garK-1) LMOf2365_2823(garK-2)
            LIN: lin2965
            LWE: lwe2762(garK-2)
            LLA: L79277(yihF)
            LLC: LACR_0925
            SPZ: M5005_Spy_1620
            SPH: MGAS10270_Spy1688
            SPI: MGAS10750_Spy1675
            SPJ: MGAS2096_Spy1644
            SPK: MGAS9429_Spy1623
            SPA: M6_Spy1628
            SPB: M28_Spy1609
            SPN: SP_1126
            SPR: spr1034(glxK)
            SPD: SPD_1011
            SAG: SAG0793(garK)
            SAN: gbs0813
            SAK: SAK_0918
            SMU: SMU.1252(grk)
            STC: str0633(grk)
            STL: stu0633(grk)
            SSA: SSA_0883(grk)
            SGO: SGO_1429
            LPL: lp_3266(glyK)
            LJO: LJ1251
            LAC: LBA0723
            LSA: LSA0712
            LSL: LSL_1707
            LDB: Ldb1044
            LBU: LBUL_0949
            LBR: LVIS_0413
            LGA: LGAS_0348
            LRE: Lreu_0622
            PPE: PEPE_0955
            EFA: EF2646
            OOE: OEOE_1478
            STH: STH2490
            CAC: CAC2834
            CPE: CPE0861
            CPF: CPF_0854(glxK)
            CTC: CTC00702
            CNO: NT01CX_0984
            CTH: Cthe_1592
            CDF: CD3084(garK)
            CBA: CLB_2174(glxK)
            CBH: CLC_2157(glxK)
            CBF: CLI_2283(glxK)
            CBE: Cbei_4479
            CHY: CHY_1268(garK)
            DSY: DSY2120
            CSC: Csac_1341
            TTE: TTE2616
            MTA: Moth_0404
            MTU: Rv2205c
            MTC: MT2261
            MBO: Mb2228c
            MPA: MAP1945c
            MAV: MAV_2286
            MSM: MSMEG_2528
            MVA: Mvan_3569
            MGI: Mflv_2944
            MMC: Mmcs_2001
            MKM: Mkms_2047
            MJL: Mjls_1982
            CGL: NCgl2000(cgl2080)
            CGB: cg2282(glxK)
            CEF: CE0236 CE1983
            CDI: DIP1548
            NFA: nfa27590 nfa55070
            RHA: RHA1_ro01141 RHA1_ro02573 RHA1_ro03229 RHA1_ro04801
                 RHA1_ro04922
            SCO: SCO2145(SC6G10.18) SCO6466(SC9C7.02)
            SMA: SAV1918(glxK)
            LXX: Lxx06640(pgk)
            CMI: CMM_2954
            ART: Arth_0123 Arth_3692
            AAU: AAur_0070 AAur_3509(glxK)
            PAC: PPA2299
            NCA: Noca_1163 Noca_3147
            TFU: Tfu_1010
            FRA: Francci3_4457
            FAL: FRAAL6785(garK)
            KRA: Krad_3519
            SEN: SACE_0098(glxK) SACE_6728(glxK)
            STP: Strop_3305
            BLO: BL0845(glxK)
            BAD: BAD_1196(glxK)
            TDE: TDE0208(glxK)
            CYA: CYA_1417
            CYB: CYB_1607
            BTH: BT_1437
            PGI: PG1859
            HWA: HQ1667A(gckA)
            PTO: PTO1442
STRUCTURES  PDB: 1TO6  1X3L  2B8N  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.31
            ExPASy - ENZYME nomenclature database: 2.7.1.31
            ExplorEnz - The Enzyme Database: 2.7.1.31
            ERGO genome analysis and discovery system: 2.7.1.31
            BRENDA, the Enzyme Database: 2.7.1.31
            CAS: 9026-61-3
///
ENTRY       EC 2.7.1.32                 Enzyme
NAME        choline kinase;
            choline kinase (phosphorylating);
            choline phosphokinase;
            choline-ethanolamine kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:choline phosphotransferase
REACTION    ATP + choline = ADP + O-phosphocholine [RN:R01021]
ALL_REAC    R01021
SUBSTRATE   ATP [CPD:C00002];
            choline [CPD:C00114]
PRODUCT     ADP [CPD:C00008];
            O-phosphocholine [CPD:C00588]
COMMENT     Ethanolamine and its methyl and ethyl derivatives can also act as
            acceptors.
REFERENCE   1  [PMID:5335908]
  AUTHORS   Hayashi SI, Lin EC.
  TITLE     Purification and properties of glycerol kinase from Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 242 (1967) 1030-5.
REFERENCE   2
  AUTHORS   Wittenberg, J. and Kornberg, A.
  TITLE     Choline phosphokinase.
  JOURNAL   J. Biol. Chem. 202 (1953) 431-444.
  ORGANISM  cow [GN:bta], Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00866  choline kinase
GENES       HSA: 1119(CHKA) 1120(CHKB)
            MMU: 12651(Chkb) 12660(Chka)
            RNO: 29194(Chka) 29367(Chkb)
            CFA: 476002(CHKA) 606800(CHKB)
            GGA: 423112(CHKA)
            SPU: 762153(LOC762153)
            OSA: 4325332 4325586
            CME: CMR011C
            SCE: YLR133W(CKI1)
            AGO: AGOS_AGL199C
            PIC: PICST_28965(CKT1)
            CGR: CAGL0M04367g
            SPO: SPAC13G7.12c
            AFM: AFUA_1G00640 AFUA_1G15930
            AOR: AO090005001098
            CNE: CNI01400
            DDI: DDBDRAFT_0217612
            PFA: PF14_0020
            CPV: cgd3_2030
            CHO: Chro.30240
            TAN: TA14380 TA14385 TA14390 TA14405 TA14410 TA14415 TA20330
            PST: PSPTO_3188
            PSB: Psyr_3054
            RSP: RSP_1457
            BPU: BPUM_2639(ytmP)
            MMO: MMOB5930(licA)
            FNU: FN1237
STRUCTURES  PDB: 1NW1  2CKO  2CKP  2CKQ  2I7Q  2IG7  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.32
            ExPASy - ENZYME nomenclature database: 2.7.1.32
            ExplorEnz - The Enzyme Database: 2.7.1.32
            ERGO genome analysis and discovery system: 2.7.1.32
            BRENDA, the Enzyme Database: 2.7.1.32
            CAS: 9026-67-9
///
ENTRY       EC 2.7.1.33                 Enzyme
NAME        pantothenate kinase;
            pantothenate kinase (phosphorylating);
            pantothenic acid kinase;
            ATP:pantothenate 4'-phosphotransferase;
            D-pantothenate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:(R)-pantothenate 4'-phosphotransferase
REACTION    ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate
            [RN:R03018]
ALL_REAC    R03018;
            (other) R02971 R04391
SUBSTRATE   ATP [CPD:C00002];
            (R)-pantothenate [CPD:C00864]
PRODUCT     ADP [CPD:C00008];
            (R)-4'-phosphopantothenate [CPD:C03492]
REFERENCE   1  [PMID:4337331]
  AUTHORS   Abiko Y, Ashida SI, Shimizu M.
  TITLE     Purification and properties of D-pantothenate kinase from rat liver.
  JOURNAL   Biochim. Biophys. Acta. 268 (1972) 364-72.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:13630913]
  AUTHORS   BROWN GM.
  TITLE     The metabolism of pantothenic acid.
  JOURNAL   J. Biol. Chem. 234 (1959) 370-8.
  ORGANISM  Lactobacillus arabinosus, Proteus morganii
REFERENCE   3  [PMID:13269369]
  AUTHORS   PIERPOINT WS, HUGHES DE, BADDILEY J, MATHIAS AP.
  TITLE     The phosphorylation of pantothenic acid by Lactobacillus arabinosus
            17-5.
  JOURNAL   Biochem. J. 61 (1955) 368-74.
  ORGANISM  Lactobacillus arabinosus
PATHWAY     PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K00867  type I pantothenate kinase
            KO: K03525  type III pantothenate kinase
            KO: K09680  type II pantothenate kinase
GENES       HSA: 53354(PANK1) 55229(PANK4) 79646(PANK3) 80025(PANK2)
            PTR: 450590(PANK1) 458070(PANK2) 462250(PANK3) 469462(PANK4)
            MMU: 211347(Pank3) 269614(Pank4) 74450(Pank2) 75735(Pank1)
            RNO: 171053(Pank4) 360511(Pank3_predicted)
            CFA: 477168(PANK2) 479579(PANK4) 486790(PANK1) 489133(PANK3)
                 608992(LOC608992)
            BTA: 510749(MGC142994) 514589(MGC142618)
            GGA: 416170(PANK3) 422935(LOC422935) 423792(PANK1)
            XLA: 446433(pank3)
            DRE: 393487(zgc:66285) 565059(zgc:158746)
            SPU: 590061(LOC590061)
            DME: Dmel_CG5725(fbl)
            SCE: YDR531W
            PIC: PICST_47307(YFH7.1) PICST_57761
            CGR: CAGL0H01551g
            AFM: AFUA_3G07180
            TAN: TA08490
            TBR: Tb11.02.5190
            TCR: 506779.80 511153.120
            LMA: LmjF28.0140
            ECO: b3974(coaA)
            ECJ: JW3942(coaA)
            ECE: Z5545(coaA)
            ECS: ECs4901
            ECC: c4933(coaA)
            ECI: UTI89_C3802(coaA)
            ECP: ECP_4188
            ECV: APECO1_2493(coaA)
            ECW: EcE24377A_4513(coaA)
            ECX: EcHS_A4208(coaA)
            STY: STY3740(coaA)
            STT: t3487(coaA)
            SPT: SPA3978(coaA)
            SEC: SC4027(coaA)
            STM: STM4139(coaA)
            YPE: YPO3758(coaA)
            YPK: y0473(coaA)
            YPM: YP_3290(coaA)
            YPA: YPA_3427
            YPN: YPN_0207
            YPP: YPDSF_3379
            YPS: YPTB0274(coaA)
            YPI: YpsIP31758_3870(coaA)
            YEN: YE0276(coaA)
            SFL: SF4052(rts)
            SFX: S3688(coaA)
            SFV: SFV_4047(coaA)
            SSN: SSON_4147(coaA)
            SBO: SBO_3994(coaA)
            SDY: SDY_3754(coaA)
            ECA: ECA0215(coaA)
            PLU: plu4731(coaA)
            WBR: WGLp514(coaA)
            SGL: SG0126
            ENT: Ent638_0189
            SPE: Spro_0269
            BPN: BPEN_191(coaA)
            HIN: HI0631(coaA)
            HIT: NTHI0713(coaA)
            HDU: HD0056(coaA)
            HSO: HS_0196(coaA)
            PMU: PM1747(coaA)
            MSU: MS2188(coaA)
            APL: APL_1513(coaA)
            XFA: XF1795
            XFT: PD1072(baf)
            XCC: XCC3937(baf)
            XCB: XC_4025
            XCV: XCV4109
            XAC: XAC4017(baf)
            XOO: XOO0429(baf)
            XOM: XOO_0391(XOO0391)
            VCH: VC0320
            VCO: VC0395_A2718(coaA)
            VVU: VV1_1200
            VVY: VV3168
            VFI: VF2424
            PPR: PBPRA3444
            PAE: PA4279
            PAU: PA14_08630
            PPU: PP_0438
            PST: PSPTO_0611
            PSB: Psyr_4563
            PSP: PSPPH_4611
            PFL: PFL_5932
            PFO: Pfl_5095
            PEN: PSEEN0472
            PAR: Psyc_0314
            PCR: Pcryo_0345
            ACI: ACIAD0840
            SON: SO_0215(panK)
            SDN: Sden_0156
            SFR: Sfri_0133
            SAZ: Sama_0198
            SBL: Sbal_4173
            SLO: Shew_0143
            SHE: Shewmr4_0183
            SHM: Shewmr7_0178
            SHN: Shewana3_0184
            SHW: Sputw3181_0141
            ILO: IL2002(bvg)
            CPS: CPS_4744
            PHA: PSHAa2912
            PAT: Patl_3997
            SDE: Sde_0916
            PIN: Ping_3622
            MAQ: Maqu_0703
            CBU: CBU_0199(coaA)
            CBD: COXBU7E912_1896(coaA)
            LPN: lpg0911
            LPF: lpl0943
            LPP: lpp0973
            MCA: MCA1780
            FTU: FTT0112 FTT1392
            FTF: FTF0112 FTF1392
            FTW: FTW_0197
            FTL: FTL_0671 FTL_1665
            FTH: FTH_0674 FTH_1606
            FTN: FTN_1355 FTN_1603
            TCX: Tcr_1947
            NOC: Noc_0189
            AEH: Mlg_0441
            HCH: HCH_06233
            CSA: Csal_0407
            ABO: ABO_0369
            AHA: AHA_4039(coaA)
            BCI: BCI_0359(coaA)
            RMA: Rmag_0337
            NME: NMB2075
            NMA: NMA0357(birA)
            NGO: NGO2001(birA)
            CVI: CV_0487
            RSO: RSc0311(RS03278)
            REU: Reut_A0103
            REH: H16_A0136
            RME: Rmet_0074
            BMA: BMA0070
            BXE: Bxe_A4227
            BUR: Bcep18194_A6248
            BCN: Bcen_2291
            BCH: Bcen2424_2905
            BAM: Bamb_2954
            BPS: BPSL0397
            BTE: BTH_I0369
            BPE: BP0097(baf)
            BBR: BB0160(baf)
            RFR: Rfer_3614
            POL: Bpro_4044
            NEU: NE2459(birA)
            NET: Neut_0233
            NMU: Nmul_A2081
            EBA: ebA4111
            AZO: azo0733(baf)
            DAR: Daro_3756
            TBD: Tbd_0461
            MFA: Mfla_2080
            HPY: HP0862
            HPJ: jhp0796
            HPA: HPAG1_0845
            HHE: HH0150
            HAC: Hac_1225
            WSU: WS0803
            TDN: Tmden_0888
            CJE: Cj0394c
            CJR: CJE0443
            CCV: CCV52592_0993
            CHA: CHAB381_1638
            CCO: CCC13826_0217
            GSU: GSU1934
            GME: Gmet_1986
            PCA: Pcar_1970
            PPD: Ppro_0655
            DVU: DVU0321
            DVL: Dvul_2660
            DDE: Dde_0294
            LIP: LI0090
            BBA: Bd3564(yacB)
            DPS: DP2278
            ADE: Adeh_2387
            MXA: MXAN_2325(coaA) MXAN_4151
            SAT: SYN_02883
            SFU: Sfum_0549
            AMA: AM271
            APH: APH_1014
            ERU: Erum1800
            ERW: ERWE_CDS_01790
            ERG: ERGA_CDS_01740
            ECN: Ecaj_0177
            ECH: ECH_0941
            PUB: SAR11_0899(yacB)
            MLO: mlr5019
            MES: Meso_3499
            SME: SMc02567(coaA)
            SMD: Smed_3257
            ATU: Atu0037(panK)
            ATC: AGR_C_59(coaA)
            RET: RHE_CH00040(coaA)
            RLE: RL0040(coaA)
            BME: BMEI1883 BMEI2039
            BMF: BAB1_2088(coaA)
            BMS: BR2087(coaA)
            BMB: BruAb1_2062(coaA)
            BOV: BOV_2007(coaA)
            OAN: Oant_0832
            BJA: blr0656(panK)
            BRA: BRADO0218(coaA)
            BBT: BBta_0140(coaA)
            RPA: RPA0315(coaA)
            RPB: RPB_0411
            RPC: RPC_0312
            RPD: RPD_0409
            RPE: RPE_0364
            NWI: Nwi_0120
            NHA: Nham_0128
            BHE: BH02050(coaA)
            BQU: BQ01930(coaA)
            BBK: BARBAKC583_1263(coaA)
            CCR: CC_1935
            SIL: SPO2761
            SIT: TM1040_0762
            RSP: RSP_2533
            RSH: Rsph17029_1193
            JAN: Jann_1198
            RDE: RD1_3266
            PDE: Pden_2229
            MMR: Mmar10_1370
            HNE: HNE_1760
            ZMO: ZMO1867
            NAR: Saro_2285
            SAL: Sala_1294
            ELI: ELI_06590
            GOX: GOX0081
            GBE: GbCGDNIH1_1287
            RRU: Rru_A1570
            MAG: amb2772
            MGM: Mmc1_1477
            ABA: Acid345_0136
            SUS: Acid_7558
            BSU: BG10133(yacB) BG11748(coaA)
            BHA: BH0086 BH2875
            BAN: BA0065 BA2901
            BAR: GBAA0065 GBAA2901
            BAA: BA_0655 BA_3417
            BAT: BAS0065 BAS2702
            BCE: BC0073 BC2898
            BCA: BCE_0064 BCE_2940
            BCZ: BCZK0061 BCZK2629
            BTK: BT9727_0061 BT9727_2652
            BTL: BALH_0064 BALH_2604
            BLI: BL00803(coaA) BL00853(yacB)
            BLD: BLi00086(yacB) BLi02540(coaA)
            BCL: ABC0107 ABC2539(coaA)
            BAY: RBAM_021890(coaA)
            BPU: BPUM_2105(coaA)
            OIH: OB0081 OB2682
            GKA: GK0063
            SAU: SA1932
            SAV: SAV2130
            SAM: MW2054
            SAR: SAR2218
            SAS: SAS2033
            SAC: SACOL2122
            SAB: SAB2014
            SAA: SAUSA300_2084(coaA)
            SAO: SAOUHSC_02371
            SEP: SE1728
            SER: SERP1737
            SHA: SH0905
            SSP: SSP0755
            LMO: lmo0221 lmo0922
            LMF: LMOf2365_0232 LMOf2365_0944(coaA)
            LIN: lin0253 lin0923
            LWE: lwe0184 lwe0901(coaA)
            LLA: L66222(coaA)
            LLC: LACR_1533
            LLM: llmg_1058(coaA)
            SPY: SPy_1233(coaA)
            SPZ: M5005_Spy_0945(coaA)
            SPM: spyM18_1183(coaA)
            SPG: SpyM3_0871(coaA)
            SPS: SPs1071
            SPH: MGAS10270_Spy1059(coaA)
            SPI: MGAS10750_Spy1094(coaA)
            SPJ: MGAS2096_Spy1004(coaA)
            SPK: MGAS9429_Spy1048(coaA)
            SPF: SpyM50853(coaA)
            SPA: M6_Spy0934
            SPB: M28_Spy0917(coaA)
            SPN: SP_0839
            SPR: spr0741(coaA)
            SPD: SPD_0733(coaA)
            SAG: SAG0951(coaA)
            SAN: gbs0939
            SAK: SAK_1046(coaA)
            SMU: SMU.1126(coaA)
            STC: str0799(coaA)
            STL: stu0799(coaA)
            STE: STER_0851
            SSA: SSA_1033(coaA)
            SGO: SGO_1077(coaA)
            LPL: lp_0913(coaA)
            LJO: LJ0619
            LAC: LBA1669(coaA)
            LSA: LSA0138(panK)
            LSL: LSL_1538(coaA)
            LDB: Ldb1912(coaA)
            LBU: LBUL_1779
            LBR: LVIS_1761
            LCA: LSEI_1980
            LRE: Lreu_1619
            PPE: PEPE_0407
            EFA: EF0168
            OOE: OEOE_1603
            STH: STH3183 STH3184
            CAC: CAC3200
            CPE: CPE2468
            CPF: CPF_2784
            CPR: CPR_2470
            CTC: CTC00207
            CNO: NT01CX_1043
            CTH: Cthe_2588
            CDF: CD3555
            CHY: CHY_2370
            DSY: DSY0216
            SWO: Swol_0109
            CSC: Csac_0770
            TTE: TTE2381
            MTA: Moth_0146
            MPU: MYPU_4730
            MMO: MMOB5910
            MSY: MS53_0006
            MTU: Rv1092c(coaA) Rv3600c
            MTC: MT1124(panK) MT3706
            MBO: Mb1122c(coaA) Mb3630c
            MBB: BCG_1152c(coaA)
            MLE: ML0232 ML1954(coaA)
            MPA: MAP0458 MAP2700(coaA)
            MAV: MAV_1214(coaA)
            MSM: MSMEG_5252(coaA) MSMEG_6096
            MUL: MUL_0189(coaA)
            MVA: Mvan_4658
            MGI: Mflv_2058
            MMC: Mmcs_4133 Mmcs_4760
            MKM: Mkms_4208
            MJL: Mjls_4364
            CGL: NCgl0953(cgl0995)
            CGB: cg1132(coaA)
            CEF: CE1057
            CDI: DIP0931(coaA)
            CJK: jk1466(coaA)
            NFA: nfa4080 nfa48170(coaA)
            RHA: RHA1_ro04417 RHA1_ro05857(coaA)
            SCO: SCO3380(SCE94.31c) SCO4738(coaA)
            SMA: SAV4690 SAV4961(coaA)
            TWH: TWT147(coaA)
            TWS: TW156(coaA)
            LXX: Lxx19970(coaA)
            CMI: CMM_2577(coaA)
            ART: Arth_2913
            AAU: AAur_2901(coaA)
            PAC: PPA1799
            NCA: Noca_0464
            TFU: Tfu_2610 Tfu_2882
            FRA: Francci3_4379
            FAL: FRAAL4036(coaA) FRAAL4037(coaA) FRAAL6674
            ACE: Acel_0215
            KRA: Krad_0723
            SEN: SACE_0408 SACE_1986(coaA)
            STP: Strop_4278
            BLO: BL1162
            BAD: BAD_0477
            RXY: Rxyl_2182
            FNU: FN0761
            RBA: RB2632
            BBU: BB0527
            BGA: BG0536
            BAF: BAPKO_0553
            TPA: TP0431
            LIL: LA0833
            LIC: LIC12792
            LBJ: LBJ_0491
            LBL: LBL_2588
            SYN: slr0812
            SYW: SYNW2163
            SYC: syc2285_d
            SYF: Synpcc7942_1808
            SYD: Syncc9605_2308
            SYE: Syncc9902_0385
            SYG: sync_2509
            CYA: CYA_0337
            CYB: CYB_1510
            TEL: tll1149
            GVI: glr2994
            ANA: alr3896
            AVA: Ava_1801
            PMA: Pro0094
            PMM: PMM0080
            PMT: PMT1623
            PMN: PMN2A_1444
            PMI: PMT9312_0083
            BTH: BT_4366
            BFR: BF1072
            BFS: BF0989
            PGI: PG0447
            SRU: SRU_0528
            CHU: CHU_3272
            CTE: CT1408
            CCH: Cag_1218
            PLT: Plut_1408
            DET: DET0428
            DEH: cbdb_A381
            DRA: DR_0461
            DGE: Dgeo_1749
            TTH: TTC1008
            TTJ: TTHA1374
            AAE: aq_1924
            TMA: TM0883
            PTO: PTO0232
STRUCTURES  PDB: 1ESM  1ESN  1SQ5  2EWS  2F9T  2F9W  2GES  2GET  2GEU  2GEV  
                 2I7N  2I7P  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.33
            ExPASy - ENZYME nomenclature database: 2.7.1.33
            ExplorEnz - The Enzyme Database: 2.7.1.33
            ERGO genome analysis and discovery system: 2.7.1.33
            BRENDA, the Enzyme Database: 2.7.1.33
            CAS: 9026-48-6
///
ENTRY       EC 2.7.1.34                 Enzyme
NAME        pantetheine kinase;
            pantetheine kinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:pantetheine 4'-phosphotransferase
REACTION    ATP + pantetheine = ADP + pantetheine 4'-phosphate [RN:R02971]
ALL_REAC    R02971
SUBSTRATE   ATP [CPD:C00002];
            pantetheine [CPD:C00831]
PRODUCT     ADP [CPD:C00008];
            pantetheine 4'-phosphate [CPD:C01134]
REFERENCE   1  [PMID:13107738]
  AUTHORS   NOVELLI GD.
  TITLE     Enzymatic synthesis and structure of CoA.
  JOURNAL   Fed. Proc. 12 (1953) 675-81.
PATHWAY     PATH: map00770  Pantothenate and CoA biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.34
            ExPASy - ENZYME nomenclature database: 2.7.1.34
            ExplorEnz - The Enzyme Database: 2.7.1.34
            ERGO genome analysis and discovery system: 2.7.1.34
            BRENDA, the Enzyme Database: 2.7.1.34
            CAS: 9026-49-7
///
ENTRY       EC 2.7.1.35                 Enzyme
NAME        pyridoxal kinase;
            pyridoxal kinase (phosphorylating);
            pyridoxal 5-phosphate-kinase;
            pyridoxal phosphokinase;
            pyridoxine kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:pyridoxal 5'-phosphotransferase
REACTION    ATP + pyridoxal = ADP + pyridoxal 5'-phosphate [RN:R00174]
ALL_REAC    R00174;
            (other) R01909 R02493
SUBSTRATE   ATP [CPD:C00002];
            pyridoxal [CPD:C00250]
PRODUCT     ADP [CPD:C00008];
            pyridoxal 5'-phosphate [CPD:C00018]
COMMENT     Pyridoxine, pyridoxamine and various derivatives can also act as
            acceptors.
REFERENCE   1
  AUTHORS   McCormick, D.B., Gregory, M.E. and Snell, E.E.
  TITLE     Pyridoxal phosphokinases. I. Assay, distribution, purification, and
            properties.
  JOURNAL   J. Biol. Chem. 236 (1961) 2076-2084.
  ORGANISM  Streptococcus faecalis, Escherichia coli [GN:eco], Saccharomyces
            carlsbergensis
REFERENCE   2
  AUTHORS   Trufanov, A.F. and Krisanova, J.A.
  TITLE     Biosynthesis of pyridoxal phosphate by liver sections of rat in
            vitro.
  JOURNAL   Byull. Eksp. Biol. Med. 22(6) (1946) 40-43.
PATHWAY     PATH: map00750  Vitamin B6 metabolism
ORTHOLOGY   KO: K00868  pyridoxine kinase
GENES       HSA: 8566(PDXK)
            PTR: 474032(RRP1)
            MMU: 216134(Pdxk)
            RNO: 83578(Pdxk)
            CFA: 487788(PDXK)
            SSC: 396983(PDXK)
            GGA: 418549(LOC418549)
            SPU: 589025(LOC589025)
            CEL: F57C9.1
            ATH: AT5G37850(SOS4)
            OSA: 4352717
            CME: CMS339C
            SCE: YNR027W(BUD17)
            AGO: AGOS_AAR047C
            PIC: PICST_31981(BUD17) PICST_34206(BUD16)
            CGR: CAGL0I03300g CAGL0M10725g
            SPO: SPAC6F6.11c SPCC18.10
            ANI: AN0270.2
            AFM: AFUA_1G02900
            AOR: AO090005000781
            UMA: UM02673.1
            DDI: DDB_0191114(pykA)
            PFA: PFF0775w
            TBR: Tb927.6.2740
            TCR: 507925.40 509059.50
            LMA: LmjF30.1250
            EHI: 117.t00005 221.t00004
            ECO: b1636(pdxY) b2418(pdxK)
            ECJ: JW1628(pdxY) JW2411(pdxK)
            ECE: Z2648(pdxY) Z3684(pdxK)
            ECS: ECs2345 ECs3290
            ECC: c2028(pdxY) c2953(pdxK)
            ECI: UTI89_C1827(pdxY) UTI89_C2752(pdxK)
            ECP: ECP_1581 ECP_2442
            ECV: APECO1_4127(pdxK) APECO1_719(pdxY)
            ECW: EcE24377A_1846(pdxY) EcE24377A_2705(pdxK)
            ECX: EcHS_A1712 EcHS_A2553
            STY: STY1672(pdxY) STY2672(pdxK)
            STT: t0423(pdxK) t1318(pdxY)
            SPT: SPA0430(pdxK) SPA1403(pdxY)
            SEC: SC1468(pdxY) SC2433(pdxK)
            STM: STM1450(pdxY) STM2435(pdxK)
            YPE: YPO2368(pdxY)
            YPK: y1967(pdxY)
            YPM: YP_2154(pdxY)
            YPA: YPA_1714
            YPN: YPN_1825
            YPS: YPTB2282(pdxY)
            SFL: SF1661(pdxY) SF2473(pdxK)
            SFX: S1793(pdxY) S2619(pdxK)
            SFV: SFV_1653(pdxY) SFV_2470(pdxK)
            SSN: SSON_1520(pdxY) SSON_2508(pdxK)
            SBO: SBO_1498(pdxY)
            SDY: SDY_1859(pdxY) SDY_2615(pdxK)
            ECA: ECA1937(pdxY)
            PLU: plu2595(pdxY)
            ENT: Ent638_1812
            SPE: Spro_2220
            HIP: CGSHiEE_00975
            HSO: HS_0933(pdxY)
            PMU: PM0290(pdxY)
            MSU: MS0805(pdxK)
            APL: APL_1485(pdxY)
            XCC: XCC1476(pdxY)
            XCB: XC_2761
            XCV: XCV1566(pdxY)
            XAC: XAC1524(pdxY)
            XOO: XOO2033(pdxY)
            XOM: XOO_1915(XOO1915)
            VVU: VV2_1237
            VVY: VVA0065
            VPA: VPA1632
            VFI: VF2056
            PPR: PBPRA2534
            PAE: PA5516(pdxY)
            PAU: PA14_72780(pdxY)
            PAP: PSPA7_6318
            PPU: PP_5357(pkxY)
            PPF: Pput_5265
            PST: PSPTO_5521(pdxY)
            PSB: Psyr_5070
            PSP: PSPPH_5152
            PFL: PFL_6169
            PFO: Pfl_5650
            PEN: PSEEN5509(pdxY)
            SPL: Spea_3913
            FTU: FTT0288c(pdxY)
            FTF: FTF0288c(pdxY)
            FTW: FTW_1798(pdxY)
            FTL: FTL_0198
            FTH: FTH_0193(pdxY)
            FTA: FTA_0214
            FTN: FTN_0202(pdxY)
            AHA: AHA_1193(pdxY-1) AHA_2417(pdxY-2)
            DNO: DNO_0929(pdxK)
            RME: Rmet_4114
            BMA: BMA0582(pdxY)
            BML: BMA10299_A2857(pdxY)
            BMN: BMA10247_1745(pdxY)
            BXE: Bxe_A2936
            BVI: Bcep1808_1085
            BUR: Bcep18194_A4279
            BCN: Bcen_0688
            BCH: Bcen2424_1167
            BAM: Bamb_1046
            BPS: BPSL2402(pdxY)
            BPM: BURPS1710b_2863
            BPL: BURPS1106A_2802(pdxY)
            BPD: BURPS668_2743(pdxY)
            BTE: BTH_I1763
            BPE: BP1321(pdxK)
            BPA: BPP2900(pdxK)
            BBR: BB2870(pdxK)
            DVU: DVU0769
            DDE: Dde_2742
            MLO: mlr4132
            MES: Meso_3224
            SME: SMc04084(pdxK)
            SMD: Smed_3186
            ATU: Atu2487(pdxK)
            ATC: AGR_C_4518
            RLE: RL4719(pdxK)
            BME: BMEI0221
            BMF: BAB1_1838
            BMS: BR1830
            BMB: BruAb1_1809
            BOV: BOV_1761
            OAN: Oant_1072
            BJA: blr4233
            RPA: RPA2799(pdxK)
            RPD: RPD_2302
            CCR: CC_0256
            RSP: RSP_1920
            MMR: Mmar10_2881
            GBE: GbCGDNIH1_1354
            ACR: Acry_2881
            RRU: Rru_A1145 Rru_A1199
            MAG: amb3949
            BAN: BA5663(thiD-2)
            BAR: GBAA5663(thiD-2)
            BAA: BA_0522(pfkB)
            BAT: BAS5266
            BCE: BC5413
            BCA: BCE_5542(thiD)
            BTK: BT9727_5093(thiD)
            OIH: OB1040(thiD)
            LMO: lmo0662(thiD)
            LMF: LMOf2365_0696(thiD-2)
            LIN: lin0667(thiD)
            SPZ: M5005_Spy_0923
            SPH: MGAS10270_Spy1037
            SPI: MGAS10750_Spy1072
            SPJ: MGAS2096_Spy0982
            SPK: MGAS9429_Spy1025
            SPA: M6_Spy0912
            SPB: M28_Spy0895
            SSA: SSA_1400(pdxK)
            LPL: lp_0863(pdx)
            LJO: LJ1562
            LAC: LBA1007
            LSA: LSA1352
            LBU: LBUL_0033
            LBR: LVIS_2152
            LCA: LSEI_0622
            EFA: EF0202
            STH: STH2862
            CAC: CAC1622
            CPE: CPE2318
            CPF: CPF_2618
            CPR: CPR_2304
            CTC: CTC00497
            CBA: CLB_1414(pdxK)
            CBH: CLC_1426(pdxK)
            CBF: CLI_1486(pdxK)
            DSY: DSY1521
            POY: PAM434(pdxK)
            CGL: NCgl0876(cgl0913) NCgl2973(cgl3079)
            CGB: cg1041(pdxK)
            CEF: CE0975 CE2917
            CDI: DIP1715
            LXX: Lxx10710(pdxY)
            PAC: PPA1225 PPA1712
            NCA: Noca_4006
            STP: Strop_2472
            BLO: BL0934
            BAD: BAD_0597
            RXY: Rxyl_0612
            BGA: BG0791(pdxK)
            BAF: BAPKO_0816(pdxK)
            TPA: TP0115(thiD)
            TDE: TDE0693(thiD)
            BTH: BT_4458
            BFR: BF3591
            BFS: BF3395
            DRA: DR_A0184
            DGE: Dgeo_0144
STRUCTURES  PDB: 1LHP  1LHR  1RFT  1RFU  1RFV  1TD2  1VI9  1YGJ  1YGK  1YHJ  
                 2AJP  2DDM  2DDO  2DDW  2F7K  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.35
            ExPASy - ENZYME nomenclature database: 2.7.1.35
            ExplorEnz - The Enzyme Database: 2.7.1.35
            ERGO genome analysis and discovery system: 2.7.1.35
            BRENDA, the Enzyme Database: 2.7.1.35
            CAS: 9026-42-0
///
ENTRY       EC 2.7.1.36                 Enzyme
NAME        mevalonate kinase;
            mevalonate kinase (phosphorylating);
            mevalonate phosphokinase;
            mevalonic acid kinase;
            mevalonic kinase;
            mevalonate 5-phosphotransferase ;
            MVA kinase;
            ATP:mevalonate 5-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:(R)-mevalonate 5-phosphotransferase
REACTION    ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate [RN:R02245]
ALL_REAC    R02245
SUBSTRATE   ATP [CPD:C00002];
            (R)-mevalonate [CPD:C00418]
PRODUCT     ADP [CPD:C00008];
            (R)-5-phosphomevalonate [CPD:C01107]
COMMENT     CTP, GTP and UTP can also act as donors.
REFERENCE   1
  AUTHORS   Hellig, H. and Popjak, G.
  TITLE     Studies on the biosynthesis of cholesterol. XIII. Phosphomevalonic
            kinase from liver.
  JOURNAL   J. Lipid Res. 2 (1961) 235-243.
  ORGANISM  pig [GN:ssc]
REFERENCE   2
  AUTHORS   Levy, G.B. and Popjak, G.
  TITLE     Studies on the biosynthesis of cholesterol. 10. Mevalonic kinase
            from liver.
  JOURNAL   Biochem. J. 75 (1960) 417-428.
  ORGANISM  pig [GN:ssc]
REFERENCE   3
  AUTHORS   Markley, K. and Smallman, E.
  TITLE     Mevalonic kinase in rabbit liver.
  JOURNAL   Biochim. Biophys. Acta 47 (1961) 327-335.
  ORGANISM  rabbit
REFERENCE   4
  AUTHORS   Tchen, T.T.
  TITLE     Mevalonic kinase: purification and properties.
  JOURNAL   J. Biol. Chem. 233 (1958) 1100-1103.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K00869  mevalonate kinase
GENES       HSA: 4598(MVK)
            MMU: 17855(Mvk)
            RNO: 81727(Mvk)
            CFA: 486309(MVK)
            BTA: 505792(MVK)
            GGA: 768555(MVK)
            DRE: 492477(zgc:103473)
            SPU: 585785(LOC585785)
            DME: Dmel_CG33671
            OSA: 4348331
            SCE: YMR208W(ERG12)
            AGO: AGOS_AER335W
            PIC: PICST_40742(ERG12)
            CGR: CAGL0F03861g
            SPO: SPAC13G6.11c
            ANI: AN3869.2
            AFM: AFUA_4G07780
            AOR: AO090023000793
            CNE: CNK01740
            ECU: ECU09_1780
            DDI: DDBDRAFT_0168621
            TET: TTHERM_00637680
            TBR: Tb927.4.4070
            TCR: 436521.9 509237.10
            LMA: LmjF31.0560
            CBU: CBU_0608 CBU_0609
            CBD: COXBU7E912_0620(mvk)
            LPN: lpg2039
            LPF: lpl2017
            LPP: lpp2022
            BBA: Bd1027(lmbP) Bd1630(mvk)
            MXA: MXAN_5019(mvk)
            OIH: OB0225
            SAU: SA0547(mvaK1)
            SAV: SAV0590(mvaK1)
            SAM: MW0545(mvaK1)
            SAR: SAR0596(mvaK1)
            SAS: SAS0549
            SAC: SACOL0636(mvk)
            SAB: SAB0540(mvaK1)
            SAA: SAUSA300_0572(mvk)
            SAO: SAOUHSC_00577
            SEP: SE0361
            SER: SERP0238(mvk)
            SHA: SH2402(mvaK1)
            SSP: SSP2122
            LMO: lmo0010
            LMF: LMOf2365_0011
            LIN: lin0010
            LWE: lwe0011(mvk)
            LLA: L7866(yeaG)
            LLC: LACR_0454
            LLM: llmg_0425(mvk)
            SPY: SPy_0876(mvaK1)
            SPZ: M5005_Spy_0682(mvaK1)
            SPM: spyM18_0937(mvaK1)
            SPG: SpyM3_0595(mvaK1)
            SPS: SPs1258
            SPH: MGAS10270_Spy0740(mvaK1)
            SPI: MGAS10750_Spy0774(mvaK1)
            SPJ: MGAS2096_Spy0753(mvaK1)
            SPK: MGAS9429_Spy0737(mvaK1)
            SPF: SpyM51126(mvaK1)
            SPA: M6_Spy0699
            SPB: M28_Spy0662(mvaK1)
            SPN: SP_0381
            SPR: spr0338(mvk)
            SPD: SPD_0346(mvk)
            SAG: SAG1326
            SAN: gbs1396
            SAK: SAK_1357(mvk)
            SMU: SMU.181
            STC: str0559(mvaK1)
            STL: stu0559(mvaK1)
            SSA: SSA_0333(mvaK1)
            SGO: SGO_0239(mvk)
            LPL: lp_1735(mvaK1)
            LJO: LJ1205
            LAC: LBA1167(mvaK)
            LSA: LSA0908(mvaK1)
            LSL: LSL_0685(eRG)
            LDB: Ldb0999(mvk)
            LBU: LBUL_0906
            LBR: LVIS_0858
            LCA: LSEI_1491
            EFA: EF0904(mvk)
            OOE: OEOE_1100
            NFA: nfa22070
            BGA: BG0711
            BAF: BAPKO_0732
            FPS: FP0313
            MMP: MMP1335
            MAE: Maeo_0775
            MAC: MA0602(mvk)
            MBA: Mbar_A1421
            MMA: MM_1762
            MBU: Mbur_2395
            MHU: Mhun_2890
            MEM: Memar_1812
            MBN: Mboo_2213
            MST: Msp_0858(mvk)
            MSI: Msm_1439
            MKA: MK0993(ERG12)
            HAL: VNG1145G(mvk)
            HMA: rrnAC0077(mvk)
            HWA: HQ2925A(mvk)
            NPH: NP2850A(mvk)
            PTO: PTO1352
            PHO: PH1625
            PAB: PAB0372(mvk)
            PFU: PF1637(mvk)
            TKO: TK1474
            RCI: LRC399(mvk)
            APE: APE_2439
            SSO: SSO0383
            STO: ST2185
            SAI: Saci_2365(mvk)
            MSE: Msed_1602
            PAI: PAE3108
            PIS: Pisl_0467
            PCL: Pcal_1835
STRUCTURES  PDB: 1KKH  1KVK  1VIS  2HFS  2HFU  2OI2  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.36
            ExPASy - ENZYME nomenclature database: 2.7.1.36
            ExplorEnz - The Enzyme Database: 2.7.1.36
            ERGO genome analysis and discovery system: 2.7.1.36
            BRENDA, the Enzyme Database: 2.7.1.36
            CAS: 9026-52-2
///
ENTRY       EC 2.7.1.37       Obsolete  Enzyme
NAME        Transferred to 2.7.11.1 and 2.7.11.8 and 2.7.11.9 and 2.7.11.10 and
            2.7.11.11 and 2.7.11.12 and 2.7.11.13 and 2.7.11.21 and 2.7.11.22
            and 2.7.11.24 and 2.7.11.25 and 2.7.11.30 and 2.7.12.1
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: protein kinase. Now divided into EC 2.7.11.1
            (non-specific serine/threonine protein kinase), EC 2.7.11.8
            (Fas-activated serine/threonine kinase), EC 2.7.11.9
            (Goodpasture-antigen-binding protein kinase), EC 2.7.11.10 (IkappaB
            kinase), EC 2.7.11.11 (cAMP-dependent protein kinase), EC 2.7.11.12
            (cGMP-dependent protein kinase), EC 2.7.11.13 (protein kinase C), EC
            2.7.11.21 (polo kinase), EC 2.7.11.22 (cyclin-dependent kinase), EC
            2.7.11.24 (mitogen-activated protein kinase), EC 2.7.11.25
            (mitogen-activated protein kinase kinase kinase), EC 2.7.11.30
            (receptor protein serine/threonine kinase) and EC 2.7.12.1
            (dual-specificity kinase). (EC 2.7.1.37 created 1961 (EC 2.7.1.70
            incorporated 2004), deleted 2005)
ORTHOLOGY   KO: K00870  protein kinase
GENES       DME: Dmel_CG15224(CkIIbeta) Dmel_CG32616(Ste12DOR)
                 Dmel_CG3263(Pka-R1) Dmel_CG33236(Ste:CG33236)
                 Dmel_CG33237(Ste:CG33237) Dmel_CG33238(Ste:CG33238)
                 Dmel_CG33239(Ste:CG33239) Dmel_CG33240(Ste:CG33240)
                 Dmel_CG33241(Ste:CG33241) Dmel_CG33242(Ste:CG33242)
                 Dmel_CG33243(Ste:CG33243) Dmel_CG33244(Ste:CG33244)
                 Dmel_CG33245(Ste:CG33245) Dmel_CG33246(Ste:CG33246)
                 Dmel_CG33247(Ste:CG33247) Dmel_CG8585(Ih)
            ATH: AT4G24740(AFC2) AT5G47750
            CME: CMA103C CMD015C CMF099C CML228C CMO051C CMQ039C CMQ204C
                 CMS463C CMT297C
            CAL: CaO19.3545
            SPO: SPBC106.01a(mph1)
            CNE: CNE03450 CNE05060
            ECU: ECU07_0360
            DDI: DDB_0216387 DDB_0220670
            PFA: MAL13P1.185 MAL3P1.1 MAL7P1.73 MAL7P1.91 PF07_0072 PF11_0147
                 PF13_0085 PF14_0227 PF14_0392 PF14_0516 PFB0150c PFB0815w
                 PFI1415w PFL0080c PFL1110c PFL1885c PFL2280w
            CPV: cgd1_2960 cgd2_1060
            CHO: Chro.10329 Chro.20118 Chro.20198 Chro.20335 Chro.20465
                 Chro.40038 Chro.70024 Chro.70159 Chro.80094
            TAN: TA02550 TA09165 TA10725 TA11120 TA11795 TA12515 TA21080
            TPV: TP01_0359 TP02_0494 TP03_0047 TP03_0140 TP03_0511 TP03_0842
                 TP04_0122 TP04_0645 TP04_0791 TP04_0880
            TBR: Tb09.211.3820 Tb10.61.2330 Tb10.61.3140 Tb10.70.0960
                 Tb10.70.0970 Tb11.01.6650 Tb927.1.3130 Tb927.3.3080
                 Tb927.3.3290 Tb927.7.5770
            TCR: 503685.10 506327.80 506327.90 506697.30 507837.20 507993.80
                 508153.310 508153.510 508173.170 508405.70 508741.320
                 508817.80 508917.10 509599.130 509599.150 509999.110 510323.10
                 511283.280
            LMA: LmjF06.1180 LmjF18.0270 LmjF28.0520 LmjF28.3000 LmjF29.1330
                 LmjF29.2490 LmjF29.2670 LmjF32.0260 LmjF36.1520
            EHI: 1.t00135 11.t00019 114.t00009 128.t00002 17.t00036 191.t00021
                 234.t00006 248.t00011 253.t00012 295.t00004 32.t00020
                 35.t00048 370.t00002 395.t00005 4.t00088 4.t00091 469.t00005
                 5.t00069 64.t00038 68.t00037 68.t00050 8.t00084 83.t00032
                 87.t00018 9.t00044
            ECI: UTI89_C0996(mukB) UTI89_C1979(yeaG)
            XCV: XCV0063 XCV2141 XCV4206 XCV4220
            XOO: XOO3035
            XOM: XOO_2888(XOO2888)
            VFI: VF0990 VF2496
            PSP: PSPPH_0629 PSPPH_1820 PSPPH_3275(ankB)
            PAR: Psyc_1446(malT) Psyc_1539(ppkA)
            PCR: Pcryo_1718
            PHA: PSHAa1485
            LPN: lpg2810(prkA)
            LPF: lpl2725
            LPP: lpp2856
            CVI: CV_1789(prkA)
            BMA: BMAA0400.1
            BXE: Bxe_A2005 Bxe_B2722
            BPS: BPSS2102
            BPM: BURPS1710b_2025(prkA) BURPS1710b_A1202 BURPS1710b_A1436(acoK)
            BTE: BTH_II0256
            EBA: ebA4966(prkA)
            DAR: Daro_0438
            TBD: Tbd_1232(prkA) Tbd_1700
            BBA: Bd0228(prkA)
            RET: RHE_PE00133(ype00062)
            RLE: pRL110587 pRL120462(impN)
            BSU: BG10129(yabT)
            BHA: BH0080
            BAN: BA2307
            BAR: GBAA2307
            BAA: BA_2810
            BAT: BAS2152
            BCE: BC2258
            BCA: BCE_2340
            BCZ: BCZK0457(prkA) BCZK2086
            BLI: BL00504(yabT) BL01719
            BLD: BLi00082(yabT) BLi00391(ybdM)
            BCL: ABC0103 ABC1474(prkA) ABC3319
            OIH: OB0076 OB2654
            GKA: GK0059 GK0486 GK1686
            MGE: MG_109
            MPN: MPN248(K04_orf389)
            MGA: MGA_0459(sps1)
            MSY: MS53_0121(pknB)
            MTC: MT0423
            MBO: Mb0418c(pknG)
            MLE: ML0304(pknG)
            MPA: MAP0017c MAP2505 MAP3893c(pknG)
            MSM: MSMEG_0786 MSMEG_4554
            MMC: Mmcs_0540
            CGL: NCgl2655(cgl2751)
            CGB: cg3046(pknG)
            CEF: CE2589(pknG)
            CDI: DIP2053
            CJK: jk0252(pknG) jk1732(pknJ)
            NFA: nfa24260 nfa53440 nfa8550
            SCO: SCO2666(SC6D10.09) SCO2974(pkaA) SCO4377(SCD10.09)
            SMA: SAV5100(pkn23) SAV5375(pkn26)
            FRA: Francci3_2424 Francci3_3623
            FAL: FRAAL3895
            BLO: BL1425(pknA2)
            FNU: FN0678
            RBA: RB9435(pkn2)
            CTR: CT301(pknD)
            CPN: CPn0095
            CPA: CP0679
            CPJ: CPj0095
            CPT: CpB0095(pkn1)
            CCA: CCA00677
            CAB: CAB647
            CFE: CF0334(pkn1)
            PCU: pc1645
            SYN: sll1574(spkA) sll1575(spkA) slr0152(spkG)
            SYC: syc0923_d
            SYF: Synpcc7942_0600
            CYA: CYA_0209 CYA_2146 CYA_2262
            CYB: CYB_0466 CYB_0522 CYB_0949
            TEL: tlr0445 tlr2304
            GVI: gll0054 gll0585 gll2103 gll2127 glr0657 glr0665 glr0915
                 glr1096 glr1346 glr4107
            ANA: all3169 all3691(pkn30) all4518
            TTH: TTC1230 TTC1856
            TTJ: TTHA0138 TTHA1594
            HMA: rrnAC1159(pknA1)
            NPH: NP3444A(prkA_1) NP3446A(prkA_2)
            PTO: PTO0135
STRUCTURES  PDB: 1APM  1AQ1  1ATP  1B38  1B39  1B6C  1BDY  1BKX  1BX6  1CDK  
                 1CKP  1CMK  1CTP  1DAW  1DAY  1DDM  1DS5  1E1V  1E1X  1E9H  
                 1F0Q  1FMO  1FOT  1FVT  1FVV  1G3N  1GIH  1GII  1GIJ  1GNG  
                 1GZ8  1H00  1H01  1H07  1H08  1H0V  1H0W  1H1W  1H8F  1HCK  
                 1HCL  1I09  1IA9  1IAH  1IAJ  1IAS  1ID0  1IK7  1J1B  1J1C  
                 1J3H  1J91  1JAM  1JBP  1JLU  1JVP  1JWH  1KE5  1KE6  1KE7  
                 1KE8  1KE9  1KTZ  1L3R  1L6E  1LL8  1LP4  1LPU  1LR4  1M2P  
                 1M2Q  1M2R  1MBY  1NA7  1O6K  1O6L  1O6Y  1O9U  1OGU  1OI9  
                 1OIQ  1OIR  1OIT  1OIU  1OIY  1OKV  1OKW  1OKY  1OKZ  1OL1  
                 1OL2  1OL5  1OL6  1OL7  1OM1  1OUK  1OUY  1OVE  1OZ1  1PF8  
                 1PJK  1PLO  1PY5  1PYX  1Q24  1Q3D  1Q3W  1Q41  1Q4L  1Q5K  
                 1Q61  1Q62  1Q8T  1Q8U  1Q8W  1QF8  1R0E  1R2A  1R39  1R3C  
                 1RDQ  1RE8  1REJ  1REK  1REW  1RGS  1RQF  1RW8  1RWI  1RWL  
                 1S4Y  1S9I  1S9J  1SMH  1STC  1SVE  1SVG  1SVH  1SYK  1SZM  
                 1T4H  1TH8  1THN  1TID  1TIL  1TVO  1U7E  1UA2  1UKH  1UKI  
                 1URC  1URW  1UTI  1UU3  1UU7  1UU8  1UU9  1UV5  1UVR  1UWH  
                 1UWJ  1V1K  1VD2  1VEB  1VJY  1VYW  1VYZ  1VZO  1W0X  1W1D  
                 1W1G  1W1H  1W7H  1W82  1W83  1W84  1W8C  1W98  1WAK  1WBN  
                 1WBO  1WBP  1WBS  1WBT  1WBV  1WBW  1WCC  1WH4  1WMH  1WMK  
                 1WRZ  1WVW  1WVX  1WVY  1WXM  1WZY  1X9X  1XH4  1XH5  1XH6  
                 1XH7  1XH8  1XH9  1XHA  1XO2  1XQZ  1XR1  1XTE  1XTN  1XWS  
                 1Y8G  1Y8Y  1Y91  1YDR  1YDS  1YDT  1YGO  1YHS  1YHV  1YHW  
                 1YI3  1YI4  1YKR  1YMI  1YQJ  1YR5  1YRP  1YW2  1YWR  1YWV  
                 1YXS  1YXT  1YXU  1YXV  1YXX  1Z57  1Z5M  1Z9X  1ZLT  1ZMU  
                 1ZMV  1ZMW  1ZOE  1ZOG  1ZOH  1ZSG  1ZXA  1ZXE  1ZY4  1ZY5  
                 1ZYC  1ZYD  1ZYJ  1ZYS  1ZZ2  1ZZL  2A0C  2A0T  2A27  2A2A  
                 2A4L  2A9I  2AC3  2AC5  2AYP  2B1P  2B52  2B53  2B54  2B55  
                 2B9F  2B9H  2B9I  2B9J  2BAJ  2BAK  2BAL  2BAQ  2BHE  2BHH  
                 2BIK  2BIL  2BIY  2BKZ  2BMC  2BPM  2BR1  2BRB  2BRG  2BRH  
                 2BRM  2BRN  2BRO  2BTR  2BTS  2BUJ  2BVA  2BZH  2BZI  2BZJ  
                 2BZK  2C1A  2C1B  2C30  2C3I  2C3J  2C3K  2C3L  2C4G  2C5N  
                 2C5O  2C5P  2C5V  2C5X  2C5Y  2C60  2C68  2C69  2C6D  2C6E  
                 2C6I  2C6K  2C6L  2C6M  2C6O  2C6T  2CCI  2CDZ  2CGU  2CGV  
                 2CGW  2CGX  2CJM  2CLX  2COS  2CPK  2CU1  2DF6  2DRN  2ERZ  
                 2ESM  2ETK  2ETO  2ETR  2EU9  2EUF  2EVA  2EWA  2EXC  2EXE  
                 2EXM  2EZW  2F2C  2F2U  2F49  2F57  2F7E  2F7X  2F7Z  2F9G  
                 2FA2  2FB8  2FK9  2FSL  2FSM  2FSO  2FST  2FUM  2FVD  2FYS  
                 2G01  2G9X  2GBL  2GCD  2GDO  2GFC  2GFS  2GHG  2GHL  2GHM  
                 2GU8  2H9R  2IW6  2IW8  2IW9  2J0I  2J4Z  2UZB  2UZD  2UZE  
                 2UZL  2UZN  2UZO  2V0D  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.37
            ExPASy - ENZYME nomenclature database: 2.7.1.37
            ExplorEnz - The Enzyme Database: 2.7.1.37
            ERGO genome analysis and discovery system: 2.7.1.37
            BRENDA, the Enzyme Database: 2.7.1.37
///
ENTRY       EC 2.7.1.38       Obsolete  Enzyme
NAME        Transferred to 2.7.11.19
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.19 phosphorylase kinase (EC
            2.7.1.38 created 1961, deleted 2005)
STRUCTURES  PDB: 1PHK  1QL6  2PHK  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.38
            ExPASy - ENZYME nomenclature database: 2.7.1.38
            ExplorEnz - The Enzyme Database: 2.7.1.38
            ERGO genome analysis and discovery system: 2.7.1.38
            BRENDA, the Enzyme Database: 2.7.1.38
///
ENTRY       EC 2.7.1.39                 Enzyme
NAME        homoserine kinase;
            homoserine kinase (phosphorylating);
            HSK
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:L-homoserine O-phosphotransferase
REACTION    ATP + L-homoserine = ADP + O-phospho-L-homoserine [RN:R01771]
ALL_REAC    R01771
SUBSTRATE   ATP [CPD:C00002];
            L-homoserine [CPD:C00263]
PRODUCT     ADP [CPD:C00008];
            O-phospho-L-homoserine [CPD:C01102]
REFERENCE   1  [PMID:13823379]
  AUTHORS   FLAVIN M, SLAUGHTER C.
  TITLE     Purification and properties of threonine synthetase of Neurospora.
  JOURNAL   J. Biol. Chem. 235 (1960) 1103-8.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2
  AUTHORS   Watanabe, Y., Konishi, S. and Shimura, K.
  TITLE     Biosynthesis of threonine from homoserine. VI. Homoserine kinase.
  JOURNAL   J. Biochem. (Tokyo) 44 (1957) 299-307.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K00872  homoserine kinase
            KO: K02203  homoserine kinase
            KO: K02204  homoserine kinase type II
GENES       ATH: AT2G17265(HSK)
            OSA: 4331255
            SCE: YHR025W(THR1)
            AGO: AGOS_ACR070W
            PIC: PICST_85224(THR1)
            CAL: CaO19_923(CaO19.923)
            CGR: CAGL0J00649g
            SPO: SPBC4C3.03
            ANI: AN8843.2
            AFM: AFUA_5G05820
            AOR: AO090009000682
            CNE: CNI02930
            UMA: UM04597.1
            TBR: Tb927.6.4430
            TCR: 503597.10 509167.150
            LMA: LmjF30.3080
            ECO: b0003(thrB)
            ECJ: JW0002(thrB)
            ECE: Z0003(thrB)
            ECS: ECs0003
            ECC: c0004(thrB)
            ECI: UTI89_C0003(thrB)
            ECP: ECP_0003
            ECV: APECO1_1975(thrB)
            ECW: EcE24377A_0002(thrB)
            ECX: EcHS_A0004(thrB)
            STY: STY0003(thrB)
            STT: t0003(thrB)
            SPT: SPA0003(thrB)
            SEC: SC0003(thrB)
            STM: STM0003(thrB)
            YPE: YPO0460(thrB)
            YPK: y3716(thrB)
            YPM: YP_3722(thrB)
            YPA: YPA_4052
            YPN: YPN_0332
            YPS: YPTB0603(thrB)
            YPI: YpsIP31758_3475(thrB)
            SFL: SF0003(thrB)
            SFX: S0003(thrB)
            SFV: SFV_0002(thrB)
            SSN: SSON_0003(thrB)
            SBO: SBO_0002(thrB)
            SDY: SDY_0003(thrB)
            ECA: ECA3890(thrB)
            PLU: plu0564(thrB)
            BUC: BU193(thrB)
            BAS: BUsg187(thrB)
            BAB: bbp182(thrB)
            BCC: BCc_126(thrB)
            SGL: SG0405
            BFL: Bfl112(thrB)
            BPN: BPEN_116(thrB)
            HIN: HI0088(thrB)
            HIT: NTHI0166(thrB)
            HIP: CGSHiEE_02845
            HIQ: CGSHiGG_02990
            HSO: HS_1213(thrB)
            PMU: PM0114(thrB)
            MSU: MS1702(thrB)
            APL: APL_0249(thrB)
            XFA: XF2224
            XFT: PD1272(thrB)
            XCC: XCC1801(thrB)
            XCB: XC_2388
            XCV: XCV1867(thrB)
            XAC: XAC1821(thrB)
            XOO: XOO2243(thrB)
            XOM: XOO_2108(XOO2108)
            VCH: VC2363
            VCO: VC0395_A1942(thrB)
            VVU: VV1_0544
            VVY: VV0651
            VPA: VP0495
            VFI: VF2117
            PPR: PBPRA0553
            PAE: PA5495(thrB)
            PAU: PA14_72510(thrB)
            PAP: PSPA7_6296(thrB)
            PPU: PP_0121(thrB)
            PPF: Pput_0138
            PST: PSPTO_0346(thrB)
            PSB: Psyr_0272(thrB)
            PSP: PSPPH_0261(thrB)
            PFL: PFL_0080(thrB)
            PFO: Pfl_0058(thrB)
            PEN: PSEEN0074(thrB)
            PMY: Pmen_0152
            PAR: Psyc_2067(thrB)
            PCR: Pcryo_2390
            PRW: PsycPRwf_2288
            ACI: ACIAD1457 ACIAD3403
            SON: SO_3414(thrB)
            SDN: Sden_2739
            SFR: Sfri_2905
            SHE: Shewmr4_1139
            SHM: Shewmr7_1210
            SHN: Shewana3_1140
            CPS: CPS_4290(thrB)
            PHA: PSHAa2378(thrB)
            PAT: Patl_3579
            FTW: FTW_1647(thrB)
            FTA: FTA_0522
            TCX: Tcr_0043
            HCH: HCH_06348(thrB)
            CSA: Csal_0546
            MMW: Mmwyl1_0284
            AHA: AHA_3017(thrB)
            NME: NMB2029(thrB)
            NMA: NMA0411(thrB)
            NMC: NMC2008(thrB)
            NGO: NGO2075(thrB)
            CVI: CV_0776(thrB)
            RSO: RSc2233(thrB)
            REU: Reut_A0870(thrB)
            REH: H16_A2744(thrB) H16_A3212 H16_A3213 H16_A3222
            RME: Rmet_2627
            BMA: BMAA0307(thrB)
            BMV: BMASAVP1_1486(thrB)
            BML: BMA10299_1682(thrB)
            BMN: BMA10247_A0338(thrB)
            BXE: Bxe_B2840
            BVI: Bcep1808_4243
            BUR: Bcep18194_B2229(thrB)
            BCN: Bcen_4497
            BCH: Bcen2424_3867
            BAM: Bamb_3235
            BPS: BPSS1779(thrB)
            BPM: BURPS1710b_A0859(thrB)
            BPL: BURPS1106A_A2419(thrB)
            BPD: BURPS668_A2556(thrB)
            BTE: BTH_II0600(thrB)
            PNU: Pnuc_1713
            BPE: BP1084(thrB)
            BPA: BPP1914(thrB)
            BBR: BB2102(thrB)
            RFR: Rfer_1323
            POL: Bpro_1727
            PNA: Pnap_1476
            AAV: Aave_1928
            AJS: Ajs_3320
            VEI: Veis_1843
            MPT: Mpe_A1146
            HAR: HEAR0267(thrB)
            MMS: mma_0321(thrB)
            NEU: NE1471(thrB)
            NET: Neut_0775
            NMU: Nmul_A0565
            EBA: ebA3979(thrB)
            AZO: azo3604(thrB)
            DAR: Daro_0166(thrB)
            MFA: Mfla_0361
            HPY: HP1050(thrB)
            HPJ: jhp0375(thrB)
            HPA: HPAG1_0397
            HHE: HH1013(thrB)
            HAC: Hac_1161(thrB)
            WSU: WS2015
            TDN: Tmden_0674
            CJE: Cj0134(thrB)
            CJR: CJE0129(thrB)
            CJJ: CJJ81176_0169(thrB)
            CJU: C8J_0127(thrB)
            CJD: JJD26997_0147(thrB)
            CFF: CFF8240_1495(thrB)
            CHA: CHAB381_1681(thrB)
            CCO: CCC13826_0413 CCC13826_1493(thrB)
            ABU: Abu_2041(thrB)
            NIS: NIS_0420(thrB)
            SUN: SUN_1973(thrB)
            BBA: Bd2045(thrB)
            ADE: Adeh_3331
            AFW: Anae109_3396
            MXA: MXAN_2524
            PUB: SAR11_0125(thrB)
            MLO: mlr7503
            MES: Meso_0749
            PLA: Plav_0685
            SME: SMc00017(thrB)
            SMD: Smed_0528
            ATU: Atu0775(thrB)
            ATC: AGR_C_1416
            RET: RHE_CH00962(thrB)
            RLE: RL1031(thrB) RL1188
            BME: BMEI1458
            BMF: BAB1_0502(thrB)
            BMS: BR0476(thrB)
            BMB: BruAb1_0498(thrB)
            BOV: BOV_0481(thrB)
            OAN: Oant_0590
            BJA: blr1315(thrB)
            BRA: BRADO6587(thrB)
            BBT: BBta_0949(thrB)
            RPA: RPA4270(thrB)
            RPB: RPB_1341
            RPC: RPC_4077
            RPD: RPD_4029
            RPE: RPE_4129
            NWI: Nwi_2688
            NHA: Nham_3744
            BHE: BH04420(thrB2)
            XAU: Xaut_2356
            CCR: CC_3364
            MMR: Mmar10_1097
            HNE: HNE_0947(thrB)
            ZMO: ZMO1600(thrB)
            NAR: Saro_1086
            SAL: Sala_1135
            SWI: Swit_2691
            ELI: ELI_01555
            GOX: GOX0178
            GBE: GbCGDNIH1_1876
            ACR: Acry_1652
            RRU: Rru_A3053
            MAG: amb0763
            MGM: Mmc1_0824
            ABA: Acid345_1479
            SUS: Acid_0902
            BSU: BG10462(thrB)
            BHA: BH3420(thrB)
            BAN: BA1970(thrB)
            BAR: GBAA1970(thrB)
            BAA: BA_2470
            BAT: BAS1827
            BCE: BC1966
            BCA: BCE_2053(thrB)
            BCZ: BCZK1784(thrB)
            BCY: Bcer98_1498
            BTK: BT9727_1801(thrB)
            BLI: BL02135(thrB)
            BLD: BLi03412(thrB)
            BCL: ABC2940(thrB)
            BAY: RBAM_029350(thrB)
            BPU: BPUM_2886(thrB)
            OIH: OB0464
            GKA: GK2962
            SAU: SA1166(thrB)
            SAV: SAV1330(thrB)
            SAM: MW1217(thrB)
            SAR: SAR1340(thrB)
            SAS: SAS1270
            SAC: SACOL1364(thrB)
            SAB: SAB1188(thrB)
            SAA: SAUSA300_1228(thrB)
            SAO: SAOUHSC_01322
            SAJ: SaurJH9_1391
            SAH: SaurJH1_1418
            SEP: SE1011
            SER: SERP0899(thrB)
            SHA: SH1577(thrB)
            SSP: SSP1436
            LMO: lmo2545(thrB)
            LMF: LMOf2365_2518(thrB)
            LIN: lin2689(thrB)
            LWE: lwe2494(thrB)
            LLA: L0091(thrB)
            LLC: LACR_1281
            LLM: llmg_1331(thrB)
            SPN: SP_1360
            SPR: spr1218(thrB)
            SPD: SPD_1194(thrB)
            SAG: SAG1119(thrB)
            SAN: gbs1186
            SAK: SAK_1204(thrB)
            SMU: SMU.966
            STC: str0470(thrB)
            STL: stu0470(thrB)
            SSA: SSA_1044(thrB)
            SGO: SGO_0802(thrB)
            LPL: lp_0572(thrB)
            LAC: LBA1211(thrB)
            LSL: LSL_1518(thrB)
            LDB: Ldb1760(thrB)
            LBU: LBUL_1630
            LBR: LVIS_0548
            LCA: LSEI_2149
            EFA: EF2420(thrB)
            STH: STH2556
            CAC: CAC1235(thrB)
            CTC: CTC02357
            CNO: NT01CX_0707(thrB)
            CDF: CD2119(thrB)
            CBO: CBO1639(thrB)
            CBA: CLB_1656(thrB)
            CBH: CLC_1665(thrB)
            CBF: CLI_1716(thrB)
            CKL: CKL_0860(thrB)
            AMT: Amet_0568
            CHY: CHY_1910(thrB)
            DSY: DSY1362
            SWO: Swol_1318
            TTE: TTE2618(thrB)
            MTA: Moth_1305
            MTU: Rv1296(thrB)
            MTC: MT1335(thrB)
            MBO: Mb1328(thrB)
            MBB: BCG_1356(thrB)
            MLE: ML1131(thrB)
            MPA: MAP2466c(thrB)
            MAV: MAV_1511(thrB)
            MSM: MSMEG_4955(thrB)
            MVA: Mvan_4346
            MGI: Mflv_2300
            MMC: Mmcs_3894
            MKM: Mkms_3968
            MJL: Mjls_3880
            CGL: NCgl1137(cgl1184)
            CGB: cg1338(thrB)
            CEF: CE1290
            CDI: DIP1037(thrB)
            CJK: jk1350(thrB)
            NFA: nfa10510(thrB)
            RHA: RHA1_ro01486(thrB)
            SCO: SCO5356(SCBAC5H2.25)
            SMA: SAV2916(thrB)
            TWH: TWT437(thrB)
            TWS: TW331(thrB)
            LXX: Lxx06890(thrB)
            ART: Arth_2621
            AAU: AAur_2610(thrB)
            PAC: PPA1256
            NCA: Noca_1746
            TFU: Tfu_2422
            FRA: Francci3_3424 Francci3_3723
            FAL: FRAAL5949(thrB)
            ACE: Acel_0632
            KRA: Krad_1254
            SEN: SACE_6296(thrB)
            STP: Strop_3647
            BLO: BL1275(thrB)
            BAD: BAD_1415(thrB)
            RXY: Rxyl_3124
            FNU: FN0922
            LIL: LA2134(thrB)
            LIC: LIC11786(thrB)
            LBJ: LBJ_1878(thrB)
            LBL: LBL_1406(thrB)
            SYN: sll1760(thrB)
            SYW: SYNW1481(thrB)
            SYC: syc0116_d(thrB)
            SYF: Synpcc7942_1440
            SYD: Syncc9605_1031
            SYE: Syncc9902_0932
            SYG: sync_1869(thrB)
            SYR: SynRCC307_0943(thrB)
            SYX: SynWH7803_0773(thrB)
            CYA: CYA_1622(thrB)
            CYB: CYB_1902(thrB)
            TEL: tlr1765(thrB)
            GVI: gll1127(thrB)
            ANA: alr0346(thrB)
            AVA: Ava_2794
            PMA: Pro1066(thrB)
            PMM: PMM0595(thrB)
            PMT: PMT0426(thrB)
            PMN: PMN2A_0031
            PMI: PMT9312_0595
            PMB: A9601_06511(thrB)
            PMC: P9515_06601(thrB)
            PMF: P9303_18581(thrB)
            PMG: P9301_06211(thrB)
            PMH: P9215_06771(thrB)
            PME: NATL1_06511(thrB)
            TER: Tery_1018
            SRU: SRU_0690(thrB)
            CHU: CHU_0074(thrB)
            GFO: GFO_1969(thrB)
            CTE: CT2034(thrB)
            CCH: Cag_0139
            CPH: Cpha266_2545
            PVI: Cvib_1629
            PLT: Plut_1986
            DRA: DR_2390
            DGE: Dgeo_2253
            TTH: TTC1028
            TTJ: TTHA1394
            AAE: aq_1309(thrB)
            TMA: TM0545
            TPT: Tpet_0375
            MJA: MJ1104(thrB)
            MMP: MMP0295(thrB)
            MKA: MK0333(thrB)
            HAL: VNG1797G(thrB)
            HMA: rrnAC3348(thrB)
            HWA: HQ3322A(thrB)
            NPH: NP4524A(thrB)
            TAC: Ta0530
            TVO: TVN1006
            PTO: PTO0476
            PHO: PH1087
            PAB: PAB1676
            PFU: PF1054
            TKO: TK1444
            RCI: RCIX2142(thrB)
            APE: APE_2067.1
            IHO: Igni_1208
            SSO: SSO2367(thrB)
            STO: ST0505
            SAI: Saci_0972
            MSE: Msed_0672
            PAI: PAE0034
            PCL: Pcal_0376
            PAS: Pars_1078
STRUCTURES  PDB: 1FWK  1FWL  1H72  1H73  1H74  2PPQ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.39
            ExPASy - ENZYME nomenclature database: 2.7.1.39
            ExplorEnz - The Enzyme Database: 2.7.1.39
            ERGO genome analysis and discovery system: 2.7.1.39
            BRENDA, the Enzyme Database: 2.7.1.39
            CAS: 9026-58-8
///
ENTRY       EC 2.7.1.40                 Enzyme
NAME        pyruvate kinase;
            phosphoenolpyruvate kinase;
            phosphoenol transphosphorylase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:pyruvate 2-O-phosphotransferase
REACTION    ATP + pyruvate = ADP + phosphoenolpyruvate [RN:R00200]
ALL_REAC    R00200;
            (other) R00430 R00572 R00659 R00724 R01138 R01858 R02320
SUBSTRATE   ATP [CPD:C00002];
            pyruvate [CPD:C00022]
PRODUCT     ADP [CPD:C00008];
            phosphoenolpyruvate [CPD:C00074]
COFACTOR    CO2 [CPD:C00011]
COMMENT     UTP, GTP, CTP, ITP and dATP can also act as donors. Also
            phosphorylates hydroxylamine and fluoride in the presence of CO2.
REFERENCE   1
  AUTHORS   Boyer, P.D.
  TITLE     Pyruvate kinase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 6, Academic Press, New York, 1962, p. 95-113.
REFERENCE   2
  AUTHORS   Kornberg, A. and Pricer, W.E.
  TITLE     Enzymatic phosphorylation of adenosine and 2,6-diaminopurine
            riboside.
  JOURNAL   J. Biol. Chem. 193 (1951) 481-495.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Kubowitz, F. and Ott, P.
  TITLE     Isolierung von Garungsfermenten aus menschlichen Muskeln.
  JOURNAL   Biochem. Z. 317 (1944) 193-203.
  ORGANISM  human [GN:hsa]
REFERENCE   4
  AUTHORS   Strominger, J.L.
  TITLE     Enzymatic synthesis of guanosine and cytidine triphosphates: a note
            on the nucleotide specificity of the pyruvate phosphokinase
            reaction.
  JOURNAL   Biochim. Biophys. Acta 16 (1955) 616-618.
  ORGANISM  rabbit
REFERENCE   5
  AUTHORS   Tietz, A. and Ochoa, S.
  TITLE     "Fluorokinase" and pyruvic kinase.
  JOURNAL   Arch. Biochem. Biophys. 78 (1958) 477-493.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00230  Purine metabolism
            PATH: map00620  Pyruvate metabolism
            PATH: map00710  Carbon fixation
            PATH: map04910  Insulin signaling pathway
            PATH: map04930  Type II diabetes mellitus
ORTHOLOGY   KO: K00873  pyruvate kinase
GENES       HSA: 5313(PKLR) 5315(PKM2)
            PTR: 469513(PKLR)
            MMU: 18746(Pkm2) 18770(Pklr)
            RNO: 24651(Pklr) 25630(Pkm2)
            CFA: 403874(PKM2) 490425(PKLR)
            GGA: 396456(PKM2)
            XLA: 380274(pkm2) 398967(MGC68714) 399448(PKM2)
            DRE: 114551(pklr) 335817(pkm2) 445094(zgc:92037)
            SPU: 756486(LOC756486)
            DME: Dmel_CG7069 Dmel_CG7070(PyK)
            CEL: F25H5.3 ZK593.1
            ATH: AT3G04050 AT3G25960 AT3G52990 AT3G55650 AT3G55810 AT5G08570
                 AT5G52920 AT5G56350 AT5G63680
            OSA: 4324263 4337406
            CME: CMA030C CMC021C CMK041C CMP260C
            SCE: YAL038W(CDC19) YOR347C(PYK2)
            AGO: AGOS_ADR368W
            PIC: PICST_83166(PYK1)
            CGR: CAGL0E05610g CAGL0M12034g
            SPO: SPAC4H3.10c
            ANI: AN5210.2
            AFM: AFUA_6G07430
            AOR: AO090005001556
            ANG: An07g08990(pkiA)
            CNE: CNC03080
            ECU: ECU09_0640
            DDI: DDB_0231421
            PFA: PF10_0363 PFF1300w
            CPV: cgd1_2040
            CHO: Chro.10234
            TAN: TA10915 TA11540
            TPV: TP02_0134 TP04_0607
            TET: TTHERM_00118600 TTHERM_01016110 TTHERM_01205300
            TBR: Tb10.61.2680
            TCR: 507993.390 511281.60
            LMA: LmjF35.0030
            EHI: 345.t00008 503.t00005 77.t00002
            ECO: b1676(pykF) b1854(pykA)
            ECJ: JW1666(pykF) JW1843(pykA)
            ECE: Z2704(pykF) Z2906(pykA)
            ECS: ECs2383 ECs2564
            ECC: c2071(pykF) c2268(pykA)
            ECI: UTI89_C1868(pykF) UTI89_C2058(pykA)
            ECP: ECP_1623 ECP_1798
            ECV: APECO1_754(pykF) APECO1_904(pykA)
            ECW: EcE24377A_1892(pykF) EcE24377A_2084(pykA)
            ECX: EcHS_A1757 EcHS_A1947
            STY: STY1744(pykF) STY2096(pykA)
            STT: t0989(pykA) t1246(pykF)
            SPT: SPA0981(pykA) SPA1475(pykF)
            SEC: SC1399(pykF) SC1407(ttrS) SC1413(ssrA) SC1894(pykA)
            STM: STM1378(pykF) STM1386(ttrS) STM1392(ssrA) STM1888(pykA)
            YPE: YPO2064(pykA) YPO2393(pykF)
            YPK: y1944(pykF) y2246(pykA)
            YPM: YP_1907(pykA) YP_2180(pykF)
            YPA: YPA_1447 YPA_1738
            YPN: YPN_1541 YPN_1847
            YPP: YPDSF_0754 YPDSF_1058
            YPS: YPTB2047(pykA) YPTB2306(pykF)
            YPI: YpsIP31758_1749(pykF) YpsIP31758_2024(pykA)
            SFL: SF1705(pykF) SF1864(pykA)
            SFX: S1838(pykF) S1930(pykA)
            SFV: SFV_1699(pykF) SFV_1856(pykA)
            SSN: SSON_1294(pykA) SSON_1480(pykF)
            SBO: SBO_1162(pykA) SBO_1454(pykF)
            SDY: SDY_1141(pykA) SDY_1905(pykF)
            ECA: ECA1867(pykF) ECA2481(pykA)
            PLU: plu2118(pykA) plu2613(pykF)
            BUC: BU319(pykA)
            BAS: BUsg311(pykA)
            BAB: bbp297(pykA)
            BCC: BCc_198(pykA)
            WBR: WGLp136(pykA)
            SGL: SG1268 SG1438
            ENT: Ent638_1768 Ent638_2423
            SPE: Spro_2187 Spro_2770
            BFL: Bfl450(pykA)
            BPN: BPEN_465(pykA)
            HIN: HI1573(pykA)
            HIT: NTHI1479(pykA)
            HIP: CGSHiEE_05445
            HIQ: CGSHiGG_00145
            HDU: HD0446(pykA)
            HSO: HS_0900(ttrS) HS_1086(pykA)
            PMU: PM0653(pykA)
            MSU: MS1197(pykF)
            APL: APL_0187(pykA)
            ASU: Asuc_1171
            XFA: XF0824
            XFT: PD1846(pykA)
            XCC: XCC3186(pykA)
            XCB: XC_0978
            XCV: XCV3463(pykA)
            XAC: XAC3345(pykA)
            XOO: XOO3413(pykA)
            XOM: XOO_3213(XOO3213)
            VCH: VC0485 VC2008 VCA0708
            VCO: VC0395_0647(pykA-2) VC0395_A0037(pykF) VC0395_A1594(pykA-1)
            VVU: VV1_0644 VV1_2992 VV2_0206
            VVY: VV0500 VV1289 VVA0713
            VPA: VP0356 VP2039 VPA0823
            VFI: VF2258 VFA0494
            PPR: PBPRA0428 PBPRA2431(pykA)
            PAE: PA1498(pykF) PA4329(pykA)
            PAU: PA14_45050(pykF) PA14_56240(pykA)
            PAP: PSPA7_3834(pyk2) PSPA7_4898(pyk1)
            PPU: PP_1362(pykA) PP_4301(pykF)
            PPF: Pput_1568 Pput_1849 Pput_4362
            PST: PSPTO_4337(pyk)
            PSB: Psyr_4029
            PSP: PSPPH_4039(pyk)
            PFL: PFL_1697(pyk) PFL_4797(pyk)
            PFO: Pfl_1594 Pfl_4448
            PEN: PSEEN1147(pykA) PSEEN1668(pykF)
            PMY: Pmen_2773 Pmen_3261
            SON: SO_2491(pykA)
            SDN: Sden_2081
            SFR: Sfri_1890
            SAZ: Sama_1814
            SBL: Sbal_2243
            SBM: Shew185_2128
            SLO: Shew_2050
            SPC: Sputcn32_1864
            SSE: Ssed_2068
            SPL: Spea_2337
            SHE: Shewmr4_2048
            SHM: Shewmr7_1927
            SHN: Shewana3_2153
            SHW: Sputw3181_2144
            ILO: IL1263(pykA)
            CPS: CPS_2279(pyk)
            PHA: PSHAa1406(pykA)
            PAT: Patl_0968
            SDE: Sde_1308
            PIN: Ping_2361 Ping_2879
            MAQ: Maqu_1831 Maqu_3252 Maqu_3917
            CBU: CBU_1781(pyk)
            CBD: COXBU7E912_0227(pyk)
            LPN: lpg0136(pykA)
            LPF: lpl0136
            LPP: lpp0151
            MCA: MCA2597(pyk)
            FTU: FTT1366c(pyk)
            FTF: FTF1366c(pyk)
            FTW: FTW_0525(pyk)
            FTL: FTL_1148
            FTH: FTH_1123(pykA)
            FTA: FTA_1211(pyk)
            FTN: FTN_1330(pyk)
            TCX: Tcr_0247
            NOC: Noc_0990 Noc_2805
            AEH: Mlg_2843
            HHA: Hhal_1040
            HCH: HCH_00431(pyk)
            CSA: Csal_1559
            ABO: ABO_2621(pykA)
            MMW: Mmwyl1_1078
            AHA: AHA_0029(pyk-1) AHA_1349(pyk-2) AHA_3052(pyk-3)
            DNO: DNO_1200(pyk)
            BCI: BCI_0310(pykA)
            RMA: Rmag_0066
            VOK: COSY_0073
            NME: NMB0089
            NMA: NMA0177(pykA)
            NMC: NMC0074(pykA)
            NGO: NGO1881
            CVI: CV_0249(pykF)
            RSO: RSc0572(pykA1) RSp1448(pykA2)
            REU: Reut_A0558 Reut_A3295
            REH: H16_A0567(pyk1) H16_A3602(pyk2) H16_B0961(pyk3)
            RME: Rmet_0502 Rmet_1519 Rmet_3452
            BMA: BMA0298(pyk)
            BMV: BMASAVP1_A0593(pyk)
            BML: BMA10299_A2427(pyk)
            BMN: BMA10247_0039(pyk)
            BXE: Bxe_A0690
            BVI: Bcep1808_2742
            BUR: Bcep18194_A5958
            BCN: Bcen_2016
            BCH: Bcen2424_2627
            BAM: Bamb_2674
            BPS: BPSL0797(pykA) BPSS0128(pyk)
            BPM: BURPS1710b_0996(pyk) BURPS1710b_A1638(pyk)
            BPL: BURPS1106A_0840(pyk) BURPS1106A_A0174(pyk)
            BPD: BURPS668_0835(pyk) BURPS668_A0263(pyk)
            BTE: BTH_I0664(pyk-1) BTH_II0202(pyk-2)
            PNU: Pnuc_1816
            BPE: BP3333(pykA)
            BPA: BPP3663(pykA)
            BBR: BB4098(pykA)
            RFR: Rfer_0205
            POL: Bpro_4634
            PNA: Pnap_3873
            AAV: Aave_4581
            AJS: Ajs_3956
            VEI: Veis_0196
            MPT: Mpe_A0290(pykF)
            HAR: HEAR0336
            MMS: mma_0383
            NEU: NE0325(pykA1)
            NET: Neut_0979 Neut_1580
            NMU: Nmul_A0385 Nmul_A1506 Nmul_A1507
            EBA: ebA1105(pykA)
            AZO: azo2842(pykA)
            DAR: Daro_2117 Daro_3595
            TBD: Tbd_0162(pykA)
            MFA: Mfla_2244
            CJE: Cj0392c(pyk)
            CJR: CJE0441(pyk)
            CJJ: CJJ81176_0415(pyk)
            CJU: C8J_0367(pyk)
            CJD: JJD26997_1566(pyk)
            CFF: CFF8240_0630(pyk)
            CCV: CCV52592_1356(pyk)
            CHA: CHAB381_1635(pyk)
            CCO: CCC13826_0964(pyk) CCC13826_1323(pyk)
            ABU: Abu_0258(pyk)
            NIS: NIS_1773
            SUN: SUN_0436
            GSU: GSU3331(pyk)
            GME: Gmet_0122
            GUR: Gura_2655 Gura_4409
            PCA: Pcar_2983
            PPD: Ppro_1852
            DVU: DVU2514(pyk)
            DVL: Dvul_0731
            DDE: Dde_1032
            LIP: LI1095(pykF)
            BBA: Bd2099(pykA)
            DPS: DP3116
            ADE: Adeh_4234
            AFW: Anae109_4383
            MXA: MXAN_3514(pyk) MXAN_6299(pyk)
            SAT: SYN_02952
            SFU: Sfum_1475 Sfum_2959
            MLO: mll3819
            MES: Meso_3256
            PLA: Plav_2030
            SME: SMc04005(pykA)
            SMD: Smed_2676
            ATU: Atu3762(pykA)
            ATC: AGR_L_2146
            RET: RHE_CH03542(pykA)
            RLE: RL4060(pykA)
            BME: BMEI0292
            BMF: BAB1_1761(pyk)
            BMS: BR1748(pyk)
            BMB: BruAb1_1733(pyk)
            BOV: BOV_1688(pyk)
            OAN: Oant_1165
            BJA: blr7138(pykA)
            BRA: BRADO1185(pyk) BRADO5093(ttuE)
            BBT: BBta_5564(ttuE) BBta_6869(pyk)
            RPA: RPA2271 RPA4193(pyk)
            RPB: RPB_1423 RPB_3169
            RPC: RPC_2956 RPC_3982
            RPD: RPD_1402 RPD_2327
            RPE: RPE_3057 RPE_4110
            NWI: Nwi_0986
            NHA: Nham_1218
            BHE: BH15120(pykA)
            XAU: Xaut_2370
            CCR: CC_2051
            SIL: SPO3600(pyk)
            SIT: TM1040_2516
            RSP: RSP_1766(pykA) RSP_1848
            RSH: Rsph17029_0412 Rsph17029_0497
            RSQ: Rsph17025_2486
            JAN: Jann_0447
            RDE: RD1_1007(pyk)
            PDE: Pden_2276
            HNE: HNE_2098(pyk)
            ZMO: ZMO0152(pyk)
            NAR: Saro_0432
            SAL: Sala_0341
            SWI: Swit_3121
            ELI: ELI_14485
            GOX: GOX2250
            GBE: GbCGDNIH1_0363
            ACR: Acry_0178
            RRU: Rru_A2465
            MAG: amb1555 amb3174
            MGM: Mmc1_0728 Mmc1_1432
            ABA: Acid345_4085 Acid345_4669
            SUS: Acid_5001
            BSU: BG12661(pykA)
            BHA: BH3163(pykA)
            BAN: BA3382(pykA-1) BA4843(pykA-2)
            BAR: GBAA3382(pykA-1) GBAA4843(pykA-2)
            BAA: BA_3882 BA_5266
            BAT: BAS3136 BAS4492
            BCE: BC3323 BC4599
            BCA: BCE_3352(pykA) BCE_4729(pykA)
            BCZ: BCZK3030(pykA) BCZK4339(pykA)
            BTK: BT9727_3123(pykA) BT9727_4327(pykA)
            BTL: BALH_3005(pykA) BALH_4181(pykA)
            BLI: BL00402(pyk)
            BLD: BLi03067(pyk2)
            BCL: ABC2718(pykA)
            BAY: RBAM_026230
            BPU: BPUM_2561
            OIH: OB2171(pykA)
            GKA: GK2739
            SAU: SA1520(pykA)
            SAV: SAV1697(pykA)
            SAM: MW1641(pykA)
            SAR: SAR1776(pyk)
            SAS: SAS1625
            SAC: SACOL1745(pyk)
            SAB: SAB1556c(pyk)
            SAA: SAUSA300_1644(pyk)
            SAO: SAOUHSC_01806
            SEP: SE1373
            SER: SERP1261(pyk)
            SHA: SH1227(pykA)
            SSP: SSP1069
            LMO: lmo1570(pykA)
            LMF: LMOf2365_1592(pyk)
            LIN: lin1605(pykA)
            LWE: lwe1583(pykA)
            LLA: L0003(pyk)
            LLC: LACR_1456
            LLM: llmg_1119(pyk)
            SPY: SPy_1282(pyk)
            SPZ: M5005_Spy_0988(pyk)
            SPM: spyM18_1230(pyk)
            SPG: SpyM3_0912(pyk)
            SPS: SPs1111
            SPH: MGAS10270_Spy1102(pyk)
            SPI: MGAS10750_Spy1138(pyk)
            SPJ: MGAS2096_Spy1048(pyk)
            SPK: MGAS9429_Spy1092(pyk)
            SPF: SpyM50813(pyk)
            SPA: M6_Spy0975
            SPB: M28_Spy0960(pyk)
            SPN: SP_0897
            SPR: spr0797(pykF)
            SPD: SPD_0790(pyk)
            SAG: SAG0941(pyk)
            SAN: gbs0931
            SAK: SAK_1037(pyk)
            SMU: SMU.1190(pykF)
            STC: str1196(pyk)
            STL: stu1196(pyk)
            SSA: SSA_0848(pykF)
            SGO: SGO_1339(pyk)
            LPL: lp_1897(pyk)
            LJO: LJ1080
            LAC: LBA0957(kpyK)
            LSA: LSA1032(pyk)
            LSL: LSL_0867(pykF)
            LDB: Ldb0839(pyk)
            LBU: LBUL_0762
            LBR: LVIS_0765
            LCA: LSEI_1365
            LRE: Lreu_0751
            EFA: EF1046(pyk)
            OOE: OEOE_1002
            STH: STH838
            CAC: CAC0518(pykA) CAC1036(pykA)
            CPE: CPE0362(pykA) CPE1025(pykA) CPE2149(pykA)
            CPF: CPF_0351(pyk) CPF_1281 CPF_2404(pyk)
            CPR: CPR_0342(pyk) CPR_1103 CPR_2116(pyk)
            CTC: CTC02489
            CNO: NT01CX_1298
            CDF: CD3394(pykF)
            CBO: CBO3372(pyk)
            CBA: CLB_3428(pykA)
            CBH: CLC_3315(pykA)
            CBF: CLI_3556(pykA)
            CBE: Cbei_0485 Cbei_1412 Cbei_4851
            CKL: CKL_3558(pyk)
            CHY: CHY_1144(pyk)
            DSY: DSY1608(pyk)
            SWO: Swol_2040
            TTE: TTE1815(pykF)
            MTA: Moth_1867
            MGE: MG_216(pyk)
            MPN: MPN303(pyk)
            MPU: MYPU_2400(pyk)
            MPE: MYPE780(pyk)
            MGA: MGA_0156(pykF)
            MMY: MSC_0261(pyk)
            MMO: MMOB3210(pyk)
            MHY: mhp255(pyk)
            MHJ: MHJ_0122(pyk)
            MHP: MHP7448_0126(pyk)
            MSY: MS53_0648(pyk)
            MCP: MCAP_0221(pyk)
            UUR: UU186(pyk)
            POY: PAM287(pykF)
            AYW: AYWB_434(pykF)
            MFL: Mfl175
            MTU: Rv1617(pykA)
            MTC: MT1653(pyk)
            MBO: Mb1643(pykA)
            MBB: BCG_1655(pykA)
            MLE: ML1277(pykA)
            MPA: MAP1310(pykA)
            MAV: MAV_3170(pyk)
            MSM: MSMEG_0154(pyk) MSMEG_3227(pyk)
            MVA: Mvan_0632 Mvan_2824
            MGI: Mflv_0262 Mflv_3591
            MMC: Mmcs_0383 Mmcs_3042
            MKM: Mkms_0392 Mkms_3101
            MJL: Mjls_0371 Mjls_3058
            CGL: NCgl2008(cgl2089)
            CGB: cg2291(pyk)
            CEF: CE1989(pyk)
            CDI: DIP1553(pyk)
            CJK: jk0801(pyk)
            NFA: nfa18650(pykA)
            RHA: RHA1_ro01007(pyk1) RHA1_ro02565(pyk2) RHA1_ro03221(pyk3)
                 RHA1_ro04800(pyk4)
            SCO: SCO2014(pyk1) SCO5423(pyk2)
            SMA: SAV2825(pykA1) SAV6217(pykA2)
            TWH: TWT290(pyk)
            TWS: TW482(pyk)
            LXX: Lxx11340(pyk)
            ART: Arth_1693
            AAU: AAur_1844(pyk)
            PAC: PPA0769
            NCA: Noca_3020
            TFU: Tfu_1179
            FRA: Francci3_1678
            FAL: FRAAL4537(pykA)
            ACE: Acel_1080
            KRA: Krad_2959
            SEN: SACE_5720(pyk3)
            STP: Strop_3160
            BLO: BL0988(pyk)
            BAD: BAD_0678(pyk)
            RXY: Rxyl_0913
            FNU: FN1765
            RBA: RB10277(pykA)
            CTR: CT332(pykF)
            CTA: CTA_0360(pykF)
            CMU: TC0609
            CPN: CPn0097(pyk)
            CPA: CP0677
            CPJ: CPj0097(pyk)
            CPT: CpB0097
            CCA: CCA00675(pyk)
            CAB: CAB645(pyk)
            CFE: CF0336(pyk)
            PCU: pc1636(pyk)
            BGA: BG0349(pyk)
            BAF: BAPKO_0357(pyk)
            TDE: TDE2535(pyk)
            LIL: LA2924(pyk1) LB353(pyk2)
            LIC: LIC11132(pykA) LIC20264(pykF)
            LBJ: LBJ_2288(pykF) LBJ_4253(pykF)
            LBL: LBL_0819(pykF) LBL_4267(pykF)
            SYN: sll0587(pyk1) sll1275(pyk2)
            SYW: SYNW1298(pykF)
            SYC: syc1406_d(pyk)
            SYF: Synpcc7942_0098
            SYD: Syncc9605_1436
            SYE: Syncc9902_1063
            SYG: sync_1415(pyk)
            SYR: SynRCC307_1399(pykF)
            SYX: SynWH7803_1218(pykF)
            CYA: CYA_1210 CYA_2206(pyk)
            CYB: CYB_1545(pyk) CYB_2384
            TEL: tll2275 tlr0516
            GVI: gll1999 gll3323 gll3495
            ANA: all2564 all4008
            AVA: Ava_0494 Ava_1694
            PMA: Pro0923(pykF)
            PMM: PMM0912(pykF)
            PMT: PMT0679(pykF)
            PMN: PMN2A_0295
            PMI: PMT9312_0888
            PMB: A9601_09491(pykF)
            PMC: P9515_09951(pykF)
            PMF: P9303_15431(pykF)
            PMG: P9301_09471(pykF)
            PMH: P9215_09791
            PME: NATL1_09671(pykF)
            TER: Tery_2926
            BTH: BT_2841
            BFR: BF4482
            BFS: BF4277(pyk)
            SRU: SRU_1027(pykA)
            CHU: CHU_1400(pykF)
            GFO: GFO_3386(pyk)
            FJO: Fjoh_1141
            FPS: FP0204(pykA)
            RRS: RoseRS_1428
            RCA: Rcas_1692
            DRA: DR_2635
            DGE: Dgeo_0005
            TTH: TTC1611
            TTJ: TTHA0003
            TMA: TM0208
            TPT: Tpet_0716
            TME: Tmel_0922
            MMP: MMP1605
            MMQ: MmarC5_1803
            MMZ: MmarC7_0853
            MAE: Maeo_0544
            MVN: Mevan_0916
            MAC: MA3890(pyk)
            MBA: Mbar_A0175
            MMA: MM_0715
            MBU: Mbur_0469
            MHU: Mhun_0465
            MEM: Memar_0527
            HAL: VNG0324G(pykA)
            HMA: rrnAC0546(pykA)
            HWA: HQ1573A(pykA)
            NPH: NP1746A(pykA)
            TAC: Ta0896
            TVO: TVN1020
            PTO: PTO0336
            PAB: PAB1441
            PFU: PF1188
            TKO: TK0511
            RCI: LRC283(pyk)
            APE: APE_0489
            SMR: Smar_0899
            HBU: Hbut_0985
            SSO: SSO0981(pyk)
            STO: ST1617
            SAI: Saci_1648
            MSE: Msed_1412
            PAI: PAE0819
            PIS: Pisl_1106
            PCL: Pcal_0029
            PAS: Pars_0063
            TPE: Tpen_0330
STRUCTURES  PDB: 1A3W  1A3X  1A49  1A5U  1AQF  1E0T  1E0U  1F3W  1F3X  1LIU  
                 1LIW  1LIX  1LIY  1PKL  1PKM  1PKN  1PKY  1PYK  1T5A  1ZJH  
                 2G50  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.40
            ExPASy - ENZYME nomenclature database: 2.7.1.40
            ExplorEnz - The Enzyme Database: 2.7.1.40
            ERGO genome analysis and discovery system: 2.7.1.40
            BRENDA, the Enzyme Database: 2.7.1.40
            CAS: 9001-59-6
///
ENTRY       EC 2.7.1.41                 Enzyme
NAME        glucose-1-phosphate phosphodismutase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     D-glucose-1-phosphate:D-glucose-1-phosphate 6-phosphotransferase
REACTION    2 D-glucose 1-phosphate = D-glucose + D-glucose 1,6-bisphosphate
            [RN:R00016]
ALL_REAC    R00016 > R00960
SUBSTRATE   D-glucose 1-phosphate [CPD:C00103]
PRODUCT     D-glucose [CPD:C00031];
            D-glucose 1,6-bisphosphate [CPD:C00660]
REFERENCE   1  [PMID:15400363]
  AUTHORS   LELOIR LF, TRUCCO RE, et al.
  TITLE     The formation of glucose diphosphate by Escherichia coli.
  JOURNAL   Arch. Biochem. 24 (1949) 65-74.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Sidbury, J.B., Rosenberg, L.L. and Najjar, V.A.
  TITLE     Muscle glucose-1-phosphate transphosphorylase.
  JOURNAL   J. Biol. Chem. 222 (1956) 89-96.
  ORGANISM  Escherichia coli [GN:eco], rabbit
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K05344  glucose-1-phosphate phosphodismutase
GENES       SPZ: M5005_Spy_0528
            SPH: MGAS10270_Spy0523
            SPI: MGAS10750_Spy0547
            SPJ: MGAS2096_Spy0540
            SPK: MGAS9429_Spy0519
            SPA: M6_Spy0549
            LSL: LSL_1279
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.41
            ExPASy - ENZYME nomenclature database: 2.7.1.41
            ExplorEnz - The Enzyme Database: 2.7.1.41
            ERGO genome analysis and discovery system: 2.7.1.41
            BRENDA, the Enzyme Database: 2.7.1.41
            CAS: 9026-25-9
///
ENTRY       EC 2.7.1.42                 Enzyme
NAME        riboflavin phosphotransferase;
            riboflavine phosphotransferase;
            glucose-1-phosphate phosphotransferase;
            G-1-P phosphotransferase;
            D-glucose-1-phosphate:riboflavin 5'-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     alpha-D-glucose-1-phosphate:riboflavin 5'-phosphotransferase
REACTION    alpha-D-glucose 1-phosphate + riboflavin = D-glucose + FMN
            [RN:R00550]
ALL_REAC    R00550
SUBSTRATE   alpha-D-glucose 1-phosphate [CPD:C00103];
            riboflavin [CPD:C00255]
PRODUCT     D-glucose [CPD:C00031];
            FMN [CPD:C00061]
REFERENCE   1
  AUTHORS   Katagiri, H., Yamada, H. and Imai, K.
  TITLE     The transphosphorylation reactions catalyzed by glucose 1-phosphate
            phosphotransferases of Escherichia coli. I. Enzymic phosphorylation
            of riboflavine.
  JOURNAL   J. Biochem. (Tokyo) 46 (1959) 1119-1126.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.42
            ExPASy - ENZYME nomenclature database: 2.7.1.42
            ExplorEnz - The Enzyme Database: 2.7.1.42
            ERGO genome analysis and discovery system: 2.7.1.42
            BRENDA, the Enzyme Database: 2.7.1.42
            CAS: 9026-26-0
///
ENTRY       EC 2.7.1.43                 Enzyme
NAME        glucuronokinase;
            glucuronokinase (phosphorylating);
            glucurono-glucuronokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-glucuronate 1-phosphotransferase
REACTION    ATP + D-glucuronate = ADP + 1-phospho-alpha-D-glucuronate
            [RN:R01476]
ALL_REAC    R01476
SUBSTRATE   ATP [CPD:C00002];
            D-glucuronate [CPD:C00191]
PRODUCT     ADP [CPD:C00008];
            1-phospho-alpha-D-glucuronate
REFERENCE   1
  AUTHORS   Neufeld, E.F., Feingold, D.S. and Hassid, W.Z.
  TITLE     Enzymic phosphorylation of D-glucuronic acid by extracts from
            seedlings of Phaseolus aureus.
  JOURNAL   Arch. Biochem. Biophys. 83 (1959) 96-100.
  ORGANISM  Phaseolus aureus
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00053  Ascorbate and aldarate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.43
            ExPASy - ENZYME nomenclature database: 2.7.1.43
            ExplorEnz - The Enzyme Database: 2.7.1.43
            ERGO genome analysis and discovery system: 2.7.1.43
            BRENDA, the Enzyme Database: 2.7.1.43
            CAS: 9026-62-4
///
ENTRY       EC 2.7.1.44                 Enzyme
NAME        galacturonokinase;
            galacturonokinase (phosphorylating) D-galacturonic acid kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-galacturonate 1-phosphotransferase
REACTION    ATP + D-galacturonate = ADP + 1-phospho-alpha-D-galacturonate
            [RN:R01980]
ALL_REAC    R01980
SUBSTRATE   ATP [CPD:C00002];
            D-galacturonate [CPD:C00333]
PRODUCT     ADP [CPD:C00008];
            1-phospho-alpha-D-galacturonate [CPD:C04037]
REFERENCE   1
  AUTHORS   Neufeld, E.F., Feingold, D.S., Ilves, S.M., Kessler, G. and Hassid,
            W.Z.
  TITLE     Phosphorylation of D-galacturonic acid by extracts from germinating
            seeds of Phaseolus aureus.
  JOURNAL   J. Biol. Chem. 236 (1961) 3102-3105.
  ORGANISM  Phaseolus aureus
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.44
            ExPASy - ENZYME nomenclature database: 2.7.1.44
            ExplorEnz - The Enzyme Database: 2.7.1.44
            ERGO genome analysis and discovery system: 2.7.1.44
            BRENDA, the Enzyme Database: 2.7.1.44
            CAS: 9026-63-5
///
ENTRY       EC 2.7.1.45                 Enzyme
NAME        2-dehydro-3-deoxygluconokinase;
            2-keto-3-deoxygluconokinase;
            2-keto-3-deoxy-D-gluconic acid kinase;
            2-keto-3-deoxygluconokinase (phosphorylating);
            2-keto-3-deoxygluconate kinase;
            ketodeoxygluconokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:2-dehydro-3-deoxy-D-gluconate 6-phosphotransferase
REACTION    ATP + 2-dehydro-3-deoxy-D-gluconate = ADP +
            6-phospho-2-dehydro-3-deoxy-D-gluconate [RN:R01541]
ALL_REAC    R01541
SUBSTRATE   ATP [CPD:C00002];
            2-dehydro-3-deoxy-D-gluconate [CPD:C00204]
PRODUCT     ADP [CPD:C00008];
            6-phospho-2-dehydro-3-deoxy-D-gluconate [CPD:C04442]
REFERENCE   1  [PMID:13813474]
  AUTHORS   CYNKIN MA, ASHWELL G.
  TITLE     Uronic acid metabolism in bacteria. IV. Purification and properties
            of 2-keto-3-deoxy-D-gluconokinase in Escherichia coli.
  JOURNAL   J. Biol. Chem. 235 (1960) 1576-9.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00030  Pentose phosphate pathway
            PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K00874  2-dehydro-3-deoxygluconokinase
GENES       ECO: b3526(kdgK)
            ECE: Z4940(kdgK)
            ECS: ECs4406
            ECC: c4337(kdgK)
            ECI: UTI89_C1968(ydjH) UTI89_C4058(kdgK)
            ECP: ECP_3626
            ECW: EcE24377A_4014(kdgK)
            ECX: EcHS_A3729(kdgK)
            STY: STY4191(kdgK)
            STT: t3905(kdgK)
            SPT: SPA3468(kdgK)
            SEC: SC3546(kdgK)
            STM: STM3612(kdgK)
            YPE: YPO3990(kdgK)
            YPK: y3838(kdgK)
            YPM: YP_3353(kdgK)
            YPA: YPA_3818
            YPN: YPN_3640
            YPS: YPTB3830(kdgK)
            YPI: YpsIP31758_4062(kdgK)
            SFL: SF3557(kdgK)
            SFX: S4209(kdgK)
            SFV: SFV_3562(kdgK)
            SSN: SSON_3865(kdgK)
            SBO: SBO_3525(kdgK)
            ECA: ECA4360(kdgK)
            PLU: plu0177(kdgK)
            SGL: SG0067
            HSO: HS_1329(kdgK)
            MSU: MS0545(rbsK) MS0565(rbsK)
            APL: APL_1019(kdgK)
            XCC: XCC0118(kdgK)
            XCB: XC_0122
            XCV: XCV0122(kdgK)
            XAC: XAC0143(kdgK)
            XOO: XOO0028(kdgK)
            XOM: XOO_0027(XOO0027)
            VVU: VV2_0905 VV2_1071
            VVY: VV0554 VVA1388 VVA1595
            VPA: VPA0082 VPA1707
            VFI: VFA0988
            PPR: PBPRA1275 PBPRB0158(kdgK) PBPRB1733 PBPRB1882
            PAE: PA2261
            PPU: PP_3378(kguK)
            PST: PSPTO_2782(kdgK)
            PSB: Psyr_2510(pfkB)
            PSP: PSPPH_2667(kdgK)
            PFL: PFL_2719 PFL_3580(kdgK)
            PFO: Pfl_2902(pfkB) Pfl_3085(pfkB)
            PHA: PSHAa1745
            PAT: Patl_3657
            SDE: Sde_0939 Sde_2656
            CBU: CBU_1223(kdgK)
            CBD: COXBU7E912_1308(kdgK)
            REU: Reut_B4023(pfkB)
            REH: H16_B1212(kdgK)
            RME: Rmet_4769
            BMA: BMA0961(kdgK)
            BXE: Bxe_A1980
            BUR: Bcep18194_A5029
            BAM: Bamb_1654
            BPS: BPSL1575
            BPM: BURPS1710b_2288(kdgK) BURPS1710b_2326
            BTE: BTH_I2260 BTH_I2296
            POL: Bpro_1737
            MLO: mlr1166
            SME: SMc01531(kdgK)
            ATU: Atu2296(kdgK)
            ATC: AGR_C_4170
            RET: RHE_CH03102(kdgK)
            RLE: RL3548(kdgK)
            BME: BMEI1108
            BMS: BR0858
            BMB: BruAb1_0870
            BJA: blr3922(kdgK)
            BRA: BRADO1805(kdgK)
            BBT: BBta_2125(kdgK)
            CCR: CC_1057 CC_1496
            SIL: SPO2420(kdgK)
            RSP: RSP_0490
            RDE: RD1_0669(kdgK)
            BSU: BG11397(kdgK)
            BHA: BH3724(kdgK)
            BAN: BA5097
            BAR: GBAA5097
            BAA: BA_5516(pfkB)
            BAT: BAS4737
            BCE: BC4843
            BCA: BCE_5000
            BCZ: BCZK4596(kdgK) pE33L466_0342(kdgK)
            BTK: BT9727_4577(kdgK)
            BTL: BALH_4410(kdgK)
            BLI: BL02471(kdgK) BL03849
            BLD: BLi03827(kdgK) BLi04072
            BCL: ABC0522(kdgK) ABC3352
            BAY: RBAM_017950
            BPU: BPUM_3244(kdgK)
            OIH: OB2213(kdgK) OB2698 OB3202
            GKA: GK1957
            SHA: SH2650
            LLA: L0021(kdgK)
            LLC: LACR_1741
            SPY: SPy_0638(kdgK)
            SPZ: M5005_Spy_0526
            SPM: spyM18_0701(kdgK)
            SPG: SpyM3_0450(kdgK)
            SPS: SPs1406
            SPH: MGAS10270_Spy0521 MGAS10270_Spy1175
            SPI: MGAS10750_Spy0545
            SPJ: MGAS2096_Spy0538
            SPK: MGAS9429_Spy0517
            SPA: M6_Spy0547
            SPB: M28_Spy0505
            SPN: SP_0318
            SPR: spr0288(kdgK)
            SAG: SAG0697 SAG1906
            SAN: gbs0670 gbs1893
            SAK: SAK_0823
            LPL: lp_0253(kdgK)
            LSA: LSA0291(kdgK)
            LBR: LVIS_0128 LVIS_0325 LVIS_0441
            LCA: LSEI_2673
            EFA: EF0424 EF0840 EF2265
            OOE: OEOE_0130
            CAC: CAC0395(kdgK) CAC2684
            CPE: CPE0146
            CNO: NT01CX_1478
            CBO: CBO0293(kdgK)
            DSY: DSY3305
            MTA: Moth_0419(pfkB)
            MSM: MSMEG_3785
            SCO: SCO3494(SCE65.30c)
            TWH: TWT646(kdgK)
            TWS: TW668
            AAU: AAur_4063(kdgK)
            PAC: PPA0370 PPA0883
            SEN: SACE_4935(kdgK) SACE_5974(kdgK)
            RXY: Rxyl_0078
            RBA: RB8731(kdgK)
            PMB: A9601_18371
            PMC: P9515_18161
            PMF: P9303_01731
            PMG: P9301_18191
            PMH: P9215_19011(rbsK)
            PME: NATL1_20791
            BTH: BT_0488
            BFR: BF2700
            BFS: BF2719
            GFO: GFO_1161(kdgK) GFO_1708(kdgK)
            TTJ: TTHB079
            TMA: TM0067
            HMA: rrnAC2551(kdgK)
            HWA: HQ1455A(kdgK)
            NPH: NP3184A(suk)
STRUCTURES  PDB: 1WYE  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.45
            ExPASy - ENZYME nomenclature database: 2.7.1.45
            ExplorEnz - The Enzyme Database: 2.7.1.45
            ERGO genome analysis and discovery system: 2.7.1.45
            BRENDA, the Enzyme Database: 2.7.1.45
            CAS: 9026-54-4
///
ENTRY       EC 2.7.1.46                 Enzyme
NAME        L-arabinokinase;
            L-arabinokinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:L-arabinose 1-phosphotransferase
REACTION    ATP + L-arabinose = ADP + beta-L-arabinose 1-phosphate [RN:R01754]
ALL_REAC    R01754
SUBSTRATE   ATP [CPD:C00002];
            L-arabinose [CPD:C00259]
PRODUCT     ADP [CPD:C00008];
            beta-L-arabinose 1-phosphate [CPD:C03906]
REFERENCE   1
  AUTHORS   Neufeld, E.F., Feingold, D.S. and Hassid, W.Z.
  TITLE     Phosphorylation of D-galactose and L-arabinose by extracts from
            Phaseolus aureus seedlings.
  JOURNAL   J. Biol. Chem. 235 (1960) 906-909.
  ORGANISM  Phaseolus aureus
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.46
            ExPASy - ENZYME nomenclature database: 2.7.1.46
            ExplorEnz - The Enzyme Database: 2.7.1.46
            ERGO genome analysis and discovery system: 2.7.1.46
            BRENDA, the Enzyme Database: 2.7.1.46
            CAS: 37277-99-9
///
ENTRY       EC 2.7.1.47                 Enzyme
NAME        D-ribulokinase;
            D-ribulokinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-ribulose 5-phosphotransferase
REACTION    ATP + D-ribulose = ADP + D-ribulose 5-phosphate [RN:R01526]
ALL_REAC    R01526
SUBSTRATE   ATP [CPD:C00002];
            D-ribulose [CPD:C00309]
PRODUCT     ADP [CPD:C00008];
            D-ribulose 5-phosphate [CPD:C00199]
REFERENCE   1  [PMID:13825363]
  AUTHORS   FROMM HJ.
  TITLE     D-Ribulokinase from Aerobacter aerogenes.
  JOURNAL   J. Biol. Chem. 234 (1959) 3097-101.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K00875  D-ribulokinase
GENES       CME: CMF097C
            BXE: Bxe_B0680
            ATU: Atu4324
            ATC: AGR_L_1075
            RLE: pRL90117
            BME: BMEII0979
            BMF: BAB2_0934
            BMS: BRA0269
            BMB: BruAb2_0911
            BJA: blr3226
            RSP: RSP_3705
            GOX: GOX2186
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.47
            ExPASy - ENZYME nomenclature database: 2.7.1.47
            ExplorEnz - The Enzyme Database: 2.7.1.47
            ERGO genome analysis and discovery system: 2.7.1.47
            BRENDA, the Enzyme Database: 2.7.1.47
            CAS: 9026-40-8
///
ENTRY       EC 2.7.1.48                 Enzyme
NAME        uridine kinase;
            pyrimidine ribonucleoside kinase;
            uridine-cytidine kinase;
            uridine kinase (phosphorylating);
            uridine phosphokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:uridine 5'-phosphotransferase
REACTION    ATP + uridine = ADP + UMP [RN:R00964]
ALL_REAC    R00964;
            (other) R00513 R00516 R00517 R00962 R00967 R00968 R00970 R01548
            R01549 R01880 R02091 R02096 R02097 R02327 R02332 R02371 R02372
SUBSTRATE   ATP [CPD:C00002];
            uridine [CPD:C00299]
PRODUCT     ADP [CPD:C00008];
            UMP [CPD:C00105]
COMMENT     Cytidine can act as acceptor; GTP and ITP can act as donors.
REFERENCE   1  [PMID:5782006]
  AUTHORS   Orengo A.
  TITLE     Regulation of enzymic activity by metabolites. I. Uridine-cytidine
            kinase of Novikoff ascites rat tumor.
  JOURNAL   J. Biol. Chem. 244 (1969) 2204-9.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Skold, O.
  TITLE     Uridine kinase from Erlich ascites tumor: purification and
            properties.
  JOURNAL   J. Biol. Chem. 235 (1960) 3273-3279.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K00876  uridine kinase
GENES       HSA: 7371(UCK2) 83549(UCK1)
            MMU: 22245(Uck1) 80914(Uck2)
            CFA: 608503(UCK1)
            GGA: 424406(UCK2) 771901(UCK1)
            XLA: 398966(MGC68736) 444114(MGC80465) 494739(LOC494739)
                 496224(LOC496224)
            SPU: 588945(LOC588945)
            DME: Dmel_CG4798(l(2)k01209) Dmel_CG6364
            CEL: B0001.4
            CME: CME192C
            SCE: YNR012W(URK1)
            AGO: AGOS_ADR288W
            PIC: PICST_81319(URK1)
            CGR: CAGL0I05654g
            SPO: SPCC162.11c
            ANI: AN7502.2
            AFM: AFUA_2G05430
            AOR: AO090001000654 AO090001000655
            UMA: UM02015.1
            DDI: DDB_0216233(udkA) DDB_0230208(udkB)
            TET: TTHERM_01205370
            LMA: LmjF31.2470
            EHI: 139.t00020 172.t00013 253.t00011 369.t00002 8.t00069
            ECO: b2066(udk)
            ECJ: JW2051(udk)
            ECE: Z3234(udk)
            ECS: ECs2873
            ECC: c2593(udk)
            ECI: UTI89_C2342(udk)
            ECP: ECP_2106
            ECV: APECO1_1157(udk)
            ECW: EcE24377A_2359(udk)
            ECX: EcHS_A2206(udk)
            STY: STY2335(udk)
            STT: t0750(udk)
            SPT: SPA0744(udk)
            SEC: SC2124(udk)
            STM: STM2122(udk)
            YPE: YPO1524(udk)
            YPK: y2646(udk)
            YPM: YP_1413(udk)
            YPA: YPA_0818
            YPN: YPN_2456
            YPP: YPDSF_1452
            YPS: YPTB1536(udk)
            YPI: YpsIP31758_2453(udk)
            SFL: SF2130(udk)
            SFX: S2254(udk)
            SFV: SFV_2125(udk)
            SSN: SSON_2119(udk)
            SBO: SBO_0893(udk)
            SDY: SDY_2196(udk)
            ECA: ECA1411(udk)
            PLU: plu1556(udk)
            SGL: SG0973
            ENT: Ent638_2680
            SPE: Spro_1162
            HIN: HI0132(udk)
            HIT: NTHI0218(udk)
            HIP: CGSHiEE_02655
            HIQ: CGSHiGG_03240
            HDU: HD1660(udk)
            HSO: HS_0644(udk)
            PMU: PM0952(udk)
            MSU: MS1582(udk)
            APL: APL_0834(udk)
            ASU: Asuc_1573
            VCH: VC1038
            VCO: VC0395_A0556(udk)
            VVU: VV1_3025
            VVY: VV1261
            VPA: VP2067
            VFI: VF1752
            PPR: PBPRA1170(udk)
            SON: SO_2617(udk)
            SDN: Sden_2054
            SFR: Sfri_2244
            SAZ: Sama_2047
            SBL: Sbal_2463
            SBM: Shew185_1102
            SLO: Shew_1575
            SPC: Sputcn32_2218
            SHE: Shewmr4_1657
            SHM: Shewmr7_1732
            SHN: Shewana3_1762
            SHW: Sputw3181_1791
            ILO: IL1536(udk)
            CPS: CPS_1974(udk)
            PHA: PSHAb0080(udk)
            PAT: Patl_0533
            PIN: Ping_1489
            CBU: CBU_0872(udk)
            CBD: COXBU7E912_0935(udk)
            LPN: lpg1165(udk) lpg1853(udk)
            LPF: lpl1173 lpl1819(udk)
            LPP: lpp1167 lpp1820(udk)
            FTU: FTT0702(udk)
            FTF: FTF0702(udk)
            FTW: FTW_1541(udk)
            FTL: FTL_1534
            FTH: FTH_1484(udk)
            FTA: FTA_1618(udk)
            FTN: FTN_0612(udk)
            HCH: HCH_00098(udk)
            MMW: Mmwyl1_1075
            AHA: AHA_2235(udk)
            CVI: CV_1085(udk)
            BBA: Bd1530(udk) Bd2645(udk)
            MXA: MXAN_4159(udk)
            MMR: Mmar10_0044
            HNE: HNE_3440
            SWI: Swit_4380
            ABA: Acid345_3054
            SUS: Acid_3182
            BSU: BG12696(udk)
            BHA: BH1275(udk)
            BAN: BA3070 BA4608(udk)
            BAR: GBAA3070 GBAA4608(udk)
            BAA: BA_3577 BA_5049
            BAT: BAS2856 BAS4276
            BCE: BC2991 BC3046 BC4375
            BCA: BCE_4462(udk)
            BCZ: BCZK2728(udk) BCZK2788 BCZK4124(udk)
            BTK: BT9727_2748(udk) BT9727_2828 BT9727_4113(udk)
            BTL: BALH_3965(udk)
            BLI: BL02025(udk)
            BLD: BLi02861(udk)
            BCL: ABC1598(udk)
            BAY: RBAM_024430(udk)
            BPU: BPUM_2369(udk)
            OIH: OB2003(udk)
            GKA: GK0179 GK2548
            GTN: GTNG_2481(udk)
            SAU: SA1439(udk)
            SAV: SAV1611(udk)
            SAM: MW1561(udk)
            SAR: SAR1690(udk)
            SAS: SAS1547
            SAC: SACOL1666(udk)
            SAB: SAB1482c(udk)
            SAA: SAUSA300_1568(udk)
            SAO: SAOUHSC_01715
            SAJ: SaurJH9_1125
            SAH: SaurJH1_1147
            SEP: SE1294
            SER: SERP1175(udk)
            SHA: SH1308(udk)
            SSP: SSP1150
            LMO: lmo1497(udk)
            LMF: LMOf2365_1516(udk)
            LIN: lin1532(udk)
            LWE: lwe1510(udk)
            LLA: L108994(udk)
            LLC: LACR_1825
            LLM: llmg_0762(udk)
            SPY: SPy_1368(udk)
            SPZ: M5005_Spy_1116(udk)
            SPM: spyM18_1380(udk)
            SPG: SpyM3_1042(udk)
            SPS: SPs0818
            SPH: MGAS10270_Spy1186(udk)
            SPI: MGAS10750_Spy1216(udk)
            SPJ: MGAS2096_Spy1179 MGAS2096_Spy1180(udk)
            SPK: MGAS9429_Spy1163(udk)
            SPF: SpyM50744(udk)
            SPA: M6_Spy1090
            SPB: M28_Spy1109(udk)
            SPN: SP_1208
            SPR: spr1090(udK)
            SPD: SPD_1068(udk)
            SAG: SAG0826(udk)
            SAN: gbs0844
            SAK: SAK_0950(udk)
            SMU: SMU.1386(urk)
            STC: str1260(udk)
            STL: stu1260(udk)
            SSA: SSA_0105 SSA_0966(udk)
            SGO: SGO_0951(udk)
            LPL: lp_1562(udk)
            LJO: LJ0763
            LAC: LBA0577
            LSA: LSA1373(udk)
            LSL: LSL_0816(udk)
            LDB: Ldb0515(udk2) Ldb0516(udk1)
            LBU: LBUL_0456 LBUL_0457
            LBR: LVIS_1007
            LCA: LSEI_1669
            LGA: LGAS_0537
            PPE: PEPE_0724
            EFA: EF0825(udk)
            OOE: OEOE_1033
            STH: STH1046
            CAC: CAC0672
            CPE: CPE1347 CPE1770
            CPF: CPF_1554 CPF_2023(udk)
            CPR: CPR_1347 CPR_1740(udk)
            CTC: CTC00344 CTC01064
            CNO: NT01CX_1382 NT01CX_2269
            CBO: CBO2554(udk)
            CBA: CLB_2495(udk)
            CBH: CLC_2425(udk)
            CBF: CLI_2617(udk)
            DSY: DSY1895
            SWO: Swol_1101
            TTE: TTE1778(udk)
            MGE: MG_382(udk)
            MPN: MPN561(udk)
            MGA: MGA_0106(udk)
            MMY: MSC_0552(udk)
            MCP: MCAP_0422(udk)
            UUR: UU332(udk)
            POY: PAM142(rplM)
            AYW: AYWB_578(udk)
            MFL: Mfl306
            PAC: PPA1725
            SEN: SACE_1035
            CPN: CPn0735
            CPA: CP0011
            CPJ: CPj0735
            CPT: CpB0763
            BBU: BB0015(udk)
            BGA: BG0015(udk)
            BAF: BAPKO_0014(udk)
            TPA: TP0667
            TDE: TDE2289
            SYW: SYNW1344
            SYD: Syncc9605_1493
            SYE: Syncc9902_1007
            SYG: sync_1595
            SYX: SynWH7803_1367(udk)
            PMM: PMM0989
            PMN: PMN2A_0388
            PMI: PMT9312_0995
            PMB: A9601_10701
            PMC: P9515_10681(udk)
            PMG: P9301_10701
            PME: NATL1_10701
            BTH: BT_0184 BT_2527
            BFR: BF3195
            BFS: BF3035(udk)
            PGI: PG1745 PG1781(udk)
            SRU: SRU_0527(udk)
            CHU: CHU_0115(udk)
            GFO: GFO_0812(udk)
            FPS: FP1119(udk)
            DRA: DR_0159
            DGE: Dgeo_0202
            TTH: TTC0210
            TTJ: TTHA0578
            TMA: TM0751
            HAL: VNG1219G(urk)
STRUCTURES  PDB: 1UDW  1UEI  1UEJ  1UFQ  1UJ2  1XRJ  2JEO  2UVQ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.48
            ExPASy - ENZYME nomenclature database: 2.7.1.48
            ExplorEnz - The Enzyme Database: 2.7.1.48
            ERGO genome analysis and discovery system: 2.7.1.48
            BRENDA, the Enzyme Database: 2.7.1.48
            CAS: 9026-39-5
///
ENTRY       EC 2.7.1.49                 Enzyme
NAME        hydroxymethylpyrimidine kinase;
            hydroxymethylpyrimidine kinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:4-amino-5-hydroxymethyl-2-methylpyrimidine 5-phosphotransferase
REACTION    ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine = ADP +
            4-amino-5-phosphonooxymethyl-2-methylpyrimidine [RN:R03471]
ALL_REAC    R03471
SUBSTRATE   ATP [CPD:C00002];
            4-amino-5-hydroxymethyl-2-methylpyrimidine [CPD:C01279]
PRODUCT     ADP [CPD:C00008];
            4-amino-5-phosphonooxymethyl-2-methylpyrimidine
COMMENT     CTP, UTP and GTP can act as donors.
REFERENCE   1
  AUTHORS   Lewin, L.M. and Brown, G.M.
  TITLE     The biosynthesis of thiamine. III. Mechanism of enzymatic formation
            of the pyrophosphate ester of
            2-methyl-4-amino-5-hydroxymethylpyrimidine.
  JOURNAL   J. Biol. Chem. 236 (1961) 2768-2771.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00730  Thiamine metabolism
ORTHOLOGY   KO: K00877  hydroxymethylpyrimidine kinase
GENES       ECO: b2103(thiD)
            ECJ: JW2090(thiD)
            ECE: Z3267(thiD)
            ECS: ECs2906
            ECC: c2630(thiD)
            ECI: UTI89_C2377(thiD)
            ECP: ECP_2141
            STY: STY2375(thiD)
            STT: t0710(thiD)
            SPT: SPA0706(thiD)
            SEC: SC2161(thiD)
            STM: STM2146(thiD)
            YPE: YPO2859(thiD)
            YPK: y1373(thiD)
            YPM: YP_2725(thiD)
            YPA: YPA_2299
            YPN: YPN_1278
            YPS: YPTB2824(thiD)
            SFL: SF2165(thiD)
            SFX: S2290(thiD)
            SFV: SFV_2158(thiD)
            SSN: SSON_2151(thiD)
            SBO: SBO_0924(thiD)
            SDY: SDY_2277(thiD)
            ECA: ECA3196(thiD)
            PLU: plu2782(thiD)
            WBR: WGLp318(thiD)
            HIN: HI0416(thiD)
            HSO: HS_0091(thiD)
            PMU: PM1261(thiD)
            MSU: MS0677(thiD)
            APL: APL_0539(thiD)
            XFA: XF0621
            XFT: PD1534(thiD)
            XCC: XCC1735(thiD)
            XAC: XAC1753(thiD)
            VCH: VC1296
            VVU: VV2_1433
            VVY: VVA0267
            VPA: VPA0136
            VFI: VFA0316
            PPR: PBPRB0688
            PAE: PA3975(thiD)
            PPU: PP_4782(thiD)
            PST: PSPTO_4798
            PSB: Psyr_4340
            PSP: PSPPH_4382
            PFL: PFL_5427(thiD)
            PFO: Pfl_4945
            PEN: PSEEN4802(thiD)
            PAR: Psyc_0167(thiD)
            PCR: Pcryo_0179
            ACI: ACIAD0875(thiD)
            TCX: Tcr_0143
            NOC: Noc_1265
            BCI: BCI_0649(thiD)
            VOK: COSY_0854(thiD)
            NME: NMB1616
            NMA: NMA1815(thiD)
            CVI: CV_0151(thiD)
            RSO: RSc0100(thiD)
            RME: Rmet_0169
            BMA: BMA1577(thiD) BMA2000
            BXE: Bxe_A3814
            BUR: Bcep18194_A3959 Bcep18194_A5350
            BPS: BPSL2181(thiD) BPSL2696 BPSS1104
            BPM: BURPS1710b_2604(thiD) BURPS1710b_3174(thiD)
                 BURPS1710b_A0060(thiD2)
            BTE: BTH_I1459 BTH_I2005(thiD)
            BPE: BP3598(thiD)
            BPA: BPP3987(thiD)
            BBR: BB4460(thiD)
            RFR: Rfer_2470
            POL: Bpro_1134 Bpro_2331
            MPT: Mpe_A3192
            NEU: NE1425(thiD)
            NMU: Nmul_A2627
            EBA: ebA1745(thiD)
            DAR: Daro_3900
            TBD: Tbd_2555
            HPY: HP0844(thi)
            HPJ: jhp0782(thiD)
            CJE: Cj1082c(thiD)
            CJU: C8J_1023(thiD)
            DVU: DVU0931(thiD)
            DDE: Dde_2688
            LIP: LI0782(thiD)
            DPS: DP0916(thiD)
            SAT: SYN_01521
            MLO: mll5788
            SME: SMb20962(thiD)
            ATU: Atu3290(thiD)
            ATC: AGR_L_3056
            RLE: pRL110441(thiD)
            BME: BMEI1732
            BMF: BAB1_0219
            BMS: BR0218(thiD)
            BJA: bll5905(thiD)
            BRA: BRADO5133(thiD)
            BBT: BBta_5600(thiD)
            RPA: RPA3971(thiD)
            RPE: RPE_1463
            NWI: Nwi_1082
            BHE: BH16280(thiD2)
            BQU: BQ13200(thiD2)
            CCR: CC_3223
            SIL: SPO0045(thiD)
            RSP: RSP_0647(thiD)
            RDE: RD1_0746(thiD) RD1_3612(thiD)
            MMR: Mmar10_0552
            GBE: GbCGDNIH1_1113
            BSU: BG13151(yjbV)
            BHA: BH1435
            BAN: BA0734(thiD-1)
            BAR: GBAA0734(thiD-1)
            BAA: BA_1322(pfkB)
            BAT: BAS0700
            BCE: BC0751
            BCA: BCE_0804(thiD)
            BTK: BT9727_0644(thiD)
            BTL: BALH_0671(thiD)
            BLI: BL01586(thiDA)
            OIH: OB0474
            LMO: lmo0317
            LMF: LMOf2365_0335(thiD-1)
            LIN: lin0342
            LLC: LACR_1376
            SPZ: M5005_Spy_1616(thiD)
            SPH: MGAS10270_Spy1684(thiD)
            SPI: MGAS10750_Spy1671(thiD)
            SPJ: MGAS2096_Spy1640(thiD)
            SPK: MGAS9429_Spy1619(thiD)
            SPA: M6_Spy1624
            SPB: M28_Spy1605(thiD)
            STH: STH156
            CAC: CAC3095(thiK)
            CPE: CPE1338(thiD)
            CPF: CPF_1545(thiD)
            CPR: CPR_1338(thiD)
            CTC: CTC01753
            DSY: DSY1405
            SWO: Swol_0639
            TTE: TTE2235(thiD)
            MTU: Rv0422c(thiD)
            MTC: MT0436(thiD)
            MBO: Mb0430c(thiD)
            MLE: ML0295(thiD)
            MPA: MAP3912c(thiD)
            CGL: NCgl1407(cgl1463)
            CEF: CE1591
            CJK: jk0297(thiD)
            SCO: SCO5563(SC7A1.07)
            SMA: SAV7205(thiD)
            PAC: PPA0110
            TFU: Tfu_2250
            FRA: Francci3_3612
            FAL: FRAAL5819(thiD)
            SEN: SACE_1297(thiD)
            BLO: BL0113(thiD)
            BAD: BAD_1146(thiD)
            FNU: FN1759
            LIL: LA0130(thiD)
            PMB: A9601_03951(thiD)
            PMC: P9515_04031(thiD)
            PMG: P9301_03941(thiD)
            PMH: P9215_04001(thiD)
            BTH: BT_0790
            BFR: BF2259
            CHU: CHU_0241(thiD)
            CTE: CT1176(thiD)
            DRA: DR_A0171
            DGE: Dgeo_1919
            TTH: TTC0321
            TTJ: TTHA0680
            TMA: TM0790
            MJA: MJ0236
            MAC: MA3197(thiD)
            MBA: Mbar_A3501
            MMA: MM_0338
            MBU: Mbur_2182
            MSI: Msm_0289
            MKA: MK0589(thiD)
            AFU: AF2208(thiD)
            HAL: VNG2606G(thiD)
            NPH: NP0546A(thiD)
            TAC: Ta1281
            PTO: PTO1290
            PHO: PH1155
            PAB: PAB1646(thiD)
            PFU: PF1333
            APE: APE_2400.1
            SSO: SSO2393(thiD-2)
            STO: ST0526
            SAI: Saci_0953
            PAI: PAE2535
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.49
            ExPASy - ENZYME nomenclature database: 2.7.1.49
            ExplorEnz - The Enzyme Database: 2.7.1.49
            ERGO genome analysis and discovery system: 2.7.1.49
            BRENDA, the Enzyme Database: 2.7.1.49
            CAS: 9026-55-5
///
ENTRY       EC 2.7.1.50                 Enzyme
NAME        hydroxyethylthiazole kinase;
            hydroxyethylthiazole kinase (phosphorylating);
            4-methyl-5-(beta-hydroxyethyl)thiazole kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:4-methyl-5-(2-hydroxyethyl)thiazole 2-phosphotransferase
REACTION    ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP +
            4-methyl-5-(2-phosphonooxyethyl)thiazole [RN:R04448]
ALL_REAC    R04448
SUBSTRATE   ATP [CPD:C00002];
            4-methyl-5-(2-hydroxyethyl)thiazole
PRODUCT     ADP [CPD:C00008];
            4-methyl-5-(2-phosphonooxyethyl)thiazole
REFERENCE   1
  AUTHORS   Lewin, L.M. and Brown, G.M.
  TITLE     The biosynthesis of thiamine. III. Mechanism of enzymatic formation
            of the pyrophosphate ester of
            2-methyl-4-amino-5-hydroxymethylpyrimidine.
  JOURNAL   J. Biol. Chem. 236 (1961) 2768-2771.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00730  Thiamine metabolism
ORTHOLOGY   KO: K00878  hydroxyethylthiazole kinase
GENES       ATH: AT3G24030
            OSA: 4325819
            SCE: YPL214C(THI6)
            AGO: AGOS_AFL110C
            CGR: CAGL0E05808g
            SPO: SPAC23H4.10c(thi4)
            CNE: CNI03710
            PFA: PFL1920c
            ECO: b2104(thiM)
            ECJ: JW2091(thiM)
            ECE: Z3268(thiM)
            ECS: ECs2907
            ECC: c2631(thiM)
            ECI: UTI89_C2378(thiM)
            ECP: ECP_2142
            ECV: APECO1_4441(thiM)
            ECW: EcE24377A_2392(thiM)
            ECX: EcHS_A2240(thiM)
            STY: STY2376
            STT: t0709
            SPT: SPA0705(thiM)
            SEC: SC2162(thiM)
            STM: STM2147(thiM)
            YEN: YE3599(thiM)
            SFL: SF2166(thiM)
            SFX: S2291(thiM)
            SFV: SFV_2159(thiM)
            SSN: SSON_2152(thiM)
            SBO: SBO_0925(thiM)
            SDY: SDY_2278(thiM)
            ECA: ECA3197(thiM)
            SGL: SG1739
            ENT: Ent638_2711
            SPE: Spro_3578
            HIN: HI0415(thim)
            HIT: NTHI0540(thiM)
            HIP: CGSHiEE_00930
            HIQ: CGSHiGG_05260
            HSO: HS_0092(thiM)
            PMU: PM1262(thiM)
            ASU: Asuc_1506
            VPA: VPA0131
            VFI: VFA0321
            PPR: PBPRA2337(thiM)
            PRW: PsycPRwf_0830
            ACI: ACIAD2011(thiM)
            PIN: Ping_2373
            DNO: DNO_0932
            CVI: CV_0024
            BPS: BPSS1135
            BPM: BURPS1710b_A0097
            BTE: BTH_II1271
            RFR: Rfer_2472
            HPY: HP0845(thiM)
            HPJ: jhp0783(thiM)
            HPA: HPAG1_0830
            DVU: DVU2363(thiM)
            DVL: Dvul_0899
            DDE: Dde_1378
            DPS: DP0499
            SAT: SYN_00303
            SFU: Sfum_3507
            ATU: Atu3288
            ATC: AGR_L_3060
            RET: RHE_PE00337(thiM)
            RLE: pRL110443(thiM)
            RSP: RSP_0649(thiM)
            RSH: Rsph17029_2302
            RSQ: Rsph17025_0583
            RDE: RD1_3610(thiM)
            NAR: Saro_2746
            GBE: GbCGDNIH1_0300
            BSU: BG10571(thiK)
            BHA: BH3349(thiK)
            BAN: BA0376(thiM)
            BAR: GBAA0376(thiM)
            BAA: BA_0952
            BAT: BAS0362
            BCE: BC0419
            BCA: BCE_0486(thiM)
            BCZ: BCZK0348(thiM)
            BCY: Bcer98_0363
            BTK: BT9727_0352(thiM)
            BTL: BALH_0374(thiM)
            BLI: BL03865(thiM)
            BLD: BLi04052(thiM)
            BCL: ABC2912(thiK)
            BAY: RBAM_035560(thiM)
            BPU: BPUM_3484(thiM)
            OIH: OB0473 OB0643
            GKA: GK1509(thiK)
            SAU: SA1895(thiM)
            SAV: SAV2092(thiM)
            SAM: MW2015(thiM)
            SAR: SAR2181(thiM)
            SAS: SAS1996
            SAC: SACOL2084(thiM)
            SAB: SAB1976c(thiM)
            SAA: SAUSA300_2048(thiM)
            SAO: SAOUHSC_02329
            SAJ: SaurJH9_2129
            SAH: SaurJH1_2167
            SEP: SE1691
            SER: SERP1699(thiM)
            SHA: SH0942(thiM)
            SSP: SSP0791
            LMO: lmo0316
            LMF: LMOf2365_0334(thiM)
            LIN: lin0341
            LWE: lwe0287(thiM)
            LLA: L94809(thiM)
            LLC: LACR_1377
            LLM: llmg_1216(thiM)
            SPN: SP_0717 SP_0724
            SPR: spr0629(thiM) spr0636(thiM)
            SPD: SPD_0623(thiM)
            SAG: SAG0841(thiM)
            SAN: gbs0859
            SAK: SAK_0964(thiM)
            LPL: lp_0113(thiM)
            LSA: LSA0059(thiM)
            LBR: LVIS_2099
            LCA: LSEI_0299
            LRE: Lreu_1013
            EFA: EF2777
            CAC: CAC3096(thiK)
            CPE: CPE1337(thiM)
            CPF: CPF_1544(thiM)
            CPR: CPR_1337(thiM)
            CTC: CTC01752
            CNO: NT01CX_0247(thiM)
            CDF: CD1600(thiK)
            CBO: CBO0450(thiK)
            CBA: CLB_0491(thiM-1) CLB_2193(thiM-2)
            CBH: CLC_0524(thiM-1) CLC_2176(thiM-2)
            CBF: CLI_0535(thiM-1) CLI_2303(thiM-2)
            CBE: Cbei_4488
            CKL: CKL_2918(thiM)
            AMT: Amet_1248
            CHY: CHY_0748(thiM)
            DSY: DSY1402
            DRM: Dred_0594
            SWO: Swol_0640
            TTE: TTE2232(thiM)
            MTA: Moth_2017
            CGL: NCgl1408(cgl1464)
            CGB: cg1655(thiM)
            CEF: CE1592
            PAC: PPA0885
            KRA: Krad_0852
            BLO: BL0115(thiM)
            BAD: BAD_1144(thiM)
            RXY: Rxyl_2790
            CCA: CCA00204(thiM)
            CAB: CAB199(thiM)
            CFE: CF0803(thiM)
            LIL: LA3365(thiM)
            LIC: LIC10800(thiM)
            LBJ: LBJ_0526
            LBL: LBL_2553
            RRS: RoseRS_1926
            RCA: Rcas_4122
            MMP: MMP1138(thiM)
            MMQ: MmarC5_0447
            MMZ: MmarC7_0389
            MVN: Mevan_0460
            MAC: MA2723(thiM)
            MBA: Mbar_A3319
            MMA: MM_3234
            MHU: Mhun_2217
            MEM: Memar_0262
            MBN: Mboo_2055
            MST: Msp_0682(thiM1) Msp_0694(thiM2)
            MSI: Msm_0916
            HWA: HQ2656A(thiM)
            NPH: NP4052A(thiM)
            PAB: PAB2432(thiM)
            PFU: PF1335
            RCI: RCIX2677(thiM)
STRUCTURES  PDB: 1C3Q  1EKK  1EKQ  1ESJ  1ESQ  1V8A  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.50
            ExPASy - ENZYME nomenclature database: 2.7.1.50
            ExplorEnz - The Enzyme Database: 2.7.1.50
            ERGO genome analysis and discovery system: 2.7.1.50
            BRENDA, the Enzyme Database: 2.7.1.50
            CAS: 9026-56-6
///
ENTRY       EC 2.7.1.51                 Enzyme
NAME        L-fuculokinase;
            L-fuculokinase (phosphorylating);
            L-fuculose kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:L-fuculose 1-phosphotransferase
REACTION    ATP + L-fuculose = ADP + L-fuculose 1-phosphate [RN:R03241]
ALL_REAC    R03241
SUBSTRATE   ATP [CPD:C00002];
            L-fuculose [CPD:C01721]
PRODUCT     ADP [CPD:C00008];
            L-fuculose 1-phosphate [CPD:C01099]
REFERENCE   1  [PMID:13905785]
  AUTHORS   HEATH EC, GHALAMBOR MA.
  TITLE     The metabolism of L-fucose. I. The purification and properties of
            L-fuculose kinase.
  JOURNAL   J. Biol. Chem. 237 (1962) 2423-6.
  ORGANISM  Escherichia coli [GN:eco], Escherichia freundii
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K00879  L-fuculokinase
GENES       ECO: b2803(fucK)
            ECJ: JW2774(fucK)
            ECE: Z4120(fucK)
            ECS: ECs3663
            ECI: UTI89_C3175(fucK)
            ECP: ECP_2786
            ECV: APECO1_3728(fucK)
            ECW: EcE24377A_3108(fucK)
            ECX: EcHS_A2947(fucK)
            STY: STY3117(fucK)
            STT: t2885(fucK)
            SPT: SPA2841(fucK)
            SEC: SC2917(fucK)
            STM: STM2977(fucK)
            SSN: SSON_2960(fucK)
            SDY: SDY_3021(fucK)
            SGL: SG0180
            HIT: NTHI0870(fucK)
            HSO: HS_1449(fucK)
            APL: APL_1685(fucK)
            VVY: VV2178
            SPN: SP_2167
            SPR: spr1973(fcsK)
            CPE: CPE0317(fucK)
            CPF: CPF_1049(fucK)
            BTH: BT_1275
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.51
            ExPASy - ENZYME nomenclature database: 2.7.1.51
            ExplorEnz - The Enzyme Database: 2.7.1.51
            ERGO genome analysis and discovery system: 2.7.1.51
            BRENDA, the Enzyme Database: 2.7.1.51
            CAS: 9026-64-6
///
ENTRY       EC 2.7.1.52                 Enzyme
NAME        fucokinase;
            fucokinase (phosphorylating);
            fucose kinase;
            L-fucose kinase;
            L-fucokinase;
            ATP:6-deoxy-L-galactose 1-phosphotransferase;
            ATP:L-fucose 1-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:beta-L-fucose 1-phosphotransferase
REACTION    ATP + L-fucose = ADP + beta-L-fucose 1-phosphate [RN:R03161]
ALL_REAC    R03161
SUBSTRATE   ATP [CPD:C00002];
            L-fucose [CPD:C01019]
PRODUCT     ADP [CPD:C00008];
            beta-L-fucose 1-phosphate [CPD:C02985]
COMMENT     Requires a divalent cation for activity, with Mg2+ and Fe2+ giving
            rise to the highest enzyme activity. Forms part of a salvage pathway
            for reutilization of L-fucose. Can also phosphorylate D-arabinose,
            but more slowly.
REFERENCE   1  [PMID:5646161]
  AUTHORS   Ishihara H, Massaro DJ, Heath EC.
  TITLE     The metabolism of L-fucose. 3. The enzymatic synthesis of
            beta-L-fucose 1-phosphate.
  JOURNAL   J. Biol. Chem. 243 (1968) 1103-9.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:2986701]
  AUTHORS   Butler W, Serif GS.
  TITLE     Fucokinase, its anomeric specificity and mechanism of phosphate
            group transfer.
  JOURNAL   Biochim. Biophys. Acta. 829 (1985) 238-43.
REFERENCE   3  [PMID:9488699]
  AUTHORS   Park SH, Pastuszak I, Drake R, Elbein AD.
  TITLE     Purification to apparent homogeneity and properties of pig kidney
            L-fucose kinase.
  JOURNAL   J. Biol. Chem. 273 (1998) 5685-91.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K05305  fucokinase
GENES       HSA: 197258(FUK)
            PTR: 468015(FUK)
            MMU: 234730(Fuk)
            CFA: 489715(FUK)
            DDI: DDBDRAFT_0190464
            TCR: 508379.10
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.52
            ExPASy - ENZYME nomenclature database: 2.7.1.52
            ExplorEnz - The Enzyme Database: 2.7.1.52
            ERGO genome analysis and discovery system: 2.7.1.52
            BRENDA, the Enzyme Database: 2.7.1.52
            CAS: 37278-00-5
///
ENTRY       EC 2.7.1.53                 Enzyme
NAME        L-xylulokinase;
            L-xylulokinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:L-xylulose 5-phosphotransferase
REACTION    ATP + L-xylulose = ADP + L-xylulose 5-phosphate [RN:R01901]
ALL_REAC    R01901;
            (other) R07127
SUBSTRATE   ATP [CPD:C00002];
            L-xylulose [CPD:C00312]
PRODUCT     ADP [CPD:C00008];
            L-xylulose 5-phosphate [CPD:C03291]
REFERENCE   1  [PMID:13861293]
  AUTHORS   ANDERSON RL, WOOD WA.
  TITLE     Purification and properties of L-xylulokinase.
  JOURNAL   J. Biol. Chem. 237 (1962) 1029-33.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K00880  L-xylulokinase
GENES       ECO: b3580(lyx)
            ECJ: JW3552(lyxK)
            ECC: c4403(lyxK)
            ECI: UTI89_C4124(lyxK)
            ECP: ECP_3685
            ECV: APECO1_2870(lyxK)
            ECW: EcE24377A_4077(lyx)
            ECX: EcHS_A3784(lyx)
            STY: STY4122(lyxK)
            STT: t3845(lyxK)
            SPT: SPA3525(lyxK)
            STM: STM3674(lyxK)
            YPE: YPO3334(sgbK)
            YPK: y0855(lyxK)
            YPM: YP_0353(sgbK)
            YPA: YPA_2810
            YPN: YPN_0759
            YPS: YPTB0797(sgbK)
            YPI: YpsIP31758_3270(lyxK)
            YEN: YE2603
            SFV: SFV_3959(lyxK)
            HSO: HS_0770(sgbK)
            PMU: PM1247(lyx)
            MSU: MS0048(xylB)
            APL: APL_1564(lyx)
            SME: SMb20497(lyx)
            ATU: Atu3874(lyxK)
            ATC: AGR_L_1942
            RET: RHE_PB00071(lyxX)
            RLE: pRL120198 pRL120763
            SIT: TM1040_1194
            GOX: GOX2214
            SAG: SAG1803
            SAN: gbs1844
            SAK: SAK_1823
            SSA: SSA_2082
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.53
            ExPASy - ENZYME nomenclature database: 2.7.1.53
            ExplorEnz - The Enzyme Database: 2.7.1.53
            ERGO genome analysis and discovery system: 2.7.1.53
            BRENDA, the Enzyme Database: 2.7.1.53
            CAS: 37278-01-6
///
ENTRY       EC 2.7.1.54                 Enzyme
NAME        D-arabinokinase;
            D-arabinokinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-arabinose 5-phosphotransferase
REACTION    ATP + D-arabinose = ADP + D-arabinose 5-phosphate [RN:R01573]
ALL_REAC    R01573
SUBSTRATE   ATP [CPD:C00002];
            D-arabinose [CPD:C00216]
PRODUCT     ADP [CPD:C00008];
            D-arabinose 5-phosphate [CPD:C01112]
REFERENCE   1
  AUTHORS   Volk, W.A.
  TITLE     Purification and properties of D-arabinokinase from
            Propionibacterium pentosaceum.
  JOURNAL   J. Biol. Chem. 237 (1962) 19-23.
  ORGANISM  Propionibacterium pentosaceum
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.54
            ExPASy - ENZYME nomenclature database: 2.7.1.54
            ExplorEnz - The Enzyme Database: 2.7.1.54
            ERGO genome analysis and discovery system: 2.7.1.54
            BRENDA, the Enzyme Database: 2.7.1.54
            CAS: 37278-02-7
///
ENTRY       EC 2.7.1.55                 Enzyme
NAME        allose kinase;
            allokinase (phosphorylating);
            allokinase;
            D-allokinase;
            D-allose-6-kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-allose 6-phosphotransferase
REACTION    ATP + D-allose = ADP + D-allose 6-phosphate [RN:R03576]
ALL_REAC    R03576
SUBSTRATE   ATP [CPD:C00002];
            D-allose [CPD:C01487]
PRODUCT     ADP [CPD:C00008];
            D-allose 6-phosphate [CPD:C02962]
REFERENCE   1
  AUTHORS   Gibbins, L.N. and Simpson, F.J.
  TITLE     The purification and properties of D-allose-6-kinase from Aerobacter
            aerogenes.
  JOURNAL   Can. J. Microbiol. 9 (1963) 769-779.
  ORGANISM  Aerobacter aerogenes
ORTHOLOGY   KO: K00881  allose kinase
GENES       ECO: b4084(alsK)
            ECJ: JW5724(alsK)
            ECC: c5090(yjcT)
            ECI: UTI89_C4680(yjcT)
            ECP: ECP_4326
            ECV: APECO1_2366(yjcT)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.55
            ExPASy - ENZYME nomenclature database: 2.7.1.55
            ExplorEnz - The Enzyme Database: 2.7.1.55
            ERGO genome analysis and discovery system: 2.7.1.55
            BRENDA, the Enzyme Database: 2.7.1.55
            CAS: 9031-78-1
///
ENTRY       EC 2.7.1.56                 Enzyme
NAME        1-phosphofructokinase;
            fructose-1-phosphate kinase;
            1-phosphofructokinase (phosphorylating);
            D-fructose-1-phosphate kinase;
            fructose 1-phosphate kinase;
            phosphofructokinase 1
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-fructose-phosphate 6-phosphotransferase
REACTION    ATP + D-fructose 1-phosphate = ADP + D-fructose 1,6-bisphosphate
ALL_REAC    (other) R02071 R03236
SUBSTRATE   ATP [CPD:C00002];
            D-fructose 1-phosphate [CPD:C01094]
PRODUCT     ADP [CPD:C00008];
            D-fructose 1,6-bisphosphate [CPD:C00354]
COMMENT     ITP, GTP or UTP can replace ATP.
REFERENCE   1  [PMID:4222878]
  AUTHORS   Reeves RE, Warren LG, Hsu DS.
  TITLE     1-Phosphofructokinase from an anaerobe.
  JOURNAL   J. Biol. Chem. 241 (1966) 1257-61.
  ORGANISM  Bacteroides symbiosus
REFERENCE   2  [PMID:4242639]
  AUTHORS   Sapico V, Anderson RL.
  TITLE     D-fructose 1-phosphate kinase and D-fructose 6-phosphate kinase from
            Aerobacter aerogenes. A comparative study of regulatory properties.
  JOURNAL   J. Biol. Chem. 244 (1969) 6280-8.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K00882  1-phosphofructokinase
GENES       ECO: b2168(fruK)
            ECJ: JW2155(fruK)
            ECE: Z3426(fruK)
            ECS: ECs3060
            ECC: c2703(fruK)
            ECI: UTI89_C2443(fruK)
            ECP: ECP_2208
            ECV: APECO1_4386(fruK)
            ECW: EcE24377A_2465(fruK)
            ECX: EcHS_A2305(fruK)
            STY: STY2441(fruK) STY3436
            STT: t0649(fruK) t3174
            SPT: SPA0646(fruK) SPA3123
            SEC: SC2221(fruK)
            STM: STM2205(fruK) STM3254
            YPE: YPO1299(fruK)
            YPK: y2886(fruK)
            YPM: YP_1293(fruK)
            YPA: YPA_1016
            YPN: YPN_2680
            YPS: YPTB1330(fruK)
            YPI: YpsIP31758_2682(fruK)
            SFL: SF2253(fruK)
            SFX: S2382(fruK)
            SFV: SFV_2243(fruK)
            SSN: SSON_2224(fruK)
            SBO: SBO_2156(fruK)
            SDY: SDY_2316(fruK)
            ECA: ECA2728(fruK)
            PLU: plu2858(fruK)
            SGL: SG0954
            SPE: Spro_3229
            HIN: HI0447(fruK)
            HIT: NTHI0574(fruK)
            HIP: CGSHiEE_00760(fruK)
            HIQ: CGSHiGG_05460(fruK)
            PMU: PM1796(fruK)
            MSU: MS2179(fruK)
            APL: APL_0344(fruK)
            ASU: Asuc_0086
            XCC: XCC2371(fruK)
            XCB: XC_1743
            XCV: XCV2680(fruK)
            XAC: XAC2502(fruK)
            XOO: XOO2811(fruK)
            XOM: XOO_2651(XOO2651)
            VCH: VCA0517
            VCO: VC0395_0450(fruK)
            VVU: VV2_0199
            VVY: VVA0705
            VPA: VPA0812
            VFI: VFA0941
            PPR: PBPRA1574
            PAE: PA3561(fruK)
            PAU: PA14_18260(fruK)
            PAP: PSPA7_1584(pfkB)
            PPU: PP_0794(fruK)
            PPF: Pput_0817
            PST: PSPTO_0955(fruK)
            PSB: Psyr_0822
            PSP: PSPPH_0848(fruK)
            PFL: PFL_0860(fruK)
            PFO: Pfl_0794(pfkB)
            PEN: PSEEN0933
            PMY: Pmen_0787
            ACI: ACIAD1992(fruK)
            ACB: A1S_1946
            PIN: Ping_3552
            CSA: Csal_2647
            AHA: AHA_2347
            CVI: CV_3053(fruK)
            RSO: RSc2862(fruK)
            BTE: BTH_II0907(pfkB)
            RSP: RSP_1787(fruK)
            RSH: Rsph17029_0434
            RSQ: Rsph17025_0611
            GBE: GbCGDNIH1_0411
            ACR: Acry_0188
            RRU: Rru_A1971
            ABA: Acid345_0661
            SUS: Acid_0818
            BSU: BG12588(fruB)
            BHA: BH0827(fruB)
            BAN: BA3847(fruB)
            BAR: GBAA3847(fruB)
            BAA: BA_4320(pfkB)
            BAT: BAS3564
            BCE: BC3719
            BCA: BCE_3745(fruB)
            BCZ: BCZK3477(fruB)
            BCY: Bcer98_2395
            BTK: BT9727_3463(fruB)
            BLI: BL01605(fruK) BL01904
            BLD: BLi01653(fruK) BLi03549
            BCL: ABC1270(fruB) ABC3198
            BAY: RBAM_014130(fruK)
            BPU: BPUM_1335(fruK) BPUM_1770
            OIH: OB0839(fruB)
            GKA: GK1839
            SAU: SA0654(fruB)
            SAV: SAV0699(fruB)
            SAM: MW0661(fruB)
            SAR: SAR0752
            SAS: SAS0664
            SAC: SACOL0758(fruK)
            SAB: SAB0648
            SAA: SAUSA300_0684(fruB)
            SAO: SAOUHSC_00707
            SAJ: SaurJH9_0723
            SAH: SaurJH1_0739
            SEP: SE0471
            SER: SERP0358(fruK)
            SHA: SH2195(fruB)
            SSP: SSP2018
            LMO: lmo2095 lmo2336(fruB)
            LMF: LMOf2365_2127 LMOf2365_2306(fruB)
            LIN: lin2199 lin2430(fruB)
            LWE: lwe0799 lwe2116 lwe2288(fruB)
            LLA: L0032(lacC)
            LLC: LACR_1032
            LLM: llmg_1569(fruC)
            SPY: SPy_0854(fruB)
            SPZ: M5005_Spy_0661(fruB)
            SPM: spyM18_0913(fruK)
            SPG: SpyM3_0579(fruK)
            SPS: SPs1275
            SPH: MGAS10270_Spy0720(fruB)
            SPI: MGAS10750_Spy0752(fruB)
            SPJ: MGAS2096_Spy0731(fruB) MGAS2096_Spy0732
            SPK: MGAS9429_Spy0716(fruB)
            SPF: SpyM51147(fruB)
            SPA: M6_Spy0680
            SPB: M28_Spy0642(fruB)
            SPN: SP_0876
            SPR: spr0779(fruB)
            SPD: SPD_0772
            SAG: SAG1347(fruK)
            SAN: gbs1417
            SAK: SAK_1378
            SMU: SMU.113 SMU.871(pfkB)
            STC: str0400(fruB)
            STL: stu0400(fruB)
            SSA: SSA_1081(fruB)
            SGO: SGO_1112(fruB)
            LPL: lp_2096(fruK)
            LJO: LJ0145 LJ0158 LJ0571
            LAC: LBA1778(fruK)
            LSA: LSA1049(fruK)
            LSL: LSL_0164(fruK)
            LDB: Ldb2041(fruK)
            LBU: LBUL_1888
            LCA: LSEI_1348 LSEI_2655
            LGA: LGAS_0148 LGAS_0161
            PPE: PEPE_0141
            EFA: EF0693(fruK-1) EF0718(fruK-2)
            STH: STH794
            CAC: CAC0232(fruB)
            CPE: CPE0585(fruB)
            CPF: CPF_0565(fruK)
            CPR: CPR_0551
            CNO: NT01CX_1725
            CDF: CD2270(fruK)
            CBO: CBO1763(fpk)
            CBA: CLB_1698(fruK)
            CBH: CLC_1706(fruK)
            CBF: CLI_1758(fruK)
            CBE: Cbei_1843
            AMT: Amet_0826 Amet_4268
            TTE: TTE2587(fruK)
            MTA: Moth_0012
            MGE: MG_063(fruK)
            MPN: MPN079(fruK)
            MPE: MYPE7750(fruK)
            MMY: MSC_0647(fruK) MSC_0832(fruB)
            MCP: MCAP_0619 MCAP_0852
            MFL: Mfl180
            MSM: MSMEG_0086 MSMEG_1378
            MMC: Mmcs_0081
            CGL: NCgl1857(cgl1932) NCgl1860(cgl1935)
            CGB: cg2119(pfkB)
            CEF: CE1828
            CDI: DIP1430
            NFA: nfa28550(fruK)
            RHA: RHA1_ro00056 RHA1_ro06783
            SCO: SCO3197(SCE22.14c)
            SMA: SAV3689(fruB)
            CMI: CMM_1503(fruK)
            AAU: AAur_0295(fruK) AAur_0349(fruK) AAur_0862(fruK)
            TFU: Tfu_0696
            SEN: SACE_2273(fruB)
            RXY: Rxyl_2297
            FNU: FN1440
            BGA: BG0651(fruK)
            DET: DET1346
            DEH: cbdb_A1296
            DEB: DehaBAV1_1157
            RRS: RoseRS_0693
            RCA: Rcas_0209
            DRA: DR_B0074
            DGE: Dgeo_2174
            MTP: Mthe_0686
STRUCTURES  PDB: 2JG5  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.56
            ExPASy - ENZYME nomenclature database: 2.7.1.56
            ExplorEnz - The Enzyme Database: 2.7.1.56
            ERGO genome analysis and discovery system: 2.7.1.56
            BRENDA, the Enzyme Database: 2.7.1.56
            CAS: 37278-03-8
///
ENTRY       EC 2.7.1.57       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Deleted entry: mannitol kinase (EC 2.7.1.57 created 1972, deleted
            1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.57
            ExPASy - ENZYME nomenclature database: 2.7.1.57
            ExplorEnz - The Enzyme Database: 2.7.1.57
            ERGO genome analysis and discovery system: 2.7.1.57
            BRENDA, the Enzyme Database: 2.7.1.57
///
ENTRY       EC 2.7.1.58                 Enzyme
NAME        2-dehydro-3-deoxygalactonokinase;
            2-keto-3-deoxygalactonokinase;
            2-keto-3-deoxygalactonate kinase (phosphorylating);
            2-oxo-3-deoxygalactonate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:2-dehydro-3-deoxy-D-galactonate 6-phosphotransferase
REACTION    ATP + 2-dehydro-3-deoxy-D-galactonate = ADP +
            2-dehydro-3-deoxy-D-galactonate 6-phosphate [RN:R03387]
ALL_REAC    R03387
SUBSTRATE   ATP [CPD:C00002];
            2-dehydro-3-deoxy-D-galactonate [CPD:C01216]
PRODUCT     ADP [CPD:C00008];
            2-dehydro-3-deoxy-D-galactonate 6-phosphate [CPD:C01286]
REFERENCE   1
  AUTHORS   Stouthamer, A.H.
  TITLE     Glucose and galactose metabolism in Gluconobacter liquefaciens.
  JOURNAL   Biochim. Biophys. Acta 48 (1961) 484-500.
  ORGANISM  Gluconobacter liquefaciens
PATHWAY     PATH: map00052  Galactose metabolism
ORTHOLOGY   KO: K00883  2-dehydro-3-deoxygalactonokinase
GENES       ECO: b3693(dgoK)
            ECJ: JW3670(dgoK)
            ECC: c4615(dgoK) c4778
            ECI: UTI89_C4245(dgoK)
            ECP: ECP_3895 ECP_4045
            ECV: APECO1_2625 APECO1_2763(dgoK)
            ECW: EcE24377A_4203(dgoK)
            ECX: EcHS_A3906
            SEC: SC3747(dgoK)
            STM: STM3829(dgoK)
            SFL: SF3770(dgoK)
            SFX: S4000(dgoK)
            SFV: SFV_3818(dgoK)
            SSN: SSON_3644(dgoK)
            ECA: ECA4418(dgoK)
            ENT: Ent638_0007
            SPE: Spro_0042
            XCC: XCC1744(dgoK)
            XCB: XC_2490
            XCV: XCV1794
            XAC: XAC1763(dgoK)
            XOO: XOO2920(dgoK)
            XOM: XOO_2771(XOO2771)
            VVY: VVA1574
            PST: PSPTO_2177(dgoK)
            PSB: Psyr_1987
            PSP: PSPPH_1956(dgoK)
            PFO: Pfl_4125
            PAT: Patl_0898
            CSA: Csal_2605
            MMW: Mmwyl1_2012
            RSO: RSc2759(dgoK)
            BMA: BMA2489(dgoK)
            BMV: BMASAVP1_A0409(dgoK)
            BML: BMA10299_A1269(dgoK)
            BMN: BMA10247_3296(dgoK)
            BXE: Bxe_A0543
            BUR: Bcep18194_A3700 Bcep18194_C6942
            BCN: Bcen_0135
            BCH: Bcen2424_0618
            BAM: Bamb_0519
            BPS: BPSL2971
            BPM: BURPS1710b_3488(dgoK)
            BPL: BURPS1106A_3489(dgoK)
            BPD: BURPS668_3451(dgoK)
            BTE: BTH_I1176
            RFR: Rfer_0937 Rfer_0949 Rfer_0962
            POL: Bpro_3534
            MLO: mlr4742
            MES: Meso_0845
            SME: SMc00881(dgoK1)
            ATU: Atu0704(dgoK)
            ATC: AGR_C_1271
            RET: RHE_CH00854(dgoK)
            RLE: RL0916(dgoK)
            BME: BMEII0357
            BMF: BAB2_0295
            BMS: BRA0939(dgoK)
            BMB: BruAb2_0294(dgoK)
            BOV: BOV_A0881(dgoK)
            BJA: bll7288(dgoK)
            BRA: BRADO1753(dgoK)
            BBT: BBta_2068(dgoK)
            CCR: CC_0785
            SIL: SPO0785
            SIT: TM1040_3489
            RSP: RSP_1371
            JAN: Jann_3833
            RDE: RD1_2867(dgoK)
            HNE: HNE_2003
            SAL: Sala_0743
            MSM: MSMEG_6175
            SEN: SACE_2638(dgoK)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.58
            ExPASy - ENZYME nomenclature database: 2.7.1.58
            ExplorEnz - The Enzyme Database: 2.7.1.58
            ERGO genome analysis and discovery system: 2.7.1.58
            BRENDA, the Enzyme Database: 2.7.1.58
            CAS: 37278-05-0
///
ENTRY       EC 2.7.1.59                 Enzyme
NAME        N-acetylglucosamine kinase;
            acetylglucosamine kinase (phosphorylating);
            ATP:2-acetylamino-2-deoxy-D-glucose 6-phosphotransferase;
            2-acetylamino-2-deoxy-D-glucose kinase;
            acetylaminodeoxyglucokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:N-acetyl-D-glucosamine 6-phosphotransferase
REACTION    ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine
            6-phosphate [RN:R01201]
ALL_REAC    R01201
SUBSTRATE   ATP [CPD:C00002];
            N-acetyl-D-glucosamine [CPD:C00140]
PRODUCT     ADP [CPD:C00008];
            N-acetyl-D-glucosamine 6-phosphate [CPD:C00357]
COMMENT     The bacterial enzyme also acts on D-glucose.
REFERENCE   1
  AUTHORS   Asensio, C. and Ruiz-Amil, M.
  TITLE     N-Acetyl-D-glucosamine kinase. II. Escherichia coli.
  JOURNAL   Methods Enzymol. 9 (1966) 421-425.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Barkulis, S.S.
  TITLE     N-Acetyl-D-glucosamine kinase. I. Streptococcus pyrogenes.
  JOURNAL   Methods Enzymol. 9 (1966) 415-420.
  ORGANISM  Streptococcus pyrogenes
REFERENCE   3  [PMID:4319609]
  AUTHORS   Datta A.
  TITLE     Studies on hog spleen N-acetylglucosamine kinase. I. Purification
            and properties of N-acetylglucosamine kinase.
  JOURNAL   Biochim. Biophys. Acta. 220 (1970) 51-60.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K00884  N-acetylglucosamine kinase
GENES       HSA: 55577(NAGK)
            RNO: 297393(Nagk)
            CFA: 492060(NAGK)
            DME: Dmel_CG6218
            ECO: b1119(nagK)
            ECJ: JW1105(ycfX)
            ECE: Z1760(ycfX)
            ECS: ECs1497
            ECC: c1394(ycfX)
            ECI: UTI89_C1247(ycfX)
            ECP: ECP_1113
            ECV: APECO1_200(ycfX)
            ECW: EcE24377A_1241(nagK)
            ECX: EcHS_A1241
            STY: STY1260
            STT: t1700
            SPT: SPA1630(ycfX)
            SEC: SC1170(ycfX)
            STM: STM1220(ycfX)
            YPE: YPO1629
            YPK: y1788
            YPM: YP_1758(nagC4)
            YPA: YPA_1896
            YPN: YPN_2003
            YPP: YPDSF_1820
            YPS: YPTB2439
            YPI: YpsIP31758_1603(nagK)
            YEN: YE1713
            SFL: SF1123(ycfX)
            SFX: S1203(ycfX)
            SFV: SFV_1139(ycfX)
            SSN: SSON_1139(ycfX)
            SBO: SBO_1942(ycfX)
            SDY: SDY_2031(ycfX)
            ECA: ECA1826
            KPN: KPN_01116(ycfX)
            HIN: HI0182
            HIT: NTHI0273
            HSO: HS_1041
            PMU: PM0675
            MSU: MS1527(nagC)
            VCH: VC1532
            VVU: VV1_2570
            VVY: VV1719
            VPA: VP1494
            VFI: VF1408
            PPR: PBPRA1747
            CVI: CV_2896
            BXE: Bxe_A0107
            RET: RHE_CH02899
            RLE: RL3360 RL4221 pRL120254
            BME: BMEII0181 BMEII0756
            BMF: BAB2_0724
            RDE: RD1_1728
            GOX: GOX1475
            CDF: CD1585
            AVA: Ava_2007
            PTO: PTO0011 PTO1094
STRUCTURES  PDB: 2CH5  2CH6  2HOE  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.59
            ExPASy - ENZYME nomenclature database: 2.7.1.59
            ExplorEnz - The Enzyme Database: 2.7.1.59
            ERGO genome analysis and discovery system: 2.7.1.59
            BRENDA, the Enzyme Database: 2.7.1.59
            CAS: 9027-48-9
///
ENTRY       EC 2.7.1.60                 Enzyme
NAME        N-acylmannosamine kinase;
            acylmannosamine kinase (phosphorylating);
            acetylamidodeoxymannokinase;
            acetylmannosamine kinase;
            acylaminodeoxymannokinase;
            acylmannosamine kinase;
            N-acyl-D-mannosamine kinase;
            N-acetylmannosamine kinase;
            ATP:N-acetylmannosamine 6-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:N-acyl-D-mannosamine 6-phosphotransferase
REACTION    ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-mannosamine 6-phosphate
            [RN:R02650]
ALL_REAC    R02650 > R02705
SUBSTRATE   ATP [CPD:C00002];
            N-acyl-D-mannosamine [CPD:C00625]
PRODUCT     ADP [CPD:C00008];
            N-acyl-D-mannosamine 6-phosphate [CPD:C00686]
COMMENT     Acts on the acetyl and glycolyl derivatives.
REFERENCE   1  [PMID:4889177]
  AUTHORS   Banerjee S, Ghosh S.
  TITLE     Purification and properties of N-acetylmannosamine kinase from
            Salmonella typhimurium.
  JOURNAL   Eur. J. Biochem. 8 (1969) 200-6.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:13704957]
  AUTHORS   GHOSH S, ROSEMAN S.
  TITLE     Enzymatic phosphorylation of N-acetyl-D-mannosamine.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 47 (1961) 955-8.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:5928201]
  AUTHORS   Kundig W, Ghosh S, Roseman S.
  TITLE     The sialic acids. VII. N-acyl-D-mannosamine kinase from rat liver.
  JOURNAL   J. Biol. Chem. 241 (1966) 5619-26.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K00885  N-acylmannosamine kinase
GENES       HSA: 10020(GNE)
            RNO: 114711(Gne)
            CFA: 481607(GNE)
            SPU: 590539(LOC590539)
            ECO: b3222(nanK)
            ECE: Z4580(yhcI)
            ECS: ECs4095
            ECC: c3976(yhcI)
            ECI: UTI89_C3652
            ECV: APECO1_3221(nanK)
            STY: STY3516
            STT: t3253
            SPT: SPA3204(nanK)
            SEC: SC3274(nanK)
            STM: STM3336(nanK)
            YPE: YPO3020
            YPK: y1461
            YPM: YP_2644(nagC7)
            YPA: YPA_2208
            YPN: YPN_1364
            YPS: YPTB2739
            SFL: SF3258(nanK)
            SFX: S3475(yhcI)
            SFV: SFV_3247(yhcI)
            SSN: SSON_3363(yhcI)
            SBO: SBO_3167(yhcI)
            SDY: SDY_3397(yhcI)
            HIN: HI0144
            HIT: NTHI0230(nanK)
            HIP: CGSHiEE_02570
            HSO: HS_0698(nanK)
            PMU: PM1712
            APL: APL_1753(nanK)
            VCH: VC1782
            VVU: VV2_0735
            VVY: VVA1205
            VFI: VF0667
            PPR: PBPRA2284
            PHA: PSHAb0149(nagK)
            BUR: Bcep18194_A4684
            RET: RHE_CH00464(frcR)
            RLE: RL0488
            BME: BMEII0857
            BMF: BAB2_0810
            BMS: BRA0411
            BMB: BruAb2_0790
            RDE: RD1_2214(frcR)
            RRU: Rru_A2630
            SPZ: M5005_Spy_0218
            SPH: MGAS10270_Spy0218
            SPI: MGAS10750_Spy0213
            SPJ: MGAS2096_Spy0236
            SPK: MGAS9429_Spy0219
            SPA: M6_Spy0250
            SPB: M28_Spy0212
            SSA: SSA_0079(glk)
            MSY: MS53_0195(nagC)
            FNU: FN1474
            DGE: Dgeo_1173
STRUCTURES  PDB: 2AA4  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.60
            ExPASy - ENZYME nomenclature database: 2.7.1.60
            ExplorEnz - The Enzyme Database: 2.7.1.60
            ERGO genome analysis and discovery system: 2.7.1.60
            BRENDA, the Enzyme Database: 2.7.1.60
            CAS: 9027-53-6
///
ENTRY       EC 2.7.1.61                 Enzyme
NAME        acyl-phosphate---hexose phosphotransferase;
            hexose phosphate:hexose phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     acyl-phosphate:D-hexose phosphotransferase
REACTION    acyl phosphate + D-hexose = an acid + D-hexose phosphate [RN:R03841]
ALL_REAC    R03841
SUBSTRATE   acyl phosphate [CPD:C02133];
            D-hexose [CPD:C00738]
PRODUCT     acid [CPD:C00174];
            D-hexose phosphate [CPD:C02672]
COMMENT     Phosphorylates D-glucose and D-mannose on O-6, and D-fructose on O-1
            or O-6.
REFERENCE   1
  AUTHORS   Anderson, R.L. and Kamel, M.Y.
  TITLE     Acyl phosphate:hexose phosphotransferase (hexose phosphate:hexose
            phosphotransferase).
  JOURNAL   Methods Enzymol. 9 (1966) 392-396.
  ORGANISM  Aerobacter aerogenes
REFERENCE   2  [PMID:6033450]
  AUTHORS   Kamel MY, Anderson RL.
  TITLE     Acyl phosphate: hexose phosphotransferase. Purification and
            properties of the enzyme from Aerobacter aerogenes and evidence for
            its common identity with hexose phosphate: hexose
            phosphotransferase.
  JOURNAL   Arch. Biochem. Biophys. 120 (1967) 322-31.
  ORGANISM  Aerobacter aerogenes
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.61
            ExPASy - ENZYME nomenclature database: 2.7.1.61
            ExplorEnz - The Enzyme Database: 2.7.1.61
            ERGO genome analysis and discovery system: 2.7.1.61
            BRENDA, the Enzyme Database: 2.7.1.61
            CAS: 37278-06-1
///
ENTRY       EC 2.7.1.62                 Enzyme
NAME        phosphoramidate---hexose phosphotransferase;
            phosphoramidate-hexose transphosphorylase;
            phosphoramidic-hexose transphosphorylase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     phosphoramidate:hexose 1-phosphotransferase
REACTION    phosphoramidate + hexose = NH3 + alpha-D-hexose 1-phosphate
            [RN:R03148]
ALL_REAC    R03148
SUBSTRATE   phosphoramidate [CPD:C02306];
            hexose [CPD:C01381]
PRODUCT     NH3 [CPD:C00014];
            alpha-D-hexose 1-phosphate [CPD:C01171]
COMMENT     Activity is observed with several hexoses; of these glucose is the
            best substrate and the product from it is alpha-D-glucose
            1-phosphate. The phosphoramidate donor can be replaced by
            N-phosphoglycine and by an N-phosphohistidine. May be identical with
            EC 3.1.3.9 glucose-6-phosphatase.
REFERENCE   1
  AUTHORS   Smith, R.A. and Thiesen, M.C.
  TITLE     Phosphoramidate-hexose transphosphorylase.
  JOURNAL   Methods Enzymol. 9 (1966) 403-407.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.62
            ExPASy - ENZYME nomenclature database: 2.7.1.62
            ExplorEnz - The Enzyme Database: 2.7.1.62
            ERGO genome analysis and discovery system: 2.7.1.62
            BRENDA, the Enzyme Database: 2.7.1.62
            CAS: 9031-45-2
///
ENTRY       EC 2.7.1.63                 Enzyme
NAME        polyphosphate---glucose phosphotransferase;
            polyphosphate glucokinase;
            polyphosphate-D-(+)-glucose-6-phosphotransferase;
            polyphosphate-glucose 6-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     polyphosphate:D-glucose 6-phosphotransferase
REACTION    (phosphate)n + D-glucose = (phosphate)n-1 + D-glucose 6-phosphate
            [RN:R02185]
ALL_REAC    R02185 > R02187 R02189
SUBSTRATE   (phosphate)n [CPD:C00404];
            D-glucose [CPD:C00031]
PRODUCT     (phosphate)n-1 [CPD:C00404];
            D-glucose 6-phosphate [CPD:C00092]
COFACTOR    Neutral salt [CPD:C01939]
COMMENT     Requires a neutral salt, e.g. KCl, for maximum activity. Also acts
            on glucosamine.
REFERENCE   1
  AUTHORS   Szymona, M.
  TITLE     Purification and properties of a new hexokinase utilizing inorganic
            pyrophosphate.
  JOURNAL   Acta Biochim. Pol. 9 (1962) 165-181.
REFERENCE   2
  AUTHORS   Szymona, M. and Ostrowski, W.
  TITLE     Inorganic polyphosphate glucokinase of Mycobacterium phlei.
  JOURNAL   Biochim. Biophys. Acta 85 (1964) 283-295.
  ORGANISM  Mycobacterium phlei
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
ORTHOLOGY   KO: K00886  polyphosphate glucokinase
GENES       AHA: AHA_0917
            BXE: Bxe_B0216
            MLO: mlr4209
            ATU: Atu4836
            ATC: AGR_L_95
            NWI: Nwi_1575
            NHA: Nham_2098
            GBE: GbCGDNIH1_0537
            MTU: Rv2702(ppgK)
            MTC: MT2776(ppgK)
            MBO: Mb2721(ppgK)
            MBB: BCG_2715(ppgK)
            MLE: ML1023(ppgK)
            MPA: MAP2819(ppgK)
            MAV: MAV_3594
            MSM: MSMEG_2760
            MVA: Mvan_2462
            MGI: Mflv_3938
            MMC: Mmcs_2186
            MKM: Mkms_2232
            MJL: Mjls_2175
            CGL: NCgl1835(cgl1911)
            CGB: cg2091(ppgK)
            CEF: CE1803
            CDI: DIP1404(ppgK)
            CJK: jk1086(ppgK)
            NFA: nfa37580
            RHA: RHA1_ro06824
            SCO: SCO5059(ppgK)
            SMA: SAV3209(ppgK)
            LXX: Lxx09960(glk)
            CMI: CMM_2953(ppgK2)
            AAU: AAur_1727(ppgK)
            PAC: PPA2125
            TFU: Tfu_1811
            FRA: Francci3_3492
            FAL: FRAAL5682(ppgK)
            SEN: SACE_1802(ppgK)
            BLO: BL0047(ppgK)
            BAD: BAD_0957(ppgK)
            ANA: all1371
            AVA: Ava_4014
            GFO: GFO_2545(ppgK)
            DRA: DR_0823
            DGE: Dgeo_0575
STRUCTURES  PDB: 1WOQ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.63
            ExPASy - ENZYME nomenclature database: 2.7.1.63
            ExplorEnz - The Enzyme Database: 2.7.1.63
            ERGO genome analysis and discovery system: 2.7.1.63
            BRENDA, the Enzyme Database: 2.7.1.63
            CAS: 9033-50-5
///
ENTRY       EC 2.7.1.64                 Enzyme
NAME        inositol 3-kinase;
            inositol-1-kinase (phosphorylating);
            myoinositol kinase;
            myo-inositol 1-kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:myo-inositol 1-phosphotransferase
REACTION    ATP + myo-inositol = ADP + 1D-myo-inositol 3-phosphate [RN:R07279]
ALL_REAC    R07279;
            (other) R01182
SUBSTRATE   ATP [CPD:C00002];
            myo-inositol [CPD:C00137]
PRODUCT     ADP [CPD:C00008];
            1D-myo-inositol 3-phosphate [CPD:C04006]
REFERENCE   1
  AUTHORS   English, P.D., Dietz, M. and Albersheim, P.
  TITLE     Myoinositol kinase: partial purification and identification of
            product.
  JOURNAL   Science 151 (1966) 198-199.
REFERENCE   2
  AUTHORS   Loewus, M.W., Sasaki, K., Leavitt, A.C., Muscell, L., Sherman, W.R.
            and Loewus, F.A.
  TITLE     Enantiomeric form of myo-inositol-1-phosphate produced by
            myo-inositol-1-phosphate synthase and myoinositol kinase in
            higher-plants.
  JOURNAL   Plant Physiol. 70 (1982) 1661-1663.
  ORGANISM  Triticum aestivum [GN:etae]
REFERENCE   3  [PMID:2176081]
  AUTHORS   Stephens LR, Kay RR, Irvine RF.
  TITLE     A myo-inositol D-3 hydroxykinase activity in Dictyostelium.
  JOURNAL   Biochem. J. 272 (1990) 201-10.
  ORGANISM  Phaseolus aureus
PATHWAY     PATH: map00562  Inositol phosphate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.64
            ExPASy - ENZYME nomenclature database: 2.7.1.64
            ExplorEnz - The Enzyme Database: 2.7.1.64
            ERGO genome analysis and discovery system: 2.7.1.64
            BRENDA, the Enzyme Database: 2.7.1.64
            CAS: 37278-07-2
///
ENTRY       EC 2.7.1.65                 Enzyme
NAME        scyllo-inosamine 4-kinase;
            scyllo-inosamine kinase (phosphorylating);
            scyllo-inosamine kinase;
            ATP:inosamine phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:1-amino-1-deoxy-scyllo-inositol 4-phosphotransferase
REACTION    ATP + 1-amino-1-deoxy-scyllo-inositol = ADP +
            1-amino-1-deoxy-scyllo-inositol 4-phosphate [RN:R03384]
ALL_REAC    R03384
SUBSTRATE   ATP [CPD:C00002];
            1-amino-1-deoxy-scyllo-inositol [CPD:C01214]
PRODUCT     ADP [CPD:C00008];
            1-amino-1-deoxy-scyllo-inositol 4-phosphate [CPD:C01283]
COMMENT     Also acts on streptamine, 2-deoxystreptamine and
            1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol.
REFERENCE   1  [PMID:4376579]
  AUTHORS   Walker JB.
  TITLE     Enzymatic reactions involved in streptomycin biosynthesis and
            metabolism.
  JOURNAL   Lloydia. 34 (1971) 363-71.
  ORGANISM  Streptomyces bikiniensis, Streptomyces griseus
REFERENCE   2  [PMID:6076630]
  AUTHORS   Walker JB, Walker MS.
  TITLE     Enzymatic synthesis of streptidine from scyllo-inosamine.
  JOURNAL   Biochemistry. 6 (1967) 3821-9.
  ORGANISM  Streptomyces bikiniensis, Streptomyces griseus
PATHWAY     PATH: map00521  Streptomycin biosynthesis
ORTHOLOGY   KO: K04339  scyllo-inosamine 4-kinase
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.65
            ExPASy - ENZYME nomenclature database: 2.7.1.65
            ExplorEnz - The Enzyme Database: 2.7.1.65
            ERGO genome analysis and discovery system: 2.7.1.65
            BRENDA, the Enzyme Database: 2.7.1.65
            CAS: 37278-08-3
///
ENTRY       EC 2.7.1.66                 Enzyme
NAME        undecaprenol kinase;
            isoprenoid alcohol kinase;
            isoprenoid alcohol phosphokinase;
            C55-isoprenoid alcohol phosphokinase;
            isoprenoid alcohol kinase (phosphorylating);
            C55-isoprenoid alcohol kinase;
            C55-isoprenyl alcohol phosphokinase;
            polyisoprenol kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:undecaprenol phosphotransferase
REACTION    ATP + undecaprenol = ADP + undecaprenyl phosphate [RN:R05626]
ALL_REAC    R05626
SUBSTRATE   ATP [CPD:C00002];
            undecaprenol [CPD:C01968]
PRODUCT     ADP [CPD:C00008];
            undecaprenyl phosphate [CPD:C00348]
REFERENCE   1  [PMID:4248528]
  AUTHORS   Higashi Y, Siewert G, Strominger JL.
  TITLE     Biosynthesis of the peptidoglycan of bacterial cell walls. XIX.
            Isoprenoid alcohol phosphokinase.
  JOURNAL   J. Biol. Chem. 245 (1970) 3683-90.
  ORGANISM  Staphylococcus aureus
PATHWAY     PATH: map00550  Peptidoglycan biosynthesis
ORTHOLOGY   KO: K00887  undecaprenol kinase
GENES       ECW: EcE24377A_3520(uppP)
            YPP: YPDSF_0433
            ENT: Ent638_3460
            PAP: PSPA7_3337
            PFO: Pfl_3826
            SBL: Sbal_1152
            SPC: Sputcn32_1112
            SHN: Shewana3_1087
            DNO: DNO_0291
            BXE: Bxe_A1299
            BVI: Bcep1808_0848 Bcep1808_1283
            BUR: Bcep18194_A4021(uppP)
            BCN: Bcen_0438
            BCH: Bcen2424_0917
            BAM: Bamb_0794
            BTE: BTH_I1512
            PNU: Pnuc_0259
            HAR: HEAR2705(bacA)
            MMS: mma_2930(bacA)
            CCV: CCV52592_0067
            CHA: CHAB381_0437
            CCO: CCC13826_1734
            SUN: SUN_1436(bacA)
            RRU: Rru_A0017
            SPH: MGAS10270_Spy0238(bacA)
            SPI: MGAS10750_Spy0235(bacA)
            SPJ: MGAS2096_Spy0257(bacA)
            SPK: MGAS9429_Spy0240(bacA)
            SPF: SpyM50217(bacA)
            SGO: SGO_1725(bacA)
            CDF: CD2986(bacA2)
            CBO: CBO0320(upk1) CBO0414(upk2)
            DRM: Dred_0427
            MSM: MSMEG_4194
            MGI: Mflv_3043
            RHA: RHA1_ro03154
            CMI: CMM_1695(bacA)
            NCA: Noca_2623
            FRA: Francci3_4459
            FAL: FRAAL3231 FRAAL3678
            PMH: P9215_09341(bacA)
            PVI: Cvib_0492
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.66
            ExPASy - ENZYME nomenclature database: 2.7.1.66
            ExplorEnz - The Enzyme Database: 2.7.1.66
            ERGO genome analysis and discovery system: 2.7.1.66
            BRENDA, the Enzyme Database: 2.7.1.66
            CAS: 9068-22-8
///
ENTRY       EC 2.7.1.67                 Enzyme
NAME        1-phosphatidylinositol 4-kinase;
            phosphatidylinositol kinase (phosphorylating);
            phosphatidylinositol 4-kinase;
            phosphatidylinositol kinase;
            type II phosphatidylinositol kinase;
            PI kinase;
            PI 4-kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:1-phosphatidyl-1D-myo-inositol 4-phosphotransferase
REACTION    ATP + 1-phosphatidyl-1D-myo-inositol = ADP +
            1-phosphatidyl-1D-myo-inositol 4-phosphate [RN:R03361]
ALL_REAC    R03361
SUBSTRATE   ATP [CPD:C00002];
            1-phosphatidyl-1D-myo-inositol [CPD:C01194]
PRODUCT     ADP [CPD:C00008];
            1-phosphatidyl-1D-myo-inositol 4-phosphate [CPD:C01277]
COMMENT     This reaction is catalysed by at least two different isoforms.
REFERENCE   1  [PMID:4284712]
  AUTHORS   Colodzin M, Kennedy EP.
  TITLE     Biosynthesis of diphosphoinositide in brain.
  JOURNAL   J. Biol. Chem. 240 (1965) 3771-80.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4290722]
  AUTHORS   Kai M, White GL, Hawthorne JN.
  TITLE     The phosphatidylinositol kinase of rat brain.
  JOURNAL   Biochem. J. 101 (1966) 328-37.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:2851325]
  AUTHORS   Walker DH, Dougherty N, Pike LJ.
  TITLE     Purification and characterization of a phosphatidylinositol kinase
            from A431 cells.
  JOURNAL   Biochemistry. 27 (1988) 6504-11.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:2833705]
  AUTHORS   Whitman M, Downes CP, Keeler M, Keller T, Cantley L.
  TITLE     Type I phosphatidylinositol kinase makes a novel inositol
            phospholipid, phosphatidylinositol-3-phosphate.
  JOURNAL   Nature. 332 (1988) 644-6.
REFERENCE   5  [PMID:11244087]
  AUTHORS   Barylko B, Gerber SH, Binns DD, Grichine N, Khvotchev M, Sudhof TC,
            Albanesi JP.
  TITLE     A novel family of phosphatidylinositol 4-kinases conserved from
            yeast to humans.
  JOURNAL   J. Biol. Chem. 276 (2001) 7705-8.
  ORGANISM  human [GN:hsa], Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00562  Inositol phosphate metabolism
            PATH: map04070  Phosphatidylinositol signaling system
ORTHOLOGY   KO: K00888  phosphatidylinositol 4-kinase
GENES       HSA: 5297(PI4KA) 5298(PI4KB)
            PTR: 470256(PI4KA)
            MMU: 107650(Pi4kb) 224020(Pi4ka)
            RNO: 64161(Pik4ca) 81747(Pik4cb)
            CFA: 483196(PI4KB) 486443(PI4KA)
            BTA: 282309(PIK4CA) 286846(PIK4CB)
            GGA: 416767(PI4KA) 425661(PI4KB)
            XLA: 444446(pi4kb) 446720(pik4ca)
            SPU: 587444(LOC587444) 590935(LOC590935)
            DME: Dmel_CG10260 Dmel_CG2929(Pi4KIIalpha) Dmel_CG7004(fwd)
            CEL: Y75B8A.24
            OSA: 4333883
            SCE: YLR305C(STT4) YNL267W(PIK1)
            AGO: AGOS_ADL033W AGOS_AFR666C
            PIC: PICST_49430(PIK1) PICST_79239(STT4)
            CAL: CaO19.3199
            CGR: CAGL0D06446g CAGL0J08140g
            SPO: SPAC22E12.16c SPBC577.06c
            ANI: AN4278.2
            AFM: AFUA_7G03760
            AOR: AO090026000840
            CNE: CNG00610 CNI02140
            UMA: UM04931.1 UM06103.1
            DDI: DDBDRAFT_0217974 DDB_0191346(pikD) DDB_0232329
            PFA: PFE0485w
            TAN: TA05835 TA08175
            TPV: TP04_0387
            TET: TTHERM_00157930 TTHERM_00323020 TTHERM_00389990
                 TTHERM_00554370 TTHERM_00655270 TTHERM_00951960
                 TTHERM_01008650
            TBR: Tb927.3.4020 Tb927.4.1140
            LMA: LmjF34.3590
            EHI: 1.t00083
STRUCTURES  PDB: 2JU0  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.67
            ExPASy - ENZYME nomenclature database: 2.7.1.67
            ExplorEnz - The Enzyme Database: 2.7.1.67
            ERGO genome analysis and discovery system: 2.7.1.67
            BRENDA, the Enzyme Database: 2.7.1.67
            CAS: 37205-54-2
///
ENTRY       EC 2.7.1.68                 Enzyme
NAME        1-phosphatidylinositol-4-phosphate 5-kinase;
            diphosphoinositide kinase;
            PIP kinase;
            phosphatidylinositol 4-phosphate kinase;
            phosphatidylinositol-4-phosphate 5-kinase;
            type I PIP kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:1-phosphatidyl-1D-myo-inositol-4-phosphate 5-phosphotransferase
REACTION    ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP +
            1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [RN:R03469]
ALL_REAC    R03469
SUBSTRATE   ATP [CPD:C00002];
            1-phosphatidyl-1D-myo-inositol 4-phosphate [CPD:C01277]
PRODUCT     ADP [CPD:C00008];
            1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [CPD:C04637]
COMMENT     This enzyme can also phosphorylate PtdIns3P in the 4-position, and
            PtdIns, PtdIns3P and PtdIns(3,4)P2 in the 5-position in vitro, but
            to a lesser extent. The last of these reactions occurs in vivo and
            is physiologically relevant. Three different isoforms are known.
REFERENCE   1  [PMID:4295336]
  AUTHORS   Kai M, Salway JG, Hawthorne JN.
  TITLE     The diphosphoinositide kinase of rat brain.
  JOURNAL   Biochem. J. 106 (1968) 791-801.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Kai, M., Salway, J.G., Michell, R.H. and Hawthorne, J.N.
  TITLE     The biosynthesis of triphosphoinositide by rat brain in vitro.
  JOURNAL   Biochem. Biophys. Res. Commun. 22 (1966) 370-375.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:9367159]
  AUTHORS   Rameh LE, Tolias KF, Duckworth BC, Cantley LC.
  TITLE     A new pathway for synthesis of
            phosphatidylinositol-4,5-bisphosphate.
  JOURNAL   Nature. 390 (1997) 192-6.
  ORGANISM  mammalian
PATHWAY     PATH: map00562  Inositol phosphate metabolism
            PATH: map04070  Phosphatidylinositol signaling system
            PATH: map04810  Regulation of actin cytoskeleton
ORTHOLOGY   KO: K00889  1-phosphatidylinositol-4-phosphate 5-kinase
GENES       HSA: 200576(PIP5K3) 23396(PIP5K1C) 5305(PIP4K2A) 79837(PIP4K2C)
                 8394(PIP5K1A) 8395(PIP5K1B) 8396(PIP4K2B)
            PTR: 455590(PIP5K1C) 459908(PIP5K3) 464513(PIP5K1B)
                 467044(PIP4K2C)
            MCC: 710115(LOC710115)
            MMU: 108083(Pip4k2b) 117150(Pip4k2c) 18711(Pip5k3) 18717(Pip5k1c)
                 18718(Pip4k2a) 18719(Pip5k1b) 18720(Pip5k1a)
            RNO: 116723(Pip5k2a) 140607(Pip5k2c) 309419(Pip5k1b)
                 314641(Pip5k1c) 316457(LOC316457) 89812(Pip5k2b)
            CFA: 474417(PIP4K2C) 475846(LOC475846) 476331(PIP5K1B)
                 478890(PIP5K3) 485054(PIP5K1C) 491034(PIP4K2B) 608414(PIP4K2A)
            GGA: 419999(PIP4K2B) 420072(PIP5K1C) 420504(RCJMB04_33l24)
                 424114(PIP5K3) 427243(RCJMB04_20j15)
            XLA: 399394(PIP5K2B) 444238(MGC80809) 496028(LOC496028)
            XTR: 448167(pip5k2c) 448746(pip5k1b)
            DRE: 373124(pip5k2)
            SPU: 578946(LOC578946) 579944(LOC579944) 580595(LOC580595)
            DME: Dmel_CG6355 Dmel_CG9985(sktl)
            CEL: F55A12.3(ppk-1) VF11C1L.1(ppk-3) Y48G9A.8(ppk-2)
            ATH: AT1G10900 AT1G21980(ATPIP5K1) AT1G60890 AT1G71010 AT1G77740
                 AT2G26420 AT2G41210 AT3G07960 AT3G09920(PIP5K9) AT3G14270
                 AT3G56960 AT4G33240
            OSA: 4332323 4333051 4333833 4333853 4340685 4344166 4345628
            CME: CMN333C
            SCE: YDR208W(MSS4)
            AGO: AGOS_AGL096W
            PIC: PICST_64487(MSS4)
            CGR: CAGL0F05335g
            SPO: SPAC19G12.14
            ANI: AN2766.2
            AFM: AFUA_3G06080
            AOR: AO090020000081
            CNE: CNA03760
            UMA: UM03809.1
            DDI: DDBDRAFT_0189390 DDBDRAFT_0218225 DDBDRAFT_0219722
                 DDB_0185056(PIPkinA)
            PFA: MAL1P2.32
            TAN: TA11845
            TPV: TP02_0200
            TET: TTHERM_00047210 TTHERM_00922920 TTHERM_01125130
                 TTHERM_01457080
            TBR: Tb927.4.1620
            TCR: 504057.104
            LMA: LmjF34.3090
            EHI: 13.t00009
            BTL: BALH_3665(ptsH) BALH_4643(ptsH)
            FNU: FN1512 FN1513 FN1514 FN1515
            CHU: CHU_0654(pip)
STRUCTURES  PDB: 1BO1  2GK9  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.68
            ExPASy - ENZYME nomenclature database: 2.7.1.68
            ExplorEnz - The Enzyme Database: 2.7.1.68
            ERGO genome analysis and discovery system: 2.7.1.68
            BRENDA, the Enzyme Database: 2.7.1.68
            CAS: 104645-76-3
///
ENTRY       EC 2.7.1.69                 Enzyme
NAME        protein-Npi-phosphohistidine---sugar phosphotransferase;
            glucose permease;
            PTS permease;
            phosphotransferase, phosphohistidinoprotein-hexose;
            enzyme IIl4ac;
            gene glC proteins;
            gene bglC RNA formation factors;
            PEP-dependent phosphotransferase enzyme II;
            PEP-sugar phosphotransferase enzyme II;
            phosphoenolpyruvate-sugar phosphotransferase enzyme II;
            phosphohistidinoprotein-hexose phosphotransferase;
            phosphohistidinoprotein-hexose phosphoribosyltransferase;
            phosphoprotein factor-hexose phosophotransferase;
            protein, specific or class, gene bglC;
            ribonucleic acid formation factor, gene glC;
            sucrose phosphotransferase system II;
            protein-Npi-phosphohistidine:sugar N-pros-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     protein-Npi-phosphohistidine:sugar Npi-phosphotransferase
REACTION    protein Npi-phospho-L-histidine + sugar = protein histidine + sugar
            phosphate [RN:R03076]
ALL_REAC    R03076 > R00811 R02630 R02631 R02704 R02738 R03232 R04076 R04111
            R04393 R04394 R05132 R05199 R05570 R05820 R06212(G) R06236(G)
            R06237(G) R07671;
            (other) R02780 R06229(G)
SUBSTRATE   protein Npi-phospho-L-histidine;
            sugar [CPD:C11477]
PRODUCT     protein histidine [CPD:C00615];
            sugar phosphate [CPD:C00934]
COMMENT     Enzyme II of the phosphotransferase system. Comprises a group of
            related enzymes. The protein substrate is a phosphocarrier protein
            of low molecular mass (9.5 kDa). The protein is phosphorylated in a
            reaction catalysed by EC 2.7.3.9 (phosphoenolpyruvate---protein
            phosphotransferase) and this acts as the phosphate donor for the
            above reaction. The enzyme translocates the sugar it phosphorylates
            into bacteria. Aldohexoses, and their glycosides and alditols, are
            phosphorylated on O-6, whereas fructose and sorbose are
            phosphorylated on O-1. Glycerone and disaccharides are also
            substrates.
REFERENCE   1  [PMID:778334]
  AUTHORS   Kornberg HL, Riordan C.
  TITLE     Uptake of galactose into Escherichia coli by facilitated diffusion.
  JOURNAL   J. Gen. Microbiol. 94 (1976) 75-89.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:187249]
  AUTHORS   .
  TITLE     The bacterial phosphoenolpyruvate: sugar phosphotransferase system.
  JOURNAL   Biochim. Biophys. Acta. 457 (1976) 213-57.
  ORGANISM  Escherichia coli [GN:eco], Salmonella typhimurium, Staphylococcus
            aureus, Bacillus subtilis [GN:bsu], Aerobacter aerogenes
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00051  Fructose and mannose metabolism
            PATH: map00052  Galactose metabolism
            PATH: map00053  Ascorbate and aldarate metabolism
            PATH: map00500  Starch and sucrose metabolism
            PATH: map00530  Aminosugars metabolism
            PATH: map02060  Phosphotransferase system (PTS)
ORTHOLOGY   KO: K00890  protein-Np-phosphohistidine-sugar phosphotransferase
            KO: K02743  PTS system, N-acetylgalactosamine-specific II component
                        {K02744+K02745+K02746+K02747}
            KO: K02744  PTS system, N-acetylgalactosamine-specific IIA component
            KO: K02745  PTS system, N-acetylgalactosamine-specific IIB component
            KO: K02748  PTS system, arbutin-like II component {K02749+K02750}
            KO: K02749  PTS system, arbutin-like IIB component
            KO: K02751  PTS system, arbutin-, cellobiose-, and salicin-specific
                        II component {K02752+K02753}
            KO: K02752  PTS system, arbutin-, cellobiose-, and salicin-specific
                        IIB component
            KO: K02754  PTS system, beta-glucosides-specific II component
                        {K02755+K02756+K02757}
            KO: K02755  PTS system, beta-glucosides-specific IIA component
            KO: K02756  PTS system, beta-glucosides-specific IIB component
            KO: K02758  PTS system, cellobiose-specific II component
                        {K02759+K02760+K02761}
            KO: K02759  PTS system, cellobiose-specific IIA component
            KO: K02760  PTS system, cellobiose-specific IIB component
            KO: K02762  PTS system, D-glucosamine-specific II component
                        {K02763+K02764+K02765}
            KO: K02763  PTS system, D-glucosamine-specific IIA component
            KO: K02764  PTS system, D-glucosamine-specific IIB component
            KO: K02767  PTS system, fructose-specific II component
                        {K02768+K02769+K02770+K02771}
            KO: K02768  PTS system, fructose-specific IIA component
            KO: K02769  PTS system, fructose-specific IIB component
            KO: K02772  PTS system, galactitol-specific II component
                        {K02773+K02774+K02775}
            KO: K02773  PTS system, galactitol-specific IIA component
            KO: K02774  PTS system, galactitol-specific IIB component
            KO: K02776  PTS system, glucose-specific II component
                        {K02777+K02778+K02779}
            KO: K02777  PTS system, glucose-specific IIA component
            KO: K02778  PTS system, glucose-specific IIB component
            KO: K02780  PTS system, glucitol/sorbitol-specific II component
                        {K02781+K02782+K02783}
            KO: K02781  PTS system, glucitol/sorbitol-specific IIA component
            KO: K02782  PTS system, glucitol/sorbitol-specific IIB component
            KO: K02785  PTS system, lactose-specific II component
                        {K02786+K02787+K02788}
            KO: K02786  PTS system, lactose-specific IIA component
            KO: K02787  PTS system, lactose-specific IIB component
            KO: K02789  PTS system, maltose and glucose-specific II component
                        {K02790+K02791}
            KO: K02790  PTS system, maltose and glucose-specific IIB component
            KO: K02792  PTS system, mannose-specific II component
                        {K02793+K02794+K02795+K02796}
            KO: K02793  PTS system, mannose-specific IIA component
            KO: K02794  PTS system, mannose-specific IIB component
            KO: K02797  PTS system, mannitol-specific II component
                        {K02798+K02799+K02800}
            KO: K02798  PTS system, mannitol-specific IIA component
            KO: K02799  PTS system, mannitol-specific IIB component
            KO: K02801  PTS system, N-acetylglucosamine-specific II component
                        {K02802+K02803+K02804}
            KO: K02802  PTS system, N-acetylglucosamine-specific IIA component
            KO: K02803  PTS system, N-acetylglucosamine-specific IIB component
            KO: K02805  PTS system, nitrogen regulatory II component {K02806}
            KO: K02806  PTS system, nitrogen regulatory IIA component
            KO: K02807  PTS system, sucrose-specific II component
                        {K02808+K02809+K02810}
            KO: K02808  PTS system, sucrose-specific IIA component
            KO: K02809  PTS system, sucrose-specific IIB component
            KO: K02811  PTS system, sorbose-specific II component
                        {K02812+K02813+K02814+K02815}
            KO: K02812  PTS system, sorbose-specific IIA component
            KO: K02813  PTS system, sorbose-specific IIB component
            KO: K02816  PTS system, trehalose-specific II component
                        {K02817+K02818+K02819}
            KO: K02817  PTS system, trehalose-specific IIA component
            KO: K02818  PTS system, trehalose-specific IIB component
            KO: K02820  PTS system, ascorbate-specific II component
                        {K02821+K02822+K03475}
            KO: K02821  PTS system, ascorbate-specific IIA component
            KO: K02822  PTS system, ascorbate-specific IIB component
GENES       ECO: b0129(yadI) b0679(nagE) b0731(hrsA) b1101(ptsG) b1621(malX)
                 b1736(celC) b1738(celA) b1817(manX) b2093(gatB) b2094(gatA)
                 b2167(fruA) b2169(fruB) b2383(ypdD) b2386(ypdG) b2387(ypdH)
                 b2417(crr) b2429(yfeV) b2702(srlA) b2703(srlE) b2704(srlB)
                 b2715(ascF) b2933(cmtA) b2934(cmtB) b3133(agaV) b3138(agaB)
                 b3204(ptsN) b3599(mtlA) b3722(bglF) b3899(frvB) b3900(frvA)
                 b3947(ptsA) b3950(frwB) b3953(frwD) b4194(sgaB) b4195(ptxA)
                 b4240(treB) b4302(sgcA) b4565(sgcB)
            ECJ: JW0125(yadI) JW0665(nagE) JW0720(mngA) JW1087(ptsG)
                 JW1613(malX) JW1725(chbA) JW1727(chbB) JW1806(manX)
                 JW2077(gatB) JW2078(gatA) JW2081(gatA) JW2154(fruA)
                 JW2156(fruB) JW2380(ypdD) JW2383(ypdG) JW2410(crr)
                 JW2422(murP) JW2673(srlB) JW2900(cmtA) JW2901(cmtB)
                 JW3102(agaV) JW3107(agaB) JW3171(ptsN) JW3573(mtlA)
                 JW3659(glvB) JW3700(bglF) JW3871(frvA) JW3922(frwB)
                 JW3925(frwD) JW4152(ulaB) JW4153(ulaC) JW4199(treB)
                 JW4264(sgcA) JW5389(ypdH) JW5429(srlA) JW5430(srlE)
                 JW5435(ascF) JW5555(ptsA) JW5967(sgcB)
            ECE: Z0140(yadI) Z0826(nagE) Z1088 Z1740(ptsG) Z2626(malX)
                 Z2766(celC) Z2768(celA) Z2860(manX) Z3256(gatB) Z3257(gatA)
                 Z3425(fruA) Z3427(fruB) Z3648 Z3652 Z3653 Z3683(crr) Z3694
                 Z4007(srlE_1) Z4009(srlE_2) Z4011(srlB) Z4023(ascF)
                 Z4277(cmtA) Z4278(cmtB) Z4485(agaV) Z4488 Z4492(agaB)
                 Z4567(ptsN) Z4875 Z4876 Z5023(mtlA) Z5178 Z5442(frvB)
                 Z5443(frvA) Z5502(ptsA) Z5506(frwB) Z5509(frwD) Z5616 Z5617
                 Z5803(sgaB) Z5804(ptxA) Z5850(treB)
            ECS: ECs0133 ECs0709 ECs0941 ECs1479 ECs2329 ECs2442 ECs2444
                 ECs2527 ECs2896 ECs2897 ECs3059 ECs3061 ECs3263 ECs3266
                 ECs3267 ECs3289 ECs3300 ECs3560 ECs3571 ECs3808 ECs3809
                 ECs4011 ECs4014 ECs4018 ECs4083 ECs4350 ECs4351 ECs4475
                 ECs4623 ECs4825 ECs4826 ECs4877 ECs4879 ECs4882 ECs5001
                 ECs5002 ECs5170 ECs5171 ECs5217
            ECC: c0158(yadI) c0335 c0336 c0755(nagE) c1373(ptsG) c1957 c1959
                 c2013(malX) c2135(celC) c2137(celA) c2223(manX) c2618(gatB)
                 c2619(gatA) c2702(fruA) c2704(fruB) c2922(ypdD) c2925 c2926
                 c2952(crr) c2962 c3256(srlA) c3257(srlE) c3258(srlB) c3408
                 c3515(cmtA) c3516(cmtB) c3888(agaV) c3891 c3895(agaB)
                 c3964(ptsN) c4277 c4278 c4416(mtlA) c4486 c4487 c4644(bglF)
                 c4758 c4906(ptsA) c4908(frwB) c4912(frwD) c4984 c4985
                 c5283(sgaB) c5284(ptxA) c5339(treB)
            ECI: UTI89_C0142(yadI) UTI89_C0674(nagE) UTI89_C1228 UTI89_C1754
                 UTI89_C1755 UTI89_C1756 UTI89_C1809(malX) UTI89_C1929(celC)
                 UTI89_C1930(celB) UTI89_C1931(celA) UTI89_C2014(manX)
                 UTI89_C2015(manY) UTI89_C2017(manZ) UTI89_C2365(gatC)
                 UTI89_C2366(gatB) UTI89_C2367(gatA) UTI89_C2442(fruA)
                 UTI89_C2444 UTI89_C2715 UTI89_C2718 UTI89_C2719
                 UTI89_C2751(crr) UTI89_C2761 UTI89_C3064(srlA)
                 UTI89_C3065(srlE) UTI89_C3066(srlB) UTI89_C3077(ascF)
                 UTI89_C3215 UTI89_C3320(cmtA) UTI89_C3321(cmtB)
                 UTI89_C3562(agaV) UTI89_C3565 UTI89_C3569(agaB)
                 UTI89_C3570(agaC) UTI89_C3571(agaD) UTI89_C3640(ptsN)
                 UTI89_C3970 UTI89_C3971 UTI89_C4000 UTI89_C4001 UTI89_C4002
                 UTI89_C4137(mtlA) UTI89_C4206 UTI89_C4207 UTI89_C4273(bglF)
                 UTI89_C4399 UTI89_C4538(ptsA) UTI89_C4539(frwC)
                 UTI89_C4540(frwB) UTI89_C4544(frwD) UTI89_C4586 UTI89_C4587
                 UTI89_C4794(sgaB) UTI89_C4795(sgaA) UTI89_C4844(treB)
                 UTI89_C5022(pptE)
            ECP: ECP_0137 ECP_0691 ECP_1093 ECP_1565 ECP_1682 ECP_1684
                 ECP_1760 ECP_1762 ECP_2130 ECP_2131 ECP_2132 ECP_2207 ECP_2209
                 ECP_2412 ECP_2413 ECP_2441 ECP_2451 ECP_2662 ECP_2663 ECP_2664
                 ECP_2676 ECP_2752 ECP_2827 ECP_2926 ECP_2927 ECP_3223 ECP_3230
                 ECP_3292 ECP_3697 ECP_3759 ECP_3760 ECP_3921 ECP_4028 ECP_4161
                 ECP_4163 ECP_4166 ECP_4236 ECP_4237 ECP_4439 ECP_4440 ECP_4489
            ECV: APECO1_1393(nagE) APECO1_182(ptsG) APECO1_1856(yadI)
                 APECO1_2105(pptE) APECO1_2152(treB) APECO1_2449 APECO1_2450
                 APECO1_2514(frwD) APECO1_2519(ptsA) APECO1_2642
                 APECO1_2739(bglF) APECO1_2799 APECO1_2800 APECO1_2858(mtlA)
                 APECO1_2970 APECO1_2971 APECO1_2997 APECO1_2998
                 APECO1_3231(ptsN) APECO1_3289(agaB) APECO1_3293(agaF)
                 APECO1_3296(agaV) APECO1_3596(cmtB) APECO1_3597(cmtA)
                 APECO1_3690 APECO1_3811(ascF) APECO1_3822(srlB)
                 APECO1_3823(srlE) APECO1_3824(srlA) APECO1_4118(yfeV)
                 APECO1_4128(crr) APECO1_4150(ypdH) APECO1_4154(ypdD)
                 APECO1_4385 APECO1_4387(fruA) APECO1_4451(gatA)
                 APECO1_4452(gatB) APECO1_652 APECO1_654 APECO1_704(malX)
                 APECO1_805(celC) APECO1_807(celA)
            ECW: EcE24377A_0705(nagE) EcE24377A_1222(ptsG) EcE24377A_1738
                 EcE24377A_1739 EcE24377A_1829(malX) EcE24377A_1957(chbA)
                 EcE24377A_1959(chbB) EcE24377A_2045(manX) EcE24377A_2381(gatB)
                 EcE24377A_2382(gatA) EcE24377A_2464(fruA) EcE24377A_2702(ptsH)
                 EcE24377A_2704(crr) EcE24377A_2715(murP) EcE24377A_2987(srlE)
                 EcE24377A_3000(ascF) EcE24377A_3267(cmtA) EcE24377A_3613(agaV)
                 EcE24377A_3620(agaB) EcE24377A_4098(mtlA) EcE24377A_4190
                 EcE24377A_4231(bglF) EcE24377A_4429 EcE24377A_4430
                 EcE24377A_4812(treB)
            ECX: EcHS_A0723 EcHS_A1223 EcHS_A1619 EcHS_A1620 EcHS_A1696
                 EcHS_A1820(chbB) EcHS_A1907 EcHS_A2229(gatB) EcHS_A2230(gatA)
                 EcHS_A2304(fruA) EcHS_A2550 EcHS_A2552(crr) EcHS_A2565
                 EcHS_A2839(srlE) EcHS_A2851 EcHS_A3323 EcHS_A3330 EcHS_A3806
                 EcHS_A3894 EcHS_A3936(bglF) EcHS_A4127 EcHS_A4128
                 EcHS_A4438(ulaB) EcHS_A4494(treB)
            STY: STY0196(yadI) STY0723(nagE) STY0918 STY1242(ptsG) STY1448
                 STY1451 STY1799(celC) STY1801(celA) STY1959(manX)
                 STY2439(fruA) STY2442(fruB) STY2573 STY2574 STY2670(crr)
                 STY2816 STY2953(srlA) STY2954(srlE) STY2955(srlB) STY3437
                 STY3438 STY3441(gatA) STY3442(gatB) STY3501(ptsN) STY3925
                 STY3998 STY3999 STY4013 STY4014 STY4111(mtlA) STY4740(sgaB)
                 STY4741(sgaA) STY4794(treB)
            STT: t0179(yadI) t0287 t0424(crr) t0520 t0521 t0650(fruB)
                 t0651(fruA) t1048(manX) t1191(celA) t1193(celC) t1522 t1523
                 t1717(ptsG) t2011 t2190(nagE) t2733(srlA) t2734(srlE)
                 t2735(srlB) t3175 t3176 t3178(gatA) t3179(gatB) t3239(ptsN)
                 t3665 t3734 t3735 t3746 t3747 t3834(mtlA) t4435(sgaB)
                 t4436(sgaA) t4489(treB)
            SPT: SPA0177(yadI) SPA0295 SPA0432(crr) SPA0520 SPA0521
                 SPA0645(fruB) SPA0647(fruA) SPA1043(manX) SPA1253(sgcA)
                 SPA1256 SPA1530(celC) SPA1532(celA) SPA1648(ptsG) SPA1877
                 SPA2056(nagE) SPA2690(srlA) SPA2691(srlE) SPA2692(srlB)
                 SPA3124 SPA3125 SPA3127(gatA) SPA3128(gatB) SPA3189(ptsN)
                 SPA3536(mtlA) SPA3621 SPA3622 SPA3633 SPA3634 SPA4201(sgaB)
                 SPA4202(sgaA) SPA4255(treB)
            SEC: SC0178(yadI) SC0706(nagE) SC0877 SC1153(ptsG) SC1333(celA)
                 SC1335(celC) SC1609(sgcB) SC1612(sgcA) SC1824(manX)
                 SC2220(fruA) SC2222(fruF) SC2344 SC2345(ptxA) SC2431(crr)
                 SC2565(yfeV) SC2765(srlA) SC2766(srlE) SC2767(slrB)
                 SC3199(ptkA) SC3200(ptkB) SC3260(ptsN) SC3609(mtlA)
                 SC3691(ptfB) SC3692 SC3704(ptkB) SC3705 SC4002(ptsA)
                 SC4004(frwB) SC4006(frwD) SC4258(sgaB) SC4259(ptxA)
                 SC4310(pttB) SC4387 SC4388(ptrB)
            STM: STM0178(yadI) STM0576 STM0577 STM0685(nagE) STM0885
                 STM1203(ptsG) STM1312(celA) STM1314(celC) STM1613 STM1616
                 STM1830(manX) STM2204(fruA) STM2206(fruF) STM2343 STM2344
                 STM2433(crr) STM2570 STM2750 STM2751 STM2752 STM2758
                 STM2832(srlA) STM2833(srlE) STM2834(slrB) STM3255 STM3256
                 STM3258 STM3259 STM3322(ptsN) STM3685(mtlA) STM3771 STM3772
                 STM3783 STM3784 STM3858 STM4110(ptsA) STM4113(frwB)
                 STM4116(frwD) STM4384(sgaB) STM4385(ptxA) STM4535 STM4536
            YPE: YPO0402 YPO0403 YPO0405 YPO0834(manX) YPO0837 YPO0851
                 YPO1298(fruB) YPO1300(fruA) YPO1608(ptsG) YPO1758(manX)
                 YPO2569 YPO2570 YPO2628(nagE) YPO2678(celA) YPO2680(celC)
                 YPO2995(crr) YPO3585(ptsN) YPO3697(treB) YPO4068(mtlA)
            YPK: y0157(ptsN) y0166(treB) y1203(nagE) y1251(celA) y1253(celC)
                 y1485(crr) y1618 y1767(ptsG) y2551(manX) y2885(fruA)
                 y2887(fruB) y3219(agaV) y3222 y3236 y3776(ptsA) y3778(frwB)
                 y3780(frwD) y4087(mtlA)
            YPM: YP_1085(nagE) YP_1292(fruA) YP_1294(fruB) YP_1634(manX1)
                 YP_2246(ptsG) YP_2380(ptsN1) YP_2381(sgaB) YP_2480(celA)
                 YP_2482(celC) YP_2620(crr) YP_3530(manX2) YP_3533(manX3)
                 YP_3776(ptsA) YP_3778(frwB) YP_3779(frwD) YP_3839(ptsN2)
                 YP_3847(treB) YP_3979(mtlA)
            YPA: YPA_0419 YPA_0433 YPA_1015 YPA_1017 YPA_1130 YPA_1917
                 YPA_2058 YPA_2059 YPA_2185 YPA_2407 YPA_2409 YPA_2469 YPA_3014
                 YPA_3710 YPA_3718 YPA_3880 YPA_3882 YPA_3883
            YPN: YPN_0272 YPN_0273 YPN_0275 YPN_1114 YPN_1164 YPN_1166
                 YPN_1387 YPN_2021 YPN_2161 YPN_2162 YPN_2365 YPN_2679 YPN_2681
                 YPN_3036 YPN_3039 YPN_3053 YPN_3467 YPN_3475 YPN_3715
            YPP: YPDSF_1594 YPDSF_1839 YPDSF_2103
            YPS: YPTB0542(frwD) YPTB0543(frwB) YPTB0544(frwC) YPTB0545(pstA)
                 YPTB1120(nagE) YPTB1329(fruB) YPTB1331(fruA) YPTB1634(manX)
                 YPTB2463(ptsG) YPTB2600 YPTB2601 YPTB2717(crr) YPTB2929(celC)
                 YPTB2931(celA) YPTB3078(manX) YPTB3081 YPTB3528(ptsN)
                 YPTB3536(treB) YPTB3918(mtlA)
            YPI: YpsIP31758_0431(treB) YpsIP31758_0940(agaV)
                 YpsIP31758_1091(chbB) YpsIP31758_1586(ptsG) YpsIP31758_2368
                 YpsIP31758_2681(fruA) YpsIP31758_2908(nagE)
                 YpsIP31758_3529(frwC) YpsIP31758_3530(frwB)
                 YpsIP31758_4128(mtlA)
            YEN: YE0552(scrA) YE0813(sorB) YE0814(sorF) YE0970(celC)
                 YE1096(gutB) YE1097(gutE) YE1256(ascF) YE1447(fpr)
                 YE2011(malX) YE2104(arbF) YE2638 YE3199(aglA) YE4103 YE4104
            SFL: SF0126(yadI) SF0566 SF0614(nagE) SF1105(ptsG) SF1411(manX)
                 SF1488(celA) SF1490(celC) SF1645(malX) SF2155(gatB)
                 SF2156(gatA) SF2252(fruA) SF2254(fruB) SF2449(ypdD)
                 SF2452(ypdG) SF2453(ypdH) SF2472(crr) SF2483(yfeV)
                 SF2726(srlE) SF2727(srlB) SF3168(agaV) SF3171(yadI)
                 SF3244(ptsN) SF3633(mtlA) SF3733 SF3780(glvC) SF3976(frvB)
                 SF3977(frvA) SF4027(frwB) SF4030(frwD) SF4091 SF4092
                 SF4250(treB) SF4349(sgaB) SF4350(ptxA)
            SFX: S0128(yadI) S0579(hrsA) S0625(nagE) S1185(ptsG) S1526(manX)
                 S1605(celA) S1607(celC) S1778(malX) S2281(gatB) S2282(gatA)
                 S2381(fruA) S2383(fruB) S2588 S2591 S2592 S2618(crr) S2630
                 S2917(srlE) S2918(srlB) S3383(agaV) S3386(agaF) S3462(ptsN)
                 S3638(sorF) S3639(sorB) S3716(frwD) S3719(frwB) S3771(frvA)
                 S3772(frvB) S3989(glvB) S4039(bglF) S4135(mtlA) S4512(treB)
                 S4619(sgaB) S4620(ptxA)
            SFV: SFV_0652(nagE) SFV_1121(ptsG) SFV_1412(manX) SFV_1482(celA)
                 SFV_1484(celC) SFV_1638(malX) SFV_2148(gatB) SFV_2242(fruA)
                 SFV_2244(fruB) SFV_2441 SFV_2445 SFV_2469(crr) SFV_2482
                 SFV_2790(ascF) SFV_2801(srlB) SFV_2803(srlA) SFV_3234(ptsN)
                 SFV_3595(frvA) SFV_3596(frvB) SFV_3785(bglF) SFV_3828(glvC)
                 SFV_3938(mtlA) SFV_4019(frwB) SFV_4022(frwD) SFV_4096(sorB)
                 SFV_4097(sorF) SFV_4350(sgaB) SFV_4351(ptxA)
            SSN: SSON_0137(yadI) SSON_0633(nagE) SSON_0682(hrsA)
                 SSON_1121(ptsG) SSON_1343(manX) SSON_1420(celA)
                 SSON_1422(celC) SSON_1537(malX) SSON_2140(gatB)
                 SSON_2223(fruA) SSON_2225(fruB) SSON_2478 SSON_2479
                 SSON_2506(crr) SSON_2846(srlA) SSON_2847(srlE) SSON_2848(srlB)
                 SSON_2859(ascF) SSON_3088(cmtB) SSON_3352(ptsN)
                 SSON_3634(glvC) SSON_3809(mtlA) SSON_3912(bglF)
                 SSON_4069(frvB) SSON_4070(frvA) SSON_4121(ptsA)
                 SSON_4126(frwD) SSON_4197(sorF) SSON_4376(sgaB)
                 SSON_4377(ptxA) SSON_4421(treB)
            SBO: SBO_0118(yadI) SBO_0541(nagE) SBO_0914(gatB) SBO_0915(gatA)
                 SBO_1352(celA) SBO_1513(malX) SBO_1962(ptsG) SBO_2155(fruB)
                 SBO_2157(fruA) SBO_2409 SBO_2413 SBO_2441(crr) SBO_2454
                 SBO_2803(ascF) SBO_2814(srlB) SBO_2815(srlE) SBO_2816(srlA)
                 SBO_3055(cmtB) SBO_3056(cmtA) SBO_3178(ptsN) SBO_3597(mtlA)
                 SBO_3688(glvC) SBO_3915(frvB) SBO_3916(frvA) SBO_3967(ptsA)
                 SBO_3969(frwB) SBO_3972(frwD) SBO_4046(sorB) SBO_4047(sorF)
                 SBO_4206(treB) SBO_4260(ptxA) SBO_4261(sgaB)
            SDY: SDY_0038(yadI) SDY_1842(malX) SDY_2049(ptsG) SDY_2265(gatB)
                 SDY_2315(fruA) SDY_2317(fruB) SDY_2586 SDY_2614(crr) SDY_2625
                 SDY_2898(srlA) SDY_2901(srlB) SDY_3143(cmtB) SDY_3144(cmtA)
                 SDY_3385(ptsN) SDY_3641 SDY_3642 SDY_3782(ptsA) SDY_3785(frwB)
                 SDY_3788(frwD) SDY_4259(treB) SDY_4363(sgaB) SDY_4364(ptxA)
            ECA: ECA0087(mtlA) ECA0286(ptsN) ECA0341 ECA0342 ECA0362(scrA)
                 ECA0661 ECA0860 ECA0891(crr) ECA1327(nagE) ECA1805(ptsG)
                 ECA1848(aglA) ECA1870(arbF) ECA2165(ascF) ECA2356
                 ECA2385(manX) ECA2488 ECA2489 ECA2727(fruA) ECA2729(fruB)
                 ECA3013(treB) ECA3136 ECA3225 ECA3645 ECA3648 ECA3773(sgcA)
                 ECA3774 ECA4409 ECA4433 ECA4435
            PLU: plu0402 plu0583(bglF) plu0585 plu0835(agaV) plu0838
                 plu1318(nagE) plu1392(crr) plu1979(sgcA) plu1980(sgaB) plu1989
                 plu1992(fruB) plu1993(fruA) plu2697(manX) plu2754(celA)
                 plu2756(celC) plu3288(treB) plu4043(ptsN)
            BUC: BU063(crr) BU356(ptsG) BU572(mtlA)
            BAS: BUsg060(crr) BUsg344(ptsG) BUsg552(mtlA)
            BAB: bbp059(crr) bbp326(ptsG) bbp517(mtlA)
            SGL: SG0014 SG0197 SG0859 SG1327 SG1703 SG1745 SG1746 SG1913
                 SG1984 SG2041 SG2042 SG2426 SG2427
            ENT: Ent638_0017 Ent638_1616 Ent638_1827 Ent638_2763 Ent638_2945
                 Ent638_3015
            KPN: KPN_04802
            SPE: Spro_1858 Spro_2813 Spro_3570 Spro_3847 Spro_4223
            BFL: Bfl445(manX)
            BPN: BPEN_459(manX)
            HIN: HI0446(fruA) HI0448(fruB) HI1147(ptsN) HI1711(crr)
            HIT: NTHI0573(fruA) NTHI1315(ptsN) NTHI2020(crr)
            HDU: HD0227(crr) HD0585(ptsN) HD0768(manX) HD1859 HD1860(sgaT)
            HSO: HS_0437 HS_0607(manZ) HS_0608(manY) HS_0609(manX)
                 HS_0677(srlB) HS_0678(srlE) HS_0679(srlA) HS_1096(crr)
                 HS_1143(gatB) HS_1144(gatA) HS_1177(ptsN) HS_1252(mtlA)
            PMU: PM0170(ptsN) PM0764 PM0765 PM0834 PM0876 PM0896(crr)
                 PM1061(ptmA) PM1575 PM1752(ptsG) PM1795(fruA) PM1797(fruB)
                 PM1846(ptsB) PM1969 PM1970 PM1971
            MSU: MS0021(ptsN) MS0022(sgaT) MS0149(ptsN) MS0150(sgaB)
                 MS0411(mtlA) MS0618 MS0784(ptsG) MS1237(ptsG) MS1508(nagE)
                 MS1717(ptsN) MS2178(fruA) MS2180(ptsN) MS2379
            APL: APL_0335(ptsN) APL_0343(fruA) APL_0345(fruB) APL_1319(ptsB)
                 APL_1324(crr) APL_1391 APL_1630(mtlA) APL_1662 APL_1699(ulaC)
                 APL_1700(ulaA) APL_1715(sgaB)
            ASU: Asuc_0286 Asuc_0435 Asuc_0455 Asuc_0938
            XFA: XF1404
            XFT: PD0633
            XCC: XCC2370(fruB) XCC2372(fruA) XCC2804(ptsN) XCC2807
            XCB: XC_1306 XC_1309 XC_1742 XC_1744
            XCV: XCV2679(fruB) XCV2681(fruA) XCV3120 XCV3123
            XAC: XAC2501(fruB) XAC2503(fruA) XAC2974(ptsN) XAC2977
            XOO: XOO1279 XOO1282(ptsN) XOO2810(fruB) XOO2812(fruA)
            XOM: XOO_1177(XOO1177) XOO_1181(XOO1181) XOO_2650(XOO2650)
                 XOO_2652(XOO2652)
            VCH: VC0207 VC0518(dnaG) VC0910 VC0964 VC0995 VC1281 VC1283 VC1820
                 VC1821 VC1822 VC1823 VC1824 VC1826 VC2013 VC2531 VCA0245
                 VCA0246 VCA0516 VCA0518 VCA0653 VCA1045
            VCO: VC0395_0196(mtlA) VC0395_0597(scrA) VC0395_A0432(treB)
                 VC0395_A0516(nagE) VC0395_A0900(celA) VC0395_A2111(ptsN)
            VVU: VV1_0179 VV1_0212 VV1_0289 VV1_0638 VV1_0694 VV1_1482
                 VV1_1484 VV1_2999 VV2_0198 VV2_0200 VV2_0860 VV2_0861 VV2_1019
                 VV2_1022 VV2_1080 VV2_1081 VV2_1142 VV2_1349 VV2_1351 VV2_1352
                 VV2_1353 VV2_1356 VV2_1357
            VVY: VV0446(ptsN) VV0505 VV0540 VV0895 VV0976 VV1012 VV1283 VV2899
                 VV2901 VVA0188 VVA0190 VVA0191 VVA0192 VVA0195 VVA0196 VVA0704
                 VVA0706 VVA1331 VVA1332 VVA1392 VVA1395 VVA1511 VVA1514
                 VVA1604 VVA1605 VVA1668
            VPA: VP0370 VP0710 VP0793 VP0831 VP2046 VP2635 VP2637 VP2672(ptsN)
                 VPA0230 VPA0231 VPA0297 VPA0298 VPA0500 VPA0501 VPA0811
                 VPA0813 VPA1420 VPA1421 VPA1422 VPA1424 VPA1667 VPA1744
            VFI: VF0385 VF0603 VF0604 VF0607 VF0808 VF1115 VF1719 VF1732
                 VF1897 VFA0060 VFA0061 VFA0128 VFA0130 VFA0369 VFA0370 VFA0438
                 VFA0709 VFA0711(HPr) VFA0712 VFA0713 VFA0786 VFA0940 VFA0942
                 VFA1000 VFA1003
            PPR: PBPRA0861 PBPRA1032(pts18CBA) PBPRA1203 PBPRA1224
                 PBPRA1573(fruB) PBPRA1575 PBPRA1760 PBPRA2052(PTS-EIIB)
                 PBPRA2055 PBPRA2715 PBPRA2718 PBPRA2719 PBPRA2776(celA)
                 PBPRA2778 PBPRA3257(ptsN) PBPRB0143 PBPRB0146 PBPRB0217
                 PBPRB0263 PBPRB0273 PBPRB0274(ptxA) PBPRB0363 PBPRB1038
                 PBPRB1041(agaF) PBPRB2005 PBPRB2008(celA)
            PAE: PA3560(fruA) PA3562 PA3760 PA3761 PA4464(ptsN)
            PAU: PA14_15780(nagE) PA14_18275(fruA) PA14_57960(ptsN)
            PPU: PP_0793(fruB) PP_0795(fruA) PP_0950(ptsN)
            PST: PSPTO_0954 PSPTO_0956 PSPTO_4455(ptsN)
            PSB: Psyr_0821 Psyr_0823 Psyr_4149(ptsN)
            PSP: PSPPH_0847 PSPPH_0849 PSPPH_4153(ptsN)
            PFL: PFL_0859 PFL_0861(fruA) PFL_0913(ptsN) PFL_1078(nagE)
                 PFL_1079 PFL_3614(ptsN) PFL_4934(treP)
            PFO: Pfl_0793 Pfl_0795 Pfl_0855(ptsN) Pfl_1003 Pfl_1004
            PEN: PSEEN0932 PSEEN0934(fruA) PSEEN1091(ptsN) PSEEN4382 PSEEN4383
            PMY: Pmen_0868
            ACI: ACIAD1990(fruB) ACIAD1993(fruA)
            SON: SO_1623(ptsG) SO_2236(crr) SO_3963(ptsN)
            SDN: Sden_0487 Sden_1548 Sden_1816
            SFR: Sfri_1264 Sfri_1767 Sfri_2652 Sfri_3379
            SAZ: Sama_1649
            SBL: Sbal_2362
            SLO: Shew_1864 Shew_3313
            SPC: Sputcn32_2120
            SHE: Shewmr4_0671 Shewmr4_1763 Shewmr4_2648
            SHM: Shewmr7_1841 Shewmr7_2715 Shewmr7_3351
            SHN: Shewana3_0670 Shewana3_2258 Shewana3_2822
            SHW: Sputw3181_1892 Sputw3181_3460
            ILO: IL0394(ptsN)
            CPS: CPS_4545(ptsN)
            PHA: PSHAa1333 PSHAa2553(ptsN)
            PAT: Patl_0570 Patl_2509
            PIN: Ping_2441 Ping_2725 Ping_2893
            MAQ: Maqu_2717
            FTU: FTT1280c(ptsN)
            FTF: FTF1280c(ptsN)
            FTL: FTL_1180
            FTH: FTH_1156
            FTN: FTN_1295(ptsN)
            NOC: Noc_2795 Noc_2798
            AEH: Mlg_2232
            HCH: HCH_05323(ptsN)
            CSA: Csal_2228
            ABO: ABO_0550(ptsN)
            AHA: AHA_0116 AHA_0172 AHA_0173 AHA_0412 AHA_0551 AHA_0807
                 AHA_0810 AHA_1168(ptsG) AHA_1418 AHA_1419 AHA_1421
                 AHA_1427(malX) AHA_1527(nagE) AHA_2341 AHA_2342 AHA_2346(fruA)
                 AHA_2979 AHA_3039(ptsH) AHA_3041(crr) AHA_3824(treP)
            ASA: ASA_0477(celC)
            DNO: DNO_0610
            BCI: BCI_0069(ptsH) BCI_0451
            NME: NMB0736 NMB2046
            NMA: NMA0390 NMA0946
            NMC: NMC2026
            NGO: NGO0313 NGO2036
            CVI: CV_0241 CV_0558 CV_0559(nagE) CV_0814 CV_0979(ptsG) CV_0980
                 CV_2310(frwB) CV_2311(ptsA) CV_3052(fruB) CV_3054(fruA)
                 CV_3300(treB) CV_3334
            RSO: RS05327(RSp1282) RSc0346(RS03313) RSc0406(ptsN) RSc2861(fruB)
                 RSc2863(fruA) RSp1285(scrA)
            REU: Reut_A0295 Reut_A0353(ptsN)
            REH: H16_A0311(nagF) H16_A0312(nagE) H16_A0324(fruA) H16_A0384
            RME: Rmet_0244 Rmet_0300
            BMA: BMA3110(ptsN) BMA3171 BMA3172(nagE) BMA3213
            BMV: BMASAVP1_A0078(ptsN) BMASAVP1_A0142(nagE) BMASAVP1_A0187
            BML: BMA10299_A1405 BMA10299_A1446(nagE) BMA10299_A1512(ptsN)
            BMN: BMA10247_2832 BMA10247_2874(nagE) BMA10247_2940(ptsN)
            BXE: Bxe_A4124 Bxe_A4152 Bxe_A4153 Bxe_A4186
            BUR: Bcep18194_A6123(ptsN) Bcep18194_A6151 Bcep18194_A6152
                 Bcep18194_A6191 Bcep18194_C7243
            BCN: Bcen_2179
            BCH: Bcen2424_2793 Bcen2424_2862
            BAM: Bamb_2853 Bamb_2917
            BPS: BPSL0438 BPSL0498 BPSL0499 BPSL0531
            BPM: BURPS1710b_0656 BURPS1710b_0723 BURPS1710b_0724(nagE)
                 BURPS1710b_0763(ptsN)
            BPL: BURPS1106A_0555(nagE) BURPS1106A_0595(ptsN)
            BPD: BURPS668_0538(nagE) BURPS668_0579(ptsN)
            BTE: BTH_I0411 BTH_I0450 BTH_I0484(ptsN) BTH_II0906 BTH_II0908
            BPE: BP0694(rpoP) BP1500
            BPA: BPP1966 BPP4034(rpoP)
            BBR: BB2153 BB4507(rpoP)
            RFR: Rfer_0601 Rfer_0751
            POL: Bpro_0297 Bpro_4612
            PNA: Pnap_3793
            AAV: Aave_4557
            AJS: Ajs_3926
            VEI: Veis_2220
            MPT: Mpe_A0225
            HAR: HEAR2883(ptsN)
            MMS: mma_0173 mma_1800
            NEU: NE0060(ptsN) NE2183
            NET: Neut_0531 Neut_2305
            NMU: Nmul_A0218
            EBA: ebA2794(manX) ebA3391(ptsN)
            AZO: azo0502(ptsN) azo3780(ptsL)
            DAR: Daro_1083 Daro_4082 Daro_4147(ptsN)
            TBD: Tbd_0531(ptsN) Tbd_2412
            MFA: Mfla_0146
            SUN: SUN_2238
            GSU: GSU0735 GSU1883
            GME: Gmet_1287 Gmet_2604
            PCA: Pcar_1933 Pcar_1934 Pcar_1936
            DVU: DVU0981 DVU1630 DVU1632 DVU1633
            DVL: Dvul_1503
            DDE: Dde_1180 Dde_1773(ptsN) Dde_1775 Dde_1776
            ADE: Adeh_0148 Adeh_0149 Adeh_3653 Adeh_4165
            MXA: MXAN_6534 MXAN_6535
            SAT: SYN_00943 SYN_02844 SYN_02845
            SFU: Sfum_2065 Sfum_2067
            MLO: mll3194 mll3610 mll3613 mll5091
            MES: Meso_3574 Meso_3665
            SME: SMc01141(ptsN) SMc02753
            ATU: Atu0031 Atu0330(ptsN)
            ATC: AGR_C_50 AGR_C_576
            RET: RHE_CH00033 RHE_CH00407(ptsNch)
            RLE: RL0033 RL0425(ptsN) RL2903
            BME: BMEI1786 BMEI2032
            BMF: BAB1_0160 BAB1_2096
            BMS: BR0161(ptsN) BR2094
            BMB: BruAb1_0157(ptsN) BruAb1_2069
            OAN: Oant_4110
            BJA: blr0725(ptsN) blr8147
            RPA: RPA0052(ptsN1) RPA0355 RPA2999(ptsN2)
            RPB: RPB_0466 RPB_0653(ptsN)
            RPC: RPC_0413 RPC_0594
            RPD: RPD_0180 RPD_0370 RPD_0667
            RPE: RPE_0432 RPE_0824
            NWI: Nwi_0179(ptsN) Nwi_0345
            NHA: Nham_0171 Nham_0440
            BHE: BH00180(ptsN) BH00590
            BQU: BQ00170(ptsN) BQ00530
            BBK: BARBAKC583_1365(ptsN)
            CCR: CC_0240 CC_0448 CC_0449 CC_0537 CC_0538 CC_3596
            SIL: SPO0077(ptsN) SPO0714
            SIT: TM1040_0021 TM1040_2437
            RSP: RSP_1158(ptsN) RSP_1685 RSP_1786(fruB) RSP_1788(fruA)
            JAN: Jann_0223
            RDE: RD1_0373(ptsN) RD1_1382
            MMR: Mmar10_0076 Mmar10_0103
            HNE: HNE_0438
            ZMO: ZMO0037(nagE) ZMO1326(nagE)
            NAR: Saro_0111 Saro_2412 Saro_2413 Saro_2903
            SAL: Sala_2051 Sala_2836
            ELI: ELI_02115 ELI_12970
            GOX: GOX0813(HPr) GOX0814
            GBE: GbCGDNIH1_0396 GbCGDNIH1_0410 GbCGDNIH1_0412
            RRU: Rru_A0009 Rru_A1970 Rru_A1972
            MAG: amb3938 amb4395
            BSU: BG10198(ptsG) BG10316(levD) BG10317(levE) BG10560(sacX)
                 BG10595(sacP) BG10934(bglP) BG11009(treP) BG11014(gamP)
                 BG11215(mtlA) BG11347(licB) BG11349(licA) BG11450(ypqE)
                 BG11567(ybbF) BG11848(malP) BG11938(fruA) BG12190(ydhM)
                 BG12191(ydhN) BG12941(nagP) BG13176(manP) BG14172(yyzE)
            BHA: BH0191(gatB) BH0192(gatA) BH0221 BH0222 BH0296 BH0422
                 BH0595(bglP) BH0673 BH0772 BH0773 BH0828(fruA) BH0844 BH0909
                 BH0910 BH1515 BH1856(sacP) BH2216 BH3574 BH3852 BH3854 BH3920
                 BH3921
            BAN: BA0372 BA0501 BA0631(treB) BA0754(scrA) BA0791(celC-1)
                 BA0792(celA-1) BA0793(celB-1) BA0823 BA2462 BA3846
                 BA4269(ptsG) BA5442(celC-2) BA5444(celA-2) BA5447(celC-3)
                 BA5449(celA-3) BA5563
            BAR: GBAA0372 GBAA0501 GBAA0631(treB) GBAA0754(scrA)
                 GBAA0791(celC-1) GBAA0792(celA-1) GBAA0793(celB-1) GBAA0823
                 GBAA2462 GBAA3846 GBAA4269(ptsG) GBAA5442(celC-2)
                 GBAA5444(celA-2) GBAA5447(celC-3) GBAA5449(celA-3) GBAA5563
            BAA: BA_0295 BA_0297 BA_0300 BA_0302 BA_0418 BA_0946 BA_1071
                 BA_1214 BA_1338 BA_1377 BA_1378 BA_1379 BA_1410 BA_2957
                 BA_4319 BA_4729
            BAT: BAS0358 BAS0472 BAS0598 BAS0718 BAS0752 BAS0753 BAS0754
                 BAS0784 BAS2290 BAS3563 BAS3960 BAS5057 BAS5059 BAS5062
                 BAS5064 BAS5169
            BCE: BC0414 BC0482 BC0631 BC0775 BC0807 BC0808 BC0809 BC0842
                 BC2393 BC3718 BC4050 BC5210 BC5215 BC5217 BC5320
            BCA: BCE_0482 BCE_0554 BCE_0699(treB) BCE_0882(celC)
                 BCE_0883(celA) BCE_0884(celB) BCE_0914 BCE_2495 BCE_2982
                 BCE_3744 BCE_4117(ptsG) BCE_5319(celC) BCE_5320(celB)
                 BCE_5321(celA) BCE_5324(celC) BCE_5325(celB) BCE_5326(celA)
                 BCE_5445
            BCZ: BCZK0344(ptsG) BCZK0411(nagE) BCZK0542(treB) BCZK0687(celC)
                 BCZK0688(celA) BCZK0689(celB) BCZK0719(scrA) BCZK0859(bglP)
                 BCZK2211(celA) BCZK2212(celB) BCZK2663 BCZK3476(fruA)
                 BCZK3806(ptsG) BCZK4902(celC) BCZK4903(celB) BCZK4904(licB)
                 BCZK4907(celC) BCZK4908(celB) BCZK4909(celA) BCZK5019
                 pE33L466_0345(levD) pE33L466_0347(levG) pE33L466_0348(levE)
            BCY: Bcer98_1790 Bcer98_3753
            BTK: BT9727_0348(ptsG) BT9727_0415(nagE) BT9727_0542(treB)
                 BT9727_0668(scrA) BT9727_0700(celC) BT9727_0701(celA)
                 BT9727_0702(celB) BT9727_0733(scrA) BT9727_0877(bglP)
                 BT9727_2253(celA) BT9727_2254(celB) BT9727_3462(fruA)
                 BT9727_3791(ptsG) BT9727_4887(celC) BT9727_4888(celB)
                 BT9727_4889(licB) BT9727_4894(celC) BT9727_4895(celB)
                 BT9727_4896(celA) BT9727_5003
            BTL: BALH_0370(ptsG) BALH_0438(nagE) BALH_0568(treP)
                 BALH_0690(scrA) BALH_0719(celC) BALH_0720(celA)
                 BALH_0721(celB) BALH_2193(celA) BALH_2194(celB)
                 BALH_3666(ptsG) BALH_4702(celC) BALH_4704(celA)
                 BALH_4708(celC) BALH_4710(celA) BALH_4764(manP) BALH_4820(crr)
            BLI: BL00088(nagP) BL00213(bglPB) BL00289(manP) BL00914(sacX)
                 BL01161 BL01380 BL01606(fruA) BL01637 BL01775 BL01800 BL01801
                 BL01901(fruAB) BL01902(fruAA) BL01947(bglPA) BL02334 BL02487
                 BL02489 BL02490 BL02718(ybbF) BL03019(malP) BL03068(treP)
                 BL03123(levE) BL03124(levD) BL03565(ptsG) BL03841(licB)
                 BL03842(licC) BL03843(licA) BL03890(sacP) BL05259
            BLD: BLi00189(ybbF) BLi00268 BLi00332 BLi00333 BLi00493
                 BLi00505(mtlA) BLi00506 BLi00748 BLi00796(treP) BLi00842(sacX)
                 BLi00857(malP) BLi01598(ptsG) BLi01654(fruA) BLi02108(manP)
                 BLi02359(ypqE) BLi02506 BLi02563(ydhN) BLi02564(ydhM)
                 BLi02830(levE) BLi03550 BLi03551 BLi03864 BLi03865
                 BLi04017(sacP) BLi04087(licA) BLi04088(licC) BLi04089(licB)
                 BLi04200 BLi04215(bglP) BLi04352(nagP)
            BCL: ABC0194(ptsG) ABC0312 ABC0446 ABC0447 ABC0448 ABC0481
                 ABC0483(licA) ABC0640 ABC0641 ABC0713 ABC0885 ABC1104 ABC1157
                 ABC1158 ABC1159 ABC1263(treP) ABC1271(fruA) ABC1773 ABC2080
                 ABC2927 ABC2929 ABC3196 ABC3197 ABC3234 ABC3235 ABC3337(nagP)
                 ABC3346 ABC3347 ABC3571 ABC3572 ABC3580(malP) ABC3666 ABC3764
                 ABC3790(bglP) ABC4070(levD) ABC4071(levE)
            BAY: RBAM_002170(ybbF) RBAM_004230 RBAM_004240 RBAM_007900
                 RBAM_007970(treP) RBAM_012170(lacF) RBAM_013660
                 RBAM_014140(fruA) RBAM_020380(ypqE) RBAM_035290(sacP)
                 RBAM_035770(licA) RBAM_035790(licB) RBAM_036360(bglP)
            BPU: BPUM_0209 BPUM_1279 BPUM_1742 BPUM_3452(sacP) BPUM_3504(licA)
                 BPUM_3506(licB) BPUM_3536 BPUM_3644
            OIH: OB0615 OB0838(fruA) OB1882 OB2275 OB2276 OB2601 OB2603 OB2754
                 OB2755 OB2758 OB2760 OB2762 OB3375 OB3415 OB3416
            GKA: GK0991 GK1747 GK1838 GK1858 GK1859 GK1946 GK1948 GK2017
                 GK3444 GK3446
            GTN: GTNG_1845
            SAU: SA0183(glcA) SA0186 SA0233 SA0236 SA0237 SA0255 SA0319 SA0320
                 SA0432(treP) SA0655(fruA) SA1255 SA1547(ptaA) SA1960(mtlF)
                 SA1962(mtlA) SA1992(lacE) SA1993(lacF) SA2114(glvC)
                 SA2167(scrA) SA2326(ptsG) SA2434
            SAV: SAV0189(glcA) SAV0192 SAV0242 SAV0245 SAV0246 SAV0265 SAV0330
                 SAV0331 SAV0474(treP) SAV0700(fruA) SAV1422 SAV1726(ptaA)
                 SAV2156(mtlF) SAV2158(mtlA) SAV2190(lacE) SAV2191(lacF)
                 SAV2323(glvC) SAV2377(scrA) SAV2538(ptsG) SAV2641
            SAM: MW0163(glcA) MW0166 MW0218 MW0221 MW0222 MW0241 MW0307 MW0308
                 MW0428(treP) MW0662(fruA) MW1312 MW1668(ptaA) MW2082(mtlF)
                 MW2084(mtlA) MW2116(lacE) MW2117(lacF) MW2244(glvC)
                 MW2299(scrA) MW2459(ptsG) MW2562
            SAR: SAR0190(glcA) SAR0193 SAR0235 SAR0240 SAR0241 SAR0263 SAR0327
                 SAR0328 SAR0473 SAR0753(fruA) SAR1435 SAR1803 SAR2244(mtlA)
                 SAR2246(mtlF) SAR2281(lacE) SAR2282(lacF) SAR2408
                 SAR2466(scrA) SAR2618(glcB) SAR2720
            SAS: SAS0164 SAS0167 SAS0218 SAS0221 SAS0222 SAS0242 SAS0307
                 SAS0308 SAS0431 SAS0665 SAS1365 SAS1652 SAS2057 SAS2059
                 SAS2091 SAS2092 SAS2216 SAS2269 SAS2424 SAS2527
            SAC: SACOL0175 SACOL0178 SACOL0224 SACOL0229 SACOL0230 SACOL0250
                 SACOL0401 SACOL0402 SACOL0516 SACOL1457 SACOL1775 SACOL2146
                 SACOL2148 SACOL2181(lacE) SACOL2182(lacF) SACOL2316 SACOL2376
                 SACOL2552 SACOL2663
            SAB: SAB0129c(glcA) SAB0132 SAB0181c SAB0184 SAB0185 SAB0186
                 SAB0204 SAB0279c SAB0280c SAB0423 SAB0649(fruA) SAB1277c
                 SAB1584c SAB2036(mtlA) SAB2038(mtlF) SAB2071c(lacE)
                 SAB2072c(lacF) SAB2200c SAB2257c(scrA) SAB2412c(glcB) SAB2516
            SAA: SAUSA300_0191(ptsG) SAUSA300_0194 SAUSA300_0236 SAUSA300_0239
                 SAUSA300_0240 SAUSA300_0259 SAUSA300_0331 SAUSA300_0332
                 SAUSA300_0448(treP) SAUSA300_0685(fruA) SAUSA300_1315(crr)
                 SAUSA300_1672(nagE) SAUSA300_2105(mtlF) SAUSA300_2107(mtlA)
                 SAUSA300_2150(lacE) SAUSA300_2151(lacF) SAUSA300_2270(glvC)
                 SAUSA300_2324 SAUSA300_2476(ptsG) SAUSA300_2576
            SAO: SAOUHSC_00155 SAOUHSC_00158 SAOUHSC_00209 SAOUHSC_00214
                 SAOUHSC_00215 SAOUHSC_00235 SAOUHSC_00311 SAOUHSC_00312
                 SAOUHSC_00437 SAOUHSC_00708 SAOUHSC_01430 SAOUHSC_01836
                 SAOUHSC_02400 SAOUHSC_02402 SAOUHSC_02450 SAOUHSC_02451
                 SAOUHSC_02597 SAOUHSC_02661 SAOUHSC_02662 SAOUHSC_02848
                 SAOUHSC_02975
            SAJ: SaurJH9_2221
            SAH: SaurJH1_2260
            SEP: SE0472 SE1115 SE1403 SE1782 SE1783 SE1890 SE1897 SE1959
                 SE2102 SE2228
            SER: SERP0359(fruA) SERP0998 SERP1290 SERP1790(lacE)
                 SERP1791(lacF) SERP1900 SERP1909 SERP1968 SERP2114 SERP2260
            SHA: SH0188 SH0190 SH0233(mtlA) SH0235(mtlF) SH0358(ptsG)
                 SH0521(ptsG) SH0671(scrA) SH0732(glvC) SH0741 SH0846(lacF)
                 SH0847(lacE) SH1198(ptaA) SH1484 SH2194(fruA) SH2538(treP)
            SSP: SSP0123 SSP0124 SSP0234 SSP0240 SSP0241 SSP0336 SSP0512
                 SSP0583 SSP0594 SSP0726 SSP0728 SSP1037 SSP1317 SSP2017
                 SSP2282
            LMO: lmo0021 lmo0022 lmo0027 lmo0096 lmo0299 lmo0301 lmo0357
                 lmo0358 lmo0374 lmo0398 lmo0399 lmo0426 lmo0427 lmo0503
                 lmo0507 lmo0542 lmo0543 lmo0631 lmo0633 lmo0738 lmo0783
                 lmo0784 lmo0874 lmo0875 lmo0914 lmo0916 lmo1017 lmo1035
                 lmo1095 lmo1255 lmo1719 lmo1720 lmo1972 lmo1973 lmo1997
                 lmo2002 lmo2097 lmo2098 lmo2136 lmo2137 lmo2259 lmo2335(fruA)
                 lmo2373 lmo2650 lmo2651 lmo2666 lmo2667 lmo2683 lmo2685
                 lmo2733 lmo2762 lmo2765 lmo2772 lmo2780 lmo2782 lmo2787(bvrB)
                 lmo2797 lmo2799
            LMF: LMOf2365_0024 LMOf2365_0025 LMOf2365_0030 LMOf2365_0113(manL)
                 LMOf2365_0320 LMOf2365_0322 LMOf2365_0390 LMOf2365_0442
                 LMOf2365_0443 LMOf2365_0532 LMOf2365_0536 LMOf2365_0571(srlB)
                 LMOf2365_0572(srlE) LMOf2365_0660 LMOf2365_0662 LMOf2365_0893
                 LMOf2365_0894 LMOf2365_0936 LMOf2365_0938 LMOf2365_1038
                 LMOf2365_1056 LMOf2365_1109 LMOf2365_1272(treB) LMOf2365_1681
                 LMOf2365_1743 LMOf2365_1744 LMOf2365_2020 LMOf2365_2025
                 LMOf2365_2129 LMOf2365_2130 LMOf2365_2292 LMOf2365_2305
                 LMOf2365_2344 LMOf2365_2622 LMOf2365_2623 LMOf2365_2646
                 LMOf2365_2647 LMOf2365_2663 LMOf2365_2665 LMOf2365_2720
                 LMOf2365_2752 LMOf2365_2755 LMOf2365_2762 LMOf2365_2771
                 LMOf2365_2773 LMOf2365_2785 LMOf2365_2787(mtlA)
            LIN: lin0020 lin0021 lin0026 lin0143 lin0327 lin0329 lin0376
                 lin0377 lin0393 lin0421 lin0422 lin0446 lin0503 lin0507
                 lin0546 lin0547 lin0776 lin0777 lin0872 lin0873 lin0914
                 lin0917 lin1016 lin1080 lin1223 lin1830 lin1831 lin2105
                 lin2110 lin2201 lin2202 lin2241 lin2242 lin2360 lin2429(fruA)
                 lin2457 lin2458 lin2472 lin2799 lin2800 lin2815 lin2816
                 lin2831 lin2833 lin2905 lin2908 lin2929 lin2931
            LWE: lwe0024 lwe0025 lwe0030 lwe0082 lwe0083 lwe0084 lwe0269
                 lwe0274 lwe0276 lwe0278 lwe0279 lwe0314 lwe0315 lwe0330
                 lwe0346 lwe0362 lwe0363 lwe0364 lwe0386 lwe0387 lwe0388
                 lwe0512(srlB) lwe0513(srlE) lwe0598 lwe0599 lwe0600
                 lwe0742(manX) lwe0743 lwe1001 lwe1070 lwe1274(treB) lwe1676
                 lwe1736 lwe1737 lwe2017 lwe2022 lwe2117 lwe2118 lwe2119
                 lwe2154 lwe2155 lwe2156 lwe2274 lwe2287(fruA) lwe2322 lwe2599
                 lwe2600 lwe2614 lwe2615 lwe2616 lwe2632 lwe2633 lwe2634
                 lwe2659 lwe2709 lwe2712 lwe2719 lwe2726 lwe2728
            LLA: L145238(yleD) L146642(yleE) L1762179(ptnAB) L185031(fruA)
                 L18872(ptcB) L19292(ptcA) L32907(mtlF) L37338(yedE)
                 L37906(yedF) L90678(ptbA)
            LLC: LACR_0027 LACR_0029 LACR_0465 LACR_0466 LACR_0481 LACR_0482
                 LACR_1033 LACR_1242 LACR_1736 LACR_1863 LACR_D01 LACR_D02
            LLM: llmg_0022(mtlA) llmg_0024(mtlF) llmg_0187(celB)
                 llmg_0437(ptcB) llmg_0438(ptcA) llmg_0440(ptcC)
                 llmg_0728(ptnC) llmg_0729(ptnAB) llmg_0866 llmg_1045(bglP)
                 llmg_1426 llmg_1568(fruA)
            SPY: SPy_0175 SPy_0176 SPy_0572 SPy_0631(agaV) SPy_0634(agaF)
                 SPy_0855 SPy_1057 SPy_1058 SPy_1323 SPy_1324 SPy_1710 SPy_1711
                 SPy_1738(manL) SPy_1815(scrA) SPy_1917(lacE) SPy_1918(lacF)
                 SPy_1986 SPy_2051 SPy_2052 SPy_2097
            SPZ: M5005_Spy_0148(ulaA) M5005_Spy_0149 M5005_Spy_0150
                 M5005_Spy_0475 M5005_Spy_0519(agaD) M5005_Spy_0520
                 M5005_Spy_0521(agaV) M5005_Spy_0662(fruA) M5005_Spy_0780
                 M5005_Spy_0781(ptsB) M5005_Spy_1081 M5005_Spy_1082
                 M5005_Spy_1083 M5005_Spy_1399 M5005_Spy_1400 M5005_Spy_1401
                 M5005_Spy_1479(manL) M5005_Spy_1480(manM) M5005_Spy_1481(manN)
                 M5005_Spy_1542(scrA) M5005_Spy_1633(lacE) M5005_Spy_1634(lacF)
                 M5005_Spy_1663 M5005_Spy_1664 M5005_Spy_1692 M5005_Spy_1693
                 M5005_Spy_1745 M5005_Spy_1746 M5005_Spy_1784
            SPM: spyM18_0174 spyM18_0175 spyM18_0641 spyM18_0696 spyM18_0698
                 spyM18_0914(fruA) spyM18_1034 spyM18_1035 spyM18_1333(ptcA)
                 spyM18_1334(ptcB) spyM18_1720 spyM18_1721 spyM18_1810
                 spyM18_1881 spyM18_1985 spyM18_1986 spyM18_2050(ptsG)
                 spyM18_2113 spyM18_2114 spyM18_2155
            SPG: SpyM3_0136 SpyM3_0137 SpyM3_0404 SpyM3_0445(agaV)
                 SpyM3_0447(agaF) SpyM3_0580(fruA) SpyM3_0741 SpyM3_0742
                 SpyM3_1002 SpyM3_1003 SpyM3_1487 SpyM3_1488 SpyM3_1511(manL)
                 SpyM3_1569(scrA) SpyM3_1654(lacE) SpyM3_1655(lacF) SpyM3_1708
                 SpyM3_1751 SpyM3_1752 SpyM3_1786
            SPS: SPs0139 SPs0140 SPs0298 SPs0356 SPs0379 SPs0380 SPs0855
                 SPs0856 SPs0942 SPs0943 SPs1274 SPs1409 SPs1410 SPs1451
                 SPs1652 SPs1653 SPs1708 SPs1749 SPs1750 SPs1783
            SPH: MGAS10270_Spy0150 MGAS10270_Spy0151 MGAS10270_Spy0152
                 MGAS10270_Spy0469 MGAS10270_Spy0514(agaD) MGAS10270_Spy0515
                 MGAS10270_Spy0516(agaV) MGAS10270_Spy0518
                 MGAS10270_Spy0721(fruA) MGAS10270_Spy0896
                 MGAS10270_Spy0897(ptsB) MGAS10270_Spy1137 MGAS10270_Spy1138
                 MGAS10270_Spy1139 MGAS10270_Spy1520 MGAS10270_Spy1521
                 MGAS10270_Spy1522 MGAS10270_Spy1546(manL)
                 MGAS10270_Spy1547(manM) MGAS10270_Spy1548(manN)
                 MGAS10270_Spy1609(scrA) MGAS10270_Spy1702(lacE)
                 MGAS10270_Spy1703(lacF) MGAS10270_Spy1731 MGAS10270_Spy1732
                 MGAS10270_Spy1759 MGAS10270_Spy1813 MGAS10270_Spy1814
                 MGAS10270_Spy1815 MGAS10270_Spy1851
            SPI: MGAS10750_Spy0154 MGAS10750_Spy0155 MGAS10750_Spy0156
                 MGAS10750_Spy0497 MGAS10750_Spy0538(agaD) MGAS10750_Spy0539
                 MGAS10750_Spy0540(agaV) MGAS10750_Spy0753(fruA)
                 MGAS10750_Spy0931 MGAS10750_Spy0932(ptsB) MGAS10750_Spy1174
                 MGAS10750_Spy1175 MGAS10750_Spy1176 MGAS10750_Spy1512
                 MGAS10750_Spy1513 MGAS10750_Spy1514 MGAS10750_Spy1538(manL)
                 MGAS10750_Spy1539(manM) MGAS10750_Spy1540(manN)
                 MGAS10750_Spy1601(scrA) MGAS10750_Spy1730(lacE)
                 MGAS10750_Spy1731(lacF) MGAS10750_Spy1757 MGAS10750_Spy1758
                 MGAS10750_Spy1784 MGAS10750_Spy1838 MGAS10750_Spy1839
                 MGAS10750_Spy1840 MGAS10750_Spy1876
            SPJ: MGAS2096_Spy0156 MGAS2096_Spy0157 MGAS2096_Spy0158
                 MGAS2096_Spy0488 MGAS2096_Spy0531(agaD) MGAS2096_Spy0532
                 MGAS2096_Spy0533(agaV) MGAS2096_Spy0535 MGAS2096_Spy0733(fruA)
                 MGAS2096_Spy0854 MGAS2096_Spy0855(ptsB) MGAS2096_Spy1082
                 MGAS2096_Spy1083 MGAS2096_Spy1084 MGAS2096_Spy1425
                 MGAS2096_Spy1426 MGAS2096_Spy1427 MGAS2096_Spy1428
                 MGAS2096_Spy1505(manL) MGAS2096_Spy1506 MGAS2096_Spy1507(manM)
                 MGAS2096_Spy1508(manN) MGAS2096_Spy1567(scrA)
                 MGAS2096_Spy1658(lacE) MGAS2096_Spy1659(lacF) MGAS2096_Spy1686
                 MGAS2096_Spy1687 MGAS2096_Spy1714 MGAS2096_Spy1778
                 MGAS2096_Spy1779 MGAS2096_Spy1780 MGAS2096_Spy1817
            SPK: MGAS9429_Spy0150 MGAS9429_Spy0151 MGAS9429_Spy0152
                 MGAS9429_Spy0467 MGAS9429_Spy0510(agaD) MGAS9429_Spy0511
                 MGAS9429_Spy0512(agaV) MGAS9429_Spy0514 MGAS9429_Spy0717(fruA)
                 MGAS9429_Spy0897 MGAS9429_Spy0898(ptsB) MGAS9429_Spy1124
                 MGAS9429_Spy1125 MGAS9429_Spy1126 MGAS9429_Spy1402
                 MGAS9429_Spy1403 MGAS9429_Spy1404 MGAS9429_Spy1481(manL)
                 MGAS9429_Spy1482(manM) MGAS9429_Spy1483(manN)
                 MGAS9429_Spy1546(scrA) MGAS9429_Spy1636(lacE)
                 MGAS9429_Spy1637(lacF) MGAS9429_Spy1664 MGAS9429_Spy1665
                 MGAS9429_Spy1693 MGAS9429_Spy1754 MGAS9429_Spy1755
                 MGAS9429_Spy1756 MGAS9429_Spy1795
            SPF: SpyM50142 SpyM50143 SpyM50144 SpyM50308(scrA) SpyM50364(manN)
                 SpyM50365(manM) SpyM50366(manL) SpyM50390 SpyM50783 SpyM50784
                 SpyM50986 SpyM51146(fruA) SpyM51343(agaW) SpyM51344(agaD)
                 SpyM51385 SpyM51608(lacE) SpyM51609(lacF) SpyM51662
            SPA: M6_Spy0194 M6_Spy0195 M6_Spy0196 M6_Spy0499 M6_Spy0540
                 M6_Spy0541 M6_Spy0542 M6_Spy0544 M6_Spy0681 M6_Spy0800
                 M6_Spy0801 M6_Spy0971 M6_Spy1050 M6_Spy1051 M6_Spy1052
                 M6_Spy1448 M6_Spy1449 M6_Spy1450 M6_Spy1473 M6_Spy1474
                 M6_Spy1475 M6_Spy1531 M6_Spy1642 M6_Spy1643 M6_Spy1671
                 M6_Spy1672 M6_Spy1698 M6_Spy1744 M6_Spy1745 M6_Spy1746
                 M6_Spy1783
            SPB: M28_Spy0146(ulaA) M28_Spy0147 M28_Spy0148 M28_Spy0456
                 M28_Spy0498(agaD) M28_Spy0499 M28_Spy0500(agaV) M28_Spy0502
                 M28_Spy0643(fruA) M28_Spy0757 M28_Spy0758(ptsB) M28_Spy1062
                 M28_Spy1063 M28_Spy1064 M28_Spy1442 M28_Spy1443 M28_Spy1444
                 M28_Spy1468(manL) M28_Spy1469(manM) M28_Spy1470(manN)
                 M28_Spy1529(scrA) M28_Spy1623(lacE) M28_Spy1624(lacF)
                 M28_Spy1651 M28_Spy1652 M28_Spy1678 M28_Spy1731 M28_Spy1732
                 M28_Spy1733 M28_Spy1768
            SPN: SP_0061 SP_0064 SP_0248 SP_0249 SP_0284 SP_0305 SP_0308
                 SP_0321 SP_0323 SP_0394 SP_0396 SP_0476 SP_0478 SP_0577
                 SP_0645 SP_0646 SP_0758 SP_0877 SP_1185 SP_1186 SP_1197
                 SP_1198 SP_1618 SP_1619 SP_1620 SP_1684 SP_1722 SP_1884
                 SP_2023 SP_2024 SP_2036 SP_2037 SP_2130 SP_2163 SP_2164
            SPR: spr0060(PTS-EIIB) spr0063(PTS-EII) spr0229(PTS-EIIA)
                 spr0230(PTS-EIIB) spr0261(manL) spr0278(PTS-EII)
                 spr0280(PTS-EII) spr0291(PTS-EII) spr0293(PTS-EII)
                 spr0356(mtlA) spr0358(mtlF) spr0423(PTS-EII) spr0425(PTS-EII)
                 spr0505(PTS-EII) spr0562(PTS-EII) spr0563 spr0668(ptsG)
                 spr0780(fruA) spr1070(lacE) spr1071(lacF) spr1080 spr1081
                 spr1528(PTS-EII) spr1566(scrA) spr1699(treP) spr1835(ptcB)
                 spr1836(ptcA) spr1847(PTS-EII) spr1848(PTS-EII) spr1939
                 spr1969(PTS-EII) spr1970(PTS-EII)
            SPD: SPD_0066 SPD_0069 SPD_0362(mtlA2) SPD_0426(lacF-1) SPD_0502
                 SPD_0559 SPD_0560 SPD_0661(exp5) SPD_0773 SPD_1496 SPD_1532
                 SPD_1664 SPD_1832
            SAG: SAG0192 SAG0197 SAG0282 SAG0328(celC) SAG0329 SAG0361(manL)
                 SAG0790 SAG1346 SAG1690 SAG1813 SAG1814 SAG1900 SAG1902
                 SAG1934 SAG1935 SAG1950 SAG1951 SAG1959
            SAN: gbs0189 gbs0192 gbs0272 gbs0316 gbs0317 gbs0348 gbs0810
                 gbs1330 gbs1331 gbs1416 gbs1734 gbs1854 gbs1855 gbs1888
                 gbs1890 gbs1921 gbs1922 gbs1938 gbs1939 gbs1946
            SAK: SAK_0257 SAK_0260 SAK_0354 SAK_0398 SAK_0399 SAK_0435
                 SAK_0524 SAK_0525 SAK_0528 SAK_0530 SAK_0915(bglF) SAK_1377
                 SAK_1702 SAK_1760 SAK_1761 SAK_1833 SAK_1834 SAK_1894 SAK_1895
                 SAK_1910 SAK_1911 SAK_1920
            SMU: SMU.100 SMU.103 SMU.114 SMU.115 SMU.1183(mtlA2)
                 SMU.1185(mtlA1) SMU.1491(lacE) SMU.1492(lacF) SMU.1598(ptcA)
                 SMU.1600(ptcB) SMU.1841(scrA) SMU.1877(ptnA) SMU.2038(pttB)
                 SMU.2047(ptsG) SMU.271(ptxB) SMU.272(ptxA) SMU.311 SMU.312
                 SMU.313 SMU.872 SMU.980(bglP)
            STC: str0189 str0190 str0191 str0192 str0333(manL) str0405 str0407
                 str0511 str0512 str0513 str0514 str1734(scrA) str1889 str1890
                 str1891
            STL: stu0189 stu0190 stu0191 stu0192 stu0333(manL) stu0401 stu0405
                 stu0406 stu0407 stu0511 stu0512 stu0513 stu0514 stu1734(scrA)
                 stu1888 stu1889 stu1890 stu1891
            STE: STER_1710
            SSA: SSA_0054 SSA_0057 SSA_0219 SSA_0220 SSA_0268(ptcB) SSA_0269
                 SSA_0270 SSA_0282 SSA_0283 SSA_0379 SSA_0456(scrA)
                 SSA_1082(fruA) SSA_1146(ptcA) SSA_1147 SSA_1148 SSA_1693(lacE)
                 SSA_1694(lacF) SSA_1752 SSA_1809(ptsG) SSA_1918 SSA_1919
                 SSA_2091(ptxA) SSA_2092(ptxB)
            SSU: SSU05_0450 SSU05_0453 SSU05_2075
            SSV: SSU98_0438 SSU98_0442 SSU98_2076 SSU98_2077
            SGO: SGO_0044 SGO_0045 SGO_0046 SGO_0047 SGO_0281 SGO_0505
                 SGO_1113(fruA) SGO_1513(lacE) SGO_1514(lacF) SGO_1522
                 SGO_1576(ptcC) SGO_1643 SGO_1644 SGO_1645 SGO_1653 SGO_1679
                 SGO_1680 SGO_1789 SGO_1857 SGO_1890 SGO_1891 SGO_1892 SGO_1893
            LPL: lp_0185(pts1BCA) lp_0230(pts2CB) lp_0232(pts2A)
                 lp_0247(pts3C) lp_0264(pts4ABC) lp_0265(pts5ABC)
                 lp_0286(pts6C) lp_0436(pts7C) lp_0439(pts8C) lp_0575(pts9AB)
                 lp_0576(pts9C) lp_0577(pts9D) lp_0586(pts10A) lp_0587(pts10B)
                 lp_0884(pts11A) lp_0886(pts11BC) lp_0905(pts12BCA) lp_0934
                 lp_1155(pts13C) lp_1164(pts14C) lp_1398(pts15A)
                 lp_1399(pts15B) lp_1400(pts15C) lp_2097(pts16ABC)
                 lp_2218(pts17A) lp_2531(pts18CBA) lp_2647(pts19A)
                 lp_2648(pts19D) lp_2649(pts19C) lp_2650(pts19B)
                 lp_2780(pts20A) lp_2781(pts20B) lp_2927(pts21A)
                 lp_2969(pts22CBA) lp_3008(pts23A) lp_3009(pts23B)
                 lp_3010(pts23C) lp_3133(pts24BCA) lp_3137(pts25B)
                 lp_3219(pts24BCA) lp_3229(pts27BCA) lp_3240(pts28ABC)
                 lp_3507(pts29C) lp_3513(pts30BCA) lp_3518(pts31BC)
                 lp_3519(pts31A) lp_3520(pts32A) lp_3522(pts32BC)
                 lp_3527(pts33BCA) lp_3541(pts34B) lp_3542 lp_3546(pts35C)
                 lp_3547(pts35B) lp_3548(pts35A) lp_3599(pts36A)
                 lp_3600(pts36B) lp_3601(pts36C) lp_3618(pts37A)
                 lp_3619(pts37BC) lp_3620(pts37C) lp_3652(pts38A)
                 lp_3653(pts38BC) lp_3654(pts38C)
            LJO: LJ0119 LJ0122 LJ0125 LJ0190 LJ0192 LJ0503 LJ0519 LJ0531
                 LJ0543 LJ0572 LJ0610 LJ0627 LJ0636 LJ0639 LJ0733 LJ0739 LJ0742
                 LJ0760 LJ0829 LJ1261 LJ1681 LJ1683 LJ1777 LJ1820
            LAC: LBA0146 LBA0227 LBA0401(scrA) LBA0452(manL) LBA0455(manM)
                 LBA0491(celB) LBA0606 LBA0609 LBA0618(ptcC) LBA0655(pthA)
                 LBA0725 LBA0876 LBA0877 LBA0989(lacE) LBA1012(treB)
                 LBA1369(celB) LBA1478 LBA1575 LBA1576 LBA1705 LBA1707
                 LBA1777(fruA) LBA1912
            LSA: LSA0060(nagE) LSA0353 LSA0449(manL) LSA0450(manM)
                 LSA0451(manN) LSA0471 LSA0759 LSA0760 LSA1050(fruA) LSA1198
                 LSA1200 LSA1457 LSA1533 LSA1690 LSA1792(scrA)
            LSL: LSL_0066(scrA) LSL_0086(manX) LSL_0087 LSL_0088
                 LSL_0165(fruA) LSL_0654(manX) LSL_0655 LSL_0656 LSL_0722
                 LSL_0914(celB) LSL_1143 LSL_1512(treB) LSL_1619 LSL_1620(mtlA)
                 LSL_1713 LSL_1714 LSL_1715 LSL_1716 LSL_1889 LSL_1890 LSL_1891
                 LSL_1949 LSL_1950 LSL_1951 LSL_1952(manX)
            LDB: Ldb0199 Ldb0542 Ldb0589 Ldb1771 Ldb1799 Ldb1800 Ldb1801
                 Ldb1823 Ldb2040 Ldb2065 Ldb2123
            LBU: LBUL_0173 LBUL_0525 LBUL_1673 LBUL_1887
            LCA: LSEI_0119 LSEI_0325 LSEI_0370 LSEI_0374 LSEI_0401 LSEI_0405
                 LSEI_0449 LSEI_0560 LSEI_0631 LSEI_0671 LSEI_0672 LSEI_0909
                 LSEI_1077 LSEI_1105 LSEI_1347 LSEI_1781 LSEI_1782 LSEI_2073
                 LSEI_2101 LSEI_2192 LSEI_2247 LSEI_2596 LSEI_2664 LSEI_2667
                 LSEI_2700 LSEI_2705 LSEI_2707 LSEI_2721 LSEI_2722 LSEI_2723
                 LSEI_2736 LSEI_2738 LSEI_2741 LSEI_2776 LSEI_2817 LSEI_2818
                 LSEI_2829 LSEI_2886 LSEI_2888 LSEI_A05
            LGA: LGAS_0117 LGAS_0120 LGAS_0125 LGAS_0192 LGAS_0194 LGAS_0342
                 LGAS_0398 LGAS_0495 LGAS_0496 LGAS_0501 LGAS_0514 LGAS_0517
                 LGAS_0535
            PPE: PEPE_0077 PEPE_0174 PEPE_0281 PEPE_0282 PEPE_0578 PEPE_1513
                 PEPE_1759 PEPE_1761
            EFA: EF0019 EF0020 EF0028 EF0270 EF0406 EF0408 EF0411 EF0412(mltF)
                 EF0457 EF0554 EF0555 EF0694 EF0695 EF0717 EF0815 EF0834 EF0958
                 EF1012 EF1017 EF1018 EF1126 EF1128(sgaB) EF1159 EF1516 EF1601
                 EF1769 EF1801 EF1804 EF1836 EF1837 EF2213 EF2267 EF2271 EF2435
                 EF2438 EF2598 EF2603 EF2965 EF2979 EF2980 EF3031 EF3045 EF3046
                 EF3136 EF3137 EF3210 EF3211 EF3305 EF3306 EF3307 EFA0067
            OOE: OEOE_0222 OEOE_0223 OEOE_0233 OEOE_0234 OEOE_0236 OEOE_0296
                 OEOE_0338 OEOE_0339 OEOE_0379 OEOE_0382 OEOE_0464 OEOE_1341
                 OEOE_1342 OEOE_1482 OEOE_1483
            STH: STH1249(agaB) STH1251(agaF) STH1276 STH1277 STH1939 STH1940
                 STH1968 STH2309 STH2448 STH350 STH795 STH796 STH951 STH953
            CAC: CAC0154(mtlA) CAC0156(mltF) CAC0233 CAC0234 CAC0383
                 CAC0384(licB) CAC0423 CAC0532 CAC0570 CAC1353 CAC1354 CAC1407
                 CAC1457 CAC1458 CAC2957 CAC2958 CAC2964(lacE) CAC2965(lacF)
                 CAC2995 CAC3425(glvC) CAC3427 CA_P0066(ptnA)
            CPE: CPE0075 CPE0076 CPE0077 CPE0196(ptiB) CPE0320 CPE0321 CPE0419
                 CPE0521 CPE0522 CPE0561 CPE0584 CPE0821 CPE1465 CPE1466
                 CPE1534 CPE2157 CPE2229 CPE2577 CPE2629 CPE2632
            CPF: CPF_0070 CPF_0071(nagE) CPF_0401 CPF_0404 CPF_0422 CPF_0501
                 CPF_0502 CPF_0541(treB) CPF_0564(fruA) CPF_0646 CPF_0818
                 CPF_1070 CPF_1716 CPF_1717 CPF_1785 CPF_2412(ptsG) CPF_2493
                 CPF_2902 CPF_2965 CPF_2968
            CPR: CPR_0092 CPR_0093(nagE) CPR_0397 CPR_0400 CPR_0418 CPR_0489
                 CPR_0490 CPR_0525 CPR_0550 CPR_0935(nagE) CPR_1513
                 CPR_2124(ptsG) CPR_2199 CPR_2581 CPR_2600 CPR_2602
            CTC: CTC00278 CTC01841
            CNO: NT01CX_0332 NT01CX_1443 NT01CX_1452 NT01CX_1858
            CDF: CD0284 CD0388(bglF) CD0765(srlE) CD0766(srlE') CD0767(srlB)
                 CD1336(malX) CD2326(gatB) CD2327(gatA) CD2332(mtlF)
                 CD2334(mtlA) CD2417(srlE) CD2512 CD2555 CD2666(crr)
                 CD2667(ptsG) CD2880(celC) CD2884(licB) CD3027(crr)
                 CD3030(malX) CD3061(glvC) CD3086(hrsA) CD3116(bglF) CD3648
            CBO: CBO0271 CBO0279(crr) CBO0655 CBO0881(bglC) CBO1327(crr)
                 CBO1987(treB) CBO2839(nagE) CBO3356(celC) CBO3357(celA)
                 CBO3414(gutB) CBO3415(gutE)
            CBA: CLB_0693 CLB_0920 CLB_1354(ptsG) CLB_1372 CLB_1927(treP)
                 CLB_1931 CLB_2782(nagE) CLB_3471 CLB_3473
            CBH: CLC_0708 CLC_0934 CLC_1364(ptsG) CLC_1382 CLC_1933(treP)
                 CLC_1937 CLC_2715(nagE) CLC_3359 CLC_3361
            CBF: CLI_0731 CLI_0962 CLI_1421(ptsG) CLI_1444 CLI_2053(treP)
                 CLI_2058 CLI_2891(nagE) CLI_2903 CLI_3597 CLI_3599
            CBE: Cbei_0242 Cbei_0337 Cbei_0527 Cbei_0711 Cbei_0751 Cbei_0950
                 Cbei_1478 Cbei_1840 Cbei_2665 Cbei_2707 Cbei_2908 Cbei_3813
                 Cbei_3873 Cbei_4535 Cbei_4634 Cbei_4638 Cbei_4683 Cbei_4913
            CKL: CKL_3586
            AMT: Amet_4187 Amet_4195
            TTE: TTE0181(ptsN) TTE0182 TTE0192(manX) TTE0193 TTE0305(sgaB)
                 TTE0335(celA) TTE0336(celC) TTE0339(mtlA) TTE0341(ptsN2)
                 TTE0468(ptsG) TTE0469(nagE) TTE0600(celA2) TTE0602(celC2)
                 TTE2585(fruA) TTE2586(ptsN3)
            MTA: Moth_0013
            MGE: MG_062(fruA) MG_069(ptsG)
            MPN: MPN078(fruA) MPN207(ptsG) MPN494(yjfU) MPN495 MPN651(mtlA)
                 MPN653(mtlF)
            MPU: MYPU_0170(ptsG) MYPU_1290(fruA) MYPU_1980(sgaT) MYPU_3610
                 MYPU_3640 MYPU_5950(sgaB) MYPU_5960(sgaA) MYPU_7400(licA)
                 MYPU_7510(mtlA) MYPU_7520(mtlA)
            MPE: MYPE1340(ptsG) MYPE4490 MYPE5910 MYPE7190 MYPE7200(sgaB)
                 MYPE7670(fruA) MYPE7760(fruA)
            MGA: MGA_0508(pts) MGA_0855(ptsG)
            MMY: MSC_0019(EIIA-mtl) MSC_0021(EIIBC-mtl) MSC_0054(ptsG)
                 MSC_0130(nagE) MSC_0161(ptsG) MSC_0250(pts) MSC_0274(crr)
                 MSC_0394(pts) MSC_0395 MSC_0646(pts) MSC_0749(pts)
                 MSC_0831(frvB) MSC_0842(frvA) MSC_0846(frvB) MSC_0860(ptsG)
                 MSC_0873(ptsG)
            MMO: MMOB0620(treB) MMOB0650(bglP) MMOB4640(scrA) MMOB6060(fruA)
            MHY: mhp386(sgaA) mhp387(sgaB) mhp490 mhp567(mtlF) mhp569(mtlA)
                 mhp572 mhp573 mhp590(nagE) mhp629
            MHJ: MHJ_0036(licA) MHJ_0370(sgaA) MHJ_0371 MHJ_0489(fruA)
                 MHJ_0552(mtlF) MHJ_0554(mtlA) MHJ_0556 MHJ_0557 MHJ_0558
                 MHJ_0575 MHJ_0612
            MHP: MHP7448_0040(licA) MHP7448_0374(sgaA) MHP7448_0375
                 MHP7448_0492(fruA) MHP7448_0548(mtlF) MHP7448_0550(mtlA)
                 MHP7448_0552 MHP7448_0553 MHP7448_0554 MHP7448_0574
                 MHP7448_0610
            MSY: MS53_0027 MS53_0028(sgaA) MS53_0147(ptsG) MS53_0282(licA)
                 MS53_0339 MS53_0681(sgaA-1) MS53_0682
            MCP: MCAP_0028 MCAP_0030 MCAP_0094(ptsG) MCAP_0129 MCAP_0155
                 MCAP_0234(crr) MCAP_0458 MCAP_0459 MCAP_0590 MCAP_0591
                 MCAP_0618 MCAP_0783 MCAP_0787 MCAP_0844 MCAP_0853(fruA)
            MFL: Mfl181 Mfl187 Mfl214 Mfl426 Mfl500 Mfl516 Mfl527
            MSM: MSMEG_0085 MSMEG_2116
            MMC: Mmcs_0080
            CGL: NCgl1305(cgl1360) NCgl1861(cgl1936) NCgl2553(cgl2642)
            CGB: cg1537(ptsG) cg2120(ptsF) cg2925(ptsS)
            CEF: CE1458(ptsM) CE1829
            CDI: DIP1151(ptsG)
            CJK: jk0206
            RHA: RHA1_ro01550 RHA1_ro01551 RHA1_ro01552
            SCO: SCO0434(malX) SCO1390(SC1A8A.10) SCO2906(SCE19A.06)
                 SCO2907(SCE19A.07) SCO3196(SCE22.13c)
            SMA: SAV3688(fruA) SAV3925(scrA) SAV5167(ptsC1) SAV5168(ptsC2)
                 SAV6975(ptsA)
            LXX: Lxx00810 Lxx00820(EIIBC-Mtl) Lxx00850 Lxx04680 Lxx06600
            CMI: CMM_1504(fruA) CMM_1505(fruB) CMM_1754 CMM_2590(mtlF)
                 CMM_2591(mtlA) CMM_2594
            ART: Arth_3514
            AAU: AAur_0294 AAur_3859(mtlA)
            PAC: PPA0021 PPA0022 PPA0023 PPA0142 PPA0293 PPA0294 PPA0355
                 PPA0356 PPA0365 PPA0366 PPA0675 PPA0679 PPA0919 PPA1109
                 PPA1142 PPA1147 PPA1149 PPA1484 PPA1485 PPA1486 PPA2232
                 PPA2233
            TFU: Tfu_2489
            SEN: SACE_2061 SACE_2062 SACE_2274(fruA) SACE_6246
            BLO: BL1632(ptsG)
            BAD: BAD_0366(ptsG)
            RXY: Rxyl_1732
            FNU: FN0631 FN0632 FN0915 FN1441 FN1491 FN1547 FN1926
            RBA: RB5795(ptsN) RB8584(fruA)
            CTR: CT290(ptsN_1) CT291(ptsN_2)
            CTA: CTA_0312(ptsN_1) CTA_0313(ptsN_2)
            CMU: TC0563 TC0564
            CPN: CPn0060(ptsN_1) CPn0061(ptsN_2)
            CPA: CP0714 CP0715
            CPJ: CPj0060(ptsN_1) CPj0061(ptsN_2)
            CPT: CpB0061(fruA) CpB0062(ptsN)
            CCA: CCA00348(ptsN_1) CCA00349
            CAB: CAB339 CAB340
            CFE: CF0657(ptsN1) CF0658(ptsN2)
            PCU: pc0266(ptsN)
            BBU: BB0116(malX) BB0408(fruA-1) BB0559(crr) BB0629(fruA-2)
                 BB0645(ptsG) BBB05(celC) BBB06(celA) BBB29(malX)
            BGA: BG0117(malX) BG0410(fruA-1) BG0569(crr) BG0650(fruA-2)
                 BG0668(ptsG) BGB06(celA)
            BAF: BAPKO_0117(malX-1) BAPKO_0588(crr) BAPKO_0689(ptsG)
                 BAPKO_5004(celC) BAPKO_5005(celA)
            TPA: TP0085 TP0755
            TDE: TDE0062 TDE1079
            LIL: LA0632(ptsN)
            LIC: LIC12955(ptsN)
            LBJ: LBJ_2334(ptsN)
            LBL: LBL_0774(ptsN)
            SRU: SRU_0838
            CTE: CT0235
            CCH: Cag_1468(ptsN)
            CPH: Cpha266_0363
            PLT: Plut_1787(ptsN)
            DRA: DR_B0073 DR_B0075(fruB)
            DGE: Dgeo_2620
            HMA: pNG7387(ptsC) pNG7388(ptsA) pNG7392(ptsB)
STRUCTURES  PDB: 1A3A  1A6J  1AX3  1BLE  1E2A  1E2B  1F3Z  1GGR  1GLA  1GLB  
                 1GLC  1GLD  1GLE  1GPR  1H9C  1IBA  1IIB  1NRZ  1O2F  1O53  
                 1PDO  1TVM  1VRC  1WCR  2A0J  2E2A  2F3G  2FEW  2GPR  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.69
            ExPASy - ENZYME nomenclature database: 2.7.1.69
            ExplorEnz - The Enzyme Database: 2.7.1.69
            ERGO genome analysis and discovery system: 2.7.1.69
            BRENDA, the Enzyme Database: 2.7.1.69
            CAS: 37278-09-4
///
ENTRY       EC 2.7.1.70       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Deleted entry: protamine kinase. Now included in EC 2.7.11.1,
            non-specific serine/threonine protein kinase (EC 2.7.1.70 created
            1972, deleted 2004)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.70
            ExPASy - ENZYME nomenclature database: 2.7.1.70
            ExplorEnz - The Enzyme Database: 2.7.1.70
            ERGO genome analysis and discovery system: 2.7.1.70
            BRENDA, the Enzyme Database: 2.7.1.70
///
ENTRY       EC 2.7.1.71                 Enzyme
NAME        shikimate kinase;
            shikimate kinase (phosphorylating);
            shikimate kinase II
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:shikimate 3-phosphotransferase
REACTION    ATP + shikimate = ADP + shikimate 3-phosphate [RN:R02412]
ALL_REAC    R02412
SUBSTRATE   ATP [CPD:C00002];
            shikimate [CPD:C00493]
PRODUCT     ADP [CPD:C00008];
            shikimate 3-phosphate [CPD:C03175]
REFERENCE   1  [PMID:4866525]
  AUTHORS   Morell H, Sprinson DB.
  TITLE     Shikimate kinase isoenzymes in Salmonella typhimurium.
  JOURNAL   J. Biol. Chem. 243 (1968) 676-7.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K00891  shikimate kinase
GENES       OSA: 4330732 4340547
            CME: CMT093C
            SCE: YDR127W(ARO1)
            AGO: AGOS_AGR066W
            CAL: CaO19_4704(CaO19.4704)
            CGR: CAGL0M11484g
            SPO: SPAC1834.02(aro1)
            AFM: AFUA_1G13740
            AOR: AO090012000502
            CNE: CNB01990
            UMA: UM03607.1
            ECO: b0388(aroL) b3390(aroK)
            ECJ: JW0379(aroL) JW5947(aroK)
            ECE: Z0484(aroL) Z4743(aroK)
            ECS: ECs0438 ECs4232
            ECC: c0495(aroL) c4160(aroK)
            ECI: UTI89_C0407(aroL) UTI89_C3888(aroK)
            ECP: ECP_0447 ECP_3476
            ECV: APECO1_1620(aroL) APECO1_3073(aroK)
            ECW: EcE24377A_0415(aroL) EcE24377A_3860(aroK)
            ECX: EcHS_A0456 EcHS_A3586
            STY: STY0421(aroL) STY4309(aroK)
            STT: t2476(aroL) t4019(aroK)
            SPT: SPA2335(aroL) SPA3352(aroK)
            SEC: SC0429(aroL) SC3419(aroK)
            STM: STM0388(aroL) STM3487(aroK)
            YPE: YPO0151(aroK) YPO3215(aroL)
            YPK: y0972(aroL) y3933(aroK)
            YPM: YP_0153(aroK1) YP_0720(aroK2)
            YPA: YPA_2707 YPA_3318
            YPN: YPN_0878 YPN_3914
            YPP: YPDSF_0078 YPDSF_2844
            YPS: YPTB0911(aroL) YPTB3750(aroK)
            YPI: YpsIP31758_3143(aroL) YpsIP31758_3966(aroK)
            SFL: SF0324(aroL)
            SFX: S0332(aroL) S4354(aroK)
            SFV: SFV_0353(aroL) SFV_3395(aroK)
            SSN: SSON_0364(aroL) SSON_3521(aroK)
            SBO: SBO_0283(aroL) SBO_3377(aroK)
            SDY: SDY_0355(aroL) SDY_3689(aroK)
            ECA: ECA1103(aroL) ECA4093(aroK)
            PLU: plu0090(aroK) plu1245(aroL)
            BUC: BU539(aroK)
            BAS: BUsg520(aroK)
            BAB: bbp481(aroK)
            BCC: BCc_353(aroK)
            WBR: WGLp578(aroK)
            SGL: SG0634 SG2309
            ENT: Ent638_0859 Ent638_3803
            KPN: KPN_03761(aroK)
            SPE: Spro_1018 Spro_4605
            BFL: Bfl572(aroK)
            BPN: BPEN_592(aroK)
            HIN: HI0207(aroK)
            HIT: NTHI0305(aroK)
            HDU: HD0423(aroK)
            HSO: HS_1113(aroK)
            PMU: PM1224(aroK)
            MSU: MS1969(aroK)
            APL: APL_0194(aroK)
            ASU: Asuc_0264
            XFA: XF1335
            XFT: PD0582(aroK)
            XCC: XCC2841(aroK)
            XCB: XC_1269
            XCV: XCV3160(aroK)
            XAC: XAC3010(aroK)
            XOO: XOO1244(aroK)
            XOM: XOO_1144(XOO1144)
            VCH: VC2629
            VCO: VC0395_A2206(aroK)
            VVU: VV1_1382
            VVY: VV2989
            VPA: VP2745
            VFI: VF2292
            PPR: PBPRA0280
            PAE: PA5039(aroK)
            PAU: PA14_66610(aroK)
            PPU: PP_5079(aroK)
            PPF: Pput_4952
            PST: PSPTO_5127(aroK)
            PSB: Psyr_0408(aroK)
            PSP: PSPPH_0395(aroK)
            PFL: PFL_0450(aroK)
            PFO: Pfl_0410
            PEN: PSEEN0334(aroK)
            PMY: Pmen_0547
            PAR: Psyc_1878(aroK)
            PCR: Pcryo_2168
            PRW: PsycPRwf_0400
            ACI: ACIAD3354(aroK)
            SON: SO_0286(aroK)
            SDN: Sden_0261
            SFR: Sfri_0375
            SAZ: Sama_3368
            SBL: Sbal_4113
            SBM: Shew185_4084
            SLO: Shew_0213
            SPC: Sputcn32_3706
            SSE: Ssed_4265
            SPL: Spea_0238
            SHE: Shewmr4_3698
            SHM: Shewmr7_0247
            SHN: Shewana3_3894
            SHW: Sputw3181_3847
            ILO: IL2472(aroK)
            CPS: CPS_0472(aroK)
            PHA: PSHAa2715(aroK)
            PAT: Patl_0666
            SDE: Sde_2686
            PIN: Ping_0163
            CBU: CBU_1892(aroK)
            CBD: COXBU7E912_0124(aroK)
            LPN: lpg0932
            LPF: lpl0963(aroK)
            LPP: lpp0994(aroK)
            MCA: MCA0330(aroK)
            FTU: FTT1155c(aroK)
            FTF: FTF1155c(aroK)
            FTW: FTW_1194(aroK)
            FTL: FTL_0801
            FTH: FTH_0794(aroK)
            FTA: FTA_0846(aroK)
            FTN: FTN_1136(aroK)
            TCX: Tcr_2137
            NOC: Noc_0252
            AEH: Mlg_0912 Mlg_2761
            HHA: Hhal_2258
            HCH: HCH_05968
            CSA: Csal_0613
            ABO: ABO_2232(aroK)
            MMW: Mmwyl1_4117
            AHA: AHA_0287(aroK-1) AHA_3189(aroK-2)
            DNO: DNO_0611(aroK)
            BCI: BCI_0024(aroK)
            RMA: Rmag_0583
            VOK: COSY_0538(aroK)
            NME: NMB1813
            NMA: NMA0648(aroK)
            NMC: NMC0407(aroK)
            NGO: NGO0093(aroK)
            CVI: CV_0828(aroK)
            RSO: RSc2970(aroK)
            REU: Reut_A3130
            REH: H16_A3435(aroL)
            RME: Rmet_3267 Rmet_4010
            BMA: BMA2747(aroK)
            BMV: BMASAVP1_A3206(aroK)
            BML: BMA10299_A1757(aroK)
            BMN: BMA10247_2797(aroK)
            BXE: Bxe_A0359 Bxe_A1421 Bxe_C0893 Bxe_C0924
            BVI: Bcep1808_0374
            BUR: Bcep18194_A3489
            BCN: Bcen_2715
            BCH: Bcen2424_0392
            BAM: Bamb_0311
            BPS: BPSL3169(aroK)
            BPM: BURPS1710b_3439(aroK) BURPS1710b_3729(aroK)
            BPL: BURPS1106A_3758(aroK)
            BPD: BURPS668_3700(aroK)
            BTE: BTH_I3024(aroK)
            PNU: Pnuc_0089
            BPE: BP3656(aroK)
            BPA: BPP0071(aroK)
            BBR: BB0071(aroK)
            RFR: Rfer_0219 Rfer_2925
            POL: Bpro_0786 Bpro_1627
            PNA: Pnap_0678
            AAV: Aave_1002
            AJS: Ajs_0150
            VEI: Veis_0013
            MPT: Mpe_A3108
            HAR: HEAR3120(aroB-aroK)
            MMS: mma_3363
            NEU: NE1980(aroK)
            NET: Neut_0382
            NMU: Nmul_A0652
            EBA: ebA2258(aroK) ebA2762(boxR) ebA5278(bzdR)
            AZO: azo3645(aroK)
            DAR: Daro_0215
            TBD: Tbd_0207
            MFA: Mfla_2456
            HPY: HP0157
            HPJ: jhp0145(aroK)
            HPA: HPAG1_0155
            HHE: HH0628(aroK)
            HAC: Hac_0340(aroK)
            WSU: WS1497(aroK)
            TDN: Tmden_0495
            CJE: Cj0387(aroK)
            CJR: CJE0436(aroK)
            CJJ: CJJ81176_0410(aroK)
            CJU: C8J_0362(aroK)
            CJD: JJD26997_1571(aroK)
            CFF: CFF8240_1340(aroK)
            CCV: CCV52592_1187(aroK)
            CHA: CHAB381_0052(aroK)
            CCO: CCC13826_0776(aroK)
            ABU: Abu_0383(aroK)
            NIS: NIS_0677
            SUN: SUN_0164
            GSU: GSU2026(aroK)
            GME: Gmet_0977
            GUR: Gura_1819
            PCA: Pcar_1776 Pcar_2174
            PPD: Ppro_2361
            DVU: DVU0892(aroK-1) DVU2521(aroK-2)
            DVL: Dvul_2092
            DDE: Dde_2609 Dde_2728
            LIP: LI0659
            DPS: DP0821 DP2499
            ADE: Adeh_0187
            AFW: Anae109_0207
            MXA: MXAN_3524
            SAT: SYN_01935
            SFU: Sfum_1639
            PUB: SAR11_0453(aroK)
            MLO: mll3573
            MES: Meso_3064
            PLA: Plav_1718
            SME: SMc00695(aroK)
            SMD: Smed_2565
            ATU: Atu3626(aroK)
            ATC: AGR_L_2400
            RET: RHE_CH03826(aroK)
            RLE: RL4353(aroK)
            BME: BMEI0042
            BMF: BAB1_2030(aroK)
            BMS: BR2029(aroK)
            BMB: BruAb1_2004(aroK)
            BOV: BOV_1951(aroK)
            OAN: Oant_0909
            BJA: bll0188
            BRA: BRADO0609 BRADO6792(aroK)
            BBT: BBta_0746(aroK) BBta_7573(aroK)
            RPA: RPA0504(aroK) RPA4787
            RPB: RPB_0535 RPB_4657
            RPC: RPC_0098 RPC_0532
            RPD: RPD_0294 RPD_0877
            RPE: RPE_0143 RPE_0475
            NWI: Nwi_0395
            NHA: Nham_0490
            BHE: BH16360(aroK)
            BQU: BQ13270(aroK)
            BBK: BARBAKC583_0038(aroK)
            XAU: Xaut_1633
            CCR: CC_3008
            SIL: SPO1634(aroK)
            SIT: TM1040_1431
            RSP: RSP_2817(aroK)
            RSH: Rsph17029_1479
            RSQ: Rsph17025_1529
            JAN: Jann_2486
            RDE: RD1_3088(aroK)
            PDE: Pden_1282
            MMR: Mmar10_2273
            HNE: HNE_0081(aroK)
            ZMO: ZMO0594(aroK)
            NAR: Saro_1900
            SAL: Sala_1799
            SWI: Swit_0008
            ELI: ELI_04970
            GOX: GOX1788
            GBE: GbCGDNIH1_0616
            RRU: Rru_A3740
            MAG: amb3926
            MGM: Mmc1_0090
            ABA: Acid345_2488
            SUS: Acid_0777
            BSU: BG10457(aroK)
            BHA: BH0500(aroI)
            BAN: BA4457(aroK)
            BAR: GBAA4457(aroK)
            BAA: BA_4909
            BAT: BAS4137
            BCE: BC4232
            BCA: BCE_4313(aroK)
            BCZ: BCZK3987(aroK)
            BCY: Bcer98_2922
            BTK: BT9727_3977(aroK)
            BTL: BALH_3834(aroK)
            BLI: BL01707(aroK)
            BLD: BLi00371(aroK)
            BCL: ABC2481(aroK)
            BAY: RBAM_003410
            BPU: BPUM_0290
            OIH: OB2455
            GKA: GK2056(aroI)
            SAU: SA1368
            SAV: SAV1538
            SAM: MW1490
            SAR: SAR1615
            SAS: SAS1476
            SAC: SACOL1596(aroK)
            SAB: SAB1410c
            SAA: SAUSA300_1499(aroK)
            SAO: SAOUHSC_01635
            SAJ: SaurJH9_1596
            SAH: SaurJH1_1629
            SEP: SE1224
            SER: SERP1103(aroK)
            SHA: SH1378
            SSP: SSP1217
            LMO: lmo1749
            LMF: LMOf2365_1774(aroK)
            LIN: lin1861
            LWE: lwe1766(aroK)
            LLA: L0056(aroK)
            LLC: LACR_1906
            LLM: llmg_1925(aroK)
            SPY: SPy_1351(aroK)
            SPZ: M5005_Spy_1100(aroK)
            SPM: spyM18_1363(aroK)
            SPG: SpyM3_1026(aroK)
            SPS: SPs0834
            SPH: MGAS10270_Spy1157(aroK)
            SPI: MGAS10750_Spy1199(aroK)
            SPJ: MGAS2096_Spy1162(aroK)
            SPK: MGAS9429_Spy1144(aroK)
            SPF: SpyM50759(aroK)
            SPA: M6_Spy1072
            SPB: M28_Spy1092(aroK)
            SPN: SP_1370
            SPR: spr1228(aroK)
            SPD: SPD_1204(aroK)
            SAG: SAG0631(aroK)
            SAN: gbs0611(aroK)
            SAK: SAK_0716(aroK)
            SMU: SMU.785(aroK)
            STC: str0646(aroK)
            STL: stu0646(aroK)
            SSA: SSA_1463(aroK)
            SGO: SGO_1367(aroK)
            LPL: lp_2033(aroI)
            LSA: LSA0895(aroK)
            EFA: EF1567(aroK)
            OOE: OEOE_0153
            STH: STH1949
            CAC: CAC0898(aroK)
            CPE: CPE0701(aroK)
            CPF: CPF_0694(aroK)
            CPR: CPR_0694(aroK)
            CTC: CTC01594
            CNO: NT01CX_0620(aroK)
            CTH: Cthe_0731
            CDF: CD1838(aroK)
            CBO: CBO1899(aroK)
            CBA: CLB_1836(aroK)
            CBH: CLC_1843(aroK)
            CBF: CLI_1963(aroK)
            CBE: Cbei_4571
            CKL: CKL_0791(aroK)
            AMT: Amet_0651
            CHY: CHY_0629(aroKB)
            DSY: DSY2391
            DRM: Dred_0781 Dred_1020
            SWO: Swol_0528
            CSC: Csac_2240
            TTE: TTE1275(aroK)
            MTA: Moth_1556
            MTU: Rv2539c(aroK)
            MTC: MT2614(aroK)
            MBO: Mb2568c(aroK)
            MBB: BCG_2561c(aroK)
            MLE: ML0517(aroK)
            MPA: MAP1092(aroK)
            MAV: MAV_2468(aroK) MAV_3416(aroK)
            MSM: MSMEG_0453(aroK) MSMEG_3031
            MVA: Mvan_2646
            MGI: Mflv_3757
            MMC: Mmcs_2353
            MKM: Mkms_2400
            MJL: Mjls_2394
            CGL: NCgl1560(aroK)
            CGB: cg1828(aroK)
            CEF: CE1741(aroK)
            CDI: DIP1344(aroK)
            CJK: jk1032(aroK)
            RHA: RHA1_ro07141(aroK)
            SCO: SCO1495(aroK)
            SMA: SAV6855(aroK)
            TWH: TWT371(aroK)
            TWS: TW398(aroK)
            LXX: Lxx10960(aroK)
            ART: Arth_2273
            AAU: AAur_0530(aroK) AAur_2276(aroK) AAur_2721(aroK)
            PAC: PPA1183
            NCA: Noca_2413
            TFU: Tfu_1091
            FRA: Francci3_3208
            FAL: FRAAL3601 FRAAL5246(aroK)
            ACE: Acel_0938 Acel_1308
            KRA: Krad_3014
            SEN: SACE_2066(aroK)
            STP: Strop_1846
            BLO: BL0877(aroB)
            RXY: Rxyl_1460
            FNU: FN0822
            RBA: RB3471
            CTR: CT367(aroL)
            CTA: CTA_0399(aroL)
            CMU: TC0646
            CPN: CPn1038(aroL)
            CPA: CP0814
            CPJ: CPj1038(aroL)
            CPT: CpB1078
            CCA: CCA00724(aroK)
            CAB: CAB691(aroM)
            CFE: CF0292(aroK)
            PCU: pc0883(aroL)
            TDE: TDE2447(aroK)
            LIL: LB123(aroK)
            LIC: LIC20099(aroK)
            LBJ: LBJ_4105(aroK)
            LBL: LBL_4121(aroK)
            SYN: sll1669(aroK)
            SYW: SYNW2202(aroK)
            SYC: syc0646_d(aroK)
            SYF: Synpcc7942_0894
            SYD: Syncc9605_2345
            SYE: Syncc9902_0346
            SYG: sync_2557(aroK)
            SYR: SynRCC307_0291(aroK)
            SYX: SynWH7803_2213(aroK)
            CYA: CYA_2646(aroK)
            CYB: CYB_1737(aroK)
            TEL: tlr0882(aroK)
            GVI: glr2710(aroK)
            ANA: alr1244
            AVA: Ava_0553
            PMA: Pro0128(aroK)
            PMM: PMM0107(aroK)
            PMT: PMT0163(aroK)
            PMN: PMN2A_1476
            PMI: PMT9312_0111
            PMB: A9601_01241(aroK)
            PMC: P9515_01201(aroK)
            PMF: P9303_02051(aroK)
            PMG: P9301_01231(aroK)
            PMH: P9215_01241
            PME: NATL1_01791(aroK)
            TER: Tery_1506
            BTH: BT_3393
            BFR: BF0235
            BFS: BF0192
            PGI: PG1593(aroK)
            SRU: SRU_0663(aroK)
            CHU: CHU_3226(aroK)
            GFO: GFO_2407(aroK)
            FJO: Fjoh_0053
            FPS: FP1443(aroK)
            CTE: CT1405(aroK)
            CCH: Cag_1220
            CPH: Cpha266_0837
            PVI: Cvib_1225
            PLT: Plut_1406
            DET: DET0464(aroK)
            DEH: cbdb_A428(aroK)
            DEB: DehaBAV1_0441
            RRS: RoseRS_4543
            RCA: Rcas_0091
            DRA: DR_0776
            DGE: Dgeo_1731
            TTH: TTC1019
            TTJ: TTHA1385
            AAE: aq_2177(aroK)
            TMA: TM0348
            TPT: Tpet_0572
            MJA: MJ1440
            MMP: MMP0320
            MAC: MA1378(aroL) MA3237(aroK)
            MBA: Mbar_A3127 Mbar_A3183
            MMA: MM_0084 MM_2362
            MBU: Mbur_0827 Mbur_0875
            MHU: Mhun_1030 Mhun_1850
            MEM: Memar_2255
            MBN: Mboo_1256
            MTH: MTH805
            MST: Msp_0104(aroK)
            MSI: Msm_0835
            MKA: MK1610
            AFU: AF0520
            HAL: VNG1245C
            HMA: rrnAC0753(aroK)
            HWA: HQ2762A(aroK)
            NPH: NP3982A(aroK)
            TAC: Ta0283
            TVO: TVN1318
            PTO: PTO0601
            PAB: PAB0301(thrB-2)
            PFU: PF1694
            TKO: TK0264
            RCI: RCIX1316(aroK)
            APE: APE_0572
            IHO: Igni_0540
            SSO: SSO0308
            STO: ST2276
            SAI: Saci_0187(aroK)
            MSE: Msed_1872
            PAI: PAE1967
            PIS: Pisl_1792
            PCL: Pcal_0915
            PAS: Pars_2042
STRUCTURES  PDB: 1E6C  1KAG  1L4U  1L4Y  1SHK  1U8A  1VIA  1WE2  1ZUH  1ZUI  
                 1ZYU  2DFN  2DFT  2G1J  2G1K  2IYQ  2IYR  2IYS  2IYT  2IYU  
                 2IYV  2IYW  2IYX  2IYY  2IYZ  2SHK  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.71
            ExPASy - ENZYME nomenclature database: 2.7.1.71
            ExplorEnz - The Enzyme Database: 2.7.1.71
            ERGO genome analysis and discovery system: 2.7.1.71
            BRENDA, the Enzyme Database: 2.7.1.71
            CAS: 9031-51-0
///
ENTRY       EC 2.7.1.72                 Enzyme
NAME        streptomycin 6-kinase;
            streptidine kinase;
            SM 6-kinase;
            streptomycin 6-kinase (phosphorylating);
            streptidine kinase (phosphorylating);
            streptomycin 6-O-phosphotransferase;
            streptomycin 6-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:streptomycin 6-phosphotransferase
REACTION    ATP + streptomycin = ADP + streptomycin 6-phosphate [RN:R02225]
ALL_REAC    R02225
SUBSTRATE   ATP [CPD:C00002];
            streptomycin [CPD:C00413]
PRODUCT     ADP [CPD:C00008];
            streptomycin 6-phosphate [CPD:C01138]
COMMENT     dATP can replace ATP; and dihydrostreptomycin, streptidine and
            2-deoxystreptidine can act as acceptors.
REFERENCE   1  [PMID:4121456]
  AUTHORS   Walker JB, Skorvaga M.
  TITLE     Phosphorylation of streptomycin and dihydrostreptomycin by
            Streptomyces. Enzymatic synthesis of different diphosphorylated
            derivatives.
  JOURNAL   J. Biol. Chem. 248 (1973) 2435-40.
  ORGANISM  Streptomyces griseus
REFERENCE   2  [PMID:6075410]
  AUTHORS   Walker JB, Walker MS.
  TITLE     Streptomycin biosynthesis. Enzymatic synthesis of
            O-phosphorylstreptidine from streptidine and adenosinetriphosphate.
  JOURNAL   Biochim. Biophys. Acta. 148 (1967) 335-41.
  ORGANISM  Streptomyces bikiniensis
PATHWAY     PATH: map00521  Streptomycin biosynthesis
ORTHOLOGY   KO: K04343  streptomycin 6-kinase
GENES       MSM: MSMEG_3480
            MJL: Mjls_2714
            RHA: RHA1_ro02532 RHA1_ro02533
            AAU: AAur_1555(sph)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.72
            ExPASy - ENZYME nomenclature database: 2.7.1.72
            ExplorEnz - The Enzyme Database: 2.7.1.72
            ERGO genome analysis and discovery system: 2.7.1.72
            BRENDA, the Enzyme Database: 2.7.1.72
            CAS: 37278-11-8
///
ENTRY       EC 2.7.1.73                 Enzyme
NAME        inosine kinase;
            inosine-guanosine kinase;
            inosine kinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:inosine 5'-phosphotransferase
REACTION    ATP + inosine = ADP + IMP [RN:R01131]
ALL_REAC    R01131;
            (other) R01228
SUBSTRATE   ATP [CPD:C00002];
            inosine [CPD:C00294]
PRODUCT     ADP [CPD:C00008];
            IMP [CPD:C00130]
REFERENCE   1  [PMID:5645030]
  AUTHORS   Pierre KJ, LePage GA.
  TITLE     Formation of inosine-5'-monophosphate by a kinase in cell-free
            extracts of Ehrlich ascites cells in vitro.
  JOURNAL   Proc. Soc. Exp. Biol. Med. 127 (1968) 432-40.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K00892  inosine kinase
GENES       ECO: b0477(gsk)
            ECJ: JW0466(gsk)
            ECE: Z0596(gsk)
            ECS: ECs0530
            ECC: c0597(gsk)
            ECI: UTI89_C0505(gsk)
            ECP: ECP_0538
            ECW: EcE24377A_0516(gsk)
            ECX: EcHS_A0554(gsk)
            STY: STY0535(gsk)
            STT: t2369(gsk)
            SPT: SPA2231(gsk)
            SEC: SC0533(gsk)
            STM: STM0491(gsk)
            YPE: YPO3095(gsk)
            YPK: y1085(gsk)
            YPM: YP_0831(gsk)
            YPA: YPA_2590
            YPN: YPN_0994
            YPP: YPDSF_2734
            YPS: YPTB1015(gsk)
            YPI: YpsIP31758_3035(gsk)
            SFL: SF0422(gsk)
            SFX: S0429(gsk)
            SFV: SFV_0450(gsk)
            SSN: SSON_0464(gsk)
            SBO: SBO_0377(gsk)
            SDY: SDY_0442(gsk)
            PLU: plu3833(gsk)
            ENT: Ent638_0956
            SPE: Spro_1144
            VCH: VC1129 VCA0801
            VCO: VC0395_0433(gsk-2) VC0395_A0647(gsk-1)
            VVU: VV1_2924 VV2_0218
            VVY: VV1345 VVA0723
            VPA: VP1132 VPA0835
            VFI: VF0911 VFA0696
            PPR: PBPRA1026 PBPRA1908
            SON: SO_2020(gsk)
            SDN: Sden_1431
            SFR: Sfri_1541
            SAZ: Sama_1317
            SBL: Sbal_2544
            SBM: Shew185_2582
            SLO: Shew_2228
            SPC: Sputcn32_2295
            SSE: Ssed_2845
            SPL: Spea_1530
            SHE: Shewmr4_2247
            SHM: Shewmr7_2319
            SHN: Shewana3_2439
            SHW: Sputw3181_1713
            PHA: PSHAa2334(gsk)
            MMW: Mmwyl1_3227
            AHA: AHA_2486
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.73
            ExPASy - ENZYME nomenclature database: 2.7.1.73
            ExplorEnz - The Enzyme Database: 2.7.1.73
            ERGO genome analysis and discovery system: 2.7.1.73
            BRENDA, the Enzyme Database: 2.7.1.73
            CAS: 37237-46-0
///
ENTRY       EC 2.7.1.74                 Enzyme
NAME        deoxycytidine kinase;
            deoxycytidine kinase (phosphorylating);
            2'-deoxycytidine kinase;
            Ara-C kinase;
            arabinofuranosylcytosine kinase;
            deoxycytidine-cytidine kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     NTP:deoxycytidine 5'-phosphotransferase
REACTION    NTP + deoxycytidine = NDP + dCMP [RN:R02321]
ALL_REAC    R02321 > R01666;
            (other) R00185
SUBSTRATE   NTP [CPD:C00201];
            deoxycytidine [CPD:C00881]
PRODUCT     NDP [CPD:C00454];
            dCMP [CPD:C00239]
COMMENT     Cytosine arabinoside can act as acceptor; all natural nucleoside
            triphosphates (except dCTP) can act as donors.
REFERENCE   1  [PMID:5442271]
  AUTHORS   Durham JP, Ives DH.
  TITLE     Deoxycytidine kinase. II. Purification and general properties of the
            calf thymus enzyme.
  JOURNAL   J. Biol. Chem. 245 (1970) 2276-84.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:5462538]
  AUTHORS   Ives DH, Durham JP.
  TITLE     Deoxycytidine kinase. 3. Kinetics and allosteric regulation of the
            calf thymus enzyme.
  JOURNAL   J. Biol. Chem. 245 (1970) 2285-94.
  ORGANISM  cow [GN:bta]
REFERENCE   3
  AUTHORS   Kessel, D.
  TITLE     Properties of deoxycytidine kinase partially purified from L1210
            cells.
  JOURNAL   J. Biol. Chem. 243 (1968) 4739-4744.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:5684726]
  AUTHORS   Momparler RL, Fischer GA.
  TITLE     Mammalian deoxynucleoside kinase. I. Deoxycytidine kinase:
            purification, properties, and kinetic studies with cytosine
            arabinoside.
  JOURNAL   J. Biol. Chem. 243 (1968) 4298-304.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K00893  deoxycitidine kinase
GENES       HSA: 1633(DCK)
            MMU: 13178(Dck)
            RNO: 79127(Dck)
            CFA: 482188(DCK)
            GGA: 422648(DCK)
            XLA: 494987(LOC494987)
            DRE: 541538(zgc:110540)
            OSA: 4338875
            BGA: BG0242(dck)
STRUCTURES  PDB: 1P5Z  1P60  1P61  1P62  2A2Z  2A30  2A7Q  2NO0  2NO1  2NO6  
                 2NO7  2NO9  2NOA  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.74
            ExPASy - ENZYME nomenclature database: 2.7.1.74
            ExplorEnz - The Enzyme Database: 2.7.1.74
            ERGO genome analysis and discovery system: 2.7.1.74
            BRENDA, the Enzyme Database: 2.7.1.74
            CAS: 9039-45-6
///
ENTRY       EC 2.7.1.75       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Deleted entry: thymidine kinase. Now EC 2.7.1.21 thymidine kinase
            (EC 2.7.1.75 created 1972, deleted 1976)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.75
            ExPASy - ENZYME nomenclature database: 2.7.1.75
            ExplorEnz - The Enzyme Database: 2.7.1.75
            ERGO genome analysis and discovery system: 2.7.1.75
            BRENDA, the Enzyme Database: 2.7.1.75
///
ENTRY       EC 2.7.1.76                 Enzyme
NAME        deoxyadenosine kinase;
            purine-deoxyribonucleoside kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:deoxyadenosine 5'-phosphotransferase
REACTION    ATP + deoxyadenosine = ADP + dAMP [RN:R02089]
ALL_REAC    R02089
SUBSTRATE   ATP [CPD:C00002];
            deoxyadenosine [CPD:C00559]
PRODUCT     ADP [CPD:C00008];
            dAMP [CPD:C00360]
COMMENT     Deoxyguanosine can also act as acceptor. Possibly identical with EC
            2.7.1.74 deoxycytidine kinase.
REFERENCE   1  [PMID:6284353]
  AUTHORS   Chang CH, Brockman RW, Bennett LL Jr.
  TITLE     Purification and some properties of a deoxyribonucleoside kinase
            from L1210 cells.
  JOURNAL   Cancer. Res. 42 (1982) 3033-9.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:5667299]
  AUTHORS   Krygier V, Momparler RL.
  TITLE     The regulatory properties of deoxyadenosine kinase.
  JOURNAL   Biochim. Biophys. Acta. 161 (1968) 578-80.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K10353  deoxyadenosine kinase
GENES       BUR: Bcep18194_A3843
            HAR: HEAR2640
            BCZ: BCZK0015(dck)
            BTL: BALH_0015(dck)
            BAY: RBAM_000190
            SPZ: M5005_Spy_0103
            SPH: MGAS10270_Spy0105
            SPI: MGAS10750_Spy0110
            SPJ: MGAS2096_Spy0106
            SPK: MGAS9429_Spy0104
            SPF: SpyM50100
            SPA: M6_Spy0152
            SPB: M28_Spy0101
            LDB: Ldb2196(dak)
            LRE: Lreu_1288 Lreu_1498
            CPF: CPF_0067
STRUCTURES  PDB: 2JAQ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.76
            ExPASy - ENZYME nomenclature database: 2.7.1.76
            ExplorEnz - The Enzyme Database: 2.7.1.76
            ERGO genome analysis and discovery system: 2.7.1.76
            BRENDA, the Enzyme Database: 2.7.1.76
            CAS: 37278-12-9
///
ENTRY       EC 2.7.1.77                 Enzyme
NAME        nucleoside phosphotransferase;
            nonspecific nucleoside phosphotransferase;
            nucleotide:3'-deoxynucleoside 5'-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     nucleotide:nucleoside 5'-phosphotransferase
REACTION    a nucleotide + a 2'-deoxynucleoside = a nucleoside + a
            2'-deoxynucleoside 5'-phosphate [RN:R07341]
ALL_REAC    R07341 > R02934 R05304
SUBSTRATE   nucleotide [CPD:C00215];
            2'-deoxynucleoside [CPD:C02269]
PRODUCT     nucleoside [CPD:C00801];
            2'-deoxynucleoside 5'-phosphate [CPD:C00676]
COMMENT     Phenyl phosphate and nucleoside 3'-phosphates can act as donors,
            although not so well as nucleoside 5'-phosphates. Nucleosides as
            well as 2'-deoxynucleosides can act as acceptors.
REFERENCE   1  [PMID:6061424]
  AUTHORS   Brunngraber EF, Chargaff E.
  TITLE     Purification and properties of a nucleoside phosphotransferase from
            carrot.
  JOURNAL   J. Biol. Chem. 242 (1967) 4834-40.
  ORGANISM  Daucus carota
REFERENCE   2  [PMID:6279651]
  AUTHORS   Prasher DC, Carr MC, Ives DH, Tsai TC, Frey PA.
  TITLE     Nucleoside phosphotransferase from barley. Characterization and
            evidence for ping pong kinetics involving phosphoryl enzyme.
  JOURNAL   J. Biol. Chem. 257 (1982) 4931-9.
  ORGANISM  Hordeum vulgare [GN:ehvu]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.77
            ExPASy - ENZYME nomenclature database: 2.7.1.77
            ExplorEnz - The Enzyme Database: 2.7.1.77
            ERGO genome analysis and discovery system: 2.7.1.77
            BRENDA, the Enzyme Database: 2.7.1.77
            CAS: 9055-37-2
///
ENTRY       EC 2.7.1.78                 Enzyme
NAME        polynucleotide 5'-hydroxyl-kinase;
            ATP:5'-dephosphopolynucleotide 5'-phosphatase;
            PNK;
            polynucleotide 5'-hydroxyl kinase (phosphorylating);
            5'-hydroxyl polynucleotide kinase;
            5'-hydroxyl polyribonucleotide kinase;
            5'-hydroxyl RNA kinase;
            DNA 5'-hydroxyl kinase;
            DNA kinase;
            polynucleotide kinase;
            polynucleotide 5'-hydroxy-kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:5'-dephosphopolynucleotide 5'-phosphotransferase
REACTION    ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA [RN:R03840]
ALL_REAC    R03840
SUBSTRATE   ATP [CPD:C00002];
            5'-dephospho-DNA [CPD:C02374]
PRODUCT     ADP [CPD:C00008];
            5'-phospho-DNA [CPD:C02128]
COMMENT     Also acts on 5'-dephospho-RNA 3'-mononucleotides.
REFERENCE   1  [PMID:4287929]
  AUTHORS   Novogrodsky A, Hurwitz J.
  TITLE     The enzymatic phosphorylation of ribonucleic acid and
            deoxyribonucleic acid. I. Phosphorylation at 5'-hydroxyl termini.
  JOURNAL   J. Biol. Chem. 241 (1966) 2923-32.
  ORGANISM  bacteriophage T4, bacteriophage T2
REFERENCE   2  [PMID:4287930]
  AUTHORS   Novogrodsky A, Tal M, Traub A, Hurwitz J.
  TITLE     The enzymatic phosphorylation of ribonucleic acid and
            deoxyribonucleic acid. II. Further properties of the 5'-hydroxyl
            polynucleotide kinase.
  JOURNAL   J. Biol. Chem. 241 (1966) 2933-43.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K08073  polynucleotide 5'-hydroxyl-kinase
GENES       HSA: 11284(PNKP)
            MMU: 59047(Pnkp)
            RNO: 308576(Pnkp)
            CFA: 484373(PNKP)
            SPU: 586494(LOC586494)
            DME: Dmel_CG9601
            CEL: F21D5.5
            SPO: SPAC23C11.04c SPAC30.02c
            ANI: AN5751.2
            AFM: AFUA_6G06820
            AOR: AO090003000060
            TET: TTHERM_01444910
STRUCTURES  PDB: 1LTQ  1LY1  1RC8  1RPZ  1RRC  1UJX  1YJ5  1YJM  2BRF  2IA5  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.78
            ExPASy - ENZYME nomenclature database: 2.7.1.78
            ExplorEnz - The Enzyme Database: 2.7.1.78
            ERGO genome analysis and discovery system: 2.7.1.78
            BRENDA, the Enzyme Database: 2.7.1.78
            CAS: 37211-65-7
///
ENTRY       EC 2.7.1.79                 Enzyme
NAME        diphosphate---glycerol phosphotransferase;
            PPi-glycerol phosphotransferase;
            pyrophosphate-glycerol phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     diphosphate:glycerol 1-phosphotransferase
REACTION    diphosphate + glycerol = phosphate + glycerol 1-phosphate
            [RN:R01044]
ALL_REAC    R01044
SUBSTRATE   diphosphate [CPD:C00013];
            glycerol [CPD:C00116]
PRODUCT     phosphate [CPD:C00009];
            glycerol 1-phosphate [CPD:C00623]
COMMENT     May be identical with EC 3.1.3.9 glucose-6-phosphatase.
REFERENCE   1  [PMID:4319153]
  AUTHORS   Stetten MR.
  TITLE     Enzymatic synthesis of glycerol I-phosphate. Elevation in diabetic
            and fasted animals, compared with glucose-6-phosphatase and related
            enzyme activities.
  JOURNAL   Biochim. Biophys. Acta. 208 (1970) 394-403.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.79
            ExPASy - ENZYME nomenclature database: 2.7.1.79
            ExplorEnz - The Enzyme Database: 2.7.1.79
            ERGO genome analysis and discovery system: 2.7.1.79
            BRENDA, the Enzyme Database: 2.7.1.79
            CAS: 37278-13-0
///
ENTRY       EC 2.7.1.80                 Enzyme
NAME        diphosphate---serine phosphotransferase;
            pyrophosphate-serine phosphotransferase;
            pyrophosphate-L-serine phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     diphosphate:L-serine O-phosphotransferase
REACTION    diphosphate + L-serine = phosphate + O-phospho-L-serine [RN:R00584]
ALL_REAC    R00584
SUBSTRATE   diphosphate [CPD:C00013];
            L-serine [CPD:C00065]
PRODUCT     phosphate [CPD:C00009];
            O-phospho-L-serine [CPD:C01005]
REFERENCE   1  [PMID:4337852]
  AUTHORS   Cagen LM, Friedmann HC.
  TITLE     Enzymatic phosphorylation of serine.
  JOURNAL   J. Biol. Chem. 247 (1972) 3382-92.
  ORGANISM  Propionibacferium shermanii
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.80
            ExPASy - ENZYME nomenclature database: 2.7.1.80
            ExplorEnz - The Enzyme Database: 2.7.1.80
            ERGO genome analysis and discovery system: 2.7.1.80
            BRENDA, the Enzyme Database: 2.7.1.80
            CAS: 37205-58-6
///
ENTRY       EC 2.7.1.81                 Enzyme
NAME        hydroxylysine kinase;
            hydroxylysine kinase (phosphorylating);
            guanosine triphosphate:5-hydroxy-L-lysine O-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     GTP:5-hydroxy-L-lysine O-phosphotransferase
REACTION    GTP + 5-hydroxy-L-lysine = GDP + 5-phosphonooxy-L-lysine [RN:R03378]
ALL_REAC    R03378
SUBSTRATE   GTP [CPD:C00044];
            5-hydroxy-L-lysine [CPD:C01211]
PRODUCT     GDP [CPD:C00035];
            5-phosphonooxy-L-lysine [CPD:C03366]
COMMENT     Both the natural 5-hydroxy-L-lysine and its 5-epimer act as
            acceptors.
REFERENCE   1  [PMID:4621658]
  AUTHORS   Hiles RA, Henderson LM.
  TITLE     The partial purification and properties of hydroxylysine kinase from
            rat liver.
  JOURNAL   J. Biol. Chem. 247 (1972) 646-51.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.81
            ExPASy - ENZYME nomenclature database: 2.7.1.81
            ExplorEnz - The Enzyme Database: 2.7.1.81
            ERGO genome analysis and discovery system: 2.7.1.81
            BRENDA, the Enzyme Database: 2.7.1.81
            CAS: 9073-58-9
///
ENTRY       EC 2.7.1.82                 Enzyme
NAME        ethanolamine kinase;
            ethanolamine kinase (phosphorylating);
            ethanolamine phosphokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:ethanolamine O-phosphotransferase
REACTION    ATP + ethanolamine = ADP + O-phosphoethanolamine [RN:R01468]
ALL_REAC    R01468
SUBSTRATE   ATP [CPD:C00002];
            ethanolamine [CPD:C00189]
PRODUCT     ADP [CPD:C00008];
            O-phosphoethanolamine [CPD:C00346]
REFERENCE   1
  AUTHORS   Faulkner, A. and Turner, J.M.
  TITLE     Phosphorylation of ethanolamine in catabolism: biodegradative
            adenosine triphosphate-ethanolamine phosphotransferase and related
            enzymes in bacteria.
  JOURNAL   Biochem. Soc. Trans. 2 (1974) 133-136.
REFERENCE   2  [PMID:5626092]
  AUTHORS   Sung CP, Johnstone RM.
  TITLE     Phosphorylation of choline and ethanolamine in Ehrlich
            ascites-carcinoma cells.
  JOURNAL   Biochem. J. 105 (1967) 497-503.
  ORGANISM  mouse [GN:mmu], rat [GN:rno]
REFERENCE   3  [PMID:5047700]
  AUTHORS   Weinhold PA, Rethy VB.
  TITLE     Ethanolamine phosphokinase: activity and properties during liver
            development.
  JOURNAL   Biochim. Biophys. Acta. 276 (1972) 143-54.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00894  ethanolamine kinase
GENES       HSA: 1120(CHKB) 55224(ETNK2) 55500(ETNK1)
            PTR: 465343(ETNK1)
            MMU: 12651(Chkb) 75320(Etnk1)
            RNO: 29367(Chkb) 360843(Etnk2_predicted)
            CFA: 606800(CHKB)
            GGA: 426690(ETNK2)
            SPU: 578881(LOC578881)
            DME: Dmel_CG3525(eas)
            SCE: YDR147W(EKI1)
            PIC: PICST_59919(EKI1)
            AFM: AFUA_1G11550
            AOR: AO090038000268
            DDI: DDBDRAFT_0217566
            PFA: PF11_0257
            TAN: TA06525
            TET: TTHERM_00317160
            TBR: Tb11.18.0017 Tb927.5.1140
            EHI: 1.t00095 6.t00004
            RLE: RL0096 pRL120157
            BBT: BBta_2597
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.82
            ExPASy - ENZYME nomenclature database: 2.7.1.82
            ExplorEnz - The Enzyme Database: 2.7.1.82
            ERGO genome analysis and discovery system: 2.7.1.82
            BRENDA, the Enzyme Database: 2.7.1.82
            CAS: 9075-78-9
///
ENTRY       EC 2.7.1.83                 Enzyme
NAME        pseudouridine kinase;
            pseudouridine kinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:pseudouridine 5'-phosphotransferase
REACTION    ATP + pseudouridine = ADP + pseudouridine 5'-phosphate [RN:R03315]
ALL_REAC    R03315
SUBSTRATE   ATP [CPD:C00002];
            pseudouridine [CPD:C02067]
PRODUCT     ADP [CPD:C00008];
            pseudouridine 5'-phosphate [CPD:C01168]
REFERENCE   1  [PMID:4334133]
  AUTHORS   Solomon LR, Breitman TR.
  TITLE     Pseudouridine kinase of escherichia coli: a new enzyme.
  JOURNAL   Biochem. Biophys. Res. Commun. 44 (1971) 299-304.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00240  Pyrimidine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.83
            ExPASy - ENZYME nomenclature database: 2.7.1.83
            ExplorEnz - The Enzyme Database: 2.7.1.83
            ERGO genome analysis and discovery system: 2.7.1.83
            BRENDA, the Enzyme Database: 2.7.1.83
            CAS: 62213-40-5
///
ENTRY       EC 2.7.1.84                 Enzyme
NAME        alkylglycerone kinase;
            alkyldihydroxyacetone kinase (phosphorylating);
            alkyldihydroxyacetone kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:O-alkylglycerone phosphotransferase
REACTION    ATP + O-alkylglycerone = ADP + O-alkylglycerone phosphate
            [RN:R03944]
ALL_REAC    R03944
SUBSTRATE   ATP [CPD:C00002];
            O-alkylglycerone [CPD:C02446]
PRODUCT     ADP [CPD:C00008];
            O-alkylglycerone phosphate [CPD:C03715]
REFERENCE   1  [PMID:4147653]
  AUTHORS   Chae K, Piantadosi C, Snyder F.
  TITLE     Reductase, phosphatase, and kinase activities in the metabolism of
            alkyldihydroxyacetone phosphate and alkyldihydroxyacetone.
  JOURNAL   J. Biol. Chem. 248 (1973) 6718-23.
  ORGANISM  mouse [GN:mmu]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.84
            ExPASy - ENZYME nomenclature database: 2.7.1.84
            ExplorEnz - The Enzyme Database: 2.7.1.84
            ERGO genome analysis and discovery system: 2.7.1.84
            BRENDA, the Enzyme Database: 2.7.1.84
            CAS: 52227-80-2
///
ENTRY       EC 2.7.1.85                 Enzyme
NAME        beta-glucoside kinase;
            beta-D-glucoside kinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:cellobiose 6-phosphotransferase
REACTION    ATP + cellobiose = ADP + 6-phospho-beta-D-glucosyl-(1,4)-D-glucose
            [RN:R01441 R06176]
ALL_REAC    R01441 R06176(G)
SUBSTRATE   ATP [CPD:C00002];
            cellobiose [CPD:C00185]
PRODUCT     ADP [CPD:C00008];
            6-phospho-beta-D-glucosyl-(1,4)-D-glucose [CPD:C04534]
COMMENT     Phosphorylates a number of beta-D-glucosides; GTP, CTP, ITP and UTP
            can also act as donors.
REFERENCE   1  [PMID:5030625]
  AUTHORS   Palmer RE, Anderson RL.
  TITLE     Cellobiose metabolism in Aerobacter aerogenes. II. Phosphorylation
            of cellobiose with adenosine 5'-triphosphate by a  -glucoside
            kinase.
  JOURNAL   J. Biol. Chem. 247 (1972) 3415-9.
  ORGANISM  Aerobacter aerogenes
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.85
            ExPASy - ENZYME nomenclature database: 2.7.1.85
            ExplorEnz - The Enzyme Database: 2.7.1.85
            ERGO genome analysis and discovery system: 2.7.1.85
            BRENDA, the Enzyme Database: 2.7.1.85
            CAS: 37205-53-1
///
ENTRY       EC 2.7.1.86                 Enzyme
NAME        NADH kinase;
            reduced nicotinamide adenine dinucleotide kinase (phosphorylating);
            DPNH kinase;
            reduced diphosphopyridine nucleotide kinase;
            NADH kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:NADH 2'-phosphotransferase
REACTION    ATP + NADH = ADP + NADPH [RN:R00105]
ALL_REAC    R00105
SUBSTRATE   ATP [CPD:C00002];
            NADH [CPD:C00004]
PRODUCT     ADP [CPD:C00008];
            NADPH [CPD:C00005]
EFFECTOR    Acetate [CPD:C00033]
COMMENT     CTP, ITP, UTP and GTP can also act as phosphate donors (in
            decreasing order of activity). The enzyme is specific for NADH.
            Activated by acetate.
REFERENCE   1  [PMID:4335000]
  AUTHORS   Griffiths MM, Bernofsky C.
  TITLE     Purification and properties of reduced diphosphopyridine nucleotide
            kinase from yeast mitochondria.
  JOURNAL   J. Biol. Chem. 247 (1972) 1473-8.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.86
            ExPASy - ENZYME nomenclature database: 2.7.1.86
            ExplorEnz - The Enzyme Database: 2.7.1.86
            ERGO genome analysis and discovery system: 2.7.1.86
            BRENDA, the Enzyme Database: 2.7.1.86
            CAS: 62213-39-2
///
ENTRY       EC 2.7.1.87                 Enzyme
NAME        streptomycin 3"-kinase;
            streptomycin 3"-kinase (phosphorylating);
            streptomycin 3"-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:streptomycin 3"-phosphotransferase
REACTION    ATP + streptomycin = ADP + streptomycin 3"-phosphate [RN:R02227]
ALL_REAC    R02227
SUBSTRATE   ATP [CPD:C00002];
            streptomycin [CPD:C00413]
PRODUCT     ADP [CPD:C00008];
            streptomycin 3''-phosphate [CPD:C03731]
COMMENT     Also phosphorylates dihydrostreptomycin, 3'-deoxydihydrostreptomycin
            and their 6-phosphates.
REFERENCE   1  [PMID:4121456]
  AUTHORS   Walker JB, Skorvaga M.
  TITLE     Phosphorylation of streptomycin and dihydrostreptomycin by
            Streptomyces. Enzymatic synthesis of different diphosphorylated
            derivatives.
  JOURNAL   J. Biol. Chem. 248 (1973) 2435-40.
  ORGANISM  Streptomyces griseus
GENES       STY: HCM1.223(strA)
            XCV: XCV2325(strB) XCV2326(strA)
            PAP: PSPA7_3432 PSPA7_3719
            PSB: Psyr_2669
            BUR: Bcep18194_B0213
            SMD: Smed_2292
            RLE: RL3433(str)
            OAN: Oant_2501
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.87
            ExPASy - ENZYME nomenclature database: 2.7.1.87
            ExplorEnz - The Enzyme Database: 2.7.1.87
            ERGO genome analysis and discovery system: 2.7.1.87
            BRENDA, the Enzyme Database: 2.7.1.87
            CAS: 39391-15-6
///
ENTRY       EC 2.7.1.88                 Enzyme
NAME        dihydrostreptomycin-6-phosphate 3'alpha-kinase;
            dihydrostreptomycin 6-phosphate kinase (phosphorylating);
            ATP:dihydrostreptomycin-6-P 3'alpha-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:dihydrostreptomycin-6-phosphate 3'alpha-phosphotransferase
REACTION    ATP + dihydrostreptomycin 6-phosphate = ADP + dihydrostreptomycin
            3'alpha,6-bisphosphate [RN:R03395]
ALL_REAC    R03395
SUBSTRATE   ATP [CPD:C00002];
            dihydrostreptomycin 6-phosphate [CPD:C01221]
PRODUCT     ADP [CPD:C00008];
            dihydrostreptomycin 3'alpha,6-bisphosphate [CPD:C01280]
COMMENT     3'-Deoxydihydrostreptomycin 6-phosphate can also act as acceptor.
REFERENCE   1  [PMID:4121456]
  AUTHORS   Walker JB, Skorvaga M.
  TITLE     Phosphorylation of streptomycin and dihydrostreptomycin by
            Streptomyces. Enzymatic synthesis of different diphosphorylated
            derivatives.
  JOURNAL   J. Biol. Chem. 248 (1973) 2435-40.
  ORGANISM  Streptomyces bikiniensis
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.88
            ExPASy - ENZYME nomenclature database: 2.7.1.88
            ExplorEnz - The Enzyme Database: 2.7.1.88
            ERGO genome analysis and discovery system: 2.7.1.88
            BRENDA, the Enzyme Database: 2.7.1.88
            CAS: 39391-14-5
///
ENTRY       EC 2.7.1.89                 Enzyme
NAME        thiamine kinase;
            thiamin kinase (phosphorylating);
            thiamin phosphokinase;
            ATP:thiamin phosphotransferase;
            thiamin kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:thiamine phosphotransferase
REACTION    ATP + thiamine = ADP + thiamine phosphate [RN:R02134]
ALL_REAC    R02134
SUBSTRATE   ATP [CPD:C00002];
            thiamine [CPD:C00378]
PRODUCT     ADP [CPD:C00008];
            thiamine phosphate [CPD:C01081]
REFERENCE   1  [PMID:4550803]
  AUTHORS   Iwashima A, Nishino H, Nose Y.
  TITLE     Conversion of thiamine to thiamine monophosphate by cell-free
            extracts of Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 258 (1972) 333-6.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00730  Thiamine metabolism
ORTHOLOGY   KO: K07251  thiamine kinase
GENES       ECO: b1106(ycfN)
            ECJ: JW1092(ycfN)
            ECE: Z1745(ycfN)
            ECS: ECs1484
            ECC: c1379(ycfN)
            ECI: UTI89_C1234(ycfN)
            ECP: ECP_1098
            ECV: APECO1_187(ycfN)
            ECW: EcE24377A_1228(thiK)
            ECX: EcHS_A1229(thiK)
            STY: STY1248
            STT: t1712
            SPT: SPA1643(ycfN)
            SEC: SC1158(ycfN)
            STM: STM1208(ycfN)
            YPI: YpsIP31758_1591(thiK)
            SFL: SF1110(ycfN)
            SFX: S1190(ycfN)
            SFV: SFV_1126(ycfN)
            SSN: SSON_1126(ycfN)
            SBO: SBO_1955(ycfN)
            SDY: SDY_2044(ycfN)
            SPE: Spro_1923
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.89
            ExPASy - ENZYME nomenclature database: 2.7.1.89
            ExplorEnz - The Enzyme Database: 2.7.1.89
            ERGO genome analysis and discovery system: 2.7.1.89
            BRENDA, the Enzyme Database: 2.7.1.89
            CAS: 62213-38-1
///
ENTRY       EC 2.7.1.90                 Enzyme
NAME        diphosphate---fructose-6-phosphate 1-phosphotransferase;
            6-phosphofructokinase (pyrophosphate);
            pyrophosphate-fructose 6-phosphate 1-phosphotransferase;
            inorganic pyrophosphate-dependent phosphofructokinase;
            inorganic pyrophosphate-phosphofructokinase;
            pyrophosphate-dependent phosphofructo-1-kinase;
            pyrophosphate-fructose 6-phosphate phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     diphosphate:D-fructose-6-phosphate 1-phosphotransferase
REACTION    diphosphate + D-fructose 6-phosphate = phosphate + D-fructose
            1,6-bisphosphate [RN:R00764]
ALL_REAC    R00764 > R02073
SUBSTRATE   diphosphate [CPD:C00013];
            D-fructose 6-phosphate [CPD:C00085]
PRODUCT     phosphate [CPD:C00009];
            D-fructose 1,6-bisphosphate [CPD:C00354]
REFERENCE   1  [PMID:178659]
  AUTHORS   Reeves RE, Serrano R, South DJ.
  TITLE     6-phosphofructokinase (pyrophosphate). Properties of the enzyme from
            Entamoeba histolytica and its reaction mechanism.
  JOURNAL   J. Biol. Chem. 251 (1976) 2958-62.
  ORGANISM  Entamoeba histolytica [GN:ehi]
REFERENCE   2  [PMID:4372217]
  AUTHORS   Reeves RE, South DJ, Blytt HJ, Warren LG.
  TITLE     Pyrophosphate:D-fructose 6-phosphate 1-phosphotransferase. A new
            enzyme with the glycolytic function of 6-phosphofructokinase.
  JOURNAL   J. Biol. Chem. 249 (1974) 7737-41.
  ORGANISM  Entamoeba histolytica [GN:ehi]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K00895  pyrophosphate--fructose-6-phosphate 1-phosphotransferase
GENES       ATH: AT1G12000 AT1G20950 AT1G76550 AT4G04040(MEE51) AT4G32840
            OSA: 4327301 4330512 4340643 4340909
            CME: CMH052C CMM196C
            PFA: PF11_0294
            TAN: TA13950
            TET: TTHERM_00170320 TTHERM_00338460
            EHI: 91.t00031
            GUR: Gura_2657
            PPD: Ppro_1644
            DDE: Dde_1589
            LIP: LI0052(pfp)
            ADE: Adeh_2085
            AFW: Anae109_1732
            SAT: SYN_00887 SYN_02953
            SFU: Sfum_2958 Sfum_3375
            SME: SMc01852(pfk)
            ATU: Atu2115(pfp)
            ATC: AGR_C_3836
            RET: RHE_CH02862(pfk)
            RLE: RL3322(pfp)
            RRU: Rru_A3407
            SUS: Acid_4739
            PAC: PPA1090
            STP: Strop_3267
            RBA: RB10591(pfk)
            CTR: CT205(pfkA_1) CT207(pfkA_2)
            CTA: CTA_0223(pfkA_1) CTA_0225(pfkA_2)
            CMU: TC0477 TC0479
            CPN: CPn0160(pfkA_1) CPn0208(pfkA_2)
            CPA: CP0559 CP0611
            CPJ: CPj0160(pfkA_1) CPj0208(pfkA_2)
            CPT: CpB0161 CpB0212
            CCA: CCA00608 CCA00610
            CAB: CAB581 CAB583
            CFE: CF0393(pfkA1) CF0395(pfkA2)
            PCU: pc0880(pfkA)
            BGA: BG0020(pfpB) BG0749(pfk)
            BAF: BAPKO_0019(pfpB) BAPKO_0771(pfk)
            TPA: TP0108 TP0542
            TDE: TDE1550
            BTH: BT_0307
            BFR: BF3100
            BFS: BF2938
            PGI: PG0163(pfk)
            RCI: RCIX1358(pfp)
STRUCTURES  PDB: 1KZH  2F48  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.90
            ExPASy - ENZYME nomenclature database: 2.7.1.90
            ExplorEnz - The Enzyme Database: 2.7.1.90
            ERGO genome analysis and discovery system: 2.7.1.90
            BRENDA, the Enzyme Database: 2.7.1.90
            CAS: 55326-40-4
///
ENTRY       EC 2.7.1.91                 Enzyme
NAME        sphinganine kinase;
            dihydrosphingosine kinase;
            dihydrosphingosine kinase (phosphorylating);
            sphingosine kinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:sphinganine 1-phosphotransferase
REACTION    ATP + sphinganine = ADP + sphinganine 1-phosphate [RN:R02976]
ALL_REAC    R02976;
            (other) R01926
SUBSTRATE   ATP [CPD:C00002];
            sphinganine [CPD:C00836]
PRODUCT     ADP [CPD:C00008];
            sphinganine 1-phosphate [CPD:C01120]
REFERENCE   1  [PMID:4373374]
  AUTHORS   Stoffel W, Bauer E, Stahl J.
  TITLE     The metabolism of sphingosine bases in Tetrahymena pyriformis.
            Sphingosine kinase and sphingosine-1-phosphate lyase.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 355 (1974) 61-74.
  ORGANISM  Tetrahymena pyriformis
REFERENCE   2  [PMID:4372149]
  AUTHORS   Stoffel W, Heimann G, Hellenbroich B.
  TITLE     Sphingosine kinase in blood platelets.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 354 (1973) 562-6.
  ORGANISM  human [GN:hsa], pig [GN:ssc]
PATHWAY     PATH: map00600  Sphingolipid metabolism
            PATH: map04020  Calcium signaling pathway
            PATH: map04370  VEGF signaling pathway
ORTHOLOGY   KO: K04718  sphingosine kinase
GENES       HSA: 56848(SPHK2) 8877(SPHK1)
            MMU: 20698(Sphk1) 56632(Sphk2)
            RNO: 170897(Sphk1) 308589(Sphk2)
            CFA: 484401(SPHK2)
            SCE: YLR260W(LCB5) YOR171C(LCB4)
            AGO: AGOS_AGR256W
            PIC: PICST_54239(SPH1)
            CGR: CAGL0K05995g
            AFM: AFUA_1G10980
            AOR: AO090038000306
            EHI: 25.t00015
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.91
            ExPASy - ENZYME nomenclature database: 2.7.1.91
            ExplorEnz - The Enzyme Database: 2.7.1.91
            ERGO genome analysis and discovery system: 2.7.1.91
            BRENDA, the Enzyme Database: 2.7.1.91
            CAS: 50864-48-7
///
ENTRY       EC 2.7.1.92                 Enzyme
NAME        5-dehydro-2-deoxygluconokinase;
            5-keto-2-deoxygluconokinase;
            5-keto-2-deoxyglucono kinase (phosphorylating);
            DKH kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:5-dehydro-2-deoxy-D-gluconate 6-phosphotransferase
REACTION    ATP + 5-dehydro-2-deoxy-D-gluconate = ADP +
            6-phospho-5-dehydro-2-deoxy-D-gluconate [RN:R04351]
ALL_REAC    R04351;
            (other) R05661
SUBSTRATE   ATP [CPD:C00002];
            5-dehydro-2-deoxy-D-gluconate [CPD:C03932]
PRODUCT     ADP [CPD:C00008];
            6-phospho-5-dehydro-2-deoxy-D-gluconate [CPD:C04456]
REFERENCE   1  [PMID:4328832]
  AUTHORS   Anderson WA, Magasanik B.
  TITLE     The pathway of myo-inositol degradation in Aerobacter aerogenes.
            Conversion of 2-deoxy-5-keto-D-gluconic acid to glycolytic
            intermediates.
  JOURNAL   J. Biol. Chem. 246 (1971) 5662-75.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00031  Inositol metabolism
ORTHOLOGY   KO: K03338  5-dehydro-2-deoxygluconokinase
GENES       YPE: YPO2585
            YPK: y1153
            YPM: YP_1130(rbsK2)
            YPA: YPA_2516
            YPN: YPN_1069
            YPS: YPTB1078
            ECA: ECA1463
            PLU: plu1801
            HSO: HS_0303(iolC)
            PPR: PBPRB0475
            PST: PSPTO_3500
            PSB: Psyr_3274(pfkB)
            PFL: PFL_2586
            LPN: lpg1651
            LPF: lpl1617(iolCB)
            LPP: lpp1622(iolCB)
            HCH: HCH_01160
            RSO: RSc1240(iolC)
            BMA: BMA0913
            BXE: Bxe_A1326
            BUR: Bcep18194_A4567
            BCN: Bcen_0941
            BCH: Bcen2424_1423
            BAM: Bamb_1303
            BPS: BPSL1994
            BPM: BURPS1710b_1831(iolC)
            BTE: BTH_I2647
            MLO: mll4982
            MES: Meso_3703
            SME: SMc01165(iolC)
            ATU: Atu4512(iolC)
            ATC: AGR_L_714
            RET: RHE_CH01344(iolC)
            RLE: RL1495(iolC)
            BME: BMEII0572
            BMF: BAB2_0526
            BMB: BruAb2_0517
            CCR: CC_1298
            SIT: TM1040_3349
            JAN: Jann_1419
            RDE: RD1_0220
            HNE: HNE_2182(iolC)
            SUS: Acid_1481
            BSU: BG11119(iolC)
            BHA: BH2319(iolC)
            BAN: BA2512
            BAR: GBAA2512
            BAA: BA_3003(pfkB)
            BAT: BAS2333
            BCZ: BCZK2252(iolC)
            BTK: BT9727_2296(iolC)
            BTL: BALH_2258
            BLI: BL00244(iolC)
            BLD: BLi04249(iolC)
            BCL: ABC0424(iolC)
            GKA: GK1888(iolC)
            LMO: lmo0385
            LMF: LMOf2365_0397
            LIN: lin0403
            CPE: CPE0087(iolC)
            CPF: CPF_0082
            CTC: CTC00508(iolC)
            MHY: mhp152(iolC)
            MHJ: MHJ_0220(iolC)
            MHP: MHP7448_0226(iolC)
            MSM: MSMEG_4661
            CGL: NCgl0155(cgl0158)
            CGB: cg0197(iolC)
            RHA: RHA1_ro01350
            SCO: SCO6978(SC8F11.04c)
            SMA: SAV5338(iolC1)
            ART: Arth_0820
            PAC: PPA0456
            ACE: Acel_1803
            RXY: Rxyl_1728
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.92
            ExPASy - ENZYME nomenclature database: 2.7.1.92
            ExplorEnz - The Enzyme Database: 2.7.1.92
            ERGO genome analysis and discovery system: 2.7.1.92
            BRENDA, the Enzyme Database: 2.7.1.92
            CAS: 62213-35-8
///
ENTRY       EC 2.7.1.93                 Enzyme
NAME        alkylglycerol kinase;
            1-alkylglycerol kinase (phosphorylating);
            ATP-alkylglycerol phosphotransferase;
            alkylglycerol phosphotransferase;
            ATP: 1-alkyl-sn-glycerol phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:1-O-alkyl-sn-glycerol 3-phosphotransferase
REACTION    ATP + 1-O-alkyl-sn-glycerol = ADP + 1-O-alkyl-sn-glycerol
            3-phosphate [RN:R04126]
ALL_REAC    R04126
SUBSTRATE   ATP [CPD:C00002];
            1-O-alkyl-sn-glycerol [CPD:C02773]
PRODUCT     ADP [CPD:C00008];
            1-O-alkyl-sn-glycerol 3-phosphate [CPD:C03968]
REFERENCE   1  [PMID:4369816]
  AUTHORS   Rock CO, Snyder F.
  TITLE     Biosynthesis of 1-alkyl-sn-glycero-3-phosphate via adenosine
            triphosphate:1-alkyl-sn-glycerol phosphotransferase.
  JOURNAL   J. Biol. Chem. 249 (1974) 5382-7.
  ORGANISM  rabbit
PATHWAY     PATH: map00565  Ether lipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.93
            ExPASy - ENZYME nomenclature database: 2.7.1.93
            ExplorEnz - The Enzyme Database: 2.7.1.93
            ERGO genome analysis and discovery system: 2.7.1.93
            BRENDA, the Enzyme Database: 2.7.1.93
            CAS: 55354-37-5
///
ENTRY       EC 2.7.1.94                 Enzyme
NAME        acylglycerol kinase;
            monoacylglycerol kinase;
            monoacylglycerol kinase (phosphorylating);
            sn-2-monoacylglycerol kinase;
            MGK;
            monoglyceride kinase;
            monoglyceride phosphokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:acylglycerol 3-phosphotransferase
REACTION    ATP + acylglycerol = ADP + acyl-sn-glycerol 3-phosphate [RN:R03754]
ALL_REAC    R03754 > R02757 R02758
SUBSTRATE   ATP [CPD:C00002];
            acylglycerol [CPD:C15590]
PRODUCT     ADP [CPD:C00008];
            acyl-sn-glycerol 3-phosphate [CPD:C03849]
COMMENT     Acts on both 1- and 2-acylglycerols.
REFERENCE   1  [PMID:14486486]
  AUTHORS   PIERINGER RA, HOKIN LE.
  TITLE     Biosynthesis of lysophosphatdic acid from monoglyceride and
            adenosine triphosphate.
  JOURNAL   J. Biol. Chem. 237 (1962) 653-8.
  ORGANISM  guinea pig, cow [GN:bta]
REFERENCE   2
  AUTHORS   Pieringer, R.A. and Kunnes, R.S.
  TITLE     The biosynthesis of phosphatidic acid and lysophosphatidic acid by
            glyceride phosphokinase pathways in Escherichia coli.
  JOURNAL   J. Biol. Chem. 240 (1965) 2833-2838.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00561  Glycerolipid metabolism
ORTHOLOGY   KO: K09881  acylglycerol kinase
GENES       HSA: 55750(AGK)
            PTR: 463784(AGK)
            MMU: 69923(Agk)
            RNO: 502749(RGD1562046_predicted)
            CFA: 482764(AGK)
            GGA: 418121(AGK)
            XLA: 379163(MGC52920)
            DRE: 334270(agk)
            SPU: 579766(LOC579766)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.94
            ExPASy - ENZYME nomenclature database: 2.7.1.94
            ExplorEnz - The Enzyme Database: 2.7.1.94
            ERGO genome analysis and discovery system: 2.7.1.94
            BRENDA, the Enzyme Database: 2.7.1.94
            CAS: 62213-37-0
///
ENTRY       EC 2.7.1.95                 Enzyme
NAME        kanamycin kinase;
            neomycin-kanamycin phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:kanamycin 3'-O-phosphotransferase
REACTION    ATP + kanamycin = ADP + kanamycin 3'-phosphate
ALL_REAC    (other) R01888
SUBSTRATE   ATP [CPD:C00002];
            kanamycin [CPD:C00304]
PRODUCT     ADP [CPD:C00008];
            kanamycin 3'-phosphate [CPD:C03281]
COMMENT     Also acts on the antibiotics neomycin, paromomycin, neamine,
            paromamine, vistamycin and gentamicin A. An enzyme from Pseudomonas
            aeruginosa also acts on butirosin.
REFERENCE   1  [PMID:4970990]
  AUTHORS   Doi O, Ogura M, Tanaka N, Umezawa H.
  TITLE     Inactivation of kanamycin, neomycin, and streptomycin by enzymes
            obtained in cells of Pseudomonas aeruginoa.
  JOURNAL   Appl. Microbiol. 16 (1968) 1276-81.
  ORGANISM  Pseudomonas aeruginoa
REFERENCE   2  [PMID:13416259]
  AUTHORS   DOLIN MI.
  TITLE     The Streptococcus faecalis oxidases for reduced diphosphopyridine
            nucleotide.  III.  Isolation and properties of a flavin peroxidase
            for reduced diphosphopyridine nucleotide.
  JOURNAL   J. Biol. Chem. 225 (1957) 557-73.
ORTHOLOGY   KO: K00897  aminoglycoside 3'-phosphotransferase
GENES       SEC: SC026(aph)
            PAE: PA4119(aph)
            PAU: PA14_10670(aph)
            PAP: PSPA7_3721
            REH: H16_A0848 H16_A1099 H16_B1333
            BUR: Bcep18194_B2197
            SUN: SUN_1240
            MLO: mlr2696
            SME: SMc03094
            RET: RHE_CH02947(ypch01023)
            RLE: RL1455 RL3397(neo)
            BCZ: BCZK1266(aph) BCZK1900(aph)
            BTK: BT9727_1264(aph)
            BPU: BPUM_1575
            SER: SEA0010(aphA)
            LLA: L33782(ymdC)
            LLC: LACR_1330
            SSA: SSA_1830
            SGO: SGO_0628(ymdC)
            LJO: LJ1688
            LAC: LBA1348
            MTU: Rv3817
            MTC: MT3925.1(aph)
            MBO: Mb3847
            NFA: nfa38480
            DRA: DR_0066
            DGE: Dgeo_2256
STRUCTURES  PDB: 1J7I  1J7L  1J7U  1L8T  1ND4  2B0Q  2BKK  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.95
            ExPASy - ENZYME nomenclature database: 2.7.1.95
            ExplorEnz - The Enzyme Database: 2.7.1.95
            ERGO genome analysis and discovery system: 2.7.1.95
            BRENDA, the Enzyme Database: 2.7.1.95
            CAS: 62213-36-9
///
ENTRY       EC 2.7.1.96       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Deleted entry: NADH kinase. Now included with EC 2.7.1.86 NADH
            kinase (EC 2.7.1.96 created 1978, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.96
            ExPASy - ENZYME nomenclature database: 2.7.1.96
            ExplorEnz - The Enzyme Database: 2.7.1.96
            ERGO genome analysis and discovery system: 2.7.1.96
            BRENDA, the Enzyme Database: 2.7.1.96
///
ENTRY       EC 2.7.1.97       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Deleted entry: identical with EC 2.7.11.14, rhodopsin kinase (EC
            2.7.1.97 created 1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.97
            ExPASy - ENZYME nomenclature database: 2.7.1.97
            ExplorEnz - The Enzyme Database: 2.7.1.97
            ERGO genome analysis and discovery system: 2.7.1.97
            BRENDA, the Enzyme Database: 2.7.1.97
///
ENTRY       EC 2.7.1.98       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Deleted entry: phosphoenolpyruvate-fructose phosphotransferase (EC
            2.7.1.98 created 1978, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.98
            ExPASy - ENZYME nomenclature database: 2.7.1.98
            ExplorEnz - The Enzyme Database: 2.7.1.98
            ERGO genome analysis and discovery system: 2.7.1.98
            BRENDA, the Enzyme Database: 2.7.1.98
///
ENTRY       EC 2.7.1.99       Obsolete  Enzyme
NAME        Transferred to 2.7.11.2
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.2 [pyruvate dehydrogenase
            (acetyl-transferring)] kinase (EC 2.7.1.99 created 1978, deleted
            2005)
STRUCTURES  PDB: 1JM6  1Y8N  1Y8O  1Y8P  2BTZ  2BU2  2BU5  2BU6  2BU7  2BU8  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.99
            ExPASy - ENZYME nomenclature database: 2.7.1.99
            ExplorEnz - The Enzyme Database: 2.7.1.99
            ERGO genome analysis and discovery system: 2.7.1.99
            BRENDA, the Enzyme Database: 2.7.1.99
///
ENTRY       EC 2.7.1.100                Enzyme
NAME        S-methyl-5-thioribose kinase;
            5-methylthioribose kinase (phosphorylating);
            methylthioribose kinase;
            5-methylthioribose kinase;
            ATP:S5-methyl-5-thio-D-ribose 1-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:S-methylmethyl-5-thio-D-ribose 1-phosphotransferase
REACTION    ATP + S-methyl-5-thio-D-ribose = ADP +
            S-methyl-5-thio-alpha-D-ribose 1-phosphate [RN:R04143]
ALL_REAC    R04143
SUBSTRATE   ATP [CPD:C00002];
            S-methyl-5-thio-D-ribose [CPD:C03089]
PRODUCT     ADP [CPD:C00008];
            S-methyl-5-thio-alpha-D-ribose 1-phosphate [CPD:C04188]
COMMENT     CTP also acts, but more slowly.
REFERENCE   1  [PMID:210167]
  AUTHORS   Ferro AJ, Barrett A, Shapiro SK.
  TITLE     5-Methylthioribose kinase. A new enzyme involved in the formation of
            methionine from 5-methylthioribose.
  JOURNAL   J. Biol. Chem. 253 (1978) 6021-5.
  ORGANISM  Enterobacter aerogenes
REFERENCE   2
  AUTHORS   Guranowski, A.
  TITLE     Plant 5-methylthioribose kinase.
  JOURNAL   Plant Physiol. 71 (1983) 932-935.
  ORGANISM  Lupinus luteus
PATHWAY     PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K00899  5-methylthioribose kinase
GENES       YPP: YPDSF_2878
            YPS: YPTB0878
            YPI: YpsIP31758_3178(mtnK)
            YEN: YE3228(mtrK)
            ECA: ECA3476(mtrK)
            ENT: Ent638_1139
            SPE: Spro_0946
            TDN: Tmden_1972
            SMD: Smed_5889
            OAN: Oant_4831
            BRA: BRADO4166
            BBT: BBta_4543
            XAU: Xaut_0964
            RDE: RD1_2383
            GOX: GOX1782
            BSU: BG13279(mtnK)
            BAN: BA0346 BA4252
            BAR: GBAA0346 GBAA4252
            BAA: BA_0917 BA_4711
            BAT: BAS0331 BAS3943
            BCE: BC0378 BC4033
            BCA: BCE_4099
            BCZ: BCZK0318(mtrK) BCZK3790(mtnK)
            BCY: Bcer98_2732
            BTK: BT9727_0315(mtrK) BT9727_3775(mtnK)
            BTL: BALH_0337(mtrK) BALH_3650(mtnK)
            BLI: BL03633(mtnK)
            BLD: BLi01512(ykrT)
            BAY: RBAM_013340
            BPU: BPUM_1250
            GKA: GK0950
            CTC: CTC00946
            CBO: CBO1267(mtnK)
            CBA: CLB_1295(mtnK)
            CBH: CLC_1305(mtnK)
            CBF: CLI_1352(mtnK)
            AMT: Amet_3756
            NCA: Noca_0407
            FNU: FN1412
            TDE: TDE0689
STRUCTURES  PDB: 2OLC  2PU8  2PUI  2PUL  2PUN  2PUP  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.100
            ExPASy - ENZYME nomenclature database: 2.7.1.100
            ExplorEnz - The Enzyme Database: 2.7.1.100
            ERGO genome analysis and discovery system: 2.7.1.100
            BRENDA, the Enzyme Database: 2.7.1.100
            CAS: 68247-56-3
///
ENTRY       EC 2.7.1.101                Enzyme
NAME        tagatose kinase;
            tagatose 6-phosphate kinase (phosphorylating);
            D-tagatose 6-phosphate kinase;
            tagatose-6-phosphate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-tagatose 6-phosphotransferase
REACTION    ATP + D-tagatose = ADP + D-tagatose 6-phosphate [RN:R02927]
ALL_REAC    R02927
SUBSTRATE   ATP [CPD:C00002];
            D-tagatose [CPD:C00795]
PRODUCT     ADP [CPD:C00008];
            D-tagatose 6-phosphate [CPD:C01097]
REFERENCE   1  [PMID:6269638]
  AUTHORS   Szumioo T.
  TITLE     A novel enzyme, tagatose kinase, from Mycobacterium butyricum.
  JOURNAL   Biochim. Biophys. Acta. 660 (1981) 366-70.
  ORGANISM  Mycobacterium butyricum
PATHWAY     PATH: map00052  Galactose metabolism
STRUCTURES  PDB: 2FIQ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.101
            ExPASy - ENZYME nomenclature database: 2.7.1.101
            ExplorEnz - The Enzyme Database: 2.7.1.101
            ERGO genome analysis and discovery system: 2.7.1.101
            BRENDA, the Enzyme Database: 2.7.1.101
            CAS: 39434-00-9
///
ENTRY       EC 2.7.1.102                Enzyme
NAME        hamamelose kinase;
            hamamelose kinase (phosphorylating);
            hamamelosekinase (ATP: hamamelose 2'-phosphotransferase);
            ATP/hamamelose 2'-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-hamamelose 2'-phosphotransferase
REACTION    ATP + D-hamamelose = ADP + D-hamamelose 2'-phosphate [RN:R03766]
ALL_REAC    R03766
SUBSTRATE   ATP [CPD:C00002];
            D-hamamelose [CPD:C01906]
PRODUCT     ADP [CPD:C00008];
            D-hamamelose 2'-phosphate
COMMENT     Also acts, more slowly, on D-hamamelitol.
REFERENCE   1  [PMID:6249593]
  AUTHORS   Beck E, Wieczorek J, Reinecke W.
  TITLE     Purification and properties of hamamelosekinase.
  JOURNAL   Eur. J. Biochem. 107 (1980) 485-9.
  ORGANISM  Kluyvera citrophila
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.102
            ExPASy - ENZYME nomenclature database: 2.7.1.102
            ExplorEnz - The Enzyme Database: 2.7.1.102
            ERGO genome analysis and discovery system: 2.7.1.102
            BRENDA, the Enzyme Database: 2.7.1.102
            CAS: 74506-53-9
///
ENTRY       EC 2.7.1.103                Enzyme
NAME        viomycin kinase;
            viomycin phosphotransferase;
            capreomycin phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:viomycin O-phosphotransferase
REACTION    ATP + viomycin = ADP + O-phosphoviomycin [RN:R03607]
ALL_REAC    R03607
SUBSTRATE   ATP [CPD:C00002];
            viomycin [CPD:C01540]
PRODUCT     ADP [CPD:C00008];
            O-phosphoviomycin [CPD:C02574]
COMMENT     Acts also on capreomycins. A serine residue in the peptide
            antibiotics acts as phosphate-acceptor.
REFERENCE   1  [PMID:6163840]
  AUTHORS   Skinner RH, Cundliffe E.
  TITLE     Resistance to the antibiotics viomycin and capreomycin in the
            Streptomyces species which produce them.
  JOURNAL   J. Gen. Microbiol. 120 (1980) 95-104.
  ORGANISM  Streptomyces vinaceus, Streptomyces capreolus
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.103
            ExPASy - ENZYME nomenclature database: 2.7.1.103
            ExplorEnz - The Enzyme Database: 2.7.1.103
            ERGO genome analysis and discovery system: 2.7.1.103
            BRENDA, the Enzyme Database: 2.7.1.103
            CAS: 77000-11-4
///
ENTRY       EC 2.7.1.104      Obsolete  Enzyme
NAME        Transferred to 2.7.99.1
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.99.1 triphosphate-protein
            phosphotransferase (EC 2.7.1.104 created 1987, deleted 2005)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.104
            ExPASy - ENZYME nomenclature database: 2.7.1.104
            ExplorEnz - The Enzyme Database: 2.7.1.104
            ERGO genome analysis and discovery system: 2.7.1.104
            BRENDA, the Enzyme Database: 2.7.1.104
///
ENTRY       EC 2.7.1.105                Enzyme
NAME        6-phosphofructo-2-kinase;
            phosphofructokinase 2;
            6-phosphofructose 2-kinase;
            6-phosphofructo-2-kinase (phosphorylating);
            fructose 6-phosphate 2-kinase;
            ATP:D-fructose-6-phosphate 2-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:beta-D-fructose-6-phosphate 2-phosphotransferase
REACTION    ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose
            2,6-bisphosphate [RN:R02732]
ALL_REAC    R02732
SUBSTRATE   ATP [CPD:C00002];
            beta-D-fructose 6-phosphate [CPD:C05345]
PRODUCT     ADP [CPD:C00008];
            beta-D-fructose 2,6-bisphosphate [CPD:C00665]
COMMENT     Not identical with EC 2.7.1.11 6-phosphofructokinase. The enzyme
            co-purifies with EC 3.1.3.46 fructose-2,6-bisphosphate
            2-phosphatase.
REFERENCE   1  [PMID:6458291]
  AUTHORS   Van Schaftingen E, Hers HG.
  TITLE     Phosphofructokinase 2: the enzyme that forms fructose
            2,6-bisphosphate from fructose 6-phosphate and ATP.
  JOURNAL   Biochem. Biophys. Res. Commun. 101 (1981) 1078-84.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K00900  6-phosphofructo-2-kinase
GENES       HSA: 5207(PFKFB1) 5208(PFKFB2) 5209(PFKFB3) 5210(PFKFB4)
            MMU: 170768(Pfkfb3) 18640(Pfkfb2) 270198(Pfkfb4)
            RNO: 117276(Pfkfb3) 24638(Pfkfb1) 24640(Pfkfb2) 54283(Pfkfb4)
            CFA: 484777(PFKFB4) 487139(PFKFB3) 491903(PFKFB1)
            BTA: 282304(PFKFB1) 287019(PFKFB2)
            GGA: 415906(PFKFB4) 418247(PFKFB3) 419850(PFKFB2)
            XLA: 432000(MGC81068) 495408(LOC495408)
            XTR: 407880(TGas144d10.1)
            DRE: 386663(pfkfb4) 393983(pfkfb2)
            SPU: 579456(LOC579456)
            CEL: K02B2.1(6-phosphofructo-2-kinase)
            OSA: 4337906
            CME: CMN085C
            SCE: YIL107C(PFK26) YOL136C(PFK27)
            AGO: AGOS_ADL183C AGOS_ADL237C
            PIC: PICST_57978(FRK26.2) PICST_66347(PFK26) PICST_85029(FRK26.1)
            CGR: CAGL0C01397g CAGL0E01529g CAGL0G01100g
            SPO: SPAC222.13c
            ANI: AN5144.2 AN6720.2
            AFM: AFUA_1G07220
            AOR: AO090012000976
            DDI: DDBDRAFT_0217769
            TBR: Tb927.3.2710 Tb927.7.1610 Tb927.8.1020
            TCR: 508153.950 508181.20
            LMA: LmjF26.0310 LmjF36.0150
            DVU: DVU3147
            DDE: Dde_0511
            LIP: LI0094(pfk)
STRUCTURES  PDB: 1BIF  1K6M  2AXN  2BIF  2DWO  2DWP  2I1V  3BIF  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.105
            ExPASy - ENZYME nomenclature database: 2.7.1.105
            ExplorEnz - The Enzyme Database: 2.7.1.105
            ERGO genome analysis and discovery system: 2.7.1.105
            BRENDA, the Enzyme Database: 2.7.1.105
            CAS: 78689-77-7
///
ENTRY       EC 2.7.1.106                Enzyme
NAME        glucose-1,6-bisphosphate synthase;
            glucose 1,6-diphosphate synthase;
            glucose-1,6-bisphosphate synthetase;
            3-phospho-D-glyceroyl-phosphate:D-glucose-1-phosphate
            6-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     3-phospho-D-glyceroyl-phosphate:alpha-D-glucose-1-phosphate
            6-phosphotransferase
REACTION    3-phospho-D-glyceroyl phosphate + alpha-D-glucose 1-phosphate =
            3-phospho-D-glycerate + alpha-D-glucose 1,6-bisphosphate [RN:R01660]
ALL_REAC    R01660
SUBSTRATE   3-phospho-D-glyceroyl phosphate [CPD:C00236];
            alpha-D-glucose 1-phosphate [CPD:C00103]
PRODUCT     3-phospho-D-glycerate [CPD:C00197];
            alpha-D-glucose 1,6-bisphosphate [CPD:C01231]
COMMENT     D-Glucose 6-phosphate can act as acceptor, forming alpha-D-glucose
            1,6-bisphosphate.
REFERENCE   1  [PMID:235548]
  AUTHORS   Rose IA, Warms JV, Kaklij G.
  TITLE     A specific enzyme for glucose 1,6-bisphosphate synthesis.
  JOURNAL   J. Biol. Chem. 250 (1975) 3466-70.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map00500  Starch and sucrose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.106
            ExPASy - ENZYME nomenclature database: 2.7.1.106
            ExplorEnz - The Enzyme Database: 2.7.1.106
            ERGO genome analysis and discovery system: 2.7.1.106
            BRENDA, the Enzyme Database: 2.7.1.106
            CAS: 56214-39-2
///
ENTRY       EC 2.7.1.107                Enzyme
NAME        diacylglycerol kinase;
            diglyceride kinase;
            1,2-diacylglycerol kinase (phosphorylating);
            1,2-diacylglycerol kinase;
            sn-1,2-diacylglycerol kinase;
            DG kinase;
            DGK;
            ATP:diacylglycerol phosphotransferase;
            arachidonoyl-specific diacylglycerol kinase;
            diacylglycerol:ATP kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:1,2-diacylglycerol 3-phosphotransferase
REACTION    ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
            [RN:R02240]
ALL_REAC    R02240
SUBSTRATE   ATP [CPD:C00002];
            1,2-diacylglycerol [CPD:C00641]
PRODUCT     ADP [CPD:C00008];
            1,2-diacyl-sn-glycerol 3-phosphate [CPD:C00416]
REFERENCE   1  [PMID:185051]
  AUTHORS   Daleo GR, Piras MM, Piras R.
  TITLE     Diglyceride kinase activity of microtubules. Characterization and
            comparison with the protein kinase and ATPase activities associated
            with vinblastine-isolated tubulin of chick embryonic muscles.
  JOURNAL   Eur. J. Biochem. 68 (1976) 339-46.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:13961253]
  AUTHORS   HOKIN LE, HOKIN MR.
  TITLE     Diglyceride kinase and other path ways for phosphatidic acid
            synthesis in the erythrocyte membrane.
  JOURNAL   Biochim. Biophys. Acta. 67 (1963) 470-84.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:4940043]
  AUTHORS   Weissbach H, Thomas E, Kaback HR.
  TITLE     Studies on the metabolism of ATP by isolated bacterial membranes:
            formation and metabolism of membrane-bound phosphatidic acid.
  JOURNAL   Arch. Biochem. Biophys. 147 (1971) 249-54.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00561  Glycerolipid metabolism
            PATH: map00564  Glycerophospholipid metabolism
            PATH: map04070  Phosphatidylinositol signaling system
ORTHOLOGY   KO: K00901  diacylglycerol kinase
GENES       HSA: 1606(DGKA) 1607(DGKB) 1608(DGKG) 160851(DGKH) 1609(DGKQ)
                 8525(DGKZ) 8526(DGKE) 8527(DGKD) 9162(DGKI)
            PTR: 451976(DGKA) 452564(DGKH) 463271(DGKB) 468414(DGKE)
            MMU: 104418(Dgkz) 110197(Dgkg) 110524(Dgkq) 13139(Dgka)
            RNO: 25666(Dgkg) 54248(Dgkb) 81821(Dgkz)
            CFA: 474393(DGKA) 476932(DGKH) 482328(DGKB) 482709(DGKI)
                 486167(DGKD) 488115(DGKG) 488867(DGKQ) 491102(DGKE)
            SSC: 397097(DGKA)
            GGA: 423197(RCJMB04_1p14) 427381(DGKQ) 769506(DGKH) 770911(DGKE)
                 772367(DGKB)
            XLA: 447404(MGC81643)
            SPU: 580494(LOC580494) 591406(LOC591406) 591454(LOC591454)
            DME: Dmel_CG10966(rdgA) Dmel_CG1747(Sk1) Dmel_CG18654(Dgk)
                 Dmel_CG31187 Dmel_CG32484(Sk2) Dmel_CG8657(Dgkepsilon)
            CEL: C09E10.2(dgk-1) F42A9.1(kinase) F54G8.2(dgk-3) K06A1.6
            ATH: AT5G07920(DGK1) AT5G63770(ATDGK2)
            OSA: 4352615
            DDI: DDB_0185037(dgkA)
            PFA: PF14_0681 PFI1485c
            CPV: cgd4_4340
            CHO: Chro.40493
            TAN: TA13375
            TET: TTHERM_00780620 TTHERM_00881480
            TCR: 507257.80
            LMA: LmjF35.5370
            EHI: 13.t00032 78.t00033
            ECO: b4042(dgkA)
            ECJ: JW4002(dgkA)
            ECE: Z1139 Z1578 Z5641(dgkA)
            ECS: ECs1316 ECs5025
            ECC: c5013(dgkA)
            ECI: UTI89_C2362 UTI89_C4612(dgkA)
            ECP: ECP_4260
            ECV: APECO1_2427(dgkA)
            ECW: EcE24377A_4595(dgkA)
            ECX: EcHS_A4282
            STY: STY4432(dgkA)
            STT: t4142(dgkA)
            SPT: SPA4053(dgkA)
            SEC: SC4115(dgkA)
            STM: STM4236(dgkA)
            YPE: YPO0313(dgkA)
            YPK: y0571(dgkA)
            YPM: YP_0469(dgkA)
            YPA: YPA_3971
            YPN: YPN_3356
            YPS: YPTB0369(dgkA)
            YPI: YpsIP31758_3771(dgkA)
            SFL: SF4163(dgkA)
            SFX: S3568(dgkA)
            SFV: SFV_4171(dgkA)
            SSN: SSON_4222(dgkA)
            SBO: SBO_4075(dgkA)
            SDY: SDY_4532(dgkA)
            ECA: ECA0629(dgkA)
            PLU: plu4375(dgkA)
            HIN: HI0335(dgkA)
            HIT: NTHI0453(dgkA)
            HDU: HD1253(dgkA)
            HSO: HS_0096(dgkA)
            PMU: PM1864(dgkA)
            MSU: MS0242(dgkA)
            APL: APL_0768(dgkA)
            XFA: XF2334
            XFT: PD1366(dgkA)
            XCC: XCC0782(dgkA)
            XCB: XC_3449
            XCV: XCV0890(dgkA)
            XAC: XAC0837(dgkA)
            XOO: XOO3757(dgkA)
            XOM: XOO_3548(XOO3548)
            VCH: VCA0714
            VCO: VC0395_0653(dgkA)
            VVU: VV1_0815 VV2_1412
            VVY: VV0296 VVA0247
            VPA: VP0195 VPA1279
            VFI: VF0418
            PPR: PBPRB0246
            PAE: PA3603(dgkA)
            PAU: PA14_17675(dgkA)
            PPU: PP_1636(dgkA-1) PP_2973(dgkA-2)
            PST: PSPTO_4026(dgkA)
            PSB: Psyr_1385
            PSP: PSPPH_3799(dgkA)
            PFL: PFL_1239(dgkA)
            PFO: Pfl_1183
            PEN: PSEEN4121(dgkA)
            PAR: Psyc_1164(dgkA)
            PCR: Pcryo_1242
            ACI: ACIAD2837(dgkA)
            ACB: A1S_2663
            SON: SO_2203(dgkA)
            SDN: Sden_0801 Sden_2308
            SFR: Sfri_0237 Sfri_1483
            SAZ: Sama_1996
            SBL: Sbal_1851
            SLO: Shew_1586
            SHE: Shewmr4_2192
            SHM: Shewmr7_2269
            SHN: Shewana3_2402
            SHW: Sputw3181_2278
            ILO: IL0089 IL1651(dgkA)
            CPS: CPS_2715(dgkA)
            PHA: PSHAa2773(dgkA) PSHAa2786(dgkA)
            SDE: Sde_1725
            PIN: Ping_0193
            MCA: MCA0048(dgkA)
            TCX: Tcr_1599
            HCH: HCH_04856
            CSA: Csal_2929
            AHA: AHA_2732(dgkA)
            NME: NMB1558
            NMA: NMA1746(dgk)
            NMC: NMC1475(dgk)
            NGO: NGO1216
            CVI: CV_4274(dgkA)
            RSO: RSc2085(dgkA)
            REU: Reut_A0939
            REH: H16_A1027(dgkA)
            RME: Rmet_0903
            BMA: BMA1856(dgkA)
            BMV: BMASAVP1_A1106(dgkA)
            BML: BMA10299_A0760(dgkA)
            BMN: BMA10247_0389(dgkA)
            BXE: Bxe_A3238
            BUR: Bcep18194_A5599
            BCN: Bcen_1660
            BCH: Bcen2424_2272
            BAM: Bamb_2310
            BPS: BPSL1189
            BPM: BURPS1710b_1411
            BPL: BURPS1106A_1273(dgkA)
            BPD: BURPS668_1266(dgkA)
            BTE: BTH_I1038
            BPE: BP3492(dgkA)
            BPA: BPP0865(dgkA)
            BBR: BB0959(dgkA)
            POL: Bpro_2312
            PNA: Pnap_1712
            AJS: Ajs_1764
            VEI: Veis_1740
            MPT: Mpe_A2110
            HAR: HEAR0819(dgkA)
            MMS: mma_0734
            EBA: ebA1477(dgkA) ebA5579(dgkA) ebA607(dgkA)
            AZO: azo0859(dgkA)
            DAR: Daro_0472 Daro_3544
            TBD: Tbd_0172
            MFA: Mfla_0788
            HPY: HP0700(dgkA)
            HPA: HPAG1_0685
            HHE: HH0220(dgkA)
            HAC: Hac_0960(dgkA)
            WSU: WS0642(dgkA)
            TDN: Tmden_0318
            CJE: Cj0257(dgkA)
            CJR: CJE0307(dgkA)
            CJJ: CJJ81176_0284(dgkA)
            CJU: C8J_0234(dgkA)
            CJD: JJD26997_1724(dgkA)
            CCV: CCV52592_0736
            CCO: CCC13826_1801 CCC13826_2155(dgkA)
            ABU: Abu_1819(dgkA)
            NIS: NIS_0210(dgkA)
            SUN: SUN_0415
            GSU: GSU2283
            GME: Gmet_2369
            PCA: Pcar_1234
            DVU: DVU3377(dgkA)
            LIP: LI0101(dgkA)
            DPS: DP1070
            MXA: MXAN_2813
            SAT: SYN_02353
            WOL: WD1163(dgkA)
            MLO: mll0823
            SME: SMc04213(dgkA)
            ATU: Atu1889(dgk)
            ATC: AGR_C_3466(dgkA)
            RET: RHE_CH02442(dgkA)
            RLE: RL2780(dgkA)
            BME: BMEI0970
            BMF: BAB1_1032
            BMS: BR1014(dgkA)
            BMB: BruAb1_1019(dgkA)
            BOV: BOV_0980(dgkA)
            BRA: BRADO4703
            BBT: BBta_3494
            RPE: RPE_1992
            NHA: Nham_1484
            RSP: RSP_3087(dgkA)
            MGM: Mmc1_2290
            BSU: BG11040(dgkA)
            BHA: BH1364
            BAN: BA4526(dgkA)
            BAR: GBAA4526(dgkA)
            BAA: BA_4973
            BAT: BAS4201
            BCE: BC4299
            BCA: BCE_4382(dgkA)
            BCZ: BCZK4049(dgkA)
            BTK: BT9727_4039(dgkA)
            BTL: BALH_3892(dgkA)
            BLD: BLi02722(dgkA)
            BCL: ABC1679(dgkA)
            BAY: RBAM_023610
            BPU: BPUM_0650(yerQ)
            OIH: OB1952(dgkA)
            GKA: GK2490
            SAU: SA1398
            SAV: SAV1569
            SAM: MW1521
            SAR: SAR1646
            SAS: SAS1507
            SAC: SACOL1626(dgkA)
            SAB: SAB1441c
            SAA: SAUSA300_1529(dgkA)
            SAO: SAOUHSC_01671
            SEP: SE1256
            SER: SERP1136(dgkA)
            SHA: SH1347
            SSP: SSP1187
            LMO: lmo1464
            LMF: LMOf2365_1483(dgkA)
            LIN: lin1501
            LWE: lwe1479(dgkA)
            LLA: L95012(dgkA)
            LLC: LACR_1187
            LLM: llmg_1486(dgkA)
            SPY: SPy_0475(dgk)
            SPZ: M5005_Spy_0389(dgk)
            SPM: spyM18_0516
            SPG: SpyM3_0336(dgk)
            SPS: SPs1521
            SPH: MGAS10270_Spy0390(dgk)
            SPI: MGAS10750_Spy0388(dgk)
            SPJ: MGAS2096_Spy0409(dgk)
            SPK: MGAS9429_Spy0389(dgk)
            SPF: SpyM51479(dgk)
            SPA: M6_Spy0414
            SPB: M28_Spy0375(dgk)
            SPN: SP_0968
            SPR: spr0870(dgkA)
            SPD: SPD_0856(dgkA)
            SAG: SAG1500(dgkA)
            SAN: gbs1561
            SAK: SAK_1526(dgkA)
            SMU: SMU.1618(dagK)
            STC: str0618(dgk)
            STL: stu0618(dgk)
            SSA: SSA_1612(dgk)
            SGO: SGO_0712(dgkA)
            LPL: lp_1968(dgk)
            LSA: LSA0877(dgkA)
            LSL: LSL_0896(dgkA)
            LBR: LVIS_0750
            LCA: LSEI_1517
            PPE: PEPE_1105
            EFA: EF2411(dgkA)
            OOE: OEOE_0988
            STH: STH532
            CAC: CAC1294(dgkA)
            CPE: CPE2017(dgkA)
            CPF: CPF_2274
            CTC: CTC02020
            CNO: NT01CX_0045(dgkA)
            CHY: CHY_0428(dgkA)
            DSY: DSY3108
            SWO: Swol_1563
            TTE: TTE0973(dgkA)
            MTA: Moth_0596
            MPE: MYPE3360(dgkA)
            RXY: Rxyl_1508
            RBA: RB6950(dgkA)
            SYN: slr0054(dgkA)
            SYW: SYNW2314(dgkA)
            SYC: syc1114_d(dgkA)
            SYF: Synpcc7942_0401
            SYD: Syncc9605_2445
            SYE: Syncc9902_2127
            SYG: sync_2662(dgkA)
            SYR: SynRCC307_2245(dgkA)
            SYX: SynWH7803_2328(dgkA)
            CYA: CYA_1623(dgkA)
            CYB: CYB_1901(dgkA)
            TEL: tlr1586
            GVI: gll1242
            ANA: all0270
            AVA: Ava_2781
            PMA: Pro0208(dgkA)
            PMM: PMM0183(dgkA)
            PMT: PMT2066(dgkA)
            PMN: PMN2A_1551
            PMI: PMT9312_0185
            PMB: A9601_02011(dgkA)
            PMC: P9515_02121(dgkA)
            PMF: P9303_27411(dgkA)
            PMG: P9301_02031(dgkA)
            PME: NATL1_02591(dgkA)
            BFR: BF2165
            BFS: BF2222
            CHU: CHU_2581(dgkA)
            GFO: GFO_2181(dgkA)
            FPS: FP1593(dgkA)
            DRA: DR_2093
            DGE: Dgeo_1274
            TTH: TTC0682
            TTJ: TTHA1044
            TMA: TM0407
STRUCTURES  PDB: 1R79  1TUZ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.107
            ExPASy - ENZYME nomenclature database: 2.7.1.107
            ExplorEnz - The Enzyme Database: 2.7.1.107
            ERGO genome analysis and discovery system: 2.7.1.107
            BRENDA, the Enzyme Database: 2.7.1.107
            CAS: 60382-71-0
///
ENTRY       EC 2.7.1.108                Enzyme
NAME        dolichol kinase;
            dolichol phosphokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     CTP:dolichol O-phosphotransferase
REACTION    CTP + dolichol = CDP + dolichyl phosphate [RN:R01018]
ALL_REAC    R01018
SUBSTRATE   CTP [CPD:C00063];
            dolichol [CPD:C00381]
PRODUCT     CDP [CPD:C00112];
            dolichyl phosphate [CPD:C00110]
REFERENCE   1  [PMID:457672]
  AUTHORS   Burton WA, Scher MG, Waechter CJ.
  TITLE     Enzymatic phosphorylation of dolichol in central nervous tissue.
  JOURNAL   J. Biol. Chem. 254 (1979) 7129-36.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:6257336]
  AUTHORS   Rip JW, Carroll KK.
  TITLE     Properties of a dolichol phosphokinase activity associated with rat
            liver microsomes.
  JOURNAL   Can. J. Biochem. 58 (1980) 1051-6.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
ORTHOLOGY   KO: K00902  dolichol kinase
GENES       OSA: 4328285
            SCE: YMR013C(SEC59)
            AGO: AGOS_ABR051C
            PIC: PICST_58284(SEC59)
            CAL: CaO19_261(CaO19.261)
            CGR: CAGL0M07700g
            SPO: SPCC63.10c
            AFM: AFUA_4G09060
            AOR: AO090023000648
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.108
            ExPASy - ENZYME nomenclature database: 2.7.1.108
            ExplorEnz - The Enzyme Database: 2.7.1.108
            ERGO genome analysis and discovery system: 2.7.1.108
            BRENDA, the Enzyme Database: 2.7.1.108
            CAS: 71768-07-5
///
ENTRY       EC 2.7.1.109      Obsolete  Enzyme
NAME        Transferred to 2.7.11.31
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.31, [hydroxymethylglutaryl-CoA
            reductase (NADPH)] kinase (EC 2.7.1.109 created 1984, deleted 2005)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.109
            ExPASy - ENZYME nomenclature database: 2.7.1.109
            ExplorEnz - The Enzyme Database: 2.7.1.109
            ERGO genome analysis and discovery system: 2.7.1.109
            BRENDA, the Enzyme Database: 2.7.1.109
///
ENTRY       EC 2.7.1.110      Obsolete  Enzyme
NAME        Transferred to 2.7.11.3
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.3 dephospho-[reductase kinase]
            kinase (EC 2.7.1.110 created 1984, deleted 2005)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.110
            ExPASy - ENZYME nomenclature database: 2.7.1.110
            ExplorEnz - The Enzyme Database: 2.7.1.110
            ERGO genome analysis and discovery system: 2.7.1.110
            BRENDA, the Enzyme Database: 2.7.1.110
///
ENTRY       EC 2.7.1.111      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Deleted entry: Now listed as EC 2.7.11.27 [acetyl-CoA carboxylase]
            kinase (EC 2.7.1.111 created 1984, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.111
            ExPASy - ENZYME nomenclature database: 2.7.1.111
            ExplorEnz - The Enzyme Database: 2.7.1.111
            ERGO genome analysis and discovery system: 2.7.1.111
            BRENDA, the Enzyme Database: 2.7.1.111
///
ENTRY       EC 2.7.1.112      Obsolete  Enzyme
NAME        Transferred to 2.7.10.2
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.10.2 non-specific protein-tyrosine
            kinase (EC 2.7.1.112 created 1984, deleted 2005)
GENES       DME: Dmel_CG2272(slpr) Dmel_CG31127(Wsck) Dmel_CG31421(Takl1)
                 Dmel_CG33531(Ddr) Dmel_CG7186(SAK) Dmel_CG7749(fat2)
                 Dmel_CG8049(Btk29A) Dmel_CG8742(Gyc76C) Dmel_CG8874(Fps85D)
            PEN: PSEEN0365
            BXE: Bxe_A2242 Bxe_A2533 Bxe_A3850 Bxe_A3864 Bxe_B0507 Bxe_B1726
                 Bxe_B2255 Bxe_C1086
            SAL: Sala_1583
            DGE: Dgeo_0342
STRUCTURES  PDB: 1A07  1A08  1A09  1A0N  1A1A  1A1B  1A1C  1A1E  1A81  1AB2  
                 1ABO  1ABQ  1AD5  1AGW  1AOT  1AOU  1AVZ  1AWJ  1AWO  1AWW  
                 1AWX  1AZG  1B55  1BHF  1BHH  1BKL  1BKM  1BLJ  1BLK  1BTK  
                 1BU1  1BWN  1BYG  1CSK  1CSY  1CSZ  1CWE  1DJS  1EFN  1F1W  
                 1F2F  1FBZ  1FGI  1FGK  1FLT  1FMK  1FPU  1FVR  1FYN  1G83  
                 1GAG  1GJO  1GL5  1HE7  1I44  1IEP  1IGR  1II4  1IIJ  1IIL  
                 1IJR  1IR3  1IS0  1IVO  1J0W  1JEG  1JQH  1JU5  1JWO  1K04  
                 1K05  1K2P  1K3A  1K40  1K9A  1KC2  1KGY  1KIK  1KSW  1KTM  
                 1LCJ  1LCK  1LUF  1LUI  1LUK  1LUM  1LUN  1M14  1M17  1M27  
                 1M52  1M61  1M6B  1M7N  1MOX  1MP8  1MQB  1MW4  1N8Z  1NLO  
                 1NLP  1NUK  1NYF  1NYG  1NZL  1NZV  1O41  1O42  1O43  1O44  
                 1O45  1O46  1O47  1O48  1O49  1O4A  1O4B  1O4C  1O4D  1O4E  
                 1O4F  1O4G  1O4H  1O4I  1O4J  1O4K  1O4L  1O4M  1O4N  1O4O  
                 1O4P  1O4Q  1O4R  1OEC  1OPJ  1OPK  1OPL  1OW6  1OW7  1OW8  
                 1P13  1P14  1P4O  1PV3  1QLY  1QPC  1QPD  1QPE  1QPJ  1QVX  
                 1QWE  1QWF  1R0P  1R1W  1RHF  1RJA  1RJB  1RQQ  1S78  1SGG  
                 1SHA  1SHB  1SHF  1SKJ  1SM2  1SNU  1SNX  1T45  1T46  1U46  
                 1U4D  1U54  1U59  1UCV  1UEF  1VR2  1W1F  1WA7  1WQU  1WVZ  
                 1X27  1X5A  1X5L  1X6G  1X8B  1XBA  1XBB  1XBC  1XKK  1Y57  
                 1Y6A  1Y6B  1YI6  1YOJ  1YOL  1YOM  1YVJ  1YWN  1YY9  1Z57  
                 1Z9I  1ZBJ  1ZZP  2A91  2ABL  2AEH  2AHX  2AL6  2AUH  2B4S  
                 2B7A  2BBA  2BDF  2BDJ  2C0I  2C0O  2C0T  2C5D  2CR3  2D8J  
                 2DBJ  2DCR  2DJS  2ETM  2ETZ  2EU0  2EU9  2EXE  2F4J  2FCI  
                 2FDB  2FGI  2FO0  2G1T  2GE9  2HCK  2HR7  2J6M  2OJ2  2OJ9  
                 2PTK  2SRC  3HCK  3LCK  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.112
            ExPASy - ENZYME nomenclature database: 2.7.1.112
            ExplorEnz - The Enzyme Database: 2.7.1.112
            ERGO genome analysis and discovery system: 2.7.1.112
            BRENDA, the Enzyme Database: 2.7.1.112
///
ENTRY       EC 2.7.1.113                Enzyme
NAME        deoxyguanosine kinase;
            deoxyguanosine kinase (phosphorylating);
            (dihydroxypropoxymethyl)guanine kinase;
            2'-deoxyguanosine kinase;
            NTP-deoxyguanosine 5'-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:deoxyguanosine 5'-phosphotransferase
REACTION    ATP + deoxyguanosine = ADP + dGMP [RN:R01967]
ALL_REAC    R01967
SUBSTRATE   ATP [CPD:C00002];
            deoxyguanosine [CPD:C00330]
PRODUCT     ADP [CPD:C00008];
            dGMP [CPD:C00362]
COMMENT     Deoxyinosine can also act as acceptor.
REFERENCE   1  [PMID:6260206]
  AUTHORS   Barker J, Lewis RA.
  TITLE     Deoxyguanosine kinase of neonatal mouse skin tissue.
  JOURNAL   Biochim. Biophys. Acta. 658 (1981) 111-23.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:218928]
  AUTHORS   Gower WR Jr, Carr MC, Ives DH.
  TITLE     Deoxyguanosine kinase. Distinct molecular forms in mitochondria and
            cytosol.
  JOURNAL   J. Biol. Chem. 254 (1979) 2180-3.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K00904  deoxyguanosine kinase
GENES       HSA: 1716(DGUOK)
            MMU: 27369(Dguok)
            RNO: 297389(Dguok_predicted)
            CFA: 475791(DGUOK)
            TET: TTHERM_00498020
            ABO: ABO_0338
            CVI: CV_1634(dgk)
            RSO: RSc2629(RS00933)
            REU: Reut_A2779
            RME: Rmet_2916
            BMA: BMA2322
            BXE: Bxe_A3957
            BCN: Bcen_0272
            BAM: Bamb_0650
            BPS: BPSL2823
            BPM: BURPS1710b_3316
            BTE: BTH_I1312
            MPT: Mpe_A3017
            MMS: mma_2877
            NEU: NE0071
            NET: Neut_2294
            NMU: Nmul_A0880
            EBA: ebA7118
            TBD: Tbd_2052
            MFA: Mfla_0598
            ABA: Acid345_4748
            BCE: BC0021
            BCZ: BCZK0016(dgk)
            BTK: BT9727_0016(dgk)
            BTL: BALH_0016(dgk)
            BCL: ABC2889(dgk) ABC2890(dck)
            BPU: BPUM_0512
            SAA: SAUSA300_0542
            LMO: lmo1705
            LMF: LMOf2365_1729
            LIN: lin1817
            LWE: lwe1725
            LLA: L169971(dukB) L93481(dukA)
            LLC: LACR_0515 LACR_1279
            LLM: llmg_0480(dukA) llmg_1333(dukB)
            SPY: SPy_0121
            SPZ: M5005_Spy_0103
            SPM: spyM18_0121
            SPG: SpyM3_0094
            SPS: SPs0096
            SPH: MGAS10270_Spy0105
            SPI: MGAS10750_Spy0110
            SPJ: MGAS2096_Spy0106
            SPK: MGAS9429_Spy0104
            SPA: M6_Spy0152
            SPB: M28_Spy0101
            SAG: SAG1826
            SAN: gbs1867
            SAK: SAK_1846
            LPL: lp_1011(dgk1) lp_1329(dgk2)
            LJO: LJ1824 LJ1825
            LAC: LBA1949 LBA1950
            LSA: LSA1805(dgk)
            LSL: LSL_0514 LSL_1642
            LDB: Ldb2197(dgk)
            LBU: LBUL_2018
            LBR: LVIS_1520 LVIS_1711
            LCA: LSEI_1205
            EFA: EF0740
            OOE: OEOE_0437 OEOE_0849
            CPE: CPE0060(dgk2)
            CPF: CPF_0067
            CPR: CPR_0070(dgk2)
            MPU: MYPU_5520(dgk)
            MMY: MSC_0388
            MSY: MS53_0140(dgk) MS53_0380
            MFL: Mfl547
STRUCTURES  PDB: 2JAQ  2JAS  2JAT  2OCP  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.113
            ExPASy - ENZYME nomenclature database: 2.7.1.113
            ExplorEnz - The Enzyme Database: 2.7.1.113
            ERGO genome analysis and discovery system: 2.7.1.113
            BRENDA, the Enzyme Database: 2.7.1.113
            CAS: 39471-28-8
///
ENTRY       EC 2.7.1.114                Enzyme
NAME        AMP---thymidine kinase;
            adenylate-nucleoside phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     AMP:thymidine 5'-phosphotransferase
REACTION    AMP + thymidine = adenosine + thymidine 5'-phosphate [RN:R01571]
ALL_REAC    R01571
SUBSTRATE   AMP [CPD:C00020];
            thymidine [CPD:C00214]
PRODUCT     adenosine [CPD:C00212];
            thymidine 5'-phosphate [CPD:C00364]
COMMENT     The deoxypyrimidine kinase complex induced by Herpes simplex virus
            catalyses this reaction as well as those of EC 2.7.1.21 (thymidine
            kinase), EC 2.7.1.118 (ADP---thymidine kinase) and EC 2.7.4.9 (dTMP
            kinase).
REFERENCE   1  [PMID:6293576]
  AUTHORS   Falke D, Labenz J, Brauer D, Muller WE.
  TITLE     Adenosine diphosphate: thymidine 5'-phosphotransferase, a new enzyme
            activity, associated with the Herpes simplex virus-induced
            deoxypyrimidine kinase.
  JOURNAL   Biochim. Biophys. Acta. 708 (1982) 99-103.
  ORGANISM  Herpes simplex
REFERENCE   2  [PMID:6267178]
  AUTHORS   Falke D, Nehrbass W, Brauer D, Muller WE.
  TITLE     Adenylic acid: deoxythymidine 5'-phosphotransferase: evidence for
            the existence of a novel herpes simplex virus-induced enzyme.
  JOURNAL   J. Gen. Virol. 53 (1981) 247-55.
  ORGANISM  Herpes simplex
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.114
            ExPASy - ENZYME nomenclature database: 2.7.1.114
            ExplorEnz - The Enzyme Database: 2.7.1.114
            ERGO genome analysis and discovery system: 2.7.1.114
            BRENDA, the Enzyme Database: 2.7.1.114
            CAS: 60440-28-0
///
ENTRY       EC 2.7.1.115      Obsolete  Enzyme
NAME        Transferred to 2.7.11.4
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.4, [3-methyl-2-oxobutanoate
            dehydrogenase (acetyl-transferring)] kinase (EC 2.7.1.115 created
            1986, deleted 2005)
STRUCTURES  PDB: 1GJV  1GKX  1GKZ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.115
            ExPASy - ENZYME nomenclature database: 2.7.1.115
            ExplorEnz - The Enzyme Database: 2.7.1.115
            ERGO genome analysis and discovery system: 2.7.1.115
            BRENDA, the Enzyme Database: 2.7.1.115
///
ENTRY       EC 2.7.1.116      Obsolete  Enzyme
NAME        Transferred to 2.7.11.5
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.5, [isocitrate dehydrogenase
            (NADP+)] kinase. (EC 2.7.1.116 created 1986, deleted 2005)
GENES       BXE: Bxe_A4253
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.116
            ExPASy - ENZYME nomenclature database: 2.7.1.116
            ExplorEnz - The Enzyme Database: 2.7.1.116
            ERGO genome analysis and discovery system: 2.7.1.116
            BRENDA, the Enzyme Database: 2.7.1.116
///
ENTRY       EC 2.7.1.117      Obsolete  Enzyme
NAME        Transferred to 2.7.11.18
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.18 myosin-light-chain kinase (EC
            2.7.1.117 created 1986, deleted 2005)
GENES       DME: Dmel_CG1915(sls) Dmel_CG32019(bt)
STRUCTURES  PDB: 1TLK  1VRK  2CQV  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.117
            ExPASy - ENZYME nomenclature database: 2.7.1.117
            ExplorEnz - The Enzyme Database: 2.7.1.117
            ERGO genome analysis and discovery system: 2.7.1.117
            BRENDA, the Enzyme Database: 2.7.1.117
///
ENTRY       EC 2.7.1.118                Enzyme
NAME        ADP---thymidine kinase;
            ADP:dThd phosphotransferase;
            adenosine diphosphate-thymidine phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ADP:thymidine 5'-phosphotransferase
REACTION    ADP + thymidine = AMP + thymidine 5'-phosphate [RN:R01568]
ALL_REAC    R01568
SUBSTRATE   ADP [CPD:C00008];
            thymidine [CPD:C00214]
PRODUCT     AMP [CPD:C00020];
            thymidine 5'-phosphate [CPD:C00364]
COMMENT     The deoxypyrimidine kinase complex induced by Herpes simplex virus
            catalyses this reaction as well as those of EC 2.7.1.21 (thymidine
            kinase), EC 2.7.1.114 (AMP---thymidine kinase) and EC 2.7.4.9 (dTMP
            kinase).
REFERENCE   1  [PMID:6293576]
  AUTHORS   Falke D, Labenz J, Brauer D, Muller WE.
  TITLE     Adenosine diphosphate: thymidine 5'-phosphotransferase, a new enzyme
            activity, associated with the Herpes simplex virus-induced
            deoxypyrimidine kinase.
  JOURNAL   Biochim. Biophys. Acta. 708 (1982) 99-103.
  ORGANISM  Herpes simplex
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.118
            ExPASy - ENZYME nomenclature database: 2.7.1.118
            ExplorEnz - The Enzyme Database: 2.7.1.118
            ERGO genome analysis and discovery system: 2.7.1.118
            BRENDA, the Enzyme Database: 2.7.1.118
            CAS: 82114-39-4
///
ENTRY       EC 2.7.1.119                Enzyme
NAME        hygromycin-B kinase;
            hygromycin B phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:hygromycin-B 7"-O-phosphotransferase
REACTION    ATP + hygromycin B = ADP + 7"-O-phosphohygromycin [RN:R03770]
ALL_REAC    R03770
SUBSTRATE   ATP [CPD:C00002];
            hygromycin B [CPD:C01925]
PRODUCT     ADP [CPD:C00008];
            7''-O-phosphohygromycin [CPD:C03368]
COMMENT     Phosphorylates the antibiotics hygromycin B, 1-N-hygromycin B and
            destomycin, but not hygromycin B2, at the 7"-hydroxy group in the
            destomic acid ring.
REFERENCE   1  [PMID:3026811]
  AUTHORS   Zalacain M, Pardo JM, Jimenez A.
  TITLE     Purification and characterization of a hygromycin B
            phosphotransferase from Streptomyces hygroscopicus.
  JOURNAL   Eur. J. Biochem. 162 (1987) 419-22.
  ORGANISM  Streptomyces hygroscopicus
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.119
            ExPASy - ENZYME nomenclature database: 2.7.1.119
            ExplorEnz - The Enzyme Database: 2.7.1.119
            ERGO genome analysis and discovery system: 2.7.1.119
            BRENDA, the Enzyme Database: 2.7.1.119
            CAS: 88361-67-5
///
ENTRY       EC 2.7.1.120      Obsolete  Enzyme
NAME        Transferred to 2.7.11.17
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.17 Ca2+/calmodulin-dependent
            protein kinase (EC 2.7.1.120 created 1989, modified 1990, deleted
            2005)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.120
            ExPASy - ENZYME nomenclature database: 2.7.1.120
            ExplorEnz - The Enzyme Database: 2.7.1.120
            ERGO genome analysis and discovery system: 2.7.1.120
            BRENDA, the Enzyme Database: 2.7.1.120
///
ENTRY       EC 2.7.1.121                Enzyme
NAME        phosphoenolpyruvate-glycerone phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     phosphoenolpyruvate:glycerone phosphotransferase
REACTION    phosphoenolpyruvate + glycerone = pyruvate + glycerone phosphate
            [RN:R01012]
ALL_REAC    R01012
SUBSTRATE   phosphoenolpyruvate [CPD:C00074];
            glycerone [CPD:C00184]
PRODUCT     pyruvate [CPD:C00022];
            glycerone phosphate [CPD:C00111]
REFERENCE   1  [PMID:6368745]
  AUTHORS   Jin RZ, Lin EC.
  TITLE     An inducible phosphoenolpyruvate: dihydroxyacetone
            phosphotransferase system in Escherichia coli.
  JOURNAL   J. Gen. Microbiol. 130 (1984) 83-8.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.121
            ExPASy - ENZYME nomenclature database: 2.7.1.121
            ExplorEnz - The Enzyme Database: 2.7.1.121
            ERGO genome analysis and discovery system: 2.7.1.121
            BRENDA, the Enzyme Database: 2.7.1.121
            CAS: 91755-81-6
///
ENTRY       EC 2.7.1.122                Enzyme
NAME        xylitol kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:xylitol 5-phosphotransferase
REACTION    ATP + xylitol = ADP + xylitol 5-phosphate [RN:R02136]
ALL_REAC    R02136
SUBSTRATE   ATP [CPD:C00002];
            xylitol [CPD:C00379]
PRODUCT     ADP [CPD:C00008];
            xylitol 5-phosphate [CPD:C02895]
REFERENCE   1  [PMID:6730972]
  AUTHORS   Assev S, Rolla G.
  TITLE     Evidence for presence of a xylitol phosphotransferase system in
            Streptococcus mutans OMZ 176.
  JOURNAL   Acta. Pathol. Microbiol. Immunol. Scand. [B]. 92 (1984) 89-92.
  ORGANISM  Streptococcus mutans [GN:smu]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.122
            ExPASy - ENZYME nomenclature database: 2.7.1.122
            ExplorEnz - The Enzyme Database: 2.7.1.122
            ERGO genome analysis and discovery system: 2.7.1.122
            BRENDA, the Enzyme Database: 2.7.1.122
            CAS: 91273-86-8
///
ENTRY       EC 2.7.1.123      Obsolete  Enzyme
NAME        Transferred to 2.7.11.17
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.17, Ca2+/calmodulin-dependent
            protein kinase (EC 2.7.1.123 created 1989, deleted 2005)
GENES       DME: Dmel_CG1495(CaMKI)
STRUCTURES  PDB: 1A06  1CM1  1CM4  1HKX  1MXE  2UX0  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.123
            ExPASy - ENZYME nomenclature database: 2.7.1.123
            ExplorEnz - The Enzyme Database: 2.7.1.123
            ERGO genome analysis and discovery system: 2.7.1.123
            BRENDA, the Enzyme Database: 2.7.1.123
///
ENTRY       EC 2.7.1.124      Obsolete  Enzyme
NAME        Transferred to 2.7.11.6
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.6, [tyrosine 3-monooxygenase]
            kinase (EC 2.7.1.124 created 1989, deleted 2005)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.124
            ExPASy - ENZYME nomenclature database: 2.7.1.124
            ExplorEnz - The Enzyme Database: 2.7.1.124
            ERGO genome analysis and discovery system: 2.7.1.124
            BRENDA, the Enzyme Database: 2.7.1.124
///
ENTRY       EC 2.7.1.125      Obsolete  Enzyme
NAME        Transferred to 2.7.11.14
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.14 rhodopsin kinase (EC 2.7.1.125
            created 1989 (EC 2.7.1.97 created 1978, incorporated 1992), deleted
            2005)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.125
            ExPASy - ENZYME nomenclature database: 2.7.1.125
            ExplorEnz - The Enzyme Database: 2.7.1.125
            ERGO genome analysis and discovery system: 2.7.1.125
            BRENDA, the Enzyme Database: 2.7.1.125
///
ENTRY       EC 2.7.1.126      Obsolete  Enzyme
NAME        Transferred to 2.7.11.15
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.15 beta-adrenergic-receptor kinase
            (EC 2.7.1.126 created 1989, deleted 2005)
STRUCTURES  PDB: 1BAK  1OMW  1YM7  2BCJ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.126
            ExPASy - ENZYME nomenclature database: 2.7.1.126
            ExplorEnz - The Enzyme Database: 2.7.1.126
            ERGO genome analysis and discovery system: 2.7.1.126
            BRENDA, the Enzyme Database: 2.7.1.126
///
ENTRY       EC 2.7.1.127                Enzyme
NAME        inositol-trisphosphate 3-kinase;
            1D-myo-inositol-trisphosphate 3-kinase;
            Ins(1,4,5)P3 3-kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:1D-myo-inositol-1,4,5-trisphosphate 3-phosphotransferase
REACTION    ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol
            1,3,4,5-tetrakisphosphate [RN:R03433]
ALL_REAC    R03433
SUBSTRATE   ATP [CPD:C00002];
            1D-myo-inositol 1,4,5-trisphosphate [CPD:C01245]
PRODUCT     ADP [CPD:C00008];
            1D-myo-inositol 1,3,4,5-tetrakisphosphate [CPD:C01272]
EFFECTOR    Calcium [CPD:C00076]
COMMENT     Activated by Ca2+. Three isoforms have been shown to exist [3].
REFERENCE   1  [PMID:3487541]
  AUTHORS   Hansen CA, Mah S, Williamson JR.
  TITLE     Formation and metabolism of inositol 1,3,4,5-tetrakisphosphate in
            liver.
  JOURNAL   J. Biol. Chem. 261 (1986) 8100-3.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:3010126]
  AUTHORS   Irvine RF, Letcher AJ, Heslop JP, Berridge MJ.
  TITLE     The inositol tris/tetrakisphosphate pathway--demonstration of
            Ins(1,4,5)P3 3-kinase activity in animal tissues.
  JOURNAL   Nature. 320 (1986) 631-4.
REFERENCE   3  [PMID:11331907]
  AUTHORS   Irvine RF, Schell MJ.
  TITLE     Back in the water: the return of the inositol phosphates.
  JOURNAL   Nat. Rev. Mol. Cell. Biol. 2 (2001) 327-38.
PATHWAY     PATH: map00562  Inositol phosphate metabolism
            PATH: map04020  Calcium signaling pathway
            PATH: map04070  Phosphatidylinositol signaling system
ORTHOLOGY   KO: K00911  1D-myo-inositol-triphosphate 3-kinase
GENES       HSA: 3706(ITPKA) 3707(ITPKB)
            MMU: 228550(Itpka) 320404(Itpkb)
            RNO: 54260(Itpkb) 81677(Itpka)
            CFA: 487507(ITPKA) 490383(ITPKB)
            GGA: 395694(ITPKA) 416743(ITPKB)
            DME: Dmel_CG13688(Ipk2) Dmel_CG1630(IP3K2) Dmel_CG4026(IP3K1)
STRUCTURES  PDB: 1TZD  2A98  2AQX  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.127
            ExPASy - ENZYME nomenclature database: 2.7.1.127
            ExplorEnz - The Enzyme Database: 2.7.1.127
            ERGO genome analysis and discovery system: 2.7.1.127
            BRENDA, the Enzyme Database: 2.7.1.127
            CAS: 106283-10-7
///
ENTRY       EC 2.7.1.128      Obsolete  Enzyme
NAME        Transferred to 2.7.11.27
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.27 [acetyl-CoA carboxylase] kinase
            (EC 2.7.1.128 created 1990 (EC 2.7.1.111 created 1984, incorporated
            1992), deleted 2005)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.128
            ExPASy - ENZYME nomenclature database: 2.7.1.128
            ExplorEnz - The Enzyme Database: 2.7.1.128
            ERGO genome analysis and discovery system: 2.7.1.128
            BRENDA, the Enzyme Database: 2.7.1.128
///
ENTRY       EC 2.7.1.129      Obsolete  Enzyme
NAME        Transferred to 2.7.11.7
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.7 myosin-heavy-chain kinase. (EC
            2.7.1.129 created 1990, deleted 2005)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.129
            ExPASy - ENZYME nomenclature database: 2.7.1.129
            ExplorEnz - The Enzyme Database: 2.7.1.129
            ERGO genome analysis and discovery system: 2.7.1.129
            BRENDA, the Enzyme Database: 2.7.1.129
///
ENTRY       EC 2.7.1.130                Enzyme
NAME        tetraacyldisaccharide 4'-kinase;
            lipid-A 4'-kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-beta-D
            -1,6-glucosaminyl-beta-phosphate 4'-O-phosphotransferase
REACTION    ATP +
            [2-N,3-O-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl]-(1->6)-[2-
            N,3-O-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl phosphate] =
            ADP +
            [2-N,3-O-bis(3-hydroxytetradecanoyl)-4-O-phosphono-beta-D-
            glucosaminyl]-(1->6)-[2-N,3-O-bis(3-hydroxytetradecanoyl)-beta-D-
            glucosaminyl phosphate] [RN:R04657]
ALL_REAC    R04657
SUBSTRATE   ATP [CPD:C00002];
            [2-N,3-O-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl]-(1->6)-[2-
            N,3-O-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl phosphate]
PRODUCT     ADP [CPD:C00008];
            [2-N,3-O-bis(3-hydroxytetradecanoyl)-4-O-phosphono-beta-D-
            glucosaminyl]-(1->6)-[2-N,3-O-bis(3-hydroxytetradecanoyl)-beta-D-
            glucosaminyl phosphate]
COMMENT     Involved with EC 2.3.1.129 (acyl-[acyl-carrier-
            protein]---UDP-N-acetylglucosamine O-acyltransferase) and EC
            2.4.1.182 (lipid-A-disaccharide synthase) in the biosynthesis of the
            phosphorylated glycolipid, lipid A, in the outer membrane of
            Escherichia coli.
REFERENCE   1  [PMID:3027079]
  AUTHORS   Ray BL, Raetz CR.
  TITLE     The biosynthesis of gram-negative endotoxin. A novel kinase in
            Escherichia coli membranes that incorporates the 4'-phosphate of
            lipid A.
  JOURNAL   J. Biol. Chem. 262 (1987) 1122-8.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00540  Lipopolysaccharide biosynthesis
ORTHOLOGY   KO: K00912  tetraacyldisaccharide 4'-kinase
GENES       ECO: b0915(lpxK)
            ECJ: JW0898(lpxK)
            ECE: Z1261(ycaH)
            ECS: ECs0998
            ECI: UTI89_C0986(lpxK)
            ECP: ECP_0926
            ECV: APECO1_27(lpxK)
            ECW: EcE24377A_1013(lpxK)
            ECX: EcHS_A1022(lpxK)
            STY: STY0986(ycaH)
            STT: t1949(lpxK)
            SPT: SPA1813(lpxK)
            SEC: SC0942(lpxK)
            STM: STM0985(lpxK)
            YPE: YPO1396(lpxK)
            YPK: y2776
            YPM: YP_1197(lpxK)
            YPA: YPA_0687
            YPN: YPN_2581
            YPP: YPDSF_2299
            YPS: YPTB1421(lpxK)
            YPI: YpsIP31758_2576(lpxK)
            YEN: YE1544(lpxK)
            SFL: SF0911(lpxK)
            SFX: S0975(ycaH)
            SFV: SFV_0916(ycaH)
            SSN: SSON_0917(ycaH)
            SBO: SBO_2203(ycaH)
            SDY: SDY_2343(ycaH)
            ECA: ECA2556(lpxK)
            PLU: plu1631(lpxK)
            WBR: WGLp253(ycaH)
            SGL: SG0996
            ENT: Ent638_1434
            SPE: Spro_1713
            BFL: Bfl378(lpxK)
            BPN: BPEN_389(lpxK)
            HIN: HI0059
            HIT: NTHI0069(lpxK)
            HIP: CGSHiEE_03005(lpxK)
            HIQ: CGSHiGG_02805(lpxK)
            HDU: HD0217(lpxK)
            HSO: HS_0656(lpxK)
            PMU: PM0860(lpxK)
            MSU: MS0933(lpxK)
            APL: APL_1278(lpxK)
            ASU: Asuc_1727
            XFA: XF1082
            XFT: PD0362(lpxK)
            XCC: XCC2119(lpxK)
            XCB: XC_1996
            XCV: XCV2255(lpxK)
            XAC: XAC2088(lpxK)
            XOO: XOO2296(lpxK)
            XOM: XOO_2174(XOO2174)
            VCH: VC1877
            VCO: VC0395_A1468(lpxK)
            VVU: VV1_2086
            VVY: VV2355
            VPA: VP0983
            VFI: VFA0425
            PPR: PBPRA2384(ycaH)
            PAE: PA2981(lpxK)
            PAU: PA14_25510(lpxK)
            PAP: PSPA7_2180(lpxK)
            PPU: PP_1900(lpxK)
            PPF: Pput_3814
            PST: PSPTO_3845(lpxK)
            PSB: Psyr_1635(lpxK)
            PSP: PSPPH_1628(lpxK)
            PFL: PFL_1778(lpxK)
            PFO: Pfl_4175(lpxK)
            PEN: PSEEN1603(lpxK)
            PMY: Pmen_1614
            PAR: Psyc_1315(lpxK)
            PCR: Pcryo_1063
            PRW: PsycPRwf_1394
            ACI: ACIAD2363(lpxK)
            SON: SO_2801(lpxK)
            SDN: Sden_2198
            SFR: Sfri_2387
            SAZ: Sama_1338
            SBL: Sbal_1684
            SBM: Shew185_1669
            SLO: Shew_1639
            SPC: Sputcn32_1558
            SSE: Ssed_2825
            SPL: Spea_1771
            SHE: Shewmr4_2421
            SHM: Shewmr7_2491
            SHN: Shewana3_2583
            SHW: Sputw3181_2541
            ILO: IL1512(lpxK)
            CPS: CPS_2126(lpxK)
            PHA: PSHAa1660(lpxK)
            PAT: Patl_1781
            SDE: Sde_2059
            PIN: Ping_0901
            MAQ: Maqu_1740
            CBU: CBU_0857(lpxK)
            CBD: COXBU7E912_0923(lpxK)
            LPN: lpg1818
            LPF: lpl1782(lpxK)
            LPP: lpp1781(lpxK)
            MCA: MCA0633(lpxK)
            FTU: FTT0110(valB)
            FTF: FTF0110(lpxK)
            FTW: FTW_0195(lpxK)
            FTL: FTL_1667
            FTH: FTH_1608(lpxK)
            FTA: FTA_1764(lpxK)
            FTN: FTN_1605(lpxK)
            TCX: Tcr_0958
            NOC: Noc_2676
            AEH: Mlg_1434
            HHA: Hhal_1245
            HCH: HCH_02704(lpxK)
            CSA: Csal_1587
            ABO: ABO_1056(lpxK)
            MMW: Mmwyl1_2152
            AHA: AHA_2777(lpxK)
            DNO: DNO_0843(lpxK)
            RMA: Rmag_0843
            VOK: COSY_0768(lpxK)
            NME: NMB0672
            NMA: NMA0872(lpxK)
            NGO: NGO0242
            CVI: CV_3346(lpxK)
            RSO: RSc2530(lpxK)
            REU: Reut_A0593
            REH: H16_A0606(lpxK)
            RME: Rmet_0535
            BMA: BMA2273(lpxK)
            BMV: BMASAVP1_A0569(lpxK)
            BML: BMA10299_A1046(lpxK)
            BMN: BMA10247_2151(lpxK)
            BXE: Bxe_A0766
            BVI: Bcep1808_2638
            BUR: Bcep18194_A5876
            BCN: Bcen_1933
            BCH: Bcen2424_2545
            BAM: Bamb_2593
            BPS: BPSL0878
            BPM: BURPS1710b_1083(lpxK)
            BPL: BURPS1106A_0930(lpxK)
            BPD: BURPS668_0927(lpxK)
            BTE: BTH_I0742(lpxK)
            PNU: Pnuc_0284
            BPE: BP2766
            BPA: BPP2563
            BBR: BB2008
            RFR: Rfer_3155
            POL: Bpro_2949
            PNA: Pnap_1923
            AAV: Aave_2564
            AJS: Ajs_2305
            VEI: Veis_4893
            MPT: Mpe_A2485
            HAR: HEAR2490(lpxK)
            MMS: mma_2579(lpxK)
            NEU: NE2164(lpxK)
            NET: Neut_2110
            EBA: ebA5085(lpxK)
            AZO: azo1470(lpxK)
            DAR: Daro_3208
            TBD: Tbd_1508
            MFA: Mfla_2089
            HPY: HP0328
            HPJ: jhp0311(lpxK)
            HPA: HPAG1_0332
            HHE: HH1009(lpxK)
            HAC: Hac_0992(lpxK)
            WSU: WS0204
            TDN: Tmden_0853
            CJE: Cj0811(lpxK)
            CJR: CJE0902(lpxK)
            CJJ: CJJ81176_0832(lpxK)
            CJU: C8J_0762(lpxK)
            CJD: JJD26997_1199(lpxK)
            CFF: CFF8240_1080(lpxK)
            CCV: CCV52592_0127(lpxK)
            CHA: CHAB381_1023(lpxK)
            ABU: Abu_1248(lpxK)
            NIS: NIS_1043
            SUN: SUN_1629
            GSU: GSU2258(lpxK)
            GME: Gmet_2347
            GUR: Gura_3228
            PCA: Pcar_1261
            PPD: Ppro_3028
            DVU: DVU2468(lpxK)
            DVL: Dvul_0773
            DDE: Dde_2600
            LIP: LI0595(lpxK)
            BBA: Bd1499(lpxK)
            DPS: DP1938(lpxK)
            ADE: Adeh_2613
            AFW: Anae109_2580
            MXA: MXAN_4711(lpxK)
            SAT: SYN_01563
            SFU: Sfum_0346
            RPR: RP719
            RTY: RT0705(lpxK)
            RCO: RC1092(lpxK)
            RFE: RF_0196(lpxK)
            RBE: RBE_0185(lpxK)
            RAK: A1C_05575(lpxK)
            RBO: A1I_06945(lpxK)
            RCM: A1E_04705(lpxK)
            RRI: A1G_06070(lpxK)
            PUB: SAR11_0149(lpxK)
            MLO: mlr8270
            MES: Meso_0439
            PLA: Plav_0624
            SME: SMc00892(lpxK)
            SMD: Smed_0426
            ATU: Atu0697(lpxK)
            ATC: AGR_C_1257
            RET: RHE_CH00846(lpxK)
            RLE: RL0904(lpxK)
            BME: BMEII1028
            BMF: BAB2_0210(lpxK)
            BMS: BRA0216(lpxK)
            BMB: BruAb2_0212(lpxK)
            BOV: BOV_A0196(lpxK)
            OAN: Oant_3047
            BJA: bll7514(lpxK)
            BRA: BRADO6095(lpxK)
            BBT: BBta_1692(lpxK)
            RPA: RPA1159(lpxK)
            RPB: RPB_1856
            RPC: RPC_4704
            RPD: RPD_4108
            RPE: RPE_0881
            NWI: Nwi_2555
            NHA: Nham_3177
            BHE: BH02670(lpxK)
            BQU: BQ02550(lpxK)
            BBK: BARBAKC583_1203(lpxK)
            XAU: Xaut_1481
            CCR: CC_0301
            SIL: SPO3445(lpxK)
            SIT: TM1040_2642
            RSP: RSP_1462(lpxK)
            RSH: Rsph17029_0113
            RSQ: Rsph17025_0060
            JAN: Jann_0399
            RDE: RD1_0294(lpxK)
            PDE: Pden_2094
            MMR: Mmar10_0632
            HNE: HNE_0700(lpxK)
            GOX: GOX1984
            GBE: GbCGDNIH1_2244
            ACR: Acry_0650
            RRU: Rru_A0582
            MGM: Mmc1_0926
            ABA: Acid345_4719
            SUS: Acid_6497
            FNU: FN1130
            RBA: RB7300(lpxK)
            CTR: CT402(lpxK)
            CTA: CTA_0437(lpxK)
            CMU: TC0682
            CPN: CPn0529(ycaH)
            CPA: CP0223
            CPJ: CPj0529(ycaH)
            CPT: CpB0550(ycaH)
            CCA: CCA00216(lpxK)
            CAB: CAB211
            CFE: CF0791(ycaH)
            PCU: pc1786(lpxK)
            LIL: LA3695(lpxK)
            LIC: LIC10531(lpxK)
            LBJ: LBJ_2673(lpxK)
            LBL: LBL_0399(lpxK)
            BTH: BT_1880
            BFR: BF3452
            BFS: BF3273
            PGI: PG0638(lpxK)
            CHU: CHU_1804(lpxK)
            GFO: GFO_2706(lpxK)
            FJO: Fjoh_0230
            FPS: FP1473(lpxK)
            CTE: CT1676(lpxK)
            CCH: Cag_0169
            CPH: Cpha266_0526
            PVI: Cvib_1444
            PLT: Plut_1655
            AAE: aq_1656
STRUCTURES  PDB: 2HF1  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.130
            ExPASy - ENZYME nomenclature database: 2.7.1.130
            ExplorEnz - The Enzyme Database: 2.7.1.130
            ERGO genome analysis and discovery system: 2.7.1.130
            BRENDA, the Enzyme Database: 2.7.1.130
            CAS: 107309-06-8
///
ENTRY       EC 2.7.1.131      Obsolete  Enzyme
NAME        Transferred to 2.7.11.29
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.29 low-density-lipoprotein receptor
            kinase (EC 2.7.1.131 created 1990, deleted 2005)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.131
            ExPASy - ENZYME nomenclature database: 2.7.1.131
            ExplorEnz - The Enzyme Database: 2.7.1.131
            ERGO genome analysis and discovery system: 2.7.1.131
            BRENDA, the Enzyme Database: 2.7.1.131
///
ENTRY       EC 2.7.1.132      Obsolete  Enzyme
NAME        Transferred to 2.7.11.28
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.28 tropomyosin kinase (EC 2.7.1.132
            created 1990, deleted 2005)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.132
            ExPASy - ENZYME nomenclature database: 2.7.1.132
            ExplorEnz - The Enzyme Database: 2.7.1.132
            ERGO genome analysis and discovery system: 2.7.1.132
            BRENDA, the Enzyme Database: 2.7.1.132
///
ENTRY       EC 2.7.1.133      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Deleted entry: inositol-trisphosphate 6-kinase. Now included with EC
            2.7.1.134, inositol-tetrakisphosphate 1-kinase (EC 2.7.1.133 created
            1990, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.133
            ExPASy - ENZYME nomenclature database: 2.7.1.133
            ExplorEnz - The Enzyme Database: 2.7.1.133
            ERGO genome analysis and discovery system: 2.7.1.133
            BRENDA, the Enzyme Database: 2.7.1.133
///
ENTRY       EC 2.7.1.134                Enzyme
NAME        inositol-tetrakisphosphate 1-kinase;
            1D-myo-inositol-tetrakisphosphate 1-kinase;
            inositol-trisphosphate 6-kinase;
            1D-myo-inositol-trisphosphate 6-kinase;
            ATP:1D-myo-inositol-1,3,4-trisphosphate 6-phosphotransferase;
            inositol-trisphosphate 5-kinase;
            1D-myo-inositol-trisphosphate 5-kinase;
            ATP:1D-myo-inositol-1,3,4-trisphosphate 5-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:1D-myo-inositol-3,4,5,6-tetrakisphosphate 1-phosphotransferase
REACTION    ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate = ADP +
            1D-myo-inositol 1,3,4,5,6-pentakisphosphate [RN:R03479]
ALL_REAC    R03479;
            (other) R03428 R03429
SUBSTRATE   ATP [CPD:C00002];
            1D-myo-inositol 3,4,5,6-tetrakisphosphate [CPD:C04520]
PRODUCT     ADP [CPD:C00008];
            1D-myo-inositol 1,3,4,5,6-pentakisphosphate [CPD:C01284]
COMMENT     This enzyme also phosphorylates Ins(1,3,4)P3 on O-5 and O-6. The
            phosphotransfer from ATP to either inositol 1,3,4-trisphosphate or
            inositol 3,4,5,6-tetrakisphosphate appears to be freely reversible
            to the extent that the enzyme can act like an inositol polyphosphate
            phosphatase in the presence of ADP. It can also catalyse an
            isomerization between Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 in the
            presence of ADP.
REFERENCE   1  [PMID:2829850]
  AUTHORS   Stephens LR, Hawkins PT, Morris AJ, Downes PC.
  TITLE     L-myo-inositol 1,4,5,6-tetrakisphosphate (3-hydroxy)kinase.
  JOURNAL   Biochem. J. 249 (1988) 283-92.
  ORGANISM  rat [GN:rno], mouse [GN:mmu]
REFERENCE   2  [PMID:3497156]
  AUTHORS   Balla T, Guillemette G, Baukal AJ, Catt KJ.
  TITLE     Metabolism of inositol 1,3,4-trisphosphate to a new
            tetrakisphosphate isomer in angiotensin-stimulated adrenal
            glomerulosa cells.
  JOURNAL   J. Biol. Chem. 262 (1987) 9952-5.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:2823793]
  AUTHORS   Shears SB, Parry JB, Tang EK, Irvine RF, Michell RH, Kirk CJ.
  TITLE     Metabolism of D-myo-inositol 1,3,4,5-tetrakisphosphate by rat liver,
            including the synthesis of a novel isomer of myo-inositol
            tetrakisphosphate.
  JOURNAL   Biochem. J. 246 (1987) 139-47.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:2584198]
  AUTHORS   Shears SB.
  TITLE     The pathway of myo-inositol 1,3,4-trisphosphate phosphorylation in
            liver. Identification of myo-inositol 1,3,4-trisphosphate 6-kinase,
            myo-inositol 1,3,4-trisphosphate 5-kinase, and myo-inositol
            1,3,4,6-tetrakisphosphate 5-kinase.
  JOURNAL   J. Biol. Chem. 264 (1989) 19879-86.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:11042108]
  AUTHORS   Yang X, Shears SB.
  TITLE     Multitasking in signal transduction by a promiscuous human
            Ins(3,4,5,6)P(4) 1-kinase/Ins(1,3,4)P(3) 5/6-kinase.
  JOURNAL   Biochem. J. 351 Pt 3 (2000) 551-5.
  ORGANISM  human [GN:hsa]
REFERENCE   6  [PMID:11909533]
  AUTHORS   Ho MW, Yang X, Carew MA, Zhang T, Hua L, Kwon YU, Chung SK, Adelt S,
            Vogel G, Riley AM, Potter BV, Shears SB.
  TITLE     Regulation of Ins(3,4,5,6)P(4) signaling by a reversible
            kinase/phosphatase.
  JOURNAL   Curr. Biol. 12 (2002) 477-82.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00562  Inositol phosphate metabolism
            PATH: map04070  Phosphatidylinositol signaling system
ORTHOLOGY   KO: K00913  1D-myo-Inositol-trisphosphate 6-kinase
GENES       HSA: 3705(ITPK1)
            MMU: 217837(Itpk1)
            BTA: 518488(LOC518488)
            GGA: 423421(ITPK1)
            XLA: 379828(itpk1)
            XTR: 549890(itpk1)
            DRE: 406290(itpk1)
            SPU: 580408(LOC580408)
            TET: TTHERM_00530360
            EHI: 151.t00008
STRUCTURES  PDB: 2ODT  2Q7D  2QB5  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.134
            ExPASy - ENZYME nomenclature database: 2.7.1.134
            ExplorEnz - The Enzyme Database: 2.7.1.134
            ERGO genome analysis and discovery system: 2.7.1.134
            BRENDA, the Enzyme Database: 2.7.1.134
///
ENTRY       EC 2.7.1.135      Obsolete  Enzyme
NAME        Transferred to 2.7.11.26
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.26 tau-protein kinase (EC 2.7.1.135
            created 1990, deleted 2005)
GENES       DME: Dmel_CG8201(par-1)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.135
            ExPASy - ENZYME nomenclature database: 2.7.1.135
            ExplorEnz - The Enzyme Database: 2.7.1.135
            ERGO genome analysis and discovery system: 2.7.1.135
            BRENDA, the Enzyme Database: 2.7.1.135
///
ENTRY       EC 2.7.1.136                Enzyme
NAME        macrolide 2'-kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:macrolide 2'-O-phosphotransferase
REACTION    ATP + oleandomycin = ADP + oleandomycin 2'-O-phosphate [RN:R03780]
ALL_REAC    R03780
SUBSTRATE   ATP [CPD:C00002];
            oleandomycin [CPD:C01946]
PRODUCT     ADP [CPD:C00008];
            oleandomycin 2'-O-phosphate [CPD:C03796]
COMMENT     Erythromycin, spiramycin and some other macrolide antibiotics can
            also act as acceptors.
REFERENCE   1  [PMID:3042731]
  AUTHORS   O'Hara K, Kanda T, Kono M.
  TITLE     Structure of a phosphorylated derivative of oleandomycin, obtained
            by reaction of oleandomycin with an extract of an
            erythromycin-resistant strain of Escherichia coli.
  JOURNAL   J. Antibiot. (Tokyo). 41 (1988) 823-7.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.136
            ExPASy - ENZYME nomenclature database: 2.7.1.136
            ExplorEnz - The Enzyme Database: 2.7.1.136
            ERGO genome analysis and discovery system: 2.7.1.136
            BRENDA, the Enzyme Database: 2.7.1.136
            CAS: 116036-69-2
///
ENTRY       EC 2.7.1.137                Enzyme
NAME        phosphatidylinositol 3-kinase;
            1-phosphatidylinositol 3-kinase;
            type III phosphoinositide 3-kinase;
            Vps34p;
            type I phosphatidylinositol kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:1-phosphatidyl-1D-myo-inositol 3-phosphotransferase
REACTION    ATP + 1-phosphatidyl-1D-myo-inositol = ADP +
            1-phosphatidyl-1D-myo-inositol 3-phosphate [RN:R03362]
ALL_REAC    R03362
SUBSTRATE   ATP [CPD:C00002];
            1-phosphatidyl-1D-myo-inositol [CPD:C01194]
PRODUCT     ADP [CPD:C00008];
            1-phosphatidyl-1D-myo-inositol 3-phosphate [CPD:C04549]
COMMENT     One mammalian isoform is known.
REFERENCE   1  [PMID:2833705]
  AUTHORS   Whitman M, Downes CP, Keeler M, Keller T, Cantley L.
  TITLE     Type I phosphatidylinositol kinase makes a novel inositol
            phospholipid, phosphatidylinositol-3-phosphate.
  JOURNAL   Nature. 332 (1988) 644-6.
REFERENCE   2  [PMID:11395417]
  AUTHORS   Vanhaesebroeck B, Leevers SJ, Ahmadi K, Timms J, Katso R, Driscoll
            PC, Woscholski R, Parker PJ, Waterfield MD.
  TITLE     Synthesis and function of 3-phosphorylated inositol lipids.
  JOURNAL   Annu. Rev. Biochem. 70 (2001) 535-602.
  ORGANISM  mammalian, Drosophila melanogaster [GN:dme], Caenorhabditis elegans
            [GN:cel], Dictyostelium discoideum [GN:ddi]
PATHWAY     PATH: map00562  Inositol phosphate metabolism
            PATH: map04070  Phosphatidylinositol signaling system
            PATH: map04140  Regulation of autophagy
ORTHOLOGY   KO: K00914  phosphatidylinositol 3-kinase
GENES       HSA: 5289(PIK3C3)
            PTR: 455385(PIK3C3)
            MMU: 225326(Pik3c3)
            RNO: 65052(Pik3c3)
            CFA: 490477(PIK3C3)
            BTA: 534815(MGC139319)
            SSC: 503700(PIK3C3)
            XLA: 446671(pik3c3)
            DRE: 548346(pik3c3)
            SPU: 591736(LOC591736)
            DME: Dmel_CG2699 Dmel_CG4141 Dmel_CG5373(Pi3K59F)
                 Dmel_CG6827(Nrx-IV)
            CEL: B0025.1(vps-34) B0334.8(age-1)
            ATH: AT1G60490(ATVPS34)
            OSA: 4337982
            CME: CMR018C
            SCE: YJR066W(TOR1) YKL203C(TOR2) YLR240W(VPS34)
            AGO: AGOS_AFR420W AGOS_AGL113C
            PIC: PICST_33151(TOR2) PICST_42745(VPS34) PICST_59212(TEL1)
            CAL: CaO19.1283(mec1)
            CGR: CAGL0G08360g
            SPO: SPAC458.05(vps34) SPBC30D10.10c SPBC646.01c
            ANI: AN4709.2
            AFM: AFUA_5G08670
            AOR: AO090020000426
            CNE: CNB03120 CNF03740
            UMA: UM00453.1
            DDI: DDB_0214908(tor) DDB_0219939(pikE)
            PFA: PFE0765w
            CPV: cgd6_1760
            CHO: Chro.60213
            TET: TTHERM_00203010 TTHERM_00649380
            TBR: Tb11.01.6980 Tb927.1.1930 Tb927.4.420 Tb927.8.6210
            TCR: 506425.80 509989.10 511903.160
            LMA: LmjF20.1120 LmjF24.2010 LmjF30.1850
            EHI: 22.t00010 6.t00051 67.t00015 9.t00048
            BTE: BTH_I2762
STRUCTURES  PDB: 1E7U  1E7V  1E8W  1E8X  1E8Y  1E8Z  1E90  1HE8  1PIC  1PKS  
                 1PKT  1W1N  2CHW  2CHX  2CHZ  2IWL  2PNA  2PNB  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.137
            ExPASy - ENZYME nomenclature database: 2.7.1.137
            ExplorEnz - The Enzyme Database: 2.7.1.137
            ERGO genome analysis and discovery system: 2.7.1.137
            BRENDA, the Enzyme Database: 2.7.1.137
            CAS: 115926-52-8
///
ENTRY       EC 2.7.1.138                Enzyme
NAME        ceramide kinase;
            acylsphingosine kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:ceramide 1-phosphotransferase
REACTION    ATP + ceramide = ADP + ceramide 1-phosphate [RN:R01495]
ALL_REAC    R01495
SUBSTRATE   ATP [CPD:C00002];
            ceramide [CPD:C00195]
PRODUCT     ADP [CPD:C00008];
            ceramide 1-phosphate [CPD:C02960]
REFERENCE   1  [PMID:2547795]
  AUTHORS   Bajjalieh SM, Martin TF, Floor E.
  TITLE     Synaptic vesicle ceramide kinase. A calcium-stimulated lipid kinase
            that co-purifies with brain synaptic vesicles.
  JOURNAL   J. Biol. Chem. 264 (1989) 14354-60.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00600  Sphingolipid metabolism
ORTHOLOGY   KO: K04715  ceramide kinase
GENES       HSA: 64781(CERK)
            MMU: 223753(Cerk)
            CFA: 474464(CERK)
            GGA: 425523(RCJMB04_16p10)
            CEL: T10B11.2
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.138
            ExPASy - ENZYME nomenclature database: 2.7.1.138
            ExplorEnz - The Enzyme Database: 2.7.1.138
            ERGO genome analysis and discovery system: 2.7.1.138
            BRENDA, the Enzyme Database: 2.7.1.138
            CAS: 123175-68-8
///
ENTRY       EC 2.7.1.139      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Deleted entry: inositol-trisphosphate 5-kinase. Now included with EC
            2.7.1.134, inositol-tetrakisphosphate 1-kinase (EC 2.7.1.139 created
            1992, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.139
            ExPASy - ENZYME nomenclature database: 2.7.1.139
            ExplorEnz - The Enzyme Database: 2.7.1.139
            ERGO genome analysis and discovery system: 2.7.1.139
            BRENDA, the Enzyme Database: 2.7.1.139
///
ENTRY       EC 2.7.1.140                Enzyme
NAME        inositol-tetrakisphosphate 5-kinase;
            1D-myo-inositol-tetrakisphosphate 5-kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:1D-myo-inositol-1,3,4,6-tetrakisphosphate 5-phosphotransferase
REACTION    ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate = ADP +
            1D-myo-inositol 1,3,4,5,6-pentakisphosphate [RN:R03478]
ALL_REAC    R03478
SUBSTRATE   ATP [CPD:C00002];
            1D-myo-inositol 1,3,4,6-tetrakisphosphate [CPD:C04477]
PRODUCT     ADP [CPD:C00008];
            1D-myo-inositol 1,3,4,5,6-pentakisphosphate [CPD:C01284]
COMMENT     The enzyme from plants and yeast can also use Ins(1,2,3,4,6)P5 as a
            substrate [2].
REFERENCE   1  [PMID:2584198]
  AUTHORS   Shears SB.
  TITLE     The pathway of myo-inositol 1,3,4-trisphosphate phosphorylation in
            liver. Identification of myo-inositol 1,3,4-trisphosphate 6-kinase,
            myo-inositol 1,3,4-trisphosphate 5-kinase, and myo-inositol
            1,3,4,6-tetrakisphosphate 5-kinase.
  JOURNAL   J. Biol. Chem. 264 (1989) 19879-86.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:12226109]
  AUTHORS   Stevenson-Paulik J, Odom AR, York JD.
  TITLE     Molecular and biochemical characterization of two plant inositol
            polyphosphate 6-/3-/5-kinases.
  JOURNAL   J. Biol. Chem. 277 (2002) 42711-8.
  ORGANISM  Arabidopsis thaliana [GN:ath]
PATHWAY     PATH: map00562  Inositol phosphate metabolism
            PATH: map04070  Phosphatidylinositol signaling system
ORTHOLOGY   KO: K00915  1D-myo-Inositol-tetrakisphosphate 5-kinase
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.140
            ExPASy - ENZYME nomenclature database: 2.7.1.140
            ExplorEnz - The Enzyme Database: 2.7.1.140
            ERGO genome analysis and discovery system: 2.7.1.140
            BRENDA, the Enzyme Database: 2.7.1.140
            CAS: 123940-40-9
///
ENTRY       EC 2.7.1.141      Obsolete  Enzyme
NAME        Transferred to 2.7.11.23
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.11.23 [RNA-polymerase]-subunit kinase
            (EC 2.7.1.141 created 1992, deleted 2005)
GENES       DME: Dmel_CG6292(CycT)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.141
            ExPASy - ENZYME nomenclature database: 2.7.1.141
            ExplorEnz - The Enzyme Database: 2.7.1.141
            ERGO genome analysis and discovery system: 2.7.1.141
            BRENDA, the Enzyme Database: 2.7.1.141
///
ENTRY       EC 2.7.1.142                Enzyme
NAME        glycerol-3-phosphate---glucose phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     sn-glycerol-3-phosphate:D-glucose 6-phosphotransferase
REACTION    sn-glycerol 3-phosphate + D-glucose = glycerol + D-glucose
            6-phosphate [RN:R00850]
ALL_REAC    R00850
SUBSTRATE   sn-glycerol 3-phosphate [CPD:C00093];
            D-glucose [CPD:C00031]
PRODUCT     glycerol [CPD:C00116];
            D-glucose 6-phosphate [CPD:C00092]
COMMENT     Involved in the anaerobic metabolism of sugars in the bloodstream of
            trypanosomes.
REFERENCE   1  [PMID:2555230]
  AUTHORS   Kiaira JK, Njogu RM.
  TITLE     Evidence for glycerol 3-phosphate:glucose transphosphorylase
            activity in bloodstream Trypanosoma brucei brucei.
  JOURNAL   Int. J. Biochem. 21 (1989) 839-45.
  ORGANISM  Trypanosoma brucei [GN:tbr]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.142
            ExPASy - ENZYME nomenclature database: 2.7.1.142
            ExplorEnz - The Enzyme Database: 2.7.1.142
            ERGO genome analysis and discovery system: 2.7.1.142
            BRENDA, the Enzyme Database: 2.7.1.142
            CAS: 125008-33-5
///
ENTRY       EC 2.7.1.143                Enzyme
NAME        diphosphate-purine nucleoside kinase;
            pyrophosphate-purine nucleoside kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     diphosphate:purine nucleoside phosphotransferase
REACTION    diphosphate + a purine nucleoside = phosphate + a purine
            mononucleotide [RN:R03699]
ALL_REAC    R03699
SUBSTRATE   diphosphate [CPD:C00013];
            purine nucleoside [CPD:C01736]
PRODUCT     phosphate [CPD:C00009];
            purine mononucleotide [CPD:C05325]
COMMENT     The enzyme from the Acholeplasma class of Mollicutes catalyses the
            conversion of adenosine, guanosine and inosine to AMP, GMP and IMP.
            ATP cannot substitute for diphosphate as a substrate.
REFERENCE   1  [PMID:6330034]
  AUTHORS   Tryon VV, Pollack D.
  TITLE     Purine metabolism in Acholeplasma laidlawii B: novel PPi-dependent
            nucleoside kinase activity.
  JOURNAL   J. Bacteriol. 159 (1984) 265-70.
  ORGANISM  Acholeplasma laidlawii
REFERENCE   2
  AUTHORS   Tryon, V.V., Pollack, J.D.
  TITLE     Distinctions in Mollicutes purine metabolism:
            pyrophosphate-dependent nucleoside kinase and dependence on
            guanylate salvage.
  JOURNAL   Int. J. Systematic Bacteriol. 35 (1985) 497-501.
  ORGANISM  Acholeplasma laidlawii, Acholeplasma axanthum, Acholeplasma
            granularum
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.143
            ExPASy - ENZYME nomenclature database: 2.7.1.143
            ExplorEnz - The Enzyme Database: 2.7.1.143
            ERGO genome analysis and discovery system: 2.7.1.143
            BRENDA, the Enzyme Database: 2.7.1.143
            CAS: 70356-41-1
///
ENTRY       EC 2.7.1.144                Enzyme
NAME        tagatose-6-phosphate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:D-tagatose-6-phosphate 1-phosphotransferase
REACTION    ATP + D-tagatose 6-phosphate = ADP + D-tagatose 1,6-bisphosphate
            [RN:R03236]
ALL_REAC    R03236
SUBSTRATE   ATP [CPD:C00002];
            D-tagatose 6-phosphate [CPD:C01097]
PRODUCT     ADP [CPD:C00008];
            D-tagatose 1,6-bisphosphate [CPD:C03785]
REFERENCE   1  [PMID:7772602]
  AUTHORS   Nobelmann B, Lengeler JW.
  TITLE     Sequence of the gat operon for galactitol utilization from a
            wild-type strain EC3132 of Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 1262 (1995) 69-72.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00052  Galactose metabolism
ORTHOLOGY   KO: K00917  tagatose 6-phosphate kinase
GENES       LMA: LmjF02.0030
            EHI: 20.t00017
            ECO: b2095(gatZ) b3132(agaZ)
            ECJ: JW2082(gatZ) JW3101(kbaZ)
            ECE: Z3258(gatZ) Z4484(agaZ)
            ECS: ECs2898 ECs4010
            ECC: c2620(gatZ) c3887(agaZ)
            ECI: UTI89_C2368(gatZ) UTI89_C3561(agaZ)
            ECP: ECP_2133 ECP_3222
            ECV: APECO1_3297(agaZ) APECO1_4450(gatZ)
            STY: STY3439
            STT: t3177
            SPT: SPA3126(gatZ)
            SEC: SC3198(gatZ)
            STM: STM3257
            YPE: YPO0832(agaZ)
            YPK: y3217(agaZ)
            YPM: YP_3528(agaZ)
            YPA: YPA_0438
            YPN: YPN_3034
            YPP: YPDSF_0682
            YPS: YPTB3076(agaZ)
            SFL: SF2157(gatZ) SF3167(agaZ)
            SFX: S2283(gatZ) S3382(agaZ)
            SFV: SFV_2150(gatZ)
            PLU: plu0833(agaZ)
            SGL: SG0177
            ENT: Ent638_3572
            SPE: Spro_3848
            HSO: HS_1145(gatZ)
            VVU: VV2_1024
            VVY: VVA1517
            VFI: VFA1005
            PPR: PBPRB0141 PBPRB1037
            SAZ: Sama_1195
            SHE: Shewmr4_2534
            SHM: Shewmr7_2601
            SHN: Shewana3_2700
            CSA: Csal_0640
            MMW: Mmwyl1_3106
            RSO: RSc2145(agaZ)
            BMV: BMASAVP1_A0630
            BML: BMA10299_A2464
            BMN: BMA10247_0078
            BVI: Bcep1808_2710
            BUR: Bcep18194_A5927
            BCN: Bcen_1986
            BCH: Bcen2424_2596
            BAM: Bamb_2644
            BPS: BPSL0828
            BPM: BURPS1710b_1033(agaZ)
            BPL: BURPS1106A_0874
            BPD: BURPS668_0870
            BTE: BTH_I0694
            VEI: Veis_1192
            MLO: mll7215
            SME: SMb21373
            SMD: Smed_4765
            ATU: Atu3167(agaZ)
            ATC: AGR_L_3286
            RET: RHE_PC00221(ypc00123)
            RLE: RL0643(agaZ) pRL120249(agaZ)
            OAN: Oant_0288
            RSQ: Rsph17025_3586
            PDE: Pden_4847
            BCA: BCE_1907(lacC)
            BCZ: BCZK1642(lacC)
            SAU: SA1995(lacC)
            SAV: SAV2193(lacC)
            SAM: MW2119(lacC)
            SAR: SAR2284(lacC)
            SAS: SAS2094
            SAC: SACOL2184(lacC)
            SAB: SAB2074c(lacC)
            SAA: SAUSA300_2153(lacC)
            SAO: SAOUHSC_02453
            SAJ: SaurJH9_2224
            SAH: SaurJH1_2263
            SEP: SE1785
            SER: SERP1793(lacC)
            SHA: SH0844(lacC)
            LLC: LACR_D04
            SPY: SPy_1921(lacC.2)
            SPZ: M5005_Spy_1396 M5005_Spy_1636(lacC.2)
            SPM: spyM18_1989
            SPG: SpyM3_1657(lacC.2)
            SPS: SPs1655
            SPH: MGAS10270_Spy1517 MGAS10270_Spy1705(lacC2)
            SPI: MGAS10750_Spy1509 MGAS10750_Spy1733(lacC2)
            SPJ: MGAS2096_Spy1421 MGAS2096_Spy1661(lacC2)
            SPK: MGAS9429_Spy1398 MGAS9429_Spy1639(lacC2)
            SPF: SpyM51611(lacC2)
            SPA: M6_Spy1445 M6_Spy1645
            SPB: M28_Spy1439 M28_Spy1626(lacC.2)
            SPN: SP_1191
            SPR: spr1074(lacC)
            SPD: SPD_1051(lacC)
            SAG: SAG1929(lacC)
            SAN: gbs1334 gbs1916
            SAK: SAK_1888(lacC)
            SMU: SMU.1494(lacC)
            SSA: SSA_1697(lacC)
            SGO: SGO_1517(lacC) SGO_1524(lacC-2)
            LCA: LSEI_0677
            EFA: EF1806(lacC)
            STH: STH1246
            CAC: CAC2951(lacC)
            CPE: CPE0328(lacC)
            CNO: NT01CX_0289
            CTH: Cthe_1956
            CDF: CD3451(lacC)
            MTA: Moth_0611
            MSM: MSMEG_0510
            SCO: SCO4283(SCD95A.16c) SCO5848(agaZ)
            SMA: SAV3942
            SEN: SACE_6317(lacC)
STRUCTURES  PDB: 2AWD  2F02  2JG1  2JGV  2Q5R  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.144
            ExPASy - ENZYME nomenclature database: 2.7.1.144
            ExplorEnz - The Enzyme Database: 2.7.1.144
            ERGO genome analysis and discovery system: 2.7.1.144
            BRENDA, the Enzyme Database: 2.7.1.144
            CAS: 39434-00-9
///
ENTRY       EC 2.7.1.145                Enzyme
NAME        deoxynucleoside kinase;
            multispecific deoxynucleoside kinase;
            ms-dNK;
            multisubstrate deoxyribonucleoside kinase;
            multifunctional deoxynucleoside kinase;
            D. melanogaster deoxynucleoside kinase;
            Dm-dNK
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:deoxynucleoside 5'-phosphotransferase
REACTION    ATP + 2'-deoxynucleoside = ADP + 2'-deoxynucleoside 5'-phosphate
            [RN:R05806]
ALL_REAC    R05806
SUBSTRATE   ATP [CPD:C00002];
            2'-deoxynucleoside [CPD:C02269]
PRODUCT     ADP [CPD:C00008];
            2'-deoxynucleoside 5'-phosphate [CPD:C00676]
COMMENT     The enzyme from embryonic cells of Drosophila melanogaster differs
            from other deoxynucleoside kinases [EC 2.7.1.76 (deoxyadenosine
            kinase) and EC 2.7.1.113 (deoxyguanosine kinase)] in its broad
            specificity for all four common deoxynucleosides.
REFERENCE   1  [PMID:9461577]
  AUTHORS   Munch-Petersen B, Piskur J, Sondergaard L.
  TITLE     Four deoxynucleoside kinase activities from Drosophila melanogaster
            are contained within a single monomeric enzyme, a new
            multifunctional deoxynucleoside kinase.
  JOURNAL   J. Biol. Chem. 273 (1998) 3926-31.
  ORGANISM  Drosophila melanogaster [GN:dme]
REFERENCE   2  [PMID:10692477]
  AUTHORS   Munch-Petersen B, Knecht W, Lenz C, Sondergaard L, Piskur J.
  TITLE     Functional expression of a multisubstrate deoxyribonucleoside kinase
            from Drosophila melanogaster and its C-terminal deletion mutants.
  JOURNAL   J. Biol. Chem. 275 (2000) 6673-9.
  ORGANISM  Drosophila melanogaster [GN:dme]
ORTHOLOGY   KO: K05961  
GENES       DME: Dmel_CG5452(dnk)
            BTK: BT9727_0015(dck)
            BPU: BPUM_0511
            SAA: SAUSA300_0541
STRUCTURES  PDB: 1OE0  1OT3  1ZM7  1ZMX  2JCS  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.145
            ExPASy - ENZYME nomenclature database: 2.7.1.145
            ExplorEnz - The Enzyme Database: 2.7.1.145
            ERGO genome analysis and discovery system: 2.7.1.145
            BRENDA, the Enzyme Database: 2.7.1.145
            CAS: 52227-81-3
///
ENTRY       EC 2.7.1.146                Enzyme
NAME        ADP-specific phosphofructokinase;
            ADP-6-phosphofructokinase, ADP-dependent phosphofructokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ADP:D-fructose-6-phosphate 1-phosphotransferase
REACTION    ADP + D-fructose 6-phosphate = AMP + D-fructose 1,6-bisphosphate
            [RN:R05805]
ALL_REAC    R05805
SUBSTRATE   ADP [CPD:C00008];
            D-fructose 6-phosphate [CPD:C00085]
PRODUCT     AMP [CPD:C00020];
            D-fructose 1,6-bisphosphate [CPD:C00354]
COMMENT     ADP can be replaced by GDP, ATP and GTP, to a limited extent.
            Divalent cations are necessary for activity, with Mg2+ followed by
            Co2+ being the most effective.
REFERENCE   1  [PMID:10409652]
  AUTHORS   Tuininga JE, Verhees CH, van der Oost J, Kengen SW, Stams AJ, de Vos
            WM.
  TITLE     Molecular and biochemical characterization of the ADP-dependent
            phosphofructokinase from the hyperthermophilic archaeon Pyrococcus
            furiosus.
  JOURNAL   J. Biol. Chem. 274 (1999) 21023-8.
  ORGANISM  Pyrococcus furiosus [GN:pfu]
ORTHOLOGY   KO: K00918  ADP-specific phosphofructokinase
GENES       MJA: MJ1604
            MMP: MMP1296(pfkC)
            MMQ: MmarC5_0297
            MMZ: MmarC7_0541
            MAE: Maeo_0005
            MVN: Mevan_0606
            MAC: MA3563(pfk)
            MBA: Mbar_A2004
            MMA: MM_0473
            MBU: Mbur_1339
            PHO: PH1645
            PAB: PAB2013
            PFU: PF1784
            TKO: TK0376
STRUCTURES  PDB: 1U2X  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.146
            ExPASy - ENZYME nomenclature database: 2.7.1.146
            ExplorEnz - The Enzyme Database: 2.7.1.146
            ERGO genome analysis and discovery system: 2.7.1.146
            BRENDA, the Enzyme Database: 2.7.1.146
            CAS: 237739-62-7
///
ENTRY       EC 2.7.1.147                Enzyme
NAME        ADP-specific glucokinase;
            ADP-dependent glucokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ADP:D-glucose 6-phosphotransferase
REACTION    ADP + D-glucose = AMP + D-glucose 6-phosphate [RN:R05804]
ALL_REAC    R05804
SUBSTRATE   ADP [CPD:C00008];
            D-glucose [CPD:C00031]
PRODUCT     AMP [CPD:C00020];
            D-glucose 6-phosphate [CPD:C00092]
COMMENT     Requires Mg2+. The enzyme from Pyrococcus furiosus is highly
            specific for D-glucose; there is some activity with
            2-deoxy-D-glucose, but no activity with D-fructose, D-mannose or
            D-galactose as the substrate. No activity is detected when ADP is
            replaced by ATP, GDP, phosphoenolpyruvate, diphosphate or
            polyphosphate.
REFERENCE   1  [PMID:8530474]
  AUTHORS   Kengen SW, Tuininga JE, de Bok FA, Stams AJ, de Vos WM.
  TITLE     Purification and characterization of a novel ADP-dependent
            glucokinase from the hyperthermophilic archaeon Pyrococcus furiosus.
  JOURNAL   J. Biol. Chem. 270 (1995) 30453-7.
  ORGANISM  Pyrococcus furiosus [GN:pfu]
ORTHOLOGY   KO: K08074  ADP-specific glucokinase
GENES       HSA: 83440(ADPGK)
            MMU: 72141(Adpgk)
            RNO: 315722(Adpgk)
            CFA: 478360(ADPGK)
            GGA: 415317(ADPGK)
            SPU: 588810(LOC588810)
            PHO: PH0589
            PAB: PAB0967
            PFU: PF0312
            TKO: TK1110
STRUCTURES  PDB: 1GC5  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.147
            ExPASy - ENZYME nomenclature database: 2.7.1.147
            ExplorEnz - The Enzyme Database: 2.7.1.147
            ERGO genome analysis and discovery system: 2.7.1.147
            BRENDA, the Enzyme Database: 2.7.1.147
///
ENTRY       EC 2.7.1.148                Enzyme
NAME        4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase;
            CDP-ME kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
            2-phosphotransferase
REACTION    ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = ADP +
            2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
            [RN:R05634]
ALL_REAC    R05634
SUBSTRATE   ATP [CPD:C00002];
            4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol [CPD:C11435]
PRODUCT     ADP [CPD:C00008];
            2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
            [CPD:C11436]
COMMENT     The enzyme from Escherichia coli requires Mg2+ or Mn2+. Forms part
            of an alternative nonmevalonate pathway for terpenoid biosynthesis
            (for diagram, click here).
REFERENCE   1  [PMID:10655484]
  AUTHORS   Luttgen H, Rohdich F, Herz S, Wungsintaweekul J, Hecht S, Schuhr CA,
            Fellermeier M, Sagner S, Zenk MH, Bacher A, Eisenreich W.
  TITLE     Biosynthesis of terpenoids: YchB protein of Escherichia coli
            phosphorylates the 2-hydroxy group of
            4-diphosphocytidyl-2C-methyl-D-erythritol.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 1062-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Kuzuyama, T., Takagi, M., Kaneda, K., Watanabe, H., Dairi, T. and
            Seto, H.
  TITLE     Studies on the nonmevalonate pathway: conversion of 4-(cytidine
            5'-diphospho)-2-C-methyl-D-erythritol to its 2-phospho derivative by
            4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase.
  JOURNAL   Tetrahedron Lett. 41 (2000) 2925-2928.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K00919  4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
GENES       ATH: AT2G26930(ATCDPMEK)
            OSA: 4327968
            CME: CMS444C
            PFA: PFE0150c
            ECO: b1208(ispE)
            ECJ: JW1199(ispE)
            ECE: Z1979(ychB)
            ECS: ECs1713
            ECC: c1666(ispE)
            ECI: UTI89_C1402(ychB)
            ECP: ECP_1256
            ECV: APECO1_324(ychB)
            ECW: EcE24377A_1356(ispE)
            ECX: EcHS_A1313
            STY: STY1905(ipk)
            STT: t1097(ipk)
            SPT: SPA1094(ipk)
            SEC: SC1773(ipk)
            STM: STM1779(ipk)
            YPE: YPO2014(ipk)
            YPK: y2293
            YPM: YP_1862(ipk)
            YPA: YPA_1398
            YPN: YPN_1496
            YPP: YPDSF_1104
            YPS: YPTB2002(ipk)
            YPI: YpsIP31758_2069(ispE)
            SFL: SF1211(ychB)
            SFX: S1295(ychB)
            SFV: SFV_1222(ychB)
            SSN: SSON_1970(ychB)
            SBO: SBO_1859(ychB)
            SDY: SDY_1257(ychB)
            ECA: ECA2187(ispE)
            PLU: plu2067(ispE)
            BUC: BU170(ychB)
            BAS: BUsg164(ipk)
            WBR: WGLp348(ychB)
            SGL: SG1879
            ENT: Ent638_2340
            SPE: Spro_1987
            BFL: Bfl347(ipk)
            BPN: BPEN_357(ispE)
            HIN: HI1608
            HIT: NTHI1434(ispE)
            HIP: CGSHiEE_05690
            HIQ: CGSHiGG_10080
            HDU: HD1628(ispE)
            HSO: HS_0997(ispE)
            PMU: PM0245
            MSU: MS1535(ispE)
            APL: APL_0776(ispE)
            ASU: Asuc_1751
            XFA: XF2645
            XFT: PD2018(ispE)
            XCC: XCC0871(ipk)
            XCB: XC_3359
            XCV: XCV0979(ispE)
            XAC: XAC0948(ipk)
            XOO: XOO3604(ipk)
            XOM: XOO_3406(XOO3406)
            VCH: VC2182
            VVU: VV1_0256
            VVY: VV0928
            VPA: VP0740
            VFI: VF0765
            PPR: PBPRA2848
            PAE: PA4669(ipk)
            PAU: PA14_61750(ipk)
            PAP: PSPA7_5318(ispE)
            PPU: PP_0723(ispE)
            PPF: Pput_0757
            PST: PSPTO_1105(ispE)
            PSB: Psyr_0945(ipk)
            PSP: PSPPH_0993(ispE)
            PFL: PFL_5163(ipk)
            PFO: Pfl_4752
            PEN: PSEEN0858(ispE)
            PMY: Pmen_1056
            PAR: Psyc_0173(ispE)
            PCR: Pcryo_0186
            PRW: PsycPRwf_2104
            ACI: ACIAD2903(ispE)
            SON: SO_3836(ispE)
            SDN: Sden_0917
            SFR: Sfri_0720
            SAZ: Sama_2569
            SBL: Sbal_0693
            SBM: Shew185_3617
            SLO: Shew_2915
            SSE: Ssed_3462
            SPL: Spea_3129
            SHE: Shewmr4_3172
            SHM: Shewmr7_0794
            SHN: Shewana3_0766
            SHW: Sputw3181_3377
            ILO: IL0928(ispE)
            CPS: CPS_3556(ispE)
            PHA: PSHAa1055(ispE)
            PAT: Patl_2566
            SDE: Sde_3255
            PIN: Ping_0912
            MAQ: Maqu_2364
            MCA: MCA1055(ispE)
            FTU: FTT0271(ispE)
            FTF: FTF0271(ispE)
            FTW: FTW_1830(ispE)
            FTL: FTL_0151
            FTH: FTH_0144(ispE)
            FTA: FTA_0164(ispE)
            FTN: FTN_0146(ispE)
            NOC: Noc_0513
            AEH: Mlg_0282
            HHA: Hhal_0990
            HCH: HCH_01727(ispE)
            CSA: Csal_1525
            ABO: ABO_0519(ispE)
            MMW: Mmwyl1_3603
            AHA: AHA_3152(ispE)
            BCI: BCI_0292(ispE)
            RMA: Rmag_0110
            VOK: COSY_0115(ispE)
            NME: NMB0874
            NMA: NMA1092
            NGO: NGO0440
            CVI: CV_4059(ispE)
            RSO: RSc0396(ipk)
            REU: Reut_A0343
            REH: H16_A0374
            RME: Rmet_0290
            BMA: BMA3118(ispE)
            BMV: BMASAVP1_A0086(ispE)
            BML: BMA10299_A1504(ispE)
            BMN: BMA10247_2932(ispE)
            BXE: Bxe_A4132
            BVI: Bcep1808_2906
            BUR: Bcep18194_A6131
            BCN: Bcen_2187
            BCH: Bcen2424_2801
            BAM: Bamb_2861
            BPS: BPSL0523
            BPM: BURPS1710b_0755(ispE)
            BPL: BURPS1106A_0587(ispE)
            BPD: BURPS668_0571(ispE)
            BTE: BTH_I0476(ispE)
            PNU: Pnuc_1919
            BPE: BP3126(ispE)
            BPA: BPP0816(ispE)
            BBR: BB0900(ispE)
            RFR: Rfer_1659
            POL: Bpro_1294
            PNA: Pnap_0900
            AAV: Aave_3609
            AJS: Ajs_0896
            VEI: Veis_0952
            MPT: Mpe_A3230
            HAR: HEAR2892(ispE)
            MMS: mma_3127
            NEU: NE1827(ipk)
            NET: Neut_1139
            NMU: Nmul_A0588
            EBA: ebA1405(ispE)
            AZO: azo0756(ispE)
            DAR: Daro_3729
            TBD: Tbd_0386
            MFA: Mfla_0679
            HPY: HP1443
            HPJ: jhp1336
            HPA: HPAG1_1369
            HHE: HH0122
            HAC: Hac_0175(ipk)
            WSU: WS0881
            TDN: Tmden_0440
            CJE: Cj1104
            CJR: CJE1247(ispE)
            CJJ: CJJ81176_1122(ispE)
            CJU: C8J_1045
            CJD: JJD26997_0618(ispE)
            CFF: CFF8240_0713
            CCV: CCV52592_0696(ispE)
            CHA: CHAB381_1110
            CCO: CCC13826_0061(ispE) CCC13826_1794
            ABU: Abu_2083(ispE)
            NIS: NIS_1475
            SUN: SUN_0381
            GSU: GSU0660(ispE)
            GME: Gmet_2849
            PCA: Pcar_2005
            DVU: DVU1576(ispE)
            DDE: Dde_2125
            LIP: LI0735(ychB)
            DPS: DP2735
            ADE: Adeh_0123
            AFW: Anae109_0127
            SAT: SYN_03046
            SFU: Sfum_3651
            WOL: WD0360(ispE)
            WBM: Wbm0173
            AMA: AM493(ispE)
            APH: APH_0574(ispE)
            ERU: Erum3340(ispE)
            ERW: ERWE_CDS_03410(ispE)
            ERG: ERGA_CDS_03370(ispE)
            ECN: Ecaj_0317
            ECH: ECH_0757(ispE)
            NSE: NSE_0720
            PUB: SAR11_0105(ispE)
            MLO: mll7422
            MES: Meso_0706
            PLA: Plav_0721
            SME: SMc00862(ipk)
            SMD: Smed_0456
            ATU: Atu0632(ipk)
            ATC: AGR_C_1122
            RET: RHE_CH00873(ispE)
            RLE: RL0935
            BME: BMEI1537
            BMF: BAB1_0423(ispE)
            BMS: BR0394(ispE)
            BMB: BruAb1_0418(ispE)
            BOV: BOV_0403(ispE)
            OAN: Oant_0512
            BJA: blr2526(ipk)
            BRA: BRADO2022(ispE)
            BBT: BBta_2348(ispE)
            RPA: RPA1039(ispE)
            RPB: RPB_1086
            RPC: RPC_4356
            RPD: RPD_1213
            RPE: RPE_4419
            NWI: Nwi_2593
            NHA: Nham_3216
            BHE: BH04210(thrB1)
            BQU: BQ03230(thrB)
            BBK: BARBAKC583_0387(ispE)
            XAU: Xaut_1381
            CCR: CC_1336
            SIL: SPO0318(ispE)
            SIT: TM1040_3743
            RSP: RSP_1779(ispE)
            RSH: Rsph17029_0426
            RSQ: Rsph17025_2471
            JAN: Jann_0486
            RDE: RD1_3402(ispE)
            PDE: Pden_0423
            MMR: Mmar10_2186
            HNE: HNE_0676(ispE)
            ZMO: ZMO1182(ispE)
            NAR: Saro_1782
            SAL: Sala_1187
            SWI: Swit_4106
            ELI: ELI_06920
            GOX: GOX1559
            GBE: GbCGDNIH1_1848
            ACR: Acry_2663
            RRU: Rru_A0263
            MAG: amb4435
            MGM: Mmc1_0819
            ABA: Acid345_4541
            BSU: BG10109(ispE)
            BHA: BH0061
            BAN: BA0043(ispE)
            BAR: GBAA0043(ispE)
            BAA: BA_0633
            BAT: BAS0044
            BCE: BC0050
            BCA: BCE_0043(ispE)
            BCZ: BCZK0040(ispE)
            BTK: BT9727_0040(ispE)
            BTL: BALH_0040(ispE)
            BLI: BL00525(ispE)
            BLD: BLi00059(ispE)
            BCL: ABC0074(ispE)
            BAY: RBAM_000550
            BPU: BPUM_0030
            OIH: OB0055
            GKA: GK0039
            SAU: SA0453
            SAV: SAV0495
            SAM: MW0450
            SAR: SAR0496
            SAS: SAS0452
            SAC: SACOL0538(ispE)
            SAB: SAB0444
            SAA: SAUSA300_0472(ispE)
            SAO: SAOUHSC_00466
            SEP: SE2288
            SER: SERP0133(ispE)
            SHA: SH2516
            SSP: SSP2261
            LMO: lmo0190(yabH)
            LMF: LMOf2365_0201(ispE)
            LIN: lin0229
            LWE: lwe0159(ispE)
            SPZ: M5005_Spy_0074 M5005_Spy_0075 M5005_Spy_0076
            SPH: MGAS10270_Spy0077 MGAS10270_Spy0078
            SPI: MGAS10750_Spy0082 MGAS10750_Spy0083
            SPJ: MGAS2096_Spy0077 MGAS2096_Spy0078 MGAS2096_Spy0079
            SPK: MGAS9429_Spy0074 MGAS9429_Spy0075 MGAS9429_Spy0076
            SPA: M6_Spy0123 M6_Spy0124
            SPB: M28_Spy0073 M28_Spy0074
            SAG: SAG0153(ispE)
            SAN: gbs0149
            SAK: SAK_0216(ispE)
            SMU: SMU.1996(ipk)
            LPL: lp_0460(ispE)
            LSA: LSA1652(ispE)
            LSL: LSL_0234(ispE)
            LBR: LVIS_0460
            LCA: LSEI_2591
            EFA: EF0051(ispE)
            STH: STH3246
            CAC: CAC2902
            CPE: CPE2212(ipk)
            CPF: CPF_2476(ispE)
            CPR: CPR_2186(ispE)
            CTC: CTC00283
            CNO: NT01CX_0566(ispE)
            CDF: CD3566(ipk)
            CBO: CBO0121(ipk)
            CBA: CLB_0157(ispE)
            CBH: CLC_0169(ispE)
            CBF: CLI_0176(ispE)
            CKL: CKL_3724(ispE)
            CHY: CHY_0188(ispE)
            DSY: DSY0148
            SWO: Swol_0064
            TTE: TTE2559(ispE)
            MTA: Moth_0072
            MGA: MGA_0635
            MTU: Rv1011(ispE)
            MTC: MT1040
            MBO: Mb1038(ispE)
            MLE: ML0242
            MPA: MAP0976
            MAV: MAV_1149(ispE)
            MSM: MSMEG_5436(ispE)
            MMC: Mmcs_4262
            CGL: NCgl0874(cgl0911)
            CGB: cg1039
            CEF: CE0973
            CDI: DIP0876
            CJK: jk1510(ispE)
            NFA: nfa49010(cmeK)
            RHA: RHA1_ro05684
            SCO: SCO3148(SCE66.27c)
            SMA: SAV3586(cmeK)
            TWH: TWT605(ispE)
            TWS: TW159(ispE)
            LXX: Lxx17480(ispE)
            CMI: CMM_2367(ispE)
            AAU: AAur_1338(ispE)
            PAC: PPA0527
            TFU: Tfu_0407
            FRA: Francci3_3958
            FAL: FRAAL6276(ispE)
            KRA: Krad_1046
            SEN: SACE_0807(ispE)
            BLO: BL0656(ispE)
            BAD: BAD_1616(ispE)
            RXY: Rxyl_0893
            RBA: RB10537(ispE)
            CTR: CT804(ychB)
            CTA: CTA_0876(ispE)
            CMU: TC0187
            CPJ: CPj0954 CPj0955
            CPT: CpB0991 CpB0992
            CCA: CCA00815(ispE)
            CAB: CAB784
            CFE: CF0199(ispE)
            PCU: pc1589
            TPA: TP0371
            TDE: TDE1338(ispE)
            LIL: LA3824(ychB)
            LIC: LIC10426(ispE)
            LBJ: LBJ_2584(ispE)
            LBL: LBL_0528(ispE)
            SYN: sll0711(ipk)
            SYW: SYNW1053(ispE)
            SYC: syc1203_d(ispE)
            SYF: Synpcc7942_0310
            SYD: Syncc9605_1188
            SYE: Syncc9902_1282
            SYG: sync_1593(ispE)
            SYR: SynRCC307_1314(ispE)
            SYX: SynWH7803_1365(ispE)
            CYA: CYA_0285(ispE)
            CYB: CYB_1390(ispE)
            TEL: tll0500
            GVI: gll0102
            ANA: alr3230
            AVA: Ava_4887
            PMA: Pro0764(ispE)
            PMM: PMM0932(ispE)
            PMT: PMT0620(ispE)
            PMN: PMN2A_0279
            PMI: PMT9312_0867
            PMB: A9601_09281(ispE)
            PMC: P9515_10151(ispE)
            PMF: P9303_16181(ispE)
            PMG: P9301_09261(ispE)
            PME: NATL1_09481(ispE)
            TER: Tery_4700
            BTH: BT_0624
            BFR: BF2589
            BFS: BF2610
            PGI: PG0935(ispE)
            SRU: SRU_0689(ispE)
            CHU: CHU_1210(ispE)
            CTE: CT1495(ispE)
            CCH: Cag_1333
            CPH: Cpha266_1884
            PVI: Cvib_1321
            PLT: Plut_1496
            DET: DET0405(ispE)
            DEH: cbdb_A356(ispE)
            DRA: DR_2605
            DGE: Dgeo_0180
            TTH: TTC1816
            TTJ: TTHA0170
            AAE: aq_915
            TMA: TM1383
            TPT: Tpet_1400
            TME: Tmel_0318
            FNO: Fnod_1663
STRUCTURES  PDB: 1OJ4  1UEK  2V2Q  2V2V  2V2Z  2V34  2V8P  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.148
            ExPASy - ENZYME nomenclature database: 2.7.1.148
            ExplorEnz - The Enzyme Database: 2.7.1.148
            ERGO genome analysis and discovery system: 2.7.1.148
            BRENDA, the Enzyme Database: 2.7.1.148
///
ENTRY       EC 2.7.1.149                Enzyme
NAME        1-phosphatidylinositol-5-phosphate 4-kinase;
            type II PIP kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:1-phosphatidyl-1D-myo-inositol-5-phosphate 4-phosphotransferase
REACTION    ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP +
            1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [RN:R05803]
ALL_REAC    R05803
SUBSTRATE   ATP [CPD:C00002];
            1-phosphatidyl-1D-myo-inositol 5-phosphate [CPD:C11557]
PRODUCT     ADP [CPD:C00008];
            1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [CPD:C04637]
REFERENCE   1  [PMID:9367159]
  AUTHORS   Rameh LE, Tolias KF, Duckworth BC, Cantley LC.
  TITLE     A new pathway for synthesis of
            phosphatidylinositol-4,5-bisphosphate.
  JOURNAL   Nature. 390 (1997) 192-6.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00562  Inositol phosphate metabolism
            PATH: map04070  Phosphatidylinositol signaling system
            PATH: map04810  Regulation of actin cytoskeleton
ORTHOLOGY   KO: K00920  1-phosphatidylinositol-5-phosphate 4-kinase
GENES       TAN: TA11845
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.149
            ExPASy - ENZYME nomenclature database: 2.7.1.149
            ExplorEnz - The Enzyme Database: 2.7.1.149
            ERGO genome analysis and discovery system: 2.7.1.149
            BRENDA, the Enzyme Database: 2.7.1.149
///
ENTRY       EC 2.7.1.150                Enzyme
NAME        1-phosphatidylinositol-3-phosphate 5-kinase;
            type III PIP kinase;
            phosphatidylinositol 3-phosphate 5-kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:1-phosphatidyl-1D-myo-inositol-3-phosphate 5-phosphotransferase
REACTION    ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate = ADP +
            1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate [RN:R05802]
ALL_REAC    R05802
SUBSTRATE   ATP [CPD:C00002];
            1-phosphatidyl-1D-myo-inositol 3-phosphate [CPD:C04549]
PRODUCT     ADP [CPD:C00008];
            1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate [CPD:C11556]
REFERENCE   1  [PMID:9811604]
  AUTHORS   Cooke FT, Dove SK, McEwen RK, Painter G, Holmes AB, Hall MN, Michell
            RH, Parker PJ.
  TITLE     The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p
            is essential for vacuole function in S. cerevisiae.
  JOURNAL   Curr. Biol. 8 (1998) 1219-22.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map04070  Phosphatidylinositol signaling system
            PATH: map04810  Regulation of actin cytoskeleton
ORTHOLOGY   KO: K00921  1-phosphatidylinositol-3-phosphate 5-kinase
GENES       SCE: YFR019W(FAB1)
            AGO: AGOS_AER188C
            PIC: PICST_59054(FAB1)
            CAL: CaO19_1513(CaO19.1513)
            CGR: CAGL0K10384g
            SPO: SPBC6B1.11c
            AFM: AFUA_6G07440
            CNE: CND03330
            UMA: UM00566.1
            DDI: DDBDRAFT_0204693
            TET: TTHERM_01005090
            EHI: 21.t00035
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.150
            ExPASy - ENZYME nomenclature database: 2.7.1.150
            ExplorEnz - The Enzyme Database: 2.7.1.150
            ERGO genome analysis and discovery system: 2.7.1.150
            BRENDA, the Enzyme Database: 2.7.1.150
///
ENTRY       EC 2.7.1.151                Enzyme
NAME        inositol-polyphosphate multikinase;
            IpK2;
            IP3/IP4 6-/3-kinase;
            IP3/IP4 dual-specificity 6-/3-kinase;
            IpmK;
            ArgRIII;
            AtIpk2alpha;
            AtIpk2beta;
            inositol polyphosphate 6-/3-/5-kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:1D-myo-inositol-1,4,5-trisphosphate 6-phosphotransferase
REACTION    (1) ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP +
            1D-myo-inositol 1,4,5,6-tetrakisphosphate [RN:R05800];
            (2) ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate = ADP +
            1D-myo-inositol 1,3,4,5,6-pentakisphosphate [RN:R05801]
ALL_REAC    R05800 R05801
SUBSTRATE   ATP [CPD:C00002];
            1D-myo-inositol 1,4,5-trisphosphate [CPD:C01245];
            1D-myo-inositol 1,4,5,6-tetrakisphosphate [CPD:C11555]
PRODUCT     ADP [CPD:C00008];
            1D-myo-inositol 1,4,5,6-tetrakisphosphate [CPD:C11555];
            1D-myo-inositol 1,3,4,5,6-pentakisphosphate [CPD:C01284]
COMMENT     This enzyme also phosphorylates Ins(1,4,5)P3 to Ins(1,3,4,5)P4,
            Ins(1,3,4,5)P4 to Ins(1,3,4,5,6)P5, and Ins(1,3,4,5,6)P4 to
            Ins(PP)P4, isomer unknown. The enzyme from the plant Arabidopsis
            thaliana can also phosphorylate Ins(1,3,4,6)P4 and Ins(1,2,3,4,6)P5
            at the D-5-position to produce 1,3,4,5,6-pentakisphosphate and
            inositol hexakisphosphate (InsP6), respectively [3]. Yeast produce
            InsP6 from Ins(1,4,5)P3 by the actions of this enzyme and EC
            2.7.1.158, inositol-pentakisphosphate 2-kinase [4].
REFERENCE   1  [PMID:10574768]
  AUTHORS   Saiardi A, Erdjument-Bromage H, Snowman AM, Tempst P, Snyder SH.
  TITLE     Synthesis of diphosphoinositol pentakisphosphate by a newly
            identified family of higher inositol polyphosphate kinases.
  JOURNAL   Curr. Biol. 9 (1999) 1323-6.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:10720331]
  AUTHORS   Odom AR, Stahlberg A, Wente SR, York JD.
  TITLE     A role for nuclear inositol 1,4,5-trisphosphate kinase in
            transcriptional control.
  JOURNAL   Science. 287 (2000) 2026-9.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:12226109]
  AUTHORS   Stevenson-Paulik J, Odom AR, York JD.
  TITLE     Molecular and biochemical characterization of two plant inositol
            polyphosphate 6-/3-/5-kinases.
  JOURNAL   J. Biol. Chem. 277 (2002) 42711-8.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   4  [PMID:15531582]
  AUTHORS   Verbsky JW, Chang SC, Wilson MP, Mochizuki Y, Majerus PW.
  TITLE     The pathway for the production of inositol hexakisphosphate in human
            cells.
  JOURNAL   J. Biol. Chem. 280 (2005) 1911-20.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00562  Inositol phosphate metabolism
ORTHOLOGY   KO: K00328  inositol-polyphosphate multikinase
GENES       HSA: 253430(IPMK)
            PTR: 450471(IPMK)
            MMU: 69718(Ipmk)
            RNO: 171458(Ipmk)
            CFA: 488988(IPMK)
            GGA: 769967(IPMK)
            SCE: YDR173C(ARG82)
            AGO: AGOS_AGL144C
            UMA: UM04962.1
STRUCTURES  PDB: 2IEW  2IF8  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.151
            ExPASy - ENZYME nomenclature database: 2.7.1.151
            ExplorEnz - The Enzyme Database: 2.7.1.151
            ERGO genome analysis and discovery system: 2.7.1.151
            BRENDA, the Enzyme Database: 2.7.1.151
///
ENTRY       EC 2.7.1.152      Obsolete  Enzyme
NAME        Transferred to 2.7.4.21
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: now EC 2.7.4.21, inositol-hexakisphosphate kinase
            (EC 2.7.1.152 created 2002, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.152
            ExPASy - ENZYME nomenclature database: 2.7.1.152
            ExplorEnz - The Enzyme Database: 2.7.1.152
            ERGO genome analysis and discovery system: 2.7.1.152
            BRENDA, the Enzyme Database: 2.7.1.152
///
ENTRY       EC 2.7.1.153                Enzyme
NAME        phosphatidylinositol-4,5-bisphosphate 3-kinase;
            type I phosphoinositide 3-kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate
            3-phosphotransferase
REACTION    ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP +
            1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate [RN:R04545]
ALL_REAC    R04545
SUBSTRATE   ATP [CPD:C00002];
            1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [CPD:C04637]
PRODUCT     ADP [CPD:C00008];
            1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate [CPD:C05981]
COMMENT     This enzyme also catalyses the phosphorylation of PtdIns4P to
            PtdIns(3,4)P2, and of PtdIns to PtdIns3P. Four mammalian isoforms
            are known to exist.
REFERENCE   1  [PMID:11395417]
  AUTHORS   Vanhaesebroeck B, Leevers SJ, Ahmadi K, Timms J, Katso R, Driscoll
            PC, Woscholski R, Parker PJ, Waterfield MD.
  TITLE     Synthesis and function of 3-phosphorylated inositol lipids.
  JOURNAL   Annu. Rev. Biochem. 70 (2001) 535-602.
  ORGANISM  mammalian, Drosophila melanogaster [GN:dme], Caenorhabditis elegans
            [GN:cel], Dictyostelium discoideum [GN:ddi]
PATHWAY     PATH: map00562  Inositol phosphate metabolism
            PATH: map04012  ErbB signaling pathway
            PATH: map04070  Phosphatidylinositol signaling system
            PATH: map04150  mTOR signaling pathway
            PATH: map04210  Apoptosis
            PATH: map04370  VEGF signaling pathway
            PATH: map04510  Focal adhesion
            PATH: map04620  Toll-like receptor signaling pathway
            PATH: map04630  Jak-STAT signaling pathway
            PATH: map04650  Natural killer cell mediated cytotoxicity
            PATH: map04660  T cell receptor signaling pathway
            PATH: map04662  B cell receptor signaling pathway
            PATH: map04664  Fc epsilon RI signaling pathway
            PATH: map04670  Leukocyte transendothelial migration
            PATH: map04810  Regulation of actin cytoskeleton
            PATH: map04910  Insulin signaling pathway
            PATH: map04914  Progesterone-mediated oocyte maturation
            PATH: map04930  Type II diabetes mellitus
            PATH: map05210  Colorectal cancer
            PATH: map05211  Renal cell carcinoma
            PATH: map05212  Pancreatic cancer
            PATH: map05213  Endometrial cancer
            PATH: map05214  Glioma
            PATH: map05215  Prostate cancer
            PATH: map05218  Melanoma
            PATH: map05220  Chronic myeloid leukemia
            PATH: map05221  Acute myeloid leukemia
            PATH: map05222  Small cell lung cancer
            PATH: map05223  Non-small cell lung cancer
ORTHOLOGY   KO: K00922  phosphatidylinositol-4,5-bisphosphate 3-kinase
GENES       HSA: 5290(PIK3CA) 5291(PIK3CB) 5293(PIK3CD) 5294(PIK3CG)
            PTR: 457922(PIK3CD) 460858(PIK3CA) 463649(PIK3CG)
            MMU: 18706(Pik3ca) 18707(Pik3cd) 30955(Pik3cg) 74769(Pik3cb)
            RNO: 170911(Pik3ca) 298947(Pik3cg_predicted)
                 366508(Pik3cd_predicted) 85243(Pik3cb)
            CFA: 477085(PIK3CB) 483266(PIK3CG) 488084(PIK3CA) 489644(PIK3CD)
            BTA: 282306(PIK3CA) 504531(LOC504531) 517948(PIK3CB)
                 530001(MGC157122)
            SSC: 396979(PIK3CG)
            GGA: 417706(PIK3CG) 419444(PIK3CD) 424826(RCJMB04_1m2)
                 424971(PIK3CA)
            XTR: 780390(pik3cb)
            DRE: 394174(pik3cd) 561737(LOC561737)
            SPU: 588097(LOC588097)
            DDI: DDB_0214949(pikA)
            TCR: 510167.10
            EHI: 269.t00003 83.t00026
STRUCTURES  PDB: 2A4Z  2A5U  2CHW  2CHX  2CHZ  2V1Y  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.153
            ExPASy - ENZYME nomenclature database: 2.7.1.153
            ExplorEnz - The Enzyme Database: 2.7.1.153
            ERGO genome analysis and discovery system: 2.7.1.153
            BRENDA, the Enzyme Database: 2.7.1.153
///
ENTRY       EC 2.7.1.154                Enzyme
NAME        phosphatidylinositol-4-phosphate 3-kinase;
            type II phosphoinositide 3-kinase;
            C2-domain-containing phosphoinositide 3-kinase;
            phosphoinositide 3-kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:1-phosphatidyl-1D-myo-inositol-4-phosphate 3-phosphotransferase
REACTION    ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP +
            1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate [RN:R05795]
ALL_REAC    R05795
SUBSTRATE   ATP [CPD:C00002];
            1-phosphatidyl-1D-myo-inositol 4-phosphate [CPD:C01277]
PRODUCT     ADP [CPD:C00008];
            1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate [CPD:C11554]
COMMENT     This enzyme also phosphorylates PtdIns to PtdIns3P. Three mammalian
            isoforms have been found to date.
REFERENCE   1  [PMID:11395417]
  AUTHORS   Vanhaesebroeck B, Leevers SJ, Ahmadi K, Timms J, Katso R, Driscoll
            PC, Woscholski R, Parker PJ, Waterfield MD.
  TITLE     Synthesis and function of 3-phosphorylated inositol lipids.
  JOURNAL   Annu. Rev. Biochem. 70 (2001) 535-602.
  ORGANISM  mammalian, Drosophila melanogaster [GN:dme], Caenorhabditis elegans
            [GN:cel]
PATHWAY     PATH: map04070  Phosphatidylinositol signaling system
ORTHOLOGY   KO: K00923  phosphatidylinositol-4-phosphate 3-kinase
GENES       HSA: 5286(PIK3C2A) 5287(PIK3C2B) 5288(PIK3C2G)
            PTR: 457657(PIK3C2B)
            MMU: 18704(Pik3c2a) 18705(Pik3c2g)
            RNO: 116720(Pik3c2g) 289021(Pik3c2b_predicted)
                 361632(Pik3c2a_predicted)
            CFA: 478938(PIK3C2B) 485399(PIK3C2A)
            GGA: 418181(PIK3C2G) 419822(PIK3C2B) 423070(PIK3C2A)
            DME: Dmel_CG11621(Pi3K68D)
            CEL: F39B1.1
STRUCTURES  PDB: 2AR5  2B3R  2IWL  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.154
            ExPASy - ENZYME nomenclature database: 2.7.1.154
            ExplorEnz - The Enzyme Database: 2.7.1.154
            ERGO genome analysis and discovery system: 2.7.1.154
            BRENDA, the Enzyme Database: 2.7.1.154
///
ENTRY       EC 2.7.1.155      Obsolete  Enzyme
NAME        Transferred to 2.7.4.24
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
COMMENT     Transferred entry: diphosphoinositol-pentakisphosphate kinase. Now
            EC 2.7.4.24, diphosphoinositol-pentakisphosphate kinase. The enzyme
            had been incorrectly classified as the reaction involves transfer of
            a phospho group to another phospho group (EC 2.7.4) rather than to
            an hydroxy group (EC 2.7.1). (EC 2.7.1.155 created 2003, deleted
            2007)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.155
            ExPASy - ENZYME nomenclature database: 2.7.1.155
            ExplorEnz - The Enzyme Database: 2.7.1.155
            ERGO genome analysis and discovery system: 2.7.1.155
            BRENDA, the Enzyme Database: 2.7.1.155
///
ENTRY       EC 2.7.1.156                Enzyme
NAME        adenosylcobinamide kinase;
            CobU;
            adenosylcobinamide kinase/adenosylcobinamide-phosphate
            guanylyltransferase;
            AdoCbi kinase/AdoCbi-phosphate guanylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     RTP:adenosylcobinamide phosphotransferase
REACTION    RTP + adenosylcobinamide = adenosylcobinamide phosphate + RDP
            [RN:R05221 R06558]
ALL_REAC    R05221 R06558
SUBSTRATE   RTP;
            adenosylcobinamide
PRODUCT     adenosylcobinamide phosphate;
            RDP
COMMENT     In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC
            2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73)
            and CobS (EC 2.7.8.26) catalyse reactions in the nucleotide loop
            assembly pathway, which convert adenosylcobinamide (AdoCbi) into
            adenosylcobalamin (AdoCbl). CobT and CobC are involved in
            5,6-dimethylbenzimidazole activation whereby
            5,6-dimethylbenzimidazole is converted to its riboside,
            alpha-ribazole. The second branch of the nucleotide loop assembly
            pathway is the cobinamide (Cbi) activation branch where AdoCbi or
            adenosylcobinamide-phosphate is converted to the activated
            intermediate AdoCbi-GDP by Cob U. The final step in
            adenosylcobalamin biosynthesis is the condensation of AdoCbi-GDP
            with alpha-ribazole, which is catalysed by EC 2.7.8.26,
            adenosylcobinamide-GDP ribazoletransferase (CobS), to yield
            adenosylcobalamin. CobU is a bifunctional enzyme that has both
            kinase (EC 2.7.1.156) and guanylyltransferase (EC 2.7.7.62,
            adenosylcobinamide-phosphate guanylyltransferase) activities.
            However, both activities are not required at all times. The kinase
            activity has been proposed to function only when S. typhimurium is
            assimilating cobinamide whereas the guanylyltransferase activity is
            required for both assimilation of exogenous cobinamide and for de
            novo synthesis of adenosylcobalamin [4].
REFERENCE   1  [PMID:7559521]
  AUTHORS   O'Toole GA, Escalante-Semerena JC.
  TITLE     Purification and characterization of the bifunctional CobU enzyme of
            Salmonella typhimurium LT2. Evidence for a CobU-GMP intermediate.
  JOURNAL   J. Biol. Chem. 270 (1995) 23560-9.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:9601028]
  AUTHORS   Thompson TB, Thomas MG, Escalante-Semerena JC, Rayment I.
  TITLE     Three-dimensional structure of adenosylcobinamide
            kinase/adenosylcobinamide phosphate guanylyltransferase from
            Salmonella typhimurium determined to 2.3 A resolution,.
  JOURNAL   Biochemistry. 37 (1998) 7686-95.
  ORGANISM  Salmonella typhimurium
REFERENCE   3  [PMID:10529169]
  AUTHORS   Thompson TB, Thomas MG, Escalante-Semerena JC, Rayment I.
  TITLE     Three-dimensional structure of adenosylcobinamide
            kinase/adenosylcobinamide phosphate guanylyltransferase (CobU)
            complexed with GMP: evidence for a substrate-induced transferase
            active site.
  JOURNAL   Biochemistry. 38 (1999) 12995-3005.
  ORGANISM  Salmonella typhimurium
REFERENCE   4  [PMID:10869342]
  AUTHORS   Thomas MG, Thompson TB, Rayment I, Escalante-Semerena JC.
  TITLE     Analysis of the adenosylcobinamide
            kinase/adenosylcobinamide-phosphate guanylyltransferase (CobU)
            enzyme of Salmonella typhimurium LT2. Identification of residue
            His-46 as the site of guanylylation.
  JOURNAL   J. Biol. Chem. 275 (2000) 27576-86.
  ORGANISM  Salmonella typhimurium
REFERENCE   5  [PMID:12195810]
  AUTHORS   Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
  TITLE     The biosynthesis of adenosylcobalamin (vitamin B12).
  JOURNAL   Nat. Prod. Rep. 19 (2002) 390-412.
  ORGANISM  Pseudomonas denitrificans, Salmonella enterica, Bacillus megaterium
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K02231  adenosylcobinamide kinase / adenosylcobinamide-phosphate
                        guanylyltransferase
GENES       ECO: b1993(cobU)
            ECJ: JW1971(cobU)
            ECE: Z3153(cobU)
            ECS: ECs2788
            ECC: c2479(cobU)
            ECI: UTI89_C2231(cobU)
            ECP: ECP_1991
            ECV: APECO1_1074(cobU)
            ECW: EcE24377A_2275(cobU)
            ECX: EcHS_A2116(cobU)
            STY: STY2221(cobU)
            STT: t0856(cobU)
            SPT: SPA0853(cobU)
            SEC: SC2026(cobU)
            STM: STM2018(cobU)
            SFL: SF2061(cobU)
            SFV: SFV_2065(cobU)
            SSN: SSON_2054(cobU)
            SDY: SDY_2240(cobU)
            PLU: plu2986(cobU)
            XCC: XCC3060(cobU)
            XCB: XC_1098
            XCV: XCV3316(cobU)
            XAC: XAC3187(cobU)
            XOO: XOO1350(cobU)
            XOM: XOO_1240(XOO1240)
            VCH: VC1239
            VVU: VV1_2786
            VVY: VV1476
            VPA: VP1306
            PPR: PBPRB0995(cobU)
            PAE: PA1278(cobP)
            PAU: PA14_47680(cobP)
            PPU: PP_1678(cobP)
            PST: PSPTO_1714(cobP)
            PSB: Psyr_3675
            PSP: PSPPH_3696(cobP)
            PFL: PFL_4425(cobU)
            PFO: Pfl_1647
            PEN: PSEEN1384
            PMY: Pmen_1756
            SON: SO_1037(cobU)
            SFR: Sfri_0878
            SHE: Shewmr4_0844
            SHM: Shewmr7_3178
            SHN: Shewana3_3276
            CPS: CPS_3657(cobP)
            PHA: PSHAa2997(cobU)
            PAT: Patl_1137
            SDE: Sde_3204
            MCA: MCA0462(cobU)
            AEH: Mlg_2824
            HCH: HCH_00963(cobU)
            ABO: ABO_2380(cobU)
            CVI: CV_0495(cobU)
            RSO: RSc2391(cobP)
            REU: Reut_A0664
            RME: Rmet_2779
            BMA: BMA0696(cobU)
            BXE: Bxe_A3493
            BUR: Bcep18194_A5778
            BCN: Bcen_1836
            BCH: Bcen2424_2447
            BAM: Bamb_2495
            BPS: BPSL0986
            BPM: BURPS1710b_1199(cobU)
            BPL: BURPS1106A_1044(cobU)
            BPD: BURPS668_1038(cobU)
            BTE: BTH_I0843
            RFR: Rfer_2622
            POL: Bpro_2783
            MPT: Mpe_A2308(cobU) Mpe_B0511(cobU)
            HAR: HEAR0966(cobU)
            EBA: ebA4011(cobU)
            DAR: Daro_0147
            TBD: Tbd_2713
            MFA: Mfla_0113
            TDN: Tmden_0112
            ABU: Abu_2182(cobP)
            GSU: GSU3010(cobU)
            GME: Gmet_0466
            PCA: Pcar_0487(cobP)
            PPD: Ppro_2805
            DVU: DVU1007(cobU)
            DDE: Dde_3495
            DPS: DP1953(cobP)
            SFU: Sfum_2608
            MLO: mll1308
            SME: SMc04305(cobP)
            SMD: Smed_1761
            ATU: Atu1542(cobU)
            ATC: AGR_C_2839(cobP)
            RET: RHE_CH02491(cobP)
            RLE: RL2832(cobP)
            BME: BMEI0693
            BMF: BAB1_1328(cobU)
            BMS: BR1308(cobU)
            BMB: BruAb1_1309(cobU)
            BJA: bll3256(cobP)
            BRA: BRADO4911(cobU)
            BBT: BBta_3140(cobU)
            RPA: RPA0714(cobU)
            RPB: RPB_0740
            RPC: RPC_3747
            RPD: RPD_0638
            RPE: RPE_2234
            SIL: SPO0405
            SIT: TM1040_0455
            RSP: RSP_0602
            RSH: Rsph17029_2255
            JAN: Jann_0905
            RDE: RD1_1196(cobP)
            PDE: Pden_1568
            HNE: HNE_1521(cobU)
            NAR: Saro_0322
            GBE: GbCGDNIH1_0656
            RRU: Rru_A0670
            MAG: amb4425
            MGM: Mmc1_2375
            BHA: BH1590(cobP)
            GKA: GK2261
            LMO: lmo1147
            LMF: LMOf2365_1154(cobU)
            LIN: lin1111
            LWE: lwe1105(cobU)
            SSA: SSA_0489(cobU)
            STH: STH1928
            CAC: CAC1383(CobU)
            CPE: CPE1035
            CPF: CPF_1290
            CPR: CPR_1109
            CTC: CTC00718
            CNO: NT01CX_2078
            CDF: CD3438(cobU)
            CBA: CLB_0950(cobU)
            CBH: CLC_0964(cobU)
            CBF: CLI_0996(cobU)
            CKL: CKL_0731(cobU)
            CHY: CHY_0768(cobP)
            DSY: DSY2115(cobU)
            TTE: TTE0381(cobU)
            MTU: Rv0254c(cobU)
            MTC: MT0267(cobU)
            MBO: Mb0260c(cobU)
            MPA: MAP1947(cobU)
            MAV: MAV_2284(cobU)
            MSM: MSMEG_4274(cobU)
            MMC: Mmcs_3304
            CGL: NCgl2119(cgl2199)
            CGB: cg2413(cobU)
            CEF: CE2091
            CDI: DIP1633(cobU)
            NFA: nfa17010(cobU)
            RHA: RHA1_ro01144(cobU)
            SCO: SCO2173(SC5F7.28)
            SMA: SAV6032(cobU)
            PAC: PPA0441
            TFU: Tfu_0997
            FRA: Francci3_3129
            FAL: FRAAL5138(cobU)
            ACE: Acel_0941
            SEN: SACE_1651(cobU)
            RXY: Rxyl_0652
            FNU: FN0913
            TDE: TDE2382(cobU)
            LIL: LB152(cobP)
            LIC: LIC20122(cobU)
            LBJ: LBJ_4190(cobU)
            LBL: LBL_4205(cobU)
            SYN: slr0216(cobP)
            SYW: SYNW1216(cobU)
            SYC: syc0554_d(cobP)
            SYF: Synpcc7942_0990
            SYD: Syncc9605_1328
            SYE: Syncc9902_1146
            SYG: sync_1327
            SYR: SynRCC307_1234(cobU)
            SYX: SynWH7803_1122(cobU)
            CYA: CYA_2240
            CYB: CYB_0367(cobU)
            TEL: tll1104(cobP)
            GVI: glr0747(cobP)
            ANA: all3174
            AVA: Ava_3872
            PMA: Pro0974(cobU)
            PMM: PMM0863(cobU)
            PMT: PMT0749(cobU)
            PMN: PMN2A_0345
            PMI: PMT9312_0938
            PMB: A9601_09991(cobU)
            PMC: P9515_09441(cobU)
            PMF: P9303_14681(cobU)
            PMG: P9301_09971(cobU)
            PMH: P9215_10301(cobU)
            PME: NATL1_10181(cobU)
            TER: Tery_3432
            BFR: BF2485
            BFS: BF2518(cobP)
            PGI: PG0701(cobU)
            FPS: FP1461(cobU)
            CTE: CT0945(cobP)
            CCH: Cag_0846(cobP)
            CPH: Cpha266_0998
            PLT: Plut_1133
            DET: DET0660(cobU-1) DET0694(cobU-2)
            DEH: cbdb_A644(cobU)
            DRA: DR_A0020
            DGE: Dgeo_2873
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.156
            ExPASy - ENZYME nomenclature database: 2.7.1.156
            ExplorEnz - The Enzyme Database: 2.7.1.156
            ERGO genome analysis and discovery system: 2.7.1.156
            BRENDA, the Enzyme Database: 2.7.1.156
///
ENTRY       EC 2.7.1.157                Enzyme
NAME        N-acetylgalactosamine kinase;
            GALK2;
            GK2;
            GalNAc kinase;
            N-acetylgalactosamine (GalNAc)-1-phosphate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:N-acetyl-D-galactosamine 1-phosphotransferase
REACTION    ATP + N-acetyl-D-galactosamine = ADP +
            N-acetyl-alpha-D-galactosamine 1-phosphate
SUBSTRATE   ATP [CPD:C00002];
            N-acetyl-D-galactosamine [CPD:C01132]
PRODUCT     ADP [CPD:C00008];
            N-acetyl-alpha-D-galactosamine 1-phosphate
COMMENT     The enzyme is highly specific for GalNAc as substrate, but has
            slight activity with D-galactose [2]. Requires Mg2+, Mn2+ or Co2+
            for activity, with Mg2+ resulting in by far the greatest stimulation
            of enzyme activity.
REFERENCE   1  [PMID:8702831]
  AUTHORS   Pastuszak I, Drake R, Elbein AD.
  TITLE     Kidney N-acetylgalactosamine (GalNAc)-1-phosphate kinase, a new
            pathway of GalNAc activation.
  JOURNAL   J. Biol. Chem. 271 (1996) 20776-82.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:8798585]
  AUTHORS   Pastuszak I, O'Donnell J, Elbein AD.
  TITLE     Identification of the GalNAc kinase amino acid sequence.
  JOURNAL   J. Biol. Chem. 271 (1996) 23653-6.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:16006554]
  AUTHORS   Thoden JB, Holden HM.
  TITLE     The molecular architecture of human N-acetyl galactosamine kinase.
  JOURNAL   J. Biol. Chem.  (2005) .
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.157
            ExPASy - ENZYME nomenclature database: 2.7.1.157
            ExplorEnz - The Enzyme Database: 2.7.1.157
            ERGO genome analysis and discovery system: 2.7.1.157
            BRENDA, the Enzyme Database: 2.7.1.157
///
ENTRY       EC 2.7.1.158                Enzyme
NAME        inositol-pentakisphosphate 2-kinase;
            IP5 2-kinase;
            Gsl1p;
            Ipk1p;
            inositol polyphosphate kinase;
            inositol 1,3,4,5,6-pentakisphosphate 2-kinase;
            Ins(1,3,4,5,6)P5 2-kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:1D-myo-inositol 1,3,4,5,6-pentakisphosphate 2-phosphotransferase
REACTION    ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate = ADP +
            1D-myo-inositol hexakisphosphate [RN:R05202]
ALL_REAC    R05202
SUBSTRATE   ATP [CPD:C00002];
            1D-myo-inositol 1,3,4,5,6-pentakisphosphate [CPD:C01284]
PRODUCT     ADP [CPD:C00008];
            1D-myo-inositol hexakisphosphate [CPD:C01204]
COMMENT     The enzyme can also use Ins(1,4,5,6)P4 [2] and Ins(1,4,5)P3 [3] as
            substrate. Inositol hexakisphosphate (phytate) accumulates in
            storage protein bodies during seed development and, when hydrolysed,
            releases stored nutrients to the developing seedling before the
            plant is capable of absorbing nutrients from its environment [5].
REFERENCE   1  [PMID:10390371]
  AUTHORS   York JD, Odom AR, Murphy R, Ives EB, Wente SR.
  TITLE     A phospholipase C-dependent inositol polyphosphate kinase pathway
            required for efficient messenger RNA export.
  JOURNAL   Science. 285 (1999) 96-100.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:7961779]
  AUTHORS   Phillippy BQ, Ullah AH, Ehrlich KC.
  TITLE     Purification and some properties of inositol
            1,3,4,5,6-Pentakisphosphate 2-kinase from immature soybean seeds.
  JOURNAL   J. Biol. Chem. 269 (1994) 28393-9.
  ORGANISM  Glycine max [GN:egma]
REFERENCE   3
  AUTHORS   Phillippy, B.Q., Ullah, A.H. and Ehrlich, K.C.
  TITLE     Additions and corrections to Purification and some properties of
            inositol 1,3,4,5,6-pentakisphosphate 2-kinase from immature soybean
            seeds.
  JOURNAL   J. Biol. Chem. 270 (1997) 7782.
REFERENCE   4  [PMID:9794810]
  AUTHORS   Ongusaha PP, Hughes PJ, Davey J, Michell RH.
  TITLE     Inositol hexakisphosphate in Schizosaccharomyces pombe: synthesis
            from Ins(1,4,5)P3 and osmotic regulation.
  JOURNAL   Biochem. J. 335 ( Pt 3) (1998) 671-9.
  ORGANISM  Schizosaccharomyces pombe [GN:spo]
REFERENCE   5  [PMID:15459192]
  AUTHORS   Miller AL, Suntharalingam M, Johnson SL, Audhya A, Emr SD, Wente SR.
  TITLE     Cytoplasmic inositol hexakisphosphate production is sufficient for
            mediating the Gle1-mRNA export pathway.
  JOURNAL   J. Biol. Chem. 279 (2004) 51022-32.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   6  [PMID:12226109]
  AUTHORS   Stevenson-Paulik J, Odom AR, York JD.
  TITLE     Molecular and biochemical characterization of two plant inositol
            polyphosphate 6-/3-/5-kinases.
  JOURNAL   J. Biol. Chem. 277 (2002) 42711-8.
  ORGANISM  Arabidopsis thaliana [GN:ath], Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.158
            ExPASy - ENZYME nomenclature database: 2.7.1.158
            ExplorEnz - The Enzyme Database: 2.7.1.158
            ERGO genome analysis and discovery system: 2.7.1.158
            BRENDA, the Enzyme Database: 2.7.1.158
///
ENTRY       EC 2.7.1.159                Enzyme
NAME        inositol-1,3,4-trisphosphate 5/6-kinase;
            Ins(1,3,4)P3 5/6-kinase;
            inositol trisphosphate 5/6-kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     ATP:1D-myo-inositol 1,3,4-trisphosphate 5-phosphotransferase
REACTION    (1) ATP + 1D-myo-inositol 1,3,4-trisphosphate = ADP +
            1D-myo-inositol 1,3,4,5-tetrakisphosphate [RN:R03428];
            (2) ATP + 1D-myo-inositol 1,3,4-trisphosphate = ADP +
            1D-myo-inositol 1,3,4,6-tetrakisphosphate [RN:R03429]
ALL_REAC    R03428 R03429
SUBSTRATE   ATP [CPD:C00002];
            1D-myo-inositol 1,3,4-trisphosphate [CPD:C01243]
PRODUCT     ADP [CPD:C00008];
            1D-myo-inositol 1,3,4,5-tetrakisphosphate [CPD:C01272];
            1D-myo-inositol 1,3,4,6-tetrakisphosphate [CPD:C04477]
COMMENT     In humans, this enzyme, along with EC 2.7.1.127
            (inositol-trisphosphate 3-kinase), EC 2.7.1.140
            (inositol-tetrakisphosphate 5-kinase) and EC 2.7.1.158 (inositol
            pentakisphosphate 2-kinase) is involved in the production of
            inositol hexakisphosphate (InsP6). InsP6 is involved in many
            cellular processes, including mRNA export from the nucleus [2].
            Yeasts do not have this enzyme, so produce InsP6 from Ins(1,4,5)P3
            by the actions of EC 2.7.1.151 (inositol-polyphosphate multikinase)
            and EC 2.7.1.158 (inositol-pentakisphosphate 2-kinase) [2].
REFERENCE   1  [PMID:8662638]
  AUTHORS   Wilson MP, Majerus PW.
  TITLE     Isolation of inositol 1,3,4-trisphosphate 5/6-kinase, cDNA cloning
            and expression of the recombinant enzyme.
  JOURNAL   J. Biol. Chem. 271 (1996) 11904-10.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:15531582]
  AUTHORS   Verbsky JW, Chang SC, Wilson MP, Mochizuki Y, Majerus PW.
  TITLE     The pathway for the production of inositol hexakisphosphate in human
            cells.
  JOURNAL   J. Biol. Chem. 280 (2005) 1911-20.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:15837423]
  AUTHORS   Miller GJ, Wilson MP, Majerus PW, Hurley JH.
  TITLE     Specificity determinants in inositol polyphosphate synthesis:
            crystal structure of inositol 1,3,4-trisphosphate 5/6-kinase.
  JOURNAL   Mol. Cell. 18 (2005) 201-12.
ORTHOLOGY   KO: K01765  inositol-1,3,4-trisphosphate 5/6-kinase
GENES       HSA: 3705(ITPK1)
            MMU: 217837(Itpk1)
            CFA: 490591(ITPK1)
            BTA: 518488(LOC518488)
            GGA: 423421(ITPK1)
            XLA: 379828(itpk1)
            XTR: 549890(itpk1)
            DRE: 406290(itpk1)
            SPU: 580408(LOC580408)
            TET: TTHERM_00530360
            EHI: 151.t00008
STRUCTURES  PDB: 2ODT  2Q7D  2QB5  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.159
            ExPASy - ENZYME nomenclature database: 2.7.1.159
            ExplorEnz - The Enzyme Database: 2.7.1.159
            ERGO genome analysis and discovery system: 2.7.1.159
            BRENDA, the Enzyme Database: 2.7.1.159
///
ENTRY       EC 2.7.1.160                Enzyme
NAME        2'-phosphotransferase;
            yeast 2'-phosphotransferase;
            Tpt1;
            Tpt1p;
            2'-phospho-tRNA:NAD+ phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
SYSNAME     2'-phospho-[ligated tRNA]:NAD+ phosphotransferase
REACTION    2'-phospho-[ligated tRNA] + NAD+ = mature tRNA + ADP-ribose
            1'',2''-phosphate + nicotinamide + H2O
SUBSTRATE   2'-phospho-[ligated tRNA];
            NAD+ [CPD:C00003]
PRODUCT     mature tRNA;
            ADP-ribose 1'',2''-phosphate;
            nicotinamide [CPD:C00153];
            H2O [CPD:C00001]
COMMENT     Catalyses the final step of tRNA splicing in the yeast Saccharomyces
            cerevisiae [2]. The reaction takes place in two steps: in the first
            step, the 2'-phosphate on the RNA substrate is ADP-ribosylated,
            causing the relase of nicotinamide and the formation of the reaction
            intermediate, ADP-ribosylated tRNA [6]. In the second step,
            dephosphorylated (mature) tRNA is formed along with ADP ribose
            1''-2''-cyclic phosphate. Highly specific for oligonucleotide
            substrates bearing an internal 2'-phosphate. Oligonucleotides with
            only a terminal 5'- or 3'-phosphate are not substrates [1].
REFERENCE   1  [PMID:11705403]
  AUTHORS   Steiger MA, Kierzek R, Turner DH, Phizicky EM.
  TITLE     Substrate recognition by a yeast 2'-phosphotransferase involved in
            tRNA splicing and by its Escherichia coli homolog.
  JOURNAL   Biochemistry. 40 (2001) 14098-105.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], Escherichia coli [GN:eco]
REFERENCE   2  [PMID:9915792]
  AUTHORS   Spinelli SL, Kierzek R, Turner DH, Phizicky EM.
  TITLE     Transient ADP-ribosylation of a 2'-phosphate implicated in its
            removal from ligated tRNA during splicing in yeast.
  JOURNAL   J. Biol. Chem. 274 (1999) 2637-44.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], Escherichia coli [GN:eco], mouse
            [GN:mmu]
REFERENCE   3  [PMID:9148937]
  AUTHORS   Culver GM, McCraith SM, Consaul SA, Stanford DR, Phizicky EM.
  TITLE     A 2'-phosphotransferase implicated in tRNA splicing is essential in
            Saccharomyces cerevisiae.
  JOURNAL   J. Biol. Chem. 272 (1997) 13203-10.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], human [GN:hsa]
REFERENCE   4  [PMID:2050693]
  AUTHORS   McCraith SM, Phizicky EM.
  TITLE     An enzyme from Saccharomyces cerevisiae uses NAD+ to transfer the
            splice junction 2'-phosphate from ligated tRNA to an acceptor
            molecule.
  JOURNAL   J. Biol. Chem. 266 (1991) 11986-92.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   5  [PMID:14504659]
  AUTHORS   Hu QD, Lu H, Huo K, Ying K, Li J, Xie Y, Mao Y, Li YY.
  TITLE     A human homolog of the yeast gene encoding tRNA
            2'-phosphotransferase: cloning, characterization and complementation
            analysis.
  JOURNAL   Cell. Mol. Life. Sci. 60 (2003) 1725-32.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   6  [PMID:15611300]
  AUTHORS   Steiger MA, Jackman JE, Phizicky EM.
  TITLE     Analysis of 2'-phosphotransferase (Tpt1p) from Saccharomyces
            cerevisiae: evidence for a conserved two-step reaction mechanism.
  JOURNAL   RNA. 11 (2005) 99-106.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], Escherichia coli [GN:eco]
REFERENCE   7  [PMID:15611301]
  AUTHORS   Sawaya R, Schwer B, Shuman S.
  TITLE     Structure-function analysis of the yeast NAD+-dependent tRNA
            2'-phosphotransferase Tpt1.
  JOURNAL   RNA. 11 (2005) 107-13.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], Escherichia coli [GN:eco]
REFERENCE   8  [PMID:15811369]
  AUTHORS   Kato-Murayama M, Bessho Y, Shirouzu M, Yokoyama S.
  TITLE     Crystal structure of the RNA 2'-phosphotransferase from Aeropyrum
            pernix K1.
  JOURNAL   J. Mol. Biol. 348 (2005) 295-305.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], Aeropyrum pernix [GN:ape]
GENES       DRE: 503604(zgc:113138)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.1.160
            ExPASy - ENZYME nomenclature database: 2.7.1.160
            ExplorEnz - The Enzyme Database: 2.7.1.160
            ERGO genome analysis and discovery system: 2.7.1.160
            BRENDA, the Enzyme Database: 2.7.1.160
///
ENTRY       EC 2.7.1.-                  Enzyme
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with an alcohol group as acceptor
REACTION    (1) Nicotinate D-ribonucleotide + ADP <=> Nicotinate
            D-ribonucleoside + ATP [RN:R03347];
            (2) myo-Inositol hexakisphosphate + ADP <=> 1D-myo-Inositol
            1,3,4,5,6-pentakisphosphate + ATP [RN:R05202];
            (3) Phenol + Alkylphosphonate <=> Phenolic phosphate + Alkane
            [RN:R05625]
SUBSTRATE   Nicotinate D-ribonucleotide [CPD:C01185];
            ADP [CPD:C00008];
            myo-Inositol hexakisphosphate [CPD:C01204];
            Phenol [CPD:C00146];
            Alkylphosphonate [CPD:C06235];
            Trehalose [GL:G00293]
PRODUCT     Nicotinate D-ribonucleoside [CPD:C05841];
            ATP [CPD:C00002];
            1D-myo-Inositol 1,3,4,5,6-pentakisphosphate [CPD:C01284];
            Phenolic phosphate [CPD:C02734];
            Alkane [CPD:C01371];
            Trehalose 6-phosphate [GL:G09795]
///
ENTRY       EC 2.7.2.1                  Enzyme
NAME        acetate kinase;
            acetokinase;
            AckA;
            AK;
            acetic kinase;
            acetate kinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a carboxy group as acceptor
SYSNAME     ATP:acetate phosphotransferase
REACTION    (1) ATP + acetate = ADP + acetyl phosphate [RN:R00315];
            (2) ATP + propanoate = ADP + propanoyl phosphate [RN:R01353]
ALL_REAC    R00315 R01353
SUBSTRATE   ATP [CPD:C00002];
            acetate [CPD:C00033];
            propanoate [CPD:C00163]
PRODUCT     ADP [CPD:C00008];
            acetyl phosphate [CPD:C00227];
            propanoyl phosphate [CPD:C02876]
COMMENT     Requires Mg2+ for activity. While purified enzyme from Escherichia
            coli is specific for acetate [4], others have found that the enzyme
            can also use propanoate as a substrate, but more slowly [7]. Acetate
            can be converted into the key metabolic intermediate acetyl-CoA by
            coupling acetate kinase with EC 2.3.1.8, phosphate
            acetyltransferase. Both this enzyme and EC 2.7.2.15, propionate
            kinase, play important roles in the production of propanoate [9].
REFERENCE   1  [PMID:6956338]
  AUTHORS   Romain Y, Demassieux S, Carriere S.
  TITLE     Partial purification and characterization of two isoenzymes involved
            in the sulfurylation of catecholamines.
  JOURNAL   Biochem. Biophys. Res. Commun. 106 (1982) 999-1005.
REFERENCE   2  [PMID:13174550]
  AUTHORS   ROMANO AH, NICKERSON WJ.
  TITLE     Cystine reductase of pea seeds and yeasts.
  JOURNAL   J. Biol. Chem. 208 (1954) 409-16.
REFERENCE   3  [PMID:14850456]
  AUTHORS   STERN JR, OCHOA S.
  TITLE     Enzymatic synthesis of citric acid. I. Synthesis with soluble
            enzymes.
  JOURNAL   J. Biol. Chem. 191 (1951) 161-72.
REFERENCE   4  [PMID:3020034]
  AUTHORS   Fox DK, Roseman S.
  TITLE     Isolation and characterization of homogeneous acetate kinase from
            Salmonella typhimurium and Escherichia coli.
  JOURNAL   J. Biol. Chem. 261 (1986) 13487-97.
  ORGANISM  Salmonella typhimurium, Escherichia coli [GN:eco]
REFERENCE   5  [PMID:11716215]
  AUTHORS   Knorr R, Ehrmann MA, Vogel RF.
  TITLE     Cloning, expression, and characterization of acetate kinase from
            Lactobacillus sanfranciscensis.
  JOURNAL   Microbiol. Res. 156 (2001) 267-77.
  ORGANISM  Lactobacillus sanfranciscensis
REFERENCE   6  [PMID:11133963]
  AUTHORS   Buss KA, Cooper DR, Ingram-Smith C, Ferry JG, Sanders DA, Hasson MS.
  TITLE     Urkinase: structure of acetate kinase, a member of the ASKHA
            superfamily of phosphotransferases.
  JOURNAL   J. Bacteriol. 183 (2001) 680-6.
  ORGANISM  Escherichia coli [GN:eco], Methanosarcina thermophila
REFERENCE   7  [PMID:15774882]
  AUTHORS   Ingram-Smith C, Gorrell A, Lawrence SH, Iyer P, Smith K, Ferry JG.
  TITLE     Characterization of the acetate binding pocket in the Methanosarcina
            thermophila acetate kinase.
  JOURNAL   J. Bacteriol. 187 (2005) 2386-94.
  ORGANISM  Methanosarcina thermophila
REFERENCE   8  [PMID:15647264]
  AUTHORS   Gorrell A, Lawrence SH, Ferry JG.
  TITLE     Structural and kinetic analyses of arginine residues in the active
            site of the acetate kinase from Methanosarcina thermophila.
  JOURNAL   J. Biol. Chem. 280 (2005) 10731-42.
  ORGANISM  Methanosarcina thermophila
REFERENCE   9  [PMID:9484901]
  AUTHORS   Hesslinger C, Fairhurst SA, Sawers G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that degrades
            L-threonine to propionate.
  JOURNAL   Mol. Microbiol. 27 (1998) 477-92.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00430  Taurine and hypotaurine metabolism
            PATH: map00620  Pyruvate metabolism
            PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K00925  acetate kinase
GENES       ANI: AN4914.2
            AFM: AFUA_3G10750
            AOR: AO090003000624
            CNE: CNN01560
            UMA: UM03413.1
            EHI: 19.t00045
            ECO: b2296(ackA)
            ECJ: JW2293(ackA)
            ECE: Z3558(ackA)
            ECS: ECs3180
            ECC: c2838(ackA)
            ECI: UTI89_C2579
            ECP: ECP_2335
            ECV: APECO1_2288 APECO1_4268(ackA)
            ECW: EcE24377A_2590(ackA)
            ECX: EcHS_A2446
            STY: STY2567(ackA)
            STT: t0527(ackA)
            SPT: SPA0527(ackA)
            SEC: SC2338(ackA)
            STM: STM2337(ackA)
            YPE: YPO2566(ackA)
            YPK: y1622(ackA)
            YPM: YP_2377(ackA)
            YPA: YPA_2055
            YPN: YPN_2158
            YPP: YPDSF_1973
            YPS: YPTB2597(ackA)
            YPI: YpsIP31758_1443(ackA)
            SFL: SF2372(ackA)
            SFX: S2507(ackA)
            SFV: SFV_2363(ackA)
            SSN: SSON_2353(ackA)
            SBO: SBO_2331(ackA)
            SDY: SDY_2492(ackA)
            ECA: ECA3039(ackA)
            PLU: plu3095(ackA)
            BUC: BU175(ackA)
            BAS: BUsg169(ackA)
            BAB: bbp164(ackA)
            BCC: BCc_114(ackA)
            WBR: WGLp181(ackA)
            SGL: SG1606
            HIT: NTHI1375(ackA)
            HIP: CGSHiEE_06020
            HIQ: CGSHiGG_09740
            HDU: HD1456(ackA)
            HSO: HS_0803(ackA)
            PMU: PM0704(ackA)
            MSU: MS0999(ackA)
            APL: APL_0645(ackA)
            VCH: VC1098 VCA0235
            VCO: VC0395_0994(ackA-2) VC0395_A0616(ackA-1)
            VVU: VV1_2221 VV2_0148
            VVY: VV2133 VVA0658
            VPA: VP2082 VPA0611
            VFI: VF0837 VFA0794
            PPR: PBPRA2798 PBPRB0074
            PAE: PA0836
            PAU: PA14_53470(ackA)
            PAP: PSPA7_4684(ackA)
            PST: PSPTO_1669(tdcD)
            PAR: Psyc_0197
            PCR: Pcryo_0217
            PRW: PsycPRwf_0346
            ACI: ACIAD0541(ack)
            ACB: A1S_0482
            SON: SO_2915(ackA)
            SDN: Sden_2409
            SFR: Sfri_2476
            SAZ: Sama_1495
            SBL: Sbal_2674
            SLO: Shew_2393
            SHE: Shewmr4_1491
            SHM: Shewmr7_1558
            SHN: Shewana3_1552 Shewana3_2650
            SHW: Sputw3181_1628
            CPS: CPS_3176(ackA)
            PAT: Patl_2590
            PIN: Ping_3311
            MAQ: Maqu_1133
            LPN: lpg2262(ackA2)
            LPF: lpl2188(ack)
            LPP: lpp2216(ack)
            MCA: MCA1589(ackA)
            FTU: FTT1753(tdcD)
            FTF: FTF1753(tdcD)
            FTW: FTW_1991(ackA)
            FTL: FTL_0015
            FTH: FTH_0015(ackA)
            FTA: FTA_0017(ackA)
            FTN: FTN_0125(ackA)
            NOC: Noc_2716
            AEH: Mlg_2377
            HCH: HCH_04450(ackA)
            AHA: AHA_0891(ackA-1) AHA_3586(ackA-2)
            DNO: DNO_0447(ackA)
            BCI: BCI_0382(ackA)
            NME: NMB0435 NMB1518
            NMA: NMA1718(ackA1) NMA2050(ackA2)
            NMC: NMC1447(ackA1) NMC1727(ackA2)
            NGO: NGO0977 NGO1521
            CVI: CV_1531(ackA) CV_3745
            REU: Reut_A0625 Reut_A1203
            REH: H16_A0670(ackA2) H16_B1630(ackA)
            RME: Rmet_0562
            BMA: BMAA0120(ackA)
            BMV: BMASAVP1_1285(ackA)
            BMN: BMA10247_A0144(ackA)
            BXE: Bxe_B0356 Bxe_B1346 Bxe_C0051
            BUR: Bcep18194_B2633
            BCN: Bcen_3495
            BCH: Bcen2424_4871
            BPS: BPSS1956
            BPM: BURPS1710b_A1060(ackA)
            BPL: BURPS1106A_A2656(ackA)
            BPD: BURPS668_A2799(ackA)
            BTE: BTH_II0416(ackA)
            BPE: BP1003(ackA)
            BPA: BPP1168(ackA)
            BBR: BB1384(ackA)
            RFR: Rfer_2975
            HAR: HEAR1515
            NEU: NE2134(ackA2)
            NET: Neut_2086
            NMU: Nmul_A0992
            EBA: ebA2248(ackA)
            AZO: azo3639(ackA)
            DAR: Daro_0974 Daro_2099 Daro_2921
            TBD: Tbd_0832
            MFA: Mfla_0741
            HPJ: jhp0840(ackA)
            HPA: HPAG1_0883 HPAG1_0884
            HHE: HH1308(ackA)
            HAC: Hac_1289(ackA)
            TDN: Tmden_0056
            CJE: Cj0689(ackA)
            CJR: CJE0788(ackA)
            CJJ: CJJ81176_0712(ackA)
            CJU: C8J_0657(ackA)
            CJD: JJD26997_1318(ackA)
            CFF: CFF8240_0812(ackA)
            CCV: CCV52592_1158(ackA)
            CHA: CHAB381_1162(ackA)
            CCO: CCC13826_0104(ackA)
            ABU: Abu_0492(ackA1) Abu_0494(ackA2) Abu_0496(ackA3)
            SUN: SUN_1996
            GSU: GSU2707(ackA-1) GSU3448(ackA-2)
            GME: Gmet_0149 Gmet_1034
            PCA: Pcar_0557 Pcar_2427 Pcar_2543
            DVU: DVU3030(ackA)
            DDE: Dde_3242
            LIP: LI0280(ackA)
            DPS: DP0559
            ADE: Adeh_2897 Adeh_3116 Adeh_3910
            SFU: Sfum_1473
            RPR: RP110
            RTY: RT0026(ackA)
            RCO: RC0148 RC0149 RC0150
            RFE: RF_0097(ackA)
            RBE: RBE_1212(ackA)
            MLO: mlr6576
            MES: Meso_2235
            SME: SMb21184(ackA2)
            RET: RHE_CH03441(ackA)
            RLE: RL1886(pduW) RL3901(ackA)
            BME: BMEII0880
            BMF: BAB2_0835
            BMS: BRA0386
            BMB: BruAb2_0815
            BOV: BOV_A0334(ackA)
            BJA: bll2517 blr3458(ackA2)
            BRA: BRADO1872(tdcD) BRADO6361(ackA)
            BBT: BBta_2189(tdcD) BBta_2655(ackA) BBta_7294(ackA)
            RPA: RPA4566(ackA)
            RPB: RPB_1027
            RPC: RPC_0642 RPC_0833 RPC_1078 RPC_1180 RPC_2006 RPC_3806
            RPD: RPD_1128
            RPE: RPE_3162 RPE_3862
            NWI: Nwi_1948
            NHA: Nham_0865 Nham_1895 Nham_4372
            SIL: SPO0116(ackA)
            RSP: RSP_1254
            RDE: RD1_3831(ackA)
            MMR: Mmar10_0189
            ACR: Acry_3055
            RRU: Rru_A0920 Rru_A1379 Rru_A1467 Rru_A2998
            MAG: amb2554
            BSU: BG10813(ackA)
            BHA: BH3192(ackA)
            BAN: BA4888(ackA)
            BAR: GBAA4888(ackA)
            BAA: BA_5309
            BAT: BAS4535
            BCE: BC4637
            BCA: BCE_4773(ackA)
            BCZ: BCZK4381(ackA)
            BTK: BT9727_4371(ackA)
            BTL: BALH_4215(ackA)
            BLI: BL00419(ackA)
            BLD: BLi03086(ackA)
            BCL: ABC2740(ackA)
            BAY: RBAM_026400
            BPU: BPUM_2579
            OIH: OB2191(ackA)
            GKA: GK2785
            SAU: SA1533(ackA)
            SAV: SAV1711(ackA)
            SAM: MW1654(ackA)
            SAR: SAR1789(ackA)
            SAS: SAS1638
            SAC: SACOL1760(ackA)
            SAB: SAB1570c(ackA)
            SAA: SAUSA300_1657(ackA)
            SAO: SAOUHSC_01820
            SEP: SE1387
            SER: SERP1275(ackA)
            SHA: SH1214
            SSP: SSP1054
            LMO: lmo1168(AckA2) lmo1581(ackA)
            LMF: LMOf2365_1176 LMOf2365_1603(ackA)
            LIN: lin1132(AckA2) lin1616(ackA)
            LWE: lwe1126(ackA2) lwe1594(ackA)
            LLA: L0224(ackA2) L73818(ackA1)
            LLC: LACR_2294 LACR_2295
            LLM: llmg_2288(ackA2) llmg_2289(ackA1)
            SPY: SPy_0109(ackA)
            SPZ: M5005_Spy_0094(ackA)
            SPM: spyM18_0111
            SPG: SpyM3_0086(ackA)
            SPS: SPs0087
            SPH: MGAS10270_Spy0096(ackA)
            SPI: MGAS10750_Spy0101(ackA)
            SPJ: MGAS2096_Spy0097(ackA)
            SPK: MGAS9429_Spy0095(ackA)
            SPF: SpyM50092(ackA)
            SPA: M6_Spy0142
            SPB: M28_Spy0092(ackA)
            SPN: SP_2044
            SPR: spr1854(ackA)
            SPD: SPD_1853(ackA)
            SAG: SAG0168(ackA)
            SAN: gbs0167(ackA)
            SAK: SAK_0234(ackA)
            SMU: SMU.1978(ackA)
            STC: str1857(ackA)
            STL: stu1857(ackA)
            SSA: SSA_0192(ackA) SSA_0541
            SGO: SGO_1916(ackA)
            LPL: lp_0210(ack1) lp_0310(ack2) lp_2242(ack3)
            LJO: LJ0485 LJ0912
            LAC: LBA0463(ackA) LBA0741(ackB) LBA1493(ackB) LBA1873(ackA)
            LSA: LSA0198(ack1) LSA1298(ack2) LSA1668(ack3)
            LSL: LSL_1114(ackA) LSL_1323(ackA)
            LDB: Ldb0686(ack)
            LBU: LBUL_0618
            LBR: LVIS_0129 LVIS_1190 LVIS_1601
            LCA: LSEI_0166 LSEI_2172
            LGA: LGAS_0431
            EFA: EF1983(ackA)
            OOE: OEOE_1249
            STH: STH2585
            CAC: CAC1743(askA)
            CPE: CPE0217(ackA) CPE1724(ackB)
            CPF: CPF_0208(ackA) CPF_1977(ackA)
            CPR: CPR_0206(ackA) CPR_1695(ackA)
            CTC: CTC01240
            CNO: NT01CX_2224(ackA)
            CTH: Cthe_1028
            CDF: CD1175(ackA)
            CBO: CBO2458(ackA)
            CBA: CLB_2324(ackA)
            CBH: CLC_2308(ackA)
            CBF: CLI_2516(ackA)
            CKL: CKL_1391(ackA)
            CHY: CHY_1455(ackA)
            DSY: DSY2668
            SWO: Swol_0768
            TTE: TTE1481(ackA)
            MTA: Moth_0940
            MGE: MG_357(ackA)
            MPN: MPN533(ackA)
            MPU: MYPU_2380(ackA)
            MPE: MYPE5700(ackA)
            MGA: MGA_0169(ackA)
            MMY: MSC_0270(ackA)
            MMO: MMOB1690(ackA)
            MHY: mhp505(ackA)
            MHJ: MHJ_0505(ackA)
            MHP: MHP7448_0508(ackA)
            MSY: MS53_0652(ackA)
            MCP: MCAP_0230(ackA)
            UUR: UU484(ackA)
            POY: PAM159(ackA)
            AYW: AYWB_560(ackA)
            MFL: Mfl044
            MTU: Rv0409(ackA)
            MTC: MT0422(ackA)
            MBO: Mb0417(ackA)
            MBB: BCG_0448(ackA)
            MPA: MAP3886(ackA)
            MAV: MAV_4758(ackA)
            MSM: MSMEG_0784(ackA)
            MMC: Mmcs_0538
            CGL: NCgl2656(cgl2752)
            CGB: cg3047(ackA)
            CEF: CE2590
            CDI: DIP2054(ackA)
            CJK: jk0251(ack)
            NFA: nfa53450(ackA)
            RHA: RHA1_ro02196(askA)
            SCO: SCO5424(ackA)
            SMA: SAV2824(ackA)
            LXX: Lxx03420(ackA)
            TFU: Tfu_2971
            FRA: Francci3_3545
            FAL: FRAAL5741(ackA)
            ACE: Acel_0522
            SEN: SACE_1922(ackA)
            BLO: BL0969(ackA)
            BAD: BAD_0689(ackA)
            FNU: FN1171
            RBA: RB2582(ackA) RB9655(ackA)
            PCU: pc1362(ackA)
            BGA: BG0641(ackA)
            BAF: BAPKO_0662(ackA)
            TPA: TP0476
            TDE: TDE0933(ackA)
            SYN: sll1299(ackA)
            SYW: SYNW0155(ackA)
            SYC: syc2014_d(ackA)
            SYF: Synpcc7942_2079
            SYX: SynWH7803_0207(ackA)
            CYA: CYA_2688(ackA)
            CYB: CYB_1384(ackA)
            TEL: tlr2340
            GVI: glr1000
            ANA: all2561(ackA)
            AVA: Ava_0490
            PMB: A9601_10931(purT)
            PMC: P9515_10891(purT)
            PMF: P9303_30161(purT)
            PMG: P9301_10931(purT)
            PME: NATL1_12301(purT)
            BTH: BT_3693
            BFR: BF0479
            BFS: BF0424(ackA)
            PGI: PG1081(ackA)
            CTE: CT1525(ackA)
            PLT: Plut_1523
            DRA: DR_2602
            DGE: Dgeo_0052
            TMA: TM0274
            MAC: MA3606(ack)
            MBA: Mbar_A1820
            MMA: MM_0495
STRUCTURES  PDB: 1G99  1TUU  1TUY  2IIR  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.2.1
            ExPASy - ENZYME nomenclature database: 2.7.2.1
            ExplorEnz - The Enzyme Database: 2.7.2.1
            ERGO genome analysis and discovery system: 2.7.2.1
            UM-BBD (Biocatalysis/Biodegradation Database): 2.7.2.1
            BRENDA, the Enzyme Database: 2.7.2.1
            CAS: 9027-42-3
///
ENTRY       EC 2.7.2.2                  Enzyme
NAME        carbamate kinase;
            CKase ;
            carbamoyl phosphokinase;
            carbamyl phosphokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a carboxy group as acceptor
SYSNAME     ATP:carbamate phosphotransferase
REACTION    ATP + NH3 + CO2 = ADP + carbamoyl phosphate [RN:R00150]
ALL_REAC    R00150;
            (other) R01395
SUBSTRATE   ATP [CPD:C00002];
            NH3 [CPD:C00014];
            CO2 [CPD:C00011]
PRODUCT     ADP [CPD:C00008];
            carbamoyl phosphate [CPD:C00169]
REFERENCE   1  [PMID:4959296]
  AUTHORS   Bishop SH, Grisolia S.
  TITLE     Crystalline carbamate kinase.
  JOURNAL   Biochim. Biophys. Acta. 118 (1966) 211-5.
REFERENCE   2  [PMID:5857367]
  AUTHORS   Davis RH.
  TITLE     Carbamyl phosphate synthesis in Neurospora crassa. I. Preliminary
            characterization of arginine-specific carbamyl phosphokinase.
  JOURNAL   Biochim. Biophys. Acta. 107 (1965) 44-53.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   3
  AUTHORS   Glasziou, K.T.
  TITLE     The metabolism of arginine in Serratia marcescens. II.
            Carbamyladenosine diphosphate phosphoferase.
  JOURNAL   Aust. J. Biol. Sci. (1956) 253-262.
REFERENCE   4
  AUTHORS   Jones, M.E., Spector, L. and Lipmann, F.
  TITLE     Carbamyl phosphate, the carbamyl donor in enzymatic citrulline
            synthesis.
  JOURNAL   J. Am. Chem. Soc. 77 (1955) 819-820.
  ORGANISM  Streptococcus faecalis
REFERENCE   5  [PMID:6895223]
  AUTHORS   Srivenugopal KS, Adiga PR.
  TITLE     Enzymic conversion of agmatine to putrescine in Lathyrus sativus
            seedlings. Purification and properties of a multifunctional enzyme
            (putrescine synthase).
  JOURNAL   J. Biol. Chem. 256 (1981) 9532-41.
  ORGANISM  Lathyrus sativus
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00251  Glutamate metabolism
            PATH: map00330  Arginine and proline metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K00926  carbamate kinase
GENES       ECO: b0323(yahI) b0521(ybcF) b2874(yqeA)
            ECJ: JW0315(yahI) JW0510(ybcF) JW2842(yqeA)
            ECE: Z0412(yahI) Z0676(arcC) Z4213(yqeA)
            ECS: ECs0372 ECs0583 ECs3747
            ECC: c0444(yahI) c0635(arcC) c3452(yqeA) c5349
            ECI: UTI89_C0352(yahI) UTI89_C0549(arcC) UTI89_C3259(yqeA)
                 UTI89_C4405 UTI89_C4856
            ECP: ECP_0399 ECP_0581 ECP_2868 ECP_4499
            ECV: APECO1_1494(arcC) APECO1_1668(yahI) APECO1_2143 APECO1_2636
                 APECO1_3652(yqeA)
            ECW: EcE24377A_0559(arcC)
            ECX: EcHS_A0595
            STY: STY0580(arcC) STY4804
            STT: t2329(arcC) t4500
            SPT: SPA2191(arcC) SPA4266
            SEC: SC0571(arcC) SC4320(arcC)
            STM: STM0532(arcC) STM4466
            SFX: S0460(arcC)
            SFV: SFV_0479(arcC)
            SSN: SSON_0310(yahI) SSON_0497(arcC) SSON_3025(yqeA)
            SBO: SBO_3110(yqeA)
            ENT: Ent638_0451
            SPE: Spro_3187
            HIN: HI0595(arcC)
            HIT: NTHI0734(arcC)
            HIP: CGSHiEE_09190
            HIQ: CGSHiGG_06305
            APL: APL_1318(arcC)
            VFI: VFA1146
            PPR: PBPRA0476 PBPRB1784 PBPRB1918
            PAE: PA5173(arcC)
            PAU: PA14_68350(arcC)
            PAP: PSPA7_5913(arcC)
            PPU: PP_0999(arcC)
            PPF: Pput_1036
            PSB: Psyr_2686
            PFL: PFL_4637(arcC)
            PFO: Pfl_4388
            PEN: PSEEN4430(arcC)
            PMY: Pmen_1106
            HCH: HCH_05488(arcC)
            AHA: AHA_2165(arcC-1) AHA_4092(arcC-2)
            DNO: DNO_1073(arcC)
            CVI: CV_3780(arcC)
            BMA: BMA1147(arcC)
            BMV: BMASAVP1_A1587(arcC)
            BML: BMA10299_A0246(arcC)
            BMN: BMA10247_0913(arcC)
            BXE: Bxe_A1875 Bxe_C0748
            BPS: BPSL1745(arcC)
            BPM: BURPS1710b_2126(arcC)
            BPL: BURPS1106A_1984(arcC)
            BPD: BURPS668_1966(arcC)
            BTE: BTH_I2386(arcC)
            MMS: mma_1119 mma_3569
            GSU: GSU2487(arcC)
            GME: Gmet_2786
            SAT: SYN_01213
            SFU: Sfum_0047
            MES: Meso_2239
            PLA: Plav_1145
            SME: SMa0697(arcC)
            SMD: Smed_5204
            OAN: Oant_4648
            ABA: Acid345_1820
            BCE: BC0409
            BCA: BCE_0475(arcC)
            BCY: Bcer98_0351
            BTK: BT9727_0344(arcC)
            BTL: BALH_0366(arcC)
            BLI: BL01102 BL01916
            BLD: BLi01134 BLi04166
            SAU: SA1013 SA2425(arcC)
            SAV: SAV1170 SAV2632(arcC)
            SAM: MW1051 MW2553(arcC)
            SAR: SAR1143 SAR2711(arcC)
            SAS: SAS1103 SAS2518
            SAC: SACOL1182(arcC1) SACOL2654(arcC2)
            SAB: SAB1034 SAB2507c(arcC)
            SAA: SAUSA300_0061(arcC) SAUSA300_1063(arcC) SAUSA300_2567(arcC)
            SAO: SAOUHSC_01129 SAOUHSC_02965
            SAJ: SaurJH9_1228 SaurJH9_2656
            SAH: SaurJH1_1253 SaurJH1_2712
            SEP: SE0102 SE0228
            SER: SERP2352(arcC)
            SHA: SH0259
            LMO: lmo0039
            LMF: LMOf2365_0048(arcC)
            LLA: L0112(arcC3) L92850(arcC2) L93826(arcC1)
            LLC: LACR_2318 LACR_2319
            LLM: llmg_2309(arcC2) llmg_2310(arcC1)
            SPY: SPy_1541(arcC)
            SPZ: M5005_Spy_1270(arcC)
            SPM: spyM18_1558
            SPG: SpyM3_1191(arcC)
            SPS: SPs0671
            SPH: MGAS10270_Spy1285(arcC)
            SPI: MGAS10750_Spy1377(arcC)
            SPJ: MGAS2096_Spy1289(arcC)
            SPK: MGAS9429_Spy1264(arcC)
            SPF: SpyM50582(arcC)
            SPA: M6_Spy1291
            SPB: M28_Spy1208(arcC)
            SPN: SP_2151
            SPR: spr1958(arcC)
            SPD: SPD_1977(arcC)
            SAG: SAG2125(arcC-1) SAG2167(arcC-2)
            SAN: gbs2084 gbs2126
            SAK: SAK_2064(arcC) SAK_2125(arcC)
            SMU: SMU.265(arcC)
            SSA: SSA_0739(arcC)
            SGO: SGO_1591(arcC)
            LSA: LSA0071 LSA0372(arcC)
            LBR: LVIS_2023 LVIS_2207
            LRE: Lreu_0426
            PPE: PEPE_1630
            EFA: EF0106(arcC-1) EF0386(arcC-2) EF0735(arcC-3) EF2575(arcC-4)
            CPE: CPE0171(arcC)
            CPF: CPF_0164(arcC)
            CPR: CPR_0160(arcC)
            CTC: CTC02524
            CBA: CLB_2535(arcC)
            CBH: CLC_2466(arcC)
            CBF: CLI_2657(arcC)
            TTE: TTE0533(arcC)
            MTA: Moth_1948 Moth_2117
            MPN: MPN307(arcC)
            MPE: MYPE6100(arcC)
            MMY: MSC_0700(arcC) MSC_0864(arcC) MSC_0877(arcC)
            MCP: MCAP_0651(arcC)
            MVA: Mvan_1389
            PAC: PPA0585
            NCA: Noca_1504 Noca_2426
            RXY: Rxyl_2848
            TDE: TDE2476(arcC)
            SYN: sll0573(arcC)
            TME: Tmel_1927
            FNO: Fnod_1788
            MEM: Memar_0247
            HAL: VNG6316G(arcC)
            NPH: NP3632A(arcC)
            TAC: Ta1350m
            TVO: TVN0259
            PTO: PTO0590
            PHO: PH1282
            PAB: PAB0593(cpa)
            PFU: PF0676
            TKO: TK2158
            APE: APE_1968
            SMR: Smar_0235
            HBU: Hbut_0269
            PAI: PAE1552
            PIS: Pisl_1620
            PCL: Pcal_0529
            TPE: Tpen_0172
STRUCTURES  PDB: 1B7B  1E19  2E9Y  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.2.2
            ExPASy - ENZYME nomenclature database: 2.7.2.2
            ExplorEnz - The Enzyme Database: 2.7.2.2
            ERGO genome analysis and discovery system: 2.7.2.2
            BRENDA, the Enzyme Database: 2.7.2.2
            CAS: 9026-69-1
///
ENTRY       EC 2.7.2.3                  Enzyme
NAME        phosphoglycerate kinase;
            PGK;
            3-PGK;
            ATP-3-phospho-D-glycerate-1-phosphotransferase;
            ATP:D-3-phosphoglycerate 1-phosphotransferase;
            3-phosphoglycerate kinase;
            3-phosphoglycerate phosphokinase;
            3-phosphoglyceric acid kinase;
            3-phosphoglyceric acid phosphokinase;
            3-phosphoglyceric kinase;
            glycerate 3-phosphate kinase;
            glycerophosphate kinase;
            phosphoglyceric acid kinase;
            phosphoglyceric kinase;
            phosphoglycerokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a carboxy group as acceptor
SYSNAME     ATP:3-phospho-D-glycerate 1-phosphotransferase
REACTION    ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
            [RN:R01512]
ALL_REAC    R01512
SUBSTRATE   ATP [CPD:C00002];
            3-phospho-D-glycerate [CPD:C00197]
PRODUCT     ADP [CPD:C00008];
            3-phospho-D-glyceroyl phosphate [CPD:C00236]
REFERENCE   1
  AUTHORS   Axelrod, B. and Bandurski, R.S.
  TITLE     Phosphoglyceroyl kinase in higher plants.
  JOURNAL   J. Biol. Chem. 204 (1953) 939-948.
  ORGANISM  Pisum sativum
REFERENCE   2
  AUTHORS   Bucher, T.
  TITLE     Uber ein phosphatubertragendes Garungsferment.
  JOURNAL   Biochim. Biophys. Acta 1 (1947) 292-314.
REFERENCE   3  [PMID:13960866]
  AUTHORS   HASHIMOTO T, YOSHIKAWA H.
  TITLE     Crystalline phosphoglycerate kinase from human erythrocytes.
  JOURNAL   Biochim. Biophys. Acta. 65 (1962) 355-7.
  ORGANISM  human [GN:hsa]
REFERENCE   4
  AUTHORS   Rao, D.R. and Oespar, P.
  TITLE     Purification and properties of muscle phosphoglycerate kinase.
  JOURNAL   Biochem. J. 81 (1961) 405-411.
  ORGANISM  rabbit
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00710  Carbon fixation
ORTHOLOGY   KO: K00927  phosphoglycerate kinase
GENES       HSA: 5230(PGK1) 5232(PGK2)
            PTR: 462757(PGK2)
            MMU: 18655(Pgk1) 18663(Pgk2)
            RNO: 24644(Pgk1)
            CFA: 474933(PGK2) 480964(PGK1)
            SSC: 396673(PGK2)
            GGA: 395833(PGK1)
            XLA: 380062(pgk1) 446763(pgk2)
            DME: Dmel_CG3127(Pgk) Dmel_CG9961
            CEL: T03F1.3(pgk-1)
            ATH: AT1G56190 AT3G12780(PGK1)
            OSA: 4327954 4328435 4341792
            CME: CMJ305C
            SCE: YCR012W(PGK1)
            AGO: AGOS_AEL038C
            PIC: PICST_78267(PGK1)
            CGR: CAGL0L07722g
            SPO: SPBC14F5.04c(pgk1)
            ANI: AN1246.2
            AFM: AFUA_1G10350
            AOR: AO090038000395
            CNE: CNG02220
            UMA: UM04871.1
            ECU: ECU05_0320
            DDI: DDB_0191349(pgkA)
            PFA: PFI1105w
            CPV: cgd7_910
            CHO: Chro.70113
            TAN: TA06655
            TPV: TP01_0965
            TET: TTHERM_00929450
            TBR: Tb927.1.700(PGKC) Tb927.1.710(PGKB) Tb927.1.720(PGKA)
            TCR: 505999.100 505999.90 511419.40 511419.50
            LMA: LmjF20.0100 LmjF20.0110 LmjF30.3380
            EHI: 75.t00020
            ECO: b2926(pgk)
            ECJ: JW2893(pgk)
            ECE: Z4265(pgk)
            ECS: ECs3797
            ECC: c3504(pgk)
            ECI: UTI89_C3309(pgk)
            ECP: ECP_2915
            ECV: APECO1_3607(pgk)
            ECW: EcE24377A_3254(pgk)
            ECX: EcHS_A3084
            STY: STY3227(pgk)
            STT: t2988(pgk)
            SPT: SPA2940(pgk)
            SEC: SC3011(pgk)
            STM: STM3069(pgk)
            YPE: YPO0921(pgk)
            YPK: y3308(pgk)
            YPM: YP_3519(pgk)
            YPA: YPA_0343
            YPN: YPN_3120
            YPP: YPDSF_0592
            YPS: YPTB3196(pgk)
            YPI: YpsIP31758_0849(pgk)
            SFL: SF2911(pgk)
            SFX: S3111(pgk)
            SFV: SFV_2972(pgk)
            SSN: SSON_3078(pgk)
            SBO: SBO_3067(pgk)
            SDY: SDY_3156(pgk)
            ECA: ECA3912(pgk)
            PLU: plu0956(pgk)
            BUC: BU450(pgk)
            BAS: BUsg435(pgk)
            BAB: bbp400(pgk)
            BCC: BCc_278(pgk)
            WBR: WGLp305(pgk)
            SGL: SG2015
            ENT: Ent638_3339
            SPE: Spro_3945
            BFL: Bfl254(pgk)
            BPN: BPEN_261(pgk)
            HIN: HI0525(pgk)
            HIT: NTHI0651(pgk)
            HIP: CGSHiEE_00365(pgk)
            HIQ: CGSHiGG_05890(pgk)
            HDU: HD0865(pgk)
            HSO: HS_0207(pgk)
            PMU: PM1860(pgk)
            MSU: MS0245(pgk)
            APL: APL_1251(pgk)
            ASU: Asuc_0535
            XFA: XF0823
            XFT: PD1847(pgk)
            XCC: XCC3188(pgk)
            XCB: XC_0976
            XCV: XCV3465(pgk)
            XAC: XAC3347(pgk)
            XOO: XOO3415(pgk)
            XOM: XOO_3215(XOO3215)
            VCH: VC0477
            VCO: VC0395_A0030(pgk)
            VVU: VV1_1540
            VVY: VV2858
            VPA: VP2600
            VFI: VF0442
            PPR: PBPRA3131(pgk)
            PAE: PA0552(pgk)
            PAU: PA14_07190(pgk)
            PPU: PP_4963(pgk)
            PPF: Pput_4836
            PST: PSPTO_0387(pgk)
            PSB: Psyr_4790
            PSP: PSPPH_4819(pgk)
            PFL: PFL_5784(pgk)
            PFO: Pfl_5265
            PEN: PSEEN5022(pgk)
            PMY: Pmen_0460
            PAR: Psyc_0706(pgk)
            PCR: Pcryo_0681
            PRW: PsycPRwf_1426
            ACI: ACIAD1927(pgk)
            SON: SO_0932(pgk)
            SDN: Sden_1085
            SFR: Sfri_0649
            SAZ: Sama_2757
            SBL: Sbal_0829
            SBM: Shew185_3538
            SLO: Shew_0754
            SPC: Sputcn32_0874
            SSE: Ssed_0876
            SPL: Spea_0790
            SHE: Shewmr4_0775
            SHM: Shewmr7_3248
            SHN: Shewana3_3351
            SHW: Sputw3181_3299
            ILO: IL2212(pgk)
            CPS: CPS_3874(pgk)
            PHA: PSHAa0595(pgk)
            PAT: Patl_3328
            SDE: Sde_0473
            PIN: Ping_0371
            MAQ: Maqu_3038
            CBU: CBU_1782(pgk)
            CBD: COXBU7E912_0226(pgk)
            LPN: lpg0137(pgk)
            LPF: lpl0137(pgk)
            LPP: lpp0152(pgk)
            MCA: MCA2021(pgk)
            FTU: FTT1367c(pgk)
            FTF: FTF1367c(pgk)
            FTW: FTW_0524(pgk)
            FTL: FTL_1147
            FTH: FTH_1122(pgk)
            FTA: FTA_1210(pgk)
            FTN: FTN_1331(pgk)
            TCX: Tcr_0246
            NOC: Noc_2806
            AEH: Mlg_2842
            HHA: Hhal_1041
            HCH: HCH_01537(pgk)
            CSA: Csal_0371
            ABO: ABO_0391(algF) ABO_2613(pgk)
            MMW: Mmwyl1_4317
            AHA: AHA_0781(pgk)
            DNO: DNO_1036(pgk)
            BCI: BCI_0645(pgk)
            RMA: Rmag_0065
            VOK: COSY_0072(pgk)
            NME: NMB0010
            NMA: NMA0257(pgk)
            NMC: NMC2148(pgk)
            NGO: NGO1919
            CVI: CV_0189(pgk)
            RSO: RSc0571(pgk)
            REU: Reut_A0559
            REH: H16_A0566(pgk) H16_B1385(cbbK2)
            RME: Rmet_0501 Rmet_1516
            BMA: BMA0295.1(pgk)
            BMV: BMASAVP1_A0591(pgk)
            BML: BMA10299_A2425(pgk)
            BMN: BMA10247_0037(pgk)
            BXE: Bxe_A0689
            BVI: Bcep1808_2743
            BUR: Bcep18194_A5959
            BCN: Bcen_2017
            BCH: Bcen2424_2628
            BAM: Bamb_2675
            BPS: BPSL0796(pgk)
            BPM: BURPS1710b_0995(pgk)
            BPL: BURPS1106A_0838(pgk)
            BPD: BURPS668_0833(pgk)
            BTE: BTH_I0663(pgk)
            PNU: Pnuc_1817
            BPE: BP1001(pgk)
            BPA: BPP1166(pgk)
            BBR: BB1382(pgk)
            RFR: Rfer_3690
            POL: Bpro_4635
            PNA: Pnap_1987 Pnap_3874
            AAV: Aave_4693
            AJS: Ajs_4056
            VEI: Veis_4078
            MPT: Mpe_A0289(pgk) Mpe_A2792(cbbK)
            HAR: HEAR2610(pgk)
            MMS: mma_2847
            NEU: NE0326(cbbK)
            NET: Neut_1579
            NMU: Nmul_A0386
            EBA: ebA1103(pgk)
            AZO: azo2839(pgk)
            DAR: Daro_3594
            TBD: Tbd_0161(cbbK)
            MFA: Mfla_2247
            HPY: HP1345
            HPJ: jhp1264(pgk)
            HPA: HPAG1_0253 HPAG1_0303 HPAG1_0304 HPAG1_1292
            HHE: HH0327(pgk)
            HAC: Hac_0274(pgk)
            WSU: WS1030(PGK)
            TDN: Tmden_1753
            CJE: Cj1402c(pgk)
            CJR: CJE1589(pgk)
            CJJ: CJJ81176_1401(pgk)
            CJU: C8J_1316(pgk)
            CJD: JJD26997_1736(pgk)
            CFF: CFF8240_1428(pgk)
            CCV: CCV52592_1248(pgk) CCV52592_1824
            CHA: CHAB381_0778(pgk)
            CCO: CCC13826_0515(pgk)
            ABU: Abu_2133(pgk)
            NIS: NIS_1491(pgk)
            SUN: SUN_2203(pgk)
            GSU: GSU1628
            GME: Gmet_1947
            GUR: Gura_2060
            PCA: Pcar_1332
            PPD: Ppro_1694
            DVU: DVU2529(pgk)
            DVL: Dvul_0716
            DDE: Dde_2630
            LIP: LI0464(pgk)
            BBA: Bd1050(pgk)
            DPS: DP0101
            ADE: Adeh_1531
            AFW: Anae109_2281
            MXA: MXAN_2816(pgk)
            SAT: SYN_01396
            SFU: Sfum_2060
            OTS: OTBS_0951
            WOL: WD1167(pgk)
            WBM: Wbm0684
            AMA: AM1326(pgk)
            APH: APH_1321(pgk)
            ERU: Erum0360(pgk)
            ERW: ERWE_CDS_00230(pgk)
            ERG: ERGA_CDS_00230(pgk)
            ECN: Ecaj_0028
            ECH: ECH_0055(pgk)
            NSE: NSE_0436(pgk)
            PUB: SAR11_0585(pgk)
            MLO: mlr3753
            MES: Meso_3437
            PLA: Plav_2106
            SME: SMc03981(pgk)
            SMD: Smed_2653
            ATU: Atu3739(pgk)
            ATC: AGR_L_2193(pgk)
            RET: RHE_CH03499(pgk)
            RLE: RL4011(pgk)
            BME: BMEI0309
            BMF: BAB1_1742
            BMS: BR1729(pgk)
            BMB: BruAb1_1714(pgk)
            BOV: BOV_1671(pgk)
            OAN: Oant_1187
            BJA: bll1522(pgk)
            BRA: BRADO1122(cbbK)
            BBT: BBta_0449(cbbK) BBta_6926(cbbK)
            RPA: RPA0943(cbbK)
            RPB: RPB_4468
            RPC: RPC_4770
            RPD: RPD_4314
            RPE: RPE_4725
            NWI: Nwi_2736
            NHA: Nham_3533
            BHE: BH15070(pgk)
            BQU: BQ11990(pgk)
            BBK: BARBAKC583_0140(pgk)
            XAU: Xaut_3076
            CCR: CC_3249
            SIL: SPO2235(pgk)
            SIT: TM1040_1084
            RSP: RSP_4044(pgk)
            RSH: Rsph17029_1152
            RSQ: Rsph17025_1097
            JAN: Jann_1694
            RDE: RD1_3008(pgk)
            PDE: Pden_1918
            MMR: Mmar10_2596
            HNE: HNE_3180(pgk)
            ZMO: ZMO0178(pgk)
            NAR: Saro_1965
            SAL: Sala_1318
            SWI: Swit_2604
            ELI: ELI_05215
            GOX: GOX0507
            GBE: GbCGDNIH1_0312
            ACR: Acry_1222
            RRU: Rru_A0221
            MAG: amb0513
            MGM: Mmc1_1886
            ABA: Acid345_2542
            SUS: Acid_4421
            BSU: BG11062(pgk)
            BHA: BH3559(pgk)
            BAN: BA5367(pgk)
            BAR: GBAA5367(pgk)
            BAA: BA_0226(PGK)
            BAT: BAS4988
            BCA: BCE_5241(pgk)
            BCZ: BCZK4827(pgk)
            BCY: Bcer98_3681
            BTK: BT9727_4817(pgk)
            BTL: BALH_4630(pgk)
            BLI: BL03465(pgk)
            BLD: BLi03664(pgk)
            BCL: ABC3020(pgk)
            BAY: RBAM_031290
            BPU: BPUM_3056
            OIH: OB2437(pgk)
            GKA: GK3057(pgk)
            SAU: SA0728(pgk)
            SAV: SAV0773(pgk)
            SAM: MW0735(pgk)
            SAR: SAR0829(pgk)
            SAS: SAS0739
            SAC: SACOL0839(pgk)
            SAB: SAB0729(pgk)
            SAA: SAUSA300_0757(pgk)
            SAO: SAOUHSC_00796
            SAJ: SaurJH9_0798
            SAH: SaurJH1_0814
            SEP: SE0558
            SER: SERP0443(pgk)
            SHA: SH2112(pgk)
            SSP: SSP1915
            LMO: lmo2458(pgk)
            LMF: LMOf2365_2431(pgk)
            LIN: lin2552(pgk)
            LWE: lwe2406(pgk)
            LLA: L0010(pgk)
            LLC: LACR_0248
            LLM: llmg_0253(pgk)
            SPY: SPy_1881(pgk)
            SPZ: M5005_Spy_1599(pgk)
            SPM: spyM18_1946(pgk)
            SPG: SpyM3_1624(pgk)
            SPS: SPs0243
            SPH: MGAS10270_Spy1670(pgk)
            SPI: MGAS10750_Spy1657(pgk)
            SPJ: MGAS2096_Spy1625(pgk)
            SPK: MGAS9429_Spy1604(pgk)
            SPF: SpyM50252(pgk)
            SPA: M6_Spy1610
            SPB: M28_Spy1591(pgk)
            SPN: SP_0499
            SPR: spr0441(pgk)
            SPD: SPD_0445(pgk)
            SAG: SAG1766(pgk)
            SAN: gbs1809
            SAK: SAK_1788(pgk)
            SMU: SMU.361(pgk)
            STC: str1782(pgk)
            STL: stu1782(pgk)
            SSA: SSA_0302(pgk)
            SGO: SGO_0209(pgk)
            LPL: lp_0790(pgk)
            LJO: LJ0873
            LAC: LBA0699
            LSA: LSA0605(pgk)
            LSL: LSL_1165(pgk)
            LDB: Ldb0636(pgk)
            LBU: LBUL_0568
            LBR: LVIS_0662
            LCA: LSEI_0968
            EFA: EF1963(pgk)
            OOE: OEOE_0638
            STH: STH242
            CAC: CAC0710(pgk)
            CPE: CPE1303(pgk)
            CPF: CPF_1510(pgk)
            CPR: CPR_1300(pgk)
            CTC: CTC00379(pgk)
            CNO: NT01CX_1411
            CTH: Cthe_0138
            CDF: CD3173(pgk)
            CBO: CBO0227(pgk)
            CBA: CLB_0268(pgk)
            CBH: CLC_0283(pgk)
            CBF: CLI_0292(pgk)
            CBE: Cbei_0598
            AMT: Amet_3579
            CHY: CHY_0281(pgk)
            DSY: DSY4841
            DRM: Dred_0133 Dred_2990
            SWO: Swol_0273
            CSC: Csac_1952
            TTE: TTE1761(pgk)
            MTA: Moth_0263
            MGE: MG_300(pgk)
            MPN: MPN429(pgk)
            MPU: MYPU_2460(pgk)
            MPE: MYPE8160(pgk)
            MGA: MGA_1187(pgk)
            MMY: MSC_0678(pgk)
            MMO: MMOB4490(pgk) MMOB4530(pgk)
            MHY: mhp488(pgk)
            MHJ: MHJ_0487(pgk)
            MHP: MHP7448_0490(pgk)
            MSY: MS53_0114(pgk)
            MCP: MCAP_0631(pgk)
            UUR: UU279(pgk)
            POY: PAM174(pgk)
            AYW: AYWB_546(pgk)
            MFL: Mfl577
            MTU: Rv1437(pgk)
            MTC: MT1481(pgk)
            MBO: Mb1472(pgk)
            MBB: BCG_1498(pgk)
            MLE: ML0571(pgk)
            MPA: MAP1165(pgk)
            MAV: MAV_3340(pgk)
            MSM: MSMEG_3085(pgk)
            MVA: Mvan_2704
            MGI: Mflv_3709
            MMC: Mmcs_2405
            MKM: Mkms_2451
            MJL: Mjls_2445
            CGL: NCgl1525(cgl1587)
            CGB: cg1790(pgk)
            CEF: CE1705(pgk)
            CDI: DIP1309(pgk)
            CJK: jk1000(pgk)
            NFA: nfa35880(pgk)
            RHA: RHA1_ro07178(pgk)
            SCO: SCO1946(pgk)
            SMA: SAV6297(pgk)
            TWH: TWT301(pgk)
            TWS: TW471(pgk)
            LXX: Lxx11530
            CMI: CMM_1743(pgkA)
            ART: Arth_2088
            AAU: AAur_2089(pgk)
            PAC: PPA0817
            NCA: Noca_2531
            TFU: Tfu_2016
            FRA: Francci3_1638
            FAL: FRAAL4587(pgk)
            ACE: Acel_1115
            KRA: Krad_2930
            SEN: SACE_2144(pgk)
            STP: Strop_3097
            BLO: BL0707(pgk)
            BAD: BAD_0835(pgk)
            RXY: Rxyl_2004
            FNU: FN0654
            RBA: RB10500(pgk)
            CTR: CT693(pgk)
            CTA: CTA_0754(pgk)
            CMU: TC0065
            CPN: CPn0679(pgk)
            CPA: CP0068
            CPJ: CPj0679(pgk)
            CPT: CpB0706
            CCA: CCA00061(pgk)
            CAB: CAB062(pgk)
            CFE: CF0943(pgk)
            PCU: pc0239(pgk)
            BGA: BG0055(pgk)
            BAF: BAPKO_0056(pgk)
            TPA: TP0538
            TDE: TDE1715(pgk)
            LIL: LA1703(pgk)
            LIC: LIC12091(pgk)
            LBJ: LBJ_1219(pgk)
            LBL: LBL_1270(pgk)
            SYN: slr0394(pgk)
            SYW: SYNW2329(pgk)
            SYC: syc0433_c
            SYF: Synpcc7942_1116
            SYD: Syncc9605_2459
            SYE: Syncc9902_2143
            SYG: sync_2709(pgk)
            SYR: SynRCC307_2229(pgk)
            SYX: SynWH7803_2351(pgk)
            CYA: CYA_0315(pgk)
            CYB: CYB_1693(pgk)
            TEL: tll2268(pgk)
            GVI: glr2313(pgk)
            ANA: all4131
            AVA: Ava_0772
            PMA: Pro0221(pgk)
            PMM: PMM0195(pgk)
            PMT: PMT2106(pgk)
            PMN: PMN2A_1562
            PMI: PMT9312_0197
            PMB: A9601_02131(pgk)
            PMC: P9515_02241(pgk)
            PMF: P9303_27971(pgk)
            PMG: P9301_02151(pgk)
            PMH: P9215_02131
            PME: NATL1_02711(pgk)
            TER: Tery_3376
            BTH: BT_1672
            BFR: BF3269
            BFS: BF3107(pgk)
            PGI: PG1677(pgk)
            SRU: SRU_1199(pgk)
            CHU: CHU_2229(pgk)
            GFO: GFO_3294(pgk)
            FJO: Fjoh_0977
            FPS: FP0018(pgk)
            CTE: CT2222(pgk)
            CCH: Cag_0044
            CPH: Cpha266_2734
            PVI: Cvib_1766
            PLT: Plut_2123
            DET: DET0744(pgk)
            DEH: cbdb_A719(pgk)
            DEB: DehaBAV1_0674
            RRS: RoseRS_1473
            RCA: Rcas_2070
            DRA: DR_1342
            DGE: Dgeo_1134
            TTH: TTC0550
            TTJ: TTHA0906
            AAE: aq_118(pgk)
            TMA: TM0689
            TPT: Tpet_0242
            TME: Tmel_1265
            FNO: Fnod_0739
            MMP: MMP1532(pgk)
            MMQ: MmarC5_0043
            MMZ: MmarC7_0780
            MAE: Maeo_0495
            MVN: Mevan_0845
            MAC: MA2669(pgk) MA3592(pgk)
            MBA: Mbar_A1808 Mbar_A3562
            MMA: MM_0485
            MBU: Mbur_1345
            MTP: Mthe_0817
            MHU: Mhun_1194
            MEM: Memar_0290 Memar_0928
            MBN: Mboo_1540 Mboo_2342
            MST: Msp_1381(pgk)
            MSI: Msm_0918
            MKA: MK1662(pgk)
            HAL: VNG1216G(pgk)
            HMA: rrnAC2364(pgk)
            HWA: HQ1395A(pgk)
            NPH: NP4130A(pgk)
            TAC: Ta1075
            TVO: TVN0530
            PTO: PTO0479 PTO1514
            PHO: PH1218
            PAB: PAB1679(pgk)
            PFU: PF1057
            TKO: TK1146
            RCI: RCIX1778(pgk-1) RRC531(pgk-2)
            APE: APE_0173.1
            SMR: Smar_0240
            IHO: Igni_0274
            HBU: Hbut_0940
            SSO: SSO0527
            STO: ST1357
            SAI: Saci_1355(pgk)
            MSE: Msed_1653
            PAI: PAE1742
            PIS: Pisl_1711
            PCL: Pcal_0633
            PAS: Pars_0744
            TPE: Tpen_0773
STRUCTURES  PDB: 13PK  16PK  1FW8  1HDI  1KF0  1LTK  1PHP  1QPG  1V6S  1VJC  
                 1VJD  1VPE  1ZMR  2CUN  2IE8  2PGK  3PGK  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.2.3
            ExPASy - ENZYME nomenclature database: 2.7.2.3
            ExplorEnz - The Enzyme Database: 2.7.2.3
            ERGO genome analysis and discovery system: 2.7.2.3
            BRENDA, the Enzyme Database: 2.7.2.3
            CAS: 9001-83-6
///
ENTRY       EC 2.7.2.4                  Enzyme
NAME        aspartate kinase;
            aspartokinase;
            AK;
            beta-aspartokinase;
            aspartic kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a carboxy group as acceptor
SYSNAME     ATP:L-aspartate 4-phosphotransferase
REACTION    ATP + L-aspartate = ADP + 4-phospho-L-aspartate [RN:R00480]
ALL_REAC    R00480
SUBSTRATE   ATP [CPD:C00002];
            L-aspartate [CPD:C00049]
PRODUCT     ADP [CPD:C00008];
            4-phospho-L-aspartate [CPD:C03082]
COMMENT     The enzyme from Escherichia coli is a multifunctional protein, which
            also catalyses the reaction of EC 1.1.1.3 homoserine dehydrogenase.
REFERENCE   1
  AUTHORS   Black, S.
  TITLE     Conversion of aspartic acid to homoserine.
  JOURNAL   Methods Enzymol. 5 (1962) 820-827.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:6058940]
  AUTHORS   Paulus H, Gray E.
  TITLE     Multivalent feedback inhibition of aspartokinase in Bacillus
            polymyxa. I. Kinetic studies.
  JOURNAL   J. Biol. Chem. 242 (1967) 4980-6.
  ORGANISM  Bacillus polymyxa
REFERENCE   3  [PMID:4551091]
  AUTHORS   Starnes WL, Munk P, Maul SB, Cunningham GN, Cox DJ, Shive W.
  TITLE     Threonine-sensitive aspartokinase-homoserine dehydrogenase complex,
            amino acid composition, molecular weight, and subunit composition of
            the complex.
  JOURNAL   Biochemistry. 11 (1972) 677-87.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:4562990]
  AUTHORS   Veron M, Falcoz-Kelly F, Cohen GN.
  TITLE     The threonine-sensitive homoserine dehydrogenase and aspartokinase
            activities of Escherichia coli K12. The two catalytic activities are
            carried by two independent regions of the polypeptide chain.
  JOURNAL   Eur. J. Biochem. 28 (1972) 520-7.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K00928  aspartate kinase
GENES       ATH: AT1G31230(AK-HSDH_I) AT5G13280(AK-LYS1)
                 AT5G14060(CARAB-AK-LYS)
            OSA: 4326958 4334794 4342980 4346642
            CME: CMJ016C CMN129C
            SCE: YER052C(HOM3)
            AGO: AGOS_ADL086C
            PIC: PICST_69242(HOM3)
            CGR: CAGL0J02882g
            SPO: SPBC19F5.04
            ANI: AN8859.2
            AFM: AFUA_5G05590
            AOR: AO090009000702
            CNE: CNI02030
            UMA: UM00872.1
            ECO: b0002(thrA) b3940(metL) b4024(lysC)
            ECJ: JW0001(thrA) JW3911(metL) JW3984(lysC)
            ECE: Z0002(thrA) Z5495(metL) Z5622(lysC)
            ECS: ECs0002 ECs4869 ECs5007
            ECC: c0003(thrA) c4893(metL) c4990(lysC)
            ECI: UTI89_C0002(thrA) UTI89_C2785(eutP) UTI89_C4525(metL)
                 UTI89_C4592(lysC)
            ECP: ECP_0002 ECP_4242
            ECV: APECO1_1976(thrA) APECO1_2444(lysC) APECO1_2531(metL)
            ECW: EcE24377A_0001(thrA) EcE24377A_4480(metL)
                 EcE24377A_4572(lysC)
            ECX: EcHS_A0003(thrA) EcHS_A4174
            STY: STY0002(thrA) STY3768(metL) STY4416(lysC)
            STT: t0002(thrA) t3517(metL) t4126(lysC)
            SPT: SPA0002(thrA) SPA3944(metL) SPA4037(lysC)
            SEC: SC0002(thrA) SC3992(metL) SC4099(lysC)
            STM: STM0002(thrA) STM4101(metL) STM4220(lysC)
            YPE: YPO0116(metL) YPO0459(thrA) YPO3719(lysC)
            YPK: y0023(lysC) y0303(metL) y3718(thrA)
            YPM: YP_0118(metL) YP_3081(lysC2) YP_3723(thrA)
            YPA: YPA_0025 YPA_0265 YPA_4051
            YPN: YPN_0022 YPN_0331 YPN_3738
            YPP: YPDSF_0181 YPDSF_3174 YPDSF_3791
            YPS: YPTB0106(metM) YPTB0602(thrA) YPTB3650(lysC)
            YPI: YpsIP31758_0122(metL) YpsIP31758_3476(thrA)
            SFL: SF0002(thrA) SF4018(metL) SF4181(lysC)
            SFX: S0002(thrA) S3550(lysC) S3729(metL)
            SFV: SFV_0001(thrA) SFV_4010(metL) SFV_4189(lysC)
            SSN: SSON_0002(thrA) SSON_4114(metL) SSON_4202(lysC)
            SBO: SBO_0001(thrA) SBO_3960(metL) SBO_4052(lysC)
            SDY: SDY_0002(thrA) SDY_3775(metL) SDY_4227(lysC)
            ECA: ECA3891(thrA) ECA3981(lysC) ECA4251(metL)
            PLU: plu0563(thrA) plu4380(lysC) plu4755(metL)
            BUC: BU194(thrA)
            BAS: BUsg188(thrA)
            BAB: bbp183(thrA)
            BCC: BCc_127(thrA)
            WBR: WGLp591(thrA)
            SGL: SG0404 SG2147
            ENT: Ent638_0229 Ent638_0564 Ent638_4034
            SPE: Spro_0683 Spro_4479 Spro_4785
            BFL: Bfl111(thrA)
            BPN: BPEN_115(thrA)
            HIT: NTHI0167(thrA)
            HDU: HD1375(lysC)
            HSO: HS_1214(thrA)
            PMU: PM0113(thrA) PM0937
            MSU: MS1613(lysC) MS1703(lysC)
            APL: APL_0250(thrA) APL_0710(lysC)
            ASU: Asuc_0801 Asuc_0925
            XFA: XF1116 XF2225
            XFT: PD0408(lysC) PD1273(lysC)
            XCC: XCC1800(metL) XCC2741(lysA)
            XCB: XC_1372 XC_2389
            XCV: XCV1866(thrA) XCV3056(lysA)
            XAC: XAC1820(metL) XAC2911(lysA)
            XOO: XOO1433(lysA) XOO2242(metL)
            XOM: XOO_1317(XOO1317) XOO_2107(XOO2107)
            VCH: VC0391 VC0547 VC2364 VC2684 VCA0822
            VCO: VC0395_A0074 VC0395_A1943(thrA) VC0395_A2257(metL)
                 VC0395_A2809(lysC)
            VVU: VV1_0545 VV1_1365 VV1_1424 VV1_1594
            VVY: VV0650 VV2802 VV2959 VV3007
            VPA: VP0494 VP1719 VP2547 VP2715 VP2764
            VFI: VF0338 VF0537 VF2118(thrA) VF2266(metL) VFA1125
            PPR: PBPRA0262 PBPRA0552 PBPRA3066 PBPRA3293 PBPRB1487 PBPRB1489
            PAE: PA0904(lysC)
            PAU: PA14_52580(lysC)
            PAP: PSPA7_4611
            PPU: PP_4473
            PPF: Pput_1442
            PST: PSPTO_1843
            PSB: Psyr_3555
            PSP: PSPPH_3511
            PFL: PFL_4505
            PFO: Pfl_0927 Pfl_4274
            PEN: PSEEN3874
            PMY: Pmen_2902
            PAR: Psyc_1461(lysC)
            PCR: Pcryo_1639
            PRW: PsycPRwf_1612
            ACI: ACIAD1252(lysC)
            ACB: A1S_1142
            SON: SO_3415(thrA) SO_3427 SO_3986(lysC) SO_4055(metL)
            SDN: Sden_0616 Sden_2740 Sden_2982
            SFR: Sfri_0535 Sfri_2906 Sfri_3550
            SAZ: Sama_0603 Sama_0905 Sama_1049 Sama_3170
            SBL: Sbal_0788 Sbal_1227 Sbal_3114 Sbal_3775
            SBM: Shew185_0537 Shew185_1271 Shew185_3123 Shew185_3717
            SLO: Shew_0521 Shew_0779 Shew_1079
            SPC: Sputcn32_0617 Sputcn32_0680 Sputcn32_2735 Sputcn32_2744
            SSE: Ssed_0817 Ssed_1175 Ssed_4040
            SPL: Spea_0561 Spea_0735 Spea_1066
            SHE: Shewmr4_0653 Shewmr4_1128 Shewmr4_1138 Shewmr4_3438
            SHM: Shewmr7_0513 Shewmr7_1199 Shewmr7_1209 Shewmr7_3369
            SHN: Shewana3_0537 Shewana3_0652 Shewana3_1129 Shewana3_1139
                 Shewana3_3613
            SHW: Sputw3181_1268 Sputw3181_1277 Sputw3181_3491 Sputw3181_3553
            ILO: IL1439(lysC) IL2466(metL)
            CPS: CPS_0456(metL) CPS_2004(lysC) CPS_4291(thrA)
            PHA: PSHAa0533(lysC) PSHAa1250(lysC) PSHAa2379(thrA)
                 PSHAa2722(metL)
            PAT: Patl_3425 Patl_3580
            SDE: Sde_1192 Sde_1300
            PIN: Ping_1275 Ping_3379
            MAQ: Maqu_0149 Maqu_0966
            CBU: CBU_1051
            CBD: COXBU7E912_0991(lysC)
            LPN: lpg1811(lysC)
            LPF: lpl1775(lysAC)
            LPP: lpp1774(lysAC)
            MCA: MCA0390
            FTW: FTW_1648
            FTA: FTA_0521
            FTN: FTN_0525(thrA) FTN_1730(lysC)
            TCX: Tcr_0521 Tcr_1589
            NOC: Noc_0927 Noc_1029
            AEH: Mlg_1480
            HHA: Hhal_1652
            HCH: HCH_05208
            CSA: Csal_0626
            ABO: ABO_1797(lysC)
            MMW: Mmwyl1_3627
            AHA: AHA_0590 AHA_2570 AHA_3018 AHA_3713
            DNO: DNO_0285
            CRP: CRP_108
            RMA: Rmag_0585
            VOK: COSY_0540
            NME: NMB1498
            NMA: NMA1701(lysC)
            NMC: NMC1429(lysC)
            NGO: NGO0956
            CVI: CV_1018(lysC)
            RSO: RSc1171(lysC)
            REU: Reut_A1126
            REH: H16_A1225(lysC)
            RME: Rmet_1089
            BMA: BMA1652
            BMV: BMASAVP1_A2154
            BML: BMA10299_A3161
            BMN: BMA10247_1427
            BXE: Bxe_A1630
            BVI: Bcep1808_1976
            BUR: Bcep18194_A5380
            BCN: Bcen_6003
            BCH: Bcen2424_2074
            BAM: Bamb_2109
            BPS: BPSL2239(ask)
            BPM: BURPS1710b_2677(ask)
            BPL: BURPS1106A_2591
            BPD: BURPS668_2540
            BTE: BTH_I1945
            PNU: Pnuc_0862
            BPE: BP1913(ask)
            BPA: BPP2287(ask)
            BBR: BB1739(ask)
            RFR: Rfer_1353
            POL: Bpro_2860
            PNA: Pnap_2889
            AAV: Aave_2324
            AJS: Ajs_1628
            VEI: Veis_4940
            MPT: Mpe_A2452
            HAR: HEAR1290(ask) HEAR2647(dnaK)
            MMS: mma_2104(lysC)
            NEU: NE2132(lysC)
            NET: Neut_2084
            NMU: Nmul_A1941
            EBA: ebA637(lysC)
            AZO: azo3115(lysC)
            DAR: Daro_2515
            TBD: Tbd_0969
            MFA: Mfla_0567
            HPY: HP1229
            HPA: HPAG1_1171
            HHE: HH0618(lysC)
            HAC: Hac_1646(lysC)
            WSU: WS1729(lysC)
            TDN: Tmden_1650
            CJE: Cj0582(lysC)
            CJR: CJE0685
            CJJ: CJJ81176_0610
            CJU: C8J_0544
            CJD: JJD26997_1087
            CFF: CFF8240_1116
            CCV: CCV52592_1570
            CHA: CHAB381_0999
            CCO: CCC13826_0334 CCC13826_2018
            ABU: Abu_1199(lysC)
            NIS: NIS_1140
            SUN: SUN_0456
            GSU: GSU1799
            GME: Gmet_1880
            GUR: Gura_2318
            PCA: Pcar_1006
            PPD: Ppro_2262
            DVU: DVU1913
            DVL: Dvul_1251
            DDE: Dde_2048
            LIP: LI1003(lysC)
            BBA: Bd0134(lysC) Bd0528(lysC)
            DPS: DP0451
            ADE: Adeh_1815 Adeh_3589
            AFW: Anae109_3710
            MXA: MXAN_0971 MXAN_2278 MXAN_3466 MXAN_4877
            SAT: SYN_02781
            SFU: Sfum_2173
            RPR: RP753
            RTY: RT0738(lysC)
            RCO: RC1164(lysC)
            RFE: RF_1200(lysC)
            RBE: RBE_1404(lysC)
            RAK: A1C_05685
            RBO: A1I_07820
            RCM: A1E_04850
            RRI: A1G_06400
            OTS: OTBS_1537(lysC)
            WOL: WD0960(lysC)
            WBM: Wbm0441
            AMA: AM1005(lysC)
            ERU: Erum7720(lysC)
            ERW: ERWE_CDS_08160(lysC)
            ERG: ERGA_CDS_08060(lysC)
            ECN: Ecaj_0808
            ECH: ECH_1001
            PUB: SAR11_0516(lysC)
            MLO: mll3437
            MES: Meso_3001
            PLA: Plav_1743
            SME: SMc02438(lysC)
            SMD: Smed_2504
            ATU: Atu4172(lysC)
            ATC: AGR_L_1357
            RET: RHE_CH03758(lysC)
            RLE: RL4284(ask)
            BME: BMEI0189
            BMF: BAB1_1874
            BMS: BR1871
            BMB: BruAb1_1850
            BOV: BOV_1802
            OAN: Oant_1034
            BJA: blr0216(lysC)
            BRA: BRADO0574(lysC)
            BBT: BBta_7602(lysC)
            RPA: RPA0604(lysC)
            RPB: RPB_0077
            RPC: RPC_0514
            RPD: RPD_0099
            RPE: RPE_0158
            NWI: Nwi_0379
            NHA: Nham_0472
            BHE: BH04030(lysC)
            BQU: BQ03060(lysC)
            BBK: BARBAKC583_0370
            XAU: Xaut_2625
            CCR: CC_0843
            SIL: SPO3035
            SIT: TM1040_0554 TM1040_1934
            RSP: RSP_1849
            RSH: Rsph17029_0498
            RSQ: Rsph17025_0636
            JAN: Jann_3191
            RDE: RD1_2157
            PDE: Pden_0862
            MMR: Mmar10_0407 Mmar10_1098 Mmar10_2259
            HNE: HNE_0618 HNE_1643
            ZMO: ZMO1653(lysC)
            NAR: Saro_3304
            SAL: Sala_2144 Sala_2953
            SWI: Swit_4503
            ELI: ELI_14545
            GOX: GOX0037
            GBE: GbCGDNIH1_0600
            ACR: Acry_1008
            RRU: Rru_A0743
            MAG: amb1612
            MGM: Mmc1_0966
            ABA: Acid345_1482 Acid345_2491
            SUS: Acid_0052 Acid_6982
            BSU: BG10350(lysC) BG10784(dapG) BG12033(yclM)
            BHA: BH1500 BH2400(dapG) BH3096(lysC)
            BAN: BA1811(dapG-1) BA3936(dapG-2)
            BAR: GBAA1811(dapG-1) GBAA3936(dapG-2)
            BAA: BA_2315 BA_4408
            BAT: BAS1676 BAS3651
            BCE: BC1748 BC3798
            BCA: BCE_1883(dapG) BCE_3837(dapG)
            BCZ: BCZK1623(dapG) BCZK3559(dapG)
            BCY: Bcer98_1430 Bcer98_2452
            BTK: BT9727_1658(dapG) BT9727_3541(dapG)
            BLI: BL00324(lysC) BL01209(dapG) BL01851
            BLD: BLi00462(yclM) BLi01901(dapG) BLi02996(lysC)
            BCL: ABC1763 ABC2215(dapG)
            BAY: RBAM_016600 RBAM_025540(lysC)
            BPU: BPUM_0356(yclM) BPUM_1580 BPUM_2505(lysC)
            OIH: OB1611(dapG) OB1871
            GKA: GK1276(dapG) GK3195
            SAU: SA1163 SA1225(lysC)
            SAV: SAV1327 SAV1393(lysC)
            SAM: MW1214 MW1281(lysC)
            SAR: SAR1337 SAR1405(lysC)
            SAS: SAS1267 SAS1334
            SAC: SACOL1360 SACOL1428(lysC)
            SAB: SAB1185c SAB1248(lysC)
            SAA: SAUSA300_1225 SAUSA300_1286
            SAO: SAOUHSC_01319 SAOUHSC_01394
            SAJ: SaurJH9_1388 SaurJH9_1454
            SAH: SaurJH1_1415 SaurJH1_1483
            SEP: SE1008 SE1073
            SER: SERP0896 SERP0963(lysC)
            SHA: SH1518(lysC) SH1580
            SSP: SSP1357 SSP1439
            LMO: lmo1235 lmo1436 lmo2374
            LMF: LMOf2365_1244 LMOf2365_1455 LMOf2365_2345
            LIN: lin1198 lin1475 lin2473
            LWE: lwe1190(dapG) lwe1453 lwe2323
            LLA: L0097(thrA)
            LLC: LACR_0783
            LLM: llmg_1820(thrA)
            SPN: SP_0413
            SPR: spr0374(lysC)
            SPD: SPD_0377
            SAG: SAG0339
            SAN: gbs0327
            SAK: SAK_0414
            SMU: SMU.1748(akh)
            STC: str0378(lysC)
            STL: stu0378(lysC)
            SSA: SSA_1943(lysC)
            SGO: SGO_1701
            LPL: lp_0979(thrA1) lp_2308(thrA2)
            LAC: LBA0850 LBA1215
            LSL: LSL_1058(lysC)
            LDB: Ldb1349(ask)
            LBU: LBUL_1258
            LCA: LSEI_0099 LSEI_2152
            LRE: Lreu_0611
            EFA: EF0368
            OOE: OEOE_1544
            STH: STH1548 STH1686
            CAC: CAC0278 CAC1810(dapG)
            CPE: CPE1678(dapG)
            CPF: CPF_1932
            CPR: CPR_1650
            CTC: CTC01282 CTC01446 CTC02356
            CNO: NT01CX_0187 NT01CX_2128
            CTH: Cthe_1375
            CDF: CD1322(dapG) CD2054(lysC)
            CBO: CBO1640(apk) CBO3337(lysC)
            CBA: CLB_1657 CLB_2273(dapG) CLB_3395(lysC)
            CBH: CLC_1666 CLC_2256(dapG) CLC_3282(lysC)
            CBF: CLI_1717 CLI_2465(dapG) CLI_3510(lysC)
            CBE: Cbei_1211 Cbei_4207
            CKL: CKL_0607(lysC1) CKL_1440(lysC2)
            AMT: Amet_0935 Amet_3194 Amet_3407
            CHY: CHY_1155 CHY_1909
            DSY: DSY2077 DSY2499 DSY5002
            DRM: Dred_1167 Dred_1940
            SWO: Swol_1317
            CSC: Csac_0991
            TTE: TTE1382(lysC)
            MTA: Moth_1067 Moth_1304
            MTU: Rv3709c(ask)
            MTC: MT3812(ask)
            MBO: Mb3736c(ask)
            MBB: BCG_3769c(ask)
            MLE: ML2323(ask)
            MPA: MAP0311c(ask)
            MAV: MAV_0393
            MSM: MSMEG_6257
            MVA: Mvan_5504
            MGI: Mflv_1304
            MMC: Mmcs_4889
            MKM: Mkms_4978
            MJL: Mjls_5257
            CGL: NCgl0247(cgl0251)
            CGB: cg0306(lysC)
            CEF: CE0220(ask)
            CDI: DIP0277(lysC)
            CJK: jk1998(lysC)
            NFA: nfa3180
            RHA: RHA1_ro04291(ask)
            SCO: SCO3615(ask)
            SMA: SAV4559(lysC)
            TWH: TWT708(ask)
            TWS: TW725(lysC)
            LXX: Lxx03450(lysC)
            CMI: CMM_0902(lysC)
            AAU: AAur_0661(ask)
            PAC: PPA2148
            NCA: Noca_0321
            TFU: Tfu_0043
            FRA: Francci3_0262 Francci3_2071
            FAL: FRAAL0605(ask) FRAAL2411
            ACE: Acel_2012
            KRA: Krad_0463
            SEN: SACE_0282(lysC)
            STP: Strop_0226
            BLO: BL0493(askB) BL0494(askA)
            BAD: BAD_0139(askA) BAD_0140(askB)
            RXY: Rxyl_0098 Rxyl_1090
            RBA: RB8926(ask)
            CTR: CT362(lysC)
            CTA: CTA_0394(lysC)
            CMU: TC0641
            CPN: CPn1049(lysC)
            CPA: CP0803
            CPJ: CPj1049(lysC)
            CPT: CpB1090
            CCA: CCA00713(lysC)
            CAB: CAB678(lysC)
            CFE: CF0305(lysC)
            PCU: pc0765(lysC)
            LIL: LA0693(lysC)
            LIC: LIC12909(lysC)
            LBJ: LBJ_0538(lysC)
            LBL: LBL_2541(lysC)
            SYN: slr0657(lysC)
            SYW: SYNW0070(lysC)
            SYC: syc0544_d(lysC)
            SYF: Synpcc7942_1001
            SYD: Syncc9605_0071
            SYE: Syncc9902_0068
            SYG: sync_0075
            SYR: SynRCC307_0075(lysC)
            SYX: SynWH7803_0081(lysC)
            CYA: CYA_1747
            CYB: CYB_0217
            TEL: tlr1833
            GVI: gll1774
            ANA: alr3644
            AVA: Ava_3642
            PMA: Pro1808(lysC)
            PMM: PMM1648(lysC)
            PMT: PMT0073(lysC)
            PMN: PMN2A_1246
            PMI: PMT9312_1740
            PMB: A9601_18571(lysC)
            PMC: P9515_18381(lysC)
            PMF: P9303_00821(lysC)
            PMG: P9301_18381(lysC)
            PME: NATL1_21161(lysC)
            TER: Tery_0087
            BTH: BT_1375 BT_2403
            BFR: BF0576 BF0608 BF3050
            BFS: BF0526 BF0558(thrA) BF2886
            PGI: PG2189(lysC)
            SRU: SRU_0301 SRU_0481(lysC) SRU_0482 SRU_0691 SRU_1745(lysC)
            CHU: CHU_0073(thrA) CHU_3721(lysC)
            GFO: GFO_1550(lysC) GFO_3518(lysC)
            FJO: Fjoh_0535 Fjoh_1494 Fjoh_2575
            FPS: FP0302(lysC)
            CTE: CT0095(lysC) CT2030
            CCH: Cag_0142 Cag_2023
            CPH: Cpha266_2542 Cpha266_2583
            PVI: Cvib_1626 Cvib_1702
            PLT: Plut_1983 Plut_2060
            DET: DET1633(metL)
            DEH: cbdb_A1731(metL)
            DEB: DehaBAV1_1378
            RRS: RoseRS_2031 RoseRS_3079
            RCA: Rcas_3005 Rcas_3187
            DRA: DR_1365
            DGE: Dgeo_1127
            TTH: TTC0166
            TTJ: TTHA0534
            AAE: aq_1152(lysC)
            TMA: TM0547 TM1518
            TPT: Tpet_1274
            TME: Tmel_0734 Tmel_1878
            FNO: Fnod_0075 Fnod_1282
            MMP: MMP1017(lysC)
            MMQ: MmarC5_0577
            MMZ: MmarC7_0259
            MAE: Maeo_0676
            MVN: Mevan_0346
            MAC: MA0131
            MBA: Mbar_A0861
            MMA: MM_1417
            MBU: Mbur_1980
            MTP: Mthe_1253
            MHU: Mhun_3054
            MEM: Memar_0222
            MBN: Mboo_0087
            MST: Msp_0107
            MSI: Msm_0832
            MKA: MK0109(lysC)
            HAL: VNG2374Gm(lysC)
            HMA: rrnAC2663(lysC)
            HWA: HQ1005A(lysC)
            NPH: NP0550A(lysC)
            TAC: Ta0364
            PTO: PTO1368
            PAB: PAB1675(lysC)
            PFU: PF1053
            TKO: TK1445
            RCI: RCIX1827(lysC)
            APE: APE_1140.1
            IHO: Igni_0199
            SSO: SSO0876(akh)
            STO: ST1241
            SAI: Saci_1412
            MSE: Msed_1699
            PAI: PAE2877
            PIS: Pisl_0273
            PCL: Pcal_0377
            PAS: Pars_0958
STRUCTURES  PDB: 2CDQ  2DT9  2DTJ  2HMF  2J0W  2J0X  2RE1  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.2.4
            ExPASy - ENZYME nomenclature database: 2.7.2.4
            ExplorEnz - The Enzyme Database: 2.7.2.4
            ERGO genome analysis and discovery system: 2.7.2.4
            BRENDA, the Enzyme Database: 2.7.2.4
            CAS: 9012-50-4
///
ENTRY       EC 2.7.2.5        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a carboxy group as acceptor
COMMENT     Deleted entry: now EC 6.3.4.16 carbamoyl-phosphate synthase
            (ammonia) (EC 2.7.2.5 created 1965, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.2.5
            ExPASy - ENZYME nomenclature database: 2.7.2.5
            ExplorEnz - The Enzyme Database: 2.7.2.5
            ERGO genome analysis and discovery system: 2.7.2.5
            BRENDA, the Enzyme Database: 2.7.2.5
///
ENTRY       EC 2.7.2.6                  Enzyme
NAME        formate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a carboxy group as acceptor
SYSNAME     ATP:formate phosphotransferase
REACTION    ATP + formate = ADP + formyl phosphate [RN:R00518]
ALL_REAC    R00518
SUBSTRATE   ATP [CPD:C00002];
            formate [CPD:C00058]
PRODUCT     ADP [CPD:C00008];
            formyl phosphate [CPD:C02405]
REFERENCE   1
  AUTHORS   Sly, W.S. and Stadtman, E.R.
  TITLE     Formate metabolism. II. Enzymatic synthesis of formyl phosphate and
            formyl coenzyme A in Clostridium cylindrosporum.
  JOURNAL   J. Biol. Chem. 238 (1963) 2639-2647.
  ORGANISM  Clostridium cylindrosporum
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.2.6
            ExPASy - ENZYME nomenclature database: 2.7.2.6
            ExplorEnz - The Enzyme Database: 2.7.2.6
            ERGO genome analysis and discovery system: 2.7.2.6
            BRENDA, the Enzyme Database: 2.7.2.6
            CAS: 9026-65-7
///
ENTRY       EC 2.7.2.7                  Enzyme
NAME        butyrate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a carboxy group as acceptor
SYSNAME     ATP:butanoate 1-phosphotransferase
REACTION    ATP + butanoate = ADP + butanoyl phosphate [RN:R01688]
ALL_REAC    R01688
SUBSTRATE   ATP [CPD:C00002];
            butanoate [CPD:C00246]
PRODUCT     ADP [CPD:C00008];
            butanoyl phosphate [CPD:C02527]
COMMENT     The enzyme from Clostridium sp. also acts, more slowly, on
            pentanoate and propanoate, and on some branched-chain fatty acids
            (cf. EC 2.7.1.14 sedoheptulokinase).
REFERENCE   1  [PMID:3027059]
  AUTHORS   Hartmanis MG.
  TITLE     Butyrate kinase from Clostridium acetobutylicum.
  JOURNAL   J. Biol. Chem. 262 (1987) 617-21.
  ORGANISM  Clostridium acetobutylicum [GN:cac]
REFERENCE   2
  AUTHORS   Twarog, R. and Wolfe, R.S.
  TITLE     Enzymatic phosphorylation of butyrate.
  JOURNAL   J. Biol. Chem. 237 (1962) 2474-2477.
  ORGANISM  Clostridium butyricum
PATHWAY     PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K00929  butyrate kinase
GENES       GME: Gmet_2106 Gmet_2128
            PCA: Pcar_2852
            DVU: DVU0628(buk)
            DDE: Dde_3128
            ADE: Adeh_0042
            SAT: SYN_01210 SYN_03090
            RDE: RD1_0841(buk)
            BSU: BG11724(buk)
            BAN: BA4386(buk)
            BAR: GBAA4386(buk)
            BAA: BA_4841
            BAT: BAS4069
            BCE: BC4161
            BCA: BCE_4236(buk)
            BCZ: BCZK3916(ackA)
            BTK: BT9727_3907(ackA)
            BLI: BL01502(buk)
            BLD: BLi02584(buk)
            BAY: RBAM_022350(buk)
            BPU: BPUM_2146(buk)
            OIH: OB1868
            GKA: GK2380
            LMO: lmo1370
            LMF: LMOf2365_1387
            LIN: lin1407
            LWE: lwe1385
            LCA: LSEI_1447
            EFA: EF1662(buk)
            STH: STH1826 STH1829
            CAC: CAC1660 CAC3075(buk)
            CPE: CPE2347(buk)
            CPF: CPF_2656(buk)
            CPR: CPR_2342
            CTC: CTC02545
            CDF: CD0113(buk) CD2379 CD2426
            CBO: CBO3426(buk1) CBO3428(buk2)
            CBA: CLB_3482(buk-1) CLB_3484(buk-2)
            CBH: CLC_3370(buk-1) CLC_3372(buk-2)
            CBF: CLI_3608(buk-1) CLI_3610(buk-2)
            DSY: DSY2401
            TTE: TTE2201 TTE2205
            BTH: BT_2552
            BFR: BF4336
            BFS: BF4137
            DRA: DR_1120
            DGE: Dgeo_1383
            TMA: TM1754 TM1756
STRUCTURES  PDB: 1SAZ  1X9J  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.2.7
            ExPASy - ENZYME nomenclature database: 2.7.2.7
            ExplorEnz - The Enzyme Database: 2.7.2.7
            ERGO genome analysis and discovery system: 2.7.2.7
            BRENDA, the Enzyme Database: 2.7.2.7
            CAS: 37278-14-1
///
ENTRY       EC 2.7.2.8                  Enzyme
NAME        acetylglutamate kinase;
            N-acetylglutamate 5-phosphotransferase;
            acetylglutamate phosphokinase;
            N-acetylglutamate phosphokinase;
            N-acetylglutamate kinase;
            N-acetylglutamic 5-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a carboxy group as acceptor
SYSNAME     ATP:N-acetyl-L-glutamate 5-phosphotransferase
REACTION    ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
            [RN:R02649]
ALL_REAC    R02649
SUBSTRATE   ATP [CPD:C00002];
            N-acetyl-L-glutamate [CPD:C00624]
PRODUCT     ADP [CPD:C00008];
            N-acetyl-L-glutamyl 5-phosphate [CPD:C04133]
REFERENCE   1  [PMID:13863980]
  AUTHORS   BAICH A, VOGEL HJ.
  TITLE     N-Acetyl-gamma-Ilutamokinase and N-acetylglutamic gamma-semialdehyde
            dehydrogenase: repressible enzymes of arginine synthesis in
            Escherichia coli.
  JOURNAL   Biochem. Biophys. Res. Commun. 7 (1962) 491-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:6040410]
  AUTHORS   Farago A, Denes G.
  TITLE     Mechanism of arginine biosynthesis in Chlamydomonas reinhardti. II.
            Purification and properties of N-acetylglutamate
            5-phosphotransferase, the allosteric enzyme of the pathway.
  JOURNAL   Biochim. Biophys. Acta. 136 (1967) 6-18.
  ORGANISM  Chlamydomonas reinhardti
REFERENCE   3
  AUTHORS   Vogel, H.J. and McLellan, W.L.
  TITLE     N-Acetyl-gamma-glutamokinase (Escherichia coli).
  JOURNAL   Methods Enzymol. 17A (1970) 251-255.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K00930  acetylglutamate kinase
GENES       ATH: AT3G57560
            OSA: 4330205 4336590
            SCE: YER069W(ARG5,6)
            AGO: AGOS_ADL062W
            PIC: PICST_55623
            CGR: CAGL0J03124g
            SPO: SPAC4G9.09c(arg11)
            CNE: CNF02250
            DDI: DDB_0231462(argC)
            ECO: b3959(argB)
            ECJ: JW5553(argB)
            ECE: Z5517(argB)
            ECS: ECs4888
            ECC: c4918(argB)
            ECI: UTI89_C4550(argB)
            ECP: ECP_4172
            ECV: APECO1_2508(argB)
            ECW: EcE24377A_4498(argB)
            ECX: EcHS_A4193
            STY: STY3751(argB)
            STT: t3502(argB)
            SPT: SPA3960(argB)
            SEC: SC4012(argB)
            STM: STM4122(argB)
            YPE: YPO3925(argB)
            YPK: y0311(argB)
            YPM: YP_3124(argB)
            YPA: YPA_0098
            YPN: YPN_0043
            YPS: YPTB0111(argB)
            YPI: YpsIP31758_0128(argB)
            SFL: SF4036(argB)
            SFX: S3710(argB)
            SFV: SFV_4028(argB)
            SSN: SSON_4132(argB)
            SBO: SBO_3978(argB)
            SDY: SDY_3794(argB)
            ECA: ECA0193(argB)
            PLU: plu4743(argB)
            BUC: BU049(argB)
            BAS: BUsg046(argB)
            BCC: BCc_031(argB)
            SGL: SG2160
            HDU: HD0891(argB)
            PMU: PM1119(argB)
            MSU: MS0236(argB)
            APL: APL_0243(argB)
            XFA: XF1001
            XFT: PD0293(argB)
            XCC: XCC2245(argB)
            XCB: XC_1873
            XCV: XCV2547(argB)
            XAC: XAC2348(argB)
            XOO: XOO2672(argB)
            XOM: XOO_2518(XOO2518)
            VCH: VC2643
            VCO: VC0395_A2219(argB)
            VVU: VV1_1372
            VVY: VV3001
            VPA: VP2758
            VFI: VF2305
            PPR: PBPRA0267
            PAE: PA5323(argB)
            PAU: PA14_70280(argB)
            PPU: PP_5289(argB)
            PPF: Pput_5198
            PST: PSPTO_0082(argB)
            PSB: Psyr_0218
            PSP: PSPPH_0206(argB)
            PFL: PFL_6055(argB)
            PFO: Pfl_5543
            PEN: PSEEN5435(argB)
            PMY: Pmen_4380
            PAR: Psyc_0579(argB)
            PCR: Pcryo_0568
            PRW: PsycPRwf_1828
            ACI: ACIAD0903(argB)
            SON: SO_0276(argB)
            SDN: Sden_0251
            SFR: Sfri_0192
            SHE: Shewmr4_3708
            SHM: Shewmr7_0237
            SHN: Shewana3_3904
            ILO: IL0613(argB)
            CPS: CPS_0461(argB)
            PHA: PSHAa2290(argB)
            PAT: Patl_0981
            SDE: Sde_3675
            PIN: Ping_0229
            MAQ: Maqu_3560
            MCA: MCA2781(argB)
            TCX: Tcr_1899
            NOC: Noc_2995
            AEH: Mlg_0084
            HHA: Hhal_2296
            HCH: HCH_01027(argB)
            CSA: Csal_2984
            ABO: ABO_0210(argB)
            MMW: Mmwyl1_0621
            AHA: AHA_0594(argB)
            RMA: Rmag_0232
            VOK: COSY_0223(argB)
            NME: NMB1074
            NMA: NMA1275(argB)
            NMC: NMC1038(argB)
            NGO: NGO0844
            CVI: CV_3921(argB)
            RSO: RSc0033(argB)
            REU: Reut_A0180
            REH: H16_A0208(argB)
            RME: Rmet_0140
            BMA: BMA3249(argB)
            BMV: BMASAVP1_A2910(argB)
            BML: BMA10299_A2179(argB)
            BMN: BMA10247_3438(argB)
            BXE: Bxe_A4385
            BVI: Bcep1808_3179
            BUR: Bcep18194_A6447 Bcep18194_B2621
            BCN: Bcen_2482
            BCH: Bcen2424_3096
            BAM: Bamb_3143
            BPS: BPSL0200(argB)
            BPM: BURPS1710b_0380(argB)
            BPL: BURPS1106A_0195(argB)
            BPD: BURPS668_0185(argB)
            BTE: BTH_I0160
            PNU: Pnuc_2013
            BPE: BP0383(argB)
            BPA: BPP4047(argB)
            BBR: BB4520(argB)
            RFR: Rfer_3524
            POL: Bpro_3982
            PNA: Pnap_3479
            AAV: Aave_4139
            AJS: Ajs_0588
            VEI: Veis_1226
            MPT: Mpe_A0499
            HAR: HEAR2988(argB)
            MMS: mma_3235
            NEU: NE1005(argB)
            NET: Neut_2384
            NMU: Nmul_A1116
            EBA: ebA4330(argB)
            AZO: azo3244(argB)
            DAR: Daro_0629
            TBD: Tbd_2686
            MFA: Mfla_2255
            HHE: HH0179(argB)
            WSU: WS2140(argB)
            TDN: Tmden_0854
            CJE: Cj0226(argB)
            CJR: CJE0277(argB)
            CJJ: CJJ81176_0251(argB)
            CJU: C8J_0204(argB)
            CJD: JJD26997_0224(argB)
            CFF: CFF8240_1081(argB)
            CCV: CCV52592_0128(argB)
            CHA: CHAB381_1022(argB)
            ABU: Abu_2068(argB)
            NIS: NIS_1042(argB)
            SUN: SUN_1628(argB)
            GSU: GSU0150(argB)
            GME: Gmet_0203
            GUR: Gura_0225
            PCA: Pcar_2413
            PPD: Ppro_3174
            DVU: DVU1466(argB)
            DVL: Dvul_1613
            DDE: Dde_2015
            LIP: LI0333(argB)
            DPS: DP0439
            ADE: Adeh_0587
            AFW: Anae109_0632
            MXA: MXAN_5105(argB)
            SAT: SYN_02154
            SFU: Sfum_0064
            RCO: RC0139(argB)
            RFE: RF_0086(argB)
            RBE: RBE_1276(argB)
            OTS: OTBS_1414(argB)
            WOL: WD0245(argB)
            WBM: Wbm0356
            AMA: AM763(agk)
            APH: APH_0422(argB)
            ERU: Erum4480(argB)
            ERW: ERWE_CDS_04700(argB)
            ERG: ERGA_CDS_04600(argB)
            ECN: Ecaj_0444
            ECH: ECH_0594(argB)
            PUB: SAR11_0465(argB)
            MLO: mlr4826
            MES: Meso_0380
            SME: SMc01726(argB)
            ATU: Atu0380(argB)
            ATC: AGR_C_666
            RET: RHE_CH00428(argB)
            RLE: RL0445(argB) RL4700
            BME: BMEII0273
            BMF: BAB2_0988
            BMS: BRA1025(argB)
            BMB: BruAb2_0965(argB)
            BOV: BOV_A0966(argB)
            OAN: Oant_1358
            BJA: blr8101(argB)
            BRA: BRADO0779(argB)
            BBT: BBta_7329(argB)
            RPA: RPA0629(argB)
            RPB: RPB_0680
            RPC: RPC_0814
            RPD: RPD_0072
            RPE: RPE_0647
            NWI: Nwi_3071
            NHA: Nham_3700
            BHE: BH00690(argB)
            BQU: BQ00620(argB)
            BBK: BARBAKC583_1326(argB)
            CCR: CC_0283
            SIL: SPO0526(argB)
            SIT: TM1040_0301
            RSP: RSP_1068(argB)
            JAN: Jann_0633
            RDE: RD1_1452(argB)
            MMR: Mmar10_0365
            HNE: HNE_0418(argB)
            ZMO: ZMO1494(argB)
            NAR: Saro_3297
            SAL: Sala_3095
            ELI: ELI_11540
            GOX: GOX1829
            GBE: GbCGDNIH1_0373 GbCGDNIH1_0734
            ACR: Acry_2143
            RRU: Rru_A3341
            MAG: amb4358
            MGM: Mmc1_3682
            ABA: Acid345_4160
            BSU: BG10193(argB)
            BHA: BH2898(argB)
            BAN: BA4353(argB)
            BAR: GBAA4353(argB)
            BAA: BA_4810
            BAT: BAS4038
            BCE: BC4128
            BCA: BCE_4201(argB)
            BCZ: BCZK3885(argB)
            BTK: BT9727_3877(argB)
            BLI: BL03243(argB)
            BLD: BLi01208(argB)
            BCL: ABC2556(argB)
            BAY: RBAM_011210
            BPU: BPUM_1044
            OIH: OB1077(argB)
            GKA: GK0792
            SAU: SA0176
            SAV: SAV0182
            SAM: MW0156
            SAR: SAR0183
            SAS: SAS0157
            SAC: SACOL0167(argB)
            SAB: SAB0122c
            SAA: SAUSA300_0184(argB)
            SAO: SAOUHSC_00147
            SEP: SE1210
            SER: SERP1090(argB)
            SSP: SSP0223
            LMO: lmo1589(argB)
            LMF: LMOf2365_1611(argB)
            LIN: lin1631(argB)
            LWE: lwe1602(argB)
            LLA: L0107(argB)
            LLC: LACR_0859
            LLM: llmg_1755(argB)
            SMU: SMU.665(argB)
            STC: str0466(argB)
            STL: stu0466(argB)
            SSA: SSA_0759(argB)
            SGO: SGO_1567(argB)
            LPL: lp_0488 lp_0530(argB)
            STH: STH2882
            CAC: CAC2389(argB)
            CNO: NT01CX_2380(argB)
            CTH: Cthe_1864
            CDF: CD2032(argB)
            CBE: Cbei_4519
            CKL: CKL_1555(argB)
            AMT: Amet_3381
            CHY: CHY_2263(argB)
            DSY: DSY0762
            DRM: Dred_0273
            SWO: Swol_2289
            CSC: Csac_1530
            TTE: TTE2496(argB)
            MTA: Moth_2288
            MTU: Rv1654(argB)
            MTC: MT1692(argB)
            MBO: Mb1682(argB)
            MBB: BCG_1693(argB)
            MLE: ML1408(argB)
            MPA: MAP1363(argB)
            MAV: MAV_3116(argB)
            MSM: MSMEG_3774(argB)
            MMC: Mmcs_2970
            CGL: NCgl1342(cgl1396)
            CGB: cg1582(argB)
            CEF: CE1528(argB)
            CDI: DIP1169(argB)
            CJK: jk0843(argB)
            NFA: nfa19380(argB)
            RHA: RHA1_ro00954(argB)
            SCO: SCO1578(argB)
            SMA: SAV6765(argB)
            LXX: Lxx06050(argB)
            CMI: CMM_1999(argB)
            ART: Arth_1498
            AAU: AAur_1633(argB)
            PAC: PPA1348
            NCA: Noca_2470
            TFU: Tfu_2055
            FRA: Francci3_3173
            FAL: FRAAL5206(argB)
            ACE: Acel_1261
            SEN: SACE_5260(argB)
            BLO: BL1062(argB)
            BAD: BAD_0923(argB)
            RXY: Rxyl_2887
            RBA: RB5983(argB)
            LIL: LB114(argB)
            LIC: LIC20090(argB)
            LBJ: LBJ_4096(argB)
            LBL: LBL_4112(argB)
            SYN: slr1898(argB)
            SYW: SYNW1780(argB)
            SYC: syc2482_c(argB)
            SYF: Synpcc7942_1496
            SYD: Syncc9605_0684
            SYE: Syncc9902_1674
            SYG: sync_2029(argB)
            SYR: SynRCC307_0886(argB)
            SYX: SynWH7803_0614(argB)
            CYA: CYA_0310(argB)
            CYB: CYB_1687(argB)
            TEL: tll1408(argB)
            GVI: gll3931(argB)
            ANA: alr1245(argB)
            AVA: Ava_0554
            PMA: Pro0499(argB)
            PMM: PMM0499(argB)
            PMT: PMT1268(argB)
            PMN: PMN2A_1832
            PMI: PMT9312_0500
            PMB: A9601_05561(argB)
            PMC: P9515_05631(argB)
            PMF: P9303_07341(argB)
            PMG: P9301_05261(argB)
            PMH: P9215_05811
            PME: NATL1_05571(argB)
            TER: Tery_1153
            BTH: BT_3395
            BFR: BF0240
            BFS: BF0197
            SRU: SRU_2219(argB)
            CHU: CHU_3086(argB)
            GFO: GFO_2101(argB)
            CTE: CT1111(argB)
            CCH: Cag_0774
            CPH: Cpha266_1322
            PVI: Cvib_0879
            PLT: Plut_1047
            DET: DET1257(argB)
            DEH: cbdb_A1180(argB)
            RCA: Rcas_3361
            DRA: DR_2442
            DGE: Dgeo_0079
            TTH: TTC1586
            TTJ: TTHA1950
            AAE: aq_2068(argB)
            TMA: TM1784
            TPT: Tpet_1071
            MMP: MMP0063(argB)
            MMQ: MmarC5_1614
            MMZ: MmarC7_1060
            MAE: Maeo_0127
            MVN: Mevan_1078
            MAC: MA4515(argB)
            MBA: Mbar_A1181
            MMA: MM_1220
            MBU: Mbur_0056
            MTP: Mthe_1732
            MHU: Mhun_3230
            MEM: Memar_0154
            MBN: Mboo_0071
            MST: Msp_0550(argB)
            MSI: Msm_0375
            MKA: MK1631(argB)
            HMA: rrnAC0078(argB1) rrnAC2676(argB2)
            HWA: HQ3716A(argB)
            NPH: NP5262A(argB)
            PTO: PTO1471
            PHO: PH1718
            PAB: PAB0292(argB)
            PFU: PF1684
            TKO: TK0276
            RCI: RRC322(argB)
            APE: APE_1461.1
            SSO: SSO0156(argB)
            STO: ST0194
            SAI: Saci_0751
            MSE: Msed_0165
            PAI: PAE2882(argB)
STRUCTURES  PDB: 1GS5  1GSJ  1OH9  1OHA  1OHB  2AP9  2BTY  2BUF  2RD5  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.2.8
            ExPASy - ENZYME nomenclature database: 2.7.2.8
            ExplorEnz - The Enzyme Database: 2.7.2.8
            ERGO genome analysis and discovery system: 2.7.2.8
            BRENDA, the Enzyme Database: 2.7.2.8
            CAS: 9027-58-1
///
ENTRY       EC 2.7.2.9        Obsolete  Enzyme
NAME        Transferred to 6.3.5.5
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a carboxy group as acceptor
COMMENT     Transferred entry: now EC 6.3.5.5, carbamoyl-phosphate synthase
            (glutamine-hydrolysing) (EC 2.7.2.9 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.2.9
            ExPASy - ENZYME nomenclature database: 2.7.2.9
            ExplorEnz - The Enzyme Database: 2.7.2.9
            ERGO genome analysis and discovery system: 2.7.2.9
            BRENDA, the Enzyme Database: 2.7.2.9
///
ENTRY       EC 2.7.2.10                 Enzyme
NAME        phosphoglycerate kinase (GTP)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a carboxy group as acceptor
SYSNAME     GTP:3-phospho-D-glycerate 1-phosphotransferase
REACTION    GTP + 3-phospho-D-glycerate = GDP + 3-phospho-D-glyceroyl phosphate
            [RN:R01517]
ALL_REAC    R01517
SUBSTRATE   GTP [CPD:C00044];
            3-phospho-D-glycerate [CPD:C00197]
PRODUCT     GDP [CPD:C00035];
            3-phospho-D-glyceroyl phosphate [CPD:C00236]
REFERENCE   1  [PMID:4365563]
  AUTHORS   Reeves RE, South DJ.
  TITLE     Phosphoglycerate kinase (GTP). An enzyme from Entamoeba histolytica
            selective for guanine nucleotides.
  JOURNAL   Biochem. Biophys. Res. Commun. 58 (1974) 1053-7.
  ORGANISM  Entamoeba histolytica [GN:ehi]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.2.10
            ExPASy - ENZYME nomenclature database: 2.7.2.10
            ExplorEnz - The Enzyme Database: 2.7.2.10
            ERGO genome analysis and discovery system: 2.7.2.10
            BRENDA, the Enzyme Database: 2.7.2.10
            CAS: 62213-34-7
///
ENTRY       EC 2.7.2.11                 Enzyme
NAME        glutamate 5-kinase;
            ATP-L-glutamate 5-phosphotransferase;
            ATP:gamma-L-glutamate phosphotransferase;
            gamma-glutamate kinase;
            gamma-glutamyl kinase;
            glutamate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a carboxy group as acceptor
SYSNAME     ATP:L-glutamate 5-phosphotransferase
REACTION    ATP + L-glutamate = ADP + L-glutamate 5-phosphate [RN:R00239]
ALL_REAC    R00239
SUBSTRATE   ATP [CPD:C00002];
            L-glutamate [CPD:C00025]
PRODUCT     ADP [CPD:C00008];
            L-glutamate 5-phosphate [CPD:C03287]
COMMENT     Product rapidly cyclizes to 5-oxoproline and phosphate.
REFERENCE   1  [PMID:4904678]
  AUTHORS   Baich A.
  TITLE     Proline synthesis in Escherichia coli. A proline-inhibitable
            glutamic acid kinase.
  JOURNAL   Biochim. Biophys. Acta. 192 (1969) 462-7.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K00931  glutamate 5-kinase
GENES       HSA: 5832(ALDH18A1)
            MMU: 56454(Aldh18a1)
            XLA: 444469(MGC81784)
            ATH: AT3G55610(P5CS2)
            OSA: 4324853 4338979
            CME: CMQ021C
            SCE: YDR300C(PRO1)
            AGO: AGOS_AAL061C
            PIC: PICST_29301(PRO2)
            CGR: CAGL0D03894g CAGL0H01441g
            SPO: SPAC17H9.13c
            ANI: AN5817.2
            AFM: AFUA_2G07570
            AOR: AO090011000935
            UMA: UM00215.1
            CPV: cgd2_2300
            CHO: Chro.20246
            LMA: LmjF26.2710
            ECO: b0242(proB)
            ECJ: JW0232(proB)
            ECE: Z0303(proB)
            ECS: ECs0269
            ECC: c0389(proB)
            ECI: UTI89_C0283(proB)
            ECP: ECP_0271
            ECV: APECO1_1727(proB)
            ECW: EcE24377A_0274(proB)
            ECX: EcHS_A0269
            STY: STY0366(proB)
            STT: t2529(proB)
            SPT: SPA2434(proB)
            SEC: SC0322(proB)
            STM: STM0321(proB)
            YPE: YPO3222(proB)
            YPK: y0966(proB)
            YPM: YP_0711(proB)
            YPA: YPA_2714
            YPN: YPN_0871
            YPP: YPDSF_2851
            YPS: YPTB0904(proB)
            YPI: YpsIP31758_3150(proB)
            SFL: SF0292(proB)
            SFX: S0313(proB)
            SFV: SFV_0286(proB)
            SSN: SSON_0284(proB)
            SBO: SBO_0248(proB)
            SDY: SDY_0474(proB)
            ECA: ECA3463(proB)
            PLU: plu1243(proB)
            SGL: SG0600
            ENT: Ent638_0768
            SPE: Spro_0967
            HIT: NTHI1066(proB)
            HSO: HS_0192(proB)
            PMU: PM1896(proB)
            MSU: MS1862(proB)
            APL: APL_0884(proB)
            ASU: Asuc_0717
            XFA: XF1004
            XFT: PD0296(proB)
            XCC: XCC2239(proB)
            XCB: XC_1879
            XCV: XCV2542(proB)
            XAC: XAC2343(proB)
            XOO: XOO2666(proB)
            XOM: XOO_2512(XOO2512)
            VCH: VC2274
            VCO: VC0395_A1864(proB)
            VVU: VV1_0326
            VVY: VV0858
            VPA: VP0676
            VFI: VF0740
            PPR: PBPRA0839
            PAE: PA4565(proB)
            PAU: PA14_60420(proB)
            PPU: PP_0691(proB)
            PPF: Pput_0723
            PST: PSPTO_0800(proB)
            PSB: Psyr_0704
            PSP: PSPPH_0716(proB)
            PFL: PFL_5326(proB)
            PFO: Pfl_4857
            PEN: PSEEN0829(proB)
            PMY: Pmen_3679
            PAR: Psyc_1503(proB)
            PCR: Pcryo_1682
            PRW: PsycPRwf_1600
            ACI: ACIAD2560(proB)
            SON: SO_1121(proB)
            SDN: Sden_0150 Sden_1180
            SFR: Sfri_0763 Sfri_0966
            SAZ: Sama_2516
            SBL: Sbal_0116 Sbal_3324
            SBM: Shew185_3416 Shew185_4284
            SLO: Shew_2848 Shew_3014
            SPC: Sputcn32_0082 Sputcn32_2976
            SSE: Ssed_3416
            SPL: Spea_3085
            SHE: Shewmr4_0952 Shewmr4_3848
            SHM: Shewmr7_0990 Shewmr7_3941
            SHN: Shewana3_0954 Shewana3_4056
            SHW: Sputw3181_0971 Sputw3181_3995
            ILO: IL1985(proB)
            CPS: CPS_4832(proB)
            PHA: PSHAa0279(proB) PSHAa0633(proB)
            PAT: Patl_4146 Patl_4269
            SDE: Sde_1011
            PIN: Ping_2635 Ping_2953
            MAQ: Maqu_0858
            LPN: lpg1610(proB)
            LPF: lpl1414(proB)
            LPP: lpp1575(proB)
            MCA: MCA2249(proB)
            TCX: Tcr_0344
            NOC: Noc_3036
            AEH: Mlg_0848
            HHA: Hhal_1845
            HCH: HCH_05938
            CSA: Csal_0477
            ABO: ABO_0455(proB)
            MMW: Mmwyl1_4235
            AHA: AHA_3421(proB)
            RMA: Rmag_0413
            VOK: COSY_0382(proB)
            NME: NMB1069
            NMA: NMA1268(proB)
            NMC: NMC1033(proB)
            CVI: CV_3960 CV_4212(proB)
            RSO: RSc2819(proB)
            REU: Reut_A2955
            REH: H16_A3249(proB)
            RME: Rmet_3103
            BMA: BMA2520(proB)
            BMV: BMASAVP1_A0443(proB)
            BML: BMA10299_A1302(proB)
            BMN: BMA10247_3261(proB)
            BXE: Bxe_A0510
            BVI: Bcep1808_0560
            BUR: Bcep18194_A3669
            BCN: Bcen_0102
            BCH: Bcen2424_0584
            BAM: Bamb_0487
            BPS: BPSL3002(proB)
            BPM: BURPS1710b_3521(proB)
            BPL: BURPS1106A_3523(proB)
            BPD: BURPS668_3486(proB)
            BTE: BTH_I1143(proB)
            PNU: Pnuc_0197
            BPE: BP0746(proB)
            BPA: BPP0308(proB)
            BBR: BB0311(proB)
            RFR: Rfer_1271
            POL: Bpro_0836
            PNA: Pnap_0748
            AAV: Aave_3672
            AJS: Ajs_0844
            VEI: Veis_3914
            MPT: Mpe_A0514
            HAR: HEAR2784(proB)
            MMS: mma_2991
            NEU: NE1290(proB)
            NET: Neut_0958
            NMU: Nmul_A1843
            EBA: ebA844(proB)
            AZO: azo3170(proB)
            DAR: Daro_3473
            TBD: Tbd_1120
            MFA: Mfla_2216
            HHE: HH0419(proB)
            WSU: WS0506(proB)
            TDN: Tmden_1413 Tmden_1684
            CJE: Cj0097(proB)
            CJR: CJE0092(proB)
            CJJ: CJJ81176_0132(proB)
            CJU: C8J_0090(proB)
            CFF: CFF8240_1535(proB)
            CCV: CCV52592_0755(proB)
            CHA: CHAB381_0677(proB)
            ABU: Abu_1607(proB)
            NIS: NIS_1231(proB)
            SUN: SUN_1781
            GSU: GSU3212(proB)
            GME: Gmet_3198
            GUR: Gura_4132
            PCA: Pcar_2580
            PPD: Ppro_2953
            DVU: DVU0930(proB)
            DVL: Dvul_2055
            DDE: Dde_2689
            DPS: DP2589
            ADE: Adeh_0211
            AFW: Anae109_0226
            MXA: MXAN_1357(proB)
            SAT: SYN_01350
            SFU: Sfum_3643
            PUB: SAR11_0223(proB)
            MLO: mll4011 mlr6298
            MES: Meso_3457
            PLA: Plav_1479
            SME: SMc03252(proB2) SMc03776(proB1)
            SMD: Smed_3010
            ATU: Atu2780(proB)
            ATC: AGR_C_5045
            RET: RHE_CH04068(proB)
            RLE: RL4682(proB)
            BME: BMEI0207
            BMF: BAB1_1852(proB)
            BMS: BR1844(proB)
            BMB: BruAb1_1823(proB)
            BOV: BOV_1777(proB)
            OAN: Oant_1055
            BJA: blr0428(proB)
            BRA: BRADO0431(proB)
            BBT: BBta_0422(proB)
            RPA: RPA0163(proB)
            RPB: RPB_0252
            RPC: RPC_0158
            RPD: RPD_0574
            RPE: RPE_0549
            NWI: Nwi_0443
            NHA: Nham_0518
            BHE: BH01570(proB)
            BQU: BQ01470(proB)
            BBK: BARBAKC583_0318(proB)
            XAU: Xaut_2056
            CCR: CC_0314
            SIL: SPO1985(proB)
            SIT: TM1040_1204
            RSP: RSP_3823(proB1)
            RSH: Rsph17029_3515
            RSQ: Rsph17025_3802
            JAN: Jann_2284
            RDE: RD1_2659(proB)
            PDE: Pden_4055
            MMR: Mmar10_2667 Mmar10_2790
            HNE: HNE_2567(proB)
            ZMO: ZMO0206(proB)
            NAR: Saro_1146
            SAL: Sala_2219
            SWI: Swit_3896
            ELI: ELI_01860
            GOX: GOX0142
            GBE: GbCGDNIH1_1706
            ACR: Acry_0234
            RRU: Rru_A1239
            MAG: amb4080
            MGM: Mmc1_3349
            ABA: Acid345_1267
            BSU: BG10963(proB) BG12658(proJ)
            BHA: BH1505
            BAN: BA2993(proB)
            BAR: GBAA2993(proB)
            BAA: BA_3500
            BAT: BAS2782
            BCE: BC2975
            BCA: BCE_3029(proB)
            BCZ: BCZK2712(proB)
            BTK: BT9727_2731(proB)
            BLI: BL01983(proJ) BL03752(proB)
            BLD: BLi01412(proB) BLi02149(proJ)
            BCL: ABC1767(proB)
            BAY: RBAM_012930 RBAM_018640
            BPU: BPUM_1207 BPUM_1823
            OIH: OB1052(proB)
            GKA: GK2048(proB)
            LMO: lmo1260(proB)
            LMF: LMOf2365_1277(proB)
            LIN: lin1228(proB)
            LWE: lwe1279(proB)
            LLA: L0117(proB)
            LLC: LACR_1717
            LLM: llmg_0885(proB)
            SPY: SPy_1672(proB)
            SPZ: M5005_Spy_1371
            SPM: spyM18_1681(proB)
            SPG: SpyM3_1407(proB)
            SPS: SPs0457
            SPH: MGAS10270_Spy1489
            SPI: MGAS10750_Spy1481
            SPJ: MGAS2096_Spy1394
            SPK: MGAS9429_Spy1369
            SPA: M6_Spy1419
            SPB: M28_Spy1414
            SPN: SP_0931
            SPR: spr0832(proB)
            SPD: SPD_0822(proB)
            SAG: SAG0283(proB)
            SAN: gbs0273(proB)
            SAK: SAK_0355(proB)
            SMU: SMU.449(proB)
            STC: str1711(proB)
            STL: stu1711(proB)
            SSA: SSA_1072(proB)
            SGO: SGO_1097(proB)
            LPL: lp_0016(proB)
            LSL: LSL_1612(proB)
            LCA: LSEI_2358
            LRE: Lreu_0346
            EFA: EF0038(proB)
            OOE: OEOE_0947
            STH: STH2540
            CAC: CAC3253(proB)
            CPE: CPE2579(proB)
            CPF: CPF_2904(proB)
            CPR: CPR_2583(proB)
            CTC: CTC01044
            CNO: NT01CX_0902(proB)
            CTH: Cthe_1766
            CBE: Cbei_0024
            CKL: CKL_0924(proB2) CKL_2736(proB1)
            AMT: Amet_0673 Amet_3645
            CHY: CHY_0380(proB)
            DSY: DSY1386
            DRM: Dred_1170
            SWO: Swol_1608
            CSC: Csac_1707
            TTE: TTE1277(proB)
            MTA: Moth_0562
            MTU: Rv2439c(proB)
            MTC: MT2515(proB)
            MBO: Mb2466c(proB)
            MBB: BCG_2459c(proB)
            MLE: ML1464(proB)
            MPA: MAP2263c(proB)
            MAV: MAV_1732(proB)
            MSM: MSMEG_4621(proB)
            MVA: Mvan_3943
            MGI: Mflv_2638
            MMC: Mmcs_3547
            MKM: Mkms_3620
            MJL: Mjls_3552
            CGL: NCgl2274(cgl2356)
            CGB: cg2588(proB)
            CEF: CE2265(proB)
            CDI: DIP1777(proB)
            CJK: jk0563(proB)
            NFA: nfa13560(proB)
            RHA: RHA1_ro01310(proB)
            SCO: SCO2587(proB)
            SMA: SAV5471(proB)
            LXX: Lxx08070(proB)
            ART: Arth_2388
            AAU: AAur_2364(proB)
            PAC: PPA0834
            NCA: Noca_3448
            TFU: Tfu_2179
            FRA: Francci3_1223
            FAL: FRAAL1928(proB)
            ACE: Acel_0759
            KRA: Krad_3454
            SEN: SACE_1417(proB)
            STP: Strop_0386
            BLO: BL1285(proB)
            BAD: BAD_0243(proB)
            RBA: RB12013(proB)
            TPA: TP0351
            LIL: LA0853(proB)
            LIC: LIC12772(proB)
            LBJ: LBJ_2491(proB)
            LBL: LBL_0620(proB)
            SYN: slr2035(proB)
            SYW: SYNW0782(proB)
            SYC: syc1900_c
            SYF: Synpcc7942_2197
            SYD: Syncc9605_1867
            SYE: Syncc9902_0786
            SYG: sync_1714(proB)
            SYR: SynRCC307_0999(proB)
            SYX: SynWH7803_1154(proB)
            CYA: CYA_2177(proB)
            CYB: CYB_0519(proB)
            TEL: tll2118(proB)
            GVI: gll0069(proB)
            ANA: alr3103
            AVA: Ava_3807
            PMA: Pro0864(proB)
            PMM: PMM0788(proB)
            PMT: PMT0529(proB)
            PMN: PMN2A_0196
            PMI: PMT9312_0796
            PMB: A9601_08521(proB)
            PMC: P9515_07931(proB)
            PMF: P9303_17361(proB)
            PMG: P9301_08491(proB)
            PMH: P9215_08831
            PME: NATL1_08281(proB)
            TER: Tery_1913
            BTH: BT_3719
            BFR: BF0499
            BFS: BF0444(proB)
            SRU: SRU_1252(proB)
            GFO: GFO_1962(proB)
            FJO: Fjoh_3431
            CTE: CT1457(proB)
            CCH: Cag_1096
            CPH: Cpha266_1864
            PVI: Cvib_1293
            PLT: Plut_1477
            DET: DET1282(proB)
            DEH: cbdb_A1212(proB)
            DEB: DehaBAV1_1093
            RRS: RoseRS_0762
            RCA: Rcas_4446
            DRA: DR_1827
            DGE: Dgeo_0992
            TTH: TTC1563
            TTJ: TTHA1927
            AAE: aq_1134(proB)
            TMA: TM0294
            TPT: Tpet_0618
            MAC: MA4101(proB)
            MBA: Mbar_A0481
            MMA: MM_0818
            MBU: Mbur_2415
            HWA: HQ1845A(proB)
            NPH: NP3976A(proB)
STRUCTURES  PDB: 2AKO  2J5T  2J5V  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.2.11
            ExPASy - ENZYME nomenclature database: 2.7.2.11
            ExplorEnz - The Enzyme Database: 2.7.2.11
            ERGO genome analysis and discovery system: 2.7.2.11
            BRENDA, the Enzyme Database: 2.7.2.11
            CAS: 54596-30-4
///
ENTRY       EC 2.7.2.12                 Enzyme
NAME        acetate kinase (diphosphate);
            pyrophosphate-acetate phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a carboxy group as acceptor
SYSNAME     diphosphate:acetate phosphotransferase
REACTION    diphosphate + acetate = phosphate + acetyl phosphate [RN:R00320]
ALL_REAC    R00320
SUBSTRATE   diphosphate [CPD:C00013];
            acetate [CPD:C00033]
PRODUCT     phosphate [CPD:C00009];
            acetyl phosphate [CPD:C00227]
REFERENCE   1  [PMID:172079]
  AUTHORS   Reeves RE, Guthrie JD.
  TITLE     Acetate kinase (pyrophosphate). A fourth pyrophosphate-dependent
            kinase from Entamoeba histolytica.
  JOURNAL   Biochem. Biophys. Res. Commun. 66 (1975) 1389-95.
  ORGANISM  Entamoeba histolytica [GN:ehi]
PATHWAY     PATH: map00620  Pyruvate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.2.12
            ExPASy - ENZYME nomenclature database: 2.7.2.12
            ExplorEnz - The Enzyme Database: 2.7.2.12
            ERGO genome analysis and discovery system: 2.7.2.12
            BRENDA, the Enzyme Database: 2.7.2.12
            CAS: 57657-58-6
///
ENTRY       EC 2.7.2.13                 Enzyme
NAME        glutamate 1-kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a carboxy group as acceptor
SYSNAME     ATP:L-glutamate 1-phosphotransferase
REACTION    ATP + L-glutamate = ADP + alpha-L-glutamyl phosphate [RN:R00241]
ALL_REAC    R00241;
            (other) R00240
SUBSTRATE   ATP [CPD:C00002];
            L-glutamate [CPD:C00025]
PRODUCT     ADP [CPD:C00008];
            alpha-L-glutamyl phosphate [CPD:C05765]
REFERENCE   1
  AUTHORS   Wang, W.-Y., Gough, S.P. and Kannangara, C.G.
  TITLE     Biosynthesis of delta-aminolevulinate in greening barley leaves. IV.
            Isolation of three soluble enzymes required for the conversion of
            glutamate to delta-aminolevulinate.
  JOURNAL   Carlsberg Res. Commun. 46 (1981) 243-257.
  ORGANISM  Hordeum vulgare [GN:ehvu]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.2.13
            ExPASy - ENZYME nomenclature database: 2.7.2.13
            ExplorEnz - The Enzyme Database: 2.7.2.13
            ERGO genome analysis and discovery system: 2.7.2.13
            BRENDA, the Enzyme Database: 2.7.2.13
            CAS: 80700-24-9
///
ENTRY       EC 2.7.2.14                 Enzyme
NAME        branched-chain-fatty-acid kinase;
            isobutyrate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a carboxy group as acceptor
SYSNAME     ATP:branched-chain-fatty-acid 1-phosphotransferase
REACTION    ATP + 2-methylpropanoate = ADP + 2-methylpropanoyl phosphate
            [RN:R04002]
ALL_REAC    R04002
SUBSTRATE   ATP [CPD:C00002];
            2-methylpropanoate [CPD:C02632]
PRODUCT     ADP [CPD:C00008];
            2-methylpropanoyl phosphate [CPD:C03754]
COMMENT     3-Methylbutanoate, 2-methylbutanoate, pentanoate, butanoate and
            propanoate can also act as acceptors (cf. EC 2.7.2.7 butyrate
            kinase).
REFERENCE   1  [PMID:6288660]
  AUTHORS   Harwood CS, Canale-Parola E.
  TITLE     Properties of acetate kinase isozymes and a branched-chain fatty
            acid kinase from a spirochete.
  JOURNAL   J. Bacteriol. 152 (1982) 246-54.
  ORGANISM  spirochete
GENES       BTL: BALH_3774
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.2.14
            ExPASy - ENZYME nomenclature database: 2.7.2.14
            ExplorEnz - The Enzyme Database: 2.7.2.14
            ERGO genome analysis and discovery system: 2.7.2.14
            BRENDA, the Enzyme Database: 2.7.2.14
            CAS: 84177-54-8
///
ENTRY       EC 2.7.2.15                 Enzyme
NAME        propionate kinase;
            PduW;
            TdcD;
            propionate/acetate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a carboxy group as acceptor
SYSNAME     ATP:propanoate phosphotransferase
REACTION    (1) ATP + propanoate = ADP + propanoyl phosphate [RN:R01353];
            (2) ATP + acetate = ADP + acetyl phosphate [RN:R00315]
ALL_REAC    R00315 R01353
SUBSTRATE   ATP [CPD:C00002];
            propanoate [CPD:C00163];
            acetate [CPD:C00033]
PRODUCT     ADP [CPD:C00008];
            propanoyl phosphate [CPD:C02876];
            acetyl phosphate [CPD:C00227]
COMMENT     Requires Mg2+. Both propanoate and acetate can act as a substrate.
            Involved in the anaerobic degradation of L-threonine in bacteria
            [1]. Both this enzyme and EC 2.7.2.1, acetate kinase, play important
            roles in the production of propanoate [1].
REFERENCE   1  [PMID:9484901]
  AUTHORS   Hesslinger C, Fairhurst SA, Sawers G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that degrades
            L-threonine to propionate.
  JOURNAL   Mol. Microbiol. 27 (1998) 477-92.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:12700259]
  AUTHORS   Palacios S, Starai VJ, Escalante-Semerena JC.
  TITLE     Propionyl coenzyme A is a common intermediate in the 1,2-propanediol
            and propionate catabolic pathways needed for expression of the
            prpBCDE operon during growth of Salmonella enterica on
            1,2-propanediol.
  JOURNAL   J. Bacteriol. 185 (2003) 2802-10.
  ORGANISM  Salmonella enterica
REFERENCE   3  [PMID:10498722]
  AUTHORS   Wei Y, Miller CG.
  TITLE     Characterization of a group of anaerobically induced, fnr-dependent
            genes of Salmonella typhimurium.
  JOURNAL   J. Bacteriol. 181 (1999) 6092-7.
  ORGANISM  Salmonella typhimurium
REFERENCE   4  [PMID:15774882]
  AUTHORS   Ingram-Smith C, Gorrell A, Lawrence SH, Iyer P, Smith K, Ferry JG.
  TITLE     Characterization of the acetate binding pocket in the Methanosarcina
            thermophila acetate kinase.
  JOURNAL   J. Bacteriol. 187 (2005) 2386-94.
  ORGANISM  Methanosarcina thermophila
REFERENCE   5
  AUTHORS   Simanshu, D.K.
  TITLE     Cloning, expression, purification, crystallization and preliminary
            X-ray diffraction analysis of propionate kinase (TdcD) from
            Salmonella typhimurium.
  JOURNAL   Acta Crystallogr. F Struct. Biol. Cryst. Commun. 61 (2005) 52-55.
  ORGANISM  Salmonella typhimurium
REFERENCE   6  [PMID:16139298]
  AUTHORS   Simanshu DK, Savithri HS, Murthy MR.
  TITLE     Crystal structures of ADP and AMPPNP-bound propionate kinase (TdcD)
            from Salmonella typhimurium: comparison with members of acetate and
            sugar kinase/heat shock cognate 70/actin superfamily.
  JOURNAL   J. Mol. Biol. 352 (2005) 876-92.
PATHWAY     PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K00932  propionate kinase
GENES       ECO: b3115(tdcD)
            ECE: Z4467(tdcD)
            ECS: ECs3995
            ECC: c4530(tdcD)
            ECI: UTI89_C3550(tdcD)
            ECV: APECO1_3309(tdcD)
            ECW: EcE24377A_3589(tdcD)
            ECX: EcHS_A3303(tdcD)
            STY: STY2262 STY3424(tdcD)
            STT: t0817 t3162(tdcD)
            SPT: SPA0814(pduW) SPA3111(tdcD)
            SEC: SC2066(pduW) SC3188(tdcD)
            STM: STM2057(pduW) STM3242(tdcD)
            SFL: SF3155(tdcD)
            SFX: S3367(tdcD)
            SFV: SFV_3156(tdcD)
            SSN: SSON_3272(tdcD)
            SBO: SBO_2980(tdcD)
            SDY: SDY_3307(tdcD)
STRUCTURES  PDB: 2E1Y  2E1Z  2E20  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.2.15
            ExPASy - ENZYME nomenclature database: 2.7.2.15
            ExplorEnz - The Enzyme Database: 2.7.2.15
            ERGO genome analysis and discovery system: 2.7.2.15
            BRENDA, the Enzyme Database: 2.7.2.15
///
ENTRY       EC 2.7.2.-                  Enzyme
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a carboxy group as acceptor
REACTION    (1) 2-Phospho-D-glycerate + ATP <=> 2,3-Bisphospho-D-glycerate + ADP
            [RN:R02664];
            (2) N2-Acetyl-L-aminoadipate + ATP <=>
            N2-Acetyl-L-aminoadipyl-delta-phosphate + ADP [RN:R06842]
SUBSTRATE   2-Phospho-D-glycerate [CPD:C00631];
            ATP [CPD:C00002];
            N2-Acetyl-L-aminoadipate [CPD:C12986]
PRODUCT     2,3-Bisphospho-D-glycerate [CPD:C01159];
            ADP [CPD:C00008];
            N2-Acetyl-L-aminoadipyl-delta-phosphate [CPD:C12987]
///
ENTRY       EC 2.7.3.1                  Enzyme
NAME        guanidinoacetate kinase;
            glycocyamine kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a nitrogenous group as acceptor
SYSNAME     ATP:guanidinoacetate N-phosphotransferase
REACTION    ATP + guanidinoacetate = ADP + phosphoguanidinoacetate [RN:R02575]
ALL_REAC    R02575
SUBSTRATE   ATP [CPD:C00002];
            guanidinoacetate [CPD:C00581]
PRODUCT     ADP [CPD:C00008];
            phosphoguanidinoacetate [CPD:C03166]
REFERENCE   1  [PMID:13403909]
  AUTHORS   HOBSON GE, REES KR.
  TITLE     The annelid phosphokinases.
  JOURNAL   Biochem. J. 65 (1957) 305-7.
  ORGANISM  Arenicola marina, Nereis diversicolor, Nereis fucata, Nephthys caeca
REFERENCE   2  [PMID:5637051]
  AUTHORS   Pradel LA, Kassab R, Conlay C, Nguyen Van Thoai.
  TITLE     [Properties and amino acid composition of purified ATP:
            guanidinoacetate phosphotransferase]
  JOURNAL   Biochim. Biophys. Acta. 154 (1968) 305-14.
  ORGANISM  Nephthys caeca
REFERENCE   3
  AUTHORS   Pradel, L.-A., Kassab, R. and Thoai, N.V.
  TITLE     Sur l'acide adenosine-triphosphorique:guanidoacetate
            phosphotransferase.
  JOURNAL   Biochim. Biophys. Acta 81 (1964) 86-95.
  ORGANISM  Nephthys caeca
REFERENCE   4
  AUTHORS   Thoai, N.V.
  TITLE     Sur la taurocyamine et la glycocyamine phosphokinase.
  JOURNAL   Bull. Soc. Chim. Biol. 39 (1957) 197-208.
  ORGANISM  Nereis diversicolor
PATHWAY     PATH: map00330  Arginine and proline metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.3.1
            ExPASy - ENZYME nomenclature database: 2.7.3.1
            ExplorEnz - The Enzyme Database: 2.7.3.1
            ERGO genome analysis and discovery system: 2.7.3.1
            BRENDA, the Enzyme Database: 2.7.3.1
            CAS: 9026-60-2
///
ENTRY       EC 2.7.3.2                  Enzyme
NAME        creatine kinase;
            ATP:creatine phosphotransferase;
            CK;
            MM-CK;
            MB-CK;
            BB-CK;
            creatine phosphokinase;
            creatine phosphotransferase;
            phosphocreatine kinase;
            adenosine triphosphate-creatine transphosphorylase;
            Mi-CK;
            CK-BB;
            CK-MM;
            CK-MB;
            CKMiMi;
            MiMi-CK
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a nitrogenous group as acceptor
SYSNAME     ATP:creatine N-phosphotransferase
REACTION    ATP + creatine = ADP + phosphocreatine [RN:R01881]
ALL_REAC    R01881
SUBSTRATE   ATP [CPD:C00002];
            creatine [CPD:C00300]
PRODUCT     ADP [CPD:C00008];
            phosphocreatine [CPD:C02305]
COMMENT     N-Ethylglycocyamine can also act as acceptor.
REFERENCE   1
  AUTHORS   Ennor, A.H., Rosenberg, H. and Armstrong, M.D.
  TITLE     Specificity of creatine phosphokinase.
  JOURNAL   Nature 175 (1955) 120.
REFERENCE   2  [PMID:5750168]
  AUTHORS   Keutel HJ, Jacobs HK, Okabe K, Yue RH, Kuby SA.
  TITLE     Studies on adenosine triphosphate transphosphorylases. VII.
            Isolation of the crystalline adenosine triphosphate--creatine
            transphosphorylase from calf brain.
  JOURNAL   Biochemistry. 7 (1968) 4283-90.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:13192073]
  AUTHORS   KUBY SA, NODA L, LARDY HA.
  TITLE     Adenosinetriphosphate-creatine transphosphorylase. I. Isolation of
            the crystalline enzyme from rabbit muscle.
  JOURNAL   J. Biol. Chem. 209 (1954) 191-201.
  ORGANISM  rabbit
REFERENCE   4
  AUTHORS   Kuby, S.A. and Noltmann, E.A.
  TITLE     ATP-creatine transphosphorylase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 6, Academic Press, New York, 1962, p. 515-603.
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K00933  creatine kinase
GENES       HSA: 1152(CKB) 1158(CKM) 1159(CKMT1B) 1160(CKMT2) 548596(CKMT1A)
            PTR: 461770(CKMT2)
            MCC: 711434(CKMT2)
            MMU: 12709(Ckb) 12715(Ckm) 12716(Ckmt1) 329504(Lcmt2) 76722(Ckmt2)
            RNO: 24264(Ckb) 24265(Ckm)
            CFA: 476435(CKM) 478277(LOC478277) 479163(CKMT2) 482930(LOC482930)
            BTA: 281692(CKMT1) 286822(CKM)
            GGA: 374002(CKMT1A) 396248(CKB) 396507(LOC396507) 396508(CKMT2)
            XLA: 379216(MGC53985) 379765(ckm) 380055(ckb) 380155(ckmt1)
            XTR: 395000(ckmt1b) 395005(ckm)
            DRE: 140744(ckb) 30095(ckm) 393670(ckmt2)
            SPU: 373287(TCK) 589605(LOC589605) 758425(LOC758425)
                 762696(LOC762696)
            DPS: DP1035
STRUCTURES  PDB: 1CRK  1G0W  1I0E  1QH4  1QK1  1U6R  1VRP  2CRK  2GL6  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.3.2
            ExPASy - ENZYME nomenclature database: 2.7.3.2
            ExplorEnz - The Enzyme Database: 2.7.3.2
            ERGO genome analysis and discovery system: 2.7.3.2
            BRENDA, the Enzyme Database: 2.7.3.2
            CAS: 9001-15-4
///
ENTRY       EC 2.7.3.3                  Enzyme
NAME        arginine kinase;
            arginine phosphokinase;
            adenosine 5'-triphosphate: L-arginine phosphotransferase;
            adenosine 5'-triphosphate-arginine phosphotransferase;
            ATP:L-arginine N-phosphotransferasel ATP:L-arginine
            omega-N-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a nitrogenous group as acceptor
SYSNAME     ATP:L-arginine Nomega-phosphotransferase
REACTION    ATP + L-arginine = ADP + Nomega-phospho-L-arginine [RN:R00554]
ALL_REAC    R00554
SUBSTRATE   ATP [CPD:C00002];
            L-arginine [CPD:C00062]
PRODUCT     ADP [CPD:C00008];
            Nomega-phospho-L-arginine
REFERENCE   1  [PMID:13339436]
  AUTHORS   ELODI P, SZORENYI E.
  TITLE     Properties of crystalline arginine-phosphoferase isolated from
            Crustacean muscle.
  JOURNAL   Acta. Physiol. Hung. 9 (1956) 367-79.
REFERENCE   2  [PMID:13403885]
  AUTHORS   MORRISON JF, GRIFFITHS DE, ENNOR AH.
  TITLE     The purification and properties of arginine phosphokinase.
  JOURNAL   Biochem. J. 65 (1957) 143-53.
  ORGANISM  Jasus verreauxi
REFERENCE   3  [PMID:16519065]
  AUTHORS   Urbancsek J, Fancsovits P, Akos M, Tothne Gilan Z, Hauzman E, Papp
            Z.
  TITLE     [In vitro fertilization at our department. A decade's work in
            figures and facts (1994-2003)]
  JOURNAL   Orv. Hetil. 147 (2006) 7-14.
REFERENCE   4  [PMID:14340045]
  AUTHORS   VIRDEN R, WATTS DC, BALDWIN E.
  TITLE     ADENOSINE 5'-TRIPHOSPHATE-ARGININE PHOSPHOTRANSFERASE FROM LOBSTER
            MUSCLE: PURIFICATION AND PROPERTIES.
  JOURNAL   Biochem. J. 94 (1965) 536-44.
  ORGANISM  lobster
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K00934  arginine kinase
GENES       DME: Dmel_CG32031(Argk) Dmel_CG5144
            CEL: F44G3.2 F46H5.3 W10C8.5 ZC434.8
            TET: TTHERM_00151390
            TBR: Tb09.160.4560 Tb09.160.4570 Tb09.160.4590
            TCR: 482369.29 507241.30
            SUN: SUN_1812
            BCZ: BCZK0076(karG)
            BTK: BT9727_0077(karG)
            BTL: BALH_0080(karG)
            BPU: BPUM_0070
            CTC: CTC02634
            CTA: CTA_0733(karG)
STRUCTURES  PDB: 1BG0  1M15  1M80  1P50  1P52  1RL9  1SD0  2J1Q  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.3.3
            ExPASy - ENZYME nomenclature database: 2.7.3.3
            ExplorEnz - The Enzyme Database: 2.7.3.3
            ERGO genome analysis and discovery system: 2.7.3.3
            BRENDA, the Enzyme Database: 2.7.3.3
            CAS: 9026-70-4
///
ENTRY       EC 2.7.3.4                  Enzyme
NAME        taurocyamine kinase;
            taurocyamine phosphotransferase;
            ATP:taurocyamine phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a nitrogenous group as acceptor
SYSNAME     ATP:taurocyamine N-phosphotransferase
REACTION    ATP + taurocyamine = ADP + N-phosphotaurocyamine [RN:R03785]
ALL_REAC    R03785
SUBSTRATE   ATP [CPD:C00002];
            taurocyamine [CPD:C01959]
PRODUCT     ADP [CPD:C00008];
            N-phosphotaurocyamine [CPD:C03149]
REFERENCE   1  [PMID:13403909]
  AUTHORS   HOBSON GE, REES KR.
  TITLE     The annelid phosphokinases.
  JOURNAL   Biochem. J. 65 (1957) 305-7.
  ORGANISM  Arenicola marina, Nereis diversicolor, Myxicola infundindum
REFERENCE   2  [PMID:5840960]
  AUTHORS   Kassab R, Pradel LA, Nguyen Van Thoai.
  TITLE     [ATP:taurocyamine and ATP:lombricine phosphotransferases.
            Purification and study of SH groups]
  JOURNAL   Biochim. Biophys. Acta. 99 (1965) 397-405.
REFERENCE   3
  AUTHORS   Thoai, N.V.
  TITLE     Sur la taurocyamine et la glycocyamine phosphokinase.
  JOURNAL   Bull. Soc. Chim. Biol. 39 (1957) 197-208.
  ORGANISM  Arenicola marina
REFERENCE   4
  AUTHORS   Thoai, N.V., Robin, Y. and Pradel, L.-A.
  TITLE     Hypotaurocyamine phosphokinase comparison avec la taurocyamine
            phosphokinase.
  JOURNAL   Biochim. Biophys. Acta 73 (1963) 437-444.
  ORGANISM  Arenicola marina
PATHWAY     PATH: map00430  Taurine and hypotaurine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.3.4
            ExPASy - ENZYME nomenclature database: 2.7.3.4
            ExplorEnz - The Enzyme Database: 2.7.3.4
            ERGO genome analysis and discovery system: 2.7.3.4
            BRENDA, the Enzyme Database: 2.7.3.4
            CAS: 9026-72-6
///
ENTRY       EC 2.7.3.5                  Enzyme
NAME        lombricine kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a nitrogenous group as acceptor
SYSNAME     ATP:lombricine N-phosphotransferase
REACTION    ATP + lombricine = ADP + N-phospholombricine [RN:R06976]
ALL_REAC    R06976;
            (other) R03691
SUBSTRATE   ATP [CPD:C00002];
            lombricine [CPD:C14177]
PRODUCT     ADP [CPD:C00008];
            N-phospholombricine [CPD:C14178]
COMMENT     Also acts on methylated lombricines such as thalassemine; the
            specificity varies with the source species.
REFERENCE   1  [PMID:5832288]
  AUTHORS   Gaffney TJ, Rosenberg H, Ennor AH.
  TITLE     The purification and properties of adenosine triphosphate-lombricine
            phosphotransferase.
  JOURNAL   Biochem. J. 90 (1964) 170-6.
  ORGANISM  Lumbricus terrestris
REFERENCE   2  [PMID:5840960]
  AUTHORS   Kassab R, Pradel LA, Nguyen Van Thoai.
  TITLE     [ATP:taurocyamine and ATP:lombricine phosphotransferases.
            Purification and study of SH groups]
  JOURNAL   Biochim. Biophys. Acta. 99 (1965) 397-405.
REFERENCE   3
  AUTHORS   Pant, R.
  TITLE     Isolation of lombricine and its enzymatic phosphorylation.
  JOURNAL   Biochem. J. 73 (1959) 30-33.
  ORGANISM  Lumbricus terrestris
REFERENCE   4  [PMID:5079888]
  AUTHORS   van Thoai N, Robin Y, Guillou Y.
  TITLE     A new phosphagen, N'-phosphorylguanidinoethylphospho-O-(
            -N,N-dimethyl)serine (phosphothalassemine).
  JOURNAL   Biochemistry. 11 (1972) 3890-5.
  ORGANISM  Lumbricus terrestris
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.3.5
            ExPASy - ENZYME nomenclature database: 2.7.3.5
            ExplorEnz - The Enzyme Database: 2.7.3.5
            ERGO genome analysis and discovery system: 2.7.3.5
            BRENDA, the Enzyme Database: 2.7.3.5
            CAS: 9026-53-3
///
ENTRY       EC 2.7.3.6                  Enzyme
NAME        hypotaurocyamine kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a nitrogenous group as acceptor
SYSNAME     ATP:hypotaurocyamine N-phosphotransferase
REACTION    ATP + hypotaurocyamine = ADP + Nomega-phosphohypotaurocyamine
            [RN:R03939]
ALL_REAC    R03939
SUBSTRATE   ATP [CPD:C00002];
            hypotaurocyamine [CPD:C02419]
PRODUCT     ADP [CPD:C00008];
            Nomega-phosphohypotaurocyamine
COMMENT     Also acts, more slowly, on taurocyamine.
REFERENCE   1
  AUTHORS   Thoai, N.V., Robin, Y. and Pradel, L.-A.
  TITLE     Hypotaurocyamine phosphokinase comparison avec la taurocyamine
            phosphokinase.
  JOURNAL   Biochim. Biophys. Acta 73 (1963) 437-444.
  ORGANISM  Phascolosoma vulgare
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.3.6
            ExPASy - ENZYME nomenclature database: 2.7.3.6
            ExplorEnz - The Enzyme Database: 2.7.3.6
            ERGO genome analysis and discovery system: 2.7.3.6
            BRENDA, the Enzyme Database: 2.7.3.6
            CAS: 9026-57-7
///
ENTRY       EC 2.7.3.7                  Enzyme
NAME        opheline kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a nitrogenous group as acceptor
SYSNAME     ATP:guanidinoethyl-methyl-phosphate phosphotransferase
REACTION    ATP + guanidinoethyl methyl phosphate = ADP +
            N'-phosphoguanidinoethyl methylphosphate [RN:R04388]
ALL_REAC    R04388
SUBSTRATE   ATP [CPD:C00002];
            guanidinoethyl methyl phosphate [CPD:C04071]
PRODUCT     ADP [CPD:C00008];
            N'-phosphoguanidinoethyl methylphosphate
COMMENT     Has a little activity on taurocyamine, lombricine and
            phosphotaurocyamine.
REFERENCE   1
  AUTHORS   Thoai, N.V., di Jeso, F., Robin, Y. and der Terrossian, E.
  TITLE     Sur la nouvelle acide adenosine 5'-triphosphorique:guanidine
            phosphotransferase, l'opheline kinase.
  JOURNAL   Biochim. Biophys. Acta 113 (1966) 542-550.
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.3.7
            ExPASy - ENZYME nomenclature database: 2.7.3.7
            ExplorEnz - The Enzyme Database: 2.7.3.7
            ERGO genome analysis and discovery system: 2.7.3.7
            BRENDA, the Enzyme Database: 2.7.3.7
            CAS: 37278-15-2
///
ENTRY       EC 2.7.3.8                  Enzyme
NAME        ammonia kinase;
            phosphoramidate-adenosine diphosphate phosphotransferase;
            phosphoramidate-ADP-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a nitrogenous group as acceptor
SYSNAME     ATP:ammonia phosphotransferase
REACTION    ATP + NH3 = ADP + phosphoramide [RN:R00141]
ALL_REAC    R00141
SUBSTRATE   ATP [CPD:C00002];
            NH3 [CPD:C00014]
PRODUCT     ADP [CPD:C00008];
            phosphoramide [CPD:C02058]
COMMENT     Has a wide specificity. In the reverse direction, N-phosphoglycine
            and N-phosphohistidine can also act as phosphate donors, and ADP,
            dADP, GDP, CDP, dTDP, dCDP, IDP and UDP can act as phosphate
            acceptors (in decreasing order of activity).
REFERENCE   1  [PMID:5647264]
  AUTHORS   Dowler MJ, Nakada HI.
  TITLE     Yeast phosphoramidate-adenosine diphosphate phosphotransferase.
  JOURNAL   J. Biol. Chem. 243 (1968) 1434-40.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.3.8
            ExPASy - ENZYME nomenclature database: 2.7.3.8
            ExplorEnz - The Enzyme Database: 2.7.3.8
            ERGO genome analysis and discovery system: 2.7.3.8
            BRENDA, the Enzyme Database: 2.7.3.8
            CAS: 37278-16-3
///
ENTRY       EC 2.7.3.9                  Enzyme
NAME        phosphoenolpyruvate---protein phosphotransferase;
            phosphoenolpyruvate sugar phosphotransferase enzyme I;
            phosphopyruvate-protein factor phosphotransferase;
            phosphopyruvate-protein phosphotransferase;
            sugar-PEP phosphotransferase enzyme I;
            phosphoenolpyruvate:protein-L-histidine N-pros-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a nitrogenous group as acceptor
SYSNAME     phosphoenolpyruvate:protein-L-histidine Npi-phosphotransferase
REACTION    phosphoenolpyruvate + protein histidine = pyruvate + protein
            Npi-phospho-L-histidine [RN:R02628]
ALL_REAC    R02628
SUBSTRATE   phosphoenolpyruvate [CPD:C00074];
            protein histidine [CPD:C00615]
PRODUCT     pyruvate [CPD:C00022];
            protein Npi-phospho-L-histidine
COMMENT     Enzyme I of the phosphotransferase system (cf. EC 2.7.1.69
            protein-Npi-phosphohistidine---sugar phosphotransferase). Acts only
            on histidine residues in specific phosphocarrier proteins of low
            molecular mass (9.5 kDa) involved in bacterial sugar transport. A
            similar reaction, where the protein is the enzyme EC 2.7.9.2
            pyruvate, water dikinase, is part of the mechanism of that enzyme.
REFERENCE   1  [PMID:187249]
  AUTHORS   .
  TITLE     The bacterial phosphoenolpyruvate: sugar phosphotransferase system.
  JOURNAL   Biochim. Biophys. Acta. 457 (1976) 213-57.
  ORGANISM  Escherichia coli [GN:eco], Salmonella typhimurium, Staphylococcus
            aureus
PATHWAY     PATH: map02060  Phosphotransferase system (PTS)
ORTHOLOGY   KO: K00935  
            KO: K02766  phosphotransferase system, enzyme I
            KO: K08483  phosphotransferase system, enzyme I, PtsI
            KO: K08484  phosphotransferase system, enzyme I, PtsP
GENES       DME: Dmel_CG2615(ik2)
            ECO: b2383(ypdD) b2416(ptsI) b2829(ptsP) b3947(ptsA)
            ECJ: JW2380(ypdD) JW2409(ptsI) JW2797(ptsP) JW5555(ptsA)
            ECE: Z3648 Z3682(ptsI) Z4146(ptsP) Z5502(ptsA)
            ECS: ECs3263 ECs3288 ECs3686 ECs4877
            ECC: c2922(ypdD) c2951(ptsI) c3424(ptsP) c4906(ptsA)
            ECI: UTI89_C2715 UTI89_C2750(ptsI) UTI89_C3231(ptsP)
                 UTI89_C4538(ptsA) UTI89_C5022(pptE)
            ECP: ECP_2409 ECP_2440 ECP_2842 ECP_4161
            ECV: APECO1_2105(pptE) APECO1_2519(ptsA) APECO1_3676(ptsP)
                 APECO1_4129(ptsI) APECO1_4154(ypdD)
            ECW: EcE24377A_2673(fryA) EcE24377A_2703(ptsI)
                 EcE24377A_3149(ptsP) EcE24377A_4487(ptsA)
            ECX: EcHS_A2520(fryA) EcHS_A2551 EcHS_A2975 EcHS_A4182
            STY: STY2668 STY3144(ptsP)
            STT: t0425 t2912(ptsP)
            SPT: SPA0433(ptsI) SPA2868(ptsP)
            SEC: SC2430(ptsI) SC2942(ptsP) SC4002(ptsA)
            STM: STM2432(ptsI) STM3003(ptsP) STM4110(ptsA)
            YPE: YPO0405 YPO0785(ptsP) YPO2994(ptsI)
            YPK: y1487(ptsI) y3173(ptsP) y3776(ptsA)
            YPM: YP_2619(ptsI) YP_2873(ptsP) YP_3776(ptsA)
            YPA: YPA_0483 YPA_2184 YPA_3880
            YPN: YPN_0275 YPN_1388 YPN_2990
            YPS: YPTB0545(pstA) YPTB2716(ptsI) YPTB3035(ptsP)
            YPI: YpsIP31758_0982(ptsP) YpsIP31758_1316(ptsI)
            SFL: SF2449(ypdD) SF2471(ptsI) SF2839(ptsP)
            SFX: S2588 S2617(ptsI) S3037(ptsP)
            SFV: SFV_2441 SFV_2468(ptsI) SFV_2907(ptsP)
            SSN: SSON_2505(ptsI) SSON_2986(ptsP) SSON_4121(ptsA)
            SBO: SBO_2409 SBO_2440(ptsI) SBO_2721(ptsP) SBO_3967(ptsA)
            SDY: SDY_2613(ptsI) SDY_3046(ptsP) SDY_3782(ptsA)
            ECA: ECA0892(ptsI) ECA0986(ptsP)
            PLU: plu0621(ptsP) plu1393(ptsI)
            BUC: BU064(ptsI)
            BAS: BUsg061(ptsI)
            BAB: bbp060(ptsI)
            SGL: SG1702 SG1979
            SPE: Spro_4270
            BFL: Bfl510(ptsI)
            BPN: BPEN_527(ptsI)
            HIN: HI1712(ptsI)
            HIT: NTHI2021(ptsI)
            HIP: CGSHiEE_03470
            HIQ: CGSHiGG_02315
            HDU: HD0228(ptsI)
            HSO: HS_1097(ptsI)
            PMU: PM0897(ptsI)
            MSU: MS1509(ptsA)
            APL: APL_1323(ptsI)
            XFA: XF1402
            XFT: PD0631(ptsA)
            XCC: XCC2370(fruB) XCC2809(ptsI)
            XCB: XC_1304 XC_1744
            XCV: XCV2679(fruB) XCV3125(ptsI)
            XAC: XAC2501(fruB) XAC2979(ptsI)
            XOO: XOO1277(ptsI) XOO2810(fruB)
            XOM: XOO_1175(XOO1175) XOO_2650(XOO2650)
            VCH: VC0672 VC0965
            VCO: VC0395_A0204(ptsP) VC0395_A0487(ptsI)
            VVU: VV1_0211 VV1_0519
            VVY: VV0676 VV0977
            VPA: VP0366 VP0521 VP0794
            VFI: VF0457 VF1895 VF1896
            PPR: PBPRA0578(ptsP) PBPRA0862 PBPRB0217
            PAE: PA0337(ptsP) PA3562 PA3760
            PAU: PA14_04410(ptsP)
            PPU: PP_0793(fruB) PP_5145(ptsP)
            PST: PSPTO_0954 PSPTO_5284(ptsP)
            PSB: Psyr_0821 Psyr_4842
            PSP: PSPPH_0847 PSPPH_4874(ptsP)
            PFL: PFL_0859 PFL_1079 PFL_4931(ptsI) PFL_5899(ptsP)
            PFO: Pfl_0793 Pfl_1004 Pfl_5377(ptsP)
            PEN: PSEEN0932 PSEEN4382 PSEEN5238(ptsP)
            ACI: ACIAD0454(ptsP) ACIAD1990(fruB)
            SON: SO_1332(ptsP) SO_2237(ptsI)
            SDN: Sden_1817 Sden_2781
            SFR: Sfri_1768 Sfri_2944
            SHE: Shewmr4_1764 Shewmr4_2864
            SHM: Shewmr7_1842 Shewmr7_2946
            SHN: Shewana3_2257 Shewana3_3042
            ILO: IL0504(ptsP)
            CPS: CPS_3624(ptsP)
            PHA: PSHAa0746(ptsP)
            PAT: Patl_3845
            SDE: Sde_0348
            CBU: CBU_1550(ptsP)
            CBD: COXBU7E912_0439(ptsP)
            LPN: lpg2871(ptsP)
            LPF: lpl2784(ptsP)
            LPP: lpp2930(ptsP)
            NOC: Noc_1552 Noc_2800
            AEH: Mlg_0428 Mlg_1177
            HCH: HCH_05090(ptsP) HCH_05983
            ABO: ABO_2348(ptsP)
            AHA: AHA_0673(ptsI-1) AHA_3040(ptsI-2) AHA_3919
            DNO: DNO_0118(ptsI)
            BCI: BCI_0070(ptsI)
            NME: NMB2044
            NMA: NMA0392(ptsI)
            NMC: NMC2024(ptsI)
            NGO: NGO2038(ptsI)
            CVI: CV_0558 CV_0816 CV_0980 CV_2311(ptsA) CV_3052(fruB)
            RSO: RS05327(RSp1282) RSc0348(ptsI) RSc2861(fruB)
            REU: Reut_A0297
            REH: H16_A0326(ptsI)
            RME: Rmet_0246
            BMA: BMA3171 BMA3211(ptsI)
            BMV: BMASAVP1_A0185(ptsI)
            BML: BMA10299_A1407(ptsI)
            BMN: BMA10247_2834(ptsI)
            BXE: Bxe_A4153 Bxe_A4184
            BUR: Bcep18194_A6152 Bcep18194_A6189
            BPS: BPSL0440 BPSL0498
            BPM: BURPS1710b_0658(ptsI) BURPS1710b_0723
            BPL: BURPS1106A_0493(ptsI) BURPS1106A_0554
            BPD: BURPS668_0474(ptsI)
            BTE: BTH_I0413(ptsI) BTH_I0449 BTH_II0906
            BPE: BP1502(ptsI)
            BPA: BPP1968(ptsI)
            BBR: BB2155(ptsI)
            RFR: Rfer_0603
            POL: Bpro_0299
            MPT: Mpe_A0326
            HAR: HEAR0149(phbI)
            MMS: mma_0175
            NEU: NE2185(ptsI)
            NET: Neut_0529
            NMU: Nmul_A0220
            EBA: ebA2795(ptsI)
            AZO: azo1538(ptsP) azo3782(ptsI)
            DAR: Daro_4084
            TBD: Tbd_2414
            MFA: Mfla_0148
            SUN: SUN_2238
            GSU: GSU1165(ptsP) GSU1881(ptsI)
            GME: Gmet_1289 Gmet_2404
            PCA: Pcar_1929 Pcar_2313
            DVU: DVU0829(ptsI) DVU0981
            DDE: Dde_1089 Dde_1180
            ADE: Adeh_0153
            MXA: MXAN_6530(ptsI)
            SAT: SYN_01729
            SFU: Sfum_0772
            MLO: mll3436 mll3609 mll5291
            MES: Meso_3000
            SME: SMc02437(ptsP)
            ATU: Atu4173(ptsI)
            ATC: AGR_L_1355
            RET: RHE_CH03757(ptsP)
            RLE: RL2904(ptsI) RL4283(ptsP)
            BME: BMEI0190
            BMF: BAB1_1873(ptsP)
            BMS: BR1870(ptsP)
            BMB: BruAb1_1849(ptsP)
            BOV: BOV_1801(ptsP)
            OAN: Oant_4112
            BJA: blr0217(ptsP) blr3575(ptsI)
            BRA: BRADO0573(ptsP) BRADO4611(ptsI)
            BBT: BBta_7603(ptsP)
            RPA: RPA0605(ptsP)
            RPB: RPB_0076(ptsP)
            RPC: RPC_0513
            RPD: RPD_0098
            RPE: RPE_0159
            NWI: Nwi_0378
            BHE: BH01410(fruB)
            BQU: BQ01340(fruB)
            CCR: CC_0448 CC_0537 CC_0849
            SIL: SPO3034
            SIT: TM1040_1933
            RSP: RSP_1786(fruB) RSP_1850(ptsI)
            JAN: Jann_3205
            RDE: RD1_2158(ptsP)
            MMR: Mmar10_2258
            HNE: HNE_0619(ptsP)
            ZMO: ZMO1651(ptsP)
            NAR: Saro_0080 Saro_2413
            SAL: Sala_2149
            ELI: ELI_00500
            GOX: GOX0812
            GBE: GbCGDNIH1_0398 GbCGDNIH1_0412 GbCGDNIH1_0602
            RRU: Rru_A0745 Rru_A1972 Rru_A3445
            MAG: amb1614 amb4393
            BSU: BG10201(ptsI)
            BHA: BH3073(ptsI)
            BAN: BA4267(ptsI)
            BAR: GBAA4267(ptsI)
            BAA: BA_4726
            BAT: BAS3958
            BCE: BC4048
            BCA: BCE_4115(ptsI)
            BCZ: BCZK3804(ptsI)
            BCY: Bcer98_2747
            BTK: BT9727_3789(ptsI)
            BTL: BALH_3664(ptsI)
            BLI: BL03569(ptsI)
            BLD: BLi01600(ptsI)
            BCL: ABC2658(ptsI)
            BAY: RBAM_013680
            BPU: BPUM_1281
            OIH: OB2432(ptsI)
            GKA: GK0996(ptsI)
            SAU: SA0935(ptsI)
            SAV: SAV1084(ptsI)
            SAM: MW0966(ptsI)
            SAR: SAR1057(ptsI)
            SAS: SAS1019
            SAC: SACOL1092(ptsI)
            SAB: SAB0950(ptsI)
            SAA: SAUSA300_0984(ptsI)
            SAO: SAOUHSC_01029
            SAJ: SaurJH9_1144
            SAH: SaurJH1_1166
            SEP: SE0782
            SER: SERP0670(ptsI)
            SHA: SH1874(ptsI)
            SSP: SSP1707
            LMO: lmo1003
            LMF: LMOf2365_1024(ptsI)
            LIN: lin1002
            LWE: lwe0987(ptsI)
            LLA: L120628(ptsI)
            LLC: LACR_0104
            LLM: llmg_0127(ptsI)
            SPY: SPy_1372(pstI)
            SPZ: M5005_Spy_1120(pstI)
            SPM: spyM18_1384(pts1)
            SPG: SpyM3_1046(ptsI)
            SPS: SPs0815
            SPH: MGAS10270_Spy1190(pstI)
            SPI: MGAS10750_Spy1222(pstI)
            SPJ: MGAS2096_Spy1185(pstI)
            SPK: MGAS9429_Spy1167(pstI)
            SPF: SpyM50740(pstI)
            SPA: M6_Spy1094
            SPB: M28_Spy1113(pstI)
            SPN: SP_1176
            SPR: spr1062(ptsI)
            SPD: SPD_1039(ptsI)
            SAG: SAG0822(ptsI)
            SAN: gbs0840(ptsI)
            SAK: SAK_0946(ptsI)
            SMU: SMU.675
            STC: str1264(ptsI)
            STL: stu1264(ptsI)
            STE: STER_1242
            SSA: SSA_0773(ptsI)
            SSU: SSU05_1200
            SSV: SSU98_1214
            SGO: SGO_1555(ptsI)
            LPL: lp_1274(ptsI)
            LJO: LJ0817
            LAC: LBA0640(ptsI)
            LSA: LSA1462(ptsI)
            LSL: LSL_0389(ptsI)
            LDB: Ldb0577(ptsI)
            LBU: LBUL_0513
            LBR: LVIS_1551
            LCA: LSEI_1759
            LRE: Lreu_0457
            EFA: EF0710(ptsI)
            OOE: OEOE_0647
            CAC: CAC3087
            CPE: CPE2357
            CPF: CPF_2666(ptsI)
            CPR: CPR_2352(ptsI)
            CTC: CTC01771
            CNO: NT01CX_0334(ptsI) NT01CX_1155(ptsI)
            CDF: CD2755(ptsI)
            CBO: CBO3438(ptsI)
            CBA: CLB_3494(ptsI)
            CBH: CLC_3382(ptsI)
            CBF: CLI_3620(ptsI)
            CKL: CKL_0307(pts1)
            DRM: Dred_0330
            CSC: Csac_2437
            TTE: TTE2334(ptsA)
            MTA: Moth_0016
            MGE: MG_429(ptsI)
            MPN: MPN627(ptsI)
            MPU: MYPU_6020(ptsI)
            MPE: MYPE5450
            MGA: MGA_0763(ptsA)
            MMY: MSC_0273(ptsI)
            MMO: MMOB0610(ptsI)
            MHY: mhp470(ptsI)
            MHJ: MHJ_0469(ptsI)
            MHP: MHP7448_0472(ptsI)
            MSY: MS53_0523(ptsI)
            MCP: MCAP_0233(ptsI)
            MFL: Mfl519
            MSM: MSMEG_0088(ptsI) MSMEG_2121
            MMC: Mmcs_0083
            CGL: NCgl1858(cgl1933)
            CGB: cg2117(ptsI)
            CEF: CE1826(ptsI)
            CDI: DIP1428(ptsI)
            NFA: nfa28570(ptsA)
            RHA: RHA1_ro01549 RHA1_ro06785
            SCO: SCO1391(SC1A8A.11)
            SMA: SAV6974(ptsP)
            LXX: Lxx00830(ptsI)
            CMI: CMM_0968(ptsA) CMM_2592
            AAU: AAur_3861(ptsI)
            PAC: PPA0351
            TFU: Tfu_2765
            SEN: SACE_2271(ptsA) SACE_6246 SACE_7368(ptsA)
            BLO: BL0411(ptsI)
            BAD: BAD_0166(ptsI)
            RXY: Rxyl_1734
            FNU: FN1793
            RBA: RB2992 RB8591(ptsI)
            CTR: CT336(ptsI)
            CTA: CTA_0364(ptsI)
            CMU: TC0613
            CPN: CPn0038(ptsI)
            CPA: CP0737
            CPJ: CPj0038(ptsI)
            CPT: CpB0042
            CCA: CCA00329(ptsI)
            CAB: CAB325
            CFE: CF0673(ptsI)
            PCU: pc0476(ptsI)
            BBU: BB0558(ptsI)
            BGA: BG0568(ptsI)
            BAF: BAPKO_0587(ptsI)
            TDE: TDE0084(ptsI)
            LIL: LA2307(ptsI)
            LIC: LIC11632(ptsI)
            LBJ: LBJ_1314(ptsA)
            LBL: LBL_1539(ptsA)
            SRU: SRU_1872(ptsI)
            CTE: CT0204(ptsI)
            CCH: Cag_1607
            PLT: Plut_1914
            DRA: DR_B0075(fruB)
            DGE: Dgeo_2622
            HMA: pNG7391(ptsI)
            HWA: HQ2709A(ptsI)
STRUCTURES  PDB: 1EZA  1EZB  1EZC  1EZD  1ZYM  2EZA  2EZB  2EZC  2HRO  2HWG  
                 3EZA  3EZB  3EZE  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.3.9
            ExPASy - ENZYME nomenclature database: 2.7.3.9
            ExplorEnz - The Enzyme Database: 2.7.3.9
            ERGO genome analysis and discovery system: 2.7.3.9
            BRENDA, the Enzyme Database: 2.7.3.9
            CAS: 37278-17-4
///
ENTRY       EC 2.7.3.10                 Enzyme
NAME        agmatine kinase;
            phosphagen phosphokinase;
            ATP:agmatine 4-N-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a nitrogenous group as acceptor
SYSNAME     ATP:agmatine N4-phosphotransferase
REACTION    ATP + agmatine = ADP + N4-phosphoagmatine [RN:R01417]
ALL_REAC    R01417
SUBSTRATE   ATP [CPD:C00002];
            agmatine [CPD:C00179]
PRODUCT     ADP [CPD:C00008];
            N4-phosphoagmatine [CPD:C02726]
COMMENT     L-Arginine can act as acceptor, but more slowly.
REFERENCE   1
  AUTHORS   Piccinni, E. and Coppellotti, O.
  TITLE     Phosphagens in protozoa. II. Presence of phosphagen kinase in
            Ochramonas danica.
  JOURNAL   Comp. Biochem. Physiol. 62B (1979) 287-289.
  ORGANISM  Ochramonas danica
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.3.10
            ExPASy - ENZYME nomenclature database: 2.7.3.10
            ExplorEnz - The Enzyme Database: 2.7.3.10
            ERGO genome analysis and discovery system: 2.7.3.10
            BRENDA, the Enzyme Database: 2.7.3.10
            CAS: 71061-39-7
///
ENTRY       EC 2.7.3.11       Obsolete  Enzyme
NAME        Transferred to 2.7.13.1
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a nitrogenous group as acceptor
COMMENT     Transferred entry: now EC 2.7.13.1 protein-histidine pros-kinase (EC
            2.7.3.11 created 1989, deleted 2005)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.3.11
            ExPASy - ENZYME nomenclature database: 2.7.3.11
            ExplorEnz - The Enzyme Database: 2.7.3.11
            ERGO genome analysis and discovery system: 2.7.3.11
            BRENDA, the Enzyme Database: 2.7.3.11
///
ENTRY       EC 2.7.3.12       Obsolete  Enzyme
NAME        Transferred to 2.7.13.2
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a nitrogenous group as acceptor
COMMENT     Transferred entry: now EC 2.7.13.2 protein-histidine tele-kinase (EC
            2.7.3.12 created 1989, deleted 2005)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.3.12
            ExPASy - ENZYME nomenclature database: 2.7.3.12
            ExplorEnz - The Enzyme Database: 2.7.3.12
            ERGO genome analysis and discovery system: 2.7.3.12
            BRENDA, the Enzyme Database: 2.7.3.12
///
ENTRY       EC 2.7.4.1                  Enzyme
NAME        polyphosphate kinase;
            polyphosphoric acid kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:polyphosphate phosphotransferase
REACTION    ATP + (phosphate)n = ADP + (phosphate)n+1 [RN:R02184]
ALL_REAC    R02184 > R00136
SUBSTRATE   ATP [CPD:C00002];
            (phosphate)n [CPD:C00404]
PRODUCT     ADP [CPD:C00008];
            (phosphate)n+1 [CPD:C00404]
REFERENCE   1  [PMID:13172250]
  AUTHORS   HOFFMANN-OSTENHOF O, KENEDY J, KECK K, GABRIEL O, SCHONFELLINGER HW.
  TITLE     [A new transphosphorylase from yeast.]
  JOURNAL   Biochim. Biophys. Acta. 14 (1954) 285.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:13315368]
  AUTHORS   KORNBERG A, KORNBERG SR, SIMMS ES.
  TITLE     Metaphosphate synthesis by an enzyme from Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 20 (1956) 215-27.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Muhammed, A.
  TITLE     Studies on biosynthesis of polymetaphosphate by an enzyme from
            Corynebacterium xerosis.
  JOURNAL   Biochim. Biophys. Acta 54 (1961) 121-132.
  ORGANISM  Corynebacterium xerosis
PATHWAY     PATH: map00190  Oxidative phosphorylation
ORTHOLOGY   KO: K00937  polyphosphate kinase
GENES       DDI: DDB_0216190(ppkA)
            ECO: b2501(ppk)
            ECJ: JW2486(ppk)
            ECE: Z3764(ppk)
            ECS: ECs3363
            ECC: c3019(ppk)
            ECI: UTI89_C2817(ppk)
            ECP: ECP_2503
            ECV: APECO1_4068(ppk)
            ECW: EcE24377A_2784(ppk)
            ECX: EcHS_A2636
            STY: STY2742(ppk)
            STT: t0356(ppk)
            SPT: SPA0366(ppk)
            SEC: SC2498(ppk)
            STM: STM2501(ppk)
            YPE: YPO2836(ppk)
            YPK: y1398(ppk)
            YPM: YP_2703(ppk)
            YPA: YPA_2273
            YPN: YPN_1301
            YPP: YPDSF_2186
            YPS: YPTB2802(ppk)
            YPI: YpsIP31758_1227(ppk)
            YEN: YE1120(ppk)
            SFL: SF2545(ppk)
            SFX: S2694(ppk)
            SFV: SFV_2546(ppk)
            SSN: SSON_2583(ppk)
            SBO: SBO_2522(ppk)
            SDY: SDY_2690(ppk)
            ECA: ECA3164(ppk)
            PLU: plu2763(ppk)
            SGL: SG1736
            ENT: Ent638_2990
            SPE: Spro_3541
            XFA: XF2591
            XFT: PD1968(ppk)
            XCC: XCC0961(ppk)
            XCB: XC_3274
            XCV: XCV1070(ppk)
            XAC: XAC1040(ppk)
            XOO: XOO3668(ppk)
            XOM: XOO_3465(XOO3465)
            VCH: VC0723
            VCO: VC0395_A0257(ppk)
            VVU: VV1_0464
            VVY: VV0727
            VPA: VP0573
            PPR: PBPRA0726
            PAE: PA5242(ppk)
            PAU: PA14_69230(ppk)
            PPU: PP_5217(ppk)
            PPF: Pput_5126
            PST: PSPTO_5250(ppk)
            PSB: Psyr_0293
            PSP: PSPPH_0280(ppk)
            PFL: PFL_5984(ppk)
            PFO: Pfl_5464
            PEN: PSEEN5336(ppk)
            PMY: Pmen_0300
            PAR: Psyc_1647(ppk)
            PCR: Pcryo_1882
            PRW: PsycPRwf_1678
            ACI: ACIAD1062(ppk) ACIAD1782(ppk)
            SAZ: Sama_2011
            SBL: Sbal_1834
            SBM: Shew185_1821
            SLO: Shew_3079
            SPC: Sputcn32_1733
            SHE: Shewmr4_2207
            SHM: Shewmr7_2284
            SHN: Shewana3_2417
            SHW: Sputw3181_2292
            ILO: IL2010(ppk)
            PAT: Patl_3322
            SDE: Sde_3654
            PIN: Ping_2414
            MAQ: Maqu_3577
            LPN: lpg0289(ppk)
            LPF: lpl0342(ppk)
            LPP: lpp0367(ppk)
            MCA: MCA1954(ppk)
            TCX: Tcr_1891
            NOC: Noc_2388
            AEH: Mlg_1870
            HHA: Hhal_0214
            HCH: HCH_01005
            CSA: Csal_0590
            ABO: ABO_2460(ppk)
            MMW: Mmwyl1_3999
            AHA: AHA_2829(ppk)
            DNO: DNO_1106(ppk)
            BCI: BCI_0074(ppk)
            VOK: COSY_0859(ppk)
            NME: NMB1900
            NMA: NMA0555(ppk)
            NMC: NMC0323(ppk)
            NGO: NGO0003
            CVI: CV_3357(ppK)
            RSO: RSc1536(ppk)
            REU: Reut_A2160 Reut_B5842
            REH: H16_A2437(ppk1) H16_B1019(ppk2)
            RME: Rmet_2178
            BMA: BMA0788(ppk)
            BMV: BMASAVP1_A1299(ppk)
            BML: BMA10299_A0570(ppk)
            BMN: BMA10247_0581(ppk) BMA10247_2378
            BXE: Bxe_A1273
            BVI: Bcep1808_1260
            BUR: Bcep18194_A4450
            BCN: Bcen_0826
            BCH: Bcen2424_1307
            BAM: Bamb_1184
            BPS: BPSL1366(ppk)
            BPM: BURPS1710b_1626(ppk)
            BPL: BURPS1106A_0185 BURPS1106A_1523(ppk)
            BPD: BURPS668_0174 BURPS668_1492(ppk)
            BTE: BTH_I2766(ppk)
            BPE: BP1072(ppk)
            BPA: BPP2072(ppk)
            BBR: BB1465(ppk)
            RFR: Rfer_2017
            POL: Bpro_2246
            PNA: Pnap_2212
            AAV: Aave_2622
            AJS: Ajs_2378
            VEI: Veis_1296
            MPT: Mpe_A3008
            HAR: HEAR1106(ppk)
            MMS: mma_2292
            NEU: NE0323
            NET: Neut_0351
            NMU: Nmul_A0382
            EBA: ebA6526(ppk)
            AZO: azo1689(ppk)
            DAR: Daro_2824
            TBD: Tbd_1085
            MFA: Mfla_0132
            HPY: HP1010
            HPA: HPAG1_0436
            HHE: HH0495(ppk)
            HAC: Hac_1114(ppk)
            WSU: WS1949
            TDN: Tmden_1578
            CJE: Cj1359(ppk)
            CJR: CJE1548(ppk)
            CJJ: CJJ81176_1361(ppk)
            CJU: C8J_1277(ppk)
            CJD: JJD26997_0339(ppk)
            CFF: CFF8240_0875(ppk)
            CCV: CCV52592_0727(ppk)
            CHA: CHAB381_1724(ppk)
            CCO: CCC13826_1334(ppk)
            NIS: NIS_0328(ppk)
            SUN: SUN_2152(ppk)
            GSU: GSU3323(ppk)
            GME: Gmet_0133
            BBA: Bd1010(ppk)
            DPS: DP1253
            AFW: Anae109_0573
            MXA: MXAN_0056(ppk)
            MLO: mlr8161
            MES: Meso_1119
            PLA: Plav_3326
            SME: SMc00618(ppk)
            SMD: Smed_0795
            ATU: Atu1144(ppk)
            ATC: AGR_C_2115
            RET: RHE_CH01491(ppk) RHE_PC00203
            RLE: RL1599(ppk) pRL100445
            BME: BMEI1205
            BMF: BAB1_0772(ppk)
            BMS: BR0748(ppk)
            BMB: BruAb1_0765(ppk)
            BOV: BOV_0742(ppk)
            OAN: Oant_2544
            BJA: bll4122(ppk)
            BRA: BRADO3341
            BBT: BBta_3849
            RPA: RPA3048
            RPB: RPB_2492
            RPC: RPC_2329
            RPD: RPD_2952
            RPE: RPE_3281
            NWI: Nwi_1594
            NHA: Nham_2115
            BHE: BH09820(ppk)
            BQU: BQ07590(ppk)
            XAU: Xaut_3127
            CCR: CC_1710
            RSP: RSP_0781
            RSH: Rsph17029_2437
            RSQ: Rsph17025_0398
            JAN: Jann_1058
            RDE: RD1_0979(ppk2) RD1_2042(ppk)
            PDE: Pden_1302 Pden_1594
            MMR: Mmar10_1250
            HNE: HNE_2260(ppk)
            ZMO: ZMO0712(ppk)
            SAL: Sala_1754
            SWI: Swit_0037
            ELI: ELI_03250
            GOX: GOX1936
            GBE: GbCGDNIH1_1622 GbCGDNIH1_2033
            ACR: Acry_2534
            RRU: Rru_A2161
            MAG: amb2840
            ABA: Acid345_1035
            SUS: Acid_3657
            BHA: BH1392(ppk)
            BAN: BA4208(ppk)
            BAR: GBAA4208(ppk)
            BAA: BA_4670
            BAT: BAS3903
            BCE: BC3993
            BCA: BCE_4043(ppk)
            BCZ: BCZK3751(ppk)
            BCY: Bcer98_2695
            BTK: BT9727_3735(ppk)
            BTL: BALH_3613
            SEP: SE2034
            SER: SERP2047(ppk)
            SHA: SH0587(ppk)
            SSP: SSP0433
            LPL: lp_0842(ppk)
            LDB: Ldb0523(ppk)
            LBU: LBUL_0464
            LBR: LVIS_0703
            LCA: LSEI_2616
            LRE: Lreu_0337
            OOE: OEOE_1629
            LME: LEUM_0243
            CAC: CAC0622
            CBE: Cbei_2419
            CKL: CKL_2252(ppk)
            DSY: DSY1023
            MTU: Rv2984(ppk)
            MTC: MT3062(ppk)
            MBO: Mb3008(ppk)
            MBB: BCG_3005(ppk)
            MLE: ML1681
            MPA: MAP3022(ppk)
            MAV: MAV_3834(ppk)
            MSM: MSMEG_2391(ppk)
            MVA: Mvan_2139
            MGI: Mflv_4223
            MMC: Mmcs_1925
            MKM: Mkms_1971
            MJL: Mjls_1905
            NFA: nfa42080(ppk)
            RHA: RHA1_ro06503(ppk)
            SCO: SCO4145(ppk)
            SMA: SAV4069(ppk)
            ART: Arth_3014
            AAU: AAur_2988(ppk)
            PAC: PPA0343
            NCA: Noca_4257
            TFU: Tfu_0323
            FRA: Francci3_3618
            FAL: FRAAL5826(ppk)
            KRA: Krad_0877
            SEN: SACE_6140(ppk)
            STP: Strop_1262
            BLO: BL1259(ppk)
            BAD: BAD_0127(ppk)
            RXY: Rxyl_2935
            RBA: RB9470(ppk)
            LIL: LA3459
            LIC: LIC10719(ppk)
            LBJ: LBJ_2339(ppk)
            LBL: LBL_0769(ppk)
            SYN: sll0290(ppk)
            SYW: SYNW2495(ppk)
            SYC: syc0024_d(ppk)
            SYF: Synpcc7942_1566
            SYD: Syncc9605_2663
            SYE: Syncc9902_2292
            SYG: sync_2906(ppk)
            SYR: SynRCC307_2503(ppk)
            SYX: SynWH7803_2500(ppk)
            CYA: CYA_2477(ppk)
            CYB: CYB_2082(ppk)
            TEL: tlr0213(ppk)
            GVI: gll1501
            ANA: alr3593
            AVA: Ava_3165
            PMA: Pro1862(ppk)
            PMM: PMM1696(ppk)
            PMT: PMT2245(ppk)
            PMN: PMN2A_1304
            PMI: PMT9312_1789
            PMB: A9601_19061(ppk)
            PMC: P9515_18871(ppk)
            PMF: P9303_29941(ppk)
            PMG: P9301_18871(ppk)
            PMH: P9215_19691
            PME: NATL1_21771(ppk)
            TER: Tery_1114
            BTH: BT_0541 BT_2019
            BFR: BF2645 BF3714
            BFS: BF2668 BF3507(ppk)
            PGI: PG1885(ppk)
            CHU: CHU_1414(ppk)
            GFO: GFO_1621(ppk) GFO_1833(ppk)
            FJO: Fjoh_3851 Fjoh_4535
            FPS: FP0969(ppk)
            CTE: CT0887(ppk-1) CT1049(ppk-2)
            CCH: Cag_0431 Cag_0900
            CPH: Cpha266_1333
            PVI: Cvib_0897
            PLT: Plut_1016
            RRS: RoseRS_3717
            RCA: Rcas_3540
            DRA: DR_1939(ppk)
            DGE: Dgeo_0438
            TTH: TTC0637
            MAC: MA0081(ppk)
            MBA: Mbar_A1195
            MMA: MM_1375
            MHU: Mhun_0889 Mhun_1431
            MBN: Mboo_1454
            MST: Msp_0720(ppk)
            MSI: Msm_1424
            HMA: pNG7302(ppk)
            HWA: HQ1743A(ppk)
STRUCTURES  PDB: 1XDO  1XDP  2O8R  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.1
            ExPASy - ENZYME nomenclature database: 2.7.4.1
            ExplorEnz - The Enzyme Database: 2.7.4.1
            ERGO genome analysis and discovery system: 2.7.4.1
            BRENDA, the Enzyme Database: 2.7.4.1
            CAS: 9026-44-2
///
ENTRY       EC 2.7.4.2                  Enzyme
NAME        phosphomevalonate kinase;
            ATP:5-phosphomevalonate phosphotransferase;
            5-phosphomevalonate kinase;
            mevalonate phosphate kinase;
            mevalonate-5-phosphate kinase;
            mevalonic acid phosphate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:(R)-5-phosphomevalonate phosphotransferase
REACTION    ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate
            [RN:R03245]
ALL_REAC    R03245
SUBSTRATE   ATP [CPD:C00002];
            (R)-5-phosphomevalonate [CPD:C01107]
PRODUCT     ADP [CPD:C00008];
            (R)-5-diphosphomevalonate [CPD:C01143]
REFERENCE   1
  AUTHORS   Bloch, K., Chaykin, S., Phillips, A.H. and de Waard, A.
  TITLE     Mevalonic acid pyrophosphate and isopentenyl pyrophosphate.
  JOURNAL   J. Biol. Chem. 234 (1959) 2595-2604.
  ORGANISM  rat [GN:rno], Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:13662013]
  AUTHORS   HENNING U, MOSLEIN EM, LYNEN F.
  TITLE     Biosynthesis of terpenes. V. Formation of 5-pyrophosphomevalonic
            acid by phosphomevalonic kinase.
  JOURNAL   Arch. Biochem. Biophys. 83 (1959) 259-67.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Levy, G.B. and Popjak, G.
  TITLE     Studies on the biosynthesis of cholesterol. 10. Mevalonic kinase
            from liver.
  JOURNAL   Biochem. J. 75 (1960) 417-428.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K00938  phosphomevalonate kinase
GENES       HSA: 10654(PMVK)
            MMU: 68603(Pmvk)
            CFA: 612251(PMVK)
            DME: Dmel_CG10268
            ATH: AT1G31910
            OSA: 4332275
            SCE: YMR220W(ERG8)
            AGO: AGOS_AER354W
            PIC: PICST_52257(ERG8)
            CGR: CAGL0F03993g
            SPO: SPAC343.01c
            ANI: AN2311.2
            AFM: AFUA_5G10680
            AOR: AO090010000471
            CNE: CNM00100
            UMA: UM00760.1
            DDI: DDBDRAFT_0184512
            TBR: Tb09.160.3690
            TCR: 507913.20 508277.140
            LMA: LmjF15.1460
            MXA: MXAN_5017
            OIH: OB0227
            SAU: SA0549(mvaK2)
            SAV: SAV0592(mvaK2)
            SAM: MW0547(mvaK2)
            SAR: SAR0598(mvaK2)
            SAS: SAS0551
            SAC: SACOL0638
            SAB: SAB0542(mvaK2)
            SAA: SAUSA300_0574
            SAO: SAOUHSC_00579
            SEP: SE0363
            SER: SERP0240
            SHA: SH2400(mvaK2)
            SSP: SSP2120
            LMO: lmo0012
            LMF: LMOf2365_0013
            LIN: lin0012
            LWE: lwe0013
            LLA: L10014(yebA)
            LLC: LACR_0456
            LLM: llmg_0427
            SPY: SPy_0878(mvaK2)
            SPZ: M5005_Spy_0684(mvaK2)
            SPM: spyM18_0939
            SPG: SpyM3_0597(mvaK2)
            SPS: SPs1256
            SPH: MGAS10270_Spy0742(mvaK2)
            SPI: MGAS10750_Spy0776(mvaK2)
            SPJ: MGAS2096_Spy0755(mvaK2)
            SPK: MGAS9429_Spy0739(mvaK2)
            SPF: SpyM51124(mvaK2)
            SPA: M6_Spy0701
            SPB: M28_Spy0664(mvaK2)
            SPN: SP_0383
            SPR: spr0340(mvaK2)
            SPD: SPD_0348(mvaK2)
            SAG: SAG1324
            SAN: gbs1394
            SAK: SAK_1355
            SMU: SMU.938
            STC: str0561(mvaK2)
            STL: stu0561(mvaK2)
            SSA: SSA_0335(mvaK2)
            SGO: SGO_0241
            LPL: lp_1733(mvaK2)
            LJO: LJ1207
            LAC: LBA1169
            LSA: LSA0906(mvaK2)
            LSL: LSL_0683
            LDB: Ldb0997(mvaK)
            LBU: LBUL_0904
            LBR: LVIS_0860
            LCA: LSEI_1092
            EFA: EF0902
            NFA: nfa22090
            BGA: BG0710
            BAF: BAPKO_0731
            NPH: NP2852A
            SSO: SSO2988
            STO: ST0978
            SAI: Saci_1244
STRUCTURES  PDB: 1K47  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.2
            ExPASy - ENZYME nomenclature database: 2.7.4.2
            ExplorEnz - The Enzyme Database: 2.7.4.2
            ERGO genome analysis and discovery system: 2.7.4.2
            BRENDA, the Enzyme Database: 2.7.4.2
            CAS: 9026-46-4
///
ENTRY       EC 2.7.4.3                  Enzyme
NAME        adenylate kinase;
            myokinase;
            5'-AMP-kinase;
            adenylic kinase;
            adenylokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:AMP phosphotransferase
REACTION    ATP + AMP = 2 ADP [RN:R00127]
ALL_REAC    R00127;
            (other) R01547
SUBSTRATE   ATP [CPD:C00002];
            AMP [CPD:C00020]
PRODUCT     ADP [CPD:C00008]
COMMENT     Inorganic triphosphate can also act as donor.
REFERENCE   1  [PMID:13693070]
  AUTHORS   CHIGA M, PLAUT GW.
  TITLE     Nucleotide transphosphorylases from liver. I. Purification and
            properties of an adenosine triphosphate-adenosine monophosphate
            transphosphorylase from swine liver.
  JOURNAL   J. Biol. Chem. 235 (1960) 3260-5.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:3027060]
  AUTHORS   Saint Girons I, Gilles AM, Margarita D, Michelson S, Monnot M,
            Fermandjian S, Danchin A, Barzu O.
  TITLE     Structural and catalytic characteristics of Escherichia coli
            adenylate kinase.
  JOURNAL   J. Biol. Chem. 262 (1987) 622-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:13549414]
  AUTHORS   NODA L.
  TITLE     Adenosine triphosphate-adenosine monophosphate transphosphorylase.
            III. Kinetic studies.
  JOURNAL   J. Biol. Chem. 232 (1958) 237-50.
  ORGANISM  rabbit
REFERENCE   4
  AUTHORS   Noda, L.
  TITLE     Nucleoside triphosphate-nucleoside monophosphokinases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 6, Academic Press, New York, 1962, p. 139-149.
REFERENCE   5
  AUTHORS   Noda, L. and Kuby, S.A.
  TITLE     Adenosine triphosphate-adenosine monophosphate transphosphorylase
            (myokinase). I. Isolation of the crystalline enzyme from rabbit
            skeletal muscle.
  JOURNAL   J. Biol. Chem. 226 (1957) 541-549.
  ORGANISM  rabbit
REFERENCE   6
  AUTHORS   Noda, L. and Kuby, S.A.
  TITLE     Adenosine triphosphate-adenosine monophosphate transphosphorylase
            (myokinase). II. Homogeneity measurements and physicochemical
            properties.
  JOURNAL   J. Biol. Chem. 226 (1957) 551-558.
REFERENCE   7
  AUTHORS   Oliver, I.T. and Peel, J.L.
  TITLE     Myokinase activity in microorganisms.
  JOURNAL   Biochim. Biophys. Acta 20 (1956) 390-392.
  ORGANISM  Escherichia coli [GN:eco], Mycobacterium phlei, Clostridium
            kluyveri, Thiobacillus denitrificans [GN:tbd], Streptococcus
            faecalis, Saccharomyces cerevisiae [GN:sce], Clostridium butyricum,
            Corynebacterium hofmanii, Proteus vulgaris, Rhodospirillum rubrum
            [GN:rru], Pseudomonas sp., Bacillus sphaericus, Rhizopus nigricans
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K00939  adenylate kinase
GENES       HSA: 122481(AK7) 203(AK1) 204(AK2) 205(AK3L1) 26289(AK5)
            PTR: 464756(AK1)
            MMU: 11636(Ak1) 11637(Ak2) 11639(Ak3l1)
            RNO: 24183(Ak1) 24184(Ak2) 29223(Ak3l1)
            CFA: 478145(AK2) 480712(AK1) 489554(LOC489554) 490204(AK5)
            BTA: 280715(AK1) 280716(AK2)
            GGA: 396002(LOC396002) 424555(AK5) 424697(AK3L2) 428227(AK2)
            XLA: 379924(ak2) 443877(MGC80095) 447507(MGC82064)
            XTR: 448011(ak2) 448536(TTpA012j16.1)
            DRE: 321793(ak2) 406590(zgc:85790) 445486(zgc:91930)
                 553671(zgc:112030)
            SPU: 588348(LOC588348) 592650(LOC592650) 753458(LOC753458)
                 758667(LOC758667)
            DME: Dmel_CG17146(Adk1) Dmel_CG3140(Adk2) Dmel_CG6612(Adk3)
            CEL: C29E4.8 F38B2.4 ZK673.2
            ATH: AT5G47840 AT5G50370
            OSA: 4344470 4345177 4350358
            CME: CMH232C
            SCE: YDR226W(ADK1) YER170W(ADK2)
            AGO: AGOS_AGR115C AGOS_AGR187W
            PIC: PICST_63834(ADK2) PICST_65737(ADK1)
            CAL: CaO19_3391(CaO19.3391)
            CGR: CAGL0K11418g CAGL0L11902g
            SPO: SPAC4G9.03(adk1)
            ANI: AN5122.2
            AFM: AFUA_1G03420 AFUA_1G07530
            AOR: AO090005000758 AO090012001004
            CNE: CNK03420
            UMA: UM02088.1
            ECU: ECU06_0650
            DDI: DDB_0230096(adkA) DDB_0230097(adkB)
            PFA: PF10_0086 PFD0755c
            CPV: cgd5_3360
            CHO: Chro.50037
            TAN: TA03055
            TPV: TP01_0633
            TET: TTHERM_00016460 TTHERM_00227800 TTHERM_00317200
                 TTHERM_00558060 TTHERM_00727630
            TBR: Tb09.211.0350 Tb10.70.1200 Tb10.70.5130 Tb10.70.5150
                 Tb10.70.7330 Tb927.2.5660 Tb927.5.3970
            TCR: 503479.30 506195.80 506195.90 506855.180 507883.80 509733.180
                 510243.50 510575.180
            LMA: LmjF04.0960 LmjF21.1250 LmjF34.0110 LmjF34.0120 LmjF36.1360
            EHI: 296.t00004 3.t00004
            ECO: b0474(adk)
            ECJ: JW0463(adk)
            ECE: Z0591(adk)
            ECS: ECs0527
            ECC: c0594(adk)
            ECI: UTI89_C0502(adk)
            ECP: ECP_0535
            ECV: APECO1_1541(adk)
            ECW: EcE24377A_0513(adk)
            ECX: EcHS_A0551
            STY: STY0532(adk)
            STT: t2372(adk)
            SPT: SPA2234(adk)
            SEC: SC0529(adk)
            STM: STM0488(adk)
            YPE: YPO3118(adk)
            YPK: y1065(adk)
            YPM: YP_0812(adk)
            YPA: YPA_2611
            YPN: YPN_0971
            YPP: YPDSF_2754
            YPS: YPTB0996(adk)
            YPI: YpsIP31758_3054(adk)
            SFL: SF0419(adk)
            SFX: S0426(adk)
            SFV: SFV_0447(adk)
            SSN: SSON_0461(adk)
            SBO: SBO_0374(adk)
            SDY: SDY_0445(adk)
            ECA: ECA1180(adk)
            PLU: plu3836(adk)
            BUC: BU484(adk)
            BAS: BUsg469(adk)
            BAB: bbp428(adk)
            BCC: BCc_303(adk)
            WBR: WGLp528(adk)
            SGL: SG0693
            ENT: Ent638_0954
            KPN: KPN_00456(adk)
            BFL: Bfl302(adk)
            BPN: BPEN_310(adk)
            HIN: HI0349(adk)
            HIT: NTHI0468(adk)
            HIP: CGSHiEE_01265(adk)
            HDU: HD0826(adk)
            HSO: HS_0648(adk)
            PMU: PM0284(adk)
            MSU: MS0796(adk)
            APL: APL_1298(adk)
            XFA: XF0275
            XFT: PD0222(adk)
            XCC: XCC3291(adk)
            XCB: XC_0873
            XCV: XCV3553(adk)
            XAC: XAC3437(adk)
            XOO: XOO0963(adk)
            XOM: XOO_0879(XOO0879)
            VCH: VC0986
            VCO: VC0395_A0507(adk)
            VVU: VV1_0188
            VVY: VV1002
            VPA: VP0822
            VFI: VF0793(adk)
            PPR: PBPRA1024
            PAE: PA3686(adk)
            PAU: PA14_16700(adk)
            PPU: PP_1506(adk)
            PST: PSPTO_1509(adk)
            PSB: Psyr_1319(adk)
            PSP: PSPPH_3863(adk)
            PFL: PFL_1148(adk)
            PFO: Pfl_1070(adk)
            PEN: PSEEN1265(adk)
            PAR: Psyc_1557(adk)
            PCR: Pcryo_1739
            ACI: ACIAD1105(adk)
            SON: SO_2018(adk)
            SDN: Sden_1430
            SFR: Sfri_1540
            SAZ: Sama_1315
            SBL: Sbal_2546
            SLO: Shew_2230
            SPC: Sputcn32_2297
            SSE: Ssed_0373
            SHE: Shewmr4_2249
            SHM: Shewmr7_2321
            SHN: Shewana3_2441
            SHW: Sputw3181_1711
            ILO: IL1845(adk)
            CPS: CPS_3900
            PHA: PSHAa1208(adk)
            PAT: Patl_2893
            SDE: Sde_2235
            PIN: Ping_0957
            MAQ: Maqu_2232
            CBU: CBU_0454(adk)
            CBD: COXBU7E912_1620(adk)
            LPN: lpg1411(adk)
            LPF: lpl1362(adk)
            LPP: lpp1366(adk)
            MCA: MCA2066(adk)
            FTU: FTT1161(adk)
            FTF: FTF1161(adk)
            FTW: FTW_1200(kad)
            FTL: FTL_0795
            FTH: FTH_0788(adk)
            FTA: FTA_0840
            FTN: FTN_1142(adk)
            TCX: Tcr_2058
            NOC: Noc_2847
            AEH: Mlg_1256
            HHA: Hhal_1784
            HCH: HCH_01814
            CSA: Csal_0857
            ABO: ABO_0840(adk)
            AHA: AHA_2489
            DNO: DNO_1071(adk)
            BCI: BCI_0118(adk)
            RMA: Rmag_0093
            VOK: COSY_0097(adk)
            NME: NMB0823
            NMA: NMA1032(adk)
            NMC: NMC0767(adk)
            NGO: NGO0400(adk)
            CVI: CV_3343(adk)
            RSO: RSc2533(adk)
            REU: Reut_A0590(adk)
            REH: H16_A0603(adk)
            RME: Rmet_0532
            BMA: BMA2277(adk)
            BMV: BMASAVP1_A0572(adk)
            BML: BMA10299_A1049(adk)
            BMN: BMA10247_2154(adk)
            BXE: Bxe_A0763
            BVI: Bcep1808_2641
            BUR: Bcep18194_A5879(adk)
            BCN: Bcen_1936
            BCH: Bcen2424_2548
            BAM: Bamb_2596
            BPS: BPSL0875(adk)
            BPM: BURPS1710b_1080(adk)
            BPL: BURPS1106A_0927(adk)
            BPD: BURPS668_0924(adk)
            BTE: BTH_I0739
            PNU: Pnuc_0281
            BPE: BP2769(adk)
            BPA: BPP2560(adk)
            BBR: BB2005(adk)
            RFR: Rfer_3158
            POL: Bpro_2952
            PNA: Pnap_1920
            AAV: Aave_2561
            AJS: Ajs_2308
            VEI: Veis_4895
            MPT: Mpe_A2488
            HAR: HEAR2487(adk)
            MMS: mma_2576
            NEU: NE1933(adk)
            NMU: Nmul_A0741
            EBA: ebA5087(adk)
            AZO: azo1473(adk)
            DAR: Daro_3205
            TBD: Tbd_1504
            MFA: Mfla_2153
            HPY: HP0618(adk)
            HPJ: jhp0561(adk)
            HPA: HPAG1_0599
            HHE: HH1771(adk)
            HAC: Hac_0834(adk)
            WSU: WS1782
            TDN: Tmden_1087 Tmden_1088
            CJE: Cj0639c(adk)
            CJR: CJE0742(adk)
            CJU: C8J_0598(adk)
            CFF: CFF8240_1197
            CCV: CCV52592_0466
            CHA: CHAB381_0295 CHAB381_1528
            ABU: Abu_0779(adk1) Abu_0780(adk2)
            NIS: NIS_0769
            SUN: SUN_0411 SUN_1507
            GSU: GSU2836(adk)
            GME: Gmet_0647
            GUR: Gura_1087
            PCA: Pcar_0722(adk)
            PPD: Ppro_0701
            DVU: DVU1932(adk)
            DDE: Dde_2028
            LIP: LI0317
            BBA: Bd2954(adk)
            DPS: DP1733
            ADE: Adeh_1925
            AFW: Anae109_1932
            MXA: MXAN_3320(adk)
            SAT: SYN_02188 SYN_02538
            SFU: Sfum_1576
            RPR: RP638(adk)
            RTY: RT0630(adk)
            RCO: RC0985(adk)
            RFE: RF_0299(adk)
            RBE: RBE_1041(adk)
            RAK: A1C_05000(adk)
            RCM: A1E_04265(adk)
            RRI: A1G_05450(adk)
            OTS: OTBS_0356(adk)
            WOL: WD0661(adk)
            WBM: Wbm0321
            AMA: AM891(adk)
            APH: APH_0300(adk)
            ERU: Erum5880(adk)
            ERW: ERWE_CDS_06180(adk)
            ERG: ERGA_CDS_06090(adk)
            ECN: Ecaj_0592
            ECH: ECH_0429(adk)
            NSE: NSE_0286(adk)
            PUB: SAR11_1096(adk)
            MLO: mlr0322
            MES: Meso_1657
            SME: SMc01288(adk)
            ATU: Atu1926(adk)
            ATC: AGR_C_3521(adk)
            RET: RHE_CH01696(adk)
            RLE: RL1795(adk) pRL100122(adk)
            BME: BMEI0778 BMEI1228
            BMF: BAB1_0742 BAB1_1234(adk)
            BMS: BR0724 BR1212(adk)
            BMB: BruAb1_0741 BruAb1_1217(adk)
            BOV: BOV_1175(adk)
            BJA: bll5379
            BRA: BRADO3087(adk)
            BBT: BBta_5049(adk) BBta_7769
            RPA: RPA3229(adk)
            RPB: RPB_2316
            RPC: RPC_3427
            RPD: RPD_3163
            RPE: RPE_3565
            NWI: Nwi_1385(adk)
            NHA: Nham_1566
            BHE: BH10300(adk)
            BQU: BQ08020(adk)
            BBK: BARBAKC583_0719(adk)
            CCR: CC_1269
            SIL: SPO0507(adk-1) SPO1812(adk-2)
            SIT: TM1040_0276 TM1040_1490
            RSP: RSP_0578 RSP_1736(adk)
            RSQ: Rsph17025_2513
            JAN: Jann_0613
            RDE: RD1_1116(adk-2) RD1_1433(adk)
            MMR: Mmar10_1774
            HNE: HNE_2830(adk)
            ZMO: ZMO0538(adk)
            NAR: Saro_1270
            SAL: Sala_2797
            ELI: ELI_08080
            GOX: GOX0359
            GBE: GbCGDNIH1_0575
            ACR: Acry_1925
            RRU: Rru_A2667
            MAG: amb3110
            MGM: Mmc1_1753
            ABA: Acid345_1247 Acid345_3213
            SUS: Acid_5097
            BSU: BG10446(adk)
            BHA: BH0155(adk)
            BAN: BA0131(adk)
            BAR: GBAA0131(adk)
            BAA: BA_0714
            BAT: BAS0131
            BCE: BC0152(adk)
            BCA: BCE_0131(adk)
            BCZ: BCZK0125(adk)
            BCY: Bcer98_0125
            BTK: BT9727_0127(adk)
            BTL: BALH_0129(adk)
            BLI: BL01030(adk)
            BLD: BLi00154(adk)
            BCL: ABC0171(adk)
            BAY: RBAM_001620
            BPU: BPUM_0123
            OIH: OB0140(adk)
            GKA: GK0127
            GTN: GTNG_0126(adk)
            SAU: SA2027(adk)
            SAV: SAV2229(adk)
            SAM: MW2148(adk)
            SAR: SAR2314(adk)
            SAS: SAS2120
            SAC: SACOL2218(adk)
            SAB: SAB2101c(adk)
            SAA: SAUSA300_2183(adk)
            SAO: SAOUHSC_02490
            SEP: SE1802
            SER: SERP1810(adk)
            SHA: SH0823(adk)
            SSP: SSP0684
            LMO: lmo2611(adk)
            LMF: LMOf2365_2584
            LIN: lin2760(adk)
            LWE: lwe2561(adk)
            LLA: L140714(adk)
            LLC: LACR_2380
            LLM: llmg_2359(adk)
            SPY: SPy_0074(adk)
            SPZ: M5005_Spy_0065(adk)
            SPM: spyM18_0074(adk)
            SPG: SpyM3_0061(adk)
            SPS: SPs0063
            SPH: MGAS10270_Spy0068(adk)
            SPI: MGAS10750_Spy0069(adk)
            SPJ: MGAS2096_Spy0068(adk)
            SPK: MGAS9429_Spy0065(adk)
            SPF: SpyM50065(adk)
            SPA: M6_Spy0114(adk)
            SPB: M28_Spy0064(adk)
            SPN: SP_0231
            SPR: spr0210(adk)
            SPD: SPD_0214(adk)
            SAG: SAG0079(adk)
            SAN: gbs0079(adk)
            SAK: SAK_0112(adk)
            SMU: SMU.2005(adk)
            STC: str1913(adk)
            STL: stu1913(adk)
            STE: STER_1886
            SSA: SSA_0128(adk)
            SSU: SSU05_0091
            SSV: SSU98_0093
            SGO: SGO_1964(adk)
            LPL: lp_1058(adk)
            LJO: LJ0357
            LAC: LBA0312
            LSA: LSA1744(adk)
            LSL: LSL_1414(adk)
            LDB: Ldb0417(adk)
            LBU: LBUL_0371
            LBR: LVIS_1669
            LCA: LSEI_2482
            LGA: LGAS_0311
            LRE: Lreu_1462
            PPE: PEPE_1397
            EFA: EF0228(adk)
            OOE: OEOE_0615
            STH: STH3054
            CAC: CAC3112(adk)
            CPE: CPE2384(adk)
            CPF: CPF_2693(adk)
            CPR: CPR_2378(adk)
            CTC: CTC02583(adk)
            CNO: NT01CX_1136
            CTH: Cthe_2924
            CDF: CD0091(adk)
            CBO: CBO3460(adk)
            CBA: CLB_3516(adk)
            CBH: CLC_3404(adk)
            CBF: CLI_3642(adk)
            CKL: CKL_0245(adk)
            CHY: CHY_1340(adk)
            DSY: DSY0492
            DRM: Dred_1718
            PTH: PTH_1418(adk)
            SWO: Swol_2312
            TTE: TTE2271(adk)
            MTA: Moth_2439
            MGE: MG_171(adk)
            MPN: MPN185(adk)
            MPU: MYPU_5670(adk)
            MPE: MYPE9970(adk)
            MGA: MGA_0743(adk)
            MMY: MSC_0725(adk)
            MMO: MMOB2550(adk)
            MHY: mhp208(adk)
            MHJ: MHJ_0170(adk)
            MHP: MHP7448_0174(adk)
            MSY: MS53_0580(adk)
            MCP: MCAP_0676(adk)
            UUR: UU251(adk)
            POY: PAM221(adk)
            AYW: AYWB_501(adk)
            MFL: Mfl144
            MTU: Rv0733(adk)
            MTC: MT0757(adk)
            MBO: Mb0754(adk)
            MBB: BCG_0783(adk)
            MLE: ML1832(adk)
            MPA: MAP4199(adk)
            MAV: MAV_4433
            MSM: MSMEG_1484
            MMC: Mmcs_1047
            CGL: NCgl0533(adk)
            CGB: cg0648(adk)
            CEF: CE0565
            CDI: DIP0541(adk)
            CJK: jk1765(adk)
            NFA: nfa7950(adk)
            RHA: RHA1_ro06154(adk1) RHA1_ro07078(adk2)
            SCO: SCO4723(adk)
            SMA: SAV4947(adk)
            TWH: TWT534(adk)
            TWS: TW226(adk)
            LXX: Lxx20130(adk)
            CMI: CMM_2597(adkA)
            AAU: AAur_2928(adk) AAur_3426(adk) AAur_pTC20149(adk)
            PAC: PPA1834(adk)
            TFU: Tfu_2625
            FRA: Francci3_0603 Francci3_3011 Francci3_3887
            FAL: FRAAL0534(adk) FRAAL1102(adk) FRAAL4963(adk) FRAAL6192
            ACE: Acel_0327
            SEN: SACE_2376(adk) SACE_6812(adk)
            STP: Strop_3902
            BLO: BL1601(adk)
            BAD: BAD_0342(adk)
            RXY: Rxyl_2134
            FNU: FN1298
            RBA: RB1079(adk) RB7867(adk)
            CTR: CT128(adk)
            CTA: CTA_0135(adk)
            CMU: TC0404
            CPN: CPn0244(adk)
            CPA: CP0518
            CPJ: CPj0244(adk)
            CPT: CpB0251
            CCA: CCA00535(adk)
            CAB: CAB521(adk)
            CFE: CF0474(adk2)
            PCU: pc1041(adk)
            BGA: BG0420(adk)
            TPA: TP0595(adk)
            TDE: TDE1112(adk)
            LIL: LA0760
            LIC: LIC12852(adk)
            LBJ: LBJ_2638(adk)
            LBL: LBL_0434(adk-1) LBL_0474(adk)
            SYN: sll1059(adk) sll1815(adk)
            SYW: SYNW2086(adk)
            SYC: syc1884_d(adk)
            SYF: Synpcc7942_2213
            SYD: Syncc9605_0357
            SYE: Syncc9902_1974
            SYG: sync_0418(adk)
            SYR: SynRCC307_2135(adk)
            SYX: SynWH7803_0415(adk)
            CYA: CYA_1159(adk)
            CYB: CYB_2616(adk)
            TEL: tlr0100
            GVI: gll1392
            ANA: all4196 alr0068
            AVA: Ava_0710(adk) Ava_2670
            PMA: Pro1693(adk)
            PMM: PMM1539(adk)
            PMT: PMT1751(adk)
            PMN: PMN2A_1110
            PMI: PMT9312_1631
            PMB: A9601_17461(adk)
            PMC: P9515_17211(adk)
            PMF: P9303_23221(adk)
            PMG: P9301_17301(adk)
            PMH: P9215_18101
            PME: NATL1_19841(adk)
            TER: Tery_2993
            BTH: BT_4387
            BFR: BF1120
            BFS: BF1032
            PGI: PG0791(adk)
            SRU: SRU_1875(adk)
            CHU: CHU_0068(adk)
            GFO: GFO_2868(adk)
            FPS: FP1359(adk)
            CTE: CT1185(adk)
            CCH: Cag_0827
            CPH: Cpha266_1541
            PVI: Cvib_0952
            PLT: Plut_0949
            DET: DET0495(adk)
            DEH: cbdb_A459(adk)
            DRA: DR_2117
            DGE: Dgeo_1846
            TTH: TTC1307
            TTJ: TTHA1671
            AAE: aq_078(kad)
            TMA: TM1479
            TME: Tmel_0974
            FNO: Fnod_1117
            MJA: MJ0479(adk)
            MMP: MMP1031(adkA)
            MMQ: MmarC5_0562
            MAC: MA1096(adk)
            MBA: Mbar_A0086
            MMA: MM_1313 MM_2148
            MBU: Mbur_0025
            MTP: Mthe_1504
            MHU: Mhun_2229
            MLA: Mlab_0476
            MEM: Memar_0588
            MBN: Mboo_0556
            MTH: MTH1663 MTH27
            MST: Msp_0884(adkA)
            MSI: Msm_0737
            MKA: MK0025(adkA)
            AFU: AF0676(adk)
            HAL: VNG1724G(adk)
            HMA: rrnAC3346(adk)
            HWA: HQ1449A(adkA) HQ2767A(adk)
            NPH: NP4910A(adk)
            TAC: Ta1247
            TVO: TVN0349
            PTO: PTO0664 PTO0809
            PHO: PH1117 PH1753
            PAB: PAB0739(adk) PAB2140
            PFU: PF1045 PF1800
            TKO: TK0812 TK1517
            RCI: RCIX2459(adk-1) RCIX2570(adk-2)
            APE: APE_0981.1
            SMR: Smar_0398
            HBU: Hbut_1324
            SSO: SSO0694(adkA)
            STO: ST0410
            SAI: Saci_0573(adk)
            PAI: PAE1681
            PIS: Pisl_1687
            PCL: Pcal_1434
            PAS: Pars_1829
            TPE: Tpen_0010 Tpen_0167
            NEQ: NEQ149
STRUCTURES  PDB: 1AK2  1AKE  1AKY  1ANK  1DVR  1E4V  1E4Y  1KHT  1KI9  1NKS  
                 1P3J  1P4S  1S3G  1Z83  1ZAK  1ZIN  1ZIO  1ZIP  2AK2  2AKY  
                 2AR7  2BBW  2BWJ  2C95  2C9Y  2CDN  2ECK  2EU8  3ADK  3AKY  
                 4AKE  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.3
            ExPASy - ENZYME nomenclature database: 2.7.4.3
            ExplorEnz - The Enzyme Database: 2.7.4.3
            ERGO genome analysis and discovery system: 2.7.4.3
            BRENDA, the Enzyme Database: 2.7.4.3
            CAS: 9013-02-9
///
ENTRY       EC 2.7.4.4                  Enzyme
NAME        nucleoside-phosphate kinase;
            NMP-kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:nucleoside-phosphate phosphotransferase
REACTION    ATP + nucleoside phosphate = ADP + nucleoside diphosphate
            [RN:R00334]
ALL_REAC    R00334 > R00158 R02098
SUBSTRATE   ATP [CPD:C00002];
            nucleoside phosphate [CPD:C03013]
PRODUCT     ADP [CPD:C00008];
            nucleoside diphosphate [CPD:C00454]
COMMENT     Many nucleotides can act as acceptors; other nucleoside
            triphosphates can act instead of ATP.
REFERENCE   1  [PMID:13363863]
  AUTHORS   AYENGAR P, GIBSON DM, SANADI DR.
  TITLE     Transphosphorylations between nucleoside phosphates.
  JOURNAL   Biochim. Biophys. Acta. 21 (1956) 86-91.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:14401179]
  AUTHORS   HEPPEL LA, STROMINGER JL, MAXWELL ES.
  TITLE     Nucleoside monophosphate kinases. II. Transphosphorylation betweeen
            adenosine monophosphate and nucleoside triphosphates.
  JOURNAL   Biochim. Biophys. Acta. 32 (1959) 422-30.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:14392176]
  AUTHORS   LIEBERMAN I, KORNBERG A, SIMMS ES.
  TITLE     Enzymatic synthesis of nucleoside diphosphates and triphosphates.
  JOURNAL   J. Biol. Chem. 215 (1955) 429-40.
  ORGANISM  cow [GN:bta]
REFERENCE   4
  AUTHORS   Noda, L.
  TITLE     Nucleoside triphosphate-nucleoside monophosphokinases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 6, Academic Press, New York, 1962, p. 139-149.
PATHWAY     PATH: map00240  Pyrimidine metabolism
STRUCTURES  PDB: 2BND  2BNE  2BNF  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.4
            ExPASy - ENZYME nomenclature database: 2.7.4.4
            ExplorEnz - The Enzyme Database: 2.7.4.4
            ERGO genome analysis and discovery system: 2.7.4.4
            BRENDA, the Enzyme Database: 2.7.4.4
            CAS: 9026-50-0
///
ENTRY       EC 2.7.4.5        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
COMMENT     Deleted entry: deoxycytidylate kinase. Now included with EC 2.7.4.14
            cytidylate kinase (EC 2.7.4.5 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.5
            ExPASy - ENZYME nomenclature database: 2.7.4.5
            ExplorEnz - The Enzyme Database: 2.7.4.5
            ERGO genome analysis and discovery system: 2.7.4.5
            BRENDA, the Enzyme Database: 2.7.4.5
///
ENTRY       EC 2.7.4.6                  Enzyme
NAME        nucleoside-diphosphate kinase;
            nucleoside 5'-diphosphate kinase;
            nucleoside diphosphate (UDP) kinase;
            nucleoside diphosphokinase;
            nucleotide phosphate kinase;
            UDP kinase;
            uridine diphosphate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:nucleoside-diphosphate phosphotransferase
REACTION    ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
            [RN:R00331]
ALL_REAC    R00331 > R00124 R00156 R00330 R00570 R00722 R01137 R01857 R02093
            R02326 R02331 R03530
SUBSTRATE   ATP [CPD:C00002];
            nucleoside diphosphate [CPD:C00454]
PRODUCT     ADP [CPD:C00008];
            nucleoside triphosphate [CPD:C00201]
COMMENT     Many nucleoside diphosphates can act as acceptors, while many ribo-
            and deoxyribonucleoside triphosphates can act as donors.
REFERENCE   1
  AUTHORS   Berg, P. and Joklik, W.K.
  TITLE     Enzymatic phosphorylation of nucleoside diphosphates.
  JOURNAL   J. Biol. Chem. 210 (1954) 657-672.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], rabbit
REFERENCE   2  [PMID:13363863]
  AUTHORS   AYENGAR P, GIBSON DM, SANADI DR.
  TITLE     Transphosphorylations between nucleoside phosphates.
  JOURNAL   Biochim. Biophys. Acta. 21 (1956) 86-91.
  ORGANISM  pig [GN:ssc]
REFERENCE   3
  AUTHORS   Kirkland, R.J.A. and Turner, J.F.
  TITLE     Nucleoside diphosphokinase of pea seeds.
  JOURNAL   Biochem. J. 72 (1959) 716-720.
  ORGANISM  Pisum sativum
REFERENCE   4  [PMID:13115426]
  AUTHORS   KREBS HA, HEMS R.
  TITLE     Some reactions of adenosine and inosine phosphates in animal
            tissues.
  JOURNAL   Biochim. Biophys. Acta. 12 (1953) 172-80.
  ORGANISM  pigeon
REFERENCE   5  [PMID:5925862]
  AUTHORS   Nakamura H, Sugino Y.
  TITLE     Metabolism of deoxyribonucleotides. 3. Purification and some
            properties of nucleoside diphosphokinase of calf thymus.
  JOURNAL   J. Biol. Chem. 241 (1966) 4917-22.
  ORGANISM  cow [GN:bta]
REFERENCE   6
  AUTHORS   Ratliff, R.L., Weaver, R.H., Lardy, H.A. and Kuby, S.A.
  TITLE     Nucleoside triphosphate-nucleoside diphosphate transphosphorylase
            (nucleoside diphosphokinase). I. Isolation of the crystalline enzyme
            from brewers' yeast.
  JOURNAL   J. Biol. Chem. 239 (1964) 301-309.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K00940  nucleoside-diphosphate kinase
GENES       HSA: 10201(NME6) 29922(NME7) 4830(NME1) 4831(NME2) 4833(NME4)
            PTR: 455134(NME1-NME2) 462089(NME5)
            MMU: 171567(Nme7) 18102(Nme1) 18103(Nme2) 54369(Nme6) 56520(Nme4)
                 75533(Nme5) 79059(Nme3)
            RNO: 171566(Nme7) 191575(Nme1) 58964(Nme6) 83782(Nme2) 85269(Nme3)
            CFA: 476638(NME6) 480558(NME1) 609873(LOC609873) 610421(NME5)
                 611104(NME3)
            BTA: 404079(NBR-B) 404189(NBR-A) 511647(NME4)
            GGA: 395916(NME2) 416373(NME5) 416399(NME3) 422094(NME1)
                 426866(NME6)
            XLA: 399333(Nme1) 414658(MGC81083) 447181(MGC85572)
                 447618(MGC85510) 495951(LOC495951)
            XTR: 448695(MGC89980) 448725(nme2)
            DRE: 30083(nme2) 30085(ndpkz3) 30086(ndpkz4) 335716(nme2l)
                 394170(nme4) 58120(ndpkz6)
            SPU: 580218(LOC580218) 583346(LOC583346) 585473(LOC585473)
                 590350(LOC590350) 594617(LOC594617)
            DME: Dmel_CG2210(awd) Dmel_CG5310 Dmel_CG8362
            CEL: F25H2.5
            ATH: AT4G23900 AT5G63310(NDPK2)
            OSA: 4339815 4343275 4349403 4352460
            CME: CMK060C CML110C
            SCE: YKL067W(YNK1)
            AGO: AGOS_ABR096C
            PIC: PICST_67856(YNK1)
            CGR: CAGL0M13277g
            SPO: SPAC806.07(ndk1)
            ANI: AN8216.2
            AFM: AFUA_5G03490
            AOR: AO090102000558
            CNE: CNE02610 CNJ00180
            UMA: UM02776.1 UM03988.1
            ECU: ECU06_1530
            DDI: DDBDRAFT_0191701 DDBDRAFT_0217316 DDB_0214817(ndkM)
            PFA: PF13_0349 PFF0275c
            CPV: cgd4_1940 cgd5_1470
            CHO: Chro.40219 Chro.50237
            TAN: TA13095
            TPV: TP02_0422
            TET: TTHERM_00161010 TTHERM_00346410 TTHERM_00894400
            TBR: Tb09.211.2560 Tb11.01.7800 Tb927.4.1720
            TCR: 508461.400 508707.200
            LMA: LmjF32.2950 LmjF35.3870
            EHI: 38.t00039
            ECO: b2518(ndk)
            ECJ: JW2502(ndk)
            ECE: Z3781(ndk)
            ECS: ECs3380
            ECC: c3041(ndk)
            ECI: UTI89_C2840(ndk)
            ECP: ECP_2523
            ECV: APECO1_4006(ndk)
            ECW: EcE24377A_2802(ndk)
            ECX: EcHS_A2669
            STY: STY2771(ndk)
            STT: t0330(ndk)
            SPT: SPA0341(ndk)
            SEC: SC2523(ndk)
            STM: STM2526(ndk)
            YPE: YPO2883(ndk)
            YPK: y1349(ndk)
            YPM: YP_2749(ndk)
            YPA: YPA_2323
            YPN: YPN_1255
            YPP: YPDSF_2228
            YPS: YPTB2845(ndk)
            YPI: YpsIP31758_1182(ndk)
            YEN: YE1069(ndk)
            SFL: SF2564(ndk)
            SFX: S2736(ndk)
            SFV: SFV_2565(ndk)
            SSN: SSON_2600(ndk)
            SBO: SBO_2542(ndk)
            SDY: SDY_2714(ndk)
            ECA: ECA3224(ndk)
            PLU: plu1372(ndk)
            WBR: WGLp570(ndk)
            SGL: SG1764
            ENT: Ent638_3012
            SPE: Spro_3613
            BFL: Bfl533(ndk)
            BPN: BPEN_553(ndk)
            HIN: HI0876(ndk)
            HIT: NTHI1039(ndk)
            HIP: CGSHiEE_07650(ndk)
            HIQ: CGSHiGG_07920(ndk)
            HDU: HD1053(ndk)
            HSO: HS_0387(ndk)
            PMU: PM1028(ndk)
            MSU: MS0668(ndk)
            APL: APL_0351(ndk)
            ASU: Asuc_0834
            XFA: XF0458
            XFT: PD1625(ndk)
            XCC: XCC1981(ndk)
            XCB: XC_2203
            XCV: XCV2066(ndk)
            XAC: XAC2015(ndk)
            XOO: XOO2535(ndk)
            XOM: XOO_2393(XOO2393)
            VCH: VC0756
            VCO: VC0395_A0285(ndk)
            VVU: VV1_0430
            VVY: VV0763
            VPA: VP0604
            VFI: VF0625 VF0793(adk)
            PPR: PBPRA0759
            PAE: PA3807(ndk)
            PAU: PA14_14820(ndk)
            PPU: PP_0849(ndk)
            PPF: Pput_0879
            PST: PSPTO_1430(ndk)
            PSB: Psyr_1244
            PSP: PSPPH_1316(ndk)
            PFL: PFL_4958(ndk)
            PFO: Pfl_4605
            PEN: PSEEN1017(ndk)
            PMY: Pmen_3504
            PAR: Psyc_0678(ndk)
            PCR: Pcryo_0647
            PRW: PsycPRwf_1906
            ACI: ACIAD0556(ndk)
            SON: SO_2274(ndk)
            SDN: Sden_2390
            SFR: Sfri_2417
            SAZ: Sama_1301
            SBL: Sbal_2389
            SBM: Shew185_2377
            SLO: Shew_2310
            SPC: Sputcn32_2141
            SSE: Ssed_2862
            SPL: Spea_1498
            SHE: Shewmr4_1747
            SHM: Shewmr7_1827
            SHN: Shewana3_2272
            SHW: Sputw3181_1870
            ILO: IL2038(ndk)
            CPS: CPS_4256(ndk)
            PHA: PSHAb0142(ndk)
            PAT: Patl_3130
            SDE: Sde_1430
            PIN: Ping_3326
            MAQ: Maqu_1123
            CBU: CBU_1258(ndk)
            CBD: COXBU7E912_1342(ndk)
            LPN: lpg1548(ndk)
            LPF: lpl1478(ndk)
            LPP: lpp1505(ndk)
            MCA: MCA2886(ndk)
            FTU: FTT0373c(ndk)
            FTF: FTF0373c(ndk)
            FTW: FTW_1707(ndk)
            FTL: FTL_1310
            FTH: FTH_1282(ndk)
            FTA: FTA_1385
            FTN: FTN_0271(ndk)
            TCX: Tcr_0619
            NOC: Noc_0899
            AEH: Mlg_1248
            HHA: Hhal_1792
            HCH: HCH_04460(ndk)
            CSA: Csal_2850
            ABO: ABO_1864(ndk)
            MMW: Mmwyl1_1352
            AHA: AHA_1755
            BCI: BCI_0007(ndk)
            RMA: Rmag_0381
            VOK: COSY_0355(ndk)
            NME: NMB1307
            NMA: NMA1521(ndk)
            NMC: NMC1244(ndk)
            NGO: NGO0597
            CVI: CV_3542(ndk)
            RSO: RSc1211(ndk)
            REU: Reut_A2090
            REH: H16_A2368(ndk)
            RME: Rmet_2110
            BMA: BMA1348(ndk)
            BMV: BMASAVP1_A1838(ndk)
            BML: BMA10299_A0059(ndk)
            BMN: BMA10247_1110(ndk)
            BXE: Bxe_A1591
            BVI: Bcep1808_1742
            BUR: Bcep18194_A5116
            BCN: Bcen_6264
            BCH: Bcen2424_1815
            BAM: Bamb_1753
            BPS: BPSL1510(ndk)
            BPM: BURPS1710b_2358(ndk)
            BPL: BURPS1106A_2231(ndk)
            BPD: BURPS668_2193(ndk)
            BTE: BTH_I2231
            PNU: Pnuc_1293
            BPE: BP2202(ndk)
            BPA: BPP2858(ndk)
            BBR: BB3179(ndk)
            RFR: Rfer_2311
            POL: Bpro_2612
            PNA: Pnap_1868
            AAV: Aave_1420
            AJS: Ajs_1166
            VEI: Veis_0084
            MPT: Mpe_A2000
            HAR: HEAR1260(ndk)
            MMS: mma_2131
            NEU: NE0144(ndk)
            NET: Neut_2172
            NMU: Nmul_A2380
            EBA: ebB37(ndk)
            AZO: azo0923(ndk)
            DAR: Daro_2989
            TBD: Tbd_0590
            MFA: Mfla_1624
            HPY: HP0198(ndk)
            HPJ: jhp0184(ndk)
            HPA: HPAG1_0192
            HHE: HH0677(ndk)
            HAC: Hac_0383(ndk)
            WSU: WS1991
            TDN: Tmden_1775
            CJE: Cj0332c(ndk)
            CJR: CJE0377(ndk)
            CJJ: CJJ81176_0354(ndk)
            CJU: C8J_0309(ndk)
            CJD: JJD26997_1626(ndk)
            CFF: CFF8240_0233(ndk)
            CCV: CCV52592_1691
            CHA: CHAB381_1488
            CCO: CCC13826_0990 CCC13826_1212
            ABU: Abu_0291(ndk)
            NIS: NIS_0395(ndk)
            SUN: SUN_2052(ndk)
            GSU: GSU1110(ndk)
            GME: Gmet_2686
            GUR: Gura_1580
            PCA: Pcar_2023
            PPD: Ppro_3244
            DVU: DVU2333(ndk)
            DVL: Dvul_0925
            DDE: Dde_1439
            LIP: LI1121(ndk)
            BBA: Bd3827(ndk)
            DPS: DP1948
            ADE: Adeh_1629
            AFW: Anae109_2182
            MXA: MXAN_3543(ndk)
            SAT: SYN_02188 SYN_02538
            SFU: Sfum_0500
            RPR: RP055(ndk)
            RTY: RT0077(ndk)
            RCO: RC0083(ndk)
            RFE: RF_0120(ndk)
            RBE: RBE_1353(ndk)
            RAK: A1C_00450(ndk)
            RBO: A1I_00785(ndk)
            RCM: A1E_00260(ndk)
            RRI: A1G_00525(ndk)
            OTS: OTBS_1862(ndk)
            WOL: WD1183(ndk)
            WBM: Wbm0717
            AMA: AM1137(ndk)
            APH: APH_1217(ndk)
            ERU: Erum8570(ndk)
            ERW: ERWE_CDS_09080(ndk)
            ERG: ERGA_CDS_08980(ndk)
            ECN: Ecaj_0893
            ECH: ECH_1117(ndk)
            NSE: NSE_0560(ndk)
            PUB: SAR11_0717(ndk)
            MLO: mll7917
            MES: Meso_1979
            PLA: Plav_3333
            SME: SMc00595(ndk)
            SMD: Smed_0775
            ATU: Atu1122(ndk)
            ATC: AGR_C_2077
            RET: RHE_CH01472(ndk)
            RLE: RL1580(ndk)
            BME: BMEI1256
            BMF: BAB1_0715(ndk)
            BMS: BR0694(ndk)
            BMB: BruAb1_0713(ndk)
            BOV: BOV_0685(ndk)
            OAN: Oant_2594
            BJA: blr4119(ndk)
            BRA: BRADO3334(ndk)
            BBT: BBta_3838(ndk)
            RPA: RPA3056
            RPB: RPB_2485
            RPC: RPC_2318
            RPD: RPD_2961
            RPE: RPE_3287
            NWI: Nwi_1601
            NHA: Nham_2122
            BHE: BH05530(ndk)
            BQU: BQ04690(ndk)
            BBK: BARBAKC583_0514(ndk)
            XAU: Xaut_2328
            CCR: CC_1699
            SIL: SPO2444(ndk)
            SIT: TM1040_0957
            RSP: RSP_2894(ndk)
            RSH: Rsph17029_1538
            RSQ: Rsph17025_1127
            JAN: Jann_1822
            RDE: RD1_3111(ndk)
            PDE: Pden_1746
            MMR: Mmar10_1234
            HNE: HNE_2269(ndk)
            NAR: Saro_0894
            SAL: Sala_1759
            SWI: Swit_0030
            ELI: ELI_08860
            GOX: GOX1927
            GBE: GbCGDNIH1_2039
            ACR: Acry_1311
            RRU: Rru_A2169
            MAG: amb3561
            MGM: Mmc1_2992
            ABA: Acid345_3873
            SUS: Acid_3376
            BSU: BG10282(ndk)
            BHA: BH1654(ndk)
            BAN: BA1536
            BAR: GBAA1536
            BAA: BA_2056
            BAT: BAS1425
            BCE: BC1515
            BCA: BCE_1642
            BCZ: BCZK1397(ndk)
            BCY: Bcer98_1238
            BTK: BT9727_1397(ndk)
            BTL: BALH_1369
            BLI: BL02781(ndk)
            BLD: BLi02408(ndk)
            BCL: ABC1890(ndk)
            BAY: RBAM_020890
            BPU: BPUM_2004
            OIH: OB1787(ndk)
            GKA: GK2209(ndk)
            SAU: SA1301(ndk)
            SAV: SAV1469(ndk)
            SAM: MW1358(ndk)
            SAR: SAR1478(ndk)
            SAS: SAS1410
            SAC: SACOL1509
            SAB: SAB1331c
            SAA: SAUSA300_1358(ndk)
            SAO: SAOUHSC_01485
            SAJ: SaurJH9_1526
            SAH: SaurJH1_1556
            SEP: SE1156
            SER: SERP1037
            SHA: SH1445(ndk)
            SSP: SSP1277
            LMO: lmo1929(ndk)
            LMF: LMOf2365_1958(ndk)
            LIN: lin2043(ndk)
            LWE: lwe1955(ndk)
            SPZ: M5005_Spy_0670 M5005_Spy_0774 M5005_Spy_0775
            SPH: MGAS10270_Spy0728 MGAS10270_Spy0890 MGAS10270_Spy0891
            SPI: MGAS10750_Spy0761 MGAS10750_Spy0925 MGAS10750_Spy0926
            SPJ: MGAS2096_Spy0741 MGAS2096_Spy0847 MGAS2096_Spy0848
            SPK: MGAS9429_Spy0065(adk) MGAS9429_Spy0725 MGAS9429_Spy0889
                 MGAS9429_Spy0890
            SPA: M6_Spy0688 M6_Spy0794 M6_Spy0795
            SPB: M28_Spy0650
            SPN: SP_1959
            SPR: spr1775(ndk)
            SPD: SPD_1757(ndk)
            SAG: SAG0905(ndk)
            SAN: gbs0916(ndk)
            SAK: SAK_1021(ndk)
            STC: str0906(ndk)
            STL: stu0906(ndk)
            LPL: lp_0242(ndk)
            LSL: LSL_1414(adk) LSL_1936(ndk)
            LBR: LVIS_1367
            LCA: LSEI_0748
            LRE: Lreu_0202
            EFA: EF1036
            STH: STH1694
            CPE: CPE1972(ndk)
            CPF: CPF_2227
            CPR: CPR_1939
            CNO: NT01CX_0238
            CTH: Cthe_0716
            CBE: Cbei_4232
            CKL: CKL_1625(ndk)
            CHY: CHY_0215(ndk)
            DSY: DSY0202
            DRM: Dred_0127
            TTE: TTE0747(ndk)
            MTA: Moth_0106
            MTU: Rv2445c(ndkA)
            MTC: MT2521(ndk)
            MBO: Mb2472c(ndkA)
            MBB: BCG_2465c(ndkA)
            MLE: ML1469(ndk)
            MPA: MAP2268c(ndkA)
            MAV: MAV_1727
            MSM: MSMEG_4627
            MVA: Mvan_3948
            MGI: Mflv_2633
            MMC: Mmcs_3552
            MKM: Mkms_3625
            MJL: Mjls_3557
            CGL: NCgl2287(cgl2370)
            CGB: cg2603(ndk)
            CEF: CE2277
            CDI: DIP1783(ndk)
            CJK: jk0554(ndk)
            NFA: nfa13510(ndk)
            RHA: RHA1_ro01315(ndkA)
            SCO: SCO2612(ndk)
            SMA: SAV5454(ndkA)
            TWH: TWT475(ndkA)
            TWS: TW290(ndk)
            LXX: Lxx08000(ndk)
            ART: Arth_2395
            AAU: AAur_2371(ndk)
            PAC: PPA0823
            NCA: Noca_3466
            TFU: Tfu_2188
            FRA: Francci3_1210
            FAL: FRAAL1915(ndk)
            ACE: Acel_0747
            KRA: Krad_3490
            SEN: SACE_1401(ndk)
            STP: Strop_3489
            RXY: Rxyl_1532
            RBA: RB11832(ndk)
            CTR: CT500(ndk)
            CTA: CTA_0548(ndk)
            CMU: TC0787
            CPN: CPn0619(ndk)
            CPA: CP0128
            CPJ: CPj0619(ndk)
            CPT: CpB0645
            CCA: CCA00121(ndk)
            CAB: CAB120(ndk)
            CFE: CF0885(ndk)
            PCU: pc0366(ndk) pc0368(ndk)
            BBU: BB0463(ndk)
            BGA: BG0476(ndk)
            BAF: BAPKO_0492(ndk)
            TPA: TP1010
            LIL: LA4168
            LIC: LIC13326(ndk)
            LBJ: LBJ_2883(ndk)
            LBL: LBL_0180(ndk)
            SYN: sll1852(ndk)
            SYW: SYNW2358
            SYC: syc1609_d(ndk)
            SYF: Synpcc7942_2497
            SYD: Syncc9605_2512
            SYE: Syncc9902_2171
            SYG: sync_2741(ndk)
            SYR: SynRCC307_2377(ndk)
            SYX: SynWH7803_2388(ndk)
            CYA: CYA_1063(ndk)
            CYB: CYB_0270(ndk)
            TEL: tlr0267
            GVI: glr0710
            ANA: alr3402
            AVA: Ava_3424
            PMA: Pro0050(ndk)
            PMM: PMM0046
            PMT: PMT2148
            PMN: PMN2A_1379
            PMI: PMT9312_0047
            PMB: A9601_00471(ndk)
            PMC: P9515_00531(ndk)
            PMF: P9303_28301(ndk)
            PMG: P9301_00491(ndk)
            PMH: P9215_00561
            PME: NATL1_00601(ndk)
            TER: Tery_1141
            BTH: BT_3925
            BFR: BF3960
            BFS: BF3733
            SRU: SRU_1075(ndk)
            CHU: CHU_3648(ndk)
            GFO: GFO_0790(ndk)
            FJO: Fjoh_4976
            FPS: FP1409(ndk)
            CTE: CT2002(ndk)
            CCH: Cag_0204
            CPH: Cpha266_2368
            PVI: Cvib_0295
            PLT: Plut_0229
            DET: DET0394(ndk)
            DEH: cbdb_A343(ndk)
            DEB: DehaBAV1_0373
            RRS: RoseRS_0772
            RCA: Rcas_0034
            DRA: DR_2499
            DGE: Dgeo_1689
            TTH: TTC1798
            TTJ: TTHA0188
            AAE: aq_1590(ndk)
            TME: Tmel_0381
            FNO: Fnod_0038
            MMP: MMP0283(ndk)
            MMQ: MmarC5_1390
            MMZ: MmarC7_1286
            MAE: Maeo_0102
            MVN: Mevan_1295
            MAC: MA1524(ndk)
            MBA: Mbar_A3385
            MMA: MM_2464
            MBU: Mbur_0222
            MTP: Mthe_0334
            MHU: Mhun_1604
            MEM: Memar_0718
            MBN: Mboo_0687
            MST: Msp_0630(ndk)
            MSI: Msm_0203
            MKA: MK1591(ndk)
            HAL: VNG1160G(ndk)
            HMA: rrnAC0106(ndk)
            HWA: HQ2882A(ndk)
            NPH: NP3666A(ndk)
            TAC: Ta1113
            TVO: TVN0452
            PTO: PTO1283
            PAB: PAB1489(ndk)
            PFU: PF0931
            TKO: TK1307
            RCI: LRC143(ndk)
            APE: APE_2377
            SMR: Smar_0828
            IHO: Igni_0725
            HBU: Hbut_0549
            SSO: SSO0230(ndk)
            STO: ST0280
            SAI: Saci_0696
            MSE: Msed_0029
            PAI: PAE1561(ndk)
            PIS: Pisl_1626
            PCL: Pcal_0523
            PAS: Pars_0653
            NEQ: NEQ307
STRUCTURES  PDB: 1B4S  1B99  1BE4  1BHN  1BUX  1EHW  1F3F  1F6T  1HHQ  1HIY  
                 1HLW  1JXV  1K44  1KDN  1LEO  1LWX  1MN7  1MN9  1NB2  1NCL  
                 1NDC  1NDK  1NDL  1NDP  1NHK  1NLK  1NPK  1NSK  1NSP  1NSQ  
                 1NUE  1PAE  1PKU  1S57  1S59  1S5Z  1U8W  1UCN  1W7W  1WKJ  
                 1WKK  1WKL  1XIQ  1XQI  1ZS6  2AZ1  2AZ3  2B8P  2B8Q  2BEF  
                 2CWK  2DXD  2DXE  2DXF  2DY9  2DYA  2HUR  2HVD  2HVE  2NCK  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.6
            ExPASy - ENZYME nomenclature database: 2.7.4.6
            ExplorEnz - The Enzyme Database: 2.7.4.6
            ERGO genome analysis and discovery system: 2.7.4.6
            BRENDA, the Enzyme Database: 2.7.4.6
            CAS: 9026-51-1
///
ENTRY       EC 2.7.4.7                  Enzyme
NAME        phosphomethylpyrimidine kinase;
            hydroxymethylpyrimidine phosphokinase;
            ATP:4-amino-2-methyl-5-phosphomethylpyrimidine phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:(4-amino-2-methylpyrimidin-5-yl)methyl-phosphate
            phosphotransferase
REACTION    ATP + (4-amino-2-methylpyrimidin-5-yl)methyl phosphate = ADP +
            (4-amino-2-methylpyrimidin-5-yl)methyl diphosphate [RN:R04509]
ALL_REAC    R04509
SUBSTRATE   ATP [CPD:C00002];
            (4-amino-2-methylpyrimidin-5-yl)methyl phosphate
PRODUCT     ADP [CPD:C00008];
            (4-amino-2-methylpyrimidin-5-yl)methyl diphosphate
REFERENCE   1
  AUTHORS   Lewin, L.M. and Brown, G.M.
  TITLE     The biosynthesis of thiamine. III. Mechanism of enzymatic formation
            of the pyrophosphate ester of
            2-methyl-4-amino-5-hydroxymethylpyrimidine.
  JOURNAL   J. Biol. Chem. 236 (1961) 2768-2771.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00730  Thiamine metabolism
ORTHOLOGY   KO: K00941  phosphomethylpyrimidine kinase
GENES       ATH: AT1G22940(TH1)
            SCE: YOL055C(THI20) YPL258C(THI21)
            PIC: PICST_70077(THI20)
            CGR: CAGL0C05071g
            PFA: PFE1030c
            ECO: b2103(thiD)
            ECJ: JW2090(thiD)
            ECE: Z3267(thiD)
            ECS: ECs2906
            ECC: c2630(thiD)
            ECI: UTI89_C2377(thiD)
            ECP: ECP_2141
            ECW: EcE24377A_2391(thiD)
            ECX: EcHS_A2239(thiD)
            STY: STY2375(thiD)
            STT: t0710(thiD)
            SPT: SPA0706(thiD)
            SEC: SC2161(thiD)
            STM: STM2146(thiD)
            YPE: YPO2859(thiD)
            YPK: y1373(thiD)
            YPM: YP_2725(thiD)
            YPA: YPA_2299
            YPN: YPN_1278
            YPP: YPDSF_2209
            YPS: YPTB2824(thiD)
            YPI: YpsIP31758_1203(thiD)
            SFL: SF2165(thiD)
            SFX: S2290(thiD)
            SFV: SFV_2158(thiD)
            SSN: SSON_2151(thiD)
            SBO: SBO_0924(thiD)
            SDY: SDY_2277(thiD)
            ECA: ECA3196(thiD)
            PLU: plu2782(thiD)
            WBR: WGLp318(thiD)
            ENT: Ent638_2710
            SPE: Spro_3577
            HIN: HI0416(thiD)
            HIT: NTHI0541(thiD)
            HIP: CGSHiEE_00915
            HSO: HS_0091(thiD)
            PMU: PM1261(thiD)
            MSU: MS0677(thiD)
            APL: APL_0539(thiD)
            XFA: XF0621
            XFT: PD1534(thiD)
            XCC: XCC1735(thiD)
            XCB: XC_2499
            XCV: XCV1784(thiD)
            XAC: XAC1753(thiD)
            XOO: XOO2928(thiD)
            XOM: XOO_2780(XOO2780)
            VCH: VC1296
            VCO: VC0395_A0914(thiD)
            VVU: VV2_1433
            VVY: VVA0267
            VPA: VPA0136
            VFI: VFA0316
            PPR: PBPRB0688
            PAE: PA3975(thiD)
            PPU: PP_4782(thiD)
            PST: PSPTO_4798
            PSB: Psyr_4340
            PSP: PSPPH_4382
            PFL: PFL_5427(thiD)
            PFO: Pfl_4945
            PEN: PSEEN4802(thiD)
            PMY: Pmen_3772
            PAR: Psyc_0167(thiD)
            PCR: Pcryo_0179
            PRW: PsycPRwf_0828
            ACI: ACIAD0875(thiD)
            SON: SO_2444(thiDE)
            SDN: Sden_1771
            SFR: Sfri_2200
            SAZ: Sama_1859
            SBL: Sbal_2023
            SBM: Shew185_2322
            SLO: Shew_2095
            SPC: Sputcn32_1923
            SSE: Ssed_2014
            SPL: Spea_2382
            SHE: Shewmr4_1882
            SHM: Shewmr7_2096
            SHN: Shewana3_1937
            SHW: Sputw3181_2085
            ILO: IL0766(thiE)
            CPS: CPS_0254(thiDE)
            PHA: PSHAa0484(thiDE)
            PAT: Patl_1935
            SDE: Sde_0368 Sde_0829
            PIN: Ping_0361 Ping_2378
            MAQ: Maqu_0688
            CBU: CBU_0334(thiDE)
            CBD: COXBU7E912_1745(thiDE)
            LPN: lpg1568(thiDE)
            LPF: lpl1457(thiDE)
            LPP: lpp1526(thiDE)
            MCA: MCA0629
            TCX: Tcr_0143
            NOC: Noc_1265
            HHA: Hhal_0134
            CSA: Csal_3133 Csal_3302
            ABO: ABO_0356(thiD)
            MMW: Mmwyl1_2391
            BCI: BCI_0649(thiD)
            VOK: COSY_0854(thiD)
            NME: NMB1616
            NMA: NMA1815(thiD)
            NMC: NMC1538(thiD)
            NGO: NGO1160(thiD)
            CVI: CV_0151(thiD)
            RSO: RSc0100(thiD)
            REU: Reut_A0212
            REH: H16_A0243
            RME: Rmet_0169
            BMA: BMA1577(thiD) BMA2000
            BMV: BMASAVP1_A2080(thiD)
            BML: BMA10299_A3232(thiD)
            BMN: BMA10247_1352(thiD)
            BXE: Bxe_A1658 Bxe_A3814
            BVI: Bcep1808_1947
            BUR: Bcep18194_A3959 Bcep18194_A5350
            BCN: Bcen_0379 Bcen_6036
            BCH: Bcen2424_0861 Bcen2424_2041
            BAM: Bamb_2073
            BPS: BPSL2181(thiD) BPSL2696 BPSS1104
            BPM: BURPS1710b_2604(thiD) BURPS1710b_3174(thiD)
                 BURPS1710b_A0060(thiD2)
            BPL: BURPS1106A_2516(thiD) BURPS1106A_A1473(thiD)
            BPD: BURPS668_2460(thiD) BURPS668_A1561(thiD)
            BTE: BTH_I1459 BTH_I2005(thiD) BTH_II1305
            PNU: Pnuc_0889
            BPE: BP0317(thiD) BP3598(thiD)
            BPA: BPP3934(thiD) BPP3987(thiD)
            BBR: BB4407(thiD) BB4460(thiD)
            RFR: Rfer_2470
            POL: Bpro_1134 Bpro_2331
            PNA: Pnap_2435
            AAV: Aave_3067
            VEI: Veis_4315
            MPT: Mpe_A1606
            HAR: HEAR2263(thiD) HEAR2749(thiD-like)
            MMS: mma_1216(thiD1) mma_2958(thiD2)
            NEU: NE1425(thiD)
            NET: Neut_1539
            NMU: Nmul_A2627
            EBA: ebA1711(thiD) ebA1745(thiD)
            AZO: azo0841(thiD1) azo3451(thiD2)
            DAR: Daro_3900
            TBD: Tbd_2555
            MFA: Mfla_0853 Mfla_0997 Mfla_2662
            HPY: HP0844(thi)
            HPJ: jhp0782(thiD)
            HPA: HPAG1_0829 HPAG1_1226
            WSU: WS0787
            CJE: Cj1082c(thiD)
            CJR: CJE1225(thiD)
            CJJ: CJJ81176_1100(thiD)
            CJU: C8J_1023(thiD)
            CJD: JJD26997_0641(thiD)
            CFF: CFF8240_0969(thiD)
            CCV: CCV52592_0496(thiD)
            CHA: CHAB381_1498(thiD)
            CCO: CCC13826_0361(thiD) CCC13826_0399(thiD) CCC13826_0950(thiD)
                 CCC13826_1843(thiD)
            ABU: Abu_1756(thiD)
            SUN: SUN_0531(thiD)
            GSU: GSU0605
            GME: Gmet_2909
            PCA: Pcar_2235
            DVU: DVU0931(thiD)
            DDE: Dde_2688
            LIP: LI0782(thiD)
            DPS: DP0916(thiD)
            ADE: Adeh_0077 Adeh_2049
            AFW: Anae109_0077 Anae109_1765
            MXA: MXAN_2287(thiD)
            SAT: SYN_01521
            SFU: Sfum_1692
            AMA: AM295(thiD)
            APH: APH_0993(thiD)
            ERU: Erum1910(thiD)
            ERW: ERWE_CDS_01920(thiD)
            ERG: ERGA_CDS_01870(thiD)
            ECN: Ecaj_0192
            ECH: ECH_0914(thiD)
            PUB: SAR11_0604(thiD)
            MLO: mll5788
            MES: Meso_2566
            SME: SMb20962(thiD)
            SMD: Smed_4962
            ATU: Atu3290(thiD)
            ATC: AGR_L_3056
            RET: RHE_PE00335(thiD)
            RLE: pRL110441(thiD)
            BME: BMEI1732
            BMF: BAB1_0219
            BMS: BR0218(thiD)
            BMB: BruAb1_0213(thiD)
            BOV: BOV_0209(thiD)
            OAN: Oant_0285
            BJA: bll5905(thiD)
            BRA: BRADO5133(thiD)
            BBT: BBta_5600(thiD)
            RPA: RPA3971(thiD)
            RPB: RPB_1617
            RPC: RPC_1443
            RPD: RPD_1628
            RPE: RPE_1463
            NWI: Nwi_1082
            NHA: Nham_1310
            BHE: BH04860(thiD1) BH16280(thiD2)
            BQU: BQ04060(thiD1) BQ13200(thiD2)
            BBK: BARBAKC583_0441(thiD)
            XAU: Xaut_4453
            CCR: CC_3223
            SIL: SPO0045(thiD)
            SIT: TM1040_3649
            RSP: RSP_0647(thiD)
            RSH: Rsph17029_2300
            RSQ: Rsph17025_0585
            RDE: RD1_0746(thiD) RD1_3611(thiDE) RD1_3612(thiD)
            PDE: Pden_0042
            MMR: Mmar10_0552
            HNE: HNE_3234(thiD)
            ZMO: ZMO1003(thiD)
            NAR: Saro_0479
            SAL: Sala_0962
            SWI: Swit_0082
            ELI: ELI_10255
            GOX: GOX2230(thiD)
            GBE: GbCGDNIH1_1113
            RRU: Rru_A1102
            MAG: amb3197
            MGM: Mmc1_0014
            ABA: Acid345_2592
            SUS: Acid_1226
            BSU: BG10598(thiD) BG13151(yjbV)
            BHA: BH1435
            BAN: BA0734(thiD-1)
            BAR: GBAA0734(thiD-1)
            BAA: BA_1322(pfkB)
            BAT: BAS0700
            BCE: BC0751
            BCA: BCE_0804(thiD)
            BCZ: BCZK0644(thiD) BCZK5110(thiD)
            BTK: BT9727_0644(thiD)
            BTL: BALH_0671(thiD) BALH_4913(thiD)
            BLI: BL01586(thiDA) BL03951(thiD)
            BLD: BLi01265(yjbV) BLi04014(thiD)
            BCL: ABC1627 ABC1737 ABC3932(thiD)
            BAY: RBAM_035260(thiD)
            BPU: BPUM_1100(thiDA) BPUM_3448(thiD)
            OIH: OB0474
            GKA: GK1510 GK3450
            SAU: SA0537(thiD) SA1896(thiD)
            SAV: SAV0580 SAV2093(thiD)
            SAM: MW0535 MW2016(thiD)
            SAR: SAR0585 SAR2182(thiD)
            SAS: SAS0538 SAS1997
            SAC: SACOL0626(thiD1) SACOL2085(thiD2)
            SAB: SAB0530c SAB1977c(thiD)
            SAA: SAUSA300_0562(thiD) SAUSA300_2049(thiD)
            SAO: SAOUHSC_00562 SAOUHSC_02330
            SEP: SE0349 SE1692
            SER: SERP0226(thiD-1) SERP1700(thiD-2)
            SHA: SH0941(thiD) SH2412(thiD)
            SSP: SSP0790 SSP2135
            LMO: lmo0317
            LMF: LMOf2365_0335(thiD-1)
            LIN: lin0342
            LWE: lwe0288 lwe0630(thiD)
            LLA: L0200(thiD1) L0202(thiD2)
            LLC: LACR_0492 LACR_1376
            LLM: llmg_0463(thiD2) llmg_1217(thiD1)
            SPY: SPy_1900(thiD)
            SPZ: M5005_Spy_1616(thiD)
            SPM: spyM18_1965(thiD)
            SPG: SpyM3_1638(thiD)
            SPS: SPs0228
            SPH: MGAS10270_Spy1684(thiD)
            SPI: MGAS10750_Spy1671(thiD)
            SPJ: MGAS2096_Spy1640(thiD)
            SPK: MGAS9429_Spy1619(thiD)
            SPA: M6_Spy1624
            SPB: M28_Spy1605(thiD)
            SPN: SP_0726 SP_1598
            SPR: spr0638(thiD) spr1450(pdxK)
            SPD: SPD_0632(thiD)
            SAG: SAG0101 SAG0840(thiD)
            SAN: gbs0100 gbs0858
            SAK: SAK_0151 SAK_0963(thiD)
            SMU: SMU.85(thiD)
            STC: str0123(thiD)
            STL: stu0123(thiD)
            SSA: SSA_2001(thiD)
            SGO: SGO_0409
            LPL: lp_0114(thiD)
            LJO: LJ0515
            LAC: LBA1879(thiD)
            LSA: LSA0058(thiD) LSA0980
            LSL: LSL_1583(thiD)
            LBR: LVIS_1934 LVIS_2098
            LCA: LSEI_0301 LSEI_0695
            EFA: EF1969 EF2775(thiD)
            OOE: OEOE_1368
            STH: STH156
            CAC: CAC3095(thiK)
            CPE: CPE1338(thiD)
            CPF: CPF_1545(thiD)
            CPR: CPR_1338(thiD)
            CTC: CTC01753
            CNO: NT01CX_0246(thiD)
            CDF: CD1599(thiD)
            CBO: CBO0451(thiD1) CBO0771(thiD2)
            CBA: CLB_0492(thiD-1) CLB_0813(thiD-2)
            CBH: CLC_0525(thiD-1) CLC_0827(thiD-2)
            CBF: CLI_0536(thiD-1) CLI_0857(thiD-2)
            CKL: CKL_2919(thiD)
            DSY: DSY1405
            SWO: Swol_0639
            CSC: Csac_0256
            TTE: TTE2235(thiD)
            MTU: Rv0422c(thiD)
            MTC: MT0436(thiD)
            MBO: Mb0430c(thiD)
            MBB: BCG_0461c(thiD)
            MLE: ML0295(thiD)
            MPA: MAP3912c(thiD)
            MAV: MAV_4732(thiD)
            MSM: MSMEG_0464 MSMEG_0825(thiD)
            MVA: Mvan_0724
            MMC: Mmcs_0564
            MKM: Mkms_0576
            MJL: Mjls_0554
            CGL: NCgl1407(cgl1463)
            CGB: cg1654(thiD1) cg3409(thiD2)
            CEF: CE1591
            CDI: DIP0035(thiD)
            CJK: jk0297(thiD)
            NFA: nfa53190(thiD)
            RHA: RHA1_ro02183(thiD)
            SCO: SCO5563(SC7A1.07)
            SMA: SAV7205(thiD)
            ART: Arth_0593 Arth_2392
            AAU: AAur_2368(thiD)
            PAC: PPA0110
            NCA: Noca_3401
            TFU: Tfu_2250
            FRA: Francci3_3612
            FAL: FRAAL5819(thiD)
            ACE: Acel_1583
            KRA: Krad_0854
            SEN: SACE_0510(thiD) SACE_1297(thiD)
            STP: Strop_3884
            BLO: BL0113(thiD)
            BAD: BAD_1146(thiD)
            RXY: Rxyl_2791
            FNU: FN1759
            RBA: RB7580(thiD)
            LIL: LA0130(thiD)
            LIC: LIC10118(thiD)
            LBJ: LBJ_0114(thiD)
            SYC: syc1726_c(thiD)
            SYF: Synpcc7942_2379
            CYA: CYA_0287(thiD)
            CYB: CYB_2833(thiD)
            GVI: glr1511
            ANA: all3540
            AVA: Ava_3519
            PMM: PMM0358(thiD)
            PMI: PMT9312_0362
            PMB: A9601_03951(thiD)
            PMC: P9515_04031(thiD)
            PMG: P9301_03941(thiD)
            PMH: P9215_04001(thiD)
            TER: Tery_3765
            BTH: BT_0790
            BFR: BF2259
            BFS: BF2353(thiD)
            SRU: SRU_1237(thiD)
            CHU: CHU_0241(thiD)
            FJO: Fjoh_1601
            FPS: FP0430(thiD)
            CTE: CT1176(thiD)
            CCH: Cag_0817
            CPH: Cpha266_1533
            PVI: Cvib_0944
            PLT: Plut_0957
            DRA: DR_A0171
            DGE: Dgeo_1919
            TTH: TTC0321
            TTJ: TTHA0680
            AAE: aq_1960(thiD)
            TMA: TM0790
            MJA: MJ0236
            MMP: MMP1639
            MMQ: MmarC5_1769
            MMZ: MmarC7_0912
            MAE: Maeo_0460
            MVN: Mevan_0944
            MAC: MA3197(thiD)
            MBA: Mbar_A3501
            MMA: MM_0338
            MBU: Mbur_2182
            MHU: Mhun_1140
            MEM: Memar_1226
            MST: Msp_1007(thiD)
            MKA: MK0589(thiD)
            AFU: AF2208(thiD)
            HAL: VNG2606G(thiD)
            HMA: rrnAC2449(thiD)
            HWA: HQ2657A(thiD)
            NPH: NP0546A(thiD)
            TAC: Ta1281
            TVO: TVN0513
            PTO: PTO1290
            PHO: PH1155
            PAB: PAB1646(thiD)
            PFU: PF1333
            TKO: TK0435
            RCI: RCIX1833(thiD)
            APE: APE_2400.1
            SSO: SSO0002(thiD-1) SSO2393(thiD-2)
            STO: ST0526 ST2329
            SAI: Saci_0273(thiD) Saci_0953
            MSE: Msed_0184
            PAI: PAE2535
STRUCTURES  PDB: 1JXH  1JXI  1UB0  2I5B  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.7
            ExPASy - ENZYME nomenclature database: 2.7.4.7
            ExplorEnz - The Enzyme Database: 2.7.4.7
            ERGO genome analysis and discovery system: 2.7.4.7
            BRENDA, the Enzyme Database: 2.7.4.7
            CAS: 37278-18-5
///
ENTRY       EC 2.7.4.8                  Enzyme
NAME        guanylate kinase;
            deoxyguanylate kinase;
            5'-GMP kinase;
            GMP kinase;
            guanosine monophosphate kinase;
            ATP:GMP phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:(d)GMP phosphotransferase
REACTION    ATP + GMP = ADP + GDP [RN:R00332]
ALL_REAC    R00332;
            (other) R02090
SUBSTRATE   ATP [CPD:C00002];
            GMP [CPD:C00144]
PRODUCT     ADP [CPD:C00008];
            GDP [CPD:C00035]
COMMENT     dGMP can also act as acceptor, and dATP can act as donor.
REFERENCE   1  [PMID:4307347]
  AUTHORS   Buccino RJ Jr, Roth JS.
  TITLE     Partial purification and properties of ATP:GMP phosphransferase from
            rat liver.
  JOURNAL   Arch. Biochem. Biophys. 132 (1969) 49-61.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:5329274]
  AUTHORS   Hiraga S, Sugino Y.
  TITLE     Nucleoside monophosphokinases of Escherichia coli infected and
            uninfected with an RNA phage.
  JOURNAL   Biochim. Biophys. Acta. 114 (1966) 416-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:5862227]
  AUTHORS   Griffith TJ, Helleiner CW.
  TITLE     The partial purification of deoxynucleoside monophosphate kinases
            from L cells.
  JOURNAL   Biochim. Biophys. Acta. 108 (1965) 114-24.
  ORGANISM  mouse [GN:mmu]
REFERENCE   4  [PMID:5333666]
  AUTHORS   Oeschger MP, Bessman MJ.
  TITLE     Purification and properties of guanylate kinase from Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 241 (1966) 5452-60.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:5552394]
  AUTHORS   Shimono H, Sugino Y.
  TITLE     Metabolism of deoxyribonucleotides. Purification and properties of
            deoxyguanosine monophosphokinase of calf thymus.
  JOURNAL   Eur. J. Biochem. 19 (1971) 256-63.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K00942  guanylate kinase
GENES       HSA: 2987(GUK1)
            MMU: 14923(Guk1)
            RNO: 303179(Guk1)
            CFA: 475178(GUK1)
            BTA: 281217(GUK1)
            GGA: 428399(GUK1)
            XLA: 446642(MGC82526) 447035(guk1)
            XTR: 493514(MGC89895)
            DRE: 393697(guk1)
            SPU: 586667(LOC586667)
            DME: Dmel_CG11811 Dmel_CG1725(dlg1) Dmel_CG30021(skf)
                 Dmel_CG30388(Magi) Dmel_CG31349(pyd) Dmel_CG32717(sdt)
            CEL: T03F1.8
            ATH: AT3G06200
            OSA: 4332674
            CME: CMD076C CMI041C
            SCE: YDR454C(GUK1)
            AGO: AGOS_AER309W
            PIC: PICST_72675(GUK1)
            CGR: CAGL0K06281g
            SPO: SPBC1198.05
            AFM: AFUA_1G08840
            CNE: CND04800
            ECU: ECU01_1220
            DDI: DDB_0230100(gmkA)
            PFA: PFI1420w
            CPV: cgd7_2190
            TAN: TA13945
            TPV: TP02_0576
            TET: TTHERM_00624830 TTHERM_00781030
            TBR: Tb10.26.0200 Tb10.6k15.3960
            TCR: 509647.70
            LMA: LmjF33.1090
            EHI: 62.t00003
            ECO: b3648(gmk)
            ECJ: JW3623(gmk)
            ECE: Z5074(gmk)
            ECS: ECs4523
            ECC: c4473(gmk)
            ECI: UTI89_C4193(gmk)
            ECP: ECP_3746
            ECV: APECO1_2813(gmk)
            ECW: EcE24377A_4151(gmk)
            ECX: EcHS_A3859(gmk)
            STY: STY4052(gmk)
            STT: t3778(gmk)
            SPT: SPA3592(gmk)
            SEC: SC3664(gmk)
            STM: STM3740(gmk)
            YPE: YPO0040(gmk)
            YPK: y0101(gmk)
            YPM: YP_0041(gmk)
            YPA: YPA_3502
            YPN: YPN_3810
            YPP: YPDSF_3865
            YPS: YPTB0037(gmk)
            YPI: YpsIP31758_0041(gmk)
            YEN: YE0047(gmk)
            SFL: SF3688(gmk)
            SFX: S4081(gmk)
            SFV: SFV_3881(gmk)
            SSN: SSON_3757(gmk)
            SBO: SBO_3729(gmk)
            SDY: SDY_4080(gmk)
            ECA: ECA0040(gmk)
            PLU: plu0274(gmk)
            BUC: BU434(gmk)
            BAS: BUsg419(gmk)
            BAB: bbp385(gmk)
            WBR: WGLp406(gmk)
            SGL: SG2221
            ENT: Ent638_0091
            KPN: KPN_03996(gmk)
            SPE: Spro_4867
            BFL: Bfl616(gmk)
            BPN: BPEN_641(gmk)
            HIN: HI1743(gmk)
            HIT: NTHI2054(gmk)
            HIP: CGSHiEE_03320(gmk)
            HIQ: CGSHiGG_02475(gmk)
            HDU: HD1830(gmk)
            HSO: HS_1457(gmk)
            PMU: PM0922(gmk)
            MSU: MS1738(gmk)
            APL: APL_0256(gmk)
            ASU: Asuc_1026
            XFA: XF1503
            XFT: PD0720(gmk)
            XCC: XCC3249(gmk)
            XCB: XC_0958
            XCV: XCV3512(gmk)
            XAC: XAC3395(gmk)
            XOO: XOO1145(gmk)
            XOM: XOO_1042(XOO1042)
            VCH: VC2708
            VCO: VC0395_A2280(gmk)
            VVU: VV1_0850
            VVY: VV0243
            VPA: VP0161
            VFI: VF0106
            PPR: PBPRA0191(gmk)
            PAE: PA5336(gmk)
            PAU: PA14_70440(gmk)
            PAP: PSPA7_6112(gmk)
            PPU: PP_5296(gmk-2)
            PPF: Pput_5204
            PST: PSPTO_0075(gmk)
            PSB: Psyr_0211(gmk)
            PSP: PSPPH_0199(gmk)
            PFL: PFL_6061(gmk)
            PFO: Pfl_5549(gmk)
            PEN: PSEEN5441(gmk)
            PMY: Pmen_4388
            PAR: Psyc_1723(gmk)
            PCR: Pcryo_2003
            PRW: PsycPRwf_0577
            ACI: ACIAD3324(gmk)
            ACB: A1S_3170
            SON: SO_0361(gmk)
            SDN: Sden_3433
            SFR: Sfri_0365
            SAZ: Sama_0266
            SBL: Sbal_0355
            SBM: Shew185_0353
            SLO: Shew_3497
            SPC: Sputcn32_3630
            SSE: Ssed_0336
            SPL: Spea_3877
            SHE: Shewmr4_3613
            SHM: Shewmr7_0330
            SHN: Shewana3_3810
            SHW: Sputw3181_3770
            ILO: IL2382(gmk)
            CPS: CPS_4971(gmk)
            PHA: PSHAa2790(gmk)
            PAT: Patl_0347
            SDE: Sde_3695
            PIN: Ping_3623
            MAQ: Maqu_0634
            CBU: CBU_0301(gmk)
            CBD: COXBU7E912_1780(gmk)
            LPN: lpg2010(gmk)
            LPF: lpl1987(gmk)
            LPP: lpp1992(gmk)
            MCA: MCA2975(gmk)
            FTU: FTT1470c(gmk)
            FTF: FTF1470c(gmk)
            FTW: FTW_0628(gmk)
            FTL: FTL_1391
            FTH: FTH_1353(gmk)
            FTA: FTA_1478
            FTN: FTN_0691(gmk)
            TCX: Tcr_2138
            NOC: Noc_1212
            AEH: Mlg_2444
            HHA: Hhal_0976
            HCH: HCH_06315
            CSA: Csal_3233
            ABO: ABO_0178(gmk-2)
            MMW: Mmwyl1_4384
            AHA: AHA_0041
            BCI: BCI_0110(gmk)
            RMA: Rmag_0559
            VOK: COSY_0513(gmk)
            NME: NMB1661
            NMA: NMA1919(gmk)
            NMC: NMC1579(gmk)
            NGO: NGO1310
            CVI: CV_3770(gmk)
            RSO: RSc2155(gmk)
            REU: Reut_A2473
            REH: H16_A0953(gmk)
            RME: Rmet_0856
            BMA: BMA2096(gmk)
            BMV: BMASAVP1_A0815(gmk)
            BML: BMA10299_A2648(gmk)
            BMN: BMA10247_1964(gmk)
            BXE: Bxe_A0905
            BVI: Bcep1808_0916
            BUR: Bcep18194_A4107
            BCN: Bcen_0520
            BCH: Bcen2424_0999
            BAM: Bamb_0859
            BPS: BPSL2563(gmk)
            BPM: BURPS1710b_3049(gmk)
            BPL: BURPS1106A_3015(gmk)
            BPD: BURPS668_2949(gmk)
            BTE: BTH_I1586
            PNU: Pnuc_1078
            BPE: BP1578(gmK)
            BPA: BPP3005(gmK)
            BBR: BB2971(gmk)
            RFR: Rfer_3147
            POL: Bpro_1335
            PNA: Pnap_0811
            AAV: Aave_3583
            AJS: Ajs_0947
            VEI: Veis_4218
            MPT: Mpe_A2715
            HAR: HEAR2130(gmk)
            MMS: mma_1328(gmk)
            NEU: NE2254(gmk)
            NET: Neut_0614
            NMU: Nmul_A0052
            EBA: ebA3494(gmk)
            AZO: azo3953(gmk)
            DAR: Daro_3845
            TBD: Tbd_0473
            MFA: Mfla_0048
            HPY: HP0321
            HPA: HPAG1_0324
            HHE: HH0707(gmk)
            HAC: Hac_1000(gmk)
            WSU: WS0188
            TDN: Tmden_1796
            CJE: Cj1177c(gmk)
            CJR: CJE1311
            CJU: C8J_1121(gmk)
            CFF: CFF8240_1436
            CCV: CCV52592_1256(gmk)
            CHA: CHAB381_1251(gmk)
            CCO: CCC13826_0545(gmk) CCC13826_1537
            ABU: Abu_0544(gmk)
            NIS: NIS_1497(gmk)
            SUN: SUN_2210(gmk)
            GSU: GSU2238(gmk)
            GME: Gmet_2327
            GUR: Gura_3162
            PCA: Pcar_1285
            PPD: Ppro_2401
            DVU: DVU0900(gmk)
            DVL: Dvul_2084
            DDE: Dde_2719
            LIP: LI0310(gmk)
            BBA: Bd1568(gmk)
            DPS: DP2860
            ADE: Adeh_2606
            AFW: Anae109_2573
            MXA: MXAN_4705(gmk)
            SAT: SYN_01279
            SFU: Sfum_3630
            RPR: RP765(gmk)
            RTY: RT0752(gmk)
            RCO: RC1194(gmk)
            RFE: RF_1229(gmk)
            RBE: RBE_0134(gmk)
            RAK: A1C_05985(gmk)
            RBO: A1I_07245(gmk)
            RCM: A1E_04945(gmk)
            RRI: A1G_06535(gmk)
            OTS: OTBS_0788(gmpK)
            WOL: WD0439(gmk)
            WBM: Wbm0580
            AMA: AM177(gmk)
            APH: APH_0170(gmk)
            ERU: Erum6740(gmk)
            ERW: ERWE_CDS_07070(gmk)
            ERG: ERGA_CDS_06990(gmk)
            ECN: Ecaj_0681
            ECH: ECH_0322(gmk)
            NSE: NSE_0726(gmk)
            PUB: SAR11_0709(gmk)
            MLO: mlr7857
            MES: Meso_1763
            PLA: Plav_3354
            SME: SMc00577(gmk)
            SMD: Smed_0759
            ATU: Atu1101(gmk)
            ATC: AGR_C_2038
            RET: RHE_CH01448(gmk2)
            RLE: RL1563(gmk)
            BME: BMEI1469
            BMF: BAB1_0489(gmk)
            BMS: BR0464(gmk)
            BMB: BruAb1_0486(gmk)
            BOV: BOV_0469(gmk)
            OAN: Oant_0576
            BJA: blr4088(gmk)
            BRA: BRADO3317(gmk)
            BBT: BBta_3823(gmk)
            RPA: RPA3069(kguA)
            RPB: RPB_2472
            RPC: RPC_2305
            RPD: RPD_2974
            RPE: RPE_3301
            NWI: Nwi_1683
            NHA: Nham_2348
            BHE: BH05390(gmk)
            BQU: BQ04570(gmk)
            BBK: BARBAKC583_0502
            XAU: Xaut_3136
            CCR: CC_1681
            SIL: SPO1945(gmk)
            SIT: TM1040_1266
            RSP: RSP_2919
            RSH: Rsph17029_1563
            RSQ: Rsph17025_1104
            JAN: Jann_2440
            RDE: RD1_2638
            PDE: Pden_3936
            MMR: Mmar10_1220
            HNE: HNE_2153
            ZMO: ZMO0433(gmk)
            NAR: Saro_1003
            SAL: Sala_3155
            SWI: Swit_2714
            ELI: ELI_09585
            GOX: GOX0989
            GBE: GbCGDNIH1_2205
            ACR: Acry_1447
            RRU: Rru_A0429
            MAG: amb0748
            MGM: Mmc1_0251
            ABA: Acid345_3778
            SUS: Acid_2353
            BSU: BG13386(gmk)
            BHA: BH2512(gmk)
            BAN: BA4009
            BAR: GBAA4009
            BAA: BA_4480
            BAT: BAS3722
            BCE: BC3869(gmk)
            BCA: BCE_3914
            BCZ: BCZK3630(gmk)
            BCY: Bcer98_2523
            BTK: BT9727_3612(gmk)
            BLI: BL02293(gmk)
            BLD: BLi01789(gmk)
            BCL: ABC2322(gmk)
            BAY: RBAM_015510(gmk)
            BPU: BPUM_1467(gmk)
            OIH: OB1502
            GKA: GK1167(gmk)
            SAU: SA1052(gmk)
            SAV: SAV1209(gmk)
            SAM: MW1092(gmk)
            SAR: SAR1185
            SAS: SAS1143
            SAC: SACOL1221(gmk)
            SAB: SAB1073(gmk)
            SAA: SAUSA300_1102(gmk)
            SAO: SAOUHSC_01176
            SAJ: SaurJH9_1268
            SAH: SaurJH1_1293
            SEP: SE0885
            SER: SERP0776(gmk)
            SHA: SH1705
            SSP: SSP1562
            LMO: lmo1827
            LMF: LMOf2365_1855
            LIN: lin1941
            LWE: lwe1846
            LLA: L149828(gmk)
            LLC: LACR_2158
            LLM: llmg_2155(gmk)
            SPY: SPy_1632(gmk)
            SPZ: M5005_Spy_1341(gmk)
            SPM: spyM18_1642(gmk)
            SPG: SpyM3_1375(gmk)
            SPS: SPs0487
            SPH: MGAS10270_Spy1457(gmk)
            SPI: MGAS10750_Spy1450(gmk)
            SPJ: MGAS2096_Spy1362(gmk)
            SPK: MGAS9429_Spy1336(gmk)
            SPF: SpyM50450(gmk)
            SPA: M6_Spy1387
            SPB: M28_Spy1382(gmk)
            SPN: SP_1738
            SPR: spr1583(gmk)
            SPD: SPD_1548(gmk)
            SAG: SAG0313(gmk)
            SAN: gbs0301
            SAK: SAK_0383(gmk)
            SMU: SMU.478(kguA)
            STC: str1431(gmk)
            STL: stu1431(gmk)
            STE: STER_1398
            SSA: SSA_1851(gmk)
            SSU: SSU05_0422
            SSV: SSU98_0409
            SGO: SGO_0594(gmk)
            LPL: lp_0866(gmk2) lp_1612(gmk1)
            LJO: LJ0596 LJ1543
            LAC: LBA1325 LBA1745
            LSA: LSA0107(gmk1) LSA0685(gmk2)
            LSL: LSL_0611(gmk)
            LDB: Ldb1415(gmk1) Ldb2023(gmk2)
            LBU: LBUL_1312 LBUL_1870
            LCA: LSEI_1629 LSEI_2027
            LGA: LGAS_0758
            LRE: Lreu_1176
            PPE: PEPE_0825
            EFA: EF2595(gmk-1) EF3127(gmk-2)
            OOE: OEOE_1231 OEOE_1432
            STH: STH1339
            CAC: CAC1718
            CPE: CPE1748(gmk)
            CPF: CPF_2001(gmk)
            CPR: CPR_1719(gmk)
            CTC: CTC01216
            CNO: NT01CX_2249
            CTH: Cthe_1315
            CDF: CD2588(gmk)
            CBO: CBO2513(gmk)
            CBA: CLB_2387(gmk)
            CBH: CLC_2369(gmk)
            CBF: CLI_2575(gmk)
            CBE: Cbei_1141
            CKL: CKL_2842(gmk)
            AMT: Amet_2790
            CHY: CHY_1488(gmk)
            DSY: DSY2729
            DRM: Dred_1700
            SWO: Swol_1237
            CSC: Csac_2086
            TTE: TTE1511(gmk)
            MTA: Moth_2099
            MGE: MG_107(gmk)
            MPN: MPN246(gmk)
            MPU: MYPU_6870(gmk)
            MPE: MYPE5640(gmk)
            MGA: MGA_0462(gmk)
            MMY: MSC_0218(gmk)
            MMO: MMOB5570(gmk)
            MHY: mhp229(gmk)
            MHJ: MHJ_0149(gmk)
            MHP: MHP7448_0153(gmk)
            MSY: MS53_0123(gmk)
            MCP: MCAP_0208(gmk)
            UUR: UU213(gmk)
            POY: PAM737(gmk)
            AYW: AYWB_655(gmk)
            MFL: Mfl195
            MTU: Rv1389(gmk)
            MTC: MT1434(gmk)
            MBO: Mb1424(gmk)
            MBB: BCG_1450(gmk)
            MLE: ML0541(gmk)
            MPA: MAP1123(gmk)
            MAV: MAV_3385
            MSM: MSMEG_3051
            MVA: Mvan_2667
            MGI: Mflv_3740
            MMC: Mmcs_2370
            MKM: Mkms_2417
            MJL: Mjls_2411
            CGL: NCgl1544(cgl1606)
            CGB: cg1810(gmk)
            CEF: CE1726
            CDI: DIP1328(gmk)
            CJK: jk1019(gmk)
            NFA: nfa36160(gmk)
            RHA: RHA1_ro07155(gmk)
            SCO: SCO1479(SC9C5.03c)
            SMA: SAV6871(gmk)
            TWH: TWT363(gmk)
            TWS: TW406(gmk)
            LXX: Lxx11120(gmk)
            CMI: CMM_1780(gmkA)
            ART: Arth_2259
            PAC: PPA1190
            NCA: Noca_2436
            TFU: Tfu_1062
            FRA: Francci3_3195
            FAL: FRAAL0810 FRAAL5231(gmk)
            ACE: Acel_1293
            KRA: Krad_2992
            SEN: SACE_2100(gmk)
            BLO: BL0070
            BAD: BAD_0538
            RXY: Rxyl_1473
            FNU: FN2033
            RBA: RB7090(gmk)
            CTR: CT030(gmk)
            CTA: CTA_0032(gmk)
            CMU: TC0299
            CPN: CPn0120(gmk)
            CPA: CP0653
            CPJ: CPj0120(gmk)
            CPT: CpB0121
            CCA: CCA00653(gmk)
            CAB: CAB624
            CFE: CF0358(gmk)
            PCU: pc0662(gmk)
            LIL: LA2598
            LBJ: LBJ_1615(gmk)
            LBL: LBL_1833(gmk)
            SYN: slr1123(gmk)
            SYW: SYNW1837(gmk)
            SYC: syc0359_c
            SYF: Synpcc7942_1191
            SYD: Syncc9605_0632
            SYE: Syncc9902_1730
            SYG: sync_2153
            SYR: SynRCC307_0708(gmk)
            SYX: SynWH7803_1846(gmk)
            CYA: CYA_2697
            CYB: CYB_0056
            TEL: tll0054
            GVI: gll1621
            ANA: alr0106
            AVA: Ava_1475
            PMA: Pro0465(gmk)
            PMM: PMM0467(gmk)
            PMT: PMT1318(gmk)
            PMN: PMN2A_1799
            PMI: PMT9312_0467
            PMB: A9601_05231(gmk)
            PMC: P9515_05311(gmk)
            PMF: P9303_06681(gmk)
            PMG: P9301_04921(gmk)
            PMH: P9215_05471(gmk)
            PME: NATL1_05221(gmk)
            TER: Tery_2834
            BTH: BT_2009
            BFR: BF3707
            BFS: BF3500(gmk)
            PGI: PG0512(gmk)
            SRU: SRU_0030
            CHU: CHU_0599(gmk)
            GFO: GFO_3432(gmk)
            FJO: Fjoh_0742
            FPS: FP0348(gmk)
            CTE: CT0247(gmk)
            CCH: Cag_1456
            CPH: Cpha266_0375
            PVI: Cvib_1555
            PLT: Plut_1773
            DET: DET0035(gmk)
            DEH: cbdb_A42(gmk)
            DEB: DehaBAV1_0032
            RRS: RoseRS_3599
            RCA: Rcas_4286
            DRA: DR_2289
            DGE: Dgeo_2284
            TTH: TTC1197
            TTJ: TTHA1562
            AAE: aq_184
            TMA: TM1689
            TPT: Tpet_0985
            TME: Tmel_0099
            FNO: Fnod_1677
STRUCTURES  PDB: 1EX6  1EX7  1GKY  1LVG  1S4Q  1S96  1Z6G  1Z8F  1ZNW  1ZNX  
                 1ZNY  1ZNZ  2AN9  2ANB  2ANC  2F3R  2F3T  2J41  2QOR  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.8
            ExPASy - ENZYME nomenclature database: 2.7.4.8
            ExplorEnz - The Enzyme Database: 2.7.4.8
            ERGO genome analysis and discovery system: 2.7.4.8
            BRENDA, the Enzyme Database: 2.7.4.8
            CAS: 9026-59-9
///
ENTRY       EC 2.7.4.9                  Enzyme
NAME        dTMP kinase;
            thymidine monophosphate kinase;
            thymidylate kinase;
            thymidylate monophosphate kinase;
            thymidylic acid kinase;
            thymidylic kinase;
            deoxythymidine 5'-monophosphate kinase;
            TMPK;
            thymidine 5'-monophosphate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:dTMP phosphotransferase
REACTION    ATP + dTMP = ADP + dTDP [RN:R02094]
ALL_REAC    R02094;
            (other) R02098
SUBSTRATE   ATP [CPD:C00002];
            dTMP [CPD:C00364]
PRODUCT     ADP [CPD:C00008];
            dTDP [CPD:C00363]
REFERENCE   1
  AUTHORS   Hurwitz, J.
  TITLE     The enzymatic incorporation of ribonucleotides into
            polydeoxynucleotide material.
  JOURNAL   J. Biol. Chem. 234 (1959) 2351-2358.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4323166]
  AUTHORS   Kielley RK.
  TITLE     Purification and properties of thymidine monophosphate kinase from
            mouse hepatoma.
  JOURNAL   J. Biol. Chem. 245 (1970) 4204-12.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:4899016]
  AUTHORS   Nelson DJ, Carter CE.
  TITLE     Purification and characterization of Thymidine 5-monophosphate
            kinase from Escherichia coli B.
  JOURNAL   J. Biol. Chem. 244 (1969) 5254-62.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K00943  dTMP kinase
GENES       HSA: 1841(DTYMK)
            MMU: 21915(Dtymk)
            CFA: 609615(LOC609615)
            GGA: 770258(DTYMK)
            XLA: 414549(MGC81047)
            XTR: 448574(dtymk)
            SPU: 578930(LOC578930) 584731(LOC584731)
            DME: Dmel_CG5757
            CEL: R53.2
            OSA: 4326794 4344056
            CME: CML322C
            SCE: YJR057W(CDC8)
            AGO: AGOS_AFR369W
            PIC: PICST_53211(CDC8)
            SPO: SPCC70.07c
            ANI: AN8213.2
            AFM: AFUA_5G03460 AFUA_5G05570
            AOR: AO090102000555
            CNE: CNC04630
            ECU: ECU04_1220
            DDI: DDB_0230101(tmkA)
            PFA: PFL2465c
            CHO: Chro.50490
            TAN: TA12510
            TPV: TP02_0319
            TET: TTHERM_00263130
            TBR: Tb927.8.3510 Tb927.8.3910
            TCR: 506685.30 509663.30
            LMA: LmjF10.0060
            EHI: 55.t00018
            ECO: b1097(yceG) b1098(tmk)
            ECJ: JW1084(tmk)
            ECE: Z1737(tmk)
            ECS: ECs1476
            ECC: c1370(tmk)
            ECI: UTI89_C1224(yceG) UTI89_C1225(tmk)
            ECP: ECP_1090
            ECV: APECO1_179(tmk)
            ECW: EcE24377A_1219(tmk)
            ECX: EcHS_A1166 EcHS_A1202(flgH) EcHS_A1220(tmk)
            STY: STY1239(tmk)
            STT: t1720(tmk)
            SPT: SPA1651(tmk)
            SEC: SC1150(tmk)
            STM: STM1200(tmk)
            YPE: YPO1605(tmk)
            YPK: y1764(tmk)
            YPM: YP_2249(tmk)
            YPA: YPA_1920
            YPN: YPN_2024
            YPP: YPDSF_1842
            YPS: YPTB2466(tmk)
            YPI: YpsIP31758_1583(tmk)
            SFL: SF1101(yceG) SF1102(tmk)
            SFX: S1182(tmk)
            SFV: SFV_1118(tmk)
            SSN: SSON_1117(yceG) SSON_1118(tmk)
            SBO: SBO_1965(tmk) SBO_1966(yceG)
            SDY: SDY_2052(tmk) SDY_2053(yceG)
            ECA: ECA1802(tmk)
            PLU: plu2828(tmk)
            BUC: BU353(tmk)
            BAS: BUsg341(tmk)
            BAB: bbp323(tmk)
            WBR: WGLp094(tmk)
            SGL: SG1065
            ENT: Ent638_1613
            SPE: Spro_1911
            BFL: Bfl401(tmk)
            BPN: BPEN_413(tmk)
            HIT: NTHI0586(tmk)
            HIP: CGSHiEE_00710(tdk)
            HIQ: CGSHiGG_05530(tdk)
            HDU: HD1933(tmk)
            HSO: HS_1487(tmk)
            PMU: PM1673
            MSU: MS0569(tmk)
            APL: APL_1817(tmk)
            ASU: Asuc_1867
            XFA: XF0580
            XFT: PD1569(tmk)
            XCC: XCC3931(tmk)
            XCB: XC_4020
            XCV: XCV4107(tmk)
            XAC: XAC4014(tmk)
            XOO: XOO0431(tmk)
            XOM: XOO_0393(XOO0393)
            VCH: VC2016
            VCO: VC0395_A1602(tmk)
            VVU: VV1_3002
            VVY: VV1280
            VPA: VP2049
            VFI: VF1735
            PPR: PBPRA1200
            PAE: PA2962(tmk)
            PAU: PA14_25740(tmk)
            PAP: PSPA7_2199(tmk)
            PPF: Pput_3795
            PST: PSPTO_3827(tmk)
            PSB: Psyr_1652
            PSP: PSPPH_1646(tmk)
            PFL: PFL_1801(tmk)
            PFO: Pfl_4152
            PEN: PSEEN1624(tmk)
            PMY: Pmen_1633
            PAR: Psyc_0145(tmk)
            PCR: Pcryo_0155
            PRW: PsycPRwf_0126
            ACI: ACIAD2588(tmk)
            SON: SO_2613(tmk)
            SDN: Sden_2051
            SFR: Sfri_2240
            SAZ: Sama_2043
            SBL: Sbal_2459
            SBM: Shew185_2452
            SLO: Shew_1579
            SPC: Sputcn32_2214
            SSE: Ssed_2648
            SPL: Spea_1923
            SHE: Shewmr4_1661
            SHM: Shewmr7_1736
            SHN: Shewana3_1766
            SHW: Sputw3181_1795
            ILO: IL1336(tmk)
            CPS: CPS_2302(tmk)
            PHA: PSHAa1803(tmk)
            PAT: Patl_2117
            SDE: Sde_1634
            PIN: Ping_1094
            MAQ: Maqu_1862
            CBU: CBU_0499(tmk)
            CBD: COXBU7E912_1577(tmk)
            LPN: lpg1399
            LPF: lpl1350(tmk)
            LPP: lpp1354(tmk)
            MCA: MCA1996(tmk)
            FTU: FTT0117(tmk)
            FTF: FTF0117(nupC2)
            FTW: FTW_0202(tmk)
            FTL: FTL_1660
            FTH: FTH_1601(tmk)
            FTA: FTA_1757(tmk)
            FTN: FTN_1598(tmk)
            TCX: Tcr_0718
            NOC: Noc_1660
            AEH: Mlg_1416
            HHA: Hhal_0006
            HCH: HCH_02148(tmk)
            CSA: Csal_1606
            ABO: ABO_1074(dsbD-2)
            MMW: Mmwyl1_2267
            AHA: AHA_2256(tmk)
            DNO: DNO_1213(tmk)
            BCI: BCI_0431(tmk)
            RMA: Rmag_0220
            VOK: COSY_0214(tmk)
            NME: NMB0670
            NMA: NMA0869(tmk)
            NMC: NMC0619(tmk)
            NGO: NGO0239
            CVI: CV_3723(tmk)
            RSO: RSc1784(tmk)
            REU: Reut_A1434
            REH: H16_A1569(tmk)
            RME: Rmet_1828
            BMA: BMA1425(tmk)
            BMV: BMASAVP1_A1916(tmk)
            BML: BMA10299_A3388(tmk)
            BMN: BMA10247_1189(tmk)
            BXE: Bxe_A2263
            BVI: Bcep1808_1817
            BUR: Bcep18194_A5193
            BCN: Bcen_6186
            BCH: Bcen2424_1893
            BAM: Bamb_1830
            BPS: BPSL1436
            BPM: BURPS1710b_2443(tmk)
            BPL: BURPS1106A_2320(tmk)
            BPD: BURPS668_2281(tmk)
            BTE: BTH_I2154(tmk)
            PNU: Pnuc_0966
            BPE: BP1847(tmk)
            BPA: BPP1559(tmk)
            BBR: BB2637(tmk)
            RFR: Rfer_2255
            POL: Bpro_2519
            PNA: Pnap_1948
            AAV: Aave_3412
            AJS: Ajs_1717
            VEI: Veis_1005
            MPT: Mpe_A1860 Mpe_B0240
            HAR: HEAR1396(tmk)
            MMS: mma_1986(tmk)
            NEU: NE2181(tmk)
            NET: Neut_0536
            NMU: Nmul_A1387
            EBA: ebA5415(tmk)
            AZO: azo1595(tmk)
            DAR: Daro_2197
            TBD: Tbd_1543
            MFA: Mfla_1500
            HPY: HP1474
            HPJ: jhp1367(tmk)
            HPA: HPAG1_1439
            HHE: HH1362(tmk)
            HAC: Hac_1734(tmk)
            WSU: WS0613
            TDN: Tmden_1126
            CJE: Cj0766c(tmk)
            CJR: CJE0857(tmk)
            CJJ: CJJ81176_0787(tmk)
            CJU: C8J_0717(tmk)
            CJD: JJD26997_1246(tmk)
            CFF: CFF8240_0893(tmk)
            CCV: CCV52592_1098(tmk) CCV52592_1903
            CHA: CHAB381_0924(tmk)
            CCO: CCC13826_1271(tmk)
            ABU: Abu_0966(tmk)
            NIS: NIS_0819(tmk)
            SUN: SUN_1354(tmk)
            GSU: GSU2229(tmk)
            GME: Gmet_2318
            GUR: Gura_2566 Gura_2643 Gura_3153
            PCA: Pcar_1691
            PPD: Ppro_1665
            DVU: DVU2140(tmk)
            DVL: Dvul_1092
            DDE: Dde_2338
            LIP: LI0760(tmk)
            BBA: Bd1040(tmk)
            DPS: DP2809
            ADE: Adeh_1721
            AFW: Anae109_2080 Anae109_3375
            MXA: MXAN_3412(tmk)
            SAT: SYN_01448 SYN_03606
            SFU: Sfum_0398
            RPR: RP684(tdk)
            RTY: RT0679(tdk)
            RCO: RC1047(tdk)
            RFE: RF_0234(tdk) RF_p13(tdk) RF_pd13(tdk)
            RBE: RBE_0237(tmk1)
            RAK: A1C_05335(tdk)
            RBO: A1I_06675(tdk)
            RCM: A1E_04550(tdk)
            RRI: A1G_05815(tdk)
            OTS: OTBS_1018(tmk)
            WOL: WD1251(tmk)
            WBM: Wbm0148
            AMA: AM111(tmk)
            APH: APH_0093(tmk)
            ERU: Erum7460(tmk)
            ERW: ERWE_CDS_07860(tmk)
            ERG: ERGA_CDS_07770(tmk)
            ECN: Ecaj_0780
            ECH: ECH_0229(tmk)
            NSE: NSE_0547(tmk)
            PUB: SAR11_0999(tmk)
            MLO: mll0424
            MES: Meso_1581
            PLA: Plav_3110
            SME: SMc01189(tmk)
            SMD: Smed_1292
            ATU: Atu1498(tmk)
            ATC: AGR_C_2760
            RET: RHE_CH02160(tmk)
            RLE: RL2476(tmk)
            BME: BMEI0005 BMEI0989
            BMF: BAB1_1011
            BMS: BR0992(tmk)
            BMB: BruAb1_0998(tmk)
            BOV: BOV_0960(tmk)
            OAN: Oant_2077
            BJA: bll4518(tmk)
            BRA: BRADO3827(tmk)
            BBT: BBta_4102(tmk)
            RPA: RPA2775
            RPB: RPB_2679
            RPC: RPC_2703
            RPD: RPD_2715
            RPE: RPE_2865
            NWI: Nwi_1464
            NHA: Nham_2010
            BHE: BH08460(tmk)
            BQU: BQ06110(tmk)
            BBK: BARBAKC583_0822(tmk)
            XAU: Xaut_4325
            CCR: CC_1824
            SIL: SPO2740(tmk)
            SIT: TM1040_3591
            RSP: RSP_0551
            RSH: Rsph17029_2202
            RSQ: Rsph17025_1236
            JAN: Jann_1277
            RDE: RD1_3466(tmk)
            PDE: Pden_2144
            MMR: Mmar10_1454
            HNE: HNE_1813(tmk)
            ZMO: ZMO1090(tmk)
            NAR: Saro_1941
            SAL: Sala_1257
            SWI: Swit_0484
            ELI: ELI_06215
            GOX: GOX0018
            GBE: GbCGDNIH1_0014 GbCGDNIH1_1075
            ACR: Acry_0970
            RRU: Rru_A1703
            MAG: amb2450
            MGM: Mmc1_1870
            ABA: Acid345_3227
            SUS: Acid_4038 Acid_7330
            BSU: BG10092(tmk)
            BHA: BH0042(tmk)
            BAN: BA0027(tmk)
            BAR: GBAA0027(tmk)
            BAA: BA_0618
            BAT: BAS0029
            BCE: BC0036(tdk)
            BCA: BCE_0028(tdk)
            BCZ: BCZK0026(tdk)
            BCY: Bcer98_0025
            BTK: BT9727_0026(tdk)
            BTL: BALH_0026(tmk)
            BLI: BL02509(tmk)
            BLD: BLi00041(tmk)
            BCL: ABC0050(tmk)
            BAY: RBAM_000370(tmk)
            BPU: BPUM_0012(tmk)
            OIH: OB0036(tdk)
            GKA: GK0024
            GTN: GTNG_0023(tmk)
            SAU: SA0440(tmk)
            SAV: SAV0482(tmk)
            SAM: MW0437(tmk)
            SAR: SAR0483(tmk)
            SAS: SAS0439
            SAC: SACOL0524(tmk)
            SAB: SAB0431(tmk)
            SAA: SAUSA300_0459(tmk)
            SAO: SAOUHSC_00451
            SAJ: SaurJH9_0503
            SAH: SaurJH1_0516
            SEP: SE2301
            SER: SERP0120(tmk)
            SHA: SH2529
            SSP: SSP2274
            LMO: lmo2693
            LMF: LMOf2365_2672(tmk)
            LIN: lin2841
            LWE: lwe2642(tmk)
            LLA: L3846(yeaB)
            LLC: LACR_0445
            LLM: llmg_0415(tmk)
            SPY: SPy_0399(tmk)
            SPZ: M5005_Spy_0330(tmk)
            SPM: spyM18_0449(tdk)
            SPG: SpyM3_0289(tmk)
            SPS: SPs1570
            SPH: MGAS10270_Spy0326(tmk)
            SPI: MGAS10750_Spy0326(tmk)
            SPJ: MGAS2096_Spy0350(tmk)
            SPK: MGAS9429_Spy0332(tmk)
            SPF: SpyM51528(tmk)
            SPA: M6_Spy0356
            SPB: M28_Spy0319(tmk)
            SPN: SP_0935
            SPR: spr0835(tmk)
            SPD: SPD_0825(tmk)
            SAG: SAG1575(tmk)
            SAN: gbs1626
            SAK: SAK_1591(tmk)
            SMU: SMU.1663(kthY)
            STC: str0489(tmk)
            STL: stu0489(tmk)
            STE: STER_0526
            SSA: SSA_1722(tmk)
            SSU: SSU05_0661
            SGO: SGO_1539(tmk)
            LPL: lp_0703(tmk)
            LJO: LJ0427
            LAC: LBA0381
            LSA: LSA0340(tmk)
            LSL: LSL_1224(tmk)
            LDB: Ldb1631(tmk)
            LBU: LBUL_1511
            LBR: LVIS_0604
            LCA: LSEI_2259
            LGA: LGAS_0372
            LRE: Lreu_0330
            PPE: PEPE_1481
            EFA: EF2764(tmk)
            OOE: OEOE_1407
            LME: LEUM_0279
            STH: STH3258
            CTC: CTC00220 CTC00965
            CNO: NT01CX_0761
            CDF: CD3550
            CBO: CBO0054
            CBE: Cbei_0113
            CKL: CKL_3795(tmk)
            AMT: Amet_0082
            CHY: CHY_0050(tmk)
            DSY: DSY1860
            DRM: Dred_0059
            SWO: Swol_0040
            CSC: Csac_0740
            TTE: TTE0094(tmk)
            MTA: Moth_0042
            MGE: MG_006(tmk)
            MPN: MPN006(D12_orf210)
            MPU: MYPU_0520(tmk)
            MPE: MYPE8140(tmk)
            MGA: MGA_0606(tmk)
            MMY: MSC_0046(tmk)
            MMO: MMOB0760(tmk)
            MHY: mhp120(tmk)
            MHJ: MHJ_0251(tmk)
            MHP: MHP7448_0259(tmk)
            MSY: MS53_0052(tmk)
            MCP: MCAP_0010(tmk)
            UUR: UU020(tmk)
            POY: PAM230(tmk)
            AYW: AYWB_074(tmk) AYWB_181(tmk) AYWB_222(tmk) AYWB_282(tmk)
                 AYWB_492(tmk)
            MFL: Mfl676
            MTU: Rv3247c(tmk)
            MTC: MT3345
            MBO: Mb3275c(tmk)
            MBB: BCG_3276c(tmk)
            MLE: ML0772(tmk)
            MPA: MAP3361c(tmk)
            MSM: MSMEG_1873
            CGL: NCgl0720(cgl0753)
            CGB: cg0861(tmk)
            CEF: CE0768
            CDI: DIP0693
            CJK: jk1636(tmk)
            NFA: nfa46120(tmk)
            RHA: RHA1_ro06323
            TWH: TWT695(tmk)
            TWS: TW714
            LXX: Lxx04070(tmk)
            ART: Arth_0717
            AAU: AAur_0888(tmk)
            PAC: PPA0243
            NCA: Noca_0386
            TFU: Tfu_2783
            FRA: Francci3_0306 Francci3_4306
            FAL: FRAAL0668(tmk) FRAAL6580(tmk)
            ACE: Acel_1971
            KRA: Krad_0489
            SEN: SACE_6448(tmk)
            STP: Strop_4023
            BLO: BL0484
            BAD: BAD_0162
            RXY: Rxyl_1962
            FNU: FN1323
            RBA: RB12445(tmk)
            CTR: CT188(tdk)
            CTA: CTA_0206(tdk)
            CMU: TC0460
            CPN: CPn0273(tdk)
            CPA: CP0486
            CPJ: CPj0273(tdk)
            CPT: CpB0280
            CCA: CCA00508(tmk)
            CAB: CAB495(tdk)
            CFE: CF0500(tdk)
            PCU: pc1073(tmk)
            BGA: BG0819(tmk)
            BAF: BAPKO_0846(tmk)
            TPA: TP0354
            TDE: TDE2599(tmk)
            LIL: LA0806
            LIC: LIC12814(tmk)
            LBJ: LBJ_0758(tmk)
            LBL: LBL_2320(tmk)
            SYN: slr0379(tmk)
            SYW: SYNW2238
            SYC: syc1411_c(tmk)
            SYF: Synpcc7942_0093
            SYD: Syncc9605_2380
            SYE: Syncc9902_0312
            SYG: sync_2593(tmk)
            SYR: SynRCC307_0254(tmk)
            SYX: SynWH7803_2244(tmk)
            CYA: CYA_2830(tmk)
            CYB: CYB_0832(tmk)
            TEL: tlr2055
            GVI: glr0678
            ANA: all4708
            AVA: Ava_1962
            PMA: Pro0152(tmk)
            PMM: PMM0130
            PMT: PMT1990
            PMN: PMN2A_1496
            PMI: PMT9312_0132
            PMB: A9601_01471(tmk)
            PMC: P9515_01581(tmk)
            PMF: P9303_26491(tmk)
            PMG: P9301_01491(tmk)
            PMH: P9215_01471(tmk)
            PME: NATL1_02021(tmk)
            TER: Tery_1564
            SRU: SRU_2701(tmk)
            CTE: CT1313(tmk)
            CCH: Cag_0925
            CPH: Cpha266_1638
            PVI: Cvib_1045
            PLT: Plut_1310
            DET: DET0778(tmk)
            DEH: cbdb_A752(tmk)
            DEB: DehaBAV1_0704
            RRS: RoseRS_3232
            RCA: Rcas_3720
            DRA: DR_0111
            DGE: Dgeo_1983
            TTH: TTC1243
            TTJ: TTHA1607
            AAE: aq_969(tmk)
            TMA: TM1099
            TPT: Tpet_1644
            TME: Tmel_0927
            FNO: Fnod_0696
            MMP: MMP1034(tmk)
            MMQ: MmarC5_0559
            MMZ: MmarC7_0288
            MAE: Maeo_0344
            MVN: Mevan_0357
            MAC: MA4433(tmk)
            MBA: Mbar_A1098
            MMA: MM_1111
            MBU: Mbur_1673
            MTP: Mthe_1246
            MHU: Mhun_2629
            MEM: Memar_1571
            MBN: Mboo_1719
            MTH: MTH1100
            MST: Msp_0357(tmk)
            MSI: Msm_0520
            MKA: MK0101(tmk)
            HAL: VNG1929G(tmk)
            HMA: rrnAC3286(tmk)
            HWA: HQ3145A(tmk)
            NPH: NP2478A(tmk)
            TAC: Ta0081
            TVO: TVN0173
            PTO: PTO1101 PTO1422
            PAB: PAB0319(tmk)
            PFU: PF1730(tmk)
            TKO: TK1403
            RCI: RCIX1311(tmk-1) RCIX2044(tmk-2)
            APE: APE_2090
            SMR: Smar_0624
            SSO: SSO0780(tmk-1) SSO1191 SSO1192(tmk-2)
            STO: ST0462 ST1542 ST1543
            SAI: Saci_0893 Saci_2019 Saci_2020
            MSE: Msed_0980 Msed_2036
            PAI: PAE0964(tmk)
            PIS: Pisl_1194
            PCL: Pcal_0126
            PAS: Pars_0156
            TPE: Tpen_1026
STRUCTURES  PDB: 1E2D  1E2E  1E2F  1E2G  1E2Q  1E98  1E99  1E9A  1E9B  1E9C  
                 1E9D  1E9E  1E9F  1G3U  1GSI  1GTV  1MRN  1MRS  1N5I  1N5J  
                 1N5K  1N5L  1NMX  1NMY  1NMZ  1NN0  1NN1  1NN3  1NN5  1TMK  
                 1W2G  1W2H  2CCG  2CCJ  2CCK  2PBR  2TMK  3TMK  4TMK  5TMP  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.9
            ExPASy - ENZYME nomenclature database: 2.7.4.9
            ExplorEnz - The Enzyme Database: 2.7.4.9
            ERGO genome analysis and discovery system: 2.7.4.9
            BRENDA, the Enzyme Database: 2.7.4.9
            CAS: 9014-43-1
///
ENTRY       EC 2.7.4.10                 Enzyme
NAME        nucleoside-triphosphate---adenylate kinase;
            guanosine triphosphate-adenylate kinase;
            nucleoside triphosphate-adenosine monophosphate transphosphorylase;
            GTP:AMP phosphotransferase;
            isozyme 3 of adenylate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     nucleoside-triphosphate:AMP phosphotransferase
REACTION    nucleoside triphosphate + AMP = nucleoside diphosphate + ADP
            [RN:R00333]
ALL_REAC    R00333 > R00157
SUBSTRATE   nucleoside triphosphate [CPD:C00201];
            AMP [CPD:C00020]
PRODUCT     nucleoside diphosphate [CPD:C00454];
            ADP [CPD:C00008]
COMMENT     Many nucleoside triphosphates can act as donors.
REFERENCE   1  [PMID:5423264]
  AUTHORS   Albrecht GJ.
  TITLE     Purification and properties of nucleoside triphosphate-adenosine
            monophosphate transphosphorylase from beef heart mitochondria.
  JOURNAL   Biochemistry. 9 (1970) 2462-70.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:13693071]
  AUTHORS   CHIGA M, ROGERS AE, PLAUT GW.
  TITLE     Nucleotide transphosphorylases from liver. II. Purification and
            properties of a 6-oxypurine nucleoside triphosphate-adenosine
            monophosphate transphosphorylase from swine liver.
  JOURNAL   J. Biol. Chem. 236 (1961) 1800-5.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K00944  nucleoside-triphosphate--adenylate kinase
GENES       HSA: 50808(AK3)
            PTR: 464977(AK3)
            MMU: 56248(Ak3)
            RNO: 26956(Ak3)
            CFA: 608853(LOC608853)
            BTA: 281613(AK3)
            GGA: 426534(LOC426534)
            XLA: 414511(MGC82246)
            SPU: 583479(LOC583479)
            SPE: Spro_1139
            ASU: Asuc_1819
            PPF: Pput_4216
            PMY: Pmen_3359
            PRW: PsycPRwf_0806
            SBM: Shew185_2584
            SSE: Ssed_2847
            SPL: Spea_1528
            MMW: Mmwyl1_1256
            SAJ: SaurJH9_2256
            SAH: SaurJH1_2297
            CBE: Cbei_0172
            AMT: Amet_4457
            CSC: Csac_2267
            DEB: DehaBAV1_0472
            RRS: RoseRS_1164
            RCA: Rcas_4005
            TPT: Tpet_1313
STRUCTURES  PDB: 1ZD8  2AK3  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.10
            ExPASy - ENZYME nomenclature database: 2.7.4.10
            ExplorEnz - The Enzyme Database: 2.7.4.10
            ERGO genome analysis and discovery system: 2.7.4.10
            BRENDA, the Enzyme Database: 2.7.4.10
            CAS: 9026-74-8
///
ENTRY       EC 2.7.4.11                 Enzyme
NAME        (deoxy)adenylate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:(d)AMP phosphotransferase
REACTION    ATP + dAMP = ADP + dADP [RN:R01547]
ALL_REAC    R01547
SUBSTRATE   ATP [CPD:C00002];
            dAMP [CPD:C00360]
PRODUCT     ADP [CPD:C00008];
            dADP [CPD:C00206]
COMMENT     AMP can also act as acceptor.
REFERENCE   1  [PMID:5862227]
  AUTHORS   Griffith TJ, Helleiner CW.
  TITLE     The partial purification of deoxynucleoside monophosphate kinases
            from L cells.
  JOURNAL   Biochim. Biophys. Acta. 108 (1965) 114-24.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map00230  Purine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.11
            ExPASy - ENZYME nomenclature database: 2.7.4.11
            ExplorEnz - The Enzyme Database: 2.7.4.11
            ERGO genome analysis and discovery system: 2.7.4.11
            BRENDA, the Enzyme Database: 2.7.4.11
            CAS: 37278-19-6
///
ENTRY       EC 2.7.4.12                 Enzyme
NAME        T2-induced deoxynucleotide kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:(d)NMP phosphotransferase
REACTION    ATP + dGMP (or dTMP) = ADP + dGDP (or dTDP) [RN:R02090 R02094]
ALL_REAC    R02090 R02094
SUBSTRATE   ATP [CPD:C00002];
            dGMP [CPD:C00362];
            dTMP [CPD:C00364]
PRODUCT     ADP [CPD:C00008];
            dGDP [CPD:C00361];
            dTDP [CPD:C00363]
COMMENT     dTMP and dAMP can act as acceptors; dATP can act as donor.
REFERENCE   1  [PMID:13967158]
  AUTHORS   BELLO LJ, BESSMAN MJ.
  TITLE     The enzymology of virus-infected bacteria. IV. Purification and
            properties of the deoxynucleotide kinase induced by bacteriophage
            T2.
  JOURNAL   J. Biol. Chem. 238 (1963) 1777-87.
  ORGANISM  Escherichia coli [GN:eco]
GENES       PMB: A9601_05231(gmk)
            PMC: P9515_05311(gmk)
            PMF: P9303_06681(gmk)
            PMG: P9301_04921(gmk)
            PME: NATL1_05221(gmk)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.12
            ExPASy - ENZYME nomenclature database: 2.7.4.12
            ExplorEnz - The Enzyme Database: 2.7.4.12
            ERGO genome analysis and discovery system: 2.7.4.12
            BRENDA, the Enzyme Database: 2.7.4.12
            CAS: 37278-99-2
///
ENTRY       EC 2.7.4.13                 Enzyme
NAME        (deoxy)nucleoside-phosphate kinase;
            deoxynucleoside monophosphate kinase;
            deoxyribonucleoside monophosphokinase;
            deoxynucleoside-5'-monophosphate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:deoxynucleoside-phosphate phosphotransferase
REACTION    ATP + deoxynucleoside phosphate = ADP + deoxynucleoside diphosphate
            [RN:R04267]
ALL_REAC    R04267
SUBSTRATE   ATP [CPD:C00002];
            deoxynucleoside phosphate [CPD:C03607]
PRODUCT     ADP [CPD:C00008];
            deoxynucleoside diphosphate [CPD:C03786]
COMMENT     dATP can substitute for ATP.
REFERENCE   1  [PMID:14253449]
  AUTHORS   BESSMAN MJ, HERRIOTT ST, ORR MJ.
  TITLE     THE ENZYMOLOGY OF VIRUS-INFECTED BACTERIA. VI. PURIFICATION AND
            PROPERTIES OF THE DEOXYNUCLEOTIDE KINASE INDUCED BY BACTERIOPHAGE
            T5.
  JOURNAL   J. Biol. Chem. 240 (1965) 439-45.
  ORGANISM  bacteriophage T5
STRUCTURES  PDB: 1DEK  1DEL  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.13
            ExPASy - ENZYME nomenclature database: 2.7.4.13
            ExplorEnz - The Enzyme Database: 2.7.4.13
            ERGO genome analysis and discovery system: 2.7.4.13
            BRENDA, the Enzyme Database: 2.7.4.13
            CAS: 37278-20-9
///
ENTRY       EC 2.7.4.14                 Enzyme
NAME        cytidylate kinase;
            deoxycytidylate kinase;
            deoxycytidylate kinase;
            CMP kinase;
            CTP:CMP phosphotransferase;
            dCMP kinase;
            deoxycytidine monophosphokinase;
            UMP-CMP kinase;
            ATP:UMP-CMP phosphotransferase;
            pyrimidine nucleoside monophosphate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:CMP phosphotransferase
REACTION    ATP + (d)CMP = ADP + (d)CDP [RN:R00512 R01665]
ALL_REAC    R00512 R01665;
            (other) R00158
SUBSTRATE   ATP [CPD:C00002];
            dCMP [CPD:C00239]
PRODUCT     ADP [CPD:C00008];
            dCDP [CPD:C00705]
COMMENT     UMP and dCMP can also act as acceptors.
REFERENCE   1
  AUTHORS   Hurwitz, J.
  TITLE     The enzymatic incorporation of ribonucleotides into
            polydeoxynucleotide material.
  JOURNAL   J. Biol. Chem. 234 (1959) 2351-2358.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Noda, L.
  TITLE     Nucleoside triphosphate-nucleoside monophosphokinases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 6, Academic Press, New York, 1962, p. 139-149.
REFERENCE   3  [PMID:5350952]
  AUTHORS   Ruffner BW Jr, Anderson EP.
  TITLE     Adenosine triphosphate: uridine monophosphate-cytidine monophosphate
            phosphotransferase from Tetrahymena pyriformis.
  JOURNAL   J. Biol. Chem. 244 (1969) 5994-6002.
  ORGANISM  Tetrahymena pyriformis
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K00945  cytidylate kinase
GENES       HSA: 51727(CMPK)
            PTR: 456837(CMPK)
            MMU: 66588(Cmpk)
            RNO: 298410(Cmpk)
            CFA: 610291(CMPK)
            BTA: 509965(MGC137127)
            GGA: 429100(RCJMB04_11f2)
            XLA: 398670(MGC64474)
            DRE: 406383(cmpk)
            SPU: 581681(LOC581681)
            DME: Dmel_CG6092
            CEL: F40F8.1
            ATH: AT5G26667
            OSA: 4330910
            SCE: YKL024C(URA6)
            AGO: AGOS_ACR170C
            PIC: PICST_90609(URA6)
            CAL: CaO19.12662(ura6)
            SPO: SPCC1795.05c
            ANI: AN4258.2
            AFM: AFUA_7G03990
            AOR: AO090026000815
            CNE: CNF00400
            ECU: ECU03_1270
            DDI: DDB_0191367(pyrK)
            PFA: MAL1P2.40
            CPV: cgd1_3140
            TAN: TA14600
            TPV: TP02_0690
            TET: TTHERM_00227210
            EHI: 121.t00014
            ECO: b0910(cmk)
            ECJ: JW0893(cmk)
            ECE: Z1256(cmk)
            ECS: ECs0993
            ECC: c1048(cmk)
            ECI: UTI89_C0981(cmk)
            ECP: ECP_0921
            ECV: APECO1_22(cmk)
            ECW: EcE24377A_1007(cmk)
            ECX: EcHS_A1016(cmk)
            STY: STY0980(cmk)
            STT: t1954(cmk)
            SPT: SPA1818(cmk)
            SEC: SC0934(cmk)
            STM: STM0980(cmk)
            YPE: YPO1391(cmk)
            YPK: y2782(cmk)
            YPM: YP_1202(cmk)
            YPA: YPA_0682
            YPN: YPN_2586
            YPP: YPDSF_2304
            YPS: YPTB1416(cmkA)
            YPI: YpsIP31758_2581(cmk)
            YEN: YE1539(cmk)
            SFL: SF0906(cmk)
            SFX: S0970(cmk)
            SFV: SFV_0911(cmk)
            SSN: SSON_0912(cmk)
            SBO: SBO_2198(cmk)
            SDY: SDY_2348(cmk)
            ECA: ECA2592(cmk)
            PLU: plu1621(mssA)
            BAB: bbp287(cmk)
            WBR: WGLp485(cmk)
            SGL: SG0992
            ENT: Ent638_1429
            KPN: KPN_00937(cmk)
            SPE: Spro_1708
            BFL: Bfl381(cmk)
            BPN: BPEN_392(cmk)
            HIN: HI1219(cmkA)
            HIT: NTHI1949(cmk)
            HIP: CGSHiEE_03825(cmk)
            HIQ: CGSHiGG_01910(cmk) CGSHiGG_09835(cmk)
            HDU: HD1351(cmk)
            HSO: HS_0977(cmkA)
            PMU: PM0802(cmkA)
            MSU: MS1477(cmk)
            APL: APL_0741(cmkA)
            ASU: Asuc_1553
            XFA: XF2439
            XFT: PD1457(cmk)
            XCC: XCC2195(cmk)
            XCB: XC_1923
            XCV: XCV2497(cmk)
            XAC: XAC2299(cmk)
            XOO: XOO2179(cmk)
            XOM: XOO_2049(XOO2049)
            VCH: VC1916
            VCO: VC0395_A1506(cmk)
            VVU: VV1_2983
            VVY: VV1299
            VPA: VP2031
            VFI: VF1760
            PPR: PBPRA2451(mssA)
            PAE: PA3163(cmk)
            PAU: PA14_23320(cmk)
            PAP: PSPA7_1966(cmk)
            PPU: PP_1771(cmk)
            PPF: Pput_3943
            PST: PSPTO_1749(cmk)
            PSB: Psyr_3643(cmk)
            PSP: PSPPH_3663(cmk)
            PFL: PFL_4309(cmk)
            PFO: Pfl_4073(cmk)
            PEN: PSEEN1491(cmk)
            PMY: Pmen_1853
            PAR: Psyc_1495(cmkA)
            PCR: Pcryo_1674
            PRW: PsycPRwf_1588
            ACI: ACIAD2348(cmk)
            SON: SO_2403(cmk)
            SDN: Sden_1752
            SFR: Sfri_2124
            SAZ: Sama_1735
            SBL: Sbal_2069
            SBM: Shew185_2280
            SLO: Shew_1953
            SPC: Sputcn32_2043
            SSE: Ssed_2299
            SPL: Spea_2072
            SHE: Shewmr4_1923
            SHM: Shewmr7_2055
            SHN: Shewana3_1976
            SHW: Sputw3181_1970
            ILO: IL1356(cmk)
            CPS: CPS_2334(cmk)
            PHA: PSHAa1424(cmk)
            PAT: Patl_2467
            SDE: Sde_2140
            PIN: Ping_3014
            MAQ: Maqu_1026
            CBU: CBU_0527(cmk)
            CBD: COXBU7E912_1536(cmk)
            LPN: lpg1420(cmk)
            LPF: lpl1371(kcy)
            LPP: lpp1375(kcy)
            MCA: MCA1414(cmk)
            FTU: FTT0559c(cmk)
            FTF: FTF0559c(cmk)
            FTW: FTW_0981(cmk)
            FTL: FTL_1017
            FTH: FTH_0992(cmk)
            FTA: FTA_1072(cmk)
            FTN: FTN_0956(cmk)
            TCX: Tcr_1197
            NOC: Noc_0179
            AEH: Mlg_0930
            HHA: Hhal_0564
            HCH: HCH_04979(cmk)
            CSA: Csal_2164
            ABO: ABO_1746(cmk)
            MMW: Mmwyl1_2856
            AHA: AHA_1808(cmk)
            DNO: DNO_0112(cmk)
            BCI: BCI_0254(cmk)
            RMA: Rmag_0593
            VOK: COSY_0548(cmk)
            NME: NMB1300
            NMA: NMA1514(cmk)
            NMC: NMC1237(cmk)
            NGO: NGO0605
            CVI: CV_3047(cmk)
            RSO: RSc0908(cmk)
            REU: Reut_A2570
            REH: H16_A0797(cmk)
            RME: Rmet_0721
            BMA: BMA0429(cmk)
            BMV: BMASAVP1_A2573(cmk)
            BML: BMA10299_A0948(cmk)
            BMN: BMA10247_0200(cmk)
            BXE: Bxe_A0981
            BVI: Bcep1808_0967
            BUR: Bcep18194_A4159
            BCN: Bcen_0567
            BCH: Bcen2424_1046
            BAM: Bamb_0922
            BPS: BPSL2516(cmk)
            BPM: BURPS1710b_2995(cmk)
            BPL: BURPS1106A_2946(cmk)
            BPD: BURPS668_2883(cmk)
            BTE: BTH_I1637(cmk)
            PNU: Pnuc_0499
            BPE: BP0949(cmk)
            BPA: BPP3129(cmk)
            BBR: BB3468(cmk)
            RFR: Rfer_1567
            POL: Bpro_1790
            PNA: Pnap_2795
            AAV: Aave_3284
            AJS: Ajs_2468
            VEI: Veis_3123
            HAR: HEAR2575(cmk)
            MMS: mma_2669(cmk)
            NEU: NE1963(cmk)
            NET: Neut_0399
            NMU: Nmul_A2070
            TBD: Tbd_0955
            MFA: Mfla_0928 Mfla_1072
            GSU: GSU2605(cmk)
            GME: Gmet_0865
            GUR: Gura_1465
            PCA: Pcar_1884
            PPD: Ppro_1348
            DVU: DVU1028(cmk)
            DVL: Dvul_1965
            DDE: Dde_1452
            LIP: LI0910(cmk)
            BBA: Bd1062(cmk)
            ADE: Adeh_1515
            AFW: Anae109_2309
            MXA: MXAN_4037(cmk)
            SAT: SYN_01231 SYN_02496 SYN_03196
            SFU: Sfum_2117
            RPR: RP522(cmk)
            RTY: RT0509(cmk)
            RCO: RC0748(cmk)
            RFE: RF_0770(cmk)
            RBE: RBE_0413(cmk)
            RAK: A1C_04245(cmk)
            RBO: A1I_05675(cmk)
            RCM: A1E_02730(cmk)
            RRI: A1G_04215(cmk)
            AMA: AM916(cmk)
            APH: APH_0274(cmkB)
            ERU: Erum6110(cmk)
            ERW: ERWE_CDS_06420(cmk)
            ERG: ERGA_CDS_06330(cmk)
            ECN: Ecaj_0616
            ECH: ECH_0403(cmk)
            PUB: SAR11_0493(cmk)
            MLO: mll5212
            MES: Meso_3607
            PLA: Plav_0150
            SME: SMc00334(cmk)
            SMD: Smed_3457
            ATU: Atu4103(cmk)
            ATC: AGR_L_1498
            RET: RHE_CH00098(cmk)
            RLE: RL0107
            BME: BMEI1916
            BMF: BAB1_0024
            BMS: BR0026(cmk)
            BMB: BruAb1_0026(cmk)
            BOV: BOV_0025(cmk)
            OAN: Oant_0030
            BJA: blr0739(cmk)
            BRA: BRADO0097(cmk)
            BBT: BBta_0104(cmk)
            RPA: RPA0063(cmk)
            RPB: RPB_0641
            RPC: RPC_0398
            RPD: RPD_0191
            RPE: RPE_0446
            NWI: Nwi_0208
            NHA: Nham_0164
            BHE: BH00940(cmk)
            BQU: BQ00870(cmk)
            BBK: BARBAKC583_1304(cmk)
            XAU: Xaut_1111
            CCR: CC_3588
            SIL: SPOA0017(cmk)
            SIT: TM1040_0197
            RSP: RSP_3591
            RSH: Rsph17029_3276
            JAN: Jann_0715
            RDE: RD1_3913
            PDE: Pden_3784
            MMR: Mmar10_0099
            HNE: HNE_0193(cmk)
            ZMO: ZMO1797(cmk)
            NAR: Saro_1324
            SAL: Sala_1494
            SWI: Swit_2457
            ELI: ELI_07500
            GOX: GOX0597
            GBE: GbCGDNIH1_2024
            ACR: Acry_0030
            RRU: Rru_A0294
            MAG: amb4262
            MGM: Mmc1_0173
            ABA: Acid345_3221
            SUS: Acid_0051
            BSU: BG11004(cmk)
            BHA: BH1634(cmk)
            BAN: BA1518(cmk)
            BAR: GBAA1518(cmk)
            BAA: BA_2039
            BAT: BAS1407
            BCE: BC1497
            BCA: BCE_1623(cmk)
            BCZ: BCZK1378(cmk)
            BCY: Bcer98_1220
            BTK: BT9727_1379(cmk)
            BTL: BALH_1352(cmk)
            BLI: BL02219(cmk)
            BLD: BLi02428(cmk)
            BCL: ABC1872(cmk)
            BAY: RBAM_021040(cmk)
            BPU: BPUM_2022(cmk)
            OIH: OB1802(cmk)
            GKA: GK2227
            SAU: SA1309(cmk)
            SAV: SAV1478(cmk)
            SAM: MW1366(cmk)
            SAR: SAR1486(cmk)
            SAS: SAS1418
            SAC: SACOL1518(cmk)
            SAB: SAB1340c(cmk)
            SAA: SAUSA300_1367(cmk)
            SAO: SAOUHSC_01496
            SAJ: SaurJH9_1534
            SAH: SaurJH1_1565
            SEP: SE1166
            SER: SERP1045(cmk)
            SHA: SH1434(cmk)
            SSP: SSP1269
            LMO: lmo1939(cmk)
            LMF: LMOf2365_1968(cmk)
            LIN: lin2053(cmk)
            LWE: lwe1965(cmk)
            LLA: L143791(cmk)
            LLC: LACR_1860
            LLM: llmg_0732(cmk)
            SPY: SPy_0803(cmk)
            SPZ: M5005_Spy_0618(cmk)
            SPM: spyM18_0865(cmk)
            SPG: SpyM3_0537(cmk)
            SPS: SPs1317
            SPH: MGAS10270_Spy0673(cmk)
            SPI: MGAS10750_Spy0705(cmk)
            SPJ: MGAS2096_Spy0683(cmk)
            SPK: MGAS9429_Spy0673(cmk)
            SPF: SpyM51189(cmk)
            SPA: M6_Spy0635(cmk)
            SPB: M28_Spy0597(cmk)
            SPN: SP_1603
            SPR: spr1456(cmk)
            SPD: SPD_1428(cmk)
            SAG: SAG1385(cmk)
            SAN: gbs1455
            SAK: SAK_1418(cmk)
            SMU: SMU.696(cmk)
            STC: str1135(cmk)
            STL: stu1135(cmk)
            SSA: SSA_1501(cmk)
            SGO: SGO_1031(cmk)
            LPL: lp_1883(cmk)
            LJO: LJ1089
            LAC: LBA0967
            LSA: LSA1018(cmk)
            LSL: LSL_0900(cmk)
            LDB: Ldb0850(cmk)
            LBU: LBUL_0774
            LBR: LVIS_0776
            LCA: LSEI_1378
            LRE: Lreu_0762
            EFA: EF1547(cmk)
            OOE: OEOE_1008
            STH: STH1668
            CAC: CAC1848(cmk)
            CPE: CPE1084(cmk)
            CPF: CPF_1340(cmk)
            CPR: CPR_1151(cmk)
            CTC: CTC01315(cmk)
            CNO: NT01CX_2095
            CTH: Cthe_0712
            CDF: CD1816(cmk)
            CBO: CBO1808(cmk)
            CBA: CLB_1743(cmk)
            CBH: CLC_1750(cmk)
            CBF: CLI_1803(cmk)
            CBE: Cbei_2544
            CKL: CKL_1566(cmk)
            AMT: Amet_2627
            CHY: CHY_1927(cmk)
            DSY: DSY2257
            DRM: Dred_1152
            SWO: Swol_1346
            CSC: Csac_1889
            TTE: TTE1350(cmk)
            MTA: Moth_1331
            MGE: MG_330(cmk)
            MPN: MPN476(cmk)
            MPU: MYPU_0890(cmk)
            MPE: MYPE2280(cmk)
            MGA: MGA_0900(cmk)
            MMY: MSC_0407(cmk)
            MMO: MMOB4840(cmk)
            MHY: mhp074(cmk)
            MHJ: MHJ_0065(cmk)
            MHP: MHP7448_0069(cmk)
            MSY: MS53_0143(cmk)
            MCP: MCAP_0578(cmk)
            UUR: UU342(cmk)
            POY: PAM239(cmk)
            AYW: AYWB_482(cmk)
            MFL: Mfl198
            MTU: Rv1712(cmk)
            MTC: MT1752(cmk)
            MBO: Mb1739(cmk)
            MBB: BCG_1751(cmk)
            MLE: ML1371(cmk)
            MPA: MAP1414(cmk)
            MAV: MAV_3064(cmk)
            MSM: MSMEG_3739(cmk)
            MVA: Mvan_3275
            MGI: Mflv_3494
            MMC: Mmcs_2928
            MKM: Mkms_2972
            MJL: Mjls_2943
            CGL: NCgl1372(cgl1427)
            CGB: cg1616(cmk)
            CEF: CE1560
            CDI: DIP1196(cmk)
            CJK: jk0878(cmk)
            NFA: nfa20120(cmk)
            RHA: RHA1_ro00924
            SCO: SCO1760(2SCI34.13c)
            SMA: SAV6522(cmk)
            LXX: Lxx05730(cmk)
            CMI: CMM_1975(cmkA)
            ART: Arth_1536
            AAU: AAur_1674(cmk)
            PAC: PPA1209
            NCA: Noca_2501
            TFU: Tfu_1209
            FRA: Francci3_1456
            FAL: FRAAL2253(cmk)
            ACE: Acel_1234
            SEN: SACE_5234(cmk)
            STP: Strop_1929
            RXY: Rxyl_1440
            FNU: FN1607
            RBA: RB10510(cmk) RB2394
            CTR: CT452(cmk)
            CTA: CTA_0494(cmk)
            CMU: TC0737
            CPN: CPn0568(cmk)
            CPA: CP0181
            CPJ: CPj0568(cmk)
            CPT: CpB0590
            CCA: CCA00174(cmk)
            CAB: CAB171(cmk)
            CFE: CF0833(cmk)
            PCU: pc0319(cmk)
            BBU: BB0128(cmk-1)
            BGA: BG0130(cmk) BG0844
            BAF: BAPKO_0130(cmk)
            TPA: TP0342
            TDE: TDE1087(cmk)
            LIL: LA1259
            LBJ: LBJ_0935(cmk)
            LBL: LBL_2098(cmk)
            SYN: sll1249(panC)
            SYW: SYNW2027(panC)
            SYC: syc0399_d(panC)
            SYF: Synpcc7942_1151
            SYD: Syncc9605_0416
            SYE: Syncc9902_1914
            SYG: sync_0483(panC)
            SYR: SynRCC307_2069
            SYX: SynWH7803_0474
            CYA: CYA_2663(panC)
            CYB: CYB_2425(panC)
            TEL: tll2450(panC)
            GVI: gll1806
            ANA: alr2936(panC)
            AVA: Ava_0964
            PMA: Pro1746(cmk)
            PMM: PMM1590(panC)
            PMT: PMT1689(panC)
            PMN: PMN2A_1165
            PMI: PMT9312_1682
            PMB: A9601_17991(cmk)
            PMC: P9515_17771(cmk)
            PMF: P9303_22471(panC)
            PMG: P9301_17821(cmk)
            PME: NATL1_20401(cmk)
            TER: Tery_2799
            BTH: BT_2060
            BFR: BF3747
            BFS: BF3535(cmk)
            PGI: PG0603(cmk)
            SRU: SRU_1788(cmk)
            CHU: CHU_0086(cmk)
            GFO: GFO_1852(cmk)
            FJO: Fjoh_2756
            FPS: FP1712(cmk)
            CTE: CT0286(cmk)
            CCH: Cag_0571
            CPH: Cpha266_0417
            PVI: Cvib_1515
            PLT: Plut_1733
            RRS: RoseRS_0324
            RCA: Rcas_0862
            DRA: DR_2543
            DGE: Dgeo_2220
            TTH: TTC0089
            TTJ: TTHA0458
            AAE: aq_2153(cmk)
            TMA: TM1443
            TPT: Tpet_1351
            TME: Tmel_1622
            FNO: Fnod_1232
            MJA: MJ0656(cmk)
            MMP: MMP0626(cmk)
            MVN: Mevan_1499
            MAC: MA1104(cmk)
            MBA: Mbar_A0083
            MMA: MM_2153
            MBU: Mbur_0027
            MHU: Mhun_2227
            MST: Msp_0881(cmk)
            MSI: Msm_0734
            MKA: MK0022(cmk)
            HAL: VNG1727G(cmk)
            HMA: rrnAC3343(cmk)
            HWA: HQ2740A(cmk) HQ2765A(cmk)
            NPH: NP4914A(cmk)
            TAC: Ta1245
            TVO: TVN0351
            PTO: PTO0666
            PAB: PAB0763(cmk)
            PFU: PF0820
            TKO: TK1514
            RCI: RCIX2574(cmk)
            APE: APE_0978.1
            IHO: Igni_0756
            HBU: Hbut_1327
            SSO: SSO0692(cmk)
            STO: ST0408
            SAI: Saci_0570
            MSE: Msed_0118
            PAI: PAE3225(cmk)
            PIS: Pisl_0399
            PCL: Pcal_1109
            PAS: Pars_1364
STRUCTURES  PDB: 1CKE  1KDO  1KDP  1KDR  1KDT  1Q3T  1QF9  1TEV  1UKE  2CMK  
                 2FEM  2FEO  2H92  2UKD  3UKD  4UKD  5UKD  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.14
            ExPASy - ENZYME nomenclature database: 2.7.4.14
            ExplorEnz - The Enzyme Database: 2.7.4.14
            ERGO genome analysis and discovery system: 2.7.4.14
            BRENDA, the Enzyme Database: 2.7.4.14
            CAS: 37278-21-0
///
ENTRY       EC 2.7.4.15                 Enzyme
NAME        thiamine-diphosphate kinase;
            ATP:thiamin-diphosphate phosphotransferase;
            TDP kinase;
            thiamin diphosphate kinase;
            thiamin diphosphate phosphotransferase;
            thiamin pyrophosphate kinase;
            thiamine diphosphate kinase;
            protein bound thiamin diphosphate:ATP phosphoryltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:thiamine-diphosphate phosphotransferase
REACTION    ATP + thiamine diphosphate = ADP + thiamine triphosphate [RN:R00616]
ALL_REAC    R00616
SUBSTRATE   ATP [CPD:C00002];
            thiamine diphosphate [CPD:C00068]
PRODUCT     ADP [CPD:C00008];
            thiamine triphosphate [CPD:C03028]
REFERENCE   1  [PMID:5661031]
  AUTHORS   Itokawa Y, Cooper JR.
  TITLE     The enzymatic synthesis of triphosphothiamin.
  JOURNAL   Biochim. Biophys. Acta. 158 (1968) 180-2.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Kikuchi, M. and Ikawa, T.
  TITLE     Presence of an enzyme mediating transfer of phosphate from thiamine
            triphosphate to ADP in germinating maize.
  JOURNAL   Bot. Mag. (Tokyo) 97 (1984) 193-205.
  ORGANISM  Zea mays [GN:ezma]
PATHWAY     PATH: map00730  Thiamine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.15
            ExPASy - ENZYME nomenclature database: 2.7.4.15
            ExplorEnz - The Enzyme Database: 2.7.4.15
            ERGO genome analysis and discovery system: 2.7.4.15
            BRENDA, the Enzyme Database: 2.7.4.15
            CAS: 9075-79-0
///
ENTRY       EC 2.7.4.16                 Enzyme
NAME        thiamine-phosphate kinase;
            thiamin-monophosphate kinase;
            thiamin monophosphatase;
            thiamin monophosphokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:thiamine-phosphate phosphotransferase
REACTION    ATP + thiamine phosphate = ADP + thiamine diphosphate [RN:R00617]
ALL_REAC    R00617
SUBSTRATE   ATP [CPD:C00002];
            thiamine phosphate [CPD:C01081]
PRODUCT     ADP [CPD:C00008];
            thiamine diphosphate [CPD:C00068]
REFERENCE   1  [PMID:4567662]
  AUTHORS   Nishino H.
  TITLE     Biogenesis of cocarboxylase in Escherichia coli. Partial
            purification and some properties of thiamine monophosphate kinase.
  JOURNAL   J. Biochem. (Tokyo). 72 (1972) 1093-100.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00730  Thiamine metabolism
ORTHOLOGY   KO: K00946  thiamine-monophosphate kinase
GENES       ECO: b0417(thiL)
            ECJ: JW0407(thiL)
            ECE: Z0519(thiL)
            ECS: ECs0470
            ECC: c0528(thiL)
            ECI: UTI89_C0440(thiL)
            ECP: ECP_0476
            ECV: APECO1_1593(thiL)
            ECW: EcE24377A_0448(thiL)
            STY: STY0458
            STT: t2444
            SPT: SPA2304(thiL)
            SEC: SC0460(thiL)
            STM: STM0419(thiL)
            YPE: YPO3180(thiL)
            YPK: y1003(thiL)
            YPM: YP_0751(thiL)
            YPA: YPA_2674
            YPN: YPN_0908
            YPP: YPDSF_2815
            YPS: YPTB0937(thiL)
            YPI: YpsIP31758_3114(thiL)
            SFL: SF0354(thiL)
            SFX: S0362(thiL)
            SFV: SFV_0382(thiL)
            SSN: SSON_0394(thiL)
            SBO: SBO_0311(thiL)
            SDY: SDY_0317(thiL)
            ECA: ECA1129(thiL)
            PLU: plu3896(thiL)
            BUC: BU460(thiL)
            BAS: BUsg444(thiL)
            WBR: WGLp465(thiL)
            SGL: SG0654
            ENT: Ent638_0885
            SPE: Spro_1075
            HIT: NTHI1618(thiL)
            HDU: HD0436(thiL)
            HSO: HS_0832(thiL)
            PMU: PM0729(thiL)
            MSU: MS0974(thiL)
            APL: APL_0202(thiL)
            ASU: Asuc_1486
            XFA: XF0956
            XFT: PD1742(thiL)
            XCC: XCC0699(thiL)
            XCB: XC_3535
            XCV: XCV0804(thiL)
            XAC: XAC0752(thiL)
            XOO: XOO3850(thiL)
            XOM: XOO_3629(XOO3629)
            VCH: VC2266
            VCO: VC0395_A1856(thiL)
            VVU: VV1_0317
            VVY: VV0866
            VPA: VP0684
            VFI: VF0705
            PPR: PBPRA0802
            PAE: PA4051(thiL)
            PAU: PA14_11460(thiL)
            PAP: PSPA7_1050(thiL)
            PPU: PP_0519(thiL)
            PPF: Pput_0554
            PST: PSPTO_0695(thiL)
            PSB: Psyr_4457
            PSP: PSPPH_4502(thiL)
            PFL: PFL_5517(thiL)
            PFO: Pfl_5014
            PEN: PSEEN0593(thiL)
            PMY: Pmen_3852
            PAR: Psyc_2071(thiL)
            PCR: Pcryo_2394
            PRW: PsycPRwf_2283
            ACI: ACIAD3573(thiL)
            SON: SO_3464(thiL)
            SDN: Sden_1149
            SFR: Sfri_1040
            SAZ: Sama_1021
            SBL: Sbal_3155
            SBM: Shew185_3153
            SLO: Shew_1192
            SPC: Sputcn32_2773
            SSE: Ssed_1278
            SPL: Spea_1167
            SHE: Shewmr4_1101
            SHM: Shewmr7_1167
            SHN: Shewana3_1101
            SHW: Sputw3181_1239
            ILO: IL2140(thiL)
            CPS: CPS_1533(thiL)
            PHA: PSHAa2369(thiL)
            PAT: Patl_1316
            SDE: Sde_3453
            PIN: Ping_2241
            MAQ: Maqu_0847
            CBU: CBU_1415(thiL)
            CBD: COXBU7E912_0581(thiL)
            LPN: lpg0728(thiL)
            LPF: lpl0765(thiL)
            LPP: lpp0794(thiL)
            MCA: MCA1653(thiL)
            TCX: Tcr_1395
            NOC: Noc_0804
            AEH: Mlg_0380
            HHA: Hhal_0895
            HCH: HCH_05952(thiL)
            CSA: Csal_2581
            ABO: ABO_2169(thiL)
            MMW: Mmwyl1_4047
            AHA: AHA_3327(thiL)
            BCI: BCI_0604(thiL)
            VOK: COSY_0388(thiL)
            NME: NMB0385
            NMA: NMA2103(thiL)
            NMC: NMC1782(thiL)
            NGO: NGO1575
            CVI: CV_2392(thiL)
            RSO: RSc2768(thiL)
            REU: Reut_A2848
            REH: H16_A3154(thiL)
            RME: Rmet_3047
            BMA: BMA2478(thiL)
            BMV: BMASAVP1_A0397(thiL)
            BML: BMA10299_A1257(thiL)
            BMN: BMA10247_3308(thiL)
            BXE: Bxe_A0556
            BVI: Bcep1808_0604
            BUR: Bcep18194_A3712
            BCN: Bcen_0147
            BCH: Bcen2424_0630
            BAM: Bamb_0531
            BPS: BPSL2960
            BPM: BURPS1710b_3475(thiL)
            BPL: BURPS1106A_3477(thiL)
            BPD: BURPS668_3440(thiL)
            BTE: BTH_I1188(thiL)
            BPE: BP3487(thiL)
            BPA: BPP0860(thiL)
            BBR: BB0954(thiL)
            RFR: Rfer_0529
            POL: Bpro_4471
            PNA: Pnap_3665
            AAV: Aave_0432
            AJS: Ajs_0356
            VEI: Veis_0583
            MPT: Mpe_A0210 Mpe_A1597
            HAR: HEAR0642(thiL)
            MMS: mma_0609(thiL)
            NEU: NE2559(thiL)
            NET: Neut_2519
            NMU: Nmul_A0013
            EBA: ebA3404(thiL)
            AZO: azo0510(thiL)
            DAR: Daro_3740
            TBD: Tbd_2193
            MFA: Mfla_0573
            HPA: HPAG1_0043
            HHE: HH1834(thiL)
            WSU: WS1272(thiL)
            TDN: Tmden_1031
            CJE: Cj1458c(thiL)
            CJR: CJE1632
            CJU: C8J_1364
            CFF: CFF8240_0088(thiL)
            CCV: CCV52592_0773(thiL)
            CHA: CHAB381_0702
            CCO: CCC13826_1042
            ABU: Abu_0740(thiL)
            NIS: NIS_0691
            SUN: SUN_1198
            GSU: GSU3194(thiL)
            GME: Gmet_3213
            PCA: Pcar_0028
            DVU: DVU0157(thiL)
            DVL: Dvul_2811
            DDE: Dde_3570
            LIP: LI0673(thiL)
            BBA: Bd1008(thiL)
            DPS: DP2270(thiL)
            ADE: Adeh_4320
            MXA: MXAN_6697(thiL)
            SFU: Sfum_1693
            AMA: AM552(thiL)
            APH: APH_0735(thiL)
            ERU: Erum4980(thiL)
            ERW: ERWE_CDS_05210(thiL)
            ERG: ERGA_CDS_05120(thiL)
            ECN: Ecaj_0505
            ECH: ECH_0528(thiL)
            NSE: NSE_0253(thiL)
            PUB: SAR11_1041(thiL)
            PLA: Plav_2915
            BJA: bll5027
            BRA: BRADO4424(thiL)
            BBT: BBta_4643(thiL)
            RPA: RPA2730(thiL)
            RPB: RPB_2640
            RPC: RPC_2665
            RPD: RPD_2677
            RPE: RPE_2814
            NWI: Nwi_1721
            NHA: Nham_1820
            XAU: Xaut_4282
            CCR: CC_1361
            MMR: Mmar10_1530
            HNE: HNE_1157(thiL)
            ZMO: ZMO1553(thiL)
            NAR: Saro_1068
            SAL: Sala_2024
            SWI: Swit_2773
            ELI: ELI_02585
            GOX: GOX2416
            GBE: GbCGDNIH1_1002
            ACR: Acry_2116
            RRU: Rru_A0305 Rru_A1820
            MAG: amb2347
            MGM: Mmc1_0163
            ABA: Acid345_4694
            SUS: Acid_0821
            BSU: BG10693(thiL)
            BHA: BH0544
            BLI: BL00841(thiL)
            BLD: BLi00611(thiL)
            BCL: ABC0867(thiL)
            BPU: BPUM_0521(thiL)
            OIH: OB0644
            CHY: CHY_0749(thiL)
            MTA: Moth_1157
            MTU: Rv2977c(thiL)
            MTC: MT3055(thiL)
            MBO: Mb3001c(thiL)
            MBB: BCG_2998c(thiL)
            MLE: ML1676(thiL)
            MPA: MAP3017c(thiL)
            MAV: MAV_3829(thiL)
            MSM: MSMEG_2398(thiL)
            MVA: Mvan_2151
            MGI: Mflv_4216
            MMC: Mmcs_1932
            MKM: Mkms_1978
            MJL: Mjls_1912
            CGL: NCgl1269(cgl1323)
            CGB: cg1495(thiL)
            CEF: CE1435
            CDI: DIP1133(thiL)
            CJK: jk1215(thiL)
            NFA: nfa42010(thiL)
            RHA: RHA1_ro03331 RHA1_ro06510(thiL)
            SCO: SCO5562(SC7A1.06)
            SMA: SAV2676(thiL)
            LXX: Lxx09720(thiL)
            CMI: CMM_1349(thiL)
            ART: Arth_2512
            AAU: AAur_2479(thiL)
            PAC: PPA1357
            NCA: Noca_3288
            TFU: Tfu_0643
            FRA: Francci3_3747
            FAL: FRAAL5979(thiL)
            KRA: Krad_1366
            SEN: SACE_3074 SACE_6127(thiL)
            STP: Strop_1275
            RXY: Rxyl_2786
            RBA: RB6809(thiL)
            LIL: LA3412
            LIC: LIC10759(thiL)
            LBJ: LBJ_2669(thiL)
            LBL: LBL_0395(thiL)
            SYN: slr1787
            SYW: SYNW0031(thiL)
            SYC: syc1543_c(thiL)
            SYF: Synpcc7942_2567
            SYD: Syncc9605_0031
            SYE: Syncc9902_0027
            SYG: sync_0030(thiL)
            SYR: SynRCC307_0029(thiL)
            SYX: SynWH7803_0030(thiL)
            CYA: CYA_1899(thiL)
            CYB: CYB_1867(thiL)
            TEL: tll2366
            GVI: glr3298
            ANA: alr5061
            AVA: Ava_2317
            PMA: Pro0024(thiL)
            PMM: PMM0024(thiL)
            PMT: PMT0029(thiL)
            PMN: PMN2A_1351
            PMI: PMT9312_0024
            PMB: A9601_00231(thiL)
            PMC: P9515_00231(thiL)
            PMF: P9303_00281(thiL)
            PMG: P9301_00231(thiL)
            PMH: P9215_00231(thiL)
            PME: NATL1_00231(thiL)
            TER: Tery_4031
            BTH: BT_1882
            BFR: BF3454
            BFS: BF3275
            PGI: PG0637(thiL)
            SRU: SRU_2426(thiL)
            CHU: CHU_2521(thiL)
            GFO: GFO_3137(thiL)
            FJO: Fjoh_0791
            FPS: FP2326(thiL)
            CTE: CT0199(thiL)
            CCH: Cag_0556(hypE) Cag_1213
            PLT: Plut_1928
            DET: DET0397(thiL)
            DEH: cbdb_A347(thiL)
            TTH: TTC0056
            TTJ: TTHA0424
            AAE: aq_2119(thiL)
            MJA: MJ0028
            MMP: MMP1124
            MMQ: MmarC5_0460
            MMZ: MmarC7_0376
            MAE: Maeo_1455
            MVN: Mevan_0447
            MAC: MA0069(hypE)
            MBA: Mbar_A1035
            MMA: MM_0761 MM_1365
            MBU: Mbur_2128
            MHU: Mhun_2605
            MLA: Mlab_0140
            MBN: Mboo_2319
            MTH: MTH1396
            MST: Msp_1564(thiL)
            MSI: Msm_1283
            MKA: MK0607(thiL)
            HAL: VNG2011G(thiL)
            HMA: rrnAC3177(thiL)
            HWA: HQ1102A(thiL)
            NPH: NP2280A(thiL)
            TAC: Ta0526
            TVO: TVN1002
            PTO: PTO0838
            PAB: PAB2358(thiL)
            PFU: PF1877
            TKO: TK0890
            RCI: RCIX1803(thiL-1) RRC167(thiL-2)
            APE: APE_0235.1
            SMR: Smar_1576
            SSO: SSO0237(thiL)
            STO: ST0287
            SAI: Saci_0704(thiL)
            PAI: PAE1022 PAE1024
            TPE: Tpen_0476
STRUCTURES  PDB: 1VQV  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.16
            ExPASy - ENZYME nomenclature database: 2.7.4.16
            ExplorEnz - The Enzyme Database: 2.7.4.16
            ERGO genome analysis and discovery system: 2.7.4.16
            BRENDA, the Enzyme Database: 2.7.4.16
            CAS: 9068-23-9
///
ENTRY       EC 2.7.4.17                 Enzyme
NAME        3-phosphoglyceroyl-phosphate---polyphosphate phosphotransferase;
            diphosphoglycerate-polyphosphate phosphotransferase;
            1,3-diphosphoglycerate-polyphosphate phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     3-phospho-D-glyceroyl-phosphate:polyphosphate phosphotransferase
REACTION    3-phospho-D-glyceroyl phosphate + (phosphate)n = 3-phosphoglycerate
            + (phosphate)n+1 [RN:R02188]
ALL_REAC    R02188
SUBSTRATE   3-phospho-D-glyceroyl phosphate [CPD:C00236];
            (phosphate)n [CPD:C00404]
PRODUCT     3-phosphoglycerate [CPD:C00597];
            (phosphate)n+1 [CPD:C00404]
REFERENCE   1
  AUTHORS   Kulaev, I.S. and Bobyk, M.A.
  TITLE     Detection of a new enzyme in Neurospora crassa -
            1,3-diphosphoglycerate:polyphosphatephosphotransferase.
  JOURNAL   Biochemistry (Moscow) 36 (1971) 356-359.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2
  AUTHORS   Kulaev, I.S., Bobyk, M.A., Nikolaev, N.N., Sergeev, N.S. and Uryson,
            S.O.
  TITLE     Polyphosphate synthesizing enzymes in some fungi and bacteria.
  JOURNAL   Biochemistry (Moscow) 36 (1971) 791-796.
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.17
            ExPASy - ENZYME nomenclature database: 2.7.4.17
            ExplorEnz - The Enzyme Database: 2.7.4.17
            ERGO genome analysis and discovery system: 2.7.4.17
            BRENDA, the Enzyme Database: 2.7.4.17
            CAS: 9055-36-1
///
ENTRY       EC 2.7.4.18                 Enzyme
NAME        farnesyl-diphosphate kinase;
            farnesyl pyrophosphate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:farnesyl-diphosphate phosphotransferase
REACTION    ATP + farnesyl diphosphate = ADP + farnesyl triphosphate [RN:R02303]
ALL_REAC    R02303
SUBSTRATE   ATP [CPD:C00002];
            farnesyl diphosphate [CPD:C00448]
PRODUCT     ADP [CPD:C00008];
            farnesyl triphosphate [CPD:C03115]
COMMENT     ADP can also act as donor.
REFERENCE   1  [PMID:4423368]
  AUTHORS   Shechter I.
  TITLE     Phosphate transfer from trans-farnesyl triphosphate to AMP in
            Gibberella fujikuroi.
  JOURNAL   Biochim. Biophys. Acta. 362 (1974) 233-44.
  ORGANISM  Gibberella fujikuroi
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.18
            ExPASy - ENZYME nomenclature database: 2.7.4.18
            ExplorEnz - The Enzyme Database: 2.7.4.18
            ERGO genome analysis and discovery system: 2.7.4.18
            BRENDA, the Enzyme Database: 2.7.4.18
            CAS: 50936-43-1
///
ENTRY       EC 2.7.4.19                 Enzyme
NAME        5-methyldeoxycytidine-5'-phosphate kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:5-methyldeoxycytidine-5'-phosphate phosphotransferase
REACTION    ATP + 5-methyldeoxycytidine 5'-phosphate = ADP +
            5-methyldeoxycytidine diphosphate [RN:R04235]
ALL_REAC    R04235
SUBSTRATE   ATP [CPD:C00002];
            5-methyldeoxycytidine 5'-phosphate [CPD:C03495]
PRODUCT     ADP [CPD:C00008];
            5-methyldeoxycytidine diphosphate [CPD:C04187]
COMMENT     The enzyme, from phage XP-12-infected Xanthomonas oryzae, converts
            m5dCMP into m5dCDP and then into m5dCTP.
REFERENCE   1  [PMID:7082669]
  AUTHORS   Wang RY, Huang LH, Ehrlich M.
  TITLE     A bacteriophage-induced 5-methyldeoxycytidine 5'-monophosphate
            kinase.
  JOURNAL   Biochim. Biophys. Acta. 696 (1982) 31-6.
  ORGANISM  Xanthomonas oryzae
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.19
            ExPASy - ENZYME nomenclature database: 2.7.4.19
            ExplorEnz - The Enzyme Database: 2.7.4.19
            ERGO genome analysis and discovery system: 2.7.4.19
            BRENDA, the Enzyme Database: 2.7.4.19
            CAS: 81032-53-3
///
ENTRY       EC 2.7.4.20                 Enzyme
NAME        dolichyl-diphosphate---polyphosphate phosphotransferase;
            dolichylpyrophosphate:polyphosphate phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     dolichyl-diphosphate:polyphosphate phosphotransferase
REACTION    dolichyl diphosphate + (phosphate)n = dolichyl phosphate +
            (phosphate)n+1 [RN:R02186]
ALL_REAC    R02186
SUBSTRATE   dolichyl diphosphate [CPD:C00621];
            (phosphate)n [CPD:C00404]
PRODUCT     dolichyl phosphate [CPD:C00110];
            (phosphate)n+1 [CPD:C00404]
REFERENCE   1
  AUTHORS   Naumov, A.V., Shabalin, Y.A., Vagabov, V.M. and Kulaev, I.S.
  TITLE     Two pathways of dephosphorylation of dolichyl diphosphate in yeasts.
  JOURNAL   Biochemistry (Moscow) 50 (1985) 551-556.
  ORGANISM  Saccharomyces carlsbergensis
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.20
            ExPASy - ENZYME nomenclature database: 2.7.4.20
            ExplorEnz - The Enzyme Database: 2.7.4.20
            ERGO genome analysis and discovery system: 2.7.4.20
            BRENDA, the Enzyme Database: 2.7.4.20
            CAS: 94949-27-6
///
ENTRY       EC 2.7.4.21                 Enzyme
NAME        inositol-hexakisphosphate kinase;
            ATP:1D-myo-inositol-hexakisphosphate phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:1D-myo-inositol-hexakisphosphate 5-phosphotransferase
REACTION    (1) ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol
            5-diphosphate 1,2,3,4,6-pentakisphosphate;
            (2) ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate = ADP +
            1D-myo-inositol diphosphate tetrakisphosphate (isomeric
            configuration unknown)
ALL_REAC    (other) R05799
SUBSTRATE   ATP [CPD:C00002];
            1D-myo-inositol hexakisphosphate [CPD:C01204];
            1D-myo-inositol 1,3,4,5,6-pentakisphosphate [CPD:C01284]
PRODUCT     ADP [CPD:C00008];
            1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate;
            1D-myo-inositol diphosphate tetrakisphosphate (isomeric
            configuration unknown)
COMMENT     Three mammalian isoforms are known to exist.
REFERENCE   1  [PMID:10574768]
  AUTHORS   Saiardi A, Erdjument-Bromage H, Snowman AM, Tempst P, Snyder SH.
  TITLE     Synthesis of diphosphoinositol pentakisphosphate by a newly
            identified family of higher inositol polyphosphate kinases.
  JOURNAL   Curr. Biol. 9 (1999) 1323-6.
  ORGANISM  mouse [GN:mmu], human [GN:hsa]
REFERENCE   2  [PMID:10567691]
  AUTHORS   Schell MJ, Letcher AJ, Brearley CA, Biber J, Murer H, Irvine RF.
  TITLE     PiUS (Pi uptake stimulator) is an inositol hexakisphosphate kinase.
  JOURNAL   FEBS. Lett. 461 (1999) 169-72.
  ORGANISM  Xenopus sp.
REFERENCE   3  [PMID:9359429]
  AUTHORS   Albert C, Safrany ST, Bembenek ME, Reddy KM, Reddy K, Falck J,
            Brocker M, Shears SB, Mayr GW.
  TITLE     Biological variability in the structures of diphosphoinositol
            polyphosphates in Dictyostelium discoideum and mammalian cells.
  JOURNAL   Biochem. J. 327 ( Pt 2) (1997) 553-60.
  ORGANISM  human [GN:hsa], hamster
ORTHOLOGY   KO: K07756  inositol-hexakisphosphate kinase
GENES       HSA: 117283(IHPK3) 51447(IHPK2) 9807(IHPK1)
            MMU: 271424(Ihpk3) 27399(Ihpk1) 76500(Ihpk2)
            RNO: 50560(Ihpk1)
            CFA: 484765(IHPK1) 612831(IHPK2)
            GGA: 419908(IHPK3)
            XLA: 443957(MGC80337) 444642(MGC84167)
            DRE: 322041(ihpk2)
            SPU: 585505(LOC585505)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.21
            ExPASy - ENZYME nomenclature database: 2.7.4.21
            ExplorEnz - The Enzyme Database: 2.7.4.21
            ERGO genome analysis and discovery system: 2.7.4.21
            BRENDA, the Enzyme Database: 2.7.4.21
            CAS: 176898-37-6
///
ENTRY       EC 2.7.4.22                 Enzyme
NAME        UMP kinase;
            uridylate kinase;
            UMPK;
            uridine monophosphate kinase;
            PyrH;
            UMP-kinase;
            SmbA
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:UMP phosphotransferase
REACTION    ATP + UMP = ADP + UDP [RN:R00158]
ALL_REAC    R00158
SUBSTRATE   ATP [CPD:C00002];
            UMP [CPD:C00105]
PRODUCT     ADP [CPD:C00008];
            UDP [CPD:C00015]
COMMENT     This enzyme is strictly specific for UMP as substrate and is used by
            prokaryotes in the de novo synthesis of pyrimidines, in contrast to
            eukaryotes, which use the dual-specificity enzyme UMP/CMP kinase (EC
            2.7.4.14) for the same purpose [2]. This enzyme is the subject of
            feedback regulation, being inhibited by UTP and activated by GTP
            [1].
REFERENCE   1  [PMID:7711027]
  AUTHORS   Serina L, Blondin C, Krin E, Sismeiro O, Danchin A, Sakamoto H,
            Gilles AM, Barzu O.
  TITLE     Escherichia coli UMP-kinase, a member of the aspartokinase family,
            is a hexamer regulated by guanine nucleotides and UTP.
  JOURNAL   Biochemistry. 34 (1995) 5066-74.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:16095620]
  AUTHORS   Marco-Marin C, Gil-Ortiz F, Rubio V.
  TITLE     The crystal structure of Pyrococcus furiosus UMP kinase provides
            insight into catalysis and regulation in microbial pyrimidine
            nucleotide biosynthesis.
  JOURNAL   J. Mol. Biol. 352 (2005) 438-54.
  ORGANISM  Pyrococcus furiosus [GN:pfu]
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K09903  uridylate kinase
GENES       ATH: AT3G18680
            ECO: b0171(pyrH)
            ECJ: JW0166(pyrH)
            ECE: Z0182(pyrH)
            ECS: ECs0173
            ECC: c0207(pyrH)
            ECI: UTI89_C0186(pyrH)
            ECP: ECP_0179
            ECV: APECO1_1816(pyrH)
            ECW: EcE24377A_0175(pyrH)
            ECX: EcHS_A0173
            STY: STY0241(pyrH)
            STT: t0219(pyrH)
            SPT: SPA0225(pyrH)
            SEC: SC0218(pyrH)
            STM: STM0218(pyrH)
            YPE: YPO1046(pyrH)
            YPK: y3134(pyrH)
            YPM: YP_2805(pyrH)
            YPA: YPA_0522
            YPN: YPN_2954
            YPS: YPTB3001(pyrH)
            SFL: SF0161(pyrH)
            SFX: S0164(pyrH)
            SFV: SFV_0154(pyrH)
            SSN: SSON_0183(pyrH)
            SBO: SBO_0159(pyrH)
            SDY: SDY_0187(pyrH)
            ECA: ECA1033(pyrH)
            PLU: plu0674(pyrH)
            BUC: BU233(pyrH)
            BAS: BUsg227(pyrH)
            BAB: bbp215(pyrH)
            BCC: BCc_144(pyrH)
            SGL: SG1941
            BFL: Bfl273(pyrH)
            BPN: BPEN_281(pyrH)
            HIN: HI1065(pyrH)
            HIT: NTHI1225(pyrH)
            HDU: HD1597(pyrH)
            HSO: HS_0987(pyrH)
            PMU: PM1986(pyrH)
            MSU: MS1930(pyrH)
            APL: APL_0569(pyrH)
            XFA: XF1058
            XFT: PD0337(pyrH)
            XCC: XCC1371(pyrH)
            XCB: XC_2867
            XCV: XCV1476(pyrH)
            XAC: XAC1419(pyrH)
            XOO: XOO1974(pyrH)
            XOM: XOO_1864(XOO1864)
            VCH: VC2258
            VVU: VV1_1861
            VVY: VV2555
            VPA: VP2316
            VFI: VF1960
            PPR: PBPRA2966
            PAE: PA3654(pyrH)
            PAU: PA14_17080(pyrH)
            PPU: PP_1593(pyrH)
            PST: PSPTO_1536(pyrH)
            PSP: PSPPH_3838(pyrH)
            PFL: PFL_1178(pyrH)
            PFO: Pfl_1103
            PEN: PSEEN4218(pyrH)
            PAR: Psyc_1535(pyrH)
            PCR: Pcryo_1714
            ACI: ACIAD1372(pyrH)
            SON: SO_1631(pyrH)
            SDN: Sden_1556
            SFR: Sfri_1272
            SAZ: Sama_1141
            SBL: Sbal_1452
            SHE: Shewmr4_2639
            SHM: Shewmr7_2706
            SHN: Shewana3_2813
            SHW: Sputw3181_2753
            ILO: IL0843(pyrH)
            CPS: CPS_1555(pyrH)
            PHA: PSHAa2034(pyrH)
            PAT: Patl_1251
            SDE: Sde_2595
            PIN: Ping_2974
            MAQ: Maqu_2546
            CBU: CBU_1384(pyrH)
            LPN: lpg1712(pyrH)
            LPF: lpl1671(pyrH)
            LPP: lpp1677(pyrH)
            MCA: MCA0569(pyrH)
            FTU: FTT0315(pyrH)
            FTF: FTF0315(pyrH)
            FTW: FTW_1767(pyrH)
            FTL: FTL_0226
            FTH: FTH_0221(pyrH)
            FTN: FTN_0229(pyrH)
            TCX: Tcr_1283
            NOC: Noc_0810
            AEH: Mlg_1861
            HHA: Hhal_1464
            HCH: HCH_05251(pyrH)
            CSA: Csal_0565
            ABO: ABO_1145(pyrH)
            AHA: AHA_1175(pyrH)
            BCI: BCI_0529(pyrH)
            NME: NMB2103
            NMA: NMA0326(pyrH)
            NMC: NMC2082(pyrH)
            NGO: NGO1973(pyrH)
            CVI: CV_2198(pyrH)
            RSO: RSc1406(pyrH)
            REU: Reut_A1879
            REH: H16_A2053
            RME: Rmet_1437
            BMA: BMA1553(pyrH)
            BMV: BMASAVP1_A2054(pyrH)
            BML: BMA10299_A3257(pyrH)
            BMN: BMA10247_1326(pyrH)
            BXE: Bxe_A1684
            BUR: Bcep18194_A5327
            BCN: Bcen_6060
            BCH: Bcen2424_2017
            BAM: Bamb_2050
            BPS: BPSL2157(pyrH)
            BPM: BURPS1710b_2581(pyrH)
            BPL: BURPS1106A_2491(pyrH)
            BPD: BURPS668_2435(pyrH)
            BTE: BTH_I2029(pyrH)
            PNU: Pnuc_1449
            BPE: BP1421(pyrH)
            BPA: BPP1529(pyrH)
            BBR: BB2607(pyrH)
            RFR: Rfer_1991
            POL: Bpro_2693
            PNA: Pnap_1760
            AAV: Aave_1825
            AJS: Ajs_2583
            VEI: Veis_1440
            MPT: Mpe_A1977
            HAR: HEAR1337(pyrH)
            NEU: NE1716(pyrH)
            NET: Neut_2033
            NMU: Nmul_A0659
            EBA: ebA5988(pyrH)
            AZO: azo1907(pyrH)
            DAR: Daro_1744
            TBD: Tbd_0787
            MFA: Mfla_1528
            HPY: HP0777(pyrH)
            HPJ: jhp0714(pyrH)
            HPA: HPAG1_0762
            HHE: HH0833(pyrH)
            HAC: Hac_0636(pyrH)
            WSU: WS0238(pyrH)
            TDN: Tmden_0717
            CJE: Cj1274c(pyrH)
            CJR: CJE1410(pyrH)
            CJJ: CJJ81176_1290(pyrH)
            CFF: CFF8240_1214(pyrH)
            GSU: GSU1919(pyrH)
            GME: Gmet_1252
            PCA: Pcar_1919
            PPD: Ppro_2046
            DVU: DVU0871(pyrH)
            DVL: Dvul_2111
            DDE: Dde_1129
            LIP: LI0382(pyrH)
            BBA: Bd3783(pyrH)
            DPS: DP1156
            ADE: Adeh_0280
            MXA: MXAN_5342(pyrH)
            SAT: SYN_00920
            SFU: Sfum_1780
            RPR: RP155(pyrH)
            RTY: RT0144(pyrH)
            RCO: RC0198(pyrH)
            RFE: RF_1126(pyrH)
            RBE: RBE_1131(pyrH)
            WOL: WD0530(pyrH)
            WBM: Wbm0806
            AMA: AM128(pyrH)
            APH: APH_0111(pyrH)
            ERU: Erum7240(pyrH)
            ERW: ERWE_CDS_07620(pyrH)
            ERG: ERGA_CDS_07540(pyrH)
            ECN: Ecaj_0759
            ECH: ECH_0266(pyrH)
            NSE: NSE_0946(pyrH)
            MLO: mll0643
            MES: Meso_1383
            SME: SMc02099(pyrH)
            ATU: Atu1376(pyrH)
            ATC: AGR_C_2544
            RET: RHE_CH01915(pyrH)
            RLE: RL2223(pyrH)
            BME: BMEI0825
            BMF: BAB1_1182(pyrH)
            BMS: BR1160(pyrH)
            BMB: BruAb1_1166(pyrH)
            BJA: bll4859(pyrH)
            RPA: RPA2920(pyrH)
            RPB: RPB_2826
            RPC: RPC_2438
            RPD: RPD_2855
            RPE: RPE_2555
            NWI: Nwi_1857
            NHA: Nham_1696
            BHE: BH06240(pyrH)
            BQU: BQ06990(pyrH)
            BBK: BARBAKC583_0585(pyrH)
            CCR: CC_1921
            SIL: SPO1662(pyrH)
            SIT: TM1040_1414
            RSP: RSP_2705(pyrH)
            JAN: Jann_2460
            RDE: RD1_2585(pyrH)
            PDE: Pden_3993
            MMR: Mmar10_1382
            HNE: HNE_1770(pyrH)
            ZMO: ZMO1154(pyrH)
            NAR: Saro_1371
            SAL: Sala_1958
            ELI: ELI_03785
            GOX: GOX1812
            GBE: GbCGDNIH1_0934
            RRU: Rru_A1588
            MAG: amb2496
            MGM: Mmc1_1842
            ABA: Acid345_0259
            SUS: Acid_0904
            BSU: BG12675(smbA)
            BHA: BH2425(smbA)
            BAN: BA1797(pyrH) BA3963
            BAR: GBAA1797(pyrH) GBAA3963
            BAA: BA_2303 BA_4433
            BAT: BAS1665 BAS3676
            BCE: BC1738 BC3823
            BCA: BCE_1870(pyrH) BCE_3866
            BCZ: BCZK1612(pyrH) BCZK3584(smbA)
            BTK: BT9727_1647(pyrH) BT9727_3566(smbA)
            BTL: BALH_1580 BALH_3456
            BLI: BL01242(pyrH)
            BLD: BLi01872(pyrH)
            BCL: ABC2240(smbA)
            BPU: BPUM_1550
            OIH: OB1588(smbA)
            GKA: GK1251(smbA)
            SAU: SA1101(smbA)
            SAV: SAV1258(smbA)
            SAM: MW1141(smbA)
            SAR: SAR1234(pyrH)
            SAS: SAS1192
            SAC: SACOL1277(pyrH)
            SAB: SAB1120(smbA)
            SAA: SAUSA300_1151(pyrH)
            SAO: SAOUHSC_01235
            SEP: SE0934
            SER: SERP0825(pyrH)
            SHA: SH1656(smbA)
            SSP: SSP1510
            LMO: lmo1313(smbA)
            LMF: LMOf2365_1330(pyrH)
            LIN: lin1350(smbA)
            LWE: lwe1328(pyrH)
            LLA: L70624(pyrH)
            LLC: LACR_2292
            LLM: llmg_2285(pyrH)
            SPY: SPy_0462(pyrH)
            SPZ: M5005_Spy_0378(pyrH) M5005_Spy_0379
            SPM: spyM18_0505(pyrH)
            SPG: SpyM3_0326(pyrH)
            SPS: SPs1531
            SPH: MGAS10270_Spy0380(pyrH)
            SPI: MGAS10750_Spy0378(pyrH)
            SPJ: MGAS2096_Spy0397(pyrH)
            SPK: MGAS9429_Spy0379(pyrH)
            SPF: SpyM51489(pyrH)
            SPA: M6_Spy0404
            SPB: M28_Spy0365(pyrH)
            SPN: SP_0944
            SPR: spr0845(pyrH)
            SPD: SPD_0834(pyrH)
            SAG: SAG1513(pyrH)
            SAN: gbs1572(pyrH)
            SAK: SAK_1537(pyrH)
            SMU: SMU.1625(pyrH)
            STC: str0438(pyrH)
            STL: stu0438(pyrH)
            STE: STER_0474
            SSA: SSA_1620(pyrH)
            LPL: lp_2053(pyrH)
            LJO: LJ1498
            LAC: LBA1268
            LSA: LSA1263(pyrH)
            LSL: LSL_0561(pyrH)
            LDB: Ldb1343(pyrH)
            LBU: LBUL_1252
            LBR: LVIS_1348
            LCA: LSEI_1584
            LGA: LGAS_0803
            PPE: PEPE_0879
            EFA: EF2396(pyrH)
            OOE: OEOE_0977
            LME: LEUM_1197
            STH: STH1493
            CAC: CAC1789(smbA)
            CPE: CPE1698
            CPF: CPF_1952(pyrH)
            CPR: CPR_1670(pyrH)
            CTC: CTC01263
            CNO: NT01CX_2147(pyrH)
            CTH: Cthe_1004
            CDF: CD2138(pyrH)
            CHY: CHY_1785(pyrH)
            DSY: DSY2544
            SWO: Swol_0884
            TTE: TTE1407(pyrH)
            MTA: Moth_1034
            MGE: MG_434(pyrH)
            MPN: MPN632(pyrH)
            MPU: MYPU_2200(pyrH)
            MPE: MYPE9570(pyrH)
            MGA: MGA_0783(pyrH)
            MMY: MSC_0601(pyrH)
            MMO: MMOB0540(pyrH)
            MHY: mhp552(pyrH)
            MHJ: MHJ_0536(pyrH)
            MHP: MHP7448_0535(pyrH)
            MSY: MS53_0677(pyrH)
            MCP: MCAP_0374(pyrH)
            UUR: UU513(pyrH)
            POY: PAM167(pyrH)
            AYW: AYWB_552(pyrH)
            MFL: Mfl556
            MTU: Rv2883c(pyrH)
            MTC: MT2951(pyrH)
            MBO: Mb2907c(pyrH)
            MBB: BCG_2904c(pyrH)
            MLE: ML1591
            MPA: MAP2946c(pyrH)
            MAV: MAV_3733(pyrH)
            MSM: MSMEG_2540(pyrH)
            MUL: MUL_2074(pyrH)
            MVA: Mvan_2220
            MMC: Mmcs_2003
            MKM: Mkms_2049
            CGL: NCgl1948(cgl2024)
            CGB: cg2218(pyrH)
            CEF: CE1911
            CDI: DIP1506(pyrH)
            CJK: jk1173(pyrH)
            NFA: nfa41290(pyrH)
            RHA: RHA1_ro06580(pyrH)
            SCO: SCO5626(pyrH)
            SMA: SAV2625(pyrH)
            TWH: TWT447(pyrH)
            TWS: TW320(pyrH)
            LXX: Lxx12460(pyrH)
            ART: Arth_1369
            AAU: AAur_1505(pyrH)
            PAC: PPA1519
            TFU: Tfu_0678
            FRA: Francci3_4268
            FAL: FRAAL6542(pyrH)
            ACE: Acel_1540
            BLO: BL1505(pyrH)
            BAD: BAD_0783(pyrH)
            RXY: Rxyl_1400
            FNU: FN1622
            RBA: RB3884(pyrH)
            CTR: CT678(pyrH)
            CTA: CTA_0738(pyrH)
            CMU: TC0049
            CPN: CPn0698(pyrH)
            CPA: CP0048
            CPJ: CPj0698(pyrH)
            CPT: CpB0725
            CCA: CCA00044(pyrH)
            CAB: CAB045
            CFE: CF0961(pyrH)
            PCU: pc1877(pyrH)
            BBU: BB0571
            BGA: BG0582(smbA)
            BAF: BAPKO_0602(smbA)
            TPA: TP0099
            TDE: TDE2085
            LIL: LA3296(pyrH)
            LIC: LIC10852(pyrH)
            LBJ: LBJ_0906(pyrH)
            LBL: LBL_0921(pyrH)
            SYN: sll0144(pyrH)
            SYW: SYNW1752(pyrH)
            SYC: syc1014_c(pyrH)
            SYF: Synpcc7942_0506
            SYD: Syncc9605_0711
            SYE: Syncc9902_1648
            SYG: sync_2004(pyrH)
            CYA: CYA_2421(pyrH)
            CYB: CYB_2292(pyrH)
            TEL: tll0260(pyrH)
            GVI: gll2340(pyrH)
            ANA: alr1207
            AVA: Ava_0628
            PMA: Pro0522(pyrH)
            PMM: PMM0522(pyrH)
            PMT: PMT1244(pyrH)
            PMN: PMN2A_1854
            PMI: PMT9312_0522
            PMB: A9601_05781(pyrH)
            PMC: P9515_05861(pyrH)
            PMF: P9303_07621(pyrH)
            PME: NATL1_05791(pyrH)
            TER: Tery_3779
            BFR: BF0697
            BFS: BF0626
            PGI: PG1902(pyrH)
            SRU: SRU_0034(pyrH)
            CHU: CHU_0577(pyrH)
            GFO: GFO_0100(pyrH)
            FPS: FP0435(pyrH)
            CTE: CT1779(pyrH)
            CCH: Cag_1646
            CPH: Cpha266_2008
            PLT: Plut_0405
            DET: DET0375(pyrH)
            DEH: cbdb_A319(pyrH)
            DRA: DR_1511
            DGE: Dgeo_1047
            TTH: TTC0507
            TTJ: TTHA0859
            AAE: aq_713(pyrH)
            TMA: TM1604
            MJA: MJ1259
            MMP: MMP0385(pyrH)
            MAC: MA0372(pyrH)
            MBA: Mbar_A0788
            MMA: MM_1611
            MBU: Mbur_1569
            MTP: Mthe_1152
            MHU: Mhun_1051
            MTH: MTH879
            MST: Msp_1362(pyrH)
            MKA: MK0760(pyrH)
            AFU: AF2042(pyrH)
            HAL: VNG2015C
            HMA: rrnAC3174(pyrH)
            HWA: HQ1098A(pyrH)
            NPH: NP2272A(pyrH)
            TAC: Ta0486
            TVO: TVN0586
            PTO: PTO1444
            PHO: PH1408
            PAB: PAB1870(pyrH)
            PFU: PF1407
            TKO: TK0305
            APE: APE_0401.1
            HBU: Hbut_1037
            SSO: SSO0976(pyrH)
            STO: ST1300
            SAI: Saci_1306
            PAI: PAE3159(pyrH)
            PIS: Pisl_0530
            TPE: Tpen_0518
STRUCTURES  PDB: 2J4J  2J4K  2J4L  2VA1  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.22
            ExPASy - ENZYME nomenclature database: 2.7.4.22
            ExplorEnz - The Enzyme Database: 2.7.4.22
            ERGO genome analysis and discovery system: 2.7.4.22
            BRENDA, the Enzyme Database: 2.7.4.22
///
ENTRY       EC 2.7.4.23                 Enzyme
NAME        ribose 1,5-bisphosphate phosphokinase;
            ribose 1,5-bisphosphokinase;
            PhnN
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:ribose-1,5-bisphosphate phosphotransferase
REACTION    ATP + ribose 1,5-bisphosphate = ADP + 5-phospho-alpha-D-ribose
            1-diphosphate [RN:R06836]
ALL_REAC    R06836
SUBSTRATE   ATP [CPD:C00002];
            ribose 1,5-bisphosphate [CPD:C01151]
PRODUCT     ADP [CPD:C00008];
            5-phospho-alpha-D-ribose 1-diphosphate [CPD:C00119]
COMMENT     This enzyme, found in NAD supression mutants of Escherichia coli,
            synthesizes 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) without
            the participation of EC 2.7.6.1, ribose-phosphate diphosphokinase.
            Ribose, ribose 1-phosphate and ribose 5-phosphate are not
            substrates, and GTP cannot act as a phosphate donor.
REFERENCE   1  [PMID:12700258]
  AUTHORS   Hove-Jensen B, Rosenkrantz TJ, Haldimann A, Wanner BL.
  TITLE     Escherichia coli phnN, encoding ribose 1,5-bisphosphokinase activity
            (phosphoribosyl diphosphate forming): dual role in phosphonate
            degradation and NAD biosynthesis pathways.
  JOURNAL   J. Bacteriol. 185 (2003) 2793-801.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00030  Pentose phosphate pathway
ORTHOLOGY   KO: K05774  ribose 1,5-bisphosphokinase
GENES       ECO: b4094(phnN)
            ECJ: JW4055(phnN)
            ECE: Z5697(phnN)
            ECS: ECs5077
            ECI: UTI89_C4689(phnN)
            ECP: ECP_4337
            ECV: APECO1_2356(phnN)
            YPE: YPO3464(phnN)
            YPK: y0721(phnN)
            YPM: YP_0619(phnN)
            YPA: YPA_2966
            YPN: YPN_0623
            YPS: YPTB0509(phnN)
            YEN: YE0470(phnN)
            SSN: SSON_4270(phnN)
            SBO: SBO_4120(phnN)
            SDY: SDY_4122(phnN)
            ECA: ECA0497(phnN)
            PAE: PA3373
            PAU: PA14_20440(phnN)
            PPU: PP_4469(gmk-1)
            PST: PSPTO_2566(phnN)
            PSB: Psyr_2258
            PSP: PSPPH_2929(phnN)
            PFO: Pfl_4269
            PEN: PSEEN3864(phnN)
            PIN: Ping_3685
            MAQ: Maqu_0224
            TCX: Tcr_2089
            CVI: CV_1849(phnN)
            REU: Reut_B4182
            REH: H16_B1291(phnN)
            RME: Rmet_0770
            BMA: BMA2397(phnN)
            BMV: BMASAVP1_A0313(phnN)
            BML: BMA10299_A1174(phnN)
            BMN: BMA10247_2583(phnN)
            BXE: Bxe_B2176
            BPS: BPSL2860(phnN)
            BPM: BURPS1710b_3359(phnN)
            BPL: BURPS1106A_3349(phnN)
            BPD: BURPS668_3315(phnN)
            RFR: Rfer_0148
            VEI: Veis_2955
            MPT: Mpe_B0431(htxM)
            TBD: Tbd_2289
            DDE: Dde_3336
            MLO: mll9141
            MES: Meso_3660
            SME: SMb21170
            ATU: Atu0168(gmk)
            ATC: AGR_C_277
            RET: RHE_CH00154(gmk1)
            RLE: RL0163(phnN)
            BME: BMEI0882
            BMF: BAB1_1123
            BMS: BR1099
            BMB: BruAb1_1105
            BJA: blr1228(gmk)
            RPA: RPA0688(phnN)
            RPB: RPB_4096
            RPC: RPC_1279
            RPD: RPD_3832
            RPE: RPE_3103
            SIL: SPO0474(phnN)
            SIT: TM1040_3697
            JAN: Jann_2855
            RDE: RD1_2388(phnN)
            PDE: Pden_4776
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.23
            ExPASy - ENZYME nomenclature database: 2.7.4.23
            ExplorEnz - The Enzyme Database: 2.7.4.23
            ERGO genome analysis and discovery system: 2.7.4.23
            BRENDA, the Enzyme Database: 2.7.4.23
///
ENTRY       EC 2.7.4.24                 Enzyme
NAME        diphosphoinositol-pentakisphosphate kinase;
            PP-IP5 kinase;
            diphosphoinositol pentakisphosphate kinase;
            ATP:5-diphospho-1D-myo-inositol-pentakisphosphate phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with a phosphate group as acceptor
SYSNAME     ATP:1D-myo-inositol-5-diphosphate-pentakisphosphate
            phosphotransferase
REACTION    ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate = ADP +
            1D-myo-inositol bisdiphosphate tetrakisphosphate (isomeric
            configuration unknown)
SUBSTRATE   ATP [CPD:C00002];
            1D-myo-inositol 5-diphosphate pentakisphosphate
PRODUCT     ADP [CPD:C00008];
            1D-myo-inositol bisdiphosphate tetrakisphosphate (isomeric
            configuration unknown)
REFERENCE   1  [PMID:7737983]
  AUTHORS   Shears SB, Ali N, Craxton A, Bembenek ME.
  TITLE     Synthesis and metabolism of bis-diphosphoinositol tetrakisphosphate
            in vitro and in vivo.
  JOURNAL   J. Biol. Chem. 270 (1995) 10489-97.
REFERENCE   2  [PMID:9359429]
  AUTHORS   Albert C, Safrany ST, Bembenek ME, Reddy KM, Reddy K, Falck J,
            Brocker M, Shears SB, Mayr GW.
  TITLE     Biological variability in the structures of diphosphoinositol
            polyphosphates in Dictyostelium discoideum and mammalian cells.
  JOURNAL   Biochem. J. 327 ( Pt 2) (1997) 553-60.
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.4.24
            ExPASy - ENZYME nomenclature database: 2.7.4.24
            ExplorEnz - The Enzyme Database: 2.7.4.24
            ERGO genome analysis and discovery system: 2.7.4.24
            BRENDA, the Enzyme Database: 2.7.4.24
///
ENTRY       EC 2.7.5.1        Obsolete  Enzyme
NAME        Transferred to 5.4.2.2
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with regeneration of donors, apparently
            catalysing intramolecular transfers (deleted sub-subclass)
COMMENT     Transferred entry: now EC 5.4.2.2 phosphoglucomutase (EC 2.7.5.1
            created 1961, deleted 1984)
STRUCTURES  PDB: 1C47  1C4G  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.5.1
            ExPASy - ENZYME nomenclature database: 2.7.5.1
            ExplorEnz - The Enzyme Database: 2.7.5.1
            ERGO genome analysis and discovery system: 2.7.5.1
            BRENDA, the Enzyme Database: 2.7.5.1
///
ENTRY       EC 2.7.5.2        Obsolete  Enzyme
NAME        Transferred to 5.4.2.3
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with regeneration of donors, apparently
            catalysing intramolecular transfers (deleted sub-subclass)
COMMENT     Transferred entry: now EC 5.4.2.3 phosphoacetylglucosamine mutase
            (EC 2.7.5.2 created 1961, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.5.2
            ExPASy - ENZYME nomenclature database: 2.7.5.2
            ExplorEnz - The Enzyme Database: 2.7.5.2
            ERGO genome analysis and discovery system: 2.7.5.2
            BRENDA, the Enzyme Database: 2.7.5.2
///
ENTRY       EC 2.7.5.3        Obsolete  Enzyme
NAME        Transferred to 5.4.2.1
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with regeneration of donors, apparently
            catalysing intramolecular transfers (deleted sub-subclass)
COMMENT     Transferred entry: now EC 5.4.2.1, phosphoglycerate mutase (EC
            2.7.5.3 created 1961, deleted 1984)
STRUCTURES  PDB: 3PGM  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.5.3
            ExPASy - ENZYME nomenclature database: 2.7.5.3
            ExplorEnz - The Enzyme Database: 2.7.5.3
            ERGO genome analysis and discovery system: 2.7.5.3
            BRENDA, the Enzyme Database: 2.7.5.3
///
ENTRY       EC 2.7.5.4        Obsolete  Enzyme
NAME        Transferred to 5.4.2.4
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with regeneration of donors, apparently
            catalysing intramolecular transfers (deleted sub-subclass)
COMMENT     Transferred entry: now EC 5.4.2.4, bisphosphoglycerate mutase (EC
            2.7.5.4 created 1961, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.5.4
            ExPASy - ENZYME nomenclature database: 2.7.5.4
            ExplorEnz - The Enzyme Database: 2.7.5.4
            ERGO genome analysis and discovery system: 2.7.5.4
            BRENDA, the Enzyme Database: 2.7.5.4
///
ENTRY       EC 2.7.5.5        Obsolete  Enzyme
NAME        Transferred to 5.4.2.5
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with regeneration of donors, apparently
            catalysing intramolecular transfers (deleted sub-subclass)
COMMENT     Transferred entry: now EC 5.4.2.5, phosphoglucomutase
            (glucose-cofactor) (EC 2.7.5.5 created 1972, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.5.5
            ExPASy - ENZYME nomenclature database: 2.7.5.5
            ExplorEnz - The Enzyme Database: 2.7.5.5
            ERGO genome analysis and discovery system: 2.7.5.5
            BRENDA, the Enzyme Database: 2.7.5.5
///
ENTRY       EC 2.7.5.6        Obsolete  Enzyme
NAME        Transferred to 5.4.2.7
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with regeneration of donors, apparently
            catalysing intramolecular transfers (deleted sub-subclass)
COMMENT     Transferred entry: now EC 5.4.2.7 phosphopentomutase (EC 2.7.5.6
            created 1972, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.5.6
            ExPASy - ENZYME nomenclature database: 2.7.5.6
            ExplorEnz - The Enzyme Database: 2.7.5.6
            ERGO genome analysis and discovery system: 2.7.5.6
            BRENDA, the Enzyme Database: 2.7.5.6
///
ENTRY       EC 2.7.5.7        Obsolete  Enzyme
NAME        Transferred to 5.4.2.8
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with regeneration of donors, apparently
            catalysing intramolecular transfers (deleted sub-subclass)
COMMENT     Transferred entry: now EC 5.4.2.8 phosphomannomutase (EC 2.7.5.7
            created 1981, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.5.7
            ExPASy - ENZYME nomenclature database: 2.7.5.7
            ExplorEnz - The Enzyme Database: 2.7.5.7
            ERGO genome analysis and discovery system: 2.7.5.7
            BRENDA, the Enzyme Database: 2.7.5.7
///
ENTRY       EC 2.7.6.1                  Enzyme
NAME        ribose-phosphate diphosphokinase;
            ribose-phosphate pyrophosphokinase;
            PRPP synthetase;
            phosphoribosylpyrophosphate synthetase;
            PPRibP synthetase;
            PP-ribose P synthetase;
            5-phosphoribosyl-1-pyrophosphate synthetase;
            5-phosphoribose pyrophosphorylase;
            5-phosphoribosyl-alpha-1-pyrophosphate synthetase;
            phosphoribosyl-diphosphate synthetase;
            phosphoribosylpyrophosphate synthase;
            pyrophosphoribosylphosphate synthetase;
            ribophosphate pyrophosphokinase;
            ribose-5-phosphate pyrophosphokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Diphosphotransferases
SYSNAME     ATP:D-ribose-5-phosphate diphosphotransferase
REACTION    ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose
            1-diphosphate [RN:R01049]
ALL_REAC    R01049
SUBSTRATE   ATP [CPD:C00002];
            D-ribose 5-phosphate [CPD:C00117]
PRODUCT     AMP [CPD:C00020];
            5-phospho-alpha-D-ribose 1-diphosphate [CPD:C00119]
COMMENT     dATP can also act as donor.
REFERENCE   1  [PMID:14944530]
  AUTHORS   HUGHES DE, WILLIAMSON DH.
  TITLE     Some properties of the glutaminase of Clostridium welchii.
  JOURNAL   Biochem. J. 51 (1952) 45-55.
  ORGANISM  Clostridium welchii
REFERENCE   2
  AUTHORS   Hurlbert, R.B. and Reichard, P.
  TITLE     The conversion of orotic acid to uridine nucleotides in vitro.
  JOURNAL   Acta Chem. Scand. 9 (1955) 251-262.
  ORGANISM  chicken [GN:gga]
REFERENCE   3
  AUTHORS   Remy, C.N., Remy, W.T. and Buchanan, J.M.
  TITLE     Biosynthesis of the purines. VIII. Enzymatic synthesis and
            utilization of alpha-5-phosphoribosylpyrophosphate.
  JOURNAL   J. Biol. Chem. 217 (1955) 885-895.
  ORGANISM  pigeon
REFERENCE   4  [PMID:4306285]
  AUTHORS   Switzer RL.
  TITLE     Regulation and mechanism of phosphoribosylpyrophosphate synthetase.
            I. Purification and properties of the enzyme from Salmonella
            typhimurium.
  JOURNAL   J. Biol. Chem. 244 (1969) 2854-63.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00030  Pentose phosphate pathway
            PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K00948  ribose-phosphate pyrophosphokinase
GENES       HSA: 221823(PRPS1L1) 5631(PRPS1) 5634(PRPS2)
            PTR: 465800(PRPS1) 472640(PRPS1L1)
            MCC: 702529(LOC702529)
            MMU: 110639(Prps2) 19139(Prps1)
            RNO: 24689(Prps2) 29562(Prps1)
            CFA: 476855(PRPS2)
            GGA: 418639(PRPS2)
            XLA: 380347(prps2)
            XTR: 394745(MGC75987) 496485(LOC496485)
            SPU: 585120(LOC585120)
            DME: Dmel_CG6767
            CEL: R151.2 W04G3.5
            ATH: AT1G32380 AT2G44530
            OSA: 4328168 4341535
            CME: CMM249C CMT113C CMT292C
            SCE: YBL068W(PRS4) YER099C(PRS2) YHL011C(PRS3) YKL181W(PRS1)
                 YOL061W(PRS5)
            AGO: AGOS_ADR314C AGOS_AER083C AGOS_AGL080C AGOS_AGR371C
            PIC: PICST_34307(KPR4) PICST_65580(PRS1) PICST_66107(PRS2)
                 PICST_78248(PRS5)
            CGR: CAGL0C05181g CAGL0D00550g CAGL0I05500g CAGL0K02541g
            SPO: SPAC4A8.14(prs1) SPBC3D6.06c SPCC1620.06c
            ANI: AN1965.2 AN3169.2 AN6711.2
            AFM: AFUA_3G13380 AFUA_4G10790 AFUA_7G05670
            AOR: AO090003001133 AO090005000432 AO090012000798
            CNE: CNG02440
            UMA: UM03306.1 UM06080.1
            DDI: DDBDRAFT_0168827 DDBDRAFT_0185586 DDBDRAFT_0186131
            PFA: PF13_0143 PF13_0157
            TAN: TA16730
            TPV: TP01_0994
            TET: TTHERM_00522760 TTHERM_00537300
            TBR: Tb10.6k15.0970 Tb11.02.0530 Tb927.5.2960 Tb927.5.3170
            TCR: 506321.310 506839.80 507773.60 507809.30 508717.30 510431.250
                 511661.90
            LMA: LmjF08.0510 LmjF08.1130 LmjF33.1930 LmjF36.5390
            EHI: 114.t00014 17.t00052
            ECO: b1207(prsA)
            ECJ: JW1198(prsA)
            ECE: Z1978(prsA)
            ECS: ECs1712
            ECC: c1665(prsA)
            ECI: UTI89_C1401(prsA)
            ECP: ECP_1255
            ECV: APECO1_323(prsA)
            ECW: EcE24377A_1355(prs)
            ECX: EcHS_A1312
            STY: STY1906(prsA)
            STT: t1096(prsA)
            SPT: SPA1093(prsA)
            SEC: SC1774(prsA)
            STM: STM1780(prsA)
            YPE: YPO2013(prsA)
            YPK: y2295(prsA)
            YPM: YP_1861(prsA)
            YPA: YPA_1396
            YPN: YPN_1494
            YPP: YPDSF_1106
            YPS: YPTB2001(prsA)
            YPI: YpsIP31758_2070(prs)
            SFL: SF1210(prsA)
            SFX: S1294(prsA)
            SFV: SFV_1221(prsA)
            SSN: SSON_1971(prsA)
            SBO: SBO_1860(prsA)
            SDY: SDY_1256(prsA)
            ECA: ECA2186(prs)
            PLU: plu2066(prsA)
            BUC: BU169(prsA)
            BAS: BUsg163(prsA)
            BAB: bbp159(prsA)
            BCC: BCc_110(prsA)
            WBR: WGLp349(prsA)
            SGL: SG1880
            ENT: Ent638_2341
            KPN: KPN_02238(prsA)
            SPE: Spro_1986
            BFL: Bfl346(prsA)
            BPN: BPEN_356(prsA)
            HIN: HI1609(prsA)
            HIT: NTHI1433(prsA)
            HIP: CGSHiEE_05695
            HIQ: CGSHiGG_10075
            HDU: HD1627(prsA)
            HSO: HS_0996(prs)
            PMU: PM0244(prsA)
            MSU: MS1536(prsA)
            APL: APL_0775(prsA)
            ASU: Asuc_1752
            XFA: XF2644
            XFT: PD2016(prsA)
            XCC: XCC0873(prsA)
            XCB: XC_3358
            XCV: XCV0980(prsA)
            XAC: XAC0950(prsA)
            XOO: XOO3603
            XOM: XOO_3405(XOO3405)
            VCH: VC2183
            VCO: VC0395_A1760(prsA)
            VVU: VV1_0257
            VVY: VV0926
            VPA: VP0739
            VFI: VF0764
            PPR: PBPRA2849
            PAE: PA4670(prs)
            PAU: PA14_61770(prs)
            PPU: PP_0722(prsA)
            PPF: Pput_0756 Pput_3009
            PST: PSPTO_1104(prsA)
            PSB: Psyr_0944
            PSP: PSPPH_0991(prsA)
            PFL: PFL_5165(prs)
            PFO: Pfl_4753
            PEN: PSEEN0857(prs)
            PMY: Pmen_1055
            PAR: Psyc_0172(prsA)
            PCR: Pcryo_0185
            PRW: PsycPRwf_2105
            ACI: ACIAD0964 ACIAD2907(prs)
            SON: SO_3837(prsA)
            SDN: Sden_0916
            SFR: Sfri_0719
            SAZ: Sama_2570
            SBL: Sbal_0692
            SBM: Shew185_3618
            SLO: Shew_2916
            SPC: Sputcn32_0797 Sputcn32_2327
            SSE: Ssed_3463
            SPL: Spea_3130
            SHE: Shewmr4_3173
            SHM: Shewmr7_0793
            SHN: Shewana3_0765
            SHW: Sputw3181_1681 Sputw3181_3378
            ILO: IL0929(prsA)
            CPS: CPS_3557(prsA)
            PHA: PSHAa1054(prs)
            PAT: Patl_2567
            SDE: Sde_3256
            PIN: Ping_0911
            MAQ: Maqu_2365
            CBU: CBU_1830(prsA)
            CBD: COXBU7E912_0060(prs)
            LPN: lpg0543(prsA) lpg1023
            LPF: lpl0588(prs)
            LPP: lpp0607(prs) lpp2358
            MCA: MCA1056(prsA) MCA1716
            FTU: FTT0674(prsA)
            FTF: FTF0674(prsA)
            FTW: FTW_1054(prsA)
            FTL: FTL_0949
            FTH: FTH_0927(prsA)
            FTA: FTA_0999
            FTN: FTN_1008(prsA)
            TCX: Tcr_0392
            NOC: Noc_0514 Noc_0983
            AEH: Mlg_0283 Mlg_1731
            HHA: Hhal_0989
            HCH: HCH_00912 HCH_01517(prsA) HCH_01726(prs)
            CSA: Csal_1524
            ABO: ABO_0518
            MMW: Mmwyl1_3604
            AHA: AHA_3154
            DNO: DNO_0065(prsA)
            BCI: BCI_0293(prsA)
            RMA: Rmag_0109
            VOK: COSY_0113(prsA)
            NME: NMB0875
            NMA: NMA1093(prsA)
            NMC: NMC0816(prsA)
            NGO: NGO0441
            CVI: CV_0033 CV_4058(prsA)
            RSO: RSc0202(RS00634) RSc0395(prsA)
            REU: Reut_A0342
            REH: H16_A0372(prsA)
            RME: Rmet_0289
            BMA: BMA3120(prsA)
            BMV: BMASAVP1_A0088(prsA)
            BML: BMA10299_A1502(prsA)
            BMN: BMA10247_2930(prsA)
            BXE: Bxe_A4133
            BVI: Bcep1808_2907
            BUR: Bcep18194_A6132
            BCN: Bcen_2188
            BCH: Bcen2424_2802
            BAM: Bamb_2862
            BPS: BPSL0521(prs)
            BPM: BURPS1710b_0753(prsA)
            BPL: BURPS1106A_0585(prs)
            BPD: BURPS668_0569(prs)
            BTE: BTH_I0474 BTH_II0918
            PNU: Pnuc_1920
            BPE: BP3125(prsA)
            BPA: BPP0817(prsA)
            BBR: BB0901(prsA)
            RFR: Rfer_0392 Rfer_1660 Rfer_2240
            POL: Bpro_1193 Bpro_1293
            PNA: Pnap_0899
            AAV: Aave_3610
            AJS: Ajs_0895 Ajs_1506 Ajs_2689
            VEI: Veis_0951
            MPT: Mpe_A3229
            HAR: HEAR2893(prs)
            MMS: mma_3128
            NEU: NE1826
            NET: Neut_1140
            NMU: Nmul_A0589
            EBA: ebA1406 ebA3224
            AZO: azo0755(prsA)
            DAR: Daro_3730
            TBD: Tbd_0387 Tbd_1465
            MFA: Mfla_0678
            HPY: HP0742
            HPA: HPAG1_0726
            HHE: HH1536(prsA)
            HAC: Hac_0677(prsA)
            WSU: WS1635(prsA)
            TDN: Tmden_1636
            CJE: Cj0918c(prsA)
            CJR: CJE0996(prsA)
            CJJ: CJJ81176_0925(prsA)
            CJU: C8J_0855(prsA)
            CJD: JJD26997_0896(prsA)
            CFF: CFF8240_1474
            CCV: CCV52592_0207 CCV52592_1446(prs)
            CHA: CHAB381_1256
            CCO: CCC13826_1015
            ABU: Abu_0482(prsA)
            NIS: NIS_0435(prsA)
            SUN: SUN_1045(prsA)
            GSU: GSU0661(prsA)
            GME: Gmet_2848
            GUR: Gura_3682
            PCA: Pcar_2004
            PPD: Ppro_0743
            DVU: DVU1575(prsA)
            DVL: Dvul_1558
            DDE: Dde_2126
            LIP: LI0736(prsA)
            BBA: Bd2704(prs)
            DPS: DP2734
            ADE: Adeh_0121
            AFW: Anae109_0125 Anae109_4122
            MXA: MXAN_5075(prs)
            SAT: SYN_02767
            SFU: Sfum_1208 Sfum_3652
            RFE: RF_0078(prs)
            RBE: RBE_1338(prs)
            WOL: WD0036(prsA)
            WBM: Wbm0103
            AMA: AM1028(prsA)
            APH: APH_1112(prsA)
            ERU: Erum7900(prsA)
            ERW: ERWE_CDS_08360(prs)
            ERG: ERGA_CDS_08250(prs)
            ECN: Ecaj_0826
            ECH: ECH_1024(prsA)
            NSE: NSE_0816(prs)
            PUB: SAR11_0094(prsA)
            MLO: mlr2685
            MES: Meso_2155 Meso_3877
            PLA: Plav_2258 Plav_3458
            SME: SMc02686(prsA)
            SMD: Smed_2257
            ATU: Atu2218(prsA)
            ATC: AGR_C_4031(prsA)
            RET: RHE_CH03023(prsAch)
            RLE: RL3468(prs)
            BME: BMEI0483
            BMF: BAB1_1549
            BMS: BR1533(prsA)
            BMB: BruAb1_1522(prsA)
            BOV: BOV_1482(prsA)
            OAN: Oant_1634
            BJA: bll3116 blr7448(prsA)
            BRA: BRADO6000(prs)
            BBT: BBta_1761(prs)
            RPA: RPA4148(prsA) RPA4362(ribP)
            RPB: RPB_4168
            RPC: RPC_1409
            RPD: RPD_1442 RPD_3879
            RPE: RPE_1430 RPE_4148
            NWI: Nwi_2501
            NHA: Nham_1899 Nham_3091
            BHE: BH11830(prsA)
            BQU: BQ03310(prsA)
            BBK: BARBAKC583_0998(prs)
            XAU: Xaut_2553
            CCR: CC_0487
            SIL: SPO3159(prs)
            SIT: TM1040_2075
            RSP: RSP_2301(prsA)
            RSH: Rsph17029_0976
            RSQ: Rsph17025_2199
            JAN: Jann_1053
            RDE: RD1_3528
            PDE: Pden_3823
            MMR: Mmar10_0190 Mmar10_0759
            HNE: HNE_0362(prs)
            ZMO: ZMO1519(prsA)
            NAR: Saro_0971
            SAL: Sala_2472 Sala_2942
            SWI: Swit_2438
            ELI: ELI_13790
            GOX: GOX0964
            GBE: GbCGDNIH1_2314
            ACR: Acry_0239 Acry_2059
            RRU: Rru_A0645
            MAG: amb0590
            MGM: Mmc1_0820
            ABA: Acid345_4540
            SUS: Acid_7096
            BSU: BG10114(prs)
            BHA: BH0066(prs)
            BAN: BA0049(prs)
            BAR: GBAA0049(prs)
            BAA: BA_0638
            BAT: BAS0049
            BCE: BC0055
            BCA: BCE_0048(prs)
            BCZ: BCZK0045(prs)
            BCY: Bcer98_0045
            BTK: BT9727_0045(prs)
            BTL: BALH_0045(prs)
            BLI: BL00519(prs)
            BLD: BLi00064(prs)
            BCL: ABC0079(prs) ABC3150
            BAY: RBAM_000600
            BPU: BPUM_0035
            OIH: OB0059
            GKA: GK0044(prs)
            GTN: GTNG_0044
            SAU: SA0458(prs)
            SAV: SAV0500(prs)
            SAM: MW0455(prs)
            SAR: SAR0501(prs)
            SAS: SAS0457
            SAC: SACOL0544(prsA)
            SAB: SAB0449(prs)
            SAA: SAUSA300_0478(prs)
            SAO: SAOUHSC_00472
            SAJ: SaurJH9_0522
            SAH: SaurJH1_0535
            SEP: SE2283
            SER: SERP0138(prsA)
            SHA: SH2511(prs)
            SSP: SSP2256
            LMO: lmo0199(prs) lmo0509(prs)
            LMF: LMOf2365_0210(prs-1) LMOf2365_0538(prs-2)
            LIN: lin0238(prs) lin0509(prs)
            LWE: lwe0168(prs) lwe0466(prs)
            LLA: L109335(prsB) L25614(prsA)
            LLC: LACR_0873 LACR_2049
            LLM: llmg_1743(prsA) llmg_2046(prsB)
            SPY: SPy_0020(prsA.2) SPy_1123(prs)
            SPZ: M5005_Spy_0018(prsA.2) M5005_Spy_0845
            SPM: spyM18_0021(prsA) spyM18_1084(prsA)
            SPG: SpyM3_0015(prsA) SpyM3_0782(prs)
            SPS: SPs0016 SPs0983
            SPH: MGAS10270_Spy0018(prsA2) MGAS10270_Spy0961
            SPI: MGAS10750_Spy0018(prsA2) MGAS10750_Spy0996
            SPJ: MGAS2096_Spy0019(prsA2) MGAS2096_Spy0920
            SPK: MGAS9429_Spy0018(prsA2) MGAS9429_Spy0964
            SPF: SpyM50016(prs1) SpyM50943(prs2)
            SPA: M6_Spy0018 M6_Spy0843
            SPB: M28_Spy0018(prsA) M28_Spy0821
            SPN: SP_0027 SP_1095
            SPR: spr0028(prsA) spr1002(prs)
            SPD: SPD_0033(prsA) SPD_0980(prs2)
            SAG: SAG0018(prsA-1) SAG1097(prsA-2)
            SAN: gbs0017 gbs1164
            SAK: SAK_0051(prs) SAK_1182(prs)
            SMU: SMU.1050(krpS) SMU.23(prs)
            STC: str0023(prsA1) str1460(prsA2)
            STL: stu0023(prsA1) stu1460(prsA2)
            STE: STER_0043
            SSA: SSA_0020(prsA) SSA_1212(prs)
            SSU: SSU05_0021
            SSV: SSU98_0024
            SGO: SGO_1224 SGO_2106
            LPL: lp_0471(prs1) lp_2166(prs2)
            LJO: LJ0103 LJ0209
            LAC: LBA0131 LBA0224(prsA)
            LSA: LSA1646(prs)
            LSL: LSL_0318(prsA) LSL_1610(prsA)
            LDB: Ldb0180(prs2) Ldb0350(prs1)
            LBU: LBUL_0156 LBUL_0305
            LBR: LVIS_0476 LVIS_1430
            LCA: LSEI_2584 LSEI_2882
            LGA: LGAS_0101 LGAS_0212
            LRE: Lreu_0221 Lreu_0609
            PPE: PEPE_0295 PEPE_1168
            EFA: EF2073(prsA-1) EF3163(prsA-2)
            OOE: OEOE_0160
            LME: LEUM_0697 LEUM_1951
            STH: STH3239
            CAC: CAC0819 CAC3221(prs)
            CPE: CPE1549(prs) CPE2489(prs)
            CPF: CPF_1800(prs) CPF_2812(prsA)
            CPR: CPR_1519(prs) CPR_2498(prsA)
            CTC: CTC00188
            CNO: NT01CX_1015
            CTH: Cthe_2630
            CDF: CD3514(prs)
            CBO: CBO3544(prs)
            CBA: CLB_3625(prs)
            CBH: CLC_3522(prs)
            CBF: CLI_3764(prsA-2)
            CBE: Cbei_0082 Cbei_2432
            CKL: CKL_0147(prs)
            AMT: Amet_0157
            CHY: CHY_0193(prs)
            DSY: DSY0153
            DRM: Dred_0100
            PTH: PTH_0105(prsA)
            SWO: Swol_0068
            CSC: Csac_1204
            TTE: TTE2571(prsA)
            MTA: Moth_0076
            MGE: MG_058(prs)
            MPN: MPN073(prs)
            MPU: MYPU_1270(prs)
            MPE: MYPE9450
            MGA: MGA_0348(prsA)
            MMY: MSC_0952(prs)
            MMO: MMOB5660(prsA)
            MHY: mhp675(prsA)
            MHJ: MHJ_0654(prsA)
            MHP: MHP7448_0654(prsA)
            MSY: MS53_0150(prsA)
            MCP: MCAP_0104(prs)
            UUR: UU193(prsA)
            MFL: Mfl076
            MTU: Rv1017c(prsA)
            MTC: MT1045(prsA)
            MBO: Mb1045c(prsA)
            MBB: BCG_1074c(prsA)
            MLE: ML0248(prsA)
            MPA: MAP0983c(prsA)
            MAV: MAV_1156
            MSM: MSMEG_5427
            MVA: Mvan_4783
            MGI: Mflv_1943
            MMC: Mmcs_4249
            MKM: Mkms_4335
            MJL: Mjls_4628
            CGL: NCgl0905(cgl0942)
            CGB: cg1075(prsA)
            CEF: CE1015
            CDI: DIP0903(prsA)
            CJK: jk1493(prsA)
            NFA: nfa48790(prsA)
            RHA: RHA1_ro05723(prsA)
            SCO: SCO0782(3SCF60.14c) SCO3123(prsA2)
            SMA: SAV3562(prsA1) SAV7451(prsA2)
            TWH: TWT187(prsA)
            TWS: TW585(prsA)
            LXX: Lxx17420(psrA)
            CMI: CMM_2274(prsA)
            ART: Arth_1218
            AAU: AAur_1344(prs)
            PAC: PPA0531
            NCA: Noca_0909
            TFU: Tfu_0415
            FRA: Francci3_2600 Francci3_3962
            FAL: FRAAL3625(prs) FRAAL6283(prs)
            ACE: Acel_1946
            KRA: Krad_0165 Krad_1052
            SEN: SACE_0816(prsA) SACE_2398(prsA)
            STP: Strop_0789 Strop_3725
            BLO: BL0418(prsA1) BL0963(prsA2)
            BAD: BAD_0898(prsA2) BAD_1484(prsA1)
            RXY: Rxyl_0895
            FNU: FN1992
            RBA: RB6844(prsA)
            CCA: CCA00569(prsA)
            CFE: CF0433(kprS)
            PCU: pc1595(prsA)
            BGA: BG0554(prs)
            BAF: BAPKO_0573(prs)
            TPA: TP0294
            TDE: TDE2723(prs)
            LIL: LA3822(prsA)
            LIC: LIC10429(prs)
            LBJ: LBJ_2587(prsA)
            LBL: LBL_0525(prsA)
            SYN: sll0469(prsA)
            SYW: SYNW0966(kprS)
            SYC: syc1979_c(kprS)
            SYF: Synpcc7942_2113
            SYD: Syncc9605_1610
            SYE: Syncc9902_1371
            SYG: sync_1011(prs)
            SYR: SynRCC307_0771(prs)
            SYX: SynWH7803_1553(prs)
            CYA: CYA_2887(prs)
            CYB: CYB_1652(prs)
            TEL: tlr1546
            GVI: gll0901
            ANA: alr4670
            AVA: Ava_1994 Ava_4123
            PMA: Pro1118(prsA)
            PMM: PMM1080(kprS)
            PMT: PMT1074(kprS)
            PMN: PMN2A_0670
            PMI: PMT9312_1091
            PMB: A9601_11861(prsA)
            PMC: P9515_11701(prsA)
            PMF: P9303_09761(prsA)
            PMG: P9301_11871(prsA)
            PMH: P9215_12161
            PME: NATL1_15031(prsA)
            TER: Tery_0597
            BTH: BT_0748
            BFR: BF2231
            BFS: BF2280(prs)
            PGI: PG2097(prsA)
            SRU: SRU_0459(prsA) SRU_0815
            CHU: CHU_2422(prsA) CHU_2627(prsA)
            GFO: GFO_3498(prs)
            FJO: Fjoh_0755 Fjoh_1126
            FPS: FP0147(prsA)
            CTE: CT1361(prsA)
            CCH: Cag_1155
            CPH: Cpha266_1674
            PVI: Cvib_0712
            PLT: Plut_1341
            DET: DET0435(prs)
            DEH: cbdb_A389(prs)
            DEB: DehaBAV1_0412
            RRS: RoseRS_0965 RoseRS_4394 RoseRS_4537
            RCA: Rcas_0083 Rcas_0737 Rcas_3812
            DRA: DR_1456
            DGE: Dgeo_0452
            TTH: TTC1184 TTC1274
            TTJ: TTHA1549 TTHA1637
            AAE: aq_1636(prs)
            TMA: TM1628
            TPT: Tpet_1163
            TME: Tmel_0161
            FNO: Fnod_0604
            MJA: MJ1366(prsA)
            MMP: MMP0410(prsA)
            MMQ: MmarC5_1228
            MMZ: MmarC7_1408
            MAE: Maeo_0167
            MVN: Mevan_1398
            MAC: MA1167(prs)
            MBA: Mbar_A0363
            MMA: MM_2205
            MBU: Mbur_1877
            MTP: Mthe_0412
            MHU: Mhun_0975
            MEM: Memar_0275
            MBN: Mboo_2392
            MTH: MTH784
            MST: Msp_1229(prs)
            MSI: Msm_1577
            MKA: MK1667(prsA)
            AFU: AF0589(prsA-1) AF1419(prsA-2)
            HAL: VNG2203G(prsA)
            HMA: rrnAC2630(prsA)
            HWA: HQ3650A(prsA)
            NPH: NP0606A(prsA)
            TAC: Ta0119m
            TVO: TVN0197
            PTO: PTO0906
            PHO: PH1923
            PAB: PAB1114(prsA)
            PFU: PF0236
            TKO: TK2235
            RCI: RCIX1327(prsA-1) RCIX2406(prsA-2)
            APE: APE_1834.1
            SMR: Smar_1238
            IHO: Igni_0252
            HBU: Hbut_0662
            SSO: SSO1045
            STO: ST0946
            SAI: Saci_1282
            MSE: Msed_1790
            PAI: PAE2980
            PIS: Pisl_0380
            PCL: Pcal_1127
            PAS: Pars_1347
            TPE: Tpen_0317 Tpen_0386
STRUCTURES  PDB: 1DKR  1DKU  1IBS  1U9Y  1U9Z  2H06  2H07  2H08  2HCR  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.6.1
            ExPASy - ENZYME nomenclature database: 2.7.6.1
            ExplorEnz - The Enzyme Database: 2.7.6.1
            ERGO genome analysis and discovery system: 2.7.6.1
            BRENDA, the Enzyme Database: 2.7.6.1
            CAS: 9015-83-2
///
ENTRY       EC 2.7.6.2                  Enzyme
NAME        thiamine diphosphokinase;
            thiamin kinase;
            thiamine pyrophosphokinase;
            ATP:thiamin pyrophosphotransferase;
            thiamin pyrophosphokinase;
            thiamin pyrophosphotransferase;
            thiaminokinase;
            thiamin:ATP pyrophosphotransferase;
            TPTase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Diphosphotransferases
SYSNAME     ATP:thiamine diphosphotransferase
REACTION    ATP + thiamine = AMP + thiamine diphosphate [RN:R00619]
ALL_REAC    R00619;
            (other) R00616
SUBSTRATE   ATP [CPD:C00002];
            thiamine [CPD:C00378]
PRODUCT     AMP [CPD:C00020];
            thiamine diphosphate [CPD:C00068]
REFERENCE   1
  AUTHORS   Leuthardt, F. and Nielsen, H.
  TITLE     Phosphorylation biologique de la thiamine.
  JOURNAL   Helv. Chim. Acta 35 (1952) 1196-1209.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Shimazono, N., Mano, Y., Tanaka, R. and Kajiro, Y.
  TITLE     Mechanism of transpyrophosphorylation with thiamine
            pyrophosphokinase.
  JOURNAL   J. Biochem. (Tokyo) 46 (1959) 959-961.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Steyn-Parve, E.P.
  TITLE     Partial purification and properties of thiaminokinase from yeast.
  JOURNAL   Biochim. Biophys. Acta 8 (1952) 310-324.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00730  Thiamine metabolism
ORTHOLOGY   KO: K00949  thiamine pyrophosphokinase
GENES       HSA: 27010(TPK1)
            PTR: 463818(TPK1)
            CFA: 475515(TPK1)
            SPU: 764757(LOC764757)
            OSA: 4326818 4338566
            CME: CMH016C
            SCE: YOR143C(THI80)
            PIC: PICST_46967(TNR3) PICST_59866(THI80)
            CGR: CAGL0I07117g
            SPO: SPAC6F12.05c(tnr3)
            ANI: AN9488.2
            AFM: AFUA_7G05410
            DDI: DDBDRAFT_0189361
            TET: TTHERM_00391440
            EHI: 1.t00126
            LPN: lpg2497
            LPF: lpl2418
            LPP: lpp2564
            FTU: FTT1316c
            FTF: FTF1316c
            FTW: FTW_1482
            FTL: FTL_1477
            FTH: FTH_1431
            FTA: FTA_1562
            FTN: FTN_0662
            DNO: DNO_0090
            REH: H16_A2506
            BPM: BURPS1710b_0775
            HPA: HPAG1_1222
            HAC: Hac_0207
            SAT: SYN_01522
            RLE: RL4610
            BBK: BARBAKC583_0128(thiN)
            JAN: Jann_3176
            RDE: RD1_1915(thiN)
            GOX: GOX0109
            GBE: GbCGDNIH1_0611
            BCE: BC3857
            BCZ: BCZK3618
            BTK: BT9727_3600
            BAY: RBAM_015630(thiN)
            SAC: SACOL1236
            SAA: SAUSA300_1116
            LWE: lwe1836
            LLC: LACR_2014
            LLM: llmg_2013(thiN)
            SPZ: M5005_Spy_0225
            SPH: MGAS10270_Spy0225
            SPI: MGAS10750_Spy0220
            SPJ: MGAS2096_Spy0243
            SPK: MGAS9429_Spy0227
            SPF: SpyM50204(thiN)
            SPA: M6_Spy0257
            SPB: M28_Spy0219
            SPD: SPD_1779
            SAK: SAK_1797
            SSA: SSA_2118
            SGO: SGO_0199
            LSA: LSA0695
            LSL: LSL_0618
            LBR: LVIS_0959
            LCA: LSEI_1619
            CPF: CPF_1988
            CPR: CPR_1706
            CTC: CTC01228
            CNO: NT01CX_2236
            CTH: Cthe_0577
            CBA: CLB_2374
            CBH: CLC_2356
            CBF: CLI_2562
            CHY: CHY_0231
            DSY: DSY2682
            SWO: Swol_2104
            CSC: Csac_2348
            TTE: TTE1497(thi80)
            FNU: FN0890
            BTH: BT_2397
            FJO: Fjoh_2175
            FPS: FP1767
STRUCTURES  PDB: 1IG0  1IG3  2F17  2G9Z  2HH9  2OMK  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.6.2
            ExPASy - ENZYME nomenclature database: 2.7.6.2
            ExplorEnz - The Enzyme Database: 2.7.6.2
            ERGO genome analysis and discovery system: 2.7.6.2
            BRENDA, the Enzyme Database: 2.7.6.2
            CAS: 9026-24-8
///
ENTRY       EC 2.7.6.3                  Enzyme
NAME        2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase;
            2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase;
            H2-pteridine-CH2OH pyrophosphokinase;
            7,8-dihydroxymethylpterin-pyrophosphokinase;
            HPPK;
            7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase;
            hydroxymethyldihydropteridine pyrophosphokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Diphosphotransferases
SYSNAME     ATP:2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
            6'-diphosphotransferase
REACTION    ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine = AMP +
            (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
            [RN:R03503]
ALL_REAC    R03503
SUBSTRATE   ATP [CPD:C00002];
            2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine [CPD:C01300]
PRODUCT     AMP [CPD:C00020];
            (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
REFERENCE   1  [PMID:4304228]
  AUTHORS   Richey DP, Brown GM.
  TITLE     The biosynthesis of folic acid. IX. Purification and properties of
            the enzymes required for the formation of dihydropteroic acid.
  JOURNAL   J. Biol. Chem. 244 (1969) 1582-92.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Richey, D.P. and Brown, G.M.
  TITLE     Hydroxymethyldihydropteridine pyrophosphokinase and dihydropteroate
            synthetase from Escherichia coli.
  JOURNAL   Methods Enzymol. 18B (1971) 765-771.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4312465]
  AUTHORS   Shiota T, Baugh CM, Jackson R, Dillard R.
  TITLE     The enzymatic synthesis of hydroxymethyldihydropteridine
            pyrophosphate and dihydrofolate.
  JOURNAL   Biochemistry. 8 (1969) 5022-8.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K00950  2-amino-4-hydroxy-6-hydroxymethyldihydropteridine
                        pyrophosphokinase
GENES       DME: Dmel_CG11020(nompC)
            CME: CMQ278C
            SCE: YNL256W(FOL1)
            AGO: AGOS_AFR647C
            PIC: PICST_66087
            CGR: CAGL0J07920g
            SPO: SPBC1734.03
            CNE: CNC04040
            DDI: DDB_0230139
            ECO: b0142(folK)
            ECJ: JW0138(folK)
            ECE: Z0153(folK)
            ECS: ECs0146
            ECC: c0175(folK)
            ECI: UTI89_C0156(folK)
            ECP: ECP_0152
            ECV: APECO1_1843(folK)
            ECW: EcE24377A_0146(folK)
            ECX: EcHS_A0145(folK)
            STY: STY0208(folK)
            STT: t0191(folK)
            SPT: SPA0189(folK)
            SEC: SC0183(folK)
            STM: STM0183(folK)
            YPE: YPO3400(folK)
            YPK: y0787(folK)
            YPM: YP_0285(folK)
            YPA: YPA_2901
            YPN: YPN_0689
            YPP: YPDSF_2956
            YPS: YPTB0731(folK)
            YPI: YpsIP31758_3341(folK)
            SFL: SF0134(folK)
            SFX: S0137(folK)
            SFV: SFV_0127(folK)
            SSN: SSON_0154(folK)
            SBO: SBO_0131(folK)
            SDY: SDY_0158(folK)
            ECA: ECA3320(folK)
            PLU: plu0873(folK)
            WBR: WGLp264(folK)
            SGL: SG0489
            ENT: Ent638_0682
            SPE: Spro_3988
            BFL: Bfl150(folK)
            BPN: BPEN_155(folK)
            HIT: NTHI0077(folK)
            HDU: HD0605(folK)
            HSO: HS_1025(folK)
            PMU: PM0865(folK)
            MSU: MS0925(folK)
            APL: APL_0177(folK)
            ASU: Asuc_1732
            XFA: XF0228 XF1456
            XFT: PD0186(folK) PD0676(folK)
            XCC: XCC1767 XCC3433(folK)
            XCB: XC_0731 XC_2469
            XCV: XCV0747(folK) XCV1815(folK)
            XAC: XAC0686(folK) XAC1784(folK)
            XOO: XOO2365(folK) XOO3933(folK)
            XOM: XOO_2246(XOO2246) XOO_3711(XOO3711)
            VCH: VC0593
            VCO: VC0395_A0053(folK-1)
            VVU: VV1_1644
            VVY: VV2762
            VPA: VP2505
            VFI: VF2168 VF2246
            PPR: PBPRA3174
            PAE: PA4728(folK)
            PAU: PA14_07600(folK) PA14_62570(folK)
            PAP: PSPA7_5445(folK)
            PPU: PP_4698(folK-2)
            PPF: Pput_4563
            PST: PSPTO_0962(folK-2)
            PSB: Psyr_0829
            PSP: PSPPH_0625(folK1) PSPPH_0855(folK2)
            PFL: PFL_5276(folK)
            PFO: Pfl_4810
            PEN: PSEEN0420 PSEEN4734(folK-2)
            PMY: Pmen_3591
            PAR: Psyc_0115(folK)
            PCR: Pcryo_0124
            PRW: PsycPRwf_2132
            ACI: ACIAD2407 ACIAD3062(folK)
            SON: SO_0871(folK-1) SO_1292(folK-2)
            SDN: Sden_2827 Sden_3173
            SFR: Sfri_2989 Sfri_3279
            SAZ: Sama_0777
            SBL: Sbal_3493
            SBM: Shew185_0846
            SLO: Shew_3132
            SPC: Sputcn32_3131
            SSE: Ssed_3902
            SPL: Spea_0695
            SHE: Shewmr4_0727 Shewmr4_2901
            SHM: Shewmr7_2983 Shewmr7_3295
            SHN: Shewana3_3080 Shewana3_3407
            SHW: Sputw3181_0812
            ILO: IL2253(folK_3)
            CPS: CPS_2675(folK1) CPS_4311(folK2) CPS_4341(folK3)
            PHA: PSHAa0603(folK)
            PAT: Patl_1045 Patl_3934
            SDE: Sde_3377
            PIN: Ping_0581
            MAQ: Maqu_0668
            CBU: CBU_0287(folK-2)
            CBD: COXBU7E912_1794(folK)
            LPN: lpg1539
            LPF: lpl1487(folK)
            LPP: lpp1496(folK)
            MCA: MCA2313(folK-1) MCA2987(folK-2)
            FTU: FTT0942c(folK)
            FTF: FTF0942c(folK)
            FTW: FTW_0836
            FTL: FTL_1265
            FTH: FTH_1240(folK)
            FTN: FTN_0819
            TCX: Tcr_1527
            NOC: Noc_0038 Noc_0884
            AEH: Mlg_0563 Mlg_2523
            HHA: Hhal_0676
            HCH: HCH_06263(folK1) HCH_06267(folK2)
            CSA: Csal_0970 Csal_3064
            ABO: ABO_0339(folK-1) ABO_2056(folK)
            MMW: Mmwyl1_4015
            AHA: AHA_3537(folK-1) AHA_3848(folK-2)
            DNO: DNO_0117
            BCI: BCI_0229(folK)
            RMA: Rmag_0414
            VOK: COSY_0383(folK) COSY_0856
            NME: NMB0745
            NMA: NMA0958(folK)
            NMC: NMC0699(folK)
            NGO: NGO0323
            CVI: CV_1633(folK)
            RSO: RSc2628(folK)
            REU: Reut_A2778
            REH: H16_A3082(folK)
            RME: Rmet_2915
            BMA: BMA2321(folK)
            BMV: BMASAVP1_A0506(folK)
            BML: BMA10299_A1093(folK)
            BMN: BMA10247_2200(folK)
            BXE: Bxe_A3956
            BVI: Bcep1808_0717
            BUR: Bcep18194_A3844
            BCN: Bcen_0273
            BCH: Bcen2424_0757
            BAM: Bamb_0651
            BPS: BPSL2822
            BPM: BURPS1710b_3315(folK)
            BPL: BURPS1106A_3305(folK)
            BPD: BURPS668_3272(folK)
            BTE: BTH_I1313
            PNU: Pnuc_1766
            BPE: BP0238(folK)
            BPA: BPP3629(folK)
            BBR: BB4064(folK)
            RFR: Rfer_2508
            POL: Bpro_3560
            PNA: Pnap_2990
            AJS: Ajs_2990
            VEI: Veis_1768
            MPT: Mpe_A3019
            HAR: HEAR2638(folK)
            MMS: mma_2875(folK)
            NEU: NE0070
            NET: Neut_2295
            NMU: Nmul_A0881
            EBA: ebA7113(folK)
            AZO: azo3141(folK)
            DAR: Daro_3183
            TBD: Tbd_2051
            MFA: Mfla_0599
            HPY: HP1036(folK)
            HPJ: jhp0388(folK)
            HPA: HPAG1_0411
            HHE: HH1142(folK)
            HAC: Hac_1140(folK)
            WSU: WS1643(folK)
            TDN: Tmden_0688
            CJE: Cj0065c(folK)
            CJR: CJE0062(folK)
            CJJ: CJJ81176_0103(folK)
            CJU: C8J_0058(folK)
            CJD: JJD26997_0075(folK)
            CFF: CFF8240_1507(folK)
            CCV: CCV52592_0366(folK)
            CHA: CHAB381_1209(folK)
            CCO: CCC13826_0368(folK) CCC13826_0803
            ABU: Abu_0486(folK)
            NIS: NIS_0432(folK)
            SUN: SUN_1040
            GSU: GSU2979(folK)
            GME: Gmet_0495
            GUR: Gura_0703
            PCA: Pcar_0250(folK)
            PPD: Ppro_0296
            DVU: DVU1656(folK)
            DDE: Dde_1969
            LIP: LI0240(folK)
            DPS: DP0430
            ADE: Adeh_4066
            MXA: MXAN_5925(folK)
            SFU: Sfum_0053
            RFE: RF_0039(folKP)
            RBE: RBE_0032(folKP)
            AMA: AM975
            APH: APH_0212(folK)
            ERU: Erum6520(folK)
            ERW: ERWE_CDS_06840(folK)
            ERG: ERGA_CDS_06750(folK)
            ECN: Ecaj_0659
            ECH: ECH_0350(folK)
            NSE: NSE_0486(folK)
            PUB: SAR11_1059(folK)
            MLO: mll0786
            MES: Meso_1414
            SME: SMc00465(folK)
            SMD: Smed_1532
            ATU: Atu1354(folK)
            ATC: AGR_C_2500(pppK)
            RET: RHE_CH02334(folK)
            RLE: RL2648
            BME: BMEI0954
            BMF: BAB1_1051(folK)
            BMS: BR1031(folK)
            BMB: BruAb1_1036(folK)
            BOV: BOV_0997(folK)
            OAN: Oant_2117
            BJA: bll3057(folK)
            BRA: BRADO2683(folK)
            BBT: BBta_3024(folK)
            RPA: RPA1838(folK)
            RPB: RPB_3535
            RPC: RPC_1763
            RPD: RPD_1930
            RPE: RPE_1855
            NWI: Nwi_2235
            NHA: Nham_2635
            XAU: Xaut_2492
            CCR: CC_1551
            SIL: SPO3205(folK)
            SIT: TM1040_2567
            RSP: RSP_1668(folK)
            JAN: Jann_0512
            RDE: RD1_1357(folK)
            MMR: Mmar10_1577
            HNE: HNE_2364(folK)
            ZMO: ZMO1647(folK)
            NAR: Saro_3092
            SAL: Sala_1552
            ELI: ELI_11270
            GBE: GbCGDNIH1_0987
            RRU: Rru_A1858
            MAG: amb2299
            MGM: Mmc1_0041
            ABA: Acid345_0083
            SUS: Acid_0958
            BSU: BG10142(folK)
            BHA: BH0095(folK)
            BAN: BA0073(folK)
            BAR: GBAA0073(folK)
            BAA: BA_0663(hppK)
            BAT: BAS0073
            BCE: BC0081
            BCA: BCE_0072(folK)
            BCZ: BCZK0069(folK)
            BCY: Bcer98_0069
            BTK: BT9727_0069(folK)
            BTL: BALH_0072(folK)
            BLI: BL05004(folK)
            BLD: BLi00095(folK)
            BCL: ABC0115(folK)
            BAY: RBAM_000900(folK)
            BPU: BPUM_0063(folK)
            OIH: OB0087
            GKA: GK0071
            SAU: SA0474(folK)
            SAV: SAV0516(folK)
            SAM: MW0471(folK)
            SAR: SAR0517(folK)
            SAS: SAS0473
            SAC: SACOL0560(folK)
            SAB: SAB0465(folK)
            SAA: SAUSA300_0494(folK)
            SAO: SAOUHSC_00491
            SAJ: SaurJH9_0538
            SAH: SaurJH1_0551
            SEP: SE2267
            SER: SERP0155(folK)
            SHA: SH2494(folK)
            SSP: SSP2240
            LMO: lmo0226(folK)
            LMF: LMOf2365_0238(folK)
            LIN: lin0258(folK)
            LWE: lwe0190(folK)
            LLA: L0175(folE)
            LLC: LACR_1275
            SPY: SPy_1100(folK)
            SPZ: M5005_Spy_0824(folK)
            SPM: spyM18_1062(folK)
            SPG: SpyM3_0762(folK)
            SPS: SPs0962
            SPH: MGAS10270_Spy0940(folK)
            SPI: MGAS10750_Spy0975(folK)
            SPJ: MGAS2096_Spy0898(folK)
            SPK: MGAS9429_Spy0943(folK)
            SPF: SpyM50964(folK)
            SPA: M6_Spy0822
            SPB: M28_Spy0801(folK)
            SPN: SP_0292
            SPR: spr0269(sulD)
            SPD: SPD_0272(sulD)
            SAG: SAG1113(folK)
            SAN: gbs1180
            SAK: SAK_1198(folK)
            SMU: SMU.971(folK)
            STC: str1540(folK)
            STL: stu1540(folK)
            SSA: SSA_0200(folK)
            LPL: lp_3298(folK)
            LSA: LSA1101(folK)
            LDB: Ldb0247(folKE)
            LBU: LBUL_0209
            LRE: Lreu_1279
            EFA: EF3268(folK)
            STH: STH3186
            CAC: CAC2927(folA)
            CPE: CPE1022(folA)
            CPF: CPF_1277(folBK)
            CPR: CPR_1099(folBK)
            CNO: NT01CX_0374
            CTH: Cthe_2583
            CDF: CD1452(folK)
            CBO: CBO0830(folK)
            CBA: CLB_0871(folK)
            CBH: CLC_0885(folK)
            CBF: CLI_0912(folK)
            CKL: CKL_0960
            AMT: Amet_2163
            CHY: CHY_2381(folK)
            DSY: DSY0209
            DRM: Dred_0156
            SWO: Swol_0099
            CSC: Csac_0112
            TTE: TTE2369(folK)
            MTA: Moth_0139
            POY: PAM580(folK)
            MTU: Rv3606c(folK)
            MTC: MT3711(folK)
            MBO: Mb3636c(folK)
            MBB: BCG_3670c(folK)
            MLE: ML0226(folK)
            MPA: MAP0452(folK)
            MAV: MAV_0546(folK)
            MSM: MSMEG_6101(folK)
            MVA: Mvan_5368
            MGI: Mflv_1420
            MMC: Mmcs_4766
            MKM: Mkms_4852
            MJL: Mjls_5152
            CGL: NCgl2599(cgl2692)
            CGB: cg2979(folK)
            CEF: CE2538
            CDI: DIP1997(folK)
            CJK: jk0282(folK)
            NFA: nfa4020(folK)
            RHA: RHA1_ro04411
            SCO: SCO3401(folK)
            TWH: TWT586(folPXK)
            TWS: TW175(folP)
            LXX: Lxx21460(folK)
            CMI: CMM_0848(folBK)
            ART: Arth_0155
            AAU: AAur_0142(folK)
            PAC: PPA0273
            NCA: Noca_0448
            TFU: Tfu_2890
            FRA: Francci3_4405
            FAL: FRAAL6708(folK)
            KRA: Krad_0542
            SEN: SACE_0400(folK)
            STP: Strop_4295
            BLO: BL1685(sulD)
            RXY: Rxyl_2183
            FNU: FN0072
            RBA: RB1874
            CTR: CT613(folP)
            CTA: CTA_0666(folP)
            CMU: TC0903
            CPN: CPn0758(folP)
            CPA: CP1114
            CPJ: CPj0758(folP)
            CPT: CpB0786
            CCA: CCA00999(folKP)
            CAB: CAB969(folKP)
            CFE: CF0014(folP)
            PCU: pc0361(folK)
            LIL: LA3959(folK)
            LIC: LIC13164(folK)
            LBJ: LBJ_0346(folK)
            LBL: LBL_2730(folK)
            SYN: slr1093(folK)
            SYW: SYNW0216(folK)
            SYC: syc1827_d(folK)
            SYF: Synpcc7942_2272
            SYD: Syncc9605_0211
            SYG: sync_0249(folK)
            SYR: SynRCC307_0223(folK)
            SYX: SynWH7803_0259(folK)
            CYA: CYA_0019(folK)
            CYB: CYB_2920(folK)
            TEL: tll0178(folK)
            ANA: asr2953
            AVA: Ava_0949
            PMA: Pro0318(folK)
            PMM: PMM0287(folK)
            PMT: PMT1886(folK)
            PMN: PMN2A_1653
            PMI: PMT9312_0289
            PMB: A9601_03101(folK)
            PMC: P9515_03201(folK)
            PMF: P9303_25191(folK)
            PMG: P9301_03111(folK)
            PME: NATL1_03671(folK)
            TER: Tery_0688
            BTH: BT_3216
            BFR: BF0059
            BFS: BF0071
            PGI: PG1541(folK)
            SRU: SRU_0955(folK)
            CHU: CHU_2468(folK)
            FPS: FP0398
            CTE: CT1938(folK)
            CCH: Cag_0230
            CPH: Cpha266_2295
            PVI: Cvib_0333
            PLT: Plut_0268
            DET: DET1604(folK)
            DEH: cbdb_A1698(folK)
            DEB: DehaBAV1_1350
            RRS: RoseRS_2866
            RCA: Rcas_2431
            DRA: DR_0170
            DGE: Dgeo_0398
            TTH: TTC1387
            TTJ: TTHA1749
            AAE: aq_162(folK)
            TMA: TM0041
            TPT: Tpet_0882
            SAI: Saci_1101
STRUCTURES  PDB: 1DY3  1EQ0  1EQM  1EX8  1F9H  1F9Y  1G4C  1HKA  1HQ2  1IM6  
                 1KBR  1Q0N  1RAO  1RB0  1RTZ  1RU1  1RU2  1TMJ  1TMM  2BMB  
                 2CG8  2F63  2F65  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.6.3
            ExPASy - ENZYME nomenclature database: 2.7.6.3
            ExplorEnz - The Enzyme Database: 2.7.6.3
            ERGO genome analysis and discovery system: 2.7.6.3
            BRENDA, the Enzyme Database: 2.7.6.3
            CAS: 37278-23-2
///
ENTRY       EC 2.7.6.4                  Enzyme
NAME        nucleotide diphosphokinase;
            nucleotide pyrophosphokinase;
            ATP:nucleotide pyrophosphotransferase;
            ATP nucleotide 3'-pyrophosphokinase;
            nucleotide 3'-pyrophosphokinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Diphosphotransferases
SYSNAME     ATP:nucleoside-5'-phosphate diphosphotransferase
REACTION    ATP + nucleoside 5'-phosphate = AMP + 5'-phosphonucleoside
            3'-diphosphate [RN:R03258]
ALL_REAC    R03258
SUBSTRATE   ATP [CPD:C00002];
            nucleoside 5'-phosphate [CPD:C01117]
PRODUCT     AMP [CPD:C00020];
            5'-phosphonucleoside 3'-diphosphate [CPD:C04292]
COMMENT     The enzyme acts on the 5'-mono-, di- and triphosphate derivatives of
            purine nucleosides.
REFERENCE   1
  AUTHORS   Murao, S. and Nishino, T.
  TITLE     Isolation and identification of ATP:nucleotide
            pyrophosphotransferase-producing microorganism.
  JOURNAL   Agric. Biol. Chem. 38 (1974) 2483-2489.
  ORGANISM  Streptomyces adephospholyticus
REFERENCE   2
  AUTHORS   Nishino, T. and Murao, S.
  TITLE     Purification and some properties of ATP:nucleotide
            pyrophosphotransferase of Streptomyces adephospholyticus.
  JOURNAL   Agric. Biol. Chem. 38 (1974) 2491-2496.
  ORGANISM  Streptomyces adephospholyticus
REFERENCE   3
  AUTHORS   Nishino, T. and Murao, S.
  TITLE     Characterization of pyrophosphoryl transfer reaction of
            ATP:nucleotide pyrophosphotransferase.
  JOURNAL   Agric. Biol. Chem. 39 (1975) 1007-1014.
  ORGANISM  Streptomyces adephospholyticus
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.6.4
            ExPASy - ENZYME nomenclature database: 2.7.6.4
            ExplorEnz - The Enzyme Database: 2.7.6.4
            ERGO genome analysis and discovery system: 2.7.6.4
            BRENDA, the Enzyme Database: 2.7.6.4
            CAS: 53167-92-3
///
ENTRY       EC 2.7.6.5                  Enzyme
NAME        GTP diphosphokinase;
            stringent factor;
            guanosine 3',5'-polyphosphate synthase;
            GTP pyrophosphokinase;
            ATP-GTP 3'-diphosphotransferase;
            guanosine 5',3'-polyphosphate synthetase;
            (p)ppGpp synthetase I;
            (p)ppGpp synthetase II;
            guanosine pentaphosphate synthetase;
            GPSI;
            GPSII
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Diphosphotransferases
SYSNAME     ATP:GTP 3'-diphosphotransferase
REACTION    ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate
            [RN:R00429]
ALL_REAC    R00429
SUBSTRATE   ATP [CPD:C00002];
            GTP [CPD:C00044]
PRODUCT     AMP [CPD:C00020];
            guanosine 3'-diphosphate 5'-triphosphate [CPD:C04494]
COMMENT     GDP can also act as acceptor.
REFERENCE   1  [PMID:6161916]
  AUTHORS   Fehr S, Richter D.
  TITLE     Stringent response of Bacillus stearothermophilus: evidence for the
            existence of two distinct guanosine 3',5'-polyphosphate synthetases.
  JOURNAL   J. Bacteriol. 145 (1981) 68-73.
  ORGANISM  Bacillus stearothermophilus
REFERENCE   2  [PMID:184817]
  AUTHORS   Sy J, Akers H.
  TITLE     Purification and properties of guanosine 5', 3'-polyphosphate
            synthetase from Bacillus brevis.
  JOURNAL   Biochemistry. 15 (1976) 4399-403.
  ORGANISM  Bacillus brevis
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K00951  GTP pyrophosphokinase
            KO: K07816  putative GTP pyrophosphokinase
GENES       ECO: b2784(relA)
            ECJ: JW2755(relA)
            ECE: Z4099(relA)
            ECS: ECs3644
            ECC: c3347(relA)
            ECI: UTI89_C3154(relA)
            ECP: ECP_2765
            ECW: EcE24377A_3088(relA)
            ECX: EcHS_A2928(relA)
            STY: STY3094(relA)
            STT: t2865(relA)
            SPT: SPA2821(relA)
            SEC: SC2896(relA)
            STM: STM2956(relA)
            YPE: YPO3380(relA)
            YPK: y0811(relA)
            YPM: YP_0306(relA)
            YPA: YPA_2877
            YPN: YPN_0713
            YPP: YPDSF_2980 YPDSF_3867
            YPS: YPTB0751(relA)
            YPI: YpsIP31758_3319(relA)
            SFL: SF2797(relA)
            SFX: S2991(relA)
            SFV: SFV_2673(relA)
            SSN: SSON_2941(relA)
            SBO: SBO_2665(relA)
            SDY: SDY_3001(relA)
            ECA: ECA3569(relA)
            PLU: plu0910(relA)
            SGL: SG0510
            ENT: Ent638_0089 Ent638_3236
            SPE: Spro_0792
            HIT: NTHI0452(relA)
            HDU: HD1185(relA)
            HSO: HS_0095(relA)
            PMU: PM1865(relA)
            MSU: MS0241(spoT)
            APL: APL_0405(relA)
            ASU: Asuc_0191
            XFA: XF1316
            XFT: PD0563(relA)
            XCC: XCC2936(relA)
            XCB: XC_1173
            XCV: XCV3244(relA)
            XAC: XAC3113(relA)
            XOO: XOO1736(relA)
            XOM: XOO_1637(XOO1637)
            VCH: VC2451
            VCO: VC0395_A2029(relA)
            VVU: VV1_1575 VV1_1576
            VVY: VV2821
            VPA: VP2564
            VFI: VF0104 VF2080
            PPR: PBPRA3082
            PAE: PA0934(relA)
            PAU: PA14_52180(relA)
            PPU: PP_1656(relA)
            PPF: Pput_4062 Pput_5211
            PST: PSPTO_1694(relA)
            PSB: Psyr_3695
            PSP: PSPPH_3716(relA)
            PFL: PFL_4446(relA)
            PFO: Pfl_4217 Pfl_5551
            PEN: PSEEN1364 PSEEN5447(spoT)
            PMY: Pmen_1735 Pmen_4390
            PAR: Psyc_0343(relA)
            PCR: Pcryo_0377 Pcryo_2005
            PRW: PsycPRwf_0383 PsycPRwf_0575
            ACI: ACIAD3068(relA)
            SON: SO_3455(relA)
            SDN: Sden_1193 Sden_3435
            SFR: Sfri_0363 Sfri_1049
            SAZ: Sama_0264 Sama_1033
            SBL: Sbal_0353 Sbal_3146
            SBM: Shew185_3144
            SLO: Shew_1202 Shew_3499
            SPC: Sputcn32_2765 Sputcn32_3632
            SSE: Ssed_0334 Ssed_1287
            SPL: Spea_1182 Spea_3879
            SHE: Shewmr4_1111 Shewmr4_3615
            SHM: Shewmr7_0328 Shewmr7_1177
            SHN: Shewana3_1111 Shewana3_3812
            SHW: Sputw3181_1247 Sputw3181_3772
            ILO: IL0804(relA)
            CPS: CPS_4115(relA)
            PHA: PSHAa0739(relA) PSHAa2793(spoT)
            PAT: Patl_0349 Patl_3707
            SDE: Sde_2238 Sde_3697
            PIN: Ping_0203 Ping_0530
            MAQ: Maqu_0636 Maqu_2238
            CBU: CBU_1375(relA)
            LPN: lpg1457(relA)
            LPF: lpl1571(relA)
            LPP: lpp1413(relA)
            MCA: MCA1920(relA)
            FTU: FTT0808(spoT) FTT1508c(relA)
            FTF: FTF0808(spoT) FTF1508c(relA)
            FTL: FTL_0285 FTL_1413
            FTH: FTH_0284(spoT1)
            FTA: FTA_0303
            FTN: FTN_1518(relA)
            TCX: Tcr_1212 Tcr_2144
            NOC: Noc_1214 Noc_1300
            AEH: Mlg_1097 Mlg_2442
            HHA: Hhal_0969 Hhal_1740
            HCH: HCH_01807(relA)
            CSA: Csal_1638 Csal_3235
            ABO: ABO_1623(relA)
            MMW: Mmwyl1_1253 Mmwyl1_4386
            AHA: AHA_0818
            DNO: DNO_0017(relA)
            RMA: Rmag_0513
            NME: NMB1735
            NMA: NMA1991(relA)
            NGO: NGO1382
            CVI: CV_3702(relA)
            RSO: RSc1576(relA) RSc2153(spoT)
            REU: Reut_A1274 Reut_A2471
            REH: H16_A0955(spoT1) H16_A1337(spoT2)
            RME: Rmet_0858 Rmet_1159
            BMA: BMA1098
            BMV: BMASAVP1_A1542
            BML: BMA10299_A0204
            BMN: BMA10247_0960
            BXE: Bxe_A0907 Bxe_A1370
            BVI: Bcep1808_0918 Bcep1808_1438
            BUR: Bcep18194_A4109 Bcep18194_A4614
            BCN: Bcen_0522 Bcen_0991
            BCH: Bcen2424_1001 Bcen2424_1473
            BAM: Bamb_0861 Bamb_1358
            BPS: BPSL1946(relA)
            BPM: BURPS1710b_1887(relA)
            BPL: BURPS1106A_1733(relA)
            BPD: BURPS668_1709(relA)
            BTE: BTH_I2597
            PNU: Pnuc_0828 Pnuc_1076
            BPE: BP3587(relA)
            BPA: BPP3325(relA)
            BBR: BB3776(relA)
            RFR: Rfer_2071 Rfer_3149
            POL: Bpro_1333 Bpro_2703
            PNA: Pnap_0809 Pnap_2537
            AAV: Aave_1588 Aave_3585
            AJS: Ajs_0949 Ajs_3149
            VEI: Veis_4220 Veis_4366
            MPT: Mpe_A1578
            HAR: HEAR1802(relA) HEAR2132(spoT)
            MMS: mma_1486(relA)
            NEU: NE0368(spoT)
            NET: Neut_1601
            NMU: Nmul_A0050 Nmul_A2505
            EBA: ebA3497(spoT) ebA6528(relA)
            AZO: azo1688(relA)
            DAR: Daro_2827 Daro_3843
            TBD: Tbd_0471 Tbd_1758
            MFA: Mfla_0050 Mfla_1298
            HAC: Hac_0638(spoT)
            TDN: Tmden_0719
            CFF: CFF8240_1212
            CCV: CCV52592_0483 CCV52592_1190(relA)
            CHA: CHAB381_1281
            CCO: CCC13826_0500
            ABU: Abu_0645(spoT)
            GSU: GSU2236(relA)
            GME: Gmet_2325
            GUR: Gura_3160
            PCA: Pcar_1287
            PPD: Ppro_2399
            DVU: DVU2083(relA)
            DVL: Dvul_1146
            DDE: Dde_1569
            LIP: LI0170(relA)
            BBA: Bd1570
            DPS: DP1165
            ADE: Adeh_2550
            AFW: Anae109_1311
            MXA: MXAN_3204(relA)
            SAT: SYN_00904 SYN_01901 SYN_03611
            SFU: Sfum_0983 Sfum_2111
            RFE: RF_0410(spoT12)
            RBE: RBE_0592(spoT12)
            PUB: SAR11_1058
            PLA: Plav_2868
            SMD: Smed_0677
            RLE: pRL120654
            BOV: BOV_0645
            OAN: Oant_2636
            BRA: BRADO4468(relA)
            BBT: BBta_4687(relA)
            RPA: RPA2693(relA)
            RPB: RPB_2608
            RPC: RPC_2635
            RPD: RPD_2647
            RPE: RPE_3026
            NWI: Nwi_1922
            NHA: Nham_2255
            BBK: BARBAKC583_0468(relA)
            XAU: Xaut_3877
            SIT: TM1040_2565
            RSP: RSP_1670(spoT)
            RSH: Rsph17029_0303
            RSQ: Rsph17025_2576
            JAN: Jann_0514
            PDE: Pden_1400
            MMR: Mmar10_1575
            NAR: Saro_2533
            SAL: Sala_2677
            SWI: Swit_3527
            GOX: GOX1807
            GBE: GbCGDNIH1_0989
            ACR: Acry_0531
            RRU: Rru_A1856
            MGM: Mmc1_0253
            ABA: Acid345_0175
            SUS: Acid_1285
            BSU: BG12665(relA) BG13142(yjbM)
            BHA: BH1242(relA) BH2849
            BAN: BA1212 BA4637(relA)
            BAR: GBAA1212 GBAA4637(relA)
            BAA: BA_1747 BA_5075
            BAT: BAS1119 BAS4302
            BCE: BC1198 BC4341 BC4401
            BCA: BCE_1320 BCE_4491(relA)
            BCZ: BCZK1095 BCZK2203(relA) BCZK4091 BCZK4151(relA)
            BCY: Bcer98_1783 Bcer98_3123
            BTK: BT9727_1101 BT9727_4080 BT9727_4140(relA)
            BTL: BALH_2184(relA) BALH_3933 BALH_3988(relA)
            BLI: BL01124(relA) BL03338(yjbM)
            BLD: BLi01254(yjbM) BLi02887(relA)
            BCL: ABC1570(relA) ABC2520
            BAY: RBAM_024710(relA)
            BPU: BPUM_2401(relA)
            OIH: OB1220 OB2024(relA)
            GKA: GK0829 GK2578
            SAU: SA0864 SA1460(relA)
            SAV: SAV1006 SAV1634(relA)
            SAM: MW0887 MW1584(relA)
            SAR: SAR0973 SAR1714(relA)
            SAS: SAS0875 SAS1570
            SAC: SACOL1010(relA1) SACOL1689(relA2)
            SAB: SAB0872 SAB1503c(relA)
            SAA: SAUSA300_0907 SAUSA300_1590
            SAO: SAOUHSC_00942 SAOUHSC_01742
            SAJ: SaurJH9_1691
            SAH: SaurJH1_1724
            SEP: SE0695 SE1315
            SER: SERP0586(relA-1) SERP1196(relA-2)
            SHA: SH1287(relA) SH1952
            SSP: SSP1125
            LMO: lmo0967 lmo1523(relA)
            LMF: LMOf2365_0987 LMOf2365_1542(relA)
            LIN: lin0966 lin1558(relA)
            LWE: lwe0949 lwe1536(relA)
            LLA: L0213(relA) L166082(ydgI)
            LLC: LACR_0092 LACR_0408
            LLM: llmg_0113(relA) llmg_0382
            SPY: SPy_1125 SPy_1981(relA)
            SPZ: M5005_Spy_0679 M5005_Spy_0847 M5005_Spy_1686(relA)
            SPM: spyM18_1086 spyM18_2045
            SPG: SpyM3_0784 SpyM3_1701(relA)
            SPS: SPs0985 SPs1702
            SPH: MGAS10270_Spy0737 MGAS10270_Spy0963 MGAS10270_Spy1755(relA)
            SPI: MGAS10750_Spy0771 MGAS10750_Spy0998 MGAS10750_Spy1780(relA)
            SPJ: MGAS2096_Spy0750 MGAS2096_Spy0922 MGAS2096_Spy0923
                 MGAS2096_Spy1709(relA)
            SPK: MGAS9429_Spy0734 MGAS9429_Spy0966 MGAS9429_Spy1689(relA)
            SPF: SpyM51658(relA)
            SPA: M6_Spy0696 M6_Spy0845 M6_Spy1694
            SPB: M28_Spy0659 M28_Spy0823 M28_Spy1674(relA)
            SPN: SP_1097 SP_1645
            SPR: spr1004 spr1487(relA)
            SPD: SPD_1458(relA)
            SAG: SAG1095 SAG1940
            SAN: gbs1162 gbs1928(relA)
            SAK: SAK_1180 SAK_1900(relA)
            SMU: SMU.1046c SMU.2044(relA)
            STC: str0145(relA) str1459
            STL: stu0145(relA) stu1459
            SSA: SSA_0250(relA) SSA_1210 SSA_1795
            SGO: SGO_1822(relA)
            LPL: lp_0293 lp_1987(relA) lp_2223
            LJO: LJ0823 LJ1394
            LAC: LBA0646 LBA0932(relA)
            LSA: LSA0737(relA) LSA1444
            LSL: LSL_0822(relA) LSL_1305
            LDB: Ldb0584 Ldb0885(relA)
            LBU: LBUL_0519
            LBR: LVIS_0728 LVIS_1473
            LCA: LSEI_0901 LSEI_1539
            LRE: Lreu_0721
            EFA: EF1974(relA) EF2671
            STH: STH2437
            CAC: CAC0642(spoT) CAC2274(spoT)
            CPE: CPE0654(relA) CPE1938(relA)
            CPF: CPF_0635 CPF_2193(relA)
            CPR: CPR_1904
            CTC: CTC00336 CTC02199
            CNO: NT01CX_1369 NT01CX_1844
            CTH: Cthe_1344
            CDF: CD2744(relA)
            CBO: CBO3059(relA)
            CBA: CLB_3088(relA)
            CBH: CLC_2961(relA)
            CBF: CLI_3118(relA)
            CBE: Cbei_1540
            CKL: CKL_3131(relA)
            AMT: Amet_2353
            CHY: CHY_2223(relA)
            DSY: DSY2451
            DRM: Dred_0733
            SWO: Swol_0806
            CSC: Csac_1001
            TTE: TTE1195(spoT)
            MTA: Moth_1680
            MMY: MSC_0475(relA)
            MCP: MCAP_0496
            POY: PAM126(spoT)
            AYW: AYWB_596(spoT)
            MFL: Mfl278
            MTU: Rv2583c(relA)
            MTC: MT2660(relA)
            MBO: Mb2614c(relA)
            MBB: BCG_2606c(relA)
            MLE: ML0491(relA)
            MPA: MAP1047(relA)
            MAV: MAV_3464(relA)
            MSM: MSMEG_2965(relA)
            MVA: Mvan_2587
            MGI: Mflv_3812
            MMC: Mmcs_2280
            MKM: Mkms_2327
            MJL: Mjls_2319
            CGL: NCgl1590(cgl1653)
            CGB: cg1861(rel)
            CEF: CE1767(relA)
            CDI: DIP1368(relA)
            CJK: jk1048(rel)
            NFA: nfa36840(relA)
            RHA: RHA1_ro06900(relA)
            SCO: SCO1513(relA)
            SMA: SAV2472(relA1) SAV6840(relA2)
            TWH: TWT275(relA)
            TWS: TW496(relA)
            LXX: Lxx10830(relA)
            CMI: CMM_1809(relA)
            ART: Arth_2297
            PAC: PPA1166
            NCA: Noca_2392
            TFU: Tfu_2090
            FRA: Francci3_1376 Francci3_1377
            FAL: FRAAL2147(relA1) FRAAL2148(relA2) FRAAL5920
            ACE: Acel_1338
            KRA: Krad_3048
            SEN: SACE_2028(relA)
            STP: Strop_1815 Strop_3287
            BLO: BL1439(relA)
            BAD: BAD_1002(relA)
            RXY: Rxyl_1338
            FNU: FN0926
            LIL: LA3085(relA)
            LIC: LIC11012
            LBJ: LBJ_0842(spoT)
            LBL: LBL_2240(spoT)
            SYD: Syncc9605_2455
            SYE: Syncc9902_2139
            AVA: Ava_1993 Ava_4989
            PMN: PMN2A_1558
            PMI: PMT9312_0193
            PMB: A9601_02091(spoT)
            PMC: P9515_02201(spoT)
            PMF: P9303_28061(spoT)
            PMG: P9301_02111(spoT)
            PME: NATL1_02671(spoT)
            TER: Tery_2653
            BTH: BT_3998
            BFR: BF0764 BF2166
            BFS: BF0692 BF2223(relA)
            PGI: PG1808(spoT)
            CHU: CHU_1704(relA)
            GFO: GFO_0778(relA)
            FJO: Fjoh_2223
            FPS: FP1866(relA)
            CTE: CT1545(relA)
            CCH: Cag_1775
            CPH: Cpha266_2023
            PVI: Cvib_0447
            PLT: Plut_0392
            DET: DET0005(relA)
            DEH: cbdb_A5(relA)
            DEB: DehaBAV1_0005
            RRS: RoseRS_4122
            RCA: Rcas_1219
            DRA: DR_1838
            DGE: Dgeo_1308
            TMA: TM0729
            TPT: Tpet_0200
            TME: Tmel_1316
            FNO: Fnod_1083
            NPH: NP3860A(relA)
STRUCTURES  PDB: 1E3H  1E3P  1VJ7  2BE3  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.6.5
            ExPASy - ENZYME nomenclature database: 2.7.6.5
            ExplorEnz - The Enzyme Database: 2.7.6.5
            ERGO genome analysis and discovery system: 2.7.6.5
            BRENDA, the Enzyme Database: 2.7.6.5
            CAS: 63690-89-1
///
ENTRY       EC 2.7.7.1                  Enzyme
NAME        nicotinamide-nucleotide adenylyltransferase;
            NAD+ pyrophosphorylase;
            adenosine triphosphate-nicotinamide mononucleotide transadenylase;
            ATP:NMN adenylyltransferase;
            diphosphopyridine nucleotide pyrophosphorylase;
            nicotinamide adenine dinucleotide pyrophosphorylase;
            nicotinamide mononucleotide adenylyltransferase;
            NMN adenylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ATP:nicotinamide-nucleotide adenylyltransferase
REACTION    ATP + nicotinamide ribonucleotide = diphosphate + NAD+ [RN:R00137]
ALL_REAC    R00137;
            (other) R03005
SUBSTRATE   ATP [CPD:C00002];
            nicotinamide ribonucleotide [CPD:C00455]
PRODUCT     diphosphate [CPD:C00013];
            NAD+ [CPD:C00003]
COMMENT     Nicotinate nucleotide can also act as acceptor. See also EC 2.7.7.18
            nicotinate-nucleotide adenylyltransferase.
REFERENCE   1  [PMID:13684981]
  AUTHORS   ATKINSON MR, JACKSON JF, MORTON RK.
  TITLE     Nicotinamide mononucleotide adenylyltransferase of pig-liver nuclei.
            The effects of nicotinamide mononucleotide concentration and pH on
            dinucleotide synthesis.
  JOURNAL   Biochem. J. 80 (1961) 318-23.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:4291828]
  AUTHORS   Dahmen W, Webb B, Preiss J.
  TITLE     The deamido-diphosphopyridine nucleotide and diphosphopyridine
            nucleotide pyrophosphorylases of Escherichia coli and yeast.
  JOURNAL   Arch. Biochem. Biophys. 120 (1967) 440-50.
  ORGANISM  Escherichia coli [GN:eco], Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Kornberg, A. and Pricer, W.E.
  TITLE     Enzymatic cleavage of diphosphopyridine nucleotide with radioactive
            pyrophosphate.
  JOURNAL   J. Biol. Chem. 191 (1951) 535-541.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K00952  nicotinamide-nucleotide adenylyltransferase
GENES       HSA: 23057(NMNAT2) 349565(NMNAT3) 64802(NMNAT1)
            MMU: 226518(Nmnat2) 66454(Nmnat1) 74080(Nmnat3)
            CFA: 477091(NMNAT3) 479601(NMNAT1) 610576(NMNAT2)
            GGA: 419446(NMNAT1) 424820(NMNAT3) 771393(NMNAT2)
            DRE: 336257(nmnat2)
            SPU: 577778(LOC577778)
            OSA: 4331124
            CME: CMF018C
            SCE: YGR010W(NMA2) YLR328W(NMA1)
            AGO: AGOS_AGR022C
            PIC: PICST_86133(NMA1)
            CAL: CaO19_7499(CaO19.7499)
            CGR: CAGL0A01023g
            SPO: SPAC806.06c
            ANI: AN1745.2
            AFM: AFUA_6G08870
            AOR: AO090001000561
            DDI: DDB_0233076
            EHI: 130.t00019
            ECO: b4390(nadR)
            ECE: Z5991(nadR)
            ECS: ECs5348
            ECC: c5475(nadR)
            ECI: UTI89_C5161(nadR)
            ECP: ECP_4774
            ECV: APECO1_1991(nadR)
            ECW: EcE24377A_4989(nadR)
            ECX: EcHS_A4625
            STY: STY4927(nadR)
            STT: t4619(nadR)
            SPT: SPA4390(nadR)
            SEC: SC4425(nadR)
            STM: STM4580.S(nadR)
            YPE: YPO0444(nadR)
            YPM: YP_3738(nadR)
            YPA: YPA_3840
            YPN: YPN_0315
            YPS: YPTB0588(nadR)
            SFL: SF4422(nadR)
            SFX: S4693(nadR)
            SFV: SFV_4424(nadR)
            SSN: SSON_4540(nadR)
            SBO: SBO_4453(nadR)
            SDY: SDY_4651(nadR)
            ECA: ECA0463(nadR)
            PLU: plu0553(nadR)
            HIN: HI0763(nadR)
            HIT: NTHI0923(nadR)
            HIP: CGSHiEE_08285
            HIQ: CGSHiGG_07310
            HSO: HS_0087(nadR)
            PMU: PM1387(nadR)
            MSU: MS0169(nadR)
            APL: APL_0046(nadR)
            XCC: XCC3446
            XCB: XC_0718
            XCV: XCV0734
            XAC: XAC0673
            XOO: XOO3948
            XOM: XOO_3725(XOO3725)
            PAR: Psyc_1913(nadR)
            PCR: Pcryo_2204
            ACI: ACIAD2606
            FTU: FTT0386(nadM)
            FTF: FTF0386(nadM)
            FTL: FTL_0452
            FTH: FTH_0449
            FTN: FTN_0483
            HCH: HCH_06993
            CSA: Csal_1837
            DNO: DNO_0139
            RSO: RS05360(RSp0835)
            RME: Rmet_5104
            BUR: Bcep18194_B0825
            BCN: Bcen_3479
            BCH: Bcen2424_4887
            BAM: Bamb_4267
            PNA: Pnap_3717
            AAV: Aave_0974
            AJS: Ajs_0701
            VEI: Veis_4845
            SAT: SYN_00623
            SFU: Sfum_3306
            MES: Meso_3455
            BME: BMEI0209(nadD)
            BMS: BR1842(nadD)
            BMB: BruAb1_1821(nadD)
            LLA: L0242(nadR)
            LLC: LACR_2249
            LLM: llmg_2241(nadR)
            STC: str0429(nadR)
            STL: stu0429(nadR)
            SSA: SSA_2195(nadR)
            OOE: OEOE_0896
            CTC: CTC02055(nadD)
            MGE: MG_240
            MTU: Rv0212c(nadR)
            MTC: MT0222
            MBO: Mb0218c(nadR)
            FNU: FN1132
            SYN: slr0787
            SYC: syc1306_c
            SYF: Synpcc7942_0205
            GVI: glr1660
            DGE: Dgeo_0228
            MJA: MJ0541
            MMP: MMP1578
            MMQ: MmarC5_1831
            MMZ: MmarC7_0825
            MAE: Maeo_0254
            MVN: Mevan_0890
            MAC: MA3731
            MBA: Mbar_A0256
            MMA: MM_0626
            MBU: Mbur_2370
            MTP: Mthe_0206
            MHU: Mhun_2915
            MEM: Memar_1582
            MBN: Mboo_1731
            MTH: MTH150
            MST: Msp_0435
            MSI: Msm_0129
            AFU: AF2315
            HAL: VNG0301C
            HMA: rrnAC1913(nadM)
            HWA: HQ1164A(nadR)
            NPH: NP0310A(nadM1_2) NP0908A(nadM1_1)
            TAC: Ta0774
            TVO: TVN0845
            PTO: PTO0129
            PHO: PH0464
            PAB: PAB1318
            PFU: PF0458
            TKO: TK0067
            RCI: RCIX2287(nadR)
            APE: APE_0513.1 APE_1986.1(nadM)
            SMR: Smar_1488
            IHO: Igni_0948
            HBU: Hbut_1560
            SSO: SSO0255
            STO: ST0302 ST0648
            SAI: Saci_0300(nadM) Saci_0720
            MSE: Msed_0004
            PAI: PAE1438 PAE2259
            PIS: Pisl_0898 Pisl_1561
            PCL: Pcal_0794 Pcal_1625
            PAS: Pars_0405 Pars_1824
            TPE: Tpen_0576 Tpen_0898
            NEQ: NEQ367
STRUCTURES  PDB: 1EJ2  1GZU  1HYB  1KKU  1KQN  1KQO  1KR2  1M8F  1M8G  1M8J  
                 1M8K  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.1
            ExPASy - ENZYME nomenclature database: 2.7.7.1
            ExplorEnz - The Enzyme Database: 2.7.7.1
            ERGO genome analysis and discovery system: 2.7.7.1
            BRENDA, the Enzyme Database: 2.7.7.1
            CAS: 9032-70-6
///
ENTRY       EC 2.7.7.2                  Enzyme
NAME        FMN adenylyltransferase;
            FAD pyrophosphorylase;
            riboflavin mononucleotide adenylyltransferase;
            adenosine triphosphate-riboflavin mononucleotide transadenylase;
            adenosine triphosphate-riboflavine mononucleotide transadenylase;
            FAD synthetase;
            riboflavin adenine dinucleotide pyrophosphorylase;
            riboflavine
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ATP:FMN adenylyltransferase
REACTION    ATP + FMN = diphosphate + FAD [RN:R00161]
ALL_REAC    R00161
SUBSTRATE   ATP [CPD:C00002];
            FMN [CPD:C00061]
PRODUCT     diphosphate [CPD:C00013];
            FAD [CPD:C00016]
REFERENCE   1  [PMID:13828163]
  AUTHORS   GIRI KV, RAO NA, CAMA HR, KUMAR SA.
  TITLE     Studies on flavinadenine dinucleotide-synthesizing enzyme in plants.
  JOURNAL   Biochem. J. 75 (1960) 381-6.
  ORGANISM  Cicer arietinum, Ricinus communis, Brassica campesteris, Phaseolus
            mungo, Phaseolus radiatus, Dolichm biflorus, Dolichos lablab,
            Cannavalia gladiata, Pisum sativum, Sesamum indicum, Cajanus
            indicus, Arachis hypogea, Solanum tuberosum [GN:estu], Ipomea
            batatus
REFERENCE   2
  AUTHORS   Schrecker, A.W. and Kornberg, A.
  TITLE     Reversible enzymatic synthesis of flavin-adenine dinucleotide.
  JOURNAL   J. Biol. Chem. 182 (1950) 795-803.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00740  Riboflavin metabolism
ORTHOLOGY   KO: K00953  FMN adenylyltransferase
GENES       HSA: 80308(FLAD1)
            MMU: 319945(Flad1)
            DME: Dmel_CG16848
            SCE: YDL045C(FAD1)
            AGO: AGOS_AER198W
            CGR: CAGL0K01397g
            SPO: SPCC1235.04c
            PFA: MAL13P1.292 PF10_0147
            TAN: TA20540
            TPV: TP03_0087
            ECO: b0025(ribF)
            ECJ: JW0023(ribF)
            ECE: Z0029(ribF)
            ECS: ECs0028
            ECC: c0029(ribF)
            ECI: UTI89_C0027(ribF)
            ECP: ECP_0023
            ECV: APECO1_1958(ribF)
            ECW: EcE24377A_0025(ribF)
            ECX: EcHS_A0027(ribF)
            STY: STY0054(ribF)
            STT: t0047(ribF)
            SPT: SPA0046(ribF)
            SEC: SC0039(ribF)
            STM: STM0045(ribF)
            YPE: YPO0474(ribF)
            YPK: y3701(ribF)
            YPM: YP_3706(ribF)
            YPA: YPA_4067
            YPN: YPN_0346
            YPP: YPDSF_3158
            YPS: YPTB0616(ribF)
            YPI: YpsIP31758_3461(ribF)
            YEN: YE0615(b0025)
            SFL: SF0021(ribF)
            SFX: S0024(ribF)
            SFV: SFV_0019(ribF)
            SBO: SBO_0024(ribF)
            SDY: SDY_0047(ribF)
            ECA: ECA3877(ribF)
            PLU: plu0590(ribF)
            BUC: BU150(ribF)
            BAS: BUsg143(ribF)
            WBR: WGLp295(ribF)
            SGL: SG0413
            ENT: Ent638_0583
            SPE: Spro_0697
            BFL: Bfl117(ribF)
            BPN: BPEN_121(ribF)
            HIN: HI0963(ribF)
            HIT: NTHI1136(ribF)
            HDU: HD0273(ribF)
            HSO: HS_0188(ribF)
            PMU: PM1661(ribF)
            MSU: MS1752(ribF)
            APL: APL_0045(ribF)
            ASU: Asuc_1877
            XFA: XF2419
            XFT: PD1438(ribF)
            XCC: XCC1154(ribF)
            XCB: XC_3088
            XCV: XCV1289(ribF)
            XAC: XAC1253(ribF)
            XOO: XOO1625(ribF)
            XOM: XOO_1511(XOO1511)
            VCH: VC0681
            VVU: VV1_0508
            VVY: VV0686
            VPA: VP0533
            VFI: VF0466
            PPR: PBPRA0590
            PAE: PA4561(ribF)
            PAU: PA14_60380(ribF)
            PAP: PSPA7_5201(ribF)
            PPU: PP_0602(ribF)
            PPF: Pput_0643
            PST: PSPTO_0805(ribF)
            PSB: Psyr_0709
            PSP: PSPPH_0720(ribF)
            PFL: PFL_5322(ribF)
            PFO: Pfl_4853
            PEN: PSEEN4693(ribF)
            PMY: Pmen_0952
            PAR: Psyc_1761(ribF)
            PCR: Pcryo_2042
            ACI: ACIAD0023(ribF)
            SON: SO_3533(ribF)
            SDN: Sden_2724
            SFR: Sfri_2891
            SAZ: Sama_0923
            SBL: Sbal_1053
            SLO: Shew_1098
            SPC: Sputcn32_1058
            SHE: Shewmr4_2958
            SHM: Shewmr7_3040
            SHN: Shewana3_3137
            SHW: Sputw3181_3107
            ILO: IL1129(ribF)
            CPS: CPS_1181(ribF)
            PHA: PSHAa0917(ribF)
            PAT: Patl_3179
            SDE: Sde_2567
            MAQ: Maqu_0861
            CBU: CBU_0391(ribF)
            CBD: COXBU7E912_1675(ribF)
            LPN: lpg0936(ribF)
            LPF: lpl0967(ribF)
            LPP: lpp0998(ribF)
            MCA: MCA2252(ribF)
            FTU: FTT0916c(ribF)
            FTF: FTF0916c(ribF)
            FTW: FTW_1263(ribF)
            FTL: FTL_0437
            FTA: FTA_0459(ribF)
            NOC: Noc_2035
            AEH: Mlg_0851
            HHA: Hhal_1837
            HCH: HCH_05934(ribF)
            CSA: Csal_0480
            ABO: ABO_0458(ribF)
            MMW: Mmwyl1_4231
            AHA: AHA_0681(ribF)
            BCI: BCI_0555(ribF)
            RMA: Rmag_0016
            VOK: COSY_0016(ribF)
            NME: NMB1834
            NMA: NMA0621(ribF)
            NMC: NMC0382(ribF)
            NGO: NGO0068
            CVI: CV_3570(ribF)
            RSO: RSc2457(ribF)
            REU: Reut_A1582
            RME: Rmet_2884
            BMA: BMA2241(ribF)
            BMV: BMASAVP1_A2657(ribF)
            BML: BMA10299_A1032(ribF)
            BMN: BMA10247_2111(ribF)
            BXE: Bxe_A0808
            BUR: Bcep18194_A5843
            BAM: Bamb_2558
            BPS: BPSL0907
            BPM: BURPS1710b_1124(ribF)
            BPL: BURPS1106A_0972(bimA)
            BPD: BURPS668_0968(bimA)
            BTE: BTH_I0771(ribF)
            PNU: Pnuc_1739
            BPE: BP1754(ribF)
            BPA: BPP1985(ribF)
            BBR: BB2173(ribF)
            RFR: Rfer_1433
            POL: Bpro_3848
            HAR: HEAR0846(ribF)
            MMS: mma_0829(ribF)
            NEU: NE1150(ribF)
            NET: Neut_1440
            NMU: Nmul_A2653(ribF)
            DAR: Daro_3047
            TBD: Tbd_1856
            MFA: Mfla_2209
            HPY: HP1087(ribC)
            HPJ: jhp0338(ribF)
            HPA: HPAG1_0360
            HHE: HH0518(ribF)
            HAC: Hac_0795(ribC)
            WSU: WS0586(ribF)
            TDN: Tmden_1341
            CJE: Cj0589(ribF)
            CJR: CJE0692
            CJU: C8J_0551(ribF)
            CFF: CFF8240_1110(ribF)
            CCV: CCV52592_1563(ribF)
            CHA: CHAB381_1014(ribF)
            CCO: CCC13826_2025(ribF)
            ABU: Abu_1836(ribF)
            GSU: GSU1487(ribF)
            GME: Gmet_1388
            PCA: Pcar_2151(ribF)
            DVU: DVU0450(ribF)
            DDE: Dde_3505(ribF)
            LIP: LI0709(ribF)
            BBA: Bd1507(ribC)
            DPS: DP1094
            ADE: Adeh_0621
            SAT: SYN_01948 SYN_03119
            SFU: Sfum_3182
            WOL: WD0759(ribF)
            WBM: Wbm0416
            AMA: AM1082(ribF)
            APH: APH_1161(ribF)
            ERU: Erum8130(ribF)
            ERW: ERWE_CDS_08610(ribF)
            ERG: ERGA_CDS_08520(ribF)
            ECN: Ecaj_0853
            ECH: ECH_1061(ribF)
            NSE: NSE_0040(ribF)
            PUB: SAR11_0159(ribF)
            MLO: mlr8243
            MES: Meso_0424
            SME: SMc00909(ribF)
            ATU: Atu0685(ribF)
            ATC: AGR_C_1228
            RET: RHE_CH00831(ribF)
            RLE: RL0886(ribF)
            BME: BMEII1044
            BMF: BAB2_0193
            BMS: BRA0201(ribF)
            BMB: BruAb2_0196(ribF)
            BOV: BOV_A0180(ribF)
            BJA: blr7480(ribF)
            BRA: BRADO6066(ribF)
            BBT: BBta_1717(ribF)
            RPA: RPA4379(ribF)
            RPB: RPB_4186(ribF)
            RPC: RPC_1399
            RPD: RPD_4040
            RPE: RPE_1410
            NWI: Nwi_2541
            NHA: Nham_3161
            BHE: BH13220(ribF)
            BQU: BQ10470(ribF)
            BBK: BARBAKC583_1163(ribF)
            CCR: CC_0703(ribF)
            SIL: SPO3154(ribF)
            RSP: RSP_2304(ribF)
            JAN: Jann_3365
            RDE: RD1_3523(ribF)
            PDE: Pden_3662
            MMR: Mmar10_0612
            HNE: HNE_0844(ribF)
            ZMO: ZMO0322(ribF)
            NAR: Saro_3260
            SAL: Sala_2358
            ELI: ELI_13560
            GOX: GOX1245
            GBE: GbCGDNIH1_0467
            ACR: Acry_0583
            RRU: Rru_A2965
            MAG: amb0832
            MGM: Mmc1_2148
            ABA: Acid345_2631
            BSU: BG11495(ribC)
            BHA: BH2409(ribC)
            BAN: BA3946(ribC)
            BAR: GBAA3946(ribC)
            BAA: BA_4417
            BAT: BAS3660(ribC)
            BCE: BC3807
            BCA: BCE_3847(ribC)
            BCZ: BCZK2057 BCZK3568(ribC)
            BCY: Bcer98_0968
            BTK: BT9727_3550(ribC)
            BLI: BL01220(ribC)
            BLD: BLi01892(ribC)
            BCL: ABC2224(ribC)
            BPU: BPUM_1570(ribC)
            OIH: OB1602(ribC) OB2871
            GKA: GK1267
            SAU: SA1115(ribC)
            SAV: SAV1272(ribC)
            SAM: MW1155(ribC)
            SAR: SAR1248
            SAS: SAS1206
            SAC: SACOL1291(ribF)
            SAB: SAB1134(ribC)
            SAA: SAUSA300_1165(ribF)
            SAO: SAOUHSC_01249
            SEP: SE0949
            SER: SERP0839(ribF)
            SHA: SH1641(ribC)
            SSP: SSP1493
            LMO: lmo1329(ribC)
            LMF: LMOf2365_1346(ribF)
            LIN: lin1366(ribC)
            LWE: lwe1344(ribF)
            LLA: L0167(ribC)
            LLC: LACR_1238
            LLM: llmg_1430(ribC)
            SPY: SPy_1250(mreA)
            SPZ: M5005_Spy_0960(mreA)
            SPM: spyM18_1199
            SPG: SpyM3_0886(mreA)
            SPS: SPs1086
            SPH: MGAS10270_Spy1075(mreA)
            SPI: MGAS10750_Spy1111(mreA)
            SPJ: MGAS2096_Spy1020(mreA)
            SPK: MGAS9429_Spy1064(mreA)
            SPF: SpyM50838(ribC)
            SPA: M6_Spy0950
            SPB: M28_Spy0933(mreA)
            SPN: SP_1110
            SPR: spr1017(mreA)
            SPD: SPD_0994(ribF)
            SAG: SAG0997(ribF)
            SAN: gbs1032
            SAK: SAK_1092(ribF)
            SMU: SMU.1143c
            STC: str0996(ribC)
            STL: stu0996(ribC)
            LPL: lp_0850(ribC1) lp_2031(ribC2)
            LJO: LJ1484
            LAC: LBA1252(ribC)
            LSA: LSA1241
            LSL: LSL_0575(ribF)
            LDB: Ldb1316(ribC)
            LBU: LBUL_1230
            LBR: LVIS_1332
            LCA: LSEI_1569
            EFA: EF1295(ribF)
            OOE: OEOE_1312
            STH: STH1526
            CAC: CAC1806
            CPE: CPE1682(ribC)
            CPF: CPF_1936(ribF)
            CPR: CPR_1654(ribF)
            CTC: CTC01279
            CBA: CLB_2278(ribF)
            CBH: CLC_2261(ribF)
            CBF: CLI_2470(ribF)
            CHY: CHY_1762(ribF)
            DSY: DSY2513(ribF)
            SWO: Swol_0904
            TTE: TTE1389(ribF)
            MTA: Moth_1054(ribF)
            MGE: MG_145
            MPN: MPN158(yaaC)
            MPU: MYPU_5480(ribF)
            MPE: MYPE9310
            MMY: MSC_0106(ribC)
            MMO: MMOB4680(ribF)
            MHY: mhp102(ribF)
            MHJ: MHJ_0270
            MHP: MHP7448_0278
            MSY: MS53_0563(ribF)
            MCP: MCAP_0061
            UUR: UU355(ribF)
            MFL: Mfl334
            MTU: Rv2786c(ribF)
            MTC: MT2856(ribF)
            MBO: Mb2809c(ribF)
            MLE: ML0852(ribF)
            MPA: MAP2893c(ribF)
            MAV: MAV_3678(ribF)
            MSM: MSMEG_2653(ribF)
            MMC: Mmcs_2098
            CGL: NCgl1903(cgl1978)
            CGB: cg2169(ribF)
            CEF: CE1871(ribF)
            CDI: DIP1470(ribF)
            CJK: jk1136(ribF)
            NFA: nfa38900(ribF)
            RHA: RHA1_ro06653(ribF)
            SCO: SCO5711(SC9F2.05c)
            SMA: SAV2546(ribF)
            TWH: TWT581(ribF)
            TWS: TW180(ribF)
            LXX: Lxx07280(ribF)
            CMI: CMM_2141(ribF)
            PAC: PPA1474
            TFU: Tfu_0782
            FRA: Francci3_3557(ribF)
            FAL: FRAAL5755(ribF)
            SEN: SACE_5918(ribF)
            BLO: BL1619(ribF)
            BAD: BAD_0357(ribF)
            FNU: FN0707
            CTR: CT093(ribF)
            CTA: CTA_0098(ribF)
            CMU: TC0368
            CPN: CPn0320(ribF)
            CPA: CP0437
            CPJ: CPj0320(ribF)
            CPT: CpB0331(ribC)
            CCA: CCA00462(ribF)
            CFE: CF0545(ribF)
            PCU: pc0758(ribF)
            TPA: TP0888
            TDE: TDE0073
            LIL: LA3449(ribF)
            LIC: LIC10728(ribF)
            LBJ: LBJ_0645(ribF)
            LBL: LBL_2434(ribF)
            SYN: slr1882(ribF)
            SYW: SYNW1603(ribF)
            SYC: syc1028_d
            SYF: Synpcc7942_0492
            SYD: Syncc9605_0897
            SYE: Syncc9902_1501
            SYG: sync_0793(ribF)
            SYR: SynRCC307_1738(ribF)
            SYX: SynWH7803_1715(ribF)
            CYA: CYA_2407(ribF)
            CYB: CYB_2202(ribF)
            TEL: tll1556(ribF)
            GVI: gll0217(ribF)
            ANA: alr4848
            AVA: Ava_2118
            PMA: Pro1347(ribF)
            PMM: PMM1273(ribF)
            PMT: PMT0364(ribF)
            PMN: PMN2A_0839
            PMI: PMT9312_1367
            PMB: A9601_14721(ribF)
            PMC: P9515_14341(ribF)
            PMF: P9303_19371(ribF)
            PMG: P9301_14581(ribF)
            PMH: P9215_14981(ribF)
            PME: NATL1_16921(ribF)
            TER: Tery_1864
            BTH: BT_2543(ribF)
            BFR: BF4346
            BFS: BF4147(ribF)
            PGI: PG0957(ribF)
            SRU: SRU_1775(ribF)
            CHU: CHU_0947(ribF)
            FPS: FP0233(ribF)
            CTE: CT0244(ribF)
            CCH: Cag_1459
            PLT: Plut_1776
            DET: DET0602(ribF)
            DEH: cbdb_A584(ribF)
            DRA: DR_1008
            DGE: Dgeo_1809
            TTH: TTC0159
            TTJ: TTHA0527
            AAE: aq_139(ribF)
            TMA: TM0857
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.2
            ExPASy - ENZYME nomenclature database: 2.7.7.2
            ExplorEnz - The Enzyme Database: 2.7.7.2
            ERGO genome analysis and discovery system: 2.7.7.2
            BRENDA, the Enzyme Database: 2.7.7.2
            CAS: 9026-37-3
///
ENTRY       EC 2.7.7.3                  Enzyme
NAME        pantetheine-phosphate adenylyltransferase;
            dephospho-CoA pyrophosphorylase;
            pantetheine phosphate adenylyltransferase;
            dephospho-coenzyme A pyrophosphorylase;
            3'-dephospho-CoA pyrophosphorylase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ATP:pantetheine-4'-phosphate adenylyltransferase
REACTION    ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA
            [RN:R03035]
ALL_REAC    R03035
SUBSTRATE   ATP [CPD:C00002];
            pantetheine 4'-phosphate [CPD:C01134]
PRODUCT     diphosphate [CPD:C00013];
            3'-dephospho-CoA
COMMENT     The enzyme from several bacteria (e.g. Escherichia coli, Bacillus
            subtilis and Haemophilus influenzae) has been shown to be
            bifunctional and also to possess the activity of EC 2.3.1.157,
            glucosamine-1-phosphate N-acetyltransferase.
REFERENCE   1  [PMID:13163064]
  AUTHORS   HOAGLAND MB, NOVELLI GD.
  TITLE     Biosynthesis of coenzyme A from phospho-pantetheine and of
            pantetheine from pantothenate.
  JOURNAL   J. Biol. Chem. 207 (1954) 767-73.
  ORGANISM  pigeon, rat [GN:rno], pig [GN:ssc]
REFERENCE   2  [PMID:13107738]
  AUTHORS   NOVELLI GD.
  TITLE     Enzymatic synthesis and structure of CoA.
  JOURNAL   Fed. Proc. 12 (1953) 675-81.
REFERENCE   3  [PMID:8389542]
  AUTHORS   Martin DP, Drueckhammer DG.
  TITLE     Separate enzymes catalyze the final two steps of coenzyme A
            biosynthesis in Brevibacterium ammoniagenes: purification of
            pantetheine phosphate adenylyltransferase.
  JOURNAL   Biochem. Biophys. Res. Commun. 192 (1993) 1155-61.
  ORGANISM  Brevibacterium ammoniagenes
REFERENCE   4  [PMID:10480925]
  AUTHORS   Geerlof A, Lewendon A, Shaw WV.
  TITLE     Purification and characterization of phosphopantetheine
            adenylyltransferase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 274 (1999) 27105-11.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:10329792]
  AUTHORS   Izard T, Geerlof A, Lewendon A, Barker JJ.
  TITLE     Cubic crystals of phosphopantetheine adenylyltransferase from
            Escherichia coli.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 55 ( Pt 6) (1999) 1226-8.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K00954  pantetheine-phosphate adenylyltransferase
            KO: K02201  pantetheine-phosphate adenylyltransferase
            KO: K02318  pantetheine-phosphate adenylyltransferase
GENES       HSA: 80347(COASY)
            MMU: 71743(Coasy)
            SSC: 396688(PPAT/DPCK)
            EHI: 53.t00026
            ECO: b3634(coaD)
            ECJ: JW3609(coaD)
            ECE: Z5058(kdtB)
            ECS: ECs4509
            ECC: c4458(kdtB)
            ECI: UTI89_C4177(kdtB)
            ECP: ECP_3732
            ECW: EcE24377A_4135(coaD)
            ECX: EcHS_A3843(coaD)
            STY: STY4069(kdtB)
            STT: t3793(coaD)
            SPT: SPA3577(coaD)
            SEC: SC3648(kdtB)
            STM: STM3725(kdtB)
            YPE: YPO0053(coaD)
            YPK: y0088(kdtB)
            YPM: YP_0054(coaD)
            YPA: YPA_3489
            YPN: YPN_3797
            YPP: YPDSF_3852
            YPS: YPTB0050(coaA)
            YPI: YpsIP31758_0065(coaD)
            SFL: SF3673(kdtB)
            SFX: S4095(kdtB)
            SFV: SFV_3895(kdtB)
            SSN: SSON_3773(kdtB)
            SBO: SBO_3636(kdtB)
            SDY: SDY_4064(kdtB)
            ECA: ECA0150(kdtB)
            PLU: plu4856(coaD)
            BUC: BU583(kdtB)
            BAS: BUsg562(kdtB)
            WBR: WGLp289(kdtB)
            SGL: SG2205
            ENT: Ent638_0105
            SPE: Spro_4838
            BPN: BPEN_634(coaD)
            HIN: HI0651(kdtB)
            HIT: NTHI0771(kdtB)
            HIP: CGSHiEE_08975(coaD)
            HIQ: CGSHiGG_06535(coaD)
            HDU: HD0453(coaD)
            HSO: HS_1589(kdtB)
            PMU: PM1304(kdtB)
            MSU: MS1951(coaD)
            APL: APL_1133(coaD)
            ASU: Asuc_0675
            XFA: XF0980
            XFT: PD0275(coaD)
            XCC: XCC2391(kdtB)
            XCB: XC_1723
            XCV: XCV2709(coaD)
            XAC: XAC2526(kdtB)
            XOO: XOO2508(kdtB)
            XOM: XOO_2372(XOO2372)
            VCH: VC0222(KdtB)
            VCO: VC0395_A2603(coaD)
            VVU: VV1_0819
            VVY: VV0292
            VPA: VP0190(kdtB)
            VFI: VF0132
            PPR: PBPRA0208
            PAE: PA0363(coaD)
            PAU: PA14_04760(coaD)
            PAP: PSPA7_0457(coaD)
            PPU: PP_5123(coaD)
            PPF: Pput_4997
            PST: PSPTO_0417
            PSB: Psyr_4758
            PSP: PSPPH_4789(coaD)
            PFL: PFL_5868(coaD)
            PFO: Pfl_5348
            PEN: PSEEN0290(coaD)
            PMY: Pmen_4191
            PAR: Psyc_0326(coaD)
            PCR: Pcryo_0359
            PRW: PsycPRwf_2006
            ACI: ACIAD2893(coaD)
            SON: SO_4684(coaD)
            SDN: Sden_0208
            SFR: Sfri_3926
            SAZ: Sama_0110
            SBL: Sbal_0068
            SBM: Shew185_4331
            SLO: Shew_3692
            SPC: Sputcn32_3888
            SSE: Ssed_0115
            SPL: Spea_4107
            SHE: Shewmr4_3888
            SHM: Shewmr7_3983
            SHN: Shewana3_4091
            SHW: Sputw3181_0060
            ILO: IL0271(coaD)
            CPS: CPS_0213(coaD)
            PHA: PSHAa2282(coaD)
            PAT: Patl_0053
            SDE: Sde_3599
            PIN: Ping_0043
            MAQ: Maqu_3575
            CBU: CBU_0288(coaD)
            CBD: COXBU7E912_1793(coaD)
            LPN: lpg0548(kdtB)
            LPF: lpl0590
            LPP: lpp0609
            MCA: MCA0066(coaD)
            FTU: FTT0581(coaD)
            FTF: FTF0581(coaD)
            FTW: FTW_1430(coaD)
            FTL: FTL_1330
            FTH: FTH_1295(coaD)
            FTA: FTA_1405(coaD)
            FTN: FTN_0754(coaD)
            TCX: Tcr_1930
            NOC: Noc_1930
            AEH: Mlg_2655
            HHA: Hhal_2309
            HCH: HCH_01010(coaD)
            CSA: Csal_2935
            ABO: ABO_0081(coaD)
            MMW: Mmwyl1_0548
            AHA: AHA_0166(coaD)
            DNO: DNO_1005(coaD)
            BCI: BCI_0176(coaD)
            RMA: Rmag_0354
            VOK: COSY_0345(coaD)
            NME: NMB2019(kdtB)
            NMA: NMA0421(kdtB)
            NGO: NGO2085
            CVI: CV_1103(kdtB)
            RSO: RSc0390(kdtB)
            REU: Reut_A0338
            REH: H16_A0367
            RME: Rmet_0285
            BMA: BMA3125(coaD)
            BMV: BMASAVP1_A0093(coaD)
            BML: BMA10299_A1497(coaD)
            BMN: BMA10247_2925(coaD)
            BXE: Bxe_A4138
            BVI: Bcep1808_2912
            BUR: Bcep18194_A6137
            BCN: Bcen_2193
            BCH: Bcen2424_2807
            BAM: Bamb_2867
            BPS: BPSL0516(coaD)
            BPM: BURPS1710b_0748(coaD)
            BPL: BURPS1106A_0580(coaD)
            BPD: BURPS668_0564(coaD)
            BTE: BTH_I0469(coaD)
            PNU: Pnuc_1924
            BPE: BP3471(coaD)
            BPA: BPP0847(coaD)
            BBR: BB0941(coaD)
            RFR: Rfer_1667
            POL: Bpro_1282
            PNA: Pnap_0895
            AAV: Aave_3869
            AJS: Ajs_3516
            VEI: Veis_4765
            MPT: Mpe_A3224
            HAR: HEAR2900(coaD)
            MMS: mma_3135(coaD)
            NEU: NE0968(coaD)
            NET: Neut_2341
            NMU: Nmul_A2734
            EBA: ebA1397(coaD)
            AZO: azo0762(coaD)
            DAR: Daro_3723
            TBD: Tbd_0380
            MFA: Mfla_0737
            HPY: HP1475(kdtB)
            HPJ: jhp1368(kdtB)
            HPA: HPAG1_1438
            HHE: HH1361(kdtB)
            HAC: Hac_1735(kdtB)
            WSU: WS0612(kdtB)
            TDN: Tmden_1125
            CJE: Cj0767c(kdtB)
            CJR: CJE0858(coaD)
            CJJ: CJJ81176_0788(coaD)
            CJU: C8J_0718(kdtB)
            CJD: JJD26997_1245(coaD)
            CFF: CFF8240_0892(coaD)
            CCV: CCV52592_1097(coaD)
            CHA: CHAB381_0923(coaD)
            CCO: CCC13826_1270(coaD)
            ABU: Abu_0967(coaD)
            NIS: NIS_0820(coaD)
            SUN: SUN_1353(coaD)
            GSU: GSU1243(coaD)
            GME: Gmet_1759
            GUR: Gura_2500
            PCA: Pcar_1640
            PPD: Ppro_2190
            DVU: DVU1532(coaD)
            DVL: Dvul_1599
            DDE: Dde_1783
            LIP: LI0282(kdtB)
            BBA: Bd0623(ppaT)
            DPS: DP2774
            ADE: Adeh_1732
            AFW: Anae109_2065
            MXA: MXAN_3385(coaD) MXAN_5358(coaD)
            SAT: SYN_00909
            SFU: Sfum_2992 Sfum_3034
            WOL: WD0524(coaD)
            WBM: Wbm0801
            AMA: AM509(coaD)
            APH: APH_0650(coaD)
            ERU: Erum3460(coaD)
            ERW: ERWE_CDS_03530(coaD)
            ERG: ERGA_CDS_03490(coaD)
            ECN: Ecaj_0329
            ECH: ECH_0737(coaD)
            NSE: NSE_0970(coaD)
            MLO: mll0730
            MES: Meso_1402
            PLA: Plav_3050
            SME: SMc01209(coaD)
            SMD: Smed_1264
            ATU: Atu1681(coaD)
            ATC: AGR_C_3091
            RET: RHE_CH02113(coaD)
            RLE: RL2403
            BME: BMEI0886
            BMF: BAB1_1119(coaD)
            BMS: BR1095(coaD)
            BMB: BruAb1_1101(coaD)
            BOV: BOV_1056(coaD)
            OAN: Oant_2180
            BJA: bll4693(coaD)
            BRA: BRADO3997(kdtB)
            BBT: BBta_4369(kdtB)
            RPA: RPA2601(kdtB)
            RPB: RPB_2874
            RPC: RPC_2588
            RPD: RPD_2598
            RPE: RPE_2766
            NWI: Nwi_1799
            NHA: Nham_1766
            BHE: BH10110(kdtB)
            BQU: BQ07840(kdtB)
            BBK: BARBAKC583_0738(coaD)
            XAU: Xaut_3787
            CCR: CC_1581(kdtB)
            SIL: SPO2200(coaD)
            SIT: TM1040_1109
            RSP: RSP_2960
            RSH: Rsph17029_1606
            RSQ: Rsph17025_1392
            JAN: Jann_1916
            RDE: RD1_2985(coaD)
            PDE: Pden_4476
            MMR: Mmar10_1872
            HNE: HNE_2759(coaD)
            ZMO: ZMO0854(coaD)
            NAR: Saro_2252
            SAL: Sala_2193
            SWI: Swit_0023
            GOX: GOX0888
            GBE: GbCGDNIH1_1218
            ACR: Acry_1178
            RRU: Rru_A1743
            MAG: amb2382
            MGM: Mmc1_1434
            ABA: Acid345_0567
            SUS: Acid_7275
            BSU: BG13361(coaD)
            BHA: BH2589(kdtB)
            BAN: BA4139(coaD)
            BAR: GBAA4139(coaD)
            BAA: BA_4606
            BAT: BAS3841
            BCE: BC3929
            BCA: BCE_3976(coaD)
            BCZ: BCZK3688(coaD)
            BCY: Bcer98_2632
            BTK: BT9727_3671(coaD)
            BLI: BL02991(coaD)
            BLD: BLi01719(ylbI)
            BCL: ABC2377(coaD)
            BAY: RBAM_014880(coaD)
            BPU: BPUM_1395(coaD)
            OIH: OB1451(coaD)
            GKA: GK1099
            SAU: SA0973
            SAV: SAV1125
            SAM: MW1007
            SAR: SAR1098(coaD)
            SAS: SAS1059
            SAC: SACOL1134(kdtB)
            SAB: SAB0989(coaD)
            SAA: SAUSA300_1024(coaD)
            SAO: SAOUHSC_01075
            SAJ: SaurJH9_1184
            SAH: SaurJH1_1206
            SEP: SE0824
            SER: SERP0715(coaD)
            SHA: SH1828
            SSP: SSP1663
            LMO: lmo2052
            LMF: LMOf2365_2083(coaD)
            LIN: lin2158
            LWE: lwe2072(coaD)
            LLA: L21952(kdtB)
            LLC: LACR_2464
            LLM: llmg_2443(kdtB)
            SPY: SPy_1537(kdtB)
            SPZ: M5005_Spy_1267
            SPM: spyM18_1554
            SPG: SpyM3_1188(kdtB)
            SPS: SPs0674
            SPH: MGAS10270_Spy1282
            SPI: MGAS10750_Spy1374
            SPJ: MGAS2096_Spy1286
            SPK: MGAS9429_Spy1261
            SPF: SpyM50586(coaD)
            SPA: M6_Spy1288
            SPB: M28_Spy1205
            SPN: SP_1968
            SPR: spr1783(kdtB)
            SPD: SPD_1766(coaD)
            SAG: SAG0454(coaD)
            SAN: gbs0501
            SAK: SAK_0555(coaD)
            SMU: SMU.517
            STC: str1648(kdtB)
            STL: stu1648(kdtB)
            SSA: SSA_0625(kdtB)
            SGO: SGO_0651(coaD)
            LPL: lp_2133(kdtB)
            LJO: LJ0999
            LAC: LBA0836(coaD)
            LSA: LSA1073(kdtB)
            LSL: LSL_0661(coaD)
            LDB: Ldb0767(coaD)
            LBU: LBUL_0700
            LBR: LVIS_1399
            LCA: LSEI_1318
            LRE: Lreu_0641
            EFA: EF2451(coaD)
            OOE: OEOE_1259
            STH: STH1439
            CAC: CAC1738(kdtB)
            CPE: CPE1729(coaD)
            CPF: CPF_1982(coaD)
            CPR: CPR_1700(coaD)
            CTC: CTC01234
            CNO: NT01CX_2230(coaD)
            CTH: Cthe_1276
            CDF: CD2558(coaD)
            CBA: CLB_2366(coaD)
            CBH: CLC_2348(coaD)
            CBF: CLI_2554(coaD)
            CBE: Cbei_1160
            CKL: CKL_1386(coaD)
            AMT: Amet_2767
            CHY: CHY_1459(coaD)
            DSY: DSY1313
            DRM: Dred_2084
            SWO: Swol_0699
            CSC: Csac_1792
            TTE: TTE1486(coaD)
            MTA: Moth_1871
            MPU: MYPU_0970(kdtB)
            MPE: MYPE9650
            MMY: MSC_0272(kdtB)
            MMO: MMOB5760(coaD)
            MSY: MS53_0651
            MCP: MCAP_0232(coaD)
            MTU: Rv2965c
            MTC: MT3043(kdtB)
            MBO: Mb2989c(kdtB)
            MBB: BCG_2986c(kdtB)
            MLE: ML1663(coaD)
            MPA: MAP3002c(kdtB)
            MAV: MAV_3810(coaD)
            MSM: MSMEG_2414(coaD)
            MVA: Mvan_2167
            MGI: Mflv_4196
            MMC: Mmcs_1945
            MKM: Mkms_1991
            MJL: Mjls_1925
            CGL: NCgl1275(coaD)
            CGB: cg1501(coaD)
            CEF: CE1441
            CDI: DIP1139(coaD)
            CJK: jk1209(coaD)
            NFA: nfa41890
            RHA: RHA1_ro06519(coaD)
            SCO: SCO5568(coaD)
            SMA: SAV2669(coaD)
            TWH: TWT565
            TWS: TW196(coaD)
            LXX: Lxx09760(coaD)
            ART: Arth_2504
            AAU: AAur_2473(coaD)
            PAC: PPA1463
            NCA: Noca_3283
            TFU: Tfu_0648
            FRA: Francci3_3605
            FAL: FRAAL5808(coaD)
            ACE: Acel_1578
            KRA: Krad_1372
            SEN: SACE_6106(coaD)
            STP: Strop_1282
            BLO: BL0291(coaD)
            RXY: Rxyl_1373
            FNU: FN0156
            RBA: RB10654(coaD)
            BBU: BB0702(kdtB)
            BGA: BG0724(kdtB)
            BAF: BAPKO_0745(kdtB)
            TPA: TP0283
            TDE: TDE1375(coaD)
            LIL: LA4167(coaD)
            LIC: LIC13325(kdtB)
            LBJ: LBJ_2884(coaD)
            LBL: LBL_0179(coaD)
            SYN: slr0847(kdtB)
            SYW: SYNW1248(coaD)
            SYC: syc2088_d(coaD)
            SYF: Synpcc7942_2007
            SYD: Syncc9605_1365
            SYE: Syncc9902_1113
            SYG: sync_1362(coaD)
            SYR: SynRCC307_1196(coaD)
            SYX: SynWH7803_1268(coaD)
            CYA: CYA_2681(coaD)
            CYB: CYB_2196(coaD)
            TEL: tlr1165
            GVI: glr0847
            ANA: alr4700
            AVA: Ava_1966
            PMA: Pro0952(coaD)
            PMM: PMM0884(coaD)
            PMT: PMT0722(coaD)
            PMN: PMN2A_0326
            PMI: PMT9312_0916
            PMB: A9601_09771(coaD)
            PMC: P9515_09661(coaD)
            PMF: P9303_14961(coaD)
            PMG: P9301_09751(coaD)
            PMH: P9215_10081(coaD)
            PME: NATL1_09991(coaD)
            TER: Tery_1572
            BTH: BT_3034
            BFR: BF4546
            BFS: BF4334
            PGI: PG0369(coaD)
            SRU: SRU_2077(coaD)
            CHU: CHU_2667(coaD)
            GFO: GFO_2685(coaD)
            FJO: Fjoh_2616
            CTE: CT0965(kdtB)
            CCH: Cag_1439
            CPH: Cpha266_1015
            PVI: Cvib_0767
            PLT: Plut_1190
            DET: DET0190(coaD)
            DEH: cbdb_A197(coaD)
            DEB: DehaBAV1_0163
            RRS: RoseRS_2610
            RCA: Rcas_1807
            DRA: DR_0642(kdtB)
            DGE: Dgeo_0286
            TTH: TTC0560
            TTJ: TTHA0929
            AAE: aq_253(kdtB)
            TMA: TM0741(kdtB)
            TPT: Tpet_0188
            TME: Tmel_0516
            FNO: Fnod_0668
            MJA: MJ1030
            MMP: MMP1093(coaD)
            MAC: MA3546
            MBA: Mbar_A2339
            MMA: MM_0458
            MBU: Mbur_2031
            MHU: Mhun_0620
            MTH: MTH1896
            MST: Msp_0514
            MSI: Msm_0785
            MKA: MK1504
            AFU: AF2206
            HAL: VNG1390a
            HMA: rrnAC0868(coaD2) rrnAC2278(coaD1)
            HWA: HQ2565A(ppaT)
            NPH: NP3368A
            TAC: Ta1194
            TVO: TVN0403
            PTO: PTO0508
            PHO: PH0624
            PAB: PAB0944
            PFU: PF1084
            TKO: TK2128
            RCI: RCIX1100(coaD)
            PAI: PAE0887
STRUCTURES  PDB: 1B6T  1GN8  1H1T  1O6B  1OD6  1QJC  1TFU  1VLH  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.3
            ExPASy - ENZYME nomenclature database: 2.7.7.3
            ExplorEnz - The Enzyme Database: 2.7.7.3
            ERGO genome analysis and discovery system: 2.7.7.3
            BRENDA, the Enzyme Database: 2.7.7.3
            CAS: 9026-99-7
///
ENTRY       EC 2.7.7.4                  Enzyme
NAME        sulfate adenylyltransferase;
            ATP-sulfurylase;
            adenosine-5'-triphosphate sulfurylase;
            adenosinetriphosphate sulfurylase;
            adenylylsulfate pyrophosphorylase;
            ATP sulfurylase;
            ATP-sulfurylase;
            sulfurylase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ATP:sulfate adenylyltransferase
REACTION    ATP + sulfate = diphosphate + adenylyl sulfate [RN:R00529]
ALL_REAC    R00529;
            (other) R04929
SUBSTRATE   ATP [CPD:C00002];
            sulfate [CPD:C00059]
PRODUCT     diphosphate [CPD:C00013];
            adenylyl sulfate [CPD:C00224]
COMMENT     The human phosphoadenosine-phosphosulfate synthase (PAPS) system is
            a bifunctional enzyme (fusion product of two catalytic activities).
            In a first step, sulfate adenylyltransferase catalyses the formation
            of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate.
            The second step is catalysed by the adenylylsulfate kinase portion
            of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which
            involves the formation of PAPS from enzyme-bound APS and ATP. In
            contrast, in bacteria, yeast, fungi and plants, the formation of
            PAPS is carried out by two individual polypeptides, sulfate
            adenylyltransferase (EC 2.7.7.4) and adenylyl-sulfate kinase (EC
            2.7.1.25).
REFERENCE   1
  AUTHORS   Bandurski, R.S., Wilson, L.G., Squires, C.L.
  TITLE     The mechanism of "active sulfate" formation.
  JOURNAL   J. Am. Chem. Soc. 78 (1956) 6408-6409.
REFERENCE   2
  AUTHORS   Hilz, H. and Lipmann, F.
  TITLE     The enzymatic activation of sulfate.
  JOURNAL   Proc. Natl. Acad. Sci. USA 41 (1955) 880-890.
  ORGANISM  Neurospora sitophila
REFERENCE   3  [PMID:9668121]
  AUTHORS   Venkatachalam KV, Akita H, Strott CA.
  TITLE     Molecular cloning, expression, and characterization of human
            bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its
            functional domains.
  JOURNAL   J. Biol. Chem. 273 (1998) 19311-20.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00450  Selenoamino acid metabolism
            PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K00955  sulfate adenylyltransferase
            KO: K00956  sulfate adenylyltransferase subunit 1
            KO: K00957  sulfate adenylyltransferase subunit 2
            KO: K00958  sulfate adenylyltransferase
GENES       HSA: 9060(PAPSS2) 9061(PAPSS1)
            PTR: 461422(PAPSS1)
            MMU: 23971(Papss1) 23972(Papss2)
            CFA: 478504(PAPSS1) 486463(PAPSS2)
            GGA: 422530(PAPSS1)
            XTR: 448413(papss1)
            SPU: 576349(LOC576349)
            DME: Dmel_CG8363(Paps)
            CEL: T14G10.1(pps-1)
            ATH: AT4G14680(APS3) AT5G43780(APS4)
            OSA: 4334073
            CME: CMS096C CMT110C
            SCE: YJR010W(MET3)
            AGO: AGOS_AGR322W
            PIC: PICST_75451(MET3)
            CGR: CAGL0B03839g
            SPO: SPBC27.08c SPBC28F2.01c
            ANI: AN4769.2
            AFM: AFUA_3G06530
            AOR: AO090020000349
            CNE: CNI03560
            UMA: UM05103.1
            DDI: DDB_0230064
            TET: TTHERM_00655750 TTHERM_00666610
            EHI: 66.t00002 79.t00002 92.t00033
            ECO: b2751(cysN) b2752(cysD)
            ECJ: JW2721(cysN) JW2722(cysD)
            ECE: Z4059(cysN) Z4060(cysD)
            ECS: ECs3605 ECs3606
            ECC: c3318(cysN) c3319(cysD)
            ECI: UTI89_C3122(cysN) UTI89_C3123(cysD)
            ECP: ECP_2733 ECP_2734
            ECV: APECO1_3772(cysD) APECO1_3773(cysN)
            ECW: EcE24377A_3052(cysN) EcE24377A_3053(cysD)
            ECX: EcHS_A2889(cysN) EcHS_A2890(cysD)
            STY: STY3059(cysN) STY3060(cysD)
            STT: t2835(cysN) t2836(cysD)
            SPT: SPA2790(cysN) SPA2791(cysD)
            SEC: SC2866(cysN) SC2867(cysD)
            STM: STM2934(cysN) STM2935(cysD)
            YPE: YPO3365(cysN) YPO3366(cysD)
            YPK: y0823(cysD) y0824(cysN)
            YPM: YP_0321(cysD) YP_0322(cysN)
            YPA: YPA_2777 YPA_2778
            YPN: YPN_0727 YPN_0728
            YPP: YPDSF_2995
            YPS: YPTB0765(cysD) YPTB0766(cysN)
            YPI: YpsIP31758_3303(cysN) YpsIP31758_3304(cysD)
            SFL: SF2774(cysN) SF2775(cysD)
            SFX: S2967(cysN) S2968(cysD)
            SFV: SFV_2746(cysD) SFV_2747(cysN)
            SSN: SSON_2899(cysN) SSON_2900(cysD)
            SBO: SBO_2768(cysD) SBO_2769(cysN)
            SDY: SDY_2950(cysN) SDY_2951(cysD)
            ECA: ECA3542(cysN) ECA3543(cysD)
            PLU: plu0709(cysD) plu0710(cysN)
            BUC: BU423(cysN) BU424(cysD)
            SGL: SG0521 SG0522
            ENT: Ent638_3222
            SPE: Spro_0819
            BFL: Bfl162(cysD) Bfl163(cysN)
            BPN: BPEN_167(cysD) BPEN_168(cysN)
            MSU: MS1251(cysN) MS1252(cysH)
            APL: APL_1844(cysN)
            ASU: Asuc_1688 Asuc_1689
            XFA: XF1500 XF1501
            XFT: PD0717(cysD) PD0718(nodQ)
            XCC: XCC3171(nodQ) XCC3172(cysD)
            XCB: XC_0993 XC_0994
            XCV: XCV3445(cysN) XCV3446(cysD)
            XAC: XAC3328(nodQ) XAC3329(cysD)
            XOO: XOO3396(nodQ) XOO3397(raxP)
            XOM: XOO_3197(XOO3197) XOO_3198(XOO3198)
            VCH: VC2559 VC2560
            VCO: VC0395_A2136(cysN) VC0395_A2137(cysD)
            VVU: VV1_0725 VV1_0726
            VVY: VV0411 VV0412
            VPA: VP0292 VP0293
            VFI: VF0320 VF0321
            PPR: PBPRA3310(cysN) PBPRA3311
            PAE: PA4442(cysN) PA4443(cysD)
            PAU: PA14_57720(cysD)
            PPU: PP_1303(cysD) PP_1304(cysNC)
            PST: PSPTO_4432(cysN/C) PSPTO_4433(cysD)
            PSB: Psyr_4126 Psyr_4128
            PSP: PSPPH_4132(cysNC) PSPPH_4133(cysD)
            PFL: PFL_0935(cysD) PFL_0936(cysN) PFL_5480(cysD) PFL_5482(cysNC)
            PFO: Pfl_0877 Pfl_0878
            PEN: PSEEN4517(cysNC) PSEEN4518(cysD)
            PAR: Psyc_1069(cysN)
            PCR: Pcryo_1393
            PRW: PsycPRwf_1111 PsycPRwf_1860 PsycPRwf_2043
            ACI: ACIAD1072(cysD) ACIAD1073(cysN)
            SON: SO_3726(cysN) SO_3727(cysD)
            SDN: Sden_0959 Sden_0960
            SFR: Sfri_3186 Sfri_3187
            SAZ: Sama_2890
            SBL: Sbal_3407
            SBM: Shew185_0929
            SLO: Shew_1423
            SPC: Sputcn32_3042
            SSE: Ssed_2960 Ssed_2987
            SPL: Spea_0664
            SHE: Shewmr4_3071
            SHM: Shewmr7_0901
            SHN: Shewana3_0863 Shewana3_0864
            SHW: Sputw3181_0903
            CPS: CPS_2142(cysD) CPS_2143(cysN)
            PHA: PSHAa0211(cysN) PSHAa0212(cysD)
            PAT: Patl_1648 Patl_1651
            SDE: Sde_2143 Sde_2145
            PIN: Ping_0798 Ping_3437
            MAQ: Maqu_2623 Maqu_2735
            CBU: CBU_0700
            CBD: COXBU7E912_0714(sat)
            MCA: MCA2628 MCA2629(cysD)
            FTU: FTT1050c(cysN)
            FTF: FTF1050c(cysN)
            FTW: FTW_0959(cysN)
            FTL: FTL_1034 FTL_1035
            FTA: FTA_1094 FTA_1095
            FTN: FTN_0927(cysN) FTN_0928(cysD)
            NOC: Noc_2288 Noc_2289
            AEH: Mlg_1260 Mlg_2344 Mlg_2345
            HHA: Hhal_2353 Hhal_2354
            HCH: HCH_05342 HCH_05344
            CSA: Csal_1686 Csal_1687 Csal_2552
            ABO: ABO_0730(sopT)
            MMW: Mmwyl1_2183
            AHA: AHA_3566 AHA_3567
            BCI: BCI_0213(cysN) BCI_0214(cysD)
            RMA: Rmag_0085
            VOK: COSY_0089(sat)
            NME: NMB1153 NMB1154 NMB1191 NMB1192
            NMA: NMA1364(cysN) NMA1365(cysD)
            NMC: NMC1093(cysN) NMC1094(cysD)
            CVI: CV_2306(cysD) CV_2307(cysN)
            RSO: RSc2421(cysN) RSc2422(cysD)
            REU: Reut_A1530 Reut_A1531 Reut_A2692 Reut_A2693
            REH: H16_A2995(cysN1) H16_A2996(cysD) H16_B0626(cysN2)
                 H16_B0627(cysH2)
            RME: Rmet_2812 Rmet_2813
            BMA: BMA0666(cysD-1) BMA0667(cysN) BMA1623(cysD-2) BMA1639
            BMV: BMASAVP1_A2125(cysD-2) BMASAVP1_A2344(cysN)
                 BMASAVP1_A2345(cysD-1)
            BML: BMA10299_A2940(cysD-1) BMA10299_A2941(cysN)
                 BMA10299_A3189(cysD-2)
            BMN: BMA10247_1399(cysD-2) BMA10247_1658(cysN)
                 BMA10247_1659(cysD-1)
            BXE: Bxe_A3660 Bxe_A3661
            BVI: Bcep1808_2554 Bcep1808_2555 Bcep1808_3209
            BUR: Bcep18194_A3432 Bcep18194_A3445(tuf) Bcep18194_A4648(typA)
                 Bcep18194_A5495 Bcep18194_A5496 Bcep18194_A5802
                 Bcep18194_A5803 Bcep18194_B2095
            BCN: Bcen_1860 Bcen_1861
            BCH: Bcen2424_2471 Bcen2424_2472
            BAM: Bamb_2520 Bamb_2521
            BPS: BPSL0959(cysD) BPSL0960(cysN) BPSL2217 BPSL2233
            BPM: BURPS1710b_1169(cysD-1) BURPS1710b_1170(cysN)
                 BURPS1710b_2649(cysD-2) BURPS1710b_2668(cysN)
            BPL: BURPS1106A_1016(cysD) BURPS1106A_1017(cysN)
                 BURPS1106A_2563(cysD)
            BPD: BURPS668_1009(cysD) BURPS668_1010(cysN) BURPS668_2510(cysD)
                 BURPS668_A1702(cysD)
            BTE: BTH_I0817 BTH_I0818 BTH_I1952 BTH_I1968
            PNU: Pnuc_1483
            BPE: BP0970A(cysD) BP0971(cysN)
            BPA: BPP1660(cysD) BPP1661(cysN)
            BBR: BB3447(cysN) BB3448(cysD)
            RFR: Rfer_2459 Rfer_2460
            POL: Bpro_2335 Bpro_2336
            PNA: Pnap_2430 Pnap_2431
            AAV: Aave_3055 Aave_3056
            AJS: Ajs_1791 Ajs_1792
            VEI: Veis_4331 Veis_4332
            MPT: Mpe_A1499 Mpe_A1500
            HAR: HEAR2066(lepA) HEAR2395(cysD) HEAR2396(cysN) HEAR2433(infB)
            MMS: mma_2455(cysD) mma_2456(cysN)
            NEU: NE0856(cysD) NE0857(cysN)
            NET: Neut_0164 Neut_1188 Neut_1189
            NMU: Nmul_A1148 Nmul_A1149
            EBA: ebA2625(cysD) ebA2628(cysN)
            AZO: azo0429(cysD)
            DAR: Daro_2944 Daro_2945
            TBD: Tbd_0210 Tbd_0874
            MFA: Mfla_1673 Mfla_1674
            WSU: WS1008 WS1009 WS1938
            TDN: Tmden_0157 Tmden_0158 Tmden_1489
            CJE: Cj1609
            CJR: CJE1781
            CJU: C8J_1510
            ABU: Abu_2174(cysD) Abu_2175(cysNC)
            SUN: SUN_1721(cysN) SUN_1722(cysD)
            GSU: GSU1717(cysD) GSU1718
            GME: Gmet_2859 Gmet_2860
            GUR: Gura_0164 Gura_1053 Gura_1066 Gura_3933
            PCA: Pcar_1768 Pcar_1769
            PPD: Ppro_0064 Ppro_0665 Ppro_0678
            DVU: DVU1295(sat) DVU1566
            DVL: Dvul_1771 Dvul_2441
            DDE: Dde_2265 Dde_3173
            DPS: DP1472 DP2110
            ADE: Adeh_1947
            AFW: Anae109_1643 Anae109_1644 Anae109_1910 Anae109_2229
                 Anae109_4403
            MXA: MXAN_2336(cysN) MXAN_2337(cysD)
            SFU: Sfum_1046 Sfum_1220
            MLO: mlr7575 mlr7576
            MES: Meso_0833 Meso_0834
            PLA: Plav_3064
            SME: SMa0855(nodP1) SMa0857(nodQ1) SMb21223(nodP2) SMb21224(nodQ2)
                 SMc00090(cysN) SMc00091(cysD)
            SMD: Smed_0557 Smed_4560 Smed_6191
            ATU: Atu0816(cysN) Atu0817(cysD)
            ATC: AGR_C_1495 AGR_C_1496
            RET: RHE_CH01130(cysN) RHE_CH01131(cysD)
            RLE: RL1260(cysN) RL1261(cysD)
            BME: BMEI1754 BMEI1755
            BMF: BAB1_0193 BAB1_0194
            BMS: BR0193(cysD) BR0194(cysNC)
            BMB: BruAb1_0188(cysD) BruAb1_0189(cysNC)
            BOV: BOV_0185(cysD) BOV_0186(cysNC)
            OAN: Oant_0201
            BJA: bll1475(nodQ) bll1476(cysD)
            BRA: BRADO1063 BRADO1064(cysD) BRADO5192 BRADO5193
            BBT: BBta_0327 BBta_0328 BBta_6983(cysD) BBta_6984(cysNC)
            RPA: RPA0752(cysD) RPA0753(cysN)
            RPB: RPB_1042 RPB_1043
            RPC: RPC_0063 RPC_0064 RPC_4016 RPC_4017
            RPD: RPD_1153 RPD_1154
            RPE: RPE_0333 RPE_0334 RPE_1761 RPE_1762
            NWI: Nwi_2763 Nwi_2764
            NHA: Nham_3564
            XAU: Xaut_1400
            CCR: CC_1482 CC_1483
            SIL: SPO0900(sat)
            SIT: TM1040_0612
            RSP: RSP_1575(sopT)
            RSH: Rsph17029_0227
            RSQ: Rsph17025_0255
            JAN: Jann_3340
            RDE: RD1_B0030(sat)
            PDE: Pden_4395 Pden_4396
            MMR: Mmar10_2450 Mmar10_2451
            HNE: HNE_0776(cysNC) HNE_0777(cysD)
            ZMO: ZMO0004(cysN) ZMO0005(cysD)
            NAR: Saro_3252 Saro_3253
            SAL: Sala_1526 Sala_1527
            SWI: Swit_3342
            ELI: ELI_13670 ELI_13675
            GOX: GOX0926 GOX0927
            GBE: GbCGDNIH1_1847 GbCGDNIH1_2160
            ACR: Acry_1319
            RRU: Rru_A0148 Rru_A2289 Rru_A2290
            MAG: amb2211 amb2212
            MGM: Mmc1_1017 Mmc1_1018
            ABA: Acid345_0828 Acid345_0829
            SUS: Acid_6513
            BSU: BG13106(yitA) BG13378(sat)
            BHA: BH1487 BH3386
            BAN: BA1441(sat)
            BAR: GBAA1441(sat)
            BAA: BA_1962
            BAT: BAS1331
            BCE: BC1422
            BCA: BCE_1545(sat)
            BCZ: BCZK1305(sat)
            BCY: Bcer98_1144
            BTK: BT9727_1304(sat)
            BLI: BL02284(sat)
            BLD: BLi01780(sat)
            BCL: ABC0612(sat)
            BAY: RBAM_015420(sat)
            BPU: BPUM_1458(sat)
            OIH: OB1659
            GKA: GK0415
            SAJ: SaurJH9_0571
            SAH: SaurJH1_0585
            SEP: SE2175
            SER: SERP2186(sat)
            SHA: SH0419
            SSP: SSP2402
            LPL: lp_1378(cysD)
            STH: STH1143
            CAC: CAC0109(cysD) CAC0110(cysN)
            CTH: Cthe_2537
            CBE: Cbei_0136 Cbei_0149 Cbei_4186
            CKL: CKL_1795(cysN) CKL_1796(cysD)
            AMT: Amet_3492
            CHY: CHY_2689(saT)
            DSY: DSY2951(cysN) DSY2952(cysD)
            DRM: Dred_0635
            CSC: Csac_0958 Csac_1643
            MTU: Rv1285(cysD) Rv1286(cysN)
            MTC: MT1323(cysD) MT1324(cysN)
            MBO: Mb1316(cysD) Mb1317(cysN)
            MBB: BCG_1344(cysD) BCG_1345(cysN)
            MPA: MAP2484c(cysN) MAP2485c(cysD) MAP2598c
            MAV: MAV_1326(sat) MAV_1436(cysD) MAV_1437(cysNC)
            MSM: MSMEG_4978(cysNC) MSMEG_4979(cysD)
            MVA: Mvan_1282 Mvan_4422 Mvan_4423
            MGI: Mflv_2271 Mflv_2272
            MMC: Mmcs_0387 Mmcs_0388 Mmcs_3918 Mmcs_3919
            MKM: Mkms_0396 Mkms_0397 Mkms_3992 Mkms_3993
            MJL: Mjls_0375 Mjls_0376 Mjls_3933
            CGL: NCgl2715(cgl2814) NCgl2716(cgl2815)
            CGB: cg3114(cysN) cg3115(cysD)
            CEF: CE2640 CE2641
            CJK: jk0246(cysD) jk0247(cysN)
            NFA: nfa14160(cysN) nfa14170(cysD) nfa24540(cysN2) nfa24550(cysD2)
                 nfa33920 nfa33930
            RHA: RHA1_ro01253 RHA1_ro01254 RHA1_ro01266 RHA1_ro01267(cysNC1)
                 RHA1_ro01518(cysNC2) RHA1_ro01519(cysD)
            SCO: SCO6097(cysN) SCO6098(cysD)
            SMA: SAV2131(cysD1) SAV2132(cysN1) SAV2133(cysN) SAV2313(cysD2)
                 SAV2314(cysN2)
            ART: Arth_2979 Arth_3122
            AAU: AAur_3090(cysN) AAur_3091(cysD)
            NCA: Noca_3922 Noca_4207 Noca_4208
            TFU: Tfu_0419 Tfu_0420 Tfu_0425
            FRA: Francci3_1339 Francci3_1341 Francci3_1342
            FAL: FRAAL2108(cysD)
            ACE: Acel_1617
            KRA: Krad_0685
            SEN: SACE_1473(cysN) SACE_1474(cysD) SACE_3527 SACE_3530
                 SACE_3531(cysN)
            STP: Strop_0793 Strop_0794
            RXY: Rxyl_0966
            RBA: RB7941(cysN) RB7943(cysD)
            LIL: LA4219(cysN) LA4220(cysD)
            LIC: LIC13370(cysN) LIC13371(cysD)
            LBJ: LBJ_2840(cysN) LBJ_2841(cysH-2)
            LBL: LBL_0230(cysH-2) LBL_0231(cysN)
            SYN: slr1165(met3)
            SYW: SYNW0304(cysD)
            SYC: syc1217_c(met3)
            SYF: Synpcc7942_0295
            SYD: Syncc9605_0300
            SYE: Syncc9902_2044
            SYG: sync_0354(sat)
            SYR: SynRCC307_2194(cysD)
            SYX: SynWH7803_0354(cysD)
            CYA: CYA_1559(sat)
            CYB: CYB_1070(sat)
            TEL: tll1044
            GVI: glr1084
            ANA: all5138
            AVA: Ava_1867(infB) Ava_2382
            PMA: Pro0256(MET3)
            PMM: PMM0227(cysD)
            PMT: PMT1799(cysD)
            PMN: PMN2A_1596
            PMI: PMT9312_0229
            PMB: A9601_02481(met3)
            PMC: P9515_02591(met3)
            PMF: P9303_23841(met3)
            PMG: P9301_02491(met3)
            PME: NATL1_03071(met3)
            TER: Tery_2625
            BTH: BT_0414 BT_0415
            BFR: BF1668 BF1669
            BFS: BF1676(cysD) BF1677(cysN)
            SRU: SRU_0580(cysD) SRU_0581
            CHU: CHU_0635(cysN) CHU_0636(cysD)
            GFO: GFO_0324(cysD) GFO_0325(cysN)
            FJO: Fjoh_1502 Fjoh_1503
            CTE: CT0862(sat)
            CCH: Cag_0490(lepA) Cag_1518(typA) Cag_1587
            PVI: Cvib_0630 Cvib_0631
            PLT: Plut_1559 Plut_1560
            RRS: RoseRS_3336
            RCA: Rcas_4308
            DRA: DR_A0016
            DGE: Dgeo_1410
            TTH: TTC0307
            TTJ: TTHA0666
            AAE: aq_1081(cysD)
            MMP: MMP0941
            MMQ: MmarC5_0208
            MMZ: MmarC7_0615
            MAE: Maeo_0782
            MVN: Mevan_0680
            MTP: Mthe_0821
            MEM: Memar_0730
            MBN: Mboo_0699
            AFU: AF1667(sat)
            HWA: HQ1668A(cysD)
            NPH: NP4570A(cysD)
            PAB: PAB1595(sat)
            PFU: PF1220 PF1221
            RCI: RRC481(sat)
            APE: APE_1197.1
            SMR: Smar_0337 Smar_0810
            IHO: Igni_0970 Igni_1150
            HBU: Hbut_1499
            SSO: SSO2912(sat)
            STO: ST2568
            SAI: Saci_2203(sat)
            MSE: Msed_0041 Msed_0963
            PAI: PAE2609
            PIS: Pisl_0397 Pisl_1511
            PCL: Pcal_1111 Pcal_1424
            PAS: Pars_1240 Pars_1362
            TPE: Tpen_0647
STRUCTURES  PDB: 1G8F  1G8G  1G8H  1I2D  1J70  1JEC  1JED  1JEE  1JHD  1M8P  
                 1R6X  1TV6  1V47  1X6V  1XJQ  1XNJ  1ZUN  2GKS  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.4
            ExPASy - ENZYME nomenclature database: 2.7.7.4
            ExplorEnz - The Enzyme Database: 2.7.7.4
            ERGO genome analysis and discovery system: 2.7.7.4
            BRENDA, the Enzyme Database: 2.7.7.4
            CAS: 9012-39-9
///
ENTRY       EC 2.7.7.5                  Enzyme
NAME        sulfate adenylyltransferase (ADP);
            ADP-sulfurylase;
            sulfate (adenosine diphosphate) adenylyltransferase;
            adenosine diphosphate sulfurylase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ADP:sulfate adenylyltransferase
REACTION    ADP + sulfate = phosphate + adenylyl sulfate [RN:R00530]
ALL_REAC    R00530
SUBSTRATE   ADP [CPD:C00008];
            sulfate [CPD:C00059]
PRODUCT     phosphate [CPD:C00009];
            adenylyl sulfate [CPD:C00224]
REFERENCE   1  [PMID:5964041]
  AUTHORS   Grunberg-Manago M, Del Campillo-Campbell A, Dondon L, Michelson AM.
  TITLE     [Yeast ADP-sulfurylase catalyzing an exchange between orthophosphate
            and the terminal phosphate of nucleoside diphosphates]
  JOURNAL   Biochim. Biophys. Acta. 123 (1966) 1-16.
  ORGANISM  Saccharomyces fragilis
REFERENCE   2  [PMID:13502346]
  AUTHORS   ROBBINS PW, LIPMANN F.
  TITLE     Isolation and identification of active sulfate.
  JOURNAL   J. Biol. Chem. 229 (1957) 837-51.
PATHWAY     PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K00959  sulfate adenylyltransferase (ADP)
GENES       SCE: YCL050C(APA1)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.5
            ExPASy - ENZYME nomenclature database: 2.7.7.5
            ExplorEnz - The Enzyme Database: 2.7.7.5
            ERGO genome analysis and discovery system: 2.7.7.5
            BRENDA, the Enzyme Database: 2.7.7.5
            CAS: 9027-70-7
///
ENTRY       EC 2.7.7.6                  Enzyme
NAME        DNA-directed RNA polymerase;
            RNA polymerase;
            RNA nucleotidyltransferase (DNA-directed);
            RNA polymerase I;
            RNA polymerase II;
            RNA polymerase III;
            RNA nucleotidyltransferase (DNA-directed);
            C RNA formation factors;
            deoxyribonucleic acid-dependent ribonucleic acid polymerase;
            DNA-dependent ribonucleate nucleotidyltransferase;
            DNA-dependent RNA nucleotidyltransferase;
            DNA-dependent RNA polymerase;
            ribonucleate nucleotidyltransferase;
            ribonucleate polymerase;
            C ribonucleic acid formation factors;
            ribonucleic acid nucleotidyltransferase;
            ribonucleic acid polymerase;
            ribonucleic acid transcriptase;
            ribonucleic polymerase;
            ribonucleic transcriptase;
            C RNA formation factors;
            RNA nucleotidyltransferase;
            RNA transcriptase;
            transcriptase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     nucleoside-triphosphate:RNA nucleotidyltransferase (DNA-directed)
REACTION    nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444]
ALL_REAC    R00444 > R00435 R00441 R00442 R00443
SUBSTRATE   nucleoside triphosphate [CPD:C00201];
            RNAn [CPD:C00046]
PRODUCT     diphosphate [CPD:C00013];
            RNAn+1 [CPD:C00046]
COMMENT     Catalyses DNA-template-directed extension of the 3'- end of an RNA
            strand by one nucleotide at a time. Can initiate a chain de novo. In
            eukaryotes, three forms of the enzyme have been distinguished on the
            basis of sensitivity to alpha-amanitin, and the type of RNA
            synthesized. See also EC 2.7.7.19 (polynucleotide
            adenylyltransferase) and EC 2.7.7.48 (RNA-directed RNA polymerase).
REFERENCE   1
  AUTHORS   Krakow, J.S. and Ochoa, S.
  TITLE     RNA polymerase from Azotobacter vinelandii.
  JOURNAL   Methods Enzymol. 6 (1963) 11-17.
  ORGANISM  Azotobacter vinelandii
REFERENCE   2  [PMID:4946277]
  AUTHORS   Mans RJ, Walter TJ.
  TITLE     Transfer RNA-primed oligoadenylate synthesis in maize seedlings. II.
            Primer, substrate and metal specificities and size of product.
  JOURNAL   Biochim. Biophys. Acta. 247 (1971) 113-21.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   3
  AUTHORS   Roeder, R.G.
  TITLE     In: Losick, R. and Chamberlin, M. (Eds.), RNA Polymerase, Cold
            Spring Harbor Laboratory, 1976, p. 285.
REFERENCE   4  [PMID:4501121]
  AUTHORS   Sheldon R, Jurale C, Kates J.
  TITLE     Detection of polyadenylic acid sequences in viral and eukaryotic
            RNA(polu(U)-cellulose columns-poly(U) filters-fiberglass-HeLa
            cells-bacteriophage T4).
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 69 (1972) 417-21.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:5289245]
  AUTHORS   Weaver RF, Blatti SP, Rutter WJ.
  TITLE     Molecular structures of DNA-dependent RNA polymerases (II) from calf
            thymus and rat liver.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 68 (1971) 2994-9.
  ORGANISM  cow [GN:bta], rat [GN:rno]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
            PATH: map02020  Two-component system - General
            PATH: map03020  RNA polymerase
ORTHOLOGY   KO: K00960  DNA-directed RNA polymerase
            KO: K02999  DNA-directed RNA polymerase I subunit A1
            KO: K03000  DNA-directed RNA polymerase I subunit A12
            KO: K03001  DNA-directed RNA polymerase I subunit A14
            KO: K03002  DNA-directed RNA polymerase I subunit A2
            KO: K03003  DNA-directed RNA polymerase I subunit A34
            KO: K03004  DNA-directed RNA polymerase I subunit A43
            KO: K03005  DNA-directed RNA polymerase I subunit A49
            KO: K03006  DNA-directed RNA polymerase II subunit A
            KO: K03007  DNA-directed RNA Polymerase II subunit L
            KO: K03008  DNA-directed RNA polymerase II subunit J
            KO: K03009  DNA-directed RNA Polymerase II subunit K
            KO: K03010  DNA-directed RNA polymerase II subunit B
            KO: K03011  DNA-directed RNA polymerase II subunit C
            KO: K03012  DNA-directed RNA polymerase II subunit D
            KO: K03013  DNA-directed RNA polymerase II subunit E
            KO: K03014  DNA-directed RNA Polymerase II subunit F
            KO: K03015  DNA-directed RNA polymerase II subunit G
            KO: K03016  DNA-directed RNA polymerase II subunit H
            KO: K03017  DNA-directed RNA polymerase II subunit I
            KO: K03018  DNA-directed RNA polymerase III subunit C1
            KO: K03019  DNA-directed RNA polymerase III subunit C11
            KO: K03020  DNA-directed RNA polymerase III subunit C19
            KO: K03021  DNA-directed RNA polymerase III subunit C2
            KO: K03022  DNA-directed RNA polymerase III subunit C25
            KO: K03023  DNA-directed RNA polymerase III subunit C3
            KO: K03024  DNA-directed RNA polymerase III subunit C31
            KO: K03025  DNA-directed RNA polymerase III subunit C34
            KO: K03026  DNA-directed RNA polymerase III subunit C4
            KO: K03027  DNA-directed RNA Polymerase III subunit C5
            KO: K03040  DNA-directed RNA polymerase subunit alpha
            KO: K03041  DNA-directed RNA polymerase subunit A'
            KO: K03042  DNA-directed RNA polymerase subunit A"
            KO: K03043  DNA-directed RNA polymerase subunit beta
            KO: K03044  DNA-directed RNA polymerase subunit B'
            KO: K03045  DNA-directed RNA polymerase subunit B"
            KO: K03046  DNA-directed RNA polymerase subunit beta'
            KO: K03047  DNA-directed RNA polymerase subunit D
            KO: K03048  DNA-directed RNA polymerase subunit delta
            KO: K03049  DNA-directed RNA polymerase subunit E'
            KO: K03050  DNA-directed RNA polymerase subunit E"
            KO: K03051  DNA-directed RNA polymerase subunit F
            KO: K03052  DNA-directed RNA polymerase subunit G
            KO: K03053  DNA-directed RNA polymerase subunit H
            KO: K03054  DNA-directed RNA polymerase subunit I
            KO: K03055  DNA-directed RNA polymerase subunit K
            KO: K03056  DNA-directed RNA polymerase subunit L
            KO: K03057  DNA-directed RNA polymerase subunit M
            KO: K03058  DNA-directed RNA polymerase subunit N
            KO: K03059  DNA-directed RNA polymerase subunit P
            KO: K03060  DNA-directed RNA polymerase subunit omega
            KO: K04329  DNA-directed RNA polymerase complex, bacteria-type
                        {K03040+K03043+K03046+K03048+K03060}
            KO: K04470  DNA-directed RNA polymerase complex, archaea-type
                        {K03042+K03041+K03044+K03045+K03053+K03055+K03058+K03047
                        +K03049+K03050+K03056+K03057+K03059+K03051+K03052+K03054
                        }
            KO: K04471  DNA-directed RNA polymerase II complex
                        {K03006+K03010+K03011+K03012+K03013+K03014+K03015+K03016
                        +K03017+K03007+K03008+K03009}
            KO: K04472  DNA-directed RNA polymerase III complex
                        {K03018+K03021+K03027+K03022+K03020+K03019+K03023+K03026
                        +K03025+K03024}
            KO: K04473  DNA-directed RNA polymerase I complex
                        {K02999+K03002+K03000+K03005+K03004+K03003+K03001}
GENES       HSA: 11128(POLR3A) 171568(POLR3H) 25885(POLR1A) 30834(ZNRD1)
                 51082(POLR1D) 51728(POLR3K) 5430(POLR2A) 5431(POLR2B)
                 5432(POLR2C) 5433(POLR2D) 5434(POLR2E) 5435(POLR2F)
                 5436(POLR2G) 5437(POLR2H) 5438(POLR2I) 5439(POLR2J)
                 5440(POLR2K) 5441(POLR2L) 5442(POLRMT) 55703(POLR3B)
                 55718(POLR3E) 64425(POLR1E) 661(POLR3D) 84172(POLR1B)
                 84265(POLR3GL) 9533(POLR1C)
            PTR: 454119(POLR2C) 457224(POLR3C) 461305(POLR2B) 461759(POLR3G)
                 464043(POLR3D) 471027(POLR2H)
            MCC: 710891(LOC710891)
            MMU: 17749(Polr2k) 20016(Rpo1-1) 20017(Rpo1-2) 20018(Rpo1-3)
                 20019(Rpo1-4) 20020(Polr2a) 20021(Polr2c) 20022(Polr2j)
                 216151(Polrmt) 218832(Polr3a) 231329(Polr2b) 245841(Polr2h)
                 26939(Polr3e) 64424(Polr1e) 66136(Znrd1) 66420(Polr2e)
                 67005(Polr3k) 67486(Polr3g) 67710(Polr2g) 69241(Polr2d)
                 69833(Polr2f) 69870(Polr3gl) 69920(Polr2i) 70408(Polr3f)
                 70428(Polr3b) 74414(Polr3c) 78929(Polr3h)
            RNO: 117017(Polr2g) 287988(Polr2h_predicted)
                 289561(Polr2b_predicted) 310685(Polr3c) 361784(Znrd1)
                 83503(Polr2f) 83581(Rpo1-4) 83582(Rpo1-2)
            CFA: 474512(POLR2F) 474531(POLR3B) 474912(POLR1C) 475152(POLR2B)
                 475766(POLR1A) 476052(POLR2G) 477143(POLR3F) 478109(POLR2C)
                 478656(POLR2H) 479256(POLR3A) 479483(POLR2A) 483159(POLR3C)
                 483863(POLR2D) 485102(POLRMT) 607850(POLR3H) 608346(POLR3GL)
                 608689(POLR3E) 611625(POLR3K) 611859(POLR2E)
            BTA: 282312(POLR2A) 282342(RPOL-1l) 614472(POLR2I)
            GGA: 395486(POLR2F) 415635(POLR2C) 416710(POLR1B) 416723(POLR3F)
                 417990(POLR3H) 418071(POLR3B) 420084(POLRMT) 420103(POLR2E)
                 421452(POLR1C) 422621(POLR2B) 424754(POLR2D) 424954(POLR2H)
                 426289(POLR2I) 427105(POLR3G) 428713(POLR1D) 768387(POLR2K)
                 768505(POLR3K) 770704(POLR2L)
            XLA: 379695(MGC68946) 379994(rpc155) 398890(MGC68569)
                 398968(MGC68604) 399046(MGC68582) 432060(MGC81245)
                 432333(MGC78824) 443871(MGC79127) 443896(MGC80152)
                 446308(polr3c) 447138(MGC85403) 494863(LOC494863)
                 495684(LOC495684) 496260(LOC496260)
            XTR: 394729(MGC76329) 394944(polr3f) 448728(polr2f)
            DRE: 324088(polr2gl) 334669(polr2c) 393201(polr3c) 393538(polr1c)
                 394162(polr3f)
            SPU: 574957(LOC574957) 575987(LOC575987) 577662(LOC577662)
                 578317(LOC578317) 581204(LOC581204) 582938(LOC582938)
                 583058(LOC583058) 583794(LOC583794) 584422(LOC584422)
                 585724(LOC585724) 588522(LOC588522) 589946(LOC589946)
                 590155(LOC590155) 590216(LOC590216) 590699(LOC590699)
                 590827(LOC590827) 594487(LOC594487)
            DME: Dmel_CG10122(RpI1) Dmel_CG10582(Sin) Dmel_CG10685
                 Dmel_CG11246 Dmel_CG1163(RpII18) Dmel_CG11979 Dmel_CG12267
                 Dmel_CG13418 Dmel_CG13628 Dmel_CG1554(RpII215) Dmel_CG17209
                 Dmel_CG18780(MED20) Dmel_CG3114(ewg) Dmel_CG31155
                 Dmel_CG3180(RpII140) Dmel_CG3284(RpII15) Dmel_CG3756
                 Dmel_CG4033(RpI135) Dmel_CG4644 Dmel_CG5147 Dmel_CG5380
                 Dmel_CG6840 Dmel_CG7281(CycC) Dmel_CG7885(RpII33)
                 Dmel_CG8344(RpIII128)
            CEL: C06A1.5 C15H11.8 C26E6.4(rpb-2) C36B1.3 C42D4.8(rpc-1)
                 C48E7.2 F09F7.3 F14B4.3 F23B2.13 F26F4.11 F36A4.7(ama-1)
                 F58A4.9 H27M09.2 H43I07.2(transferase) W01G7.3 W09C3.4 Y37E3.3
                 Y54E10BR.6 Y77E11A.6 Y97E10AR.5 ZK856.10
            ATH: AT1G01210 AT1G61700 AT3G22900 AT4G21710(NRPB2)
                 AT4G35800(NRPB1) AT5G09920(RPB15.9) AT5G59180 ArthCp012(rpoC2)
                 ArthCp013(rpoC1) ArthCp014(rpoB) ArthCp055(rpoA)
            OSA: 3131431(rpoA) 3131432(rpoB) 3131433(rpoC1) 3131434(rpoC2)
                 4325277 4325870 4327549 4328083 4328330 4330285 4332531
                 4333066 4333343 4333888 4334766 4335250 4335691 4336254
                 4337169 4337831 4337866 4338726 4340256 4341695 4341946
                 4342517 4343168 4343220 4346392 4346491 4349001 4349985
                 4351463 4351715
            CME: CMB005C CMD026C CME101C CMG169C CMG179C CMH017C CMH117C
                 CMJ257C CMK037C CMK059C CMP008C CMP043C CMR224C CMR232C
                 CMS114C CMT451C CMT583C
            SCE: YBR154C(RPB5) YDL140C(RPO21) YDL150W(RPC53) YDR045C(RPC11)
                 YDR156W(RPA14) YDR404C(RPB7) YFL036W(RPO41) YGL070C(RPB9)
                 YHR143W-A(RPC10) YIL021W(RPB3) YJL140W(RPB4) YJL148W(RPA34)
                 YJR063W(RPA12) YKL144C(RPC25) YNL113W(RPC19) YNL151C(RPC31)
                 YNL248C(RPA49) YNR003C(RPC34) YOL005C(RPB11) YOR116C(RPO31)
                 YOR151C(RPB2) YOR207C(RET1) YOR210W(RPB10) YOR224C(RPB8)
                 YOR340C(RPA43) YOR341W(RPA190) YPR010C(RPA135) YPR110C(RPC40)
                 YPR187W(RPO26) YPR190C(RPC82)
            AGO: AGOS_ABR029W AGOS_ACL005C AGOS_ACR049W AGOS_ACR111C
                 AGOS_ACR163W AGOS_ACR224C AGOS_ACR243W AGOS_ACR250W
                 AGOS_ADL120C AGOS_ADL275C AGOS_ADR031C AGOS_ADR070W
                 AGOS_ADR086C AGOS_ADR374C AGOS_ADR377W AGOS_AEL279C
                 AGOS_AEL282W AGOS_AER036W AGOS_AER191W AGOS_AER252C
                 AGOS_AFL088W AGOS_AFL220C AGOS_AFR026C AGOS_AFR056W
                 AGOS_AFR402C AGOS_AFR404C AGOS_AFR417W AGOS_AFR638C
                 AGOS_AGR029W
            PIC: PICST_28240(RPB7) PICST_34146(RPB140) PICST_34242(RPC25)
                 PICST_36598(RPO41) PICST_37319(RPC10) PICST_37912(RPB10)
                 PICST_40538(RPS34) PICST_43548(RPC31) PICST_45576(RPC34)
                 PICST_46661(RPS43) PICST_47067(RPC11) PICST_48804(RPA12)
                 PICST_53602(RPB5) PICST_58607(RPB4) PICST_60150(RPO32)
                 PICST_60409(RPO26) PICST_61635(RPB9) PICST_62535(RBP11)
                 PICST_65363(RPC19) PICST_66237(RPO31) PICST_73507(RPA190)
                 PICST_74652(RPC40) PICST_75374(RPO21) PICST_77977(RPA135)
                 PICST_80709(RPB3) PICST_82840(RPC82) PICST_85953(RPC53)
                 PICST_87046(RPB8) PICST_87381(RET1) PICST_88096(RPA49)
            CAL: CaO19.172(rpc19) CaO19.2276 CaO19.2287 CaO19_1248(CaO19.1248)
                 CaO19_2594(CaO19.2594) CaO19_2715(CaO19.2715)
                 CaO19_2831(CaO19.2831) CaO19_3103(CaO19.3103)
                 CaO19_5360(CaO19.5360) CaO19_7655(CaO19.7655)
            CGR: CAGL0B04125g CAGL0E02453g CAGL0E05478g CAGL0E05500g
                 CAGL0F00561g CAGL0F02673g CAGL0G05874g CAGL0G10043g
                 CAGL0G10109g CAGL0H03509g CAGL0I03630g CAGL0I03828g
                 CAGL0I04400g CAGL0I06006g CAGL0I07799g CAGL0J00869g
                 CAGL0J01848g CAGL0J02420g CAGL0J04070g CAGL0J05698g
                 CAGL0J07766g CAGL0K12628g CAGL0L02849g CAGL0L04246g
                 CAGL0L11660g CAGL0M03487g
            SPO: SPAC1B3.12c(rpb10) SPAC22A12.05(rpc11) SPAC23C4.15
                 SPAC23G3.01(rpb2) SPAC26H5.12 SPAC2F3.03c SPAC3A12.07
                 SPAC4G9.08c SPAPB1E7.03 SPAPYUG7.04c(rpb9) SPBC1289.07c
                 SPBC14C8.12(rpb8) SPBC19C2.03(rpc10) SPBC28F2.12(rpb1)
                 SPBC2G5.07c SPBC337.14 SPBC3B9.07c SPBC4C3.05c(nuc1)
                 SPBC651.08c SPBC839.12 SPBP23A10.07 SPCC1020.04c(rpb6)
                 SPCC1259.03 SPCC1442.10c(rpb3) SPCC290.02
            ANI: AN0192.2 AN0321.2 AN0752.2 AN0809.2 AN1447.2 AN1521.2
                 AN2235.2 AN2283.2 AN2415.2 AN2512.2 AN2747.2 AN3933.2 AN4219.2
                 AN4269.2 AN6252.2 AN6558.2 AN7609.2 AN8272.2 AN9120.2 AN9125.2
            AFM: AFUA_1G02460 AFUA_1G05160 AFUA_1G06380 AFUA_1G13900
                 AFUA_1G14110 AFUA_1G14680 AFUA_2G05480 AFUA_2G08540
                 AFUA_2G13090 AFUA_2G13720 AFUA_2G15610 AFUA_3G08040
                 AFUA_3G14370 AFUA_4G11970 AFUA_4G12400 AFUA_5G04200
                 AFUA_5G06280 AFUA_5G11120 AFUA_6G04610 AFUA_6G08300
                 AFUA_6G10930 AFUA_7G01850 AFUA_7G01920 AFUA_7G02080
                 AFUA_7G02620 AFUA_8G04350 AFUA_8G05300
            AOR: AO090001000659 AO090003000096 AO090003000491 AO090005000619
                 AO090005000851 AO090005001477 AO090009000629 AO090011000849
                 AO090012000268 AO090012000486 AO090020000625 AO090026000228
                 AO090026000333 AO090026000830 AO090038000563 AO090038000568
                 AO090102000624 AO090103000052 AO090120000079 AO090701000084
                 AO090701000228
            CNE: CNA07710 CNB00680 CNB01360 CNB01370 CNB02280 CNC02990
                 CND03040 CND03140 CND03540 CND04750 CND05820 CNE03720 CNE05120
                 CNF00390 CNF03750 CNF04080 CNG00720 CNI00420 CNI01770 CNI02630
                 CNJ01580
            UMA: UM01133.1 UM02059.1 UM02324.1 UM02446.1 UM02628.1 UM02903.1
                 UM03058.1 UM03550.1 UM03584.1 UM03863.1 UM04460.1 UM04722.1
                 UM04879.1 UM05334.1 UM06156.1 UM06331.1
            ECU: ECU01_0600 ECU03_0290 ECU03_0440 ECU03_0490 ECU04_1400
                 ECU05_0275 ECU06_0320 ECU06_0600 ECU07_0090 ECU07_0840
                 ECU07_0960 ECU07_1750 ECU08_0320 ECU08_0650 ECU08_0765
                 ECU08_1330 ECU10_0210 ECU10_0250 ECU11_0370 ECU11_0590
                 ECU11_1400
            DDI: DDB_0191106(rpmA) DDB_0215406(rpb1) DDB_0216272(rpb6)
                 DDB_0216273(rpb10) DDB_0216277(rpb2) DDB_0216278(rpa2)
                 DDB_0216286(rpc19) DDB_0216287(rpb5) DDB_0216288(rpa5)
                 DDB_0216289(rpb3) DDB_0216290(rpa43) DDB_0216292(rpa1)
                 DDB_0216293(rpc1) DDB_0216294(rpb4) DDB_0216295(rpb7)
                 DDB_0216297(rpb8) DDB_0216298(rpb9) DDB_0216300(rpb12)
                 DDB_0216301(rpa49) DDB_0216313(rpc2) DDB_0216314(rpc3)
                 DDB_0216315(rpc34) DDB_0216317(rpc11)
            PFA: MAL13P1.213 MAL1P2.30 MAL3P1.13 MAL3P6.20 PF07_0027 PF10_0269
                 PF11_0058 PF11_0264 PF11_0358 PF11_0445 PF13_0023 PF13_0040
                 PF13_0150 PF13_0341 PF14_0150 PF14_0207 PF14_0695 PFB0245c
                 PFB0290c PFB0715w PFE0465c PFI1130c PFL0330c PFL0665c
            CPV: cgd1_1960 cgd1_2260 cgd1_2710 cgd1_2770 cgd2_980 cgd3_1870
                 cgd3_2620 cgd3_4320 cgd6_3290 cgd6_4580 cgd7_3720 cgd7_4770
                 cgd7_510 cgd8_170 cgd8_300
            CHO: Chro.10225 Chro.10257 Chro.10306 Chro.10312 Chro.20109
                 Chro.30221 Chro.30301 Chro.60382 Chro.60525 Chro.70415
                 Chro.70529 Chro.80042
            TAN: TA02635 TA02970 TA03235 TA03310 TA05785 TA07900 TA07925
                 TA08570 TA08625 TA08895 TA10195 TA10710 TA11880 TA12655
                 TA12735 TA14965 TA16240 TA18040 TA18990 TA19500 TA19535
                 TA19735
            TPV: TP01_0029 TP01_0225 TP01_0233 TP01_0652 TP01_0809 TP01_0975
                 TP02_0205 TP02_0237 TP02_0359 TP02_0766 TP03_0016 TP03_0027
                 TP03_0185 TP03_0199 TP03_0746 TP04_0334 TP04_0340 TP04_0471
                 TP04_0529 TP04_0648 TP04_0911 TP05_0028 TP05_0029 TP05_0042
                 TP05_0043
            TET: TTHERM_00011760 TTHERM_00037340 TTHERM_00047550
                 TTHERM_00077230 TTHERM_00085650 TTHERM_00094210
                 TTHERM_00370920 TTHERM_00421170 TTHERM_00444250
                 TTHERM_00446180 TTHERM_00475220 TTHERM_00485990
                 TTHERM_00522180 TTHERM_00538940 TTHERM_00549610
                 TTHERM_00809150 TTHERM_00888020 TTHERM_00941450
                 TTHERM_00989510 TTHERM_01016100 TTHERM_01075780
                 TTHERM_01076830 TTHERM_01119540 TTHERM_01680240
            TBR: Tb10.389.0110 Tb10.61.1360 Tb10.70.4870 Tb11.01.0625
                 Tb11.02.5180 Tb11.02.5790 Tb11.03.0450 Tb11.03.0935
                 Tb11.57.0004 Tb927.1.540 Tb927.3.1250 Tb927.3.5500
                 Tb927.4.3490 Tb927.4.3510 Tb927.4.3810 Tb927.4.5020
                 Tb927.8.5090 Tb927.8.7400
            TCR: 503821.10 504105.30 505997.210 506199.5 506203.129 506357.90
                 506779.60 506871.80 506925.40 506933.80 507159.44 507159.65
                 507159.90 507467.94 507485.15 507485.34 507673.65 508355.104
                 508409.30 509011.20 509453.40 509683.24 510029.40 511381.40
                 511417.40
            LMA: LmjF13.1120 LmjF16.1350 LmjF18.0780 LmjF19.0420 LmjF20.0010
                 LmjF25.0620 LmjF27.1550 LmjF28.0120 LmjF28.0810 LmjF29.0140
                 LmjF31.0160 LmjF31.2610 LmjF34.0360 LmjF34.0890
            EHI: 10.t00022 114.t00006 121.t00002 147.t00005 162.t00003
                 169.t00023 200.t00008 24.t00027 27.t00035 3.t00003 310.t00009
                 344.t00001 406.t00002 41.t00010 41.t00044 428.t00008 51.t00031
                 59.t00015 59.t00027 64.t00037 7.t00016 73.t00023 81.t00015
            ECO: b3295(rpoA) b3649(rpoZ) b3987(rpoB) b3988(rpoC)
            ECJ: JW3257(rpoA) JW3624(rpoZ) JW3950(rpoB) JW3951(rpoC)
            ECE: Z4665(rpoA) Z5075(rpoZ) Z5560(rpoB) Z5561(rpoC)
            ECS: ECs4160 ECs4524 ECs4910 ECs4911
            ECC: c4056(rpoA) c4474(rpoZ) c4944(rpoB) c4945(rpoC)
            ECI: UTI89_C3740(rpoA) UTI89_C3831(rpoC) UTI89_C3832(rpoB)
                 UTI89_C4194(rpoZ) UTI89_C4702(phnA)
            ECP: ECP_3383 ECP_3747 ECP_4200 ECP_4201
            ECV: APECO1_2485(rpoC) APECO1_2486(rpoB) APECO1_2812(rpoZ)
                 APECO1_3152(rpoA)
            ECW: EcE24377A_3778(rpoA) EcE24377A_4152(rpoZ)
                 EcE24377A_4528(rpoB) EcE24377A_4529(rpoC)
            ECX: EcHS_A3489(rpoA) EcHS_A3723 EcHS_A3860(rpoZ) EcHS_A4102
                 EcHS_A4220(rpoB) EcHS_A4221(rpoC) EcHS_A4286(zur)
            STY: STY3731(rpoC) STY3732(rpoB) STY4051(rpoZ) STY4383(rpoA)
            STT: t3473(rpoC) t3474(rpoB) t3777(rpoZ) t4090(rpoA)
            SPT: SPA3281(rpoA) SPA3593(rpoZ) SPA3991(rpoB) SPA3992(rpoC)
            SEC: SC3350(rpoA) SC3665(RPOZ) SC4037(rpoB) SC4038(rpoC)
            STM: STM3415(rpoA) STM3741(rpoZ) STM4153(rpoB) STM4154(rpoC)
            YPE: YPO0039(rpoZ) YPO0234(rpoA) YPO3746(rpoC) YPO3747(rpoB)
            YPK: y0102(rpoZ) y0484(rpoB) y0485(rpoC) y4015(rpoA)
            YPM: YP_0040(rpoZ) YP_0232(rpoA) YP_3109(rpoC) YP_3110(rpoB)
            YPA: YPA_3239 YPA_3503 YPA_3618 YPA_3619
            YPN: YPN_0219 YPN_0220 YPN_3811 YPN_3835
            YPP: YPDSF_0156 YPDSF_3744 YPDSF_3745 YPDSF_3866
            YPS: YPTB0036(rpoZ) YPTB0283(rpoB) YPTB0284(rpoC) YPTB3673(rpoA)
            YPI: YpsIP31758_0040(rpoZ) YpsIP31758_3859(rpoC)
                 YpsIP31758_3860(rpoB) YpsIP31758_3890(rpoA)
            YEN: YE0046(rpoZ) YE0286(groN) YE0287(rpoC)
            SFL: SF3327(rpoA) SF3689(rpoZ) SF4060(rpoB) SF4061(rpoC)
            SFX: S3674(rpoC) S3675(rpoB) S4080(rpoZ) S4435(rpoA)
            SFV: SFV_3315(rpoA) SFV_3880(rpoZ) SFV_4059(rpoB) SFV_4060(rpoC)
            SSN: SSON_3436(rpoA) SSON_3756(rpoZ) SSON_4160(rpoB)
                 SSON_4161(rpoC)
            SBO: SBO_3289(rpoA) SBO_3728(rpoZ) SBO_4007(rpoB) SBO_4008(rpoC)
            SDY: SDY_3471(rpoA) SDY_3740(rpoC) SDY_3741(rpoB) SDY_4081(rpoZ)
            ECA: ECA0039(rpoZ) ECA0223(rpoB) ECA0224(rpoC) ECA4006(rpoA)
            PLU: plu0273(rpoZ) plu0439(rpoB) plu0440(rpoC) plu4702(rpoA)
            BUC: BU033(rpoC) BU034(rpoB) BU499(rpoA)
            BAS: BUsg034(rpoC) BUsg035(rpoB) BUsg480(rpoA)
            BAB: bbp034(rpoC) bbp035(rpoB) bbp081(ytfN) bbp442(rpoA)
            BCC: BCc_016(rpoH) BCc_018(rpoC) BCc_019(rpoB) BCc_316(rpoA)
            WBR: WGLp405(rpoZ) WGLp522(rpoB) WGLp523(rpoC) WGLp568(rpoA)
            SGL: SG0134 SG0135 SG2222 SG2253
            ENT: Ent638_0090 Ent638_0197 Ent638_0198 Ent638_3726
            KPN: KPN_04365(rpoB)
            BFL: Bfl216(rpoA) Bfl556(rpoC) Bfl557(rpoB) Bfl617(rpoZ)
            BPN: BPEN_223(rpoA) BPEN_576(rpoC) BPEN_577(rpoB) BPEN_642(rpoZ)
            HIN: HI0514(rpoC) HI0515(rpoB) HI0802(rpoA) HI1742(rpoZ)
            HIT: NTHI0640(rpoC) NTHI0641(rpoB) NTHI0965(rpoA) NTHI2053(rpoZ)
            HIP: CGSHiEE_00425(rpoB) CGSHiEE_00430 CGSHiEE_03335(rpoZ)
                 CGSHiEE_08050
            HIQ: CGSHiGG_02455(rpoZ) CGSHiGG_05820 CGSHiGG_05825(rpoB)
                 CGSHiGG_07510
            HDU: HD1876(rpoC) HD1877(rpoB) HD1923(rpoZ) HD1951(rpoA)
            HSO: HS_0084(rpoA) HS_1456(rpoZ) HS_1564(rpoC) HS_1565(rpoB)
            PMU: PM0921(rpoZ) PM1390(rpoA) PM1736(rpoC) PM1737(rpoB)
            MSU: MS0212(rpoB) MS0213(rpoC) MS1737(rpoZ) MS2023(rpoA)
            APL: APL_1727(rpoB) APL_1728(rpoC) APL_1784(rpoA) APL_1826(rpoZ)
            XFA: XF1176 XF1502 XF2632 XF2633
            XFT: PD0461(rpoA) PD0719(rpoZ) PD2000(rpoC) PD2001(rpoB)
            XCC: XCC0888(rpoB) XCC0889(rpoC) XCC0919(rpoA) XCC3248(rpoZ)
            XCB: XC_0957 XC_3316 XC_3346 XC_3347
            XCV: XCV0991(rpoB) XCV0992(rpoC) XCV1023(rpoA) XCV3511(rpoZ)
            XAC: XAC0965(rpoB) XAC0966(rpoC) XAC0996(rpoA) XAC3394(rpoZ)
            XOO: XOO1148(rpoZ) XOO3558(rpoA) XOO3590(rpoC) XOO3591(rpoB)
            XOM: XOO_1045(XOO1045) XOO_3363(XOO3363) XOO_3393(XOO3393)
                 XOO_3394(XOO3394)
            VCH: VC0328 VC0329 VC2571 VC2709
            VCO: VC0395_A2149(rpoA) VC0395_A2281(rpoZ) VC0395_A2730(rpoB)
                 VC0395_A2731(rpoC)
            VVU: VV1_0736 VV1_0851 VV1_1211 VV1_1212
            VVY: VV0242 VV0399 VV3158 VV3159
            VPA: VP0160 VP0282 VP2921 VP2922
            VFI: VF0105 VF0262 VF2411 VF2412 VF2413 VF2414
            PPR: PBPRA0190 PBPRA0345 PBPRA3431 PBPRA3432
            PAE: PA4238(rpoA) PA4269(rpoC) PA4270(rpoB) PA5337(rpoZ)
            PAU: PA14_08760(rpoB) PA14_08780(rpoC) PA14_09115(rpoA)
                 PA14_70450(rpoZ)
            PAP: PSPA7_0830(rpoB) PSPA7_0831(rpoC) PSPA7_0862(rpoA)
                 PSPA7_6113(rpoZ)
            PPU: PP_0447(rpoB) PP_0448(rpoC) PP_0479(rpoA) PP_5301(rpoZ)
            PST: PSPTO_0074(rpoZ) PSPTO_0619(rpoB) PSPTO_0620(rpoC)
                 PSPTO_0651(rpoA)
            PSB: Psyr_0210 Psyr_4524 Psyr_4554 Psyr_4555
            PSP: PSPPH_0198(rpoZ) PSPPH_4567(rpoA) PSPPH_4598(rpoC)
                 PSPPH_4599(rpoB)
            PFL: PFL_5558 PFL_5588(rpoC) PFL_5589(rpoB) PFL_6062(rpoZ)
            PFO: Pfl_5055 Pfl_5085 Pfl_5086 Pfl_5550
            PEN: PSEEN0482(rpoB) PSEEN0483(rpoC) PSEEN0514(rpoA)
                 PSEEN5446(rpoZ)
            PMY: Pmen_3916 Pmen_4389
            PAR: Psyc_0514(rpoA) Psyc_1724(rpoZ) Psyc_1886(rpoC)
                 Psyc_1887(rpoB)
            PCR: Pcryo_0509 Pcryo_2004 Pcryo_2176 Pcryo_2177
            ACI: ACIAD0307(rpoB) ACIAD0308(rpoC) ACIAD3194(rpoA)
                 ACIAD3325(rpoZ)
            ACB: A1S_0287 A1S_0288 A1S_3171
            SON: SO_0224(rpoB) SO_0225(rpoC) SO_0256(rpoA) SO_0360(rpoZ)
            SDN: Sden_0163 Sden_0164 Sden_0195 Sden_3434
            SFR: Sfri_0141 Sfri_0142 Sfri_0173 Sfri_0364
            SAZ: Sama_0206 Sama_0207 Sama_0238
            SBL: Sbal_4145 Sbal_4463 Sbal_4464
            SLO: Shew_0151 Shew_0152 Shew_0183
            SPC: Sputcn32_3734 Sputcn32_3765 Sputcn32_3766
            SHE: Shewmr4_0192 Shewmr4_0193 Shewmr4_0224 Shewmr4_3614
            SHM: Shewmr7_0187 Shewmr7_0188 Shewmr7_0219 Shewmr7_0329
            SHN: Shewana3_0192 Shewana3_0193 Shewana3_0224 Shewana3_3811
                 Shewana3_3939
            SHW: Sputw3181_0149 Sputw3181_0150 Sputw3181_0181
            ILO: IL0345(rpoB) IL0346(rpoC) IL1891(rpoA) IL2381(rpoZ)
            CPS: CPS_0626(rpoA) CPS_4768(rpoC) CPS_4769(rpoB) CPS_4972(rpoZ)
            PHA: PSHAa0222(rpoB) PSHAa0223(rpoC) PSHAa2791(rpoZ)
                 PSHAa2806(rpoA)
            PAT: Patl_0348 Patl_0598 Patl_0599 Patl_1014
            SDE: Sde_0924 Sde_0925 Sde_0984 Sde_3696
            PIN: Ping_2614 Ping_3445 Ping_3446 Ping_3499
            MAQ: Maqu_0635 Maqu_0712 Maqu_0713 Maqu_0744
            CBU: CBU_0231(rpoB) CBU_0232(rpoC) CBU_0263(rpoA) CBU_0302(rpoZ)
            CBD: COXBU7E912_1779(rpoZ) COXBU7E912_1829(rpoA)
                 COXBU7E912_1860(rpoC) COXBU7E912_1862(rpoB)
            LPN: lpg0322(rpoB) lpg0323(rpoC) lpg0354(rpoA)
            LPF: lpl0362(rpoB) lpl0363(rpoC) lpl0395(rpoA) lpl1986(rpoZ)
            LPP: lpp0387(rpoB) lpp0388(rpoC) lpp0419(rpoA) lpp1991(rpoZ)
            MCA: MCA1066(rpoB) MCA1067(rpoC) MCA2022(rpoZ) MCA2347(rpoA)
            FTU: FTT0144(rpoB) FTT0145(rpoC) FTT0350(rpoA1) FTT0703(rpoZ)
                 FTT1442c(rpoA2)
            FTF: FTF0144(rpoB) FTF0145(rpoC) FTF0350(rpoA1) FTF0703(rpoZ)
                 FTF1442c(rpoA2)
            FTW: FTW_0234(rpoB) FTW_0235(rpoC) FTW_0446(rpoA1) FTW_1540(rpoZ)
                 FTW_1733(rpoA2)
            FTL: FTL_0261 FTL_0616 FTL_1533 FTL_1743 FTL_1744
            FTH: FTH_0256(rpoA1) FTH_0618(rpoA2) FTH_0840(rpoH) FTH_1483(rpoZ)
                 FTH_1682(rpoC) FTH_1683(rpoB)
            FTA: FTA_0275(rpoA1) FTA_0649(rpoA2) FTA_1617(rpoZ) FTA_1846
                 FTA_1847(rpoC) FTA_1848(rpoB)
            FTN: FTN_0264(rpoA) FTN_0613(rpoZ) FTN_1412 FTN_1567(rpoC)
                 FTN_1568(rpoB)
            TCX: Tcr_0288 Tcr_0289 Tcr_0319 Tcr_2143
            NOC: Noc_1213 Noc_2300 Noc_2330 Noc_2331
            AEH: Mlg_0451 Mlg_0452 Mlg_0483
            HHA: Hhal_0833 Hhal_0864 Hhal_0865 Hhal_0970
            HCH: HCH_06193(rpoA) HCH_06223(rpoC) HCH_06224(rpoB)
                 HCH_06314(rpoZ)
            CSA: Csal_0414 Csal_0415 Csal_0446 Csal_3234
            ABO: ABO_0177(rpoZ) ABO_0378(rpoB) ABO_0379(rpoC) ABO_0422(rpoA)
            AHA: AHA_0040(rpoZ) AHA_0333(rpoA) AHA_4027(rpoC) AHA_4028(rpoB)
            DNO: DNO_1021(rpoZ) DNO_1251(rpoA) DNO_1282(rpoB)
            BCI: BCI_0111(rpoZ) BCI_0353(rpoA) BCI_0502(rpoB) BCI_0503(rpoC)
            CRP: CRP_135 CRP_161 CRP_162
            RMA: Rmag_0190 Rmag_0405 Rmag_0810 Rmag_0811
            VOK: COSY_0194(rpoA) COSY_0376(rpoZ) COSY_0735(rpoC)
                 COSY_0736(rpoB)
            NME: NMB0132 NMB0133 NMB0168 NMB1660
            NMA: NMA0103(rpoA) NMA0141(rpoC) NMA0142(rpoB) NMA1918(rpoZ)
            NMC: NMC0123(rpoB) NMC0124(rpoC) NMC0158(rpoA) NMC1578(rpoZ)
            NGO: NGO1309(rpoZ) NGO1818(rpoA) NGO1850 NGO1851
            CVI: CV_3769(rpoZ) CV_4160(rpoA) CV_4192(rpoC) CV_4193(rpoB)
            RSO: RSc2154(rpoZ) RSc2993(rpoA) RSc3033(rpoC) RSc3034(rpoB)
            REU: Reut_A2472 Reut_A3154 Reut_A3188 Reut_A3189
            REH: H16_A0354(rpoH) H16_A0387(rpoN) H16_A0954(rpoZ)
                 H16_A1034(rpoE2) H16_A1096(rpoE3) H16_A1626(rpoD1)
                 H16_A2373(rpoS) H16_A2563(rpoE1) H16_A2725(rpoD1)
                 H16_A2923(rpoE4) H16_A3447(rpoE5) H16_A3458(rpoA)
                 H16_A3496(rpoC) H16_A3497(rpoB) H16_B0256(fliA)
                 H16_B1727(prtI) H16_B2413(rpoE6)
            RME: Rmet_0857 Rmet_3291 Rmet_3333 Rmet_3334
            BMA: BMA2095(rpoZ) BMA2606(rpoA) BMA2640(rpoC)
            BMV: BMASAVP1_A0816(rpoZ) BMASAVP1_A3143(rpoA)
                 BMASAVP1_A3177(rpoC) BMASAVP1_A3178(rpoB)
            BML: BMA10299_A1914(rpoB) BMA10299_A1915(rpoC)
                 BMA10299_A1950(rpoA) BMA10299_A2649(rpoZ)
            BMN: BMA10247_1963(rpoZ) BMA10247_3469(rpoB) BMA10247_3470(rpoC)
                 BMA10247_3504(rpoA)
            BXE: Bxe_A0306 Bxe_A0307 Bxe_A0340 Bxe_A0906
            BVI: Bcep1808_0322 Bcep1808_0323 Bcep1808_0356 Bcep1808_0917
            BUR: Bcep18194_A3439 Bcep18194_A3440 Bcep18194_A3473
                 Bcep18194_A4108
            BCN: Bcen_0521 Bcen_2733 Bcen_2766 Bcen_2767
            BCH: Bcen2424_0340 Bcen2424_0341 Bcen2424_0374 Bcen2424_1000
            BAM: Bamb_0259 Bamb_0260 Bamb_0293 Bamb_0860
            BPS: BPSL2562(rpoZ) BPSL3187(rpoA) BPSL3220(rpoC) BPSL3221
            BPM: BURPS1710b_1652 BURPS1710b_2228 BURPS1710b_3048(rpoZ)
                 BURPS1710b_3750(rpoA) BURPS1710b_3785(rpoC)
                 BURPS1710b_3786(rpoB)
            BPL: BURPS1106A_3014(rpoZ) BURPS1106A_3778(rpoA)
                 BURPS1106A_3815(rpoC) BURPS1106A_3816(rpoB)
            BPD: BURPS668_2948(rpoZ) BURPS668_3720(rpoA) BURPS668_3753(rpoC)
                 BURPS668_3754(rpoB)
            BTE: BTH_I1587(rpoZ) BTH_I3042(rpoA) BTH_I3075(rpoC)
                 BTH_I3076(rpoB)
            PNU: Pnuc_0046 Pnuc_0047 Pnuc_0078 Pnuc_1077
            BPE: BP0015(rpoB) BP0016(rpoC) BP1577(rpoZ) BP3642(rpoA)
            BPA: BPP0014(rpoB) BPP0015(rpoC) BPP0057(rpoA) BPP3006(rpoZ)
            BBR: BB0014(rpoB) BB0015(rpoC) BB0057(rpoA) BB2972(rpoZ)
            RFR: Rfer_3148 Rfer_3591 Rfer_3592 Rfer_4217
            POL: Bpro_0501 Bpro_1334 Bpro_4441 Bpro_4442
            PNA: Pnap_0345 Pnap_0810 Pnap_3639 Pnap_3640
            AAV: Aave_0626 Aave_3584 Aave_4530 Aave_4531
            AJS: Ajs_0406 Ajs_3896 Ajs_3897
            VEI: Veis_2264 Veis_2265 Veis_2301
            MPT: Mpe_A2716 Mpe_A3417 Mpe_A3450 Mpe_A3451
            HAR: HEAR2131 HEAR3141(rpoA) HEAR3172(rpoC) HEAR3173(rpoB)
            MMS: mma_1327(rpoZ) mma_3385(rpoA) mma_3419(rpoC) mma_3420(rpoB)
            NEU: NE0426(rpoA) NE2045(rpoC) NE2046(rpoB) NE2255(rpoZ)
            NET: Neut_0583 Neut_0613 Neut_1794 Neut_1795
            NMU: Nmul_A0051 Nmul_A0759 Nmul_A0760 Nmul_A0792
            EBA: ebA3495(rpoZ) ebA3818(rpoB) ebA3819(rpoC) ebA3853(rpoA)
                 ebA4367(dnaG)
            AZO: azo3391(rpoA) azo3423(rpoC) azo3424(rpoB) azo3952(rpoZ)
            DAR: Daro_0312 Daro_0313 Daro_0345 Daro_3844
            TBD: Tbd_0398 Tbd_0399 Tbd_0430 Tbd_0472
            MFA: Mfla_0049 Mfla_0272 Mfla_0273 Mfla_0304
            HPY: HP0776 HP1198(rpoB) HP1293(rpoA)
            HPJ: jhp0713 jhp1121(rpoB) jhp1213(rpoA)
            HPA: HPAG1_0089 HPAG1_0761 HPAG1_1137 HPAG1_1238
            HHE: HH0361(rpoB) HH0832(rpoZ) HH1403(rpoA)
            HAC: Hac_0160(rpoA) Hac_0637(rpoZ) Hac_1578(rpoB)
            WSU: WS0239 WS0467(rpoB) WS1692(rpoA)
            TDN: Tmden_0327 Tmden_0353 Tmden_0354 Tmden_0718
            CJE: Cj0478(rpoB) Cj0479(rpoC) Cj1273c(rpoZ) Cj1595(rpoA)
            CJR: CJE0528(rpoB) CJE0529(rpoC) CJE1409(rpoZ) CJE1767(rpoA)
            CJJ: CJJ81176_0509(rpoB) CJJ81176_0510(rpoC) CJJ81176_1289(rpoZ)
                 CJJ81176_1582(rpoA)
            CJU: C8J_0451(rpoB) C8J_0452(rpoC) C8J_1217(rpoZ) C8J_1497(rpoA)
            CJD: JJD26997_0452(rpoZ) JJD26997_1948(rpoA)
            CFF: CFF8240_0059(rpoA) CFF8240_1213(rpoZ) CFF8240_1314(rpoC)
                 CFF8240_1316(rpoB)
            CCV: CCV52592_0482(rpoZ) CCV52592_1008(rpoA)
            CHA: CHAB381_0205(rpoA) CHAB381_1282(rpoZ)
            CCO: CCC13826_0175(rpoC) CCC13826_0257 CCC13826_0501(rpoZ)
                 CCC13826_1196 CCC13826_1197 CCC13826_1751(rpoA)
            ABU: Abu_0646(rpoZ) Abu_1020(rpoA) Abu_1883(rpoC) Abu_1884(rpoB)
            NIS: NIS_0249(rpoA) NIS_0268(rpoB) NIS_0269(rpoC) NIS_0759
            SUN: SUN_0131(rpoB) SUN_0132(rpoC) SUN_1746 SUN_2347(rpoA)
            GSU: GSU2237(rpoZ) GSU2831(rpoA) GSU2863(rpoB)
            GME: Gmet_0619 Gmet_0620 Gmet_0653 Gmet_2326
            PCA: Pcar_0694 Pcar_0695 Pcar_0728 Pcar_1286
            PPD: Ppro_0673 Ppro_0674 Ppro_0706 Ppro_2400
            DVU: DVU1329(rpoA) DVU2928(rpoB) DVU2929(rpoC) DVU3242(rpoZ)
            DVL: Dvul_0438 Dvul_0439 Dvul_1739
            DDE: Dde_0247 Dde_2231 Dde_2997 Dde_2998
            LIP: LI0904(rpoB) LI0905(rpoB) LI0982(rpoA)
            BBA: Bd1569(rnpO) Bd2950(rpoA) Bd2983(rpoC) Bd2984(rpoB)
            DPS: DP1117 DP1118 DP1152 DP1481
            ADE: Adeh_1592 Adeh_1593 Adeh_1919 Adeh_3590
            MXA: MXAN_3077(rpoB) MXAN_3078(rpoC) MXAN_3326(rpoA)
                 MXAN_4890(rpoZ)
            SAT: SYN_00063 SYN_00064 SYN_01280 SYN_01601
            SFU: Sfum_1549 Sfum_1550 Sfum_1582 Sfum_1758
            RPR: RP140(rpoB) RP141(rpoC) RP578 RP635(rpoA)
            RTY: RT0129(rpoB) RT0130(rpoC) RT0567(rpoZ) RT0627(rpoA)
            RCO: RC0181(rpoB) RC0182(rpoC) RC0882(rpoZ) RC0982(rpoA)
            RFE: RF_0302(rpoA) RF_0944(rpoZ) RF_1145(rpoC) RF_1146(rpoB)
            RBE: RBE_0993(rpoZ) RBE_1038(rpoA) RBE_1152(rpoC) RBE_1153(rpoB)
            RAK: A1C_01010(rpoB) A1C_01015 A1C_04500(rpoZ) A1C_04985
            RBO: A1I_01515(rpoB) A1I_01520 A1I_02160 A1I_03690(rpoZ)
            RCM: A1E_00715(rpoB) A1E_00725 A1E_04250
            RRI: A1G_01035(rpoB) A1G_01040 A1G_04870(rpoZ) A1G_05435
            OTS: OTBS_0207(rpoC) OTBS_0208(rpoB) OTBS_0353(rpoA)
            WOL: WD0024(rpoBC) WD0658(rpoA) WD1303(rpoZ)
            WBM: Wbm0318(rpoA) Wbm0387(rpoZ) Wbm0647
            AMA: AM262(rpoB) AM263(rpoC) AM442(rpoZ) AM631(rpoH) AM887(rpoA)
            APH: APH_0303(rpoA) APH_0514(rpoZ) APH_1023(rpoC) APH_1024(rpoB)
            ERU: Erum1720(rpoB) Erum1730(rpoC) Erum2990(rpoZ) Erum5850(rpoA)
            ERW: ERWE_CDS_01710(rpoB) ERWE_CDS_01720(rpoC)
                 ERWE_CDS_03050(rpoZ) ERWE_CDS_06150(rpoA)
            ERG: ERGA_CDS_01650(rpoB) ERGA_CDS_01660(rpoC)
                 ERGA_CDS_02990(rpoZ) ERGA_CDS_06060(rpoA)
            ECN: Ecaj_0169 Ecaj_0170 Ecaj_0280 Ecaj_0589
            ECH: ECH_0432(rpoA) ECH_0796(rpoZ) ECH_0951(rpoC) ECH_0952(rpoB)
            NSE: NSE_0039(rpoZ) NSE_0289(rpoA) NSE_0677(rpoC) NSE_0678(rpoB)
            PUB: SAR11_1093(rpoA) SAR11_1122(rpoC) SAR11_1123(rpoB)
                 SAR11_1194(rpoZ)
            MLO: mlr0276 mlr0277 mlr0325 mlr7753
            MES: Meso_0945 Meso_1654 Meso_1818 Meso_1819
            SME: SMc01285(rpoA) SMc01316(rpoC) SMc01317(rpoB) SMc02408(rpoZ)
            ATU: Atu1029(rnpO) Atu1923(rpoA) Atu1955(rpoC) Atu1956(rpoB)
            ATC: AGR_C_1894 AGR_C_3518 AGR_C_3568 AGR_C_3569
            RET: RHE_CH01384(rpoZ) RHE_CH01667(rpoB) RHE_CH01668(rpoC)
                 RHE_CH01699(rpoA)
            RLE: RL1505 RL1766(rpoB) RL1767(rpoC) RL1798(rpoA)
            BME: BMEI0749 BMEI0750 BMEI0781 BMEI1297
            BMF: BAB1_0671 BAB1_1231(rpoA) BAB1_1263(rpoC) BAB1_1264
            BMS: BR0651(rpoZ) BR1209(rpoA) BR1242(rpoC) BR1243(rpoB)
            BMB: BruAb1_0668(rpoZ) BruAb1_1214(rpoA) BruAb1_1247(rpoC)
                 BruAb1_1248(rpoB)
            BOV: BOV_0644 BOV_1172(rpoA) BOV_1204(rpoC) BOV_1205(rpoB)
            BJA: bll5066(rnpO) bll5376(rpoA) bll5409(rpoC) bll5410(rpoB)
            BRA: BRADO3054(rpoB) BRADO3055(rpoC) BRADO3090(rpoA)
                 BRADO4469(rpoZ)
            BBT: BBta_4688 BBta_5046(rpoA) BBta_5080(rpoC) BBta_5081(rpoB)
            RPA: RPA2527 RPA2692(rnpO) RPA3226(rpoA) RPA3267(rpoC)
                 RPA3268(rpoB)
            RPB: RPB_2285 RPB_2286 RPB_2319 RPB_2607
            RPC: RPC_2634 RPC_3424 RPC_3457 RPC_3458
            RPD: RPD_2646 RPD_3160 RPD_3194 RPD_3195
            RPE: RPE_3027 RPE_3562 RPE_3596 RPE_3597
            NWI: Nwi_1350 Nwi_1351 Nwi_1388 Nwi_1923
            NHA: Nham_1531 Nham_1532 Nham_1569 Nham_2256
            BHE: BH05030(rpoZ) BH06100(rpoB) BH06110(rpoC) BH10270(rpoA)
            BQU: BQ04220(rpoZ) BQ07120(rpoC) BQ07130(rpoB) BQ07990(rpoA)
            BBK: BARBAKC583_0467(rpoZ) BARBAKC583_0571(rpoB)
                 BARBAKC583_0572(rpoC) BARBAKC583_0722(rpoA)
            CCR: CC_0502 CC_0503 CC_1272 CC_1552
            SIL: SPO0511(rpoA) SPO3204(rpoZ) SPO3507(rpoC) SPO3508(rpoB)
            SIT: TM1040_0234 TM1040_0235 TM1040_0279 TM1040_2566
            RSP: RSP_1669(rpoZ) RSP_1699(rpoB) RSP_1712(rpoC) RSP_1739(rpoA)
            RSH: Rsph17029_0302 Rsph17029_0339 Rsph17029_0340 Rsph17029_0353
                 Rsph17029_0354 Rsph17029_0385
            JAN: Jann_0513 Jann_0568 Jann_0569 Jann_0617
            RDE: RD1_1358(rpoZ) RD1_1437(rpoA) RD1_1924(dnaE2) RD1_4018(rpoC)
                 RD1_4019(rpoB)
            PDE: Pden_0747 Pden_0749 Pden_0784 Pden_1401
            MMR: Mmar10_1576 Mmar10_1771 Mmar10_1801 Mmar10_1802
            HNE: HNE_0872(rpoZ) HNE_2827(rpoA) HNE_2857(rpoC) HNE_2858(rpoB)
            ZMO: ZMO0541(rpoA) ZMO0731 ZMO0732 ZMO1720
            NAR: Saro_0023 Saro_0024 Saro_0141 Saro_2527
            SAL: Sala_0565 Sala_1485 Sala_1486 Sala_1602
            ELI: ELI_08060 ELI_10980 ELI_14460 ELI_14470
            GOX: GOX0356 GOX0385 GOX0386
            GBE: GbCGDNIH1_0548 GbCGDNIH1_0549 GbCGDNIH1_0578 GbCGDNIH1_0988
            RRU: Rru_A1857 Rru_A2664 Rru_A2694 Rru_A2695
            MAG: amb2252 amb3108 amb3139 amb3140
            MGM: Mmc1_0252 Mmc1_0840 Mmc1_0841 Mmc1_0872
            ABA: Acid345_1255 Acid345_3777 Acid345_4675 Acid345_4676
            SUS: Acid_5090 Acid_5456 Acid_5457
            BSU: BG10409(rpoE) BG10728(rpoB) BG10729(rpoC) BG10732(rpoA)
                 BG13387(yloH)
            BHA: BH0126(rpoB) BH0127(rpoC) BH0162(rpoA) BH2511 BH3793(rpoE)
            BAN: BA0102(rpoB) BA0103(rpoC) BA0137(rpoA) BA4008(rpoZ)
                 BA5584(rpoE)
            BAR: GBAA0102(rpoB) GBAA0103(rpoC) GBAA0137(rpoA) GBAA4008(rpoZ)
                 GBAA5584(rpoE)
            BAA: BA_0440 BA_0689 BA_0690 BA_0719 BA_4479
            BAT: BAS0102 BAS0103 BAS0137 BAS3721 BAS5188
            BCE: BC0122 BC0123 BC0158 BC3868 BC5339
            BCA: BCE_0102(rpoB) BCE_0103(rpoC) BCE_0137(rpoA) BCE_5470(rpoE)
            BCZ: BCZK0096(rpoB) BCZK0097(rpoC) BCZK0130(rpoA) BCZK3297
                 BCZK3629(rpoZ) BCZK5039(rpoE)
            BTK: BT9727_0098(rpoB) BT9727_0099(rpoC) BT9727_0132(rpoA)
                 BT9727_3611(rpoZ) BT9727_5023(rpoE)
            BTL: BALH_0100(rpoB) BALH_0101(rpoC) BALH_0134(rpoA)
                 BALH_3229(sigW) BALH_3501 BALH_4837(rpoE)
            BLI: BL01025(rpoA) BL02294(rpoZ) BL02626(rpoC) BL02798(rpoB)
                 BL05358(rpoE)
            BLD: BLi00125(rpoB) BLi00126(rpoC) BLi00161(rpoA) BLi01790(yloH)
                 BLi03964(rpoE)
            BCL: ABC0142(rpoB) ABC0143(rpoC) ABC0177(rpoA) ABC2321
                 ABC3887(rpoE)
            BAY: RBAM_001320(rpoB) RBAM_001330(rpoC) RBAM_001680(rpoA)
                 RBAM_015520(rpoZ) RBAM_034320(rpoE)
            BPU: BPUM_0093(rpoB) BPUM_0094(rpoC) BPUM_0130(rpoA)
                 BPUM_0902(sigM) BPUM_1468(rpoZ)
            OIH: OB0112(rpoB) OB0113(rpoC) OB0145(rpoA) OB1503 OB3008(rpoE)
            GKA: GK0098(rpoB) GK0099(rpoC) GK0133(rpoA) GK1168 GK3390
            GTN: GTNG_0098 GTNG_0099 GTNG_0131 GTNG_3335
            SAU: SA0500(rpoB) SA0501(rpoC) SA1053 SA1930(rpoE) SA2023(rpoA)
            SAV: SAV0542(rpoB) SAV0543(rpoC) SAV1210 SAV2128(rpoE)
                 SAV2224(rpoA)
            SAM: MW0497(rpoB) MW0498(rpoC) MW1093 MW2052(rpoE) MW2143(rpoA)
            SAR: SAR0547(rpoB) SAR0548(rpoC) SAR1186 SAR2216(rpoE)
                 SAR2309(rpoA)
            SAS: SAS0500 SAS0501 SAS1144 SAS2031 SAS2115
            SAC: SACOL0588(rpoB) SACOL0589(rpoC) SACOL1222(rpoZ)
                 SACOL2120(rpoE) SACOL2213(rpoA)
            SAB: SAB0493(rpoB) SAB0494(rpoC) SAB1074 SAB2012c(rpoE)
                 SAB2097c(rpoA)
            SAA: SAUSA300_0527(rpoB) SAUSA300_0528(rpoC) SAUSA300_1103(rpoZ)
                 SAUSA300_2082(rpoE) SAUSA300_2178(rpoA)
            SAO: SAOUHSC_00524 SAOUHSC_00525 SAOUHSC_01177 SAOUHSC_02369
                 SAOUHSC_02485
            SEP: SE0306 SE0307 SE0886 SE1726 SE1797
            SER: SERP0183(rpoB) SERP0184(rpoC) SERP0777(rpoZ) SERP1735(rpoE)
                 SERP1805(rpoA)
            SHA: SH0828(rpoA) SH0907(rpoE) SH1704 SH2464(rpoC) SH2465(rpoB)
            SSP: SSP0689 SSP0757 SSP1561 SSP2212 SSP2213
            LMO: lmo0258(rpoB) lmo0259(rpoC) lmo1826 lmo2560 lmo2606(rpoA)
            LMF: LMOf2365_0274(rpoB) LMOf2365_0275(rpoC) LMOf2365_1854(rpoZ)
                 LMOf2365_2532(rpoE) LMOf2365_2579(rpoA)
            LIN: lin0285(rpoB) lin0286(rpoC) lin1940 lin2705 lin2755(rpoA)
            LWE: lwe0227(rpoB) lwe0228(rpoC) lwe1845(rpoZ) lwe2510(rpoE)
                 lwe2556(rpoA)
            LLA: L0136(rpoA) L0137(rpoB) L0138(rpoC) L0141(rpoE) L149295(ytgE)
            LLC: LACR_0658 LACR_1980 LACR_1981 LACR_2157 LACR_2375
            LLM: llmg_0608(rpoE) llmg_1981(rpoC) llmg_1982(rpoB)
                 llmg_2154(rpoZ) llmg_2354(rpoA)
            SPY: SPy_0080(rpoA) SPy_0098(rpoB) SPy_0099(rpoC) SPy_1630
                 SPy_1895(rpoE)
            SPZ: M5005_Spy_0070(rpoA) M5005_Spy_0083(rpoB)
                 M5005_Spy_0084(rpoC) M5005_Spy_1340 M5005_Spy_1611(rpoE)
            SPM: spyM18_0079(rpoA) spyM18_0099(ropB) spyM18_0100(ropC)
                 spyM18_1640 spyM18_1960(rpoE)
            SPG: SpyM3_0066(rpoA) SpyM3_0075(rpoB) SpyM3_0076(rpoC) SpyM3_1374
                 SpyM3_1633(rpoE)
            SPS: SPs0068 SPs0076 SPs0077 SPs0233 SPs0488
            SPH: MGAS10270_Spy0073(rpoA) MGAS10270_Spy0085(rpoB)
                 MGAS10270_Spy0086(rpoC) MGAS10270_Spy1456
                 MGAS10270_Spy1679(rpoE)
            SPI: MGAS10750_Spy0074(rpoA) MGAS10750_Spy0090(rpoB)
                 MGAS10750_Spy0091(rpoC) MGAS10750_Spy1449
                 MGAS10750_Spy1666(rpoE)
            SPJ: MGAS2096_Spy0073(rpoA) MGAS2096_Spy0086(rpoB)
                 MGAS2096_Spy0087(rpoC) MGAS2096_Spy1361 MGAS2096_Spy1634(rpoE)
            SPK: MGAS9429_Spy0070(rpoA) MGAS9429_Spy0083(rpoB)
                 MGAS9429_Spy0084 MGAS9429_Spy0085(rpoC) MGAS9429_Spy1335
                 MGAS9429_Spy1614(rpoE)
            SPF: SpyM50069(rpoA) SpyM50081(rpoB) SpyM50082(rpoC)
                 SpyM50243(rpoE) SpyM50451(rpoZ)
            SPA: M6_Spy0119 M6_Spy0131 M6_Spy0132 M6_Spy1386 M6_Spy1619
            SPB: M28_Spy0069(rpoA) M28_Spy0081(rpoB) M28_Spy0082(rpoC)
                 M28_Spy1381 M28_Spy1600(rpoE)
            SPN: SP_0236 SP_0493 SP_1737 SP_1960 SP_1961
            SPR: spr0215(rpoA) spr0437(rpoE) spr1582 spr1776(rpoC)
                 spr1777(rpoB)
            SPD: SPD_0218(rpoA) SPD_0441 SPD_1547 SPD_1758(rpoC)
                 SPD_1759(rpoB)
            SAG: SAG0084(rpoA) SAG0106 SAG0160(rpoB) SAG0161(rpoC) SAG0314
            SAN: gbs0084(rpoA) gbs0105 gbs0156(rpoB) gbs0157(rpoC) gbs0302
            SAK: SAK_0116(rpoA) SAK_0156(rpoE) SAK_0223(rpoB) SAK_0224(rpoC)
                 SAK_0384(rpoZ)
            SMU: SMU.1989(rpoC) SMU.1990(rpoB) SMU.2001(rpoA) SMU.479(rpoZ)
                 SMU.96(rpoE)
            STC: str0133(rpoE) str1430(rpoZ) str1867(rpoC) str1868(rpoB)
                 str1908(rpoA)
            STL: stu0133(rpoE) stu1430(rpoZ) stu1867(rpoC) stu1868(rpoB)
                 stu1908(rpoA)
            STE: STER_0192 STER_1844 STER_1845 STER_1881
            SSA: SSA_0132(rpoA) SSA_0176(rpoB) SSA_0177(rpoC) SSA_1850(rpoZ)
                 SSA_1996(rpoE)
            SSU: SSU05_0095 SSU05_0121 SSU05_0122 SSU05_0334
            SSV: SSU98_0097 SSU98_0122 SSU98_0123 SSU98_0328
            SGO: SGO_0413 SGO_0595 SGO_1926(rpoC) SGO_1927(rpoB)
                 SGO_1959(rpoA)
            LPL: lp_0480(rpoE) lp_1021(rpoB) lp_1022(rpoC) lp_1062(rpoA)
                 lp_1613(rpoZ)
            LJO: LJ0223 LJ0332 LJ0333 LJ0361 LJ1542
            LAC: LBA0232 LBA0284 LBA0285 LBA0317 LBA1324(rpoZ)
            LSA: LSA0686(rpoZ) LSA1631(rpoE) LSA1739(rpoA) LSA1774(rpoC)
                 LSA1775(rpoB)
            LSL: LSL_0197(rpoB) LSL_0198(rpoC) LSL_0341(rpoE) LSL_0612
                 LSL_1409(rpoA)
            LDB: Ldb0353(rpoE) Ldb0386(rpoB) Ldb0387(rpoC) Ldb0422(rpoA)
                 Ldb1414(rpoZ)
            LBU: LBUL_0308 LBUL_0342 LBUL_0343 LBUL_0376 LBUL_1311
            LBR: LVIS_0486 LVIS_0968 LVIS_1664 LVIS_1697 LVIS_1698
            LCA: LSEI_1628 LSEI_2477 LSEI_2515 LSEI_2516 LSEI_2573
            LGA: LGAS_0225 LGAS_0284 LGAS_0285 LGAS_0316 LGAS_0759
            LRE: Lreu_1175
            PPE: PEPE_0826 PEPE_1392 PEPE_1425 PEPE_1426 PEPE_1572
            EFA: EF0233(rpoA) EF1146 EF3126(rpoZ) EF3237(rpoC) EF3238(rpoB)
            OOE: OEOE_0620 OEOE_1230 OEOE_1374 OEOE_1375 OEOE_1788
            LME: LEUM_0221 LEUM_0513 LEUM_1712 LEUM_1824 LEUM_1825
            STH: STH1340(rpoZ) STH3047(rpoA) STH3084(rpoC) STH3085(rpoB)
                 STH39(rpoE)
            CAC: CAC1719(rpoZ) CAC3104(rpoA) CAC3142(rpoC) CAC3143(rpoB)
            CPE: CPE1747(rpoZ) CPE2376(rpoA) CPE2412(rpoC) CPE2413(rpoB)
            CPF: CPF_2000(rpoZ) CPF_2685(rpoA) CPF_2721(rpoC) CPF_2722(rpoB)
            CPR: CPR_1718(rpoZ) CPR_2370(rpoA) CPR_2407(rpoC) CPR_2408(rpoB)
            CTC: CTC02578 CTC02608 CTC02609
            CNO: NT01CX_1107(rpoB) NT01CX_1108(rpoC) NT01CX_1144(rpoA)
                 NT01CX_2248(rpoZ)
            CTH: Cthe_2724 Cthe_2725 Cthe_2932
            CDF: CD0066(rpoB) CD0067(rpoC) CD0098(rpoA) CD2587A(rpoZ)
            CBO: CBO3452(rpoA) CBO3487(rpoC) CBO3488(rpoB)
            CBA: CLB_2386(rpoZ) CLB_3508(rpoA) CLB_3544(rpoC) CLB_3545(rpoB)
            CBH: CLC_2368(rpoZ) CLC_3396(rpoA) CLC_3432(rpoC) CLC_3433(rpoB)
            CBF: CLI_2574(rpoZ) CLI_3634(rpoA) CLI_3670(rpoC) CLI_3671(rpoB)
            CKL: CKL_0216(rpoB) CKL_0217(rpoC) CKL_0252(rpoA) CKL_1366
            CHY: CHY_1487(rpoZ) CHY_2281(rpoA) CHY_2317(rpoC) CHY_2318(rpoB)
            DSY: DSY0463 DSY0464 DSY0499 DSY2728 DSY4945
            DRM: Dred_0207 Dred_0208 Dred_0243
            PTH: PTH_0312(rpoB) PTH_0313(rpoC) PTH_0349(rpoA)
            SWO: Swol_2304 Swol_2340 Swol_2341
            CSC: Csac_0951 Csac_0952 Csac_2259
            TTE: TTE1510(rpoZ) TTE2263(rpoA) TTE2300(rpoC) TTE2301(rpoB)
            MTA: Moth_0892 Moth_2431 Moth_2467 Moth_2468
            MGE: MG_022(rpoE) MG_177(rpoA) MG_340(rpoC) MG_341(rpoB)
            MPN: MPN024(rpoE) MPN191(rpoA) MPN515(rpoC) MPN516(rpoB)
            MPU: MYPU_5450(rpoC) MYPU_5460(rpoB) MYPU_5610(rpoA)
            MPE: MYPE10350(rpoE) MYPE790(rpoB) MYPE800(rpoC) MYPE9920(rpoA)
            MGA: MGA_0443(rpoA) MGA_0497(rpoE) MGA_1000(rpoB) MGA_1005(rpoC)
            MMY: MSC_0133 MSC_0721(rpoA) MSC_1008(rpoB) MSC_1009(rpoC)
            MMO: MMOB2610(rpoA) MMOB2810(rpoB) MMOB2820(rpoC)
            MHY: mhp213(rpoA) mhp635(rpoC) mhp636(rpoB)
            MHJ: MHJ_0164(rpoA) MHJ_0617(rpoC) MHJ_0618(rpoB)
            MHP: MHP7448_0168(rpoA) MHP7448_0616(rpoC) MHP7448_0617(rpoB)
            MSY: MS53_0484(rpoC) MS53_0485(rpoB) MS53_0574(rpoA)
            MCP: MCAP_0070(rpoB) MCAP_0071(rpoC) MCAP_0132 MCAP_0670(rpoA)
            UUR: UU187(rpoB) UU188(rpoC) UU257(rpoA) UU597(rpoE)
            POY: PAM227(rpoA) PAM260(rpoB) PAM261(rpoC)
            AYW: AYWB_460(rpoC) AYWB_461(rpoB) AYWB_495(rpoA) AYWB_654(rpoZ)
            MFL: Mfl150 Mfl597 Mfl598 Mfl649
            MTU: Rv0667(rpoB) Rv0668(rpoC) Rv1390(rpoZ) Rv3457c(rpoA)
            MTC: MT0695(rpoB) MT0696(rpoC) MT1435 MT3564(rpoA)
            MBO: Mb0686(rpoB) Mb0687(rpoC) Mb1425(rpoZ) Mb3486c(rpoA)
            MBB: BCG_0716(rpoB) BCG_0717(rpoC) BCG_1451(rpoZ) BCG_3522c(rpoA)
            MLE: ML0542 ML1890(rpoC) ML1891(rpoB) ML1957(rpoA)
            MPA: MAP1124 MAP4130(rpoB) MAP4131(rpoC) MAP4233(rpoA)
            MAV: MAV_3384 MAV_4398(rpoA) MAV_4502(rpoC) MAV_4503(rpoB)
            MSM: MSMEG_1367(rpoB) MSMEG_1368(rpoC) MSMEG_1524(rpoA)
                 MSMEG_3053(rpoZ)
            MVA: Mvan_1257 Mvan_1258 Mvan_1436
            MGI: Mflv_4970 Mflv_5096 Mflv_5097
            MMC: Mmcs_0969 Mmcs_0970 Mmcs_1113 Mmcs_2371
            MKM: Mkms_0987 Mkms_0988 Mkms_1130
            MJL: Mjls_0997 Mjls_0998 Mjls_1142
            CGL: NCgl0471(cgl0488) NCgl0472(cgl0489) NCgl0540(cgl0564)
                 NCgl1543(cgl1605)
            CGB: cg0576(rpoB) cg0577(rpoC) cg0655(rpoA) cg0738(dnaE2) cg1809
            CEF: CE0497 CE0498 CE0572 CE1725
            CDI: DIP0446(rpoB) DIP0447(rpoC) DIP0549(rpoA) DIP1327(rpoZ)
            CJK: jk1018(rpoZ) jk1758(rpoA) jk1845(rpoC) jk1846(rpoB)
            NFA: nfa36150(rpoZ) nfa46460(rpoB2) nfa50980(rpoC) nfa50990(rpoB)
                 nfa8370(rpoA)
            RHA: RHA1_ro01961(rpoC) RHA1_ro01962(rpoB) RHA1_ro06162(rpoA)
                 RHA1_ro07156(rpoZ)
            SCO: SCO1478(SC9C5.02c) SCO4654(rpoB) SCO4655(rpoC) SCO4729(rpoA)
            SMA: SAV440(rpoA2) SAV4914(rpoB) SAV4915(rpoC) SAV4953(rpoA)
                 SAV6872(rpoZ)
            TWH: TWT071(rpoB) TWT072(rpoC) TWT362(rpoZ) TWT528(rpoA)
            TWS: TW081(rpoB) TW082(rpoC) TW232(rpoA) TW407(rpoZ)
            LXX: Lxx11130(rpoZ) Lxx20080(rpoA) Lxx20630(rpoC) Lxx20640(rpoB)
            CMI: CMM_1779(rpoZ) CMM_2584(rpoA) CMM_2630(rpoC) CMM_2631(rpoB)
            ART: Arth_2940 Arth_2983 Arth_2984
            AAU: AAur_2261(rpoZ) AAur_2918(rpoA) AAur_2956(rpoC)
                 AAur_2957(rpoB)
            PAC: PPA1191 PPA1826 PPA1883 PPA1884
            NCA: Noca_0711 Noca_0712 Noca_3875
            TFU: Tfu_1063 Tfu_2618 Tfu_2653 Tfu_2654
            FRA: Francci3_0573 Francci3_0574 Francci3_0610
            FAL: FRAAL1072(rpoB) FRAAL1073(rpoC) FRAAL1110(rpoA)
                 FRAAL5229(rpoZ)
            ACE: Acel_0299 Acel_0300 Acel_0334
            SEN: SACE_2101 SACE_6803 SACE_6853 SACE_6854
            STP: Strop_3932
            BLO: BL1204(rpoC) BL1205(rpoB) BL1606(rpoA) BL1787(rpoZ)
            BAD: BAD_0347(rpoA) BAD_0540(rpoZ) BAD_1318(rpoC) BAD_1319(rpoB)
            RXY: Rxyl_1472 Rxyl_2128 Rxyl_2161 Rxyl_2162
            FNU: FN1283 FN2032 FN2035 FN2036
            RBA: RB12626(rpoA) RB1964(rpoA) RB5414(rpoB) RB5416(rpoC)
                 RB7070(rpoA)
            CTR: CT314(rpoC) CT315(rpoB) CT507(rpoA)
            CTA: CTA_0336(rpoC) CTA_0337(rpoB) CTA_0556(rpoA)
            CMU: TC0588 TC0589 TC0794
            CPN: CPn0081(rpoB) CPn0082(rpoC) CPn0626(rpoA)
            CPA: CP0121 CP0693 CP0694
            CPJ: CPj0081(rpoB) CPj0082(rpoC) CPj0626(rpoA)
            CPT: CpB0081 CpB0082 CpB0652
            CCA: CCA00114(rpoA) CCA00690(rpoC) CCA00691(rpoB)
            CAB: CAB113(rpoA) CAB660(rpoC) CAB661(rpoB)
            CFE: CF0320(rpoB) CF0321(rpoC) CF0892(rpoA)
            PCU: pc0433(rpoA) pc0604(rpoB) pc0605(rpoC)
            BBU: BB0388(rpoC) BB0389(rpoB) BB0502(rpoA)
            BGA: BG0389(rpoC) BG0390(rpoB) BG0514(rpoA)
            BAF: BAPKO_0403(rpoC) BAPKO_0404(rpoB) BAPKO_0530(rpoA)
            TPA: TP0212 TP0241 TP0242 TP0701
            TDE: TDE0791(rpoA) TDE2420 TDE2421(rpoB)
            LIL: LA0765(rpoA) LA3419(rpoC) LA3420(rpoB)
            LIC: LIC10753(rpoB) LIC10754(rpoC) LIC12846(rpoA)
            LBJ: LBJ_2364(rpoC) LBJ_2365(rpoB) LBJ_2632(rpoA)
            LBL: LBL_0440(rpoA-1) LBL_0480(rpoA) LBL_0743(rpoB) LBL_0744(rpoC)
            SYN: sll1787(rpoB) sll1789(rpoC2) sll1818(rpoA) slr1265(rpoC1)
                 ssl2982(ycf61)
            SYW: SYNW0525(rpoZ) SYNW0613(rpoB) SYNW0614(rpoC1) SYNW0615(rpoC2)
                 SYNW2090(rpoA)
            SYC: syc1888_d(rpoA) syc2381_c(rpoZ) syc2507_d(rpoB)
                 syc2508_d(rpoC1) syc2509_d(rpoC2)
            SYF: Synpcc7942_1522 Synpcc7942_1523 Synpcc7942_1524
                 Synpcc7942_1710 Synpcc7942_2209
            SYD: Syncc9605_0353 Syncc9605_0785 Syncc9605_2065 Syncc9605_2066
                 Syncc9605_2067 Syncc9605_2158
            SYE: Syncc9902_0519 Syncc9902_0605 Syncc9902_0606 Syncc9902_0607
                 Syncc9902_1978
            SYG: sync_0414(rpoA) sync_2269 sync_2356(rpoC2) sync_2357(rpoC1)
                 sync_2358(rpoB)
            SYR: SynRCC307_1851(rpoZ) SynRCC307_1956(rpoC2)
                 SynRCC307_1957(rpoC1) SynRCC307_1959(rpoB)
                 SynRCC307_2139(rpoA)
            SYX: SynWH7803_0411(rpoA) SynWH7803_1989(rpoZ)
                 SynWH7803_2060(rpoC2) SynWH7803_2061(rpoC1)
                 SynWH7803_2062(rpoB)
            CYA: CYA_0155 CYA_0409(rpoB) CYA_0410(rpoC1) CYA_0411(rpoC2)
                 CYA_1451(rpoA)
            CYB: CYB_1580(rpoA) CYB_2308 CYB_2436(rpoB) CYB_2437(rpoC1)
                 CYB_2438(rpoC2)
            TEL: tll0640(rpoC2) tll0641(rpoC1) tll0642(rpoB) tlr0105(rpoA)
                 tsr2257(ycf61)
            GVI: gll3571(rpoA) glr2283(rpoB) glr4277(rpoC1) glr4278(rpoC2)
                 gsl1620
            ANA: all4191(rpoA) alr1594(rpoB) alr1595(rpoC1) alr1596(rpoC2)
                 asr4648
            AVA: Ava_0715 Ava_2015 Ava_4207 Ava_4208 Ava_4209
            PMA: Pro1584(rpoZ) Pro1638(rpoC) Pro1639(rpoC) Pro1640(rpoB)
                 Pro1689(rpoA)
            PMM: PMM1431(rpoZ) PMM1483(rpoC2) PMM1484(rpoC1) PMM1485(rpoB)
                 PMM1535(rpoA)
            PMT: PMT1442(rpoZ) PMT1505(rpoC2) PMT1506(rpoC1) PMT1507(rpoB)
                 PMT1755(rpoA)
            PMN: PMN2A_0963 PMN2A_1014 PMN2A_1015 PMN2A_1016 PMN2A_1106
            PMI: PMT9312_1524 PMT9312_1576 PMT9312_1577 PMT9312_1578
                 PMT9312_1628
            PMB: A9601_16331(rpoZ) A9601_16871(rpoC2) A9601_16881(rpoC1)
                 A9601_16891(rpoB) A9601_17431(rpoA)
            PMC: P9515_16091(rpoZ) P9515_16631(rpoC2) P9515_16641(rpoC1)
                 P9515_16651(rpoB) P9515_17171(rpoA)
            PMF: P9303_04361(rpoB) P9303_04371(rpoC1) P9303_04391(rpoC2)
                 P9303_05121(rpoZ) P9303_23261(rpoA)
            PMG: P9301_16211(rpoZ) P9301_16741(rpoC2) P9301_16751(rpoC1)
                 P9301_16761(rpoB) P9301_17271(rpoA)
            PMH: P9215_18071(rpoA)
            PME: NATL1_18311(rpoZ) NATL1_18841(rpoC2) NATL1_18851(rpoC1)
                 NATL1_18861(rpoB) NATL1_19811(rpoA)
            TER: Tery_2937 Tery_2938 Tery_2939 Tery_2988 Tery_3443
            BTH: BT_2701 BT_2733 BT_2734
            BFR: BF4155 BF4191 BF4192
            BFS: BF3976(rpoA) BF4014(rpoC) BF4015(rpoB)
            PGI: PG0394(rpoB) PG0395(rpoC) PG1911(rpoA)
            SRU: SRU_1060(rpoA) SRU_1757(rpoC) SRU_1758(rpoB)
            CHU: CHU_3136(rpoA) CHU_3168(rpoC) CHU_3169(rpoB) CHU_3562(rpoE)
            GFO: GFO_2814(rpoA)
            FPS: FP1176(rpoB) FP1313(rpoA)
            CTE: CT0155(rpoB) CT0156(rpoC) CT2162(rpoA)
            CCH: Cag_0357 Cag_0358 Cag_1824
            CPH: Cpha266_0233 Cpha266_0234 Cpha266_2396
            PVI: Cvib_0273 Cvib_1604 Cvib_1605
            PLT: Plut_0207 Plut_1961 Plut_1962
            DET: DET0502(rpoA) DET0603(rpoB) DET0604(rpoC)
            DEH: cbdb_A466(rpoA) cbdb_A586(rpoB) cbdb_A587(rpoC)
            DRA: DR_0911 DR_0912 DR_2128 DR_2494
            DGE: Dgeo_0252 Dgeo_0635 Dgeo_0636 Dgeo_1840
            TTH: TTC1196(rpoZ) TTC1300 TTC1460 TTC1461
            TTJ: TTHA1561 TTHA1664 TTHA1812 TTHA1813
            AAE: aq_070(rpoA) aq_183a(rpoZ) aq_1939(rpoB) aq_1945(rpoC)
            TMA: TM0458 TM0459 TM1472
            MJA: MJ0039 MJ0192(rpoD) MJ0196(rpoN) MJ0197(rpoK) MJ0387(rpoL)
                 MJ0396(rpoE2) MJ0397(rpoE1) MJ0593a(RPC10) MJ1039(rpoH)
                 MJ1040(rpoB2) MJ1041(rpoB1) MJ1042(rpoA1) MJ1043(rpoA2)
                 MJ1148(rpm) MJ1390(rpoI)
            MMP: MMP0092(rpoF) MMP0248 MMP0261 MMP0440 MMP0441(rpoE2)
                 MMP1322(rpoD) MMP1326(rpoN) MMP1327(rpoK) MMP1360(rpoH)
                 MMP1361(rpoB2) MMP1362(rpoB1) MMP1363(rpoA1) MMP1364(rpoA2)
                 MMP1429(rpm)
            MMQ: MmarC5_0214 MmarC5_0216 MmarC5_0217 MmarC5_1197
            MAC: MA0112 MA0598(rpoN) MA0599(rpoK) MA0721(rpoL) MA1262(rpoA2)
                 MA1263(rpoA1) MA1264(rpoB1) MA1265(rpoB2) MA1266(rpoH) MA1444
                 MA3692(rpoE1) MA3693(rpoE2) MA4672(rpoP)
            MBA: Mbar_A0075 Mbar_A0284 Mbar_A0285 Mbar_A0878 Mbar_A1424
                 Mbar_A1425 Mbar_A1637 Mbar_A2509 Mbar_A2536 Mbar_A3232
                 Mbar_A3691 Mbar_A3692 Mbar_A3693 Mbar_A3694 Mbar_A3695
            MMA: MM_0596 MM_0597 MM_1398 MM_1758 MM_1759 MM_1880 MM_2158
                 MM_2270 MM_2271 MM_2272 MM_2273 MM_2274 MM_2338 MM_2537
                 MM_2626
            MBU: Mbur_0039 Mbur_0202 Mbur_0904 Mbur_1176 Mbur_1177 Mbur_1178
                 Mbur_1179 Mbur_1180 Mbur_1439 Mbur_2194 Mbur_2280 Mbur_2281
                 Mbur_2391 Mbur_2392
            MTP: Mthe_0027 Mthe_0028 Mthe_0030 Mthe_0994 Mthe_1321 Mthe_1359
            MHU: Mhun_0049 Mhun_0050 Mhun_0051 Mhun_0052 Mhun_0053 Mhun_2285
                 Mhun_2336 Mhun_2863 Mhun_2864 Mhun_2894 Mhun_2895 Mhun_2899
                 Mhun_3027
            MLA: Mlab_1156
            MEM: Memar_0298 Memar_0299 Memar_0301 Memar_0312 Memar_0313
                 Memar_0315
            MBN: Mboo_1931 Mboo_1933 Mboo_1934 Mboo_2222
            MTH: MTH1048 MTH1049(rpoB2) MTH1050(rpoB1) MTH1051(rpoA1)
                 MTH1052(rpoA2) MTH1314 MTH1317 MTH1324 MTH264 MTH265 MTH297
                 MTH298 MTH299 MTH37 MTH40 MTH42 MTH680a
            MST: Msp_0623(rpoE2) Msp_0624(rpoE1) Msp_0863(rpoK) Msp_0864(rpoN)
                 Msp_0868(rpoD) Msp_1242(rpoM2) Msp_1372(rpoA2) Msp_1373(rpoA1)
                 Msp_1374(rpoB1) Msp_1375(rpoB2) Msp_1376(rpoH) Msp_1533(rpoM1)
                 Msp_1535(rpoL) Msp_1543
            MSI: Msm_0196 Msm_0197 Msm_0908 Msm_0909 Msm_0910 Msm_0911
                 Msm_0912 Msm_1354 Msm_1356 Msm_1376 Msm_1428 Msm_1432 Msm_1433
            MKA: MK0058(RPB11) MK0378(RPC10) MK0684(rpoC_1) MK0685(rpoC_2)
                 MK0686(rpoB_1) MK0687(rpoB_2) MK0688(RPB5) MK1451(rpoE1)
                 MK1452(rpoE2) MK1474(rpoA) MK1478(RPB10) MK1580(rpoZ)
            AFU: AF0056 AF0207(rpoL) AF1116(rpoE2) AF1117(rpoE1) AF1130(rpoN)
                 AF1131(rpoK) AF1235 AF1530 AF1885(rpoH) AF1886(rpoB2)
                 AF1887(rpoB1) AF1888(rpoA1) AF1889(rpoA2) AF2282(rpoD)
            HAL: VNG0237H VNG0426G(rpoM) VNG0860G(rpoL) VNG1136G(rpb3)
                 VNG1140G(rpoN) VNG1141G(rpoK) VNG1169C VNG2051G(rpoE'')
                 VNG2053G(rpoE') VNG2662G(rpoC) VNG2664Gm(rpoA) VNG2665G(rpoB')
                 VNG2666G(rpoB'') VNG2668G(rpoH)
            HMA: rrnAC0062(rpoD) rrnAC0067(rpoN) rrnAC0068(rpoK)
                 rrnAC0218(rpoM) rrnAC0259(rpb4) rrnAC0313(rpoM)
                 rrnAC1396(rpoL) rrnAC1668(rpoP) rrnAC2427(rpoC)
                 rrnAC2428(rpoA) rrnAC2429(rpoB) rrnAC2430(rpoB)
                 rrnAC2432(rpoH) rrnAC2829(rpoE') rrnAC2830(rpoE'')
            HWA: HQ1284A(rpoP) HQ1337A(rpoE1) HQ1338A(rpoE2) HQ1696A(rpoL)
                 HQ2396A(rpoM1) HQ2895A(rpoF) HQ2936A(rpoK) HQ2937A(rpoN)
                 HQ2941A(rpoD) HQ3190A(rpoM2) HQ3393A(rpoA2) HQ3394A(rpoA)
                 HQ3395A(rpoB1) HQ3396A(rpoB2) HQ3397A(rpoH)
            NPH: NP0108A(rpoH) NP0110A(rpoB2) NP0112A(rpoB1) NP0114A(rpoA1)
                 NP0116A(rpoA2) NP0364A(rpoM_1) NP2834A(rpoD) NP2842A(rpoN)
                 NP2844A(rpoK) NP3682A(rpoF) NP4162A(rpoL) NP4938A(rpoM_2)
                 NP5078A(rpoE2) NP5080A(rpoE1) NP5234A(rpoP)
            TAC: Ta0389 Ta0390 Ta0391 Ta0392 Ta0431 Ta1006 Ta1030 Ta1089m
                 Ta1090 Ta1160 Ta1298 Ta1416
            TVO: TVN0313 TVN0485 TVN0486 TVN0565 TVN0742 TVN1137 TVN1180
                 TVN1181 TVN1182 TVN1183 TVN1225 TVN1435
            PTO: PTO0257 PTO0258 PTO0259 PTO0260 PTO0325 PTO0388 PTO0391
                 PTO0413 PTO0543 PTO0866 PTO0867 PTO0894 PTO1222
            PHO: PH0664 PH1127 PH1544 PH1545 PH1546 PH1632 PH1637 PH1908
                 PHS044 PHS056
            PAB: PAB0423(rpoB) PAB0424(rpoA1) PAB0425(rpoA2) PAB0732
                 PAB1105(rpoE1) PAB1464 PAB2316(rpoL) PAB2410(rpoD) PAB3072
                 PAB7131(rpoN) PAB7132(rpoK) PAB7151(rpoH) PAB7428(rpoE2)
            PFU: PF0050 PF0255 PF0256 PF0986 PF1036 PF1562 PF1563 PF1564
                 PF1565 PF1642 PF1643 PF1647 PF2009
            TKO: TK0533 TK0616 TK0901 TK1081 TK1082 TK1083 TK1084 TK1167
                 TK1498 TK1499 TK1503 TK1698 TK1699
            RCI: LRC270(rpoL) LRC354(rpoB1) LRC356(rpoB2) LRC357(rpoA1)
                 LRC358(rpoA2) LRC403(rpoK) LRC404(rpoN) RCIX2017(rpoE)
                 RCIX2127(rpoP) RCIX2350(rpoF) RCIX2583(rpoD)
            APE: APE_0256a.1 APE_0257 APE_0442.1 APE_0443.1 APE_0549.1
                 APE_0914 APE_1007a APE_1629a.1 APE_1744.1 APE_1749a APE_1852.1
                 APE_1853.1 APE_1856 APE_1856a
            SMR: Smar_0802 Smar_0804
            HBU: Hbut_0438 Hbut_0439 Hbut_0530 Hbut_0534 Hbut_0917 Hbut_1572
                 Hbut_1573 Hbut_1574 Hbut_1646 Hbut_1648
            SSO: SSO0071(rpoD) SSO0223(rpoA2) SSO0225(rpoA1) SSO0227(rpoB1)
                 SSO0277(rpoG) SSO0291(rpoM-1) SSO0415(rpoE1) SSO0751(rpoF)
                 SSO3254(rpoB2) SSO5140(rpoN) SSO5468(rpoH) SSO5576(rpoM-like)
                 SSO5577(rpoL) SSO5798(rpoE2) SSO5865(rpoP) SSO6768(rpoK)
                 SSO9221(rpoM-2)
            STO: ST0275 ST0276 ST0277 ST0351 ST0379 ST0458 ST1472 ST2067
                 ST2261 STS038 STS052 STS136 STS221 STS238
            SAI: Saci_0083(rpoD) Saci_0087 Saci_0171(rpoM) Saci_0173(rpoL)
                 Saci_0625(rpoF) Saci_0661(rpoG) Saci_0691(rpoA2)
                 Saci_0692(rpoA1) Saci_0693(rpoB) Saci_0694(rpoH)
                 Saci_0834(rpoE) Saci_0835 Saci_0864(rpoP) Saci_1370(rpoK)
                 Saci_1587(rpoM)
            PAI: PAE0664(rpoH) PAE0665(rpoB) PAE0666(rpoA1) PAE0667(rpoA2)
                 PAE0671(rpoD) PAE0675a(rpoN) PAE1978(rpoL) PAE2258 PAE3040
                 PAE3271 PAE3335 PAE3480 PAE3562(rpoE1) PAE3563(rpoE2)
            PIS: Pisl_0701 Pisl_0703
            PCL: Pcal_2091 Pcal_2093
            PAS: Pars_2321 Pars_2323
            TPE: Tpen_0284 Tpen_0286
            NEQ: NEQ156 NEQ173 NEQ182 NEQ231 NEQ338 NEQ370 NEQ377 NEQ411
                 NEQ427 NEQ452 NEQ503 NEQ507
STRUCTURES  PDB: 1A1D  1ARO  1BDF  1CEZ  1DZF  1EF4  1EIK  1GO3  1H38  1HQM  
                 1I3Q  1I50  1I6H  1I6V  1IW7  1K83  1L9U  1L9Z  1LB2  1MSW  
                 1NIK  1NT9  1PQV  1QKL  1QLN  1R5U  1R9S  1R9T  1S0V  1S76  
                 1S77  1SFO  1SMY  1TWA  1TWC  1TWF  1TWG  1TWH  1WCM  1XPP  
                 1XS9  1Y14  1Y1V  1Y1W  1Y1Y  1Y77  1YNJ  1YNN  1Z3E  1ZYR  
                 2A68  2A69  2A6E  2A6H  2AUJ  2AUK  2B63  2B8K  2BE5  2C35  
                 2CKZ  2CW0  2DK5  2DK8  2E2H  2E2I  2E2J  2F3I  2GHO  2GHQ  
                 2GHT  2JA5  2JA6  2JA7  2JA8  2NVQ  2NVT  2NVX  2NVY  2NVZ  
                 2O5I  2O5J  2PI4  2PI5  2PPB  2YU9  4RNP  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.6
            ExPASy - ENZYME nomenclature database: 2.7.7.6
            ExplorEnz - The Enzyme Database: 2.7.7.6
            ERGO genome analysis and discovery system: 2.7.7.6
            BRENDA, the Enzyme Database: 2.7.7.6
            CAS: 9014-24-8
///
ENTRY       EC 2.7.7.7                  Enzyme
NAME        DNA-directed DNA polymerase;
            DNA polymerase I;
            DNA polymerase II;
            DNA polymerase III;
            DNA polymerase alpha;
            DNA polymerase beta;
            DNA polymerase gamma;
            DNA nucleotidyltransferase (DNA-directed);
            DNA nucleotidyltransferase (DNA-directed);
            deoxyribonucleate nucleotidyltransferase;
            deoxynucleate polymerase;
            deoxyribonucleic acid duplicase;
            deoxyribonucleic acid polymerase;
            deoxyribonucleic duplicase;
            deoxyribonucleic polymerase;
            deoxyribonucleic polymerase I;
            DNA duplicase;
            DNA nucleotidyltransferase;
            DNA polymerase;
            DNA replicase;
            DNA-dependent DNA polymerase;
            duplicase;
            Klenow fragment;
            sequenase;
            Taq DNA polymerase;
            Taq Pol I;
            Tca DNA polymerase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     deoxynucleoside-triphosphate:DNA deoxynucleotidyltransferase
            (DNA-directed)
REACTION    deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1
            [RN:R00379]
ALL_REAC    R00379 > R00375 R00376 R00377 R00378
SUBSTRATE   deoxynucleoside triphosphate [CPD:C00677];
            DNAn [CPD:C00039]
PRODUCT     diphosphate [CPD:C00013];
            DNAn+1 [CPD:C00039]
COMMENT     Catalyses DNA-template-directed extension of the 3'- end of a DNA
            strand by one nucleotide at a time. Cannot initiate a chain de novo.
            Requires a primer, which may be DNA or RNA. See also EC 2.7.7.49
            RNA-directed DNA polymerase.
REFERENCE   1  [PMID:13802334]
  AUTHORS   BOLLUM FJ.
  TITLE     Calf thymus polymerase.
  JOURNAL   J. Biol. Chem. 235 (1960) 2399-403.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:4957767]
  AUTHORS   Falaschi A, Kornberg A.
  TITLE     Biochemical studies of bacterial sporulation. II. Deoxy- ribonucleic
            acid polymerase in spores of Bacillus subtilis.
  JOURNAL   J. Biol. Chem. 241 (1966) 1478-82.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   3  [PMID:13563462]
  AUTHORS   LEHMAN IR, BESSMAN MJ, SIMMS ES, KORNBERG A.
  TITLE     Enzymatic synthesis of deoxyribonucleic acid. I. Preparation of
            substrates and partial purification of an enzyme from Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 233 (1958) 163-70.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4
  AUTHORS   Richardson, C.C., Schildkraut, C.L., Aposhian, H.V. and Kornberg, A.
  TITLE     Enzymatic synthesis of deoxyribonucleic acid. XIV. Further
            purification and properties of deoxyribonucleic acid polymerase of
            Escherichia coli.
  JOURNAL   J. Biol. Chem. 239 (1964) 222-232.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5
  AUTHORS   Schachman, H.K., Adler, J., Radding, C.M., Lehman, I.R. and
            Kornberg, A.
  TITLE     Enzymatic synthesis of deoxyribonucleic acid. VII. Synthesis of a
            polymer of deoxyadenylate and deoxythymidylate.
  JOURNAL   J. Biol. Chem. 235 (1960) 3242-3249.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:5946628]
  AUTHORS   Zimmerman BK.
  TITLE     Purification and properties of deoxyribonucleic acid polymerase from
            Micrococcus lysodeikticus.
  JOURNAL   J. Biol. Chem. 241 (1966) 2035-41.
  ORGANISM  Micrococcus lysodeikticus
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
            PATH: map03030  DNA polymerase
ORTHOLOGY   KO: K00961  DNA polymerase
            KO: K02319  DNA polymerase I
            KO: K02320  DNA polymerase alpha, subunit A
            KO: K02321  DNA polymerase alpha, subunit B
            KO: K02322  DNA polymerase II large subunit
            KO: K02323  DNA polymerase II small subunit
            KO: K02324  DNA polymerase epsilon, subunit A
            KO: K02325  DNA Polymerase epsilon, subunit B
            KO: K02326  DNA Polymerase epsilon, subunit C
            KO: K02327  DNA polymerase delta, subunit A
            KO: K02328  DNA polymerase delta, subunit B
            KO: K02330  DNA polymerase beta subunit
            KO: K02331  DNA polymerase phi subunit
            KO: K02332  DNA polymerase gamma subunit
            KO: K02333  DNA polymerase gamma2 subunit
            KO: K02334  DNA polymerase bacteriophage-type
            KO: K02335  DNA polymerase I
            KO: K02336  DNA polymerase II
            KO: K02337  DNA polymerase III alpha subunit
            KO: K02338  DNA polymerase III beta subunit
            KO: K02339  DNA polymerase III chi subunit
            KO: K02340  DNA polymerase III delta subunit
            KO: K02341  DNA polymerase III delta' subunit
            KO: K02342  DNA polymerase III epsilon subunit
            KO: K02343  DNA polymerase III gamma and tau subunit
            KO: K02344  DNA polymerase III psi subunit
            KO: K02345  DNA polymerase III theta subunit
            KO: K02346  DNA polymerase IV
            KO: K02349  DNA polymerase theta subunit
            KO: K02350  DNA polymerase zeta subunit
            KO: K03504  DNA polymerase delta, subunit C
            KO: K03505  DNA polymerase delta, subunit D
            KO: K03506  DNA polymerase epsilon, subunit D
            KO: K03508  DNA polymerase zeta subunit
            KO: K03509  DNA polymerase eta subunit
            KO: K03510  DNA polymerase iota subunit
            KO: K03511  DNA polymerase kappa subunit
            KO: K03512  DNA polymerase lambda subunit
            KO: K03513  DNA polymerase mu subunit
            KO: K03514  DNA polymerase sigma subunit
            KO: K03763  DNA polymerase III alpha subunit, the Gram-positive type
            KO: K04330  DNA polymerase III complex
                        {K02337+K03763+K02342+K02345+K02343+K02341+K02340+K02339
                        +K02344+K02338}
            KO: K04474  DNA polymerase alpha / primase complex
                        {K02320+K02321+K02685+K02684}
            KO: K04475  DNA polymerase delta complex
                        {K02327+K02328+K03504+K03505}
            KO: K04476  DNA polymerase epsilon complex
                        {K02324+K02325+K02326+K03506}
            KO: K04479  DNA polymerase IV (archaeal DinB-lile DNA polymerase)
            KO: K04480  archaeal DnaQ-like DNA polymerase
            KO: K04481  DNA polymerase II complex {K02322+K02323}
GENES       HSA: 10714(POLD3) 10721(POLQ) 11044(POLS) 11201(POLI) 11232(POLG2)
                 23649(POLA2) 27343(POLL) 27434(POLM) 51426(POLK) 54107(POLE3)
                 5422(POLA1) 5423(POLB) 5424(POLD1) 5425(POLD2) 5426(POLE)
                 5427(POLE2) 5428(POLG) 5429(POLH) 56655(POLE4) 57804(POLD4)
                 5980(REV3L) 5985(RFC5)
            PTR: 450687(POLL) 451318(POLA2) 451422(POLD3) 452888(POLE2)
                 455266(POLG2) 455429(POLI) 461803(POLK) 462720(POLH)
                 467754(POLG) 472654(POLD2)
            MCC: 693548(RFC2) 710562(LOC710562) 720633(LOC720633)
            MMU: 18968(Pola1) 18969(Pola2) 18970(Polb) 18971(Pold1)
                 18972(Pold2) 18973(Pole) 18974(Pole2) 18975(Polg) 19075(Prim1)
                 19714(Rev3l) 210106(Pols) 214627(Papd5) 26447(Poli)
                 27015(Polk) 50776(Polg2) 54125(Polm) 56626(Poll) 59001(Pole3)
                 66979(Pole4) 67967(Pold3) 69745(Pold4) 72151(Rfc5) 77782(Polq)
                 80905(Polh)
            RNO: 171525(Polk) 288079(Polq_predicted) 289757(Polm)
                 289758(Pold2) 291526(Poli_predicted) 29240(Polb) 293144(Pold3)
                 298098(Pole3) 299112(Pole2_predicted) 303612(Polg2_predicted)
                 304573(Pole) 306672(Pols_predicted) 307745(Papd5_predicted)
                 309812(Rev3l) 316235(Polh_predicted) 361698(Pold4)
                 361767(Poll) 362385(Pole4_predicted) 59294(Pold1) 85242(Pola2)
                 85472(Polg)
            CFA: 474915(POLH) 476025(POLA2) 476806(POLD3) 477499(RFC5)
                 478131(PAPD5) 479180(POLK) 480869(POLA1) 482686(POLD2)
                 483096(POLE4) 486223(POLE) 488003(POLQ) 488057(POLS)
                 488732(POLG) 490910(POLG2) 494001(POLB) 608341(POLL)
                 608973(POLE2) 610047(POLD1) 611847(POLD4) 612550(POLE3)
            BTA: 281990(POLD1) 281991(POLD2) 535323(LOC535323)
            GGA: 374003(POLK) 395102(POLH) 404292(POLG) 415733(PAPD5)
                 416997(POLE) 417275(POLE3) 418326(POLQ) 418593(POLA1)
                 419053(POLD3) 423567(POLE2) 423853(RCJMB04_8k6) 426794(POLB)
                 428622(REV3L) 770992(LOC770992)
            XLA: 379793(pold2) 380369(rfc5) 398707(POLD3) 443952(MGC80325)
                 446387(polk) 446807(MGC80532) 446909(polh) 447518(pold)
            XTR: 448219(polk) 448271(pold2) 448613(TGas140j02.1) 496525(rfc5)
            DRE: 192320(pole2) 322059(pola2) 368733(pold2) 393218(zgc:56122)
                 393774(zgc:73351) 406697(poll)
            SPU: 574732(LOC574732) 575728(LOC575728) 578718(LOC578718)
                 580013(LOC580013) 580054(LOC580054) 580288(LOC580288)
                 580974(LOC580974) 582628(LOC582628) 583312(LOC583312)
                 586784(LOC586784) 592046(LOC592046) 592195(LOC592195)
                 756629(LOC756629)
            DME: Dmel_CG10489 Dmel_CG11265 Dmel_CG11301 Dmel_CG12018
                 Dmel_CG12189 Dmel_CG14999(RfC40) Dmel_CG17462
                 Dmel_CG1925(mus205) Dmel_CG5923(DNApol-alpha73)
                 Dmel_CG5949(DNApol-delta) Dmel_CG6019(mus308)
                 Dmel_CG6189(l(1)1Bi) Dmel_CG6258(RfC38)
                 Dmel_CG6349(DNApol-alpha180) Dmel_CG6768(DNApol-epsilon)
                 Dmel_CG7108(DNApol-alpha50) Dmel_CG7143 Dmel_CG7602
                 Dmel_CG8987(tam)
            CEL: F08B4.5 F10C2.4 F12F6.7 F22B7.6(mucb) F33H2.5 F53A3.2(polh-1)
                 R01H10.1(div-1) T26A5.8 Y37B11A.2 Y47D3A.29 Y53F4B.3
                 Y57A10A.15 ZK858.1
            ATH: AT1G08260(EMB2284/POL2A/TIL1) AT1G09815 AT1G10520
                 AT1G67500(ATREV3) AT1G67630 AT2G02480(STI)
                 AT2G27120(POL2B/TIL2) AT4G24790 AT5G22110(DBP2) AT5G44740
                 AT5G53770 AT5G63960 AT5G67100
            OSA: 4325052 4325305 4329458 4331489 4333450 4337150 4337886
                 4340604 4347604 4349968 4351872
            CME: CMA062C CMB052C CMH082C CMI176C CMN199C CMQ098C CMR103C
                 CMT350C CMT462C
            SCE: YBL035C(POL12) YBR278W(DPB3) YCR014C(POL4) YDL102W(CDC2)
                 YDR121W(DPB4) YDR419W(RAD30) YEL055C(POL5) YIL139C(REV7)
                 YJL090C(DPB11) YJR006W(HYS2) YJR043C(POL32) YNL102W(POL1)
                 YNL262W(POL2) YNL299W(TRF5) YOL115W(PAP2) YOR330C(MIP1)
                 YPL167C(REV3) YPR175W(DPB2)
            AGO: AGOS_AAL099C AGOS_AAL132C AGOS_AAR136W AGOS_ACR020C
                 AGOS_ADL299C AGOS_ADR357C AGOS_AEL075W AGOS_AEL207W
                 AGOS_AEL267C AGOS_AER381C AGOS_AER420C AGOS_AFL189W
                 AGOS_AFR095C AGOS_AFR657C AGOS_AGR053W
            PIC: PICST_14247(MIP1) PICST_28505(LIP10) PICST_30658(DPB3)
                 PICST_34779 PICST_36809(MTR4) PICST_39313(RFC4)
                 PICST_40682(HYS2) PICST_41858(RAD30) PICST_42338(REV3)
                 PICST_52420(TRF4) PICST_54312(SLH1) PICST_56859(POL5)
                 PICST_60537(RCF3) PICST_61628(MGS1) PICST_63206(DPOD)
                 PICST_66970(POL2) PICST_72583(RCF2) PICST_74461(DPB2)
                 PICST_83141(DPB11) PICST_86981(POL1) PICST_90280(POL12)
            CAL: CaO19.1434 CaO19.2796(pol12) CaO19_2088(CaO19.2088)
                 CaO19_3431(CaO19.3431) CaO19_3960(CaO19.3960)
                 CaO19_7564(CaO19.7564) CaO19_866(CaO19.866)
            CGR: CAGL0B03553g CAGL0B03707g CAGL0E02101g CAGL0E05324g
                 CAGL0F02959g CAGL0F04323g CAGL0G09801g CAGL0I03256g
                 CAGL0J08030g CAGL0L07348g CAGL0L08316g CAGL0M02035g
                 CAGL0M03575g CAGL0M03751g
            SPO: SPAC12G12.13c(cid14) SPAC23C4.18c(rad4) SPAC27E2.05(cdc1)
                 SPAC3H5.06c(pol1) SPAC688.10 SPBC12D12.02c SPBC14C8.14c(pol5)
                 SPBC16A3.11 SPBC1734.02c(cdc27) SPBC25H2.13c(cdc20)
                 SPBC336.04(pol3) SPBC3D6.09 SPBP8B7.14c SPCC553.07c
                 SPCC553.09c
            ANI: AN2446.2 AN2739.2 AN3067.2 AN3373.2 AN3857.2 AN3944.2
                 AN4678.2 AN4789.2 AN5620.2 AN5694.2 AN6855.2 AN7325.2 AN7439.2
            AFM: AFUA_1G05260 AFUA_1G10480 AFUA_2G06190 AFUA_2G16600
                 AFUA_3G06780 AFUA_3G09560 AFUA_4G07970 AFUA_4G11140
                 AFUA_5G09000 AFUA_5G12640 AFUA_5G13020 AFUA_6G08170
                 AFUA_6G10560 AFUA_7G01270 AFUA_7G04130
            AOR: AO090001000736 AO090003000106 AO090003000822 AO090005000098
                 AO090005001292 AO090010000199 AO090020000319 AO090020000472
                 AO090023000217 AO090038000378 AO090102000174 AO090120000390
                 AO090120000422
            CNE: CNB00310 CNB00780 CNB03700 CNC01540 CNE03660 CNF03830
                 CNF04130 CNK00560 CNK01430 CNL04490 CNL05040 CNM01440
            UMA: UM00101.1 UM00275.1 UM00527.1 UM00599.1 UM01008.1 UM01293.1
                 UM01931.1 UM02557.1 UM02760.1 UM04623.1 UM04976.1 UM05141.1
            ECU: ECU05_0990 ECU09_0430 ECU09_0770 ECU10_1080
            DDI: DDBDRAFT_0204579 DDB_0191131(polA) DDB_0216318(YBL1)
                 DDB_0216320 DDB_0216321 DDB_0216394 DDB_0232268(polDA)
                 DDB_0232271(polZ) DDB_0232274(polA1) DDB_0232277(polA2)
            PFA: MAL3P3.4 PF10_0165 PF10_0362 PF14_0112 PF14_0234 PF14_0602
                 PFD0590c PFF1225c PFF1470c PFL1285c
            CPV: cgd3_4290 cgd4_3920 cgd6_4410 cgd8_1240 cgd8_1620 cgd8_870
            CHO: Chro.30484 Chro.60506 Chro.80106 Chro.80147 Chro.80190
            TAN: TA03330 TA06290 TA09840 TA12280 TA13340 TA20960
            TPV: TP01_0899 TP01_0978 TP02_0469 TP03_0202 TP04_0813 TP04_0814
            TET: TTHERM_00043780 TTHERM_00048980 TTHERM_00112520
                 TTHERM_00391570 TTHERM_00424700 TTHERM_00437650
                 TTHERM_00636920
            TBR: Tb09.211.1820 Tb09.244.2820 Tb10.70.6190 Tb11.01.0010
                 Tb11.01.0020 Tb11.01.0030 Tb11.01.0040 Tb11.01.0050
                 Tb11.01.0060 Tb11.01.0080 Tb11.02.2300 Tb11.12.0001
                 Tb11.12.0003 Tb927.2.1800 Tb927.3.1130 Tb927.4.2950
                 Tb927.5.2790 Tb927.8.3290 Tb927.8.4880
            TCR: 503755.10 503755.30 503879.10 506147.180 506227.80 506265.30
                 506435.30 507265.30 508837.180 509215.10 509455.70 509671.160
                 509769.130 510131.50 510131.70 510733.60 510763.80 511847.60
                 511911.120
            LMA: LmjF13.0080 LmjF16.1540 LmjF21.0630 LmjF23.1330 LmjF25.1410
                 LmjF28.1420 LmjF33.1690 LmjF34.1260 LmjF35.1790 LmjF35.4360
            EHI: 2.t00064 268.t00004 281.t00008 370.t00004 406.t00005
                 436.t00002 53.t00034 59.t00030 8.t00042
            ECO: b0060(polB) b0184(dnaE) b0215(dnaQ) b0231(dinB) b0470(dnaX)
                 b0640(holA) b1099(holB) b1842(holE) b3701(dnaN) b3863(polA)
                 b4259(holC) b4372(holD)
            ECJ: JW0059(polB) JW0179(dnaE) JW0205(dnaQ) JW0221(dinB)
                 JW0459(dnaX) JW0635(holA) JW1085(holB) JW1831(holE)
                 JW3678(dnaN) JW3835(polA) JW4216(holC) JW4334(holD)
            ECE: Z0068(polB) Z0196(dnaE) Z0241(dnaQ) Z0292(dinP) Z0587(dnaX)
                 Z0787(holA) Z1738(holB) Z2891(holE) Z5192(dnaN) Z5398(polA)
                 Z5871(holC) Z5973(holD)
            ECS: ECs0064 ECs0186 ECs0211 ECs0258 ECs0523 ECs0678 ECs1477
                 ECs2552 ECs4636 ECs4786 ECs5236 ECs5330
            ECC: c0071(polB) c0221(dnaE) c0252(dnaQ) c0379(dinP) c0589(dnaX)
                 c0731(holA) c1371(holB) c2252(holE) c4623(dnaN) c5359(holC)
                 c5452(holD)
            ECI: UTI89_C0065(polB) UTI89_C0199(dnaE) UTI89_C0234(dnaQ)
                 UTI89_C0271(dinP) UTI89_C0497(dnaX) UTI89_C0643(holA)
                 UTI89_C1155(ycdX) UTI89_C1226(holB) UTI89_C2044(holE)
                 UTI89_C2114(uvrC) UTI89_C2848(hscA) UTI89_C4251(dnaN)
                 UTI89_C4452(polA) UTI89_C4865(holC) UTI89_C5081(holD)
            ECP: ECP_0061 ECP_0192 ECP_0221 ECP_0260 ECP_0531 ECP_0670
                 ECP_1091 ECP_1786 ECP_3902 ECP_4074 ECP_4508 ECP_4755
            ECV: APECO1_1415(holA) APECO1_1545(dnaX) APECO1_1738(dinB)
                 APECO1_1775(dnaQ) APECO1_180(holB) APECO1_1803(dnaE)
                 APECO1_1924(polB) APECO1_2135(holC) APECO1_2598(polA)
                 APECO1_2756(dnaN)
            ECW: EcE24377A_0062(polB) EcE24377A_0188(dnaE)
                 EcE24377A_0221(dnaQ) EcE24377A_0265(dinB) EcE24377A_0507(dnaX)
                 EcE24377A_0666(holA) EcE24377A_1220(holB) EcE24377A_2071(holE)
                 EcE24377A_4211(dnaN) EcE24377A_4382(polA) EcE24377A_4830(holC)
                 EcE24377A_4967(holD)
            ECX: EcHS_A0064 EcHS_A0186 EcHS_A0218 EcHS_A0260 EcHS_A0547
                 EcHS_A0692(holA) EcHS_A1221(holB) EcHS_A1893(fadD)
                 EcHS_A1933(holE) EcHS_A3914 EcHS_A4088 EcHS_A4515(holC)
                 EcHS_A4606(holD)
            STY: HCM2.0015c STY0112(polB) STY0254(dnaE) STY0285(dnaQ)
                 STY0358(dinP) STY0528(dnaX) STY0697(holA) STY1240(holB)
                 STY2082(holE) STY3881(polA) STY3941(dnaN) STY4815(holC)
                 STY4907(holD)
            STT: t0100(polB) t0232(dnaE) t1001(holE) t1719(holB) t2221(holA)
                 t2376(dnaX) t2537(dinP) t2601(dnaQ) t3621(polA) t3682(dnaN)
                 t4511(holC) t4600(holD)
            SPT: SPA0098(polB) SPA0238(dnaE) SPA0993(holE) SPA1650(holB)
                 SPA2088(holA) SPA2238(dnaX) SPA2442(dinP) SPA2505(dnaQ)
                 SPA3681(dnaN) SPA3840(polA) SPA4277(holC) SPA4371(holD)
            SEC: SC0092(polB) SC0231(dnaE) SC0260(dnaQ) SC0314(dinP)
                 SC0525(dnaX) SC0676(holA) SC1151(holB) SC1881(holE)
                 SC3755(dnaN) SC3891(polA) SC4332(holC)
            STM: STM0097(polB) STM0231(dnaE) STM0264(dnaQ) STM0313(dinP)
                 STM0484(dnaX) STM0646(holA) STM1201(holB) STM1876(holE)
                 STM3837(dnaN) STM3999(polA) STM4476.S(holC) STM4557(holD)
            YPE: YPO0017(polA) YPO0428(holD) YPO0518(polB) YPO1059(dnaE)
                 YPO1082(dnaQ) YPO1606(holB) YPO1782(holE) YPO2608(holA)
                 YPO3122(dnaX) YPO3231(dinP) YPO3442(holC) YPO4096(dnaN)
            YPK: y0745(holC) y0959(dinP) y1060(dnaX) y1182(holA) y1765(holB)
                 y2525(holE) y3094(dnaQ) y3120(dnaE) y3655(polB) y3752(holD)
                 y3811(polA) y4112(dnaN)
            YPM: YP_0018(polA) YP_0642(holC) YP_0702(dinP) YP_0807(dnaX)
                 YP_1105(holA) YP_1611(holE) YP_2248(holB) YP_2767(dnaQ)
                 YP_2791(dnaE) YP_3661(polB) YP_3753(holD) YP_4004(dnaN)
            YPA: YPA_0535 YPA_0560 YPA_1157 YPA_1919 YPA_2489 YPA_2616
                 YPA_2721 YPA_3525 YPA_3577 YPA_3856 YPA_4142 YPA_MT0059
            YPN: YPN_0244 YPN_0299 YPN_0393 YPN_0646 YPN_0864 YPN_0966
                 YPN_1093 YPN_2023 YPN_2341 YPN_2916 YPN_2941 YPN_3954
                 YPN_MT0059
            YPP: YPDSF_0002 YPDSF_1630 YPDSF_1653 YPDSF_1841 YPDSF_2645
                 YPDSF_2759 YPDSF_2858 YPDSF_3116 YPDSF_3886 YPDSF_4091
            YPS: YPTB0018(polA) YPTB0530(holC) YPTB0573(holD) YPTB0659(polB)
                 YPTB0896(dinP) YPTB0992(dnaX) YPTB1101(holA) YPTB1658(holE)
                 YPTB2465(holB) YPTB2964(dnaQ) YPTB2988(dnaE) YPTB3136
                 YPTB3942(dnaN)
            YPI: YpsIP31758_0021(polA) YpsIP31758_1028(dnaE)
                 YpsIP31758_1055(dnaQ) YpsIP31758_1584(holB)
                 YpsIP31758_2343(holE) YpsIP31758_2928(holA)
                 YpsIP31758_3059(dnaX) YpsIP31758_3157(dinB)
                 YpsIP31758_3418(polB) YpsIP31758_3506(holD)
                 YpsIP31758_3544(holC) YpsIP31758_4152(dnaN)
            YEN: YE0021(polA) YE0637(dinA) YE0922(dnaQ)
            SFL: SF0055(polB) SF0174(dnaE) SF0200(dnaQ) SF0279(dinP)
                 SF0415(dnaX) SF0641(holA) SF1103(holB) SF1853(holE)
                 SF3763(dnaN) SF3934(polA) SF4230(holC) SF4403(holD)
            SFX: S0057(polB) S0177(dnaE) S0209(dnaQ) S0300(dinP) S0422(dnaX)
                 S0663(holA) S1183(holB) S1918(holE) S3813(polA) S4008(dnaN)
                 S4491(holC) S4675(holD)
            SFV: SFV_0052(polB) SFV_0167(dnaE) SFV_0198(dnaQ) SFV_0299(dinP)
                 SFV_0443(dnaX) SFV_0686(holA) SFV_1119(holB) SFV_1844(holE)
                 SFV_3637(polA) SFV_3811(dnaN) SFV_4234(holC) SFV_4406(holD)
            SSN: SSON_0066(polB) SSON_0196(dnaE) SSON_0229(dnaQ)
                 SSON_0274(dinP) SSON_0457(dnaX) SSON_0594(holA)
                 SSON_1119(holB) SSON_1306(holE) SSON_3651(dnaN)
                 SSON_4036(polA) SSON_4444(holC) SSON_4522(holD)
            SBO: SBO_0047(polB) SBO_0172(dnaE) SBO_0204(dnaQ) SBO_0370(dnaX)
                 SBO_0504(holA) SBO_1146(holE) SBO_1964(holB) SBO_3676(dnaN)
                 SBO_3876(polA) SBO_4181(holC) SBO_4433(holD)
            SDY: SDY_0200(dnaE) SDY_0234(dnaQ) SDY_0449(dnaX) SDY_0483(dinP)
                 SDY_0562(holA) SDY_1128(holE) SDY_2051(holB) SDY_3879(polA)
                 SDY_4183(dnaN) SDY_4283(holC) SDY_4631(holD)
            ECA: ECA0021(polA) ECA0403(holC) ECA0734(holD) ECA1046(dnaE)
                 ECA1176(dnaX) ECA1307(holA) ECA1803(holB) ECA2363
                 ECA2475(holE) ECA3339(dnaQ) ECA3468(dinB) ECA3852(polB)
                 ECA4440(dnaN)
            PLU: plu0002(dnaN) plu0386(polA) plu0687(dnaE) plu0943(dnaQ)
                 plu1239(dinP) plu1301(holA) plu2690(holE) plu2827(holB)
                 plu3841(dnaX) plu4251(holD) plu4482(holC)
            BUC: BU011(dnaN) BU238(dnaE) BU248(dnaQ) BU354(holB) BU431(polA)
                 BU445(holA) BU481(dnaX)
            BAS: BUsg011(dnaN) BUsg233(dnaE) BUsg240(dnaQ) BUsg342(holB)
                 BUsg416(pol) BUsg430(holA) BUsg466(dnaX)
            BAB: bbp011(dnaN) bbp220(dnaE) bbp230(dnaQ) bbp324(holB)
                 bbp382(polA) bbp396(holA) bbp425(dnaX)
            BCC: BCc_003(dnaN) BCc_148(dnaE) BCc_156(dnaQ) BCc_219(holB)
                 BCc_265(polA) BCc_275(holA) BCc_300(dnaX)
            WBR: WGLp015(dnaN) WGLp069(dnaQ) WGLp095(holB) WGLp170(holA)
                 WGLp216(holE) WGLp256(polA) WGLp379(dnaE) WGLp525(dnaX)
            SGL: SG0002 SG0390 SG0592 SG0689 SG0801 SG1066 SG1274 SG1928
                 SG2110 SG2235
            ENT: Ent638_0002 Ent638_0722 Ent638_0749 Ent638_0762 Ent638_0950
                 Ent638_1174 Ent638_1614 Ent638_1908 Ent638_2212 Ent638_4102
            KPN: KPN_00230(dnaQ)
            SPE: Spro_0033 Spro_0561 Spro_0731 Spro_0912 Spro_0962 Spro_1135
                 Spro_1205 Spro_1912 Spro_2606 Spro_3775 Spro_4887
            BFL: Bfl016(dnaN) Bfl034(holC) Bfl110(holD) Bfl225(dnaQ)
                 Bfl286(dnaE) Bfl301(dnaX) Bfl311(holA) Bfl400(holB)
                 Bfl619(polA)
            BPN: BPEN_015(dnaN) BPEN_034(holC) BPEN_114(holD) BPEN_232(dnaQ)
                 BPEN_294(dnaE) BPEN_309(dnaX) BPEN_319(holA) BPEN_412(holB)
                 BPEN_645(polA)
            HIN: HI0011(holD) HI0137(dnaQ) HI0455(holB) HI0739(dnaE)
                 HI0856(polA) HI0923(holA) HI0992(dnaN) HI1229(dnaX)
                 HI1397(holC)
            HIT: NTHI0015(holD) NTHI0223(dnaQ) NTHI0582(holB) NTHI0897(dnaE)
                 NTHI1024(polA) NTHI1092(holA) NTHI1166(dnaN) NTHI1753(holC)
                 NTHI1939(dnaX)
            HIP: CGSHiEE_00745 CGSHiEE_03880 CGSHiEE_07005
            HIQ: CGSHiGG_01860 CGSHiGG_05515 CGSHiGG_07200(dnaE) CGSHiGG_08555
            HDU: HD0211(holD) HD0223(dnaQ) HD0551(dnaE) HD0667(holC)
                 HD0850(dnaN) HD1130(holA) HD1236(polA) HD1819(dnaX)
                 HD1935(holB)
            HSO: HS_0137(dnaN) HS_0198(dnaE) HS_0301(dnaQ) HS_0490(holD)
                 HS_0603(dnaQ) HS_0718(polA) HS_0931(dinP) HS_1200(dnaX)
                 HS_1264(holC) HS_1486(holB) HS_1555(holA)
            PMU: PM0034(dnaE) PM0106(dnaQ) PM0364(dnaX) PM0467(dinP)
                 PM0822(holC) PM0959(hold) PM1065(polA) PM1160(dnaN)
                 PM1216(holA) PM1674(holB)
            MSU: MS0225(polA) MS0332(holA) MS0486(dnaN) MS0570(holB)
                 MS0574(dnaE) MS0871(dnaX) MS1135(dinP) MS1557(holC)
                 MS1570(dnaQ) MS1589
            APL: APL_0002(dnaN) APL_0265(dnaX) APL_0473(polA) APL_0874(holA)
                 APL_1040(dinP) APL_1105(dnaE) APL_1282(dnaQ) APL_1505(holC)
                 APL_1816(holB) APL_2006(holD)
            ASU: Asuc_0002 Asuc_0021 Asuc_0746 Asuc_0875 Asuc_0971 Asuc_1058
                 Asuc_1452 Asuc_1862 Asuc_1866
            XFA: XF0002 XF0136 XF0204 XF0676 XF1103 XF1807 XF2157 XF2178
            XFT: PD0002(dnaN) PD0104(holC) PD0165(dnaE) PD0396(polA)
                 PD1059(dnaX) PD1217(dnaQ) PD1232(holA) PD1498(holB)
            XCC: XCC0002(dnaN) XCC0583(dinP) XCC0648(holC) XCC0988(dnaQ)
                 XCC1001(dnaX) XCC1023(holB) XCC1101(dnaE2) XCC1358(dnaE1)
                 XCC2617(holA) XCC3664 XCC4020(polA)
            XCB: XC_0002 XC_1499 XC_2880 XC_3148 XC_3222 XC_3244 XC_3255
                 XC_3586 XC_3650 XC_3735 XC_3967 XC_4109
            XCV: XCV0002(dnaN) XCV1090(dnaQ) XCV1127(dnaX) XCV1151(holB)
                 XCV1226(dnaE1) XCV1463(dnaE2) XCV2935(holA) XCV3683(holC)
                 XCV3740(dinP) XCV3825 XCV4200(polA)
            XAC: XAC0002(dnaN) XAC1090(dnaQ) XAC1109(dnaX) XAC1132(holB)
                 XAC1199(dnaE2) XAC1406(dnaE1) XAC2779(holA) XAC3558(holC)
                 XAC3622(dinP) XAC3704 XAC4110(polA)
            XOO: XOO0002(dnaN) XOO0670 XOO0763(dinP) XOO0832(holC)
                 XOO0886(holB) XOO1042(dnaQ) XOO1064(dnaX) XOO1962(dnaE1)
                 XOO3327(holA) XOO3439(dnaE2) XOO4240(polA)
            XOM: XOO_0002(XOO0002) XOO_0609(XOO0609) XOO_0693(XOO0693)
                 XOO_0758(XOO0758) XOO_0811(XOO0811) XOO_0941(XOO0941)
                 XOO_0964(XOO0964) XOO_1852(XOO1852) XOO_3140(XOO3140)
                 XOO_3239(XOO3239) XOO_4004(XOO4004)
            VCH: VC0013 VC0108 VC0299 VC0656 VC0953 VC1054 VC1212 VC1290
                 VC2015 VC2233 VC2245 VC2287 VC2502
            VCO: VC0395_A0187(holD) VC0395_A0476(holA) VC0395_A0572(dnaZX)
                 VC0395_A0831(polB) VC0395_A1601(holB) VC0395_A1825(dnaQ)
                 VC0395_A1836(dnaE) VC0395_A1876(dinP) VC0395_A2084(holC)
                 VC0395_A2409(polI) VC0395_A2506(dnaN)
            VVU: VV1_0275 VV1_0901 VV1_0998 VV1_1238 VV1_1475 VV1_1717
                 VV1_1830 VV1_1875 VV1_1887 VV1_2003 VV1_2245 VV1_2989 VV1_3001
                 VV1_3055 VV2_1003
            VVY: VV0012 VV0186 VV0909 VV1232 VV1281 VV1294 VV2101 VV2411
                 VV2529 VV2541 VV2581 VV2687 VV2908 VV3132 VVA1495
            VPA: VP0012 VP0107 VP0725 VP1724 VP1903 VP1946 VP2036 VP2048
                 VP2179 VP2292 VP2303 VP2342 VP2442 VP2645 VP2877 VPA0793
            VFI: VF0010 VF0074 VF0412 VF0498 VF0734 VF0751 VF1628 VF1687
                 VF1734 VF1935 VF1947 VF2382 VF2514 VFA0016 VFA0065 VFA0349
                 VFA0774
            PPR: PBPRA0009 PBPRA0623 PBPRA0832 PBPRA1017 PBPRA1201 PBPRA1531
                 PBPRA2517 PBPRA2887 PBPRA2917 PBPRA2953(dnaE) PBPRA3402
                 PBPRA3503 PBPRB1229(dnaQ-1)
            PAE: PA0002(dnaN) PA0669 PA0923(dinP) PA1532(dnaX) PA1816(dnaQ)
                 PA1886(polB) PA2961(holB) PA3232 PA3640(dnaE) PA3832(holC)
                 PA3989(holA) PA5493(polA)
            PAU: PA14_00020(dnaN) PA14_12200(holA) PA14_14460(holC)
                 PA14_17260(dnaE) PA14_22380 PA14_25760(holB) PA14_40120(polB)
                 PA14_41050(dnaQ) PA14_44630(dnaX) PA14_52310(dinP) PA14_55610
                 PA14_72490(polA)
            PAP: PSPA7_0002(dnaN) PSPA7_1119(holA) PSPA7_3480(dnaQ) PSPA7_3801
            PPU: PP_0011(dnaN) PP_0123(polA) PP_0979(holC) PP_1203(dinP)
                 PP_1606(dnaE) PP_1966(holB) PP_2393(polB) PP_3119
                 PP_4141(dnaQ) PP_4269(dnaX) PP_4768 PP_4796(holA)
            PPF: Pput_0002 Pput_0140 Pput_1017 Pput_1232 Pput_1599 Pput_1724
                 Pput_2598 Pput_2950 Pput_3794 Pput_4171 Pput_4643 Pput_4671
                 Pput_5030
            PST: PSPTO_0002(dnaN) PSPTO_0344(polI) PSPTO_1270(holC)
                 PSPTO_1549(dnaE) PSPTO_2621(polB) PSPTO_2795 PSPTO_3646(dnaZX)
                 PSPTO_3711(dnaQ) PSPTO_3826(holB) PSPTO_3990(dinP) PSPTO_4665
                 PSPTO_4814(holA)
            PSB: Psyr_0002 Psyr_0270 Psyr_1090(holC) Psyr_1358 Psyr_1397
                 Psyr_1653 Psyr_1764 Psyr_1825 Psyr_2361 Psyr_2523 Psyr_4300
                 Psyr_4354
            PSP: PSPPH_0002(dnaN) PSPPH_0259(polA) PSPPH_1156(holC)
                 PSPPH_1647(holB) PSPPH_1715(dnaQ) PSPPH_1785(dnaZX)
                 PSPPH_2495(polB) PSPPH_2680 PSPPH_3785(dinP) PSPPH_3825(dnaE)
                 PSPPH_4357 PSPPH_4396(holA)
            PFL: PFL_0002(dnaN) PFL_0082(polA) PFL_1065(holC) PFL_1191(dnaE)
                 PFL_1254(dinP) PFL_1802(holB) PFL_1904(dnaX) PFL_2480(polB)
                 PFL_3294(dnaQ) PFL_3697 PFL_5412 PFL_5441(holA)
            PFO: Pfl_0002 Pfl_0056 Pfl_0988(holC) Pfl_1116 Pfl_1195 Pfl_1805
                 Pfl_2187 Pfl_3149 Pfl_3734 Pfl_4151 Pfl_4924 Pfl_4959
            PEN: PSEEN0002(dnaN) PSEEN0076(polA) PSEEN1625(holB)
                 PSEEN1788(dnaX) PSEEN2415 PSEEN3365(polB) PSEEN3558(dnaQ)
                 PSEEN4107(dinP) PSEEN4205(dnaE) PSEEN4444(holC)
                 PSEEN4815(holA)
            PMY: Pmen_0002 Pmen_0154 Pmen_1634 Pmen_1726 Pmen_1934 Pmen_2067
                 Pmen_2647 Pmen_3038 Pmen_3572 Pmen_3729 Pmen_3788
            PAR: Psyc_0002(dnaN) Psyc_0042(holC) Psyc_0378(polA)
                 Psyc_0391(dnaQ) Psyc_0574(holA) Psyc_0833(dnaQ)
                 Psyc_1055(dnaX) Psyc_1177(dnaE) Psyc_1313(holB)
            PCR: Pcryo_0004 Pcryo_0050 Pcryo_0419 Pcryo_0564 Pcryo_0855
                 Pcryo_1065 Pcryo_1214 Pcryo_1407 Pcryo_1563
            PRW: PsycPRwf_0003 PsycPRwf_1232 PsycPRwf_1391 PsycPRwf_1454
                 PsycPRwf_1923 PsycPRwf_2048
            ACI: ACIAD0002(dnaN) ACIAD0225(dinP) ACIAD0252(holC)
                 ACIAD1137(rnhA-dnaQ) ACIAD1970(dnaX) ACIAD2089(dnaE)
                 ACIAD2361(holB) ACIAD3030(polA) ACIAD3108
            ACB: A1S_0539 A1S_1465 A1S_1558
            SON: SO_0009(dnaN) SO_1114(dinP) SO_1172(holA) SO_1644(dnaE)
                 SO_1820(polB) SO_2013(dnaX) SO_2245(dnaQ-1) SO_2559(dnaQ-2)
                 SO_2612(holB) SO_3423(holC) SO_4669(polA)
            SDN: Sden_0002 Sden_0795 Sden_1185 Sden_1569 Sden_2018 Sden_2050
                 Sden_2381 Sden_2428 Sden_2866 Sden_3235 Sden_3620 Sden_3773
            SFR: Sfri_0002 Sfri_0703 Sfri_0917 Sfri_0961 Sfri_1285 Sfri_1964
                 Sfri_2204 Sfri_2239 Sfri_2407 Sfri_2629 Sfri_3453 Sfri_3943
                 Sfri_4061
            SAZ: Sama_0014 Sama_0093 Sama_1154 Sama_1250 Sama_1310 Sama_1863
                 Sama_1880 Sama_2042 Sama_2527 Sama_2584
            SBL: Sbal_0002 Sbal_0053 Sbal_0935 Sbal_1465 Sbal_1630 Sbal_2000
                 Sbal_2353 Sbal_2355 Sbal_2458 Sbal_2574 Sbal_3111 Sbal_3271
                 Sbal_3553
            SBM: Shew185_0002 Shew185_1460 Shew185_2015 Shew185_2342
                 Shew185_2344 Shew185_2451 Shew185_2615 Shew185_3313
                 Shew185_3427 Shew185_4268 Shew185_4345
            SLO: Shew_0002 Shew_0924 Shew_1580 Shew_1871 Shew_2100 Shew_2111
                 Shew_2235 Shew_2482 Shew_2620 Shew_2871 Shew_2931 Shew_3714
            SPC: Sputcn32_0002 Sputcn32_0951 Sputcn32_1363 Sputcn32_1780
                 Sputcn32_2114 Sputcn32_2213 Sputcn32_2302 Sputcn32_2865
                 Sputcn32_3906
            SSE: Ssed_0007 Ssed_0096 Ssed_1993 Ssed_2410 Ssed_2647 Ssed_2852
                 Ssed_3146 Ssed_3422 Ssed_3481
            SPL: Spea_0002 Spea_0102 Spea_1508 Spea_1924 Spea_1999 Spea_2195
                 Spea_2402 Spea_2870 Spea_3092 Spea_3145
            SHE: Shewmr4_0002 Shewmr4_0947 Shewmr4_0995 Shewmr4_1131
                 Shewmr4_1662 Shewmr4_1770 Shewmr4_2157 Shewmr4_2254
                 Shewmr4_2469 Shewmr4_2626 Shewmr4_3210 Shewmr4_3905
            SHM: Shewmr7_0002 Shewmr7_0985 Shewmr7_1060 Shewmr7_1202
                 Shewmr7_1737 Shewmr7_1848 Shewmr7_2196 Shewmr7_2234
                 Shewmr7_2326 Shewmr7_2537 Shewmr7_2693 Shewmr7_3997
            SHN: Shewana3_0010 Shewana3_0031 Shewana3_0949 Shewana3_0999
                 Shewana3_1132 Shewana3_1767 Shewana3_2251 Shewana3_2365
                 Shewana3_2446 Shewana3_2629 Shewana3_2800 Shewana3_3217
                 Shewana3_4109 Shewana3_4172
            SHW: Sputw3181_0002 Sputw3181_0045 Sputw3181_1038 Sputw3181_1082
                 Sputw3181_1271 Sputw3181_1706 Sputw3181_1796 Sputw3181_1898
                 Sputw3181_2245 Sputw3181_2586 Sputw3181_2740 Sputw3181_3225
            ILO: IL0002(dnaN) IL0025(polA) IL0204(dinP) IL0949(holA)
                 IL1335(holB) IL1420 IL1689(dnaE_1) IL1693(dnaQ) IL1849(dnaX)
                 IL1949(holC) IL2566(dnaE_2)
            CPS: CPS_0002(dnaN) CPS_0739(holC) CPS_0780 CPS_1040(dinB)
                 CPS_1570(dnaE) CPS_1720(holA) CPS_2255(dnaQ) CPS_2273(polB)
                 CPS_2303(holB) CPS_3744(dnaX) CPS_4955 CPS_4978(polA)
            PHA: PSHAa0002(dnaN) PSHAa0589 PSHAa1029(holA) PSHAa1201 PSHAa1435
                 PSHAa1714(rarA) PSHAa1802(holB) PSHAa1963(dnaQ) PSHAa1990
                 PSHAa2015(dnaE) PSHAa2389(dinB) PSHAa2424(holC)
                 PSHAa2757(polA)
            PAT: Patl_0002 Patl_0015 Patl_0460 Patl_1264 Patl_1564 Patl_2116
                 Patl_2344 Patl_2348 Patl_2364 Patl_2897 Patl_3563 Patl_3630
            SDE: Sde_0002 Sde_0073 Sde_1028 Sde_1106 Sde_1335 Sde_1371
                 Sde_1511 Sde_1652 Sde_2021 Sde_2507 Sde_3310 Sde_3411
            PIN: Ping_0495 Ping_1095 Ping_1189 Ping_1342 Ping_1857 Ping_1885
                 Ping_2277 Ping_2961 Ping_3185 Ping_3715
            MAQ: Maqu_0002 Maqu_0541 Maqu_0916 Maqu_0973 Maqu_1533 Maqu_1574
                 Maqu_1613 Maqu_2332 Maqu_2746 Maqu_4000
            CBU: CBU_0002(dnaN) CBU_0280(dinP) CBU_0317(dnaQ) CBU_0500(holB)
                 CBU_0557(holA) CBU_0659(dnaZX) CBU_1337(dnaE) CBU_1795(polI)
            CBD: COXBU7E912_0002(dnaN) COXBU7E912_0021(polA)
                 COXBU7E912_0669(dnaX) COXBU7E912_1426(dnaE)
                 COXBU7E912_1508(holA) COXBU7E912_1576(holB)
                 COXBU7E912_1761(dnaQ)
            LPN: lpg0002 lpg0099(polI) lpg0262 lpg0554(dinP) lpg0962(dnaE)
                 lpg1346(holA) lpg1384(dnaQ) lpg1400(holB) lpg2632(holC)
                 lpg2754(dnaZX)
            LPF: lpl0002(dnaN) lpl0099(polA) lpl0314 lpl0597(dinP)
                 lpl0991(dnaE) lpl1299(holA) lpl1335(dnaQ) lpl1351
                 lpl2557(holC) lpl2671(dnaX)
            LPP: lpp0002(dnaN) lpp0113(polA) lpp0333 lpp0614(dinP)
                 lpp1024(dnaE) lpp1300(holA) lpp1339(dnaQ) lpp1355
                 lpp2685(holC) lpp2802(dnaX)
            MCA: MCA0720(dnaQ) MCA1286(dnaE) MCA1328(dnaZX) MCA1451(holA)
                 MCA1995(holB) MCA2098 MCA2164 MCA2276 MCA2573(polI)
                 MCA3032(dnaN)
            FTU: FTT0002(dnaN) FTT0111(polA) FTT0190c(dnaX) FTT0197c(holA)
                 FTT0298(holC) FTT0402(dnaE) FTT0460(holB) FTT0548(dnaQ)
            FTF: FTF0002(dnaN) FTF0111(polA) FTF0190c(dnaX) FTF0197c(holA)
                 FTF0298(holC) FTF0402(dnaE) FTF0460(holB) FTF0548(dnaQ)
            FTW: FTW_0002(dnaN) FTW_0196(polA) FTW_0993(dnaQ) FTW_1610
                 FTW_1672(dnaE) FTW_1787(holC) FTW_1894(holA) FTW_1901(dnaX)
            FTL: FTL_0002 FTL_0209 FTL_0472 FTL_0981 FTL_1003 FTL_1604
                 FTL_1666 FTL_1898 FTL_1905
            FTH: FTH_0002(dnaN) FTH_0204(holC) FTH_0469(dnaE) FTH_0960(dinB)
                 FTH_0980(dnaQ) FTH_1550(holB) FTH_1607(polA) FTH_1820(holA)
                 FTH_1828(dnaX)
            FTA: FTA_0003(dnaN) FTA_0498 FTA_1057(dnaQ) FTA_1763
                 FTA_2005(holA)
            FTN: FTN_0002(dnaN) FTN_0166(dnaX) FTN_0173(holA) FTN_0213(holC)
                 FTN_0499(dnaE) FTN_0551(holB) FTN_0968(dnaQ) FTN_0986(dinP)
                 FTN_1604(polA)
            TCX: Tcr_0002 Tcr_0044 Tcr_0481 Tcr_0529 Tcr_0719 Tcr_0859
                 Tcr_0930 Tcr_1115 Tcr_1120 Tcr_1749
            NOC: Noc_0002 Noc_0288(holC) Noc_0554 Noc_0636 Noc_0846 Noc_1085
                 Noc_1659 Noc_2515 Noc_2593 Noc_2663 Noc_2814
            AEH: Mlg_0002 Mlg_0402 Mlg_0552 Mlg_0557 Mlg_0668 Mlg_1175
                 Mlg_1415 Mlg_1510 Mlg_1849 Mlg_1991 Mlg_2006 Mlg_2053 Mlg_2775
                 Mlg_2860
            HHA: Hhal_0007 Hhal_0232 Hhal_0262 Hhal_0463 Hhal_0682 Hhal_1226
                 Hhal_1279 Hhal_1453 Hhal_1867 Hhal_1902 Hhal_2143 Hhal_2421
            HCH: HCH_00003(dnaN) HCH_01557(polB) HCH_01861(dnaE1)
                 HCH_01930(holC) HCH_02200(dnaE2) HCH_02528(dnaQ)
                 HCH_02613(dnaX) HCH_02670(holB) HCH_04322(dinP)
                 HCH_05357(holA) HCH_06350
            CSA: Csal_0002 Csal_0548 Csal_0578 Csal_1335 Csal_1369 Csal_1458
                 Csal_1607 Csal_1941 Csal_2071 Csal_2346 Csal_2921
            ABO: ABO_0002(dnaN) ABO_0386(alg44) ABO_0494(holC) ABO_0659(dinP)
                 ABO_1075(holB) ABO_1158(dnaE) ABO_1225(dnaQ) ABO_1775(dnaX)
                 ABO_1949(holA) ABO_2156 ABO_2659(polA)
            MMW: Mmwyl1_0002 Mmwyl1_0280 Mmwyl1_1287 Mmwyl1_1705 Mmwyl1_1982
                 Mmwyl1_2266 Mmwyl1_2534 Mmwyl1_2917 Mmwyl1_3784
            AHA: AHA_0002(dnaN) AHA_0196(polA) AHA_1145(dinB) AHA_1188(dnaE)
                 AHA_1570(dnaQ) AHA_2058 AHA_2107(polB) AHA_2211(dnaX)
                 AHA_2257(holB) AHA_3250(holA) AHA_3701
            DNO: DNO_0002(dnaN) DNO_0206(polA) DNO_0244(holA) DNO_0457(holC)
                 DNO_0688(dnaE) DNO_0906(dnaQ) DNO_0955(dnaX)
            BCI: BCI_0114(polA) BCI_0115(dnaX) BCI_0132(dnaN) BCI_0233(holA)
                 BCI_0286(holC) BCI_0430(holB) BCI_0473(dnaQ) BCI_0538(dnaE)
                 BCI_0625(holD)
            CRP: CRP_023 CRP_087
            RMA: Rmag_0002 Rmag_0078 Rmag_0134 Rmag_0404 Rmag_0466 Rmag_0803
            VOK: COSY_0002(dnaN) COSY_0084(polA) COSY_0136(holA)
                 COSY_0215(holB) COSY_0375(dnaQ) COSY_0431(dnaX)
                 COSY_0728(dnaE)
            NME: NMB0708 NMB0769 NMB1443(dnaX) NMB1448 NMB1451 NMB1514 NMB1568
                 NMB1827 NMB1873 NMB1902 NMB1982
            NMA: NMA0462(polA) NMA0553(dnaN) NMA0583 NMA0632(dnaE)
                 NMA0913(holA) NMA0980(holB) NMA1656(dnaZX) NMA1661 NMA1665
                 NMA1714(dnaQ) NMA1757(holC)
            NMC: NMC0321(dnaN) NMC0389(dnaE) NMC0658(holA) NMC0722(holB)
                 NMC1379(dnaZX) NMC1443(dnaQ) NMC1488(holC) NMC1957(polA)
            NGO: NGO0002 NGO0030 NGO0078 NGO0283 NGO0347 NGO0738 NGO0743
                 NGO0973 NGO1226(holC) NGO2103(polA)
            CVI: CV_0002(dnaN) CV_0507(holA) CV_0779(polA) CV_0911(dnaE)
                 CV_1020 CV_1257(dnaQ) CV_1610(dnaX) CV_2751 CV_2913(holC)
                 CV_2946 CV_3454 CV_3722(holB) CV_4363(dinP)
            RSO: RSc1191(dnaX) RSc1369(RS04652) RSc1587(dinP) RSc1785(holB)
                 RSc1872(dnaQ) RSc2205(dnaE1) RSc2230(polA) RSc2414(holC)
                 RSc2742(holA) RSc3441(dnaN) RSp0800(dnaE2)
            REU: Reut_A0002 Reut_A0873 Reut_A1435 Reut_A1937 Reut_A2112
                 Reut_A2190 Reut_A2534 Reut_A2682(holC) Reut_A2832 Reut_A3394
                 Reut_B3616 Reut_B4396 Reut_B4523 Reut_B4584
            REH: H16_A0002(dnaN) H16_A0900(dnaE1) H16_A1570(holB)
                 H16_A1651(polB) H16_A2116 H16_A2389(dnaX) H16_A2467(dnaQ)
                 H16_A2741(polA) H16_A2989(holC) H16_A3137(holA)
                 H16_A3686(dinP) H16_B1062(dnaE2)
            RME: Rmet_0002 Rmet_0754 Rmet_1397 Rmet_1645 Rmet_1827 Rmet_2129
                 Rmet_2209 Rmet_2624 Rmet_2806 Rmet_2971 Rmet_3545 Rmet_3922
                 Rmet_4130
            BMA: BMA0002(dnaN) BMA0673 BMA0762(dnaQ) BMA1361 BMA1424(holB)
                 BMA1580 BMA1727(dinB) BMA1913(dnaE1) BMA2451(holA)
                 BMA3145(dnaE2) BMAA0319(polA)
            BMV: BMASAVP1_1500(polA) BMASAVP1_A0114(dnaE2)
                 BMASAVP1_A0368(holA) BMASAVP1_A1044(dnaE1)
                 BMASAVP1_A1272(dnaQ) BMASAVP1_A1851 BMASAVP1_A1915(holB)
                 BMASAVP1_A2236(dinB) BMASAVP1_A2338 BMASAVP1_A2849(dnaN)
            BML: BMA10299_1696(polA) BMA10299_A0597(dnaQ)
                 BMA10299_A0824(dnaE1) BMA10299_A1227(holA)
                 BMA10299_A1474(dnaE2) BMA10299_A2236(dnaN) BMA10299_A2948
                 BMA10299_A3083(dinB) BMA10299_A3389(holB)
            BMN: BMA10247_0002(dnaN) BMA10247_0327(dnaE-2) BMA10247_0555(dnaQ)
                 BMA10247_1123(dnaX) BMA10247_1188(holB) BMA10247_1508(dinB)
                 BMA10247_1652(holC) BMA10247_2638(holA) BMA10247_2902(dnaE-1)
                 BMA10247_A0353(polA)
            BXE: Bxe_A0578 Bxe_A0914 Bxe_A1250 Bxe_A1656 Bxe_A2262 Bxe_A2361
                 Bxe_A3164 Bxe_A3292 Bxe_A3637 Bxe_A4461 Bxe_B0404 Bxe_B0929
                 Bxe_B2067 Bxe_B2228 Bxe_B2834
            BVI: Bcep1808_0002 Bcep1808_0624 Bcep1808_0926 Bcep1808_1237
                 Bcep1808_1754 Bcep1808_1816 Bcep1808_2007 Bcep1808_2222
                 Bcep1808_2402 Bcep1808_2930 Bcep1808_3849 Bcep1808_4248
                 Bcep1808_7142
            BUR: Bcep18194_A3183 Bcep18194_A3742 Bcep18194_A4080
                 Bcep18194_A4114 Bcep18194_A4426 Bcep18194_A5128
                 Bcep18194_A5192 Bcep18194_A5296 Bcep18194_A5352
                 Bcep18194_A5448 Bcep18194_A5655 Bcep18194_A5796(holC)
                 Bcep18194_A6156 Bcep18194_B2218 Bcep18194_B3002
                 Bcep18194_C6768
            BCN: Bcen_0173 Bcen_0528 Bcen_0803 Bcen_1701 Bcen_1854 Bcen_2213
                 Bcen_2554 Bcen_4493 Bcen_5012 Bcen_5935 Bcen_6034 Bcen_6094
                 Bcen_6187 Bcen_6252
            BCH: Bcen2424_0002 Bcen2424_0656 Bcen2424_1006 Bcen2424_1284
                 Bcen2424_1827 Bcen2424_1892 Bcen2424_1983 Bcen2424_2043
                 Bcen2424_2142 Bcen2424_2313 Bcen2424_2465 Bcen2424_2826
                 Bcen2424_3872 Bcen2424_5848 Bcen2424_6465 Bcen2424_6832
                 Bcen2424_6871
            BAM: Bamb_0002 Bamb_0551 Bamb_0866 Bamb_1161 Bamb_1765 Bamb_1829
                 Bamb_2075 Bamb_2179 Bamb_2352 Bamb_2514 Bamb_2886 Bamb_3243
                 Bamb_4910 Bamb_5084
            BPS: BPSL0074(dnaN) BPSL0472 BPSL0966 BPSL1117(dnaE)
                 BPSL1341(dnaQ) BPSL1437 BPSL1498(dnaX) BPSL2183 BPSL2306
                 BPSL2556 BPSL2936 BPSS1770(polA) BPSS2233
            BPM: BURPS1710b_0300(dnaN) BURPS1710b_0692(dnaE2)
                 BURPS1710b_1177(holC) BURPS1710b_1355(dnaE)
                 BURPS1710b_1356(dnaE) BURPS1710b_1599(dnaQ)
                 BURPS1710b_2373(dnaX) BURPS1710b_2442(holB) BURPS1710b_2607
                 BURPS1710b_2751(dinB) BURPS1710b_3040(cho)
                 BURPS1710b_3449(holA) BURPS1710b_A0851(polA) BURPS1710b_A1364
            BPL: BURPS1106A_0102(dnaN) BURPS1106A_0527(dnaE)
                 BURPS1106A_1023(holC) BURPS1106A_1206(dnaE)
                 BURPS1106A_1495(dnaQ) BURPS1106A_2244(dnaX)
                 BURPS1106A_2319(holB) BURPS1106A_2675(dinB) BURPS1106A_3006
                 BURPS1106A_3448(holA) BURPS1106A_A2403(polA)
            BPD: BURPS668_0088(dnaN) BURPS668_0510(dnaE) BURPS668_1016(holC)
                 BURPS668_1197(dnaE) BURPS668_1465(dnaQ) BURPS668_2206(dnaX)
                 BURPS668_2280(holB) BURPS668_2619(dinB) BURPS668_2940
                 BURPS668_3413(holA) BURPS668_A2546(polA)
            BTE: BTH_I0445(dnaE) BTH_I0824 BTH_I0984 BTH_I1213 BTH_I1595
                 BTH_I1859 BTH_I2003 BTH_I2155 BTH_I2219 BTH_I2791(dnaQ)
                 BTH_I3240(dnaN) BTH_II0605
            PNU: Pnuc_0002 Pnuc_0234 Pnuc_0606 Pnuc_0700 Pnuc_0705 Pnuc_0965
                 Pnuc_1027 Pnuc_1711
            BPE: BP0406(dnaQ) BP0490(dnaN) BP0909(dinP) BP1254(polA)
                 BP1549(dnaX) BP1848(holB) BP2042(holA) BP2332(dnaE) BP2422
                 BP3556
            BPA: BPP1221(dnaX) BPP1560(holB) BPP1635(dinP) BPP1640
                 BPP1707(dnaE) BPP1729(holA) BPP1869(polA) BPP3286 BPP3357
                 BPP3831(dnaQ) BPP4400(dnaN)
            BBR: BB1438(dnaX) BB2638(holB) BB3088 BB3093(dinP) BB3239(polA)
                 BB3379(holA) BB3401(dnaE) BB3737 BB3808 BB4275(dnaQ)
                 BB4988(dnaN)
            RFR: Rfer_0002 Rfer_0187 Rfer_0760 Rfer_1227 Rfer_1325 Rfer_1457
                 Rfer_2040 Rfer_2117 Rfer_2183 Rfer_2256 Rfer_2353 Rfer_2572
                 Rfer_3777 Rfer_4311 Rfer_4341
            POL: Bpro_0002 Bpro_0009 Bpro_1729 Bpro_2184 Bpro_2268 Bpro_2388
                 Bpro_2409 Bpro_2518 Bpro_2893 Bpro_3696 Bpro_4151 Bpro_4600
                 Bpro_4619
            PNA: Pnap_1478 Pnap_1670 Pnap_1949 Pnap_2284 Pnap_2925 Pnap_3159
                 Pnap_3769 Pnap_4118 Pnap_4120 Pnap_4896
            AAV: Aave_0002 Aave_0016 Aave_0518 Aave_1930 Aave_1964 Aave_2449
                 Aave_2644 Aave_2672 Aave_2732 Aave_3240 Aave_3411 Aave_4546
            AJS: Ajs_1718 Ajs_1830 Ajs_1967 Ajs_2138 Ajs_2350 Ajs_3296
                 Ajs_3317 Ajs_3915 Ajs_4145 Ajs_4160
            VEI: Veis_0002 Veis_0511 Veis_1006 Veis_1647 Veis_1841 Veis_2379
                 Veis_4484
            MPT: Mpe_A0002 Mpe_A0049 Mpe_A0216 Mpe_A0303 Mpe_A1148 Mpe_A1234
                 Mpe_A1532 Mpe_A1859 Mpe_A1941 Mpe_A2252 Mpe_A2256 Mpe_A2534
                 Mpe_B0234 Mpe_B0619
            HAR: HEAR0003(dnaN) HEAR0269(polA) HEAR0456(dnaE) HEAR0580
                 HEAR0663 HEAR0742 HEAR1045(dnaX) HEAR1397(holB) HEAR2318(dnaQ)
                 HEAR2663(holA) HEAR3363(dinP)
            MMS: mma_0002 mma_0162 mma_0323 mma_0669(holC) mma_1212 mma_1522
                 mma_1913 mma_1985(holB) mma_2330 mma_2898(holA) mma_3585
            NEU: NE0002(dnaN) NE0141(dnaQ) NE0433(dnaX) NE0442(holC)
                 NE1137(holA) NE1219 NE1398 NE1468(polA) NE1978(dnaE1)
                 NE2180(holB)
            NET: Neut_0002 Neut_0384 Neut_0543 Neut_0590 Neut_0600 Neut_0778
                 Neut_1427 Neut_1620 Neut_2175 Neut_2575 Neut_2622
            NMU: Nmul_A0002 Nmul_A0513 Nmul_A0568 Nmul_A0745(holC) Nmul_A0949
                 Nmul_A1286 Nmul_A1386 Nmul_A1618 Nmul_A1858 Nmul_A2002
                 Nmul_A2121 Nmul_A2599 Nmul_A2731
            EBA: ebA1024(dinP) ebA1203(dnaX) ebA2847(dnaN) ebA3077(polC)
                 ebA3982(polA) ebA4383(holA) ebA4398(dnaE) ebA5417(holB)
                 ebA6456(dnaQ) ebA6487 ebA7175(holC)
            AZO: azo0002(dnaN) azo0067(polC) azo0957(dnaX) azo1596(holB)
                 azo1713 azo2054(dnaQ) azo2202 azo2249 azo2410 azo2786(dinP)
                 azo2905(holC) azo3208(dnaE1) azo3217(holA) azo3600(polA)
                 azo3948 azo3957
            DAR: Daro_0002 Daro_0163 Daro_0542 Daro_0559 Daro_0806 Daro_1381
                 Daro_1592 Daro_1907 Daro_1942 Daro_1983 Daro_2123 Daro_2196
                 Daro_3083(holC)
            TBD: Tbd_0002 Tbd_0515 Tbd_0579 Tbd_0827 Tbd_0828 Tbd_0858
                 Tbd_1481 Tbd_1542 Tbd_1662 Tbd_1723 Tbd_2443 Tbd_2453
            MFA: Mfla_0002 Mfla_0008 Mfla_0223 Mfla_0358 Mfla_0414 Mfla_1247
                 Mfla_1478 Mfla_1499 Mfla_1553 Mfla_1572 Mfla_1758 Mfla_2157
            HPY: HP0500(dnaN) HP0717(dnaX) HP1231(holB) HP1247 HP1387(dnaQ)
                 HP1460(dnaE) HP1470(polA)
            HPJ: jhp0452(dnaN) jhp0655(dnaX) jhp1152(holB) jhp1168
                 jhp1353(dnaE) jhp1363(polA) jhp1438
            HPA: HPAG1_0421 HPAG1_0425 HPAG1_0476 HPAG1_0702 HPAG1_1173
                 HPAG1_1190 HPAG1_1445 HPAG1_1455 HPAG1_1481
            HHE: HH0535 HH0620(holB) HH1077(dnaX) HH1126(dnaN) HH1270(dnaE)
                 HH1317(polA) HH1347(dnaQ)
            HAC: Hac_0124(dnaE) Hac_0246(dnaX) Hac_0821(dnaN) Hac_0940(dnaX)
                 Hac_1064 Hac_1126(polA) Hac_1644(holB) Hac_1719(polA)
                 Hac_1778(dnaQ)
            WSU: WS0001(dnaN) WS0221 WS0430(polA) WS0596 WS1731 WS1874
                 WS1983(dnaE) WS2096(dnaX)
            TDN: Tmden_0002 Tmden_0542 Tmden_0559 Tmden_0910 Tmden_0963
                 Tmden_1244 Tmden_1452 Tmden_1557 Tmden_1607 Tmden_1648
                 Tmden_1790 Tmden_1840
            CJE: Cj0002(dnaN) Cj0338c(polA) Cj0452(dnaQ) Cj0584 Cj0630c
                 Cj0718(dnaE) Cj0963 Cj1157(dnaX)
            CJR: CJE0002(dnaN) CJE0383(polA) CJE0502 CJE0687 CJE0733
                 CJE0818(dnaE) CJE1043 CJE1293(dnaX)
            CJJ: CJJ81176_0028(dnaN) CJJ81176_0360(polA) CJJ81176_0741(dnaE)
                 CJJ81176_1174(dnaX)
            CJU: C8J_0002(dnaN) C8J_0315(polA) C8J_0425(dnaQ) C8J_0546
                 C8J_0589 C8J_0685(dnaE) C8J_0905 C8J_1103(dnaX)
            CJD: JJD26997_0002(dnaN) JJD26997_0571(dnaX) JJD26997_1288(dnaE)
                 JJD26997_1620(polA)
            CFF: CFF8240_0002(dnaN) CFF8240_0229 CFF8240_0419 CFF8240_1238
                 CFF8240_1423
            CCV: CCV52592_0506 CCV52592_1311 CCV52592_1705(polA)
                 CCV52592_2055(dnaN)
            CHA: CHAB381_0003(dnaN) CHAB381_1255 CHAB381_1538 CHAB381_1725
            CCO: CCC13826_0930 CCC13826_1448 CCC13826_1851(dnaN)
            ABU: Abu_0002(dnaN) Abu_0240 Abu_0285(dnaX) Abu_0497(dnaQ1)
                 Abu_0503(dnaQ2) Abu_0858(dnaQ3) Abu_1201(holB) Abu_1258(dnaQ4)
                 Abu_1270(polA) Abu_1492(dinP) Abu_2262(dnaE)
            NIS: NIS_0002(dnaN) NIS_0279 NIS_0522 NIS_0678(dnaE) NIS_1138
                 NIS_1188(polA) NIS_1457
            SUN: SUN_0002(dnaN) SUN_0458 SUN_0567(dnaE) SUN_1149(dnaQ)
                 SUN_1315(polA) SUN_1378 SUN_2046(dnaX)
            GSU: GSU0001(dnaN) GSU0043 GSU0094(dnaX) GSU0541(polA) GSU1126
                 GSU1383 GSU1401(dnaE) GSU1616 GSU2207 GSU2230(holB)
            GME: Gmet_0002 Gmet_1215 Gmet_1441 Gmet_2298 Gmet_2319 Gmet_2671
                 Gmet_2983 Gmet_3055 Gmet_3422
            GUR: Gura_0002 Gura_1132 Gura_2507 Gura_3154 Gura_3902 Gura_4327
            PCA: Pcar_0002 Pcar_0374 Pcar_0592 Pcar_1222 Pcar_1415 Pcar_1548
                 Pcar_1692 Pcar_2009 Pcar_2613 Pcar_3129
            PPD: Ppro_0002 Ppro_0190 Ppro_0301 Ppro_1574 Ppro_1664 Ppro_1904
                 Ppro_2068 Ppro_2346
            DVU: DVU0002(dnaN) DVU0071(dinP) DVU0443 DVU0496(polA) DVU1194
                 DVU1353(dnaE) DVU3198 DVU3203
            DVL: Dvul_0006 Dvul_0189 Dvul_0459 Dvul_1715 Dvul_2445 Dvul_2890
            DDE: Dde_0002 Dde_0066 Dde_0177 Dde_0628 Dde_2196 Dde_2441
                 Dde_2973 Dde_3450 Dde_3621
            LIP: LI0011(polB) LI0102(polB) LI0150 LI0257(dnaE) LI0786(dnaN)
                 LI0916(dnaX)
            BBA: Bd0002(dnaN) Bd0254(uvrC) Bd0349(dinP) Bd0384(dnaE)
                 Bd0802(polA) Bd1041(holB) Bd1464 Bd2078(dnaE) Bd2140(polC)
                 Bd3251(polC) Bd3731(dnaX) Bd3834(polC)
            DPS: DP0648 DP0784 DP0965 DP1087 DP1431 DP1663 DP1760 DP2198
            ADE: Adeh_0002 Adeh_0141 Adeh_1181 Adeh_1310 Adeh_1312 Adeh_1313
                 Adeh_1612 Adeh_2370 Adeh_3445 Adeh_3637 Adeh_3694
            AFW: Anae109_0002 Anae109_0145 Anae109_2451 Anae109_2455
                 Anae109_3247 Anae109_3552 Anae109_3762
            MXA: MXAN_0236(dnaN) MXAN_1933 MXAN_2546 MXAN_2800(holB)
                 MXAN_2801(holA) MXAN_3109(polA) MXAN_3982(dnaE)
                 MXAN_5844(dnaE)
            SAT: SYN_00163 SYN_00561 SYN_00896 SYN_01765 SYN_02012 SYN_02050
                 SYN_02261
            SFU: Sfum_0156 Sfum_0466 Sfum_0738 Sfum_0928 Sfum_0929 Sfum_1224
                 Sfum_1225 Sfum_1612 Sfum_2086 Sfum_2688 Sfum_2789
            RPR: RP172(holB) RP189 RP419(dnaN) RP732(dnaQ) RP776(polA)
                 RP778(dnaE) RP845 RP865(dnaX) RP872
            RTY: RT0163(holB) RT0179 RT0405(dnaN) RT0718(dnaQ) RT0763(polA)
                 RT0765(dnaE) RT0833 RT0855(dnaX) RT0856(dnaX) RT0863(holC)
            RCO: RC0213(holB) RC0238 RC0583(dnaN) RC1112(dnaQ) RC1206(polA)
                 RC1211(dnaE) RC1309 RC1336(dnaX) RC1346
            RFE: RF_0176(dnaQ) RF_0649(dnaN) RF_1078(holA) RF_1107(holB)
                 RF_1239(polA) RF_1244(dnaE) RF_1364(dnaX) RF_1375
            RBE: RBE_0047(dnaX) RBE_0074(dnaE) RBE_0362(dnaQ) RBE_0656(dnaN)
                 RBE_1106(holA) RBE_1148(holB) RBE_1207(polA) RBE_1421(holC)
            RAK: A1C_01225 A1C_03150 A1C_06050(dnaE) A1C_06700
            RBO: A1I_00665 A1I_01540 A1I_04260 A1I_07575(dnaE)
            RCM: A1E_01035 A1E_04995(dnaE) A1E_05420 A1E_05545
            RRI: A1G_01210 A1G_03290 A1G_06640(dnaE) A1G_07305
            OTS: OTBS_0002(dnaN) OTBS_0272(dnaE) OTBS_1022(polA)
                 OTBS_1217(dnaQ) OTBS_1912(dnaX)
            WOL: WD0108(dnaQ) WD0164 WD0364 WD0780(dnaE) WD0819 WD1003(polA)
                 WD1060(dnaX) WD1067(dnaN)
            WBM: Wbm0115 Wbm0176 Wbm0429 Wbm0434 Wbm0499 Wbm0543 Wbm0639(holB)
                 Wbm0725(polA)
            AMA: AM1014(dnaN) AM1185 AM1214(polA) AM1237 AM1280(dnaZ)
                 AM287(dnaE) AM435 AM625(dnaQ)
            APH: APH_0001(polA) APH_0730(dnaQ) APH_0783 APH_1003(dnaE)
                 APH_1097(dnaN) APH_1252(holA) APH_1348(dnaX)
            ERU: Erum0040(dnaZ) Erum0481 Erum0482 Erum0490(polA) Erum0870
                 Erum1870(dnaE) Erum2940(holB) Erum4990(dnaQ) Erum7880(dnaN)
            ERW: ERWE_CDS_00390(polA) ERWE_CDS_00440 ERWE_CDS_00830
                 ERWE_CDS_01870(dnaE) ERWE_CDS_03000(dnaX) ERWE_CDS_05220(dnaQ)
                 ERWE_CDS_08330(dnaN) ERWE_CDS_09490(dnaX)
            ERG: ERGA_CDS_00380(polA) ERGA_CDS_00800 ERGA_CDS_01820(dnaE)
                 ERGA_CDS_05130(dnaQ) ERGA_CDS_08230(dnaN) ERGA_CDS_09410(dnaX)
            ECN: Ecaj_0048 Ecaj_0077 Ecaj_0187 Ecaj_0275 Ecaj_0506 Ecaj_0815
                 Ecaj_0942
            ECH: ECH_0014(dnaX) ECH_0074 ECH_0080(polA) ECH_0126 ECH_0803
                 ECH_0922(dnaE) ECH_1009(dnaN) ECH_1010
            NSE: NSE_0167(dnaE) NSE_0170(dnaN) NSE_0470(dnaQ) NSE_0492
                 NSE_0675(polA)
            PUB: SAR11_0107 SAR11_0200(polA) SAR11_0339(dnaQ) SAR11_0355(holA)
                 SAR11_0411(dnaN) SAR11_0507(dnaX) SAR11_0634(umuC)
                 SAR11_0906(dnaE) SAR11_1000(holB)
            MLO: mll0423 mll0870 mll5147 mll5580 mll7705 mll9709 mlr0866
                 mlr1877 mlr3298 mlr4428 mlr4475 mlr4495 mlr5503 mlr7869
            MES: Meso_0002 Meso_0909 Meso_1255 Meso_1582 Meso_1755 Meso_2502
                 Meso_3263 Meso_3317 Meso_3482 Meso_3809 Meso_3945 Meso_4057
            PLA: Plav_0004 Plav_0105 Plav_0255 Plav_1251 Plav_2531 Plav_2809
                 Plav_3197
            SME: SMa0892(dnaE3) SMa2355 SMb21448 SMc00415(dnaN) SMc00586
                 SMc01190 SMc01373(dinP) SMc01375(dnaE1) SMc02375
                 SMc02789(dnaQ) SMc02802 SMc02850(polA) SMc02905(dnaX)
                 SMc03788(dnaE2)
            SMD: Smed_0921 Smed_0923 Smed_3021 Smed_3213 Smed_3381 Smed_3432
                 Smed_3543 Smed_5353
            ATU: Atu0005(dnaQ) Atu0096 Atu0110(polA) Atu0301(dnaN) Atu0987
                 Atu1111 Atu1292(dnaE) Atu1294(dinP) Atu1497(holB) Atu2077
                 Atu2180 Atu2750 Atu3228(dnaE) Atu5100(dnaE) Atu5469(dinP)
                 Atu6093(dnaE)
            ATC: AGR_C_147(dnaX) AGR_C_169 AGR_C_1810 AGR_C_2056 AGR_C_2379
                 AGR_C_2382 AGR_C_2759 AGR_C_3764 AGR_C_3961 AGR_C_4988
                 AGR_C_520 AGR_C_7 AGR_L_3173 AGR_pAT_692 AGR_pAT_bx5
                 AGR_pTi_175
            RET: RHE_CH00005(dnaQ) RHE_CH00126(dnaX) RHE_CH00151(polA)
                 RHE_CH00318(dnaN) RHE_CH01302 RHE_CH01457 RHE_CH01627(dnaEch1)
                 RHE_CH01629(dinP) RHE_CH02159(holB) RHE_CH02833 RHE_CH02967
                 RHE_CH04083(dnaEch2) RHE_CH04118 RHE_PE00232
                 RHE_PE00402(ype00209) RHE_PF00149(dinB) RHE_PF00152(dnaEf)
            RLE: RL0005 RL0134(dnaX) RL0160(polA) RL0334(dnaN) RL1451 RL1572
                 RL1723(dnaE) RL1725 RL2117(dnaE) RL2475(holB) RL3291 RL3420
                 RL4697(dnaE) RL4698 RL4734 pRL100039 pRL110312 pRL110533
            BME: BMEI0011 BMEI0988 BMEI1137 BMEI1260 BMEI1321 BMEI1825
                 BMEI1876 BMEI1908 BMEI1942 BMEI2056 BMEII0290 BMEII0650
                 BMEII0656
            BMF: BAB1_0002(dnaN) BAB1_0031 BAB1_0066 BAB1_0120 BAB1_0644
                 BAB1_0711 BAB1_0845 BAB1_1012 BAB1_2058 BAB1_2072(dnaQ)
                 BAB2_0617 BAB2_0625
            BMS: BR0002(dnaN) BR0034(dnaX) BR0069(dnaE-1) BR0123(polA) BR0620
                 BR0690 BR0825(dnaE-2) BR0993 BR2057 BR2071(dnaQ) BRA0615
                 BRA0626
            BMB: BruAb1_0002(dnaN) BruAb1_0034(dnaX) BruAb1_0069(dnaE-1)
                 BruAb1_0120(polA) BruAb1_0639 BruAb1_0709 BruAb1_0839(dnaE-2)
                 BruAb1_0999 BruAb1_2032 BruAb1_2046(dnaQ) BruAb2_0600
                 BruAb2_0610
            BOV: BOV_0002(dnaN) BOV_0119(polA) BOV_0819(dnaE-2) BOV_1977(holA)
                 BOV_1991(dnaQ)
            OAN: Oant_0004 Oant_0021 Oant_0079 Oant_0137 Oant_0849 Oant_2282
                 Oant_2402 Oant_3147 Oant_3681
            BJA: bll0829(dnaN) bll0861(dinP) bll2523 bll3023 bll4517
                 bll4866(dnaE) bll8116 blr0629 blr0640(dnaQ) blr3026(dnaE)
                 blr4109 blr4117 blr5126 blr8131(polA)
            BRA: BRADO0002(dnaN) BRADO0202(dnaQ) BRADO0752(polA) BRADO0763
                 BRADO1464(dinB) BRADO2019 BRADO2646 BRADO2647(dnaE2) BRADO3329
                 BRADO3828 BRADO4145(dnaE) BRADO4523(dinB)
            BBT: BBta_0002(dnaN) BBta_0158(dnaQ) BBta_1442 BBta_2345 BBta_2986
                 BBta_2987(dnaE2) BBta_3265(dinB) BBta_3833 BBta_4101
                 BBta_4522(dnaE) BBta_4749(dinB) BBta_7346 BBta_7357(polA)
            RPA: RPA0002(dnaN) RPA0289 RPA0301(dnaQ) RPA0615(dnaX)
                 RPA1036(polN) RPA1799(ung) RPA1803(dnaE2) RPA2776
                 RPA2924(dnaE) RPA3059 RPA3135(dinP) RPA4723(polA)
            RPB: RPB_0002 RPB_0387 RPB_0398 RPB_0668 RPB_0848 RPB_1083
                 RPB_2410 RPB_2482(holC) RPB_2601 RPB_2680 RPB_3563
            RPC: RPC_0002 RPC_0286 RPC_0297 RPC_1733 RPC_2315 RPC_2433
                 RPC_2704 RPC_3311 RPC_4359 RPC_4848 RPC_4857
            RPD: RPD_0002 RPD_0087 RPD_0423 RPD_0434 RPD_0956 RPD_1210
                 RPD_1899 RPD_1903 RPD_2716 RPD_2858 RPD_2964 RPD_3041 RPD_3636
            RPE: RPE_0002 RPE_0377 RPE_0388 RPE_1823 RPE_1827 RPE_2550
                 RPE_2866 RPE_3290 RPE_3388 RPE_4422 RPE_4813 RPE_4821
            NWI: Nwi_0002 Nwi_0093 Nwi_0105 Nwi_0357 Nwi_0369 Nwi_1429
                 Nwi_1463 Nwi_1675 Nwi_1860 Nwi_2255 Nwi_2259 Nwi_2261 Nwi_2596
                 Nwi_2860
            NHA: Nham_0002 Nham_0100 Nham_0115 Nham_0453 Nham_0462 Nham_1693
                 Nham_2009 Nham_2338 Nham_2445 Nham_2666 Nham_3219 Nham_3765
                 Nham_4004
            BHE: BH00050(dnaQ) BH00060(polA) BH01190(dnaN) BH02320(dnaX)
                 BH04850 BH05460 BH08470(dnaC) BH09850(dnaE) BH16220
            BQU: BQ00050(dnaQ) BQ00060(polA) BQ01120(dnaN) BQ02200(dnaX)
                 BQ04050 BQ04640 BQ06100(dnaC) BQ07620(dnaE) BQ13150
            BBK: BARBAKC583_0002(polA) BARBAKC583_0004(dnaQ)
                 BARBAKC583_0050(holA) BARBAKC583_0509(holC)
                 BARBAKC583_0821(holB) BARBAKC583_0872(dnaE)
                 BARBAKC583_1238(dnaX) BARBAKC583_1278(dnaN)
            XAU: Xaut_0002 Xaut_0808 Xaut_1831 Xaut_2168 Xaut_2377 Xaut_2426
                 Xaut_3468 Xaut_3857 Xaut_4284 Xaut_4326
            CCR: CC_0005 CC_0156 CC_0267 CC_1333 CC_1693 CC_1823 CC_1926
                 CC_2333 CC_2466 CC_3211 CC_3464 CC_3751
            SIL: SPO0150(dnaN) SPO0656(dnaE) SPO0670 SPO2452 SPO2741 SPO3280
                 SPO3434 SPO3550(dnaX) SPO3844(polA) SPO3889(dnaQ)
            SIT: TM1040_0002 TM1040_0043 TM1040_0127 TM1040_0166 TM1040_0175
                 TM1040_0500 TM1040_0951 TM1040_2764 TM1040_2858 TM1040_3061
                 TM1040_3592 TM1040_3669
            RSP: RSP_0674 RSP_0710(dnaX) RSP_0838 RSP_1001 RSP_1028
                 RSP_1123(dnaE) RSP_1236(dnaQ) RSP_1343 RSP_1400 RSP_2232
                 RSP_2898 RSP_3553(dnaE)
            RSH: Rsph17029_0012 Rsph17029_0068 Rsph17029_2225 Rsph17029_2328
                 Rsph17029_2365 Rsph17029_2689 Rsph17029_2785 Rsph17029_2897
                 Rsph17029_3236
            RSQ: Rsph17025_0003 Rsph17025_0200 Rsph17025_0503 Rsph17025_0521
                 Rsph17025_2673 Rsph17025_2808
            JAN: Jann_0002 Jann_0194 Jann_0409 Jann_0940 Jann_1276 Jann_1558
                 Jann_1683 Jann_1816 Jann_3876 Jann_3901 Jann_3995
            RDE: RD1_0052 RD1_0209(dnaN) RD1_0216 RD1_0336(dnaE)
                 RD1_0349(polA) RD1_0440(dnaQ) RD1_0719(dinB) RD1_1047(dnaX)
                 RD1_1111 RD1_3117 RD1_3425(udgA) RD1_3467 RD1_4067(dnaE)
            PDE: Pden_0342 Pden_0732 Pden_0970 Pden_1762 Pden_1853 Pden_2145
                 Pden_2815 Pden_2834 Pden_3649 Pden_4291 Pden_4556 Pden_5114
            MMR: Mmar10_0002 Mmar10_0016 Mmar10_0435 Mmar10_1228 Mmar10_1274
                 Mmar10_1378 Mmar10_1453 Mmar10_1831 Mmar10_2189 Mmar10_2959
                 Mmar10_2978
            HNE: HNE_0005(dnaQ) HNE_0372(dnaX) HNE_0563(dnaN) HNE_1412(polA)
                 HNE_1767(dnaE) HNE_1812 HNE_1908 HNE_2272 HNE_2286 HNE_2466
                 HNE_3559(holA)
            ZMO: ZMO0039(dnaQ) ZMO0227(polA) ZMO0861(dnaZX) ZMO0980(dnaN)
                 ZMO1091(holB) ZMO1308(holC) ZMO1433(holA) ZMO1538(dnaE)
            NAR: Saro_0113 Saro_0278 Saro_0639 Saro_0892 Saro_1357 Saro_1429
                 Saro_1538 Saro_1770 Saro_1940 Saro_2039 Saro_2656 Saro_3217
            SAL: Sala_0625 Sala_0708 Sala_0756 Sala_0796 Sala_1179 Sala_1258
                 Sala_1760 Sala_2780 Sala_2838 Sala_3018
            SWI: Swit_0055 Swit_0450 Swit_0485 Swit_1119 Swit_2340 Swit_2795
                 Swit_2828 Swit_3597
            ELI: ELI_03680 ELI_05385 ELI_05390 ELI_06220 ELI_06980 ELI_07330
                 ELI_08870 ELI_09915 ELI_12980 ELI_14330
            GOX: GOX0002 GOX0017(dnaC) GOX0076 GOX0136 GOX0292 GOX0412 GOX0604
                 GOX0785 GOX0844 GOX1562 GOX1724 GOX1961 GOX2598
            GBE: GbCGDNIH1_0007 GbCGDNIH1_0216 GbCGDNIH1_0261 GbCGDNIH1_0319
                 GbCGDNIH1_1076 GbCGDNIH1_1280 GbCGDNIH1_1965 GbCGDNIH1_2142
                 GbCGDNIH1_2203
            ACR: Acry_0971 Acry_1437 Acry_1504 Acry_2000 Acry_2396 Acry_2765
                 Acry_2844 Acry_3292
            RRU: Rru_A0002 Rru_A0015 Rru_A0266 Rru_A0633 Rru_A1582 Rru_A1702
                 Rru_A2660 Rru_A3473 Rru_A3514 Rru_A3530 Rru_A3611 Rru_A3629
            MAG: amb0029 amb0623 amb0637 amb2449 amb2569 amb3000 amb3674
                 amb4103 amb4211 amb4438 amb4545
            MGM: Mmc1_0002 Mmc1_0028 Mmc1_1044 Mmc1_1738 Mmc1_1869 Mmc1_2106
                 Mmc1_2675 Mmc1_3229 Mmc1_3261 Mmc1_3379 Mmc1_3405 Mmc1_3537
            ABA: Acid345_0002 Acid345_1189 Acid345_1547 Acid345_1975
                 Acid345_2356 Acid345_2747 Acid345_3354 Acid345_3775
                 Acid345_4047 Acid345_4479
            SUS: Acid_0002 Acid_0012 Acid_0850 Acid_1347 Acid_3165 Acid_7035
            BSU: BG10066(dnaN) BG10083(dnaX) BG10095(holB) BG10263(polC)
                 BG11642(yqeN) BG11737(yqjH) BG11752(yqjW) BG12583(dnaE)
                 BG12656(polA) BG13696(yorL)
            BHA: BH0002(dnaN) BH0034(dnaX) BH0044(holB) BH1337 BH1472
                 BH2418(polC) BH2741 BH3153(polA) BH3169(dnaE)
            BAN: BA0002(dnaN-1) BA0019(dnaX) BA0028(holB) BA1552
                 BA2684(dnaN-2) BA3672 BA3955(polC) BA4366 BA4548 BA4831(polA)
                 BA4849(dnaE)
            BAR: GBAA0002(dnaN-1) GBAA0019(dnaX) GBAA0028(holB) GBAA1552
                 GBAA2684(dnaN-2) GBAA3672 GBAA3955(polC) GBAA4366 GBAA4548
                 GBAA4831(polA) GBAA4849(dnaE)
            BAA: BA_0597 BA_0613 BA_0619 BA_2070 BA_3202 BA_4159 BA_4426
                 BA_4822 BA_4995 BA_5255 BA_5272
            BAT: BAS0002 BAS0021 BAS0030 BAS1439 BAS2499 BAS3404 BAS3669
                 BAS4051 BAS4222 BAS4482 BAS4498
            BCE: BC0002 BC0024 BC0037 BC1529 BC1864 BC2693 BC3611 BC3816
                 BC4142 BC4321 BC4587 BC4605
            BCA: BCE_0002(dnaN) BCE_0020(dnaX) BCE_0029(holB) BCE_1657
                 BCE_2720(dnaN) BCE_3631 BCE_3859 BCE_4214 BCE_4404
                 BCE_4718(polA) BCE_4735(dnaE) BCE_A0091(dnaN)
            BCZ: BCZK0002(dnaN) BCZK0019(dnaX) BCZK0027(holB) BCZK1412(ung)
                 BCZK2430(dnaN) BCZK3316(dnaE) BCZK3577(polC) BCZK3897(dinP)
                 BCZK4070 BCZK4328(polA) BCZK4345(dnaE) pE33L466_0012(dnaQ)
                 pE33L466_0313(dnaX)
            BCY: Bcer98_0002 Bcer98_0018 Bcer98_0026 Bcer98_1265 Bcer98_2260
                 Bcer98_2470 Bcer98_2840 Bcer98_3288
            BTK: BT9727_0002(dnaN) BT9727_0019(dnaX) BT9727_0027(holB)
                 BT9727_1411(ung) BT9727_2460(dnaN) BT9727_3366(dnaE)
                 BT9727_3559(polC) BT9727_3889(dinP) BT9727_4060
                 BT9727_4317(polA) BT9727_4333(dnaE)
            BTL: BALH_0002(dnaN) BALH_0019(dnaX) BALH_0027(holB) BALH_1383
                 BALH_3250(dnaE) BALH_3446(dnaE) BALH_3448(polC) BALH_3912
                 BALH_4171(polA) BALH_4187(dnaE) BALH_p0040(uvrX)
            BLI: BL00077(dnaN) BL00394(polA) BL00408(dnaE) BL00541(holB)
                 BL01234(polC) BL01384(dinB1) BL02088(holA) BL02357(dnaX)
            BLD: BLi00002(dnaN) BLi00028(dnaX) BLi00044(holB) BLi01879(polC)
                 BLi02568(yqjH) BLi02748(yqeN) BLi03057(polA) BLi03072(dnaE)
            BCL: ABC0002(dnaN) ABC0037(dnaX) ABC0052(holB) ABC1650(holA)
                 ABC2169 ABC2233(polC) ABC2596 ABC2709(polA) ABC2724(dnaE)
                 ABC3826
            BAY: RBAM_000020 RBAM_000250 RBAM_000400(holB) RBAM_016420
                 RBAM_019740(uvrX) RBAM_021830(yqjW) RBAM_026130
            BPU: BPUM_0002 BPUM_0015(holB) BPUM_0516 BPUM_1557 BPUM_2102
                 BPUM_2125 BPUM_2289(holA) BPUM_2551 BPUM_2566
            OIH: OB0002(dnaN) OB0029 OB0039 OB1593(polC) OB1858 OB1977
                 OB2163(polA) OB2177(dnaE)
            GKA: GK0002(dnaN) GK0017(dnaX) GK0025 GK1258(polC) GK2513
                 GK2730(polA) GK2744
            GTN: GTNG_0002 GTNG_0016(dnaZX) GTNG_1112
            SAU: SA0002(dnaN) SA0436(dnaX) SA0442(holB) SA1107(polC) SA1415
                 SA1513(polA) SA1525(dnaE) SA1711
            SAV: SAV0002(dnaN) SAV0478(dnaX) SAV0484(holB) SAV1264(polC)
                 SAV1587 SAV1690(polA) SAV1703(dnaE) SAV1895
            SAM: MW0002(dnaN) MW0433(dnaX) MW0439(holB) MW1147(polC) MW1538
                 MW1633(polA) MW1646(dnaE) MW1836
            SAR: SAR0002(dnaN) SAR0477(dnaX) SAR0485(holB) SAR1240(polC)
                 SAR1541 SAR1664 SAR1769(polA) SAR1781(dnaE) SAR1986
            SAS: SAS0002 SAS0435 SAS0441 SAS0909 SAS1198 SAS1524 SAS1618
                 SAS1630 SAS1817
            SAC: SACOL0002(dnaN) SACOL0520(dnaX) SACOL0526 SACOL1283 SACOL1643
                 SACOL1737(polA) SACOL1750(dnaE) SACOL1955(dinP)
            SAB: SAB0002(dnaN) SAB0427(dnaX) SAB0433(holB) SAB1126(polC)
                 SAB1459c SAB1549c(polA) SAB1561c(dnaE) SAB1826 SAB1827c
            SAA: SAUSA300_0002(dnaN) SAUSA300_0452(dnaX) SAUSA300_0461(holB)
                 SAUSA300_1157(polC) SAUSA300_1423(polA) SAUSA300_1546(holA)
                 SAUSA300_1636(polA) SAUSA300_1649(dnaE) SAUSA300_1876
            SAO: SAOUHSC_00002 SAOUHSC_00442 SAOUHSC_00454 SAOUHSC_01241
                 SAOUHSC_01563 SAOUHSC_01690 SAOUHSC_01797 SAOUHSC_01811
                 SAOUHSC_02111
            SAJ: SaurJH9_0002 SaurJH9_0499 SaurJH9_0505 SaurJH9_1324
                 SaurJH9_1425 SaurJH9_1759 SaurJH9_1949
            SAH: SaurJH1_0002 SaurJH1_0512 SaurJH1_0518 SaurJH1_1350
                 SaurJH1_1454 SaurJH1_1793 SaurJH1_1983
            SEP: SE0002 SE0940 SE1273 SE1367 SE1378 SE1580 SE2299 SE2307
            SER: SERP0114(dnaX) SERP0122 SERP0831 SERP1154 SERP1254(polA)
                 SERP1266(dnaE) SERP1433(dinP) SERP1537 SERP1538 SERP2552(dnaN)
            SHA: SH0002(dnaN) SH1058 SH1222(dnaE) SH1234(polA) SH1328
                 SH1650(polC) SH2527 SH2534(dnaX)
            SSP: SSP0002 SSP0896 SSP1064 SSP1075 SSP1171 SSP1504 SSP2272
                 SSP2278
            LMO: lmo0002(dnaN) lmo0162 lmo1320(polC) lmo1481 lmo1565(polA)
                 lmo1574(dnaE) lmo1975 lmo2704(dnaX)
            LMF: LMOf2365_0002(dnaN) LMOf2365_0177(holB) LMOf2365_1337(polC)
                 LMOf2365_1500 LMOf2365_1587(polA) LMOf2365_1596(dnaE)
                 LMOf2365_1998 LMOf2365_2684(dnaX)
            LIN: lin0002(dnaN) lin0205 lin1357(polC) lin1516 lin1600(polA)
                 lin1609(dnaE) lin2082 lin2852(dnaX)
            LWE: lwe0002(dnaN) lwe0143 lwe1186 lwe1335(polC) lwe1494
                 lwe1578(polA) lwe1587(dnaE) lwe1994 lwe2655(dnaX)
            LLA: L0270(polA) L0275(dnaN) L0278(polC) L0279(dnaH) L0280(holB)
                 L0305(dinP) L0307(dnaE) L102491(yraC) L9094(dnaQ)
            LLC: LACR_0002 LACR_0446 LACR_0519 LACR_1068 LACR_1819 LACR_2314
                 LACR_2429 LACR_2445 LACR_2506
            LLM: llmg_0002(dnaN) llmg_0416(holB) llmg_0483(dnaE)
                 llmg_0768(holA) llmg_1537(dnaQ) llmg_2305(dinP)
                 llmg_2409(polC) llmg_2425(polA) llmg_2478(dnaX)
            SPY: SPy_0003(dnaN) SPy_0185(polA) SPy_0400 SPy_1284(dnaE)
                 SPy_1364(dnaX) SPy_1407(holA) SPy_1846(dinP) SPy_1864(dnaQ)
                 SPy_1961(polC)
            SPZ: M5005_Spy_0002(dnaN) M5005_Spy_0159(polA)
                 M5005_Spy_0331(dnaX) M5005_Spy_0990(dnaE) M5005_Spy_1112
                 M5005_Spy_1146 M5005_Spy_1286 M5005_Spy_1450
                 M5005_Spy_1568(dinP) M5005_Spy_1582(dnaQ) M5005_Spy_1672(polC)
            SPM: spyM18_0002(dnaN) spyM18_0184 spyM18_0450 spyM18_1232(dnaE)
                 spyM18_1376(dnaX) spyM18_1415 spyM18_1910(dinP) spyM18_1928
                 spyM18_2028(dnaE)
            SPG: SpyM3_0002(dnaN) SpyM3_0145(polA.1) SpyM3_0290
                 SpyM3_0914(dnaE) SpyM3_1038(dnaX) SpyM3_1072(holA)
                 SpyM3_1595(dinP) SpyM3_1608(dnaQ) SpyM3_1687(polC)
            SPS: SPs0002 SPs0149 SPs0259 SPs0272 SPs0791 SPs0822 SPs1113
                 SPs1569 SPs1689
            SPH: MGAS10270_Spy0002(dnaN) MGAS10270_Spy0161(polA)
                 MGAS10270_Spy0327(dnaX) MGAS10270_Spy1104(dnaE)
                 MGAS10270_Spy1182 MGAS10270_Spy1217 MGAS10270_Spy1635(dinP)
                 MGAS10270_Spy1649(dnaQ) MGAS10270_Spy1740(polC)
            SPI: MGAS10750_Spy0002(dnaN) MGAS10750_Spy0165(polA)
                 MGAS10750_Spy0327(dnaX) MGAS10750_Spy1140(dnaE)
                 MGAS10750_Spy1211 MGAS10750_Spy1212 MGAS10750_Spy1253
                 MGAS10750_Spy1627(dinP) MGAS10750_Spy1640(dnaQ)
                 MGAS10750_Spy1766(polC)
            SPJ: MGAS2096_Spy0002(dnaN) MGAS2096_Spy0170(polA)
                 MGAS2096_Spy0351(dnaX) MGAS2096_Spy1050(dnaE) MGAS2096_Spy1175
                 MGAS2096_Spy1212 MGAS2096_Spy1476 MGAS2096_Spy1593(dinP)
                 MGAS2096_Spy1607(dnaQ) MGAS2096_Spy1695(polC)
            SPK: MGAS9429_Spy0002(dnaN) MGAS9429_Spy0161(polA)
                 MGAS9429_Spy0333(dnaX) MGAS9429_Spy1094(dnaE) MGAS9429_Spy1159
                 MGAS9429_Spy1193 MGAS9429_Spy1452 MGAS9429_Spy1573(dinP)
                 MGAS9429_Spy1587(dnaQ) MGAS9429_Spy1673(polC)
            SPF: SpyM50002(dnaN) SpyM50152(pol) SpyM50282(dinB) SpyM50713
                 SpyM50748(dnaH) SpyM50811(dnaE) SpyM51055 SpyM51527(holB)
                 SpyM51644(polC)
            SPA: M6_Spy0002 M6_Spy0034 M6_Spy0205 M6_Spy0357 M6_Spy0977
                 M6_Spy1086 M6_Spy1121 M6_Spy1155 M6_Spy1580 M6_Spy1594
                 M6_Spy1680
            SPB: M28_Spy0002(dnaN) M28_Spy0157(polA) M28_Spy0320(dnaX)
                 M28_Spy0962(dnaE) M28_Spy1105 M28_Spy1140 M28_Spy1556(dinP)
                 M28_Spy1570(dnaQ) M28_Spy1660(polC)
            SPN: SP_0002 SP_0032 SP_0274 SP_0458 SP_0765 SP_0865 SP_0895
                 SP_0936 SP_0993
            SPR: spr0002(dnaN) spr0032(polA) spr0251(polC) spr0414(dinP)
                 spr0673(holA) spr0769(dnaX) spr0795(dnaE) spr0836(holB)
                 spr0896(dnaQ)
            SPD: SPD_0002(dnaN) SPD_0038 SPD_0254(polC) SPD_0419(dinP)
                 SPD_0666(holA) SPD_0760(dnaX) SPD_0788(dnaE) SPD_0826(holB)
            SAG: SAG0002(dnaN) SAG0389(polA) SAG0787 SAG0828(dnaX)
                 SAG0939(dnaE) SAG1574 SAG1726(dinP) SAG1750 SAG1911
            SAN: gbs0002(dnaN) gbs0425(polA) gbs0807 gbs0846 gbs0929(dnaE)
                 gbs1625 gbs1771 gbs1794 gbs1898(polC)
            SAK: SAK_0002(dnaN) SAK_0463(polA) SAK_0725 SAK_0912(holA)
                 SAK_0952(dnaX) SAK_1035(dnaE) SAK_1590(holB) SAK_1734(dinB)
                 SAK_1773 SAK_1869(polC)
            SMU: SMU.02(dnaN) SMU.1192(dnaE) SMU.123 SMU.1581(dnaX)
                 SMU.1662(holB) SMU.297(polI) SMU.403 SMU.628
            STC: str0002(dnaN) str0062(polC) str0490(dnaH) str0719(holA)
                 str1174(dnaX) str1198(dnaE) str1601(dnaQ) str1656(dinP)
                 str1761(polA)
            STL: stu0002(dnaN) stu0062(polC) stu0490(dnaH) stu0719(holA)
                 stu1174(dnaX) stu1198(dnaE) stu1601(dnaQ) stu1656(dinP)
                 stu1761(polA)
            STE: STER_0002 STER_0095 STER_0527 STER_0761 STER_1621
            SSA: SSA_0002(dnaN) SSA_0100(polA) SSA_0343(dinP) SSA_0720(holA)
                 SSA_0846(dnaE) SSA_0997(dnaX) SSA_1721(holB) SSA_2066(polC)
            SSU: SSU05_0002 SSU05_0201 SSU05_0662 SSU05_1540 SSU05_1954
            SSV: SSU98_0002 SSU98_0202 SSU98_0662 SSU98_1551 SSU98_1959
            SGO: SGO_0002(dnaN) SGO_0145(polI) SGO_0248 SGO_0647 SGO_0901
                 SGO_1341(dnaE) SGO_1538 SGO_1847(polC)
            LPL: lp_0002(dnaN) lp_0698(dnaX) lp_0705(holB) lp_0811
                 lp_1508(polA) lp_1899(dnaE) lp_2045(polC) lp_2128(holA)
                 lp_2280(dinP)
            LJO: LJ0002 LJ0423 LJ0429 LJ0471 LJ0886 LJ1004 LJ1077 LJ1492
                 LJ1509 LJ1651
            LAC: LBA0002(dnaN) LBA0376 LBA0383 LBA0414 LBA0706 LBA0840 LBA0955
                 LBA1261 LBA1282 LBA1550(polA) LBA1648
            LSA: LSA0002(dnaN) LSA0336(dnaX) LSA0342(holB) LSA0382(dinP)
                 LSA1034(dnaE) LSA1068(holA) LSA1256(polC) LSA1339(dnaQ)
                 LSA1406(polA)
            LSL: LSL_0002(dnaN) LSL_0488(polA) LSL_0567(dnaE) LSL_0681(holA)
                 LSL_0758 LSL_0865(dnaE) LSL_1149(dnaQ) LSL_1162(dinP)
                 LSL_1223(holB) LSL_1228(dnaX)
            LDB: Ldb0002(dnaN) Ldb0645 Ldb0771(holA) Ldb0837(dnaE)
                 Ldb1337(polC) Ldb1512(polA) Ldb1610(dinB) Ldb1629
                 Ldb1635(dnaX)
            LBU: LBUL_0002 LBUL_0576 LBUL_0704 LBUL_0760 LBUL_1246 LBUL_1407
                 LBUL_1489 LBUL_1509 LBUL_1515
            LBR: LVIS_0002 LVIS_0600 LVIS_0606 LVIS_0678 LVIS_0763 LVIS_1042
                 LVIS_1226 LVIS_1341 LVIS_1394
            LCA: LSEI_0002 LSEI_0779 LSEI_1001 LSEI_1326 LSEI_1363 LSEI_1578
                 LSEI_1709 LSEI_2257 LSEI_2263
            LGA: LGAS_0002 LGAS_0368 LGAS_0374 LGAS_0418 LGAS_0792 LGAS_0809
                 LGAS_1173
            LRE: Lreu_0002 Lreu_0326 Lreu_0332 Lreu_0694 Lreu_0750 Lreu_1526
            PPE: PEPE_0002 PEPE_0885 PEPE_1148 PEPE_1266 PEPE_1479 PEPE_1484
            EFA: EF0002(dnaN) EF0053(dnaQ) EF0659 EF0878(polA) EF1044(dnaE)
                 EF2378 EF2446 EF2736 EF2756(dinP) EF2762(holB) EF2781(dnaX)
            OOE: OEOE_0002 OEOE_0673 OEOE_0965 OEOE_0983 OEOE_1000 OEOE_1405
                 OEOE_1410 OEOE_1663
            LME: LEUM_0002 LEUM_0689 LEUM_1586 LEUM_1587
            STH: STH1032 STH13 STH1512(dnaE3) STH1885(dnaE2) STH2 STH2917
                 STH475 STH659(dnaE1) STH848
            CAC: CAC0002(dnaN) CAC0125(dnaX) CAC0219 CAC0285 CAC0300
                 CAC0516(dnaE) CAC0738 CAC1098(polA) CAC1223(dnaE) CAC1273
                 CAC2997 CAC3442(polC)
            CPE: CPE0002(dnaN) CPE0045(dnaX) CPE0360(dnaE) CPE1401
                 CPE1566(dinP) CPE1691(polC) CPE1994(polA) CPE2043
                 CPE2449(holB)
            CPF: CPF_0002(dnaN) CPF_0052(dnaX) CPF_1818(dinB) CPF_1945(polC)
                 CPF_2250(polA) CPF_2300(holA) CPF_2759
            CPR: CPR_0002(dnaN) CPR_0055(dnaX) CPR_0340 CPR_1538(dinB)
                 CPR_1663(polC) CPR_1962(polA) CPR_2015(holA) CPR_2444
            CTC: CTC00062 CTC00075 CTC00093 CTC00221 CTC00242 CTC00437
                 CTC01116 CTC01271 CTC02041 CTC02103 CTC02491
            CNO: NT01CX_0014 NT01CX_0066 NT01CX_0702 NT01CX_0759 NT01CX_0790
                 NT01CX_0825(dnaX) NT01CX_0866(dnaN) NT01CX_1296(dnaE)
                 NT01CX_1677 NT01CX_2140(polC)
            CTH: Cthe_0886 Cthe_0996 Cthe_1040 Cthe_1264 Cthe_1650 Cthe_2083
                 Cthe_2105 Cthe_2144 Cthe_2372 Cthe_3109
            CDF: CD0002(dnaN) CD0016(dnaH) CD0899(dinB) CD1128(polA)
                 CD1305(dnaF) CD3396(dnaE) CD3549
            CBO: CBO0002(dnaG) CBO0031(dnaH) CBO0056 CBO2423(dnaF)
                 CBO2818(dinB) CBO3014(polA) CBO3374(dnaE)
            CBA: CLB_0002(dnaN) CLB_0042(dnaX) CLB_2287(polC) CLB_2761(dinB)
                 CLB_2932(holA) CLB_3039(polA) CLB_3430(dnaE)
            CBH: CLC_0002(dnaN) CLC_0051(dnaX) CLC_2270(polC) CLC_2694(dinB)
                 CLC_2864(holA) CLC_2911(polA) CLC_3317(dnaE)
            CBF: CLI_0002(dnaN) CLI_0047(dnaX) CLI_2434(polA-1) CLI_2479(polC)
                 CLI_2867(dinB) CLI_3021(holA) CLI_3068(polA-2) CLI_3558(dnaE)
            CBE: Cbei_0002 Cbei_0801 Cbei_3203 Cbei_4241 Cbei_4853 Cbei_4951
            CKL: CKL_0002(dnaN) CKL_0669(polA) CKL_1426(polC) CKL_2661
                 CKL_3439(dinB) CKL_3560(dnaE) CKL_3827(dnaX)
            AMT: Amet_0002 Amet_0084 Amet_1769 Amet_2678 Amet_3125 Amet_4071
                 Amet_4216 Amet_4781
            CHY: CHY_0051 CHY_0959(dnaE1) CHY_1137(dnaE2) CHY_1650(polA)
                 CHY_1651(dinB) CHY_1772(polC) CHY_2675 CHY_2709(dnaN)
            DSY: DSY0002(dnaN) DSY0111 DSY0122 DSY0420 DSY1312 DSY1340 DSY3146
                 DSY3422 DSY3733 DSY4185 DSY4311 DSY4361
            DRM: Dred_0002 Dred_0042 Dred_0060 Dred_1743 Dred_1965 Dred_2319
                 Dred_2506
            PTH: PTH_0002(dnaN) PTH_0051(xerD) PTH_0867(holA)
            SWO: Swol_0002 Swol_0030 Swol_0042 Swol_0895 Swol_1362 Swol_1588
                 Swol_1670 Swol_2017 Swol_2043
            CSC: Csac_0002 Csac_0617 Csac_0743 Csac_1322 Csac_1827 Csac_1988
                 Csac_2349
            TTE: TTE0002(dnaN) TTE0039(dnaX) TTE0077 TTE0097(holB)
                 TTE0254(dinP) TTE0874(polA) TTE0942(holA) TTE1398(polC)
                 TTE1818(dnaE)
            MTA: Moth_0003 Moth_0027 Moth_0043 Moth_0576 Moth_1045 Moth_1154
                 Moth_1229 Moth_1841 Moth_1872 Moth_2161
            MGE: MG_001(dnaN) MG_007 MG_031(polC) MG_261(dnaE) MG_315 MG_360
                 MG_419
            MPN: MPN001(dnaN) MPN007(holB) MPN034(polC) MPN378(dnaE)
                 MPN450(orf7) MPN537(mucB) MPN618(dnaX)
            MPU: MYPU_0020(dnaN) MYPU_0490(dnaX) MYPU_0530(dnaX)
                 MYPU_1880(mucB) MYPU_4620 MYPU_6750(polC) MYPU_7190(dnaE)
                 MYPU_7200(polA)
            MPE: MYPE1490(mucB) MYPE1980(dnaE) MYPE20(dnaN) MYPE450
                 MYPE8080(dnaX) MYPE8130 MYPE9170(polC)
            MGA: MGA_0344 MGA_0401(dnaX) MGA_0605(holB) MGA_0618(dnaN)
                 MGA_0791(polC) MGA_1048(dnaE)
            MMY: MSC_0002(dnaN) MSC_0045(holB) MSC_0048(dnaX) MSC_0091(polA)
                 MSC_0355(polC) MSC_0549(dinP) MSC_0683(polA) MSC_0684(dnaE)
                 MSC_0945
            MMO: MMOB0020(dnaN) MMOB0570(dnaE) MMOB0730(dnaX) MMOB2750(mucB)
                 MMOB3600(holA) MMOB4870(dnaE) MMOB4880(polA) MMOB5260(holB)
            MHY: mhp002(dnaN) mhp047 mhp119 mhp123(dnaX) mhp549(polC)
                 mhp598(polA) mhp599(dnaE)
            MHJ: MHJ_0002(dnaN) MHJ_0041(dinP) MHJ_0248(dnaX) MHJ_0252
                 MHJ_0533(polC) MHJ_0583(dnaE)
            MHP: MHP7448_0002(dnaN) MHP7448_0045(dinP) MHP7448_0256(dnaX)
                 MHP7448_0260 MHP7448_0532(polC) MHP7448_0582(dnaE)
            MSY: MS53_0002(dnaN) MS53_0004(polC) MS53_0055(dnaX)
                 MS53_0320(dinP) MS53_0528 MS53_0529(dnaE)
            MCP: MCAP_0002(dnaN) MCAP_0008(dnaX) MCAP_0011 MCAP_0047
                 MCAP_0339(polC) MCAP_0423 MCAP_0636(polA) MCAP_0637(dnaE)
                 MCAP_0772
            UUR: UU019(dnaH) UU079(dnaN) UU087(dnaX) UU328 UU377(polC)
                 UU415(dnaE) UU437
            POY: PAM002(dnaN) PAM016(holA) PAM231(holB) PAM465(polC)
                 PAM591(dnaE) PAM617(dnaX) PAM676(exo)
            AYW: AYWB_002(dnaN) AYWB_010(holA) AYWB_066(polA) AYWB_117(dnaX)
                 AYWB_129(dnaE) AYWB_313(polC) AYWB_491(holB)
            MFL: Mfl002 Mfl055 Mfl288 Mfl328 Mfl368 Mfl582 Mfl583 Mfl675
                 Mfl678
            MTU: Rv0002(dnaN) Rv1537(dinX) Rv1547(dnaE1) Rv1629(polA) Rv2191
                 Rv2413c Rv3056(dinP) Rv3370c(dnaE2) Rv3644c Rv3711c(dnaQ)
                 Rv3721c(dnaZX)
            MTC: MT0002(dnaN) MT1589 MT1598(dnaE) MT1665(polA) MT2247 MT2486
                 MT3142 MT3480 MT3747(holB) MT3814(dnaQ) MT3824(dnaZX)
            MBO: Mb0002(dnaN) Mb1564(dinX) Mb1574(dnaE1) Mb1655(polA) Mb2214
                 Mb2436c Mb3082(dinP) Mb3405c(dnaE2) Mb3668c Mb3738c(dnaQ)
                 Mb3748c(dnaZX)
            MBB: BCG_0002(dnaN_1) BCG_0032(dnaN_2) BCG_1600(dnaE1)
                 BCG_1667(polA) BCG_3442c(dnaE2) BCG_3771c(dnaQ)
                 BCG_3781c(dnaZX)
            MLE: ML0002(dnaN) ML0202 ML0603 ML1207(dnaE) ML1381(polA)
                 ML2335(dnaZX)
            MPA: MAP0002(dnaN) MAP0178c MAP0313c(dnaQ) MAP0322c(dnaZX) MAP0427
                 MAP1248(dinX) MAP1257(dnaE1) MAP1322(polA) MAP1930 MAP2225c
                 MAP3106(dinP) MAP3256c MAP3476c(dnaE2)
            MAV: MAV_0002(dnaN) MAV_0172 MAV_0382 MAV_0391 MAV_0520 MAV_3155
                 MAV_3224 MAV_3232 MAV_3925
            MSM: MSMEG_0001(dnaN) MSMEG_0265 MSMEG_1014(dinB) MSMEG_1633
                 MSMEG_2294(dinB) MSMEG_3172 MSMEG_3178 MSMEG_3839 MSMEG_4259
                 MSMEG_4572 MSMEG_6153 MSMEG_6275 MSMEG_6285 MSMEG_6443(dinP)
            MUL: MUL_0002(dnaN) MUL_4315(dnaZX)
            MVA: Mvan_0002 Mvan_1530 Mvan_2037 Mvan_2771 Mvan_2777 Mvan_3361
                 Mvan_5394 Mvan_5534 Mvan_5685
            MGI: Mflv_0826 Mflv_1122 Mflv_1281 Mflv_1396 Mflv_2958 Mflv_3564
                 Mflv_3636 Mflv_3642 Mflv_4310 Mflv_4893
            MMC: Mmcs_0002 Mmcs_1183 Mmcs_1812 Mmcs_2993 Mmcs_3011 Mmcs_3087
                 Mmcs_3095 Mmcs_3289 Mmcs_3511 Mmcs_4794 Mmcs_4900 Mmcs_4909
                 Mmcs_5059
            MKM: Mkms_0010 Mkms_1200 Mkms_1859 Mkms_3057 Mkms_3147 Mkms_3155
                 Mkms_3351 Mkms_4880 Mkms_4998 Mkms_5147
            MJL: Mjls_0002 Mjls_1210 Mjls_1793 Mjls_3026 Mjls_3107 Mjls_3115
                 Mjls_3300 Mjls_5180 Mjls_5277 Mjls_5438
            CGL: NCgl0002(cgl0003) NCgl0239(cgl0242) NCgl0307(cgl0312)
                 NCgl0611(cgl0638) NCgl1195(cgl1243) NCgl1240(cgl1289)
                 NCgl1299(cgl1353) NCgl2035(cgl2116) NCgl2049(cgl2130)
                 NCgl2064(cgl2144) NCgl2264(cgl2346)
            CGB: cg0004(dnaN) cg0296(dnaZX) cg0376(dnaX) cg1400 cg1457(dnaQ2)
                 cg1525(polA) cg2321 cg2338(dnaE1) cg2576
            CEF: CE0003 CE0209 CE0311 CE0632 CE1385 CE1455 CE2015 CE2029
                 CE2040 CE2247
            CDI: DIP0002(dnaN) DIP0259(dnaX) DIP0333 DIP0612 DIP1076
                 DIP1146(polA) DIP1573 DIP1580(dnaE) DIP1588(dinB) DIP1769
            CJK: jk0002(dnaN) jk0573(holA) jk0723 jk0761(dinX) jk0771(dnaE)
                 jk0818(polA) jk1315(dnaQ2) jk1709(dnaE2) jk1951(holB)
                 jk2003(dnaQ) jk2012(dnaX)
            NFA: nfa13940 nfa17220 nfa17790 nfa18000(dnaE) nfa18750(polA)
                 nfa20(dnaN) nfa26700 nfa27290 nfa2840 nfa3680 nfa39660(dnaN2)
                 nfa56150 nfa9150(dnaE2)
            RHA: RHA1_ro00990(polA) RHA1_ro01069(dnaE1) RHA1_ro01077
                 RHA1_ro01126 RHA1_ro01383 RHA1_ro01702 RHA1_ro02325
                 RHA1_ro03667(dnaN) RHA1_ro03989 RHA1_ro04199 RHA1_ro04354
                 RHA1_ro06227(dnaE2)
            SCO: SCO1380(SC10A9.22c) SCO1739(SCI11.28c) SCO1827(SCI8.12)
                 SCO2003(polA) SCO2064(dnaE) SCO2564(SCC123.02c)
                 SCO3541(SCH5.03c) SCO3878(dnaN) SCO4067(dnaZ)
                 SCO4495(SCD35.02) SCO6084(SCBAC1A6.08) SCP1.119(dnaN)
                 SCP1.224c(dnaE)
            SMA: SAV2147(dnaQ3) SAV3362(dnaN2) SAV4150(dnaZX) SAV4317(dnaN1)
                 SAV4623(holB) SAV5558 SAV6143(dnaE1) SAV6227(polA1)
                 SAV6439(dnaQ1) SAV6555(dnaE2) SAV6985(dinB)
            TWH: TWT002(dnaN) TWT292(polA) TWT381(holA) TWT510(dnaE) TWT694
                 TWT710(dnaZX)
            TWS: TW002(dnaN) TW252(dnaE) TW389 TW480(polA) TW713 TW727(dnaX)
            LXX: Lxx00020(dnaN) Lxx03430(dnaZ) Lxx04080 Lxx11410(polA)
                 Lxx11820 Lxx14270 Lxx14720 Lxx15160(dnaE) Lxx16640
            CMI: CMM_0002(dnaN) CMM_0900 CMM_0929(holB) CMM_1427(dinB)
                 CMM_1518(dnaE1) CMM_1550(holA) CMM_1612(polA2) CMM_1715(dnaQ)
                 CMM_1755(polA1)
            ART: Arth_0002 Arth_0555 Arth_0716 Arth_1559 Arth_1581 Arth_2021
                 Arth_2063 Arth_2318 Arth_3841
            AAU: AAur_0002(dnaN) AAur_0666(dnaX) AAur_1721(dnaE)
                 AAur_2065(polA) AAur_2242(holA)
            PAC: PPA0002 PPA0204 PPA0244 PPA0720 PPA0774 PPA0897 PPA1150
                 PPA1650 PPA1670
            NCA: Noca_0002 Noca_0317 Noca_0387 Noca_1897 Noca_2975 Noca_3006
                 Noca_3050 Noca_3128 Noca_3703 Noca_4549
            TFU: Tfu_0002 Tfu_0047 Tfu_0051 Tfu_0086 Tfu_0183 Tfu_0823
                 Tfu_0902 Tfu_1027 Tfu_1096 Tfu_1189 Tfu_2782
            FRA: Francci3_0003 Francci3_0075 Francci3_0270 Francci3_0738
                 Francci3_1259 Francci3_1621 Francci3_1710 Francci3_3104
                 Francci3_4082 Francci3_4168 Francci3_4307
            FAL: FRAAL0004(dnaN) FRAAL0102 FRAAL0612 FRAAL1257 FRAAL1999
                 FRAAL2179 FRAAL2180 FRAAL2182 FRAAL3779 FRAAL4407(dnaE)
                 FRAAL4613(polA) FRAAL5108 FRAAL5255 FRAAL6581(holB)
            ACE: Acel_0002 Acel_0118 Acel_0356 Acel_0775 Acel_0968 Acel_0995
                 Acel_1054 Acel_1088 Acel_1444 Acel_1970 Acel_2016
            KRA: Krad_0002 Krad_0466 Krad_0490 Krad_1769 Krad_2951 Krad_3187
                 Krad_3213 Krad_3215 Krad_3247 Krad_4326 Krad_4598
            SEN: SACE_0003(dnaN) SACE_0251 SACE_0327(dnaN) SACE_0379(holB)
                 SACE_1438 SACE_1689 SACE_2336 SACE_3814(dinP) SACE_4189
                 SACE_4190 SACE_5437(polA) SACE_5815(dnaE) SACE_6234(dinX)
                 SACE_6660(dnaE2) SACE_6661
            STP: Strop_0003 Strop_0213 Strop_1798 Strop_3145 Strop_3236
                 Strop_3239 Strop_3286 Strop_4022
            BLO: BL0071(dnaQ) BL0127(dnaE) BL0483 BL0500(dnaX) BL0638(dnaN)
                 BL0985(polA) BL1454 BL1565
            BAD: BAD_0002(dnaN) BAD_0137(dnaX) BAD_0163 BAD_0303
                 BAD_0680(polA) BAD_0861 BAD_0985(dnaQ1) BAD_1130(dnaE1)
            RXY: Rxyl_0002 Rxyl_0503 Rxyl_1096 Rxyl_1518 Rxyl_1922 Rxyl_1961
                 Rxyl_2025 Rxyl_2444 Rxyl_2984 Rxyl_3166
            FNU: FN0281 FN0536 FN0617 FN0705 FN0901 FN0917 FN1199 FN1383
                 FN1576 FN1830
            RBA: RB10108(dnaN) RB10816(holB) RB12116(dnaQ) RB1262(dnaE)
                 RB12799(polA) RB2871 RB3103(dnaE) RB3915(dpoL) RB4224(dinP)
                 RB5620 RB6494(dnaX)
            CTR: CT047 CT075(dnaN) CT187(dnaX_1) CT261(dnaQ_1) CT334(dnaX_2)
                 CT493(polA) CT536(dnaQ_2) CT545(dnaE)
            CTA: CTA_0051 CTA_0080(dnaN) CTA_0205(dnaX_1) CTA_0283(dnaQ_1)
                 CTA_0362(dnaX_2) CTA_0540(polA) CTA_0585(dnaQ_2)
                 CTA_0595(dnaE)
            CMU: TC0317 TC0347 TC0459 TC0532 TC0611 TC0780 TC0823 TC0832
            CPN: CPn0040(dnaX_1) CPn0272(dnaX_2) CPn0338(dnaN) CPn0383
                 CPn0410(dnaQ_1) CPn0612(polA) CPn0655(dnaQ_2) CPn0666(dnaE)
            CPA: CP0081 CP0092 CP0135 CP0344 CP0372 CP0419 CP0487 CP0735
            CPJ: CPj0040(dnaX_1) CPj0272(dnaX_2) CPj0338(dnaN) CPj0383
                 CPj0410(dnaQ_1) CPj0612(polA) CPj0655(dnaQ_2) CPj0666(dnaE)
            CPT: CpB0044 CpB0278(dnaX) CpB0347 CpB0395 CpB0426 CpB0636 CpB0681
                 CpB0692
            CCA: CCA00073(dnaE) CCA00085(dnaQ-1) CCA00128(polA) CCA00331(dnaZ)
                 CCA00384(dnaQ-2) CCA00413 CCA00445(dnaN) CCA00509
            CAB: CAB075(dnaE) CAB085(dnaF) CAB127(polA) CAB327(dnaX)
                 CAB371(dnaQ) CAB399 CAB431(dnaN) CAB496
            CFE: CF0499(dnaX1) CF0562(dnaN) CF0594 CF0624(dnaQ1) CF0671(dnaX2)
                 CF0878(polA) CF0921(dnaQ2) CF0931(dnaE)
            PCU: pc0223(polA) pc0236(dnaQ_2) pc0389(dnaE) pc0478(dnaX)
                 pc1072(holB) pc1100 pc1161(dnaQ) pc1705(dnaN) pc1820(dinP)
            BBU: BB0438(dnaN) BB0455 BB0461(dnaX) BB0548(polA) BB0579(dnaE)
                 BB0765
            BGA: BG0445(dnaN) BG0464 BG0474(dnaX) BG0558(polA) BG0591(dnaE)
                 BG0788
            BAF: BAPKO_0460(dnaN) BAPKO_0478 BAPKO_0490(dnaX) BAPKO_0577(polA)
                 BAPKO_0610(dnaE)
            TPA: TP0002 TP0105 TP0229 TP0521 TP0588 TP0643 TP0669 TP1005
            TDE: TDE0231(dnaN) TDE0963(dinB) TDE1637(polA) TDE1971 TDE1999
                 TDE2491 TDE2586 TDE2786(dnaE)
            LIL: LA0002(dnaN) LA0014 LA0258(dnaE) LA0503(dinP) LA3625(polA)
                 LA3668 LA4331(dnaX1) LA4361(dnaX2)
            LIC: LIC10002(dnaN) LIC10014 LIC10222(dnaE) LIC10548
                 LIC10586(polA) LIC13052(dinP) LIC13474(dnaX) LIC13497
            LBJ: LBJ_0003(dnaX-1) LBJ_0005(dnaN) LBJ_0015(holA) LBJ_2564(polA)
                 LBJ_2712 LBJ_2783(dnaE) LBJ_3001(dnaX-2)
            LBL: LBL_0003(dnaX-1) LBL_0005(dnaN) LBL_0015(holA)
                 LBL_0064(dnaX-2) LBL_0288(dnaE) LBL_0362 LBL_0548(polA)
            SYN: sll0544 sll1360(dnaX) sll1572(dnaE-c) slr0446(dnaX)
                 slr0603(dnaE-n) slr0707(polA) slr0965(dnaN)
            SYW: SYNW0001(dnaN) SYNW0061(dnaX) SYNW0073 SYNW0702(polA)
                 SYNW1016(dnaQ) SYNW1032(dnaE) SYNW1173 SYNW2237(holB)
            SYC: syc0630_c(dnaX) syc0952_d(dnaE) syc1111_c(holA)
                 syc1317_d(polA) syc1410_c(holB) syc1496_c(dnaN) syc1567_d
                 syc1898_d(dnaE)
            SYF: Synpcc7942_0001 Synpcc7942_0094 Synpcc7942_0194
                 Synpcc7942_0405 Synpcc7942_0570 Synpcc7942_0912
                 Synpcc7942_2199 Synpcc7942_2543
            SYD: Syncc9605_0001 Syncc9605_0062 Syncc9605_0072 Syncc9605_1158
                 Syncc9605_1297 Syncc9605_1966 Syncc9605_2379
            SYE: Syncc9902_0001 Syncc9902_0058 Syncc9902_0072 Syncc9902_0313
                 Syncc9902_0693 Syncc9902_1180 Syncc9902_1301
            SYG: sync_0001(dnaN) sync_0062(dnaX) sync_0077(holA)
                 sync_0928(polA) sync_1557 sync_1630(dnaE) sync_2592(holB)
            SYR: SynRCC307_0001(dnaN) SynRCC307_0063(dnaX)
                 SynRCC307_0076(holA) SynRCC307_0255(holB) SynRCC307_1325(dnaE)
                 SynRCC307_1341(dnaQ) SynRCC307_1669(polA)
            SYX: SynWH7803_0062(dnaX) SynWH7803_0082(holA)
                 SynWH7803_1043(dnaQ) SynWH7803_1067(dnaE) SynWH7803_1617(polA)
                 SynWH7803_2243(holB)
            CYA: CYA_0057(dnaE) CYA_0531(polA) CYA_0563(dnaX) CYA_1270(holB)
                 CYA_1511(holA) CYA_1647(dnaN)
            CYB: CYB_0126(polA) CYB_1099 CYB_1183(dnaE) CYB_1304(dnaX)
                 CYB_1539(dnaN) CYB_2699(holA)
            TEL: tll0518(dnaX) tll1339(polA) tll1956 tll2056(dnaE)
                 tll2069(dnaE) tll2349(dnaN) tlr1132 tlr1573
            GVI: gll0066 gll0636(polA) gll1432(dnaX) glr1609(dnaX) glr2408
                 glr3232(dnaN) glr3934(dnaE)
            ANA: all3578 all4705 alr1054 alr1254 alr2010(dnaN) alr3018 alr3444
                 alr4932 alr7254 alr7569 alr7570 alr7575
            AVA: Ava_0002 Ava_0581 Ava_0893 Ava_1603 Ava_1963 Ava_2215
                 Ava_3469 Ava_3748 Ava_B0112 Ava_C0075 Ava_C0076 Ava_C0084
            PMA: Pro0001(dnaN) Pro0151(holB) Pro0751(dnaE) Pro0777(dnaQ)
                 Pro1016 Pro1234(polA) Pro1807(holA) Pro1818(dnaX)
            PMM: PMM0001(dnaN) PMM0129(holB) PMM0621(dnaQ) PMM0675
                 PMM0945(dnaE) PMM1140(polA) PMM1647 PMM1658(dnaX)
            PMT: PMT0001(dnaN) PMT0059(dnaX) PMT0074 PMT0386(dnaQ)
                 PMT0647(dnaE) PMT0778 PMT1157(polA) PMT1989(holB)
            PMN: PMN2A_0108 PMN2A_0265 PMN2A_0274 PMN2A_0748 PMN2A_1245
                 PMN2A_1256 PMN2A_1328 PMN2A_1495
            PMI: PMT9312_0001 PMT9312_0131 PMT9312_0621 PMT9312_0675
                 PMT9312_0854 PMT9312_0862 PMT9312_1236 PMT9312_1739
                 PMT9312_1750
            PMB: A9601_00001(dnaN) A9601_01461(holB) A9601_06771(dnaQ)
                 A9601_07301 A9601_09151(dnaE) A9601_09231(umuC)
                 A9601_13151(polA) A9601_18561(holA) A9601_18671(dnaX)
            PMC: P9515_00001(dnaN) P9515_01571(holB) P9515_06861(dnaQ)
                 P9515_07481 P9515_10201(umuC) P9515_10281(dnaE)
                 P9515_13041(polA) P9515_18371(holA) P9515_18481(dnaX)
            PMF: P9303_00001(dnaN) P9303_00641(dnaX) P9303_00831(holA)
                 P9303_08691(polA) P9303_14331 P9303_15831(dnaE)
                 P9303_15961(umuC) P9303_19021(dnaQ) P9303_26481(holB)
            PMG: P9301_00001(dnaN) P9301_01481(holB) P9301_06471(dnaQ)
                 P9301_07281 P9301_09131(dnaE) P9301_09211(umuC)
                 P9301_13291(polA) P9301_18371(holA) P9301_18481(dnaX)
            PMH: P9215_00001 P9215_09451 P9215_13441
            PME: NATL1_00001(dnaN) NATL1_02011(holB) NATL1_06801(dnaQ)
                 NATL1_07331 NATL1_09341(dnaE) NATL1_09431(umuC)
                 NATL1_15881(polA) NATL1_21151(holA) NATL1_21271(dnaX)
            TER: Tery_0008 Tery_0212 Tery_0413 Tery_0546 Tery_0832 Tery_1565
                 Tery_1889 Tery_1905
            BTH: BT_1363 BT_1364 BT_1431 BT_1610 BT_2230 BT_3260 BT_3820
                 BT_4409
            BFR: BF0091 BF0712 BF1131 BF1174 BF2396 BF2980 BF2981 BF3231
                 BF4093
            BFS: BF0104(polA) BF0641(dnaE) BF1043(dinB) BF1141 BF2856 BF2857
                 BF3071 BF3909
            PGI: PG0035(dnaE) PG0223 PG0932 PG0949 PG1418(dnaX) PG1794(polA)
                 PG1852 PG1853(dnaN)
            SRU: SRU_0002(dnaN) SRU_0027 SRU_0498(holA) SRU_0857 SRU_0950
                 SRU_0979(dnaE) SRU_1441 SRU_1539 SRU_1635(polA) SRU_2557
            CHU: CHU_0009(dnaQ) CHU_0094(dnaE) CHU_0491 CHU_1233(dnaX)
                 CHU_1347 CHU_1537 CHU_1549(dnaN) CHU_1679(dinB) CHU_1680(dnaQ)
                 CHU_3657(polA)
            GFO: GFO_0140(polA) GFO_1830(dnaX) GFO_1914(dnaN) GFO_2248(dnaQ)
                 GFO_2314 GFO_3028(dnaE) GFO_3077(dinB) GFO_3078(dnaE)
                 GFO_3295(holB) GFO_3388(dinB2)
            FJO: Fjoh_0883 Fjoh_1310 Fjoh_1617 Fjoh_1965 Fjoh_1966 Fjoh_2651
                 Fjoh_2720 Fjoh_3568 Fjoh_3569 Fjoh_3768 Fjoh_3769 Fjoh_4530
            FPS: FP0011(holB) FP0290(polA) FP0341(dnaE) FP0965 FP1053(holA)
                 FP1091(dnaN) FP1195(dnaQ) FP1438 FP1915
            CTE: CT0001(dnaN) CT0206 CT0840(dnaE) CT1039(dnaQ) CT1324(dnaZX)
                 CT1606 CT1667(polA) CT1948
            CCH: Cag_0002 Cag_0179 Cag_0224 Cag_0626 Cag_0893 Cag_0934
                 Cag_1778
            CPH: Cpha266_0002 Cpha266_0536 Cpha266_0587 Cpha266_1031
                 Cpha266_1195 Cpha266_1576 Cpha266_1652
            PVI: Cvib_0002 Cvib_0129 Cvib_0730 Cvib_1013 Cvib_1392 Cvib_1434
            PLT: Plut_0001 Plut_0260 Plut_1200 Plut_1262 Plut_1322 Plut_1602
                 Plut_1645
            DET: DET0011 DET0047 DET0437 DET0535(holB) DET0585 DET1227(dnaN)
                 DET1391(polA) DET1464(dnaE)
            DEH: cbdb_A1145(dnaN) cbdb_A12(dinB) cbdb_A1348(polA)
                 cbdb_A1436(dnaE) cbdb_A391 cbdb_A509(holB) cbdb_A563(dnaX)
                 cbdb_A60(holA)
            DEB: DehaBAV1_0010 DehaBAV1_0414 DehaBAV1_0511 DehaBAV1_0559
                 DehaBAV1_1036 DehaBAV1_1200 DehaBAV1_1265
            RRS: RoseRS_0091 RoseRS_1535 RoseRS_1899 RoseRS_3415 RoseRS_3588
                 RoseRS_4406
            RCA: Rcas_0198 Rcas_0749 Rcas_1512 Rcas_1545 Rcas_2293 Rcas_4275
            DRA: DR_0001 DR_0507 DR_0856 DR_1244 DR_1707 DR_1751 DR_2410
            DGE: Dgeo_0003 Dgeo_0255 Dgeo_0745 Dgeo_1556 Dgeo_1666 Dgeo_1818
                 Dgeo_2135
            TTH: TTC0366 TTC0434 TTC0690 TTC1509 TTC1588 TTC1609 TTC1806
            TTJ: TTHA0001 TTHA0180 TTHA0718 TTHA0788 TTHA1054 TTHA1860
                 TTHA1952
            AAE: aq_1008(dnaE) aq_1104 aq_1526 aq_1693(dplF) aq_1855(dnaX)
                 aq_1882(dnaN) aq_1967(polA) aq_2108 aq_932(dnaQ)
            TMA: TM0181 TM0262 TM0461 TM0496 TM0511 TM0576 TM0686 TM0771
                 TM1619
            TPT: Tpet_0245 Tpet_0342 Tpet_0424 Tpet_0459 Tpet_0662 Tpet_1172
            TME: Tmel_0535 Tmel_1039 Tmel_1397 Tmel_1524 Tmel_1917
            FNO: Fnod_0277 Fnod_0360 Fnod_0984 Fnod_1203 Fnod_1721
            MJA: MJ0702 MJ0885 MJ1630
            MMP: MMP0008(DP1) MMP0026(DP2) MMP0380(dnaB)
            MMQ: MmarC5_1656 MmarC5_1676
            MMZ: MmarC7_1005 MmarC7_1023
            MAE: Maeo_1141 Maeo_1166
            MVN: Mevan_1196 Mevan_1212
            MAC: MA0037 MA0885 MA3593(udg) MA4027 MA4552
            MBA: Mbar_A0560 Mbar_A0899 Mbar_A1005 Mbar_A1777 Mbar_A1809
                 Mbar_A2765
            MMA: MM_0486 MM_0886 MM_1246 MM_1345 MM_2004 MM_2876
            MBU: Mbur_0144 Mbur_1688 Mbur_2166 Mbur_2338 Mbur_2423
            MTP: Mthe_0659 Mthe_1250
            MHU: Mhun_0839 Mhun_1156 Mhun_1469 Mhun_2412 Mhun_2435
            MLA: Mlab_0059
            MEM: Memar_0045 Memar_0380 Memar_2124
            MBN: Mboo_0035 Mboo_0126 Mboo_0622
            MTH: MTH1208 MTH1405 MTH1536 MTH208
            MST: Msp_0255(polC) Msp_1281 Msp_1507(pol) Msp_1584(polB)
            MSI: Msm_1041 Msm_1176 Msm_1271 Msm_1384 Msm_1481
            MKA: MK1039(polB) MK1583(hYS2) MK1650
            AFU: AF0497(polB) AF0972(dnaQ) AF1722 AF1790 AF2277
            HAL: VNG0521G(polB1) VNG1014G(yqjH) VNG2082G(polC) VNG2338G(polA2)
                 VNG2417G(polA1) VNG6362G(polB2)
            HMA: pNG6176(polB2) rrnAC0540(dinB) rrnAC1831(polB1)
                 rrnAC2691(polA2) rrnAC2714(polA1)
            HWA: HQ1003A(polA1) HQ1220A(polIVx) HQ1705A(polB1) HQ3359A(polIVy)
                 HQ3461A(polA2)
            NPH: NP0084A NP0476A(polA2) NP0482A(polA1) NP0854A NP1508A(polB1)
                 NP2918A
            TAC: Ta0036m Ta0222 Ta0450 Ta0907 Ta1376
            TVO: TVN0035 TVN0823 TVN1045 TVN1372
            PTO: PTO0003 PTO0049 PTO0128 PTO0558 PTO1155
            PHO: PH0121 PH0123 PH1472 PH1947
            PAB: PAB0474 PAB1128(polI) PAB2266 PAB2404
            PFU: PF0018 PF0019 PF0212 PF1385
            TKO: TK0001 TK1902 TK1903 TK2143
            RCI: LRC154(polB-1) RCIX1121(pol2a) RCIX1179(polX)
                 RCIX2734(polB-3) RCIX8(polB-2) RCIX896(pol2b) RRC383(polB-4)
            APE: APE_0099 APE_0427.1 APE_2098.1 APE_2229.1
            IHO: Igni_0062
            HBU: Hbut_1274
            SSO: SSO0081(dpo3) SSO0552(dpo1) SSO1459(dpo2) SSO2275
                 SSO2448(dinP)
            STO: ST0573 ST1426 ST1680 ST2076 ST2238
            SAI: Saci_0074 Saci_0159 Saci_0554(polIV) Saci_1537(dpo1)
            MSE: Msed_0598
            PAI: PAE0651 PAE2109 PAE2180
            PIS: Pisl_0656
            NEQ: NEQ068 NEQ240 NEQ372 NEQ420
STRUCTURES  PDB: 1A5T  1BGX  1BNO  1BNP  1BPB  1BPD  1BPE  1BPX  1BPY  1BPZ  
                 1CLQ  1CMW  1D1U  1D5A  1D8Y  1D9D  1D9F  1DK2  1DK3  1DML  
                 1DPI  1DU2  1EM8  1H15  1HUO  1HUZ  1IG9  1IH7  1IM4  1J53  
                 1J54  1JN3  1JQJ  1JQL  1JR3  1JX4  1JXE  1JXL  1K0P  1K18  
                 1KFD  1KFS  1KLN  1KRP  1KSP  1KTQ  1L3S  1L3T  1L3U  1L3V  
                 1L5U  1LV5  1MMI  1MQ2  1MQ3  1N48  1N5G  1NJF  1NJG  1NJW  
                 1NJX  1NJY  1NJZ  1NK0  1NK4  1NK5  1NK6  1NK7  1NK8  1NK9  
                 1NKB  1NKC  1NKE  1NOM  1NOY  1NOZ  1NZP  1OK7  1Q8I  1Q9X  
                 1Q9Y  1QHT  1QQC  1QSL  1QSS  1QSY  1QTM  1RYR  1RYS  1RZT  
                 1S0M  1S0N  1S0O  1S10  1S5J  1S97  1S9F  1SKR  1SKS  1SKW  
                 1SL0  1SL1  1SL2  1T7P  1T8E  1TAQ  1TAU  1TGO  1TK0  1TK5  
                 1TK8  1TKD  1TV9  1TVA  1U45  1U47  1U48  1U49  1U4B  1UA0  
                 1UA1  1UNN  1VPK  1WAF  1WAJ  1WN7  1WNS  1X9M  1X9S  1X9W  
                 1XC9  1XHX  1XHZ  1XI1  1XSL  1XSN  1XSP  1XWL  1XXH  1XXI  
                 1YYP  1ZD7  1ZDE  1ZJM  1ZJN  1ZQA  1ZQB  1ZQC  1ZQD  1ZQE  
                 1ZQF  1ZQG  1ZQH  1ZQI  1ZQJ  1ZQK  1ZQL  1ZQM  1ZQN  1ZQO  
                 1ZQP  1ZQQ  1ZQR  1ZQS  1ZQT  1ZQU  1ZQV  1ZQW  1ZQX  1ZQY  
                 1ZQZ  1ZYQ  2AE9  2AGO  2AGP  2AGQ  2AJQ  2ALZ  2ASD  2ASJ  
                 2ASL  2ATL  2ATQ  2AU0  2AWA  2AXD  2AYA  2BCQ  2BCR  2BCS  
                 2BCU  2BCV  2BPC  2BPF  2BPG  2BQ3  2BQR  2BQU  2BR0  2C22  
                 2C28  2C2D  2C2E  2C2R  2DPI  2DPJ  2DTU  2DUN  2DY4  2EX3  
                 2FLL  2FLN  2FLP  2FMP  2FMQ  2FMS  2G4C  2GUI  2GV9  2GWS  
                 2HHQ  2HHS  2HHT  2HHU  2HHV  2HHW  2HHX  2HNH  2HPI  2HPM  
                 2HQA  2HTF  2HVH  2HVI  2HW3  2I5O  2I9G  2IA6  2IBK  2IDO  
                 2IHM  2IMW  2ISO  2ISP  2J6S  2J6T  2J6U  2JEF  2JEG  2JEI  
                 2JEJ  2KFN  2KFZ  2KTQ  2KZM  2KZZ  2OH2  2P1J  2P5O  2P66  
                 2PFN  2PFO  2PFP  2PFQ  2POL  2PY5  2PYJ  2PYL  2PZS  2UVR  
                 2UVU  2UVV  2UVW  3BDP  3KTQ  4KTQ  5KTQ  7ICE  7ICF  7ICG  
                 7ICH  7ICI  7ICJ  7ICK  7ICL  7ICM  7ICN  7ICO  7ICP  7ICQ  
                 7ICR  7ICS  7ICT  7ICU  7ICV  8ICA  8ICB  8ICC  8ICE  8ICF  
                 8ICG  8ICH  8ICI  8ICJ  8ICK  8ICL  8ICM  8ICN  8ICO  8ICP  
                 8ICQ  8ICR  8ICS  8ICT  8ICU  8ICV  8ICW  8ICX  8ICY  8ICZ  
                 9ICA  9ICB  9ICC  9ICE  9ICF  9ICG  9ICH  9ICI  9ICJ  9ICK  
                 9ICL  9ICM  9ICN  9ICO  9ICP  9ICQ  9ICR  9ICS  9ICT  9ICU  
                 9ICV  9ICW  9ICX  9ICY  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.7
            ExPASy - ENZYME nomenclature database: 2.7.7.7
            ExplorEnz - The Enzyme Database: 2.7.7.7
            ERGO genome analysis and discovery system: 2.7.7.7
            BRENDA, the Enzyme Database: 2.7.7.7
            CAS: 9012-90-2
///
ENTRY       EC 2.7.7.8                  Enzyme
NAME        polyribonucleotide nucleotidyltransferase;
            polynucleotide phosphorylase;
            PNPase;
            nucleoside diphosphate:polynucleotidyl transferase;
            polyribonucleotide nucleotidyltransferase;
            polynucleotide phosphorylase;
            polyribonucleotide phosphorylase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     polyribonucleotide:phosphate nucleotidyltransferase
REACTION    RNAn+1 + phosphate = RNAn + a nucleoside diphosphate [RN:R07282]
ALL_REAC    R07282 > R00437 R00438 R00439 R00440
SUBSTRATE   RNAn+1 [CPD:C00046];
            phosphate [CPD:C00009]
PRODUCT     RNAn [CPD:C00046];
            nucleoside diphosphate [CPD:C00454]
COMMENT     ADP, IDP, GDP, UDP and CDP can act as donors.
REFERENCE   1
  AUTHORS   Hakim, A.A.
  TITLE     Synthetic activity of polynucleotide phosphorylase from sperm.
  JOURNAL   Nature 183 (1959) 334.
REFERENCE   2  [PMID:13438894]
  AUTHORS   LITTAUER UZ, KORNBERG A.
  TITLE     Reversible synthesis of polyribonucleotides with an enzyme from
            Escherichia coli.
  JOURNAL   J. Biol. Chem. 226 (1957) 1077-92.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Ochoa, S. and Mii, S.
  TITLE     Enzymatic synthesis of polynucleotides. IV. Purification and
            properties of polynucleotide phosphorylase from Azotobacter
            vinelandii.
  JOURNAL   J. Biol. Chem. 236 (1961) 3303-3311.
  ORGANISM  Azotobacter vinelandii
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K00962  polyribonucleotide nucleotidyltransferase
GENES       HSA: 87178(PNPT1)
            PTR: 459247(PNPT1)
            MMU: 71701(Pnpt1)
            RNO: 360992(Pnpt1)
            CFA: 481376(PNPT1)
            GGA: 421206(PNPT1)
            SPU: 583679(LOC583679)
            DME: Dmel_CG11337
            CEL: BE0003N10.1
            ATH: AT5G14580
            OSA: 4342497
            CME: CMH146C CMQ324C
            ECO: b3164(pnp)
            ECJ: JW5851(pnp)
            ECE: Z4525(pnp)
            ECS: ECs4045
            ECC: c3920(pnp)
            ECI: UTI89_C3594(pnp)
            ECP: ECP_3252
            ECV: APECO1_3266(pnp)
            ECW: EcE24377A_3647(pnp)
            ECX: EcHS_A3356 EcHS_A3454(fis)
            STY: STY3463(pnp)
            STT: t3200(pnp)
            SPT: SPA3149(pnp)
            SEC: SC3223(pnp)
            STM: STM3282(pnp)
            YPE: YPO3490(pnp)
            YPK: y0694(pnp)
            YPM: YP_0593(pnp)
            YPA: YPA_2992
            YPN: YPN_0597
            YPP: YPDSF_3299
            YPS: YPTB0484(pnp)
            YPI: YpsIP31758_3592(pnp)
            YEN: YE0438(pnp)
            SFL: SF3205(pnp)
            SFX: S3422(pnp)
            SFV: SFV_3194(pnp)
            SSN: SSON_3310(pnp)
            SBO: SBO_3218(pnp)
            SDY: SDY_3343(pnp)
            ECA: ECA0716(pnp)
            PLU: plu4525(pnp)
            BUC: BU373(pnp)
            BAS: BUsg361(pnp)
            BAB: bbp336(pnp)
            BCC: BCc_227(pnp)
            WBR: WGLp222(pnp)
            SGL: SG0381
            ENT: Ent638_3601
            SPE: Spro_0493
            BFL: Bfl108(pnp)
            BPN: BPEN_112(pnp)
            HIN: HI0229(pnp)
            HIT: NTHI0334(pnp)
            HDU: HD1588(pnp)
            HSO: HS_0703(pnp)
            PMU: PM1114(pnp)
            MSU: MS0493(pnp)
            APL: APL_0577(pnp)
            ASU: Asuc_2061
            XFA: XF0239
            XFT: PD0198(pnp)
            XCC: XCC2507(pnp)
            XCB: XC_1609
            XCV: XCV2833(pnp)
            XAC: XAC2683(pnp)
            XOO: XOO3214(pnp)
            XOM: XOO_3047(XOO3047)
            VCH: VC0647
            VCO: VC0395_A0178(pnp)
            VVU: VV1_1708
            VVY: VV2697
            VPA: VP2452
            VFI: VF0490
            PPR: PBPRA0616
            PAE: PA4740(pnp)
            PAU: PA14_62710(pnp)
            PPU: PP_4708(pnp)
            PPF: Pput_4573
            PST: PSPTO_4486(pnp)
            PSB: Psyr_4176
            PSP: PSPPH_4185(pnp)
            PFL: PFL_0848(pnp)
            PFO: Pfl_0783
            PEN: PSEEN0799(pnp)
            PMY: Pmen_3604
            PAR: Psyc_0074(pnp)
            PCR: Pcryo_0080
            PRW: PsycPRwf_0164
            ACI: ACIAD0402(pnp)
            SON: SO_1209(pnp)
            SDN: Sden_1019
            SFR: Sfri_0995
            SAZ: Sama_0966
            SBL: Sbal_3234
            SBM: Shew185_3275
            SLO: Shew_2822
            SPC: Sputcn32_2829
            SSE: Ssed_3384
            SPL: Spea_3055
            SHE: Shewmr4_1031
            SHM: Shewmr7_1096
            SHN: Shewana3_1035
            SHW: Sputw3181_1075
            ILO: IL0964(pnp)
            CPS: CPS_2207(pnp)
            PHA: PSHAa1001(pnp)
            PAT: Patl_1632
            SDE: Sde_2704
            PIN: Ping_0825
            MAQ: Maqu_3344
            CBU: CBU_0852(pnp)
            CBD: COXBU7E912_0917(pnp)
            LPN: lpg2768(pnp)
            LPF: lpl2685(pnp)
            LPP: lpp2816(pnp)
            MCA: MCA1309(pnp)
            FTU: FTT0699(pnp)
            FTF: FTF0699(pnp)
            FTL: FTL_1537
            FTH: FTH_1487(pnp)
            FTN: FTN_0609(pnp)
            TCX: Tcr_1129
            NOC: Noc_2116
            AEH: Mlg_1944
            HHA: Hhal_1745
            HCH: HCH_01244(pnp)
            CSA: Csal_3070
            ABO: ABO_0333(pnp)
            MMW: Mmwyl1_1031
            AHA: AHA_3299
            DNO: DNO_1047(pnp)
            BCI: BCI_0627(pnp)
            RMA: Rmag_0461
            VOK: COSY_0426(pnp)
            NME: NMB0758
            NMA: NMA0969(pnp)
            NMC: NMC0710(pnp)
            NGO: NGO0335
            CVI: CV_1466(pnp)
            RSO: RSc2067(pnp)
            REU: Reut_A0957
            REH: H16_A1045(pnp)
            RME: Rmet_0923
            BMA: BMA1834(pnp)
            BMV: BMASAVP1_A1125(pnp)
            BML: BMA10299_A0742(pnp)
            BMN: BMA10247_0408(pnp)
            BXE: Bxe_A3218
            BUR: Bcep18194_A5099 Bcep18194_A5581
            BCH: Bcen2424_2253
            BAM: Bamb_2291
            BPS: BPSL1207(pnp)
            BPM: BURPS1710b_1430
            BPL: BURPS1106A_1294(pnp)
            BPD: BURPS668_1285(pnp)
            BTE: BTH_I1056
            BPE: BP0795(pnp)
            BPA: BPP3431(pnp)
            BBR: BB3881(pnp)
            RFR: Rfer_1489
            POL: Bpro_3260
            MPT: Mpe_A1399
            HAR: HEAR1829(pnp)
            MMS: mma_1459
            NEU: NE0172(pnp)
            NET: Neut_2157
            NMU: Nmul_A2553
            EBA: ebA5846(pnp)
            AZO: azo2103(pnp)
            DAR: Daro_2448
            TBD: Tbd_0693
            MFA: Mfla_0071
            HPY: HP1213(pnp)
            HPA: HPAG1_1154
            HHE: HH0594(pnp)
            HAC: Hac_1591(pnp)
            WSU: WS0899(PNP)
            TDN: Tmden_0428
            CJE: Cj1253(pnp)
            CJR: CJE1390(pnp)
            CJJ: CJJ81176_1269(pnp)
            CJU: C8J_1197(pnp)
            CJD: JJD26997_0472(pnp)
            CCV: CCV52592_0953
            CHA: CHAB381_0237
            CCO: CCC13826_0933(pnp)
            ABU: Abu_1183(pnp)
            NIS: NIS_1333(pnp)
            SUN: SUN_1886(pnp)
            GSU: GSU1593(pnp)
            GME: Gmet_1591
            GUR: Gura_1906
            PCA: Pcar_1561
            PPD: Ppro_0968
            DVU: DVU0503(pnp)
            DVL: Dvul_2438
            DDE: Dde_3167
            LIP: LI1006(pnpA)
            BBA: Bd1551(pnp)
            DPS: DP2608
            ADE: Adeh_1107
            AFW: Anae109_1146
            MXA: MXAN_2073(pnpA)
            SAT: SYN_01780
            SFU: Sfum_1234
            RPR: RP504
            RTY: RT0489(pnp)
            RCO: RC0663(pnp)
            RFE: RF_0721(pnp)
            RBE: RBE_0773(pnp)
            RCM: A1E_02925
            OTS: OTBS_0162(pnp)
            WOL: WD0906(pnp)
            WBM: Wbm0019
            AMA: AM526(pnp)
            APH: APH_0767(pnp)
            ERU: Erum3540(pnp)
            ERW: ERWE_CDS_03610(pnp)
            ERG: ERGA_CDS_03570(pnp)
            ECN: Ecaj_0338
            ECH: ECH_0726(pnp)
            NSE: NSE_0057(pnp)
            PUB: SAR11_0392(pnp)
            MLO: mlr5562
            MES: Meso_3935
            PLA: Plav_3632
            SME: SMc00324(pnp)
            SMD: Smed_3446
            ATU: Atu0082(pnpA)
            ATC: AGR_C_124
            RET: RHE_CH00111(pnp)
            RLE: RL0120(pnp)
            BME: BMEI1961
            BMF: BAB1_2169
            BMS: BR2169(pnp)
            BMB: BruAb1_2142(pnp)
            BOV: BOV_2081(pnp)
            OAN: Oant_0743
            BJA: bll0779(pnpA)
            BRA: BRADO0057(pnp)
            BBT: BBta_0062(pnp)
            RPA: RPA0432(pnp)
            RPB: RPB_0605
            RPC: RPC_0484
            RPD: RPD_0227
            RPE: RPE_0192
            NWI: Nwi_0028
            NHA: Nham_0035
            BHE: BH02100(pnp)
            BQU: BQ01980(pnp)
            BBK: BARBAKC583_1258(pnp)
            XAU: Xaut_0288
            CCR: CC_0034
            SIL: SPO3389(pnp)
            SIT: TM1040_0078
            RSP: RSP_1112(pnp)
            RSH: Rsph17029_2774
            RSQ: Rsph17025_2918
            JAN: Jann_4028
            RDE: RD1_0637(pnp)
            MMR: Mmar10_3050
            HNE: HNE_3441(pnpA)
            ZMO: ZMO0549(pnp)
            NAR: Saro_2482
            SAL: Sala_0543
            SWI: Swit_3810
            ELI: ELI_03535
            GOX: GOX1586
            GBE: GbCGDNIH1_2351
            ACR: Acry_0369
            RRU: Rru_A3785
            MAG: amb4117
            MGM: Mmc1_3722
            ABA: Acid345_1995
            BSU: BG11491(pnpA)
            BHA: BH2407(pnpA)
            BAN: BA3944(pnp)
            BAR: GBAA3944(pnp)
            BAA: BA_4415
            BAT: BAS3658
            BCE: BC3805
            BCA: BCE_3845(pnp)
            BCZ: BCZK3566(pnpA)
            BCY: Bcer98_2459
            BTK: BT9727_3548(pnpA)
            BTL: BALH_3435(pnpA)
            BLI: BL01217(pnpA)
            BLD: BLi01894(pnpA)
            BCL: ABC2222(pnpA)
            BAY: RBAM_016530
            BPU: BPUM_1572
            OIH: OB1604(pnpA)
            GKA: GK1269
            SAU: SA1117(pnpA)
            SAV: SAV1274(pnpA)
            SAM: MW1157(pnpA)
            SAR: SAR1250(pnpA)
            SAS: SAS1208
            SAC: SACOL1293(pnp)
            SAB: SAB1136(pnpA)
            SAA: SAUSA300_0486 SAUSA300_1167(pnpA)
            SAO: SAOUHSC_01251
            SAJ: SaurJH9_1334
            SAH: SaurJH1_1360
            SEP: SE0951
            SER: SERP0841(pnp)
            SHA: SH1639(pnpA)
            SSP: SSP1491
            LMO: lmo1331(pnpA)
            LMF: LMOf2365_1348(pnp)
            LIN: lin1368(pnpA)
            LWE: lwe1346(pnpA)
            LLA: L0325(pnpA)
            LLC: LACR_2047
            LLM: llmg_2044(pnpA)
            SPY: SPy_1946(pnpA)
            SPZ: M5005_Spy_1660
            SPM: spyM18_2014(pnp)
            SPG: SpyM3_1676(pnp)
            SPS: SPs1678
            SPH: MGAS10270_Spy1728
            SPI: MGAS10750_Spy1754
            SPJ: MGAS2096_Spy1683
            SPK: MGAS9429_Spy1661
            SPF: SpyM51633(comR)
            SPA: M6_Spy1668
            SPB: M28_Spy1648
            SPN: SP_0588
            SPR: spr0516(pnpA)
            SPD: SPD_0512(pnp)
            SAG: SAG0203(pnp)
            SAN: gbs0198(pnpA)
            SAK: SAK_0266(pnp)
            SMU: SMU.155(pnpA)
            STC: str0081(pnpA)
            STL: stu0081(pnpA)
            SSA: SSA_2049(pnpA)
            SGO: SGO_0344(pnpA)
            EFA: EF3064(pnpA)
            STH: STH1531
            CAC: CAC1808(pnpA)
            CPE: CPE1680(pnpA)
            CPF: CPF_1934(pnpA)
            CPR: CPR_1652(pnpA)
            CTC: CTC01280
            CNO: NT01CX_2130
            CTH: Cthe_0418
            CDF: CD1318(comR)
            CBO: CBO2413(comR)
            CBA: CLB_2276(pnpA)
            CBH: CLC_2259(pnpA)
            CBF: CLI_2468(pnpA)
            CBE: Cbei_1208
            CKL: CKL_1437(pnp)
            AMT: Amet_1001 Amet_1006 Amet_1737 Amet_2667
            CHY: CHY_1758(pnpA)
            DSY: DSY2509
            DRM: Dred_1950
            SWO: Swol_0906
            CSC: Csac_2064
            TTE: TTE1387(pnp)
            MTA: Moth_1056
            POY: PAM251(pnp)
            AYW: AYWB_470(pnp)
            MTU: Rv2783c(gpsI)
            MTC: MT2853(gpsI)
            MBO: Mb2806c(gpsI)
            MBB: BCG_2801c(gpsI)
            MLE: ML0854(gpsI)
            MPA: MAP2891c(gpsI)
            MAV: MAV_3676(gpsI)
            MSM: MSMEG_2656(gpsI)
            MVA: Mvan_2350
            MGI: Mflv_4023
            MMC: Mmcs_2100
            MKM: Mkms_2146
            MJL: Mjls_2083
            CGL: NCgl1900(cgl1975)
            CGB: cg2166(gpsI)
            CEF: CE1868
            CDI: DIP1467(gpsI)
            CJK: jk1132(pnp)
            NFA: nfa38870(pnp)
            RHA: RHA1_ro06655
            SCO: SCO5737(gpsI)
            SMA: SAV2523(pnp)
            TWH: TWT421(gpsI)
            TWS: TW347(pnp)
            LXX: Lxx09030(pnp)
            CMI: CMM_2047(pnpA)
            ART: Arth_1434
            PAC: PPA1471
            NCA: Noca_3177
            TFU: Tfu_0784
            FRA: Francci3_3555
            FAL: FRAAL5753(pnp)
            ACE: Acel_1508
            KRA: Krad_1466
            SEN: SACE_5914
            STP: Strop_1381
            BLO: BL1546(pnpA)
            BAD: BAD_0260(pnpA)
            RXY: Rxyl_1418
            FNU: FN1708
            RBA: RB5804(pnp)
            CTR: CT842(pnp)
            CTA: CTA_0918(pnp)
            CMU: TC0230
            CPN: CPn0999(pnp)
            CPA: CP0855
            CPJ: CPj0999(pnp)
            CPT: CpB1037
            CCA: CCA00762(pnpA)
            CAB: CAB730(pnpA)
            CFE: CF0252(pnp)
            PCU: pc0643(pnp)
            BGA: BG0831(pnpA)
            BAF: BAPKO_0858(pnpA)
            TPA: TP0886
            TDE: TDE1041(pnp)
            LIL: LA0947
            LIC: LIC12701(pnpA)
            LBJ: LBJ_0950(pnp)
            LBL: LBL_2083(pnp)
            SYN: sll1043(pnp)
            SYW: SYNW1897(pnp)
            SYC: syc1666_d(pnp)
            SYF: Synpcc7942_2440
            SYD: Syncc9605_0570
            SYE: Syncc9902_1794
            SYG: sync_2088(pnpA)
            SYR: SynRCC307_0543(pnp)
            SYX: SynWH7803_1908(pnp)
            CYA: CYA_2218(pnpA)
            CYB: CYB_1445(pnpA)
            TEL: tll2193
            GVI: gll3149
            ANA: all4396
            AVA: Ava_1534 Ava_3279
            PMA: Pro1307(pnp)
            PMM: PMM1191(pnp)
            PMT: PMT1377(pnp)
            PMN: PMN2A_0810
            PMI: PMT9312_1292
            PMB: A9601_13841
            PMC: P9515_13631
            PMF: P9303_06021
            PMG: P9301_13921
            PMH: P9215_14051
            PME: NATL1_16651
            TER: Tery_1541
            BTH: BT_2563
            BFR: BF4326
            BFS: BF4129(pnpA)
            PGI: PG0766(pnpA)
            SRU: SRU_1773(pnp)
            CHU: CHU_1786(pnp)
            GFO: GFO_0380(pnpA)
            FJO: Fjoh_1444
            FPS: FP2046(pnp)
            CTE: CT1649(pnp)
            CCH: Cag_1689
            CPH: Cpha266_0552
            PVI: Cvib_1424
            PLT: Plut_1635
            DET: DET0970(pnp)
            DEH: cbdb_A932(pnp)
            DEB: DehaBAV1_0861
            RRS: RoseRS_0949
            RCA: Rcas_3588
            DRA: DR_2063
            DGE: Dgeo_0401
            TTH: TTC0774
            TTJ: TTHA1139
            AAE: aq_221(phpA)
            TMA: TM1345
            TPT: Tpet_1438
            TME: Tmel_1612
            FNO: Fnod_0392
STRUCTURES  PDB: 1E3H  1E3P  1WHU  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.8
            ExPASy - ENZYME nomenclature database: 2.7.7.8
            ExplorEnz - The Enzyme Database: 2.7.7.8
            ERGO genome analysis and discovery system: 2.7.7.8
            BRENDA, the Enzyme Database: 2.7.7.8
            CAS: 9014-12-4
///
ENTRY       EC 2.7.7.9                  Enzyme
NAME        UTP---glucose-1-phosphate uridylyltransferase;
            UDP glucose pyrophosphorylase;
            glucose-1-phosphate uridylyltransferase;
            UDPG phosphorylase;
            UDPG pyrophosphorylase;
            uridine 5'-diphosphoglucose pyrophosphorylase;
            uridine diphosphoglucose pyrophosphorylase;
            uridine diphosphate-D-glucose pyrophosphorylase;
            uridine-diphosphate glucose pyrophosphorylase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     UTP:alpha-D-glucose-1-phosphate uridylyltransferase
REACTION    UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
            [RN:R00289]
ALL_REAC    R00289
SUBSTRATE   UTP [CPD:C00075];
            alpha-D-glucose 1-phosphate [CPD:C00103]
PRODUCT     diphosphate [CPD:C00013];
            UDP-glucose [CPD:C00029]
REFERENCE   1  [PMID:13115434]
  AUTHORS   KALCKAR HM.
  TITLE     The role of phosphoglycosyl compounds in the biosynthesis of
            nucleosides and nucleotides.
  JOURNAL   Biochim. Biophys. Acta. 12 (1953) 250-64.
  ORGANISM  Saccharomyces fragilis
REFERENCE   2  [PMID:4284510]
  AUTHORS   Kamogawa A, Kurahashi K.
  TITLE     Purification and properties of uridinediphosphate glucose
            pyrophosphorylase from Escherichia coli K12.
  JOURNAL   J. Biochem. (Tokyo). 57 (1965) 758-65.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:6304512]
  AUTHORS   Lobelle-Rich PA, Reeves RE.
  TITLE     Separation and characterization of two UTP-utilizing hexose
            phosphate uridylyltransferases from Entamoeba histolytica.
  JOURNAL   Mol. Biochem. Parasitol. 7 (1983) 173-82.
  ORGANISM  Entamoeba histolytica [GN:ehi]
REFERENCE   4  [PMID:13260264]
  AUTHORS   SMITH EE, MILLS GT.
  TITLE     The uridyl transferase of mammary gland.
  JOURNAL   Biochim. Biophys. Acta. 18 (1955) 152.
  ORGANISM  Saccharomyces fragilis, rat [GN:rno]
REFERENCE   5  [PMID:4436332]
  AUTHORS   Turnquist RL, Gillett TA, Hansen RG.
  TITLE     Uridine diphosphate glucose pyrophosphorylase. Crystallization and
            properties of the enzyme from rabbit liver and species comparisons.
  JOURNAL   J. Biol. Chem. 249 (1974) 7695-700.
  ORGANISM  rabbit
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00052  Galactose metabolism
            PATH: map00500  Starch and sucrose metabolism
            PATH: map00520  Nucleotide sugars metabolism
ORTHOLOGY   KO: K00963  UTP--glucose-1-phosphate uridylyltransferase
GENES       HSA: 7360(UGP2)
            MMU: 216558(Ugp2)
            CFA: 474615(UGP2)
            BTA: 281565(UGP2)
            SSC: 397040(UGP2)
            GGA: 373900(UGP2)
            XLA: 398814(MGC68615) 446468(ugp2)
            XTR: 493237(ugp2)
            DRE: 334420(zgc:85662)
            SPU: 576855(LOC576855)
            DME: Dmel_CG4347(UGP)
            CEL: K08E3.5
            ATH: AT5G17310
            OSA: 4347800
            CME: CMS159C
            SCE: YHL012W YKL035W(UGP1)
            AGO: AGOS_AGL082W
            PIC: PICST_40866(UGP1)
            CGR: CAGL0L01925g
            SPO: SPCC1322.04 SPCC794.10
            ANI: AN9148.2
            AFM: AFUA_7G01830
            AOR: AO090038000558
            CNE: CNC03700
            UMA: UM05584.1
            ECU: ECU03_0280
            DDI: DDB_0214911(ugpB)
            TBR: Tb10.389.0330
            TCR: 503521.50 506359.60
            LMA: LmjF18.0990
            EHI: 106.t00014
            ECO: b1236(galU) b2042(galF)
            ECJ: JW1224(galU) JW2027(galF)
            ECE: Z2012(galU) Z3205(galF)
            ECS: ECs1738 ECs2846
            ECC: c1700(galU) c2567(galF)
            ECI: UTI89_C1432(galU) UTI89_C2314(galF)
            ECP: ECP_1283 ECP_2082
            ECV: APECO1_1132(galF) APECO1_350(galU)
            ECW: EcE24377A_1385(galU)
            ECX: EcHS_A1344(galU)
            STY: STY1298(galU) STY2308(galF)
            STT: t0774(galF) t1663(galU)
            SPT: SPA1126(galU)
            SEC: SC1747(galU) SC2099(galF)
            STM: STM1752(galU) STM2098(galF)
            YPE: YPO1539(galU) YPO1540(galF)
            YPK: y2630(galF) y2631(galU)
            YPM: YP_1428(galU1) YP_1429(galF)
            YPA: YPA_0834 YPA_0835
            YPN: YPN_2440 YPN_2441
            YPP: YPDSF_1437
            YPS: YPTB1551(galU) YPTB1552(galF)
            YPI: YpsIP31758_2438(galU)
            SFL: SF1236(galU) SF2105(galF)
            SFX: S1322(galU) S2228(galF)
            SFV: SFV_1249(galU) SFV_2099(galF)
            SSN: SSON_1943(galU)
            SBO: SBO_0869(galF) SBO_1833(galU)
            SDY: SDY_1288(galU) SDY_2203(galF)
            ECA: ECA1443(galF) ECA2329(galU)
            PLU: plu2501(galU)
            WBR: WGLp369(galU)
            SGL: SG1113 SG1367
            ENT: Ent638_2307 Ent638_2656
            HIN: HI0812(galU)
            HIT: NTHI0976(galU)
            HDU: HD1431(galU)
            HSO: HS_1117(galU)
            PMU: PM1289(galU)
            MSU: MS0345(galU)
            APL: APL_0651(galU)
            XFA: XF2432
            XFT: PD1450(gtaB)
            XCC: XCC2188(galU)
            XCB: XC_1930
            XCV: XCV2490(galU)
            XAC: XAC2292(galU)
            XOO: XOO2186(galU)
            XOM: XOO_2056(XOO2056)
            VCH: VC0395
            VCO: VC0395_A2813(galU)
            VVU: VV1_1428
            VVY: VV0366 VV2955
            VPA: VP0237 VP2711
            VFI: VF0342
            PPR: PBPRA2674(galU)
            PAE: PA2023(galU)
            PAU: PA14_38350(galU)
            PAP: PSPA7_3265(galU)
            PPU: PP_3821(galU)
            PST: PSPTO_3113(galU)
            PSB: Psyr_2980
            PSP: PSPPH_2260(galU)
            PFL: PFL_3399(galU)
            PFO: Pfl_2929 Pfl_3835
            PEN: PSEEN2294(galU)
            PAR: Psyc_0108(galU)
            PCR: Pcryo_0117
            ACI: ACIAD0099(galU)
            SON: SO_1665(galU)
            SDN: Sden_2596
            SFR: Sfri_1389 Sfri_2823
            SAZ: Sama_2223
            SBL: Sbal_1483
            SBM: Shew185_1478
            SLO: Shew_1434
            SPC: Sputcn32_1385
            SSE: Ssed_2931
            SPL: Spea_1447
            SHE: Shewmr4_2608
            SHM: Shewmr7_2675
            SHN: Shewana3_2782
            SHW: Sputw3181_2716
            ILO: IL1094(galU)
            CPS: CPS_0593(galU1) CPS_2107(galU2)
            PHA: PSHAa0750(galU)
            PAT: Patl_3199
            SDE: Sde_1000
            PIN: Ping_1064
            MAQ: Maqu_1672
            CBU: CBU_0849(galU)
            CBD: COXBU7E912_0914(galU)
            MCA: MCA2203(galU)
            FTU: FTT0757(galU)
            FTF: FTF0757(galU)
            FTW: FTW_0667(galU)
            FTL: FTL_1357
            FTH: FTH_1320(galU)
            FTA: FTA_1435(galU)
            FTN: FTN_0729(galU)
            TCX: Tcr_0607
            NOC: Noc_2280
            AEH: Mlg_2473
            HHA: Hhal_2195
            HCH: HCH_04897(galU)
            CSA: Csal_1859
            ABO: ABO_0934(galU)
            MMW: Mmwyl1_3531
            AHA: AHA_3499(galU)
            DNO: DNO_0327(galU)
            VOK: COSY_0811(galU)
            NME: NMB0638
            NMA: NMA0848(galU)
            NMC: NMC0581(galU)
            NGO: NGO0220
            CVI: CV_3901(galU)
            RSO: RSc2237(galU1) RSp0006(galU2)
            REU: Reut_A0862
            REH: H16_A2752(galU)
            RME: Rmet_2631
            BMA: BMA0926(galU-1) BMAA1702(galU-2)
            BMV: BMASAVP1_1669(galU-2) BMASAVP1_A1459(galU-1)
            BML: BMA10299_1877(galU-2) BMA10299_A0423(galU-1)
            BMN: BMA10247_0740(galU-1) BMA10247_A0549(galU-2)
            BXE: Bxe_A1334 Bxe_A2225 Bxe_B1737 Bxe_C1095
            BVI: Bcep1808_1402
            BUR: Bcep18194_A4584 Bcep18194_B2109 Bcep18194_C7385
            BCN: Bcen_0958 Bcen_4390
            BCH: Bcen2424_1440 Bcen2424_3977
            BAM: Bamb_1320 Bamb_3367
            BPS: BPSL1981(galU) BPSL2769 BPSS1682(gtaB)
            BPM: BURPS1710b_1845(galU) BURPS1710b_3261(galU)
                 BURPS1710b_A0749(galU-2)
            BPL: BURPS1106A_1690(galU) BURPS1106A_3248(galU)
                 BURPS1106A_A2283(galU)
            BPD: BURPS668_1668(galU) BURPS668_3209(galU) BURPS668_A2422(galU)
            BTE: BTH_I1363(galU-1) BTH_I2634(galU-2) BTH_II0699(galU-3)
            PNU: Pnuc_1717
            BPE: BP3403
            BPA: BPP3556
            BBR: BB3991
            POL: Bpro_3723
            PNA: Pnap_3175
            AAV: Aave_1991
            AJS: Ajs_2897
            VEI: Veis_1034
            MPT: Mpe_A1135
            HAR: HEAR1329(galU)
            MMS: mma_2064(galU)
            NEU: NE1382(galU1) NE1383(galU1)
            NET: Neut_0698
            NMU: Nmul_A0648 Nmul_A0680
            EBA: ebA6378(epsT)
            AZO: azo2000(galU)
            DAR: Daro_1735
            TBD: Tbd_0625
            MFA: Mfla_1279
            HPY: HP0646(galU)
            HPA: HPAG1_0631
            HHE: HH0578(galU)
            HAC: Hac_1068(galU)
            WSU: WS0340(galU)
            TDN: Tmden_1473
            CJE: Cj1536c(galU)
            CJR: CJE1707(galU)
            CJJ: CJJ81176_1521(galU)
            CJU: C8J_1435(galU)
            CJD: JJD26997_1888(galU)
            CFF: CFF8240_0078(galU)
            CCV: CCV52592_2201(galU)
            CHA: CHAB381_0523(galU)
            CCO: CCC13826_0429(galU)
            ABU: Abu_0839(galU)
            NIS: NIS_0555
            SUN: SUN_1936(galU)
            GSU: GSU0859(galU)
            GME: Gmet_1159
            DVU: DVU1283(galU) DVU2322
            DVL: Dvul_0936
            DDE: Dde_1315 Dde_1518
            LIP: LI0193(galU)
            BBA: Bd3773(galF)
            DPS: DP0022 DPPB68
            ADE: Adeh_3469
            MXA: MXAN_1425(galU)
            PUB: SAR11_1087(galU)
            MLO: mll3025 mlr5275
            MES: Meso_0659 Meso_2739
            SME: SMb20960(exoN) SMc04023(exoN2)
            SMD: Smed_2707
            ATU: Atu3778(galU) Atu4050(exoN)
            ATC: AGR_L_1611(exoN) AGR_L_2114(exoN)
            RET: RHE_CH03561(exoN)
            RLE: RL4081(exoN)
            BME: BMEII0023
            BMF: BAB2_0070(galU)
            BMS: BRA0071(galU)
            BMB: BruAb2_0071(galU)
            BOV: BOV_A0066(galU)
            BJA: blr1499(exoN)
            BRA: BRADO1089(galU)
            BBT: BBta_6959(galU)
            RPA: RPA0887(exoN)
            RPB: RPB_4535
            RPC: RPC_0765
            RPD: RPD_0870
            RPE: RPE_0687
            NWI: Nwi_2958
            NHA: Nham_1131
            BHE: BH01750(galU)
            BQU: BQ01640(galU)
            BBK: BARBAKC583_0334(galU)
            XAU: Xaut_0389
            CCR: CC_3637
            SIT: TM1040_0015
            RSP: RSP_1159(galU) RSP_2565(ugpG)
            RSH: Rsph17029_1224 Rsph17029_2820
            RSQ: Rsph17025_1957
            JAN: Jann_0218
            RDE: RD1_0374(gtaB)
            MMR: Mmar10_2491
            HNE: HNE_1147(galU)
            ZMO: ZMO1767(celA)
            SWI: Swit_2861
            GOX: GOX0044
            GBE: GbCGDNIH1_0589
            RRU: Rru_A2117
            MAG: amb0577 amb4451
            MGM: Mmc1_0335
            ABA: Acid345_4550
            SUS: Acid_6549
            BSU: BG10402(gtaB) BG11199(ytdA) BG13453(yngB)
            BHA: BH2303 BH3652 BH3717(gtaB)
            BAN: BA5152(gtaB)
            BAR: GBAA5152(gtaB) GBAA_pXO1_0129(galU)
            BAA: BA_0025 BXA0129(galU)
            BAT: BAS4789
            BCE: BC4918 BC5275
            BCA: BCE_5057(gtaB) BCE_5396(galU)
            BCZ: BCZK4650(gtaB)
            BTK: BT9727_4630(gtaB) BT9727_4956(gtaB)
            BTL: BALH_4458(gtaB) BALH_4779(gtaB)
            BLI: BL02431(gtaB) BL02664(yngB)
            BLD: BLi01281(yngB) BLi03813(gtaB)
            BCL: ABC3098 ABC3698(gtaB)
            BAY: RBAM_032820(gtaB)
            BPU: BPUM_3219(gtaB)
            OIH: OB2894 OB2930
            GKA: GK3269 GK3320
            GTN: GTNG_3200
            SAU: SA2288(gtaB)
            SAV: SAV2500(gtaB)
            SAM: MW2419(gtaB)
            SAR: SAR2579(gtaB)
            SAS: SAS2386
            SAC: SACOL2508(galU)
            SAB: SAB2374c(gtaB)
            SAA: SAUSA300_2439(galU)
            SAO: SAOUHSC_02801
            SAJ: SaurJH9_2524
            SEP: SE2043
            SER: SERP2056(galU)
            SHA: SH0579(gtaB)
            SSP: SSP0059 SSP2021
            LMO: lmo1078
            LMF: LMOf2365_1099(galU)
            LIN: lin1070
            LWE: lwe1059(galU)
            LLA: L177590(hasC)
            LLC: LACR_1462
            LLM: llmg_1113(galU)
            SPY: SPy_0224(hasC.2) SPy_2202(hasC)
            SPZ: M5005_Spy_0192(hasC.2) M5005_Spy_1853(hasC)
            SPM: spyM18_0210(hasC2) spyM18_2240(hasC)
            SPG: SpyM3_0160(hasC.2) SpyM3_1853(hasC)
            SPS: SPs0166 SPs1849
            SPH: MGAS10270_Spy0192(hasC2) MGAS10270_Spy1973(hasC)
            SPI: MGAS10750_Spy0188(hasC)
            SPJ: MGAS2096_Spy0205(hasC2) MGAS2096_Spy1884(hasC)
            SPK: MGAS9429_Spy0194(hasC2) MGAS9429_Spy1864(hasC)
            SPF: SpyM50172(hasC2) SpyM51826(hasC1)
            SPA: M6_Spy0224 M6_Spy1871
            SPB: M28_Spy0187(hasC.2) M28_Spy1886(hasC)
            SPN: SP_2092
            SPR: spr1903(galU)
            SPD: SPD_1919(galU)
            SAG: SAG0406(galU)
            SAN: gbs0441
            SAK: SAK_0479(galU)
            SMU: SMU.322c
            STC: str1833(galU)
            STL: stu1833(galU)
            STE: STER_1810
            SSA: SSA_2169(galU)
            SSU: SSU05_2041
            SSV: SSU98_2041
            SGO: SGO_0163(galU)
            LPL: lp_0757(galU)
            LJO: LJ1593
            LAC: LBA0625 LBA1719
            LSA: LSA1507(galU)
            LSL: LSL_1268(galU)
            LDB: Ldb0558(galU)
            LBU: LBUL_0498
            LBR: LVIS_0644
            LCA: LSEI_1093
            LGA: LGAS_0702
            LRE: Lreu_0372
            PPE: PEPE_0444
            EFA: EF1746(galU)
            OOE: OEOE_0565
            LME: LEUM_0599
            STH: STH2713
            CAC: CAC2250 CAC2335
            CPE: CPE0506(galF) CPE0510(galF)
            CPF: CPF_0483(galU) CPF_0487(galU)
            CPR: CPR_0465(galU) CPR_0469(galU)
            CTC: CTC02269
            CNO: NT01CX_1540(galU) NT01CX_1778(galU)
            CTH: Cthe_2183
            CDF: CD2715(gtaB) CD3488(gtaB)
            CBO: CBO3112(gtaB)
            CBA: CLB_3143(galU)
            CBH: CLC_3016(galU)
            CBF: CLI_3172(galU)
            CKL: CKL_3178(galU)
            CHY: CHY_2582(galU)
            DSY: DSY3353
            DRM: Dred_3101
            PTH: PTH_2768(galU)
            CSC: Csac_1600
            TTE: TTE0732(galU)
            MTA: Moth_1369
            MGE: MG_453(gtaB)
            MPN: MPN667(gtaB)
            MPE: MYPE160
            MMY: MSC_0110(galU) MSC_0990(galU)
            MMO: MMOB1170(galU)
            MCP: MCAP_0064
            MTU: Rv0993(galU)
            MTC: MT1022(galU)
            MBO: Mb1020(galU)
            MBB: BCG_1048(galU)
            MLE: ML0182(galU)
            MPA: MAP0924(galU)
            MSM: MSMEG_5471(galU)
            MMC: Mmcs_4290
            CGL: NCgl0356(cgl0367) NCgl0846(cgl0882)
            CGB: cg0442(galU2) cg1004(galU1)
            CEF: CE0620 CE0956
            CDI: DIP0862
            CJK: jk1525(galU)
            NFA: nfa17780 nfa49530(galU)
            RHA: RHA1_ro05437(galU1) RHA1_ro05632(galU2)
            SCO: SCO3182(gtaB)
            SMA: SAV3673(gtaB)
            LXX: Lxx05910(galU)
            CMI: CMM_2446(galU)
            AAU: AAur_2852(galU) AAur_pTC20227(galU)
            PAC: PPA0489
            NCA: Noca_0790
            TFU: Tfu_0373
            FRA: Francci3_4040
            FAL: FRAAL6397(galU)
            ACE: Acel_0166
            SEN: SACE_0774(galU)
            BLO: BL0739(ugpA)
            BAD: BAD_0816(ugpA)
            FNU: FN1266
            RBA: RB9094(hasC)
            BGA: BG0209(gtaB)
            BAF: BAPKO_0214(gtaB)
            LIL: LB262(galF)
            LIC: LIC20199(galU)
            LBJ: LBJ_4113
            LBL: LBL_4129
            ANA: all3274
            AVA: Ava_4927
            TER: Tery_2112
            AAE: aq_1705(galF)
            MMP: MMP1091
            MAC: MA4459
            MBA: Mbar_A1121 Mbar_A2905
            MMA: MM_1133
            MBU: Mbur_1612
            MHU: Mhun_2114 Mhun_3079
            MTH: MTH634
            MST: Msp_1101
            MSI: Msm_1604
            PTO: PTO0307
            PAB: PAB0771
            PFU: PF0770 PF1356
            SSO: SSO0813
STRUCTURES  PDB: 2E3D  2I5K  2ICX  2ICY  2OEF  2OEG  2PA4  2Q4J  2UX8  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.9
            ExPASy - ENZYME nomenclature database: 2.7.7.9
            ExplorEnz - The Enzyme Database: 2.7.7.9
            ERGO genome analysis and discovery system: 2.7.7.9
            BRENDA, the Enzyme Database: 2.7.7.9
            CAS: 9026-22-6
///
ENTRY       EC 2.7.7.10                 Enzyme
NAME        UTP---hexose-1-phosphate uridylyltransferase;
            galactose-1-phosphate uridylyltransferase;
            galactose 1-phosphate uridylyltransferase;
            alpha-D-galactose 1-phosphate uridylyltransferase;
            galactose 1-phosphate uridyltransferase;
            UDPgalactose pyrophosphorylase;
            uridine diphosphate galactose pyrophosphorylase;
            uridine diphosphogalactose pyrophosphorylase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     UTP:alpha-D-hexose-1-phosphate uridylyltransferase
REACTION    UTP + alpha-D-galactose 1-phosphate = diphosphate + UDP-galactose
            [RN:R00502]
ALL_REAC    R00502
SUBSTRATE   UTP [CPD:C00075];
            alpha-D-galactose 1-phosphate [CPD:C00446]
PRODUCT     diphosphate [CPD:C00013];
            UDP-galactose [CPD:C00052]
COMMENT     alpha-D-Glucose 1-phosphate can also act as acceptor, but more
            slowly.
REFERENCE   1  [PMID:13549431]
  AUTHORS   ISSELBACHER KJ.
  TITLE     A mammalian uridinediphosphate galactose pyrophosphorylase.
  JOURNAL   J. Biol. Chem. 232 (1958) 429-44.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:13115434]
  AUTHORS   KALCKAR HM.
  TITLE     The role of phosphoglycosyl compounds in the biosynthesis of
            nucleosides and nucleotides.
  JOURNAL   Biochim. Biophys. Acta. 12 (1953) 250-64.
  ORGANISM  Saccharomyces fragilis
REFERENCE   3  [PMID:500588]
  AUTHORS   Lee L, Kimura A, Tochikura T.
  TITLE     Purification and properties of UDP-glucose (UDP-galactose)
            pyrophosphorylase from Bifidobacterium bifidum.
  JOURNAL   J. Biochem. (Tokyo). 86 (1979) 923-8.
  ORGANISM  Bifidobacterium bifidum
REFERENCE   4  [PMID:6304512]
  AUTHORS   Lobelle-Rich PA, Reeves RE.
  TITLE     Separation and characterization of two UTP-utilizing hexose
            phosphate uridylyltransferases from Entamoeba histolytica.
  JOURNAL   Mol. Biochem. Parasitol. 7 (1983) 173-82.
  ORGANISM  Entamoeba histolytica [GN:ehi]
PATHWAY     PATH: map00052  Galactose metabolism
            PATH: map00520  Nucleotide sugars metabolism
ORTHOLOGY   KO: K00964  galactose-1-phosphate uridylyltransferase
GENES       ATH: AT5G18200
            OSA: 4342514
            CME: CMQ030C
            ANI: AN6182.2
            AFM: AFUA_2G11560
            AOR: AO090026000490
            CNE: CNM00620
            DDI: DDBDRAFT_0204814
            ECP: ECP_0769
            ECW: EcE24377A_0785(galT)
            ECX: EcHS_A0812(galT)
            YPI: YpsIP31758_2856(galT)
            MSU: MS0647(galT)
            VCO: VC0395_A1198(galT)
            VVU: VV1_1771
            VVY: VV2638
            VFI: VFA0353 VFA0354
            FTW: FTW_0623(galT)
            FTA: FTA_1483(galT)
            FTN: FTN_0686(galT)
            TBD: Tbd_0601
            NIS: NIS_0939(galT)
            SUN: SUN_1272(galT)
            GSU: GSU3256(galT)
            GME: Gmet_3176
            PCA: Pcar_2956
            ABA: Acid345_0343
            BSU: BG10582(galT)
            BHA: BH1109(galT)
            BCZ: pE33L466_0356(galT)
            BLI: BL00193(galT)
            BLD: BLi04284(galT)
            BAY: RBAM_012130(galT1)
            BPU: BPUM_3466(galT)
            GKA: GK2148
            SSP: SSP0631
            LLA: L0027(galT)
            LLC: LACR_2243
            LLM: llmg_1726 llmg_2234(galT)
            SPN: SP_1829 SP_1852
            SPR: spr1648(galT) spr1667(galT)
            SPD: SPD_1613(galT-1) SPD_1633(galT-2)
            SAK: SAK_0537(galT)
            SMU: SMU.887(galT)
            STC: str1401(galT)
            STL: stu1401(galT)
            SSA: SSA_1009(galT)
            SGO: SGO_0933(galT)
            LPL: lp_3480(galT)
            LJO: LJ0860
            LAC: LBA1458(galT)
            LSA: LSA0766(galT)
            LSL: LSL_0383
            LBR: LVIS_1902
            LCA: LSEI_0666
            EFA: EF1071(galT)
            OOE: OEOE_0303
            CAC: CAC2844(galT) CAC2961(galT)
            CPE: CPE1346(galT)
            CPF: CPF_1553(galT)
            CPR: CPR_1346
            CTC: CTC00864
            TTE: TTE0273(galT) TTE1929
            MTU: Rv0618(galTa) Rv0619(galTb)
            MBO: Mb0635(galT)
            MBB: BCG_0665(galT)
            MPA: MAP4071(galT)
            MAV: MAV_4565(galT)
            MSM: MSMEG_3691(galT)
            CDI: DIP1014(galT)
            CJK: jk0290(galT)
            NFA: nfa11640(galT)
            SCO: SCO3138(galT)
            SMA: SAV3576(galT)
            AAU: AAur_1280(galT)
            SEN: SACE_0764(galT)
            BLO: BL1211(galT1) BL1643(galT2)
            BAD: BAD_1332(galT1)
            FNU: FN2108
            RBA: RB6656(galT)
            SRU: SRU_1285(galT)
            TTH: TT_P0071
            TTJ: TTHB114
            TMA: TM0896 TM1191
            MAC: MA3680
            MBA: Mbar_A0295
            MMA: MM_0586
            MBU: Mbur_0434
            PFU: PF0441
            TKO: TK1828
            RCI: RCIX1322(galT)
            PAI: PAE1184
STRUCTURES  PDB: 1GUP  1GUQ  1HXP  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.10
            ExPASy - ENZYME nomenclature database: 2.7.7.10
            ExplorEnz - The Enzyme Database: 2.7.7.10
            ERGO genome analysis and discovery system: 2.7.7.10
            BRENDA, the Enzyme Database: 2.7.7.10
            CAS: 9016-11-9
///
ENTRY       EC 2.7.7.11                 Enzyme
NAME        UTP---xylose-1-phosphate uridylyltransferase;
            xylose-1-phosphate uridylyltransferase;
            uridylyltransferase, xylose 1-phosphate;
            UDP-xylose pyrophosphorylase;
            uridine diphosphoxylose pyrophosphorylase;
            xylose 1-phosphate uridylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     UTP:alpha-D-xylose-1-phosphate uridylyltransferase
REACTION    UTP + alpha-D-xylose 1-phosphate = diphosphate + UDP-xylose
            [RN:R01471]
ALL_REAC    R01471
SUBSTRATE   UTP [CPD:C00075];
            alpha-D-xylose 1-phosphate [CPD:C03737]
PRODUCT     diphosphate [CPD:C00013];
            UDP-xylose [CPD:C00190]
REFERENCE   1  [PMID:16578456]
  AUTHORS   Ginsburg V, Neufeld EF, Hassid WZ.
  TITLE     ENZYMATIC SYNTHESIS OF URIDINE DIPHOSPHATE XYLOSE AND URIDINE
            DIPHOSPHATE ARABINOSE.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 42 (1956) 333-5.
  ORGANISM  Vigna radiata
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.11
            ExPASy - ENZYME nomenclature database: 2.7.7.11
            ExplorEnz - The Enzyme Database: 2.7.7.11
            ERGO genome analysis and discovery system: 2.7.7.11
            BRENDA, the Enzyme Database: 2.7.7.11
            CAS: 9026-20-4
///
ENTRY       EC 2.7.7.12                 Enzyme
NAME        UDP-glucose---hexose-1-phosphate uridylyltransferase;
            uridyl transferase;
            hexose-1-phosphate uridylyltransferase;
            uridyltransferase;
            hexose 1-phosphate uridyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase
REACTION    UDP-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose
            1-phosphate + UDP-galactose [RN:R00955]
ALL_REAC    R00955
SUBSTRATE   UDP-glucose [CPD:C00029];
            alpha-D-galactose 1-phosphate [CPD:C00446]
PRODUCT     alpha-D-glucose 1-phosphate [CPD:C00103];
            UDP-galactose [CPD:C00052]
REFERENCE   1  [PMID:13111247]
  AUTHORS   KALCKAR HM, BRAGANCA B, MUNCH-PETERSEN HM.
  TITLE     Uridyl transferases and the formation of uridine diphosphogalactose.
  JOURNAL   Nature. 172 (1953) 1038.
REFERENCE   2  [PMID:14412847]
  AUTHORS   KURAHASHI K, SUGIMURA A.
  TITLE     Purification and properties of galactose 1-phosphate uridyl
            transferase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 235 (1960) 940-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Mayes, J.S. and Hansen, R.G.
  TITLE     Galactose 1-phosphate uridyl transferase.
  JOURNAL   Methods Enzymol. 9 (1966) 708-713.
  ORGANISM  cow [GN:bta], human [GN:hsa], Saccharomyces cerevisiae [GN:sce]
REFERENCE   4  [PMID:5338129]
  AUTHORS   Saito S, Ozutsumi M, Kurahashi K.
  TITLE     Galactose 1-phosphate uridylyltransferase of Escherichia coli. II.
            Further purification and characterization.
  JOURNAL   J. Biol. Chem. 242 (1967) 2362-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:13260264]
  AUTHORS   SMITH EE, MILLS GT.
  TITLE     The uridyl transferase of mammary gland.
  JOURNAL   Biochim. Biophys. Acta. 18 (1955) 152.
  ORGANISM  Saccharomyces fragilis, rat [GN:rno]
PATHWAY     PATH: map00052  Galactose metabolism
            PATH: map00520  Nucleotide sugars metabolism
ORTHOLOGY   KO: K00965  UDPglucose--hexose-1-phosphate uridylyltransferase
GENES       HSA: 2592(GALT)
            MMU: 14430(Galt)
            CFA: 474751(GALT)
            CEL: ZK1058.3
            SCE: YBR018C(GAL7)
            PIC: PICST_57493(GAL7)
            SPO: SPBPB2B2.10c
            UMA: UM01875.1
            ECO: b0758(galT)
            ECJ: JW0741(galT)
            ECE: Z0928(galT)
            ECS: ECs0786
            ECC: c0834(galT)
            ECI: UTI89_C0755(galT)
            ECV: APECO1_1330(galT)
            STY: STY0808(galT)
            STT: t2112(galT)
            SPT: SPA1977(galT)
            SEC: SC0773(galT)
            STM: STM0775(galT)
            YPE: YPO1138(galT)
            YPK: y3044(galT)
            YPM: YP_1021(galT)
            YPA: YPA_1046
            YPN: YPN_2862
            YPP: YPDSF_2559
            YPS: YPTB1170(galT)
            SFL: SF0546(galT)
            SFX: S0554(galT)
            SFV: SFV_0582(galT)
            SSN: SSON_0710(galT)
            SBO: SBO_0613(galT)
            SDY: SDY_0705(galT)
            ECA: ECA3171(galT)
            PLU: plu0575(galT)
            ENT: Ent638_1249
            SPE: Spro_1292
            HIN: HI0820(galT)
            HIT: NTHI0984(galT)
            HIP: CGSHiEE_07960
            HIQ: CGSHiGG_07610
            PMU: PM1036(galT)
            APL: APL_0994(galT)
            ASU: Asuc_1899
            VCH: VC1596
            VVU: VV2_1094
            VVY: VVA1617
            VPA: VP2399
            PPR: PBPRA2081
            SBM: Shew185_3337
            SLO: Shew_2288
            SSE: Ssed_2341
            SPL: Spea_1631
            PHA: PSHAa1770(galT)
            PAT: Patl_0648
            SDE: Sde_1098
            PIN: Ping_2016
            FTU: FTT1475(galT)
            FTF: FTF1475(galT)
            FTL: FTL_1396
            FTH: FTH_1358(galT)
            AHA: AHA_4104(galT)
            NMU: Nmul_A1939
            GUR: Gura_0857
            PPD: Ppro_0026
            DDE: Dde_3652
            ADE: Adeh_0134
            AFW: Anae109_0138
            PLA: Plav_1933
            NAR: Saro_0543
            ABA: Acid345_1703
            SUS: Acid_4361 Acid_7827
            BCL: ABC3220(galT)
            BAY: RBAM_035450(galT)
            SSA: SSA_1009(galT)
            LRE: Lreu_1776
            CBE: Cbei_4421
            CSC: Csac_1510
            MTA: Moth_1935
            RHA: RHA1_ro05491(galT)
            ART: Arth_1162
            FRA: Francci3_3452
            FAL: FRAAL5627(galT)
            ACE: Acel_1675
            KRA: Krad_3972
            GFO: GFO_2147(galT)
            FJO: Fjoh_1113
            RRS: RoseRS_2890 RoseRS_3828
            RCA: Rcas_0974 Rcas_1885
            DGE: Dgeo_2480
            TPT: Tpet_0031 Tpet_1561
            TME: Tmel_0076 Tmel_0424
            FNO: Fnod_0305 Fnod_0416
            SMR: Smar_1154
            PCL: Pcal_0777
            PAS: Pars_0315
            TPE: Tpen_1112
STRUCTURES  PDB: 1HXQ  2H39  2Q4H  2Q4L  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.12
            ExPASy - ENZYME nomenclature database: 2.7.7.12
            ExplorEnz - The Enzyme Database: 2.7.7.12
            ERGO genome analysis and discovery system: 2.7.7.12
            BRENDA, the Enzyme Database: 2.7.7.12
            CAS: 9026-21-5
///
ENTRY       EC 2.7.7.13                 Enzyme
NAME        mannose-1-phosphate guanylyltransferase;
            GTP-mannose-1-phosphate guanylyltransferase;
            PIM-GMP (phosphomannose isomerase-guanosine 5'-diphospho-D-mannose
            pyrophosphorylase);
            GDP-mannose pyrophosphorylase;
            guanosine 5'-diphospho-D-mannose pyrophosphorylase;
            guanosine diphosphomannose pyrophosphorylase;
            guanosine triphosphate-mannose 1-phosphate guanylyltransferase;
            mannose 1-phosphate guanylyltransferase (guanosine triphosphate)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     GTP:alpha-D-mannose-1-phosphate guanylyltransferase
REACTION    GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
ALL_REAC    (other) R00885
SUBSTRATE   GTP [CPD:C00044];
            alpha-D-mannose 1-phosphate [CPD:C00636]
PRODUCT     diphosphate [CPD:C00013];
            GDP-mannose [CPD:C00096]
COMMENT     The bacterial enzyme can also use ITP and dGTP as donors.
REFERENCE   1
  AUTHORS   Munch-Peterson, A.
  TITLE     Enzymatic synthesis and phosphorolysis of guanosine diphosphate
            mannose.
  JOURNAL   Arch. Biochem. Biophys. 55 (1955) 592-593.
  ORGANISM  Saccharomyces fragilis
REFERENCE   2  [PMID:14245350]
  AUTHORS   PREISS J, WOOD E.
  TITLE     SUGAR NUCLEOTIDE REACTIONS IN ARTHROBACTER. I. GUANOSINE DIPHOSPHATE
            MANNOSE PYROPHOSPHORYLASE: PURIFICATION AND PROPERTIES.
  JOURNAL   J. Biol. Chem. 239 (1964) 3119-26.
  ORGANISM  Arthrobacter sp.
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K00966  mannose-1-phosphate guanylyltransferase
GENES       XLA: 447346(MGC84017)
            XTR: 493267(gmppb)
            DME: Dmel_CG1129 Dmel_CG8207
            CEL: C42C1.5(guanyltransferase)
            CME: CML145C CMO003C
            SCE: YDL055C(PSA1)
            AGO: AGOS_AFR599W
            PIC: PICST_74665(MPG1)
            CGR: CAGL0D01034g CAGL0H04983g
            SPO: SPBC13G1.02 SPCC1906.01
            ANI: AN5586.2
            AFM: AFUA_4G11510 AFUA_6G07620
            AOR: AO090003000189 AO090003001069
            CNE: CNC03020
            ECU: ECU11_0690
            DDI: DDB_0231665(mpgA)
            PFA: PF14_0774
            CPV: cgd2_1770
            CHO: Chro.20192
            TAN: TA14300
            TPV: TP02_0639
            TET: TTHERM_00628710
            TBR: Tb927.8.2050
            TCR: 503589.10 510947.10
            LMA: LmjF23.0110
            XFA: XF0591
            XFT: PD1560
            XCC: XCC2785(glgC)
            XCB: XC_1328
            XCV: XCV3100
            XAC: XAC2955
            XOO: XOO1302
            XOM: XOO_1202(XOO1202)
            VVU: VV1_0804
            VFI: VF0145
            PSP: PSPPH_0638
            PFL: PFL_5644
            PFO: Pfl_5130
            PEN: PSEEN0433 PSEEN2466
            PHA: PSHAa2630
            FTW: FTW_0453
            TCX: Tcr_1456 Tcr_1652
            NOC: Noc_2431
            CVI: CV_4226
            REU: Reut_A0722
            BUR: Bcep18194_A6040
            RFR: Rfer_0712
            MMS: mma_0645
            NET: Neut_0159
            AZO: azo2231
            DAR: Daro_3661
            TDN: Tmden_0175
            GSU: GSU3254
            GME: Gmet_3178
            PCA: Pcar_2958
            BBA: Bd0153 Bd1685
            SAT: SYN_01129
            MLO: mlr6764
            RLE: RL0028
            BME: BMEI2025
            BMF: BAB1_2103
            BRA: BRADO0082 BRADO5165
            BBT: BBta_0088 BBta_5632
            RPA: RPA3919
            RPB: RPB_3804
            RPE: RPE_0462
            NWI: Nwi_0048 Nwi_2394
            RDE: RD1_0454
            SAL: Sala_0159
            GBE: GbCGDNIH1_2008
            RRU: Rru_A3436
            MGM: Mmc1_0560 Mmc1_0963
            BHA: BH1416(mpg)
            BAN: BA4491
            BAR: GBAA4491
            BAA: BA_4938
            BAT: BAS4169
            BCE: BC4264
            BCA: BCE_4347
            BCZ: BCZK4017
            BTK: BT9727_4007
            GKA: GK0360
            STH: STH1120
            CAC: CAC2981 CAC3056
            DSY: DSY4439
            SWO: Swol_2137
            TTE: TTE0065(gcd1) TTE2013(gcd1.2)
            MTA: Moth_0757 Moth_1925
            MTU: Rv3264c(manB)
            MTC: MT3364(mpg1)
            MLE: ML0753(rmlA2)
            MPA: MAP3378c(rmlA2)
            MMC: Mmcs_1321
            CGL: NCgl0710(cgl0742)
            CEF: CE0756
            CDI: DIP0682
            CJK: jk1645
            RHA: RHA1_ro06307
            SCO: SCO1388(SC1A8A.08c) SCO3039(SCE34.20c)
            SMA: SAV358(mpg1) SAV5037(rmlA) SAV6977(mpg3)
            TFU: Tfu_1394
            FRA: Francci3_0737 Francci3_1463
            FAL: FRAAL1255 FRAAL2265
            SEN: SACE_6470(manB)
            LIL: LA1581 LA1611
            LIC: LIC12171 LIC12201
            SYN: sll1496 sll1558
            SYW: SYNW2266
            SYC: syc1022_c syc2123_d
            SYF: Synpcc7942_0498 Synpcc7942_1973
            SYD: Syncc9605_2404
            SYE: Syncc9902_0289
            SYG: sync_2617
            CYA: CYA_1231
            CYB: CYB_1549
            TEL: tlr0436 tlr0611
            GVI: gll1782(rfbM) gll2200 gll3084 gll3341 gll3703 glr0471
                 glr3480(rfbM)
            ANA: alr2361 alr3400
            AVA: Ava_0182 Ava_3422
            PMA: Pro0175(GCD1)
            PMM: PMM0152
            PMT: PMT2012
            PMN: PMN2A_1518
            PMI: PMT9312_0154
            PMB: A9601_01691 A9601_14401
            PMC: P9515_01801
            PMF: P9303_00981 P9303_01171 P9303_26731
            PMG: P9301_01711 P9301_14051
            PME: NATL1_02241
            TER: Tery_1143 Tery_3188
            BTH: BT_1633
            BFR: BF1436
            CTE: CT2056
            CCH: Cag_0193
            PLT: Plut_2007
            DEH: cbdb_A1125
            DRA: DR_0710
            AAE: aq_718(mpg)
            MAC: MA3140(rfbM)
            MBA: Mbar_A1937
            MMA: MM_0378
            MHU: Mhun_2619
            MTH: MTH1759
            MKA: MK0917
            HWA: HQ3261A(manC)
            TAC: Ta1486
            TVO: TVN0081
            PTO: PTO0702
            PHO: PH1022 PH1697
            PAB: PAB0317(mpg) PAB0645
            PFU: PF0868 PF1728
            TKO: TK0955
            RCI: RCIX300(rfbM)
            APE: APE_0255.1
            SSO: SSO0317
            STO: ST2284
            SAI: Saci_0196(mpg1)
            PAI: PAE3554
STRUCTURES  PDB: 2CU2  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.13
            ExPASy - ENZYME nomenclature database: 2.7.7.13
            ExplorEnz - The Enzyme Database: 2.7.7.13
            ERGO genome analysis and discovery system: 2.7.7.13
            BRENDA, the Enzyme Database: 2.7.7.13
            CAS: 37278-24-3
///
ENTRY       EC 2.7.7.14                 Enzyme
NAME        ethanolamine-phosphate cytidylyltransferase;
            phosphorylethanolamine transferase;
            ET;
            CTP-phosphoethanolamine cytidylyltransferase;
            phosphoethanolamine cytidylyltransferase;
            ethanolamine phosphate cytidylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     CTP:ethanolamine-phosphate cytidylyltransferase
REACTION    CTP + ethanolamine phosphate = diphosphate + CDP-ethanolamine
            [RN:R02038]
ALL_REAC    R02038;
            (other) R04247
SUBSTRATE   CTP [CPD:C00063];
            ethanolamine phosphate [CPD:C00346]
PRODUCT     diphosphate [CPD:C00013];
            CDP-ethanolamine [CPD:C00570]
REFERENCE   1  [PMID:13366993]
  AUTHORS   KENNEDY EP, WEISS SB.
  TITLE     The function of cytidine coenzymes in the biosynthesis of
            phospholipides.
  JOURNAL   J. Biol. Chem. 222 (1956) 193-214.
REFERENCE   2  [PMID:241749]
  AUTHORS   Sundler R.
  TITLE     Ethanolaminephosphate cytidylyltransferase. Purification and
            characterization of the enzyme from rat liver.
  JOURNAL   J. Biol. Chem. 250 (1975) 8585-90.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:2549956]
  AUTHORS   Visedo-Gonzalez E, Dixon HB.
  TITLE     2-Aminoethylarsonic acid as an analogue of ethanolamine phosphate.
            Endowment of ethanolamine-phosphate cytidylyltransferase with CTP
            pyrophosphatase activity.
  JOURNAL   Biochem. J. 260 (1989) 299-301.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00440  Aminophosphonate metabolism
            PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00967  ethanolamine-phosphate cytidylyltransferase
GENES       MCC: 715006(PCYT2)
            MMU: 68671(Pcyt2)
            RNO: 89841(Pcyt2)
            CFA: 607608(PCYT2)
            XLA: 444649(MGC84177)
            XTR: 496753(pcyt2)
            DME: Dmel_CG5547(Pect)
            CEL: Y37E3.11
            ATH: AT2G38670(PECT1)
            OSA: 4351359
            CME: CMS052C
            SCE: YGR007W(MUQ1)
            AGO: AGOS_AFR504W
            PIC: PICST_76493(MUQ1)
            CGR: CAGL0F08723g
            SPO: SPAC15E1.05c
            ANI: AN4303.2
            AFM: AFUA_4G05940
            AOR: AO090023001003
            ECU: ECU11_0870
            DDI: DDB_0191331(pctA)
            PFA: PF13_0253
            CPV: cgd7_2950
            CHO: Chro.70332
            TAN: TA07160
            TPV: TP04_0187
            TET: TTHERM_00015980 TTHERM_00429910
            TBR: Tb11.01.5730
            TCR: 511727.120
            LMA: LmjF32.0890
            EHI: 269.t00004 60.t00017
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.14
            ExPASy - ENZYME nomenclature database: 2.7.7.14
            ExplorEnz - The Enzyme Database: 2.7.7.14
            ERGO genome analysis and discovery system: 2.7.7.14
            BRENDA, the Enzyme Database: 2.7.7.14
            CAS: 9026-33-9
///
ENTRY       EC 2.7.7.15                 Enzyme
NAME        choline-phosphate cytidylyltransferase;
            phosphorylcholine transferase;
            CDP-choline pyrophosphorylase;
            CDP-choline synthetase;
            choline phosphate cytidylyltransferase;
            CTP-phosphocholine cytidylyltransferase;
            CTP:phosphorylcholine cytidylyltransferase;
            cytidine diphosphocholine pyrophosphorylase;
            phosphocholine cytidylyltransferase;
            phosphorylcholine cytidylyltransferase;
            phosphorylcholine:CTP cytidylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     CTP:choline-phosphate cytidylyltransferase
REACTION    CTP + choline phosphate = diphosphate + CDP-choline [RN:R01890]
ALL_REAC    R01890;
            (other) R02590
SUBSTRATE   CTP [CPD:C00063];
            choline phosphate [CPD:C00588]
PRODUCT     diphosphate [CPD:C00013];
            CDP-choline [CPD:C00307]
REFERENCE   1  [PMID:13463016]
  AUTHORS   BORKENHAGEN LF, KENNEDY EP.
  TITLE     The enzymatic synthesis of cytidine diphosphate choline.
  JOURNAL   J. Biol. Chem. 227 (1957) 951-62.
  ORGANISM  guinea pig
REFERENCE   2  [PMID:13366993]
  AUTHORS   KENNEDY EP, WEISS SB.
  TITLE     The function of cytidine coenzymes in the biosynthesis of
            phospholipides.
  JOURNAL   J. Biol. Chem. 222 (1956) 193-214.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Williams-Ashman, H.G. and Banks, J.
  TITLE     Participation of cytidine coenzymes in the metabolism of choline by
            seminal vesicles.
  JOURNAL   J. Biol. Chem. 223 (1956) 509-521.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00440  Aminophosphonate metabolism
            PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00968  choline-phosphate cytidylyltransferase
GENES       HSA: 5130(PCYT1A) 9468(PCYT1B)
            PTR: 465542(PCYT1B) 471049(LOC471049)
            MMU: 13026(Pcyt1a) 236899(Pcyt1b)
            RNO: 140544(Pcyt1a) 286936(Pcyt1b)
            CFA: 478600(PCYT1A) 491780(PCYT1B)
            GGA: 418594(PCYT1B) 424915(PCYT1A)
            XLA: 380231(pcyt1a)
            SPU: 752968(LOC752968)
            DME: Dmel_CG1049(Cct1) Dmel_CG18330(Cct2)
            CEL: F08C6.2
            SCE: YGR202C(PCT1)
            AGO: AGOS_ACL118C
            PIC: PICST_31198(PCT1)
            CGR: CAGL0B04015g
            AFM: AFUA_1G09290
            AOR: AO090005001594
            DDI: DDB_0231750
            PFA: MAL13P1.86
            CPV: cgd8_1150
            CHO: Chro.80135
            TAN: TA15365
            TBR: Tb10.389.0730
            SAC: SACOL0698(tagD)
            FNU: FN1237
STRUCTURES  PDB: 1PEH  1PEI  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.15
            ExPASy - ENZYME nomenclature database: 2.7.7.15
            ExplorEnz - The Enzyme Database: 2.7.7.15
            ERGO genome analysis and discovery system: 2.7.7.15
            BRENDA, the Enzyme Database: 2.7.7.15
            CAS: 9026-34-0
///
ENTRY       EC 2.7.7.16       Obsolete  Enzyme
NAME        Transferred to 3.1.27.5
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
COMMENT     Transferred entry: now EC 3.1.27.5 pancreatic ribonuclease (EC
            2.7.7.16 created 1961, deleted 1972, [transferred to EC 3.1.4.22,
            deleted 1980])
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.16
            ExPASy - ENZYME nomenclature database: 2.7.7.16
            ExplorEnz - The Enzyme Database: 2.7.7.16
            ERGO genome analysis and discovery system: 2.7.7.16
            BRENDA, the Enzyme Database: 2.7.7.16
///
ENTRY       EC 2.7.7.17       Obsolete  Enzyme
NAME        Transferred to 3.1.27.1
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
COMMENT     Transferred entry: now EC 3.1.27.1 ribonuclease T2 (EC 2.7.7.17
            created 1965, deleted 1972, [transferred to EC 3.1.4.23, deleted
            1980])
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.17
            ExPASy - ENZYME nomenclature database: 2.7.7.17
            ExplorEnz - The Enzyme Database: 2.7.7.17
            ERGO genome analysis and discovery system: 2.7.7.17
            BRENDA, the Enzyme Database: 2.7.7.17
///
ENTRY       EC 2.7.7.18                 Enzyme
NAME        nicotinate-nucleotide adenylyltransferase;
            deamido-NAD+ pyrophosphorylase;
            nicotinate mononucleotide adenylyltransferase;
            deamidonicotinamide adenine dinucleotide pyrophosphorylase;
            NaMN-ATase;
            nicotinic acid mononucleotide adenylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ATP:nicotinate-ribonucleotide adenylyltransferase
REACTION    ATP + nicotinate ribonucleotide = diphosphate + deamido-NAD+
            [RN:R03005]
ALL_REAC    R03005;
            (other) R00137
SUBSTRATE   ATP [CPD:C00002];
            nicotinate ribonucleotide [CPD:C01185]
PRODUCT     diphosphate [CPD:C00013];
            deamido-NAD+ [CPD:C00857]
REFERENCE   1  [PMID:13717628]
  AUTHORS   IMSANDE J.
  TITLE     Pathway of diphosphopyridine nucleotide biosynthesis in Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 236 (1961) 1494-7.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K00969  nicotinate-nucleotide adenylyltransferase
GENES       PIC: PICST_81173
            TET: TTHERM_00075630
            ECO: b0639(nadD)
            ECJ: JW0634(nadD)
            ECE: Z0786(ybeN)
            ECS: ECs0677
            ECC: c0730(nadD)
            ECI: UTI89_C0642(ybeN)
            ECP: ECP_0669
            ECV: APECO1_1416(nadD)
            ECW: EcE24377A_0665(nadD)
            STY: STY0696
            STT: t2222
            SPT: SPA2089(ybeN)
            SEC: SC0675(nadD)
            STM: STM0645(nadD)
            YPE: YPO2607(nadD)
            YPK: y1181
            YPM: YP_1106(nadD)
            YPA: YPA_2490
            YPN: YPN_1092
            YPP: YPDSF_2646
            YPS: YPTB1100(nadD)
            YPI: YpsIP31758_2929(nadD)
            SFL: SF0642(nadD)
            SFX: S0664(ybeN)
            SFV: SFV_0687(ybeN)
            SSN: SSON_0593(ybeN)
            SBO: SBO_0503(ybeN)
            SDY: SDY_0561(ybeN)
            ECA: ECA1306(nadD)
            PLU: plu1300(nadD)
            BUC: BU446(ybeN)
            BAS: BUsg431(ybeN)
            WBR: WGLp171(ybeN)
            SGL: SG0800
            ENT: Ent638_1173
            XFA: XF2179
            XFT: PD1233(nadD)
            XCC: XCC2616(nadD)
            XCB: XC_1500
            XCV: XCV2934(nadD)
            XAC: XAC2778(nadD)
            XOO: XOO3326(nadD)
            XOM: XOO_3139(XOO3139)
            VFI: VFA0601
            PAE: PA4006
            PAP: PSPA7_1103(nadD)
            PPU: PP_4810
            PST: PSPTO_4828(nadD)
            PSB: Psyr_4368(nadD)
            PSP: PSPPH_4410(nadD)
            PFL: PFL_5455(nadD)
            PFO: Pfl_4973
            PEN: PSEEN4829(nadD)
            PAR: Psyc_0195(nadD)
            SON: SO_1171(nad)
            SDN: Sden_0794
            SFR: Sfri_0702
            SAZ: Sama_2585
            SBL: Sbal_3272
            SLO: Shew_2932
            SPC: Sputcn32_2866
            SHE: Shewmr4_0994
            SHM: Shewmr7_1059
            SHN: Shewana3_0998
            SHW: Sputw3181_1037
            ILO: IL0950
            CPS: CPS_1718(nadD)
            PHA: PSHAa1028(nadD)
            PAT: Patl_1563
            SDE: Sde_3344
            PIN: Ping_1188
            MAQ: Maqu_2416
            CBU: CBU_0556(nadD)
            CBD: COXBU7E912_1509(nadD)
            LPN: lpg1345
            LPF: lpl1298(nadD)
            LPP: lpp1299(nadD)
            MCA: MCA1879(nadD)
            TCX: Tcr_0484
            NOC: Noc_2661(nadD)
            AEH: Mlg_0404
            HHA: Hhal_2141
            HCH: HCH_05846(nadD)
            CSA: Csal_1542
            ABO: ABO_1952
            AHA: AHA_3251(nadD)
            BCI: BCI_0234(nadD)
            VOK: COSY_0307(nadD)
            NME: NMB2024
            NMA: NMA0416
            NGO: NGO2080
            CVI: CV_0519
            RSO: RSc2193(RS01406)
            REU: Reut_A2525
            REH: H16_A0913(nadD)
            RME: Rmet_0782
            BMA: BMA1887(nadD)
            BMV: BMASAVP1_A1072(nadD)
            BML: BMA10299_A0795(nadD)
            BMN: BMA10247_0355(nadD)
            BXE: Bxe_A3262
            BUR: Bcep18194_A5624
            BCN: Bcen_1685
            BCH: Bcen2424_2297
            BAM: Bamb_2335
            BPS: BPSL1162
            BPM: BURPS1710b_1382(nadD)
            BPL: BURPS1106A_1237(nadD)
            BPD: BURPS668_1228(nadD)
            BTE: BTH_I1012(nadD)
            PNU: Pnuc_0615
            BPE: BP2311(nadD)
            BPA: BPP2419(nadD)
            BBR: BB1868(nadD)
            RFR: Rfer_2078
            POL: Bpro_1971
            MPT: Mpe_A1340
            HAR: HEAR0555(nadD)
            MMS: mma_0541
            NEU: NE0359(nadD)
            NET: Neut_1610
            NMU: Nmul_A0360
            EBA: ebA3972(nadD)
            AZO: azo3607(nadD)
            DAR: Daro_0169
            TBD: Tbd_2441
            MFA: Mfla_2159
            HPY: HP1337
            HPJ: jhp1256
            HPA: HPAG1_1284
            HHE: HH0351
            HAC: Hac_0266(nadD)
            TDN: Tmden_1755
            CJE: Cj1404
            CJR: CJE1591(nadD)
            CJU: C8J_1318
            CFF: CFF8240_1430(nadD)
            CCV: CCV52592_1250
            CHA: CHAB381_0776
            ABU: Abu_2131(nadD)
            NIS: NIS_1493(nadD)
            SUN: SUN_2205
            GSU: GSU3210(nadD)
            GME: Gmet_3200
            PCA: Pcar_2578
            PPD: Ppro_3614
            DVU: DVU1954(nadD)
            DDE: Dde_1632
            LIP: LI0062(ybeN)
            BBA: Bd3846
            DPS: DP2587
            ADE: Adeh_2409
            MXA: MXAN_4185(nadD)
            SAT: SYN_02003
            SFU: Sfum_3645
            AMA: AM432
            APH: APH_0791
            ERU: Erum2910(nadD)
            ERW: ERWE_CDS_02970(nadD)
            ERG: ERGA_CDS_02910(nadD)
            ECN: Ecaj_0272
            ECH: ECH_0806(nadD)
            NSE: NSE_0711
            PUB: SAR11_0225(ybeN)
            MLO: mll4008
            MES: Meso_3455
            PLA: Plav_1477
            SME: SMc03778
            SMD: Smed_3012
            ATU: Atu2778(nadD)
            ATC: AGR_C_5040
            RET: RHE_CH04070(nadD)
            RLE: RL4684(nadD)
            BME: BMEI0209(nadD)
            BMF: BAB1_1850
            BMS: BR1842(nadD)
            BMB: BruAb1_1821(nadD)
            BOV: BOV_1775(nadD)
            OAN: Oant_1057
            BJA: blr0430(nadD)
            BRA: BRADO0429
            BBT: BBta_0418
            RPA: RPA0165
            RPB: RPB_0254
            RPC: RPC_0162
            RPD: RPD_0570
            RPE: RPE_0267
            NWI: Nwi_0445(nadD)
            NHA: Nham_0521
            BHE: BH01590(nadD)
            BQU: BQ01490(nadD)
            BBK: BARBAKC583_0320(nadD)
            CCR: CC_3431
            SIL: SPO0449(nadD)
            SIT: TM1040_2258
            RSP: RSP_0586(nadD)
            RSH: Rsph17029_2239
            JAN: Jann_3629
            RDE: RD1_1243(nadD)
            PDE: Pden_1318 Pden_1579
            MMR: Mmar10_2791
            HNE: HNE_3430(nadD)
            ZMO: ZMO1662(nadD)
            NAR: Saro_0059
            SAL: Sala_0578
            ELI: ELI_13225
            GOX: GOX1148(nadD)
            GBE: GbCGDNIH1_1709
            RRU: Rru_A1237
            MAG: amb4083
            MGM: Mmc1_3347
            ABA: Acid345_0021
            SUS: Acid_4829
            BSU: BG11638(nadD)
            BHA: BH1326
            BAN: BA4558(nadD)
            BAR: GBAA4558(nadD)
            BAA: BA_5003
            BAT: BAS4230
            BCE: BC4329(nadD)
            BCA: BCE_4413(nadD)
            BCZ: BCZK4078(nadD)
            BTK: BT9727_4068(nadD)
            BTL: BALH_3920(nadD)
            BLI: BL02081(nadD)
            BLD: BLi02757(yqeJ)
            BCL: ABC1640(nadD)
            BPU: BPUM_2298
            OIH: OB1985(nadD)
            GKA: GK2522(nadD)
            SAU: SA1422
            SAV: SAV1594
            SAM: MW1545
            SAR: SAR1671
            SAS: SAS1531
            SAC: SACOL1650(nadD)
            SAB: SAB1466c
            SAA: SAUSA300_1553(nadD)
            SAO: SAOUHSC_01697
            SAJ: SaurJH9_1651
            SAH: SaurJH1_1686
            SEP: SE1280
            SER: SERP1161(nadD)
            SHA: SH1321
            SSP: SSP1164
            LMO: lmo1488
            LMF: LMOf2365_1507(nadD)
            LIN: lin1523
            LWE: lwe1501(nadD)
            LLA: L106374(ylaE)
            LLC: LACR_0231 LACR_1200
            LLM: llmg_0236(nadD1) llmg_1473(nadD2)
            SPY: SPy_0308
            SPZ: M5005_Spy_0263(nadD)
            SPM: spyM18_0304
            SPG: SpyM3_0226
            SPS: SPs1634
            SPH: MGAS10270_Spy0260(nadD)
            SPI: MGAS10750_Spy0257(nadD)
            SPJ: MGAS2096_Spy0281(nadD)
            SPK: MGAS9429_Spy0262(nadD)
            SPF: SpyM51591
            SPA: M6_Spy0291(nadD)
            SPB: M28_Spy0255(nadD)
            SPN: SP_1747
            SPR: spr1592
            SPD: SPD_1557(nadD)
            SAG: SAG1662
            SAN: gbs1706
            SAK: SAK_1674(nadD)
            SMU: SMU.1799(nadD)
            STC: str1619
            STL: stu1619
            SSA: SSA_0578(nadD)
            SGO: SGO_0447(nadD)
            LPL: lp_1530(nadD)
            LJO: LJ1636
            LAC: LBA1530(nadD)
            LSA: LSA1391(nadD)
            LSL: LSL_0502(nadD)
            LDB: Ldb1498(nadD)
            LBU: LBUL_1394
            LBR: LVIS_1029
            LCA: LSEI_1688
            EFA: EF2871(nadD)
            OOE: OEOE_0908
            STH: STH434
            CAC: CAC1262
            CPE: CPE2125
            CPF: CPF_2380(nadD)
            CPR: CPR_2092(nadD)
            CTC: CTC02055(nadD)
            CNO: NT01CX_0075(nadD)
            CTH: Cthe_1241
            CDF: CD2524(nadD)
            CBO: CBO2984(nadD)
            CBA: CLB_3009(nadD)
            CBH: CLC_2881(nadD)
            CBF: CLI_3038(nadD)
            CKL: CKL_0883(nadD)
            CHY: CHY_0388(nadD)
            DSY: DSY3161(nadD)
            DRM: Dred_2519
            SWO: Swol_1603
            TTE: TTE0918(nadD)
            MTA: Moth_0564
            MMY: MSC_0442
            MMO: MMOB2760(nadD)
            MHY: mhp474
            MHJ: MHJ_0473
            MHP: MHP7448_0476
            MSY: MS53_0319
            MCP: MCAP_0529
            UUR: UU469
            MTU: Rv2421c(nadD)
            MTC: MT2494
            MBO: Mb2444c(nadD)
            MBB: BCG_2437c(nadD)
            MLE: ML1454
            MPA: MAP2244c
            MAV: MAV_1750(nadD)
            MSM: MSMEG_4581(nadD)
            MUL: MUL_3692(nadD)
            MVA: Mvan_3926
            MGI: Mflv_2653
            MMC: Mmcs_3530
            MKM: Mkms_3603
            MJL: Mjls_3535
            CGL: NCgl2270(nadD)
            CGB: cg2584(nadD)
            CEF: CE2257
            CDI: DIP1775
            CJK: jk0567(nadD)
            NFA: nfa13760
            RHA: RHA1_ro01297
            SCO: SCO2579(SCC123.17c)
            SMA: SAV5478(nadD)
            TWH: TWT469(nadD)
            TWS: TW296(nadD)
            LXX: Lxx08100(nadD)
            CMI: CMM_1495(nadD)
            ART: Arth_2385
            AAU: AAur_2361(nadD)
            PAC: PPA0836(nadD)
            NCA: Noca_1820
            TFU: Tfu_2171(nadD)
            FRA: Francci3_1232
            FAL: FRAAL1936(nadD)
            ACE: Acel_0762
            SEN: SACE_1428(nadD)
            BLO: BL1032
            BAD: BAD_0899(nadD)
            RXY: Rxyl_1522
            FNU: FN1132
            RBA: RB8455(nadD)
            BBU: BB0782
            BGA: BG0806
            TPA: TP0741
            TDE: TDE1747(nadD)
            LIL: LA0855(nadD)
            LIC: LIC12770(nadD)
            LBJ: LBJ_2489(nadD)
            LBL: LBL_0618(nadD)
            SYN: sll1916
            SYW: SYNW0503(nadD)
            SYC: syc1398_d(nadD)
            SYF: Synpcc7942_0106
            SYD: Syncc9605_2179(nadD)
            SYE: Syncc9902_0496(nadD)
            SYG: sync_2293(nadD)
            SYR: SynRCC307_1869(nadD)
            SYX: SynWH7803_2008(nadD)
            CYA: CYA_0491(nadD)
            CYB: CYB_0547(nadD)
            TEL: tlr1178
            GVI: glr4016
            ANA: all5063 alr2483
            AVA: Ava_0415(nadD) Ava_2319
            PMA: Pro1598(nadD)
            PMM: PMM1445(nadD)
            PMT: PMT1460(nadD)
            PMN: PMN2A_0976
            PMB: A9601_16471(nadD)
            PMC: P9515_16241(nadD)
            PMF: P9303_04901(nadD)
            PMG: P9301_16351(nadD)
            PME: NATL1_18441(nadD)
            TER: Tery_0319
            BTH: BT_2011
            BFR: BF3708
            BFS: BF3501(nadD)
            PGI: PG0058(nadD)
            SRU: SRU_2072(nadD)
            CHU: CHU_0598(nadD)
            GFO: GFO_3431(nadD)
            FJO: Fjoh_0744
            FPS: FP0143(nadD)
            CTE: CT0016(nadD)
            CCH: Cag_0069
            DET: DET0003(nadD)
            DEH: cbdb_A3(nadD)
            TTH: TTC1421
            TTJ: TTHA1780
            AAE: aq_036
            TMA: TM0097
            TPT: Tpet_0827
STRUCTURES  PDB: 1K4K  1K4M  1KAM  1KAQ  1YUL  1YUM  1YUN  2H29  2H2A  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.18
            ExPASy - ENZYME nomenclature database: 2.7.7.18
            ExplorEnz - The Enzyme Database: 2.7.7.18
            ERGO genome analysis and discovery system: 2.7.7.18
            BRENDA, the Enzyme Database: 2.7.7.18
            CAS: 9026-98-6
///
ENTRY       EC 2.7.7.19                 Enzyme
NAME        polynucleotide adenylyltransferase;
            NTP polymerase;
            RNA adenylating enzyme;
            AMP polynucleotidylexotransferase;
            ATP-polynucleotide adenylyltransferase;
            ATP:polynucleotidylexotransferase;
            poly(A) polymerase;
            poly(A) synthetase;
            polyadenylate nucleotidyltransferase;
            polyadenylate polymerase;
            polyadenylate synthetase;
            polyadenylic acid polymerase;
            polyadenylic polymerase;
            terminal riboadenylate transferase;
            poly(A) hydrolase;
            RNA formation factors, PF1;
            adenosine triphosphate:ribonucleic acid adenylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ATP:polynucleotide adenylyltransferase
REACTION    ATP + RNAn = diphosphate + RNAn+1 [RN:R00435]
ALL_REAC    R00435
SUBSTRATE   ATP [CPD:C00002];
            RNAn [CPD:C00046]
PRODUCT     diphosphate [CPD:C00013];
            RNAn+1 [CPD:C00046]
COMMENT     Also acts slowly with CTP. Catalyses template-independent extension
            of the 3'- end of a DNA strand by one nucleotide at a time. Cannot
            initiate a chain de novo. The primer, depending on the source of the
            enzyme, may be an RNA or DNA fragment, or oligo(A) bearing a 3'-OH
            terminal group. See also EC 2.7.7.6 DNA-directed RNA polymerase.
REFERENCE   1  [PMID:13965521]
  AUTHORS   AUGUST JT, ORTIZ PJ, HURWITZ J.
  TITLE     Ribonucleic acid-dependent ribonucleotide incorporation. I.
            Purification and properties of the enzyme.
  JOURNAL   J. Biol. Chem. 237 (1962) 3786-93.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Edmonds, M. and Abrams, R.
  TITLE     Polynucleotide biosynthesis: formation of a sequence of adenylate
            units from adenosine triphosphate by an enzyme from thymus nuclei.
  JOURNAL   J. Biol. Chem. 235 (1960) 1142-1149.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:4288534]
  AUTHORS   Gottesman ME, Canellakis ES.
  TITLE     The terminal nucleotidyltransferases of calf thymus nuclei.
  JOURNAL   J. Biol. Chem. 241 (1966) 4339-52.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:14459258]
  AUTHORS   KRAKOW JS, COUTSOGEORGOPOULOS C, CANELLAKIS ES.
  TITLE     Studies on the incorporation of deoxyribonucleic acid.
  JOURNAL   Biochim. Biophys. Acta. 55 (1962) 639-50.
  ORGANISM  cow [GN:bta]
REFERENCE   5  [PMID:4946277]
  AUTHORS   Mans RJ, Walter TJ.
  TITLE     Transfer RNA-primed oligoadenylate synthesis in maize seedlings. II.
            Primer, substrate and metal specificities and size of product.
  JOURNAL   Biochim. Biophys. Acta. 247 (1971) 113-21.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   6  [PMID:4501121]
  AUTHORS   Sheldon R, Jurale C, Kates J.
  TITLE     Detection of polyadenylic acid sequences in viral and eukaryotic
            RNA(polu(U)-cellulose columns-poly(U) filters-fiberglass-HeLa
            cells-bacteriophage T4).
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 69 (1972) 417-21.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K00970  poly(A) polymerase
GENES       HSA: 10914(PAPOLA) 56903(PAPOLB) 64895(PAPOLG)
            PTR: 459259(PAPOLG)
            MMU: 18789(Papola) 216578(Papolg) 56522(Papolb)
            RNO: 305586(Papolg_predicted)
            CFA: 480430(PAPOLA) 481382(PAPOLG)
            BTA: 338051(PAPOLB)
            GGA: 395878(RCJMB04_34p17)
            XLA: 399024(pap)
            XTR: 448186(papolb)
            DRE: 393593(papolg)
            SPU: 575500(LOC575500)
            DME: Dmel_CG9854(hrg)
            CEL: T15H9.6 Y32F6A.3(pap-1)
            ATH: AT1G17980
            OSA: 4328790
            CME: CMQ424C
            SCE: YKR002W(PAP1)
            AGO: AGOS_ABL002C
            PIC: PICST_85400(PAP1)
            CGR: CAGL0L02277g
            SPO: SPBC646.04(pla1)
            ANI: AN0874.2
            AFM: AFUA_1G15340
            AOR: AO090005001182 AO090011000221
            CNE: CNA05330
            UMA: UM05991.1
            ECU: ECU02_0730
            DDI: DDB_0216279(papA)
            PFA: PFF1240w
            CPV: cgd4_930
            TAN: TA19770
            TPV: TP01_0037
            TET: TTHERM_00089190 TTHERM_00149900
            TBR: Tb927.3.3160 Tb927.7.3780
            TCR: 506795.50 508153.440 509937.10 510317.30
            LMA: LmjF14.1180 LmjF29.2600
            EHI: 16.t00038
            ECO: b0143(pcnB)
            ECJ: JW5808(pcnB)
            ECE: Z0154(pcnB)
            ECS: ECs0147
            ECC: c0176(pcnB)
            ECI: UTI89_C0157(pcnB)
            ECP: ECP_0153
            ECV: APECO1_1842(pcnB)
            ECW: EcE24377A_0147(pcnB)
            ECX: EcHS_A0146
            STY: STY0209(pcnB)
            STT: t0192(pcnB)
            SPT: SPA0190(pcnB)
            SEC: SC0184(pcnB)
            STM: STM0184(pcnB)
            YPE: YPO3399(pcnB)
            YPK: y0788(pcnB)
            YPM: YP_0286(pcnB)
            YPA: YPA_2900
            YPN: YPN_0690
            YPP: YPDSF_2957
            YPS: YPTB0732(pcnB)
            YPI: YpsIP31758_3340(pcnB)
            YEN: YE0723(pcnB)
            SFL: SF0135(pcnB)
            SFX: S0138(pcnB)
            SFV: SFV_0128(pcnB)
            SSN: SSON_0155(pcnB)
            SBO: SBO_0132(pcnB)
            SDY: SDY_0159(pcnB)
            ECA: ECA3319(pcnB)
            PLU: plu0874(pcnB)
            BCC: BCc_128(pcnB)
            SGL: SG0490
            ENT: Ent638_0683
            KPN: KPN_00143(pcnB)
            SPE: Spro_3987
            HIN: HI0063(pcnB)
            HIT: NTHI0076(pcnB)
            HDU: HD0604(pcnB)
            HSO: HS_1024(pcnB)
            PMU: PM0864(pcnB)
            MSU: MS0926(pcnB)
            APL: APL_0176(pcnB)
            ASU: Asuc_1731
            XFA: XF0227
            XFT: PD0185(pcnB)
            XCC: XCC1766(pcnB)
            XCB: XC_2470
            XCV: XCV1814(pcnB)
            XAC: XAC1783(pcnB)
            XOO: XOO2366(pcnB)
            XOM: XOO_2247(XOO2247)
            VCH: VC0594
            VCO: VC0395_A0125(pcnB)
            VVU: VV1_1645
            VVY: VV2761
            VPA: VP2504
            VFI: VF2166 VF2167
            PPR: PBPRA3173
            PAE: PA4727(pcnB)
            PAU: PA14_62560(pcnB)
            PPU: PP_4697(pcnB)
            PPF: Pput_4562
            PST: PSPTO_0963(pcnB)
            PSB: Psyr_0830
            PSP: PSPPH_0856(pcnB) PSPPH_1055 PSPPH_4759
            PFL: PFL_5275(pcnB) PFL_5715
            PFO: Pfl_4809
            PEN: PSEEN4733(pcnB)
            PMY: Pmen_3590
            PSA: PST_3294(pcnB)
            PAR: Psyc_0114
            PCR: Pcryo_0123
            ACI: ACIAD3063(pcnB)
            ACB: A1S_0583
            SON: SO_0872(pcnB)
            SDN: Sden_3172
            SFR: Sfri_3278
            SAZ: Sama_0778
            SBL: Sbal_3492
            SBM: Shew185_0847
            SLO: Shew_3131
            SPC: Sputcn32_3130
            SSE: Ssed_3901
            SPL: Spea_0696
            SHE: Shewmr4_0728
            SHM: Shewmr7_3294
            SHN: Shewana3_3406
            SHW: Sputw3181_0813
            ILO: IL2252(pcnB)
            CPS: CPS_4310(pcnB)
            PHA: PSHAa0604(pcnB)
            PAT: Patl_3935
            SDE: Sde_3376
            PIN: Ping_0582
            MAQ: Maqu_0669
            CBU: CBU_0286(pcnB)
            CBD: COXBU7E912_1795(pcnB)
            LPN: lpg1538(pcnB)
            LPF: lpl1488(pcnB)
            LPP: lpp1495(pcnB)
            MCA: MCA2312(pcnB)
            TCX: Tcr_1528
            NOC: Noc_0883
            AEH: Mlg_0562
            HHA: Hhal_0677
            HCH: HCH_06262
            CSA: Csal_3063
            ABO: ABO_0340(pcnB)
            MMW: Mmwyl1_4014
            AHA: AHA_3536
            ASA: ASA_0781(pcnB)
            DNO: DNO_0116(pcnB)
            BCI: BCI_0228(pcnB)
            RMA: Rmag_0480
            VOK: COSY_0443(pcnB)
            NME: NMB0843
            NMA: NMA1053(pcnB)
            NMC: NMC0781(pcnB)
            NGO: NGO0415(pcnB)
            CVI: CV_1632(pcnB)
            RSO: RSc2627(pcnB)
            REU: Reut_A2777(pcnB)
            REH: H16_A3081(pcnB)
            RME: Rmet_2914
            BMA: BMA2320(pcnB)
            BMV: BMASAVP1_A0507(pcnB)
            BML: BMA10299_A1092(pcnB)
            BMN: BMA10247_2199(pcnB)
            BXE: Bxe_A3955
            BVI: Bcep1808_0718
            BUR: Bcep18194_A3845
            BCN: Bcen_0274
            BCH: Bcen2424_0758
            BAM: Bamb_0652
            BPS: BPSL2821
            BPM: BURPS1710b_3314(pcnB)
            BPL: BURPS1106A_3304(pcnB)
            BPD: BURPS668_3271(pcnB)
            BTE: BTH_I1314
            PNU: Pnuc_1765
            BPE: BP0239(pcnB)
            BPA: BPP3628(pcnB)
            BBR: BB4063(pcnB)
            RFR: Rfer_2509
            POL: Bpro_3561
            PNA: Pnap_2991
            AAV: Aave_1973
            AJS: Ajs_2991
            VEI: Veis_1769
            MPT: Mpe_A3020
            HAR: HEAR2637(pcnB)
            MMS: mma_2874
            NEU: NE0069(pcnB)
            NET: Neut_2296
            NMU: Nmul_A0882
            EBA: ebA7112(pcnB)
            AZO: azo3140(pcnB)
            DAR: Daro_3182(pcnB)
            TBD: Tbd_2050(pcnB)
            MFA: Mfla_0600
            HPY: HP0640(papS)
            HPJ: jhp0583(pcnB)
            HPA: HPAG1_0623
            HHE: HH1708(pcnB)
            HAC: Hac_0768(papS)
            GSU: GSU1581 GSU3250(pcnB)
            GME: Gmet_1578 Gmet_3182
            GUR: Gura_0292
            PCA: Pcar_1297 Pcar_3101
            PPD: Ppro_1618
            DVU: DVU1653 DVU2903
            DDE: Dde_1972 Dde_2966
            BBA: Bd3464(pcnB)
            DPS: DP0061 DP0573 DP2910
            ADE: Adeh_0279
            AFW: Anae109_0303
            MXA: MXAN_2545(pcnB)
            SAT: SYN_00533 SYN_01518
            SFU: Sfum_0308
            RPR: RP015(pcnB)
            RTY: RT0014(pcnB)
            RCO: RC0015(pcnB)
            RFE: RF_0019(pcnB)
            RBE: RBE_0165(pcnB)
            RCM: A1E_00060
            OTS: OTBS_0442(pcnB)
            WOL: WD0444
            WBM: Wbm0160
            AMA: AM1136(pcnB)
            ERW: ERWE_CDS_09070(pcnB)
            PUB: SAR11_0104(pcnB)
            MLO: mll2726
            ATU: Atu2250(papS)
            RET: RHE_CH03049(papS)
            RLE: RL3496(papS)
            BMF: BAB1_1570
            BMS: BR1553
            BMB: BruAb1_1542
            BJA: blr2469(papS)
            RPA: RPA1188
            RPB: RPB_1196
            RPC: RPC_0920
            RPD: RPD_1299
            BHE: BH11930(pcnB)
            BQU: BQ09350(pcnB)
            CCR: CC_0408
            SIL: SPO0026
            SIT: TM1040_2891
            RSP: RSP_1205
            SAL: Sala_2110
            GOX: GOX0336
            GBE: GbCGDNIH1_1633
            ABA: Acid345_0497
            SUS: Acid_4618
            BHA: BH2881
            BAA: BA_2077
            GTN: GTNG_2115
            SAB: SAB1321c(papS)
            SAA: SAUSA300_1348
            SHA: SH1455
            SSP: SSP1287
            LWE: lwe1924
            LLC: LACR_1653
            LLM: llmg_0942(papL)
            SPI: MGAS10750_Spy0764(papS)
            SPJ: MGAS2096_Spy0744(papS)
            SPK: MGAS9429_Spy1661
            SAK: SAK_1372(papS)
            SSA: SSA_1086(papS)
            SGO: SGO_1117(pcnA)
            LSA: LSA1004(papS)
            LSL: LSL_0706(pcnB)
            STH: STH1054 STH1805
            CAC: CAC0311 CAC2062
            CPE: CPE0022(papS)
            CPF: CPF_0026
            CPR: CPR_0026
            CNO: NT01CX_0749
            CDF: CD2466
            DSY: DSY1293 DSY2291
            SWO: Swol_1420
            TTE: TTE0109(pcnB) TTE1322(pcnB2)
            POY: PAM102(pcnB)
            AYW: AYWB_607(pcnB)
            MTU: Rv3907c(pcnA)
            MTC: MT4026(pcnB)
            MBO: Mb3937c(pcnA)
            MBB: BCG_3964c(pcnA)
            MLE: ML2697(pcnA)
            MPA: MAP4332c(pcnA)
            CGL: NCgl2979(cgl3085)
            CGB: cg3415(pcnA)
            CEF: CE2928
            CDI: DIP2368
            NFA: nfa56560
            RHA: RHA1_ro03641
            SCO: SCO3896(SCH24.18)
            SMA: SAV4299(pcnA)
            TWH: TWT800(pcnA)
            TWS: TW810
            LXX: Lxx25190(pcnB)
            PAC: PPA2301
            TFU: Tfu_3102
            FRA: Francci3_4531
            SEN: SACE_7377(pcnA)
            BLO: BL0654(pcnA)
            BAD: BAD_1618(pcnA)
            FNU: FN0243
            RBA: RB1993(papS)
            CTR: CT410(pcnB_1) CT704(pcnB_2)
            CTA: CTA_0445(pcnB_1) CTA_0765(pcnB_2)
            CMU: TC0077 TC0691
            CPN: CPn0845(pcnB_1) CPn0966(pcnB_2)
            CPA: CP0894 CP1024
            CPJ: CPj0845(pcnB_1) CPj0966(pcnB_2)
            CPT: CpB0874 CpB1003
            CCA: CCA00791 CCA00922
            CAB: CAB758 CAB890
            CFE: CF0092(pcnB1) CF0222(pcnB2)
            PCU: pc0140(pcnB) pc1308(pcnB)
            BBU: BB0706(papS)
            BGA: BG0728(papS)
            TPA: TP0596
            TDE: TDE1033 TDE1726
            LIL: LA1970(papS) LA3002(pcnB)
            LIC: LIC11065(pcnB) LIC11934
            LBJ: LBJ_1990(pcnB)
            LBL: LBL_1060(pcnB)
            SYN: sll0825(pcnB) sll1253(pcnB)
            SYW: SYNW2254
            SYC: syc0568_c syc0746_d(pcnB)
            SYF: Synpcc7942_0791 Synpcc7942_0976
            SYD: Syncc9605_2392
            SYE: Syncc9902_0301
            SYG: sync_2605
            CYA: CYA_0702 CYA_1863
            CYB: CYB_2855 CYB_2898
            TEL: tll0519
            GVI: gll1453 gll2924
            ANA: all3136 all3989
            AVA: Ava_1708
            PMA: Pro0334(pcnB)
            PMM: PMM0303
            PMT: PMT2001
            PMI: PMT9312_0305
            PMB: A9601_01581 A9601_03261
            PMC: P9515_01691 P9515_03361
            PMF: P9303_25491 P9303_26611
            PMG: P9301_01601 P9301_03271
            PME: NATL1_02131 NATL1_03821
            TER: Tery_1421
            BTH: BT_1975
            BFR: BF3640
            BFS: BF3442
            PGI: PG0801
            SRU: SRU_2436
            CHU: CHU_2535(cca)
            CTE: CT0990
            PLT: Plut_1151
            DET: DET0334 DET0409
            DEH: cbdb_A275 cbdb_A361
            TTH: TTC0556
            TTJ: TTHA0831 TTHA0925
            AAE: aq_2158(pcnB2) aq_411(pcnB1)
STRUCTURES  PDB: 1AV6  1B42  1BKY  1EAM  1EQA  1F5A  1FA0  1JSZ  1JTE  1JTF  
                 1P39  1Q78  1Q79  1V39  1VFG  1VP3  1VP9  1VPT  2GA9  2GAF  
                 2HHP  2O1P  2Q66  2VP3  3MAG  3MCT  4DCG  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.19
            ExPASy - ENZYME nomenclature database: 2.7.7.19
            ExplorEnz - The Enzyme Database: 2.7.7.19
            ERGO genome analysis and discovery system: 2.7.7.19
            BRENDA, the Enzyme Database: 2.7.7.19
            CAS: 9026-30-6
///
ENTRY       EC 2.7.7.20       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
COMMENT     Deleted entry: This entry was identical with EC 2.7.7.25 tRNA
            adenylyltransferase (EC 2.7.7.20 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.20
            ExPASy - ENZYME nomenclature database: 2.7.7.20
            ExplorEnz - The Enzyme Database: 2.7.7.20
            ERGO genome analysis and discovery system: 2.7.7.20
            BRENDA, the Enzyme Database: 2.7.7.20
///
ENTRY       EC 2.7.7.21                 Enzyme
NAME        tRNA cytidylyltransferase;
            tRNA CCA-pyrophosphorylase;
            tRNA-nucleotidyltransferase;
            transfer-RNA nucleotidyltransferase;
            transfer ribonucleic acid nucleotidyl transferase;
            CTP(ATP):tRNA nucleotidyltransferase;
            transfer ribonucleate adenylyltransferase;
            transfer RNA adenylyltransferase;
            transfer ribonucleate nucleotidyltransferase;
            ATP (CTP):tRNA nucleotidyltransferase;
            ribonucleic cytidylic cytidylic adenylic pyrophosphorylase;
            transfer ribonucleate nucleotidyltransferase;
            transfer ribonucleic adenylyl (cytidylyl) transferase;
            transfer ribonucleic-terminal trinucleotide nucleotidyltransferase;
            transfer ribonucleate cytidylyltransferase;
            ribonucleic cytidylyltransferase;
            -C-C-A pyrophosphorylase;
            ATP(CTP)-tRNA nucleotidyltransferase;
            tRNA adenylyl(cytidylyl)transferase;
            ATP(CTP):tRNA nucleotidyltransferase;
            tRNA adenylyltransferase;
            ATP:tRNA adenylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     CTP:tRNA cytidylyltransferase
REACTION    CTP + tRNAn = diphosphate + tRNAn+1 [RN:R07283]
ALL_REAC    R07283
SUBSTRATE   CTP [CPD:C00063];
            tRNA(n) [CPD:C00066]
PRODUCT     diphosphate [CPD:C00013];
            tRNA(n+1) [CPD:C00066]
COMMENT     May be identical with EC 2.7.7.25 tRNA adenylyltransferase.
REFERENCE   1  [PMID:4927556]
  AUTHORS   Best AN, Novelli GD.
  TITLE     Studies with tRNA adenylyl(cytidylyl)transferase from Escherichia
            coli B. I. Purification and kinetic properties.
  JOURNAL   Arch. Biochem. Biophys. 142 (1971) 527-38.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4927557]
  AUTHORS   Best AN, Novelli GD.
  TITLE     Studies with tRNA adenylyl(cytidylyl)transferase from Escherichia
            coli B. II. Regulation of AMP and CMP incorporation into tRNApCpC
            and tRNApC.
  JOURNAL   Arch. Biochem. Biophys. 142 (1971) 539-47.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Deutscher, M.
  TITLE     Synthesis and functions of the -C-C-A terminus of transfer RNA.
  JOURNAL   Prog. Nucleic Acid Res. Mol. Biol. 13 (1972) 51-92.
REFERENCE   4  [PMID:5846983]
  AUTHORS   Edmonds M.
  TITLE     A cytidine triphosphate polymerase from thymus nuclei. 1.
            Purification and properties of the enzyme and its polynucleotide
            primer.
  JOURNAL   J. Biol. Chem. 240 (1965) 4621-8.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K00974  tRNA nucleotidyltransferase (CCA-adding enzyme)
            KO: K07558  tRNA nucleotidyltransferase (CCA-adding enzyme)
GENES       HSA: 51095(TRNT1)
            PTR: 470735(TRNT1)
            MMU: 70047(Trnt1)
            RNO: 312616(Trnt1) 64183(Pde4dip)
            CFA: 476552(TRNT1)
            XTR: 394602(trnt1)
            DRE: 415249(trnt1)
            SPU: 581945(LOC581945)
            DME: Dmel_CG2100
            CEL: F55B12.4
            ATH: AT1G28090
            CME: CML128C
            SCE: YER168C(CCA1)
            AGO: AGOS_AGR118W
            CGR: CAGL0L11858g
            SPO: SPAC1093.04c
            ECU: ECU03_1440
            PFA: PF11_0212
            CHO: Chro.30241
            ECO: b3056(cca)
            ECJ: JW3028(cca)
            ECE: Z4409(cca)
            ECS: ECs3939
            ECC: c3806(cca)
            ECI: UTI89_C3492(cca)
            ECP: ECP_3146
            ECV: APECO1_3358(cca)
            ECW: EcE24377A_3519(cca)
            ECX: EcHS_A3233(cca)
            STY: STY3383(cca)
            STT: t3124(cca)
            SPT: SPA3072(cca)
            SEC: SC3151(cca)
            STM: STM3204(cca)
            YPE: YPO0650(cca)
            YPK: y3529(cca)
            YPM: YP_2965(cca)
            YPA: YPA_3140
            YPN: YPN_0510
            YPS: YPTB3411(cca)
            YPI: YpsIP31758_0560(cca)
            SFL: SF3097(cca)
            SFX: S3302(cca)
            SFV: SFV_3096(cca)
            SSN: SSON_3193(cca)
            SBO: SBO_2912(cca)
            SDY: SDY_3239(cca)
            ECA: ECA3588(cca)
            PLU: plu3972(cca)
            BUC: BU061(cca)
            BAS: BUsg058(cca)
            BAB: bbp057(cca)
            BCC: BCc_038(cca)
            WBR: WGLp238(cca)
            SGL: SG0258
            BFL: Bfl062(cca)
            HIN: HI1606(cca)
            HDU: HD1091(cca)
            HSO: HS_1193(cca)
            PMU: PM0247(cca)
            MSU: MS2312(pcnB)
            APL: APL_0915
            XFA: XF1362
            XFT: PD0602(cca)
            XCC: XCC3407(cca)
            XCB: XC_0757
            XCV: XCV0773(cca)
            XAC: XAC0717(cca)
            XOO: XOO3900(cca)
            XOM: XOO_3681(XOO3681)
            VCH: VC2446
            VVU: VV1_0622
            VVY: VV0571
            VPA: VP0414
            VFI: VF2244
            PPR: PBPRA0439
            PAE: PA0584(cca)
            PAU: PA14_07620(cca)
            PPU: PP_0394
            PPF: Pput_4170
            PST: PSPTO_0544(cca)
            PSB: Psyr_4634
            PSP: PSPPH_0626(cca)
            PFL: PFL_5656(cca)
            PEN: PSEEN0421(cca)
            PAR: Psyc_1368(cca)
            PRW: PsycPRwf_0332 PsycPRwf_1271
            ACI: ACIAD2288(cca)
            SON: SO_1295.2
            SDN: Sden_2823
            SHN: Shewana3_3076
            ILO: IL1966(cca)
            PHA: PSHAa0625(cca)
            CBU: CBU_1827
            LPN: lpg2742
            LPF: lpl2667(cca)
            LPP: lpp2798(cca)
            MCA: MCA0022(cca)
            FTU: FTT0108c(cca)
            FTF: FTF0108c(cca)
            FTW: FTW_0193
            FTL: FTL_1669
            FTH: FTH_1610(cca)
            FTA: FTA_1766
            FTN: FTN_1607(cca)
            TCX: Tcr_0240
            NOC: Noc_0389
            HCH: HCH_01366(cca)
            ABO: ABO_2052(cca)
            AHA: AHA_3784
            BCI: BCI_0622(cca)
            VOK: COSY_0197(cca)
            NME: NMB1241
            NMA: NMA1410(cca)
            NGO: NGO0763
            CVI: CV_2032(cca)
            RSO: RSc0085(cca)
            REU: Reut_A0222
            RME: Rmet_0179
            BMA: BMA3317(cca)
            BXE: Bxe_A0201
            BUR: Bcep18194_A6378
            BAM: Bamb_3076
            BPS: BPSL0265(cca)
            BPM: BURPS1710b_0457(cca)
            BTE: BTH_I0236
            BPE: BP3059(cca)
            BPA: BPP0203(cca)
            BBR: BB0207(cca)
            RFR: Rfer_1090
            POL: Bpro_3914
            NEU: NE1614(cca)
            NET: Neut_0503
            NMU: Nmul_A2451
            EBA: ebA3379(cca)
            DAR: Daro_4135
            MFA: Mfla_2259
            TDN: Tmden_0005
            CJE: Cj0789
            CJU: C8J_0740
            CCO: CCC13826_1816
            GSU: GSU2184
            GME: Gmet_2285
            DDE: Dde_2083
            BBA: Bd1820
            ADE: Adeh_1480
            AFW: Anae109_2353
            MES: Meso_2176
            SME: SMc02700
            ATC: AGR_C_4092(pcnB)
            BME: BMEI0463
            RPE: RPE_0944
            NWI: Nwi_2622
            RDE: RD1_0409
            NAR: Saro_1021
            ELI: ELI_02245
            RRU: Rru_A0366
            MAG: amb4158
            MGM: Mmc1_1939
            BSU: BG11208(cca)
            BHA: BH1684(papS)
            BAN: BA1559(pcnB)
            BAR: GBAA1559(pcnB)
            BAT: BAS1446
            BCE: BC1536
            BCA: BCE_1665(pcnB)
            BCZ: BCZK1419(pcnB)
            BTK: BT9727_1418(pcnB)
            BLI: BL02754(cca)
            BLD: BLi02380(cca)
            BCL: ABC2069(cca)
            BPU: BPUM_1976(cca)
            OIH: OB1765
            GKA: GK2181
            SAU: SA1290
            SAV: SAV1457
            SAM: MW1347
            SAR: SAR1468(papS)
            SAS: SAS1400
            SAC: SACOL1497(papS)
            SAO: SAOUHSC_01474
            SEP: SE1145
            SER: SERP1027(papS)
            LMO: lmo1905(cca)
            LMF: LMOf2365_1934
            LIN: lin2019(cca)
            LLA: L0324(papL)
            SPY: SPy_0866(papS)
            SPZ: M5005_Spy_0673(papS)
            SPM: spyM18_0927(papS)
            SPG: SpyM3_0587(papS)
            SPS: SPs1266
            SPH: MGAS10270_Spy0731(papS)
            SPA: M6_Spy0691
            SPB: M28_Spy0653(papS)
            SPN: SP_1554
            SPR: spr1413(cca)
            SAG: SAG1341
            SAN: gbs1411
            SMU: SMU.901(papS)
            STC: str0425(papL)
            STL: stu0425(papL)
            LPL: lp_1873(papL)
            LJO: LJ1100
            LAC: LBA0973
            LDB: Ldb1280(cca)
            LBU: LBUL_1197
            LBR: LVIS_0782
            LCA: LSEI_1384
            EFA: EF1558(papS)
            CTC: CTC01205
            CKL: CKL_1254(cca)
            SWO: Swol_1813
            TPA: TP0270(pcnA)
            SYW: SYNW0188
            CYA: CYA_1032
            TEL: tlr0715
            AVA: Ava_3833
            PMA: Pro0164(pcnB)
            PMM: PMM0141
            PMT: PMT1910
            PMC: P9515_01691
            RCA: Rcas_2928
            TTH: TTC0479
            TMA: TM0715
            MJA: MJ1111(cca)
            MMP: MMP0949
            MMZ: MmarC7_0196
            MAE: Maeo_1256
            MVN: Mevan_0240
            MAC: MA3559(cca)
            MBA: Mbar_A2014
            MMA: MM_0469
            MBU: Mbur_1130
            MHU: Mhun_2808
            MTH: MTH584
            MST: Msp_0086
            MSI: Msm_0053
            MKA: MK1100 MK1366(CCA1)
            AFU: AF0410 AF2156(cca)
            HAL: VNG0137G(cca)
            HMA: rrnAC2298(cca)
            HWA: HQ1438A(cca)
            NPH: NP0320A(cca)
            TAC: Ta1446
            PTO: PTO0469 PTO0535
            PHO: PH0101
            PAB: PAB0063(cca)
            PFU: PF0026(cca)
            TKO: TK1741
            APE: APE_1791.1
            SSO: SSO1039
            STO: ST0012 ST0952
            SAI: Saci_1288
            MSE: Msed_1784
            PAI: PAE3325
            NEQ: NEQ152
STRUCTURES  PDB: 2DR5  2DR7  2DR8  2DR9  2DRA  2DRB  2DVI  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.21
            ExPASy - ENZYME nomenclature database: 2.7.7.21
            ExplorEnz - The Enzyme Database: 2.7.7.21
            ERGO genome analysis and discovery system: 2.7.7.21
            BRENDA, the Enzyme Database: 2.7.7.21
            CAS: 9026-32-8
///
ENTRY       EC 2.7.7.22                 Enzyme
NAME        mannose-1-phosphate guanylyltransferase (GDP);
            GDP mannose phosphorylase;
            mannose 1-phosphate (guanosine diphosphate) guanylyltransferase;
            GDP mannose phosphorylase;
            GDP-mannose 1-phosphate guanylyltransferase;
            guanosine diphosphate-mannose 1-phosphate guanylyltransferase;
            guanosine diphosphomannose phosphorylase;
            mannose 1-phosphate guanylyltransferase;
            GDP:D-mannose-1-phosphate guanylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     GDP:alpha-D-mannose-1-phosphate guanylyltransferase
REACTION    GDP + alpha-D-mannose 1-phosphate = phosphate + GDP-mannose
ALL_REAC    (other) R00883
SUBSTRATE   GDP [CPD:C00035];
            alpha-D-mannose 1-phosphate [CPD:C00636]
PRODUCT     phosphate [CPD:C00009];
            GDP-mannose [CPD:C00096]
REFERENCE   1  [PMID:13876695]
  AUTHORS   CARMINATTI H, CABIB E.
  TITLE     Phosphorolysis of the pyrophosphate bond of some nucleotides.
  JOURNAL   Biochim. Biophys. Acta. 53 (1961) 417-9.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K00971  mannose-1-phosphate guanylyltransferase
GENES       HSA: 29925(GMPPB) 29926(GMPPA)
            PTR: 460378(GMPPB)
            MMU: 331026(Gmppb)
            RNO: 363145(Gmppb_predicted)
            CFA: 484766(AMIGO3)
            ATH: AT2G39770(CYT1) AT3G55590
            OSA: 4332373
            TAN: TA14300
            EHI: 218.t00017
            ECO: b2049(cpsB)
            ECJ: JW2034(cpsB)
            ECE: Z3195(manC) Z3213(cpsB)
            ECS: ECs2836 ECs2854
            ECC: c2558 c2575(cpsB)
            ECI: UTI89_C2323(cpsB)
            ECP: ECP_2074 ECP_2089
            ECV: APECO1_1139(cpsB)
            ECW: EcE24377A_2342(manC)
            ECX: EcHS_A2173
            STY: STY2293(rfbM2) STY2317(cpsB)
            STT: t0767(manC) t0789(rfbM)
            SPT: SPA0761(manC) SPA0787(rfbM)
            SEC: SC2094(manC) SC2106(manC)
            STM: STM2084(rfbM) STM2105.S(manC)
            YPE: YPO3099(manC)
            YPK: y1081(cpsB)
            YPA: YPA_2594
            YPN: YPN_0988
            YPP: YPDSF_2738
            YPS: YPTB1011(manC)
            SFL: SF2112(cpsB_1)
            SFX: S2235(cpsB)
            SFV: SFV_2106(cpsB)
            SSN: SSON_2102(cpsB)
            SBO: SBO_0876(cpsB)
            ECA: ECA1438(rfbM)
            SGL: SG1114
            ENT: Ent638_2644 Ent638_2663
            SPE: Spro_1599
            XFA: XF0259
            XFT: PD0212(xanB)
            XCC: XCC0625(xanB)
            XCB: XC_3609
            XCV: XCV3704(xanB)
            XAC: XAC3580(xanB)
            XOO: XOO0796(xanB)
            XOM: XOO_0724(XOO0724)
            VCH: VC0241
            VCO: VC0395_A2621(rfbA)
            VVY: VV0352
            PAE: PA2232 PA3551(algA) PA5452(wbpW)
            PAU: PA14_71970(wbpW)
            PPU: PP_1277(algA) PP_1776
            PST: PSPTO_1232(algA) PSPTO_3530
            PSB: Psyr_0937 Psyr_1052 Psyr_3302
            PSP: PSPPH_0984 PSPPH_1107(algA) PSPPH_3223
            PFL: PFL_1013 PFL_4209
            PFO: Pfl_0949 Pfl_5683
            PEN: PSEEN3742 PSEEN4546(algA)
            PMY: Pmen_1677 Pmen_4287
            ACI: ACIAD0086(epsM)
            SBM: Shew185_2890
            SHE: Shewmr4_1328
            CPS: CPS_4988
            PHA: PSHAa2920(cpsB)
            PAT: Patl_1792
            SDE: Sde_2134
            PIN: Ping_0766
            MAQ: Maqu_0794
            CBU: CBU_0671(rfbA)
            LPN: lpg2887(rfbA)
            LPF: lpl2800
            LPP: lpp2946
            MCA: MCA2033
            FTU: FTT1448c(manC)
            FTF: FTF1448c(manC)
            FTL: FTL_0608
            FTH: FTH_0609(manC)
            FTN: FTN_1418(manC)
            TCX: Tcr_1678
            NOC: Noc_2483
            AEH: Mlg_0100
            HHA: Hhal_1538
            HCH: HCH_02412
            CSA: Csal_1692
            ABO: ABO_0395(algA)
            MMW: Mmwyl1_0820
            AHA: AHA_2904
            RMA: Rmag_0904
            CVI: CV_3178(manC)
            REH: H16_A1854(manC1) H16_A2905(manC2)
            RME: Rmet_5843
            BMA: BMA0029 BMA2310
            BXE: Bxe_A2248 Bxe_A2514 Bxe_A3867 Bxe_C1090
            BVI: Bcep1808_0815 Bcep1808_4200 Bcep1808_4774 Bcep1808_5609
                 Bcep1808_6528
            BUR: Bcep18194_A3856 Bcep18194_A3979 Bcep18194_B1812
                 Bcep18194_B2277
            BCN: Bcen_0397 Bcen_4160 Bcen_4544
            BCH: Bcen2424_0879 Bcen2424_3819 Bcen2424_4206
            BAM: Bamb_0755 Bamb_3629 Bamb_6494
            BPS: BPSL0605(manC) BPSL2810(manC) BPSS1835
            BPM: BURPS1710b_0808 BURPS1710b_3304 BURPS1710b_A0919
            BTE: BTH_I0522 BTH_I1324 BTH_II0542
            PNU: Pnuc_0301
            RFR: Rfer_0711
            POL: Bpro_3999 Bpro_4942
            PNA: Pnap_3192
            AAV: Aave_0948
            MPT: Mpe_A0629 Mpe_A2729
            HAR: HEAR0728(cpsB)
            MMS: mma_0646(xanB)
            NEU: NE2250
            NET: Neut_0618
            NMU: Nmul_A0261
            EBA: ebA1533(xanB) ebA4723(algA)
            AZO: azo2085(xanB)
            DAR: Daro_2389
            TBD: Tbd_1239
            MFA: Mfla_1268 Mfla_2012
            HPY: HP0043(algA)
            HPJ: jhp0037(manC)
            HPA: HPAG1_0040
            HHE: HH0675
            HAC: Hac_0055(algA)
            TDN: Tmden_1734
            NIS: NIS_0195 NIS_1380
            SUN: SUN_0324 SUN_1275
            GSU: GSU1202
            GME: Gmet_1104
            PCA: Pcar_1279 Pcar_1794
            PPD: Ppro_2094
            DVU: DVU0697
            DVL: Dvul_2267
            DDE: Dde_2931
            LIP: LI0984(xanB)
            BBA: Bd2941(manC)
            DPS: DP2926
            ADE: Adeh_0159
            AFW: Anae109_0165
            SAT: SYN_01031
            SFU: Sfum_3324
            RCO: RC1039 RC1040
            RFE: RF_0241(manC)
            RBE: RBE_0246
            MLO: mlr5802 mlr7607
            MES: Meso_0456
            PLA: Plav_1927
            SME: SMb21082(manC)
            SMD: Smed_4795
            ATU: Atu3353(manC)
            ATC: AGR_L_2939
            RET: RHE_CH03244(noeJ)
            BME: BMEI1395 BMEII0900
            BMF: BAB1_0561 BAB2_0856
            BMS: BR0538 BRA0347
            BMB: BruAb1_0561 BruAb2_0834
            OAN: Oant_2715
            BJA: bll5919(manC)
            BRA: BRADO5152(manC)
            BBT: BBta_5620(manC)
            RPA: RPA3322(manC)
            RPB: RPB_1524
            RPC: RPC_4235
            RPD: RPD_1618
            RPE: RPE_3497 RPE_4272
            NWI: Nwi_1075
            NHA: Nham_1303 Nham_2782
            XAU: Xaut_3550
            CCR: CC_3618
            SIT: TM1040_3778
            RSP: RSP_0834(xanB) RSP_4053(xanB)
            RSH: Rsph17029_2491
            JAN: Jann_4214
            RDE: RD1_B0036(xanB)
            PDE: Pden_4038
            MMR: Mmar10_2434
            NAR: Saro_0742
            SAL: Sala_1593
            SWI: Swit_3438
            ELI: ELI_13430
            GBE: GbCGDNIH1_0356
            ACR: Acry_0548
            RRU: Rru_B0046
            MAG: amb0037
            MGM: Mmc1_0913
            ABA: Acid345_0570
            SUS: Acid_4553
            GKA: GK3304
            CAC: CAC2968 CAC3058 CAC3072
            CPE: CPE0495 CPE2308
            CPR: CPR_2294
            CTC: CTC00265
            CDF: CD2779(manC)
            CBO: CBO0102
            CBE: Cbei_0318
            CKL: CKL_3746(manC)
            DRM: Dred_1397 Dred_3136
            SWO: Swol_0751 Swol_1914
            CSC: Csac_0276 Csac_2018
            MBO: Mb3292c(manC)
            MBB: BCG_3293c(manC)
            CGB: cg0849(rmlA2)
            TWH: TWT356(manC)
            TWS: TW414
            LXX: Lxx04570(manC)
            ART: Arth_1132
            PAC: PPA1696
            NCA: Noca_1407
            KRA: Krad_3951
            STP: Strop_0940
            RBA: RB6254(manC)
            LIL: LA1518(rfbM1) LA3892(rfbM2)
            LIC: LIC12243(manC)
            LBJ: LBJ_1700(manC)
            LBL: LBL_1919(manC)
            SYN: sll1370(rfbM) slr0493(rfbM) slr2074(manA)
            SYW: SYNW0148(manC) SYNW0919
            SYC: syc0065_d(manC)
            SYF: Synpcc7942_1608
            SYD: Syncc9605_0129
            SYE: Syncc9902_0175
            SYG: sync_0160
            SYR: SynRCC307_0649(manC)
            SYX: SynWH7803_0200(manC)
            CYA: CYA_0028 CYA_2501
            CYB: CYB_0688
            TEL: tlr0018
            GVI: glr2138
            ANA: all4342 alr0188
            AVA: Ava_1292 Ava_2680
            PMA: Pro1765(manC)
            PMM: PMM1196(manC)
            PMT: PMT1952(manC)
            PMN: PMN2A_1182
            PMI: PMT9312_1314
            PMB: A9601_13981(manC)
            PMC: P9515_13701(manC)
            PMF: P9303_09641 P9303_26031(manC)
            PMG: P9301_14331(manC)
            PMH: P9215_14171
            PME: NATL1_20571(manC)
            TER: Tery_1856
            BTH: BT_0558 BT_2781
            BFR: BF2935 BF4322
            BFS: BF2817 BF4125
            PGI: PG2215(manC)
            SRU: SRU_0567(manC)
            CHU: CHU_0300(manC)
            GFO: GFO_2884(manC)
            FJO: Fjoh_0355
            FPS: FP1381(manC)
            CTE: CT0309 CT2159
            CCH: Cag_0518 Cag_1821
            CPH: Cpha266_2393 Cpha266_2595
            PVI: Cvib_0276 Cvib_0473
            PLT: Plut_0210 Plut_0421
            DRA: DR_A0032
            DGE: Dgeo_0341
            TTH: TTC1388
            TTJ: TTHA1750
            AAE: aq_589(xanB)
            TMA: TM1033
            TPT: Tpet_1717
            TME: Tmel_0653
            FNO: Fnod_0559
            MMQ: MmarC5_1299
            MMZ: MmarC7_0332
            MAE: Maeo_0403
            MAC: MA3781(rfbM)
            MBA: Mbar_A0229
            MMA: MM_0660
            MBU: Mbur_1613
            MHU: Mhun_3065
            MEM: Memar_0761
            MBN: Mboo_2443
            HAL: VNG2159Gm(manC)
            HMA: rrnAC2742(manC)
            NPH: NP3568A NP4718A
            PAB: PAB0818(manC)
            PFU: PF0589
            TKO: TK1109
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.22
            ExPASy - ENZYME nomenclature database: 2.7.7.22
            ExplorEnz - The Enzyme Database: 2.7.7.22
            ERGO genome analysis and discovery system: 2.7.7.22
            BRENDA, the Enzyme Database: 2.7.7.22
            CAS: 9026-31-7
///
ENTRY       EC 2.7.7.23                 Enzyme
NAME        UDP-N-acetylglucosamine diphosphorylase;
            UDP-N-acetylglucosamine pyrophosphorylase;
            uridine diphosphoacetylglucosamine pyrophosphorylase;
            UTP:2-acetamido-2-deoxy-alpha-D-glucose-1-phosphate
            uridylyltransferase;
            UDP-GlcNAc pyrophosphorylase;
            GlmU uridylyltransferase;
            Acetylglucosamine 1-phosphate uridylyltransferase;
            UDP-acetylglucosamine pyrophosphorylase;
            uridine diphosphate-N-acetylglucosamine pyrophosphorylase;
            uridine diphosphoacetylglucosamine phosphorylase;
            acetylglucosamine 1-phosphate uridylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     UTP:N-acetyl-alpha-D-glucosamine-1-phosphate uridylyltransferase
REACTION    UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate +
            UDP-N-acetyl-D-glucosamine [RN:R00416]
ALL_REAC    R00416;
            (other) R00415
SUBSTRATE   UTP [CPD:C00075];
            N-acetyl-alpha-D-glucosamine 1-phosphate [CPD:C04501]
PRODUCT     diphosphate [CPD:C00013];
            UDP-N-acetyl-D-glucosamine [CPD:C00043]
REFERENCE   1
  AUTHORS   Pattabiramin, T.N. and Bachhawat, B.K.
  TITLE     Purification of uridine diphosphoacetylglucosamine pyrophosphorylase
            from sheep brain.
  JOURNAL   Biochim. Biophys. Acta 50 (1961) 129-134.
  ORGANISM  sheep
REFERENCE   2
  AUTHORS   Strominger, J.L. and Smith, M.S.
  TITLE     Uridine diphosphoacetylglucosamine pyrophosphorylase.
  JOURNAL   J. Biol. Chem. 234 (1959) 1822-1827.
  ORGANISM  cow [GN:bta], Staphylococcus aureus
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K00972  UDP-N-acetylglucosamine pyrophosphorylase
GENES       HSA: 6675(UAP1)
            MMU: 107652(Uap1)
            CFA: 488664(UAP1) 491239(LOC491239)
            BTA: 535325(UAP1)
            XLA: 446803(uap1)
            XTR: 496559(uap1)
            DRE: 322513(uap1)
            CEL: C36A4.4
            ATH: AT1G31070
            OSA: 4336977 4344934
            SCE: YDL103C(QRI1)
            AGO: AGOS_AFL192C
            PIC: PICST_61206(UAP1)
            CAL: CaO19_4265(CaO19.4265)
            CGR: CAGL0L07370g
            SPO: SPBC1289.08
            ANI: AN9094.2
            AFM: AFUA_7G02180
            AOR: AO090038000595
            CNE: CNF01520
            UMA: UM02897.1
            DDI: DDBDRAFT_0219512
            PFA: MAL13P1.218
            CPV: cgd4_810
            CHO: Chro.40100
            TAN: TA20605
            TPV: TP01_0489
            TET: TTHERM_00703670 TTHERM_00929520 TTHERM_00951720
                 TTHERM_01179880
            TBR: Tb11.02.0120
            TCR: 504153.180
            LMA: LmjF33.2520
            EHI: 138.t00017 30.t00023
            ECO: b3730(glmU)
            ECJ: JW3708(glmU)
            ECE: Z5228(glmU)
            ECS: ECs4672
            ECC: c4655(glmU)
            ECI: UTI89_C4282(glmU)
            ECP: ECP_3929
            ECV: APECO1_2731(glmU)
            ECW: EcE24377A_4245(glmU)
            ECX: EcHS_A3945(glmU)
            STY: STY3916(glmU)
            STT: t3657(glmU)
            SPT: SPA3701(glmU)
            SEC: SC3775(glmU)
            STM: STM3862(glmU)
            YPE: YPO4119(glmU)
            YPK: y4133(glmU)
            YPM: YP_4026(glmU)
            YPA: YPA_4164
            YPN: YPN_3976
            YPP: YPDSF_3916
            YPS: YPTB3965(glmU)
            YPI: YpsIP31758_4174(glmU)
            SFL: SF3810(glmU)
            SFX: S3958(glmU)
            SFV: SFV_3756(glmU)
            SSN: SSON_3889(glmU)
            SBO: SBO_3757(glmU)
            SDY: SDY_4018(glmU)
            ECA: ECA4509(glmU)
            PLU: plu0038(glmU)
            BUC: BU027(glmU)
            BAS: BUsg028(glmU)
            BAB: bbp029(glmU)
            WBR: WGLp010(glmU)
            SGL: SG2416
            BFL: Bfl010(glmU)
            BPN: BPEN_010(glmU)
            HIN: HI0642(glmU)
            HIT: NTHI0762(glmU)
            HIP: CGSHiEE_09010(glmU)
            HIQ: CGSHiGG_06500(glmU)
            HDU: HD1511(glmU)
            HSO: HS_0333(glmU)
            PMU: PM1806(glmU)
            MSU: MS1949(glmU)
            APL: APL_0588(glmU)
            XFA: XF1140
            XFT: PD0425(glmU)
            XCC: XCC0558(glmU)
            XCB: XC_3674
            XCV: XCV3762(glmU)
            XAC: XAC3644(glmU)
            XOO: XOO0736(glmU)
            XOM: XOO_0673(XOO0673)
            VCH: VC2762
            VCO: VC0395_A2530(glmU)
            VVU: VV1_1023
            VVY: VV3249
            VPA: VP3067
            VFI: VF2562
            PPR: PBPRA3601
            PAE: PA5552(glmU)
            PAU: PA14_73220(glmU)
            PAP: PSPA7_6354(glmU)
            PPU: PP_5411(glmU)
            PST: PSPTO_5597(glmU)
            PSB: Psyr_5119
            PSP: PSPPH_5205(glmU)
            PFL: PFL_6214(glmU)
            PFO: Pfl_5728
            PEN: PSEEN4849 PSEEN5540(glmU)
            PAR: Psyc_2073(glmU)
            ACI: ACIAD3575(glmU)
            SON: SO_4745(glmU)
            SAZ: Sama_3642
            SLO: Shew_3842
            SPC: Sputcn32_3954
            SHE: Shewmr4_3923
            SHM: Shewmr7_4015
            SHN: Shewana3_0009 Shewana3_4128
            SHW: Sputw3181_4051
            ILO: IL2617(glmU)
            CPS: CPS_4944(glmU)
            PHA: PSHAa3006(glmU)
            PAT: Patl_3879
            SDE: Sde_3959
            PIN: Ping_3204
            CBU: CBU_1947(glmU)
            CBD: COXBU7E912_0173(glmU)
            LPN: lpg2875(glmU)
            LPF: lpl2788(glmU)
            LPP: lpp2934(glmU)
            MCA: MCA0014(glmU)
            FTU: FTT0387(glmU)
            FTF: FTF0387(glmU)
            FTW: FTW_1687(glmU)
            FTL: FTL_0453
            FTH: FTH_0450(glmU)
            FTA: FTA_0480(glmU)
            FTN: FTN_0484(glmU)
            TCX: Tcr_2163
            NOC: Noc_3072
            AEH: Mlg_2867
            HHA: Hhal_2428
            HCH: HCH_07069(glmU)
            CSA: Csal_3282
            AHA: AHA_4260(glmU)
            DNO: DNO_1140(glmU)
            BCI: BCI_0139(glmU)
            VOK: COSY_0932(glmU)
            NME: NMB0038
            NMA: NMA0284(glmU)
            NMC: NMC0015(glmU)
            NGO: NGO2053
            CVI: CV_0674(glmU) CV_3103
            RSO: RSc0177(glmU)
            REU: Reut_A0229
            REH: H16_A0262(glmU)
            RME: Rmet_0186
            BMA: BMA3380(glmU)
            BMV: BMASAVP1_A3051(glmU)
            BML: BMA10299_A2041(glmU)
            BMN: BMA10247_2243(glmU)
            BUR: Bcep18194_A6330
            BCN: Bcen_2367
            BCH: Bcen2424_2981
            BAM: Bamb_3028
            BPS: BPSL0313(glmU)
            BPM: BURPS1710b_0518(glmU)
            BPL: BURPS1106A_0337(glmU)
            BPD: BURPS668_0324(glmU)
            BTE: BTH_I0289(glmU)
            PNU: Pnuc_1992
            BPE: BP3730(glmU)
            BPA: BPP4229(glmU)
            BBR: BB4817(glmU)
            RFR: Rfer_1083
            POL: Bpro_0671
            AJS: Ajs_0636
            VEI: Veis_1504
            MPT: Mpe_A0557
            HAR: HEAR3196(glmU)
            MMS: mma_3441(glmU)
            NEU: NE0208(glmU)
            NET: Neut_0279
            NMU: Nmul_A0312
            EBA: ebA2245(glmU)
            DAR: Daro_0220
            TBD: Tbd_2794
            MFA: Mfla_2742
            HPY: HP0683(glmU)
            HPJ: jhp0624(glmU)
            HPA: HPAG1_0667
            HHE: HH0691(glmU)
            HAC: Hac_0863(glmU)
            WSU: WS2089
            TDN: Tmden_1014
            CJE: Cj0821(glmU)
            CJR: CJE0908(glmU)
            CJJ: CJJ81176_0838(glmU)
            CJU: C8J_0768(glmU)
            CJD: JJD26997_1193(glmU)
            CFF: CFF8240_0753
            CCV: CCV52592_1268(glmU)
            CHA: CHAB381_0968(glmU)
            CCO: CCC13826_0692(glmU)
            ABU: Abu_2204(glmU)
            NIS: NIS_1103(glmU)
            SUN: SUN_1836(glmU)
            GSU: GSU0271(glmU)
            PCA: Pcar_2934
            DVU: DVU2668
            DVL: Dvul_0588
            DDE: Dde_0981 Dde_3640
            LIP: LI0801(glmU)
            BBA: Bd3425(glmU)
            DPS: DP1737
            ADE: Adeh_3958
            MXA: MXAN_1385(glmU)
            SAT: SYN_02437 SYN_02960
            SFU: Sfum_2914
            RPR: RP454
            RTY: RT0441(glmU)
            RCO: RC0680(glmU)
            RFE: RF_0798(glmU)
            RBE: RBE_0567(glmU)
            WOL: WD0133(glmU) WD0611
            WBM: Wbm0088
            AMA: AM058(glmU)
            PUB: SAR11_1152(glmU)
            MLO: mll0836
            MES: Meso_1770
            SME: SMc00232(glmU)
            ATU: Atu1787(glmU)
            ATC: AGR_C_3287
            RET: RHE_CH02090(glmU)
            RLE: RL2381
            BME: BMEII0684
            BMF: BAB2_0657
            BMS: BRA0583(glmU)
            BMB: BruAb2_0641(glmU)
            BOV: BOV_A0548(glmU)
            BJA: bll4608(glmU)
            BRA: BRADO3760(glmU)
            BBT: BBta_4168(glmU)
            RPA: RPA2659(glmU)
            RPB: RPB_2855
            RPC: RPC_2605
            RPD: RPD_2617
            RPE: RPE_2785
            BHE: BH09930(glmU)
            BQU: BQ07650(glmU)
            CCR: CC_2304
            SIL: SPO2797(glmU)
            SIT: TM1040_0728
            RSP: RSP_2503(glmU)
            JAN: Jann_3185
            RDE: RD1_3304(glmU)
            HNE: HNE_0705(glmU)
            ZMO: ZMO0498(glmU)
            NAR: Saro_1199
            SAL: Sala_1370
            ELI: ELI_08815
            GOX: GOX0006(glmU)
            GBE: GbCGDNIH1_1239
            RRU: Rru_A3030
            MAG: amb1280
            ABA: Acid345_1714
            SUS: Acid_4364
            BSU: BG10113(gcaD)
            BHA: BH0065(gcaD)
            BAN: BA0048(gcaD)
            BAR: GBAA0048(gcaD)
            BAA: BA_0637
            BAT: BAS0048
            BCE: BC0054
            BCA: BCE_0047(gcaD)
            BCZ: BCZK0044(gcaD)
            BTK: BT9727_0044(gcaD)
            BTL: BALH_0044(gcaD)
            BLI: BL00520(gcaD)
            BLD: BLi00063(gcaD)
            BCL: ABC0078(gcaD)
            BAY: RBAM_000590(gcaD)
            BPU: BPUM_0034(gcaD)
            OIH: OB0058
            GKA: GK0043
            SAU: SA0457(gcaD) SA1974
            SAV: SAV0499(gcaD) SAV2171
            SAM: MW0454(gcaD) MW2097
            SAR: SAR0500(gcaD) SAR2262
            SAS: SAS0456 SAS2072
            SAC: SACOL0543(glmU) SACOL2161
            SAB: SAB0448(gcaD) SAB2052c
            SAA: SAUSA300_0477(glmU) SAUSA300_2130
            SAO: SAOUHSC_00471 SAOUHSC_02423
            SEP: SE1761 SE2284
            SER: SERP0137(glmU) SERP1770
            SHA: SH0870 SH2512(gcaD)
            SSP: SSP0716 SSP2257
            LMO: lmo0198(gcaD)
            LMF: LMOf2365_0209
            LIN: lin0237(gcaD)
            LWE: lwe0167(gcaD)
            LLA: L134450(glmU)
            LLC: LACR_2079
            LLM: llmg_2076(glmU)
            SPY: SPy_0443(gcaD)
            SPZ: M5005_Spy_0362(gcaD)
            SPM: spyM18_0486(glmU)
            SPG: SpyM3_0312(glmU)
            SPS: SPs1545
            SPH: MGAS10270_Spy0365(gcaD)
            SPI: MGAS10750_Spy0364(gcaD)
            SPJ: MGAS2096_Spy0381(gcaD)
            SPK: MGAS9429_Spy0365(gcaD)
            SPF: SpyM51503(gcaD)
            SPA: M6_Spy0386
            SPB: M28_Spy0351(gcaD)
            SPN: SP_0988
            SPR: spr0891(gcaD)
            SPD: SPD_0874(glmU)
            SAG: SAG1538(glmU)
            SAN: gbs1594
            SAK: SAK_1561(glmU)
            SMU: SMU.1635(glmU)
            STC: str0563(gcaD)
            STL: stu0563(gcaD)
            STE: STER_0603
            SSU: SSU05_1584
            SSV: SSU98_1594
            SGO: SGO_1469(glmU)
            LPL: lp_0467(glmU)
            LJO: LJ0208
            LAC: LBA0219
            LSA: LSA1648(glmU)
            LSL: LSL_0317(glmU)
            LDB: Ldb0348(gcaD)
            LBU: LBUL_0303
            LBR: LVIS_0475
            LGA: LGAS_0211
            PPE: PEPE_0293
            EFA: EF0059(glmU)
            OOE: OEOE_1542
            STH: STH3240
            CAC: CAC3222(gcaD)
            CPE: CPE2490
            CPF: CPF_2813(glmU)
            CPR: CPR_2499(glmU)
            CTC: CTC00187
            CNO: NT01CX_1014
            CDF: CD3515(gcaD)
            CBO: CBO3545(glmU)
            CBA: CLB_3626(glmU)
            CBH: CLC_3523(glmU)
            CBF: CLI_3765(glmU)
            CHY: CHY_0192(glmU)
            DSY: DSY0152
            DRM: Dred_0099
            SWO: Swol_0067
            TTE: TTE2572(glmU)
            MTA: Moth_0075
            MTU: Rv1018c(glmU)
            MTC: MT1046(glmU)
            MBO: Mb1046c(glmU)
            MBB: BCG_1075c(glmU)
            MLE: ML0249(glmU)
            MPA: MAP0984c(glmU)
            MAV: MAV_1157(glmU)
            MSM: MSMEG_5426(glmU)
            MVA: Mvan_4782
            MMC: Mmcs_4248
            CGL: NCgl0906(cgl0943)
            CGB: cg1076(glmU)
            CEF: CE1016
            CDI: DIP0904
            CJK: jk1492(glmU)
            NFA: nfa48780(glmU)
            RHA: RHA1_ro05724
            SCO: SCO3122(SCE41.31)
            SMA: SAV3561(glmU)
            TWH: TWT188
            TWS: TW584
            LXX: Lxx17430(glmU)
            CMI: CMM_2275(glmU)
            PAC: PPA0530
            NCA: Noca_0908
            TFU: Tfu_0414
            FAL: FRAAL6282(glmU)
            ACE: Acel_1947
            SEN: SACE_0817(glmU)
            BLO: BL0964(glmU)
            FNU: FN1991
            RBA: RB6841(glmU) RB6977
            CTR: CT629(glmU) CT715
            CTA: CTA_0682(glmU) CTA_0777
            CMU: TC0088 TC0918
            CPN: CPn0749(glmU) CPn0856
            CPA: CP1013 CP1124
            CPJ: CPj0749(glmU) CPj0856
            CPT: CpB0777 CpB0885
            CCA: CCA00911 CCA01008
            CAB: CAB879 CAB978
            CFE: CF0004(glmU) CF0103(uap)
            PCU: pc0016(glmU) pc1997(glmU)
            LIL: LA3823(glmU)
            LIC: LIC10428(glmU)
            LBJ: LBJ_2586(glmU)
            LBL: LBL_0526(glmU)
            SYN: sll0899(glmU)
            SYW: SYNW1003(glmU)
            SYC: syc1224_d(glmU)
            SYF: Synpcc7942_0288
            SYD: Syncc9605_1129
            SYE: Syncc9902_1328
            SYG: sync_1533
            SYR: SynRCC307_1148(glmU)
            SYX: SynWH7803_1030(glmU)
            CYA: CYA_1151(glmU)
            CYB: CYB_2635(glmU)
            TEL: tlr0393
            GVI: glr0443
            ANA: alr3921
            AVA: Ava_1776
            PMA: Pro1050(glmU)
            PMM: PMM0611(glmU)
            PMT: PMT0400(glmU)
            PMN: PMN2A_0047
            PMI: PMT9312_0611
            PMB: A9601_06671(glmU)
            PMC: P9515_06761(glmU)
            PMF: P9303_18871(glmU)
            PMG: P9301_06371(glmU)
            PMH: P9215_06931(glmU)
            CHU: CHU_0658(glmU) CHU_1978(flu)
            CTE: CT0251
            CPH: Cpha266_0378
            PLT: Plut_1770
            DRA: DR_0808
            DGE: Dgeo_1967
            TTH: TTC0017
            TTJ: TTHA0385
            AAE: aq_607(glmU)
            TMA: TM1629
            HMA: pNG7236(glmU)
STRUCTURES  PDB: 1FWY  1FXJ  1G95  1G97  1HM0  1HM8  1HM9  1HV9  1JVD  1JVG  
                 1VM8  2NPO  2OI5  2OI6  2OI7  2YQC  2YQH  2YQJ  2YQS  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.23
            ExPASy - ENZYME nomenclature database: 2.7.7.23
            ExplorEnz - The Enzyme Database: 2.7.7.23
            ERGO genome analysis and discovery system: 2.7.7.23
            BRENDA, the Enzyme Database: 2.7.7.23
            CAS: 9023-06-7
///
ENTRY       EC 2.7.7.24                 Enzyme
NAME        glucose-1-phosphate thymidylyltransferase;
            glucose 1-phosphate thymidylyltransferase;
            dTDP-glucose synthase;
            dTDP-glucose pyrophosphorylase;
            thymidine diphosphoglucose pyrophosphorylase;
            thymidine diphosphate glucose pyrophosphorylase;
            TDP-glucose pyrophosphorylase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     dTTP:alpha-D-glucose-1-phosphate thymidylyltransferase
REACTION    dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-glucose
            [RN:R02328]
ALL_REAC    R02328
SUBSTRATE   dTTP [CPD:C00459];
            alpha-D-glucose 1-phosphate [CPD:C00103]
PRODUCT     diphosphate [CPD:C00013];
            dTDP-glucose [CPD:C00842]
REFERENCE   1
  AUTHORS   Kornfeld, S. and Glaser, L.
  TITLE     The enzymic synthesis of thymidine-linked sugars. I. Thymidine
            diphosphate glucose.
  JOURNAL   J. Biol. Chem. 236 (1961) 1791-1794.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   2
  AUTHORS   Pazur, J.H. and Shuey, E.W.
  TITLE     The enzymatic synthesis of thymidine diphosphate glucose and its
            conversion to thymidine diphosphate rhamnose.
  JOURNAL   J. Biol. Chem. 236 (1961) 1780-1785.
  ORGANISM  Streptococcus faecalis
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
            PATH: map00521  Streptomycin biosynthesis
            PATH: map00523  Polyketide sugar unit biosynthesis
ORTHOLOGY   KO: K00973  glucose-1-phosphate thymidylyltransferase
GENES       ECO: b2039(rfbA) b3789(rffH)
            ECJ: JW2024(rfbA) JW3763(rffH)
            ECE: Z5300(rffH)
            ECS: ECs4722
            ECC: c4709(rffH)
            ECI: UTI89_C2241 UTI89_C2310(rfbA) UTI89_C4345(rffH)
            ECP: ECP_3980
            ECV: APECO1_1129(rmlA) APECO1_2686(rffH)
            ECW: EcE24377A_2330(rfbA1) EcE24377A_4300(rfbA2)
            ECX: EcHS_A2181(rfbA2) EcHS_A4006(rfbA1)
            STY: STY2305(rfbA) STY3632(rffH)
            STT: t0777(rfbA) t3374(rffH)
            SPT: SPA0771(rfbA) SPA3763(rffH)
            SEC: SC3828(rffH)
            STM: STM2095(rfbA)
            YPE: YPO3861(rffH)
            YPK: y0367(rffH)
            YPM: YP_3184(rffH)
            YPA: YPA_0157
            YPN: YPN_0102
            YPS: YPTB0173(rffH)
            YPI: YpsIP31758_0187(rfbA)
            YEN: YE0174(rffH)
            SFL: SF2102(rfbA) SF3863(rffH)
            SFX: S2225(rfbA) S3897(rffH)
            SFV: SFV_2096(rfbA) SFV_3715(rffH)
            SSN: SSON_3961(rffH)
            SBO: SBO_0866(rfbA) SBO_3800(rffH)
            SDY: SDY_2206(rfbA) SDY_3959(rffH)
            ECA: ECA1442(rfbA)
            PLU: plu4657(rffH) plu4811(wblO)
            SGL: SG2380
            HDU: HD0688(rmlA)
            XFA: XF0256
            XFT: PD0209(rfbA)
            XCC: XCC0622(rmlA)
            XCB: XC_3612
            XCV: XCV3708(rmlA)
            XAC: XAC3584(rmlA)
            XOO: XOO0793(rmlA)
            XOM: XOO_0721(XOO0721)
            VVY: VV0301
            VPA: VP0223
            VFI: VF0167
            PAE: PA5163(rmlA)
            PAU: PA14_68200(rmlA)
            PAP: PSPA7_5902(rfbA)
            PPU: PP_1783(rmlA)
            PST: PSPTO_1079(rfbA)
            PSB: Psyr_0924
            PSP: PSPPH_0967(rfbA)
            PFL: PFL_0304(rfbA)
            PFO: Pfl_0702 Pfl_4056
            PEN: PSEEN0252(rmlA) PSEEN4744(rmlA-2)
            PAR: Psyc_1214(rfbA)
            PCR: Pcryo_0625
            ACI: ACIAD0079(rmlA)
            SON: SO_3186(rfbA)
            SDN: Sden_2662
            SFR: Sfri_2758 Sfri_2829
            SBL: Sbal_2889
            SLO: Shew_1402
            SHE: Shewmr4_1319
            SHM: Shewmr7_1403
            SHN: Shewana3_1380 Shewana3_1391
            SHW: Sputw3181_1464
            ILO: IL0542(rffH)
            PAT: Patl_2131
            SDE: Sde_2130
            PIN: Ping_3464
            CBU: CBU_1834(rmlA)
            CBD: COXBU7E912_0064(rfbA)
            LPN: lpg0760(rfbA)
            LPF: lpl0797(rmlA)
            LPP: lpp0826(rmlA)
            MCA: MCA1283(rfbA)
            FTU: FTT1451c(wbtL)
            FTF: FTF1451c(wbtL)
            FTW: FTW_0424(wbtL)
            FTL: FTL_0605
            FTH: FTH_0605
            FTA: FTA_0639(rfbA)
            NOC: Noc_0774
            AEH: Mlg_2319
            HCH: HCH_02408(rfbA)
            ABO: ABO_0913(rmlA)
            AHA: AHA_2906(rfbA)
            NME: NMB0062 NMB0080
            NMA: NMA0188(rfbA2) NMA0205(rfbA)
            NMC: NMC0046(rfbA) NMC0064(rfbA2)
            NGO: NGO1898
            CVI: CV_0674(glmU) CV_3103 CV_4012(rfbA) CV_4226
            RSO: RSc0684(rfbA)
            REU: Reut_A0714
            REH: H16_A1864(rfbA) H16_A2907
            RME: Rmet_2733
            BMA: BMA1989(rfbA)
            BMV: BMASAVP1_A0924(rfbA)
            BML: BMA10299_A2754(rfbA)
            BMN: BMA10247_1851(rfbA)
            BXE: Bxe_A3726 Bxe_A3801 Bxe_B1715
            BUR: Bcep18194_A3970
            BCN: Bcen_0390
            BCH: Bcen2424_0872 Bcen2424_6649
            BAM: Bamb_0752 Bamb_3386
            BPS: BPSL2685(rmlA)
            BPM: BURPS1710b_3162(rfbA)
            BPL: BURPS1106A_3140(rfbA)
            BPD: BURPS668_3103(rfbA)
            BTE: BTH_I1470(rfbA)
            RFR: Rfer_2677
            POL: Bpro_4018
            PNA: Pnap_3489
            AAV: Aave_4164
            AJS: Ajs_0539
            VEI: Veis_0696
            MPT: Mpe_A0626
            HAR: HEAR1153(rfbA)
            MMS: mma_2252(rfbA)
            NEU: NE0677(rmlA)
            NET: Neut_1880
            NMU: Nmul_A0266
            EBA: ebA2277(rmlA)
            AZO: azo1875(rmlA)
            DAR: Daro_1238
            TBD: Tbd_1779
            MFA: Mfla_2009
            HHE: HH0100
            CCV: CCV52592_0305(rfbA)
            ABU: Abu_1817
            SUN: SUN_1554
            GSU: GSU2083(rfbA)
            GME: Gmet_0924
            PCA: Pcar_0276 Pcar_2595
            DVU: DVU0925(rfbA)
            DDE: Dde_2693
            LIP: LI0577
            BBA: Bd1870(rfbA)
            DPS: DP0044 DP2221
            ADE: Adeh_4290
            MXA: MXAN_4611(rfbA)
            SAT: SYN_02647
            SFU: Sfum_2263 Sfum_3965
            MLO: mlr7550
            MES: Meso_2760
            SME: SMb21324(expA7)
            ATU: Atu4615
            ATC: AGR_L_532
            RET: RHE_CH01512(ypch00521)
            RLE: RL0795 RL1623(rfbA)
            BRA: BRADO2073 BRADO7028(rfbA)
            BBT: BBta_1073(rfbA)
            RPA: RPA0120(rmlA)
            RPB: RPB_1565
            RPC: RPC_4186
            RPD: RPD_1574
            NWI: Nwi_0545
            NHA: Nham_1059 Nham_3052
            CCR: CC_1141
            SIT: TM1040_3859
            RSP: RSP_3848(rmlA)
            JAN: Jann_3841
            RDE: RD1_B0017(rfbA)
            MMR: Mmar10_2458
            HNE: HNE_0789(rfbA)
            NAR: Saro_3238
            GOX: GOX1052
            GBE: GbCGDNIH1_0103
            RRU: Rru_B0048
            MAG: amb0059
            MGM: Mmc1_1406
            BSU: BG10617(spsI)
            BHA: BH3363(spsI)
            BAN: BA1228
            BAR: GBAA1228
            BAA: BA_1763
            BAT: BAS1135
            BCE: BC1212
            BCA: BCE_1335
            BCZ: BCZK1109(rfbA)
            BTK: BT9727_1115(rfbA)
            BTL: BALH_1075(rfbA)
            BCL: ABC3691
            BPU: BPUM_3227
            OIH: OB1129 OB2421
            LMO: lmo1081
            LLA: L197041(rmlA)
            LLC: LACR_0200
            LLM: llmg_0206(rmlA)
            SPY: SPy_0933(cpsFO)
            SPZ: M5005_Spy_0734(cpsFO)
            SPM: spyM18_0990(cpsFO)
            SPG: SpyM3_0646(rmlA)
            SPS: SPs1206
            SPH: MGAS10270_Spy0793(cpsFO)
            SPI: MGAS10750_Spy0828(cpsFO)
            SPJ: MGAS2096_Spy0808(cpsFO)
            SPK: MGAS9429_Spy0792(cpsFO)
            SPF: SpyM51073(rmlA)
            SPA: M6_Spy0760
            SPB: M28_Spy0714(cpsFO)
            SPR: spr0320(cps2L)
            SPD: SPD_0328(cps2L)
            SAG: SAG1200(rfbA)
            SAN: gbs1273(rmlA)
            SAK: SAK_1287(rfbA)
            SMU: SMU.1461(rmlA)
            STC: str1244(rmlA)
            STL: stu1244(rmlA)
            STE: STER_1224
            SSA: SSA_1411(rmlA)
            SGO: SGO_1009(rfbA-1)
            LPL: lp_1186(rfbA)
            LJO: LJ1050
            LSL: LSL_1572(rfbA)
            LDB: Ldb1695(rfbA)
            LBU: LBUL_1570
            LCA: LSEI_2015
            EFA: EF2194(rfbA)
            OOE: OEOE_1449
            STH: STH777
            CAC: CAC2333(spsI)
            CPE: CPE0616(rfbA)
            CPF: CPF_0479(rfbA) CPF_0597(rfbA)
            CBO: CBO2055
            CBA: CLB_1994
            CBH: CLC_1999
            CBF: CLI_2115
            CHY: CHY_0976
            DSY: DSY3317
            MTU: Rv0334(rmlA)
            MTC: MT0348(rfbA)
            MBO: Mb0341(rmlA)
            MBB: BCG_0373(rmlA)
            MLE: ML2503(rfbA)
            MPA: MAP3828(rmlA)
            MAV: MAV_4820(rfbA)
            MSM: MSMEG_0384(rfbA) MSMEG_5983(rfbA)
            MMC: Mmcs_0436
            CGL: NCgl0325(cgl0332)
            CGB: cg0401(rmlA1)
            CEF: CE0342
            CDI: DIP0360(rfbA)
            CJK: jk1882(rmlA)
            NFA: nfa2070(rfbA)
            RHA: RHA1_ro04097
            SMA: SAV947(aveBIII)
            TWH: TWT032(rmlA)
            TWS: TW036
            LXX: Lxx04930(rmlA)
            CMI: CMM_1013(rmlA)
            AAU: AAur_2166(rfbA) AAur_3159(rfbA)
            PAC: PPA2288
            FRA: Francci3_0713
            FAL: FRAAL1228
            ACE: Acel_0413
            SEN: SACE_6883(rfbA)
            BLO: BL0227(rmlA)
            BAD: BAD_1509
            RXY: Rxyl_3121
            RBA: RB4043
            PCU: pc0123(rfbA)
            TDE: TDE1440(rfbA)
            LIL: LA1662(rmlA) LA3802(rfbA)
            LIC: LIC10444 LIC12123(rfbA)
            LBJ: LBJ_1184(rmlA)
            LBL: LBL_1238(rmlA)
            SYN: sll0207(rfbA)
            SYW: SYNW0649(rmlA)
            SYC: syc1992_c(rfbA)
            SYF: Synpcc7942_2101
            SYD: Syncc9605_2032
            SYE: Syncc9902_0637
            SYR: SynRCC307_0081(rmlA)
            SYX: SynWH7803_0102(rmlA)
            TEL: tll0457(rfbA)
            GVI: gll1783 glr0469(rfbA) glr3237(rfbA)
            ANA: alr4491
            AVA: Ava_3356
            PMT: PMT0084 PMT0112(rmlA)
            PMN: PMN2A_1237
            PMB: A9601_14401
            PMC: P9515_14101(rfbA)
            PMF: P9303_00981
            PMH: P9215_14411
            PME: NATL1_21091(rfbA)
            TER: Tery_1537
            BTH: BT_0463 BT_2017
            BFR: BF0805 BF1094 BF2583 BF3664 BF3712
            BFS: BF1011(rmlA2) BF1551(rmlA1) BF3453(rffH1) BF3505(rffH2)
            PGI: PG1563(rfbA)
            SRU: SRU_0589(rfbA) SRU_0651(graD)
            CHU: CHU_0020(rfbA) CHU_3390(rfbA)
            GFO: GFO_2036(rmlA)
            FPS: FP1293(rmlA)
            CTE: CT0305(rfbA) CT0727
            CCH: Cag_0512 Cag_1546
            PLT: Plut_0416 Plut_0673
            DET: DET0529 DET0530
            DEH: cbdb_A499(rfbA) cbdb_A500
            DRA: DR_A0031 DR_A0042
            DGE: Dgeo_0340 Dgeo_2643
            TTH: TTC1762
            TTJ: TTHA0224
            TMA: TM0862
            MMP: MMP1076
            MAC: MA2183(rbfA) MA3022(rfbA) MA3025(rfbA) MA3777(rfbA)
            MBA: Mbar_A0233 Mbar_A2020 Mbar_A2023
            MMA: MM_0299 MM_0302 MM_1169 MM_2216
            MBU: Mbur_2230 Mbur_2341 Mbur_2344
            MHU: Mhun_3075 Mhun_3107
            MST: Msp_1102 Msp_1301
            MSI: Msm_0655 Msm_1307
            MKA: MK0892
            HAL: VNG0008G(graD5) VNG0009G(graD2) VNG0047Gm(graD6)
                 VNG0064G(graD3) VNG0390G(graD1) VNG1055G(graD4)
            HMA: pNG7218(rffH4) rrnAC0633(rffH2) rrnAC1081(rffH1)
                 rrnAC1960(graD4b) rrnAC2343(rfbA) rrnAC3232(graD4c)
                 rrnAC3238(rffH3)
            HWA: HQ1670A(graD) HQ2682A(graD) HQ2989A(graD) HQ2992A(graD)
                 HQ3507A(graD)
            NPH: NP0384A(graD_7) NP2386A(graD_5) NP4276A(graD_6)
                 NP4652A(graD_1) NP4656A(graD_2) NP4674A(graD_3)
            TAC: Ta1074
            TVO: TVN0529 TVN0899
            PTO: PTO1079
            PHO: PH0380 PH1925
            PAB: PAB0784(graD-3) PAB1053(graD-1) PAB1115(graD-2)
            PFU: PF0235 PF0446
            TKO: TK1188 TK1711 TK2279
            RCI: LRC555(rfbA-2) RCIX1434(rfbA-3) RCIX1438(rfbA-4)
                 RCIX198(rfbA-1)
            APE: APE_1181 APE_1202.1 APE_1208.1 APE_2291
            SSO: SSO0745 SSO0831 SSO1782
            STO: ST0452 ST1971
            SAI: Saci_0619 Saci_1703
            NEQ: NEQ025
STRUCTURES  PDB: 1FXO  1FZW  1G0R  1G1L  1G23  1G2V  1G3L  1H5R  1H5S  1H5T  
                 1IIM  1IIN  1LVW  1MC3  1MP3  1MP4  1MP5  2GGO  2GGQ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.24
            ExPASy - ENZYME nomenclature database: 2.7.7.24
            ExplorEnz - The Enzyme Database: 2.7.7.24
            ERGO genome analysis and discovery system: 2.7.7.24
            BRENDA, the Enzyme Database: 2.7.7.24
            CAS: 9026-03-3
///
ENTRY       EC 2.7.7.25                 Enzyme
NAME        tRNA adenylyltransferase;
            tRNA CCA-pyrophosphorylase;
            tRNA-nucleotidyltransferase;
            transfer-RNA nucleotidyltransferase;
            transfer ribonucleic acid nucleotidyl transferase;
            CTP(ATP):tRNA nucleotidyltransferase;
            transfer ribonucleate adenylyltransferase;
            transfer ribonucleate adenyltransferase;
            transfer RNA adenylyltransferase;
            transfer ribonucleate nucleotidyltransferase;
            ATP (CTP):tRNA nucleotidyltransferase;
            ribonucleic cytidylic cytidylic adenylic pyrophosphorylase;
            transfer ribonucleate nucleotidyltransferase;
            transfer ribonucleic adenylyl (cytidylyl) transferase;
            transfer ribonucleic-terminal trinucleotide nucleotidyltransferase;
            transfer ribonucleate cytidylyltransferase;
            ribonucleic cytidylyltransferase;
            -C-C-A pyrophosphorylase;
            tRNA cytidylyltransferase;
            ATP(CTP)-tRNA nucleotidyltransferase;
            tRNA adenylyl(cytidylyl)transferase;
            CTP:tRNA cytidylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ATP:tRNA adenylyltransferase
REACTION    ATP + tRNAn = diphosphate + tRNAn+1 [RN:R07284]
ALL_REAC    R07284
SUBSTRATE   ATP [CPD:C00002];
            tRNA(n) [CPD:C00066]
PRODUCT     diphosphate [CPD:C00013];
            tRNA(n+1) [CPD:C00066]
COMMENT     May be identical with EC 2.7.7.21 tRNA cytidylyltransferase.
REFERENCE   1  [PMID:4927556]
  AUTHORS   Best AN, Novelli GD.
  TITLE     Studies with tRNA adenylyl(cytidylyl)transferase from Escherichia
            coli B. I. Purification and kinetic properties.
  JOURNAL   Arch. Biochem. Biophys. 142 (1971) 527-38.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4927557]
  AUTHORS   Best AN, Novelli GD.
  TITLE     Studies with tRNA adenylyl(cytidylyl)transferase from Escherichia
            coli B. II. Regulation of AMP and CMP incorporation into tRNApCpC
            and tRNApC.
  JOURNAL   Arch. Biochem. Biophys. 142 (1971) 539-47.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Deutscher, M.
  TITLE     Synthesis and functions of the -C-C-A terminus of transfer RNA.
  JOURNAL   Prog. Nucleic Acid Res. Mol. Biol. 13 (1972) 51-92.
REFERENCE   4
  AUTHORS   Starr, J.L. and Goldthwait, D.A.
  TITLE     The incorporation of nucleotides into amino acid transfer
            ribonucleic acid. I. The partial purification and properties of an
            enzyme catalyzing the incorporation of adenylic acid into the
            terminal position.
  JOURNAL   J. Biol. Chem. 238 (1963) 682-689.
  ORGANISM  rabbit
ORTHOLOGY   KO: K00974  tRNA nucleotidyltransferase (CCA-adding enzyme)
            KO: K07558  tRNA nucleotidyltransferase (CCA-adding enzyme)
GENES       HSA: 51095(TRNT1)
            PTR: 470735(TRNT1)
            MMU: 70047(Trnt1)
            RNO: 312616(Trnt1) 64183(Pde4dip)
            CFA: 476552(TRNT1)
            XTR: 394602(trnt1)
            DRE: 415249(trnt1)
            SPU: 581945(LOC581945)
            DME: Dmel_CG2100
            CEL: F55B12.4
            ATH: AT1G22660 AT1G28090
            CME: CML128C
            SCE: YER168C(CCA1)
            AGO: AGOS_AGR118W
            CGR: CAGL0L11858g
            SPO: SPAC1093.04c SPCC645.10
            AFM: AFUA_2G16660
            CNE: CNB02860
            ECU: ECU03_1440
            DDI: DDBDRAFT_0191978 DDBDRAFT_0216798
            PFA: PF11_0212
            CPV: cgd3_2040
            CHO: Chro.30241
            TPV: TP03_0507
            TBR: Tb09.211.0590
            TCR: 506649.100 508349.20
            LMA: LmjF04.1190
            EHI: 133.t00030 44.t00011
            ECO: b3056(cca)
            ECJ: JW3028(cca)
            ECE: Z4409(cca)
            ECS: ECs3939
            ECC: c3806(cca)
            ECI: UTI89_C3492(cca)
            ECP: ECP_3146
            ECV: APECO1_3358(cca)
            ECW: EcE24377A_3519(cca)
            ECX: EcHS_A3233(cca)
            STY: STY3383(cca)
            STT: t3124(cca)
            SPT: SPA3072(cca)
            SEC: SC3151(cca)
            STM: STM3204(cca)
            YPE: YPO0650(cca)
            YPK: y3529(cca)
            YPM: YP_2965(cca)
            YPA: YPA_3140
            YPN: YPN_0510
            YPS: YPTB3411(cca)
            YPI: YpsIP31758_0560(cca)
            SFL: SF3097(cca)
            SFX: S3302(cca)
            SFV: SFV_3096(cca)
            SSN: SSON_3193(cca)
            SBO: SBO_2912(cca)
            SDY: SDY_3239(cca)
            ECA: ECA3588(cca)
            PLU: plu3972(cca)
            BUC: BU061(cca)
            BAS: BUsg058(cca)
            BAB: bbp057(cca)
            BCC: BCc_038(cca)
            WBR: WGLp238(cca)
            SGL: SG0258
            BFL: Bfl062(cca)
            BPN: BPEN_064(cca)
            HIN: HI1606(cca)
            HIT: NTHI1436(cca)
            HDU: HD1091(cca)
            HSO: HS_1193(cca)
            PMU: PM0247(cca)
            MSU: MS2312(pcnB)
            APL: APL_0915
            XFA: XF1362
            XFT: PD0602(cca)
            XCC: XCC3407(cca)
            XCB: XC_0757
            XCV: XCV0773(cca)
            XAC: XAC0717(cca)
            XOO: XOO3900(cca)
            XOM: XOO_3681(XOO3681)
            VCH: VC2446
            VCO: VC0395_A2024(cca)
            VVU: VV1_0622
            VVY: VV0571
            VPA: VP0414
            VFI: VF2244
            PPR: PBPRA0439
            PAE: PA0584(cca)
            PAU: PA14_07620(cca)
            PPU: PP_0394
            PST: PSPTO_0544(cca)
            PSB: Psyr_4634
            PSP: PSPPH_0626(cca)
            PFL: PFL_5656(cca)
            PFO: Pfl_5142
            PEN: PSEEN0421(cca)
            PMY: Pmen_3037
            PAR: Psyc_1368(cca)
            ACI: ACIAD2288(cca)
            SON: SO_1295.2
            SDN: Sden_2823
            SHN: Shewana3_3076
            ILO: IL1966(cca)
            CPS: CPS_4215(cca)
            PHA: PSHAa0625(cca)
            CBU: CBU_1827
            LPN: lpg2742
            LPF: lpl2667(cca)
            LPP: lpp2798(cca)
            MCA: MCA0022(cca)
            FTU: FTT0108c(cca)
            FTF: FTF0108c(cca)
            FTW: FTW_0193
            FTL: FTL_1669
            FTH: FTH_1610(cca)
            FTA: FTA_1766
            FTN: FTN_1607(cca)
            TCX: Tcr_0240
            NOC: Noc_0389
            HCH: HCH_01366(cca)
            ABO: ABO_2052(cca)
            AHA: AHA_3784
            DNO: DNO_1060(cca)
            BCI: BCI_0622(cca)
            VOK: COSY_0197(cca)
            NME: NMB1241
            NMA: NMA1410(cca)
            NMC: NMC1142(cca)
            NGO: NGO0763
            CVI: CV_2032(cca)
            RSO: RSc0085(cca)
            REU: Reut_A0222
            REH: H16_A0253(cca)
            RME: Rmet_0179
            BMA: BMA3317(cca)
            BMV: BMASAVP1_A2987(cca)
            BML: BMA10299_A2105(cca)
            BXE: Bxe_A0201
            BUR: Bcep18194_A6378
            BAM: Bamb_3076
            BPS: BPSL0265(cca)
            BPM: BURPS1710b_0457(cca)
            BTE: BTH_I0236
            BPE: BP3059(cca)
            BPA: BPP0203(cca)
            BBR: BB0207(cca)
            RFR: Rfer_1090
            POL: Bpro_3914
            MPT: Mpe_A3298
            HAR: HEAR2944(cca)
            MMS: mma_3190(cca)
            NEU: NE1614(cca)
            NET: Neut_0503
            NMU: Nmul_A2451
            EBA: ebA3379(cca)
            AZO: azo0493(cca1) azo2549(cca2)
            DAR: Daro_4135
            TBD: Tbd_2360
            MFA: Mfla_2259
            WSU: WS1819
            TDN: Tmden_0005
            CJE: Cj0789
            CJR: CJE0880
            CJU: C8J_0740
            CCO: CCC13826_1816
            ABU: Abu_0390
            SUN: SUN_0962(cca)
            GSU: GSU2184
            GME: Gmet_2285
            PPD: Ppro_2054
            DVU: DVU1836
            DDE: Dde_2083
            BBA: Bd1820
            ADE: Adeh_1480
            ECN: Ecaj_0892
            MES: Meso_2176
            SME: SMc02700
            ATC: AGR_C_4092(pcnB)
            BME: BMEI0463
            BRA: BRADO1968
            BBT: BBta_2275
            RPE: RPE_0944
            NWI: Nwi_2622
            BBK: BARBAKC583_1006(trnT)
            RDE: RD1_0409
            ZMO: ZMO1056(cca)
            NAR: Saro_1021
            ELI: ELI_02245
            GBE: GbCGDNIH1_1633
            RRU: Rru_A0366
            MAG: amb4158
            MGM: Mmc1_1939
            BSU: BG11208(cca)
            BHA: BH1684(papS)
            BAN: BA1559(pcnB)
            BAR: GBAA1559(pcnB)
            BAT: BAS1446
            BCE: BC1536
            BCA: BCE_1665(pcnB)
            BCZ: BCZK1419(pcnB)
            BCY: Bcer98_3284
            BTK: BT9727_1418(pcnB)
            BLI: BL02754(cca)
            BLD: BLi02380(cca)
            BCL: ABC2069(cca)
            BAY: RBAM_020600(cca)
            BPU: BPUM_1976(cca)
            OIH: OB1765
            GKA: GK2181
            SAU: SA1290
            SAV: SAV1457
            SAM: MW1347
            SAR: SAR1468(papS)
            SAS: SAS1400
            SAC: SACOL1497(papS)
            SAO: SAOUHSC_01474
            SAJ: SaurJH9_1756
            SAH: SaurJH1_1790
            SEP: SE1145
            SER: SERP1027(papS)
            LMO: lmo1905(cca)
            LMF: LMOf2365_1934
            LIN: lin2019(cca)
            LLA: L0324(papL)
            SPY: SPy_0866(papS)
            SPZ: M5005_Spy_0673(papS)
            SPM: spyM18_0927(papS)
            SPG: SpyM3_0587(papS)
            SPS: SPs1266
            SPH: MGAS10270_Spy0731(papS)
            SPI: MGAS10750_Spy0764(papS)
            SPJ: MGAS2096_Spy0744(papS)
            SPK: MGAS9429_Spy0728(papS)
            SPF: SpyM51134(cca)
            SPA: M6_Spy0691
            SPB: M28_Spy0653(papS)
            SPN: SP_1554
            SPR: spr1413(cca)
            SAG: SAG1341
            SAN: gbs1411
            SMU: SMU.901(papS)
            STC: str0425(papL)
            STL: stu0425(papL)
            SSA: SSA_1086(papS)
            LPL: lp_1873(papL)
            LJO: LJ1100
            LAC: LBA0973
            LDB: Ldb1280(cca)
            LBU: LBUL_1197
            LBR: LVIS_0782
            LCA: LSEI_1384
            EFA: EF1558(papS)
            CTC: CTC01205
            CTH: Cthe_1389
            CBE: Cbei_1891
            CKL: CKL_1254(cca)
            SWO: Swol_1813
            CSC: Csac_2250
            TTE: TTE0109(pcnB)
            MAV: MAV_5294
            MSM: MSMEG_6926
            CJK: jk2088(cca)
            ART: Arth_4157
            NCA: Noca_4681
            FAL: FRAAL6862(cca)
            ACE: Acel_2139
            FNU: FN0243
            CTA: CTA_0445(pcnB_1) CTA_0765(pcnB_2)
            TPA: TP0270(pcnA)
            SYW: SYNW0188
            CYA: CYA_1032
            TEL: tlr0715
            AVA: Ava_3833
            PMA: Pro0164(pcnB)
            PMM: PMM0141
            PMT: PMT1910
            PMC: P9515_01691
            GFO: GFO_2283
            FPS: FP1644(cca)
            CCH: Cag_0722
            DRA: DR_0983 DR_1191
            TTH: TTC0479 TTC0556
            TTJ: TTHA0925
            TMA: TM0715
            MJA: MJ1111(cca)
            MMP: MMP0949
            MMQ: MmarC5_0756
            MAC: MA3559(cca)
            MBA: Mbar_A2014
            MMA: MM_0469
            MBU: Mbur_1130
            MTP: Mthe_0675
            MHU: Mhun_2808
            MEM: Memar_0323
            MBN: Mboo_1706
            MTH: MTH584
            MST: Msp_0086
            MSI: Msm_0053
            MKA: MK1100 MK1366(CCA1)
            AFU: AF0410 AF2156(cca)
            HAL: VNG0137G(cca)
            HMA: rrnAC2298(cca)
            HWA: HQ1438A(cca)
            NPH: NP0320A(cca)
            TAC: Ta1446
            TVO: TVN0117
            PTO: PTO0469 PTO0535
            PHO: PH0101
            PAB: PAB0063(cca)
            PFU: PF0026(cca)
            TKO: TK1741
            RCI: RCIX1175(cca)
            APE: APE_1791.1
            SMR: Smar_1232
            IHO: Igni_0849
            HBU: Hbut_0014
            SSO: SSO1039
            STO: ST0012 ST0952
            SAI: Saci_1288
            PAI: PAE3325
            PIS: Pisl_0570
            PCL: Pcal_1737
            PAS: Pars_1740
            TPE: Tpen_0368
            NEQ: NEQ152
STRUCTURES  PDB: 1R89  1R8A  1R8B  1R8C  1SZ1  1TFW  1TFY  1UET  1UEU  1UEV  
                 2DR5  2DR7  2DR8  2DR9  2DRA  2DRB  2DVI  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.25
            ExPASy - ENZYME nomenclature database: 2.7.7.25
            ExplorEnz - The Enzyme Database: 2.7.7.25
            ERGO genome analysis and discovery system: 2.7.7.25
            BRENDA, the Enzyme Database: 2.7.7.25
            CAS: 52523-59-8
///
ENTRY       EC 2.7.7.26       Obsolete  Enzyme
NAME        Transferred to 3.1.27.3
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
COMMENT     Transferred entry: now EC 3.1.27.3 ribonuclease T1 (EC 2.7.7.26
            created 1961 as EC 3.1.4.8, transferred 1965 to EC 2.7.7.26, deleted
            1972)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.26
            ExPASy - ENZYME nomenclature database: 2.7.7.26
            ExplorEnz - The Enzyme Database: 2.7.7.26
            ERGO genome analysis and discovery system: 2.7.7.26
            BRENDA, the Enzyme Database: 2.7.7.26
///
ENTRY       EC 2.7.7.27                 Enzyme
NAME        glucose-1-phosphate adenylyltransferase;
            ADP glucose pyrophosphorylase;
            glucose 1-phosphate adenylyltransferase;
            adenosine diphosphate glucose pyrophosphorylase;
            adenosine diphosphoglucose pyrophosphorylase;
            ADP-glucose pyrophosphorylase;
            ADP-glucose synthase;
            ADP-glucose synthetase;
            ADPG pyrophosphorylase;
            ADP:alpha-D-glucose-1-phosphate adenylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ATP:alpha-D-glucose-1-phosphate adenylyltransferase
REACTION    ATP + alpha-D-glucose 1-phosphate = diphosphate + ADP-glucose
            [RN:R00948]
ALL_REAC    R00948
SUBSTRATE   ATP [CPD:C00002];
            alpha-D-glucose 1-phosphate [CPD:C00103]
PRODUCT     diphosphate [CPD:C00013];
            ADP-glucose [CPD:C00498]
REFERENCE   1  [PMID:5922972]
  AUTHORS   Ghosh HP, Preiss J.
  TITLE     Adenosine diphosphate glucose pyrophosphorylase. A regulatory enzyme
            in the biosynthesis of starch in spinach leaf chloroplasts.
  JOURNAL   J. Biol. Chem. 241 (1966) 4491-504.
  ORGANISM  spinach
REFERENCE   2
  AUTHORS   Shen, L. and Preiss, J.
  TITLE     Biosynthesis of bacterial glycogen. I. Purification and properties
            of the adenosine diphosphoglucose pyrophosphorylase of Arthrobacter
            species NRRL B1973.
  JOURNAL   J. Biol. Chem. 240 (1965) 2334-2340.
  ORGANISM  Arthrobacter sp.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K00975  glucose-1-phosphate adenylyltransferase
GENES       ATH: AT1G05610(APS2) AT1G27680(APL2) AT4G39210(APL3)
                 AT5G19220(ADG2) AT5G48300(ADG1)
            OSA: 4334020 4342819 4345339 4346656
            TET: TTHERM_00656080
            ECO: b3430(glgC)
            ECJ: JW3393(glgC)
            ECE: Z4792(glgC)
            ECS: ECs4275
            ECC: c4217(glgC)
            ECI: UTI89_C3939(glgC)
            ECP: ECP_3524
            ECV: APECO1_3027(glgC)
            ECW: EcE24377A_3909(glgC)
            ECX: EcHS_A3630(glgC)
            STY: STY4274(glgC)
            STT: t3984(glgC)
            SPT: SPA3387(glgC)
            SEC: SC3466(glgC)
            STM: STM3536(glgC)
            YPE: YPO3940(glgC)
            YPK: y3888(glgC)
            YPM: YP_3302(glgC)
            YPA: YPA_3769
            YPN: YPN_3588
            YPS: YPTB3785(glgC)
            YPI: YpsIP31758_4004(glgC)
            YEN: YE2601(glgC2)
            SFL: SF3453(glgC)
            SFX: S4310(glgC)
            SFV: SFV_3439(glgC)
            SSN: SSON_3670(glgC)
            SBO: SBO_3428(glgC)
            SDY: SDY_3576(glgC)
            ECA: ECA4149(glgC)
            HIN: HI1359(glgC)
            HIT: NTHI1807(glgC)
            HIP: CGSHiEE_04325(glgC)
            HIQ: CGSHiGG_00450(glgC)
            HSO: HS_0887(glgC)
            PMU: PM0543(glgC)
            MSU: MS1121(glgC)
            APL: APL_0348(glgC)
            VCH: VC1727 VCA0699
            VCO: VC0395_0637(glgC-2) VC0395_A1330(glgC-1)
            VVU: VV1_2131 VV2_0214
            VVY: VV2313 VVA0721
            VPA: VP1023 VPA0833
            VFI: VFA0806(glgC)
            PPR: PBPRB0405
            SON: SO_1498(glgC)
            SFR: Sfri_2162
            SAZ: Sama_2450
            SBL: Sbal_1334
            SLO: Shew_1171
            SHE: Shewmr4_2755
            SHM: Shewmr7_2833
            SHN: Shewana3_2931
            SHW: Sputw3181_2853
            PAT: Patl_2932 Patl_3581
            SDE: Sde_0990
            PIN: Ping_0299 Ping_1296 Ping_3033 Ping_3034
            MAQ: Maqu_1433
            MCA: MCA1474(glgC)
            FTW: FTW_1658(glgC)
            FTL: FTL_0485
            FTH: FTH_0483(glgC)
            FTA: FTA_0511(glgC)
            FTN: FTN_0515(glgC)
            TCX: Tcr_0508
            NOC: Noc_0905
            AEH: Mlg_0655 Mlg_0959
            HHA: Hhal_1106
            AHA: AHA_2482(glgC-1) AHA_2740(glgC-2) AHA_3803(glgC-3)
            BXE: Bxe_A2934
            RFR: Rfer_0513
            PNA: Pnap_1106
            AAV: Aave_2982
            HAR: HEAR0727
            NEU: NE2030
            NET: Neut_1292
            NMU: Nmul_A0718
            EBA: ebA6921(glgC)
            AZO: azo1797(glgC)
            DAR: Daro_0585
            TBD: Tbd_1175 Tbd_2061
            MFA: Mfla_1368
            GME: Gmet_2768
            ADE: Adeh_0100
            MXA: MXAN_1524(glgC)
            SFU: Sfum_3485
            MLO: mlr7588
            SME: SMc03923(glgC)
            ATU: Atu4076(glgC)
            ATC: AGR_L_1560
            RET: RHE_CH03595(glgC)
            RLE: RL3983 RL4116(glgC)
            BJA: blr6458(glgC)
            BRA: BRADO6613(glgC)
            BBT: BBta_0922(glgC)
            RPA: RPA0381(glgC)
            RPB: RPB_0442
            RPC: RPC_0611
            RPD: RPD_0345
            RPE: RPE_0801
            RSP: RSP_2227(glgC) RSP_2886(glgC)
            RSH: Rsph17029_1532
            RSQ: Rsph17025_1134 Rsph17025_2266
            JAN: Jann_3114
            RDE: RD1_2874(glgC)
            PDE: Pden_4427
            ZMO: ZMO0153(yebC)
            NAR: Saro_1657
            GBE: GbCGDNIH1_2340
            ACR: Acry_0131
            RRU: Rru_A2246
            MAG: amb2110
            MGM: Mmc1_1522
            ABA: Acid345_1020
            SUS: Acid_1105
            BSU: BG10908(glgC) BG10909(glgD)
            BHA: BH1086(glgD) BH1087(glgC)
            BAN: BA5121(glgD) BA5122(glgC)
            BAR: GBAA5121(glgD) GBAA5122(glgC)
            BAA: BA_5540 BA_5541
            BAT: BAS4759(glgD) BAS4760
            BCE: BC4866(glgC)
            BCA: BCE_5026(glgD) BCE_5027(glgC)
            BCZ: BCZK4619(glgD) BCZK4620(glgC)
            BCY: Bcer98_3502
            BTK: BT9727_4597(glgD) BT9727_4598(glgC)
            BTL: BALH_4430(glgD) BALH_4431(glgC)
            BLI: BL01417(glgD) BL01418(glgC)
            BLD: BLi03228(glgD) BLi03229(glgC)
            OIH: OB0407(glgC) OB0408
            LLA: L95975(glgC) L97131(glgD)
            LLC: LACR_0724
            LLM: llmg_1873(glgD) llmg_1874(glgC)
            SPN: SP_1122 SP_1123
            SPR: spr1030(glgC) spr1031(glgD)
            SPD: SPD_1006(glgC) SPD_1007(glgD)
            SAG: SAG0854(glgC)
            SAN: gbs0872 gbs0873
            SAK: SAK_0977(glgC) SAK_0978(glgD)
            SMU: SMU.1537(glgD) SMU.1538(glgC)
            SSA: SSA_0776(glgC) SSA_0777(glgD)
            SGO: SGO_1552(glgD) SGO_1553(glgC)
            LPL: lp_0021(glgC) lp_0022(glgD)
            LAC: LBA0681(glgC) LBA0682(glgD)
            LSL: LSL_1292(glgC) LSL_1293(glgC)
            LCA: LSEI_2038 LSEI_2039
            CAC: CAC2237(glgC) CAC2238(glgC)
            CPE: CPE0068(glgC) CPE0069(glgD)
            CPR: CPR_0086(glgC) CPR_0087(glgD)
            CTC: CTC02215
            CNO: NT01CX_0723(glgC) NT01CX_0724(glgD)
            CTH: Cthe_3167
            CDF: CD0882(glgC)
            CBE: Cbei_4904
            CKL: CKL_3494(glgC)
            AMT: Amet_2947
            DSY: DSY2037 DSY2038
            DRM: Dred_1456
            CSC: Csac_0782
            MMO: MMOB3980(glgC) MMOB3990(glgC)
            MTU: Rv1213(glgC)
            MTC: MT1251(glgC)
            MBO: Mb1245(glgC)
            MBB: BCG_1273(glgC)
            MLE: ML1069(glgC)
            MPA: MAP2564c(glgC)
            MAV: MAV_1358(glgC)
            MSM: MSMEG_5078(glgC)
            MMC: Mmcs_4000
            CGL: NCgl1073(glgC)
            CGB: cg1269(glgC)
            CEF: CE1175
            CDI: DIP0992(glgC)
            CJK: jk1383(glgC)
            NFA: nfa47260(glgC)
            RHA: RHA1_ro05975(glgC)
            SCO: SCO0961(glgC)
            SMA: SAV7254(glgC)
            LXX: Lxx11760(glgC)
            CMI: CMM_1719(glgC)
            ART: Arth_2140
            AAU: AAur_2136(glgC)
            PAC: PPA0640(glgC)
            NCA: Noca_3717
            FRA: Francci3_1667
            FAL: FRAAL4553(glgC)
            ACE: Acel_1821
            BLO: BL0866(glgC)
            BAD: BAD_0716(glgC)
            FNU: FN0854 FN0855(glgC)
            RBA: RB10465(glgC) RB1358(glgC)
            CTR: CT489(glgC)
            CTA: CTA_0536(glgC)
            CMU: TC0776
            CPN: CPn0607(glgC)
            CPA: CP0140
            CPJ: CPj0607(glgC)
            CPT: CpB0631
            CCA: CCA00133(glgC)
            CAB: CAB132(glgC)
            CFE: CF0873(glgC)
            PCU: pc0109(glgC)
            TDE: TDE2035(glgC)
            SYN: slr1176(glgC)
            SYW: SYNW1118(glgC)
            SYC: syc0921_d(glgC)
            SYF: Synpcc7942_0603
            SYD: Syncc9605_1255(glgC)
            SYE: Syncc9902_1227(glgC)
            SYG: sync_1687(glgC)
            SYR: SynRCC307_1253(glgC)
            SYX: SynWH7803_1298(glgC)
            CYA: CYA_1562(glgC)
            CYB: CYB_1067(glgC)
            TEL: tlr1287
            GVI: gll4260
            ANA: all4645(agp)
            AVA: Ava_2020(glgC)
            PMA: Pro0842(glgC)
            PMM: PMM0769(glgC)
            PMT: PMT0566(glgC)
            PMN: PMN2A_0175(glgC)
            PMI: PMT9312_0777
            PMB: A9601_08311(glgC)
            PMC: P9515_08141(glgC)
            PMF: P9303_05381 P9303_16851(glgC)
            PMG: P9301_08291(glgC)
            PMH: P9215_08631(glgC)
            PME: NATL1_08071(glgC)
            TER: Tery_4395
            SRU: SRU_1929
            DRA: DR_1689 DR_1824
            DGE: Dgeo_0861
            TTH: TTC1976 TTC1977
            TTJ: TTHA0022
            TMA: TM0239 TM0240
STRUCTURES  PDB: 1YP2  1YP3  1YP4  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.27
            ExPASy - ENZYME nomenclature database: 2.7.7.27
            ExplorEnz - The Enzyme Database: 2.7.7.27
            ERGO genome analysis and discovery system: 2.7.7.27
            BRENDA, the Enzyme Database: 2.7.7.27
            CAS: 9027-71-8
///
ENTRY       EC 2.7.7.28                 Enzyme
NAME        nucleoside-triphosphate-aldose-1-phosphate nucleotidyltransferase;
            NDP hexose pyrophosphorylase;
            hexose 1-phosphate nucleotidyltransferase;
            hexose nucleotidylating enzyme;
            nucleoside diphosphohexose pyrophosphorylase;
            hexose-1-phosphate guanylyltransferase;
            GTP:alpha-D-hexose-1-phosphate guanylyltransferase;
            GDP hexose pyrophosphorylase;
            guanosine diphosphohexose pyrophosphorylase;
            nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase;
            NTP:hexose-1-phosphate nucleotidyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     NTP:alpha-D-aldose-1-phosphate nucleotidyltransferase
REACTION    nucleoside triphosphate + alpha-D-aldose 1-phosphate = diphosphate +
            NDP-hexose
ALL_REAC    (other) R03149 R03318
SUBSTRATE   nucleoside triphosphate [CPD:C00201];
            alpha-D-aldose 1-phosphate [CPD:C00991]
PRODUCT     diphosphate [CPD:C00013];
            NDP-hexose [CPD:C01600]
COMMENT     In decreasing order of activity, guanosine, inosine and adenosine
            diphosphate hexoses are substrates in the reverse reaction, with
            either glucose or mannose as the sugar.
REFERENCE   1  [PMID:5946626]
  AUTHORS   Verachtert H, Rodriguez P, Bass ST, Hansen RG.
  TITLE     Purification and properties of guanosine diphosphate hexose
            pyrophosphorylase from mammalian tissues.
  JOURNAL   J. Biol. Chem. 241 (1966) 2007-13.
  ORGANISM  cow [GN:bta], rat [GN:rno]
REFERENCE   2
  AUTHORS   Hansen, R.G., Verachtert, H., Rodriguez, P. and Bass, S.T.
  TITLE     GDP-hexose pyrophosphorylase from liver.
  JOURNAL   Methods Enzymol. 8 (1966) 269-271.
  ORGANISM  cow [GN:bta]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.28
            ExPASy - ENZYME nomenclature database: 2.7.7.28
            ExplorEnz - The Enzyme Database: 2.7.7.28
            ERGO genome analysis and discovery system: 2.7.7.28
            BRENDA, the Enzyme Database: 2.7.7.28
            CAS: 37278-26-5
///
ENTRY       EC 2.7.7.29       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
COMMENT     Deleted entry: hexose-1-phosphate guanylyltransferase. Enzyme is not
            specific for GTP and therefore is identical to EC 2.7.7.28,
            nucleoside-triphosphate-aldose-1-phosphate nucleotidyltransferase
            (EC 2.7.7.29 created 1972, deleted 2004)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.29
            ExPASy - ENZYME nomenclature database: 2.7.7.29
            ExplorEnz - The Enzyme Database: 2.7.7.29
            ERGO genome analysis and discovery system: 2.7.7.29
            BRENDA, the Enzyme Database: 2.7.7.29
///
ENTRY       EC 2.7.7.30                 Enzyme
NAME        fucose-1-phosphate guanylyltransferase;
            GDP fucose pyrophosphorylase;
            guanosine diphosphate L-fucose pyrophosphorylase;
            GDP-L-fucose pyrophosphorylase;
            GDP-fucose pyrophosphorylase;
            GTP:L-fucose-1-phosphate guanylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     GTP:beta-L-fucose-1-phosphate guanylyltransferase
REACTION    GTP + beta-L-fucose 1-phosphate = diphosphate + GDP-L-fucose
            [RN:R01951]
ALL_REAC    R01951
SUBSTRATE   GTP [CPD:C00044];
            beta-L-fucose 1-phosphate [CPD:C02985]
PRODUCT     diphosphate [CPD:C00013];
            GDP-L-fucose [CPD:C00325]
REFERENCE   1  [PMID:5646162]
  AUTHORS   Ishihara H, Heath EC.
  TITLE     The metabolism of L-fucose. IV. The biosynthesis of guanosine
            diphosphate L-fucose in porcine liver.
  JOURNAL   J. Biol. Chem. 243 (1968) 1110-5.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K00976  fucose-1-phosphate guanylyltransferase
GENES       HSA: 8790(FPGT)
            MMU: 75540(Fpgt)
            RNO: 310935(Fpgt)
            SPU: 757180(LOC757180)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.30
            ExPASy - ENZYME nomenclature database: 2.7.7.30
            ExplorEnz - The Enzyme Database: 2.7.7.30
            ERGO genome analysis and discovery system: 2.7.7.30
            BRENDA, the Enzyme Database: 2.7.7.30
            CAS: 9033-14-1
///
ENTRY       EC 2.7.7.31                 Enzyme
NAME        DNA nucleotidylexotransferase;
            terminal deoxyribonucleotidyltransferase;
            terminal addition enzyme;
            addase;
            deoxynucleotidyl terminal transferase;
            deoxyribonucleic acid nucleotidyltransferase;
            deoxyribonucleic nucleotidyltransferase;
            terminal deoxynucleotide transferase;
            TdT
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     nucleoside-triphosphate:DNA deoxynucleotidylexotransferase
REACTION    deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1
            [RN:R00379]
ALL_REAC    R00379
SUBSTRATE   deoxynucleoside triphosphate [CPD:C00677];
            DNAn [CPD:C00039]
PRODUCT     diphosphate [CPD:C00013];
            DNAn+1 [CPD:C00039]
COMMENT     Catalyses template-independent extension of the 3'- end of a DNA
            strand by one nucleotide at a time. Cannot initiate a chain de novo.
            Nucleoside may be ribo- or deoxyribo-.
REFERENCE   1  [PMID:5543689]
  AUTHORS   Chang LM, Bollum FJ.
  TITLE     Deoxynucleotide-polymerizing enzymes of calf thymus gland. V.
            Homogeneous terminal deoxynucleotidyl transferase.
  JOURNAL   J. Biol. Chem. 246 (1971) 909-16.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:4288534]
  AUTHORS   Gottesman ME, Canellakis ES.
  TITLE     The terminal nucleotidyltransferases of calf thymus nuclei.
  JOURNAL   J. Biol. Chem. 241 (1966) 4339-52.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:14459258]
  AUTHORS   KRAKOW JS, COUTSOGEORGOPOULOS C, CANELLAKIS ES.
  TITLE     Studies on the incorporation of deoxyribonucleic acid.
  JOURNAL   Biochim. Biophys. Acta. 55 (1962) 639-50.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map04640  Hematopoietic cell lineage
ORTHOLOGY   KO: K00977  DNA nucleotidylexotransferase
GENES       HSA: 1791(DNTT)
            PTR: 466167(DNTT)
            RNO: 294051(Dntt)
            CFA: 486815(DNTT)
            BTA: 281120(DNTT)
            MDO: 554183(DNTT)
            GGA: 396351(DNTT)
            TET: TTHERM_00732550
STRUCTURES  PDB: 1JMS  1KDH  1KEJ  2COE  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.31
            ExPASy - ENZYME nomenclature database: 2.7.7.31
            ExplorEnz - The Enzyme Database: 2.7.7.31
            ERGO genome analysis and discovery system: 2.7.7.31
            BRENDA, the Enzyme Database: 2.7.7.31
            CAS: 9027-67-2
///
ENTRY       EC 2.7.7.32                 Enzyme
NAME        galactose-1-phosphate thymidylyltransferase;
            dTDP galactose pyrophosphorylase;
            galactose 1-phosphate thymidylyl transferase;
            thymidine diphosphogalactose pyrophosphorylase;
            thymidine triphosphate:alpha-D-galactose 1-phosphate
            thymidylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     dTTP:alpha-D-galactose-1-phosphate thymidylyltransferase
REACTION    dTTP + alpha-D-galactose 1-phosphate = diphosphate + dTDP-galactose
            [RN:R02329]
ALL_REAC    R02329
SUBSTRATE   dTTP [CPD:C00459];
            alpha-D-galactose 1-phosphate [CPD:C00446]
PRODUCT     diphosphate [CPD:C00013];
            dTDP-galactose [CPD:C02097]
REFERENCE   1
  AUTHORS   Pazur, J.H. and Anderson, J.S.
  TITLE     Thymidine triphosphate: alpha-D-galactose 1-phosphate
            thymidylyltransferase from Streptococcus faecalis grown on
            D-galactose.
  JOURNAL   J. Biol. Chem. 238 (1963) 3155-3160.
  ORGANISM  Streptococcus faecalis
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.32
            ExPASy - ENZYME nomenclature database: 2.7.7.32
            ExplorEnz - The Enzyme Database: 2.7.7.32
            ERGO genome analysis and discovery system: 2.7.7.32
            BRENDA, the Enzyme Database: 2.7.7.32
            CAS: 9023-25-0
///
ENTRY       EC 2.7.7.33                 Enzyme
NAME        glucose-1-phosphate cytidylyltransferase;
            CDP glucose pyrophosphorylase;
            cytidine diphosphoglucose pyrophosphorylase;
            cytidine diphosphate glucose pyrophosphorylase;
            cytidine diphosphate-D-glucose pyrophosphorylase;
            CTP:D-glucose-1-phosphate cytidylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     CTP:alpha-D-glucose-1-phosphate cytidylyltransferase
REACTION    CTP + alpha-D-glucose 1-phosphate = diphosphate + CDP-glucose
            [RN:R00956]
ALL_REAC    R00956;
            (other) R02328
SUBSTRATE   CTP [CPD:C00063];
            alpha-D-glucose 1-phosphate [CPD:C00103]
PRODUCT     diphosphate [CPD:C00013];
            CDP-glucose [CPD:C00501]
REFERENCE   1  [PMID:14299608]
  AUTHORS   MAYER RM, GINSBURG V.
  TITLE     PURIFICATION AND PROPERTIES OF CYTIDINE DIPHOSPHATE D-GLUCOSE
            PYROPHOSPHORYLASE FROM SALMONELLA PARATYPHI A.
  JOURNAL   J. Biol. Chem. 240 (1965) 1900-4.
  ORGANISM  Salmonella paratyphi
PATHWAY     PATH: map00500  Starch and sucrose metabolism
            PATH: map00520  Nucleotide sugars metabolism
ORTHOLOGY   KO: K00978  glucose-1-phosphate cytidylyltransferase
GENES       STY: STY2302(rfbF)
            STT: t0780(rfbF)
            SPT: SPA0774(rfbF)
            STM: STM2092(rfbF)
            YPE: YPO3115(ddhA)
            YPK: y1068
            YPM: YP_0815(ddhA)
            YPA: YPA_2608
            YPN: YPN_0974
            YPS: YPTB0999(ddhA)
            YPI: YpsIP31758_3051(ddhA)
            ECA: ECA1422(rfbF)
            XCC: XCC2015
            XCB: XC_2169
            VFI: VF0182
            PSP: PSPPH_0961
            PFL: PFL_5094(rfbF)
            PFO: Pfl_1510
            SDN: Sden_2657
            PAT: Patl_3063
            TCX: Tcr_1690
            AHA: AHA_4166(rfbF)
            CVI: CV_3893(ddhA)
            REH: H16_A2893(rfbF)
            BPS: BPSS0419(rfbF)
            BPM: BURPS1710b_A1961(rfbF)
            BPL: BURPS1106A_A0568(rfbF)
            BPD: BURPS668_A0662(rfbF)
            BTE: BTH_II1984(rfbF)
            RFR: Rfer_1250
            POL: Bpro_4009
            HAR: HEAR1136(rfbF)
            DAR: Daro_1256
            TBD: Tbd_1881
            SUN: SUN_2137
            PCA: Pcar_1132
            DVU: DVU0072
            DDE: Dde_3694
            SAT: SYN_02649
            SME: SMb21058 SMb21059 SMb21416(ddhA)
            ATU: Atu4797(rfbF)
            ATC: AGR_L_170
            RLE: RL0246(ddhA)
            BME: BMEII0827
            BMS: BRA0439
            OAN: Oant_3391
            BJA: bll5980
            BBT: BBta_1052
            RPA: RPA4048(rfbF)
            RPE: RPE_4253
            RSP: RSP_1538
            BSU: BG12979(yfnH)
            BCE: BC3358 BC3514
            BCA: BCE_3395
            BCZ: BCZK3069(rfbF)
            BAY: RBAM_007520(yfnH)
            BPU: BPUM_0676(yfnH)
            CBO: CBO2718
            CBA: CLB_2659
            CBH: CLC_2592
            RHA: RHA1_ro05747
            SCO: SCO0393(SCF62.19)
            FRA: Francci3_1563 Francci3_3930
            FAL: FRAAL6241
            LIL: LA1631(rfbF1)
            LIC: LIC12152
            SYN: slr0983(rfbF)
            SYC: syc1440_d(rfbF)
            SYF: Synpcc7942_0062
            GVI: gll2185 gll2208(rfbF)
            ANA: alr2825
            AVA: Ava_1106
            PMM: PMM1204(ddhA)
            PMB: A9601_14071
            PMC: P9515_07601
            PMF: P9303_01391
            TER: Tery_2260
            BTH: BT_1351
            BFR: BF1534
            BFS: BF2603
STRUCTURES  PDB: 1TZF  1WVC  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.33
            ExPASy - ENZYME nomenclature database: 2.7.7.33
            ExplorEnz - The Enzyme Database: 2.7.7.33
            ERGO genome analysis and discovery system: 2.7.7.33
            BRENDA, the Enzyme Database: 2.7.7.33
            CAS: 9027-10-5
///
ENTRY       EC 2.7.7.34                 Enzyme
NAME        glucose-1-phosphate guanylyltransferase;
            GDP glucose pyrophosphorylase;
            guanosine diphosphoglucose pyrophosphorylase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     GTP:alpha-D-glucose-1-phosphate guanylyltransferase
REACTION    GTP + alpha-D-glucose 1-phosphate = diphosphate + GDP-glucose
            [RN:R00954]
ALL_REAC    R00954
SUBSTRATE   GTP [CPD:C00044];
            alpha-D-glucose 1-phosphate [CPD:C00103]
PRODUCT     diphosphate [CPD:C00013];
            GDP-glucose [CPD:C00394]
COMMENT     Also acts, more slowly, on D-mannose 1-phosphate.
REFERENCE   1  [PMID:6034677]
  AUTHORS   Danishefsky I, Heritier-Watkins O.
  TITLE     Nucleoside diphosphate glucose pyrophosphorylases in mast cell
            tumors.
  JOURNAL   Biochim. Biophys. Acta. 139 (1967) 349-57.
  ORGANISM  Eremothecium ashbyii, mammalian
PATHWAY     PATH: map00500  Starch and sucrose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.34
            ExPASy - ENZYME nomenclature database: 2.7.7.34
            ExplorEnz - The Enzyme Database: 2.7.7.34
            ERGO genome analysis and discovery system: 2.7.7.34
            BRENDA, the Enzyme Database: 2.7.7.34
            CAS: 9033-13-0
///
ENTRY       EC 2.7.7.35                 Enzyme
NAME        ribose-5-phosphate adenylyltransferase;
            ADP ribose phosphorylase;
            adenosine diphosphoribose phosphorylase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ADP:D-ribose-5-phosphate adenylyltransferase
REACTION    ADP + D-ribose 5-phosphate = phosphate + ADP-ribose [RN:R01052]
ALL_REAC    R01052
SUBSTRATE   ADP [CPD:C00008];
            D-ribose 5-phosphate [CPD:C00117]
PRODUCT     phosphate [CPD:C00009];
            ADP-ribose [CPD:C00301]
REFERENCE   1  [PMID:4287446]
  AUTHORS   Evans WR, San Pietro A.
  TITLE     Phosphorolysis of adenosine diphosphoribose.
  JOURNAL   Arch. Biochem. Biophys. 113 (1966) 236-44.
  ORGANISM  Euglena gracilis
REFERENCE   2  [PMID:5970863]
  AUTHORS   Stern AI, Avron M.
  TITLE     An adenosine 5'-diphosphate ribose:orthophosphate
            adenylyltransferase from Euglena gracilis.
  JOURNAL   Biochim. Biophys. Acta. 118 (1966) 577-91.
  ORGANISM  Euglena gracilis
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.35
            ExPASy - ENZYME nomenclature database: 2.7.7.35
            ExplorEnz - The Enzyme Database: 2.7.7.35
            ERGO genome analysis and discovery system: 2.7.7.35
            BRENDA, the Enzyme Database: 2.7.7.35
            CAS: 9054-55-1
///
ENTRY       EC 2.7.7.36                 Enzyme
NAME        aldose-1-phosphate adenylyltransferase;
            sugar-1-phosphate adenylyltransferase;
            ADPaldose phosphorylase;
            adenosine diphosphosugar phosphorylase;
            ADP sugar phosphorylase;
            adenosine diphosphate glucose:orthophosphate adenylyltransferase;
            ADP:aldose-1-phosphate adenylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ADP:alpha-D-aldose-1-phosphate adenylyltransferase
REACTION    ADP + alpha-D-aldose 1-phosphate = phosphate + ADP-aldose
            [RN:R03142]
ALL_REAC    R03142
SUBSTRATE   ADP [CPD:C00008];
            alpha-D-aldose 1-phosphate [CPD:C00991]
PRODUCT     phosphate [CPD:C00009];
            ADP-aldose [CPD:C01547]
REFERENCE   1
  AUTHORS   Dankert, M., Goncalves, I.R.J. and Recondo, E.
  TITLE     Adenosine diphosphate glucose: orthophosphate adenylyltransferase in
            wheat germ.
  JOURNAL   Biochim. Biophys. Acta 81 (1964) 78-85.
  ORGANISM  Triticum aestivum [GN:etae]
REFERENCE   2
  AUTHORS   Passeron, S., Recondo, E. and Dankert, M.
  TITLE     Biosynthesis of adenosine diphosphate D-hexoses.
  JOURNAL   Biochim. Biophys. Acta 89 (1964) 372-374.
  ORGANISM  Zea mays [GN:ezma]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.36
            ExPASy - ENZYME nomenclature database: 2.7.7.36
            ExplorEnz - The Enzyme Database: 2.7.7.36
            ERGO genome analysis and discovery system: 2.7.7.36
            BRENDA, the Enzyme Database: 2.7.7.36
            CAS: 37278-27-6
///
ENTRY       EC 2.7.7.37                 Enzyme
NAME        aldose-1-phosphate nucleotidyltransferase;
            sugar-1-phosphate nucleotidyltransferase;
            NDPaldose phosphorylase;
            glucose 1-phosphate inosityltransferase;
            NDP sugar phosphorylase;
            nucleoside diphosphosugar phosphorylase;
            sugar phosphate nucleotidyltransferase;
            nucleoside diphosphate sugar:orthophosphate nucleotidyltransferase;
            sugar nucleotide phosphorylase;
            NDP:aldose-1-phosphate nucleotidyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     NDP:alpha-D-aldose-1-phosphate nucleotidyltransferase
REACTION    NDP + alpha-D-aldose 1-phosphate = phosphate + NDP-aldose
            [RN:R03143]
ALL_REAC    R03143;
            (other) R03077
SUBSTRATE   NDP [CPD:C00454];
            alpha-D-aldose 1-phosphate [CPD:C00991]
PRODUCT     phosphate [CPD:C00009];
            NDP-aldose [CPD:C01599]
COMMENT     The enzyme works on a variety of alpha-D-aldose 1-phosphates and
            beta-L-aldose 1-phosphates (which have the same anomeric
            configuration as the former; see 2-Carb-6.2).
REFERENCE   1  [PMID:14299635]
  AUTHORS   CABIB E, CARMINATTI H, WOYSKOVSKY NM.
  TITLE     PHOSPHOROLYSIS OF THE PYROPHOSPHATE BOND OF SUGAR NUCLEOTIDES. II.
            PURIFICATION AND PROPERTIES OF THE ENZYME.
  JOURNAL   J. Biol. Chem. 240 (1965) 2114-21.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.37
            ExPASy - ENZYME nomenclature database: 2.7.7.37
            ExplorEnz - The Enzyme Database: 2.7.7.37
            ERGO genome analysis and discovery system: 2.7.7.37
            BRENDA, the Enzyme Database: 2.7.7.37
            CAS: 9033-61-8
///
ENTRY       EC 2.7.7.38                 Enzyme
NAME        3-deoxy-manno-octulosonate cytidylyltransferase;
            CMP-3-deoxy-D-manno-octulosonate pyrophosphorylase;
            2-keto-3-deoxyoctonate cytidylyltransferase;
            3-Deoxy-D-manno-octulosonate cytidylyltransferase;
            CMP-3-deoxy-D-manno-octulosonate synthetase;
            CMP-KDO synthetase;
            CTP:CMP-3-deoxy-D-manno-octulosonate cytidylyltransferase;
            cytidine monophospho-3-deoxy-D-manno-octulosonate pyrophosphorylase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     CTP:3-deoxy-D-manno-octulosonate cytidylyltransferase
REACTION    CTP + 3-deoxy-D-manno-octulosonate = diphosphate +
            CMP-3-deoxy-D-manno-octulosonate [RN:R03351]
ALL_REAC    R03351
SUBSTRATE   CTP [CPD:C00063];
            3-deoxy-D-manno-octulosonate [CPD:C01187]
PRODUCT     diphosphate [CPD:C00013];
            CMP-3-deoxy-D-manno-octulosonate [CPD:C04121]
REFERENCE   1  [PMID:5330266]
  AUTHORS   Ghalambor MA, Heath EC.
  TITLE     The biosynthesis of cell wall lipopolysaccharide in Escherichia
            coli. IV. Purification and properties of cytidine monophosphate
            3-deoxy-d-manno-octulosonate synthetase.
  JOURNAL   J. Biol. Chem. 241 (1966) 3216-21.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00540  Lipopolysaccharide biosynthesis
ORTHOLOGY   KO: K00979  3-deoxy-manno-octulosonate cytidylyltransferase (CMP-KDO
                        synthetase)
GENES       ATH: AT1G53000
            OSA: 4339603
            ECO: b0918(kdsB)
            ECJ: JW0901(kdsB)
            ECE: Z1264(kdsB)
            ECS: ECs1001
            ECC: c1059(kdsB) c3689
            ECI: UTI89_C0989(kdsB) UTI89_C3365(kpsU)
            ECP: ECP_0929 ECP_3023
            ECV: APECO1_30(kdsB) APECO1_3479(kpsU)
            ECW: EcE24377A_1016(kdsB)
            ECX: EcHS_A1025(kdsB)
            STY: STY0990(kdsB)
            STT: t1946(kdsB)
            SPT: SPA1810(kdsB)
            SEC: SC0945(kdsB)
            STM: STM0988(kdsB)
            YPE: YPO1400(kdsB)
            YPK: y2772(kdsB)
            YPM: YP_1193(kdsB)
            YPA: YPA_0694
            YPN: YPN_2577
            YPP: YPDSF_2295
            YPS: YPTB1425(kdsB)
            YPI: YpsIP31758_2571(kdsB)
            YEN: YE1550(kdsB)
            SFL: SF0914(kdsB)
            SFX: S0978(kdsB)
            SFV: SFV_0919(kdsB)
            SSN: SSON_0920(kdsB)
            SBO: SBO_2206(kdsB)
            SDY: SDY_2340(kdsB)
            ECA: ECA2554(kdsB)
            PLU: plu1634(kdsB)
            WBR: WGLp251(kdsB)
            SGL: SG0998
            ENT: Ent638_1437
            KPN: KPN_00945(kdsB)
            BFL: Bfl376(kdsB)
            BPN: BPEN_387(kdsB)
            HIN: HI0058(kdsB)
            HIT: NTHI0068(kdsB)
            HIP: CGSHiEE_03010
            HIQ: CGSHiGG_02800
            HDU: HD0334(kdsB)
            HSO: HS_0658(kdsB)
            PMU: PM0858(kdsB)
            MSU: MS0935(kdsB)
            APL: APL_0085(kdsB) APL_1577(kdsB)
            ASU: Asuc_1726
            XFA: XF2299
            XFT: PD1337(kdsB)
            XCC: XCC2118(kdsB)
            XCB: XC_1997
            XCV: XCV2003(kdsB1) XCV2256(kdsB2)
            XAC: XAC2089(kdsB)
            XOO: XOO2295(kdsB)
            XOM: XOO_2173(XOO2173)
            VCH: VC1875
            VCO: VC0395_A1466(kdsB)
            VVU: VV1_2088
            VVY: VV2353
            VPA: VP0984
            VFI: VF0178 VFA0427
            PPR: PBPRA2382(kdsB)
            PAE: PA2979(kdsB)
            PAU: PA14_25530(kdsB)
            PAP: PSPA7_2182(kdsB)
            PPU: PP_1902(kdsB)
            PPF: Pput_3812 Pput_3909
            PST: PSPTO_3843(kdsB)
            PSB: Psyr_1636
            PSP: PSPPH_0533(kdtA) PSPPH_1630(kdsB)
            PFL: PFL_1780(kdsB)
            PFO: Pfl_4173
            PEN: PSEEN1605(kdsB)
            PMY: Pmen_1616
            PAR: Psyc_1314(kdsB)
            PCR: Pcryo_1064
            PRW: PsycPRwf_1393
            ACI: ACIAD2362(kdsB)
            SON: SO_2478(kdsB)
            SDN: Sden_2134 Sden_2666
            SFR: Sfri_1759
            SAZ: Sama_1639
            SBL: Sbal_2375
            SLO: Shew_1856
            SPC: Sputcn32_2127
            SHE: Shewmr4_1851
            SHM: Shewmr7_2127
            SHN: Shewana3_1906
            SHW: Sputw3181_1884
            ILO: IL1510(kdsB)
            CPS: CPS_2128(kdsB)
            PHA: PSHAa1658(kdsB)
            PAT: Patl_1783
            SDE: Sde_2058
            PIN: Ping_0903
            MAQ: Maqu_1738
            CBU: CBU_0479(kdsB)
            CBD: COXBU7E912_1596(kdsB)
            LPN: lpg1919(kdsB)
            LPF: lpl1883(kdsB)
            LPP: lpp1894(kdsB)
            MCA: MCA0635(kdsB)
            FTU: FTT1478c(kdsB)
            FTF: FTF1478c(kdsB)
            FTW: FTW_0620(kdsB)
            FTL: FTL_1399
            FTH: FTH_1361(kdsB)
            FTA: FTA_1486(kdsB)
            FTN: FTN_0683(kdsB)
            TCX: Tcr_0960 Tcr_2141
            NOC: Noc_2840
            AEH: Mlg_1433
            HHA: Hhal_1244
            HCH: HCH_02706(kdsB)
            CSA: Csal_1589
            ABO: ABO_1057(kdsB)
            MMW: Mmwyl1_1126
            AHA: AHA_2775(kdsB)
            DNO: DNO_0304(kdsB)
            RMA: Rmag_0841
            VOK: COSY_0766(kdsB)
            NME: NMB0675
            NMA: NMA0875(kdsB)
            NMC: NMC0624(kdsB)
            NGO: NGO0245
            CVI: CV_3344(kdsB)
            RSO: RSc2532(kdsB)
            REU: Reut_A0591
            REH: H16_A0604(kdsB)
            RME: Rmet_0533 Rmet_5734
            BMA: BMA2275(kdsB)
            BMV: BMASAVP1_A0571(kdsB)
            BML: BMA10299_A1048(kdsB)
            BMN: BMA10247_2153(kdsB)
            BXE: Bxe_A0764
            BVI: Bcep1808_2640
            BUR: Bcep18194_A5878 Bcep18194_C7390
            BCN: Bcen_1935
            BCH: Bcen2424_2547
            BAM: Bamb_2595 Bamb_6184
            BPS: BPSL0876(kdsB)
            BPM: BURPS1710b_1081(kdsB)
            BPL: BURPS1106A_0928(kdsB)
            BPD: BURPS668_0925(kdsB)
            BTE: BTH_I0740(kdsB)
            PNU: Pnuc_0282
            BPE: BP2768
            BPA: BPP2561
            BBR: BB2006
            RFR: Rfer_1242 Rfer_3157
            POL: Bpro_2951
            PNA: Pnap_1921
            AAV: Aave_2562
            AJS: Ajs_2307
            VEI: Veis_4894
            MPT: Mpe_A2487
            HAR: HEAR1123 HEAR2488(kdsB)
            MMS: mma_2577(kdsB)
            NEU: NE1686
            NET: Neut_0435
            NMU: Nmul_A0430
            EBA: ebA5086(kdsB)
            AZO: azo1472(kdsB)
            DAR: Daro_3206
            TBD: Tbd_1505
            MFA: Mfla_2087
            HPY: HP0230
            HPA: HPAG1_0233
            HHE: HH0168(kdsB)
            HAC: Hac_0307(kdsB)
            WSU: WS1917(kdsB)
            TDN: Tmden_0727
            CJE: Cj0813(kdsB)
            CJR: CJE0904(kdsB)
            CJJ: CJJ81176_0834(kdsB)
            CJU: C8J_0764(kdsB)
            CJD: JJD26997_1197(kdsB)
            CFF: CFF8240_1083(kdsB)
            CCV: CCV52592_0131(kdsB)
            CHA: CHAB381_1019(kdsB)
            CCO: CCC13826_2053(kdsB)
            ABU: Abu_1272(kdsB)
            NIS: NIS_0993(kdsB)
            SUN: SUN_1670(kdsB)
            GSU: GSU1896(kdsB)
            GME: Gmet_1275
            GUR: Gura_2980
            PCA: Pcar_1946
            PPD: Ppro_1613
            DVU: DVU0341 DVU3114(kdsB)
            DVL: Dvul_0267 Dvul_2642
            DDE: Dde_3647 Dde_3687
            LIP: LI0989
            BBA: Bd0807(cks)
            ADE: Adeh_4175
            AFW: Anae109_4319
            MXA: MXAN_1100(kdsB) MXAN_4714(kdtA)
            SAT: SYN_02057
            SFU: Sfum_0010
            RPR: RP379
            RTY: RT0368(kdsB)
            RCO: RC0524(kdsB)
            RFE: RF_0594(kdsB)
            RBE: RBE_0988(kdsB)
            RAK: A1C_02855
            RBO: A1I_03715
            RRI: A1G_02975
            PUB: SAR11_0505(kdsB)
            MLO: mlr5497
            MES: Meso_4086
            PLA: Plav_0251
            SME: SMc02898(kdsB)
            SMD: Smed_3427
            ATU: Atu0100(kdsB)
            ATC: AGR_C_152
            RET: RHE_CH00132(kdsB1)
            RLE: RL0140(kdsB)
            BME: BMEI1904
            BMF: BAB1_0035
            BMS: BR0038(kdsB)
            BMB: BruAb1_0038(kdsB)
            BOV: BOV_0038(kdsB)
            OAN: Oant_0017
            BJA: bll1422(kdsB)
            BRA: BRADO1000(kdsB)
            BBT: BBta_7057(kdsB)
            RPA: RPA3694(kdsB)
            RPB: RPB_1768
            RPC: RPC_3731
            RPD: RPD_3537
            RPE: RPE_3769
            NWI: Nwi_0286
            NHA: Nham_0376
            BHE: BH02360(kdsB)
            BQU: BQ02230(kdsB)
            BBK: BARBAKC583_1204(kdtA) BARBAKC583_1236(kdsB)
            XAU: Xaut_2630
            CCR: CC_2934
            SIL: SPO0038(kdsB)
            SIT: TM1040_0014
            RSP: RSP_1160(kdsB)
            RSH: Rsph17029_2821
            RSQ: Rsph17025_2752
            JAN: Jann_0216
            RDE: RD1_0375(kdsB)
            PDE: Pden_2299
            MMR: Mmar10_0363
            HNE: HNE_2908
            ZMO: ZMO1489(kdsB)
            NAR: Saro_1284
            SWI: Swit_3964
            GOX: GOX0063
            GBE: GbCGDNIH1_1993
            ACR: Acry_0643
            RRU: Rru_A3163
            MAG: amb0133 amb4168
            MGM: Mmc1_2117
            ABA: Acid345_0573
            SUS: Acid_6216
            FNU: FN0807
            RBA: RB12690(kpsU)
            CTR: CT182(kdsB)
            CTA: CTA_0200(kdsB)
            CMU: TC0454
            CPN: CPn0235(kdsB)
            CPA: CP0527
            CPJ: CPj0235(kdsB)
            CPT: CpB0241
            CCA: CCA00596(kdsB)
            CAB: CAB569
            CFE: CF0408(kdtA2)
            PCU: pc0825(kdsB)
            LIL: LA1625(kdsB1) LA3573(kdsB2)
            LIC: LIC10625(kdsB) LIC12157
            LBJ: LBJ_0338(kdsB-1) LBJ_1144(kdsB-2)
            LBL: LBL_1198(kdsB-2) LBL_2738(kdsB-1)
            SYW: SYNW0184(kdsB2) SYNW0425(kdsB1)
            SYC: syc1810_d
            SYF: Synpcc7942_2290
            SYD: Syncc9605_0141 Syncc9605_0180
            SYE: Syncc9902_0209
            SYR: SynRCC307_0287(kdsB)
            SYX: SynWH7803_0233(kdsB)
            PMT: PMT1914(kdsB)
            PMF: P9303_25531(kdsB)
            PMG: P9301_14031(kdsB)
            BTH: BT_0745
            BFR: BF2223
            BFS: BF2274
            PGI: PG1815(kdsB)
            CHU: CHU_2845(kdsB)
            GFO: GFO_1823(kdsB)
            FPS: FP0981(kdsB)
            CTE: CT1830(kpsU)
            CCH: Cag_0320
            CPH: Cpha266_2079
            PVI: Cvib_0404 Cvib_0680
            PLT: Plut_0339
            AAE: aq_692(kpsU)
STRUCTURES  PDB: 1GQ9  1GQC  1H6J  1H7E  1H7F  1H7G  1H7H  1H7T  1VH1  1VH3  
                 1VIC  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.38
            ExPASy - ENZYME nomenclature database: 2.7.7.38
            ExplorEnz - The Enzyme Database: 2.7.7.38
            ERGO genome analysis and discovery system: 2.7.7.38
            BRENDA, the Enzyme Database: 2.7.7.38
            CAS: 37278-28-7
///
ENTRY       EC 2.7.7.39                 Enzyme
NAME        glycerol-3-phosphate cytidylyltransferase;
            CDP-glycerol pyrophosphorylase;
            cytidine diphosphoglycerol pyrophosphorylase;
            cytidine diphosphate glycerol pyrophosphorylase;
            CTP:glycerol 3-phosphate cytidylyltransferase;
            Gro-PCT
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     CTP:sn-glycerol-3-phosphate cytidylyltransferase
REACTION    CTP + sn-glycerol 3-phosphate = diphosphate + CDP-glycerol
            [RN:R00856]
ALL_REAC    R00856
SUBSTRATE   CTP [CPD:C00063];
            sn-glycerol 3-phosphate [CPD:C00093]
PRODUCT     diphosphate [CPD:C00013];
            CDP-glycerol [CPD:C00513]
REFERENCE   1
  AUTHORS   Shaw, D.R.D.
  TITLE     Pyrophosphorolysis and enzymic synthesis of cytidine diphosphate
            glycerol and cytidine diphosphate ribitol.
  JOURNAL   Biochem. J. 82 (1962) 297-312.
  ORGANISM  Lactobacillus arabinosus, Escherichia coli [GN:eco]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00980  glycerol-3-phosphate cytidylyltransferase
GENES       EHI: 39.t00005
            ECC: c3696
            MSU: MS0658(tagD)
            ASU: Asuc_0816
            PPR: PBPRA2685 PBPRA2703(tagD1)
            SFR: Sfri_3930
            SSE: Ssed_2953
            SPL: Spea_1422
            SHN: Shewana3_2003
            CPS: CPS_4205(tagD)
            PAT: Patl_3211
            REU: Reut_B4994
            NIS: NIS_1257
            JAN: Jann_0819
            BSU: BG10449(tagD)
            BLI: BL02464(tagD)
            BLD: BLi03818(tagD)
            BCL: ABC3101(tagD)
            BAY: RBAM_032870(tagD)
            BPU: BPUM_3230(tagD)
            OIH: OB2908(tagD)
            SAU: SA0597(tagD)
            SAV: SAV0641(tagD)
            SAM: MW0603(tagD)
            SAR: SAR0651(tagD)
            SAS: SAS0607
            SAB: SAB0591(tagD)
            SAA: SAUSA300_0628
            SAO: SAOUHSC_00645
            SAJ: SaurJH9_0664
            SAH: SaurJH1_0679
            SEP: SE0415
            SER: SERP0300(tagD)
            SHA: SH2255(tagD)
            SSP: SSP2078
            LMO: lmo1089(tagD)
            LMF: LMOf2365_1105(tagD)
            LIN: lin1076(tagD)
            LWE: lwe1066(tagD)
            LLA: L150584(tagD2) L19816(tagD1)
            LLM: llmg_1606(tagD2)
            LPL: lp_0267(tagD1) lp_1248(tagD2)
            LJO: LJ1738
            LAC: LBA0518(tagD)
            LSA: LSA1574(tagD)
            LDB: Ldb1937(tagD)
            LBU: LBUL_1800
            LBR: LVIS_1565
            EFA: EF1175(gct)
            CPE: CPE0483
            CMI: CMM_0818(tagD)
            BLO: BL0210
            FNU: FN0930
            LIL: LA2410(tagD)
            LIC: LIC11539(tagD)
            LBJ: LBJ_1452
            LBL: LBL_1676
            PGI: PG2068(tagD)
            AAE: aq_1368(tagD2) aq_185(tagD1)
            MJA: MJ1179(taqD)
            MMP: MMP0943(taqD)
            MAC: MA1820(taqD)
            MBA: Mbar_A2084
            MMA: MM_0242
            MBU: Mbur_0427
            MHU: Mhun_2404
            MTH: MTH844
            MST: Msp_0390
            MSI: Msm_0859 Msm_1514
            MKA: MK0578(tagD)
            AFU: AF1418(taqD)
            HAL: VNG0777G(taqD)
            HMA: rrnAC1438(taqD)
            HWA: HQ1579A(taqD)
            NPH: NP3220A
            TAC: Ta1139
            TVO: TVN1215
            PTO: PTO1010
            PHO: PH0735
            PAB: PAB1507
            PFU: PF1116
            TKO: TK2274
            RCI: LRC62(taqD)
STRUCTURES  PDB: 1COZ  1N1D  2B7L  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.39
            ExPASy - ENZYME nomenclature database: 2.7.7.39
            ExplorEnz - The Enzyme Database: 2.7.7.39
            ERGO genome analysis and discovery system: 2.7.7.39
            BRENDA, the Enzyme Database: 2.7.7.39
            CAS: 9027-11-6
///
ENTRY       EC 2.7.7.40                 Enzyme
NAME        D-ribitol-5-phosphate cytidylyltransferase;
            CDP ribitol pyrophosphorylase;
            cytidine diphosphate ribitol pyrophosphorylase;
            ribitol 5-phosphate cytidylyltransferase;
            cytidine diphosphoribitol pyrophosphorylase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     CTP:D-ribitol-5-phosphate cytidylyltransferase
REACTION    CTP + D-ribitol 5-phosphate = diphosphate + CDP-ribitol [RN:R02921]
ALL_REAC    R02921
SUBSTRATE   CTP [CPD:C00063];
            D-ribitol 5-phosphate [CPD:C01068]
PRODUCT     diphosphate [CPD:C00013];
            CDP-ribitol [CPD:C00789]
REFERENCE   1
  AUTHORS   Shaw, D.R.D.
  TITLE     Pyrophosphorolysis and enzymic synthesis of cytidine diphosphate
            glycerol and cytidine diphosphate ribitol.
  JOURNAL   Biochem. J. 82 (1962) 297-312.
  ORGANISM  Lactobacillus arabinosus
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
GENES       SAJ: SaurJH9_0240
            SAH: SaurJH1_0246
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.40
            ExPASy - ENZYME nomenclature database: 2.7.7.40
            ExplorEnz - The Enzyme Database: 2.7.7.40
            ERGO genome analysis and discovery system: 2.7.7.40
            BRENDA, the Enzyme Database: 2.7.7.40
            CAS: 9027-07-0
///
ENTRY       EC 2.7.7.41                 Enzyme
NAME        phosphatidate cytidylyltransferase;
            CDP diglyceride pyrophosphorylase;
            CDP-diacylglycerol synthase;
            CDP-diacylglyceride synthetase;
            cytidine diphosphoglyceride pyrophosphorylase;
            phosphatidate cytidyltransferase;
            phosphatidic acid cytidylyltransferase;
            CTP:1,2-diacylglycerophosphate-cytidyl transferase;
            CTP-diacylglycerol synthetase;
            DAG synthetase;
            CDP-DG
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     CTP:phosphatidate cytidylyltransferase
REACTION    CTP + phosphatidate = diphosphate + CDP-diacylglycerol [RN:R01799]
ALL_REAC    R01799
SUBSTRATE   CTP [CPD:C00063];
            phosphatidate [CPD:C00416]
PRODUCT     diphosphate [CPD:C00013];
            CDP-diacylglycerol [CPD:C00269]
REFERENCE   1  [PMID:4291255]
  AUTHORS   Carter JR, Kennedy EP.
  TITLE     Enzymatic synthesis of cytidine diphosphate diglyceride.
  JOURNAL   J. Lipid. Res. 7 (1966) 678-83.
  ORGANISM  guinea pig
REFERENCE   2  [PMID:5679981]
  AUTHORS   McCaman RE, Finnerty WR.
  TITLE     Biosynthesis of cytidine diphosphate-diglyceride by a particulate
            fracgion from Micrococcus cerificans.
  JOURNAL   J. Biol. Chem. 243 (1968) 5074-80.
  ORGANISM  Micrococcus cerificans
REFERENCE   3  [PMID:6067194]
  AUTHORS   Petzold GL, Agranoff BW.
  TITLE     The biosynthesis of cytidine diphosphate diglyceride by embryonic
            chick brain.
  JOURNAL   J. Biol. Chem. 242 (1967) 1187-91.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
            PATH: map04070  Phosphatidylinositol signaling system
ORTHOLOGY   KO: K00981  phosphatidate cytidylyltransferase
GENES       HSA: 1040(CDS1) 8760(CDS2)
            PTR: 469872(CDS2)
            MMU: 74596(Cds1)
            RNO: 114101(Cds2) 81925(Cds1)
            CFA: 485780(CDS2) 487840(CDS1)
            GGA: 419517(CDS2) 422611(CDS1)
            DRE: 394161(cds2)
            SPU: 590057(LOC590057)
            DME: Dmel_CG7962(CdsA)
            ATH: AT1G62430(ATCDS1) AT4G26770
            OSA: 4325310
            CME: CMN215C
            SCE: YBR029C(CDS1)
            AGO: AGOS_AEL084W
            PIC: PICST_78259
            CGR: CAGL0I04752g
            SPO: SPBC13A2.03
            ANI: AN5166.2
            AFM: AFUA_1G07010 AFUA_3G13270
            AOR: AO090012000953
            CNE: CND00990
            UMA: UM02266.1
            ECU: ECU05_1250(cds)
            DDI: DDB_0233125(cdsA)
            PFA: PF14_0097
            CPV: cgd7_450
            CHO: Chro.70059
            TAN: TA17300
            TPV: TP04_0048
            TET: TTHERM_00059210 TTHERM_00579230
            TBR: Tb927.7.220
            TCR: 511237.40
            LMA: LmjF26.1620
            EHI: 133.t00020
            ECO: b0175(cdsA) b1409(ynbB)
            ECJ: JW1406(ynbB) JW5810(cdsA)
            ECE: Z0186(cdsA) Z2318
            ECS: ECs0177 ECs2011
            ECC: c0212(cdsA) c1835(ynbB)
            ECI: UTI89_C0190(cdsA) UTI89_C1631(ynbB)
            ECP: ECP_0183 ECP_1414
            ECV: APECO1_1812(cdsA) APECO1_560(ynbB)
            ECW: EcE24377A_0179(cdsA1) EcE24377A_1590(cdsA2)
            ECX: EcHS_A0177(cdsA1) EcHS_A1492(cdsA2)
            STY: STY0245(cdsA)
            STT: t0223(cdsA)
            SPT: SPA0229(cdsA)
            SEC: SC0222(cdsA)
            STM: STM0222(cdsA)
            YPE: YPO1050(cdsA) YPO2816(ynbB)
            YPK: y1116 y3129(cdsA)
            YPM: YP_0865(cdsA1) YP_2800(cdsA2)
            YPA: YPA_0526 YPA_2561
            YPN: YPN_1025 YPN_2950
            YPP: YPDSF_1662
            YPS: YPTB1045 YPTB2997(cdsA)
            YPI: YpsIP31758_1019(cdsA1) YpsIP31758_3005(cdsA2)
            SFL: SF0165(cdsA) SF1809(ynbB)
            SFX: S0168(cdsA) S1465
            SFV: SFV_0158(cdsA) SFV_1800
            SSN: SSON_0187(cdsA)
            SBO: SBO_0163(cdsA)
            SDY: SDY_0191(cdsA)
            ECA: ECA1037(cdsA)
            PLU: plu0678(cdsA) plu4775
            WBR: WGLp386(cdsA)
            SGL: SG1937
            ENT: Ent638_0713
            SPE: Spro_3784
            BFL: Bfl277(cdsA)
            BPN: BPEN_285(cdsA)
            HIN: HI0919(cdsA)
            HIT: NTHI1087(cdsA)
            HDU: HD1193(cdsA)
            HSO: HS_0982(cdsA)
            PMU: PM1990(cdsA) PM2002
            MSU: MS1926(cdsA)
            APL: APL_0413(cdsA)
            XFA: XF1049
            XFT: PD0329(cdsA)
            XCC: XCC0506(cdsA) XCC1368(cdsA)
            XCB: XC_0518 XC_2870
            XCV: XCV0555 XCV1473(cdsA)
            XAC: XAC0521(cdsA) XAC1416(cdsA)
            XOO: XOO1971(cdsA)
            XOM: XOO_1861(XOO1861)
            VCH: VC1936 VC2255
            VCO: VC0395_A1846(cdsA)
            VVU: VV1_1865
            VVY: VV2552
            VPA: VP2313
            VFI: VF1957
            PPR: PBPRA2963
            PAE: PA2536 PA3651(cdsA)
            PAU: PA14_17120(cdsA) PA14_31760(cdsA)
            PPU: PP_1596(cdsA)
            PPF: Pput_4181
            PST: PSPTO_1539(cdsA-1) PSPTO_5541(cdsA-2)
            PSB: Psyr_1348
            PSP: PSPPH_3835(cdsA)
            PFL: PFL_1181(cdsA) PFL_6200(cdsA)
            PFO: Pfl_1106
            PEN: PSEEN0705 PSEEN4215(cdsA)
            PMY: Pmen_3048
            PAR: Psyc_1532(cdsA)
            PCR: Pcryo_1711
            ACI: ACIAD1375(cdsA) ACIAD1664
            ACB: A1S_1972
            SON: SO_1634(cdsA)
            SDN: Sden_1559
            SFR: Sfri_1275
            SAZ: Sama_1144
            SBL: Sbal_1455
            SHE: Shewmr4_2636
            SHM: Shewmr7_2703
            SHN: Shewana3_2810
            SHW: Sputw3181_2750
            ILO: IL0840(cdsA)
            CPS: CPS_1558(cdsA)
            PHA: PSHAa2031(cdsA)
            PAT: Patl_1254
            SDE: Sde_2592
            MAQ: Maqu_2543
            CBU: CBU_1381(cdsA)
            CBD: COXBU7E912_0613(cdsA)
            LPN: lpg0504(cdsA)
            LPF: lpl0543(cdsA)
            LPP: lpp0567(cdsA)
            MCA: MCA0572(cdsA)
            FTU: FTT0318(cdsA)
            FTF: FTF0318(cdsA)
            FTW: FTW_1764(cdsA)
            FTL: FTL_0229
            FTH: FTH_0224
            FTA: FTA_0245(cdsA)
            FTN: FTN_0232(cdsA)
            TCX: Tcr_1280
            NOC: Noc_0813 Noc_1726
            AEH: Mlg_1858
            HCH: HCH_05247
            CSA: Csal_0568
            ABO: ABO_1148(cdsA)
            AHA: AHA_1178(cdsA)
            DNO: DNO_0718(cdsA)
            BCI: BCI_0533(cdsA)
            RMA: Rmag_0026
            VOK: COSY_0026(cdsA)
            NME: NMB0185
            NMA: NMA0082(cdsA)
            NMC: NMC0176(cdsA)
            NGO: NGO1798
            CVI: CV_2201(cdsA)
            RSO: RSc1409(cdsA)
            REU: Reut_A1876 Reut_B4016
            REH: H16_A2088
            RME: Rmet_1440
            BMA: BMA1550(cdsA)
            BMV: BMASAVP1_A2051(cdsA)
            BML: BMA10299_A3260(cdsA)
            BMN: BMA10247_1323(cdsA)
            BXE: Bxe_A1687
            BUR: Bcep18194_A4517 Bcep18194_A5324
            BCN: Bcen_0890 Bcen_6063
            BCH: Bcen2424_1372 Bcen2424_2014
            BAM: Bamb_1250 Bamb_2047
            BPS: BPSL2154
            BPM: BURPS1710b_2578(cdsA)
            BPL: BURPS1106A_2488(cdsA)
            BPD: BURPS668_2432(cdsA)
            BTE: BTH_I2032(cdsA)
            PNU: Pnuc_1446
            BPE: BP1424(cdsA)
            BPA: BPP1532(cdsA)
            BBR: BB2610(cdsA)
            RFR: Rfer_1993
            POL: Bpro_1084 Bpro_2690
            MPT: Mpe_A0483 Mpe_A1974
            HAR: HEAR1340(cdsA)
            MMS: mma_2053(cdsA)
            NEU: NE1713(cdsA)
            NET: Neut_2030
            NMU: Nmul_A0662
            EBA: ebA5992(cdsA)
            AZO: azo0668 azo1904(cdsA)
            DAR: Daro_1747
            TBD: Tbd_0790
            MFA: Mfla_1525
            HPY: HP0215(cdsA)
            HPJ: jhp0201(cdsA)
            HPA: HPAG1_0216
            HHE: HH0523(cdsA)
            HAC: Hac_1504(cdsA)
            WSU: WS0813(cdsA)
            TDN: Tmden_0125
            CJE: Cj1347c(cdsA)
            CJR: CJE1536(cdsA)
            CJJ: CJJ81176_1346(cdsA)
            CJU: C8J_1263(cdsA)
            CJD: JJD26997_0363(cdsA)
            CFF: CFF8240_0209(cdsA)
            CCV: CCV52592_0595(cdsA) CCV52592_1174(cdsA)
            CHA: CHAB381_0122(cdsA)
            CCO: CCC13826_0421(cdsA)
            ABU: Abu_0160(cdsA)
            NIS: NIS_1667(cdsA)
            SUN: SUN_0145
            GSU: GSU1916(cdsA)
            GME: Gmet_1255
            PCA: Pcar_1916 Pcar_2778
            DVU: DVU0868(cdsA)
            DDE: Dde_1125
            LIP: LI0385(cdsA)
            BBA: Bd2894 Bd3786(cdsA)
            DPS: DP1159
            ADE: Adeh_3584
            MXA: MXAN_2556
            SAT: SYN_00917
            SFU: Sfum_1783
            RPR: RP424
            RTY: RT0410(cdsA)
            RCO: RC0589(cdsA)
            RFE: RF_0655(cdsA)
            RBE: RBE_0746(cdsA)
            OTS: OTBS_0267(cdsA)
            WOL: WD0526(cdsA)
            WBM: Wbm0803
            AMA: AM132(cdsA)
            APH: APH_0113
            ERU: Erum7220
            ERW: ERWE_CDS_07600(cdsA)
            ERG: ERGA_CDS_07520(cdsA)
            ECN: Ecaj_0757
            ECH: ECH_0269
            NSE: NSE_0942
            PUB: SAR11_0911(cdsA)
            MLO: mll0639
            MES: Meso_1386
            SME: SMc02096(cdsA)
            ATU: Atu1379(cdsA)
            ATC: AGR_C_2551
            RET: RHE_CH01918(cdsAch) RHE_PB00099(cdsAb)
            RLE: RL2226(cdsA) pRL90200
            BME: BMEI0828
            BMF: BAB1_1179(cdsA)
            BMS: BR1157(cdsA)
            BMB: BruAb1_1163(cdsA)
            BOV: BOV_1114(cdsA)
            OAN: Oant_2034
            BJA: bll4856(cdsA)
            BRA: BRADO4135(cdsA)
            BBT: BBta_4512(cdsA)
            RPA: RPA2917(cdsA)
            RPB: RPB_2823
            RPC: RPC_2441
            RPD: RPD_2852
            RPE: RPE_2558
            NWI: Nwi_1854
            NHA: Nham_1699
            BHE: BH06260(cdsA1)
            BQU: BQ06970(cdsA2)
            BBK: BARBAKC583_0587(cdsA)
            CCR: CC_1918
            SIL: SPO1666(cdsA)
            SIT: TM1040_1411
            RSP: RSP_2708(cdsA)
            JAN: Jann_2456
            RDE: RD1_2588
            MMR: Mmar10_1385
            HNE: HNE_1773(cdsA)
            ZMO: ZMO1151(cdsA)
            NAR: Saro_1374
            SAL: Sala_1955
            ELI: ELI_03800
            GOX: GOX1815
            GBE: GbCGDNIH1_0937
            RRU: Rru_A1591
            MAG: amb2493
            MGM: Mmc1_1845
            ABA: Acid345_1418
            BSU: BG12575(cdsA)
            BHA: BH2422(cdsA)
            BAN: BA3960(cdsA)
            BAR: GBAA3960(cdsA)
            BAA: BA_4430
            BAT: BAS3673
            BCE: BC3820
            BCA: BCE_3863(cdsA)
            BCZ: BCZK3581(cdsA)
            BCY: Bcer98_2474
            BTK: BT9727_3563(cdsA)
            BTL: BALH_3453
            BLI: BL01238(cdsA)
            BLD: BLi01875(cdsA)
            BCL: ABC2237(cdsA)
            BAY: RBAM_016380(cdsA)
            BPU: BPUM_1553(cdsA)
            OIH: OB1591(cdsA)
            GKA: GK1254
            SAU: SA1104(cdsA)
            SAV: SAV1261(cdsA)
            SAM: MW1144(cdsA)
            SAR: SAR1237
            SAS: SAS1195
            SAC: SACOL1280(cdsA)
            SAB: SAB1123(cdsA)
            SAA: SAUSA300_1154(cdsA)
            SAO: SAOUHSC_01238
            SAJ: SaurJH9_1321
            SAH: SaurJH1_1347
            SEP: SE0937
            SER: SERP0828(cdsA)
            SHA: SH1653(cdsA)
            SSP: SSP1507
            LMO: lmo1316(cdsA)
            LMF: LMOf2365_1333(cdsA)
            LIN: lin1353(cdsA)
            LWE: lwe1331(cdsA)
            LLA: L182799(cdsA)
            LLC: LACR_2434
            LLM: llmg_2414(cdsA)
            SPY: SPy_1964(cdsA)
            SPZ: M5005_Spy_1675(cdsA)
            SPM: spyM18_2032(cdsA)
            SPG: SpyM3_1690(cdsA)
            SPS: SPs1692
            SPH: MGAS10270_Spy1743(cdsA)
            SPI: MGAS10750_Spy1769(cdsA)
            SPJ: MGAS2096_Spy1698(cdsA)
            SPK: MGAS9429_Spy1676(cdsA)
            SPA: M6_Spy1683
            SPB: M28_Spy1663(cdsA)
            SPN: SP_0262
            SPR: spr0241(cdsA)
            SPD: SPD_0244(cdsA)
            SAG: SAG1915(cdsA)
            SAN: gbs1902
            SAK: SAK_1873(cdsA)
            SMU: SMU.1785(cdsA)
            STC: str0198(cdsA)
            STL: stu0198(cdsA)
            SSA: SSA_2072(cdsA)
            SGO: SGO_1853(cdsA)
            LPL: lp_2050(cdsA)
            LJO: LJ1495
            LAC: LBA1265(cdsA)
            LSA: LSA1259(cdsA)
            LSL: LSL_0564(cdsA)
            LDB: Ldb1340(cdsA)
            LBU: LBUL_1249
            LBR: LVIS_1344
            LCA: LSEI_1581
            LGA: LGAS_0806
            LRE: Lreu_0691
            PPE: PEPE_0882
            EFA: EF2494(cdsA)
            OOE: OEOE_0980
            LME: LEUM_0686
            STH: STH1497
            CAC: CAC1792(cdsA)
            CPE: CPE1695(cdsA)
            CPF: CPF_1949(cdsA)
            CPR: CPR_1667(cdsA)
            CTC: CTC01266
            CNO: NT01CX_2144(cdsA)
            CBA: CLB_2294(cdsA)
            CBH: CLC_2277(cdsA)
            CBF: CLI_2486(cdsA)
            CHY: CHY_1780(cdsA)
            DSY: DSY2541
            SWO: Swol_0887
            TTE: TTE1403(cdsA)
            MTA: Moth_1039
            MGE: MG_437
            MPN: MPN637(cdsA)
            MPU: MYPU_4740(cdsA)
            MGA: MGA_0785(cdsA)
            MMY: MSC_0356(cdsA)
            MMO: MMOB0560(cdsA)
            MHY: mhp550(cdsA)
            MHJ: MHJ_0534
            MHP: MHP7448_0533
            MSY: MS53_0005(cdsA)
            MCP: MCAP_0340(cdsA)
            UUR: UU511(cdsA)
            POY: PAM169(cdsA)
            AYW: AYWB_550(cdsA)
            MFL: Mfl286
            MTU: Rv2881c(cdsA)
            MTC: MT2948
            MBO: Mb2905c(cdsA)
            MBB: BCG_2902c(cdsA)
            MLE: ML1589
            MPA: MAP2944c(cdsA)
            MAV: MAV_3731(cdsA)
            MSM: MSMEG_2543(cdsA)
            MMC: Mmcs_2005
            CGL: NCgl1946(cgl2022)
            CGB: cg2216(cdsA)
            CEF: CE1909
            CDI: DIP1504
            CJK: jk1171(cdsA)
            NFA: nfa41270(cdsA)
            RHA: RHA1_ro06582(cdsA)
            SCO: SCO5628(SC6A9.39c)
            SMA: SAV2623(cdsA)
            TWH: TWT445(cdsA)
            TWS: TW322
            LXX: Lxx12480(cdsA)
            CMI: CMM_1387(cdsA)
            PAC: PPA1517
            TFU: Tfu_0680
            FRA: Francci3_3578
            FAL: FRAAL5777(cdsA)
            SEN: SACE_6034(cdsA)
            STP: Strop_1326
            BLO: BL1507(cdsA)
            BAD: BAD_0785(cdsA)
            RXY: Rxyl_1403
            FNU: FN1308 FN1325
            RBA: RB11255 RB12598(cdsA) RB4583(cds)
            CTR: CT451(cdsA)
            CTA: CTA_0493(cdsA)
            CMU: TC0736
            CPN: CPn0567(cdsA)
            CPA: CP0182
            CPJ: CPj0567(cdsA)
            CPT: CpB0589
            CCA: CCA00175
            CAB: CAB172
            CFE: CF0832(cdsA)
            PCU: pc0320(cdsA)
            BBU: BB0119(cdsA)
            BGA: BG0120
            BAF: BAPKO_0120
            TPA: TP0602
            TDE: TDE2343(cdsA)
            LIL: LA3293(cdsA)
            LIC: LIC10855(cds)
            LBJ: LBJ_0909(cdsA)
            LBL: LBL_0924(cdsA)
            SYN: slr1369(cdsA)
            SYW: SYNW0942
            SYC: syc1121_d(cdsA)
            SYF: Synpcc7942_0394
            SYD: Syncc9605_1623
            SYE: Syncc9902_1385
            SYG: sync_1023(cdsA)
            SYR: SynRCC307_0784(cdsA)
            SYX: SynWH7803_1539(cdsA)
            CYA: CYA_0516(cdsA)
            CYB: CYB_0300(cdsA)
            TEL: tll2108(cdsA)
            GVI: gll1396
            ANA: all3875
            AVA: Ava_1818
            PMA: Pro1111(cdsA)
            PMM: PMM1085
            PMT: PMT1065
            PMN: PMN2A_0664
            PMI: PMT9312_1096
            PMB: A9601_11911(cdsA)
            PMC: P9515_11751(cdsA)
            PMF: P9303_09871(cdsA)
            PMG: P9301_11921(cdsA)
            PME: NATL1_14961(cdsA)
            BTH: BT_4006 BT_4463
            BFR: BF0773 BF3587
            BFS: BF0701 BF3391
            PGI: PG0046(cdsA)
            SRU: SRU_1704(cdsA) SRU_1714(cdsA)
            CHU: CHU_0358(cdsA)
            GFO: GFO_2696(cdsA)
            FPS: FP0605(cdsA)
            CTE: CT0233(cdsA)
            CCH: Cag_1470
            PLT: Plut_1788
            DET: DET0372(cdsA)
            DEH: cbdb_A315(cdsA)
            DRA: DR_1509
            DGE: Dgeo_1045
            TTH: TTC0505
            TTJ: TTHA0857
            AAE: aq_1249(cds)
            TMA: TM1397
            HWA: HQ3230A(cdsA)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.41
            ExPASy - ENZYME nomenclature database: 2.7.7.41
            ExplorEnz - The Enzyme Database: 2.7.7.41
            ERGO genome analysis and discovery system: 2.7.7.41
            BRENDA, the Enzyme Database: 2.7.7.41
            CAS: 9067-83-8
///
ENTRY       EC 2.7.7.42                 Enzyme
NAME        [glutamate---ammonia-ligase] adenylyltransferase;
            glutamine-synthetase adenylyltransferase;
            ATP:glutamine synthetase adenylyltransferase;
            adenosine triphosphate:glutamine synthetase adenylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyltransferase
REACTION    ATP + [L-glutamate:ammonia ligase (ADP-forming)] = diphosphate +
            adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] [RN:R03473]
ALL_REAC    R03473
SUBSTRATE   ATP [CPD:C00002];
            [L-glutamate:ammonia ligase (ADP-forming)] [CPD:C01281]
PRODUCT     diphosphate [CPD:C00013];
            adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] [CPD:C01299]
REFERENCE   1  [PMID:4920894]
  AUTHORS   Ebner E, Wolf D, Gancedo C, Elsasser S, Holzer H.
  TITLE     ATP: glutamine synthetase adenylyltransferase from Escherichia coli
            B. Purification and properties.
  JOURNAL   Eur. J. Biochem. 14 (1970) 535-44.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4867671]
  AUTHORS   Kingdon HS, Shapiro BM, Stadtman ER.
  TITLE     Regulation of glutamine synthetase. 8. ATP: glutamine synthetase
            adenylyltransferase, an enzyme that catalyzes alterations in the
            regulatory properties of glutamine synthetase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 58 (1967) 1703-10.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:5338440]
  AUTHORS   Mecke D, Wulff K, Liess K, Holzer H.
  TITLE     Characterization of a glutamine synthetase inactivating enzyme from
            Escherichia coli.
  JOURNAL   Biochem. Biophys. Res. Commun. 24 (1966) 452-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4
  AUTHORS   Mecke, D., Wulff, K. and Holzer, H.
  TITLE     Metabolit-induzierte Inaktivierung von Glutaminsynthetase aus
            Escherichia coli im zellfreien System.
  JOURNAL   Biochim. Biophys. Acta 128 (1966) 559-567.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:4298074]
  AUTHORS   Shapiro BM, Stadtman ER.
  TITLE     5'-adenylyl-O-tyrosine. The novel phosphodiester residue of
            adenylylated glutamine synthetase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 243 (1968) 3769-71.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:4402680]
  AUTHORS   Wolf D, Ebner E, Hinze H.
  TITLE     Inactivation, stabilization and some properties of ATP: glutamine
            synthetase adenylyltransferase from Escherichia coli B.
  JOURNAL   Eur. J. Biochem. 25 (1972) 239-44.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K00982  glutamate-ammonia-ligase adenylyltransferase
GENES       ECO: b3053(glnE)
            ECJ: JW3025(glnE)
            ECE: Z4406(glnE)
            ECS: ECs3936
            ECC: c3801(glnE)
            ECI: UTI89_C3489(glnE)
            ECP: ECP_3142 ECP_3143
            ECW: EcE24377A_3516(glnE)
            ECX: EcHS_A3230(glnE)
            STY: STY3380(glnE)
            STT: t3121(glnE)
            SPT: SPA3069(glnE)
            SEC: SC3148(glnE)
            STM: STM3201(glnE)
            YPE: YPO0653(glnE)
            YPK: y3525(glnE)
            YPM: YP_2968(glnE)
            YPA: YPA_3137
            YPN: YPN_0513
            YPP: YPDSF_0437
            YPS: YPTB3408(glnE)
            YPI: YpsIP31758_0563(glnE)
            SFL: SF3094(glnE)
            SFX: S3299(glnE)
            SFV: SFV_3093(glnE)
            SSN: SSON_3190(glnE)
            SBO: SBO_2909(glnE)
            SDY: SDY_3236(glnE)
            ECA: ECA3585(glnE)
            PLU: plu3969(glnE)
            SGL: SG0260
            ENT: Ent638_3456
            SPE: Spro_4290
            HIT: NTHI0082(glnE)
            HDU: HD1709(glnE)
            HSO: HS_1218(glnE)
            PMU: PM0375(glnE)
            MSU: MS1278(glnE)
            APL: APL_0969(glnE)
            ASU: Asuc_1490
            XCC: XCC3599(glnE)
            XCB: XC_0562
            XCV: XCV0579(glnE)
            XAC: XAC0550(glnE)
            XOO: XOO4274(glnE)
            XOM: XOO_4031(XOO4031)
            VCH: VC2438
            VCO: VC0395_A2015(glnE)
            VVU: VV1_0614
            VVY: VV0581
            VPA: VP0423
            VFI: VF2235
            PPR: PBPRA0448(glnE)
            PAE: PA5014(glnE)
            PAU: PA14_66270(glnE)
            PPU: PP_0340(glnE)
            PPF: Pput_0365
            PST: PSPTO_5004(glnE)
            PSB: Psyr_0519
            PSP: PSPPH_0509(glnE)
            PFL: PFL_0510(glnE)
            PFO: Pfl_0464
            PEN: PSEEN5144(glnE)
            PMY: Pmen_0577
            PAR: Psyc_1217(glnE)
            PCR: Pcryo_1175
            PRW: PsycPRwf_0980
            ACI: ACIAD0596(glnE)
            SON: SO_3760(glnE)
            SDN: Sden_0702
            SFR: Sfri_3261
            SAZ: Sama_2663
            SBL: Sbal_3445
            SBM: Shew185_0893
            SLO: Shew_0628
            SPC: Sputcn32_3086
            SSE: Ssed_3833
            SPL: Spea_3477
            SHE: Shewmr4_3109
            SHM: Shewmr7_0863
            SHN: Shewana3_0832
            SHW: Sputw3181_0858
            ILO: IL1959(glnE)
            CPS: CPS_4185(glnE)
            PHA: PSHAa2595(glnE)
            PAT: Patl_3601
            SDE: Sde_0389
            PIN: Ping_0187
            MAQ: Maqu_0776
            LPN: lpg0679
            LPF: lpl0715(glnE)
            LPP: lpp0735(glnE)
            MCA: MCA2345(glnE)
            TCX: Tcr_1497
            NOC: Noc_0135
            AEH: Mlg_2698
            HHA: Hhal_2348
            HCH: HCH_01044(glnE)
            CSA: Csal_2926
            ABO: ABO_2302(glnE)
            MMW: Mmwyl1_1106
            AHA: AHA_0771
            NME: NMB0224
            NMA: NMA0035(glnE)
            NMC: NMC0224(glnE)
            NGO: NGO1758
            CVI: CV_2095(glnE)
            RSO: RSc2656(glnE)
            REU: Reut_A1030
            RME: Rmet_0994
            BMA: BMA2334(glnE)
            BMV: BMASAVP1_A0491(glnE)
            BML: BMA10299_A1108(glnE)
            BMN: BMA10247_2215(glnE)
            BXE: Bxe_A3969
            BVI: Bcep1808_0703
            BUR: Bcep18194_A3830
            BCN: Bcen_0258
            BCH: Bcen2424_0742
            BAM: Bamb_0635
            BPS: BPSL2835(glnE)
            BPM: BURPS1710b_3331(glnE)
            BPL: BURPS1106A_3320(glnE)
            BPD: BURPS668_3287(glnE)
            BTE: BTH_I1299
            PNU: Pnuc_1775
            BPE: BP1260(glnE)
            BPA: BPP1875(glnE)
            BBR: BB3233(glnE)
            RFR: Rfer_0367
            POL: Bpro_4656
            PNA: Pnap_3898
            AAV: Aave_4657
            AJS: Ajs_4019
            VEI: Veis_4832
            MPT: Mpe_A0242
            HAR: HEAR0859(glnE)
            MMS: mma_0834(glnE)
            NEU: NE1329(glnE)
            NET: Neut_1266
            NMU: Nmul_A1058
            EBA: ebA977(glnE)
            AZO: azo1293(glnE)
            DAR: Daro_3331
            TBD: Tbd_0503
            MFA: Mfla_1726
            GSU: GSU3378
            GME: Gmet_0071
            GUR: Gura_4321
            PCA: Pcar_2171
            PPD: Ppro_0511
            BBA: Bd0178(glnE)
            ADE: Adeh_1054
            AFW: Anae109_1104
            SFU: Sfum_0011
            MLO: mlr7698
            MES: Meso_0904
            PLA: Plav_0946
            SME: SMc02368(glnE)
            SMD: Smed_0640
            ATU: Atu0981(glnE)
            ATC: AGR_C_1798
            RET: RHE_CH01296(glnE)
            RLE: RL1443(glnE)
            BME: BMEI1327
            BMF: BAB1_0638(glnE)
            BMS: BR0614(glnE)
            BMB: BruAb1_0633(glnE)
            BOV: BOV_0613(glnE)
            OAN: Oant_2664
            BJA: blr3133(glnE)
            BRA: BRADO2744(glnE)
            BBT: BBta_3086(glnE)
            RPA: RPA1933(glnE)
            RPB: RPB_3440
            RPC: RPC_1846
            RPD: RPD_2014
            RPE: RPE_1944
            NWI: Nwi_1199
            NHA: Nham_1448
            BHE: BH04800(glnE)
            BQU: BQ04000(glnE)
            XAU: Xaut_3519
            CCR: CC_2753
            SIL: SPO2523(glnE)
            SIT: TM1040_0885
            RSP: RSP_2643(glnE)
            RSH: Rsph17029_1300
            RSQ: Rsph17025_1178
            JAN: Jann_2446
            RDE: RD1_2802(glnE)
            PDE: Pden_2167
            MMR: Mmar10_0945
            HNE: HNE_1316(glnE)
            NAR: Saro_3154
            SAL: Sala_2185
            SWI: Swit_3922
            ELI: ELI_12340
            GBE: GbCGDNIH1_1951
            ACR: Acry_0150
            RRU: Rru_A2038
            MAG: amb2683
            MGM: Mmc1_1862
            SUS: Acid_0069
            MTU: Rv2221c(glnE)
            MTC: MT2279
            MBO: Mb2245c(glnE)
            MBB: BCG_2238c(glnE)
            MLE: ML1630(glnE)
            MPA: MAP1965c(glnE)
            MAV: MAV_2245
            MSM: MSMEG_4293
            MVA: Mvan_3597
            MGI: Mflv_2910
            MMC: Mmcs_3327
            MKM: Mkms_3389
            MJL: Mjls_3338
            CGL: NCgl2147(cgl2228)
            CGB: cg2446(glnE)
            CEF: CE2126(glnE)
            CDI: DIP1670(glnE)
            CJK: jk0676(glnE)
            NFA: nfa16610(glnE)
            RHA: RHA1_ro01166(glnE)
            SCO: SCO2234(glnE)
            SMA: SAV5972(glnE)
            LXX: Lxx10020(glnE)
            CMI: CMM_1635(glnE)
            ART: Arth_1593
            PAC: PPA0666
            NCA: Noca_2048
            TFU: Tfu_0986
            FRA: Francci3_3144
            FAL: FRAAL5164(glnE)
            ACE: Acel_0920
            KRA: Krad_3295
            SEN: SACE_1619(glnE)
            BLO: BL0795(glnE)
            BAD: BAD_0758(glnE)
            RBA: RB6825(glnE)
            AAE: aq_1774(glnE)
STRUCTURES  PDB: 1V4A  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.42
            ExPASy - ENZYME nomenclature database: 2.7.7.42
            ExplorEnz - The Enzyme Database: 2.7.7.42
            ERGO genome analysis and discovery system: 2.7.7.42
            BRENDA, the Enzyme Database: 2.7.7.42
            CAS: 9077-66-1
///
ENTRY       EC 2.7.7.43                 Enzyme
NAME        N-acylneuraminate cytidylyltransferase;
            CMP-sialate pyrophosphorylase;
            CMP-sialate synthase;
            cytidine 5'-monophosphosialic acid synthetase;
            CMP-Neu5Ac synthetase;
            CMP-NeuAc synthetase;
            acylneuraminate cytidyltransferase;
            CMP-N-acetylneuraminate synthetase;
            CMP-N-acetylneuraminate synthase;
            CMP-N-acetylneuraminic acid synthase;
            CMP-NANA synthetase;
            CMP-sialate synthetase;
            CMP-sialic synthetase;
            cytidine 5'-monophospho-N-acetylneuraminic acid synthetase;
            cytidine 5-monophosphate N-acetylneuraminic acid synthetase;
            cytidine monophosphosialic acid synthetase;
            cytidine monophosphoacetylneuraminic synthetase;
            cytidine monophosphosialate pyrophosphorylase;
            cytidine monophosphosialate synthetase;
            acetylneuraminate cytidylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     CTP:N-acylneuraminate cytidylyltransferase
REACTION    CTP + N-acylneuraminate = diphosphate + CMP-N-acylneuraminate
            [RN:R02599]
ALL_REAC    R02599 > R01117 R04215
SUBSTRATE   CTP [CPD:C00063];
            N-acylneuraminate [CPD:C00591]
PRODUCT     diphosphate [CPD:C00013];
            CMP-N-acylneuraminate [CPD:C01064]
COMMENT     Acts on N-acetyl- and N-glycolyl- derivatives.
REFERENCE   1  [PMID:4288894]
  AUTHORS   Kean EL, Roseman S.
  TITLE     The sialic acids. X. Purification and properties of cytidine
            5'-monophosphosialic acid synthetase.
  JOURNAL   J. Biol. Chem. 241 (1966) 5643-50.
  ORGANISM  pig [GN:ssc], Neisseria meningitidis, sheep
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K00983  N-acylneuraminate cytidylyltransferase
GENES       HSA: 55907(CMAS)
            MMU: 12764(Cmas)
            RNO: 312826(Cmas)
            GGA: 418199(CMAS)
            SPU: 588508(LOC588508)
            ECI: UTI89_C3371(neuA)
            HIT: NTHI1891(siaB)
            HDU: HD0685(neuA)
            HSO: HS_0700(neuA) HS_0706(neuA)
            PMU: PM0187(neuA)
            VVU: VV1_0803
            VVY: VV0316
            VPA: VP0203
            VFI: VF0147
            PPR: PBPRA2709(neuA)
            PFL: PFL_1623
            PFO: Pfl_1521
            PAR: Psyc_0656(neuA2)
            SDN: Sden_1288
            SBM: Shew185_2981
            SSE: Ssed_3104
            SHN: Shewana3_1309
            ILO: IL0554
            CPS: CPS_2094
            PAT: Patl_3078
            LPN: lpg0751(neuA)
            LPF: lpl0788(neuA)
            LPP: lpp0817(neuA)
            TCX: Tcr_1455
            AEH: Mlg_2324
            HCH: HCH_04832
            AHA: AHA_4178
            NME: NMB0069(siaB)
            NMC: NMC0053(siaB)
            CVI: CV_4028(neuA)
            NEU: NE1569(neuA1)
            NET: Neut_1548
            NMU: Nmul_A0410
            HPY: HP0326(neuA)
            HPA: HPAG1_0219 HPAG1_0329 HPAG1_0330
            HHE: HH0900(neuA)
            HAC: Hac_0994(neuA_fragment_2) Hac_0995(neuA_fragment_1)
                 Hac_1269(neuA)
            WSU: WS2106
            TDN: Tmden_0599
            CJE: Cj1143(neuA1) Cj1311(neuA2) Cj1331(ptmB)
            CJR: CJE1506(neuA) CJE1520(ptmB)
            CJJ: CJJ81176_1328(neuA)
            CJU: C8J_1244(neuA2)
            CCO: CCC13826_2299
            ABU: Abu_2183 Abu_2245(neuA)
            GSU: GSU1972
            DVL: Dvul_2588
            DDE: Dde_3257
            BBA: Bd1686(neuA)
            BJA: blr5972(neuA)
            RPB: RPB_1536
            RPE: RPE_4239
            NWI: Nwi_2397
            SAL: Sala_1578
            MGM: Mmc1_0559 Mmc1_2414
            BPU: BPUM_1898
            GKA: GK3120
            SAG: SAG1158(neuA)
            SAN: gbs1233(neuA)
            SAK: SAK_1247(neuA)
            CNO: NT01CX_1783
            CBF: CLI_2773
            CKL: CKL_2466(neuA)
            DSY: DSY3307
            MTA: Moth_0758
            LIL: LA1605(neuA1) LA1615(neuA2)
            LIC: LIC12167 LIC12177(neuA)
            SYW: SYNW0398 SYNW0444
            SYD: Syncc9605_2217
            SYE: Syncc9902_0462
            SYG: sync_0170(neuA-1) sync_0182(neuA-2)
            PMI: PMT9312_1349
            PMB: A9601_13421
            PMF: P9303_01151
            PMG: P9301_14131
            SRU: SRU_0608
            CHU: CHU_2758(neuB)
            GFO: GFO_0572(neuA) GFO_2023(neuA)
            FPS: FP1257(neuA)
            CTE: CT1153(neuA)
            CCH: Cag_1132
            MHU: Mhun_3094
            MSI: Msm_0944
            HWA: HQ3518A(neuA)
STRUCTURES  PDB: 1EYR  1EZI  1QWJ  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.43
            ExPASy - ENZYME nomenclature database: 2.7.7.43
            ExplorEnz - The Enzyme Database: 2.7.7.43
            ERGO genome analysis and discovery system: 2.7.7.43
            BRENDA, the Enzyme Database: 2.7.7.43
            CAS: 9067-82-7
///
ENTRY       EC 2.7.7.44                 Enzyme
NAME        glucuronate-1-phosphate uridylyltransferase;
            UDP-glucuronate pyrophosphorylase;
            UDP-D-glucuronic acid pyrophosphorylase;
            UDP-glucuronic acid pyrophosphorylase;
            uridine diphosphoglucuronic pyrophosphorylase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     UTP:1-phospho-alpha-D-glucuronate uridylyltransferase
REACTION    UTP + 1-phospho-alpha-D-glucuronate = diphosphate + UDP-glucuronate
            [RN:R01381]
ALL_REAC    R01381
SUBSTRATE   UTP [CPD:C00075];
            1-phospho-alpha-D-glucuronate
PRODUCT     diphosphate [CPD:C00013];
            UDP-glucuronate [CPD:C00167]
COMMENT     Also acts slowly with CTP.
REFERENCE   1  [PMID:5570433]
  AUTHORS   Roberts RM.
  TITLE     The formation of uridine diphosphate-glucuronic acid in plants.
            Uridine diphosphate-glucuronic acid pyrophosphorylase from barley
            seedlings.
  JOURNAL   J. Biol. Chem. 246 (1971) 4995-5002.
  ORGANISM  Hordeum vulgare [GN:ehvu]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00053  Ascorbate and aldarate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.44
            ExPASy - ENZYME nomenclature database: 2.7.7.44
            ExplorEnz - The Enzyme Database: 2.7.7.44
            ERGO genome analysis and discovery system: 2.7.7.44
            BRENDA, the Enzyme Database: 2.7.7.44
            CAS: 52228-05-4
///
ENTRY       EC 2.7.7.45                 Enzyme
NAME        guanosine-triphosphate guanylyltransferase;
            diguanosine tetraphosphate synthetase;
            GTP-GTP guanylyltransferase;
            Gp4G synthetase;
            guanosine triphosphate-guanose triphosphate guanylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     GTP:GTP guanylyltransferase
REACTION    2 GTP = diphosphate + P1,P4-bis(5'-guanosyl) tetraphosphate
            [RN:R00012]
ALL_REAC    R00012
SUBSTRATE   GTP [CPD:C00044]
PRODUCT     diphosphate [CPD:C00013];
            P1,P4-bis(5'-guanosyl) tetraphosphate [CPD:C01261]
COMMENT     Also acts, more slowly, on GDP to form P1,P3-bis(5'-guanosyl)
            triphosphate.
REFERENCE   1  [PMID:4208243]
  AUTHORS   Warner AH, Beers PC, Huang FL.
  TITLE     Biosynthesis of the diguanosine nucleotides. I. Purification and
            properties of an enzyme from yolk platelets of brine shrimp embryos.
  JOURNAL   Can. J. Biochem. 52 (1974) 231-40.
  ORGANISM  Artemia salina
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.45
            ExPASy - ENZYME nomenclature database: 2.7.7.45
            ExplorEnz - The Enzyme Database: 2.7.7.45
            ERGO genome analysis and discovery system: 2.7.7.45
            BRENDA, the Enzyme Database: 2.7.7.45
            CAS: 54576-89-5
///
ENTRY       EC 2.7.7.46                 Enzyme
NAME        gentamicin 2"-nucleotidyltransferase;
            gentamicin 2"-adenylyltransferase;
            aminoglycoside adenylyltransferase;
            gentamycin 2"-nucleotidyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     NTP:gentamicin 2"-nucleotidyltransferase
REACTION    nucleoside triphosphate + gentamicin = diphosphate +
            2"-nucleotidylgentamicin [RN:R02432]
ALL_REAC    R02432
SUBSTRATE   nucleoside triphosphate [CPD:C00201];
            gentamicin [CPD:C00505]
PRODUCT     diphosphate [CPD:C00013];
            2''-nucleotidylgentamicin [CPD:C03565]
COMMENT     ATP, dATP, CTP, ITP and GTP can act as donors; kanamycin, tobramycin
            and sisomicin can also act as acceptors. The nucleotidyl residue is
            transferred to the 2-hydroxy of the 3-amino-3-deoxy-D-glucose moiety
            in the antibiotic.
REFERENCE   1  [PMID:6281224]
  AUTHORS   Angelatou F, Litsas SB, Kontomichalou P.
  TITLE     Purification and properties of two gentamicin-modifying enzymes,
            coded by a single plasmid pPK237 originating from Pseudomonas
            aeruginosa.
  JOURNAL   J. Antibiot. (Tokyo). 35 (1982) 235-44.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   2  [PMID:4946513]
  AUTHORS   Naganawa H, Yagisawa M, Kondo S, Takeuchi T, Umezawa H.
  TITLE     The structure determination of an enzymatic inactivation product of
            3',4'-dideoxykanamycin B.
  JOURNAL   J. Antibiot. (Tokyo). 24 (1971) 913-4.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4946512]
  AUTHORS   Yagisawa M, Naganawa H, Kondo S, Hamada M, Takeuchi T.
  TITLE     Adenylyldideoxykanamycin B, a product of the inactivation of
            dideoxykanamycin B by Escherichia coli carrying R factor.
  JOURNAL   J. Antibiot. (Tokyo). 24 (1971) 911-2.
  ORGANISM  Escherichia coli [GN:eco]
GENES       ANA: alr7069
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.46
            ExPASy - ENZYME nomenclature database: 2.7.7.46
            ExplorEnz - The Enzyme Database: 2.7.7.46
            ERGO genome analysis and discovery system: 2.7.7.46
            BRENDA, the Enzyme Database: 2.7.7.46
            CAS: 62213-33-6
///
ENTRY       EC 2.7.7.47                 Enzyme
NAME        streptomycin 3"-adenylyltransferase;
            streptomycin adenylate synthetase;
            streptomycin adenyltransferase;
            streptomycin adenylylase;
            streptomycin adenylyltransferase;
            streptomycin-spectinomycin adenylyltransferase;
            AAD (3");
            aminoglycoside 3"-adenylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ATP:streptomycin 3"-adenylyltransferase
REACTION    ATP + streptomycin = diphosphate + 3"-adenylylstreptomycin
            [RN:R02226]
ALL_REAC    R02226
SUBSTRATE   ATP [CPD:C00002];
            streptomycin [CPD:C00413]
PRODUCT     diphosphate [CPD:C00013];
            3''-adenylylstreptomycin [CPD:C03462]
COMMENT     Also acts on spectinomycin.
REFERENCE   1  [PMID:4887506]
  AUTHORS   Harwood JH, Smith DH.
  TITLE     Resistance factor-mediated streptomycin resistance.
  JOURNAL   J. Bacteriol. 97 (1969) 1262-71.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K00984  streptomycin 3"-adenylyltransferase
GENES       AOR: AO090005000196
            STY: STY1857(aadA)
            STT: t1142(aadA)
            SPT: SPA1582(aadA)
            SEC: SC032(aadA2) SC051(aadA2) SC053(aadA2) SC1275(aadA)
            STM: STM1264(aadA)
            SSN: SSON_3896(aadA)
            PMY: Pmen_2178
            LPP: plpp0092
            BUR: Bcep18194_B2105
            BAM: Bamb_3372
            BPA: BPP1010(aadA4)
            BBR: BB1224(aadA4)
            MMS: mma_1582
            NMU: Nmul_A0161
            SME: SMa2315 SMa2317
            SMD: Smed_5877
            PDE: Pden_4803
            SAU: SA0049(ant(9)) SA0765(ant(9)) SA1481(ant(9)) SA1952(ant(9))
                 SA2385(ant(9))
            SAV: SAV0053(ant(9)) SAV1656(ant(9))
            SAR: SAR0051(spc1) SAR1736(spc2)
            SAJ: SaurJH9_0040 SaurJH9_1714
            SAH: SaurJH1_0040 SaurJH1_1748
            SER: SERP1221(spc-1) SERP1344(spc-2) SERP2509(spC)
            CKL: CKL_2614
            DSY: DSY4374
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.47
            ExPASy - ENZYME nomenclature database: 2.7.7.47
            ExplorEnz - The Enzyme Database: 2.7.7.47
            ERGO genome analysis and discovery system: 2.7.7.47
            BRENDA, the Enzyme Database: 2.7.7.47
            CAS: 52660-23-8
///
ENTRY       EC 2.7.7.48                 Enzyme
NAME        RNA-directed RNA polymerase;
            RNA nucleotidyltransferase (RNA-directed);
            RNA nucleotidyltransferase (RNA-directed);
            RNA-dependent ribonucleate nucleotidyltransferase;
            3D polymerase;
            PB1 proteins;
            PB2 proteins;
            phage f2 replicase;
            polymerase L;
            Q-beta replicase;
            phage f2 replicase;
            ribonucleic acid replicase;
            ribonucleic acid-dependent ribonucleate nucleotidyltransferase;
            ribonucleic acid-dependent ribonucleic acid polymerase;
            ribonucleic replicase;
            ribonucleic synthetase;
            RNA replicase;
            RNA synthetase;
            RNA transcriptase;
            RNA-dependent ribonucleate nucleotidyltransferase;
            RDRP;
            RNA-dependent RNA polymerase;
            RNA-dependent RNA replicase;
            transcriptase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     nucleoside-triphosphate:RNA nucleotidyltransferase (RNA-directed)
REACTION    nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444]
ALL_REAC    R00444 > R00435
SUBSTRATE   nucleoside triphosphate [CPD:C00201];
            RNAn [CPD:C00046]
PRODUCT     diphosphate [CPD:C00013];
            RNAn+1 [CPD:C00046]
COMMENT     Catalyses RNA-template-directed extension of the 3'- end of an RNA
            strand by one nucleotide at a time. Can initiate a chain de novo.
            See also EC 2.7.7.6 DNA-directed RNA polymerase.
REFERENCE   1
  AUTHORS   August, J.T., Cooper, S., Shapiro, L. and Zinder, N.D.
  TITLE     RNA phage induced RNA polymerase.
  JOURNAL   Cold Spring Harbour Symp. Quant. Biol. 28 (1963) 95-97.
REFERENCE   2
  AUTHORS   Haruna, J., Nozu, K., Ohtaka, Y. and Spiegelman, S.
  TITLE     An RNA "Replicase" induced by and selective for a viral RNA:
            isolation and properties.
  JOURNAL   Proc. Natl. Acad. Sci. USA 50 (1963) 905-911.
REFERENCE   3
  AUTHORS   Weismann, C., Simon, L. and Ochoa, S.
  TITLE     Induction by an RNA phage of an enzyme catalyzing incorporation of
            ribonucleotides into ribonucleic acid.
  JOURNAL   Proc. Natl. Acad. Sci. USA 49 (1963) 407-414.
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K00985  RNA-directed RNA polymerase
GENES       AFM: AFUA_3G06790 AFUA_5G09430
            BUR: Bcep18194_A6181
STRUCTURES  PDB: 1C2P  1CSJ  1EZJ  1GX5  1GX6  1HAV  1KHV  1KHW  1L9K  1N64  
                 1NB4  1NB6  1NB7  1NHU  1NHV  1OKS  1QUV  1R4G  1R6A  1RA6  
                 1RA7  1RAJ  1RDR  1SH0  1SH2  1SH3  1TP7  1TQL  1U09  1UTY  
                 1VYI  1WNE  1XR5  1XR6  1XR7  1YN6  1YN7  1YVF  1Z4U  2AWZ  
                 2AX0  2AX1  2BRK  2BRL  2CJQ  2CKW  2D3U  2D3Z  2D41  2D7S  
                 2DXS  2E9R  2E9T  2E9Z  2EC0  2F8E  2GC8  2GIQ  2GIR  2HAI  
                 2HCS  2HFZ  2HWH  2HWI  2I1R  2IJD  2IJF  2IJN  2ILY  2ILZ  
                 2IM0  2IM1  2IM2  2IM3  2O5D  2P1D  2P3L  2P3O  2P3Q  2P40  
                 2P41  2PGG  2PX2  2PX4  2PX5  2PX8  2PXA  2PXC  2QE2  2QE5  
                 2UUT  2UUW  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.48
            ExPASy - ENZYME nomenclature database: 2.7.7.48
            ExplorEnz - The Enzyme Database: 2.7.7.48
            ERGO genome analysis and discovery system: 2.7.7.48
            BRENDA, the Enzyme Database: 2.7.7.48
            CAS: 9026-28-2
///
ENTRY       EC 2.7.7.49                 Enzyme
NAME        RNA-directed DNA polymerase;
            DNA nucleotidyltransferase (RNA-directed);
            reverse transcriptase;
            revertase;
            RNA-dependent deoxyribonucleate nucleotidyltransferase;
            RNA revertase;
            RNA-dependent DNA polymerase;
            RNA-instructed DNA polymerase;
            RT
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     deoxynucleoside-triphosphate:DNA deoxynucleotidyltransferase
            (RNA-directed)
REACTION    deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1
            [RN:R00379]
ALL_REAC    R00379
SUBSTRATE   deoxynucleoside triphosphate [CPD:C00677];
            DNAn [CPD:C00039]
PRODUCT     diphosphate [CPD:C00013];
            DNAn+1 [CPD:C00039]
COMMENT     Catalyses RNA-template-directed extension of the 3'- end of a DNA
            strand by one deoxynucleotide at a time. Cannot initiate a chain de
            novo. Requires an RNA or DNA primer. DNA can also serve as template.
            See also EC 2.7.7.7 DNA-directed DNA polymerase.
REFERENCE   1  [PMID:4316300]
  AUTHORS   Baltimore D.
  TITLE     RNA-dependent DNA polymerase in virions of RNA tumour viruses.
  JOURNAL   Nature. 226 (1970) 1209-11.
REFERENCE   2  [PMID:4316301]
  AUTHORS   Temin HM, Mizutani S.
  TITLE     RNA-dependent DNA polymerase in virions of Rous sarcoma virus.
  JOURNAL   Nature. 226 (1970) 1211-3.
  ORGANISM  Rous sarcoma virus
ORTHOLOGY   KO: K00986  RNA-directed DNA polymerase
GENES       PIC: PICST_28003(POL5.8) PICST_31695(POL5.7) PICST_32752(POL5.6)
            XCC: XCC3626
            XCB: XC_0589
            VCH: VC2385
            VCO: VC0395_A1962
            VFI: VF1044
            PAU: PA14_07480
            SFR: Sfri_3486
            SBL: Sbal_2317
            SSE: Ssed_1438 Ssed_2561 Ssed_2712
            SHE: Shewmr4_2118
            SHM: Shewmr7_0556
            ABO: ABO_0635
            REH: H16_A2488
            RME: Rmet_0253 Rmet_2883
            BUR: Bcep18194_C7580
            POL: Bpro_0949 Bpro_4601 Bpro_4617 Bpro_4899 Bpro_5394
            AJS: Ajs_2219
            HAR: HEAR0998
            GSU: GSU1363
            SAT: SYN_02976
            OAN: Oant_4498 Oant_4626
            BBT: BBta_4614 BBta_6534
            NWI: Nwi_0254 Nwi_0782 Nwi_0838 Nwi_0865 Nwi_0870 Nwi_0872
                 Nwi_1018 Nwi_1143 Nwi_1293 Nwi_2665
            NHA: Nham_3886
            NAR: Saro_2196
            SWI: Swit_4971
            MGM: Mmc1_1986 Mmc1_2705
            SUS: Acid_2554
            BCZ: pE33L466_0196
            BCY: Bcer98_3169
            SPI: MGAS10750_Spy1709
            SPA: M6_Spy0158
            CBE: Cbei_0694
            MVA: Mvan_2212
            RHA: RHA1_ro00799 RHA1_ro08026 RHA1_ro10191
            FRA: Francci3_2197 Francci3_2318
            STP: Strop_4139
            FNU: FN0161
            RBA: RB818
            AVA: Ava_3254 Ava_B0014 Ava_C0033
            BFS: BF2112
            PVI: Cvib_0153
            PLT: Plut_0650 Plut_1820
            MAC: MA3645
            MMA: MM_2683 MM_2695 MM_2698
            MBU: Mbur_0690 Mbur_0765 Mbur_2004 Mbur_2039
            MHU: Mhun_1207 Mhun_1335 Mhun_2134 Mhun_2646 Mhun_2784 Mhun_3124
STRUCTURES  PDB: 1A5V  1A5W  1A5X  1B92  1B9D  1B9F  1BHL  1BQM  1BQN  1C0M  
                 1C0T  1C0U  1C1A  1C1B  1C1C  1D0E  1DLO  1EET  1EP4  1FK9  
                 1FKO  1FKP  1GNM  1GNN  1GNO  1HAR  1HMV  1HNI  1HNV  1HPZ  
                 1HQE  1HQU  1HVU  1HYS  1HYV  1HYZ  1I6J  1IKV  1IKW  1IKX  
                 1IKY  1J5O  1JKH  1JLA  1JLB  1JLC  1JLE  1JLF  1JLG  1JLQ  
                 1K6Y  1KLM  1LW0  1LW2  1LWC  1LWE  1LWF  1MU2  1N4L  1N5Y  
                 1N6Q  1NND  1Q94  1QAI  1QAJ  1QE1  1QS4  1R0A  1RDH  1REV  
                 1RT1  1RT2  1RT3  1RT4  1RT5  1RT6  1RT7  1RTD  1RTH  1RTI  
                 1RTJ  1RW3  1S1T  1S1U  1S1V  1S1W  1S1X  1S6P  1S6Q  1S9E  
                 1S9G  1SUQ  1SV5  1T03  1T05  1TKT  1TKX  1TKZ  1TL1  1TL3  
                 1TVR  1UWB  1VRT  1VRU  1VSK  1VSM  1ZTT  1ZTW  2B2A  2B5J  
                 2B6A  2BAN  2BCK  2BE2  2FJV  2FJW  2FJX  2FVP  2FVQ  2FVR  
                 2FVS  2HMI  2HND  2HNY  2HNZ  2I5J  2IAJ  2IC3  2OPP  2OPQ  
                 2OPR  2OPS  3HVT  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.49
            ExPASy - ENZYME nomenclature database: 2.7.7.49
            ExplorEnz - The Enzyme Database: 2.7.7.49
            ERGO genome analysis and discovery system: 2.7.7.49
            BRENDA, the Enzyme Database: 2.7.7.49
            CAS: 9068-38-6
///
ENTRY       EC 2.7.7.50                 Enzyme
NAME        mRNA guanylyltransferase;
            mRNA capping enzyme;
            messenger RNA guanylyltransferase;
            Protein 2
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     GTP:mRNA guanylyltransferase
REACTION    GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA [RN:R03828]
ALL_REAC    R03828
SUBSTRATE   GTP [CPD:C00044];
            (5')ppPur-mRNA [CPD:C02100]
PRODUCT     diphosphate [CPD:C00013];
            G(5')pppPur-mRNA [CPD:C02407]
COMMENT     The enzyme can also modify synthetic poly(A) and poly(G) to form the
            structures m7G(5')pppAn and m7G(5')pppGn.
REFERENCE   1  [PMID:1058472]
  AUTHORS   Ensinger MJ, Martin SA, Paoletti E, Moss B.
  TITLE     Modification of the 5'-terminus of mRNA by soluble guanylyl and
            methyl transferases from vaccinia virus.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 72 (1975) 2525-9.
  ORGANISM  Vaccinia virus
REFERENCE   2  [PMID:629955]
  AUTHORS   Groner Y, Gilboa E, Aviv H.
  TITLE     Methylation and capping of RNA polymerase II primary transcripts by
            HeLa nuclear homogenates.
  JOURNAL   Biochemistry. 17 (1978) 977-82.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:3029058]
  AUTHORS   Itoh N, Yamada H, Kaziro Y, Mizumoto K.
  TITLE     Messenger RNA guanylyltransferase from Saccharomyces cerevisiae.
            Large scale purification, subunit functions, and subcellular
            localization.
  JOURNAL   J. Biol. Chem. 262 (1987) 1989-95.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4  [PMID:1194287]
  AUTHORS   Martin SA, Moss B.
  TITLE     Modification of RNA by mRNA guanylyltransferase and mRNA
            (guanine-7-)methyltransferase from vaccinia virions.
  JOURNAL   J. Biol. Chem. 250 (1975) 9330-5.
  ORGANISM  Vaccinia virus
REFERENCE   5  [PMID:1194286]
  AUTHORS   Martin SA, Paoletti E, Moss B.
  TITLE     Purification of mRNA guanylyltransferase and mRNA (guanine-7-)
            methyltransferase from vaccinia virions.
  JOURNAL   J. Biol. Chem. 250 (1975) 9322-9.
  ORGANISM  Vaccinia virus
ORTHOLOGY   KO: K00987  mRNA guanylyltransferase
GENES       HSA: 8732(RNGTT)
            PTR: 462878(RNGTT)
            MMU: 24018(Rngtt)
            RNO: 313131(Rngtt_predicted)
            CFA: 481914(RNGTT)
            BTA: 511408(LOC511408)
            GGA: 421819(RNGTT)
            XTR: 407900(rngtt)
            DME: Dmel_CG1810
            CME: CMA035C
            SCE: YGL130W(CEG1)
            AGO: AGOS_AFL107W
            PIC: PICST_34053(CEG1)
            CGR: CAGL0I09570g
            SPO: SPBC2F12.08c(ceg1)
            ANI: AN7473.2
            AFM: AFUA_2G05780
            AOR: AO090001000697
            CNE: CNB01130
            UMA: UM04881.1
            ECU: ECU09_0400
            DDI: DDBDRAFT_0188303
            PFA: PF14_0144
            CPV: cgd6_2380
            CHO: Chro.60277
            TAN: TA12700
            TPV: TP02_0352
            TET: TTHERM_00760200
            EHI: 128.t00009
STRUCTURES  PDB: 1CKM  1CKN  1CKO  1P16  2C46  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.50
            ExPASy - ENZYME nomenclature database: 2.7.7.50
            ExplorEnz - The Enzyme Database: 2.7.7.50
            ERGO genome analysis and discovery system: 2.7.7.50
            BRENDA, the Enzyme Database: 2.7.7.50
            CAS: 56941-23-2
///
ENTRY       EC 2.7.7.51                 Enzyme
NAME        adenylylsulfate---ammonia adenylyltransferase;
            APSAT;
            adenylylsulfate:ammonia adenylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     adenylyl-sulfate:ammonia adenylyltransferase
REACTION    adenylyl sulfate + NH3 = adenosine 5'-phosphoramidate + sulfate
            [RN:R01619]
ALL_REAC    R01619
SUBSTRATE   adenylyl sulfate [CPD:C00224];
            NH3 [CPD:C00014]
PRODUCT     adenosine 5'-phosphoramidate [CPD:C03851];
            sulfate [CPD:C00059]
REFERENCE   1
  AUTHORS   Fankhauser, H., Garber, L. and Schiff, J.A.
  TITLE     Adenylyl sulfate (APS):ammonia adenylyl transferase (APSAT) forming
            adenosine 5' phosphoramidate (APA) from APS and ammonia.
  JOURNAL   Plant Physiol. 63S (1979) 162.
REFERENCE   2
  AUTHORS   Fankhauser, H. and Schiff, J.A.
  TITLE     Further purification and properties of adenylyl sulfate (APS):
            ammonia adenylyl transferase (APSAT) from Chlorella.
  JOURNAL   Plant Physiol. 65S (1980) 17.
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.51
            ExPASy - ENZYME nomenclature database: 2.7.7.51
            ExplorEnz - The Enzyme Database: 2.7.7.51
            ERGO genome analysis and discovery system: 2.7.7.51
            BRENDA, the Enzyme Database: 2.7.7.51
            CAS: 79121-94-1
///
ENTRY       EC 2.7.7.52                 Enzyme
NAME        RNA uridylyltransferase;
            terminal uridylyltransferase;
            TUT
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     UTP:RNA uridylyltransferase
REACTION    UTP + RNAn = diphosphate + RNAn+1 [RN:R00443]
ALL_REAC    R00443
SUBSTRATE   UTP [CPD:C00075];
            RNAn [CPD:C00046]
PRODUCT     diphosphate [CPD:C00013];
            RNAn+1 [CPD:C00046]
COMMENT     The enzyme requires an oligoribonucleotide or polyribonucleotide
            with a free terminal 3'-OH as a primer.
REFERENCE   1  [PMID:6269049]
  AUTHORS   Zabel P, Dorssers L, Wernars K, Van Kammen A.
  TITLE     Terminal uridylyl transferase of Vigna unguiculata: purification and
            characterization of an enzyme catalyzing the addition of a single
            UMP residue to the 3'-end of an RNA primer.
  JOURNAL   Nucleic. Acids. Res. 9 (1981) 2433-53.
  ORGANISM  Vigna unguiculata
STRUCTURES  PDB: 2E5G  2IKF  2NOM  2Q0C  2Q0D  2Q0E  2Q0F  2Q0G  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.52
            ExPASy - ENZYME nomenclature database: 2.7.7.52
            ExplorEnz - The Enzyme Database: 2.7.7.52
            ERGO genome analysis and discovery system: 2.7.7.52
            BRENDA, the Enzyme Database: 2.7.7.52
            CAS: 78519-53-6
///
ENTRY       EC 2.7.7.53                 Enzyme
NAME        ATP adenylyltransferase;
            bis(5'-nucleosyl)-tetraphosphate phosphorylase (NDP-forming);
            diadenosinetetraphosphate alphabeta-phosphorylase;
            adenine triphosphate adenylyltransferase;
            diadenosine 5',5'"-P1,P4-tetraphosphate alphabeta-phosphorylase
            (ADP-forming);
            dinucleoside oligophosphate alphabeta-phosphorylase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ADP:ATP adenylyltransferase
REACTION    ADP + ATP = phosphate + P1,P4-bis(5'-adenosyl) tetraphosphate
            [RN:R00126]
ALL_REAC    R00126;
            (other) R01618
SUBSTRATE   ADP [CPD:C00008];
            ATP [CPD:C00002]
PRODUCT     phosphate [CPD:C00009];
            P1,P4-bis(5'-adenosyl) tetraphosphate [CPD:C01260]
COMMENT     GTP and adenosine tetraphosphate can also act as adenylyl acceptors.
REFERENCE   1  [PMID:2982863]
  AUTHORS   Guranowski A, Blanquet S.
  TITLE     Phosphorolytic cleavage of diadenosine 5',5'''-P1,P4-tetraphosphate.
            Properties of homogeneous diadenosine 5',5'''-P1,P4-tetraphosphate
            alpha, beta-phosphorylase from Saccharomyces cerevisiae.
  JOURNAL   J. Biol. Chem. 260 (1985) 3542-7.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K00988  ATP adenylyltransferase
GENES       SCE: YCL050C(APA1) YDR530C(APA2)
            PIC: PICST_48616(APA2)
            ANI: AN5855.2
            AFM: AFUA_5G14690
            UMA: UM03318.1
            PPR: PBPRA1434
            HCH: HCH_06654
            REH: H16_A1656
            EBA: ebA5257
            SYN: sll0509
            SYW: SYNW1233
            SYC: syc0057_d
            SYF: Synpcc7942_1600
            SYD: Syncc9605_1349
            SYE: Syncc9902_1129
            SYG: sync_1346
            SYR: SynRCC307_1217
            SYX: SynWH7803_1283
            ANA: alr4466
            AVA: Ava_3329
            PMA: Pro0961(APA2)
            PMM: PMM0874
            PMT: PMT0732
            PMN: PMN2A_0335
            PMI: PMT9312_0926
            PMB: A9601_09871(apa2)
            PMC: P9515_09561(apa2)
            PMF: P9303_14851(apa2)
            PMG: P9301_09851(apa2)
            PME: NATL1_10081(apa2)
            TER: Tery_0108
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.53
            ExPASy - ENZYME nomenclature database: 2.7.7.53
            ExplorEnz - The Enzyme Database: 2.7.7.53
            ERGO genome analysis and discovery system: 2.7.7.53
            BRENDA, the Enzyme Database: 2.7.7.53
            CAS: 96697-71-1
///
ENTRY       EC 2.7.7.54                 Enzyme
NAME        phenylalanine adenylyltransferase;
            L-phenylalanine adenylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ATP:L-phenylalanine adenylyltransferase
REACTION    ATP + L-phenylalanine = diphosphate + N-adenylyl-L-phenylalanine
            [RN:R00687]
ALL_REAC    R00687
SUBSTRATE   ATP [CPD:C00002];
            L-phenylalanine [CPD:C00079]
PRODUCT     diphosphate [CPD:C00013];
            N-adenylyl-L-phenylalanine [CPD:C03709]
COMMENT     Part of the system for biosynthesis of the alkaloid cyclopeptine in
            Penicillium cyclopium.
REFERENCE   1  [PMID:2995633]
  AUTHORS   Lerbs W, Luckner M.
  TITLE     Cyclopeptine synthetase activity in surface cultures of Penicillium
            cyclopium.
  JOURNAL   J. Basic. Microbiol. 25 (1985) 387-91.
  ORGANISM  Penicillium cyclopium
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.54
            ExPASy - ENZYME nomenclature database: 2.7.7.54
            ExplorEnz - The Enzyme Database: 2.7.7.54
            ERGO genome analysis and discovery system: 2.7.7.54
            BRENDA, the Enzyme Database: 2.7.7.54
            CAS: 98285-55-3
///
ENTRY       EC 2.7.7.55                 Enzyme
NAME        anthranilate adenylyltransferase;
            anthranilic acid adenylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ATP:anthranilate N-adenylyltransferase
REACTION    ATP + anthranilate = diphosphate + N-adenylylanthranilate
            [RN:R00979]
ALL_REAC    R00979
SUBSTRATE   ATP [CPD:C00002];
            anthranilate [CPD:C00108]
PRODUCT     diphosphate [CPD:C00013];
            N-adenylylanthranilate [CPD:C03293]
COMMENT     Part of the system for biosynthesis of the alkaloid cyclopeptine in
            Penicillium cyclopium.
REFERENCE   1  [PMID:2995633]
  AUTHORS   Lerbs W, Luckner M.
  TITLE     Cyclopeptine synthetase activity in surface cultures of Penicillium
            cyclopium.
  JOURNAL   J. Basic. Microbiol. 25 (1985) 387-91.
  ORGANISM  Penicillium cyclopium
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.55
            ExPASy - ENZYME nomenclature database: 2.7.7.55
            ExplorEnz - The Enzyme Database: 2.7.7.55
            ERGO genome analysis and discovery system: 2.7.7.55
            BRENDA, the Enzyme Database: 2.7.7.55
            CAS: 70248-64-5
///
ENTRY       EC 2.7.7.56                 Enzyme
NAME        tRNA nucleotidyltransferase;
            phosphate-dependent exonuclease;
            RNase PH;
            ribonuclease PH
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     tRNA:phosphate nucleotidyltransferase
REACTION    tRNAn+1 + phosphate = tRNAn + a nucleoside diphosphate [RN:R07285]
ALL_REAC    R07285
SUBSTRATE   tRNA(n+1) [CPD:C00066];
            phosphate [CPD:C00009]
PRODUCT     tRNA(n) [CPD:C00066];
            nucleoside diphosphate [CPD:C00454]
COMMENT     Brings about the final exonucleolytic trimming of the 3'-terminus of
            tRNA precursors in Escherichia coli by a phosphorolysis, producing a
            mature 3'-terminus on tRNA and nucleoside diphosphate. Not identical
            with EC 2.7.7.8 polyribonucleotide nucleotidyltransferase.
REFERENCE   1  [PMID:3275667]
  AUTHORS   Cudny H, Deutscher MP.
  TITLE     3' processing of tRNA precursors in ribonuclease-deficient
            Escherichia coli. Development and characterization of an in vitro
            processing system and evidence for a phosphate requirement.
  JOURNAL   J. Biol. Chem. 263 (1988) 1518-23.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:2455297]
  AUTHORS   Deutscher MP, Marshall GT, Cudny H.
  TITLE     RNase PH: an Escherichia coli phosphate-dependent nuclease distinct
            from polynucleotide phosphorylase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 4710-4.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K00989  ribonuclease PH
GENES       PIC: PICST_57180(MTR3)
            ECJ: JW3618(rph)
            ECE: Z5068(rph)
            ECS: ECs4518
            ECC: c4467(rph)
            ECI: UTI89_C4187(rph)
            ECP: ECP_3741
            ECV: APECO1_2818(rph)
            ECW: EcE24377A_4144(rph)
            ECX: EcHS_A3852(rph)
            STY: STY4060(rph)
            STT: t3784(rph)
            SPT: SPA3586(rph)
            SEC: SC3657(rph)
            STM: STM3734(rph)
            YPE: YPO0044(rph)
            YPK: y0097(rph)
            YPM: YP_0045(rph)
            YPA: YPA_3498
            YPN: YPN_3806
            YPP: YPDSF_3861
            YPS: YPTB0041(rph)
            YPI: YpsIP31758_0056(rph)
            YEN: YE0058(rph)
            SFL: SF3682(rph)
            SFX: S4086(rph)
            SFV: SFV_3887(rph)
            SSN: SSON_3763(rph)
            SBO: SBO_3645(rph)
            SDY: SDY_4074(rph)
            ECA: ECA0140(rph)
            PLU: plu4870(rph)
            SGL: SG2213
            ENT: Ent638_0096
            SPE: Spro_4847
            HIN: HI0273(rph)
            HIT: NTHI0381(rph)
            HIP: CGSHiEE_01685(rph)
            HDU: HD0301(rph)
            HSO: HS_1292(rph)
            PMU: PM1876(rph)
            MSU: MS0252(rph)
            APL: APL_0055(rph)
            ASU: Asuc_0420
            XFA: XF1505
            XFT: PD0722(rph)
            XCC: XCC3251(rph)
            XCB: XC_0960
            XCV: XCV3514(rph)
            XAC: XAC3397(rph)
            XOO: XOO1143(rph)
            XOM: XOO_1040(XOO1040)
            VCH: VC0210
            VCO: VC0395_A2589(rph)
            VVU: VV1_0832
            VVY: VV0279
            VPA: VP0177
            VFI: VF0111
            PPR: PBPRA0198
            PAE: PA5334(rph)
            PAU: PA14_70420(rph)
            PAP: PSPA7_6110(rph)
            PPU: PP_5294(rph)
            PPF: Pput_5202
            PST: PSPTO_0077(rph)
            PSB: Psyr_0213(rph)
            PSP: PSPPH_0201(rph)
            PFL: PFL_6059(rph)
            PFO: Pfl_5547(rph)
            PEN: PSEEN5439(rph)
            PMY: Pmen_4386
            PAR: Psyc_1865(rph)
            PCR: Pcryo_2154
            PRW: PsycPRwf_2191
            ACI: ACIAD0050(rph)
            SON: SO_4256(rph)
            SDN: Sden_0319
            SFR: Sfri_3836
            SAZ: Sama_0320
            SBL: Sbal_0370
            SBM: Shew185_0369
            SLO: Shew_3488
            SPC: Sputcn32_0456
            SSE: Ssed_0378
            SPL: Spea_3844
            SHE: Shewmr4_3604
            SHM: Shewmr7_0352
            SHN: Shewana3_3777
            SHW: Sputw3181_0332
            ILO: IL2425(rph)
            CPS: CPS_0112(rph)
            PHA: PSHAa2788(rph)
            PAT: Patl_4282
            SDE: Sde_3683
            PIN: Ping_3479
            MAQ: Maqu_0548
            CBU: CBU_0299(rph)
            CBD: COXBU7E912_1782(rph)
            LPN: lpg2012(rph)
            LPF: lpl1989(rph)
            LPP: lpp1994(rph)
            MCA: MCA3024(rph)
            FTU: FTT0858(rph)
            FTF: FTF0858(rph)
            FTW: FTW_1326(rph)
            FTL: FTL_0357
            FTH: FTH_0352(rph)
            FTA: FTA_0378(rph)
            FTN: FTN_0387
            NOC: Noc_2442
            AEH: Mlg_2446
            HHA: Hhal_0973
            HCH: HCH_06338(rph)
            CSA: Csal_3206
            ABO: ABO_0206(rph)
            MMW: Mmwyl1_4361
            AHA: AHA_4224(rph)
            DNO: DNO_0664(rph)
            NME: NMB1499
            NMA: NMA1702(rph)
            NMC: NMC1430(rph)
            NGO: NGO0958
            CVI: CV_3847(rph)
            RSO: RSc2159(rph)
            REU: Reut_A2477(rph)
            REH: H16_A0949
            RME: Rmet_0852
            BMA: BMA2098(rph)
            BMV: BMASAVP1_A0813(rph)
            BML: BMA10299_A2646(rph)
            BMN: BMA10247_1966(rph)
            BXE: Bxe_A0903
            BVI: Bcep1808_0914
            BUR: Bcep18194_A4105(rph)
            BCN: Bcen_0518
            BCH: Bcen2424_0997
            BAM: Bamb_0857
            BPS: BPSL2565(rph)
            BPM: BURPS1710b_3051(rph)
            BPL: BURPS1106A_3017(rph)
            BPD: BURPS668_2951(rph)
            BTE: BTH_I1584(rph)
            PNU: Pnuc_1080
            BPE: BP1588(rph)
            BPA: BPP2995(rph)
            BBR: BB2961(rph)
            RFR: Rfer_1629
            POL: Bpro_1339
            AAV: Aave_3579
            AJS: Ajs_0923
            MPT: Mpe_A2705
            HAR: HEAR2126(rph)
            MMS: mma_1332(rph)
            NEU: NE0276(rph)
            NET: Neut_0308
            NMU: Nmul_A0066
            EBA: c1A232(rph)
            AZO: azo3963(rph)
            DAR: Daro_3851
            TBD: Tbd_0477
            MFA: Mfla_0043
            GSU: GSU1795(rph)
            GME: Gmet_1876
            GUR: Gura_2256
            PCA: Pcar_2030
            PPD: Ppro_2311
            BBA: Bd2700(rph)
            DPS: DP1273
            ADE: Adeh_3361
            AFW: Anae109_3425
            MXA: MXAN_2004(rph)
            SAT: SYN_00902
            RPR: RP628(rph)
            RTY: RT0619(rph)
            RCO: RC0975(rph)
            RFE: RF_0403(rph)
            RBE: RBE_0607(rph)
            RAK: A1C_04950(rph)
            RBO: A1I_03465(rph)
            RCM: A1E_01610(rph)
            RRI: A1G_05365(rph)
            OTS: OTBS_0260(rph)
            MLO: mlr4622
            MES: Meso_4016
            PLA: Plav_3580
            SME: SMc01144(rph)
            SMD: Smed_0010
            ATU: Atu0327(rph)
            ATC: AGR_C_571(rph)
            RET: RHE_CH00363(rph)
            RLE: RL0380(rph)
            BME: BMEI1775
            BMF: BAB1_0172(rph)
            BMS: BR0173(rph)
            BMB: BruAb1_0169(rph)
            BOV: BOV_0167(rph)
            OAN: Oant_0182
            BJA: bll0674(rph)
            BRA: BRADO0173(rph)
            BBT: BBta_0186(rph)
            RPA: RPA0329(rph)
            RPB: RPB_0425
            RPC: RPC_0325
            RPD: RPD_0395
            RPE: RPE_0353
            NWI: Nwi_0193(rph)
            NHA: Nham_0151
            XAU: Xaut_2535
            CCR: CC_0152
            SIL: SPO0008(rph)
            SIT: TM1040_2872
            RSP: RSP_1221(rph)
            RSH: Rsph17029_2882
            RSQ: Rsph17025_2658
            JAN: Jann_0206
            RDE: RD1_0426(rph)
            PDE: Pden_0010
            MMR: Mmar10_3006
            HNE: HNE_3315(rph)
            ZMO: ZMO0014(rph)
            NAR: Saro_2061
            SAL: Sala_0254
            SWI: Swit_0567
            ELI: ELI_06010
            GOX: GOX1282
            GBE: GbCGDNIH1_0025
            ACR: Acry_1664
            RRU: Rru_A3641
            MAG: amb4498
            MGM: Mmc1_0051
            ABA: Acid345_1616
            SUS: Acid_7723
            BSU: BG10357(rph)
            BHA: BH3068(rph)
            BAN: BA4715(rph)
            BAR: GBAA4715(rph)
            BAA: BA_5149
            BAT: BAS4377
            BCE: BC4494(rph)
            BCA: BCE_4586(rph)
            BCZ: BCZK4234(rph)
            BCY: Bcer98_3202
            BTK: BT9727_4218(rph)
            BTL: BALH_4073(rph)
            BLI: BL00312(rph)
            BLD: BLi02985(rph)
            BCL: ABC2652(rph)
            BAY: RBAM_025440(rph)
            BPU: BPUM_2491(rph)
            OIH: OB2106(rph)
            GKA: GK2666(rph)
            LMO: lmo1238
            LMF: LMOf2365_1247(rph)
            LIN: lin1201
            LWE: lwe1193(rph)
            EFA: EF1122(rph)
            STH: STH343
            CPE: CPE2254(rnpH)
            CPF: CPF_2536(rph)
            CPR: CPR_2240(rph)
            CTH: Cthe_0188
            CDF: CD3308(rph)
            CKL: CKL_3464(rph)
            AMT: Amet_0956
            CHY: CHY_0314(rph)
            DSY: DSY3222
            DRM: Dred_2684
            SWO: Swol_0453
            CSC: Csac_0985
            TTE: TTE0618(rph)
            MTA: Moth_0519
            MTU: Rv1340(rph)
            MTC: MT1381(rph)
            MBO: Mb1375(rph)
            MBB: BCG_1402(rphA)
            MLE: ML1174(rphA)
            MPA: MAP2422c(rphA)
            MAV: MAV_1557(rph)
            MSM: MSMEG_4901(rph)
            MVA: Mvan_4287
            MGI: Mflv_2358
            MMC: Mmcs_3844
            MKM: Mkms_3918
            MJL: Mjls_3830
            CGL: NCgl2415(rph)
            CGB: cg2753(rph)
            CEF: CE2401
            CDI: DIP1851(rph)
            CJK: jk0498(rphA)
            NFA: nfa10950(rph)
            RHA: RHA1_ro01433
            SCO: SCO2904(rph)
            SMA: SAV5170(rphA)
            TWH: TWT622(rph)
            TWS: TW640(rph)
            LXX: Lxx13580(rph)
            CMI: CMM_1295(rphA)
            ART: Arth_2581
            AAU: AAur_2570(rph)
            PAC: PPA1674(rph)
            NCA: Noca_1323
            TFU: Tfu_2365(rph)
            FRA: Francci3_0870
            FAL: FRAAL1503(rph)
            ACE: Acel_1684
            KRA: Krad_3763
            SEN: SACE_1212(rph)
            STP: Strop_1104
            BLO: BL0286
            FNU: FN1851
            RBA: RB5725(rph)
            SYW: SYNW0276(rph)
            SYC: syc0476_c
            SYF: Synpcc7942_1073
            SYD: Syncc9605_0270
            SYE: Syncc9902_2074
            SYG: sync_0317(rph)
            SYX: SynWH7803_0320(rph)
            CYA: CYA_2643(rph)
            CYB: CYB_1741(rph)
            TEL: tlr0592
            ANA: alr0069
            AVA: Ava_2671(rph)
            PMT: PMT1830(rph)
            PMF: P9303_24551(rph)
            TER: Tery_2089
            DET: DET1289(rph)
            DEH: cbdb_A1225(rph)
            DEB: DehaBAV1_1100
            RRS: RoseRS_2001
            RCA: Rcas_3937
            DRA: DR_1585
            DGE: Dgeo_2086
            AAE: aq_924(rnpH)
            MBA: Mbar_A2506
            MMA: MM_2623
            MBU: Mbur_0199
            MST: Msp_1251
            MSI: Msm_0242
            MKA: MK0381(rph)
            TAC: Ta1293
            TVO: TVN0307
            PTO: PTO0393 PTO0394
            PAB: PAB0420(rph)
            PFU: PF1568
            TKO: TK1634
            APE: APE_1447
            HBU: Hbut_0571
            SSO: SSO0735(rph)
            STO: ST0443
            SAI: Saci_0610(rph)
            PAI: PAE2207
            NEQ: NEQ248
STRUCTURES  PDB: 1OYP  1OYR  1OYS  1R6L  1R6M  1UDN  1UDO  1UDQ  1UDS  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.56
            ExPASy - ENZYME nomenclature database: 2.7.7.56
            ExplorEnz - The Enzyme Database: 2.7.7.56
            ERGO genome analysis and discovery system: 2.7.7.56
            BRENDA, the Enzyme Database: 2.7.7.56
            CAS: 116412-36-3
///
ENTRY       EC 2.7.7.57                 Enzyme
NAME        N-methylphosphoethanolamine cytidylyltransferase;
            monomethylethanolamine phosphate cytidylyltransferase;
            CTP:P-MEA cytidylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     CTP:N-methylethanolamine-phosphate cytidylyltransferase
REACTION    CTP + N-methylethanolamine phosphate = diphosphate +
            CDP-N-methylethanolamine [RN:R03375]
ALL_REAC    R03375
SUBSTRATE   CTP [CPD:C00063];
            N-methylethanolamine phosphate [CPD:C01210]
PRODUCT     diphosphate [CPD:C00013];
            CDP-N-methylethanolamine [CPD:C03486]
REFERENCE   1
  AUTHORS   Datko, A.H. and Mudd, S.H.
  TITLE     Enzymes of phosphatidylcholine synthesis in Lemna, soybean, and
            carrot.
  JOURNAL   Plant Physiol. 88 (1988) 1338-1348.
  ORGANISM  Daucus carota, Glycine max [GN:egma], Lemma paucicostata
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.57
            ExPASy - ENZYME nomenclature database: 2.7.7.57
            ExplorEnz - The Enzyme Database: 2.7.7.57
            ERGO genome analysis and discovery system: 2.7.7.57
            BRENDA, the Enzyme Database: 2.7.7.57
            CAS: 119345-28-7
///
ENTRY       EC 2.7.7.58                 Enzyme
NAME        (2,3-dihydroxybenzoyl)adenylate synthase;
            2,3-dihydroxybenzoate-AMP ligase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ATP:2,3-dihydroxybenzoate adenylyltransferase
REACTION    ATP + 2,3-dihydroxybenzoate = diphosphate +
            (2,3-dihydroxybenzoyl)adenylate [RN:R01504]
ALL_REAC    R01504
SUBSTRATE   ATP [CPD:C00002];
            2,3-dihydroxybenzoate [CPD:C00196]
PRODUCT     diphosphate [CPD:C00013];
            (2,3-dihydroxybenzoyl)adenylate [CPD:C04030]
REFERENCE   1  [PMID:2531000]
  AUTHORS   Rusnak F, Faraci WS, Walsh CT.
  TITLE     Subcloning, expression, and purification of the enterobactin
            biosynthetic enzyme 2,3-dihydroxybenzoate-AMP ligase: demonstration
            of enzyme-bound (2,3-dihydroxybenzoyl)adenylate product.
  JOURNAL   Biochemistry. 28 (1989) 6827-35.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map01053  Biosynthesis of siderophore group nonribosomal
                            peptides
ORTHOLOGY   KO: K02312  2,3-dihydroxybenzoate-AMP ligase
            KO: K02363  enterobactin 2,3-dihydroxybenzoate-AMP ligase /
                        S-dihydroxybenzoyltransferase
            KO: K04776  vibriobactin-specific 2,3-dihydroxybenzoate-AMP ligase
GENES       ECO: b0594(entE)
            ECJ: JW0586(entE)
            ECE: Z0736(entE)
            ECS: ECs0633
            ECC: c0681(entE)
            ECI: UTI89_C0596(entE)
            ECP: ECP_0626
            ECV: APECO1_1455(entE)
            ECW: EcE24377A_0614(entE)
            ECX: EcHS_A0645(entE)
            STY: STY0640(entE)
            STT: t2272(entE)
            SPT: SPA2138(entE)
            SEC: SC0627(entE)
            STM: STM0596(entE)
            SFL: SF0508(entE)
            SFX: S0514(entE)
            SFV: SFV_0542(entE)
            SSN: SSON_0545(entE)
            SBO: SBO_0455(entE)
            SDY: SDY_0525(entE)
            ECA: ECA0478(entE)
            PLU: plu2729(entE)
            PPR: PBPRB1823
            PEN: PSEEN2505(pmsE)
            ACI: ACIAD2770(entE)
            SDE: Sde_3399
            HCH: HCH_06564
            AHA: AHA_2478
            CVI: CV_1484(entE)
            BUR: Bcep18194_A4900 Bcep18194_B0670 Bcep18194_B3103
            BAM: Bamb_1689
            MXA: MXAN_3645
            SAT: SYN_01638
            BME: BMEII0078
            BMF: BAB2_0014
            BMS: BRA0015(entE)
            BMB: BruAb2_0015(entE)
            BOV: BOV_A0012
            BAN: BA2370(dhbE)
            BAR: GBAA2370(dhbE)
            BAA: BA_2864
            BAT: BAS2206
            BCE: BC2304
            BCA: BCE_2400(dhbE)
            BCZ: BCZK2129(entE)
            BTK: BT9727_2145(entE)
            BTL: BALH_2109(entE)
            OIH: OB0956(dhbE)
            DSY: DSY2823
            CJK: jk1820(dhbE)
            RHA: RHA1_ro04793
            FAL: FRAAL4648
            SEN: SACE_2694(dhbE) SACE_3853(dhbE)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.58
            ExPASy - ENZYME nomenclature database: 2.7.7.58
            ExplorEnz - The Enzyme Database: 2.7.7.58
            ERGO genome analysis and discovery system: 2.7.7.58
            BRENDA, the Enzyme Database: 2.7.7.58
            CAS: 122332-73-4
///
ENTRY       EC 2.7.7.59                 Enzyme
NAME        [protein-PII] uridylyltransferase;
            PII uridylyl-transferase;
            uridyl removing enzyme
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     UTP:[protein-PII] uridylyltransferase
REACTION    UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]
            [RN:R04733]
ALL_REAC    R04733
SUBSTRATE   UTP [CPD:C00075];
            [protein-PII] [CPD:C05250]
PRODUCT     diphosphate [CPD:C00013];
            uridylyl-[protein-PII] [CPD:C05326]
COMMENT     The enzyme uridylylates and de-uridylylates the small trimeric
            protein PII. The enzymes from Escherichia coli and Salmonella
            typhimurium have been wrongly identified, in some databases, as EC
            2.7.7.12 (UDP-glucose---hexose-1-phosphate uridylyltransferase),
            from which it differs greatly in both reaction catalysed and
            sequence.
REFERENCE   1  [PMID:6130097]
  AUTHORS   Garcia E, Rhee SG.
  TITLE     Cascade control of Escherichia coli glutamine synthetase.
            Purification and properties of PII uridylyltransferase and
            uridylyl-removing enzyme.
  JOURNAL   J. Biol. Chem. 258 (1983) 2246-53.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:8412694]
  AUTHORS   van Heeswijk WC, Rabenberg M, Westerhoff HV, Kahn D.
  TITLE     The genes of the glutamine synthetase adenylylation cascade are not
            regulated by nitrogen in Escherichia coli.
  JOURNAL   Mol. Microbiol. 9 (1993) 443-57.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K00990  [protein-PII] uridylyltransferase
GENES       ECO: b0167(glnD)
            ECJ: JW0162(glnD)
            ECE: Z0177(glnD)
            ECS: ECs0169
            ECC: c0202(glnD)
            ECI: UTI89_C0181(glnD)
            ECP: ECP_0175
            ECW: EcE24377A_0170(glnD)
            ECX: EcHS_A0169(glnD)
            STY: STY0237(glnD)
            STT: t0215(glnD)
            SPT: SPA0220(glnD)
            SEC: SC0214(glnD)
            STM: STM0214(glnD)
            YPE: YPO1042(glnD)
            YPK: y3139(glnD)
            YPM: YP_2809(glnD)
            YPA: YPA_0516
            YPN: YPN_2959
            YPP: YPDSF_1671
            YPS: YPTB3005(glnD)
            YPI: YpsIP31758_1011(glnD)
            SFL: SF0157(glnD)
            SFX: S0160(glnD)
            SFV: SFV_0150(glnD)
            SSN: SSON_0179(glnD)
            SBO: SBO_0155(glnD)
            SDY: SDY_0183(glnD)
            ECA: ECA1029(glnD)
            PLU: plu0670(glnD)
            SGL: SG1945
            ENT: Ent638_0705
            SPE: Spro_3792
            HIT: NTHI2026(glnD)
            HIP: CGSHiEE_03450(glnD)
            HSO: HS_0829(glnD)
            PMU: PM0460(glnD)
            MSU: MS1305(glnD)
            APL: APL_0598(glnD)
            ASU: Asuc_1032
            XCC: XCC1383(glnD)
            XCB: XC_2855
            XCV: XCV1486(glnD)
            XAC: XAC1429(glnD)
            XOO: XOO1984(glnD)
            XOM: XOO_1875(XOO1875)
            VCH: VC2262
            VCO: VC0395_A1853(glnD)
            VVU: VV1_1857
            VVY: VV2559
            VPA: VP2320
            VFI: VF1964
            PPR: PBPRA2970
            PAE: PA3658(glnD)
            PAU: PA14_17040(glnD)
            PAP: PSPA7_1481(glnD)
            PPU: PP_1589(glnD)
            PPF: Pput_4188
            PST: PSPTO_1532(glnD)
            PSB: Psyr_1341(glnD)
            PSP: PSPPH_3842(glnD)
            PFL: PFL_1174(glnD)
            PFO: Pfl_1099(glnD)
            PEN: PSEEN4222(glnD)
            PMY: Pmen_3055
            PAR: Psyc_0395(glnD)
            PCR: Pcryo_0441
            PRW: PsycPRwf_0556
            ACI: ACIAD2079(glnD)
            SON: SO_1626(glnD)
            SDN: Sden_1552 Sden_2877
            SFR: Sfri_0910 Sfri_1268
            SAZ: Sama_1137
            SBL: Sbal_1448
            SBM: Shew185_1443
            SLO: Shew_2637
            SPC: Sputcn32_1346
            SSE: Ssed_3163 Ssed_3746
            SPL: Spea_2887 Spea_3229
            SHE: Shewmr4_2643
            SHM: Shewmr7_2710
            SHN: Shewana3_2817
            SHW: Sputw3181_2757
            ILO: IL0847(glnD)
            CPS: CPS_1549(glnD)
            PHA: PSHAa2038(glnD)
            PAT: Patl_1247
            SDE: Sde_2602
            PIN: Ping_3004
            MAQ: Maqu_2550
            LPN: lpg1720(glnD)
            LPF: lpl1684(glnD)
            LPP: lpp1685(glnD)
            MCA: MCA0565(glnD)
            TCX: Tcr_1287
            NOC: Noc_0806
            AEH: Mlg_1865
            HHA: Hhal_1468
            HCH: HCH_05255(glnD)
            CSA: Csal_0561
            ABO: ABO_1141(glnD)
            MMW: Mmwyl1_1270
            AHA: AHA_1171(glnD)
            RMA: Rmag_0475
            VOK: COSY_0438(glnD)
            NME: NMB1203
            NMA: NMA1374(glnD)
            NMC: NMC1104(glnD)
            NGO: NGO0798
            CVI: CV_2917(glnD)
            RSO: RSc1402(glnD)
            REU: Reut_A1883
            RME: Rmet_1433
            BMA: BMA1557(glnD)
            BMV: BMASAVP1_A2059(glnD)
            BML: BMA10299_A3252(glnD)
            BMN: BMA10247_1331(glnD)
            BXE: Bxe_A1679
            BVI: Bcep1808_1928
            BUR: Bcep18194_A5331
            BCN: Bcen_6056
            BCH: Bcen2424_2021
            BAM: Bamb_2054
            BPS: BPSL2161
            BPM: BURPS1710b_2585(glnD)
            BPL: BURPS1106A_2496(glnD)
            BPD: BURPS668_2439(glnD)
            BTE: BTH_I2025(glnD)
            PNU: Pnuc_1453
            BPE: BP1417(glnD)
            BPA: BPP1525(glnD)
            BBR: BB2603(glnD)
            RFR: Rfer_2422
            POL: Bpro_2588
            PNA: Pnap_1819
            AAV: Aave_3101
            AJS: Ajs_2294
            VEI: Veis_3611
            MPT: Mpe_A1759
            HAR: HEAR1333(glnD)
            MMS: mma_2060(glnD)
            NMU: Nmul_A2633
            EBA: ebA5982(glnD)
            AZO: azo1911(glnD)
            DAR: Daro_1739
            TBD: Tbd_0783
            MFA: Mfla_1532
            TDN: Tmden_1482
            ABU: Abu_0194(glnD)
            GSU: GSU1820
            GME: Gmet_1426
            GUR: Gura_2384
            PCA: Pcar_1512
            PPD: Ppro_1343
            DVU: DVU1233
            DVL: Dvul_1829
            DDE: Dde_2309
            BBA: Bd1955(glnD)
            DPS: DP0929
            ADE: Adeh_1692
            AFW: Anae109_2112
            SFU: Sfum_0485 Sfum_0574
            MLO: mll5321
            MES: Meso_4033
            PLA: Plav_3602
            SME: SMc01124(glnD)
            SMD: Smed_0031
            ATU: Atu0346(glnD)
            ATC: AGR_C_606
            RET: RHE_CH00387(glnD)
            RLE: RL0405(glnD)
            BME: BMEI1804
            BMF: BAB1_0143
            BMS: BR0144
            BMB: BruAb1_0141
            BOV: BOV_0139(glnD)
            OAN: Oant_0157
            BJA: bll0916(glnD)
            BRA: BRADO0530(glnD)
            BBT: BBta_7648(glnD)
            RPA: RPA0591(glnD)
            RPB: RPB_0032
            RPC: RPC_0342
            RPD: RPD_0116
            RPE: RPE_0260
            NWI: Nwi_0133
            NHA: Nham_0226
            XAU: Xaut_0284
            CCR: CC_0013
            SIL: SPO0397(glnD)
            SIT: TM1040_0446
            RSP: RSP_1811(glnD)
            RSH: Rsph17029_0458
            RSQ: Rsph17025_0469
            JAN: Jann_0897
            RDE: RD1_1188(glnD)
            PDE: Pden_3956
            MMR: Mmar10_3022
            HNE: HNE_0518(glnD)
            ZMO: ZMO0766(glnD)
            NAR: Saro_0682
            SAL: Sala_2787
            SWI: Swit_2766 Swit_2768
            ELI: ELI_11825
            GOX: GOX1872
            GBE: GbCGDNIH1_0415
            ACR: Acry_0914
            RRU: Rru_A3539
            MAG: amb4476
            MGM: Mmc1_1411
            ABA: Acid345_1488
            SUS: Acid_7188
            MTU: Rv2918c(glnD)
            MTC: MT2986(glnD)
            MBO: Mb2942c(glnD)
            MBB: BCG_2939c(glnD)
            MPA: MAP2986c(glnD)
            MAV: MAV_3773(glnD)
            MSM: MSMEG_2427(glnD)
            MVA: Mvan_2180
            MGI: Mflv_4183
            MMC: Mmcs_1958
            MKM: Mkms_2004
            MJL: Mjls_1938
            CGL: NCgl1981(glnD)
            CGB: cg2258(glnD)
            CEF: CE1966(glnD)
            CDI: DIP1534(glnD)
            NFA: nfa41620(glnD)
            RHA: RHA1_ro06532(glnD)
            SCO: SCO5585(glnD)
            SMA: SAV2649(glnD)
            NCA: Noca_3267
            FRA: Francci3_0420
            FAL: FRAAL0903(glnD)
            ACE: Acel_1564
            KRA: Krad_1395
            STP: Strop_1300
            BLO: BL0433(glnD)
            BAD: BAD_0115(glnD)
            RBA: RB2974(glnD)
            LIL: LA3921(glnD)
            LIC: LIC13130(glnD)
            LBJ: LBJ_1581
            LBL: LBL_1799
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.59
            ExPASy - ENZYME nomenclature database: 2.7.7.59
            ExplorEnz - The Enzyme Database: 2.7.7.59
            ERGO genome analysis and discovery system: 2.7.7.59
            BRENDA, the Enzyme Database: 2.7.7.59
            CAS: 57657-57-5
///
ENTRY       EC 2.7.7.60                 Enzyme
NAME        2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase;
            MEP cytidylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     CTP:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
REACTION    CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate +
            4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol [RN:R05633]
ALL_REAC    R05633
SUBSTRATE   CTP [CPD:C00063];
            2-C-methyl-D-erythritol 4-phosphate [CPD:C11434]
PRODUCT     diphosphate [CPD:C00013];
            4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol [CPD:C11435]
COMMENT     The enzyme from Escherichia coli requires Mg2+ or Mn2+. ATP or UTP
            can replace CTP, but both are less effective. GTP and TTP are not
            substrates. Forms part of an alternative nonmevalonate pathway for
            terpenoid biosynthesis (for diagram, click here).
REFERENCE   1  [PMID:10518523]
  AUTHORS   Rohdich F, Wungsintaweekul J, Fellermeier M, Sagner S, Herz S, Kis
            K, Eisenreich W, Bacher A, Zenk MH.
  TITLE     Cytidine 5'-triphosphate-dependent biosynthesis of isoprenoids: YgbP
            protein of Escherichia coli catalyzes the formation of
            4-diphosphocytidyl-2-C-methylerythritol.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 11758-63.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Kuzuyama, T., Takagi, M., Kaneda, K., Dairi, T. and Seto, H.
  TITLE     Formation of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol from
            2-C-methyl-D-erythritol 4-phosphate by 2-C-methyl-D-erythritol
            4-phosphate cytidylyltransferase, a new enzyme in the nonmevalonate
            pathway.
  JOURNAL   Tetrahedron Lett. 41 (2000) 703-706.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K00991  2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
GENES       OSA: 4324893
            CME: CMH115C
            TAN: TA02505
            TPV: TP03_0057
            ECO: b2747(ispD)
            ECJ: JW2717(ispD)
            ECE: Z4055(ygbP)
            ECS: ECs3601
            ECC: c3314(ispD)
            ECI: UTI89_C3118(ygbP)
            ECP: ECP_2729
            ECV: APECO1_3776(ispD)
            ECW: EcE24377A_3048(ispD)
            ECX: EcHS_A2885
            STY: STY3055(ygbP)
            STT: t2831(ygbP)
            SPT: SPA2786(ygbP)
            SEC: SC2862(ispD)
            STM: STM2930(ispD)
            YPE: YPO3361(ispD)
            YPK: y0828
            YPM: YP_0326(ispD)
            YPA: YPA_2782
            YPN: YPN_0732
            YPP: YPDSF_2999
            YPS: YPTB0770(ispD)
            YPI: YpsIP31758_3299(ispD)
            YEN: YE0769(b2747)
            SFL: SF2770(ispD)
            SFX: S2963(ygbP)
            SFV: SFV_2751(ygbP)
            SSN: SSON_2895(ygbP)
            SBO: SBO_2773(ygbP)
            SDY: SDY_2946(ygbP)
            ECA: ECA3535(ispD)
            PLU: plu0713(ispD)
            BUC: BU420(ygbP)
            BAS: BUsg405(ygbP)
            WBR: WGLp532(ygbP)
            SGL: SG0526
            ENT: Ent638_3218
            KPN: KPN_03109(ispD)
            BPN: BPEN_171(ispD)
            HIN: HI0672(ygbP)
            HIT: NTHI0794(ispD)
            HIP: CGSHiEE_08815(ispD)
            HIQ: CGSHiGG_06635(ispD)
            HDU: HD1329(ispD)
            HSO: HS_1496(ispD)
            PMU: PM1608
            MSU: MS2275(ispD)
            APL: APL_0802(ispD)
            XFA: XF1293
            XFT: PD0545(ispD)
            XCC: XCC1702(ispD)
            XCB: XC_2529
            XCV: XCV1754(ispD)
            XAC: XAC1721(ispD)
            XOO: XOO2961(ispD)
            XOM: XOO_2812(XOO2812)
            VCH: VC0528
            VVU: VV1_1582
            VVY: VV2816
            VPA: VP1320 VP2559
            VFI: VF2073(ispD)
            PPR: PBPRA3077(ygbP)
            PAE: PA3633
            PAU: PA14_17340(ispD)
            PAP: PSPA7_1506(ispD)
            PPU: PP_1614(ispD)
            PST: PSPTO_1556(ispD)
            PSB: Psyr_1365
            PSP: PSPPH_3818(ispD)
            PFL: PFL_1198(ispD)
            PFO: Pfl_1123
            PEN: PSEEN4198(ispD)
            PMY: Pmen_3031
            PAR: Psyc_1634
            PCR: Pcryo_1868
            ACI: ACIAD1999(ispD)
            ACB: A1S_1895
            SON: SO_3438(ispD)
            SDN: Sden_1198
            SFR: Sfri_1054
            SAZ: Sama_1038
            SBL: Sbal_3125
            SLO: Shew_1207
            SPC: Sputcn32_2755
            SHE: Shewmr4_1117
            SHM: Shewmr7_1188
            SHN: Shewana3_1118
            SHW: Sputw3181_1257
            ILO: IL0752(ispD)
            CPS: CPS_1072(ispD)
            PHA: PSHAa0684(ispD)
            PAT: Patl_3857
            SDE: Sde_1247
            PIN: Ping_0672
            MAQ: Maqu_0923
            MCA: MCA2517(ispD)
            FTU: FTT0711(ispD)
            FTF: FTF0711(ispD)
            FTW: FTW_1530(ispD)
            FTL: FTL_1525
            FTH: FTH_1475(ispD)
            FTA: FTA_1609(ispD)
            FTN: FTN_0623(ispD)
            NOC: Noc_0854
            AEH: Mlg_1837
            HHA: Hhal_1435
            HCH: HCH_01869(ispD)
            CSA: Csal_2638
            ABO: ABO_1166(ispD)
            AHA: AHA_0823(ispD)
            BCI: BCI_0211(ispD)
            RMA: Rmag_0755
            VOK: COSY_0697(ispD)
            NME: NMB1513
            NMA: NMA1713
            NGO: NGO0972
            CVI: CV_1258(ispD)
            RSO: RSc1643(RS04018)
            REU: Reut_A1361
            REH: H16_A1456
            RME: Rmet_1954
            BMA: BMA1490(ispD)
            BMV: BMASAVP1_A1987(ispD)
            BML: BMA10299_A3319(ispD)
            BMN: BMA10247_1259(ispD)
            BXE: Bxe_A2312
            BUR: Bcep18194_A5254(ispD)
            BCN: Bcen_6136
            BCH: Bcen2424_1943
            BAM: Bamb_1931
            BPS: BPSL2099(ispD)
            BPM: BURPS1710b_2512(ispD)
            BPL: BURPS1106A_2401(ispD)
            BPD: BURPS668_2358(ispD)
            BTE: BTH_I2089(ispD)
            PNU: Pnuc_0930
            BPE: BP0865(ispD)
            BPA: BPP3366(ispD)
            BBR: BB3817(ispD)
            RFR: Rfer_1332
            POL: Bpro_2716
            MPT: Mpe_A1570
            HAR: HEAR1912(ispD)
            MMS: mma_1409
            NEU: NE1412
            NET: Neut_1525
            NMU: Nmul_A2127
            EBA: ebA6543(ispD)
            AZO: azo1682
            DAR: Daro_1973
            TBD: Tbd_1003
            MFA: Mfla_1116
            HPY: HP1020
            HPJ: jhp0404
            HPA: HPAG1_0427
            HHE: HH1582
            HAC: Hac_1124(ispD)
            WSU: WS1940
            TDN: Tmden_1487
            CJE: Cj1607
            CJR: CJE1779
            CJU: C8J_1508
            CFF: CFF8240_0409
            CHA: CHAB381_0932
            CCO: CCC13826_0390
            ABU: Abu_0126(ispDF)
            NIS: NIS_0595
            SUN: SUN_0522
            GSU: GSU3368(ispD)
            GME: Gmet_0060
            PCA: Pcar_0103
            DVU: DVU1454(ispD)
            DDE: Dde_1726
            LIP: LI0446
            DPS: DP0257
            ADE: Adeh_1272
            SAT: SYN_01401
            SFU: Sfum_1637
            WOL: WD1143
            WBM: Wbm0409
            AMA: AM1357(ispD)
            APH: APH_1277(ispD)
            ERU: Erum1030(ispD)
            ERW: ERWE_CDS_01000(ispD)
            ERG: ERGA_CDS_00960(ispD)
            ECN: Ecaj_0103
            ECH: ECH_0157(ispD)
            NSE: NSE_0178
            PUB: SAR11_0945(ispD)
            MLO: mll0395
            MES: Meso_1621
            SME: SMc01040
            ATU: Atu1443(ispF)
            ATC: AGR_C_2659
            RET: RHE_CH01945(ispDF)
            RLE: RL2254(ispDF)
            BME: BMEI0863
            BMF: BAB1_1143
            BMS: BR1120
            BMB: BruAb1_1126(ispDF)
            BOV: BOV_1078
            BJA: bll4485
            BRA: BRADO3869(ispDF)
            BBT: BBta_4067(ispDF)
            RPA: RPA2590(ispD)
            RPB: RPB_2885
            RPC: RPC_2575
            RPD: RPD_2587
            RPE: RPE_2755
            NWI: Nwi_1442
            NHA: Nham_1834
            BHE: BH05820
            BQU: BQ04980(ispDF)
            BBK: BARBAKC583_0540(ispDF)
            CCR: CC_1738
            SIL: SPO2090(ispDF)
            RSP: RSP_2835(ispD)
            RDE: RD1_2766(ispD)
            MMR: Mmar10_1439
            HNE: HNE_2014(ispDF)
            ZMO: ZMO1128
            NAR: Saro_1925
            SAL: Sala_1278
            ELI: ELI_06290
            GOX: GOX1669(ispD)
            GBE: GbCGDNIH1_1019
            RRU: Rru_A1674
            MAG: amb2363
            MGM: Mmc1_2672
            ABA: Acid345_0188
            BSU: BG10152(ispD)
            BHA: BH0107
            BAN: BA0084(ispD)
            BAR: GBAA0084(ispD)
            BAA: BA_0674
            BAT: BAS0085
            BCE: BC0106(ispD)
            BCA: BCE_0085(ispD)
            BCZ: BCZK0081(ispD)
            BTK: BT9727_0082(ispD)
            BTL: BALH_0085(ispD)
            BLI: BL03265
            BLD: BLi00108(yacM)
            BCL: ABC0125(ispD)
            BAY: RBAM_001150(yacM)
            BPU: BPUM_0075
            GKA: GK0081(ispD)
            SAU: SA0241 SA0245
            SAV: SAV0251 SAV0255
            SAM: MW0227 MW0231
            SAR: SAR0246 SAR0252
            SAS: SAS0227 SAS0232
            SAC: SACOL0236 SACOL0240
            SAB: SAB0190 SAB0194
            SAA: SAUSA300_0245 SAUSA300_0249
            SAO: SAOUHSC_00220 SAOUHSC_00225
            SAJ: SaurJH9_0236
            SAH: SaurJH1_0242
            SEP: SE0319
            SER: SERP0196
            SSP: SSP0354
            LMO: lmo0235 lmo1086
            LMF: LMOf2365_0247(ispD) LMOf2365_1100
            LIN: lin0267 lin1071
            LWE: lwe0199(ispD) lwe1061
            SPN: SP_1271
            SPR: spr1149
            SPD: SPD_1127(ispD)
            SAG: SAG1417
            SAN: gbs1487
            SAK: SAK_1452(ispD)
            SSA: SSA_2214
            SGO: SGO_2017
            LPL: lp_1816
            LCA: LSEI_1098
            EFA: EF2172(ispD)
            STH: STH3123
            CAC: CAC3184
            CPE: CPE2429
            CPF: CPF_2739(ispD)
            CPR: CPR_2426(ispD)
            CTC: CTC02626
            CNO: NT01CX_1092(ispD)
            CDF: CD0047(ispD)
            CBO: CBO3504(ispD)
            CBA: CLB_3564(ispD)
            CBH: CLC_3453(ispD)
            CBF: CLI_3691(ispD)
            CKL: CKL_0200(ispD)
            CHY: CHY_2342(ispD)
            DSY: DSY0443 DSY3011
            SWO: Swol_2361
            TTE: TTE2322(ispD)
            MTA: Moth_2487
            MPE: MYPE2770
            MTU: Rv3582c(ispD)
            MTC: MT3688
            MBO: Mb3613c(ispD)
            MLE: ML0321
            MPA: MAP0476
            MAV: MAV_0571(ispD)
            MSM: MSMEG_6076(ispD)
            MVA: Mvan_4129
            MMC: Mmcs_4739
            CGL: NCgl2570(ispD)
            CGB: cg2945(ispD)
            CEF: CE2521
            CDI: DIP1973
            CJK: jk0308(ispD)
            NFA: nfa4360(mecT)
            RHA: RHA1_ro04460
            SCO: SCO4233(ispD)
            SMA: SAV3969(mecT)
            TWH: TWT348(ispDF)
            TWS: TW422
            LXX: Lxx18250(ispF)
            CMI: CMM_2489(ispDF)
            AAU: AAur_0898(ispD)
            PAC: PPA0353
            FRA: Francci3_3932 Francci3_4254
            FAL: FRAAL6243 FRAAL6524(ispD)
            ACE: Acel_0080
            SEN: SACE_0439(ispD)
            BLO: BL0324(ispD)
            RXY: Rxyl_2176
            FNU: FN1580
            RBA: RB9133(ispD)
            CTR: CT462(ygbP)
            CTA: CTA_0505(ispD)
            CMU: TC0747
            CPN: CPn0579(yacM)
            CPA: CP0169
            CPJ: CPj0579(yacM)
            CPT: CpB0603
            CCA: CCA00162(ispD)
            CAB: CAB160(ispD)
            CFE: CF0845(yacM)
            PCU: pc0327(ispD)
            TPA: TP0512
            TDE: TDE2291(ispD)
            LIL: LA1048(ygbP)
            LIC: LIC12617(ispD)
            LBJ: LBJ_0280(ispD)
            LBL: LBL_2796(ispD)
            SYN: slr0951
            SYW: SYNW1849(ispD)
            SYC: syc0848_d(ispD)
            SYF: Synpcc7942_0681
            SYD: Syncc9605_0620(ispD)
            SYE: Syncc9902_1742(ispD)
            SYG: sync_2140(ispD)
            SYR: SynRCC307_0684(ispD)
            SYX: SynWH7803_1858(ispD)
            CYA: CYA_1505(ispD)
            CYB: CYB_2706(ispD)
            TEL: tlr0605
            GVI: glr2791
            ANA: all5167
            AVA: Ava_2414(ispD)
            PMA: Pro0453(ispD)
            PMM: PMM0454(ispD)
            PMT: PMT1330(ispD)
            PMN: PMN2A_1786(ispD)
            PMI: PMT9312_0454
            PMB: A9601_05101(ispD)
            PMC: P9515_05171(ispD)
            PMF: P9303_06551(ispD)
            PMG: P9301_04791(ispD)
            PMH: P9215_05341
            PME: NATL1_05091(ispD)
            TER: Tery_0609
            BTH: BT_2881 BT_3923
            BFR: BF3962
            BFS: BF3735
            PGI: PG1434(ispD)
            SRU: SRU_1652
            CHU: CHU_3100(ispD)
            CTE: CT1317(ispD)
            CCH: Cag_0929
            DET: DET0059(ispD)
            DEH: cbdb_A74(ispD)
            DRA: DR_2604
            DGE: Dgeo_0181
            TTH: TTC1815
            TTJ: TTHA0171
            AAE: aq_1323
            TMA: TM1393
            MSI: Msm_0377 Msm_1542
            HMA: rrnAC1932(ispD)
STRUCTURES  PDB: 1H3M  1VGT  1VGU  1VGZ  1VPA  1W55  1W57  1W77  2PX7  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.60
            ExPASy - ENZYME nomenclature database: 2.7.7.60
            ExplorEnz - The Enzyme Database: 2.7.7.60
            ERGO genome analysis and discovery system: 2.7.7.60
            BRENDA, the Enzyme Database: 2.7.7.60
///
ENTRY       EC 2.7.7.61                 Enzyme
NAME        holo-ACP synthase;
            2'-(5"-phosphoribosyl)-3'-dephospho-CoA transferase;
            2'-(5"-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase;
            CitX
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     2'-(5''-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase
            adenylyltransferase
REACTION    2'-(5"-triphosphoribosyl)-3'-dephospho-CoA + apo-citrate lyase =
            holo-citrate lyase + diphosphate
SUBSTRATE   2'-(5''-triphosphoribosyl)-3'-dephospho-CoA;
            apo-citrate lyase
PRODUCT     holo-citrate lyase;
            diphosphate [CPD:C00013]
COMMENT     Requires Mg2+. The enzyme from Escherichia coli can also use ATP,
            CTP, GTP and UTP as a substrate in vitro. The corresponding
            mononucleotides are transferred to serine-14 of the acyl carrier
            protein of citrate lyase with release of diphosphate; the linkage to
            serine is via a phosphodiester bond.
REFERENCE   1  [PMID:10924139]
  AUTHORS   Schneider K, Dimroth P, Bott M.
  TITLE     Biosynthesis of the prosthetic group of citrate lyase.
  JOURNAL   Biochemistry. 39 (2000) 9438-50.
  ORGANISM  Klebsiella pneumoniae, Escherichia coli [GN:eco]
REFERENCE   2  [PMID:11042274]
  AUTHORS   Schneider K, Dimroth P, Bott M.
  TITLE     Identification of triphosphoribosyl-dephospho-CoA as precursor of
            the citrate lyase prosthetic group.
  JOURNAL   FEBS. Lett. 483 (2000) 165-8.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K05964  holo-ACP synthase
GENES       ECO: b0614(ybdU)
            ECJ: JW0606(citX)
            ECE: Z0758(ybdU)
            ECS: ECs0653
            ECC: c0702(ybdU)
            ECI: UTI89_C0616(citX)
            ECP: ECP_0645
            ECV: APECO1_1437(citX)
            ECW: EcE24377A_0636(citX)
            ECX: EcHS_A0665(citX)
            STY: STY0669(citX)
            STT: t2247(citX)
            SPT: SPA2114(citX)
            SEC: SC0649(citX)
            STM: STM0620(citX)
            SFX: S0538(ybdU)
            SFV: SFV_0567(ybdU)
            SSN: SSON_0566(ybdU)
            SBO: SBO_0479(ybdU)
            ECA: ECA2570(citX)
            ENT: Ent638_3371
            SPE: Spro_3167
            HIN: HI0021(citG)
            HIT: NTHI0028(citG)
            HDU: HD1245(citG)
            ASU: Asuc_1198
            VCH: VC0800
            PPR: PBPRA2291
            PAP: PSPA7_0297(mdcG)
            BPL: BURPS1106A_1486(mdcG)
            BPD: BURPS668_1456(mdcG)
            RFR: Rfer_2406
            RPE: RPE_3431
            SPY: SPy_1190(citX)
            SPZ: M5005_Spy_0908(citX)
            SPM: spyM18_1141(citX)
            SPG: SpyM3_0835(citX)
            SPS: SPs1035
            SPH: MGAS10270_Spy1022(citX)
            SPI: MGAS10750_Spy1058(citX)
            SPF: SpyM50889(citX)
            SPA: M6_Spy0897
            SPB: M28_Spy0881(citX)
            LPL: lp_1114(citX)
            LAC: LBA1232(citX)
            LSA: LSA1223(citX)
            LCA: LSEI_1856
            EFA: EF3318(citX)
            OOE: OEOE_0424
            CNO: NT01CX_1153
            MSM: MSMEG_6631(mdcG)
            TDE: TDE1523
STRUCTURES  PDB: 2BDD  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.61
            ExPASy - ENZYME nomenclature database: 2.7.7.61
            ExplorEnz - The Enzyme Database: 2.7.7.61
            ERGO genome analysis and discovery system: 2.7.7.61
            BRENDA, the Enzyme Database: 2.7.7.61
            CAS: 312492-44-7
///
ENTRY       EC 2.7.7.62                 Enzyme
NAME        adenosylcobinamide-phosphate guanylyltransferase;
            CobU;
            adenosylcobinamide kinase/adenosylcobinamide-phosphate
            guanylyltransferase;
            AdoCbi kinase/AdoCbi-phosphate guanylyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     GTP:adenosylcobinamide-phosphate guanylyltransferase
REACTION    GTP + adenosylcobinamide phosphate = diphosphate +
            adenosylcobinamide-GDP [RN:R05222]
ALL_REAC    R05222
SUBSTRATE   GTP [CPD:C00044];
            adenosylcobinamide phosphate
PRODUCT     diphosphate [CPD:C00013];
            adenosylcobinamide-GDP [CPD:C06510]
COMMENT     In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC
            2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73)
            and CobS (EC 2.7.8.26) catalyse reactions in the nucleotide loop
            assembly pathway, which convert adenosylcobinamide (AdoCbi) into
            adenosylcobalamin (AdoCbl). CobT and CobC are involved in
            5,6-dimethylbenzimidazole activation whereby
            5,6-dimethylbenzimidazole is converted to its riboside,
            alpha-ribazole. The second branch of the nuclotide loop assembly
            pathway is the cobinamide (Cbi) activation branch where AdoCbi or
            adenosylcobinamide-phosphate is converted to the activated
            intermediate AdoCbi-GDP by the bifunctional enzyme Cob U. The final
            step in adenosylcobalamin biosynthesis is the condensation of
            AdoCbi-GDP with alpha-ribazole, which is catalysed by EC 2.7.8.26,
            cobalamin synthase (CobS), to yield adenosylcobalamin. CobU is a
            bifunctional enzyme that has both kinase (EC 2.7.1.156) and
            guanylyltransferase (EC 2.7.7.62) activities. However, both
            activities are not required at all times.The kinase activity has
            been proposed to function only when S. typhimurium is assimilating
            cobinamide whereas the guanylyltransferase activity is required for
            both assimilation of exogenous cobinamide and for de novo synthesis
            of adenosylcobalamin [4]. The guanylyltransferase reaction is a
            two-stage reaction with formation of a CobU-GMP intermediate [1].
            Guanylylation takes place at histidine-46.
REFERENCE   1  [PMID:7559521]
  AUTHORS   O'Toole GA, Escalante-Semerena JC.
  TITLE     Purification and characterization of the bifunctional CobU enzyme of
            Salmonella typhimurium LT2. Evidence for a CobU-GMP intermediate.
  JOURNAL   J. Biol. Chem. 270 (1995) 23560-9.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:9601028]
  AUTHORS   Thompson TB, Thomas MG, Escalante-Semerena JC, Rayment I.
  TITLE     Three-dimensional structure of adenosylcobinamide
            kinase/adenosylcobinamide phosphate guanylyltransferase from
            Salmonella typhimurium determined to 2.3 A resolution,.
  JOURNAL   Biochemistry. 37 (1998) 7686-95.
  ORGANISM  Salmonella typhimurium
REFERENCE   3  [PMID:10529169]
  AUTHORS   Thompson TB, Thomas MG, Escalante-Semerena JC, Rayment I.
  TITLE     Three-dimensional structure of adenosylcobinamide
            kinase/adenosylcobinamide phosphate guanylyltransferase (CobU)
            complexed with GMP: evidence for a substrate-induced transferase
            active site.
  JOURNAL   Biochemistry. 38 (1999) 12995-3005.
  ORGANISM  Salmonella typhimurium
REFERENCE   4  [PMID:10869342]
  AUTHORS   Thomas MG, Thompson TB, Rayment I, Escalante-Semerena JC.
  TITLE     Analysis of the adenosylcobinamide
            kinase/adenosylcobinamide-phosphate guanylyltransferase (CobU)
            enzyme of Salmonella typhimurium LT2. Identification of residue
            His-46 as the site of guanylylation.
  JOURNAL   J. Biol. Chem. 275 (2000) 27576-86.
  ORGANISM  Salmonella typhimurium
REFERENCE   5  [PMID:12195810]
  AUTHORS   Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
  TITLE     The biosynthesis of adenosylcobalamin (vitamin B12).
  JOURNAL   Nat. Prod. Rep. 19 (2002) 390-412.
  ORGANISM  Pseudomonas denitrificans, Salmonella enterica, Bacillus megaterium
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K02231  adenosylcobinamide kinase / adenosylcobinamide-phosphate
                        guanylyltransferase
GENES       ECO: b1993(cobU)
            ECJ: JW1971(cobU)
            ECE: Z3153(cobU)
            ECS: ECs2788
            ECC: c2479(cobU)
            ECI: UTI89_C2231(cobU)
            ECP: ECP_1991
            ECV: APECO1_1074(cobU)
            ECW: EcE24377A_2275(cobU)
            ECX: EcHS_A2116(cobU)
            STY: STY2221(cobU)
            STT: t0856(cobU)
            SPT: SPA0853(cobU)
            SEC: SC2026(cobU)
            STM: STM2018(cobU)
            SFL: SF2061(cobU)
            SFV: SFV_2065(cobU)
            SSN: SSON_2054(cobU)
            SDY: SDY_2240(cobU)
            PLU: plu2986(cobU)
            XCC: XCC3060(cobU)
            XCB: XC_1098
            XCV: XCV3316(cobU)
            XAC: XAC3187(cobU)
            XOO: XOO1350(cobU)
            XOM: XOO_1240(XOO1240)
            VCH: VC1239
            VVU: VV1_2786
            VVY: VV1476
            VPA: VP1306
            PPR: PBPRB0995(cobU)
            PAE: PA1278(cobP)
            PAU: PA14_47680(cobP)
            PPU: PP_1678(cobP)
            PPF: Pput_4041
            PST: PSPTO_1714(cobP)
            PSB: Psyr_3675
            PSP: PSPPH_3696(cobP)
            PFL: PFL_4425(cobU)
            PFO: Pfl_1647
            PEN: PSEEN1384
            SON: SO_1037(cobU)
            SFR: Sfri_0878
            SHE: Shewmr4_0844
            SHM: Shewmr7_3178
            SHN: Shewana3_3276
            CPS: CPS_3657(cobP)
            PHA: PSHAa2997(cobU)
            PAT: Patl_1137
            SDE: Sde_3204
            MCA: MCA0462(cobU)
            AEH: Mlg_2824
            HCH: HCH_00963(cobU)
            ABO: ABO_2380(cobU)
            MMW: Mmwyl1_3675
            CVI: CV_0495(cobU)
            RSO: RSc2391(cobP)
            REH: H16_A2962(cobU)
            RME: Rmet_2779
            BMA: BMA0696(cobU)
            BXE: Bxe_A3493
            BVI: Bcep1808_2531
            BPS: BPSL0986
            BPM: BURPS1710b_1199(cobU)
            BPL: BURPS1106A_1044(cobU)
            BPD: BURPS668_1038(cobU)
            BTE: BTH_I0843
            RFR: Rfer_2622
            POL: Bpro_2783
            HAR: HEAR0966(cobU)
            EBA: ebA4011(cobU)
            TBD: Tbd_2713
            MFA: Mfla_0113
            TDN: Tmden_0112
            ABU: Abu_2182(cobP)
            GSU: GSU3010(cobU)
            GUR: Gura_4188
            PCA: Pcar_0487(cobP)
            DVU: DVU1007(cobU)
            DDE: Dde_3495
            DPS: DP1953(cobP)
            SFU: Sfum_2608
            MLO: mll1308
            SME: SMc04305(cobP)
            ATU: Atu1542(cobU)
            ATC: AGR_C_2839(cobP)
            RET: RHE_CH02491(cobP)
            RLE: RL2832(cobP)
            BME: BMEI0693
            BMF: BAB1_1328(cobU)
            BMS: BR1308(cobU)
            BMB: BruAb1_1309(cobU)
            OAN: Oant_1875
            BJA: bll3256(cobP)
            BRA: BRADO4911(cobU)
            BBT: BBta_3140(cobU)
            RPA: RPA0714(cobU)
            RPB: RPB_0740
            RPD: RPD_0638
            RPE: RPE_2234
            XAU: Xaut_3776
            SIL: SPO0405
            RSP: RSP_0602
            RSQ: Rsph17025_0481
            JAN: Jann_0905
            RDE: RD1_1196(cobP)
            HNE: HNE_1521(cobU)
            NAR: Saro_0322
            GBE: GbCGDNIH1_0656
            MAG: amb4425
            MGM: Mmc1_2375
            BHA: BH1590(cobP)
            GKA: GK2261
            LMO: lmo1147
            LMF: LMOf2365_1154(cobU)
            LIN: lin1111
            LWE: lwe1105(cobU)
            STH: STH1928
            CAC: CAC1383(CobU)
            CPE: CPE1035
            CPF: CPF_1290
            CPR: CPR_1109
            CTC: CTC00718
            CNO: NT01CX_2078
            CTH: Cthe_3151
            CDF: CD3438(cobU)
            CBA: CLB_0950(cobU)
            CBH: CLC_0964(cobU)
            CBF: CLI_0996(cobU)
            CKL: CKL_0731(cobU)
            AMT: Amet_3623
            CHY: CHY_0768(cobP)
            DSY: DSY2115(cobU)
            DRM: Dred_1910
            TTE: TTE0381(cobU)
            MTA: Moth_1087
            MTU: Rv0254c(cobU)
            MTC: MT0267(cobU)
            MBO: Mb0260c(cobU)
            MPA: MAP1947(cobU)
            MAV: MAV_2284(cobU)
            MSM: MSMEG_4274(cobU)
            MMC: Mmcs_3304
            CGL: NCgl2119(cgl2199)
            CGB: cg2413(cobU)
            CEF: CE2091
            CDI: DIP1633(cobU)
            NFA: nfa17010(cobU)
            RHA: RHA1_ro01144(cobU)
            SCO: SCO2173(SC5F7.28)
            SMA: SAV6032(cobU)
            PAC: PPA0441
            FRA: Francci3_3129
            FAL: FRAAL5138(cobU)
            ACE: Acel_0941
            SEN: SACE_1651(cobU)
            FNU: FN0913
            TDE: TDE2382(cobU)
            LIL: LB152(cobP)
            LIC: LIC20122(cobU)
            LBJ: LBJ_4190(cobU)
            LBL: LBL_4205(cobU)
            SYN: slr0216(cobP)
            SYW: SYNW1216(cobU)
            SYC: syc0554_d(cobP)
            SYF: Synpcc7942_0990
            SYD: Syncc9605_1328
            SYE: Syncc9902_1146
            SYG: sync_1327
            SYR: SynRCC307_1234(cobU)
            SYX: SynWH7803_1122(cobU)
            CYA: CYA_2240
            CYB: CYB_0367(cobU)
            TEL: tll1104(cobP)
            GVI: glr0747(cobP)
            ANA: all3174
            AVA: Ava_3872
            PMA: Pro0974(cobU)
            PMM: PMM0863(cobU)
            PMT: PMT0749(cobU)
            PMI: PMT9312_0938
            PMB: A9601_09991(cobU)
            PMC: P9515_09441(cobU)
            PMF: P9303_14681(cobU)
            PMG: P9301_09971(cobU)
            PMH: P9215_10301(cobU)
            PME: NATL1_10181(cobU)
            TER: Tery_3432
            BFR: BF2485
            BFS: BF2518(cobP)
            PGI: PG0701(cobU)
            FPS: FP1461(cobU)
            CTE: CT0945(cobP)
            CCH: Cag_0846(cobP)
            PVI: Cvib_0821
            PLT: Plut_1133
            DET: DET0660(cobU-1) DET0694(cobU-2)
            DEH: cbdb_A644(cobU)
            RRS: RoseRS_0575
            RCA: Rcas_0634
            DRA: DR_A0020
            DGE: Dgeo_2873
            APE: APE_2034.1(cobY)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.62
            ExPASy - ENZYME nomenclature database: 2.7.7.62
            ExplorEnz - The Enzyme Database: 2.7.7.62
            ERGO genome analysis and discovery system: 2.7.7.62
            BRENDA, the Enzyme Database: 2.7.7.62
///
ENTRY       EC 2.7.7.63                 Enzyme
NAME        lipoate---protein ligase;
            LplA;
            lipoate protein ligase;
            lipoate-protein ligase A;
            LPL;
            LPL-B
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
SYSNAME     ATP:lipoate adenylyltransferase
REACTION    (1) ATP + lipoate = diphosphate + lipoyl-AMP [RN:R07770];
            (2) lipoyl-AMP + apoprotein = protein N6-(lipoyl)lysine + AMP
            [RN:R07771]
ALL_REAC    R07770 R07771
SUBSTRATE   ATP [CPD:C00002];
            lipoate [CPD:C00725];
            lipoyl-AMP [CPD:C16238];
            apoprotein [CPD:C16240]
PRODUCT     diphosphate [CPD:C00013];
            lipoyl-AMP [CPD:C16238];
            protein N6-(lipoyl)lysine [CPD:C16237];
            AMP [CPD:C00020]
COMMENT     Requires Mg2+. Both 6S- and 6R-lipoates can act as substrates but
            there is a preference for the naturally occurring R-form.
            Selenolipoate, i.e. 5-(1,2-diselenolan-3-yl)pentanoic acid, and
            6-sulfanyloctanoate can also act as substrates, but more slowly [2].
            This enzyme is responsible for lipoylation in the presence of
            exogenous lipoic acid [7]. Lipoylation is essential for the function
            of several key enzymes involved in oxidative metabolism, including
            pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2
            domain), the branched-chain 2-oxoacid dehydrogenases and the glycine
            cleavage system (H protein) [6]. This enzyme attaches lipoic acid to
            the lipoyl domains of these proteins, converting apoproteins into
            holoproteins. It is likely that an alternative pathway, involving EC
            2.3.1.181, lipoyl(octanoyl) transferase and EC 2.8.1.8, lipoyl
            synthase, is the normal route for lipoylation [7].
REFERENCE   1  [PMID:8206909]
  AUTHORS   Morris TW, Reed KE, Cronan JE Jr.
  TITLE     Identification of the gene encoding lipoate-protein ligase A of
            Escherichia coli. Molecular cloning and characterization of the lplA
            gene and gene product.
  JOURNAL   J. Biol. Chem. 269 (1994) 16091-100.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:7639702]
  AUTHORS   Green DE, Morris TW, Green J, Cronan JE Jr, Guest JR.
  TITLE     Purification and properties of the lipoate protein ligase of
            Escherichia coli.
  JOURNAL   Biochem. J. 309 ( Pt 3) (1995) 853-62.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:14700636]
  AUTHORS   Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE.
  TITLE     Assembly of the covalent linkage between lipoic acid and its cognate
            enzymes.
  JOURNAL   Chem. Biol. 10 (2003) 1293-302.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:16141198]
  AUTHORS   Kim do J, Kim KH, Lee HH, Lee SJ, Ha JY, Yoon HJ, Suh SW.
  TITLE     Crystal structure of lipoate-protein ligase A bound with the
            activated intermediate: insights into interaction with lipoyl
            domains.
  JOURNAL   J. Biol. Chem. 280 (2005) 38081-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:16043486]
  AUTHORS   Fujiwara K, Toma S, Okamura-Ikeda K, Motokawa Y, Nakagawa A,
            Taniguchi H.
  TITLE     Crystal structure of lipoate-protein ligase A from Escherichia coli.
            Determination of the lipoic acid-binding site.
  JOURNAL   J. Biol. Chem. 280 (2005) 33645-51.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:9218413]
  AUTHORS   Jordan SW, Cronan JE Jr.
  TITLE     A new metabolic link. The acyl carrier protein of lipid synthesis
            donates lipoic acid to the pyruvate dehydrogenase complex in
            Escherichia coli and mitochondria.
  JOURNAL   J. Biol. Chem. 272 (1997) 17903-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   7  [PMID:10966480]
  AUTHORS   Perham RN.
  TITLE     Swinging arms and swinging domains in multifunctional enzymes:
            catalytic machines for multistep reactions.
  JOURNAL   Annu. Rev. Biochem. 69 (2000) 961-1004.
PATHWAY     PATH: map00785  Lipoic acid metabolism
ORTHOLOGY   KO: K03800  lipoate-protein ligase A
GENES       CME: CMQ023C
            SCE: YJL046W
            AGO: AGOS_AFR609C
            PIC: PICST_58727
            CAL: CaO19_13012(CaO19.13012)
            CGR: CAGL0J04840g
            SPO: SPBC17A3.09c
            ANI: AN5732.2
            AFM: AFUA_1G06950
            AOR: AO090003000080
            CNE: CNB01600
            UMA: UM03661.1
            DDI: DDBDRAFT_0218884
            PFA: PF13_0083
            TAN: TA03985 TA09645
            TPV: TP01_1192
            TBR: Tb927.8.630
            TCR: 510857.50
            LMA: LmjF07.1060
            TVA: TVAG_094820
            ECO: b4386(lplA)
            ECJ: JW4349(lplA)
            ECE: Z5988
            ECS: ECs5345
            ECC: c5471(lplA)
            ECI: UTI89_C5157(lplA)
            ECP: ECP_4770
            ECV: APECO1_1995(lplA)
            STY: STY4923(lplA)
            STT: t4615(lplA)
            SPT: SPA4386(lplA)
            SEC: SC4420(lplA)
            STM: STM4576(lplA)
            YPE: YPO2414(lplA)
            YPK: y1926(lplA)
            YPM: YP_2200(lplA)
            YPA: YPA_1758
            YPN: YPN_1868
            YPP: YPDSF_0736
            YPS: YPTB2322(lplA)
            YEN: YE2184(lplA)
            SSN: SSON_4536(lplA)
            SBO: SBO_4449(lplA)
            SDY: SDY_4647(lplA)
            BFL: Bfl357(lplA)
            BPN: BPEN_368(lplA)
            MSU: MS1058(lplA)
            VCH: VC1388
            PPR: PBPRB1373 PBPRB1808(lplA)
            PCR: Pcryo_0197
            ILO: IL0300(lplA)
            FTU: FTT0690c(lplA)
            FTF: FTF0690c(lplA)
            FTL: FTL_0967
            FTH: FTH_0944(lplA)
            FTN: FTN_0993(lplA)
            AHA: AHA_2967
            BPE: BP1297
            BPA: BPP2921
            BBR: BB2891
            GSU: GSU0379
            GME: Gmet_3151
            PPD: Ppro_2238
            BBA: Bd2507(lplA)
            DPS: DP2092 DPPB42
            BSU: BG11701(yqhM) BG13055(yhfJ)
            BHA: BH0683(lplA) BH2812
            BAN: BA1089 BA4431
            BAR: GBAA1089 GBAA4431
            BAA: BA_1640 BA_4884
            BAT: BAS1017 BAS4111
            BCE: BC1086 BC4209
            BCA: BCE_1189 BCE_4284
            BCZ: BCZK1004(lplA) BCZK3962(lplA)
            BTK: BT9727_1001(lplA) BT9727_3952(lplA)
            BTL: BALH_0968 BALH_3813(lplA)
            BLI: BL01079 BL01548(yqhM)
            BLD: BLi01102(yhfJ) BLi02624(yqhM)
            BCL: ABC1613 ABC2491
            BPU: BPUM_0968(yhfJ) BPUM_3400
            OIH: OB1174 OB1283
            GKA: GK2420
            SAU: SA0316 SA0884 SA1363
            SAV: SAV0327 SAV1028 SAV1533
            SAM: MW0304 MW0908 MW1485
            SAR: SAR0324 SAR0997 SAR1610
            SAS: SAS0304 SAS0960 SAS1471
            SAC: SACOL0398 SACOL1034 SACOL1591
            SAB: SAB0277 SAB0893c SAB1405c
            SAA: SAUSA300_0328 SAUSA300_0930 SAUSA300_1494
            SAO: SAOUHSC_00308 SAOUHSC_00963 SAOUHSC_01629
            SEP: SE0728 SE1217
            SER: SERP0616 SERP1097
            SHA: SH0263 SH1383 SH1931(lplA)
            SSP: SSP1222 SSP1757
            LMO: lmo0764 lmo0931
            LMF: LMOf2365_0788 LMOf2365_0952
            LIN: lin0758 lin0931
            LWE: lwe0725 lwe0911
            LLA: L64373(lplL)
            LLC: LACR_0052
            LLM: llmg_0075(lplL)
            SPY: SPy_1033 SPy_1214(lplA)
            SPZ: M5005_Spy_0758(lplB) M5005_Spy_0928(lplA)
            SPM: spyM18_1015 spyM18_1166(lplA)
            SPG: SpyM3_0666 SpyM3_0854(lplA)
            SPS: SPs1054 SPs1187
            SPH: MGAS10270_Spy0875(lplB) MGAS10270_Spy1042(lplA)
            SPI: MGAS10750_Spy0910(lplB) MGAS10750_Spy1077(lplA)
            SPJ: MGAS2096_Spy0832(lplB) MGAS2096_Spy0987(lplA)
            SPK: MGAS9429_Spy0872(lplB) MGAS9429_Spy1031(lplA)
            SPA: M6_Spy0783 M6_Spy0917
            SPB: M28_Spy0737(lplB) M28_Spy0900(lplA)
            SPN: SP_1160
            SPR: spr1047(lplA)
            SPD: SPD_1024
            SAG: SAG0882(lplA-1) SAG1056(lplA-2)
            SAN: gbs0899 gbs1090
            SAK: SAK_1005(lplA) SAK_1145(lplA)
            SMU: SMU.131(lplA)
            STC: str1009(lplA)
            STL: stu1009(lplA)
            STE: STER_1014
            SSA: SSA_1173(lplA)
            SSU: SSU05_1836
            SSV: SSU98_1835
            LPL: lp_2643(lplA1) lp_2734(lplA2)
            LSA: LSA0934(lplA)
            LSL: LSL_0157(lplA)
            LBR: LVIS_0180 LVIS_1647 LVIS_1950
            LCA: LSEI_1473
            PPE: PEPE_1774
            EFA: EF0650(lplA-1) EF2741(lplA-2)
            OOE: OEOE_0327 OEOE_1555
            LME: LEUM_0736
            STH: STH1918 STH561
            CTC: CTC02045
            CDF: CD0046 CD0733 CD1654(lplA)
            CHY: CHY_0495
            DSY: DSY1742
            SWO: Swol_1974
            TTE: TTE0297(lplA)
            MTA: Moth_0443 Moth_1939
            MGE: MG_270(lpla)
            MPN: MPN389(lplA)
            MPU: MYPU_0320(lplA) MYPU_4430(lplA)
            MPE: MYPE8650(lplA)
            MGA: MGA_0158(lplA)
            MMY: MSC_0264(lplA) MSC_0527(lplA)
            MMO: MMOB0580(lplA)
            MHY: mhp125(lplA) mhp323(lplA)
            MHJ: MHJ_0246(lplA) MHJ_0302(lplA-1)
            MHP: MHP7448_0254(lplA) MHP7448_0310(lplA-1)
            MSY: MS53_0060(lplA)
            MCP: MCAP_0224 MCAP_0449
            POY: PAM309(lplA)
            AYW: AYWB_412(lplA)
            MFL: Mfl038
            CGL: NCgl1029(cgl1074)
            CGB: cg1222(lplA)
            CEF: CE1123
            SCO: SCO6423(SC1A6.12c)
            ART: Arth_2128
            AAU: AAur_2129
            SEN: SACE_3586(lplA)
            BLO: BL1217(snoP)
            BAD: BAD_1338(snoP)
            RXY: Rxyl_0450
            RBA: RB7072(lplA) RB7583(lplA)
            CTR: CT285(lplA_1) CT499(lplA_2)
            CTA: CTA_0307(lplA_1) CTA_0547(lplA_2)
            CMU: TC0558 TC0786
            CPN: CPn0436(lplA_1) CPn0618(lplA_2)
            CPA: CP0129 CP0317
            CPJ: CPj0436(lplA_1) CPj0618(lplA_2)
            CPT: CpB0452 CpB0644
            CCA: CCA00122 CCA00356
            CAB: CAB121 CAB347
            CFE: CF0651(lplA2) CF0884(lplA1)
            PCU: pc0276 pc1838(lplA)
            TDE: TDE1551 TDE2647
            LIL: LA1410
            LIC: LIC12334(lplA)
            LBJ: LBJ_2131(lplA)
            LBL: LBL_2128(lplA)
            SYN: sll0809
            SYW: SYNW1731
            SYC: syc0144_d
            SYF: Synpcc7942_1411
            SYD: Syncc9605_0735
            SYE: Syncc9902_1628
            SYG: sync_1982
            CYA: CYA_1633
            CYB: CYB_1281
            TEL: tlr0228
            GVI: glr3295
            ANA: alr1961
            AVA: Ava_4350
            PMA: Pro0540(lplA)
            PMM: PMM0539
            PMT: PMT1224
            PMN: PMN2A_1869
            PMI: PMT9312_0539
            PMB: A9601_05951(lplA)
            PMC: P9515_06031(lplA)
            PMF: P9303_07881(lplA)
            PMG: P9301_05651(lplA)
            PME: NATL1_05941(lplA)
            TER: Tery_3831
            BTH: BT_0310
            BFR: BF1619
            BFS: BF1632(lplA)
            SRU: SRU_0239
            CTE: CT1342
            CCH: Cag_0906
            PLT: Plut_1329
            AAE: aq_1638(lplA) aq_264
            TMA: TM0708
            HAL: VNG0181G(lpl) VNG6256G(lipB)
            HMA: rrnAC2019(lpl)
            NPH: NP5116A(lpl_1)
            TAC: Ta0514
            TVO: TVN0991
            PHO: PH1487
            PAB: PAB1916
            PFU: PF1374
            TKO: TK1908
            APE: APE_2341 APE_2342.1(lipB)
            SMR: Smar_0191
            HBU: Hbut_0801
            SSO: SSO1112(lplA-like2) SSO3157(lplA-1) SSO3159(lplA-2)
            STO: ST1193 ST1888
            SAI: Saci_0307 Saci_0310 Saci_0345
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.63
            ExPASy - ENZYME nomenclature database: 2.7.7.63
            ExplorEnz - The Enzyme Database: 2.7.7.63
            ERGO genome analysis and discovery system: 2.7.7.63
            BRENDA, the Enzyme Database: 2.7.7.63
///
ENTRY       EC 2.7.7.64                 Enzyme
NAME        UTP-monosaccharide-1-phosphate uridylyltransferase;
            UDP-sugar pyrophosphorylase;
            PsUSP
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
REACTION    UTP + a monosaccharide 1-phosphate = diphosphate +
            UDP-monosaccharide
SUBSTRATE   UTP [CPD:C00075];
            monosaccharide 1-phosphate
PRODUCT     diphosphate [CPD:C00013];
            UDP-monosaccharide
COMMENT     Requires Mg2+ or Mn2+ for maximal activity. The reaction can occur
            in either direction and it has been postulated that MgUTP and
            Mg-diphosphate are the actual substrates [1,2]. The enzyme catalyses
            the formation of UDP-Glc, UDP-Gal, UDP-GlcA, UDP-L-Ara and UDP-Xyl,
            showing broad substrate specificity towards monosaccharide
            1-phosphates. Mannose 1-phosphate, L-Fucose 1-phosphate and glucose
            6-phosphate are not substrates and UTP cannot be replaced by other
            nucleotide triphosphates [1].
REFERENCE   1  [PMID:15326166]
  AUTHORS   Kotake T, Yamaguchi D, Ohzono H, Hojo S, Kaneko S, Ishida HK,
            Tsumuraya Y.
  TITLE     UDP-sugar pyrophosphorylase with broad substrate specificity toward
            various monosaccharide 1-phosphates from pea sprouts.
  JOURNAL   J. Biol. Chem. 279 (2004) 45728-36.
REFERENCE   2  [PMID:4430676]
  AUTHORS   Rudick VL, Weisman RA.
  TITLE     Uridine diphosphate glucose pyrophosphorylase of Acanthamoeba
            castellanii. Purification, kinetic, and developmental studies.
  JOURNAL   J. Biol. Chem. 249 (1974) 7832-40.
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.7.64
            ExPASy - ENZYME nomenclature database: 2.7.7.64
            ExplorEnz - The Enzyme Database: 2.7.7.64
            ERGO genome analysis and discovery system: 2.7.7.64
            BRENDA, the Enzyme Database: 2.7.7.64
///
ENTRY       EC 2.7.7.-                  Enzyme
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Nucleotidyltransferases
REACTION    L-Serine + ATP <=> (L-Seryl)adenylate + Pyrophosphate [RN:R00580]
SUBSTRATE   L-Serine [CPD:C00065];
            ATP [CPD:C00002]
PRODUCT     (L-Seryl)adenylate [CPD:C05820];
            Pyrophosphate [CPD:C00013]
///
ENTRY       EC 2.7.8.1                  Enzyme
NAME        ethanolaminephosphotransferase;
            EPT;
            diacylglycerol ethanolaminephosphotransferase;
            CDPethanolamine diglyceride phosphotransferase;
            phosphorylethanolamine-glyceride transferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     CDP-ethanolamine:1,2-diacylglycerol ethanolaminephosphotransferase
REACTION    CDP-ethanolamine + 1,2-diacylglycerol = CMP + a
            phosphatidylethanolamine [RN:R02057]
ALL_REAC    R02057;
            (other) R04920 R06364 R07384
SUBSTRATE   CDP-ethanolamine [CPD:C00570];
            1,2-diacylglycerol [CPD:C00641]
PRODUCT     CMP [CPD:C00055];
            phosphatidylethanolamine [CPD:C00350]
REFERENCE   1  [PMID:13366993]
  AUTHORS   KENNEDY EP, WEISS SB.
  TITLE     The function of cytidine coenzymes in the biosynthesis of
            phospholipides.
  JOURNAL   J. Biol. Chem. 222 (1956) 193-214.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00440  Aminophosphonate metabolism
            PATH: map00564  Glycerophospholipid metabolism
            PATH: map00565  Ether lipid metabolism
ORTHOLOGY   KO: K00993  ethanolaminephosphotransferase
GENES       CEL: F22E10.5(phosphotransferase)
            ATH: AT1G13560(AAPT1)
            OSA: 4328107
            SCE: YHR123W(EPT1)
            AGO: AGOS_AGR344W
            PIC: PICST_40464(EPT1)
            CGR: CAGL0L13068g
            SPO: SPAC22A12.10
            ANI: AN4778.2
            AFM: AFUA_3G06650
            AOR: AO090020000334
            CNE: CNF04740
            DDI: DDBDRAFT_0216903 DDBDRAFT_0218127
            PFA: PFF1375c
            CPV: cgd4_2790
            CHO: Chro.40314
            TAN: TA09530
            TPV: TP01_1171
            TBR: Tb10.6k15.1570
            TCR: 509791.150
            LMA: LmjF36.5900
            EHI: 78.t00028
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.1
            ExPASy - ENZYME nomenclature database: 2.7.8.1
            ExplorEnz - The Enzyme Database: 2.7.8.1
            ERGO genome analysis and discovery system: 2.7.8.1
            BRENDA, the Enzyme Database: 2.7.8.1
            CAS: 9026-19-1
///
ENTRY       EC 2.7.8.2                  Enzyme
NAME        diacylglycerol cholinephosphotransferase;
            phosphorylcholine-glyceride transferase;
            alkylacylglycerol cholinephosphotransferase;
            1-alkyl-2-acetylglycerol cholinephosphotransferase;
            cholinephosphotransferase;
            CPT;
            alkylacylglycerol choline phosphotransferase;
            diacylglycerol choline phosphotransferase;
            1-alkyl-2-acetyl-m-glycerol:CDPcholine choline phosphotransferase;
            CDP-choline diglyceride phosphotransferase;
            cytidine diphosphocholine glyceride transferase;
            cytidine diphosphorylcholine diglyceride transferase;
            phosphocholine diacylglyceroltransferase;
            sn-1,2-diacylglycerol cholinephosphotransferase;
            1-alkyl-2-acetyl-sn-glycerol cholinephosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     CDP choline:1,2-diacylglycerol cholinephosphotransferase
REACTION    CDP-choline + 1,2-diacylglycerol = CMP + a phosphatidylcholine
            [RN:R01321]
ALL_REAC    R01321;
            (other) R04321 R04922 R07389
SUBSTRATE   CDP-choline [CPD:C00307];
            1,2-diacylglycerol [CPD:C00641]
PRODUCT     CMP [CPD:C00055];
            phosphatidylcholine [CPD:C00157]
COMMENT     1-Alkyl-2-acylglycerol can act as acceptor; this activity was
            previously listed separately.
REFERENCE   1  [PMID:192727]
  AUTHORS   Coleman R, Bell RM.
  TITLE     Phospholipid synthesis in isolated fat cells. Studies of microsomal
            diacylglycerol cholinephosphotransferase and diacylglycerol
            ethanolaminephosphotransferase activities.
  JOURNAL   J. Biol. Chem. 252 (1977) 3050-6.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6295501]
  AUTHORS   Lee TC, Blank ML, Fitzgerald V, Snyder F.
  TITLE     Formation of alkylacyl- and diacylglycerophosphocholines via
            diradylglycerol cholinephosphotransferase in rat liver.
  JOURNAL   Biochim. Biophys. Acta. 713 (1982) 479-83.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:204847]
  AUTHORS   Parthasarathy S, Cady RK, Kraushaar DS, Sladek NE, Baumann WJ.
  TITLE     Inhibition of diacylglycerol:CDPcholine cholinephosphotransferase
            activity by dimethylaminoethyl p-chlorophenoxyacetate.
  JOURNAL   Lipids. 13 (1978) 161-4.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:6260215]
  AUTHORS   Renooij W, Snyder F.
  TITLE     Biosynthesis of 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine
            (platelet activating factor and a hypotensive lipid) by
            cholinephosphotransferase in various rat tissues.
  JOURNAL   Biochim. Biophys. Acta. 663 (1981) 545-56.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00440  Aminophosphonate metabolism
            PATH: map00564  Glycerophospholipid metabolism
            PATH: map00565  Ether lipid metabolism
ORTHOLOGY   KO: K00994  diacylglycerol cholinephosphotransferase
GENES       HSA: 56994(CHPT1)
            CFA: 610214(CHPT1)
            SCE: YNL130C(CPT1)
            TET: TTHERM_00656030
            TPA: TP0671
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.2
            ExPASy - ENZYME nomenclature database: 2.7.8.2
            ExplorEnz - The Enzyme Database: 2.7.8.2
            ERGO genome analysis and discovery system: 2.7.8.2
            BRENDA, the Enzyme Database: 2.7.8.2
            CAS: 9026-13-5
///
ENTRY       EC 2.7.8.3                  Enzyme
NAME        ceramide cholinephosphotransferase;
            phosphorylcholine-ceramide transferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     CDP-choline:N-acylsphingosine cholinephosphotransferase
REACTION    CDP-choline + N-acylsphingosine = CMP + sphingomyelin [RN:R01891]
ALL_REAC    R01891
SUBSTRATE   CDP-choline [CPD:C00307];
            N-acylsphingosine [CPD:C00195]
PRODUCT     CMP [CPD:C00055];
            sphingomyelin [CPD:C00550]
REFERENCE   1
  AUTHORS   Kennedy, E.P.
  TITLE     Phosphorylcholine-glyceride transferase.
  JOURNAL   Methods Enzymol. 5 (1962) 484-486.
  ORGANISM  chicken [GN:gga]
REFERENCE   2
  AUTHORS   Sribney, M. and Kennedy, E.P.
  TITLE     The enzymatic synthesis of sphingomyelin.
  JOURNAL   J. Biol. Chem. 233 (1958) 1315-1322.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00600  Sphingolipid metabolism
ORTHOLOGY   KO: K04714  ceramide cholinephosphotransferase
GENES       HSA: 166929(SGMS2) 259230(SGMS1)
            MMU: 208449(Sgms1) 74442(Sgms2)
            RNO: 353229(Tmem23)
            CFA: 477582(SGMS1)
            GGA: 378907(SGMS1) 422529(SGMS2)
            XTR: 496853(LOC496853)
            CEL: F53H8.4(sms-2) H21P03.3(sms-1) Y22D7AL.8(sms-3)
            EHI: 204.t00003
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.3
            ExPASy - ENZYME nomenclature database: 2.7.8.3
            ExplorEnz - The Enzyme Database: 2.7.8.3
            ERGO genome analysis and discovery system: 2.7.8.3
            BRENDA, the Enzyme Database: 2.7.8.3
            CAS: 9026-14-6
///
ENTRY       EC 2.7.8.4                  Enzyme
NAME        serine-phosphoethanolamine synthase;
            serine ethanolamine phosphate synthetase;
            serine ethanolamine phosphodiester synthase;
            serine ethanolaminephosphotransferase;
            serine-phosphinico-ethanolamine synthase;
            serinephosphoethanolamine synthase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     CDP-ethanolamine:L-serine ethanolamine phosphotransferase
REACTION    CDP-ethanolamine + L-serine = CMP + L-serine-phosphoethanolamine
            [RN:R02563]
ALL_REAC    R02563
SUBSTRATE   CDP-ethanolamine [CPD:C00570];
            L-serine [CPD:C00065]
PRODUCT     CMP [CPD:C00055];
            L-serine-phosphoethanolamine [CPD:C03872]
REFERENCE   1  [PMID:5636380]
  AUTHORS   Allen AK, Rosenberg H.
  TITLE     The mechanism of action and some properties of serine ethanolamine
            phosphate synthetase.
  JOURNAL   Biochim. Biophys. Acta. 151 (1968) 504-19.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.4
            ExPASy - ENZYME nomenclature database: 2.7.8.4
            ExplorEnz - The Enzyme Database: 2.7.8.4
            ERGO genome analysis and discovery system: 2.7.8.4
            BRENDA, the Enzyme Database: 2.7.8.4
            CAS: 9023-23-8
///
ENTRY       EC 2.7.8.5                  Enzyme
NAME        CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase;
            glycerophosphate phosphatidyltransferase;
            3-phosphatidyl-1'-glycerol-3'-phosphate synthase;
            CDPdiacylglycerol:glycerol-3-phosphate phosphatidyltransferase;
            cytidine 5'-diphospho-1,2-diacyl-sn-glycerol
            (CDPdiglyceride):sn-glycerol-3-phosphate phosphatidyltransferase;
            phosphatidylglycerophosphate synthase;
            phosphatidylglycerolphosphate synthase;
            PGP synthase;
            CDPdiacylglycerol-sn-glycerol-3-phosphate 3-phosphatidyltransferase;
            CDPdiacylglycerol:sn-glycero-3-phosphate phosphatidyltransferase;
            glycerol phosphate phosphatidyltransferase;
            glycerol 3-phosphate phosphatidyltransferase;
            phosphatidylglycerol phosphate synthase;
            phosphatidylglycerol phosphate synthetase;
            phosphatidylglycerophosphate synthetase;
            sn-glycerol-3-phosphate phosphatidyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     CDP-diacylglycerol:sn-glycerol-3-phosphate 3-phosphatidyltransferase
REACTION    CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP +
            3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate [RN:R01801]
ALL_REAC    R01801
SUBSTRATE   CDP-diacylglycerol [CPD:C00269];
            sn-glycerol 3-phosphate [CPD:C00093]
PRODUCT     CMP [CPD:C00055];
            3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate [CPD:C03892]
REFERENCE   1  [PMID:7074121]
  AUTHORS   Bleasdale JE, Johnston JM.
  TITLE     CMP-dependent incorporation of [14C]Glycerol 3-phosphate into
            phosphatidylglycerol and phosphatidylglycerol phosphate by rabbit
            lung microsomes.
  JOURNAL   Biochim. Biophys. Acta. 710 (1982) 377-90.
  ORGANISM  rabbit
REFERENCE   2  [PMID:793612]
  AUTHORS   Hirabayashi T, Larson TJ, Dowhan W.
  TITLE     Membrane-associated phosphatidylglycerophosphate synthetase from
            Escherichia coli: purification by substrate affinity chromatography
            on cytidine 5'-diphospho-1,2-diacyl-sn-glycerol sepharose.
  JOURNAL   Biochemistry. 15 (1976) 5205-11.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00995  CDP-diacylglycerol--glycerol-3-phosphate
                        3-phosphatidyltransferase
GENES       ATH: AT2G39290(PGPS1) AT3G55030(PGPS2)
            OSA: 4332460
            CME: CMN196C
            SCE: YDL142C(CRD1)
            AGO: AGOS_ADR084C
            PIC: PICST_52642(CRD2)
            AFM: AFUA_6G04460
            UMA: UM05220.1
            PFA: MAL8P1.58
            TAN: TA16500
            TPV: TP01_1130
            TBR: Tb927.8.1720
            TCR: 505071.100 511395.20
            LMA: LmjF07.0200
            ECO: b1912(pgsA)
            ECJ: JW1897(pgsA)
            ECE: Z3000(pgsA)
            ECS: ECs2650
            ECC: c2325(pgsA)
            ECI: UTI89_C2113(pgsA)
            ECP: ECP_1852
            ECV: APECO1_559(ynbA) APECO1_954(pgsA)
            ECW: EcE24377A_2145(pgsA)
            ECX: EcHS_A2010
            STY: STY2153(pgsA)
            STT: t0931(pgsA)
            SPT: SPA0924(pgsA)
            SEC: SC1948(pgsA)
            STM: STM1945(pgsA)
            YPE: YPO1867(pgsA)
            YPK: y2441(pgsA)
            YPM: YP_1526(pgsA2)
            YPA: YPA_1245
            YPN: YPN_2257
            YPP: YPDSF_1259
            YPS: YPTB1737(pgsA)
            YPI: YpsIP31758_2251(pgsA)
            SFL: SF1955(pgsA)
            SFX: S2051(pgsA)
            SFV: SFV_1956(pgsA)
            SSN: SSON_1206(pgsA)
            SBO: SBO_1094(pgsA)
            SDY: SDY_1106(pgsA)
            ECA: ECA2880(pgsA)
            PLU: plu2026(pgsA)
            WBR: WGLp315(pgsA)
            SGL: SG1172
            ENT: Ent638_2499
            BFL: Bfl415(pgsA)
            BPN: BPEN_427(pgsA)
            HIN: HI0123(pgsA)
            HIT: NTHI0213(pgsA)
            HDU: HD1813(pgsA)
            HSO: HS_1153(pgsA)
            PMU: PM0856(pgsA)
            MSU: MS0959(pgsA)
            APL: APL_0275(pgsA)
            ASU: Asuc_1699
            XFA: XF2310
            XFT: PD1326(pgsA)
            XCC: XCC0499(pgsA) XCC2114(pgsA)
            XCB: XC_0511 XC_2001
            XCV: XCV0548(pgsA) XCV2260(pgsA)
            XAC: XAC0514(pgsA) XAC2093(pgsA)
            XOO: XOO2291(pgsA)
            XOM: XOO_0507(XOO0507) XOO_2169(XOO2169)
            VCH: VC1215
            VCO: VC0395_A0835(pgsA)
            VVU: VV1_3052
            VVY: VV1235
            VPA: VP1943
            VFI: VF1625 VFA0094
            PPR: PBPRA2236
            PAE: PA2541 PA2584(pgsA)
            PAU: PA14_30670(pgsA) PA14_31700(pgsA)
            PAP: PSPA7_2615(pgsA)
            PPU: PP_4097(pgsA)
            PPF: Pput_1767
            PST: PSPTO_3022(pgsA) PSPTO_5536
            PSB: Psyr_2895
            PSP: PSPPH_2330(pgsA)
            PFL: PFL_3561(pgsA) PFL_6195
            PFO: Pfl_3065
            PEN: PSEEN0710 PSEEN3448(pgsA)
            PMY: Pmen_2373
            PAR: Psyc_0185(pgsA)
            PCR: Pcryo_0206
            ACI: ACIAD0342(pgsA)
            SON: SO_1862(pgsA)
            SDN: Sden_1438
            SFR: Sfri_2647
            SAZ: Sama_1609
            SBL: Sbal_2560
            SBM: Shew185_2598
            SLO: Shew_1826
            SPC: Sputcn32_1641
            SHE: Shewmr4_1549
            SHM: Shewmr7_1616
            SHN: Shewana3_1610
            SHW: Sputw3181_2384
            ILO: IL0652(pgsA)
            CPS: CPS_3269(pgsA)
            PHA: PSHAa1914(pgsA)
            PAT: Patl_2448
            SDE: Sde_2052
            PIN: Ping_1194
            MAQ: Maqu_1193
            CBU: CBU_1034(pgsA)
            CBD: COXBU7E912_1012(pgsA)
            LPN: lpg2293(pgsA) lpg2801
            LPF: lpl2212(pgsA) lpl2716
            LPP: lpp2240(pgsA) lpp2847
            MCA: MCA0372 MCA1682(pgsA)
            FTU: FTT0320(pgsA)
            FTF: FTF0320(pgsA)
            FTW: FTW_1762(pgsA)
            FTL: FTL_0231
            FTH: FTH_0226(pgsA)
            FTA: FTA_0247(pgsA)
            FTN: FTN_0234(pgsA)
            TCX: Tcr_1146
            NOC: Noc_1186 Noc_1643 Noc_1725 Noc_2982
            AEH: Mlg_1363
            HHA: Hhal_0021
            HCH: HCH_01908 HCH_04043(pgsA)
            CSA: Csal_2134
            ABO: ABO_1306(pgsA)
            AHA: AHA_2772(pgsA)
            DNO: DNO_0306(pgsA)
            BCI: BCI_0240(pgsA)
            VOK: COSY_0157(pgsA)
            NME: NMB1588
            NMA: NMA1779(pgsA)
            NMC: NMC1509(pgsA)
            NGO: NGO1247
            CVI: CV_1306(pgsA) CV_4039
            RSO: RSc1072(pgsA)
            REU: Reut_A2243 Reut_B4011
            REH: H16_A2546
            RME: Rmet_2409
            BMA: BMA0553(pgsA)
            BMV: BMASAVP1_A1261(citG) BMASAVP1_A2455(pgsA)
            BML: BMA10299_A0609(citG) BMA10299_A2825(pgsA)
            BMN: BMA10247_1778(pgsA)
            BXE: Bxe_A1096
            BVI: Bcep1808_1063
            BUR: Bcep18194_A4256 Bcep18194_A4519
            BCN: Bcen_0664 Bcen_0892
            BCH: Bcen2424_1144 Bcen2424_1374
            BAM: Bamb_1020 Bamb_1252
            BPS: BPSL2419
            BPM: BURPS1710b_2883(pgsA)
            BPL: BURPS1106A_2828(pgsA)
            BPD: BURPS668_2768(pgsA)
            BTE: BTH_I1740(pgsA)
            PNU: Pnuc_0416
            BPE: BP2082(pgsA)
            BPA: BPP1766(pgsA)
            BBR: BB3342(pgsA)
            RFR: Rfer_2245
            POL: Bpro_3070
            PNA: Pnap_1628
            AAV: Aave_1665
            AJS: Ajs_2622
            VEI: Veis_2699
            MPT: Mpe_A1958
            HAR: HEAR2056(pgsA)
            MMS: mma_1377
            NEU: NE2127(pgsA)
            NET: Neut_2079
            NMU: Nmul_A1272
            EBA: ebA5549(pgsA)
            AZO: azo1649(pgsA)
            DAR: Daro_2039
            TBD: Tbd_0700 Tbd_2007
            MFA: Mfla_1803
            HPY: HP1016(pgsA)
            HPA: HPAG1_0430
            HHE: HH1680(pgsA)
            HAC: Hac_1120(pgsA)
            WSU: WS2223(pgsA)
            TDN: Tmden_1233
            CJE: Cj1067(pgsA)
            CJR: CJE1210(pgsA)
            CJJ: CJJ81176_1085(pgsA)
            CJU: C8J_1008(pgsA)
            CJD: JJD26997_0656(pgsA)
            CFF: CFF8240_0782(pgsA)
            CCV: CCV52592_1136(pgsA)
            CHA: CHAB381_0585(pgsA)
            CCO: CCC13826_0122(pgsA)
            ABU: Abu_0872(pgsA)
            NIS: NIS_0697(pgsA)
            SUN: SUN_0807(pgsA) SUN_1448
            GSU: GSU1825(pgsA)
            GME: Gmet_0822 Gmet_1952
            PCA: Pcar_1307 Pcar_2777
            DVU: DVU1846(pgsA)
            DDE: Dde_2074
            LIP: LI0373(pgsA)
            BBA: Bd1917(pgsA)
            DPS: DP0426
            ADE: Adeh_1983 Adeh_3563
            MXA: MXAN_4626(pgsA) MXAN_7302
            SAT: SYN_01716 SYN_02166
            SFU: Sfum_0049 Sfum_0423
            RPR: RP049
            RTY: RT0081(pgsA)
            RCO: RC0075(pgsA)
            RFE: RF_0130(pgsA)
            RBE: RBE_0010(pgsA)
            OTS: OTBS_1929(pgsA)
            WOL: WD0487(pgsA)
            WBM: Wbm0673
            AMA: AM1100(pgsA)
            APH: APH_1206(pgsA)
            ERU: Erum8300(pgsA)
            ERW: ERWE_CDS_08790(pgsA)
            ERG: ERGA_CDS_08700(pgsA)
            ECN: Ecaj_0867
            ECH: ECH_1078(pgsA)
            NSE: NSE_0009(pgsA)
            PUB: SAR11_0085(pgsA)
            MLO: mlr7913 mlr7964
            MES: Meso_1965 Meso_1976
            PLA: Plav_2275
            SME: SMc00601(pgsA)
            ATU: Atu1128(pgsA)
            ATC: AGR_C_2087
            RET: RHE_CH01478(pgsAch) RHE_CH03135 RHE_PB00101(pgsAb)
            RLE: RL1586(pgsA) pRL90202
            BME: BMEI1252
            BMF: BAB1_0719(pgsA)
            BMS: BR0698(pgsA)
            BMB: BruAb1_0717(pgsA)
            BOV: BOV_0689(pgsA)
            BJA: bll4124 blr7471(pgsA)
            BRA: BRADO3343 BRADO6057(pgsA)
            BBT: BBta_3851
            RPA: RPA1170(pgsA) RPA3050
            RPB: RPB_1176 RPB_2490
            RPC: RPC_0902 RPC_2327
            RPD: RPD_1280 RPD_2954
            RPE: RPE_0925 RPE_3283
            NWI: Nwi_1596 Nwi_2525
            NHA: Nham_2117 Nham_3145
            BHE: BH05540(pgsA)
            BQU: BQ04700(pgsA)
            BBK: BARBAKC583_0515(pgsA)
            CCR: CC_2908
            SIL: SPO3635(pgsA)
            SIT: TM1040_3631
            RSP: RSP_1073(pgsA)
            JAN: Jann_3918
            RDE: RD1_2347 RD1_4086(pgsA)
            MMR: Mmar10_0768
            HNE: HNE_0456(pgsA)
            ZMO: ZMO0096(pgsA)
            NAR: Saro_1335
            SAL: Sala_1154
            ELI: ELI_03945
            GOX: GOX2274
            GBE: GbCGDNIH1_2036 GbCGDNIH1_2083
            RRU: Rru_A2165 Rru_A2221
            MAG: amb3799
            MGM: Mmc1_1878 Mmc1_2314
            ABA: Acid345_0551 Acid345_3995 Acid345_4113
            SUS: Acid_6304
            BSU: BG11373(pgsA)
            BHA: BH2386(pgsA)
            BAN: BA3917(pgsA)
            BAR: GBAA3917(pgsA)
            BAA: BA_4388
            BAT: BAS3631
            BCE: BC3781
            BCA: BCE_3816(pgsA)
            BCZ: BCZK3541(pgsA)
            BCY: Bcer98_2433
            BTK: BT9727_3523(pgsA)
            BLI: BL01195(pgsA)
            BLD: BLi01916(pgsA)
            BCL: ABC2202(pgsA)
            BAY: RBAM_016760
            BPU: BPUM_1596
            OIH: OB1622(pgsA)
            GKA: GK1293(pgsA)
            SAU: SA1126(pgsA)
            SAV: SAV1283(pgsA)
            SAM: MW1166(pgsA)
            SAR: SAR1259(pgsA)
            SAS: SAS1217
            SAC: SACOL1302(pgsA)
            SAB: SAB1145(pgsA)
            SAA: SAUSA300_1176(pgsA)
            SAO: SAOUHSC_01260
            SEP: SE0960
            SER: SERP0850(pgsA)
            SHA: SH1630(pgsA)
            SSP: SSP1482
            LMO: lmo1396
            LMF: LMOf2365_1415(pgsA)
            LIN: lin1433
            LWE: lwe1412(pgsA)
            LLA: L29672(pgsA)
            LLC: LACR_2233
            LLM: llmg_2224(pgsA)
            SPY: SPy_2196(pgsA)
            SPZ: M5005_Spy_1847
            SPM: spyM18_2231
            SPG: SpyM3_1847(pgsA)
            SPS: SPs1843
            SPH: MGAS10270_Spy1966
            SPI: MGAS10750_Spy1963
            SPJ: MGAS2096_Spy1878
            SPK: MGAS9429_Spy1858
            SPF: SpyM51819(pgsA)
            SPA: M6_Spy1864
            SPB: M28_Spy1879
            SPN: SP_2222
            SPR: spr2027(pgsA)
            SPD: SPD_2049(pgsA)
            SAG: SAG2152(pgsA)
            SAN: gbs2111(pgsA)
            SAK: SAK_2110(pgsA)
            SMU: SMU.2151(pgsA)
            STC: str2010(pgsA)
            STL: stu2010(pgsA)
            SSA: SSA_2368(pgsA)
            SGO: SGO_0014(pgsA)
            LPL: lp_2303(pgsA)
            LAC: LBA0664(pgsA)
            LSA: LSA0486(pgsA)
            LSL: LSL_1131(pgsA)
            LDB: Ldb0598(pgsA)
            LBU: LBUL_0534
            LBR: LVIS_1239
            LCA: LSEI_0921
            EFA: EF3148(pgsA)
            OOE: OEOE_1383
            CAC: CAC1814(pgsA) CAC3596(pgsA)
            CPE: CPE1674
            CPF: CPF_1928(pgsA)
            CPR: CPR_0545 CPR_1646(pgsA)
            CTC: CTC00117 CTC01288
            CNO: NT01CX_2124(pgsA)
            CTH: Cthe_0941
            CDF: CD1327(pgsA)
            CBA: CLB_2269(pgsA)
            CBH: CLC_2252(pgsA)
            CBF: CLI_2461(pgsA)
            CKL: CKL_1444(pgsA)
            DSY: DSY1965
            DRM: Dred_1925
            SWO: Swol_1261
            TTE: TTE0757(pgsA) TTE1376(pgsA2)
            MTA: Moth_1075
            MGE: MG_114(pgsA)
            MPN: MPN253(pgsA)
            MPU: MYPU_1680(pgsA)
            MPE: MYPE4050(pgsA)
            MGA: MGA_1067(pgsA)
            MMY: MSC_0911(pgsA)
            MMO: MMOB3570(pgsA)
            MHY: mhp099(psgA)
            MHJ: MHJ_0273(pgsA)
            MHP: MHP7448_0281(pgsA)
            MSY: MS53_0494(pgsA)
            MCP: MCAP_0808(pgsA)
            UUR: UU364(psgA)
            POY: PAM718
            AYW: AYWB_053(pgsA)
            MFL: Mfl663
            MTU: Rv1822(pgsA2) Rv2746c(pgsA3)
            MTC: MT1870(pgsA-1) MT2687 MT2817(pgsA-2)
            MBO: Mb1853(pgsA2) Mb2767c(pgsA3)
            MBB: BCG_1857(pgsA2) BCG_2762c(pgsA3)
            MLE: ML0454(pgsA) ML0979 ML2081(pgsA2)
            MPA: MAP1535(pgsA2) MAP2714c(pgsA) MAP2857c(pgsA3)
            MAV: MAV_3637(pgsA)
            MSM: MSMEG_2692(pgsA) MSMEG_3652
            MMC: Mmcs_2123
            CGL: NCgl1605(cgl1669) NCgl1889(cgl1964)
            CGB: cg1878(pgsA1) cg2154(pgsA2)
            CEF: CE1783 CE1857
            CDI: DIP1386 DIP1458
            CJK: jk1064(pgsA1) jk1124(pgsA2)
            NFA: nfa24840(pgsA1) nfa37100 nfa38580(pgsA2)
            RHA: RHA1_ro00911(pgsA) RHA1_ro06754 RHA1_ro06880
            SCO: SCO1389(SC1A8A.09c) SCO1527(SCL2.17c) SCO5753(pgsA)
            SMA: SAV2507(pgsA1) SAV6826(pgsA2) SAV6976(pgsA3)
            TWH: TWT612(pgsA)
            TWS: TW629(pgsA)
            LXX: Lxx15520(pgsA) Lxx16070(pgsA)
            AAU: AAur_1589(pgsA)
            PAC: PPA1007 PPA1078 PPA1079
            TFU: Tfu_0796 Tfu_1393 Tfu_2103
            FRA: Francci3_1362 Francci3_1462 Francci3_3539
            FAL: FRAAL2165 FRAAL2264(pgsA) FRAAL5733(pgsA)
            SEN: SACE_2007 SACE_3847(pgsA) SACE_5881
            BLO: BL0750(pgsA) BL1412(pgsA3)
            BAD: BAD_0796(pgsA) BAD_0801 BAD_1028(pgsA3)
            RXY: Rxyl_1218 Rxyl_2978
            FNU: FN1307 FN1709
            RBA: RB10878(pgsA) RB11253(pgsA)
            CTR: CT496(pgsA_1) CT797(pgsA_2)
            CTA: CTA_0543(pgsA_1) CTA_0868(pgsA_2)
            CMU: TC0180 TC0783
            CPN: CPn0615(pgsA_1) CPn0947(pgsA_2)
            CPA: CP0132 CP0912
            CPJ: CPj0615(pgsA_1) CPj0947(pgsA_2)
            CPT: CpB0639 CpB0984
            CCA: CCA00125 CCA00822(pgsA)
            CAB: CAB124 CAB791
            CFE: CF0192(pgsA2) CF0881(pgsA1)
            PCU: pc0242(pgsA) pc1597(pgsA)
            BGA: BG0743
            BAF: BAPKO_0765
            TPA: TP0256 TP0730
            TDE: TDE2572(pgsA)
            LIL: LA1139(pgsA1) LA2001(pgsA2)
            LIC: LIC11906 LIC12542(pgsA)
            LBJ: LBJ_1800(pgsA-2) LBJ_2158(pgsA-1)
            LBL: LBL_1307(pgsA-2) LBL_2152(pgsA-1)
            SYN: sll1522(pgsA)
            SYW: SYNW0771(pgsA)
            SYC: syc2269_c(pgsA)
            SYF: Synpcc7942_1825
            SYD: Syncc9605_1878
            SYE: Syncc9902_0775
            SYG: sync_1725(pgsA)
            SYR: SynRCC307_1012(pgsA)
            SYX: SynWH7803_1165(pgsA)
            CYA: CYA_1904(pgsA)
            CYB: CYB_0492(pgsA)
            TEL: tll1275(PgsA)
            GVI: glr0301(PgsA)
            ANA: all4063(PgsA)
            AVA: Ava_1643
            PMA: Pro0874(pgsA)
            PMM: PMM0798(pgsA)
            PMT: PMT0518(pgsA)
            PMN: PMN2A_0206
            PMI: PMT9312_0806
            PMB: A9601_08621(pgsA)
            PMC: P9515_07831(pgsA)
            PMF: P9303_17481(pgsA)
            PMG: P9301_08591(pgsA)
            PMH: P9215_08931
            PME: NATL1_08381(pgsA)
            TER: Tery_0298
            BTH: BT_1523
            SRU: SRU_1301(pgsA) SRU_2173
            CTE: CT0335(pgsA) CT1663
            CCH: Cag_0163 Cag_1419
            PLT: Plut_1641
            DET: DET0977
            DEH: cbdb_A940
            AAE: aq_1480 aq_2154(pgsA1) aq_958(pgsA2)
            TMA: TM1861
            MAC: MA0264 MA0525
            MBA: Mbar_A1250 Mbar_A1498
            MMA: MM_1536 MM_1685
            MBU: Mbur_0463 Mbur_2209
            MHU: Mhun_2523
            MTH: MTH1691
            MST: Msp_0095
            MSI: Msm_0613
            HAL: VNG1030G(pgsA)
            HMA: rrnAC0532(pgsA)
            HWA: HQ1730A(pgsA) HQ3362A(pgsA)
            NPH: NP1334A NP2144A(pgsA)
            TAC: Ta0569
            TVO: TVN0621
            PTO: PTO1167
            PHO: PH0460
            PAB: PAB1041(pgsA)
            PFU: PF0462
            TKO: TK0059
            APE: APE_1526.1
            SSO: SSO0556(pgsA)
            STO: ST1430
            SAI: Saci_1541
            PAI: PAE2176(pgsA)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.5
            ExPASy - ENZYME nomenclature database: 2.7.8.5
            ExplorEnz - The Enzyme Database: 2.7.8.5
            ERGO genome analysis and discovery system: 2.7.8.5
            BRENDA, the Enzyme Database: 2.7.8.5
            CAS: 9068-49-9
///
ENTRY       EC 2.7.8.6                  Enzyme
NAME        undecaprenyl-phosphate galactose phosphotransferase;
            poly(isoprenol)-phosphate galactose phosphotransferase;
            poly(isoprenyl)phosphate galactosephosphatetransferase;
            undecaprenyl phosphate galactosyl-1-phosphate transferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     UDP-galactose:undecaprenyl-phosphate galactose phosphotransferase
REACTION    UDP-galactose + undecaprenyl phosphate = UMP +
            alpha-D-galactosyl-diphosphoundecaprenol [RN:R01535]
ALL_REAC    R01535
SUBSTRATE   UDP-galactose [CPD:C00052];
            undecaprenyl phosphate [CPD:C00348]
PRODUCT     UMP [CPD:C00105];
            alpha-D-galactosyl-diphosphoundecaprenol [CPD:C04507]
REFERENCE   1  [PMID:4878433]
  AUTHORS   Osborn MJ, Tze-Yuen RY.
  TITLE     Biosynthesis of bacterial lipopolysaccharide. VII. Enzymatic
            formation of the first intermediate in biosynthesis of the O-antigen
            of Salmonella typhimurium.
  JOURNAL   J. Biol. Chem. 243 (1968) 5145-52.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:4291948]
  AUTHORS   Wright A, Dankert M, Fennessey P, Robbins PW.
  TITLE     Characterization of a polyisoprenoid compound functional in
            O-antigen biosynthesis.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 57 (1967) 1798-803.
  ORGANISM  Salmonella newington
ORTHOLOGY   KO: K00996  undecaprenyl-phosphate galactose phosphotransferase
GENES       STY: STY2291(rfbP)
            STT: t0791(rfbP)
            SPT: SPA0789(rfbP)
            STM: STM2082(rfbP)
            ECA: ECA1420(rfbP)
            ENT: Ent638_2661
            ASU: Asuc_0102 Asuc_0822
            PPF: Pput_2572
            PCR: Pcryo_0636
            SDN: Sden_2648
            SPL: Spea_1424
            SDE: Sde_0131 Sde_3797
            PIN: Ping_0461
            TCX: Tcr_1675
            NOC: Noc_1508 Noc_1999
            AEH: Mlg_0159
            CSA: Csal_1693
            MMW: Mmwyl1_0842
            REU: Reut_B5365
            BUR: Bcep18194_B1801 Bcep18194_B2276 Bcep18194_B2863
                 Bcep18194_C7401
            BCN: Bcen_4149
            BCH: Bcen2424_4217
            BAM: Bamb_6172 Bamb_6491
            BPS: BPSL2781
            BPM: BURPS1710b_3275(rfbP)
            BTE: BTH_I1351(rfbP)
            RFR: Rfer_0702
            AJS: Ajs_3034
            NMU: Nmul_A2673
            TDN: Tmden_1700
            CCV: CCV52592_0291
            NIS: NIS_1249
            SUN: SUN_0104
            GUR: Gura_1698 Gura_3177
            PCA: Pcar_1519
            PPD: Ppro_2877
            DVL: Dvul_2699
            DDE: Dde_0481 Dde_0829
            LIP: LI0512
            ADE: Adeh_2455 Adeh_2766
            AFW: Anae109_1412 Anae109_2622
            SAT: SYN_01131 SYN_02686
            SFU: Sfum_0975
            PLA: Plav_1932
            SMD: Smed_0851 Smed_4800 Smed_4946
            RET: RHE_CH03385(exoY)
            RLE: RL1661(cpsA) RL3820 pRL90146
            OAN: Oant_2509
            BRA: BRADO2232 BRADO7064
            BBT: BBta_1032 BBta_1068
            RPC: RPC_2682
            RPE: RPE_1093 RPE_3504
            SIT: TM1040_2411
            RSH: Rsph17029_1206 Rsph17029_3680
            RSQ: Rsph17025_1975
            JAN: Jann_4237
            RDE: RD1_1699 RD1_3853 RD1_B0024
            PDE: Pden_0842
            NAR: Saro_2049
            SAL: Sala_0948
            ELI: ELI_05315
            RRU: Rru_A1482 Rru_A3102 Rru_A3721
            ABA: Acid345_2591 Acid345_2726 Acid345_3807 Acid345_3821
            SUS: Acid_7288
            BCE: BC1586 BC5270
            BTK: BT9727_1466
            LRE: Lreu_1375
            CPE: CPE0614(rfbP)
            CTC: CTC02253
            CTH: Cthe_1349 Cthe_2344
            CBE: Cbei_4739 Cbei_4757
            CKL: CKL_3161
            DSY: DSY3342
            DRM: Dred_3137
            CSC: Csac_2566
            MTA: Moth_0669
            MSM: MSMEG_5984
            MVA: Mvan_1703
            MGI: Mflv_4755
            MMC: Mmcs_1295 Mmcs_1301 Mmcs_3584
            MKM: Mkms_1312 Mkms_1318 Mkms_3657
            MJL: Mjls_1331 Mjls_1337 Mjls_3589
            RHA: RHA1_ro05434 RHA1_ro05438
            ART: Arth_3206 Arth_4061
            FRA: Francci3_1338 Francci3_1577 Francci3_3854
            FAL: FRAAL2105 FRAAL6106(rfbP)
            ACE: Acel_1939
            KRA: Krad_0013 Krad_1048 Krad_3681
            SEN: SACE_3176 SACE_3917
            STP: Strop_3593 Strop_4492
            RXY: Rxyl_0571 Rxyl_1931 Rxyl_2690
            SYN: sll1535(rfbP)
            SYW: SYNW1652
            SYD: Syncc9605_0837
            SYE: Syncc9902_1552
            SYG: sync_0183 sync_0723
            ANA: all4829
            AVA: Ava_0744 Ava_1046 Ava_1374 Ava_1951 Ava_2093 Ava_2099
                 Ava_4832
            PMT: PMT0311
            PMN: PMN2A_0883
            PMF: P9303_20081(wcaJ)
            PME: NATL1_17381(wcaJ)
            TER: Tery_0489 Tery_1523
            FJO: Fjoh_4994
            CPH: Cpha266_1830
            PLT: Plut_1363
            RRS: RoseRS_1134 RoseRS_2370 RoseRS_2948 RoseRS_3578 RoseRS_3644
                 RoseRS_4262
            RCA: Rcas_0494 Rcas_1345 Rcas_1950 Rcas_3108 Rcas_3974 Rcas_4266
            DGE: Dgeo_0343 Dgeo_2671
            TTH: TTC0275
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.6
            ExPASy - ENZYME nomenclature database: 2.7.8.6
            ExplorEnz - The Enzyme Database: 2.7.8.6
            ERGO genome analysis and discovery system: 2.7.8.6
            BRENDA, the Enzyme Database: 2.7.8.6
            CAS: 37278-29-8
///
ENTRY       EC 2.7.8.7                  Enzyme
NAME        holo-[acyl-carrier-protein] synthase;
            acyl carrier protein holoprotein (holo-ACP) synthetase;
            holo-ACP synthetase;
            coenzyme A:fatty acid synthetase apoenzyme 4'-phosphopantetheine
            transferase;
            holosynthase;
            acyl carrier protein synthetase;
            holo-ACP synthase;
            PPTase;
            AcpS;
            ACPS;
            acyl carrier protein synthase;
            P-pant transferase;
            CoA:apo-[acyl-carrier-protein] pantetheinephosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     CoA-[4'-phosphopantetheine]:apo-[acyl-carrier-protein]
            4'-pantetheinephosphotransferase
REACTION    CoA-[4'-phosphopantetheine] + apo-[acyl-carrier-protein] = adenosine
            3',5'-bisphosphate + holo-[acyl-carrier-protein] [RN:R01625]
ALL_REAC    R01625
SUBSTRATE   CoA-[4'-phosphopantetheine];
            apo-[acyl-carrier-protein] [CPD:C03688]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            holo-[acyl-carrier-protein]
COMMENT     Requires Mg2+. All polyketide synthases, fatty-acid synthases and
            non-ribosomal peptide synthases require post-translational
            modification of their constituent acyl-carrier-protein (ACP) domains
            to become catalytically active. The inactive apo-proteins are
            converted into their active holo-forms by transfer of the
            4'-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group
            of a conserved serine residue in each ACP domain [3]. The enzyme
            from human can activate both the ACP domain of the human cytosolic
            multifunctional fatty acid synthase and that associated with human
            mitochondria as well as peptidyl-carrier and acyl-carrier-proteins
            from prokaryotes [6]. Removal of the 4-phosphopantetheinyl moiety
            from holo-ACP is carried out by EC 3.1.4.14, [acyl-carrier-protein]
            phosphodiesterase.
REFERENCE   1  [PMID:4872726]
  AUTHORS   Elovson J, Vagelos PR.
  TITLE     Acyl carrier protein. X. Acyl carrier protein synthetase.
  JOURNAL   J. Biol. Chem. 243 (1968) 3603-11.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4561013]
  AUTHORS   Prescott DJ, Vagelos PR.
  TITLE     Acyl carrier protein.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 36 (1972) 269-311.
REFERENCE   3  [PMID:8939709]
  AUTHORS   Lambalot RH, Gehring AM, Flugel RS, Zuber P, LaCelle M, Marahiel MA,
            Reid R, Khosla C, Walsh CT.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases.
  JOURNAL   Chem. Biol. 3 (1996) 923-36.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:9667867]
  AUTHORS   Walsh CT, Gehring AM, Weinreb PH, Quadri LE, Flugel RS.
  TITLE     Post-translational modification of polyketide and nonribosomal
            peptide synthases.
  JOURNAL   Curr. Opin. Chem. Biol. 1 (1997) 309-15.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:11489886]
  AUTHORS   Mootz HD, Finking R, Marahiel MA.
  TITLE     4'-phosphopantetheine transfer in primary and secondary metabolism
            of Bacillus subtilis.
  JOURNAL   J. Biol. Chem. 276 (2001) 37289-98.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   6  [PMID:12815048]
  AUTHORS   Joshi AK, Zhang L, Rangan VS, Smith S.
  TITLE     Cloning, expression, and characterization of a human
            4'-phosphopantetheinyl transferase with broad substrate specificity.
  JOURNAL   J. Biol. Chem. 278 (2003) 33142-9.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K00997  holo-[acyl-carrier protein] synthase
GENES       DME: Dmel_CG32099(eap)
            ANI: AN7043.2
            AFM: AFUA_4G04040
            AOR: AO090206000106
            CNE: CNI03060
            DDI: DDBDRAFT_0217726
            PFA: PFD0980w
            TET: TTHERM_00485960
            ECO: b2563(acpS)
            ECJ: JW2547(acpS)
            ECE: Z1544 Z3844(acpS)
            ECS: ECs1284 ECs3429
            ECC: c3087(acpS)
            ECI: UTI89_C2884(acpS) UTI89_C3991(acpT)
            ECP: ECP_2565
            ECV: APECO1_3968(acpS)
            ECW: EcE24377A_2849(acpS)
            ECX: EcHS_A2718
            STY: STY2823(acpS)
            STT: t0280(acpS)
            SPT: SPA0288(acpS)
            SEC: SC2572(acpS)
            STM: STM2577(acpS)
            YPE: YPO2929(acpS)
            YPK: y1301(acpS)
            YPM: YP_2526(acpS)
            YPA: YPA_2368
            YPN: YPN_1210
            YPP: YPDSF_1549
            YPS: YPTB2886(acpS)
            YPI: YpsIP31758_1140(acpS)
            SFL: SF2625(acpS)
            SFX: S2798(acpS)
            SFV: SFV_2626(acpS)
            SSN: SSON_2687(acpS)
            SBO: SBO_2591(acpS)
            SDY: SDY_2804(acpS)
            ECA: ECA3274(acpS)
            PLU: plu3336(acpS)
            BUC: BU256(acpS)
            BAS: BUsg247(acpS)
            BAB: bbp237(acpS)
            BCC: BCc_161(acpS)
            WBR: WGLp198(acpS)
            SGL: SG1783
            ENT: Ent638_3050
            SPE: Spro_3665
            BFL: Bfl538(acpS)
            BPN: BPEN_558(acpS)
            VCH: VC2457
            VCO: VC0395_A2035(acpS)
            VVU: VV1_1569
            VVY: VV2827
            VPA: VP2568
            VFI: VF2083
            PPR: PBPRA3085
            SON: SO_1352(acpS)
            SDN: Sden_2762
            SFR: Sfri_2925
            SAZ: Sama_0884
            SBL: Sbal_1205
            SBM: Shew185_1249
            SLO: Shew_1058
            SPC: Sputcn32_1163
            SSE: Ssed_1152
            SPL: Spea_1041
            SHE: Shewmr4_2844
            SHM: Shewmr7_2926
            SHN: Shewana3_3022
            SHW: Sputw3181_3001
            ILO: IL0806(acpS)
            PAT: Patl_3708
            TCX: Tcr_0738
            NOC: Noc_0796
            AEH: Mlg_1351
            HHA: Hhal_0030
            MMW: Mmwyl1_1249
            BCI: BCI_0278(acpS)
            RMA: Rmag_0610
            VOK: COSY_0563(acpS)
            NME: NMB0452
            NMA: NMA2033(acpS)
            NMC: NMC1700(acpS)
            NGO: NGO1507
            CVI: CV_2072(acpS)
            RSO: RSc1067(acpS)
            REU: Reut_A2248
            REH: H16_A2551(acpS)
            RME: Rmet_2414
            BMA: BMA0547(acpS)
            BMV: BMASAVP1_A2462(acpS)
            BML: BMA10299_A2819(acpS)
            BMN: BMA10247_1785(acpS)
            BXE: Bxe_A1089
            BVI: Bcep1808_1057
            BUR: Bcep18194_A4250
            BCN: Bcen_0658
            BCH: Bcen2424_1138
            BAM: Bamb_1014
            BPS: BPSL2425
            BPM: BURPS1710b_2891(acpS)
            BPL: BURPS1106A_2836(acpS)
            BPD: BURPS668_2775(acpS)
            BTE: BTH_I1734
            BPE: BP2079(acpS)
            BPA: BPP1763(acpS)
            BBR: BB3345(acpS)
            RFR: Rfer_1753
            POL: Bpro_3631
            PNA: Pnap_3057
            AAV: Aave_1200
            MPT: Mpe_A0654
            HAR: HEAR2059(acpS)
            MMS: mma_1374
            NEU: NE2321(acpS)
            NET: Neut_1775
            NMU: Nmul_A1760
            EBA: ebB196(acpS)
            AZO: azo1646(acpS)
            DAR: Daro_2033
            TBD: Tbd_0728
            MFA: Mfla_0868 Mfla_1012
            HPY: HP0808(acpS)
            HPJ: jhp0744(acpS)
            HPA: HPAG1_0793
            HHE: HH1555(acpS)
            HAC: Hac_0830
            WSU: WS1971(acpS)
            TDN: Tmden_0839
            CJE: Cj1409(acpS)
            CJR: CJE1596(acpS)
            CJJ: CJJ81176_1408(acpS)
            CJU: C8J_1323(acpS)
            CJD: JJD26997_1742(acpS)
            CFF: CFF8240_0921(acpS)
            CCV: CCV52592_1391(acpS)
            CHA: CHAB381_1428(acpS)
            CCO: CCC13826_1319(acpS) CCC13826_2069
            ABU: Abu_0217(acpS)
            NIS: NIS_1060(acpS)
            SUN: SUN_0595
            GSU: GSU1803(acpS)
            GME: Gmet_1884
            PCA: Pcar_1003
            PPD: Ppro_2258
            DVU: DVU1909(acpS)
            DDE: Dde_2044
            LIP: LI0731(acpS)
            ADE: Adeh_1501
            MXA: MXAN_4350(acpS)
            SAT: SYN_02779
            SFU: Sfum_2167
            RPR: RP577(acpS)
            RTY: RT0566(acpS)
            RCO: RC0881(acpS)
            RFE: RF_0943(acpS)
            RBE: RBE_0992(acpS)
            RAK: A1C_04495(acpS)
            RBO: A1I_03695(acpS)
            RRI: A1G_04865(acpS)
            OTS: OTBS_0918(acpS)
            WOL: WD0814(acpS)
            WBM: Wbm0078
            AMA: AM506(acpS)
            APH: APH_0646(acpS)
            ERU: Erum3430(acpS)
            ERW: ERWE_CDS_03500(acpS)
            ERG: ERGA_CDS_03460(acpS)
            ECN: Ecaj_0326
            ECH: ECH_0741(acpS)
            NSE: NSE_0962(acpS)
            PUB: SAR11_1055(acpS)
            MLO: mlr7761(acpS)
            MES: Meso_0948
            PLA: Plav_2872
            SME: SMc02654(acpS)
            SMD: Smed_0680
            ATU: Atu1033(acpS)
            ATC: AGR_C_1902
            RET: RHE_CH01388(acpS)
            RLE: RL1509(acpS)
            BME: BMEI1289
            BMF: BAB1_0679(acpS)
            BMS: BR0659(acpS)
            BMB: BruAb1_0676(acpS)
            BOV: BOV_0652(acpS)
            OAN: Oant_2629
            BJA: bll5063(acpS)
            BRA: BRADO4466(acpS)
            BBT: BBta_4685(acpS)
            RPA: RPA2695(acpS)
            RPB: RPB_2610
            RPC: RPC_2638
            RPD: RPD_2649
            RPE: RPE_3024
            NWI: Nwi_1920
            NHA: Nham_2253
            BHE: BH05070(acpS)
            BQU: BQ04260(acpS)
            BBK: BARBAKC583_0471(acpS)
            XAU: Xaut_3879
            CCR: CC_1558
            SIL: SPO3200(acpS)
            SIT: TM1040_2561
            RSP: RSP_1673
            RSQ: Rsph17025_2573
            JAN: Jann_0520
            RDE: RD1_1364(acpS)
            MMR: Mmar10_1572
            HNE: HNE_0876
            ZMO: ZMO1709(acpS)
            NAR: Saro_0910
            SAL: Sala_1409
            SWI: Swit_3872
            ELI: ELI_02710
            GOX: GOX1808
            GBE: GbCGDNIH1_0990
            ACR: Acry_0532
            MAG: amb2256
            MGM: Mmc1_1859
            ABA: Acid345_4518
            SUS: Acid_6712
            BSU: BG12089(acpS)
            BHA: BH0518
            BAN: BA0250(acpS)
            BAR: GBAA0250(acpS)
            BAA: BA_0820
            BAT: BAS0236
            BCE: BC0262
            BCA: BCE_0270(acpS)
            BCZ: BCZK0224(acpS)
            BCY: Bcer98_0236
            BTK: BT9727_0222(acpS)
            BTL: BALH_0235(acpS)
            BCL: ABC0805(acpS)
            BPU: BPUM_0435
            OIH: OB0619
            GKA: GK0228
            GTN: GTNG_0203
            SAU: SA1875(dpj)
            SAV: SAV2071(dpj)
            SAM: MW1995(dpj)
            SAR: SAR2159(acpS)
            SAS: SAS1976
            SAC: SACOL2061(acpS)
            SAB: SAB1956c(acpS)
            SAA: SAUSA300_2028(acpS)
            SAO: SAOUHSC_02306
            SAJ: SaurJH9_2108
            SAH: SaurJH1_2146
            SEP: SE1675
            SER: SERP1684(acpS)
            SHA: SH0960(dpj)
            SSP: SSP0806
            LMO: lmo0885
            LMF: LMOf2365_0904(acpS)
            LIN: lin0884
            LWE: lwe0867(acpS)
            LLA: L61355(acpS)
            LLC: LACR_0909
            LLM: llmg_1705(acpS)
            SPY: SPy_1804(acpS)
            SPZ: M5005_Spy_1533(acpS)
            SPM: spyM18_1872(acpS)
            SPG: SpyM3_1564(acpS)
            SPS: SPs0303
            SPH: MGAS10270_Spy1601(alr)
            SPI: MGAS10750_Spy1592(alr)
            SPJ: MGAS2096_Spy1560(alr)
            SPK: MGAS9429_Spy1537(alr)
            SPF: SpyM50313(acpS)
            SPA: M6_Spy1525(acpS)
            SPB: M28_Spy1523(acpS)
            SPN: SP_1699
            SPR: spr1541(acpS)
            SPD: SPD_1509(acpS)
            SAG: SAG1685(acpS)
            SAN: gbs1729
            SAK: SAK_1697(acpS)
            SMU: SMU.1835(acpS)
            STC: str1727(acpS)
            STL: stu1727(acpS)
            STE: STER_1702
            SSA: SSA_0547(acpS)
            SSU: SSU05_1813
            SSV: SSU98_1817
            SGO: SGO_0417(acpS)
            LPL: lp_0522(acpS)
            LJO: LJ0271
            LAC: LBA0268(acpS)
            LSA: LSA1614(acpS)
            LSL: LSL_0357(acpS)
            LDB: Ldb0359(acpS)
            LBU: LBUL_0314
            LBR: LVIS_0507
            LCA: LSEI_2561
            LGA: LGAS_0266
            PPE: PEPE_1560
            EFA: EF0848(acpS)
            OOE: OEOE_1642
            LME: LEUM_1813
            STH: STH2938
            CAC: CAC0489
            CPE: CPE0291(acpS)
            CPF: CPF_0287(acpS)
            CPR: CPR_0282(acpS)
            CTC: CTC02516(acpS)
            CNO: NT01CX_1261(acpS)
            CDF: CD3466(acpS)
            CBO: CBO3400(acpS)
            CBA: CLB_3457(acpS)
            CBH: CLC_3344(acpS)
            CBF: CLI_3585(acpS)
            CKL: CKL_3584(acpS)
            CHY: CHY_0664(acpS)
            DSY: DSY4024
            SWO: Swol_1885
            TTE: TTE2171(acpS)
            MTA: Moth_2169
            MGE: MG_482
            MPN: MPN298(H10_orf119)
            MPU: MYPU_1130(acpS)
            MPE: MYPE350
            MGA: MGA_0041(acpS)
            MMY: MSC_0578(acpS)
            MMO: MMOB4790(acpS)
            MSY: MS53_0098(acpS)
            MCP: MCAP_0400
            UUR: UU393(acpS)
            POY: PAM440(acpS)
            AYW: AYWB_323(acpS)
            MFL: Mfl384
            MTU: Rv2523c(acpS)
            MTC: MT2599
            MBO: Mb2552c(acpS)
            MBB: BCG_2544c(acpS)
            MLE: ML1192(acpS)
            MPA: MAP2331c(acpS)
            MAV: MAV_1651
            MSM: MSMEG_4756(acpS)
            MMC: Mmcs_3647
            CGL: NCgl2405(acpS)
            CGB: cg2738(ppt1)
            CEF: CE2389
            CDI: DIP1845(ppt1)
            NFA: nfa12580(acpS)
            RHA: RHA1_ro01425 RHA1_ro05754
            SCO: SCO4744(acpS)
            SMA: SAV4964(acpS)
            LXX: Lxx19960(acpS)
            CMI: CMM_2575(acpS)
            PAC: PPA1793
            FRA: Francci3_0620
            FAL: FRAAL1120
            SEN: SACE_6767(acpS)
            STP: Strop_3859
            BAD: BAD_0257
            RXY: Rxyl_0801
            FNU: FN1342
            RBA: RB6435(acpS)
            CTR: CT100(acpS)
            CTA: CTA_0106(acpS)
            CMU: TC0376
            CPN: CPn0313(acpS)
            CPA: CP0445
            CPJ: CPj0313(acpS)
            CPT: CpB0323
            CCA: CCA00469(acpS)
            CAB: CAB455(acpS)
            CFE: CF0538(acpS)
            PCU: pc1711(acpS)
            BBU: BB0010
            BGA: BG0010
            BAF: BAPKO_0009
            TPA: TP0828
            TDE: TDE1907(acpS)
            LIL: LA3302(acpS)
            LIC: LIC10846(acpS)
            LBJ: LBJ_0900(acpS)
            LBL: LBL_0915(acpS)
            GVI: glr4008
            CHU: CHU_2126(acpS)
            CTE: CT1935(acpS)
            CCH: Cag_0235
            PLT: Plut_0271
            DET: DET0445(acpS)
            DEH: cbdb_A401(acpS)
            DEB: DehaBAV1_0422
            DRA: DR_0247
            DGE: Dgeo_1927
            TTH: TTC1022
            TTJ: TTHA1388
            AAE: aq_813(acpS)
            TMA: TM0692
            MHU: Mhun_3109 Mhun_3160
STRUCTURES  PDB: 1F7L  1F7T  1F80  1FTE  1FTF  1FTH  2JBZ  2JCA  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.7
            ExPASy - ENZYME nomenclature database: 2.7.8.7
            ExplorEnz - The Enzyme Database: 2.7.8.7
            ERGO genome analysis and discovery system: 2.7.8.7
            BRENDA, the Enzyme Database: 2.7.8.7
            CAS: 37278-30-1
///
ENTRY       EC 2.7.8.8                  Enzyme
NAME        CDP-diacylglycerol---serine O-phosphatidyltransferase;
            phosphatidylserine synthase;
            CDPdiglyceride-serine O-phosphatidyltransferase;
            PS synthase;
            cytidine 5'-diphospho-1,2-diacyl-sn-glycerol
            (CDPdiglyceride):L-serine O-phosphatidyltransferase;
            phosphatidylserine synthetase;
            CDP-diacylglycerol-L-serine O-phosphatidyltransferase;
            cytidine diphosphoglyceride-serine O-phosphatidyltransferase;
            CDP-diglyceride-L-serine phosphatidyltransferase;
            CDP-diglyceride:serine phosphatidyltransferase;
            cytidine 5'-diphospho-1,2-diacyl-sn-glycerol:L-serine
            O-phosphatidyltransferase;
            CDP-diacylglycerol:L-serine 3-O-phosphatidyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     CDP-diacylglycerol:L-serine 3-sn-phosphatidyltransferase
REACTION    CDP-diacylglycerol + L-serine = CMP + (3-sn-phosphatidyl)-L-serine
            [RN:R01800]
ALL_REAC    R01800
SUBSTRATE   CDP-diacylglycerol [CPD:C00269];
            L-serine [CPD:C00065]
PRODUCT     CMP [CPD:C00055];
            (3-sn-phosphatidyl)-L-serine
REFERENCE   1  [PMID:187212]
  AUTHORS   Larson TJ, Dowhan W.
  TITLE     Ribosomal-associated phosphatidylserine synthetase from Escherichia
            coli: purification by substrate-specific elution from
            phosphocellulose using cytidine 5'-diphospho-1,2-diacyl-sn-glycerol.
  JOURNAL   Biochemistry. 15 (1976) 5212-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4604873]
  AUTHORS   Raetz CR, Kennedy EP.
  TITLE     Partial purification and properties of phosphatidylserine synthetase
            from Escherichia coli.
  JOURNAL   J. Biol. Chem. 249 (1974) 5083-45.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K00998  phosphatidylserine synthase
GENES       SCE: YCL004W(PGS1) YER026C(CHO1)
            AGO: AGOS_AAL003W AGOS_AER357C
            PIC: PICST_51913(CHO1) PICST_63914(PGS1)
            CGR: CAGL0C03069g
            SPO: SPBP18G5.02 SPCC1442.12
            ANI: AN2261.2 AN5661.2
            AFM: AFUA_4G13680 AFUA_5G06530
            AOR: AO090009000203 AO090701000187
            CNE: CNC04600 CNC07110
            UMA: UM01120.1 UM04590.1
            ECO: b2585(pssA)
            ECJ: JW2569(pssA)
            ECE: Z3870(pssA)
            ECS: ECs3452
            ECC: c3110(pssA)
            ECI: UTI89_C2908(pss)
            ECP: ECP_2587
            ECV: APECO1_3947(pssA)
            ECW: EcE24377A_2872(pssA)
            ECX: EcHS_A2742
            STY: STY2845(pssA)
            STT: t0258(pssA)
            SPT: SPA0265(pssA)
            SEC: SC2657(pssA)
            STM: STM2652(pssA)
            YPE: YPO3273(pssA)
            YPK: y0916(pssA)
            YPM: YP_0658(pssA)
            YPA: YPA_2764
            YPN: YPN_0823
            YPS: YPTB0850(pssA)
            YPI: YpsIP31758_3207(pssA)
            SFX: S2820(pssA)
            SFV: SFV_2648(pssA)
            SSN: SSON_2711(pssA)
            SBO: SBO_2617(pssA)
            SDY: SDY_2828(pssA)
            ECA: ECA3520(pssA)
            PLU: plu1271(pssA)
            WBR: WGLp134(pssA)
            SGL: SG1911
            BFL: Bfl551(pssA)
            BPN: BPEN_571(pssA)
            HIT: NTHI0549(pssA)
            HIP: CGSHiEE_00885(pssA)
            HIQ: CGSHiGG_05335(pssA)
            HDU: HD0271(pssA)
            HSO: HS_0300(pssA)
            PMU: PM1856(pssA)
            MSU: MS0250(cls)
            APL: APL_0043(pssA)
            XFA: XF0442
            XFT: PD1637(pssA)
            XCC: XCC0641(pssA) XCC2161(pssA)
            XCB: XC_1957 XC_3594
            XCV: XCV2207(pssA) XCV3690(pssA)
            XAC: XAC2046(pssA) XAC3565(pssA)
            XOO: XOO0811(pssA) XOO2219(pssA)
            XOM: XOO_0739(XOO0739) XOO_2084(XOO2084)
            VCH: VC0315
            VCO: VC0395_A2714(pssA)
            VVU: VV1_1195
            VVY: VV3172
            VPA: VP2934
            VFI: VF2428(pssA)
            PPR: PBPRA3448
            PAE: PA4693(pssA)
            PAU: PA14_62120(pssA)
            PPU: PP_3664(pssA-1) PP_4677(pssA-2)
            PPF: Pput_4541
            PST: PSPTO_0984(pssA-1) PSPTO_3463(pssA-2)
            PSB: Psyr_0849 Psyr_3244
            PSP: PSPPH_0875(pssA1)
            PFL: PFL_3260(pssA) PFL_5252
            PFO: Pfl_2876 Pfl_4785
            PEN: PSEEN4708
            PMY: Pmen_1010
            PAR: Psyc_0564(pssA)
            PCR: Pcryo_0552
            PRW: PsycPRwf_0645
            ACI: ACIAD3149(pssA)
            SON: SO_2390(pssA) SO_3575
            SDN: Sden_1779 Sden_2859
            SFR: Sfri_0671 Sfri_1921
            SAZ: Sama_1747 Sama_2600
            SBL: Sbal_1021
            SBM: Shew185_1090
            SLO: Shew_2945
            SPC: Sputcn32_1026
            SSE: Ssed_3495
            SHE: Shewmr4_2989
            SHM: Shewmr7_3070
            SHN: Shewana3_1988 Shewana3_3167
            SHW: Sputw3181_3139
            ILO: IL1180
            CPS: CPS_0926(pssA)
            PHA: PSHAa1719(pssA)
            PAT: Patl_1340
            SDE: Sde_2538
            MAQ: Maqu_0885
            CBU: CBU_0097(pssA)
            CBD: COXBU7E912_2011(pssA)
            LPN: lpg0474
            LPF: lpl0515(pssA)
            LPP: lpp0539(pssA)
            MCA: MCA2273(pssA)
            FTU: FTT0835
            FTF: FTF0835
            FTW: FTW_1351
            FTL: FTL_0329
            FTH: FTH_0327
            FTN: FTN_0350(pssA)
            TCX: Tcr_0610
            NOC: Noc_2517
            AEH: Mlg_0549
            HHA: Hhal_0691
            HCH: HCH_05913(pssA)
            CSA: Csal_0505
            ABO: ABO_0486(pssA)
            MMW: Mmwyl1_1329
            AHA: AHA_0285(pssA)
            DNO: DNO_0565(pssA)
            BCI: BCI_0025(pssA)
            RMA: Rmag_0448
            VOK: COSY_0414(pssA)
            NME: NMB1318
            NMA: NMA1532(pss)
            NMC: NMC1255(pss)
            NGO: NGO0586
            CVI: CV_1111(pssA)
            RSO: RSc2073(pssA)
            REU: Reut_A0951 Reut_B4325
            REH: H16_A1039(pssA)
            RME: Rmet_0916 Rmet_4861
            BMA: BMA1844(pssA)
            BMV: BMASAVP1_A1117(pssA)
            BML: BMA10299_A0749(pssA)
            BMN: BMA10247_0400(pssA)
            BXE: Bxe_A3227
            BUR: Bcep18194_A5588
            BCH: Bcen2424_2261
            BAM: Bamb_2299
            BPS: BPSL1200
            BPM: BURPS1710b_1423(pssA)
            BPL: BURPS1106A_1285(pssA)
            BPD: BURPS668_1278(pssA)
            BTE: BTH_I1049
            PNU: Pnuc_1059
            BPE: BP0792(pssA)
            BPA: BPP3434(pssA)
            BBR: BB3884(pssA)
            RFR: Rfer_2496 Rfer_3325
            POL: Bpro_2320
            PNA: Pnap_1720
            AAV: Aave_3109
            AJS: Ajs_1772
            VEI: Veis_1753
            MPT: Mpe_A2045 Mpe_A2102
            HAR: HEAR1241 HEAR2940
            MMS: mma_2146 mma_3189
            NEU: NE1321(pssA)
            NET: Neut_1258
            NMU: Nmul_A0470
            EBA: ebA7137(pssA)
            AZO: azo3157(pssA)
            DAR: Daro_3072
            TBD: Tbd_1482 Tbd_1987
            MFA: Mfla_0515
            HPY: HP1071(pssA)
            HPA: HPAG1_0376
            HHE: HH0820(pssA)
            HAC: Hac_1181(pssA)
            WSU: WS0623(pssA)
            TDN: Tmden_1764
            CJE: Cj1114c(pssA)
            CJR: CJE1257(pssA)
            CJJ: CJJ81176_1132(pssA)
            CJU: C8J_1055(pssA)
            CJD: JJD26997_0608(pssA)
            CFF: CFF8240_1345(pssA)
            CHA: CHAB381_0490(pssA)
            CCO: CCC13826_0991
            ABU: Abu_1153(pssA)
            NIS: NIS_1408
            SUN: SUN_1954 SUN_2216
            GSU: GSU1907(pssA)
            GME: Gmet_1264
            GUR: Gura_3716
            PCA: Pcar_2802
            PPD: Ppro_2553
            DVU: DVU2980(pssA)
            DDE: Dde_3217
            LIP: LI0777
            BBA: Bd0483(pssA)
            DPS: DP2772
            ADE: Adeh_3612
            MXA: MXAN_1437(pssA) MXAN_2907(pssA)
            SAT: SYN_00912
            SFU: Sfum_2986 Sfum_3028
            RPR: RP242
            RTY: RT0234(pssA)
            RCO: RC0326(pssA)
            RFE: RF_1045(pssA)
            RBE: RBE_0968(pssA)
            OTS: OTBS_0146(pssA)
            WOL: WD1048
            WBM: Wbm0425
            AMA: AM462(pssA)
            APH: APH_0543(pssA)
            ERW: ERWE_CDS_03210(pssA)
            ERG: ERGA_CDS_03160(pssA)
            ECN: Ecaj_0295
            ECH: ECH_0780
            NSE: NSE_0247
            PUB: SAR11_0646(pssA)
            MLO: mlr7822
            MES: Meso_0979
            PLA: Plav_1115
            SME: SMc00552(pssA)
            SMD: Smed_0724
            ATU: Atu1062(pssA)
            ATC: AGR_C_1962
            RET: RHE_CH01410(pssA1)
            RLE: RL1532
            BME: BMEI1490
            BMF: BAB1_0470(pssA)
            BMS: BR0444(pssA)
            BMB: BruAb1_0466(pssA)
            OAN: Oant_0557
            BJA: blr3797(pssA)
            BRA: BRADO4691(pssA)
            BBT: BBta_3506(pssA)
            RPA: RPA2007(pssA)
            RPB: RPB_3366
            RPC: RPC_2096
            RPD: RPD_2076
            RPE: RPE_2009
            NWI: Nwi_1235
            NHA: Nham_1494
            BHE: BH05220(pssA)
            BQU: BQ04410(pssA)
            BBK: BARBAKC583_0484(pssA)
            XAU: Xaut_4661
            SIL: SPOA0293(pssA)
            SIT: TM1040_3085
            RSP: RSP_0720(pssA)
            PDE: Pden_4691
            ZMO: ZMO1159(pssA)
            NAR: Saro_1367
            SAL: Sala_1962
            SWI: Swit_0459
            ELI: ELI_03755
            GOX: GOX0283
            GBE: GbCGDNIH1_0342
            RRU: Rru_A3584
            MAG: amb0603
            MGM: Mmc1_0902
            ABA: Acid345_2359
            BSU: BG11012(pssA)
            BHA: BH1310(pssA)
            BAN: BA0959(pssA) BA1435
            BAR: GBAA0959(pssA) GBAA1435
            BAA: BA_1534 BA_1956
            BAT: BAS0901 BAS1326
            BCE: BC0976 BC1416 BC3509
            BCA: BCE_1046(pssA) BCE_1536
            BCZ: BCZK0862(pssA) BCZK1300(pssA)
            BTK: BT9727_0880(pssA) BT9727_1299(pssA)
            BTL: BALH_0866
            BLI: BL02540(pssA)
            BLD: BLi03337(pssA)
            BAY: RBAM_002700
            GKA: GK2529
            SSA: SSA_1013
            SGO: SGO_0937
            STH: STH1716
            CAC: CAC0676(pssA) CAC0798
            CPE: CPE1329
            CPF: CPF_1536(pssA)
            CPR: CPR_1329(pssA)
            CTC: CTC00346 CTC01356
            CNO: NT01CX_1384(pssA)
            CBO: CBO0198
            CBA: CLB_0239(pssA)
            CBH: CLC_0254(pssA)
            CBF: CLI_0263(pssA)
            CKL: CKL_3593(pssA)
            CHY: CHY_0922(pssA)
            DSY: DSY1871
            POY: PAM613(pssA)
            AYW: AYWB_120(pssA)
            MTU: Rv0436c(pssA)
            MTC: MT0452(pssA)
            MBO: Mb0444c(pssA)
            MBB: BCG_0475c(pssA)
            MLE: ML0310(pssA)
            MPA: MAP3929c(pssA)
            MAV: MAV_4714
            MSM: MSMEG_0860
            MVA: Mvan_0750
            MGI: Mflv_0154
            MMC: Mmcs_0593
            MKM: Mkms_0606
            MJL: Mjls_0584
            NFA: nfa52800(pssA)
            RHA: RHA1_ro02160(pssA)
            SCO: SCO6467(SC9C7.03c)
            SMA: SAV1917(pssA)
            TFU: Tfu_1895
            SEN: SACE_0520(pssA)
            RXY: Rxyl_0289
            FNU: FN0991
            RBA: RB3820(pss)
            CTR: CT826(pssA)
            CTA: CTA_0900(pssA)
            CMU: TC0213
            CPN: CPn0983(pssA)
            CPA: CP0873
            CPJ: CPj0983(pssA)
            CPT: CpB1020
            CCA: CCA00778
            CAB: CAB746
            CFE: CF0235(pssA)
            PCU: pc1270(pssA)
            LIL: LA1451(pssA)
            LIC: LIC12301(pssA)
            LBJ: LBJ_1981(pssA)
            LBL: LBL_1067(pssA)
            BTH: BT_2232
            BFR: BF0710
            BFS: BF0639
            SRU: SRU_0962
            GFO: GFO_0587(pssA)
            FPS: FP1239(pssA)
            CTE: CT1340(pssA)
            CCH: Cag_0939
            PLT: Plut_1327
            MMP: MMP1171(pssA)
            MAE: Maeo_1058
            MAC: MA0116(pss)
            MBA: Mbar_A0874
            MMA: MM_1403
            MBU: Mbur_2198
            MSI: Msm_0982
            MKA: MK0161(pssA)
            HAL: VNG0784G(pssA)
            HMA: rrnAC0788(pssA)
            HWA: HQ2356A(pssA) HQ2523A(pssA)
            NPH: NP3230A(pssA)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.8
            ExPASy - ENZYME nomenclature database: 2.7.8.8
            ExplorEnz - The Enzyme Database: 2.7.8.8
            ERGO genome analysis and discovery system: 2.7.8.8
            BRENDA, the Enzyme Database: 2.7.8.8
            CAS: 9068-48-8
///
ENTRY       EC 2.7.8.9                  Enzyme
NAME        phosphomannan mannosephosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     GDP-mannose:phosphomannan mannose phosphotransferase
REACTION    GDP-mannose + (phosphomannan)n = GMP + (phosphomannan)n+1
            [RN:R03924]
ALL_REAC    R03924
SUBSTRATE   GDP-mannose [CPD:C00096];
            (phosphomannan)n [CPD:C02347]
PRODUCT     GMP [CPD:C00144];
            (phosphomannan)n+1 [CPD:C02347]
REFERENCE   1  [PMID:4311996]
  AUTHORS   Bretthauer RK, Kozak LP, Irwin WE.
  TITLE     Phosphate and mannose transfer from guanosine diphosphate mannose to
            yeast mannan acceptors.
  JOURNAL   Biochem. Biophys. Res. Commun. 37 (1969) 820-7.
  ORGANISM  Hansenula holstii
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.9
            ExPASy - ENZYME nomenclature database: 2.7.8.9
            ExplorEnz - The Enzyme Database: 2.7.8.9
            ERGO genome analysis and discovery system: 2.7.8.9
            BRENDA, the Enzyme Database: 2.7.8.9
            CAS: 37278-31-2
///
ENTRY       EC 2.7.8.10                 Enzyme
NAME        sphingosine cholinephosphotransferase;
            CDP-choline-sphingosine cholinephosphotransferase;
            phosphorylcholine-sphingosine transferase;
            cytidine diphosphocholine-sphingosine cholinephosphotransferase;
            sphingosine choline phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     CDP-choline:sphingosine cholinephosphotransferase
REACTION    CDP-choline + sphingosine = CMP + sphingosyl-phosphocholine
            [RN:R01929]
ALL_REAC    R01929
SUBSTRATE   CDP-choline [CPD:C00307];
            sphingosine [CPD:C00319]
PRODUCT     CMP [CPD:C00055];
            sphingosyl-phosphocholine [CPD:C03640]
REFERENCE   1  [PMID:5679375]
  AUTHORS   Fujino Y, Negishi T, Ito S.
  TITLE     Enzymic synthesis of sphingosylphosphorylcholine.
  JOURNAL   Biochem. J. 109 (1968) 310-1.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00600  Sphingolipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.10
            ExPASy - ENZYME nomenclature database: 2.7.8.10
            ExplorEnz - The Enzyme Database: 2.7.8.10
            ERGO genome analysis and discovery system: 2.7.8.10
            BRENDA, the Enzyme Database: 2.7.8.10
            CAS: 9027-12-7
///
ENTRY       EC 2.7.8.11                 Enzyme
NAME        CDP-diacylglycerol---inositol 3-phosphatidyltransferase;
            CDP-diglyceride-inositol phosphatidyltransferase;
            phosphatidylinositol synthase;
            CDP-diacylglycerol-inositol phosphatidyltransferase;
            CDP-diglyceride:inositol transferase;
            cytidine 5'-diphospho-1,2-diacyl-sn-glycerol:myo-inositol
            3-phosphatidyltransferase;
            CDP-DG:inositol transferase;
            cytidine diphosphodiglyceride-inositol phosphatidyltransferase;
            CDP-diacylglycerol:myo-inositol-3-phosphatidyltransferase;
            CDP-diglyceride-inositol transferase;
            cytidine diphosphoglyceride-inositol phosphatidyltransferase;
            cytidine diphosphoglyceride-inositol transferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     CDP-diacylglycerol:myo-inositol 3-phosphatidyltransferase
REACTION    CDP-diacylglycerol + myo-inositol = CMP +
            phosphatidyl-1D-myo-inositol [RN:R01802]
ALL_REAC    R01802
SUBSTRATE   CDP-diacylglycerol [CPD:C00269];
            myo-inositol [CPD:C00137]
PRODUCT     CMP [CPD:C00055];
            phosphatidyl-1D-myo-inositol [CPD:C01194]
REFERENCE   1  [PMID:41587]
  AUTHORS   Bleasdale JE, Wallis P, MacDonald PC, Johnston JM.
  TITLE     Characterization of the forward and reverse reactions catalyzed by
            CDP-diacylglycerol:inositol transferase in rabbit lung tissue.
  JOURNAL   Biochim. Biophys. Acta. 575 (1979) 135-47.
  ORGANISM  rabbit
REFERENCE   2  [PMID:4293959]
  AUTHORS   Prottey C, Hawthorne JN.
  TITLE     The biosynthesis of phosphatidic acid and phosphatidylinositol in
            mammalian pancreas.
  JOURNAL   Biochem. J. 105 (1967) 379-92.
  ORGANISM  guinea pig
REFERENCE   3  [PMID:4295616]
  AUTHORS   Salway JG, Harwood JL, Kai M, White GL, Haworne JN.
  TITLE     Enzymes of phosphoinositide metabolism during rat brain development.
  JOURNAL   J. Neurochem. 15 (1968) 221-6.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:18462]
  AUTHORS   Takenawa T, Egawa K.
  TITLE     CDP-diglyceride:inositol transferase from rat liver. Purification
            and properties.
  JOURNAL   J. Biol. Chem. 252 (1977) 5419-23.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
            PATH: map04070  Phosphatidylinositol signaling system
ORTHOLOGY   KO: K00999  CDP-diacylglycerol--inositol 3-phosphatidyltransferase
GENES       HSA: 10423(CDIPT)
            PTR: 454028(CDIPT)
            MCC: 707141(CDIPT)
            MMU: 52858(Cdipt)
            RNO: 192260(Cdipt)
            CFA: 489940(CDIPT)
            BTA: 515135(MGC127038)
            XLA: 414725(MGC81124) 443837(MGC82599)
            DRE: 404620(cdipt)
            SPU: 593468(LOC593468)
            DME: Dmel_CG9245
            CEL: Y46G5A.5(pisy-1)
            ATH: AT1G68000(ATPIS1) AT4G38570(PIS2)
            OSA: 4328140 4341084
            CME: CMM125C
            SCE: YPR113W(PIS1)
            AGO: AGOS_AAR037W
            PIC: PICST_28132(PIS1)
            CGR: CAGL0G03157g
            SPO: SPAC1D4.08
            AFM: AFUA_1G15790
            AOR: AO090003001013 AO090005001121
            ECU: ECU01_1000
            DDI: DDBDRAFT_0218645
            PFA: MAL13P1.82
            CHO: Chro.80072
            TAN: TA15380
            TPV: TP02_0830
            TET: TTHERM_00678350
            TBR: Tb09.160.0530
            TCR: 503925.80
            LMA: LmjF26.2480
            EHI: 194.t00007
            MTU: Rv2612c(pgsA1)
            MBO: Mb2644c(pgsA1)
            MBB: BCG_2637c(pgsA1)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.11
            ExPASy - ENZYME nomenclature database: 2.7.8.11
            ExplorEnz - The Enzyme Database: 2.7.8.11
            ERGO genome analysis and discovery system: 2.7.8.11
            BRENDA, the Enzyme Database: 2.7.8.11
            CAS: 9027-01-4
///
ENTRY       EC 2.7.8.12                 Enzyme
NAME        CDP-glycerol glycerophosphotransferase;
            teichoic-acid synthase;
            cytidine diphosphoglycerol glycerophosphotransferase;
            poly(glycerol phosphate) polymerase;
            teichoic acid glycerol transferase;
            glycerophosphate synthetase;
            CGPTase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase
REACTION    CDP-glycerol + (glycerophosphate)n = CMP + (glycerophosphate)n+1
            [RN:R04042]
ALL_REAC    R04042
SUBSTRATE   CDP-glycerol [CPD:C00513];
            (glycerophosphate)n [CPD:C02768]
PRODUCT     CMP [CPD:C00055];
            (glycerophosphate)n+1 [CPD:C02768]
REFERENCE   1  [PMID:14245357]
  AUTHORS   BURGER MM, GLASER L.
  TITLE     THE SYNTHESIS OF TEICHOIC ACIDS. I. POLYGLYCEROPHOSPHATE.
  JOURNAL   J. Biol. Chem. 239 (1964) 3168-77.
  ORGANISM  Bacillus licheniformis, Bacillus subtilis [GN:bsu]
ORTHOLOGY   KO: K09809  CDP-glycerol glycerophosphotransferase
GENES       BSU: BG10725(tagF)
            BLI: BL02463(tagFB)
            BLD: BLi03817(tagF)
            BCL: ABC3103
            BAY: RBAM_032850(tagF)
            BPU: BPUM_3225 BPUM_3228(tagF) BPUM_3232(tagB)
            SAB: SAB0193
            LWE: lwe1064
            LBR: LVIS_1563
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.12
            ExPASy - ENZYME nomenclature database: 2.7.8.12
            ExplorEnz - The Enzyme Database: 2.7.8.12
            ERGO genome analysis and discovery system: 2.7.8.12
            BRENDA, the Enzyme Database: 2.7.8.12
            CAS: 9076-71-5
///
ENTRY       EC 2.7.8.13                 Enzyme
NAME        phospho-N-acetylmuramoyl-pentapeptide-transferase;
            MraY transferase;
            UDP-MurNAc-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala:C55-isoprenoid
            alcohol transferase;
            UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla:undecaprenylphosphate
            transferase;
            phospho-N-acetylmuramoyl pentapeptide translocase;
            phospho-MurNAc-pentapeptide transferase;
            phospho-NAc-muramoyl-pentapeptide translocase (UMP);
            phosphoacetylmuramoylpentapeptide translocase;
            phosphoacetylmuramoylpentapeptidetransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     UDP-MurAc(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala):undecaprenyl-phos
            phate phospho-N-acetylmuramoyl-pentapeptide-transferase
REACTION    UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl
            phosphate = UMP +
            Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
            diphosphoundecaprenol [RN:R05629]
ALL_REAC    R05629;
            (other) R05628 R05630
SUBSTRATE   UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala);
            undecaprenyl phosphate [CPD:C00348]
PRODUCT     UMP [CPD:C00105];
            Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
            diphosphoundecaprenol
COMMENT     In Gram-negative and some Gram-positive organisms the L-lysine is
            replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate,
            A2pm), which is combined with adjacent residues through its
            L-centre. The undecaprenol involved is ditrans,octacis-undecaprenol
            (for definitions, click here).
REFERENCE   1  [PMID:5805290]
  AUTHORS   Heydanek MG Jr, Neuhaus FC.
  TITLE     The initial stage in peptidoglycan synthesis. IV. Solubilization of
            phospho-N-acetylmuramyl-pentapeptide translocase.
  JOURNAL   Biochemistry. 8 (1969) 1474-81.
  ORGANISM  Staphylococcus aureus
REFERENCE   2  [PMID:5231417]
  AUTHORS   Higashi Y, Strominger JL, Sweeley CC.
  TITLE     Structure of a lipid intermediate in cell wall peptidoglycan
            synthesis: a derivative of a C55 isoprenoid alcohol.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 57 (1967) 1878-84.
  ORGANISM  Micrococcus lysodeikticus
REFERENCE   3  [PMID:5938956]
  AUTHORS   Struve WG, Sinha RK, Neuhaus FC.
  TITLE     On the initial stage in peptidoglycan synthesis.
            Phospho-N-acetylmuramyl-pentapeptide translocase (uridine
            monophosphate).
  JOURNAL   Biochemistry. 5 (1966) 82-93.
  ORGANISM  Staphylococcus aureus
REFERENCE   4  [PMID:11699883]
  AUTHORS   van Heijenoort J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit.
  JOURNAL   Nat. Prod. Rep. 18 (2001) 503-19.
  ORGANISM  Staphylococcus aureus
PATHWAY     PATH: map00550  Peptidoglycan biosynthesis
ORTHOLOGY   KO: K01000  phospho-N-acetylmuramoyl-pentapeptide-transferase
GENES       OSA: 4325561
            ECO: b0087(mraY)
            ECJ: JW0085(mraY)
            ECE: Z0097(mraY)
            ECS: ECs0091
            ECC: c0105(mraY)
            ECI: UTI89_C0096(mraY)
            ECP: ECP_0089
            ECW: EcE24377A_0089(mraY)
            ECX: EcHS_A0093
            STY: STY0145(mraY)
            STT: t0129(mraY)
            SPT: SPA0127(mraY)
            SEC: SC0122(mraY)
            STM: STM0125(mraY)
            YPE: YPO0552(mraY)
            YPK: y3629(mraY)
            YPM: YP_3632(mraY)
            YPA: YPA_3549
            YPN: YPN_0418
            YPP: YPDSF_3090
            YPS: YPTB0685(mraY)
            YPI: YpsIP31758_3390(mraY)
            SFL: SF0084(mraY)
            SFX: S0086(mraY)
            SFV: SFV_0080(mraY)
            SSN: SSON_0095(mraY)
            SBO: SBO_0075(mraY)
            SDY: SDY_0117(mraY)
            ECA: ECA3818(mraY)
            PLU: plu3657(mraY)
            BUC: BU219(mraY)
            BAB: bbp201(mraY)
            WBR: WGLp209(mraY)
            SGL: SG0446
            ENT: Ent638_0633
            SPE: Spro_0758
            BFL: Bfl139(mraY)
            BPN: BPEN_143(mraY)
            HIN: HI1135(mraY)
            HIT: NTHI1302(mraY)
            HIP: CGSHiEE_06380(mraY)
            HIQ: CGSHiGG_09335(mraY)
            HDU: HD0244(mraY)
            HSO: HS_0355(mraY)
            PMU: PM0139(mraY)
            MSU: MS1670(rfe)
            APL: APL_0015(mraY)
            ASU: Asuc_1935
            XFA: XF0795
            XFT: PD1868(mraY)
            XCC: XCC0723(mraY)
            XCB: XC_3512
            XCV: XCV0828(mraY)
            XAC: XAC0777(mraY)
            XOO: XOO3828(mraY)
            XOM: XOO_3606(XOO3606)
            VCH: VC2404
            VCO: VC0395_A1982(mraY)
            VVU: VV1_0581
            VVY: VV0611
            VPA: VP0457
            VFI: VF0856 VF2204
            PPR: PBPRA3218(mraY)
            PAE: PA4415(mraY)
            PAU: PA14_57380(mraY)
            PAP: PSPA7_4987(mraY)
            PPU: PP_1334(mraY)
            PPF: Pput_4390
            PST: PSPTO_4411(mraY)
            PSB: Psyr_4105(mraY)
            PSP: PSPPH_4111(mraY)
            PFL: PFL_5064(mraY)
            PFO: Pfl_4676(mraY)
            PEN: PSEEN4488(mraY)
            PMY: Pmen_0919
            PAR: Psyc_2051(mraY)
            PCR: Pcryo_2375
            PRW: PsycPRwf_0137
            ACI: ACIAD3363(mraY)
            SON: SO_4222(mraY)
            SDN: Sden_0352
            SFR: Sfri_3807
            SAZ: Sama_0351
            SBL: Sbal_0399
            SBM: Shew185_0398
            SLO: Shew_3456
            SPC: Sputcn32_0484
            SSE: Ssed_0407
            SPL: Spea_3814
            SHE: Shewmr4_3573
            SHM: Shewmr7_0383
            SHN: Shewana3_3746
            SHW: Sputw3181_0387
            ILO: IL0433(mraY)
            CPS: CPS_4468(mraY)
            PHA: PSHAa2507(mraY)
            PAT: Patl_3522
            SDE: Sde_0845
            PIN: Ping_1144
            MAQ: Maqu_2455
            CBU: CBU_0125(mraY)
            CBD: COXBU7E912_1980(mraY)
            LPN: lpg2617(mraY)
            LPF: lpl2540(mraY)
            LPP: lpp2670(mraY)
            MCA: MCA2432(mraY)
            FTU: FTT0450(mraY)
            FTF: FTF0450(mraY)
            FTW: FTW_1620(mraY)
            FTL: FTL_1615
            FTH: FTH_1562(mraY)
            FTA: FTA_1703(mraY)
            FTN: FTN_0541(mraY)
            TCX: Tcr_0565
            NOC: Noc_2864(mraY)
            AEH: Mlg_2196
            HHA: Hhal_2094
            HCH: HCH_02404(rfe) HCH_05886(mraY)
            CSA: Csal_2193
            ABO: ABO_0595(murX)
            MMW: Mmwyl1_2617
            AHA: AHA_3887(mraY)
            DNO: DNO_0984(mraY)
            BCI: BCI_0521(mraY)
            RMA: Rmag_0309
            VOK: COSY_0291(mraY)
            NME: NMB0418
            NMA: NMA2066(mraY)
            NMC: NMC1747(mraY)
            NGO: NGO1537
            CVI: CV_4346(mraY)
            RSO: RSc2847(mraY)
            REU: Reut_A2982
            REH: H16_A3276(mraY)
            RME: Rmet_3131
            BMA: BMA2554(mraY)
            BMV: BMASAVP1_A0475(mraY)
            BML: BMA10299_A1334(mraY)
            BMN: BMA10247_3229(mraY)
            BXE: Bxe_A0483
            BVI: Bcep1808_0532
            BUR: Bcep18194_A3642 Bcep18194_A3983
            BCN: Bcen_0074
            BCH: Bcen2424_0556
            BAM: Bamb_0460
            BPS: BPSL3028(mraY)
            BPM: BURPS1710b_3548(mraY)
            BPL: BURPS1106A_3553(mraY)
            BPD: BURPS668_3528(mraY)
            BTE: BTH_I1115(mraY)
            PNU: Pnuc_0164
            BPE: BP3026(murX)
            BPA: BPP3755(murX)
            BBR: BB4201(murX)
            RFR: Rfer_3428
            POL: Bpro_1072
            PNA: Pnap_3420
            AAV: Aave_0818
            AJS: Ajs_3673
            VEI: Veis_4567
            MPT: Mpe_A0459
            HAR: HEAR2814(mraY)
            MMS: mma_3018
            NEU: NE0988(mraY)
            NET: Neut_0249
            NMU: Nmul_A2497
            EBA: ebA1448(mraY)
            AZO: azo0881(mraY)
            DAR: Daro_3501
            TBD: Tbd_0116
            MFA: Mfla_2272
            HPY: HP0493
            HPJ: jhp0445(mraY)
            HPA: HPAG1_0469
            HHE: HH1168(mraY)
            HAC: Hac_0812(mraY)
            WSU: WS2038(mraY)
            TDN: Tmden_1615
            CJE: Cj0433c(mraY)
            CJR: CJE0483(mraY)
            CJJ: CJJ81176_0459(mraY)
            CJU: C8J_0408(mraY)
            CJD: JJD26997_0047(mraY) JJD26997_1511(mraY)
            CFF: CFF8240_1359(mraY)
            CCV: CCV52592_1045(mraY)
            CHA: CHAB381_1594(mraY)
            ABU: Abu_1899(mraY)
            NIS: NIS_0312(mraY)
            SUN: SUN_2192(mraY)
            GSU: GSU3072(mraY)
            GME: Gmet_0409
            GUR: Gura_3977
            PCA: Pcar_2205
            PPD: Ppro_3292
            DVU: DVU2507(mraY)
            DVL: Dvul_0738
            DDE: Dde_1039
            LIP: LI1101(mraY)
            BBA: Bd3201(mraY)
            DPS: DP2900
            ADE: Adeh_3768
            AFW: Anae109_3881
            MXA: MXAN_5607(mraY)
            SAT: SYN_01743
            SFU: Sfum_2755
            RPR: RP595(mraY)
            RTY: RT0583(mraY)
            RCO: RC0910(mraY)
            RFE: RF_0370(mraY)
            RBE: RBE_0854(mraY1)
            RAK: A1C_04655(mraY)
            RBO: A1I_02650(mraY)
            RRI: A1G_05020(mraY)
            OTS: OTBS_0697(mraY)
            WOL: WD1102(mraY)
            WBM: Wbm0643
            AMA: AM1207(mraY1)
            PUB: SAR11_0027(mraY)
            MLO: mll1558
            MES: Meso_2010
            PLA: Plav_2418
            SME: SMc01863(mraY)
            SMD: Smed_2085
            ATU: Atu2097(mraY)
            ATC: AGR_C_3805
            RET: RHE_CH02850(mraY)
            RLE: RL3310(mraY)
            BME: BMEI0576
            BMF: BAB1_1453(mraY)
            BMS: BR1434(mraY)
            BMB: BruAb1_1429(mraY)
            BOV: BOV_1391(mraY)
            OAN: Oant_1741
            BJA: bll6605(mraY)
            BRA: BRADO5662(mraY)
            BBT: BBta_6177(mraY)
            RPA: RPA3533(mraY)
            RPB: RPB_1991
            RPC: RPC_2191
            RPD: RPD_3397
            RPE: RPE_2104
            NWI: Nwi_1048 Nwi_2383
            NHA: Nham_1276
            BHE: BH11270(mraY)
            BQU: BQ08890(mraY)
            BBK: BARBAKC583_0950(mraY)
            XAU: Xaut_1847
            SIL: SPO1184(mraY)
            SIT: TM1040_2020
            RSP: RSP_2101(mraY)
            RSH: Rsph17029_0777
            RSQ: Rsph17025_0688
            JAN: Jann_2764
            RDE: RD1_3363(mraY)
            PDE: Pden_0588
            MMR: Mmar10_2081
            HNE: HNE_3027(mraY)
            ZMO: ZMO0828(mraY)
            NAR: Saro_1130
            SAL: Sala_1884
            SWI: Swit_3950
            ELI: ELI_01780
            GOX: GOX0155
            GBE: GbCGDNIH1_0432
            ACR: Acry_0060
            RRU: Rru_A0953
            MAG: amb3845
            MGM: Mmc1_0756
            ABA: Acid345_3632
            SUS: Acid_7314
            BSU: BG10224(mraY)
            BHA: BH2568(mraY)
            BAN: BA4052(mraY)
            BAR: GBAA4052(mraY)
            BAA: BA_4523
            BAT: BAS3764
            BCE: BC3913
            BCA: BCE_3959(mraY)
            BCZ: BCZK3672(murY)
            BCY: Bcer98_2563
            BTK: BT9727_3655(murY)
            BTL: BALH_3543(mraY)
            BLI: BL02240(mraY)
            BLD: BLi01736(mraY)
            BCL: ABC2358(mraY)
            BAY: RBAM_015050
            BPU: BPUM_1412 BPUM_3202
            OIH: OB1468(mraY)
            GKA: GK1117(mraY)
            SAU: SA1025(mraY)
            SAV: SAV1182(mraY)
            SAM: MW1065(mraY)
            SAR: SAR1158(mraY)
            SAS: SAS1116
            SAC: SACOL1195(mraY)
            SAB: SAB1046(mraY)
            SAA: SAUSA300_1076(mraY)
            SAO: SAOUHSC_01146
            SAJ: SaurJH9_1241
            SAH: SaurJH1_1266
            SEP: SE0857
            SER: SERP0747(mraY)
            SHA: SH1733(mraY)
            SSP: SSP1589
            LMO: lmo2037(mraY)
            LMF: LMOf2365_2069(mraY)
            LIN: lin2143(mraY)
            LWE: lwe2051(mraY)
            LLA: L91444(mraY)
            LLC: LACR_0938
            LLM: llmg_1678(mraY)
            SPY: SPy_1662(mraY)
            SPZ: M5005_Spy_1365
            SPM: spyM18_1673
            SPG: SpyM3_1400(mraY)
            SPS: SPs0462
            SPH: MGAS10270_Spy1483
            SPI: MGAS10750_Spy1475
            SPJ: MGAS2096_Spy1388
            SPK: MGAS9429_Spy1362
            SPF: SpyM50426(mraY)
            SPA: M6_Spy1412
            SPB: M28_Spy1407
            SPN: SP_0337
            SPR: spr0305(mraY)
            SPD: SPD_0307(mraY)
            SAG: SAG0288(mraY)
            SAN: gbs0278(mraY)
            SAK: SAK_0360(mraY)
            SMU: SMU.456(mraY)
            STC: str1700(mraY)
            STL: stu1700(mraY)
            SSA: SSA_1870(mraY)
            SGO: SGO_0576(mraY)
            LPL: lp_2199(mraY)
            LJO: LJ0970
            LAC: LBA0806(mraY)
            LSA: LSA0746(mraY)
            LSL: LSL_1052(mraY)
            LDB: Ldb0739(mraY)
            LBU: LBUL_0672
            LBR: LVIS_1451
            LCA: LSEI_1270
            LRE: Lreu_0588
            EFA: EF0992(mraY)
            OOE: OEOE_1148
            STH: STH1208
            CAC: CAC2127(mraY)
            CPE: CPE1860(mraY)
            CPF: CPF_2114(mraY)
            CPR: CPR_1828(mraY)
            CTC: CTC01630(mraY)
            CNO: NT01CX_1939(mraY)
            CTH: Cthe_0976
            CDF: CD2654(mraY)
            CBO: CBO0884(mraY1) CBO1459(mraY2)
            CBA: CLB_0923(mraY-1) CLB_1484(mraY-2)
            CBH: CLC_0937(mraY-1) CLC_1496(mraY-2)
            CBF: CLI_0965(mraY-1) CLI_1543(mraY-2)
            CKL: CKL_1186(mraY)
            AMT: Amet_2882
            CHY: CHY_2072(mraY)
            DSY: DSY2910
            DRM: Dred_0672
            SWO: Swol_0823
            CSC: Csac_0922
            TTE: TTE1648(rfe2)
            MTA: Moth_0840
            MTU: Rv2156c(murX)
            MTC: MT2215(mraY)
            MBO: Mb2180c(murX)
            MBB: BCG_2173c(murX)
            MLE: ML0911(mraY)
            MPA: MAP1900c(murX)
            MAV: MAV_2333(mraY)
            MSM: MSMEG_4230(mraY)
            MVA: Mvan_3526
            MGI: Mflv_2985
            MMC: Mmcs_3259
            MKM: Mkms_3321
            MJL: Mjls_3270
            CGL: NCgl2081(cgl2161)
            CGB: cg2372(mraY)
            CEF: CE2056
            CDI: DIP1601(mraY)
            CJK: jk0747(murX)
            NFA: nfa17630(mraY)
            RHA: RHA1_ro01091 RHA1_ro01480
            SCO: SCO2087(murX)
            SMA: SAV6119(murX)
            TWH: TWT224(murX)
            TWS: TW546(mraY)
            LXX: Lxx15290(murX)
            CMI: CMM_1862(mraY)
            ART: Arth_1567
            AAU: AAur_1707(mraY)
            PAC: PPA0755
            NCA: Noca_3066
            TFU: Tfu_1107
            FRA: Francci3_1412
            FAL: FRAAL2193(murX)
            ACE: Acel_1007
            KRA: Krad_3202
            SEN: SACE_5854(murX)
            STP: Strop_3215
            BLO: BL1320(murX)
            BAD: BAD_1104(murX)
            RXY: Rxyl_1496
            FNU: FN1459
            CTR: CT757(mraY)
            CTA: CTA_0827(mraY)
            CMU: TC0138
            CPN: CPn0900(mraY)
            CPA: CP0966
            CPJ: CPj0900(mraY)
            CPT: CpB0932
            CCA: CCA00868(mraY)
            CAB: CAB834
            CFE: CF0148(mraY)
            PCU: pc1252(mraY)
            BBU: BB0303(mraY)
            BGA: BG0307(mraY)
            BAF: BAPKO_0314(mraY)
            TPA: TP0345
            TDE: TDE2249(mraY)
            LIL: LA2048(mraY1)
            LIC: LIC11866(mraY)
            LBJ: LBJ_0478(mraY)
            LBL: LBL_2601(mraY)
            SYN: sll0657(mraY)
            SYW: SYNW2516(mraY)
            SYC: syc1353_d(mraY)
            SYF: Synpcc7942_0152
            SYD: Syncc9605_2682
            SYE: Syncc9902_2311
            SYG: sync_2931(mraY)
            SYR: SynRCC307_2525(mraY)
            SYX: SynWH7803_2522(mraY)
            CYA: CYA_1982(mraY)
            CYB: CYB_1146(mraY)
            TEL: tll0971
            GVI: gll3738
            ANA: all4316
            AVA: Ava_1267 Ava_2077 Ava_3765
            PMA: Pro1878(rfe)
            PMM: PMM1709(mraY)
            PMT: PMT2264(mraY)
            PMN: PMN2A_1320
            PMI: PMT9312_1802
            PMB: A9601_19191(mraY)
            PMC: P9515_19011(mraY)
            PMF: P9303_30121(mraY)
            PMG: P9301_19001(mraY)
            PMH: P9215_19821
            PME: NATL1_21931(mraY)
            TER: Tery_4589
            BTH: BT_3451
            BFR: BF0309
            BFS: BF0257(mraY)
            PGI: PG0577(mraY)
            SRU: SRU_0557(mraY)
            CHU: CHU_2742(mraY)
            GFO: GFO_2771(mraY)
            FJO: Fjoh_1807
            FPS: FP2060(mraY)
            CTE: CT0037(mraY)
            CCH: Cag_0052 Cag_0647
            CPH: Cpha266_2724
            PVI: Cvib_1756
            PLT: Plut_2113
            RRS: RoseRS_3782
            RCA: Rcas_1099
            DRA: DR_1835
            DGE: Dgeo_1461
            TTH: TTC0716
            TTJ: TTHA1081
            AAE: aq_053(mraY)
            TMA: TM0235
            TPT: Tpet_0689
            TME: Tmel_0665
            FNO: Fnod_0443
            MSI: Msm_0360
            MKA: MK0753(mraY)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.13
            ExPASy - ENZYME nomenclature database: 2.7.8.13
            ExplorEnz - The Enzyme Database: 2.7.8.13
            ERGO genome analysis and discovery system: 2.7.8.13
            BRENDA, the Enzyme Database: 2.7.8.13
            CAS: 9068-50-2
///
ENTRY       EC 2.7.8.14                 Enzyme
NAME        CDP-ribitol ribitolphosphotransferase;
            teichoic-acid synthase;
            polyribitol phosphate synthetase;
            teichoate synthetase;
            poly(ribitol phosphate) synthetase;
            polyribitol phosphate polymerase;
            teichoate synthase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     CDP-ribitol:poly(ribitol phosphate) ribitolphosphotransferase
REACTION    CDP-ribitol + (ribitol phosphate)n = CMP + (ribitol phosphate)n+1
            [RN:R04083 R06235]
ALL_REAC    R04083 R06235(G)
SUBSTRATE   CDP-ribitol [CPD:C00789];
            (ribitol phosphate)n [CPD:C00653]
PRODUCT     CMP [CPD:C00055];
            (ribitol phosphate)n+1 [CPD:C00653]
REFERENCE   1  [PMID:5908130]
  AUTHORS   Ishimoto N, Strominger JL.
  TITLE     Polyribitol phosphate synthetase of Staphylococcus aureus.
  JOURNAL   J. Biol. Chem. 241 (1966) 639-50.
  ORGANISM  Staphylococcus aureus
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.14
            ExPASy - ENZYME nomenclature database: 2.7.8.14
            ExplorEnz - The Enzyme Database: 2.7.8.14
            ERGO genome analysis and discovery system: 2.7.8.14
            BRENDA, the Enzyme Database: 2.7.8.14
            CAS: 9076-71-5
///
ENTRY       EC 2.7.8.15                 Enzyme
NAME        UDP-N-acetylglucosamine---dolichyl-phosphate
            N-acetylglucosaminephosphotransferase;
            UDP-D-N-acetylglucosamine N-acetylglucosamine 1-phosphate
            transferase;
            UDP-GlcNAc:dolichyl-phosphate GlcNAc-1-phosphate transferase;
            UDP-N-acetyl-D-glucosamine:dolichol phosphate
            N-acetyl-D-glucosamine-1-phosphate transferase;
            uridine diphosphoacetylglucosamine-dolichyl phosphate
            acetylglucosamine-1-phosphotransferase;
            chitobiosylpyrophosphoryldolichol synthase;
            dolichol phosphate N-acetylglucosamine-1-phosphotransferase;
            UDP-acetylglucosamine-dolichol phosphate acetylglucosamine
            phosphotransferase;
            UDP-acetylglucosamine-dolichol phosphate
            acetylglucosamine-1-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     UDP-N-acetyl-D-glucosamine:dolichyl-phosphate
            N-acetyl-D-glucosaminephosphotransferase
REACTION    UDP-N-acetyl-D-glucosamine + dolichyl phosphate = UMP +
            N-acetyl-D-glucosaminyl-diphosphodolichol [RN:R01007 R05969]
ALL_REAC    R01007 R05969(G)
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            dolichyl phosphate [CPD:C00110]
PRODUCT     UMP [CPD:C00105];
            N-acetyl-D-glucosaminyl-diphosphodolichol [CPD:C04500]
REFERENCE   1  [PMID:6215245]
  AUTHORS   Sharma CB, Lehle L, Tanner W.
  TITLE     Solubilization and characterization of the initial enzymes of the
            dolichol pathway from yeast.
  JOURNAL   Eur. J. Biochem. 126 (1982) 319-25.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:6447695]
  AUTHORS   Villemez CL, Carlo PL.
  TITLE     Properties of a soluble polyprenyl phosphate.
            UDP-D-N-acetylglucosamine N-acetylglucosamine-1-phosphate
            transferase.
  JOURNAL   J. Biol. Chem. 255 (1980) 8174-8.
  ORGANISM  Acanthamoeba castellanii
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K01001  UDP-N-acetylglucosamine--dolichyl-phosphate
                        N-acetylglucosaminephosphstransferase
GENES       HSA: 1798(DPAGT1)
            PTR: 451602(DPAGT1)
            MMU: 13478(Dpagt1)
            RNO: 300668(H2afx)
            CFA: 489371(DPAGT1)
            BTA: 537812(DPAGT1)
            GGA: 419699(DPAGT1)
            DRE: 566539(dpagt1)
            SPU: 590324(LOC590324)
            DME: Dmel_CG5287
            CEL: Y60A3A.14
            ATH: AT2G41490(GPT) AT3G57220
            OSA: 4344180
            CME: CMQ042C
            SCE: YBR243C(ALG7)
            AGO: AGOS_AFL037W
            PIC: PICST_36364(ALG7)
            CGR: CAGL0C01727g
            SPO: SPBC15D4.04(gpt)
            ANI: AN5888.2
            AFM: AFUA_2G11240
            AOR: AO090026000526
            CNE: CNK00270
            UMA: UM03679.1
            DDI: DDBDRAFT_0229808
            PFA: MAL3P7.16
            CPV: cgd5_2240
            CHO: Chro.50156
            TAN: TA18965
            TPV: TP01_0118
            TET: TTHERM_00070990
            TBR: Tb11.01.2220
            TCR: 503823.104 510283.140
            LMA: LmjF36.4180
            EHI: 142.t00005
            MJA: MJ1113
            MMP: MMP1423
            MMA: MM_2096
            MBU: Mbur_0124
            MTH: MTH590
            MST: Msp_0080
            MSI: Msm_0066
            PHO: PH0348
            PAB: PAB1288
            PFU: PF0394
            TKO: TK2254
            SSO: SSO0060(gnptA)
            STO: ST2057
            SAI: Saci_0093
            PAI: PAE3488
            NEQ: NEQ061
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.15
            ExPASy - ENZYME nomenclature database: 2.7.8.15
            ExplorEnz - The Enzyme Database: 2.7.8.15
            ERGO genome analysis and discovery system: 2.7.8.15
            BRENDA, the Enzyme Database: 2.7.8.15
            CAS: 70431-08-2
///
ENTRY       EC 2.7.8.16       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
COMMENT     Deleted entry: 1-alkyl-2-acetylglycerol choline phosphotransferase.
            Now included with EC 2.7.8.2 diacylglycerol
            cholinephosphotransferase (EC 2.7.8.16 created 1983, deleted 1986)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.16
            ExPASy - ENZYME nomenclature database: 2.7.8.16
            ExplorEnz - The Enzyme Database: 2.7.8.16
            ERGO genome analysis and discovery system: 2.7.8.16
            BRENDA, the Enzyme Database: 2.7.8.16
///
ENTRY       EC 2.7.8.17                 Enzyme
NAME        UDP-N-acetylglucosamine---lysosomal-enzyme
            N-acetylglucosaminephosphotransferase;
            N-acetylglucosaminylphosphotransferase;
            UDP-N-acetylglucosamine:lysosomal enzyme
            N-acetylglucosamine-1-phosphotransferase;
            UDP-GlcNAc:glycoprotein N-acetylglucosamine-1-phosphotransferase;
            uridine diphosphoacetylglucosamine-lysosomal enzyme precursor
            acetylglucosamine-1-phosphotransferase;
            uridine diphosphoacetylglucosamine-glycoprotein
            acetylglucosamine-1-phosphotransferase;
            lysosomal enzyme precursor acetylglucosamine-1-phosphotransferase;
            N-acetylglucosaminyl phosphotransferase;
            UDP-acetylglucosamine:lysosomal enzyme
            N-acetylglucosamine-1-phosphotransferase;
            UDP-GlcNAc:lysosomal enzyme
            N-acetylglucosamine-1-phosphotransferase;
            UDP-N-acetylglucosamine:glycoprotein
            N-acetylglucosamine-1-phosphotransferase;
            UDP-N-acetylglucosamine:glycoprotein
            N-acetylglucosaminyl-1-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     UDP-N-acetyl-D-glucosamine:lysosomal-enzyme
            N-acetylglucosaminephosphotransferase
REACTION    UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose = UMP +
            lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
            [RN:R04291]
ALL_REAC    R04291
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043];
            lysosomal-enzyme D-mannose [CPD:C03706]
PRODUCT     UMP [CPD:C00105];
            lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
            [CPD:C04789]
COMMENT     Some other glycoproteins with high-mannose can act as acceptors, but
            much more slowly than lysosomal enzymes.
REFERENCE   1  [PMID:6452459]
  AUTHORS   Reitman ML, Kornfeld S.
  TITLE     UDP-N-acetylglucosamine:glycoprotein
            N-acetylglucosamine-1-phosphotransferase. Proposed enzyme for the
            phosphorylation of the high mannose oligosaccharide units of
            lysosomal enzymes.
  JOURNAL   J. Biol. Chem. 256 (1981) 4275-81.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6457829]
  AUTHORS   Reitman ML, Kornfeld S.
  TITLE     Lysosomal enzyme targeting. N-Acetylglucosaminylphosphotransferase
            selectively phosphorylates native lysosomal enzymes.
  JOURNAL   J. Biol. Chem. 256 (1981) 11977-80.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:6288715]
  AUTHORS   Waheed A, Hasilik A, von Figura K.
  TITLE     UDP-N-acetylglucosamine:lysosomal enzyme precursor
            N-acetylglucosamine-1-phosphotransferase. Partial purification and
            characterization of the rat liver Golgi enzyme.
  JOURNAL   J. Biol. Chem. 257 (1982) 12322-31.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:6260788]
  AUTHORS   Waheed A, Pohlmann R, Hasilik A, von Figura K.
  TITLE     Subcellular location of two enzymes involved in the synthesis of
            phosphorylated recognition markers in lysosomal enzymes.
  JOURNAL   J. Biol. Chem. 256 (1981) 4150-2.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K08239  UDP-N-acetylglucosamine-lysosomal-enzyme
GENES       HSA: 79158(GNPTAB)
            PTR: 452176(GNPTAB)
            MMU: 432486(Gnptab)
            RNO: 362865(RGD1564821_predicted)
            CFA: 475443(GNPTAB)
            BTA: 509610(LOC509610)
            GGA: 418096(GNPTAB)
            DRE: 553365(si:ch211-234f20.3)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.17
            ExPASy - ENZYME nomenclature database: 2.7.8.17
            ExplorEnz - The Enzyme Database: 2.7.8.17
            ERGO genome analysis and discovery system: 2.7.8.17
            BRENDA, the Enzyme Database: 2.7.8.17
            CAS: 84012-69-1
///
ENTRY       EC 2.7.8.18                 Enzyme
NAME        UDP-galactose---UDP-N-acetylglucosamine galactose
            phosphotransferase;
            uridine diphosphogalactose-uridine diphosphoacetylglucosamine
            galactose-1-phosphotransferase;
            galactose-1-phosphotransferase;
            galactosyl phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     UDP-galactose:UDP-N-acetyl-D-glucosamine galactose
            phosphotransferase
REACTION    UDP-galactose + UDP-N-acetyl-D-glucosamine = UMP +
            UDP-N-acetyl-6-(D-galactose-1-phospho)-D-glucosamine [RN:R00504]
ALL_REAC    R00504
SUBSTRATE   UDP-galactose [CPD:C00052];
            UDP-N-acetyl-D-glucosamine [CPD:C00043]
PRODUCT     UMP [CPD:C00105];
            UDP-N-acetyl-6-(D-galactose-1-phospho)-D-glucosamine [CPD:C04739]
COMMENT     N-Acetylglucosamine end-groups in glycoproteins can also act as
            acceptors.
REFERENCE   1  [PMID:6130977]
  AUTHORS   Nakanishi Y, Otsu K, Suzuki S.
  TITLE     Enzymatic transfer of galactosyl phosphate from UDP-galactose to
            UDP-N-acetylglucosamine.
  JOURNAL   FEBS. Lett. 151 (1983) 15-8.
  ORGANISM  chicken [GN:gga]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.18
            ExPASy - ENZYME nomenclature database: 2.7.8.18
            ExplorEnz - The Enzyme Database: 2.7.8.18
            ERGO genome analysis and discovery system: 2.7.8.18
            BRENDA, the Enzyme Database: 2.7.8.18
            CAS: 84932-43-4
///
ENTRY       EC 2.7.8.19                 Enzyme
NAME        UDP-glucose---glycoprotein glucose phosphotransferase;
            UDP-glucose:glycoprotein glucose-1-phosphotransferase;
            GlcPTase;
            Glc-phosphotransferase;
            uridine diphosphoglucose-glycoprotein glucose-1-phosphotransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     UDP-glucose:glycoprotein-D-mannose glucosephosphotransferase
REACTION    UDP-glucose + glycoprotein D-mannose = UMP + glycoprotein
            6-(D-glucose-1-phospho)-D-mannose [RN:R04179]
ALL_REAC    R04179
SUBSTRATE   UDP-glucose [CPD:C00029];
            glycoprotein D-mannose [CPD:C03268]
PRODUCT     UMP [CPD:C00105];
            glycoprotein 6-(D-glucose-1-phospho)-D-mannose [CPD:C04645]
COMMENT     Penultimate mannose residues on oligo-mannose type glycoproteins can
            act as acceptors.
REFERENCE   1  [PMID:6297779]
  AUTHORS   Koro LA, Marchase RB.
  TITLE     A UDP-glucose:glycoprotein glucose-1-phosphotransferase in embryonic
            chicken neural retina.
  JOURNAL   Cell. 31 (1982) 739-48.
  ORGANISM  chicken [GN:gga]
ORTHOLOGY   KO: K05965  
GENES       PIC: PICST_45091(KRE5)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.19
            ExPASy - ENZYME nomenclature database: 2.7.8.19
            ExplorEnz - The Enzyme Database: 2.7.8.19
            ERGO genome analysis and discovery system: 2.7.8.19
            BRENDA, the Enzyme Database: 2.7.8.19
            CAS: 84861-40-5
///
ENTRY       EC 2.7.8.20                 Enzyme
NAME        phosphatidylglycerol---membrane-oligosaccharide
            glycerophosphotransferase;
            phosphoglycerol transferase;
            oligosaccharide glycerophosphotransferase;
            phosphoglycerol transferase I
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     phosphatidylglycerol:membrane-derived-oligosaccharide-D-glucose
            glycerophosphotransferase
REACTION    phosphatidylglycerol + membrane-derived-oligosaccharide D-glucose =
            1,2-diacyl-sn-glycerol + membrane-derived-oligosaccharide
            6-(glycerophospho)-D-glucose [RN:R04511]
ALL_REAC    R04511;
            (other) R05081
SUBSTRATE   phosphatidylglycerol [CPD:C00344];
            membrane-derived-oligosaccharide D-glucose [CPD:C04566]
PRODUCT     1,2-diacyl-sn-glycerol [CPD:C00641];
            membrane-derived-oligosaccharide 6-(glycerophospho)-D-glucose
            [CPD:C04809]
COMMENT     1,2-beta- and 1,6-beta-linked glucose residues in membrane
            polysaccharides and in synthetic glucosides can act as acceptors.
REFERENCE   1  [PMID:6296144]
  AUTHORS   Jackson BJ, Kennedy EP.
  TITLE     The biosynthesis of membrane-derived oligosaccharides. A
            membrane-bound phosphoglycerol transferase.
  JOURNAL   J. Biol. Chem. 258 (1983) 2394-8.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00561  Glycerolipid metabolism
ORTHOLOGY   KO: K01002  phosphoglycerol transferase
GENES       ECO: b4359(mdoB)
            ECJ: JW5794(mdoB)
            ECE: Z5959(mdoB)
            ECS: ECs5319
            ECC: c5438(mdoB)
            ECI: UTI89_C5065(mdoB)
            ECP: ECP_4690
            ECV: APECO1_2065(mdoB)
            ECW: EcE24377A_4952(mdoB)
            ECX: EcHS_A4591
            STY: STY4894(mdoB)
            STT: t4584(mdoB)
            SPT: SPA4355(mdoB)
            SEC: SC4393(mdoB)
            STM: STM4541(mdoB)
            SFL: SF4390(mdoB)
            SFX: S4660(mdoB)
            SFV: SFV_4390(mdoB)
            SSN: SSON_4505(mdoB)
            SBO: SBO_4419(mdoB)
            SDY: SDY_4613(mdoB)
            ENT: Ent638_0514 Ent638_3516
            SPE: Spro_3126
            XCC: XCC0403(mdoB)
            XCB: XC_0416
            XCV: XCV0446(mdoB)
            XAC: XAC0421(mdoB)
            PHA: PSHAa2774(mdoB)
            CSA: Csal_0010
            EBA: ebA3535(mdoB)
            HPA: HPAG1_0557
            CHA: CHAB381_1557
            ABU: Abu_1799
            BCZ: BCZK2666
            BTL: BALH_2635
            BPU: BPUM_2214(yqgS)
            LIL: LA2580
            FPS: FP0883 FP0962
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.20
            ExPASy - ENZYME nomenclature database: 2.7.8.20
            ExplorEnz - The Enzyme Database: 2.7.8.20
            ERGO genome analysis and discovery system: 2.7.8.20
            BRENDA, the Enzyme Database: 2.7.8.20
            CAS: 80146-86-7
///
ENTRY       EC 2.7.8.21                 Enzyme
NAME        membrane-oligosaccharide glycerophosphotransferase;
            periplasmic phosphoglycerotransferase;
            phosphoglycerol cyclase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     membrane-derived-oligosaccharide-6-(glycerophospho)-D-glucose:membra
            ne-derived-oligosaccharide-D-glucose glycerophosphotransferase
REACTION    Transfer of a glycerophospho group from one membrane-derived
            oligosaccharide to another
COMMENT     beta-Linked glucose residues in simple glucosides, such as
            gentiobiose, can act as acceptors. In the presence of low
            concentrations of acceptor, free cyclic 1,2-phosphoglycerol is
            formed.
REFERENCE   1  [PMID:6272307]
  AUTHORS   Goldberg DE, Rumley MK, Kennedy EP.
  TITLE     Biosynthesis of membrane-derived oligosaccharides: a periplasmic
            phosphoglyceroltransferase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 78 (1981) 5513-7.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.21
            ExPASy - ENZYME nomenclature database: 2.7.8.21
            ExplorEnz - The Enzyme Database: 2.7.8.21
            ERGO genome analysis and discovery system: 2.7.8.21
            BRENDA, the Enzyme Database: 2.7.8.21
            CAS: 80146-86-7
///
ENTRY       EC 2.7.8.22                 Enzyme
NAME        1-alkenyl-2-acylglycerol choline phosphotransferase;
            CDP-choline-1-alkenyl-2-acyl-glycerol phosphocholinetransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     CDP-choline:1-alkenyl-2-acylglycerol cholinephosphotransferase
REACTION    CDP-choline + 1-alkenyl-2-acylglycerol = CMP + plasmenylcholine
            [RN:R03110]
ALL_REAC    R03110
SUBSTRATE   CDP-choline [CPD:C00307];
            1-alkenyl-2-acylglycerol [CPD:C03454]
PRODUCT     CMP [CPD:C00055];
            plasmenylcholine [CPD:C00958]
REFERENCE   1  [PMID:3447597]
  AUTHORS   Wientzek M, Man RY, Choy PC.
  TITLE     Choline glycerophospholipid biosynthesis in the guinea pig heart.
  JOURNAL   Biochem. Cell. Biol. 65 (1987) 860-8.
  ORGANISM  guinea pig
PATHWAY     PATH: map00565  Ether lipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.22
            ExPASy - ENZYME nomenclature database: 2.7.8.22
            ExplorEnz - The Enzyme Database: 2.7.8.22
            ERGO genome analysis and discovery system: 2.7.8.22
            BRENDA, the Enzyme Database: 2.7.8.22
            CAS: 113066-36-7
///
ENTRY       EC 2.7.8.23                 Enzyme
NAME        carboxyvinyl-carboxyphosphonate phosphorylmutase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     1-carboxyvinyl carboxyphosphonate phosphorylmutase (decarboxylating)
REACTION    1-carboxyvinyl carboxyphosphonate =
            3-(hydrohydroxyphosphoryl)pyruvate + CO2 [RN:R05165]
ALL_REAC    R05165
SUBSTRATE   1-carboxyvinyl carboxyphosphonate [CPD:C06367]
PRODUCT     3-(hydrohydroxyphosphoryl)pyruvate [CPD:C06368];
            CO2 [CPD:C00011]
COMMENT     Catalyses the transfer and decarboxylation of the
            carboxy(hydroxy)phosphoryl group, HOOC-P(O)(OH)- (phosphoryl being a
            3-valent group), in the formation of an unusual C-P bond that is
            involved in the biosynthesis of the antibiotic bialaphos.
REFERENCE   1  [PMID:1330557]
  AUTHORS   Pollack SJ, Freeman S, Pompliano DL, Knowles JR.
  TITLE     Cloning, overexpression and mechanistic studies of
            carboxyphosphonoenolpyruvate mutase from Streptomyces hygroscopicus.
  JOURNAL   Eur. J. Biochem. 209 (1992) 735-43.
  ORGANISM  Streptomyces hygroscopicus
REFERENCE   2  [PMID:3611020]
  AUTHORS   Anzai H, Murakami T, Imai S, Satoh A, Nagaoka K, Thompson CJ.
  TITLE     Transcriptional regulation of bialaphos biosynthesis in Streptomyces
            hygroscopicus.
  JOURNAL   J. Bacteriol. 169 (1987) 3482-8.
  ORGANISM  Streptomyces hygroscopicus
ORTHOLOGY   KO: K01003  carboxyvinyl-carboxyphosphonate phosphorylmutase
GENES       AFM: AFUA_5G07230
            PAE: PA4872
            PAU: PA14_16740 PA14_64440(bcpA)
            PPU: PP_1389
            PST: PSPTO_1443(bcpA)
            PSB: Psyr_1256
            PSP: PSPPH_1328(bcpA)
            PFL: PFL_2455
            PFO: Pfl_2052
            PEN: PSEEN1269 PSEEN4356
            CSA: Csal_0251
            CVI: CV_1518 CV_2057(prpB)
            RSO: RSc2000(prpB1)
            REU: Reut_B4474
            RME: Rmet_4291
            BXE: Bxe_B0461 Bxe_B1203 Bxe_B2147 Bxe_C0659 Bxe_C0661
            BUR: Bcep18194_B1614
            BPE: BP0718
            BPA: BPP1125 BPP3673
            BBR: BB0718(bcpA) BB1341 BB4108
            HAR: HEAR3266
            MMS: mma_3487
            HHE: HH0397(prpB)
            MES: Meso_2513
            RLE: RL4464
            BJA: bll5266
            BRA: BRADO3250 BRADO5508
            BBT: BBta_1130 BBta_4901 BBta_5990
            RPA: RPA2395(prpB) RPA3174
            RPB: RPB_2368
            RPC: RPC_3351 RPC_3510
            RPD: RPD_3092
            RPE: RPE_3171 RPE_3438
            RDE: RD1_2188
            RRU: Rru_A2320
            BSU: BG11720(yqiQ)
            BHA: BH3922
            BAN: BA2350(yqiQ)
            BAR: GBAA2350(yqiQ)
            BAT: BAS2190
            BCE: BC2287
            BCA: BCE_2378(yqiQ)
            BTK: BT9727_2127(prpB)
            BLI: BL00563(yqiQ)
            BLD: BLi04096(yqiQ)
            BCL: ABC1807
            BPU: BPUM_1846(yqiQ)
            OIH: OB2267
            MSM: MSMEG_0422 MSMEG_2506 MSMEG_4393 MSMEG_6855
            MMC: Mmcs_0256
            RHA: RHA1_ro02162
            FRA: Francci3_2201
            SEN: SACE_0758 SACE_4109
            LIL: LA1416
            LIC: LIC12331
            SYG: sync_2678
            SYR: SynRCC307_0523
            NPH: NP4432A(prpB_2) NP6212A(prpB_1)
            TAC: Ta1227
            TVO: TVN0368
            APE: APE_0222.1
            SSO: SSO2587(prpB)
            STO: ST1808
            SAI: Saci_0244
            PAI: PAE1716(prpB)
STRUCTURES  PDB: 2QIW  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.23
            ExPASy - ENZYME nomenclature database: 2.7.8.23
            ExplorEnz - The Enzyme Database: 2.7.8.23
            ERGO genome analysis and discovery system: 2.7.8.23
            BRENDA, the Enzyme Database: 2.7.8.23
            CAS: 122799-57-9
///
ENTRY       EC 2.7.8.24                 Enzyme
NAME        phosphatidylcholine synthase;
            CDP-diglyceride-choline O-phosphatidyltransferase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     CDP-diacylglycerol:choline O-phosphatidyltransferase
REACTION    CDP-diacylglycerol + choline = CMP + phosphatidylcholine [RN:R05794]
ALL_REAC    R05794
SUBSTRATE   CDP-diacylglycerol [CPD:C00269];
            choline [CPD:C00114]
PRODUCT     CMP [CPD:C00055];
            phosphatidylcholine [CPD:C00157]
COMMENT     Requires divalent cations, with Mn2+ being more effective than Mg2+.
REFERENCE   1  [PMID:10391951]
  AUTHORS   de Rudder KE, Sohlenkamp C, Geiger O.
  TITLE     Plant-exuded choline is used for rhizobial membrane lipid
            biosynthesis by phosphatidylcholine synthase.
  JOURNAL   J. Biol. Chem. 274 (1999) 20011-6.
  ORGANISM  Sinorhizobium meliloti [GN:sme]
REFERENCE   2  [PMID:10858449]
  AUTHORS   Sohlenkamp C, de Rudder KE, Rohrs V, Lopez-Lara IM, Geiger O.
  TITLE     Cloning and characterization of the gene for phosphatidylcholine
            synthase.
  JOURNAL   J. Biol. Chem. 275 (2000) 18919-25.
  ORGANISM  Sinorhizobium meliloti [GN:sme]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K01004  phosphatidylcholine synthase
GENES       PAE: PA3857
            PAU: PA14_14110(pcs)
            PST: PSPTO_1000
            PSB: Psyr_0866
            PSP: PSPPH_0901
            PFL: PFL_4055
            PFO: Pfl_2093
            PMY: Pmen_3554
            LPN: lpg1584
            LPF: lpl1441(lidK)
            LPP: lpp1542(lidK)
            FTU: FTT1563(pcs)
            FTF: FTF1563(pcs)
            FTL: FTL_0545
            FTH: FTH_0547(pcs)
            FTN: FTN_1471(pcs)
            MLO: mll0506
            MES: Meso_1695
            PLA: Plav_1484
            SME: SMc00247(pcs)
            SMD: Smed_1420
            ATU: Atu1793(pcs)
            ATC: AGR_C_3299
            RET: RHE_CH02079(pcs)
            RLE: RL2370(pcs)
            BME: BMEII0695
            BMF: BAB2_0668
            BMS: BRA0572(pcs)
            BMB: BruAb2_0652(pcs)
            BOV: BOV_A0538
            OAN: Oant_3634
            BJA: bll4585(pcs)
            BRA: BRADO3781
            BBT: BBta_4148
            RPA: RPA2672
            RPB: RPB_2842
            RPC: RPC_2618
            RPD: RPD_2630
            RPE: RPE_2798
            NWI: Nwi_1506
            NHA: Nham_2046
            BHE: BH08530(pcsA)
            BQU: BQ06040(pcsA)
            BBK: BARBAKC583_0817(pcs)
            SIL: SPO3131(pcs)
            SIT: TM1040_2382
            RSP: RSP_0565
            RSH: Rsph17029_2217
            RSQ: Rsph17025_0497
            JAN: Jann_1029
            RDE: RD1_2077(pcs)
            PDE: Pden_0811
            RXY: Rxyl_0272
            RBA: RB4506
            BBU: BB0249
            BGA: BG0251
            BAF: BAPKO_0258
            SRU: SRU_0340
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.24
            ExPASy - ENZYME nomenclature database: 2.7.8.24
            ExplorEnz - The Enzyme Database: 2.7.8.24
            ERGO genome analysis and discovery system: 2.7.8.24
            BRENDA, the Enzyme Database: 2.7.8.24
            CAS: 243666-86-6
///
ENTRY       EC 2.7.8.25                 Enzyme
NAME        triphosphoribosyl-dephospho-CoA synthase;
            2'-(5"-triphosphoribosyl)-3-dephospho-CoA synthase;
            ATP:dephospho-CoA 5-triphosphoribosyl transferase;
            CitG
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     ATP:3-dephospho-CoA 5"-triphosphoribosyltransferase
REACTION    ATP + 3-dephospho-CoA = 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA +
            adenine
SUBSTRATE   ATP [CPD:C00002];
            3-dephospho-CoA
PRODUCT     2'-(5''-triphosphoribosyl)-3'-dephospho-CoA;
            adenine [CPD:C00147]
COMMENT     ATP cannot be replaced by GTP, CTP, UTP, ADP or AMP.
            2'-(5"-Triphosphoribosyl)-3'-dephospho-CoA is the precursor of the
            phosphoribosyl-3-dephospho-CoA prosthetic group of the acyl carrier
            protein subunit of EC 4.1.3.6, citrate (pro-3S) lyase.
REFERENCE   1  [PMID:10924139]
  AUTHORS   Schneider K, Dimroth P, Bott M.
  TITLE     Biosynthesis of the prosthetic group of citrate lyase.
  JOURNAL   Biochemistry. 39 (2000) 9438-50.
  ORGANISM  Escherichia coli [GN:eco], Klebsiella pneumoniae
REFERENCE   2  [PMID:11042274]
  AUTHORS   Schneider K, Dimroth P, Bott M.
  TITLE     Identification of triphosphoribosyl-dephospho-CoA as precursor of
            the citrate lyase prosthetic group.
  JOURNAL   FEBS. Lett. 483 (2000) 165-8.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K05966  triphosphoribosyl-dephospho-CoA synthase
GENES       ECO: b0613(citG)
            ECJ: JW0605(citG)
            ECE: Z0757(citG)
            ECS: ECs0652
            ECC: c0701(citG)
            ECI: UTI89_C0615(citG)
            ECV: APECO1_1438(citG)
            ECW: EcE24377A_0635(citG)
            ECX: EcHS_A0664(citG)
            STY: STY0072(citG2) STY0668(citG)
            STT: t0065(citG) t2248(citG)
            SPT: SPA0064(citG) SPA2115(citG)
            SEC: SC0057(citG2) SC0648(citG)
            STM: STM0063(citG2) STM0619(citG)
            SFX: S0537(citG)
            SFV: SFV_0566(citG)
            SSN: SSON_0565(citG)
            SBO: SBO_0478(citG)
            ECA: ECA2569(citG)
            ENT: Ent638_3370 Ent638_3778
            SPE: Spro_3166
            HIN: HI0021(citG)
            HIT: NTHI0028(citG)
            HDU: HD1245(citG)
            ASU: Asuc_1198
            XCC: XCC3614(citG)
            XCB: XC_0577
            XCV: XCV0599(mdcB)
            XAC: XAC0565(citG)
            VCH: VC0801
            VCO: VC0395_A0328(citG)
            PPR: PBPRA2290
            PAE: PA0209
            PAU: PA14_02560(mdcB)
            PAP: PSPA7_0293(mdcB)
            PST: PSPTO_5086(mdcB)
            PSB: Psyr_0443
            PSP: PSPPH_0434(citG)
            PFO: Pfl_5301
            PAR: Psyc_1141(mdc)
            ACI: ACIAD1754(mdcB)
            PIN: Ping_3658
            LPN: lpg2430(mdcB)
            LPP: lpp2497
            REU: Reut_B4926
            BMA: BMA3032(citG)
            BMN: BMA10247_0544(mdcB)
            BVI: Bcep1808_1228
            BUR: Bcep18194_A4417
            BCN: Bcen_0793
            BCH: Bcen2424_1274
            BAM: Bamb_1152
            BPS: BPSL1334
            BPM: BURPS1710b_1589(citG)
            BPD: BURPS668_1457(mdcB)
            RFR: Rfer_1848 Rfer_2405
            PNA: Pnap_0947
            VEI: Veis_2891
            MPT: Mpe_A0789 Mpe_A2891
            HAR: HEAR1474
            DAR: Daro_4015
            GSU: GSU0806(citG)
            BJA: bll0265(mdcB) bll1272(mdcB)
            RPB: RPB_3301
            RPC: RPC_1054 RPC_4592
            RPE: RPE_3432
            SWI: Swit_4291
            RRU: Rru_A1319
            SPY: SPy_1178(citG)
            SPZ: M5005_Spy_0898
            SPM: spyM18_1130
            SPG: SpyM3_0826(citG)
            SPS: SPs1026
            SPH: MGAS10270_Spy1012
            SPI: MGAS10750_Spy1047
            SPF: SpyM50899(citG)
            SPA: M6_Spy0887
            SPB: M28_Spy0871
            SMU: SMU.1011(citG)
            LPL: lp_1093(citG)
            LAC: LBA1240(citG)
            LSA: LSA1220(citG)
            LCA: LSEI_1853
            EFA: EF3315
            OOE: OEOE_0425
            CPE: CPE1145(citG)
            CPR: CPR_1161(citG)
            CTC: CTC02555(citG)
            AMT: Amet_3408
            MSM: MSMEG_6634(mdcB)
            SMA: SAV4233(mdcB)
            FNU: FN1377(citG)
            TDE: TDE1523
            MAC: MA0694
            MMA: MM_1852
            MHU: Mhun_0666
            MTH: MTH743
            MKA: MK0876(citG_2)
            HWA: HQ3014A(citG)
            NPH: NP2024A
            APE: APE_1715.1(citG)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.25
            ExPASy - ENZYME nomenclature database: 2.7.8.25
            ExplorEnz - The Enzyme Database: 2.7.8.25
            ERGO genome analysis and discovery system: 2.7.8.25
            BRENDA, the Enzyme Database: 2.7.8.25
            CAS: 313345-38-9
///
ENTRY       EC 2.7.8.26                 Enzyme
NAME        adenosylcobinamide-GDP ribazoletransferase;
            CobS;
            cobalamin synthase;
            cobalamin-5'-phosphate synthase;
            cobalamin (5'-phosphate) synthase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     adenosylcobinamide-GDP:alpha-ribazole ribazoletransferase
REACTION    (1) adenosylcobinamide-GDP + alpha-ribazole = GMP +
            adenosylcobalamin [RN:R05223];
            (2) adenosylcobinamide-GDP + alpha-ribazole 5'-phosphate = GMP +
            adenosylcobalamin 5'-phosphate
ALL_REAC    R05223
SUBSTRATE   adenosylcobinamide-GDP [CPD:C06510];
            alpha-ribazole [CPD:C05775];
            alpha-ribazole 5'-phosphate [CPD:C04778]
PRODUCT     GMP [CPD:C00144];
            adenosylcobalamin [CPD:C00194];
            adenosylcobalamin 5'-phosphate
COMMENT     In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC
            2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73)
            and CobS (EC 2.7.8.26) catalyse reactions in the nucleotide loop
            assembly pathway, which convert adenosylcobinamide (AdoCbi) into
            adenosylcobalamin (AdoCbl). CobT and CobC are involved in
            5,6-dimethylbenzimidazole activation whereby
            5,6-dimethylbenzimidazole is converted to its riboside,
            alpha-ribazole. The second branch of the nucleotide loop assembly
            pathway is the cobinamide activation branch where AdoCbi or
            adenosylcobinamide-phosphate is converted to the activated
            intermediate AdoCbi-GDP by the bifunctional enzyme Cob U. CobS
            catalyses the final step in adenosylcobalamin biosynthesis, which is
            the condensation of AdoCbi-GDP with alpha-ribazole to yield
            adenosylcobalamin.
REFERENCE   1  [PMID:10518530]
  AUTHORS   Maggio-Hall LA, Escalante-Semerena JC.
  TITLE     In vitro synthesis of the nucleotide loop of cobalamin by Salmonella
            typhimurium enzymes.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 11798-803.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:12195810]
  AUTHORS   Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
  TITLE     The biosynthesis of adenosylcobalamin (vitamin B12).
  JOURNAL   Nat. Prod. Rep. 19 (2002) 390-412.
  ORGANISM  Pseudomonas denitrificans
REFERENCE   3  [PMID:1917841]
  AUTHORS   Cameron B, Blanche F, Rouyez MC, Bisch D, Famechon A, Couder M,
            Cauchois L, Thibaut D, Debussche L, Crouzet J.
  TITLE     Genetic analysis, nucleotide sequence, and products of two
            Pseudomonas denitrificans cob genes encoding nicotinate-nucleotide:
            dimethylbenzimidazole phosphoribosyltransferase and cobalamin
            (5'-phosphate) synthase.
  JOURNAL   J. Bacteriol. 173 (1991) 6066-73.
  ORGANISM  Pseudomonas denitrificans
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K02233  adenosylcobinamide-GDP ribazoletransferase
GENES       ECO: b1992(cobS)
            ECJ: JW1970(cobS)
            ECE: Z3152(cobS)
            ECS: ECs2787
            ECC: c2478(cobS)
            ECI: UTI89_C2230(cobS)
            ECP: ECP_1990
            ECV: APECO1_1073(cobS)
            ECW: EcE24377A_2274(cobS)
            ECX: EcHS_A2115(cobS)
            STY: STY2220(cobS)
            STT: t0857(cobS)
            SPT: SPA0854(cobS)
            SEC: SC2025(cobS)
            STM: STM2017(cobS)
            SFL: SF2060(cobS)
            SFX: S2170(cobS)
            SFV: SFV_2064(cobS)
            SSN: SSON_2053(cobS)
            SBO: SBO_1211(cobS)
            SDY: SDY_2241(cobS)
            PLU: plu2985(cobS)
            XCC: XCC3057(cobS)
            XCB: XC_1101
            XCV: XCV3313(cobS)
            XAC: XAC3184(cobS)
            XOO: XOO1353(cobS)
            XOM: XOO_1243(XOO1243)
            VCH: VC1238
            VVU: VV1_2787
            VVY: VV1475
            VPA: VP1305
            PPR: PBPRA1181
            PAE: PA1281(cobV)
            PAU: PA14_47650(cobV)
            PAP: PSPA7_4108(cobS)
            PPU: PP_1681(cobS)
            PST: PSPTO_1717(cobS)
            PSB: Psyr_3672(cobS)
            PSP: PSPPH_3693(cobS)
            PFL: PFL_4422(cobS)
            PFO: Pfl_1650(cobS)
            PEN: PSEEN1387
            PCR: Pcryo_1027
            SON: SO_1036(cobS)
            SDN: Sden_1118
            SFR: Sfri_0877
            SHE: Shewmr4_0843
            SHM: Shewmr7_3179
            SHN: Shewana3_3277
            CPS: CPS_3658(cobS)
            PHA: PSHAa2998(cobS)
            PAT: Patl_1138
            SDE: Sde_0631
            MCA: MCA0465(cobS)
            AEH: Mlg_2816
            HHA: Hhal_1856
            HCH: HCH_00965(cobS)
            ABO: ABO_0147(cobS)
            CVI: CV_0491(cobS)
            RSO: RSc2396(cobS)
            REU: Reut_A0659(cobS)
            REH: H16_A2967(cobS1)
            RME: Rmet_2784
            BMA: BMA0689(cobS)
            BMV: BMASAVP1_A2323(cobS)
            BML: BMA10299_A2963(cobS)
            BMN: BMA10247_1635(cobS)
            BXE: Bxe_A3498
            BUR: Bcep18194_A5783(cobS)
            BAM: Bamb_2500
            BPS: BPSL0980
            BPM: BURPS1710b_1192(cobS)
            BPL: BURPS1106A_1038(cobS)
            BPD: BURPS668_1032(cobS)
            BTE: BTH_I0838(cobS)
            RFR: Rfer_2610
            POL: Bpro_0740
            MPT: Mpe_A2302(copS) Mpe_B0520(cobS)
            EBA: ebA4005(cobS)
            AZO: azo3561(cobS)
            DAR: Daro_0149(cobS)
            TBD: Tbd_2710(cobS)
            MFA: Mfla_0099
            TDN: Tmden_0111
            ABU: Abu_2181(cobS)
            GSU: GSU3008(cobS)
            GME: Gmet_0468
            PCA: Pcar_0485(cobS)
            DVU: DVU0914(cobS)
            DDE: Dde_2704
            DPS: DP1951(cobS)
            SFU: Sfum_2609
            MLO: mlr1388
            SME: SMc04215(cobV)
            ATU: Atu1891(cobS)
            ATC: AGR_C_3470
            RET: RHE_CH02444(cobV)
            RLE: RL2781A(cobS)
            BME: BMEI1100
            BMF: BAB1_0885(cobS)
            BMS: BR0866(cobS)
            BMB: BruAb1_0878(cobS)
            BOV: BOV_0858(cobS-2)
            BJA: bll3255(cobV)
            RPA: RPA1257(cobS) RPA2095
            RPB: RPB_1259 RPB_3283(cobS)
            RPC: RPC_1894
            RPD: RPD_2325 RPD_3857
            RPE: RPE_3123 RPE_3848
            SIL: SPO1422
            SIT: TM1040_0577
            RSP: RSP_2427(cobV)
            JAN: Jann_3306
            RDE: RD1_1826(cobS)
            HNE: HNE_1511
            NAR: Saro_0326
            GBE: GbCGDNIH1_0670
            RRU: Rru_A0668
            MGM: Mmc1_3278
            BHA: BH1592(cobS)
            GKA: GK2260
            LMO: lmo1148
            LMF: LMOf2365_1155(cobS)
            LIN: lin1112
            LWE: lwe1106(cobS)
            SSA: SSA_0490
            STH: STH1926
            CAC: CAC1384(cobS)
            CPE: CPE1036(cobS)
            CPF: CPF_1291(cobS)
            CPR: CPR_1110(cobS)
            CTC: CTC00719(cobS)
            CNO: NT01CX_2079(cobS)
            CBA: CLB_0862(cobS)
            CBH: CLC_0876(cobS)
            CBF: CLI_0902(cobS)
            DSY: DSY2116(cobS)
            TTE: TTE0382(cobS)
            MTA: Moth_1102
            MTU: Rv2208(cobS)
            MTC: MT2264(cobS)
            MBO: Mb2231(cobS)
            MBB: BCG_2224(cobS)
            MPA: MAP1949(cobS)
            MAV: MAV_2282(cobS)
            MSM: MSMEG_4277(cobS)
            MMC: Mmcs_3306
            CGL: NCgl2121(cgl2201)
            CGB: cg2415(cobS)
            CEF: CE2093
            CDI: DIP1635
            NFA: nfa16990(cobS)
            RHA: RHA1_ro01146(cobS)
            SCO: SCO2177(SC5F7.24)
            SMA: SAV6026(cobS)
            PAC: PPA0442
            TFU: Tfu_0996
            FRA: Francci3_3131
            FAL: FRAAL5142(cobS)
            SEN: SACE_1649(cobS)
            RXY: Rxyl_0648
            FNU: FN0912
            TDE: TDE2383(cobS)
            LIL: LA4205(cobS)
            LIC: LIC13357(cobS)
            LBJ: LBJ_2827(cobS)
            LBL: LBL_0244(cobS)
            SYN: slr0636
            SYW: SYNW0245(cobS)
            SYC: syc1064_d(cobS)
            SYF: Synpcc7942_0454
            SYD: Syncc9605_0239
            SYE: Syncc9902_0268
            SYG: sync_0285(cobS)
            SYR: SynRCC307_2312(cobS)
            SYX: SynWH7803_0289(cobS)
            CYA: CYA_2408(cobS)
            CYB: CYB_2204(cobS)
            TEL: tll1337
            GVI: gll3727(cobS)
            ANA: alr0379
            AVA: Ava_2824
            PMA: Pro0302(cobS)
            PMM: PMM0270(cobS)
            PMT: PMT1861(cobS)
            PMN: PMN2A_1636
            PMI: PMT9312_0272
            PMB: A9601_02921(cobS)
            PMC: P9515_03031(cobS)
            PMF: P9303_24891(cobS)
            PMG: P9301_02931
            PME: NATL1_03491(cobS)
            TER: Tery_2458
            BFR: BF2487
            BFS: BF2520
            PGI: PG0703
            FPS: FP1459(cobS)
            CTE: CT0948(cobS)
            CCH: Cag_1057(cobS)
            PLT: Plut_1131
            DET: DET0658(cobS-1) DET0692(cobS-2)
            DEH: cbdb_A642(cobS)
            DRA: DR_A0239
            DGE: Dgeo_2367
            TTH: TT_P0004
            TTJ: TTHB046
            MJA: MJ1438(cobS)
            MMP: MMP0938(cobS)
            MAC: MA0939(cobS)
            MBA: Mbar_A3456
            MMA: MM_2057
            MBU: Mbur_2092
            MTH: MTH1112
            MSI: Msm_0933
            MKA: MK1671(cobS)
            AFU: AF0037(cobS-1) AF2323(cobS-2)
            HAL: VNG1580H
            HMA: rrnAC1931(cobS)
            HWA: HQ1410A(cobS)
            TAC: Ta1079
            TVO: TVN0495
            PTO: PTO0693
            PHO: PH0373
            PAB: PAB2320(cobS-1)
            PFU: PF0299 PF0836 PF0837
            TKO: TK0857
            RCI: RCIX2652(cobS)
            APE: APE_2037.1
            SSO: SSO3234
            STO: ST2343
            SAI: Saci_0412
            PAI: PAE0379(cobS)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.26
            ExPASy - ENZYME nomenclature database: 2.7.8.26
            ExplorEnz - The Enzyme Database: 2.7.8.26
            ERGO genome analysis and discovery system: 2.7.8.26
            BRENDA, the Enzyme Database: 2.7.8.26
///
ENTRY       EC 2.7.8.27                 Enzyme
NAME        sphingomyelin synthase;
            SM synthase;
            SMS1;
            SMS2
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
SYSNAME     ceramide:phosphatidylcholine cholinephosphotransferase
REACTION    a ceramide + a phosphatidylcholine = a sphingomyelin + a
            1,2-diacyl-sn-glycerol
SUBSTRATE   ceramide [CPD:C00195];
            phosphatidylcholine [CPD:C00157]
PRODUCT     sphingomyelin [CPD:C00550];
            1,2-diacyl-sn-glycerol [CPD:C00641]
COMMENT     The reaction can occur in both directions [3]. This enzyme occupies
            a central position in sphingolipid and glycerophospholipid
            metabolism [4]. Up- and down-regulation of its activity has been
            linked to mitogenic and pro-apoptotic signalling in a variety of
            mammalian cell types [4]. Unlike EC 2.7.8.3, ceramide
            cholinephosphotransferase, CDP-choline cannot replace
            phosphatidylcholine as the donor of the phosphocholine moiety of
            sphingomyelin [2].
REFERENCE   1  [PMID:4817756]
  AUTHORS   Ullman MD, Radin NS.
  TITLE     The enzymatic formation of sphingomyelin from ceramide and lecithin
            in mouse liver.
  JOURNAL   J. Biol. Chem. 249 (1974) 1506-12.
REFERENCE   2  [PMID:7093220]
  AUTHORS   Voelker DR, Kennedy EP.
  TITLE     Cellular and enzymic synthesis of sphingomyelin.
  JOURNAL   Biochemistry. 21 (1982) 2753-9.
REFERENCE   3  [PMID:14685263]
  AUTHORS   Huitema K, van den Dikkenberg J, Brouwers JF, Holthuis JC.
  TITLE     Identification of a family of animal sphingomyelin synthases.
  JOURNAL   EMBO. J. 23 (2004) 33-44.
REFERENCE   4  [PMID:16905542]
  AUTHORS   Tafesse FG, Ternes P, Holthuis JC.
  TITLE     The multigenic sphingomyelin synthase family.
  JOURNAL   J. Biol. Chem. 281 (2006) 29421-5.
REFERENCE   5  [PMID:14976195]
  AUTHORS   Yamaoka S, Miyaji M, Kitano T, Umehara H, Okazaki T.
  TITLE     Expression cloning of a human cDNA restoring sphingomyelin synthesis
            and cell growth in sphingomyelin synthase-defective lymphoid cells.
  JOURNAL   J. Biol. Chem. 279 (2004) 18688-93.
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.8.27
            ExPASy - ENZYME nomenclature database: 2.7.8.27
            ExplorEnz - The Enzyme Database: 2.7.8.27
            ERGO genome analysis and discovery system: 2.7.8.27
            BRENDA, the Enzyme Database: 2.7.8.27
///
ENTRY       EC 2.7.8.-                  Enzyme
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Transferases for other substituted phosphate groups
REACTION    (1) CDP-ethanolamine + N-Acylsphingosine <=> CMP + Ceramide
            phosphoethanolamine [RN:R01503];
            (2) Phosphatidylglycerol + CDP-diacylglycerol <=> Cardiolipin + CMP
            [RN:R02030];
            (3) CMP-2-aminoethylphosphonate + N-Acylsphingosine <=> Ceramide
            2-aminoethylphosphonate + CMP [RN:R04921];
            (4) 2 Phosphatidylglycerol <=> Cardiolipin + Glycerol [RN:R07390];
            (5) UDP-L-Ara4FN + Undecaprenyl phosphate <=> Undecaprenyl phosphate
            alpha-L-Ara4FN + UDP [RN:R07661]
SUBSTRATE   CDP-ethanolamine [CPD:C00570];
            N-Acylsphingosine [CPD:C00195];
            Phosphatidylglycerol [CPD:C00344];
            CDP-diacylglycerol [CPD:C00269];
            CMP-2-aminoethylphosphonate [CPD:C05673]
PRODUCT     CMP [CPD:C00055];
            Ceramide phosphoethanolamine [CPD:C06062];
            Cardiolipin [CPD:C05980];
            Ceramide 2-aminoethylphosphonate [CPD:C05681];
            Glycerol [CPD:C00116]
///
ENTRY       EC 2.7.9.1                  Enzyme
NAME        pyruvate, phosphate dikinase;
            pyruvate, orthophosphate dikinase;
            pyruvate-phosphate dikinase (phosphorylating);
            pyruvate, phosphate dikinase;
            pyruvate-inorganic phosphate dikinase;
            pyruvate-phosphate dikinase;
            pyruvate-phosphate ligase;
            pyruvic-phosphate dikinase;
            pyruvic-phosphate ligase;
            pyruvate, Pi dikinase;
            PPDK
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with paired acceptors
SYSNAME     ATP:pyruvate, phosphate phosphotransferase
REACTION    ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate
            [RN:R00206]
ALL_REAC    R00206
SUBSTRATE   ATP [CPD:C00002];
            pyruvate [CPD:C00022];
            phosphate [CPD:C00009]
PRODUCT     AMP [CPD:C00020];
            phosphoenolpyruvate [CPD:C00074];
            diphosphate [CPD:C00013]
REFERENCE   1  [PMID:4305612]
  AUTHORS   Hatch MD, Slack CR.
  TITLE     A new enzyme for the interconversion of pyruvate and phosphopyruvate
            and its role in the C4 dicarboxylic acid pathway of photosynthesis.
  JOURNAL   Biochem. J. 106 (1968) 141-6.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   2  [PMID:4297474]
  AUTHORS   Reeves RE.
  TITLE     A new enzyme with the glycolytic function of pyruvate kinase.
  JOURNAL   J. Biol. Chem. 243 (1968) 3202-4.
  ORGANISM  Entamoeba histolytica [GN:ehi]
REFERENCE   3  [PMID:5144757]
  AUTHORS   Reeves RE.
  TITLE     Pyruvate,phosphate dikinase from Bacteroides symbiosus.
  JOURNAL   Biochem. J. 125 (1971) 531-9.
  ORGANISM  Bacteroides symbiosus
REFERENCE   4  [PMID:4302788]
  AUTHORS   Reeves RE, Menzies RA, Hsu DS.
  TITLE     The pyruvate-phosphate dikinase reaction. The fate of phosphate and
            the equilibrium.
  JOURNAL   J. Biol. Chem. 243 (1968) 5486-91.
  ORGANISM  Entamoeba histolytica [GN:ehi]
PATHWAY     PATH: map00620  Pyruvate metabolism
            PATH: map00710  Carbon fixation
ORTHOLOGY   KO: K01006  pyruvate,orthophosphate dikinase
GENES       OSA: 4333181 4338750
            TBR: Tb11.02.4150
            TCR: 506297.190 510101.140
            LMA: LmjF11.1000
            EHI: 3.t00080 3.t00082 47.t00016
            PIN: Ping_2762
            MCA: MCA3020(ppdK)
            FTU: FTT0250(ppdK)
            FTF: FTF0250(ppdK)
            FTW: FTW_1867(ppdK)
            FTL: FTL_0132
            FTH: FTH_0123(ppdK)
            FTA: FTA_0143(ppdK)
            FTN: FTN_0064(ppdK)
            BXE: Bxe_B2644
            RFR: Rfer_0088
            MPT: Mpe_B0506 Mpe_B0560
            TBD: Tbd_0368
            GSU: GSU0580(ppdK)
            GME: Gmet_2940
            GUR: Gura_3671
            PCA: Pcar_0600
            PPD: Ppro_0642 Ppro_3511
            BBA: Bd1150(ppdK)
            DPS: DP1368
            ADE: Adeh_4044
            AFW: Anae109_0385
            SFU: Sfum_2063 Sfum_2562
            RPR: RP492
            RTY: RT0478(ppdK)
            RCO: RC0783(ppdK)
            RFE: RF_0735(ppdK)
            RBE: RBE_1205(ppdK)
            RAK: A1C_03635
            RBO: A1I_01250
            RCM: A1E_02910
            RRI: A1G_03835
            OTS: OTBS_0767(ppdK)
            WOL: WD0690(ppdK)
            WBM: Wbm0209
            AMA: AM195(ppdK)
            APH: APH_0185(ppdK)
            ERU: Erum6690(ppdK)
            ERW: ERWE_CDS_07020(ppdK)
            ERG: ERGA_CDS_06940(ppdK)
            ECN: Ecaj_0675
            ECH: ECH_0330(ppdK)
            NSE: NSE_0369(ppdK)
            PUB: SAR11_0618(ppdK)
            MLO: mlr7532
            MES: Meso_0772
            PLA: Plav_0729
            SME: SMc00025(ppdK)
            SMD: Smed_0548
            ATU: Atu0803(ppdK)
            ATC: AGR_C_1470
            RET: RHE_CH01003(ppdK)
            RLE: RL1086(ppdK)
            BME: BMEI1436
            BMF: BAB1_0525(ppdK)
            BMS: BR0500(ppdK)
            BMB: BruAb1_0522(ppdK)
            BOV: BOV_0503(ppdK)
            OAN: Oant_0686
            BJA: blr2538(ppdK)
            BRA: BRADO2034(ppdK) BRADO6353
            BBT: BBta_2338 BBta_2360(ppdK)
            RPA: RPA1051
            RPB: RPB_1099
            RPC: RPC_4343
            RPD: RPD_1224
            RPE: RPE_4405
            NWI: Nwi_2709
            NHA: Nham_3505
            BHE: BH04570(ppdK)
            BQU: BQ03760(ppdK)
            BBK: BARBAKC583_0418(ppdK)
            XAU: Xaut_0494
            CCR: CC_1471
            SIL: SPO1359(ppdK)
            SIT: TM1040_2309
            RSP: RSP_1859(ppdK)
            JAN: Jann_2730
            RDE: RD1_1948(ppdK)
            PDE: Pden_0541
            MMR: Mmar10_2177
            HNE: HNE_0686(ppdK)
            NAR: Saro_2110
            SAL: Sala_1610
            SWI: Swit_4859 Swit_4922
            ELI: ELI_05870(ppdK)
            GBE: GbCGDNIH1_2098
            ACR: Acry_2184
            RRU: Rru_A2956
            MAG: amb2649
            MGM: Mmc1_2194 Mmc1_2398
            ABA: Acid345_1196
            SUS: Acid_7204
            SEP: SE2160
            SER: SERP2170(ppdK)
            SHA: SH0441(ppsA)
            SSP: SSP0180
            LMO: lmo1867
            LMF: LMOf2365_1896(ppdK)
            LIN: lin1981
            LWE: lwe1886(ppdK)
            SPZ: M5005_Spy_1509 M5005_Spy_1510
            SPH: MGAS10270_Spy1577 MGAS10270_Spy1578
            SPI: MGAS10750_Spy1569 MGAS10750_Spy1570
            SPJ: MGAS2096_Spy1537
            SPK: MGAS9429_Spy1511
            SPA: M6_Spy1503
            SPB: M28_Spy1498 M28_Spy1499
            SAG: SAG1670(ppdK)
            SAN: gbs1714
            SAK: SAK_1682(ppdK)
            SSA: SSA_1053
            SGO: SGO_0810(ppdK)
            LSA: LSA1141(ppdK)
            LCA: LSEI_2334
            EFA: EF1024(ppdK)
            STH: STH586
            CPE: CPE2011(podK)
            CPF: CPF_2268(ppdK)
            CPR: CPR_1983(ppdK)
            CTC: CTC02014
            CNO: NT01CX_1167(ppdK)
            CTH: Cthe_1308
            CDF: CD2410(ppdK)
            CBO: CBO2942(ppdK)
            CBA: CLB_2905(ppdK)
            CBH: CLC_2837(ppdK)
            CBF: CLI_2994(ppdK)
            CBE: Cbei_0849
            CKL: CKL_0920(ppdK)
            AMT: Amet_3019
            CHY: CHY_0443(ppdK)
            DRM: Dred_2469
            SWO: Swol_1512
            CSC: Csac_1955
            TTE: TTE0981(ppsA2)
            MTA: Moth_0607
            MTU: Rv1127c(ppdK)
            MTC: MT1159
            MBO: Mb1158c(ppdK)
            MBB: BCG_1188c(ppdK)
            MLE: ML0955(ppdK)
            MPA: MAP2664(ppdK)
            MAV: MAV_5059
            SCO: SCO0208(SCJ12.20) SCO2494(SC7A8.33c)
            SMA: SAV5654(ppdK)
            PAC: PPA2048
            NCA: Noca_0987
            TFU: Tfu_0863
            FRA: Francci3_1276
            ACE: Acel_0801
            STP: Strop_3429
            FNU: FN0796
            RBA: RB1998(ppdK)
            TPA: TP0746
            TDE: TDE0844 TDE1501(ppdK)
            BTH: BT_0644
            BFR: BF2538
            BFS: BF2567(ppdK)
            PGI: PG1017(ppdK)
            CTE: CT1682(ppd)
            CCH: Cag_0155
            CPH: Cpha266_0518
            PLT: Plut_1661
            RRS: RoseRS_1064
            RCA: Rcas_2482
            TTH: TTC0304
            TTJ: TTHA0663
            TMA: TM0272
            TPT: Tpet_0652
            TME: Tmel_0158
            FNO: Fnod_0607
            MAC: MA0608(ppdK)
            MBA: Mbar_A1396
            MMA: MM_1770
            MBU: Mbur_0966
            MHU: Mhun_1141
            TAC: Ta0886
            TVO: TVN0976
            PAI: PAE3383
            PCL: Pcal_0162
            PAS: Pars_1008
STRUCTURES  PDB: 1DIK  1GGO  1H6Z  1JDE  1KBL  1KC7  1VBG  1VBH  2DIK  2FM4  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.9.1
            ExPASy - ENZYME nomenclature database: 2.7.9.1
            ExplorEnz - The Enzyme Database: 2.7.9.1
            ERGO genome analysis and discovery system: 2.7.9.1
            BRENDA, the Enzyme Database: 2.7.9.1
            CAS: 9027-40-1
///
ENTRY       EC 2.7.9.2                  Enzyme
NAME        pyruvate, water dikinase;
            phosphoenolpyruvate synthase;
            pyruvate-water dikinase (phosphorylating);
            PEP synthetase;
            phosphoenolpyruvate synthase;
            phoephoenolpyruvate synthetase;
            phosphoenolpyruvic synthase;
            phosphopyruvate synthetase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with paired acceptors
SYSNAME     ATP:pyruvate, water phosphotransferase
REACTION    ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
            [RN:R00199]
ALL_REAC    R00199
SUBSTRATE   ATP [CPD:C00002];
            pyruvate [CPD:C00022];
            H2O [CPD:C00001]
PRODUCT     AMP [CPD:C00020];
            phosphoenolpyruvate [CPD:C00074];
            phosphate [CPD:C00009]
COFACTOR    Manganese [CPD:C00034]
COMMENT     A manganese protein.
REFERENCE   1  [PMID:4319237]
  AUTHORS   Berman KM, Cohn M.
  TITLE     Phosphoenolpyruvate synthetase of Escherichia coli. Purification,
            some properties, and the role of divalent metal ions.
  JOURNAL   J. Biol. Chem. 245 (1970) 5309-18.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4319238]
  AUTHORS   Berman KM, Cohn M.
  TITLE     Phosphoenolpyruvate synthetase. Partial reactions studied with
            adenosine triphosphate analogues and the inorganic phosphate-H2 18O
            exchange reaction.
  JOURNAL   J. Biol. Chem. 245 (1970) 5319-25.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:5322808]
  AUTHORS   Cooper RA, Kornberg HL.
  TITLE     Net formation of phosphoenolpyruvate from pyruvate by Escherichia
            coli.
  JOURNAL   Biochim. Biophys. Acta. 104 (1965) 618-20.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4
  AUTHORS   Cooper, R.A. and Kornberg, H.L.
  TITLE     Phosphoenolpyruvate synthetase.
  JOURNAL   Methods Enzymol. 13 (1969) 309-314.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00620  Pyruvate metabolism
            PATH: map00720  Reductive carboxylate cycle (CO2 fixation)
ORTHOLOGY   KO: K01007  pyruvate,water dikinase
GENES       CEL: T21C9.6
            CME: CMF012C
            ANI: AN5843.2
            AFM: AFUA_5G14790
            ECO: b1702(pps)
            ECJ: JW1692(pps)
            ECE: Z2731(ppsA)
            ECS: ECs2409
            ECC: c2098(ppsA)
            ECI: UTI89_C1895(ppsA)
            ECP: ECP_1649
            ECW: EcE24377A_1919(ppsA)
            ECX: EcHS_A1781
            STY: STY1761(ppsA)
            STT: t1230(ppsA)
            SPT: SPA1494(ppsA)
            SEC: SC1368(pps)
            STM: STM1349(pps)
            YPE: YPO2409(ppsA)
            YPK: y1930(ppsA)
            YPM: YP_2196(ppsA)
            YPA: YPA_1753
            YPN: YPN_1863
            YPS: YPTB2318(ppsA)
            YPI: YpsIP31758_1737(ppsA)
            SFL: SF1528(ppsA)
            SFX: S1646(ppsA)
            SFV: SFV_1522(ppsA)
            SSN: SSON_1457(ppsA)
            SBO: SBO_1427(ppsA)
            SDY: SDY_1794(ppsA)
            ECA: ECA1853(ppsA)
            PLU: plu2628(ppsA)
            SGL: SG1429
            XFA: XF1259
            XFT: PD0524(ppsA)
            XCC: XCC2166(ppsA)
            XCB: XC_1952
            XCV: XCV2202(ppsA)
            XAC: XAC2041(ppsA)
            XOO: XOO2211(ppsA)
            XOM: XOO_2079(XOO2079)
            VCH: VCA0987
            VCO: VC0395_0251(ppsA)
            VVU: VV2_0005
            VVY: VVA0514
            VPA: VPA0372
            VFI: VF1242
            PPR: PBPRA1751
            PAE: PA1770(ppsA)
            PAU: PA14_41670(ppsA)
            PAP: PSPA7_3536(ppsA)
            PPU: PP_2082(ppsA)
            PPF: Pput_3658
            PST: PSPTO_2292(ppsA)
            PSB: Psyr_2090
            PSP: PSPPH_2061(ppsA)
            PFL: PFL_1869(ppsA)
            PFO: Pfl_1770
            PEN: PSEEN1742(ppsA)
            PMY: Pmen_2085
            PAR: Psyc_1335(ppsA)
            PCR: Pcryo_1034
            PRW: PsycPRwf_0949
            ACI: ACIAD2423(ppsA)
            ACB: A1S_2164
            SON: SO_2644(ppsA)
            SDN: Sden_2009
            SFR: Sfri_2297
            SAZ: Sama_2072
            SBL: Sbal_2488
            SBM: Shew185_2481
            SLO: Shew_1549
            SPC: Sputcn32_2243
            SSE: Ssed_1871
            SHE: Shewmr4_1592
            SHN: Shewana3_1736
            SHW: Sputw3181_1765
            ILO: IL1316(ppsA)
            CPS: CPS_3011(ppsA)
            PHA: PSHAb0557(ppsA)
            PAT: Patl_1744
            MAQ: Maqu_1883
            LPN: lpg0805
            LPF: lpl0838(ppsA)
            LPP: lpp0867(ppsA)
            TCX: Tcr_1186
            NOC: Noc_1446
            AEH: Mlg_1890
            HHA: Hhal_0220
            HCH: HCH_02123(ppsA) HCH_06026
            CSA: Csal_2062
            ABO: ABO_1427(ppsA)
            MMW: Mmwyl1_1405
            AHA: AHA_2691(ppsA)
            DNO: DNO_0630(ppsA)
            NME: NMB0618
            NMA: NMA0826(ppsA)
            NMC: NMC0561(ppsA)
            NGO: NGO0200
            CVI: CV_3709(ppsA)
            RSO: RSc1421(ppsA)
            REU: Reut_A1162 Reut_A1864
            REH: H16_A2038(ppsA)
            RME: Rmet_1453
            BMA: BMA1535(ppsA)
            BMV: BMASAVP1_A2035(ppsA)
            BML: BMA10299_A3277(ppsA)
            BMN: BMA10247_1306(ppsA)
            BXE: Bxe_A1699
            BVI: Bcep1808_1908
            BUR: Bcep18194_A5312
            BCN: Bcen_6075
            BCH: Bcen2424_2002
            BAM: Bamb_2035
            BPS: BPSL2140(ppsA)
            BPM: BURPS1710b_2561(ppsA)
            BPL: BURPS1106A_2470(ppsA)
            BPD: BURPS668_2415(ppsA)
            BTE: BTH_I2046(ppsA)
            BPE: BP1436(ppsA)
            BPA: BPP1544(ppsA)
            BBR: BB2622(ppsA)
            RFR: Rfer_2191
            POL: Bpro_2757 Bpro_3042
            PNA: Pnap_2081
            AAV: Aave_1382
            AJS: Ajs_2879
            MPT: Mpe_A1521
            HAR: HEAR1352(pps)
            MMS: mma_2041
            NEU: NE2359(ppsA) NE2366(ppsA)
            NET: Neut_0868
            NMU: Nmul_A0998 Nmul_A1613
            EBA: ebA5781(ppsA) ebA5830(pps)
            AZO: azo2167(ppsA1) azo2486(ppsA2)
            DAR: Daro_1768
            TBD: Tbd_0618
            MFA: Mfla_2203
            HPY: HP0121
            HPJ: jhp0111(ppsA)
            HPA: HPAG1_0120
            HHE: HH1824(ppsA)
            HAC: Hac_1459(ppsA)
            WSU: WS0826
            NIS: NIS_0923(ppsA)
            SUN: SUN_1214(ppsA)
            GSU: GSU0803(ppsA)
            GME: Gmet_0770
            PCA: Pcar_2435
            DVU: DVU1833
            DVL: Dvul_0151 Dvul_0174 Dvul_0567 Dvul_2815
            DDE: Dde_0604 Dde_2080
            LIP: LI0025(ppsA)
            BBA: Bd3153(ppsA)
            MXA: MXAN_6800(ppsA)
            SAT: SYN_01243 SYN_02383 SYN_02966
            SFU: Sfum_0630 Sfum_0634 Sfum_0649 Sfum_2666
            AMA: AM195(ppdK)
            BJA: blr4655(ppsA)
            BRA: BRADO1573(pps)
            BBT: BBta_1604 BBta_1605 BBta_6481(pps)
            BSU: BG12657(pps)
            BAN: BA3116(ppsA)
            BAR: GBAA3116(ppsA)
            BAA: BA_3618
            BAT: BAS2899
            BCE: BC3087
            BCA: BCE_3137(ppsA)
            BCZ: BCZK2825(ppsA)
            BTK: BT9727_2868(ppsA)
            BTL: BALH_2779(ppsA) BALH_2780
            BLI: BL01065 BL01998(ppsI) BL05212(ppsII)
            BLD: BLi00634 BLi02172(pps) BLi02241
            BAY: RBAM_017370
            BPU: BPUM_3151
            LMO: lmo0411
            LMF: LMOf2365_0430
            LIN: lin0432
            SSA: SSA_1012 SSA_1016
            SGO: SGO_0936 SGO_0940(ppsA)
            LPL: lp_1912(pps)
            CAC: CAC0534(pps)
            CKL: CKL_0066(ppsA)
            DSY: DSY2123(pps) DSY3072 DSY3080(pps) DSY3730(pps) DSY4219(pps)
                 DSY4274
            DRM: Dred_2466
            MSM: MSMEG_3934
            MVA: Mvan_1818 Mvan_2632
            MGI: Mflv_0493 Mflv_4990
            MMC: Mmcs_3406
            CGL: NCgl0528(cgl0551)
            CGB: cg0642
            CEF: CE0560
            SCO: SCO5896(redH)
            ART: Arth_0384 Arth_0474 Arth_1972 Arth_1995 Arth_2857
            AAU: AAur_1894(ppsA)
            NCA: Noca_1185
            FRA: Francci3_2689
            KRA: Krad_2434
            SEN: SACE_0388 SACE_2459 SACE_2483 SACE_7324(ppsII)
            RXY: Rxyl_1574 Rxyl_3073
            TDE: TDE0349
            SYN: slr0301(ppsA)
            SYC: syc0756_d(ppsA)
            SYF: Synpcc7942_0781
            CYA: CYA_0741(ppsA)
            CYB: CYB_1115(ppsA)
            TEL: tll0583 tlr0765
            GVI: gll1985 glr2690
            ANA: all0635 all2509 alr3146 alr3147 alr3397
            AVA: Ava_0441 Ava_1694 Ava_3388 Ava_3841 Ava_4569
            TER: Tery_0910 Tery_4209
            SRU: SRU_1138(ppsA)
            CHU: CHU_2293
            DET: DET0554(ppsA)
            DEH: cbdb_A529(ppsA)
            DRA: DR_1727
            DGE: Dgeo_0621
            TTH: TTC1136
            TTJ: TTHA1500
            AAE: aq_2142(ppsA)
            MMP: MMP1094(ppsA)
            MMQ: MmarC5_0490
            MAC: MA2458(ppsA) MA2667(ppsA) MA3408(ppsA)
            MBA: Mbar_A2223 Mbar_A3094 Mbar_A3264
            MMA: MM_2723
            MBU: Mbur_0799
            MTP: Mthe_1637
            MHU: Mhun_2610
            MEM: Memar_1849
            MBN: Mboo_0034 Mboo_2165
            MST: Msp_0328(ppsA)
            MSI: Msm_0988
            MKA: MK0252(ppsA)
            HAL: VNG0330G(ppsA)
            HMA: rrnAC1795(ppsA)
            HWA: HQ1570A(ppsA1) HQ2024A(ppsA2)
            NPH: NP1196A(ppsA)
            PTO: PTO1519
            PHO: PH0092
            PAB: PAB0057(ppsA)
            PFU: PF0043
            TKO: TK1292
            RCI: RCIX1188(ppsA-1) RCIX1540(ppsA-2)
            APE: APE_0026 APE_0028 APE_0650.1
            SMR: Smar_0141
            SSO: SSO0883(ppsA-1)
            STO: ST1235
            SAI: Saci_1417
            MSE: Msed_0431
            PAI: PAE2423
            PIS: Pisl_1888
            PCL: Pcal_0313
            PAS: Pars_0510 Pars_1445
            TPE: Tpen_0588
STRUCTURES  PDB: 2OLS  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.9.2
            ExPASy - ENZYME nomenclature database: 2.7.9.2
            ExplorEnz - The Enzyme Database: 2.7.9.2
            ERGO genome analysis and discovery system: 2.7.9.2
            BRENDA, the Enzyme Database: 2.7.9.2
            CAS: 9013-09-6
///
ENTRY       EC 2.7.9.3                  Enzyme
NAME        selenide, water dikinase;
            selenophosphate synthase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with paired acceptors
SYSNAME     ATP:selenide, water phosphotransferase
REACTION    ATP + selenide + H2O = AMP + selenophosphate + phosphate [RN:R03595]
ALL_REAC    R03595
SUBSTRATE   ATP [CPD:C00002];
            selenide [CPD:C01528];
            H2O [CPD:C00001]
PRODUCT     AMP [CPD:C00020];
            selenophosphate [CPD:C05172];
            phosphate [CPD:C00009]
COMMENT     Mg2+-dependent enzyme identified in Escherichia coli
REFERENCE   1  [PMID:1557403]
  AUTHORS   Veres Z, Tsai L, Scholz TD, Politino M, Balaban RS, Stadtman TC.
  TITLE     Synthesis of 5-methylaminomethyl-2-selenouridine in tRNAs: 31P NMR
            studies show the labile selenium donor synthesized by the selD gene
            product contains selenium bonded to phosphorus.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 2975-9.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00450  Selenoamino acid metabolism
ORTHOLOGY   KO: K01008  selenide,water dikinase
GENES       HSA: 22928(SEPHS2) 22929(SEPHS1)
            MMU: 109079(Sephs1) 20768(Sephs2)
            CFA: 477999(SEPHS1) 489904(SEPHS2)
            GGA: 426612(SEPHS1)
            XLA: 379650(MGC68922)
            XTR: 448749(sephs1)
            DRE: 324947(sephs1)
            DME: Dmel_CG5025(Sps2) Dmel_CG8553(SelD)
            CEL: Y45F10A.4
            CME: CMP189C
            DDI: DDB_0214887(selD)
            PFA: PFI0505c
            TET: TTHERM_00522580
            TBR: Tb10.6k15.0990
            TCR: 504079.6 508717.36
            LMA: LmjF36.5410
            ECO: b1764(selD)
            ECJ: JW1753(selD)
            ECE: Z2797(selD)
            ECS: ECs2470
            ECC: c2167(selD)
            ECI: UTI89_C1959(selD)
            ECP: ECP_1712
            ECW: EcE24377A_1987(selD)
            ECX: EcHS_A1848(selD)
            STY: STY1817(selD)
            STT: t1176(selD)
            SPT: SPA1547(selD)
            SEC: SC1319(selD)
            STM: STM1297(selD)
            YPE: YPO2164(selD)
            YPK: y2157(selD)
            YPM: YP_1964(selD)
            YPA: YPA_1521
            YPN: YPN_1630
            YPS: YPTB2090(selD)
            YPI: YpsIP31758_1980(selD)
            SFL: SF1459(selD)
            SFX: S1574(selD)
            SFV: SFV_1453(selD)
            SSN: SSON_1391(selD)
            SBO: SBO_1323(selD)
            SDY: SDY_1509(selD)
            PLU: plu2551(selD)
            SPE: Spro_2720
            HIT: NTHI0297(selD)
            HDU: HD0577(selD)
            PMU: PM0790(selD)
            MSU: MS1241(selD)
            APL: APL_0327(selD)
            PPR: PBPRA2592 PBPRB1545
            PAE: PA1642(selD)
            PAU: PA14_43280(selD)
            PAP: PSPA7_3631(selD)
            PPU: PP_0823(selD)
            PPF: Pput_0850
            PST: PSPTO_0793(selD)
            PSB: Psyr_0696
            PFL: PFL_2278(selD)
            PFO: Pfl_3755
            PEN: PSEEN0991(selD)
            SON: SO_0196(selD)
            SDN: Sden_0228
            SFR: Sfri_0120
            SBL: Sbal_4182
            SBM: Shew185_0173
            SPC: Sputcn32_3543
            SPL: Spea_0161
            SHE: Shewmr4_0175
            SHM: Shewmr7_0170
            SHN: Shewana3_0176
            SHW: Sputw3181_3680
            CPS: CPS_0768(selD)
            TCX: Tcr_1022
            HCH: HCH_00239(selD)
            CSA: Csal_0511
            AHA: AHA_2224(selD)
            REU: Reut_A0300
            REH: H16_B0295(selD)
            RME: Rmet_3860
            BMA: BMAA1473(selD)
            BML: BMA10299_2135(selD)
            BMN: BMA10247_A0819(selD)
            BXE: Bxe_B2555
            BUR: Bcep18194_B0287
            BCN: Bcen_3008
            BCH: Bcen2424_5358
            BPS: BPSS0287(selD)
            BPM: BURPS1710b_A1832(selD)
            BPL: BURPS1106A_A0405(selD)
            BPD: BURPS668_A0503(selD)
            BTE: BTH_II2116(selD)
            BBR: BB4738(selD)
            RFR: Rfer_1613 Rfer_2844
            POL: Bpro_1754
            VEI: Veis_1621
            MPT: Mpe_A2198
            HAR: HEAR0828(selD)
            MMS: mma_1199(selD)
            NEU: NE0733(selD)
            NET: Neut_1654
            EBA: ebA6817(selD)
            AZO: azo1665
            DAR: Daro_1054
            TBD: Tbd_1021
            HHE: HH1734(selD)
            WSU: WS0997(selD1)
            TDN: Tmden_0830 Tmden_1162
            CJE: Cj1504c(selD)
            CJR: CJE1677(selD)
            CJJ: CJJ81176_1496(selD)
            CJU: C8J_1407(selD)
            CFF: CFF8240_0340(selD)
            CHA: CHAB381_1778(selD)
            CCO: CCC13826_2135(selD)
            ABU: Abu_1513(selD)
            SUN: SUN_1829(selD)
            GSU: GSU0607(selD)
            GME: Gmet_2907
            GUR: Gura_3849
            PCA: Pcar_0822
            DVU: DVU1332(selD)
            DDE: Dde_2225
            BBA: Bd2571(selD)
            DPS: DP0969
            ADE: Adeh_3363
            MXA: MXAN_2002(selD)
            SAT: SYN_02118
            SFU: Sfum_3401
            SME: SMa0028(selD)
            SIL: SPO2899
            SIT: TM1040_1544
            RSP: RSP_3716(selD)
            MMR: Mmar10_1925
            HNE: HNE_2490
            MGM: Mmc1_2385
            ABA: Acid345_0099
            SUS: Acid_4725
            EFA: EF2567(selD)
            STH: STH2590
            CPE: CPE2118(selD)
            CPF: CPF_2374(selD)
            CPR: CPR_2086(selD)
            CDF: CD2496(selD)
            CBO: CBO2977(selD)
            CBA: CLB_3002(selD)
            CBH: CLC_2874(selD)
            CBF: CLI_3031(selD)
            CHY: CHY_2058(selD)
            DSY: DSY4694
            DRM: Dred_1241
            SWO: Swol_2542
            TTE: TTE1873(selD)
            MTA: Moth_1625
            MPA: MAP0366(selD)
            MAV: MAV_0420(selD)
            MSM: MSMEG_1852(selD)
            MMC: Mmcs_5214
            KRA: Krad_1607
            SEN: SACE_3560(selD)
            STP: Strop_0583
            RXY: Rxyl_1061
            TDE: TDE2461(selD)
            SYW: SYNW0190
            SYD: Syncc9605_0186
            SYE: Syncc9902_0214
            SYG: sync_0230
            CYA: CYA_0055(selD)
            CYB: CYB_1184(selD)
            PMA: Pro0333(ndh)
            PMM: PMM0302(selD)
            PMT: PMT1909(selD)
            PMN: PMN2A_1667
            PMI: PMT9312_0304
            PMB: A9601_03251
            PMC: P9515_03351
            PMF: P9303_25471
            PMG: P9301_03261
            PME: NATL1_03811
            TER: Tery_4785
            PGI: PG1753(selD)
            AAE: aq_1030(selD)
            MMP: MMP0904(selD)
            MKA: MK1369(selD)
            HMA: pNG7239(selD)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.9.3
            ExPASy - ENZYME nomenclature database: 2.7.9.3
            ExplorEnz - The Enzyme Database: 2.7.9.3
            ERGO genome analysis and discovery system: 2.7.9.3
            UM-BBD (Biocatalysis/Biodegradation Database): 2.7.9.3
            BRENDA, the Enzyme Database: 2.7.9.3
///
ENTRY       EC 2.7.9.4                  Enzyme
NAME        alpha-glucan, water dikinase;
            starch-related R1 protein, GWD
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with paired acceptors
SYSNAME     ATP:alpha-glucan, water phosphotransferase
REACTION    ATP + alpha-glucan + H2O = AMP + phospho-alpha-glucan + phosphate
SUBSTRATE   ATP [CPD:C00002];
            alpha-glucan;
            H2O [CPD:C00001]
PRODUCT     AMP [CPD:C00020];
            phospho-alpha-glucan;
            phosphate [CPD:C00009]
COMMENT     Requires Mg2+. ATP appears to be the only phosphate donor. No
            activity could be detected using GTP, UTP, phosphoenolpyruvate or
            diphosphate [1]. The protein phosphorylates glucans exclusively on
            O-6 of glucosyl residues [2]. The protein phosphorylates itself with
            the beta-phosphate of ATP, which is then transferred to the glucan
            [1].
REFERENCE   1  [PMID:12011472]
  AUTHORS   Ritte G, Lloyd JR, Eckermann N, Rottmann A, Kossmann J, Steup M.
  TITLE     The starch-related R1 protein is an alpha -glucan, water dikinase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 7166-71.
  ORGANISM  Solanum tuberosum [GN:estu]
REFERENCE   2  [PMID:16914145]
  AUTHORS   Ritte G, Heydenreich M, Mahlow S, Haebel S, Kotting O, Steup M.
  TITLE     Phosphorylation of C6- and C3-positions of glucosyl residues in
            starch is catalysed by distinct dikinases.
  JOURNAL   FEBS. Lett. 580 (2006) 4872-6.
  ORGANISM  Arabidopsis thaliana [GN:ath]
ORTHOLOGY   KO: K08244  alpha-glucan, water dikinase
GENES       ATH: AT1G10760(SEX1)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.9.4
            ExPASy - ENZYME nomenclature database: 2.7.9.4
            ExplorEnz - The Enzyme Database: 2.7.9.4
            ERGO genome analysis and discovery system: 2.7.9.4
            BRENDA, the Enzyme Database: 2.7.9.4
            CAS: 664327-94-0
///
ENTRY       EC 2.7.9.5                  Enzyme
NAME        phosphoglucan, water dikinase;
            PWD;
            OK1
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Phosphotransferases with paired acceptors
SYSNAME     ATP:phospho-alpha-glucan, water phosphotransferase
REACTION    ATP + [phospho-alpha-glucan] + H2O = AMP +
            O-phospho-[phospho-alpha-glucan] + phosphate
SUBSTRATE   ATP [CPD:C00002];
            [phospho-alpha-glucan];
            H2O [CPD:C00001]
PRODUCT     AMP [CPD:C00020];
            O-phospho-[phospho-alpha-glucan];
            phosphate [CPD:C00009]
COMMENT     The enzyme phosphorylates granular starch that has previously been
            phosphorylated by EC 2.7.9.4, alpha-glucan, water dikinase; there is
            no activity with unphosphorylated glucans. It transfers the
            beta-phosphate of ATP to the phosphoglucan, whereas the
            gamma-phosphate is transferred to water [1]. In contrast to EC
            2.7.9.4, which phosphorylates glucose groups in glucans on O-6, this
            enzyme phosphorylates glucose groups in phosphorylated starch on O-3
            [2]. The protein phosphorylates itself with the beta-phosphate of
            ATP, which is then transferred to the glucan [1].
REFERENCE   1  [PMID:15618411]
  AUTHORS   Kotting O, Pusch K, Tiessen A, Geigenberger P, Steup M, Ritte G.
  TITLE     Identification of a novel enzyme required for starch metabolism in
            Arabidopsis leaves. The phosphoglucan, water dikinase.
  JOURNAL   Plant. Physiol. 137 (2005) 242-52.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   2  [PMID:16914145]
  AUTHORS   Ritte G, Heydenreich M, Mahlow S, Haebel S, Kotting O, Steup M.
  TITLE     Phosphorylation of C6- and C3-positions of glucosyl residues in
            starch is catalysed by distinct dikinases.
  JOURNAL   FEBS. Lett. 580 (2006) 4872-6.
  ORGANISM  Arabidopsis thaliana [GN:ath]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.9.5
            ExPASy - ENZYME nomenclature database: 2.7.9.5
            ExplorEnz - The Enzyme Database: 2.7.9.5
            ERGO genome analysis and discovery system: 2.7.9.5
            BRENDA, the Enzyme Database: 2.7.9.5
            CAS: 912567-76-1
///
ENTRY       EC 2.7.10.1                 Enzyme
NAME        receptor protein-tyrosine kinase;
            AATK;
            AATYK;
            AATYK2;
            AATYK3;
            ACH;
            ALK;
            anaplastic lymphoma kinase;
            ARK;
            ATP:protein-tyrosine O-phosphotransferase (ambiguous);
            AXL;
            Bek;
            Bfgfr;
            BRT;
            Bsk;
            C-FMS;
            CAK;
            CCK4;
            CD115;
            CD135;
            CDw135;
            Cek1;
            Cek10;
            Cek11;
            Cek2;
            Cek3;
            Cek5;
            Cek6;
            Cek7;
            CFD1;
            CKIT;
            CSF1R;
            DAlk;
            DDR1;
            DDR2;
            Dek;
            DKFZp434C1418;
            Drosophila Eph kinase;
            DRT;
            DTK;
            Ebk;
            ECK;
            EDDR1;
            Eek;
            EGFR;
            Ehk2;
            Ehk3;
            Elk;
            EPH;
            EPHA1;
            EPHA2;
            EPHA6;
            EPHA7;
            EPHA8;
            EPHB1;
            EPHB2;
            EPHB3;
            EPHB4;
            EphB5;
            ephrin-B3 receptor tyrosine kinase;
            EPHT;
            EPHT2;
            EPHT3;
            EPHX;
            ERBB;
            ERBB1;
            ERBB2;
            ERBB3;
            ERBB4;
            ERK;
            Eyk;
            FGFR1;
            FGFR2;
            FGFR3;
            FGFR4;
            FLG;
            FLK1;
            FLK2;
            FLT1;
            FLT2;
            FLT3;
            FLT4;
            FMS;
            Fv2;
            HBGFR;
            HEK11;
            HEK2;
            HEK3;
            HEK5;
            HEK6;
            HEP;
            HER2;
            HER3;
            HER4;
            HGFR;
            HSCR1;
            HTK;
            IGF1R;
            INSR;
            INSRR;
            insulin receptor protein-tyrosine kinase;
            IR;
            IRR;
            JTK12;
            JTK13;
            JTK14;
            JWS;
            K-SAM;
            KDR;
            KGFR;
            KIA0641;
            KIAA1079;
            KIAA1459;
            Kil;
            Kin15;
            Kin16;
            KIT;
            KLG;
            LTK;
            MCF3;
            Mdk1;
            Mdk2;
            Mdk5;
            MEhk1;
            MEN2A/B;
            Mep;
            MER;
            MERTK;
            MET;
            Mlk1;
            Mlk2;
            Mrk;
            MST1R;
            MTC1;
            MUSK;
            Myk1;
            N-SAM;
            NEP;
            NET;
            Neu;
            neurite outgrowth regulating kinase;
            NGL;
            NOK;
            nork;
            novel oncogene with kinase-domain;
            Nsk2;
            NTRK1;
            NTRK2;
            NTRK3;
            NTRK4;
            NTRKR1;
            NTRKR2;
            NTRKR3;
            Nuk;
            NYK;
            PCL;
            PDGFR;
            PDGFRA;
            PDGFRB;
            PHB6;
            protein-tyrosine kinase (ambiguous);
            protein tyrosine kinase (ambiguous);
            PTK;
            PTK3;
            PTK7;
            receptor protein tyrosine kinase;
            RET;
            RON;
            ROR1;
            ROR2;
            ROS1;
            RSE;
            RTK;
            RYK;
            SEA;
            Sek2;
            Sek3;
            Sek4;
            Sfr;
            SKY;
            STK;
            STK1;
            TEK;
            TIE;
            TIE1;
            TIE2;
            TIF;
            TKT;
            TRK;
            TRKA;
            TRKB;
            TRKC;
            TRKE;
            TYK1;
            TYRO10;
            Tyro11;
            TYRO3;
            Tyro5;
            Tyro6;
            TYRO7;
            UFO;
            VEGFR1;
            VEGFR2;
            VEGFR3;
            Vik;
            YK1;
            Yrk
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-tyrosine kinases
SYSNAME     ATP:[protein]-L-tyrosine O-phosphotransferase (receptor-type)
REACTION    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine
            phosphate [RN:R02584]
ALL_REAC    R02584
SUBSTRATE   ATP [CPD:C00002];
            [protein]-L-tyrosine [CPD:C00585]
PRODUCT     ADP [CPD:C00008];
            [protein]-L-tyrosine phosphate [CPD:C01167]
COMMENT     The receptor protein-tyrosine kinases, which can be defined as
            having a transmembrane domain, are a large and diverse multigene
            family found only in Metazoans [1]. In the human genome, 58
            receptor-type protein-tyrosine kinases have been identified and
            these are distributed into 20 subfamilies.
REFERENCE   1  [PMID:11114734]
  AUTHORS   Robinson DR, Wu YM, Lin SF.
  TITLE     The protein tyrosine kinase family of the human genome.
  JOURNAL   Oncogene. 19 (2000) 5548-57.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:9053841]
  AUTHORS   Iwahara T, Fujimoto J, Wen D, Cupples R, Bucay N, Arakawa T, Mori S,
            Ratzkin B, Yamamoto T.
  TITLE     Molecular characterization of ALK, a receptor tyrosine kinase
            expressed specifically in the nervous system.
  JOURNAL   Oncogene. 14 (1997) 439-49.
  ORGANISM  human [GN:hsa], mouse [GN:mmu]
REFERENCE   3  [PMID:11442633]
  AUTHORS   Loren CE, Scully A, Grabbe C, Edeen PT, Thomas J, McKeown M, Hunter
            T, Palmer RH.
  TITLE     Identification and characterization of DAlk: a novel Drosophila
            melanogaster RTK which drives ERK activation in vivo.
  JOURNAL   Genes. Cells. 6 (2001) 531-44.
  ORGANISM  Drosophila melanogaster [GN:dme]
PATHWAY     PATH: map04010  MAPK signaling pathway
            PATH: map04012  ErbB signaling pathway
            PATH: map04020  Calcium signaling pathway
            PATH: map04060  Cytokine-cytokine receptor interaction
            PATH: map04210  Apoptosis
            PATH: map04320  Dorso-ventral axis formation
            PATH: map04360  Axon guidance
            PATH: map04370  VEGF signaling pathway
            PATH: map04510  Focal adhesion
            PATH: map04520  Adherens junction
            PATH: map04540  Gap junction
            PATH: map04640  Hematopoietic cell lineage
            PATH: map04730  Long-term depression
            PATH: map04810  Regulation of actin cytoskeleton
            PATH: map04910  Insulin signaling pathway
            PATH: map04912  GnRH signaling pathway
            PATH: map04914  Progesterone-mediated oocyte maturation
            PATH: map04916  Melanogenesis
            PATH: map04930  Type II diabetes mellitus
            PATH: map05050  Dentatorubropallidoluysian atrophy (DRPLA)
            PATH: map05120  Epithelial cell signaling in Helicobacter pylori
                            infection
            PATH: map05210  Colorectal cancer
            PATH: map05211  Renal cell carcinoma
            PATH: map05212  Pancreatic cancer
            PATH: map05213  Endometrial cancer
            PATH: map05214  Glioma
            PATH: map05215  Prostate cancer
            PATH: map05216  Thyroid cancer
            PATH: map05218  Melanoma
            PATH: map05219  Bladder cancer
            PATH: map05221  Acute myeloid leukemia
            PATH: map05223  Non-small cell lung cancer
ORTHOLOGY   KO: K03176  neurotrophic tyrosine kinase, receptor, type 1
            KO: K04360  neurotrophic tyrosine kinase, receptor, type 2
            KO: K04361  epidermal growth factor receptor
            KO: K04362  fibroblast growth factor receptor 1
            KO: K04363  platelet-derived growth factor receptor, alpha
                        polypeptide
            KO: K04527  insulin receptor
            KO: K05083  receptor tyrosine-protein kinase erbB-2
            KO: K05084  receptor tyrosine-protein kinase erbB-3
            KO: K05085  receptor tyrosine-protein kinase erbB-4
            KO: K05086  insulin receptor-related receptor
            KO: K05087  insulin-like growth factor 1 receptor
            KO: K05088  proto-oncogene tyrosine-protein kinase ROS
            KO: K05089  platelet-derived growth factor receptor, beta
                        polypeptide
            KO: K05090  colony-stimulating factor 1 receptor (macrophage)
            KO: K05091  proto-oncogene tyrosine-protein kinase Kit
            KO: K05092  fms-related tyrosine kinase 3
            KO: K05093  fibroblast growth factor receptor 2
            KO: K05094  fibroblast growth factor receptor 3
            KO: K05095  fibroblast growth factor receptor 4
            KO: K05096  FMS-like tyrosine kinase 1
            KO: K05097  FMS-like tyrosine kinase 4
            KO: K05098  kinase insert domain protein receptor
            KO: K05099  proto-oncogene tyrosine-protein kinase Met
            KO: K05100  macrophage-stimulating 1 receptor
            KO: K05101  neurotrophic tyrosine kinase, receptor, type 3
            KO: K05102  Eph receptor A1
            KO: K05103  Eph receptor A2
            KO: K05104  Eph receptor A3
            KO: K05105  Eph receptor A4
            KO: K05106  Eph receptor A5
            KO: K05107  Eph receptor A6
            KO: K05108  EphA7
            KO: K05109  Eph receptor A8
            KO: K05110  Eph receptor B1
            KO: K05111  Eph receptor B2
            KO: K05112  Eph receptor B3
            KO: K05113  Eph receptor B4
            KO: K05114  Eph receptor B6
            KO: K05115  AXL receptor tyrosine kinase
            KO: K05116  TYRO3 protein tyrosine kinase 3
            KO: K05117  c-mer proto-oncogene tyrosine kinase
            KO: K05118  leukocyte tyrosine kinase
            KO: K05119  anaplastic lymphoma kinase
            KO: K05120  tyrosine kinase receptor 1
            KO: K05121  endothelial-specific receptor tyrosine kinase
            KO: K05122  receptor tyrosine kinase-like orphan receptor 1
            KO: K05123  receptor tyrosine kinase-like orphan receptor 2
            KO: K05124  discoidin domain receptor family, member 1
            KO: K05125  discoidin domain receptor family, member 2
            KO: K05126  proto-oncogene tyrosine-protein kinase Ret
            KO: K05127  PTK7 protein tyrosine kinase 7
            KO: K05128  RYK receptor-like tyrosine kinase
            KO: K05129  muscle, skeletal, receptor tyrosine kinase
            KO: K08252  receptor protein-tyrosine kinase
            KO: K08885  tyrosine kinase, non-receptor, 1
            KO: K08886  tyrosine kinase, non-receptor, 2
            KO: K08897  Eph receptor A10
            KO: K08898  lemur tyrosine kinase 2
            KO: K08899  lemur tyrosine kinase 3
GENES       HSA: 10188(TNK2) 10461(MERTK) 114783(LMTK3) 1436(CSF1R) 1956(EGFR)
                 1969(EPHA2) 2041(EPHA1) 2042(EPHA3) 2043(EPHA4) 2044(EPHA5)
                 2045(EPHA7) 2046(EPHA8) 2047(EPHB1) 2048(EPHB2) 2049(EPHB3)
                 2050(EPHB4) 2051(EPHB6) 2064(ERBB2) 2065(ERBB3) 2066(ERBB4)
                 2260(FGFR1) 2261(FGFR3) 2263(FGFR2) 2264(FGFR4) 22853(LMTK2)
                 2321(FLT1) 2322(FLT3) 2324(FLT4) 238(ALK) 284656(EPHA10)
                 285220(EPHA6) 3480(IGF1R) 3643(INSR) 3645(INSRR) 3791(KDR)
                 3815(KIT) 4058(LTK) 4233(MET) 4486(MST1R) 4593(MUSK)
                 4914(NTRK1) 4915(NTRK2) 4916(NTRK3) 4919(ROR1) 4920(ROR2)
                 4921(DDR2) 5156(PDGFRA) 5159(PDGFRB) 558(AXL) 5754(PTK7)
                 5979(RET) 6098(ROS1) 6259(RYK) 7010(TEK) 7075(TIE1)
                 7301(TYRO3) 780(DDR1) 8711(TNK1)
            PTR: 451980(ERBB3) 452508(FLT3) 452512(FLT1) 453350(LTK)
                 453676(IGF1R) 455225(TNK1) 455649(INSR) 456182(LOC456182)
                 456613(EPHB2) 456910(ROR1) 457467(DDR2) 459126(LOC459126)
                 459492(MERTK) 459919(ERBB4) 460531(EPHA3) 460538(EPHA6)
                 461315(KDR) 461316(KIT) 462188(PDGFRB) 462301(FGFR4)
                 462339(FLT4) 462548(DDR1) 462708(PTK7) 463415(EGFR)
                 463610(EPHB4) 463671(MET) 463799(EPHB6) 463808(EPHA1)
                 464122(FGFR1) 464589(ROR2) 464653(MUSK) 465028(TEK)
                 466220(FGFR2) 467751(NTRK3) 469308(TIE1) 470660(EPHA4)
                 472108(ROS1) 472454(LMTK2) 744480(MST1R)
            MCC: 712829(FGFR3)
            MMU: 11682(Alk) 12305(Ddr1) 12978(Csf1r) 13649(Egfr) 13835(Epha1)
                 13836(Epha2) 13837(Epha3) 13838(Epha4) 13839(Epha5)
                 13840(Epha6) 13841(Epha7) 13842(Epha8) 13844(Ephb2)
                 13845(Ephb3) 13846(Ephb4) 13848(Ephb6) 13866(Erbb2)
                 13867(Erbb3) 13869(Erbb4) 14182(Fgfr1) 14183(Fgfr2)
                 14184(Fgfr3) 14186(Fgfr4) 14254(Flt1) 14255(Flt3) 14257(Flt4)
                 16001(Igf1r) 16337(Insr) 16542(Kdr) 16590(Kit) 17005(Ltk)
                 17289(Mertk) 17295(Met) 18198(Musk) 18211(Ntrk1) 18212(Ntrk2)
                 18213(Ntrk3) 18214(Ddr2) 18595(Pdgfra) 18596(Pdgfrb)
                 19713(Ret) 19882(Mst1r) 19886(Ros1) 20187(Ryk) 21687(Tek)
                 21846(Tie1) 22174(Tyro3) 231876(Lmtk2) 23920(Insrr) 26362(Axl)
                 26563(Ror1) 26564(Ror2) 270190(Ephb1) 381983(Lmtk3)
                 51789(Tnk2) 71461(Ptk7) 83813(Tnk1)
            RNO: 114110(Flt4) 140585(Ryk) 140635(Flt3) 171287(Epha7)
                 24329(Egfr) 24337(Erbb2) 24338(Ephb1) 24553(Met) 24629(Pdgfrb)
                 24716(Ret) 24954(Insr) 25022(Fgfr2) 25054(Ntrk2) 25114(Fgfr4)
                 25232(Tyro3) 25267(Pdgfra) 25346(Ros1) 25589(Kdr) 25678(Ddr1)
                 25718(Igf1r) 266802(Alk) 287989(Ephb3_predicted)
                 29202(Epha6_predicted) 29210(Epha3) 29496(Erbb3) 29613(Ntrk3)
                 298528(RGD1562679_predicted) 300999(Mst1r_predicted)
                 301242(Ptk7_predicted) 303247(Tnk1_predicted) 303882(Tnk2)
                 304286(LOC304286) 306782(Ror2_predicted) 307403(Csf1r)
                 308444(Axl) 311337(Ltk_predicted) 312275(Ephb6)
                 312279(Epha1_predicted) 313633(Ephb2_predicted)
                 316539(RGD1560587_predicted) 362550(RGD1559469_predicted)
                 366492(Epha2_predicted) 54251(Flt1) 59109(Ntrk1) 59323(Erbb4)
                 60589(Epha8) 60663(Insrr) 64030(Kit) 65037(Mertk) 79114(Fgfr1)
                 79208(Epha5) 81725(Musk) 84489(Fgfr3) 89804(Tek) 89806(Tie1)
            CFA: 403438(MET) 403494(RET) 403727(FLT1) 403811(KIT)
                 403883(ERBB2) 404306(EGFR) 415125(FGFR2) 442860(PDGFRA)
                 442951(IGF1R) 442985(PDGFRB) 444854(MST1R) 474832(DDR1)
                 474997(EPHA7) 475519(EPHB6) 475582(FGFR1) 477074(RYK)
                 478925(EPHA4) 478987(DDR2) 481105(ERBB3) 481464(FLT4)
                 481662(MUSK) 481808(PTK7) 482154(KDR) 482471(EPHA10)
                 482535(TIE1) 482735(EPHA1) 483021(ALK) 483060(MERTK)
                 484098(ROS1) 484147(NTRK2) 484193(ROR2) 484490(AXL)
                 484990(INSR) 485671(EPHB1) 486025(FLT3) 487380(EPHB2)
                 487383(EPHA8) 487421(EPHA2) 487509(TYRO3) 487930(EPHA3)
                 488025(TNK2) 488108(EPHB3) 488508(ERBB4) 488808(FGFR3)
                 489095(FGFR4) 489188(CSF1R) 489470(TNK1) 489557(ROR1)
                 489830(EPHB4) 490404(NTRK1) 490405(INSRR) 607935(EPHA6)
                 608946(LMTK2) 609087(NTRK3)
            BTA: 280710(ACK1) 280832(KIT) 280855(MET) 280939(TEK) 280941(TIE)
                 281768(FGFR1) 281769(FGFR3) 281848(IGF1R) 282301(PDGFRA)
                 317696(FGFR4) 353111(NTRK1) 404193(FGFR2) 407170(flk-1)
                 407217(EGFR) 408017(LOC408017) 504429(LOC504429) 505824(NTRK2)
                 509418(LOC509418) 510356(LOC510356) 512290(LOC512290)
                 512700(LOC512700) 512798(LOC512798) 514819(LOC514819)
                 515019(LOC515019) 515756(LOC515756) 517368(LOC517368)
                 520192(MGC142975) 525504(LOC525504) 525946(LOC525946)
                 527165(LOC527165) 529800(LOC529800) 533523(MGC140218)
                 534092(DDR1) 535137(LOC535137) 536642(LOC536642)
                 537806(LOC537806) 537951(LOC537951) 538224(LOC538224)
                 540052(LOC540052) 540907(LOC540907)
            SSC: 396810(KIT) 397070(EGFR) 397350(IGF1R) 397511(TRKC)
                 654328(MET)
            GGA: 373897(MUSK) 374008(EPHA6) 374100(FLT1) 378782(EPHA1)
                 378783(KIT) 395179(ROR1) 395323(KDR) 395336(TYRO3) 395409(RYK)
                 395509(PDGFRA) 395559(EPHA4) 395671(ERBB4) 395742(FLT4)
                 395836(RCJMB04_2i14) 395889(IGF1R) 395967(EPHA7) 395997(EPHA5)
                 396081(NTRK3) 396107(RET) 396134(MET) 396157(NTRK2)
                 396177(EPHB1) 396179(EPHB3) 396259(FGFR2) 396337(NTRK1)
                 396402(EPHA3) 396404(DDR2) 396406(CSF1R) 396494(LOC396494)
                 396513(EPHB2) 396515(FGFR3) 396516(FGFR1) 418308(EPHB6)
                 420133(INSR) 421257(PTK7) 421297(ALK) 422316(LOC422316)
                 423216(LTK) 424562(TIE1) 426130(ERBB2) 427368(TEK)
                 427573(MST1R) 693245(ERBB3) 769200(LMTK2) 769516(ROR2)
                 770488(PDGFRB)
            XLA: 373772(kl1-A) 379148(pag) 379266(trkb-b) 379546(MGC68952)
                 380245(pdgfra) 397701(LOC397701) 398862(MGC68806)
                 398941(MGC68585) 398981(MGC69083) 399325(Fgfr2) 399444(X1FGFR)
                 444707(MGC84433)
            XTR: 448450(epha2) 493543(csf1r) 548551(ror2) 548648(fgfr1)
                 549077(fgfr4) 550026(ryk)
            DRE: 100001635(LOC100001635) 245699(insra) 245700(insrb)
                 245701(igf1ra) 245702(igf1rb) 245951(ros1) 30121(flt4)
                 30256(kita) 30311(ek1) 30313(ek3) 30512(ret1) 30688(ephb4a)
                 30689(rtk6) 30705(fgfr1) 30706(fgfr4) 30709(dtk) 30745(pdgfra)
                 30747(tie2) 352940(fgfr2) 378478(egfr) 386635(erbb3a)
                 386966(erbb2) 492292(met) 497629(kitb) 544664(erbb3b)
                 544667(flt1) 554230(kdrb) 558502(zgc:158381) 561183(LOC561183)
                 562176(LOC562176) 562887(LOC562887) 563509(LOC563509)
                 564470(LOC564470) 564666(LOC564666) 565029(zgc:154019)
                 565333(ddr2) 566249(LOC566249) 568282(si:dkey-209n16.1)
                 568668(si:dkey-18e5.1) 570240(LOC570240) 58106(kdr)
                 58129(fgfr3) 64270(epha4b) 64271(epha4a) 64274(csf1r)
            SPU: 373310(FGFR) 579152(IR) 579837(LOC579837) 583375(LOC583375)
                 587032(LOC587032) 587396(LOC587396) 588763(LOC588763)
                 589012(LOC589012) 590851(LOC590851) 592402(LOC592402)
            DME: Dmel_CG10079(Egfr) Dmel_CG10244 Dmel_CG1389(tor)
                 Dmel_CG14396(Ret) Dmel_CG14992 Dmel_CG1511(Eph)
                 Dmel_CG17348(drl) Dmel_CG17559(dnt) Dmel_CG18085(sev)
                 Dmel_CG18402(InR) Dmel_CG32134(btl) Dmel_CG3915(Drl-2)
                 Dmel_CG3969(PR2) Dmel_CG4007(Nrk) Dmel_CG4926 Dmel_CG7223(htl)
                 Dmel_CG7525(Tie) Dmel_CG8222(Pvr) Dmel_CG8250 Dmel_CG8967(otk)
            CEL: C01C7.1(ark-1) C01G6.8(cam-1) C08H9.8 C16B8.1(lin-18)
                 C16D9.2(rol-3) C24G6.2 F09A5.2 F11D5.3 F11E6.8 F59F3.1(ver-3)
                 M03A1.1(vab-1) M176.6(kin-15) M176.7(kin-16) T10H9.2(scd-2)
                 Y55D5A.5(daf-2) ZK1067.1(let-23)
            TET: TTHERM_00051780 TTHERM_00260780 TTHERM_00388610
                 TTHERM_00392920 TTHERM_00426220 TTHERM_00697080
                 TTHERM_00720110 TTHERM_00777360 TTHERM_01100450
                 TTHERM_01111050 TTHERM_01251240 TTHERM_01639960
            ECP: ECP_2100
            ECW: EcE24377A_2353(wzc)
            ECX: EcHS_A2191(etk2)
            ENT: Ent638_2674 Ent638_2715
            PAT: Patl_1073 Patl_1168 Patl_4000
            BVI: Bcep1808_4205 Bcep1808_4770 Bcep1808_5614 Bcep1808_6524
            BAM: Bamb_5116 Bamb_6175
            PNA: Pnap_3132 Pnap_3194
            AJS: Ajs_3012
            HAR: HEAR0716 HEAR3415(soj)
            NET: Neut_2120
            AZO: azo2240(wzc1) azo3281(wzc2)
            MFA: Mfla_2024
            PPD: Ppro_2473
            DVL: Dvul_3069
            SFU: Sfum_2183
            RLE: pRL90134
            RSH: Rsph17029_1220 Rsph17029_3692
            MGM: Mmc1_0586
            ABA: Acid345_3310
            SUS: Acid_1649 Acid_4639 Acid_4855 Acid_4881
            CTH: Cthe_1363
            CBO: CBO2687
            DRM: Dred_3000
            MVA: Mvan_1681
            MGI: Mflv_4771
            MMC: Mmcs_0946
            MKM: Mkms_0964
            MJL: Mjls_0956
            RHA: RHA1_ro05453 RHA1_ro05735 RHA1_ro07020
            NCA: Noca_4185
            FAL: FRAAL1244
            RXY: Rxyl_0560 Rxyl_1943
            TER: Tery_1925
            CHU: CHU_0880(wzc)
            GFO: GFO_1983
            CPH: Cpha266_2649
STRUCTURES  PDB: 2CKN  2DTG  2E7H  2E9W  2EAO  2EC8  2GS2  2GS6  2GS7  2GSF  
                 2GY5  2GY7  2HEN  2HLE  2I0V  2I0Y  2I1M  2IEP  2IFG  2ITN  
                 2ITO  2ITP  2ITQ  2ITT  2ITU  2ITV  2ITW  2ITX  2ITY  2ITZ  
                 2IVS  2IVT  2IVU  2IVV  2J5E  2J5F  2J6M  2O26  2OGV  2OH4  
                 2OJ9  2OO8  2OSC  2P0C  2P2H  2P2I  2P4I  2PSQ  2PVF  2PVY  
                 2PWL  2PY3  2PZ5  2PZP  2PZR  2Q0B  2QKQ  2QO2  2QO7  2QO9  
                 2QOB  2QOC  2QOD  2QOF  2QOI  2QOK  2QOL  2QON  2QOO  2QOQ  
                 2QU5  2QU6  2R2P  2Z4F  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.10.1
            ExPASy - ENZYME nomenclature database: 2.7.10.1
            ExplorEnz - The Enzyme Database: 2.7.10.1
            ERGO genome analysis and discovery system: 2.7.10.1
            BRENDA, the Enzyme Database: 2.7.10.1
///
ENTRY       EC 2.7.10.2                 Enzyme
NAME        non-specific protein-tyrosine kinase;
            ABL;
            ABL1;
            ABL2;
            ABLL;
            ACK1;
            ACK2;
            AGMX1;
            ARG;
            ATK;
            ATP:protein-tyrosine O-phosphotransferase (ambiguous);
            BLK;
            Bmk;
            BMX;
            BRK;
            Bruton's tyrosine kinase;
            Bsk;
            BTK;
            BTKL;
            CAKb;
            Cdgip;
            CHK;
            CSK;
            CTK;
            CYL;
            cytoplasmic protein tyrosine kinase;
            EMT;
            ETK;
            Fadk;
            FAK;
            FAK2;
            FER;
            Fert1/2;
            FES;
            FGR;
            focal adhesion kinase;
            FPS;
            FRK;
            FYN;
            HCK;
            HCTK;
            HYL;
            IMD1;
            ITK;
            IYK;
            JAK1;
            JAK2;
            JAK3;
            Janus kinase 1;
            Janus kinase 2;
            Janus kinase 3;
            JTK1;
            JTK9;
            L-JAK;
            LCK;
            LSK;
            LYN;
            MATK;
            Ntk;
            p60c-src protein tyrosine kinase;
            PKB;
            protein-tyrosine kinase (ambiguous);
            PSCTK;
            PSCTK1;
            PSCTK2;
            PSCTK4;
            PSCTK5;
            PTK2;
            PTK2B;
            PTK6;
            PYK2;
            RAFTK;
            RAK;
            Rlk;
            Sik;
            SLK;
            SRC;
            SRC2;
            SRK;
            SRM;
            SRMS;
            STD;
            SYK;
            SYN;
            Tck;
            TEC;
            TNK1;
            Tsk;
            TXK;
            TYK2;
            TYK3;
            YES1;
            YK2;
            ZAP70
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-tyrosine kinases
SYSNAME     ATP:[protein]-L-tyrosine O-phosphotransferase (non-specific)
REACTION    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine
            phosphate [RN:R02584]
ALL_REAC    R02584
SUBSTRATE   ATP [CPD:C00002];
            [protein]-L-tyrosine [CPD:C00585]
PRODUCT     ADP [CPD:C00008];
            [protein]-L-tyrosine phosphate [CPD:C01167]
COMMENT     Unlike EC 2.7.10.1, receptor protein-tyrosine kinase, this
            protein-tyrosine kinase does not have a transmembrane domain. In the
            human genome, 32 non-specific protein-tyrosine kinases have been
            identified and these can be divided into ten families [1].
REFERENCE   1  [PMID:11114734]
  AUTHORS   Robinson DR, Wu YM, Lin SF.
  TITLE     The protein tyrosine kinase family of the human genome.
  JOURNAL   Oncogene. 19 (2000) 5548-57.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:15504335]
  AUTHORS   Roskoski R Jr.
  TITLE     Src protein-tyrosine kinase structure and regulation.
  JOURNAL   Biochem. Biophys. Res. Commun. 324 (2004) 1155-64.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04012  ErbB signaling pathway
            PATH: map04020  Calcium signaling pathway
            PATH: map04110  Cell cycle
            PATH: map04360  Axon guidance
            PATH: map04370  VEGF signaling pathway
            PATH: map04510  Focal adhesion
            PATH: map04520  Adherens junction
            PATH: map04530  Tight junction
            PATH: map04540  Gap junction
            PATH: map04630  Jak-STAT signaling pathway
            PATH: map04650  Natural killer cell mediated cytotoxicity
            PATH: map04660  T cell receptor signaling pathway
            PATH: map04662  B cell receptor signaling pathway
            PATH: map04664  Fc epsilon RI signaling pathway
            PATH: map04670  Leukocyte transendothelial migration
            PATH: map04730  Long-term depression
            PATH: map04810  Regulation of actin cytoskeleton
            PATH: map04912  GnRH signaling pathway
            PATH: map04920  Adipocytokine signaling pathway
            PATH: map05120  Epithelial cell signaling in Helicobacter pylori
                            infection
            PATH: map05130  Pathogenic Escherichia coli infection - EHEC
            PATH: map05131  Pathogenic Escherichia coli infection - EPEC
            PATH: map05220  Chronic myeloid leukemia
            PATH: map05222  Small cell lung cancer
ORTHOLOGY   KO: K04447  Janus kinase
            KO: K05703  proto-oncogene tyrosine-protein kinase Fyn
            KO: K05704  proto-oncogene tyrosine-protein kinase Src
            KO: K05705  proto-oncogene tyrosine-protein kinase Yes
            KO: K05725  PTK2 protein tyrosine kinase 2
            KO: K05728  c-src tyrosine kinase
            KO: K05854  tyrosine-protein kinase Lyn
            KO: K05855  spleen tyrosine kinase
            KO: K05856  lymphocyte-specific protein tyrosine kinase
            KO: K05871  protein tyrosine kinase 2 beta
            KO: K06619  proto-oncogene tyrosine-protein kinase ABL1
            KO: K07360  zeta-chain (TCR) associated protein kinase
            KO: K07363  IL2-inducible T-cell kinase
            KO: K07364  tec protein tyrosine kinase
            KO: K07370  Bruton agammaglobulinemia tyrosine kinase
            KO: K07527  proto-oncogene tyrosine-protein kinase Fes/Fps
            KO: K08016  TXK tyrosine kinase
            KO: K08253  non-specific protein-tyrosine kinase
            KO: K08887  proto-oncogene tyrosine-protein kinase ABL2
            KO: K08888  megakaryocyte-associated tyrosine kinase
            KO: K08889  fer (fps/fes related) tyrosine kinase
            KO: K08890  B lymphoid tyrosine kinase
            KO: K08891  proto-oncogene tyrosine-protein kinase FGR
            KO: K08892  fyn-related kinase
            KO: K08893  hemopoietic cell kinase
            KO: K08894  PTK6 protein tyrosine kinase 6
            KO: K08895  src-related kinase lacking C-terminal regulatory
                        tyrosine and N-terminal myristylation sites
            KO: K08896  BMX non-receptor tyrosine kinase
GENES       HSA: 1445(CSK) 2185(PTK2B) 2241(FER) 2242(FES) 2268(FGR) 2444(FRK)
                 25(ABL1) 2534(FYN) 27(ABL2) 3055(HCK) 3702(ITK) 3716(JAK1)
                 3717(JAK2) 3718(JAK3) 3932(LCK) 4067(LYN) 4145(MATK)
                 55359(STYK1) 5747(PTK2) 5753(PTK6) 640(BLK) 660(BMX) 6714(SRC)
                 6725(SRMS) 6850(SYK) 695(BTK) 7006(TEC) 7294(TXK) 7297(TYK2)
                 7525(YES1) 7535(ZAP70)
            PTR: 453745(CSK) 455322(YES1) 455592(LOC455592) 455703(TYK2)
                 455848(JAK3) 457552(ABL2) 458163(HCK) 458229(SRC)
                 458409(LOC458409) 459427(ZAP70) 461343(TEC) 461344(TXK)
                 461981(FER) 462953(FRK) 464073(PTK2B) 464422(PTK2) 464586(SYK)
                 464802(ABL1) 464979(JAK2) 465759(BTK) 470000(SRMS) 472771(LYN)
            MCC: 712787(LOC712787)
            MMU: 11350(Abl1) 11352(Abl2) 12143(Blk) 12169(Bmx) 12229(Btk)
                 12988(Csk) 14083(Ptk2) 14158(Fert2) 14159(Fes) 14191(Fgr)
                 14302(Frk) 14360(Fyn) 15162(Hck) 16428(Itk) 16451(Jak1)
                 16452(Jak2) 16453(Jak3) 16818(Lck) 17096(Lyn) 17179(Matk)
                 19229(Ptk2b) 20459(Ptk6) 20779(Src) 20811(Srms) 20963(Syk)
                 21682(Tec) 22165(Txk) 22612(Yes1) 22637(Zap70) 243659(Styk1)
                 54721(Tyk2)
            RNO: 24514(Jak2) 24884(Yes1) 25150(Fyn) 25155(Syk) 25326(Jak3)
                 25614(Ptk2) 25734(Hck) 296472(Srms) 301348(Zap70)
                 301737(Fert2) 305311(Txk) 311860(Abl1) 313050(Lck) 315707(Csk)
                 361597(RGD1564385_predicted) 363577(Itk_predicted) 364403(Blk)
                 366275(Ptk6_predicted) 367786(RGD1565643_predicted)
                 367901(Btk) 500340(RGD1564211_predicted) 50646(Ptk2b)
                 60450(Matk) 79113(Fgr) 79209(Frk) 81515(Lyn) 83805(Src)
                 84492(Tec) 84598(Jak1)
            CFA: 403754(FER) 403917(YES) 442952(JAK1) 475032(FYN) 475108(PTK2)
                 476714(TYK2) 477286(SRMS) 477886(LYN) 478151(LCK) 480052(ABL2)
                 481970(FRK) 482139(TXK) 482140(TEC) 484185(JAK2) 484196(SYK)
                 485828(HCK) 485864(SRC) 486080(BLK) 486102(PTK2B)
                 486689(STYK1) 487341(FGR) 487649(CSK) 489159(ITK) 490532(YES1)
                 491292(ABL1) 491750(BMX) 492019(BTK) 607259(LOC607259)
                 609483(FES) 610004(JAK3) 611999(MATK) 612522(LOC612522)
            BTA: 504509(LOC504509) 504668(MATK) 504782(TXK) 507304(FES)
                 507632(LOC507632) 508890(MGC126900) 509227(LOC509227)
                 509246(MGC142896) 511845(LOC511845) 512484(LOC512484)
                 513920(SYTK1) 515515(SYK) 516133(MGC159776) 521816(LOC521816)
                 525246(LOC525246) 527263(FYN) 529814(LOC529814)
                 531514(LOC531514) 532587(MGC142356) 533459(BTK)
                 534996(LOC534996) 535742(LOC535742) 536759(LOC536759)
                 540876(LOC540876) 541008(MGC139227)
            SSC: 397201(JAK2) 397202(JAK1)
            GGA: 374075(BTK) 374199(JAK2) 395410(ABL2) 395681(RCJMB04_5p6)
                 395845(JAK3) 396238(YES1) 396294(FYN) 396396(CSK)
                 396407(RCJMB04_29e6) 396416(PTK2) 396442(SRC) 415614(FER)
                 416247(ITK) 417181(ABL1) 418310(STYK1) 419246(SRMS)
                 419280(HCK) 420069(APBA3) 420086(ZAP70) 421127(LYN)
                 421747(FRK) 422035(BLK) 427272(RCJMB04_19o18) 428003(BMX)
                 429374(FES) 429577(LOC429577) 769076(MATK) 770387(TXK)
            XLA: 379169(MGC53012) 379629(yes) 379812(fyn) 380430(src)
                 399022(MGC68754) 403362(MGC69056) 432072(MGC83487)
                 443637(LOC443637) 444089(MGC83617) 444292(MGC80946)
                 446500(syk) 446697(jak1) 446840(zap70)
            XTR: 448557(zap70) 493548(yes1) 496459(ptk2b) 496893(src)
                 548439(MGC107870) 549656(LOC549656) 549989(lyn)
            DRE: 142986(ptk2.1) 245950(ptk2b) 30280(jak1) 30298(jak2b)
                 30307(jak2a) 30323(itk) 325084(src) 337571(yrk) 386705(ptk2.2)
                 405769(syk) 407620(yes1) 414333(lck) 447804(zgc:92124)
                 553615(zgc:110383) 555232(LOC555232) 556454(csk)
                 561155(LOC561155) 565199(LOC565199) 566739(LOC566739)
                 567405(LOC567405) 567764(si:dkey-33i22.2) 568653(LOC568653)
                 569627(LOC569627) 570636(LOC570636) 573009(LOC573009)
                 574422(fynb)
            SPU: 373187(abl) 373472(SFK1) 581102(LOC581102) 583220(LOC583220)
                 589201(LOC589201) 594826(LOC594826) 752814(LOC752814)
            DME: Dmel_CG10023(Fak56D) Dmel_CG1594(hop) Dmel_CG17309(Csk)
                 Dmel_CG18247(shark) Dmel_CG4032(Abl) Dmel_CG7524(Src64B)
                 Dmel_CG7873(Src42A)
            CEL: B0523.1(kin-31) C30F8.4(kin-32) F49B2.5(src-2) M79.1(abl-1)
                 T06C10.6(kin-26) Y92H12A.1(src-1) ZK622.1
            ECW: EcE24377A_1097(etk)
            ECX: EcHS_A1090(etk1)
            SPE: Spro_1585 Spro_2893
            ASU: Asuc_0096
            PPF: Pput_2587
            PRW: PsycPRwf_0251
            AHA: AHA_2877
            GUR: Gura_1670 Gura_2363 Gura_2579
            AFW: Anae109_1251 Anae109_2615 Anae109_2632 Anae109_4428
            PLA: Plav_1906 Plav_2999
            SMD: Smed_4961
            RLE: RL3662(exoP)
            BRA: BRADO0927 BRADO2234 BRADO2514 BRADO3825 BRADO4812
            BBT: BBta_1034
            RSQ: Rsph17025_1961
            SWI: Swit_4528 Swit_4817
            ACR: Acry_1523
            SAJ: SaurJH9_0136 SaurJH9_2687
            SAH: SaurJH1_0141 SaurJH1_2744
            CBE: Cbei_4741
            FAL: FRAAL0753 FRAAL0755 FRAAL2247 FRAAL3292
            KRA: Krad_0012
            SEN: SACE_5241
            FJO: Fjoh_0360
            RRS: RoseRS_4042 RoseRS_4270
            RCA: Rcas_1353 Rcas_3668
STRUCTURES  PDB: 2DM0  2DQ7  2E2B  2E6I  2EKX  2GQG  2H8H  2HDA  2HIW  2HK5  
                 2HWO  2HWP  2HYY  2HZ0  2HZ4  2HZI  2HZN  2IJM  2IN6  2IO6  
                 2J0J  2J0K  2J0L  2J0M  2O88  2OF2  2OF4  2OFU  2OFV  2OG8  
                 2OI3  2OIQ  2OQ1  2OZO  2PL0  2QOH  2V7A  2YS2  2YUQ  2Z60  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.10.2
            ExPASy - ENZYME nomenclature database: 2.7.10.2
            ExplorEnz - The Enzyme Database: 2.7.10.2
            ERGO genome analysis and discovery system: 2.7.10.2
            BRENDA, the Enzyme Database: 2.7.10.2
///
ENTRY       EC 2.7.11.1                 Enzyme
NAME        non-specific serine/threonine protein kinase;
            A-kinase;
            AP50 kinase;
            ATP-protein transphosphorylase;
            calcium-dependent protein kinase C;
            calcium/phospholipid-dependent protein kinase;
            cAMP-dependent protein kinase;
            cAMP-dependent protein kinase A;
            casein kinase;
            casein kinase (phosphorylating);
            casein kinase 2;
            casein kinase I;
            casein kinase II;
            cGMP-dependent protein kinase;
            CK-2;
            CKI;
            CKII;
            cyclic AMP-dependent protein kinase;
            cyclic AMP-dependent protein kinase A;
            cyclic monophosphate-dependent protein kinase;
            cyclic nucleotide-dependent protein kinase;
            cyclin-dependent kinase;
            cytidine 3',5'-cyclic monophosphate-responsive protein kinase;
            dsk1;
            glycogen synthase a kinase;
            glycogen synthase kinase;
            HIPK2;
            Hpr kinase;
            hydroxyalkyl-protein kinase;
            hydroxyalkyl-protein kinase;
            M phase-specific cdc2 kinase;
            mitogen-activated S6 kinase;
            p82 kinase;
            phosphorylase b kinase kinase;
            PKA;
            protein glutamyl kinase;
            protein kinase (phosphorylating);
            protein kinase A;
            protein kinase CK2;
            protein kinase p58;
            protein phosphokinase;
            protein serine kinase;
            protein serine-threonine kinase;
            protein-aspartyl kinase;
            protein-cysteine kinase;
            protein-serine kinase;
            Prp4 protein kinase;
            Raf kinase;
            Raf-1;
            ribosomal protein S6 kinase II;
            ribosomal S6 protein kinase;
            serine kinase;
            serine protein kinase;
            serine-specific protein kinase;
            serine(threonine) protein kinase;
            serine/threonine protein kinase;
            STK32;
            T-antigen kinase;
            threonine-specific protein kinase;
            twitchin kinase;
            type-2 casein kinase;
            betaIIPKC;
            epsilon PKC;
            Wee 1-like kinase;
            Wee-kinase;
            WEE1Hu
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:protein phosphotransferase (non-specific)
REACTION    ATP + a protein = ADP + a phosphoprotein [RN:R00162]
ALL_REAC    R00162;
            (other) R03632
SUBSTRATE   ATP [CPD:C00002];
            protein [CPD:C00017]
PRODUCT     ADP [CPD:C00008];
            phosphoprotein [CPD:C00562]
COMMENT     This is a heterogeneous group of serine/threonine protein kinases
            that do not have an activating compound and are either non-specific
            or their specificity has not been analysed to date.
REFERENCE   1  [PMID:2835010]
  AUTHORS   Damuni Z, Reed LJ.
  TITLE     Purification and properties of a protamine kinase and a type II
            casein kinase from bovine kidney mitochondria.
  JOURNAL   Arch. Biochem. Biophys. 262 (1988) 574-84.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:5456997]
  AUTHORS   Baggio B, Pinna LA, Moret V, Siliprandi N.
  TITLE     A simple procedure for the purification of rat liver phosvitin
            kinase.
  JOURNAL   Biochim. Biophys. Acta. 212 (1970) 515-7.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:4312674]
  AUTHORS   Jergil B, Dixon GH.
  TITLE     Protamine kinase from rainbow trout testis. Partial purification and
            characterization.
  JOURNAL   J. Biol. Chem. 245 (1970) 425-34.
  ORGANISM  rainbow trout
REFERENCE   4  [PMID:4310608]
  AUTHORS   Langan TA.
  TITLE     Action of adenosine 3',5'-monophosphate-dependent histone kinase in
            vivo.
  JOURNAL   J. Biol. Chem. 244 (1969) 5763-5.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:8485317]
  AUTHORS   Takeuchi M, Yanagida M.
  TITLE     A mitotic role for a novel fission yeast protein kinase dsk1 with
            cell cycle stage dependent phosphorylation and localization.
  JOURNAL   Mol. Biol. Cell. 4 (1993) 247-60.
  ORGANISM  Schizosaccharomyces pombe [GN:spo]
REFERENCE   6  [PMID:9102632]
  AUTHORS   Gross T, Lutzelberger M, Weigmann H, Klingenhoff A, Shenoy S, Kaufer
            NF.
  TITLE     Functional analysis of the fission yeast Prp4 protein kinase
            involved in pre-mRNA splicing and isolation of a putative mammalian
            homologue.
  JOURNAL   Nucleic. Acids. Res. 25 (1997) 1028-35.
  ORGANISM  Schizosaccharomyces pombe [GN:spo]
REFERENCE   7  [PMID:11267674]
  AUTHORS   Wang Y, Hofmann TG, Runkel L, Haaf T, Schaller H, Debatin K, Hug H.
  TITLE     Isolation and characterization of cDNAs for the protein kinase
            HIPK2.
  JOURNAL   Biochim. Biophys. Acta. 1518 (2001) 168-72.
  ORGANISM  human [GN:hsa], mouse [GN:mmu]
PATHWAY     PATH: map01510  Neurodegenerative Disorders
            PATH: map03320  PPAR signaling pathway
            PATH: map04010  MAPK signaling pathway
            PATH: map04012  ErbB signaling pathway
            PATH: map04110  Cell cycle
            PATH: map04111  Cell cycle - yeast
            PATH: map04115  p53 signaling pathway
            PATH: map04140  Regulation of autophagy
            PATH: map04150  mTOR signaling pathway
            PATH: map04210  Apoptosis
            PATH: map04310  Wnt signaling pathway
            PATH: map04320  Dorso-ventral axis formation
            PATH: map04340  Hedgehog signaling pathway
            PATH: map04350  TGF-beta signaling pathway
            PATH: map04360  Axon guidance
            PATH: map04370  VEGF signaling pathway
            PATH: map04510  Focal adhesion
            PATH: map04520  Adherens junction
            PATH: map04530  Tight junction
            PATH: map04540  Gap junction
            PATH: map04620  Toll-like receptor signaling pathway
            PATH: map04630  Jak-STAT signaling pathway
            PATH: map04650  Natural killer cell mediated cytotoxicity
            PATH: map04660  T cell receptor signaling pathway
            PATH: map04662  B cell receptor signaling pathway
            PATH: map04664  Fc epsilon RI signaling pathway
            PATH: map04670  Leukocyte transendothelial migration
            PATH: map04710  Circadian rhythm
            PATH: map04720  Long-term potentiation
            PATH: map04730  Long-term depression
            PATH: map04810  Regulation of actin cytoskeleton
            PATH: map04910  Insulin signaling pathway
            PATH: map04912  GnRH signaling pathway
            PATH: map04914  Progesterone-mediated oocyte maturation
            PATH: map04916  Melanogenesis
            PATH: map04920  Adipocytokine signaling pathway
            PATH: map05020  Parkinson's disease
            PATH: map05120  Epithelial cell signaling in Helicobacter pylori
                            infection
            PATH: map05130  Pathogenic Escherichia coli infection - EHEC
            PATH: map05131  Pathogenic Escherichia coli infection - EPEC
            PATH: map05210  Colorectal cancer
            PATH: map05211  Renal cell carcinoma
            PATH: map05212  Pancreatic cancer
            PATH: map05213  Endometrial cancer
            PATH: map05214  Glioma
            PATH: map05215  Prostate cancer
            PATH: map05216  Thyroid cancer
            PATH: map05217  Basal cell carcinoma
            PATH: map05218  Melanoma
            PATH: map05219  Bladder cancer
            PATH: map05220  Chronic myeloid leukemia
            PATH: map05221  Acute myeloid leukemia
            PATH: map05222  Small cell lung cancer
            PATH: map05223  Non-small cell lung cancer
ORTHOLOGY   KO: K02178  checkpoint serine/threonine-protein kinase
            KO: K02214  cell division control protein CDC7
            KO: K02216  serine/threonine-protein kinase Chk1
            KO: K02218  casein kinase 1
            KO: K02861  receptor-interacting serine/threonine-protein kinase 1
            KO: K03097  casein kinase 2, alpha polypeptide
            KO: K03114  mitosis inhibitor protein kinase SWE1
            KO: K03115  casein kinase 2, beta polypeptide
            KO: K04365  B-Raf proto-oncogene serine/threonine-protein kinase
            KO: K04366  RAF proto-oncogene serine/threonine-protein kinase
            KO: K04367  proto-oncogene serine/threonine-protein kinase mos
            KO: K04372  MAP kinase interacting serine/threonine kinase
            KO: K04373  p90 ribosomal S6 kinase
            KO: K04406  mitogen-activated protein kinase kinase kinase kinase 3
            KO: K04407  mitogen-activated protein kinase kinase kinase kinase 4
            KO: K04408  mitogen-activated protein kinase kinase kinase kinase 1
            KO: K04409  p21-activated kinase 1
            KO: K04410  p21-activated kinase 2
            KO: K04413  misshapen/NIK-related kinase
            KO: K04414  mitogen-activated protein kinase kinase kinase kinase 2
            KO: K04429  thousand and one amino acid protein kinase
            KO: K04442  mitogen-activated protein kinase-activated protein
                        kinase 5
            KO: K04443  mitogen-activated protein kinase-activated protein
                        kinase 2
            KO: K04444  mitogen-activated protein kinase-activated protein
                        kinase 3
            KO: K04445  mitogen-,stress activated protein kinases
            KO: K04456  RAC serine/threonine-protein kinase
            KO: K04514  Rho-associated, coiled-coil containing protein kinase
            KO: K04688  p70 ribosomal S6 kinase
            KO: K04702  proto-oncogene serine/threonine-protein kinase Pim-1
            KO: K04728  ataxia telangectasia mutated family protein
            KO: K04730  interleukin-1 receptor-associated kinase 1
            KO: K04731  interleukin-1 receptor-associated kinase 2
            KO: K04732  interleukin-1 receptor-associated kinase 3
            KO: K04733  interleukin-1 receptor-associated kinase 4
            KO: K04757  anti-sigma B factor
            KO: K04981  transient receptor potential cation channel, subfamily
                        M, member 6
            KO: K04982  transient receptor potential cation channel, subfamily
                        M, member 7
            KO: K05688  PTEN induced putative kinase 1
            KO: K05733  p21-activated kinase 3
            KO: K05734  p21-activated kinase 4
            KO: K05735  p21-activated kinase 6
            KO: K05736  p21-activated kinase 7
            KO: K05743  LIM domain kinase 1
            KO: K05744  LIM domain kinase 2
            KO: K06103  calcium/calmodulin-dependent serine protein kinase
            KO: K06228  fused
            KO: K06272  integrin-linked kinase
            KO: K06276  3-phosphoinositide dependent protein kinase-1
            KO: K06379  stage II sporulation protein AB (anti-sigma F factor)
            KO: K06632  wee1-like protein kinase
            KO: K06633  membrane-associated tyrosine- and threonine-specific
                        cdc2-inhibitory kinase
            KO: K06637  mitotic checkpoint serine/threonine-protein kinase BUB1
                        beta
            KO: K06640  ataxia telangiectasia and Rad3 related
            KO: K06641  serine/threonine-protein kinase Chk2
            KO: K06642  protein kinase, DNA-activated, catalytic polypeptide
            KO: K06683  cell division control protein CDC15
            KO: K07178  RIO kinase 1
            KO: K07179  RIO kinase 2
            KO: K08269  unc51-like kinase
            KO: K08282  non-specific serine/threonine protein kinase
            KO: K08333  phosphoinositide-3-kinase, regulatory subunit 4, p150
            KO: K08788  dystrophia myotonica-protein kinase
            KO: K08789  microtubule-associated serine/threonine kinase
            KO: K08790  serine/threonine kinase 38
            KO: K08791  LATS, large tumor suppressor
            KO: K08792  serum/glucocorticoid regulated kinase
            KO: K08793  serine/threonine kinase 32
            KO: K08796  BR serine/threonine kinase
            KO: K08797  hormonally upregulated Neu-associated kinase
            KO: K08798  MAP/microtubule affinity-regulating kinase
            KO: K08799  maternal embryonic leucine zipper kinase
            KO: K08800  NUAK family, SNF1-like kinase
            KO: K08801  PAS domain containing serine/threonine kinase
            KO: K08802  SNF related kinase
            KO: K08803  death-associated protein kinase
            KO: K08804  serine/threonine kinase 17
            KO: K08805  doublecortin and CaM kinase-like 1
            KO: K08806  proto-oncogene serine/threonine-protein kinase Pim-2
            KO: K08807  proto-oncogene serine/threonine-protein kinase Pim-3
            KO: K08808  protein serine kinase H
            KO: K08809  striated muscle-specific serine/threonine protein kinase
            KO: K08811  testis-specific serine kinase
            KO: K08816  vaccinia related kinase
            KO: K08826  homeodomain interacting protein kinase
            KO: K08827  PRP4 pre-mRNA processing factor 4
            KO: K08831  SFRS protein kinase
            KO: K08832  serine/threonine kinase 23
            KO: K08833  mitogen-activated protein kinase kinase kinase kinase 5
            KO: K08834  myosin III
            KO: K08835  oxidative-stress responsive protein 1
            KO: K08836  STE20-like kinase
            KO: K08837  serine/threonine kinase 10
            KO: K08838  serine/threonine kinase 24
            KO: K08840  TRAF2 and NCK interacting kinase
            KO: K08843  leucine-rich repeat kinase 1
            KO: K08844  leucine-rich repeat kinase 2
            KO: K08845  A-Raf proto-oncogene serine/threonine-protein kinase
            KO: K08846  receptor-interacting serine/threonine-protein kinase 2
            KO: K08847  receptor-interacting serine/threonine-protein kinase 3
            KO: K08848  receptor-interacting serine/threonine-protein kinase 4
            KO: K08849  mixed lineage kinase domain-like
            KO: K08850  aurora kinase
            KO: K08851  TP53 regulating kinase
            KO: K08852  endoplasmic reticulum to nucleus signalling IRE
            KO: K08853  AP2-associated kinase
            KO: K08854  BMP2 inducible kinase
            KO: K08855  cyclin G-associated kinase
            KO: K08856  serine/threonine kinase 16
            KO: K08857  NIMA (never in mitosis gene a)-related kinase
            KO: K08858  SH3-binding domain kinase 1
            KO: K08859  serine/threonine kinase 35
            KO: K08860  eukaryotic translation initiation factor 2-alpha kinase
            KO: K08864  tousled-like kinase
            KO: K08867  WNK lysine deficient protein kinase
            KO: K08872  RIO kinase 3
            KO: K08877  U2AF homology motif (UHM) kinase 1
            KO: K08878  breakpoint cluster region protein
            KO: K08880  serine/threonine kinase 19
            KO: K08884  serine/threonine protein kinase, bacterial
            KO: K08957  casein kinase 1, alpha
            KO: K08958  casein kinase 1, gamma
            KO: K08959  casein kinase 1, delta
            KO: K08960  casein kinase 1, epsilon
GENES       HSA: 10000(AKT3) 10110(SGK2) 10114(HIPK3) 10290(SPEG) 10298(PAK4)
                 10494(STK25) 10595(ERN2) 10783(NEK6) 11011(TLK2) 11035(RIPK3)
                 11040(PIM2) 1111(CHEK1) 11113(CIT) 11183(MAP4K5) 11184(MAP4K1)
                 11200(CHEK2) 11213(IRAK3) 112858(TP53RK) 11329(STK38)
                 120892(LRRK2) 122011(CSNK1A1L) 127933(UHMK1) 140469(MYO3B)
                 140609(NEK7) 140803(TRPM6) 140901(STK35) 1452(CSNK1A1)
                 1453(CSNK1D) 1454(CSNK1E) 1455(CSNK1G2) 1456(CSNK1G3)
                 1457(CSNK2A1) 1459(CSNK2A2) 1460(CSNK2B) 1612(DAPK1)
                 1613(DAPK3) 166614(DCLK2) 1760(DMPK) 197259(MLKL) 2011(MARK2)
                 202374(STK32A) 204851(HIPK1) 207(AKT1) 208(AKT2) 2081(ERN1)
                 22848(AAK1) 22983(MAST1) 23012(STK38L) 23031(MAST3)
                 23043(TNIK) 23139(MAST2) 23178(PASK) 23604(DAPK2) 23617(TSSK2)
                 23678(SGK3) 25778(RIPK5) 2580(GAK) 25989(ULK3) 26524(LATS2)
                 26576(SRPK3) 27102(EIF2AK1) 27148(STK36) 27330(RPS6KA6)
                 27347(STK39) 282974(STK32C) 283629(TSSK4) 284086(NEK8)
                 2872(MKNK2) 28996(HIPK2) 30811(HUNK) 30849(PIK3R4)
                 341676(NEK5) 347359(BMP2KL) 3611(ILK) 3654(IRAK1) 3656(IRAK2)
                 369(ARAF) 388228(SBK1) 3984(LIMK1) 3985(LIMK2) 4139(MARK1)
                 4140(MARK3) 415116(PIM3) 4342(MOS) 440275(EIF2AK4) 472(ATM)
                 4750(NEK1) 4751(NEK2) 4752(NEK3) 50488(MINK1) 5058(PAK1)
                 5062(PAK2) 5063(PAK3) 51135(IRAK4) 51231(VRK3) 51347(TAOK3)
                 5170(PDPK1) 51765(RP6-213H19.1) 5292(PIM1) 53904(MYO3A)
                 53944(CSNK1G1) 54101(RIPK4) 545(ATR) 54822(TRPM7) 54861(SNRK)
                 55351(STK32B) 55589(BMP2K) 55781(RIOK2) 5591(PRKDC)
                 5610(EIF2AK2) 5681(PSKH1) 56924(PAK6) 57144(PAK7) 57551(TAOK1)
                 57787(MARK4) 5871(MAP4K2) 5894(RAF1) 6093(ROCK1) 613(BCR)
                 6195(RPS6KA1) 6196(RPS6KA2) 6197(RPS6KA3) 6198(RPS6KB1)
                 6199(RPS6KB2) 6446(SGK) 65018(PINK1) 65125(WNK1) 65266(WNK4)
                 65267(WNK3) 65268(WNK2) 653052(LOC653052) 65975(STK33)
                 673(BRAF) 6732(SRPK1) 6733(SRPK2) 6787(NEK4) 6790(AURKA)
                 6793(STK10) 6795(AURKC) 699(BUB1) 701(BUB1B) 729871(LOC729871)
                 7443(VRK1) 7444(VRK2) 7465(WEE1) 7867(MAPKAPK3) 79705(LRRK1)
                 79858(NEK11) 81629(TSSK3) 81788(NUAK2) 8317(CDC7) 83732(RIOK1)
                 83942(TSSK1B) 83983(TSSK6) 8408(ULK1) 8428(STK24) 84446(BRSK1)
                 8491(MAP4K3) 84930(MASTL) 85481(PSKH2) 8550(MAPKAPK5)
                 8569(MKNK1) 8573(CASK) 8576(STK16) 8737(RIPK1) 8767(RIPK2)
                 8780(RIOK3) 8859(STK19) 8899(PRPF4B) 8986(RPS6KA4) 9024(BRSK2)
                 9088(PKMYT1) 9113(LATS1) 9128(PRPF4) 91754(NEK9) 9201(DCLK1)
                 9212(AURKB) 9252(RPS6KA5) 9261(MAPKAPK2) 9262(STK17B)
                 9263(STK17A) 9344(TAOK2) 9448(MAP4K4) 9451(EIF2AK3)
                 9475(ROCK2) 9706(ULK2) 9748(SLK) 9833(MELK) 9874(TLK1)
                 9891(NUAK1) 9943(OXSR1)
            PTR: 450118(PAK3) 450359(MYO3A) 450367(MASTL) 450716(SLK)
                 451368(LOC451368) 451439(PAK1) 451530(ATM) 451648(STT3A)
                 451739(WNK1) 452292(TAOK3) 452298(CIT) 452466(LATS2)
                 452633(STK24) 452737(NEK3) 452820(RIPK3) 453148(VRK1)
                 453184(MARK3) 453321(EIF2AK4) 453324(BUB1B) 453326(LOC453326)
                 453429(TRPM7) 453504(CSNK1G1) 453689(LRRK1) 453747(ULK3)
                 454242(RFWD3) 454455(MINK1) 454507(ULK2) 454548(TAOK1)
                 454769(ERN1) 455033(NEK8) 455095(AURKB) 455326(ROCK1)
                 455594(DAPK3) 455853(MAST3) 456035(AKT2) 456139(DMPK)
                 456230(VRK3) 456568(MAST2) 457666(RIPK5) 458041(STK35)
                 458303(TP53RK) 458733(CHEK2) 459155(EIF2AK2) 459250(VRK2)
                 459459(MAP4K4) 459484(BUB1) 459711(STK39) 459729(TLK1)
                 459843(STK17B) 460077(PASK) 460165(IRAK2) 460182(RAF1)
                 460301(SNRK) 460400(MAPKAPK3) 460692(PIK3R4) 460745(ATR)
                 460849(TNIK) 460965(PAK2) 461048(GAK) 461534(DCLK2)
                 461961(RIOK2) 462027(CSNK1G3) 462182(CSNK1A1) 462265(STK10)
                 462397(RIPK1) 462406(PRPF4B) 462576(STK19) 462640(SRPK1)
                 462647(STK38) 463011(SGK) 463255(EIF2AK1) 463466(LIMK1)
                 463641(SRPK2) 463772(HIPK2) 463781(BRAF) 464165(PRKDC)
                 464217(SGK3) 464277(RIPK2) 464571(DAPK1) 464671(PRPF4)
                 465095(MELK) 465653(WNK3) 465935(IRAK1) 466440(WEE1)
                 466962(IRAK4) 467058(IRAK3) 467259(DCLK1) 467264(CSNK1A1L)
                 467451(MAP4K5) 467880(PKMYT1) 468207(TLK2) 468426(RPS6KB1)
                 468499(RIOK3) 468777(TSSK6) 469189(MKNK1) 469560(UHMK1)
                 469876(PAK7) 469980(AURKA) 470307(ROCK2) 470579(MYO3B)
                 470791(OXSR1) 471345(NEK1) 471847(RIOK1) 472772(MOS)
                 472957(TRPM6) 473669(BMP2KL) 740898(AKT1)
            MCC: 693391(MYO3B) 707165(LOC707165) 719039(SRPK1)
            MMU: 101568(Vrk3) 102626(Mapkapk3) 103236(Csnk1g2) 104175(Sbk1)
                 104318(Csnk1d) 106504(Stk38) 108737(Oxsr1) 108960(Irak2)
                 109880(Braf) 110157(Raf1) 110279(Bcr) 110651(Rps6ka3)
                 11651(Akt1) 11652(Akt2) 117229(Stk33) 11790(Speg) 11836(Araf)
                 11920(Atm) 12235(Bub1) 12236(Bub1b) 12361(Cask) 12545(Cdc7)
                 12649(Chek1) 12704(Cit) 12995(Csnk2a1) 13000(Csnk2a2)
                 13001(Csnk2b) 13143(Dapk2) 13144(Dapk3) 13175(Dclk1)
                 13400(Dmpk) 13666(Eif2ak3) 13728(Mark2) 140780(Bmp2k)
                 140859(Nek8) 15257(Hipk1) 15258(Hipk2) 15259(Hipk3)
                 15467(Eif2ak1) 16179(Irak1) 16202(Ilk) 16589(Uhmk1)
                 16798(Lats1) 16885(Limk1) 16886(Limk2) 170755(Sgk3)
                 17164(Mapkapk2) 17165(Mapkapk5) 17169(Mark3) 17279(Melk)
                 17346(Mknk1) 17347(Mknk2) 17451(Mos) 17776(Mast2) 18004(Nek1)
                 18005(Nek2) 18479(Pak1) 18481(Pak3) 18607(Pdpk1) 18712(Pim1)
                 18715(Pim2) 19090(Prkdc) 19106(Eif2ak2) 19134(Prpf4b)
                 192656(Ripk2) 19766(Ripk1) 19877(Rock1) 19878(Rock2)
                 20111(Rps6ka1) 20112(Rps6ka2) 20393(Sgk) 20623(Snrk)
                 20815(Srpk1) 20817(Srpk2) 208583(Nek11) 20868(Stk10)
                 20871(Aurkc) 20872(Stk16) 20874(Slk) 20877(Aurkb) 20878(Aurka)
                 213452(Ripk5) 214230(Pak6) 214897(Csnk1g1) 216965(Taok1)
                 217718(Nek9) 22114(Tssk1) 22115(Tssk2) 22241(Ulk1)
                 223255(Stk24) 22367(Vrk1) 223775(Pim3) 22390(Wee1)
                 224105(Pak2) 225028(Map4k3) 225997(Trpm6) 226778(Mark1)
                 228012(Tlk1) 231580(Gak) 232341(Wnk1) 232533(Stk38l)
                 232944(Mark4) 233328(Lrrk1) 23797(Akt3) 23954(Nek3)
                 23955(Nek4) 240505(Cdc42bpg) 24086(Tlk2) 241656(Pak7)
                 244631(Pskh1) 26411(Map4k1) 26412(Map4k2) 26559(Hunk)
                 266632(Irak4) 268930(Pkmyt1) 269019(Stk32a) 26918(Ern2)
                 269209(Stk36) 26921(Map4k4) 269224(Pask) 269774(Aak1)
                 27103(Eif2ak4) 27219(Sgk2) 27373(Csnk1e) 279561(Wnk3)
                 29869(Ulk2) 328329(Mast4) 329421(Myo3b) 330177(Taok3)
                 330721(Nek5) 381979(Brsk1) 399510(Map4k5) 50523(Lats2)
                 50883(Chek2) 50932(Mink1) 53416(Stk39) 54402(Stk19)
                 545618(LOC545618) 546071(Mast3) 56504(Srpk3) 56527(Mast1)
                 56532(Ripk3) 56613(Rps6ka4) 57740(Stk32c) 58800(Trpm7)
                 58864(Tssk3) 58988(Rps6kb2) 59041(Stk25) 59125(Nek7)
                 59126(Nek6) 630567(LOC630567) 64293(Stk32b) 66725(Lrrk2)
                 667663(Myo3a) 66878(Riok3) 67045(Riok2) 67071(Rps6ka6)
                 67121(Mastl) 68943(Pink1) 69635(Dapk1) 69847(Wnk4) 69922(Vrk2)
                 70052(Prpf4) 70584(Pak4) 70762(Dclk2) 71099(Tssk4)
                 71340(Riok1) 71742(Ulk3) 72388(Ripk4) 72508(Rps6kb1)
                 73086(Rps6ka5) 73914(Irak3) 74137(Nuak2) 74568(Mlkl)
                 75607(Wnk2) 75669(Pik3r4) 75770(Brsk2) 76367(Trp53rk)
                 77976(Nuak1) 78943(Ern1) 83984(Tssk6) 93687(Csnk1a1)
                 98267(Stk17b)
            RNO: 113907(Sbk1) 113927(Csnk1a1) 114212(Chek2) 114482(Nek2)
                 114486(Braf) 114592(Aurkb) 114859(Eif2ak4_predicted)
                 116477(Prkwnk1) 116549(Csnk2a1) 117016(Mark1) 117269(Rps6ka2)
                 140583(Chek1) 170577(Mark3) 170837(Snrk) 170904(Stk17b)
                 170920(Map4k3) 170922(Ilk) 171497(Sgk2) 171498(Sgkl)
                 171576(Bub1b) 24185(Akt1) 24559(Mos) 246240(Ripk3)
                 246332(Uhmk1) 24649(Pim1) 24703(Raf1) 25233(Akt2) 25537(Rock2)
                 261730(Stk6) 27137(Eif2ak1) 286927(Stk16) 286993(Taok1)
                 287101(Pkmyt1_predicted) 287473(Nek8_predicted) 287715(Wnk4)
                 288275(RGD1565091_predicted) 288358(Tssk1) 289014(Mapkapk2)
                 289419(Nuak2) 290229(RGD1560814_predicted)
                 290670(Tssk6_predicted) 290705(Nek1_predicted) 291061(Riok1)
                 291078(Prpf4b) 292554(Aurkc_predicted) 292756(Pak4_predicted)
                 292763(Map4k1_predicted) 293631(Brsk2)
                 293694(Map4k2_predicted) 293854(Srpk3) 293874(Trpm6)
                 29398(Stk10) 29414(Akt3) 29431(Pak1) 29432(Pak2) 29433(Pak3)
                 294917(RGD1561817_predicted) 29517(Sgk) 29524(Limk2)
                 296078(Pak6_predicted) 296137(Bub1_predicted) 29647(Cask)
                 296753(Srpk2_predicted) 29702(Eif2ak3) 297891(Tssk3)
                 298095(Prpf4) 298575(Pink1_predicted) 299204(Nek9_predicted)
                 299618(Mknk2) 299694(Nuak1) 300160(Lrrk2)
                 300177(Irak4_predicted) 300711(Atm) 300944(Xrn1_predicted)
                 301363(Map4k4_predicted) 301516(Stk36_predicted) 301617(Pask)
                 303206(Ulk2_predicted) 303259(LOC303259)
                 303592(Tlk2_predicted) 304053(Ripk4_predicted) 304181(Tssk2)
                 304530(JIK) 304791(Ripk5) 305431(Stk32b_predicted)
                 305922(Lats2_predicted) 306252(Nek4) 306576(Nek3_predicted)
                 306722(Dapk1_predicted) 306811(RGD1307284_predicted)
                 306886(Ripk1_predicted) 307169(Mastl_predicted)
                 307641(Csnk2a2_predicted) 308201(Riok2)
                 308265(RGD1564085_predicted) 308405(Dmpk_predicted)
                 308703(Lrrk1_predicted) 308937(Wee1) 309696(Bcr_predicted)
                 310040(RGD1310139_predicted) 310698(Dclk2_predicted)
                 311118(Tlk1_predicted) 311419(Stk35_predicted)
                 311450(Pak7_predicted) 313819(Mast2_predicted)
                 314384(Rps6ka5_predicted) 314870(Irak3_predicted)
                 315978(Nek11_predicted) 315994(Mapkapk3)
                 316064(Oxsr1_predicted) 317203(Rps6ka6_predicted)
                 353118(MAST1) 360161(Nek6) 360748(Prkdc_predicted)
                 360827(Ulk1) 360850(Nek7_predicted) 360908(Cdc7_predicted)
                 360991(Vrk2_predicted) 361092(RGD1561742_predicted)
                 361293(Riok3_predicted) 361409(RGD1305243_predicted)
                 361565(Vrk3) 361623(LOC361623) 361696(Rps6kb2)
                 361715(Rps6ka4_predicted) 361800(Stk19) 361811(Srpk1)
                 362272(Trp53rk_predicted) 362342(Hipk2_predicted)
                 362418(Irak2) 362491(Ripk2) 362510(Melk_predicted)
                 362779(Vrk1) 363131(Pik3r4_predicted) 363256(LOC363256)
                 363520(Irak1_predicted) 364858(Stk32a_predicted)
                 364993(Pskh1_predicted) 365363(Ern2_predicted)
                 365381(Stk32c_predicted) 365895(Hipk1_predicted)
                 366069(RGD1560313_predicted) 367198(LOC367198) 373542(Stk25)
                 498013(RGD1559716_predicted) 498183(MGC116327) 498333(Bmp2k)
                 498806(RGD1560083_predicted) 499073(RGD1563268_predicted)
                 499884(LOC499884) 500244(RGD1563580_predicted)
                 500526(MGC112775) 501560(RGD1563860_predicted)
                 503027(RGD1562028_predicted) 54287(Prkr) 54308(Slk)
                 54348(Stk39) 58822(Csnk1e) 60328(Mark2) 64086(Csnk1g1)
                 64391(Dapk3) 64462(Csnk1d) 64534(Pim3) 64666(Taok2)
                 64823(Csnk1g3) 65172(Limk1) 65278(Csnk1g2) 680407(LOC680407)
                 684053(LOC684053) 686318(LOC686318) 686495(LOC686495)
                 686577(LOC686577) 686663(LOC686663) 686800(LOC686800)
                 687705(LOC687705) 688540(LOC688540) 690209(LOC690209)
                 691171(LOC691171) 81650(Csnk2b) 81659(Gak) 81745(Pdpk1)
                 81762(Rock1) 81771(Rps6ka1) 83617(Hipk3) 83620(Cit)
                 83825(Dclk1) 83840(Rps6kb1)
            CFA: 403531(LOC403531) 403647(SGK) 442959(PIM2) 442964(AKT3)
                 449021(AKT2) 474176(PRKDC) 474510(CSNK1E) 474605(VRK2)
                 474625(AAK1) 474807(PRPF4) 474844(CSNK2B) 474887(SRPK1)
                 475526(BRAF) 475734(MAP4K3) 475756(EIF2AK3) 475803(HIPK1)
                 475894(SRPK2) 475928(CSNK1D) 475947(HIPK3) 476241(LATS1)
                 476591(NEK4) 476660(TSSK6) 476670(MAST3) 476745(DAPK3)
                 476751(CSNK1G2) 476836(ILK) 476841(STK33) 476847(WEE1)
                 477011(SNRK) 477064(PIK3R4) 477101(ATR) 477185(CSNK2A1)
                 477304(DCLK1) 477343(LATS2) 477437(ULK1) 477480(MAPKAPK5)
                 477502(TAOK3) 477663(STK38L) 477728(WNK1) 477936(RIPK2)
                 478108(CSNK2A2) 478257(EIF2AK4) 478300(TRPM7) 478338(CSNK1G1)
                 478713(RIOK1) 478779(STK39) 478790(LOC478790)
                 478792(LOC478792) 478795(TLK1) 478913(STK36) 478924(DES)
                 478942(RIPK5) 478965(MARK1) 478986(UHMK1) 479133(LOC479133)
                 479147(RIOK2) 479331(CSNK1A1) 479450(ATM) 479492(AURKB)
                 479875(PDPK1) 479955(CDC7) 480008(NEK7) 480021(NEK2)
                 480174(RIOK3) 480181(ROCK1) 480262(TSSK4) 480580(RPS6KB1)
                 480632(TAOK1) 480887(CASK) 481150(IRAK3) 481296(NUAK1)
                 481331(MAP4K4) 481481(CSNK1G3) 481608(MELK) 481766(STK38)
                 481772(PIM1) 482509(MKNK1) 482513(MAST2) 482642(DCLK2)
                 482772(LOC482772) 482970(ROCK2) 483241(STK17A)
                 483658(LOC483658) 483757(CDC42BPG) 483759(MAP4K2)
                 483769(MARK2) 484142(DAPK1) 484163(TRPM6) 484210(LOC484210)
                 484297(BRSK1) 484367(VRK3) 484436(DMPK) 484449(MARK4)
                 484513(PAK4) 484527(MAP4K1) 484648(RAF1) 484657(IRAK2)
                 484756(MAPKAPK3) 485660(NEK11) 485772(PAK7) 485940(AURKA)
                 486058(NEK1) 486338(CHEK2) 486363(LIMK2) 486426(TSSK2)
                 486427(TSSK1B) 486601(IRAK4) 486608(LRRK2) 486876(SLK)
                 486959(MOS) 486981(SGK3) 487033(PSKH2) 487106(MYO3A)
                 487203(LOC487203) 487308(TSSK3) 487353(RPS6KA1) 487490(PAK6)
                 487651(ULK3) 487733(HUNK) 487772(RIPK4) 487819(BMP2K)
                 488166(TNIK) 488195(RIPK1) 488199(PRPF4B) 488436(LOC488436)
                 488453(STK17B) 488536(STK16) 488570(NUAK2) 488706(LRRK1)
                 489121(STK10) 489525(LOC489525) 489800(LIMK1) 489943(TAOK2)
                 489954(SBK1) 489970(ERN2) 490050(PKMYT1) 490263(MAPKAPK2)
                 490685(MAP4K5) 490790(NEK9) 490831(RPS6KA5) 490848(VRK1)
                 490878(AKT1) 490915(TLK2) 490959(LOC490959) 491171(NEK8)
                 491427(LOC491427) 491589(STK32C) 491768(RPS6KA3) 491857(ARAF)
                 491900(WNK3) 491989(RPS6KA6) 492067(PAK3) 492247(IRAK1)
                 607216(MASTL) 607482(BCR) 607545(STK19) 607809(OXSR1)
                 607885(PAK1) 608350(BUB1B) 608391(LOC608391) 608486(RIPK3)
                 609003(NEK6) 609111(LOC609111) 609432(STK35) 609502(PASK)
                 609767(CHEK1) 610499(RPS6KB2) 610682(DAPK2) 610766(ERN1)
                 610835(SGK2) 611147(STK32B) 611235(TP53RK) 611285(MARK3)
                 611397(EIF2AK2) 612105(RPS6KA4) 612212(MKNK2) 612448(RPS6KA2)
                 612525(SRPK3) 612814(PAK2) 612904(LOC612904)
            BTA: 280991(AKT1) 281402(PIM1) 282041(ROCK2) 282419(CSNK2A1)
                 282420(CSNK2A2) 282684(CSNK1A1) 347700(PRKR) 360192(AURKB)
                 373543(STK25) 404181(RPS6KB1) 407190(CSNK1G3) 444869(C-MOS)
                 504408(LOC504408) 504437(MGC134472) 504480(LOC504480)
                 504727(RIPK1) 504869(LOC504869) 505876(NEK3) 505945(LOC505945)
                 506060(LOC506060) 506063(MGC137117) 506083(LOC506083)
                 506433(LOC506433) 506520(LOC506520) 507414(LOC507414)
                 507624(LOC507624) 507689(EIF2AK1) 508208(LOC508208)
                 508325(SRPK3) 508408(LOC508408) 508424(LOC508424)
                 508668(LOC508668) 508735(MGC129043) 509656(PSKH1)
                 510158(MGC152387) 510342(LOC510342) 511190(MGC160087)
                 511296(GAK) 511373(MGC134048) 511455(MGC159441)
                 512154(LOC512154) 512233(LOC512233) 512236(MGC139658)
                 512631(LOC512631) 512740(LOC512740) 513432(LOC513432)
                 513539(LIMK2) 513673(LOC513673) 513678(LOC513678)
                 513994(LOC513994) 514777(MGC148432) 514787(STK38L)
                 515034(IRAK2) 515816(MGC149008) 515854(MGC166421)
                 516094(MGC128732) 516289(LOC516289) 517909(MGC139463)
                 518632(NUAK2) 518897(CHEK2) 519558(MINK) 520058(LOC520058)
                 520088(LOC520088) 520302(MGC133825) 521237(MGC137500)
                 522002(MAP4K1) 522613(LOC522613) 522917(RIOK3)
                 523490(LOC523490) 523542(MGC166392) 523998(MGC137163)
                 524218(LOC524218) 525506(LOC525506) 525647(MKNK1)
                 525675(MARK4) 526227(LOC526227) 526310(LOC526310)
                 526376(LOC526376) 526824(LOC526824) 526949(MGC139049)
                 527597(LOC527597) 527889(CSNK1G1) 528309(MGC139553)
                 529131(LOC529131) 529193(LOC529193) 532332(LOC532332)
                 532455(STK24-LIKE) 532546(LOC532546) 533677(MGC155151)
                 533692(MGC137816) 533897(LOC533897) 533908(MGC139400)
                 533953(IRAK1) 534230(LOC534230) 534407(RIPK2)
                 534526(LOC534526) 534620(LOC534620) 534684(RIPK5)
                 534705(LOC534705) 534872(LOC534872) 534923(LOC534923)
                 535197(MGC140219) 535342(LOC535342) 535625(LOC535625)
                 535652(LOC535652) 535824(LOC535824) 535868(LOC535868)
                 535935(LOC535935) 536051(LOC536051) 536110(LOC536110)
                 536123(LOC536123) 536532(LOC536532) 537027(LOC537027)
                 537517(LOC537517) 537640(LOC537640) 538009(LOC538009)
                 538519(LOC538519) 538659(LOC538659) 538770(LOC538770)
                 538866(LOC538866) 539224(LOC539224) 539235(LOC539235)
                 539477(LOC539477) 539563(LOC539563) 539627(LOC539627)
                 539707(LOC539707) 539742(MGC138047) 540072(LOC540072)
                 540206(LOC540206) 540207(ILK) 540421(ARAF) 540772(RIOK2)
                 540873(LOC540873) 540979(LOC540979) 613449(LOC613449)
                 615215(MAPKAPK3) 618599(LOC618599) 618601(MGC160050)
                 618880(VRK1) 619100(MGC159543)
            SSC: 396955(AURKB) 397588(PKR) 397601(ARAF1) 397618(OSR1)
                 574063(AURKA)
            MDO: 100024555(LOC100024555)
            GGA: 373922(LIMK1) 373929(MAPKAPK5) 373970(ROCK1) 374018(ILK)
                 374138(HIPK2) 374182(ROCK2) 374260(STT3A) 378801(STK25)
                 378891(CSNK1E) 378921(RIPK1) 378922(RCJMB04_19f17) 395133(SGK)
                 395147(EIF2AK2) 395171(RIPK5) 395360(EIF2AK1) 395376(PRKDC)
                 395401(ATM) 395499(TAOK3) 395924(CSNK1A1) 395928(AKT1)
                 396010(LIMK2) 396239(BRAF) 396245(RAF1) 415328(CSNK1G1)
                 415626(CSNK2A2) 415658(PSKH1) 415900(NEK4) 415917(MAPKAPK3)
                 415984(WNK2) 416118(RCJMB04_29d24) 416204(STK10)
                 416351(STK32A) 416588(PDPK1) 416734(PAK7) 416800(ULK1)
                 416914(LOC416914) 416952(BCR) 416984(CIT) 417101(NEK6)
                 417270(PRPF4) 417378(CSNK1D) 417576(NEK8) 417583(TAOK1)
                 417614(ULK2) 417637(RCJMB04_4j14) 417711(SRPK2)
                 417796(RCJMB04_17b10) 418074(NUAK1) 418217(RCJMB04_5c4)
                 418529(RIPK4) 418565(CASK) 418605(RPS6KA3) 418714(MAP4K4)
                 418780(RCJMB04_30a20) 418881(NEK5) 418903(DCLK1) 418949(LATS2)
                 419083(PAK1) 419166(SGK2) 419512(AAK1) 419828(NUAK2)
                 419847(MAPKAPK2) 419880(HIPK1) 419949(TLK2) 420020(LOC420020)
                 420130(MAST3) 420167(RCJMB04_16g8) 420215(RCJMB04_15n4)
                 420421(OXSR1) 420487(MASTL) 420494(MYO3A) 420675(SNRK)
                 420775(RCJMB04_1c13) 420870(RIOK1) 420879(RCJMB04_6j9)
                 421074(RIOK3) 421185(SRPK1) 421226(RCJMB04_5c21) 421342(MARK1)
                 421376(RCJMB04_1d15) 421497(AKT3) 421570(RPS6KA2)
                 421597(HIPK3) 421627(LATS1) 422273(RPS6KA6) 422342(PAK3)
                 422380(RCJMB04_3c16) 422433(NEK1) 422473(DCLK2) 422578(BMP2K)
                 422850(STK32B) 422930(EIF2AK3) 423045(RCJMB04_4a6)
                 423098(BRSK2) 423285(EIF2AK4) 423408(RPS6KA5) 423443(VRK1)
                 423480(MARK3) 423576(MAP4K5) 423878(SLK) 424049(RCJMB04_3f1)
                 424157(MYO3B) 424173(STK39) 424210(STK36) 424350(RCJMB04_11e2)
                 424369(UHMK1) 424507(CDC7) 424606(MAST2) 424845(PASK)
                 424860(PAK2) 425370(PINK1) 426442(SBK1) 427278(RIOK2)
                 427291(GAK) 427465(DAPK1) 427502(TRPM7) 427925(WNK1)
                 428145(TP53RK) 428167(AURKA) 428260(STK38)
                 428391(RCJMB04_7d18) 428449(RCJMB04_7f1) 428537(MOS)
                 428634(LOC428634) 428837(PAK6) 429001(TSSK6) 429024(TLK1)
                 429033(LOC429033) 429036(STK16) 429269(LOC429269)
                 429381(LOC429381) 429520(LRRK2) 431670(RCJMB04_1b10)
                 432370(CSNK2A1) 768913(CHEK2) 769291(STK32C) 770196(NEK3)
                 770440(VRK3) 770462(PAK4) 771376(TSSK3) 771724(STK35)
                 771961(MKNK1)
            XLA: 378923(Bub1b) 379165(MGC52943) 379176(MGC53195)
                 379177(MGC53202) 379624(ck1) 379626(myt1) 379783(akt2)
                 379800(vrk2) 379971(camk1) 380107(ankrd3) 380110(trc)
                 380117(mark2) 380238(csnk1a1) 380361(ckIdelta) 387327(mnk1)
                 394276(rps6kb1-A) 397857(c-raf) 397925(LOC397925) 398126(PAK1)
                 398191(LOC398191) 398224(PAK5) 398234(LOC398234)
                 398349(LOC398349) 398457(LOC398457) 398600(LOC398600)
                 398892(MGC68526) 399056(ARAF) 399068(MGC68447) 399130(Sgk)
                 399319(ck2a1) 399320(ck2b) 399355(wee1B) 399376(RSK2)
                 399395(MARK3) 414526(MGC81311) 414527(MGC81305)
                 414585(MGC83260) 414676(LOC414676) 414693(MGC83214)
                 414882(Nek7) 431807(MGC83745) 431882(MGC81497)
                 432004(MGC80023) 432084(MGC78852) 432161(MGC81183)
                 432172(MGC78893) 432180(MGC83125) 432197(MGC81103)
                 432201(MGC80341) 432258(MGC83541) 432315(MGC78994)
                 443729(RPS6KA1) 443942(MGC80293) 444075(MGC83537)
                 444083(MGC83575) 444087(MGC83604) 444155(MGC80614)
                 444414(MGC82989) 444447(MGC83646) 444618(MGC84110)
                 444676(MGC84283) 445821(MGC81220) 446555(mink) 446562(dapk1)
                 446640(ilk) 446749(stk39) 446771(osr1) 446778(MGC80412)
                 446880(riok3) 446996(cask) 447161(MGC85492) 447257(MGC86290)
                 447268(MGC86346) 447339(MGC83247) 447476(MGC81780)
                 447699(MGC81565) 447712(MGC81705) 495048(LOC495048)
                 495118(LOC495118) 495151(LOC495151) 495265(LOC495265)
                 495312(LOC495312) 495423(LOC495423) 495481(LOC495481)
                 495516(LOC495516) 496007(LOC496007) 496293(LOC496293)
            XTR: 394552(MGC75762) 394655(prpf4) 394689(TEgg020f01.1)
                 394938(rps6kb1) 407849(MGC76030) 407897(csnk1a1) 407902(stk39)
                 448012(MGC69350) 448124(csnk1g1) 448198(nek3) 448328(nek7)
                 448357(irak1) 448427(stk38l) 448471(MGC89575) 448643(mapkapk5)
                 448656(csnk2b) 448753(nek8) 493205(RIPK5) 493227(irak2)
                 493413(mknk1) 493442(csnk2a2) 493494(pim3) 496553(csnk1e)
                 548355(stk24) 548958(cask) 549104(gak) 549144(melk)
                 549214(LOC549214) 549324(aurka) 549335(cdc7) 549436(riok2)
                 549733(stk33) 549766(dapk3) 549784(pskh1) 549871(raf1)
                 550101(mapkapk3) 550105(srpk1) 594939(mark2) 594981(MGC107956)
                 779958(ripk1) 780181(MGC145460) 780207(MGC146781)
            DRE: 171094(nek8) 192306(stka) 192307(csnk1a1) 259195(cask)
                 266749(pak2) 280653(trpm7) 30428(ck2b) 30488(ck2a2)
                 30502(ck2a1) 30716(raf1) 30724(melk) 317747(rock2a)
                 322106(csnk1dl) 323679(srpk1) 324140(sgk) 324509(speg)
                 325034(zgc:113857) 325042(tnika) 326734(wu:fe11e12)
                 326944(prpf4) 327060(wee1) 327321(mapkapk2) 334167(zgc:55587)
                 334300(mark3) 334565(map4k5) 336998(zgc:55865) 337670(rps6kal)
                 338219(rps6ka3) 373103(pak1) 373121(mknk2) 373874(ripk2)
                 378972(akt2) 393132(irak4) 393162(zgc:56093) 393507(stk17b)
                 393513(zgc:66101) 393543(ilk) 393806(zgc:73231) 393957(stk38l)
                 393987(nek4) 394025(nek2) 394108(zgc:63495) 394145(vrk2)
                 394150(zgc:55494) 402814(myo3a) 402817(mos) 402922(ripk5)
                 403000(zgc:77318) 403063(zgc:92074) 403065(braf) 403146(akt2l)
                 405767(bsk146) 405898(pak7) 406268(riok1) 406349(rps6kb1)
                 406351(zgc:55705) 406533(csnk1d) 406600(stk25) 406694(vrk1)
                 406758(prpf4b) 406765(zgc:55572) 406786(zgc:66137)
                 406833(riok2) 407732(zgc:136697) 415254(zgc:86598)
                 431769(zgc:92014) 436608(mapkapk5) 436661(snrk) 436924(limk2)
                 445215(mastl) 445220(riok3) 445223(nek7) 445246(zgc:100912)
                 492768(zgc:101602) 494092(zgc:101563) 503703(pkz)
                 541443(zgc:113420) 548344(zgc:113355) 550323(zgc:112393)
                 553164(lats1) 553551(zgc:109932) 553571(zgc:110000)
                 554152(zgc:110719) 554840(zgc:113034) 554896(LOC554896)
                 555647(LOC555647) 555650(LOC555650) 555702(LOC555702)
                 555974(LOC555974) 556002(nek1) 556067(LOC556067)
                 556172(LOC556172) 556464(LOC556464) 557131(si:ch211-285c6.3)
                 557309(LOC557309) 557475(si:dkey-192d15.1)
                 557551(CH211-1E14.2) 557558(si:dkey-192d15.2)
                 557560(LOC557560) 557667(si:dkey-158b13.2) 557713(LOC557713)
                 557765(LOC557765) 557915(si:dkey-11n6.4) 558281(LOC558281)
                 558313(LOC558313) 558314(CH211-66I11.1) 558381(LOC558381)
                 558390(LOC558390) 558448(LOC558448) 558848(LOC558848)
                 558997(dclk1) 559050(zgc:154065) 559366(LOC559366)
                 559564(zgc:152949) 559792(LOC559792) 560226(LOC560226)
                 560275(LOC560275) 560549(LOC560549) 561159(si:ch211-240l19.1)
                 561496(LOC561496) 561563(si:dkey-261e22.1) 561724(zgc:153415)
                 561878(LOC561878) 561959(LOC561959) 562194(LOC562194)
                 562242(LOC562242) 562419(LOC562419) 562769(LOC562769)
                 564235(LOC564235) 564255(LOC564255) 564273(LOC564273)
                 564413(DKEY-21K24.2) 564523(zgc:162253) 564701(LOC564701)
                 564703(LOC564703) 565173(LOC565173) 565338(eif2ak1)
                 565462(LOC565462) 565679(LOC565679) 565828(CH211-208C6.6)
                 565957(LOC565957) 566214(LOC566214) 566605(LOC566605)
                 566628(LOC566628) 567006(LOC567006) 567283(LOC567283)
                 567460(si:ch211-241e1.1) 567617(LOC567617) 567674(LOC567674)
                 567770(LOC567770) 567874(CH211-158B22.3) 567888(LOC567888)
                 568080(stk35) 568320(si:dkey-83d9.7) 568602(zgc:165661)
                 568838(LOC568838) 569156(LOC569156) 569226(LOC569226)
                 569317(LOC569317) 569984(LOC569984) 570504(LOC570504)
                 571214(LOC571214) 571285(LOC571285) 571354(LOC571354)
                 571705(si:dkeyp-1e8.1) 572042(LOC572042) 572238(LOC572238)
                 572323(LOC572323) 572469(zgc:153997) 572901(LOC572901)
                 57929(stk19) 58054(pim1) 678631(zgc:136657)
            SPU: 373229(LOC373229) 373495(LOC373495) 574554(LOC574554)
                 575157(LOC575157) 575551(LOC575551) 575613(LOC575613)
                 575733(mnk1) 575764(LOC575764) 575899(LOC575899)
                 576091(LOC576091) 576140(LOC576140) 576342(LOC576342)
                 576359(LOC576359) 576569(LOC576569) 576586(LOC576586)
                 577188(LOC577188) 577477(LOC577477) 577602(LOC577602)
                 577755(LOC577755) 577885(LOC577885) 578120(LOC578120)
                 578274(LOC578274) 578600(LOC578600) 579202(LOC579202)
                 579218(LOC579218) 579320(LOC579320) 579505(LOC579505)
                 579511(LOC579511) 579979(LOC579979) 580315(LOC580315)
                 580385(LOC580385) 580563(LOC580563) 580976(LOC580976)
                 581062(LOC581062) 581288(LOC581288) 581333(LOC581333)
                 581345(LOC581345) 581399(LOC581399) 581490(LOC581490)
                 581714(LOC581714) 581730(LOC581730) 582192(LOC582192)
                 582803(LOC582803) 582897(LOC582897) 582923(LOC582923)
                 583309(LOC583309) 583376(LOC583376) 583941(LOC583941)
                 584463(LOC584463) 586101(LOC586101) 586937(LOC586937)
                 587307(LOC587307) 587664(LOC587664) 587733(LOC587733)
                 587817(LOC587817) 587829(LOC587829) 587831(LOC587831)
                 588704(LOC588704) 588904(LOC588904) 589762(LOC589762)
                 589861(LOC589861) 590257(LOC590257) 590401(LOC590401)
                 591473(LOC591473) 591674(LOC591674) 591895(LOC591895)
                 592325(LOC592325) 592974(Chk1) 593505(LOC593505)
                 594031(LOC594031) 594202(LOC594202) 594325(LOC594325)
                 752085(LOC752085) 754534(LOC754534) 761753(LOC761753)
            DME: Dmel_CG10295(Pak) Dmel_CG10504(Ilk) Dmel_CG10539(S6k)
                 Dmel_CG10951(niki) Dmel_CG10967(Atg1) Dmel_CG1107
                 Dmel_CG12072(wts) Dmel_CG13591(Ssl) Dmel_CG14030 Dmel_CG14217
                 Dmel_CG14305 Dmel_CG1609 Dmel_CG17090 Dmel_CG17161(grp)
                 Dmel_CG17256 Dmel_CG17520(CkIIalpha) Dmel_CG17596(S6kII)
                 Dmel_CG1848(LIMK1) Dmel_CG2028(CkIalpha) Dmel_CG2048(dco)
                 Dmel_CG2087 Dmel_CG2845(phl) Dmel_CG3086(MAPk-Ak2) Dmel_CG3105
                 Dmel_CG32417 Dmel_CG32742(l(1)G0148) Dmel_CG32782(tlk)
                 Dmel_CG4006 Dmel_CG4488 Dmel_CG4527(slik) Dmel_CG4583
                 Dmel_CG4945 Dmel_CG5125(ninaC) Dmel_CG5790 Dmel_CG6114
                 Dmel_CG6386(ball) Dmel_CG6498 Dmel_CG6551(fu)
                 Dmel_CG6703(Caki) Dmel_CG7177 Dmel_CG7693(fray) Dmel_CG8174
                 Dmel_CG8485 Dmel_CG8637(trc) Dmel_CG8866
                 Dmel_CG8914(CkIIbeta2) Dmel_CG9222 Dmel_CG9746
                 Dmel_CG9774(rok)
            CEL: B0205.7(kin-3) B0207.4(air-2) C03C10.1(kin-19)
                 C04A11.3(gck-4) C10C6.1(kin-4) C10H11.9(let-502)
                 C12D8.10(akt-1) C29F9.7(pat-4) C36B1.5 C41C4.4(ire-1)
                 C54G4.1(rskn-2) D2045.7 EEED8.9(pink-1) F15A2.6(sad-1)
                 F17E5.1(lin-2) F20B6.8(hpk-1) F22D6.5(prp-4) F28B12.3(vrk-1)
                 F28H6.1(akt-2) F35G12.3(sel-5) F35H8.7(wee-1.1) F46C3.1(pek-1)
                 F47F2.1 H39E23.1(par-1) H42K12.1(pdk-1) K12C11.4(dapk-1)
                 M03C11.1 R03D7.5 R06A10.4 R06C7.8(bub-1) R166.5(mnk-1)
                 T01G9.6(kin-10) T17E9.1(kin-18) T27C10.6(lrk-1) W03G1.6(pig-1)
                 W10G6.2(sgk-1) Y105E8B.3 Y106G6E.6(csnk-1) Y39G10AR.3
                 Y47D3A.16(rsks-1) Y59A8B.23(gck-3) Y60A3A.1(unc-51)
                 Y60A3A.12(chk-2) Y79H2A.11(zyg-8) ZC504.4(mig-15) ZC581.1
                 ZK524.4 ZK632.3 ZK930.1
            ATH: AT1G54510 AT1G72710 AT2G23070 AT2G23080 AT2G24990 AT2G32850
                 AT2G33560 AT2G37840 AT2G41500 AT3G04810 AT3G10540 AT3G20860
                 AT3G23340(CKL10) AT3G25840 AT3G44200 AT3G44850
                 AT3G45780(PHOT1) AT3G48190(ATM) AT3G50000(CKA2) AT3G51270
                 AT3G53930 AT3G59410 AT3G60250(CKB3) AT3G63280 AT4G16970
                 AT4G17640(CKB2) AT4G29380 AT5G04510(PDK1) AT5G20930(TSL)
                 AT5G26110 AT5G28290 AT5G38990 AT5G40820(ATR)
            OSA: 4324901 4324953 4327302 4327683 4328593 4332748 4332861
                 4333522 4333875 4334107 4334117 4334197 4334206 4336257
                 4337389 4338922 4339803 4342103 4342248 4342459 4342542
                 4343157 4343287 4346899 4352122
            CME: CMG167C CMK182C CMM005C CMN167C CMO271C CMP128C CMQ044C
                 CMQ173C CMR183C CMR193C CMS377C CMT481C CMT590C
            SCE: YBR097W(VPS15) YBR274W(CHK1) YDL017W(CDC7) YDL079C(MRK1)
                 YDR283C(GCN2) YGL019W(CKB1) YGL180W(ATG1) YGR188C(BUB1)
                 YHL007C(STE20) YHR079C(IRE1) YIL035C(CKA1) YJL187C(SWE1)
                 YKL126W(YPK1) YMR104C(YPK2) YMR216C(SKY1) YNL154C(YCK2)
                 YNL207W(RIO2) YOR039W(CKB2) YOR061W(CKA2) YOR119C(RIO1)
                 YPL204W(HRR25) YPL236C YPR178W(PRP4)
            AGO: AGOS_AAL083W AGOS_ABL028W AGOS_ABL166W AGOS_ABR014W
                 AGOS_ACL054W AGOS_ACR087C AGOS_ADL102C AGOS_ADL217W
                 AGOS_ADL316C AGOS_ADR204W AGOS_ADR293C AGOS_AEL149C
                 AGOS_AEL185C AGOS_AEL269C AGOS_AER216C AGOS_AER257W
                 AGOS_AER348C AGOS_AFL091W AGOS_AFL143C AGOS_AFR040W
                 AGOS_AGR163W AGOS_AGR315C
            PIC: PICST_33177(CHK1) PICST_33379 PICST_35896 PICST_37533
                 PICST_37961(CDC15) PICST_40055(ATG1) PICST_65270(YCK2)
                 PICST_67511(HRR25) PICST_69545(CKA1) PICST_79384(KIN3)
                 PICST_81982(CKB1) PICST_82126(RIO1) PICST_83851 PICST_83988
                 PICST_84188(CST20) PICST_86322(CKA2) PICST_89119(YCK1)
            CAL: CaO19.3561 CaO19.6913(GCN2) CaO19.7001 CaO19.7164
                 CaO19_2102(CaO19.2102) CaO19_4242(CaO19.4242)
                 CaO19_4297(CaO19.4297) CaO19_5068(CaO19.5068)
                 CaO19_5357(CaO19.5357) CaO19_7343(CaO19.7343)
            CGR: CAGL0A00275g CAGL0C05005g CAGL0E05720g CAGL0F08415g
                 CAGL0G02035g CAGL0G09845g CAGL0H00979g CAGL0H01199g
                 CAGL0H03553g CAGL0H04609g CAGL0H08019g CAGL0I00946g
                 CAGL0I04422g CAGL0I05192g CAGL0I08899g CAGL0J05940g
                 CAGL0K00693g CAGL0K01815g CAGL0K02673g CAGL0K03399g
                 CAGL0L06006g CAGL0L11594g
            SPO: SPAC10F6.10 SPAC167.01 SPAC1851.03(ckb1) SPAC19E9.02
                 SPAC20G4.03c SPAC222.07c SPAC227.12 SPAC23C11.11(cka1)
                 SPAC3H1.13 SPAP27G11.07c SPBC119.07 SPBC1347.06c(cki1)
                 SPBC1604.14c(pak1) SPBC1703.05 SPBC21C3.18(spo4) SPBC2G5.02c
                 SPBC36B7.09 SPBC3H7.15(hhp1) SPBC530.14c(dsk1) SPBC6B1.02
                 SPCC1259.13(chk1) SPCC1322.12c(bub1) SPCC18B5.03(wee1)
                 SPCC18B5.11c(cds1) SPCC24B10.07 SPCC576.15c(ksg1) SPCC63.08c
                 SPCC777.14(prp4)
            ANI: AN0038.2 AN0124.2 AN0235.2 AN0576.2 AN1272.2 AN1468.2
                 AN1476.2 AN1485.2 AN1632.2 AN2067.2 AN2246.2 AN2513.2 AN3110.2
                 AN3450.2 AN3946.2 AN4194.2 AN4279.2 AN4563.2 AN4936.2 AN5494.2
                 AN5757.2 AN5815.2 AN5822.2 AN5973.2 AN6363.2 AN7185.2 AN7321.2
                 AN7537.2 AN9504.2
            AFM: AFUA_1G01720 AFUA_1G05930 AFUA_1G09950 AFUA_2G02530
                 AFUA_2G07550 AFUA_2G07690 AFUA_2G10620 AFUA_2G14090
                 AFUA_2G16620 AFUA_3G02460 AFUA_3G05540 AFUA_3G10520
                 AFUA_3G12670 AFUA_3G14290 AFUA_4G03140 AFUA_4G06180
                 AFUA_4G09050 AFUA_5G04130 AFUA_5G05510 AFUA_5G06730
                 AFUA_5G06750 AFUA_5G08570 AFUA_5G11730 AFUA_5G12660
                 AFUA_6G02590 AFUA_6G02670 AFUA_6G06870 AFUA_6G08120
                 AFUA_6G09240 AFUA_6G11190 AFUA_6G13160 AFUA_7G03750
                 AFUA_7G04330 AFUA_8G04670 AFUA_8G04810
            AOR: AO090001000603 AO090003000068 AO090003000118 AO090003000267
                 AO090003000441 AO090003000598 AO090005000666 AO090005000934
                 AO090011000088 AO090011000574 AO090011000925 AO090011000937
                 AO090012000858 AO090020000026 AO090020000622 AO090023000312
                 AO090023000320 AO090023000496 AO090023000647 AO090023000971
                 AO090026000135 AO090026000593 AO090026000841 AO090038000436
                 AO090120000083 AO090120000152 AO090120000291 AO090120000393
                 AO090701000211
            CNE: CNA05390 CNB01690 CNB02900 CNB03020 CNC01960 CNC05730
                 CND05530 CND05790 CNE02360 CNF00140 CNF02800 CNG03850 CNG03960
                 CNG04000 CNI02840 CNJ01100 CNK01680 CNL06100 CNM01750 CNN01780
            UMA: UM00145.1 UM00274.1 UM00471.1 UM00484.1 UM00584.1 UM01033.1
                 UM01094.1 UM01110.1 UM02168.1 UM02406.1 UM03081.1 UM03796.1
                 UM03841.1 UM03973.1 UM04583.1 UM04732.1 UM05432.1 UM05726.1
                 UM06107.1 UM06142.1 UM06337.1 UM06363.1
            ECU: ECU05_1070 ECU05_1510 ECU07_0520 ECU08_1960 ECU09_1260
                 ECU10_0120 ECU10_1200i
            DDI: DDBDRAFT_0219417 DDB_0185025(casK) DDB_0185150(gskA)
                 DDB_0185178(atg1) DDB_0185182(cak1) DDB_0191195(pkbA)
                 DDB_0191365(pkgB) DDB_0191487(kinX) DDB_0191503(pats1)
                 DDB_0216243(pdkA) DDB_0216246(pdkB) DDB_0216254(aurB)
                 DDB_0216281(prpf4B) DDB_0216282(nek2) DDB_0216323(mrkC)
                 DDB_0216334(vps15) DDB_0216346 DDB_0216373 DDB_0216402(bud32)
                 DDB_0216428(rio1) DDB_0216429(rio2) DDB_0220003(nek3)
                 DDB_0220004 DDB_0220031(fhkC) DDB_0220652 DDB_0220702
                 DDB_0220709 DDB_0229345 DDB_0229350 DDB_0229382(tsuA)
                 DDB_0231210(cdc7) DDB_0231217(ireA) DDB_0231500(bub1)
                 DDB_0233058(prpf4)
            PFA: PF11_0048 PF11_0096 PF11_0156 PF11_0377 PF13_0232 PFD0975w
                 PFE1290w PFL1490w
            CPV: cgd3_1850 cgd3_3670 cgd5_2000 cgd7_2000 cgd7_440 cgd8_750
            CHO: Chro.30215 Chro.30219 Chro.50179 Chro.50272 Chro.60083
                 Chro.70230 Chro.80590
            TAN: TA03895 TA06180 TA06185 TA06530 TA10630 TA11250 TA12090
                 TA13995 TA20625 TA21325
            TPV: TP01_0303 TP01_0483 TP01_0880 TP01_0881 TP02_0241 TP02_0584
                 TP03_0315 TP04_0659 TP04_0848
            TET: TTHERM_00011890 TTHERM_00035510 TTHERM_00035550
                 TTHERM_00037530 TTHERM_00040360 TTHERM_00046660
                 TTHERM_00046680 TTHERM_00047740 TTHERM_00050510
                 TTHERM_00101380 TTHERM_00107120 TTHERM_00112910
                 TTHERM_00122330 TTHERM_00158430 TTHERM_00161100
                 TTHERM_00161570 TTHERM_00170550 TTHERM_00185770
                 TTHERM_00193700 TTHERM_00202780 TTHERM_00260770
                 TTHERM_00260780 TTHERM_00265180 TTHERM_00294650
                 TTHERM_00326840 TTHERM_00343420 TTHERM_00355550
                 TTHERM_00389910 TTHERM_00390000 TTHERM_00390060
                 TTHERM_00393030 TTHERM_00394590 TTHERM_00394690
                 TTHERM_00415780 TTHERM_00449170 TTHERM_00450990
                 TTHERM_00463090 TTHERM_00467740 TTHERM_00529780
                 TTHERM_00532000 TTHERM_00532680 TTHERM_00534050
                 TTHERM_00575520 TTHERM_00577090 TTHERM_00624260
                 TTHERM_00624920 TTHERM_00628440 TTHERM_00637810
                 TTHERM_00641080 TTHERM_00666380 TTHERM_00697500
                 TTHERM_00700970 TTHERM_00717780 TTHERM_00721400
                 TTHERM_00726040 TTHERM_00726440 TTHERM_00726480
                 TTHERM_00775960 TTHERM_00780530 TTHERM_00784290
                 TTHERM_00790580 TTHERM_00790590 TTHERM_00821800
                 TTHERM_00865320 TTHERM_00898280 TTHERM_00899480
                 TTHERM_00923040 TTHERM_00941510 TTHERM_00971920
                 TTHERM_00992970 TTHERM_01000150 TTHERM_01000180
                 TTHERM_01001430 TTHERM_01016020 TTHERM_01016070
                 TTHERM_01030010 TTHERM_01046870 TTHERM_01049260
                 TTHERM_01080610 TTHERM_01114180 TTHERM_01142670
                 TTHERM_01144900 TTHERM_01207660 TTHERM_01246760
                 TTHERM_01266090 TTHERM_01284760 TTHERM_01309100
                 TTHERM_01345780 TTHERM_01347900 TTHERM_01502010
            TBR: Tb09.211.4890 Tb10.70.7860 Tb11.01.0930 Tb11.01.2590
                 Tb11.02.2050 Tb11.02.5050 Tb11.03.0290 Tb927.2.2430
                 Tb927.3.3190 Tb927.3.5400 Tb927.4.5180 Tb927.5.800
                 Tb927.6.2840 Tb927.6.4970 Tb927.8.7220
            TCR: 503513.10 503757.40 504001.6 504929.10 506851.10 506925.260
                 506945.110 506945.220 507305.20 508153.400 508409.150
                 508541.230 510761.60 510901.120 511753.70
            LMA: LmjF02.0360 LmjF11.0060 LmjF13.0440 LmjF21.1565 LmjF28.1760
                 LmjF29.0240 LmjF29.2570 LmjF30.1360 LmjF30.3470 LmjF30.3580
                 LmjF34.2150 LmjF35.1010 LmjF35.1730 LmjF36.5090
            EHI: 100.t00021 120.t00016 144.t00004 16.t00063 169.t00007
                 183.t00019 186.t00021 192.t00015 2.t00008 203.t00017 23.t00059
                 3.t00149 394.t00006 4.t00082 429.t00007 53.t00023 6.t00006
                 61.t00012 7.t00025 90.t00001
            YPE: YPO1734
            YPK: y2574
            YPM: YP_1474(rIO1)
            YPA: YPA_1108
            YPN: YPN_2388
            YPS: YPTB1613
            ECA: ECA3207
            XCC: XCC0374
            XCB: XC_0386
            XCV: XCV0388
            XAC: XAC0374
            XOO: XOO0489
            XOM: XOO_0456(XOO0456)
            VFI: VFA1077
            PPR: PBPRA1235
            PAE: PA0074(ppkA) PA4780
            PAU: PA14_63200
            PPU: PP_2912
            PPF: Pput_1936 Pput_3596 Pput_4615
            PST: PSPTO_0748
            PSB: Psyr_0650
            PSP: PSPPH_4645
            PFL: PFL_0708
            PFO: Pfl_0658
            PEN: PSEEN0537(stk1)
            PMY: Pmen_3239
            SON: SO_3973
            SDN: Sden_1654
            SFR: Sfri_2139
            SBM: Shew185_1466
            SSE: Ssed_2387
            SHE: Shewmr4_0664
            SHM: Shewmr7_3358
            SHN: Shewana3_0663
            CPS: CPS_4795
            PHA: PSHAb0252
            PAT: Patl_3392
            SDE: Sde_1558
            CBD: COXBU7E912_1925(pkn2)
            MCA: MCA1685
            NOC: Noc_2977
            ABO: ABO_0084
            AHA: AHA_2103
            BMV: BMASAVP1_1598
            BXE: Bxe_B2078
            BPL: BURPS1106A_1873(prkA)
            BPD: BURPS668_1861(prkA)
            RFR: Rfer_4056
            POL: Bpro_1235 Bpro_3868
            MPT: Mpe_A1034 Mpe_A1493 Mpe_A1546 Mpe_A2951 Mpe_A2971
            HAR: HEAR0296 HEAR1012
            EBA: ebA56
            AZO: azo2041 azo2073(prkA) azo2585(yloP) azo3774 azo3908
            DAR: Daro_1866
            TBD: Tbd_0611
            HPA: HPAG1_0057
            GSU: GSU1426
            GME: Gmet_1228
            GUR: Gura_0598 Gura_4402
            PCA: Pcar_1875
            DDE: Dde_1722
            ADE: Adeh_0115 Adeh_2195 Adeh_3649
            AFW: Anae109_3229 Anae109_3304 Anae109_4057
            MXA: MXAN_0755(pkn9) MXAN_2680
            SAT: SYN_00228
            SFU: Sfum_2452
            PUB: SAR11_0057(rsbW)
            MLO: mlr2363
            SMD: Smed_5577 Smed_5757
            RET: RHE_PF00532
            RLE: RL1847
            BRA: BRADO1478(kaiC) BRADO2838 BRADO3982(kaiC)
            BBT: BBta_4356(kaiC) BBta_6554(kaiC)
            RDE: RD1_0027(rsbW)
            HNE: HNE_1246 HNE_1496 HNE_2144
            ABA: Acid345_0037 Acid345_2515
            BSU: BG10297(spoIIAB) BG10734(rsbW) BG12726(ybdM) BG13391(prkC)
            BHA: BH0528(rsbW) BH1537(spoIIAB) BH2504
            BAN: BA0991(rsbW) BA4000 BA4295(spoIIAB)
            BAR: GBAA0991(rsbW) GBAA4000 GBAA4295(spoIIAB)
            BAA: BA_1559 BA_4471 BA_4754
            BAT: BAS0927 BAS3713 BAS3984
            BCE: BC1003 BC3860 BC4073
            BCA: BCE_1085(rsbW) BCE_3904 BCE_4143(spoIIAB)
            BCZ: BCZK0895(rsbW) BCZK3621 BCZK3830(spoIIAB)
            BCY: Bcer98_1424 Bcer98_2772 Bcer98_3777
            BTK: BT9727_0912(rsbW) BT9727_3603 BT9727_3814(spoIIAB)
            BTL: BALH_0489(prkA) BALH_3493 BALH_3691
            BLI: BL00777(spoIIAB) BL02207(rsbW) BL02302(prkC)
            BLD: BLi00559(rsbW) BLi01798(prkC) BLi02496(spoIIAB)
            BCL: ABC0815(rsbW) ABC1794(spoIIAB) ABC2315(prkC)
            BPU: BPUM_0442(rsbT) BPUM_0445(rsbW) BPUM_2077(spoIIAB)
            OIH: OB0629 OB1509 OB1840(spoIIAB)
            GKA: GK1176 GK2309 GK3423
            GTN: GTNG_1029
            SAU: SA1063 SA1870(rsbW)
            SAV: SAV1220 SAV2065(rsbW)
            SAM: MW1103 MW1989(rsbW)
            SAR: SAR1196(pknB) SAR2153(rsbW)
            SAS: SAS1154 SAS1970
            SAC: SACOL2055(rsbW)
            SAB: SAB1084(pknB) SAB1950c(rsbW)
            SAA: SAUSA300_1113(pknB) SAUSA300_2023(rsbW)
            SAO: SAOUHSC_01187 SAOUHSC_02299
            SAJ: SaurJH9_1279 SaurJH9_2102
            SAH: SaurJH1_2139
            SEP: SE0895 SE1669
            SER: SERP0786 SERP1678(rsbW)
            SHA: SH0966(rsbW) SH1695
            SSP: SSP0812 SSP1552
            LMO: lmo0894(rsbW) lmo1820
            LMF: LMOf2365_0913 LMOf2365_1848
            LIN: lin0893(rsbW) lin1934
            LWE: lwe0876(rsbW) lwe1839
            LLA: L138452(pknB)
            LLC: LACR_2082
            LLM: llmg_2079(pknB)
            SPY: SPy_1625
            SPZ: M5005_Spy_1335
            SPM: spyM18_1634(pnk)
            SPG: SpyM3_1369
            SPS: SPs0493
            SPH: MGAS10270_Spy1451
            SPI: MGAS10750_Spy1444
            SPJ: MGAS2096_Spy1356
            SPK: MGAS9429_Spy1330
            SPF: SpyM50456(stk1)
            SPA: M6_Spy1381
            SPB: M28_Spy1376
            SPN: SP_1732
            SPR: spr1577(pkn2)
            SPD: SPD_1542
            SAG: SAG0319
            SAN: gbs0307
            SAK: SAK_0389(stk1)
            SMU: SMU.484(pknB)
            STC: str1425(pknB)
            STL: stu1425(pknB)
            SSA: SSA_1845(pkn)
            SSU: SSU05_0428
            SSV: SSU98_0415
            LPL: lp_1619(pkn1)
            LJO: LJ1537
            LAC: LBA1317
            LSA: LSA0692
            LDB: Ldb1409
            LBU: LBUL_1306
            LBR: LVIS_0962
            LCA: LSEI_1622
            LGA: LGAS_0764
            LRE: Lreu_1169
            EFA: EF3120
            OOE: OEOE_0789
            STH: STH1353 STH1813(spoIIAB)
            CAC: CAC0404 CAC1728 CAC2307
            CPE: CPE1738 CPE2049(spoIIAB)
            CPF: CPF_1541(prkA) CPF_1991 CPF_2306(spoIIAB)
            CPR: CPR_1334(prkA) CPR_1709 CPR_2021(spoIIAB)
            CTC: CTC01225 CTC02247
            CNO: NT01CX_1805(spoIIAB) NT01CX_2239
            CTH: Cthe_0574
            CDF: CD0771(spoIIAB)
            CBO: CBO3088(spoIIAB)
            CBA: CLB_3117(spoIIAB)
            CBH: CLC_2990(spoIIAB)
            CBF: CLI_3147(spoIIAB)
            CBE: Cbei_0813 Cbei_0972 Cbei_2643 Cbei_2671
            CKL: CKL_3155(spoIIAB)
            AMT: Amet_0594 Amet_2213 Amet_3791
            CHY: CHY_1478 CHY_1960
            DSY: DSY2303 DSY2685
            DRM: Dred_1714
            PTH: PTH_1781
            SWO: Swol_0614 Swol_1225
            CSC: Csac_1658 Csac_2076 Csac_2585
            TTE: TTE1316(rsbW3) TTE1500(sps1)
            MTA: Moth_0912 Moth_1497
            MTU: Rv0014c(pknB) Rv0015c(pknA) Rv0931c(pknD) Rv1266c(pknH)
                 Rv1743(pknE) Rv1746(pknF) Rv2088(pknJ) Rv2176(pknL)
                 Rv2914c(pknI) Rv3080c(pknK)
            MTC: MT0017 MT0018 MT0958 MT1304 MT1785 MT1788 MT2149 MT2232
                 MT2982 MT3165
            MBO: Mb0014c(pknB) Mb0015c(pknA) Mb0954c(pknDb) Mb1297c(pknH)
                 Mb1772(pknE) Mb1775(pknF) Mb2115(pknJ) Mb2198(pknL)
                 Mb2938c(pknI) Mb3107c(pknK)
            MBB: BCG_0044c(pknB) BCG_0045c(pknA) BCG_2935c(pknI)
            MLE: ML0016(pknB) ML0017(pknA) ML0897
            MPA: MAP0016c(pknB) MAP0018c(pknA) MAP1332(pknF) MAP1914(pknL)
                 MAP2504 MAP3387c(pknD)
            MAV: MAV_0017 MAV_0019 MAV_0432 MAV_1417 MAV_2162 MAV_4238
            MSM: MSMEG_0028 MSMEG_0030(pknA) MSMEG_0529 MSMEG_0886 MSMEG_1190
                 MSMEG_1200 MSMEG_1215 MSMEG_3677 MSMEG_4243 MSMEG_4366
                 MSMEG_5437 MSMEG_5513 MSMEG_6206
            MUL: MUL_0018(pknB) MUL_0019(pknA)
            MMC: Mmcs_0015 Mmcs_0016 Mmcs_3272 Mmcs_3400 Mmcs_4317 Mmcs_5007
                 Mmcs_5526
            MKM: Mkms_0023
            MJL: Mjls_0015
            CGL: NCgl0040(cgl0041) NCgl0041(cgl0042) NCgl2095(cgl2175)
            CGB: cg0057(pknB) cg0059(pknA) cg2388(pknL)
            CEF: CE0033 CE0034 CE2070
            CDI: DIP0053(pknB) DIP0054(pknA) DIP1615
            CJK: jk0037(pknB) jk0038(pknA) jk0733(pknL)
            NFA: nfa17330 nfa2870 nfa42450 nfa46660 nfa46670 nfa800 nfa810
            RHA: RHA1_ro00279 RHA1_ro00283 RHA1_ro00755 RHA1_ro01111
                 RHA1_ro01705 RHA1_ro02195 RHA1_ro02405 RHA1_ro02581
                 RHA1_ro02716 RHA1_ro03019 RHA1_ro03370 RHA1_ro03373
                 RHA1_ro03592 RHA1_ro03696 RHA1_ro03697 RHA1_ro04280
                 RHA1_ro05330 RHA1_ro05837 RHA1_ro06211 RHA1_ro06941
                 RHA1_ro08540 RHA1_ro08852 RHA1_ro08893 RHA1_ro10230
                 RHA1_ro10362 RHA1_ro10389 RHA1_ro11058 RHA1_ro11100
                 RHA1_ro11102 RHA1_ro11306(pknK2)
            SCO: SCO2110(pkaF) SCO3848(SCH69.18)
            SMA: SAV1157(pkn3) SAV4338(pkn11) SAV6092(pkn28)
            TWH: TWT216(pknB) TWT777(pknA)
            TWS: TW555 TW788
            LXX: Lxx00210(pknB) Lxx00220(pknA) Lxx15400(pkaF)
            PAC: PPA0184 PPA0729
            TFU: Tfu_1041 Tfu_3065 Tfu_3066
            FRA: Francci3_0044 Francci3_3077 Francci3_4185 Francci3_4435
                 Francci3_4436
            FAL: FRAAL0266 FRAAL0272 FRAAL0426 FRAAL0427 FRAAL1023 FRAAL1155
                 FRAAL1277 FRAAL1817 FRAAL1820 FRAAL3262 FRAAL3306 FRAAL4020
                 FRAAL4330 FRAAL4349 FRAAL4415 FRAAL4416 FRAAL4418 FRAAL4943
                 FRAAL5081 FRAAL5298 FRAAL5541 FRAAL5831 FRAAL6754(pknA)
                 FRAAL6755
            ACE: Acel_0019 Acel_0986
            KRA: Krad_1013
            SEN: SACE_0044(pknB) SACE_0045(pknA) SACE_0526(pknJ) SACE_1285
                 SACE_1710 SACE_1981 SACE_2091 SACE_3192(pknD) SACE_4652
                 SACE_4653 SACE_4654 SACE_4748 SACE_4851 SACE_5066 SACE_5728
                 SACE_5941 SACE_6615 SACE_7196 SACE_7332
            STP: Strop_3363
            BLO: BL0589(pknB)
            BAD: BAD_0038(pknB)
            RXY: Rxyl_0021 Rxyl_0943 Rxyl_2974
            LBJ: LBJ_1485(rsbW)
            LBL: LBL_1709(rsbW)
            SYN: sll0776(spkD) slr0599(spkC) slr1225(spkF) slr1443(spkE)
                 slr1697(spkB)
            SYC: syc0259_c syc0428_d syc0438_d
            SYF: Synpcc7942_1111 Synpcc7942_1121 Synpcc7942_1294
            SYD: Syncc9605_0116
            SYE: Syncc9902_0160
            SYG: sync_0122
            SYR: SynRCC307_1301(rsbW)
            SYX: SynWH7803_1352(rsbW)
            CYA: CYA_1882
            CYB: CYB_1515 CYB_1522
            TEL: tlr0551 tlr1326 tlr1460 tlr2432
            GVI: glr1552
            ANA: all1702 all4813(pknC) alr2412 alr3268 alr3423 alr3997
                 alr4366(pknA) alr4368(pknD)
            AVA: Ava_0220 Ava_0663 Ava_1700 Ava_2084 Ava_3308 Ava_3310
                 Ava_3443 Ava_4923
            PMT: PMT0154
            PMC: P9515_00761(hit)
            TER: Tery_4818
            SRU: SRU_1358
            FJO: Fjoh_1760 Fjoh_4008
            RRS: RoseRS_3359 RoseRS_3980
            RCA: Rcas_0671 Rcas_3328 Rcas_4148
            DRA: DR_2209 DR_A0335
            DGE: Dgeo_0361
            TMA: TM0733
            TPT: Tpet_0547
            MJA: MJ0444 MJ1073
            MMP: MMP0004 MMP0604
            MMZ: MmarC7_1619 MmarC7_1626
            MAE: Maeo_0594 Maeo_0761
            MVN: Mevan_1469 Mevan_1476
            MAC: MA0894 MA2518
            MBA: Mbar_A1785 Mbar_A2841
            MMA: MM_2013 MM_3081
            MBU: Mbur_0099 Mbur_0947
            MHU: Mhun_2464 Mhun_2603
            MTH: MTH1005
            MST: Msp_1337
            MKA: MK0514(RIO1_1) MK1000
            AFU: AF1804 AF2426
            HAL: VNG0179C VNG2233C
            HMA: rrnAC2036(pkn) rrnAC2476(prk2)
            HWA: HQ1420A(pkn) HQ3002A(prkA) HQ3003A(prkA) HQ3398A
            NPH: NP0248A NP1312A
            TAC: Ta0396m
            TVO: TVN1177
            PTO: PTO0252
            PHO: PH0512 PH1567
            PAB: PAB0405 PAB1013
            PFU: PF0364 PF1581
            TKO: TK0801 TK2250
            APE: APE_0751 APE_1602.1
            IHO: Igni_0675
            SSO: SSO0197 SSO2374
            STO: ST0233 ST0513
            SAI: Saci_0796 Saci_0965
            MSE: Msed_0654 Msed_1723
            PAI: PAE0680 PAE3474
            NEQ: NEQ460 NEQ464
STRUCTURES  PDB: 1MRY  1UL7  1WAK  2CKE  2CMW  2CN5  2CN8  2DWB  2EHB  2H34  
                 2H6D  2H9V  2HAK  2HOG  2HW6  2HW7  2HXL  2HXQ  2HY0  2HY8  
                 2I3S  2ILL  2IWI  2IZR  2IZS  2IZT  2IZU  2J0I  2J2I  2J4Z  
                 2J50  2J51  2J7T  2J8H  2J8O  2J90  2JBO  2JBP  2JD5  2JDO  
                 2JDR  2JFL  2JFM  2JII  2JO8  2NP8  2NRU  2NRY  2NZI  2O3P  
                 2O63  2O64  2O65  2OBJ  2OI4  2OIB  2OIC  2OID  2OKR  2ONL  
                 2OOX  2OOY  2OV2  2OXD  2OXX  2OXY  2OZA  2P3G  2PE0  2PE1  
                 2PE2  2PVR  2PZI  2PZY  2Q0N  2QKW  2QLV  2QME  2QNJ  2UUE  
                 2UV2  2UVM  2UW9  2UZR  2UZS  2V3S  2V62  2V8Q  2V92  2V9J  
                 2YWP  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.1
            ExPASy - ENZYME nomenclature database: 2.7.11.1
            ExplorEnz - The Enzyme Database: 2.7.11.1
            ERGO genome analysis and discovery system: 2.7.11.1
            BRENDA, the Enzyme Database: 2.7.11.1
///
ENTRY       EC 2.7.11.2                 Enzyme
NAME        [pyruvate dehydrogenase (acetyl-transferring)] kinase;
            PDH kinase;
            PDHK;
            PDK;
            PDK1;
            PDK2;
            PDK3;
            PDK4;
            pyruvate dehydrogenase kinase;
            pyruvate dehydrogenase kinase (phosphorylating);
            pyruvate dehydrogenase kinase activator protein;
            STK1
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[pyruvate dehydrogenase (acetyl-transferring)]
            phosphotransferase
REACTION    ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP +
            [pyruvate dehydrogenase (acetyl-transferring)] phosphate [RN:R03449]
ALL_REAC    R03449
SUBSTRATE   ATP [CPD:C00002];
            [pyruvate dehydrogenase (acetyl-transferring)] [CPD:C01256]
PRODUCT     ADP [CPD:C00008];
            [pyruvate dehydrogenase (acetyl-transferring)] phosphate
            [CPD:C01293]
COMMENT     The enzyme has no activating compound but is specific for its
            substrate. It is a mitochondrial enzyme associated with the pyruvate
            dehydrogenase complex in mammals. Phosphorylation inactivates EC
            1.2.4.1, pyruvate dehydrogenase (acetyl-transferring).
REFERENCE   1  [PMID:4401694]
  AUTHORS   Linn TC, Pelley JW, Pettit FH, Hucho F, Randall DD, Reed LJ.
  TITLE     -Keto acid dehydrogenase complexes. XV. Purification and properties
            of the component enzymes of the pyruvate dehydrogenase complexes
            from bovine kidney and heart.
  JOURNAL   Arch. Biochem. Biophys. 148 (1972) 327-42.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:3004826]
  AUTHORS   Reed LJ, Damuni Z, Merryfield ML.
  TITLE     Regulation of mammalian pyruvate and branched-chain alpha-keto acid
            dehydrogenase complexes by phosphorylation-dephosphorylation.
  JOURNAL   Curr. Top. Cell. Regul. 27 (1985) 41-9.
REFERENCE   3  [PMID:15629119]
  AUTHORS   Tovar-Mendez A, Hirani TA, Miernyk JA, Randall DD.
  TITLE     Analysis of the catalytic mechanism of pyruvate dehydrogenase
            kinase.
  JOURNAL   Arch. Biochem. Biophys. 434 (2005) 159-68.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   4  [PMID:15491151]
  AUTHORS   Bao H, Kasten SA, Yan X, Hiromasa Y, Roche TE.
  TITLE     Pyruvate dehydrogenase kinase isoform 2 activity stimulated by
            speeding up the rate of dissociation of ADP.
  JOURNAL   Biochemistry. 43 (2004) 13442-51.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:12631265]
  AUTHORS   Roche TE, Hiromasa Y, Turkan A, Gong X, Peng T, Yan X, Kasten SA,
            Bao H, Dong J.
  TITLE     Essential roles of lipoyl domains in the activated function and
            control of pyruvate dehydrogenase kinases and phosphatase isoform 1.
  JOURNAL   Eur. J. Biochem. 270 (2003) 1050-6.
  ORGANISM  human [GN:hsa], rat [GN:rno]
ORTHOLOGY   KO: K00898  pyruvate dehydrogenase kinase
GENES       HSA: 5163(PDK1) 5164(PDK2) 5165(PDK3) 5166(PDK4)
            PTR: 459743(PDK1) 468402(PDK2) 472448(PDK4)
            MMU: 18604(Pdk2) 228026(Pdk1) 236900(Pdk3) 27273(Pdk4)
            RNO: 116551(Pdk1) 296849(Pdk3) 81530(Pdk2) 89813(Pdk4)
            CFA: 476828(PDK1) 478801(LOC478801) 480868(PDK3) 482310(PDK4)
                 491075(PDK2)
            BTA: 507367(MGC166250) 510841(MGC166016) 524075(PDK2)
                 528655(LOC528655)
            GGA: 418595(PDK3) 420570(PDK4) 425178(LOC425178)
                 425972(RCJMB04_4o20)
            XLA: 379789(3j828) 398840(MGC68579) 432080(MGC81400)
                 494745(LOC494745)
            XTR: 448511(pdk4)
            DRE: 393971(pdk2) 555522(LOC555522) 555840(LOC555840)
                 560068(LOC560068) 561007(si:rp71-57j15.4)
            SPU: 587933(LOC587933)
            DME: Dmel_CG8808(Pdk)
            CEL: ZK370.5(Phosphoprotein)
            OSA: 4344039
            CME: CMR225C
            AGO: AGOS_AER270W
            CAL: CaO19_7281(CaO19.7281)
            SPO: SPAC644.11c
            ANI: AN6207.2
            AFM: AFUA_2G11900
            AOR: AO090026000452
            CNE: CNA00360
            TBR: Tb11.02.2390
            TCR: 509875.170
            LMA: LmjF24.0010
STRUCTURES  PDB: 2E0A  2PNR  2Q8F  2Q8G  2Q8H  2Q8I  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.2
            ExPASy - ENZYME nomenclature database: 2.7.11.2
            ExplorEnz - The Enzyme Database: 2.7.11.2
            ERGO genome analysis and discovery system: 2.7.11.2
            BRENDA, the Enzyme Database: 2.7.11.2
            CAS: 9074-01-5
///
ENTRY       EC 2.7.11.3                 Enzyme
NAME        dephospho-[reductase kinase] kinase;
            AMP-activated kinase;
            AMP-activated protein kinase kinase;
            hydroxymethylglutaryl coenzyme A reductase kinase kinase;
            hydroxymethylglutaryl coenzyme A reductase kinase kinase
            (phosphorylating);
            reductase kinase;
            reductase kinase kinase;
            STK30
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}
            phosphotransferase
REACTION    ATP + dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)]
            kinase} = ADP + {[hydroxymethylglutaryl-CoA reductase (NADPH)]
            kinase} [RN:R04589]
ALL_REAC    R04589
SUBSTRATE   ATP [CPD:C00002];
            dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}
PRODUCT     ADP [CPD:C00008];
            {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}
COMMENT     The enzyme is activated by AMP and is specific for its substrate.
            Phosphorylates and activates EC 2.7.11.31,
            [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase, that has been
            inactivated by EC 3.1.3.16, phosphoprotein phosphatase.
REFERENCE   1  [PMID:291971]
  AUTHORS   Beg ZH, Stonik JA, Brewer HB Jr.
  TITLE     Characterization and regulation of reductase kinase, a protein
            kinase that modulates the enzymic activity of
            3-hydroxy-3-methylglutaryl-coenzyme A reductase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 4375-9.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:666819]
  AUTHORS   Ingebritsen TS, Lee HS, Parker RA, Gibson DM.
  TITLE     Reversible modulation of the activities of both liver microsomal
            hydroxymethylglutaryl coenzyme A reductase and its inactivating
            enzyme. Evidence for regulation by
            phosphorylation-dephosphorylation.
  JOURNAL   Biochem. Biophys. Res. Commun. 81 (1978) 1268-77.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:3155737]
  AUTHORS   Beg ZH, Stonik JA, Brewer HB Jr.
  TITLE     Phosphorylation of hepatic 3-hydroxy-3-methylglutaryl coenzyme A
            reductase and modulation of its enzymic activity by
            calcium-activated and phospholipid-dependent protein kinase.
  JOURNAL   J. Biol. Chem. 260 (1985) 1682-7.
  ORGANISM  rat [GN:rno], human [GN:hsa]
REFERENCE   4  [PMID:2369897]
  AUTHORS   Clarke PR, Hardie DG.
  TITLE     Regulation of HMG-CoA reductase: identification of the site
            phosphorylated by the AMP-activated protein kinase in vitro and in
            intact rat liver.
  JOURNAL   EMBO. J. 9 (1990) 2439-46.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:8415689]
  AUTHORS   Sato R, Goldstein JL, Brown MS.
  TITLE     Replacement of serine-871 of hamster 3-hydroxy-3-methylglutaryl-CoA
            reductase prevents phosphorylation by AMP-activated kinase and
            blocks inhibition of sterol synthesis induced by ATP depletion.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 9261-5.
  ORGANISM  hamster
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.3
            ExPASy - ENZYME nomenclature database: 2.7.11.3
            ExplorEnz - The Enzyme Database: 2.7.11.3
            ERGO genome analysis and discovery system: 2.7.11.3
            BRENDA, the Enzyme Database: 2.7.11.3
            CAS: 72060-33-4
///
ENTRY       EC 2.7.11.4                 Enzyme
NAME        [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
            kinase;
            BCK;
            BCKD kinase;
            BCODH kinase;
            branched-chain alpha-ketoacid dehydrogenase kinase;
            branched-chain 2-oxo acid dehydrogenase kinase;
            branched-chain keto acid dehydrogenase kinase;
            branched-chain oxo acid dehydrogenase kinase (phosphorylating);
            STK2
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
            phosphotransferase
REACTION    ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
            = ADP + [3-methyl-2-oxobutanoate dehydrogenase
            (acetyl-transferring)] phosphate
ALL_REAC    (other) R03516
SUBSTRATE   ATP [CPD:C00002];
            [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
PRODUCT     ADP [CPD:C00008];
            [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
            phosphate
COMMENT     The enzyme has no activating compound but is specific for its
            substrate. It is a mitochondrial enzyme associated with the
            branched-chain 2-oxoacid dehydrogenase complex. Phosphorylation
            inactivates EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase
            (2-methylpropanoyl-transferring).
REFERENCE   1  [PMID:7142221]
  AUTHORS   Paxton R, Harris RA.
  TITLE     Isolation of rabbit liver branched chain alpha-ketoacid
            dehydrogenase and regulation by phosphorylation.
  JOURNAL   J. Biol. Chem. 257 (1982) 14433-9.
  ORGANISM  rabbit
REFERENCE   2  [PMID:10903321]
  AUTHORS   Wynn RM, Chuang JL, Cote CD, Chuang DT.
  TITLE     Tetrameric assembly and conservation in the ATP-binding domain of
            rat branched-chain alpha-ketoacid dehydrogenase kinase.
  JOURNAL   J. Biol. Chem. 275 (2000) 30512-9.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:12189132]
  AUTHORS   Chuang JL, Wynn RM, Chuang DT.
  TITLE     The C-terminal hinge region of lipoic acid-bearing domain of E2b is
            essential for domain interaction with branched-chain alpha-keto acid
            dehydrogenase kinase.
  JOURNAL   J. Biol. Chem. 277 (2002) 36905-8.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:9344245]
  AUTHORS   Popov KM, Hawes JW, Harris RA.
  TITLE     Mitochondrial alpha-ketoacid dehydrogenase kinases: a new family of
            protein kinases.
  JOURNAL   Adv. Second. Messenger. Phosphoprotein. Res. 31 (1997) 105-11.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K00905  [3-methyl-2-oxobutanoate dehydrogenase
                        (acetyl-transferring)] kinase
GENES       HSA: 10295(BCKDK)
            MMU: 12041(Bckdk)
            RNO: 29603(Bckdk)
            CFA: 479776(BCKDK)
            BTA: 505005(BCKDK)
            XLA: 432076(MGC78818)
            SPU: 574737(LOC574737)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.4
            ExPASy - ENZYME nomenclature database: 2.7.11.4
            ExplorEnz - The Enzyme Database: 2.7.11.4
            ERGO genome analysis and discovery system: 2.7.11.4
            BRENDA, the Enzyme Database: 2.7.11.4
            CAS: 82391-38-6
///
ENTRY       EC 2.7.11.5                 Enzyme
NAME        [isocitrate dehydrogenase (NADP+)] kinase;
            [isocitrate dehydrogenase (NADP+)] kinase;
            ICDH kinase/phosphatase;
            IDH kinase;
            IDH kinase/phosphatase;
            IDH-K/P;
            IDHK/P;
            isocitrate dehydrogenase kinase (phosphorylating);
            isocitrate dehydrogenase kinase/phosphatase;
            STK3
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[isocitrate dehydrogenase (NADP+)] phosphotransferase
REACTION    ATP + [isocitrate dehydrogenase (NADP+)] = ADP + [isocitrate
            dehydrogenase (NADP+)] phosphate [RN:R04401]
ALL_REAC    R04401
SUBSTRATE   ATP [CPD:C00002];
            [isocitrate dehydrogenase (NADP+)] [CPD:C04125]
PRODUCT     ADP [CPD:C00008];
            [isocitrate dehydrogenase (NADP+)] phosphate [CPD:C04564]
COMMENT     The enzyme has no activating compound but is specific for its
            substrate. Phosphorylates and inactivates EC 1.1.1.42, isocitrate
            dehydrogenase (NADP+).
REFERENCE   1  [PMID:6756316]
  AUTHORS   Wang JY, Koshland DE Jr.
  TITLE     The reversible phosphorylation of isocitrate dehydrogenase of
            Salmonella typhimurium.
  JOURNAL   Arch. Biochem. Biophys. 218 (1982) 59-67.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:8702587]
  AUTHORS   Miller SP, Karschnia EJ, Ikeda TP, LaPorte DC.
  TITLE     Isocitrate dehydrogenase kinase/phosphatase. Kinetic characteristics
            of the wild-type and two mutant proteins.
  JOURNAL   J. Biol. Chem. 271 (1996) 19124-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:11290745]
  AUTHORS   Singh SK, Matsuno K, LaPorte DC, Banaszak LJ.
  TITLE     Crystal structure of Bacillus subtilis isocitrate dehydrogenase at
            1.55 A. Insights into the nature of substrate specificity exhibited
            by Escherichia coli isocitrate dehydrogenase kinase/phosphatase.
  JOURNAL   J. Biol. Chem. 276 (2001) 26154-63.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:11258918]
  AUTHORS   Oudot C, Cortay JC, Blanchet C, Laporte DC, Di Pietro A, Cozzone AJ,
            Jault JM.
  TITLE     The &quot;catalytic&quot; triad of isocitrate dehydrogenase
            kinase/phosphatase from E. coli and its relationship with that found
            in eukaryotic protein kinases.
  JOURNAL   Biochemistry. 40 (2001) 3047-55.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map04010  MAPK signaling pathway
ORTHOLOGY   KO: K00906  [isocitrate dehydrogenase (NADP+)] kinase
            KO: K04412  serine/threonine kinase 3
GENES       HSA: 6788(STK3)
            PTR: 472829(STK3)
            MMU: 56274(Stk3)
            RNO: 65189(Stk3)
            CFA: 475045(STK3)
            XLA: 432210(MGC79096)
            DRE: 324125(stk3)
            EHI: 242.t00007
            ECO: b4016(aceK)
            ECJ: JW3976(aceK)
            ECE: Z5602(aceK)
            ECS: ECs4934
            ECC: c4974(aceK)
            ECI: UTI89_C4575(aceK)
            ECP: ECP_4226
            ECV: APECO1_2460(aceK)
            ECW: EcE24377A_4561(aceK)
            ECX: EcHS_A4251
            STY: STY4403(aceK)
            STT: t4113(aceK)
            SEC: SC4064(aceK)
            STM: STM4185(aceK)
            YPE: YPO3724(aceK)
            YPK: y0018(aceK)
            YPM: YP_3086(aceK)
            YPA: YPA_0019
            YPN: YPN_0016
            YPP: YPDSF_0175
            YPS: YPTB3655(aceK)
            YPI: YpsIP31758_0296(aceK)
            SBO: SBO_4036(aceK)
            SDY: SDY_4327(aceK)
            ECA: ECA3989(aceK)
            PLU: plu4394(aceK)
            ENT: Ent638_0220
            SPE: Spro_4501
            XCC: XCC3780(aceK)
            XCB: XC_3852
            XCV: XCV3958(aceK)
            XAC: XAC3832(aceK)
            PPR: PBPRA0551
            PAE: PA1376(aceK)
            PAU: PA14_46450(aceK)
            PPU: PP_4565(aceK)
            PPF: Pput_1324
            PFL: PFL_1530(aceK)
            PFO: Pfl_1419
            PEN: PSEEN4009(aceK)
            PMY: Pmen_1792
            ILO: IL0607(aceK)
            CPS: CPS_1118(aceK)
            PHA: PSHAa1307(aceK) PSHAa1821(aceK)
            PAT: Patl_0758
            AHA: AHA_3021(aceK)
            RSO: RSc0278(aceK)
            REU: Reut_A0136
            REH: H16_A0168(aceK)
            RME: Rmet_0104
            BMA: BMA0094(aceK)
            BMV: BMASAVP1_A3087(aceK)
            BML: BMA10299_A2008(aceK)
            BMN: BMA10247_2279(aceK)
            BVI: Bcep1808_3021
            BUR: Bcep18194_A6269
            BCN: Bcen_2312
            BCH: Bcen2424_2926
            BAM: Bamb_2975
            BPS: BPSL0373
            BPM: BURPS1710b_0581(aceK)
            BPL: BURPS1106A_0419(aceK)
            BPD: BURPS668_0398(aceK)
            BTE: BTH_I0346
            BPE: BP0445(aceK)
            BPA: BPP4360(aceK)
            BBR: BB4946(aceK)
            RFR: Rfer_3840
            POL: Bpro_4188
            PNA: Pnap_0457
            AAV: Aave_4369
            AJS: Ajs_3777
            MPT: Mpe_A3368
            EBA: ebA835(aceK)
            AZO: azo1145(aceK)
            DAR: Daro_3121
            ADE: Adeh_2039
            AFW: Anae109_1775
            RPA: RPA0347(aceK)
            RPB: RPB_0473
            RPD: RPD_0377
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.5
            ExPASy - ENZYME nomenclature database: 2.7.11.5
            ExplorEnz - The Enzyme Database: 2.7.11.5
            ERGO genome analysis and discovery system: 2.7.11.5
            BRENDA, the Enzyme Database: 2.7.11.5
            CAS: 83682-93-3
///
ENTRY       EC 2.7.11.6                 Enzyme
NAME        [tyrosine 3-monooxygenase] kinase;
            pheochromocytoma tyrosine hydroxylase-associated kinase;
            STK4;
            tyrosine 3-monooxygenase kinase (phosphorylating)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[tyrosine-3-monoxygenase] phosphotransferase
REACTION    ATP + [tyrosine-3-monooxygenase] = ADP +
            phospho-[tyrosine-3-monooxygenase]
ALL_REAC    (other) R04275
SUBSTRATE   ATP [CPD:C00002];
            [tyrosine-3-monooxygenase]
PRODUCT     ADP [CPD:C00008];
            phospho-[tyrosine-3-monooxygenase]
COMMENT     The enzyme has no activating compound but is specific for its
            substrate, with which it co-purifies. Requires Mg2+. Activates EC
            1.14.16.2, tyrosine 3-monooxygenase, by phosphorylation.
REFERENCE   1  [PMID:2872947]
  AUTHORS   Pigeon D, Drissi-Daoudi R, Gros F, Thibault J.
  TITLE     [Copurification of tyrosine hydroxylase from rat pheochromocytoma by
            protein kinase]
  JOURNAL   C. R. Acad. Sci. III. 302 (1986) 435-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:2883182]
  AUTHORS   Pigeon D, Ferrara P, Gros F, Thibault J.
  TITLE     Rat pheochromocytoma tyrosine hydroxylase is phosphorylated on
            serine 40 by an associated protein kinase.
  JOURNAL   J. Biol. Chem. 262 (1987) 6155-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map04010  MAPK signaling pathway
            PATH: map05223  Non-small cell lung cancer
ORTHOLOGY   KO: K04411  serine/threonine kinase 4
GENES       HSA: 6789(STK4)
            PTR: 458275(STK4)
            MMU: 58231(Stk4)
            RNO: 311622(Stk4_predicted)
            CFA: 477240(STK4)
            BTA: 514886(STK4)
            GGA: 419187(RCJMB04_17i1)
            XTR: 394860(stk4)
            SPU: 576378(LOC576378)
            DDI: DDB_0191170(krsA)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.6
            ExPASy - ENZYME nomenclature database: 2.7.11.6
            ExplorEnz - The Enzyme Database: 2.7.11.6
            ERGO genome analysis and discovery system: 2.7.11.6
            BRENDA, the Enzyme Database: 2.7.11.6
            CAS: 103537-12-8
///
ENTRY       EC 2.7.11.7                 Enzyme
NAME        myosin-heavy-chain kinase;
            ATP:myosin-heavy-chain O-phosphotransferase;
            calmodulin-dependent myosin heavy chain kinase;
            MHCK;
            MIHC kinase;
            myosin heavy chain kinase;
            myosin I heavy-chain kinase;
            myosin II heavy-chain kinase;
            [myosin-heavy-chain] kinase;
            myosin heavy chain kinase A;
            STK6
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[myosin heavy-chain] O-phosphotransferase
REACTION    ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate
ALL_REAC    (other) R04023
SUBSTRATE   ATP [CPD:C00002];
            [myosin heavy-chain]
PRODUCT     ADP [CPD:C00008];
            myosin heavy-chain phosphate [CPD:C03874]
COMMENT     The enzyme from Dictyostelium sp. (slime moulds) brings about
            phosphorylation of the heavy chains of Dictyostelium myosin,
            inhibiting the actin-activated ATPase activity of the myosin. One
            threonine residue in each heavy chain acts as acceptor. While the
            enzyme from some species is activated by actin, in other cases
            Ca2+/calmodulin are required for activity.
REFERENCE   1  [PMID:3027076]
  AUTHORS   Cote GP, Bukiejko U.
  TITLE     Purification and characterization of a myosin heavy chain kinase
            from Dictyostelium discoideum.
  JOURNAL   J. Biol. Chem. 262 (1987) 1065-72.
  ORGANISM  Dictyostelium discoideum [GN:ddi]
REFERENCE   2  [PMID:6309772]
  AUTHORS   Hammer JA 3rd, Albanesi JP, Korn ED.
  TITLE     Purification and characterization of a myosin I heavy chain kinase
            from Acanthamoeba castellanii.
  JOURNAL   J. Biol. Chem. 258 (1983) 10168-75.
  ORGANISM  Acanthamoeba castellanii
REFERENCE   3  [PMID:2822719]
  AUTHORS   Rieker JP, Swanljung-Collins H, Collins JH.
  TITLE     Purification and characterization of a calmodulin-dependent myosin
            heavy chain kinase from intestinal brush border.
  JOURNAL   J. Biol. Chem. 262 (1987) 15262-8.
  ORGANISM  chicken [GN:gga]
REFERENCE   4  [PMID:2549052]
  AUTHORS   Ravid S, Spudich JA.
  TITLE     Myosin heavy chain kinase from developed Dictyostelium cells.
            Purification and characterization.
  JOURNAL   J. Biol. Chem. 264 (1989) 15144-50.
  ORGANISM  Dictyostelium discoideum [GN:ddi]
REFERENCE   5  [PMID:2168881]
  AUTHORS   Brzeska H, Lynch TJ, Martin B, Corigliano-Murphy A, Korn ED.
  TITLE     Substrate specificity of Acanthamoeba myosin I heavy chain kinase as
            determined with synthetic peptides.
  JOURNAL   J. Biol. Chem. 265 (1990) 16138-44.
  ORGANISM  Acanthamoeba castellanii
REFERENCE   6  [PMID:1321427]
  AUTHORS   Ravid S, Spudich JA.
  TITLE     Membrane-bound Dictyostelium myosin heavy chain kinase: a
            developmentally regulated substrate-specific member of the protein
            kinase C family.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 5877-81.
  ORGANISM  Dictyostelium discoideum [GN:ddi]
REFERENCE   7  [PMID:7822274]
  AUTHORS   Futey LM, Medley QG, Cote GP, Egelhoff TT.
  TITLE     Structural analysis of myosin heavy chain kinase A from
            Dictyostelium. Evidence for a highly divergent protein kinase
            domain, an amino-terminal coiled-coil domain, and a domain
            homologous to the beta-subunit of heterotrimeric G proteins.
  JOURNAL   J. Biol. Chem. 270 (1995) 523-9.
  ORGANISM  Dictyostelium discoideum [GN:ddi]
REFERENCE   8  [PMID:9539704]
  AUTHORS   Szczepanowska J, Ramachandran U, Herring CJ, Gruschus JM, Qin J,
            Korn ED, Brzeska H.
  TITLE     Effect of mutating the regulatory phosphoserine and conserved
            threonine on the activity of the expressed catalytic domain of
            Acanthamoeba myosin I heavy chain kinase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 4146-51.
  ORGANISM  Acanthamoeba castellanii
REFERENCE   9  [PMID:15545285]
  AUTHORS   Egelhoff TT, Croft D, Steimle PA.
  TITLE     Actin activation of myosin heavy chain kinase A in Dictyostelium: a
            biochemical mechanism for the spatial regulation of myosin II
            filament disassembly.
  JOURNAL   J. Biol. Chem. 280 (2005) 2879-87.
  ORGANISM  Dictyostelium discoideum [GN:ddi]
ORTHOLOGY   KO: K08240  myosin-heavy-chain kinase
GENES       TBR: Tb927.4.4970 Tb927.8.7450
            TCR: 509011.100 510681.20
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.7
            ExPASy - ENZYME nomenclature database: 2.7.11.7
            ExplorEnz - The Enzyme Database: 2.7.11.7
            ERGO genome analysis and discovery system: 2.7.11.7
            BRENDA, the Enzyme Database: 2.7.11.7
            CAS: 64763-54-8
///
ENTRY       EC 2.7.11.8                 Enzyme
NAME        Fas-activated serine/threonine kinase;
            FAST;
            FASTK;
            STK10
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[Fas-activated serine/threonine protein] phosphotransferase
REACTION    ATP + [Fas-activated serine/threonine protein] = ADP +
            [Fas-activated serine/threonine phosphoprotein]
ALL_REAC    (other) R00162
SUBSTRATE   ATP [CPD:C00002];
            [Fas-activated serine/threonine protein]
PRODUCT     ADP [CPD:C00008];
            [Fas-activated serine/threonine phosphoprotein]
COMMENT     This enzyme is activated during Fas-mediated apoptosis. Following
            Fas ligation, the enzyme, which is constitutively phosphorylated, is
            dephosphorylated, and it is the dephosphorylated form that causes
            phosphorylation of TIA-1, a nuclear RNA-binding protein.
            Phosphorylation of TIA-1 precedes the onset of DNA fragmentation.
REFERENCE   1  [PMID:7544399]
  AUTHORS   Tian Q, Taupin J, Elledge S, Robertson M, Anderson P.
  TITLE     Fas-activated serine/threonine kinase (FAST) phosphorylates TIA-1
            during Fas-mediated apoptosis.
  JOURNAL   J. Exp. Med. 182 (1995) 865-74.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:15572676]
  AUTHORS   Li W, Simarro M, Kedersha N, Anderson P.
  TITLE     FAST is a survival protein that senses mitochondrial stress and
            modulates TIA-1-regulated changes in protein expression.
  JOURNAL   Mol. Cell. Biol. 24 (2004) 10718-32.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K08290  Fas-activated serine/threonine kinase
GENES       HSA: 10922(FASTK)
            PTR: 472626(FASTK)
            MMU: 66587(Fastk)
            RNO: 296741(Fastk)
            CFA: 482802(FASTK)
            BTA: 509781(FASTK)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.8
            ExPASy - ENZYME nomenclature database: 2.7.11.8
            ExplorEnz - The Enzyme Database: 2.7.11.8
            ERGO genome analysis and discovery system: 2.7.11.8
            BRENDA, the Enzyme Database: 2.7.11.8
///
ENTRY       EC 2.7.11.9                 Enzyme
NAME        Goodpasture-antigen-binding protein kinase;
            GPBPK;
            GPBP kinase;
            STK11;
            Goodpasture antigen-binding protein kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[Goodpasture antigen-binding protein] phosphotransferase
REACTION    ATP + [Goodpasture antigen-binding protein] = ADP + [Goodpasture
            antigen-binding phosphoprotein]
ALL_REAC    (other) R00162
SUBSTRATE   ATP [CPD:C00002];
            [Goodpasture antigen-binding protein]
PRODUCT     ADP [CPD:C00008];
            [Goodpasture antigen-binding phosphoprotein]
COMMENT     This serine/threonine kinase specifically binds to and
            phosphorylates the N-terminal region of the human Goodpasture
            antigen, which is located on the alpha3 chain of collagen IV and is
            involved in autoimmune disease.
REFERENCE   1  [PMID:10212244]
  AUTHORS   Raya A, Revert F, Navarro S, Saus J.
  TITLE     Characterization of a novel type of serine/threonine kinase that
            specifically phosphorylates the human goodpasture antigen.
  JOURNAL   J. Biol. Chem. 274 (1999) 12642-9.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:11007769]
  AUTHORS   Raya A, Revert-Ros F, Martinez-Martinez P, Navarro S, Rosello E,
            Vieites B, Granero F, Forteza J, Saus J.
  TITLE     Goodpasture antigen-binding protein, the kinase that phosphorylates
            the goodpasture antigen, is an alternatively spliced variant
            implicated in autoimmune pathogenesis.
  JOURNAL   J. Biol. Chem. 275 (2000) 40392-9.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04150  mTOR signaling pathway
            PATH: map04920  Adipocytokine signaling pathway
ORTHOLOGY   KO: K07298  serine/threonine-protein kinase 11
            KO: K08283  Goodpasture-antigen-binding protein kinase
GENES       HSA: 10087(COL4A3BP) 6794(STK11)
            PTR: 468641(STK11) 471515(COL4A3BP)
            MMU: 20869(Stk11) 68018(Col4a3bp)
            RNO: 314621(Stk11_predicted)
            CFA: 485088(STK11) 612799(COL4A3BP)
            BTA: 286797(COL4A3BP) 515245(LOC515245)
            GGA: 420105(STK11) 427209(COL4A3BP)
            XLA: 399100(XEEK1) 432007(MGC80009)
            XTR: 387331(col4a3bp) 549287(stk11)
            DRE: 550537(zgc:110180)
            SPU: 575272(LOC575272) 760252(LOC760252)
            DME: Dmel_CG7207 Dmel_CG9374
            CEL: F25H2.6 Y59A8B.14(par-4)
            CME: CMT325C
            DDI: DDB_0229349(lkb1)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.9
            ExPASy - ENZYME nomenclature database: 2.7.11.9
            ExplorEnz - The Enzyme Database: 2.7.11.9
            ERGO genome analysis and discovery system: 2.7.11.9
            BRENDA, the Enzyme Database: 2.7.11.9
///
ENTRY       EC 2.7.11.10                Enzyme
NAME        IkappaB kinase;
            CHUK;
            IKBKA;
            IKBKB;
            IKK;
            IKK-1;
            IKK-2;
            inhibitor of NFkappaB kinase;
            inhibitor of NF-kappaB kinase;
            STK12;
            TANK-binding kinase 1;
            TBK1
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[IkappaB protein] phosphotransferase
REACTION    ATP + [IkappaB protein] = ADP + [IkappaB phosphoprotein]
ALL_REAC    (other) R00162
SUBSTRATE   ATP [CPD:C00002];
            [IkappaB protein]
PRODUCT     ADP [CPD:C00008];
            [IkappaB phosphoprotein]
COMMENT     The enzyme phosphorylates IkappaB proteins at specific serine
            residues, which marks them for destruction via the ubiquitination
            pathway. Subsequent degradation of the IkB complex (IKK) activates
            NF-kappaB, a translation factor that plays an important role in
            inflammation, immunity, cell proliferation and apoptosis. If the
            serine residues are replaced by threonine residues, the activity of
            the enzyme is decreased considerably.
REFERENCE   1  [PMID:9244310]
  AUTHORS   Regnier CH, Song HY, Gao X, Goeddel DV, Cao Z, Rothe M.
  TITLE     Identification and characterization of an IkappaB kinase.
  JOURNAL   Cell. 90 (1997) 373-83.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:9346484]
  AUTHORS   Mercurio F, Zhu H, Murray BW, Shevchenko A, Bennett BL, Li J, Young
            DB, Barbosa M, Mann M, Manning A, Rao A.
  TITLE     IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for
            NF-kappaB activation.
  JOURNAL   Science. 278 (1997) 860-6.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:9346241]
  AUTHORS   Zandi E, Rothwarf DM, Delhase M, Hayakawa M, Karin M.
  TITLE     The IkappaB kinase complex (IKK) contains two kinase subunits,
            IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and
            NF-kappaB activation.
  JOURNAL   Cell. 91 (1997) 243-52.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:15653325]
  AUTHORS   Viatour P, Merville MP, Bours V, Chariot A.
  TITLE     Phosphorylation of NF-kappaB and IkappaB proteins: implications in
            cancer and inflammation.
  JOURNAL   Trends. Biochem. Sci. 30 (2005) 43-52.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04010  MAPK signaling pathway
            PATH: map04210  Apoptosis
            PATH: map04620  Toll-like receptor signaling pathway
            PATH: map04660  T cell receptor signaling pathway
            PATH: map04662  B cell receptor signaling pathway
            PATH: map04910  Insulin signaling pathway
            PATH: map04920  Adipocytokine signaling pathway
            PATH: map04930  Type II diabetes mellitus
            PATH: map05120  Epithelial cell signaling in Helicobacter pylori
                            infection
            PATH: map05212  Pancreatic cancer
            PATH: map05215  Prostate cancer
            PATH: map05220  Chronic myeloid leukemia
            PATH: map05221  Acute myeloid leukemia
            PATH: map05222  Small cell lung cancer
ORTHOLOGY   KO: K04467  inhibitor of nuclear factor kappa-B kinase alpha subunit
            KO: K05410  TANK-binding kinase 1
            KO: K07209  inhibitor of nuclear factor kappa-B kinase beta subunit
            KO: K07211  inhibitor of nuclear factor kappa-B kinase epsilon
                        subunit
GENES       HSA: 1147(CHUK) 29110(TBK1) 3551(IKBKB) 9641(IKBKE)
            PTR: 450673(CHUK) 452047(TBK1) 472749(IKBKB) 742813(IKBKE)
            MMU: 12675(Chuk) 16150(Ikbkb) 56480(Tbk1) 56489(Ikbke)
            RNO: 299827(LOC299827) 309361(Chuk_predicted)
                 363984(Ikbke_predicted) 84351(Ikbkb)
            CFA: 477796(CHUK) 478950(IKBKE) 481145(TBK1) 482839(IKBKB)
            BTA: 281073(CHUK) 281854(IKBKB) 533141(LOC533141)
                 533216(MGC137373)
            GGA: 417825(TBK1) 423669(RCJMB04_19h23) 426792(RCJMB04_29g15)
                 430480(IKBKE)
            XLA: 432200(MGC80376) 444556(MGC83432) 446351(tbk1)
            XTR: 448125(ikbkb) 549654(chuk)
            DRE: 393287(chuk) 437024(zgc:100844) 563560(LOC563560)
            SPU: 579073(LOC579073)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.10
            ExPASy - ENZYME nomenclature database: 2.7.11.10
            ExplorEnz - The Enzyme Database: 2.7.11.10
            ERGO genome analysis and discovery system: 2.7.11.10
            BRENDA, the Enzyme Database: 2.7.11.10
///
ENTRY       EC 2.7.11.11                Enzyme
NAME        cAMP-dependent protein kinase;
            AMPK;
            PKA;
            PKA C;
            protein kinase A;
            STK22
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:protein phosphotransferase (cAMP-dependent)
REACTION    ATP + a protein = ADP + a phosphoprotein [RN:R00162]
ALL_REAC    R00162
SUBSTRATE   ATP [CPD:C00002];
            protein [CPD:C00017]
PRODUCT     ADP [CPD:C00008];
            phosphoprotein [CPD:C00562]
COMMENT     CAMP is required to activate this enzyme. The inactive holoenzyme of
            cAMP-dependent protein kinase is a tetramer composed of two
            regulatory (R) and two catalytic (C) subunits. cAMP causes the
            dissociation of the inactive holoenzyme into a dimer of regulatory
            subunits bound to four cAMP molecules and two free monomeric
            catalytic subunits [i.e. R2C2 + 4 cAMP = R2(cAMP)4 + 2 C].
REFERENCE   1  [PMID:11705384]
  AUTHORS   Technikova-Dobrova Z, Sardanelli AM, Speranza F, Scacco S, Signorile
            A, Lorusso V, Papa S.
  TITLE     Cyclic adenosine monophosphate-dependent phosphorylation of
            mammalian mitochondrial proteins: enzyme and substrate
            characterization and functional role.
  JOURNAL   Biochemistry. 40 (2001) 13941-7.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:11278927]
  AUTHORS   Andersen MD, Shaffer J, Jennings PA, Adams JA.
  TITLE     Structural characterization of protein kinase A as a function of
            nucleotide binding. Hydrogen-deuterium exchange studies using
            matrix-assisted laser desorption ionization-time of flight mass
            spectrometry detection.
  JOURNAL   J. Biol. Chem. 276 (2001) 14204-11.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:3036817]
  AUTHORS   Johnson KE, Cameron S, Toda T, Wigler M, Zoller MJ.
  TITLE     Expression in Escherichia coli of BCY1, the regulatory subunit of
            cyclic AMP-dependent protein kinase from Saccharomyces cerevisiae.
            Purification and characterization.
  JOURNAL   J. Biol. Chem. 262 (1987) 8636-42.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4  [PMID:10699496]
  AUTHORS   Haq E, Sharma S, Khuller GK.
  TITLE     Purification and characterization of cAMP dependent protein kinase
            from Microsporum gypseum.
  JOURNAL   Biochim. Biophys. Acta. 1474 (2000) 100-6.
  ORGANISM  Microsporum gypseum
PATHWAY     PATH: map04010  MAPK signaling pathway
            PATH: map04020  Calcium signaling pathway
            PATH: map04140  Regulation of autophagy
            PATH: map04150  mTOR signaling pathway
            PATH: map04310  Wnt signaling pathway
            PATH: map04340  Hedgehog signaling pathway
            PATH: map04540  Gap junction
            PATH: map04720  Long-term potentiation
            PATH: map04740  Olfactory transduction
            PATH: map04742  Taste transduction
            PATH: map04910  Insulin signaling pathway
            PATH: map04912  GnRH signaling pathway
            PATH: map04914  Progesterone-mediated oocyte maturation
            PATH: map04916  Melanogenesis
            PATH: map04920  Adipocytokine signaling pathway
ORTHOLOGY   KO: K04345  protein kinase A
            KO: K07198  5'-AMP-activated protein kinase, catalytic alpha subunit
GENES       HSA: 5562(PRKAA1) 5563(PRKAA2) 5566(PRKACA) 5567(PRKACB)
                 5568(PRKACG) 5613(PRKX) 5616(PRKY)
            PTR: 469367(PRKACB) 472944(PRKACG)
            MMU: 105787(Prkaa1) 108079(Prkaa2) 18747(Prkaca) 18749(Prkacb)
                 19108(Prkx)
            RNO: 25636(Prkaca) 293508(Prkacb) 65248(Prkaa1) 78975(Prkaa2)
            CFA: 403556(PRKACA) 479351(PRKAA1) 479975(PRKACB) 489571(PRKAA2)
                 610031(PRKX)
            BTA: 282322(PRKACA) 282323(PRKACB) 538954(LOC538954)
                 540404(LOC540404)
            SSC: 397504(AMPKA2)
            GGA: 418656(PRKX) 424542(PRKACB) 427185(PRKAA1) 429110(PRKAA2)
            XLA: 380388(kin-1) 495290(LOC495290)
            XTR: 549157(prkaca)
            DRE: 393998(zgc:64054) 445076(zgc:91856) 563147(zgc:110804)
                 564064(zgc:158799)
            SPU: 589947(LOC589947)
            DME: Dmel_CG12066(Pka-C2) Dmel_CG3051(SNF1A) Dmel_CG4379(Pka-C1)
                 Dmel_CG6117(Pka-C3)
            CEL: T01C8.1(aak-2)
            SCE: YJL164C(TPK1) YKL166C(TPK3) YPL203W(TPK2)
            AGO: AGOS_AEL115C AGOS_AFL090W
            PIC: PICST_68202(TPK2)
            CAL: CaO19.2277
            CGR: CAGL0G09020g
            SPO: SPBC106.10(pka1)
            ANI: AN6305.2
            AFM: AFUA_2G12200
            AOR: AO090026000426
            CNE: CNA03840
            UMA: UM01124.1 UM04456.1
            DDI: DDB_0215408(pkaC)
            PFA: PFI1685w
            CHO: Chro.30344
            TAN: TA12860 TA14790
            TPV: TP02_0378
            TET: TTHERM_00433560 TTHERM_00992710 TTHERM_01020820
            TBR: Tb09.211.2360 Tb09.211.2410 Tb10.389.0490
            TCR: 508461.310 511269.50
            LMA: LmjF18.1080 LmjF35.3960 LmjF35.4010
            EHI: 4.t00093
STRUCTURES  PDB: 2GNF  2GNG  2GNH  2GNI  2GNJ  2GNL  2HWN  2IZX  2IZY  2JDS  
                 2JDT  2JDV  2OH0  2OJF  2UW3  2UW4  2UW5  2UW8  2UZT  2UZU  
                 2UZV  2UZW  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.11
            ExPASy - ENZYME nomenclature database: 2.7.11.11
            ExplorEnz - The Enzyme Database: 2.7.11.11
            ERGO genome analysis and discovery system: 2.7.11.11
            BRENDA, the Enzyme Database: 2.7.11.11
///
ENTRY       EC 2.7.11.12                Enzyme
NAME        cGMP-dependent protein kinase;
            3':5'-cyclic GMP-dependent protein kinase;
            cGMP-dependent protein kinase Ibeta;
            guanosine 3':5'-cyclic monophosphate-dependent protein kinase;
            PKG;
            PKG 1alpha;
            PKG 1beta;
            PKG II;
            STK23
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:protein phosphotransferase (cGMP-dependent)
REACTION    ATP + a protein = ADP + a phosphoprotein [RN:R00162]
ALL_REAC    R00162
SUBSTRATE   ATP [CPD:C00002];
            protein [CPD:C00017]
PRODUCT     ADP [CPD:C00008];
            phosphoprotein [CPD:C00562]
COMMENT     CGMP is required to activate this enzyme. The enzyme occurs as a
            dimer in higher eukaryotes. The C-terminal region of each
            polypeptide chain contains the catalytic domain that includes the
            ATP and protein substrate binding sites. This domain catalyses the
            phosphorylation by ATP to specific serine or threonine residues in
            protein substrates [3]. The enzyme also has two allosteric
            cGMP-binding sites (sites A and B). Binding of cGMP causes a
            conformational change that is associated with activation of the
            kinase [4].
REFERENCE   1  [PMID:186778]
  AUTHORS   Gill GN, Holdy KE, Walton GM, Kanstein CB.
  TITLE     Purification and characterization of 3':5'-cyclic GMP-dependent
            protein kinase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 73 (1976) 3918-22.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:15312978]
  AUTHORS   Murthy KS.
  TITLE     Modulation of soluble guanylate cyclase activity by phosphorylation.
  JOURNAL   Neurochem. Int. 45 (2004) 845-51.
REFERENCE   3  [PMID:12933804]
  AUTHORS   Richie-Jannetta R, Francis SH, Corbin JD.
  TITLE     Dimerization of cGMP-dependent protein kinase Ibeta is mediated by
            an extensive amino-terminal leucine zipper motif, and dimerization
            modulates enzyme function.
  JOURNAL   J. Biol. Chem. 278 (2003) 50070-9.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:9395542]
  AUTHORS   Zhao J, Trewhella J, Corbin J, Francis S, Mitchell R, Brushia R,
            Walsh D.
  TITLE     Progressive cyclic nucleotide-induced conformational changes in the
            cGMP-dependent protein kinase studied by small angle X-ray
            scattering in solution.
  JOURNAL   J. Biol. Chem. 272 (1997) 31929-36.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map04540  Gap junction
            PATH: map04730  Long-term depression
            PATH: map04740  Olfactory transduction
ORTHOLOGY   KO: K07376  protein kinase, cGMP-dependent
GENES       HSA: 5592(PRKG1) 5593(PRKG2)
            PTR: 461217(PRKG2)
            MMU: 19091(Prkg1) 19092(Prkg2)
            RNO: 25523(Prkg2) 54286(Prkg1_predicted)
            CFA: 487827(PRKG2) 609616(LOC609616)
            BTA: 282004(PRKG1) 533330(LOC533330)
            XLA: 444025(MGC82580)
            DRE: 394005(prkg1) 556339(LOC556339)
            SPU: 585077(LOC585077)
            DME: Dmel_CG10033(for) Dmel_CG3324(Pkg21D) Dmel_CG4839
            CEL: F55A8.2(egl-4)
            PFA: PF14_0346
            TET: TTHERM_00046530
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.12
            ExPASy - ENZYME nomenclature database: 2.7.11.12
            ExplorEnz - The Enzyme Database: 2.7.11.12
            ERGO genome analysis and discovery system: 2.7.11.12
            BRENDA, the Enzyme Database: 2.7.11.12
///
ENTRY       EC 2.7.11.13                Enzyme
NAME        protein kinase C;
            calcium-dependent protein kinase C;
            calcium-independent protein kinase C;
            calcium/phospholipid dependent protein kinase;
            cPKCalpha;
            cPKCbeta;
            cPKCgamma;
            nPKCdelta;
            nPKCepsilon;
            nPKC;
            nPKC;
            PKC;
            PKCalpha;
            PKCbeta;
            PKCgamma;
            PKCdelta;
            PKCepsilon;
            PKCzeta;
            Pkc1p;
            protein kinase Cepsilon;
            STK24
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:protein phosphotransferase (diacylglycerol-dependent)
REACTION    ATP + a protein = ADP + a phosphoprotein [RN:R00162]
ALL_REAC    R00162
SUBSTRATE   ATP [CPD:C00002];
            protein [CPD:C00017]
PRODUCT     ADP [CPD:C00008];
            phosphoprotein [CPD:C00562]
COMMENT     A family of serine- and threonine-specific protein kinases that
            depend on lipids for activity. They can be activated by calcium but
            have a requirement for the second messenger diacylglycerol. Members
            of this group of enzymes phosphorylate a wide variety of protein
            targets and are known to be involved in diverse cell-signalling
            pathways. Members of the protein kinase C family also serve as major
            receptors for phorbol esters, a class of tumour promoters.
REFERENCE   1  [PMID:2194521]
  AUTHORS   Jaken S.
  TITLE     Protein kinase C and tumor promoters.
  JOURNAL   Curr. Opin. Cell. Biol. 2 (1990) 192-7.
REFERENCE   2  [PMID:10675318]
  AUTHORS   Parekh DB, Ziegler W, Parker PJ.
  TITLE     Multiple pathways control protein kinase C phosphorylation.
  JOURNAL   EMBO. J. 19 (2000) 496-503.
  ORGANISM  mammalian
REFERENCE   3  [PMID:10604989]
  AUTHORS   Valledor AF, Xaus J, Comalada M, Soler C, Celada A.
  TITLE     Protein kinase C epsilon is required for the induction of
            mitogen-activated protein kinase phosphatase-1 in
            lipopolysaccharide-stimulated macrophages.
  JOURNAL   J. Immunol. 164 (2000) 29-37.
  ORGANISM  mouse [GN:mmu]
REFERENCE   4  [PMID:9480876]
  AUTHORS   Lendenfeld T, Kubicek CP.
  TITLE     Characterization and properties of protein kinase C from the
            filamentous fungus Trichoderma reesei.
  JOURNAL   Biochem. J. 330 ( Pt 2) (1998) 689-94.
  ORGANISM  Trichoderma reesei
REFERENCE   5  [PMID:9530509]
  AUTHORS   Brooks SP, Storey KB.
  TITLE     Protein kinase C from rainbow trout brain: identification and
            characterization of three isozymes.
  JOURNAL   Biochem. Mol. Biol. Int. 44 (1998) 259-67.
  ORGANISM  rainbow trout
PATHWAY     PATH: map04010  MAPK signaling pathway
            PATH: map04012  ErbB signaling pathway
            PATH: map04020  Calcium signaling pathway
            PATH: map04070  Phosphatidylinositol signaling system
            PATH: map04310  Wnt signaling pathway
            PATH: map04370  VEGF signaling pathway
            PATH: map04510  Focal adhesion
            PATH: map04530  Tight junction
            PATH: map04540  Gap junction
            PATH: map04650  Natural killer cell mediated cytotoxicity
            PATH: map04670  Leukocyte transendothelial migration
            PATH: map04720  Long-term potentiation
            PATH: map04730  Long-term depression
            PATH: map04910  Insulin signaling pathway
            PATH: map04916  Melanogenesis
            PATH: map05214  Glioma
            PATH: map05223  Non-small cell lung cancer
ORTHOLOGY   KO: K02677  classical protein kinase C
            KO: K06068  novel protein kinase C
            KO: K06069  atypical protein kinase C
            KO: K06070  protein kinase D
            KO: K06071  protein kinase N
GENES       HSA: 23683(PRKD3) 25865(PRKD2) 29941(PKN3) 5578(PRKCA)
                 5579(PRKCB1) 5580(PRKCD) 5581(PRKCE) 5582(PRKCG) 5583(PRKCH)
                 5584(PRKCI) 5585(PKN1) 5586(PKN2) 5587(PRKD1) 5588(PRKCQ)
                 5590(PRKCZ)
            PTR: 450143(PRKCI) 450288(PRKCQ) 452834(PRKD1) 455785(PKN1)
                 456998(PKN2) 459158(PRKD3) 468929(PRKD2)
            MMU: 101540(Prkd2) 109333(Pkn2) 18750(Prkca) 18751(Prkcb1)
                 18752(Prkcc) 18753(Prkcd) 18754(Prkce) 18755(Prkch)
                 18759(Prkci) 18760(Prkcm) 18761(Prkcq) 18762(Prkcz)
                 263803(Pkn3) 320795(Pkn1) 75292(Prkcn)
            RNO: 170538(Prkcd) 207122(Pkn2) 24680(Prkca) 24681(Prkcc)
                 25023(Prkcb1) 25522(Prkcz) 292658(Prkd2) 29340(Prkce)
                 29355(Pkn1) 296619(Pkn3) 313834(Prkcn) 60580(Hint1)
                 81749(Prkch) 84006(Prkci) 85420(PRKCQ) 85421(Prkcm)
            CFA: 478013(PRKCQ) 478686(PRKCI) 479577(PRKCZ) 483036(PRKD3)
                 484316(PRKCG) 484427(PRKD2) 484903(PKN1) 489968(PRKCB1)
                 490174(PKN2) 490722(PRKCH) 490904(PRKCA) 491313(PKN3)
                 494005(PRKCD) 609091(PRKD1)
            BTA: 282001(PRKCA) 282002(PRKCG) 282325(PRKCB1) 286877(PRKCZ)
                 505353(LOC505353) 505708(PRKCD) 509080(MGC142408)
                 519754(LOC519754) 528478(LOC528478) 533270(LOC533270)
                 538447(LOC538447)
            GGA: 415905(PRKCD) 416567(PRKCB1) 417430(RCJMB04_5a10)
                 419399(PRKCZ) 421478(PRKD3) 423302(RCJMB04_12k21)
                 423518(PRKCH) 424519(PKN2) 424991(RCJMB04_16p24)
            XLA: 404226(PKC-delta1) 444221(MGC80770) 447031(prkca)
                 447531(MGC83727)
            XTR: 503517(prkci)
            DRE: 117507(prkci) 334571(zgc:56558) 393953(prkcb1)
                 394004(prkcb1l) 555521(prkcq) 555737(prkcz) 557123(LOC557123)
                 557337(LOC557337) 560840(LOC560840) 567134(zgc:153916)
                 569086(LOC569086)
            SPU: 575375(LOC575375) 578578(LOC578578) 581257(LOC581257)
                 582022(LOC582022) 582463(LOC582463)
            DME: Dmel_CG10261(aPKC) Dmel_CG1954(Pkc98E) Dmel_CG2049(Pkn)
                 Dmel_CG6518(inaC) Dmel_CG6622(Pkc53E) Dmel_CG7125(PKD)
            CEL: B0545.1(tpa-1) E01H11.1(pkc-2) F09E5.1(pkc-3) F46F6.2
                 F57F5.5(pkc-1) T25E12.4 W09C5.5
            SCE: YBL105C(PKC1)
            AGO: AGOS_ACR191C
            PIC: PICST_81215
            CAL: CaO19_13322(CaO19.13322) CaO19_5901(CaO19.5901)
            CGR: CAGL0M09361g
            SPO: SPBC12D12.04c(pck2)
            ANI: AN0106.2
            AFM: AFUA_5G11970
            AOR: AO090120000316
            CNE: CNC03300
            PMF: P9303_03141(hit)
STRUCTURES  PDB: 2I0E  2UZP  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.13
            ExPASy - ENZYME nomenclature database: 2.7.11.13
            ExplorEnz - The Enzyme Database: 2.7.11.13
            ERGO genome analysis and discovery system: 2.7.11.13
            BRENDA, the Enzyme Database: 2.7.11.13
///
ENTRY       EC 2.7.11.14                Enzyme
NAME        rhodopsin kinase;
            cone opsin kinase;
            G-protein-coupled receptor kinase 1;
            GPCR kinase 1;
            GRK1;
            GRK7;
            opsin kinase;
            opsin kinase (phosphorylating);
            rhodopsin kinase (phosphorylating);
            RK;
            STK14
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:rhodopsin phosphotransferase
REACTION    ATP + rhodopsin = ADP + phosphorhodopsin [RN:R02903]
ALL_REAC    R02903
SUBSTRATE   ATP [CPD:C00002];
            rhodopsin [CPD:C00778]
PRODUCT     ADP [CPD:C00008];
            phosphorhodopsin [CPD:C02456]
INHIBITOR   Zinc [CPD:C00038];
            Digitonin [CPD:C00765]
COMMENT     Requires G-protein for activation and therefore belongs to the
            family of G-protein-dependent receptor kinases (GRKs). Acts on the
            bleached or activated form of rhodopsin; also phosphorylates the
            beta-adrenergic receptor, but more slowly. Does not act on casein,
            histones or phosphvitin. Inhibited by Zn2+ and digitonin (cf. EC
            2.7.11.15, beta-adrenergic-receptor kinase and EC 2.7.11.16,
            G-protein-coupled receptor kinase).
REFERENCE   1  [PMID:3014340]
  AUTHORS   Benovic JL, Mayor F Jr, Somers RL, Caron MG, Lefkowitz RJ.
  TITLE     Light-dependent phosphorylation of rhodopsin by beta-adrenergic
            receptor kinase.
  JOURNAL   Nature. 321 (1986) 869-72.
REFERENCE   2  [PMID:690139]
  AUTHORS   Shichi H, Somers RL.
  TITLE     Light-dependent phosphorylation of rhodopsin. Purification and
            properties of rhodopsin kinase.
  JOURNAL   J. Biol. Chem. 253 (1978) 7040-6.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:2844754]
  AUTHORS   Palczewski K, McDowell JH, Hargrave PA.
  TITLE     Purification and characterization of rhodopsin kinase.
  JOURNAL   J. Biol. Chem. 263 (1988) 14067-73.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:164024]
  AUTHORS   Weller M, Virmaux N, Mandel P.
  TITLE     Light-stimulated phosphorylation of rhodopsin in the retina: the
            presence of a protein kinase that is specific for photobleached
            rhodopsin.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 72 (1975) 381-5.
  ORGANISM  cow [GN:bta]
REFERENCE   5  [PMID:9380677]
  AUTHORS   Cha K, Bruel C, Inglese J, Khorana HG.
  TITLE     Rhodopsin kinase: expression in baculovirus-infected insect cells,
            and characterization of post-translational modifications.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 10577-82.
  ORGANISM  cow [GN:bta]
REFERENCE   6  [PMID:8812493]
  AUTHORS   Khani SC, Abitbol M, Yamamoto S, Maravic-Magovcevic I, Dryja TP.
  TITLE     Characterization and chromosomal localization of the gene for human
            rhodopsin kinase.
  JOURNAL   Genomics. 35 (1996) 571-6.
  ORGANISM  human [GN:hsa]
REFERENCE   7  [PMID:11754336]
  AUTHORS   Chen CK, Zhang K, Church-Kopish J, Huang W, Zhang H, Chen YJ,
            Frederick JM, Baehr W.
  TITLE     Characterization of human GRK7 as a potential cone opsin kinase.
  JOURNAL   Mol. Vis. 7 (2001) 305-13.
  ORGANISM  human [GN:hsa]
REFERENCE   8  [PMID:14654303]
  AUTHORS   Willets JM, Challiss RA, Nahorski SR.
  TITLE     Non-visual GRKs: are we seeing the whole picture?
  JOURNAL   Trends. Pharmacol. Sci. 24 (2003) 626-33.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K00909  G protein-coupled receptor kinase 1
GENES       HSA: 131890(GRK7) 6011(GRK1)
            PTR: 470950(GRK7)
            MMU: 24013(Grk1)
            RNO: 81760(Grk1)
            CFA: 485557(LOC485557) 485693(GRK7)
            BTA: 281457(RHOK) 281802(GPRK7)
            SSC: 397114(GPRK7)
            GGA: 395431(GRK1) 429125(GRK7)
            DRE: 373871(grk7b) 550406(grk1b) 564152(grk1a) 564282(LOC564282)
                 566120(grk7a)
            TET: TTHERM_00013270 TTHERM_00016020 TTHERM_00040400
                 TTHERM_00047570 TTHERM_00077610 TTHERM_00105520
                 TTHERM_00320440 TTHERM_00571930 TTHERM_00624250
                 TTHERM_00717760 TTHERM_00865280 TTHERM_01055410
                 TTHERM_01513280
STRUCTURES  PDB: 2I94  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.14
            ExPASy - ENZYME nomenclature database: 2.7.11.14
            ExplorEnz - The Enzyme Database: 2.7.11.14
            ERGO genome analysis and discovery system: 2.7.11.14
            BRENDA, the Enzyme Database: 2.7.11.14
            CAS: 54004-64-7
///
ENTRY       EC 2.7.11.15                Enzyme
NAME        beta-adrenergic-receptor kinase;
            ATP:beta-adrenergic-receptor phosphotransferase;
            [beta-adrenergic-receptor] kinase;
            beta-adrenergic receptor-specific kinase;
            beta-AR kinase;
            beta-ARK;
            beta-ARK 1;
            beta-ARK 2;
            beta-receptor kinase;
            GRK2;
            GRK3;
            beta-adrenergic-receptor kinase (phosphorylating);
            beta2ARK;
            betaARK1;
            beta-adrenoceptor kinase;
            beta-adrenoceptor kinase 1;
            beta-adrenoceptor kinase 2;
            ADRBK1;
            BARK1;
            adrenergic receptor kinase;
            STK15
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[beta-adrenergic receptor] phosphotransferase
REACTION    ATP + [beta-adrenergic receptor] = ADP + phospho-[beta-adrenergic
            receptor] [RN:R03274]
ALL_REAC    R03274
SUBSTRATE   ATP [CPD:C00002];
            beta-adrenergic receptor [CPD:C01141]
PRODUCT     ADP [CPD:C00008];
            phospho-beta-adrenergic receptor [CPD:C04141]
INHIBITOR   Zinc [CPD:C00038];
            Digitonin [CPD:C00765]
COMMENT     Requires G-protein for activation and therefore belongs to the
            family of G-protein-dependent receptor kinases (GRKs). Acts on the
            agonist-occupied form of the receptor; also phosphorylates
            rhodopsin, but more slowly. Does not act on casein or histones. The
            enzyme is inhibited by Zn2+ and digitonin but is unaffected by
            cyclic-AMP (cf. EC 2.7.11.14, rhodopsin kinase and EC 2.7.11.16,
            G-protein-coupled receptor kinase).
REFERENCE   1  [PMID:87250541]
  AUTHORS   Benovic JL, Mayor F Jr, Staniszewski C, Lefkowitz RJ, Caron MG.
  TITLE     Purification and characterization of the beta-adrenergic receptor
            kinase.
  JOURNAL   J. Biol. Chem. 262 (1987) 9026-32.
REFERENCE   2  [PMID:8394172]
  AUTHORS   Kim CM, Dion SB, Onorato JJ, Benovic JL.
  TITLE     Expression and characterization of two beta-adrenergic receptor
            kinase isoforms using the baculovirus expression system.
  JOURNAL   Receptor. 3 (1993) 39-55.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:9349395]
  AUTHORS   Laugwitz KL, Kronsbein K, Schmitt M, Hoffmann K, Seyfarth M, Schomig
            A, Ungerer M.
  TITLE     Characterization and inhibition of beta-adrenergic receptor kinase
            in intact myocytes.
  JOURNAL   Cardiovasc. Res. 35 (1997) 324-33.
  ORGANISM  rat [GN:rno], hamster
REFERENCE   4  [PMID:7559596]
  AUTHORS   Ferguson SS, Menard L, Barak LS, Koch WJ, Colapietro AM, Caron MG.
  TITLE     Role of phosphorylation in agonist-promoted beta 2-adrenergic
            receptor sequestration. Rescue of a sequestration-defective mutant
            receptor by beta ARK1.
  JOURNAL   J. Biol. Chem. 270 (1995) 24782-9.
  ORGANISM  cow [GN:bta]
REFERENCE   5  [PMID:14654303]
  AUTHORS   Willets JM, Challiss RA, Nahorski SR.
  TITLE     Non-visual GRKs: are we seeing the whole picture?
  JOURNAL   Trends. Pharmacol. Sci. 24 (2003) 626-33.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K00910  beta-adrenergic-receptor kinase
GENES       HSA: 156(ADRBK1) 157(ADRBK2)
            PTR: 451363(ADRBK1)
            MMU: 110355(Adrbk1)
            RNO: 25238(Adrbk1) 25372(Adrbk2)
            CFA: 483701(ADRBK1) 486327(ADRBK2)
            BTA: 282136(ADRBK2) 282682(ADRBK1)
            GGA: 416904(ADRBK2) 426000(RCJMB04_19g20)
            DRE: 569403(LOC569403)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.15
            ExPASy - ENZYME nomenclature database: 2.7.11.15
            ExplorEnz - The Enzyme Database: 2.7.11.15
            ERGO genome analysis and discovery system: 2.7.11.15
            BRENDA, the Enzyme Database: 2.7.11.15
            CAS: 102925-39-3
///
ENTRY       EC 2.7.11.16                Enzyme
NAME        G-protein-coupled receptor kinase;
            G protein-coupled receptor kinase;
            GPCR kinase;
            GPCRK;
            GRK4;
            GRK5;
            GRK6;
            STK16
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[G-protein-coupled receptor] phosphotransferase
REACTION    ATP + [G-protein-coupled receptor] = ADP + [G-protein-coupled
            receptor] phosphate
SUBSTRATE   ATP [CPD:C00002];
            [G-protein-coupled receptor]
PRODUCT     ADP [CPD:C00008];
            [G-protein-coupled receptor] phosphate
COMMENT     Requires G-protein for activation and therefore belongs to the
            family of G-protein-dependent receptor kinases (GRKs). All members
            of this enzyme subfamily possess a highly conserved binding site for
            1-phosphatidylinositol 4,5-bisphosphate. (cf. EC 2.7.11.14,
            rhodopsin kinase and EC 2.7.11.15, beta-adrenergic-receptor kinase).
REFERENCE   1  [PMID:8288567]
  AUTHORS   Kunapuli P, Onorato JJ, Hosey MM, Benovic JL.
  TITLE     Expression, purification, and characterization of the G
            protein-coupled receptor kinase GRK5.
  JOURNAL   J. Biol. Chem. 269 (1994) 1099-105.
  ORGANISM  cow [GN:bta], human [GN:hsa]
REFERENCE   2  [PMID:8120045]
  AUTHORS   Premont RT, Koch WJ, Inglese J, Lefkowitz RJ.
  TITLE     Identification, purification, and characterization of GRK5, a member
            of the family of G protein-coupled receptor kinases.
  JOURNAL   J. Biol. Chem. 269 (1994) 6832-41.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:14654303]
  AUTHORS   Willets JM, Challiss RA, Nahorski SR.
  TITLE     Non-visual GRKs: are we seeing the whole picture?
  JOURNAL   Trends. Pharmacol. Sci. 24 (2003) 626-33.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K08291  G protein-coupled receptor kinase
GENES       HSA: 2868(GRK4) 2869(GRK5) 2870(GRK6)
            PTR: 461082(GRK4) 471760(GRK6)
            MCC: 700000(GRK6)
            MMU: 14772(Grk4) 14773(Grk5) 26385(Grk6)
            RNO: 59075(Gprk5) 59076(Gprk6) 59077(Gprk2l)
            CFA: 479075(GRK4) 486915(GRK5)
            BTA: 281801(GPRK5) 512489(LOC512489)
            GGA: 416361(GRK6) 422879(GRK4) 423929(GRK5)
            XLA: 446831(gprk4-a) 447337(MGC83187) 474158(gprk4-b)
            XTR: 448587(grk4) 550070(LOC550070)
            DRE: 560761(zgc:153020) 561288(LOC561288) 567452(LOC567452)
            SPU: 593171(LOC593171)
            DME: Dmel_CG17998(Gprk2)
            CEL: F19C6.1(grk-1)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.16
            ExPASy - ENZYME nomenclature database: 2.7.11.16
            ExplorEnz - The Enzyme Database: 2.7.11.16
            ERGO genome analysis and discovery system: 2.7.11.16
            BRENDA, the Enzyme Database: 2.7.11.16
///
ENTRY       EC 2.7.11.17                Enzyme
NAME        Ca2+/calmodulin-dependent protein kinase;
            ATP:caldesmon O-phosphotransferase;
            caldesmon kinase;
            caldesmon kinase (phosphorylating);
            Ca2+/calmodulin-dependent microtubule-associated protein 2 kinase;
            Ca2+/calmodulin-dependent protein kinase 1;
            Ca2+/calmodulin-dependent protein kinase II;
            Ca2+/calmodulin-dependent protein kinase IV;
            Ca2+/calmodulin-dependent protein kinase kinase;
            Ca2+/calmodulin-dependent protein kinase kinase beta;
            calmodulin-dependent kinase II;
            CaM kinase;
            CaM kinase II;
            CAM PKII;
            CaM-regulated serine/threonine kinase;
            CaMKI;
            CaMKII;
            CaMKIV;
            CaMKKalpha;
            CaMKKbeta;
            microtubule-associated protein 2 kinase;
            STK20
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:protein phosphotransferase (Ca2+/calmodulin-dependent)
REACTION    ATP + a protein = ADP + a phosphoprotein
ALL_REAC    (other) R00162
SUBSTRATE   ATP [CPD:C00002];
            protein [CPD:C00017]
PRODUCT     ADP [CPD:C00008];
            phosphoprotein [CPD:C00562]
COFACTOR    Calcium [CPD:C00076];
            Calmodulin [CPD:C00391]
EFFECTOR    Calcium [CPD:C00076];
            Calmodulin [CPD:C00391]
COMMENT     Requires calmodulin and Ca2+ for activity. A wide range of proteins
            can act as acceptor, including vimentin, synapsin, glycogen
            synthase, myosin light chains and the microtubule-associated tau
            protein. Not identical with EC 2.7.11.18 (myosin-light-chain kinase)
            or EC 2.7.11.26 (tau-protein kinase).
REFERENCE   1  [PMID:3040904]
  AUTHORS   Adlersberg M, Liu KP, Hsiung SC, Ehrlich Y, Tamir H.
  TITLE     A Ca2+-dependent protein kinase activity associated with serotonin
            binding protein.
  JOURNAL   J. Neurochem. 49 (1987) 1105-15.
REFERENCE   2  [PMID:3121601]
  AUTHORS   Baudier J, Cole RD.
  TITLE     Phosphorylation of tau proteins to a state like that in Alzheimer's
            brain is catalyzed by a calcium/calmodulin-dependent kinase and
            modulated by phospholipids.
  JOURNAL   J. Biol. Chem. 262 (1987) 17577-83.
  ORGANISM  cow [GN:bta], rat [GN:rno]
REFERENCE   3  [PMID:4074698]
  AUTHORS   Schulman H, Kuret J, Jefferson AB, Nose PS, Spitzer KH.
  TITLE     Ca2+/calmodulin-dependent microtubule-associated protein 2 kinase:
            broad substrate specificity and multifunctional potential in diverse
            tissues.
  JOURNAL   Biochemistry. 24 (1985) 5320-7.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:9822657]
  AUTHORS   Anderson KA, Means RL, Huang QH, Kemp BE, Goldstein EG, Selbert MA,
            Edelman AM, Fremeau RT, Means AR.
  TITLE     Components of a calmodulin-dependent protein kinase cascade.
            Molecular cloning, functional characterization and cellular
            localization of Ca2+/calmodulin-dependent protein kinase kinase
            beta.
  JOURNAL   J. Biol. Chem. 273 (1998) 31880-9.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:9705275]
  AUTHORS   Matsushita M, Nairn AC.
  TITLE     Characterization of the mechanism of regulation of Ca2+/
            calmodulin-dependent protein kinase I by calmodulin and by
            Ca2+/calmodulin-dependent protein kinase kinase.
  JOURNAL   J. Biol. Chem. 273 (1998) 21473-81.
  ORGANISM  rat [GN:rno]
REFERENCE   6  [PMID:2538431]
  AUTHORS   Ohmstede CA, Jensen KF, Sahyoun NE.
  TITLE     Ca2+/calmodulin-dependent protein kinase enriched in cerebellar
            granule cells. Identification of a novel neuronal
            calmodulin-dependent protein kinase.
  JOURNAL   J. Biol. Chem. 264 (1989) 5866-75.
  ORGANISM  rat [GN:rno]
REFERENCE   7  [PMID:2822719]
  AUTHORS   Rieker JP, Swanljung-Collins H, Collins JH.
  TITLE     Purification and characterization of a calmodulin-dependent myosin
            heavy chain kinase from intestinal brush border.
  JOURNAL   J. Biol. Chem. 262 (1987) 15262-8.
  ORGANISM  chicken [GN:gga]
REFERENCE   8  [PMID:3089163]
  AUTHORS   Iwasa T, Inoue N, Fukunaga K, Isobe T, Okuyama T, Miyamoto E.
  TITLE     Purification and characterization of a multifunctional
            calmodulin-dependent protein kinase from canine myocardial cytosol.
  JOURNAL   Arch. Biochem. Biophys. 248 (1986) 21-9.
  ORGANISM  dog [GN:cfa]
REFERENCE   9  [PMID:10864438]
  AUTHORS   Gomes AV, Barnes JA, Vogel HJ.
  TITLE     Spectroscopic characterization of the interaction between
            calmodulin-dependent protein kinase I and calmodulin.
  JOURNAL   Arch. Biochem. Biophys. 379 (2000) 28-36.
  ORGANISM  rat [GN:rno]
REFERENCE   10 [PMID:12390014]
  AUTHORS   Mal TK, Skrynnikov NR, Yap KL, Kay LE, Ikura M.
  TITLE     Detecting protein kinase recognition modes of calmodulin by residual
            dipolar couplings in solution NMR.
  JOURNAL   Biochemistry. 41 (2002) 12899-906.
  ORGANISM  human [GN:hsa]
REFERENCE   11 [PMID:6150036]
  AUTHORS   Ngai PK, Walsh MP.
  TITLE     Inhibition of smooth muscle actin-activated myosin Mg2+-ATPase
            activity by caldesmon.
  JOURNAL   J. Biol. Chem. 259 (1984) 13656-9.
  ORGANISM  chicken [GN:gga]
REFERENCE   12 [PMID:2176896]
  AUTHORS   Ikebe M, Reardon S, Scott-Woo GC, Zhou Z, Koda Y.
  TITLE     Purification and characterization of calmodulin-dependent
            multifunctional protein kinase from smooth muscle: isolation of
            caldesmon kinase.
  JOURNAL   Biochemistry. 29 (1990) 11242-8.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map04012  ErbB signaling pathway
            PATH: map04020  Calcium signaling pathway
            PATH: map04310  Wnt signaling pathway
            PATH: map04720  Long-term potentiation
            PATH: map04740  Olfactory transduction
            PATH: map04912  GnRH signaling pathway
            PATH: map04916  Melanogenesis
            PATH: map04920  Adipocytokine signaling pathway
            PATH: map05214  Glioma
ORTHOLOGY   KO: K00908  Ca2+/calmodulin-dependent protein kinase
            KO: K04515  calcium/calmodulin-dependent protein kinase (CaM kinase)
                        II
            KO: K05869  calcium/calmodulin-dependent protein kinase IV
            KO: K07359  calcium/calmodulin-dependent protein kinase kinase
            KO: K08794  calcium/calmodulin-dependent protein kinase I
            KO: K08795  pregnancy upregulated non-ubiquitously expressed CaM
                        kinase
GENES       HSA: 10645(CAMKK2) 139728(PNCK) 57118(CAMK1D) 57172(CAMK1G)
                 814(CAMK4) 815(CAMK2A) 816(CAMK2B) 817(CAMK2D) 818(CAMK2G)
                 84254(CAMKK1) 8536(CAMK1)
            PTR: 450529(LOC450529) 460153(CAMK1) 461445(CAMK2D) 461992(CAMK4)
                 462189(CAMK2A) 469667(CAMK1G)
            MMU: 108058(Camk2d) 12322(Camk2a) 12323(Camk2b) 12325(Camk2g)
                 12326(Camk4) 207565(Camkk2) 215303(Camk1g) 227541(Camk1d)
                 52163(Camk1) 55984(Camkk1) 93843(Pnck)
            RNO: 171140(Camk2g) 171358(Camk1g) 171503(Camk1) 24245(Camk2b)
                 24246(Camk2d) 25050(Camk4) 25400(Camk2a) 29660(Pnck)
                 307124(RGD1560691_predicted) 60341(Camkk1) 83506(Camkk2)
            CFA: 484665(CAMK1) 486263(CAMKK2) 489050(CAMK2G) 490273(CAMK1G)
                 492241(PNCK) 607636(CAMK1D) 610764(CAMK2D) 611124(CAMKK1)
                 612941(CAMK2A)
            BTA: 282162(CAMK2G) 509084(MGC139717) 510260(LOC510260)
                 511504(MGC142748) 520498(MGC142688) 525416(MGC128545)
                 530719(CAMK2A) 532713(CAMK2D) 614251(MGC142416)
            SSC: 397394(CAMK2G) 397674(CAMK2D)
            GGA: 374174(CAMK2B) 374175(CAMK2A) 396405(CAMKK2) 419859(CAMK1G)
                 422688(RCJMB04_10k21) 423737(CAMK2G) 723973(CAMK4)
                 771003(CAMKK1)
            XLA: 380508(camk2g) 397789(LOC397789) 398402(CaM-KIa)
                 399357(CaM-KI) 444524(MGC82022)
            XTR: 549023(camk1)
            DRE: 393802(zgc:73155) 436815(camk2da) 445208(camk2db)
                 541526(zgc:113440) 550270(camk4) 550436(camk2a)
                 555945(LOC555945) 558989(camk2ga) 562064(LOC562064)
                 562629(LOC562629) 571673(LOC571673)
            SPU: 373512(CaMK-II) 582789(LOC582789)
            DME: Dmel_CG18069(CaMKII)
            CEL: K07A9.2(cmk-1) K11E8.1(unc-43)
            ATH: AT3G45240(GRIK1)
            OSA: 4342456 4343002
            CME: CMF051C
            SCE: YER129W(SAK1) YFR014C(CMK1) YOL016C(CMK2)
            AGO: AGOS_AAR009W
            PIC: PICST_53820 PICST_73399(SAT4)
            CAL: CaO19.1754 CaO19.3068 CaO19.3854 CaO19_5911(CaO19.5911)
            CGR: CAGL0F04741g CAGL0K02167g
            SPO: SPCC297.03(ssp1)
            ANI: AN2412.2 AN5728.2 AN8827.2
            AFM: AFUA_1G06920 AFUA_2G13680 AFUA_5G05980
            AOR: AO090001000493 AO090009000663 AO090026000231
            CNE: CNH01060 CNI04110
            UMA: UM06019.1
            DDI: DDB_0214815(mlkA) DDB_0216308 DDB_0220010
            PFA: MAL13P1.185 MAL3P3.17 MAL7P1.73 PF13_0211 PF14_0227 PFL1885c
            CPV: cgd2_1060 cgd2_1300
            CHO: Chro.20118 Chro.20142
            TAN: TA12965
            TPV: TP02_0399
            TET: TTHERM_00000020 TTHERM_00011220 TTHERM_00011380
                 TTHERM_00075550 TTHERM_00075800 TTHERM_00077200
                 TTHERM_00077720 TTHERM_00079490 TTHERM_00094330
                 TTHERM_00106700 TTHERM_00160930 TTHERM_00185750
                 TTHERM_00193200 TTHERM_00222260 TTHERM_00355740
                 TTHERM_00377310 TTHERM_00384880 TTHERM_00622950
                 TTHERM_00622990 TTHERM_00624440 TTHERM_00637040
                 TTHERM_00969600 TTHERM_01014460 TTHERM_01015890
                 TTHERM_01018400 TTHERM_01049230 TTHERM_01052880
                 TTHERM_01052920 TTHERM_01075630 TTHERM_01126380
                 TTHERM_01164090 TTHERM_01227720 TTHERM_01344710
            EHI: 113.t00001 20.t00012 70.t00038
            BUR: Bcep18194_B1590 Bcep18194_B3160
            RRU: Rru_A2187
            RHA: RHA1_ro05066
            AVA: Ava_0012 Ava_0083 Ava_0084 Ava_0153 Ava_0219 Ava_0353
                 Ava_0434 Ava_0762 Ava_1153 Ava_1552 Ava_1592 Ava_1816 Ava_1995
                 Ava_2109 Ava_2519 Ava_2528 Ava_2684 Ava_2803 Ava_2809 Ava_2851
                 Ava_2989 Ava_2990 Ava_3036 Ava_3384 Ava_3535 Ava_3584 Ava_3596
                 Ava_3867 Ava_3995 Ava_4106 Ava_4391 Ava_4489 Ava_4504 Ava_4681
                 Ava_4764 Ava_4855 Ava_4862 Ava_5054 Ava_A0032 Ava_B0202
STRUCTURES  PDB: 2JAM  2JC6  2V7O  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.17
            ExPASy - ENZYME nomenclature database: 2.7.11.17
            ExplorEnz - The Enzyme Database: 2.7.11.17
            ERGO genome analysis and discovery system: 2.7.11.17
            BRENDA, the Enzyme Database: 2.7.11.17
            CAS: 97350-82-8
///
ENTRY       EC 2.7.11.18                Enzyme
NAME        myosin-light-chain kinase;
            [myosin-light-chain] kinase;
            ATP:myosin-light-chain O-phosphotransferase;
            calcium/calmodulin-dependent myosin light chain kinase;
            MLCK;
            MLCKase;
            myosin kinase;
            myosin light chain kinase;
            myosin light chain protein kinase;
            myosin light-chain kinase (phosphorylating);
            smooth-muscle-myosin-light-chain kinase;
            STK18
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[myosin light chain] O-phosphotransferase
REACTION    ATP + [myosin light chain] = ADP + [myosin light chain] phosphate
            [RN:R03150]
ALL_REAC    R03150
SUBSTRATE   ATP [CPD:C00002];
            myosin light chain [CPD:C01003]
PRODUCT     ADP [CPD:C00008];
            myosin light chain phosphate [CPD:C03875]
COFACTOR    Calcium [CPD:C00076];
            Calmodulin [CPD:C00391]
COMMENT     Requires Ca2+ and calmodulin for activity. The 20-kDa light chain
            from smooth muscle myosin is phosphorylated more rapidly than any
            other acceptor, but light chains from other myosins and myosin
            itself can act as acceptors, but more slowly.
REFERENCE   1  [PMID:6894756]
  AUTHORS   Adelstein RS, Klee CB.
  TITLE     Purification and characterization of smooth muscle myosin light
            chain kinase.
  JOURNAL   J. Biol. Chem. 256 (1981) 7501-9.
  ORGANISM  turkey
REFERENCE   2  [PMID:156362]
  AUTHORS   Hathaway DR, Adelstein RS.
  TITLE     Human platelet myosin light chain kinase requires the
            calcium-binding protein calmodulin for activity.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 1653-7.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:4853304]
  AUTHORS   Pires E, Perry SV, Thomas MA.
  TITLE     Myosin light-chain kinase, a new enzyme from striated muscle.
  JOURNAL   FEBS. Lett. 41 (1974) 292-6.
  ORGANISM  rabbit
REFERENCE   4  [PMID:3881420]
  AUTHORS   Nunnally MH, Rybicki SB, Stull JT.
  TITLE     Characterization of chicken skeletal muscle myosin light chain
            kinase. Evidence for muscle-specific isozymes.
  JOURNAL   J. Biol. Chem. 260 (1985) 1020-6.
  ORGANISM  chicken [GN:gga]
REFERENCE   5  [PMID:3897230]
  AUTHORS   Edelman AM, Takio K, Blumenthal DK, Hansen RS, Walsh KA, Titani K,
            Krebs EG.
  TITLE     Characterization of the calmodulin-binding and catalytic domains in
            skeletal muscle myosin light chain kinase.
  JOURNAL   J. Biol. Chem. 260 (1985) 11275-85.
  ORGANISM  rabbit
REFERENCE   6  [PMID:12390014]
  AUTHORS   Mal TK, Skrynnikov NR, Yap KL, Kay LE, Ikura M.
  TITLE     Detecting protein kinase recognition modes of calmodulin by residual
            dipolar couplings in solution NMR.
  JOURNAL   Biochemistry. 41 (2002) 12899-906.
  ORGANISM  chicken [GN:gga]
REFERENCE   7  [PMID:10231558]
  AUTHORS   Sobieszek A.
  TITLE     Enzyme kinetic characterization of the smooth muscle myosin
            phosphorylating system: activation by calcium and calmodulin and
            possible inhibitory mechanisms of antagonists.
  JOURNAL   Biochim. Biophys. Acta. 1450 (1999) 77-91.
  ORGANISM  turkey
REFERENCE   8  [PMID:9054394]
  AUTHORS   Sobieszek A, Borkowski J, Babiychuk VS.
  TITLE     Purification and characterization of a smooth muscle myosin light
            chain kinase-phosphatase complex.
  JOURNAL   J. Biol. Chem. 272 (1997) 7034-41.
  ORGANISM  turkey
REFERENCE   9  [PMID:10098974]
  AUTHORS   Fujita K, Ye LH, Sato M, Okagaki T, Nagamachi Y, Kohama K.
  TITLE     Myosin light chain kinase from skeletal muscle regulates an
            ATP-dependent interaction between actin and myosin by binding to
            actin.
  JOURNAL   Mol. Cell. Biochem. 190 (1999) 85-90.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map04020  Calcium signaling pathway
            PATH: map04510  Focal adhesion
            PATH: map04810  Regulation of actin cytoskeleton
ORTHOLOGY   KO: K00907  myosin-light-chain kinase
GENES       HSA: 340156(RP11-145H9.1) 4638(MYLK) 7273(TTN) 85366(MYLK2)
                 91807(MLCK)
            PTR: 460640(MYLK)
            MMU: 107589(Mylk) 213435(D830007F02Rik) 228785(Mylk2)
            RNO: 288057(Mylk_predicted)
            CFA: 477187(MYLK2) 488012(MYLK) 488190(LOC488190)
            BTA: 338037(MYLK)
            GGA: 396356(MYLK2) 396445(MYLK) 415748(LOC415748)
                 420893(LOC420893) 428278(LOC428278)
            DRE: 559667(LOC559667) 569510(LOC569510)
            DME: Dmel_CG1776 Dmel_CG18255(Strn-Mlck)
            CEL: ZC373.4
            AVA: Ava_2845
STRUCTURES  PDB: 2YR3  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.18
            ExPASy - ENZYME nomenclature database: 2.7.11.18
            ExplorEnz - The Enzyme Database: 2.7.11.18
            ERGO genome analysis and discovery system: 2.7.11.18
            BRENDA, the Enzyme Database: 2.7.11.18
            CAS: 51845-53-5
///
ENTRY       EC 2.7.11.19                Enzyme
NAME        phosphorylase kinase;
            dephosphophosphorylase kinase;
            glycogen phosphorylase kinase;
            PHK;
            phosphorylase b kinase;
            phosphorylase B kinase;
            phosphorylase kinase (phosphorylating);
            STK17
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:phosphorylase-b phosphotransferase
REACTION    2 ATP + phosphorylase b = 2 ADP + phosphorylase a [RN:R00076]
ALL_REAC    R00076
SUBSTRATE   ATP [CPD:C00002];
            phosphorylase b [CPD:C02308]
PRODUCT     ADP [CPD:C00008];
            phosphorylase a [CPD:C02307]
COMMENT     Requires Ca2+ and calmodulin for activity. The enzyme phosphorylates
            a specific serine residue in each of the subunits of the dimeric
            phosphorylase b. For muscle phosphorylase but not liver
            phosphorylase, this is accompanied by a further dimerization to form
            a tetrameric phosphorylase. The enzyme couples muscle contraction
            with energy production via glycogenolysis---glycolysis by catalysing
            the Ca2+-dependent phosphorylation and activation of glycogen
            phosphorylase b [5]. The gamma subunit of the tetrameric enzyme is
            the catalytic subunit.
REFERENCE   1  [PMID:13315361]
  AUTHORS   KREBS EG, FISCHER EH.
  TITLE     The phosphorylase b to a converting enzyme of rabbit skeletal
            muscle.
  JOURNAL   Biochim. Biophys. Acta. 20 (1956) 150-7.
  ORGANISM  rabbit
REFERENCE   2  [PMID:13538949]
  AUTHORS   KREBS EG, KENT AB, FISCHER EH.
  TITLE     The muscle phosphorylase b kinase reaction.
  JOURNAL   J. Biol. Chem. 231 (1958) 73-83.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:13315351]
  AUTHORS   RALL TW, WOSILAIT WD, SUTHERLAND EW.
  TITLE     The interconversion of phosphorylase a and phosphorylase b from dog
            heart muscle.
  JOURNAL   Biochim. Biophys. Acta. 20 (1956) 69-76.
  ORGANISM  dog [GN:cfa]
REFERENCE   4  [PMID:4029141]
  AUTHORS   Nikolaropoulos S, Sotiroudis TG.
  TITLE     Phosphorylase kinase from chicken gizzard. Partial purification and
            characterization.
  JOURNAL   Eur. J. Biochem. 151 (1985) 467-73.
  ORGANISM  chicken [GN:gga]
REFERENCE   5  [PMID:1931956]
  AUTHORS   Farrar YJ, Carlson GM.
  TITLE     Kinetic characterization of the calmodulin-activated catalytic
            subunit of phosphorylase kinase.
  JOURNAL   Biochemistry. 30 (1991) 10274-9.
  ORGANISM  rabbit
REFERENCE   6  [PMID:7673209]
  AUTHORS   Dasgupta M, Blumenthal DK.
  TITLE     Characterization of the regulatory domain of the gamma-subunit of
            phosphorylase kinase. The two noncontiguous calmodulin-binding
            subdomains are also autoinhibitory.
  JOURNAL   J. Biol. Chem. 270 (1995) 22283-9.
  ORGANISM  rabbit
REFERENCE   7  [PMID:9362479]
  AUTHORS   Lowe ED, Noble ME, Skamnaki VT, Oikonomakos NG, Owen DJ, Johnson LN.
  TITLE     The crystal structure of a phosphorylase kinase peptide substrate
            complex: kinase substrate recognition.
  JOURNAL   EMBO. J. 16 (1997) 6646-58.
  ORGANISM  rabbit
PATHWAY     PATH: map04020  Calcium signaling pathway
            PATH: map04910  Insulin signaling pathway
ORTHOLOGY   KO: K00871  phosphorylase kinase gamma subunit
GENES       HSA: 5260(PHKG1) 5261(PHKG2)
            MMU: 18682(Phkg1) 68961(Phkg2)
            RNO: 140671(Phkg2) 29353(Phkg1)
            CFA: 489784(PHKG1) 607275(PHKG2)
            BTA: 540682(MGC137450)
            GGA: 417543(PHKG1)
            XLA: 373780(psph-A) 496328(LOC496328)
            XTR: 448255(phkg1)
            DRE: 393937(zgc:55863) 555085(LOC555085) 559261(LOC559261)
                 565379(zgc:153009)
            SPU: 582497(LOC582497)
            DME: Dmel_CG1830(PhKgamma)
            PIC: PICST_32412(PAK3)
            CAL: CaO19.2781
            SYG: sync_0281
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.19
            ExPASy - ENZYME nomenclature database: 2.7.11.19
            ExplorEnz - The Enzyme Database: 2.7.11.19
            ERGO genome analysis and discovery system: 2.7.11.19
            BRENDA, the Enzyme Database: 2.7.11.19
            CAS: 9001-88-1
///
ENTRY       EC 2.7.11.20                Enzyme
NAME        elongation factor 2 kinase;
            Ca/CaM-kinase III;
            calmodulin-dependent protein kinase III;
            CaM kinase III;
            eEF2 kinase;
            eEF2K;
            EF2K;
            STK19
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[elongation factor 2] phosphotransferase
REACTION    ATP + [elongation factor 2] = ADP + [elongation factor 2] phosphate
SUBSTRATE   ATP [CPD:C00002];
            [elongation factor 2]
PRODUCT     ADP [CPD:C00008];
            [elongation factor 2] phosphate
COMMENT     Requires Ca2+ and calmodulin for activity. The enzyme can also be
            phosphorylated by the catalytic subunit of EC 2.7.11.11,
            cAMP-dependent protein kinase. Elongation factor 2 is phosphorylated
            in several cell types in response to various growth factors,
            hormones and other stimuli that raise intracellular Ca2+ [1,2].
REFERENCE   1  [PMID:8514778]
  AUTHORS   Mitsui K, Brady M, Palfrey HC, Nairn AC.
  TITLE     Purification and characterization of calmodulin-dependent protein
            kinase III from rabbit reticulocytes and rat pancreas.
  JOURNAL   J. Biol. Chem. 268 (1993) 13422-33.
  ORGANISM  rabbit, rat [GN:rno]
REFERENCE   2  [PMID:1372803]
  AUTHORS   Hincke MT, Nairn AC.
  TITLE     Phosphorylation of elongation factor 2 during Ca(2+)-mediated
            secretion from rat parotid acini.
  JOURNAL   Biochem. J. 282 ( Pt 3) (1992) 877-82.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:11500363]
  AUTHORS   Knebel A, Morrice N, Cohen P.
  TITLE     A novel method to identify protein kinase substrates: eEF2 kinase is
            phosphorylated and inhibited by SAPK4/p38delta.
  JOURNAL   EMBO. J. 20 (2001) 4360-9.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:15158453]
  AUTHORS   Sans MD, Xie Q, Williams JA.
  TITLE     Regulation of translation elongation and phosphorylation of eEF2 in
            rat pancreatic acini.
  JOURNAL   Biochem. Biophys. Res. Commun. 319 (2004) 144-51.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:14709557]
  AUTHORS   Browne GJ, Finn SG, Proud CG.
  TITLE     Stimulation of the AMP-activated protein kinase leads to activation
            of eukaryotic elongation factor 2 kinase and to its phosphorylation
            at a novel site, serine 398.
  JOURNAL   J. Biol. Chem. 279 (2004) 12220-31.
  ORGANISM  human [GN:hsa]
REFERENCE   6  [PMID:11904175]
  AUTHORS   Ryazanov AG.
  TITLE     Elongation factor-2 kinase and its newly discovered relatives.
  JOURNAL   FEBS. Lett. 514 (2002) 26-9.
  ORGANISM  Caenorhabditis elegans [GN:cel]
ORTHOLOGY   KO: K08292  elongation factor 2 kinase
GENES       HSA: 29904(EEF2K)
            PTR: 454350(EEF2K)
            MMU: 13631(Eef2k)
            RNO: 25435(Eef2k)
            CFA: 479812(EEF2K)
            BTA: 521730(LOC521730)
            GGA: 416619(EEF2K)
            DRE: 437013(eef2k)
            SPU: 583067(LOC583067)
            CEL: F42A10.4(efk-1)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.20
            ExPASy - ENZYME nomenclature database: 2.7.11.20
            ExplorEnz - The Enzyme Database: 2.7.11.20
            ERGO genome analysis and discovery system: 2.7.11.20
            BRENDA, the Enzyme Database: 2.7.11.20
///
ENTRY       EC 2.7.11.21                Enzyme
NAME        polo kinase;
            Cdc5;
            Cdc5p;
            Plk;
            PLK;
            Plk1;
            Plo1;
            POLO kinase;
            polo serine-threonine kinase;
            polo-like kinase;
            polo-like kinase 1;
            serine/threonine-specific Drosophila kinase polo;
            STK21
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:protein phosphotransferase (spindle-pole-dependent)
REACTION    ATP + a protein = ADP + a phosphoprotein [RN:R00162]
ALL_REAC    R00162
SUBSTRATE   ATP [CPD:C00002];
            protein [CPD:C00017]
PRODUCT     ADP [CPD:C00008];
            phosphoprotein [CPD:C00562]
COMMENT     The enzyme associates with the spindle pole during mitosis and is
            thought to play an important role in the dynamic function of the
            mitotic spindle during chromosome segregation. The human form of the
            enzyme, Plk1, does not phosphorylate histone H1, enolase and
            phosvitin but it can phosphorylate myelin basic protein and
            microtubule-associated protein MAP-2, although to a lesser extent
            than casein [2].
REFERENCE   1  [PMID:1660828]
  AUTHORS   Llamazares S, Moreira A, Tavares A, Girdham C, Spruce BA, Gonzalez
            C, Karess RE, Glover DM, Sunkel CE.
  TITLE     polo encodes a protein kinase homolog required for mitosis in
            Drosophila.
  JOURNAL   Genes. Dev. 5 (1991) 2153-65.
REFERENCE   2  [PMID:7790358]
  AUTHORS   Golsteyn RM, Mundt KE, Fry AM, Nigg EA.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function.
  JOURNAL   J. Cell. Biol. 129 (1995) 1617-28.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:12186944]
  AUTHORS   Mulvihill DP, Hyams JS.
  TITLE     Cytokinetic actomyosin ring formation and septation in fission yeast
            are dependent on the full recruitment of the polo-like kinase Plo1
            to the spindle pole body and a functional spindle assembly
            checkpoint.
  JOURNAL   J. Cell. Sci. 115 (2002) 3575-86.
  ORGANISM  Schizosaccharomyces pombe [GN:spo]
REFERENCE   4  [PMID:14654016]
  AUTHORS   Ohkura H.
  TITLE     Phosphorylation: polo kinase joins an elite club.
  JOURNAL   Curr. Biol. 13 (2003) R912-4.
  ORGANISM  human [GN:hsa], Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map04110  Cell cycle
            PATH: map04111  Cell cycle - yeast
            PATH: map04914  Progesterone-mediated oocyte maturation
ORTHOLOGY   KO: K06631  polo-like kinase 1
            KO: K06660  cell cycle serine/threonine-protein kinase CDC5/MSD2
            KO: K08250  polo kinase
            KO: K08861  polo-like kinase 2
            KO: K08862  polo-like kinase 3
            KO: K08863  polo-like kinase 4
GENES       HSA: 10733(PLK4) 10769(PLK2) 1263(PLK3) 5347(PLK1)
            PTR: 453991(PLK1) 456546(PLK3) 461480(PLK4) 461861(PLK2)
            MCC: 708835(PLK2)
            MMU: 12795(Plk3) 18817(Plk1) 20620(Plk2) 20873(Plk4)
            RNO: 25515(Plk1) 310344(Plk4_predicted) 58936(Plk3) 83722(Plk2)
            CFA: 475380(PLK3) 476087(PLK4) 478063(PLK2) 489971(PLK1)
            BTA: 504282(PLK3) 538238(PLK1) 539449(LOC539449)
            GGA: 416575(RCJMB04_20p15) 424586(PLK3) 427150(PLK2)
            XLA: 379315(MGC53542) 380481(plk) 398770(MGC68791)
            XTR: 407937(plk1) 448451(plk3)
            DRE: 280649(plk1) 565576(zgc:165644)
            SPU: 579629(LOC579629) 589028(LOC589028)
            CEL: C14B9.4(plk-1) F55G1.8(plk-3) Y71F9B.7(plk-2)
            CME: CME146C
            SCE: YMR001C(CDC5)
            AGO: AGOS_ACL006W
            PIC: PICST_68049
            CAL: CaO19_6010(CaO19.6010)
            CGR: CAGL0J11638g
            SPO: SPAC23C11.16(plo1)
            CNE: CNK02500
            DDI: DDB_0216332(PLK)
            TET: TTHERM_00191790 TTHERM_01443850
            TBR: Tb927.7.6310
            TCR: 506513.160
            LMA: LmjF17.0790
STRUCTURES  PDB: 2OGQ  2OJS  2OJX  2OU7  2OWB  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.21
            ExPASy - ENZYME nomenclature database: 2.7.11.21
            ExplorEnz - The Enzyme Database: 2.7.11.21
            ERGO genome analysis and discovery system: 2.7.11.21
            BRENDA, the Enzyme Database: 2.7.11.21
///
ENTRY       EC 2.7.11.22                Enzyme
NAME        cyclin-dependent kinase;
            Bur1;
            Bur1 Cdk;
            Cak1;
            Cak1p;
            cdc2;
            cdc2 kinase;
            Cdc28p;
            CDK;
            cdk-activating kinase;
            Cdk-activating protein kinase;
            cdk1;
            cdk2;
            Cdk2;
            cdk3;
            cdk4;
            cdk5;
            cdk6;
            cdk7;
            cdk8;
            cdk9;
            cyclin A-activated cdc2;
            cyclin A-activated cdk2;
            cyclin D-cdk6 kinase;
            cyclin D-dependent kinase;
            cyclin E kinase;
            cyclin-A associated kinase;
            cyclin-dependent kinase 6;
            cyclin-dependent kinase-2;
            cyclin-dependent kinase-4;
            cyclin-dependent protein kinase activating kinase;
            cyk;
            D-type cyclin kinase;
            nclk;
            neuronal cdc2-like kinase;
            PCTAIRE-1;
            STK25
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:cyclin phosphotransferase
REACTION    ATP + a protein = ADP + a phosphoprotein [RN:R00162]
ALL_REAC    R00162
SUBSTRATE   ATP [CPD:C00002];
            protein [CPD:C00017]
PRODUCT     ADP [CPD:C00008];
            phosphoprotein [CPD:C00562]
COMMENT     Activation of cyclin-dependent kinases requires association of the
            enzyme with a regulatory subunit referred to as a cyclin. It is the
            sequential activation and inactivation of cyclin-dependent kinases,
            through the periodic synthesis and destruction of cyclins, that
            provides the primary means of cell-cycle regulation.
REFERENCE   1  [PMID:10331086]
  AUTHORS   Johnson DG, Walker CL.
  TITLE     Cyclins and cell cycle checkpoints.
  JOURNAL   Annu. Rev. Pharmacol. Toxicol. 39 (1999) 295-312.
  ORGANISM  mammalian
REFERENCE   2  [PMID:8397207]
  AUTHORS   Pan ZQ, Amin A, Hurwitz J.
  TITLE     Characterization of the in vitro reconstituted cyclin A or
            B1-dependent cdk2 and cdc2 kinase activities.
  JOURNAL   J. Biol. Chem. 268 (1993) 20443-51.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:8550604]
  AUTHORS   Yee A, Wu L, Liu L, Kobayashi R, Xiong Y, Hall FL.
  TITLE     Biochemical characterization of the human cyclin-dependent protein
            kinase activating kinase. Identification of p35 as a novel
            regulatory subunit.
  JOURNAL   J. Biol. Chem. 271 (1996) 471-7.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04110  Cell cycle
            PATH: map04111  Cell cycle - yeast
            PATH: map04115  p53 signaling pathway
            PATH: map04360  Axon guidance
            PATH: map04530  Tight junction
            PATH: map04540  Gap junction
            PATH: map04660  T cell receptor signaling pathway
            PATH: map04914  Progesterone-mediated oocyte maturation
            PATH: map05212  Pancreatic cancer
            PATH: map05214  Glioma
            PATH: map05215  Prostate cancer
            PATH: map05218  Melanoma
            PATH: map05219  Bladder cancer
            PATH: map05220  Chronic myeloid leukemia
            PATH: map05222  Small cell lung cancer
            PATH: map05223  Non-small cell lung cancer
ORTHOLOGY   KO: K02087  cyclin-dependent kinase 1
            KO: K02088  cyclin-dependent kinase 3
            KO: K02089  cyclin-dependent kinase 4
            KO: K02090  cyclin-dependent kinase 5
            KO: K02091  cyclin-dependent kinase 6
            KO: K02202  cyclin-dependent kinase 7
            KO: K02206  cyclin-dependent kinase 2
            KO: K02208  cyclin-dependent kinase 8/11
            KO: K02211  cyclin-dependent kinase 9
            KO: K02449  cyclin-dependent kinase 10
            KO: K04563  cyclin-dependent kinase
            KO: K06655  negative regulator of the PHO system
            KO: K06667  serine/threonine-protein kinase CAK1
            KO: K07760  cyclin-dependent kinase
            KO: K08817  cell cycle related kinase
            KO: K08818  cell division cycle 2-like
            KO: K08819  Cdc2-related kinase, arginine/serine-rich
            KO: K08820  PCTAIRE protein kinase
            KO: K08821  PFTAIRE protein kinase
            KO: K08824  cyclin-dependent kinase-like
            KO: K08828  intestinal cell (MAK-like) kinase
            KO: K08829  male germ cell-associated kinase
            KO: K08830  renal tumor antigen
            KO: K08839  serine/threonine kinase 25
GENES       HSA: 1017(CDK2) 1018(CDK3) 1019(CDK4) 1020(CDK5) 1021(CDK6)
                 1022(CDK7) 1024(CDK8) 1025(CDK9) 22858(ICK) 23097(CDC2L6)
                 23552(CCRK) 344387(CDKL4) 4117(MAK) 51265(CDKL3) 5127(PCTK1)
                 5128(PCTK2) 5129(PCTK3) 51755(CRKRS) 5218(PFTK1) 5891(RAGE)
                 65061(ALS2CR7) 6792(CDKL5) 728642(CDC2L2) 8558(CDK10)
                 8621(CDC2L5) 8814(CDKL1) 8999(CDKL2) 983(CDC2) 984(CDC2L1)
            PTR: 450481(CDC2) 452025(CDK4) 452146(PCTK2) 452501(CDK8)
                 453176(RAGE) 462064(CDKL3) 462378(CDK7) 463522(PFTK1)
                 463534(LOC463534) 463891(CDK5) 464755(CDK9) 465602(PCTK1)
                 467032(CDK2) 468331(CDK3)
            MMU: 105278(Ccrk) 107951(Cdk9) 12534(Cdc2a) 12537(Cdc2l1)
                 12566(Cdk2) 12567(Cdk4) 12568(Cdk5) 12571(Cdk6) 12572(Cdk7)
                 17152(Mak) 18555(Pctk1) 18557(Pctk3) 18647(Pftk1)
                 213084(Cdkl3) 234854(Cdk10) 237459(Pctk2) 264064(Cdk8)
                 26448(Rage) 271697(Als2cr7) 381113(Cdkl4) 53886(Cdkl2)
                 56542(Ick) 640611(LOC640611) 69131(Crkrs) 69562(Cdc2l5)
                 69681(Cdk3) 71091(Cdkl1) 78334(Cdc2l6)
            RNO: 114483(Cdk6) 140908(Cdk5) 171150(Cdk7) 192350(Crkrs)
                 252879(Cdc2l1) 25677(Mak) 289019(Pctk3)
                 301439(Als2cr7_predicted) 305242(Cdkl2) 306998(Cdc2l5)
                 309804(Cdc2l6_predicted) 314198(Cdkl1_predicted) 314743(Pctk2)
                 315362(RGD1566355_predicted) 361434(Cdk10) 362110(Cdk9)
                 362316(Pftk1_predicted) 362787(Rage) 362817(Cdk2) 364666(Ccrk)
                 498140(RGD1560888_predicted) 503009(LOC503009) 54237(Cdc2a)
                 60396(Cdkl3) 81741(Pctk1) 84411(Ick) 94201(Cdk4)
            CFA: 475223(PFTK1) 475537(CDK5) 475874(CDC2L5) 476354(CCRK)
                 478428(CDKL2) 478721(MAK) 478873(LOC478873) 480317(CDKL1)
                 480897(PCTK1) 481131(CDK4) 481843(ICK) 482614(PCTK2)
                 483323(CDK3) 486035(CDK8) 488573(PCTK3) 488997(CDC2)
                 489591(LOC489591) 489655(CDK10) 490863(RAGE) 491027(CRKRS)
                 491325(CDK9) 491761(CDKL5) 606931(CDK2) 608339(CDKL3)
                 608441(CDK7) 608890(CDKL4) 609920(CDK6) 612317(CDC2L6)
                 612475(LOC612475)
            BTA: 281061(CDC2) 281066(CDK5) 493708(CDK11) 506286(MGC157129)
                 507149(LOC507149) 510618(CDK4) 510920(CCRK) 511513(LOC511513)
                 511802(LOC511802) 515462(MGC140417) 517478(CDKL4) 519217(CDK2)
                 520580(LOC520580) 523900(LOC523900) 534048(MGC155091)
                 536048(MAK) 539655(LOC539655) 541279(LOC541279)
                 613810(LOC613810) 615171(MGC134436) 616277(LOC616277)
                 618631(MGC160000)
            GGA: 396252(CDC2) 415840(CDK10) 417226(CDK9) 417920(PCTK2)
                 419406(LOC419406) 420546(PFTK1) 420558(CDK6) 420766(CDC2L5)
                 421756(CDC2L6) 421896(ICK) 423575(CDKL1) 428001(CDKL5)
                 428080(CDK8) 428306(CRKRS) 428736(CDKL2) 428910(RAGE)
                 429642(CDK3) 771294(LOC771294) 771736(PCTK3)
            XLA: 379406(MGC52574) 379785(cdc2a) 379846(pctk2-a) 380229(cdk9)
                 380246(cdc2) 380415(cdk-8) 399296(cdk5) 431841(MGC81521)
                 432036(MGC81499) 444781(MGC81972) 446531(MGC80275) 447015(mak)
                 447409(MGC81962) 495331(LOC495331)
            XTR: 394503(cdc2) 394856(cdc2l6) 448039(cdk9) 448581(pctk3)
                 493498(MGC89594) 549329(cdk10) 549496(LOC549496)
                 549737(TNeu122g07.1) 549973(cdk7)
            DRE: 321602(cdk9) 335339(mak) 373868(cdk8) 405897(cdk7)
                 406715(cdk2) 445316(zgc:101002) 494103(zgc:101589)
                 494112(zgc:101530) 550285(zgc:110252) 559341(LOC559341)
                 570790(LOC570790) 65234(cdk5) 678550(zgc:136819) 80973(cdc2)
            SPU: 373289(cdk4) 578167(LOC578167) 578803(LOC578803)
                 580960(LOC580960) 581028(LOC581028) 584384(LOC584384)
                 585189(LOC585189) 585950(LOC585950) 588123(LOC588123)
                 591372(LOC591372) 592381(LOC592381) 593706(LOC593706)
                 594579(LOC594579) 761423(LOC761423) 764563(LOC764563)
            DME: Dmel_CG10498 Dmel_CG10572(Cdk8) Dmel_CG10579(Eip63E)
                 Dmel_CG3319(Cdk7) Dmel_CG4268 Dmel_CG5179(Cdk9) Dmel_CG5363
                 Dmel_CG7236 Dmel_CG7597 Dmel_CG8203(Cdk5)
            CEL: B0285.1 B0495.2(CDC2) C07G1.3(pct-1) F39H11.3(cdk-8)
                 M04C9.5(dyf-5) T05G5.3(cdk-1) T27E9.3(cdk-5) Y39G10AL.3(cdk-7)
                 Y42A5A.4
            ATH: AT1G18040(AT;CDCKD;3/CAK2AT/CDKD1;3)
                 AT1G66750(AT;CDKD;2/CAK4AT/CDKD1;2/CDKD;2) AT1G67580
                 AT3G48750(CDC2/CDC2A/CDC2AAT/CDK2/CDKA;1) AT3G54180(CDC2B)
                 AT4G19110 AT5G10270(CDKC;1) AT5G63370 AT5G63610(HEN3)
            OSA: 4325101 4325386 4325730 4329899 4331415 4336224 4338689
                 4339927 4349519
            CME: CME119C CMN139C CMQ195C
            SCE: YBR160W(CDC28) YDL108W(KIN28) YFL029C(CAK1) YPL031C(PHO85)
                 YPR161C(SGV1)
            AGO: AGOS_ABR177C AGOS_ADL283W AGOS_ADR058C AGOS_AFR150C
                 AGOS_AGL242C
            PIC: PICST_48986(PHO85) PICST_54142(KIN28) PICST_5847(CRK1)
                 PICST_77457(CTK1) PICST_90135(CDC28)
            CAL: CaO19.3856 CaO19_6239(CaO19.6239) CaO19_793(CaO19.793)
            CGR: CAGL0H07535g CAGL0H10318g CAGL0I08349g CAGL0K12496g
                 CAGL0L12474g
            SPO: SPAC1D4.06c(csk1) SPAC23H4.17c SPAC2F3.15 SPBC11B10.09(cdc2)
                 SPBC19F8.07(crk1) SPCC16C4.11
            ANI: AN0699.2 AN1867.2 AN4182.2 AN6243.2 AN8190.2
            AFM: AFUA_1G13600 AFUA_2G13140 AFUA_5G03160 AFUA_6G07980
                 AFUA_7G03720
            AOR: AO090003000133 AO090003000244 AO090012000514 AO090026000271
                 AO090102000520
            CNE: CNA04030 CNC01750 CNM01920 CNN01700
            UMA: UM02513.1 UM04925.1
            ECU: ECU02_1450 ECU08_1920
            DDI: DDB_0185028(cdk1) DDB_0191155(cdk5) DDB_0191261(cdk8)
                 DDB_0191429(cdk7) DDB_0216376(cdk11) DDB_0229430
            PFA: MAL13P1.279 PF10_0141
            CPV: cgd5_2510
            CHO: Chro.10015 Chro.50127 Chro.70041 Chro.70056
            TAN: TA06730
            TPV: TP01_0728 TP01_0781 TP04_0551
            TET: TTHERM_00011670 TTHERM_00058800 TTHERM_00066860
                 TTHERM_00267860 TTHERM_01035490
            TBR: Tb09.211.0960 Tb10.61.1850 Tb10.70.2210 Tb10.70.7040
                 Tb11.01.8550
            TCR: 504181.40 506677.20 506885.120 511025.30 511289.50
            LMA: LmjF19.0180 LmjF32.3250 LmjF35.5010
            EHI: 119.t00008 13.t00001 597.t00004 6.t00087
STRUCTURES  PDB: 2CLX  2DS1  2DUV  2I40  2QKR  2UZB  2UZD  2UZE  2UZL  2UZN  
                 2UZO  2V0D  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.22
            ExPASy - ENZYME nomenclature database: 2.7.11.22
            ExplorEnz - The Enzyme Database: 2.7.11.22
            ERGO genome analysis and discovery system: 2.7.11.22
            BRENDA, the Enzyme Database: 2.7.11.22
///
ENTRY       EC 2.7.11.23                Enzyme
NAME        [RNA-polymerase]-subunit kinase;
            CTD kinase;
            STK9
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[DNA-directed RNA polymerase] phosphotransferase
REACTION    ATP + [DNA-directed RNA polymerase] = ADP + phospho-[DNA-directed
            RNA polymerase] [RN:R04358]
ALL_REAC    R04358
SUBSTRATE   ATP [CPD:C00002];
            [DNA-directed RNA polymerase] [CPD:C03959]
PRODUCT     ADP [CPD:C00008];
            phospho-[DNA-directed RNA polymerase] [CPD:C04395]
COMMENT     The enzyme appears to be distinct from other protein kinases. It
            brings about multiple phosphorylations of the unique C-terminal
            repeat domain of the largest subunit of eukaryotic DNA-directed RNA
            polymerase (EC 2.7.7.6). The enzyme does not phosphorylate casein,
            phosvitin or histone.
REFERENCE   1  [PMID:2657724]
  AUTHORS   Lee JM, Greenleaf AL.
  TITLE     A protein kinase that phosphorylates the C-terminal repeat domain of
            the largest subunit of RNA polymerase II.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 3624-8.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K00916  [RNA-polymerase]-subunit kinase
GENES       SCE: YKL139W(CTK1)
            AGO: AGOS_AFR205C
            CGR: CAGL0D02002g
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.23
            ExPASy - ENZYME nomenclature database: 2.7.11.23
            ExplorEnz - The Enzyme Database: 2.7.11.23
            ERGO genome analysis and discovery system: 2.7.11.23
            BRENDA, the Enzyme Database: 2.7.11.23
            CAS: 122097-00-1
///
ENTRY       EC 2.7.11.24                Enzyme
NAME        mitogen-activated protein kinase;
            c-Jun N-terminal kinase;
            Dp38;
            ERK;
            ERK1;
            ERK2;
            extracellular signal-regulated kinase;
            JNK;
            JNK3alpha1;
            LeMPK3;
            MAP kinase;
            MAP-2 kinase;
            MAPK;
            MBP kinase I;
            MBP kinase II;
            microtubule-associated protein 2 kinase;
            microtubule-associated protein kinase;
            myelin basic protein kinase;
            p38delta;
            p38-2;
            p42 mitogen-activated protein kinase;
            p42mapk;
            PMK-1;
            PMK-2;
            PMK-3;
            pp42;
            pp44mapk;
            p44mpk;
            SAPK;
            STK26;
            stress-activated protein kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:protein phosphotransferase (MAPKK-activated)
REACTION    ATP + a protein = ADP + a phosphoprotein [RN:R00162]
ALL_REAC    R00162
SUBSTRATE   ATP [CPD:C00002];
            protein [CPD:C00017]
PRODUCT     ADP [CPD:C00008];
            phosphoprotein [CPD:C00562]
COMMENT     Phosphorylation of specific tyrosine and threonine residues in the
            activation loop of this enzyme by EC 2.7.12.2, mitogen-activated
            protein kinase kinase (MAPKK) is necessary for enzyme activation.
            Once activated, the enzyme phosphorylates target substrates on
            serine or threonine residues followed by a proline [6]. A
            distinguishing feature of all MAPKs is the conserved sequence
            Thr-Xaa-Tyr (TXY). Mitogen-activated protein kinase (MAPK) signal
            transduction pathways are among the most widespread mechanisms of
            cellular regulation. Mammalian MAPK pathways can be recruited by a
            wide variety of stimuli including hormones (e.g. insulin and growth
            hormone), mitogens (e.g. epidermal growth factor and
            platelet-derived growth factor), vasoactive peptides (e.g.
            angiotensin-II and endothelin), inflammatory cytokines of the tumour
            necrosis factor (TNF) family and environmental stresses such as
            osmotic shock, ionizing radiation and ischaemic injury.
REFERENCE   1  [PMID:2842341]
  AUTHORS   Ray LB, Sturgill TW.
  TITLE     Characterization of insulin-stimulated microtubule-associated
            protein kinase. Rapid isolation and stabilization of a novel
            serine/threonine kinase from 3T3-L1 cells.
  JOURNAL   J. Biol. Chem. 263 (1988) 12721-7.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:1657919]
  AUTHORS   Rossomando AJ, Sanghera JS, Marsden LA, Weber MJ, Pelech SL,
            Sturgill TW.
  TITLE     Biochemical characterization of a family of serine/threonine protein
            kinases regulated by tyrosine and serine/threonine phosphorylations.
  JOURNAL   J. Biol. Chem. 266 (1991) 20270-5.
  ORGANISM  mouse [GN:mmu], Xenopus laevis
REFERENCE   3  [PMID:1321146]
  AUTHORS   Seger R, Ahn NG, Posada J, Munar ES, Jensen AM, Cooper JA, Cobb MH,
            Krebs EG.
  TITLE     Purification and characterization of mitogen-activated protein
            kinase activator(s) from epidermal growth factor-stimulated A431
            cells.
  JOURNAL   J. Biol. Chem. 267 (1992) 14373-81.
  ORGANISM  Xenopus laevis
REFERENCE   4  [PMID:9235954]
  AUTHORS   Stein B, Yang MX, Young DB, Janknecht R, Hunter T, Murray BW,
            Barbosa MS.
  TITLE     p38-2, a novel mitogen-activated protein kinase with distinct
            properties.
  JOURNAL   J. Biol. Chem. 272 (1997) 19509-17.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:10715136]
  AUTHORS   Lisnock J, Griffin P, Calaycay J, Frantz B, Parsons J, O'Keefe SJ,
            LoGrasso P.
  TITLE     Activation of JNK3 alpha 1 requires both MKK4 and MKK7: kinetic
            characterization of in vitro phosphorylated JNK3 alpha 1.
  JOURNAL   Biochemistry. 39 (2000) 3141-8.
  ORGANISM  human [GN:hsa]
REFERENCE   6  [PMID:15187187]
  AUTHORS   Roux PP, Blenis J.
  TITLE     ERK and p38 MAPK-activated protein kinases: a family of protein
            kinases with diverse biological functions.
  JOURNAL   Microbiol. Mol. Biol. Rev. 68 (2004) 320-44.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], mammalian
PATHWAY     PATH: map04010  MAPK signaling pathway
            PATH: map04012  ErbB signaling pathway
            PATH: map04150  mTOR signaling pathway
            PATH: map04310  Wnt signaling pathway
            PATH: map04320  Dorso-ventral axis formation
            PATH: map04350  TGF-beta signaling pathway
            PATH: map04360  Axon guidance
            PATH: map04370  VEGF signaling pathway
            PATH: map04510  Focal adhesion
            PATH: map04520  Adherens junction
            PATH: map04540  Gap junction
            PATH: map04620  Toll-like receptor signaling pathway
            PATH: map04650  Natural killer cell mediated cytotoxicity
            PATH: map04664  Fc epsilon RI signaling pathway
            PATH: map04670  Leukocyte transendothelial migration
            PATH: map04720  Long-term potentiation
            PATH: map04730  Long-term depression
            PATH: map04810  Regulation of actin cytoskeleton
            PATH: map04910  Insulin signaling pathway
            PATH: map04912  GnRH signaling pathway
            PATH: map04914  Progesterone-mediated oocyte maturation
            PATH: map04916  Melanogenesis
            PATH: map04920  Adipocytokine signaling pathway
            PATH: map04930  Type II diabetes mellitus
            PATH: map05120  Epithelial cell signaling in Helicobacter pylori
                            infection
            PATH: map05210  Colorectal cancer
            PATH: map05211  Renal cell carcinoma
            PATH: map05212  Pancreatic cancer
            PATH: map05213  Endometrial cancer
            PATH: map05214  Glioma
            PATH: map05215  Prostate cancer
            PATH: map05216  Thyroid cancer
            PATH: map05218  Melanoma
            PATH: map05219  Bladder cancer
            PATH: map05220  Chronic myeloid leukemia
            PATH: map05221  Acute myeloid leukemia
            PATH: map05223  Non-small cell lung cancer
ORTHOLOGY   KO: K04371  extracellular signal-regulated kinase 1/2
            KO: K04440  c-Jun N-terminal kinase
            KO: K04441  p38 MAP kinase
            KO: K04464  mitogen-activated protein kinase 7
            KO: K04468  nemo like kinase
            KO: K06855  mitogen-activated protein kinase 4/6
            KO: K08293  mitogen-activated protein kinase
GENES       HSA: 1432(MAPK14) 225689(MAPK15) 51701(NLK) 5594(MAPK1)
                 5595(MAPK3) 5596(MAPK4) 5597(MAPK6) 5598(MAPK7) 5599(MAPK8)
                 5600(MAPK11) 5601(MAPK9) 5602(MAPK10) 5603(MAPK13)
                 6300(MAPK12)
            PTR: 450161(MAPK14) 450445(MAPK8) 453439(MAPK6) 454037(MAPK3)
                 454499(MAPK7) 458680(MAPK1) 461358(MAPK10) 462336(MAPK9)
                 462644(MAPK13) 472977(LOC472977)
            MCC: 699736(LOC699736) 715745(MAPK12) 715794(LOC715794)
                 718976(LOC718976)
            MMU: 18099(Nlk) 19094(Mapk11) 225724(Mapk4) 23939(Mapk7)
                 26413(Mapk1) 26414(Mapk10) 26415(Mapk13) 26416(Mapk14)
                 26417(Mapk3) 26419(Mapk8) 26420(Mapk9) 29857(Mapk12)
                 332110(Mapk15) 50772(Mapk6)
            RNO: 116554(Mapk8) 116590(Mapk1) 25272(Mapk10) 286997(Mapk15)
                 29513(Mapk13) 497961(RGD1561602_predicted) 50658(Mapk9)
                 50689(Mapk3) 54268(Mapk4) 58840(Mapk6) 60352(Mapk12)
                 679007(LOC679007) 689314(LOC689314) 81649(Mapk14)
            CFA: 403856(MAPK14) 474652(MAPK9) 477575(MAPK1) 477746(MAPK8)
                 478311(MAPK6) 478464(MAPK10) 479790(LOC479790) 482080(MAPK15)
                 486758(MAPK3) 489532(MAPK7) 491160(NLK) 491690(MAPK4)
                 607019(MAPK11) 607023(MAPK12) 612821(MAPK13)
            BTA: 327672(MAPK1) 507204(LOC507204) 512125(MGC138052)
                 512943(MGC160082) 529183(MGC152151) 531391(LOC531391)
                 534125(MGC137545) 534492(MGC142910) 535327(MAPK13)
                 537631(LOC537631) 538094(MAPK6) 539941(LOC539941)
                 618906(MGC139500)
            SSC: 574062(MAPK12)
            MDO: 100010279(LOC100010279) 100010891(LOC100010891)
                 100026324(LOC100026324) 100028821(LOC100028821)
            GGA: 373953(MAPK1) 395983(MAPK9) 415419(RCJMB04_5i17) 417669(NLK)
                 417739(MAPK11) 421183(MAPK14) 422592(MAPK10) 423778(MAPK8)
                 769763(MAPK12) 771145(MAPK13)
            XLA: 379876(mapk8) 379992(mapk14a) 397785(Xp42) 398592(mapk12)
                 398985(mpk1) 414522(MGC81364) 494669(LOC494669)
            XTR: 448296(mapk14) 549834(mapk12) 549881(mapk1)
            DRE: 266756(mapk14b) 30681(mapk12) 360144(mapk1) 399480(mapk3)
                 406782(mapk4) 415185(zgc:86905) 541323(mapk7) 553780(mapk15)
                 557810(si:dkey-14d8.5) 558298(LOC558298) 562552(LOC562552)
                 562720(LOC562720) 563460(LOC563460) 565830(mapk6)
                 569698(zgc:123234) 573310(LOC573310) 65236(mapk8)
                 65237(mapk14a) 797284(LOC797284)
            SPU: 373525(LOC373525) 574783(LOC574783) 577728(LOC577728)
                 580919(LOC580919) 587330(LOC587330)
            DME: CG12559(rl) Dmel_CG32703 Dmel_CG5475 Dmel_CG5680(bsk)
                 Dmel_CG7393
            CEL: B0218.3(pmk-1) B0478.1(jnk-1) C05D10.2 F42G8.3(pmk-2)
                 F42G8.4(pmk-3) F43C1.2(mpk-1) W06F12.1(lit-1)
            ATH: AT1G10210(ATMPK1) AT2G18170(ATMPK7) AT2G43790(ATMPK6)
                 AT3G45640(ATMPK3) AT3G59790(ATMPK10) AT4G01370(ATMPK4)
                 AT4G11330(ATMPK5)
            OSA: 4332475 4344698
            CME: CMS295C
            SCE: YBL016W(FUS3) YGR040W(KSS1) YHR030C(SLT2) YKL161C(MLP1)
                 YLR113W(HOG1) YPR054W(SMK1)
            AGO: AGOS_ACL191C AGOS_ADL315C AGOS_AER232C AGOS_AFR019W
                 AGOS_AGR048C
            KLA: KLLA0F20053g
            DHA: DEHA0E22110g(DEHA-HOG1)
            PIC: PICST_18249 PICST_33003 PICST_38082(ERK1) PICST_54431
            CAL: CaO19_10404(CaO19.10404) CaO19_7523(CaO19.7523)
                 CaO19_8514(CaO19.8514)
            CGR: CAGL0D01694g CAGL0J00539g CAGL0J04290g CAGL0K04169g
                 CAGL0M11748g
            SPO: SPAC24B11.06c(sty1) SPAC31G5.09c(spk1) SPBC119.08(spm1)
            MGR: MGG_01822
            ANI: AN1017.2 AN3719.2 AN4668.2
            AFM: AFUA_1G12940 AFUA_4G13720 AFUA_6G12820
            AOR: AO090003000402 AO090009000199 AO090020000466 AO090701000642
            CNE: CNC06590 CNE00350 CNE00520 CNI00410
            UMA: UM02357.1 UM03305.1
            DDI: DDB_0191457(erkB) DDB_0201635(erkA)
            PFA: PF14_0294
            CHO: Chro.20213 Chro.30343
            TAN: TA02810
            TET: TTHERM_00195990 TTHERM_00469230
            TBR: Tb10.389.1730 Tb10.61.0250 Tb10.70.2070
            TCR: 506007.40 510295.50 511299.70
            LMA: LmjF33.1380 LmjF36.0720
            EHI: 67.t00005
STRUCTURES  PDB: 1PMQ  2E14  2GMX  2GPH  2GTM  2GTN  2H96  2I0H  2I6L  2NO3  
                 2O0U  2O2U  2OJG  2OJI  2OJJ  2OK1  2OKR  2ONL  2OZA  2P33  
                 2PKJ  2PTJ  2PTO  2PV5  2PV8  2QD9  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.24
            ExPASy - ENZYME nomenclature database: 2.7.11.24
            ExplorEnz - The Enzyme Database: 2.7.11.24
            ERGO genome analysis and discovery system: 2.7.11.24
            BRENDA, the Enzyme Database: 2.7.11.24
///
ENTRY       EC 2.7.11.25                Enzyme
NAME        mitogen-activated protein kinase kinase kinase;
            cMos;
            cRaf;
            MAPKKK;
            MAP3K;
            MAP kinase kinase kinase;
            MEKK;
            MEKK1;
            MEKK2;
            MEKK3;
            MEK kinase;
            Mil/Raf;
            MLK-like mitogen-activated protein triple kinase;
            MLTK;
            MLTKa;
            MLTKb;
            REKS;
            STK28
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:protein phosphotransferase (MAPKKKK-activated)
REACTION    ATP + a protein = ADP + a phosphoprotein [RN:R00162]
ALL_REAC    R00162
SUBSTRATE   ATP [CPD:C00002];
            protein [CPD:C00017]
PRODUCT     ADP [CPD:C00008];
            phosphoprotein [CPD:C00562]
COMMENT     This enzyme phosphorylates and activates its downstream protein
            kinase, EC 2.7.12.2, mitogen-activated protein kinase kinase (MAPKK)
            but requires MAPKKKK for activation. Some members of this family can
            be activated by p21-activated kinases (PAK/STE20) or Ras. While
            c-Raf and c-Mos activate the classical MAPK/ERK pathway, MEKK1 and
            MEKK2 preferentially activate the c-Jun N-terminal protein
            kinase(JNK)/stress-activated protein kinase (SAPK) pathway [2].
            Mitogen-activated protein kinase (MAPK) signal transduction pathways
            are among the most widespread mechanisms of cellular regulation.
            Mammalian MAPK pathways can be recruited by a wide variety of
            stimuli including hormones (e.g. insulin and growth hormone),
            mitogens (e.g. epidermal growth factor and platelet-derived growth
            factor), vasoactive peptides (e.g. angiotensin-II and endothelin),
            inflammatory cytokines of the tumour necrosis factor (TNF) family
            and environmental stresses such as osmotic shock, ionizing radiation
            and ischaemic injury.
REFERENCE   1  [PMID:8940179]
  AUTHORS   Wang XS, Diener K, Jannuzzi D, Trollinger D, Tan TH, Lichenstein H,
            Zukowski M, Yao Z.
  TITLE     Molecular cloning and characterization of a novel protein kinase
            with a catalytic domain homologous to mitogen-activated protein
            kinase kinase kinase.
  JOURNAL   J. Biol. Chem. 271 (1996) 31607-11.
  ORGANISM  mouse [GN:mmu], Drosophila melanogaster [GN:dme], Saccharomyces
            cerevisiae [GN:sce], Schizosaccharomyces pombe [GN:spo]
REFERENCE   2  [PMID:11042189]
  AUTHORS   Gotoh I, Adachi M, Nishida E.
  TITLE     Identification and characterization of a novel MAP kinase kinase
            kinase, MLTK.
  JOURNAL   J. Biol. Chem. 276 (2001) 4276-86.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:8334704]
  AUTHORS   Vojtek AB, Hollenberg SM, Cooper JA.
  TITLE     Mammalian Ras interacts directly with the serine/threonine kinase
            Raf.
  JOURNAL   Cell. 74 (1993) 205-14.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map04010  MAPK signaling pathway
            PATH: map04210  Apoptosis
            PATH: map04310  Wnt signaling pathway
            PATH: map04520  Adherens junction
            PATH: map04530  Tight junction
            PATH: map04540  Gap junction
            PATH: map04620  Toll-like receptor signaling pathway
            PATH: map04660  T cell receptor signaling pathway
            PATH: map04912  GnRH signaling pathway
            PATH: map05120  Epithelial cell signaling in Helicobacter pylori
                            infection
ORTHOLOGY   KO: K04415  mitogen-activated protein kinase kinase kinase 8
            KO: K04416  mitogen-activated protein kinase kinase kinase 1
            KO: K04417  mitogen-activated protein kinase kinase kinase 9
            KO: K04418  mitogen-activated protein kinase kinase kinase 10
            KO: K04419  mitogen-activated protein kinase kinase kinase 11
            KO: K04420  mitogen-activated protein kinase kinase kinase 2
            KO: K04421  mitogen-activated protein kinase kinase kinase 3
            KO: K04422  mitogen-activated protein kinase kinase kinase 13
            KO: K04423  mitogen-activated protein kinase kinase kinase 12
            KO: K04424  sterile alpha motif and leucine zipper containing kinase
                        AZK
            KO: K04425  mitogen-activated protein kinase kinase kinase 6
            KO: K04426  mitogen-activated protein kinase kinase kinase 5
            KO: K04427  mitogen-activated protein kinase kinase kinase 7
            KO: K04428  mitogen-activated protein kinase kinase kinase 4
            KO: K04466  mitogen-activated protein kinase kinase kinase 14
GENES       HSA: 10746(MAP3K2) 1326(MAP3K8) 4214(MAP3K1) 4215(MAP3K3)
                 4216(MAP3K4) 4217(MAP3K5) 4293(MAP3K9) 4294(MAP3K10)
                 4296(MAP3K11) 51776(ZAK) 6885(MAP3K7) 7786(MAP3K12)
                 9020(MAP3K14) 9064(MAP3K6) 9175(MAP3K13)
            PTR: 450384(MAP3K8) 451326(MAP3K11) 451940(MAP3K12) 462888(MAP3K7)
                 467498(MAP3K9)
            MMU: 26401(Map3k1) 26403(Map3k11) 26404(Map3k12) 26405(Map3k2)
                 26406(Map3k3) 26407(Map3k4) 26408(Map3k5) 26409(Map3k7)
                 26410(Map3k8) 269881(Map3k10) 338372(Map3k9) 53608(Map3k6)
                 53859(Map3k14) 65964(B230120H23Rik) 71751(Map3k13)
            RNO: 116596(Map3k8) 116667(Map3k1) 25579(Map3k12)
                 303604(Map3k3_predicted) 303823(LOC303823)
                 308106(Map3k4_predicted) 308463(Map3k10) 309168(Map3k11)
                 311743(RGD1561394_predicted) 313121(Map3k7_predicted)
                 360640(Map3k14_predicted) 500690(RGD1562149_predicted)
                 501558(RGD1560603_predicted)
            CFA: 476215(MAP3K5) 476262(MAP3K4) 478061(MAP3K1)
                 478802(LOC478802) 480481(MAP3K3) 483732(MAP3K11)
                 484504(MAP3K10) 487085(MAP3K8) 487345(MAP3K6) 490765(MAP3K9)
                 490926(MAP3K14) 491765(MAP3K15) 607170(MAP3K12) 612902(MAP3K2)
            BTA: 504592(LOC504592) 505369(MGC179376) 508943(LOC508943)
                 511779(LOC511779) 514210(MGC165851) 520648(LOC520648)
                 523962(LOC523962) 529146(MGC154981) 535622(MGC159463)
                 537380(LOC537380)
            GGA: 419954(MAP3K3) 419964(RCJMB04_34h16) 420479(MAP3K8)
                 421579(MAP3K4) 421688(MAP3K5) 421808(MAP3K7) 424149(ZAK)
                 424225(MAP3K2) 424876(MAP3K13) 427144(MAP3K1)
                 430793(LOC430793) 776822(MAP3K9)
            XLA: 379399(MGC53150) 399459(MAP3K7)
            DRE: 404626(map3k12) 553788(map3k7) 558321(LOC558321)
                 559247(LOC559247) 560211(LOC560211) 560932(LOC560932)
                 563727(LOC563727) 569330(LOC569330)
            SPU: 590385(LOC590385) 590478(LOC590478) 590951(LOC590951)
                 592507(LOC592507) 592876(LOC592876)
            DME: Dmel_CG18492(Tak1) Dmel_CG4720(Pk92B)
            CEL: B0414.7(mtk-1)
            ATH: AT5G11850
            AGO: AGOS_AER264C
            SPO: SPAC9G1.02(wis4)
            ANI: AN1180.2
            AFM: AFUA_1G10940
            AOR: AO090038000313
            DDI: DDB_0214883(rsc21)
            TET: TTHERM_00193390
            EHI: 51.t00028
STRUCTURES  PDB: 2CLQ  2JRH  2NPT  2O2V  2PPH  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.25
            ExPASy - ENZYME nomenclature database: 2.7.11.25
            ExplorEnz - The Enzyme Database: 2.7.11.25
            ERGO genome analysis and discovery system: 2.7.11.25
            BRENDA, the Enzyme Database: 2.7.11.25
///
ENTRY       EC 2.7.11.26                Enzyme
NAME        tau-protein kinase;
            ATP:tau-protein O-hosphotransferase;
            brain protein kinase PK40erk;
            cdk5/p20;
            CDK5/p23;
            glycogen synthase kinase-3beta;
            GSK;
            protein tau kinase;
            STK31;
            tau kinase;
            [tau-protein] kinase;
            tau-protein kinase I;
            tau-protein kinase II;
            tau-tubulin kinase;
            TPK;
            TPK I;
            TPK II;
            TTK
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[tau-protein] O-phosphotransferase
REACTION    ATP + [tau-protein] = ADP + O-phospho-[tau-protein]
ALL_REAC    (other) R03744
SUBSTRATE   ATP [CPD:C00002];
            tau-protein [CPD:C01867]
PRODUCT     ADP [CPD:C00008];
            O-phospho-tau-protein [CPD:C03157]
COMMENT     Activated by tubulin. Involved in the formation of paired helical
            filaments, which are the main fibrous component of all fibrillary
            lesions in brain and are associated with Alzheimer's disease.
REFERENCE   1  [PMID:2467901]
  AUTHORS   Ishiguro K, Ihara Y, Uchida T, Imahori K.
  TITLE     A novel tubulin-dependent protein kinase forming a paired helical
            filament epitope on tau.
  JOURNAL   J. Biochem. (Tokyo). 104 (1988) 319-21.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:11181841]
  AUTHORS   Lund ET, McKenna R, Evans DB, Sharma SK, Mathews WR.
  TITLE     Characterization of the in vitro phosphorylation of human tau by tau
            protein kinase II (cdk5/p20) using mass spectrometry.
  JOURNAL   J. Neurochem. 76 (2001) 1221-32.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:9565682]
  AUTHORS   Michel G, Mercken M, Murayama M, Noguchi K, Ishiguro K, Imahori K,
            Takashima A.
  TITLE     Characterization of tau phosphorylation in glycogen synthase
            kinase-3beta and cyclin dependent kinase-5 activator (p23)
            transfected cells.
  JOURNAL   Biochim. Biophys. Acta. 1380 (1998) 177-82.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:11053853]
  AUTHORS   Aoki M, Iwamoto-Sugai M, Sugiura I, Sasaki C, Hasegawa T, Okumura C,
            Sugio S, Kohno T, Matsuzaki T.
  TITLE     Expression, purification and crystallization of human tau-protein
            kinase I/glycogen synthase kinase-3beta.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 56 ( Pt 11) (2000) 1464-5.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04012  ErbB signaling pathway
            PATH: map04110  Cell cycle
            PATH: map04310  Wnt signaling pathway
            PATH: map04340  Hedgehog signaling pathway
            PATH: map04360  Axon guidance
            PATH: map04510  Focal adhesion
            PATH: map04662  B cell receptor signaling pathway
            PATH: map04910  Insulin signaling pathway
            PATH: map04916  Melanogenesis
            PATH: map05010  Alzheimer's disease
            PATH: map05210  Colorectal cancer
            PATH: map05213  Endometrial cancer
            PATH: map05215  Prostate cancer
            PATH: map05217  Basal cell carcinoma
ORTHOLOGY   KO: K03083  glycogen synthase kinase 3 beta
            KO: K05960  tau-protein kinase
            KO: K08815  tau tubulin kinase
            KO: K08822  glycogen synthase kinase 3 alpha
GENES       HSA: 146057(TTBK2) 2931(GSK3A) 2932(GSK3B) 84630(TTBK1)
            PTR: 453368(TTBK2)
            MMU: 140810(Ttbk2) 56637(Gsk3b) 606496(Gsk3a)
            RNO: 311349(Ttbk1_predicted) 316229(RGD1559518_predicted)
                 50686(Gsk3a) 84027(Gsk3b)
            CFA: 474910(LOC474910) 478575(GSK3B) 484476(GSK3A) 487520(TTBK2)
            BTA: 534761(LOC534761) 536561(MGC159759) 541215(LOC541215)
            GGA: 416713(TTBK1) 418335(GSK3B) 423241(TTBK2)
            DRE: 30654(gsk3b) 30664(gsk3a) 557460(LOC557460) 567393(LOC567393)
                 569881(si:dkey-12h9.11) 571094(LOC571094)
            SPU: 764638(LOC764638)
            DME: Dmel_CG11533 Dmel_CG2621(sgg)
            CEL: R90.1 Y18D10A.5(gsk-3)
            ATH: AT5G14640
            OSA: 4326720 4341251
            CNE: CNB00720
            DDI: DDB_0216336
            TBR: Tb927.4.1700
            TCR: 504057.170
            LMA: LmjF34.3020
STRUCTURES  PDB: 2JDO  2JDR  2UW9  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.26
            ExPASy - ENZYME nomenclature database: 2.7.11.26
            ExplorEnz - The Enzyme Database: 2.7.11.26
            ERGO genome analysis and discovery system: 2.7.11.26
            BRENDA, the Enzyme Database: 2.7.11.26
            CAS: 111694-09-8
///
ENTRY       EC 2.7.11.27                Enzyme
NAME        [acetyl-CoA carboxylase] kinase;
            acetyl coenzyme A carboxylase kinase (phosphorylating);
            acetyl-CoA carboxylase bound kinase;
            acetyl-CoA carboxylase kinase;
            acetyl-CoA carboxylase kinase (cAMP-independent);
            acetyl-CoA carboxylase kinase 2;
            acetyl-CoA carboxylase kinase-2;
            acetyl-CoA carboxylase kinase-3 (AMP-activated);
            acetyl-coenzyme A carboxylase kinase;
            ACK2;
            ACK3;
            AMPK;
            I-peptide kinase;
            STK5
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[acetyl-CoA carboxylase] phosphotransferase
REACTION    ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase]
            phosphate [RN:R03272]
ALL_REAC    R03272
SUBSTRATE   ATP [CPD:C00002];
            [acetyl-CoA carboxylase] [CPD:C01139]
PRODUCT     ADP [CPD:C00008];
            [acetyl-CoA carboxylase] phosphate [CPD:C01247]
COMMENT     Phosphorylates and inactivates EC 6.4.1.2, acetyl-CoA carboxylase,
            which can be dephosphorylated and reactivated by EC 3.1.3.17,
            [phosphorylase] phosphatase. The enzyme is more active towards the
            dimeric form of acetyl-CoA carboxylase than the polymeric form [5].
            Phosphorylates serine residues.
REFERENCE   1  [PMID:2879833]
  AUTHORS   Jamil H, Madsen NB.
  TITLE     Phosphorylation state of acetyl-coenzyme A carboxylase. I. Linear
            inverse relationship to activity ratios at different citrate
            concentrations.
  JOURNAL   J. Biol. Chem. 262 (1987) 630-7.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6120170]
  AUTHORS   Lent B, Kim KH.
  TITLE     Purification and properties of a kinase which phosphorylates and
            inactivates acetyl-CoA carboxylase.
  JOURNAL   J. Biol. Chem. 257 (1982) 1897-901.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:6146523]
  AUTHORS   Munday MR, Hardie DG.
  TITLE     Isolation of three cyclic-AMP-independent acetyl-CoA carboxylase
            kinases from lactating rat mammary gland and characterization of
            their effects on enzyme activity.
  JOURNAL   Eur. J. Biochem. 141 (1984) 617-27.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:7907095]
  AUTHORS   Mohamed AH, Huang WY, Huang W, Venkatachalam KV, Wakil SJ.
  TITLE     Isolation and characterization of a novel acetyl-CoA carboxylase
            kinase from rat liver.
  JOURNAL   J. Biol. Chem. 269 (1994) 6859-65.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:9475166]
  AUTHORS   Heesom KJ, Moule SK, Denton RM.
  TITLE     Purification and characterisation of an insulin-stimulated
            protein-serine kinase which phosphorylates acetyl-CoA carboxylase.
  JOURNAL   FEBS. Lett. 422 (1998) 43-6.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K05959  [acetyl-CoA carboxylase] kinase
GENES       CAL: CaO19_1936(CaO19.1936)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.27
            ExPASy - ENZYME nomenclature database: 2.7.11.27
            ExplorEnz - The Enzyme Database: 2.7.11.27
            ERGO genome analysis and discovery system: 2.7.11.27
            BRENDA, the Enzyme Database: 2.7.11.27
            CAS: 77000-06-7
///
ENTRY       EC 2.7.11.28                Enzyme
NAME        tropomyosin kinase;
            tropomyosin kinase (phosphorylating);
            STK
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:tropomyosin O-phosphotransferase
REACTION    ATP + tropomyosin = ADP + O-phosphotropomyosin [RN:R02980]
ALL_REAC    R02980
SUBSTRATE   ATP [CPD:C00002];
            tropomyosin [CPD:C00839]
PRODUCT     ADP [CPD:C00008];
            O-phosphotropomyosin [CPD:C03016]
COMMENT     The enzyme phosphorylates casein equally well, and histone and
            phosvitin to a lesser extent. The acceptor is a serine residue in
            the protein.
REFERENCE   1  [PMID:3593768]
  AUTHORS   deBelle I, Mak AS.
  TITLE     Isolation and characterization of tropomyosin kinase from chicken
            embryo.
  JOURNAL   Biochim. Biophys. Acta. 925 (1987) 17-26.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:6325440]
  AUTHORS   Montgomery K, Mak AS.
  TITLE     In vitro phosphorylation of tropomyosin by a kinase from chicken
            embryo.
  JOURNAL   J. Biol. Chem. 259 (1984) 5555-60.
  ORGANISM  chicken [GN:gga]
REFERENCE   3  [PMID:3166994]
  AUTHORS   Watson MH, Taneja AK, Hodges RS, Mak AS.
  TITLE     Phosphorylation of alpha alpha- and beta beta-tropomyosin and
            synthetic peptide analogues.
  JOURNAL   Biochemistry. 27 (1988) 4506-12.
  ORGANISM  chicken [GN:gga]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.28
            ExPASy - ENZYME nomenclature database: 2.7.11.28
            ExplorEnz - The Enzyme Database: 2.7.11.28
            ERGO genome analysis and discovery system: 2.7.11.28
            BRENDA, the Enzyme Database: 2.7.11.28
            CAS: 90804-56-1
///
ENTRY       EC 2.7.11.29                Enzyme
NAME        low-density-lipoprotein receptor kinase;
            ATP:low-density-lipoprotein-L-serine O-phosphotransferase;
            LDL receptor kinase;
            [low-density-lipoprotein] kinase;
            low-density lipoprotein kinase;
            low-density-lipoprotein receptor kinase (phosphorylating);
            STK7
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[low-density-lipoprotein receptor]-L-serine O-phosphotransferase
REACTION    ATP + [low-density-lipoprotein receptor]-L-serine = ADP +
            [low-density-lipoprotein receptor]-O-phospho-L-serine
ALL_REAC    (other) R04403
SUBSTRATE   ATP [CPD:C00002];
            [low-density-lipoprotein receptor]-L-serine
PRODUCT     ADP [CPD:C00008];
            [low-density-lipoprotein receptor]-O-phospho-L-serine
COMMENT     Phosphorylates the last serine residue (Ser-833) in the cytoplasmic
            domain of the low-density lipoprotein receptor from bovine adrenal
            cortex. Casein can also act as a substrate but with lower affinity.
            GTP can act instead of ATP.
REFERENCE   1  [PMID:3100530]
  AUTHORS   Kishimoto A, Brown MS, Slaughter CA, Goldstein JL.
  TITLE     Phosphorylation of serine 833 in cytoplasmic domain of low density
            lipoprotein receptor by a high molecular weight enzyme resembling
            casein kinase II.
  JOURNAL   J. Biol. Chem. 262 (1987) 1344-51.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:3597414]
  AUTHORS   Kishimoto A, Goldstein JL, Brown MS.
  TITLE     Purification of catalytic subunit of low density lipoprotein
            receptor kinase and identification of heat-stable activator protein.
  JOURNAL   J. Biol. Chem. 262 (1987) 9367-73.
  ORGANISM  cow [GN:bta]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.29
            ExPASy - ENZYME nomenclature database: 2.7.11.29
            ExplorEnz - The Enzyme Database: 2.7.11.29
            ERGO genome analysis and discovery system: 2.7.11.29
            BRENDA, the Enzyme Database: 2.7.11.29
            CAS: 107445-00-1
///
ENTRY       EC 2.7.11.30                Enzyme
NAME        receptor protein serine/threonine kinase;
            activin receptor kinase;
            receptor type I serine/threonine protein kinase;
            receptor type II serine/threonine protein kinase;
            STK13;
            TGF-beta kinase;
            receptor serine/threonine protein kinase
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[receptor-protein] phosphotransferase
REACTION    ATP + [receptor-protein] = ADP + [receptor-protein] phosphate
ALL_REAC    (other) R00162
SUBSTRATE   ATP [CPD:C00002];
            [receptor-protein]
PRODUCT     ADP [CPD:C00008];
            [receptor-protein] phosphate
COMMENT     The transforming growth factor beta (TGF-beta) family of cytokines
            regulates cell proliferation, differentiation, recognition and
            death. Signalling occurs by the binding of ligand to the type II
            receptor, which is the constitutively active kinase. Bound TGF-beta
            is then recognized by receptor I, which is phosphorylated and can
            propagate the signal to downstream substrates [1,3].
REFERENCE   1  [PMID:8047140]
  AUTHORS   Wrana JL, Attisano L, Wieser R, Ventura F, Massague J.
  TITLE     Mechanism of activation of the TGF-beta receptor.
  JOURNAL   Nature. 370 (1994) 341-7.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:10733523]
  AUTHORS   Massague J, Chen YG.
  TITLE     Controlling TGF-beta signaling.
  JOURNAL   Genes. Dev. 14 (2000) 627-44.
  ORGANISM  Caenorhabditis elegans [GN:cel], mammalian
REFERENCE   3  [PMID:9153220]
  AUTHORS   de Caestecker MP, Hemmati P, Larisch-Bloch S, Ajmera R, Roberts AB,
            Lechleider RJ.
  TITLE     Characterization of functional domains within Smad4/DPC4.
  JOURNAL   J. Biol. Chem. 272 (1997) 13690-6.
  ORGANISM  Caenorhabditis elegans [GN:cel]
PATHWAY     PATH: map04010  MAPK signaling pathway
            PATH: map04060  Cytokine-cytokine receptor interaction
            PATH: map04350  TGF-beta signaling pathway
            PATH: map04520  Adherens junction
            PATH: map05210  Colorectal cancer
            PATH: map05212  Pancreatic cancer
            PATH: map05220  Chronic myeloid leukemia
ORTHOLOGY   KO: K04388  transforming growth factor, beta receptor II
            KO: K04669  transforming growth factor, beta, other
            KO: K04670  activin receptor, type II
            KO: K04671  bone morphogenetic protein receptor, type II
            KO: K04672  anti-Mullerian hormone receptor, type II
            KO: K04673  bone morphogenetic protein receptor, type I
            KO: K04674  transforming growth factor, beta receptor I
            KO: K04675  activin receptor, type I
GENES       HSA: 130399(ACVR1C) 269(AMHR2) 657(BMPR1A) 658(BMPR1B) 659(BMPR2)
                 7046(TGFBR1) 7048(TGFBR2) 90(ACVR1) 91(ACVR1B) 92(ACVR2A)
                 93(ACVR2B) 94(ACVRL1)
            PTR: 450572(BMPR1A) 451910(ACVRL1) 460243(TGFBR2) 461683(BMPR1B)
                 467005(AMHR2) 470564(ACVR1C) 470565(ACVR1) 472992(TGFBR1)
                 745829(LOC745829)
            MCC: 696898(LOC696898) 705474(LOC705474)
            MMU: 110542(Amhr2) 11477(Acvr1) 11479(Acvr1b) 11480(Acvr2a)
                 11481(Acvr2b) 11482(Acvrl1) 12166(Bmpr1a) 12167(Bmpr1b)
                 12168(Bmpr2) 21812(Tgfbr1) 21813(Tgfbr2) 269275(Acvr1c)
            RNO: 140590(Bmpr2) 245921(Acvr1c) 25237(Acvrl1) 25366(Acvr2b)
                 29263(Acvr2a) 29381(Acvr1b) 29530(Amhr2) 29591(Tgfbr1)
                 310914(Bmpr1b) 79558(Acvr1) 81507(Bmpr1a) 81810(Tgfbr2)
            CFA: 476140(ACVR2A) 477039(TGFBR2) 477603(ACVRL1) 478757(ACVR1)
                 478875(LOC478875) 481628(TGFBR1) 485590(ACVR2B) 486506(AMHR2)
                 486537(ACVR1B) 488361(ACVR1C) 489077(BMPR1A) 609202(LOC609202)
            BTA: 281598(ACVR2) 282131(ACVR2B) 282382(TGFBR1) 338068(ACVR1)
                 404101(BMPR1A) 407127(bmprii) 407128(BMPRIB) 535376(LOC535376)
                 536380(LOC536380)
            SSC: 396665(ALK-5) 396691(BMPR1B) 448845(ACVR2B)
            MDO: 100016370(LOC100016370) 100026839(LOC100026839)
            GGA: 374094(TGFBR1) 374147(BMPR2) 374213(ACVR2B) 395246(ACVR1)
                 396030(BMPR1B) 396308(BMPR1A) 396324(ACVR2A) 396399(TGFBR2)
                 424325(ACVR1C) 768878(ACVR1B)
            XLA: 397711(LOC397711) 397712(LOC397712) 397859(XSTK2)
                 399083(xALK-2) 399103(sax) 399283(Acvr2) 399295(X-TrR1)
            XTR: 448641(acvr2b) 548715(tgfbr1) 550111(acvr1) 780089(bmpr1b)
            DRE: 30183(acvr1b) 30457(acvr2b) 30615(acvr1) 30739(tgfbr2)
                 30742(bmpr1b) 447846(bmpr1ab) 553359(acvr2a) 555655(bmpr2b)
                 560578(zgc:123263) 58145(bmpr1a)
            SPU: 574893(LOC574893) 580712(LOC580712) 586095(LOC586095)
                 590282(LOC590282)
            DME: Dmel_CG16987(Alp23B) Dmel_CG1838 Dmel_CG31695(scw)
                 Dmel_CG7904(put)
            CEL: B0412.2(daf-7) C05D2.1(daf-4) C32D5.2(sma-6) C53D6.2(unc-129)
                 F39G3.8(tig-2)
STRUCTURES  PDB: 2GOO  2H62  2H64  2HLQ  2HLR  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.30
            ExPASy - ENZYME nomenclature database: 2.7.11.30
            ExplorEnz - The Enzyme Database: 2.7.11.30
            ERGO genome analysis and discovery system: 2.7.11.30
            BRENDA, the Enzyme Database: 2.7.11.30
///
ENTRY       EC 2.7.11.31                Enzyme
NAME        [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase;
            AMPK;
            AMP-activated protein kinase;
            HMG-CoA reductase kinase;
            beta-hydroxy-beta-methylglutaryl-CoA reductase kinase;
            [hydroxymethylglutaryl-CoA reductase (NADPH2)] kinase;
            3-hydroxy-3-methylglutaryl coenzyme A reductase kinase;
            3-hydroxy-3-methylglutaryl-CoA reductase kinase;
            hydroxymethylglutaryl coenzyme A reductase kinase;
            hydroxymethylglutaryl coenzyme A reductase kinase (phosphorylating);
            hydroxymethylglutaryl-CoA reductase kinase;
            reductase kinase;
            STK29
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-serine/threonine kinases
SYSNAME     ATP:[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphotransferase
REACTION    ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = ADP +
            [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate [RN:R04555]
ALL_REAC    R04555
SUBSTRATE   ATP [CPD:C00002];
            [hydroxymethylglutaryl-CoA reductase (NADPH)] [CPD:C04632]
PRODUCT     ADP [CPD:C00008];
            [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate [CPD:C04768]
COMMENT     The enzyme is activated by AMP. EC 1.1.1.34,
            hydroxymethylglutaryl-CoA reductase (NADPH) is inactivated by the
            phosphorylation of the enzyme protein. Histones can also act as
            acceptors. The enzyme can also phosphorylate hepatic acetyl-CoA
            carboxylase (EC 6.4.1.2) and adipose hormone-sensitive lipase (EC
            3.1.1.79) [5]. Thr-172 within the catalytic subunit (alpha-subunit)
            is the major site phosphorylated by the AMP-activated protein kinase
            kinase [7]. GTP can act instead of ATP [4]
REFERENCE   1  [PMID:278983]
  AUTHORS   Beg ZH, Stonik JA, Brewer HB Jr.
  TITLE     3-Hydroxy-3-methylglutaryl coenzyme A reductase: regulation of
            enzymatic activity by phosphorylation and dephosphorylation.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 75 (1978) 3678-82.
  ORGANISM  rat [GN:rno], human [GN:hsa]
REFERENCE   2  [PMID:216867]
  AUTHORS   Gibson DM, Ingebritsen TS.
  TITLE     Reversible modulation of liver hydroxymethylglutaryl CoA reductase.
  JOURNAL   Life. Sci. 23 (1978) 2649-64.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:666819]
  AUTHORS   Ingebritsen TS, Lee HS, Parker RA, Gibson DM.
  TITLE     Reversible modulation of the activities of both liver microsomal
            hydroxymethylglutaryl coenzyme A reductase and its inactivating
            enzyme. Evidence for regulation by
            phosphorylation-dephosphorylation.
  JOURNAL   Biochem. Biophys. Res. Commun. 81 (1978) 1268-77.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:3689494]
  AUTHORS   Ferrer A, Caelles C, Massot N, Hegardt FG.
  TITLE     Allosteric activation of rat liver microsomal
            [hydroxymethylglutaryl-CoA reductase (NADPH)]kinase by nucleoside
            phosphates.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 368 (1987) 249-57.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:7902296]
  AUTHORS   Weekes J, Ball KL, Caudwell FB, Hardie DG.
  TITLE     Specificity determinants for the AMP-activated protein kinase and
            its plant homologue analysed using synthetic peptides.
  JOURNAL   FEBS. Lett. 334 (1993) 335-9.
  ORGANISM  rat [GN:rno]
REFERENCE   6  [PMID:9857077]
  AUTHORS   Crute BE, Seefeld K, Gamble J, Kemp BE, Witters LA.
  TITLE     Functional domains of the alpha1 catalytic subunit of the
            AMP-activated protein kinase.
  JOURNAL   J. Biol. Chem. 273 (1998) 35347-54.
  ORGANISM  rat [GN:rno], human [GN:hsa]
REFERENCE   7  [PMID:10642499]
  AUTHORS   Stein SC, Woods A, Jones NA, Davison MD, Carling D.
  TITLE     The regulation of AMP-activated protein kinase by phosphorylation.
  JOURNAL   Biochem. J. 345 Pt 3 (2000) 437-43.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K05958  [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase
GENES       PIC: PICST_65458(KIN2) PICST_68332(SNF1)
            CAL: CaO19_1936(CaO19.1936) CaO19_4347(CaO19.4347)
                 CaO19_7510(CaO19.7510)
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.11.31
            ExPASy - ENZYME nomenclature database: 2.7.11.31
            ExplorEnz - The Enzyme Database: 2.7.11.31
            ERGO genome analysis and discovery system: 2.7.11.31
            BRENDA, the Enzyme Database: 2.7.11.31
            CAS: 172522-01-9
///
ENTRY       EC 2.7.12.1                 Enzyme
NAME        dual-specificity kinase;
            ADK1;
            Arabidopsis dual specificity kinase 1;
            CLK1;
            dDYRK2;
            Mps1p
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Dual-specificity kinases (those acting on Ser/Thr and Tyr residues)
SYSNAME     ATP:protein phosphotransferase (Ser/Thr- and Tyr-phosphorylating)
REACTION    ATP + a protein = ADP + a phosphoprotein [RN:R00162]
ALL_REAC    R00162
SUBSTRATE   ATP [CPD:C00002];
            protein [CPD:C00017]
PRODUCT     ADP [CPD:C00008];
            phosphoprotein [CPD:C00562]
COMMENT     This family of enzymes can phosphorylate both Ser/Thr and Tyr
            residues.
REFERENCE   1  [PMID:7527390]
  AUTHORS   Ali N, Halfter U, Chua NH.
  TITLE     Cloning and biochemical characterization of a plant protein kinase
            that phosphorylates serine, threonine, and tyrosine.
  JOURNAL   J. Biol. Chem. 269 (1994) 31626-9.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   2  [PMID:7737118]
  AUTHORS   Lauze E, Stoelcker B, Luca FC, Weiss E, Schutz AR, Winey M.
  TITLE     Yeast spindle pole body duplication gene MPS1 encodes an essential
            dual specificity protein kinase.
  JOURNAL   EMBO. J. 14 (1995) 1655-63.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:10954422]
  AUTHORS   Menegay HJ, Myers MP, Moeslein FM, Landreth GE.
  TITLE     Biochemical characterization and localization of the dual
            specificity kinase CLK1.
  JOURNAL   J. Cell. Sci. 113 ( Pt 18) (2000) 3241-53.
  ORGANISM  Arabidopsis thaliana [GN:ath], Drosophila melanogaster [GN:dme],
            mouse [GN:mmu], human [GN:hsa]
REFERENCE   4  [PMID:12786602]
  AUTHORS   Lochhead PA, Sibbet G, Kinstrie R, Cleghon T, Rylatt M, Morrison DK,
            Cleghon V.
  TITLE     dDYRK2: a novel dual-specificity tyrosine-phosphorylation-regulated
            kinase in Drosophila.
  JOURNAL   Biochem. J. 374 (2003) 381-91.
  ORGANISM  Drosophila melanogaster [GN:dme], human [GN:hsa]
PATHWAY     PATH: map04111  Cell cycle - yeast
ORTHOLOGY   KO: K02559  ser/thr protein kinase MPS1 (regulatory cell
                        proliferation kinase 1)
            KO: K08287  dual-specificity kinase
            KO: K08823  CDC-like kinase
            KO: K08825  dual-specificity tyrosine-(Y)-phosphorylation regulated
                        kinase
            KO: K08841  testis-specific kinase 1
            KO: K08842  testis-specific kinase 2
            KO: K08866  TTK protein kinase
GENES       HSA: 10420(TESK2) 1195(CLK1) 1196(CLK2) 1198(CLK3) 1859(DYRK1A)
                 57396(CLK4) 7016(TESK1) 7272(TTK) 8444(DYRK3) 8445(DYRK2)
                 8798(DYRK4) 9149(DYRK1B)
            PTR: 452061(DYRK2) 453742(CLK3) 456030(DYRK1B) 458545(DYRK1A)
                 459865(CLK1) 462844(TTK) 465074(TESK1) 466926(DYRK4)
                 469142(DYRK3) 469181(TESK2) 471811(CLK4)
            MMU: 101320(Dyrk4) 102414(Clk3) 12747(Clk1) 12748(Clk2)
                 12750(Clk4) 13548(Dyrk1a) 13549(Dyrk1b) 21754(Tesk1)
                 22137(Ttk) 226419(Dyrk3) 230661(Tesk2) 69181(Dyrk2)
            RNO: 170908(Tesk2) 171305(Clk3) 25255(Dyrk1a) 29460(Tesk1)
                 301434(Clk1) 304775(Dyrk3) 308468(Dyrk1b_predicted)
                 312721(Rad51ap1_predicted) 314862(Dyrk2_predicted)
                 315852(Ttk_predicted) 365842(LOC365842)
            CFA: 474645(CLK4) 477720(LOC477720) 478367(CLK3) 478866(LOC478866)
                 480010(LOC480010) 481152(LOC481152) 481895(TTK) 484506(DYRK1B)
                 487755(DYRK1A) 490427(CLK2) 608657(TESK2)
            BTA: 505149(LOC505149) 505499(CLK3) 507571(DYRK1A)
                 514916(LOC514916) 524925(LOC524925) 527643(LOC527643)
                 529633(LOC529633) 531276(LOC531276) 532989(LOC532989)
                 539979(LOC539979) 613808(MGC148790)
            GGA: 395233(DYRK1A) 415295(CLK3) 416295(CLK4) 419846(LOC419846)
                 421849(TTK) 424596(TESK2) 425060(RCJMB04_20c6)
                 427864(RCJMB04_23i19)
            XLA: 379763(clk2) 379954(dyrk1a) 496058(LOC496058)
            XTR: 493520(MGC89944) 496828(clk2) 549675(LOC549675)
                 549894(LOC549894)
            DRE: 317763(ttk) 556048(LOC556048) 556212(LOC556212) 557602(dyrk2)
                 558981(LOC558981) 564001(LOC564001) 568213(zgc:158349)
            SPU: 579475(LOC579475) 581224(LOC581224) 592598(LOC592598)
                 594612(LOC594612) 757175(LOC757175)
            DME: CG40478 Dmel_CG40478 Dmel_CG4551(smi35A) Dmel_CG6027(cdi)
                 Dmel_CG7826(mnb)
            CEL: F49E11.1(mbk-2) F52C9.7 T04C10.1(mbk-1)
            OSA: 4327372 4333851
            CME: CMB064C CMB108C CMR245C
            SCE: YDL028C(MPS1) YLL019C(KNS1)
            AGO: AGOS_ADL043C AGOS_ADR317C
            PIC: PICST_34686(KNS1) PICST_47887(MPS1) PICST_81803(YAK1)
            CAL: CaO19_4979(CaO19.4979) CaO19_7293(CaO19.7293)
            CGR: CAGL0D06600g CAGL0K01617g
            SPO: SPAC1D4.11c(lkh1)
            ANI: AN0988.2 AN2927.2 AN7104.2 AN7678.2
            AFM: AFUA_1G16780 AFUA_2G01520 AFUA_4G03850
            AOR: AO090005001004 AO090005001468 AO090011000341 AO090701000798
            CNE: CNA06620 CNI01240 CNI03350
            UMA: UM04543.1
            DDI: DDB_0220499(mps1) DDB_0229429(dyrk1) DDB_0230102(dyrk2)
                 DDB_0230105(clkA)
            PFA: PF14_0431
            CHO: Chro.50371
            TAN: TA19110
            TPV: TP01_0149
            TET: TTHERM_00348940
            LMA: LmjF09.0400 LmjF15.0180
            EHI: 277.t00007 48.t00021
STRUCTURES  PDB: 2VAG  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.12.1
            ExPASy - ENZYME nomenclature database: 2.7.12.1
            ExplorEnz - The Enzyme Database: 2.7.12.1
            ERGO genome analysis and discovery system: 2.7.12.1
            BRENDA, the Enzyme Database: 2.7.12.1
///
ENTRY       EC 2.7.12.2                 Enzyme
NAME        mitogen-activated protein kinase kinase;
            MAP kinase kinase;
            MAP kinase kinase 4;
            MAP kinase kinase 7;
            MAP kinase or ERK kinase;
            MAP2K;
            MAPKK;
            MAPKK1;
            MEK;
            MEK1;
            MEK2;
            MKK;
            MKK2;
            MKK4;
            MKK6;
            MKK7;
            STK27
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Dual-specificity kinases (those acting on Ser/Thr and Tyr residues)
SYSNAME     ATP:protein phosphotransferase (MAPKKK-activated)
REACTION    ATP + a protein = ADP + a phosphoprotein [RN:R00162]
ALL_REAC    R00162
SUBSTRATE   ATP [CPD:C00002];
            protein [CPD:C00017]
PRODUCT     ADP [CPD:C00008];
            phosphoprotein [CPD:C00562]
COMMENT     This enzyme is a dual-specific protein kinase and requires
            mitogen-activated protein kinase kinase kinase (MAPKKK) for
            activation. It is required for activation of EC 2.7.11.24,
            mitogen-activated protein kinase. Phosphorylation of MEK1 by Raf
            involves phosphorylation of two serine residues [5].
            Mitogen-activated protein kinase (MAPK) signal transduction pathways
            are among the most widespread mechanisms of cellular regulation.
            Mammalian MAPK pathways can be recruited by a wide variety of
            stimuli including hormones (e.g. insulin and growth hormone),
            mitogens (e.g. epidermal growth factor and platelet-derived growth
            factor), vasoactive peptides (e.g. angiotensin-II and endothelin),
            inflammatory cytokines of the tumour necrosis factor (TNF) family
            and environmental stresses such as osmotic shock, ionizing radiation
            and ischaemic injury.
REFERENCE   1  [PMID:8004006]
  AUTHORS   Mordret G.
  TITLE     MAP kinase kinase: a node connecting multiple pathways.
  JOURNAL   Biol. Cell. 79 (1993) 193-207.
  ORGANISM  human [GN:hsa], rat [GN:rno], Schizosaccharomyces pombe [GN:spo],
            mouse [GN:mmu], rabbit, Xenopus laevis, Saccharomyces cerevisiae
            [GN:sce], Drosophila melanogaster [GN:dme]
REFERENCE   2  [PMID:8388392]
  AUTHORS   Zheng CF, Guan KL.
  TITLE     Cloning and characterization of two distinct human extracellular
            signal-regulated kinase activator kinases, MEK1 and MEK2.
  JOURNAL   J. Biol. Chem. 268 (1993) 11435-9.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:8393135]
  AUTHORS   Wu J, Harrison JK, Dent P, Lynch KR, Weber MJ, Sturgill TW.
  TITLE     Identification and characterization of a new mammalian
            mitogen-activated protein kinase kinase, MKK2.
  JOURNAL   Mol. Cell. Biol. 13 (1993) 4539-48.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:8157000]
  AUTHORS   Alessi DR, Saito Y, Campbell DG, Cohen P, Sithanandam G, Rapp U,
            Ashworth A, Marshall CJ, Cowley S.
  TITLE     Identification of the sites in MAP kinase kinase-1 phosphorylated by
            p74raf-1.
  JOURNAL   EMBO. J. 13 (1994) 1610-9.
  ORGANISM  rabbit
REFERENCE   5  [PMID:7731726]
  AUTHORS   Pham CD, Arlinghaus RB, Zheng CF, Guan KL, Singh B.
  TITLE     Characterization of MEK1 phosphorylation by the v-Mos protein.
  JOURNAL   Oncogene. 10 (1995) 1683-8.
REFERENCE   6  [PMID:8621675]
  AUTHORS   Han J, Lee JD, Jiang Y, Li Z, Feng L, Ulevitch RJ.
  TITLE     Characterization of the structure and function of a novel MAP kinase
            kinase (MKK6).
  JOURNAL   J. Biol. Chem. 271 (1996) 2886-91.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04010  MAPK signaling pathway
            PATH: map04012  ErbB signaling pathway
            PATH: map04320  Dorso-ventral axis formation
            PATH: map04370  VEGF signaling pathway
            PATH: map04510  Focal adhesion
            PATH: map04540  Gap junction
            PATH: map04620  Toll-like receptor signaling pathway
            PATH: map04650  Natural killer cell mediated cytotoxicity
            PATH: map04664  Fc epsilon RI signaling pathway
            PATH: map04720  Long-term potentiation
            PATH: map04730  Long-term depression
            PATH: map04810  Regulation of actin cytoskeleton
            PATH: map04910  Insulin signaling pathway
            PATH: map04912  GnRH signaling pathway
            PATH: map04914  Progesterone-mediated oocyte maturation
            PATH: map04916  Melanogenesis
            PATH: map05120  Epithelial cell signaling in Helicobacter pylori
                            infection
            PATH: map05210  Colorectal cancer
            PATH: map05211  Renal cell carcinoma
            PATH: map05212  Pancreatic cancer
            PATH: map05213  Endometrial cancer
            PATH: map05214  Glioma
            PATH: map05215  Prostate cancer
            PATH: map05216  Thyroid cancer
            PATH: map05218  Melanoma
            PATH: map05219  Bladder cancer
            PATH: map05220  Chronic myeloid leukemia
            PATH: map05221  Acute myeloid leukemia
            PATH: map05223  Non-small cell lung cancer
ORTHOLOGY   KO: K04368  mitogen-activated protein kinase kinase 1
            KO: K04369  mitogen-activated protein kinase kinase 2
            KO: K04430  mitogen-activated protein kinase kinase 4
            KO: K04431  mitogen-activated protein kinase kinase 7
            KO: K04432  mitogen-activated protein kinase kinase 3
            KO: K04433  mitogen-activated protein kinase kinase 6
            KO: K04463  mitogen-activated protein kinase kinase 5
            KO: K08294  mitogen-activated protein kinase kinase
            KO: K08865  PDZ-binding kinase
GENES       HSA: 55872(PBK) 5604(MAP2K1) 5605(MAP2K2) 5606(MAP2K3)
                 5607(MAP2K5) 5608(MAP2K6) 5609(MAP2K7) 6416(MAP2K4)
            PTR: 450188(MAP2K1) 453532(MAP2K5) 454515(MAP2K3) 455065(MAP2K4)
                 456390(MAP2K2) 464496(PBK) 468310(MAP2K6) 743199(MAP2K7)
            MMU: 23938(Map2k5) 26395(Map2k1) 26396(Map2k2) 26397(Map2k3)
                 26398(Map2k4) 26399(Map2k6) 26400(Map2k7) 52033(Pbk)
            RNO: 114495(Map2k6) 170851(Map2k1) 287398(Map2k4)
                 290326(Pbk_predicted) 29568(Map2k5) 303200(Map2k3)
                 363855(Map2k7) 58960(Map2k2)
            CFA: 477371(PBK) 478347(MAP2K1) 480454(MAP2K6) 485004(MAP2K7)
                 489508(MAP2K4) 489547(MAP2K3) 609559(LOC609559) 611939(MAP2K2)
            BTA: 286883(MAP2K6) 510434(MGC134398) 516039(MGC151903)
                 526469(MGC140244) 533199(LOC533199) 534781(MGC165897)
                 787278(LOC787278)
            GGA: 396349(MAP2K2) 415549(MAP2K1) 415557(RCJMB04_36h7)
                 416496(RCJMB04_8f10) 417312(MAP2K4) 422003(PBK)
            XLA: 379638(MGC68865) 379991(mek-2) 394391(map2k7-A)
                 414694(MGC83167) 496340(LOC496340)
            XTR: 448132(map2k6) 493420(map2k1) 496810(TGas097i05.1)
                 549042(LOC549042) 613115(map2k7)
            DRE: 360218(pbk) 403052(zMKK4) 406728(map2k1) 560913(LOC560913)
                 564496(LOC564496) 568951(LOC568951) 65239(map2k3)
            SPU: 581169(LOC581169) 591137(LOC591137) 594211(LOC594211)
            DME: Dmel_CG12244(lic) Dmel_CG15793(Dsor1) Dmel_CG4353(hep)
                 Dmel_CG9738(Mkk4)
            CEL: F42G10.2(mkk-4) Y54E10BL.6(mek-2)
            OSA: 4340126
            SCE: YDL159W(STE7) YJL128C(PBS2) YOR231W(MKK1)
            AGO: AGOS_ACR117W AGOS_ACR196C AGOS_AFL217C
            PIC: PICST_35816 PICST_40600
            CAL: CaO19.6889 CaO19_7388(CaO19.7388)
            CGR: CAGL0J03828g CAGL0L05632g
            SPO: SPBC409.07c(wis1) SPBC543.07(skh1)
            ANI: AN0931.2 AN4189.2
            AFM: AFUA_1G05800 AFUA_1G15950
            AOR: AO090005001093 AO090009000347
            CNE: CNA07470 CNC02350 CNE01930
            UMA: UM01514.1 UM06342.1
STRUCTURES  PDB: 2DYL  2NPT  2O2V  2P55  2QK6  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.12.2
            ExPASy - ENZYME nomenclature database: 2.7.12.2
            ExplorEnz - The Enzyme Database: 2.7.12.2
            ERGO genome analysis and discovery system: 2.7.12.2
            BRENDA, the Enzyme Database: 2.7.12.2
///
ENTRY       EC 2.7.13.1                 Enzyme
NAME        protein-histidine pros-kinase;
            ATP:protein-L-histidine N-pros-phosphotransferase;
            histidine kinase (ambiguous);
            histidine protein kinase (ambiguous);
            protein histidine kinase (ambiguous);
            protein kinase (histidine) (ambiguous);
            HK2
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-histidine kinases
SYSNAME     ATP:protein-L-histidine Npi-phosphotransferase
REACTION    ATP + protein L-histidine = ADP + protein Npi-phospho-L-histidine
            [RN:R02625]
ALL_REAC    R02625
SUBSTRATE   ATP [CPD:C00002];
            protein L-histidine [CPD:C00615]
PRODUCT     ADP [CPD:C00008];
            protein Npi-phospho-L-histidine
COMMENT     A number of histones can act as acceptor.
REFERENCE   1  [PMID:7196259]
  AUTHORS   Fujitaki JM, Fung G, Oh EY, Smith RA.
  TITLE     Characterization of chemical and enzymatic acid-labile
            phosphorylation of histone H4 using phosphorus-31 nuclear magnetic
            resonance.
  JOURNAL   Biochemistry. 20 (1981) 3658-64.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4066704]
  AUTHORS   Huebner VD, Matthews HR.
  TITLE     Phosphorylation of histidine in proteins by a nuclear extract of
            Physarum polycephalum plasmodia.
  JOURNAL   J. Biol. Chem. 260 (1985) 16106-13.
  ORGANISM  Physarum polycephalum
ORTHOLOGY   KO: K05962  protein-histidine pros-kinase
GENES       AZO: azo0053(rstB) azo0165(phoR) azo0263 azo0408(cheA1)
                 azo0458(ragB) azo0518(nifL) azo0568(vsrA) azo0918(dctS)
                 azo0976(basS) azo1451(cheA2) azo1462(cheA3) azo1492(divJ)
                 azo1504(moxY) azo2402(barA) azo2575(gacS) azo2672
                 azo2715(fleS) azo2746(envZ2) azo2768(yfhK) azo2799(kdpD1)
                 azo2945(copS) azo2979(elmS) azo3094(kdpD2) azo3159(colS)
                 azo3357(pilS) azo3616(envZ3) azo3673(qseC2) azo3810(hoxJ)
                 azo3909(mnsA) azo3983(ntrY)
            RBA: RB2008
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.13.1
            ExPASy - ENZYME nomenclature database: 2.7.13.1
            ExplorEnz - The Enzyme Database: 2.7.13.1
            ERGO genome analysis and discovery system: 2.7.13.1
            BRENDA, the Enzyme Database: 2.7.13.1
            CAS: 99283-67-7
///
ENTRY       EC 2.7.13.2                 Enzyme
NAME        protein-histidine tele-kinase;
            ATP:protein-L-histidine N-tele-phosphotransferase;
            histidine kinase (ambiguous);
            histidine protein kinase (ambiguous);
            protein histidine kinase (ambiguous);
            protein kinase (histidine) (ambiguous);
            HK3
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-histidine kinases
SYSNAME     ATP:protein-L-histidine Ntau-phosphotransferase
REACTION    ATP + protein L-histidine = ADP + protein Ntau-phospho-L-histidine
            [RN:R02626]
ALL_REAC    R02626
SUBSTRATE   ATP [CPD:C00002];
            protein L-histidine [CPD:C00615]
PRODUCT     ADP [CPD:C00008];
            protein Ntau-phospho-L-histidine
COMMENT     A number of histones can act as acceptor.
REFERENCE   1  [PMID:7196259]
  AUTHORS   Fujitaki JM, Fung G, Oh EY, Smith RA.
  TITLE     Characterization of chemical and enzymatic acid-labile
            phosphorylation of histone H4 using phosphorus-31 nuclear magnetic
            resonance.
  JOURNAL   Biochemistry. 20 (1981) 3658-64.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4066704]
  AUTHORS   Huebner VD, Matthews HR.
  TITLE     Phosphorylation of histidine in proteins by a nuclear extract of
            Physarum polycephalum plasmodia.
  JOURNAL   J. Biol. Chem. 260 (1985) 16106-13.
  ORGANISM  Physarum polycephalum
GENES       ABO: ABO_2000
            CVI: CV_0074(pilS)
            BPU: BPUM_2915
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.13.2
            ExPASy - ENZYME nomenclature database: 2.7.13.2
            ExplorEnz - The Enzyme Database: 2.7.13.2
            ERGO genome analysis and discovery system: 2.7.13.2
            BRENDA, the Enzyme Database: 2.7.13.2
            CAS: 99283-67-7
///
ENTRY       EC 2.7.13.3                 Enzyme
NAME        histidine kinase;
            EnvZ;
            histidine kinase (ambiguous);
            histidine protein kinase (ambiguous);
            protein histidine kinase (ambiguous);
            protein kinase (histidine) (ambiguous);
            HK1;
            HP165;
            Sln1p
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Protein-histidine kinases
SYSNAME     ATP:protein-L-histidine N-phosphotransferase
REACTION    ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
SUBSTRATE   ATP [CPD:C00002];
            protein L-histidine [CPD:C00615]
PRODUCT     ADP [CPD:C00008];
            protein N-phospho-L-histidine
COMMENT     This entry has been included to accommodate those protein-histidine
            kinases for which the phosphorylation site has not been established
            (i.e. either the pros- or tele-nitrogen of histidine). A number of
            histones can act as acceptor.
REFERENCE   1  [PMID:12110368]
  AUTHORS   Kowluru A.
  TITLE     Identification and characterization of a novel protein histidine
            kinase in the islet beta cell: evidence for its regulation by
            mastoparan, an activator of G-proteins and insulin secretion.
  JOURNAL   Biochem. Pharmacol. 63 (2002) 2091-100.
  ORGANISM  charomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:14752661]
  AUTHORS   Yoshimi A, Tsuda M, Tanaka C.
  TITLE     Cloning and characterization of the histidine kinase gene Dic1 from
            Cochliobolus heterostrophus that confers dicarboximide resistance
            and osmotic adaptation.
  JOURNAL   Mol. Genet. Genomics. 271 (2004) 228-36.
  ORGANISM  Cochliobolus heterostrophus
REFERENCE   3  [PMID:10735847]
  AUTHORS   Beier D, Frank R.
  TITLE     Molecular characterization of two-component systems of Helicobacter
            pylori.
  JOURNAL   J. Bacteriol. 182 (2000) 2068-76.
  ORGANISM  Helicobacter pylori
REFERENCE   4  [PMID:15109719]
  AUTHORS   Pflock M, Dietz P, Schar J, Beier D.
  TITLE     Genetic evidence for histidine kinase HP165 being an acid sensor of
            Helicobacter pylori.
  JOURNAL   FEMS. Microbiol. Lett. 234 (2004) 51-61.
  ORGANISM  Helicobacter pylori
REFERENCE   5  [PMID:8132603]
  AUTHORS   Roberts DL, Bennett DW, Forst SA.
  TITLE     Identification of the site of phosphorylation on the osmosensor,
            EnvZ, of Escherichia coli.
  JOURNAL   J. Biol. Chem. 269 (1994) 8728-33.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map02020  Two-component system - General
            PATH: map02030  Bacterial chemotaxis - General
            PATH: map02031  Bacterial chemotaxis - Organism-specific
            PATH: map03090  Type II secretion system
ORTHOLOGY   KO: K02476  two-component system, CitB family, sensor kinase
            KO: K02478  two-component system, LytT family, sensor kinase
            KO: K02480  two-component system, NarL family, sensor kinase
            KO: K02482  two-component system, NtrC family, sensor kinase
            KO: K02484  two-component system, OmpR family, sensor kinase
            KO: K02486  two-component system, unclassified family, sensor kinase
            KO: K02489  two-component system, PleD related family, sensor kinase
            KO: K02491  two-component system, sporulation family, sensor
                        sporulation kinase A
            KO: K02668  two-component system sensor kinase PilS
            KO: K03407  two-component system, chemotaxis family, sensor kinase
                        CheA
            KO: K07636  two-component system, OmpR family, phosphate regulon
                        sensor histidine kinase PhoR
            KO: K07637  two-component system, OmpR family, sensor histidine
                        kinase PhoQ
            KO: K07638  two-component system, OmpR family, osmolarity sensor
                        histidine kinase EnvZ
            KO: K07639  two-component system, OmpR family, sensor histidine
                        kinase RstB
            KO: K07640  two-component system, OmpR family, sensor histidine
                        kinase CpxA
            KO: K07641  two-component system, OmpR family, sensor histidine
                        kinase CreC
            KO: K07642  two-component system, OmpR family, sensor histidine
                        kinase BaeS
            KO: K07643  two-component system, OmpR family, sensor histidine
                        kinase BasS
            KO: K07644  two-component system, OmpR family, heavy metal sensor
                        histidine kinase CusS
            KO: K07645  two-component system, OmpR family, sensor histidine
                        kinase QseC
            KO: K07646  two-component system, OmpR family, sensor histidine
                        kinase KdpD
            KO: K07647  two-component system, OmpR family, sensor histidine
                        kinase TorS
            KO: K07648  two-component system, OmpR family, aerobic respiration
                        control sensor histidine kinase ArcB
            KO: K07649  two-component system, OmpR family, sensor histidine
                        kinase TctE
            KO: K07650  two-component system, OmpR family, sensor histidine
                        kinase CssS
            KO: K07651  two-component system, OmpR family, sensor histidine
                        kinase ResE
            KO: K07652  two-component system, OmpR family, sensor histidine
                        kinase VicK
            KO: K07653  two-component system, OmpR family, sensor histidine
                        kinase MprB
            KO: K07654  two-component system, OmpR family, sensor histiidine
                        kinase MtrB
            KO: K07655  two-component system, OmpR family, sensor histidine
                        kinase PrrB
            KO: K07656  two-component system, OmpR family, sensor histidine
                        kinase TcrS
            KO: K07673  two-component system, NarL family, nitrate/nitrite
                        sensor histidine kinase NarX
            KO: K07674  two-component system, NarL family, nitrate/nitrite
                        sensor histidine kinase NarQ
            KO: K07675  two-component system, NarL family, sensor histidine
                        kinase UhpB
            KO: K07676  two-component system, NarL family, sensor histidine
                        kinase YojN
            KO: K07677  two-component system, NarL family, capsular synthesis
                        sensor histidine kinase RcsC
            KO: K07678  two-component system, NarL family, sensor histidine
                        kinase BarA
            KO: K07679  two-component system, NarL family, sensor histidine
                        kinase EvgS
            KO: K07680  two-component system, NarL family, sensor histidine
                        kinase ComP
            KO: K07681  two-component system, NarL family, vancomycin resistance
                        sensor histidine kinase VraS
            KO: K07682  two-component system, NarL family, sensor histidine
                        kinase DevS
            KO: K07683  two-component system, NarL family, sensor histidine
                        kinase NreB
            KO: K07697  two-component system, sporulation family, sensor
                        sporulation kinase B
            KO: K07698  two-component system, sporulation family, sensor
                        sporulation kinase C
            KO: K07700  two-component system, CitB family, cit operon sensor
                        histidine kinase CitA
            KO: K07701  two-component system, CitB family, sensor histidine
                        kinase DcuS
            KO: K07704  two-component system, LytT family, sensor histidine
                        kinase LytS
            KO: K07706  two-component system, AgrA family, sensor histidine
                        kinase AgrC
            KO: K07708  two-component system, NtrC family, nitrogen regulation
                        sensor histidine kinase GlnL
            KO: K07709  two-component system, NtrC family, sensor histidine
                        kinase HydH
            KO: K07710  two-component system, NtrC family, sensor histidine
                        kinase AtoS
            KO: K07711  two-component system, NtrC family, sensor histidine
                        kinase YfhK
            KO: K07716  two-component system, PleD family, sensor histidine
                        kinase PleC
            KO: K07717  two-component system, sensor histidine kinase YcbA
            KO: K07718  two-component system, sensor histidine kinase YesM
            KO: K07768  two-component system, OmpR family, sensor histidine
                        kinase SenX3
            KO: K07769  two-component system, OmpR family, snsor histidine
                        kinase NblS
            KO: K07777  two-component system, NarL family, sensor histidine
                        kinase DegS
            KO: K07778  two-component system, NarL family, sensor histidine
                        kinase DesK
            KO: K08082  two-component system, sensor histidine kinase, alginate
                        biosynthesis protein AlgZ/FimS
            KO: K08475  two-component system, NtrC family, phosphoglycerate
                        transport system sensor histidine kinase PgtB
            KO: K08479  two-component system, OmpR family, clock-associated
                        histidine kinase SasA
            KO: K10125  two-component system, NarL family, C4-dicarboxylate
                        transport sensor histidine kinase DctB
GENES       CFA: 484891(OR08D07)
            ATH: AT2G18790(PHYB)
            SCE: YDL235C(YPD1)
            AGO: AGOS_ABL182C
            CAL: CaO19.4443
            SPO: SPAC27E2.09 SPBC725.02 SPCC74.06
            ANI: AN2005.2
            AOR: AO090003001194
            CNE: CNM01530
            ECO: b0400(phoR) b0570(cusS) b0619(citA) b0695(kdpD) b0993(torS)
                 b1129(phoQ) b1222(narX) b1609(rstB) b1968(yedV) b2078(baeS)
                 b2126(yehU) b2216(yojN) b2218(rcsC) b2219(atoS) b2370(evgS)
                 b2380(ypdA) b2469(narQ) b2556(yfhK) b2786(barA) b3026(ygiY)
                 b3210(arcB) b3404(envZ) b3668(uhpB) b3869(glnL) b3911(cpxA)
                 b4003(zraS) b4112(basS) b4125(dcuS) b4399(creC)
            ECJ: JW0390(phoR) JW0611(citA) JW0683(kdpD) JW1115(phoQ)
                 JW1213(narX) JW1601(rstB) JW1951(yedV) JW2063(baeS)
                 JW2204(rcsD) JW2213(atoS) JW2367(evgS) JW2453(narQ)
                 JW2757(barA) JW2994(qseC) JW3367(envZ) JW3643(uhpB)
                 JW3840(glnL) JW3882(cpxA) JW3967(zraS) JW4073(basS)
                 JW4086(dcuS) JW4362(creC) JW5082(cusS) JW5135(torS)
                 JW5353(yehU) JW5388(ypdA) JW5407(yfhK) JW5536(arcB)
                 JW5920(rcsC)
            ECE: Z0462 Z0498(phoR) Z0708(ybcZ) Z0764(citA) Z0842(kdpD)
                 Z1410(torS) Z1858(phoQ) Z1998(narX) Z2610(rstB) Z3060(yedV)
                 Z3247(baeS) Z3303(yehU) Z3475(yojN) Z3477(rcsC) Z3632(evgS)
                 Z3645 Z3726(narQ) Z3833(yfhK) Z4101(barA) Z4378(qseC)
                 Z4574(arcB) Z4759(envZ) Z5158(uhpB) Z5405(glnL) Z5456(cpxA)
                 Z5579(hydH) Z5714(basS) Z5727(yjdH) Z6002(creC)
            ECS: ECs0417 ECs0450 ECs0608 ECs0658 ECs0723 ECs1148 ECs1601
                 ECs1727 ECs2315 ECs2706 ECs2886 ECs2937 ECs3105 ECs3107
                 ECs3249 ECs3260 ECs3331 ECs3422 ECs3646 ECs4089 ECs4246
                 ECs4605 ECs4791 ECs4837 ECs4926 ECs5094 ECs5107 ECs5357
            ECC: c0509(phoR) c0656(cusS) c0710(citA) c0780(kdpD) c1128(torS)
                 c1508(phoQ) c1682(narX) c2001(rstB) c2386(yedV) c2604(baeS)
                 c2656(yehU) c2759(yojN) c2761(rcsC) c2762(atoS) c2906(evgS)
                 c2919(ypdA) c2996(narQ) c3079(yfhK) c3349(barA) c3765(ygiY)
                 c3970(arcB) c4180(envZ) c4592(uhpB) c4818(glnL) c4863(cpxA)
                 c4961(hydH) c5041 c5117(basS) c5131(yjdH) c5203(pgtB)
                 c5486(creC)
            ECI: UTI89_C0421(phoR) UTI89_C0570(cusS) UTI89_C0623(dpiB)
                 UTI89_C0699(kdpD) UTI89_C1056(torS) UTI89_C1258(phoQ)
                 UTI89_C1418(narX) UTI89_C1797(rstB) UTI89_C2167(yedV)
                 UTI89_C2353(baeS) UTI89_C2398(yehU) UTI89_C2498(yojN)
                 UTI89_C2500(rcsC) UTI89_C2501(atoS) UTI89_C2702(evgS)
                 UTI89_C2712(ypdA) UTI89_C2795(narQ) UTI89_C2876(yfhK)
                 UTI89_C3156(barA) UTI89_C3451(qseC) UTI89_C3646(arcB)
                 UTI89_C3816(zraS) UTI89_C3904(envZ) UTI89_C4224(uhpB)
                 UTI89_C4458(glnL) UTI89_C4495(cpxA) UTI89_C4639
                 UTI89_C4706(basS) UTI89_C4719(yjdH) UTI89_C5172(creC)
            ECP: ECP_0459 ECP_0601 ECP_0650 ECP_0991 ECP_1124 ECP_1271
                 ECP_1553 ECP_1901 ECP_2118 ECP_2259 ECP_2261 ECP_2262 ECP_2395
                 ECP_2406 ECP_2481 ECP_2558 ECP_2767 ECP_3113 ECP_3298 ECP_3490
                 ECP_3874 ECP_4080 ECP_4121 ECP_4216 ECP_4282 ECP_4355 ECP_4368
                 ECP_4785
            ECV: APECO1_1168(baeS) APECO1_1372(kdpD) APECO1_1433(dpiB)
                 APECO1_1478(cusS) APECO1_1610(phoR) APECO1_1980(creC)
                 APECO1_2327(yjdH) APECO1_2339(basS) APECO1_2402
                 APECO1_2472(zraS) APECO1_2557(cpxA) APECO1_2593(glnL)
                 APECO1_2784(uhpB) APECO1_3060(envZ) APECO1_3225(arcB)
                 APECO1_339(narX) APECO1_3395(qseC) APECO1_3508(pgtB)
                 APECO1_3745(barA) APECO1_3975(yfhK) APECO1_4157(ypdA)
                 APECO1_4166(evgS) APECO1_4340(atoS) APECO1_4341(rcsC)
                 APECO1_4343(yojN) APECO1_4423(yehU) APECO1_692(rstB)
                 APECO1_86(torS) APECO1_936(cheA)
            ECW: EcE24377A_0588(cusS) EcE24377A_0721(kdpD)
                 EcE24377A_1292(phoQ) EcE24377A_1372(narX) EcE24377A_1817(rstB)
                 EcE24377A_2121(cheA) EcE24377A_2515(yojN) EcE24377A_3090(barA)
                 EcE24377A_4391(glnL) EcE24377A_4998(creC)
            ECX: EcHS_A0617(cusS) EcHS_A0742(kdpD) EcHS_A1249 EcHS_A1331
                 EcHS_A1684(rstB) EcHS_A1984(cheA) EcHS_A2356(yojN)
                 EcHS_A2930(barA) EcHS_A4096(glnL) EcHS_A4635(creC)
            STY: STY0433(phoR) STY0674(dpiB) STY0744(kdpD) STY1127(copS)
                 STY1270(phoQ) STY1286(narX) STY1651(rstB) STY2343(baeS)
                 STY2389(yehU) STY2494(yojN) STY2496(rcsC) STY2634(pgtB)
                 STY2718(narQ) STY2811 STY2903(tctE) STY3096(barA) STY3355
                 STY3507(arcB) STY3712(hydH) STY3813(cpxA) STY3875(glnL)
                 STY3951(torS) STY3993(uhpB) STY4295(envZ) STY4490(pmrB)
                 STY4502(dcuS) STY4936(creC)
            STT: t0292 t0379(narQ) t0461(pgtB) t0594(rcsC) t0596(yojN)
                 t0696(yehU) t0742(baeS) t1339(rstB) t1676(narX) t1690(phoQ)
                 t1824(copS) t2173(kdpD) t2242(dpiB) t2466(phoR) t2678(tctE)
                 t2867(barA) t3099 t3245(arcB) t3458(hydH) t3561(cpxA)
                 t3615(glnL) t3692(torS) t3729(uhpB) t4005(envZ) t4198(pmrB)
                 t4211(dcuS) t4628(creC)
            SPT: SPA0302(yfhK) SPA0593(rcsC) SPA0595(yojN) SPA0692(yehU)
                 SPA0735(baeS) SPA1107(narX) SPA1384(rstB) SPA1620(phoQ)
                 SPA1755(copS) SPA2038(kdpD) SPA2325(phoR) SPA2640(tctE)
                 SPA2823(barA) SPA3047(ygiY) SPA3196(arcB) SPA3366(envZ)
                 SPA3676(torS) SPA3847(glnL) SPA3901(cpxA) SPA4010(hydH)
                 SPA4109(pmrB) SPA4399(creC)
            SEC: SC0439(phoR) SC0599(cusS) SC0655(dpiB) SC0723(kdpD)
                 SC1045(copS) SC1181(phoQ) SC1488(rstB) SC1760(narX)
                 SC2132(baeS) SC2175(yehU) SC2272(yojN) SC2274(rcsC)
                 SC2398(pgtB) SC2559(yfhK) SC2715(tctE) SC2898(barA)
                 SC3122(ygiY) SC3266(arcB) SC3433(envZ) SC3709(uhpB)
                 SC3743(torS) SC3898(ntrB) SC3949(cpxA) SC4054(hydH)
                 SC4170(basS) SC4182(dcuS) SC4434(creC)
            STM: STM0398(phoR) STM0561 STM0625(dpiB) STM0703(kdpD)
                 STM1095(copS) STM1230(phoQ) STM1471(rstB) STM1766(narX)
                 STM2130(baeS) STM2159(yehU) STM2269(yojN) STM2271(rcsC)
                 STM2397(pgtB) STM2480(narQ) STM2564(yfhK) STM2784(tctE)
                 STM2958(barA) STM3178(ygiY) STM3328(arcB) STM3501(envZ)
                 STM3789(uhpB) STM3826(torS) STM4006(glnL) STM4058(cpxA)
                 STM4173(hydH) STM4291(basS) STM4304(dcuS) STM4589(creC)
            YPE: YPO0023(ntrB) YPO0073(cpxA) YPO0137(envZ) YPO0895(creC)
                 YPO1217(rcsC) YPO1633(phoQ) YPO1959(narX) YPO2000
                 YPO2309(rstB) YPO2689(kdpD) YPO2916 YPO3204(phoR)
                 YPO3381(barA) YPO3508(basS) YPO3555(arcB) YPO3943
            YPK: y0069(cpxA) y0126(arcB) y0676(basS) y0808(barA) y0979(phoR)
                 y1262(kdpD) y1313 y1793(phoQ) y2140(rstB) y2308 y2351(narX)
                 y2387 y2968 y2969 y2971(rcsC) y3279(creC) y3805(glnL)
                 y3820(uhpB) y3885 y3917(envZ) y4032
            YPM: YP_0024(ntrB) YP_0073(cpxA) YP_0138(envZ) YP_0304(barA)
                 YP_0575(basS) YP_0728(phoR) YP_0920(rcsC) YP_0984(baeS2)
                 YP_1666(baeS3) YP_1704(narX) YP_1763(phoQ) YP_1847(baeS4)
                 YP_2492(kdpD1) YP_2541(baeS5) YP_2718(baeS8) YP_3305 YP_3370
                 YP_3591(creC) YP_3809(arcB)
            YPA: YPA_0058 YPA_0374 YPA_0931 YPA_0933 YPA_0934 YPA_1084
                 YPA_1302 YPA_1342 YPA_1382 YPA_1657 YPA_1891 YPA_2290 YPA_2355
                 YPA_2419 YPA_2697 YPA_2880 YPA_3332 YPA_3470 YPA_3519 YPA_3748
                 YPA_3772 YPA_3835
            YPN: YPN_0250 YPN_0710 YPN_0885 YPN_1176 YPN_1222 YPN_1287
                 YPN_1480 YPN_1769 YPN_1998 YPN_2760 YPN_3094 YPN_3252 YPN_3437
                 YPN_3591 YPN_3656 YPN_3778 YPN_3928
            YPP: YPDSF_2202
            YPS: YPTB0023(ntrB) YPTB0069(cpxA) YPTB0468(basS) YPTB0750(barA)
                 YPTB0918(phoR) YPTB1204 YPTB1257(rcsC) YPTB1259(yojN) YPTB1922
                 YPTB1957(narX) YPTB1992 YPTB2231(rstB) YPTB2435(phoQ)
                 YPTB2817(baeS) YPTB2876 YPTB2919(kdpD) YPTB3170(creC)
                 YPTB3500(arcB) YPTB3763(envZ) YPTB3788 YPTB3846(uhpB)
            YPI: YpsIP31758_0026(ntrB) YpsIP31758_0083(cpxA)
                 YpsIP31758_0876(creC) YpsIP31758_1103(kdpD)
                 YpsIP31758_1211(baeS) YpsIP31758_1607(phoQ)
                 YpsIP31758_1638(cheA) YpsIP31758_1825(rstB)
                 YpsIP31758_2123(narX) YpsIP31758_2765(rcsC)
                 YpsIP31758_3322(barA) YpsIP31758_3608(basS)
                 YpsIP31758_3979(envZ) YpsIP31758_4079(uhpB)
            YEN: YE0026(glnR) YE0085(cpxA) YE0422(basS) YE0742(barA) YE1035
                 YE1105(baeS) YE1396(rcsC)
            SFL: SF0337(phoR) SF0471(ybcZ) SF0995(torS) SF1148(phoQ)
                 SF1225(narX) SF1632(rstB) SF2015(yedV) SF2143(baeS)
                 SF2198(yehU) SF2300(yojN) SF2302(rcsC) SF2437(evgS)
                 SF2603(yfhK) SF2799(barA) SF3067(ygiY) SF3250(arcB)
                 SF3423(envZ) SF3793(uhpB) SF3939(glnL) SF3990(cpxA)
                 SF4075(hydH) SF4098(dcuS) SF4111(basS) SF4431(creC)
            SFX: S0345(phoR) S0479(ybcZ) S1231(phoQ) S1309(narX) S1763(rstB)
                 S2112(yedV) S2268(baeS) S2325(yehU) S2431(yojN) S2433(rcsC)
                 S2574(evgS) S2775(yfhK) S2993(barA) S3271(ygiY) S3468(arcB)
                 S3619(basS) S3632(yjdH) S3660(hydH) S3758(cpxA) S3807(glnL)
                 S3975(uhpB) S4340(envZ) S4702(creC)
            SFV: SFV_0365(phoR) SFV_0503(ybcZ) SFV_1004(torS) SFV_1164(phoQ)
                 SFV_1238(narX) SFV_1625(rstB) SFV_1934(cheA) SFV_2013(yedV)
                 SFV_2139(baeS) SFV_2182(yehU) SFV_2291(yojN) SFV_2293(rcsC)
                 SFV_2429(evgS) SFV_2438 SFV_2604(yfhK) SFV_2671(barA)
                 SFV_3072(qseC) SFV_3240(arcB) SFV_3409(envZ) SFV_3582(cpxA)
                 SFV_3632(glnL) SFV_3841(uhpB) SFV_4075(hydH) SFV_4105(yjdH)
                 SFV_4118(basS) SFV_4433(creC)
            SSN: SSON_0377(phoR) SSON_0521(ybcZ) SSON_0572(citA)
                 SSON_0646(kdpD) SSON_1001(torS) SSON_1147(phoQ)
                 SSON_1551(rstB) SSON_1955(narX) SSON_2026(yedV)
                 SSON_2130(baeS) SSON_2172(yehU) SSON_2275(yojN)
                 SSON_2277(rcsC) SSON_2278(atoS) SSON_2461(evgS)
                 SSON_2549(narQ) SSON_2639(yfhK) SSON_2943(barA)
                 SSON_3165(qseC) SSON_3358(arcB) SSON_3535(envZ)
                 SSON_3622(uhpB) SSON_4041(glnL) SSON_4081(cpxA)
                 SSON_4176(hydH) SSON_4287(basS) SSON_4302(yjdH)
                 SSON_4549(creC)
            SBO: SBO_0294(phoR) SBO_0557(kdpD) SBO_0904(baeS) SBO_0949(yehU)
                 SBO_1038(yedV) SBO_1527(rstB) SBO_1844(narX) SBO_1910(phoQ)
                 SBO_2089(rcsC) SBO_2091(yojN) SBO_2238(torS) SBO_2396(evgS)
                 SBO_2406 SBO_2485(narQ) SBO_2584(yfhK) SBO_2667(barA)
                 SBO_2885(qseC) SBO_3172(arcB) SBO_3391(envZ) SBO_3701(uhpB)
                 SBO_3881(glnL) SBO_3929(cpxA) SBO_4024(hydH) SBO_4139(basS)
                 SBO_4329(yjdH) SBO_4462(creC)
            SDY: SDY_0507 SDY_0856(rcsC) SDY_0858(yojN) SDY_1276(narX)
                 SDY_1825(rstB) SDY_2023(phoQ) SDY_2163(yehU) SDY_2187(baeS)
                 SDY_2579 SDY_2653(narQ) SDY_2746(yfhK) SDY_3003(barA)
                 SDY_3213(qseC) SDY_3391(arcB) SDY_3672(envZ) SDY_3723(hydH)
                 SDY_3835(cpxA) SDY_3874(glnL) SDY_4101(basS) SDY_4149(uhpB)
                 SDY_4238(yjdH) SDY_4478(evgS)
            ECA: ECA0007(qseC) ECA0028(glnL) ECA0314(arcB) ECA1111(phoR)
                 ECA1202(rcsC) ECA1204 ECA1339(kdpD) ECA1496(uhpB)
                 ECA1900(narQ) ECA2012(rstB) ECA2029(narX) ECA2432
                 ECA2446(pehS) ECA2577(citA) ECA3188(baeS) ECA3257
                 ECA3571(rpfA) ECA4045(pmrB) ECA4107(envZ) ECA4152
                 ECA4312(cpxA) ECA4399(dcuS)
            PLU: plu0213(envZ) plu0236(glnL) plu0814(uhpB) plu0908(barA)
                 plu1417(kdpD) plu2284(bvgS) plu2777(baeS) plu2808(phoQ)
                 plu3047 plu3049(rcsC) plu3178(tctE) plu3313 plu3910(phoR)
                 plu4008(arcB) plu4795(cpxA)
            SGL: SG0220 SG0508 SG0960 SG1081 SG1579 SG1581 SG2181 SG2231
                 SG2318
            SPE: Spro_0790 Spro_3268 Spro_4735
            HIN: HI0220(arcB) HI0267(narQ) HI1378(phoR) HI1707(ygiY)
            HIT: NTHI0321(arcB) NTHI0374(narQ) NTHI1779(phoR) NTHI2015(qseC)
            HDU: HD1470(cpxA)
            HSO: HS_0402(arcB) HS_1510(narQ)
            PMU: PM0215(ygiY) PM0313(arcB) PM0431(phoR) PM1339(uhpB)
                 PM1591(narQ) PM1888(cpxA)
            MSU: MS1244(baeS) MS1730(baeS) MS1914(baeS) MS2286(baeS)
                 MS2288(baeS)
            APL: APL_0627 APL_1064(qseC) APL_1256(phoR)
            XFA: XF0323 XF0390 XF1625 XF1849 XF2592
            XFT: PD0266(tctE) PD1020(ntrB) PD1154(algZ) PD1678(phoQ)
                 PD1969(phoR)
            XCC: XCC0188(ntrB) XCC0705(kdpD) XCC0962(phoR) XCC2694(creC)
                 XCC3348 XCC3351(tctE) XCC3395 XCC3513(algZ) XCC3942(phoQ)
            XCB: XC_0197 XC_0647 XC_0769 XC_0813 XC_0818 XC_1421 XC_3273
                 XC_3529 XC_4030
            XCV: XCV0191(ntrB) XCV0335 XCV0677 XCV0783 XCV0811(kdpD)
                 XCV1071(phoR) XCV2965 XCV3014(creC) XCV3601 XCV3610(tctE)
                 XCV4115(phoQ)
            XAC: XAC0207(ntrB) XAC0326(smeS) XAC0620(algZ) XAC0729
                 XAC0759(kdpD) XAC1041(phoR) XAC2804(baeS) XAC2854(creC)
                 XAC3473 XAC3482(tctE) XAC4022(phoQ)
            XOO: XOO0424(phoQ) XOO1106(tctE) XOO1115 XOO1189 XOO1558(baeS)
                 XOO3667(phoR) XOO3843(kdpD) XOO3871 XOO4009(algZ)
                 XOO4484(ntrB)
            XOM: XOO_0386(XOO0386) XOO_1004(XOO1004) XOO_1012(XOO1012)
                 XOO_1084(XOO1084) XOO_1371(XOO1371) XOO_1446(XOO1446)
                 XOO_1475(XOO1475) XOO_2483(XOO2483) XOO_2693(XOO2693)
                 XOO_3464(XOO3464) XOO_3621(XOO3621) XOO_3652(XOO3652)
                 XOO_3780(XOO3780) XOO_4225(XOO4225)
            VCH: VC0694 VC0720(phoR) VC0791(citA) VC1276 VC1521 VC1639
                 VC1653(vieS) VC1925 VC2369(fexB) VC2453 VC2693(cpxA)
                 VC2713(envZ) VC2748 VCA0531 VCA0675(narQ) VCA0683(uhpB)
                 VCA0709(torS)
            VVU: VV1_0025 VV1_0467 VV1_0502 VV1_0550(fexB) VV1_0857(envZ)
                 VV1_0891(ntrB) VV1_1253 VV1_1573 VV1_2686 VV2_0125 VV2_0137
                 VV2_0512 VV2_0719 VV2_0992 VV2_1277
            VVY: VV0197(ntrB) VV0237(envZ) VV0644 VV0692 VV0724 VV1101
                 VV1603(citA) VV1711 VV2823 VV3114 VVA0112 VVA0633 VVA0647
                 VVA1062 VVA1188(narQ) VVA1485
            VPA: VP0119 VP0155(envZ) VP0362 VP0487(fexB) VP0539 VP0570(phoR)
                 VP0915 VP1503 VP1712(citA) VP1735 VP1908 VP2567 VP2859(cpxA)
                 VPA0675(torS) VPA0965(uhpB) VPA1196(narQ)
            VFI: VF0096(ntrB) VF0115(envZ) VF0525(phoQ) VF1149 VF1397(phoQ)
                 VF1400(dctB) VF1619(torS) VF1908(narQ) VF1987(phoR)
                 VF2082(barA) VF2122(arcB) VF2344(cpxA) VFA0040(uhpB)
                 VFA0178(irlS)
            PPR: PBPRA0185(envZ) PBPRA0230(cpxA) PBPRA0545(fexB)
                 PBPRA0722(phoR) PBPRA0850(narQ) PBPRA0987 PBPRA1232(torS)
                 PBPRA1887 PBPRA2300(citA) PBPRA2346(uhpB) PBPRA2422(phoQ)
                 PBPRA2763 PBPRA3027 PBPRA3084 PBPRA3494(glnL) PBPRB0026(torS)
                 PBPRB0377 PBPRB1912(ypdA) PBPRB1913 PBPRB2016
            PAE: PA0464(creC) PA0757 PA0928 PA1180(phoQ) PA1336 PA1438
                 PA1636(kdpD) PA1798 PA2810 PA3878(narX) PA3946 PA4777 PA4886
                 PA5124(ntrB) PA5165 PA5199(envZ) PA5262(algZ) PA5361(phoR)
                 PA5484
            PAU: PA14_02250(cheA) PA14_06070(creC) PA14_12820 PA14_16470(wspE)
                 PA14_41270 PA14_45590(cheA) PA14_46980 PA14_52260(lemA)
                 PA14_54500 PA14_59800 PA14_60250(pilS) PA14_63160(pmrB)
                 PA14_64580 PA14_67670(ntrB) PA14_68230 PA14_69480(algZ)
                 PA14_70760(phoR) PA14_72390(kinB)
            PAP: PSPA7_2094 PSPA7_3716 PSPA7_3868 PSPA7_4410 PSPA7_4580
                 PSPA7_6283
            PPU: PP_0132 PP_0247(envZ) PP_0264 PP_1067 PP_1187(phoQ) PP_1421
                 PP_1437 PP_1650(gacS) PP_2100 PP_2157 PP_2945 PP_3453
                 PP_4158(kdpD) PP_4224 PP_5047(ntrB) PP_5321(phoR)
                 PP_5384(copS)
            PPF: Pput_0149 Pput_1695 Pput_3639 Pput_3749 Pput_4067 Pput_4284
            PST: PSPTO_0126 PSPTO_0329(envZ) PSPTO_0335 PSPTO_0353(ntrB)
                 PSPTO_0379 PSPTO_1306 PSPTO_1482 PSPTO_1673 PSPTO_1680(phoQ)
                 PSPTO_1691(gacS) PSPTO_1893 PSPTO_2245(kdpD) PSPTO_2326
                 PSPTO_3604 PSPTO_4175 PSPTO_4230 PSPTO_5398 PSPTO_5478(phoR)
            PSB: Psyr_0259 Psyr_0264 Psyr_1126 Psyr_1292 Psyr_1498 Psyr_2050
                 Psyr_2113 Psyr_2867 Psyr_3085 Psyr_3375 Psyr_3512 Psyr_3698
                 Psyr_3708 Psyr_3912 Psyr_3964 Psyr_4799 Psyr_4821 Psyr_4937
                 Psyr_5033
            PSP: PSPPH_0147 PSPPH_0247(envZ) PSPPH_0253 PSPPH_1194
                 PSPPH_2021(kdpD) PSPPH_2377(baeS2) PSPPH_2980 PSPPH_3295
                 PSPPH_3454 PSPPH_3719(gacS) PSPPH_3729 PSPPH_3736 PSPPH_3906
                 PSPPH_3961(tctE) PSPPH_4827 PSPPH_4852(glnL) PSPPH_5115(phoR)
            PFL: PFL_0090(kinB) PFL_0201 PFL_0277 PFL_0301 PFL_0378(glnL)
                 PFL_1105 PFL_1442 PFL_1964 PFL_2516 PFL_2638 PFL_2709 PFL_3148
                 PFL_3193 PFL_3328 PFL_3853 PFL_4294(kdpD) PFL_4451(gacS)
                 PFL_4469(phoQ) PFL_4570(kdpD) PFL_4875 PFL_5051 PFL_5712(creE)
                 PFL_6109(phoR)
            PFO: Pfl_0047 Pfl_0203(sthK) Pfl_0261 Pfl_0288 Pfl_0340(ntrB)
                 Pfl_1355 Pfl_1864 Pfl_3038 Pfl_3380(sthK) Pfl_3390
                 Pfl_3625(sthK) Pfl_3856(sthK) Pfl_3975 Pfl_4030 Pfl_4222
                 Pfl_4239 Pfl_4539 Pfl_4664(sthK) Pfl_5195 Pfl_5607
            PEN: PSEEN0086(kinB) PSEEN0228(envZ) PSEEN0387(ntrB) PSEEN0942
                 PSEEN1249 PSEEN1340 PSEEN1346(phoQ) PSEEN1359(gacS) PSEEN2417
                 PSEEN2424 PSEEN2694 PSEEN2758 PSEEN2968 PSEEN3606(kdpD)
                 PSEEN3670 PSEEN3705 PSEEN3768 PSEEN3793(cheA) PSEEN4286
                 PSEEN4302 PSEEN5151(creC) PSEEN5465(phoR)
            PMY: Pmen_0835 Pmen_1173 Pmen_1730 Pmen_2468 Pmen_2958 Pmen_3648
                 Pmen_4184 Pmen_4311 Pmen_4312 Pmen_4313
            PAR: Psyc_0347 Psyc_0603(narX) Psyc_1537(ntrB) Psyc_1597
                 Psyc_1922(phoR) Psyc_2020(envZ) Psyc_2021 Psyc_2077
            PCR: Pcryo_0096 Pcryo_1767
            PRW: PsycPRwf_2092
            ACI: ACIAD0284(algZ) ACIAD0626(baeS) ACIAD1369(glnL)
                 ACIAD2960(qseC) ACIAD2975(kdpD) ACIAD3072(barA)
                 ACIAD3389(envZ) ACIAD3558(phoR)
            ACB: A1S_3230
            SON: SO_1230(torS) SO_1559(phoR) SO_1945(phoQ) SO_2105 SO_2822
                 SO_3136.1 SO_3457 SO_3981(narQ) SO_4471(ntrB) SO_4478(cpxA)
                 SO_4634(envZ) SO_4648
            SDN: Sden_0235 Sden_1191 Sden_1263 Sden_1346 Sden_2688 Sden_3296
                 Sden_3457 Sden_3462 Sden_3539
            SFR: Sfri_0217 Sfri_0321 Sfri_1047 Sfri_1202 Sfri_2718
            SAZ: Sama_0126 Sama_1031 Sama_2212 Sama_3426 Sama_3433 Sama_3511
            SBL: Sbal_0084 Sbal_0267 Sbal_2809 Sbal_3148
            SBM: Shew185_0835 Shew185_1365 Shew185_3788
            SLO: Shew_1200 Shew_1443 Shew_3560 Shew_3638
            SSE: Ssed_0139 Ssed_0290 Ssed_0627 Ssed_0987 Ssed_1285 Ssed_1648
            SPL: Spea_0286 Spea_0628 Spea_1180 Spea_3702
            SHE: Shewmr4_0056 Shewmr4_0258 Shewmr4_1109 Shewmr4_1302
                 Shewmr4_1360 Shewmr4_2093 Shewmr4_3812 Shewmr4_3872
            SHM: Shewmr7_0054 Shewmr7_1175 Shewmr7_1369 Shewmr7_1425
                 Shewmr7_1881 Shewmr7_3364 Shewmr7_3763 Shewmr7_3903
                 Shewmr7_3965
            SHN: Shewana3_0252 Shewana3_0259 Shewana3_0657 Shewana3_1053
                 Shewana3_1109 Shewana3_1362 Shewana3_1413 Shewana3_1723
                 Shewana3_1886 Shewana3_2218 Shewana3_2593 Shewana3_2878
                 Shewana3_3185 Shewana3_4018 Shewana3_4026 Shewana3_4075
                 Shewana3_4295
            SHW: Sputw3181_0106 Sputw3181_0222 Sputw3181_1245 Sputw3181_1505
            ILO: IL0184(narX) IL0321(envZ) IL1647(qseC_2) IL2110(phoR)
                 IL2436(glnL)
            CPS: CPS_0398(ntrB) CPS_1209(phoR) CPS_1261 CPS_1389(phoQ)
                 CPS_1405 CPS_1749(cpxA) CPS_1826(torS) CPS_2012(dctB) CPS_3170
                 CPS_3304(baeS) CPS_4117 CPS_4270 CPS_4596(envZ)
            PHA: PSHAa0164(glnL) PSHAa0374 PSHAa0550(arcB) PSHAa0598(phoR)
                 PSHAa0620 PSHAa0737(barA) PSHAa0854(rstB) PSHAa0922(algZ)
                 PSHAa1282(phoQ) PSHAa1592(uhpB) PSHAa2196(baeS)
                 PSHAa2849(envZ) PSHAb0013(cusS) PSHAb0361
            PAT: Patl_0226 Patl_0988 Patl_1027 Patl_1054 Patl_1528 Patl_1601
                 Patl_3747
            SDE: Sde_0500 Sde_1949 Sde_2161 Sde_3107 Sde_3669
            PIN: Ping_0528 Ping_0714 Ping_3487
            MAQ: Maqu_0767 Maqu_2241 Maqu_2348
            CBU: CBU_0366 CBU_1228
            CBD: COXBU7E912_1313(qseC)
            LPN: lpg0714 lpg1291 lpg1437(cpxA) lpg1912
            LPF: lpl1253 lpl1604(cpxA)
            LPP: lpp0780 lpp1254 lpp1392(cpxA) lpp1887(gacS)
            MCA: MCA1715 MCA1765 MCA2214(kdpD) MCA2542(ntrB) MCA3104(phoR)
            FTU: FTT0094c(qseC) FTT1736c(kdpD)
            FTF: FTF0094c(qseC) FTF1736c(kdpD)
            FTW: FTW_0062(kdpD) FTW_0175
            FTL: FTL_1762 FTL_1878 FTL_1879
            FTN: FTN_1617
            TCX: Tcr_0066 Tcr_0542 Tcr_0905 Tcr_0968 Tcr_2180 Tcr_2189
            NOC: Noc_0783 Noc_2400(phoR)
            AEH: Mlg_0015 Mlg_0988 Mlg_2152
            HHA: Hhal_1216
            HCH: HCH_00065 HCH_00293 HCH_00309 HCH_00325 HCH_00418 HCH_00770
                 HCH_01034 HCH_01429 HCH_01636 HCH_01758 HCH_01804 HCH_02554
                 HCH_03612 HCH_04013 HCH_04119 HCH_06619 HCH_06659
            CSA: Csal_0245 Csal_0715 Csal_1635 Csal_2024 Csal_2406
            ABO: ABO_0167(phoR) ABO_0269(envZ) ABO_0713(rstB) ABO_1627(gacS)
                 ABO_2260(ntrB) ABO_2324(algZ)
            MMW: Mmwyl1_0136 Mmwyl1_0202 Mmwyl1_0357 Mmwyl1_0602 Mmwyl1_1087
                 Mmwyl1_1181 Mmwyl1_1250 Mmwyl1_1644 Mmwyl1_2022 Mmwyl1_2871
                 Mmwyl1_3381
            AHA: AHA_0032 AHA_0066 AHA_0189(cpxA) AHA_0275(glnL)
                 AHA_0306(envZ) AHA_0816 AHA_1036(cheA-1) AHA_1385(cheA-2)
                 AHA_2529 AHA_2797(uhpB) AHA_3290(lytS) AHA_4061 AHA_4193
                 AHA_4257
            NME: NMB0594 NMB1249 NMB1792
            NMA: NMA0670 NMA0797 NMA1418
            NGO: NGO0112 NGO0176 NGO0753
            CVI: CV_0217(ompB) CV_0563(phoR) CV_0892(qseC) CV_1596(kdpD)
                 CV_1665 CV_1771 CV_2324 CV_2534(narX) CV_3591(ntrB) CV_3844
                 CV_4218
            RSO: RS02109(RSp1553) RS02380(RSp1043) RS03139(RSp1195)
                 RS05645(RSp1162) RSc0331(dctB2) RSc1260(ntrB) RSc1535(phoR)
                 RSc1647(risS) RSc1735(RS02923) RSc3063(RS00507) RSc3385(kdpD)
                 RSp0008(dctB1) RSp0488(czcS) RSp0654(copS) RSp0979(narX)
                 RSp1622(rcsC)
            REU: Reut_A0184 Reut_A0276 Reut_A0391 Reut_A1814 Reut_A2055
                 Reut_A2102 Reut_A2161 Reut_A2290 Reut_A2491 Reut_A2668
                 Reut_A3418 Reut_B3962 Reut_B5065 Reut_B5169 Reut_B5325
            REH: H16_A0294 H16_A0298(gltS1) H16_A0542 H16_A0692(gltS2)
                 H16_A1462 H16_A2333(ntrB) H16_B0895(kdpD2)
            RME: Rmet_0041 Rmet_0229 Rmet_0464 Rmet_0516 Rmet_0589 Rmet_1626
                 Rmet_1651 Rmet_1752 Rmet_1948 Rmet_2060 Rmet_2086 Rmet_2179
                 Rmet_3005 Rmet_3575 Rmet_3584 Rmet_3882 Rmet_3935 Rmet_4339
                 Rmet_4466 Rmet_4626 Rmet_4830 Rmet_4963 Rmet_4977 Rmet_5332
                 Rmet_5393 Rmet_5673 Rmet_5710 Rmet_5797 Rmet_6110
            BMA: BMA0270 BMA0309 BMA0751 BMA0786(phoR) BMA1486(risS) BMA1735
                 BMA1741(ntrB) BMAA0785 BMAA1027(irlS) BMAA1126(tctE) BMAA1145
                 BMAA1660 BMAA2070
            BMV: BMASAVP1_1230 BMASAVP1_1718 BMASAVP1_A1087 BMASAVP1_A1981
                 BMASAVP1_A2670
            BML: BMA10299_0115(tctE) BMA10299_1510 BMA10299_1925
                 BMA10299_A2406 BMA10299_A3068(ntrB) BMA10299_A3324
            BMN: BMA10247_0019 BMA10247_0370 BMA10247_A0085 BMA10247_A0601
                 BMA10247_A1500(tctE) BMA10247_A1518
            BXE: Bxe_A0119 Bxe_A0669 Bxe_A1523 Bxe_A1734 Bxe_A3249 Bxe_A4196
                 Bxe_B1046 Bxe_B2068 Bxe_C1380
            BUR: Bcep18194_A4449 Bcep18194_A4493 Bcep18194_A5250
                 Bcep18194_A5457(ntrB) Bcep18194_A5612 Bcep18194_A5727
                 Bcep18194_A5948 Bcep18194_A5981 Bcep18194_A6214
                 Bcep18194_B0027 Bcep18194_B0307 Bcep18194_B0907
                 Bcep18194_B0913 Bcep18194_B1730 Bcep18194_B1763
                 Bcep18194_B2429 Bcep18194_B2769 Bcep18194_B2879
                 Bcep18194_B2882
            BCN: Bcen_0870 Bcen_1673 Bcen_1788 Bcen_2043 Bcen_2258 Bcen_2851
                 Bcen_3025 Bcen_3570 Bcen_4572 Bcen_5929 Bcen_6140
            BCH: Bcen2424_0256 Bcen2424_1351 Bcen2424_1939 Bcen2424_2148
                 Bcen2424_2285 Bcen2424_2400 Bcen2424_2654 Bcen2424_2872
                 Bcen2424_3791 Bcen2424_4797 Bcen2424_5341
            BAM: Bamb_0169 Bamb_1183 Bamb_1235 Bamb_1927 Bamb_2185 Bamb_2323
                 Bamb_2445 Bamb_2701 Bamb_2927 Bamb_4691
            BPS: BPSL0426(dctB) BPSL0774 BPSL0807 BPSL1037 BPSL1174(kdpD)
                 BPSL1365 BPSL1634 BPSL2095 BPSL2313 BPSL2317(glnL) BPSS0062
                 BPSS0117 BPSS0687 BPSS0706 BPSS1039(irlS) BPSS1460 BPSS1646
                 BPSS1995(irlS2) BPSS2314
            BPM: BURPS1710b_0641(dctB) BURPS1710b_0970(tctE) BURPS1710b_1010
                 BURPS1710b_1253(envZ) BURPS1710b_1396(kdpD)
                 BURPS1710b_1625(phoR) BURPS1710b_2224(rcsC)
                 BURPS1710b_2508(risS) BURPS1710b_2763(narX)
                 BURPS1710b_2768(glnL) BURPS1710b_A0029(irlS) BURPS1710b_A0489
                 BURPS1710b_A0709 BURPS1710b_A1104(irlS2) BURPS1710b_A1462
                 BURPS1710b_A1572(dctB1) BURPS1710b_A1627(rcsC)
                 BURPS1710b_A2258(rpeA) BURPS1710b_A2278(tctE)
            BPL: BURPS1106A_0477(dctB) BURPS1106A_0812 BURPS1106A_2396(risS)
                 BURPS1106A_2689(ntrB) BURPS1106A_A0082 BURPS1106A_A0933
                 BURPS1106A_A2229
            BPD: BURPS668_0457(dctB) BURPS668_0808 BURPS668_2353(risS)
                 BURPS668_2633(ntrB) BURPS668_3855 BURPS668_A0101
                 BURPS668_A1018 BURPS668_A1523 BURPS668_A2312 BURPS668_A2870
            BTE: BTH_I0400(dctB) BTH_I0641 BTH_I0674 BTH_I0894 BTH_I1024(kdpD)
                 BTH_I1845 BTH_I1850 BTH_I2093(risS) BTH_I2767(phoR) BTH_II0141
                 BTH_II0156(cheA) BTH_II0375(irlS) BTH_II0505 BTH_II0904
                 BTH_II1377(irlS) BTH_II1588 BTH_II1723 BTH_II1740 BTH_II2334
            BPE: BP0157 BP0159(phoR) BP1597(glnL) BP1877(bvgS) BP2206
                 BP2483(kdpD) BP2548 BP3223 BP3866
            BPA: BPP2631 BPP2987(glnL) BPP3029(bvgS) BPP3360(risS)
                 BPP3471(kdpD) BPP3575 BPP3997(phoR) BPP3999 BPP4420
            BBR: BB2074 BB2953(glnL) BB2995(bvgS) BB3811(risS) BB3920(kdpD)
                 BB4010 BB4470(phoR) BB4472 BB4543 BB5008
            RFR: Rfer_0423 Rfer_0504 Rfer_0577 Rfer_2400 Rfer_2453 Rfer_2541
                 Rfer_2733 Rfer_2742 Rfer_2788 Rfer_2981 Rfer_3121 Rfer_3454
                 Rfer_3522 Rfer_3684 Rfer_3821 Rfer_3951
            POL: Bpro_0236 Bpro_1119 Bpro_1451 Bpro_1809 Bpro_1957 Bpro_2258
                 Bpro_2714 Bpro_3675 Bpro_3980 Bpro_4254 Bpro_4688
            PNA: Pnap_2778 Pnap_3959
            AAV: Aave_0229 Aave_1444 Aave_4637
            AJS: Ajs_0010 Ajs_1191 Ajs_3154 Ajs_3998
            VEI: Veis_0358 Veis_3152
            MPT: Mpe_A0077
            HAR: HEAR0950(glnL) HEAR1908 HEAR2631
            NEU: NE0015(yfhK) NE0343 NE0515(baeS) NE1288(phoR) NE1408
            NET: Neut_0017 Neut_0136 Neut_1167 Neut_1565
            NMU: Nmul_A1159 Nmul_A2232
            EBA: ebA1181 ebA2023 ebA3021(phoR) ebA3507(narX) ebA4117(ntrB)
                 ebA6233 ebA6280(narX) ebA6498 ebA6722 ebA960(yfhK)
            AZO: azo0448(dctB1) azo0703(creC) azo0736(ntrB) azo1708(envZ1)
                 azo1915(dctB2) azo3492
            DAR: Daro_0430 Daro_0478 Daro_0833 Daro_1080 Daro_1580 Daro_1802
                 Daro_1979 Daro_2094 Daro_2150 Daro_2258 Daro_2816 Daro_3017
                 Daro_3147 Daro_3177 Daro_3568 Daro_3759
            TBD: Tbd_0217 Tbd_0230 Tbd_1400 Tbd_1744 Tbd_1750 Tbd_2353
                 Tbd_2501 Tbd_2769
            MFA: Mfla_0215 Mfla_0653 Mfla_0913 Mfla_1308 Mfla_1936 Mfla_2449
            HPY: HP0164 HP0165 HP0244(atoS) HP1364
            HPJ: jhp0151 jhp0229 jhp1282
            HPA: HPAG1_0161 HPAG1_1000 HPAG1_1311
            HHE: HH0140 HH1607 HH1657
            HAC: Hac_0191 Hac_0346 Hac_0450(cheA) Hac_1373(atoS)
            WSU: WS1464 WS1590 WS1818
            TDN: Tmden_0914
            CJE: Cj0679(kdpD')
            CCV: CCV52592_1657
            GSU: GSU0599 GSU1004 GSU1101 GSU2483(kdpD) GSU2947 GSU3119
            GME: Gmet_0527 Gmet_1057 Gmet_2436 Gmet_2562 Gmet_2694 Gmet_2698
                 Gmet_2923
            GUR: Gura_0025 Gura_0915 Gura_1221 Gura_1422 Gura_1547 Gura_1571
                 Gura_1987 Gura_2017 Gura_2062 Gura_3741 Gura_4294
            PCA: Pcar_0258 Pcar_0361 Pcar_0496 Pcar_0654 Pcar_1993(ntrB)
            PPD: Ppro_2719
            DVU: DVU0013 DVU0270 DVU0597(lytS) DVU3216 DVU3336 DVU3382(zraS)
            DVL: Dvul_0172 Dvul_2710
            DDE: Dde_0110 Dde_0160 Dde_0320 Dde_0711 Dde_3782
            LIP: LI1078(hydH) LI1144(cheA_2)
            BBA: Bd0216 Bd1018(phoR) Bd1758(kdpD) Bd3650
            DPS: DP0883 DP1489 DP1886
            ADE: Adeh_0603 Adeh_0613 Adeh_0625 Adeh_0892 Adeh_1193 Adeh_1277
                 Adeh_1370 Adeh_1379 Adeh_2736
            AFW: Anae109_0027 Anae109_0111 Anae109_0416 Anae109_0529
                 Anae109_0539 Anae109_0540 Anae109_0803 Anae109_0881
                 Anae109_1040 Anae109_1492 Anae109_1597 Anae109_1671
                 Anae109_1722 Anae109_1854 Anae109_2005 Anae109_2030
                 Anae109_2142 Anae109_2356 Anae109_2387 Anae109_2452
                 Anae109_2663 Anae109_2929 Anae109_3005 Anae109_3408
                 Anae109_3795 Anae109_4054 Anae109_4186 Anae109_4250
                 Anae109_4365 Anae109_4466
            MXA: MXAN_0167 MXAN_4758(cheA) MXAN_5365(hsfB) MXAN_5785(pilS)
                 MXAN_6951 MXAN_7206
            SAT: SYN_00174 SYN_00431 SYN_00963 SYN_01364
            SFU: Sfum_0631 Sfum_1650 Sfum_2294 Sfum_2617 Sfum_2657 Sfum_2891
            RPR: RP229(barA) RP426(envZ) RP465(phoR) RP614(ntrY)
            RTY: RT0221 RT0412(envZ)
            RCO: RC0592(envZ)
            RFE: RF_0657(envZ)
            RBE: RBE_0744
            ERU: Erum2120
            ERW: ERWE_CDS_02140
            ERG: ERGA_CDS_02090
            PUB: SAR11_0089(envZ)
            MLO: mll3127 mll6540 mll7700 mll7952 mlr0397(nirB) mlr0562 mlr2667
                 mlr5642 mlr7238 mlr7649
            MES: Meso_0012 Meso_4124
            PLA: Plav_0393 Plav_0431 Plav_0648 Plav_0956 Plav_1850 Plav_1935
                 Plav_1968 Plav_3595
            SME: SMa2327 SMb20721 SMb21201 SMc00059 SMc00776 SMc01042(ntrB)
                 SMc01595 SMc02147(phoR) SMc02369 SMc04212
            SMD: Smed_0118 Smed_0617 Smed_0641
            ATU: Atu0113(dctB) Atu0419(phoR) Atu0614(pleC) Atu0921
                 Atu0982(pleC) Atu1445(ntrB) Atu1888 Atu2207(envZ)
                 Atu2465(tctE) Atu3787(kdpD) Atu4018 Atu4711(phoQ) Atu5266
            ATC: AGR_C_1094 AGR_C_1677 AGR_C_174 AGR_C_1799 AGR_C_2663(ntrB)
                 AGR_C_3465 AGR_C_4011(envZ) AGR_C_4477 AGR_C_736(phoR)
                 AGR_L_1672 AGR_L_2094(kdpD) AGR_pAT_381
            RET: RHE_CH00508(phoR) RHE_CH00720 RHE_CH01252 RHE_CH01287(feuQ)
                 RHE_CH01297 RHE_CH01947(ntrB) RHE_CH02441 RHE_CH03009
                 RHE_CH03434 RHE_CH03588 RHE_PC00157(mctS) RHE_PE00263(kdpD)
                 RHE_PF00310
            RLE: RL0540 RL0688(cheA) RL0769 RL1382 RL1434(feuQ) RL1445
                 RL2256(ntrB) RL2278 RL2779 RL3068 RL3425(dctB) RL3453
                 RL3893(dctB) RL4035(cheA) RL4108 pRL100407 pRL110378(kdpD)
                 pRL120668
            BME: BMEI0417 BMEI0492 BMEI0865 BMEI1325 BMEI1336 BMEI1357
                 BMEI1583 BMEI1624 BMEII1015
            BMF: BAB1_0369 BAB1_0601 BAB1_0640 BAB1_1141 BAB1_1539 BAB1_1621
                 BAB2_0221
            BMS: BR0298 BR0616 BR1118(ntrB) BR1522 BR1606 BRA0228
            BMB: BruAb1_0367 BruAb1_0635 BruAb1_1124(ntrB) BruAb1_1513(envZ)
                 BruAb1_1593 BruAb2_0223
            OAN: Oant_0381 Oant_4784
            BJA: bll3140 bll3738 bll6776 blr1090(phoR) blr3071 blr3730
                 blr4487(ntrB) blr7396 blr7462
            BRA: BRADO0236 BRADO2303
            RPA: RPA1328 RPA1858 RPA1938 RPA1972 RPA2135 RPA2592(ntrB)
                 RPA3001(kdpD) RPA4367 RPA4781(phoR)
            RPB: RPB_0213 RPB_0775 RPB_2883(ntrB) RPB_3395 RPB_3436 RPB_3515
                 RPB_4172 RPB_4358 RPB_4648
            RPC: RPC_1385 RPC_1779 RPC_2064 RPC_2577 RPC_3208 RPC_4547
                 RPC_4905 RPC_4924
            RPD: RPD_0665 RPD_0887 RPD_1944 RPD_2018 RPD_2046 RPD_2347
                 RPD_2589 RPD_3678 RPD_3883 RPD_4242
            RPE: RPE_1193 RPE_1426 RPE_1872 RPE_1951 RPE_1978 RPE_2415
                 RPE_2757 RPE_3631 RPE_3926 RPE_4063 RPE_4284 RPE_4627 RPE_4675
                 RPE_4892
            NWI: Nwi_0505 Nwi_1012 Nwi_1200 Nwi_1444(ntrB) Nwi_2221 Nwi_2517
            NHA: Nham_0349 Nham_3136 Nham_3376
            BHE: BH04830 BH11760(envZ)
            BQU: BQ03380(envZ) BQ04030
            BBK: BARBAKC583_0542(ntrY) BARBAKC583_1333(bvrS)
            XAU: Xaut_0196 Xaut_1406 Xaut_2428 Xaut_4400
            CCR: CC_0759(fixL) CC_1594(kdpD) CC_1740 CC_2482
            SIL: SPO0188 SPO1947 SPO2036 SPO2088(ntrB) SPO2173 SPO2574
                 SPOA0236(dctB)
            SIT: TM1040_0406 TM1040_0877 TM1040_1263 TM1040_1462 TM1040_1815
                 TM1040_2734 TM1040_3206
            RSP: RSP_0203 RSP_1268(kdpD) RSP_1611 RSP_2129 RSP_2837(ntrB)
                 RSP_2915(phoR) RSP_3431 RSP_3975
            RSH: Rsph17029_0265 Rsph17029_0804
            RSQ: Rsph17025_0015 Rsph17025_1106 Rsph17025_3048
            JAN: Jann_1731
            RDE: RD1_2250 RD1_2265(dctB) RD1_2641(phoR) RD1_2764(ntrB)
                 RD1_2810(degS) RD1_2944 RD1_3059(cheA) RD1_3461 RD1_3666(torS)
            PDE: Pden_4406
            MMR: Mmar10_0658 Mmar10_0765
            ZMO: ZMO0601
            NAR: Saro_0031 Saro_0387 Saro_1511 Saro_1774 Saro_1927
            SAL: Sala_1276 Sala_1457 Sala_1727 Sala_1740
            SWI: Swit_2689 Swit_5353 Swit_5356
            ELI: ELI_02520 ELI_06280(ntrB) ELI_11265(cheA)
            GOX: GOX0120(envZ)
            GBE: GbCGDNIH1_0185 GbCGDNIH1_2242
            ACR: Acry_3107
            RRU: Rru_A0377 Rru_A1158 Rru_A1436 Rru_A1677 Rru_A2226
            MAG: amb0548 amb1657 amb1912 amb1967 amb2366
            MGM: Mmc1_0630 Mmc1_1482 Mmc1_3444 Mmc1_3576
            ABA: Acid345_0507 Acid345_0508 Acid345_1524 Acid345_1771
                 Acid345_2497 Acid345_3600
            SUS: Acid_0392
            BSU: BG10204(kinA) BG10364(phoR) BG10380(comP) BG10392(degS)
                 BG10411(spo0F) BG10535(resE) BG10745(kinB) BG10871(ycbA)
                 BG10989(kinC) BG11127(yxdK) BG11168(ycbM) BG11461(yycG)
                 BG11783(yrkQ) BG11896(yxjM) BG11952(lytS) BG11997(yccG)
                 BG12032(yclK) BG12073(dctS) BG12155(ydfH) BG12215(yfiJ)
                 BG12347(yufL) BG12406(yvcQ) BG12445(yvfT) BG12498(ywpD)
                 BG12576(citS) BG12724(ybdK) BG12847(yesM) BG13005(yhcY)
                 BG13519(desK) BG13919(ytsB) BG14132(cssS) BG14146(yvrG)
            BHA: BH0582 BH1173 BH1581(resE) BH1920 BH2716 BH3156(phoR) BH3447
                 BH3629(degS) BH3787(spo0F) BH3839(citS) BH4026
            BAN: BA0576 BA0742(kdpD) BA0923 BA1498(resE) BA1802 BA2264 BA2636
                 BA3007 BA4223(kinB-3) BA4832(phoR) BA5581(spo0F) BA5598
                 BA5692(lytS) BA5714(yycG)
            BAR: GBAA0742(kdpD) GBAA0923 GBAA1498(resE) GBAA1802 GBAA2636
                 GBAA3007 GBAA4223(kinB-3) GBAA4832(phoR) GBAA5581(spo0F)
                 GBAA5598 GBAA5692 GBAA5714(yycG)
            BAA: BA_0437 BA_0455 BA_0550 BA_0572 BA_1327(kdpD) BA_1502 BA_2022
                 BA_2307 BA_3155 BA_3515 BA_4684 BA_5256
            BAT: BAS0706 BAS0869 BAS1387 BAS1669 BAS2456 BAS2795 BAS3916
                 BAS4483 BAS5185 BAS5201 BAS5296 BAS5318
            BCE: BC0577 BC0756(kdpD) BC0881(comP) BC0936 BC1478(resE) BC2619
                 BC3114 BC4007 BC4588(phoR) BC5336 BC5353 BC5441 BC5462
            BCA: BCE_0639 BCE_0812(kdpD) BCE_1009 BCE_1602(resE) BCE_1874
                 BCE_2662 BCE_3043 BCE_4058(kinB) BCE_4719(phoR)
                 BCE_5466(spo0F) BCE_5483 BCE_5574(lytS) BCE_5614(yycG)
            BCZ: BCZK0489 BCZK0649(kdpD) BCZK1359(resE) BCZK3764(kinB)
                 BCZK4329(phoR) BCZK5036(spo0F) BCZK5051 BCZK5138(lytS)
                 BCZK5162
            BCY: Bcer98_0502 Bcer98_0546 Bcer98_1022 Bcer98_1201 Bcer98_3273
                 Bcer98_4005
            BTK: BT9727_0487 BT9727_0650(kdpD) BT9727_0837(citS)
                 BT9727_1033(comP) BT9727_1360(resE) BT9727_2419 BT9727_2744
                 BT9727_2889(kinA) BT9727_2906 BT9727_3748(kinB)
                 BT9727_4318(phoR) BT9727_5020(spo0F) BT9727_5035
                 BT9727_5123(lytS) BT9727_5146
            BTL: BALH_0893 BALH_1334(resE) BALH_1584 BALH_2024(yhcY) BALH_2371
                 BALH_2691 BALH_2816 BALH_3627(kinB) BALH_4172(phoR)
                 BALH_4851(yvfT) BALH_4948(lytS) BALH_4972
            BLI: BL00210(bceS) BL00380(lytS) BL00395(phoR) BL00657(resE)
                 BL00707(yvrG) BL00749(cssS) BL00910(citS) BL01611(kinC)
                 BL01640 BL02105(desK) BL02372(yycG) BL02538 BL02605(comPA)
                 BL02898 BL02955 BL03342 BL03360(degS) BL03536(kinE)
                 BL03576(kinA) BL03796(yesM) BL03938 BL03968(spo0F)
                 BL05387(yvfT)
            BLD: BLi00225(citS) BLi00440 BLi00460(yclK) BLi01000(yhcY)
                 BLi01245 BLi01366(yesM) BLi01609(kinA) BLi01665(kinC)
                 BLi02456(resE1) BLi02808(yocF) BLi03040(lytS) BLi03058(phoR)
                 BLi03334(yufL) BLi03354(comP) BLi03483(cssS) BLi03517(yvrG)
                 BLi03794(degS) BLi03961(spo0F) BLi04065(ydfH) BLi04212(ytsB)
                 BLi04303(yvfT) BLi04334(yycG)
            BCL: ABC0720(nreB) ABC0735(desK) ABC0915 ABC1255(kinB)
                 ABC1836(resE) ABC2710(phoR) ABC3087(degS) ABC3228 ABC3586
                 ABC3884(spo0F) ABC4058(lytS) ABC4098
            BAY: RBAM_013770(kinA) RBAM_014230(kinC)
            BPU: BPUM_0245(ycbA) BPUM_0250(yccG) BPUM_0354 BPUM_0417
                 BPUM_0707(citS) BPUM_0726 BPUM_0869 BPUM_1031 BPUM_1220(ykoH)
                 BPUM_1247(kinE) BPUM_1290(kinA) BPUM_1542(cheA) BPUM_1745
                 BPUM_2044(resE) BPUM_2552 BPUM_2589 BPUM_2593(ytsB) BPUM_2787
                 BPUM_2788 BPUM_2789 BPUM_2790 BPUM_2820 BPUM_2954(cssS)
                 BPUM_3017 BPUM_3156 BPUM_3199 BPUM_3240 BPUM_3688(yycG)
            OIH: OB0777 OB0832 OB1642 OB1680(kinC) OB1818 OB2164 OB2520(degS)
                 OB2851 OB3220 OB3251 OB3451
            GKA: GK0559 GK1912 GK2278 GK2341 GK2731 GK3151 GK3245
                 GK3387(spo0F) GK3473
            GTN: GTNG_3414(yycG)
            SAU: SA0018(vicK) SA0067(kdpD(SCCmec)) SA0216 SA0250(lytS) SA0615
                 SA1158 SA1322(srrB) SA1515(phoR) SA1667 SA1701(vraS)
                 SA1843(agrC) SA1882(kdpD) SA2152 SA2180 SA2417
            SAV: SAV0019(vicK) SAV0071(kdpD) SAV0260(lytS) SAV1491(srrB)
                 SAV1692(phoR) SAV1885(vraS) SAV2038(agrC) SAV2078(kdpD)
                 SAV2392
            SAM: MW0019(vicK) MW0236(lytS) MW1445(srrB) MW1636(phoR)
                 MW1825(vraS) MW1962(agrC) MW2002(kdpD) MW2314
            SAR: SAR0019(yycG) SAR0069 SAR0257(lytS) SAR1567(srrB)
                 SAR1771(phoR) SAR1975(vraS) SAR2125(agrC) SAR2166(kdpD)
                 SAR2481
            SAS: SAS0019 SAS0237 SAS1431 SAS1620 SAS1807 SAS1943 SAS1983
                 SAS2283
            SAC: SACOL0020(yycG) SACOL0245(lytS) SACOL1534(srrB) SACOL1739
                 SACOL1943(vraS) SACOL2070(kdpD) SACOL2390
            SAB: SAB0019(yycG) SAB0199(lytS) SAB0609 SAB1352c(srrB)
                 SAB1551c(phoR) SAB1817c(vraS) SAB1922(agrC) SAB1963(kdpD)
                 SAB2271c
            SAA: SAUSA300_0021 SAUSA300_0254 SAUSA300_1441(srrB)
                 SAUSA300_1866(vraS) SAUSA300_1991(agrC) SAUSA300_2035(kdpD)
                 SAUSA300_2338
            SAO: SAOUHSC_00021 SAOUHSC_00230 SAOUHSC_01585 SAOUHSC_01799
                 SAOUHSC_02099 SAOUHSC_02264 SAOUHSC_02314 SAOUHSC_02644
                 SAOUHSC_02676
            SAJ: SaurJH9_0019 SaurJH9_1548 SaurJH9_1749 SaurJH9_1939
            SAH: SaurJH1_0019 SaurJH1_1579 SaurJH1_1783 SaurJH1_1973
            SEP: SE0019 SE0428 SE1175 SE1368 SE1570 SE1637 SE1970 SE2011
            SER: SERP0313 SERP0888 SERP1054(srrB) SERP1255(phoR)
                 SERP1423(vraS) SERP1982 SERP2024(lytS) SERP2489(kdpD)
                 SERP2533(yycG)
            SHA: SH0018(vicK) SH0032(kdpD) SH0613(lytS) SH0659(nreB)
                 SH0994(agrC) SH1070(vraS) SH1233(phoR) SH1425(srrB) SH1587
                 SH2234
            SSP: SSP0022 SSP0464 SSP0840 SSP0908 SSP1074 SSP1261(srrB) SSP2061
            LMO: lmo0050 lmo0288 lmo1947(resE) lmo2011 lmo2500(phoR) lmo2679
            LMF: LMOf2365_0059(agrC) LMOf2365_0308 LMOf2365_1977(resE)
                 LMOf2365_2035 LMOf2365_2473 LMOf2365_2659(kdpD)
            LIN: lin0043 lin0316 lin2061(resE) lin2119 lin2643(phoR) lin2827
                 pli0050
            LWE: lwe0041 lwe0262 lwe0661(cheA) lwe1973(resE) lwe2031 lwe2448
                 lwe2628(kdpD)
            LLA: L0122(kinB)
            LLC: LACR_0443 LACR_1524
            SPY: SPy_0242 SPy_0529(vicK) SPy_1107
            SPZ: M5005_Spy_0204(fasB) M5005_Spy_0436(vicK)
                 M5005_Spy_0831(dpiB) M5005_Spy_1280
            SPM: spyM18_0539 spyM18_0595(vicK) spyM18_1069 spyM18_1569
            SPG: SpyM3_0171 SpyM3_0373(vicK) SpyM3_0769 SpyM3_1201(yesM)
            SPS: SPs0178 SPs0661 SPs0969 SPs1480
            SPH: MGAS10270_Spy0437(vicK) MGAS10270_Spy1295
            SPI: MGAS10750_Spy0456(vicK) MGAS10750_Spy1387
            SPJ: MGAS2096_Spy0455(vicK) MGAS2096_Spy1299
            SPK: MGAS9429_Spy0435(vicK) MGAS9429_Spy1274
            SPA: M6_Spy0235(fasB) M6_Spy0470(vicK) M6_Spy0829 M6_Spy1301(yesM)
            SPB: M28_Spy0198(fasB) M28_Spy0424(vicK) M28_Spy0808(dpiB)
                 M28_Spy1218
            SPN: SP_0155 SP_0527 SP_0662 SP_1226 SP_2083
            SPR: spr0464(hk13) spr0579(hk09) spr1106(hk02) spr1894(phoR-pnpS)
            SPD: SPD_0702(ciaH)
            SAG: SAG0182 SAG0720 SAG1017 SAG1960 SAG2127
            SAN: gbs0180 gbs0742 gbs1052 gbs1947 gbs2086
            SAK: SAK_0248 SAK_0846 SAK_1112 SAK_1921 SAK_2066
            SMU: SMU.1516(covS) SMU.1916(comD) SMU.577(lytS)
            LPL: lp_0037(hpk1) lp_0744(hpk3) lp_1943(hpk6) lp_3581(agrC)
            LJO: LJ0066 LJ0448
            LAC: LBA0079
            LSA: LSA0078 LSA0501 LSA0548 LSA1370
            LSL: LSL_0036
            LDB: Ldb0136 Ldb0963(phoR)
            LBU: LBUL_0022 LBUL_0112 LBUL_0873
            LBR: LVIS_0030 LVIS_0202 LVIS_2029
            LCA: LSEI_0935 LSEI_2807 LSEI_2868
            LGA: LGAS_0065
            LRE: Lreu_0020 Lreu_0118
            PPE: PEPE_1796
            EFA: EF0570(kdpD) EF1194(vicK) EF1209 EF1704 EF1820 EF2219 EF3197
            OOE: OEOE_0106 OEOE_0884
            LME: LEUM_1949
            STH: STH3307 STH749 STH986
            CAC: CAC0080(agrC) CAC1701 CAC3662 CAC3678(kdpD)
            CPE: CPE0531 CPE0574 CPE1757
            CPF: CPF_0554
            CPR: CPR_0538
            CTC: CTC01131(phoR) CTC01524(dpiB) CTC01848(yesM) CTC01978
            CNO: NT01CX_1257 NT01CX_1864(cheA)
            CTH: Cthe_0582
            CBE: Cbei_0361 Cbei_0535 Cbei_0710 Cbei_1126 Cbei_1553 Cbei_2027
                 Cbei_2160 Cbei_2435 Cbei_2515 Cbei_2786 Cbei_2950 Cbei_3052
                 Cbei_4484 Cbei_4925
            AMT: Amet_0655 Amet_1013 Amet_1100 Amet_1278 Amet_1519 Amet_2326
                 Amet_2865 Amet_3086 Amet_3258 Amet_4407 Amet_4411 Amet_4433
                 Amet_4757
            CHY: CHY_0657 CHY_1856 CHY_2219 CHY_2566
            DSY: DSY0339 DSY0847 DSY1644 DSY2019 DSY2575 DSY2890 DSY2994
                 DSY3141 DSY3999 DSY4025 DSY4316 DSY4695 DSY4737 DSY4759
            DRM: Dred_1500
            SWO: Swol_0874 Swol_1332 Swol_1455
            CSC: Csac_2033 Csac_2558
            TTE: TTE0562(baeS2) TTE0871 TTE1202(baeS6) TTE1632(baeS7)
                 TTE1682(baeS8) TTE2009(kdpD) TTE2155(kdpD2) TTE2344(lytS2)
                 TTE2688(baeS12)
            MTA: Moth_0974 Moth_1965 Moth_2171 Moth_2494
            MTU: Rv0490(senX3) Rv0600c Rv0601c Rv0758(phoR) Rv0845
                 Rv0902c(prrB) Rv0982(mprB) Rv1028c(kdpD) Rv1032c(trcS)
                 Rv3132c(devS) Rv3245c(mtrB) Rv3764c
            MTC: MT0509(senX3) MT0783 MT0867 MT0925 MT1010 MT1057(kdpD)
                 MT1061(tcrS) MT3218 MT3343(mtrB) MT3871
            MBO: Mb0500(senX3) Mb0617c Mb0781(phoR) Mb0868 Mb0926c(prrB)
                 Mb1008(mprB) Mb1056c(kdpD) Mb1061c(trcS) Mb3156c(devS)
                 Mb3273c(mtrB) Mb3790c
            MLE: ML0175 ML0774(mtrB) ML2124 ML2440
            MPA: MAP0260 MAP0592(phoR) MAP0690 MAP0833c MAP0917 MAP0996c(kdpD)
                 MAP1001c MAP3359c(mtrB) MAP3982(senX3)
            MAV: MAV_0147 MAV_1021 MAV_1170 MAV_4208
            MSM: MSMEG_0936(senX3) MSMEG_1875 MSMEG_5372 MSMEG_5395 MSMEG_5487
                 MSMEG_5663 MSMEG_5870
            CGL: NCgl0067(cgl0068) NCgl0391(cgl0403) NCgl0722(cgl0755)
                 NCgl0840(cgl0875) NCgl2517(cgl2606)
            CGB: cg0089(citA) cg0483(cgtS4) cg0997(cgtS2) cg2887(cgtS3)
            CEF: CE0424 CE0770 CE0949 CE2493 CE2905
            CDI: DIP0390 DIP0695(mtrB) DIP0855 DIP1935
            CJK: jk0342(tcsS1) jk1272(kdpD) jk1531(tcsS5) jk1634(mtrB)
                 jk1911(tcsS8)
            NFA: nfa15690(kdpD) nfa49630 nfa51870 nfa5450 nfa6630
            RHA: RHA1_ro02069(senX3) RHA1_ro04742(phoR) RHA1_ro06325(mtrB)
            SCO: SCO3012(SCE33.14c) SCO4021(2SC10A7.25) SCO4155(SCD84.22c)
                 SCO4229(SCD8A.02) SCO5829(SC5B8.19c) SCO5871(kdpD)
                 SCO7076(SC3A4.02)
            SMA: SAV2396(kdpD) SAV3973(phoR) SAV4048 SAV5064 SAV7118(lytS)
            LXX: Lxx03130 Lxx05360 Lxx18290
            PAC: PPA0118 PPA0360 PPA2113
            TFU: Tfu_0256 Tfu_2495 Tfu_2909
            FRA: Francci3_0235 Francci3_0309 Francci3_0320 Francci3_0470
                 Francci3_1156 Francci3_3283
            FAL: FRAAL0672 FRAAL1851 FRAAL5304(kdpD)
            ACE: Acel_0089
            KRA: Krad_0895
            SEN: SACE_6094(phoR) SACE_6966
            STP: Strop_0336 Strop_0623
            BLO: BL0317
            FNU: FN0190 FN0220
            RBA: RB7410(phoR1)
            CTR: CT467(atoS)
            CTA: CTA_0511(atoS)
            CMU: TC0752
            CPN: CPn0584(atoS)
            CPA: CP0164
            CPJ: CPj0584(atoS)
            CPT: CpB0608(atoS)
            CCA: CCA00157
            CFE: CF0850(atoS)
            PCU: pc1365 pc1881(phoR)
            BBU: BB0420 BB0764
            BGA: BG0423 BG0787
            BAF: BAPKO_0597(cheA-1) BAPKO_0713(cheA-2)
            LIL: LA2012 LA2421 LA3109(kdpD)
            LIC: LIC10993(kdpD) LIC11528 LIC11895
            LBJ: LBJ_0927 LBJ_1964
            LBL: LBL_1320 LBL_2106
            SYN: sll0337(phoR) sll0698(hik33) sll0750(hik8) sll0790(hik31)
                 sll0798(nrsS) sll1228(hik4) sll1555(hik42) sll1590(hik20)
                 sll1672(hik12) sll1871(hik6) slr0311(hik29) slr0533(hik10)
                 slr0640(manS) slr1731(kdpD) slr1759(hik14) slr1805(hik16)
                 slr2098(hik21) slr2099(hik40) slr2104(hik22)
            SYW: SYNW0551(nblS) SYNW0753 SYNW0807 SYNW0948(phoR)
            SYC: syc0534_d(sphS) syc0618_d(dfr) syc1978_c(sasA)
                 syc2362_c(kdpD)
            SYF: Synpcc7942_0924 Synpcc7942_1011 Synpcc7942_1729
                 Synpcc7942_2114
            SYD: Syncc9605_1915 Syncc9605_2123
            SYE: Syncc9902_0550 Syncc9902_0751
            SYG: sync_1006(sasA)
            CYA: CYA_0637(sasA) CYA_2352 CYA_2659
            CYB: CYB_0858 CYB_1895(sasA) CYB_2421
            TEL: tll0925 tll1282 tll1909 tlr0029 tlr0437(hik33)
            GVI: gll0055(hik33) gll0570(kdpD) glr0418
            ANA: all0323(pkn28) all2875 all3600 all4242 all4502 alr1171
                 alr2137 alr3155 alr3511(hik33)
            AVA: Ava_1191 Ava_3171 Ava_3226 Ava_3368 Ava_4716 Ava_B0190
                 Ava_B0208
            PMA: Pro1121 Pro1422
            PMM: PMM0706(phoR) PMM1077 PMM1341(nblS)
            PMT: PMT0804 PMT1099 PMT1417(nblS)
            PMN: PMN2A_0674
            PMI: PMT9312_0718 PMT9312_1088 PMT9312_1439
            TER: Tery_4224
            BTH: BT_2420(frrD) BT_2421
            BFR: BF0582 BF1575
            BFS: BF0532(kdpD)
            SRU: SRU_0865 SRU_2602(cheA)
            FJO: Fjoh_0229 Fjoh_0543 Fjoh_0637 Fjoh_3354 Fjoh_4243
            CTE: CT0195 CT0658
            CCH: Cag_0436
            PLT: Plut_0633
            DET: DET0127 DET1059
            DEH: cbdb_A1033 cbdb_A148 cbdb_A159
            DEB: DehaBAV1_0123 DehaBAV1_0234 DehaBAV1_0598 DehaBAV1_0938
            RRS: RoseRS_0113 RoseRS_0196 RoseRS_0204 RoseRS_0231 RoseRS_0412
                 RoseRS_0520 RoseRS_0613 RoseRS_0804 RoseRS_1308 RoseRS_1619
                 RoseRS_1897 RoseRS_2057 RoseRS_2295 RoseRS_2304 RoseRS_2346
                 RoseRS_2626 RoseRS_3026 RoseRS_3188 RoseRS_3486 RoseRS_3611
                 RoseRS_3736 RoseRS_3771 RoseRS_3817 RoseRS_3876 RoseRS_4452
                 RoseRS_4482
            RCA: Rcas_0230 Rcas_0352 Rcas_0805 Rcas_0833 Rcas_0959 Rcas_0996
                 Rcas_1057 Rcas_1113 Rcas_1175 Rcas_1273 Rcas_1503 Rcas_1645
                 Rcas_2148 Rcas_2598 Rcas_2639 Rcas_2781 Rcas_2916 Rcas_3032
                 Rcas_3170 Rcas_3307 Rcas_3419 Rcas_3600 Rcas_3826 Rcas_4343
            DRA: DR_B0088
            DGE: Dgeo_2852
            TTH: TTC1361(phoR)
            TTJ: TTHB174
            AAE: aq_1115(hksP1) aq_231(hksP4) aq_316(hksP2)
            TMA: TM0127 TM0400 TM0853 TM1258 TM1359 TM1654(hpkA)
            TPT: Tpet_0074 Tpet_0520 Tpet_1137
            TME: Tmel_1496 Tmel_1839
            FNO: Fnod_0404 Fnod_1277 Fnod_1489
            MMP: MMP1120
            MMZ: MmarC7_0372 MmarC7_0548
            MAE: Maeo_1437
            MVN: Mevan_0140 Mevan_0142 Mevan_0613
            MAC: MA2294
            MMA: MM_3205
            MBU: Mbur_0361
            MHU: Mhun_0110 Mhun_0989
            MTH: MTH444 MTH446 MTH459
            AFU: AF0450
STRUCTURES  PDB: 1P0Z  2CMN  2GJ3  2HJE  2J48  2O9B  2O9C  2R78  2R8R  
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.13.3
            ExPASy - ENZYME nomenclature database: 2.7.13.3
            ExplorEnz - The Enzyme Database: 2.7.13.3
            ERGO genome analysis and discovery system: 2.7.13.3
            BRENDA, the Enzyme Database: 2.7.13.3
///
ENTRY       EC 2.7.99.1                 Enzyme
NAME        triphosphate---protein phosphotransferase;
            diphosphate:microsomal-membrane-protein O-phosphotransferase
            (erroneous);
            DiPPT (erroneous);
            pyrophosphate:protein phosphotransferase (erroneous);
            diphosphate---protein phosphotransferase (erroneous);
            diphosphate:[microsomal-membrane-protein] O-phosphotransferase
            (erroneous)
CLASS       Transferases;
            Transferring phosphorus-containing groups;
            Other protein kinases
SYSNAME     triphosphate:[microsomal-membrane-protein] phosphotransferase
REACTION    triphosphate + [microsomal-membrane protein] = diphosphate +
            phospho-[microsomal-membrane protein] [RN:R04312]
ALL_REAC    R04312
SUBSTRATE   triphosphate [CPD:C00536];
            microsomal-membrane protein [CPD:C03788]
PRODUCT     diphosphate [CPD:C00013];
            phospho-[microsomal-membrane protein]
COMMENT     This enzyme was originally thought to use diphosphate as substrate
            [1] but this has since been disproved [2]. The activity is observed
            as the second part of a biphasic reaction after depletion of ATP.
            Tripolyphosphate is a contaminant of [gamma-32P]ATP.
REFERENCE   1  [PMID:6246514]
  AUTHORS   Lam KS, Kasper CB.
  TITLE     Pyrophosphate:protein phosphotransferase: a membrane-bound enzyme of
            endoplasmic reticulum.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 77 (1980) 1927-31.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:3949741]
  AUTHORS   Tsutsui K.
  TITLE     Tripolyphosphate is an alternative phosphodonor of the selective
            protein phosphorylation of liver microsomal membrane.
  JOURNAL   J. Biol. Chem. 261 (1986) 2645-53.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.7.99.1
            ExPASy - ENZYME nomenclature database: 2.7.99.1
            ExplorEnz - The Enzyme Database: 2.7.99.1
            ERGO genome analysis and discovery system: 2.7.99.1
            BRENDA, the Enzyme Database: 2.7.99.1
            CAS: 74092-32-3
///
ENTRY       EC 2.7.-.-                  Enzyme
CLASS       Transferases;
            Transferring phosphorus-containing groups
REACTION    (1) ATP + D-glycero-D-manno-Heptose 1-phosphate <=> Pyrophosphate +
            ADP-D-glycero-D-manno-heptose [RN:R05644];
            (2) ATP + D-glycero-D-manno-Heptose 7-phosphate <=> ADP +
            D-glycero-D-manno-Heptose 1,7-bisphosphate [RN:R05646];
            (3) Phosphatidylethanolamine + G00141 <=> Diacylglycerol + G00151
            [RN:R05924];
            (4) GDP-L-galactose + Orthophosphate <=> L-Galactose 1-phosphate +
            GDP [RN:R07678]
SUBSTRATE   ATP [CPD:C00002];
            D-glycero-D-manno-Heptose 1-phosphate [CPD:C07838];
            D-glycero-D-manno-Heptose 7-phosphate [CPD:C07836];
            Phosphatidylethanolamine [CPD:C00350];
            [GL:G00141]
PRODUCT     Pyrophosphate [CPD:C00013];
            ADP-D-glycero-D-manno-heptose [CPD:C06397];
            ADP [CPD:C00008];
            D-glycero-D-manno-Heptose 1,7-bisphosphate [CPD:C11472];
            Diacylglycerol [CPD:C00165];
            [GL:G00151]
///
ENTRY       EC 2.8.1.1                  Enzyme
NAME        thiosulfate sulfurtransferase;
            thiosulfate cyanide transsulfurase;
            thiosulfate thiotransferase;
            rhodanese;
            rhodanase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfurtransferases
SYSNAME     thiosulfate:cyanide sulfurtransferase
REACTION    thiosulfate + cyanide = sulfite + thiocyanate [RN:R01931]
ALL_REAC    R01931
SUBSTRATE   thiosulfate [CPD:C00320];
            cyanide [CPD:C00177]
PRODUCT     sulfite [CPD:C00094];
            thiocyanate [CPD:C01755]
COMMENT     A few other sulfur compounds can act as donors.
REFERENCE   1
  AUTHORS   Sorbo, B.H.
  TITLE     Crystalline rhodanese. I. Purification and physicochemical
            examination.
  JOURNAL   Acta Chem. Scand. 7 (1953) 1129-1136.
REFERENCE   2
  AUTHORS   Sorbo, B.H.
  TITLE     Crystalline rhodanese. II. The enzyme catalyzed reaction.
  JOURNAL   Acta Chem. Scand. 7 (1953) 1137-1145.
REFERENCE   3
  AUTHORS   Westley, J. and Green, J.R.
  TITLE     Crystalline beef kidney rhodanese.
  JOURNAL   J. Biol. Chem. 234 (1959) 2325-2326.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K01010  thiosulfate sulfurtransferase
            KO: K02439  thiosulfate sulfurtransferase
GENES       HSA: 7263(TST)
            MMU: 22117(Tst)
            RNO: 25274(Tst)
            CFA: 481275(TST)
            BTA: 280946(TST)
            GGA: 418049(TST)
            XLA: 446361(tst) 495276(LOC495276)
            XTR: 448116(tst)
            SPU: 579216(LOC579216) 591646(LOC591646)
            CEL: D2023.5 F11G11.9 H12D21.4
            ATH: AT1G79230(ST1)
            OSA: 4328418
            SCE: YOR251C
            AGO: AGOS_AAL096W
            PIC: PICST_60020(THT5)
            CGR: CAGL0K09064g
            AFM: AFUA_7G01370
            AOR: AO090010000212
            CNE: CND03690
            TET: TTHERM_00920760
            ECO: b1757(ynjE) b3425(glpE)
            ECJ: JW3388(glpE) JW5287(ynjE)
            ECE: Z2789 Z4785(glpE)
            ECS: ECs2463 ECs4268
            ECC: c2158 c4202(glpE)
            ECI: UTI89_C1953 UTI89_C3925(glpE)
            ECP: ECP_1703 ECP_3510
            ECV: APECO1_3042(glpE) APECO1_827(ynjE)
            ECW: EcE24377A_1518(pspE) EcE24377A_1980 EcE24377A_3901(glpE)
            ECX: EcHS_A1423 EcHS_A3622(glpE)
            STY: STY2779(sseA) STY4278(glpE)
            STT: t0323(sseA) t3988(glpE)
            SPT: SPA0334(sseA) SPA3383(glpE)
            SEC: SC2528(sseA) SC3456(glpE)
            STM: STM2533(sseA) STM3525(glpE)
            YPE: YPO0122 YPO1194
            YPK: y2995(sseA) y3899(glpE)
            YPM: YP_0124(glpE) YP_0942(sseA)
            YPA: YPA_3347
            YPN: YPN_3946
            YPS: YPTB1235 YPTB3777
            YPI: YpsIP31758_3995(glpE)
            SFL: SF3447(glpE)
            SFX: S4317(glpE)
            SFV: SFV_3432(glpE)
            SSN: SSON_1400 SSON_3662(glpE)
            SBO: SBO_1332 SBO_3413(glpE)
            SDY: SDY_3650(glpE)
            ECA: ECA4139(glpE)
            PLU: plu0197(glpE) plu1522(sseA)
            SGL: SG1765 SG2328
            ENT: Ent638_3834
            HIN: HI0679(glpE)
            HIT: NTHI0801(glpE)
            HDU: HD0330(glpE) HD0795
            HSO: HS_0160(glpE)
            PMU: PM1436(glpE)
            MSU: MS1140(sseA) MS1141(sseA) MS2183(pspE)
            APL: APL_0079(glpE) APL_2045(sseA)
            XCC: XCC1537(sseA)
            XCB: XC_2697
            XCV: XCV1628(sseA)
            XAC: XAC1587(sseA)
            XOO: XOO2447(sseA)
            XOM: XOO_2320(XOO2320)
            VCH: VC0100 VCA0620
            VVU: VV1_1160 VV2_0547
            VVY: VV0117 VVA1095
            VPA: VP2952 VPA1175(sseA)
            VFI: VF2448 VFA0101
            PPR: PBPRA0156(glpE) PBPRA1240 PBPRB0882
            PAE: PA0589 PA1292 PA4956(rhdA)
            PAU: PA14_07690(glpE) PA14_65480(rhdA)
            PPU: PP_0398 PP_4907(rhdA-2) PP_5118
            PST: PSPTO_0420 PSPTO_0548
            PSB: Psyr_4630 Psyr_4756
            PSP: PSPPH_0630(glpE) PSPPH_4787
            PFL: PFL_0553(cysA-1) PFL_5652(glpE) PFL_5863
            PFO: Pfl_0510 Pfl_5138
            PEN: PSEEN0295 PSEEN0425(glpE) PSEEN4960(rhdA)
            ACI: ACIAD3561(rhdA)
            SON: SO_1261 SO_4672(glpE)
            SDN: Sden_3617
            SFR: Sfri_3940
            SHE: Shewmr4_3902
            SHM: Shewmr7_3994
            SHN: Shewana3_4106
            ILO: IL0268(glpE)
            CPS: CPS_0122(glpE)
            PHA: PSHAa0367 PSHAa2314(glpE)
            PAT: Patl_0063
            CBU: CBU_0587
            FTU: FTT1748(glpE)
            FTF: FTF1748(glpE)
            FTL: FTL_0010
            FTH: FTH_0010
            FTN: FTN_0120
            NOC: Noc_0191
            AEH: Mlg_1180 Mlg_1897
            HCH: HCH_05396
            CSA: Csal_0923 Csal_2528
            ABO: ABO_1921 ABO_2212(glpE)
            AHA: AHA_0106 AHA_3479
            CVI: CV_4245(sseA)
            RSO: RSc2226(sseA)
            REU: Reut_A1183
            RME: Rmet_2620
            BMA: BMAA0325
            BXE: Bxe_B2831 Bxe_C0931
            BUR: Bcep18194_A4015 Bcep18194_A6185
            BPS: BPSS1766
            BPM: BURPS1710b_3125(moeB) BURPS1710b_A0847(sseA)
            BTE: BTH_II0610
            BPE: BP2280
            BPA: BPP2448
            BBR: BB1896
            POL: Bpro_1376 Bpro_4850
            MPT: Mpe_A2636
            HAR: HEAR2709 HEAR2974
            MMS: mma_0256(sseA1) mma_0326(sseA2)
            EBA: ebA4460(tst)
            AZO: azo0740 azo0849 azo2754(sseA) azo3374
            DAR: Daro_1458 Daro_3055
            CFF: CFF8240_0959
            BBA: Bd2337(sseA)
            DPS: DP2117
            ADE: Adeh_3515
            SAT: SYN_00143
            PUB: SAR11_0189(sseA) SAR11_1074(yceA)
            MLO: mlr0355
            MES: Meso_1426 Meso_3785
            SME: SMb21549(thtR) SMc01172(sseA)
            ATU: Atu1215
            ATC: AGR_C_2243
            RET: RHE_CH01773(sseA)
            RLE: RL1977(sseA)
            BME: BMEI0931
            BMF: BAB1_1075
            BMS: BR1055
            BMB: BruAb1_1060
            BJA: bll5736 bll6690 blr2556
            BRA: BRADO1848 BRADO2770 BRADO5429
            BBT: BBta_2170 BBta_2586 BBta_5416 BBta_5914
            RPA: RPA3613
            RPB: RPB_0306
            CCR: CC_1425
            SIL: SPO3719
            RSP: RSP_0885(sseA) RSP_2581 RSP_2738
            ZMO: ZMO1460(sseA)
            GOX: GOX0068
            MAG: amb1299
            MGM: Mmc1_0501
            SUS: Acid_5630 Acid_6501
            BHA: BH1708
            BAN: BA1599
            BAR: GBAA1599
            BAA: BA_2117
            BAT: BAS1483
            BCE: BC1576
            BCA: BCE_1705
            BCZ: BCZK1455
            BTK: BT9727_0690 BT9727_1455
            BTL: BALH_0708
            BLI: BL01805
            BLD: BLi00344
            BCL: ABC0765
            OIH: OB0532 OB3193
            GKA: GK1556
            CPE: CPE1052
            CPF: CPF_1308
            CPR: CPR_1124
            CDF: CD0121
            CBO: CBO1141
            MTU: Rv0815c(cysA2) Rv2291(sseB) Rv3117(cysA3) Rv3283(sseA)
            MTC: MT0837(sseA-1) MT2348(sseA-2) MT3199(sseA-3) MT3382(sseA-4)
            MBO: Mb0838c(cysA2) Mb2314(sseB) Mb3144(cysA3) Mb3311(sseA)
            MBB: BCG_0867c(cysA2) BCG_3142(cysA3) BCG_3312(sseA)
            MLE: ML0728(sseA) ML2198(cysA3)
            MPA: MAP0645c(cysA3) MAP2046(sseB) MAP3402(sseA)
            MAV: MAV_0756 MAV_4253
            MSM: MSMEG_1809 MSMEG_5789
            MVA: Mvan_5101
            MGI: Mflv_1646
            MMC: Mmcs_1291 Mmcs_4529 Mmcs_4720
            MKM: Mkms_4616 Mkms_4806
            MJL: Mjls_4912 Mjls_5105
            CGL: NCgl0671(cgl0701) NCgl1369(cgl1424) NCgl2678(cgl2775)
            CGB: cg0803(thtR) cg1613(sseA2) cg3073(sseA1)
            CEF: CE0720 CE1557 CE2606
            CDI: DIP0650(sseA) DIP1270 DIP2099
            CJK: jk0205(sseB) jk1668(sseA)
            NFA: nfa10240 nfa5940 nfa9900
            RHA: RHA1_ro00329 RHA1_ro04856 RHA1_ro05373 RHA1_ro06285
            SCO: SCO4164(cysA) SCO5854(SC9B10.21)
            SMA: SAV1336 SAV2412(sseB) SAV4037(cysA2)
            TWH: TWT390(sseA)
            TWS: TW380
            LXX: Lxx10550(sseA)
            CMI: CMM_1667(sseA) CMM_2426(sseB)
            ART: Arth_1666
            AAU: AAur_1807(sseA)
            NCA: Noca_2918
            TFU: Tfu_2719
            FRA: Francci3_0449 Francci3_2415
            FAL: FRAAL0943
            ACE: Acel_0059 Acel_1417
            SEN: SACE_7106(cysA3)
            RXY: Rxyl_0976 Rxyl_2352 Rxyl_2802
            LIL: LA2947
            LIC: LIC11115(sseA)
            LBJ: LBJ_2050(sseA)
            LBL: LBL_1000(sseA)
            SYC: syc1679_c syc2401_c
            SYF: Synpcc7942_1689
            CYB: CYB_2710(rhdA)
            TEL: tll0397
            ANA: all0903 all3918
            AVA: Ava_1779 Ava_4079 Ava_4507
            TER: Tery_4532
            SRU: SRU_0931 SRU_0989
            DRA: DR_0217 DR_2531
            DGE: Dgeo_2206
            TTH: TTC0666 TTC1258
            TTJ: TTHA1028 TTHA1622
            AAE: aq_1076(rhdA1) aq_1799(rhdA2)
            MTH: MTH622
            HAL: VNG2393G(tssA)
            HMA: rrnAC2128(sseA1) rrnAC2129(sseA2)
            HWA: HQ2038A(cysA) HQ2288A HQ3152A HQ3729A(cysA) HQ3730A(cysA)
            NPH: NP2670A NP3186A(cysA)
            PTO: PTO0951
            APE: APE_2595.1
            SSO: SSO1019(cysA-1) SSO1817(cysA-2)
            STO: ST1784 ST2564
            SAI: Saci_2198
            PAI: PAE2733
            PCL: Pcal_1409
            PAS: Pars_0899
STRUCTURES  PDB: 1BOH  1BOI  1DP2  1E0C  1H4K  1H4M  1ORB  1RHD  1RHS  1UAR  
                 2ORA  
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.1.1
            ExPASy - ENZYME nomenclature database: 2.8.1.1
            ExplorEnz - The Enzyme Database: 2.8.1.1
            ERGO genome analysis and discovery system: 2.8.1.1
            BRENDA, the Enzyme Database: 2.8.1.1
            CAS: 9026-04-4
///
ENTRY       EC 2.8.1.2                  Enzyme
NAME        3-mercaptopyruvate sulfurtransferase;
            beta-mercaptopyruvate sulfurtransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfurtransferases
SYSNAME     3-mercaptopyruvate:cyanide sulfurtransferase
REACTION    3-mercaptopyruvate + cyanide = pyruvate + thiocyanate [RN:R07286]
ALL_REAC    R07286;
            (other) R03105 R05208
SUBSTRATE   3-mercaptopyruvate [CPD:C00957];
            cyanide [CPD:C00177]
PRODUCT     pyruvate [CPD:C00022];
            thiocyanate [CPD:C01755]
COMMENT     Sulfite, sulfinates, mercaptoethanol and mercaptopyruvate can also
            act as acceptors. The bacterial enzyme is a zinc protein.
REFERENCE   1
  AUTHORS   Fiedler, H. and Wood, J.L.
  TITLE     Specificity studies on the beta-mercaptopyruvate-cyanide
            transsulfuration system.
  JOURNAL   J. Biol. Chem. 222 (1956) 387-397.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:13673028]
  AUTHORS   HYLIN JW, WOOD JL.
  TITLE     Enzymatic formation of polysulfides from mercaptopyruvate.
  JOURNAL   J. Biol. Chem. 234 (1959) 2141-4.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Sorbo, B.H.
  TITLE     Enzymic transfer of sulfur from mercaptopyruvate to sulfite or
            sulfinates.
  JOURNAL   Biochem. Biophys. Acta 24 (1957) 324-329.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:4550801]
  AUTHORS   Vachek H, Wood JL.
  TITLE     Purification and properties of mercaptopyruvate sulfur transferase
            of Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 258 (1972) 133-46.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:6026243]
  AUTHORS   Van den Hamer CJ, Morell AG, Scheinberg IH.
  TITLE     A study of the cooper content of beta-mercaptopyruvate
            trans-sulfurase.
  JOURNAL   J. Biol. Chem. 242 (1967) 2514-6.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00272  Cysteine metabolism
ORTHOLOGY   KO: K01011  3-mercaptopyruvate sulfurtransferase
GENES       HSA: 4357(MPST)
            MMU: 246221(Mpst)
            RNO: 192172(Mpst)
            CFA: 474515(MPST)
            PIC: PICST_60020(THT5)
            TBR: Tb927.7.5920
            TCR: 508173.40
            LMA: LmjF05.0970
            ECO: b2521(sseA)
            ECJ: JW2505(sseA)
            ECE: Z3788(sseA)
            ECS: ECs3387
            ECC: c3044(sseA)
            ECI: UTI89_C2843(sseA)
            ECP: ECP_2526
            ECV: APECO1_4003(sseA)
            ECW: EcE24377A_2805(sseA)
            ECX: EcHS_A2672(sseA)
            YPA: YPA_0906
            YPN: YPN_2782
            YPP: YPDSF_2501
            YPI: YpsIP31758_2787(sseA)
            SSN: SSON_2603(sseA)
            SBO: SBO_2545(sseA)
            SDY: SDY_2717(sseA)
            ECA: ECA3227(sseA)
            ENT: Ent638_3017
            VFI: VF1387
            PFO: Pfl_5343
            SFR: Sfri_3019
            SLO: Shew_0968
            SPC: Sputcn32_1088
            SHE: Shewmr4_2924
            SHM: Shewmr7_3006
            SHN: Shewana3_3103
            SHW: Sputw3181_3076
            PHA: PSHAa0459(sseA)
            PAT: Patl_2221
            PIN: Ping_0854
            MCA: MCA1555(sseA)
            NOC: Noc_0593
            REU: Reut_A0877
            BVI: Bcep1808_4252
            BUR: Bcep18194_B2215
            BCN: Bcen_4490
            BCH: Bcen2424_3875
            BAM: Bamb_3246
            BPD: BURPS668_A2539
            PNU: Pnuc_1708
            RFR: Rfer_2880
            POL: Bpro_1742
            PNA: Pnap_1496
            AAV: Aave_2010 Aave_3212
            AJS: Ajs_1033
            VEI: Veis_3278
            HAR: HEAR0273
            TBD: Tbd_2489
            BRA: BRADO5744(sseA)
            BBT: BBta_2500 BBta_6256(sseA) BBta_7251
            RPB: RPB_1915
            RPC: RPC_2127
            RPD: RPD_3457
            RPE: RPE_2035
            NWI: Nwi_2490
            NHA: Nham_2916
            SIT: TM1040_2634
            RSH: Rsph17029_2544
            JAN: Jann_0030
            RDE: RD1_0934(mst)
            PDE: Pden_0631
            MMR: Mmar10_1494
            NAR: Saro_2553
            SAL: Sala_3061
            GBE: GbCGDNIH1_0971
            RRU: Rru_A1615
            CDF: CD1535(sseA)
            CBO: CBO0792(sseA)
            MVA: Mvan_5322
            MGI: Mflv_1452
            ART: Arth_2635
            TFU: Tfu_0354
            FAL: FRAAL5355(sseA)
            SEN: SACE_1777(sseA)
            SYF: Synpcc7942_2427
            TER: Tery_0556
            DGE: Dgeo_0159
STRUCTURES  PDB: 1OKG  1URH  
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.1.2
            ExPASy - ENZYME nomenclature database: 2.8.1.2
            ExplorEnz - The Enzyme Database: 2.8.1.2
            ERGO genome analysis and discovery system: 2.8.1.2
            BRENDA, the Enzyme Database: 2.8.1.2
            CAS: 9026-05-5
///
ENTRY       EC 2.8.1.3                  Enzyme
NAME        thiosulfate---thiol sulfurtransferase;
            glutathione-dependent thiosulfate reductase;
            sulfane reductase;
            sulfane sulfurtransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfurtransferases
SYSNAME     thiosulfate:thiol sulfurtransferase
REACTION    thiosulfate + 2 glutathione = sulfite + glutathione disulfide +
            sulfide [RN:R01875]
ALL_REAC    R01875
SUBSTRATE   thiosulfate [CPD:C00320];
            glutathione [CPD:C00051]
PRODUCT     sulfite [CPD:C00094];
            glutathione disulfide [CPD:C00127];
            sulfide [CPD:C00297]
COMMENT     The primary product is glutathione hydrodisulfide, which reacts with
            glutathione to give glutathione disulfide and sulfide. L-Cysteine
            can also act as acceptor.
REFERENCE   1  [PMID:14484816]
  AUTHORS   PECK HD Jr, FISHER E Jr.
  TITLE     The oxidation of thiosulfate and phosphorylation in extracts of
            Thiobacillus thioparus.
  JOURNAL   J. Biol. Chem. 237 (1962) 190-7.
  ORGANISM  Thiobacillus thioparus
REFERENCE   2
  AUTHORS   Sido, B. and Koj, A.
  TITLE     Separation of rhodanese and thiosulfate reductase activities in carp
            liver extracts.
  JOURNAL   Acta Biol. Cracow Ser. Zoo. 15 (1972) 97-103.
  ORGANISM  carp
REFERENCE   3  [PMID:383018]
  AUTHORS   Uhteg LC, Westley J.
  TITLE     Purification and steady-state kinetic analysis of yeast thiosulfate
            reductase.
  JOURNAL   Arch. Biochem. Biophys. 195 (1979) 211-22.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00480  Glutathione metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.1.3
            ExPASy - ENZYME nomenclature database: 2.8.1.3
            ExplorEnz - The Enzyme Database: 2.8.1.3
            ERGO genome analysis and discovery system: 2.8.1.3
            BRENDA, the Enzyme Database: 2.8.1.3
            CAS: 111070-24-7
///
ENTRY       EC 2.8.1.4                  Enzyme
NAME        tRNA sulfurtransferase;
            transfer ribonucleate sulfurtransferase;
            RNA sulfurtransferase;
            ribonucleate sulfurtransferase;
            transfer RNA sulfurtransferase;
            transfer RNA thiolase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfurtransferases
SYSNAME     L-cysteine:tRNA sulfurtransferase
REACTION    L-cysteine + 'activated' tRNA = L-serine + tRNA containing a
            thionucleotide [RN:R03923]
ALL_REAC    R03923
SUBSTRATE   L-cysteine [CPD:C00097];
            'activated' tRNA [CPD:C02342]
PRODUCT     L-serine [CPD:C00065];
            tRNA containing a thionucleotide [CPD:C04161]
COMMENT     A group of enzymes transferring sulfur to various nucleotides in a
            tRNA chain, producing residues such as 4-thiouridylate. With some
            enzymes mercaptopyruvate can act as sulfur donor.
REFERENCE   1  [PMID:5541999]
  AUTHORS   Abrell JW, Kaufman EE, Lipsett MN.
  TITLE     The biosynthesis of 4-thiouridylate. Separation and purification of
            two enzymes in the transfer ribonucleic acid-sulfurtransferase
            system.
  JOURNAL   J. Biol. Chem. 246 (1971) 294-301.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:5334200]
  AUTHORS   Hayward RS, Weiss SB.
  TITLE     RNA thiolase: the enzymatic transfer of sulfur from cysteine to sRNA
            in Escherichia coli extracts.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 55 (1966) 1161-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:5334201]
  AUTHORS   Lipsett MN, Peterkofsky A.
  TITLE     Enzymatic thiolation of E. coli sRNA.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 55 (1966) 1169-74.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:4987417]
  AUTHORS   Wong TW, Weiss SB, Eliceiri GL, Bryant J.
  TITLE     Ribonucleic acid sulfurtransferase from Bacillus subtilis W168.
            Sulfuration with beta-mercaptopyruvate and properties of the enzyme
            system.
  JOURNAL   Biochemistry. 9 (1970) 2376-86.
  ORGANISM  Bacillus subtilis [GN:bsu]
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.1.4
            ExPASy - ENZYME nomenclature database: 2.8.1.4
            ExplorEnz - The Enzyme Database: 2.8.1.4
            ERGO genome analysis and discovery system: 2.8.1.4
            BRENDA, the Enzyme Database: 2.8.1.4
            CAS: 9055-57-6
///
ENTRY       EC 2.8.1.5                  Enzyme
NAME        thiosulfate---dithiol sulfurtransferase;
            thiosulfate reductase;
            TSR
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfurtransferases
SYSNAME     thiosulfate:dithioerythritol sulfurtransferase
REACTION    thiosulfate + dithioerythritol = sulfite +
            4,5-cis-dihydroxy-1,2-dithiacyclohexane (i.e. oxidized
            dithioerythritol) + sulfide
ALL_REAC    (other) R03085 R05072
SUBSTRATE   thiosulfate [CPD:C00320];
            dithioerythritol [CPD:C00950]
PRODUCT     sulfite [CPD:C00094];
            4,5-cis-dihydroxy-1,2-dithiacyclohexane [CPD:C06484];
            sulfide [CPD:C00297]
COMMENT     The enzyme from Chlorella shows very little activity towards
            monothiols such as glutathione and cysteine (cf. EC 2.8.1.3
            thiosulfate---thiolsulfurtransferase). The enzyme probably transfers
            the sulfur atom onto one thiol group to form -S-S-, and sulfide is
            spontaneously expelled from this by reaction with the other thiol
            group. May be identical with EC 2.8.1.1 thiosulfate
            sulfurtransferase.
REFERENCE   1
  AUTHORS   Schmidt, A., Erdle, I. and Gamon, B.
  TITLE     Isolation and characterization of thiosulfate reductases from the
            green alga Chlorella fusca.
  JOURNAL   Planta 162 (1984) 243-249.
  ORGANISM  Chlorella fusca
PATHWAY     PATH: map00920  Sulfur metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.1.5
            ExPASy - ENZYME nomenclature database: 2.8.1.5
            ExplorEnz - The Enzyme Database: 2.8.1.5
            ERGO genome analysis and discovery system: 2.8.1.5
            BRENDA, the Enzyme Database: 2.8.1.5
            CAS: 9059-49-8
///
ENTRY       EC 2.8.1.6                  Enzyme
NAME        biotin synthase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfurtransferases
SYSNAME     dethiobiotin:sulfur sulfurtransferase
REACTION    dethiobiotin + sulfur + 2 S-adenosyl-L-methionine = biotin + 2
            L-methionine + 2 5'-deoxyadenosine [RN:R01078]
ALL_REAC    R01078
SUBSTRATE   dethiobiotin [CPD:C01909];
            sulfur [CPD:C00087];
            S-adenosyl-L-methionine [CPD:C00019]
PRODUCT     biotin [CPD:C00120];
            L-methionine [CPD:C00073];
            5'-deoxyadenosine [CPD:C05198]
COFACTOR    Iron-sulfur [CPD:C00824]
COMMENT     This single-turnover enzyme is a member of the 'AdoMet radical '
            (radical SAM) family, all members of which produce the
            5'-deoxyadenosin-5'-yl radical and methionine from AdoMet [i.e.
            S-adenosylmethionine, or S-(5'-deoxyadenosin-5'-yl)methionine], by
            the addition of an electron from an iron-sulfur centre. The enzyme
            has both a [2Fe-2S] and a [4Fe-4S] centre, and the latter is
            believed to donate the electron. Two molecules of AdoMet are
            converted into radicals; these activate positions 6 and 9 of
            dethiobiotin by abstracting a hydrogen atom from each, and thereby
            forming 5'-deoxyadenosine. Sulfur insertion into dethiobiotin at C-6
            takes place with retention of configuration [3]. The sulfur donor
            has not been identified to date --- it is neither elemental sulfur
            nor from AdoMet, but it may be from the [2Fe-2S] centre [4].
REFERENCE   1  [PMID:2971595]
  AUTHORS   Shiuan D, Campbell A.
  TITLE     Transcriptional regulation and gene arrangement of Escherichia coli,
            Citrobacter freundii and Salmonella typhimurium biotin operons.
  JOURNAL   Gene. 67 (1988) 203-11.
  ORGANISM  Escherichia coli [GN:eco], Citrobacter freundii, Salmonella
            typhimurium
REFERENCE   2  [PMID:8117110]
  AUTHORS   Zhang S, Sanyal I, Bulboaca GH, Rich A, Flint DH.
  TITLE     The gene for biotin synthase from Saccharomyces cerevisiae: cloning,
            sequencing, and complementation of Escherichia coli strains lacking
            biotin synthase.
  JOURNAL   Arch. Biochem. Biophys. 309 (1994) 29-35.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Trainor, D.A., Parry, R.J. and Gitterman, A.
  TITLE     Biotin biosynthesis. 2. Stereochemistry of sulfur introduction at
            C-4 of dethiobiotin.
  JOURNAL   J. Am. Chem. Soc. 102 (1980) 1467-1468.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:16042606]
  AUTHORS   Lotierzo M, Tse Sum Bui B, Florentin D, Escalettes F, Marquet A.
  TITLE     Biotin synthase mechanism: an overview.
  JOURNAL   Biochem. Soc. Trans. 33 (2005) 820-3.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:14704425]
  AUTHORS   Berkovitch F, Nicolet Y, Wan JT, Jarrett JT, Drennan CL.
  TITLE     Crystal structure of biotin synthase, an
            S-adenosylmethionine-dependent radical enzyme.
  JOURNAL   Science. 303 (2004) 76-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:11444981]
  AUTHORS   Ugulava NB, Gibney BR, Jarrett JT.
  TITLE     Biotin synthase contains two distinct iron-sulfur cluster binding
            sites: chemical and spectroelectrochemical analysis of iron-sulfur
            cluster interconversions.
  JOURNAL   Biochemistry. 40 (2001) 8343-51.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00780  Biotin metabolism
ORTHOLOGY   KO: K01012  biotin synthetase
GENES       OSA: 4346185
            CME: CML210C
            SCE: YGR286C(BIO2)
            PIC: PICST_30955(BIO2)
            SPO: SPCC1235.02(bio2)
            ANI: AN6643.2
            AFM: AFUA_6G03670
            CNE: CNF03970
            UMA: UM00315.1
            ECO: b0775(bioB)
            ECJ: JW0758(bioB)
            ECE: Z0994(bioB)
            ECS: ECs0853
            ECC: c0855(bioB)
            ECI: UTI89_C0773(bioB)
            ECP: ECP_0789
            ECV: APECO1_1314(bioB)
            ECW: EcE24377A_0838(bioB)
            ECX: EcHS_A0828(bioB)
            STY: STY0827(bioB)
            STT: t2093(bioB)
            SPT: SPA1958(bioB)
            SEC: SC0792(bioB)
            STM: STM0794(bioB)
            YPE: YPO1151(bioB)
            YPK: y3031(bioB)
            YPM: YP_1009(bioB)
            YPA: YPA_1058
            YPN: YPN_2850
            YPP: YPDSF_2546
            YPS: YPTB1182(bioB)
            YPI: YpsIP31758_2844(bioB)
            SFL: SF0724(bioB)
            SFX: S0766(bioB)
            SFV: SFV_0757(bioB)
            SSN: SSON_0754(bioB)
            SBO: SBO_0662(bioB)
            SDY: SDY_0831(bioB)
            ECA: ECA2825(bioB)
            PLU: plu1485(bioB)
            BUC: BU291(bioB)
            BAS: BUsg280(bioB)
            BAB: bbp272(bioB)
            WBR: WGLp453(bioB)
            SGL: SG0903
            ENT: Ent638_1266
            KPN: KPN_00800(bioB)
            SPE: Spro_1311
            HIT: NTHI1188(bioB)
            HDU: HD1007(bioB)
            HSO: HS_1010(bioB)
            PMU: PM0379(bioB)
            MSU: MS1523(bioB)
            APL: APL_0117(bioB)
            ASU: Asuc_1132
            XFA: XF0064
            XFT: PD0043(bioB)
            XCC: XCC0388(bioB)
            XCB: XC_0400
            XCV: XCV0403(bioB)
            XAC: XAC0388(bioB)
            XOO: XOO0455(bioB)
            XOM: XOO_0419(XOO0419)
            VCH: VC1112
            VCO: VC0395_A0630(bioB)
            VVU: VV1_2943
            VVY: VV1327
            VPA: VP1113
            PPR: PBPRA2329
            PAE: PA0500(bioB)
            PAU: PA14_06500(bioB)
            PAP: PSPA7_0600(bioB)
            PPU: PP_0362(bioB)
            PPF: Pput_0388
            PST: PSPTO_0494(bioB)
            PSB: Psyr_4687
            PSP: PSPPH_4721(bioB)
            PFL: PFL_5693
            PFO: Pfl_5176
            PEN: PSEEN5121(bioB)
            PMY: Pmen_4088
            PAR: Psyc_1861(bioB)
            PCR: Pcryo_2150
            PRW: PsycPRwf_2187
            ACI: ACIAD2045(bioB)
            SON: SO_2740(bioB) SO_3925
            SDN: Sden_1658
            SFR: Sfri_1475
            SAZ: Sama_1438
            SBL: Sbal_1758
            SBM: Shew185_1751
            SLO: Shew_1719
            SPC: Sputcn32_2345
            SSE: Ssed_2776
            SPL: Spea_1801
            SHE: Shewmr4_2359 Shewmr4_3255
            SHM: Shewmr7_2431
            SHN: Shewana3_0706 Shewana3_2519
            SHW: Sputw3181_1663
            ILO: IL1324(bioB)
            CPS: CPS_2594(bioB)
            PHA: PSHAa1609(bioB)
            PAT: Patl_2557
            SDE: Sde_3139
            PIN: Ping_1924
            MAQ: Maqu_2756
            CBU: CBU_1007(bioB)
            CBD: COXBU7E912_1040(bioB)
            LPN: lpg1472
            LPF: lpl1556(bioB)
            LPP: lpp1428(bioB)
            MCA: MCA1125(bioB)
            FTU: FTT0937c(bioB)
            FTF: FTF0937c(bioB)
            FTW: FTW_0831(bioB)
            FTL: FTL_1272
            FTH: FTH_1245(bioB)
            FTA: FTA_1345(bioB)
            FTN: FTN_0815(bioB)
            TCX: Tcr_1978
            NOC: Noc_2101
            AEH: Mlg_2436
            HHA: Hhal_0963
            HCH: HCH_05371(bioB)
            CSA: Csal_1167
            ABO: ABO_2220(bioB)
            MMW: Mmwyl1_3457
            AHA: AHA_1489(bioB)
            BCI: BCI_0246(bioB)
            RMA: Rmag_0499
            VOK: COSY_0459(bioB)
            NME: NMB1146 NMB1184
            NMA: NMA1358(bioB)
            NMC: NMC1087(bioB)
            NGO: NGO0813
            CVI: CV_4381(bioB)
            RSO: RSc0266(bioB)
            REU: Reut_A0150
            REH: H16_A0183(bioB)
            RME: Rmet_0117
            BMA: BMA0103(bioB)
            BMV: BMASAVP1_A3077(bioB)
            BML: BMA10299_A2017(bioB)
            BMN: BMA10247_2269(bioB)
            BXE: Bxe_A4266
            BVI: Bcep1808_3029
            BUR: Bcep18194_A6278
            BCN: Bcen_2320
            BCH: Bcen2424_2934
            BAM: Bamb_2983
            BPS: BPSL0364(bioB)
            BPM: BURPS1710b_0570(bioB)
            BPL: BURPS1106A_0409(bioB)
            BPD: BURPS668_0388(bioB)
            BTE: BTH_I0337(bioB)
            PNU: Pnuc_0156
            BPE: BP2718
            BPA: BPP1121
            BBR: BB1337
            RFR: Rfer_2292
            POL: Bpro_0897 Bpro_1580
            PNA: Pnap_4030
            AAV: Aave_2518
            AJS: Ajs_2045
            MPT: Mpe_A1786
            HAR: HEAR0102(bioB)
            MMS: mma_0123(bioB)
            NEU: NE2300(bioB)
            NET: Neut_2138
            NMU: Nmul_A1129
            EBA: ebA1066(bioB)
            AZO: azo2817(bioB)
            DAR: Daro_0618
            TBD: Tbd_0319
            MFA: Mfla_2164
            HPY: HP1406
            HPA: HPAG1_0639 HPAG1_1330
            HHE: HH1731(bioB)
            HAC: Hac_1730(bioB)
            WSU: WS1500(bioB)
            TDN: Tmden_0169
            CJE: Cj1685c(bioB)
            CJR: CJE1853(bioB)
            CJJ: CJJ81176_1677(bioB)
            CJU: C8J_1582(bioB)
            CJD: JJD26997_2057(bioB)
            CFF: CFF8240_0176
            CCV: CCV52592_0574
            CHA: CHAB381_0711(bioB)
            CCO: CCC13826_2293
            ABU: Abu_2237(bioB)
            NIS: NIS_1653(bioB)
            SUN: SUN_0087(bioB)
            GSU: GSU1584(bioB)
            GME: Gmet_1582
            GUR: Gura_2242
            PCA: Pcar_1458 Pcar_1607 Pcar_1632 Pcar_1722
            PPD: Ppro_1175
            DVU: DVU1767 DVU2558(bioB)
            DVL: Dvul_0690
            DDE: Dde_2277(miaB) Dde_2655
            LIP: LI0420(bioB)
            DPS: DP0475 DP2376 DP2549(bioB)
            ADE: Adeh_3453
            AFW: Anae109_3562
            MXA: MXAN_1257(bioB)
            SAT: SYN_00212 SYN_02134
            SFU: Sfum_1825 Sfum_1844
            RFE: RF_0527(bioB)
            AMA: AM969(bioB)
            APH: APH_0218(bioB)
            ERU: Erum6500(bioB)
            ERW: ERWE_CDS_06820(bioB)
            ERG: ERGA_CDS_06730(bioB)
            ECN: Ecaj_0657
            ECH: ECH_0352(bioB)
            NSE: NSE_0612(bioB)
            MLO: mll5831 mll6007 mll9100
            PLA: Plav_0036
            ATU: Atu3997(bioB)
            ATC: AGR_L_1708(bioB)
            BME: BMEII0775
            BMF: BAB2_0744(bioB)
            BMS: BRA0492(bioB)
            BMB: BruAb2_0730(bioB)
            BOV: BOV_A0430(bioB)
            OAN: Oant_2823
            BJA: blr2095(bioB)
            BRA: BRADO2424(bioB)
            BBT: BBta_2776(bioB)
            RPA: RPA2045(bioB)
            RPB: RPB_3331
            RPC: RPC_3236
            RPD: RPD_2111
            RPE: RPE_2208
            NWI: Nwi_0243
            NHA: Nham_0277
            XAU: Xaut_1117
            CCR: CC_3521
            SIL: SPO3338(bioB)
            RSP: RSP_1923(bioB)
            RSH: Rsph17029_0574
            RDE: RD1_2561(bioY)
            PDE: Pden_1433 Pden_2916
            MMR: Mmar10_0058
            HNE: HNE_0048(bioB)
            ZMO: ZMO0094(bioB)
            NAR: Saro_0719
            SAL: Sala_1222
            SWI: Swit_2890
            ELI: ELI_04920
            GOX: GOX2031
            GBE: GbCGDNIH1_0499
            ACR: Acry_1869
            MAG: amb2757
            MGM: Mmc1_0034
            BSU: BG11525(bioB)
            BHA: BH1748(bioB)
            BAN: BA4336(bioB)
            BAR: GBAA4336(bioB)
            BAA: BA_4795
            BAT: BAS4023
            BCE: BC4114
            BCA: BCE_4184(bioB)
            BCZ: BCZK3870(bioB)
            BCY: Bcer98_2813
            BTK: BT9727_3856(bioB)
            BLI: BL00956(bioB)
            BLD: BLi00770(bioB)
            BAY: RBAM_018250(bioB)
            BPU: BPUM_2779(bioB)
            OIH: OB1717
            GKA: GK1570(bioB)
            SAU: SA2213(bioB)
            SAV: SAV2425(bioB)
            SAM: MW2348(bioB)
            SAR: SAR2515(bioB)
            SAS: SAS2316
            SAC: SACOL2426(bioB)
            SAB: SAB2306c(bioB)
            SAA: SAUSA300_2371(bioB)
            SAO: SAOUHSC_02714
            SAJ: SaurJH9_2451
            SAH: SaurJH1_2499
            SEP: SE0234
            SER: SERP2347(bioB)
            SHA: SH0269(bioB)
            LLM: llmg_0332
            SAG: SAG0464(bioB)
            SAN: gbs0511
            SAK: SAK_0566(bioB)
            SGO: SGO_0746(bioY-1) SGO_1070(bioY-2)
            STH: STH353
            CAC: CAC0210(bioB) CAC1631
            CPE: CPE1544(bioB) CPE2460(bioB)
            CPF: CPF_1795(bioB) CPF_2775
            CPR: CPR_2462
            CTC: CTC00151 CTC01327
            CNO: NT01CX_1470(bioB) NT01CX_1484
            CTH: Cthe_0020
            CDF: CD0297
            CBO: CBO3582(bioB)
            CBA: CLB_2200(bioB)
            CBH: CLC_2183(bioB)
            CBF: CLI_2309(bioB)
            CBE: Cbei_1914
            CKL: CKL_1696(bioB2)
            AMT: Amet_3241
            CHY: CHY_0889(bioB) CHY_2448
            DSY: DSY3492 DSY3831 DSY4958
            DRM: Dred_0430
            SWO: Swol_1020
            CSC: Csac_0307
            TTE: TTE1073(bioB) TTE1885(bioB2)
            MTA: Moth_1735
            MTU: Rv1589(bioB)
            MTC: MT1624(bioB)
            MBO: Mb1615(bioB)
            MLE: ML1220(bioB)
            MPA: MAP1283(bioB)
            MAV: MAV_3196(bioB)
            MSM: MSMEG_3194(bioB)
            MVA: Mvan_2793
            MGI: Mflv_3624
            MMC: Mmcs_3073
            MKM: Mkms_3133
            MJL: Mjls_3090
            CGL: NCgl0071(cgl0072)
            CGB: cg0095(bioB)
            CEF: CE0089(bioB)
            CDI: DIP0105(bioB) DIP1124
            CJK: jk0682(bioB)
            NFA: nfa18320(bioB)
            RHA: RHA1_ro01043
            SCO: SCO1244(2SCG1.19)
            SMA: SAV7093(bioB)
            ART: Arth_0875
            AAU: AAur_1091(bioB)
            PAC: PPA1407
            NCA: Noca_3415
            FRA: Francci3_3763 Francci3_4187
            FAL: FRAAL6003(bioB)
            ACE: Acel_1035
            SEN: SACE_4683(bioB)
            STP: Strop_1569
            FNU: FN1000
            RBA: RB10275(bioB)
            CPN: CPn1044(bioB)
            CPA: CP0808
            CPJ: CPj1044(bioB)
            CPT: CpB1084
            CAB: CAB685(bioB)
            CFE: CF0298(bioB)
            LIL: LA2143(bioB)
            LIC: LIC11777(bioB)
            LBJ: LBJ_1870(bioB)
            LBL: LBL_1414(bioB)
            SYN: slr1364(bioB)
            SYW: SYNW0933(bioB)
            SYC: syc1098_d(bioB)
            SYF: Synpcc7942_0419
            SYD: Syncc9605_1632
            SYE: Syncc9902_1394
            SYG: sync_1032(bioB)
            SYR: SynRCC307_0793(bioB)
            SYX: SynWH7803_1530(bioB)
            CYA: CYA_2658(bioB)
            TEL: tll0661(bioB)
            GVI: glr4328(bioB)
            ANA: alr1921
            AVA: Ava_4389
            PMA: Pro1102(cioB)
            PMM: PMM1093(bioB)
            PMT: PMT1056(bioB)
            PMN: PMN2A_0655
            PMI: PMT9312_1104
            PMB: A9601_11991(bioB)
            PMC: P9515_11841(bioB)
            PMF: P9303_09961(bioB)
            PMG: P9301_12001(bioB)
            PMH: P9215_12291(bioB)
            PME: NATL1_14871(bioB)
            TER: Tery_3533
            BTH: BT_1442 BT_1835
            BFR: BF3893
            BFS: BF3663
            PGI: PG2081(bioB)
            SRU: SRU_0756(bioB)
            CHU: CHU_2466(bioB)
            GFO: GFO_3566(bioB)
            FJO: Fjoh_0801
            FPS: FP0234(bioB)
            CTE: CT0052(bioB)
            CCH: Cag_0078
            CPH: Cpha266_0112
            PVI: Cvib_1711
            PLT: Plut_2070
            TTH: TTC0242
            TTJ: TTHA0607
            AAE: aq_975(bioB)
            TMA: TM1269
            TPT: Tpet_0559
            MJA: MJ0785
            MMP: MMP0126(bioB) MMP1238(bioB)
            MMQ: MmarC5_0353
            MMZ: MmarC7_0484
            MAE: Maeo_0183
            MVN: Mevan_0552
            MAC: MA0154(bioB)
            MBA: Mbar_A0838
            MMA: MM_1444
            MBU: Mbur_2085
            MTH: MTH1143
            MSI: Msm_0573
            MKA: MK0016
            HMA: rrnAC0883(bioB)
            NPH: NP4236A(bioB)
            PHO: PH0234
            PAB: PAB2355(bioB-like)
            PFU: PF0144
            TKO: TK2248
            SSO: SSO1115(bioB)
            STO: ST1886
            SAI: Saci_0343
STRUCTURES  PDB: 1R30  
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.1.6
            ExPASy - ENZYME nomenclature database: 2.8.1.6
            ExplorEnz - The Enzyme Database: 2.8.1.6
            ERGO genome analysis and discovery system: 2.8.1.6
            BRENDA, the Enzyme Database: 2.8.1.6
            CAS: 80146-93-6
///
ENTRY       EC 2.8.1.7                  Enzyme
NAME        cysteine desulfurase;
            IscS;
            NIFS;
            NifS;
            SufS;
            cysteine desulfurylase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfurtransferases
SYSNAME     L-cysteine:[enzyme cysteine] sulfurtransferase
REACTION    L-cysteine + [enzyme]-cysteine = L-alanine +
            [enzyme]-S-sulfanylcysteine
ALL_REAC    (other) R07460
SUBSTRATE   L-cysteine [CPD:C00097];
            [enzyme]-cysteine
PRODUCT     L-alanine [CPD:C00041];
            [enzyme]-S-sulfanylcysteine
COMMENT     A pyridoxal-phosphate protein. The reaction shown is the first part
            of a catalytic reaction, which is completed by passing on its extra
            sulfur to other acceptors. In Azotobacter vinelandii, this sulfur
            provides the inorganic sulfide required for nitrogenous
            metallocluster formation [1]. The enzyme is involved in the
            biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA,
            thiamine, biotin, lipoate and pyranopterin (molybdopterin) and
            functions by mobilizing sulfur [2].
REFERENCE   1  [PMID:8464885]
  AUTHORS   Zheng L, White RH, Cash VL, Jack RF, Dean DR.
  TITLE     Cysteine desulfurase activity indicates a role for NIFS in
            metallocluster biosynthesis.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 2754-8.
  ORGANISM  Azotobacter vinelandii
REFERENCE   2  [PMID:12382038]
  AUTHORS   Mihara H, Esaki N.
  TITLE     Bacterial cysteine desulfurases: their function and mechanisms.
  JOURNAL   Appl. Microbiol. Biotechnol. 60 (2002) 12-23.
  ORGANISM  Azotobacter vinelandii, Escherichia coli [GN:eco], Haemophilus
            influenzae, Pseudomonas aeruginosa, Synechocystis sp.
REFERENCE   3  [PMID:12714048]
  AUTHORS   Frazzon J, Dean DR.
  TITLE     Formation of iron-sulfur clusters in bacteria: an emerging field in
            bioinorganic chemistry.
  JOURNAL   Curr. Opin. Chem. Biol. 7 (2003) 166-73.
  ORGANISM  Azotobacter vinelandii, Escherichia coli [GN:eco], Helicobacter
            pylori
PATHWAY     PATH: map00730  Thiamine metabolism
ORTHOLOGY   KO: K04487  cysteine desulfurase
GENES       HSA: 9054(NFS1)
            MMU: 18041(Nfs1)
            RNO: 84594(Nfs1)
            CFA: 477214(NFS1)
            GGA: 419133(RCJMB04_9m12)
            SPU: 584446(LOC584446)
            DME: Dmel_CG12264
            CEL: B0205.6(aminotransferase)
            ATH: AT5G65720(ATNIFS1/NIFS1)
            OSA: 4346775
            CME: CMT234C
            SCE: YCL017C(NFS1)
            AGO: AGOS_AAL013W
            PIC: PICST_85588
            CAL: CaO19.7081
            CGR: CAGL0H03817g
            SPO: SPBC21D10.11c
            ANI: AN2508.2
            AFM: AFUA_3G14240
            AOR: AO090020000619
            CNE: CND05560
            ECU: ECU11_1770
            DDI: DDB_0232198
            PFA: MAL7P1.150
            CPV: cgd4_3040
            CHO: Chro.40346
            TPV: TP01_0024
            TET: TTHERM_00085100 TTHERM_00418550 TTHERM_01169360
            TBR: Tb11.55.0013
            TCR: 506629.70 509831.10
            LMA: LmjF27.1060
            EHI: 33.t00021
            ECO: b1680(sufS) b2530(iscS)
            ECJ: JW1670(sufS) JW2514(iscS)
            ECE: Z2708 Z3797(yfhO)
            ECS: ECs2387 ECs3396
            ECC: c2075 c3056(yfhO)
            ECI: UTI89_C1872(sufS) UTI89_C2852(iscS)
            ECP: ECP_2535
            ECV: APECO1_3995(iscS) APECO1_757(sufS)
            ECW: EcE24377A_1896(sufS) EcE24377A_2815(iscS)
                 EcE24377A_3116(csdA)
            ECX: EcHS_A1761(sufS) EcHS_A2681 EcHS_A2954(csdA)
            STY: STY1750 STY2789
            STT: t0313 t1241
            SPT: SPA0323(nifS)
            SEC: SC1393(sufS) SC2537(nifS)
            STM: STM1373(sufS) STM2543(nifS)
            YPE: YPO2138 YPO2400 YPO2896(iscS)
            YPK: y1334 y1938 y2182
            YPM: YP_1941(nifS) YP_2187(csdB1) YP_2558(nifS_2)
            YPA: YPA_1498 YPA_1745 YPA_2337
            YPN: YPN_1241 YPN_1607 YPN_1855
            YPS: YPTB2067 YPTB2310 YPTB2859(iscS)
            YPI: YpsIP31758_1168(iscS) YpsIP31758_1745(sufS)
            SFL: SF2577(yfhO)
            SFX: S1842 S2749(yfhO)
            SFV: SFV_1703 SFV_2578(yfhO)
            SSN: SSON_1476 SSON_2612(yfhO)
            SBO: SBO_1450 SBO_2554(yfhO)
            SDY: SDY_1911 SDY_2726(yfhO)
            ECA: ECA1863(sufS) ECA2945(nifS) ECA3237(iscS)
            PLU: plu0915 plu2618(sufS) plu3283(iscS)
            BUC: BU602(yfhO)
            BAS: BUsg577(nifS)
            BAB: bbp544(nifS)
            BCC: BCc_391(iscS)
            WBR: WGLp284(yfhO) WGLp357
            SGL: SG1435 SG1769
            SPE: Spro_3869
            BFL: Bfl534(nifS)
            BPN: BPEN_373(sufS) BPEN_554(nifS)
            HIN: HI0378(nifS)
            HIT: NTHI0498(nifS2)
            HDU: HD1082(iscS)
            HSO: HS_0281(nifS) HS_0967(csd)
            PMU: PM0318(nifS_1)
            MSU: MS1726(nifS)
            APL: APL_0931(iscS)
            VCH: VC0748 VC2309
            VVU: VV1_0438
            VVY: VV0755
            VPA: VP0596
            VFI: VF0617
            PPR: PBPRA0750
            PAE: PA2062 PA3814(iscS)
            PAU: PA14_14730(iscS) PA14_37830(iscS)
            PAP: PSPA7_1299(iscS)
            PPU: PP_0842(iscS-1) PP_2435(iscS-2)
            PST: PSPTO_0272(iscS-1) PSPTO_1423(iscS-2) PSPTO_3438(iscS-3)
            PSB: Psyr_0134 Psyr_1237(iscS) Psyr_3220
            PSP: PSPPH_1309(iscS) PSPPH_3139 PSPPH_3847 PSPPH_5053
            PFL: PFL_4152 PFL_4965(iscS)
            PFO: Pfl_3912 Pfl_4612(iscS)
            PEN: PSEEN1010(iscS-1) PSEEN3349(iscS-2) PSEEN4228(csdA)
            PAR: Psyc_1477
            PCR: Pcryo_1656
            ACI: ACIAD1404(iscS)
            SON: SO_2264(iscS) SO_3789
            SDN: Sden_0753 Sden_1458
            SFR: Sfri_2424 Sfri_3181
            SAZ: Sama_1506
            SBL: Sbal_2397
            SHE: Shewmr4_1739 Shewmr4_3131
            SHM: Shewmr7_1819
            SHN: Shewana3_0808 Shewana3_2280
            ILO: IL2040
            CPS: CPS_1132(iscS)
            PHA: PSHAa0186(csd) PSHAa1654(csdA) PSHAa2671(iscS)
                 PSHAb0099(iscS)
            PAT: Patl_1238
            SDE: Sde_1413
            PIN: Ping_1324
            CBU: CBU_1129(nifS) CBU_1182(iscS)
            CBD: COXBU7E912_1228(iscS)
            LPN: lpg1746(iscS)
            LPF: lpl1710(iscS)
            MCA: MCA0212(nifS) MCA0247(iscS) MCA2884
            FTU: FTT1226c(iscS)
            FTF: FTF1226c(iscS)
            FTW: FTW_1433
            FTL: FTL_0718
            FTH: FTH_0720(iscS)
            FTA: FTA_1408
            NOC: Noc_1649 Noc_1656 Noc_2487
            HCH: HCH_04461
            CSA: Csal_2848
            ABO: ABO_1872(iscS)
            AHA: AHA_1747(iscS) AHA_4239
            DNO: DNO_1196(iscS)
            BCI: BCI_0006(iscS) BCI_0462(sufS)
            VOK: COSY_0532(iscS)
            NME: NMB1379
            NMA: NMA1594
            NGO: NGO0636
            CVI: CV_1094(nifS)
            RSO: RSc1019(nifS)
            REU: Reut_A1058(iscS) Reut_C6331(iscS)
            REH: H16_A1158(iscS) H16_B0494 H16_B1515(sufS)
            RME: Rmet_1025 Rmet_5230
            BMA: BMA1708(iscS-1) BMAA0379(iscS-2)
            BXE: Bxe_A1553 Bxe_B1444 Bxe_B1453
            BUR: Bcep18194_A5432 Bcep18194_B2318 Bcep18194_B2412
                 Bcep18194_B2622 Bcep18194_B2744
            BCN: Bcen_4665 Bcen_4740 Bcen_5951
            BCH: Bcen2424_2126 Bcen2424_3426 Bcen2424_3517 Bcen2424_3698
            BAM: Bamb_2163 Bamb_5203
            BPS: BPSL2289(iscS) BPSS2121
            BPM: BURPS1710b_2733(iscS) BURPS1710b_A1225(iscS-2)
            BPL: BURPS1106A_2655(iscS) BURPS1106A_A1818
            BPD: BURPS668_2599(iscS)
            BTE: BTH_I1875(iscS)
            BPE: BP1799(iscS)
            BPA: BPP2028(iscS)
            BBR: BB2276(iscS)
            RFR: Rfer_1863 Rfer_2177
            POL: Bpro_2178
            MPT: Mpe_A2262
            HAR: HEAR2239(iscS)
            NEU: NE0174
            NET: Neut_0269 Neut_1238
            NMU: Nmul_A0675 Nmul_A0699
            EBA: ebA6401(iscS) ebA6402(iscS1)
            AZO: azo0552(nifS) azo2016(iscS1) azo2017(iscS2)
            DAR: Daro_1515 Daro_1949 Daro_1950(iscS)
            TBD: Tbd_1164(iscS)
            MFA: Mfla_0808 Mfla_0809
            HPY: HP0220(nifS)
            HPJ: jhp0206
            HPA: HPAG1_0222
            HHE: HH0564(nifS)
            HAC: Hac_1498(nifS)
            WSU: WS2206
            TDN: Tmden_2008
            CJE: Cj0240c
            CJR: CJE0291
            CJU: C8J_0218
            CFF: CFF8240_1696
            CCV: CCV52592_1770(nifS)
            CHA: CHAB381_0042(nifS)
            CCO: CCC13826_1163(nifS)
            ABU: Abu_0608(sufS) Abu_0612(iscS) Abu_2178
            SUN: SUN_0007(iscS)
            GSU: GSU2011 GSU2570 GSU2786
            GME: Gmet_0872 Gmet_0992
            PCA: Pcar_0050 Pcar_1841 Pcar_1860
            DVU: DVU0664
            DDE: Dde_3079
            LIP: LI0265
            BBA: Bd1194(spl1) Bd1938(sufS)
            DPS: DP2229(nifS)
            ADE: Adeh_0592 Adeh_1048
            MXA: MXAN_2983 MXAN_5001
            SAT: SYN_01071 SYN_01251 SYN_02126
            SFU: Sfum_2683
            RPR: RP486(spl1) RP487(spl1)
            RTY: RT0473(iscS1) RT0474(iscS2)
            RCO: RC0730(spl1) RC0731(spl1)
            RFE: RF_0845(iscS) RF_0846(spl1)
            RBE: RBE_0947(iscS) RBE_0948(spl1)
            WOL: WD0705 WD0997(iscS)
            WBM: Wbm0021 Wbm0028
            AMA: AM655(iscS) AM656
            APH: APH_0674(iscS)
            ERU: Erum4150(iscS)
            ERW: ERWE_CDS_04310(iscS)
            ERG: ERGA_CDS_04250(iscS)
            ECN: Ecaj_0410
            ECH: ECH_0629(iscS)
            NSE: NSE_0303(iscS)
            MLO: mll5865(nifS) mlr0015(nifS)
            MES: Meso_1782
            SME: SMc00529(nifS)
            SMD: Smed_2982
            ATU: Atu1825(nifS)
            ATC: AGR_C_3350
            RET: RHE_CH02254(nifSch) RHE_PD00222(nifSd)
            RLE: RL2583(nifS) pRL80059 pRL80073
            BME: BMEI1043
            BMF: BAB1_0947
            BMS: BR0930
            BMB: BruAb1_0939
            BJA: blr1756(nifS) blr4338(nifS)
            BRA: BRADO3539(nifS) BRADO3544(sufS) BRADO5423(nifS)
                 BRADO5444(sufS)
            BBT: BBta_3965(nifS) BBta_3969(sufS) BBta_5907(nifS)
                 BBta_5928(sufS)
            RPA: RPA2463(nifS1) RPA4608(nifS2)
            RPB: RPB_0981(nifS) RPB_2995
            RPC: RPC_2842 RPC_4451
            RPD: RPD_1085 RPD_2455
            RPE: RPE_2969 RPE_4521
            NWI: Nwi_1665
            NHA: Nham_2329
            BHE: BH08650(nifS2)
            BQU: BQ05940(nifS1)
            CCR: CC_1865
            SIT: TM1040_1241
            RSP: RSP_0442 RSP_0530(nifS)
            RSH: Rsph17029_2095
            RSQ: Rsph17025_2363
            JAN: Jann_2365
            RDE: RD1_0802(nifS) RD1_2293 RD1_2698(nifS)
            PDE: Pden_3963
            MMR: Mmar10_1312
            ZMO: ZMO1834(nifS)
            NAR: Saro_2797 Saro_2798
            SAL: Sala_0794
            SWI: Swit_0051
            GBE: GbCGDNIH1_1322 GbCGDNIH1_1943
            RRU: Rru_A1068 Rru_A2027 Rru_A2570 Rru_A3040
            MAG: amb3028 amb3029
            MGM: Mmc1_3062 Mmc1_3063
            ABA: Acid345_0484 Acid345_2275 Acid345_4166
            BSU: BG10866(nifS) BG12632(nifZ) BG13809(yrvO) BG14009(csd)
            BHA: BH1217(nifS) BH1260 BH3204(nifZ) BH3469
            BAN: BA4626 BA4663 BA4900
            BAR: GBAA4626 GBAA4900
            BAA: BA_5066 BA_5102 BA_5320
            BAT: BAS4292 BAS4328 BAS4546
            BCE: BC4392 BC4424 BC4648
            BCA: BCE_4480 BCE_4516 BCE_4785
            BCZ: BCZK0830(nifS) BCZK4140 BCZK4176(nifS) BCZK4392
            BTK: BT9727_4129 BT9727_4165(nifS) BT9727_4382
            BTL: BALH_4513
            BLI: BL00432(nifZ) BL01136(nifS) BL02040(yrvO)
            BLD: BLi02876(yrvO) BLi02915(nifS) BLi03101(nifZ)
            BCL: ABC1585
            BAY: RBAM_029770(csd)
            BPU: BPUM_2392(yrvO) BPUM_2925(csd)
            OIH: OB2015 OB2199
            GKA: GK2564 GK2796 GK2993
            SAU: SA0776 SA1450 SA1538
            SAV: SAV0844 SAV1622 SAV1716(nifZ)
            SAM: MW0797 MW1572 MW1659
            SAR: SAR0878(csdB) SAR1702 SAR1794
            SAS: SAS0786 SAS1558 SAS1643
            SAC: SACOL0916 SACOL1677 SACOL1765
            SAB: SAB1493c SAB1575c
            SAA: SAUSA300_0820(sufS) SAUSA300_1579 SAUSA300_1662
            SAO: SAOUHSC_00849 SAOUHSC_01727 SAOUHSC_01825
            SEP: SE0608 SE1305 SE1392
            SER: SERP0498(sufS) SERP1186 SERP1280
            SHA: SH1209 SH1297 SH2037
            SSP: SSP1047 SSP1139 SSP1859
            LMO: lmo1513 lmo1593 lmo2022
            LMF: LMOf2365_1532 LMOf2365_1615 LMOf2365_2047
            LIN: lin1548 lin1635 lin2130
            LWE: lwe1526
            LLA: L111126(nifS) L122222(nifZ)
            LLC: LACR_0534
            LLM: llmg_0505(nifZ) llmg_2048(nifS)
            SPY: SPy_0816 SPy_1122
            SPZ: M5005_Spy_0630(nifS1) M5005_Spy_0844(nifS2)
            SPM: spyM18_0878(nifS) spyM18_1083(nifS)
            SPG: SpyM3_0549(nifS) SpyM3_0781
            SPS: SPs0982 SPs1305
            SPH: MGAS10270_Spy0244(nifS3) MGAS10270_Spy0686(nifS1)
                 MGAS10270_Spy0960(nifS2)
            SPI: MGAS10750_Spy0241(nifS3) MGAS10750_Spy0718(nifS1)
                 MGAS10750_Spy0995(nifS2)
            SPJ: MGAS2096_Spy0263(nifS3) MGAS2096_Spy0695(nifS1)
                 MGAS2096_Spy0919(nifS2)
            SPK: MGAS9429_Spy0246(nifS3) MGAS9429_Spy0685(nifS1)
                 MGAS9429_Spy0963(nifS2)
            SPA: M6_Spy0647 M6_Spy0842
            SPN: SP_0880 SP_1094
            SPR: spr0783 spr1001(nifS)
            SAG: SAG1098(iscS-1) SAG1373(iscS-2)
            SAN: gbs1165 gbs1443
            SAK: SAK_1183 SAK_1406
            SMU: SMU.1051 SMU.841
            STC: str0411(nifS2) str1461(nifS3)
            STL: stu0411(nifS2) stu1461(nifS3)
            SSA: SSA_1057 SSA_1213
            LPL: lp_2180(csd2) lp_2326(csd3)
            LJO: LJ0953 LJ0984
            LAC: LBA0789(nifS) LBA1177
            LSA: LSA0791 LSA0846 LSA1111
            LSL: LSL_0860(nifS) LSL_1074(nifS)
            LBR: LVIS_1256 LVIS_1436
            LCA: LSEI_1289
            EFA: EF0371 EF2072
            STH: STH2390 STH641
            CAC: CAC2234(nifS) CAC2972(nifS)
            CPE: CPE1413(nifS) CPE1785(nifS)
            CPF: CPF_1667 CPF_2039(iscS)
            CPR: CPR_1403 CPR_1755(iscS)
            CTC: CTC01050 CTC01459
            CNO: NT01CX_2283
            CDF: CD0753(iscS1) CD1279(iscS2)
            CBO: CBO1182(iscS) CBO2568(iscS)
            CBA: CLB_1213(iscS-1) CLB_2509(iscS-2)
            CBH: CLC_1225(iscS-1) CLC_2440(iscS-2)
            CBF: CLI_1264(iscS-1) CLI_2631(iscS-2)
            CBE: Cbei_0585
            CKL: CKL_0816(iscS) CKL_0831(sufS) CKL_1087(nifS1) CKL_1318(nifS2)
            AMT: Amet_1345
            CHY: CHY_2199(iscS)
            DSY: DSY2426
            SWO: Swol_2429
            TTE: TTE1663(nifS) TTE2465(nifS2)
            MTA: Moth_0199 Moth_1652
            MGE: MG_336
            MPN: MPN487(nifS)
            UUR: UU454(nifS)
            MTU: Rv3025c(iscS)
            MTC: MT3109
            MBO: Mb3051c(iscS)
            MLE: ML0596 ML1708
            MPA: MAP3058c
            MAV: MAV_3315 MAV_3872
            MSM: MSMEG_1242(iscS) MSMEG_2357 MSMEG_3125
            MMC: Mmcs_1875
            CGL: NCgl1022(cgl1067) NCgl1184(cgl1232)
            CGB: cg1214 cg1388(nifS1)
            CEF: CE1114 CE1330
            CDI: DIP1072
            CJK: jk1321(iscS)
            NFA: nfa42680
            RHA: RHA1_ro04117 RHA1_ro05699 RHA1_ro06466
            SCO: SCO5486(SC2A11.20)
            SMA: SAV2756 SAV2933(iscS)
            TWH: TWT416
            TWS: TW352
            LXX: Lxx14420(nifS) Lxx16520(iscS)
            ART: Arth_2656
            PAC: PPA1116
            NCA: Noca_3142 Noca_3438
            TFU: Tfu_0595
            FRA: Francci3_3650 Francci3_4475
            FAL: FRAAL5862(iscS)
            ACE: Acel_0688
            SEN: SACE_0202 SACE_1797(csd) SACE_2615(iscS) SACE_5825 SACE_6188
            STP: Strop_1769
            BLO: BL1377
            RXY: Rxyl_0109 Rxyl_2890
            FNU: FN0058
            RBA: RB11582 RB9210(nifS)
            CTR: CT258(yhfO) CT687(yfhO_1) CT721(yfhO_2)
            CTA: CTA_0280(yfhO_1) CTA_0748(yfhO_2) CTA_0783(yfhO_3)
            CMU: TC0059 TC0094 TC0529
            CPN: CPn0396(yhfO) CPn0689(yfhO_1) CPn0862(yfhO_2)
            CPA: CP0057 CP0359 CP1007
            CPJ: CPj0396(yhfO) CPj0689(yfhO_1)
            CPT: CpB0408(nifS) CpB0716 CpB0891(nifS)
            CCA: CCA00053 CCA00400 CCA00905
            CAB: CAB054 CAB387 CAB873
            CFE: CF0109(nifS1) CF0607(nifS2) CF0951(csdB)
            PCU: pc0162(nifS) pc0721(nifS)
            BBU: BB0084(nifS)
            BGA: BG0082(nifS)
            BAF: BAPKO_0084(nifS)
            TPA: TP0614 TP0863
            LBJ: LBJ_1384
            LBL: LBL_1610
            SYN: sll0704(nifS2) slr0387(nifS1)
            SYW: SYNW1253(nifS) SYNW2291
            SYC: syc1552_c(nifS)
            SYF: Synpcc7942_1929 Synpcc7942_2558
            SYD: Syncc9605_1370 Syncc9605_2429
            SYE: Syncc9902_1108 Syncc9902_2109
            SYG: sync_1367(nifS) sync_2644(spl1)
            SYR: SynRCC307_1191(nifS) SynRCC307_2259(nifS)
            SYX: SynWH7803_1263(nifS) SynWH7803_2311
            CYA: CYA_1826(nifS) CYA_2891
            CYB: CYB_0419(nifS) CYB_1648
            TEL: tll0913(nifS) tlr0115(nifS)
            GVI: gll4384
            ANA: all1457(nifS) alr2505 alr3088(nifS)
            AVA: Ava_0427 Ava_0437 Ava_1826 Ava_3914 Ava_4245 Ava_4856
                 Ava_4866 Ava_B0304
            PMA: Pro0195(nifS) Pro0949(nifS)
            PMM: PMM0170 PMM0887(nifS)
            PMT: PMT0717(nifS) PMT2045
            PMN: PMN2A_0323 PMN2A_1538
            PMI: PMT9312_0172 PMT9312_0913
            PMB: A9601_00821 A9601_01881 A9601_09741
            PMC: P9515_00791 P9515_01991 P9515_09691
            PMF: P9303_03051 P9303_27201
            PMG: P9301_00811 P9301_01901 P9301_09721
            PMH: P9215_00821(csdB) P9215_01881
            PME: NATL1_01341 NATL1_02451 NATL1_09961
            TER: Tery_0201 Tery_1872 Tery_4044 Tery_4134
            SRU: SRU_1858
            CHU: CHU_3381(iscS) CHU_3485(iscS)
            GFO: GFO_0447(iscS) GFO_1879(iscS) GFO_3130(sufS)
            FPS: FP0708 FP2389(sufS)
            CTE: CT1995(iscS)
            CCH: Cag_0206
            PLT: Plut_0235
            DET: DET0248
            DEH: cbdb_A257
            RRS: RoseRS_3113
            RCA: Rcas_2971
            DRA: DR_0215
            DGE: Dgeo_1952
            TTH: TTC0087
            TTJ: TTHA0456
            AAE: aq_1053(nifS1) aq_739(nifS2)
            TMA: TM1371 TM1692
            TPT: Tpet_0988 Tpet_1412
            TME: Tmel_0048
            MAC: MA2718 MA3264
            MBA: Mbar_A2424 Mbar_A3201
            MMA: MM_0109
            MHU: Mhun_2213
            MTH: MTH1389
            MST: Msp_1002(iscS)
            AFU: AF0186(nifS-1) AF0564(nifS-2)
            HAL: VNG2471G(nifS)
            HWA: HQ1862A(nifS) HQ3427A(nifS)
            NPH: NP0790A(nifS_2) NP0936A(nifS)
            PAB: PAB0157
            TKO: TK1990
            RCI: RCIX2151(nifS)
            APE: APE_2023
STRUCTURES  PDB: 1T3I  
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.1.7
            ExPASy - ENZYME nomenclature database: 2.8.1.7
            ExplorEnz - The Enzyme Database: 2.8.1.7
            ERGO genome analysis and discovery system: 2.8.1.7
            BRENDA, the Enzyme Database: 2.8.1.7
///
ENTRY       EC 2.8.1.8                  Enzyme
NAME        lipoyl synthase;
            LS;
            LipA;
            lipoate synthase;
            protein 6-N-(octanoyl)lysine:sulfur sulfurtransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfurtransferases
SYSNAME     protein N6-(octanoyl)lysine:sulfur sulfurtransferase
REACTION    protein N6-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine =
            protein N6-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosine
            [RN:R07767]
ALL_REAC    R07767;
            (other) R07768
SUBSTRATE   protein N6-(octanoyl)lysine [CPD:C16236];
            sulfur [CPD:C00087];
            S-adenosyl-L-methionine [CPD:C00019]
PRODUCT     protein N6-(lipoyl)lysine [CPD:C16237];
            L-methionine [CPD:C00073];
            5'-deoxyadenosine [CPD:C05198]
COMMENT     This enzyme is a member of the 'AdoMet radical' (radical SAM)
            family, all members of which produce the 5'-deoxyadenosin-5'-yl
            radical and methionine from AdoMet [i.e. S-adenosylmethionine, or
            S-(5'-deoxyadenosin-5'-yl)methionine], by the addition of an
            electron from an iron-sulfur centre. The radical is converted into
            5'-deoxyadenosine when it abstracts a hydrogen atom from C-6 and
            C-8, leaving reactive radicals at these positions so that they can
            add sulfur, with inversion of configuration [4]. This enzyme
            catalyses the final step in the de-novo biosynthesis of the lipoyl
            cofactor, with the other enzyme involved being EC 2.3.1.181,
            lipoyl(octanoyl) transferase. Lipoylation is essential for the
            function of several key enzymes involved in oxidative metabolism, as
            it converts apoprotein into the biologically active holoprotein.
            Examples of such lipoylated proteins include pyruvate dehydrogenase
            (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the
            branched-chain 2-oxoacid dehydrogenases and the glycine cleavage
            system (H protein) [2,5]. An alternative lipoylation pathway
            involves EC 2.7.7.63, lipoate---protein ligase, which can lipoylate
            apoproteins using exogenous lipoic acid (or its analogues) [7].
REFERENCE   1  [PMID:15740115]
  AUTHORS   Cicchillo RM, Booker SJ.
  TITLE     Mechanistic investigations of lipoic acid biosynthesis in
            Escherichia coli: both sulfur atoms in lipoic acid are contributed
            by the same lipoyl synthase polypeptide.
  JOURNAL   J. Am. Chem. Soc. 127 (2005) 2860-1.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:1655709]
  AUTHORS   Vanden Boom TJ, Reed KE, Cronan JE Jr.
  TITLE     Lipoic acid metabolism in Escherichia coli: isolation of null
            mutants defective in lipoic acid biosynthesis, molecular cloning and
            characterization of the E. coli lip locus, and identification of the
            lipoylated protein of the glycine cleavage system.
  JOURNAL   J. Bacteriol. 173 (1991) 6411-20.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:14700636]
  AUTHORS   Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE.
  TITLE     Assembly of the covalent linkage between lipoic acid and its cognate
            enzymes.
  JOURNAL   Chem. Biol. 10 (2003) 1293-302.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:15157071]
  AUTHORS   Cicchillo RM, Iwig DF, Jones AD, Nesbitt NM, Baleanu-Gogonea C,
            Souder MG, Tu L, Booker SJ.
  TITLE     Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine
            to synthesize one equivalent of lipoic acid.
  JOURNAL   Biochemistry. 43 (2004) 6378-86.
  ORGANISM  Escherichia coli [GN:eco], human [GN:hsa], Arabidopsis thaliana
            [GN:ath], Saccharomyces cerevisiae [GN:sce]
REFERENCE   5  [PMID:9218413]
  AUTHORS   Jordan SW, Cronan JE Jr.
  TITLE     A new metabolic link. The acyl carrier protein of lipid synthesis
            donates lipoic acid to the pyruvate dehydrogenase complex in
            Escherichia coli and mitochondria.
  JOURNAL   J. Biol. Chem. 272 (1997) 17903-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:11106496]
  AUTHORS   Miller JR, Busby RW, Jordan SW, Cheek J, Henshaw TF, Ashley GW,
            Broderick JB, Cronan JE Jr, Marletta MA.
  TITLE     Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of
            lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier
            protein.
  JOURNAL   Biochemistry. 39 (2000) 15166-78.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   7  [PMID:10966480]
  AUTHORS   Perham RN.
  TITLE     Swinging arms and swinging domains in multifunctional enzymes:
            catalytic machines for multistep reactions.
  JOURNAL   Annu. Rev. Biochem. 69 (2000) 961-1004.
PATHWAY     PATH: map00785  Lipoic acid metabolism
ORTHOLOGY   KO: K03644  lipoic acid synthetase
GENES       HSA: 11019(LIAS)
            PTR: 471170(LIAS)
            MMU: 79464(Lias)
            RNO: 305348(Lias)
            CFA: 479108(LIAS)
            BTA: 530865(LIAS)
            GGA: 422791(LIAS)
            XLA: 443960(MGC80349)
            XTR: 496674(lias)
            DRE: 393528(zgc:66080) 572803(LOC572803)
            DME: Dmel_CG5231(Las)
            CEL: M01F1.3
            ATH: AT2G20860(LIP1) AT5G08415
            OSA: 4325595 4336023 4339289
            CME: CML179C CMQ441C
            SCE: YOR196C(LIP5)
            AGO: AGOS_AGR231C
            PIC: PICST_86231(LIP12)
            CAL: CaO19_10290(CaO19.10290)
            CGR: CAGL0I10923g
            SPO: SPBC8D2.15
            ANI: AN9486.2
            AFM: AFUA_3G06560
            AOR: AO090020000344
            CNE: CNL04340
            PFA: MAL13P1.220
            TBR: Tb10.61.1530
            TCR: 506211.10 511291.30
            LMA: LmjF19.0350
            ECO: b0628(lipA)
            ECJ: JW0623(lipA)
            ECE: Z0773(lipA)
            ECS: ECs0666
            ECC: c0718(lipA)
            ECI: UTI89_C0631(lipA)
            ECP: ECP_0658
            ECV: APECO1_1427(lipA)
            STY: STY0683(lipA)
            STT: t2234(lipA)
            SPT: SPA2101(lipA)
            SEC: SC0662(lipA)
            STM: STM0633(lipA)
            YPE: YPO2598(lipA)
            YPK: y1171(lipA)
            YPM: YP_1115(lipA)
            YPA: YPA_2501
            YPN: YPN_1083
            YPP: YPDSF_2655
            YPS: YPTB1091(lipA)
            YEN: YE3008(lip)
            SFL: SF0653(lipA)
            SFX: S0675(lipA)
            SFV: SFV_0698(lipA)
            SSN: SSON_0582(lipA)
            SBO: SBO_0492(lipA)
            SDY: SDY_0550(lipA)
            ECA: ECA1297(lipA)
            PLU: plu1291(lipA)
            BUC: BU269(lipA)
            BAS: BUsg259(lipA)
            BAB: bbp250(lipA)
            BCC: BCc_170(lipA)
            WBR: WGLp176(lipA)
            SGL: SG0792
            HIN: HI0026(lipA)
            HIT: NTHI0033(lipA)
            HDU: HD2012(lipA)
            HSO: HS_0315(lipA)
            PMU: PM1930(lipA)
            MSU: MS1826(lipA)
            APL: APL_1593(lipA)
            XFA: XF1269
            XFT: PD0530(lipA)
            XCC: XCC3451(lipA)
            XCB: XC_0713
            XCV: XCV0729(lipA)
            XAC: XAC0668(lipA)
            XOO: XOO3952(lipA)
            XOM: XOO_3730(XOO3730)
            VCH: VC0943
            VVU: VV1_0284
            VVY: VV0900
            VPA: VP0716
            VFI: VF0742
            PPR: PBPRA2896
            PAE: PA3996(lipA)
            PAU: PA14_12130(lis)
            PPU: PP_4800(lipA)
            PST: PSPTO_4818(lipA)
            PSB: Psyr_4358
            PSP: PSPPH_4399(lipA)
            PFL: PFL_5445(lipA)
            PFO: Pfl_4963
            PEN: PSEEN4819(lipA)
            PMY: Pmen_3791
            PAR: Psyc_0749(lipA)
            PCR: Pcryo_0744
            ACI: ACIAD1015(lipA) ACIAD2275(lipA)
            ACB: A1S_2329
            SON: SO_1161(lipA)
            SDN: Sden_0867
            SFR: Sfri_0692
            SAZ: Sama_2595
            SBL: Sbal_3282
            SLO: Shew_2942
            SHE: Shewmr4_0984
            SHM: Shewmr7_1049
            SHN: Shewana3_0988
            SHW: Sputw3181_1027
            ILO: IL0960(lipA)
            CPS: CPS_1709(lipA)
            PHA: PSHAa1019(lipA)
            PAT: Patl_1553
            SDE: Sde_3334
            PIN: Ping_3030
            MAQ: Maqu_2373
            CBU: CBU_1266(lipA)
            LPN: lpg0745
            LPF: lpl0781(lipA)
            LPP: lpp0810(lipA)
            MCA: MCA0110(lipA)
            FTU: FTT0653(lipA)
            FTF: FTF0653(lipA)
            FTW: FTW_1075(lipA)
            FTL: FTL_0927
            FTH: FTH_0906(lipA)
            FTN: FTN_1030(lipA)
            TCX: Tcr_1639
            NOC: Noc_2629
            AEH: Mlg_1586
            HHA: Hhal_0116
            HCH: HCH_05836(lipA)
            CSA: Csal_1552
            ABO: ABO_1964(lipA)
            AHA: AHA_3263(lipA)
            BCI: BCI_0238(lipA)
            RMA: Rmag_0543
            NME: NMB1216
            NMA: NMA1378(lipA)
            NMC: NMC1110(lipA)
            NGO: NGO0793
            CVI: CV_3097(lipA)
            RSO: RSc0322(lipA)
            REU: Reut_A0086
            REH: H16_A0123(lipA)
            RME: Rmet_0061
            BMA: BMA0052(lipA)
            BMV: BMASAVP1_A0218(lipA-2)
            BML: BMA10299_A1375(lipA)
            BMN: BMA10247_3186(lipA-2)
            BXE: Bxe_A4212 Bxe_B0316
            BUR: Bcep18194_A5137 Bcep18194_A6230
            BCN: Bcen_2272 Bcen_6243
            BCH: Bcen2424_1836 Bcen2424_2887
            BAM: Bamb_1774 Bamb_2937
            BPS: BPSL0414(lipA)
            BPM: BURPS1710b_0628(lipA)
            BPL: BURPS1106A_0464(lipA)
            BPD: BURPS668_0444(lipA)
            BTE: BTH_I0386(lipA) BTH_I2210
            PNU: Pnuc_1961
            BPE: BP0106(lipA)
            BPA: BPP0170(lipA)
            BBR: BB0172(lipA)
            RFR: Rfer_3934
            POL: Bpro_0313
            PNA: Pnap_0242
            AAV: Aave_0362
            AJS: Ajs_0298
            VEI: Veis_0470
            MPT: Mpe_A0316
            HAR: HEAR3003(lipA)
            NEU: NE1489(lipA)
            NET: Neut_0757
            NMU: Nmul_A1987
            EBA: ebA3050(lipA)
            AZO: azo0184(lipA)
            DAR: Daro_0287
            TBD: Tbd_0274
            MFA: Mfla_2501
            GSU: GSU0380(lipA)
            GME: Gmet_3150
            PCA: Pcar_0346
            PPD: Ppro_1029 Ppro_2239
            DVU: DVU0905(lipA)
            DVL: Dvul_2079
            DDE: Dde_2714
            DPS: DP0296(lipA)
            ADE: Adeh_1828
            MXA: MXAN_4218(lipA)
            SFU: Sfum_2644
            RPR: RP742(lipA)
            RTY: RT0727(lipA)
            RCO: RC1145(lipA)
            RFE: RF_1187(lipA)
            RBE: RBE_1309(lipA)
            WOL: WD0392(lipA)
            WBM: Wbm0303
            AMA: AM820(lipA)
            APH: APH_0367(lipA)
            ERU: Erum5290(lipA)
            ERW: ERWE_CDS_05550(lipA)
            ERG: ERGA_CDS_05440(lipA)
            ECN: Ecaj_0537
            ECH: ECH_0490(lipA)
            NSE: NSE_0322(lipA)
            PUB: SAR11_0941(lipA)
            MLO: mlr0392
            MES: Meso_1624
            SME: SMc01037(lipA)
            ATU: Atu1436(lipA)
            ATC: AGR_C_2646
            RET: RHE_CH01941(lipA)
            RLE: RL2249
            BME: BMEI0859
            BMF: BAB1_1147(lipA)
            BMS: BR1124(lipA)
            BMB: BruAb1_1130(lipA)
            BJA: bll3717(lipA) blr4477(lipA)
            BRA: BRADO3879(lipA)
            RPA: RPA2587(lipA2)
            RPB: RPB_2888
            RPC: RPC_2572
            RPD: RPD_2584
            RPE: RPE_2752
            NWI: Nwi_1439
            NHA: Nham_1831
            BHE: BH05790(lipA)
            BQU: BQ04950(lipA)
            BBK: BARBAKC583_0538(lipA)
            CCR: CC_1735
            SIL: SPO2102(lipA)
            SIT: TM1040_1371
            RSP: RSP_2783(lipA)
            RSH: Rsph17029_1425
            JAN: Jann_2226
            RDE: RD1_2773(lipA)
            PDE: Pden_1376
            MMR: Mmar10_1436
            HNE: HNE_2021(lipA)
            ZMO: ZMO1132(lipA)
            NAR: Saro_1921
            SAL: Sala_1281
            ELI: ELI_06310
            GOX: GOX2293
            GBE: GbCGDNIH1_1188
            RRU: Rru_A1877
            MAG: amb2322
            MGM: Mmc1_0527
            ABA: Acid345_4487
            SUS: Acid_1501 Acid_4705
            BSU: BG14038(lipA)
            BHA: BH3435
            BAN: BA5205(lipA)
            BAR: GBAA5205(lipA)
            BAA: BA_0078
            BAT: BAS4840
            BCE: BC4973
            BCA: BCE_5109(lipA)
            BCZ: BCZK4698(lipA)
            BTK: BT9727_4682(lipA)
            BTL: BALH_4504(lipA)
            BLI: BL02143(lipA)
            BLD: BLi03422(lipA)
            BCL: ABC2950(lipS)
            BPU: BPUM_2896(lipA)
            OIH: OB1284
            GKA: GK2974
            GTN: GTNG_2924
            SAU: SA0785(lipA)
            SAV: SAV0924(lipA)
            SAM: MW0807(lipA)
            SAR: SAR0887(lipA)
            SAS: SAS0795
            SAC: SACOL0927(lipA)
            SAB: SAB0791
            SAA: SAUSA300_0829(lipA)
            SAO: SAOUHSC_00861
            SEP: SE0617
            SER: SERP0511(lipA)
            SHA: SH2028(lipA)
            SSP: SSP1850
            STH: STH2153
            TTE: TTE1672(lipA2)
            MTA: Moth_1762
            MTU: Rv2218(lipA)
            MTC: MT2275(lipA)
            MBO: Mb2241(lipA)
            MBB: BCG_2234(lipA)
            MLE: ML0858(lipA)
            MPA: MAP1959(lipA)
            MAV: MAV_2270(lipA)
            MSM: MSMEG_4286(lipA)
            MUL: MUL_1343(lipA)
            MVA: Mvan_0914 Mvan_3582
            MMC: Mmcs_3316
            MKM: Mkms_3378
            MJL: Mjls_3327
            CGL: NCgl2128(cgl2209)
            CGB: cg2423(lipA)
            CEF: CE2100
            CDI: DIP1641(lipA)
            CJK: jk0705(lipA)
            NFA: nfa16860(lipA)
            RHA: RHA1_ro01154 RHA1_ro02928
            SCO: SCO2194(lipA)
            SMA: SAV6009(lipA)
            TWH: TWT464(lipA)
            TWS: TW301(lipA)
            LXX: Lxx10130(lipA)
            ART: Arth_0062 Arth_1604
            AAU: AAur_1747(lipA)
            PAC: PPA0689
            TFU: Tfu_0991
            FRA: Francci3_3138
            FAL: FRAAL5157(lipA)
            ACE: Acel_0926
            SEN: SACE_1626(lipA)
            STP: Strop_3328
            RXY: Rxyl_2548
            RBA: RB4868
            CTR: CT558(lipA)
            CTA: CTA_0608(lipA)
            CMU: TC0847
            CPN: CPn0832(lipA)
            CPA: CP1038
            CPJ: CPj0832(lipA)
            CPT: CpB0861
            CCA: CCA00934(lipA)
            CAB: CAB903(lipA3)
            CFE: CF0080(lipA)
            PCU: pc0152(lipA)
            TDE: TDE1575(lipA)
            LIL: LA2292
            LIC: LIC11646(lipA)
            LBJ: LBJ_1322(lipA)
            LBL: LBL_1547(lipA)
            SYN: sll0868(lipA) slr1598(lipA)
            SYW: SYNW0929(lipA) SYNW2130(lipA)
            SYC: syc0979_c(lipA) syc2492_c(lipA)
            SYF: Synpcc7942_0542 Synpcc7942_1507
            SYD: Syncc9605_0328 Syncc9605_1638
            SYE: Syncc9902_1398 Syncc9902_2014
            SYG: sync_0389(lipA-1) sync_1037(lipA-2)
            CYA: CYA_0692(lipA) CYA_0714(lipA) CYA_2347(lipA)
            CYB: CYB_1117(lipA) CYB_2905(lipA)
            TEL: tll0574 tlr0613
            GVI: gll1029 gll3526
            ANA: all1694 alr1282
            AVA: Ava_1162 Ava_3006
            PMA: Pro1099(lipA) Pro1670(lipA)
            PMM: PMM1096(lipA) PMM1514(lipA)
            PMT: PMT1076(lipA) PMT1775(lipA)
            PMN: PMN2A_0652 PMN2A_1080
            PMI: PMT9312_1107 PMT9312_1606
            PMB: A9601_12021 A9601_17181
            PMC: P9515_11871 P9515_16941
            PMF: P9303_09741 P9303_23551
            PMG: P9301_12031 P9301_17061
            PME: NATL1_14841 NATL1_19551
            TER: Tery_1957 Tery_3493
            BTH: BT_4192
            BFR: BF0976
            BFS: BF0898
            PGI: PG0504(lipA)
            SRU: SRU_0796(lipA)
            CHU: CHU_3189(lipA)
            GFO: GFO_2703(lipA)
            FJO: Fjoh_0227
            CTE: CT1078(lipA)
            CCH: Cag_1068
            CPH: Cpha266_1277
            PLT: Plut_1084
            DRA: DR_0765
            DGE: Dgeo_1742
            TTH: TTC1747
            TTJ: TTHA0239
            AAE: aq_1355(lipA)
            HAL: VNG2216G(lip)
            HMA: rrnAC2959(lipA)
            NPH: NP0562A(lipA)
            PTO: PTO0550
            APE: APE_2344.1
            SSO: SSO3158(lipA)
            SAI: Saci_0309(lipA)
            PAI: PAE2643
            PCL: Pcal_1406
            PAS: Pars_1184
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.1.8
            ExPASy - ENZYME nomenclature database: 2.8.1.8
            ExplorEnz - The Enzyme Database: 2.8.1.8
            ERGO genome analysis and discovery system: 2.8.1.8
            BRENDA, the Enzyme Database: 2.8.1.8
///
ENTRY       EC 2.8.2.1                  Enzyme
NAME        aryl sulfotransferase;
            phenol sulfotransferase;
            sulfokinase;
            1-naphthol phenol sulfotransferase;
            2-naphtholsulfotransferase;
            4-nitrocatechol sulfokinase;
            arylsulfotransferase;
            dopamine sulfotransferase;
            p-nitrophenol sulfotransferase;
            phenol sulfokinase;
            ritodrine sulfotransferase;
            PST
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:phenol sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate
            + an aryl sulfate
ALL_REAC    (other) R01242
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            phenol [CPD:C00146]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            aryl sulfate [CPD:C00850]
COMMENT     A number of aromatic compounds can act as acceptors. Organic
            hydroxylamines are not substrates (cf. EC 2.8.2.9 tyrosine-ester
            sulfotransferase).
REFERENCE   1  [PMID:6956338]
  AUTHORS   Romain Y, Demassieux S, Carriere S.
  TITLE     Partial purification and characterization of two isoenzymes involved
            in the sulfurylation of catecholamines.
  JOURNAL   Biochem. Biophys. Res. Commun. 106 (1982) 999-1005.
  ORGANISM  dog [GN:cfa]
REFERENCE   2  [PMID:447677]
  AUTHORS   Sekura RD, Jakoby WB.
  TITLE     Phenol sulfotransferases.
  JOURNAL   J. Biol. Chem. 254 (1979) 5658-63.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K01014  aryl sulfotransferase
GENES       HSA: 445329(SULT1A4) 6799(SULT1A2) 6817(SULT1A1) 6818(SULT1A3)
            MMU: 20887(Sult1a1)
            RNO: 83783(Sult1a1)
            CFA: 403892(SULT1A1)
            BTA: 282485(SULT1A1)
            SSC: 396640(SULT1A1)
            XCC: XCC2911
            XCB: XC_1198
            XCV: XCV0854
            XAC: XAC0802
            XOO: XOO3800
            XOM: XOO_3581(XOO3581)
            NOC: Noc_0082
            SAL: Sala_2372
            RRU: Rru_A1463
STRUCTURES  PDB: 1LS6  1Z28  1Z29  2A3R  2D06  
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.1
            ExPASy - ENZYME nomenclature database: 2.8.2.1
            ExplorEnz - The Enzyme Database: 2.8.2.1
            ERGO genome analysis and discovery system: 2.8.2.1
            BRENDA, the Enzyme Database: 2.8.2.1
            CAS: 9026-09-9
///
ENTRY       EC 2.8.2.2                  Enzyme
NAME        alcohol sulfotransferase;
            hydroxysteroid sulfotransferase;
            3beta-hydroxy steroid sulfotransferase;
            Delta5-3beta-hydroxysteroid sulfokinase;
            3beta-hydroxy steroid sulfotransferase;
            3-hydroxysteroid sulfotransferase;
            HST;
            5alpha-androstenol sulfotransferase;
            cholesterol sulfotransferase;
            dehydroepiandrosterone sulfotransferase;
            estrogen sulfokinase;
            estrogen sulfotransferase;
            steroid alcohol sulfotransferase;
            steroid sulfokinase;
            steroid sulfotransferase;
            sterol sulfokinase;
            sterol sulfotransferase;
            alcohol/hydroxysteroid sulfotransferase;
            3beta-hydroxysteroid sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:alcohol sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + an alcohol = adenosine
            3',5'-bisphosphate + an alkyl sulfate [RN:R00629]
ALL_REAC    R00629;
            (other) R03405
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            alcohol [CPD:C00069]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            alkyl sulfate [CPD:C02000]
COMMENT     Primary and secondary alcohols, including aliphatic alcohols,
            ascorbic acid, chloramphenicol, ephedrine and hydroxysteroids, but
            not phenolic steroids, can act as acceptors (cf. EC 2.8.2.15 steroid
            sulfotransferase).
REFERENCE   1  [PMID:6935986]
  AUTHORS   Lyon ES, Jakoby WB.
  TITLE     The identity of alcohol sulfotransferases with hydroxysteroid
            sulfotransferases.
  JOURNAL   Arch. Biochem. Biophys. 202 (1980) 474-81.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6173569]
  AUTHORS   Lyon ES, Marcus CJ, Wang JL, Jakoby WB.
  TITLE     Hydroxysteroid sulfotransferase.
  JOURNAL   Methods. Enzymol. 77 (1981) 206-13.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00150  Androgen and estrogen metabolism
            PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K01015  alcohol sulfotransferase
GENES       HSA: 6820(SULT2B1) 6822(SULT2A1)
            MMU: 20865(C730007P19Rik) 54200(Sult2b1)
            RNO: 24902(Smp2a) 24912(Sult2a1) 361510(Sult2a2_predicted)
            CFA: 484403(SULT2B1)
            GGA: 426825(LOC426825)
            SME: SMb21249
STRUCTURES  PDB: 1EFH  1J99  1OV4  
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.2
            ExPASy - ENZYME nomenclature database: 2.8.2.2
            ExplorEnz - The Enzyme Database: 2.8.2.2
            ERGO genome analysis and discovery system: 2.8.2.2
            BRENDA, the Enzyme Database: 2.8.2.2
            CAS: 9032-76-2
///
ENTRY       EC 2.8.2.3                  Enzyme
NAME        amine sulfotransferase;
            arylamine sulfotransferase;
            amine N-sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:amine N-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + an amine = adenosine 3',5'-bisphosphate
            + a sulfamate [RN:R02809]
ALL_REAC    R02809 > R01861
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            amine [CPD:C00706]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            sulfamate [CPD:C01614]
COMMENT     A large number of primary and secondary amines can act as acceptors,
            including aniline, 2-naphthylamine, cyclohexylamine and octylamine.
REFERENCE   1  [PMID:3475273]
  AUTHORS   Ramaswamy SG, Jakoby WB.
  TITLE     Amine N-sulfotransferase.
  JOURNAL   J. Biol. Chem. 262 (1987) 10039-43.
  ORGANISM  guinea pig
REFERENCE   2
  AUTHORS   Roy, A.B.
  TITLE     The enzymic synthesis of aryl sulphamates.
  JOURNAL   Biochem. J. 74 (1960) 49-56.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00920  Sulfur metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.3
            ExPASy - ENZYME nomenclature database: 2.8.2.3
            ExplorEnz - The Enzyme Database: 2.8.2.3
            ERGO genome analysis and discovery system: 2.8.2.3
            BRENDA, the Enzyme Database: 2.8.2.3
            CAS: 9026-08-8
///
ENTRY       EC 2.8.2.4                  Enzyme
NAME        estrone sulfotransferase;
            3'-phosphoadenylyl sulfate-estrone 3-sulfotransferase;
            estrogen sulfotransferase;
            estrogen sulphotransferase;
            oestrogen sulphotransferase;
            3'-phosphoadenylylsulfate:oestrone sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:estrone 3-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate
            + estrone 3-sulfate [RN:R02350]
ALL_REAC    R02350
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            estrone [CPD:C00468]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            estrone 3-sulfate [CPD:C02538]
REFERENCE   1  [PMID:4965224]
  AUTHORS   Adams JB, Poulos A.
  TITLE     Enzymic synthesis of steroid sulphates. 3. Isolation and properties
            of estrogen sulphotransferase of bovine adrenal glands.
  JOURNAL   Biochim. Biophys. Acta. 146 (1967) 493-508.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   Rozhin, J., Zemlicka, J. and Brooks, S.C.
  TITLE     Studies on bovine adrenal estrogen sulfotransferase. Inhibition and
            possible involvement of adenine-estrogen stacking.
  JOURNAL   J. Biol. Chem. 252 (1967) 7214-7220.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:4473218]
  AUTHORS   Adams JB, Ellyard RK, Low J.
  TITLE     Enzymic synthesis of steroid sulphates. IX. Physical and chemical
            properties of purified oestrogen sulphotransferase from bovine
            adrenal glands, the nature of its isoenzymic forms and a proposed
            model to explain its wave-like kinetics.
  JOURNAL   Biochim. Biophys. Acta. 370 (1974) 160-88.
PATHWAY     PATH: map00150  Androgen and estrogen metabolism
            PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K01016  estrone sulfotransferase
GENES       HSA: 6783(SULT1E1)
            MMU: 20860(Sult1e1)
            RNO: 25355(Ste)
            CFA: 482182(SULT1E1)
            BTA: 280934(STE)
            SSC: 397052(STE)
STRUCTURES  PDB: 1AQU  1AQY  1BO6  1G3M  1HY3  
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.4
            ExPASy - ENZYME nomenclature database: 2.8.2.4
            ExplorEnz - The Enzyme Database: 2.8.2.4
            ERGO genome analysis and discovery system: 2.8.2.4
            BRENDA, the Enzyme Database: 2.8.2.4
            CAS: 9026-06-6
///
ENTRY       EC 2.8.2.5                  Enzyme
NAME        chondroitin 4-sulfotransferase;
            chondroitin sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:chondroitin 4'-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + chondroitin = adenosine
            3',5'-bisphosphate + chondroitin 4'-sulfate [RN:R02180]
ALL_REAC    R02180
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            chondroitin [CPD:C00401]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            chondroitin 4'-sulfate [CPD:C00634]
COMMENT     The sulfation takes place at the 4-position of
            N-acetyl-galactosamine residues of chondroitin. Not identical with
            EC 2.8.2.17 chondroitin 6-sulfotransferase.
REFERENCE   1  [PMID:6957247]
  AUTHORS   Habuchi O, Miyashita N.
  TITLE     Separation and characterization of chondroitin 6-sulfotransferase
            and chondroitin 4-sulfotransferase from chick embryo cartilage.
  JOURNAL   Biochim. Biophys. Acta. 717 (1982) 414-21.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:6130977]
  AUTHORS   Nakanishi Y, Otsu K, Suzuki S.
  TITLE     Enzymatic transfer of galactosyl phosphate from UDP-galactose to
            UDP-N-acetylglucosamine.
  JOURNAL   FEBS. Lett. 151 (1983) 15-8.
  ORGANISM  chicken [GN:gga]
REFERENCE   3  [PMID:6787041]
  AUTHORS   Nakanishi Y, Shimizu M, Otsu K, Kato S, Tsuji M, Suzuki S.
  TITLE     A terminal 6-sulfotransferase catalyzing a synthesis of
            N-acetylgalactosamine 4,6-bissulfate residue at the nonreducing
            terminal position of chondroitin sulfate.
  JOURNAL   J. Biol. Chem. 256 (1981) 5443-9.
  ORGANISM  chicken [GN:gga]
REFERENCE   4
  AUTHORS   Suzuki, S. and Strominger, J.L.
  TITLE     Enzymatic sulfation of mucopolysaccharides in hen oviduct. I.
            Transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate to
            mucopolysaccharides.
  JOURNAL   J. Biol. Chem. 235 (1960) 257-266.
  ORGANISM  chicken [GN:gga]
REFERENCE   5
  AUTHORS   Suzuki, S. and Strominger, J.L.
  TITLE     Enzymatic sulfation of mucopolysaccharides in hen oviduct. II.
            Mechanism of the reaction studied with oligosaccharides and
            monosaccharides as acceptors.
  JOURNAL   J. Biol. Chem. 235 (1960) 267-273.
  ORGANISM  chicken [GN:gga]
REFERENCE   6
  AUTHORS   Suzuki, S. and Strominger, J.L.
  TITLE     Enzymatic sulfation of mucopolysaccharides in hen oviduct. III.
            Mechanism of sulfation of chondroitin and chondroitin sulfate A.
  JOURNAL   J. Biol. Chem. 235 (1960) 274-276.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00532  Chondroitin sulfate biosynthesis
            PATH: map00920  Sulfur metabolism
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K01017  chondroitin 4-sulfotransferase 11
            KO: K04742  chondroitin 4-sulfotransferase 12
            KO: K07779  chondroitin 4-sulfotransferase 13
GENES       HSA: 166012(CHST13) 50515(CHST11) 55501(CHST12)
            PTR: 467113(CHST11) 471065(CHST13) 472270(CHST12)
            MMU: 58250(Chst11) 59031(Chst12) 71797(Chst13)
            RNO: 304322(Chst12) 314694(Chst11_predicted)
                 500257(RGD1562825_predicted)
            CFA: 481299(CHST11) 484618(CHST13) 609635(CHST12)
            BTA: 513030(CHST12) 523460(MGC157264) 528860(LOC528860)
            GGA: 416032(LOC416032) 416469(CHST12) 418081(CHST11)
            XLA: 380581(chst11) 496355(LOC496355)
            XTR: 493458(MGC89155) 548703(chst12)
            DRE: 404232(chst11) 407076(zC4ST-2)
            SPU: 752230(LOC752230) 753496(LOC753496)
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.5
            ExPASy - ENZYME nomenclature database: 2.8.2.5
            ExplorEnz - The Enzyme Database: 2.8.2.5
            ERGO genome analysis and discovery system: 2.8.2.5
            BRENDA, the Enzyme Database: 2.8.2.5
            CAS: 83589-04-2
///
ENTRY       EC 2.8.2.6                  Enzyme
NAME        choline sulfotransferase;
            choline sulphokinase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:choline sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + choline = adenosine 3',5'-bisphosphate
            + choline sulfate [RN:R01027]
ALL_REAC    R01027
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            choline [CPD:C00114]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            choline sulfate [CPD:C00919]
REFERENCE   1
  AUTHORS   Orsi, B.A. and Spencer, B.
  TITLE     Choline sulphokinase (sulphotransferase).
  JOURNAL   J. Biochem. (Tokyo) 56 (1964) 81-91.
  ORGANISM  Aspergillus nidulans [GN:ani]
PATHWAY     PATH: map00920  Sulfur metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.6
            ExPASy - ENZYME nomenclature database: 2.8.2.6
            ExplorEnz - The Enzyme Database: 2.8.2.6
            ERGO genome analysis and discovery system: 2.8.2.6
            BRENDA, the Enzyme Database: 2.8.2.6
            CAS: 9047-23-8
///
ENTRY       EC 2.8.2.7                  Enzyme
NAME        UDP-N-acetylgalactosamine-4-sulfate sulfotransferase;
            uridine diphosphoacetylgalactosamine 4-sulfate sulfotransferase;
            uridine diphospho-N-acetylgalactosamine 4-sulfate sulfotransferase;
            uridine diphosphoacetylgalactosamine 4-sulfate sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:UDP-N-acetyl-D-galactosamine-4-sulfate
            6-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + UDP-N-acetyl-D-galactosamine 4-sulfate
            = adenosine 3',5'-bisphosphate + UDP-N-acetyl-D-galactosamine
            4,6-bissulfate [RN:R04476]
ALL_REAC    R04476
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            UDP-N-acetyl-D-galactosamine 4-sulfate [CPD:C04426]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            UDP-N-acetyl-D-galactosamine 4,6-bissulfate [CPD:C04589]
REFERENCE   1  [PMID:6022874]
  AUTHORS   Harada T, Shimizu S, Nakanishi Y, Suzuki S.
  TITLE     Enzymatic transfer of sulfate from 3'-phosphoadenosine
            5'-phosphosulfate to uridine diphosphate N-acetylgalactosamine
            4-sulfate.
  JOURNAL   J. Biol. Chem. 242 (1967) 2288-90.
  ORGANISM  chicken [GN:gga]
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.7
            ExPASy - ENZYME nomenclature database: 2.8.2.7
            ExplorEnz - The Enzyme Database: 2.8.2.7
            ERGO genome analysis and discovery system: 2.8.2.7
            BRENDA, the Enzyme Database: 2.8.2.7
            CAS: 37278-32-3
///
ENTRY       EC 2.8.2.8                  Enzyme
NAME        [heparan sulfate]-glucosamine N-sulfotransferase;
            heparin N-sulfotransferase;
            3'-phosphoadenylylsulfate:N-desulfoheparin sulfotransferase;
            PAPS:N-desulfoheparin sulfotransferase;
            PAPS:DSH sulfotransferase;
            N-HSST;
            N-heparan sulfate sulfotransferase;
            heparan sulfate N-deacetylase/N-sulfotransferase;
            heparan sulfate 2-N-sulfotransferase;
            heparan sulfate N-sulfotransferase;
            heparan sulfate sulfotransferase;
            N-desulfoheparin sulfotransferase;
            desulfoheparin sulfotransferase;
            3'-phosphoadenylyl-sulfate:N-desulfoheparin N-sulfotransferase;
            heparitin sulfotransferase;
            3'-phosphoadenylyl-sulfate:heparitin N-sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine
            N-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine =
            adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
ALL_REAC    (other) R02122
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            [heparan sulfate]-glucosamine
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            [heparan sulfate]-N-sulfoglucosamine
COMMENT     The enzyme also catalyses the sulfation of chondroitin 4-sulfate and
            dermatan sulfate, but to a much more limited extent.
REFERENCE   1
  AUTHORS   Suzuki, S., Trenn, R.H. and Strominger, J.L.
  TITLE     Separation of specific mucopolysaccharide sulfotransferases.
  JOURNAL   Biochim. Biophys. Acta 50 (1961) 169-174.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:4964017]
  AUTHORS   Eisenman RA, Balasubramanian AS, Marx W.
  TITLE     3'-Phosphoadenylylsulfate:N-desulfoheparin sulfotransferase
            associated with a postmicrosomal particulate mastocytoma fraction.
  JOURNAL   Arch. Biochem. Biophys. 119 (1967) 387-97.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:4270798]
  AUTHORS   Johnson AH, Baker JR.
  TITLE     The enzymatic sulphation of heparan sulphate by hen's uterus.
  JOURNAL   Biochim. Biophys. Acta. 320 (1973) 341-51.
  ORGANISM  chicken [GN:gga]
GENES       HSA: 3340(NDST1)
            MMU: 15531(Ndst1)
            RNO: 29633(Ndst1)
            CFA: 489185(NDST1)
            BTA: 514172(LOC514172)
            XLA: 443855(MGC79080)
            XTR: 496577(ndst1)
            DME: Dmel_CG8339(sfl)
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.8
            ExPASy - ENZYME nomenclature database: 2.8.2.8
            ExplorEnz - The Enzyme Database: 2.8.2.8
            ERGO genome analysis and discovery system: 2.8.2.8
            BRENDA, the Enzyme Database: 2.8.2.8
            CAS: 9026-75-9
///
ENTRY       EC 2.8.2.9                  Enzyme
NAME        tyrosine-ester sulfotransferase;
            aryl sulfotransferase IV;
            L-tyrosine methyl ester sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:L-tyrosine-methyl-ester sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + L-tyrosine methyl ester = adenosine
            3',5'-bisphosphate + L-tyrosine methyl ester 4-sulfate [RN:R04213]
ALL_REAC    R04213
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            L-tyrosine methyl ester [CPD:C03404]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            L-tyrosine methyl ester 4-sulfate [CPD:C04201]
COMMENT     Phenols and organic hydroxylamines can act as acceptors (cf. EC
            2.8.2.1 aryl sulfotransferase).
REFERENCE   1  [PMID:6945304]
  AUTHORS   Duffel MW, Jakoby WB.
  TITLE     On the mechanism of aryl sulfotransferase.
  JOURNAL   J. Biol. Chem. 256 (1981) 11123-7.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:5441369]
  AUTHORS   Mattock P, Jones JG.
  TITLE     Partial purification and properties of an enzyme from rat liver that
            catalyses the sulphation of L-tyrosyl derivatives.
  JOURNAL   Biochem. J. 116 (1970) 797-803.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:6946725]
  AUTHORS   Sekura RD, Jakoby WB.
  TITLE     Aryl sulfotransferase IV from rat liver.
  JOURNAL   Arch. Biochem. Biophys. 211 (1981) 352-9.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K01018  tyrosine-ester sulfotransferase
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.9
            ExPASy - ENZYME nomenclature database: 2.8.2.9
            ExplorEnz - The Enzyme Database: 2.8.2.9
            ERGO genome analysis and discovery system: 2.8.2.9
            BRENDA, the Enzyme Database: 2.8.2.9
            CAS: 9055-56-5
///
ENTRY       EC 2.8.2.10                 Enzyme
NAME        Renilla-luciferin sulfotransferase;
            luciferin sulfotransferase;
            luciferin sulfokinase;
            luciferin sulfokinase (3'-phosphoadenylyl sulfate:luciferin
            sulfotransferase)
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:Renilla luciferin sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + Renilla luciferin = adenosine
            3',5'-bisphosphate + luciferyl sulfate [RN:R03138]
ALL_REAC    R03138
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            Renilla luciferin [CPD:C00982]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            luciferyl sulfate [CPD:C02555]
COMMENT     The product may be identical with Watasenia luciferin.
REFERENCE   1  [PMID:4392153]
  AUTHORS   Cormier MJ, Hori K, Karkhanis YD.
  TITLE     Studies on the bioluminescence of Renilla reniformis. VII.
            Conversion of luciferin into luciferyl sulfate by luciferin
            sulfokinase.
  JOURNAL   Biochemistry. 9 (1970) 1184-9.
  ORGANISM  Renilla reniformis
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.10
            ExPASy - ENZYME nomenclature database: 2.8.2.10
            ExplorEnz - The Enzyme Database: 2.8.2.10
            ERGO genome analysis and discovery system: 2.8.2.10
            BRENDA, the Enzyme Database: 2.8.2.10
            CAS: 37278-33-4
///
ENTRY       EC 2.8.2.11                 Enzyme
NAME        galactosylceramide sulfotransferase;
            GSase;
            3'-phosphoadenosine-5'-phosphosulfate-cerebroside sulfotransferase;
            galactocerebroside sulfotransferase;
            galactolipid sulfotransferase;
            glycolipid sulfotransferase;
            glycosphingolipid sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:galactosylceramide 3'-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + a galactosylceramide = adenosine
            3',5'-bisphosphate + a galactosylceramidesulfate [RN:R04017 R06279]
ALL_REAC    R04017 R06279(G);
            (other) R05105 R06122(G)
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            galactosylceramide [CPD:C02686]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            galactosylceramidesulfate [CPD:C06125]
COMMENT     Also acts on lactosylceramide.
REFERENCE   1  [PMID:5850675]
  AUTHORS   McKhann GM, Levy R, Ho W.
  TITLE     Metabolism of sulfatides. I. The effect of galactocerebrosides on
            the synthesis of sulfatides.
  JOURNAL   Biochem. Biophys. Res. Commun. 20 (1965) 109-13.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:2562926]
  AUTHORS   Sakakibara N, Gasa S, Kamio K, Makita A, Koyanagi T.
  TITLE     Association of elevated sulfatides and sulfotransferase activities
            with human renal cell carcinoma.
  JOURNAL   Cancer. Res. 49 (1989) 335-9.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00600  Sphingolipid metabolism
ORTHOLOGY   KO: K01019  galactosylceramide sulfotransferase
GENES       HSA: 9514(GAL3ST1)
            PTR: 458758(GAL3ST1)
            MMU: 53897(Gal3st1)
            RNO: 683713(LOC683713)
            CFA: 611960(GAL3ST1)
            BTA: 513295(MGC140153)
            GGA: 417006(GAL3ST1)
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.11
            ExPASy - ENZYME nomenclature database: 2.8.2.11
            ExplorEnz - The Enzyme Database: 2.8.2.11
            ERGO genome analysis and discovery system: 2.8.2.11
            BRENDA, the Enzyme Database: 2.8.2.11
            CAS: 9081-06-5
///
ENTRY       EC 2.8.2.12       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
COMMENT     Deleted entry: heparitin sulfotransferase. Enzyme identical to EC
            2.8.2.8, [heparan sulfate]-glucosamine N-sulfotransferase (EC
            2.8.2.12 created 1972, deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.12
            ExPASy - ENZYME nomenclature database: 2.8.2.12
            ExplorEnz - The Enzyme Database: 2.8.2.12
            ERGO genome analysis and discovery system: 2.8.2.12
            BRENDA, the Enzyme Database: 2.8.2.12
///
ENTRY       EC 2.8.2.13                 Enzyme
NAME        psychosine sulfotransferase;
            PAPS:psychosine sulphotransferase;
            3'-phosphoadenosine 5'-phosphosulfate-psychosine sulphotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:galactosylsphingosine sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + galactosylsphingosine = adenosine
            3',5'-bisphosphate + psychosine sulfate [RN:R03700]
ALL_REAC    R03700
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            galactosylsphingosine [CPD:C01747]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            psychosine sulfate [CPD:C02744]
REFERENCE   1  [PMID:5042474]
  AUTHORS   Nussbaum JL, Mandel P.
  TITLE     Enzymic synthesis of psychosine sulphate.
  JOURNAL   J. Neurochem. 19 (1972) 1789-802.
  ORGANISM  mouse [GN:mmu]
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.13
            ExPASy - ENZYME nomenclature database: 2.8.2.13
            ExplorEnz - The Enzyme Database: 2.8.2.13
            ERGO genome analysis and discovery system: 2.8.2.13
            BRENDA, the Enzyme Database: 2.8.2.13
            CAS: 37259-76-0
///
ENTRY       EC 2.8.2.14                 Enzyme
NAME        bile-salt sulfotransferase;
            BAST I;
            bile acid:3'-phosphoadenosine-5'-phosphosulfate sulfotransferase;
            bile salt:3'phosphoadenosine-5'-phosphosulfate:sulfotransferase;
            bile acid sulfotransferase I;
            glycolithocholate sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:glycolithocholate sulfotransferase
REACTION    (1) 3'-phosphoadenylyl sulfate + glycolithocholate = adenosine
            3',5'-bisphosphate + glycolithocholate 3-sulfate [RN:R07287];
            (2) 3'-phosphoadenylyl sulfate + taurolithocholate = adenosine
            3',5'-bisphosphate + taurolithocholate sulfate [RN:R03987]
ALL_REAC    R03987 R07287
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            glycolithocholate [CPD:C15557];
            taurolithocholate [CPD:C02592]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            glycolithocholate 3-sulfate [CPD:C11301];
            taurolithocholate sulfate [CPD:C03642]
COMMENT     The formation of sulfate esters of bile acids is an essential step
            in the prevention of toxicity by monohydroxy bile acids in many
            species [3]. This enzyme is both a bile salt and a 3-hydroxysteroid
            sulfotransferase. In addition to the 5beta-bile acid
            glycolithocholate, deoxycholate, 3beta-hydroxy-5-cholenoate and
            dehydroepiandrosterone (3beta-hydroxyandrost-5-en-17-one) also act
            as substrates [see also EC 2.8.2.2 (alcohol sulfotransferase) and EC
            2.8.2.34 (glycochenodeoxycholate sulfotransferase)]. May be
            identical to EC 2.8.2.2 [3].
REFERENCE   1  [PMID:831833]
  AUTHORS   Chen LJ, Bolt RJ, Admirand WH.
  TITLE     Enzymatic sulfation of bile salts. Partial purification and
            characterization of an enzyme from rat liver that catalyzes the
            sulfation of bile salts.
  JOURNAL   Biochim. Biophys. Acta. 480 (1977) 219-27.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:3470420]
  AUTHORS   Barnes S, Waldrop R, Crenshaw J, King RJ, Taylor KB.
  TITLE     Evidence for an ordered reaction mechanism for bile salt:
            3'phosphoadenosine-5'-phosphosulfate: sulfotransferase from rhesus
            monkey liver that catalyzes the sulfation of the hepatotoxin
            glycolithocholate.
  JOURNAL   J. Lipid. Res. 27 (1986) 1111-23.
  ORGANISM  monkey
REFERENCE   3  [PMID:2754334]
  AUTHORS   Barnes S, Buchina ES, King RJ, McBurnett T, Taylor KB.
  TITLE     Bile acid sulfotransferase I from rat liver sulfates bile acids and
            3-hydroxy steroids: purification, N-terminal amino acid sequence,
            and kinetic properties.
  JOURNAL   J. Lipid. Res. 30 (1989) 529-40.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:12543708]
  AUTHORS   Russell DW.
  TITLE     The enzymes, regulation, and genetics of bile acid synthesis.
  JOURNAL   Annu. Rev. Biochem. 72 (2003) 137-74.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.14
            ExPASy - ENZYME nomenclature database: 2.8.2.14
            ExplorEnz - The Enzyme Database: 2.8.2.14
            ERGO genome analysis and discovery system: 2.8.2.14
            BRENDA, the Enzyme Database: 2.8.2.14
            CAS: 65802-92-8
///
ENTRY       EC 2.8.2.15                 Enzyme
NAME        steroid sulfotransferase;
            steroid alcohol sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:phenolic-steroid sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + a phenolic steroid = adenosine
            3',5'-bisphosphate + steroid O-sulfate [RN:R03946]
ALL_REAC    R03946 > R00535 R00536 R00537 R02350
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            phenolic steroid [CPD:C02453]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            steroid O-sulfate [CPD:C02590]
COMMENT     Broad specificity resembling EC 2.8.2.2 alcohol sulfotransferase,
            but also acts on estrone.
REFERENCE   1  [PMID:6932974]
  AUTHORS   Adams JB, McDonald D.
  TITLE     Enzymic synthesis of steroid sulphates. XIII. Isolation and
            properties of dehydroepiandrosterone sulphotransferase from human
            foetal adrenals.
  JOURNAL   Biochim. Biophys. Acta. 615 (1980) 275-8.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00150  Androgen and estrogen metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.15
            ExPASy - ENZYME nomenclature database: 2.8.2.15
            ExplorEnz - The Enzyme Database: 2.8.2.15
            ERGO genome analysis and discovery system: 2.8.2.15
            BRENDA, the Enzyme Database: 2.8.2.15
            CAS: 9032-76-2
///
ENTRY       EC 2.8.2.16                 Enzyme
NAME        thiol sulfotransferase;
            phosphoadenylylsulfate-thiol sulfotransferase;
            PAPS sulfotransferase;
            adenosine 3'-phosphate 5'-sulphatophosphate sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:thiol S-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + a thiol = adenosine 3',5'-bisphosphate
            + an S-alkyl thiosulfate [RN:R01236]
ALL_REAC    R01236
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            thiol [CPD:C00145]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            S-alkyl thiosulfate [CPD:C02885]
COMMENT     Also acts on dithiols; substrates include glutathione,
            dithioerythritol and 2,3-mercaptopropanol.
REFERENCE   1
  AUTHORS   Schmidt, A.
  TITLE     The adenosine-5'-phosphosulfate sulfotransferase from spinach
            (Spinacea oleracea L.). Stabilization, partial purification, and
            properties.
  JOURNAL   Planta 130 (1976) 257-263.
  ORGANISM  spinach
REFERENCE   2
  AUTHORS   Schmidt, A. and Christen, U.
  TITLE     A PAPS-dependent sulfotransferase in Cyanophora paradoxa inhibited
            by 5'-AMP, 5'-ADP and APS.
  JOURNAL   Z. Naturforsch. C: Biosci. 34 (1979) 222-228.
  ORGANISM  Cyanophora paradoxa
REFERENCE   3
  AUTHORS   Tsang, M.
  TITLE     L.-S. and Schiff, J.A. Studies of sulfate utilization by algae. 17.
            Reactions of the adenosine 5'-phosphosulfate (APS) sulfotransferase
            from Chlorella and studies of model reactions which explain the
            diversity of side products with thiols.
  JOURNAL   Plant Cell Physiol. 17 (1976) 1209-1220.
  ORGANISM  Chlorella pyrenoidosa
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.16
            ExPASy - ENZYME nomenclature database: 2.8.2.16
            ExplorEnz - The Enzyme Database: 2.8.2.16
            ERGO genome analysis and discovery system: 2.8.2.16
            BRENDA, the Enzyme Database: 2.8.2.16
            CAS: 70356-45-5
///
ENTRY       EC 2.8.2.17                 Enzyme
NAME        chondroitin 6-sulfotransferase;
            chondroitin 6-O-sulfotransferase;
            3'-phosphoadenosine 5'-phosphosulfate (PAPS):chondroitin sulfate
            sulfotransferase;
            terminal 6-sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:chondroitin 6'-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + chondroitin = adenosine
            3',5'-bisphosphate + chondroitin 6'-sulfate [RN:R02181]
ALL_REAC    R02181
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            chondroitin [CPD:C00401]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            chondroitin 6'-sulfate [CPD:C00635]
COMMENT     The sulfation is at the 6-position of N-acetylgalactosamine residues
            of chondroitin. Not identical with EC 2.8.2.5 chondroitin
            4-sulfotransferase.
REFERENCE   1  [PMID:6957247]
  AUTHORS   Habuchi O, Miyashita N.
  TITLE     Separation and characterization of chondroitin 6-sulfotransferase
            and chondroitin 4-sulfotransferase from chick embryo cartilage.
  JOURNAL   Biochim. Biophys. Acta. 717 (1982) 414-21.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00532  Chondroitin sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K01020  chondroitin 6-sulfotransferase 3
            KO: K04743  chondroitin 6-sulfotransferase 7
GENES       HSA: 56548(CHST7) 9469(CHST3)
            PTR: 466290(CHST3)
            MMU: 53374(Chst3) 60322(Chst7)
            RNO: 302302(Chst7) 84468(Chst3)
            CFA: 489036(CHST3) 491852(CHST7)
            BTA: 506758(LOC506758) 540357(LOC540357)
            GGA: 396018(CHST3)
            DRE: 556800(LOC556800) 563748(LOC563748)
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.17
            ExPASy - ENZYME nomenclature database: 2.8.2.17
            ExplorEnz - The Enzyme Database: 2.8.2.17
            ERGO genome analysis and discovery system: 2.8.2.17
            BRENDA, the Enzyme Database: 2.8.2.17
            CAS: 83589-04-2
///
ENTRY       EC 2.8.2.18                 Enzyme
NAME        cortisol sulfotransferase;
            glucocorticosteroid sulfotransferase;
            glucocorticoid sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:cortisol 21-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + cortisol = adenosine 3',5'-bisphosphate
            + cortisol 21-sulfate [RN:R02839]
ALL_REAC    R02839
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            cortisol [CPD:C00735]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            cortisol 21-sulfate [CPD:C02822]
REFERENCE   1  [PMID:6957246]
  AUTHORS   Singer SS, Brill B.
  TITLE     Enzymatic sulfation of steroids. XVII. The properties of the
            glucocorticoid sulfotransferase activity of guinea pig liver
            cytosol.
  JOURNAL   Biochim. Biophys. Acta. 712 (1982) 590-6.
  ORGANISM  guinea pig
REFERENCE   2  [PMID:1278101]
  AUTHORS   Singer SS, Giera D, Johnson J, Sylvester S.
  TITLE     Enzymatic sulfation of steroids: I. The enzymatic basis for the sex
            difference in cortisol sulfation by rat liver preparations.
  JOURNAL   Endocrinology. 98 (1976) 963-74.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.18
            ExPASy - ENZYME nomenclature database: 2.8.2.18
            ExplorEnz - The Enzyme Database: 2.8.2.18
            ERGO genome analysis and discovery system: 2.8.2.18
            BRENDA, the Enzyme Database: 2.8.2.18
            CAS: 71427-08-2
///
ENTRY       EC 2.8.2.19                 Enzyme
NAME        triglucosylalkylacylglycerol sulfotransferase;
            triglucosylmonoalkylmonoacyl sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:triglucosyl-1-O-alkyl-2-O-acylglycerol
            6-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate +
            alpha-D-glucosyl-1,6-alpha-D-glucosyl-1,6-alpha-D-glucosyl-1,3-1-O-
            alkyl-2-O-acylglycerol = adenosine 3',5'-bisphosphate +
            6-sulfo-alpha-D-glucosyl-1,6-alpha-D-glucosyl-1,6-alpha-D-glucosyl-
            1,3-1-O-alkyl-2-O-acylglycerol [RN:R04643]
ALL_REAC    R04643
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            alpha-D-glucosyl-1,6-alpha-D-glucosyl-1,6-alpha-D-glucosyl-1,3-1-O-
            alkyl-2-O-acylglycerol [CPD:C04909]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            6-sulfo-alpha-D-glucosyl-1,6-alpha-D-glucosyl-1,6-alpha-D-glucosyl-
            1,3-1-O-alkyl-2-O-acylglycerol [CPD:C04920]
REFERENCE   1  [PMID:6956577]
  AUTHORS   Liau YH, Zdebska E, Slomiany A, Slomiany BL.
  TITLE     Biosynthesis in vitro of a sulfated triglucosyl
            monoalkylmonoacylglycerol by rat gastric mucosa.
  JOURNAL   J. Biol. Chem. 257 (1982) 12019-23.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.19
            ExPASy - ENZYME nomenclature database: 2.8.2.19
            ExplorEnz - The Enzyme Database: 2.8.2.19
            ERGO genome analysis and discovery system: 2.8.2.19
            BRENDA, the Enzyme Database: 2.8.2.19
            CAS: 83589-05-3
///
ENTRY       EC 2.8.2.20                 Enzyme
NAME        protein-tyrosine sulfotransferase;
            tyrosylprotein sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:protein-tyrosine O-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + protein tyrosine = adenosine
            3',5'-bisphosphate + protein tyrosine-O-sulfate [RN:R02586]
ALL_REAC    R02586
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            protein tyrosine [CPD:C00585]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            protein tyrosine-O-sulfate [CPD:C03721]
COMMENT     The tyrosine residues of some specific proteins of rat
            pheochromocytoma cells act as acceptors.
REFERENCE   1  [PMID:6577005]
  AUTHORS   Lee RW, Huttner WB.
  TITLE     Tyrosine-O-sulfated proteins of PC12 pheochromocytoma cells and
            their sulfation by a tyrosylprotein sulfotransferase.
  JOURNAL   J. Biol. Chem. 258 (1983) 11326-34.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K01021  protein-tyrosine sulfotransferase
GENES       HSA: 8459(TPST2) 8460(TPST1)
            PTR: 472398(TPST1)
            MMU: 22021(Tpst1) 22022(Tpst2)
            CFA: 486332(TPST2) 489788(TPST1)
            GGA: 416910(RCJMB04_17p1) 417546(TPST1)
            XLA: 444016(MGC82552) 495291(LOC495291)
            DRE: 30677(tpst1) 393171(tpst1l)
            DME: Dmel_CG32632(Tango13)
            CEL: F42G9.8 Y111B2A.15
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.20
            ExPASy - ENZYME nomenclature database: 2.8.2.20
            ExplorEnz - The Enzyme Database: 2.8.2.20
            ERGO genome analysis and discovery system: 2.8.2.20
            BRENDA, the Enzyme Database: 2.8.2.20
            CAS: 87588-33-8
///
ENTRY       EC 2.8.2.21                 Enzyme
NAME        keratan sulfotransferase;
            3'-phosphoadenylyl keratan sulfotransferase;
            keratan sulfate sulfotransferase;
            3'-phosphoadenylylsulfate:keratan sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:keratan 6'-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + keratan = adenosine 3',5'-bisphosphate
            + keratan 6'-sulfate [RN:R03553]
ALL_REAC    R03553
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            keratan [CPD:C00573]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            keratan 6'-sulfate [CPD:C00573]
COMMENT     Sulfation takes place at the 6-position of galactosyl and
            N-acetylglucosaminyl residues in keratan, a proteoglycan. Not
            identical with EC 2.8.2.5 (chondroitin 4-sulfotransferase), EC
            2.8.2.6 (choline sulfotransferase) or EC 2.8.2.17 (chondroitin
            6-sulfotransferase).
REFERENCE   1  [PMID:6592165]
  AUTHORS   Ruter ER, Kresse H.
  TITLE     Partial purification and characterization of
            3'-phosphoadenylylsulfate:keratan sulfate sulfotransferases.
  JOURNAL   J. Biol. Chem. 259 (1984) 11771-6.
  ORGANISM  cow [GN:bta]
GENES       HSA: 8534(CHST1)
            MMU: 76969(Chst1)
            RNO: 295934(Chst1)
            DRE: 445124(chst1)
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.21
            ExPASy - ENZYME nomenclature database: 2.8.2.21
            ExplorEnz - The Enzyme Database: 2.8.2.21
            ERGO genome analysis and discovery system: 2.8.2.21
            BRENDA, the Enzyme Database: 2.8.2.21
            CAS: 62168-79-0
///
ENTRY       EC 2.8.2.22                 Enzyme
NAME        aryl-sulfate sulfotransferase;
            arylsulfate-phenol sulfotransferase;
            arylsulfotransferase;
            ASST;
            arylsulfate sulfotransferase;
            arylsulfate:phenol sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     aryl-sulfate:phenol sulfotransferase
REACTION    an aryl sulfate + a phenol = a phenol + an aryl sulfate
ALL_REAC    (other) R02996
SUBSTRATE   aryl sulfate [CPD:C00850];
            phenol [CPD:C00146]
PRODUCT     phenol [CPD:C00146];
            aryl sulfate [CPD:C00850]
COMMENT     Hydroxy groups of tyrosine residues in peptides such as angiotensin
            can act as acceptors. Does not act on 3'-phosphoadenylyl sulfate or
            adenosine 3',5'-bisphosphate.
REFERENCE   1  [PMID:3460636]
  AUTHORS   Kim DH, Konishi L, Kobashi K.
  TITLE     Purification, characterization and reaction mechanism of novel
            arylsulfotransferase obtained from an anaerobic bacterium of human
            intestine.
  JOURNAL   Biochim. Biophys. Acta. 872 (1986) 33-41.
  ORGANISM  human [GN:hsa]
REFERENCE   2
  AUTHORS   Kobashi, K., Kim, D.-H. and Morikawa, T.
  TITLE     A novel type of arylsulfotransferase.
  JOURNAL   J. Protein Chem. 6 (1987) 237-244.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01023  arylsulfate sulfotransferase
GENES       ECC: c3785(assT)
            ECI: UTI89_C3473(assT)
            ECP: ECP_3130
            ECV: APECO1_3375(assT)
            STY: STY3771
            PEN: PSEEN0187
            LPL: lp_1381(astA)
            LSA: LSA0090 LSA0091
            LBR: LVIS_2143
            DSY: DSY2571
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.22
            ExPASy - ENZYME nomenclature database: 2.8.2.22
            ExplorEnz - The Enzyme Database: 2.8.2.22
            ERGO genome analysis and discovery system: 2.8.2.22
            BRENDA, the Enzyme Database: 2.8.2.22
            CAS: 158254-86-5
///
ENTRY       EC 2.8.2.23                 Enzyme
NAME        [heparan sulfate]-glucosamine 3-sulfotransferase 1;
            heparin-glucosamine 3-O-sulfotransferase;
            3'-phosphoadenylyl-sulfate:heparin-glucosamine 3-O-sulfotransferase;
            glucosaminyl 3-O-sulfotransferase;
            heparan sulfate D-glucosaminyl 3-O-sulfotransferase;
            isoform/isozyme 1 (3-OST-1, HS3ST1)
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine
            3-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine =
            adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine
            3-sulfate
ALL_REAC    (other) R04064
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            [heparan sulfate]-glucosamine
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            [heparan sulfate]-glucosamine 3-sulfate [CPD:C11553]
COMMENT     This enzyme differs from the other [heparan sulfate]-glucosamine
            3-sulfotransferases [EC 2.8.2.29 ([heparan sulfate]-glucosamine
            3-sulfotransferase 2) and EC 2.8.2.30 ([heparan sulfate]-glucosamine
            3-sulfotransferase 3)] by being the most selective for a precursor
            of the antithrombin-binding site. It has a minimal acceptor sequence
            of: -> GlcNAc6S-> GlcA-> GlcN2S*+/-6S-> IdoA2S-> GlcN2S-> , the
            asterisk marking the target (symbols as in 2-Carb-38) using +/- to
            mean the presence or absence of a substituent, and > to separate a
            predominant structure from a minor one. Thus Glc(N2S > NAc) means a
            residue of glucosamine where the N carries a sulfo group mainly but
            occasionally an acetyl group.) [1-4]. It can also modify other
            precursor sequences within heparan sulfate but this action does not
            create functional antithrombin-binding sites. These precursors are
            variants of the consensus sequence: -> Glc(N2S > NAc)+/-6S-> GlcA->
            GlcN2S*+/-6S-> GlcA > IdoA+/-2S-> Glc(N2S/NAc)+/-6S-> [5]. If the
            heparan sulfate substrate lacks 2-O-sulfation of GlcA residues, then
            enzyme specificity is expanded to modify selected glucosamine
            residues preceded by IdoA as well as GlcA [6].
REFERENCE   1  [PMID:3139669]
  AUTHORS   Kusche M, Backstrom G, Riesenfeld J, Petitou M, Choay J, Lindahl U.
  TITLE     Biosynthesis of heparin. O-sulfation of the antithrombin-binding
            region.
  JOURNAL   J. Biol. Chem. 263 (1988) 15474-84.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:8900197]
  AUTHORS   Shworak NW, Fritze LM, Liu J, Butler LD, Rosenberg RD.
  TITLE     Cell-free synthesis of anticoagulant heparan sulfate reveals a
            limiting converting activity that modifies an excess precursor pool.
  JOURNAL   J. Biol. Chem. 271 (1996) 27063-71.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:8900198]
  AUTHORS   Liu J, Shworak NW, Fritze LM, Edelberg JM, Rosenberg RD.
  TITLE     Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferase.
  JOURNAL   J. Biol. Chem. 271 (1996) 27072-82.
  ORGANISM  mouse [GN:mmu]
REFERENCE   4  [PMID:9346953]
  AUTHORS   Shworak NW, Liu J, Fritze LM, Schwartz JJ, Zhang L, Logeart D,
            Rosenberg RD.
  TITLE     Molecular cloning and expression of mouse and human cDNAs encoding
            heparan sulfate D-glucosaminyl 3-O-sulfotransferase.
  JOURNAL   J. Biol. Chem. 272 (1997) 28008-19.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:10026187]
  AUTHORS   Zhang L, Yoshida K, Liu J, Rosenberg RD.
  TITLE     Anticoagulant heparan sulfate precursor structures in F9 embryonal
            carcinoma cells.
  JOURNAL   J. Biol. Chem. 274 (1999) 5681-91.
  ORGANISM  cow [GN:bta]
REFERENCE   6  [PMID:11375390]
  AUTHORS   Zhang L, Lawrence R, Schwartz JJ, Bai X, Wei G, Esko JD, Rosenberg
            RD.
  TITLE     The effect of precursor structures on the action of glucosaminyl
            3-O-sulfotransferase-1 and the biosynthesis of anticoagulant heparan
            sulfate.
  JOURNAL   J. Biol. Chem. 276 (2001) 28806-13.
  ORGANISM  hamster
PATHWAY     PATH: map00534  Heparan sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K01024  [heparan sulfate]-glucosamine 3-sulfotransferase 1
            KO: K08104  [heparan sulfate]-glucosamine 3-sulfotransferase 5
GENES       HSA: 222537(HS3ST5) 9951(HS3ST4) 9957(HS3ST1)
            PTR: 468097(HS3ST4) 471144(HS3ST1)
            MMU: 15476(Hs3st1) 319415(Hs3st5) 628779(EG628779)
            RNO: 294449(Hs3st5_predicted) 687675(LOC687675) 84406(Hs3st1)
            CFA: 403672(HS3ST1) 481968(HS3ST5) 489960(HS3ST4)
            BTA: 525835(LOC525835) 538691(MGC142451) 540355(MGC139532)
            GGA: 422840(HS3ST1) 427674(HS3ST4) 428621(HS3ST5)
            XLA: 398971(LOC398971)
            XTR: 496940(hs3st1)
            DRE: 557111(LOC557111)
            SPU: 594559(LOC594559)
            DME: Dmel_CG7890
STRUCTURES  PDB: 1VKJ  1ZRH  
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.23
            ExPASy - ENZYME nomenclature database: 2.8.2.23
            ExplorEnz - The Enzyme Database: 2.8.2.23
            ERGO genome analysis and discovery system: 2.8.2.23
            BRENDA, the Enzyme Database: 2.8.2.23
            CAS: 118113-79-4
///
ENTRY       EC 2.8.2.24                 Enzyme
NAME        desulfoglucosinolate sulfotransferase;
            PAPS-desulfoglucosinolate sulfotransferase;
            3'-phosphoadenosine-5'-phosphosulfate:desulfoglucosinolate
            sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:desulfoglucosinolate sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + desulfoglucotropeolin = adenosine
            3',5'-bisphosphate + glucotropeolin [RN:R03214]
ALL_REAC    R03214
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            desulfoglucotropeolin [CPD:C01069]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            glucotropeolin [CPD:C02153]
COMMENT     Involved with EC 2.4.1.195 thiohydroximate
            beta-D-glucosyltransferase, in the biosynthesis of thioglycosides in
            cruciferous plants.
REFERENCE   1  [PMID:2524977]
  AUTHORS   Jain JC, Reed DW, GrootWassink JW, Underhill EW.
  TITLE     A radioassay of enzymes catalyzing the glucosylation and sulfation
            steps of glucosinolate biosynthesis in Brassica species.
  JOURNAL   Anal. Biochem. 178 (1989) 137-40.
  ORGANISM  Brassica napus [GN:ebna], Brassica juncea, Brassica campestris,
            Brassica oleracea, Brassica nigra
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.24
            ExPASy - ENZYME nomenclature database: 2.8.2.24
            ExplorEnz - The Enzyme Database: 2.8.2.24
            ERGO genome analysis and discovery system: 2.8.2.24
            BRENDA, the Enzyme Database: 2.8.2.24
            CAS: 121479-85-4
///
ENTRY       EC 2.8.2.25                 Enzyme
NAME        flavonol 3-sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:quercetin 3-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + quercetin = adenosine
            3',5'-bisphosphate + quercetin 3-sulfate [RN:R02159]
ALL_REAC    R02159
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            quercetin [CPD:C00389]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            quercetin 3-sulfate [CPD:C00616]
COMMENT     Also acts on some other flavonol aglycones.
REFERENCE   1
  AUTHORS   Varin, L. and Ibrahim, R.K.
  TITLE     Partial purification and characterization of 3 flavonol-specific
            sulfotransferases from Flaveria chloraefolia.
  JOURNAL   Plant Physiol. 90 (1989) 977-981.
  ORGANISM  Flaveria chloraefolia
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.25
            ExPASy - ENZYME nomenclature database: 2.8.2.25
            ExplorEnz - The Enzyme Database: 2.8.2.25
            ERGO genome analysis and discovery system: 2.8.2.25
            BRENDA, the Enzyme Database: 2.8.2.25
            CAS: 121855-10-5
///
ENTRY       EC 2.8.2.26                 Enzyme
NAME        quercetin-3-sulfate 3'-sulfotransferase;
            flavonol 3'-sulfotransferase;
            3'-Sulfotransferase;
            PAPS:flavonol 3-sulfate 3'-sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:quercetin-3-sulfate 3'-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + quercetin 3-sulfate = adenosine
            3',5'-bisphosphate + quercetin 3,3'-bissulfate [RN:R02632]
ALL_REAC    R02632
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            quercetin 3-sulfate [CPD:C00616]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            quercetin 3,3'-bissulfate [CPD:C01155]
REFERENCE   1
  AUTHORS   Varin, L. and Ibrahim, R.K.
  TITLE     Partial purification and characterization of 3 flavonol-specific
            sulfotransferases from Flaveria chloraefolia.
  JOURNAL   Plant Physiol. 90 (1989) 977-981.
  ORGANISM  Flaveria chloraefolia
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.26
            ExPASy - ENZYME nomenclature database: 2.8.2.26
            ExplorEnz - The Enzyme Database: 2.8.2.26
            ERGO genome analysis and discovery system: 2.8.2.26
            BRENDA, the Enzyme Database: 2.8.2.26
            CAS: 121855-11-6
///
ENTRY       EC 2.8.2.27                 Enzyme
NAME        quercetin-3-sulfate 4'-sulfotransferase;
            flavonol 4'-sulfotransferase;
            PAPS:flavonol 3-sulfate 4'-sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:quercetin-3-sulfate 4'-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + quercetin 3-sulfate = adenosine
            3',5'-bisphosphate + quercetin 3,4'-bissulfate [RN:R02633]
ALL_REAC    R02633
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            quercetin 3-sulfate [CPD:C00616]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            quercetin 3,4'-bissulfate [CPD:C01156]
REFERENCE   1
  AUTHORS   Varin, L. and Ibrahim, R.K.
  TITLE     Partial purification and characterization of 3 flavonol-specific
            sulfotransferases from Flaveria chloraefolia.
  JOURNAL   Plant Physiol. 90 (1989) 977-981.
  ORGANISM  Flaveria chloraefolia
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.27
            ExPASy - ENZYME nomenclature database: 2.8.2.27
            ExplorEnz - The Enzyme Database: 2.8.2.27
            ERGO genome analysis and discovery system: 2.8.2.27
            BRENDA, the Enzyme Database: 2.8.2.27
            CAS: 121855-12-7
///
ENTRY       EC 2.8.2.28                 Enzyme
NAME        quercetin-3,3'-bissulfate 7-sulfotransferase;
            flavonol 7-sulfotransferase;
            7-sulfotransferase;
            PAPS:flavonol 3,3'/3,4'-disulfate 7-sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:quercetin-3,3'-bissulfate
            7-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + quercetin 3,3'-bissulfate = adenosine
            3',5'-bisphosphate + quercetin 3,7,3'-trissulfate [RN:R03289]
ALL_REAC    R03289;
            (other) R06809
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            quercetin 3,3'-bissulfate [CPD:C01155]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            quercetin 3,7,3'-trissulfate
COMMENT     Quercetin 3,4'-bissulfate can also act as acceptor.
REFERENCE   1
  AUTHORS   Varin, L.
  TITLE     Enzymatic synthesis of sulfated flavonoids in Flaveria spp.
  JOURNAL   Bull. Liaison-Groupe Polyphenols 14 (1988) 248-257.
  ORGANISM  Flaveria spp.
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.28
            ExPASy - ENZYME nomenclature database: 2.8.2.28
            ExplorEnz - The Enzyme Database: 2.8.2.28
            ERGO genome analysis and discovery system: 2.8.2.28
            BRENDA, the Enzyme Database: 2.8.2.28
            CAS: 121855-13-8
///
ENTRY       EC 2.8.2.29                 Enzyme
NAME        [heparan sulfate]-glucosamine 3-sulfotransferase 2;
            glucosaminyl 3-O-sulfotransferase;
            heparan sulfate D-glucosaminyl 3-O-sulfotransferase;
            isoform/isozyme 2 (3-OST-2, HS3ST2)
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine
            3-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine =
            adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine
            3-sulfate [RN:R05798]
ALL_REAC    R05798
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            [heparan sulfate]-glucosamine
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            [heparan sulfate]-glucosamine 3-sulfate [CPD:C11553]
COMMENT     This enzyme sulfates the residues marked with an asterisk in
            sequences containing at least -> IdoA2S-> GlcN*-> or -> GlcA2S->
            GlcN*-> (symbols as in 2-Carb-38). Preference for GlcN2S vs.
            unmodified GlcN has not yet been established. Additional structural
            features are presumably required for substrate recognition, since
            the 3-O-sulfated residue is of low abundance, whereas the above
            IdoA-containing sequence is quite abundant. This enzyme differs from
            the other [heparan sulfate]-glucosamine 3-sulfotransferases by
            modifying selected glucosamine residues preceded by GlcA2S; EC
            2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1)
            prefers GlcA or IdoA, whereas EC 2.8.2.30 ([heparan
            sulfate]-glucosamine 3-sulfotransferase 3) prefers IdoA2S.
REFERENCE   1  [PMID:9988767]
  AUTHORS   Shworak NW, Liu J, Petros LM, Zhang L, Kobayashi M, Copeland NG,
            Jenkins NA, Rosenberg RD.
  TITLE     Multiple isoforms of heparan sulfate D-glucosaminyl
            3-O-sulfotransferase. Isolation, characterization, and expression of
            human cdnas and identification of distinct genomic loci.
  JOURNAL   J. Biol. Chem. 274 (1999) 5170-84.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:9988768]
  AUTHORS   Liu J, Shworak NW, Sinay P, Schwartz JJ, Zhang L, Fritze LM,
            Rosenberg RD.
  TITLE     Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase
            isoforms reveals novel substrate specificities.
  JOURNAL   J. Biol. Chem. 274 (1999) 5185-92.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00534  Heparan sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K07808  [heparan sulfate]-glucosamine 3-sulfotransferase 2
GENES       HSA: 9956(HS3ST2)
            PTR: 467924(HS3ST2)
            MMU: 195646(Hs3st2)
            RNO: 293451(Hs3st2)
            CFA: 489975(HS3ST2)
            BTA: 532099(LOC532099)
            GGA: 416581(HS3ST2)
            DRE: 571246(hs3st2)
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.29
            ExPASy - ENZYME nomenclature database: 2.8.2.29
            ExplorEnz - The Enzyme Database: 2.8.2.29
            ERGO genome analysis and discovery system: 2.8.2.29
            BRENDA, the Enzyme Database: 2.8.2.29
///
ENTRY       EC 2.8.2.30                 Enzyme
NAME        [heparan sulfate]-glucosamine 3-sulfotransferase 3
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine
            3-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine =
            adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine
            3-sulfate [RN:R05798]
ALL_REAC    R05798
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            [heparan sulfate]-glucosamine
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            [heparan sulfate]-glucosamine 3-sulfate [CPD:C11553]
COMMENT     Two major substrates contain the tetrasaccharides: -> undetermined
            2-sulfo-uronic acid-> GlcN2S-> IdoA2S-> GlcN*-> and -> undetermined
            2-sulfo-uronic acid-> GlcN2S-> IdoA2S-> GlcN6S*-> (symbols as in
            2-Carb-38) with modification of the N-unsubstituted glucosamine
            residue (shown with an asterisk) [1,4]. Modification of selected
            sequences containing N-sulfo-glucosamine residues cannot yet be
            excluded. The 3-O-sulfated heparan sulfate can be utilized by Herpes
            simplex virus type 1 as an entry receptor to infect the target cells
            [2]. There are two isozymes, known as 3-OST-3A and 3-OST-3B, which
            have identical catalytic domains but are encoded by different
            mammalian genes [3]. The specificity of this enzyme differs from
            that of the other [heparan sulfate]-glucosamine 3-sulfotransferases.
            It is inefficient at modifying precursors of the antithrombin
            binding site [in contrast to EC 2.8.2.23 ([heparan
            sulfate]-glucosamine 3-sulfotransferase 1)] and it does not modify
            glucosamine preceded by GlcA2S [unlike EC 2.8.2.29 ([heparan
            sulfate]-glucosamine 3-sulfotransferase 2)].
REFERENCE   1  [PMID:10608887]
  AUTHORS   Liu J, Shriver Z, Blaiklock P, Yoshida K, Sasisekharan R, Rosenberg
            RD.
  TITLE     Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A sulfates
            N-unsubstituted glucosamine residues.
  JOURNAL   J. Biol. Chem. 274 (1999) 38155-62.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:10520990]
  AUTHORS   Shukla D, Liu J, Blaiklock P, Shworak NW, Bai X, Esko JD, Cohen GH,
            Eisenberg RJ, Rosenberg RD, Spear PG.
  TITLE     A novel role for 3-O-sulfated heparan sulfate in herpes simplex
            virus 1 entry.
  JOURNAL   Cell. 99 (1999) 13-22.
  ORGANISM  human [GN:hsa], mouse [GN:mmu]
REFERENCE   3  [PMID:9988767]
  AUTHORS   Shworak NW, Liu J, Petros LM, Zhang L, Kobayashi M, Copeland NG,
            Jenkins NA, Rosenberg RD.
  TITLE     Multiple isoforms of heparan sulfate D-glucosaminyl
            3-O-sulfotransferase. Isolation, characterization, and expression of
            human cdnas and identification of distinct genomic loci.
  JOURNAL   J. Biol. Chem. 274 (1999) 5170-84.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:9988768]
  AUTHORS   Liu J, Shworak NW, Sinay P, Schwartz JJ, Zhang L, Fritze LM,
            Rosenberg RD.
  TITLE     Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase
            isoforms reveals novel substrate specificities.
  JOURNAL   J. Biol. Chem. 274 (1999) 5185-92.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00534  Heparan sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K07809  [heparan sulfate]-glucosamine 3-sulfotransferase 3
GENES       HSA: 9953(HS3ST3B1) 9955(HS3ST3A1)
            PTR: 468393(HS3ST3B1)
            MMU: 15478(Hs3st3a1) 54710(Hs3st3b1)
            RNO: 303218(Hs3st3b1_predicted) 363618(RGD1561262_predicted)
            CFA: 489512(HS3ST3A1) 489516(HS3ST3B1)
            BTA: 521959(LOC521959) 617069(LOC617069)
            GGA: 769490(HS3ST3A1)
            DRE: 558084(hs3st3b1b)
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.30
            ExPASy - ENZYME nomenclature database: 2.8.2.30
            ExplorEnz - The Enzyme Database: 2.8.2.30
            ERGO genome analysis and discovery system: 2.8.2.30
            BRENDA, the Enzyme Database: 2.8.2.30
///
ENTRY       EC 2.8.2.31                 Enzyme
NAME        petromyzonol sulfotransferase;
            PZ-SULT
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:5alpha-cholan-3alpha,7alpha,12alpha,24-te
            trol sulfotransferase
REACTION    3'-phosphoadenylyl sulfate +
            5alpha-cholan-3alpha,7alpha,12alpha,24-tetrol = adenosine
            3',5'-bisphosphate + 5alpha-cholan-3alpha,7alpha,12alpha-triol
            24-sulfate [RN:R07797]
ALL_REAC    R07797
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            5alpha-cholan-3alpha,7alpha,12alpha,24-tetrol [CPD:C16258]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            5alpha-cholan-3alpha,7alpha,12alpha-triol 24-sulfate [CPD:C16259]
COMMENT     The enzyme from the lamprey Petromyzon marinus can also use the
            corresponding 3-ketone as a substrate. It is stereoselective
            (5alpha-cholane) and regioselective, exhibiting a preference for an
            hydroxy group at C-24. The enzyme is inactive when allocholic acid,
            which has a carboxy group at C-24, is used as a substrate.
REFERENCE   1  [PMID:14657197]
  AUTHORS   Venkatachalam KV, Llanos DE, Karami KJ, Malinovskii VA.
  TITLE     Isolation, partial purification, and characterization of a novel
            petromyzonol sulfotransferase from Petromyzon marinus (lamprey)
            larval liver.
  JOURNAL   J. Lipid. Res. 45 (2004) 486-95.
  ORGANISM  Petromyzon marinus
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.31
            ExPASy - ENZYME nomenclature database: 2.8.2.31
            ExplorEnz - The Enzyme Database: 2.8.2.31
            ERGO genome analysis and discovery system: 2.8.2.31
            BRENDA, the Enzyme Database: 2.8.2.31
///
ENTRY       EC 2.8.2.32                 Enzyme
NAME        scymnol sulfotransferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenosine 5'-phosphosulfate:5beta-scymnol sulfotransferase
REACTION    3'-phosphoadenosine 5'-phosphosulfate + 5beta-scymnol = adenosine
            3',5'-bisphosphate + 5beta-scymnol sulfate [RN:R07798]
ALL_REAC    R07798
SUBSTRATE   3'-phosphoadenosine 5'-phosphosulfate [CPD:C00053];
            5beta-scymnol [CPD:C16260]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            5beta-scymnol sulfate [CPD:C16261]
COMMENT     The enzyme from the shark Heterodontus portusjacksoni is able to
            sulfate the C27 bile salts 5beta-scymnol (the natural bile salt) and
            5alpha-cyprinol (the carp bile salt). Enzyme activity is activated
            by Mg2+ but inhibited by the product 5beta-scymnol sulfate.
REFERENCE   1  [PMID:7749614]
  AUTHORS   Macrides TA, Faktor DA, Kalafatis N, Amiet RG.
  TITLE     Enzymic sulfation of bile salts. Partial purification and
            characterization of an enzyme from the liver of the shark
            Heterodontus portusjacksoni that catalyses the sulfation of the
            shark bile steroid 5 beta-scymnol.
  JOURNAL   Comp. Biochem. Physiol. Biochem. Mol. Biol. 107 (1994) 461-9.
  ORGANISM  Heterodontus portusjacksoni
REFERENCE   2
  AUTHORS   Pettigrew, N.E., Wright, P.F.A. and Macrides, T.A.
  TITLE     Investigation of 5beta-scymnol sulfotransferase from the kidney and
            testes of Heterodontus portusjacksoni.
  JOURNAL   Comp. Biochem. Physiol. 121 (1998) 243-249.
REFERENCE   3
  AUTHORS   Pettigrew, N.E., Wright, P.F.A. and Macrides, T.A.
  TITLE     5beta-Scymnol sulfotransferase isolated from the tissues of an
            Australian shark species.
  JOURNAL   Comp. Biochem. Physiol. 121 (1998) 299-307.
REFERENCE   4
  AUTHORS   Pettigrew, N.E., Wright, P.F.A. and Macrides, T.A.
  TITLE     5beta-scymnol sulfotransferase isolated from the liver of two
            Australian ray species.
  JOURNAL   Comp. Biochem. Physiol. 121 (1998) 341-348.
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.32
            ExPASy - ENZYME nomenclature database: 2.8.2.32
            ExplorEnz - The Enzyme Database: 2.8.2.32
            ERGO genome analysis and discovery system: 2.8.2.32
            BRENDA, the Enzyme Database: 2.8.2.32
///
ENTRY       EC 2.8.2.33                 Enzyme
NAME        N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase;
            GalNAc4S-6ST
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:dermatan 6'-sulfotransferase
REACTION    (1) 3'-phosphoadenylyl sulfate + dermatan = adenosine
            3',5'-bisphosphate + dermatan 6'-sulfate [RN:R07288];
            (2) 3'-phosphoadenylyl sulfate + chondroitin = adenosine
            3',5'-bisphosphate + chondroitin 6'-sulfate [RN:R02181]
ALL_REAC    R02181 R07288
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            dermatan [CPD:C01490];
            chondroitin [CPD:C00401]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            dermatan 6'-sulfate [CPD:C15558];
            chondroitin 6'-sulfate [CPD:C00635]
COMMENT     The enzyme is activated by divalent cations and reduced glutathione.
            The enzyme from human transfers sulfate to position 6 of both
            internal residues and nonreducing terminal GalNAc 4-sulfate residues
            of chondroitin sulfate. Oligosaccharides derived from chondroitin
            sulfate also serve as acceptors but chondroitin sulfate E, keratan
            sulfate and heparan sulfate do not. Differs from EC 2.8.2.17,
            chondroitin 6-sulfotransferase, in being able to use both condoitin
            and dermatan as effective substrates
REFERENCE   1  [PMID:10871629]
  AUTHORS   Ito Y, Habuchi O.
  TITLE     Purification and characterization of N-acetylgalactosamine 4-sulfate
            6-O-sulfotransferase from the squid cartilage.
  JOURNAL   J. Biol. Chem. 275 (2000) 34728-36.
  ORGANISM  Ommastrephes sloani pacificus
REFERENCE   2  [PMID:11572857]
  AUTHORS   Ohtake S, Ito Y, Fukuta M, Habuchi O.
  TITLE     Human N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase cDNA is
            related to human B cell recombination activating gene-associated
            gene.
  JOURNAL   J. Biol. Chem. 276 (2001) 43894-900.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00532  Chondroitin sulfate biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K08106  N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase
GENES       HSA: 51363(GALNAC4S-6ST)
            PTR: 466249(LOC466249)
            MMU: 77590(4631426J05Rik)
            RNO: 286974(GalNAc4S6ST)
            CFA: 486928(LOC486928)
            BTA: 534506(LOC534506)
            GGA: 423952(LOC423952)
            DRE: 565523(LOC565523)
            SPU: 591575(LOC591575)
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.33
            ExPASy - ENZYME nomenclature database: 2.8.2.33
            ExplorEnz - The Enzyme Database: 2.8.2.33
            ERGO genome analysis and discovery system: 2.8.2.33
            BRENDA, the Enzyme Database: 2.8.2.33
///
ENTRY       EC 2.8.2.34                 Enzyme
NAME        glycochenodeoxycholate sulfotransferase;
            bile acid:3'-phosphoadenosine-5'-phosphosulfate sulfotransferase;
            bile acid:PAPS:sulfotransferase;
            BAST
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
SYSNAME     3'-phosphoadenylyl-sulfate:glycochenodeoxycholate 7-sulfotransferase
REACTION    3'-phosphoadenylyl sulfate + glycochenodeoxycholate = adenosine
            3',5'-bisphosphate + glycochenodeoxycholate 7-sulfate [RN:R07289]
ALL_REAC    R07289
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            glycochenodeoxycholate [CPD:C05466]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            glycochenodeoxycholate 7-sulfate [CPD:C15559]
COMMENT     The enzyme specifically sulfates glycochenodeoxycholate at the
            7alpha-position (see also EC 2.8.2.14 bile-salt sulfotransferase).
            The monohydroxy bile acids glycolithocholate, chenodeoxycholate and
            ursodeoxycholate act as inhibitors.
REFERENCE   1  [PMID:533830]
  AUTHORS   Barnes S, Burhol PG, Zander R, Haggstrom G, Settine RL, Hirschowitz
            BI.
  TITLE     Enzymatic sulfation of glycochenodeoxycholic acid by tissue
            fractions from adult hamsters.
  JOURNAL   J. Lipid. Res. 20 (1979) 952-9.
  ORGANISM  hamster
REFERENCE   2  [PMID:12543708]
  AUTHORS   Russell DW.
  TITLE     The enzymes, regulation, and genetics of bile acid synthesis.
  JOURNAL   Annu. Rev. Biochem. 72 (2003) 137-74.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.2.34
            ExPASy - ENZYME nomenclature database: 2.8.2.34
            ExplorEnz - The Enzyme Database: 2.8.2.34
            ERGO genome analysis and discovery system: 2.8.2.34
            BRENDA, the Enzyme Database: 2.8.2.34
///
ENTRY       EC 2.8.2.-                  Enzyme
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Sulfotransferases
REACTION    2-Aminoacrylate + 3'-Phosphoadenylyl sulfate <=> L-Cysteate +
            Adenosine 3',5'-bisphosphate [RN:R02435]
SUBSTRATE   2-Aminoacrylate [CPD:C02218];
            3'-Phosphoadenylyl sulfate [CPD:C00053]
PRODUCT     L-Cysteate [CPD:C00506];
            Adenosine 3',5'-bisphosphate [CPD:C00054]
///
ENTRY       EC 2.8.3.1                  Enzyme
NAME        propionate CoA-transferase;
            propionate coenzyme A-transferase;
            propionate-CoA:lactoyl-CoA transferase;
            propionyl CoA:acetate CoA transferase;
            propionyl-CoA transferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
SYSNAME     acetyl-CoA:propanoate CoA-transferase
REACTION    acetyl-CoA + propanoate = acetate + propanoyl-CoA [RN:R00928]
ALL_REAC    R00928;
            (other) R01449 R05508
SUBSTRATE   acetyl-CoA [CPD:C00024];
            propanoate [CPD:C00163]
PRODUCT     acetate [CPD:C00033];
            propanoyl-CoA [CPD:C00100]
COMMENT     Butanoate and lactate can also act as acceptors.
REFERENCE   1
  AUTHORS   Stadtman, E.R.
  TITLE     Acyl-coenzyme A synthesis by phosphotransacetylase and coenzyme A
            transphorase.
  JOURNAL   Fed. Proc. 11 (1952) 291.
  ORGANISM  Clostridium kluyveri
PATHWAY     PATH: map00620  Pyruvate metabolism
            PATH: map00640  Propanoate metabolism
            PATH: map00643  Styrene degradation
ORTHOLOGY   KO: K01026  propionate CoA-transferase
GENES       ECC: c5024
            ECV: APECO1_770(ydiF)
            REH: H16_A2718(pct)
            SAT: SYN_02597
            RLE: RL1821 pRL100119 pRL120745(pct)
            RDE: RD1_0510(pct)
            SAB: SAB0174c
            LMF: LMOf2365_2204(pct)
            LWE: lwe2190(pct)
            CPF: CPF_0091
            FNU: FN0814
            APE: APE_2468.1
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.1
            ExPASy - ENZYME nomenclature database: 2.8.3.1
            ExplorEnz - The Enzyme Database: 2.8.3.1
            ERGO genome analysis and discovery system: 2.8.3.1
            UM-BBD (Biocatalysis/Biodegradation Database): 2.8.3.1
            BRENDA, the Enzyme Database: 2.8.3.1
            CAS: 9026-15-7
///
ENTRY       EC 2.8.3.2                  Enzyme
NAME        oxalate CoA-transferase;
            succinyl---beta-ketoacyl-CoA transferase;
            oxalate coenzyme A-transferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
SYSNAME     succinyl-CoA:oxalate CoA-transferase
REACTION    succinyl-CoA + oxalate = succinate + oxalyl-CoA [RN:R01559]
ALL_REAC    R01559
SUBSTRATE   succinyl-CoA [CPD:C00091];
            oxalate [CPD:C00209]
PRODUCT     succinate [CPD:C00042];
            oxalyl-CoA [CPD:C00313]
REFERENCE   1  [PMID:16748872]
  AUTHORS   Quayle JR, Keech DB, Taylor GA.
  TITLE     Carbon assimilation by Pseudomonas oxalaticus (OXI). 4. Metabolism
            of oxalate in cell-free extracts of the organism grown on oxalate.
  JOURNAL   Biochem. J. 78 (1961) 225-36.
  ORGANISM  Pseudomonas oxalaticus
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.2
            ExPASy - ENZYME nomenclature database: 2.8.3.2
            ExplorEnz - The Enzyme Database: 2.8.3.2
            ERGO genome analysis and discovery system: 2.8.3.2
            BRENDA, the Enzyme Database: 2.8.3.2
            CAS: 9026-17-9
///
ENTRY       EC 2.8.3.3                  Enzyme
NAME        malonate CoA-transferase;
            malonate coenzyme A-transferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
SYSNAME     acetyl-CoA:malonate CoA-transferase
REACTION    acetyl-CoA + malonate = acetate + malonyl-CoA [RN:R00743]
ALL_REAC    R00743
SUBSTRATE   acetyl-CoA [CPD:C00024];
            malonate [CPD:C00383]
PRODUCT     acetate [CPD:C00033];
            malonyl-CoA [CPD:C00083]
COMMENT     The enzyme from Pseudomonas ovalis also catalyses the reaction of EC
            4.1.1.9 malonyl-CoA decarboxylase.
REFERENCE   1  [PMID:14392148]
  AUTHORS   HAYAISHI O.
  TITLE     Enzymatic decarboxylation of malonic acid.
  JOURNAL   J. Biol. Chem. 215 (1955) 125-36.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   2
  AUTHORS   Takamura, Y. and Kitayama, Y.
  TITLE     Purification and some properties of malonate decarboxylase from
            Pseudomonas ovalis: an oligomeric enzyme with bifunctional
            properties.
  JOURNAL   Biochem. Int. 3 (1981) 483-491.
  ORGANISM  Pseudomonas ovalis
PATHWAY     PATH: map00410  beta-Alanine metabolism
            PATH: map00640  Propanoate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.3
            ExPASy - ENZYME nomenclature database: 2.8.3.3
            ExplorEnz - The Enzyme Database: 2.8.3.3
            ERGO genome analysis and discovery system: 2.8.3.3
            BRENDA, the Enzyme Database: 2.8.3.3
            CAS: 9026-18-0
///
ENTRY       EC 2.8.3.4        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
COMMENT     Deleted entry: butyrate CoA-transferase (EC 2.8.3.4 created 1961,
            deleted 1964)
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.4
            ExPASy - ENZYME nomenclature database: 2.8.3.4
            ExplorEnz - The Enzyme Database: 2.8.3.4
            ERGO genome analysis and discovery system: 2.8.3.4
            BRENDA, the Enzyme Database: 2.8.3.4
///
ENTRY       EC 2.8.3.5                  Enzyme
NAME        3-oxoacid CoA-transferase;
            3-oxoacid coenzyme A-transferase;
            3-ketoacid CoA-transferase;
            3-ketoacid coenzyme A transferase;
            3-oxo-CoA transferase;
            3-oxoacid CoA dehydrogenase;
            acetoacetate succinyl-CoA transferase;
            acetoacetyl coenzyme A-succinic thiophorase;
            succinyl coenzyme A-acetoacetyl coenzyme A-transferase;
            succinyl-CoA transferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
SYSNAME     succinyl-CoA:3-oxo-acid CoA-transferase
REACTION    succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA
            [RN:R01780]
ALL_REAC    R01780 > R00410
SUBSTRATE   succinyl-CoA [CPD:C00091];
            3-oxo acid [CPD:C01656]
PRODUCT     succinate [CPD:C00042];
            3-oxoacyl-CoA [CPD:C00264]
COMMENT     Acetoacetate and, more slowly, 3-oxopropanoate, 3-oxopentanoate,
            3-oxo-4-methylpentanoate or 3-oxohexanoate can act as acceptors;
            malonyl-CoA can act instead of succinyl-CoA.
REFERENCE   1
  AUTHORS   Hersh, L.B. and Jencks, W.P.
  TITLE     Coenzyme A transferase. Kinetics and exchange reactions.
  JOURNAL   J. Biol. Chem. 242 (1967) 3468-3480.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:13115439]
  AUTHORS   LYNEN F, OCHOA S.
  TITLE     Enzymes of fatty acid metabolism.
  JOURNAL   Biochim. Biophys. Acta. 12 (1953) 299-314.
  ORGANISM  Clostridiurn kluyveri
REFERENCE   3
  AUTHORS   Menon, G.K.K. and Stern, J.R.
  TITLE     Enzymic synthesis and metabolism of malonyl coenzyme A and glutaryl
            coenzyme A.
  JOURNAL   J. Biol. Chem. 235 (1960) 3393-3398.
  ORGANISM  pig [GN:ssc]
REFERENCE   4
  AUTHORS   Stern, J.R., Coon, M.J., del Campillo, A. and Schneider, M.C.
  TITLE     Enzymes of fatty acid metabolism. IV. Preparation and properties of
            coenzyme A transferase.
  JOURNAL   J. Biol. Chem. 221 (1956) 15-31.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00072  Synthesis and degradation of ketone bodies
            PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K01027  3-oxoacid CoA-transferase
            KO: K01028  3-oxoacid CoA-transferase subunit A
            KO: K01029  3-oxoacid CoA-transferase subunit B
GENES       HSA: 5019(OXCT1) 64064(OXCT2)
            MMU: 64059(Oxct2a) 67041(Oxct1)
            SSC: 396978(OXCT)
            GGA: 427190(OXCT1)
            XLA: 398820(MGC69180)
            XTR: 493307(oxct1)
            SPU: 589818(LOC589818)
            DME: Dmel_CG1140
            CEL: C05C10.3
            PIC: PICST_33142(OCA3)
            CAL: CaO19.2281
            ANI: AN5669.2
            AFM: AFUA_3G04030 AFUA_6G12250
            AOR: AO090009000195 AO090124000071
            CNE: CNL05860
            UMA: UM02667.1
            DDI: DDBDRAFT_0187790
            TET: TTHERM_00442180
            TBR: Tb11.02.0290
            TCR: 504153.360 506301.50
            LMA: LmjF30.1940 LmjF33.2340
            SSN: SSON_2280(atoD) SSON_2281(atoA)
            SPE: Spro_0590 Spro_0591 Spro_3037
            XCC: XCC0627(ipsI) XCC0628(ipsJ)
            XCB: XC_3606 XC_3607
            XCV: XCV3701(wxcJ) XCV3702(wxcI)
            XAC: XAC3577(ipsJ) XAC3578(ipsI)
            XOO: XOO0798(ipsI) XOO0799(ipsJ)
            XOM: XOO_0726(XOO0726) XOO_0727(XOO0727)
            PAE: PA1999 PA2000
            PAU: PA14_38640(scoB) PA14_38660(scoA)
            PPU: PP_3122 PP_3123
            PPF: Pput_1871 Pput_2593 Pput_2594 Pput_5289
            PST: PSPTO_3455 PSPTO_3456
            PSB: Psyr_3237 Psyr_3238
            PFL: PFL_2322 PFL_2323
            PFO: Pfl_2075 Pfl_2076
            PEN: PSEEN2464(lpsI) PSEEN2465(lpsJ)
            PMY: Pmen_1139 Pmen_1140
            PAR: Psyc_1429 Psyc_1430(lpsI)
            PCR: Pcryo_1593 Pcryo_1594
            PRW: PsycPRwf_1705 PsycPRwf_1706
            SON: SO_1891 SO_1892(atoD)
            SDN: Sden_2251 Sden_2252
            SFR: Sfri_2732 Sfri_2733
            SAZ: Sama_0518 Sama_0519 Sama_1356 Sama_1357
            SBL: Sbal_2833 Sbal_2834
            SBM: Shew185_2851 Shew185_2852
            SLO: Shew_2575 Shew_2576
            SPC: Sputcn32_1713 Sputcn32_1714
            SSE: Ssed_1452 Ssed_1453 Ssed_3710
            SPL: Spea_2803 Spea_2804
            SHE: Shewmr4_2327 Shewmr4_2328 Shewmr4_3291 Shewmr4_3292
            SHM: Shewmr7_0655 Shewmr7_0656 Shewmr7_2399 Shewmr7_2400
            SHN: Shewana3_1666 Shewana3_1667 Shewana3_3467 Shewana3_3468
            SHW: Sputw3181_2311 Sputw3181_2312
            CPS: CPS_1597(dxnH) CPS_1598(dxnG)
            PHA: PSHAa1446(atoA) PSHAa1447 PSHAa2942 PSHAa2943
            PAT: Patl_1619 Patl_1620
            MMW: Mmwyl1_3054 Mmwyl1_3055
            RSO: RSc1570(lpsI) RSc1571(lpsJ)
            REU: Reut_A1269 Reut_A1270 Reut_B4483
            REH: H16_A1331 H16_A1332
            RME: Rmet_1153 Rmet_1154
            BMA: BMA1107 BMA1108
            BXE: Bxe_A1366 Bxe_A1367 Bxe_C0572
            BVI: Bcep1808_1430 Bcep1808_1431
            BUR: Bcep18194_A4610 Bcep18194_A4611
            BCN: Bcen_0983 Bcen_0984
            BCH: Bcen2424_1465 Bcen2424_1466
            BAM: Bamb_1350 Bamb_1351
            BPS: BPSL1954(scoB) BPSL1955(scoA)
            BPM: BURPS1710b_1877(scoA) BURPS1710b_1878(scoB)
            BPD: BURPS668_1700
            BTE: BTH_I2607 BTH_I2608
            PNU: Pnuc_0825 Pnuc_0826
            BPE: BP2400
            BPA: BPP0358(scoB) BPP0359(scoA) BPP3265 BPP3266
            BBR: BB0361(scoB) BB0362(scoA) BB3717
            RFR: Rfer_2634 Rfer_2635
            POL: Bpro_1905 Bpro_1906
            PNA: Pnap_2657 Pnap_2658
            AAV: Aave_3126 Aave_3127
            AJS: Ajs_1961 Ajs_1962
            VEI: Veis_2607 Veis_2608
            MPT: Mpe_A1456 Mpe_A1457
            HAR: HEAR1806(atoA) HEAR1807(lpsI)
            MMS: mma_1481(scoA)
            EBA: ebA4718(kctA) ebA4719(kctB)
            DAR: Daro_1021
            HPY: HP0691(yxjD) HP0692(yxjE)
            HPJ: jhp0636(scoB) jhp0637(scoA)
            HPA: HPAG1_0676 HPAG1_0677
            HAC: Hac_0956(scoB) Hac_0957(scoA)
            GME: Gmet_3296 Gmet_3297
            GUR: Gura_4355 Gura_4356
            BBA: Bd2096 Bd2097
            ADE: Adeh_2363 Adeh_2364
            AFW: Anae109_1505 Anae109_1506
            MXA: MXAN_3789 MXAN_3790
            SFU: Sfum_2290
            RCO: RC0904 RC0905 RC0906(scoB)
            RFE: RF_0373(scoB) RF_0374(scoA)
            RBE: RBE_1007(scoB)
            SMD: Smed_5092
            OAN: Oant_3720
            RPC: RPC_0638
            RPE: RPE_4077 RPE_4078
            NWI: Nwi_1010 Nwi_1011
            NHA: Nham_1246
            XAU: Xaut_1120 Xaut_2349 Xaut_2350
            SIT: TM1040_2340 TM1040_2341
            RSP: RSP_1914
            RSH: Rsph17029_0563 Rsph17029_0564
            RSQ: Rsph17025_3108 Rsph17025_3109
            JAN: Jann_1005 Jann_1009
            PDE: Pden_4683 Pden_4684 Pden_5021
            MMR: Mmar10_1476 Mmar10_1477
            HNE: HNE_2893(dxnH)
            NAR: Saro_0566 Saro_0568
            SAL: Sala_2123 Sala_2124
            SWI: Swit_0958 Swit_0959 Swit_4164 Swit_4165 Swit_4338 Swit_4888
                 Swit_4889 Swit_5023 Swit_5064
            ELI: ELI_14300 ELI_14310
            ACR: Acry_1846 Acry_2257 Acry_2258
            ABA: Acid345_1163 Acid345_1164
            BSU: BG11153(scoA) BG11154(scoB)
            BCY: Bcer98_1684
            BCL: ABC4024(scoE) ABC4025(scoA)
            BAY: RBAM_018210(scoB) RBAM_018220(scoA)
            SSP: SSP2199 SSP2200
            SPI: MGAS10750_Spy0126
            SPB: M28_Spy0119
            MTU: Rv2503c(scoB) Rv2504c(scoA)
            MTC: MT2578(scoB) MT2579(scoA)
            MBO: Mb2531c(scoB)
            MBB: BCG_2523c(scoB)
            MPA: MAP3861(scoB)
            MAV: MAV_4786
            MSM: MSMEG_1898 MSMEG_1899
            MVA: Mvan_4892 Mvan_4893
            MGI: Mflv_1349 Mflv_1350
            MMC: Mmcs_1368 Mmcs_1369
            MKM: Mkms_1386 Mkms_1387
            MJL: Mjls_1402 Mjls_1403
            CGL: NCgl2306(cgl2389) NCgl2307(cgl2390)
            CGB: cg2622(scoB) cg2623(scoA)
            CEF: CE0326 CE1268 CE1269 CE2292 CE2293
            CJK: jk1544(scoB) jk1545(scoA)
            RHA: RHA1_ro01334(pcaI) RHA1_ro03780(pcaJ2) RHA1_ro03781(pcaI1)
                 RHA1_ro03893(pcaJ3) RHA1_ro03894(pcaI2)
            SCO: SCO6702(pcaJ) SCO6703(pcaI)
            SMA: SAV1700(scoA) SAV1701(scoB)
            ART: Arth_0490 Arth_0491 Arth_1388 Arth_1389
            NCA: Noca_0330 Noca_0331
            FRA: Francci3_2503 Francci3_2504
            FAL: FRAAL2504(atoA) FRAAL2505(atoD) FRAAL3148(scoA)
                 FRAAL3149(atoA)
            KRA: Krad_2883
            LIL: LA1424(scoA)
            GFO: GFO_3238(scoB) GFO_3240(scoA)
            FJO: Fjoh_0887 Fjoh_0888
            FPS: FP0026(atoD) FP0030(atoA)
            DRA: DR_A0054 DR_A0067 DR_A0068
            DGE: Dgeo_0808 Dgeo_0809 Dgeo_1306
            NPH: NP6032A NP6034A
STRUCTURES  PDB: 1M3E  1O9L  1OOY  1OOZ  1OPE  2NRB  2NRC  
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.5
            ExPASy - ENZYME nomenclature database: 2.8.3.5
            ExplorEnz - The Enzyme Database: 2.8.3.5
            ERGO genome analysis and discovery system: 2.8.3.5
            BRENDA, the Enzyme Database: 2.8.3.5
            CAS: 9027-43-4
///
ENTRY       EC 2.8.3.6                  Enzyme
NAME        3-oxoadipate CoA-transferase;
            3-oxoadipate coenzyme A-transferase;
            3-oxoadipate succinyl-CoA transferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
SYSNAME     succinyl-CoA:3-oxoadipate CoA-transferase
REACTION    succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA
            [RN:R02990]
ALL_REAC    R02990
SUBSTRATE   succinyl-CoA [CPD:C00091];
            3-oxoadipate [CPD:C00846]
PRODUCT     succinate [CPD:C00042];
            3-oxoadipyl-CoA [CPD:C02232]
REFERENCE   1  [PMID:13428776]
  AUTHORS   KATAGIRI M, HAYAISHI O.
  TITLE     Enzymatic degradation of beta-ketoadipic acid.
  JOURNAL   J. Biol. Chem. 226 (1957) 439-48.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
ORTHOLOGY   KO: K01030  3-oxoadipate CoA-transferase
            KO: K01031  3-oxoadipate CoA-transferase, alpha subunit
            KO: K01032  3-oxoadipate CoA-transferase, beta subunit
GENES       PIC: PICST_33142(OCA3)
            CAL: CaO19.2281
            ECW: EcE24377A_1670(pcaI)
            ECX: EcHS_A2362
            SPE: Spro_3038
            PPU: PP_3951(pcaI) PP_3952(pcaJ)
            PPF: Pput_1870 Pput_5290
            PSP: PSPPH_3156(dxnG) PSPPH_3157(dxnH) PSPPH_4018(catJ)
                 PSPPH_4019(catI)
            PFL: PFL_1317(catI) PFL_1318(catJ)
            PFO: Pfl_1267 Pfl_1268
            PEN: PSEEN1163(catI) PSEEN1164(catJ)
            PCR: Pcryo_1261 Pcryo_1262
            ACI: ACIAD1448(catI) ACIAD1449(catJ) ACIAD1695(dcaI)
                 ACIAD1696(dcaJ) ACIAD1704(pcaI) ACIAD1705(pcaJ)
            SSE: Ssed_3709
            CPS: CPS_3592(pcaJ)
            RSO: RSc2253(pcaJ) RSc2254(pcaI)
            REU: Reut_A1505 Reut_A1506 Reut_B5585 Reut_B5586
            REH: H16_B0198(pcaI) H16_B0199(pcaJ)
            RME: Rmet_3667 Rmet_3668 Rmet_5059 Rmet_5060
            BMA: BMAA0046(pcaI) BMAA0047
            BMV: BMASAVP1_1200(pcaI)
            BML: BMA10299_1483(pcaI)
            BMN: BMA10247_A0056(pcaI)
            BXE: Bxe_B0643(pcaI) Bxe_B0644(pcaJ) Bxe_C0573
            BVI: Bcep1808_3742 Bcep1808_3743
            BUR: Bcep18194_B3128 Bcep18194_B3129
            BCN: Bcen_5112 Bcen_5113
            BCH: Bcen2424_5746 Bcen2424_5747
            BAM: Bamb_5017 Bamb_5018
            BPS: BPSS0043(pcaI) BPSS0044(pcaJ)
            BPM: BURPS1710b_A1552(pcaI) BURPS1710b_A1554(pcaJ)
            BPL: BURPS1106A_A0054(pcaI) BURPS1106A_A0055(pcaJ)
            BPD: BURPS668_A0067(pcaI) BURPS668_A0068(pcaJ)
            BTE: BTH_II0046 BTH_II0047
            PNU: Pnuc_1503 Pnuc_1504
            BPE: BP0221(catI) BP0222(catJ) BP1788(pcaI) BP1789(pcaJ)
            BPA: BPP0411(catJ) BPP0412(catI) BPP2019(pcaI) BPP2020(pcaJ)
            BBR: BB0413(catJ) BB0414(catI) BB2267(pcaI) BB2268(pcaJ)
            RFR: Rfer_1035 Rfer_1036
            POL: Bpro_1229 Bpro_1230
            PNA: Pnap_0865 Pnap_0866
            AAV: Aave_3945 Aave_3946
            AJS: Ajs_3549 Ajs_3550
            VEI: Veis_4026 Veis_4621
            SMD: Smed_5093
            ATU: Atu4547(pcaI) Atu4548(pcaJ)
            ATC: AGR_L_1055GM AGR_L_642
            RET: RHE_PE00201(pcaI) RHE_PE00202(pcaJ)
            RLE: pRL110287(pcaI) pRL110288(pcaJ)
            BME: BMEII0643 BMEII0644 BMEII0645
            BMF: BAB2_0604(pcaI) BAB2_0605(pcaJ)
            BMS: BRA0637(pcaJ) BRA0638(pcaI)
            BMB: BruAb2_0588(pcaI) BruAb2_0589(pcaJ)
            BOV: BOV_A0600(pcaI)
            OAN: Oant_3719
            BJA: bll7092(pcaJ) bll7093(pcaI)
            RPA: RPA4155 RPA4156
            RPB: RPB_1458 RPB_1459
            RPC: RPC_1076 RPC_1077 RPC_3949 RPC_3950
            RPD: RPD_1434 RPD_1435
            NHA: Nham_1247
            XAU: Xaut_1119
            CCR: CC_0206 CC_0207 CC_2405 CC_2406
            SIL: SPO3082(dxnG) SPO3083(dxnH)
            RSP: RSP_1913
            RDE: RD1_2128(dxnH) RD1_2130(dxnG)
            PDE: Pden_5020
            HNE: HNE_2894(dxnG)
            SWI: Swit_4337
            ACR: Acry_1845
            MBO: Mb2532c(scoA)
            MBB: BCG_2524c(scoA)
            MVA: Mvan_0564 Mvan_0565 Mvan_4403
            MGI: Mflv_0525 Mflv_0526
            MMC: Mmcs_1702 Mmcs_1703
            MKM: Mkms_1730 Mkms_1731 Mkms_1746 Mkms_1747
            MJL: Mjls_1680 Mjls_1681
            RHA: RHA1_ro01333(pcaJ1)
            ART: Arth_4071 Arth_4072
            AAU: AAur_0471 AAur_0472 AAur_4037 AAur_4038
            NCA: Noca_1014 Noca_1015
            SEN: SACE_3515(catJ) SACE_3516(catI) SACE_4008(catI)
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.6
            ExPASy - ENZYME nomenclature database: 2.8.3.6
            ExplorEnz - The Enzyme Database: 2.8.3.6
            ERGO genome analysis and discovery system: 2.8.3.6
            UM-BBD (Biocatalysis/Biodegradation Database): 2.8.3.6
            BRENDA, the Enzyme Database: 2.8.3.6
            CAS: 9026-16-8
///
ENTRY       EC 2.8.3.7                  Enzyme
NAME        succinate---citramalate CoA-transferase;
            itaconate CoA-transferase;
            citramalate CoA-transferase;
            citramalate coenzyme A-transferase;
            succinyl coenzyme A-citramalyl coenzyme A transferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
SYSNAME     succinyl-CoA:citramalate CoA-transferase
REACTION    succinyl-CoA + citramalate = succinate + citramalyl-CoA [RN:R02956]
ALL_REAC    R02956 > R03154;
            (other) R02407
SUBSTRATE   succinyl-CoA [CPD:C00091];
            citramalate [CPD:C00815]
PRODUCT     succinate [CPD:C00042];
            citramalyl-CoA [CPD:C00904]
COMMENT     Itaconate can also act as acceptor.
REFERENCE   1  [PMID:4284209]
  AUTHORS   Cooper RA, Kornberg HL.
  TITLE     The utilization of itaconate by Pseudomonas sp.
  JOURNAL   Biochem. J. 91 (1964) 82-91.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00660  C5-Branched dibasic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.7
            ExPASy - ENZYME nomenclature database: 2.8.3.7
            ExplorEnz - The Enzyme Database: 2.8.3.7
            ERGO genome analysis and discovery system: 2.8.3.7
            BRENDA, the Enzyme Database: 2.8.3.7
            CAS: 9033-60-7
///
ENTRY       EC 2.8.3.8                  Enzyme
NAME        acetate CoA-transferase;
            acetate coenzyme A-transferase;
            butyryl CoA:acetate CoA transferase;
            butyryl coenzyme A transferase;
            succinyl-CoA:acetate CoA transferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
SYSNAME     acyl-CoA:acetate CoA-transferase
REACTION    acyl-CoA + acetate = a fatty acid anion + acetyl-CoA [RN:R00393]
ALL_REAC    R00393 > R01179 R01359 R07832
SUBSTRATE   acyl-CoA [CPD:C00040];
            acetate [CPD:C00033]
PRODUCT     fatty acid anion [CPD:C02403];
            acetyl-CoA [CPD:C00024]
COMMENT     Acts on butanoyl-CoA and pentanoyl-CoA.
REFERENCE   1  [PMID:4884054]
  AUTHORS   Vanderwinkel E, Furmanski P, Reeves HC, Ajl SJ.
  TITLE     Growth of Escherichia coli on fatty acids: requirement for coenzyme
            A transferase activity.
  JOURNAL   Biochem. Biophys. Res. Commun. 33 (1968) 902-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:11741862]
  AUTHORS   Kaschabek SR, Kuhn B, Muller D, Schmidt E, Reineke W.
  TITLE     Degradation of aromatics and chloroaromatics by Pseudomonas sp.
            strain B13: purification and characterization of
            3-oxoadipate:succinyl-coenzyme A (CoA) transferase and
            3-oxoadipyl-CoA thiolase.
  JOURNAL   J. Bacteriol. 184 (2002) 207-15.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:11741863]
  AUTHORS   Gobel M, Kassel-Cati K, Schmidt E, Reineke W.
  TITLE     Degradation of aromatics and chloroaromatics by Pseudomonas sp.
            strain B13: cloning, characterization, and analysis of sequences
            encoding 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and
            3-oxoadipyl-CoA thiolase.
  JOURNAL   J. Bacteriol. 184 (2002) 216-23.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
            PATH: map00640  Propanoate metabolism
            PATH: map00650  Butanoate metabolism
            PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K01033  acetate CoA-transferase
            KO: K01034  acetate CoA-transferase alpha subunit
            KO: K01035  acetate CoA-transferase beta subunit
GENES       ECO: b2221(atoD) b2222(atoA)
            ECJ: JW2215(atoD) JW2216(atoA)
            ECC: c2764(atoD) c2765(atoA)
            ECI: UTI89_C2503(atoD) UTI89_C2504(atoA)
            ECP: ECP_2266
            ECV: APECO1_4337(atoA) APECO1_4338(atoD)
            ECA: ECA1283(atoA) ECA1284(atoD)
            PLU: plu3799(atoD) plu3800(atoA)
            HIN: HI0773(atoA) HI0774(atoD)
            HIT: NTHI0934(atoA) NTHI0935(atoD)
            ACI: ACIAD2513(atoD) ACIAD2514(atoA)
            CPS: CPS_3591(pcaI)
            BBA: Bd1620
            SFU: Sfum_2291
            BME: BMEI0928
            BJA: bll3461(pcaJ)
            RPC: RPC_0637 RPC_0829 RPC_2003
            NHA: Nham_0867 Nham_0868
            RRU: Rru_A1383 Rru_A1472
            BCA: BCE_2329(atoD)
            BCZ: BCZK2074(atoD) BCZK2075(atoA)
            BCY: Bcer98_1683
            BTK: BT9727_2078(atoD) BT9727_2079(atoA)
            BPU: BPUM_0613 BPUM_0614(yodR)
            SPY: SPy_0141(atoD.2) SPy_0142 SPy_1638(atoD.1) SPy_1639(atoA)
            SPZ: M5005_Spy_0120(atoD.2) M5005_Spy_1345(atoD.1)
                 M5005_Spy_1346(atoA)
            SPM: spyM18_0137 spyM18_0138 spyM18_1646(atoD) spyM18_1647(atoA)
            SPG: SpyM3_0109(atoD.2) SpyM3_0110 SpyM3_1379(atoD.1)
                 SpyM3_1380(atoA)
            SPS: SPs0111 SPs0112 SPs0482 SPs0483
            SPH: MGAS10270_Spy0122(atoD2) MGAS10270_Spy0123
                 MGAS10270_Spy1462(atoD1) MGAS10270_Spy1463(atoA)
            SPI: MGAS10750_Spy0125(atoD2) MGAS10750_Spy1454(atoD1)
                 MGAS10750_Spy1455(atoA)
            SPJ: MGAS2096_Spy0124(atoD2) MGAS2096_Spy0125
                 MGAS2096_Spy1366(atoD1) MGAS2096_Spy1367(atoA)
            SPK: MGAS9429_Spy0122(atoD2) MGAS9429_Spy0123
                 MGAS9429_Spy1340(atoD1) MGAS9429_Spy1341(atoA)
            SPF: SpyM50446(atoD2)
            SPA: M6_Spy0167 M6_Spy0168 M6_Spy1391 M6_Spy1392
            SPB: M28_Spy0118(atoD.2) M28_Spy1386(atoD.1) M28_Spy1387(atoA)
            CBO: CBO2847(ctfA) CBO2848(ctfB)
            CKL: CKL_3595(cat3)
            TTE: TTE0720(atoD) TTE0721(atoA)
            CGL: NCgl0485(cgl0503)
            CGB: cg0592 cg2840(actA)
            PGI: PG1066(ctfA) PG1075
            TME: Tmel_1136
            FNO: Fnod_0212
STRUCTURES  PDB: 1K6D  
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.8
            ExPASy - ENZYME nomenclature database: 2.8.3.8
            ExplorEnz - The Enzyme Database: 2.8.3.8
            ERGO genome analysis and discovery system: 2.8.3.8
            UM-BBD (Biocatalysis/Biodegradation Database): 2.8.3.8
            BRENDA, the Enzyme Database: 2.8.3.8
            CAS: 37278-35-6
///
ENTRY       EC 2.8.3.9                  Enzyme
NAME        butyrate---acetoacetate CoA-transferase;
            butyryl coenzyme A-acetoacetate coenzyme A-transferase;
            butyryl-CoA-acetoacetate CoA-transferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
SYSNAME     butanoyl-CoA:acetoacetate CoA-transferase
REACTION    butanoyl-CoA + acetoacetate = butanoate + acetoacetyl-CoA
            [RN:R01365]
ALL_REAC    R01365
SUBSTRATE   butanoyl-CoA [CPD:C00136];
            acetoacetate [CPD:C00164]
PRODUCT     butanoate [CPD:C00246];
            acetoacetyl-CoA [CPD:C00332]
COMMENT     Butanoate, acetoacetate and their CoA thioesters are the preferred
            substrates, but the enzyme also acts, more slowly, on the
            derivatives of a number of C2 to C6 monocarboxylic acids.
REFERENCE   1  [PMID:624727]
  AUTHORS   Barker HA, Jeng IM, Neff N, Robertson JM, Tam FK, Hosaka S.
  TITLE     Butyryl-CoA:acetoacetate CoA-transferase from a lysine-fermenting
            Clostridium.
  JOURNAL   J. Biol. Chem. 253 (1978) 1219-25.
  ORGANISM  Ctostridium sp., Clostridiurn sticklandii
ORTHOLOGY   KO: K01036  butyrate-acetoacetate CoA-transferase
GENES       PIC: PICST_33142(OCA3)
            CAL: CaO19.2281
            RPC: RPC_0830 RPC_2004
            RRU: Rru_A1382 Rru_A1471
            OIH: OB2633 OB2634
            CAC: CA_P0163(ctfA) CA_P0164(ctfB)
            CDF: CD2677(ctfA) CD2678(ctfB)
            CBE: Cbei_2653 Cbei_2654 Cbei_3833 Cbei_3834
            AMT: Amet_4246 Amet_4247
            FNU: FN0272 FN0273 FN1856 FN1857
            TME: Tmel_1135
            FNO: Fnod_0211
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.9
            ExPASy - ENZYME nomenclature database: 2.8.3.9
            ExplorEnz - The Enzyme Database: 2.8.3.9
            ERGO genome analysis and discovery system: 2.8.3.9
            BRENDA, the Enzyme Database: 2.8.3.9
            CAS: 66231-37-6
///
ENTRY       EC 2.8.3.10                 Enzyme
NAME        citrate CoA-transferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
SYSNAME     acetyl-CoA:citrate CoA-transferase
REACTION    acetyl-CoA + citrate = acetate + (3S)-citryl-CoA [RN:R01323]
ALL_REAC    R01323
SUBSTRATE   acetyl-CoA [CPD:C00024];
            citrate [CPD:C00158]
PRODUCT     acetate [CPD:C00033];
            (3S)-citryl-CoA [CPD:C00566]
COMMENT     The enzyme is a component of EC 4.1.3.6 [citrate (pro-3S)-lyase].
            Also catalyses the transfer of thioacyl carrier protein from its
            acetyl thioester to citrate.
REFERENCE   1  [PMID:336371]
  AUTHORS   Dimroth P, Loyal R, Eggerer H.
  TITLE     Characterization of the isolated transferase subunit of citrate
            lyase as a CoA-Transferase. Evidence against a covalent
            enzyme-substrate intermediate.
  JOURNAL   Eur. J. Biochem. 80 (1977) 479-88.
  ORGANISM  Klebsiellu aerogenes
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
ORTHOLOGY   KO: K01037  citrate CoA-transferase
GENES       ECO: b0615(citF)
            ECJ: JW5087(citF)
            ECE: Z0759(citF)
            ECS: ECs0654
            ECC: c0704(citF)
            ECI: UTI89_C0618(citF)
            ECP: ECP_0646
            ECV: APECO1_1436(citF)
            ECW: EcE24377A_0637(citF)
            ECX: EcHS_A0666(citF)
            STY: STY0670(citF)
            STT: t2246(citF)
            SPT: SPA2113(citF)
            SEC: SC0650(citF)
            STM: STM0621(citF)
            SFL: SF0532(citF)
            SFX: S0539(citF)
            SFV: SFV_0568(citF)
            SSN: SSON_0567(citF)
            SBO: SBO_0480(citF)
            SPE: Spro_3168
            HIN: HI0022(citF)
            HIT: NTHI0029(citF)
            HDU: HD1243(citF)
            ASU: Asuc_1196
            VCH: VC0799
            PPR: PBPRA2292(citF)
            PPD: Ppro_1084
            LLA: L0041(citF)
            SPY: SPy_1189(citF)
            SPZ: M5005_Spy_0907(citF)
            SPM: spyM18_1140(citF)
            SPG: SpyM3_0834(citF)
            SPS: SPs1034
            SPH: MGAS10270_Spy1021(citF)
            SPI: MGAS10750_Spy1057(citF)
            SPF: SpyM50890(citF)
            SPA: M6_Spy0896
            SPB: M28_Spy0880(citF)
            SMU: SMU.1021(cilA)
            LPL: lp_1109(citF)
            LAC: LBA0917(citF)
            LSA: LSA1224(citF)
            LCA: LSEI_1857
            EFA: EF3319(citF)
            OOE: OEOE_0423
            CPE: CPE1149(cilA)
            CPR: CPR_1165(citF)
            CTC: CTC02559
            AMT: Amet_3223 Amet_3409
            DSY: DSY3038
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.10
            ExPASy - ENZYME nomenclature database: 2.8.3.10
            ExplorEnz - The Enzyme Database: 2.8.3.10
            ERGO genome analysis and discovery system: 2.8.3.10
            BRENDA, the Enzyme Database: 2.8.3.10
            CAS: 65187-14-6
///
ENTRY       EC 2.8.3.11                 Enzyme
NAME        citramalate CoA-transferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
SYSNAME     acetyl-CoA:citramalate CoA-transferase
REACTION    acetyl-CoA + citramalate = acetate + (3S)-citramalyl-CoA [RN:R02955]
ALL_REAC    R02955 > R03153
SUBSTRATE   acetyl-CoA [CPD:C00024];
            citramalate [CPD:C00815]
PRODUCT     acetate [CPD:C00033];
            (3S)-citramalyl-CoA [CPD:C01011]
COMMENT     The enzyme is a component of EC 4.1.3.22 citramalate lyase. Also
            catalyses the transfer of thioacyl carrier protein from its acetyl
            thioester to citramalate.
REFERENCE   1  [PMID:923590]
  AUTHORS   Dimroth P, Buckel W, Loyal R, Eggerer H.
  TITLE     Isolation and function of the subunits of citramalate lyase and
            formation of hybrids with the subunits of citrate lyase.
  JOURNAL   Eur. J. Biochem. 80 (1977) 469-77.
  ORGANISM  Clostridium tetanomorphum
PATHWAY     PATH: map00660  C5-Branched dibasic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.11
            ExPASy - ENZYME nomenclature database: 2.8.3.11
            ExplorEnz - The Enzyme Database: 2.8.3.11
            ERGO genome analysis and discovery system: 2.8.3.11
            BRENDA, the Enzyme Database: 2.8.3.11
            CAS: 9033-60-7
///
ENTRY       EC 2.8.3.12                 Enzyme
NAME        glutaconate CoA-transferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
SYSNAME     acetyl-CoA:(E)-glutaconate CoA-transferase
REACTION    acetyl-CoA + (E)-glutaconate = acetate + glutaconyl-1-CoA
            [RN:R03884]
ALL_REAC    R03884;
            (other) R04000 R05509
SUBSTRATE   acetyl-CoA [CPD:C00024];
            (E)-glutaconate [CPD:C02214]
PRODUCT     acetate [CPD:C00033];
            glutaconyl-1-CoA [CPD:C02411]
COMMENT     Glutarate, (R)-2-hydroxyglutarate, propenoate and propanoate, but
            not (Z)-glutaconate, can also act as acceptors.
REFERENCE   1  [PMID:6945182]
  AUTHORS   Buckel W, Dorn U, Semmler R.
  TITLE     Glutaconate CoA-transferase from Acidaminococcus fermentans.
  JOURNAL   Eur. J. Biochem. 118 (1981) 315-21.
  ORGANISM  Acidaminococcus fermentans
PATHWAY     PATH: map00643  Styrene degradation
            PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K01038  glutaconate CoA-transferase
            KO: K01039  glutaconate CoA-transferase, subunit A
            KO: K01040  glutaconate CoA-transferase, subunit B
GENES       PLU: plu0143
            XCC: XCC0364(gctA)
            XCB: XC_0376
            XCV: XCV0378(gctA)
            XAC: XAC0364(gctA)
            PAE: PA0226
            PST: PSPTO_4309(catI)
            PSB: Psyr_4013
            BXE: Bxe_B1888 Bxe_B1889 Bxe_C1040
            BUR: Bcep18194_B1432
            GUR: Gura_3034 Gura_3035
            MXA: MXAN_4264 MXAN_4265
            SFU: Sfum_0809 Sfum_0810 Sfum_1132
            MLO: mll4183
            MES: Meso_2823
            BJA: bll1293(gctA)
            RPA: RPA1029 RPA2317(gctB) RPA2318(gctA) RPA4651
            RPB: RPB_1076
            RPD: RPD_1203
            DSY: DSY1569 DSY1570
            DRM: Dred_0403 Dred_0404 Dred_1891
            SWO: Swol_1481
            NFA: nfa35190
            RHA: RHA1_ro11179
            ACE: Acel_1644
            SEN: SACE_4007 SACE_4877(gctA)
            RXY: Rxyl_1583 Rxyl_1584
            FNU: FN0202 FN0203
            AFU: AF1199(gctA)
            SSO: SSO1083(gctA) SSO1085(gctB)
            STO: ST0822 ST0823
            SAI: Saci_0366 Saci_0367
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.12
            ExPASy - ENZYME nomenclature database: 2.8.3.12
            ExplorEnz - The Enzyme Database: 2.8.3.12
            ERGO genome analysis and discovery system: 2.8.3.12
            UM-BBD (Biocatalysis/Biodegradation Database): 2.8.3.12
            BRENDA, the Enzyme Database: 2.8.3.12
            CAS: 79078-99-2
///
ENTRY       EC 2.8.3.13                 Enzyme
NAME        succinate---hydroxymethylglutarate CoA-transferase;
            hydroxymethylglutarate coenzyme A-transferase;
            dicarboxyl-CoA:dicarboxylic acid coenzyme A transferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
SYSNAME     succinyl-CoA:3-hydroxy-3-methylglutarate CoA-transferase
REACTION    succinyl-CoA + 3-hydroxy-3-methylglutarate = succinate +
            (S)-3-hydroxy-3-methylglutaryl-CoA [RN:R02084]
ALL_REAC    R02084
SUBSTRATE   succinyl-CoA [CPD:C00091];
            3-hydroxy-3-methylglutarate [CPD:C03761]
PRODUCT     succinate [CPD:C00042];
            (S)-3-hydroxy-3-methylglutaryl-CoA [CPD:C00356]
COMMENT     Malonyl-CoA can also act as donor, but more slowly.
REFERENCE   1  [PMID:6946836]
  AUTHORS   Deana R, Rigoni F, Deana AD, Galzigna L.
  TITLE     Submitochondrial localization and partial purification of the
            succinylCoA: 3-hydroxy-3-methylglutarate coenzyme A transferase from
            rat liver.
  JOURNAL   Biochim. Biophys. Acta. 662 (1981) 119-24.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.13
            ExPASy - ENZYME nomenclature database: 2.8.3.13
            ExplorEnz - The Enzyme Database: 2.8.3.13
            ERGO genome analysis and discovery system: 2.8.3.13
            BRENDA, the Enzyme Database: 2.8.3.13
            CAS: 80237-90-7
///
ENTRY       EC 2.8.3.14                 Enzyme
NAME        5-hydroxypentanoate CoA-transferase;
            5-hydroxyvalerate CoA-transferase;
            5-hydroxyvalerate coenzyme A transferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
SYSNAME     acetyl-CoA:5-hydroxypentanoate CoA-transferase
REACTION    acetyl-CoA + 5-hydroxypentanoate = acetate + 5-hydroxypentanoyl-CoA
            [RN:R04057]
ALL_REAC    R04057
SUBSTRATE   acetyl-CoA [CPD:C00024];
            5-hydroxypentanoate [CPD:C02804]
PRODUCT     acetate [CPD:C00033];
            5-hydroxypentanoyl-CoA [CPD:C03237]
COMMENT     Propanoyl-CoA, acetyl-CoA, butanoyl-CoA and some other acyl-CoAs can
            act as substrates, but more slowly than 5-hydroxypentanoyl-CoA.
REFERENCE   1  [PMID:2085413]
  AUTHORS   Eikmanns U, Buckel W.
  TITLE     Properties of 5-hydroxyvalerate CoA-transferase from Clostridium
            aminovalericum.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 371 (1990) 1077-82.
  ORGANISM  Clostridium aminovalericum
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.14
            ExPASy - ENZYME nomenclature database: 2.8.3.14
            ExplorEnz - The Enzyme Database: 2.8.3.14
            ERGO genome analysis and discovery system: 2.8.3.14
            BRENDA, the Enzyme Database: 2.8.3.14
            CAS: 111684-68-5
///
ENTRY       EC 2.8.3.15                 Enzyme
NAME        succinyl-CoA:(R)-benzylsuccinate CoA-transferase;
            benzylsuccinate CoA-transferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
SYSNAME     succinyl-CoA:(R)-2-benzylsuccinate CoA-transferase
REACTION    succinyl-CoA + (R)-2-benzylsuccinate = succinate +
            (R)-2-benzylsuccinyl-CoA [RN:R05588]
ALL_REAC    R05588
SUBSTRATE   succinyl-CoA [CPD:C00091];
            (R)-2-benzylsuccinate [CPD:C09816]
PRODUCT     succinate [CPD:C00042];
            (R)-2-benzylsuccinyl-CoA [CPD:C09817]
COMMENT     Involved in anaerobic catabolism of toluene and is a strictly
            toluene-induced enzyme that catalyses the reversible regio- and
            enantio-selective synthesis of (R)-2-benzylsuccinyl-CoA. The enzyme
            from Thauera aromatica is inactive when (R)-benzylsuccinate is
            replaced by (S)-benzylsuccinate.
REFERENCE   1  [PMID:11418570]
  AUTHORS   Leutwein C, Heider J.
  TITLE     Succinyl-CoA:(R)-benzylsuccinate CoA-transferase: an enzyme of the
            anaerobic toluene catabolic pathway in denitrifying bacteria.
  JOURNAL   J. Bacteriol. 183 (2001) 4288-95.
  ORGANISM  Thauera aromatica
REFERENCE   2  [PMID:10589736]
  AUTHORS   Leutwein C, Heider J.
  TITLE     Anaerobic toluene-catabolic pathway in denitrifying Thauera
            aromatica: activation and beta-oxidation of the first intermediate,
            (R)-(+)-benzylsuccinate.
  JOURNAL   Microbiology. 145 ( Pt 11) (1999) 3265-71.
  ORGANISM  Thauera aromatica
REFERENCE   3  [PMID:10629170]
  AUTHORS   Leuthner B, Heider J.
  TITLE     Anaerobic toluene catabolism of Thauera aromatica: the bbs operon
            codes for enzymes of beta oxidation of the intermediate
            benzylsuccinate.
  JOURNAL   J. Bacteriol. 182 (2000) 272-7.
  ORGANISM  Thauera aromatica
REFERENCE   4  [PMID:11749953]
  AUTHORS   Heider J.
  TITLE     A new family of CoA-transferases.
  JOURNAL   FEBS. Lett. 509 (2001) 345-9.
  ORGANISM  Thauera aromatica
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
ORTHOLOGY   KO: K07543  benzylsuccinate CoA-transferase BbsE subunit
            KO: K07544  benzylsuccinate CoA-transferase BbsF subunit
            KO: K07551  benzylsuccinate CoA-transferase
GENES       BBR: BB4333(bbsE) BB4334(bbsF)
            EBA: c2A311(bbsF) c2A312(bbsE)
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.15
            ExPASy - ENZYME nomenclature database: 2.8.3.15
            ExplorEnz - The Enzyme Database: 2.8.3.15
            ERGO genome analysis and discovery system: 2.8.3.15
            BRENDA, the Enzyme Database: 2.8.3.15
///
ENTRY       EC 2.8.3.16                 Enzyme
NAME        formyl-CoA transferase;
            formyl-coenzyme A transferase;
            formyl-CoA oxalate CoA-transferase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
SYSNAME     formyl-CoA:oxalate CoA-transferase
REACTION    formyl-CoA + oxalate = formate + oxalyl-CoA [RN:R07290]
ALL_REAC    R07290
SUBSTRATE   formyl-CoA [CPD:C00798];
            oxalate [CPD:C00209]
PRODUCT     formate [CPD:C00058];
            oxalyl-CoA [CPD:C00313]
COMMENT     The enzyme from Oxalobacter formigenes can also catalyse the
            transfer of CoA from formyl-CoA to succinate.
REFERENCE   1  [PMID:2361939]
  AUTHORS   Baetz AL, Allison MJ.
  TITLE     Purification and characterization of formyl-coenzyme A transferase
            from Oxalobacter formigenes.
  JOURNAL   J. Bacteriol. 172 (1990) 3537-40.
  ORGANISM  Oxalobacter formigenes
REFERENCE   2  [PMID:9150242]
  AUTHORS   Sidhu H, Ogden SD, Lung HY, Luttge BG, Baetz AL, Peck AB.
  TITLE     DNA sequencing and expression of the formyl coenzyme A transferase
            gene, frc, from Oxalobacter formigenes.
  JOURNAL   J. Bacteriol. 179 (1997) 3378-81.
  ORGANISM  Oxalobacter formigenes
ORTHOLOGY   KO: K07749  formyl-CoA transferase
GENES       TET: TTHERM_00942980
            ECO: b2374(yfdW)
            ECJ: JW2371(frc)
            ECE: Z3639
            ECS: ECs3254
            ECC: c2910(yfdW)
            ECI: UTI89_C2706(yfdW)
            ECP: ECP_2399
            ECV: APECO1_4162(yfdW)
            ECW: EcE24377A_2662(frc)
            ECX: EcHS_A2511(frc)
            SFL: SF2441
            SFX: S2578
            SFV: SFV_2433
            SSN: SSON_2465
            SBO: SBO_2400
            SDY: SDY_2572
            PPF: Pput_0178
            PEN: PSEEN4246
            PCR: Pcryo_0816
            CSA: Csal_3187
            REU: Reut_A0849 Reut_A2108 Reut_A2908 Reut_A3087 Reut_B4663
                 Reut_B4669 Reut_B4958 Reut_B5243 Reut_C5950 Reut_C6256
                 Reut_C6300 Reut_C6317
            REH: H16_B1711 H16_B1717
            RME: Rmet_2125 Rmet_4361
            BXE: Bxe_A1310 Bxe_A2358 Bxe_A2730 Bxe_B2760 Bxe_B2997
            BVI: Bcep1808_1372 Bcep1808_4753
            BUR: Bcep18194_A4039 Bcep18194_A4552 Bcep18194_A4814
                 Bcep18194_A4852 Bcep18194_A5125 Bcep18194_A5468
                 Bcep18194_A6218 Bcep18194_B0150 Bcep18194_B1149
                 Bcep18194_B1398 Bcep18194_B1719 Bcep18194_B2644
                 Bcep18194_B3030 Bcep18194_C6960 Bcep18194_C7130
                 Bcep18194_C7159 Bcep18194_C7275 Bcep18194_C7291
                 Bcep18194_C7301 Bcep18194_C7334 Bcep18194_C7487
                 Bcep18194_C7488
            BCN: Bcen_0458 Bcen_0926 Bcen_5531
            BCH: Bcen2424_0937 Bcen2424_1408 Bcen2424_1824 Bcen2424_5895
            BAM: Bamb_1285 Bamb_1599 Bamb_1762 Bamb_6417 Bamb_6531
            BPM: BURPS1710b_2370
            BTE: BTH_I2222
            PNU: Pnuc_0638 Pnuc_0872 Pnuc_0899
            RFR: Rfer_2745
            POL: Bpro_2484 Bpro_2751 Bpro_2801 Bpro_3024 Bpro_4036
            PNA: Pnap_3505
            AAV: Aave_1651 Aave_1981
            VEI: Veis_0880 Veis_1135 Veis_1581 Veis_1735 Veis_3615 Veis_3863
            HAR: HEAR0354(frcA) HEAR0355(frcB) HEAR1048
            MMS: mma_0401(caiB1)
            MES: Meso_2971
            SMD: Smed_5748
            RET: RHE_CH02877
            RLE: RL3337 pRL110024
            BJA: bll3156
            BRA: BRADO0103 BRADO1428 BRADO1441 BRADO2455 BRADO3125 BRADO4956
                 BRADO5270 BRADO5313
            BBT: BBta_0110 BBta_2631 BBta_2801 BBta_3108 BBta_3113 BBta_3565
                 BBta_5721 BBta_5761 BBta_6664 BBta_6680
            RPA: RPA1945
            RPB: RPB_2058 RPB_3427
            RPC: RPC_0403 RPC_1854
            RPD: RPD_0187 RPD_2027
            RPE: RPE_0441 RPE_1958 RPE_4318
            SIT: TM1040_2729
            JAN: Jann_3751
            RDE: RD1_1673 RD1_3680
            NAR: Saro_0174
            RRU: Rru_A2006 Rru_A2550
            SUS: Acid_3090
            LAC: LBA0395
            LGA: LGAS_0247
            CTC: CTC02087
            AMT: Amet_0692
            MSM: MSMEG_0158 MSMEG_0168 MSMEG_1154
            MGI: Mflv_4465
            MMC: Mmcs_1589
            MKM: Mkms_1613
            MJL: Mjls_1559
            RHA: RHA1_ro00763 RHA1_ro02283 RHA1_ro02936 RHA1_ro03351
                 RHA1_ro04635 RHA1_ro04925 RHA1_ro07076
            SCO: SCO6583
            SMA: SAV1820
            ART: Arth_1080
            NCA: Noca_0039 Noca_0047 Noca_2158
            FRA: Francci3_2429
            FAL: FRAAL0382 FRAAL0723 FRAAL2614 FRAAL3495 FRAAL3522 FRAAL3596
            SEN: SACE_1910 SACE_2328 SACE_3741 SACE_4399 SACE_4588
            RXY: Rxyl_0244 Rxyl_0365 Rxyl_1698
            RRS: RoseRS_0050 RoseRS_3860
            RCA: Rcas_0558 Rcas_3495
            PCL: Pcal_0206
STRUCTURES  PDB: 1T3Z  1T4C  1VGQ  1VGR  
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.16
            ExPASy - ENZYME nomenclature database: 2.8.3.16
            ExplorEnz - The Enzyme Database: 2.8.3.16
            ERGO genome analysis and discovery system: 2.8.3.16
            BRENDA, the Enzyme Database: 2.8.3.16
            CAS: 128826-27-7
///
ENTRY       EC 2.8.3.17                 Enzyme
NAME        cinnamoyl-CoA:phenyllactate CoA-transferase;
            FldA
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
SYSNAME     (E)-cinnamoyl-CoA:(R)-phenyllactate CoA-transferase
REACTION    (E)-cinnamoyl-CoA + (R)-phenyllactate = (E)-cinnamate +
            (R)-phenyllactyl-CoA [RN:R07796]
ALL_REAC    R07796
SUBSTRATE   (E)-cinnamoyl-CoA [CPD:C16256];
            (R)-phenyllactate [CPD:C05607]
PRODUCT     (E)-cinnamate [CPD:C00423];
            (R)-phenyllactyl-CoA [CPD:C16257]
COMMENT     3-Phenylproprionate is a better CoA acceptor than (R)-phenyllactate
            in vitro. The enzyme from Clostridium sporogenes is specific for
            derivatives of 3-phenylpropionate and 4-phenylbutyrate.
REFERENCE   1  [PMID:10849007]
  AUTHORS   Dickert S, Pierik AJ, Linder D, Buckel W.
  TITLE     The involvement of coenzyme A esters in the dehydration of
            (R)-phenyllactate to (E)-cinnamate by Clostridium sporogenes.
  JOURNAL   Eur. J. Biochem. 267 (2000) 3874-84.
  ORGANISM  Clostridium sporogenes
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.3.17
            ExPASy - ENZYME nomenclature database: 2.8.3.17
            ExplorEnz - The Enzyme Database: 2.8.3.17
            ERGO genome analysis and discovery system: 2.8.3.17
            BRENDA, the Enzyme Database: 2.8.3.17
///
ENTRY       EC 2.8.3.-                  Enzyme
CLASS       Transferases;
            Transferring sulfur-containing groups;
            CoA-transferases
REACTION    (1) Naphthyl-2-methyl-succinic acid + Succinyl-CoA <=>
            Naphthyl-2-methyl-succinyl-CoA + Succinate [RN:R06904];
            (2) 2-Naphthoyl-CoA + H2O <=> 2-Naphthoic acid + CoA [RN:R07881]
SUBSTRATE   Naphthyl-2-methyl-succinic acid [CPD:C14115];
            Succinyl-CoA [CPD:C00091]
PRODUCT     Naphthyl-2-methyl-succinyl-CoA [CPD:C14116];
            Succinate [CPD:C00042]
///
ENTRY       EC 2.8.4.1                  Enzyme
NAME        coenzyme-B sulfoethylthiotransferase;
            methyl-CoM reductase;
            methyl coenzyme M reductase
CLASS       Transferases;
            Transferring sulfur-containing groups;
            Transferring alkylthio groups
SYSNAME     2-(methylthio)ethanesulfonate:N-(7-thioheptanoyl)-3-O-phosphothreoni
            ne S-(2-sulfoethyl)thiotransferase
REACTION    2-(methylthio)ethanesulfonate (methyl-CoM) +
            N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) =
            CoM-S-S-CoB + methane [RN:R04541]
ALL_REAC    R04541
SUBSTRATE   2-(methylthio)ethanesulfonate [CPD:C03920];
            N-(7-mercaptoheptanoyl)threonine 3-O-phosphate [CPD:C04628]
PRODUCT     CoM-S-S-CoB [CPD:C04832];
            methane [CPD:C01438]
COMMENT     The enzyme from methanogenic bacteria requires the hydroporphinoid
            nickel complex coenzyme F430. Highly specific for coenzyme B with a
            heptanoyl chain; ethyl CoM and difluoromethyl CoM are poor
            substrates. The sulfide sulfur can be replaced by selenium but not
            by oxygen.
REFERENCE   1  [PMID:3122735]
  AUTHORS   Bobik TA, Olson KD, Noll KM, Wolfe RS.
  TITLE     Evidence that the heterodisulfide of coenzyme M and
            7-mercaptoheptanoylthreonine phosphate is a product of the
            methylreductase reaction in Methanobacterium.
  JOURNAL   Biochem. Biophys. Res. Commun. 149 (1987) 455-60.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
REFERENCE   2
  AUTHORS   Ellermann, J., Hedderich, R., Boecher, R. and Thauer, R.K.
  TITLE     The final step in methane formation: investigations with highly
            purified methyl coenzyme M reductase component C from
            Methanobacterium thermoautotrophicum (strain Marburg).
  JOURNAL   Eur. J. Biochem. 184 (1988) 63-68.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
REFERENCE   3  [PMID:9367957]
  AUTHORS   Ermler U, Grabarse W, Shima S, Goubeaud M, Thauer RK.
  TITLE     Crystal structure of methyl-coenzyme M reductase: the key enzyme of
            biological methane formation.
  JOURNAL   Science. 278 (1997) 1457-62.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
REFERENCE   4  [PMID:11072815]
  AUTHORS   Signor L, Knuppe C, Hug R, Schweizer B, Pfaltz A, Jaun B.
  TITLE     Methane formation by reaction of a methyl thioether with a
            photo-excited nickel thiolate--a process mimicking methanogenesis in
            archaea.
  JOURNAL   Chemistry. 6 (2000) 3508-16.
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K00398  methyl-coenzyme M reductase
            KO: K00399  methyl-coenzyme M reductase alpha subunit
            KO: K00401  methyl-coenzyme M reductase beta subunit
            KO: K00402  methyl-coenzyme M reductase gamma subunit
GENES       MJA: MJ0081(mcrB) MJ0082(mcrG) MJ0083(mcrA) MJ0842(mrtB)
                 MJ0845(mrtG) MJ0846(mrtA)
            MMP: MMP1555(mcrB) MMP1558(mcrG) MMP1559(mcrA)
            MMQ: MmarC5_0017
            MMZ: MmarC7_0802 MmarC7_0806
            MAE: Maeo_1264 Maeo_1268
            MVN: Mevan_0868 Mevan_0872
            MAC: MA4546 MA4547 MA4550
            MBA: Mbar_A0893 Mbar_A0894 Mbar_A0897
            MMA: MM_1240 MM_1241 MM_1244
            MBU: Mbur_2417 Mbur_2418 Mbur_2421
            MTP: Mthe_0569
            MHU: Mhun_2144 Mhun_2147 Mhun_2148
            MLA: Mlab_1242
            MEM: Memar_0378 Memar_0613
            MBN: Mboo_0582
            MTH: MTH1129(mrtA) MTH1130(mrtG) MTH1132(mrtB) MTH1164(mcrA)
                 MTH1165(mcrG) MTH1168(mcrB)
            MST: Msp_0318(mrtB) Msp_0320(mrtG) Msp_0321(mrtA)
            MSI: Msm_0902 Msm_0903 Msm_0905 Msm_1019
            MKA: MK0651(mcrB) MK0654(mcrG) MK0655(mcrA)
            RCI: RCIX2059(mcrB) RCIX2060(mcrD-1) RCIX2061(mcrC) RCIX2062(mcrG)
                 RCIX2063(mcrA) RCIX962(mcrD-2)
DBLINKS     IUBMB Enzyme Nomenclature: 2.8.4.1
            ExPASy - ENZYME nomenclature database: 2.8.4.1
            ExplorEnz - The Enzyme Database: 2.8.4.1
            ERGO genome analysis and discovery system: 2.8.4.1
            BRENDA, the Enzyme Database: 2.8.4.1
///
ENTRY       EC 2.9.1.1                  Enzyme
NAME        L-seryl-tRNASec selenium transferase;
            L-selenocysteinyl-tRNASel synthase;
            L-selenocysteinyl-tRNASec synthase selenocysteine synthase;
            cysteinyl-tRNASec-selenium transferase;
            cysteinyl-tRNASec-selenium transferase
CLASS       Transferases;
            Transferring selenium-containing groups;
            Selenotransferases
SYSNAME     selenophosphate:L-seryl-tRNASec selenium transferase
REACTION    L-seryl-tRNASec + selenophosphate = L-selenocysteinyl-tRNASec +
            phosphate
ALL_REAC    (other) R04689
SUBSTRATE   L-seryl-tRNASec;
            selenophosphate [CPD:C05172]
PRODUCT     L-selenocysteinyl-tRNASec;
            phosphate [CPD:C00009]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal 5'-phosphate enzyme identified in Escherichia coli.
            Recognises specifically tRNASec-species. Binding of tRNASec also
            occurs in the absence of the seryl group. 2-Aminoacryloyl-tRNA,
            bound to the enzyme as an imine with the pyridoxal phosphate, is an
            intermediate in the reaction. Since the selenium atom replaces
            oxygen in serine, the product may also be referred to as
            L-selenoseryl-tRNASec. The symbol Sel has also been used for
            selenocysteine but Sec is preferred.
REFERENCE   1  [PMID:2007585]
  AUTHORS   Forchhammer K, Bock A.
  TITLE     Selenocysteine synthase from Escherichia coli. Analysis of the
            reaction sequence.
  JOURNAL   J. Biol. Chem. 266 (1991) 6324-8.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00450  Selenoamino acid metabolism
ORTHOLOGY   KO: K01042  L-seryl-tRNA(Ser) seleniumtransferase
GENES       ECO: b3591(selA)
            ECJ: JW3564(selA)
            ECE: Z5012(selA)
            ECS: ECs4468
            ECC: c4412(selA)
            ECI: UTI89_C4133(selA)
            ECP: ECP_3693
            ECV: APECO1_2862(selA)
            ECW: EcE24377A_4089(selA)
            ECX: EcHS_A3796(selA)
            STY: STY4017 STY4113(selA)
            STT: t3750 t3836(selA)
            SPT: SPA3534(selA) SPA3618
            SEC: SC3607(selA)
            STM: STM3683(selA) STM3768
            YPE: YPO4054(selA)
            YPK: y4074(selA)
            YPM: YP_3966(selA)
            YPA: YPA_3031
            YPN: YPN_3701
            YPP: YPDSF_0039
            YPS: YPTB3931(selA)
            YPI: YpsIP31758_4115(selA)
            SFL: SF3629(selA)
            SFX: S4139(selA)
            SFV: SFV_3942(selA)
            SSN: SSON_3817(selA)
            SBO: SBO_3591(selA)
            SDY: SDY_4212(selA)
            PLU: plu4897(selA)
            ENT: Ent638_0140
            SPE: Spro_0090
            HIT: NTHI0835(selA)
            HIP: CGSHiEE_08605
            HIQ: CGSHiGG_06875
            HDU: HD1994(selA)
            PMU: PM1768(selA)
            MSU: MS2338(selA)
            APL: APL_1562(selA)
            ASU: Asuc_0441
            PPR: PBPRB1540(selA)
            PAE: PA4808(selA)
            PAU: PA14_63540(selA)
            PAP: PSPA7_5527(selA)
            PPU: PP_0493(selA)
            PPF: Pput_0527
            PFO: Pfl_2706
            PEN: PSEEN0568(selA)
            SON: SO_0105(selA)
            SBM: Shew185_0104
            SPL: Spea_0442
            SHE: Shewmr4_0106
            SHM: Shewmr7_0101
            SHN: Shewana3_0106
            AHA: AHA_2508(selA) AHA_3916
            BMA: BMAA1678.1(selA)
            BMV: BMASAVP1_1696(selA)
            BML: BMA10299_1903(selA)
            BMN: BMA10247_A0575(selA)
            BXE: Bxe_B2549
            BVI: Bcep1808_4490
            BUR: Bcep18194_B2096
            BCH: Bcen2424_3988
            BAM: Bamb_3381
            BPS: BPSS1663(selA)
            BPM: BURPS1710b_A0726(selA)
            BPL: BURPS1106A_A2255(selA)
            BPD: BURPS668_A2392(selA)
            BTE: BTH_II0711(selA)
            RFR: Rfer_0940
            DAR: Daro_1814
            HPY: HP1513(selA)
            HPJ: jhp1406(selA)
            HPA: HPAG1_1399
            HHE: HH0740(selA)
            HAC: Hac_0070(selA)
            WSU: WS0840(selA)
            TDN: Tmden_0831
            CJE: Cj1378(selA)
            CJR: CJE1569(selA)
            CJJ: CJJ81176_1380(selA)
            CJU: C8J_1296(selA)
            CJD: JJD26997_0273(selA)
            CFF: CFF8240_1546(selA)
            CCV: CCV52592_0540(selA) CCV52592_0995
            CHA: CHAB381_0765(selA)
            CCO: CCC13826_0688 CCC13826_0755(selA)
            ABU: Abu_1524(selA)
            GSU: GSU3369(selA)
            GME: Gmet_0061
            GUR: Gura_4162
            PCA: Pcar_0819
            DVU: DVU2883(selA)
            DVL: Dvul_0482
            DDE: Dde_3059
            LIP: LI0132(selA)
            DPS: DP1691
            ADE: Adeh_0412
            AFW: Anae109_4157
            MXA: MXAN_3346(selA)
            SAT: SYN_01801
            SFU: Sfum_3477
            MLO: mlr3804
            SME: SMa0011(selA)
            ATU: Atu3263(selA)
            ATC: AGR_L_3109
            RET: RHE_PE00344(selA)
            RLE: pRL110458
            OAN: Oant_2867
            XAU: Xaut_0658
            PDE: Pden_0301
            HNE: HNE_2489(selA)
            ABA: Acid345_4521
            SUS: Acid_3675
            BAN: BA5099
            BAR: GBAA5099
            BAA: BA_5518
            BAT: BAS4739
            BCE: BC4845
            BCA: BCE_5002
            BCZ: BCZK4598(selA)
            BTK: BT9727_4579(selA)
            BTL: BALH_4412(selA)
            BCL: ABC1413
            OIH: OB3204
            LPL: lp_0251(selA)
            LCA: LSEI_2712
            EFA: EF0838
            STH: STH2591
            CPE: CPE2117(selA)
            CPF: CPF_2373(selA)
            CPR: CPR_2085(selA)
            CDF: CD2495(fdhA)
            CBO: CBO2976(fdhA)
            CBA: CLB_3001(selA)
            CBH: CLC_2873(selA)
            CBF: CLI_3030(selA)
            AMT: Amet_2323
            CHY: CHY_1803(selA)
            DSY: DSY3097(selA)
            DRM: Dred_2186
            SWO: Swol_2561
            TTE: TTE1872(selA)
            MTA: Moth_2504
            MPA: MAP0365c
            MAV: MAV_0418(selA)
            MSM: MSMEG_1850(selA)
            MMC: Mmcs_5215
            MKM: Mkms_5303
            MJL: Mjls_5595
            FRA: Francci3_0439
            FAL: FRAAL0930(selA)
            KRA: Krad_1608
            SEN: SACE_3552
            STP: Strop_0594
            RXY: Rxyl_1983
            TDE: TDE2477(selA)
            AAE: aq_1031(selA)
            MST: Msp_0916
            TAC: Ta0673
DBLINKS     IUBMB Enzyme Nomenclature: 2.9.1.1
            ExPASy - ENZYME nomenclature database: 2.9.1.1
            ExplorEnz - The Enzyme Database: 2.9.1.1
            ERGO genome analysis and discovery system: 2.9.1.1
            BRENDA, the Enzyme Database: 2.9.1.1
///
ENTRY       EC 2.-.-.-                  Enzyme
CLASS       Transferases
REACTION    (1)
            2,3,2'3'-Tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-
            glucosamine 1,4'-bisphosphate + CMP-3-deoxy-D-manno-octulosonate <=>
            3-Deoxy-D-manno-octulosonyl-lipid IV(A) + CMP [RN:R04658];
            (2) 3-Deoxy-D-manno-octulosonyl-lipid IV(A) +
            CMP-3-deoxy-D-manno-octulosonate <=>
            Di[3-deoxy-D-manno-octulosonyl]-lipid IV(A) + CMP [RN:R05074]
SUBSTRATE   2,3,2'3'-Tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-
            glucosamine 1,4'-bisphosphate [CPD:C04919];
            CMP-3-deoxy-D-manno-octulosonate [CPD:C04121];
            3-Deoxy-D-manno-octulosonyl-lipid IV(A) [CPD:C06024]
PRODUCT     3-Deoxy-D-manno-octulosonyl-lipid IV(A) [CPD:C06024];
            CMP [CPD:C00055];
            Di[3-deoxy-D-manno-octulosonyl]-lipid IV(A) [CPD:C06025]
///
ENTRY       EC 3.1.1.1                  Enzyme
NAME        carboxylesterase;
            ali-esterase;
            B-esterase;
            monobutyrase;
            cocaine esterase;
            procaine esterase;
            methylbutyrase;
            vitamin A esterase;
            butyryl esterase;
            carboxyesterase;
            carboxylate esterase;
            carboxylic esterase;
            methylbutyrate esterase;
            triacetin esterase;
            carboxyl ester hydrolase;
            butyrate esterase;
            methylbutyrase;
            alpha-carboxylesterase;
            propionyl esterase;
            nonspecific carboxylesterase;
            esterase D;
            esterase B;
            esterase A;
            serine esterase;
            carboxylic acid esterase;
            cocaine esterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     carboxylic-ester hydrolase
REACTION    a carboxylic ester + H2O = an alcohol + a carboxylate [RN:R00630]
ALL_REAC    R00630 > R06728
SUBSTRATE   carboxylic ester [CPD:C02391];
            H2O [CPD:C00001]
PRODUCT     alcohol [CPD:C00069];
            carboxylate [CPD:C00060]
COMMENT     Wide specificity. The enzymes from microsomes also catalyse the
            reactions of EC 3.1.1.2 (arylesterase), EC 3.1.1.5
            (lysophospholipase), EC 3.1.1.6 (acetylesterase), EC 3.1.1.23
            (acylglycerol lipase), EC 3.1.1.28 (acylcarnitine hydrolase), EC
            3.1.2.2 (palmitoyl-CoA hydrolase), EC 3.5.1.4 (amidase) and EC
            3.5.1.13 (aryl-acylamidase). Also hydrolyses vitamin A esters.
REFERENCE   1  [PMID:4884138]
  AUTHORS   Augusteyn RC, de Jersey J, Webb EC, Zerner B.
  TITLE     On the homology of the active-site peptides of liver
            carboxylesterases.
  JOURNAL   Biochim. Biophys. Acta. 171 (1969) 128-37.
  ORGANISM  pig [GN:ssc], sheep, chicken [GN:gga], cow [GN:bta]
REFERENCE   2  [PMID:4981346]
  AUTHORS   Barker DL, Jencks WP.
  TITLE     Pig liver esterase. Physical properties.
  JOURNAL   Biochemistry. 8 (1969) 3879-89.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:5353595]
  AUTHORS   Bertram J, Krisch K.
  TITLE     Hydrolysis of vitamin A acetate by unspecific carboxylesterases from
            liver and kidney.
  JOURNAL   Eur. J. Biochem. 11 (1969) 122-6.
  ORGANISM  pig [GN:ssc], human [GN:hsa], cow [GN:bta]
REFERENCE   4  [PMID:13208632]
  AUTHORS   BURCH J.
  TITLE     The purification and properties of horse liver esterase.
  JOURNAL   Biochem. J. 58 (1954) 415-26.
  ORGANISM  horse
REFERENCE   5  [PMID:5785220]
  AUTHORS   Horgan DJ, Stoops JK, Webb EC, Zerner B.
  TITLE     Carboxylesterases (EC 3.1.1). A large-scale purification of pig
            liver carboxylesterase.
  JOURNAL   Biochemistry. 8 (1969) 2000-6.
  ORGANISM  pig [GN:ssc]
REFERENCE   6
  AUTHORS   Malhotra, O.P. and Philip, G.
  TITLE     Specificity of goat intestinal esterase.
  JOURNAL   Biochem. Z. 346 (1966) 386-402.
  ORGANISM  goat
REFERENCE   7  [PMID:6208846]
  AUTHORS   Mentlein R, Schumann M, Heymann E.
  TITLE     Comparative chemical and immunological characterization of five
            lipolytic enzymes (carboxylesterases) from rat liver microsomes.
  JOURNAL   Arch. Biochem. Biophys. 234 (1984) 612-21.
  ORGANISM  rat [GN:rno]
REFERENCE   8  [PMID:5785222]
  AUTHORS   Runnegar MT, Scott K, Webb EC, Zerner B.
  TITLE     Carboxylesterases (EC 3.1.1). Purification and titration of ox liver
            carboxylesterase.
  JOURNAL   Biochemistry. 8 (1969) 2013-8.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00960  Alkaloid biosynthesis II
ORTHOLOGY   KO: K01044  carboxylesterase
            KO: K03927  carboxylesterase type B
            KO: K03928  carboxylesterase
GENES       HSA: 1066(CES1) 2098(ESD) 221223(CES7) 3988(LIPA) 8824(CES2)
            MCC: 699486(CES1)
            MMU: 13884(Es1) 13885(Esd) 13897(Es22) 13909(EG13909) 234673(Ces5)
                 382053(Es31) 436059(EG436059) 72361(2210023G05Rik)
            RNO: 113902(Ces3) 171118(Ces2) 246252(Ces6) 29225(Ces1)
            CFA: 403643(CES1) 489769(CES2)
            SSC: 397127(ESD)
            GGA: 415786(CES1)
            XLA: 447149(MGC85439) 447584(MGC84363)
            XTR: 496692(LOC496692)
            DME: Dmel_CG1031(alpha-Est1) Dmel_CG1082(alpha-Est4)
                 Dmel_CG1089(alpha-Est5) Dmel_CG1108(alpha-Est6)
                 Dmel_CG1112(alpha-Est7) Dmel_CG1257(alpha-Est3)
                 Dmel_CG13772(neuroligin) Dmel_CG17148(Est-P)
                 Dmel_CG2505(alpha-Est2) Dmel_CG3903(Gli) Dmel_CG4390
                 Dmel_CG6917(Est-6) Dmel_CG8424(Jhedup) Dmel_CG9858(clt)
            CEL: C52A10.2(carboxylesterase) F07C4.12(carboxylesterase)
                 F13H6.3(carboxylesterase) F13H6.4(carboxylesterase)
                 F15A8.6(esterase) R12A1.4(carboxylesterase)
                 ZC376.3(carboxylesterase)
            CAL: CaO19.6596
            AFM: AFUA_3G09230
            ANG: An12g05010(aceA)
            CNE: CNJ02970 CNM01720
            UMA: UM05964.1
            DDI: DDB_0191254(cryS)
            TET: TTHERM_00854230 TTHERM_01083050
            ECI: UTI89_C2800(ypfH) UTI89_C3913(bioH) UTI89_C4790(yjfP)
            STY: STY1441
            STT: t1532
            STM: STM1623
            YPA: YPA_0796
            YPP: YPDSF_1476
            YPS: YPTB1516
            YPI: YpsIP31758_3988(bioH)
            ENT: Ent638_2755
            SPE: Spro_1556
            ASU: Asuc_0066
            XCC: XCC0143(estA1) XCC3164
            XCB: XC_0152 XC_1001
            XCV: XCV0144 XCV0676 XCV0790 XCV1242 XCV3433
            XAC: XAC0159(estA1) XAC1213 XAC3315
            XOM: XOO_3189(XOO3189)
            PPF: Pput_0390 Pput_0452 Pput_4160 Pput_4429
            PSB: Psyr_1071 Psyr_1368
            PSP: PSPPH_1129 PSPPH_1407(estC) PSPPH_3053
            PFL: PFL_1047 PFL_1281(estC) PFL_4885(est)
            PEN: PSEEN0445(estA) PSEEN4526(estB)
            PMY: Pmen_3027 Pmen_3561 Pmen_4086
            PCR: Pcryo_1633 Pcryo_1996
            PRW: PsycPRwf_0583 PsycPRwf_0967 PsycPRwf_2327
            ACI: ACIAD3648(estA)
            SDN: Sden_2138
            SFR: Sfri_2310 Sfri_3426 Sfri_4058
            SAZ: Sama_0003 Sama_2022
            SBL: Sbal_2418
            SBM: Shew185_2407 Shew185_2626 Shew185_4199
            SLO: Shew_1541 Shew_2136
            SPC: Sputcn32_2173 Sputcn32_2312
            SSE: Ssed_0176 Ssed_2670 Ssed_4226
            SPL: Spea_0270 Spea_1907 Spea_4013
            SHE: Shewmr4_1787 Shewmr4_2265
            SHM: Shewmr7_2190 Shewmr7_2337
            SHN: Shewana3_2455
            SHW: Sputw3181_1696 Sputw3181_1836
            PAT: Patl_0345 Patl_0510 Patl_0874 Patl_1439 Patl_1828
            SDE: Sde_0051 Sde_1514
            PIN: Ping_2608 Ping_3531
            MAQ: Maqu_0257 Maqu_2252 Maqu_3288
            LPN: lpg2845
            LPF: lpl2757
            LPP: lpp2904
            FTL: FTL_0139
            TCX: Tcr_1846
            NOC: Noc_1393
            AEH: Mlg_0211
            HCH: HCH_04813
            CSA: Csal_1107
            ABO: ABO_1251(estC)
            MMW: Mmwyl1_3455 Mmwyl1_3679 Mmwyl1_3782
            AHA: AHA_0471
            NMC: NMC1242(esd)
            CVI: CV_0739 CV_0759
            REU: Reut_B3999 Reut_B4297
            REH: H16_B1155
            BMA: BMAA1467
            BVI: Bcep1808_2717
            BUR: Bcep18194_A5198 Bcep18194_A5934 Bcep18194_B0954
                 Bcep18194_B3077 Bcep18194_C6775 Bcep18194_C7656
            BCN: Bcen_1993
            BCH: Bcen2424_2603
            BPS: BPSS0291
            BPM: BURPS1710b_1005(estA) BURPS1710b_2673(estA) BURPS1710b_A1076
                 BURPS1710b_A1839(llpE)
            BTE: BTH_II2107
            RFR: Rfer_1674
            POL: Bpro_3402
            PNA: Pnap_1229
            AAV: Aave_2194
            AJS: Ajs_2801
            VEI: Veis_4023
            HAR: HEAR0995 HEAR1069
            NET: Neut_1182
            NMU: Nmul_A2273
            AZO: azo1421 azo2859(estB)
            MFA: Mfla_1791 Mfla_2130
            PCA: Pcar_0758
            DVU: DVU1824
            DDE: Dde_1813
            BBA: Bd0899(esd) Bd2632 Bd3289
            ADE: Adeh_3458
            MXA: MXAN_1649 MXAN_6764
            PLA: Plav_2452
            SMD: Smed_1021 Smed_3945
            RET: RHE_PB00109 RHE_PD00086(ypd00019)
            RLE: RL0122 RL1125 RL3123 pRL110316 pRL120770
            OAN: Oant_0141
            BRA: BRADO2319 BRADO5591
            BBT: BBta_2505
            RPA: RPA1568 RPA2627 RPA3893 RPA4646
            RPB: RPB_3278
            RPC: RPC_0099
            RPE: RPE_0251 RPE_4680
            XAU: Xaut_2645
            CCR: CC_0799
            SIT: TM1040_3448
            RSH: Rsph17029_2511
            RSQ: Rsph17025_3123
            JAN: Jann_0052
            PDE: Pden_0019
            MMR: Mmar10_0226 Mmar10_0807
            NAR: Saro_2922
            SAL: Sala_3037
            SWI: Swit_1177
            GOX: GOX2019
            GBE: GbCGDNIH1_0710 GbCGDNIH1_1155 GbCGDNIH1_1164
            ACR: Acry_0002
            BSU: BG11844(pnbA) BG11957(nap) BG12740(ybfK) BG14066(yvaK)
            BHA: BH3554
            BAN: BA2738 BA5335(estA)
            BAR: GBAA2738 GBAA5335(estA)
            BAA: BA_0195 BA_3262
            BAT: BAS2551 BAS4957
            BCE: BC2743 BC5130
            BCA: BCE_2771 BCE_5233(estA)
            BCZ: BCZK2473(estA) BCZK4819(est) pE33L466_0366
            BCY: Bcer98_2815
            BTK: BT9727_2507(estA) BT9727_4809(est)
            BTL: BALH_2462(estA) BALH_4623(est)
            BLI: BL01300 BL03481(yvaK)
            BLD: BLi00638(pnbA) BLi03642(yvaK)
            BCL: ABC3005 ABC3006
            BAY: RBAM_031690
            BPU: BPUM_0429 BPUM_0466 BPUM_3032(bioH)
            OIH: OB0300 OB2429
            GKA: GK0225 GK3045 GK3049
            SAU: SA0416 SA0734 SA2240
            SAV: SAV0457 SAV0779 SAV2451
            SAM: MW0411 MW0741 MW2375
            SAR: SAR0457 SAR0835(est) SAR2541
            SAS: SAS0415 SAS0745 SAS2343
            SAC: SACOL0499 SACOL0845(est) SACOL2459(pnbA)
            SAB: SAB0407 SAB0735 SAB2333
            SAA: SAUSA300_0430 SAUSA300_0763(est) SAUSA300_2396(pnbA)
            SAO: SAOUHSC_00417 SAOUHSC_00802 SAOUHSC_02751
            SEP: SE0564 SE2022 SE2328
            SER: SERP0090 SERP0449(est) SERP2035
            SHA: SH0602 SH2106 SH2555
            SSP: SSP1908 SSP2303
            LMO: lmo2450 lmo2452
            LMF: LMOf2365_2423(est-1) LMOf2365_2425(est-2)
            LIN: lin2544 lin2546
            LWE: lwe2398(est-1) lwe2400(est-2)
            LPL: lp_0796
            LSA: LSA1412
            LBR: LVIS_0668
            LCA: LSEI_0975
            EFA: EF2618
            STH: STH2045 STH251
            CAC: CA_P0050(pnbA)
            DSY: DSY0640
            MTU: Rv2045c(lipT)
            MTC: MT2105
            MPA: MAP1780c(lipT) MAP2689c
            MSM: MSMEG_0611 MSMEG_3667 MSMEG_3848
            MMC: Mmcs_2511 Mmcs_2865 Mmcs_4216
            CGB: cg1284(lipT)
            CDI: DIP1007
            CJK: jk0325(lipT1) jk1370(lipT2)
            NFA: nfa46420 nfa50190
            RHA: RHA1_ro01288 RHA1_ro01595 RHA1_ro03811 RHA1_ro05560
                 RHA1_ro05561
            SCO: SCO2123(SC6E10.17)
            SMA: SAV433 SAV6079 SAV7363(pnbA)
            CMI: CMM_2085(lipT)
            AAU: AAur_3811(estA)
            FRA: Francci3_3089
            FAL: FRAAL0320 FRAAL5088
            SEN: SACE_0989(estC) SACE_1410(pnbA) SACE_2543(pnbA) SACE_2896
                 SACE_2933(pnbA) SACE_3662(estC) SACE_3682 SACE_3712
            CTA: CTA_0143
            TPA: TP0902
            TDE: TDE0187
            SYG: sync_0827(est)
            CYA: CYA_1871(est)
            CYB: CYB_1563(est)
            TEL: tll0989
            GVI: gll2009
            AVA: Ava_1087 Ava_3813
            TER: Tery_2838
            CTE: CT2271
            CCH: Cag_1691 Cag_1939
            PLT: Plut_2086
            DRA: DR_2626
            DGE: Dgeo_2074
            TTH: TTC1341
            TTJ: TTHA0199 TTHA1705
            TMA: TM1022
            PTO: PTO0988
            SSO: SSO2517(est)
STRUCTURES  PDB: 1AUO  1AUR  1CI8  1CI9  1EVQ  1JJI  1K4Y  1L7Q  1L7R  1MX1  
                 1MX5  1MX9  1QZ3  1R1D  1TQH  1U4N  1YA4  1YA8  1YAH  1YAJ  
                 2C7B  2DQY  2DQZ  2DR0  2FJ0  2H1I  2H7C  2HM7  2HRQ  2HRR  
                 2JEY  2JEZ  2JF0  2O7R  2O7V  2OGS  2OGT  2R11  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.1
            ExPASy - ENZYME nomenclature database: 3.1.1.1
            ExplorEnz - The Enzyme Database: 3.1.1.1
            ERGO genome analysis and discovery system: 3.1.1.1
            UM-BBD (Biocatalysis/Biodegradation Database): 3.1.1.1
            BRENDA, the Enzyme Database: 3.1.1.1
            CAS: 9016-18-6
///
ENTRY       EC 3.1.1.2                  Enzyme
NAME        arylesterase;
            A-esterase;
            paraoxonase;
            aromatic esterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     aryl-ester hydrolase
REACTION    a phenyl acetate + H2O = a phenol + acetate [RN:R07342]
ALL_REAC    R07342 > R01241 R06893
SUBSTRATE   phenyl acetate [CPD:C00548];
            H2O [CPD:C00001]
PRODUCT     phenol [CPD:C00146];
            acetate [CPD:C00033]
COMMENT     Acts on many phenolic esters. The reactions of EC 3.1.8.1
            aryldialkylphosphatase, were previously attributed to this enzyme.
            It is likely that the three forms of human paraoxonase are
            lactonases rather than aromatic esterases [7,8]. The natural
            substrates of the paraoxonases are lactones [7,8], with
            (+/-)-5-hydroxy-6E,8Z,11Z,4Z-eicostetraenoic-acid 1,5-lactone being
            the best substrate [8].
REFERENCE   1  [PMID:13032041]
  AUTHORS   ALDRIDGE WN.
  TITLE     Serum esterases.  I.  Two types of esterase (A and B) hydrolysing
            p-nitrophenyl acetate, propionate and butyrate, and a method for
            their determination.
  JOURNAL   Biochem. J. 53 (1953) 110-7.
  ORGANISM  rabbit, rat [GN:rno], horse
REFERENCE   2  [PMID:13638253]
  AUTHORS   AUGUSTINSSON KB, OLSSON B.
  TITLE     Esterases in the milk and blood plasma of swine. I. Substrate
            specificity and electrophoresis studies.
  JOURNAL   Biochem. J. 71 (1959) 477-84.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:5047702]
  AUTHORS   Bosmann HB.
  TITLE     Membrane marker enzymes. Characterization of an arylesterase of
            guinea pig cerebral cortex utilizing p-nitrophenyl acetate as
            substrate.
  JOURNAL   Biochim. Biophys. Acta. 276 (1972) 180-91.
  ORGANISM  guinea pig
REFERENCE   4  [PMID:2152179]
  AUTHORS   Kim DH, Yang YS, Jakoby WB.
  TITLE     Nonserine esterases from rat liver cytosol.
  JOURNAL   Protein. Expr. Purif. 1 (1990) 19-27.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:2822017]
  AUTHORS   Mackness MI, Thompson HM, Hardy AR, Walker CH.
  TITLE     Distinction between 'A'-esterases and arylesterases. Implications
            for esterase classification.
  JOURNAL   Biochem. J. 245 (1987) 293-6.
  ORGANISM  cow [GN:bta], rabbit, mouse [GN:mmu], sheep, goat, pig [GN:ssc],
            cat, human [GN:hsa]
REFERENCE   6
  AUTHORS   In: Reiner, E., Aldridge, W.N. and Hoskin, C.G. (Eds.), Enzymes
            Hydrolysing Organophosphorus Compounds, Ellis Horwood, Chichester,
            UK, 1989.
  TITLE     7  [PMID:15835926]
  JOURNAL   Khersonsky O, Tawfik DS.
REFERENCE   Structure-reactivity studies of serum paraoxonase PON1 suggest that
            its native activity is lactonase.
  AUTHORS   Biochemistry. 44 (2005) 6371-82.
  TITLE     8  [PMID:15772423]
  JOURNAL   Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN.
REFERENCE   Human paraoxonases (PON1, PON2, and PON3) are lactonases with
            overlapping and distinct substrate specificities.
  AUTHORS   J. Lipid. Res. 46 (2005) 1239-47.
PATHWAY     PATH: map00363  Bisphenol A degradation
ORTHOLOGY   KO: K01045  arylesterase
GENES       HSA: 5444(PON1) 5445(PON2) 5446(PON3)
            PTR: 463547(PON1) 463548(PON3) 463549(PON2)
            MMU: 18979(Pon1) 269823(Pon3) 330260(Pon2)
            RNO: 296851(Pon2) 84024(Pon1)
            CFA: 403855(PON2)
            BTA: 281417(PON2)
            GGA: 395830(PON2)
            SPU: 582780(LOC582780)
            YPA: YPA_2575
            YPN: YPN_1009
            YPP: YPDSF_2718
            ENT: Ent638_0968
            VCH: VCA0783
            VCO: VC0395_0724
            VPA: VPA0872
            PPF: Pput_3451
            PSP: PSPPH_4522(cpoF)
            PEN: PSEEN1886
            SDN: Sden_2368
            SFR: Sfri_2568
            SAZ: Sama_1485
            SBL: Sbal_2688
            SBM: Shew185_2709
            SLO: Shew_2403
            SPC: Sputcn32_2392
            SSE: Ssed_1696
            SPL: Spea_1660
            SHE: Shewmr4_1478
            SHM: Shewmr7_1543
            SHN: Shewana3_1537
            SHW: Sputw3181_1616
            PAT: Patl_2914
            SDE: Sde_3444
            PIN: Ping_2959
            MAQ: Maqu_1044
            MCA: MCA1401
            TCX: Tcr_0549
            NOC: Noc_0429 Noc_1154
            AEH: Mlg_2409
            HHA: Hhal_2068
            CSA: Csal_2620
            MMW: Mmwyl1_2207
            RSO: RS03189(RSp1245)
            REU: Reut_A1384 Reut_A1943
            BVI: Bcep1808_1851 Bcep1808_3328
            BUR: Bcep18194_A5220
            BAM: Bamb_1907
            PNU: Pnuc_0938
            POL: Bpro_3031
            VEI: Veis_3412
            HAR: HEAR1747(tesA)
            NMU: Nmul_A1973
            AZO: azo0201
            MFA: Mfla_1250
            DDE: Dde_0413
            PUB: SAR11_0851
            MLO: mlr0387
            PLA: Plav_2097
            SME: SMc01033
            ATU: Atu1433(ada) Atu3454(ada)
            ATC: AGR_C_2642 AGR_L_2749
            RET: RHE_CH01936(ypch00628)
            RLE: RL1292 RL2244(ada)
            BME: BMEI1861
            BMB: BruAb1_0083
            BJA: blr6960
            BRA: BRADO0988
            NWI: Nwi_0416
            RDE: RD1_1228
            RRU: Rru_A3650
            BCE: BC3122
            BTK: BT9727_2915
            LCA: LSEI_1052
            CKL: CKL_2267
            RBA: RB3830
STRUCTURES  PDB: 1V04  1VA4  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.2
            ExPASy - ENZYME nomenclature database: 3.1.1.2
            ExplorEnz - The Enzyme Database: 3.1.1.2
            ERGO genome analysis and discovery system: 3.1.1.2
            UM-BBD (Biocatalysis/Biodegradation Database): 3.1.1.2
            BRENDA, the Enzyme Database: 3.1.1.2
            CAS: 9032-73-9
///
ENTRY       EC 3.1.1.3                  Enzyme
NAME        triacylglycerol lipase;
            lipase;
            triglyceride lipase;
            tributyrase;
            butyrinase;
            glycerol ester hydrolase;
            tributyrinase;
            Tween hydrolase;
            steapsin;
            triacetinase;
            tributyrin esterase;
            Tweenase;
            amno N-AP;
            Takedo 1969-4-9;
            Meito MY 30;
            Tweenesterase;
            GA 56;
            capalase L;
            triglyceride hydrolase;
            triolein hydrolase;
            tween-hydrolyzing esterase;
            amano CE;
            cacordase;
            triglyceridase;
            triacylglycerol ester hydrolase;
            amano P;
            amano AP;
            PPL;
            glycerol-ester hydrolase;
            GEH;
            meito Sangyo OF lipase;
            hepatic lipase;
            lipazin;
            post-heparin plasma protamine-resistant lipase;
            salt-resistant post-heparin lipase;
            heparin releasable hepatic lipase;
            amano CES;
            amano B;
            tributyrase;
            triglyceride lipase;
            liver lipase;
            hepatic monoacylglycerol acyltransferase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     triacylglycerol acylhydrolase
REACTION    triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
ALL_REAC    R01369 > R02250;
            (other) R02687 R02688 R05209
SUBSTRATE   triacylglycerol [CPD:C00422];
            H2O [CPD:C00001]
PRODUCT     diacylglycerol [CPD:C00165];
            carboxylate [CPD:C00060]
COMMENT     The pancreatic enzyme acts only on an ester-water interface; the
            outer ester links are preferentially hydrolysed.
REFERENCE   1  [PMID:13438870]
  AUTHORS   KORN ED, QUIGLEY TW Jr.
  TITLE     Lipoprotein lipase of chicken adipose tissue.
  JOURNAL   J. Biol. Chem. 226 (1957) 833-9.
  ORGANISM  chicken [GN:gga]
REFERENCE   2
  AUTHORS   Lynn, W.S. and Perryman, N.C.
  TITLE     Properties and purification of adipose tissue lipase.
  JOURNAL   J. Biol. Chem. 235 (1960) 1912-1916.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:13618257]
  AUTHORS   SARDA L, DESNUELLE P.
  TITLE     [Actions of pancreatic lipase on esters in emulsions.]
  JOURNAL   Biochim. Biophys. Acta. 30 (1958) 513-21.
REFERENCE   4
  AUTHORS   Singer, T.P. and Hofstee, B.H.J.
  TITLE     Studies on wheat germ lipase. I. Methods of estimation, purification
            and general properties of the enzyme.
  JOURNAL   Arch. Biochem. 18 (1948) 229-243.
  ORGANISM  Triticum aestivum [GN:etae]
REFERENCE   5
  AUTHORS   Singer, T.P. and Hofstee, B.H.J.
  TITLE     Studies on wheat germ lipase. II. Kinetics.
  JOURNAL   Arch. Biochem. 18 (1948) 245-259.
  ORGANISM  Triticum aestivum [GN:etae]
PATHWAY     PATH: map00561  Glycerolipid metabolism
ORTHOLOGY   KO: K01046  triacylglycerol lipase
GENES       HSA: 1056(CEL) 3988(LIPA) 3990(LIPC) 5406(PNLIP) 5407(PNLIPRP1)
                 5408(PNLIPRP2) 80339(PNPLA3) 8513(LIPF) 9388(LIPG)
            PTR: 450759(PNLIPRP2) 466143(LIPF)
            MMU: 116939(Pnpla3) 12613(Cel) 15450(Lipc) 16891(Lipg)
                 18947(Pnliprp2) 67717(Lipf)
            RNO: 117554(Pnliprp2) 24254(Cel) 24538(Lipc) 25055(Lip1)
                 25702(Pnlip) 50682(Lipf) 84028(Pnliprp1)
            CFA: 404010(PNLIPRP1) 477830(PNLIP) 478320(LIPC) 486903(PNLIPRP2)
            BTA: 280748(CEL) 281283(LIPF)
            GGA: 417165(CEL) 423916(PNLIP) 426846(LIPG)
            XLA: 379474(MGC64411) 380547(cel)
            DRE: 393997(lipc)
            SPU: 575047(LOC575047)
            DME: Dmel_CG17116(Lip2) Dmel_CG7329 Dmel_CG8093 Dmel_CG8823
            SCE: YDR058C(TGL2)
            AGO: AGOS_AAR046C AGOS_AFR650W
            PIC: PICST_60390(LIP11) PICST_78871 PICST_80311(SEC31)
            CGR: CAGL0E04708g
            YLI: YALI0B09361g(LIP8) YALI0D19184g(LIP7) YALI0E08492g(LIP4)
            SPO: SPCC1672.09
            ANI: AN9106.2
            AFM: AFUA_2G06010 AFUA_2G10900 AFUA_3G13880 AFUA_4G04010
                 AFUA_5G02040 AFUA_5G03770 AFUA_5G14150 AFUA_6G06510
                 AFUA_7G01180 AFUA_7G02040 AFUA_8G02530
            AOR: AO090038000580
            CNE: CNE02710
            UMA: UM03528.1
            DDI: DDBDRAFT_0215301
            TET: TTHERM_00013720 TTHERM_00047280 TTHERM_00112930
                 TTHERM_00112940 TTHERM_00313400 TTHERM_00378810
                 TTHERM_00570540 TTHERM_00701020
            TBR: Tb927.1.2740
            YEN: YE1842
            SPE: Spro_0065 Spro_2209 Spro_2957
            XFA: XF1181
            VCH: VCA0221
            VCO: VC0395_1006(hlyC)
            VVU: VV1_2349
            VVY: VV1990
            VPA: VP1181
            PPR: PBPRB1960
            PAE: PA2862(lip)
            PAU: PA14_27100(lipA)
            PAP: PSPA7_5359
            PPU: PP_4854(lip)
            PPF: Pput_1511
            PFL: PFL_0617
            PFO: Pfl_0571 Pfl_2685 Pfl_3071
            PEN: PSEEN2195 PSEEN3432 PSEEN4903(lip)
            PMY: Pmen_2564 Pmen_2812 Pmen_4422
            PRW: PsycPRwf_1952
            ACI: ACIAD1121(lip1) ACIAD3309
            SDN: Sden_1098
            SFR: Sfri_3849
            SBM: Shew185_2926
            SSE: Ssed_0083 Ssed_3056
            SPL: Spea_0089 Spea_1371
            HCH: HCH_04261
            ABO: ABO_1975(lip)
            MMW: Mmwyl1_3434
            AHA: AHA_0104 AHA_0512
            CVI: CV_2714
            REH: H16_A1322
            RME: Rmet_3796
            BMA: BMAA2080
            BMV: BMASAVP1_1107(lipA-1)
            BML: BMA10299_1386 BMA10299_1807
            BMN: BMA10247_A0478 BMA10247_A2371(lipA-1)
            BXE: Bxe_A2284
            BVI: Bcep1808_4391 Bcep1808_4392
            BUR: Bcep18194_B0085 Bcep18194_B0145 Bcep18194_B0294
                 Bcep18194_B1213 Bcep18194_B2173 Bcep18194_B3090
                 Bcep18194_B3121 Bcep18194_C6777
            BCN: Bcen_4451 Bcen_5251
            BCH: Bcen2424_3915 Bcen2424_5608
            BAM: Bamb_3293
            BPS: BPSS1741(lipA1) BPSS2319(lipA2)
            BPM: BURPS1710b_A0820(lipA1) BURPS1710b_A1467
            BPL: BURPS1106A_A2366 BURPS1106A_A3138(lipA)
            BPD: BURPS668_A2505 BURPS668_A3253(lipA)
            BTE: BTH_II0639 BTH_II2339
            RFR: Rfer_3358
            AAV: Aave_4189
            NEU: NE0777(TGL2)
            NMU: Nmul_A0873
            GUR: Gura_4199
            BBA: Bd0737
            AFW: Anae109_0745
            SAT: SYN_00679
            PLA: Plav_2568
            SMD: Smed_0264
            RLE: RL0662 pRL120023
            OAN: Oant_4203
            BRA: BRADO3493 BRADO4409 BRADO4633
            BBT: BBta_1090 BBta_4223 BBta_5035 BBta_6643
            RSQ: Rsph17025_1651 Rsph17025_2742
            SWI: Swit_0217
            ACR: Acry_2135
            BSU: BG10679(lipA) BG11951(lipB)
            BAN: BA2607 BA5117
            BAR: GBAA2607 GBAA5117
            BAA: BA_3118 BA_5536
            BAT: BAS2432 BAS4756
            BCE: BC4862
            BCA: BCE_2625 BCE_5022
            BCZ: BCZK0931 BCZK2353 BCZK4616
            BCY: Bcer98_1381
            BTK: BT9727_2387(lipA) BT9727_4594
            BTL: BALH_0914 BALH_4427
            BLI: BL05255(lip)
            BLD: BLi02525(lip) BLi03371
            BCL: ABC2996(lipB)
            BAY: RBAM_003010(lip)
            BPU: BPUM_2613(lip)
            GKA: GK1986
            SAU: SA0309(geh) SA2463(lip)
            SAV: SAV0320(geh) SAV2671(lip)
            SAM: MW0297(geh) MW2590(lip)
            SAR: SAR0317(geh) SAR2753(lip)
            SAS: SAS0297 SAS2556
            SAC: SACOL0317 SACOL2694(geh)
            SAB: SAB0257(geh) SAB2546c(lip)
            SAA: SAUSA300_0320 SAUSA300_2603(lip)
            SAO: SAOUHSC_00300 SAOUHSC_03006
            SAJ: SaurJH9_0303 SaurJH9_2694
            SAH: SaurJH1_0310 SaurJH1_2751
            SEP: SE0281 SE2403
            SER: SERP0018 SERP2297(geh-1) SERP2388(geh-2)
            SHA: SH0168(lip)
            SSP: SSP0502
            CTC: CTC00947 CTC01505
            CNO: NT01CX_0630 NT01CX_2047
            CBE: Cbei_4256
            AMT: Amet_2707
            CSC: Csac_1273
            MMY: MSC_0368(lip1) MSC_0530(lip2) MSC_0531(lip3)
            MMO: MMOB0660(lip2) MMOB2000(lip)
            MHY: mhp248(lip3)
            MSY: MS53_0382(lip3)
            MCP: MCAP_0445 MCAP_0446 MCAP_0606
            UUR: UU021(lip3)
            MTU: Rv3097c(PE_PGRS63)
            MBO: Mb3124c(PE_PGRS63)
            MBB: BCG_3122c(PE_PGRS63)
            MVA: Mvan_2796
            MGI: Mflv_3621
            MMC: Mmcs_0424 Mmcs_1338 Mmcs_3070
            MKM: Mkms_0434 Mkms_1356 Mkms_3130
            MJL: Mjls_0411 Mjls_1374 Mjls_3087
            CGL: NCgl0079(cgl0080) NCgl0080(cgl0081) NCgl1426(cgl1481)
            CGB: cg0109 cg0110 cg1320(lipP) cg1676(lip)
            RHA: RHA1_ro01897 RHA1_ro02361 RHA1_ro02663 RHA1_ro04722
                 RHA1_ro06372
            PAC: PPA1035 PPA1796 PPA2105
            TFU: Tfu_0882 Tfu_0883
            KRA: Krad_1666 Krad_3830
            SEN: SACE_0083 SACE_0795 SACE_0950 SACE_2354 SACE_3929(lipB)
            FNU: FN0484
            RBA: RB12482 RB5993
            LIL: LA0587
            LIC: LIC12988
            SYN: sll1969(lipA)
            SYW: SYNW1484
            SYD: Syncc9605_1028
            SYE: Syncc9902_0929
            SYG: sync_1876
            ANA: alr1352
            AVA: Ava_2832 Ava_5039
            PMA: Pro1069(lipA)
            PMM: PMM0592
            PMT: PMT0434
            PMN: PMN2A_0028
            PMI: PMT9312_0592
            PMB: A9601_06481
            PMC: P9515_06571
            PMF: P9303_18471
            PMG: P9301_06181
            PME: NATL1_06481
            TER: Tery_3549
            DRA: DR_2078
            TTH: TTC1787
            TPT: Tpet_0232
            TME: Tmel_0929
            FNO: Fnod_0694
STRUCTURES  PDB: 1AKN  1BU8  1CRL  1CUA  1CUB  1CUC  1CUD  1CUE  1CUF  1CUG  
                 1CUH  1CUI  1CUJ  1CUU  1CUV  1CUW  1CUX  1CUY  1CUZ  1CVL  
                 1DT3  1DT5  1DTE  1DU4  1EIN  1ETH  1EX9  1F6W  1FFA  1FFB  
                 1FFC  1FFD  1FFE  1GPL  1GT6  1GZ7  1HLG  1HPL  1HQD  1I6W  
                 1ISP  1JI3  1JMY  1K8Q  1KU0  1LBS  1LBT  1LGY  1LLF  1LPA  
                 1LPB  1LPM  1LPN  1LPO  1LPP  1LPS  1N8S  1OIL  1QGE  1R4Z  
                 1R50  1RP1  1T2N  1T4M  1TAH  1TCA  1TCB  1TCC  1TGL  1THG  
                 1TIA  1TIB  1TIC  1TRH  1YS1  1YS2  2DSN  2ES4  2FX5  2HIH  
                 2LIP  2OXE  2PPL  2QUA  2QUB  3LIP  3TGL  4LIP  4TGL  5LIP  
                 5TGL  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.3
            ExPASy - ENZYME nomenclature database: 3.1.1.3
            ExplorEnz - The Enzyme Database: 3.1.1.3
            ERGO genome analysis and discovery system: 3.1.1.3
            BRENDA, the Enzyme Database: 3.1.1.3
            CAS: 9001-62-1
///
ENTRY       EC 3.1.1.4                  Enzyme
NAME        phospholipase A2;
            lecithinase A;
            phosphatidase;
            phosphatidolipase;
            phospholipase A
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     phosphatidylcholine 2-acylhydrolase
REACTION    phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a
            carboxylate [RN:R01313]
ALL_REAC    R01313;
            (other) R01315 R01317 R02053 R03107 R07064 R07291 R07379 R07387
            R07859
SUBSTRATE   phosphatidylcholine [CPD:C00157];
            H2O [CPD:C00001]
PRODUCT     1-acylglycerophosphocholine [CPD:C04230];
            carboxylate [CPD:C00060]
COFACTOR    Calcium [CPD:C00076]
INHIBITOR   AACOCF3 [CPD:C01397];
            1-Hexadecylthio-1-deoxy-2-hexadecylphosphono-sn-glycero-3-phosphocho
            line [CPD:C04862];
            1-Hexadecylthio-2-hexadecanoylamino-1,2-dideoxy-sn-glycero-3-phospho
            choline [CPD:C04873]
COMMENT     Also acts on phosphatidylethanolamine, choline plasmalogen and
            phosphatides, removing the fatty acid attached to the 2-position.
            Requires Ca2+.
REFERENCE   1  [PMID:13723433]
  AUTHORS   DOERY HM, PEARSON JE.
  TITLE     Haemolysins in venoms of Australian snakes. Observations on the
            haemolysins of the venoms of some Australian snakes and the
            separation of phospholipase A from the venom of Pseudechis
            porphyriacus.
  JOURNAL   Biochem. J. 78 (1961) 820-7.
  ORGANISM  Pseudechis porphyriacus
REFERENCE   2  [PMID:15433984]
  AUTHORS   FRAENKEL-CONRAT H, FRAENKEL-CONRAT J.
  TITLE     Inactivation of crotoxin by group-specific reagents.
  JOURNAL   Biochim. Biophys. Acta. 5 (1950) 98-104.
  ORGANISM  rotalus terrificus terrificus
REFERENCE   3
  AUTHORS   Hanahan, D.J., Brockerhoff, H. and Barron, E.J.
  TITLE     The site of attack of phospholipase (lecithinase) A on lecithin: a
            re-evaluation. Position of fatty acids on lecithins and
            triglycerides.
  JOURNAL   J. Biol. Chem. 235 (1960) 1917-1923.
  ORGANISM  Crotalus adamanteus
REFERENCE   4
  AUTHORS   Moore, J.H. and Williams, D.L.
  TITLE     Some observations on the specificity of phospholipase A.
  JOURNAL   Biochim. Biophys. Acta 84 (1964) 41-54.
  ORGANISM  Crotalus adamanteus, pig [GN:ssc]
REFERENCE   5
  AUTHORS   Saito, K. and Hanahan, D.J.
  TITLE     A study of the purification and properties of the phospholipase A of
            Crotalus adamanteus venom.
  JOURNAL   Biochemistry 1 (1962) 521-532.
  ORGANISM  Crotalus adamanteus
REFERENCE   6  [PMID:6252969]
  AUTHORS   van den Bosch H.
  TITLE     Intracellular phospholipases A.
  JOURNAL   Biochim. Biophys. Acta. 604 (1980) 191-246.
  ORGANISM  Crotalus adamanteus
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
            PATH: map00565  Ether lipid metabolism
            PATH: map00590  Arachidonic acid metabolism
            PATH: map00591  Linoleic acid metabolism
            PATH: map00592  alpha-Linolenic acid metabolism
            PATH: map04010  MAPK signaling pathway
            PATH: map04370  VEGF signaling pathway
            PATH: map04664  Fc epsilon RI signaling pathway
            PATH: map04730  Long-term depression
            PATH: map04912  GnRH signaling pathway
ORTHOLOGY   KO: K01047  phospholipase A2
GENES       HSA: 26279(PLA2G2D) 30814(PLA2G2E) 50487(PLA2G3) 5319(PLA2G1B)
                 5320(PLA2G2A) 5321(PLA2G4A) 5322(PLA2G5) 64600(PLA2G2F)
                 81579(PLA2G12A) 8398(PLA2G6) 8399(PLA2G10) 84647(PLA2G12B)
            PTR: 466292(PLA2G12B) 469137(PLA2G2C) 469200(PLA2G2D)
            MCC: 704520(PLA2G2A) 704735(LOC704735)
            MMU: 18778(Pla2g1b) 18780(Pla2g2a) 18781(Pla2g2c) 18782(Pla2g2d)
                 18783(Pla2g4a) 18784(Pla2g5) 26565(Pla2g10) 26970(Pla2g2e)
                 26971(Pla2g2f) 329502(Pla2g4e) 53357(Pla2g6) 66350(Pla2g12a)
                 69836(Pla2g12b)
            RNO: 24653(Pla2g4a) 29354(Pla2g5) 29359(Pla2g10) 29387(Pla2g2c)
                 29526(Pla2g1b) 29692(Pla2g2a) 360426(Pla2g6)
                 362039(Pla2g12a_predicted)
            CFA: 404011(PLA2G1B) 478207(PLA2G5) 478514(PLA2G12A)
                 481256(PLA2G6) 487396(PLA2G2C) 487397(PLA2G2F) 487398(PLA2G2D)
                 489045(PLA2G12B)
            BTA: 282457(PLA2G1B) 494318(PLA2G2D1) 503625(PLA2G2D4)
            SSC: 445525(PLA2G1B)
            GGA: 416425(PLA2G10) 416980(PLA2G1B) 418028(PLA2G6)
                 423705(PLA2G12B) 426747(LOC426747) 426748(PLA2G2A)
                 770292(LOC770292) 771655(PLA2G5) 772082(PLA2G12A)
            XLA: 380561(pla2g4a) 443906(MGC80173) 447090(MGC85254)
            SPU: 585809(LOC585809) 590364(LOC590364) 752200(LOC752200)
                 757138(LOC757138) 759233(LOC759233) 764528(LOC764528)
            DME: Dmel_CG10706(SK) Dmel_CG11124(sPLA2) Dmel_CG14507
                 Dmel_CG17035(GXIVsPLA2) Dmel_CG4346(rad)
            CEL: C03H5.4(phospholipase) C07E3.9
            OSA: 4333862
            AFM: AFUA_2G11970 AFUA_5G01340
            UMA: UM05871.1
            ECW: EcE24377A_4342(pldA)
            ECX: EcHS_A4045
            BPM: BURPS1710b_A0715
            APE: APE_2325
STRUCTURES  PDB: 1A2A  1A3D  1A3F  1AE7  1AOK  1AYP  1B4W  1BBC  1BCI  1BJJ  
                 1BK9  1BP2  1BPQ  1BUN  1BVM  1C1J  1C74  1CEH  1CJY  1CL5  
                 1CLP  1DB4  1DB5  1DCY  1DPY  1FAZ  1FDK  1FE5  1FX9  1FXF  
                 1G0Z  1G2X  1G4I  1GH4  1GMZ  1GOD  1GP7  1HN4  1IJL  1IRB  
                 1IT4  1IT5  1J1A  1JIA  1JLT  1JQ8  1JQ9  1KP4  1KPM  1KQU  
                 1KVO  1KVW  1KVX  1KVY  1L8S  1LE6  1LE7  1LN8  1LWB  1M8R  
                 1M8S  1M8T  1MF4  1MG6  1MH2  1MH7  1MH8  1MKS  1MKT  1MKU  
                 1MKV  1N28  1N29  1O2E  1O3W  1OQS  1OWS  1OXL  1OXR  1OYF  
                 1OZ6  1OZY  1P2P  1P7O  1PA0  1PC9  1PIR  1PIS  1PO8  1POA  
                 1POB  1POC  1POD  1POE  1PP2  1PPA  1PSH  1PSJ  1PWO  1Q6V  
                 1Q7A  1QLL  1RGB  1RLW  1S6B  1S8G  1S8H  1S8I  1SFV  1SFW  
                 1SKG  1SQZ  1SV3  1SV9  1SXK  1SZ8  1T37  1TC8  1TD7  1TDV  
                 1TG1  1TG4  1TGM  1TH6  1TJ9  1TJK  1TJQ  1TK4  1TP2  1U4J  
                 1U73  1UNE  1VAP  1VIP  1VKQ  1VL9  1XXS  1XXW  1Y38  1Y4L  
                 1Y6O  1Y6P  1Y75  1YXH  1YXL  1Z76  1ZL7  1ZLB  1ZM6  1ZR8  
                 1ZWP  1ZYX  2ARM  2AZY  2AZZ  2B00  2B01  2B03  2B04  2B17  
                 2B96  2BAX  2BCH  2BD1  2BPP  2DO2  2DPZ  2DV8  2FNX  2G58  
                 2GNS  2H4C  2I0U  2NOT  2O1N  2OLI  2OSH  2OSN  2OTF  2OTH  
                 2OUB  2OYF  2PB8  2PHI  2PMJ  2PVT  2PWS  2PYC  2Q1P  2QU9  
                 2QUE  2QVD  2RD4  3BP2  3P2P  4BP2  4P2P  5P2P  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.4
            ExPASy - ENZYME nomenclature database: 3.1.1.4
            ExplorEnz - The Enzyme Database: 3.1.1.4
            ERGO genome analysis and discovery system: 3.1.1.4
            BRENDA, the Enzyme Database: 3.1.1.4
            CAS: 9001-84-7
///
ENTRY       EC 3.1.1.5                  Enzyme
NAME        lysophospholipase;
            lecithinase B;
            lysolecithinase;
            phospholipase B;
            lysophosphatidase;
            lecitholipase;
            phosphatidase B;
            lysophosphatidylcholine hydrolase;
            lysophospholipase A1;
            lysophopholipase L2;
            lysophospholipase transacylase;
            neuropathy target esterase;
            NTE;
            NTE-LysoPLA;
            NTE-lysophospholipase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     2-lysophosphatidylcholine acylhydrolase
REACTION    2-lysophosphatidylcholine + H2O = glycerophosphocholine + a
            carboxylate
ALL_REAC    (other) R01309 R02744 R02746 R02747 R03416 R03417 R04499
SUBSTRATE   2-lysophosphatidylcholine [CPD:C04230];
            H2O [CPD:C00001]
PRODUCT     glycerophosphocholine [CPD:C00670];
            carboxylate [CPD:C00060]
REFERENCE   1
  AUTHORS   Abe, M., Ohno, K. and Sato, R.
  TITLE     Possible identity of lysolecithin acyl-hydrolase with
            lysolecithin-lysolecithin acyl-transferase in rat-lung soluble
            fraction.
  JOURNAL   Biochim. Biophys. Acta 369 (1974) 361-370.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Contardi, A. and Ercoli, A.
  TITLE     The enzymic cleavage of lecithin and lysolecithin.
  JOURNAL   Biochem. Z. 261 (1933) 275-302.
REFERENCE   3
  AUTHORS   Dawson, R.M.C.
  TITLE     Studies on the hydrolysis of lecithin by Penicillium notatum
            phospholipase B preparation.
  JOURNAL   Biochem. J. 70 (1958) 559-570.
  ORGANISM  Penicillium notatum
REFERENCE   4
  AUTHORS   Fairbairn, D.
  TITLE     The preparation and properties of a lysophospholipase from
            Penicillium notatum.
  JOURNAL   J. Biol. Chem. 173 (1948) 705-714.
  ORGANISM  Penicillium notatum
REFERENCE   5  [PMID:13032127]
  AUTHORS   SHAPIRO B.
  TITLE     Purification and properties of a lysolecithinase from pancreas.
  JOURNAL   Biochem. J. 53 (1953) 663-6.
  ORGANISM  cow [GN:bta]
REFERENCE   6  [PMID:4693514]
  AUTHORS   van den Bosch H, Aarsman AJ, de Jong JG, van Deenem LL.
  TITLE     Studies on lysophospholipases. I. Purification and some properties
            of a lysophospholipase from beef pancreas.
  JOURNAL   Biochim. Biophys. Acta. 296 (1973) 94-104.
  ORGANISM  cow [GN:bta]
REFERENCE   7  [PMID:7278668]
  AUTHORS   van den Bosch H, Vianen GM, van Heusden GP.
  TITLE     Lysophospholipase--transacylase from rat lung.
  JOURNAL   Methods. Enzymol. 71 Pt C (1981) 513-21.
  ORGANISM  rat [GN:rno]
REFERENCE   8  [PMID:11927584]
  AUTHORS   van Tienhoven M, Atkins J, Li Y, Glynn P.
  TITLE     Human neuropathy target esterase catalyzes hydrolysis of membrane
            lipids.
  JOURNAL   J. Biol. Chem. 277 (2002) 20942-8.
  ORGANISM  human [GN:hsa]
REFERENCE   9  [PMID:12805562]
  AUTHORS   Quistad GB, Barlow C, Winrow CJ, Sparks SE, Casida JE.
  TITLE     Evidence that mouse brain neuropathy target esterase is a
            lysophospholipase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 7983-7.
  ORGANISM  mouse [GN:mmu]
REFERENCE   10 [PMID:9576844]
  AUTHORS   Lush MJ, Li Y, Read DJ, Willis AC, Glynn P.
  TITLE     Neuropathy target esterase and a homologous Drosophila
            neurodegeneration-associated mutant protein contain a novel domain
            conserved from bacteria to man.
  JOURNAL   Biochem. J. 332 ( Pt 1) (1998) 1-4.
  ORGANISM  human [GN:hsa]
REFERENCE   11 [PMID:12640454]
  AUTHORS   Winrow CJ, Hemming ML, Allen DM, Quistad GB, Casida JE, Barlow C.
  TITLE     Loss of neuropathy target esterase in mice links organophosphate
            exposure to hyperactivity.
  JOURNAL   Nat. Genet. 33 (2003) 477-85.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K01048  lysophospholipase
            KO: K06128  lysophospholipase I
            KO: K06129  lysophospholipase III
            KO: K06130  lysophospholipase II
GENES       HSA: 10434(LYPLA1) 11313(LYPLA2) 1178(CLC) 23529(CLCF1)
                 23659(LYPLA3) 29124(LGALS13) 5321(PLA2G4A)
            PTR: 464177(LYPLA1) 469081(LGALS13)
            MCC: 699292(LGALS13)
            MMU: 18777(Lypla1) 18783(Pla2g4a) 192654(Lypla3) 26394(Lypla2)
            RNO: 24653(Pla2g4a) 25514(Lypla1) 83510(Lypla2)
            CFA: 403403(LYPLA3) 487374(LYPLA2) 609018(LYPLA1)
            BTA: 282271(LYPLA3)
            GGA: 419685(LYPLA2) 768530(LYPLA3)
            XLA: 379246(MGC52664) 380561(pla2g4a)
            XTR: 394905(MGC75683)
            DRE: 30554(cpla2) 393722(zgc:73210)
            DME: Dmel_CG18815 Dmel_CG6428
            OSA: 4337344
            SCE: YMR006C(PLB2) YMR008C(PLB1) YOL011W(PLB3)
            PIC: PICST_48846(PLB6) PICST_62092(PLB2) PICST_81360(PLB4)
                 PICST_82807(PLB1)
            CGR: CAGL0J11748g CAGL0J11770g
            SPO: SPAC1786.02 SPAC1A6.03c SPAC1A6.04c SPAC977.09c SPAC977.09ca
                 SPCC1450.09c
            ANI: AN1675.2
            AFM: AFUA_1G03630 AFUA_3G14680 AFUA_4G08720 AFUA_8G04370
            AOR: AO090023000685 AO090701000473
            CNE: CNF02430 CNM00920
            UMA: UM00130.1 UM01035.1
            DDI: DDBDRAFT_0205082
            TBR: Tb927.8.6390
            TCR: 511907.50
            LMA: LmjF24.1840
            EHI: 120.t00014 472.t00001
            ECO: b0494(tesA) b3825(pldB)
            ECJ: JW0483(tesA) JW5584(pldB)
            ECE: Z5346(pldB)
            ECS: ECs4755
            ECC: c0615(tesA) c4747(pldB)
            ECI: UTI89_C0529(tesA) UTI89_C4389(pldB)
            ECP: ECP_4019
            ECV: APECO1_1515(tesA)
            ECW: EcE24377A_0533(tesA) EcE24377A_4346(pldB)
            ECX: EcHS_A0574(tesA) EcHS_A4049
            STY: STY3598(pldB)
            STT: t3336(pldB)
            SPT: SPA3802(pldB)
            SEC: SC3860(pldB)
            STM: STM3961(pldB)
            YPE: YPO3830(pldB)
            YPK: y0400(pldB)
            YPM: YP_3218(pldB2)
            YPA: YPA_0192
            YPN: YPN_0134
            YPS: YPTB0205(pldB)
            YPI: YpsIP31758_0221(pldB)
            SFL: SF3903(pldB)
            SFX: S3852(pldB)
            SFV: SFV_3673(pldB)
            SSN: SSON_3999(pldB)
            SBO: SBO_3837(pldB)
            SDY: SDY_3918(pldB)
            ECA: ECA4169(pldB)
            PLU: plu4619(pldB)
            SPE: Spro_0196 Spro_1157
            HIT: NTHI0764(pldB)
            HSO: HS_0775(pldB)
            PMU: PM1631(pldB)
            MSU: MS0004(pldB)
            ASU: Asuc_0277
            VCH: VC0135
            VVU: VV1_1137
            VVY: VV0096
            VPA: VP2974
            VFI: VF2481
            PPR: PBPRA0137 PBPRB1931
            PMY: Pmen_2558
            ACI: ACIAD1057(tesA)
            SON: SO_4733(lypA)
            SDN: Sden_3669
            SFR: Sfri_0039
            SSE: Ssed_0088 Ssed_2312
            SHE: Shewmr4_3914
            SHM: Shewmr7_4006
            SHN: Shewana3_4119
            ILO: IL2432(pldB)
            CPS: CPS_4384(pldB)
            PHA: PSHAa0373 PSHAa1880(apeA)
            PAT: Patl_0989
            HCH: HCH_01539(pldB)
            AHA: AHA_0036 AHA_3489
            REH: H16_A1312 H16_A3666(pldB)
            MLO: mlr3034
            MES: Meso_2747
            SME: SMc04041(pldB)
            ATU: Atu3886(pldB)
            ATC: AGR_L_1924
            RET: RHE_CH02875 RHE_CH03572(pldB)
            RLE: RL3335 RL4090
            BME: BMEI0552 BMEII0047
            BMF: BAB2_0045
            BMS: BRA0046
            BMB: BruAb2_0046
            OAN: Oant_4281
            BJA: bll7739(pldB)
            BRA: BRADO0400(tesA) BRADO6235
            BBT: BBta_0389(tesA) BBta_1374
            RPA: RPA0888
            RPB: RPB_4534
            RPC: RPC_0764
            RPD: RPD_0871
            RPE: RPE_0686
            NWI: Nwi_2951
            NHA: Nham_1140
            BHE: BH07290
            BQU: BQ05220
            CCR: CC_2253
            SIL: SPO1414
            SIT: TM1040_0570
            RSP: RSP_2418(pldB)
            JAN: Jann_3314
            RDE: RD1_1819(pldB)
            HNE: HNE_0098
            NAR: Saro_1082
            ELI: ELI_01535
            BAN: BA5009
            BAR: GBAA5009
            BAA: BA_5429
            BAT: BAS4654
            BCE: BC1788 BC4753
            BCA: BCE_4904
            BCZ: BCZK4510
            BTK: BT9727_4492
            BTL: BALH_4334
            BCL: ABC1422 ABC2876
            BPU: BPUM_2683(ytpA) BPUM_2912
            SAB: SAB1163
            LLC: LACR_1660
            CAC: CAC2246
            CPE: CPE0944(pldB)
            CPF: CPF_1188
            CTC: CTC00812
            DSY: DSY0424
            MMY: MSC_0837(pldB)
            MMO: MMOB3850(pldB)
            RHA: RHA1_ro02357
            PAC: PPA0594
            RBA: RB668(pldB) RB6876
            LIL: LA3604
STRUCTURES  PDB: 1G86  1HDK  1IVN  1J00  1JRL  1LCL  1QKQ  1U8U  1V2G  2G07  
                 2G08  2G09  2G0A  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.5
            ExPASy - ENZYME nomenclature database: 3.1.1.5
            ExplorEnz - The Enzyme Database: 3.1.1.5
            ERGO genome analysis and discovery system: 3.1.1.5
            BRENDA, the Enzyme Database: 3.1.1.5
            CAS: 9001-85-8
///
ENTRY       EC 3.1.1.6                  Enzyme
NAME        acetylesterase;
            C-esterase (in animal tissues);
            acetic ester hydrolase;
            chloroesterase;
            p-nitrophenyl acetate esterase;
            Citrus acetylesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     acetic-ester acetylhydrolase
REACTION    an acetic ester + H2O = an alcohol + acetate [RN:R00628]
ALL_REAC    R00628
SUBSTRATE   acetic ester [CPD:C01883];
            H2O [CPD:C00001]
PRODUCT     alcohol [CPD:C00069];
            acetate [CPD:C00033]
REFERENCE   1  [PMID:13032041]
  AUTHORS   ALDRIDGE WN.
  TITLE     Serum esterases.  I.  Two types of esterase (A and B) hydrolysing
            p-nitrophenyl acetate, propionate and butyrate, and a method for
            their determination.
  JOURNAL   Biochem. J. 53 (1953) 110-7.
  ORGANISM  rabbit, rat [GN:rno], horse
REFERENCE   2
  AUTHORS   Bergmann, F. and Rimon, S.
  TITLE     Fractionation of C-esterase from the hog's kidney extract.
  JOURNAL   Biochem. J. 77 (1960) 209-214.
  ORGANISM  pig [GN:ssc]
REFERENCE   3
  AUTHORS   Jansen, E.F., Nutting, M.-D.F. and Balls, A.K.
  TITLE     The reversible inhibition of acetylesterase by diisopropyl
            fluorophosphate and tetraethyl pyrophosphate.
  JOURNAL   J. Biol. Chem. 175 (1948) 975-987.
  ORGANISM  citrus, Triticum aestivum [GN:etae]
ORTHOLOGY   KO: K05968  
GENES       ECA: ECA2408(paeX) ECA3252(paeY)
            AZO: azo2361
            BLD: BLi04100
STRUCTURES  PDB: 1BS9  1G66  2AXE  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.6
            ExPASy - ENZYME nomenclature database: 3.1.1.6
            ExplorEnz - The Enzyme Database: 3.1.1.6
            ERGO genome analysis and discovery system: 3.1.1.6
            UM-BBD (Biocatalysis/Biodegradation Database): 3.1.1.6
            BRENDA, the Enzyme Database: 3.1.1.6
            CAS: 9000-82-2
///
ENTRY       EC 3.1.1.7                  Enzyme
NAME        acetylcholinesterase;
            true cholinesterase;
            choline esterase I;
            cholinesterase;
            acetylthiocholinesterase;
            acetylcholine hydrolase;
            acetyl.beta-methylcholinesterase;
            AcCholE
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     acetylcholine acetylhydrolase
REACTION    acetylcholine + H2O = choline + acetate [RN:R01026]
ALL_REAC    R01026
SUBSTRATE   acetylcholine [CPD:C01996];
            H2O [CPD:C00001]
PRODUCT     choline [CPD:C00114];
            acetate [CPD:C00033]
INHIBITOR   Tacrine [CPD:C01453]
COMMENT     Acts on a variety of acetic esters; also catalyses
            transacetylations.
REFERENCE   1
  AUTHORS   Augustinsson, K.-B.
  TITLE     Cholinesterases. A study in comparative enzymology.
  JOURNAL   Acta Physiol. Scand. 15, Suppl. 2 (1948)
REFERENCE   2  [PMID:13522650]
  AUTHORS   BERGMANN F, RIMON S, SEGAL R.
  TITLE     Effect of pH on the activity of eel esterase towards different
            substrates.
  JOURNAL   Biochem. J. 68 (1958) 493-9.
  ORGANISM  cow [GN:bta], rat [GN:rno]
REFERENCE   3  [PMID:5073758]
  AUTHORS   Ciliv G, Ozand PT.
  TITLE     Human erythrocyte acetylcholinesterase purification, properties and
            kinetic behavior.
  JOURNAL   Biochim. Biophys. Acta. 284 (1972) 136-56.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:5238989]
  AUTHORS   Leuzinger W, Baker AL, Cauvin E.
  TITLE     Acetylcholinesterase. II. Crystallization, absorption spectra,
            isoionic point.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 59 (1968) 620-3.
  ORGANISM  Electrophorus electricus
REFERENCE   5  [PMID:14885021]
  AUTHORS   NACHMANSOHN D, WILSON IB.
  TITLE     The enzymic hydrolysis and synthesis of acetylcholine.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 12 (1951) 259-339.
REFERENCE   6  [PMID:14377597]
  AUTHORS   ZITTLE CA, DELLAMONICA ES, CUSTER JH, KRIKORIAN R.
  TITLE     Purification of human red cell acetylcholinesterase by
            electrophoresis, ultracentrifugation and gradient extraction.
  JOURNAL   Arch. Biochem. 56 (1955) 469-75.
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K01049  acetylcholinesterase
GENES       HSA: 43(ACHE)
            MMU: 11423(Ache)
            RNO: 83817(Ache)
            CFA: 489828(ACHE)
            GGA: 396388(ACHE)
            DRE: 114549(ache)
            SPU: 576746(LOC576746)
            DME: Dmel_CG17907(Ace)
            CEL: W09B12.1(ace-1) Y44E3A.2(carboxylesterase)
                 Y48B6A.7(acetylcholinesterase)
            AFM: AFUA_7G01710
            MSM: MSMEG_1432
STRUCTURES  PDB: 1ACJ  1ACL  1AMN  1AX9  1B41  1C2B  1C2O  1CFJ  1DX4  1DX6  
                 1E3Q  1E66  1EA5  1EEA  1EVE  1F8U  1FSS  1GPK  1GPN  1GQR  
                 1GQS  1H22  1H23  1HBJ  1J06  1J07  1JJB  1MAA  1MAH  1N5M  
                 1N5R  1OCE  1ODC  1Q83  1Q84  1QID  1QIE  1QIF  1QIG  1QIH  
                 1QII  1QIJ  1QIK  1QIM  1QO9  1QON  1QTI  1SOM  1U65  1UT6  
                 1VOT  1VXO  1VXR  1VZJ  1W4L  1W6R  1W75  1W76  1ZGB  1ZGC  
                 2ACE  2ACK  2BAG  2C0P  2C0Q  2C4H  2C58  2C5F  2C5G  2CEK  
                 2CKM  2CMF  2DFP  2GYU  2GYV  2GYW  2H9Y  2HA0  2HA2  2HA3  
                 2HA4  2HA5  2HA6  2HA7  2J3Q  2J4F  2JEY  2JEZ  2JF0  2JGE  
                 2JGF  2JGG  2JGH  2JGI  2JGJ  2JGK  2JGL  2JGM  2VB4  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.7
            ExPASy - ENZYME nomenclature database: 3.1.1.7
            ExplorEnz - The Enzyme Database: 3.1.1.7
            ERGO genome analysis and discovery system: 3.1.1.7
            BRENDA, the Enzyme Database: 3.1.1.7
            CAS: 9000-81-1
///
ENTRY       EC 3.1.1.8                  Enzyme
NAME        cholinesterase;
            pseudocholinesterase;
            butyrylcholine esterase;
            non-specific cholinesterase;
            choline esterase II (unspecific);
            benzoylcholinesterase;
            choline esterase;
            butyrylcholinesterase;
            propionylcholinesterase;
            anticholineesterase;
            BtChoEase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     acylcholine acylhydrolase
REACTION    an acylcholine + H2O = choline + a carboxylate [RN:R01029]
ALL_REAC    R01029
SUBSTRATE   acylcholine [CPD:C01777];
            H2O [CPD:C00001]
PRODUCT     choline [CPD:C00114];
            carboxylate [CPD:C00060]
COMMENT     Acts on a variety of choline esters and a few other compounds.
REFERENCE   1
  AUTHORS   Augustinsson, K.-B.
  TITLE     Cholinesterases. A study in comparative enzymology.
  JOURNAL   Acta Physiol. Scand. 15, Suppl. 2 (1948)
REFERENCE   2  [PMID:13638253]
  AUTHORS   AUGUSTINSSON KB, OLSSON B.
  TITLE     Esterases in the milk and blood plasma of swine. I. Substrate
            specificity and electrophoresis studies.
  JOURNAL   Biochem. J. 71 (1959) 477-84.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:13032058]
  AUTHORS   KOELLE GB.
  TITLE     Cholinesterases of the tissues and sera of rabbits.
  JOURNAL   Biochem. J. 53 (1953) 217-26.
  ORGANISM  rabbit
REFERENCE   4  [PMID:14885021]
  AUTHORS   NACHMANSOHN D, WILSON IB.
  TITLE     The enzymic hydrolysis and synthesis of acetylcholine.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 12 (1951) 259-339.
REFERENCE   5
  AUTHORS   Sawyer, C.H.
  TITLE     Hydrolysis of choline esters by liver.
  JOURNAL   Science 101 (1945) 385-386.
REFERENCE   6
  AUTHORS   Strelitz, F.
  TITLE     Studies on cholinesterase. 4. Purification of pseudo-cholinesterase
            from horse serum.
  JOURNAL   Biochem. J. 38 (1944) 86-88.
  ORGANISM  horse
ORTHOLOGY   KO: K01050  cholinesterase
GENES       HSA: 590(BCHE)
            MMU: 12038(Bche)
            RNO: 65036(Bche)
            CFA: 488143(BCHE)
            GGA: 395358(BCHE)
            DME: Dmel_CG1128(alpha-Est9) Dmel_CG1131(alpha-Est10)
            AFM: AFUA_8G04210
STRUCTURES  PDB: 1P0I  1P0M  1P0P  1P0Q  1XLU  1XLV  1XLW  2J4C  2PM8  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.8
            ExPASy - ENZYME nomenclature database: 3.1.1.8
            ExplorEnz - The Enzyme Database: 3.1.1.8
            ERGO genome analysis and discovery system: 3.1.1.8
            BRENDA, the Enzyme Database: 3.1.1.8
            CAS: 9001-08-5
///
ENTRY       EC 3.1.1.9        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
COMMENT     Deleted entry: benzoylcholinesterase; a side reaction of EC 3.1.1.8
            cholinesterase (EC 3.1.1.9 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.9
            ExPASy - ENZYME nomenclature database: 3.1.1.9
            ExplorEnz - The Enzyme Database: 3.1.1.9
            ERGO genome analysis and discovery system: 3.1.1.9
            BRENDA, the Enzyme Database: 3.1.1.9
///
ENTRY       EC 3.1.1.10                 Enzyme
NAME        tropinesterase;
            tropine esterase;
            atropinase;
            atropine esterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     atropine acylhydrolase
REACTION    atropine + H2O = tropine + tropate [RN:R03563]
ALL_REAC    R03563
SUBSTRATE   atropine [CPD:C01479];
            H2O [CPD:C00001]
PRODUCT     tropine [CPD:C00729];
            tropate [CPD:C01456]
COMMENT     Also acts on cocaine and other tropine esters.
REFERENCE   1
  AUTHORS   Glick, D., Glaubach, S. and Moore, D.H.
  TITLE     Azolesterase activities of electrophoretically separated proteins of
            serum.
  JOURNAL   J. Biol. Chem. 144 (1942) 525-528.
  ORGANISM  rabbit
REFERENCE   2  [PMID:4435736]
  AUTHORS   Moog P, Krisch K.
  TITLE     [The purification and characterization of atropine esterase from
            rabbit liver microsomes (author's transl)]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 355 (1974) 529-42.
  ORGANISM  rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.10
            ExPASy - ENZYME nomenclature database: 3.1.1.10
            ExplorEnz - The Enzyme Database: 3.1.1.10
            ERGO genome analysis and discovery system: 3.1.1.10
            BRENDA, the Enzyme Database: 3.1.1.10
            CAS: 59536-71-9
///
ENTRY       EC 3.1.1.11                 Enzyme
NAME        pectinesterase;
            pectin demethoxylase;
            pectin methoxylase;
            pectin methylesterase;
            pectase;
            pectin methyl esterase;
            pectinoesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     pectin pectylhydrolase
REACTION    pectin + n H2O = n methanol + pectate [RN:R02362 R06250]
ALL_REAC    R02362 R06250(G)
SUBSTRATE   pectin [CPD:C00714];
            H2O [CPD:C00001]
PRODUCT     methanol [CPD:C00132];
            pectate [CPD:C00470]
REFERENCE   1
  AUTHORS   Deuel, H. and Stutz, E.
  TITLE     Pectic substances and pectic enzymes.
  JOURNAL   Adv. Enzymol. Relat. Areas Mol. Biol. 20 (1958) 341-382.
REFERENCE   2
  AUTHORS   Lineweaver, H. and Jansen, E.F.
  TITLE     Pectic enzymes.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 267-295.
REFERENCE   3
  AUTHORS   Mills, G.B.
  TITLE     A biochemical study of Pseudomonas prunicola Wormald. I. Pectin
            esterase.
  JOURNAL   Biochem. J. 44 (1949) 302-305.
  ORGANISM  Pseudomonas prunicola
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01051  pectinesterase
GENES       ATH: AT1G53830(ATPME2) AT3G43270
            OSA: 4326549 4345722
            AFM: AFUA_3G07650
            ECO: b0772(ybhC)
            ECJ: JW0755(ybhC)
            ECE: Z0943(ybhC)
            ECS: ECs0800
            ECC: c0849(ybhC)
            ECI: UTI89_C0770(ybhC)
            ECV: APECO1_1317(ybhC)
            STY: STY0819(ybhC)
            STT: t2101(ybhC)
            SPT: SPA1966(ybhC)
            SEC: SC0784(ybhC)
            STM: STM0786(ybhC)
            YPE: YPO0424
            YPK: y3757
            YPM: YP_3757
            YPA: YPA_3861
            YPN: YPN_0294
            YPP: YPDSF_3208
            YPS: YPTB0569
            YPI: YpsIP31758_3511(pemA)
            SFL: SF0893(ybhC)
            SFX: S0940(ybhC)
            SFV: SFV_0755(ybhC)
            SSN: SSON_0745(ybhC)
            SBO: SBO_0659(ybhC)
            ECA: ECA0107(pmeB) ECA3253(pemA)
            XCC: XCC2265
            XCB: XC_1850
            XOO: XOO2696
            XOM: XOO_2543(XOO2543)
            SDE: Sde_0944
            MMW: Mmwyl1_0740
            RSO: RSp0138(pme)
            SUS: Acid_1249 Acid_7771
            BPU: BPUM_1808
            FJO: Fjoh_4096 Fjoh_4248
            HMA: rrnAC0616(pecE)
STRUCTURES  PDB: 1GQ8  1QJV  1XG2  2NSP  2NST  2NT6  2NT9  2NTB  2NTP  2NTQ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.11
            ExPASy - ENZYME nomenclature database: 3.1.1.11
            ExplorEnz - The Enzyme Database: 3.1.1.11
            ERGO genome analysis and discovery system: 3.1.1.11
            BRENDA, the Enzyme Database: 3.1.1.11
            CAS: 9025-98-3
///
ENTRY       EC 3.1.1.12       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
COMMENT     Deleted entry: vitamin A esterase, now believed to be identical with
            EC 3.1.1.1 carboxylesterase (EC 3.1.1.12 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.12
            ExPASy - ENZYME nomenclature database: 3.1.1.12
            ExplorEnz - The Enzyme Database: 3.1.1.12
            ERGO genome analysis and discovery system: 3.1.1.12
            BRENDA, the Enzyme Database: 3.1.1.12
///
ENTRY       EC 3.1.1.13                 Enzyme
NAME        sterol esterase;
            cholesterol esterase;
            cholesteryl ester synthase;
            triterpenol esterase;
            cholesteryl esterase;
            cholesteryl ester hydrolase;
            sterol ester hydrolase;
            cholesterol ester hydrolase;
            cholesterase;
            acylcholesterol lipase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     steryl-ester acylhydrolase
REACTION    a steryl ester + H2O = a sterol + a fatty acid [RN:R02115]
ALL_REAC    R02115 > R01462
SUBSTRATE   steryl ester [CPD:C01958];
            H2O [CPD:C00001]
PRODUCT     sterol [CPD:C00370];
            fatty acid [CPD:C00162]
COMMENT     A group of enzymes of broad specificity, acting on esters of sterols
            and long-chain fatty acids, that may also bring about the
            esterification of sterols. Activated by bile salts.
REFERENCE   1  [PMID:5780846]
  AUTHORS   Hyun J, Kothari H, Herm E, Mortenson J, Treadwell CR, Vahouny GV.
  TITLE     Purification and properties of pancreatic juice cholesterol
            esterase.
  JOURNAL   J. Biol. Chem. 244 (1969) 1937-45.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:19426]
  AUTHORS   Okawa Y, Yamaguchi T.
  TITLE     Studies on sterol-ester hydrolase from Fusarium oxysporum. I.
            Partial purification and properties.
  JOURNAL   J. Biochem. (Tokyo). 81 (1977) 1209-15.
  ORGANISM  Fusarium oxysporum
REFERENCE   3  [PMID:4877146]
  AUTHORS   Vahouny GV, Treadwell CR.
  TITLE     Enzymatic synthesis and hydrolysis of cholesterol esters.
  JOURNAL   Methods. Biochem. Anal. 16 (1968) 219-72.
REFERENCE   4
  AUTHORS   Warnaar, F.
  TITLE     Triterpene ester synthesis in latex of Euphorbia species.
  JOURNAL   Phytochemistry 26 (1987) 2715-2721.
  ORGANISM  mammalian
PATHWAY     PATH: map00120  Bile acid biosynthesis
ORTHOLOGY   KO: K01052  cholesterol esterase
GENES       HSA: 1056(CEL) 3988(LIPA)
            PTR: 466150(LIPA)
            MMU: 12613(Cel) 16889(Lipa)
            RNO: 24254(Cel) 25055(Lip1)
            CFA: 610650(LIPA)
            BTA: 280748(CEL)
            GGA: 417165(CEL) 423789(RCJMB04_5e3)
            XLA: 379474(MGC64411) 380547(cel)
            ANI: AN4684.2
            AFM: AFUA_5G08960
            AOR: AO090020000490
            DDI: DDB_0230058
STRUCTURES  PDB: 1AQL  2BCE  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.13
            ExPASy - ENZYME nomenclature database: 3.1.1.13
            ExplorEnz - The Enzyme Database: 3.1.1.13
            ERGO genome analysis and discovery system: 3.1.1.13
            BRENDA, the Enzyme Database: 3.1.1.13
            CAS: 9026-00-0
///
ENTRY       EC 3.1.1.14                 Enzyme
NAME        chlorophyllase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     chlorophyll chlorophyllidohydrolase
REACTION    chlorophyll + H2O = phytol + chlorophyllide
ALL_REAC    (other) R05618
SUBSTRATE   chlorophyll [CPD:C01793];
            H2O [CPD:C00001]
PRODUCT     phytol [CPD:C01389];
            chlorophyllide [CPD:C02139]
COMMENT     Also catalyses chlorophyllide transfer, e.g. converts chlorophyll to
            methylchlorophyllide.
REFERENCE   1  [PMID:13715233]
  AUTHORS   HOLDEN M.
  TITLE     The breakdown of chlorophyll by chlorophyllase.
  JOURNAL   Biochem. J. 78 (1961) 359-64.
  ORGANISM  Beta vulgaris
REFERENCE   2  [PMID:13756631]
  AUTHORS   KLEIN AO, VISHNIAC W.
  TITLE     Activity and partial purification of chlorophyllase in aqueous
            systems.
  JOURNAL   J. Biol. Chem. 236 (1961) 2544-7.
  ORGANISM  Secale cereale
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K08099  chlorophyllase
GENES       ATH: AT1G19670(ATCLH1) AT5G43860(ATCLH2)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.14
            ExPASy - ENZYME nomenclature database: 3.1.1.14
            ExplorEnz - The Enzyme Database: 3.1.1.14
            ERGO genome analysis and discovery system: 3.1.1.14
            BRENDA, the Enzyme Database: 3.1.1.14
            CAS: 9025-96-1
///
ENTRY       EC 3.1.1.15                 Enzyme
NAME        L-arabinonolactonase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     L-arabinono-1,4-lactone lactonohydrolase
REACTION    L-arabinono-1,4-lactone + H2O = L-arabinonate [RN:R02526]
ALL_REAC    R02526
SUBSTRATE   L-arabinono-1,4-lactone [CPD:C01114];
            H2O [CPD:C00001]
PRODUCT     L-arabinonate [CPD:C00545]
REFERENCE   1
  AUTHORS   Weimberg, R. and Doudoroff, M.
  TITLE     The oxidation of L-arabinose by Pseudomonas saccharophila.
  JOURNAL   J. Biol. Chem. 217 (1955) 607-624.
  ORGANISM  Pseudomonas saccharophila
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.15
            ExPASy - ENZYME nomenclature database: 3.1.1.15
            ExplorEnz - The Enzyme Database: 3.1.1.15
            ERGO genome analysis and discovery system: 3.1.1.15
            BRENDA, the Enzyme Database: 3.1.1.15
            CAS: 9025-95-0
///
ENTRY       EC 3.1.1.16       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
COMMENT     Deleted entry: 4-carboxymethyl-4-hydroxyisocrotonolactonase. This
            reaction was due to a mixture of EC 5.3.3.4 (muconolactone
            Delta-isomerase) and EC 3.1.1.24 (3-oxoadipate enol-lactonase) (EC
            3.1.1.16 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.16
            ExPASy - ENZYME nomenclature database: 3.1.1.16
            ExplorEnz - The Enzyme Database: 3.1.1.16
            ERGO genome analysis and discovery system: 3.1.1.16
            BRENDA, the Enzyme Database: 3.1.1.16
///
ENTRY       EC 3.1.1.17                 Enzyme
NAME        gluconolactonase;
            lactonase;
            aldonolactonase;
            glucono-delta-lactonase;
            gulonolactonase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     D-glucono-1,5-lactone lactonohydrolase
REACTION    D-glucono-1,5-lactone + H2O = D-gluconate [RN:R01519]
ALL_REAC    R01519;
            (other) R02525 R02933 R03751 R04785
SUBSTRATE   D-glucono-1,5-lactone [CPD:C00198];
            H2O [CPD:C00001]
PRODUCT     D-gluconate [CPD:C00257]
COMMENT     Acts on a wide range of hexose-1,5-lactones. The hydrolysis of
            L-gulono-1,5-lactone was previously listed separately.
REFERENCE   1  [PMID:14353869]
  AUTHORS   BRODIE AF, LIPMANN F.
  TITLE     Identification of a gluconolactonase.
  JOURNAL   J. Biol. Chem. 212 (1955) 677-85.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2
  AUTHORS   Bublitz, C. and Lehninger, A.L.
  TITLE     The role of aldonolactonase in the conversion of L-gulonate to
            L-ascorbate.
  JOURNAL   Biochim. Biophys. Acta 47 (1961) 288-297.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Suzuki, K., Kawada, M. and Shimazono, N.
  TITLE     Soluble lactonase. Identity of lactonase I and aldonolactonase with
            gluconolactonase.
  JOURNAL   J. Biochem. (Tokyo) 49 (1961) 448-449.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00030  Pentose phosphate pathway
            PATH: map00053  Ascorbate and aldarate metabolism
            PATH: map00930  Caprolactam degradation
ORTHOLOGY   KO: K01053  gluconolactonase
GENES       PIC: PICST_28583(CGR1)
            ANI: AN8977.2
            AFM: AFUA_1G08990 AFUA_1G11330
            AOR: AO090701000487
            UMA: UM05603.1
            TBR: Tb11.02.4200
            TCR: 503713.30 503945.40
            LMA: LmjF26.2700
            SPE: Spro_3932
            HSO: HS_0766
            PMU: PM1248
            MSU: MS0684
            APL: APL_1565
            XFA: XF1297
            XFT: PD0548
            XCC: XCC3591(GNL) XCC4113(gnl)
            XCB: XC_0553 XC_4205
            XCV: XCV0577(gnl) XCV4353(gnl1)
            XAC: XAC0548(GNL) XAC4248(gnl)
            XOO: XOO4276
            XOM: XOO_4033(XOO4033)
            PST: PSPTO_1345(gnl) PSPTO_2470
            PSB: Psyr_0764 Psyr_2235
            PSP: PSPPH_2952
            PFO: Pfl_2803
            ACI: ACIAD2819
            PAT: Patl_2641
            CSA: Csal_2779
            RSO: RS05371(RSp0824)
            REU: Reut_B4613
            REH: H16_A3012(gnl1) H16_B0345(gnl2) H16_B1441(gnl3)
            BMA: BMAA0036
            BXE: Bxe_B0611 Bxe_C0908 Bxe_C0969
            BCN: Bcen_5466
            BCH: Bcen2424_5396
            BPS: BPSS0035
            BPM: BURPS1710b_A1542
            BBR: BB1048
            POL: Bpro_4512
            AAV: Aave_2596
            AJS: Ajs_1999
            HAR: HEAR0216
            AZO: azo2341(gnl)
            PUB: SAR11_0777(gnl)
            MLO: mll4328
            SME: SMa0196 SMb20453
            SMD: Smed_5316
            ATU: Atu4029
            ATC: AGR_L_1647
            RET: RHE_CH00852 RHE_CH03704(ypch01327) RHE_PC00140(ypc00076)
                 RHE_PF00485(ypf00253)
            RLE: RL0914 RL4240 pRL100387 pRL120288 pRL120777
            BME: BMEI1997
            OAN: Oant_3913
            BJA: bll2817 bll2956 blr6437
            BRA: BRADO1816 BRADO2487 BRADO2582 BRADO3863 BRADO4769 BRADO5762
                 BRADO6760
            BBT: BBta_2136 BBta_2832 BBta_2929 BBta_4803 BBta_6274 BBta_6492
            RPA: RPA3624
            RPE: RPE_2028
            XAU: Xaut_4321
            CCR: CC_1224
            SIL: SPO2559(gnl) SPOA0241
            RDE: RD1_0868(gnl) RD1_3716(gnl)
            MMR: Mmar10_2728
            ZMO: ZMO1649(gnl)
            GOX: GOX1375 GOX1381
            ACR: Acry_2591 Acry_2596
            ABA: Acid345_0646
            SUS: Acid_2801 Acid_7716
            MSM: MSMEG_1274
            SCO: SCO0524(SCF11.04)
            AAU: AAur_0566(gnl)
            KRA: Krad_1491
            SEN: SACE_3449 SACE_3789(gnl)
            STP: Strop_0658
            RBA: RB1022 RB12740(gnl) RB3234 RB5577(gnl)
            SYG: sync_0856 sync_1920
            SYR: SynRCC307_1922
            SYX: SynWH7803_0722
            RRS: RoseRS_2498
            RCA: Rcas_2848
            PTO: PTO0907
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.17
            ExPASy - ENZYME nomenclature database: 3.1.1.17
            ExplorEnz - The Enzyme Database: 3.1.1.17
            ERGO genome analysis and discovery system: 3.1.1.17
            BRENDA, the Enzyme Database: 3.1.1.17
            CAS: 9012-73-1
///
ENTRY       EC 3.1.1.18       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
COMMENT     Deleted entry: aldonolactonase. Now included with EC 3.1.1.17
            gluconolactonase (EC 3.1.1.18 created 1961, deleted 1982)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.18
            ExPASy - ENZYME nomenclature database: 3.1.1.18
            ExplorEnz - The Enzyme Database: 3.1.1.18
            ERGO genome analysis and discovery system: 3.1.1.18
            BRENDA, the Enzyme Database: 3.1.1.18
///
ENTRY       EC 3.1.1.19                 Enzyme
NAME        uronolactonase;
            glucuronolactonase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     D-glucurono-6,2-lactone lactonohydrolase
REACTION    D-glucurono-6,2-lactone + H2O = D-glucuronate [RN:R01484]
ALL_REAC    R01484;
            (other) R01483
SUBSTRATE   D-glucurono-6,2-lactone [CPD:C03387];
            H2O [CPD:C00001]
PRODUCT     D-glucuronate [CPD:C00191]
REFERENCE   1
  AUTHORS   Winkelman, J. and Lehninger, A.L.
  TITLE     Aldono- and uronolactonase of animal tissues.
  JOURNAL   J. Biol. Chem. 233 (1958) 794-799.
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.19
            ExPASy - ENZYME nomenclature database: 3.1.1.19
            ExplorEnz - The Enzyme Database: 3.1.1.19
            ERGO genome analysis and discovery system: 3.1.1.19
            BRENDA, the Enzyme Database: 3.1.1.19
            CAS: 9025-93-8
///
ENTRY       EC 3.1.1.20                 Enzyme
NAME        tannase;
            tannase S;
            tannin acetylhydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     tannin acylhydrolase
REACTION    digallate + H2O = 2 gallate [RN:R00053]
ALL_REAC    R00053
SUBSTRATE   digallate [CPD:C01572];
            H2O [CPD:C00001]
PRODUCT     gallate [CPD:C01424]
COMMENT     Also hydrolyses ester links in other tannins.
REFERENCE   1
  AUTHORS   Dyckerhoff, H. and Armbruster, R.
  TITLE     Zur Kenntnis der Tannase.
  JOURNAL   Hoppe-Seyler's Z. Physiol. Chem. 219 (1933) 38-56.
GENES       AFM: AFUA_4G03470 AFUA_7G06720
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.20
            ExPASy - ENZYME nomenclature database: 3.1.1.20
            ExplorEnz - The Enzyme Database: 3.1.1.20
            ERGO genome analysis and discovery system: 3.1.1.20
            BRENDA, the Enzyme Database: 3.1.1.20
            CAS: 9025-71-2
///
ENTRY       EC 3.1.1.21                 Enzyme
NAME        retinyl-palmitate esterase;
            retinyl palmitate hydrolase;
            retinyl palmitate hydrolyase;
            retinyl ester hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     retinyl-palmitate palmitohydrolase
REACTION    retinyl palmitate + H2O = retinol + palmitate [RN:R02368]
ALL_REAC    R02368
SUBSTRATE   retinyl palmitate [CPD:C02588];
            H2O [CPD:C00001]
PRODUCT     retinol [CPD:C00473];
            palmitate [CPD:C00249]
REFERENCE   1  [PMID:5901057]
  AUTHORS   Mahadevan S, Ayyoub NI, Roels OA.
  TITLE     Hydrolysis of retinol palmitate by rat liver.
  JOURNAL   J. Biol. Chem. 241 (1966) 57-64.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00830  Retinol metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.21
            ExPASy - ENZYME nomenclature database: 3.1.1.21
            ExplorEnz - The Enzyme Database: 3.1.1.21
            ERGO genome analysis and discovery system: 3.1.1.21
            BRENDA, the Enzyme Database: 3.1.1.21
            CAS: 9063-69-8
///
ENTRY       EC 3.1.1.22                 Enzyme
NAME        hydroxybutyrate-dimer hydrolase;
            D-(-)-3-hydroxybutyrate-dimer hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     (R)-3-((R)-3-hydroxybutanoyloxy)butanoate hydroxybutanoylhydrolase
REACTION    (R)-3-((R)-3-hydroxybutanoyloxy)butanoate + H2O = 2
            (R)-3-hydroxybutanoate [RN:R00048]
ALL_REAC    R00048
SUBSTRATE   (R)-3-((R)-3-hydroxybutanoyloxy)butanoate [CPD:C04546];
            H2O [CPD:C00001]
PRODUCT     (R)-3-hydroxybutanoate [CPD:C01089]
REFERENCE   1  [PMID:4954074]
  AUTHORS   Delafield FP, Cooksey KE, Doudoroff M.
  TITLE     beta-Hydroxybutyric dehydrogenase and dimer hydrolase of Pseudomonas
            lemoignei.
  JOURNAL   J. Biol. Chem. 240 (1965) 4023-8.
  ORGANISM  Pseudomonas lemoignei
PATHWAY     PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K07518  hydroxybutyrate-dimer hydrolase
GENES       REH: H16_A1335(phaY2) H16_A2251(phaY1)
            RME: Rmet_1960
            BMA: BMA2028
            BML: BMA10299_A2720
            BPS: BPSL2716
            BPM: BURPS1710b_3200
            BTE: BTH_I1420
            RFR: Rfer_3022
            POL: Bpro_4732
            AZO: azo3634
            RLE: RL1500
            RDE: RD1_3930
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.22
            ExPASy - ENZYME nomenclature database: 3.1.1.22
            ExplorEnz - The Enzyme Database: 3.1.1.22
            ERGO genome analysis and discovery system: 3.1.1.22
            BRENDA, the Enzyme Database: 3.1.1.22
            CAS: 37278-37-8
///
ENTRY       EC 3.1.1.23                 Enzyme
NAME        acylglycerol lipase;
            monoacylglycerol lipase;
            monoacylglycerolipase;
            monoglyceride lipase;
            monoglyceride hydrolase;
            fatty acyl monoester lipase;
            monoacylglycerol hydrolase;
            monoglyceridyllipase;
            monoglyceridase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     glycerol-ester acylhydrolase
REACTION    Hydrolyses glycerol monoesters of long-chain fatty acids
ALL_REAC    (other) R01351 R01352
REFERENCE   1  [PMID:6776896]
  AUTHORS   Mentlein R, Heiland S, Heymann E.
  TITLE     Simultaneous purification and comparative characterization of six
            serine hydrolases from rat liver microsomes.
  JOURNAL   Arch. Biochem. Biophys. 200 (1980) 547-59.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:5916497]
  AUTHORS   Pope JL, McPherson JC, Tidwell HC.
  TITLE     A study of a monoglyceride-hydrolyzing enzyme of intestinal mucosa.
  JOURNAL   J. Biol. Chem. 241 (1966) 2306-10.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00561  Glycerolipid metabolism
ORTHOLOGY   KO: K01054  acylglycerol lipase
GENES       HSA: 11343(MGLL)
            RNO: 29254(Mgll)
            GGA: 416024(MGLL)
            XLA: 447764(MGC84195)
            DRE: 378960(mgll)
            SPU: 594062(LOC594062)
            TET: TTHERM_00582150 TTHERM_00654080 TTHERM_00794420
            TBR: Tb927.4.4360 Tb927.8.8020
            TCR: 506489.20
            LMA: LmjF31.1140
            NOC: Noc_1375 Noc_1728
            BVI: Bcep1808_0979
            BUR: Bcep18194_A4171
            SAL: Sala_0197
            RRU: Rru_A0068
            GKA: GK1825
            MSM: MSMEG_0220
            MGI: Mflv_0518
            MMC: Mmcs_0140
            MKM: Mkms_0149
            MJL: Mjls_0130
            AVA: Ava_4455
            DEB: DehaBAV1_0222
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.23
            ExPASy - ENZYME nomenclature database: 3.1.1.23
            ExplorEnz - The Enzyme Database: 3.1.1.23
            ERGO genome analysis and discovery system: 3.1.1.23
            BRENDA, the Enzyme Database: 3.1.1.23
            CAS: 9040-75-9
///
ENTRY       EC 3.1.1.24                 Enzyme
NAME        3-oxoadipate enol-lactonase;
            carboxymethylbutenolide lactonase;
            beta-ketoadipic enol-lactone hydrolase;
            3-ketoadipate enol-lactonase;
            3-oxoadipic enol-lactone hydrolase;
            beta-ketoadipate enol-lactone hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     4-carboxymethylbut-3-en-4-olide enol-lactonohydrolase
REACTION    3-oxoadipate enol-lactone + H2O = 3-oxoadipate [RN:R02991]
ALL_REAC    R02991
SUBSTRATE   3-oxoadipate enol-lactone [CPD:C03586];
            H2O [CPD:C00001]
PRODUCT     3-oxoadipate [CPD:C00846]
COMMENT     The enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone
            decarboxylase.
REFERENCE   1  [PMID:5916392]
  AUTHORS   Ornston LN.
  TITLE     The conversion of catechol and protocatechuate to beta-ketoadipate
            by Pseudomonas putida. II. Enzymes of the protocatechuate pathway.
  JOURNAL   J. Biol. Chem. 241 (1966) 3787-94.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2
  AUTHORS   Ornston, L.N.
  TITLE     Conversion of catechol and protocatechuate to beta-ketoadipate
            (Pseudomonas putida).
  JOURNAL   Methods Enzymol. 17A (1970) 529-549.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
ORTHOLOGY   KO: K01055  3-oxoadipate enol-lactonase
GENES       XCC: XCC0370(catD)
            XCB: XC_0382
            XCV: XCV0384
            XAC: XAC0370(catD)
            XOO: XOO0485(catD)
            XOM: XOO_0452(XOO0452)
            PAE: PA0231(pcaD) PA0480
            PAU: PA14_02840(pcaD)
            PAP: PSPA7_0317(pcaD)
            PPU: PP_1380(pcaD)
            PST: PSPTO_3138
            PSB: Psyr_3005
            PSP: PSPPH_1434(catD1) PSPPH_2235(catD2) PSPPH_2566(catD3)
            PFL: PFL_1324(pcaD)
            PFO: Pfl_1274
            PEN: PSEEN1168(pcaD) PSEEN2033
            PCR: Pcryo_1259
            ACI: ACIAD1451(catD) ACIAD1708(pcaD)
            CVI: CV_1331(pcaD)
            RSO: RSc0298(pcaD2) RSc2250(pcaD)
            REU: Reut_A1692 Reut_B5022
            REH: H16_A1968(catD1) H16_B1583(catD2)
            RME: Rmet_4016 Rmet_4676 Rmet_4875
            BMV: BMASAVP1_1203(pcaD)
            BML: BMA10299_1486(pcaD)
            BXE: Bxe_A4238 Bxe_B0595 Bxe_B0646(pcaD)
            BUR: Bcep18194_B3126
            BCN: Bcen_5110
            BCH: Bcen2424_5749
            BPS: BPSS0046
            BPM: BURPS1710b_2216 BURPS1710b_A1556(pcaD) BURPS1710b_A2497
            BPL: BURPS1106A_A0057(pcaD)
            BPD: BURPS668_A0070(pcaD)
            BTE: BTH_II0049
            BPE: BP0225(catD2)
            BPA: BPP0408(catD2)
            BBR: BB0410(catD2)
            POL: Bpro_1857
            AAV: Aave_3943
            AJS: Ajs_3547
            MPT: Mpe_A3531
            BBA: Bd2017(pcaD)
            MLO: mll2481 mlr7206
            MES: Meso_0446
            SME: SMb20579(pcaD)
            ATU: Atu4542(pcaD)
            ATC: AGR_L_652
            RET: RHE_PE00059(pcaD)
            RLE: pRL100243 pRL110089
            BME: BMEII0638
            BMF: BAB2_0598(pcaL)
            BMS: BRA0643(pcaL)
            BMB: BruAb2_0583(pcaL)
            BJA: blr5668(pcaD)
            BRA: BRADO2319 BRADO2855(catD)
            BBT: BBta_3352 BBta_5320(catD)
            RPE: RPE_1653
            NWI: Nwi_2207
            CCR: CC_2411
            SIL: SPOA0434(catD)
            SIT: TM1040_0560 TM1040_3567
            RSP: RSP_2251 RSP_3962(pcaD)
            JAN: Jann_1663
            RDE: RD1_3932(pcaD)
            PDE: Pden_1182
            ZMO: ZMO0053(pcaD)
            GBE: GbCGDNIH1_0525
            BCE: BC3312
            BCZ: BCZK2995(pcaD)
            BTK: BT9727_3084(pcaD)
            BTL: BALH_2964(pcaD)
            STH: STH807
            DSY: DSY3635
            MSM: MSMEG_1897(pcaD)
            MMC: Mmcs_1367 Mmcs_1701
            CGL: NCgl2310(cgl2393)
            CGB: cg2626(pcaL) cg2628(pcaI)
            CEF: CE2296
            RHA: RHA1_ro01338(pcaL) RHA1_ro02519(catD)
            SCO: SCO6697(pcaL)
            SMA: SAV1706(pcaL1)
            TFU: Tfu_0874
            SEN: SACE_3511(catD2)
            RXY: Rxyl_1578
            TTH: TTC0341 TTC1376
            HMA: rrnAC0572(catD)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.24
            ExPASy - ENZYME nomenclature database: 3.1.1.24
            ExplorEnz - The Enzyme Database: 3.1.1.24
            ERGO genome analysis and discovery system: 3.1.1.24
            BRENDA, the Enzyme Database: 3.1.1.24
            CAS: 9031-04-3
///
ENTRY       EC 3.1.1.25                 Enzyme
NAME        1,4-lactonase;
            gamma-lactonase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     1,4-lactone hydroxyacylhydrolase
REACTION    a 1,4-lactone + H2O = a 4-hydroxyacid [RN:R03708]
ALL_REAC    R03708 > R02933 R03034
SUBSTRATE   1,4-lactone [CPD:C01770];
            H2O [CPD:C00001]
PRODUCT     4-hydroxyacid [CPD:C01991]
COFACTOR    Calcium [CPD:C00076]
COMMENT     The enzyme is specific for 1,4-lactones with 4-8 carbon atoms. It
            does not hydrolyse simple aliphatic esters, acetylcholine, sugar
            lactones or substituted aliphatic lactones, e.g.
            3-hydroxy-4-butyrolactone; requires Ca2+.
REFERENCE   1  [PMID:4958984]
  AUTHORS   Fishbein WN, Bessman SP.
  TITLE     Purification and properties of an enzyme in human blood and rat
            liver microsomes catalyzing the formation and hydrolysis of
            gamma-lactones. I. Tissue localization, stoichiometry, specificity,
            distinction from esterase.
  JOURNAL   J. Biol. Chem. 241 (1966) 4835-41.
  ORGANISM  human [GN:hsa], rat [GN:rno]
REFERENCE   2  [PMID:4958985]
  AUTHORS   Fishbein WN, Bessman SP.
  TITLE     Purification and properties of an enzyme in human blood and rat
            liver microsomes catalyzing the formation and hydrolysis of
            gamma-lactones. II. Metal ion effects, kinetics, and equilibra.
  JOURNAL   J. Biol. Chem. 241 (1966) 4842-7.
  ORGANISM  human [GN:hsa], rat [GN:rno]
PATHWAY     PATH: map00052  Galactose metabolism
            PATH: map00053  Ascorbate and aldarate metabolism
STRUCTURES  PDB: 2DG0  2DG1  2DSO  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.25
            ExPASy - ENZYME nomenclature database: 3.1.1.25
            ExplorEnz - The Enzyme Database: 3.1.1.25
            ERGO genome analysis and discovery system: 3.1.1.25
            BRENDA, the Enzyme Database: 3.1.1.25
            CAS: 37278-38-9
///
ENTRY       EC 3.1.1.26                 Enzyme
NAME        galactolipase;
            galactolipid lipase;
            polygalactolipase;
            galactolipid acylhydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     1,2-diacyl-3-beta-D-galactosyl-sn-glycerol acylhydrolase
REACTION    1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + 2 H2O =
            3-beta-D-galactosyl-sn-glycerol + 2 carboxylates [RN:R03467]
ALL_REAC    R03467;
            (other) R04471
SUBSTRATE   1,2-diacyl-3-beta-D-galactosyl-sn-glycerol [CPD:C03692];
            H2O [CPD:C00001]
PRODUCT     3-beta-D-galactosyl-sn-glycerol [CPD:C05401];
            carboxylate [CPD:C00060]
COMMENT     Also acts on
            2,3-di-O-acyl-1-O-(6-O-alpha-D-galactosyl-beta-D-galactosyl)-D-glyce
            rol, and phosphatidylcholine and other phospholipids.
REFERENCE   1  [PMID:5784904]
  AUTHORS   Helmsing PJ.
  TITLE     Purification and properties of galactolipase.
  JOURNAL   Biochim. Biophys. Acta. 178 (1969) 519-33.
  ORGANISM  Phaseolus multiflorus
REFERENCE   2  [PMID:236765]
  AUTHORS   Hirayama O, Matsuda H, Takeda H, Maenaka K, Takatsuka H.
  TITLE     Purification and properties of a lipid acyl-hydrolase from potato
            tubers.
  JOURNAL   Biochim. Biophys. Acta. 384 (1975) 127-37.
  ORGANISM  Solanum tuberosum [GN:estu]
PATHWAY     PATH: map00561  Glycerolipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.26
            ExPASy - ENZYME nomenclature database: 3.1.1.26
            ExplorEnz - The Enzyme Database: 3.1.1.26
            ERGO genome analysis and discovery system: 3.1.1.26
            BRENDA, the Enzyme Database: 3.1.1.26
            CAS: 37278-40-3
///
ENTRY       EC 3.1.1.27                 Enzyme
NAME        4-pyridoxolactonase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     4-pyridoxolactone lactonohydrolase
REACTION    4-pyridoxolactone + H2O = 4-pyridoxate [RN:R02992]
ALL_REAC    R02992
SUBSTRATE   4-pyridoxolactone [CPD:C00971];
            H2O [CPD:C00001]
PRODUCT     4-pyridoxate [CPD:C00847]
REFERENCE   1  [PMID:4306030]
  AUTHORS   Burg RW, Snell EE.
  TITLE     The bacterial oxidation of vitamin B6. VI. Pyridoxal dehydrogenase
            and 4-pyridoxolactonase.
  JOURNAL   J. Biol. Chem. 244 (1969) 2585-9.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00750  Vitamin B6 metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.27
            ExPASy - ENZYME nomenclature database: 3.1.1.27
            ExplorEnz - The Enzyme Database: 3.1.1.27
            ERGO genome analysis and discovery system: 3.1.1.27
            BRENDA, the Enzyme Database: 3.1.1.27
            CAS: 37278-41-4
///
ENTRY       EC 3.1.1.28                 Enzyme
NAME        acylcarnitine hydrolase;
            high activity acylcarnitine hydrolase;
            HACH;
            carnitine ester hydrolase;
            palmitoylcarnitine hydrolase;
            palmitoyl-L-carnitine hydrolase;
            long-chain acyl-L-carnitine hydrolase;
            palmitoyl carnitine hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     O-acylcarnitine acylhydrolase
REACTION    O-acylcarnitine + H2O = a fatty acid + L-carnitine [RN:R01924]
ALL_REAC    R01924
SUBSTRATE   O-acylcarnitine [CPD:C02301];
            H2O [CPD:C00001]
PRODUCT     fatty acid [CPD:C00162];
            L-carnitine [CPD:C00318]
COMMENT     Acts on higher fatty acid (C6 to C18) esters of L-carnitine; highest
            activity is with O-decanoyl-L-carnitine.
REFERENCE   1  [PMID:5806585]
  AUTHORS   Mahadevan S, Sauer F.
  TITLE     Carnitine ester hydrolase of rat liver.
  JOURNAL   J. Biol. Chem. 244 (1969) 4448-53.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4026306]
  AUTHORS   Mentlein R, Reuter G, Heymann E.
  TITLE     Specificity of two different purified acylcarnitine hydrolases from
            rat liver, their identity with other carboxylesterases, and their
            possible function.
  JOURNAL   Arch. Biochem. Biophys. 240 (1985) 801-10.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.28
            ExPASy - ENZYME nomenclature database: 3.1.1.28
            ExplorEnz - The Enzyme Database: 3.1.1.28
            ERGO genome analysis and discovery system: 3.1.1.28
            BRENDA, the Enzyme Database: 3.1.1.28
            CAS: 37278-42-5
///
ENTRY       EC 3.1.1.29                 Enzyme
NAME        aminoacyl-tRNA hydrolase;
            aminoacyl-transfer ribonucleate hydrolase;
            N-substituted aminoacyl transfer RNA hydrolase;
            peptidyl-tRNA hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     aminoacyl-tRNA aminoacylhydrolase
REACTION    N-Substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA
            [RN:R04238]
ALL_REAC    R04238
SUBSTRATE   N-Substituted aminoacyl-tRNA [CPD:C03880];
            H2O [CPD:C00001]
PRODUCT     N-substituted amino acid [CPD:C03523];
            tRNA [CPD:C00066]
REFERENCE   1  [PMID:4981785]
  AUTHORS   Jost JP, Bock RM.
  TITLE     Enzymatic hydrolysis of N-substituted aminoacyl transfer ribonucleic
            acid in yeast.
  JOURNAL   J. Biol. Chem. 244 (1969) 5866-73.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K01056  peptidyl-tRNA hydrolase, PTH1 family
            KO: K04794  peptidyl-tRNA hydrolase, PTH2 family
            KO: K05969  
GENES       HSA: 51651(PTRH2)
            MMU: 217057(Ptrh2)
            GGA: 417634(PTRH2)
            SPU: 575194(LOC575194)
            DME: Dmel_CG1307
            OSA: 4323881 4325801 4332828 4337239 4339347
            SCE: YBL057C(PTH2) YHR189W(PTH1)
            AGO: AGOS_ABR210W AGOS_AFR445C
            PIC: PICST_30021 PICST_30737 PICST_64167
            CAL: CaO19_1502(CaO19.1502)
            CGR: CAGL0A04323g CAGL0M07073g
            SPO: SPAC19A8.14 SPBC2D10.15c
            ANI: AN1991.2 AN8832.2
            AFM: AFUA_4G10430 AFUA_5G05940
            AOR: AO090003001169 AO090009000669
            CNE: CNI01630
            UMA: UM01860.1
            DDI: DDBDRAFT_0203421
            PFA: PFD0355c PFI1575c
            CHO: Chro.80369
            TAN: TA06050
            TPV: TP01_0859
            TET: TTHERM_00313840
            TBR: Tb927.7.5520
            TCR: 510303.230
            LMA: LmjF06.0910
            EHI: 178.t00017 46.t00040 77.t00027
            ECO: b1204(pth)
            ECJ: JW1195(pth)
            ECE: Z1975(pth)
            ECS: ECs1709
            ECC: c1662(pth)
            ECI: UTI89_C1398(pth) UTI89_C1405(prfA)
            ECP: ECP_1252
            ECV: APECO1_320(pth)
            ECW: EcE24377A_1351(pth)
            ECX: EcHS_A1309
            STY: STY1909(pth)
            STT: t1093(pth)
            SPT: SPA1090(pth)
            SEC: SC1777(pth)
            STM: STM1783.S(pth)
            YPE: YPO2011(pth)
            YPK: y2297(pth)
            YPM: YP_1859(pth)
            YPA: YPA_1394
            YPN: YPN_1492
            YPP: YPDSF_1108
            YPS: YPTB1999(pth)
            YPI: YpsIP31758_2074(pth)
            SFL: SF1207(pth)
            SFX: S1291(pth)
            SFV: SFV_1218(pth)
            SSN: SSON_1974(pth)
            SBO: SBO_1863(pth)
            SDY: SDY_1253(pth)
            ECA: ECA2184(pth)
            PLU: plu2055(pth)
            BUC: BU190(pth)
            BAS: BUsg184(pth)
            BAB: bbp179(pth)
            BCC: BCc_123(pth)
            WBR: WGLp350(pth)
            SGL: SG1881
            ENT: Ent638_2344
            KPN: KPN_02242(pth)
            SPE: Spro_1984
            BFL: Bfl345(pth)
            BPN: BPEN_355(pth)
            HIN: HI0394(pth)
            HIT: NTHI0514(pth)
            HIP: CGSHiEE_01025
            HIQ: CGSHiGG_05145
            HDU: HD0996(pth)
            HSO: HS_0504(pth)
            PMU: PM0164(pth)
            MSU: MS0556(pth)
            APL: APL_0033(pth)
            ASU: Asuc_1412
            XFA: XF2642
            XFT: PD2014(pth)
            XCC: XCC0875(pth)
            XCB: XC_3356
            XCV: XCV0982(pth)
            XAC: XAC0952(pth)
            XOO: XOO3601(pth)
            XOM: XOO_3403(XOO3403)
            VCH: VC2184
            VCO: VC0395_A1761(pth)
            VVU: VV1_0258
            VVY: VV0925
            VPA: VP0738
            VFI: VF0763
            PPR: PBPRA2850
            PAE: PA4672
            PAU: PA14_61790(pth)
            PAP: PSPA7_5322(pth)
            PPU: PP_0720(pth)
            PPF: Pput_0754
            PST: PSPTO_1102(pth)
            PSB: Psyr_0942
            PSP: PSPPH_0989(pth)
            PFL: PFL_5167(pth)
            PFO: Pfl_4755 Pfl_5036
            PEN: PSEEN0855(pth)
            PMY: Pmen_1053
            PAR: Psyc_0170(pth)
            PCR: Pcryo_0183
            PRW: PsycPRwf_2107
            ACI: ACIAD2909(pth)
            SON: SO_1184(pth)
            SDN: Sden_0818
            SFR: Sfri_0716
            SAZ: Sama_2572
            SBL: Sbal_3258
            SBM: Shew185_3300
            SLO: Shew_2920
            SPC: Sputcn32_2853
            SSE: Ssed_3468
            SPL: Spea_3134
            SHE: Shewmr4_1007
            SHM: Shewmr7_1072
            SHN: Shewana3_1011
            SHW: Sputw3181_1051
            ILO: IL0931(pth)
            CPS: CPS_3559(pth)
            PHA: PSHAa1052(pth)
            PAT: Patl_2570
            SDE: Sde_3258
            PIN: Ping_0909
            MAQ: Maqu_2367
            CBU: CBU_1841(pth)
            CBD: COXBU7E912_0071(pth)
            LPN: lpg2653(pth)
            LPF: lpl2578(pth)
            LPP: lpp2706(pth)
            MCA: MCA1058(pth)
            FTU: FTT0680c(pth)
            FTF: FTF0680c(pth)
            FTW: FTW_1048(pth)
            FTL: FTL_0956
            FTH: FTH_0934(pth)
            FTA: FTA_1007(pth)
            FTN: FTN_1003(pth)
            TCX: Tcr_0394
            NOC: Noc_0516
            AEH: Mlg_0285
            HHA: Hhal_0987
            HCH: HCH_01723(pth)
            CSA: Csal_1522
            ABO: ABO_0516(pth)
            MMW: Mmwyl1_3606
            AHA: AHA_3156(pth)
            DNO: DNO_0063(pth)
            BCI: BCI_0294(pth)
            RMA: Rmag_1068
            VOK: COSY_0967(pth)
            NME: NMB0795
            NMA: NMA1004(pth)
            NMC: NMC0747(pth)
            NGO: NGO0379
            CVI: CV_4056(pth)
            RSO: RSc0393(pth)
            REU: Reut_A0340
            REH: H16_A0370(pth1) H16_A1169(prfB) H16_A3340(prfA)
                 H16_A3611(pth2)
            RME: Rmet_0287
            BMA: BMA3122(pth)
            BMV: BMASAVP1_A0090(pth)
            BML: BMA10299_A1500(pth)
            BMN: BMA10247_2928(pth)
            BXE: Bxe_A4135
            BVI: Bcep1808_2909
            BUR: Bcep18194_A6134
            BCN: Bcen_2190
            BCH: Bcen2424_2804
            BAM: Bamb_2864
            BPS: BPSL0519(pth)
            BPM: BURPS1710b_0751(pth)
            BPL: BURPS1106A_0583(pth)
            BPD: BURPS668_0567(pth)
            BTE: BTH_I0472(pth)
            PNU: Pnuc_1922
            BPE: BP3123(pth)
            BPA: BPP0819(pth)
            BBR: BB0903(pth)
            RFR: Rfer_1662
            POL: Bpro_1291
            PNA: Pnap_0897
            AAV: Aave_3612
            AJS: Ajs_0893
            VEI: Veis_0949
            MPT: Mpe_A3227
            HAR: HEAR2895(pth)
            MMS: mma_3130
            NEU: NE1824(pth)
            NET: Neut_1142
            NMU: Nmul_A0591
            EBA: ebA1411(pth)
            AZO: azo0753(pth)
            DAR: Daro_3732
            TBD: Tbd_0389
            MFA: Mfla_0676
            HPY: HP1497(pth)
            HPJ: jhp1390(pth)
            HPA: HPAG1_0078 HPAG1_0167 HPAG1_1416
            HHE: HH1495(pth)
            HAC: Hac_1757(pth)
            WSU: WS2078(pth)
            TDN: Tmden_0466
            CJE: Cj0312(pth)
            CJR: CJE0357(pth)
            CJJ: CJJ81176_0334(pth)
            CJU: C8J_0289(pth)
            CJD: JJD26997_1653(pth)
            CFF: CFF8240_0337(pth)
            CCV: CCV52592_1663(pth)
            CHA: CHAB381_1303(pth)
            CCO: CCC13826_0506
            ABU: Abu_0639(pth)
            NIS: NIS_0385(pth)
            SUN: SUN_2060(pth)
            GSU: GSU0663(pth)
            GME: Gmet_2846
            GUR: Gura_3680
            PCA: Pcar_2002
            PPD: Ppro_0745
            DVU: DVU1573(pth)
            DVL: Dvul_1560
            DDE: Dde_2128
            LIP: LI0738
            BBA: Bd2706(pth)
            DPS: DP2732
            ADE: Adeh_0119
            AFW: Anae109_0123
            MXA: MXAN_5077(pth)
            SAT: SYN_02769
            SFU: Sfum_3654
            RPR: RP605(pth)
            RTY: RT0593(pth)
            RCO: RC0931(pth)
            RFE: RF_0353(pth)
            RBE: RBE_0861(pth)
            RAK: A1C_04745
            RBO: A1I_02595
            RCM: A1E_01770
            RRI: A1G_05130
            OTS: OTBS_1803(pth)
            WOL: WD0175(pth)
            WBM: Wbm0093
            AMA: AM1339(pth)
            APH: APH_1301(pth)
            ERU: Erum0910(pth)
            ERW: ERWE_CDS_00880(pth)
            ERG: ERGA_CDS_00840(pth)
            ECN: Ecaj_0091
            ECH: ECH_0141(pth)
            NSE: NSE_0307(pth)
            PUB: SAR11_0096(pth)
            MLO: mlr2694
            MES: Meso_2158
            PLA: Plav_2256
            SME: SMc02693(pth)
            SMD: Smed_2264
            ATU: Atu2230(pth)
            ATC: AGR_C_4055
            RET: RHE_CH03028(pth)
            RLE: RL0038 RL3474(pth)
            BME: BMEI0480
            BMF: BAB1_1552(pth)
            BMS: BR1536(pth)
            BMB: BruAb1_1525(pth)
            BOV: BOV_1485(pth)
            OAN: Oant_1630
            BJA: bll7440(pth)
            BRA: BRADO6007(pth)
            BBT: BBta_1768(pth)
            RPA: RPA4355(pth)
            RPB: RPB_4160
            RPC: RPC_1416
            RPD: RPD_4000
            RPE: RPE_1438
            NWI: Nwi_2511
            NHA: Nham_3102
            BHE: BH11860(pth)
            BQU: BQ03280(pth)
            BBK: BARBAKC583_1000(pth)
            XAU: Xaut_2606
            CCR: CC_0484
            SIL: SPO0811(pth)
            SIT: TM1040_0214
            RSP: RSP_0824(pth)
            RSH: Rsph17029_2483
            RSQ: Rsph17025_0352
            JAN: Jann_3592
            RDE: RD1_3900(pth)
            PDE: Pden_1264
            MMR: Mmar10_0756
            HNE: HNE_1396(pth)
            ZMO: ZMO1911
            NAR: Saro_2116
            SAL: Sala_1618
            SWI: Swit_1378
            ELI: ELI_05835
            GOX: GOX0884 GOX1142
            GBE: GbCGDNIH1_2317
            ACR: Acry_1675
            RRU: Rru_A3747
            MAG: amb4347
            MGM: Mmc1_0822
            ABA: Acid345_4538
            SUS: Acid_7094
            BSU: BG10116(pth)
            BHA: BH0068(spoVC)
            BAN: BA0050(spoVC)
            BAR: GBAA0050(spoVC)
            BAA: BA_0639
            BAT: BAS0050
            BCE: BC0056
            BCA: BCE_0049(spoVC)
            BCZ: BCZK0046(spoVC)
            BCY: Bcer98_0046
            BTK: BT9727_0046(spoVC)
            BTL: BALH_0046(spoVC)
            BLI: BL00517(spoVC)
            BLD: BLi00066(spoVC)
            BCL: ABC0081(pth)
            BAY: RBAM_000620(spoVC)
            BPU: BPUM_0037(spoVC)
            OIH: OB0061
            GKA: GK0046(spoVC)
            GTN: GTNG_0046
            SAU: SA0460(pth)
            SAV: SAV0502(pth)
            SAM: MW0457(pth)
            SAR: SAR0503
            SAS: SAS0459
            SAC: SACOL0546(pth)
            SAB: SAB0451
            SAA: SAUSA300_0480(pth)
            SAO: SAOUHSC_00475
            SAJ: SaurJH9_0524
            SAH: SaurJH1_0537
            SEP: SE2281
            SER: SERP0140(pth)
            SHA: SH2509(pth)
            SSP: SSP2254
            LMO: lmo0213(pth)
            LMF: LMOf2365_0224(pth)
            LIN: lin0245(pth)
            LWE: lwe0175(pth)
            LLA: L0365(pth)
            LLC: LACR_0010
            LLM: llmg_0012(pth)
            SPY: SPy_0007(pth)
            SPZ: M5005_Spy_0005(pth)
            SPM: spyM18_0005(pth)
            SPG: SpyM3_0005(pth)
            SPS: SPs0005
            SPH: MGAS10270_Spy0005(pth)
            SPI: MGAS10750_Spy0005(pth)
            SPJ: MGAS2096_Spy0005(pth)
            SPK: MGAS9429_Spy0005(pth)
            SPF: SpyM50005(pth)
            SPA: M6_Spy0005
            SPB: M28_Spy0005(pth)
            SPN: SP_0005
            SPR: spr0005(pth)
            SPD: SPD_0005(pth)
            SAG: SAG0007(pth)
            SAN: gbs0007
            SAK: SAK_0007(pth)
            SMU: SMU.07(pth)
            STC: str0005(pth)
            STL: stu0005(pth)
            STE: STER_0006
            SSA: SSA_0006(pth)
            SSU: SSU05_0007
            SSV: SSU98_0009
            SGO: SGO_2141(pth)
            LPL: lp_0538(pth)
            LJO: LJ0276
            LAC: LBA0272
            LSA: LSA1605(pth)
            LSL: LSL_1361(pth)
            LDB: Ldb0362(pth)
            LBU: LBUL_0317
            LBR: LVIS_0515
            LCA: LSEI_2548
            LGA: LGAS_0270
            LRE: Lreu_0261
            PPE: PEPE_1553
            EFA: EF0256(pth)
            OOE: OEOE_0182
            LME: LEUM_0398
            STH: STH3238(spoVC)
            CAC: CAC3217(spoVC)
            CPE: CPE2485(spoVC)
            CPF: CPF_2808(pth)
            CPR: CPR_2494(pth)
            CTC: CTC00193
            CNO: NT01CX_1019
            CTH: Cthe_2631
            CDF: CD3502(pth)
            CBO: CBO3540(pth)
            CBA: CLB_3621(pth)
            CBH: CLC_3518(pth)
            CBF: CLI_3760(pth)
            CBE: Cbei_0085
            CKL: CKL_0151(pth)
            AMT: Amet_0158
            CHY: CHY_0196(pth)
            DSY: DSY0179
            DRM: Dred_0109
            SWO: Swol_0070
            CSC: Csac_1205
            TTE: TTE2567(pth)
            MTA: Moth_0079
            MGE: MG_083(PTH)
            MPN: MPN221(pth)
            MPU: MYPU_7810(pth)
            MPE: MYPE1450(pth)
            MGA: MGA_0506(pth)
            MMY: MSC_0954(pth)
            MMO: MMOB5410(pth)
            MHY: mhp177(pth)
            MHJ: MHJ_0200(pth)
            MHP: MHP7448_0204(pth)
            MSY: MS53_0616(pth)
            MCP: MCAP_0105(pth)
            UUR: UU078(pth)
            POY: PAM152(pth)
            AYW: AYWB_567(pth)
            MFL: Mfl077
            MTU: Rv1014c(pth)
            MTC: MT1042(pth)
            MBO: Mb1042c(pth)
            MBB: BCG_1071c(pth)
            MLE: ML0244(pth)
            MPA: MAP0978c(pth)
            MAV: MAV_1151(pth)
            MSM: MSMEG_5432(pth)
            MVA: Mvan_4788
            MGI: Mflv_1938
            MMC: Mmcs_4254
            MKM: Mkms_4340
            MJL: Mjls_4633
            CGL: NCgl0898(cgl0935) NCgl0901(cgl0938)
            CGB: cg1067(pth2) cg1071(pth1)
            CEF: CE1006 CE1011
            CDI: DIP0897 DIP0900
            CJK: jk1495(pthA) jk1496(pthB)
            NFA: nfa48930(pth)
            RHA: RHA1_ro05694
            SCO: SCO3125(pth)
            SMA: SAV3564(pth)
            TWH: TWT651(pth)
            TWS: TW673(pth)
            LXX: Lxx17290(pth)
            CMI: CMM_2269(pthA)
            ART: Arth_1220
            AAU: AAur_1346(pth)
            PAC: PPA0536
            NCA: Noca_0912
            TFU: Tfu_0417
            FRA: Francci3_3951
            FAL: FRAAL6266(pth)
            ACE: Acel_1944
            KRA: Krad_1054
            SEN: SACE_0810(pth)
            STP: Strop_0791
            BLO: BL1026(pth)
            BAD: BAD_0643(pth)
            RXY: Rxyl_0897
            FNU: FN1597
            RBA: RB9922(pth)
            CTR: CT800(pth)
            CTA: CTA_0872(pth)
            CMU: TC0183
            CPN: CPn0950(pth)
            CPA: CP0909
            CPJ: CPj0950(pth)
            CPT: CpB0987
            CCA: CCA00819(pth)
            CAB: CAB788(pth)
            CFE: CF0195(pth)
            PCU: pc1593(spoVc)
            BBU: BB0787(pth)
            BGA: BG0812(pth)
            BAF: BAPKO_0839(pth)
            TPA: TP1011
            TDE: TDE0643(pth)
            LIL: LA2349 LA3820
            LIC: LIC10431 LIC11598(pth)
            LBJ: LBJ_1281(pth-1) LBJ_2589(pth-2)
            LBL: LBL_0523(pth-2) LBL_1506(pth-1)
            SYN: slr0922(PTH)
            SYW: SYNW0271(pth)
            SYC: syc1286_c(pth)
            SYF: Synpcc7942_0227
            SYD: Syncc9605_0265
            SYE: Syncc9902_2079
            SYG: sync_0312(pth)
            SYR: SynRCC307_2340(pth)
            SYX: SynWH7803_0315(pth)
            CYA: CYA_1253(pth)
            CYB: CYB_0725(pth)
            TEL: tll1384(pth)
            GVI: gll0538(pth)
            ANA: all0844
            AVA: Ava_4448
            PMA: Pro0281(pth)
            PMM: PMM0250(pth)
            PMT: PMT1835(pth)
            PMN: PMN2A_1616
            PMI: PMT9312_0252
            PMB: A9601_02721(pth)
            PMC: P9515_02831(pth)
            PMF: P9303_24601(pth) P9303_29401
            PMG: P9301_02731(pth)
            PMH: P9215_02731
            PME: NATL1_03281(pth)
            TER: Tery_2870
            BTH: BT_4588
            BFR: BF1196
            BFS: BF1163(pth)
            PGI: PG0166(pth)
            SRU: SRU_0813
            CHU: CHU_2625(pth)
            GFO: GFO_3503(pth)
            FJO: Fjoh_1128
            FPS: FP0230(pth)
            CTE: CT1252(pth)
            CCH: Cag_1089
            CPH: Cpha266_1409
            PVI: Cvib_0757
            PLT: Plut_1203
            DET: DET0595(pth)
            DEH: cbdb_A576(pth)
            DEB: DehaBAV1_0570
            RRS: RoseRS_1001
            RCA: Rcas_1729
            DRA: DR_2372
            DGE: Dgeo_2056
            TTH: TTC1224
            TTJ: TTHA1588
            AAE: aq_346(pth)
            TMA: TM1626
            TPT: Tpet_1165
            TME: Tmel_0163
            FNO: Fnod_0602
            MJA: MJ0051
            MMP: MMP0609(pth2)
            MMQ: MmarC5_0997
            MMZ: MmarC7_1631
            MAE: Maeo_1251
            MVN: Mevan_1481
            MAC: MA3269
            MBA: Mbar_A3204
            MMA: MM_0112
            MBU: Mbur_1277
            MTP: Mthe_0865
            MHU: Mhun_0809
            MLA: Mlab_1537
            MEM: Memar_1400
            MBN: Mboo_0905
            MTH: MTH1697
            MST: Msp_1156(pth)
            MSI: Msm_0605
            MKA: MK1597
            AFU: AF2095
            HAL: VNG0240a
            HMA: rrnAC1774
            HWA: HQ1279A
            NPH: NP5224A
            TAC: Ta0108
            TVO: TVN0187
            PTO: PTO1103
            PHO: PH1539
            PAB: PAB0429
            PFU: PF1556
            TKO: TK2300
            RCI: RCIX2710(pth)
            APE: APE_1661
            IHO: Igni_0720
            HBU: Hbut_0765
            SSO: SSO0175
            STO: ST0208
            SAI: Saci_0770
            MSE: Msed_0207
            PAI: PAE0710
            PIS: Pisl_0675
            PCL: Pcal_2123
            PAS: Pars_2354
            TPE: Tpen_0684
            NEQ: NEQ244
STRUCTURES  PDB: 1RYB  1WN2  1XTY  2D3K  2E1B  2PTH  2Z2I  2Z2J  2Z2K  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.29
            ExPASy - ENZYME nomenclature database: 3.1.1.29
            ExplorEnz - The Enzyme Database: 3.1.1.29
            ERGO genome analysis and discovery system: 3.1.1.29
            BRENDA, the Enzyme Database: 3.1.1.29
            CAS: 9054-98-2
///
ENTRY       EC 3.1.1.30                 Enzyme
NAME        D-arabinonolactonase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     D-arabinono-1,4-lactone lactonohydrolase
REACTION    D-arabinono-1,4-lactone + H2O = D-arabinonate [RN:R02714]
ALL_REAC    R02714
SUBSTRATE   D-arabinono-1,4-lactone [CPD:C00652];
            H2O [CPD:C00001]
PRODUCT     D-arabinonate [CPD:C00878]
REFERENCE   1
  AUTHORS   Palleroni, N.J. and Doudoroff, M.
  TITLE     Metabolism of carbohydrates by Pseudomonas saccharophilla. III.
            Oxidation of D-arabinose.
  JOURNAL   J. Bacteriol. 74 (1957) 180-185.
  ORGANISM  Pseudomonas saccharophila
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.30
            ExPASy - ENZYME nomenclature database: 3.1.1.30
            ExplorEnz - The Enzyme Database: 3.1.1.30
            ERGO genome analysis and discovery system: 3.1.1.30
            BRENDA, the Enzyme Database: 3.1.1.30
            CAS: 37278-44-7
///
ENTRY       EC 3.1.1.31                 Enzyme
NAME        6-phosphogluconolactonase;
            phosphogluconolactonase;
            6-PGL
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     6-phospho-D-glucono-1,5-lactone lactonohydrolase
REACTION    6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
            [RN:R02035]
ALL_REAC    R02035
SUBSTRATE   6-phospho-D-glucono-1,5-lactone [CPD:C01236];
            H2O [CPD:C00001]
PRODUCT     6-phospho-D-gluconate [CPD:C00345]
COFACTOR    Magnesium [CPD:C00305]
REFERENCE   1  [PMID:14454532]
  AUTHORS   KAWADA M, KAGAWA Y, TAKIGUCHI H, SHIMAZONO N.
  TITLE     Purification of 6-phosphogluconolactonase from rat liver and yeast;
            its separation from gluconolactonase.
  JOURNAL   Biochim. Biophys. Acta. 57 (1962) 404-7.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:11457850]
  AUTHORS   Miclet E, Stoven V, Michels PA, Opperdoes FR, Lallemand JY, Duffieux
            F.
  TITLE     NMR spectroscopic analysis of the first two steps of the
            pentose-phosphate pathway elucidates the role of
            6-phosphogluconolactonase.
  JOURNAL   J. Biol. Chem. 276 (2001) 34840-6.
  ORGANISM  human [GN:hsa], Trypanosoma brucei [GN:tbr], Plasmodium falciparum
            [GN:pfa]
PATHWAY     PATH: map00030  Pentose phosphate pathway
ORTHOLOGY   KO: K01057  6-phosphogluconolactonase
            KO: K07404  6-phosphogluconolactonase
GENES       HSA: 25796(PGLS) 9563(H6PD)
            MMU: 100198(H6pd) 66171(Pgls)
            RNO: 298655(H6pd_predicted)
            CFA: 489642(H6PD) 610090(PGLS)
            GGA: 428188(H6PD) 430442(RCJMB04_14h20)
            SPU: 587057(LOC587057)
            DME: Dmel_CG17333
            CEL: Y57G11C.3
            ATH: AT1G13700 AT3G49360 AT5G24400(EMB2024) AT5G24410 AT5G24420
            OSA: 4333117 4347654
            CME: CMC120C
            SCE: YCR073W-A(SOL2) YGR248W(SOL4) YHR163W(SOL3) YNR034W(SOL1)
            AGO: AGOS_AEL215C AGOS_AER268W
            PIC: PICST_82104(SOL2)
            CGR: CAGL0I02200g CAGL0M06963g CAGL0M10956g
            SPO: SPCC16C4.10
            ANI: AN0285.2
            AFM: AFUA_1G02980
            AOR: AO090005000789
            CNE: CND03390 CNE04030
            UMA: UM03811.1
            ECU: ECU04_0730
            DDI: DDB_0231287(pgl)
            PFA: PF14_0511
            TAN: TA05220
            TPV: TP03_0558
            TCR: 503713.30 503945.40
            ECO: b0767(ybhE)
            ECJ: JW0750(ybhE)
            ECE: Z0938(ybhE)
            ECS: ECs0795
            ECC: c0844(ybhE)
            ECI: UTI89_C0765(ybhE)
            ECP: ECP_0779
            ECV: APECO1_1322(ybhE)
            ECW: EcE24377A_0794(pgl)
            ECX: EcHS_A0821
            STY: STY0818(ybhE)
            STT: t2102(ybhE)
            SPT: SPA1967(ybhE)
            SEC: SC0783(ybhE)
            STM: STM0785(ybhE)
            YPE: YPO1149
            YPK: y3033
            YPM: YP_1011
            YPA: YPA_1056
            YPN: YPN_2852
            YPS: YPTB1180
            YPI: YpsIP31758_2846(pgl)
            SFL: SF0888(ybhE)
            SFX: S0935(ybhE)
            SFV: SFV_0750(ybhE)
            SSN: SSON_0741(ybhE)
            SBO: SBO_0654(ybhE)
            SDY: SDY_2011(ybhE)
            ECA: ECA1403
            PLU: plu1480
            BUC: BU293(ybhE)
            BAS: BUsg282(ybhE)
            BAB: bbp274(ybhE)
            BCC: BCc_179(pgl)
            SGL: SG0900
            SPE: Spro_1307 Spro_4373
            BFL: Bfl341(ybhE)
            BPN: BPEN_351(ybhE)
            HIN: HI0556(devB)
            HIT: NTHI0685(devB)
            HDU: HD0836(pgl)
            HSO: HS_1652(pgl)
            PMU: PM1550(devB)
            MSU: MS0015(nagB)
            APL: APL_1310(pgl)
            XFA: XF1063
            XFT: PD0344(pgl)
            XCC: XCC2138(pgl)
            XCB: XC_1975
            XCV: XCV2235(pgl)
            XAC: XAC2069(pgl)
            XOO: XOO2316(pgl)
            XOM: XOO_2193(XOO2193)
            VCH: VCA0897
            VCO: VC0395_0340(pgl)
            VVU: VV1_2683
            VVY: VV1606
            VPA: VP1709
            VFI: VFA0469
            PPR: PBPRA1443
            PAE: PA3182
            PAU: PA14_23080(pgl)
            PPU: PP_1023(pgl)
            PPF: Pput_3721
            PST: PSPTO_1301(pgl)
            PSB: Psyr_1121
            PSP: PSPPH_1189(pgl)
            PFL: PFL_4609(pgl)
            PFO: Pfl_4362
            PEN: PSEEN4404(pgl)
            SON: SO_2488(pgl)
            SDN: Sden_2078
            SFR: Sfri_1893
            SAZ: Sama_1811
            SBL: Sbal_2240
            SLO: Shew_2047
            SHE: Shewmr4_2045
            SHM: Shewmr7_1930
            SHN: Shewana3_2150
            SHW: Sputw3181_2141
            CPS: CPS_2282(pgl)
            PHA: PSHAa1141(agaI)
            PAT: Patl_0971
            MAQ: Maqu_1833
            LPN: lpg0417(pgl)
            LPF: lpl0460(pgl)
            LPP: lpp0484(pgl)
            MCA: MCA0024(pgl-1) MCA2970(pgl-2)
            TCX: Tcr_1213
            NOC: Noc_1348
            HCH: HCH_00348
            CSA: Csal_2740
            AHA: AHA_3055
            DNO: DNO_1222(pgl)
            BCI: BCI_0244(pgl)
            NME: NMB1391
            NMA: NMA1608(pgl)
            NMC: NMC1330(pgl)
            NGO: NGO0716
            CVI: CV_0146(pgl)
            RSO: RSp1558(pgl)
            REU: Reut_B4086 Reut_B5328
            REH: H16_B2565(pgl)
            RME: Rmet_5800
            BMA: BMA2131(pgl)
            BMV: BMASAVP1_A0779(pgl)
            BML: BMA10299_A2613(pgl)
            BMN: BMA10247_2001(pgl)
            BXE: Bxe_A3453 Bxe_C0539
            BVI: Bcep1808_0882
            BUR: Bcep18194_A4069
            BCN: Bcen_0487
            BCH: Bcen2424_0966
            BAM: Bamb_0826
            BPS: BPSL2613(pgl)
            BPM: BURPS1710b_3089(pgl)
            BPL: BURPS1106A_3054(pgl)
            BPD: BURPS668_3000(pgl)
            BTE: BTH_I1551(pgl)
            NEU: NE1691
            NET: Neut_0430
            NMU: Nmul_A1628
            DAR: Daro_2071
            TBD: Tbd_2121
            MFA: Mfla_0919 Mfla_1063
            HPY: HP1102(devB)
            HPJ: jhp1028
            HPA: HPAG1_1040
            HAC: Hac_0440(pgl)
            CJD: JJD26997_1269(pgl)
            GME: Gmet_2618
            PCA: Pcar_0923
            DVU: DVU2313(pgl)
            DDE: Dde_1324
            ADE: Adeh_1440
            MXA: MXAN_0952(pgl)
            MLO: mll6514
            MES: Meso_0158
            SME: SMc03069(pgl)
            ATU: Atu0599(pgl)
            ATC: AGR_C_1063(6PGL)
            RET: RHE_CH00703(pgl)
            RLE: RL0752(pgl)
            BME: BMEII0512
            BMF: BAB2_0459(pgl)
            BMS: BRA0779(pgl)
            BMB: BruAb2_0453
            BOV: BOV_A0729(pgl)
            BJA: blr6761
            BRA: BRADO5812
            BBT: BBta_6318
            RPA: RPA3637(pgl)
            RPB: RPB_1889
            RPC: RPC_3673
            RPD: RPD_3477
            RPE: RPE_3711
            NWI: Nwi_2644
            NHA: Nham_3272
            BHE: BH03920(pgl)
            BQU: BQ02940(pgl)
            CCR: CC_2056
            SIL: SPO2047(pgl)
            SIT: TM1040_1330
            RSP: RSP_2735(pgl)
            RSH: Rsph17029_1393
            RSQ: Rsph17025_1777
            JAN: Jann_1970
            RDE: RD1_2721(pgl)
            PDE: Pden_1951
            MMR: Mmar10_2641
            HNE: HNE_1739(pgl)
            ZMO: ZMO1478(pgl)
            NAR: Saro_1894
            ELI: ELI_09925
            GOX: GOX1707
            GBE: GbCGDNIH1_0851
            MGM: Mmc1_1586 Mmc1_3705
            ABA: Acid345_2814
            BCY: Bcer98_2410
            BPU: BPUM_2474
            LSL: LSL_1142
            LRE: Lreu_0578
            MTU: Rv1445c(devB)
            MTC: MT1492
            MBO: Mb1480c(devB)
            MBB: BCG_1506c(devB)
            MLE: ML0579(pgl)
            MPA: MAP1174c(devB)
            MAV: MAV_3331(pgl)
            MSM: MSMEG_3099(pgl)
            MMC: Mmcs_2410
            CGL: NCgl1516(cgl1578)
            CGB: cg1780(devB)
            CEF: CE1698
            CDI: DIP1306
            CJK: jk0996(pgl)
            NFA: nfa35770
            RHA: RHA1_ro07182(pgl)
            SCO: SCO1939(SCC22.21)
            SMA: SAV6311(pgl)
            TWH: TWT308(devB)
            TWS: TW464(pgl)
            LXX: Lxx11570(pgl)
            CMI: CMM_1739(pglA)
            AAU: AAur_2092(pgl)
            PAC: PPA1565
            TFU: Tfu_2007
            FRA: Francci3_1645
            FAL: FRAAL4578(devB)
            SEN: SACE_2155(devB)
            BLO: BL0443
            BAD: BAD_0629
            RXY: Rxyl_0053
            RBA: RB9089(pgl)
            CTR: CT186(devB)
            CTA: CTA_0204(devB)
            CMU: TC0458
            CPN: CPn0239(devB)
            CPA: CP0523
            CPJ: CPj0239(devB)
            CPT: CpB0245
            CCA: CCA00539(pgl)
            CAB: CAB525(pgl)
            CFE: CF0469(devB)
            PCU: pc0819(devB)
            BBU: BB0222
            BGA: BG0225(pgl)
            BAF: BAPKO_0230(pgl)
            TPA: TP0477
            LIL: LA1621
            LIC: LIC12161(nagB)
            SYN: sll1479
            SYW: SYNW1120
            SYC: syc0992_c(nagB)
            SYF: Synpcc7942_0529
            SYD: Syncc9605_1257
            SYE: Syncc9902_1225
            SYG: sync_1689(pgl)
            SYR: SynRCC307_1251(pgl)
            SYX: SynWH7803_1296(pgl)
            CYA: CYA_1259(pgl)
            CYB: CYB_2885(pgl)
            TEL: tlr1076
            GVI: glr3180
            ANA: alr1602(devB)
            AVA: Ava_4215
            PMA: Pro0844(nagB)
            PMM: PMM0771
            PMT: PMT0564
            PMN: PMN2A_0177
            PMI: PMT9312_0779
            PMB: A9601_08331
            PMC: P9515_08121
            PMF: P9303_16881
            PMG: P9301_08311
            PME: NATL1_08091
            TER: Tery_0535
            BTH: BT_1220
            BFR: BF1855
            BFS: BF1921(pgl)
            SRU: SRU_0864(pgl)
            CHU: CHU_3561(pgl)
            FJO: Fjoh_2451 Fjoh_4700
            CTE: CT1871
            CCH: Cag_1793
            PLT: Plut_0308
            DGE: Dgeo_1976
            TMA: TM1154
STRUCTURES  PDB: 1PBT  1VL1  2J0E  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.31
            ExPASy - ENZYME nomenclature database: 3.1.1.31
            ExplorEnz - The Enzyme Database: 3.1.1.31
            ERGO genome analysis and discovery system: 3.1.1.31
            BRENDA, the Enzyme Database: 3.1.1.31
            CAS: 37278-45-8
///
ENTRY       EC 3.1.1.32                 Enzyme
NAME        phospholipase A1
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     phosphatidylcholine 1-acylhydrolase
REACTION    phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a
            carboxylate [RN:R01314]
ALL_REAC    R01314 > R01316;
            (other) R02054 R04034 R07860
SUBSTRATE   phosphatidylcholine [CPD:C00157];
            H2O [CPD:C00001]
PRODUCT     2-acylglycerophosphocholine;
            carboxylate [CPD:C00060]
COFACTOR    Calcium [CPD:C00076]
COMMENT     This enzyme has a much broader specificity than EC 3.1.1.4
            phospholipase A2. Requires Ca2+.
REFERENCE   1  [PMID:5657461]
  AUTHORS   Gatt S.
  TITLE     Purification and properties of phospholipase A-1 from rat and calf
            brain.
  JOURNAL   Biochim. Biophys. Acta. 159 (1968) 304-16.
  ORGANISM  rat [GN:rno], cow [GN:bta]
REFERENCE   2  [PMID:4946924]
  AUTHORS   Scandella CJ, Kornberg A.
  TITLE     A membrane-bound phospholipase A1 purified from Escherichia coli.
  JOURNAL   Biochemistry. 10 (1971) 4447-56.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:6252969]
  AUTHORS   van den Bosch H.
  TITLE     Intracellular phospholipases A.
  JOURNAL   Biochim. Biophys. Acta. 604 (1980) 191-246.
  ORGANISM  Escherichia coli [GN:eco], Mycobacterium phlei
REFERENCE   4  [PMID:4858811]
  AUTHORS   van den Bosch H, Aarsman AJ, van Deenen LL.
  TITLE     Isolation and properties of a phospholipase A1 activity from beef
            pancreas.
  JOURNAL   Biochim. Biophys. Acta. 348 (1974) 197-209.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
            PATH: map00592  alpha-Linolenic acid metabolism
ORTHOLOGY   KO: K01058  phospholipase A1
GENES       DME: Dmel_CG4979(sxe2)
            TBR: Tb927.1.4830
            ECO: b3821(pldA)
            ECJ: JW3794(pldA)
            ECE: Z5342(pldA)
            ECS: ECs4751
            ECC: c4742(pldA)
            ECI: UTI89_C4384(pldA)
            ECP: ECP_4015
            ECV: APECO1_2655(pldA)
            ECW: EcE24377A_4342(pldA)
            ECX: EcHS_A4045
            STY: STY3602(pldA)
            STT: t3340(pldA)
            SPT: SPA3798(pldA)
            SEC: SC3856(pldA)
            STM: STM3957(pldA)
            YPE: YPO3834(pldA)
            YPK: y0396(pldA)
            YPM: YP_3214(pldA)
            YPA: YPA_0188 YPA_2439
            YPN: YPN_0130 YPN_1194
            YPP: YPDSF_1565 YPDSF_3451
            YPS: YPTB0201(pldA)
            SFL: SF3899(pldA)
            SFX: S3856(pldA)
            SFV: SFV_3677(pldA)
            SSN: SSON_3995(pldA)
            SBO: SBO_3833(pldA)
            SDY: SDY_3922(pldA)
            ECA: ECA4173(pldA)
            SGL: SG2338
            ENT: Ent638_3975
            SPE: Spro_0192 Spro_3681
            PMU: PM1426
            XCC: XCC1420 XCC2722
            XCB: XC_1394 XC_2818
            XCV: XCV1520(pldA) XCV3039
            XAC: XAC1463 XAC2885
            XOO: XOO2334
            XOM: XOO_2214(XOO2214)
            VVU: VV1_2799
            VVY: VV1466
            VPA: VP1260 VPA0788
            VFI: VF1556
            PPR: PBPRA1301
            PAR: Psyc_0231(pldA)
            PCR: Pcryo_0260
            PRW: PsycPRwf_2026
            ACI: ACIAD1354
            SDN: Sden_0955
            SFR: Sfri_3189
            SAZ: Sama_2893
            SBL: Sbal_3410
            SBM: Shew185_0926
            SLO: Shew_0671
            SPC: Sputcn32_3045
            SSE: Ssed_0681
            SPL: Spea_0661
            SHE: Shewmr4_3074
            SHM: Shewmr7_0898
            SHN: Shewana3_0861
            SHW: Sputw3181_0900
            ILO: IL2489
            CPS: CPS_1960(pldA)
            PHA: PSHAa0175(pldA)
            PAT: Patl_2081
            PIN: Ping_3493
            MAQ: Maqu_0459 Maqu_0625
            CBU: CBU_0489
            TCX: Tcr_0489
            HCH: HCH_01113 HCH_05407
            CSA: Csal_1446
            ABO: ABO_2104(pldA)
            MMW: Mmwyl1_3291
            NME: NMB0464
            NMA: NMA2021
            NGO: NGO1492
            REH: H16_A1139
            BXE: Bxe_A1948
            RFR: Rfer_0525
            POL: Bpro_4284
            MPT: Mpe_A3505
            DAR: Daro_2090
            TBD: Tbd_0096
            HPY: HP0499
            HPA: HPAG1_0475
            HHE: HH0853(pldA)
            HAC: Hac_0820(pldA)
            WSU: WS0018(pldA)
            TDN: Tmden_0016
            CJE: Cj1351(pldA)
            CJR: CJE1540(pldA)
            CJJ: CJJ81176_1350(pldA)
            CJU: C8J_1267(pldA)
            ABU: Abu_0861(pldA)
            CHU: CHU_0769(pldA)
            GFO: GFO_0043
STRUCTURES  PDB: 1FW2  1FW3  1ILD  1ILZ  1IM0  1QD5  1QD6  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.32
            ExPASy - ENZYME nomenclature database: 3.1.1.32
            ExplorEnz - The Enzyme Database: 3.1.1.32
            ERGO genome analysis and discovery system: 3.1.1.32
            BRENDA, the Enzyme Database: 3.1.1.32
            CAS: 9043-29-2
///
ENTRY       EC 3.1.1.33                 Enzyme
NAME        6-acetylglucose deacetylase;
            6-O-acetylglucose deacetylase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     6-acetyl-D-glucose acetylhydrolase
REACTION    6-acetyl-D-glucose + H2O = D-glucose + acetate [RN:R00327]
ALL_REAC    R00327
SUBSTRATE   6-acetyl-D-glucose [CPD:C02655];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031];
            acetate [CPD:C00033]
REFERENCE   1  [PMID:13596370]
  AUTHORS   DUFF RB, WEBLEY DM.
  TITLE     Metabolism of 6-O-acetyl-D-glucopyranose and other monoacetyl-sugars
            by strains of Bacillus megaterium and other soil organisms.
  JOURNAL   Biochem. J. 70 (1958) 520-8.
  ORGANISM  Bacillus megaterium
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.33
            ExPASy - ENZYME nomenclature database: 3.1.1.33
            ExplorEnz - The Enzyme Database: 3.1.1.33
            ERGO genome analysis and discovery system: 3.1.1.33
            BRENDA, the Enzyme Database: 3.1.1.33
            CAS: 37278-46-9
///
ENTRY       EC 3.1.1.34                 Enzyme
NAME        lipoprotein lipase;
            clearing factor lipase;
            diglyceride lipase;
            diacylglycerol lipase;
            postheparin esterase;
            diglyceride lipase;
            postheparin lipase;
            diacylglycerol hydrolase;
            lipemia-clearing factor
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     triacylglycero-protein acylhydrolase
REACTION    triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
ALL_REAC    R01369;
            (other) R01350
SUBSTRATE   triacylglycerol [CPD:C00422];
            H2O [CPD:C00001]
PRODUCT     diacylglycerol [CPD:C00165];
            carboxylate [CPD:C00060]
COMMENT     Hydrolyses triacylglycerols in chylomicrons and low-density
            lipoproteins. Also hydrolyses diacylglycerol.
REFERENCE   1  [PMID:4703566]
  AUTHORS   Egelrud T, Olivecrona T.
  TITLE     Purified bovine milk (lipoprotein) lipase: activity against lipid
            substrates in the absence of exogenous serum factors.
  JOURNAL   Biochim. Biophys. Acta. 306 (1973) 115-27.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:5441398]
  AUTHORS   Fielding CJ.
  TITLE     Human lipoprotein lipase. I. Purification and substrate specificity.
  JOURNAL   Biochim. Biophys. Acta. 206 (1970) 109-17.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:5466051]
  AUTHORS   Greten H, Levy RI, Fales H, Fredrickson DS.
  TITLE     Hydrolysis of diglyceride and glyceryl monoester diethers with
            &quot;lipoprotein lipase&quot;.
  JOURNAL   Biochim. Biophys. Acta. 210 (1970) 39-45.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:5076762]
  AUTHORS   Morley N, Kuksis A.
  TITLE     Positional specificity of lipoprotein lipase.
  JOURNAL   J. Biol. Chem. 247 (1972) 6389-93.
  ORGANISM  cow [GN:bta], rat [GN:rno]
REFERENCE   5  [PMID:5168777]
  AUTHORS   Nilsson-Ehle P, Belfrage P, Borgstrom B.
  TITLE     Purified human lipoprotein lipase: positional specificity.
  JOURNAL   Biochim. Biophys. Acta. 248 (1971) 114-20.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00561  Glycerolipid metabolism
            PATH: map03320  PPAR signaling pathway
            PATH: map05010  Alzheimer's disease
ORTHOLOGY   KO: K01059  lipoprotein lipase
GENES       HSA: 4023(LPL)
            PTR: 464031(LPL)
            MMU: 16956(Lpl) 669888(LOC669888)
            RNO: 24539(Lpl)
            CFA: 403626(LPL)
            BTA: 280843(LPL)
            SSC: 397537(LPL)
            GGA: 396219(LPL)
            DRE: 30354(lpl)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.34
            ExPASy - ENZYME nomenclature database: 3.1.1.34
            ExplorEnz - The Enzyme Database: 3.1.1.34
            ERGO genome analysis and discovery system: 3.1.1.34
            BRENDA, the Enzyme Database: 3.1.1.34
            CAS: 9004-02-8
///
ENTRY       EC 3.1.1.35                 Enzyme
NAME        dihydrocoumarin hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     dihydrocoumarin lactonohydrolase
REACTION    dihydrocoumarin + H2O = melilotate [RN:R03692]
ALL_REAC    R03692
SUBSTRATE   dihydrocoumarin [CPD:C02274];
            H2O [CPD:C00001]
PRODUCT     melilotate [CPD:C01198]
COMMENT     Also hydrolyses some other benzenoid 1,4-lactones.
REFERENCE   1  [PMID:14458747]
  AUTHORS   KOSUGE T, CONN EE.
  TITLE     The metabolism of aromatic compounds in higher plants. V.
            Purification and properties of dihydrocoumarin hydrolase of
            Melilotus alba.
  JOURNAL   J. Biol. Chem. 237 (1962) 1653-6.
  ORGANISM  Melilotus alba
PATHWAY     PATH: map00628  Fluorene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.35
            ExPASy - ENZYME nomenclature database: 3.1.1.35
            ExplorEnz - The Enzyme Database: 3.1.1.35
            ERGO genome analysis and discovery system: 3.1.1.35
            BRENDA, the Enzyme Database: 3.1.1.35
            CAS: 37278-47-0
///
ENTRY       EC 3.1.1.36                 Enzyme
NAME        limonin-D-ring-lactonase;
            limonin-D-ring-lactone hydrolase;
            limonin lactone hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     limonoate-D-ring-lactone lactonohydrolase
REACTION    limonoate D-ring-lactone + H2O = limonoate [RN:R03624]
ALL_REAC    R03624
SUBSTRATE   limonoate D-ring-lactone [CPD:C03514];
            H2O [CPD:C00001]
PRODUCT     limonoate [CPD:C01593]
COMMENT     Limonoate is a triterpenoid.
REFERENCE   1
  AUTHORS   Maier, V.P., Hasegawa, S. and Hera, E.
  TITLE     Limonin D-ring-lactone hydrolase. A new enzyme from Citrus seeds.
  JOURNAL   Phytochemistry 8 (1969) 405-407.
  ORGANISM  Citrus sinensis [GN:ecsi]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.36
            ExPASy - ENZYME nomenclature database: 3.1.1.36
            ExplorEnz - The Enzyme Database: 3.1.1.36
            ERGO genome analysis and discovery system: 3.1.1.36
            BRENDA, the Enzyme Database: 3.1.1.36
            CAS: 9031-17-8
///
ENTRY       EC 3.1.1.37                 Enzyme
NAME        steroid-lactonase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     testololactone lactonohydrolase
REACTION    testololactone + H2O = testolate [RN:R03641]
ALL_REAC    R03641
SUBSTRATE   testololactone [CPD:C04676];
            H2O [CPD:C00001]
PRODUCT     testolate [CPD:C01618]
REFERENCE   1  [PMID:14281950]
  AUTHORS   HOLMLUND CE, BLANK RH.
  TITLE     PREPARATION AND PROPERTIES OF A STEROID LACTONASE.
  JOURNAL   Arch. Biochem. Biophys. 109 (1965) 29-35.
  ORGANISM  Cephalosporium acremonium
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.37
            ExPASy - ENZYME nomenclature database: 3.1.1.37
            ExplorEnz - The Enzyme Database: 3.1.1.37
            ERGO genome analysis and discovery system: 3.1.1.37
            BRENDA, the Enzyme Database: 3.1.1.37
            CAS: 37288-08-7
///
ENTRY       EC 3.1.1.38                 Enzyme
NAME        triacetate-lactonase;
            triacetic lactone hydrolase;
            triacetic acid lactone hydrolase;
            TAL hydrolase;
            triacetate lactone hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     triacetolactone lactonohydrolase
REACTION    triacetate lactone + H2O = triacetate [RN:R03702]
ALL_REAC    R03702
SUBSTRATE   triacetate lactone [CPD:C02752];
            H2O [CPD:C00001]
PRODUCT     triacetate [CPD:C01757]
REFERENCE   1
  AUTHORS   Kato, S., Ueda, H., Nonomura, S. and Tatsumi, C.
  TITLE     [Degradation of dehydroacetic acid by microorganisms. III.
            Properties of triacetic acid lactone hydrolase.].
  JOURNAL   Nippon Nogei Kagaku Kaishi 42 (1968) 596-600.
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.38
            ExPASy - ENZYME nomenclature database: 3.1.1.38
            ExplorEnz - The Enzyme Database: 3.1.1.38
            ERGO genome analysis and discovery system: 3.1.1.38
            BRENDA, the Enzyme Database: 3.1.1.38
            CAS: 9023-02-3
///
ENTRY       EC 3.1.1.39                 Enzyme
NAME        actinomycin lactonase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     actinomycin lactonohydrolase
REACTION    actinomycin + H2O = actinomycinic monolactone [RN:R03711]
ALL_REAC    R03711
SUBSTRATE   actinomycin [CPD:C01775];
            H2O [CPD:C00001]
PRODUCT     actinomycinic monolactone [CPD:C03597]
REFERENCE   1  [PMID:4191854]
  AUTHORS   Hou CT, Perlman D.
  TITLE     Microbial transformations of peptide antibiotics. V. Purification
            and properties of the actinomycin lactonase from Actinoplanes
            missouriensis.
  JOURNAL   J. Biol. Chem. 245 (1970) 1289-95.
  ORGANISM  Actinoplanes missouriensis
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.39
            ExPASy - ENZYME nomenclature database: 3.1.1.39
            ExplorEnz - The Enzyme Database: 3.1.1.39
            ERGO genome analysis and discovery system: 3.1.1.39
            BRENDA, the Enzyme Database: 3.1.1.39
            CAS: 37288-09-8
///
ENTRY       EC 3.1.1.40                 Enzyme
NAME        orsellinate-depside hydrolase;
            lecanorate hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     orsellinate-depside hydrolase
REACTION    orsellinate depside + H2O = 2 orsellinate [RN:R00054]
ALL_REAC    R00054
SUBSTRATE   orsellinate depside [CPD:C02868];
            H2O [CPD:C00001]
PRODUCT     orsellinate [CPD:C01839]
COMMENT     The enzyme will only hydrolyse those substrates based on the
            2,4-dihydroxy-6-methylbenzoate structure that also have a free
            hydroxy group ortho to the depside linkage.
REFERENCE   1  [PMID:5116606]
  AUTHORS   Schultz J, Mosbach K.
  TITLE     Studies on lichen enzymes. Purification and properties of an
            orsellinate depside hydrolase obtained from Lasallia pustulata.
  JOURNAL   Eur. J. Biochem. 22 (1971) 153-7.
  ORGANISM  Lasallia pustulata
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.40
            ExPASy - ENZYME nomenclature database: 3.1.1.40
            ExplorEnz - The Enzyme Database: 3.1.1.40
            ERGO genome analysis and discovery system: 3.1.1.40
            BRENDA, the Enzyme Database: 3.1.1.40
            CAS: 62213-12-1
///
ENTRY       EC 3.1.1.41                 Enzyme
NAME        cephalosporin-C deacetylase;
            cephalosporin C acetyl-hydrolase;
            cephalosporin C acetylase;
            cephalosporin acetylesterase;
            cephalosporin C acetylesterase;
            cephalosporin C acetyl-esterase;
            cephalosporin C deacetylase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     cephalosporin-C acetylhydrolase
REACTION    cephalosporin C + H2O = deacetylcephalosporin C + acetate
            [RN:R03062]
ALL_REAC    R03062
SUBSTRATE   cephalosporin C [CPD:C00916];
            H2O [CPD:C00001]
PRODUCT     deacetylcephalosporin C [CPD:C03112];
            acetate [CPD:C00033]
COMMENT     Hydrolyses the acetyl ester bond on the 10-position of the
            antibiotic cephalosporin C.
REFERENCE   1  [PMID:4519146]
  AUTHORS   Fujisawa Y, Shirafugi H, Kida M, Nara K, Yoneda M, Kanzaki T.
  TITLE     New findings on cephalosporin C biosynthesis.
  JOURNAL   Nat. New. Biol. 246 (1973) 154-5.
  ORGANISM  Cephalosporium sp.
PATHWAY     PATH: map00311  Penicillin and cephalosporin biosynthesis
ORTHOLOGY   KO: K01060  cephalosporin-C deacetylase
GENES       MLO: mlr6993
            RLE: RL2908
            MGM: Mmc1_2518
            BSU: BG11919(cah)
            BHA: BH3326
            BLI: BL01713(cah)
            BLD: BLi00379(cah)
            BCL: ABC1769(cah)
            BAY: RBAM_003420(cah)
            BPU: BPUM_0297(cah)
            SPN: SP_1695
            SPR: spr1538(axe1)
            SAG: SAG0041
            SAN: gbs0040
            SAK: SAK_0074
            SSA: SSA_0070(axe1)
            EFA: EF1236
            CPE: CPE1596
            DSY: DSY0351
            SCO: SCO7057(SC4G1.23c)
            SMA: SAV1302(axe1) SAV1457(axe2)
            TMA: TM0077
STRUCTURES  PDB: 1L7A  1ODS  1ODT  1VLQ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.41
            ExPASy - ENZYME nomenclature database: 3.1.1.41
            ExplorEnz - The Enzyme Database: 3.1.1.41
            ERGO genome analysis and discovery system: 3.1.1.41
            BRENDA, the Enzyme Database: 3.1.1.41
            CAS: 52227-71-1
///
ENTRY       EC 3.1.1.42                 Enzyme
NAME        chlorogenate hydrolase;
            chlorogenase;
            chlorogenic acid esterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     chlorogenate hydrolase
REACTION    chlorogenate + H2O = caffeate + quinate [RN:R02997]
ALL_REAC    R02997
SUBSTRATE   chlorogenate [CPD:C00852];
            H2O [CPD:C00001]
PRODUCT     caffeate [CPD:C01481];
            quinate [CPD:C00296]
COMMENT     Also acts, more slowly, on isochlorogenate. No other substrates are
            known.
REFERENCE   1  [PMID:7385941]
  AUTHORS   Schobel B, Pollmann W.
  TITLE     Isolation and characterization of a chlorogenic acid esterase from
            Aspergillus niger.
  JOURNAL   Z. Naturforsch. [C]. 35 (1980) 209-12.
  ORGANISM  Aspergillus niger
REFERENCE   2  [PMID:7445677]
  AUTHORS   Schobel B, Pollmann W.
  TITLE     [Further characterization of a chlorogenic acid hydrolase from
            Aspergillus niger (author's transl)]
  JOURNAL   Z. Naturforsch. [C]. 35 (1980) 699-701.
  ORGANISM  Aspergillus niger
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.42
            ExPASy - ENZYME nomenclature database: 3.1.1.42
            ExplorEnz - The Enzyme Database: 3.1.1.42
            ERGO genome analysis and discovery system: 3.1.1.42
            BRENDA, the Enzyme Database: 3.1.1.42
            CAS: 74082-59-0
///
ENTRY       EC 3.1.1.43                 Enzyme
NAME        alpha-amino-acid esterase;
            alpha-amino acid ester hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     alpha-amino-acid-ester aminoacylhydrolase
REACTION    an alpha-amino acid ester + H2O = an alpha-amino acid + an alcohol
            [RN:R04191]
ALL_REAC    R04191
SUBSTRATE   alpha-amino acid ester [CPD:C03317];
            H2O [CPD:C00001]
PRODUCT     alpha-amino acid [CPD:C05167];
            alcohol [CPD:C00069]
COMMENT     Also catalyses alpha-aminoacyl transfer to a number of amine
            nucleophiles.
REFERENCE   1
  AUTHORS   Kato, K., Kawahara, K., Takahashi, T. and Kakinuma, A.
  TITLE     Purification of an alpha-amino acid ester hydrolase from Xanthomonas
            citri.
  JOURNAL   Agric. Biol. Chem. 44 (1980) 1069-1074.
  ORGANISM  Xanthomonas citri
REFERENCE   2
  AUTHORS   Kato, K., Kawahara, K., Takahashi, T. and Kakinuma, A.
  TITLE     Substrate specificity of an alpha-amino acid ester hydrolase from
            Xanthomonas citri.
  JOURNAL   Agric. Biol. Chem. 44 (1980) 1075-1081.
  ORGANISM  Xanthomonas citri
REFERENCE   3  [PMID:4424889]
  AUTHORS   Takahashi T, Yamazaki Y, Kato K.
  TITLE     Substrate specificity of an alpha-amino acid ester hydrolase
            produced by Acetobacter turbidans A.T.C.C. 9325.
  JOURNAL   Biochem. J. 137 (1974) 497-503.
  ORGANISM  Acetobacter turbidans
GENES       XCV: XCV2539
            GOX: GOX2492
STRUCTURES  PDB: 1MPX  1NX9  1RYY  2B4K  2B9V  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.43
            ExPASy - ENZYME nomenclature database: 3.1.1.43
            ExplorEnz - The Enzyme Database: 3.1.1.43
            ERGO genome analysis and discovery system: 3.1.1.43
            BRENDA, the Enzyme Database: 3.1.1.43
            CAS: 74506-40-4
///
ENTRY       EC 3.1.1.44                 Enzyme
NAME        4-methyloxaloacetate esterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     oxaloacetate-4-methyl-ester oxaloacetohydrolase
REACTION    oxaloacetate 4-methyl ester + H2O = oxaloacetate + methanol
            [RN:R01144]
ALL_REAC    R01144
SUBSTRATE   oxaloacetate 4-methyl ester [CPD:C03716];
            H2O [CPD:C00001]
PRODUCT     oxaloacetate [CPD:C00036];
            methanol [CPD:C00132]
REFERENCE   1  [PMID:7380811]
  AUTHORS   Donnelly MI, Dagley S.
  TITLE     Production of methanol from aromatic acids by Pseudomonas putida.
  JOURNAL   J. Bacteriol. 142 (1980) 916-24.
  ORGANISM  Pseudomonas putida [GN:ppu]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.44
            ExPASy - ENZYME nomenclature database: 3.1.1.44
            ExplorEnz - The Enzyme Database: 3.1.1.44
            ERGO genome analysis and discovery system: 3.1.1.44
            BRENDA, the Enzyme Database: 3.1.1.44
            CAS: 74812-46-7
///
ENTRY       EC 3.1.1.45                 Enzyme
NAME        carboxymethylenebutenolidase;
            maleylacetate enol-lactonase;
            dienelactone hydrolase;
            carboxymethylene butenolide hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     4-carboxymethylenebut-2-en-4-olide lactonohydrolase
REACTION    4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate
            [RN:R03893]
ALL_REAC    R03893;
            (other) R05510 R05511 R06835 R06838
SUBSTRATE   4-carboxymethylenebut-2-en-4-olide [CPD:C04431];
            H2O [CPD:C00001]
PRODUCT     4-oxohex-2-enedioate [CPD:C02222]
REFERENCE   1  [PMID:7305906]
  AUTHORS   Schmidt E, Knackmuss HJ.
  TITLE     Chemical structure and biodegradability of halogenated aromatic
            compounds. Conversion of chlorinated muconic acids into
            maleoylacetic acid.
  JOURNAL   Biochem. J. 192 (1980) 339-47.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
            PATH: map00627  1,4-Dichlorobenzene degradation
ORTHOLOGY   KO: K01061  carboxymethylenebutenolidase
GENES       HSA: 134147(CMBL)
            SCE: YDL086W
            AGO: AGOS_ADR265C
            PIC: PICST_78962(DLH1)
            CGR: CAGL0L06974g
            ANI: AN5184.2
            AFM: AFUA_1G07130
            AOR: AO090012000964
            CNE: CNA06410
            TET: TTHERM_00594110
            ECO: b3830(ysgA)
            ECE: Z5352
            ECS: ECs4760
            ECC: c4771
            ECI: UTI89_C3421 UTI89_C4410
            ECP: ECP_4039
            ECV: APECO1_2631 APECO1_3423
            STY: STY3592(ysgA)
            STT: t3330(ysgA)
            SPT: SPA3808(ysgA)
            SEC: SC3865(dlhH)
            STM: STM3967(dlhH)
            YPE: YPO3787
            YPK: y0443
            YPM: YP_3262
            YPA: YPA_0237
            YPN: YPN_0177
            YPP: YPDSF_3404
            YPS: YPTB0249
            SFL: SF3908
            SFV: SFV_3668(ysgA)
            SSN: SSON_4005(ysgA)
            SBO: SBO_3844
            SDY: SDY_3913
            ECA: ECA0184
            ENT: Ent638_3409 Ent638_3963
            SPE: Spro_0243
            XCC: XCC2566 XCC2737
            XCB: XC_1376 XC_1552
            XCV: XCV2888 XCV3051
            XAC: XAC2736 XAC2907
            XOO: XOO1437 XOO3274
            XOM: XOO_1321(XOO1321) XOO_3099(XOO3099)
            PSB: Psyr_2534
            PEN: PSEEN1342 PSEEN3627
            SDN: Sden_3046
            SHE: Shewmr4_0833
            SHM: Shewmr7_3190
            SHN: Shewana3_3286 Shewana3_3320
            CPS: CPS_4005
            PAT: Patl_0207 Patl_1546
            CSA: Csal_2697
            MMW: Mmwyl1_3288
            CVI: CV_3204
            RSO: RSc2228(RS01371)
            REU: Reut_A0875 Reut_A3180 Reut_B5577 Reut_B5771 Reut_C6316
                 Reut_C6385 Reut_D6464 Reut_D6472
            RME: Rmet_2622 Rmet_3321 Rmet_3645
            BMA: BMA2838 BMAA0324
            BXE: Bxe_A1127(clcD) Bxe_A3568 Bxe_A4330 Bxe_B0274 Bxe_B0548
                 Bxe_B2832
            BVI: Bcep1808_0236 Bcep1808_4251 Bcep1808_5490 Bcep1808_6461
            BUR: Bcep18194_A3379 Bcep18194_B2216 Bcep18194_C6610
                 Bcep18194_C7069 Bcep18194_C7177
            BCN: Bcen_2831 Bcen_4491 Bcen_5485 Bcen_5840
            BCH: Bcen2424_0276 Bcen2424_3874 Bcen2424_6207 Bcen2424_6771
            BAM: Bamb_0190 Bamb_3245 Bamb_5994 Bamb_6309
            BPS: BPSL3286 BPSS1767
            BPM: BURPS1710b_0053 BURPS1710b_A0848
            BTE: BTH_I3160 BTH_II0609
            PNU: Pnuc_1276 Pnuc_1710
            BPE: BP1256 BP2713
            BPA: BPP1116 BPP1871 BPP2783
            BBR: BB1332 BB2702 BB3237
            RFR: Rfer_3313 Rfer_3810
            POL: Bpro_0241 Bpro_1733 Bpro_2724
            PNA: Pnap_0188 Pnap_2091
            AAV: Aave_0321 Aave_1943
            AJS: Ajs_0260 Ajs_3316
            VEI: Veis_1220
            MPT: Mpe_A3005
            HAR: HEAR0270
            MMS: mma_0324
            AZO: azo2647(dlhH)
            DAR: Daro_0181
            MFA: Mfla_2602
            PLA: Plav_1266
            SME: SMc00817
            SMD: Smed_0381
            RET: RHE_PE00366(ype00187)
            RLE: pRL110484
            OAN: Oant_3327
            BJA: bll0837 bll6841
            BRA: BRADO0895 BRADO1986 BRADO2952 BRADO3398 BRADO5403 BRADO7139
            BBT: BBta_2303 BBta_4308 BBta_4503 BBta_5221 BBta_5888 BBta_7175
                 BBta_7870
            RPA: RPA4832(clcD)
            RPB: RPB_1202
            RPC: RPC_0926
            RPD: RPD_1304
            RPE: RPE_0950
            PDE: Pden_0735
            MMR: Mmar10_2526
            ZMO: ZMO1351(clcD) ZMO1992(clcD)
            NAR: Saro_0139
            SAL: Sala_2285 Sala_2851
            SWI: Swit_0846 Swit_2080 Swit_2842
            GOX: GOX1900
            GBE: GbCGDNIH1_1367
            ACR: Acry_0900 Acry_2181
            RRU: Rru_A2775
            MAG: amb4377
            ABA: Acid345_2787
            SUS: Acid_3046 Acid_3528
            MTU: Rv2054
            MTC: MT2114 MT2835
            MBO: Mb2080
            MLE: ML1444
            MPA: MAP1803
            MSM: MSMEG_3558
            MMC: Mmcs_2499 Mmcs_2750
            MJL: Mjls_2780
            NFA: nfa29410
            RHA: RHA1_ro01784 RHA1_ro02271 RHA1_ro03727
            CMI: CMM_1520
            FRA: Francci3_0536 Francci3_2614
            FAL: FRAAL0697 FRAAL4887 FRAAL5270
            ACE: Acel_1423 Acel_1445
            KRA: Krad_3055
            SEN: SACE_0218 SACE_5348
            RBA: RB5825 RB745 RB8248
            SYN: sll1298(clcD)
            SYW: SYNW0092 SYNW2419
            SYC: syc0574_d syc1415_d(clcD)
            SYF: Synpcc7942_0089 Synpcc7942_0969
            SYD: Syncc9605_0084
            SYG: sync_0089
            SYR: SynRCC307_0089
            SYX: SynWH7803_0144 SynWH7803_2450
            TEL: tlr1423
            GVI: glr3401
            ANA: all0955 alr1077 alr1362 alr4786
            AVA: Ava_0533 Ava_2055 Ava_3733 Ava_4024 Ava_4152
            PMT: PMT1031(clcD)
            PMI: PMT9312_1497
            PMF: P9303_10371
            PMG: P9301_16031
            TER: Tery_0392 Tery_2503
            FJO: Fjoh_4137
            AAE: aq_1997
            PTO: PTO1128
            SSO: SSO2087(clcD)
            STO: ST2511
            SAI: Saci_1718
            MSE: Msed_1285
STRUCTURES  PDB: 1DIN  1GGV  1ZI6  1ZI8  1ZI9  1ZIC  1ZIX  1ZIY  1ZJ4  1ZJ5  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.45
            ExPASy - ENZYME nomenclature database: 3.1.1.45
            ExplorEnz - The Enzyme Database: 3.1.1.45
            ERGO genome analysis and discovery system: 3.1.1.45
            UM-BBD (Biocatalysis/Biodegradation Database): 3.1.1.45
            BRENDA, the Enzyme Database: 3.1.1.45
            CAS: 76689-22-0
///
ENTRY       EC 3.1.1.46                 Enzyme
NAME        deoxylimonate A-ring-lactonase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     deoxylimonate A-ring-lactonohydrolase
REACTION    deoxylimonate + H2O = deoxylimononic acid D-ring-lactone [RN:R03803]
ALL_REAC    R03803
SUBSTRATE   deoxylimonate [CPD:C02027];
            H2O [CPD:C00001]
PRODUCT     deoxylimononic acid D-ring-lactone [CPD:C04251]
COMMENT     The enzyme opens the A-ring-lactone of the triterpenoid deoxylimonic
            acid, leaving the D-ring-lactone intact.
REFERENCE   1
  AUTHORS   Hasegawa, H., Bennett, R.D. and Verdon, C.P.
  TITLE     Metabolism of limonoids via a deoxylimonoid pathway in Citrus.
  JOURNAL   Phytochemistry 19 (1980) 1445-1447.
  ORGANISM  Citrus microcarpa
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.46
            ExPASy - ENZYME nomenclature database: 3.1.1.46
            ExplorEnz - The Enzyme Database: 3.1.1.46
            ERGO genome analysis and discovery system: 3.1.1.46
            BRENDA, the Enzyme Database: 3.1.1.46
            CAS: 75788-82-8
///
ENTRY       EC 3.1.1.47                 Enzyme
NAME        1-alkyl-2-acetylglycerophosphocholine esterase;
            1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetylhydrolase;
            alkylacetyl-GPC:acetylhydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetohydrolase
REACTION    1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O =
            1-alkyl-sn-glycero-3-phosphocholine + acetate [RN:R04452]
ALL_REAC    R04452
SUBSTRATE   1-alkyl-2-acetyl-sn-glycero-3-phosphocholine;
            H2O [CPD:C00001]
PRODUCT     1-alkyl-sn-glycero-3-phosphocholine [CPD:C04317];
            acetate [CPD:C00033]
REFERENCE   1  [PMID:7451433]
  AUTHORS   Blank ML, Lee T, Fitzgerald V, Snyder F.
  TITLE     A specific acetylhydrolase for
            1-alkyl-2-acetyl-sn-glycero-3-phosphocholine (a hypotensive and
            platelet-activating lipid).
  JOURNAL   J. Biol. Chem. 256 (1981) 175-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00565  Ether lipid metabolism
ORTHOLOGY   KO: K01062  1-alkyl-2-acetylglycerophosphocholine esterase
GENES       HSA: 5048(PAFAH1B1) 5049(PAFAH1B2) 5050(PAFAH1B3) 5051(PAFAH2)
            PTR: 462744(PLA2G7)
            MMU: 100163(Pafah2) 18472(Pafah1b1) 18475(Pafah1b2)
                 18476(Pafah1b3) 27226(Pla2g7)
            RNO: 114113(Pafah1b3) 313611(Pafah2) 64189(Pafah1b2)
                 83572(Pafah1b1)
            CFA: 403848(PLA2G7) 476449(PAFAH1B3) 478174(PAFAH2)
            BTA: 282299(PAFAH2) 282311(PLA2G7) 282513(PAFAH1B1)
                 282514(PAFAH1B2) 282515(PAFAH1B3)
            SSC: 397482(PAFAH1B1)
            GGA: 374224(PAFAH1B1) 395816(PLA2G7) 419765(RCJMB04_1f10)
            XLA: 379732(MGC69176) 495446(LOC495446)
            XTR: 403097(TNeu059p06.1)
            DRE: 406470(zgc:77563)
            SPU: 582170(LOC582170) 585843(LOC585843)
            DME: Dmel_CG8440(Lis-1) Dmel_CG8962(Paf-AHalpha)
            CEL: C52B9.7(paf-2) T03F6.5(lis-1)
            CME: CMQ394C
            CGR: CAGL0C02937g
            SPO: SPBC106.11c
            CNE: CNG00990
            UMA: UM03164.1
            DDI: DDB_0219930(lis1)
            TET: TTHERM_00030370 TTHERM_00418380
            TCR: 510659.250
            XCC: XCC1515
            XCB: XC_2719
            XCV: XCV1606
            XAC: XAC1564
            XOO: XOO2079
            XOM: XOO_1958(XOO1958)
            SBM: Shew185_2295
            RLE: RL0666
            SGO: SGO_0288
            FJO: Fjoh_1280
STRUCTURES  PDB: 1BWP  1BWQ  1BWR  1ES9  1FXW  1VYH  1WAB  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.47
            ExPASy - ENZYME nomenclature database: 3.1.1.47
            ExplorEnz - The Enzyme Database: 3.1.1.47
            ERGO genome analysis and discovery system: 3.1.1.47
            BRENDA, the Enzyme Database: 3.1.1.47
            CAS: 76901-00-3
///
ENTRY       EC 3.1.1.48                 Enzyme
NAME        fusarinine-C ornithinesterase;
            ornithine esterase;
            5-N-acyl-L-ornithine-ester hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     N5-acyl-L-ornithine-ester hydrolase
REACTION    N5-acyl-L-ornithine ester + H2O = N5-acyl-L-ornithine + an alcohol
            [RN:R04070]
ALL_REAC    R04070
SUBSTRATE   N5-acyl-L-ornithine ester [CPD:C03625];
            H2O [CPD:C00001]
PRODUCT     N5-acyl-L-ornithine [CPD:C02858];
            alcohol [CPD:C00069]
COMMENT     Hydrolyses the three ornithine ester bonds in fusarinine C. Also
            acts on N5-dinitrophenyl-L-ornithine methyl ester.
REFERENCE   1  [PMID:949472]
  AUTHORS   Emery T.
  TITLE     Fungal ornithine esterases: relationship to iron transport.
  JOURNAL   Biochemistry. 15 (1976) 2723-8.
  ORGANISM  Fusarium roseum, Penicillium sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.48
            ExPASy - ENZYME nomenclature database: 3.1.1.48
            ExplorEnz - The Enzyme Database: 3.1.1.48
            ERGO genome analysis and discovery system: 3.1.1.48
            BRENDA, the Enzyme Database: 3.1.1.48
            CAS: 60202-10-0
///
ENTRY       EC 3.1.1.49                 Enzyme
NAME        sinapine esterase;
            aromatic choline esterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     sinapoylcholine sinapohydrolase
REACTION    sinapoylcholine + H2O = sinapate + choline [RN:R02381]
ALL_REAC    R02381
SUBSTRATE   sinapoylcholine [CPD:C00933];
            H2O [CPD:C00001]
PRODUCT     sinapate [CPD:C00482];
            choline [CPD:C00114]
REFERENCE   1
  AUTHORS   Nurmann, G. and Strack, D.
  TITLE     Sinapine esterase. 1. Characterization of sinapine esterase from
            cotyledons of Raphanus sativus.
  JOURNAL   Z. Naturforsch. C: Biosci. 34 (1979) 715-720.
  ORGANISM  Raphanus sativus
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.49
            ExPASy - ENZYME nomenclature database: 3.1.1.49
            ExplorEnz - The Enzyme Database: 3.1.1.49
            ERGO genome analysis and discovery system: 3.1.1.49
            BRENDA, the Enzyme Database: 3.1.1.49
            CAS: 72506-67-3
///
ENTRY       EC 3.1.1.50                 Enzyme
NAME        wax-ester hydrolase;
            jojoba wax esterase;
            WEH
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     wax-ester acylhydrolase
REACTION    a wax ester + H2O = a long-chain alcohol + a long-chain carboxylate
            [RN:R02042]
ALL_REAC    R02042
SUBSTRATE   wax ester [CPD:C01629];
            H2O [CPD:C00001]
PRODUCT     long-chain alcohol [CPD:C00339];
            long-chain carboxylate [CPD:C00347]
COMMENT     Also acts on long-chain acylglycerol, but not diacyl- or
            triacylglycerols.
REFERENCE   1
  AUTHORS   Huang, A.H.C., Moreau, R.A. and Liu, K.D.F.
  TITLE     Development and properties of a wax ester hydrolase in the
            cotyledons of jojoba seedlings.
  JOURNAL   Plant Physiol. 61 (1978) 339-341.
  ORGANISM  Simmondsia chinensis
REFERENCE   2
  AUTHORS   Moreau, R.A. and Huang, A.H.C.
  TITLE     Enzymes of wax ester catabolism in jojoba.
  JOURNAL   Methods Enzymol. 71 (1981) 804-813.
  ORGANISM  Simmondsia chinensis
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.50
            ExPASy - ENZYME nomenclature database: 3.1.1.50
            ExplorEnz - The Enzyme Database: 3.1.1.50
            ERGO genome analysis and discovery system: 3.1.1.50
            BRENDA, the Enzyme Database: 3.1.1.50
            CAS: 66625-78-3
///
ENTRY       EC 3.1.1.51                 Enzyme
NAME        phorbol-diester hydrolase;
            diacylphorbate 12-hydrolase;
            diacylphorbate 12-hydrolase;
            phorbol-12,13-diester 12-ester hydrolase;
            PDEH
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     12,13-diacylphorbate 12-acylhydrolase
REACTION    phorbol 12,13-dibutanoate + H2O = phorbol 13-butanoate + butanoate
            [RN:R04119]
ALL_REAC    R04119
SUBSTRATE   phorbol 12,13-dibutanoate [CPD:C03634];
            H2O [CPD:C00001]
PRODUCT     phorbol 13-butanoate [CPD:C03019];
            butanoate [CPD:C00246]
COMMENT     Hydrolyses the 12-ester bond in a variety of 12,13-diacylphorbols
            (phorbol is a diterpenoid); this reaction inactivates the tumour
            promotor 12-O-tetradecanoylphorbol-13-acetate from croton oil.
REFERENCE   1  [PMID:6946062]
  AUTHORS   Shoyab M, Warren TC, Todaro GJ.
  TITLE     Isolation and characterization of an ester hydrolase active on
            phorbol diesters from murine liver.
  JOURNAL   J. Biol. Chem. 256 (1981) 12529-34.
  ORGANISM  mouse [GN:mmu]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.51
            ExPASy - ENZYME nomenclature database: 3.1.1.51
            ExplorEnz - The Enzyme Database: 3.1.1.51
            ERGO genome analysis and discovery system: 3.1.1.51
            BRENDA, the Enzyme Database: 3.1.1.51
            CAS: 81181-74-0
///
ENTRY       EC 3.1.1.52                 Enzyme
NAME        phosphatidylinositol deacylase;
            phosphatidylinositol phospholipase A2;
            phospholipase A2
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     1-phosphatidyl-D-myo-inositol 2-acylhydrolase
REACTION    1-phosphatidyl-D-myo-inositol + H2O = 1-acylglycerophosphoinositol +
            a carboxylate [RN:R03360]
ALL_REAC    R03360
SUBSTRATE   1-phosphatidyl-D-myo-inositol [CPD:C01194];
            H2O [CPD:C00001]
PRODUCT     1-acylglycerophosphoinositol [CPD:C03819];
            carboxylate [CPD:C00060]
REFERENCE   1  [PMID:7083039]
  AUTHORS   Gray NC, Strickland KP.
  TITLE     The purification and characterization of a phospholipase A2 activity
            from the 106,000 X g pellet (microsomal fraction) of bovine brain
            acting on phosphatidylinositol.
  JOURNAL   Can. J. Biochem. 60 (1982) 108-17.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:7087686]
  AUTHORS   Gray NC, Strickland KP.
  TITLE     On the specificity of a phospholipase A2 purified from the 106,000 X
            g pellet of bovine brain.
  JOURNAL   Lipids. 17 (1982) 91-6.
  ORGANISM  cow [GN:bta]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.52
            ExPASy - ENZYME nomenclature database: 3.1.1.52
            ExplorEnz - The Enzyme Database: 3.1.1.52
            ERGO genome analysis and discovery system: 3.1.1.52
            BRENDA, the Enzyme Database: 3.1.1.52
            CAS: 81604-94-6
///
ENTRY       EC 3.1.1.53                 Enzyme
NAME        sialate O-acetylesterase;
            N-acetylneuraminate acetyltransferase;
            sialate 9(4)-O-acetylesterase;
            sialidase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     N-acyl-O-acetylneuraminate O-acetylhydrolase
REACTION    N-acetyl-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate
            [RN:R01810]
ALL_REAC    R01810
SUBSTRATE   N-acetyl-O-acetylneuraminate [CPD:C03708];
            H2O [CPD:C00001]
PRODUCT     N-acetylneuraminate [CPD:C00270];
            acetate [CPD:C00033]
COMMENT     Acts on free and glycosidically bound N-acetyl- or
            N-glycoloyl-neuraminic acid; acts mainly on the 4-O- and 9-O-acetyl
            groups. Also acts on some other O-acetyl esters, both cyclic and
            acyclic compounds, which are not sialic acids.
REFERENCE   1  [PMID:1991039]
  AUTHORS   Garcia-Sastre A, Villar E, Manuguerra JC, Hannoun C, Cabezas JA.
  TITLE     Activity of influenza C virus O-acetylesterase with
            O-acetyl-containing compounds.
  JOURNAL   Biochem. J. 273(Pt 2) (1991) 435-41.
  ORGANISM  influenza C virus
REFERENCE   2
  AUTHORS   Shukla, A.K. and Schauer, R.
  TITLE     High performance liquid chromatography of enzymes of sialic acid
            metabolism.
  JOURNAL   Hoppe-Seyler's Z. Physiol. Chem. 363 (1982) 1039-1040.
ORTHOLOGY   KO: K05970  
GENES       MMU: 22619(Siae)
            XCC: XCC1753 XCC4103
            XCB: XC_2482 XC_4194
            XCV: XCV1803 XCV4334
            XAC: XAC1771 XAC4228
            XOO: XOO4420
            XOM: XOO_4163(XOO4163)
            ABA: Acid345_1697
            SUS: Acid_3201
            LLC: LACR_1436
            LLM: llmg_1161 llmg_1162
            BAD: BAD_0429
            RBA: RB10048
            FJO: Fjoh_4100 Fjoh_4232 Fjoh_4964
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.53
            ExPASy - ENZYME nomenclature database: 3.1.1.53
            ExplorEnz - The Enzyme Database: 3.1.1.53
            ERGO genome analysis and discovery system: 3.1.1.53
            BRENDA, the Enzyme Database: 3.1.1.53
            CAS: 89400-31-7
///
ENTRY       EC 3.1.1.54                 Enzyme
NAME        acetoxybutynylbithiophene deacetylase;
            acetoxybutynylbithiophene esterase;
            5-(4-acetoxy-1-butynyl)-2,2'-bithiophene:acetate esterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     5-(4-acetoxybut-1-ynyl)-2,2'-bithiophene O-acetylhydrolase
REACTION    5-(4-acetoxybut-1-ynyl)-2,2'-bithiophene + H2O =
            5-(4-hydroxybut-1-ynyl)-2,2'-bithiophene + acetate [RN:R04490]
ALL_REAC    R04490
SUBSTRATE   5-(4-acetoxybut-1-ynyl)-2,2'-bithiophene [CPD:C04485];
            H2O [CPD:C00001]
PRODUCT     5-(4-hydroxybut-1-ynyl)-2,2'-bithiophene [CPD:C04486];
            acetate [CPD:C00033]
COMMENT     The enzyme is highly specific.
REFERENCE   1  [PMID:16526078]
  AUTHORS   Granander J, Sott R, Hilmersson G.
  TITLE     Correlation between the 6Li,15N coupling constant and the
            coordination number at lithium.
  JOURNAL   Chemistry. 12 (2006) 4191-7.
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.54
            ExPASy - ENZYME nomenclature database: 3.1.1.54
            ExplorEnz - The Enzyme Database: 3.1.1.54
            ERGO genome analysis and discovery system: 3.1.1.54
            BRENDA, the Enzyme Database: 3.1.1.54
            CAS: 82346-63-2
///
ENTRY       EC 3.1.1.55                 Enzyme
NAME        acetylsalicylate deacetylase;
            aspirin esterase;
            aspirin esterase;
            acetylsalicylic acid esterase;
            aspirin hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     acetylsalicylate O-acetylhydrolase
REACTION    acetylsalicylate + H2O = salicylate + acetate [RN:R02942]
ALL_REAC    R02942
SUBSTRATE   acetylsalicylate [CPD:C01405];
            H2O [CPD:C00001]
PRODUCT     salicylate [CPD:C00805];
            acetate [CPD:C00033]
COMMENT     Not identical with EC 3.1.1.1 (carboxylesterase), EC 3.1.1.2
            (arylesterase), EC 3.1.1.7 (acetylcholinesterase) or EC 3.1.1.8
            (cholinesterase). The activity of the liver cytosol enzyme is
            highest with acetyl esters of aryl alcohols, and thioesters are also
            hydrolysed; the microsomal enzyme also hydrolyses some other
            negatively charged esters, with highest activity on esters of
            salicylate with long-chain alcohols.
REFERENCE   1  [PMID:6875867]
  AUTHORS   Ali B, Kaur S.
  TITLE     Mammalian tissue acetylsalicylic acid esterase(s): identification,
            distribution and discrimination from other esterases.
  JOURNAL   J. Pharmacol. Exp. Ther. 226 (1983) 589-94.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:2383281]
  AUTHORS   Kim DH, Yang YS, Jakoby WB.
  TITLE     Aspirin hydrolyzing esterases from rat liver cytosol.
  JOURNAL   Biochem. Pharmacol. 40 (1990) 481-7.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:6704404]
  AUTHORS   White KN, Hope DB.
  TITLE     Partial purification and characterization of a microsomal
            carboxylesterase specific for salicylate esters from guinea-pig
            liver.
  JOURNAL   Biochim. Biophys. Acta. 785 (1984) 138-47.
  ORGANISM  guinea pig
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.55
            ExPASy - ENZYME nomenclature database: 3.1.1.55
            ExplorEnz - The Enzyme Database: 3.1.1.55
            ERGO genome analysis and discovery system: 3.1.1.55
            BRENDA, the Enzyme Database: 3.1.1.55
            CAS: 87348-04-7
///
ENTRY       EC 3.1.1.56                 Enzyme
NAME        methylumbelliferyl-acetate deacetylase;
            esterase D
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     4-methylumbelliferyl-acetate acylhydrolase
REACTION    4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone + acetate
            [RN:R04141]
ALL_REAC    R04141
SUBSTRATE   4-methylumbelliferyl acetate [CPD:C03837];
            H2O [CPD:C00001]
PRODUCT     4-methylumbelliferone [CPD:C03081];
            acetate [CPD:C00033]
COMMENT     Acts on short-chain acyl esters of 4-methylumbelliferone, but not on
            naphthyl, indoxyl or thiocholine esters.
REFERENCE   1  [PMID:4768551]
  AUTHORS   Hopkinson DA, Mestriner MA, Cortner J, Harris H.
  TITLE     Esterase D: a new human polymorphism.
  JOURNAL   Ann. Hum. Genet. 37 (1973) 119-37.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.56
            ExPASy - ENZYME nomenclature database: 3.1.1.56
            ExplorEnz - The Enzyme Database: 3.1.1.56
            ERGO genome analysis and discovery system: 3.1.1.56
            BRENDA, the Enzyme Database: 3.1.1.56
            CAS: 83380-83-0
///
ENTRY       EC 3.1.1.57                 Enzyme
NAME        2-pyrone-4,6-dicarboxylate lactonase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     2-pyrone-4,6-dicarboxylate lactonohydrolase
REACTION    2-pyrone-4,6-dicarboxylate + H2O =
            4-carboxy-2-hydroxyhexa-2,4-dienedioate [RN:R04277]
ALL_REAC    R04277
SUBSTRATE   2-pyrone-4,6-dicarboxylate [CPD:C03671];
            H2O [CPD:C00001]
PRODUCT     4-carboxy-2-hydroxyhexa-2,4-dienedioate [CPD:C04451]
COMMENT     The product isomerizes to 4-oxalmesaconate.
REFERENCE   1  [PMID:7142106]
  AUTHORS   Kersten PJ, Dagley S, Whittaker JW, Arciero DM, Lipscomb JD.
  TITLE     2-pyrone-4,6-dicarboxylic acid, a catabolite of gallic acids in
            Pseudomonas species.
  JOURNAL   J. Bacteriol. 152 (1982) 1154-62.
  ORGANISM  Pseudomonas testosteroni
REFERENCE   2  [PMID:6841353]
  AUTHORS   Maruyama K.
  TITLE     Purification and properties of 2-pyrone-4,6-dicarboxylate hydrolase.
  JOURNAL   J. Biochem. (Tokyo). 93 (1983) 557-65.
  ORGANISM  Pseudomonas ochraceae
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
ORTHOLOGY   KO: K10221  2-pyrone-4,6-dicarboxylate lactonase
GENES       PAT: Patl_3887
            RFR: Rfer_0332
            POL: Bpro_4322
            PNA: Pnap_2029
            VEI: Veis_0169
            AZO: azo2539(ligI)
            RLE: pRL120277(ligI)
            BRA: BRADO2340(ligI)
            BBT: BBta_2700(ligI)
            RPA: RPA4700(ligI)
            RPB: RPB_0874
            RPD: RPD_0984
            RPE: RPE_0749
            MAG: amb0254
            ART: Arth_4374
STRUCTURES  PDB: 2QAH  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.57
            ExPASy - ENZYME nomenclature database: 3.1.1.57
            ExplorEnz - The Enzyme Database: 3.1.1.57
            ERGO genome analysis and discovery system: 3.1.1.57
            BRENDA, the Enzyme Database: 3.1.1.57
            CAS: 84177-55-9
///
ENTRY       EC 3.1.1.58                 Enzyme
NAME        N-acetylgalactosaminoglycan deacetylase;
            polysaccharide deacetylase;
            polysaccharide deacetylase;
            Vi-polysaccharide deacetylase;
            N-acetyl galactosaminoglycan deacetylase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     N-acetyl-D-galactosaminoglycan acetylhydrolase
REACTION    N-acetyl-D-galactosaminoglycan + H2O = D-galactosaminoglycan +
            acetate [RN:R04146]
ALL_REAC    R04146
SUBSTRATE   N-acetyl-D-galactosaminoglycan [CPD:C04018];
            H2O [CPD:C00001]
PRODUCT     D-galactosaminoglycan [CPD:C03106];
            acetate [CPD:C00033]
REFERENCE   1  [PMID:6217857]
  AUTHORS   Jorge JA, Kinney SG, Reissig JL.
  TITLE     Purification and characterization of Neurospora crassa N-acetyl
            galactosaminoglycan deacetylase.
  JOURNAL   Braz. J. Med. Biol. Res. 15 (1982) 29-34.
  ORGANISM  Neurospora crassa [GN:dncr]
GENES       AZO: azo3266
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.58
            ExPASy - ENZYME nomenclature database: 3.1.1.58
            ExplorEnz - The Enzyme Database: 3.1.1.58
            ERGO genome analysis and discovery system: 3.1.1.58
            BRENDA, the Enzyme Database: 3.1.1.58
            CAS: 52410-59-0
///
ENTRY       EC 3.1.1.59                 Enzyme
NAME        juvenile-hormone esterase;
            JH-esterase;
            juvenile hormone analog esterase;
            juvenile hormone carboxyesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     methyl-(2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-die
            noate acylhydrolase
REACTION    methyl
            (2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate +
            H2O =
            (2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate +
            methanol [RN:R04608]
ALL_REAC    R04608
SUBSTRATE   methyl
            (2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate
            [CPD:C04867];
            H2O [CPD:C00001]
PRODUCT     (2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate
            [CPD:C04834];
            methanol [CPD:C00132]
COMMENT     Demethylates the insect juvenile hormones, JH1 and JH3, but does not
            hydrolyse the analogous ethyl or isopropyl esters.
REFERENCE   1  [PMID:16526094]
  AUTHORS   Foucher AL, McIntosh A, Douce G, Wastling J, Tait A, Turner CM.
  TITLE     A proteomic analysis of arsenical drug resistance in Trypanosoma
            brucei.
  JOURNAL   Proteomics. 6 (2006) 2726-32.
REFERENCE   2
  AUTHORS   Mitsui, T., Riddiford, L.M. and Bellamy, G.
  TITLE     Metabolism of juvenile hormone by the epidermis of the tobacco
            hornworm (Manduca sexta).
  JOURNAL   Insect Biochem. 9 (1979) 637-643.
  ORGANISM  Manduca sexta
ORTHOLOGY   KO: K01063  juvenile-hormone esterase
GENES       DME: Dmel_CG8425(Jhe)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.59
            ExPASy - ENZYME nomenclature database: 3.1.1.59
            ExplorEnz - The Enzyme Database: 3.1.1.59
            ERGO genome analysis and discovery system: 3.1.1.59
            BRENDA, the Enzyme Database: 3.1.1.59
            CAS: 50812-15-2
///
ENTRY       EC 3.1.1.60                 Enzyme
NAME        bis(2-ethylhexyl)phthalate esterase;
            DEHP esterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     bis(2-ethylhexyl)phthalate acylhydrolase
REACTION    bis(2-ethylhexyl)phthalate + H2O = 2-ethylhexyl phthalate +
            2-ethylhexan-1-ol [RN:R04202]
ALL_REAC    R04202
SUBSTRATE   bis(2-ethylhexyl)phthalate [CPD:C03690];
            H2O [CPD:C00001]
PRODUCT     2-ethylhexyl phthalate [CPD:C03343];
            2-ethylhexan-1-ol [CPD:C02498]
COMMENT     Also acts on 4-nitrophenyl esters, with optimum chain-length C6 to
            C8.
REFERENCE   1  [PMID:6468391]
  AUTHORS   Krell HW, Sandermann H Jr.
  TITLE     Plant biochemistry of xenobiotics. Purification and properties of a
            wheat esterase hydrolyzing the plasticizer chemical,
            bis(2-ethylhexyl)phthalate.
  JOURNAL   Eur. J. Biochem. 143 (1984) 57-62.
  ORGANISM  Triticum aestivum [GN:etae]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.60
            ExPASy - ENZYME nomenclature database: 3.1.1.60
            ExplorEnz - The Enzyme Database: 3.1.1.60
            ERGO genome analysis and discovery system: 3.1.1.60
            BRENDA, the Enzyme Database: 3.1.1.60
            CAS: 92480-02-9
///
ENTRY       EC 3.1.1.61                 Enzyme
NAME        protein-glutamate methylesterase;
            chemotaxis-specific methylesterase;
            methyl-accepting chemotaxis protein methyl-esterase;
            CheB methylesterase;
            methylesterase CheB;
            protein methyl-esterase;
            protein carboxyl methylesterase;
            PME;
            protein methylesterase;
            protein-L-glutamate-5-O-methyl-ester acylhydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     protein-L-glutamate-O5-methyl-ester acylhydrolase
REACTION    protein L-glutamate O5-methyl ester + H2O = protein L-glutamate +
            methanol [RN:R02624]
ALL_REAC    R02624
SUBSTRATE   protein L-glutamate O5-methyl ester [CPD:C04310];
            H2O [CPD:C00001]
PRODUCT     protein L-glutamate [CPD:C00614];
            methanol [CPD:C00132]
COMMENT     Hydrolyses the products of EC 2.1.1.77
            (protein-L-isoaspartate(D-aspartate) O-methyltransferase), EC
            2.1.1.78 (isoorientin 3'-O-methyltransferase), EC 2.1.1.80
            (protein-glutamate O-methyltransferase) and EC 2.1.1.100
            (protein-S-isoprenylcysteine O-methyltransferase).
REFERENCE   1  [PMID:6469959]
  AUTHORS   Gagnon C, Harbour D, Camato R.
  TITLE     Purification and characterization of protein methylesterase from rat
            kidney.
  JOURNAL   J. Biol. Chem. 259 (1984) 10212-5.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6384215]
  AUTHORS   Kehry MR, Doak TG, Dahlquist FW.
  TITLE     Stimulus-induced changes in methylesterase activity during
            chemotaxis in Escherichia coli.
  JOURNAL   J. Biol. Chem. 259 (1984) 11828-35.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map02020  Two-component system - General
            PATH: map02030  Bacterial chemotaxis - General
            PATH: map02031  Bacterial chemotaxis - Organism-specific
ORTHOLOGY   KO: K03412  protein-glutamate methylesterase, two-component system,
                        chemotaxis family, response regulator CheB
            KO: K05971  
GENES       TET: TTHERM_00265180 TTHERM_00532330
            ECO: b1883(cheB)
            ECJ: JW1872(cheB)
            ECE: Z2937(cheB)
            ECS: ECs2593
            ECC: c2298(cheB)
            ECI: UTI89_C2087(cheB)
            ECP: ECP_1828
            ECV: APECO1_932(cheB)
            ECW: EcE24377A_2116(cheB)
            ECX: EcHS_A1979(cheB)
            STY: STY2126(cheB)
            STT: t0960(cheB)
            SPT: SPA0951(cheB)
            SEC: SC1924(cheB)
            STM: STM1917(cheB)
            YPE: YPO1679(cheB)
            YPK: y1841(cheB)
            YPM: YP_1809(cheB)
            YPA: YPA_1843
            YPN: YPN_1952
            YPP: YPDSF_1769
            YPS: YPTB2398(cheB)
            YPI: YpsIP31758_1645(cheB)
            SFL: SF1932(cheB)
            SFX: S2023(cheB)
            SFV: SFV_1929(cheB)
            SSN: SSON_1234(cheB)
            SBO: SBO_1117(cheB)
            ECA: ECA1693(cheB)
            PLU: plu1856(cheB)
            SGL: SG2065
            ENT: Ent638_2454
            SPE: Spro_2980
            XCC: XCC1183(cheB) XCC1866(cheB) XCC2021(cheB) XCC2705(cheB)
                 XCC2822(cheB) XCC3686(cheR)
            XCB: XC_1290(cheB) XC_1409 XC_2163 XC_2323 XC_3059 XC_3757
            XCV: XCV1330(cheB) XCV1930(cheB1) XCV3025(cheB2) XCV3849(cheR4)
            XAC: XAC1280(cheB) XAC1888(cheB) XAC2870(cheB) XAC3730(cheR)
            XOO: XOO1465(cheB) XOO2859(cheB)
            XOM: XOO_1366(XOO1366) XOO_2714(XOO2714)
            VCH: VC1401(cheB) VC2062(cheB)
            VCO: VC0395_A1013(cheB-1)
            VVU: VV1_1956 VV2_0378 VV2_1161
            VVY: VV2460(cheB) VVA0935 VVA1685
            VPA: VP2228(cheB)
            VFI: VF1830
            PPR: PBPRA0778 PBPRA0943(cheB)
            PAE: PA0173 PA1459 PA3703
            PAU: PA14_02180(cheB) PA14_16480(wspF) PA14_45580(cheB)
            PPU: PP_1493 PP_3759 PP_4337(cheB)
            PPF: Pput_1530 Pput_2004 Pput_4229
            PST: PSPTO_0908(cheB-1) PSPTO_1498 PSPTO_1983(cheB-2) PSPTO_2714
            PSB: Psyr_0781 Psyr_1308 Psyr_2447 Psyr_3433
            PSP: PSPPH_0800(cheB1) PSPPH_2603(cheB2) PSPPH_3359(cheB3)
                 PSPPH_3876(wspF)
            PFL: PFL_1134 PFL_1671 PFL_3249
            PFO: Pfl_1057 Pfl_1567 Pfl_2648
            PEN: PSEEN1250 PSEEN3203 PSEEN3792(cheB)
            PMY: Pmen_0171 Pmen_1564 Pmen_2801
            ACI: ACIAD0627(baeR)
            SON: SO_2126(cheB-1) SO_2327(cheB-2) SO_3206(cheB-3)
            SDN: Sden_1347 Sden_3301
            SFR: Sfri_1203
            SAZ: Sama_2276 Sama_3499
            SBL: Sbal_2117 Sbal_2905
            SBM: Shew185_2242 Shew185_2915
            SLO: Shew_0109 Shew_1387
            SPC: Sputcn32_2555
            SSE: Ssed_0182 Ssed_1646 Ssed_3045
            SPL: Spea_1382
            SHE: Shewmr4_1303 Shewmr4_2088
            SHM: Shewmr7_1370 Shewmr7_1886
            SHN: Shewana3_1363 Shewana3_2213
            SHW: Sputw3181_1448
            ILO: IL1113(cheB)
            CPS: CPS_1523(cheB)
            PHA: PSHAa0810(cheY) PSHAa0813(cheB) PSHAa0913 PSHAa1916(uvrY)
                 PSHAa2380
            PAT: Patl_3026
            SDE: Sde_2160 Sde_3102
            PIN: Ping_3721
            MAQ: Maqu_1971
            MCA: MCA0832 MCA1246
            TCX: Tcr_0758
            NOC: Noc_0125 Noc_1601
            AEH: Mlg_0989 Mlg_1118
            HHA: Hhal_0473 Hhal_2160
            HCH: HCH_00463 HCH_03703 HCH_03846 HCH_05166
            CSA: Csal_2020
            ABO: ABO_0103(cheB) ABO_1310(cheB)
            MMW: Mmwyl1_3304 Mmwyl1_3424
            AHA: AHA_1030(cheB-1) AHA_1386(cheB-2) AHA_2533(cheB-3)
            CVI: CV_1009(cheB2) CV_2506(cheB1) CV_3139 CV_3436(cheB3)
            RSO: RSp1403(cheB)
            REU: Reut_A0607 Reut_B3648 Reut_B4915 Reut_B5191 Reut_B5612
            RME: Rmet_3693 Rmet_3968
            BMA: BMA2854(cheB) BMAA0221.1
            BMV: BMASAVP1_A3429(cheB)
            BML: BMA10299_A1689(cheB)
            BMN: BMA10247_3122(cheB)
            BXE: Bxe_A0124 Bxe_B1218
            BVI: Bcep1808_0220 Bcep1808_4178
            BUR: Bcep18194_A3363 Bcep18194_A5728 Bcep18194_A6471
                 Bcep18194_B0012 Bcep18194_B2017 Bcep18194_B2303
                 Bcep18194_B2520 Bcep18194_B3050 Bcep18194_C7173
            BCN: Bcen_2846 Bcen_4310 Bcen_4571
            BCH: Bcen2424_0261 Bcen2424_3792 Bcen2424_4056
            BAM: Bamb_0174 Bamb_3450 Bamb_5518
            BPS: BPSL3301(cheB) BPSS1870
            BPM: BURPS1710b_0071(cheB) BURPS1710b_A0963(cheB)
            BPL: BURPS1106A_3931(cheB) BURPS1106A_A2537(cheB)
            BPD: BURPS668_3850(cheB) BURPS668_A0209 BURPS668_A0210
                 BURPS668_A2682(cheB)
            BTE: BTH_I3177(cheB) BTH_II0161(cheB) BTH_II0162(cheB) BTH_II0506
            BPE: BP1032(cheB)
            BPA: BPP1476(cheB)
            BBR: BB2550(cheB)
            RFR: Rfer_0571 Rfer_0906 Rfer_2355 Rfer_3013
            POL: Bpro_2467
            PNA: Pnap_3575
            AAV: Aave_3548 Aave_4374
            AJS: Ajs_0649 Ajs_3786
            VEI: Veis_2172
            MPT: Mpe_A2702(cheB)
            HAR: HEAR1305(cheB) HEAR2520(vsrD) HEAR2743
            MMS: mma_0013(cheB1) mma_2091(cheB2)
            NEU: NE1859(cheB)
            NET: Neut_1173
            NMU: Nmul_A0334
            EBA: ebA2146 ebA2148(cheB)
            AZO: azo0402(cheB1) azo1456(cheB2)
            DAR: Daro_0732 Daro_1148 Daro_2045
            TBD: Tbd_1615(cheY)
            MFA: Mfla_1930 Mfla_2589
            HPA: HPAG1_0162 HPAG1_0380 HPAG1_0404 HPAG1_1312
            HHE: HH0456(cheB) HH0825(cheY)
            HAC: Hac_1178(cheY)
            WSU: WS1213
            TDN: Tmden_0978 Tmden_1939
            CJE: Cj0924c(cheB')
            CJR: CJE1002(cheB)
            CJJ: CJJ81176_0931(cheB)
            CJU: C8J_0861(cheB')
            CJD: JJD26997_0890(cheB)
            CFF: CFF8240_0805
            CCV: CCV52592_1332
            CCO: CCC13826_0841(cheB)
            ABU: Abu_1188(cheB)
            NIS: NIS_0273(cheB)
            GSU: GSU0293(cheB-1) GSU1145(cheB-2) GSU2214(cheB-3)
            GME: Gmet_0780 Gmet_1075 Gmet_2304 Gmet_2418 Gmet_2640 Gmet_2711
                 Gmet_3269
            GUR: Gura_2165 Gura_2688 Gura_2982 Gura_3138 Gura_4172 Gura_4423
            PCA: Pcar_1200
            PPD: Ppro_0880 Ppro_1611
            DVU: DVU0449 DVU1596(cheB-1) DVU2078(cheB-2)
            DVL: Dvul_1150 Dvul_1538
            DDE: Dde_1571 Dde_2104
            LIP: LI1137(cheB)
            BBA: Bd0580(cheB) Bd3467(cheB)
            DPS: DP1791(cheB) DP2644
            ADE: Adeh_0600 Adeh_0614 Adeh_1192 Adeh_1373 Adeh_1383 Adeh_2730
                 Adeh_3183
            AFW: Anae109_0470 Anae109_0644 Anae109_0658 Anae109_2298
                 Anae109_2366 Anae109_3532
            MXA: MXAN_0714 MXAN_4139(frzG) MXAN_4752(cheB) MXAN_5145(cheB3)
                 MXAN_6028 MXAN_6952(cheB) MXAN_6959(cheB)
            SAT: SYN_00430 SYN_00964
            SFU: Sfum_1645 Sfum_1652
            MLO: mll9510
            MES: Meso_0601
            SME: SMa1561(cheB2) SMb20514 SMb20515 SMc03010(cheB)
            SMD: Smed_0238 Smed_5119 Smed_5775
            ATU: Atu0519(cheB)
            ATC: AGR_C_916
            RET: RHE_CH00642(cheBch1) RHE_CH03515(cheBch2) RHE_PF00075(cheBf)
                 RHE_PF00076(cheRf)
            RLE: RL0691(cheB) RL4028(cheB)
            OAN: Oant_4782
            BJA: blr2195(cheB) blr2349(cheB)
            BRA: BRADO0819(cheB) BRADO1476(cheB) BRADO1827(cheB)
                 BRADO4520(pleD)
            BBT: BBta_2148(cheB) BBta_4746(pleD) BBta_6556(cheB)
                 BBta_6730(cheB) BBta_7833(cheB)
            RPA: RPA0137(cheB1) RPA1630(cheB2) RPA3316
            RPB: RPB_3917
            RPC: RPC_4244 RPC_4611 RPC_4668
            RPD: RPD_3675
            RPE: RPE_1198 RPE_3635 RPE_4281 RPE_4669
            NWI: Nwi_0522 Nwi_0523
            NHA: Nham_3373
            CCR: CC_0436 CC_0597
            SIT: TM1040_3210
            RSP: RSP_0047(cheB2) RSP_1588(cheB1) RSP_2229
            RSH: Rsph17029_0240 Rsph17029_1682
            RSQ: Rsph17025_0268 Rsph17025_1635
            JAN: Jann_2844
            RDE: RD1_2244(cheB) RD1_3107
            MMR: Mmar10_0661
            ZMO: ZMO0081(cheB) ZMO0878(cheB) ZMO0880(cheA)
            SAL: Sala_1737
            SWI: Swit_0068 Swit_3186 Swit_5355
            ELI: ELI_11250
            GOX: GOX1555(cheB)
            GBE: GbCGDNIH1_1133
            ACR: Acry_2711
            RRU: Rru_A0376 Rru_A0522 Rru_A0523 Rru_A1385 Rru_A1398 Rru_A1406
                 Rru_A1500 Rru_A2323 Rru_A2929
            MAG: amb0323 amb1966 amb3002 amb3654 amb3880
            MGM: Mmc1_0626 Mmc1_1480 Mmc1_1835 Mmc1_3390 Mmc1_3581
            ABA: Acid345_1528 Acid345_1770
            SUS: Acid_5374
            BSU: BG10255(cheB)
            BHA: BH2435(cheB)
            BLI: BL01251(cheB)
            BLD: BLi01863(cheB)
            BCL: ABC2247(cheB)
            BAY: RBAM_016260(cheB)
            BPU: BPUM_1541(cheB)
            OIH: OB1578(cheB)
            GKA: GK1241(cheB)
            STH: STH1541(cheB)
            CAC: CAC2222(cheB)
            CTC: CTC01733
            CNO: NT01CX_1862
            CTH: Cthe_0489 Cthe_0807 Cthe_2281 Cthe_2821
            CBO: CBO2750(cheB)
            CBA: CLB_2691(cheB)
            CBH: CLC_2624(cheB)
            CBF: CLI_2800(cheB)
            CBE: Cbei_4180 Cbei_4309 Cbei_4826
            CKL: CKL_0573(cheB1) CKL_2131(cheB2)
            AMT: Amet_2699
            CHY: CHY_0968(cheB1) CHY_1031(cheB2)
            DSY: DSY2992
            DRM: Dred_2439
            SWO: Swol_0873 Swol_1329 Swol_1449
            CSC: Csac_0179 Csac_0813 Csac_0949
            TTE: TTE1035(cheB) TTE1418(cheB2)
            MTA: Moth_0743
            MPA: MAP3235c
            MAV: MAV_4066(cheB)
            RHA: RHA1_ro04741(phoP) RHA1_ro05622
            NCA: Noca_3599
            FAL: FRAAL1304 FRAAL1628 FRAAL4813
            ACE: Acel_0222 Acel_1789
            KRA: Krad_0321 Krad_1847
            SEN: SACE_0787 SACE_3669
            RBA: RB4511
            BBU: BB0415(cheB-1) BB0568(cheB-2)
            BGA: BG0418(cheB-1) BG0578(cheB-2)
            BAF: BAPKO_0598(cheB-2)
            TPA: TP0631
            TDE: TDE0648(cheB)
            LIL: LA1252(cheB1) LA1744(cheB2) LA2429(cheB3)
            LIC: LIC11520(cheB) LIC12061 LIC12455
            LBJ: LBJ_0928(cheB) LBJ_1249 LBJ_1816
            LBL: LBL_1298 LBL_1467 LBL_2105(cheB)
            GVI: gll1854 glr3562
            ANA: all1716 all1847
            AVA: Ava_0124 Ava_0239 Ava_0314 Ava_0508(cheY) Ava_1005 Ava_1030
                 Ava_1777 Ava_1878 Ava_2028 Ava_2149 Ava_2150 Ava_2562 Ava_3166
                 Ava_3170 Ava_3369 Ava_3616 Ava_3851 Ava_3976 Ava_4136 Ava_4293
                 Ava_4631 Ava_4701 Ava_4702 Ava_4782 Ava_B0029 Ava_B0209
                 Ava_C0116
            PMB: A9601_01451(rpaA) A9601_01511 A9601_18291
            PMC: P9515_01561(rpaA) P9515_01621 P9515_18081
            PMF: P9303_01831 P9303_26471(rpaA) P9303_26531(rpaB)
            PMG: P9301_01471(rpaA) P9301_01531 P9301_12431(phoB) P9301_18111
            PME: NATL1_02061 NATL1_11471(phoB) NATL1_20711
            TER: Tery_4227
            SRU: SRU_0336(cheB) SRU_2601
            CHU: CHU_2078(cheB)
            FJO: Fjoh_3351
            CCH: Cag_0563
            RRS: RoseRS_0034 RoseRS_0994
            RCA: Rcas_3196 Rcas_4208
            TMA: TM0408
            TPT: Tpet_0512
            TME: Tmel_1770
            FNO: Fnod_0046
            MMP: MMP0926(cheB)
            MMQ: MmarC5_0733
            MMZ: MmarC7_0173
            MVN: Mevan_0219
            MAC: MA0015(cheB2) MA3067(cheB1) MA3542
            MBA: Mbar_A0985
            MMA: MM_0329 MM_1326
            MBU: Mbur_0360
            MHU: Mhun_0109 Mhun_0887 Mhun_0952 Mhun_0988
            MEM: Memar_0944 Memar_2125
            MBN: Mboo_1337
            AFU: AF1041(cheB)
            HAL: VNG0973G(cheB)
            HMA: rrnAC2204(cheB)
            NPH: NP2174A(cheB)
            PHO: PH0483(cheB)
            PAB: PAB1331(cheB)
            TKO: TK0633
            RCI: LRC570(cheB)
STRUCTURES  PDB: 1A2O  1CHD  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.61
            ExPASy - ENZYME nomenclature database: 3.1.1.61
            ExplorEnz - The Enzyme Database: 3.1.1.61
            ERGO genome analysis and discovery system: 3.1.1.61
            BRENDA, the Enzyme Database: 3.1.1.61
            CAS: 93792-01-9
///
ENTRY       EC 3.1.1.62       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
COMMENT     Deleted entry: Now listed as EC 3.5.1.47, N-acetyldiaminopimelate
            deacetylase (EC 3.1.1.62 created 1989, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.62
            ExPASy - ENZYME nomenclature database: 3.1.1.62
            ExplorEnz - The Enzyme Database: 3.1.1.62
            ERGO genome analysis and discovery system: 3.1.1.62
            BRENDA, the Enzyme Database: 3.1.1.62
///
ENTRY       EC 3.1.1.63                 Enzyme
NAME        11-cis-retinyl-palmitate hydrolase;
            11-cis-retinol palmitate esterase;
            RPH
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     11-cis-retinyl-palmitate acylhydrolase
REACTION    11-cis-retinyl palmitate + H2O = 11-cis-retinol + palmitate
            [RN:R03049]
ALL_REAC    R03049
SUBSTRATE   11-cis-retinyl palmitate [CPD:C03455];
            H2O [CPD:C00001]
PRODUCT     11-cis-retinol [CPD:C00899];
            palmitate [CPD:C00249]
EFFECTOR    Bile salt [CPD:C01558]
COMMENT     Activated by bile salts.
REFERENCE   1  [PMID:3793734]
  AUTHORS   Blaner WS, Das SR, Gouras P, Flood MT.
  TITLE     Hydrolysis of 11-cis- and all-trans-retinyl palmitate by homogenates
            of human retinal epithelial cells.
  JOURNAL   J. Biol. Chem. 262 (1987) 53-8.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:6743673]
  AUTHORS   Blaner WS, Prystowsky JH, Smith JE, Goodman DS.
  TITLE     Rat liver retinyl palmitate hydrolase activity. Relationship to
            cholesteryl oleate and triolein hydrolase activities.
  JOURNAL   Biochim. Biophys. Acta. 794 (1984) 419-27.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00830  Retinol metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.63
            ExPASy - ENZYME nomenclature database: 3.1.1.63
            ExplorEnz - The Enzyme Database: 3.1.1.63
            ERGO genome analysis and discovery system: 3.1.1.63
            BRENDA, the Enzyme Database: 3.1.1.63
///
ENTRY       EC 3.1.1.64                 Enzyme
NAME        all-trans-retinyl-palmitate hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     all-trans-retinyl-palmitate acylhydrolase
REACTION    all-trans-retinyl palmitate + H2O = all-trans-retinol + palmitate
            [RN:R02368]
ALL_REAC    R02368
SUBSTRATE   all-trans-retinyl palmitate [CPD:C02588];
            H2O [CPD:C00001]
PRODUCT     all-trans-retinol [CPD:C00473];
            palmitate [CPD:C00249]
EFFECTOR    Detergents [CPD:C01689]
COMMENT     Requires detergents for activity.
REFERENCE   1  [PMID:3793734]
  AUTHORS   Blaner WS, Das SR, Gouras P, Flood MT.
  TITLE     Hydrolysis of 11-cis- and all-trans-retinyl palmitate by homogenates
            of human retinal epithelial cells.
  JOURNAL   J. Biol. Chem. 262 (1987) 53-8.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00830  Retinol metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.64
            ExPASy - ENZYME nomenclature database: 3.1.1.64
            ExplorEnz - The Enzyme Database: 3.1.1.64
            ERGO genome analysis and discovery system: 3.1.1.64
            BRENDA, the Enzyme Database: 3.1.1.64
///
ENTRY       EC 3.1.1.65                 Enzyme
NAME        L-rhamnono-1,4-lactonase;
            L-rhamno-gamma-lactonase;
            L-rhamnono-gamma-lactonase;
            L-rhamnonate dehydratase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     L-rhamnono-1,4-lactone lactonohydrolase
REACTION    L-rhamnono-1,4-lactone + H2O = L-rhamnonate [RN:R03772]
ALL_REAC    R03772
SUBSTRATE   L-rhamnono-1,4-lactone [CPD:C02991];
            H2O [CPD:C00001]
PRODUCT     L-rhamnonate [CPD:C01934]
REFERENCE   1
  AUTHORS   Rigo, L.U., Marechal, L.R., Vieira, M.M. and Veiga, L.A.
  TITLE     Oxidative pathway for L-rhamnose degradation in Pallularia
            pullulans.
  JOURNAL   Can. J. Microbiol. 31 (1985) 817-822.
  ORGANISM  Pullularia pullulans
PATHWAY     PATH: map00051  Fructose and mannose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.65
            ExPASy - ENZYME nomenclature database: 3.1.1.65
            ExplorEnz - The Enzyme Database: 3.1.1.65
            ERGO genome analysis and discovery system: 3.1.1.65
            BRENDA, the Enzyme Database: 3.1.1.65
///
ENTRY       EC 3.1.1.66                 Enzyme
NAME        5-(3,4-diacetoxybut-1-ynyl)-2,2'-bithiophene deacetylase;
            diacetoxybutynylbithiophene acetate esterase;
            3,4-diacetoxybutinylbithiophene:4-acetate esterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     5-(3,4-diacetoxybut-1-ynyl)-2,2'-bithiophene acetylhydrolase
REACTION    5-(3,4-diacetoxybut-1-ynyl)-2,2'-bithiophene + H2O =
            5-(3-hydroxy-4-acetoxybut-1-ynyl)-2,2'-bithiophene + acetate
            [RN:R04525]
ALL_REAC    R04525
SUBSTRATE   5-(3,4-diacetoxybut-1-ynyl)-2,2'-bithiophene [CPD:C04606];
            H2O [CPD:C00001]
PRODUCT     5-(3-hydroxy-4-acetoxybut-1-ynyl)-2,2'-bithiophene [CPD:C04711];
            acetate [CPD:C00033]
COMMENT     A highly specific enzyme from Tagetes patula.
REFERENCE   1
  AUTHORS   Pensl, R. and Suetfeld, R.
  TITLE     Occurrence of 3,4-diacetoybutinylbithiophene in Tagetes patula and
            its enzymatic conversion.
  JOURNAL   Z. Naturforsch. C: Biosci. 40 (1985) 3-7.
  ORGANISM  Tagetes patula
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.66
            ExPASy - ENZYME nomenclature database: 3.1.1.66
            ExplorEnz - The Enzyme Database: 3.1.1.66
            ERGO genome analysis and discovery system: 3.1.1.66
            BRENDA, the Enzyme Database: 3.1.1.66
///
ENTRY       EC 3.1.1.67                 Enzyme
NAME        fatty-acyl-ethyl-ester synthase;
            FAEES
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     long-chain-fatty-acyl-ethyl-ester acylhydrolase
REACTION    a long-chain-fatty-acyl ethyl ester + H2O = a long-chain-fatty acid
            + ethanol [RN:R02682]
ALL_REAC    R02682
SUBSTRATE   long-chain-fatty-acyl ethyl ester [CPD:C04202];
            H2O [CPD:C00001]
PRODUCT     long-chain-fatty acid;
            ethanol [CPD:C00469]
COMMENT     In the reverse reaction, forms ethyl esters from fatty acids and
            ethanol in the absence of coenzyme A or ATP. Best substrates are
            unsaturated octadecanoic acids; palmitate, stearate and arachidonate
            also act, but more slowly.
REFERENCE   1  [PMID:6487591]
  AUTHORS   Mogelson S, Lange LG.
  TITLE     Nonoxidative ethanol metabolism in rabbit myocardium: purification
            to homogeneity of fatty acyl ethyl ester synthase.
  JOURNAL   Biochemistry. 23 (1984) 4075-81.
  ORGANISM  rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.67
            ExPASy - ENZYME nomenclature database: 3.1.1.67
            ExplorEnz - The Enzyme Database: 3.1.1.67
            ERGO genome analysis and discovery system: 3.1.1.67
            BRENDA, the Enzyme Database: 3.1.1.67
///
ENTRY       EC 3.1.1.68                 Enzyme
NAME        xylono-1,4-lactonase;
            xylono-g-lactonase;
            xylonolactonase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     D-xylono-1,4-lactone lactonohydrolase
REACTION    D-xylono-1,4-lactone + H2O = D-xylonate [RN:R02428]
ALL_REAC    R02428;
            (other) R02427
SUBSTRATE   D-xylono-1,4-lactone [CPD:C02753];
            H2O [CPD:C00001]
PRODUCT     D-xylonate [CPD:C00502]
REFERENCE   1
  AUTHORS   Buchert, J. and Viikari, L.
  TITLE     The role of xylonolactone in xylonic acid production by Pseudomonas
            fragi.
  JOURNAL   Appl. Microbiol. Biotechnol. 27 (1988) 333-336.
  ORGANISM  Pseudomonas fragi
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.68
            ExPASy - ENZYME nomenclature database: 3.1.1.68
            ExplorEnz - The Enzyme Database: 3.1.1.68
            ERGO genome analysis and discovery system: 3.1.1.68
            BRENDA, the Enzyme Database: 3.1.1.68
///
ENTRY       EC 3.1.1.69       Obsolete  Enzyme
NAME        Transferred to 3.5.1.89
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
COMMENT     Transferred entry: now EC 3.5.1.89,
            N-acetylglucosaminylphosphatidylinositol deacetylase. Previously
            classified erroneously as an enzyme that hydrolysed an ester and not
            an amide (EC 3.1.1.69 created 1992, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.69
            ExPASy - ENZYME nomenclature database: 3.1.1.69
            ExplorEnz - The Enzyme Database: 3.1.1.69
            ERGO genome analysis and discovery system: 3.1.1.69
            BRENDA, the Enzyme Database: 3.1.1.69
///
ENTRY       EC 3.1.1.70                 Enzyme
NAME        cetraxate benzylesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     cetraxate-benzyl-ester benzylhydrolase
REACTION    cetraxate benzyl ester + H2O = cetraxate + benzyl alcohol
            [RN:R03612]
ALL_REAC    R03612
SUBSTRATE   cetraxate benzyl ester [CPD:C03256];
            H2O [CPD:C00001]
PRODUCT     cetraxate [CPD:C01564];
            benzyl alcohol [CPD:C00556]
COMMENT     Acts on a number of benzyl esters of substituted phenyl propanoates,
            and on the benzyl esters of phenylalanine and tyrosine.
REFERENCE   1  [PMID:2632040]
  AUTHORS   Kuroda H, Miyadera A, Imura A, Suzuki A.
  TITLE     Partial purification, and some properties and reactivities of
            cetraxate benzyl ester hydrochloride-hydrolyzing enzyme.
  JOURNAL   Chem. Pharm. Bull. (Tokyo). 37 (1989) 2929-32.
  ORGANISM  Aspergillus niger
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.70
            ExPASy - ENZYME nomenclature database: 3.1.1.70
            ExplorEnz - The Enzyme Database: 3.1.1.70
            ERGO genome analysis and discovery system: 3.1.1.70
            BRENDA, the Enzyme Database: 3.1.1.70
///
ENTRY       EC 3.1.1.71                 Enzyme
NAME        acetylalkylglycerol acetylhydrolase;
            alkylacetylglycerol acetylhydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     2-acetyl-1-alkyl-sn-glycerol acetylhydrolase
REACTION    2-acetyl-1-alkyl-sn-glycerol + H2O = 1-alkyl-sn-glycerol + acetate
            [RN:R04043]
ALL_REAC    R04043
SUBSTRATE   2-acetyl-1-alkyl-sn-glycerol [CPD:C03820];
            H2O [CPD:C00001]
PRODUCT     1-alkyl-sn-glycerol [CPD:C02773];
            acetate [CPD:C00033]
COMMENT     Hydrolysis of the acetyl group from the 1-alkyl-2-acetyl and
            1-alkyl-3-acetyl substrates occurs at apparently identical rates.
            The enzyme from Erlich ascites cells is membrane-bound. It differs
            from lipoprotein lipase (EC 3.1.1.34) since
            1,2-diacetyl-sn-glycerols are not substrates. It also differs from
            EC 3.1.1.47, 1-acetyl-2-alkyl-glycerophosphocholine esterase.
REFERENCE   1  [PMID:2302414]
  AUTHORS   Blank ML, Smith ZL, Cress EA, Snyder F.
  TITLE     Characterization of the enzymatic hydrolysis of acetate from
            alkylacetylglycerols in the de novo pathway of PAF biosynthesis.
  JOURNAL   Biochim. Biophys. Acta. 1042 (1990) 153-8.
  ORGANISM  mouse [GN:mmu]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.71
            ExPASy - ENZYME nomenclature database: 3.1.1.71
            ExplorEnz - The Enzyme Database: 3.1.1.71
            ERGO genome analysis and discovery system: 3.1.1.71
            BRENDA, the Enzyme Database: 3.1.1.71
///
ENTRY       EC 3.1.1.72                 Enzyme
NAME        acetylxylan esterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     acetylxylan esterase
REACTION    Deacetylation of xylans and xylo-oligosaccharides
COMMENT     Catalyses the hydrolysis of acetyl groups from polymeric xylan,
            acetylated xylose, acetylated glucose, alpha-napthyl acetate,
            p-nitrophenyl acetate but not from triacetylglycerol. Does not act
            on acetylated mannan or pectin.
REFERENCE   1
  AUTHORS   Sundberg, M., Poutanen, K.
  TITLE     Purification and properties of two acetylxylan esterases of
            Trichoderma reesei.
  JOURNAL   Biotechnol. Appl. Biochem. 13 (1991) 1-11.
  ORGANISM  Trichoderma reesei
REFERENCE   2
  AUTHORS   Poutanen, K., Sundberg, M., Korte, H., Puls, J.
  TITLE     Deacetylation of xylans by acetyl esterases of Trichoderma reesei.
  JOURNAL   Appl. Microbiol. Biotechnol. 33 (1990) 506-510.
  ORGANISM  Trichoderma reesei
REFERENCE   3  [PMID:8647098]
  AUTHORS   Margolles-Clark E, Tenkanen M, Soderlund H, Penttila M.
  TITLE     Acetyl xylan esterase from Trichoderma reesei contains an
            active-site serine residue and a cellulose-binding domain.
  JOURNAL   Eur. J. Biochem. 237 (1996) 553-60.
  ORGANISM  Trichoderma reesei
ORTHOLOGY   KO: K05972  
GENES       CPF: CPF_1848(axe1)
            LIL: LA1864(axeA)
            CHU: CHU_1239
STRUCTURES  PDB: 1QOZ  2C71  2C79  2CC0  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.72
            ExPASy - ENZYME nomenclature database: 3.1.1.72
            ExplorEnz - The Enzyme Database: 3.1.1.72
            ERGO genome analysis and discovery system: 3.1.1.72
            BRENDA, the Enzyme Database: 3.1.1.72
///
ENTRY       EC 3.1.1.73                 Enzyme
NAME        feruloyl esterase;
            ferulic acid esterase, hydroxycinnamoyl esterase, hemicellulase
            accessory enzymes;
            FAE-III, cinnamoyl ester hydrolase, FAEA, cinnAE, FAE-I, FAE-II
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
REACTION    feruloyl-polysaccharide + H2O = ferulate + polysaccharide
            [RN:R07292]
ALL_REAC    R07292
SUBSTRATE   feruloyl-polysaccharide [CPD:C06741];
            H2O [CPD:C00001]
PRODUCT     ferulate [CPD:C01494];
            polysaccharide [CPD:C00420]
COMMENT     Catalyses the hydrolysis of the 4-hydroxy-3-methoxycinnamoyl
            (feruloyl) group from an esterified sugar, which is usually
            arabinose in "natural" substrates. p-Nitrophenol acetate and methyl
            ferulate are poorer substrates. All microbial ferulate esterases are
            secreted into the culture medium. They are sometimes called
            hemicellulase accessory enzymes, since they help xylanases and
            pectinases to break down plant cell wall hemicellulose.
REFERENCE   1  [PMID:1663152]
  AUTHORS   Faulds CB, Williamson G.
  TITLE     The purification and characterization of 4-hydroxy-3-methoxycinnamic
            (ferulic) acid esterase from Streptomyces olivochromogenes.
  JOURNAL   J. Gen. Microbiol. 137 (1991) 2339-45.
  ORGANISM  Streptomyces olivochromogenes
REFERENCE   2
  AUTHORS   Faulds, C.B. and Williamson, G.
  TITLE     Purification and characterisation of a ferulic acid esterase
            (FAE-III) from Aspergillus niger. Specificity for the phenolic
            moiety and binding to microcrystalline cellulose.
  JOURNAL   Microbiology 140 (1994) 779-787.
  ORGANISM  Aspergillus niger
REFERENCE   3  [PMID:8679110]
  AUTHORS   Kroon PA, Faulds CB, Williamson G.
  TITLE     Purification and characterization of a novel esterase induced by
            growth of Aspergillus niger on sugar-beet pulp.
  JOURNAL   Biotechnol. Appl. Biochem. 23 ( Pt 3) (1996) 255-62.
  ORGANISM  Aspergillus niger
REFERENCE   4  [PMID:9406381]
  AUTHORS   de Vries RP, Michelsen B, Poulsen CH, Kroon PA, van den Heuvel RH,
            Faulds CB, Williamson G, van den Hombergh JP, Visser J.
  TITLE     The faeA genes from Aspergillus niger and Aspergillus tubingensis
            encode ferulic acid esterases involved in degradation of complex
            cell wall polysaccharides.
  JOURNAL   Appl. Environ. Microbiol. 63 (1997) 4638-44.
  ORGANISM  Aspergillus niger, Aspergillus tubingensis
REFERENCE   5
  AUTHORS   Castanares, A., Mccrae, S.I. and Wood, T.M.
  TITLE     Purification and properties of a feruloyl/p-coumaroyl esterase from
            the fungus Penicillium pinophilum.
  JOURNAL   Enzyme Microbiol. Technol. 14 (1992) 875-884.
  ORGANISM  Penicillium pinophilum
ORTHOLOGY   KO: K09252  feruloyl esterase
GENES       AFM: AFUA_6G00450 AFUA_6G09040 AFUA_7G02380
            TET: TTHERM_00002660 TTHERM_00194580 TTHERM_00194590
                 TTHERM_00320120 TTHERM_00320130 TTHERM_00320160
                 TTHERM_00925390
            PSB: Psyr_2863
            SFR: Sfri_3696
            SBM: Shew185_1156
            REU: Reut_B4873
            BVI: Bcep1808_3848
            BUR: Bcep18194_B0055 Bcep18194_B2234 Bcep18194_C7221
                 Bcep18194_C7567
            BCN: Bcen_1301 Bcen_5228
            BCH: Bcen2424_5631 Bcen2424_6529
            BAM: Bamb_4911
            BPM: BURPS1710b_A2366(hcaG)
            BRA: BRADO2353 BRADO2873 BRADO4865
            BBT: BBta_2711 BBta_3196 BBta_5301
            RPE: RPE_0236
            RRU: Rru_A1969
            SUS: Acid_4215
            TFU: Tfu_0082
            FAL: FRAAL2454
            SEN: SACE_2827 SACE_3366 SACE_3632 SACE_3720 SACE_4675 SACE_4861
                 SACE_5296 SACE_5648
STRUCTURES  PDB: 1USW  1UWC  1UZA  2BJH  2HL6  2IX9  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.73
            ExPASy - ENZYME nomenclature database: 3.1.1.73
            ExplorEnz - The Enzyme Database: 3.1.1.73
            ERGO genome analysis and discovery system: 3.1.1.73
            BRENDA, the Enzyme Database: 3.1.1.73
            CAS: 134712-49-5
///
ENTRY       EC 3.1.1.74                 Enzyme
NAME        cutinase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     cutin hydrolase
REACTION    cutin + H2O = cutin monomers [RN:R05793]
ALL_REAC    R05793
SUBSTRATE   cutin [CPD:C07299];
            H2O [CPD:C00001]
PRODUCT     cutin monomer [CPD:C07300]
COMMENT     Cutin, a polymeric structural component of plant cuticles, is a
            polymer of hydroxy fatty acids that are usually C16 or C18 and
            contain up to three hydroxy groups. The enzyme from several fungal
            sources also hydrolyses the p-nitrophenyl esters of hexadecanoic
            acid. It is however inactive towards several esters that are
            substrates for non-specific esterases.
REFERENCE   1  [PMID:9281862]
  AUTHORS   Garcia-Lepe R, Nuero OM, Reyes F, Santamaria F.
  TITLE     Lipases in autolysed cultures of filamentous fungi.
  JOURNAL   Lett. Appl. Microbiol. 25 (1997) 127-30.
  ORGANISM  Aspergillus nidulans [GN:ani], Fusarium decemcellulare, Fusarium
            moniliforme, Fusarium oxysporum, Fusarium semitectum
REFERENCE   2  [PMID:1156575]
  AUTHORS   Purdy RE, Kolattukudy PE.
  TITLE     Hydrolysis of plant cuticle by plant pathogens. Purification, amino
            acid composition, and molecular weight of two isozymes of cutinase
            and a nonspecific esterase from Fusarium solani f. pisi.
  JOURNAL   Biochemistry. 14 (1975) 2824-31.
  ORGANISM  Fusarium solani
REFERENCE   3  [PMID:239740]
  AUTHORS   Purdy RE, Kolattukudy PE.
  TITLE     Hydrolysis of plant cuticle by plant pathogens. Properties of
            cutinase I, cutinase II, and a nonspecific esterase isolated from
            Fusarium solani pisi.
  JOURNAL   Biochemistry. 14 (1975) 2832-40.
  ORGANISM  Fusarium solani
ORTHOLOGY   KO: K08095  cutinase
GENES       ANI: AN7541.2
            AFM: AFUA_2G09380 AFUA_2G14420 AFUA_4G03210 AFUA_4G14120
            AOR: AO090011000665
            MTU: Rv1984c(cfp21) Rv3451(cut3)
            MTC: MT2037 MT3557
            MBO: Mb2006c(cfp21) Mb3481(cut3)
            MPA: MAP1680c MAP4237c
            MAV: MAV_2741 MAV_2961 MAV_4283 MAV_4396
            MSM: MSMEG_1526 MSMEG_1528 MSMEG_2474 MSMEG_4465
            MVA: Mvan_1441 Mvan_3105 Mvan_3344
            MGI: Mflv_3373 Mflv_4432 Mflv_4439
            MMC: Mmcs_1116 Mmcs_1117
            MKM: Mkms_1133
            MJL: Mjls_1145
            RHA: RHA1_ro00629
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.74
            ExPASy - ENZYME nomenclature database: 3.1.1.74
            ExplorEnz - The Enzyme Database: 3.1.1.74
            ERGO genome analysis and discovery system: 3.1.1.74
            BRENDA, the Enzyme Database: 3.1.1.74
///
ENTRY       EC 3.1.1.75                 Enzyme
NAME        poly(3-hydroxybutyrate) depolymerase;
            PHB depolymerase;
            poly(3HB) depolymerase;
            poly[(R)-hydroxyalkanoic acid] depolymerase;
            poly(HA) depolymerase;
            poly(HASCL) depolymerase;
            poly[(R)-3-hydroxybutyrate] hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     poly[(R)-3-hydroxybutanoate] hydrolase
REACTION    poly[(R)-3-hydroxybutanoate]n + H2O =
            poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x; x =
            1-5 [RN:R05797]
ALL_REAC    R05797
SUBSTRATE   poly[(R)-3-hydroxybutanoate]n [CPD:C11551];
            H2O [CPD:C00001]
PRODUCT     poly[(R)-3-hydroxybutanoate]n-x [CPD:C11551];
            poly[(R)-3-hydroxybutanoate]x; x
COMMENT     Reaction also occurs with esters of other short-chain-length (C1-C5)
            hydroxyalkanoic acids (HA). There are two types of polymers: native
            (intracellular) granules are amorphous and have an intact surface
            layer; denatured (extracellular) granules either have no surface
            layer or a damaged surface layer and are partially crystalline.
REFERENCE   1  [PMID:11217416]
  AUTHORS   Jendrossek D.
  TITLE     Microbial degradation of polyesters.
  JOURNAL   Adv. Biochem. Eng. Biotechnol. 71 (2001) 293-325.
  ORGANISM  Alcaligenes faecalis, Aureobacterium saperdae, Comamonas
            acidovorans, Comamonas testosteroni, Comamonas sp., Pseudomonas
            lemoignei, Pseudomonas stutzeri, Ralstonia pickettii, Streptomyces
            exfoliatus, Paecilomyces lilacinus, Penicillium funiculosum,
            Acidovorax sp.
REFERENCE   2  [PMID:10506180]
  AUTHORS   Garcia B, Olivera ER, Minambres B, Fernandez-Valverde M, Canedo LM,
            Prieto MA, Garcia JL, Martinez M, Luengo JM.
  TITLE     Novel biodegradable aromatic plastics from a bacterial source.
            Genetic and biochemical studies on a route of the phenylacetyl-coa
            catabolon.
  JOURNAL   J. Biol. Chem. 274 (1999) 29228-41.
  ORGANISM  Pseudomonas putida [GN:ppu]
ORTHOLOGY   KO: K05973  
GENES       CVI: CV_0172(phaZ1) CV_0729(phaZ2)
            REH: H16_A1150(phaZ1) H16_A2862(phaZ2) H16_B0339(phaZ3)
                 H16_B1014(phaZ5) H16_B2073(phaZ6) H16_B2401(phaZ7)
            BMA: BMA0824
            BMV: BMASAVP1_A1342
            BML: BMA10299_A0529
            BMN: BMA10247_0624
            BPS: BPSL2073(phaZ)
            BPM: BURPS1710b_1740(phaZ)
            BPL: BURPS1106A_1570 BURPS1106A_2146
            BPD: BURPS668_1547
            BTE: BTH_I2713
            AZO: azo0050(phaZ)
            RLE: pRL110460
STRUCTURES  PDB: 2D80  2D81  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.75
            ExPASy - ENZYME nomenclature database: 3.1.1.75
            ExplorEnz - The Enzyme Database: 3.1.1.75
            ERGO genome analysis and discovery system: 3.1.1.75
            BRENDA, the Enzyme Database: 3.1.1.75
///
ENTRY       EC 3.1.1.76                 Enzyme
NAME        poly(3-hydroxyoctanoate) depolymerase;
            PHO depolymerase, poly(3HO) depolymerase;
            poly[(R)-hydroxyalkanoic acid] depolymerase;
            poly(HA) depolymerase;
            poly(HAMCL) depolymerase;
            poly[(R)-3-hydroxyoctanoate] hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     poly{oxycarbonyl[(R)-2-pentylethylene]} hydrolase
REACTION    Hydrolyses the polyester poly{oxycarbonyl[(R)-2-pentylethylene]} to
            oligomers [RN:R05796]
ALL_REAC    R05796
COMMENT     The main product after prolonged incubation is the dimer [3].
            Besides hydrolysing polymers of 3-hydroxyoctanoic acid, the enzyme
            also hydrolyses other polymers derived from medium-chain-length
            (C6-C12) hydroxyalkanoic acids and copolymers of mixtures of these.
            It also hydrolyses p-nitrophenyl esters of fatty acids. Polymers of
            short-chain-length hydroxyalkanoic acids such as
            poly[(R)-3-hydroxybutanoic acid] and poly[(R)-3-hydroxypentanoic
            acid] are not hydrolysed.
REFERENCE   1  [PMID:11217416]
  AUTHORS   Jendrossek D.
  TITLE     Microbial degradation of polyesters.
  JOURNAL   Adv. Biochem. Eng. Biotechnol. 71 (2001) 293-325.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   2  [PMID:10506180]
  AUTHORS   Garcia B, Olivera ER, Minambres B, Fernandez-Valverde M, Canedo LM,
            Prieto MA, Garcia JL, Martinez M, Luengo JM.
  TITLE     Novel biodegradable aromatic plastics from a bacterial source.
            Genetic and biochemical studies on a route of the phenylacetyl-coa
            catabolon.
  JOURNAL   J. Biol. Chem. 274 (1999) 29228-41.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   3  [PMID:8476295]
  AUTHORS   Schirmer A, Jendrossek D, Schlegel HG.
  TITLE     Degradation of poly(3-hydroxyoctanoic acid) [P(3HO)] by bacteria:
            purification and properties of a P(3HO) depolymerase from
            Pseudomonas fluorescens GK13.
  JOURNAL   Appl. Environ. Microbiol. 59 (1993) 1220-7.
  ORGANISM  Pseudomonas fluorescens
ORTHOLOGY   KO: K05974  
GENES       BBA: Bd3709
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.76
            ExPASy - ENZYME nomenclature database: 3.1.1.76
            ExplorEnz - The Enzyme Database: 3.1.1.76
            ERGO genome analysis and discovery system: 3.1.1.76
            BRENDA, the Enzyme Database: 3.1.1.76
///
ENTRY       EC 3.1.1.77                 Enzyme
NAME        acyloxyacyl hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
REACTION    3-(acyloxy)acyl group of bacterial toxin = 3-hydroxyacyl group of
            bacterial toxin + a fatty acid [RN:R05792]
ALL_REAC    R05792
SUBSTRATE   3-(acyloxy)acyl group of bacterial toxin [CPD:C11547]
PRODUCT     3-hydroxyacyl group of bacterial toxin [CPD:C11548];
            fatty acid [CPD:C00162]
COMMENT     The substrate is lipid A on the reducing end of the toxic
            lipopolysaccharide (LPS) of Salmonella typhimurium and related
            organisms. It consists of diglucosamine, beta-D-GlcN-(1-> 6)-D-GlcN,
            attached by glycosylation on O-6 of its non-reducing residue,
            phosphorylated on O-4 of this residue and on O-1 of its potentially
            reducing residue. Both residues carry 3-(acyloxy)acyl groups on N-2
            and O-3. The enzyme from human leucocytes detoxifies the lipid by
            hydrolysing the secondary acyl groups from O-3 of the 3-hydroxyacyl
            groups on the disaccharide (LPS). It also possesses a wide range of
            phospholipase and acyltransferase activities [e.g. EC 3.1.1.4
            (phospholipase A2), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.32
            (phospholipase A1) and EC 3.1.1.52 (phosphatidylinositol
            deacylase)], hydrolysing diacylglycerol and phosphatidyl compounds,
            but not triacylglycerols. It has a preference for saturated C12-C16
            acyl groups.
REFERENCE   1  [PMID:2398058]
  AUTHORS   Erwin AL, Munford RS.
  TITLE     Deacylation of structurally diverse lipopolysaccharides by human
            acyloxyacyl hydrolase.
  JOURNAL   J. Biol. Chem. 265 (1990) 16444-9.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:1883828]
  AUTHORS   Hagen FS, Grant FJ, Kuijper JL, Slaughter CA, Moomaw CR, Orth K,
            O'Hara PJ, Munford RS.
  TITLE     Expression and characterization of recombinant human acyloxyacyl
            hydrolase, a leukocyte enzyme that deacylates bacterial
            lipopolysaccharides.
  JOURNAL   Biochemistry. 30 (1991) 8415-23.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:1577781]
  AUTHORS   Munford RS, Hunter JP.
  TITLE     Acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial
            lipopolysaccharides, has phospholipase, lysophospholipase,
            diacylglycerollipase, and acyltransferase activities in vitro.
  JOURNAL   J. Biol. Chem. 267 (1992) 10116-21.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01065  acyloxyacyl hydrolase
GENES       HSA: 313(AOAH)
            PTR: 463352(AOAH)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.77
            ExPASy - ENZYME nomenclature database: 3.1.1.77
            ExplorEnz - The Enzyme Database: 3.1.1.77
            ERGO genome analysis and discovery system: 3.1.1.77
            BRENDA, the Enzyme Database: 3.1.1.77
///
ENTRY       EC 3.1.1.78                 Enzyme
NAME        polyneuridine-aldehyde esterase;
            polyneuridine aldehyde esterase;
            PNAE
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     polyneuridine aldehyde hydrolase (decarboxylating)
REACTION    polyneuridine aldehyde + H2O = 16-epivellosimine + CO2 + methanol
            [RN:R05825]
ALL_REAC    R05825
SUBSTRATE   polyneuridine aldehyde [CPD:C11632];
            H2O [CPD:C00001]
PRODUCT     16-epivellosimine [CPD:C11633];
            CO2 [CPD:C00011];
            methanol [CPD:C00132]
COMMENT     Following hydrolysis of this indole alkaloid ester the carboxylic
            acid decarboxylates spontaneously giving the sarpagan skeleton. The
            enzyme also acts on akuammidine aldehyde (the 16-epimer of
            polyneuridine aldehyde).
REFERENCE   1
  AUTHORS   Pfitzner, A. and Stockigt, J.
  TITLE     Characterization of polyneuridine aldehyde esterase, a key enzyme in
            the biosynthesis of sarpagine ajmaline type alkaloids.
  JOURNAL   Planta Med. 48 (1983) 221-227.
REFERENCE   2
  AUTHORS   Pfitzner, A. and Stockigt, J.
  TITLE     Polyneuridine aldehyde esterase: an unusual specific enzyme involved
            in the biosynthesis of sarpagine type alkaloids.
  JOURNAL   J. Chem. Soc. Chem. Commun. (1983) 459-460.
  ORGANISM  Rauwolfia serpentina
REFERENCE   3  [PMID:10691977]
  AUTHORS   Dogru E, Warzecha H, Seibel F, Haebel S, Lottspeich F, Stockigt J.
  TITLE     The gene encoding polyneuridine aldehyde esterase of monoterpenoid
            indole alkaloid biosynthesis in plants is an ortholog of the
            alpha/betahydrolase super family.
  JOURNAL   Eur. J. Biochem. 267 (2000) 1397-406.
  ORGANISM  Rauwolfia serpentina
REFERENCE   4  [PMID:12071952]
  AUTHORS   Mattern-Dogru E, Ma X, Hartmann J, Decker H, Stockigt J.
  TITLE     Potential active-site residues in polyneuridine aldehyde esterase, a
            central enzyme of indole alkaloid biosynthesis, by modelling and
            site-directed mutagenesis.
  JOURNAL   Eur. J. Biochem. 269 (2002) 2889-96.
  ORGANISM  Rauwolfia serpentina
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
ORTHOLOGY   KO: K08233  polyneuridine-aldehyde esterase
GENES       ATH: AT2G23600(ACL) AT2G23610 AT4G37150 AT5G10300
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.78
            ExPASy - ENZYME nomenclature database: 3.1.1.78
            ExplorEnz - The Enzyme Database: 3.1.1.78
            ERGO genome analysis and discovery system: 3.1.1.78
            BRENDA, the Enzyme Database: 3.1.1.78
            CAS: 87041-55-2
///
ENTRY       EC 3.1.1.79                 Enzyme
NAME        hormone-sensitive lipase;
            HSL
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     diacylglycerol acylhydrolase
REACTION    (1) diacylglycerol + H2O = monoacylglycerol + a carboxylate
            [RN:R05209];
            (2) triacylglycerol + H2O = diacylglycerol + a carboxylate
            [RN:R01369];
            (3) monoacylglycerol + H2O = glycerol + a carboxylate [RN:R07293]
ALL_REAC    R01369 R05209 R07293
SUBSTRATE   diacylglycerol [CPD:C00165];
            H2O [CPD:C00001];
            triacylglycerol [CPD:C00422];
            monoacylglycerol [CPD:C01885]
PRODUCT     monoacylglycerol [CPD:C01885];
            carboxylate [CPD:C00060];
            diacylglycerol [CPD:C00165];
            glycerol [CPD:C00116]
COMMENT     This enzyme is a serine hydrolase. Compared with other lipases,
            hormone-sensitive lipase has a uniquely broad substrate specificity.
            It hydrolyses all acylglycerols (triacylglycerol, diacylglycerol and
            monoacylglycerol) [2,3,4] as well as cholesteryl esters [2,4],
            steroid fatty acid esters [5], retinyl esters [6] and p-nitrophenyl
            esters [4,7]. It exhibits a preference for the 1- or 3-ester bond of
            its acylglycerol substrate compared with the 2-ester bond [8]. The
            enzyme shows little preference for the fatty acids in the
            triacylglycerol, although there is some increase in activity with
            decreasing chain length. The enzyme activity is increased in
            response to hormones that elevate intracellular levels of cAMP.
REFERENCE   1  [PMID:10940339]
  AUTHORS   Holm C, Osterlund T, Laurell H, Contreras JA.
  TITLE     Molecular mechanisms regulating hormone-sensitive lipase and
            lipolysis.
  JOURNAL   Annu. Rev. Nutr. 20 (2000) 365-93.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:7240206]
  AUTHORS   Fredrikson G, Stralfors P, Nilsson NO, Belfrage P.
  TITLE     Hormone-sensitive lipase of rat adipose tissue. Purification and
            some properties.
  JOURNAL   J. Biol. Chem. 256 (1981) 6311-20.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:14169138]
  AUTHORS   VAUGHAN M, BERGER JE, STEINBERG D.
  TITLE     HORMONE-SENSITIVE LIPASE AND MONOGLYCERIDE LIPASE  ACTIVITIES IN
            ADIPOSE TISSUE.
  JOURNAL   J. Biol. Chem. 239 (1964) 401-9.
  ORGANISM  rabbit
REFERENCE   4  [PMID:8912675]
  AUTHORS   Osterlund T, Danielsson B, Degerman E, Contreras JA, Edgren G, Davis
            RC, Schotz MC, Holm C.
  TITLE     Domain-structure analysis of recombinant rat hormone-sensitive
            lipase.
  JOURNAL   Biochem. J. 319 ( Pt 2) (1996) 411-20.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:3196730]
  AUTHORS   Lee FT, Adams JB, Garton AJ, Yeaman SJ.
  TITLE     Hormone-sensitive lipase is involved in the hydrolysis of lipoidal
            derivatives of estrogens and other steroid hormones.
  JOURNAL   Biochim. Biophys. Acta. 963 (1988) 258-64.
  ORGANISM  cow [GN:bta]
REFERENCE   6  [PMID:9162045]
  AUTHORS   Wei S, Lai K, Patel S, Piantedosi R, Shen H, Colantuoni V, Kraemer
            FB, Blaner WS.
  TITLE     Retinyl ester hydrolysis and retinol efflux from BFC-1beta
            adipocytes.
  JOURNAL   J. Biol. Chem. 272 (1997) 14159-65.
  ORGANISM  cow [GN:bta]
REFERENCE   7  [PMID:2794798]
  AUTHORS   Tsujita T, Ninomiya H, Okuda H.
  TITLE     p-nitrophenyl butyrate hydrolyzing activity of hormone-sensitive
            lipase from bovine adipose tissue.
  JOURNAL   J. Lipid. Res. 30 (1989) 997-1004.
  ORGANISM  cow [GN:bta]
REFERENCE   8  [PMID:14725507]
  AUTHORS   Yeaman SJ.
  TITLE     Hormone-sensitive lipase--new roles for an old enzyme.
  JOURNAL   Biochem. J. 379 (2004) 11-22.
  ORGANISM  rat [GN:rno], human [GN:hsa]
PATHWAY     PATH: map04910  Insulin signaling pathway
ORTHOLOGY   KO: K07188  hormone-sensitive lipase
GENES       HSA: 3991(LIPE)
            MMU: 16890(Lipe)
            RNO: 25330(Lipe)
            CFA: 403607(LIPE)
            BTA: 286879(LIPE)
            SSC: 397583(LIPE)
            SPU: 585712(LOC585712)
            TET: TTHERM_00185900 TTHERM_00721650 TTHERM_00827140
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.79
            ExPASy - ENZYME nomenclature database: 3.1.1.79
            ExplorEnz - The Enzyme Database: 3.1.1.79
            ERGO genome analysis and discovery system: 3.1.1.79
            BRENDA, the Enzyme Database: 3.1.1.79
///
ENTRY       EC 3.1.1.80                 Enzyme
NAME        acetylajmaline esterase;
            AAE;
            2beta(R)-17-O-acetylajmalan:acetylesterase;
            acetylajmalan esterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic-ester hydrolases
SYSNAME     17-O-acetylajmaline O-acetylhydrolase
REACTION    (1) 17-O-acetylajmaline + H2O = ajmaline + acetate [RN:R07513];
            (2) 17-O-acetylnorajmaline + H2O = norajmaline + acetate [RN:R05880]
ALL_REAC    R05880 R07513
SUBSTRATE   17-O-acetylajmaline [CPD:C15985];
            H2O [CPD:C00001];
            17-O-acetylnorajmaline [CPD:C11809]
PRODUCT     ajmaline [CPD:C06542];
            acetate [CPD:C00033];
            norajmaline [CPD:C11810]
COMMENT     This plant enzyme is responsible for the last stages in the
            biosynthesis of the indole alkaloid ajmaline. The enzyme is highly
            specific for the substrates 17-O-acetylajmaline and
            17-O-acetylnorajmaline as the structurally related acetylated
            alkaloids vinorine, vomilenine, 1,2-dihydrovomilenine and
            1,2-dihydroraucaffricine cannot act as substrates [2]. This is a
            novel member of the GDSL family of serine esterases/lipases.
REFERENCE   1  [PMID:2955586]
  AUTHORS   Polz L, Schubel H, Stockigt J.
  TITLE     Characterization of 2 beta (R)-17-O-acetylajmalan: acetylesterase--a
            specific enzyme involved in the biosynthesis of the Rauwolfia
            alkaloid ajmaline.
  JOURNAL   Z. Naturforsch. [C]. 42 (1987) 333-42.
  ORGANISM  Rauwolfia serpentina
REFERENCE   2  [PMID:16133216]
  AUTHORS   Ruppert M, Woll J, Giritch A, Genady E, Ma X, Stockigt J.
  TITLE     Functional expression of an ajmaline pathway-specific esterase from
            Rauvolfia in a novel plant-virus expression system.
  JOURNAL   Planta. 222 (2005) 888-98.
  ORGANISM  Rauwolfia serpentina
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.1.80
            ExPASy - ENZYME nomenclature database: 3.1.1.80
            ExplorEnz - The Enzyme Database: 3.1.1.80
            ERGO genome analysis and discovery system: 3.1.1.80
            BRENDA, the Enzyme Database: 3.1.1.80
///
ENTRY       EC 3.1.1.-                  Enzyme
CLASS       Hydrolases;
            Acting on ester bonds;
            Carboxylic ester hydrolases
REACTION    (1) Poly-beta-hydroxybutyrate + H2O <=> ((R)-3-Hydroxybutanoyl)(n-2)
            + (R)-3-((R)-3-Hydroxybutanoyloxy)butanoate [RN:R05118];
            (2) 4-Sulfolactone + HO- <=> HSO3- + 2-Maleylacetate [RN:R05420];
            (3) Ecgonine methyl ester + H2O <=> Ecgonine + Methanol [RN:R06729];
            (4) L-Ascorbate 6-phosphate + H2O <=> 3-Dehydro-L-gulonate
            6-phosphate [RN:R07677];
            (5) L-Galactono-1,4-lactone + H2O <=> L-Galactonate [RN:R07680]
SUBSTRATE   Poly-beta-hydroxybutyrate [CPD:C06143];
            H2O [CPD:C00001];
            4-Sulfolactone [CPD:C06676];
            HO- [CPD:C01328];
            Ecgonine methyl ester [CPD:C12448]
PRODUCT     ((R)-3-Hydroxybutanoyl)(n-2) [CPD:C06147];
            (R)-3-((R)-3-Hydroxybutanoyloxy)butanoate [CPD:C04546];
            HSO3- [CPD:C11481];
            2-Maleylacetate [CPD:C02222];
            Ecgonine [CPD:C10858];
            Methanol [CPD:C00132]
///
ENTRY       EC 3.1.2.1                  Enzyme
NAME        acetyl-CoA hydrolase;
            acetyl-CoA deacylase;
            acetyl-CoA acylase;
            acetyl coenzyme A hydrolase;
            acetyl coenzyme A deacylase;
            acetyl coenzyme A acylase;
            acetyl-CoA thiol esterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     acetyl-CoA hydrolase
REACTION    acetyl-CoA + H2O = CoA + acetate [RN:R00227]
ALL_REAC    R00227
SUBSTRATE   acetyl-CoA [CPD:C00024];
            H2O [CPD:C00001]
PRODUCT     CoA [CPD:C00010];
            acetate [CPD:C00033]
REFERENCE   1
  AUTHORS   Gergely, J., Hele, P. and Ramakrishnan, C.V.
  TITLE     Succinyl and acetyl coenzyme A deacylases.
  JOURNAL   J. Biol. Chem. 198 (1952) 323-334.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K01067  acetyl-CoA hydrolase
GENES       HSA: 134526(ACOT12)
            MMU: 74156(Acot12)
            RNO: 170570(Acot12)
            CFA: 488925(ACOT12)
            XLA: 444535(MGC82100)
            SCE: YBL015W(ACH1)
            AGO: AGOS_AFR020W
            PIC: PICST_78208(ACH1)
            CGR: CAGL0J04268g
            SPO: SPAC1952.09c
            ANI: AN1547.2
            AFM: AFUA_8G05580
            AOR: AO090005000588
            DDI: DDB_0233380
            PPF: Pput_0172
            PFO: Pfl_0111
            PEN: PSEEN0113
            PCR: Pcryo_1227
            PHA: PSHAa2002(ygfH)
            PAT: Patl_3791
            REU: Reut_A1290
            REH: H16_A1358 H16_B1368
            RME: Rmet_4895
            BXE: Bxe_B0292 Bxe_B0397 Bxe_B1860
            BVI: Bcep1808_4692
            BUR: Bcep18194_A4202 Bcep18194_B1909 Bcep18194_C7279
            BCN: Bcen_4240
            BCH: Bcen2424_4126
            BAM: Bamb_3540
            RFR: Rfer_1216
            PNA: Pnap_0073
            AAV: Aave_0100
            AJS: Ajs_0046
            GUR: Gura_1337 Gura_4029
            PPD: Ppro_0286
            ADE: Adeh_1288
            AFW: Anae109_2477
            MXA: MXAN_2285
            SFU: Sfum_0388 Sfum_0389
            RLE: pRL90030
            OAN: Oant_2146
            RPB: RPB_0503
            RPC: RPC_0254
            RPD: RPD_0322
            RPE: RPE_0804
            XAU: Xaut_1730
            RSP: RSP_0029
            RSH: Rsph17029_1658
            RSQ: Rsph17025_2183
            PDE: Pden_4309
            ACR: Acry_1436
            RRU: Rru_A1927
            MAG: amb1383
            ABA: Acid345_0950
            SUS: Acid_6953
            RHA: RHA1_ro03558 RHA1_ro10175
            FAL: FRAAL3473
            CCH: Cag_0060
            MSE: Msed_1217
STRUCTURES  PDB: 2H4U  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.1
            ExPASy - ENZYME nomenclature database: 3.1.2.1
            ExplorEnz - The Enzyme Database: 3.1.2.1
            ERGO genome analysis and discovery system: 3.1.2.1
            BRENDA, the Enzyme Database: 3.1.2.1
            CAS: 9027-54-7
///
ENTRY       EC 3.1.2.2                  Enzyme
NAME        palmitoyl-CoA hydrolase;
            long-chain fatty-acyl-CoA hydrolase;
            palmitoyl coenzyme A hydrolase;
            palmitoyl thioesterase;
            palmitoyl coenzyme A hydrolase;
            palmitoyl-CoA deacylase;
            palmityl thioesterase;
            palmityl-CoA deacylase;
            fatty acyl thioesterase I;
            palmityl thioesterase I
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     palmitoyl-CoA hydrolase
REACTION    palmitoyl-CoA + H2O = CoA + palmitate [RN:R01274]
ALL_REAC    R01274
SUBSTRATE   palmitoyl-CoA [CPD:C00154];
            H2O [CPD:C00001]
PRODUCT     CoA [CPD:C00010];
            palmitate [CPD:C00249]
COMMENT     Also hydrolyses CoA thioesters of other long-chain fatty acids.
REFERENCE   1  [PMID:4871199]
  AUTHORS   Barnes EM Jr, Wakil SJ.
  TITLE     Studies on the mechanism of fatty acid synthesis. XIX. Preparation
            and general properties of palmityl thioesterase.
  JOURNAL   J. Biol. Chem. 243 (1968) 2955-62.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:6116156]
  AUTHORS   Berge RK, Farstad M.
  TITLE     Long-chain fatty acyl-CoA hydrolase from rat liver mitochondria.
  JOURNAL   Methods. Enzymol. 71 Pt C (1981) 234-42.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:6115749]
  AUTHORS   Miyazawa S, Furuta S, Hashimoto T.
  TITLE     Induction of a novel long-chain acyl-CoA hydrolase in rat liver by
            administration of peroxisome proliferators.
  JOURNAL   Eur. J. Biochem. 117 (1981) 425-30.
  ORGANISM  rat [GN:rno]
REFERENCE   4
  AUTHORS   Srere, P.A., Seubert, W. and Lynen, F.
  TITLE     Palmityl coenzyme A deacylase.
  JOURNAL   Biochim. Biophys. Acta 33 (1959) 313-319.
  ORGANISM  pig [GN:ssc]
REFERENCE   5
  AUTHORS   Yabusaki, K.K. and Ballou, C.E.
  TITLE     Long-chain fatty acyl-CoA thioesterases from Mycobacterium
            smegmatis.
  JOURNAL   Methods Enzymol. 71 (1981) 242-246.
  ORGANISM  Mycobacterium smegmatis [GN:msm]
ORTHOLOGY   KO: K01068  palmitoyl-CoA hydrolase
GENES       HSA: 10005(ACOT8) 10965(ACOT2) 11332(ACOT7) 122970(ACOT4)
                 570(BAAT)
            MMU: 170789(Acot8) 171210(Acot2) 171281(Acot3) 171282(Acot4)
                 217698(Acot5) 217700(Acot6) 26897(Acot1) 70025(Acot7)
            RNO: 170588(Acot8) 192272(Mte1) 26759(Acot7) 29725(Baat)
                 50559(Cte1)
            CFA: 477247(ACOT8) 490770(ACOT2) 490771(ACOT4)
            GGA: 419371(ACOT7)
            XLA: 414573(MGC83099)
            SPU: 577168(LOC577168) 589369(LOC589369)
            SCE: YJR019C(TES1)
            AGO: AGOS_ACL122W
            CGR: CAGL0B04059g
            AOR: AO090005001196
            UMA: UM00334.1
            YPA: YPA_2636
            YPP: YPDSF_2776
            ENT: Ent638_0920
            SPE: Spro_1111
            HSO: HS_1268(yciA)
            ASU: Asuc_1095
            PPF: Pput_4636
            PMY: Pmen_3719
            PCR: Pcryo_2285
            PRW: PsycPRwf_0166
            SDN: Sden_1670
            SFR: Sfri_2722
            SAZ: Sama_1368
            SBL: Sbal_2818
            SBM: Shew185_2836
            SLO: Shew_2556
            SPC: Sputcn32_1728
            SSE: Ssed_1466
            SPL: Spea_2791
            SHE: Shewmr4_1619
            SHM: Shewmr7_1694
            SHN: Shewana3_1688
            SHW: Sputw3181_2297
            PHA: PSHAa0141(tesB)
            PAT: Patl_2041
            SDE: Sde_2001
            PIN: Ping_1278
            MAQ: Maqu_3590
            MMW: Mmwyl1_1316
            BPA: BPP1246
            BBR: BB2315
            RFR: Rfer_0997
            VEI: Veis_0818
            HAR: HEAR3455(tesB)
            PLA: Plav_2850
            SMD: Smed_3049
            OAN: Oant_0958
            BRA: BRADO0310
            BBT: BBta_0297(tesB)
            RPC: RPC_0268
            RPD: RPD_0452
            RPE: RPE_0406
            NWI: Nwi_0078
            NHA: Nham_0087
            XAU: Xaut_2210
            MMR: Mmar10_2666
            NAR: Saro_1064
            SAL: Sala_1443
            SWI: Swit_0296 Swit_1035 Swit_2248
            ELI: ELI_02555
            SUS: Acid_3161
            BLD: BLi01024
            MVA: Mvan_2565
            MGI: Mflv_3831
            MMC: Mmcs_2249
            MKM: Mkms_2296
            MJL: Mjls_2288
            ART: Arth_2417
            NCA: Noca_2850 Noca_2851
            TFU: Tfu_0531
            KRA: Krad_3540
            SEN: SACE_1184
            STP: Strop_3159
            HBU: Hbut_0590
STRUCTURES  PDB: 1TBU  2Q2B  2QQ2  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.2
            ExPASy - ENZYME nomenclature database: 3.1.2.2
            ExplorEnz - The Enzyme Database: 3.1.2.2
            ERGO genome analysis and discovery system: 3.1.2.2
            BRENDA, the Enzyme Database: 3.1.2.2
            CAS: 9025-87-0
///
ENTRY       EC 3.1.2.3                  Enzyme
NAME        succinyl-CoA hydrolase;
            succinyl-CoA acylase;
            succinyl coenzyme A hydrolase;
            succinyl coenzyme A deacylase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     succinyl-CoA hydrolase
REACTION    succinyl-CoA + H2O = CoA + succinate [RN:R00407]
ALL_REAC    R00407
SUBSTRATE   succinyl-CoA [CPD:C00091];
            H2O [CPD:C00001]
PRODUCT     CoA [CPD:C00010];
            succinate [CPD:C00042]
REFERENCE   1
  AUTHORS   Gergely, J., Hele, P. and Ramakrishnan, C.V.
  TITLE     Succinyl and acetyl coenzyme A deacylases.
  JOURNAL   J. Biol. Chem. 198 (1952) 323-334.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.3
            ExPASy - ENZYME nomenclature database: 3.1.2.3
            ExplorEnz - The Enzyme Database: 3.1.2.3
            ERGO genome analysis and discovery system: 3.1.2.3
            BRENDA, the Enzyme Database: 3.1.2.3
            CAS: 9025-86-9
///
ENTRY       EC 3.1.2.4                  Enzyme
NAME        3-hydroxyisobutyryl-CoA hydrolase;
            3-hydroxy-isobutyryl CoA hydrolase;
            HIB CoA deacylase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     3-hydroxy-2-methylpropanoyl-CoA hydrolase
REACTION    3-hydroxy-2-methylpropanoyl-CoA + H2O = CoA +
            3-hydroxy-2-methylpropanoate [RN:R03352]
ALL_REAC    R03352;
            (other) R03157 R03158 R05064
SUBSTRATE   3-hydroxy-2-methylpropanoyl-CoA [CPD:C04047];
            H2O [CPD:C00001]
PRODUCT     CoA [CPD:C00010];
            3-hydroxy-2-methylpropanoate [CPD:C01188]
COMMENT     Also hydrolyses 3-hydroxypropanoyl-CoA.
REFERENCE   1
  AUTHORS   Rendina, G. and Coon, M.J.
  TITLE     Enzymatic hydrolysis of the coenzyme A thiol esters of
            beta-hydroxypropionic and beta-hydroxyisobutyric acids.
  JOURNAL   J. Biol. Chem. 225 (1957) 523-534.
  ORGANISM  pig [GN:ssc], Tetrahymena pyriformis, Neurospora crassa [GN:dncr]
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00410  beta-Alanine metabolism
            PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K05605  3-hydroxyisobutyryl-CoA hydrolase
GENES       HSA: 26275(HIBCH)
            MMU: 227095(Hibch)
            RNO: 301384(Hibch)
            BTA: 535883(HIBCH)
            GGA: 423979(RCJMB04_20j11)
            XTR: 548942(LOC548942)
            PFA: PFL1940w
            GBE: GbCGDNIH1_1815
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.4
            ExPASy - ENZYME nomenclature database: 3.1.2.4
            ExplorEnz - The Enzyme Database: 3.1.2.4
            ERGO genome analysis and discovery system: 3.1.2.4
            BRENDA, the Enzyme Database: 3.1.2.4
            CAS: 9025-88-1
///
ENTRY       EC 3.1.2.5                  Enzyme
NAME        hydroxymethylglutaryl-CoA hydrolase;
            beta-hydroxy-beta-methylglutaryl coenzyme A hydrolase;
            beta-hydroxy-beta-methylglutaryl coenzyme A deacylase;
            hydroxymethylglutaryl coenzyme A hydrolase;
            hydroxymethylglutaryl coenzyme A deacylase;
            3-hydroxy-3-methylglutaryl-CoA hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     (S)-3-hydroxy-3-methylglutaryl-CoA hydrolase
REACTION    (S)-3-hydroxy-3-methylglutaryl-CoA + H2O = CoA +
            3-hydroxy-3-methylglutarate [RN:R02083]
ALL_REAC    R02083
SUBSTRATE   (S)-3-hydroxy-3-methylglutaryl-CoA [CPD:C00356];
            H2O [CPD:C00001]
PRODUCT     CoA [CPD:C00010];
            3-hydroxy-3-methylglutarate [CPD:C03761]
REFERENCE   1  [PMID:13563516]
  AUTHORS   DEKKER EE, SCHLESINGER MJ, COON MJ.
  TITLE     beta-Hydroxy-beta-methylglutaryl coenzyme A deacylase.
  JOURNAL   J. Biol. Chem. 233 (1958) 434-8.
  ORGANISM  chicken [GN:gga], pig [GN:ssc], Neurospora crassa [GN:dncr],
            Escherichia coli [GN:eco], Tetrahymena pyriformis
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.5
            ExPASy - ENZYME nomenclature database: 3.1.2.5
            ExplorEnz - The Enzyme Database: 3.1.2.5
            ERGO genome analysis and discovery system: 3.1.2.5
            BRENDA, the Enzyme Database: 3.1.2.5
            CAS: 9025-89-2
///
ENTRY       EC 3.1.2.6                  Enzyme
NAME        hydroxyacylglutathione hydrolase;
            glyoxalase II;
            S-2-hydroxylacylglutathione hydrolase;
            hydroxyacylglutathione hydrolase;
            acetoacetylglutathione hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     S-(2-hydroxyacyl)glutathione hydrolase
REACTION    S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy
            carboxylate [RN:R04090]
ALL_REAC    R04090 > R01736
SUBSTRATE   S-(2-hydroxyacyl)glutathione [CPD:C03899];
            H2O [CPD:C00001]
PRODUCT     glutathione [CPD:C00051];
            2-hydroxy carboxylate [CPD:C02929]
COMMENT     Also hydrolyses S-acetoacetylglutathione, but more slowly.
REFERENCE   1  [PMID:13032160]
  AUTHORS   RACKER E.
  TITLE     Spectrophotometric measurements of the metabolic formation and
            degradation of thiol esters and enediol compounds.
  JOURNAL   Biochim. Biophys. Acta. 9 (1952) 577-8.
REFERENCE   2  [PMID:4200890]
  AUTHORS   Uotila L.
  TITLE     Preparation and assay of glutathione thiol esters. Survey of human
            liver glutathione thiol esterases.
  JOURNAL   Biochemistry. 12 (1973) 3938-43.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:4745654]
  AUTHORS   Uotila L.
  TITLE     Purification and characterization of S-2-hydroxyacylglutathione
            hydrolase (glyoxalase II) from human liver.
  JOURNAL   Biochemistry. 12 (1973) 3944-51.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K01069  hydroxyacylglutathione hydrolase
GENES       HSA: 3029(HAGH) 84264(HAGHL)
            PTR: 453828(HAGH)
            MMU: 14651(Hagh) 68977(Haghl)
            RNO: 24439(Hagh)
            CFA: 479888(HAGH) 490087(HAGHL)
            GGA: 416536(RCJMB04_21j14) 416537(RCJMB04_31d24)
            DRE: 336977(hagh)
            SPU: 578596(LOC578596)
            CEL: Y17G7B.3
            OSA: 4332736
            CME: CMT117C
            SCE: YDR272W(GLO2) YOR040W(GLO4)
            AGO: AGOS_ACR084C
            PIC: PICST_31656(GLO2)
            CGR: CAGL0I00924g
            SPO: SPAC824.07 SPCC13B11.03c
            ANI: AN6840.2
            AFM: AFUA_5G12840
            AOR: AO090120000408
            CNE: CND02510
            UMA: UM00589.1
            DDI: DDB_0230988(gloB1)
            PFA: PFD0311w PFL0285w
            TAN: TA21365
            TPV: TP01_0292
            TET: TTHERM_00052170 TTHERM_00120980 TTHERM_00361730
                 TTHERM_01467280
            TBR: Tb927.4.1350 Tb927.6.1080
            TCR: 507603.230 509429.290
            LMA: LmjF12.0220
            EHI: 61.t00038
            ECO: b0212(gloB)
            ECJ: JW0202(gloB)
            ECE: Z0236(gloB)
            ECS: ECs0208
            ECC: c0249(gloB)
            ECI: UTI89_C0231(gloB)
            ECP: ECP_0218
            ECV: APECO1_1778(gloB)
            ECW: EcE24377A_0217(gloB)
            ECX: EcHS_A0216(gloB)
            STY: STY0282(gloB)
            STT: t2604(gloB)
            SPT: SPA2508(gloB)
            SEC: SC0257(gloB)
            STM: STM0261(gloB)
            YPE: YPO1079(gloB)
            YPK: y3097(gloB)
            YPM: YP_2770(gloB3)
            YPA: YPA_0557
            YPN: YPN_2919
            YPP: YPDSF_1633
            YPS: YPTB2967(gloB)
            YEN: YE0919(gloB)
            SFL: SF0198(gloB)
            SFX: S0206(gloB)
            SFV: SFV_0196(gloB)
            SSN: SSON_0226(gloB)
            SBO: SBO_0201(gloB)
            SDY: SDY_0231(gloB)
            ECA: ECA3342(gloB)
            PLU: plu0940(gloB)
            BUC: BU246(gloB)
            BAS: BUsg238(gloB)
            BAB: bbp228(gloB)
            WBR: WGLp067(gloB)
            SGL: SG0589
            ENT: Ent638_0746
            KPN: KPN_00227(gloB)
            SPE: Spro_0909
            BFL: Bfl223(gloB)
            BPN: BPEN_230(gloB)
            HIT: NTHI1896(gloB)
            HDU: HD1197(gloB)
            HSO: HS_0809(gloB)
            PMU: PM0685
            MSU: MS0946(gloB)
            APL: APL_0415(gloB)
            ASU: Asuc_1187
            XFA: XF2160
            XFT: PD1220(gloB)
            XCC: XCC0985(gloB)
            XCB: XC_3258
            XCV: XCV1087(gloB)
            XAC: XAC1087(gloB)
            XOO: XOO1039(gloB)
            XOM: XOO_0938(XOO0938)
            VCH: VC2236
            VVU: VV1_1883(gloB)
            VVY: VV0153 VV2532(gloB)
            VPA: VP2295(gloB)
            VFI: VF1938
            PPR: PBPRA2920(gloB)
            PAE: PA1813
            PAU: PA14_41080
            PAP: PSPA7_3483(gloB)
            PPU: PP_4144(gloB)
            PPF: Pput_1721
            PST: PSPTO_3714
            PSB: Psyr_1761
            PSP: PSPPH_1710
            PFL: PFL_3299
            PFO: Pfl_2184
            PEN: PSEEN0914 PSEEN3561
            PMY: Pmen_2064
            PAR: Psyc_1038
            PCR: Pcryo_1432 Pcryo_1778
            PRW: PsycPRwf_1411
            ACI: ACIAD2452
            SON: SO_2563
            SDN: Sden_2021
            SFR: Sfri_2207
            SAZ: Sama_1884
            SBL: Sbal_1996
            SBM: Shew185_2011
            SLO: Shew_2114
            SPC: Sputcn32_1776
            SSE: Ssed_1989
            SPL: Spea_2406
            SHE: Shewmr4_2161
            SHM: Shewmr7_2238
            SHN: Shewana3_2369
            SHW: Sputw3181_2249
            ILO: IL1697(gloB)
            CPS: CPS_1999
            PHA: PSHAa1401 PSHAa1966(gloB)
            PAT: Patl_1895
            SDE: Sde_2023
            PIN: Ping_0498
            MAQ: Maqu_1536
            CBU: CBU_0314
            LPN: lpg1295
            LPF: lpl1257(gloB)
            LPP: lpp1258(gloB)
            MCA: MCA0343
            FTU: FTT1405c(gloB)
            FTF: FTF1405c(gloB)
            FTL: FTL_0657
            FTH: FTH_0660(gloB)
            FTN: FTN_1370(gloB)
            TCX: Tcr_0926 Tcr_0932
            NOC: Noc_1532 Noc_1713 Noc_1750 Noc_2007
            AEH: Mlg_1994
            HHA: Hhal_1587
            HCH: HCH_02525
            CSA: Csal_1944
            ABO: ABO_1336(blaB)
            MMW: Mmwyl1_1702
            AHA: AHA_1567
            BCI: BCI_0475(gloB)
            VOK: COSY_0753
            NME: NMB1997
            NMA: NMA0444
            NMC: NMC1973
            NGO: NGO1187(gloB)
            CVI: CV_1254(gloB)
            RSO: RSc1515(gloB)
            REU: Reut_A2187
            REH: H16_A0190(gloB1) H16_A1980 H16_A2209 H16_A2464(gloB2)
                 H16_A3582(gloB3) H16_A3623
            RME: Rmet_2206 Rmet_3484
            BMA: BMA0765(gloB)
            BMV: BMASAVP1_A1275(gloB)
            BML: BMA10299_A0594(gloB)
            BMN: BMA10247_0558(gloB)
            BXE: Bxe_A1253
            BVI: Bcep1808_1240
            BUR: Bcep18194_A3388 Bcep18194_A4429 Bcep18194_A5043
                 Bcep18194_B0182
            BCN: Bcen_0806
            BCH: Bcen2424_1287
            BAM: Bamb_0199 Bamb_1164
            BPS: BPSL1344
            BPM: BURPS1710b_0044(glob1) BURPS1710b_1602(gloB) BURPS1710b_2664
            BTE: BTH_I2788
            PNU: Pnuc_1022
            BPE: BP3213(gloB)
            BPA: BPP3836(gloB)
            BBR: BB4280(gloB)
            RFR: Rfer_1462
            POL: Bpro_2055
            PNA: Pnap_1678
            AAV: Aave_2651
            AJS: Ajs_1743
            VEI: Veis_0591
            MPT: Mpe_A0934 Mpe_A2529
            HAR: HEAR0917 HEAR2321
            MMS: mma_1210(gloB)
            NEU: NE0138
            NET: Neut_2178
            NMU: Nmul_A1621
            EBA: ebA6461
            AZO: azo1208(gloB1) azo2057(gloB2) azo3379
            DAR: Daro_1595
            TBD: Tbd_1665
            MFA: Mfla_1481 Mfla_1733
            HPA: HPAG1_0798
            PCA: Pcar_3076
            BBA: Bd2204(gloB) Bd3549
            ADE: Adeh_1984
            AFW: Anae109_1866
            MXA: MXAN_0179 MXAN_2490
            SAT: SYN_01158 SYN_01287 SYN_02709
            PUB: SAR11_0219(gloB) SAR11_1229
            MLO: mlr3546
            MES: Meso_3080
            PLA: Plav_1578
            SME: SMc00708(gloB)
            SMD: Smed_2552
            ATU: Atu3614(gloB)
            ATC: AGR_L_2423
            RET: RHE_CH01013 RHE_CH03013 RHE_CH03812(gloB) RHE_PC00020
                 RHE_PE00220
            RLE: RL1093 RL3458 RL4340(gloB) pRL100240
            BME: BMEI0129 BMEI0496 BMEI1432 BMEII0771
            BMF: BAB1_1936 BAB2_0739
            BMS: BR1936
            BMB: BruAb1_1912
            BOV: BOV_1863(gloB)
            OAN: Oant_0923
            BJA: blr0222(gloB)
            BRA: BRADO0567
            BBT: BBta_7609
            RPA: RPA0610
            RPB: RPB_0069
            RPC: RPC_0508
            RPD: RPD_0093
            RPE: RPE_0164 RPE_0233 RPE_3980 RPE_4355
            NWI: Nwi_0113 Nwi_0373 Nwi_0890 Nwi_2895
            NHA: Nham_0466
            BHE: BH16640(gloB)
            BQU: BQ13520(gloB)
            XAU: Xaut_2019
            CCR: CC_0519
            SIL: SPO3168
            SIT: TM1040_2091
            RSP: RSP_0204 RSP_2294(gloB)
            RSH: Rsph17029_0969
            RSQ: Rsph17025_2206
            JAN: Jann_1042
            RDE: RD1_0533 RD1_0785 RD1_2249 RD1_3539(gloB)
            PDE: Pden_3813
            MMR: Mmar10_2381
            HNE: HNE_3406
            ZMO: ZMO0759
            NAR: Saro_1321
            SAL: Sala_0684
            SWI: Swit_1663 Swit_1986 Swit_2505 Swit_2798
            ELI: ELI_07510
            GOX: GOX0280 GOX2647
            GBE: GbCGDNIH1_0453
            ACR: Acry_1778
            RRU: Rru_A1522 Rru_A3270
            MAG: amb4192
            MGM: Mmc1_1222 Mmc1_1657
            BAN: BA2538
            BAR: GBAA2538
            BAA: BA_3036
            BAT: BAS2361
            BCE: BC3511
            BCZ: BCZK2277(gloB)
            BTK: BT9727_2319(gloB)
            BTL: BALH_2913(gloB)
            BLI: BL02060
            BLD: BLi02785
            BAY: RBAM_014270(ykqC) RBAM_016900(baeB)
            GKA: GK2088
            SAB: SAB0031
            SAA: SAUSA300_0086
            SPZ: M5005_Spy_0533
            SPH: MGAS10270_Spy0528
            SPI: MGAS10750_Spy0552
            SPJ: MGAS2096_Spy0545
            SPK: MGAS9429_Spy0524
            SPF: SpyM51330
            SPA: M6_Spy0554
            SPB: M28_Spy0512
            SAK: SAK_0673
            CTC: CTC02196
            MTU: Rv0634c Rv2581c
            MBO: Mb0651c Mb2612c
            MBB: BCG_0681c BCG_2604c
            MSM: MSMEG_1334 MSMEG_5385
            MMC: Mmcs_0914 Mmcs_2284 Mmcs_5312
            RHA: RHA1_ro06806 RHA1_ro06903
            FRA: Francci3_1241
            SEN: SACE_3148 SACE_4442 SACE_4489
            FNU: FN1162
            LIL: LA2116(gloB)
            LBJ: LBJ_1894
            LBL: LBL_1390
            SYN: sll1019(gloB) slr1259
            SYW: SYNW1543
            SYC: syc0152_d syc0605_d
            SYF: Synpcc7942_0937 Synpcc7942_1403
            SYD: Syncc9605_0966
            SYE: Syncc9902_0879
            SYG: sync_1941
            SYR: SynRCC307_0839(gloB)
            SYX: SynWH7803_0694(gloB)
            CYA: CYA_1132 CYA_1720
            CYB: CYB_0151 CYB_1927
            TEL: tll1639 tlr1626
            GVI: gll3339
            ANA: all0580 alr3904
            AVA: Ava_0328 Ava_1793
            PMA: Pro0561(gloB)
            PMM: PMM0559
            PMT: PMT1194
            PMN: PMN2A_1889
            PMI: PMT9312_0559
            PMB: A9601_06151
            PMC: P9515_06231
            PMF: P9303_08221
            PMG: P9301_05851
            PMH: P9215_06401(gloB)
            PME: NATL1_06141
            TER: Tery_3786
            CHU: CHU_1354
            CTE: CT2045
            CCH: Cag_0125
            PLT: Plut_1997
            DEH: cbdb_A762
            DGE: Dgeo_2681
            TTJ: TTHA0837
            MAC: MA2320
            MBA: Mbar_A2729
            MMA: MM_2931
            HWA: HQ1377A HQ2288A HQ3137A
            NPH: NP2670A NP3944A NP3970A NP4032A
            PAB: PAB0703
STRUCTURES  PDB: 1QH3  1QH5  1XM8  2GCU  2Q42  2QED  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.6
            ExPASy - ENZYME nomenclature database: 3.1.2.6
            ExplorEnz - The Enzyme Database: 3.1.2.6
            ERGO genome analysis and discovery system: 3.1.2.6
            BRENDA, the Enzyme Database: 3.1.2.6
            CAS: 9025-90-5
///
ENTRY       EC 3.1.2.7                  Enzyme
NAME        glutathione thiolesterase;
            citryl-glutathione thioesterhydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     S-acylglutathione hydrolase
REACTION    S-acylglutathione + H2O = glutathione + a carboxylate [RN:R00547]
ALL_REAC    R00547
SUBSTRATE   S-acylglutathione [CPD:C02589];
            H2O [CPD:C00001]
PRODUCT     glutathione [CPD:C00051];
            carboxylate [CPD:C00060]
REFERENCE   1  [PMID:13130552]
  AUTHORS   KIELLEY WW, BRADLEY LB.
  TITLE     Glutathione thiolesterase.
  JOURNAL   J. Biol. Chem. 206 (1954) 327-33.
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.7
            ExPASy - ENZYME nomenclature database: 3.1.2.7
            ExplorEnz - The Enzyme Database: 3.1.2.7
            ERGO genome analysis and discovery system: 3.1.2.7
            BRENDA, the Enzyme Database: 3.1.2.7
            CAS: 9025-99-4
///
ENTRY       EC 3.1.2.8        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
COMMENT     Deleted entry: S-acetoacylglutathione hydrolase. Now included with
            EC 3.1.2.6 hydroxyacylglutathione hydrolase (EC 3.1.2.8 created
            1961, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.8
            ExPASy - ENZYME nomenclature database: 3.1.2.8
            ExplorEnz - The Enzyme Database: 3.1.2.8
            ERGO genome analysis and discovery system: 3.1.2.8
            BRENDA, the Enzyme Database: 3.1.2.8
///
ENTRY       EC 3.1.2.9        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
COMMENT     Deleted entry: S-acetoacetylhydrolipoate hydrolase (EC 3.1.2.9
            created 1961, deleted 1964)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.9
            ExPASy - ENZYME nomenclature database: 3.1.2.9
            ExplorEnz - The Enzyme Database: 3.1.2.9
            ERGO genome analysis and discovery system: 3.1.2.9
            BRENDA, the Enzyme Database: 3.1.2.9
///
ENTRY       EC 3.1.2.10                 Enzyme
NAME        formyl-CoA hydrolase;
            formyl coenzyme A hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     formyl-CoA hydrolase
REACTION    formyl-CoA + H2O = CoA + formate [RN:R00521]
ALL_REAC    R00521
SUBSTRATE   formyl-CoA [CPD:C00798];
            H2O [CPD:C00001]
PRODUCT     CoA [CPD:C00010];
            formate [CPD:C00058]
REFERENCE   1
  AUTHORS   Sly, W.S. and Stadtman, E.R.
  TITLE     Formate metabolism. I. Formyl coenzyme A, an intermediate in the
            formate-dependent decomposition of acetyl phosphate in Clostridium
            kluyveri.
  JOURNAL   J. Biol. Chem. 238 (1963) 2632-2638.
  ORGANISM  Clostridium kluyveri
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.10
            ExPASy - ENZYME nomenclature database: 3.1.2.10
            ExplorEnz - The Enzyme Database: 3.1.2.10
            ERGO genome analysis and discovery system: 3.1.2.10
            BRENDA, the Enzyme Database: 3.1.2.10
            CAS: 9025-91-6
///
ENTRY       EC 3.1.2.11                 Enzyme
NAME        acetoacetyl-CoA hydrolase;
            acetoacetyl coenzyme A hydrolase;
            acetoacetyl CoA deacylase;
            acetoacetyl coenzyme A deacylase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     acetoacetyl-CoA hydrolase
REACTION    acetoacetyl-CoA + H2O = CoA + acetoacetate [RN:R01358]
ALL_REAC    R01358
SUBSTRATE   acetoacetyl-CoA [CPD:C00332];
            H2O [CPD:C00001]
PRODUCT     CoA [CPD:C00010];
            acetoacetate [CPD:C00164]
REFERENCE   1  [PMID:6131897]
  AUTHORS   Aragon JJ, Lowenstein JM.
  TITLE     A survey of enzymes which generate or use acetoacetyl thioesters in
            rat liver.
  JOURNAL   J. Biol. Chem. 258 (1983) 4725-33.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:13818236]
  AUTHORS   DRUMMOND GI, STERN JR.
  TITLE     Enzymes of ketone body metabolism. II. Properties of an
            acetoacetate-synthesizing enzyme prepared from ox liver.
  JOURNAL   J. Biol. Chem. 235 (1960) 318-25.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00650  Butanoate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.11
            ExPASy - ENZYME nomenclature database: 3.1.2.11
            ExplorEnz - The Enzyme Database: 3.1.2.11
            ERGO genome analysis and discovery system: 3.1.2.11
            BRENDA, the Enzyme Database: 3.1.2.11
            CAS: 37288-10-1
///
ENTRY       EC 3.1.2.12                 Enzyme
NAME        S-formylglutathione hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     S-formylglutathione hydrolase
REACTION    S-formylglutathione + H2O = glutathione + formate [RN:R00527]
ALL_REAC    R00527
SUBSTRATE   S-formylglutathione [CPD:C01031];
            H2O [CPD:C00001]
PRODUCT     glutathione [CPD:C00051];
            formate [CPD:C00058]
COMMENT     Also hydrolyses S-acetylglutathione, but more slowly.
REFERENCE   1  [PMID:4200890]
  AUTHORS   Uotila L.
  TITLE     Preparation and assay of glutathione thiol esters. Survey of human
            liver glutathione thiol esterases.
  JOURNAL   Biochemistry. 12 (1973) 3938-43.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:4436331]
  AUTHORS   Uotila L, Koivusalo M.
  TITLE     Purification and properties of S-formylglutathione hydrolase from
            human liver.
  JOURNAL   J. Biol. Chem. 249 (1974) 7664-72.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:8892832]
  AUTHORS   Harms N, Ras J, Reijnders WN, van Spanning RJ, Stouthamer AH.
  TITLE     S-formylglutathione hydrolase of Paracoccus denitrificans is
            homologous to human esterase D: a universal pathway for formaldehyde
            detoxification?
  JOURNAL   J. Bacteriol. 178 (1996) 6296-9.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00680  Methane metabolism
ORTHOLOGY   KO: K01070  S-formylglutathione hydrolase
GENES       CAL: CaO19.6596
            CNE: CNG03680
            UMA: UM04202.1
            ECW: EcE24377A_0380(fghA1) EcE24377A_2450(fghA2)
            ECX: EcHS_A0420(fghA2) EcHS_A2288(fghA1)
            YPI: YpsIP31758_2474(fghA)
            VFI: VF0644
            PAP: PSPA7_1511(fghA)
            PAR: Psyc_1717
            CVI: CV_0739
            BPL: BURPS1106A_0867(fghA)
            BPD: BURPS668_0863(fghA)
            HAR: HEAR2036(fghA)
            MXA: MXAN_7093(fghA)
            BOV: BOV_0122(fghA)
            BRA: BRADO5460(fghA)
            BBT: BBta_5942(fghA)
            RSP: RSP_0852(fghA)
            RDE: RD1_0888
            HNE: HNE_0555(fghA)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.12
            ExPASy - ENZYME nomenclature database: 3.1.2.12
            ExplorEnz - The Enzyme Database: 3.1.2.12
            ERGO genome analysis and discovery system: 3.1.2.12
            UM-BBD (Biocatalysis/Biodegradation Database): 3.1.2.12
            BRENDA, the Enzyme Database: 3.1.2.12
            CAS: 50812-21-0
///
ENTRY       EC 3.1.2.13                 Enzyme
NAME        S-succinylglutathione hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     S-succinylglutathione hydrolase
REACTION    S-succinylglutathione + H2O = glutathione + succinate [RN:R00499]
ALL_REAC    R00499
SUBSTRATE   S-succinylglutathione [CPD:C03174];
            H2O [CPD:C00001]
PRODUCT     glutathione [CPD:C00051];
            succinate [CPD:C00042]
REFERENCE   1  [PMID:4200890]
  AUTHORS   Uotila L.
  TITLE     Preparation and assay of glutathione thiol esters. Survey of human
            liver glutathione thiol esterases.
  JOURNAL   Biochemistry. 12 (1973) 3938-43.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:457667]
  AUTHORS   Uotila L.
  TITLE     Purification and properties of S-succinylglutathione hydrolase from
            human liver.
  JOURNAL   J. Biol. Chem. 254 (1979) 7024-9.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.13
            ExPASy - ENZYME nomenclature database: 3.1.2.13
            ExplorEnz - The Enzyme Database: 3.1.2.13
            ERGO genome analysis and discovery system: 3.1.2.13
            BRENDA, the Enzyme Database: 3.1.2.13
            CAS: 50812-22-1
///
ENTRY       EC 3.1.2.14                 Enzyme
NAME        oleoyl-[acyl-carrier-protein] hydrolase;
            acyl-[acyl-carrier-protein] hydrolase;
            acyl-ACP-hydrolase;
            acyl-acyl carrier protein hydrolase;
            oleoyl-ACP thioesterase;
            oleoyl-acyl carrier protein thioesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     oleoyl-[acyl-carrier-protein] hydrolase
REACTION    oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] +
            oleate [RN:R02814]
ALL_REAC    R02814;
            (other) R01706
SUBSTRATE   oleoyl-[acyl-carrier-protein];
            H2O [CPD:C00001]
PRODUCT     [acyl-carrier-protein];
            oleate [CPD:C00712]
COMMENT     Acts on acyl-carrier-protein thioesters of fatty acids from C12 to
            C18, but the derivative of oleic acid is hydrolysed much more
            rapidly than any other compound tested.
REFERENCE   1  [PMID:30409]
  AUTHORS   Ohlrogge JB, Shine WE, Stumpf PK.
  TITLE     Fat metabolism in higher plants. Characterization of plant acyl-ACP
            and acyl-CoA hydrolases.
  JOURNAL   Arch. Biochem. Biophys. 189 (1978) 382-91.
  ORGANISM  Persea americana
REFERENCE   2  [PMID:3134]
  AUTHORS   Shine WE, Mancha M, Stumpf PK.
  TITLE     Fat metabolism in higher plants. The function of acyl thioesterases
            in the metabolism of acyl-coenzymes A and acyl-acyl carrier
            proteins.
  JOURNAL   Arch. Biochem. Biophys. 172 (1976) 110-6.
  ORGANISM  Persea americana
PATHWAY     PATH: map00061  Fatty acid biosynthesis
ORTHOLOGY   KO: K01071  oleoyl-[acyl-carrier-protein] hydrolase
GENES       HSA: 2194(FASN) 55301(OLAH)
            MMU: 14104(Fasn) 99035(Olah)
            RNO: 50671(Fasn) 64669(Thedc1)
            BTA: 281152(FASN)
            GGA: 396061(FASN) 420532(OLAH)
            SPU: 582714(LOC582714)
            CEL: F32H2.5(fasn-1)
            SCE: YKL182W(FAS1)
            AGO: AGOS_AER085C
            CGR: CAGL0D00528g
            SPO: SPAC926.09c(fas1)
            CNE: CNE04370
            PEN: PSEEN2139
            SDE: Sde_3728
            BUR: Bcep18194_B0669
            BAM: Bamb_6482
            DDE: Dde_1605
            XAU: Xaut_1005
            SPZ: M5005_Spy_0766
            SPM: spyM18_1023
            SPG: SpyM3_0674
            SPS: SPs1179
            SPH: MGAS10270_Spy0883
            SPI: MGAS10750_Spy0918
            SPJ: MGAS2096_Spy0840
            SPK: MGAS9429_Spy0881
            SPF: SpyM50993
            SPA: M6_Spy0791
            SPB: M28_Spy0745
            SMU: SMU.1417c
            STC: str1235
            STL: stu1235
            STE: STER_1215
            SSA: SSA_1076
            LPL: lp_0708(fat)
            LJO: LJ0432
            LAC: LBA0386
            LSA: LSA0345
            LSL: LSL_1220
            LDB: Ldb1626
            LBU: LBUL_1506
            LBR: LVIS_0609
            LCA: LSEI_2254
            LGA: LGAS_0377
            EFA: EF0365
            CTC: CTC00119
            CBE: Cbei_0248
            DSY: DSY2004
            CGB: cg0957(fas-IB) cg2743(fas-IA)
            FAL: FRAAL2559 FRAAL3859
            SEN: SACE_0729 SACE_2628 SACE_3258 SACE_4275 SACE_4286
            AVA: Ava_3990 Ava_4730
STRUCTURES  PDB: 2OWN  2PFF  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.14
            ExPASy - ENZYME nomenclature database: 3.1.2.14
            ExplorEnz - The Enzyme Database: 3.1.2.14
            ERGO genome analysis and discovery system: 3.1.2.14
            BRENDA, the Enzyme Database: 3.1.2.14
            CAS: 68009-83-6
///
ENTRY       EC 3.1.2.15                 Enzyme
NAME        ubiquitin thiolesterase;
            ubiquitin carboxy-terminal esterase;
            isopeptidase;
            isopeptidase T;
            ubiquitin C-terminal hydrolase;
            ubiquitin carboxy-terminal hydrolase;
            ubiquitin-C-terminal-thiolester hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     ubiquitin-C-terminal-thioester hydrolase
REACTION    ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol
            [RN:R02418]
ALL_REAC    R02418
SUBSTRATE   ubiquitin C-terminal thioester;
            H2O [CPD:C00001]
PRODUCT     ubiquitin [CPD:C00496];
            thiol [CPD:C00145]
COMMENT     Acts on esters formed between thiols such as dithiothreitol or
            glutathione and the C-terminal glycine residue of the polypeptide
            ubiquitin. Also acts on AMP-ubiquitin. May be the same as EC
            3.4.19.12, ubiquitinyl hydrolase 1.
REFERENCE   1  [PMID:6313036]
  AUTHORS   Rose IA, Warms JV.
  TITLE     An enzyme with ubiquitin carboxy-terminal esterase activity from
            reticulocytes.
  JOURNAL   Biochemistry. 22 (1983) 4234-7.
  ORGANISM  rabbit
ORTHOLOGY   KO: K01072  ubiquitin thiolesterase
            KO: K08601  ubiquitin thioesterase CYLD
GENES       HSA: 10600(USP16) 10617(STAMBP) 10868(USP20) 11274(USP18)
                 1540(CYLD) 158880(USP51) 219333(USP12) 23032(USP33)
                 23326(USP22) 27005(USP21) 29761(USP25) 55031(USP47)
                 55230(USP40) 57558(USP35) 57602(USP36) 57646(USP28)
                 57663(USP29) 57695(USP37) 64854(USP46) 7375(USP4) 7398(USP1)
                 7874(USP7) 8078(USP5) 8237(USP11) 8239(USP9X) 8287(USP9Y)
                 83844(USP26) 84101(USP44) 84132(USP42) 84640(USP38)
                 84669(USP32) 84749(USP30) 8975(USP13) 9097(USP14) 9098(USP6)
                 9099(USP2) 9100(USP10) 9101(USP8) 9958(USP15) 9960(USP3)
            PTR: 451029(USP47) 453499(USP3) 453907(USP7) 455325(USP14)
                 460367(USP4) 461515(USP38) 465165(CYLD) 465660(USP51)
                 469031(USP29) 469556(USP21) 471009(USP13) 473918(USP25)
                 739448(STAMBP)
            MCC: 706514(LOC706514)
            MMU: 13531(Dub1) 14479(Usp15) 170822(Usp33) 22217(Usp12)
                 22224(Usp10) 22225(Usp5) 22258(Usp4) 22284(Usp9x)
                 227334(Usp40) 230484(Usp1) 235441(Usp3) 24110(Usp18)
                 252870(Usp7) 30940(Usp25) 30941(Usp21) 319651(Usp37)
                 53376(Usp2) 57775(Usp29) 59025(Usp14) 69727(Usp46)
                 70527(Stambp) 72607(Usp13) 74256(Cyld) 74841(Usp38)
                 74996(Usp47) 83563(Usp26) 84092(Usp8)
            RNO: 115771(Usp2) 171329(Usp15) 171565(Stambp) 290864(LOC290864)
                 307764(Usp38_predicted) 310306(Usp13_predicted) 313387(Usp1)
            CFA: 404014(USP11) 476071(USP38) 476624(USP4) 478387(USP25)
                 478398(USP16) 478640(USP13) 479549(USP1) 479625(USP10)
                 479754(USP42) 479854(USP7) 480182(USP14) 480696(USP20)
                 480885(LOC480885) 483344(USP36) 485168(USP35) 486033(USP12)
                 486168(USP40) 486718(USP5) 486763(USP18) 487590(USP3)
                 488523(USP37) 489400(USP28) 492143(USP26) 608188(USP2)
                 611649(CYLD)
            BTA: 536421(MGC137952)
            SSC: 396777(UBP)
            GGA: 395126(USP7) 395644(USP15) 395766(USP2) 415369(USP3)
                 415451(USP8) 415725(CYLD) 415817(USP10) 415937(USP4)
                 416431(USP42) 416501(USP22) 416896(USP30) 417188(USP20)
                 418167(USP18) 418290(USP5) 418471(USP25) 418485(USP16)
                 418569(USP9X) 421063(USP14) 422455(USP38) 422758(USP46)
                 423032(USP47) 424029(USP40) 424216(USP37) 424553(USP33)
                 424685(RCJMB04_19b7) 425176(STAMBP) 428078(USP12)
                 428246(RCJMB04_27l24) 429286(USP13)
            XLA: 379981(usp46) 380243(usp8) 398480(LOC398480) 446581(usp25)
                 447256(MGC86287) 447469(MGC81730) 447733(MGC81945)
                 494775(LOC494775) 495686(LOC495686)
            XTR: 448110(usp14) 448475(usp3)
            DRE: 335736(usp14) 393470(stambp) 406508(usp33) 406618(usp5)
                 556823(LOC556823)
            SPU: 575057(LOC575057) 576305(LOC576305) 577573(LOC577573)
                 578149(LOC578149) 579661(LOC579661) 581896(LOC581896)
                 583779(LOC583779) 592342(LOC592342) 752405(LOC752405)
            DME: Dmel_CG11025(isopeptidase-T-3) Dmel_CG12082 Dmel_CG1490(Usp7)
                 Dmel_CG1945(faf) Dmel_CG2904(ec) Dmel_CG4166(not) Dmel_CG5384
                 Dmel_CG5486(Ubp64E) Dmel_CG5505(mule) Dmel_CG5603(CYLD)
                 Dmel_CG5798
            CEL: C13B4.2(usp-14) H19N07.2(math-33) H34C03.2 K02C4.3 R10E11.3
                 T27A3.2
            ATH: AT1G51710(UBP6) AT2G22310(ATUBP4) AT3G11910 AT3G20630(UBP14)
                 AT3G21280(UBP7) AT4G39910(ATUBP3)
            OSA: 4323863 4326194 4331901 4336009 4342469
            CME: CMG042C CMT098C CMT224C
            SCE: YBL067C(UBP13) YBR058C(UBP14) YDL122W(UBP1) YDR069C(DOA4)
                 YER098W(UBP9) YER144C(UBP5) YER151C(UBP3) YFR010W(UBP6)
                 YIL156W(UBP7) YJL197W(UBP12) YKR098C(UBP11) YMR223W(UBP8)
                 YMR304W(UBP15) YNL186W(UBP10) YOR124C(UBP2)
            AGO: AGOS_ABL145W AGOS_ACL164C AGOS_AEL029W AGOS_AEL242W
                 AGOS_AFR551W AGOS_AFR627C AGOS_AGL357W AGOS_AGR023C
                 AGOS_AGR139C AGOS_AGR370W AGOS_AGR389C
            PIC: PICST_32361 PICST_48002 PICST_54531 PICST_61453(USP39)
                 PICST_62413 PICST_65573 PICST_69820 PICST_90001(UBP15)
            CAL: CaO19.1777 CaO19.3370(ubp10) CaO19.7207
                 CaO19_1516(CaO19.1516) CaO19_457(CaO19.457)
                 CaO19_7367(CaO19.7367)
            CGR: CAGL0A04477g CAGL0G05247g CAGL0H05335g CAGL0H06721g
                 CAGL0H10186g CAGL0H10582g CAGL0I06600g CAGL0I06765g
                 CAGL0K10252g CAGL0K10494g CAGL0L01639g CAGL0M11198g
                 CAGL0M13783g
            SPO: SPAC13A11.04c SPAC27F1.03c SPAC6G9.08 SPBC1703.12 SPBC6B1.06c
                 SPBC713.02c(ubpd) SPCC1494.05c SPCC16A11.12c SPCC188.08c
            ANI: AN2072.2 AN2873.2 AN3711.2 AN6354.2 AN6913.2 AN7422.2
            AFM: AFUA_1G07160 AFUA_2G04720 AFUA_2G06330 AFUA_2G08440
                 AFUA_2G14130 AFUA_3G11700 AFUA_4G07520 AFUA_4G12910
                 AFUA_5G01750 AFUA_5G03250 AFUA_5G11950 AFUA_5G13620
                 AFUA_6G02380 AFUA_6G12270 AFUA_6G12710
            AOR: AO090001000752 AO090003000271 AO090003000389 AO090003000728
                 AO090009000193 AO090023000173 AO090102000527 AO090113000003
                 AO090120000125
            CNE: CNA02030 CNA07360 CNF02660 CNG04540 CNH02890
            UMA: UM00298.1 UM02269.1 UM02340.1 UM02639.1 UM02911.1
            DDI: DDBDRAFT_0167082 DDBDRAFT_0192113 DDBDRAFT_0202821
                 DDBDRAFT_0219558 DDB_0191402(ubpB) DDB_0231492(ubpA)
            PFA: MAL1P1.34b MAL7P1.147 PF11_0177 PF13_0096 PF14_0576 PFD0165w
                 PFD0655c PFE0835w PFE1355c
            CPV: cgd1_290 cgd2_3450 cgd6_4550
            CHO: Chro.10040 Chro.20366 Chro.60521
            TAN: TA04875 TA10095 TA12645 TA16070 TA17680 TA19865 TA21275
            TPV: TP01_0316 TP03_0494 TP04_0767
            TET: TTHERM_00047700 TTHERM_00048860 TTHERM_00077370
                 TTHERM_00101230 TTHERM_00161340 TTHERM_00193880
                 TTHERM_00312010 TTHERM_00313670 TTHERM_00324420
                 TTHERM_00378550 TTHERM_00590040 TTHERM_00721760
                 TTHERM_00757780 TTHERM_00847000 TTHERM_00895800
                 TTHERM_01094790 TTHERM_01108760 TTHERM_01205390
                 TTHERM_01261800 TTHERM_01289070
            TBR: Tb09.160.4020 Tb09.211.4270 Tb09.211.4910 Tb10.70.5540
                 Tb11.01.4060 Tb11.01.6080 Tb11.01.7760 Tb11.02.2940
                 Tb11.46.0014 Tb927.3.4840 Tb927.4.3790 Tb927.5.2400
                 Tb927.6.1110 Tb927.6.2690 Tb927.8.5620
            TCR: 504125.30 504131.170 504443.10 506569.10 506871.50 507507.40
                 508153.120 509955.10 509965.40 510325.10 510761.70 511499.50
            LMA: LmjF24.0620 LmjF29.2300 LmjF30.1200 LmjF31.0140 LmjF32.1250
                 LmjF35.1740
            EHI: 12.t00002 16.t00011 45.t00006 64.t00009
STRUCTURES  PDB: 1CMX  1IXD  1NB8  1NBF  1UCH  1VDL  1VJV  1W6V  1WGG  1WH0  
                 1WHB  1YY6  1YZE  2A9U  2AYN  2AYO  2DAG  2DAK  2F1W  2F1Z  
                 2FOJ  2FOO  2FOP  2G43  2G45  2GFO  2GWF  2HD5  2I50  2IBI  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.15
            ExPASy - ENZYME nomenclature database: 3.1.2.15
            ExplorEnz - The Enzyme Database: 3.1.2.15
            ERGO genome analysis and discovery system: 3.1.2.15
            BRENDA, the Enzyme Database: 3.1.2.15
            CAS: 86480-67-3
///
ENTRY       EC 3.1.2.16                 Enzyme
NAME        citrate lyase deacetylase;
            [citrate-(pro-3S)-lyase] thiolesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     [citrate-(pro-3S)-lyase](acetyl-form) hydrolase
REACTION    [citrate (pro-3S)-lyase](acetyl form) + H2O = [citrate
            (pro-3S)-lyase](thiol form) + acetate [RN:R04450]
ALL_REAC    R04450
SUBSTRATE   [citrate (pro-3S)-lyase](acetyl form) [CPD:C04334];
            H2O [CPD:C00001]
PRODUCT     [citrate (pro-3S)-lyase](thiol form) [CPD:C04298];
            acetate [CPD:C00033]
COMMENT     Hydrolysis inactivates EC 4.1.3.6 citrate (pro-3S)-lyase.
REFERENCE   1  [PMID:7460909]
  AUTHORS   Giffhorn F, Rode H, Kuhn A, Gottschalk G.
  TITLE     Citrate lyase deacetylase of Rhodopseudomonas gelatinosa. Isolation
            of the enzyme and studies on the inhibition by L-glutamate.
  JOURNAL   Eur. J. Biochem. 111 (1980) 461-71.
  ORGANISM  Rhodopseudomonas gelatinosa
ORTHOLOGY   KO: K05975  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.16
            ExPASy - ENZYME nomenclature database: 3.1.2.16
            ExplorEnz - The Enzyme Database: 3.1.2.16
            ERGO genome analysis and discovery system: 3.1.2.16
            BRENDA, the Enzyme Database: 3.1.2.16
            CAS: 58319-93-0
///
ENTRY       EC 3.1.2.17                 Enzyme
NAME        (S)-methylmalonyl-CoA hydrolase;
            D-methylmalonyl-coenzyme A hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     (S)-methylmalonyl-CoA hydrolase
REACTION    (S)-methylmalonyl-CoA + H2O = methylmalonate + CoA [RN:R02764]
ALL_REAC    R02764
SUBSTRATE   (S)-methylmalonyl-CoA [CPD:C00683];
            H2O [CPD:C00001]
PRODUCT     methylmalonate [CPD:C02170];
            CoA [CPD:C00010]
REFERENCE   1  [PMID:6885824]
  AUTHORS   Kovachy RJ, Copley SD, Allen RH.
  TITLE     Recognition, isolation, and characterization of rat liver
            D-methylmalonyl coenzyme A hydrolase.
  JOURNAL   J. Biol. Chem. 258 (1983) 11415-21.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00640  Propanoate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.17
            ExPASy - ENZYME nomenclature database: 3.1.2.17
            ExplorEnz - The Enzyme Database: 3.1.2.17
            ERGO genome analysis and discovery system: 3.1.2.17
            BRENDA, the Enzyme Database: 3.1.2.17
            CAS: 87928-03-8
///
ENTRY       EC 3.1.2.18                 Enzyme
NAME        ADP-dependent short-chain-acyl-CoA hydrolase;
            short-chain acyl coenzyme A hydrolase;
            propionyl coenzyme A hydrolase;
            propionyl-CoA hydrolase;
            propionyl-CoA thioesterase;
            short-chain acyl-CoA hydrolase;
            short-chain acyl-CoA thioesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     ADP-dependent-short-chain-acyl-CoA hydrolase
REACTION    acyl-CoA + H2O = CoA + a carboxylate [RN:R00383]
ALL_REAC    R00383
SUBSTRATE   acyl-CoA [CPD:C00040];
            H2O [CPD:C00001]
PRODUCT     CoA [CPD:C00010];
            carboxylate [CPD:C00060]
COFACTOR    ADP [CPD:C00008]
INHIBITOR   NADH [CPD:C00004]
COMMENT     Requires ADP; inhibited by NADH. Maximum activity is shown with
            propanoyl-CoA.
REFERENCE   1  [PMID:2901416]
  AUTHORS   Alexson SE, Nedergaard J.
  TITLE     A novel type of short- and medium-chain acyl-CoA hydrolases in brown
            adipose tissue mitochondria.
  JOURNAL   J. Biol. Chem. 263 (1988) 13564-71.
  ORGANISM  hamster
REFERENCE   2  [PMID:2570608]
  AUTHORS   Alexson SE, Svensson LT, Nedergaard J.
  TITLE     NADH-sensitive propionyl-CoA hydrolase in brown-adipose-tissue
            mitochondria of the rat.
  JOURNAL   Biochim. Biophys. Acta. 1005 (1989) 13-9.
  ORGANISM  rat [GN:rno]
GENES       GBE: GbCGDNIH1_1102
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.18
            ExPASy - ENZYME nomenclature database: 3.1.2.18
            ExplorEnz - The Enzyme Database: 3.1.2.18
            ERGO genome analysis and discovery system: 3.1.2.18
            BRENDA, the Enzyme Database: 3.1.2.18
            CAS: 117698-16-5
///
ENTRY       EC 3.1.2.19                 Enzyme
NAME        ADP-dependent medium-chain-acyl-CoA hydrolase;
            medium-chain acyl coenzyme A hydrolase;
            medium-chain acyl-CoA hydrolase;
            medium-chain acyl-thioester hydrolase;
            medium-chain hydrolase;
            myristoyl-CoA thioesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     ADP-dependent-medium-chain-acyl-CoA hydrolase
REACTION    acyl-CoA + H2O = CoA + a carboxylate [RN:R00383]
ALL_REAC    R00383
SUBSTRATE   acyl-CoA [CPD:C00040];
            H2O [CPD:C00001]
PRODUCT     CoA [CPD:C00010];
            carboxylate [CPD:C00060]
COFACTOR    ADP [CPD:C00008]
INHIBITOR   NADH [CPD:C00004]
COMMENT     Requires ADP; inhibited by NADH. Maximum activity is shown with
            nonanoyl-CoA.
REFERENCE   1  [PMID:2901416]
  AUTHORS   Alexson SE, Nedergaard J.
  TITLE     A novel type of short- and medium-chain acyl-CoA hydrolases in brown
            adipose tissue mitochondria.
  JOURNAL   J. Biol. Chem. 263 (1988) 13564-71.
  ORGANISM  hamster
ORTHOLOGY   KO: K05976  
GENES       CVI: CV_2722
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.19
            ExPASy - ENZYME nomenclature database: 3.1.2.19
            ExplorEnz - The Enzyme Database: 3.1.2.19
            ERGO genome analysis and discovery system: 3.1.2.19
            BRENDA, the Enzyme Database: 3.1.2.19
            CAS: 63363-75-7
///
ENTRY       EC 3.1.2.20                 Enzyme
NAME        acyl-CoA hydrolase;
            acyl coenzyme A thioesterase;
            acyl-CoA thioesterase;
            acyl coenzyme A hydrolase;
            thioesterase B;
            thioesterase II;
            acyl-CoA thioesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     acyl-CoA hydrolase
REACTION    acyl-CoA + H2O = CoA + a carboxylate [RN:R00383]
ALL_REAC    R00383
SUBSTRATE   acyl-CoA [CPD:C00040];
            H2O [CPD:C00001]
PRODUCT     CoA [CPD:C00010];
            carboxylate [CPD:C00060]
COMMENT     Broad specificity for medium- to long-chain acyl-CoA. Insensitive to
            NAD+ (cf. EC 3.1.2.19 ADP-dependent medium-chain-acyl-CoA hydrolase)
REFERENCE   1  [PMID:2570608]
  AUTHORS   Alexson SE, Svensson LT, Nedergaard J.
  TITLE     NADH-sensitive propionyl-CoA hydrolase in brown-adipose-tissue
            mitochondria of the rat.
  JOURNAL   Biochim. Biophys. Acta. 1005 (1989) 13-9.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K01073  acyl-CoA hydrolase
GENES       ABO: ABO_1029(tesB) ABO_1111
            CVI: CV_3735(tesA)
            REH: H16_A0465 H16_B1236
            BPM: BURPS1710b_2941
            AZO: azo1666(tesA1) azo2123(tesA2)
            SAT: SYN_01088
            BME: BMEI0503
            BMB: BruAb1_1502
            SIT: TM1040_0858
            GBE: GbCGDNIH1_2360
            BAN: BA2053
            BAR: GBAA2053
            BAT: BAS1906
            BCE: BC2038
            BCA: BCE_2122
            BCZ: BCZK1859
            BTK: BT9727_1869
            BTL: BALH_1815
            LSA: LSA0644
            LSL: LSL_1721
            LCA: LSEI_1984
            CTA: CTA_0584(yciA)
            TTH: TTC1452
            PTO: PTO0793
STRUCTURES  PDB: 1Y7U  2GVH  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.20
            ExPASy - ENZYME nomenclature database: 3.1.2.20
            ExplorEnz - The Enzyme Database: 3.1.2.20
            ERGO genome analysis and discovery system: 3.1.2.20
            BRENDA, the Enzyme Database: 3.1.2.20
            CAS: 37270-64-7
///
ENTRY       EC 3.1.2.21                 Enzyme
NAME        dodecanoyl-[acyl-carrier-protein] hydrolase;
            lauryl-acyl-carrier-protein hydrolase;
            dodecanoyl-acyl-carrier-protein hydrolase;
            dodecyl-acyl-carrier protein hydrolase;
            dodecanoyl-[acyl-carrier protein] hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     dodecanoyl-[acyl-carrier-protein] hydrolase
REACTION    dodecanoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] +
            dodecanoate [RN:R04014]
ALL_REAC    R04014
SUBSTRATE   dodecanoyl-[acyl-carrier-protein];
            H2O [CPD:C00001]
PRODUCT     [acyl-carrier-protein];
            dodecanoate [CPD:C02679]
COMMENT     Acts on the acyl-carrier-protein thioester of C12 and, with a much
            lower activity, C14 fatty acids. The derivative of oleic acid is
            hydrolysed very slowly (cf. EC 3.1.2.14,
            oleoyl-[acyl-carrier-protein] hydrolase).
REFERENCE   1  [PMID:1989513]
  AUTHORS   Pollard MR, Anderson L, Fan C, Hawkins DJ, Davies HM.
  TITLE     A specific acyl-ACP thioesterase implicated in medium-chain fatty
            acid production in immature cotyledons of Umbellularia californica.
  JOURNAL   Arch. Biochem. Biophys. 284 (1991) 306-12.
  ORGANISM  Umbellularia californica
REFERENCE   2  [PMID:1898097]
  AUTHORS   Davies HM, Anderson L, Fan C, Hawkins DJ.
  TITLE     Developmental induction, purification, and further characterization
            of 12:0-ACP thioesterase from immature cotyledons of Umbellularia
            californica.
  JOURNAL   Arch. Biochem. Biophys. 290 (1991) 37-45.
  ORGANISM  Umbellularia californica
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.21
            ExPASy - ENZYME nomenclature database: 3.1.2.21
            ExplorEnz - The Enzyme Database: 3.1.2.21
            ERGO genome analysis and discovery system: 3.1.2.21
            BRENDA, the Enzyme Database: 3.1.2.21
            CAS: 137903-37-8
///
ENTRY       EC 3.1.2.22                 Enzyme
NAME        palmitoyl[protein] hydrolase;
            palmitoyl-protein thioesterase;
            palmitoyl-(protein) hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     palmitoyl[protein] hydrolase
REACTION    palmitoyl[protein] + H2O = palmitate + protein [RN:R01705]
ALL_REAC    R01705;
            (other) R01274
SUBSTRATE   palmitoyl[protein];
            H2O [CPD:C00001]
PRODUCT     palmitate [CPD:C00249];
            protein [CPD:C00017]
COMMENT     Specific for long-chain thioesters of fatty acids. Hydrolyses fatty
            acids from S-acylated cysteine residues in proteins, palmitoyl
            cysteine and palmitoyl-CoA.
REFERENCE   1  [PMID:7651163]
  AUTHORS   Camp LA, Hofmann SL.
  TITLE     Assay and isolation of palmitoyl-protein thioesterase from bovine
            brain using palmitoylated H-Ras as substrate.
  JOURNAL   Methods. Enzymol. 250 (1995) 336-47.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:8786130]
  AUTHORS   Schriner JE, Yi W, Hofmann SL.
  TITLE     cDNA and genomic cloning of human palmitoyl-protein thioesterase
            (PPT), the enzyme defective in infantile neuronal ceroid
            lipofuscinosis.
  JOURNAL   Genomics. 34 (1996) 317-22.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:8663305]
  AUTHORS   Verkruyse LA, Hofmann SL.
  TITLE     Lysosomal targeting of palmitoyl-protein thioesterase.
  JOURNAL   J. Biol. Chem. 271 (1996) 15831-6.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00062  Fatty acid elongation in mitochondria
ORTHOLOGY   KO: K01074  palmitoyl-protein thioesterase
GENES       HSA: 5538(PPT1) 9374(PPT2)
            MMU: 19063(Ppt1) 54397(Ppt2)
            RNO: 29411(Ppt1) 54398(Ppt2)
            CFA: 474856(PPT2) 475316(PPT1)
            BTA: 281421(PPT1)
            GGA: 419681(RCJMB04_15o4)
            XLA: 379689(MGC68884)
            XTR: 448650(ppt1)
            DRE: 393135(zgc:55621) 406648(ppt1)
            SPU: 587708(LOC587708)
            DME: Dmel_CG12108(Ppt1) Dmel_CG4851
            CEL: F44C4.5(ppt-1)
            ATH: AT4G17470
            OSA: 4331284
            PIC: PICST_83712
            ANI: AN2497.2
            AFM: AFUA_3G14060
            AOR: AO090012000721
            CNE: CNA00890
            UMA: UM05641.1
            DDI: DDBDRAFT_0186550 DDBDRAFT_0188120
            TET: TTHERM_00591650
STRUCTURES  PDB: 1EH5  1EI9  1EXW  1PJA  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.22
            ExPASy - ENZYME nomenclature database: 3.1.2.22
            ExplorEnz - The Enzyme Database: 3.1.2.22
            ERGO genome analysis and discovery system: 3.1.2.22
            BRENDA, the Enzyme Database: 3.1.2.22
            CAS: 150605-49-5
///
ENTRY       EC 3.1.2.23                 Enzyme
NAME        4-hydroxybenzoyl-CoA thioesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     4-hydroxybenzoyl-CoA hydrolase
REACTION    4-hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA [RN:R01301]
ALL_REAC    R01301
SUBSTRATE   4-hydroxybenzoyl-CoA [CPD:C02949];
            H2O [CPD:C00001]
PRODUCT     4-hydroxybenzoate [CPD:C00156];
            CoA [CPD:C00010]
COMMENT     This enzyme is part of the bacterial 2,4-dichlorobenzoate
            degradation pathway.
REFERENCE   1  [PMID:1610806]
  AUTHORS   Chang KH, Liang PH, Beck W, Scholten JD, Dunaway-Mariano D.
  TITLE     Isolation and characterization of the three polypeptide components
            of 4-chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS-3.
  JOURNAL   Biochemistry. 31 (1992) 5605-10.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:7765837]
  AUTHORS   Dunaway-Mariano D, Babbitt PC.
  TITLE     On the origins and functions of the enzymes of the 4-chlorobenzoate
            to 4-hydroxybenzoate converting pathway.
  JOURNAL   Biodegradation. 5 (1994) 259-76.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
ORTHOLOGY   KO: K01075  4-hydroxybenzoyl-CoA thioesterase
GENES       RSO: RS02013(RSp0038) RSc1827(RS04258)
            REU: Reut_A2179
            REH: H16_A1529 H16_A2456
            RME: Rmet_2197
            BXE: Bxe_B0277
            BPE: BP0312
            BPA: BPP3939
            BBR: BB4412
            RFR: Rfer_0270
            POL: Bpro_0588 Bpro_3115
            PNA: Pnap_0799
            AZO: azo1929 azo2495(fcbC1) azo3044(ybgC) azo3771(fcbC2)
            BJA: blr3414 blr7847
            BRA: BRADO0965
            BBT: BBta_3245 BBta_7090
            RPE: RPE_3801
            SIL: SPO0786 SPO1457
            SIT: TM1040_2232
            JAN: Jann_1329
            BCZ: BCZK3313
            BTL: BALH_3247 BALH_4099
            BPU: BPUM_1704(yneP)
            RHA: RHA1_ro02376
            RBA: RB8462
            LIL: LA1207 LA3529 LA4149
            LIC: LIC12488
STRUCTURES  PDB: 1HN1  1LO7  1LO8  1LO9  1Q4S  1Q4T  1Q4U  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.23
            ExPASy - ENZYME nomenclature database: 3.1.2.23
            ExplorEnz - The Enzyme Database: 3.1.2.23
            ERGO genome analysis and discovery system: 3.1.2.23
            UM-BBD (Biocatalysis/Biodegradation Database): 3.1.2.23
            BRENDA, the Enzyme Database: 3.1.2.23
            CAS: 141583-19-9
///
ENTRY       EC 3.1.2.24       Obsolete  Enzyme
NAME        Transferred to 3.13.1.3
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
COMMENT     Transferred entry: 2-(2-hydroxyphenyl)benzenesulfinate hydrolase,
            the enzyme was incorrectly classified as a thioester hydrolase when
            the bond broken is a C-S bond, which is not an ester. Now EC
            3.13.1.3, 2'-hydroxybiphenyl-2-sulfinate desulfinase (EC 3.1.2.24
            created 2000, deleted 2005)
GENES       BBA: Bd2489(ruvC)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.24
            ExPASy - ENZYME nomenclature database: 3.1.2.24
            ExplorEnz - The Enzyme Database: 3.1.2.24
            ERGO genome analysis and discovery system: 3.1.2.24
            BRENDA, the Enzyme Database: 3.1.2.24
///
ENTRY       EC 3.1.2.25                 Enzyme
NAME        phenylacetyl-CoA hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     phenylglyoxylyl-CoA hydrolase
REACTION    phenylglyoxylyl-CoA + H2O = phenylglyoxylate + CoA [RN:R07294]
ALL_REAC    R07294
SUBSTRATE   phenylglyoxylyl-CoA [CPD:C15524];
            H2O [CPD:C00001]
PRODUCT     phenylglyoxylate [CPD:C02137];
            CoA [CPD:C00010]
COMMENT     This is the second step in the conversion of phenylacetyl-CoA to
            phenylglyoxylate, the first step being carried out by EC 1.17.5.1,
            phenylacetyl-CoA dehydrogenase.
REFERENCE   1  [PMID:10336636]
  AUTHORS   Rhee SK, Fuchs G.
  TITLE     Phenylacetyl-CoA:acceptor oxidoreductase, a membrane-bound
            molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of
            phenylalanine in the denitrifying bacterium Thauera aromatica.
  JOURNAL   Eur. J. Biochem. 262 (1999) 507-15.
  ORGANISM  Thauera aromatica
REFERENCE   2  [PMID:9575237]
  AUTHORS   Schneider S, Fuchs G.
  TITLE     Phenylacetyl-CoA:acceptor oxidoreductase, a new alpha-oxidizing
            enzyme that produces phenylglyoxylate. Assay, membrane localization,
            and differential production in Thauera aromatica.
  JOURNAL   Arch. Microbiol. 169 (1998) 509-16.
  ORGANISM  Thauera aromatica
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.25
            ExPASy - ENZYME nomenclature database: 3.1.2.25
            ExplorEnz - The Enzyme Database: 3.1.2.25
            ERGO genome analysis and discovery system: 3.1.2.25
            BRENDA, the Enzyme Database: 3.1.2.25
///
ENTRY       EC 3.1.2.26                 Enzyme
NAME        bile-acid-CoA hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     deoxycholoyl-CoA hydrolase
REACTION    deoxycholoyl-CoA + H2O = CoA + deoxycholate [RN:R07295]
ALL_REAC    R07295
SUBSTRATE   deoxycholoyl-CoA [CPD:C15560];
            H2O [CPD:C00001]
PRODUCT     CoA [CPD:C00010];
            deoxycholate [CPD:C04483]
COMMENT     Choloyl-CoA, 3-dehydrocholoyl-CoA and chenodeoxycholoyl-CoA can also
            act as substrates, but acetyl-CoA, isovaleryl-CoA, palmitoyl-CoA and
            phenylacetyl-CoA cannot.
REFERENCE   1  [PMID:9869646]
  AUTHORS   Ye HQ, Mallonee DH, Wells JE, Bjorkhem I, Hylemon PB.
  TITLE     The bile acid-inducible baiF gene from Eubacterium sp. strain VPI
            12708 encodes a bile acid-coenzyme A hydrolase.
  JOURNAL   J. Lipid. Res. 40 (1999) 17-23.
  ORGANISM  Eubacterium sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.26
            ExPASy - ENZYME nomenclature database: 3.1.2.26
            ExplorEnz - The Enzyme Database: 3.1.2.26
            ERGO genome analysis and discovery system: 3.1.2.26
            BRENDA, the Enzyme Database: 3.1.2.26
///
ENTRY       EC 3.1.2.27                 Enzyme
NAME        choloyl-CoA hydrolase;
            PTE-2 (ambiguous);
            choloyl-coenzyme A thioesterase;
            chenodeoxycholoyl-coenzyme A thioesterase;
            peroxisomal acyl-CoA thioesterase 2
CLASS       Hydrolases;
            Acting on ester bonds;
            Thioester hydrolases
SYSNAME     choloyl-CoA hydrolase
REACTION    choloyl-CoA + H2O = cholate + CoA [RN:R07296]
ALL_REAC    R07296
SUBSTRATE   choloyl-CoA [CPD:C01794];
            H2O [CPD:C00001]
PRODUCT     cholate [CPD:C00695];
            CoA [CPD:C00010]
COMMENT     Also acts on chenodeoxycholoyl-CoA and to a lesser extent on short-
            and medium- to long-chain acyl-CoAs, and other substrates, including
            trihydroxycoprostanoyl-CoA, hydroxymethylglutaryl-CoA and branched
            chain acyl-CoAs, all of which are present in peroxisomes. The enzyme
            is strongly inhibited by CoA and may be involved in controlling CoA
            levels in the peroxisome [1].
REFERENCE   1  [PMID:11673457]
  AUTHORS   Hunt MC, Solaas K, Kase BF, Alexson SE.
  TITLE     Characterization of an acyl-coA thioesterase that functions as a
            major regulator of peroxisomal lipid metabolism.
  JOURNAL   J. Biol. Chem. 277 (2002) 1128-38.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:10817395]
  AUTHORS   Solaas K, Sletta RJ, Soreide O, Kase BF.
  TITLE     Presence of choloyl- and chenodeoxycholoyl-coenzyme A thioesterase
            activity in human liver.
  JOURNAL   Scand. J. Clin. Lab. Invest. 60 (2000) 91-102.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:12543708]
  AUTHORS   Russell DW.
  TITLE     The enzymes, regulation, and genetics of bile acid synthesis.
  JOURNAL   Annu. Rev. Biochem. 72 (2003) 137-74.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.2.27
            ExPASy - ENZYME nomenclature database: 3.1.2.27
            ExplorEnz - The Enzyme Database: 3.1.2.27
            ERGO genome analysis and discovery system: 3.1.2.27
            BRENDA, the Enzyme Database: 3.1.2.27
///
ENTRY       EC 3.1.2.-                  Enzyme
CLASS       Hydrolases;
            Acting on ester bonds;
            Thiolester hydrolases
REACTION    (1) 2-Ketocyclohexane-1-carboxyl-CoA + H2O <=> 6-Carboxyhexanoyl-CoA
            [RN:R05592];
            (2) 6-Oxo-2-hydroxycyclohexane-1-carboxyl-CoA + H2O <=>
            3-Hydroxypimeloyl-CoA [RN:R05593];
            (3) 3-Isopropylbut-3-enoyl-CoA + H2O <=> 3-Isopropylbut-3-enoic acid
            + CoA [RN:R06415];
            (4) 1,4-Dihydroxy-2-naphthoyl-CoA + H2O <=>
            1,4-Dihydroxy-2-naphthoate + CoA [RN:R07262]
SUBSTRATE   2-Ketocyclohexane-1-carboxyl-CoA [CPD:C09813];
            H2O [CPD:C00001];
            6-Oxo-2-hydroxycyclohexane-1-carboxyl-CoA [CPD:C09825];
            3-Isopropylbut-3-enoyl-CoA [CPD:C11949];
            1,4-Dihydroxy-2-naphthoyl-CoA [CPD:C15547]
PRODUCT     6-Carboxyhexanoyl-CoA [CPD:C01063];
            3-Hydroxypimeloyl-CoA [CPD:C06714];
            3-Isopropylbut-3-enoic acid [CPD:C11950];
            CoA [CPD:C00010];
            1,4-Dihydroxy-2-naphthoate [CPD:C03657]
///
ENTRY       EC 3.1.3.1                  Enzyme
NAME        alkaline phosphatase;
            alkaline phosphomonoesterase;
            phosphomonoesterase;
            glycerophosphatase;
            alkaline phosphohydrolase;
            alkaline phenyl phosphatase;
            orthophosphoric-monoester phosphohydrolase (alkaline optimum)
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     phosphate-monoester phosphohydrolase (alkaline optimum)
REACTION    a phosphate monoester + H2O = an alcohol + phosphate [RN:R00626]
ALL_REAC    R00626 > R01010 R03024;
            (other) R04620
SUBSTRATE   phosphate monoester [CPD:C01153];
            H2O [CPD:C00001]
PRODUCT     alcohol [CPD:C00069];
            phosphate [CPD:C00009]
COMMENT     Wide specificity. Also catalyses transphosphorylations. The human
            placental enzyme is a zinc protein. Some enzymes hydrolyse
            diphosphate (cf. EC 3.6.1.1 inorganic diphosphatase)
REFERENCE   1
  AUTHORS   Engstrom, L.
  TITLE     Studies on calf-intestinal alkaline phosphatase. I. Chromatographic
            purification, microheterogeneity and some other properties of the
            purified enzyme.
  JOURNAL   Biochim. Biophys. Acta 52 (1961) 36-48.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:4970479]
  AUTHORS   Harkness DR.
  TITLE     Studies on human placental alkaline phosphatase. II. Kinetic
            properties and studies on the apoenzyme.
  JOURNAL   Arch. Biochem. Biophys. 126 (1968) 513-23.
  ORGANISM  human [GN:hsa]
REFERENCE   3
  AUTHORS   Malamy, M.H. and Horecker, B.L.
  TITLE     Purification and crystallization of the alkaline phosphatase of
            Escherichia coli.
  JOURNAL   Biochemistry 3 (1964) 1893-1897.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:13115375]
  AUTHORS   MORTON RK.
  TITLE     Alkaline phosphatase of milk. 2. Purification of the enzyme.
  JOURNAL   Biochem. J. 55 (1953) 795-800.
  ORGANISM  cow [GN:bta]
REFERENCE   5
  AUTHORS   Stadtman, T.C.
  TITLE     Alkaline phosphatases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 5, Academic Press, New York, 1961, p. 55-71.
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
            PATH: map00790  Folate biosynthesis
            PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K01077  alkaline phosphatase
GENES       HSA: 248(ALPI) 249(ALPL) 250(ALPP) 251(ALPPL2)
            MMU: 11647(Akp2) 11648(Akp3) 11650(Akp5)
            RNO: 24197(Alpi) 25586(Alpl) 64621(Alpi2)
            CFA: 403548(ALPL) 403736(ALPI)
            BTA: 280993(ALPI) 280994(ALPL)
            GGA: 396317(ALPL) 424936(ALPI)
            XLA: 380589(alpl)
            DRE: 393982(alp)
            SPU: 577089(LOC577089) 578161(LOC578161) 580300(LOC580300)
                 584498(LOC584498)
            DME: Dmel_CG10592 Dmel_CG10827 Dmel_CG1462(Aph-4) Dmel_CG16771
                 Dmel_CG1809 Dmel_CG3264 Dmel_CG3290 Dmel_CG3292 Dmel_CG5150
                 Dmel_CG5656 Dmel_CG8105
            SCE: YDR481C(PHO8)
            AGO: AGOS_AGL260W
            PIC: PICST_43722(PHO82) PICST_82654(PHO8)
            CGR: CAGL0H07359g
            SPO: SPBC14F5.13c
            ANI: AN4516.2
            AFM: AFUA_2G03110 AFUA_6G08710
            AOR: AO090023000621 AO090120000280
            UMA: UM03579.1 UM04114.1
            DDI: DDB_0231570(alp)
            ECO: b0383(phoA)
            ECJ: JW0374(phoA) JW0445(ybaA)
            ECE: Z0479(phoA)
            ECS: ECs0433
            ECC: c0490(phoA)
            ECI: UTI89_C0402(phoA)
            ECP: ECP_0442
            ECV: APECO1_1625(phoA)
            ECW: EcE24377A_0410(phoA)
            ECX: EcHS_A0451
            YPE: YPO2298(phoA)
            YPK: y2130(phoA)
            YPM: YP_2083(phoA)
            YPA: YPA_1647
            YPN: YPN_1759
            YPP: YPDSF_0845
            YPS: YPTB2220(phoA)
            YPI: YpsIP31758_1835
            SFL: SF0230(phoA)
            SFX: S0252(phoA)
            SFV: SFV_0346(phoA)
            SSN: SSON_0358(phoA) SSON_0443(ybaA)
            SBO: SBO_0278(phoA)
            ECA: ECA4130
            PLU: plu4256(phoA)
            ENT: Ent638_0854
            SPE: Spro_0139 Spro_1272 Spro_1528 Spro_1881 Spro_1932 Spro_2233
                 Spro_2700 Spro_3766
            ASU: Asuc_1796
            XFA: XF0657
            XFT: PD1515(phoA)
            XCC: XCC2597(phoA)
            XCB: XC_1519
            XCV: XCV2913(phoA) XCV4265(phoD1) XCV4266(phoD2)
            XAC: XAC2759(phoA)
            XOO: XOO3296(phoA)
            XOM: XOO_3119(XOO3119)
            VPA: VPA1073
            PPR: PBPRB0359(csaP)
            PAE: PA3296(phoA)
            PAU: PA14_21410(phoA)
            PPF: Pput_0920
            PSP: PSPPH_0910(phoD) PSPPH_4180
            PMY: Pmen_0747 Pmen_0840
            PRW: PsycPRwf_0022 PsycPRwf_0328 PsycPRwf_2335
            SON: SO_0830
            SDN: Sden_2976 Sden_3287
            SFR: Sfri_0541 Sfri_2542 Sfri_2543
            SAZ: Sama_0502
            SBL: Sbal_3691 Sbal_3692
            SBM: Shew185_0664 Shew185_0665 Shew185_1174 Shew185_1551
                 Shew185_2905 Shew185_2992 Shew185_3654
            SLO: Shew_1157 Shew_1158 Shew_3226
            SSE: Ssed_0910 Ssed_1105 Ssed_1250 Ssed_3034 Ssed_3117
            SPL: Spea_0598 Spea_0820 Spea_1144 Spea_1145 Spea_1319 Spea_1393
            SHE: Shewmr4_0688 Shewmr4_3369 Shewmr4_3370
            SHM: Shewmr7_0583 Shewmr7_0584 Shewmr7_3334
            SHN: Shewana3_3446 Shewana3_3482 Shewana3_3539
            ILO: IL2011(phoA)
            CPS: CPS_1963 CPS_3933
            PHA: PSHAa1860(phoD) PSHAa2976 PSHAa2977 PSHAb0500
            PAT: Patl_1216
            SDE: Sde_0655
            PIN: Ping_3408 Ping_3409
            MCA: MCA2187
            AEH: Mlg_1869
            MMW: Mmwyl1_1506 Mmwyl1_4405
            AHA: AHA_2791 AHA_2792
            DNO: DNO_0105
            CVI: CV_1513(phoA2) CV_1514(phoA1)
            RSO: RSc0097(RS02267) RSc0098(RS02280)
            REH: H16_A2182 H16_A2183 H16_B0842(phoD)
            RME: Rmet_4084 Rmet_4085
            BMA: BMA0106
            BUR: Bcep18194_B2852 Bcep18194_B2853
            BPS: BPSL0360 BPSL0361
            BPM: BURPS1710b_0567 BURPS1710b_0568(phoA2)
            BTE: BTH_I0332 BTH_I0333
            EBA: ebA362
            AZO: azo3855
            DAR: Daro_3229
            MFA: Mfla_0451 Mfla_1206
            GUR: Gura_2162 Gura_2889
            PCA: Pcar_0512
            PPD: Ppro_1376
            DDE: Dde_1216
            BBA: Bd3653(ybaA)
            ADE: Adeh_0981 Adeh_0982
            AFW: Anae109_1656
            PLA: Plav_0979 Plav_3044
            SMD: Smed_4686
            RET: RHE_CH01592 RHE_CH04099(phoA)
            RLE: RL1341 RL1693 RL3386 RL4713
            BME: BMEI0790 BMEII0655
            BMF: BAB1_1222
            BMS: BR1200(phoA)
            BMB: BruAb1_1205(phoA)
            BOV: BOV_1163(phoA)
            OAN: Oant_1583 Oant_3542 Oant_3600
            BJA: blr0534
            RPA: RPA0391 RPA4514
            RPB: RPB_0089
            RPC: RPC_0030
            RPD: RPD_0714
            RPE: RPE_0033 RPE_3453
            CCR: CC_0455
            RSQ: Rsph17025_2889
            MMR: Mmar10_2404
            HNE: HNE_1260(phoD1) HNE_3483 HNE_3501(phoD2)
            ZMO: ZMO0938(phoD)
            SWI: Swit_0078 Swit_0541 Swit_3735
            ELI: ELI_11965
            GOX: GOX0675
            ACR: Acry_1634
            RRU: Rru_A1289
            BSU: BG10183(phoA) BG10697(phoB)
            BHA: BH0874
            BAN: BA3001 BA4574
            BAR: GBAA3001 GBAA4574
            BAA: BA_3509 BA_5016
            BAT: BAS2789 BAS4244
            BCE: BC2986 BC4343
            BCA: BCE_3038 BCE_4427
            BCZ: BCZK2719(phoB) BCZK4093
            BCY: Bcer98_0531 Bcer98_1737 Bcer98_3069 Bcer98_3465
            BTK: BT9727_2738(phoB) BT9727_4082
            BTL: BALH_3935
            BLI: BL01381(phoB)
            BLD: BLi02565(phoB)
            BCL: ABC0731 ABC3952(phoB)
            BAY: RBAM_009670
            BPU: BPUM_0641 BPUM_0896
            OIH: OB1029 OB2407
            GKA: GK2701
            SAU: SA2420(phoB)
            SAV: SAV2627(phoB)
            SAM: MW2547(phoB)
            SAS: SAS2513
            SAC: SACOL2648
            SAB: SAB2386 SAB2502(phoB)
            SAA: SAUSA300_2561(phoB)
            SAO: SAOUHSC_02958
            SAJ: SaurJH9_0750 SaurJH9_2650
            SAH: SaurJH1_0767 SaurJH1_2706
            SEP: SE2197
            SER: SERP2208
            SHA: SH0401(phoB)
            SSP: SSP0592
            LLC: LACR_0747
            LLM: llmg_1854(apl)
            LSL: LSL_1322
            LRE: Lreu_0277
            EFA: EF2973(phoZ)
            CTC: CTC00659
            CBE: Cbei_2122
            DSY: DSY4404
            CSC: Csac_2767
            MSM: MSMEG_1012
            MVA: Mvan_3577
            CGL: NCgl2185(cgl2265) NCgl2371(cgl2457)
            CGB: cg2485(phoD) cg2700(phoB)
            CEF: CE1217
            NFA: nfa36460
            SCO: SCO0828(SCF43A.18)
            SMA: SAV6139(phoD1)
            ART: Arth_4197 Arth_4297 Arth_4466
            KRA: Krad_0138 Krad_0180 Krad_1784 Krad_4547
            STP: Strop_0765 Strop_2394
            RXY: Rxyl_0447
            RBA: RB1934 RB3532 RB5778(phoA) RB5813(phoD) RB88(phoD)
                 RB8889(phoD)
            LIL: LA4246
            LIC: LIC13397(phoD)
            SYW: SYNW0196
            SYX: SynWH7803_1802(phoD)
            CYA: CYA_0781 CYA_2506(phoD)
            CYB: CYB_0684(phoD) CYB_1198
            GVI: gll0363 gll0567
            PMB: A9601_18341(dedA)
            PMC: P9515_18131(dedA)
            PMF: P9303_01771(dedA)
            PMG: P9301_18161(dedA)
            PME: NATL1_11501 NATL1_20761(dedA)
            BTH: BT_3708
            BFR: BF0480
            BFS: BF0425
            PGI: PG0890
            SRU: SRU_0238 SRU_2450
            FJO: Fjoh_1420 Fjoh_1421 Fjoh_3187 Fjoh_3249 Fjoh_4878
            FPS: FP1761(pafA)
            CCH: Cag_0406 Cag_0787
            PLT: Plut_2085
            DRA: DR_B0046(phoB)
            DGE: Dgeo_2364
            TTH: TT_P0024
            TTJ: TTHB067
            TMA: TM0156
            TPT: Tpet_0770
            FNO: Fnod_0754
            MAE: Maeo_0541
            MAC: MA4354(phoA)
            MBA: Mbar_A1231
            MMA: MM_0572
            HAL: VNG6301G(aph)
            HMA: rrnAC0273(phoD)
            PAB: PAB2366(phoA)
            PFU: PF1004
STRUCTURES  PDB: 1AJA  1AJB  1AJC  1AJD  1ALH  1ALI  1ALJ  1ALK  1ANI  1ANJ  
                 1B8J  1ED8  1ED9  1ELX  1ELY  1ELZ  1EW2  1EW8  1EW9  1HJK  
                 1HQA  1K7H  1KH4  1KH5  1KH7  1KH9  1KHJ  1KHK  1KHL  1KHN  
                 1SHN  1SHQ  1URA  1URB  1Y6V  1Y7A  1ZEB  1ZED  1ZEF  2ANH  
                 2G9Y  2GA3  2GLQ  2IUC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.1
            ExPASy - ENZYME nomenclature database: 3.1.3.1
            ExplorEnz - The Enzyme Database: 3.1.3.1
            ERGO genome analysis and discovery system: 3.1.3.1
            BRENDA, the Enzyme Database: 3.1.3.1
            CAS: 9001-78-9
///
ENTRY       EC 3.1.3.2                  Enzyme
NAME        acid phosphatase;
            acid phosphomonoesterase;
            phosphomonoesterase;
            glycerophosphatase;
            acid monophosphatase;
            acid phosphohydrolase;
            acid phosphomonoester hydrolase;
            uteroferrin;
            acid nucleoside diphosphate phosphatase;
            orthophosphoric-monoester phosphohydrolase (acid optimum)
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     phosphate-monoester phosphohydrolase (acid optimum)
REACTION    a phosphate monoester + H2O = an alcohol + phosphate [RN:R00626]
ALL_REAC    R00626 > R00548 R03024
SUBSTRATE   phosphate monoester [CPD:C01153];
            H2O [CPD:C00001]
PRODUCT     alcohol [CPD:C00069];
            phosphate [CPD:C00009]
INHIBITOR   (R,R)-Tartaric acid [CPD:C00898]
COMMENT     Wide specificity. Also catalyses transphosphorylations.
REFERENCE   1
  AUTHORS   Joyce, B.K. and Grisolia, S.
  TITLE     Purification and properties of a nonspecific acid phosphatase from
            wheat germ.
  JOURNAL   J. Biol. Chem. 235 (1960) 2278-2281.
  ORGANISM  Triticum aestivum [GN:etae]
REFERENCE   2
  AUTHORS   Kuo, M.-H. and Blumenthal, H.J.
  TITLE     Purification and properties of an acid phosphomonoesterase from
            Neurospora crassa.
  JOURNAL   Biochim. Biophys. Acta 52 (1961) 13-29.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   3
  AUTHORS   Tsuboi, K.K., Wiener, G. and Hudson, P.B.
  TITLE     Acid phosphatase. VII. Yeast phosphomonoesterase; isolation
            procedure and stability characteristics.
  JOURNAL   J. Biol. Chem. 224 (1957) 621-635.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
            PATH: map00740  Riboflavin metabolism
            PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K01078  acid phosphatase
            KO: K03788  acid phosphatase (class B)
            KO: K09474  acid phosphatase (class A)
GENES       HSA: 51205(ACP6) 52(ACP1) 53(ACP2) 54(ACP5) 55(ACPP) 93650(ACPT)
            PTR: 451166(ACP2)
            MMU: 11431(Acp1) 11432(Acp2) 11433(Acp5) 56318(Acpp) 66659(Acp6)
            RNO: 24161(Acp1) 24162(Acp2) 25732(Acp5) 56780(Acpp)
            CFA: 475822(ACP6) 476705(ACP5) 484357(ACPT) 485662(ACPP)
                 606814(LOC606814)
            BTA: 280977(ACP1)
            SSC: 397414(UF)
            GGA: 418458(ACP6) 421909(RCJMB04_11a4) 428864(RCJMB04_28i17)
                 776390(ACPP)
            XLA: 444090(MGC83618) 496027(LOC496027)
            XTR: 448657(MGC89650)
            SPU: 579390(LOC579390) 579609(LOC579609) 591824(LOC591824)
                 756773(LOC756773)
            DME: Dmel_CG7899(Acph-1)
            CEL: B0361.7 C05C10.1 C05C10.4 F02E9.7 F26C11.1
            ATH: AT1G14700(ATPAP3/PAP3)
            SCE: YAR071W(PHO11) YBR092C(PHO3) YBR093C(PHO5) YDL024C(DIA3)
                 YHR215W(PHO12) YPR073C(LTP1)
            AGO: AGOS_ADL365W
            PIC: PICST_46121(PHO12) PICST_46975(PHO5) PICST_61096(PHO6)
                 PICST_83142(PHO3.3)
            CGR: CAGL0D01320g
            SPO: SPAC1071.12c(stp1) SPBC21H7.03c SPBC4.06 SPBC428.03c(pho4)
                 SPBP4G3.02(pho1)
            ANI: AN7142.2 AN8063.2 AN8389.2
            AFM: AFUA_1G00580 AFUA_1G03570 AFUA_1G16480 AFUA_2G03960
                 AFUA_2G09890 AFUA_3G14570 AFUA_4G03660 AFUA_5G01330
                 AFUA_5G01880 AFUA_6G11330 AFUA_7G00800 AFUA_8G01910
                 AFUA_8G04050
            AOR: AO090003001336 AO090005001062 AO090011000300 AO090701000505
            ANG: An13g01750(aphA)
            UMA: UM01812.1 UM01827.1 UM02069.1 UM06428.1
            DDI: DDBDRAFT_0189318 DDB_0229833(CF60)
            PFA: PFI0880c
            TAN: TA04960
            TPV: TP03_0512
            TET: TTHERM_00415620 TTHERM_00529800 TTHERM_00885820
                 TTHERM_00930840 TTHERM_00930850 TTHERM_00997700
                 TTHERM_01050660 TTHERM_01193550
            TCR: 503723.60
            EHI: 276.t00009 49.t00013
            ECO: b0980(appA) b4055(aphA)
            ECJ: JW0963(appA) JW4015(aphA)
            ECE: Z1397(appA) Z5654(aphA)
            ECS: ECs1136 ECs5037
            ECC: c1121(appA) c5045(aphA)
            ECI: UTI89_C1049(appA) UTI89_C4641(aphA)
            ECP: ECP_0985 ECP_4283
            ECV: APECO1_2401(aphA) APECO1_84(appA)
            ECW: EcE24377A_1096(appA) EcE24377A_4607(aphA)
            ECX: EcHS_A1089
            STY: STY4445(aphA) STY4519(phoN)
            STT: t4155(aphA) t4225(phoN)
            SPT: SPA4066(aphA) SPA4136(phoN)
            SEC: SC4128(aphA) SC4197(phoN)
            STM: STM4249(aphA) STM4319(phoN)
            YPE: YPO1648
            YPK: y1810(appA)
            YPM: YP_1778(appA)
            YPA: YPA_1875
            YPN: YPN_1982
            YPP: YPDSF_3002
            YPS: YPTB2421
            YPI: YpsIP31758_1622(appA)
            SFL: CP0190(phoN1) SF0982(appA) SF4149(aphA)
            SFX: S1048(appA) S3580(aphA)
            SFV: SFV_0989(appA) SFV_4158(aphA)
            SSN: SSON_0987(appA) SSON_4235(aphA) SSO_P004(phoN2)
            SBO: SBO_2250(appA) SBO_4084(aphA) SBO_P006(phoN2)
            SDY: SDY_0956(appA) SDY_P067(phoN1)
            ENT: Ent638_0259 Ent638_3215
            SPE: Spro_2722 Spro_4496
            HIT: NTHI0623(aphA)
            HIP: CGSHiEE_00525(aphA) CGSHiEE_08630(surE)
            HIQ: CGSHiGG_05725(aphA) CGSHiGG_06840(surE)
            ASU: Asuc_1410 Asuc_1571
            XCC: XCC0760(appA) XCC4135(lppC) XCC4236(phoC)
            XCB: XC_3473 XC_4227 XC_4326
            XCV: XCV0590(appA) XCV0864(appA) XCV4225 XCV4379 XCV4482(phoN)
            XAC: XAC0557(appA) XAC0812(appA) XAC4132(appA) XAC4277(lppC)
                 XAC4369(phoC)
            XOO: XOO0246(lppC) XOO3792(appA) XOO4633(phoC)
            XOM: XOO_0225(XOO0225) XOO_3574(XOO3574) XOO_4367(XOO4367)
            PSB: Psyr_4500
            PFL: PFL_0997
            PMY: Pmen_1617
            SFR: Sfri_1057
            SAZ: Sama_1041
            SBL: Sbal_3122
            SBM: Shew185_2294
            SLO: Shew_1210
            SPC: Sputcn32_2752
            SSE: Ssed_2311
            SPL: Spea_2253
            SHW: Sputw3181_1260
            PIN: Ping_0675
            MAQ: Maqu_0926
            LPN: lpg1119
            LPF: lpl1124(map)
            LPP: lpp1120(map)
            MCA: MCA2221(phoC)
            FTU: FTT0156
            FTF: FTF0156
            FTL: FTL_0031 FTL_1732
            FTH: FTH_0030 FTH_1671
            FTN: FTN_0022
            HHA: Hhal_1431
            MMW: Mmwyl1_3860
            AHA: AHA_0425(aphA)
            DNO: DNO_0959(surE)
            RMA: Rmag_0910
            VOK: COSY_0817(surE)
            CVI: CV_3525(acpA) CV_4286
            RSO: RSp1174(acpA)
            REU: Reut_B4538
            REH: H16_A0767(pgpB) H16_B1238
            RME: Rmet_4809
            BMA: BMA0886
            BMV: BMASAVP1_A1847(surE)
            BML: BMA10299_A0050(surE)
            BMN: BMA10247_1119(surE) BMA10247_3086(acpA)
            BXE: Bxe_B0169
            BVI: Bcep1808_1750
            BCH: Bcen2424_1823 Bcen2424_3354
            BAM: Bamb_5133
            BPS: BPSL2018
            BPM: BURPS1710b_1804 BURPS1710b_A2344(acpA)
            BPL: BURPS1106A_2239(surE) BURPS1106A_3966(acpA)
            BPD: BURPS668_2201(surE) BURPS668_3884(acpA)
            BTE: BTH_I2671(acpA)
            PNU: Pnuc_1299
            PNA: Pnap_2579
            AAV: Aave_1414
            AJS: Ajs_1160
            VEI: Veis_0090
            MPT: Mpe_A1252
            HAR: HEAR1254(surE)
            MMS: mma_2137(surE) mma_3474
            AZO: azo1087(surE)
            HPA: HPAG1_1228
            CJJ: CJJ81176_0317(surE)
            CJD: JJD26997_1670(surE)
            ABU: Abu_2263(surE)
            NIS: NIS_1318(surE)
            SUN: SUN_1306(surE) SUN_2383
            PPD: Ppro_2737
            DVL: Dvul_1090
            DPS: DP2365
            AFW: Anae109_1186
            MLO: mll2704
            RSH: Rsph17029_1205
            PDE: Pden_2731 Pden_4654
            ZMO: ZMO0130(phoC)
            SWI: Swit_0522
            GOX: GOX0994 GOX1076 GOX1624 GOX1940
            GBE: GbCGDNIH1_0469 GbCGDNIH1_1410 GbCGDNIH1_1412 GbCGDNIH1_1821
            ACR: Acry_0053 Acry_2003
            MGM: Mmc1_0373
            ABA: Acid345_1617 Acid345_2127
            BAN: BA4746
            BAR: GBAA4746
            BAA: BA_5177
            BAT: BAS4406
            BCE: BC4511
            BCA: BCE_4638
            BCZ: BCZK4258
            BCY: Bcer98_0393
            BTK: BT9727_4246
            BTL: BALH_4095
            SPY: SPy_1113
            SPZ: M5005_Spy_0835 M5005_Spy_0836 M5005_Spy_1600(lppC)
            SPM: spyM18_1074
            SPG: SpyM3_0773
            SPS: SPs0973
            SPH: MGAS10270_Spy0951 MGAS10270_Spy1671(lppC)
            SPI: MGAS10750_Spy0986 MGAS10750_Spy1658(lppC)
            SPJ: MGAS2096_Spy0910 MGAS2096_Spy1626(lppC)
            SPK: MGAS9429_Spy0954 MGAS9429_Spy1605(lppC)
            SPF: SpyM50953
            SPA: M6_Spy0834 M6_Spy1611
            SPB: M28_Spy0812 M28_Spy1592(lppC)
            SAG: SAG0635
            SAN: gbs0615
            SAK: SAK_0768
            CBO: CBO0233(surE)
            CBA: CLB_0274(surE)
            CBH: CLC_0289(surE)
            CBF: CLI_0298(surE)
            DRM: Dred_1760
            MTU: Rv3310
            MBO: Mb3338
            MBB: BCG_3375(sapM)
            MPA: MAP3432
            MSM: MSMEG_6820(surE)
            CJK: jk0010(acpA)
            FAL: FRAAL3218
            SYR: SynRCC307_0458(phoC)
            AVA: Ava_1170
            PMT: PMT1569(phoN)
            PMB: A9601_14701(surE)
            PMC: P9515_14321(surE)
            PMF: P9303_03461 P9303_19351(surE)
            PMG: P9301_14561(surE)
            PMH: P9215_14961(surE)
            PME: NATL1_16901(surE)
            TER: Tery_1774
            SRU: SRU_1440(lppC)
            FJO: Fjoh_1631
            CPH: Cpha266_2034
            PVI: Cvib_0420
            RRS: RoseRS_1819 RoseRS_2394 RoseRS_3252
            RCA: Rcas_2526 Rcas_3085 Rcas_3741
            TTH: TTC1252
            MMQ: MmarC5_0542
            MTP: Mthe_1272
            MEM: Memar_1385
            MBN: Mboo_0919
            RCI: RCIX2221(surE)
            PAI: PAE3523
            PIS: Pisl_0305 Pisl_0936
            PCL: Pcal_0353 Pcal_1981
            PAS: Pars_0988 Pars_1952
            TPE: Tpen_0142 Tpen_1004
STRUCTURES  PDB: 1BVH  1C0E  1CVI  1D2T  1DKL  1DKM  1DKN  1DKO  1DKP  1DKQ  
                 1EOI  1IW8  1KBP  1N8N  1N9K  1ND5  1ND6  1PNT  1QFC  1QHW  
                 1RMQ  1RMT  1RMY  1RPA  1RPT  1UTE  1WAR  1XWW  1XZW  1Z12  
                 1Z13  1Z5G  1Z5U  1Z88  2A96  2AKC  2AUT  2B82  2B8J  2BQ8  
                 2D1G  2G1A  2GLA  2GLB  2GLC  2HLK  2HLL  2HPA  2I33  2I34  
                 2IPB  2P4U  3KBP  4KBP  5PNT  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.2
            ExPASy - ENZYME nomenclature database: 3.1.3.2
            ExplorEnz - The Enzyme Database: 3.1.3.2
            ERGO genome analysis and discovery system: 3.1.3.2
            BRENDA, the Enzyme Database: 3.1.3.2
            CAS: 9001-77-8
///
ENTRY       EC 3.1.3.3                  Enzyme
NAME        phosphoserine phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     O-phosphoserine phosphohydrolase
REACTION    O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate
            [RN:R00582 R02853]
ALL_REAC    R00582 R02853
SUBSTRATE   O-phospho-L-serine [CPD:C01005];
            O-phospho-D-serine;
            H2O [CPD:C00001]
PRODUCT     L-serine [CPD:C00065];
            D-serine [CPD:C00740];
            phosphate [CPD:C00009]
REFERENCE   1  [PMID:13654276]
  AUTHORS   BORKENHAGEN LF, KENNEDY EP.
  TITLE     The enzymatic exchange of L-serine with O-phospho-L-serine catalyzed
            by a specific phosphatase.
  JOURNAL   J. Biol. Chem. 234 (1959) 849-53.
  ORGANISM  chicken [GN:gga], rat [GN:rno]
REFERENCE   2
  AUTHORS   Byrne, W.L.
  TITLE     Glucose-6-phosphatase and phosphoserine phosphatase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 5, Academic Press, New York, 1961, p. 73-78.
REFERENCE   3
  AUTHORS   Neuhaus, F.C. and Byrne, W.L.
  TITLE     Metabolism of phosphoserine. II. Purification and properties of
            O-phosphoserine phosphatase.
  JOURNAL   J. Biol. Chem. 234 (1959) 113-121.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K01079  phosphoserine phosphatase
            KO: K05518  negative regulator of sigma-B (phosphoserine
                        phosphatase)
GENES       HSA: 5723(PSPH)
            MMU: 100678(Psph)
            RNO: 304429(Psph)
            CFA: 489783(PSPH)
            XLA: 446328(psph)
            DME: Dmel_CG3705(aay)
            CME: CMI086C
            SCE: YGR208W(SER2)
            AGO: AGOS_ACL130C
            CGR: CAGL0K00825g
            SPO: SPBC3H7.07c
            AFM: AFUA_3G06550
            DDI: DDB_0230054(serB)
            ECO: b4388(serB)
            ECJ: JW4351(serB)
            ECE: Z5989(serB)
            ECS: ECs5346
            ECC: c5473(serB)
            ECI: UTI89_C2806(gcvR) UTI89_C4247(yidA) UTI89_C5159(serB)
            ECP: ECP_4772
            ECV: APECO1_1993(serB)
            ECW: EcE24377A_4987(serB)
            ECX: EcHS_A4623(serB)
            STY: STY4925(serB)
            STT: t4617(serB)
            SPT: SPA4388(serB)
            SEC: SC4423(serB)
            STM: STM4578(serB)
            YPE: YPO0442(serB)
            YPK: y3738(serB)
            YPM: YP_3740(serB3)
            YPA: YPA_3842
            YPN: YPN_0313
            YPP: YPDSF_3192
            YPS: YPTB0586(serB)
            YPI: YpsIP31758_3493(serB)
            SFL: SF4420(serB)
            SFX: S4691(serB)
            SFV: SFV_4422(serB)
            SSN: SSON_4538(serB)
            SBO: SBO_4451(serB)
            SDY: SDY_4649(serB)
            ECA: ECA0465(serB)
            PLU: plu0551(serB)
            SGL: SG0398
            ENT: Ent638_0547
            SPE: Spro_0666
            HIT: NTHI1192(serB)
            HIP: CGSHiEE_06895(serB)
            HIQ: CGSHiGG_08785(serB)
            HSO: HS_0687(serB)
            PMU: PM1657(serB)
            MSU: MS1758(serB)
            APL: APL_1230(serB)
            ASU: Asuc_2112
            VCH: VC2345
            VCO: VC0395_A1924(serB)
            VVU: VV1_1730
            VVY: VV2674
            VPA: VP2431
            VFI: VF0509
            PPR: PBPRA0635
            PAE: PA4960
            PAU: PA14_65560(serB)
            PAP: PSPA7_3550(thrH)
            PPU: PP_4909(serB)
            PPF: Pput_4785
            PST: PSPTO_4957
            PSB: Psyr_0557
            PSP: PSPPH_0550(serB) PSPPH_2050(thrH)
            PFL: PFL_0551
            PFO: Pfl_0506(serB)
            PEN: PSEEN4962(serB)
            PMY: Pmen_0618
            PAR: Psyc_1857(serB)
            PCR: Pcryo_2146
            PRW: PsycPRwf_2184
            ACI: ACIAD3567(serB)
            SON: SO_1223(serB)
            SDN: Sden_1032
            SFR: Sfri_1007
            SAZ: Sama_0978
            SBL: Sbal_3222
            SBM: Shew185_3223
            SLO: Shew_2810
            SPC: Sputcn32_2817
            SSE: Ssed_3373
            SPL: Spea_3043
            SHE: Shewmr4_1042
            SHM: Shewmr7_1107
            SHN: Shewana3_1046
            SHW: Sputw3181_1194
            ILO: IL1876(serB_2)
            CPS: CPS_1107(serB)
            PHA: PSHAa0661(serB)
            PAT: Patl_1278
            SDE: Sde_1075
            PIN: Ping_2446
            MAQ: Maqu_2786
            CBU: CBU_1730
            MCA: MCA1267(serB)
            FTH: FTH_1390
            FTN: FTN_0742(serB)
            TCX: Tcr_1620
            NOC: Noc_0206 Noc_2504
            AEH: Mlg_2041
            HHA: Hhal_1598
            HCH: HCH_02661(thrH) HCH_05403(serB)
            CSA: Csal_2542
            ABO: ABO_2442(serB)
            MMW: Mmwyl1_1310
            AHA: AHA_3685
            RMA: Rmag_0271
            VOK: COSY_0257(serB)
            NME: NMB0981
            NMA: NMA1179(serB)
            NMC: NMC0961(serB)
            NGO: NGO1468
            CVI: CV_3516(serB)
            RSO: RSc1640(serB)
            REU: Reut_A1357
            REH: H16_A1452(serB1) H16_A3080(serB2) H16_B1164(serB3)
            RME: Rmet_1368
            BMA: BMA0338 BMA1313(serB)
            BMV: BMASAVP1_A1802(serB)
            BML: BMA10299_A0094(serB)
            BMN: BMA10247_1073(serB)
            BXE: Bxe_A2331
            BVI: Bcep1808_1709
            BUR: Bcep18194_A5077
            BCN: Bcen_6301
            BCH: Bcen2424_1778
            BAM: Bamb_1718
            BPS: BPSL0834 BPSL1543
            BPM: BURPS1710b_1041 BURPS1710b_2322(serB)
            BPL: BURPS1106A_2194(serB)
            BPD: BURPS668_2157(serB)
            BTE: BTH_I0700 BTH_I2264
            PNU: Pnuc_0928
            BPE: BP0863(serB)
            BPA: BPP3368(serB)
            BBR: BB3819(serB)
            RFR: Rfer_1329
            POL: Bpro_2720
            PNA: Pnap_2554
            AAV: Aave_1576
            AJS: Ajs_3159
            VEI: Veis_4883
            MPT: Mpe_A1568
            HAR: HEAR1915
            MMS: mma_1407(serB)
            NEU: NE0439(serB)
            NET: Neut_0597
            NMU: Nmul_A0636
            EBA: ebA6034(serB)
            AZO: azo0501(hprK) azo1668(serB) azo3743(thrH)
            DAR: Daro_1962
            MFA: Mfla_1890
            HPY: HP0652(serB)
            HPA: HPAG1_0637
            HHE: HH0078(serB)
            HAC: Hac_0485(serB) Hac_1062(serB)
            WSU: WS2081(serB)
            TDN: Tmden_1665
            CJE: Cj0282c(serB)
            CJR: CJE0330(serB)
            CJJ: CJJ81176_0308(serB)
            CJU: C8J_0258(serB)
            CJD: JJD26997_1689(serB)
            CFF: CFF8240_0333(serB)
            CCV: CCV52592_1659(serB)
            CHA: CHAB381_1307(serB)
            CCO: CCC13826_1582(serB)
            ABU: Abu_0221(serB)
            NIS: NIS_1308
            SUN: SUN_0642
            PCA: Pcar_2283
            MXA: MXAN_1089(serB) MXAN_1530
            SAT: SYN_02182
            MLO: mlr1449
            MES: Meso_1744
            PLA: Plav_2462
            SME: SMc01494(serB)
            SMD: Smed_2012
            ATU: Atu2040(serB)
            ATC: AGR_C_3697(serB)
            RET: RHE_CH02794(serB)
            RLE: RL3250(serB)
            BME: BMEI0615
            BMF: BAB1_1410
            BMS: BR1391(serB)
            BMB: BruAb1_1387(serB)
            BOV: BOV_1348(serB)
            OAN: Oant_1800
            BJA: blr6505(serB)
            BRA: BRADO5568(serB)
            BBT: BBta_6089(serB)
            RPA: RPA2029(serB)
            RPB: RPB_3347
            RPC: RPC_3257
            RPD: RPD_2096
            RPE: RPE_2185
            NWI: Nwi_2345
            NHA: Nham_2724
            XAU: Xaut_1660
            CCR: CC_2097
            SIL: SPO2363(serB-1) SPO3353(serB-2)
            SIT: TM1040_3019
            RSP: RSP_1350(serB)
            RSH: Rsph17029_0018
            RSQ: Rsph17025_0008
            JAN: Jann_0252
            RDE: RD1_0195(serB)
            PDE: Pden_0812
            HNE: HNE_0453(serB)
            ZMO: ZMO1137(serB)
            NAR: Saro_2259
            SAL: Sala_1468
            SWI: Swit_0607
            ELI: ELI_05525
            GOX: GOX1085
            GBE: GbCGDNIH1_1483
            ACR: Acry_2835
            RRU: Rru_A0465
            MAG: amb3479
            ABA: Acid345_2803
            BSU: BG10736(rsbX)
            BHA: BH0530(rsbX)
            BLI: BL02209(rsbX)
            BLD: BLi00561(rsbX)
            BCL: ABC0817(rsbX)
            BPU: BPUM_0443(rsbU) BPUM_0447(rsbX)
            OIH: OB0631
            LMO: lmo0896(rsbX)
            LMF: LMOf2365_0915
            LIN: lin0895(rsbX)
            LWE: lwe0878(rsbX)
            LLA: L0085(serB)
            LLC: LACR_0621
            LLM: llmg_0567(serB)
            SPR: spr1033
            SAG: SAG0625(serB)
            SAN: gbs0605
            SAK: SAK_0710(serB)
            SMU: SMU.1269(serB)
            STC: str1519(serB)
            STL: stu1519(serB)
            SSA: SSA_0882(serB)
            SGO: SGO_0389 SGO_1430(serB)
            CPF: CPF_1375
            CPR: CPR_1188
            CTC: CTC00969 CTC01739
            CNO: NT01CX_0181
            CDF: CD0241
            DSY: DSY1404
            SWO: Swol_0642
            TTE: TTE2448(serB)
            MTU: Rv0505c(serB1) Rv2483c(plsC) Rv3042c(serB2)
            MTC: MT0526 MT3127(serB)
            MBO: Mb0517c(serB1) Mb2508c(plsC) Mb3068c(serB2)
            MBB: BCG_0548c(serB1) BCG_2501c(plsC) BCG_3066c(serB2)
            MLE: ML1727
            MPA: MAP3090c(serB2) MAP3997c(serB)
            MAV: MAV_3907(serB)
            MSM: MSMEG_0949 MSMEG_1041(serB) MSMEG_2321(serB)
            MVA: Mvan_2083
            MGI: Mflv_4276
            MMC: Mmcs_0674 Mmcs_1853 Mmcs_5506
            MKM: Mkms_1900 Mkms_5907
            MJL: Mjls_1834
            CGL: NCgl0294(cgl0299) NCgl0400(cgl0415) NCgl2436(cgl2522)
            CGB: cg0495 cg2779(serB)
            CEF: CE0434 CE2417
            CDI: DIP1863
            CJK: jk0483(serB)
            NFA: nfa42930(serB) nfa51730
            RHA: RHA1_ro02056 RHA1_ro05647 RHA1_ro06447(serB)
            SCO: SCO1808(SCI28.02)
            SMA: SAV6470(serB2)
            LXX: Lxx11750(serB)
            CMI: CMM_0549(serB1)
            ART: Arth_2123
            AAU: AAur_2124(serB)
            PAC: PPA2051
            NCA: Noca_2574
            TFU: Tfu_0136
            FRA: Francci3_0481
            FAL: FRAAL0979(serB)
            KRA: Krad_2903
            SEN: SACE_1188(serB) SACE_6952(serB)
            BLO: BL1792(serB)
            BAD: BAD_0545(serB)
            FNU: FN0091 FN0892
            RBA: RB8037(serB)
            LIL: LA2145(serB)
            LIC: LIC11775(serB)
            LBJ: LBJ_1868(serB)
            LBL: LBL_1416(serB)
            AVA: Ava_0278 Ava_3723
            BTH: BT_0832
            BFR: BF2300
            BFS: BF2389
            PGI: PG0653(serB)
            FJO: Fjoh_1712
            CTE: CT0173(serB)
            CCH: Cag_0409(serB)
            CPH: Cpha266_0250
            PVI: Cvib_1591
            PLT: Plut_1948(serB)
            MMP: MMP0541(serB)
            MMQ: MmarC5_1066
            MMZ: MmarC7_1560
            MAE: Maeo_1052
            MVN: Mevan_1695
            MAC: MA0678 MA4428 MA4429(serB)
            MBA: Mbar_A1093 Mbar_A1094
            MMA: MM_1106 MM_1107 MM_1833
            MBU: Mbur_0935 Mbur_0936
            MHU: Mhun_0943
            MST: Msp_1096
            MSI: Msm_0719
            MKA: MK0121(serB)
            AFU: AF2138(serB)
            HAL: VNG2423G(serB)
            HMA: pNG7333(serB2) rrnAC1820 rrnAC2717(serB1)
            HWA: HQ1044A(serB)
            NPH: NP0274A(serB) NP4058A
            TAC: Ta0936
            TVO: TVN1082
            PTO: PTO0700 PTO0776 PTO1365
            PAB: PAB1207(serB)
            PFU: PF1921
            TKO: TK0052
            RCI: RCIX1733(serB-1) RCIX1735(serB-2)
            APE: APE_0683
            PAI: PAE2017(serB)
STRUCTURES  PDB: 1F5S  1J97  1L7M  1L7N  1L7O  1L7P  1L8L  1L8O  1NNL  2J6Y  
                 2J6Z  2J70  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.3
            ExPASy - ENZYME nomenclature database: 3.1.3.3
            ExplorEnz - The Enzyme Database: 3.1.3.3
            ERGO genome analysis and discovery system: 3.1.3.3
            BRENDA, the Enzyme Database: 3.1.3.3
            CAS: 9025-73-4
///
ENTRY       EC 3.1.3.4                  Enzyme
NAME        phosphatidate phosphatase;
            phosphatic acid phosphatase;
            acid phosphatidyl phosphatase;
            phosphatic acid phosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     3-sn-phosphatidate phosphohydrolase
REACTION    a 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
            [RN:R02239]
ALL_REAC    R02239;
            (other) R04162 R06520 R06521 R06522
SUBSTRATE   3-sn-phosphatidate [CPD:C00416];
            H2O [CPD:C00001]
PRODUCT     1,2-diacyl-sn-glycerol [CPD:C00641];
            phosphate [CPD:C00009]
REFERENCE   1
  AUTHORS   Smith, S.W., Weiss, S.B. and Kennedy, E.P.
  TITLE     The enzymatic dephosphorylation of phosphatidic acids.
  JOURNAL   J. Biol. Chem. 228 (1957) 915-922.
  ORGANISM  rat [GN:rno], guinea pig
PATHWAY     PATH: map00561  Glycerolipid metabolism
            PATH: map00564  Glycerophospholipid metabolism
            PATH: map00565  Ether lipid metabolism
            PATH: map00600  Sphingolipid metabolism
ORTHOLOGY   KO: K01080  phosphatidate phosphatase
GENES       HSA: 8611(PPAP2A) 8612(PPAP2C) 8613(PPAP2B)
            PTR: 461869(PPAP2A)
            MMU: 19012(Ppap2a) 50784(Ppap2c) 67916(Ppap2b)
            RNO: 192270(Ppap2b) 246115(Ppap2c) 64369(Ppap2a)
            CFA: 479557(PPAP2B) 607962(PPAP2A) 612442(PPAP2C)
            GGA: 424666(PPAP2B) 427138(PPAP2A)
            XLA: 444206(MGC80748)
            XTR: 394722(ppap2c) 496488(ppap2a)
            SPU: 576030(LOC576030)
            DME: Dmel_CG32491(mod(mdg4)) Dmel_CG8804(wun) Dmel_CG8805(wun2)
            TBR: Tb10.389.0020 Tb10.61.2970
            TCR: 511277.370
            FTW: FTW_0252
            FTL: FTL_1728
            FTH: FTH_1667
            BPU: BPUM_1658
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.4
            ExPASy - ENZYME nomenclature database: 3.1.3.4
            ExplorEnz - The Enzyme Database: 3.1.3.4
            ERGO genome analysis and discovery system: 3.1.3.4
            BRENDA, the Enzyme Database: 3.1.3.4
            CAS: 9025-77-8
///
ENTRY       EC 3.1.3.5                  Enzyme
NAME        5'-nucleotidase;
            uridine 5'-nucleotidase;
            5'-adenylic phosphatase;
            adenosine 5'-phosphatase;
            AMP phosphatase;
            adenosine monophosphatase;
            5'-mononucleotidase;
            AMPase;
            UMPase;
            snake venom 5'-nucleotidase;
            thimidine monophosphate nucleotidase;
            5'-AMPase;
            5'-AMP nucleotidase;
            AMP phosphohydrolase;
            IMP 5'-nucleotidase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     5'-ribonucleotide phosphohydrolase
REACTION    a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R07297]
ALL_REAC    R07297 > R00183 R00511 R00963 R01126 R01227 R02323 R02719 R03346;
            (other) R01569 R01664 R01968 R02088
SUBSTRATE   5'-ribonucleotide [CPD:C02520];
            H2O [CPD:C00001]
PRODUCT     ribonucleoside [CPD:C00911];
            phosphate [CPD:C00009]
COMMENT     Wide specificity for 5'-nucleotides.
REFERENCE   1
  AUTHORS   Gulland, J.M. and Jackson, E.M.
  TITLE     5-Nucleotidase.
  JOURNAL   Biochem. J. 32 (1938) 597-601.
  ORGANISM  rat [GN:rno], rabbit, frog, cow [GN:bta]
REFERENCE   2  [PMID:14824154]
  AUTHORS   HEPPEL LA, HILMORE RJ.
  TITLE     Purification and properties of 5-nucleotidase.
  JOURNAL   J. Biol. Chem. 188 (1951) 665-76.
  ORGANISM  cow [GN:bta], Crotalus adamanteus
REFERENCE   3
  AUTHORS   Segal, H.L. and Brenner, B.M.
  TITLE     5'-Nucleotidase of rat liver microsomes.
  JOURNAL   J. Biol. Chem. 235 (1960) 471-474.
  ORGANISM  rat [GN:rno], cow [GN:bta]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
            PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K01081  5'-nucleotidase
            KO: K03787  5'-nucleotidase
            KO: K08722  5'-nucleotidase
            KO: K08723  5'-nucleotidase
GENES       HSA: 30833(NT5C) 4907(NT5E) 51251(NT5C3) 56953(NT5M) 84618(NT5C1A)
                 93034(NT5C1B)
            PTR: 450706(NT5C2) 462864(NT5E) 469289(NT5C1A) 470316(NT5C1B)
            MCC: 700964(NT5C)
            MMU: 107569(Nt5c3) 230718(Nt5c1a) 23959(Nt5e) 70881(Nt5c1b)
                 76952(Nt5c2)
            RNO: 313574(Nt5c1a_predicted) 58813(Nt5e)
            CFA: 474984(NT5E) 475277(NT5C3) 609545(NT5M)
            BTA: 281363(NT5E) 281951(NT5C2)
            GGA: 395080(NT5C3) 416505(NT5M) 419675(NT5C1A) 421833(NT5E)
                 421954(NT5C1B) 423871(RCJMB04_22h21)
            XLA: 444729(MGC84715) 494724(LOC494724)
            XTR: 448172(nt5m)
            DRE: 321720(zgc:66117) 324845(nt5c2) 393906(nt5e)
                 554883(LOC554883)
            SPU: 576495(LOC576495) 584571(LOC584571)
            DME: Dmel_CG30104
            OSA: 4327823 4342678
            PIC: PICST_32593(PHO3) PICST_47650(PHO3.2)
            CAL: CaO19.4424
            ANI: AN5939.2
            TET: TTHERM_00105640
            ECO: b0480(ushA) b2291(yfbR) b2744(surE) b4374(yjjG)
            ECJ: JW0469(ushA) JW2288(yfbR) JW2714(surE) JW4336(yjjG)
            ECE: Z0599(ushA) Z3552 Z4052(surE) Z5975(yjjG)
            ECS: ECs0533 ECs3175 ECs3598 ECs5332
            ECC: c0600(ushA) c2832(yfbR) c3311(surE) c5454(yjjG)
            ECI: UTI89_C0508(ushA) UTI89_C2573(yfbR) UTI89_C3115(surE)
                 UTI89_C5083(yjjG)
            ECP: ECP_0541 ECP_2330 ECP_2726 ECP_4154 ECP_4757
            ECV: APECO1_1535(ushA) APECO1_20522(yjjG) APECO1_2526
                 APECO1_3779(surE) APECO1_4273(yfbR)
            ECW: EcE24377A_0519(ushA) EcE24377A_2584(yfbR)
                 EcE24377A_3045(surE) EcE24377A_4970(yjjG)
            ECX: EcHS_A0557(ushA) EcHS_A2440(yfbR) EcHS_A2882(surE)
                 EcHS_A4608(yjjG)
            STY: STY2562 STY3052(surE) STY4909
            STT: t0532 t2828(surE) t4602
            SPT: SPA0532 SPA2228(ushA) SPA2783(surE) SPA4373(yjjG)
            SEC: SC0536(ushA) SC2333(yfbR) SC2859(surE) SC4407(yjjG)
            STM: STM0494(ushA) STM2332 STM2927(surE) STM4559.S(yjjG)
            YPE: YPO2559 YPO3358(surE)
            YPK: y0831(surE) y1627
            YPM: YP_0329(surE) YP_2370
            YPA: YPA_2050 YPA_2785
            YPN: YPN_0735 YPN_2153
            YPS: YPTB0773(surE) YPTB2590
            YPI: YpsIP31758_1449(yfbR) YpsIP31758_3032(ushA)
                 YpsIP31758_3296(surE)
            SFL: SF0425(ushA) SF2367 SF2767(surE) SF4405(yjjG)
            SFX: S0432(ushA) S2502 S2960(surE) S4677(yjjG)
            SFV: SFV_2358 SFV_2754(surE) SFV_4408(yjjG)
            SSN: SSON_0469(ushA) SSON_2348 SSON_2892(surE) SSON_4524(yjjG)
            SBO: SBO_0382(ushA) SBO_2776(surE) SBO_4435(yjjG)
            SDY: SDY_0438(ushA) SDY_2487 SDY_2943(surE) SDY_4633(yjjG)
            ECA: ECA1184(ushA) ECA3034
            PLU: plu0716(surE) plu3092 plu3828(ushA)
            WBR: WGLp307(surE)
            SGL: SG0528 SG1603
            SPE: Spro_3311
            HIN: HI0702(surE)
            HIT: NTHI0303(nadN) NTHI0825(surE)
            HDU: HD0758(surE)
            HSO: HS_1500(surE)
            PMU: PM1193 PM1612(surE)
            MSU: MS1658(ushA) MS2272(surE)
            APL: APL_0769(ushA) APL_1927(surE)
            XFA: XF0858(surE) XF2089
            XFT: PD0787(ushA) PD1817(surE)
            XCC: XCC1547 XCC1706(surE)
            XCB: XC_2525 XC_2687
            XCV: XCV1637 XCV1758(surE)
            XAC: XAC1596 XAC1725(surE)
            XOO: XOO2434 XOO2956(surE) XOO4323
            XOM: XOO_2311(XOO2311) XOO_2808(XOO2808) XOO_4073(XOO4073)
            VCH: VC0531(surE) VC2174 VCA0545
            VCO: VC0395_A1751(ushA)
            VVU: VV1_0248 VV1_1585 VV2_0237
            VVY: VV0936 VV2812(surE) VVA0742
            VPA: VP0748 VP1207 VP2556(surE) VPA0855
            VFI: VF0778 VF2070 VFA0396
            PPR: PBPRA2836 PBPRA3074 PBPRB0897 PBPRB1892
            PAE: PA3625(surE)
            PAU: PA14_17450(surE)
            PAP: PSPA7_1514(surE)
            PPU: PP_1414(ushA) PP_1620(surE) PP_2531
            PPF: Pput_3189
            PST: PSPTO_1562(surE) PSPTO_2277 PSPTO_3043
            PSB: Psyr_1371(surE) Psyr_2075
            PSP: PSPPH_2046 PSPPH_3812(surE)
            PFL: PFL_0994 PFL_1204(surE) PFL_4270
            PFO: Pfl_1129(surE) Pfl_4005
            PEN: PSEEN1936 PSEEN4192(surE)
            PMY: Pmen_2548
            PCR: Pcryo_0660 Pcryo_2257
            PRW: PsycPRwf_2135
            ACI: ACIAD0015 ACIAD1227(surE)
            SON: SO_2001(ushA) SO_3317 SO_3435(surE)
            SDN: Sden_1201 Sden_1252 Sden_1994 Sden_2137
            SFR: Sfri_2309
            SAZ: Sama_2021
            SBM: Shew185_2135
            SLO: Shew_1285 Shew_2135
            SPC: Sputcn32_2311
            SSE: Ssed_2345
            SPL: Spea_1300 Spea_2047
            SHE: Shewmr4_1120 Shewmr4_2264
            SHM: Shewmr7_1191 Shewmr7_2336
            SHN: Shewana3_1121 Shewana3_1224 Shewana3_2454
            SHW: Sputw3181_1697
            ILO: IL0749(surE) IL1668(ushA)
            CPS: CPS_1075(surE)
            PHA: PSHAa0687(surE) PSHAb0345(ushA)
            PAT: Patl_3860
            SDE: Sde_1665
            MAQ: Maqu_0357
            CBU: CBU_1233 CBU_1671(surE)
            CBD: COXBU7E912_0329(surE)
            LPN: lpg1282(surE) lpg2677
            LPF: lpl1245(surE) lpl2604
            LPP: lpp1245(surE) lpp2731
            MCA: MCA0448 MCA1322 MCA2418(surE)
            FTA: FTA_1509
            TCX: Tcr_1257
            NOC: Noc_0789 Noc_1810
            AEH: Mlg_1829
            HCH: HCH_00409 HCH_01872(surE) HCH_02315
            CSA: Csal_2635
            ABO: ABO_1438
            MMW: Mmwyl1_2729
            AHA: AHA_0826(surE) AHA_1916 AHA_2008 AHA_3155
            NME: NMB1484(surE)
            NMA: NMA1693(surE)
            NGO: NGO1058(surE)
            CVI: CV_1743(ushA) CV_3083 CV_3679(surE)
            RSO: RSc1204(surE)
            REU: Reut_A2098(surE)
            REH: H16_A2376(surE)
            RME: Rmet_2118 Rmet_4019
            BMA: BMA1357(surE)
            BXE: Bxe_A2353
            BUR: Bcep18194_A5124 Bcep18194_B2902
            BCN: Bcen_4813 Bcen_6256
            BAM: Bamb_1761
            BPS: BPSL1502(surE)
            BPM: BURPS1710b_2368(surE)
            BTE: BTH_I2223(surE)
            BPE: BP0294 BP1719(surE)
            BPA: BPP0431 BPP3057(surE)
            BBR: BB0433 BB3020(surE)
            RFR: Rfer_0734 Rfer_2782
            POL: Bpro_0738 Bpro_3061
            AAV: Aave_4022
            AJS: Ajs_0692
            HAR: HEAR0649 HEAR1476
            MMS: mma_0612(ushA)
            NEU: NE0950(surE)
            NET: Neut_2324
            NMU: Nmul_A0495(surE)
            EBA: ebA782(surE)
            AZO: azo1483
            DAR: Daro_2524(surE)
            TBD: Tbd_0356 Tbd_0835(surE)
            MFA: Mfla_1824
            HPY: HP0930(surE)
            HPJ: jhp0865(surE)
            HPA: HPAG1_0911
            HHE: HH0335(surE)
            HAC: Hac_1085(surE)
            WSU: WS1678(surE)
            TDN: Tmden_1536
            CJE: Cj0293(surE)
            CJR: CJE0339(surE)
            CJU: C8J_0270(surE)
            CFF: CFF8240_0325(surE)
            CCV: CCV52592_1650(surE)
            CHA: CHAB381_1313(surE)
            CCO: CCC13826_0495 CCC13826_1575(surE)
            ABU: Abu_0572(soxB)
            GSU: GSU1523(surE)
            GME: Gmet_1419(surE)
            GUR: Gura_2619
            PCA: Pcar_1426(surE)
            DVU: DVU2142(surE)
            DDE: Dde_0789 Dde_2340(surE)
            LIP: LI0762(surE) LI1171
            DPS: DP1354
            ADE: Adeh_0753
            AFW: Anae109_0790 Anae109_1969
            MXA: MXAN_2236 MXAN_4450(surE)
            SAT: SYN_01984 SYN_02264
            SFU: Sfum_1169 Sfum_2979
            WOL: WD1077(surE)
            WBM: Wbm0549
            AMA: AM451(surE)
            APH: APH_0524(surE)
            ERU: Erum3050(surE)
            ERW: ERWE_CDS_03100(surE)
            ERG: ERGA_CDS_03050(surE)
            ECN: Ecaj_0285(surE)
            ECH: ECH_0791(surE)
            NSE: NSE_0374(surE)
            MLO: mll1080(surE) mlr3017
            MES: Meso_1802 Meso_2725
            PLA: Plav_3031
            SME: SMc02063(surE) SMc04018
            SMD: Smed_1168
            ATU: Atu1702(surE) Atu3770
            ATC: AGR_C_3128 AGR_L_2132
            RET: RHE_CH01827(surE) RHE_CH03555(ypch01255)
            RLE: RL2050(surE) RL4075
            BME: BMEI1081(surE)
            BMF: BAB1_0905(surE)
            BMS: BR0886(surE)
            BMB: BruAb1_0898(surE)
            BOV: BOV_0877(surE)
            OAN: Oant_2341
            BJA: bll2654 bll4746(surE)
            BRA: BRADO2166 BRADO4042(surE) BRADO6851
            BBT: BBta_0692 BBta_2482 BBta_4412(surE)
            RPA: RPA0955 RPA2841(surE)
            RPB: RPB_2739(surE) RPB_4457
            RPC: RPC_1152 RPC_2519
            RPD: RPD_2784 RPD_4302
            RPE: RPE_1070 RPE_2703
            NWI: Nwi_1775(surE)
            NHA: Nham_1792
            XAU: Xaut_4403
            CCR: CC_1998(surE)
            SIL: SPO2688(surE) SPO2904
            SIT: TM1040_1548 TM1040_1791
            RSP: RSP_0955 RSP_2545(surE)
            JAN: Jann_1068 Jann_2961
            RDE: RD1_1960 RD1_3249(surE) RD1_3959
            MMR: Mmar10_1904
            HNE: HNE_0420 HNE_1929(surE)
            ZMO: ZMO0985
            NAR: Saro_0559
            SAL: Sala_0721
            SWI: Swit_0638
            ELI: ELI_00605
            RRU: Rru_A1769 Rru_A2483
            MAG: amb2520
            BSU: BG12930(yfkN)
            BAN: BA3162 BA4322
            BAR: GBAA3162 GBAA4322
            BAA: BA_0082 BA_4779
            BAT: BAS2939 BAS4009 BAS4844
            BCE: BC3121 BC4100 BC4977
            BCA: BCE_3157 BCE_4169 BCE_5113
            BCZ: BCZK2864(ushA) BCZK3393 BCZK3856 BCZK3878(ushA) BCZK4702
            BTK: BT9727_2913(ushA) BT9727_3842 BT9727_4686
            BTL: BALH_2824(ushA) BALH_4508(ushA)
            BLI: BL03110
            BLD: BLi00814(yfkN)
            BCL: ABC1445 ABC2957
            GKA: GK1763
            SAB: SAB0023
            LLC: LACR_1194
            LLM: llmg_0192 llmg_1479(nucA)
            SPZ: M5005_Spy_0678
            SPH: MGAS10270_Spy0736
            SPI: MGAS10750_Spy0770
            SPJ: MGAS2096_Spy0749
            SPK: MGAS9429_Spy0733
            SPF: SpyM51130
            SPA: M6_Spy0695
            SPB: M28_Spy0658
            SGO: SGO_1247
            LDB: Ldb1363 Ldb1591
            LBR: LVIS_0040
            STH: STH1714
            CTC: CTC00147
            CBE: Cbei_1007
            CKL: CKL_0997(surE)
            AMT: Amet_2636
            CHY: CHY_0957(surE)
            DSY: DSY1823
            SWO: Swol_1150
            TTE: TTE1338(surE)
            MTA: Moth_1144(surE)
            MPU: MYPU_0550
            MMO: MMOB0990(ushA)
            MHY: mhp651(ushA)
            MHJ: MHJ_0631
            MHP: MHP7448_0630
            MSM: MSMEG_4308
            CGL: NCgl0021(cgl0022)
            CGB: cg0397
            CJK: jk1044
            RHA: RHA1_ro04127
            SCO: SCO4152(SCD84.19)
            SMA: SAV4057
            FAL: FRAAL0277(surE)
            SEN: SACE_4720
            RXY: Rxyl_0306 Rxyl_2311
            RBA: RB10258(surE) RB9952(surE)
            CTR: CT218(surE)
            CTA: CTA_0238(surE)
            CMU: TC0491(surE)
            CPN: CPn0262(surE)
            CPA: CP0499(surE)
            CPJ: CPj0262(surE)
            CPT: CpB0269(surE)
            CCA: CCA00519 CCA00520
            CAB: CAB506
            CFE: CF0488(surE)
            PCU: pc0864(surE)
            TPA: TP0104 TP0419(surE)
            LIL: LA3874(surE)
            LIC: LIC13094(surE)
            LBJ: LBJ_2481(surE)
            LBL: LBL_0610(surE)
            SYN: sll1108(surE) sll1459
            SYW: SYNW1601(surE)
            SYC: syc2030_d(surE)
            SYF: Synpcc7942_2063
            SYD: Syncc9605_0899
            SYE: Syncc9902_1499
            SYG: sync_0795(surE)
            SYR: SynRCC307_1740(surE)
            SYX: SynWH7803_1713(surE)
            CYA: CYA_0017(surE-1) CYA_0967(surE-2)
            CYB: CYB_0884(surE-1) CYB_1427(surE-2)
            TEL: tll1786 tlr1272
            GVI: gll0444
            ANA: alr3139 alr4846
            AVA: Ava_2116(surE) Ava_3836(surE) Ava_3996
            PMA: Pro1345(surE)
            PMM: PMM1271(surE)
            PMT: PMT0366(surE)
            PMN: PMN2A_0837(surE)
            PMI: PMT9312_1365
            PMB: A9601_14701(surE)
            PMC: P9515_14321(surE)
            PMF: P9303_19351(surE)
            PMG: P9301_14561(surE)
            PMH: P9215_14961(surE)
            PME: NATL1_16901(surE)
            TER: Tery_2384 Tery_3481
            BTH: BT_4003(surE)
            BFR: BF0770(surE)
            BFS: BF0698(surE)
            PGI: PG2163(surE)
            SRU: SRU_1842(surE)
            CHU: CHU_0932(surE)
            GFO: GFO_0643 GFO_0644 GFO_1276(ushA) GFO_1279 GFO_1282(ushA)
                 GFO_2964(surE)
            FJO: Fjoh_1429
            FPS: FP1833 FP2332(surE)
            CTE: CT1557(surE)
            CCH: Cag_0291(surE) Cag_1927
            PLT: Plut_0361(surE)
            DET: DET0797(surE)
            DEH: cbdb_A776(surE)
            DEB: DehaBAV1_0723
            DRA: DR_0505 DR_2397(surE) DR_A0018
            DGE: Dgeo_0040 Dgeo_2368 Dgeo_2751
            TTH: TTC0964 TTC1625(surE) TT_P0028(surE)
            TTJ: TTHA0360 TTHA1328 TTHB070
            AAE: aq_832(surE)
            TMA: TM1662(surE) TM1878
            TPT: Tpet_1129
            TME: Tmel_0836
            FNO: Fnod_0953
            MJA: MJ0559(surE)
            MMP: MMP1051(surE)
            MMZ: MmarC7_0305
            MAC: MA0104(surE)
            MBA: Mbar_A1192(surE)
            MMA: MM_1391(surE)
            MBU: Mbur_2188
            MHU: Mhun_0570 Mhun_2724
            MTH: MTH1435(surE)
            MST: Msp_0020(surE)
            MSI: Msm_1218
            MKA: MK0433(surE)
            AFU: AF0942(surE)
            HAL: VNG1241G(surE)
            HMA: rrnAC0514(surE)
            HWA: HQ2723A(ushA) HQ3350A(surE) HQ3676A(surE)
            NPH: NP1854A(ushA_1) NP2590A(ushA_2) NP4208A(surE)
            PTO: PTO1456(surE)
            TKO: TK1137
            APE: APE_0801.1(surE)
            PAI: PAE2908
STRUCTURES  PDB: 1HO5  1HP1  1HPU  1MH9  1OI8  1OID  1OIE  1Q91  1Q92  1USH  
                 2BDU  2CN1  2E69  2E6B  2E6C  2E6E  2E6G  2E6H  2G06  2J2C  
                 2JC9  2JCM  2JGA  2PAQ  2Q4T  2USH  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.5
            ExPASy - ENZYME nomenclature database: 3.1.3.5
            ExplorEnz - The Enzyme Database: 3.1.3.5
            ERGO genome analysis and discovery system: 3.1.3.5
            BRENDA, the Enzyme Database: 3.1.3.5
            CAS: 9027-73-0
///
ENTRY       EC 3.1.3.6                  Enzyme
NAME        3'-nucleotidase;
            3'-mononucleotidase;
            3'-phosphatase;
            3'-ribonucleotidase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     3'-ribonucleotide phosphohydrolase
REACTION    a 3'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R03060]
ALL_REAC    R03060 > R01562 R01877 R02148 R02370
SUBSTRATE   3'-ribonucleotide [CPD:C02508];
            H2O [CPD:C00001]
PRODUCT     ribonucleoside [CPD:C00911];
            phosphate [CPD:C00009]
COMMENT     Wide specificity for 3'-nucleotides.
REFERENCE   1  [PMID:13061389]
  AUTHORS   SHUSTER L, KAPLAN NO.
  TITLE     A specific b nucleotidase.
  JOURNAL   J. Biol. Chem. 201 (1953) 535-46.
  ORGANISM  Hordeum vulgare [GN:ehvu], Secale cereale
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K08693  3'-nucleotidase
GENES       ECO: b2744(surE)
            ECJ: JW2714(surE)
            ECE: Z4052(surE)
            ECS: ECs3598
            ECC: c3311(surE)
            ECV: APECO1_3779(surE)
            ECW: EcE24377A_3045(surE)
            ECX: EcHS_A2882(surE)
            STY: STY3052(surE)
            STT: t2828(surE)
            SPT: SPA2783(surE)
            SEC: SC2859(surE)
            STM: STM2927(surE)
            YPE: YPO3358(surE)
            YPK: y0831(surE)
            YPM: YP_0329(surE)
            YPS: YPTB0773(surE)
            YPI: YpsIP31758_3296(surE)
            SFL: SF2767(surE)
            SFX: S2960(surE)
            SSN: SSON_2892(surE)
            SBO: SBO_2776(surE)
            SDY: SDY_2943(surE)
            PLU: plu0716(surE)
            WBR: WGLp307(surE)
            SGL: SG0528
            SPE: Spro_0829
            ASU: Asuc_0562
            PAP: PSPA7_1514(surE)
            SSE: Ssed_1295
            CBD: COXBU7E912_0329(surE)
            MMW: Mmwyl1_1304
            CFF: CFF8240_0325(surE)
            CCV: CCV52592_1650(surE)
            CHA: CHAB381_1313(surE)
            CCO: CCC13826_1575(surE)
            BOV: BOV_0877(surE)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.6
            ExPASy - ENZYME nomenclature database: 3.1.3.6
            ExplorEnz - The Enzyme Database: 3.1.3.6
            ERGO genome analysis and discovery system: 3.1.3.6
            BRENDA, the Enzyme Database: 3.1.3.6
            CAS: 9025-84-7
///
ENTRY       EC 3.1.3.7                  Enzyme
NAME        3'(2'),5'-bisphosphate nucleotidase;
            phosphoadenylate 3'-nucleotidase;
            3'-phosphoadenylylsulfate 3'-phosphatase;
            phosphoadenylate 3'-nucleotidase;
            3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     adenosine-3'(2'),5'-bisphosphate 3'(2')-phosphohydrolase
REACTION    adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate +
            phosphate [RN:R00188]
ALL_REAC    R00188;
            (other) R00508
SUBSTRATE   adenosine 3',5'-bisphosphate [CPD:C00054];
            H2O [CPD:C00001]
PRODUCT     adenosine 5'-phosphate [CPD:C00020];
            phosphate [CPD:C00009]
COMMENT     Also acts on 3'-phosphoadenylyl sulfate, and on the corresponding
            2'-phosphates.
REFERENCE   1
  AUTHORS   Brungraber, E.G.
  TITLE     Nucleotides involved in the enzymatic conjugation of phenols with
            sulfate.
  JOURNAL   J. Biol. Chem. 233 (1958) 472-477.
  ORGANISM  rabbit
REFERENCE   2  [PMID:4313079]
  AUTHORS   Farooqui AA, Balasubramanian AS.
  TITLE     Enzymatic dephosphorylation 3'-phosphoadenosine 5'-phoaphosulfate to
            adenosine 5'-phosphosulfate in sheep brain.
  JOURNAL   Biochim. Biophys. Acta. 198 (1970) 56-65.
  ORGANISM  sheep
REFERENCE   3  [PMID:3038862]
  AUTHORS   Ramaswamy SG, Jakoby WB.
  TITLE     (2')3',5'-Bisphosphate nucleotidase.
  JOURNAL   J. Biol. Chem. 262 (1987) 10044-7.
  ORGANISM  guinea pig
REFERENCE   4  [PMID:179817]
  AUTHORS   Lik-Shing Tsang M, Schiff JA.
  TITLE     Properties of enzyme fraction A from Chlorella and copurification of
            3' (2'), 5'-biphosphonucleoside 3' (2')-phosphohydrolase, adenosine
            5'phosphosulfate sulfohydrolase and adenosine-5'-phosphosulfate
            cyclase activities.
  JOURNAL   Eur. J. Biochem. 65 (1976) 113-21.
  ORGANISM  Chlorella pyrenoidosa
PATHWAY     PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K01082  3'(2'), 5'-bisphosphate nucleotidase
GENES       HSA: 10380(BPNT1)
            MMU: 23827(Bpnt1)
            RNO: 64473(Bpnt1)
            CFA: 608525(BPNT1)
            GGA: 421347(RCJMB04_1g3)
            XLA: 447000(MGC82412)
            SPU: 580070(LOC580070)
            DME: Dmel_CG7789
            CEL: ZK430.2(tag-231)
            ATH: AT5G63980(SAL1)
            OSA: 4351686
            CME: CMR198C
            SCE: YOL064C(MET22)
            PIC: PICST_47423(MET22)
            CAL: CaO19.105
            CGR: CAGL0C05247g
            SPO: SPCC1753.04
            ANI: AN1769.2
            AFM: AFUA_4G04200 AFUA_6G09070
            AOR: AO090001000584
            UMA: UM01664.1
            DDI: DDBDRAFT_0167248 DDBDRAFT_0189923
            EHI: 139.t00015 26.t00063
            ECW: EcE24377A_4785(cysQ)
            ECX: EcHS_A4468(cysQ)
            YPI: YpsIP31758_3630(cysQ)
            PAP: PSPA7_5915(cysQ)
            PSP: PSPPH_0144(cysQ)
            PFL: PFL_0298(cysQ)
            CPS: CPS_0425(cysQ)
            CBD: COXBU7E912_0715(cysQ2) COXBU7E912_1466(cysQ1)
            MCA: MCA2983(cysQ)
            HCH: HCH_00565(cysQ)
            AHA: AHA_0584(cysQ-1) AHA_3497(cysQ-2)
            BCI: BCI_0570(cysQ)
            VOK: COSY_0110(cysQ)
            CJR: CJE1850(cysQ)
            CJJ: CJJ81176_1674(cysQ)
            CJU: C8J_1579(cysQ)
            CJD: JJD26997_2054(cysQ)
            CFF: CFF8240_0179(cysQ)
            RTY: RT0288(cysQ)
            RFE: RF_0482(cysQ)
            RBE: RBE_0639(cysQ)
            BOV: BOV_0187(cysQ)
            NWI: Nwi_0518
            RDE: RD1_0376(cysQ)
            HNE: HNE_0169(cysQ)
            GBE: GbCGDNIH1_2201
            CTR: CT774(cysQ)
            CTA: CTA_0844(cysQ)
            CMU: TC0155
            CPN: CPn0920(cysQ)
            CPA: CP0946
            CPJ: CPj0920(cysQ)
            CPT: CpB0952
            CCA: CCA00849
            CAB: CAB814
            CFE: CF0167(cysQ)
            PMC: P9515_13641(cysQ)
            PMF: P9303_06011(cysQ)
            PME: NATL1_16661(cysQ)
            SRU: SRU_1326
            CHU: CHU_0638(cysQ)
STRUCTURES  PDB: 1JP4  1K9Y  1K9Z  1KA0  1KA1  1QGX  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.7
            ExPASy - ENZYME nomenclature database: 3.1.3.7
            ExplorEnz - The Enzyme Database: 3.1.3.7
            ERGO genome analysis and discovery system: 3.1.3.7
            BRENDA, the Enzyme Database: 3.1.3.7
            CAS: 9025-83-6
///
ENTRY       EC 3.1.3.8                  Enzyme
NAME        3-phytase;
            1-phytase;
            phytase;
            phytate 1-phosphatase;
            phytate 6-phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     myo-inositol-hexakisphosphate 3-phosphohydrolase
REACTION    myo-inositol hexakisphosphate + H2O = 1D-myo-inositol
            1,2,4,5,6-pentakisphosphate + phosphate [RN:R03371]
ALL_REAC    R03371
SUBSTRATE   myo-inositol hexakisphosphate [CPD:C01204];
            H2O [CPD:C00001]
PRODUCT     1D-myo-inositol 1,2,4,5,6-pentakisphosphate [CPD:C04563];
            phosphate [CPD:C00009]
REFERENCE   1  [PMID:4310381]
  AUTHORS   Cosgrove DJ.
  TITLE     Ion-exchange chromatography of inositol polyphosphates.
  JOURNAL   Ann. N. Y. Acad. Sci. 165 (1969) 677-86.
REFERENCE   2  [PMID:4310376]
  AUTHORS   Johnson LF, Tate ME.
  TITLE     The structure of myo-inositol pentaphosphates.
  JOURNAL   Ann. N. Y. Acad. Sci. 165 (1969) 526-32.
REFERENCE   3  [PMID:4342816]
  AUTHORS   Irving GC, Cosgrove DJ.
  TITLE     Inositol phosphate phosphatases of microbiological origin: the
            inositol pentaphosphate products of Aspergillus ficuum phytases.
  JOURNAL   J. Bacteriol. 112 (1972) 434-8.
  ORGANISM  Aspergillus ficuum
REFERENCE   4
  AUTHORS   Cosgrove, D.J.
  TITLE     Inositol Phosphates: Their Chemistry, Biochemistry, and Physiology,
            Elsevier, Amsterdam, 1980.
PATHWAY     PATH: map00562  Inositol phosphate metabolism
ORTHOLOGY   KO: K01083  3-phytase
GENES       AFM: AFUA_3G00310 AFUA_4G08630 AFUA_7G01240
            ANG: An04g03460(phyA)
            ECA: ECA4198
            PSP: PSPPH_2990
            PMY: Pmen_4063
            SHE: Shewmr4_2083
            SHM: Shewmr7_1892
            SHN: Shewana3_2208
            SDE: Sde_3999
            MXA: MXAN_5326
            RLE: RL2519
            MMR: Mmar10_2368
            HNE: HNE_0176
            ZMO: ZMO0061(phyM)
            SAL: Sala_3124
            SWI: Swit_0531
            BSU: BG11198(phy)
            BAY: RBAM_019640
            SEN: SACE_0205 SACE_7374
            AVA: Ava_3999
STRUCTURES  PDB: 1CVM  1IHP  1POO  1QFX  1QLG  1QWO  1SK8  1SK9  1SKA  1SKB  
                 2GFI  2POO  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.8
            ExPASy - ENZYME nomenclature database: 3.1.3.8
            ExplorEnz - The Enzyme Database: 3.1.3.8
            ERGO genome analysis and discovery system: 3.1.3.8
            BRENDA, the Enzyme Database: 3.1.3.8
            CAS: 37288-11-2
///
ENTRY       EC 3.1.3.9                  Enzyme
NAME        glucose-6-phosphatase;
            glucose 6-phosphate phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     D-glucose-6-phosphate phosphohydrolase
REACTION    D-glucose 6-phosphate + H2O = D-glucose + phosphate [RN:R00303]
ALL_REAC    R00303 > R01788
SUBSTRATE   D-glucose 6-phosphate [CPD:C00092];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031];
            phosphate [CPD:C00009]
COMMENT     Wide distribution in animal tissues. Also catalyses potent
            transphosphorylations from carbamoyl phosphate, hexose phosphates,
            diphosphate, phosphoenolpyruvate and nucleoside di- and
            triphosphates, to D-glucose, D-mannose, 3-methyl-D-glucose or
            2-deoxy-D-glucose [cf. EC 2.7.1.62 (phosphoramidate---hexose
            phosphotransferase), EC 2.7.1.79 (diphosphate---glycerol
            phosphotransferase) and EC 3.9.1.1 (phosphoamidase)].
REFERENCE   1  [PMID:169241]
  AUTHORS   Anchors JM, Karnovsky ML.
  TITLE     Purification of cerebral glucose-6-phosphatase. An enzyme involved
            in sleep.
  JOURNAL   J. Biol. Chem. 250 (1975) 6408-16.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:164220]
  AUTHORS   Colilla W, Jorgenson RA, Nordlie RC.
  TITLE     Mammalian carbamyl phosphate : glucose phosphotransferase and
            glucose-6-phosphate phosphohydrolase: extended tissue distribution.
  JOURNAL   Biochim. Biophys. Acta. 377 (1975) 117-25.
  ORGANISM  rat [GN:rno], cow [GN:bta]
REFERENCE   3
  AUTHORS   Nordlie, R.C.
  TITLE     Glucose-6-phosphatase, hydrolytic and synthetic activities.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 4, Academic Press,
            New York, 1971, p. 543-610.
REFERENCE   4  [PMID:4370737]
  AUTHORS   Nordlie RC.
  TITLE     Metabolic regulation by multifunctional glucose-6-phosphatase.
  JOURNAL   Curr. Top. Cell. Regul. 8 (1974) 33-117.
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00052  Galactose metabolism
            PATH: map00500  Starch and sucrose metabolism
            PATH: map04910  Insulin signaling pathway
            PATH: map04920  Adipocytokine signaling pathway
ORTHOLOGY   KO: K01084  glucose-6-phosphatase
GENES       HSA: 2538(G6PC) 57818(G6PC2)
            MMU: 14377(G6pc)
            RNO: 25634(G6pc)
            CFA: 403492(G6PC)
            XLA: 379290(MGC53852) 379852(g6pc)
            XTR: 448183(g6pc)
            HMA: rrnAC2781(pap2a) rrnAC3274(pap2b)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.9
            ExPASy - ENZYME nomenclature database: 3.1.3.9
            ExplorEnz - The Enzyme Database: 3.1.3.9
            ERGO genome analysis and discovery system: 3.1.3.9
            BRENDA, the Enzyme Database: 3.1.3.9
            CAS: 9001-39-2
///
ENTRY       EC 3.1.3.10                 Enzyme
NAME        glucose-1-phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     alpha-D-glucose-1-phosphate phosphohydrolase
REACTION    alpha-D-glucose 1-phosphate + H2O = D-glucose + phosphate
            [RN:R00304]
ALL_REAC    R00304 > R00947
SUBSTRATE   alpha-D-glucose 1-phosphate [CPD:C00103];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031];
            phosphate [CPD:C00009]
COMMENT     Also acts, more slowly, on D-galactose 1-phosphate.
REFERENCE   1  [PMID:13249953]
  AUTHORS   FAULKNER P.
  TITLE     A hexose-1-phosphatase in silkworm blood.
  JOURNAL   Biochem. J. 60 (1955) 590-6.
  ORGANISM  Bombyx mori [GN:dbmo]
REFERENCE   2
  AUTHORS   Turner, D.H. and Turner, J.F.
  TITLE     The hydrolysis of glucose monophosphates by a phosphatase
            preparation from pea seeds.
  JOURNAL   Biochem. J. 74 (1960) 486-491.
  ORGANISM  Pisum sativum
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
ORTHOLOGY   KO: K01085  glucose-1-phosphatase
GENES       ECO: b1002(agp)
            ECJ: JW0987(agp)
            ECE: Z1421(agp)
            ECS: ECs1158
            ECC: c1137(agp)
            ECI: UTI89_C1065(agp)
            ECP: ECP_1001
            ECW: EcE24377A_1120(agp)
            ECX: EcHS_A1115
            STY: STY1153(agp)
            STT: t1803(agp)
            SPT: SPA1733(agp)
            SEC: SC1067(agp)
            STM: STM1117(agp)
            SFL: SF1006(agp)
            SFX: S1075(agp)
            SFV: SFV_1014(agp)
            SSN: SSON_1012(agp)
            SDY: SDY_0978(agp)
            ENT: Ent638_1514
            SPE: Spro_3164
            GOX: GOX1190
STRUCTURES  PDB: 1NT4  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.10
            ExPASy - ENZYME nomenclature database: 3.1.3.10
            ExplorEnz - The Enzyme Database: 3.1.3.10
            ERGO genome analysis and discovery system: 3.1.3.10
            BRENDA, the Enzyme Database: 3.1.3.10
            CAS: 9001-38-1
///
ENTRY       EC 3.1.3.11                 Enzyme
NAME        fructose-bisphosphatase;
            hexose diphosphatase;
            FBPase;
            fructose 1,6-diphosphatase;
            fructose 1,6-diphosphate phosphatase;
            D-fructose 1,6-diphosphatase;
            fructose 1,6-bisphosphatase;
            fructose diphosphatase;
            fructose diphosphate phosphatase;
            fructose bisphosphate phosphatase;
            fructose 1,6-bisphosphate 1-phosphatase;
            fructose 1,6-bisphosphate phosphatase;
            hexose bisphosphatase;
            D-fructose-1,6-bisphosphate phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     D-fructose-1,6-bisphosphate 1-phosphohydrolase
REACTION    D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate +
            phosphate [RN:R00762]
ALL_REAC    R00762 > R04780;
            (other) R01845
SUBSTRATE   D-fructose 1,6-bisphosphate [CPD:C00354];
            H2O [CPD:C00001]
PRODUCT     D-fructose 6-phosphate [CPD:C00085];
            phosphate [CPD:C00009]
COMMENT     The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
REFERENCE   1
  AUTHORS   El-Badry, A.M.
  TITLE     Hexosediphosphatase from spinach chloroplasts. Purification,
            crystallization and some properties.
  JOURNAL   Biochim. Biophys. Acta 333 (1974) 366-377.
  ORGANISM  spinach
REFERENCE   2
  AUTHORS   Gomori, G.
  TITLE     Hexosediphosphatase.
  JOURNAL   J. Biol. Chem. 148 (1943) 139-149.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Mokrash, L.C. and McGilvery, R.N.
  TITLE     Purification and properties of fructose-1,6-diphosphatase.
  JOURNAL   J. Biol. Chem. 221 (1956) 909-917.
  ORGANISM  rabbit
REFERENCE   4  [PMID:4284291]
  AUTHORS   Pontremoli S, Traniello S, Luppis B, Wood WA.
  TITLE     Fructose diphosphatase from rabbit liver. I. Purification and
            properties.
  JOURNAL   J. Biol. Chem. 240 (1965) 3459-63.
  ORGANISM  rabbit
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00030  Pentose phosphate pathway
            PATH: map00051  Fructose and mannose metabolism
            PATH: map00710  Carbon fixation
            PATH: map04910  Insulin signaling pathway
ORTHOLOGY   KO: K01086  fructose-1,6-bisphosphatase
            KO: K02446  fructose-1,6-bisphosphatase II
            KO: K03841  fructose-1,6-bisphosphatase I
            KO: K04041  fructose-1,6-bisphosphatase III
GENES       HSA: 2203(FBP1) 8789(FBP2)
            PTR: 465261(FBP2)
            MMU: 14120(Fbp2) 14121(Fbp1)
            RNO: 114508(Fbp2) 24362(Fbp1)
            CFA: 476299(FBP1) 476300(FBP2)
            SSC: 397038(FBP)
            GGA: 395217(FBP2) 395218(FBP1)
            XLA: 380220(fbp)
            XTR: 394750(MGC75708)
            SPU: 577064(LOC577064)
            DME: Dmel_CG31692(fbp)
            CEL: K07A3.1(fructose-bisphosphatase)
            ATH: AT1G43670 AT3G54050
            OSA: 4325071 4332364 4338912
            CME: CMD041C CMO245C CMP129C
            SCE: YLR377C(FBP1)
            AGO: AGOS_AFR593C
            PIC: PICST_51462(FBP1)
            CAL: CaO19.6178(fbp1)
            CGR: CAGL0H04939g CAGL0I04048g
            SPO: SPBC1198.14c(fbp1)
            ANI: AN5604.2
            AFM: AFUA_4G11310
            AOR: AO090003001089
            CNE: CNA00470
            UMA: UM02703.1
            DDI: DDB_0216231(fbp)
            TET: TTHERM_00058590 TTHERM_01035580
            TBR: Tb09.211.0540
            TCR: 506649.70 508351.10
            LMA: LmjF04.1160
            ECO: b3925(glpX) b4232(fbp)
            ECJ: JW3896(glpX) JW4191(fbp)
            ECE: Z5470(glpX) Z5842(fbp)
            ECS: ECs4850 ECs5209
            ECC: c4877(glpX) c5329(fbp)
            ECI: UTI89_C4509(glpX) UTI89_C4836(fbp)
            ECP: ECP_4134 ECP_4481
            ECV: APECO1_2160(fbp) APECO1_2544(glpX)
            ECW: EcE24377A_0793(ybhA) EcE24377A_3265(glpX1)
                 EcE24377A_4459(glpX) EcE24377A_4801(fbp)
            ECX: EcHS_A0820(ybhA) EcHS_A3088(glpX2) EcHS_A4156(glpX1)
                 EcHS_A4485(fbp)
            STY: STY3785(glpX) STY4774(fbp)
            STT: t3533(glpX) t4469(fbp)
            SPT: SPA3928(glpX) SPA4235(fbp)
            SEC: SC3974(glpX) SC4289(fbp)
            STM: STM4085(glpX) STM4415(fbp)
            YPE: YPO3520(fbp)
            YPK: y0048(glpX) y0664(fbp)
            YPM: YP_0093(glpX) YP_0563(fbp)
            YPA: YPA_0070 YPA_3452
            YPN: YPN_3264 YPN_3759
            YPS: YPTB0085(glpX) YPTB0456(fbp)
            YPI: YpsIP31758_0100(glpX) YpsIP31758_3621(fbp)
            SFL: SF4003(glpX) SF4258(fbp)
            SFX: S3744(glpX) S4520(fbp)
            SFV: SFV_3996(glpX) SFV_4259(fbp)
            SSN: SSON_4094(glpX) SSON_4413(fbp)
            SBO: SBO_3942(glpX) SBO_4214(fbp)
            SDY: SDY_3819(glpX) SDY_4250(fbp)
            ECA: ECA3927(fbp) ECA4268(glpX)
            PLU: plu4550(fbp)
            WBR: WGLp479(fbp)
            SGL: SG0356
            HIN: HI0667(glpX) HI1645(fbp)
            HIT: NTHI0789(glpX) NTHI1394(fbp)
            HIP: CGSHiEE_05925 CGSHiEE_08915(glpX)
            HIQ: CGSHiGG_06615(glpX)
            HDU: HD0702(fbp)
            HSO: HS_1248(fbp)
            PMU: PM0930(fbp) PM1482(glpX)
            MSU: MS1615(fbp) MS2254(glpX)
            APL: APL_0624(glpX) APL_1450(fbp)
            XCC: XCC0096(cbbFC)
            XCB: XC_0098
            XCV: XCV0098(cbbFC)
            XAC: XAC0124(cbbFC)
            XOO: XOO0015(cbbFC)
            XOM: XOO_0016(XOO0016)
            VCH: VC2544 VC2688
            VCO: VC0395_A2122(fbp)
            VVU: VV1_0707 VV1_1349
            VVY: VV0434 VV3020
            VPA: VP0244 VP0313
            VFI: VF0209 VF0264
            PPR: PBPRA0240 PBPRA0384
            PAE: PA5110(fbp)
            PAU: PA14_67490(fbp)
            PPU: PP_5040(fbp)
            PST: PSPTO_5168(fbp)
            PSB: Psyr_0370
            PSP: PSPPH_0353(fbp)
            PFL: PFL_0393(fbp)
            PFO: Pfl_0352
            PEN: PSEEN5106(fbp)
            PAR: Psyc_0541(fbp)
            PCR: Pcryo_0530
            ACI: ACIAD2625(fbp)
            SON: SO_3991(fbp)
            SDN: Sden_2986
            SFR: Sfri_0531
            SHE: Shewmr4_0649
            SHM: Shewmr7_3373
            SHN: Shewana3_0648 Shewana3_3505
            ILO: IL2262(fbp)
            CPS: CPS_4614(fbp)
            PHA: PSHAa0463(fbp) PSHAa1742 PSHAb0549
            PAT: Patl_0242
            FTU: FTT1631c(gplX)
            FTF: FTF1631c(gplX)
            FTW: FTW_0283(glpX)
            FTL: FTL_1701
            FTH: FTH_1638(glpX)
            FTA: FTA_1800(glpX)
            FTN: FTN_0298(gplX)
            TCX: Tcr_1495
            NOC: Noc_0021
            AEH: Mlg_2636
            HCH: HCH_06446
            AHA: AHA_0464(glpX) AHA_2002(fbp)
            DNO: DNO_0468(fbp)
            NME: NMB1060
            NMA: NMA1259(fbp)
            NMC: NMC1022(fbp)
            NGO: NGO0862
            CVI: CV_2427(fbp)
            RSO: RSc2126(fbp)
            REU: Reut_A2444
            REH: H16_A0999(fbp) H16_B1390(cbbF2)
            RME: Rmet_0875 Rmet_1511
            BMA: BMA0469(fbp)
            BMV: BMASAVP1_A2618(fbp)
            BML: BMA10299_A0990(fbp)
            BMN: BMA10247_0157(fbp)
            BXE: Bxe_A0920 Bxe_B2450
            BUR: Bcep18194_A4125
            BCN: Bcen_0535
            BCH: Bcen2424_1014
            BAM: Bamb_0877
            BPS: BPSL2547(fbp)
            BPM: BURPS1710b_3031(fbp)
            BPL: BURPS1106A_2987(fbp)
            BPD: BURPS668_2925(fbp)
            BTE: BTH_I1604(cbbF)
            BPE: BP0868(fbp)
            BPA: BPP2482(fbp)
            BBR: BB1929(fbp)
            RFR: Rfer_1393 Rfer_2704
            POL: Bpro_1586
            MPT: Mpe_A1481(cbbF) Mpe_A2775(cbbF) Mpe_A2788(cbbF)
            HAR: HEAR0572(fbp)
            MMS: mma_0554(fbp)
            NEU: NE0521(cbbF)
            NET: Neut_1176
            EBA: ebA1191(fbp)
            AZO: azo0968(cbbF)
            DAR: Daro_3589 Daro_3628
            TBD: Tbd_2577(cbbF)
            MFA: Mfla_0586
            HPY: HP1385
            HPJ: jhp1440(fbp)
            HPA: HPAG1_1483
            HHE: HH1344(fbp)
            HAC: Hac_1780(fbp)
            WSU: WS0218(fbp)
            TDN: Tmden_1063
            CJE: Cj0840c(fbp)
            CJR: CJE0927(fbp)
            CJJ: CJJ81176_0857(fbp)
            CJU: C8J_0787(fbp)
            CJD: JJD26997_0990(fbp)
            CFF: CFF8240_0794(fbp)
            CCV: CCV52592_0443(fbp)
            CHA: CHAB381_0729(fbp)
            CCO: CCC13826_1544(fbp)
            ABU: Abu_1219(fbp)
            NIS: NIS_0796(fbp)
            SUN: SUN_1133(fbp)
            GSU: GSU1651(fbP-1)
            GME: Gmet_1921
            GUR: Gura_2378
            PCA: Pcar_1027 Pcar_2334
            PPD: Ppro_1776
            DVU: DVU1539(glpX) DVU1841(fbp)
            DDE: Dde_1796 Dde_2069
            LIP: LI0228(glpX) LI0369(fbp)
            BBA: Bd1919(glpX)
            DPS: DP1665 DP1666
            ADE: Adeh_1640
            MXA: MXAN_4455(glpX)
            SAT: SYN_01924 SYN_02232
            WOL: WD0687(glpX)
            WBM: Wbm0158
            AMA: AM964(glpX)
            APH: APH_0222(glpX)
            ERU: Erum6470(glpX)
            ERW: ERWE_CDS_06780
            ERG: ERGA_CDS_06690
            ECN: Ecaj_0654(glpX)
            ECH: ECH_0356(glpX)
            NSE: NSE_0592(glpX)
            PUB: SAR11_1009(glpX)
            MLO: mll0929
            MES: Meso_0989
            SME: SMb20202(cbbF)
            BME: BMEI0726 BMEII0422
            BMF: BAB1_1292(glpX) BAB2_0364
            BMS: BR1273(glpX) BRA0872(fbp)
            BMB: BruAb1_1274(glpX) BruAb2_0360(fbp)
            BOV: BOV_1236(glpX) BOV_A0819(fbp)
            BJA: blr2581(cbbF) blr4363
            BRA: BRADO1655(cbbF) BRADO3573(glpX)
            BBT: BBta_0445(cbbF) BBta_3997(glpX) BBta_6401(cbbF)
            RPA: RPA2505(glpX) RPA4645(cbbF)
            RPB: RPB_0947 RPB_2965
            RPC: RPC_2815 RPC_2899
            RPD: RPD_1050 RPD_2496
            RPE: RPE_2682 RPE_2936
            NWI: Nwi_1646(glpX) Nwi_2694
            NHA: Nham_2308 Nham_3754 Nham_4046
            BHE: BH10020(glpX)
            BQU: BQ07740(glpX)
            BBK: BARBAKC583_0746(glpX)
            CCR: CC_1384 CC_1385
            SIL: SPO1733(glpX)
            SIT: TM1040_2165
            RSP: RSP_0404 RSP_1285(cbbF1) RSP_3266(fbpB)
            JAN: Jann_3000
            RDE: RD1_2537(glpX)
            MMR: Mmar10_1507
            HNE: HNE_2309(glpX)
            ZMO: ZMO0329(cbbF) ZMO0482(cbbF) ZMO1409(cbbF) ZMO1518(cbbF)
            NAR: Saro_0021
            SAL: Sala_2107
            ELI: ELI_13785
            GOX: GOX1516
            GBE: GbCGDNIH1_1399
            RRU: Rru_A2403 Rru_A2409
            MAG: amb1382 amb2661 amb3729
            ABA: Acid345_0609
            BSU: BG10415(ywjI) BG11478(fbp)
            BHA: BH3783
            BAN: BA5195(fbp-1) BA5576(fbp-2)
            BAR: GBAA5195(fbp-1) GBAA5576(fbp-2)
            BAT: BAS4830 BAS5182
            BCE: BC4962 BC5333
            BCA: BCE_5099(fbp) BCE_5462(fbp)
            BCZ: BCZK4688(fbp) BCZK5033
            BTK: BT9727_4671(fbp) BT9727_5017(fbp)
            BTL: BALH_4495(fbp) BALH_4831(fbp)
            BLI: BL03972(ywjI)
            BLD: BLi03957(ywjI)
            BCL: ABC3608 ABC3880
            BAY: RBAM_037000(fbp)
            BPU: BPUM_3353(ywjI)
            OIH: OB2859 OB3002
            GKA: GK3383
            SAU: SA2304(fbp)
            SAV: SAV2516(fbp)
            SAM: MW2435(fbp)
            SAR: SAR2596
            SAS: SAS2401
            SAC: SACOL2527
            SAB: SAB2390
            SAA: SAUSA300_2455
            SAO: SAOUHSC_02822
            SEP: SE2063
            SER: SERP2076
            SHA: SH0559(fbp)
            SSP: SSP0398
            LMO: lmo0830(fbp)
            LMF: LMOf2365_0847
            LIN: lin0825(fbp)
            LWE: lwe0821(fbp)
            LLA: L54021(fbp)
            LLM: llmg_0264(fbp)
            SAG: SAG0516
            SAN: gbs0562
            SAK: SAK_0666(fbp)
            SSA: SSA_1056
            SGO: SGO_0813
            LSA: LSA1778(fbp)
            LSL: LSL_1903
            LCA: LSEI_2045
            EFA: EF1503
            STH: STH67
            CAC: CAC1088(glpX) CAC1572
            CTC: CTC00604 CTC01007(glpX)
            CNO: NT01CX_1512 NT01CX_1655(glpX)
            CDF: CD1191(fbp)
            CBO: CBO0516(fbp)
            CBA: CLB_0556 CLB_2558(glpX)
            CBH: CLC_0589 CLC_2489(glpX)
            CBF: CLI_0596 CLI_2680(glpX)
            CKL: CKL_0799(fbp)
            CHY: CHY_0787(glpX)
            DSY: DSY4937
            SWO: Swol_2409
            MTU: Rv1099c
            MTC: MT1131(glpX)
            MBO: Mb1129c
            MLE: ML1946
            MPA: MAP2692
            MAV: MAV_1222(glpX)
            MSM: MSMEG_5239(glpX)
            MMC: Mmcs_4121
            CGL: NCgl0976(cgl1019)
            CGB: cg1157(glpX)
            CEF: CE1075
            CDI: DIP0939
            NFA: nfa48000
            RHA: RHA1_ro05865(glpX)
            SCO: SCO5047(SCK7.20c)
            SMA: SAV3215(glpX)
            LXX: Lxx16670
            CMI: CMM_2735(glpX)
            AAU: AAur_1302(glpX)
            TFU: Tfu_0464(glpX)
            FRA: Francci3_3876
            FAL: FRAAL6145(glpX)
            SEN: SACE_0934(glpX) SACE_4900(glpX)
            RXY: Rxyl_1656
            FNU: FN0798 FN1159
            LIL: LA2226(fbp)
            LIC: LIC11707(fbp)
            LBJ: LBJ_1370(fbp)
            LBL: LBL_1595(fbp)
            SYN: slr0952(fbpII) slr2094(fbpI)
            SYW: SYNW1116(glpX)
            SYC: syc1015_d(glpX) syc1767_d(fbpI)
            SYF: Synpcc7942_0505 Synpcc7942_2335
            SYD: Syncc9605_1253
            SYE: Syncc9902_1229
            SYG: sync_1685(glpX)
            SYR: SynRCC307_1255(glpX)
            SYX: SynWH7803_1300(glpX)
            CYA: CYA_0542(glpX) CYA_1698(fbp)
            CYB: CYB_1986(fbp) CYB_2257(glpX)
            TEL: tll0541(fbpII) tll1276(fbpI)
            GVI: glr3129(fbp) glr3342(fbp)
            ANA: all4021(fbp) alr1041
            AVA: Ava_1680 Ava_3697(glpX)
            PMA: Pro0840(glpX)
            PMM: PMM0767(glpX)
            PMT: PMT0568(glpX)
            PMN: PMN2A_0173(glpX)
            PMI: PMT9312_0775
            PMB: A9601_08291(glpX)
            PMC: P9515_08161(glpX)
            PMF: P9303_16831(glpX)
            PMG: P9301_08271(glpX)
            PMH: P9215_08611(glpX)
            PME: NATL1_08051(glpX)
            TER: Tery_0682 Tery_0948
            BTH: BT_1228
            BFR: BF1819
            BFS: BF1884
            PGI: PG0793(fbp)
            SRU: SRU_1474(fbp) SRU_1856(fbp)
            CHU: CHU_2896(fbp)
            GFO: GFO_1163(fbp) GFO_3521(fbp)
            FPS: FP0299(fbp)
            CTE: CT0358(fbp)
            CCH: Cag_0602
            PLT: Plut_0461 Plut_0462
            DRA: DR_2013
            DGE: Dgeo_1876
            TTH: TTC1081
            TTJ: TTHA1446
            MAC: MA1152(fbp)
            MBA: Mbar_A1836
            MMA: MM_2181
            MBU: Mbur_1354
            MHU: Mhun_1206
            MBN: Mboo_1610
            HAL: VNG0684G(fbp)
            HMA: rrnAC0772(fbp2) rrnAC1138(fbp1)
            HWA: HQ1465A(suhB) HQ1881A(fbp) HQ2795A(suhB)
            NPH: NP1592A(fbp) NP4188A(suhB)
STRUCTURES  PDB: 1BK4  1CNQ  1D9Q  1DBZ  1DCU  1EYI  1EYJ  1EYK  1FBC  1FBD  
                 1FBE  1FBF  1FBG  1FBH  1FBP  1FJ6  1FJ9  1FPB  1FPD  1FPE  
                 1FPF  1FPG  1FPI  1FPJ  1FPK  1FPL  1FRP  1FSA  1FTA  1KZ8  
                 1LBV  1LBW  1LBX  1LBY  1LBZ  1LEV  1NUW  1NUX  1NUY  1NUZ  
                 1NV0  1NV1  1NV2  1NV3  1NV4  1NV5  1NV6  1NV7  1Q9D  1RDX  
                 1RDY  1RDZ  1SPI  1UMG  1YXI  1YYZ  1YZ0  2F3B  2F3D  2F3H  
                 2FBP  2FHY  2FIE  2FIX  2GQ1  2OWZ  2OX3  2Q8M  3FBP  4FBP  
                 5FBP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.11
            ExPASy - ENZYME nomenclature database: 3.1.3.11
            ExplorEnz - The Enzyme Database: 3.1.3.11
            ERGO genome analysis and discovery system: 3.1.3.11
            BRENDA, the Enzyme Database: 3.1.3.11
            CAS: 9001-52-9
///
ENTRY       EC 3.1.3.12                 Enzyme
NAME        trehalose-phosphatase;
            trehalose 6-phosphatase;
            trehalose 6-phosphate phosphatase;
            trehalose-6-phosphate phosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     alpha,alpha-trehalose-6-phosphate phosphohydrolase
REACTION    alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose +
            phosphate [RN:R02778 R06228]
ALL_REAC    R02778 R06228(G)
SUBSTRATE   alpha,alpha'-trehalose 6-phosphate [CPD:C00689];
            H2O [CPD:C00001]
PRODUCT     alpha,alpha-trehalose [CPD:C01083];
            phosphate [CPD:C00009]
REFERENCE   1  [PMID:13538966]
  AUTHORS   CABIB E, LELOIR LF.
  TITLE     The biosynthesis of trehalose phosphate.
  JOURNAL   J. Biol. Chem. 231 (1958) 259-75.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:13690400]
  AUTHORS   CANDY DJ, KILBY BA.
  TITLE     The biosynthesis of trehalose in the locust fat body.
  JOURNAL   Biochem. J. 78 (1961) 531-6.
  ORGANISM  Phormia regina
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01087  trehalose-phosphatase
GENES       ATH: AT1G06410(ATTPS7)
            CME: CMQ148C
            SCE: YDR074W(TPS2)
            AGO: AGOS_AGR132W
            PIC: PICST_79118(TPS2)
            CAL: CaO19_3038(CaO19.3038)
            CGR: CAGL0G05335g
            SPO: SPAC19G12.15c SPAC3G6.09c
            CNE: CNB02610
            DDI: DDB_0231987(tpsB)
            TAN: TA20125
            TET: TTHERM_00077390
            ECO: b1897(otsB)
            ECJ: JW1886(otsB)
            ECE: Z2950(otsB)
            ECS: ECs2605
            ECC: c2311(otsB)
            ECI: UTI89_C2098(otsB)
            ECP: ECP_1839
            ECV: APECO1_943(otsB)
            ECW: EcE24377A_2129(otsB)
            ECX: EcHS_A1994
            STY: STY2138(otsB)
            STT: t0948(otsB)
            SPT: SPA0939(otsB)
            SEC: SC1936(otsB)
            STM: STM1929(otsB)
            SFL: SF1944(otsB)
            SFX: S2036(otsB)
            SFV: SFV_1941(otsB)
            SSN: SSON_1220(otsB)
            SGL: SG1240
            ENT: Ent638_2473
            XCC: XCC3080(ostB)
            XCB: XC_1078
            XCV: XCV3334(ostB)
            XAC: XAC3209(ostB)
            XOO: XOO1603(ostB)
            XOM: XOO_1487(XOO1487)
            PCR: Pcryo_1803
            ACI: ACIAD1775(otsB)
            NOC: Noc_1775
            AEH: Mlg_0005
            CSA: Csal_0236
            RSO: RSp1104(otsB)
            REU: Reut_A0414
            REH: H16_A0428(otsB)
            RME: Rmet_0355
            BMA: BMA0565(otsB)
            BMV: BMASAVP1_A2443(otsB)
            BML: BMA10299_A2838(otsB)
            BMN: BMA10247_1766(otsB)
            BXE: Bxe_A1241
            BVI: Bcep1808_1075
            BUR: Bcep18194_A4269
            BCN: Bcen_0678
            BCH: Bcen2424_1157
            BAM: Bamb_1035
            BPS: BPSL2411(otsB)
            BPM: BURPS1710b_2873(otsB)
            BPL: BURPS1106A_2815(otsB)
            BPD: BURPS668_2755(otsB)
            BTE: BTH_I1752(otsB)
            RFR: Rfer_2155
            POL: Bpro_3915
            PNA: Pnap_0526
            AAV: Aave_4210
            AJS: Ajs_0503
            VEI: Veis_1468
            MPT: Mpe_A3792
            GSU: GSU2336(otsB)
            PCA: Pcar_0054
            DDE: Dde_2061
            ADE: Adeh_0450
            AFW: Anae109_3011
            MXA: MXAN_1192(otsAB)
            SAT: SYN_00622 SYN_02627
            MLO: mll0690
            PLA: Plav_0306
            SMD: Smed_5910
            RET: RHE_PC00228(otsB)
            RLE: pRL100466(otsB)
            OAN: Oant_2714
            BJA: bll0323(otsB)
            BRA: BRADO6953(otsB)
            BBT: BBta_0577(otsB)
            RPA: RPA4661(otsB)
            RPB: RPB_0916
            RPC: RPC_4524
            RPD: RPD_1027
            RPE: RPE_4552
            NWI: Nwi_3026
            NHA: Nham_3613
            XAU: Xaut_1722
            RSP: RSP_0949(ostB)
            RSH: Rsph17029_2609
            RSQ: Rsph17025_2945
            JAN: Jann_2062
            MMR: Mmar10_1019
            HNE: HNE_1576(otsB)
            NAR: Saro_1503
            SWI: Swit_3608
            ELI: ELI_04680
            GOX: GOX1118
            GBE: GbCGDNIH1_1732
            RRU: Rru_A2549
            CHY: CHY_0671(otsB)
            MTA: Moth_1368
            MTU: Rv3372(otsB2)
            MTC: MT3482
            MBO: Mb3407(otsB2)
            MBB: BCG_3444(otsB2)
            MLE: ML0414(otsB2)
            MPA: MAP3478(otsB2)
            MSM: MSMEG_6043(otsB)
            MMC: Mmcs_4714
            CGL: NCgl2537(cgl2626)
            CGB: cg2909(otsB)
            CEF: CE2510
            CDI: DIP1968
            CJK: jk0330(otsB)
            RHA: RHA1_ro00045
            LXX: Lxx13220(otsB)
            CMI: CMM_1086(otsB)
            AAU: AAur_0930(otsB) AAur_3722(otsB)
            PAC: PPA0962
            FAL: FRAAL6697(otsB)
            SEN: SACE_2445 SACE_2447 SACE_3700(otsB2)
            SRU: SRU_0568(otsB)
            DGE: Dgeo_0060
            TTJ: TTHA0479
            MTP: Mthe_0799
            MEM: Memar_2216
            TAC: Ta1209m
            TVO: TVN1255
            PTO: PTO1210
            PIS: Pisl_1339
            PCL: Pcal_1363
            PAS: Pars_0598
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.12
            ExPASy - ENZYME nomenclature database: 3.1.3.12
            ExplorEnz - The Enzyme Database: 3.1.3.12
            ERGO genome analysis and discovery system: 3.1.3.12
            BRENDA, the Enzyme Database: 3.1.3.12
            CAS: 9025-72-3
///
ENTRY       EC 3.1.3.13                 Enzyme
NAME        bisphosphoglycerate phosphatase;
            2,3-diphosphoglycerate phosphatase;
            diphosphoglycerate phosphatase;
            2,3-diphosphoglyceric acid phosphatase;
            2,3-bisphosphoglycerate phosphatase;
            glycerate-2,3-diphosphate phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     2,3-bisphospho-D-glycerate 2-phosphohydrolase
REACTION    2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate
            [RN:R01516]
ALL_REAC    R01516
SUBSTRATE   2,3-bisphospho-D-glycerate [CPD:C01159];
            H2O [CPD:C00001]
PRODUCT     3-phospho-D-glycerate [CPD:C00197];
            phosphate [CPD:C00009]
REFERENCE   1  [PMID:13563500]
  AUTHORS   JOYCE BK, GRISOLIA S.
  TITLE     Studies on glycerate 2,3-diphosphatase.
  JOURNAL   J. Biol. Chem. 233 (1958) 350-4.
  ORGANISM  rat [GN:rno], rabbit, chicken [GN:gga], Saccharomyces cerevisiae
            [GN:sce]
REFERENCE   2  [PMID:14832286]
  AUTHORS   RAPOPORT S, LUEBERING J.
  TITLE     Glycerate-2,3-diphosphatase.
  JOURNAL   J. Biol. Chem. 189 (1951) 683-94.
  ORGANISM  rabbit
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
ORTHOLOGY   KO: K01088  bisphosphoglycerate phosphatase
GENES       HSA: 441531(PGAM4) 5223(PGAM1) 5224(PGAM2) 669(BPGM)
            PTR: 463746(BPGM) 494122(PGAM4)
            MMU: 12183(Bpgm) 18648(Pgam1) 56012(Pgam2)
            RNO: 24642(Pgam1) 24959(Pgam2)
            CFA: 475495(PGAM2) 477786(PGAM1) 482704(BPGM)
            BTA: 404148(PGAM1)
            GGA: 418172(RCJMB04_32o10) 428969(RCJMB04_5g20)
            XLA: 432058(MGC81450) 444102(MGC80400) 447767(MGC84250)
            XTR: 448157(pgam1)
            DRE: 393999(pgam2) 408255(pgam1l)
            DME: Dmel_CG1721(Pglym78)
STRUCTURES  PDB: 1YFK  1YJX  2F90  2H4X  2H4Z  2H52  2HHJ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.13
            ExPASy - ENZYME nomenclature database: 3.1.3.13
            ExplorEnz - The Enzyme Database: 3.1.3.13
            ERGO genome analysis and discovery system: 3.1.3.13
            BRENDA, the Enzyme Database: 3.1.3.13
            CAS: 9033-04-9
///
ENTRY       EC 3.1.3.14                 Enzyme
NAME        methylphosphothioglycerate phosphatase;
            methylthiophosphoglycerate phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     S-methyl-3-phospho-1-thio-D-glycerate phosphohydrolase
REACTION    S-methyl-3-phospho-1-thio-D-glycerate + H2O =
            S-methyl-1-thio-D-glycerate + phosphate [RN:R04317]
ALL_REAC    R04317
SUBSTRATE   S-methyl-3-phospho-1-thio-D-glycerate [CPD:C04399];
            H2O [CPD:C00001]
PRODUCT     S-methyl-1-thio-D-glycerate [CPD:C03804];
            phosphate [CPD:C00009]
REFERENCE   1
  AUTHORS   Black, S. and Wright, N.G.
  TITLE     Enzymatic formation of glyceryl and phosphoglyceryl methylthiol
            esters.
  JOURNAL   J. Biol. Chem. 221 (1956) 171-180.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.14
            ExPASy - ENZYME nomenclature database: 3.1.3.14
            ExplorEnz - The Enzyme Database: 3.1.3.14
            ERGO genome analysis and discovery system: 3.1.3.14
            BRENDA, the Enzyme Database: 3.1.3.14
            CAS: 9025-78-9
///
ENTRY       EC 3.1.3.15                 Enzyme
NAME        histidinol-phosphatase;
            histidinol phosphate phosphatase;
            L-histidinol phosphate phosphatase;
            histidinolphosphate phosphatase;
            HPpase;
            histidinolphosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     L-histidinol-phosphate phosphohydrolase
REACTION    L-histidinol phosphate + H2O = L-histidinol + phosphate [RN:R03013]
ALL_REAC    R03013
SUBSTRATE   L-histidinol phosphate [CPD:C01100];
            H2O [CPD:C00001]
PRODUCT     L-histidinol [CPD:C00860];
            phosphate [CPD:C00009]
REFERENCE   1  [PMID:13438843]
  AUTHORS   AMES BN.
  TITLE     The biosynthesis of histidine; L-histidinol phosphate phosphatase.
  JOURNAL   J. Biol. Chem. 226 (1957) 583-93.
  ORGANISM  Neurospora crassa [GN:dncr], Escherichia coli [GN:eco]
PATHWAY     PATH: map00340  Histidine metabolism
ORTHOLOGY   KO: K01089  histidinol-phosphatase
            KO: K04486  histidinol-phosphatase (PHP family)
            KO: K05602  histidinol-phosphatase
GENES       SCE: YFR025C(HIS2)
            AGO: AGOS_AEL022W
            PIC: PICST_33066(HIS9)
            CAL: CaO19.6699(HIS2)
            CGR: CAGL0I09009g
            SPO: SPCp023
            ANI: AN7044.2
            AFM: AFUA_4G04030
            AOR: AO090010000720 AO090206000105
            CNE: CNC04790
            UMA: UM03583.1
            ECO: b2022(hisB)
            ECJ: JW2004(hisB)
            ECE: Z3184(hisB)
            ECS: ECs2823
            ECC: c2549(hisB)
            ECI: UTI89_C2295(hisB)
            ECP: ECP_2065
            ECW: EcE24377A_2313(hisB)
            ECX: EcHS_A2161(hisB)
            STY: STY2283(hisB)
            STT: t0799(hisB)
            SPT: SPA0797(hisB)
            SEC: SC2084(hisB)
            STM: STM2074(hisB)
            YPE: YPO1546(hisB)
            YPK: y2623(hisB)
            YPM: YP_1435(hisB1)
            YPA: YPA_0842
            YPN: YPN_2433
            YPP: YPDSF_1430
            YPS: YPTB1559(hisB)
            YPI: YpsIP31758_2431(hisB)
            SFL: SF2084(hisB)
            SFX: S2205(hisB)
            SFV: SFV_2082(hisB)
            SSN: SSON_2093(hisB)
            SBO: SBO_0848(hisB)
            SDY: SDY_2219(hisB)
            ECA: ECA2585(hisB)
            PLU: plu1568(hisB)
            BUC: BU102(hisB)
            BAS: BUsg095(hisB)
            BAB: bbp096(hisB)
            BCC: BCc_066(hisB)
            SGL: SG1127
            ENT: Ent638_2634
            SPE: Spro_1613
            BFL: Bfl465(hisB)
            BPN: BPEN_480(hisB)
            HIN: HI0471(hisB)
            HIT: NTHI0602(hisB)
            PMU: PM1200(hisB)
            MSU: MS1890(hisB)
            APL: APL_2023(hisB)
            ASU: Asuc_0634
            XFA: XF2217
            XFT: PD1265(hisB)
            XCC: XCC1811(hisB)
            XCB: XC_2378
            XCV: XCV1877(hisB)
            XAC: XAC1831(hisB)
            XOO: XOO2258(hisB)
            XOM: XOO_2121(XOO2121)
            VCH: VC1135
            VVU: VV1_2917
            VVY: VV1353
            VPA: VP1140
            VFI: VF1015
            PPR: PBPRA1089
            PAU: PA14_00070
            PEN: PSEEN0015 PSEEN5195(hisB)
            ACI: ACIAD3395(hisB)
            SON: SO_2071(hisB)
            SDN: Sden_1615
            SFR: Sfri_1717
            SAZ: Sama_1944
            SBL: Sbal_2428
            SBM: Shew185_2421
            SLO: Shew_2200
            SPC: Sputcn32_2181
            SSE: Ssed_2544
            SPL: Spea_2459
            SHE: Shewmr4_1797
            SHM: Shewmr7_2180
            SHN: Shewana3_1851
            SHW: Sputw3181_1828
            ILO: IL1837(hisB)
            CPS: CPS_3892(hisB)
            PHA: PSHAb0491(hisB)
            PAT: Patl_2883
            PIN: Ping_1654
            LPN: lpg1197
            LPF: lpl1205(hisB)
            LPP: lpp1199(hisB)
            NOC: Noc_0374
            AHA: AHA_2193
            BCI: BCI_0402(hisB)
            CVI: CV_1657
            BUR: Bcep18194_A6030
            BAM: Bamb_2755
            HAR: HEAR0374
            MMS: mma_0424
            HHE: HH1714
            WSU: WS0471
            TDN: Tmden_1866
            CJE: Cj1599(hisB)
            CJR: CJE1771(hisB)
            CJU: C8J_1501(hisB)
            ABU: Abu_1904(hisJ)
            NIS: NIS_1518
            SUN: SUN_0354
            DVU: DVU2490
            DDE: Dde_1057(hisJ)
            LIP: LI0725(hisB)
            DPS: DP0093 DP2888
            BRA: BRADO5205
            BBT: BBta_5672
            NWI: Nwi_1067
            MMR: Mmar10_1614
            RRU: Rru_A3564
            MGM: Mmc1_1555
            BSU: BG13931(hisJ)
            BHA: BH3206
            BAN: BA1432
            BAR: GBAA1432
            BAA: BA_1953 BA_2730
            BAT: BAS1324 BAS2071
            BCE: BC1413 BC2182
            BCA: BCE_1533 BCE_2256
            BCZ: BCZK1298(hisK)
            BTK: BT9727_1297(hisK)
            BLI: BL00372(hisJ)
            BLD: BLi03106(hisJ)
            BCL: ABC0751 ABC1953 ABC2752(hisJ)
            BAY: RBAM_026550(hisJ)
            BPU: BPUM_2607(hisK)
            OIH: OB0554
            GKA: GK2248 GK2799
            LMO: lmo0570(hisJ)
            LMF: LMOf2365_0599(hisK)
            LIN: lin0579(hisJ)
            LWE: lwe0536(hisJ)
            LLA: L37351(hisK)
            LLC: LACR_1325
            LLM: llmg_1288(hisK)
            SGO: SGO_1401
            LPL: lp_2563(hisK)
            LCA: LSEI_1206
            STH: STH2574
            CAC: CAC2727
            CPF: CPF_1229 CPF_1312(hisK) CPF_2137
            CPR: CPR_1128(hisK) CPR_1849
            CTC: CTC01046
            CNO: NT01CX_0001 NT01CX_0128
            CTH: Cthe_0724
            CDF: CD0737(hisK)
            CBA: CLB_2512(hisK)
            CBH: CLC_2443(hisK)
            CBF: CLI_2634(hisK)
            CBE: Cbei_2106
            CKL: CKL_1305(hisK)
            CHY: CHY_2084(hisJ)
            DSY: DSY1025 DSY2929
            DRM: Dred_0665
            SWO: Swol_0653
            CSC: Csac_2251
            TTE: TTE2610(his2.2)
            MTA: Moth_0817(hisJ)
            RXY: Rxyl_2572
            FNU: FN0428
            BTH: BT_0203(hisB) BT_1478
            BFR: BF1583 BF3187(hisB)
            BFS: BF1597 BF3027(hisB)
            CHU: CHU_1270(hisB) CHU_1575(hisB)
            GFO: GFO_1761(hisB)
            FJO: Fjoh_2875
            FPS: FP0957(hisB)
            CCH: Cag_1807
            PLT: Plut_0221
            DRA: DR_0470
            DGE: Dgeo_1608
            TTH: TTC1652
            TTJ: TTHA0331
            TMA: TM0804
            TPT: Tpet_0124
            MBU: Mbur_1333
            PTO: PTO1332(hisF)
STRUCTURES  PDB: 2FPR  2FPS  2FPU  2FPW  2FPX  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.15
            ExPASy - ENZYME nomenclature database: 3.1.3.15
            ExplorEnz - The Enzyme Database: 3.1.3.15
            ERGO genome analysis and discovery system: 3.1.3.15
            BRENDA, the Enzyme Database: 3.1.3.15
            CAS: 9025-79-0
///
ENTRY       EC 3.1.3.16                 Enzyme
NAME        phosphoprotein phosphatase;
            protein phosphatase-1;
            protein phosphatase-2A;
            protein phosphatase-2B;
            protein phosphatase-2C;
            protein D phosphatase;
            phosphospectrin phosphatase;
            casein phosphatase;
            Aspergillus awamori acid protein phosphatase;
            calcineurin;
            phosphatase 2A;
            phosphatase 2B;
            phosphatase II;
            phosphatase IB;
            phosphatase C-II;
            polycation modulated (PCM-) phosphatase;
            phosphopyruvate dehydrogenase phosphatase;
            phosphatase SP;
            branched-chain alpha-keto acid dehydrogenase phosphatase;
            BCKDH phosphatase;
            3-hydroxy 3-methylglutaryl coenzymeA reductase phosphatase;
            HMG-CoA reductase phosphatase;
            phosphatase H-II;
            phosphatase III;
            phosphatase I;
            protein phosphatase;
            phosphatase IV
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     phosphoprotein phosphohydrolase
REACTION    a phosphoprotein + H2O = a protein + phosphate [RN:R00164]
ALL_REAC    R00164
SUBSTRATE   phosphoprotein [CPD:C00562];
            H2O [CPD:C00001]
PRODUCT     protein [CPD:C00017];
            phosphate [CPD:C00009]
COFACTOR    Calcium [CPD:C00076];
            Calmodulin [CPD:C00391]
INHIBITOR   Tacrolimus [CPD:C01375];
            Okadaic acid [CPD:C01945];
            Cyclosporin A [CPD:C05086];
            Calyculin A [CPD:C05370];
            Microcystin-LR [CPD:C05371];
            Tautomycin [CPD:C05372]
COMMENT     A group of enzymes removing the serine- or threonine-bound phosphate
            group from a wide range of phosphoproteins, including a number of
            enzymes that have been phosphorylated under the action of a kinase
            (cf. EC 3.1.3.48 protein-tyrosine-phosphatase). The spleen enzyme
            also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1
            phosphoamidase)
REFERENCE   1  [PMID:2993239]
  AUTHORS   Deutscher J, Kessler U, Hengstenberg W.
  TITLE     Streptococcal phosphoenolpyruvate: sugar phosphotransferase system:
            purification and characterization of a phosphoprotein phosphatase
            which hydrolyzes the phosphoryl bond in seryl-phosphorylated
            histidine-containing protein.
  JOURNAL   J. Bacteriol. 163 (1985) 1203-9.
  ORGANISM  Streptococcus faecalis
REFERENCE   2  [PMID:6301824]
  AUTHORS   Ingebritsen TS, Cohen P.
  TITLE     The protein phosphatases involved in cellular regulation. 1.
            Classification and substrate specificities.
  JOURNAL   Eur. J. Biochem. 132 (1983) 255-61.
  ORGANISM  mammalian
REFERENCE   3
  AUTHORS   Sundarajan, T.A. and Sarma, P.S.
  TITLE     Substrate specificity of phosphoprotein phosphatase from spleen.
  JOURNAL   Biochem. J. 71 (1959) 537-544.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:6092084]
  AUTHORS   Tonks NK, Cohen P.
  TITLE     The protein phosphatases involved in cellular regulation.
            Identification of the inhibitor-2 phosphatases in rabbit skeletal
            muscle.
  JOURNAL   Eur. J. Biochem. 145 (1984) 65-70.
  ORGANISM  rabbit
PATHWAY     PATH: map04010  MAPK signaling pathway
            PATH: map04020  Calcium signaling pathway
            PATH: map04115  p53 signaling pathway
            PATH: map04210  Apoptosis
            PATH: map04310  Wnt signaling pathway
            PATH: map04350  TGF-beta signaling pathway
            PATH: map04360  Axon guidance
            PATH: map04370  VEGF signaling pathway
            PATH: map04510  Focal adhesion
            PATH: map04530  Tight junction
            PATH: map04650  Natural killer cell mediated cytotoxicity
            PATH: map04660  T cell receptor signaling pathway
            PATH: map04662  B cell receptor signaling pathway
            PATH: map04720  Long-term potentiation
            PATH: map04730  Long-term depression
            PATH: map04910  Insulin signaling pathway
ORTHOLOGY   KO: K01090  protein phosphatase
            KO: K04348  protein phosphatase 3, catalytic subunit
            KO: K04382  protein phosphatase 2 (formerly 2A), catalytic subunit
            KO: K04457  protein phosphatase 1A (formerly 2C)
            KO: K04459  dual specificity phosphatase
            KO: K04460  protein phosphatase 5
            KO: K04461  protein phosphatase 1B (formerly 2C)
            KO: K06269  protein phosphatase 1, catalytic subunit
            KO: K06382  stage II sporulation protein E
            KO: K07313  serine/threonine protein phosphatase 1
            KO: K07314  serine/threonine protein phosphatase 2
            KO: K10147  protein phosphatase 1D (formerly 2C)
GENES       HSA: 11072(DUSP14) 11221(DUSP10) 11266(DUSP12) 128853(DUSP15)
                 132160(PPM1M) 134510(UBLCP1) 142679(DUSP19) 150290(DUSP18)
                 1843(DUSP1) 1844(DUSP2) 1845(DUSP3) 1846(DUSP4) 1847(DUSP5)
                 1848(DUSP6) 1849(DUSP7) 1850(DUSP8) 1852(DUSP9) 22843(PPM1E)
                 23035(PHLPPL) 23239(PHLPP) 28227(PPP2R3B) 51207(DUSP13)
                 5470(PPEF2) 5475(PPEF1) 5494(PPM1A) 5495(PPM1B) 5496(PPM1G)
                 5499(PPP1CA) 5500(PPP1CB) 5501(PPP1CC) 5515(PPP2CA)
                 5516(PPP2CB) 5523(PPP2R3A) 5530(PPP3CA) 5531(PPP4C)
                 5532(PPP3CB) 5533(PPP3CC) 5536(PPP5C) 5537(PPP6C)
                 58190(CTDSP1) 63904(DUSP21) 7957(EPM2A) 80824(DUSP16)
                 84152(PPP1R1B) 8493(PPM1D) 8555(CDC14B) 8556(CDC14A)
                 9150(CTDP1) 9647(PPM1F)
            PTR: 454803(PPM1D) 460715(PPP2R3A) 462795(PPP1CC) 464100(PPP2CB)
                 464497(DUSP4) 465251(CDC14B) 465297(DUSP16) 468271(DUSP3)
                 468424(PPM1E) 468563(PHLPP) 469145(DUSP10) 470826(DUSP7)
                 471202(PPEF2) 471742(DUSP1) 472712(SORBS3)
            MMU: 13537(Dusp2) 13853(Epm2a) 14208(Ppm1g) 18218(Dusp8)
                 19023(Ppef2) 19042(Ppm1a) 19043(Ppm1b) 19045(Ppp1ca)
                 19046(Ppp1cb) 19047(Ppp1cc) 19052(Ppp2ca) 19053(Ppp2cb)
                 19055(Ppp3ca) 19056(Ppp3cb) 19057(Ppp3cc) 19060(Ppp5c)
                 19252(Dusp1) 218294(Cdc14b) 227292(Ctdsp1) 229776(Cdc14a)
                 235542(3222402P14Rik) 235584(Dusp7) 237178(Ppef1)
                 240672(Dusp5) 244650(Phlppl) 252864(Dusp15) 27389(Dusp13)
                 319520(Dusp4) 320472(Ppm1e) 53892(Ppm1d) 56405(Dusp14)
                 56420(Ppp4c) 63953(Dusp10) 67603(Dusp6) 67655(Ctdp1)
                 67857(Ppp6c) 67905(Ppm1m) 68082(Dusp19) 68606(Ppm1f)
                 70686(Dusp16) 72349(Dusp3) 75219(Dusp18) 75590(Dusp9)
                 79560(Ublcp1) 80915(Dusp12) 98432(Phlpp)
            RNO: 114856(Dusp1) 116663(Dusp6) 171109(Dusp5) 171121(Ppp6c)
                 171378(Ppp3cc) 24666(Ppm1a) 24667(Ppm1b) 24668(Ppp1ca)
                 24669(Ppp1cc) 24672(Ppp2ca) 24673(Ppp2cb) 24674(Ppp3ca)
                 24675(Ppp3cb) 25594(Ppp1cb) 259229(Ppm1g)
                 287585(Ppm1d_predicted) 287931(Ppm1f) 293847(Dusp9)
                 300980(Dusp7) 305246(Ppef2_predicted) 310806(Cdc14a_predicted)
                 311151(Dusp19_predicted) 317498(Ppef1) 360514(Ublcp1)
                 360593(Ppm1e) 361195(Cdc14b_predicted) 363122(Ppp2r3a)
                 363249(Ctdsp1) 59265(Phlpp) 60587(Dusp4)
                 63995(Dusp10_predicted) 64014(Dusp12) 65179(Ppp5c)
            CFA: 403486(PPP3CA) 403557(PPP1CC) 403558(PPP1CB) 403608(PPP2CA)
                 403609(PPP1CA) 475703(PPM1G) 476179(PHLPP) 476294(CDC14B)
                 479248(PPP3CB) 480344(PPM1A) 480505(DUSP3) 482594(DUSP6)
                 482873(PPP2CB) 482880(DUSP4) 483660(LOC483660) 484022(EPM2A)
                 484739(LOC484739) 484742(DUSP7) 485672(PPP2R3A) 486357(DUSP18)
                 486448(PPM1F) 486683(DUSP16) 486884(DUSP5) 487812(PPEF2)
                 488433(DUSP19) 488673(DUSP10) 489117(DUSP1) 489724(PHLPPL)
                 489947(PPP4C) 491131(DUSP14) 492240(DUSP9) 607103(PPP2R3B)
                 608466(CTDSP1) 609027(PPP3CC) 611653(DUSP2) 612199(PPP5C)
                 612897(PPM1E) 612934(PPM1D)
            BTA: 281994(PPM1A) 281995(PPM1B) 282318(PPP1CC) 282320(PPP2CA)
                 286852(PPP3CA) 286880(PPM1G) 508163(MGC128319) 516175(PPP1CA)
                 538829(MGC129042) 540398(MGC166039) 614306(LOC614306)
            SSC: 397241(PPP3CA) 397378(PPP1CB) 397589(CDKN3) 397656(PPP2CA)
            GGA: 374192(DUSP1) 374272(DUSP6) 378890(RCJMB04_24n15)
                 395113(PPP3CA) 395642(DUSP4) 396019(PPP1CB) 396021(PPP2CB)
                 415881(PHLPPL) 415941(RCJMB04_2e20) 416237(RCJMB04_17j14)
                 416318(PPP2CA) 416772(PPM1F) 416872(PPP1CC) 417005(DUSP18)
                 417627(PPM1E) 417644(PPM1D) 417657(DUSP14) 418670(PPP2R3B)
                 420904(PHLPP) 421340(RCJMB04_18i8) 421404(RCJMB04_26p17)
                 421611(RCJMB04_7n21) 422640(PPEF2) 423525(PPM1A) 423890(DUSP5)
                 423999(DUSP19) 424733(PPP2R3A) 425349(DUSP12) 425527(DUSP3)
                 427473(CDC14B) 770435(DUSP8) 772354(RCJMB04_23h2)
            XLA: 379914(ppp1ca) 379993(ppm1g) 380045(ppp2ca) 380058(ppm1a)
                 380507(ppp3ca) 380598(ppp1cc) 397767(LOC397767) 398004(PP5)
                 398829(MGC68682) 399343(Ppp2cb) 403393(CDC14a)
                 432106(MGC81043) 432133(MGC80245) 432334(MGC78774)
                 443852(MGC79074) 443988(MGC80458) 444752(MGC84792)
                 447196(MGC79144) 495060(LOC495060)
            XTR: 394540(ppp4c) 394888(ppp2ca) 407879(ppp1cc)
                 448031(TEgg040c14.1) 448043(dusp1) 493275(ppp5c) 493392(ppm1b)
                 496958(LOC496958) 733814(dusp7)
            DRE: 30704(pp2ca2) 325708(ppp4c) 327246(dusp7) 327301(zgc:76940)
                 353314(dusp6) 368275(ppm1g) 368904(ppp1cb) 393885(zgc:56064)
                 393980(ppp6c) 394124(zgc:63654) 394146(zgc:55423)
                 406340(dusp1) 406523(zgc:77247) 407980(zgc:85729)
                 436591(ublcp1) 492468(zgc:103518) 550437(zgc:112536)
                 562705(LOC562705) 573730(LOC573730)
            SPU: 574724(LOC574724) 576159(LOC576159) 576623(LOC576623)
                 579231(LOC579231) 580852(LOC580852) 582153(LOC582153)
                 582330(LOC582330) 584461(LOC584461) 585369(LOC585369)
                 585672(LOC585672) 586142(LOC586142) 586442(LOC586442)
                 586673(LOC586673) 587147(LOC587147) 589648(LOC589648)
                 590781(LOC590781) 592155(LOC592155) 594091(LOC594091)
                 594644(LOC594644) 752338(LOC752338)
            DME: Dmel_CG10138(PpD5) Dmel_CG10417 Dmel_CG10930(PpY-55A)
                 Dmel_CG12151 Dmel_CG12217(PpV) Dmel_CG14080(Mkp3) Dmel_CG14211
                 Dmel_CG1455(CanA1) Dmel_CG15528 Dmel_CG17746 Dmel_CG2096(flw)
                 Dmel_CG2984(Pp2C1) Dmel_CG32156(Mbs) Dmel_CG3245(PpN58A)
                 Dmel_CG32505(Pp4-19C) Dmel_CG4123(Mipp1) Dmel_CG5650(Pp1-87B)
                 Dmel_CG5830 Dmel_CG6235(tws) Dmel_CG6571(rdgC)
                 Dmel_CG6593(Pp1alpha-96A) Dmel_CG6896(MYPT-75D)
                 Dmel_CG7109(mts) Dmel_CG7850(puc) Dmel_CG8402(PpD3)
                 Dmel_CG8822(PpD6) Dmel_CG9156(Pp1-13C) Dmel_CG9764(yrt)
                 Dmel_CG9819(CanA-14F) Dmel_CG9842(Pp2B-14D)
            CEL: C04F12.8 C05A2.1(pph-1) C06A1.3 C09H5.7(phophatase) C23G10.1
                 C24H11.1 C24H11.2 C27B7.6 C34C12.3(pph-6) C34D4.2 C47A4.3
                 F08B1.1(vhp-1) F20D6.6 F22D6.9 F23B12.1 F23H11.8(pef-1)
                 F25B3.4 F26B1.5 F29F11.6(gsp-1) F38H4.9(let-92) F40E3.5
                 F42G8.8 F42G9.1 F49E11.7 F52H3.6 F56C9.1(gsp-2) F58G1.3
                 R03D7.8 R08A2.2 R08C7.8 R13A5.11 T03F1.5(gsp-4) T16G12.7
                 T19C3.8(fem-2) T23F11.1(phosphatase) T25B9.2 W03D8.2
                 W09C3.6(gsp-3) Y39B6A.2(pph-5) Y40H4A.2 Y69E1A.4
                 Y75B8A.30(pph-4.1) ZC477.2 ZK354.9 ZK938.1
            ATH: AT1G10430(PP2A-2) AT1G50370 AT1G59830(PP2A-1)
                 AT1G64040(TOPP3) AT1G69960(PP2A) AT2G25070 AT3G05580
                 AT3G19980(ATFYPP3) AT3G46820(TOPP5) AT3G58500(PP2A-3)
                 AT4G03080 AT4G26080(ABI1) AT5G19280(KAPP) AT5G51760
                 AT5G55260(PPX2) AT5G57050(ABI2) AT5G59220
            OSA: 4325641 4328505 4328734 4331166 4332369 4334494 4334526
                 4337723 4337785 4338070 4340228 4340847 4341364 4341433
                 4341693 4346619
            CME: CMD083C CME079C CML332C CMP075C CMS179C
            SCE: YBL056W(PTC3) YBR125C(PTC4) YDL006W(PTC1) YDL047W(SIT4)
                 YDL134C(PPH21) YDL188C(PPH22) YDR075W(PPH3) YDR436W(PPZ2)
                 YER089C(PTC2) YER133W(GLC7) YGR123C(PPT1) YLR433C(CNA1)
                 YML016C(PPZ1) YML057W(CMP2) YMR277W(FCP1) YNR032W(PPG1)
                 YPL179W(PPQ1)
            AGO: AGOS_AAR083C AGOS_ACR239C AGOS_ADL377W AGOS_ADR099C
                 AGOS_AEL010W AGOS_AER118C AGOS_AER202C AGOS_AER265W
                 AGOS_AER334C AGOS_AFL051W AGOS_AFR166C
            PIC: PICST_37600(GAC2) PICST_43575 PICST_50823(MCO15)
                 PICST_52303(KEL2) PICST_56574 PICST_61419 PICST_68058
                 PICST_70660 PICST_81748(TOM70) PICST_81790 PICST_85252(GLC7)
                 PICST_85643 PICST_85954(PPG1) PICST_89530(GAC1) PICST_90276
            CAL: CaO19.6285(glc7) CaO19_1673(CaO19.1673)
                 CaO19_1683(CaO19.1683) CaO19_6033(CaO19.6033)
            CGR: CAGL0A04301g CAGL0C01507g CAGL0C04499g CAGL0D05060g
                 CAGL0F03223g CAGL0H04851g CAGL0I03938g CAGL0I05038g
                 CAGL0J09834g CAGL0K01331g CAGL0K02079g CAGL0K10208g
                 CAGL0L11110g CAGL0M10890g
            SPO: SPAC10F6.17c SPAC22H10.04 SPAC2G11.07c(ptc3) SPAC2G11.15c
                 SPAC57A7.08(phz1) SPAC823.15(ppa1) SPBC16H5.07c(ppa2)
                 SPBC17A3.06 SPBC26H8.05c SPBC3F6.01c SPBC776.02c(dis2)
                 SPBP4H10.04(ppb1) SPCC1223.11(ptc2) SPCC1739.12(ppe1)
                 SPCC31H12.05c(sds21) SPCC4F11.02(ptc1)
            ANI: AN0103.2 AN0164.2 AN0410.2 AN0504.2 AN1358.2 AN3793.2
                 AN6391.2 AN6892.2
            AFM: AFUA_1G04950 AFUA_1G09280 AFUA_1G09830 AFUA_2G03950
                 AFUA_4G00720 AFUA_5G06700 AFUA_5G08620 AFUA_5G09360
                 AFUA_5G11370 AFUA_5G13340 AFUA_5G13740 AFUA_6G10830
                 AFUA_6G11470
            AOR: AO090005001522 AO090005001595 AO090012000155 AO090020000552
                 AO090023000433 AO090026000701 AO090120000320 AO090120000479
                 AO090701000208 AO090701000351
            CNE: CNA03970 CNA04830 CNB01720 CNB02030 CNC00360 CNC06840
                 CND05500 CNE03050 CNE03610 CNJ02230
            UMA: UM01391.1 UM02303.1 UM02445.1 UM03080.1 UM03957.1 UM04320.1
                 UM04827.1 UM05193.1
            ECU: ECU04_0700 ECU09_0980(pp1-1) ECU10_1280 ECU11_0660
            DDI: DDBDRAFT_0185382 DDBDRAFT_0185403 DDBDRAFT_0185918
                 DDBDRAFT_0205052 DDB_0185021(canA) DDB_0185058(pppB)
                 DDB_0185210(pppD) DDB_0185222(pppC) DDB_0191299(pho2A)
            PFA: MAL13P1.274 MAL13P1.44 MAL3P5.5 MAL8P1.108 PF08_0129
                 PF11_0139 PF11_0396 PF14_0142 PF14_0224 PF14_0523 PFE0455w
                 PFI1245c PFI1360c
            CPV: cgd3_2020 cgd6_4200 cgd7_810
            CHO: Chro.10265 Chro.20310 Chro.30238 Chro.50440 Chro.60481
                 Chro.70100 Chro.70303 Chro.70393
            TAN: TA08350 TA12680 TA12800 TA12805 TA15515 TA15545 TA15975
                 TA19470 TA19895
            TPV: TP02_0042 TP02_0350 TP02_0853 TP02_0861 TP02_0944 TP04_0410
                 TP04_0423 TP04_0474
            TET: TTHERM_00040430 TTHERM_00046430 TTHERM_00088160
                 TTHERM_00088170 TTHERM_00112800 TTHERM_00114370
                 TTHERM_00161460 TTHERM_00185500 TTHERM_00189500
                 TTHERM_00250870 TTHERM_00378510 TTHERM_00378520
                 TTHERM_00389660 TTHERM_00446510 TTHERM_00532720
                 TTHERM_00585480 TTHERM_00623060 TTHERM_00624140
                 TTHERM_00686110 TTHERM_00688720 TTHERM_00697520
                 TTHERM_00794350 TTHERM_00804750 TTHERM_00841340
                 TTHERM_00865300 TTHERM_00899570 TTHERM_01004940
                 TTHERM_01055570 TTHERM_01107320 TTHERM_01125140
                 TTHERM_01289010 TTHERM_01345810
            TBR: Tb09.160.0480 Tb10.05.0110 Tb10.70.0250 Tb10.70.0350
                 Tb10.70.1410 Tb10.70.2270 Tb11.01.0450 Tb11.01.3770
                 Tb11.01.4320 Tb11.01.6540 Tb11.01.8740 Tb11.03.0390
                 Tb927.2.5050 Tb927.3.1240 Tb927.4.1870 Tb927.4.2110
                 Tb927.4.3560 Tb927.4.3610 Tb927.4.3620 Tb927.4.3630
                 Tb927.4.3640 Tb927.4.4510 Tb927.4.5030 Tb927.5.1660
                 Tb927.5.4380 Tb927.6.1800 Tb927.7.4020 Tb927.8.7390
            TCR: 420989.10 438059.10 504013.110 506201.30 506201.70 506221.30
                 506315.100 506559.530 506739.200 507601.10 507671.39
                 507993.190 508413.40 508815.110 509029.10 509453.50 510187.400
                 510187.500 510291.30 510351.150 510687.40 510755.138 510879.10
                 511021.10 511127.400 511211.60 511277.630 511491.100 511537.40
                 511881.20
            LMA: LmjF05.0100 LmjF08.0100 LmjF09.0470 LmjF14.0900 LmjF15.0170
                 LmjF18.0150 LmjF25.0750 LmjF25.1320 LmjF26.2530 LmjF28.0690
                 LmjF28.2670 LmjF30.0380 LmjF31.2630 LmjF32.1690 LmjF32.3040
                 LmjF34.0810 LmjF34.0850 LmjF34.2510 LmjF34.2770 LmjF34.4190
                 LmjF36.0530 LmjF36.1980 LmjF36.2050
            EHI: 101.t00013 107.t00002 142.t00019 15.t00037 156.t00006
                 157.t00022 159.t00006 16.t00005 17.t00013 183.t00006
                 185.t00009 2.t00016 2.t00018 2.t00060 202.t00013 204.t00018
                 26.t00028 260.t00008 318.t00006 33.t00008 4.t00016 43.t00014
                 5.t00022 5.t00051 51.t00010 52.t00016 56.t00041 60.t00035
                 63.t00008 69.t00006 83.t00018 84.t00008 9.t00086 90.t00028
                 92.t00028 95.t00023
            ECO: b1838(pphA) b2734(pphB)
            ECJ: JW1827(pphA) JW2704(pphB)
            ECE: Z2885(pphA) Z3933 Z4044(pphB)
            ECS: ECs0813 ECs2548 ECs3590
            ECC: c2247(pphA) c3295(pphB)
            ECI: UTI89_C2039(pphA)
            ECP: ECP_1782 ECP_2712
            ECV: APECO1_3790(pphB) APECO1_4021 APECO1_891(pphA)
            ECW: EcE24377A_2067(pphA) EcE24377A_3031(pphB)
            ECX: EcHS_A1929 EcHS_A2872
            STY: STY1984(pphA) STY3030
            STT: t1025(pphA) t2807
            SPT: SPA1020(pphA)
            SEC: SC1849(prpA) SC2836(pphB)
            STM: STM1853(prpA) STM2907(pphB)
            YEN: YE3016
            SBO: SBO_1253(pphA) SBO_2786(pphB)
            HIT: NTHI1635
            MSU: MS0548(apaH)
            XFA: XF2156
            XFT: PD1216
            XCC: XCC0989
            XCB: XC_3254
            XCV: XCV1091(pppL) XCV2140 XCV4207
            XAC: XAC1091 XAC4117(ptc1)
            XOO: XOO1045 XOO3036(ptc1)
            XOM: XOO_0942(XOO0942) XOO_2889(XOO2889)
            VVU: VV2_0038 VV2_0439
            VVY: VVA0546 VVA0989
            VPA: VPA1037
            VFI: VF0991
            PPR: PBPRA0664
            PAE: PA1670(stp1)
            PAU: PA14_00890 PA14_42890(stp1)
            PPU: PP_3020
            PST: PSPTO_5417
            PFL: PFL_6079
            PFO: Pfl_5576
            PEN: PSEEN0536(stp1) PSEEN3165
            PCR: Pcryo_0944
            SFR: Sfri_2371
            CPS: CPS_3671
            SDE: Sde_1774
            CBU: CBU_0488
            NOC: Noc_0594 Noc_1730
            AEH: Mlg_0525
            HCH: HCH_01953 HCH_04296 HCH_04849
            CVI: CV_2188(pphA)
            REU: Reut_A2423
            REH: H16_A2091 H16_A2682
            RME: Rmet_2562
            BXE: Bxe_B0477 Bxe_B2858
            BUR: Bcep18194_B2251
            BCH: Bcen2424_3845
            BPS: BPSS1819
            BPM: BURPS1710b_A0903(pphA)
            BTE: BTH_II0558
            BPE: BP0904(pphA)
            BPA: BPP1630(pphA)
            BBR: BB3098(pphA)
            RFR: Rfer_3941
            POL: Bpro_4678
            PNA: Pnap_3950
            AJS: Ajs_4044
            MPT: Mpe_A0068
            HAR: HEAR2127 HEAR2621
            MMS: mma_2858
            NMU: Nmul_A1997
            EBA: ebA1663
            AZO: azo3331(pppL)
            DAR: Daro_0437 Daro_3360
            GSU: GSU2630
            GME: Gmet_0841
            PCA: Pcar_0412
            BBA: Bd0397
            DPS: DP2574
            MXA: MXAN_2044(pph1) MXAN_5349
            SFU: Sfum_1247
            RFE: RF_0259
            MLO: mll6908 mlr2361
            SME: SMb21213(pphA)
            ATU: Atu3542(prp1)
            ATC: AGR_L_2581
            RET: RHE_CH03239 RHE_CH03362(ypch01177)
            RLE: RL3129 RL3668 RL3788
            BJA: bll2356(prp1)
            BRA: BRADO7062
            BBT: BBta_1036
            RPA: RPA3353
            RPE: RPE_1083
            NWI: Nwi_3015
            CCR: CC_0168
            SIL: SPO3358
            SIT: TM1040_3022
            RSP: RSP_1353 RSP_3492
            RSH: Rsph17029_3136
            MMR: Mmar10_0167
            HNE: HNE_2798
            GOX: GOX2002
            GBE: GbCGDNIH1_0900
            RRU: Rru_A1488 Rru_A3111
            MAG: amb0777 amb1449
            MGM: Mmc1_3143
            ABA: Acid345_1977 Acid345_4330
            BSU: BG10127(spoIIE) BG12441(rsbP) BG13390(prpC)
            BHA: BH0078(spoIIE) BH2505
            BAN: BA0061(spoIIE) BA0570 BA1217 BA3071 BA4001
            BAR: GBAA0061(spoIIE) GBAA0570 GBAA1217 GBAA3071 GBAA4001
            BAA: BA_0651 BA_1150 BA_1753 BA_2584 BA_3578 BA_4472
            BAT: BAS0061 BAS0539 BAS1124 BAS1941 BAS2857 BAS3714
            BCE: BC0069 BC0571 BC1202 BC2070 BC3047 BC3861
            BCA: BCE_0060(spoIIE) BCE_0633 BCE_1324 BCE_2172 BCE_3099 BCE_3905
            BCZ: BCZK0057(spoIIE) BCZK0483(pphA) BCZK1099(prpA) BCZK1892
                 BCZK2789(prpA) BCZK3622
            BCY: Bcer98_0057
            BTK: BT9727_0057(spoIIE) BT9727_0481(pphA) BT9727_1105(prpA)
                 BT9727_1902 BT9727_1903 BT9727_2829(prpA) BT9727_3604
            BTL: BALH_0060(spoIIE) BALH_0510(pphA) BALH_1064(prpA)
                 BALH_2741(prpA) BALH_3494
            BLI: BL00506(spoIIE) BL02301(prpC)
            BLD: BLi00080(spoIIE) BLi00557(rsbU) BLi01797(prpC)
            BCL: ABC0101(spoIIE) ABC0813(rsbU) ABC2316(prpC)
            BAY: RBAM_000750(spoIIE)
            BPU: BPUM_0048(spoIIE) BPUM_1677
            OIH: OB0074 OB1508
            GKA: GK0057(spoIIE) GK0832 GK1175
            GTN: GTNG_1028
            SAU: SA1062
            SAV: SAV1219
            SAM: MW1102
            SAR: SAR1195
            SAS: SAS1153
            SAC: SACOL1231
            SAB: SAB1083 SAB1952c(rsbU)
            SAA: SAUSA300_1112
            SAO: SAOUHSC_01186
            SAJ: SaurJH9_1278
            SEP: SE0894
            SER: SERP0785 SERP1555
            SHA: SH1696
            SSP: SSP1553
            LMO: lmo0655 lmo1821
            LMF: LMOf2365_0686 LMOf2365_1849
            LIN: lin0658 lin1935
            LWE: lwe0623 lwe0874(rsbU) lwe1840
            LLA: L140754(pppL)
            LLC: LACR_2083 LACR_B1
            LLM: llmg_2080(pppL)
            SPY: SPy_1626(pppL)
            SPZ: M5005_Spy_1336(pppL)
            SPM: spyM18_1635
            SPG: SpyM3_1370(pppL)
            SPS: SPs0492
            SPH: MGAS10270_Spy1452(pppL)
            SPI: MGAS10750_Spy1445(pppL)
            SPJ: MGAS2096_Spy1357(pppL)
            SPK: MGAS9429_Spy1331(pppL)
            SPF: SpyM50455
            SPA: M6_Spy1382
            SPB: M28_Spy1377(pppL)
            SPN: SP_1201 SP_1733
            SPR: spr1083(pphA) spr1578(pppL)
            SPD: SPD_1543
            SAG: SAG0318
            SAN: gbs0306
            SAK: SAK_0388(stp1)
            SMU: SMU.483
            STC: str1426(pppL)
            STL: stu1426(pppL)
            STE: STER_1393
            SSA: SSA_0680(pphA) SSA_1846(pppL)
            SSU: SSU05_0427
            SSV: SSU98_0414
            SGO: SGO_0699
            LPL: lp_1618(pppL)
            LJO: LJ1538
            LAC: LBA1318
            LSA: LSA0691
            LSL: LSL_0616
            LDB: Ldb1410(pppL)
            LBU: LBUL_1307
            LBR: LVIS_0963
            LCA: LSEI_0167 LSEI_1623
            LGA: LGAS_0763
            LRE: Lreu_1170
            PPE: PEPE_0831
            EFA: EF1311 EF3121
            OOE: OEOE_0788
            LME: LEUM_1512
            STH: STH1352 STH3200(spoIIE) STH3301
            CAC: CAC1727 CAC2787 CAC3205(spoIIE)
            CPE: CPE1739 CPE2473(spoIIE)
            CPF: CPF_1992 CPF_2789(spoIIE)
            CPR: CPR_1710 CPR_2475
            CTC: CTC00201 CTC01224
            CNO: NT01CX_1037 NT01CX_2240
            CTH: Cthe_0573 Cthe_2681
            CDF: CD3490(spoIIE)
            CBA: CLB_3602(spoIIE)
            CBH: CLC_3491(spoIIE)
            CBF: CLI_3736(spoIIE)
            CBE: Cbei_0097
            AMT: Amet_0173
            CHY: CHY_0212 CHY_1479
            DSY: DSY0199 DSY2688
            DRM: Dred_0124 Dred_1711
            PTH: PTH_1784(PTC1)
            SWO: Swol_0093
            CSC: Csac_0117 Csac_2077
            TTE: TTE1501(ptc1) TTE2396(rsbU)
            MTA: Moth_0103
            MGE: MG_108
            MPN: MPN247(ptc1)
            MPU: MYPU_6860
            MPE: MYPE5620
            MGA: MGA_0461(ptc1)
            MMY: MSC_0308
            MMO: MMOB5580
            MSY: MS53_0122(prpC)
            MCP: MCAP_0264
            UUR: UU215(ptc1)
            MFL: Mfl220
            MTU: Rv0018c(ppp)
            MTC: MT0021
            MBO: Mb0018c(ppp)
            MBB: BCG_0048c(pstP)
            MLE: ML0020
            MPA: MAP0021c(ppp)
            MAV: MAV_0022
            MSM: MSMEG_0033
            MMC: Mmcs_0019
            CGL: NCgl0044(cgl0045)
            CGB: cg0062(ppp)
            CEF: CE0037
            CDI: DIP0057
            CJK: jk0041(ppp)
            RHA: RHA1_ro03700
            SCO: SCO3845(SCH69.15) SCO5973(StBAC16H6.08)
            SMA: SAV2323(prpA1) SAV4341(prpB8)
            TWH: TWT090
            TWS: TW100
            LXX: Lxx00250
            PAC: PPA0187
            TFU: Tfu_2592
            FRA: Francci3_4432
            FAL: FRAAL0280 FRAAL6751(pphA)
            SEN: SACE_6613(prpB8)
            BLO: BL0585
            BAD: BAD_0042
            RBA: RB5674 RB5905 RB8362(pph1)
            CTR: CT259
            CTA: CTA_0281
            CMU: TC0530
            CPN: CPn0397
            CPA: CP0358
            CPJ: CPj0397
            CPT: CpB0409
            CCA: CCA00399
            CAB: CAB386
            CFE: CF0608(pp2C)
            PCU: pc0720
            LIL: LA1428 LA4107(rsbP)
            LIC: LIC12319 LIC13273
            LBJ: LBJ_2180
            LBL: LBL_2174
            SYN: sll0602 sll1033 sll1387(pppA) sll1771(pphA)
            SYW: SYNW0913
            SYC: syc0419_c syc2163_c syc2500_d
            SYF: Synpcc7942_1130 Synpcc7942_1515 Synpcc7942_1931
            SYD: Syncc9605_1654
            SYG: sync_1056
            SYX: SynWH7803_1506
            CYA: CYA_0212
            CYB: CYB_0947
            TEL: tll0923 tll2421 tlr1644 tlr2243
            GVI: gll0589 gll2757
            ANA: all0373 all1731 all2470 alr0547 alr3731(prpA) alr4370 alr4516
            AVA: Ava_0304 Ava_0354 Ava_0402 Ava_1593 Ava_3306 Ava_3382
                 Ava_A0002
            PMT: PMT1090
            PMF: P9303_09581
            TER: Tery_0619 Tery_3297 Tery_3336
            BTH: BT_2772
            SRU: SRU_0016
            CHU: CHU_1580(pphA)
            FPS: FP0138(pphA)
            DRA: DR_0295 DR_2249
            DGE: Dgeo_0272
            TTH: TTC0111 TTC1231 TTC1510 TTC1799
            TTJ: TTHA0187 TTHA1595
            TMA: TM0742
            MMA: MM_0102 MM_0751 MM_1657
            HMA: pNG7301(pphA)
            NPH: NP0728A
            PTO: PTO0288 PTO1092
            RCI: RCIX1649
            APE: APE_0777
            SSO: SSO1090
            STO: ST2367
            SAI: Saci_0884
            PAI: PAE2004
STRUCTURES  PDB: 1A17  1A6Q  1AUI  1FJM  1HZM  1IT6  1JK7  1M3G  1M63  1MF8  
                 1MKP  1MZK  1S70  1S95  1T9Z  1TA0  1TCO  1TXO  1U32  1WAO  
                 1ZZW  2BCD  2BDX  2BUG  2CM1  2ESB  2FYS  2G6Z  2GHQ  2GHT  
                 2GWO  2IAE  2IE3  2IE4  2IMG  2JOG  2NPP  2NT2  2NYL  2NYM  
                 2O8A  2O8G  2OUC  2OUD  2P4D  2P8E  2PK0  2PQ5  2Q05  2Q5E  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.16
            ExPASy - ENZYME nomenclature database: 3.1.3.16
            ExplorEnz - The Enzyme Database: 3.1.3.16
            ERGO genome analysis and discovery system: 3.1.3.16
            BRENDA, the Enzyme Database: 3.1.3.16
            CAS: 9025-75-6
///
ENTRY       EC 3.1.3.17                 Enzyme
NAME        [phosphorylase] phosphatase;
            PR-enzyme;
            phosphorylase a phosphatase;
            glycogen phosphorylase phosphatase;
            protein phosphatase C;
            type 1 protein phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     [phosphorylase a] phosphohydrolase
REACTION    [phosphorylase a] + 4 H2O = 2 [phosphorylase b] + 4 phosphate
            [RN:R00077]
ALL_REAC    R00077
SUBSTRATE   [phosphorylase a] [CPD:C02307];
            H2O [CPD:C00001]
PRODUCT     [phosphorylase b] [CPD:C02308];
            phosphate [CPD:C00009]
REFERENCE   1  [PMID:240850]
  AUTHORS   Brandt H, Capulong ZL, Lee EY.
  TITLE     Purification and properties of rabbit liver phosphorylase
            phosphatase.
  JOURNAL   J. Biol. Chem. 250 (1975) 8038-44.
  ORGANISM  rabbit
REFERENCE   2  [PMID:13829077]
  AUTHORS   GRAVES DJ, FISCHER EH, KREBS EG.
  TITLE     Specificity studies on muscle phosphorylase phosphatase.
  JOURNAL   J. Biol. Chem. 235 (1960) 805-9.
  ORGANISM  rabbit
REFERENCE   3  [PMID:13315351]
  AUTHORS   RALL TW, WOSILAIT WD, SUTHERLAND EW.
  TITLE     The interconversion of phosphorylase a and phosphorylase b from dog
            heart muscle.
  JOURNAL   Biochim. Biophys. Acta. 20 (1956) 69-76.
  ORGANISM  dog [GN:cfa]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.17
            ExPASy - ENZYME nomenclature database: 3.1.3.17
            ExplorEnz - The Enzyme Database: 3.1.3.17
            ERGO genome analysis and discovery system: 3.1.3.17
            BRENDA, the Enzyme Database: 3.1.3.17
            CAS: 9025-74-5
///
ENTRY       EC 3.1.3.18                 Enzyme
NAME        phosphoglycolate phosphatase;
            phosphoglycolate hydrolase;
            2-phosphoglycolate phosphatase;
            P-glycolate phosphatase;
            phosphoglycollate phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     2-phosphoglycolate phosphohydrolase
REACTION    2-phosphoglycolate + H2O = glycolate + phosphate [RN:R01334]
ALL_REAC    R01334
SUBSTRATE   2-phosphoglycolate [CPD:C00988];
            H2O [CPD:C00001]
PRODUCT     glycolate [CPD:C00160];
            phosphate [CPD:C00009]
REFERENCE   1  [PMID:204630]
  AUTHORS   Christeller JT, Tolbert NE.
  TITLE     Phosphoglycolate phosphatase. Purification and properties.
  JOURNAL   J. Biol. Chem. 253 (1978) 1780-5.
  ORGANISM  spinach
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K01091  phosphoglycolate phosphatase
GENES       PIC: PICST_84214(SDT1)
            CAL: CaO19_3922(CaO19.3922)
            AFM: AFUA_7G00760
            ECO: b3385(gph)
            ECJ: JW3348(gph)
            ECE: Z4738(gph)
            ECS: ECs4227
            ECC: c4155(gph)
            ECI: UTI89_C3052(yqaB) UTI89_C3883(gph)
            ECP: ECP_3470
            ECV: APECO1_3078(gph)
            ECW: EcE24377A_3854(gph)
            ECX: EcHS_A3581(gph)
            STY: STY4314(gph)
            STT: t4025(gph)
            SPT: SPA3347(gph)
            SEC: SC3414(gph)
            STM: STM3482(gph)
            YPE: YPO0156(gph)
            YPK: y3939(gph)
            YPM: YP_0158(gph)
            YPA: YPA_3313
            YPN: YPN_3909
            YPP: YPDSF_0083
            YPS: YPTB3745(gph)
            YPI: YpsIP31758_3961(gph2)
            SFL: SF3403(gph)
            SFX: S4359(gph)
            SFV: SFV_3390(gph)
            SSN: SSON_3516(gph)
            SBO: SBO_3372(gph)
            SDY: SDY_3694(gph)
            ECA: ECA4088(gph)
            PLU: plu0085(gph)
            HIN: HI0565(gph)
            HIT: NTHI0697(gph)
            HDU: HD0176(gph)
            HSO: HS_0176(gph)
            PMU: PM1620(gph)
            MSU: MS2331(gph)
            APL: APL_1893(gph)
            XFA: XF2470
            XFT: PD1487
            XCC: XCC0584(gph) XCC2268(cbbZ)
            XCB: XC_0581 XC_1847 XC_3649
            XCV: XCV2573(cbbZ) XCV3739
            XAC: XAC2376(cbbZ) XAC3621(gph)
            XOO: XOO0764(gph) XOO2701(cbbZ)
            XOM: XOO_0694(XOO0694) XOO_2547(XOO2547)
            VCH: VC2624
            VCO: VC0395_A2201(gph)
            VVU: VV1_1306
            VVY: VV3059
            VPA: VP2805
            VFI: VF2287 VFA0937
            PPR: PBPRA0285 PBPRA1188 PBPRA2458(cbbZ)
            PAE: PA0065 PA0608 PA2974 PA3172
            PAU: PA14_00770 PA14_07930(gph) PA14_23210 PA14_25590
            PAP: PSPA7_0752(gph1) PSPA7_1957(gph2)
            PPU: PP_0094 PP_0416(gph) PP_1764 PP_1907
            PST: PSPTO_0567(gph-1) PSPTO_1741(gph-2) PSPTO_3839
            PSB: Psyr_1640 Psyr_3651 Psyr_4610(gph)
            PSP: PSPPH_0648(gph1) PSPPH_1634 PSPPH_3671(gph2)
            PFL: PFL_0048 PFL_1789 PFL_4318(gph) PFL_5630(gph)
            PFO: Pfl_0092 Pfl_4082 Pfl_4164 Pfl_5119(gph)
            PEN: PSEEN0048 PSEEN0443(gph) PSEEN0963 PSEEN1483 PSEEN1610
            PMY: Pmen_3998
            PAR: Psyc_0122 Psyc_0258 Psyc_2124(gph)
            PCR: Pcryo_0131 Pcryo_0284 Pcryo_2446
            ACI: ACIAD0043 ACIAD0296(gph) ACIAD0443
            SON: SO_0293(gph) SO_2414
            SDN: Sden_0268 Sden_1950 Sden_2300
            SFR: Sfri_0382 Sfri_2132
            SAZ: Sama_1729 Sama_3361
            SBL: Sbal_2060 Sbal_4106
            SBM: Shew185_2289
            SLO: Shew_0220 Shew_1947
            SPC: Sputcn32_2072 Sputcn32_3699
            SHE: Shewmr4_1917 Shewmr4_2403 Shewmr4_3691
            SHM: Shewmr7_0254 Shewmr7_2061 Shewmr7_2473
            SHN: Shewana3_1970 Shewana3_2565 Shewana3_3887
            SHW: Sputw3181_1940 Sputw3181_3841
            ILO: IL1347 IL1362(gph)
            CPS: CPS_0261(gph) CPS_2291
            PHA: PSHAa1419 PSHAa1814 PSHAa2709(gph)
            PAT: Patl_2472
            SDE: Sde_2151
            PIN: Ping_1410
            MAQ: Maqu_2496 Maqu_3516
            CBU: CBU_0349(gph)
            CBD: COXBU7E912_1730(gph)
            LPN: lpg2294
            LPF: lpl2213
            LPP: lpp2241
            MCA: MCA2583(cbbZ)
            FTU: FTT0491c(gph)
            FTF: FTF0491c(gph)
            FTW: FTW_1578(gph)
            FTL: FTL_1569
            FTH: FTH_1517(gph)
            FTN: FTN_0582(gph)
            TCX: Tcr_0265 Tcr_0705 Tcr_1189
            NOC: Noc_0178 Noc_2493
            AEH: Mlg_0909 Mlg_2251
            HHA: Hhal_0576 Hhal_2083
            HCH: HCH_02137 HCH_03071 HCH_04358 HCH_06113(gph)
            CSA: Csal_1594 Csal_1857 Csal_2324
            ABO: ABO_0119(dhlA) ABO_1062 ABO_1684(pgp) ABO_1754(gph)
            AHA: AHA_2332(gph-1) AHA_3184(gph-2)
            DNO: DNO_0537(gph)
            RMA: Rmag_0117 Rmag_0488
            VOK: COSY_0122(gph)
            NME: NMB0620 NMB1830
            NMA: NMA0625 NMA0828 NMA1688
            NMC: NMC1414
            NGO: NGO0073 NGO0203 NGO1052
            CVI: CV_1402 CV_1817 CV_2180(gph) CV_3092
            RSO: RS00363(RSp0485) RSc0581(RS04884) RSc0897(RS04518)
                 RSc1042(RS04208) RSc2880(gph)
            REU: Reut_A2273 Reut_A2581 Reut_A3022
            REH: H16_A0174 H16_A3318(gph) H16_B1387(cbbZ2)
            RME: Rmet_0710 Rmet_1514 Rmet_2438 Rmet_3177
            BMA: BMA0438(gph-1) BMAA0534(gph-2)
            BMV: BMASAVP1_0643(gph-2) BMASAVP1_A2583(gph-1)
            BML: BMA10299_0939(gph-2) BMA10299_A0957(gph-1)
            BMN: BMA10247_0190(gph-1) BMA10247_A1909(gph-2)
            BXE: Bxe_A0462 Bxe_A0971 Bxe_A1064 Bxe_B2479
            BVI: Bcep1808_0512 Bcep1808_0958
            BUR: Bcep18194_A3622 Bcep18194_A4150 Bcep18194_A4225
                 Bcep18194_A5761 Bcep18194_A5923 Bcep18194_B0841
                 Bcep18194_B0962 Bcep18194_C7037
            BCN: Bcen_0558 Bcen_2570 Bcen_3487
            BCH: Bcen2424_0535 Bcen2424_1037 Bcen2424_1113 Bcen2424_4879
            BAM: Bamb_0440 Bamb_0913 Bamb_0989
            BPS: BPSL2450 BPSL2524 BPSL3049
            BPM: BURPS1710b_0896 BURPS1710b_2916 BURPS1710b_3004(gph)
                 BURPS1710b_3574(gph)
            BPL: BURPS1106A_2861 BURPS1106A_2955(gph) BURPS1106A_3582(gph)
            BPD: BURPS668_2800 BURPS668_2893(gph) BURPS668_3555(gph)
            BTE: BTH_I1629(gph-1) BTH_I1709 BTH_I2908(gph-2) BTH_II1098
            PNU: Pnuc_0490
            BPE: BP0478 BP0549 BP0941 BP3265(gph)
            BPA: BPP0246 BPP3137 BPP3316 BPP4155(gph)
            BBR: BB0250 BB3476 BB3767 BB4625(gph)
            RFR: Rfer_1722 Rfer_2829 Rfer_3611
            POL: Bpro_1798 Bpro_3658 Bpro_4462
            PNA: Pnap_2787 Pnap_3656
            AAV: Aave_0440 Aave_3277
            AJS: Ajs_0363 Ajs_2461
            VEI: Veis_3116 Veis_3364
            MPT: Mpe_A0658 Mpe_A1483(cbbZ) Mpe_A2235 Mpe_A2787(cbbZ) Mpe_B0504
            HAR: HEAR0201 HEAR2086 HEAR2585(gph)
            MMS: mma_0236(gph1) mma_1348(gph2) mma_2679(gph3)
            NEU: NE2149(cbbZ) NE2546
            NET: Neut_2097 Neut_2506
            NMU: Nmul_A2185 Nmul_A2370
            EBA: ebA4174(cbbZ) ebA5444
            AZO: azo1615 azo2617 azo2819(ssm) azo3326(cbbZ)
            DAR: Daro_1226 Daro_3482
            TBD: Tbd_0945 Tbd_1562 Tbd_2229(cbbZ)
            MFA: Mfla_1323 Mfla_1536 Mfla_1575
            TDN: Tmden_0919
            CFF: CFF8240_0391
            ABU: Abu_1097 Abu_2153(gph)
            SUN: SUN_1195(gph)
            GSU: GSU2192(cbbZ)
            GME: Gmet_2290
            PCA: Pcar_0401 Pcar_2285
            PPD: Ppro_1187
            DVU: DVU0130 DVU1358
            DVL: Dvul_2834
            DDE: Dde_2190
            LIP: LI0364(gph)
            BBA: Bd0379(pgp)
            DPS: DP2134
            ADE: Adeh_1117
            MXA: MXAN_6859(gph)
            SAT: SYN_00311 SYN_02775
            SFU: Sfum_3382
            PUB: SAR11_1153(gph)
            MLO: mlr0528 mlr5413
            MES: Meso_1458
            SME: SMc00151(gph1) SMc00893 SMc01276(gph2)
            ATU: Atu0696 Atu1472 Atu1614(gph)
            ATC: AGR_C_1255 AGR_C_2715 AGR_C_2974
            RET: RHE_CH00845(ypch00279) RHE_CH02235(gph1) RHE_CH02381(gph2)
            RLE: RL0903(gph) RL1064 RL2566 RL2699
            BME: BMEI0975 BMEI0981 BMEI1446 BMEI1634 BMEII0272 BMEII0327
            BMF: BAB1_0318 BAB1_1021 BAB1_1027(cbbZ)
            BMS: BR0287 BR1002 BR1008(cbbZ)
            BMB: BruAb1_0313 BruAb1_1007 BruAb1_1013(cbbZ)
            BOV: BOV_0975(gph)
            BJA: bll0498 bll3754(gph) bll8046 blr4704
            BRA: BRADO0021 BRADO0849 BRADO1662 BRADO1971 BRADO4011
                 BRADO4715(cbbZ)
            BBT: BBta_0025 BBta_0456(cbbZ) BBta_0457 BBta_2295 BBta_3482(cbbZ)
                 BBta_4383 BBta_6394 BBta_7216
            RPA: RPA1980(cbbZ)
            RPB: RPB_3387
            RPC: RPC_2075
            RPD: RPD_2054
            RPE: RPE_1986
            NWI: Nwi_0649 Nwi_1220
            NHA: Nham_1479
            CCR: CC_1643 CC_2305
            SIL: SPO0517 SPO0787(gph-1) SPO2751 SPO2796(gph-2)
            SIT: TM1040_0729 TM1040_2172
            RSP: RSP_0412 RSP_1278(cbbZ) RSP_2504(gph)
            RSH: Rsph17029_2937
            JAN: Jann_1973 Jann_3129 Jann_3184
            RDE: RD1_0723 RD1_1442 RD1_2529 RD1_3303(gph) RD1_3476(gph)
            PDE: Pden_0617 Pden_4023
            MMR: Mmar10_0969
            HNE: HNE_0704(gph)
            ZMO: ZMO0497 ZMO1805(cbbZ)
            NAR: Saro_1198
            SAL: Sala_1371
            ELI: ELI_08820
            GOX: GOX0579
            GBE: GbCGDNIH1_1240
            RRU: Rru_A1268 Rru_A1683 Rru_A1956 Rru_A3031
            MGM: Mmc1_1778 Mmc1_3193
            ABA: Acid345_1784
            SUS: Acid_5253 Acid_7073
            BAN: BA0324 BA2220 BA2231
            BAR: GBAA0324 GBAA2220 GBAA2231
            BAA: BA_0894 BA_2722 BA_2735
            BAT: BAS0309 BAS2064 BAS2077
            BCE: BC0354 BC2174 BC2187
            BCA: BCE_0353 BCE_2250 BCE_2262
            BCZ: BCZK0296 BCZK2003(gph) BCZK2014(gph) BCZK2727(gph)
                 BCZK4527(gph) pE33L466_0261(gph)
            BTK: BT9727_0292 BT9727_2004(gph) BT9727_2015(gph)
            BTL: BALH_4346(gph)
            BLD: BLi03743(hprPe)
            SAU: SA0513
            SAV: SAV0555
            SAM: MW0510
            SAR: SAR0560
            SAS: SAS0513
            SAC: SACOL0602
            SAB: SAB0506
            SAO: SAOUHSC_00538
            SEP: SE0322
            SER: SERP0199
            SHA: SH2437
            SSP: SSP2160
            SPH: MGAS10270_Spy1168
            SPN: SP_0104
            SPR: spr0093(gph)
            SMU: SMU.1254
            STC: str0942
            STL: stu0942
            SSA: SSA_2363
            SGO: SGO_0141 SGO_1433 SGO_1988
            LPL: lp_0872(gph1) lp_1932(gph2) lp_3544(gph3)
            LSA: LSA0022
            LSL: LSL_0824
            LDB: Ldb1158(pgp)
            LBU: LBUL_1077
            LCA: LSEI_0754
            EFA: EF2916
            CAC: CAC0418
            CTH: Cthe_0261
            DSY: DSY4241
            DRM: Dred_2449
            MTA: Moth_2007
            UUR: UU115(gph)
            MSM: MSMEG_4183
            CGL: NCgl2158(cgl2239)
            RHA: RHA1_ro01185 RHA1_ro02900
            FAL: FRAAL0916 FRAAL1709
            SEN: SACE_2872(rifM) SACE_4385
            BAD: BAD_0820
            RBA: RB2754
            BGA: BG0699(gph)
            BAF: BAPKO_0720(gph)
            TPA: TP0407 TP0554
            TDE: TDE2716
            LIL: LA2702
            SYN: sll1349(cbbZp) slr1762
            SYW: SYNW1986
            SYC: syc0837_d syc1497_d(cbbZp)
            SYF: Synpcc7942_0693 Synpcc7942_2613
            SYG: sync_0530(gph)
            TEL: tll1470
            GVI: gll0254
            ANA: all0135 all2681 alr4944
            AVA: Ava_0109 Ava_0113 Ava_0809 Ava_1504 Ava_2228 Ava_3420
                 Ava_4069 Ava_4333
            PMA: Pro0350(gph)
            PMT: PMT1669
            PMN: PMN2A_1688
            TER: Tery_4662
            BTH: BT_4184 BT_4315
            BFR: BF0877 BF1014
            BFS: BF0801 BF0931 BF3860
            SRU: SRU_0533
            CTE: CT0889(gph)
            CCH: Cag_0976
            CPH: Cpha266_1237
            PVI: Cvib_1004
            PLT: Plut_1252
            TTH: TTC1471
            AAE: aq_1342(gph)
            MBA: Mbar_A2726
            MMA: MM_3329
            HWA: HQ2788A
            TAC: Ta0845
            TVO: TVN0942
            PTO: PTO1108
            RCI: RCIX953(gph)
            HBU: Hbut_0505
            STO: ST2055
            PAI: PAE3068
STRUCTURES  PDB: 1TE2  1WR8  2HDO  2HI0  2NYV  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.18
            ExPASy - ENZYME nomenclature database: 3.1.3.18
            ExplorEnz - The Enzyme Database: 3.1.3.18
            ERGO genome analysis and discovery system: 3.1.3.18
            BRENDA, the Enzyme Database: 3.1.3.18
            CAS: 9025-76-7
///
ENTRY       EC 3.1.3.19                 Enzyme
NAME        glycerol-2-phosphatase;
            beta-glycerophosphatase;
            beta-glycerophosphate phosphatase;
            2-glycerophosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     glycerol-2-phosphate phosphohydrolase
REACTION    glycerol 2-phosphate + H2O = glycerol + phosphate [RN:R01043]
ALL_REAC    R01043
SUBSTRATE   glycerol 2-phosphate [CPD:C02979];
            H2O [CPD:C00001]
PRODUCT     glycerol [CPD:C00116];
            phosphate [CPD:C00009]
REFERENCE   1
  AUTHORS   Schmidt, G.
  TITLE     Nonspecific acid phosphomonoesterases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 5, Academic Press, New York, 1961, p. 37-47.
REFERENCE   2
  AUTHORS   Tsuboi, K.K., Wiener, G. and Hudson, P.B.
  TITLE     Acid phosphatase. VII. Yeast phosphomonoesterase; isolation
            procedure and stability characteristics.
  JOURNAL   J. Biol. Chem. 224 (1957) 621-635.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.19
            ExPASy - ENZYME nomenclature database: 3.1.3.19
            ExplorEnz - The Enzyme Database: 3.1.3.19
            ERGO genome analysis and discovery system: 3.1.3.19
            BRENDA, the Enzyme Database: 3.1.3.19
            CAS: 9027-39-8
///
ENTRY       EC 3.1.3.20                 Enzyme
NAME        phosphoglycerate phosphatase;
            D-2-phosphoglycerate phosphatase;
            glycerophosphate phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     D-glycerate-2-phosphate phosphohydrolase
REACTION    D-glycerate 2-phosphate + H2O = D-glycerate + phosphate [RN:R01748]
ALL_REAC    R01748
SUBSTRATE   D-glycerate 2-phosphate [CPD:C00631];
            H2O [CPD:C00001]
PRODUCT     D-glycerate [CPD:C00258];
            phosphate [CPD:C00009]
REFERENCE   1  [PMID:4284998]
  AUTHORS   Fallon HJ, Byrne WL.
  TITLE     2-phosphoglyceric acid phosphatase: identification and properties of
            the beef-liver enzyme.
  JOURNAL   Biochim. Biophys. Acta. 105 (1965) 43-53.
  ORGANISM  cow [GN:bta]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.20
            ExPASy - ENZYME nomenclature database: 3.1.3.20
            ExplorEnz - The Enzyme Database: 3.1.3.20
            ERGO genome analysis and discovery system: 3.1.3.20
            BRENDA, the Enzyme Database: 3.1.3.20
            CAS: 9055-30-5
///
ENTRY       EC 3.1.3.21                 Enzyme
NAME        glycerol-1-phosphatase;
            alpha-glycerophosphatase;
            alpha-glycerol phosphatase;
            glycerol 3-phosphatase;
            glycerol-3-phosphate phosphatase;
            glycerol 3-phosphate phosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     glycerol-1-phosphate phosphohydrolase
REACTION    glycerol 1-phosphate + H2O = glycerol + phosphate [RN:R07298]
ALL_REAC    R07298;
            (other) R00841
SUBSTRATE   glycerol 1-phosphate [CPD:C00623];
            H2O [CPD:C00001]
PRODUCT     glycerol [CPD:C00116];
            phosphate [CPD:C00009]
COMMENT     The Dunaliella enzyme acts more rapidly on sn-glycerol 1-phosphate
            than on the 3-phosphate. The enzyme from yeast also acts on
            propane-1,2-diol 1-phosphate, but not on a variety of other
            phosphate esters.
REFERENCE   1
  AUTHORS   Sussman, I. and Avron, M.
  TITLE     Characterization and partial purification of
            DL-glycerol-1-phosphatase from Dunaliella salina.
  JOURNAL   Biochim. Biophys. Acta 661 (1981) 199-204.
  ORGANISM  Dunaliella salina
PATHWAY     PATH: map00561  Glycerolipid metabolism
ORTHOLOGY   KO: K06116  glycerol 3-phosphatase 1
            KO: K06117  glycerol 3-phosphatase 2
GENES       SCE: YER062C(HOR2) YIL053W(RHR2)
            AGO: AGOS_ADL071C
            PIC: PICST_42440(GPP1)
            CAL: CaO19_5437(CaO19.5437)
            CGR: CAGL0M11660g
            AFM: AFUA_1G10570
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.21
            ExPASy - ENZYME nomenclature database: 3.1.3.21
            ExplorEnz - The Enzyme Database: 3.1.3.21
            ERGO genome analysis and discovery system: 3.1.3.21
            BRENDA, the Enzyme Database: 3.1.3.21
            CAS: 37228-75-4
///
ENTRY       EC 3.1.3.22                 Enzyme
NAME        mannitol-1-phosphatase;
            mannitol-1-phosphate phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     D-mannitol-1-phosphate phosphohydrolase
REACTION    D-mannitol 1-phosphate + H2O = D-mannitol + phosphate [RN:R02167]
ALL_REAC    R02167
SUBSTRATE   D-mannitol 1-phosphate [CPD:C00644];
            H2O [CPD:C00001]
PRODUCT     D-mannitol [CPD:C00392];
            phosphate [CPD:C00009]
REFERENCE   1
  AUTHORS   Rumpho, M.E., Edwards, G.E. and Loescher, W.H.
  TITLE     A pathway for photosynthetic carbon flow to mannitol in celery
            leaves Activity and localization of key enzymes.
  JOURNAL   Plant Physiol. 73 (1983) 869-873.
  ORGANISM  celery
REFERENCE   2
  AUTHORS   Yamada, H., Okamoto, K., Kodama, K., Noguchi, F. and Tanaka, S.
  TITLE     Enzymatic studies on mannitol formation by Piricularia oryzae.
  JOURNAL   J. Biochem. (Tokyo) 49 (1961) 404-410.
  ORGANISM  Pyricularia oryzae
PATHWAY     PATH: map00051  Fructose and mannose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.22
            ExPASy - ENZYME nomenclature database: 3.1.3.22
            ExplorEnz - The Enzyme Database: 3.1.3.22
            ERGO genome analysis and discovery system: 3.1.3.22
            BRENDA, the Enzyme Database: 3.1.3.22
            CAS: 9055-29-2
///
ENTRY       EC 3.1.3.23                 Enzyme
NAME        sugar-phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     sugar-phosphate phosphohydrolase
REACTION    sugar phosphate + H2O = sugar + phosphate [RN:R00804]
ALL_REAC    R00804
SUBSTRATE   sugar phosphate [CPD:C00934];
            H2O [CPD:C00001]
PRODUCT     sugar [CPD:C11477];
            phosphate [CPD:C00009]
COMMENT     Has a wide specificity, acting on aldohexose 1-phosphates,
            ketohexose 1-phosphates, aldohexose 6-phosphates, ketohexose
            6-phosphates, both phosphate ester bonds of fructose
            1,6-bisphosphate, phosphoric esters of disaccharides, and on pentose
            and triose phosphates, but at a slower rate.
REFERENCE   1  [PMID:4290224]
  AUTHORS   Lee YP, Sowokinos JR.
  TITLE     Sugar phosphate phosphohydrolase. I. Substrate specificity,
            intracellular localization, and purification from Neisseria
            meningitidis.
  JOURNAL   J. Biol. Chem. 242 (1967) 2264-71.
  ORGANISM  Neisseria meningitidis
ORTHOLOGY   KO: K07757  sugar-phosphatase
GENES       ECO: b0822(ybiV)
            ECJ: JW0806(ybiV)
            ECE: Z1044
            ECS: ECs0899
            ECC: c0907(ybiV)
            ECI: UTI89_C0825(ybiV)
            ECP: ECP_0835
            ECV: APECO1_1271(ybiV)
            ECW: EcE24377A_0893(supH) EcE24377A_2586(yfbT)
            ECX: EcHS_A0880(supH) EcHS_A2442(yfbT)
            STY: STY0881
            STT: t2047
            SPT: SPA1913(ybiV(1))
            SEC: SC0837(ybiV(1))
            STM: STM0842(ybiV(1))
            SFL: SF0772
            SFX: S0815
            SFV: SFV_0805
            SSN: SSON_0804
            SBO: SBO_0712
            SDY: SDY_0765
            SAJ: SaurJH9_2548
            SAH: SaurJH1_2600
            GFO: GFO_2192
STRUCTURES  PDB: 2HF2  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.23
            ExPASy - ENZYME nomenclature database: 3.1.3.23
            ExplorEnz - The Enzyme Database: 3.1.3.23
            ERGO genome analysis and discovery system: 3.1.3.23
            BRENDA, the Enzyme Database: 3.1.3.23
            CAS: 9023-07-8
///
ENTRY       EC 3.1.3.24                 Enzyme
NAME        sucrose-phosphatase;
            sucrose 6-phosphate hydrolase;
            sucrose-phosphate hydrolase;
            sucrose-phosphate phosphohydrolase;
            sucrose-6-phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     sucrose-6F-phosphate phosphohydrolase
REACTION    sucrose 6F-phosphate + H2O = sucrose + phosphate [RN:R00805 R06211]
ALL_REAC    R00805 R06211(G)
SUBSTRATE   sucrose 6F-phosphate [CPD:C02591];
            H2O [CPD:C00001]
PRODUCT     sucrose [CPD:C00089];
            phosphate [CPD:C00009]
REFERENCE   1  [PMID:4290548]
  AUTHORS   Hawker JS, Hatch MD.
  TITLE     A specific sucrose phosphatase from plant tissues.
  JOURNAL   Biochem. J. 99 (1966) 102-7.
  ORGANISM  Saccharum officinarum [GN:esof], Daucus carota
PATHWAY     PATH: map00500  Starch and sucrose metabolism
STRUCTURES  PDB: 1S2O  1TJ3  1TJ4  1TJ5  1U2S  1U2T  2B1Q  2B1R  2D2V  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.24
            ExPASy - ENZYME nomenclature database: 3.1.3.24
            ExplorEnz - The Enzyme Database: 3.1.3.24
            ERGO genome analysis and discovery system: 3.1.3.24
            BRENDA, the Enzyme Database: 3.1.3.24
            CAS: 9059-33-0
///
ENTRY       EC 3.1.3.25                 Enzyme
NAME        inositol-phosphate phosphatase;
            myo-inositol-1(or 4)-monophosphatase;
            inositol 1-phosphatase;
            L-myo-inositol-1-phosphate phosphatase;
            myo-inositol 1-phosphatase;
            inositol phosphatase;
            inositol monophosphate phosphatase;
            inositol-1(or 4)-monophosphatase;
            myo-inositol-1(or 4)-phosphate phosphohydrolase;
            myo-inositol monophosphatase;
            myo-inositol-1-phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     myo-inositol-phosphate phosphohydrolase
REACTION    myo-inositol phosphate + H2O = myo-inositol + phosphate [RN:R07343]
ALL_REAC    R07343 > R01185 R01186 R01187
SUBSTRATE   myo-inositol phosphate [CPD:C15585];
            H2O [CPD:C00001]
PRODUCT     myo-inositol [CPD:C00137];
            phosphate [CPD:C00009]
COMMENT     Acts on five of the six isomers of myo-inositol phosphate, all
            except myo-inositol 2-phosphate, but does not act on myo-inositol
            bearing more than one phosphate group. It also acts on adenosine
            2'-phosphate (but not the 3'- or 5'- phosphates), sn-glycerol
            3-phosphate and glycerol 2-phosphate. Two isoforms are known [4].
REFERENCE   1  [PMID:4290245]
  AUTHORS   Eisenberg F Jr.
  TITLE     D-myoinositol 1-phosphate as product of cyclization of glucose
            6-phosphate and substrate for a specific phosphatase in rat testis.
  JOURNAL   J. Biol. Chem. 242 (1967) 1375-82.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:2833231]
  AUTHORS   Gee NS, Ragan CI, Watling KJ, Aspley S, Jackson RG, Reid GG, Gani D,
            Shute JK.
  TITLE     The purification and properties of myo-inositol monophosphatase from
            bovine brain.
  JOURNAL   Biochem. J. 249 (1988) 883-9.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:6253491]
  AUTHORS   Hallcher LM, Sherman WR.
  TITLE     The effects of lithium ion and other agents on the activity of
            myo-inositol-1-phosphatase from bovine brain.
  JOURNAL   J. Biol. Chem. 255 (1980) 10896-901.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:9322233]
  AUTHORS   Yoshikawa T, Turner G, Esterling LE, Sanders AR, Detera-Wadleigh SD.
  TITLE     A novel human myo-inositol monophosphatase gene, IMP.18p, maps to a
            susceptibility region for bipolar disorder.
  JOURNAL   Mol. Psychiatry. 2 (1997) 393-7.
  ORGANISM  human [GN:hsa]
REFERENCE   5
  AUTHORS   Woscholski, R. and Parker, P.J.
  TITLE     Inositol phosphatases: constructive destruction of phosphoinositides
            and inositol phosphates.
  JOURNAL   In: Cockcroft, S. (Ed.), Biology of Phosphoinositides, Biology of
            Phosphoinositides, Oxford, 2000, p. 320-338.
REFERENCE   6  [PMID:3036092]
  AUTHORS   Ackermann KE, Gish BG, Honchar MP, Sherman WR.
  TITLE     Evidence that inositol 1-phosphate in brain of lithium-treated rats
            results mainly from phosphatidylinositol metabolism.
  JOURNAL   Biochem. J. 242 (1987) 517-24.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00521  Streptomycin biosynthesis
            PATH: map00562  Inositol phosphate metabolism
            PATH: map04070  Phosphatidylinositol signaling system
ORTHOLOGY   KO: K01092  myo-inositol-1(or 4)-monophosphatase
GENES       HSA: 3612(IMPA1) 3613(IMPA2)
            PTR: 455286(IMPA2)
            MMU: 114663(Impa2) 55980(Impa1)
            RNO: 282636(Impa2) 83523(Impa1)
            CFA: 477925(IMPA1)
            BTA: 281865(IMPA1)
            SSC: 397425(IMPA1)
            GGA: 420199(IMPA1) 421032(IMPA2)
            XLA: 380327(impa1) 444552(MGC83403)
            DME: Dmel_CG17028
            CEL: F13G3.5(myo-inositol-1-monophosphatase)
            ATH: AT3G02870(VTC4)
            OSA: 4328439 4333347
            CME: CMH255C CMQ201C
            CGR: CAGL0J00319g
            AFM: AFUA_1G11600
            AOR: AO090038000262
            DDI: DDBDRAFT_0204100
            TBR: Tb927.5.2690
            TCR: 507047.120 509179.140
            LMA: LmjF17.1390
            EHI: 208.t00004
            ECO: b2533(suhB)
            ECJ: JW2517(suhB)
            ECS: ECs3399
            ECC: c3059(suhB)
            ECI: UTI89_C2855(suhB)
            ECP: ECP_2538
            ECV: APECO1_3992(suhB)
            ECW: EcE24377A_2818(suhB)
            ECX: EcHS_A2685(suhB)
            STY: STY2792(suhB)
            STT: t0310(suhB)
            SPT: SPA0320(suhB)
            SEC: SC2540(suhB)
            STM: STM2546(suhB)
            YPE: YPO2899(suhB)
            YPK: y1331(suhB)
            YPM: YP_2555(suhB)
            YPA: YPA_2340
            YPN: YPN_1238
            YPP: YPDSF_2244
            YPS: YPTB2862(suhB)
            YPI: YpsIP31758_1165(suhB)
            YEN: YE1054(suhB) YE2054
            SFL: SF2580(suhB)
            SFX: S2752(suhB)
            SFV: SFV_2581(suhB)
            SSN: SSON_2615(suhB)
            SBO: SBO_2557(suhB)
            SDY: SDY_2729(suhB)
            ECA: ECA3240(suhB)
            PLU: plu3286(suhB)
            BUC: BU285(suhB)
            BAS: BUsg274(suhB)
            BAB: bbp264(suhB)
            BCC: BCc_175(suhB)
            WBR: WGLp285(suhB)
            SGL: SG1772
            KPN: KPN_02865(suhB)
            SPE: Spro_3118 Spro_3630
            BFL: Bfl535(suhB)
            BPN: BPEN_555(suhB)
            HIN: HI0937(suhB)
            HIT: NTHI1108(suhB)
            HDU: HD0440(suhB)
            HSO: HS_0278(suhB)
            PMU: PM0315(suhB)
            MSU: MS1729(suhB)
            APL: APL_0206(suhB)
            ASU: Asuc_0861
            XFA: XF2476
            XFT: PD1493(suhB)
            XCC: XCC2277(suhB)
            XCB: XC_1838
            XCV: XCV2582(suhB)
            XAC: XAC2385(suhB)
            XOO: XOO2711(suhB)
            XOM: XOO_2556(XOO2556)
            VCH: VC0745
            VVU: VV1_0441
            VVY: VV0752
            VPA: VP0593
            VFI: VF0614
            PPR: PBPRA0747(suhB)
            PAE: PA3818
            PAU: PA14_14680(suhB)
            PPU: PP_0838(suhB)
            PPF: Pput_0868
            PST: PSPTO_1419(suhB)
            PSB: Psyr_1233
            PSP: PSPPH_1305 PSPPH_4535
            PFL: PFL_4969(suhB)
            PFO: Pfl_4616
            PEN: PSEEN1005(suhB) PSEEN3013
            PMY: Pmen_3515
            PAR: Psyc_0222(suhB)
            PCR: Pcryo_0246
            PRW: PsycPRwf_0412
            ACI: ACIAD3246(suhB)
            SON: SO_2260(suhB)
            SDN: Sden_1454
            SFR: Sfri_2428
            SAZ: Sama_1289
            SBL: Sbal_2401
            SBM: Shew185_2390
            SLO: Shew_2321
            SPC: Sputcn32_2153
            SSE: Ssed_2875
            SPL: Spea_1484
            SHE: Shewmr4_1735
            SHM: Shewmr7_1815
            SHN: Shewana3_2284
            SHW: Sputw3181_1858
            ILO: IL2043(suhB)
            CPS: CPS_1128(suhB)
            PHA: PSHAa0323(suhB)
            PAT: Patl_1232
            SDE: Sde_1410
            PIN: Ping_1321
            CBU: CBU_1133(suhB)
            CBD: COXBU7E912_1231(suhB)
            LPN: lpg1748(suhB)
            LPF: lpl1712
            LPP: lpp1712
            MCA: MCA2471 MCA2609
            FTU: FTT1382(suhB)
            FTF: FTF1382(suhB)
            FTL: FTL_1132
            FTH: FTH_1107(suhB)
            FTN: FTN_1346
            TCX: Tcr_0614 Tcr_0995
            NOC: Noc_0719 Noc_1838
            AEH: Mlg_1244
            HHA: Hhal_1796
            HCH: HCH_03301 HCH_06096
            CSA: Csal_1824 Csal_2845
            ABO: ABO_0512(suhB)
            MMW: Mmwyl1_0186 Mmwyl1_1604 Mmwyl1_3781
            AHA: AHA_1710
            BCI: BCI_0005(suhB)
            RMA: Rmag_0491
            VOK: COSY_0452(suhB)
            NME: NMB1347(suhB) NMB1924
            NMA: NMA0529 NMA1559
            NGO: NGO0671(suhB) NGO2161
            CVI: CV_0366(suhB2) CV_3644(suhB)
            RSO: RSc1160(suhB)
            REU: Reut_A1115
            REH: H16_A1214(suhB)
            RME: Rmet_1078
            BMA: BMA1664(suhB)
            BMV: BMASAVP1_A2168(suhB)
            BML: BMA10299_A3149(suhB)
            BMN: BMA10247_1441(suhB)
            BXE: Bxe_A1619
            BUR: Bcep18194_A5391
            BCN: Bcen_5992
            BCH: Bcen2424_2085 Bcen2424_6307
            BAM: Bamb_2120
            BPS: BPSL2250(suhB)
            BPM: BURPS1710b_2689(suhB)
            BPL: BURPS1106A_2605
            BPD: BURPS668_2553
            BTE: BTH_I1934
            BPE: BP1902(suhB) BP2813
            BPA: BPP2277(suhB) BPP3728
            BBR: BB1729(suhB) BB4174
            RFR: Rfer_2892
            POL: Bpro_3293
            PNA: Pnap_1380
            AAV: Aave_2070
            AJS: Ajs_1045
            VEI: Veis_4248
            MPT: Mpe_A2841
            HAR: HEAR2165(cysQ)
            MMS: mma_1298(suhB)
            NEU: NE0781 NE1954(suhB)
            NET: Neut_0407 Neut_1051
            NMU: Nmul_A0377 Nmul_A0672 Nmul_A1789
            EBA: ebA1097(suhB) ebA6410(suhB)
            AZO: azo2021(suhB1) azo2833(suhB2) azo3824(imp)
            DAR: Daro_1681
            TBD: Tbd_0158 Tbd_1160
            MFA: Mfla_0813
            ABU: Abu_0443(suhB) Abu_1825
            NIS: NIS_1712(suhB)
            GSU: GSU0942(suhB)
            GME: Gmet_0697
            GUR: Gura_3355
            PCA: Pcar_2439
            DVU: DVU1680(suhB)
            DDE: Dde_1992
            BBA: Bd3335(suhB)
            ADE: Adeh_3387
            AFW: Anae109_3449
            MXA: MXAN_1914(suhB)
            SAT: SYN_00928
            SFU: Sfum_1393 Sfum_2095
            RFE: RF_1048(suhB)
            RBE: RBE_0971(suhB)
            WOL: WD1280
            WBM: Wbm0132
            AMA: AM473(suhB)
            APH: APH_0548
            ERU: Erum3200(suhB)
            ERW: ERWE_CDS_03250(suhB)
            ERG: ERGA_CDS_03200(suhB)
            ECN: Ecaj_0302
            ECH: ECH_0776
            PUB: SAR11_0581(suhB) SAR11_0783
            MLO: mlr3921(suhB)
            MES: Meso_3185
            PLA: Plav_0630 Plav_2101
            SME: SMb20362 SMc03994(suhB)
            SMD: Smed_2665 Smed_3755 Smed_3959 Smed_3968
            ATU: Atu3748(suhB)
            ATC: AGR_L_2172(suhB)
            RET: RHE_CH02123(ypch00696) RHE_CH03514(suhBch) RHE_CH03573
                 RHE_PB00111(suhBb) RHE_PB00133(ypb00084)
            RLE: RL0900 RL2620 RL2621 RL3130 RL4025(suhB) RL4091 pRL90217
                 pRL90264
            BME: BMEI0326 BMEII0568 BMEII1032
            BMF: BAB1_1723 BAB2_0206 BAB2_0522
            BMS: BR1711 BRA0717
            BMB: BruAb1_1696 BruAb2_0513
            OAN: Oant_1205 Oant_3842
            BJA: bll1517(suhB)
            BRA: BRADO1117 BRADO1471(cysQ) BRADO6099 BRADO6215
            BBT: BBta_1389 BBta_1688 BBta_2598 BBta_6561(cysQ) BBta_6932
            RPA: RPA0937
            RPB: RPB_1853 RPB_4474 RPB_4517
            RPC: RPC_0779 RPC_4707 RPC_4776
            RPD: RPD_4111 RPD_4320 RPD_4358
            RPE: RPE_0706 RPE_0878 RPE_4719
            NWI: Nwi_2559 Nwi_2740 Nwi_2950
            NHA: Nham_1141 Nham_3181 Nham_3537
            BHE: BH15030(suhB)
            BQU: BQ11950(suhB)
            XAU: Xaut_3055
            CCR: CC_3269(suhB)
            SIL: SPO3012
            SIT: TM1040_1698
            RSP: RSP_0651 RSP_2169(suhB)
            RSH: Rsph17029_2304
            RSQ: Rsph17025_0581 Rsph17025_2324 Rsph17025_3002
            JAN: Jann_0402 Jann_1028 Jann_1366
            RDE: RD1_0291 RD1_2006 RD1_2209 RD1_2507(suhB)
            PDE: Pden_4652
            MMR: Mmar10_2588
            HNE: HNE_3187(suhB)
            NAR: Saro_1957
            SAL: Sala_1313
            SWI: Swit_2683 Swit_2981
            GOX: GOX0064 GOX0237 GOX2045
            GBE: GbCGDNIH1_1084 GbCGDNIH1_1991 GbCGDNIH1_2201
            ACR: Acry_1707
            RRU: Rru_A0445 Rru_A1076 Rru_A1687 Rru_A3165
            MAG: amb1286
            MGM: Mmc1_0078 Mmc1_3283
            ABA: Acid345_2060
            SUS: Acid_5909
            BSU: BG11818(yktC)
            BHA: BH2635
            BAN: BA4168
            BAR: GBAA4168
            BAA: BA_4639
            BAT: BAS3870
            BCE: BC3958
            BCA: BCE_4005
            BCZ: BCZK3718(suhB)
            BCY: Bcer98_2660
            BTK: BT9727_3703(suhB)
            BLI: BL05151(suhB)
            BLD: BLi01685(yktC)
            BCL: ABC2404
            BAY: RBAM_014530(suhB)
            BPU: BPUM_1365(suhB)
            OIH: OB1422
            GKA: GK1068
            SAU: SA0958
            SAV: SAV1107
            SAM: MW0990
            SAR: SAR1081
            SAS: SAS1042
            SAC: SACOL1116
            SAB: SAB0973
            SAA: SAUSA300_1007 SAUSA300_2260
            SAO: SAOUHSC_01055
            SAJ: SaurJH9_1167 SaurJH9_2335
            SAH: SaurJH1_1189 SaurJH1_2378
            SEP: SE0805
            SER: SERP0694
            SHA: SH1845
            SSP: SSP1682
            LMO: lmo1066
            LMF: LMOf2365_1083
            LIN: lin1054
            LWE: lwe1044
            LLA: L133367(yfdE)
            LLC: LACR_0547
            LLM: llmg_0516(suhB)
            SPY: SPy_1247
            SPZ: M5005_Spy_0957
            SPM: spyM18_1196
            SPG: SpyM3_0883
            SPS: SPs1083
            SPH: MGAS10270_Spy1072
            SPI: MGAS10750_Spy1107 MGAS10750_Spy1108
            SPJ: MGAS2096_Spy1017
            SPK: MGAS9429_Spy1061
            SPF: SpyM50841
            SPA: M6_Spy0947
            SPB: M28_Spy0930
            SPN: SP_1403
            SPR: spr1260
            SAG: SAG0994
            SAN: gbs1029
            SAK: SAK_1089
            SMU: SMU.1140c
            STC: str0999(suhB)
            STL: stu0999(suhB)
            SSA: SSA_0939(suhB)
            SGO: SGO_1053(app)
            LPL: lp_2147(suhB)
            LSA: LSA1080
            LSL: LSL_0652
            LBR: LVIS_1404
            LCA: LSEI_1312
            LRE: Lreu_0636
            EFA: EF2461
            MTU: Rv1604(impA) Rv2701c(suhB)
            MTC: MT2775
            MBO: Mb1630(impA) Mb2720c(suhB)
            MBB: BCG_1642(impA)
            MLE: ML1024(suhB)
            MPA: MAP2818c(suhB)
            MAV: MAV_3593
            MSM: MSMEG_2083 MSMEG_2762 MSMEG_3116 MSMEG_3210
            MVA: Mvan_1908 Mvan_2463 Mvan_2809
            MGI: Mflv_3608 Mflv_3937 Mflv_4454
            MMC: Mmcs_2187 Mmcs_2424 Mmcs_3058
            MKM: Mkms_2233 Mkms_2469
            MJL: Mjls_2176 Mjls_2463 Mjls_3074
            CGL: NCgl1834(cgl1909)
            CGB: cg2090(suhB) cg2298(impA)
            CEF: CE1802
            CDI: DIP1403
            CJK: jk0792(impA) jk1085(suhB)
            NFA: nfa15800 nfa37570
            RHA: RHA1_ro01023(suhB) RHA1_ro06402 RHA1_ro06825
            SCO: SCO5860(SC9B10.27)
            SMA: SAV2406(suhB1)
            LXX: Lxx02030(suhB)
            CMI: CMM_2799(suhB)
            ART: Arth_1299
            AAU: AAur_1435(suhB)
            NCA: Noca_2912 Noca_3679
            TFU: Tfu_1943
            FRA: Francci3_1313
            FAL: FRAAL2074(suhB)
            ACE: Acel_1405
            KRA: Krad_1553
            SEN: SACE_1803(suhB) SACE_6492 SACE_6907(suhB)
            STP: Strop_1476
            RXY: Rxyl_0695 Rxyl_1545 Rxyl_2307
            RBA: RB422(suhB) RB5696(suhB)
            PCU: pc1576(suhB)
            LIL: LA0033(suhB1) LA0229(suhB2)
            LIC: LIC10029 LIC10198(suhB)
            LBJ: LBJ_0165(suhB) LBJ_2986
            LBL: LBL_0079 LBL_2918(suhB)
            SYN: sll1329 sll1383(suhB)
            SYW: SYNW1275 SYNW2186
            SYC: syc1528_c(impA) syc2329_c
            SYF: Synpcc7942_1763 Synpcc7942_2582
            SYD: Syncc9605_1401 Syncc9605_2329
            SYE: Syncc9902_1086
            SYG: sync_1395(suhB) sync_2540
            SYR: SynRCC307_1368(suhB)
            SYX: SynWH7803_1241(suhB)
            CYA: CYA_0375 CYA_2675
            CYB: CYB_1862 CYB_2170
            TEL: tlr1657 tlr2119
            GVI: glr1322
            ANA: all2917 all4461
            AVA: Ava_0983 Ava_3333
            PMA: Pro0115 Pro0937(suhB)
            PMM: PMM0096 PMM0899
            PMT: PMT0183 PMT0699(suhB)
            PMN: PMN2A_0308 PMN2A_1464
            PMI: PMT9312_0100 PMT9312_0901
            PMB: A9601_09621(suhB)
            PMC: P9515_09811(suhB)
            PMG: P9301_09601(suhB)
            PMH: P9215_09931(suhB)
            PME: NATL1_09811(suhB)
            TER: Tery_0756 Tery_4756
            BTH: BT_2801
            BFR: BF4389
            BFS: BF4187(suhB)
            SRU: SRU_0531
            CHU: CHU_3258(suhB)
            CTE: CT1661(suhB)
            CCH: Cag_0161 Cag_1522
            CPH: Cpha266_0543
            PVI: Cvib_1247 Cvib_1428
            PLT: Plut_1639
            RRS: RoseRS_1153 RoseRS_3700
            RCA: Rcas_0945
            TTH: TTC1928
            TTJ: TTHA0077
            AAE: aq_1983(imp2)
            TMA: TM1415
            TME: Tmel_1174
            MJA: MJ0109
            MMQ: MmarC5_0088
            MAC: MA3344
            MBA: Mbar_A2190
            MMA: MM_2783
            MBU: Mbur_0852
            MTP: Mthe_0841
            MHU: Mhun_0903
            MEM: Memar_0967
            MBN: Mboo_1351
            MTH: MTH871
            MST: Msp_1329(suhB)
            MKA: MK0741(suhB)
            AFU: AF2372(suhB)
            HMA: rrnAC1004(suhB1) rrnB0102(suhB2)
            HWA: HQ1465A(suhB) HQ2795A(suhB)
            NPH: NP4188A(suhB)
            PHO: PH1897
            PAB: PAB0189(imp1)
            PFU: PF2014
            RCI: RRC40(suhB)
            APE: APE_1798.1
            SSO: SSO2418(imp3)
            STO: ST0547(suhB)
            SAI: Saci_0930
            PAI: PAE3055(suhB)
            TPE: Tpen_0200
STRUCTURES  PDB: 1AWB  1DK4  1G0H  1G0I  1IMA  1IMB  1IMC  1IMD  1IME  1IMF  
                 1LBV  1LBW  1LBX  1LBY  1LBZ  2BJI  2CZH  2CZI  2CZK  2DDK  
                 2FVZ  2HHM  2P3N  2P3V  2PCR  2QFL  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.25
            ExPASy - ENZYME nomenclature database: 3.1.3.25
            ExplorEnz - The Enzyme Database: 3.1.3.25
            ERGO genome analysis and discovery system: 3.1.3.25
            BRENDA, the Enzyme Database: 3.1.3.25
            CAS: 37184-63-7
///
ENTRY       EC 3.1.3.26                 Enzyme
NAME        4-phytase;
            6-phytase (name based on 1L-numbering system and not 1D-numbering);
            phytase;
            phytate 6-phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     myo-inositol-hexakisphosphate 6-phosphohydrolase
REACTION    myo-inositol hexakisphosphate + H2O = 1D-myo-inositol
            1,2,3,4,5-pentakisphosphate + phosphate [RN:R03372]
ALL_REAC    R03372
SUBSTRATE   myo-inositol hexakisphosphate [CPD:C01204];
            H2O [CPD:C00001]
PRODUCT     1D-myo-inositol 1,2,3,4,5-pentakisphosphate [CPD:C04579];
            phosphate [CPD:C00009]
REFERENCE   1  [PMID:4310376]
  AUTHORS   Johnson LF, Tate ME.
  TITLE     The structure of myo-inositol pentaphosphates.
  JOURNAL   Ann. N. Y. Acad. Sci. 165 (1969) 526-32.
REFERENCE   2
  AUTHORS   Tomlinson, R.V. and Ballou, C.E.
  TITLE     Myoinositol polyphosphate intermediates in the dephosphorylation of
            phytic acid by phytase.
  JOURNAL   Biochemistry 1 (1962) 166-171.
  ORGANISM  Triticum aestivum [GN:etae]
REFERENCE   3  [PMID:4349266]
  AUTHORS   Lim PE, Tate ME.
  TITLE     The phytases. II. Properties of phytase fractions F 1  and F 2  from
            wheat bran and the myoinositol phosphates produced by fraction F 2 .
  JOURNAL   Biochim. Biophys. Acta. 302 (1973) 316-28.
  ORGANISM  Triticum aestivum [GN:etae]
REFERENCE   4
  AUTHORS   Cosgrove, D.J.
  TITLE     Inositol Phosphates: Their Chemistry, Biochemistry, and Physiology,
            Elsevier, Amsterdam, 1980.
PATHWAY     PATH: map00562  Inositol phosphate metabolism
ORTHOLOGY   KO: K01093  6-phytase
GENES       ECO: b0980(appA)
            ECJ: JW0963(appA)
            ECE: Z1397(appA)
            ECS: ECs1136
            ECC: c1121(appA)
            ECI: UTI89_C1049(appA)
            ECP: ECP_0985
            ECV: APECO1_84(appA)
            ECW: EcE24377A_1096(appA)
            ECX: EcHS_A1089
            YPE: YPO1648
            YPK: y1810(appA)
            YPM: YP_1778(appA)
            YPA: YPA_1875
            YPN: YPN_1982
            YPP: YPDSF_1799
            YPS: YPTB2421
            YPI: YpsIP31758_1622(appA)
            SFL: SF0982(appA)
            SFX: S1048(appA)
            SFV: SFV_0989(appA)
            SSN: SSON_0987(appA)
            SBO: SBO_2250(appA)
            SDY: SDY_0956(appA)
            SPE: Spro_2916
            ASU: Asuc_1115
            XCC: XCC0760(appA)
            XCB: XC_3473
            XCV: XCV0590(appA) XCV0864(appA) XCV4225
            XAC: XAC0557(appA) XAC0812(appA) XAC4132(appA)
            XOO: XOO3792(appA)
            XOM: XOO_3574(XOO3574)
            PSB: Psyr_4500
            PMY: Pmen_4375
            GUR: Gura_1189 Gura_2285
            SMD: Smed_3647 Smed_5167
            OAN: Oant_2957 Oant_4615
            XAU: Xaut_3381
            SWI: Swit_3853
            GOX: GOX1076
            GBE: GbCGDNIH1_1410 GbCGDNIH1_1412
            BCY: Bcer98_1436 Bcer98_1532 Bcer98_1935
            SAJ: SaurJH9_0989
            SAH: SaurJH1_1008
            KRA: Krad_1125
            STP: Strop_2461 Strop_2462 Strop_3796 Strop_3823
            FJO: Fjoh_1718
            TPT: Tpet_0460
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.26
            ExPASy - ENZYME nomenclature database: 3.1.3.26
            ExplorEnz - The Enzyme Database: 3.1.3.26
            ERGO genome analysis and discovery system: 3.1.3.26
            BRENDA, the Enzyme Database: 3.1.3.26
            CAS: 9001-89-2
///
ENTRY       EC 3.1.3.27                 Enzyme
NAME        phosphatidylglycerophosphatase;
            phosphatidylglycerol phosphate phosphatase;
            phosphatidylglycerol phosphatase;
            PGP phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     phosphatidylglycerophosphate phosphohydrolase
REACTION    phosphatidylglycerophosphate + H2O = phosphatidylglycerol +
            phosphate [RN:R02029]
ALL_REAC    R02029
SUBSTRATE   phosphatidylglycerophosphate [CPD:C03892];
            H2O [CPD:C00001]
PRODUCT     phosphatidylglycerol [CPD:C00344];
            phosphate [CPD:C00009]
REFERENCE   1  [PMID:4292860]
  AUTHORS   Chang YY, Kennedy EP.
  TITLE     Phosphatidyl glycerophosphate phosphatase.
  JOURNAL   J. Lipid. Res. 8 (1967) 456-62.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K01094  phosphatidylglycerophosphatase
            KO: K01095  phosphatidylglycerophosphatase A
            KO: K01096  phosphatidylglycerophosphatase B
GENES       ECO: b0418(pgpA) b1278(pgpB)
            ECJ: JW0408(pgpA) JW1270(pgpB)
            ECE: Z0520(pgpA) Z2529(pgpB)
            ECS: ECs0471 ECs1851
            ECC: c0529(pgpA) c1747(pgpB)
            ECI: UTI89_C0441(pgpA) UTI89_C1549(pgpB)
            ECP: ECP_0477 ECP_1331
            ECV: APECO1_1592(pgpA) APECO1_438(pgpB)
            ECW: EcE24377A_0449(pgpA) EcE24377A_1480(pgpB)
            ECX: EcHS_A0489 EcHS_A1389
            STY: STY0459 STY1341(pgpB)
            STT: t1623(pgpB) t2443
            SPT: SPA1166(pgpB) SPA2303(pgpA)
            SEC: SC0461(pgpA) SC1705(pgpB)
            STM: STM0420(pgpA) STM1710(pgpB)
            YPE: YPO2223(pgpB) YPO3179(pgpA)
            YPK: y1004(pgpA) y2065(pgpB)
            YPM: YP_0752(pgpA) YP_2022(pgpB5)
            YPA: YPA_1583 YPA_2673
            YPN: YPN_0909 YPN_1692
            YPP: YPDSF_0911 YPDSF_2814
            YPS: YPTB0938(pgpA) YPTB2145(pgpB)
            SFL: SF0355(pgpA) SF1282(pgpB)
            SFX: S0363(pgpA) S1365(pgpB)
            SFV: SFV_0383(pgpA) SFV_1291(pgpB)
            SSN: SSON_0395(pgpA) SSON_1862(pgpB)
            SBO: SBO_0312(pgpA) SBO_1786(pgpB)
            SDY: SDY_0316(pgpA) SDY_1354(pgpB)
            ECA: ECA1130(pgpA) ECA1944(pgpB)
            PLU: plu3895(pgpA)
            WBR: WGLp466(pgpA)
            SGL: SG0655 SG1411
            ENT: Ent638_2190
            SPE: Spro_2652
            BFL: Bfl237(pgpA)
            BPN: BPEN_243(pgpA)
            HIN: HI0211(pgpB) HI1306(pgpA)
            HIT: NTHI0308(pgpB) NTHI1619(pgpA)
            HDU: HD0437(pgpA) HD1199(pgpB)
            HSO: HS_0833(pgpA) HS_1042(pgpB)
            PMU: PM0676(pdpB) PM0728(pgpA)
            MSU: MS0973(pgpA) MS1532(pgpB)
            APL: APL_0203(pgpA) APL_0417(pgpB)
            ASU: Asuc_1503
            VCH: VC2265 VCA0035
            VCO: VC0395_A1855(pgpA)
            VVU: VV1_0316 VV2_1432
            VVY: VV0867 VVA0266
            VPA: VP0685 VPA0129
            VFI: VF0706 VF1544
            PPR: PBPRA0803 PBPRA1902
            PAE: PA4050(pg)
            PAU: PA14_11470(pgpA)
            PPU: PP_0520(pgpA)
            PFL: PFL_5516
            PFO: Pfl_5013
            PEN: PSEEN0594(pgpA)
            PAR: Psyc_2072(pgpA)
            PCR: Pcryo_2395
            ACI: ACIAD0554 ACIAD2942 ACIAD3574(pgpA)
            SON: SO_3463(pgpA) SO_4335
            SDN: Sden_1150
            SFR: Sfri_1041
            SAZ: Sama_1022
            SBL: Sbal_3154
            SLO: Shew_1193
            SPC: Sputcn32_2772
            SHE: Shewmr4_0369 Shewmr4_1102
            SHM: Shewmr7_1168 Shewmr7_3657
            SHN: Shewana3_0364 Shewana3_1102 Shewana3_3063
            SHW: Sputw3181_1240
            ILO: IL2139(pgpA)
            CPS: CPS_1534(pgpA)
            PHA: PSHAa2368
            PAT: Patl_1317
            SDE: Sde_3452
            MAQ: Maqu_0848
            LPN: lpg0729(pgpA)
            LPF: lpl0766(pgpA)
            LPP: lpp0795(pgpA)
            MCA: MCA1652(pgpA)
            TCX: Tcr_0915
            NOC: Noc_0805
            AEH: Mlg_0390
            HCH: HCH_05951
            CSA: Csal_2580
            ABO: ABO_2168(pgpA)
            AHA: AHA_2684 AHA_3326
            DNO: DNO_0668(pgpA)
            BCI: BCI_0605(pgpA)
            NME: NMB0386
            NMA: NMA2102(pgpA)
            NMC: NMC1781(pgpA)
            NGO: NGO1574
            CVI: CV_2393(pgpA)
            RSO: RSc2769(pgpA)
            REU: Reut_A2849
            REH: H16_A3155(pgpA)
            RME: Rmet_3048
            BMA: BMA2479
            BXE: Bxe_A0555
            BUR: Bcep18194_A3711
            BCN: Bcen_0146
            BCH: Bcen2424_0629
            BAM: Bamb_0530
            BPS: BPSL2961
            BPM: BURPS1710b_3476
            BTE: BTH_I1187
            BPE: BP3488
            BPA: BPP0861
            BBR: BB0955
            RFR: Rfer_0077
            POL: Bpro_4475
            MPT: Mpe_A0211
            HAR: HEAR0641(pgpA)
            MMS: mma_0608
            NEU: NE2560(pgpA)
            NET: Neut_2520
            NMU: Nmul_A0014
            EBA: ebA3402(pgpA) p1B319(pgpA)
            AZO: azo0509
            DAR: Daro_3741
            TBD: Tbd_2194
            MFA: Mfla_0572
            HPY: HP0737
            HPJ: jhp0674(pgpA)
            HPA: HPAG1_0721 HPAG1_0834
            HHE: HH1584(pgpA)
            HAC: Hac_0682(pgpA)
            WSU: WS1937(pgpA)
            TDN: Tmden_1490
            CJE: Cj1610(pgpA)
            CJR: CJE1782(pgpA)
            CJJ: CJJ81176_1597(pgpA)
            CJU: C8J_1511(pgpA)
            CJD: JJD26997_1964(pgpA)
            CCV: CCV52592_0199(pgpA)
            CHA: CHAB381_0994(pgpA)
            CCO: CCC13826_0387 CCC13826_1464(pgpA)
            ABU: Abu_0128(pgpA)
            NIS: NIS_0592(pgpA)
            SUN: SUN_0519
            GSU: GSU0142(pgpA)
            GME: Gmet_0195
            PCA: Pcar_2402
            DVU: DVU0528
            DDE: Dde_0641
            LIP: LI0564(pgpA)
            BBA: Bd0509(pgpA)
            DPS: DP0749
            ADE: Adeh_3613
            SAT: SYN_02031
            SFU: Sfum_2321
            RPR: RP750(pgpA)
            RTY: RT0735(pgpA)
            RCO: RC1161(pgpA)
            RFE: RF_1197(pgpA)
            RBE: RBE_1409(pgpA)
            OTS: OTBS_0342(pgpA)
            WOL: WD0730
            AMA: AM305(pgpA)
            APH: APH_0974(pgpA)
            ERU: Erum1980(pgpA)
            ERW: ERWE_CDS_02000(pgpA)
            ERG: ERGA_CDS_01950(pgpA)
            ECN: Ecaj_0200
            ECH: ECH_0905(pgpA)
            NSE: NSE_0292(pgpA)
            PUB: SAR11_0944(pgpA)
            BME: BMEI1212 BMEII1103
            SIL: SPO2091
            SIT: TM1040_1365
            RSP: RSP_2834(pgpA)
            JAN: Jann_2234
            RDE: RD1_2768(pgpA)
            GBE: GbCGDNIH1_1193
            RRU: Rru_A1869
            MAG: amb2547
            MGM: Mmc1_0491
            ABA: Acid345_2142
            BAN: BA1301
            BAR: GBAA1301
            BAA: BA_1828
            BAT: BAS1203
            BCE: BC1290 BC2260
            BCA: BCE_1402
            BCZ: BCZK1183(pbpB) BCZK2088(pgpB) BCZK4512(pgpB)
            BTK: BT9727_1181(pbpB) BT9727_2092(pgpB) BT9727_4494(pgpB)
            BTL: BALH_4336(pgpB)
            BCL: ABC3193
            BPU: BPUM_1917 BPUM_2891
            GKA: GK1433
            SAA: SAUSA300_1310
            SPZ: M5005_Spy_1560
            SPH: MGAS10270_Spy1627
            SPI: MGAS10750_Spy1619
            SPJ: MGAS2096_Spy1585
            SPK: MGAS9429_Spy1565
            SPA: M6_Spy1572
            SPB: M28_Spy1548
            LSL: LSL_0923(pgpB) LSL_1484(pgpB)
            FNU: FN1930
            BTH: BT_1525
            CTE: CT0336(pgpA)
            CCH: Cag_1418
            PLT: Plut_0449
            AAE: aq_314
            NPH: NP0190A NP2984A
            PAB: PAB2021
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.27
            ExPASy - ENZYME nomenclature database: 3.1.3.27
            ExplorEnz - The Enzyme Database: 3.1.3.27
            ERGO genome analysis and discovery system: 3.1.3.27
            BRENDA, the Enzyme Database: 3.1.3.27
            CAS: 9033-46-9
///
ENTRY       EC 3.1.3.28                 Enzyme
NAME        ADP-phosphoglycerate phosphatase;
            adenosine diphosphate phosphoglycerate phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     3-(ADP)-2-phosphoglycerate phosphohydrolase
REACTION    3-(ADP)-2-phosphoglycerate + H2O = 3-(ADP)-glycerate + phosphate
            [RN:R03969]
ALL_REAC    R03969
SUBSTRATE   3-(ADP)-2-phosphoglycerate [CPD:C03673];
            H2O [CPD:C00001]
PRODUCT     3-(ADP)-glycerate [CPD:C02509];
            phosphate [CPD:C00009]
COMMENT     Also acts on 2,3-bisphosphoglycerate.
REFERENCE   1
  AUTHORS   Zancan, G.T., Recondo, E.F. and Leloir, L.F.
  TITLE     Enzymic dephosphorylation of adenosine diphosphate phosphoglyceric
            acid.
  JOURNAL   Biochim. Biophys. Acta 92 (1964) 125-131.
  ORGANISM  rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.28
            ExPASy - ENZYME nomenclature database: 3.1.3.28
            ExplorEnz - The Enzyme Database: 3.1.3.28
            ERGO genome analysis and discovery system: 3.1.3.28
            BRENDA, the Enzyme Database: 3.1.3.28
            CAS: 37288-12-3
///
ENTRY       EC 3.1.3.29                 Enzyme
NAME        N-acylneuraminate-9-phosphatase;
            acylneuraminate 9-phosphatase;
            N-acylneuraminic acid 9-phosphate phosphatase;
            N-acylneuraminic (sialic) acid 9-phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     N-acylneuraminate-9-phosphate phosphohydrolase
REACTION    N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate
            [RN:R02597]
ALL_REAC    R02597 > R01805
SUBSTRATE   N-acylneuraminate 9-phosphate [CPD:C01200];
            H2O [CPD:C00001]
PRODUCT     N-acylneuraminate [CPD:C00591];
            phosphate [CPD:C00009]
REFERENCE   1
  AUTHORS   Jourdian, G.W., Swanson, A., Watson, D. and Roseman, S.
  TITLE     N-Acetylneuraminic (sialic) acid 9-phosphatase.
  JOURNAL   Methods Enzymol. 8 (1966) 205-208.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K01097  N-acylneuraminate-9-phosphatase
GENES       FNU: FN0213
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.29
            ExPASy - ENZYME nomenclature database: 3.1.3.29
            ExplorEnz - The Enzyme Database: 3.1.3.29
            ERGO genome analysis and discovery system: 3.1.3.29
            BRENDA, the Enzyme Database: 3.1.3.29
            CAS: 37288-13-4
///
ENTRY       EC 3.1.3.30       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
COMMENT     Deleted entry: 3'-phosphoadenylylsulfate 3'-phosphatase. Now
            included with EC 3.1.3.7 3'(2'),5'-bisphosphate nucleotidase (EC
            3.1.3.30 created 1972, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.30
            ExPASy - ENZYME nomenclature database: 3.1.3.30
            ExplorEnz - The Enzyme Database: 3.1.3.30
            ERGO genome analysis and discovery system: 3.1.3.30
            BRENDA, the Enzyme Database: 3.1.3.30
///
ENTRY       EC 3.1.3.31                 Enzyme
NAME        nucleotidase;
            nucleotide phosphatase;
            nucleotide-specific phosphatase;
            NSP I;
            NSP II;
            deoxyribonucleoside-activated nucleotidase (DAN);
            deoxyinosine-activated nucleotidase (DIAN);
            acid nucleotidase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     nucleotide phosphohydrolase
REACTION    a nucleotide + H2O = a nucleoside + phosphate [RN:R01572]
ALL_REAC    R01572
SUBSTRATE   nucleotide [CPD:C00215];
            H2O [CPD:C00001]
PRODUCT     nucleoside [CPD:C00801];
            phosphate [CPD:C00009]
COMMENT     A wide specificity for 2', 3'- and 5'- nucleotides; also hydrolyses
            glycerol phosphate and 4-nitrophenyl phosphate.
REFERENCE   1  [PMID:5699060]
  AUTHORS   Arsenis C, Touster O.
  TITLE     Purification and properties of an acid nucleotidase from rat liver
            lysosomes.
  JOURNAL   J. Biol. Chem. 243 (1968) 5702-8.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.31
            ExPASy - ENZYME nomenclature database: 3.1.3.31
            ExplorEnz - The Enzyme Database: 3.1.3.31
            ERGO genome analysis and discovery system: 3.1.3.31
            BRENDA, the Enzyme Database: 3.1.3.31
            CAS: 9033-33-4
///
ENTRY       EC 3.1.3.32                 Enzyme
NAME        polynucleotide 3'-phosphatase;
            2'(3')-polynucleotidase;
            DNA 3'-phosphatase;
            deoxyribonucleate 3'-phosphatase;
            5'-polynucleotidekinase 3'-phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     polynucleotide 3'-phosphohydrolase
REACTION    a 3'-phosphopolynucleotide + H2O = a polynucleotide + phosphate
            [RN:R02248]
ALL_REAC    R02248
SUBSTRATE   3'-phosphopolynucleotide [CPD:C03463];
            H2O [CPD:C00001]
PRODUCT     polynucleotide [CPD:C00419];
            phosphate [CPD:C00009]
COMMENT     Also hydrolyses nucleoside 2'-, 3'- and 5'-monophosphates, but only
            2'- and 3'-phosphopolynucleotides.
REFERENCE   1  [PMID:4289819]
  AUTHORS   Becker A, Hurwitz J.
  TITLE     The enzymatic cleavage of phosphate termini from polynucleotides.
  JOURNAL   J. Biol. Chem. 242 (1967) 936-50.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K08075  polynucleotide 3'-phosphatase
GENES       HSA: 11284(PNKP)
            MMU: 59047(Pnkp)
            RNO: 308576(Pnkp)
            CFA: 484373(PNKP)
            SPU: 586494(LOC586494)
            DME: Dmel_CG9601
            CEL: F21D5.5
            SCE: YMR156C(TPP1)
            CAL: CaO19_1547(CaO19.1547)
            CGR: CAGL0M09636g
            SPO: SPAC23C11.04c
            ANI: AN5751.2
            AFM: AFUA_6G06820
            AOR: AO090003000060
STRUCTURES  PDB: 1UJX  2BRF  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.32
            ExPASy - ENZYME nomenclature database: 3.1.3.32
            ExplorEnz - The Enzyme Database: 3.1.3.32
            ERGO genome analysis and discovery system: 3.1.3.32
            BRENDA, the Enzyme Database: 3.1.3.32
            CAS: 37288-16-7
///
ENTRY       EC 3.1.3.33                 Enzyme
NAME        polynucleotide 5'-phosphatase;
            5'-polynucleotidase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     polynucleotide 5'-phosphohydrolase
REACTION    a 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate
            [RN:R02249]
ALL_REAC    R02249
SUBSTRATE   5'-phosphopolynucleotide [CPD:C03475];
            H2O [CPD:C00001]
PRODUCT     polynucleotide [CPD:C00419];
            phosphate [CPD:C00009]
COMMENT     Does not act on nucleoside monophosphates. Induced in Escherichia
            coli by T-even phages.
REFERENCE   1  [PMID:4289819]
  AUTHORS   Becker A, Hurwitz J.
  TITLE     The enzymatic cleavage of phosphate termini from polynucleotides.
  JOURNAL   J. Biol. Chem. 242 (1967) 936-50.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01098  polynucleotide 5'-phosphatase
GENES       HSA: 8732(RNGTT)
            PTR: 462878(RNGTT)
            MMU: 24018(Rngtt)
            RNO: 313131(Rngtt_predicted)
            CFA: 481914(RNGTT)
            BTA: 511408(LOC511408)
            GGA: 421819(RNGTT)
            SCE: YMR180C(CTL1) YPL228W(CET1)
            AGO: AGOS_AFL134W
            CGR: CAGL0E06050g
            SPO: SPAC644.04
            UMA: UM04672.1
STRUCTURES  PDB: 1D8H  1D8I  1I9S  1I9T  1YN9  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.33
            ExPASy - ENZYME nomenclature database: 3.1.3.33
            ExplorEnz - The Enzyme Database: 3.1.3.33
            ERGO genome analysis and discovery system: 3.1.3.33
            BRENDA, the Enzyme Database: 3.1.3.33
            CAS: 37288-17-8
///
ENTRY       EC 3.1.3.34                 Enzyme
NAME        deoxynucleotide 3'-phosphatase;
            3'-deoxynucleotidase;
            3'-deoxyribonucleotidase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     deoxyribonucleotide 3'-phosphohydrolase
REACTION    a deoxynucleoside 3'-phosphate + H2O = a deoxynucleoside + phosphate
            [RN:R02751]
ALL_REAC    R02751
SUBSTRATE   deoxynucleoside 3'-phosphate [CPD:C00675];
            H2O [CPD:C00001]
PRODUCT     deoxynucleoside [CPD:C02269];
            phosphate [CPD:C00009]
COMMENT     Also catalyses the selective removal of 3'-phosphate groups from DNA
            and oligodeoxynucleotides. Induced in Escherichia coli by T-even
            phages.
REFERENCE   1  [PMID:4289819]
  AUTHORS   Becker A, Hurwitz J.
  TITLE     The enzymatic cleavage of phosphate termini from polynucleotides.
  JOURNAL   J. Biol. Chem. 242 (1967) 936-50.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.34
            ExPASy - ENZYME nomenclature database: 3.1.3.34
            ExplorEnz - The Enzyme Database: 3.1.3.34
            ERGO genome analysis and discovery system: 3.1.3.34
            BRENDA, the Enzyme Database: 3.1.3.34
            CAS: 37288-18-9
///
ENTRY       EC 3.1.3.35                 Enzyme
NAME        thymidylate 5'-phosphatase;
            thymidylate 5'-nucleotidase;
            deoxythymidylate 5'-nucleotidase;
            thymidylate nucleotidase;
            deoxythymidylic 5'-nucleotidase;
            deoxythymidylate phosphohydrolase;
            dTMPase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     thymidylate 5'-phosphohydrolase
REACTION    thymidylate + H2O = thymidine + phosphate [RN:R01569]
ALL_REAC    R01569
SUBSTRATE   thymidylate [CPD:C00364];
            H2O [CPD:C00001]
PRODUCT     thymidine [CPD:C00214];
            phosphate [CPD:C00009]
COMMENT     Acts on 5-methyl-dCMP and on TMP, but more slowly than on dTMP.
REFERENCE   1  [PMID:4958986]
  AUTHORS   Aposhian HV, Tremblay GY.
  TITLE     Deoxythymidylate 5'-nucleotidase. Purification and properties of an
            enzyme found after infection of Bacillus subtilis with phage SP5C.
  JOURNAL   J. Biol. Chem. 241 (1966) 5095-101.
  ORGANISM  Bacillus subtilis [GN:bsu]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.35
            ExPASy - ENZYME nomenclature database: 3.1.3.35
            ExplorEnz - The Enzyme Database: 3.1.3.35
            ERGO genome analysis and discovery system: 3.1.3.35
            BRENDA, the Enzyme Database: 3.1.3.35
            CAS: 9026-80-6
///
ENTRY       EC 3.1.3.36                 Enzyme
NAME        phosphoinositide 5-phosphatase;
            type II inositol polyphosphate 5-phosphatase;
            triphosphoinositide phosphatase;
            IP3 phosphatase;
            PtdIns(4,5)P2 phosphatase;
            triphosphoinositide phosphomonoesterase;
            diphosphoinositide phosphatase;
            inositol 1,4,5-triphosphate 5-phosphomonoesterase;
            inositol triphosphate 5-phosphomonoesterase;
            phosphatidylinositol-bisphosphatase;
            phosphatidyl-myo-inositol-4,5-bisphosphate phosphatase;
            phosphatidylinositol 4,5-bisphosphate phosphatase;
            polyphosphoinositol lipid 5-phosphatase;
            phosphatidyl-inositol-bisphosphate phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     phosphatidyl-myo-inositol-4,5-bisphosphate 4-phosphohydrolase
REACTION    1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O =
            1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate [RN:R04404]
ALL_REAC    R04404
SUBSTRATE   1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [CPD:C04637];
            H2O [CPD:C00001]
PRODUCT     1-phosphatidyl-1D-myo-inositol 4-phosphate [CPD:C01277];
            phosphate [CPD:C00009]
COMMENT     These enzymes can also remove the 5-phosphate from Ins(1,4,5)P3
            and/or Ins(1,3,4,5)P4. They are a diverse family of enzymes, with
            differing abilities to catalyse two or more of the four reactions
            listed. They are thought to use inositol lipids rather than inositol
            phosphates as substrates in vivo. All of them can use either or both
            of PtdIns(4,5)P2 and PtdIns(3,4,5)P3 as substrates; this is the main
            property that distinguishes them from EC 3.1.3.56,
            inositol-polyphosphate 5-phosphatase.
REFERENCE   1  [PMID:4284485]
  AUTHORS   Dawson RM, Thompson W.
  TITLE     The triphosphoinositide phosphomonoesterase of brain tissue.
  JOURNAL   Biochem. J. 91 (1964) 244-50.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:6271223]
  AUTHORS   Roach PD, Palmer FB.
  TITLE     Human erythrocyte cytosol phosphatidyl-inositol-bisphosphate
            phosphatase.
  JOURNAL   Biochim. Biophys. Acta. 661 (1981) 323-33.
  ORGANISM  human [GN:hsa]
REFERENCE   3
  AUTHORS   Woscholski, R. and Parker, P.J.
  TITLE     Inositol phosphatases: constructive destruction of phosphoinositides
            and inositol phosphates.
  JOURNAL   In: Cockcroft, S. (Ed.), Biology of Phosphoinositides, Biology of
            Phosphoinositides, Oxford, 2000, p. 320-338.
PATHWAY     PATH: map00562  Inositol phosphate metabolism
            PATH: map04070  Phosphatidylinositol signaling system
ORTHOLOGY   KO: K01099  phosphatidylinositol-bisphosphatase
GENES       HSA: 114971(PTPMT1) 3633(INPP5B) 4952(OCRL) 56623(INPP5E)
                 8867(SYNJ1) 8871(SYNJ2)
            PTR: 473959(SYNJ1)
            MMU: 104015(Synj1) 20975(Synj2) 320634(Ocrl) 64436(Inpp5e)
            RNO: 85238(Synj1)
            CFA: 478403(SYNJ1) 484052(SYNJ2) 492123(OCRL) 607443(INPP5E)
            BTA: 282087(SYNJ1)
            GGA: 417135(INPP5E) 418498(SYNJ1) 419609(INPP5B)
            TET: TTHERM_00035480 TTHERM_00079570 TTHERM_00621470
            TBR: Tb11.02.3170
            EHI: 13.t00027
            ECI: UTI89_C2744(zipA)
STRUCTURES  PDB: 1UFW  1W80  2DNR  2QV2  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.36
            ExPASy - ENZYME nomenclature database: 3.1.3.36
            ExplorEnz - The Enzyme Database: 3.1.3.36
            ERGO genome analysis and discovery system: 3.1.3.36
            BRENDA, the Enzyme Database: 3.1.3.36
            CAS: 9036-01-5
///
ENTRY       EC 3.1.3.37                 Enzyme
NAME        sedoheptulose-bisphosphatase;
            SBPase;
            sedoheptulose 1,7-diphospate phosphatase;
            sedoheptulose 1,7-diphosphatase;
            sedoheptulose diphosphatase;
            sedoheptulose bisphosphatase;
            sedoheptulose 1,7-bisphosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     sedoheptulose-1,7-bisphosphate 1-phosphohydrolase
REACTION    sedoheptulose 1,7-bisphosphate + H2O = sedoheptulose 7-phosphate +
            phosphate [RN:R01845]
ALL_REAC    R01845
SUBSTRATE   sedoheptulose 1,7-bisphosphate;
            H2O [CPD:C00001]
PRODUCT     sedoheptulose 7-phosphate [CPD:C00281];
            phosphate [CPD:C00009]
REFERENCE   1
  AUTHORS   Racker, E.
  TITLE     Sedoheptulose-1,7-diphosphatase from yeast.
  JOURNAL   Methods Enzymol. 5 (1962) 270-272.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:4329855]
  AUTHORS   Traniello S, Calcagno M, Pontremoli S.
  TITLE     Fructose 1,6-diphosphatase and sedoheptulose 1,7-diphosphatase from
            Candida utilis: purification and properties.
  JOURNAL   Arch. Biochem. Biophys. 146 (1971) 603-10.
  ORGANISM  Candida utilis
PATHWAY     PATH: map00710  Carbon fixation
ORTHOLOGY   KO: K01100  sedoheptulose-bisphosphatase
GENES       ATH: AT3G55800(SBPASE)
            OSA: 4335227
            CME: CMI196C CMT362C
            TBR: Tb927.2.5800
            BAN: BA5195(fbp-1)
            BAR: GBAA5195(fbp-1)
            BCE: BC4962
            CJK: jk1453(fbp)
            SYR: SynRCC307_1255(glpX)
            SYX: SynWH7803_1300(glpX)
            PMB: A9601_08291(glpX)
            PMG: P9301_08271(glpX)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.37
            ExPASy - ENZYME nomenclature database: 3.1.3.37
            ExplorEnz - The Enzyme Database: 3.1.3.37
            ERGO genome analysis and discovery system: 3.1.3.37
            BRENDA, the Enzyme Database: 3.1.3.37
            CAS: 9055-32-7
///
ENTRY       EC 3.1.3.38                 Enzyme
NAME        3-phosphoglycerate phosphatase;
            D-3-Phosphoglycerate phosphatase;
            3-PGA phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     D-glycerate-3-phosphate phosphohydrolase
REACTION    D-glycerate 3-phosphate + H2O = D-glycerate + phosphate [RN:R01511]
ALL_REAC    R01511
SUBSTRATE   D-glycerate 3-phosphate [CPD:C00197];
            H2O [CPD:C00001]
PRODUCT     D-glycerate [CPD:C00258];
            phosphate [CPD:C00009]
COMMENT     Wide specificity, but 3-phosphoglycerate is the best substrate.
REFERENCE   1  [PMID:10970181]
  AUTHORS   Randall DD, Tolbert NE.
  TITLE     3-Phosphoglycerate phosphatase in plants. I. Isolation and
            characterization from sugarcane leaves.
  JOURNAL   J. Biol. Chem. 246 (1971) 5510-7.
  ORGANISM  Saccharum officinarum [GN:esof]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.38
            ExPASy - ENZYME nomenclature database: 3.1.3.38
            ExplorEnz - The Enzyme Database: 3.1.3.38
            ERGO genome analysis and discovery system: 3.1.3.38
            BRENDA, the Enzyme Database: 3.1.3.38
            CAS: 62213-13-2
///
ENTRY       EC 3.1.3.39                 Enzyme
NAME        streptomycin-6-phosphatase;
            streptomycin 6-phosphate phosphatase;
            streptomycin 6-phosphate phosphohydrolase;
            streptomycin-6-P phosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     streptomycin-6-phosphate phosphohydrolase
REACTION    streptomycin 6-phosphate + H2O = streptomycin + phosphate
            [RN:R02228]
ALL_REAC    R02228
SUBSTRATE   streptomycin 6-phosphate [CPD:C01138];
            H2O [CPD:C00001]
PRODUCT     streptomycin [CPD:C00413];
            phosphate [CPD:C00009]
COMMENT     Also acts on dihydrostreptomycin 3'alpha,6-bisphosphate and
            streptidine 6-phosphate.
REFERENCE   1  [PMID:4121457]
  AUTHORS   Walker JB, Skorvaga M.
  TITLE     Streptomycin biosynthesis and metabolism. Phosphate transfer from
            dihydrostreptomycin 6-phosphate to inosamines, streptamine, and
            2-deoxystreptamine.
  JOURNAL   J. Biol. Chem. 248 (1973) 2441-6.
  ORGANISM  Streptomyces bikiniensis
REFERENCE   2  [PMID:4331203]
  AUTHORS   Walker MS, Walker JB.
  TITLE     Streptomycin biosynthesis. Separation and substrate specificities of
            phosphatases acting on guanidinodeoxy-scyllo-inositol phosphate and
            streptomycin-(streptidino)phosphate.
  JOURNAL   J. Biol. Chem. 246 (1971) 7034-40.
  ORGANISM  Streptomyces bikiniensis
PATHWAY     PATH: map00521  Streptomycin biosynthesis
ORTHOLOGY   KO: K04342  streptomycin-6-phosphatase
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.39
            ExPASy - ENZYME nomenclature database: 3.1.3.39
            ExplorEnz - The Enzyme Database: 3.1.3.39
            ERGO genome analysis and discovery system: 3.1.3.39
            BRENDA, the Enzyme Database: 3.1.3.39
            CAS: 9055-33-8
///
ENTRY       EC 3.1.3.40                 Enzyme
NAME        guanidinodeoxy-scyllo-inositol-4-phosphatase;
            1-guanidino-scyllo-inositol 4-phosphatase;
            1-guanidino-1-deoxy-scyllo-inositol-4-P phosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     1-guanidino-1-deoxy-scyllo-inositol-4-phosphate 4-phosphohydrolase
REACTION    1-guanidino-1-deoxy-scyllo-inositol 4-phosphate + H2O =
            1-guanidino-1-deoxy-scyllo-inositol + phosphate [RN:R03496]
ALL_REAC    R03496
SUBSTRATE   1-guanidino-1-deoxy-scyllo-inositol 4-phosphate [CPD:C01294];
            H2O [CPD:C00001]
PRODUCT     1-guanidino-1-deoxy-scyllo-inositol [CPD:C04280];
            phosphate [CPD:C00009]
REFERENCE   1  [PMID:4331203]
  AUTHORS   Walker MS, Walker JB.
  TITLE     Streptomycin biosynthesis. Separation and substrate specificities of
            phosphatases acting on guanidinodeoxy-scyllo-inositol phosphate and
            streptomycin-(streptidino)phosphate.
  JOURNAL   J. Biol. Chem. 246 (1971) 7034-40.
  ORGANISM  Streptomyces galbus, Streptomyces griseocarneus, Streptomyces
            griseus
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.40
            ExPASy - ENZYME nomenclature database: 3.1.3.40
            ExplorEnz - The Enzyme Database: 3.1.3.40
            ERGO genome analysis and discovery system: 3.1.3.40
            BRENDA, the Enzyme Database: 3.1.3.40
            CAS: 9055-28-1
///
ENTRY       EC 3.1.3.41                 Enzyme
NAME        4-nitrophenylphosphatase;
            nitrophenyl phosphatase;
            p-nitrophenylphosphatase;
            para-nitrophenyl phosphatase;
            K-pNPPase;
            NPPase;
            PNPPase;
            Ecto-p-nitrophenyl phosphatase;
            p-nitrophenylphosphate phosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     4-nitrophenylphosphate phosphohydrolase
REACTION    4-nitrophenyl phosphate + H2O = 4-nitrophenol + phosphate
            [RN:R03024]
ALL_REAC    R03024
SUBSTRATE   4-nitrophenyl phosphate [CPD:C03360];
            H2O [CPD:C00001]
PRODUCT     4-nitrophenol [CPD:C00870];
            phosphate [CPD:C00009]
COMMENT     A number of other substances, including phenyl phosphate,
            4-nitrophenyl sulfate, acetyl phosphate and glycerol phosphate, are
            not substrates.
REFERENCE   1  [PMID:4554643]
  AUTHORS   Attias J, Bonnet JL.
  TITLE     A specific alkaline p-nitrophenylphosphatase activity from baker's
            yeast.
  JOURNAL   Biochim. Biophys. Acta. 268 (1972) 422-30.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:4357666]
  AUTHORS   Attias J, Durand H.
  TITLE     Further characterization of a specific p-nitrophenylphosphatase from
            baker's yeast.
  JOURNAL   Biochim. Biophys. Acta. 321 (1973) 561-8.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
ORTHOLOGY   KO: K01101  4-nitrophenyl phosphatase
GENES       MMU: 67078(1700012G19Rik)
            DME: Dmel_CG10352 Dmel_CG11291 Dmel_CG15739 Dmel_CG2680
                 Dmel_CG5567
            CEL: C53A3.2 F44E7.2(nitrophenylphosphatase)
                 K09H11.7(nitrophenylphosphatase)
            ATH: AT5G47760(ATPK5)
            OSA: 4336245 4346547
            CME: CMR421C
            SCE: YDL236W(PHO13)
            AGO: AGOS_ABL184W
            PIC: PICST_55335(PHO13)
            CAL: CaO19.4444
            CGR: CAGL0C05511g
            SPO: SPBC15D4.15(pho2)
            ANI: AN2970.2
            AFM: AFUA_3G08310 AFUA_4G01380
            AOR: AO090005001442
            CNE: CNB04360 CNB04450
            UMA: UM04979.1
            DDI: DDBDRAFT_0186160
            PFA: PF07_0059
            TET: TTHERM_00455490 TTHERM_01093670
            TBR: Tb927.8.7510
            TCR: 511439.100
            LMA: LmjF31.2340
            ECI: UTI89_C0669(nagD)
            BAN: BA5192
            BAR: GBAA5192
            BAT: BAS4827
            BCE: BC4959
            BCA: BCE_5096
            BCZ: BCZK4685
            BTK: BT9727_4668
            BLI: BL02140(yutF)
            BLD: BLi03418(yutF)
            BCL: ABC2945
            GKA: GK2968
            SAB: SAB0795
            LLC: LACR_1254
            SPZ: M5005_Spy_0767
            SPH: MGAS10270_Spy0884
            SPI: MGAS10750_Spy0919
            SPA: M6_Spy0792
            SPB: M28_Spy0746
            SAK: SAK_1015
            SSA: SSA_1077(nagD)
            LJO: LJ0498
            LAC: LBA0436
            LSA: LSA0432
            LCA: LSEI_0821
            LGA: LGAS_0444
            CJK: jk0862
            FNU: FN0048
            RBA: RB9200(nagD)
            AAE: aq_966
            PHO: PH1952
            PAB: PAB1056
            PFU: PF0432
            TKO: TK1734
            APE: APE_1605.1
            SSO: SSO2355(nagD-like)
            STO: ST0496
            SAI: Saci_0983
STRUCTURES  PDB: 1VJR  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.41
            ExPASy - ENZYME nomenclature database: 3.1.3.41
            ExplorEnz - The Enzyme Database: 3.1.3.41
            ERGO genome analysis and discovery system: 3.1.3.41
            BRENDA, the Enzyme Database: 3.1.3.41
            CAS: 9073-68-1
///
ENTRY       EC 3.1.3.42                 Enzyme
NAME        [glycogen-synthase-D] phosphatase;
            uridine diphosphoglucose-glycogen glucosyltransferase phosphatase;
            UDP-glycogen glucosyltransferase phosphatase;
            UDPglucose-glycogen glucosyltransferase phosphatase;
            glycogen glucosyltransferase phosphatase;
            glycogen synthetase phosphatase;
            glycogen synthase phosphatase;
            glycogen synthase D phosphatase;
            Mg2+ dependent glycogen synthase phosphatase;
            phosphatase type 2_degree_C
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     [UDP-glucose:glycogen 4-alpha-D-glucosyltransferase-D]
            phosphohydrolase
REACTION    [glycogen-synthase D] + H2O = [glycogen-synthase I] + phosphate
            [RN:R04156]
ALL_REAC    R04156
SUBSTRATE   [glycogen-synthase D] [CPD:C03185];
            H2O [CPD:C00001]
PRODUCT     [glycogen-synthase I] [CPD:C03186];
            phosphate [CPD:C00009]
COMMENT     The product is EC 2.4.1.11 glycogen(starch) synthase.
REFERENCE   1  [PMID:4367978]
  AUTHORS   Abe N, Tsuiki S.
  TITLE     Studies on glycogen synthase D phosphatase of rat liver--multiple
            nature.
  JOURNAL   Biochim. Biophys. Acta. 350 (1974) 383-91.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.42
            ExPASy - ENZYME nomenclature database: 3.1.3.42
            ExplorEnz - The Enzyme Database: 3.1.3.42
            ERGO genome analysis and discovery system: 3.1.3.42
            BRENDA, the Enzyme Database: 3.1.3.42
            CAS: 9043-28-1
///
ENTRY       EC 3.1.3.43                 Enzyme
NAME        [pyruvate dehydrogenase (acetyl-transferring)]-phosphatase;
            pyruvate dehydrogenase phosphatase;
            phosphopyruvate dehydrogenase phosphatase;
            [pyruvate dehydrogenase (lipoamide)]-phosphatase;
            [pyruvate dehydrogenase (lipoamide)]-phosphate phosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     [pyruvate dehydrogenase (acetyl-transferring)]-phosphate
            phosphohydrolase
REACTION    [pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O =
            [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
            [RN:R03450]
ALL_REAC    R03450
SUBSTRATE   [pyruvate dehydrogenase (acetyl-transferring)] phosphate
            [CPD:C01293];
            H2O [CPD:C00001]
PRODUCT     [pyruvate dehydrogenase (acetyl-transferring)] [CPD:C01256];
            phosphate [CPD:C00009]
COMMENT     A mitochondrial enzyme associated with EC 1.2.4.1 pyruvate
            dehydrogenase (acetyl-transferring), in the pyruvate dehydrogenase
            complex.
REFERENCE   1  [PMID:4401694]
  AUTHORS   Linn TC, Pelley JW, Pettit FH, Hucho F, Randall DD, Reed LJ.
  TITLE     -Keto acid dehydrogenase complexes. XV. Purification and properties
            of the component enzymes of the pyruvate dehydrogenase complexes
            from bovine kidney and heart.
  JOURNAL   Arch. Biochem. Biophys. 148 (1972) 327-42.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:3004826]
  AUTHORS   Reed LJ, Damuni Z, Merryfield ML.
  TITLE     Regulation of mammalian pyruvate and branched-chain alpha-keto acid
            dehydrogenase complexes by phosphorylation-dephosphorylation.
  JOURNAL   Curr. Top. Cell. Regul. 27 (1985) 41-9.
ORTHOLOGY   KO: K01102  pyruvate dehydrogenase phosphatase
GENES       HSA: 54704(PPM2C) 57546(PDP2)
            PTR: 472819(PPM2C)
            MMU: 382051(4833426J09Rik)
            RNO: 246311(Pdp2) 54705(Ppm2c)
            CFA: 477941(PPM2C) 489771(LOC489771)
            BTA: 280891(PDP)
            GGA: 427550(LOC427550) 428372(PPM2C)
            SPU: 584018(LOC584018)
            TET: TTHERM_00703440 TTHERM_00942970 TTHERM_01243430
STRUCTURES  PDB: 2PNQ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.43
            ExPASy - ENZYME nomenclature database: 3.1.3.43
            ExplorEnz - The Enzyme Database: 3.1.3.43
            ERGO genome analysis and discovery system: 3.1.3.43
            BRENDA, the Enzyme Database: 3.1.3.43
            CAS: 9073-70-5
///
ENTRY       EC 3.1.3.44                 Enzyme
NAME        [acetyl-CoA carboxylase]-phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]-phosphate
            phosphohydrolase
REACTION    [acetyl-CoA carboxylase] phosphate + H2O = [acetyl-CoA carboxylase]
            + phosphate [RN:R03273]
ALL_REAC    R03273
SUBSTRATE   [acetyl-CoA carboxylase] phosphate [CPD:C01247];
            H2O [CPD:C00001]
PRODUCT     [acetyl-CoA carboxylase] [CPD:C01139];
            phosphate [CPD:C00009]
COMMENT     Simultaneously dephosphorylates and activates EC 6.4.1.2 acetyl-CoA
            carboxylase. Acts similarly on EC 1.1.1.88
            (hydroxymethylglutaryl-CoA reductase), EC 2.4.1.1 (phosphorylase),
            EC 2.4.1.11 [glycogen(starch) synthase], and dephosphorylates
            phosphoprotamine and 4-nitrophenyl phosphate. Not identical to EC
            3.1.3.17 ([phosphorylase] phosphatase ) or EC 3.1.3.43 {[pyruvate
            dehydrogenase (acetyl-transferring)]-phosphatase}.
REFERENCE   1
  AUTHORS   Krakower, G.R. and Kim, K.-H.
  TITLE     Purification and properties of acetyl-CoA carboxylase phosphatase.
  JOURNAL   J. Biol. Chem. 256 (1980) 2408-2413.
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.44
            ExPASy - ENZYME nomenclature database: 3.1.3.44
            ExplorEnz - The Enzyme Database: 3.1.3.44
            ERGO genome analysis and discovery system: 3.1.3.44
            BRENDA, the Enzyme Database: 3.1.3.44
            CAS: 77000-10-3
///
ENTRY       EC 3.1.3.45                 Enzyme
NAME        3-deoxy-manno-octulosonate-8-phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     3-deoxy-D-manno-octulosonate-8-phosphate 8-phosphohydrolase
REACTION    3-deoxy-D-manno-octulosonate 8-phosphate + H2O =
            3-deoxy-D-manno-octulosonate + phosphate [RN:R03350]
ALL_REAC    R03350
SUBSTRATE   3-deoxy-D-manno-octulosonate 8-phosphate [CPD:C04478];
            H2O [CPD:C00001]
PRODUCT     3-deoxy-D-manno-octulosonate [CPD:C01187];
            phosphate [CPD:C00009]
REFERENCE   1  [PMID:6246070]
  AUTHORS   Ray PH, Benedict CD.
  TITLE     Purification and characterization of specific
            3-deoxy-D-manno-octulosonate 8-phosphate phosphatase from
            Escherichia coli B.
  JOURNAL   J. Bacteriol. 142 (1980) 60-8.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00540  Lipopolysaccharide biosynthesis
ORTHOLOGY   KO: K03270  3-deoxy-D-manno-octulosonate 8-phosphate phosphatase
                        (KDO 8-P phosphatase)
GENES       ECO: b3198(yrbI)
            ECJ: JW3165(kdsC)
            ECE: Z4561(yrbI)
            ECS: ECs4077
            ECC: c3958(yrbI)
            ECI: UTI89_C3634(yrbI)
            ECP: ECP_3286
            ECV: APECO1_3237(yrbI)
            ECW: EcE24377A_3686(kdsC)
            ECX: EcHS_A3391(kdsC)
            STY: STY3495
            STT: t3233
            SPT: SPA3183(yrbI)
            SEC: SC3254(yrbI)
            STM: STM3316(yrbI)
            YPE: YPO3578
            YPK: y0150
            YPM: YP_3833
            YPA: YPA_3725
            YPN: YPN_3460
            YPP: YPDSF_0319
            YPS: YPTB3522
            YPI: YpsIP31758_0445(kdsC)
            SFL: SF3238(yrbI)
            SFX: S3456(yrbI)
            SFV: SFV_3228(yrbI)
            SSN: SSON_3346(yrbI)
            SBO: SBO_3184(yrbI)
            SDY: SDY_3379(yrbI)
            ECA: ECA0292
            PLU: plu4037
            SGL: SG0203
            ENT: Ent638_3634
            KPN: KPN_03608(yrbI)
            SPE: Spro_4363
            HIN: HI1679(yrbI)
            HIT: NTHI1982(yrbI)
            HDU: HD0297
            HSO: HS_0919(kdsC)
            PMU: PM0524
            MSU: MS0995
            APL: APL_0051
            ASU: Asuc_1672
            XFA: XF1412
            XFT: PD0641
            XCC: XCC2798
            XCB: XC_1315
            XCV: XCV3114
            XAC: XAC2968
            XOO: XOO1288
            XOM: XOO_1187(XOO1187)
            VCH: VC2524
            VVU: VV1_0688
            VVY: VV0452
            VFI: VF0177 VF0391
            PPR: PBPRA3251
            PAE: PA4458
            PAU: PA14_57900
            PPU: PP_0956
            PPF: Pput_0995 Pput_3909
            PST: PSPTO_4449
            PSB: Psyr_4143
            PSP: PSPPH_4147
            PFL: PFL_0919(kdsC)
            PFO: Pfl_0861
            PEN: PSEEN1097
            PMY: Pmen_0874
            PAR: Psyc_0923
            PCR: Pcryo_1491
            PRW: PsycPRwf_0823
            ACI: ACIAD1483(kdsC)
            SON: SO_3957
            SDN: Sden_0493
            SFR: Sfri_3373
            SAZ: Sama_3084
            SBL: Sbal_3664
            SBM: Shew185_0690
            SLO: Shew_3307
            SPC: Sputcn32_0719
            SSE: Ssed_0730
            SPL: Spea_3612
            SHE: Shewmr4_0677
            SHM: Shewmr7_3345
            SHN: Shewana3_0676
            SHW: Sputw3181_3454
            ILO: IL0400
            CPS: CPS_4539
            PHA: PSHAa2547(kdsC)
            PAT: Patl_0564
            SDE: Sde_3175
            PIN: Ping_2888
            MAQ: Maqu_2711
            CBU: CBU_0749
            LPN: lpg0839
            LPF: lpl0870
            LPP: lpp0901
            MCA: MCA0745
            FTU: FTT1027c(yrbI)
            FTF: FTF1027c(yrbI)
            FTL: FTL_1062
            FTH: FTH_1038(kdsC)
            FTN: FTN_0905(yrbI)
            TCX: Tcr_0976
            NOC: Noc_2789
            AEH: Mlg_2226
            HHA: Hhal_2122
            HCH: HCH_05316
            CSA: Csal_2222
            MMW: Mmwyl1_1125
            AHA: AHA_3927
            RMA: Rmag_1043
            VOK: COSY_0943(kdsC)
            NME: NMB0353
            NMA: NMA2134
            NMC: NMC1815
            NGO: NGO1608
            CVI: CV_3328
            RSO: RSc0412(RS03380)
            BMA: BMA3103
            BXE: Bxe_A4118
            BVI: Bcep1808_2892
            BUR: Bcep18194_A6117 Bcep18194_C7391
            BCN: Bcen_2173
            BCH: Bcen2424_2787
            BAM: Bamb_2847
            BPS: BPSL0537 BPSL2771
            BPM: BURPS1710b_0769 BURPS1710b_3263
            BTE: BTH_I0490 BTH_I1361
            PNU: Pnuc_1908
            BPE: BP0700
            BPA: BPP4029
            BBR: BB4502
            RFR: Rfer_4236
            POL: Bpro_4897
            MPT: Mpe_A3808
            HAR: HEAR3105(kdsC)
            NMU: Nmul_A0088
            EBA: ebA1316 ebD6(ppcC)
            DAR: Daro_3419(kdsC)
            TBD: Tbd_0537(kdsC)
            MFA: Mfla_0138
            HPY: HP1570
            HPJ: jhp1478
            HPA: HPAG1_1519
            HHE: HH1326
            HAC: Hac_1677
            WSU: WS2069
            TDN: Tmden_1079
            CJE: Cj0647
            CJR: CJE0750
            CJU: C8J_0606
            CFF: CFF8240_1188
            CCV: CCV52592_0456
            CHA: CHAB381_0303
            CCO: CCC13826_1761
            ABU: Abu_0978
            GSU: GSU1892
            GME: Gmet_1279
            GUR: Gura_2976
            PCA: Pcar_1942
            PPD: Ppro_0970
            DVU: DVU1625
            DDE: Dde_1767(kdsC)
            LIP: LI0453
            BBA: Bd0827
            ADE: Adeh_4172
            MXA: MXAN_1094(kdsC)
            SAT: SYN_00949
            SFU: Sfum_2073
            RPE: RPE_4240
            MGM: Mmc1_3338
            ABA: Acid345_2842 Acid345_3769
            TFU: Tfu_0009
            RBA: RB9821
            SYW: SYNW0186
            SYC: syc1812_d
            SYF: Synpcc7942_2288
            SYD: Syncc9605_0182
            SYE: Syncc9902_0210
            SYR: SynRCC307_0286
            PMT: PMT1912
            PMF: P9303_25511
            BTH: BT_1677
            BFR: BF3282
            BFS: BF3121
            PGI: PG0658
            GFO: GFO_1811(kdsC)
            FPS: FP1420(kdsC)
            CTE: CT0087
            CCH: Cag_1073 Cag_1975
            PLT: Plut_2052(kdsC)
            AAE: aq_2171
            MAC: MA3766(neuA)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.45
            ExPASy - ENZYME nomenclature database: 3.1.3.45
            ExplorEnz - The Enzyme Database: 3.1.3.45
            ERGO genome analysis and discovery system: 3.1.3.45
            BRENDA, the Enzyme Database: 3.1.3.45
            CAS: 59088-24-3
///
ENTRY       EC 3.1.3.46                 Enzyme
NAME        fructose-2,6-bisphosphate 2-phosphatase;
            fructose-2,6-bisphosphatase;
            D-fructose-2,6-bisphosphate 2-phosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     beta-D-fructose-2,6-bisphosphate 2-phosphohydrolase
REACTION    beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate +
            phosphate [RN:R00763]
ALL_REAC    R00763 > R02731
SUBSTRATE   beta-D-fructose 2,6-bisphosphate [CPD:C00665];
            H2O [CPD:C00001]
PRODUCT     D-fructose 6-phosphate [CPD:C00085];
            phosphate [CPD:C00009]
COMMENT     The enzyme copurifies with EC 2.7.1.105 6-phosphofructo-2-kinase.
            (cf. EC 3.1.3.54 fructose-2,6-bisphosphate 6-phosphatase).
REFERENCE   1  [PMID:6282585]
  AUTHORS   van Schaftingen E, Davies DR, Hers HG.
  TITLE     Fructose-2,6-bisphosphatase from rat liver.
  JOURNAL   Eur. J. Biochem. 124 (1982) 143-9.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K01103  fructose-2,6-bisphosphatase
GENES       HSA: 5207(PFKFB1) 5208(PFKFB2) 5209(PFKFB3) 5210(PFKFB4)
            MMU: 170768(Pfkfb3) 18640(Pfkfb2) 270198(Pfkfb4)
            RNO: 117276(Pfkfb3) 24638(Pfkfb1) 24640(Pfkfb2) 54283(Pfkfb4)
            CFA: 484777(PFKFB4) 487139(PFKFB3) 491903(PFKFB1)
            BTA: 282304(PFKFB1) 287019(PFKFB2)
            GGA: 415906(PFKFB4) 418247(PFKFB3) 419850(PFKFB2)
            XLA: 432000(MGC81068) 495408(LOC495408)
            XTR: 407880(TGas144d10.1)
            DRE: 386663(pfkfb4) 393983(pfkfb2)
            SPU: 579456(LOC579456)
            DME: Dmel_CG3400(Pfrx)
            CEL: K02B2.1(6-phosphofructo-2-kinase)
            OSA: 4332523 4337906
            SCE: YJL155C(FBP26)
            AGO: AGOS_AEL106W
            PIC: PICST_68318(FBP26)
            CGR: CAGL0I06094g
            SPO: SPAC144.17c SPAC732.02c
            ANI: AN6720.2
            AFM: AFUA_7G05800
            AOR: AO090005000443
            TBR: Tb10.70.2700 Tb927.7.1610 Tb927.8.1020
            LMA: LmjF26.0310
            REH: H16_A1100 H16_B0760
            HAR: HEAR1955
            DVU: DVU3147
            DDE: Dde_0511
            LIP: LI0094(pfk)
            GBE: GbCGDNIH1_2335
            BPU: BPUM_0834
            LDB: Ldb1036 Ldb1737 Ldb1921
            HWA: HQ3517A(gpmB)
            NPH: NP1332A(gpmB)
STRUCTURES  PDB: 1BIF  1C7Z  1C80  1C81  1FBT  1K6M  1TIP  2AXN  2BIF  2DWO  
                 2DWP  2I1V  3BIF  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.46
            ExPASy - ENZYME nomenclature database: 3.1.3.46
            ExplorEnz - The Enzyme Database: 3.1.3.46
            ERGO genome analysis and discovery system: 3.1.3.46
            BRENDA, the Enzyme Database: 3.1.3.46
            CAS: 81611-75-8
///
ENTRY       EC 3.1.3.47                 Enzyme
NAME        [hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase;
            reductase phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     [hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphate
            phosphohydrolase
REACTION    [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate + H2O =
            [hydroxymethylglutaryl-CoA reductase (NADPH)] + phosphate
            [RN:R04542]
ALL_REAC    R04542
SUBSTRATE   [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
            [CPD:C04768];
            H2O [CPD:C00001]
PRODUCT     [hydroxymethylglutaryl-CoA reductase (NADPH)] [CPD:C04632];
            phosphate [CPD:C00009]
COMMENT     Acts on the product of the reaction catalysed by EC 2.7.11.31
            [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase, simultaneously
            dephosphorylating and activating EC 1.1.1.34
            hydroxymethylglutaryl-CoA reductase (NADPH).
REFERENCE   1  [PMID:6282220]
  AUTHORS   Gil G, Hegardt FG.
  TITLE     Some properties of purified 3-hydroxy-3-methylglutaryl coenzyme A
            reductase phosphatases from rat liver.
  JOURNAL   Arch. Biochem. Biophys. 214 (1982) 192-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6260210]
  AUTHORS   Gil G, Sitges M, Hegardt FG.
  TITLE     Purification and properties of rat liver hydroxymethylglutaryl
            coenzyme A reductase phosphatases.
  JOURNAL   Biochim. Biophys. Acta. 663 (1981) 211-21.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.47
            ExPASy - ENZYME nomenclature database: 3.1.3.47
            ExplorEnz - The Enzyme Database: 3.1.3.47
            ERGO genome analysis and discovery system: 3.1.3.47
            BRENDA, the Enzyme Database: 3.1.3.47
            CAS: 73507-97-8
///
ENTRY       EC 3.1.3.48                 Enzyme
NAME        protein-tyrosine-phosphatase;
            phosphotyrosine phosphatase;
            phosphoprotein phosphatase (phosphotyrosine);
            phosphotyrosine histone phosphatase;
            protein phosphotyrosine phosphatase;
            tyrosylprotein phosphatase;
            phosphotyrosine protein phosphatase;
            phosphotyrosylprotein phosphatase;
            tyrosine O-phosphate phosphatase;
            PPT-phosphatase;
            PTPase;
            [phosphotyrosine]protein phosphatase;
            PTP-phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     protein-tyrosine-phosphate phosphohydrolase
REACTION    protein tyrosine phosphate + H2O = protein tyrosine + phosphate
            [RN:R02585]
ALL_REAC    R02585
SUBSTRATE   protein tyrosine phosphate [CPD:C01167];
            H2O [CPD:C00001]
PRODUCT     protein tyrosine [CPD:C00585];
            phosphate [CPD:C00009]
COMMENT     Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such
            as the products of EC 2.7.10.2, non-specific protein-tyrosine
            kinase.
REFERENCE   1  [PMID:6169552]
  AUTHORS   Foulkes JG, Howard RF, Ziemiecki A.
  TITLE     Detection of a novel mammalian protein phosphatase with activity for
            phosphotyrosine.
  JOURNAL   FEBS. Lett. 130 (1981) 197-200.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6273884]
  AUTHORS   Gallis B, Bornstein P, Brautigan DL.
  TITLE     Tyrosylprotein kinase and phosphatase activities in membrane
            vesicles from normal and Rous sarcoma virus-transformed rat cells.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 78 (1981) 6689-93.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map04010  MAPK signaling pathway
            PATH: map04110  Cell cycle
            PATH: map04111  Cell cycle - yeast
            PATH: map04514  Cell adhesion molecules (CAMs)
            PATH: map04520  Adherens junction
            PATH: map04630  Jak-STAT signaling pathway
            PATH: map04650  Natural killer cell mediated cytotoxicity
            PATH: map04660  T cell receptor signaling pathway
            PATH: map04662  B cell receptor signaling pathway
            PATH: map04670  Leukocyte transendothelial migration
            PATH: map04910  Insulin signaling pathway
            PATH: map04914  Progesterone-mediated oocyte maturation
            PATH: map04920  Adipocytokine signaling pathway
            PATH: map04940  Type I diabetes mellitus
            PATH: map05120  Epithelial cell signaling in Helicobacter pylori
                            infection
            PATH: map05211  Renal cell carcinoma
            PATH: map05220  Chronic myeloid leukemia
ORTHOLOGY   KO: K01104  protein-tyrosine phosphatase
            KO: K02555  M-phase inducer tyrosine phosphatase
            KO: K04458  protein-tyrosine phosphatase
            KO: K04459  dual specificity phosphatase
            KO: K05693  protein tyrosine phosphatase, receptor type, M
            KO: K05694  protein tyrosine phosphatase, receptor type, B
            KO: K05695  protein tyrosine phosphatase, receptor type, F
            KO: K05696  protein tyrosine phosphatase, non-receptor type 1
            KO: K05697  protein tyrosine phosphatase, non-receptor type 6
            KO: K05698  protein tyrosine phosphatase, receptor type, J
            KO: K05866  cell division cycle 25B
            KO: K05867  cell division cycle 25C
            KO: K06478  protein tyrosine phosphatase, receptor type, C
            KO: K06639  cell division cycle 14
            KO: K06645  cell division cycle 25A
            KO: K06776  protein tyrosine phosphatase, receptor type, K
            KO: K06777  protein tyrosine phosphatase, receptor type, D
            KO: K06778  protein tyrosine phosphatase, receptor type, S
            KO: K07293  protein tyrosine phosphatase, non-receptor type 11
            KO: K07817  protein tyrosine phosphatase, receptor type, N
            KO: K08114  protein tyrosine phosphatase, receptor-type, Z
                        polypeptide
GENES       HSA: 11072(DUSP14) 11099(PTPN21) 11221(DUSP10) 11266(DUSP12)
                 128853(DUSP15) 138639(PTPDC1) 142679(DUSP19) 150290(DUSP18)
                 1843(DUSP1) 1844(DUSP2) 1845(DUSP3) 1846(DUSP4) 1847(DUSP5)
                 1848(DUSP6) 1849(DUSP7) 1850(DUSP8) 1852(DUSP9) 2139(EYA2)
                 2140(EYA3) 25930(PTPN23) 26191(PTPN22) 26469(PTPN18)
                 4534(MTM1) 51207(DUSP13) 52(ACP1) 5770(PTPN1) 5771(PTPN2)
                 5774(PTPN3) 5775(PTPN4) 5777(PTPN6) 5778(PTPN7) 5780(PTPN9)
                 5781(PTPN11) 5782(PTPN12) 5783(PTPN13) 5784(PTPN14)
                 5786(PTPRA) 5787(PTPRB) 5788(PTPRC) 5789(PTPRD) 5791(PTPRE)
                 5792(PTPRF) 5793(PTPRG) 5794(PTPRH) 5795(PTPRJ) 5796(PTPRK)
                 5797(PTPRM) 5798(PTPRN) 5799(PTPRN2) 5800(PTPRO) 5801(PTPRR)
                 5802(PTPRS) 5803(PTPRZ1) 63904(DUSP21) 7179(TPTE) 7803(PTP4A1)
                 7957(EPM2A) 8073(PTP4A2) 80824(DUSP16) 8446(DUSP11)
                 84867(PTPN5) 8555(CDC14B) 8556(CDC14A) 8897(MTMR3) 993(CDC25A)
                 994(CDC25B) 995(CDC25C)
            PTR: 450865(PTPRE) 451181(PTPRJ) 452074(PTPRB) 452076(PTPRR)
                 453090(PTPN21) 455298(PTPRM) 455504(PTPN2) 457058(CDC14A)
                 457607(PTPRC) 459962(PTPRN) 460341(CDC25A) 463494(PTPN12)
                 464497(DUSP4) 465251(CDC14B) 465297(DUSP16) 467135(PTPN11)
                 468271(DUSP3) 469145(DUSP10) 469248(EYA3) 469970(PTPN1)
                 470521(PTPN4) 470826(DUSP7) 471742(DUSP1) 472046(PTP4A1)
            MCC: 702266(LOC702266) 707494(LOC707494)
            MMU: 104831(Ptpn23) 11431(Acp1) 12530(Cdc25a) 12531(Cdc25b)
                 12532(Cdc25c) 13537(Dusp2) 13853(Epm2a) 13924(Ptprv)
                 14048(Eya1) 14049(Eya2) 14050(Eya3) 15170(Ptpn6) 17772(Mtm1)
                 18218(Dusp8) 19243(Ptp4a1) 19244(Ptp4a2) 19245(Ptp4a3)
                 19246(Ptpn1) 19247(Ptpn11) 19248(Ptpn12) 19249(Ptpn13)
                 19250(Ptpn14) 19252(Dusp1) 19253(Ptpn18) 19255(Ptpn2)
                 19258(Ptpn4) 19259(Ptpn5) 19260(Ptpn22) 19262(Ptpra)
                 19263(Ptprb) 19264(Ptprc) 19266(Ptprd) 19267(Ptpre)
                 19268(Ptprf) 19270(Ptprg) 19271(Ptprj) 19272(Ptprk)
                 19273(Ptpru) 19274(Ptprm) 19275(Ptprn) 19276(Ptprn2)
                 19277(Ptpro) 19279(Ptprr) 19280(Ptprs) 19283(Ptprz1)
                 218232(Ptpdc1) 218294(Cdc14b) 229776(Cdc14a) 235584(Dusp7)
                 24000(Ptpn21) 240672(Dusp5) 252864(Dusp15) 27389(Dusp13)
                 319520(Dusp4) 320139(Ptpn7) 56294(Ptpn9) 56405(Dusp14)
                 63953(Dusp10) 67603(Dusp6) 68082(Dusp19) 70686(Dusp16)
                 72102(Dusp11) 72349(Dusp3) 74302(Mtmr3) 75219(Dusp18)
                 75590(Dusp9) 80915(Dusp12)
            RNO: 114856(Dusp1) 116660(Ptprn) 116663(Dusp6) 116680(Ptpru)
                 116689(Ptpn6) 117063(Ptpn2) 117255(Ptpn12) 117552(Ptpn23)
                 171070(Ptpn21) 171102(Cdc25a) 171103(Cdc25b) 171109(Dusp5)
                 171357(Ptprg) 24161(Acp1) 246781(Ptpn7) 24697(Ptpn1)
                 24699(Ptprc) 25167(Ptpra) 25529(Ptprd) 25613(Ptprz1)
                 25622(Ptpn11) 293847(Dusp9) 29463(Ptp4a1) 29616(Ptprm)
                 29644(Ptpn5) 29645(Ptprj) 29714(Ptprn2) 297412(Dusp11)
                 300980(Dusp7) 307511(Cdc25c_predicted)
                 310806(Cdc14a_predicted) 311151(Dusp19_predicted)
                 313278(RGD1561090_predicted) 314843(Ptprb_predicted)
                 361195(Cdc14b_predicted) 50677(Ptpro) 60587(Dusp4)
                 63995(Dusp10_predicted) 64014(Dusp12) 64576(Ptprv)
                 85237(Ptp4a2) 94202(Ptprr)
            CFA: 475389(PTPRF) 476290(PTPRK) 476294(CDC14B) 477176(PTPRA)
                 477263(PTPN1) 477488(PTPN11) 478921(PTPRN) 479926(CDC14A)
                 480505(DUSP3) 481162(PTPRB) 481163(PTPRR) 481538(PTPRD)
                 481863(PTP4A1) 482428(LOC482428) 482594(DUSP6) 482825(PTPRN2)
                 482880(DUSP4) 483124(PTPN22) 483277(PTPN12) 483617(PTPRJ)
                 483660(LOC483660) 483882(PTPN4) 484022(EPM2A) 484706(PTPRG)
                 484742(DUSP7) 484780(CDC25A) 485030(PTPRS) 485409(PTPN5)
                 485790(CDC25B) 486349(MTMR3) 486357(DUSP18) 486664(PTPRO)
                 486683(DUSP16) 486717(PTPN6) 486884(DUSP5) 487328(PTPRU)
                 488433(DUSP19) 488673(DUSP10) 489117(DUSP1) 490255(PTPRC)
                 490293(PTPN14) 490563(PTPN2) 490823(PTPN21) 491131(DUSP14)
                 492240(DUSP9) 606814(LOC606814) 606961(PTP4A3) 607227(PTPN7)
                 609852(PTPRE) 609926(EYA2) 610061(EYA3) 610456(CDC25C)
                 610692(PTPN3) 611653(DUSP2) 612385(MTM1) 612991(PTPN9)
            BTA: 280977(ACP1) 282333(PTPN13) 286810(PTPRN) 317725(PTPRZ1)
                 407152(cd45) 508150(LOC508150) 533590(LOC533590)
                 614306(LOC614306)
            SSC: 397589(CDKN3)
            GGA: 373911(PTPRO) 374192(DUSP1) 374208(PTPRG) 374272(DUSP6)
                 386580(PTPRC) 395153(PTPRU) 395330(PTPRJ) 395642(DUSP4)
                 395688(PTPN1) 395717(EYA3) 395745(EYA2) 395815(PTPN11)
                 396060(PTPRA) 396375(CRYPALPHA) 396403(PTPRZ1) 396409(PTPN2)
                 415308(PTPN9) 417005(DUSP18) 417657(DUSP14) 417725(PTPN12)
                 417853(PTPRB) 419649(PTP4A2) 420375(CDC25A) 420449(PTPRN2)
                 420963(PTPN3) 421174(LOC421174) 421340(RCJMB04_18i8)
                 421360(PTPN14) 421611(RCJMB04_7n21) 421711(PTPRK)
                 421877(PTP4A1) 421909(RCJMB04_11a4) 422388(MTM1) 423085(PTPN5)
                 423398(PTPN21) 423818(LOC423818) 423890(DUSP5) 423962(PTPRE)
                 423999(DUSP19) 424234(PTPN4) 424568(PTPRF) 425349(DUSP12)
                 425527(DUSP3) 427473(CDC14B) 427947(RCJMB04_15p22)
                 768713(PTP4A3) 770435(DUSP8) 770905(PTPN7) 771985(PTPRR)
                 772032(PTPN22)
            XLA: 379146(MGC52584) 379701(Mtmr3) 379932(ptp4a2) 394358(ptpa-a)
                 398141(LOC398141) 398829(MGC68682) 399291(ptp-2)
                 403393(CDC14a) 431920(MGC83117) 444088(MGC83614)
                 444514(MGC81984) 444752(MGC84792) 446679(ptp4a1)
                 495060(LOC495060)
            XTR: 448043(dusp1) 448657(MGC89650) 493385(MGC79517) 733814(dusp7)
            DRE: 140818(ptpra) 30436(eya1) 327246(dusp7) 333979(ptpn11)
                 335573(ptpn6) 353314(dusp6) 368448(ptpn4) 393148(cdc14a)
                 393438(ptpn2) 393642(ptpn12) 394124(zgc:63654)
                 394146(zgc:55423) 406340(dusp1) 406460(ptp4a3)
                 406523(zgc:77247) 407634(si:rp71-1n18.2) 559154(ptprc)
                 559679(LOC559679) 561613(ptpn2l)
            SPU: 576121(LOC576121) 576159(LOC576159) 578045(LOC578045)
                 578886(LOC578886) 579231(LOC579231) 580769(LOC580769)
                 582330(LOC582330) 582421(LOC582421) 584048(LOC584048)
                 584461(LOC584461) 586673(LOC586673) 587147(LOC587147)
                 589648(LOC589648) 590781(LOC590781) 591564(LOC591564)
                 591824(LOC591824) 592279(LOC592279) 594103(LOC594103)
                 759332(LOC759332) 763053(LOC763053)
            DME: Dmel_CG10443(Lar) Dmel_CG10975(Ptp69D) Dmel_CG1228(Ptpmeg)
                 Dmel_CG13197 Dmel_CG1395(stg) Dmel_CG14080(Mkp3) Dmel_CG14211
                 Dmel_CG14226(dome) Dmel_CG15528 Dmel_CG1817(Ptp10D)
                 Dmel_CG18243(Ptp52F) Dmel_CG2005(Ptp99A) Dmel_CG31795(ia2)
                 Dmel_CG32697(l(1)G0232) Dmel_CG3954(csw) Dmel_CG4965(twe)
                 Dmel_CG4993 Dmel_CG6542(EDTP) Dmel_CG6899(Ptp4E) Dmel_CG7134
                 Dmel_CG7850(puc) Dmel_CG9181(Ptp61F) Dmel_CG9493
                 Dmel_CG9554(eya) Dmel_CG9856(PTP-ER)
            CEL: C04F12.8 C17G10.4(cdc-14) C48D5.2(ptp-1) F44G4.8(dep-1)
                 F47B3.7 F54C8.4 T19D2.2(prl-1)
            ATH: AT3G44620
            OSA: 4340847
            CME: CMI092C
            SCE: YBR276C(PPS1) YDL230W(PTP1) YER075C(PTP3) YFR028C(CDC14)
                 YIL113W(SDP1) YIR026C(YVH1) YMR036C(MIH1) YNL053W(MSG5)
                 YOR208W(PTP2) YPR073C(LTP1)
            AGO: AGOS_ABL172C AGOS_ABR087C AGOS_ACL102W AGOS_ACR158W
                 AGOS_ADL245W AGOS_ADL365W AGOS_AEL025W AGOS_AEL160C
            PIC: PICST_36969 PICST_42742 PICST_60041(PPS1) PICST_60110(CDC14)
                 PICST_74151(YVH1) PICST_80995(PTP2)
            CAL: CaO19.3071(mih1)
            CGR: CAGL0B03377g CAGL0C05423g CAGL0D01320g CAGL0F05973g
                 CAGL0F06809g CAGL0G01320g CAGL0I09064g CAGL0L02827g
            SPO: SPAC11E3.09(pyp3) SPAC1782.09c SPAC19A8.03 SPAC19D5.01(pyp2)
                 SPAC24H6.05(cdc25) SPAC26F1.10c(pyp1) SPBC1685.01(pmp1)
                 SPBC17A3.06 SPBC609.02
            ANI: AN3941.2 AN4896.2 AN5057.2 AN6982.2
            AFM: AFUA_2G11990 AFUA_3G10970 AFUA_3G12250 AFUA_4G04710
                 AFUA_6G06650 AFUA_6G08200
            AOR: AO090003000105 AO090003000651 AO090003000789 AO090206000016
            CNE: CNB03600
            UMA: UM00992.1 UM02069.1 UM02303.1
            DDI: DDBDRAFT_0184168 DDBDRAFT_0189318 DDBDRAFT_0205052
                 DDB_0214985(ptpB)
            PFA: PF11_0139
            CPV: cgd7_4470
            CHO: Chro.70494
            TAN: TA12800 TA16540
            TPV: TP01_1140
            TET: TTHERM_00046430 TTHERM_00189500 TTHERM_00250870
                 TTHERM_00564190 TTHERM_00688720 TTHERM_00697520
            TBR: Tb10.406.0240 Tb10.70.0070 Tb927.4.2460 Tb927.5.3620
                 Tb927.8.5780
            TCR: 503471.10 503583.80 504625.50 506559.190 506743.130 506839.60
                 508717.10 509109.130 509779.60 510075.30 510949.10 511653.20
            LMA: LmjF08.0100 LmjF16.0250 LmjF34.2190 LmjF36.5370
            EHI: 13.t00019 13.t00053 131.t00016 189.t00011 21.t00031
                 286.t00009 3.t00135 5.t00033 85.t00023
            ECO: b0982(yccY) b2061(wzb)
            ECJ: JW2046(wzb)
            ECE: Z1399(yccY) Z3226(wzb)
            ECS: ECs1138 ECs2866
            ECI: UTI89_C1633(ynbD) UTI89_C2335(wzb)
            ECP: ECP_2101
            ECV: APECO1_1151(wzb)
            ECW: EcE24377A_2354(wzb)
            ECX: EcHS_A1091(etp) EcHS_A2192(wzb)
            STY: STY2330(wzb)
            STT: t0755(wzb)
            SPT: SPA0749(wzb)
            SEC: SC2118(wzb)
            STM: STM2117(wzb)
            YPN: YPN_0179
            SFL: SF0984(yccY) SF2125(wzb)
            SFX: S1051(yccY) S2249(wzb)
            SFV: SFV_0991(yccY) SFV_2120(wzb)
            SSN: SSON_0989(yccY) SSON_2114(wzb)
            SBO: SBO_0888(wzb) SBO_2248(yccY)
            SDY: SDY_0958(yccY)
            ECA: ECA1418(wzb)
            PLU: plu3744(wzb)
            SGL: SG0979
            SPE: Spro_4044
            HSO: HS_0817(yfkJ)
            PMU: PM1017 PM1569(yfkJ)
            ASU: Asuc_0541
            XFA: XF2298
            XFT: PD1338
            XCC: XCC2117
            XCB: XC_1998
            XCV: XCV2257
            XAC: XAC2090
            XOO: XOO2294
            XOM: XOO_2172(XOO2172)
            VCH: VC0916 VC1041
            VCO: VC0395_A0440 VC0395_A0559
            VVU: VV1_0783 VV1_3021
            VVY: VV0339 VV1264
            VPA: VP2064 VPA1603
            VFI: VF0164
            PPR: PBPRA1184 PBPRA2687(orf40)
            PAE: PA2978(pt)
            PAU: PA14_25540(ptpA)
            PPU: PP_1903
            PST: PSPTO_3442
            PSB: Psyr_3224
            PSP: PSPPH_3143
            PFL: PFL_1781
            PFO: Pfl_3845 Pfl_4172
            PEN: PSEEN1606
            PAR: Psyc_0648(epsP) Psyc_0949
            PCR: Pcryo_0610 Pcryo_1469
            ACI: ACIAD0069(ptp) ACIAD1946
            SON: SO_2208
            SDN: Sden_2307
            SFR: Sfri_1485
            SHE: Shewmr4_2189
            SHM: Shewmr7_2266
            SHN: Shewana3_2399
            CPS: CPS_0579 CPS_3015
            PHA: PSHAa0527 PSHAa1779
            PAT: Patl_1074 Patl_1706
            SDE: Sde_2057
            MAQ: Maqu_1737
            MCA: MCA1179
            FTU: FTT0635(wzb)
            FTF: FTF0635(wzb)
            FTW: FTW_1094
            FTL: FTL_0905
            FTH: FTH_0888(wzb)
            FTN: FTN_1046(wzb)
            TCX: Tcr_0702
            NOC: Noc_1496 Noc_2842
            AEH: Mlg_0798 Mlg_1431
            HHA: Hhal_1243
            HCH: HCH_02707
            CSA: Csal_1590 Csal_1703
            ABO: ABO_0906(wzb) ABO_1058(pt)
            AHA: AHA_2878
            NME: NMB1267
            NMA: NMA1472
            NMC: NMC1198
            NGO: NGO0541
            CVI: CV_3140
            RSO: RSp1019(epsP)
            REU: Reut_B5369
            REH: H16_A0669 H16_A1155 H16_A2177 H16_A2178
            RME: Rmet_0561 Rmet_1022 Rmet_5850
            BMA: BMA1710(ptpA)
            BMV: BMASAVP1_A2219(ptpA)
            BML: BMA10299_A3101(ptpA)
            BMN: BMA10247_1491(ptpA)
            BXE: Bxe_A1551 Bxe_A2244 Bxe_B0508 Bxe_B1727 Bxe_B2256 Bxe_C1087
            BVI: Bcep1808_2207
            BUR: Bcep18194_A5434 Bcep18194_B2274 Bcep18194_B2515
                 Bcep18194_B2865 Bcep18194_C7399
            BCN: Bcen_4541 Bcen_5949
            BCH: Bcen2424_2128 Bcen2424_3822
            BAM: Bamb_2165 Bamb_5117
            BPS: BPSL2291 BPSL2779 BPSS1832
            BPM: BURPS1710b_2735 BURPS1710b_3273(epsP) BURPS1710b_A0916
            BPL: BURPS1106A_2657(ptpA) BURPS1106A_A2483
            BPD: BURPS668_2601(ptpA) BURPS668_A2621
            BTE: BTH_I1353 BTH_I1873 BTH_II0545
            BPE: BP1797(ptpA)
            BPA: BPP2026(ptpA)
            BBR: BB2274(ptpA)
            RFR: Rfer_0657 Rfer_3410
            AAV: Aave_2532
            MPT: Mpe_A2264
            NEU: NE1785(pt) NE2278(epsP)
            NET: Neut_0914 Neut_2118
            NMU: Nmul_A1063
            EBA: ebA4284 ebA5440 ebA6802(capC)
            AZO: azo1612(ptpA)
            DAR: Daro_2004
            TBD: Tbd_1565
            HHE: HH1763
            WSU: WS1323(pt)
            CJE: Cj1258
            CJR: CJE1394
            CJJ: CJJ81176_1274
            CJU: C8J_1202
            ABU: Abu_0594
            NIS: NIS_0029
            SUN: SUN_1381
            PCA: Pcar_1540
            BBA: Bd0771 Bd0812(pt) Bd1204
            ADE: Adeh_4276
            MXA: MXAN_4427
            MLO: mll4349
            MES: Meso_3348
            ATU: Atu2677
            RET: RHE_CH03935(ypch01397)
            RLE: RL3007 RL4527
            BME: BMEI1863
            BMS: BR0083
            BOV: BOV_0082
            RPE: RPE_2412
            CCR: CC_2368
            SIL: SPO0979
            SIT: TM1040_0675
            RSP: RSP_3326 RSP_4085
            RSH: Rsph17029_4051
            MMR: Mmar10_0410 Mmar10_2913
            ZMO: ZMO0140(ptpA)
            NAR: Saro_1047
            SAL: Sala_0815
            ELI: ELI_05130
            GOX: GOX0416
            GBE: GbCGDNIH1_0759 GbCGDNIH1_0832
            RRU: Rru_A2769 Rru_A3646
            MAG: amb0869
            MGM: Mmc1_2136
            BSU: BG10941(ywlE) BG12509(ywqE) BG12926(yfkJ)
            BHA: BH2238 BH3667 BH3769
            BAN: BA0407 BA3394 BA5561
            BAR: GBAA0407 GBAA3394 GBAA5561
            BAA: BA_0417 BA_0982 BA_3893
            BAT: BAS0393 BAS3147 BAS5168
            BCE: BC0450 BC3335 BC5276 BC5319
            BCA: BCE_0521 BCE_3365 BCE_5397 BCE_5444
            BCZ: BCZK0381(ptp) BCZK3041 BCZK5018
            BCY: Bcer98_1604
            BTK: BT9727_0384(ptp) BT9727_3134 BT9727_4957(epsC) BT9727_5001
            BTL: BALH_0407 BALH_4780(epsC) BALH_4819
            BLI: BL02482(ywqE) BL03081(yfkJ) BL03988(ywlE)
            BLD: BLi00818(yfkJ) BLi03854(ywqE) BLi03938(ywlE)
            BCL: ABC3814 ABC3867
            BPU: BPUM_0736(yfkJ) BPUM_1788 BPUM_3338(ywlE)
            OIH: OB0873 OB2988
            GKA: GK0419 GK3323 GK3373
            SAU: SA1697 SA1917
            SAV: SAV1881 SAV2115
            SAM: MW1821 MW2039
            SAR: SAR1971 SAR2203
            SAS: SAS1803 SAS2018
            SAC: SACOL1939 SACOL2107
            SAB: SAB1813 SAB1999c
            SAA: SAUSA300_0154(cap5C) SAUSA300_1862 SAUSA300_2069
                 SAUSA300_2596(cap1C)
            SAO: SAOUHSC_02095 SAOUHSC_02356
            SAJ: SaurJH9_0137 SaurJH9_1935 SaurJH9_2686
            SAH: SaurJH1_0142 SaurJH1_1969 SaurJH1_2743
            SEP: SE1566 SE1712
            SER: SERP1419 SERP1721
            SHA: SH0920 SH1075
            SSP: SSP0769 SSP0912
            LMO: lmo0938 lmo1800 lmo2540
            LMF: LMOf2365_0959 LMOf2365_1827 LMOf2365_2513
            LIN: lin0937 lin1914 lin2684
            LWE: lwe0917 lwe1819 lwe1961 lwe2489
            LLA: L67624(ptpL)
            LLC: LACR_2514
            LLM: llmg_2486(ptpL)
            SPY: SPy_0039
            SPZ: M5005_Spy_0036
            SPM: spyM18_0040
            SPG: SpyM3_0033
            SPS: SPs0034
            SPH: MGAS10270_Spy0038
            SPI: MGAS10750_Spy0038
            SPJ: MGAS2096_Spy0038
            SPK: MGAS9429_Spy0037
            SPF: SpyM50036
            SPA: M6_Spy0085
            SPB: M28_Spy0036
            SPN: SP_2028
            SPR: spr1839
            SPD: SPD_0316(cps2B)
            SAG: SAG0050
            SAN: gbs0050
            SAK: SAK_0083
            SMU: SMU.65
            STC: str1939
            STL: stu1939
            SSA: SSA_0065
            SGO: SGO_0110 SGO_2027(wzh)
            LPL: lp_0069(ptp1) lp_2106(cps4C) lp_2735(ptp3) lp_3272(ptp2)
            LJO: LJ0127 LJ1013 LJ1024
            LAC: LBA0147 LBA0722 LBA1734(epsD)
            LSA: LSA0036 LSA0164 LSA0275
            LSL: LSL_1454 LSL_1552 LSL_1802
            LDB: Ldb0200 Ldb0670 Ldb2059 Ldb2093 Ldb2096
            LBU: LBUL_0174 LBUL_0602 LBUL_1857
            LBR: LVIS_0231 LVIS_0499 LVIS_2036
            LCA: LSEI_2049 LSEI_2215 LSEI_2788
            LGA: LGAS_0127
            LRE: Lreu_1034
            PPE: PEPE_0342 PEPE_0343
            EFA: EF3058
            OOE: OEOE_0332
            STH: STH76
            CAC: CAC2881
            CTC: CTC00306
            CNO: NT01CX_0544 NT01CX_1524
            CDF: CD3481
            CBO: CBO0143 CBO2688
            CBA: CLB_0179
            CBH: CLC_0191
            CBF: CLI_0198
            CBE: Cbei_4740
            CHY: CHY_2481 CHY_2559
            DSY: DSY4930
            SWO: Swol_2393
            MPE: MYPE8980
            MTU: Rv0153c(ptbB) Rv2234(ptpA)
            MTC: MT2293(ptpA)
            MBO: Mb0158c(ptbB) Mb2258(ptpA)
            MBB: BCG_0189c(ptbB) BCG_2251(ptpA)
            MPA: MAP1985(ptpA)
            MAV: MAV_2206
            MSM: MSMEG_0100 MSMEG_4309
            MMC: Mmcs_0097 Mmcs_0932 Mmcs_3347
            CGL: NCgl0338(cgl0345) NCgl1648(cgl1716) NCgl2159(cgl2240)
            CGB: cg0415(ptpA2) cg2459(ptpA)
            CEF: CE0358 CE2138
            CDI: DIP1683
            CJK: jk0665(ptpA)
            NFA: nfa16310(ptpA)
            RHA: RHA1_ro01186 RHA1_ro01524 RHA1_ro05454
            SCO: SCO3921(ptpA)
            SMA: SAV4272(ptpB2)
            CMI: CMM_2949
            ART: Arth_3227
            AAU: AAur_3227
            PAC: PPA2110
            TFU: Tfu_2341
            FRA: Francci3_1290
            FAL: FRAAL2037 FRAAL3007
            SEN: SACE_1579
            BLO: BL0248 BL1667(ptpA)
            BAD: BAD_0390(ptpA) BAD_1357
            RXY: Rxyl_1930 Rxyl_2075
            RBA: RB10818
            PCU: pc1079(wzb)
            LIL: LB035(amsI)
            LIC: LIC20027(wzb)
            LBJ: LBJ_4030(wzb)
            LBL: LBL_4030(wzb)
            SYN: slr0328
            SYW: SYNW0915 SYNW2026
            SYC: syc1055_d
            SYF: Synpcc7942_0463
            SYD: Syncc9605_0417
            SYE: Syncc9902_1913
            SYG: sync_0484
            SYR: SynRCC307_2068
            SYX: SynWH7803_0475
            CYA: CYA_1629
            CYB: CYB_0906
            TEL: tlr1810
            GVI: gll3174
            ANA: alr1067 alr5068
            AVA: Ava_2323 Ava_3780
            PMA: Pro1747(wzb)
            PMM: PMM1591
            PMT: PMT1688
            PMN: PMN2A_1166
            PMI: PMT9312_1683
            PMB: A9601_18001(wzb)
            PMC: P9515_17781(wzb)
            PMF: P9303_22461(wzb)
            PMG: P9301_17831(wzb)
            PMH: P9215_18641(wzb)
            PME: NATL1_20411(wzb)
            TER: Tery_3848 Tery_4026
            BTH: BT_2750
            BFR: BF4208
            BFS: BF4032
            PGI: PG1641
            SRU: SRU_0502 SRU_0739
            CHU: CHU_0542(ptpA) CHU_1113(ptpA) CHU_2721(ptpA)
            GFO: GFO_0629 GFO_1982
            FPS: FP1209
            CTE: CT1568
            CCH: Cag_0407
            TTH: TTC0816
            TTJ: TTHA1180
            HWA: HQ3170A(arsC) HQ3636A(arsC)
            NPH: NP6092A(arsC)
STRUCTURES  PDB: 1A5Y  1AAX  1AYA  1AYB  1AYC  1AYD  1BZC  1BZH  1BZJ  1C25  
                 1C83  1C84  1C85  1C86  1C87  1C88  1CWR  1D1P  1D1Q  1D2A  
                 1D5R  1DG9  1ECV  1EEN  1EEO  1FPR  1FPZ  1FQ1  1G1F  1G1G  
                 1G1H  1G7F  1G7G  1GFY  1GM1  1GWZ  1HUF  1HZM  1I57  1I8G  
                 1J4X  1JEG  1JF7  1JLN  1K46  1KAK  1KAV  1L8G  1L8K  1LAR  
                 1LQF  1LYV  1M0V  1M3G  1MKP  1NL9  1NNY  1NO6  1NWE  1NWL  
                 1NZ7  1OEM  1OEO  1OES  1OET  1OEU  1OEV  1ONY  1ONZ  1OZI  
                 1P15  1P8A  1PA1  1PA9  1PH0  1PHR  1PTT  1PTU  1PTV  1PTY  
                 1PXH  1PYN  1Q1M  1Q6J  1Q6M  1Q6N  1Q6P  1Q6S  1Q6T  1QB0  
                 1QXK  1QZ0  1R6H  1RPM  1SUG  1T3K  1T48  1T49  1T4J  1U2P  
                 1U2Q  1V3A  1V73  1VHR  1VJ6  1WAX  1WCH  1WRM  1X24  1X5Z  
                 1X6C  1XBO  1XM2  1XWW  1XXP  1XXV  1YFO  1YGU  1YM9  1YMD  
                 1YMK  1YML  1YPT  1YS0  1YTN  1YTS  1YTW  1YZ4  1Z12  1Z13  
                 1ZC0  1ZCL  1ZGG  1ZZW  2A2K  2A8B  2AHS  2AZR  2B07  2B3O  
                 2B49  2B4S  2B9I  2BGD  2BGE  2BIJ  2BV5  2BZL  2C7S  2C9A  
                 2CFV  2CJZ  2CM2  2CM3  2CM7  2CM8  2CMA  2CMB  2CMC  2CNE  
                 2CNF  2CNG  2CNH  2CNI  2CS5  2DJU  2DLE  2DLH  2DN7  2DXP  
                 2EDX  2EDY  2ESB  2F6F  2F6T  2F6V  2F6W  2F6Y  2F6Z  2F70  
                 2F71  2FEK  2FH7  2FJM  2FJN  2FXI  2FYS  2G59  2G6Z  2GI4  
                 2GJT  2GP0  2GPH  2GWO  2H02  2H03  2H04  2H4G  2H4K  2H4V  
                 2HB1  2HC1  2HC2  2HNP  2HNQ  2HVL  2HXP  2HY3  2I1Y  2I3R  
                 2I3U  2I42  2I4E  2I4G  2I4H  2I5X  2I6J  2I6M  2I6O  2I6P  
                 2I75  2IFD  2IFV  2IMG  2IPA  2J16  2J17  2NLK  2NT2  2NT7  
                 2NTA  2NZ6  2OC3  2OOQ  2OUC  2OUD  2P4D  2P6X  2PA5  2PBN  
                 2PQ5  2Q05  2Q47  2QEP  2SHP  2V5Y  3PDZ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.48
            ExPASy - ENZYME nomenclature database: 3.1.3.48
            ExplorEnz - The Enzyme Database: 3.1.3.48
            ERGO genome analysis and discovery system: 3.1.3.48
            BRENDA, the Enzyme Database: 3.1.3.48
            CAS: 79747-53-8
///
ENTRY       EC 3.1.3.49                 Enzyme
NAME        [pyruvate kinase]-phosphatase;
            pyruvate kinase phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     [ATP:pyruvate 2-O-phosphotransferase]-phosphate phosphohydrolase
REACTION    [pyruvate kinase] phosphate + H2O = [pyruvate kinase] + phosphate
            [RN:R03993]
ALL_REAC    R03993
SUBSTRATE   [pyruvate kinase] phosphate [CPD:C03808];
            H2O [CPD:C00001]
PRODUCT     [pyruvate kinase] [CPD:C02601];
            phosphate [CPD:C00009]
COMMENT     Simultaneously dephosphorylates and activates EC 2.7.1.40 pyruvate
            kinase, that has been inactivated by protein kinase.
REFERENCE   1  [PMID:6271587]
  AUTHORS   Jett MF, Hue L, Hers HG.
  TITLE     Pyruvate kinase phosphatase.
  JOURNAL   FEBS. Lett. 132 (1981) 183-6.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.49
            ExPASy - ENZYME nomenclature database: 3.1.3.49
            ExplorEnz - The Enzyme Database: 3.1.3.49
            ERGO genome analysis and discovery system: 3.1.3.49
            BRENDA, the Enzyme Database: 3.1.3.49
            CAS: 79986-25-7
///
ENTRY       EC 3.1.3.50                 Enzyme
NAME        sorbitol-6-phosphatase;
            sorbitol-6-phosphate phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     sorbitol-6-phosphate phosphohydrolase
REACTION    sorbitol 6-phosphate + H2O = sorbitol + phosphate [RN:R02866]
ALL_REAC    R02866
SUBSTRATE   sorbitol 6-phosphate [CPD:C01096];
            H2O [CPD:C00001]
PRODUCT     sorbitol [CPD:C00794];
            phosphate [CPD:C00009]
COMMENT     Acts, very slowly, on hexose 6-phosphates.
REFERENCE   1
  AUTHORS   Grant, C.R. and ap Rees, T.
  TITLE     Sorbitol metabolism by apple seedlings.
  JOURNAL   Phytochemistry 20 (1981) 1505-1511.
  ORGANISM  Malus domestica
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.50
            ExPASy - ENZYME nomenclature database: 3.1.3.50
            ExplorEnz - The Enzyme Database: 3.1.3.50
            ERGO genome analysis and discovery system: 3.1.3.50
            BRENDA, the Enzyme Database: 3.1.3.50
            CAS: 80449-21-4
///
ENTRY       EC 3.1.3.51                 Enzyme
NAME        dolichyl-phosphatase;
            dolichol phosphate phosphatase;
            dolichol phosphatase;
            dolichol monophosphatase;
            dolichyl monophosphate phosphatase;
            dolichyl phosphate phosphatase;
            polyisoprenyl phosphate phosphatase;
            polyprenylphosphate phosphatase;
            Dol-P phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     dolichyl-phosphate phosphohydrolase
REACTION    dolichyl phosphate + H2O = dolichol + phosphate [RN:R01003]
ALL_REAC    R01003
SUBSTRATE   dolichyl phosphate [CPD:C00110];
            H2O [CPD:C00001]
PRODUCT     dolichol [CPD:C00381];
            phosphate [CPD:C00009]
REFERENCE   1  [PMID:229909]
  AUTHORS   Adrian GS, Keenan RW.
  TITLE     A dolichyl phosphate-cleaving acid phosphatase from Tetrahymena
            pyriformis.
  JOURNAL   Biochim. Biophys. Acta. 575 (1979) 431-8.
  ORGANISM  Tetrahymena pyriformis
REFERENCE   2  [PMID:6257694]
  AUTHORS   Rip JW, Rupar CA, Chaudhary N, Carroll KK.
  TITLE     Localization of a dolichyl phosphate phosphatase in plasma membranes
            of rat liver.
  JOURNAL   J. Biol. Chem. 256 (1981) 1929-34.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:6243292]
  AUTHORS   Wedgwood JF, Strominger JL.
  TITLE     Enzymatic activities in cultured human lymphocytes that
            dephosphorylate dolichyl pyrophosphate and dolichyl phosphate.
  JOURNAL   J. Biol. Chem. 255 (1980) 1120-3.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.51
            ExPASy - ENZYME nomenclature database: 3.1.3.51
            ExplorEnz - The Enzyme Database: 3.1.3.51
            ERGO genome analysis and discovery system: 3.1.3.51
            BRENDA, the Enzyme Database: 3.1.3.51
            CAS: 72994-50-4
///
ENTRY       EC 3.1.3.52                 Enzyme
NAME        [3-methyl-2-oxobutanoate dehydrogenase
            (2-methylpropanoyl-transferring)]-phosphatase;
            branched-chain oxo-acid dehydrogenase phosphatase;
            branched-chain 2-keto acid dehydrogenase phosphatase;
            branched-chain alpha-keto acid dehydrogenase phosphatase;
            BCKDH;
            [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]-phosphatase;
            [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]-phosphate
            phosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     [3-methyl-2-oxobutanoate dehydrogenase
            (2-methylpropanoyl-transferring)]-phosphate phosphohydrolase
REACTION    [3-methyl-2-oxobutanoate dehydrogenase
            (2-methylpropanoyl-transferring)] phosphate + H2O =
            [3-methyl-2-oxobutanoate dehydrogenase
            (2-methylpropanoyl-transferring)] + phosphate
ALL_REAC    (other) R03515
SUBSTRATE   [3-methyl-2-oxobutanoate dehydrogenase
            (2-methylpropanoyl-transferring)] phosphate;
            H2O [CPD:C00001]
PRODUCT     [3-methyl-2-oxobutanoate dehydrogenase
            (2-methylpropanoyl-transferring)];
            phosphate [CPD:C00009]
COMMENT     A mitochondrial enzyme associated with the 3-methyl-2-oxobutanoate
            dehydrogenase complex. Simultaneously dephosphorylates and activates
            EC 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase
            (2-methylpropanoyl-transferring), that has been inactivated by
            phosphorylation.
REFERENCE   1  [PMID:6307746]
  AUTHORS   Fatania HR, Patston PA, Randle PJ.
  TITLE     Dephosphorylation and reactivation of phosphorylated purified
            ox-kidney branched-chain dehydrogenase complex by co-purified
            phosphatase.
  JOURNAL   FEBS. Lett. 158 (1983) 234-8.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:3004826]
  AUTHORS   Reed LJ, Damuni Z, Merryfield ML.
  TITLE     Regulation of mammalian pyruvate and branched-chain alpha-keto acid
            dehydrogenase complexes by phosphorylation-dephosphorylation.
  JOURNAL   Curr. Top. Cell. Regul. 27 (1985) 41-9.
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.52
            ExPASy - ENZYME nomenclature database: 3.1.3.52
            ExplorEnz - The Enzyme Database: 3.1.3.52
            ERGO genome analysis and discovery system: 3.1.3.52
            BRENDA, the Enzyme Database: 3.1.3.52
            CAS: 87244-20-0
///
ENTRY       EC 3.1.3.53                 Enzyme
NAME        [myosin-light-chain] phosphatase;
            myosin light chain kinase phosphatase;
            myosin phosphatase;
            myosin phosphatase;
            protein phosphatase 2A;
            myosin-light-chain-phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     [myosin-light-chain]-phosphate phosphohydrolase
REACTION    [myosin light-chain] phosphate + H2O = [myosin light-chain] +
            phosphate [RN:R03151]
ALL_REAC    R03151
SUBSTRATE   myosin light-chain phosphate [CPD:C03875];
            H2O [CPD:C00001]
PRODUCT     [myosin light-chain];
            phosphate [CPD:C00009]
COMMENT     The enzyme is composed of three subunits. The holoenzyme
            dephosphorylates myosin light chains and EC 2.7.11.18,
            myosin-light-chain kinase, but not myosin; the catalytic subunit
            acts on all three substrates.
REFERENCE   1  [PMID:6304072]
  AUTHORS   Pato MD, Adelstein RS.
  TITLE     Purification and characterization of a multisubunit phosphatase from
            turkey gizzard smooth muscle. The effect of calmodulin binding to
            myosin light chain kinase on dephosphorylation.
  JOURNAL   J. Biol. Chem. 258 (1983) 7047-54.
  ORGANISM  turkey
ORTHOLOGY   KO: K01105  myosin-light-chain-phosphatase
GENES       CAL: CaO19_4950(CaO19.4950)
STRUCTURES  PDB: 1S70  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.53
            ExPASy - ENZYME nomenclature database: 3.1.3.53
            ExplorEnz - The Enzyme Database: 3.1.3.53
            ERGO genome analysis and discovery system: 3.1.3.53
            BRENDA, the Enzyme Database: 3.1.3.53
            CAS: 86417-96-1
///
ENTRY       EC 3.1.3.54                 Enzyme
NAME        fructose-2,6-bisphosphate 6-phosphatase;
            fructose 2,6-bisphosphate-6-phosphohydrolase;
            fructose-2,6-bisphosphate 6-phosphohydrolase;
            D-fructose-2,6-bisphosphate 6-phosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     beta-D-fructose-2,6-bisphosphate 6-phosphohydrolase
REACTION    beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructofuranose
            2-phosphate + phosphate [RN:R02730]
ALL_REAC    R02730
SUBSTRATE   beta-D-fructose 2,6-bisphosphate [CPD:C00665];
            H2O [CPD:C00001]
PRODUCT     beta-D-fructofuranose 2-phosphate [CPD:C03267];
            phosphate [CPD:C00009]
COMMENT     cf. EC 3.1.3.46 fructose-2,6-bisphosphate 2-phosphatase.
REFERENCE   1
  AUTHORS   Purwin, C., Laux, M. and Holzer, H.
  TITLE     Fructose 2-phosphate, an intermediate of the dephosphorylation of
            fructose 2,6-bisposphate with purified yeast enzyme.
  JOURNAL   Eur. J. Biochem. 164 (1986) 27-30.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:3036508]
  AUTHORS   Purwin C, Laux M, Holzer H.
  TITLE     Fructofuranose 2-phosphate is the product of dephosphorylation of
            fructose 2,6-bisphosphate.
  JOURNAL   Eur. J. Biochem. 165 (1987) 543-5.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.54
            ExPASy - ENZYME nomenclature database: 3.1.3.54
            ExplorEnz - The Enzyme Database: 3.1.3.54
            ERGO genome analysis and discovery system: 3.1.3.54
            BRENDA, the Enzyme Database: 3.1.3.54
            CAS: 111684-53-8
///
ENTRY       EC 3.1.3.55                 Enzyme
NAME        caldesmon-phosphatase;
            SMP-I;
            smooth muscle caldesmon phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     caldesmon-phosphate phosphohydrolase
REACTION    caldesmon phosphate + H2O = caldesmon + phosphate [RN:R02885]
ALL_REAC    R02885
SUBSTRATE   caldesmon phosphate [CPD:C01022];
            H2O [CPD:C00001]
PRODUCT     caldesmon [CPD:C00759];
            phosphate [CPD:C00009]
COMMENT     Dephosphorylation activates the calmodulin- and actin-binding
            ability of the protein caldesmon.
REFERENCE   1  [PMID:6150036]
  AUTHORS   Ngai PK, Walsh MP.
  TITLE     Inhibition of smooth muscle actin-activated myosin Mg2+-ATPase
            activity by caldesmon.
  JOURNAL   J. Biol. Chem. 259 (1984) 13656-9.
  ORGANISM  chicken [GN:gga]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.55
            ExPASy - ENZYME nomenclature database: 3.1.3.55
            ExplorEnz - The Enzyme Database: 3.1.3.55
            ERGO genome analysis and discovery system: 3.1.3.55
            BRENDA, the Enzyme Database: 3.1.3.55
            CAS: 93229-71-1
///
ENTRY       EC 3.1.3.56                 Enzyme
NAME        inositol-polyphosphate 5-phosphatase;
            type I inositol-polyphosphate phosphatase;
            inositol trisphosphate phosphomonoesterase;
            InsP3/Ins(1,3,4,5)P4 5-phosphatase;
            inosine triphosphatase;
            D-myo-inositol 1,4,5-triphosphate 5-phosphatase;
            D-myo-inositol 1,4,5-trisphosphate 5-phosphatase;
            L-myo-inositol 1,4,5-trisphosphate-monoesterase;
            inositol phosphate 5-phosphomonoesterase;
            inositol-1,4,5-trisphosphate/1,3,4,5-tetrakisphosphate
            5-phosphatase;
            Ins(1,4,5)P3 5-phosphatase;
            D-myo-inositol(1,4,5)/(1,3,4,5)-polyphosphate 5-phosphatase;
            inositol 1,4,5-trisphosphate phosphatase;
            inositol polyphosphate-5-phosphatase;
            myo-inositol-1,4,5-trisphosphate 5-phosphatase;
            inositol-1,4,5-trisphosphate 5-phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     1D-myo-inositol-1,4,5-trisphosphate 5-phosphohydrolase
REACTION    (1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol
            1,4-bisphosphate + phosphate [RN:R03394];
            (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O =
            1D-myo-inositol 1,3,4-trisphosphate + phosphate [RN:R03430]
ALL_REAC    R03394 R03430
SUBSTRATE   D-myo-inositol 1,4,5-trisphosphate [CPD:C01245];
            H2O [CPD:C00001];
            1D-myo-inositol 1,3,4,5-tetrakisphosphate [CPD:C01272]
PRODUCT     myo-inositol 1,4-bisphosphate [CPD:C01220];
            phosphate [CPD:C00009];
            1D-myo-inositol 1,3,4-trisphosphate [CPD:C01243]
COMMENT     One mammalian isoform is known. This enzyme is distinguished from
            the family of enzymes classified under EC 3.1.3.36, phosphoinositide
            5-phosphatase, by its inability to dephosphorylate inositol lipids.
REFERENCE   1  [PMID:6285891]
  AUTHORS   Downes CP, Mussat MC, Michell RH.
  TITLE     The inositol trisphosphate phosphomonoesterase of the human
            erythrocyte membrane.
  JOURNAL   Biochem. J. 203 (1982) 169-77.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:2540972]
  AUTHORS   Erneux C, Lemos M, Verjans B, Vanderhaeghen P, Delvaux A, Dumont JE.
  TITLE     Soluble and particulate Ins(1,4,5)P3/Ins(1,3,4,5)P4 5-phosphatase in
            bovine brain.
  JOURNAL   Eur. J. Biochem. 181 (1989) 317-22.
  ORGANISM  cow [GN:bta]
REFERENCE   3
  AUTHORS   Woscholski, R. and Parker, P.J.
  TITLE     Inositol phosphatases: constructive destruction of phosphoinositides
            and inositol phosphates.
  JOURNAL   In: Cockcroft, S. (Ed.), Biology of Phosphoinositides, Biology of
            Phosphoinositides, Oxford, 2000, p. 320-338.
REFERENCE   4  [PMID:8198557]
  AUTHORS   Verjans B, De Smedt F, Lecocq R, Vanweyenberg V, Moreau C, Erneux C.
  TITLE     Cloning and expression in Escherichia coli of a dog thyroid cDNA
            encoding a novel inositol 1,4,5-trisphosphate 5-phosphatase.
  JOURNAL   Biochem. J. 300 ( Pt 1) (1994) 85-90.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00562  Inositol phosphate metabolism
            PATH: map04070  Phosphatidylinositol signaling system
ORTHOLOGY   KO: K01106  inositol-1,4,5-trisphosphate 5-phosphatase
GENES       HSA: 27124(PIB5PA) 3632(INPP5A) 3636(INPPL1) 51763(SKIP)
            PTR: 451403(INPPL1) 454410(LOC454410)
            MMU: 16330(Inpp5b) 16332(Inppl1) 170835(Pib5pa)
                 19062(RP23-136K12.4) 212111(Inpp5a)
            RNO: 171088(Pib5pa) 65038(Inppl1) 84018(Synj2)
            CFA: 403937(INPP5A) 485209(INPPL1) 486360(LOC486360)
            GGA: 416996(LOC416996) 423973(INPP5A) 428692(INPPL1)
            XLA: 447532(MGC83747)
            SPU: 575498(LOC575498) 576800(LOC576800)
            DME: Dmel_CG31107(5PtaseI) Dmel_CG31110 Dmel_CG6562(synj)
            CEL: C09B8.1(ipp-5)
            SCE: YNL106C(INP52) YOL065C(INP54) YOR109W(INP53)
            PIC: PICST_58872(INP51) PICST_82710(INP52)
            CGR: CAGL0C05269g
            UMA: UM02595.1
            CPV: cgd2_230
            TBR: Tb09.160.4180 Tb11.02.4140
            TCR: 506297.200 510101.130
            LMA: LmjF11.1010
            EHI: 213.t00015
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.56
            ExPASy - ENZYME nomenclature database: 3.1.3.56
            ExplorEnz - The Enzyme Database: 3.1.3.56
            ERGO genome analysis and discovery system: 3.1.3.56
            BRENDA, the Enzyme Database: 3.1.3.56
            CAS: 9082-57-9
///
ENTRY       EC 3.1.3.57                 Enzyme
NAME        inositol-1,4-bisphosphate 1-phosphatase;
            inositol-polyphosphate 1-phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     1D-myo-inositol-1,4-bisphosphate 1-phosphohydrolase
REACTION    1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate
            + phosphate [RN:R03393]
ALL_REAC    R03393;
            (other) R03427
SUBSTRATE   1D-myo-inositol 1,4-bisphosphate [CPD:C01220];
            H2O [CPD:C00001]
PRODUCT     1D-myo-inositol 4-phosphate [CPD:C03546];
            phosphate [CPD:C00009]
COMMENT     The enzyme acts on inositol 1,4-bisphosphate and inositol
            1,3,4-trisphosphate (forming inositol 3,4-bisphosphate) with similar
            Vmax values for both substrates, but with a five-times higher
            affinity for the bisphosphate. Does not act on inositol 1-phosphate,
            inositol 1,4,5-trisphosphate or inositol 1,3,4,5-tetrakisphosphate.
REFERENCE   1  [PMID:6309146]
  AUTHORS   Berridge MJ, Dawson RM, Downes CP, Heslop JP, Irvine RF.
  TITLE     Changes in the levels of inositol phosphates after agonist-dependent
            hydrolysis of membrane phosphoinositides.
  JOURNAL   Biochem. J. 212 (1983) 473-82.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:3029066]
  AUTHORS   Connolly TM, Bansal VS, Bross TE, Irvine RF, Majerus PW.
  TITLE     The metabolism of tris- and tetraphosphates of inositol by
            5-phosphomonoesterase and 3-kinase enzymes.
  JOURNAL   J. Biol. Chem. 262 (1987) 2146-9.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:2824473]
  AUTHORS   Inhorn RC, Majerus PW.
  TITLE     Inositol polyphosphate 1-phosphatase from calf brain. Purification
            and inhibition by Li+, Ca2+, and Mn2+.
  JOURNAL   J. Biol. Chem. 262 (1987) 15946-52.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00562  Inositol phosphate metabolism
            PATH: map04070  Phosphatidylinositol signaling system
ORTHOLOGY   KO: K01107  inositol polyphosphate 1-phosphatase
GENES       HSA: 3628(INPP1)
            MMU: 16329(Inpp1)
            CFA: 478842(INPP1)
            BTA: 281869(INPP1)
            DME: Dmel_CG3028(Ipp)
            ATH: AT5G63980(SAL1)
            TBR: Tb927.8.7170
STRUCTURES  PDB: 1INP  1JP4  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.57
            ExPASy - ENZYME nomenclature database: 3.1.3.57
            ExplorEnz - The Enzyme Database: 3.1.3.57
            ERGO genome analysis and discovery system: 3.1.3.57
            BRENDA, the Enzyme Database: 3.1.3.57
            CAS: 111070-17-8
///
ENTRY       EC 3.1.3.58                 Enzyme
NAME        sugar-terminal-phosphatase;
            xylitol-5-phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     sugar-omega-phosphate phosphohydrolase
REACTION    D-glucose 6-phosphate + H2O = D-glucose + phosphate [RN:R00303]
ALL_REAC    R00303
SUBSTRATE   D-glucose 6-phosphate [CPD:C00092];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031];
            phosphate [CPD:C00009]
COMMENT     Acts on sugars and polyols phosphorylated on the terminal carbon,
            with a preference for sugars with a D-erythro-configuration, e.g.
            good substrates are glucose 6-phosphate, mannose 6-phosphate,
            6-phosphogluconate, erythrose 4-phosphate and xylitol 5-phosphate.
REFERENCE   1  [PMID:2993253]
  AUTHORS   London J, Hausman SZ, Thompson J.
  TITLE     Characterization of a membrane-regulated sugar phosphate
            phosphohydrolase from Lactobacillus casei.
  JOURNAL   J. Bacteriol. 163 (1985) 951-6.
  ORGANISM  Lactobacillus casei [GN:lca]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.58
            ExPASy - ENZYME nomenclature database: 3.1.3.58
            ExplorEnz - The Enzyme Database: 3.1.3.58
            ERGO genome analysis and discovery system: 3.1.3.58
            BRENDA, the Enzyme Database: 3.1.3.58
            CAS: 99283-70-2
///
ENTRY       EC 3.1.3.59                 Enzyme
NAME        alkylacetylglycerophosphatase;
            1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase;
            alkylacetylglycerophosphate phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     1-alkyl-2-acetyl-sn-glycero-3-phosphate phosphohydrolase
REACTION    1-alkyl-2-acetyl-sn-glycero-3-phosphate + H2O =
            1-alkyl-2-acetyl-sn-glycerol + phosphate [RN:R03454]
ALL_REAC    R03454
SUBSTRATE   1-alkyl-2-acetyl-sn-glycero-3-phosphate;
            H2O [CPD:C00001]
PRODUCT     1-alkyl-2-acetyl-sn-glycerol [CPD:C03820];
            phosphate [CPD:C00009]
COMMENT     Involved in the biosynthesis of thrombocyte activating factor in
            animal tissues.
REFERENCE   1  [PMID:3007498]
  AUTHORS   Lee TC, Malone B, Snyder F.
  TITLE     A new de novo pathway for the formation of
            1-alkyl-2-acetyl-sn-glycerols, precursors of platelet activating
            factor. Biochemical characterization of
            1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase in rat
            spleen.
  JOURNAL   J. Biol. Chem. 261 (1986) 5373-7.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00565  Ether lipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.59
            ExPASy - ENZYME nomenclature database: 3.1.3.59
            ExplorEnz - The Enzyme Database: 3.1.3.59
            ERGO genome analysis and discovery system: 3.1.3.59
            BRENDA, the Enzyme Database: 3.1.3.59
            CAS: 102925-45-1
///
ENTRY       EC 3.1.3.60                 Enzyme
NAME        phosphoenolpyruvate phosphatase;
            PEP phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     phosphoenolpyruvate phosphohydrolase
REACTION    phosphoenolpyruvate + H2O = pyruvate + phosphate [RN:R00208]
ALL_REAC    R00208
SUBSTRATE   phosphoenolpyruvate [CPD:C00074];
            H2O [CPD:C00001]
PRODUCT     pyruvate [CPD:C00022];
            phosphate [CPD:C00009]
COMMENT     Also acts, but more slowly, on a wide range of other monophosphates.
REFERENCE   1
  AUTHORS   Duff, S.M.G., Lefebvre, D.D. and Plaxton, W.C.
  TITLE     Purification and characterization of a phosphoenolpyruvate
            phosphatase from Brassica nigra suspension cells.
  JOURNAL   Plant Physiol. 90 (1989) 734-741.
  ORGANISM  Brassica nigra
REFERENCE   2
  AUTHORS   Malhotra, O.P. and Kayastha, A.M.
  TITLE     Chemical inactivation and active site groups of
            phosphoenolpyruvate-phosphatase from germinating mung beans (Vigna
            radiata).
  JOURNAL   Plant Sci. 65 (1989) 161-170.
  ORGANISM  Vigna radiata
REFERENCE   3
  AUTHORS   Malhotra, O.P. and Kayastha, A.M.
  TITLE     Isolation and characterization of phosphoenolpyruvate phosphatase
            from germinating mung beans (Vigna radiata).
  JOURNAL   Plant Physiol. 93 (1990) 194-200.
  ORGANISM  Vigna radiata
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.60
            ExPASy - ENZYME nomenclature database: 3.1.3.60
            ExplorEnz - The Enzyme Database: 3.1.3.60
            ERGO genome analysis and discovery system: 3.1.3.60
            BRENDA, the Enzyme Database: 3.1.3.60
            CAS: 122319-89-5
///
ENTRY       EC 3.1.3.61       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
COMMENT     Deleted entry: inositol-1,4,5-trisphosphate 1-phosphatase, as its
            existence has not been established (EC 3.1.3.61 created 1992,
            deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.61
            ExPASy - ENZYME nomenclature database: 3.1.3.61
            ExplorEnz - The Enzyme Database: 3.1.3.61
            ERGO genome analysis and discovery system: 3.1.3.61
            BRENDA, the Enzyme Database: 3.1.3.61
///
ENTRY       EC 3.1.3.62                 Enzyme
NAME        multiple inositol-polyphosphate phosphatase;
            inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase;
            inositol 1,3,4,5-tetrakisphosphate 3-phosphomonoesterase;
            inositol 1,3,4,5-tetrakisphosphate-5-phosphomonoesterase;
            inositol tetrakisphosphate phosphomonoesterase;
            inositol-1,3,4,5-tetrakisphosphate 3-phosphatase;
            MIPP
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     1D-myo-inositol-hexakisphosphate 5-phosphohydrolase
REACTION    myo-inositol hexakisphosphate + H2O = myo-inositol pentakisphosphate
            (mixed isomers) + phosphate [RN:R07584]
ALL_REAC    R07584 > R03371 R03372 R07583;
            (other) R03434
SUBSTRATE   myo-inositol hexakisphosphate [CPD:C01204];
            H2O [CPD:C00001]
PRODUCT     myo-inositol pentakisphosphate [CPD:C15991];
            phosphate [CPD:C00009]
COMMENT     This enzyme exists in two isoforms. It also acts on Ins(1,3,4,5)P4
            to yield Ins(1,4,5)P3.
REFERENCE   1  [PMID:2786415]
  AUTHORS   Cullen PJ, Irvine RF, Drobak BK, Dawson AP.
  TITLE     Inositol 1,3,4,5-tetrakisphosphate causes release of Ca2+ from
            permeabilized mouse lymphoma L1210 cells by its conversion into
            inositol 1,4,5-trisphosphate.
  JOURNAL   Biochem. J. 259 (1989) 931-3.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:9359836]
  AUTHORS   Craxton A, Caffrey JJ, Burkhart W, Safrany ST, Shears SB.
  TITLE     Molecular cloning and expression of a rat hepatic multiple inositol
            polyphosphate phosphatase.
  JOURNAL   Biochem. J. 328 ( Pt 1) (1997) 75-81.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00562  Inositol phosphate metabolism
ORTHOLOGY   KO: K03103  multiple inositol-polyphosphate phosphatase
GENES       HSA: 9562(MINPP1)
            PTR: 450579(MINPP1)
            MMU: 17330(Minpp1)
            CFA: 486462(MINPP1)
            GGA: 395356(MINPP1)
            DRE: 394075(zgc:56080)
            DME: Dmel_CG4317(Mipp2)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.62
            ExPASy - ENZYME nomenclature database: 3.1.3.62
            ExplorEnz - The Enzyme Database: 3.1.3.62
            ERGO genome analysis and discovery system: 3.1.3.62
            BRENDA, the Enzyme Database: 3.1.3.62
            CAS: 116958-30-6
///
ENTRY       EC 3.1.3.63                 Enzyme
NAME        2-carboxy-D-arabinitol-1-phosphatase;
            2-carboxyarabinitol 1-phosphatase;
            2-carboxy-D-arabinitol 1-phosphate phosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     2-carboxy-D-arabinitol-1-phosphate 1-phosphohydrolase
REACTION    2-carboxy-D-arabinitol 1-phosphate + H2O = 2-carboxy-D-arabinitol +
            phosphate [RN:R04167]
ALL_REAC    R04167
SUBSTRATE   2-carboxy-D-arabinitol 1-phosphate [CPD:C04234];
            H2O [CPD:C00001]
PRODUCT     2-carboxy-D-arabinitol [CPD:C03215];
            phosphate [CPD:C00009]
REFERENCE   1
  AUTHORS   Salvucci, M.E. and Holbrook, G.P.
  TITLE     Purification and properties of 2-carboxy-D-arabinitol 1-phosphatase.
  JOURNAL   Plant Physiol. 90 (1989) 679-685.
  ORGANISM  Nicotiana tabacum
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.63
            ExPASy - ENZYME nomenclature database: 3.1.3.63
            ExplorEnz - The Enzyme Database: 3.1.3.63
            ERGO genome analysis and discovery system: 3.1.3.63
            BRENDA, the Enzyme Database: 3.1.3.63
            CAS: 122319-88-4
///
ENTRY       EC 3.1.3.64                 Enzyme
NAME        phosphatidylinositol-3-phosphatase;
            inositol-1,3-bisphosphate 3-phosphatase;
            inositol 1,3-bisphosphate phosphatase;
            inositol-polyphosphate 3-phosphatase;
            D-myo-inositol-1,3-bisphosphate 3-phosphohydrolase;
            phosphatidyl-3-phosphate 3-phosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     1-phosphatidyl-1D-myo-inositol-3-phosphate 3-phosphohydrolase
REACTION    1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O =
            1-phosphatidyl-1D-myo-inositol + phosphate [RN:R03363]
ALL_REAC    R03363;
            (other) R03330 R06875
SUBSTRATE   1-phosphatidyl-1D-myo-inositol 3-phosphate [CPD:C04549];
            H2O [CPD:C00001]
PRODUCT     1-phosphatidyl-1D-myo-inositol [CPD:C01194];
            phosphate [CPD:C00009]
COMMENT     This enzyme still works when the 2,3-bis(acyloxy)propyl group is
            removed, i.e., it hydrolyses Ins(1,3)P2 to Ins-1-P.
REFERENCE   1  [PMID:2555336]
  AUTHORS   Lips DL, Majerus PW.
  TITLE     The discovery of a 3-phosphomonoesterase that hydrolyzes
            phosphatidylinositol 3-phosphate in NIH 3T3 cells.
  JOURNAL   J. Biol. Chem. 264 (1989) 19911-5.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:1655747]
  AUTHORS   Caldwell KK, Lips DL, Bansal VS, Majerus PW.
  TITLE     Isolation and characterization of two 3-phosphatases that hydrolyze
            both phosphatidylinositol 3-phosphate and inositol 1,3-bisphosphate.
  JOURNAL   J. Biol. Chem. 266 (1991) 18378-86.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00562  Inositol phosphate metabolism
            PATH: map04070  Phosphatidylinositol signaling system
ORTHOLOGY   KO: K01108  phosphatidylinositol-3-phosphatase
STRUCTURES  PDB: 1LW3  1M7R  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.64
            ExPASy - ENZYME nomenclature database: 3.1.3.64
            ExplorEnz - The Enzyme Database: 3.1.3.64
            ERGO genome analysis and discovery system: 3.1.3.64
            BRENDA, the Enzyme Database: 3.1.3.64
            CAS: 124248-47-1
///
ENTRY       EC 3.1.3.65       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
COMMENT     Deleted entry: inositol-1,3-bisphosphate 3-phosphatase. Now included
            with EC 3.1.3.64, phosphatidylinositol-3-phosphatase (EC 3.1.3.65
            created 1992, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.65
            ExPASy - ENZYME nomenclature database: 3.1.3.65
            ExplorEnz - The Enzyme Database: 3.1.3.65
            ERGO genome analysis and discovery system: 3.1.3.65
            BRENDA, the Enzyme Database: 3.1.3.65
///
ENTRY       EC 3.1.3.66                 Enzyme
NAME        phosphatidylinositol-3,4-bisphosphate 4-phosphatase;
            inositol-3,4-bisphosphate 4-phosphatase;
            D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase;
            phosphoinositide 4-phosphatase;
            inositol polyphosphate 4-phosphatase;
            D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase;
            inositol polyphosphate 4-phosphatase type II
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     1-phosphatidyl-1D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase
REACTION    1-phosphatidyl-myo-inositol 3,4-bisphosphate + H2O =
            1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate [RN:R07299]
ALL_REAC    R07299;
            (other) R04372
SUBSTRATE   1-phosphatidyl-myo-inositol 3,4-bisphosphate;
            H2O [CPD:C00001]
PRODUCT     1-phosphatidyl-1D-myo-inositol 3-phosphate [CPD:C04549];
            phosphate [CPD:C00009]
COMMENT     Mg2+-independent. This enzyme still works when the
            2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyses
            Ins(1,3,4)P3 to Ins(1,3)P2. It also converts Ins(3,4)P2 into
            Ins-3-P.
REFERENCE   1  [PMID:2546770]
  AUTHORS   Howell S, Barnaby RJ, Rowe T, Ragan CI, Gee NS.
  TITLE     Evidence for at least four different inositol bisphosphatases in
            bovine brain.
  JOURNAL   Eur. J. Biochem. 183 (1989) 169-72.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:7608176]
  AUTHORS   Norris FA, Auethavekiat V, Majerus PW.
  TITLE     The isolation and characterization of cDNA encoding human and rat
            brain inositol polyphosphate 4-phosphatase.
  JOURNAL   J. Biol. Chem. 270 (1995) 16128-33.
  ORGANISM  rat [GN:rno], human [GN:hsa]
REFERENCE   3  [PMID:9295334]
  AUTHORS   Norris FA, Atkins RC, Majerus PW.
  TITLE     The cDNA cloning and characterization of inositol polyphosphate
            4-phosphatase type II. Evidence for conserved alternative splicing
            in the 4-phosphatase family.
  JOURNAL   J. Biol. Chem. 272 (1997) 23859-64.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00562  Inositol phosphate metabolism
            PATH: map04070  Phosphatidylinositol signaling system
ORTHOLOGY   KO: K01109  inositol polyphosphate-4-phosphatase
GENES       HSA: 3631(INPP4A) 8821(INPP4B)
            PTR: 461514(INPP4B)
            MMU: 234515(Inpp4b) 269180(Inpp4a)
            RNO: 116699(Inpp4b) 80849(Inpp4a)
            CFA: 474563(INPP4A) 476072(INPP4B)
            GGA: 418690(INPP4A) 422454(INPP4B)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.66
            ExPASy - ENZYME nomenclature database: 3.1.3.66
            ExplorEnz - The Enzyme Database: 3.1.3.66
            ERGO genome analysis and discovery system: 3.1.3.66
            BRENDA, the Enzyme Database: 3.1.3.66
            CAS: 122653-78-5
///
ENTRY       EC 3.1.3.67                 Enzyme
NAME        phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase;
            PTEN, MMAC1;
            phosphatidylinositol-3,4,5-trisphosphate 3-phosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     1-phosphatidyl-1D-myo-inositol-3,4,5-trisphosphate
            3-phosphohydrolase
REACTION    phosphatidylinositol 3,4,5-trisphosphate + H2O =
            phosphatidylinositol 4,5-bisphosphate + phosphate [RN:R04513]
ALL_REAC    R04513
SUBSTRATE   phosphatidylinositol 3,4,5-trisphosphate;
            H2O [CPD:C00001]
PRODUCT     phosphatidylinositol 4,5-bisphosphate;
            phosphate [CPD:C00009]
COFACTOR    Magnesium [CPD:C00305]
COMMENT     Requires Mg2+. Does not dephosphorylate inositol 4,5-bisphosphate.
            This enzyme still works when the 2,3-bis(acyloxy)propyl group is
            removed, i.e., it hydrolyses Ins(1,3,4,5)P4 to Ins(1,4,5)P3
REFERENCE   1  [PMID:8681945]
  AUTHORS   Kabuyama Y, Nakatsu N, Homma Y, Fukui Y.
  TITLE     Purification and characterization of the
            phosphatidylinositol-3,4,5-trisphosphate phosphatase in bovine
            thymus.
  JOURNAL   Eur. J. Biochem. 238 (1996) 350-6.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:9593664]
  AUTHORS   Maehama T, Dixon JE.
  TITLE     The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second
            messenger, phosphatidylinositol 3,4,5-trisphosphate.
  JOURNAL   J. Biol. Chem. 273 (1998) 13375-8.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00562  Inositol phosphate metabolism
            PATH: map04070  Phosphatidylinositol signaling system
            PATH: map04115  p53 signaling pathway
            PATH: map04510  Focal adhesion
            PATH: map04530  Tight junction
            PATH: map05213  Endometrial cancer
            PATH: map05214  Glioma
            PATH: map05215  Prostate cancer
            PATH: map05218  Melanoma
            PATH: map05222  Small cell lung cancer
ORTHOLOGY   KO: K01110  phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
GENES       HSA: 5728(PTEN)
            PTR: 466142(PTEN)
            MMU: 19211(Pten)
            RNO: 50557(Pten)
            CFA: 403832(PTEN)
            BTA: 540786(LOC540786)
            DRE: 325051(ptena) 368415(ptenb)
            SPU: 590938(LOC590938)
            DME: Dmel_CG5671
            ATH: AT3G19420 AT3G50110
            DDI: DDBDRAFT_0218761 DDB_0191093(pteN)
            TET: TTHERM_00313160 TTHERM_00538950
            TCR: 510879.160
            EHI: 19.t00008 355.t00004 92.t00017
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.67
            ExPASy - ENZYME nomenclature database: 3.1.3.67
            ExplorEnz - The Enzyme Database: 3.1.3.67
            ERGO genome analysis and discovery system: 3.1.3.67
            BRENDA, the Enzyme Database: 3.1.3.67
///
ENTRY       EC 3.1.3.68                 Enzyme
NAME        2-deoxyglucose-6-phosphatase;
            2-deoxyglucose-6-phosphate phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     2-deoxy-D-glucose-6-phosphate phosphohydrolase
REACTION    2-deoxy-D-glucose 6-phosphate + H2O = 2-deoxy-D-glucose + phosphate
            [RN:R02587]
ALL_REAC    R02587;
            (other) R02069
SUBSTRATE   2-deoxy-D-glucose 6-phosphate [CPD:C06369];
            H2O [CPD:C00001]
PRODUCT     2-deoxy-D-glucose [CPD:C00586];
            phosphate [CPD:C00009]
COMMENT     Also active towards fructose 1-phosphate
REFERENCE   1  [PMID:8091229]
  AUTHORS   Johnston M, Andrews S, Brinkman R, Cooper J, Ding H, Dover J, Du Z,
            Favello A, Fulton L, Gattung S, et al.
  TITLE     Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
            VIII.
  JOURNAL   Science. 265 (1994) 2077-82.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:8553694]
  AUTHORS   Randez-Gil F, Blasco A, Prieto JA, Sanz P.
  TITLE     DOGR1 and DOGR2: two genes from Saccharomyces cerevisiae that confer
            2-deoxyglucose resistance when overexpressed.
  JOURNAL   Yeast. 11 (1995) 1233-40.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K01111  2-deoxyglucose-6-phosphatase
GENES       SCE: YHR043C(DOG2) YHR044C(DOG1)
            AGO: AGOS_AAL123W
            CGR: CAGL0D04092g
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.68
            ExPASy - ENZYME nomenclature database: 3.1.3.68
            ExplorEnz - The Enzyme Database: 3.1.3.68
            ERGO genome analysis and discovery system: 3.1.3.68
            BRENDA, the Enzyme Database: 3.1.3.68
            CAS: 65187-56-6
///
ENTRY       EC 3.1.3.69                 Enzyme
NAME        glucosylglycerol 3-phosphatase;
            salt tolerance protein A, StpA
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     2-(beta-D-glucosyl)-sn-glycerol-3-phosphate phosphohydrolase
REACTION    2-(beta-D-glucosyl)-sn-glycerol-3-phosphate + H2O =
            2-(beta-D-glucosyl)-sn-glycerol + phosphate [RN:R05791]
ALL_REAC    R05791
SUBSTRATE   2-(beta-D-glucosyl)-sn-glycerol-3-phosphate;
            H2O [CPD:C00001]
PRODUCT     2-(beta-D-glucosyl)-sn-glycerol [CPD:C11546];
            phosphate [CPD:C00009]
COMMENT     Acts with EC 2.4.1.213 (glucosylglycerol-phosphate synthase) to form
            glucosylglycerol, an osmolyte that endows cyanobacteria with
            resistance to salt.
REFERENCE   1
  AUTHORS   Hagemann, M. and Erdmann, N.
  TITLE     Activation and pathway of glucosylglycerol biosynthesis in the
            cyanobacterium Synechocystis sp. PCC 6803.
  JOURNAL   Microbiology 140 (1994) 1427-1431.
  ORGANISM  Synechosytis sp.
REFERENCE   2  [PMID:8772170]
  AUTHORS   Hagemann M, Richter S, Zuther E, Schoor A.
  TITLE     Characterization of a glucosylglycerol-phosphate-accumulating,
            salt-sensitive mutant of the cyanobacterium Synechocystis sp. strain
            PCC 6803.
  JOURNAL   Arch. Microbiol. 166 (1996) 83-91.
  ORGANISM  Synechosytis sp.
REFERENCE   3  [PMID:9045835]
  AUTHORS   Hagemann M, Schoor A, Jeanjean R, Zuther E, Joset F.
  TITLE     The stpA gene form synechocystis sp. strain PCC 6803 encodes the
            glucosylglycerol-phosphate phosphatase involved in cyanobacterial
            osmotic response to salt shock.
  JOURNAL   J. Bacteriol. 179 (1997) 1727-33.
  ORGANISM  Synechosytis sp.
ORTHOLOGY   KO: K05978  
GENES       SYN: slr0746(stpA)
            SYW: SYNW0860(stpA)
            SYD: Syncc9605_1780
            SYE: Syncc9902_0865
            SYG: sync_1171(stpA)
            SYR: SynRCC307_1379(stpA)
            SYX: SynWH7803_1398(stpA)
            PMA: Pro0796
            PMM: PMM0639(stpA)
            PMT: PMT0863(stpA)
            PMN: PMN2A_0079
            PMI: PMT9312_0639
            PMB: A9601_06951(stpA)
            PMC: P9515_07051(stpA)
            PMF: P9303_13331(stpA)
            PMG: P9301_06661(stpA)
            PME: NATL1_07021(stpA)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.69
            ExPASy - ENZYME nomenclature database: 3.1.3.69
            ExplorEnz - The Enzyme Database: 3.1.3.69
            ERGO genome analysis and discovery system: 3.1.3.69
            BRENDA, the Enzyme Database: 3.1.3.69
///
ENTRY       EC 3.1.3.70                 Enzyme
NAME        mannosyl-3-phosphoglycerate phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     alpha-D-mannosyl-3-phosphoglycerate phosphohydrolase
REACTION    2(alpha-D-mannosyl)-3-phosphoglycerate + H2O =
            2(alpha-D-mannosyl)-D-glycerate + phosphate [RN:R05790]
ALL_REAC    R05790
SUBSTRATE   2(alpha-D-mannosyl)-3-phosphoglycerate;
            H2O [CPD:C00001]
PRODUCT     2(alpha-D-mannosyl)-D-glycerate [CPD:C11544];
            phosphate [CPD:C00009]
COMMENT     Requires Mg2+. The enzyme from Pyrococcus horikoshii is specific for
            alpha-D-mannosyl-3-phosphoglycerate and forms part of the pathway
            for the synthesis of mannosylglycerate.
REFERENCE   1  [PMID:11562374]
  AUTHORS   Empadinhas N, Marugg JD, Borges N, Santos H, da Costa MS.
  TITLE     Pathway for the synthesis of mannosylglycerate in the
            hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and
            genetic characterization of key enzymes.
  JOURNAL   J. Biol. Chem. 276 (2001) 43580-8.
  ORGANISM  Pyrococcus horikoshii [GN:pho]
ORTHOLOGY   KO: K07026  mannosyl-3-phosphoglycerate phosphatase
GENES       ECO: b1955(yedP)
            ECJ: JW1938(yedP)
            ECE: Z3045
            ECS: ECs2693
            ECC: c2373(yedP)
            ECI: UTI89_C2156
            ECP: ECP_1888
            ECV: APECO1_993(yedP)
            STY: STY2193
            STT: t0892
            SPT: SPA0884(yedP)
            SEC: SC1990(yedP)
            STM: STM1986(yedP)
            SSN: SSON_2012
            SBO: SBO_1053
            SDY: SDY_1051
            ECA: ECA2248
            ENT: Ent638_2545
            SPE: Spro_2341
            PCR: Pcryo_2501
            SFR: Sfri_2848
            CPS: CPS_0508
            PAT: Patl_2162
            SDE: Sde_3208
            PIN: Ping_2602
            MAQ: Maqu_2568 Maqu_2575 Maqu_2582
            TCX: Tcr_0772
            HCH: HCH_00271
            CSA: Csal_2604
            SIT: TM1040_0421
            RDE: RD1_3713(mpgP)
            SYW: SYNW2434
            SYD: Syncc9605_2605
            SYE: Syncc9902_2242
            CYA: CYA_1804
            CYB: CYB_2388
            PMA: Pro0729
            PMM: PMM0960
            PMN: PMN2A_0247(yedP)
            PMI: PMT9312_0839
            TTH: TTC0589
            TTJ: TTHA0955
            MBU: Mbur_0736
            PHO: PH0926
            PAB: PAB0817
            PFU: PF0590
            APE: APE_0887.1
STRUCTURES  PDB: 1WZC  1XVI  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.70
            ExPASy - ENZYME nomenclature database: 3.1.3.70
            ExplorEnz - The Enzyme Database: 3.1.3.70
            ERGO genome analysis and discovery system: 3.1.3.70
            BRENDA, the Enzyme Database: 3.1.3.70
///
ENTRY       EC 3.1.3.71                 Enzyme
NAME        2-phosphosulfolactate phosphatase;
            (2R)-phosphosulfolactate phosphohydrolase;
            ComB phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     (R)-2-phospho-3-sulfolactate phosphohydrolase
REACTION    (2R)-2-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate +
            phosphate [RN:R05789]
ALL_REAC    R05789
SUBSTRATE   (2R)-2-phospho-3-sulfolactate;
            H2O [CPD:C00001]
PRODUCT     (2R)-3-sulfolactate [CPD:C11537];
            phosphate [CPD:C00009]
COMMENT     Requires Mg2+. The enzyme from Methanococcus jannaschii acts on both
            stereoisoimers of the substrate and also hydrolyses a number of
            phosphate monoesters of (S)-2-hydroxycarboxylic acids, including
            2-phosphomalate, 2-phospholactate and 2-phosphoglycolate. This
            enzyme can also hydrolyze phosphate monoesters of
            (R)-2-hydroxycarboxylic acids such as (S)-2-phospho-3-sulfolactate
            and (R)-2-phosphomalate, which, presumably, bind to the enzyme in
            opposite orientations.
REFERENCE   1  [PMID:11589710]
  AUTHORS   Graham DE, Graupner M, Xu H, White RH.
  TITLE     Identification of coenzyme M biosynthetic 2-phosphosulfolactate
            phosphatase. A member of a new class of Mg(2+)-dependent acid
            phosphatases.
  JOURNAL   Eur. J. Biochem. 268 (2001) 5176-88.
  ORGANISM  Methanococcus jannaschii [GN:mja]
ORTHOLOGY   KO: K05979  
GENES       EHI: 87.t00023
            CBU: CBU_1392
            CBD: COXBU7E912_0601(comB)
            DAR: Daro_4162
            BSU: BG13108(yitC)
            GKA: GK1033
            STH: STH1711
            CAC: CAC3233
            CPE: CPE2556
            CPF: CPF_2881(comB)
            CPR: CPR_2562(comB)
            CTC: CTC00180
            CNO: NT01CX_0616
            CBO: CBO3553
            CBA: CLB_3635
            CBH: CLC_3533
            CBF: CLI_3775
            CBE: Cbei_0040
            CKL: CKL_0138(comB)
            DRM: Dred_2444
            CSC: Csac_0183
            TTE: TTE1972
            MTA: Moth_0119
            SCO: SCO7611(SC2H2.09)
            RXY: Rxyl_0750 Rxyl_2338
            RBA: RB12002
            SYN: slr1718
            SYW: SYNW1007
            SYC: syc1521_c
            SYF: Synpcc7942_2589
            SYD: Syncc9605_1133
            SYE: Syncc9902_1324
            SYG: sync_1547(comB)
            SYR: SynRCC307_1155(comB)
            SYX: SynWH7803_1034(comB)
            CYA: CYA_0651(comB)
            CYB: CYB_0287(comB)
            TEL: tll0403
            GVI: gll2974
            ANA: all2568
            AVA: Ava_0497
            PMA: Pro1046
            PMM: PMM0614
            PMT: PMT0396
            PMN: PMN2A_0051
            PMI: PMT9312_0614
            PMB: A9601_06701
            PMC: P9515_06791
            PMF: P9303_18911
            PMG: P9301_06401
            PME: NATL1_06721
            TER: Tery_1206
            PGI: PG0013
            SRU: SRU_1618
            DRA: DR_1400
            DGE: Dgeo_1318
            TTH: TTC1073
            TTJ: TTHA1438
            TMA: TM0797
            TPT: Tpet_0131
            TME: Tmel_0377
            FNO: Fnod_0473
            MJA: MJ1140
            MMP: MMP0161(comB)
            MMQ: MmarC5_1514
            MMZ: MmarC7_1161
            MAE: Maeo_1002
            MVN: Mevan_1166
            MTH: MTH1182
            MST: Msp_0286(comB1) Msp_0973(comB2)
            MKA: MK0138
            TAC: Ta1432
            TVO: TVN0096
            PTO: PTO0436
            RCI: RCIX630(comB)
STRUCTURES  PDB: 1VR0  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.71
            ExPASy - ENZYME nomenclature database: 3.1.3.71
            ExplorEnz - The Enzyme Database: 3.1.3.71
            ERGO genome analysis and discovery system: 3.1.3.71
            BRENDA, the Enzyme Database: 3.1.3.71
///
ENTRY       EC 3.1.3.72                 Enzyme
NAME        5-phytase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     myo-inositol-hexakisphosphate 5-phosphohydrolase
REACTION    myo-inositol hexakisphosphate + H2O = 1L-myo-inositol
            1,2,3,4,6-pentakisphosphate + phosphate [RN:R07583]
ALL_REAC    R07583
SUBSTRATE   myo-inositol hexakisphosphate [CPD:C01204];
            H2O [CPD:C00001]
PRODUCT     1L-myo-inositol 1,2,3,4,6-pentakisphosphate [CPD:C15990];
            phosphate [CPD:C00009]
COMMENT     The enzyme attacks the product of the above reaction more slowly to
            yield Ins(1,2,3)P3.
REFERENCE   1  [PMID:7846160]
  AUTHORS   Barrientos L, Scott JJ, Murthy PP.
  TITLE     Specificity of hydrolysis of phytic acid by alkaline phytase from
            lily pollen.
  JOURNAL   Plant. Physiol. 106 (1994) 1489-95.
  ORGANISM  Lilium longiflorum
STRUCTURES  PDB: 1U24  1U25  1U26  2B4O  2B4P  2B4U  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.72
            ExPASy - ENZYME nomenclature database: 3.1.3.72
            ExplorEnz - The Enzyme Database: 3.1.3.72
            ERGO genome analysis and discovery system: 3.1.3.72
            BRENDA, the Enzyme Database: 3.1.3.72
            CAS: 37341-58-5
///
ENTRY       EC 3.1.3.73                 Enzyme
NAME        alpha-ribazole phosphatase;
            CobC
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     alpha-ribazole-5'-phosphate phosphohydrolase
REACTION    alpha-ribazole 5'-phosphate + H2O = alpha-ribazole + phosphate
            [RN:R04594]
ALL_REAC    R04594
SUBSTRATE   alpha-ribazole 5'-phosphate [CPD:C04778];
            H2O [CPD:C00001]
PRODUCT     alpha-ribazole [CPD:C05775];
            phosphate [CPD:C00009]
COMMENT     In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC
            2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73)
            and CobS (EC 2.7.8.26) catalyse reactions in the nucleotide loop
            assembly pathway, which convert adenosylcobinamide (AdoCbi) into
            adenosylcobalamin (AdoCbl). CobT and CobC are involved in
            5,6-dimethylbenzimidazole activation whereby
            5,6-dimethylbenzimidazole is converted to its riboside,
            alpha-ribazole. The second branch of the nuclotide loop assembly
            pathway is the cobinamide (Cbi) activation branch where AdoCbi or
            adenosylcobinamide-phosphate is converted to the activated
            intermediate AdoCbi-GDP by the bifunctional enzyme CobU. CobS
            catalyses the final step in adenosylcobalamin biosynthesis, which is
            the condensation of AdoCbi-GDP with alpha-ribazole to yield
            adenosylcobalamin.
REFERENCE   1  [PMID:7929373]
  AUTHORS   O'Toole GA, Trzebiatowski JR, Escalante-Semerena JC.
  TITLE     The cobC gene of Salmonella typhimurium codes for a novel
            phosphatase involved in the assembly of the nucleotide loop of
            cobalamin.
  JOURNAL   J. Biol. Chem. 269 (1994) 26503-11.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:12195810]
  AUTHORS   Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
  TITLE     The biosynthesis of adenosylcobalamin (vitamin B12).
  JOURNAL   Nat. Prod. Rep. 19 (2002) 390-412.
  ORGANISM  Escherichia coli [GN:eco], Salmonella enterica
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K02226  alpha-ribazole phosphatase
GENES       ECO: b0638(phpB)
            ECJ: JW0633(cobC)
            ECE: Z0785(phpB)
            ECS: ECs0676
            ECC: c0729(phpB)
            ECI: UTI89_C0641(phpB)
            ECV: APECO1_1417(phpB)
            ECW: EcE24377A_0664(cobC)
            ECX: EcHS_A0690(cobC)
            STY: STY0694(phpB)
            STT: t2224(cobC)
            SPT: SPA2091(cobC)
            SEC: SC0673(cobC)
            STM: STM0643(cobC)
            SFL: SF0643(phpB)
            SFX: S0665(phpB)
            SFV: SFV_0688(phpB)
            SSN: SSON_0592(phpB)
            PLU: plu2981(cobC)
            VCH: VC1240
            VVU: VV1_2785
            VVY: VV1477
            VPA: VP1307(cobC)
            PEN: PSEEN1386
            PAT: Patl_1136
            VOK: COSY_0841(cobC)
            REH: H16_A2966(cobC)
            BMN: BMA10247_1634(cobC-2)
            BPL: BURPS1106A_1039(cobC)
            BPD: BURPS668_1033(cobC)
            AZO: azo3562
            TDN: Tmden_0110
            MXA: MXAN_2572(cobC)
            BRA: BRADO4917
            BBT: BBta_3134
            GBE: GbCGDNIH1_0069
            BHA: BH1593
            LMO: lmo1149
            LMF: LMOf2365_1156(cobC)
            LIN: lin1113
            LWE: lwe1107(cobC)
            SSA: SSA_0491
            CAC: CAC1385(cobC)
            CPE: CPE1038(cobC)
            CPF: CPF_1293
            CPR: CPR_1112
            CTC: CTC00717
            CNO: NT01CX_2080
            CBA: CLB_0860(cobC)
            CBH: CLC_0874(cobC)
            CBF: CLI_0900(cobC)
            CKL: CKL_0191(cobC1) CKL_0732(cobC2)
            DSY: DSY1979(cobC)
            FNU: FN0911
            PMF: P9303_09371
            DET: DET0659 DET0693
            DEH: cbdb_A643(cobC)
STRUCTURES  PDB: 2ENU  2ENW  2EOA  2OWE  2P2Y  2P2Z  2P30  2P6M  2P6O  2P75  
                 2P77  2P78  2P79  2P9Y  2P9Z  2PA0  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.73
            ExPASy - ENZYME nomenclature database: 3.1.3.73
            ExplorEnz - The Enzyme Database: 3.1.3.73
            ERGO genome analysis and discovery system: 3.1.3.73
            BRENDA, the Enzyme Database: 3.1.3.73
            CAS: 251991-06-7
///
ENTRY       EC 3.1.3.74                 Enzyme
NAME        pyridoxal phosphatase;
            vitamine B6 (pyridoxine) phosphatase;
            PLP phosphatase;
            vitamin B6-phosphate phosphatase;
            PNP phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     pyridoxal-5'-phosphate phosphohydrolase
REACTION    pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate [RN:R00173]
ALL_REAC    R00173;
            (other) R01911 R02494
SUBSTRATE   pyridoxal 5'-phosphate [CPD:C00018];
            H2O [CPD:C00001]
PRODUCT     pyridoxal [CPD:C00250];
            phosphate [CPD:C00009]
COMMENT     Requires Mg2+. This enzyme is specific for phosphorylated vitamin B6
            compounds: it acts not only on pyridoxal phosphate (PLP), but also
            on pyridoxine phosphate (PNP), pyridoxamine phosphate (PMP),
            4-pyridoxic acid phosphate and 4-deoxypyridoxine phosphate. This
            reaction can also be carried out by EC 3.1.3.1 (alkaline
            phosphatase) and EC 3.1.3.2 (acid phosphatase), but these enzymes
            have very broad substrate specificities.
REFERENCE   1  [PMID:1322411]
  AUTHORS   Fonda ML.
  TITLE     Purification and characterization of vitamin B6-phosphate
            phosphatase from human erythrocytes.
  JOURNAL   J. Biol. Chem. 267 (1992) 15978-83.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:7625842]
  AUTHORS   Fonda ML, Zhang YN.
  TITLE     Kinetic mechanism and divalent metal activation of human erythrocyte
            pyridoxal phosphatase.
  JOURNAL   Arch. Biochem. Biophys. 320 (1995) 345-52.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:14522954]
  AUTHORS   Jang YM, Kim DW, Kang TC, Won MH, Baek NI, Moon BJ, Choi SY, Kwon
            OS.
  TITLE     Human pyridoxal phosphatase. Molecular cloning, functional
            expression, and tissue distribution.
  JOURNAL   J. Biol. Chem. 278 (2003) 50040-6.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00750  Vitamin B6 metabolism
ORTHOLOGY   KO: K07758  pyridoxal phosphatase
GENES       HSA: 57026(PDXP)
            MMU: 57028(Pdxp)
            RNO: 300067(Sh3bp1_predicted)
            SRU: SRU_1890
STRUCTURES  PDB: 2CFR  2CFS  2CFT  2OYC  2P27  2P69  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.74
            ExPASy - ENZYME nomenclature database: 3.1.3.74
            ExplorEnz - The Enzyme Database: 3.1.3.74
            ERGO genome analysis and discovery system: 3.1.3.74
            BRENDA, the Enzyme Database: 3.1.3.74
///
ENTRY       EC 3.1.3.75                 Enzyme
NAME        phosphoethanolamine/phosphocholine phosphatase;
            PHOSPHO1;
            3X11A
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     phosphoethanolamine phosphohydrolase
REACTION    (1) O-phosphoethanolamine + H2O = ethanolamine + phosphate
            [RN:R06870];
            (2) phosphocholine + H2O = choline + phosphate [RN:R06871]
ALL_REAC    R06870 R06871
SUBSTRATE   O-phosphoethanolamine [CPD:C00346];
            H2O [CPD:C00001];
            phosphocholine [CPD:C00588]
PRODUCT     ethanolamine [CPD:C00189];
            phosphate [CPD:C00009];
            choline [CPD:C00114]
COMMENT     Requires active site Mg2+ but also works, to a lesser extent, with
            Co2+ and Mn2+. The enzyme is highly specific for phosphoethanolamine
            and phosphocholine.
REFERENCE   1  [PMID:9990301]
  AUTHORS   Houston B, Seawright E, Jefferies D, Hoogland E, Lester D, Whitehead
            C, Farquharson C.
  TITLE     Identification and cloning of a novel phosphatase expressed at high
            levels in differentiating growth plate chondrocytes.
  JOURNAL   Biochim. Biophys. Acta. 1448 (1999) 500-6.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:14983068]
  AUTHORS   Stewart AJ, Schmid R, Blindauer CA, Paisey SJ, Farquharson C.
  TITLE     Comparative modelling of human PHOSPHO1 reveals a new group of
            phosphatases within the haloacid dehalogenase superfamily.
  JOURNAL   Protein. Eng. 16 (2003) 889-95.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:15175005]
  AUTHORS   Roberts SJ, Stewart AJ, Sadler PJ, Farquharson C.
  TITLE     Human PHOSPHO1 exhibits high specific phosphoethanolamine and
            phosphocholine phosphatase activities.
  JOURNAL   Biochem. J. 382 (2004) 59-65.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K06124  phosphoethanolamine/phosphocholine phosphatase
GENES       HSA: 162466(PHOSPHO1)
            MMU: 237928(Phospho1)
            RNO: 287644(Phospho1_predicted)
            CFA: 491069(PHOSPHO1)
            GGA: 395650(PHOSPHO1)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.75
            ExPASy - ENZYME nomenclature database: 3.1.3.75
            ExplorEnz - The Enzyme Database: 3.1.3.75
            ERGO genome analysis and discovery system: 3.1.3.75
            BRENDA, the Enzyme Database: 3.1.3.75
///
ENTRY       EC 3.1.3.76                 Enzyme
NAME        lipid-phosphate phosphatase;
            hydroxy fatty acid phosphatase;
            dihydroxy fatty acid phosphatase;
            hydroxy lipid phosphatase;
            sEH (ambiguous);
            soluble epoxide hydrolase (ambiguous)
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate phosphohydrolase
REACTION    (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H2O =
            (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate [RN:R07582]
ALL_REAC    R07582
SUBSTRATE   (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate [CPD:C15989];
            H2O [CPD:C00001]
PRODUCT     (9S,10S)-9,10-dihydroxyoctadecanoate [CPD:C15988];
            phosphate [CPD:C00009]
COMMENT     Requires Mg2+ for maximal activity. The enzyme from mammals is a
            bifunctional enzyme: the N-terminal domain exhibits
            lipid-phosphate-phosphatase activity and the C-terminal domain has
            the activity of EC 3.3.2.10, soluble epoxide hydrolase (sEH) [1].
            The best substrates for this enzyme are
            10-hydroxy-9-(phosphonooxy)octadecanoates, with the threo- form
            being a better substrate than the erythro- form [1]. The phosphatase
            activity is not found in plant sEH or in EC 3.3.2.9, microsomal
            epoxide hydrolase, from mammals [1].
REFERENCE   1  [PMID:12574510]
  AUTHORS   Newman JW, Morisseau C, Harris TR, Hammock BD.
  TITLE     The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional
            enzyme with novel lipid phosphate phosphatase activity.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 1558-63.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:12574508]
  AUTHORS   Cronin A, Mowbray S, Durk H, Homburg S, Fleming I, Fisslthaler B,
            Oesch F, Arand M.
  TITLE     The N-terminal domain of mammalian soluble epoxide hydrolase is a
            phosphatase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 1552-7.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:15822179]
  AUTHORS   Morisseau C, Hammock BD.
  TITLE     Epoxide hydrolases: mechanisms, inhibitor designs, and biological
            roles.
  JOURNAL   Annu. Rev. Pharmacol. Toxicol. 45 (2005) 311-33.
  ORGANISM  mammalian
REFERENCE   4  [PMID:16142916]
  AUTHORS   Tran KL, Aronov PA, Tanaka H, Newman JW, Hammock BD, Morisseau C.
  TITLE     Lipid sulfates and sulfonates are allosteric competitive inhibitors
            of the N-terminal phosphatase activity of the mammalian soluble
            epoxide hydrolase.
  JOURNAL   Biochemistry. 44 (2005) 12179-87.
  ORGANISM  mammalian
REFERENCE   5  [PMID:15748653]
  AUTHORS   Newman JW, Morisseau C, Hammock BD.
  TITLE     Epoxide hydrolases: their roles and interactions with lipid
            metabolism.
  JOURNAL   Prog. Lipid. Res. 44 (2005) 1-51.
  ORGANISM  human [GN:hsa], rainbow trout, Oryzias latipes, Pimphales promelas,
            Stenotomus chrysops, mouse [GN:mmu], rat [GN:rno], rabbit, guinea
            pig, hamster, pig [GN:ssc], horse, monkey, baboon
REFERENCE   6  [PMID:15196990]
  AUTHORS   Srivastava PK, Sharma VK, Kalonia DS, Grant DF.
  TITLE     Polymorphisms in human soluble epoxide hydrolase: effects on enzyme
            activity, enzyme stability, and quaternary structure.
  JOURNAL   Arch. Biochem. Biophys. 427 (2004) 164-9.
  ORGANISM  human [GN:hsa]
REFERENCE   7  [PMID:15096040]
  AUTHORS   Gomez GA, Morisseau C, Hammock BD, Christianson DW.
  TITLE     Structure of human epoxide hydrolase reveals mechanistic inferences
            on bifunctional catalysis in epoxide and phosphate ester hydrolysis.
  JOURNAL   Biochemistry. 43 (2004) 4716-23.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.76
            ExPASy - ENZYME nomenclature database: 3.1.3.76
            ExplorEnz - The Enzyme Database: 3.1.3.76
            ERGO genome analysis and discovery system: 3.1.3.76
            BRENDA, the Enzyme Database: 3.1.3.76
///
ENTRY       EC 3.1.3.77                 Enzyme
NAME        acireductone synthase;
            E1;
            E-1 enolase-phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-monoester hydrolases
SYSNAME     5-(methylthio)-2,3-dioxopentyl-phosphate phosphohydrolase
            (isomerizing)
REACTION    (1) 5-(methylthio)-2,3-dioxopentyl phosphate + H2O =
            1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate [RN:R07395];
            (2) (1a) 5-(methylthio)-2,3-dioxopentyl phosphate =
            2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate [RN:R07393];
            (3) (1b) 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate + H2O =
            1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate [RN:R07394]
ALL_REAC    R07393 R07394 R07395
SUBSTRATE   5-(methylthio)-2,3-dioxopentyl phosphate [CPD:C15650];
            H2O [CPD:C00001];
            2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate [CPD:C15651]
PRODUCT     1,2-dihydroxy-5-(methylthio)pent-1-en-3-one [CPD:C15606];
            phosphate [CPD:C00009];
            2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate [CPD:C15651]
COMMENT     This bifunctional enzyme first enolizes the substrate to form the
            intermediate 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate,
            which is then dephosphorylated to form the acireductone
            1,2-dihydroxy-5-(methylthio)pent-1-en-3-one [2]. The acireductone
            represents a branch point in the methione-salvage pathway as it is
            used in the formation of formate, CO and 3-(methylthio)propanoate by
            EC 1.13.11.53 [acireductone dioxygenase (Ni2+-requiring)] and of
            formate and 4-methylthio-2-oxobutanoate either by a spontaneous
            reaction under aerobic conditions or by EC 1.13.11.54 {acireductone
            dioxygenase [iron(II)-requiring]} [1,2].
REFERENCE   1  [PMID:8227039]
  AUTHORS   Myers RW, Wray JW, Fish S, Abeles RH.
  TITLE     Purification and characterization of an enzyme involved in oxidative
            carbon-carbon bond cleavage reactions in the methionine salvage
            pathway of Klebsiella pneumoniae.
  JOURNAL   J. Biol. Chem. 268 (1993) 24785-91.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   2  [PMID:7852397]
  AUTHORS   Wray JW, Abeles RH.
  TITLE     The methionine salvage pathway in Klebsiella pneumoniae and rat
            liver. Identification and characterization of two novel
            dioxygenases.
  JOURNAL   J. Biol. Chem. 270 (1995) 3147-53.
  ORGANISM  Klebsiella pneumoniae, rat [GN:rno]
PATHWAY     PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K08965  2,3-diketo-5-methylthiopentyl-1-phosphate enolase
            KO: K08966  2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate
                        phosphatase
            KO: K09880  acireductone synthase
GENES       HSA: 58478(ENOPH1)
            PTR: 461214(ENOPH1)
            MMU: 67870(Enoph1)
            RNO: 305177(RGD1309016)
            CFA: 478452(ENOPH1)
            BTA: 525563(MGC139556)
            GGA: 422600(ENOPH1)
            XTR: 733933(LOC733933)
            DRE: 431773(zgc:91991)
            SPU: 589774(LOC589774)
            ADE: Adeh_0655
            BSU: BG13282(mtnW) BG13283(mtnX)
            BAN: BA4255 BA4256
            BAR: GBAA4255 GBAA4256
            BAA: BA_4714 BA_4715
            BAT: BAS3946 BAS3947
            BCE: BC4036 BC4037
            BCA: BCE_4103 BCE_4104
            BCZ: BCZK3793(rbcL) BCZK3794
            BTK: BT9727_3778(rbcL) BT9727_3779
            BLI: BL03540(mtnW) BL03541
            BLD: BLi01515(ykrW) BLi01516(ykrY)
            GKA: GK0953 GK0954
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.3.77
            ExPASy - ENZYME nomenclature database: 3.1.3.77
            ExplorEnz - The Enzyme Database: 3.1.3.77
            ERGO genome analysis and discovery system: 3.1.3.77
            BRENDA, the Enzyme Database: 3.1.3.77
///
ENTRY       EC 3.1.3.-                  Enzyme
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric monoester hydrolases
REACTION    (1) NADP+ + H2O <=> Orthophosphate + NAD+ [RN:R00118];
            (2) beta-D-Fructose 2-phosphate + H2O <=> D-Fructose +
            Orthophosphate [RN:R00872];
            (3) Thiamin + Orthophosphate <=> Thiamin monophosphate + H2O
            [RN:R02135];
            (4) N-Acetyl-D-mannosamine + Orthophosphate <=>
            N-Acetyl-D-mannosamine 6-phosphate + H2O [RN:R02706];
            (5) Sphinganine 1-phosphate + H2O <=> Sphinganine + Orthophosphate
            [RN:R06520];
            (6) Sphingosine 1-phosphate + H2O <=> Sphingosine + Orthophosphate
            [RN:R06521];
            (7) Ceramide 1-phosphate + H2O <=> N-Acylsphingosine +
            Orthophosphate [RN:R06522];
            (8) 5-Amino-6-(5'-phosphoribitylamino)uracil + H2O <=>
            4-(1-D-Ribitylamino)-5-amino-2,6-dihydroxypyrimidine +
            Orthophosphate [RN:R07280];
            (9) 2-Acyl-1-(1-alkenyl)-sn-glycero-3-phosphate + H2O <=>
            1-Alkenyl-2-acylglycerol + Orthophosphate [RN:R07383];
            (10) L-Galactose 1-phosphate + H2O <=> L-Galactose + Orthophosphate
            [RN:R07674]
SUBSTRATE   NADP+ [CPD:C00006];
            H2O [CPD:C00001];
            beta-D-Fructose 2-phosphate [CPD:C03267];
            Thiamin [CPD:C00378];
            Orthophosphate [CPD:C00009];
            N-Acetyl-D-mannosamine [CPD:C00645];
            Sphinganine 1-phosphate [CPD:C01120];
            Sphingosine 1-phosphate [CPD:C06124];
            Ceramide 1-phosphate [CPD:C02960];
            5-Amino-6-(5'-phosphoribitylamino)uracil [CPD:C04454];
            2-Acyl-1-(1-alkenyl)-sn-glycero-3-phosphate [CPD:C15647]
PRODUCT     Orthophosphate [CPD:C00009];
            NAD+ [CPD:C00003];
            D-Fructose [CPD:C00095];
            Thiamin monophosphate [CPD:C01081];
            H2O [CPD:C00001];
            N-Acetyl-D-mannosamine 6-phosphate [CPD:C04257];
            Sphinganine [CPD:C00836];
            Sphingosine [CPD:C00319];
            N-Acylsphingosine [CPD:C00195];
            4-(1-D-Ribitylamino)-5-amino-2,6-dihydroxypyrimidine [CPD:C04732];
            1-Alkenyl-2-acylglycerol [CPD:C03454]
///
ENTRY       EC 3.1.4.1                  Enzyme
NAME        phosphodiesterase I;
            5'-exonuclease;
            5'-phosphodiesterase;
            5'-nucleotide phosphodiesterase;
            oligonucleate 5'-nucleotidohydrolase;
            5' nucleotide phosphodiesterase/alkaline phosphodiesterase I;
            5'-NPDase;
            5'-PDase;
            5'-PDE;
            5'NPDE;
            alkaline phosphodiesterase;
            nucleotide pyrophosphatase/phosphodiesterase I;
            orthophosphoric diester phosphohydrolase;
            PDE I;
            phosphodiesterase;
            exonuclease I;
            oligonucleate 5'-nucleotidohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     oligonucleotide 5'-nucleotidohydrolase
REACTION    Hydrolytically removes 5'-nucleotides successively from the
            3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides
COMMENT     Hydrolyses both ribonucleotides and deoxyribonucleotides. Has low
            activity towards polynucleotides. A 3'-phosphate terminus on the
            substrate inhibits hydrolysis.
REFERENCE   1
  AUTHORS   Khorana, G.H.
  TITLE     Phosphodiesterases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 5, Academic Press, New York, 1961, p. 79-94.
ORTHOLOGY   KO: K01113  phosphodiesterase/alkaline phosphatase D
GENES       HSA: 5167(ENPP1) 5168(ENPP2) 5169(ENPP3) 55775(TDP1)
            PTR: 453096(TDP1) 463000(ENPP3) 463002(ENPP1) 464353(ENPP2)
            MCC: 705287(ENPP2) 710140(ENPP1) 710232(ENPP3)
            MMU: 104884(Tdp1) 18605(Enpp1) 18606(Enpp2) 209558(Enpp3)
            RNO: 54410(Enpp3) 84050(Enpp2) 85496(Enpp1)
            CFA: 482026(ENPP2) 490828(TDP1)
            GGA: 420361(ENPP2) 423403(TDP1) 426929(ENPP1)
            XLA: 380218(enpp2) 446983(tdp1)
            DME: Dmel_CG8825(gkt)
            ATH: AT5G15170
            PIC: PICST_70997(ENP3)
            ANI: AN5903.2
            AFM: AFUA_5G03120
            XCC: XCC4042
            XCB: XC_4131
            XAC: XAC4166(phoD) XAC4167
            XOO: XOO4554 XOO4555(phoD)
            XOM: XOO_4290(XOO4290) XOO_4291(XOO4291)
            PAE: PA3910
            PST: PSPTO_1010(phoD) PSPTO_4480
            PSB: Psyr_0872 Psyr_4171
            PSP: PSPPH_0910(phoD)
            PFL: PFL_0862
            PFO: Pfl_0796
            PAT: Patl_1106
            CVI: CV_4282(phoD)
            REU: Reut_B5489
            RFR: Rfer_1326
            MPT: Mpe_A3516
            AZO: azo1144(soxZ)
            BBA: Bd2513(phoD)
            MXA: MXAN_1389
            MLO: mll4115
            SME: SMc03243
            CCR: CC_1565
            SIL: SPO0260
            MMR: Mmar10_1878
            HNE: HNE_2455
            ABA: Acid345_1449 Acid345_3950
            BSU: BG11174(phoD)
            BLI: BL01643(phoD) BL05301
            BLD: BLi00281(phoD) BLi03038
            BAY: RBAM_002930
            CNO: NT01CX_0280
            MSM: MSMEG_5508
            CJK: jk0107(phoD) jk1287
            NFA: nfa43870
            RHA: RHA1_ro05554
            SCO: SCO1290(2SCG18.36) SCO2286(SCC75A.32c)
            SMA: SAV5915(phoA) SAV7064(phoD2)
            TFU: Tfu_1673
            FRA: Francci3_1011 Francci3_3820
            FAL: FRAAL6077(phoD)
            SEN: SACE_0052(phoD) SACE_0175(phoD) SACE_1400 SACE_6716(phoD)
                 SACE_6720(phoD)
            RXY: Rxyl_0308
            GVI: gll0490 gll1318 gll2991 glr1198
            ANA: all0207 alr2234(phoD) alr4976
            AVA: Ava_2252 Ava_2698 Ava_4130
            FJO: Fjoh_1841
            PTO: PTO1053 PTO1526
STRUCTURES  PDB: 2OTD  2YS0  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.1
            ExPASy - ENZYME nomenclature database: 3.1.4.1
            ExplorEnz - The Enzyme Database: 3.1.4.1
            ERGO genome analysis and discovery system: 3.1.4.1
            BRENDA, the Enzyme Database: 3.1.4.1
            CAS: 9025-82-5
///
ENTRY       EC 3.1.4.2                  Enzyme
NAME        glycerophosphocholine phosphodiesterase;
            glycerophosphinicocholine diesterase;
            glycerylphosphorylcholinediesterase;
            sn-glycero-3-phosphorylcholine diesterase;
            glycerolphosphorylcholine phosphodiesterase;
            glycerophosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     sn-glycero-3-phosphocholine glycerophosphohydrolase
REACTION    sn-glycero-3-phosphocholine + H2O = choline + sn-glycerol
            3-phosphate [RN:R01030]
ALL_REAC    R01030;
            (other) R01470
SUBSTRATE   sn-glycero-3-phosphocholine [CPD:C00670];
            H2O [CPD:C00001]
PRODUCT     choline [CPD:C00114];
            sn-glycerol 3-phosphate [CPD:C00093]
COMMENT     Also acts on sn-glycero-3-phosphoethanolamine.
REFERENCE   1
  AUTHORS   Dawson, R.M.C.
  TITLE     Liver glycerylphosphorylcholine diesterase.
  JOURNAL   Biochem. J. 62 (1956) 689-693.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:13143024]
  AUTHORS   HAYAISHI O, KORNBERG A.
  TITLE     Metabolism of phospholipides by bacterial enzymes.
  JOURNAL   J. Biol. Chem. 206 (1954) 647-63.
  ORGANISM  Serratia plymuthica
REFERENCE   3
  AUTHORS   Webster, G.R., Marples, E.A. and Thompson, R.H.S.
  TITLE     Glycerylphosphorylcholine diesterase activity in nervous tissue.
  JOURNAL   Biochem. J. 65 (1957) 374-377.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.2
            ExPASy - ENZYME nomenclature database: 3.1.4.2
            ExplorEnz - The Enzyme Database: 3.1.4.2
            ERGO genome analysis and discovery system: 3.1.4.2
            BRENDA, the Enzyme Database: 3.1.4.2
            CAS: 9025-85-8
///
ENTRY       EC 3.1.4.3                  Enzyme
NAME        phospholipase C;
            lipophosphodiesterase I;
            lecithinase C;
            Clostridium welchii alpha-toxin;
            Clostridium oedematiens beta- and gamma-toxins;
            lipophosphodiesterase C;
            phosphatidase C;
            heat-labile hemolysin;
            alpha-toxin
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     phosphatidylcholine cholinephosphohydrolase
REACTION    a phosphatidylcholine + H2O = 1,2-diacylglycerol + choline phosphate
            [RN:R01312]
ALL_REAC    R01312;
            (other) R02027 R02052 R03332 R07381
SUBSTRATE   phosphatidylcholine [CPD:C00157];
            H2O [CPD:C00001]
PRODUCT     1,2-diacylglycerol [CPD:C00641];
            choline phosphate [CPD:C00588]
COFACTOR    Zinc [CPD:C00038]
COMMENT     The bacterial enzyme, which is a zinc protein, also acts on
            sphingomyelin and phosphatidylinositol; that from seminal plasma
            does not act on phosphatidylinositol.
REFERENCE   1
  AUTHORS   Druzhinina, K.V. and Kritzman, M.G.
  TITLE     [Lecithinase from animal tissues.].
  JOURNAL   Biokhimiya 17 (1952) 77-81.
REFERENCE   2  [PMID:807246]
  AUTHORS   Little C, Otnass AB.
  TITLE     The metal ion dependence of phospholipase C from Bacillus cereus.
  JOURNAL   Biochim. Biophys. Acta. 391 (1975) 326-33.
  ORGANISM  Bacillus cereus
REFERENCE   3  [PMID:3086312]
  AUTHORS   Sheikhnejad RG, Srivastava PN.
  TITLE     Isolation and properties of a phosphatidylcholine-specific
            phospholipase C from bull seminal plasma.
  JOURNAL   J. Biol. Chem. 261 (1986) 7544-9.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:4365891]
  AUTHORS   Takahashi T, Sugahara T, Ohsaka A.
  TITLE     Purification of Clostridium perfringens phospholipase C
            (alpha-toxin) by affinity chromatography on agarose-linked egg-yolk
            lipoprotein.
  JOURNAL   Biochim. Biophys. Acta. 351 (1974) 155-71.
  ORGANISM  Clostridium perfringens
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00562  Inositol phosphate metabolism
            PATH: map00564  Glycerophospholipid metabolism
            PATH: map00565  Ether lipid metabolism
ORTHOLOGY   KO: K01114  phospholipase C
GENES       OSA: 4325407
            ANI: AN7691.2 AN8546.2
            AFM: AFUA_1G17590 AFUA_3G01530 AFUA_7G04910
            AOR: AO090005001097 AO090103000073
            PFA: PF10_0132
            TET: TTHERM_00417920 TTHERM_00417930 TTHERM_00417940
                 TTHERM_00467860 TTHERM_02563200
            EHI: 118.t00030
            SPE: Spro_4198
            XCC: XCC0947 XCC3037(plcN)
            XCB: XC_1121 XC_3288
            XCV: XCV1054(phlN1) XCV3291(phlN2)
            XAC: XAC1024 XAC3160(plcN)
            XOO: XOO1651(plcN) XOO3682
            XOM: XOO_3479(XOO3479)
            PAE: PA0844(plcH) PA3319(plcN)
            PAU: PA14_21110(plcN) PA14_53360(plcH)
            PAP: PSPA7_1801 PSPA7_4676
            PFL: PFL_3126(plcB)
            PEN: PSEEN1065
            SAZ: Sama_0115
            ILO: IL2595(plcC)
            FTU: FTT0221(acpA)
            FTF: FTF0221(acpA)
            FTW: FTW_1838
            FTL: FTL_0158
            FTN: FTN_0090
            CVI: CV_0909(plcN)
            RSO: RSc0319(plcN)
            REU: Reut_B4287
            REH: H16_A2724(plcN1) H16_B0534(plcN2) H16_B1067(plcN3)
                 H16_B1166(plcN4)
            RME: Rmet_4192 Rmet_4624
            BMA: BMA0584 BMA0886 BMA1268 BMAA0079 BMAA0968
            BMV: BMASAVP1_1239(plcN) BMASAVP1_A3463(acpA)
            BML: BMA10299_1520 BMA10299_A1655(acpA) BMA10299_A2858
            BMN: BMA10247_1743(plcN-2) BMA10247_A0095(plcN)
            BXE: Bxe_A0663 Bxe_A1415 Bxe_A2871 Bxe_B0211
            BVI: Bcep1808_1084 Bcep1808_3044 Bcep1808_3698 Bcep1808_4878
            BUR: Bcep18194_A4278 Bcep18194_A4545 Bcep18194_A6306
                 Bcep18194_A6500 Bcep18194_B0123 Bcep18194_B0302
                 Bcep18194_B0428 Bcep18194_B1454 Bcep18194_B1519
                 Bcep18194_B1674 Bcep18194_B2801 Bcep18194_C7529
            BCN: Bcen_0687 Bcen_2532 Bcen_3132 Bcen_3906 Bcen_4021 Bcen_5326
            BCH: Bcen2424_1166 Bcen2424_3145 Bcen2424_4345 Bcen2424_4462
                 Bcen2424_5235 Bcen2424_5534
            BAM: Bamb_1045 Bamb_1278 Bamb_3003 Bamb_3198 Bamb_3755 Bamb_4858
            BPS: BPSL0338(plcN2) BPSL1876 BPSL2018 BPSL2403(plcN) BPSS0067
                 BPSS1312
            BPM: BURPS1710b_0549 BURPS1710b_1804 BURPS1710b_1966
                 BURPS1710b_2865(plcN) BURPS1710b_A0331 BURPS1710b_A1577(plcN)
            BPL: BURPS1106A_0372(plcN) BURPS1106A_2804(plcN) BURPS1106A_A0091
            BPD: BURPS668_0358(plcN) BURPS668_2745(plcN) BURPS668_A0114(plcN)
            BTE: BTH_I0317(plcN) BTH_I1762 BTH_I2671(acpA) BTH_II0078
                 BTH_II1106
            BPE: BP2337
            BPA: BPP1702
            BBR: BB3406
            RFR: Rfer_3735 Rfer_3736
            AAV: Aave_0219 Aave_1377
            BRA: BRADO5754(plcN)
            BBT: BBta_1163(plcN) BBta_6264(plcN)
            CCR: CC_3031
            NAR: Saro_1552
            GOX: GOX2176
            ABA: Acid345_0731 Acid345_4181
            SUS: Acid_6235 Acid_7328
            BAN: BA0677(plC)
            BAR: GBAA0677(plC)
            BAA: BA_1264
            BAT: BAS0643
            BCE: BC0670
            BCA: BCE_0744(plc)
            BCZ: BCZK0588(plc)
            BCY: Bcer98_0567
            BTK: BT9727_0587(plc)
            BTL: BALH_0617(plc)
            SAM: MW1940
            SAS: SAS1862(hlb)
            SAC: SACOL2003(hlb)
            SAB: SAB1874
            SAO: SAOUHSC_02240
            SAJ: SaurJH9_2061
            SAH: SaurJH1_2098
            LMO: lmo0205(plcB)
            LMF: LMOf2365_0216(plcB)
            CPE: CPE0036(plc)
            CPF: CPF_0042(plc)
            CPR: CPR_0041(plc)
            CNO: NT01CX_0979
            MTU: Rv1755c(plcD) Rv2349c(plcC) Rv2350c(plcB) Rv2351c(plcA)
            MTC: MT1799 MT2414 MT2415 MT2416
            MBO: Mb1784c(plcD)
            MBB: BCG_1794c(plcD)
            RHA: RHA1_ro02476
            SCO: SCO6691(SC4C6.01)
            SMA: SAV1715(plcA)
            CMI: CMM_0504
            SEN: SACE_5775(plcN)
STRUCTURES  PDB: 1AH7  1CA1  1GYG  1IHJ  1OLP  1P5X  1P6D  1P6E  1QM6  1QMD  
                 2FFZ  2FGN  2HUC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.3
            ExPASy - ENZYME nomenclature database: 3.1.4.3
            ExplorEnz - The Enzyme Database: 3.1.4.3
            ERGO genome analysis and discovery system: 3.1.4.3
            BRENDA, the Enzyme Database: 3.1.4.3
            CAS: 9001-86-9
///
ENTRY       EC 3.1.4.4                  Enzyme
NAME        phospholipase D;
            lipophosphodiesterase II;
            lecithinase D;
            choline phosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     phosphatidylcholine phosphatidohydrolase
REACTION    a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310]
ALL_REAC    R01310;
            (other) R02051 R07385
SUBSTRATE   phosphatidylcholine [CPD:C00157];
            H2O [CPD:C00001]
PRODUCT     choline [CPD:C00114];
            phosphatidate [CPD:C00416]
COFACTOR    Zinc [CPD:C00038]
COMMENT     Also acts on other phosphatidyl esters.
REFERENCE   1  [PMID:4632675]
  AUTHORS   Astrachan L.
  TITLE     The bond hydrolyzed by cardiolipin-specific phospholipase D.
  JOURNAL   Biochim. Biophys. Acta. 296 (1973) 79-88.
  ORGANISM  Hemophilus parainfluenza
REFERENCE   2  [PMID:13539005]
  AUTHORS   EINSET E, CLARK WL.
  TITLE     The enzymatically catalyzed release of choline from lecithin.
  JOURNAL   J. Biol. Chem. 231 (1958) 703-15.
  ORGANISM  rutabaga, Daucus carota, beet, Brassica oleracea, spinach
REFERENCE   3
  AUTHORS   Hanahan, D.J. and Chaikoff, I.L.
  TITLE     On the nature of the phosphorus-containing lipides of cabbage leaves
            and their relation to a phospholipide-splitting enzyme contained in
            these leaves.
  JOURNAL   J. Biol. Chem. 172 (1948) 191-198.
  ORGANISM  Brassica oleracea
REFERENCE   4
  AUTHORS   Tookey, H.L. and Balls, A.K.
  TITLE     Plant phospholipase D. I. Studies on cottonseed and cabbage
            phospholipase D.
  JOURNAL   J. Biol. Chem. 218 (1956) 213-224.
  ORGANISM  Brassica oleracea
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
            PATH: map00565  Ether lipid metabolism
            PATH: map04912  GnRH signaling pathway
ORTHOLOGY   KO: K01115  phospholipase D
GENES       HSA: 5337(PLD1) 5338(PLD2)
            PTR: 454454(PLD2) 470996(PLD1)
            MMU: 18805(Pld1) 18806(Pld2)
            RNO: 25096(Pld1) 25097(Pld2)
            CFA: 479473(PLD2) 488167(PLD1)
            GGA: 424986(PLD1)
            SPU: 579234(LOC579234)
            DME: Dmel_CG12110(Pld)
            CEL: C04G6.3(pld-1)
            ATH: AT1G55180(PLDEPSILON) AT2G42010(PLDBETA1) AT3G05630(PLDP2)
                 AT3G15730(PLDALPHA1) AT4G11840(PLDGAMMA3) AT4G11850(PLDGAMMA1)
                 AT5G25370(PLDALPHA3)
            OSA: 4327647 4331421 4337942 4338532 4341467 4341468 4341469
                 4349161
            SCE: YKR031C(SPO14)
            AGO: AGOS_AFR071W
            PIC: PICST_81277(SPO14)
            CGR: CAGL0L03135g
            SPO: SPAC2F7.16c
            AFM: AFUA_2G16520 AFUA_3G05630
            CNE: CND05920
            DDI: DDB_0231506(pldA)
            TET: TTHERM_00048790 TTHERM_00187130 TTHERM_00827020
            EHI: 145.t00004 350.t00005
            PCR: Pcryo_0797
            PAT: Patl_3732
            REH: H16_B0932 H16_B1107
            BUR: Bcep18194_B2998
            RET: RHE_PF00247(ypf00118)
            RLE: pRL120739
            RSP: RSP_0113
            RDE: RD1_2477(pld)
            SWI: Swit_0142
            RRU: Rru_A0202
            BPU: BPUM_3375(ywjE)
            CTA: CTA_0306
STRUCTURES  PDB: 1F0I  1V0R  1V0S  1V0T  1V0U  1V0V  1V0W  1V0Y  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.4
            ExPASy - ENZYME nomenclature database: 3.1.4.4
            ExplorEnz - The Enzyme Database: 3.1.4.4
            ERGO genome analysis and discovery system: 3.1.4.4
            BRENDA, the Enzyme Database: 3.1.4.4
            CAS: 9001-87-0
///
ENTRY       EC 3.1.4.5        Obsolete  Enzyme
NAME        Transferred to 3.1.21.1
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 3.1.21.1 deoxyribonuclease I (EC 3.1.4.5
            created 1961, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.5
            ExPASy - ENZYME nomenclature database: 3.1.4.5
            ExplorEnz - The Enzyme Database: 3.1.4.5
            ERGO genome analysis and discovery system: 3.1.4.5
            BRENDA, the Enzyme Database: 3.1.4.5
///
ENTRY       EC 3.1.4.6        Obsolete  Enzyme
NAME        Transferred to 3.1.22.1
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 3.1.22.1 deoxyribonuclease II (EC 3.1.4.6
            created 1961, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.6
            ExPASy - ENZYME nomenclature database: 3.1.4.6
            ExplorEnz - The Enzyme Database: 3.1.4.6
            ERGO genome analysis and discovery system: 3.1.4.6
            BRENDA, the Enzyme Database: 3.1.4.6
///
ENTRY       EC 3.1.4.7        Obsolete  Enzyme
NAME        Transferred to 3.1.31.1
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 3.1.31.1 micrococcal nuclease (EC 3.1.4.7
            created 1961, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.7
            ExPASy - ENZYME nomenclature database: 3.1.4.7
            ExplorEnz - The Enzyme Database: 3.1.4.7
            ERGO genome analysis and discovery system: 3.1.4.7
            BRENDA, the Enzyme Database: 3.1.4.7
///
ENTRY       EC 3.1.4.8        Obsolete  Enzyme
NAME        Transferred to 3.1.27.3
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 3.1.27.3 ribonuclease T1 (EC 3.1.4.8
            created 1961, transferred 1965 to EC 2.7.7.26, reinstated 1972,
            deleted 1978)
STRUCTURES  PDB: 1PY3  1PYL  1SAR  2SAR  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.8
            ExPASy - ENZYME nomenclature database: 3.1.4.8
            ExplorEnz - The Enzyme Database: 3.1.4.8
            ERGO genome analysis and discovery system: 3.1.4.8
            BRENDA, the Enzyme Database: 3.1.4.8
///
ENTRY       EC 3.1.4.9        Obsolete  Enzyme
NAME        Transferred to 3.1.30.2
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 3.1.30.2 Serratia marcescens nuclease (EC
            3.1.4.9 created 1965, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.9
            ExPASy - ENZYME nomenclature database: 3.1.4.9
            ExplorEnz - The Enzyme Database: 3.1.4.9
            ERGO genome analysis and discovery system: 3.1.4.9
            BRENDA, the Enzyme Database: 3.1.4.9
///
ENTRY       EC 3.1.4.10       Obsolete  Enzyme
NAME        Transferred to 4.6.1.13
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 4.6.1.13 phosphatidylinositol
            diacylglycerol-lyase. As there is no hydrolysis of the inositol
            1,2-cyclic phosphate formed, previous classification of the enzyme
            as a hydrolase was incorrect. (EC 3.1.4.10 created 1972, modified
            1976, deleted 2002)
STRUCTURES  PDB: 1AOD  1GYM  1PTD  1PTG  2PLC  2PTD  3PTD  4PTD  5PTD  6PTD  
                 7PTD  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.10
            ExPASy - ENZYME nomenclature database: 3.1.4.10
            ExplorEnz - The Enzyme Database: 3.1.4.10
            ERGO genome analysis and discovery system: 3.1.4.10
            BRENDA, the Enzyme Database: 3.1.4.10
///
ENTRY       EC 3.1.4.11                 Enzyme
NAME        phosphoinositide phospholipase C;
            triphosphoinositide phosphodiesterase;
            phosphoinositidase C;
            1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase;
            monophosphatidylinositol phosphodiesterase;
            phosphatidylinositol phospholipase C;
            PI-PLC;
            1-phosphatidyl-D-myo-inositol-4,5-bisphosphate
            inositoltrisphosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate
            inositoltrisphosphohydrolase
REACTION    1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O =
            1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
ALL_REAC    (other) R03435
SUBSTRATE   1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [CPD:C04637];
            H2O [CPD:C00001]
PRODUCT     1D-myo-inositol 1,4,5-trisphosphate [CPD:C01245];
            diacylglycerol [CPD:C00165]
COMMENT     These enzymes form some of the cyclic phosphate
            Ins(cyclic1,2)P(4,5)P2 as well as Ins(1,4,5)P3. They show activity
            towards phosphatidylinositol, i.e., the activity of EC 4.6.1.13,
            phosphatidylinositol diacylglycerol-lyase, in vitro at high [Ca2+].
            Four beta-isoforms regulated by G-proteins, two gamma-forms
            regulated by tyrosine kinases, four delta-forms regulated at least
            in part by calcium and an epsilon-form, probably regulated by the
            oncogene ras, have been found.
REFERENCE   1  [PMID:6275838]
  AUTHORS   Downes CP, Michell RH.
  TITLE     The polyphosphoinositide phosphodiesterase of erythrocyte membranes.
  JOURNAL   Biochem. J. 198 (1981) 133-40.
  ORGANISM  human [GN:hsa], rabbit, rat [GN:rno]
REFERENCE   2
  AUTHORS   Thompson, W. and Dawson, R.M.C.
  TITLE     The triphosphoinositide phosphodiesterase of brain tissue.
  JOURNAL   Biochem. J. 91 (1964) 237-243.
REFERENCE   3  [PMID:9182519]
  AUTHORS   Rhee SG, Bae YS.
  TITLE     Regulation of phosphoinositide-specific phospholipase C isozymes.
  JOURNAL   J. Biol. Chem. 272 (1997) 15045-8.
  ORGANISM  mammalian
PATHWAY     PATH: map00562  Inositol phosphate metabolism
            PATH: map04012  ErbB signaling pathway
            PATH: map04020  Calcium signaling pathway
            PATH: map04070  Phosphatidylinositol signaling system
            PATH: map04310  Wnt signaling pathway
            PATH: map04370  VEGF signaling pathway
            PATH: map04540  Gap junction
            PATH: map04650  Natural killer cell mediated cytotoxicity
            PATH: map04664  Fc epsilon RI signaling pathway
            PATH: map04670  Leukocyte transendothelial migration
            PATH: map04720  Long-term potentiation
            PATH: map04730  Long-term depression
            PATH: map04912  GnRH signaling pathway
            PATH: map04916  Melanogenesis
            PATH: map05120  Epithelial cell signaling in Helicobacter pylori
                            infection
            PATH: map05214  Glioma
            PATH: map05223  Non-small cell lung cancer
ORTHOLOGY   KO: K01116  1-phosphatidylinositol-4,5-bisphosphate
                        phosphodiesterase
            KO: K05857  phospholipase C, delta
            KO: K05858  phospholipase C, beta
            KO: K05859  phospholipase C, gamma
GENES       HSA: 113026(PLCD3) 23236(PLCB1) 5330(PLCB2) 5331(PLCB3)
                 5332(PLCB4) 5333(PLCD1) 5335(PLCG1) 5336(PLCG2) 84812(PLCD4)
            PTR: 453330(PLCB2) 468279(PLCD3) 470647(PLCD4)
            MMU: 18795(Plcb1) 18797(Plcb3) 18798(Plcb4) 18799(Plcd1)
                 18802(Plcd4) 18803(Plcg1) 234779(Plcg2) 72469(Plcd3)
            RNO: 140693(Plcd4) 24654(Plcb1) 24655(Plcd1) 25031(Plcb4)
                 25738(Plcg1) 287745(Plcd3_predicted) 29322(Plcb3) 29337(Plcg2)
                 85240(Plcb2)
            CFA: 476034(PLCB3) 477160(PLCB4) 478910(PLCD4) 485586(PLCD1)
                 485773(PLCB1) 485874(PLCG1) 487491(PLCB2) 489692(PLCG2)
                 490929(PLCD3)
            BTA: 281985(PLCB4) 281986(PLCD1) 281987(PLCG1) 287026(PLCB1)
            SSC: 397119(PLCD4)
            GGA: 415805(PLCG2) 416730(PLCB4) 420416(PLCD1) 423014(PLCB2)
                 427687(PLCB1)
            XLA: 398359(LOC398359) 398360(LOC398360)
            DRE: 337489(zgc:55868) 373867(plcg1)
            SPU: 494023(PLCd) 579102(LOC579102) 587412(LOC587412)
            DME: Dmel_CG4200(sl) Dmel_CG4574(Plc21C)
            CEL: B0348.4(egl-8) R05G6.8(phospholipase) T01E8.3(plc-3)
            OSA: 4332497 4337686
            SCE: YPL268W(PLC1)
            AGO: AGOS_ACR024W
            PIC: PICST_42966(PLC1)
            CGR: CAGL0A01177g
            SPO: SPAC22F8.11(plc1)
            ANI: AN0664.2
            AFM: AFUA_1G13250
            AOR: AO090012000557
            CNE: CNC04820
            DDI: DDB_0201656(pipA)
            PFA: PF10_0132
            CPV: cgd4_2560
            CHO: Chro.40288
            TAN: TA06965
            TET: TTHERM_00085110
            TBR: Tb11.02.3780
            LMA: LmjF30.2950
STRUCTURES  PDB: 1DJG  1DJH  1DJI  1DJW  1DJX  1DJY  1DJZ  1HSQ  1JAD  1MAI  
                 1QAS  1QAT  1Y0M  1YWO  1YWP  2C5L  2FCI  2FJL  2FJU  2HSP  
                 2ISD  2PLD  2PLE  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.11
            ExPASy - ENZYME nomenclature database: 3.1.4.11
            ExplorEnz - The Enzyme Database: 3.1.4.11
            ERGO genome analysis and discovery system: 3.1.4.11
            BRENDA, the Enzyme Database: 3.1.4.11
            CAS: 37213-51-7
///
ENTRY       EC 3.1.4.12                 Enzyme
NAME        sphingomyelin phosphodiesterase;
            neutral sphingomyelinase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     sphingomyelin cholinephosphohydrolase
REACTION    sphingomyelin + H2O = N-acylsphingosine + choline phosphate
            [RN:R02541]
ALL_REAC    R02541
SUBSTRATE   sphingomyelin [CPD:C00550];
            H2O [CPD:C00001]
PRODUCT     N-acylsphingosine [CPD:C00195];
            choline phosphate [CPD:C00588]
COMMENT     Has very little activity on phosphatidylcholine.
REFERENCE   1  [PMID:5916388]
  AUTHORS   Barnholz Y, Roitman A, Gatt S.
  TITLE     Enzymatic hydrolysis of sphingolipids. II. Hydrolysis of
            sphingomyelin by an enzyme from rat brain.
  JOURNAL   J. Biol. Chem. 241 (1966) 3731-7.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:2545711]
  AUTHORS   Chatterjee S, Ghosh N.
  TITLE     Neutral sphingomyelinase from human urine. Purification and
            preparation of monospecific antibodies.
  JOURNAL   J. Biol. Chem. 264 (1989) 12554-61.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:5911524]
  AUTHORS   Heller M, Shapiro B.
  TITLE     Enzymic hydrolysis of sphingomyelin by rat liver.
  JOURNAL   Biochem. J. 98 (1966) 763-9.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:5933867]
  AUTHORS   Kanfer JN, Young OM, Shapiro D, Brady RO.
  TITLE     The metabolism of sphingomyelin. I. Purification and properties of a
            sphingomyelin-cleaving enzyme from rat liver tissue.
  JOURNAL   J. Biol. Chem. 241 (1966) 1081-4.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00600  Sphingolipid metabolism
ORTHOLOGY   KO: K01117  sphingomyelin phosphodiesterase
GENES       HSA: 339221(ENPP7) 55512(SMPD3) 55627(SMPD4) 6609(SMPD1)
                 6610(SMPD2)
            PTR: 450990(SMPD1) 462928(SMPD2)
            MMU: 20597(Smpd1) 20598(Smpd2) 238011(Enpp7) 58994(Smpd3)
                 77626(Smpd4)
            RNO: 83537(Smpd2) 94338(Smpd3)
            CFA: 481957(SMPD2) 485334(SMPD1) 489743(SMPD3)
            GGA: 415619(SMPD3) 416942(SMPD4) 426249(ENPP7) 770663(SMPD2)
            XLA: 495009(LOC495009)
            DRE: 406664(smpd4)
            SPU: 576943(LOC576943)
            DME: Dmel_CG12034
            CEL: B0252.2(asm-1) T27F6.6 W03G1.7(asm-3) ZK455.4(asm-2)
            PIC: PICST_51970(IFP3)
            SPO: SPBC685.10c
            AFM: AFUA_4G06640
            AOR: AO090023000919
            DDI: DDB_0232049(sgmB)
            TAN: TA09680
            TPV: TP01_1199
            TET: TTHERM_01054320
            EHI: 18.t00042 29.t00040 427.t00005 43.t00036 539.t00001 99.t00001
            BAN: BA0678(spH)
            BAR: GBAA0678(spH)
            BAT: BAS0644
            BCE: BC0671
            BCA: BCE_0745(sph)
            BCZ: BCZK0589(sph)
            BCY: Bcer98_0568
            BTK: BT9727_0588(sph)
            BTL: BALH_0618(sph)
            STP: Strop_2045
            LIL: LA1027(sph1) LA1029(sph2) LA3540(sphH) LA4004(sph3)
            LIC: LIC12631 LIC12632 LIC13198
            LBJ: LBJ_0291
            LBL: LBL_2785
STRUCTURES  PDB: 1ZWX  2DDR  2DDS  2DDT  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.12
            ExPASy - ENZYME nomenclature database: 3.1.4.12
            ExplorEnz - The Enzyme Database: 3.1.4.12
            ERGO genome analysis and discovery system: 3.1.4.12
            BRENDA, the Enzyme Database: 3.1.4.12
            CAS: 9031-54-3
///
ENTRY       EC 3.1.4.13                 Enzyme
NAME        serine-ethanolaminephosphate phosphodiesterase;
            serine ethanolamine phosphodiester phosphodiesterase;
            SEP diesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     serine-phosphoethanolamine ethanolaminephosphohydrolase
REACTION    serine phosphoethanolamine + H2O = serine + ethanolamine phosphate
            [RN:R02817]
ALL_REAC    R02817
SUBSTRATE   serine phosphoethanolamine [CPD:C03872];
            H2O [CPD:C00001]
PRODUCT     serine [CPD:C00716];
            ethanolamine phosphate [CPD:C00346]
COMMENT     Acts only on those phosphodiesters that have ethanolamine as a
            component part of the molecule.
REFERENCE   1  [PMID:14284710]
  AUTHORS   HAGERMAN DD, ROSENBERG H, ENNOR AH, SCHIFF P, INOUE S.
  TITLE     THE ISOLATION AND PROPERTIES OF CHICKEN KIDNEY SERINE ETHANOLAMINE
            PHOSPHATE PHOSPHODIESTERASE.
  JOURNAL   J. Biol. Chem. 240 (1965) 1108-12.
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K05980  serine-ethanolaminephosphate phosphodiesterase
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.13
            ExPASy - ENZYME nomenclature database: 3.1.4.13
            ExplorEnz - The Enzyme Database: 3.1.4.13
            ERGO genome analysis and discovery system: 3.1.4.13
            BRENDA, the Enzyme Database: 3.1.4.13
            CAS: 37288-20-3
///
ENTRY       EC 3.1.4.14                 Enzyme
NAME        [acyl-carrier-protein] phosphodiesterase;
            ACP hydrolyase;
            ACP phosphodiesterase;
            AcpH;
            [acyl-carrier-protein] 4'-pantetheine-phosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     holo-[acyl-carrier-protein] 4'-pantetheine-phosphohydrolase
REACTION    holo-[acyl-carrier-protein] + H2O = 4'-phosphopantetheine +
            apo-[acyl-carrier-protein] [RN:R01623]
ALL_REAC    R01623
SUBSTRATE   holo-[acyl-carrier-protein];
            H2O [CPD:C00001]
PRODUCT     4'-phosphopantetheine [CPD:C01134];
            apo-[acyl-carrier-protein] [CPD:C03688]
COMMENT     The enzyme cleaves acyl-[acyl-carrier-protein] species with acyl
            chains of 6-16 carbon atoms although it appears to demonstrate a
            preference for the unacylated acyl-carrier-protein (ACP) and
            short-chain ACPs over the medium- and long-chain species [3].
            Deletion of the gene encoding this enzyme abolishes ACP
            prosthetic-group turnover in vivo [3]. Activation of apo-ACP to form
            the holoenzyme is carried out by EC 2.7.8.7,
            holo-[acyl-carrier-protein] synthase.
REFERENCE   1  [PMID:224058]
  AUTHORS   Sobhy C.
  TITLE     Regulation of fatty acid synthetase activity. The
            4'-phosphopantetheine hydrolase of rat liver.
  JOURNAL   J. Biol. Chem. 254 (1979) 8561-6.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4290442]
  AUTHORS   Vagelos PR, Larrabes AR.
  TITLE     Acyl carrier protein. IX. Acyl carrier protein hydrolase.
  JOURNAL   J. Biol. Chem. 242 (1967) 1776-81.
  ORGANISM  Escherichia coli [GN:eco], Clostridium bufyricum
REFERENCE   3  [PMID:16107329]
  AUTHORS   Thomas J, Cronan JE.
  TITLE     The enigmatic acyl carrier protein phosphodiesterase of Escherichia
            coli: genetic and enzymological characterization.
  JOURNAL   J. Biol. Chem. 280 (2005) 34675-83.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K08682  acyl carrier protein phosphodiesterase
GENES       ECO: b0404(yajB)
            ECJ: JW0394(yajB)
            ECE: Z0503(yajB)
            ECS: ECs0455
            ECC: c0514(yajB)
            ECI: UTI89_C0426(yajB)
            ECP: ECP_0463
            ECV: APECO1_1606(yajB)
            ECW: EcE24377A_0434(acpH)
            ECX: EcHS_A0474
            STY: STY0441(yajB)
            STT: t2460(yajB)
            SPT: SPA2320(yajB)
            SEC: SC0445(yajB)
            STM: STM0403(yajB)
            YPE: YPO3193
            YPK: y0989
            YPM: YP_0738
            YPA: YPA_2688
            YPP: YPDSF_0823
            YPS: YPTB0926(yajB)
            YPI: YpsIP31758_1814(azoR) YpsIP31758_3125(acpH)
            SFL: SF0341(yajB)
            SSN: SSON_0381(yajB)
            SBO: SBO_0298(yajB)
            SDY: SDY_0330(yajB)
            ECA: ECA1118
            PLU: plu3906
            SGL: SG0644
            ENT: Ent638_0387 Ent638_1947
            SPE: Spro_1059
            SAZ: Sama_3398
            SBL: Sbal_0320 Sbal_4073
            SLO: Shew_3529
            SPC: Sputcn32_0423
            SHE: Shewmr4_0321
            SHM: Shewmr7_3703
            SHN: Shewana3_0316
            SHW: Sputw3181_0277
            PIN: Ping_1242
            AEH: Mlg_2463
            ABO: ABO_0027(acpD)
            AHA: AHA_3576
            REH: H16_A1577
            BML: BMA10299_0946(acpD)
            BVI: Bcep1808_0505 Bcep1808_5861
            BCH: Bcen2424_0528 Bcen2424_3293 Bcen2424_5994 Bcen2424_6039
                 Bcen2424_6319
            BAM: Bamb_0433
            PNA: Pnap_1540
            AAV: Aave_0699 Aave_2541
            AJS: Ajs_2340
            HAR: HEAR0564
            MMS: mma_0547 mma_0969 mma_1228 mma_1884
            AZO: azo3370(acpD)
            DVL: Dvul_0699
            RLE: RL1959(acpD)
            BRA: BRADO4768 BRADO6190
            BBT: BBta_2663(azoR) BBta_4802
            RSH: Rsph17029_3461
            PDE: Pden_4165
            BPU: BPUM_0385 BPUM_2922
            LLM: llmg_0397 llmg_0431
            MSM: MSMEG_3381
            FAL: FRAAL2435
STRUCTURES  PDB: 1T5B  1TIK  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.14
            ExPASy - ENZYME nomenclature database: 3.1.4.14
            ExplorEnz - The Enzyme Database: 3.1.4.14
            ERGO genome analysis and discovery system: 3.1.4.14
            BRENDA, the Enzyme Database: 3.1.4.14
            CAS: 37288-21-4
///
ENTRY       EC 3.1.4.15                 Enzyme
NAME        adenylyl-[glutamate---ammonia ligase] hydrolase;
            adenylyl-[glutamine-synthetase]hydrolase;
            adenylyl(glutamine synthetase) hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     adenylyl-[L-glutamate:ammonia ligase (ADP-forming)]
            adenylylhydrolase
REACTION    adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O =
            adenylate + [L-glutamate:ammonia ligase (ADP-forming)] [RN:R03474]
ALL_REAC    R03474
SUBSTRATE   adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] [CPD:C01299];
            H2O [CPD:C00001]
PRODUCT     adenylate [CPD:C00020];
            [L-glutamate:ammonia ligase (ADP-forming)] [CPD:C01281]
REFERENCE   1
  AUTHORS   Heilmeyer, L., Battig, F. and Holzer, H.
  TITLE     Characterization of a glutamine synthetase b activating
            (deadenylylating) enzyme system in Escherichia coli.
  JOURNAL   Eur. J. Biochem. 9 (1968) 259-262.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4893578]
  AUTHORS   Shapiro BM.
  TITLE     The glutamine synthetase deadenylylating enzyme system from
            Escherichia coli. Resolution into two components, specific
            nucleotide stimulation, and cofactor requirements.
  JOURNAL   Biochemistry. 8 (1969) 659-70.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4298074]
  AUTHORS   Shapiro BM, Stadtman ER.
  TITLE     5'-adenylyl-O-tyrosine. The novel phosphodiester residue of
            adenylylated glutamine synthetase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 243 (1968) 3769-71.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.15
            ExPASy - ENZYME nomenclature database: 3.1.4.15
            ExplorEnz - The Enzyme Database: 3.1.4.15
            ERGO genome analysis and discovery system: 3.1.4.15
            BRENDA, the Enzyme Database: 3.1.4.15
            CAS: 37288-22-5
///
ENTRY       EC 3.1.4.16                 Enzyme
NAME        2',3'-cyclic-nucleotide 2'-phosphodiesterase;
            ribonucleoside 2',3'-cyclic phosphate diesterase;
            2',3 '-cyclic AMP phosphodiesterase;
            2',3'-cyclic nucleotidase;
            cyclic 2',3'-nucleotide 2'-phosphodiesterase;
            cyclic 2',3'-nucleotide phosphodiesterase;
            2',3'-cyclic nucleoside monophosphate phosphodiesterase;
            2',3'-cyclic AMP 2'-phosphohydrolase;
            cyclic phosphodiesterase:3'-nucleotidase;
            2',3'-cyclic nucleotide phosphohydrolase;
            2':3'-cyclic phosphodiesterase;
            2':3'-cyclic nucleotide phosphodiesterase:3'-nucleotidase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     nucleoside-2',3'-cyclic-phosphate 3'-nucleotidohydrolase
REACTION    nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 3'-phosphate
            [RN:R03423]
ALL_REAC    R03423 > R03537 R03538 R03929 R05135
SUBSTRATE   nucleoside 2',3'-cyclic phosphate [CPD:C01240];
            H2O [CPD:C00001]
PRODUCT     nucleoside 3'-phosphate [CPD:C03419]
COMMENT     Also hydrolyses 3'-nucleoside monophosphates and bis-4-nitrophenyl
            phosphate, but not 3'-deoxynucleotides. Similar reactions are
            carried out by EC 3.1.27.3 (ribonuclease T1) and EC 3.1.27.5
            (pancreatic ribonuclease).
REFERENCE   1  [PMID:14245396]
  AUTHORS   ANRAKU Y.
  TITLE     A NEW CYCLIC PHOSPHODIESTERASE HAVING A 3'-NUCLEOTIDASE ACTIVITY
            FROM ESCHERICHIA COLI B. I. PURIFICATION AND SOME PROPERTIES OF THE
            ENZYME.
  JOURNAL   J. Biol. Chem. 239 (1964) 3412-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:14245397]
  AUTHORS   ANRAKU Y.
  TITLE     A NEW CYCLIC PHOSPHODIESTERASE HAVING A 3'-NUCLEOTIDASE ACTIVITY
            FROM ESCHERICHIA COLI B. II. FURTHER STUDIES ON SUBSTRATE
            SPECIFICITY AND MODE OF ACTION OF THE ENZYME.
  JOURNAL   J. Biol. Chem. 239 (1964) 3420-4.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4295113]
  AUTHORS   Center MS, Behal FJ.
  TITLE     A cyclic phosphodiesterase with 3'-nucleotidase activity from
            Proteus mirabilis.
  JOURNAL   J. Biol. Chem. 243 (1968) 138-43.
  ORGANISM  Proteus mirabilis
REFERENCE   4  [PMID:4310670]
  AUTHORS   Olafson RW, Drummond GI, Lee JF.
  TITLE     Studies on 2',3'-cyclic nucleotide-3'-phosphohydrolase from brain.
  JOURNAL   Can. J. Biochem. 47 (1969) 961-6.
REFERENCE   5  [PMID:4303200]
  AUTHORS   Unemoto T, Hayashi M.
  TITLE     Chloride ion as a modifier of 2',3'-cyclic phosphodiesterase
            purified from halophilic Vibrio alginolyticus.
  JOURNAL   Biochim. Biophys. Acta. 171 (1969) 89-102.
  ORGANISM  Vibrio alginolyticus
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K01119  2',3'-cyclic-nucleotide 2'-phosphodiesterase
GENES       ECO: b4213(cpdB)
            ECJ: JW4171(cpdB)
            ECE: Z5824(cpdB)
            ECS: ECs5191
            ECC: c5312
            ECI: UTI89_C4822(cpdB)
            ECP: ECP_4467
            ECV: APECO1_2173(cpdB)
            ECW: EcE24377A_4783(cpdB)
            ECX: EcHS_A4467(cpdB)
            STY: STY4761(cpdB)
            STT: t4456(cpdB)
            SPT: SPA4222(cpdB)
            SEC: SC4278(cpdB)
            STM: STM4403(cpdB)
            YPE: YPO3530(cpdB)
            YPK: y0653(cpdB)
            YPM: YP_0553(cpdB)
            YPA: YPA_0080
            YPN: YPN_3274
            YPS: YPTB0446(cpdB)
            YPI: YpsIP31758_3631(cpdB)
            SFL: SF4273(cpdB)
            SFX: S4538(cpdB)
            SFV: SFV_4274(cpdB)
            SSN: SSON_4398(cpdB)
            SBO: SBO_4230(cpdB)
            SDY: SDY_4383(cpdB)
            ECA: ECA0053 ECA3602(cpdB)
            PLU: plu3927(cpdB)
            HIT: NTHI0741(cpdB)
            HIP: CGSHiEE_00045(cpdB)
            HIQ: CGSHiGG_06380(cpdB)
            PMU: PM2014(cpdB)
            MSU: MS0064(ushA)
            APL: APL_0646(cpdB)
            VCH: VC2416 VC2562
            VCO: VC0395_A2139(cpdB)
            VVU: VV1_0728 VV1_2771
            VVY: VV0409
            VPA: VP0290
            VFI: VF0319(cpdB) VF1511
            PPR: PBPRA3313 PBPRB1234(cpdC)
            SON: SO_3565(cpdB)
            SDN: Sden_1596
            SHE: Shewmr4_1524
            SHM: Shewmr7_1591
            SHN: Shewana3_1585
            SDE: Sde_0780
            ABO: ABO_2701(ushA)
            AHA: AHA_0559
            CVI: CV_0292(cpdB)
            RSO: RSc3363(cpdB)
            RME: Rmet_0572
            BMA: BMA0067(cpdB)
            BMV: BMASAVP1_A0233(cpdB)
            BML: BMA10299_A1360(cpdB)
            BMN: BMA10247_3202(cpdB)
            BUR: Bcep18194_A6244
            BAM: Bamb_2951
            BPS: BPSL0400(cpdB)
            BPM: BURPS1710b_0611(cpdB)
            BTE: BTH_I0372
            HPY: HP0104(cpdB)
            HPA: HPAG1_0104
            HAC: Hac_0790(cpdB)
            MXA: MXAN_6266
            MLO: mlr0366
            SME: SMc04449(cpdB)
            ATU: Atu1210(cpdB)
            ATC: AGR_C_2233
            RET: RHE_CH01766(cpdB)
            RLE: RL1961(cpdB)
            SIL: SPO3542
            SIT: TM1040_1036
            RSP: RSP_0709(cpdB)
            RDE: RD1_1258(cpdB)
            SUS: Acid_1294
            BSU: BG12930(yfkN)
            BAN: BA4346(cpdB)
            BAR: GBAA4346(cpdB)
            BAA: BA_4803
            BAT: BAS4031
            BCE: BC3687
            BCA: BCE_3724 BCE_4194(cpdB)
            BCZ: BCZK2261(cpdC)
            BTK: BT9727_2304(cpdC) BT9727_3442(cpdC) BT9727_3864(ushA)
            BTL: BALH_2267(cpdC) BALH_3325(cpdC)
            BLI: BL03110
            BLD: BLi00814(yfkN)
            BPU: BPUM_0732(yfkN)
            GKA: GK3182(yfkN)
            SAB: SAB0086(cpdB)
            SAA: SAUSA300_0147
            LLC: LACR_0338
            LLM: llmg_0316(cpdC)
            SAG: SAG1941(cpdB)
            SAN: gbs1929
            SAK: SAK_1901(cpdB)
            STC: str0139 str0140 str0141 str0142
            STL: stu0139 stu0140 stu0141 stu0142
            SSA: SSA_0243
            LBR: LVIS_2142
            LCA: LSEI_1360
            CAC: CAC0353
            CPE: CPE2162(cpdC)
            CTC: CTC01995
            CNO: NT01CX_0213
            CHY: CHY_2488
            TTE: TTE0343(ushA)
            MMO: MMOB0990(ushA)
            SCO: SCO2015(SC7H2.29)
            SMA: SAV6215(cpdB)
            PAC: PPA1871
            KRA: Krad_4241
            TDE: TDE0870
            CYA: CYA_0972
            CYB: CYB_2932
            BTH: BT_1236
            BFR: BF1808
            BFS: BF1873
            PGI: PG0171
            DRA: DR_1736
            DGE: Dgeo_0627
            HMA: rrnAC0282(cpdB3) rrnAC0894(cpdB2)
            HWA: HQ2723A(ushA)
            NPH: NP1854A(ushA_1) NP2590A(ushA_2)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.16
            ExPASy - ENZYME nomenclature database: 3.1.4.16
            ExplorEnz - The Enzyme Database: 3.1.4.16
            ERGO genome analysis and discovery system: 3.1.4.16
            BRENDA, the Enzyme Database: 3.1.4.16
            CAS: 9037-18-7
///
ENTRY       EC 3.1.4.17                 Enzyme
NAME        3',5'-cyclic-nucleotide phosphodiesterase;
            cyclic 3',5'-mononucleotide phosphodiesterase;
            PDE;
            cyclic 3',5'-nucleotide phosphodiesterase;
            cyclic 3',5'-phosphodiesterase;
            3',5'-nucleotide phosphodiesterase;
            3':5'-cyclic nucleotide 5'-nucleotidohydrolase;
            3',5'-cyclonucleotide phosphodiesterase;
            cyclic nucleotide phosphodiesterase;
            3', 5'-cyclic nucleoside monophosphate phosphodiesterase;
            3': 5'-monophosphate phosphodiesterase (cyclic CMP);
            cytidine 3':5'-monophosphate phosphodiesterase (cyclic CMP);
            cyclic 3',5-nucleotide monophosphate phosphodiesterase;
            nucleoside 3',5'-cyclic phosphate diesterase;
            nucleoside-3',5-monophosphate phosphodiesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     3',5'-cyclic-nucleotide 5'-nucleotidohydrolase
REACTION    nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
            [RN:R03259]
ALL_REAC    R03259 > R00191 R01234
SUBSTRATE   nucleoside 3',5'-cyclic phosphate [CPD:C04212];
            H2O [CPD:C00001]
PRODUCT     nucleoside 5'-phosphate [CPD:C01117]
COMMENT     Acts on 3',5'-cyclic AMP, 3',5'-cyclic dAMP, 3',5'-cyclic IMP,
            3',5'-cyclic GMP and 3',5'-cyclic CMP.
REFERENCE   1  [PMID:4365506]
  AUTHORS   Fischer U, Amrhein N.
  TITLE     Cyclic nucleotide phosphodiesterase of Chlamydomonas reinhardtii.
  JOURNAL   Biochim. Biophys. Acta. 341 (1974) 412-20.
  ORGANISM  Chlamydomonas reinhardtii
REFERENCE   2  [PMID:4287216]
  AUTHORS   Nair KG.
  TITLE     Purification and properties of 3',5'-cyclic nucleotide
            phosphodiesterase from dog heart.
  JOURNAL   Biochemistry. 5 (1966) 150-7.
  ORGANISM  dog [GN:cfa]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map04914  Progesterone-mediated oocyte maturation
ORTHOLOGY   KO: K01120  3',5'-cyclic-nucleotide phosphodiesterase
GENES       HSA: 10846(PDE10A) 27115(PDE7B) 50940(PDE11A) 5136(PDE1A)
                 5137(PDE1C) 5138(PDE2A) 5140(PDE3B) 5141(PDE4A) 5142(PDE4B)
                 5143(PDE4C) 5144(PDE4D) 5147(PDE6D) 5148(PDE6G) 5149(PDE6H)
                 5150(PDE7A) 5151(PDE8A) 5152(PDE9A) 8622(PDE8B) 8654(PDE5A)
            PTR: 461796(PDE8B) 461860(PDE4D) 463123(PDE10A) 464213(PDE7A)
            MMU: 18573(Pde1a) 18574(Pde1b) 18575(Pde1c) 18576(Pde3b)
                 18577(Pde4a) 18578(Pde4b) 18582(Pde6d) 18583(Pde7a)
                 18584(Pde8a) 18585(Pde9a) 18588(Pde6g) 207728(Pde2a)
                 218461(Pde8b) 238871(Pde4d) 23984(Pde10a) 242202(Pde5a)
                 29863(Pde7b) 54611(Pde3a) 78600(Pde6h)
            RNO: 114248(Pde6h) 171115(Pde5a) 191569(Pde9a) 24626(Pde4b)
                 24627(Pde4d) 25638(Pde4a) 29516(Pde3b) 29691(Pde1b)
                 308776(Pde8a) 309962(Pde8b) 363272(Pde6d_predicted)
                 50678(Pde3a) 63885(Pde10a) 81529(Pde1a) 81742(Pde1c)
                 81743(Pde2a)
            CFA: 403652(PDE1A) 403781(PDE6D) 403825(PDE5A) 403911(PDE6G)
                 475272(PDE1C) 479540(PDE4B) 483996(PDE7B) 484073(PDE10A)
                 486975(PDE7A) 487221(PDE4D) 488752(PDE8A) 488939(PDE8B)
                 609574(PDE2A) 609938(PDE4C) 611022(PDE9A) 611031(PDE6H)
                 611730(PDE3B)
            BTA: 281969(PDE1A) 281970(PDE1B) 281971(PDE2A) 281972(PDE5A)
                 281976(PDE6D) 281977(PDE6G) 281978(PDE6H)
            SSC: 396555(PDE3A)
            GGA: 378929(PDE6H) 395091(PDE6G) 415455(PDE8A) 418185(PDE3A)
                 418538(PDE9A) 420752(PDE1C) 421574(PDE10A) 421692(PDE7B)
                 423064(RCJMB04_11f1) 424700(RCJMB04_9i13) 424932(PDE6D)
                 427645(PDE8B)
            XLA: 444661(MGC84234) 444670(MGC84265) 447555(MGC84203)
                 495103(LOC495103) 495146(LOC495146) 496104(LOC496104)
            DRE: 373876(pde6g) 394077(pde10a)
            SPU: 579864(LOC579864) 584165(LOC584165) 589178(LOC589178)
                 589578(LOC589578) 594283(LOC594283) 758840(LOC758840)
            DME: Dmel_CG14940(Pde1c) Dmel_CG32498(dnc) Dmel_CG8279(Pde6)
            CEL: C32E12.2(pde-5) T04D3.3(pde-1) Y95B8A.10(phosphodiesterase)
            SCE: YGL248W(PDE1) YOR360C(PDE2)
            AGO: AGOS_ADR395C
            PIC: PICST_78746(PDE2)
            CGR: CAGL0H07667g CAGL0K09944g
            SPO: SPCC285.09c(cgs2)
            ANI: AN2740.2
            AOR: AO090003000819 AO090005001243
            DDI: DDB_0219974(pdsA)
            PFA: MAL13P1.118 MAL13P1.119 PF14_0672 PFL0475w
            TAN: TA02890
            TET: TTHERM_00001240 TTHERM_00148930 TTHERM_00293350
                 TTHERM_00387020 TTHERM_00463080 TTHERM_00627210
                 TTHERM_00653840 TTHERM_00725920 TTHERM_01015870
                 TTHERM_01216060
            ECI: UTI89_C3466(icc)
            YPE: YPO2696
            YPK: y1271
            YPM: YP_2500
            YPA: YPA_2427
            YPN: YPN_1184
            YPP: YPDSF_1575
            YPS: YPTB2912
            YPI: YpsIP31758_1113(cpdP)
            SPE: Spro_1253
            HSO: HS_0581(icc)
            VFI: VF1256 VF2230
            PFL: PFL_0543(icc)
            PAR: Psyc_2036
            PAT: Patl_0338
            CBD: COXBU7E912_1625(cpdP)
            LPN: lpg1952
            LPF: lpl1921
            LPP: lpp1934
            NOC: Noc_1260
            CVI: CV_0835(icc)
            BML: BMA10299_A1577
            EBA: ebA1682
            AZO: azo0139(cpdA) azo0595 azo3329
            MLO: mll8078 mll9676
            LPL: lp_3251
            CMI: CMM_0485(cpdA)
            RBA: RB11266(cpdA)
            LIL: LA2847
            AVA: Ava_0091 Ava_3735
            FJO: Fjoh_1224
STRUCTURES  PDB: 1E9K  1F0J  1FQJ  1KSG  1KSH  1KSJ  1LOI  1MKD  1OYN  1PTW  
                 1Q9M  1RKP  1RO6  1RO9  1ROR  1SO2  1SOJ  1T9R  1T9S  1TAZ  
                 1TB5  1TB7  1TBB  1TBF  1UDT  1UDU  1UHO  1XLX  1XLZ  1XM4  
                 1XM6  1XMU  1XMY  1XN0  1XOM  1XON  1XOQ  1XOR  1XOS  1XOT  
                 1XOZ  1XP0  1Y2B  1Y2C  1Y2D  1Y2E  1Y2H  1Y2J  1Y2K  1Z1L  
                 1ZKL  1ZKN  2CHM  2FM0  2FM5  2HY1  2HYO  2HYP  2O8H  2OUN  
                 2OUP  2OUQ  2OUR  2OUS  2OUU  2OUV  2OUY  2OVV  2OVY  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.17
            ExPASy - ENZYME nomenclature database: 3.1.4.17
            ExplorEnz - The Enzyme Database: 3.1.4.17
            ERGO genome analysis and discovery system: 3.1.4.17
            BRENDA, the Enzyme Database: 3.1.4.17
            CAS: 9040-59-9
///
ENTRY       EC 3.1.4.18       Obsolete  Enzyme
NAME        Transferred to 3.1.16.1
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 3.1.16.1 spleen exonuclease (EC 3.1.4.18
            created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.18
            ExPASy - ENZYME nomenclature database: 3.1.4.18
            ExplorEnz - The Enzyme Database: 3.1.4.18
            ERGO genome analysis and discovery system: 3.1.4.18
            BRENDA, the Enzyme Database: 3.1.4.18
///
ENTRY       EC 3.1.4.19       Obsolete  Enzyme
NAME        Transferred to 3.1.13.3
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 3.1.13.3 oligonucleotidase (EC 3.1.4.19
            created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.19
            ExPASy - ENZYME nomenclature database: 3.1.4.19
            ExplorEnz - The Enzyme Database: 3.1.4.19
            ERGO genome analysis and discovery system: 3.1.4.19
            BRENDA, the Enzyme Database: 3.1.4.19
///
ENTRY       EC 3.1.4.20       Obsolete  Enzyme
NAME        Transferred to 3.1.13.1
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 3.1.13.1 exoribonuclease II (EC 3.1.4.20
            created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.20
            ExPASy - ENZYME nomenclature database: 3.1.4.20
            ExplorEnz - The Enzyme Database: 3.1.4.20
            ERGO genome analysis and discovery system: 3.1.4.20
            BRENDA, the Enzyme Database: 3.1.4.20
///
ENTRY       EC 3.1.4.21       Obsolete  Enzyme
NAME        Transferred to 3.1.30.1
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 3.1.30.1 Aspergillus nuclease S1 (EC
            3.1.4.21 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.21
            ExPASy - ENZYME nomenclature database: 3.1.4.21
            ExplorEnz - The Enzyme Database: 3.1.4.21
            ERGO genome analysis and discovery system: 3.1.4.21
            BRENDA, the Enzyme Database: 3.1.4.21
///
ENTRY       EC 3.1.4.22       Obsolete  Enzyme
NAME        Transferred to 3.1.27.5
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 3.1.27.5 pancreatic ribonuclease (EC
            3.1.4.22 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.22
            ExPASy - ENZYME nomenclature database: 3.1.4.22
            ExplorEnz - The Enzyme Database: 3.1.4.22
            ERGO genome analysis and discovery system: 3.1.4.22
            BRENDA, the Enzyme Database: 3.1.4.22
///
ENTRY       EC 3.1.4.23       Obsolete  Enzyme
NAME        Transferred to 3.1.27.1
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 3.1.27.1, ribonuclease T2 (EC 3.1.4.23
            created 1972, deleted 1978)
STRUCTURES  PDB: 1RMS  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.23
            ExPASy - ENZYME nomenclature database: 3.1.4.23
            ExplorEnz - The Enzyme Database: 3.1.4.23
            ERGO genome analysis and discovery system: 3.1.4.23
            BRENDA, the Enzyme Database: 3.1.4.23
///
ENTRY       EC 3.1.4.24       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Deleted entry: endoribonuclease III (EC 3.1.4.24 created 1972,
            deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.24
            ExPASy - ENZYME nomenclature database: 3.1.4.24
            ExplorEnz - The Enzyme Database: 3.1.4.24
            ERGO genome analysis and discovery system: 3.1.4.24
            BRENDA, the Enzyme Database: 3.1.4.24
///
ENTRY       EC 3.1.4.25       Obsolete  Enzyme
NAME        Transferred to 3.1.11.1
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 3.1.11.1 exodeoxyribonuclease I (EC
            3.1.4.25 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.25
            ExPASy - ENZYME nomenclature database: 3.1.4.25
            ExplorEnz - The Enzyme Database: 3.1.4.25
            ERGO genome analysis and discovery system: 3.1.4.25
            BRENDA, the Enzyme Database: 3.1.4.25
///
ENTRY       EC 3.1.4.26       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Deleted entry: exodeoxyribonuclease II (EC 3.1.4.26 created 1972,
            deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.26
            ExPASy - ENZYME nomenclature database: 3.1.4.26
            ExplorEnz - The Enzyme Database: 3.1.4.26
            ERGO genome analysis and discovery system: 3.1.4.26
            BRENDA, the Enzyme Database: 3.1.4.26
///
ENTRY       EC 3.1.4.27       Obsolete  Enzyme
NAME        Transferred to 3.1.11.2
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 3.1.11.2 exodeoxyribonuclease III (EC
            3.1.4.27 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.27
            ExPASy - ENZYME nomenclature database: 3.1.4.27
            ExplorEnz - The Enzyme Database: 3.1.4.27
            ERGO genome analysis and discovery system: 3.1.4.27
            BRENDA, the Enzyme Database: 3.1.4.27
///
ENTRY       EC 3.1.4.28       Obsolete  Enzyme
NAME        Transferred to 3.1.11.3
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 3.1.11.3, exodeoxyribonuclease
            (lambda-induced) (EC 3.1.4.28 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.28
            ExPASy - ENZYME nomenclature database: 3.1.4.28
            ExplorEnz - The Enzyme Database: 3.1.4.28
            ERGO genome analysis and discovery system: 3.1.4.28
            BRENDA, the Enzyme Database: 3.1.4.28
///
ENTRY       EC 3.1.4.29       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Deleted entry: oligodeoxyribonucleate exonuclease (EC 3.1.4.29
            created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.29
            ExPASy - ENZYME nomenclature database: 3.1.4.29
            ExplorEnz - The Enzyme Database: 3.1.4.29
            ERGO genome analysis and discovery system: 3.1.4.29
            BRENDA, the Enzyme Database: 3.1.4.29
///
ENTRY       EC 3.1.4.30       Obsolete  Enzyme
NAME        Transferred to 3.1.21.2
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 3.1.21.2, deoxyribonuclease IV
            (phage-T4-induced) (EC 3.1.4.30 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.30
            ExPASy - ENZYME nomenclature database: 3.1.4.30
            ExplorEnz - The Enzyme Database: 3.1.4.30
            ERGO genome analysis and discovery system: 3.1.4.30
            BRENDA, the Enzyme Database: 3.1.4.30
///
ENTRY       EC 3.1.4.31       Obsolete  Enzyme
NAME        Transferred to 3.1.11.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 3.1.11.4, exodeoxyribonuclease (phage
            SP3-induced) (EC 3.1.4.31 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.31
            ExPASy - ENZYME nomenclature database: 3.1.4.31
            ExplorEnz - The Enzyme Database: 3.1.4.31
            ERGO genome analysis and discovery system: 3.1.4.31
            BRENDA, the Enzyme Database: 3.1.4.31
///
ENTRY       EC 3.1.4.32       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Deleted entry: endodeoxyribonuclease (ATP- and
            S-adenosylmethionine-dependent). See EC 3.1.21.3 type 1
            site-specific deoxyribonuclease and EC 3.1.21.5 type III
            site-specific deoxyribonuclease (EC 3.1.4.32 created 1972, deleted
            1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.32
            ExPASy - ENZYME nomenclature database: 3.1.4.32
            ExplorEnz - The Enzyme Database: 3.1.4.32
            ERGO genome analysis and discovery system: 3.1.4.32
            BRENDA, the Enzyme Database: 3.1.4.32
///
ENTRY       EC 3.1.4.33       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Deleted entry: endodeoxyribonuclease (ATP-hydrolysing). See EC
            3.1.21.3 type 1 site-specific deoxyribonuclease and EC 3.1.21.5 type
            III site-specific deoxyribonuclease (EC 3.1.4.33 created 1972,
            deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.33
            ExPASy - ENZYME nomenclature database: 3.1.4.33
            ExplorEnz - The Enzyme Database: 3.1.4.33
            ERGO genome analysis and discovery system: 3.1.4.33
            BRENDA, the Enzyme Database: 3.1.4.33
///
ENTRY       EC 3.1.4.34       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Deleted entry: hybrid nuclease. See subclasses EC 3.1.15, EC 3.1.16,
            EC 3.1.30 and EC 3.1.31 (EC 3.1.4.34 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.34
            ExPASy - ENZYME nomenclature database: 3.1.4.34
            ExplorEnz - The Enzyme Database: 3.1.4.34
            ERGO genome analysis and discovery system: 3.1.4.34
            BRENDA, the Enzyme Database: 3.1.4.34
///
ENTRY       EC 3.1.4.35                 Enzyme
NAME        3',5'-cyclic-GMP phosphodiesterase;
            guanosine cyclic 3',5'-phosphate phosphodiesterase;
            cyclic GMP phosphodiesterase;
            cyclic 3',5'-GMP phosphodiesterase;
            cyclic guanosine 3',5'-monophosphate phosphodiesterase;
            cyclic guanosine 3',5'-phosphate phosphodiesterase;
            cGMP phosphodiesterase;
            cGMP-PDE;
            cyclic guanosine 3',5'-phosphate phosphodiesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     3',5'-cyclic-GMP 5'-nucleotidohydrolase
REACTION    guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate
            [RN:R01234]
ALL_REAC    R01234
SUBSTRATE   guanosine 3',5'-cyclic phosphate [CPD:C00942];
            H2O [CPD:C00001]
PRODUCT     guanosine 5'-phosphate [CPD:C00144]
REFERENCE   1
  AUTHORS   Marks, F. and Raab, I.
  TITLE     The second messenger system of mouse epidermis. IV. Cyclic AMP and
            cyclic GMP phosphodiesterase.
  JOURNAL   Biochim. Biophys. Acta 334 (1974) 368-377.
  ORGANISM  mouse [GN:mmu]
ORTHOLOGY   KO: K08718  3',5'-cyclic-GMP phosphodiesterase
GENES       HSA: 50940(PDE11A) 5145(PDE6A) 5146(PDE6C) 5158(PDE6B)
            MMU: 110855(Pde6c) 18587(Pde6b) 225600(Pde6a)
            RNO: 289878(Pde6b_predicted) 307401(Pde6a_predicted)
                 361752(Pde6c_predicted)
            CFA: 399653(PDE6B) 403620(PDE6A) 486805(PDE6C)
            BTA: 281973(PDE6A) 281974(PDE6B) 281975(PDE6C)
            GGA: 395092(PDE6B) 395834(PDE6C)
            DRE: 368410(pde6a) 393845(pde6c) 559332(LOC559332)
STRUCTURES  PDB: 1MC0  2CHM  2H40  2H42  2H44  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.35
            ExPASy - ENZYME nomenclature database: 3.1.4.35
            ExplorEnz - The Enzyme Database: 3.1.4.35
            ERGO genome analysis and discovery system: 3.1.4.35
            BRENDA, the Enzyme Database: 3.1.4.35
            CAS: 9068-52-4
///
ENTRY       EC 3.1.4.36       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Deleted entry: 1,2-cyclic-inositol-phosphate phosphodiesterase. Now
            included with EC 3.1.4.43, glycerophosphoinositol
            inositolphosphodiesterase (EC 3.1.4.36 created 1976, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.36
            ExPASy - ENZYME nomenclature database: 3.1.4.36
            ExplorEnz - The Enzyme Database: 3.1.4.36
            ERGO genome analysis and discovery system: 3.1.4.36
            BRENDA, the Enzyme Database: 3.1.4.36
///
ENTRY       EC 3.1.4.37                 Enzyme
NAME        2',3'-cyclic-nucleotide 3'-phosphodiesterase;
            cyclic-CMP phosphodiesterase;
            2',3'-cyclic AMP phosphodiesterase;
            cyclic 2',3'-nucleotide 3'-phosphodiesterase;
            cyclic 2',3'-nucleotide phosphodiesterase;
            2',3'-cyclic nucleoside monophosphate phosphodiesterase;
            2',3'-cyclic nucleotide 3'-phosphohydrolase;
            CNPase;
            2',3'-cyclic nucleotide phosphohydrolase;
            2':3'-cyclic nucleotide 3'-phosphodiesterase;
            2':3'-CNMP-3'-ase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     nucleoside-2',3'-cyclic-phosphate 2'-nucleotidohydrolase
REACTION    nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 2'-phosphate
            [RN:R03422]
ALL_REAC    R03422
SUBSTRATE   nucleoside 2',3'-cyclic phosphate [CPD:C01240];
            H2O [CPD:C00001]
PRODUCT     nucleoside 2'-phosphate [CPD:C03418]
COMMENT     The brain enzyme acts on 2',3'-cyclic AMP more rapidly than on the
            UMP or CMP derivatives. An enzyme from liver acts on 2',3'-cyclic
            CMP more rapidly than on the purine derivatives; it also hydrolyses
            the corresponding 3',5'-cyclic phosphates, but more slowly. This
            latter enzyme has been called cyclic-CMP phosphodiesterase.
REFERENCE   1
  AUTHORS   Drummond, G.I., Iyer, N.T. and Keith, J.
  TITLE     Hydrolysis of ribonucleoside 2',3'-cyclic phosphates by a diesterase
            from brain.
  JOURNAL   J. Biol. Chem. 237 (1962) 3535-3539.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:6274851]
  AUTHORS   Helfman DM, Kuo JF.
  TITLE     A homogeneous cyclic CMP phosphodiesterase hydrolyzes both
            pyrimidine and purine cyclic 2':3'- and 3':5'-nucleotides.
  JOURNAL   J. Biol. Chem. 257 (1982) 1044-7.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:6263914]
  AUTHORS   Helfman DM, Shoji M, Kuo JF.
  TITLE     Purification to homogeneity and general properties of a novel
            phosphodiesterase hydrolyzing cyclic CMP and cyclic AMP.
  JOURNAL   J. Biol. Chem. 256 (1981) 6327-34.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:6272743]
  AUTHORS   Kurihara T, Nishizawa Y, Takahashi Y, Odani S.
  TITLE     Chemical, immunological and catalytic properties of 2':3'-cyclic
            nucleotide 3'-phosphodiesterase purified from brain white matter.
  JOURNAL   Biochem. J. 195 (1981) 153-7.
  ORGANISM  cow [GN:bta]
REFERENCE   5  [PMID:6258586]
  AUTHORS   Nishizawa Y, Kurihara T, Takahashi Y.
  TITLE     Spectrophotometric assay, solubilization and purification of brain
            2':3'-cyclic nucleotide 3'-phosphodiesterase.
  JOURNAL   Biochem. J. 191 (1980) 71-82.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K01121  2',3'-cyclic-nucleotide 3'-phosphodiesterase
GENES       HSA: 1267(CNP)
            PTR: 454673(CNP)
            MCC: 641337(CNP)
            MMU: 12799(Cnp)
            RNO: 25275(Cnp1)
            CFA: 607694(CNP)
            BTA: 280752(CNP)
            GGA: 395921(CNP)
            SPU: 582388(LOC582388)
            FNU: FN1603
STRUCTURES  PDB: 1WOJ  2I3E  2ILX  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.37
            ExPASy - ENZYME nomenclature database: 3.1.4.37
            ExplorEnz - The Enzyme Database: 3.1.4.37
            ERGO genome analysis and discovery system: 3.1.4.37
            BRENDA, the Enzyme Database: 3.1.4.37
            CAS: 60098-35-3
///
ENTRY       EC 3.1.4.38                 Enzyme
NAME        glycerophosphocholine cholinephosphodiesterase;
            L-3-glycerylphosphinicocholine cholinephosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     sn-glycero-3-phosphocholine cholinephosphohydrolase
REACTION    sn-glycero-3-phosphocholine + H2O = glycerol + choline phosphate
            [RN:R02591]
ALL_REAC    R02591
SUBSTRATE   sn-glycero-3-phosphocholine [CPD:C00670];
            H2O [CPD:C00001]
PRODUCT     glycerol [CPD:C00116];
            choline phosphate [CPD:C00588]
COMMENT     No activity on sn-3-glycerophosphoethanolamine.
REFERENCE   1  [PMID:166661]
  AUTHORS   Abra RM, Quinn PJ.
  TITLE     A novel pathway for phosphatidylcholine catabolism in rat brain
            homogenates.
  JOURNAL   Biochim. Biophys. Acta. 380 (1975) 436-41.
  ORGANISM  rat [GN:rno]
STRUCTURES  PDB: 1WRA  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.38
            ExPASy - ENZYME nomenclature database: 3.1.4.38
            ExplorEnz - The Enzyme Database: 3.1.4.38
            ERGO genome analysis and discovery system: 3.1.4.38
            BRENDA, the Enzyme Database: 3.1.4.38
            CAS: 60063-78-7
///
ENTRY       EC 3.1.4.39                 Enzyme
NAME        alkylglycerophosphoethanolamine phosphodiesterase;
            lysophospholipase D
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     1-alkyl-sn-glycero-3-phosphoethanolamine ethanolaminehydrolase
REACTION    1-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-alkyl-sn-glycerol
            3-phosphate + ethanolamine [RN:R04362]
ALL_REAC    R04362;
            (other) R07388
SUBSTRATE   1-alkyl-sn-glycero-3-phosphoethanolamine [CPD:C04476];
            H2O [CPD:C00001]
PRODUCT     1-alkyl-sn-glycerol 3-phosphate [CPD:C03968];
            ethanolamine [CPD:C00189]
COMMENT     Also acts on acyl and choline analogues.
REFERENCE   1  [PMID:4855486]
  AUTHORS   Wykle RL, Schremmer JM.
  TITLE     A lysophospholipase D pathway in the metabolism of ether-linked
            lipids in brain microsomes.
  JOURNAL   J. Biol. Chem. 249 (1974) 1742-6.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00565  Ether lipid metabolism
ORTHOLOGY   KO: K01122  alkylglycerophosphoethanolamine phosphodiesterase
STRUCTURES  PDB: 1FJ2  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.39
            ExPASy - ENZYME nomenclature database: 3.1.4.39
            ExplorEnz - The Enzyme Database: 3.1.4.39
            ERGO genome analysis and discovery system: 3.1.4.39
            BRENDA, the Enzyme Database: 3.1.4.39
            CAS: 62213-15-4
///
ENTRY       EC 3.1.4.40                 Enzyme
NAME        CMP-N-acylneuraminate phosphodiesterase;
            CMP-sialate hydrolase;
            CMP-sialic acid hydrolase;
            CMP-N-acylneuraminic acid hydrolase;
            cytidine monophosphosialic hydrolase;
            cytidine monophosphosialate hydrolase;
            cytidine monophosphate-N-acetylneuraminic acid hydrolase;
            CMP-N-acetylneuraminate hydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     CMP-N-acylneuraminate N-acylneuraminohydrolase
REACTION    CMP-N-acylneuraminate + H2O = CMP + N-acylneuraminate [RN:R02598]
ALL_REAC    R02598
SUBSTRATE   CMP-N-acylneuraminate [CPD:C01064];
            H2O [CPD:C00001]
PRODUCT     CMP [CPD:C00055];
            N-acylneuraminate [CPD:C00591]
REFERENCE   1  [PMID:4372219]
  AUTHORS   Kean EL, Bighouse KJ.
  TITLE     Cytidine 5'-monophosphosialic acid hydrolase. Subcellular location
            and properties.
  JOURNAL   J. Biol. Chem. 249 (1974) 7813-23.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.40
            ExPASy - ENZYME nomenclature database: 3.1.4.40
            ExplorEnz - The Enzyme Database: 3.1.4.40
            ERGO genome analysis and discovery system: 3.1.4.40
            BRENDA, the Enzyme Database: 3.1.4.40
            CAS: 55326-41-5
///
ENTRY       EC 3.1.4.41                 Enzyme
NAME        sphingomyelin phosphodiesterase D;
            sphingomyelinase D
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     sphingomyelin ceramide-phosphohydrolase
REACTION    sphingomyelin + H2O = ceramide phosphate + choline [RN:R02542]
ALL_REAC    R02542
SUBSTRATE   sphingomyelin [CPD:C00550];
            H2O [CPD:C00001]
PRODUCT     ceramide phosphate [CPD:C02960];
            choline [CPD:C00114]
COMMENT     Does not act on phosphatidylcholine, but hydrolyses
            2-lysophosphatidylcholine to choline and 2-lysophosphatidate.
REFERENCE   1  [PMID:622164]
  AUTHORS   Carne HR, Onon EO.
  TITLE     Action of Corynebacterium ovis exotoxin on endothelial cells of
            blood vessels.
  JOURNAL   Nature. 271 (1978) 246-8.
  ORGANISM  Corynebacterium ovis
REFERENCE   2  [PMID:5543581]
  AUTHORS   Soucek A, Michalec C, Souckova A.
  TITLE     Identification and characterization of a new enzyme of the group
            &quot;phospholipase D&quot; isolated from Corynebacterium ovis.
  JOURNAL   Biochim. Biophys. Acta. 227 (1971) 116-28.
  ORGANISM  Corynebacterium ovis
PATHWAY     PATH: map00600  Sphingolipid metabolism
ORTHOLOGY   KO: K01123  sphingomyelin phosphodiesterase D
STRUCTURES  PDB: 1XX1  2F9R  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.41
            ExPASy - ENZYME nomenclature database: 3.1.4.41
            ExplorEnz - The Enzyme Database: 3.1.4.41
            ERGO genome analysis and discovery system: 3.1.4.41
            BRENDA, the Enzyme Database: 3.1.4.41
            CAS: 54992-31-3
///
ENTRY       EC 3.1.4.42                 Enzyme
NAME        glycerol-1,2-cyclic-phosphate 2-phosphodiesterase;
            rac-glycerol 1:2-cyclic phosphate 2-phosphodiesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     rac-glycerol-1,2-cyclic-phosphate 2-glycerophosphohydrolase
REACTION    glycerol 1,2-cyclic phosphate + H2O = glycerol 1-phosphate
            [RN:R02648]
ALL_REAC    R02648
SUBSTRATE   glycerol 1,2-cyclic phosphate [CPD:C03947];
            H2O [CPD:C00001]
PRODUCT     glycerol 1-phosphate [CPD:C00623]
COMMENT     Acts on both stereoisomers of the substrate and also, more slowly,
            on 3',5'-cyclic AMP and on 2',3'-cyclic AMP.
REFERENCE   1  [PMID:212014]
  AUTHORS   Clarke N, Dawson RM.
  TITLE     rac-Glycerol 1:2-cyclic phosphate 2-phosphodiesterase, a new soluble
            phosphodiesterase of mammalian tissues.
  JOURNAL   Biochem. J. 173 (1978) 579-89.
  ORGANISM  rat [GN:rno], mouse [GN:mmu], guinea pig, sheep, pig [GN:ssc]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.42
            ExPASy - ENZYME nomenclature database: 3.1.4.42
            ExplorEnz - The Enzyme Database: 3.1.4.42
            ERGO genome analysis and discovery system: 3.1.4.42
            BRENDA, the Enzyme Database: 3.1.4.42
            CAS: 69458-89-5
///
ENTRY       EC 3.1.4.43                 Enzyme
NAME        glycerophosphoinositol inositolphosphodiesterase;
            1,2-cyclic-inositol-phosphate phosphodiesterase;
            D-myo-inositol 1:2-cyclic phosphate 2-phosphohydrolase;
            D-inositol 1,2-cyclic phosphate 2-phosphohydrolase;
            D-myo-inositol 1,2-cyclic phosphate 2-phosphohydrolase;
            1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase;
            inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     1-(sn-glycero-3-phospho)-1D-myo-inositol inositolphosphohydrolase
REACTION    1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O = glycerol +
            1D-myo-inositol 1-phosphate [RN:R03331]
ALL_REAC    R03331;
            (other) R03333
SUBSTRATE   1-(sn-glycero-3-phospho)-1D-myo-inositol [CPD:C01225];
            H2O [CPD:C00001]
PRODUCT     glycerol [CPD:C00116];
            1D-myo-inositol 1-phosphate [CPD:C01177]
COMMENT     This enzyme also hydrolyses Ins(cyclic1,2)P to Ins-1-P
REFERENCE   1  [PMID:192216]
  AUTHORS   Dawson RM, Hemington N.
  TITLE     A phosphodiesterase in rat kidney cortex that hydrolyses
            glycerylphosphorylinositol.
  JOURNAL   Biochem. J. 162 (1977) 241-5.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4342209]
  AUTHORS   Dawson RM, Clarke N.
  TITLE     D-myoinositol 1:2-cyclic phosphate 2-phosphohydrolase.
  JOURNAL   Biochem. J. 127 (1972) 113-8.
  ORGANISM  rat [GN:rno], pig [GN:ssc], cow [GN:bta]
REFERENCE   3  [PMID:4353088]
  AUTHORS   Dawson RM, Clarke NG.
  TITLE     A comparison of D-inositol 1:2-cyclic phosphate 2-phosphohydrolase
            with other phosphodiesterases of kidney.
  JOURNAL   Biochem. J. 134 (1973) 59-67.
  ORGANISM  rat [GN:rno], mouse [GN:mmu], guinea pig, cow [GN:bta]
REFERENCE   4  [PMID:1845995]
  AUTHORS   Ross TS, Majerus PW.
  TITLE     Inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase. Substrate
            specificity and regulation of activity by phospholipids, metal ion
            chelators, and inositol 2-phosphate.
  JOURNAL   J. Biol. Chem. 266 (1991) 851-6.
  ORGANISM  rat [GN:rno], human [GN:hsa]
ORTHOLOGY   KO: K01124  glycerophosphoinositol inositolphosphodiesterase
GENES       HSA: 306(ANXA3)
            MMU: 11745(Anxa3)
            RNO: 25291(Anxa3)
            CFA: 478447(ANXA3)
            XLA: 443953(MGC80326)
            REH: H16_A0498(ruvA)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.43
            ExPASy - ENZYME nomenclature database: 3.1.4.43
            ExplorEnz - The Enzyme Database: 3.1.4.43
            ERGO genome analysis and discovery system: 3.1.4.43
            BRENDA, the Enzyme Database: 3.1.4.43
            CAS: 9076-91-9
///
ENTRY       EC 3.1.4.44                 Enzyme
NAME        glycerophosphoinositol glycerophosphodiesterase;
            sn-glycero(3)phosphoinositol glycerophosphohydrolase;
            sn-glycero-3-phospho-1-inositol glycerophosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     1-(sn-glycero-3-phospho)-1D-myo-inositol glycerophosphohydrolase
REACTION    1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O = myo-inositol +
            sn-glycerol 3-phosphate [RN:R01193]
ALL_REAC    R01193
SUBSTRATE   1-(sn-glycero-3-phospho)-1D-myo-inositol [CPD:C01225];
            H2O [CPD:C00001]
PRODUCT     myo-inositol [CPD:C00137];
            sn-glycerol 3-phosphate [CPD:C00093]
REFERENCE   1  [PMID:40550]
  AUTHORS   Dawson RM, Hemington N, Richards DE, Irvine RF.
  TITLE     sn-Glycero(3)phosphoinositol glycerophosphohydrolase. A new
            phosphodiesterase in rat tissues.
  JOURNAL   Biochem. J. 182 (1979) 39-49.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.44
            ExPASy - ENZYME nomenclature database: 3.1.4.44
            ExplorEnz - The Enzyme Database: 3.1.4.44
            ERGO genome analysis and discovery system: 3.1.4.44
            BRENDA, the Enzyme Database: 3.1.4.44
            CAS: 72414-13-2
///
ENTRY       EC 3.1.4.45                 Enzyme
NAME        N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase;
            alpha-N-acetylglucosaminyl phosphodiesterase;
            lysosomal alpha-N-acetylglucosaminidase;
            phosphodiester glycosidase;
            alpha-N-acetyl-D-glucosamine-1-phosphodiester
            N-acetylglucosaminidase;
            2-acetamido-2-deoxy-alpha-D-glucose 1-phosphodiester
            acetamidodeoxyglucohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     glycoprotein-N-acetyl-D-glucosaminyl-phospho-D-mannose
            N-acetyl-D-glucosaminylphosphohydrolase
REACTION    glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O =
            N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose [RN:R04373]
ALL_REAC    R04373
SUBSTRATE   glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose [CPD:C04755];
            H2O [CPD:C00001]
PRODUCT     N-acetyl-D-glucosamine [CPD:C00140];
            glycoprotein phospho-D-mannose [CPD:C04010]
COMMENT     Acts on a variety of compounds in which N-acetyl-D-glucosamine is
            alpha-linked to a phosphate group, including the biosynthetic
            intermediates of the high mannose oligosaccharide components of some
            lysosomal enzymes and the products of EC 2.7.8.17
            UDP-N-acetylglucosamine#151;lysosomal-enzyme
            N-acetylglucosaminephosphotransferase.
REFERENCE   1  [PMID:16525953]
  AUTHORS   Hildebrand F, van Griensven M, Giannoudis P, Schreiber T, Frink M,
            Probst C, Grotz M, Krettek C, Pape HC.
  TITLE     Impact of hypothermia on the immunologic response after trauma and
            elective surgery.
  JOURNAL   Surg. Technol. Int. 14 (2005) 41-50.
REFERENCE   2  [PMID:4399430]
  AUTHORS   van der Drift C, van Helvoort PE, Vogels GD.
  TITLE     S-ureidoglycolate dehydrogenase: purification and properties.
  JOURNAL   Arch. Biochem. Biophys. 145 (1971) 465-9.
REFERENCE   3  [PMID:237557]
  AUTHORS   Van der Drift L, Vogels GD, Van der Drift C.
  TITLE     Allantoin racemase: a new enzyme from Pseudomonas species.
  JOURNAL   Biochim. Biophys. Acta. 391 (1975) 240-8.
REFERENCE   4  [PMID:6263889]
  AUTHORS   Waheed A, Hasilik A, von Figura K.
  TITLE     Processing of the phosphorylated recognition marker in lysosomal
            enzymes. Characterization and partial purification of a microsomal
            alpha-N-acetylglucosaminyl phosphodiesterase.
  JOURNAL   J. Biol. Chem. 256 (1981) 5717-21.
  ORGANISM  human [GN:hsa], rat [GN:rno]
ORTHOLOGY   KO: K01125  N-acetylglucosamine-1-phosphodiester
                        alpha-N-acetylglucosaminidase
GENES       HSA: 51172(NAGPA)
            MMU: 27426(Nagpa)
            CFA: 490019(NAGPA)
            GGA: 416395(NAGPA)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.45
            ExPASy - ENZYME nomenclature database: 3.1.4.45
            ExplorEnz - The Enzyme Database: 3.1.4.45
            ERGO genome analysis and discovery system: 3.1.4.45
            BRENDA, the Enzyme Database: 3.1.4.45
            CAS: 75788-84-0
///
ENTRY       EC 3.1.4.46                 Enzyme
NAME        glycerophosphodiester phosphodiesterase;
            gene hpd protein;
            glycerophosphoryl diester phosphodiesterase;
            IgD-binding protein D
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     glycerophosphodiester glycerophosphohydrolase
REACTION    a glycerophosphodiester + H2O = an alcohol + sn-glycerol 3-phosphate
            [RN:R00857]
ALL_REAC    R00857 > R01030 R01470
SUBSTRATE   glycerophosphodiester [CPD:C03120];
            H2O [CPD:C00001]
PRODUCT     alcohol [CPD:C00069];
            sn-glycerol 3-phosphate [CPD:C00093]
COMMENT     Broad specificity for glycerophosphodiesters; glycerophosphocholine,
            glycerophosphoethanolamine, glycerophosphoglycerol and
            bis(glycerophospho)-glycerol are hydrolysed.
REFERENCE   1  [PMID:6304089]
  AUTHORS   Larson TJ, Ehrmann M, Boos W.
  TITLE     Periplasmic glycerophosphodiester phosphodiesterase of Escherichia
            coli, a new enzyme of the glp regulon.
  JOURNAL   J. Biol. Chem. 258 (1983) 5428-32.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K01126  glycerophosphoryl diester phosphodiesterase
GENES       CEL: F55C5.2 T12B3.3(phosphodiesterase)
            ATH: AT1G74210 AT5G08030
            OSA: 4327034 4333407
            SCE: YPL206C
            AGO: AGOS_AFL096C
            PIC: PICST_35844(GLP1)
            CGR: CAGL0E05654g
            SPO: SPAC4D7.02c
            AFM: AFUA_2G00990 AFUA_6G12240
            UMA: UM00004.1
            DDI: DDBDRAFT_0216796
            CHO: Chro.40291
            TET: TTHERM_00250990 TTHERM_00701150 TTHERM_00957590
            LMA: LmjF36.5960
            EHI: 101.t00008 298.t00013 61.t00044
            ECO: b2239(glpQ) b3449(ugpQ)
            ECJ: JW2233(glpQ) JW3414(ugpQ)
            ECE: Z3497(glpQ) Z4817(ugpQ)
            ECS: ECs3124 ECs4295
            ECC: c2780(glpQ) c4238(ugpQ)
            ECI: UTI89_C2519(glpQ) UTI89_C3956(ugpQ)
            ECP: ECP_2281 ECP_3542
            ECV: APECO1_3010(ugpQ) APECO1_4322(glpQ)
            ECW: EcE24377A_2536(glpQ) EcE24377A_3926
            ECX: EcHS_A2379(glpQ) EcHS_A3646
            STY: STY2511(glpQ) STY4258(ugpQ)
            STT: t0582(glpQ) t3968(ugpQ)
            SPT: SPA0582(glpQ) SPA3405(ugpQ)
            SEC: SC2285(glpQ) SC3482(ugpQ)
            STM: STM2282(glpQ) STM3553(ugpQ)
            YPE: YPO3792(ugpQ) YPO3827(glpQ)
            YPK: y0403(glpQ) y0438(ugpQ)
            YPM: YP_3221(glpQ) YP_3257(ugpQ4)
            YPA: YPA_0195 YPA_0232
            YPN: YPN_0137 YPN_0172
            YPP: YPDSF_3409 YPDSF_3444
            YPS: YPTB0208(glpQ) YPTB0242(ugpQ)
            YPI: YpsIP31758_0224(glpQ) YpsIP31758_0260(ugpQ)
            YEN: YE0245(ugpQ)
            SFL: SF2321(glpQ) SF3466(ugpQ)
            SFX: S2454(glpQ) S4296(ugpQ)
            SFV: SFV_2311(glpQ) SFV_3452(ugpQ)
            SSN: SSON_2300(glpQ) SSON_3687(ugpQ)
            SBO: SBO_2055(glpQ) SBO_3445(ugpQ)
            SDY: SDY_2434(glpQ)
            ECA: ECA4167(glpQ) ECA4318(ugpQ)
            PLU: plu4120(glpQ)
            ENT: Ent638_3852
            KPN: KPN_02645(glpQ)
            SPE: Spro_0238
            HIN: HI0689(glpQ)
            HIT: NTHI0811(glpQ)
            HIP: CGSHiEE_08675(glpQ) CGSHiEE_08750(glpQ)
            HIQ: CGSHiGG_06740(glpQ) CGSHiGG_06785(glpQ)
            HSO: HS_0510(glpQ)
            PMU: PM1444(glpQ)
            MSU: MS1992(ugpQ)
            APL: APL_0378(glpQ)
            XCC: XCC1042(glpQ) XCC4234(glpQ)
            XCB: XC_3204 XC_4324
            XCV: XCV1166 XCV4479
            XAC: XAC1147(glpQ) XAC4367(glpQ)
            XOO: XOO0902(glpQ) XOO4628(glpQ)
            XOM: XOO_0828(XOO0828) XOO_4364(XOO4364)
            VCH: VC1554 VCA0136
            VCO: VC0395_0002(glpQ)
            VVU: VV1_2754 VV2_0407
            VVY: VV1507 VVA0967
            VPA: VP2381 VPA0146
            VFI: VFA0958
            PPR: PBPRA1100 PBPRB1005(glpQ) PBPRB1006
            PAE: PA0347(glpQ) PA2352 PA2990
            PAU: PA14_04550(glpQ) PA14_25400(ugpQ) PA14_34250 PA14_63330
            PPU: PP_2152
            PST: PSPTO_0660 PSPTO_2107 PSPTO_3461(glpQ)
            PSB: Psyr_1902 Psyr_3242 Psyr_4506
            PSP: PSPPH_1857 PSPPH_3162(glpQ) PSPPH_4534
            PFL: PFL_1959 PFL_3296(glpQ-1) PFL_4539
            PFO: Pfl_3861 Pfl_4314
            PEN: PSEEN3710 PSEEN4329
            PMY: Pmen_0662
            PAR: Psyc_1364
            PCR: Pcryo_1000
            ACI: ACIAD0632
            SON: SO_0587
            SDN: Sden_3215
            SFR: Sfri_3322
            SBL: Sbal_4260
            SHE: Shewmr4_0586
            SHM: Shewmr7_3444
            SHN: Shewana3_0585 Shewana3_3480
            ILO: IL2162(glpQ) IL2303(ugpQ)
            CPS: CPS_0915
            PHA: PSHAa2483
            PAT: Patl_1401 Patl_3485
            SDE: Sde_1481
            PIN: Ping_2092 Ping_3177
            MAQ: Maqu_1922
            CBU: CBU_0642
            LPN: lpg2274(ugpQ) lpg2970
            LPF: lpl2200 lpl2900
            LPP: lpp2228 lpp3042
            FTU: FTT0726c FTT1132c(glpQ)
            FTF: FTF0726c FTF1132c(glpQ)
            FTW: FTW_1165 FTW_1512
            FTL: FTL_0829 FTL_1511
            FTH: FTH_0819(glpQ) FTH_1463(ugpQ)
            FTN: FTN_0637(ugpQ) FTN_1114(glpQ)
            NOC: Noc_1686
            AEH: Mlg_1886
            HCH: HCH_01669(ugpQ) HCH_02696
            CSA: Csal_1506 Csal_2061
            ABO: ABO_0426 ABO_1042
            MMW: Mmwyl1_0608
            AHA: AHA_1653 AHA_3206
            CVI: CV_2854(glpQ) CV_3652(ugpQ)
            RSO: RSc0502(glpQ) RSc1268(ugpQ)
            REU: Reut_A0485 Reut_A2048(ugpQ)
            REH: H16_A0497(ruvB) H16_A0499(gdpD) H16_A2326(ugpQ)
            RME: Rmet_0425 Rmet_2051 Rmet_2204
            BMA: BMA2022 BMA2740(ugpQ) BMAA0512
            BMV: BMASAVP1_A3213(ugpQ)
            BML: BMA10299_A1764(ugpQ)
            BMN: BMA10247_2790(ugpQ)
            BXE: Bxe_A0449 Bxe_A4202
            BVI: Bcep1808_0381
            BUR: Bcep18194_A3496(ugpQ) Bcep18194_B1750
            BCN: Bcen_2708 Bcen_4105
            BCH: Bcen2424_0399 Bcen2424_4261
            BAM: Bamb_0318
            BPS: BPSL2712 BPSL3066 BPSL3162(ugpQ)
            BPM: BURPS1710b_3194(glpQ) BURPS1710b_3593 BURPS1710b_3721(ugpQ)
            BPL: BURPS1106A_3751(ugpQ)
            BPD: BURPS668_3693(ugpQ)
            BTE: BTH_I1425 BTH_I3017
            BPE: BP1731(ugpQ)
            BPA: BPP3045(ugpQ)
            BBR: BB3008(ugpQ)
            RFR: Rfer_1116 Rfer_1283
            POL: Bpro_0853 Bpro_1464 Bpro_3128
            AAV: Aave_3655
            AJS: Ajs_0858
            VEI: Veis_1306
            MPT: Mpe_A2739
            HAR: HEAR0615(ugpQ)
            MMS: mma_0582(glpQ)
            NEU: NE0371
            NET: Neut_1769
            NMU: Nmul_A2091
            EBA: ebA4509(ugpQ)
            AZO: azo1013(ugpQ)
            DAR: Daro_0237 Daro_3305
            TDN: Tmden_1231
            NIS: NIS_0508(ugpQ)
            PCA: Pcar_1855 Pcar_2333
            DVU: DVU0176
            DDE: Dde_0435
            BBA: Bd1385(glpQ) Bd2198 Bd2817(ugpQ)
            DPS: DP0285 DP0335
            ADE: Adeh_3985
            MXA: MXAN_2592 MXAN_5810
            MES: Meso_0996
            SME: SMc03129
            ATU: Atu4212(ugpQ)
            ATC: AGR_L_1291
            RET: RHE_CH02749(glpQ) RHE_PB00135(ypb00086) RHE_PC00082(ugpQ)
            RLE: RL1291 RL2217 RL3131 pRL120015 pRL90114 pRL90266
            BJA: blr6584
            BRA: BRADO4526
            BBT: BBta_4752
            RPE: RPE_3392 RPE_3536
            BHE: BH01830
            BQU: BQ01720
            CCR: CC_3272
            SIL: SPO0236 SPO0301
            SIT: TM1040_0853
            RDE: RD1_0308(glpQ) RD1_1698
            MMR: Mmar10_2872
            HNE: HNE_0902 HNE_2409(glpQ)
            ZMO: ZMO0168(glpQ) ZMO0170(glpQ)
            ELI: ELI_14530
            GOX: GOX1714
            GBE: GbCGDNIH1_0114
            RRU: Rru_A3786
            MAG: amb0527
            MGM: Mmc1_0646
            ABA: Acid345_2183
            SUS: Acid_4915
            BSU: BG10646(glpQ) BG11719(yqiK) BG13029(yhdW)
            BHA: BH1080 BH1776 BH3700(glpQ)
            BAN: BA0591 BA2668 BA3560 BA4391 BA5622
            BAR: GBAA0591 GBAA2668 GBAA3560 GBAA4391 GBAA5622
            BAA: BA_0477 BA_3184 BA_4051 BA_4846
            BAT: BAS0560 BAS2484 BAS3300 BAS4074 BAS5222
            BCE: BC0591 BC2676 BC3495 BC4167 BC5374
            BCA: BCE_0658 BCE_2703 BCE_3514 BCE_4241 BCE_5503
            BCZ: BCZK0504(glpQ) BCZK2415(glpQ) BCZK3215(glpQ) BCZK3921(glpQ)
                 BCZK5070(glpQ)
            BCY: Bcer98_2205 Bcer98_2863 Bcer98_3887
            BTK: BT9727_0502(glpQ) BT9727_2446(glpQ) BT9727_3270(glpQ)
                 BT9727_3912(glpQ) BT9727_5054(glpQ)
            BTL: BALH_0531(glpQ) BALH_2402(glpQ) BALH_2916(glpQ)
                 BALH_3152(glpQ) BALH_3778(glpQ) BALH_4870(glpQ)
            BLI: BL00184(glpQ) BL02843 BL02963 BL05263
            BLD: BLi01034(yhdW) BLi02589(yqiK) BLi04156 BLi04254(glpQ)
            BCL: ABC0356 ABC0363 ABC1440 ABC1494
            BAY: RBAM_002600(glpQ) RBAM_009850(yhdW) RBAM_022460(yqiK)
                 RBAM_027510
            BPU: BPUM_0181 BPUM_0910(ugpQ) BPUM_2151(glpQ)
            OIH: OB1855 OB2833
            GKA: GK1814(glpQ) GK2385
            SAU: SA0036 SA0220 SA0820(glpQ) SA0969 SA1542
            SAV: SAV0035(aadD) SAV0039 SAV0228 SAV0959(glpQ) SAV1121 SAV1721
            SAM: MW0029 MW0204 MW0841(glpQ) MW1003 MW1663
            SAR: SAR0037(ugpQ) SAR0220 SAR0921(glpQ) SAR1094 SAR1798
            SAS: SAS0204 SAS0829 SAS1055 SAS1647
            SAC: SACOL0031 SACOL0207 SACOL0962 SACOL1130 SACOL1770
            SAB: SAB0167 SAB0827c(glpQ) SAB0985c SAB1579c
            SAA: SAUSA300_0030 SAUSA300_0222 SAUSA300_0862(glpQ) SAUSA300_1020
                 SAUSA300_1667
            SAO: SAOUHSC_00190 SAOUHSC_00897 SAOUHSC_01071 SAOUHSC_01830
            SAJ: SaurJH9_0027 SaurJH9_0959
            SAH: SaurJH1_0027 SaurJH1_0978
            SEP: SE0655 SE0819 SE1397
            SER: SERP0547 SERP0710 SERP1285 SERP2523
            SHA: SH0089 SH1203 SH1832 SH1991(glpQ)
            SSP: SSP0170 SSP1042 SSP1667 SSP1816
            LMO: lmo0616 lmo1292
            LMF: LMOf2365_0645 LMOf2365_1309
            LIN: lin0625 lin1330
            LWE: lwe0586 lwe1307
            LLA: L1007(yagA) L58914(yuhH)
            LLC: LACR_0053 LACR_2279
            LLM: llmg_0076
            SPY: SPy_0839
            SPZ: M5005_Spy_0647
            SPM: spyM18_0899
            SPG: SpyM3_0566
            SPS: SPs1288
            SPH: MGAS10270_Spy0706
            SPI: MGAS10750_Spy0737
            SPJ: MGAS2096_Spy0715
            SPK: MGAS9429_Spy0703
            SPF: SpyM51160
            SPA: M6_Spy0666
            SPB: M28_Spy0628
            SPN: SP_0994
            SPR: spr0897
            SPD: SPD_0880
            SAN: gbs1293
            SAK: SAK_1307
            SMU: SMU.724
            SSA: SSA_0325(ugpQ) SSA_1649
            LPL: lp_1328(glpQ1) lp_1578(glpQ2) lp_2344(glpQ3) lp_2582(glpQ4)
            LJO: LJ0530
            LAC: LBA0101 LBA0498
            LSA: LSA0243 LSA0583(glpQ)
            LSL: LSL_1601 LSL_1710
            LDB: Ldb1922(glpQ)
            LBR: LVIS_0118 LVIS_0993 LVIS_1267
            LCA: LSEI_1733 LSEI_2760
            PPE: PEPE_0735
            EFA: EF0779 EF1904 EF2163
            OOE: OEOE_0949
            LME: LEUM_1700
            STH: STH2458 STH2737
            CAC: CAC0430 CA_P0015
            CPE: CPE0421(glpQ) CPE1877(glpQ)
            CPF: CPF_0424 CPF_2131
            CPR: CPR_0420(glpQ)
            CTC: CTC00427
            CNO: NT01CX_0196 NT01CX_0833
            CDF: CD1402(glpQ) CD1666
            CBO: CBO2928(glpQ) CBO3212(glpQ)
            CBF: CLI_3350
            AMT: Amet_0561
            TTE: TTE0993(ugpQ)
            MGE: MG_293 MG_385
            MPN: MPN420(glpQ) MPN566(glpQ)
            MPU: MYPU_2630(glpQ)
            MPE: MYPE5750(glpQ)
            MMY: MSC_0145(glpQ)
            MMO: MMOB2050(glpQ)
            MHY: mhp317(glpQ)
            MHJ: MHJ_0295(ugpQ)
            MHP: MHP7448_0303(ugpQ)
            MSY: MS53_0023(glpQ)
            MCP: MCAP_0139
            MTU: Rv0317c(glpQ2) Rv3842c(glpQ1)
            MTC: MT0332 MT3950
            MBO: Mb0325c(glpQ2) Mb3872c(glpQ1)
            MBB: BCG_0357c(glpQ2) BCG_3905c(glpQ1)
            MLE: ML0074(glpQ)
            MPA: MAP0190(glpQ1) MAP0480
            MAV: MAV_0186 MAV_0576
            MSM: MSMEG_6423
            MVA: Mvan_0998
            MGI: Mflv_1140
            MMC: Mmcs_4734 Mmcs_5040
            MKM: Mkms_4820 Mkms_5128
            MJL: Mjls_5119 Mjls_5420
            CGL: NCgl1333(cgl1387) NCgl2807(cgl2907)
            CGB: cg1572(glpQ2) cg3215(glpQ1)
            CEF: CE1518 CE2750
            CDI: DIP2254
            CJK: jk0114(ugpQ) jk0886(glpQ)
            NFA: nfa1250
            RHA: RHA1_ro04024
            SCO: SCO1090(2SCG4.06) SCO1419(SC6D7.20c) SCO1565(SCL11.21c)
                 SCO1968(SC3C9.03) SCO3976(SCBAC25E3.13c) SCO7550(SC5F1.04c)
            SMA: SAV1492(glpQ5) SAV4224(glpQ2) SAV6271(glpQ6) SAV6784(glpQ3)
                 SAV6927(glpQ4)
            LXX: Lxx19750(glpQ)
            CMI: CMM_1682(glpQ2)
            ART: Arth_0320 Arth_0950
            AAU: AAur_0369(glpQ)
            PAC: PPA1224 PPA1839
            TFU: Tfu_0245 Tfu_1757
            FRA: Francci3_2432 Francci3_3758 Francci3_3774
            FAL: FRAAL3448(glpQ) FRAAL5997 FRAAL6018
            KRA: Krad_3613
            SEN: SACE_0126(glpQ1) SACE_2292(glpQ4) SACE_4968(glpQ) SACE_6355
                 SACE_7169(glpQ)
            STP: Strop_2954 Strop_4513
            RXY: Rxyl_0307 Rxyl_1999
            FNU: FN1891 FN1908
            RBA: RB2825(ugpQ)
            TPA: TP0257
            TDE: TDE0799 TDE0957
            LIL: LA0339(glpQ1) LA3980(glpQ2)
            LIC: LIC10293(glpQ) LIC13182(ugpQ)
            LBJ: LBJ_0420(ugpQ) LBJ_2725(glpQ)
            LBL: LBL_0345(glpQ) LBL_2657(ugpQ)
            CYA: CYA_0909
            CYB: CYB_2183
            GVI: glr4378
            ANA: all0275 all1051
            AVA: Ava_3745 Ava_4727
            TER: Tery_1053
            BTH: BT_0550
            BFR: BF2640 BF4444
            BFS: BF2662 BF4242(ugpQ)
            SRU: SRU_0571(glpQ)
            CHU: CHU_1005(ugpQ) CHU_2752(ugpQ)
            GFO: GFO_3193(glpQ) GFO_3635(glpQ)
            CTE: CT0079(ugpQ)
            PLT: Plut_0147
            RRS: RoseRS_4126
            RCA: Rcas_1216
            DRA: DR_0542 DR_2084 DR_B0111
            DGE: Dgeo_1506 Dgeo_2661
            TTJ: TTHB141
            TMA: TM1621
            HAL: VNG1846C
            HMA: rrnAC1917(glpQ2) rrnB0316(glpQ1)
            HWA: HQ2118A(ugpQ) HQ2379A(ugpQ)
            NPH: NP4360A(ugpQ)
            TAC: Ta0634
            TVO: TVN0841
            PTO: PTO0636
            PAB: PAB0180
            PFU: PF2003
            TKO: TK1397 TK1398
            RCI: RCIX2417(glpQ)
            APE: APE_0262
            STO: ST0669
            SAI: Saci_2165
            MSE: Msed_1178
            PAI: PAE1058
            TPE: Tpen_1581
STRUCTURES  PDB: 1O1Z  1T8Q  1V8E  1VD6  1YDY  2DXL  2DXN  2OOG  2P76  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.46
            ExPASy - ENZYME nomenclature database: 3.1.4.46
            ExplorEnz - The Enzyme Database: 3.1.4.46
            ERGO genome analysis and discovery system: 3.1.4.46
            BRENDA, the Enzyme Database: 3.1.4.46
            CAS: 86280-59-3
///
ENTRY       EC 3.1.4.47       Obsolete  Enzyme
NAME        Transferred to 4.6.1.14
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
COMMENT     Transferred entry: now EC 4.6.1.14 glycosylphosphatidylinositol
            diacylglycerol-lyase (EC 3.1.4.47 created 1989, deleted 2002)
GENES       TBR: Tb927.2.6000
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.47
            ExPASy - ENZYME nomenclature database: 3.1.4.47
            ExplorEnz - The Enzyme Database: 3.1.4.47
            ERGO genome analysis and discovery system: 3.1.4.47
            BRENDA, the Enzyme Database: 3.1.4.47
///
ENTRY       EC 3.1.4.48                 Enzyme
NAME        dolichylphosphate-glucose phosphodiesterase;
            dolichol phosphoglucose phosphodiesterase;
            Dol-P-Glc phosphodiesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     dolichyl-beta-D-glucosyl-phosphate dolichylphosphohydrolase
REACTION    dolichyl beta-D-glucosyl phosphate + H2O = dolichyl phosphate +
            D-glucose [RN:R01006]
ALL_REAC    R01006
SUBSTRATE   dolichyl beta-D-glucosyl phosphate [CPD:C01246];
            H2O [CPD:C00001]
PRODUCT     dolichyl phosphate [CPD:C00110];
            D-glucose [CPD:C00031]
REFERENCE   1
  AUTHORS   Crean, E.V.
  TITLE     Synthesis and degradation of dolichyl phosphoryl glucose by the
            cellular slime mold, Dictyostelium discoideum.
  JOURNAL   Biochim. Biophys. Acta 792 (1984) 149-157.
  ORGANISM  Dictyostelium discoideum [GN:ddi]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.48
            ExPASy - ENZYME nomenclature database: 3.1.4.48
            ExplorEnz - The Enzyme Database: 3.1.4.48
            ERGO genome analysis and discovery system: 3.1.4.48
            BRENDA, the Enzyme Database: 3.1.4.48
            CAS: 89287-42-3
///
ENTRY       EC 3.1.4.49                 Enzyme
NAME        dolichylphosphate-mannose phosphodiesterase;
            mannosylphosphodolichol phosphodiesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     dolichyl-beta-D-mannosyl-phosphate dolichylphosphohydrolase
REACTION    dolichyl beta-D-mannosyl phosphate + H2O = dolichyl phosphate +
            D-mannose [RN:R01328]
ALL_REAC    R01328
SUBSTRATE   dolichyl beta-D-mannosyl phosphate [CPD:C04252];
            H2O [CPD:C00001]
PRODUCT     dolichyl phosphate [CPD:C00110];
            D-mannose [CPD:C00159]
REFERENCE   1  [PMID:2826159]
  AUTHORS   Tomita Y, Motokawa Y.
  TITLE     Characterization and partial purification of a novel
            mannosylphosphodolichol phosphodiesterase from chicken liver
            microsomes.
  JOURNAL   Eur. J. Biochem. 170 (1987) 363-8.
  ORGANISM  chicken [GN:gga]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.49
            ExPASy - ENZYME nomenclature database: 3.1.4.49
            ExplorEnz - The Enzyme Database: 3.1.4.49
            ERGO genome analysis and discovery system: 3.1.4.49
            BRENDA, the Enzyme Database: 3.1.4.49
            CAS: 111839-07-7
///
ENTRY       EC 3.1.4.50                 Enzyme
NAME        glycosylphosphatidylinositol phospholipase D;
            GPI-PLD;
            glycoprotein phospholipase D;
            phosphatidylinositol phospholipase D;
            phosphatidylinositol-specific phospholipase D
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     glycoprotein-phosphatidylinositol phosphatidohydrolase
REACTION    6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O =
            6-(alpha-D-glucosaminyl)-1D-myo-inositol + 3-sn-phosphatidate
            [RN:R06623]
ALL_REAC    R06623(G);
            (other) R04149 R07398
SUBSTRATE   6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
            [CPD:C04248];
            H2O [CPD:C00001]
PRODUCT     6-(alpha-D-glucosaminyl)-1D-myo-inositol [CPD:C15658];
            3-sn-phosphatidate [CPD:C00416]
COMMENT     This enzyme is also active when O-4 of the glucosamine is
            substituted by carrying the oligosaccharide that can link a protein
            to the structure. It therefore cleaves proteins from the lipid part
            of the glycosylphosphatidylinositol (GPI) anchors, but does so by
            hydrolysis, whereas glycosylphosphatidylinositol
            diacylglycerol-lyase (EC 4.6.1.14) does so by elimination. It acts
            on plasma membranes only after solubilization of the substrate with
            detergents or solvents, but it may act on intracellular membranes.
REFERENCE   1  [PMID:3422494]
  AUTHORS   Low MG, Prasad AR.
  TITLE     A phospholipase D specific for the phosphatidylinositol anchor of
            cell-surface proteins is abundant in plasma.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 980-4.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:3028377]
  AUTHORS   Malik AS, Low MG.
  TITLE     Conversion of human placental alkaline phosphatase from a high Mr
            form to a low Mr form during butanol extraction. An investigation of
            the role of endogenous phosphoinositide-specific phospholipases.
  JOURNAL   Biochem. J. 240 (1986) 519-27.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:7961859]
  AUTHORS   Li JY, Hollfelder K, Huang KS, Low MG.
  TITLE     Structural features of GPI-specific phospholipase D revealed by
            proteolytic fragmentation and Ca2+ binding studies.
  JOURNAL   J. Biol. Chem. 269 (1994) 28963-71.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:11254757]
  AUTHORS   Deeg MA, Bierman EL, Cheung MC.
  TITLE     GPI-specific phospholipase D associates with an apoA-I- and
            apoA-IV-containing complex.
  JOURNAL   J. Lipid. Res. 42 (2001) 442-51.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00563  Glycosylphosphatidylinositol(GPI)-anchor
                            biosynthesis
ORTHOLOGY   KO: K01127  glycosylphosphatidylinositol phospholipase D
GENES       HSA: 2822(GPLD1)
            PTR: 462473(GPLD1)
            MMU: 14756(Gpld1)
            RNO: 291132(Gpld1)
            CFA: 478735(GPLD1)
            BTA: 287025(GPLD1)
            GGA: 420819(GPLD1)
            SPU: 754425(LOC754425)
            DDI: DDB_0229914(pldG)
            NOC: Noc_2092 Noc_2093
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.50
            ExPASy - ENZYME nomenclature database: 3.1.4.50
            ExplorEnz - The Enzyme Database: 3.1.4.50
            ERGO genome analysis and discovery system: 3.1.4.50
            BRENDA, the Enzyme Database: 3.1.4.50
            CAS: 113756-14-2
///
ENTRY       EC 3.1.4.51                 Enzyme
NAME        glucose-1-phospho-D-mannosylglycoprotein phosphodiesterase;
            alpha-glucose-1-phosphate phosphodiesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-diester hydrolases
SYSNAME     6-(D-glucose-1-phospho)-D-mannosylglycoprotein
            glucose-1-phosphohydrolase
REACTION    6-(D-glucose-1-phospho)-D-mannosylglycoprotein + H2O =
            alpha-D-glucose 1-phosphate + D-mannosylglycoprotein [RN:R04180]
ALL_REAC    R04180
SUBSTRATE   6-(D-glucose-1-phospho)-D-mannosylglycoprotein [CPD:C04645];
            H2O [CPD:C00001]
PRODUCT     alpha-D-glucose 1-phosphate [CPD:C00103];
            D-mannosylglycoprotein [CPD:C03268]
COMMENT     The enzyme is specific for the product of EC 2.7.8.19
            UDP-glucose---glycoprotein glucose phosphotransferase.
REFERENCE   1  [PMID:2555363]
  AUTHORS   Srisomsap C, Richardson KL, Jay JC, Marchase RB.
  TITLE     An alpha-glucose-1-phosphate phosphodiesterase is present in rat
            liver cytosol.
  JOURNAL   J. Biol. Chem. 264 (1989) 20540-6.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.4.51
            ExPASy - ENZYME nomenclature database: 3.1.4.51
            ExplorEnz - The Enzyme Database: 3.1.4.51
            ERGO genome analysis and discovery system: 3.1.4.51
            BRENDA, the Enzyme Database: 3.1.4.51
            CAS: 123940-44-3
///
ENTRY       EC 3.1.4.-                  Enzyme
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric diester hydrolases
REACTION    (1) N-Acetyl-D-mannosamine + UDP <=> UDP-N-acetyl-D-mannosamine +
            H2O [RN:R02707];
            (2) 1-(1-Alkenyl)-sn-glycero-3-phosphoethanolamine + H2O <=>
            1-(1-Alkenyl)-sn-glycerol + Ethanolamine phosphate [RN:R07380]
SUBSTRATE   N-Acetyl-D-mannosamine [CPD:C00645];
            UDP [CPD:C00015];
            1-(1-Alkenyl)-sn-glycero-3-phosphoethanolamine [CPD:C04635];
            H2O [CPD:C00001]
PRODUCT     UDP-N-acetyl-D-mannosamine [CPD:C01170];
            H2O [CPD:C00001];
            1-(1-Alkenyl)-sn-glycerol [CPD:C15645];
            Ethanolamine phosphate [CPD:C00346]
///
ENTRY       EC 3.1.5.1                  Enzyme
NAME        dGTPase;
            deoxy-GTPase;
            deoxyguanosine 5-triphosphate triphosphohydrolase;
            deoxyguanosine triphosphatase;
            deoxyguanosine triphosphate triphosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Triphosphoric-monoester hydrolases
SYSNAME     dGTP triphosphohydrolase
REACTION    dGTP + H2O = deoxyguanosine + triphosphate [RN:R01856]
ALL_REAC    R01856
SUBSTRATE   dGTP [CPD:C00286];
            H2O [CPD:C00001]
PRODUCT     deoxyguanosine [CPD:C00330];
            triphosphate [CPD:C00536]
COMMENT     Also acts on GTP.
REFERENCE   1  [PMID:13563461]
  AUTHORS   KORNBERG SR, LEHMAN IR, BESSMAN MJ, SIMMS ES, KORNBERG A.
  TITLE     Enzymatic cleavage of deoxyguanosine triphosphate to deoxyguanosine
            and tripolyphosphate.
  JOURNAL   J. Biol. Chem. 233 (1958) 159-62.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01129  dGTPase
GENES       ANG: An14g00010(srgA)
            ECO: b0160(dgt)
            ECJ: JW0156(dgt)
            ECE: Z0171(dgt)
            ECS: ECs0164
            ECC: c0196(dgt)
            ECI: UTI89_C0176(dgt)
            ECP: ECP_0170
            ECV: APECO1_1825(dgt)
            ECW: EcE24377A_0165(dgt)
            ECX: EcHS_A0164
            STY: STY0230(dgt)
            STT: t0209(dgt)
            SPT: SPA0214(dgt)
            SEC: SC0208(dgt)
            STM: STM0208(dgt)
            YPE: YPO3383(dgt)
            YPK: y0806(dgt)
            YPM: YP_0302(dgt)
            YPA: YPA_2882
            YPN: YPN_0708
            YPP: YPDSF_2975
            YPS: YPTB0748(dgt)
            YEN: YE0740(dgt)
            SFL: SF0152(dgt)
            SFX: S0155(dgt)
            SFV: SFV_0145(dgt)
            SBO: SBO_0149(dgt)
            ECA: ECA3302(dgt)
            PLU: plu0907(dgt)
            SGL: SG0504
            ENT: Ent638_0700
            SPE: Spro_0788
            HIT: NTHI1825
            HSO: HS_0964(dgt)
            PMU: PM0878
            MSU: MS1269(dgt)
            APL: APL_0313
            XOO: XOO4247(dgt)
            VCH: VC1979
            VCO: VC0395_A1566(dgt)
            VVU: VV1_0014
            VVY: VV1112
            VPA: VP0925
            VFI: VF1682
            PPR: PBPRA2536 PBPRA2628
            PAE: PA1124(dgt) PA3043
            PAU: PA14_24730 PA14_49840(dgt)
            PAP: PSPA7_4245(dgt)
            PPU: PP_2102
            PPF: Pput_3637
            PST: PSPTO_2331
            PSB: Psyr_2116
            PSP: PSPPH_2088
            PFL: PFL_4235
            PFO: Pfl_3973
            PEN: PSEEN3766(dgt)
            PMY: Pmen_3004
            PAR: Psyc_0893(dgt)
            PCR: Pcryo_1525
            PRW: PsycPRwf_1911
            ACI: ACIAD2613(dgt)
            ACB: A1S_2586
            SON: SO_2485
            SDN: Sden_1995
            SFR: Sfri_1905
            SAZ: Sama_1695
            SBL: Sbal_2237
            SLO: Shew_1912
            SPC: Sputcn32_1870
            SPL: Spea_2917
            SHE: Shewmr4_2042
            SHM: Shewmr7_1933
            SHN: Shewana3_2147
            SHW: Sputw3181_2138
            ILO: IL0741
            CPS: CPS_2110
            PHA: PSHAa1274(dgt) PSHAb0109(dgt)
            PAT: Patl_2015 Patl_3793
            PIN: Ping_1412
            LPN: lpg1080 lpg1877
            LPF: lpl1839
            LPP: lpp1842
            FTU: FTT0720c(dgt)
            FTF: FTF0720c(dgt)
            FTW: FTW_1519(dgt)
            FTL: FTL_1503
            FTH: FTH_1457(dgt)
            FTN: FTN_0632
            TCX: Tcr_1079
            AEH: Mlg_1929
            HCH: HCH_06393
            CSA: Csal_0252
            ABO: ABO_2640(dgt)
            AHA: AHA_0906
            DNO: DNO_0254(dgt)
            CVI: CV_3210(dgt)
            RSO: RSc2968(dgt)
            REU: Reut_A2939(dgt) Reut_A3128
            REH: H16_A3433(dgt)
            RME: Rmet_3265
            BMA: BMA2745
            BXE: Bxe_A0361
            BVI: Bcep1808_0261 Bcep1808_0376
            BUR: Bcep18194_A3491
            BCN: Bcen_2713
            BCH: Bcen2424_0394
            BAM: Bamb_0313
            BPS: BPSL3167
            BPM: BURPS1710b_3727(dgt)
            BTE: BTH_I3022
            BPE: BP3658
            BPA: BPP0073
            BBR: BB0073
            RFR: Rfer_2927
            POL: Bpro_0788
            MPT: Mpe_A3106
            HAR: HEAR3119(dgt)
            MMS: mma_3362
            NEU: NE1982(dgt)
            NET: Neut_0380
            NMU: Nmul_A0704
            EBA: ebA2254(dgt1)
            AZO: azo0933(hflX1)
            DAR: Daro_1938
            TBD: Tbd_0316
            MFA: Mfla_0177 Mfla_2454
            WSU: WS0299 WS2052
            TDN: Tmden_0021 Tmden_0745
            ABU: Abu_1070(dgt)
            NIS: NIS_1853(dgt)
            SUN: SUN_0043
            GSU: GSU1246
            GME: Gmet_1762
            PCA: Pcar_1638
            DPS: DP1797
            ADE: Adeh_2590 Adeh_3864
            MXA: MXAN_5163
            SAT: SYN_01066
            SFU: Sfum_0190
            RPR: RP064
            RTY: RT0068(dgtP)
            RCO: RC0094(dgtP)
            RFE: RF_0110(dgt)
            RBE: RBE_1301(dgt)
            WOL: WD0709
            WBM: Wbm0025
            ERU: Erum3740
            ERW: ERWE_CDS_03860
            ERG: ERGA_CDS_03820
            ECN: Ecaj_0364
            ECH: ECH_0688
            NSE: NSE_0460
            PUB: SAR11_0969(dgtP)
            MLO: mll1093 mlr6429
            MES: Meso_1814
            SME: SMc02074
            ATU: Atu1712(dgt)
            ATC: AGR_C_3147
            RET: RHE_CH01817(dgt)
            RLE: RL2040(dgt)
            BME: BMEI1090
            BMF: BAB1_0895(dgt)
            BMS: BR0876(dgt)
            BMB: BruAb1_0888(dgt)
            BOV: BOV_0867(dgt)
            BJA: bll4758(dgt)
            BRA: BRADO4053
            BBT: BBta_4424
            RPA: RPA2855
            RPB: RPB_2751
            RPC: RPC_2507
            RPD: RPD_2796
            RPE: RPE_2630
            NWI: Nwi_1808
            NHA: Nham_1757
            BHE: BH09970(dgt)
            BQU: BQ07690(dgt)
            BBK: BARBAKC583_0750
            CCR: CC_2008
            SIL: SPO2505
            SIT: TM1040_0145 TM1040_0902
            RSP: RSP_1621 RSP_2659(dgt) RSP_3644
            JAN: Jann_1505
            RDE: RD1_3167
            PDE: Pden_0927
            MMR: Mmar10_1914
            HNE: HNE_2050
            ZMO: ZMO0842(dgtP) ZMO1485
            NAR: Saro_1848
            SAL: Sala_1873
            ELI: ELI_02380
            GOX: GOX1752
            GBE: GbCGDNIH1_1261
            RRU: Rru_A1780
            MGM: Mmc1_3548
            ABA: Acid345_0225 Acid345_4602
            LMO: lmo2657
            LMF: LMOf2365_2636(dgt)
            LIN: lin2806
            LWE: lwe2606(dgt)
            EFA: EF1958
            CPE: CPE2009(dgtP)
            CPF: CPF_2266
            CPR: CPR_1977
            CTC: CTC02012
            CHY: CHY_0453
            DSY: DSY3050 DSY3289
            SWO: Swol_1509
            TTE: TTE1757(dgt)
            MTA: Moth_0622
            MTU: Rv2344c(dgt)
            MTC: MT2409
            MBO: Mb2373c(dgt)
            MBB: BCG_2367c(dgt)
            MLE: ML0831(dgt)
            MPA: MAP2132c(dgt)
            MSM: MSMEG_4483
            MUL: MUL_1458(dgt)
            MVA: Mvan_3815
            MMC: Mmcs_3443
            CGL: NCgl2193(cgl2273)
            CGB: cg2494(dgt)
            CEF: CE2173
            CDI: DIP1703
            CJK: jk0619(dgt)
            NFA: nfa14690(dgt)
            RHA: RHA1_ro01216
            SCO: SCO2470(SC7A8.09c)
            SMA: SAV5674(dgt)
            TWH: TWT287(dgt)
            TWS: TW485(dgt)
            LXX: Lxx08500(dgt)
            CMI: CMM_1585(dgtA)
            ART: Arth_1337
            AAU: AAur_1487
            PAC: PPA0955
            NCA: Noca_1945
            TFU: Tfu_0865
            FRA: Francci3_1281
            FAL: FRAAL2024
            ACE: Acel_0802
            SEN: SACE_1502(dgt) SACE_2185
            STP: Strop_3428
            BLO: BL1148(dgt)
            BAD: BAD_0497
            RXY: Rxyl_1503
            RBA: RB284(dgt)
            PCU: pc0465(dgt)
            LIL: LA2274
            LIC: LIC11663(dgt)
            LBJ: LBJ_1337(dgt)
            LBL: LBL_1562(dgt)
            SYN: sll0398(dgt)
            BTH: BT_3460
            BFR: BF0323
            BFS: BF0271(dgt)
            PGI: PG2003(dgt)
            CHU: CHU_2101(dgt)
            GFO: GFO_3472(dgt)
            FJO: Fjoh_1521
            FPS: FP0282(dgt)
            DET: DET0553
            DEH: cbdb_A1195 cbdb_A528
            DRA: DR_1006 DR_1808
            DGE: Dgeo_1804
            TTH: TTC0044
            TTJ: TTHA0412
            RCI: LRC530(dgt)
STRUCTURES  PDB: 1HA3  2C77  2C78  2DQB  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.5.1
            ExPASy - ENZYME nomenclature database: 3.1.5.1
            ExplorEnz - The Enzyme Database: 3.1.5.1
            ERGO genome analysis and discovery system: 3.1.5.1
            BRENDA, the Enzyme Database: 3.1.5.1
            CAS: 9025-63-2
///
ENTRY       EC 3.1.6.1                  Enzyme
NAME        arylsulfatase;
            sulfatase;
            nitrocatechol sulfatase;
            phenolsulfatase;
            phenylsulfatase;
            p-nitrophenyl sulfatase;
            arylsulfohydrolase;
            4-methylumbelliferyl sulfatase;
            estrogen sulfatase;
            arylsulfatase C;
            arylsulfatase B;
            arylsulfatase A
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     aryl-sulfate sulfohydrolase
REACTION    a phenol sulfate + H2O = a phenol + sulfate [RN:R01243]
ALL_REAC    R01243 > R03980;
            (other) R04856 R06280(G)
SUBSTRATE   phenol sulfate [CPD:C02180];
            H2O [CPD:C00001]
PRODUCT     phenol [CPD:C00146];
            sulfate [CPD:C00059]
COMMENT     A group of enzymes with rather similar specificities.
REFERENCE   1  [PMID:13363831]
  AUTHORS   DODGSON KS, SPENCER B, WILLIAMS K.
  TITLE     Studies on sulphatases.  13.  The hydrolysis of substituted phenyl
            sulphates by the arylsulphatase of Alcaligenes metalcaligenes.
  JOURNAL   Biochem. J. 64 (1956) 216-21.
  ORGANISM  Alcaligenes metacaligenes
REFERENCE   2
  AUTHORS   Roy, A.B.
  TITLE     The synthesis and hydrolysis of sulfate esters.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 22 (1960) 205-235.
REFERENCE   3  [PMID:13772]
  AUTHORS   Roy AB.
  TITLE     Sulphatases, lysosomes and disease.
  JOURNAL   Aust. J. Exp. Biol. Med. Sci. 54 (1976) 111-35.
  ORGANISM  cow [GN:bta], pig [GN:ssc], human [GN:hsa]
REFERENCE   4
  AUTHORS   Webb, E.C. and Morrow, P.F.W.
  TITLE     The activation of an arysulphatase from ox liver by chloride and
            other anions.
  JOURNAL   Biochem. J. 73 (1959) 7-15.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00150  Androgen and estrogen metabolism
            PATH: map00600  Sphingolipid metabolism
ORTHOLOGY   KO: K01130  arylsulfatase
GENES       HSA: 414(ARSD) 415(ARSE)
            CFA: 491718(ARSD) 491719(ARSE)
            GGA: 418658(ARSD)
            SPO: SPBPB10D8.02c
            ANI: AN6847.2
            AFM: AFUA_5G12940 AFUA_8G02520
            AOR: AO090120000416
            CNE: CNC06820
            UMA: UM05068.1
            ECO: b3801(aslA)
            ECJ: JW3773(aslA)
            ECE: Z5314(aslA)
            ECS: ECs4731
            ECC: c4719(aslA)
            ECI: UTI89_C4359(aslA)
            ECP: ECP_3993
            SEC: SC3062(ars)
            STM: STM3122
            SDY: SDY_3945(aslA)
            VVU: VV2_0149 VV2_0151
            VVY: VVA0659 VVA0661
            VPA: VPA0600(atsD) VPA0680 VPA0683
            VFI: VF1427 VF1428 VF1430 VFA0899 VFA0992
            PAE: PA0183(atsA)
            PAU: PA14_02310(atsA)
            PAP: PSPA7_2624 PSPA7_3903
            PPU: PP_3352
            PFL: PFL_0205 PFL_2842
            PFO: Pfl_0208
            ACI: ACIAD1598(atsA)
            SHE: Shewmr4_2074
            SHM: Shewmr7_1901
            CPS: CPS_0660 CPS_0841(atsA) CPS_2983 CPS_2984 CPS_2985 CPS_3032
            PAT: Patl_0870
            FTU: FTT0783(ars)
            FTF: FTF0783(ars)
            REU: Reut_A2893 Reut_B4569
            REH: H16_B0315 H16_B0483
            RME: Rmet_5416 Rmet_5423
            BXE: Bxe_A2132
            BUR: Bcep18194_B2584
            BCH: Bcen2424_3543
            BPE: BP1635
            BPA: BPP2750
            BBR: BB2736
            MPT: Mpe_A2680
            MMS: mma_2412 mma_2424 mma_2430
            SUN: SUN_1413 SUN_2381
            MXA: MXAN_6507
            MLO: mll5471
            SME: SMa0943 SMb20915(aslA1)
            RLE: RL1149 RL1237 RL1238 RL1911 RL1918 RL2264 RL2267
            BJA: bll5074(arsA)
            BBT: BBta_0599 BBta_3535
            SIL: SPO3286(atsA)
            RDE: RD1_0531 RD1_3744
            MTU: Rv0663(atsD) Rv3299c(atsB)
            MTC: MT0692 MT0738(atsA) MT3398
            MBO: Mb0682(atsD) Mb0731(atsAa) Mb0732(atsAb) Mb3327c(atsB)
            MBB: BCG_0712(atsD) BCG_0761(atsA) BCG_3328c(atsB)
                 BCG_3364c(atsB_2)
            MAV: MAV_2989
            MSM: MSMEG_1451
            MMC: Mmcs_1023 Mmcs_3964 Mmcs_4113
            CGL: NCgl2422(cgl2508)
            CEF: CE1568
            RHA: RHA1_ro02004 RHA1_ro03308 RHA1_ro04570 RHA1_ro05958
            SEN: SACE_3101(atsD) SACE_4314
            RBA: RB11116(aslA) RB1477(atsA) RB1610(aslA) RB1736 RB2367
                 RB3876(arsA) RB3877(aslA) RB607 RB684 RB686 RB7772(atsA)
                 RB9498(arsA) RB9530(aslA)
            AVA: Ava_0111
            PMT: PMT1515
            PMF: P9303_04271
            BTH: BT_3093
            BFR: BF0017
            BFS: BF0016
            MAC: MA2648(atsA)
            MBA: Mbar_A3081
            MMA: MM_1892
            HWA: HQ2428A(aslA) HQ2690A(aslA) HQ3203A(aslA) HQ3464A(aslA)
                 HQ3540A(aslA) HQ3543A
            NPH: NP0946A
            RCI: RCIX63(atsA)
STRUCTURES  PDB: 1HDH  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.1
            ExPASy - ENZYME nomenclature database: 3.1.6.1
            ExplorEnz - The Enzyme Database: 3.1.6.1
            ERGO genome analysis and discovery system: 3.1.6.1
            BRENDA, the Enzyme Database: 3.1.6.1
            CAS: 9016-17-5
///
ENTRY       EC 3.1.6.2                  Enzyme
NAME        steryl-sulfatase;
            arylsulfatase;
            steroid sulfatase;
            sterol sulfatase;
            dehydroepiandrosterone sulfate sulfatase;
            arylsulfatase C;
            steroid 3-sulfatase;
            steroid sulfate sulfohydrolase;
            dehydroepiandrosterone sulfatase;
            pregnenolone sulfatase;
            phenolic steroid sulfatase;
            3-beta-hydroxysteroid sulfate sulfatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     steryl-sulfate sulfohydrolase
REACTION    3beta-hydroxyandrost-5-en-17-one 3-sulfate + H2O =
            3beta-hydroxyandrost-5-en-17-one + sulfate [RN:R03404]
ALL_REAC    R03404
SUBSTRATE   3beta-hydroxyandrost-5-en-17-one 3-sulfate [CPD:C04555];
            H2O [CPD:C00001]
PRODUCT     3beta-hydroxyandrost-5-en-17-one [CPD:C01227];
            sulfate [CPD:C00059]
COMMENT     Also acts on some related steryl sulfates.
REFERENCE   1  [PMID:13208702]
  AUTHORS   ROY AB.
  TITLE     The steroid sulphatase of Patella vulgata.
  JOURNAL   Biochim. Biophys. Acta. 15 (1954) 300-1.
  ORGANISM  Patella vlugata
REFERENCE   2
  AUTHORS   Roy, A.B.
  TITLE     The synthesis and hydrolysis of sulfate esters.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 22 (1960) 205-235.
REFERENCE   3
  AUTHORS   Stitch, S.R., Halkerston, I.D.K. and Hillman, J.
  TITLE     The enzymic hydrolysis of steroid conjugates. 1. Sulphatase and
            beta-glucuronidase activity of molluscan extracts.
  JOURNAL   Biochem. J. 63 (1965) 705-710.
  ORGANISM  Patella vlugata
PATHWAY     PATH: map00150  Androgen and estrogen metabolism
ORTHOLOGY   KO: K01131  steryl-sulfatase
GENES       HSA: 412(STS)
            PTR: 465478(STS)
            MMU: 20905(Sts)
            RNO: 24800(Sts)
            CFA: 491727(STS)
            BTA: 509206(STS)
            GGA: 418654(STS)
            SPU: 591748(LOC591748)
            BUR: Bcep18194_B0483
            PLA: Plav_0360
STRUCTURES  PDB: 1P49  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.2
            ExPASy - ENZYME nomenclature database: 3.1.6.2
            ExplorEnz - The Enzyme Database: 3.1.6.2
            ERGO genome analysis and discovery system: 3.1.6.2
            BRENDA, the Enzyme Database: 3.1.6.2
            CAS: 9025-62-1
///
ENTRY       EC 3.1.6.3                  Enzyme
NAME        glycosulfatase;
            glucosulfatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     sugar-sulfate sulfohydrolase
REACTION    D-glucose 6-sulfate + H2O = D-glucose + sulfate [RN:R00534]
ALL_REAC    R00534 > R01601 R01789
SUBSTRATE   D-glucose 6-sulfate [CPD:C02827];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031];
            sulfate [CPD:C00059]
COMMENT     Also acts on other sulfates of monosaccharides and disaccharides and
            on adenosine 5'-sulfate.
REFERENCE   1
  AUTHORS   Dodgson, K.S.
  TITLE     Glycosulphatase: observations on the activity of partially purified
            preparations towards the sulphate esters of certain monosaccharides
            and steroids.
  JOURNAL   Biochem. J. 78 (1961) 324-333.
  ORGANISM  Patella vulgata, Littorina littorea
REFERENCE   2
  AUTHORS   Egami, F. and Takahaski, N.
  TITLE     Syntheses of adenosinesulfuric acids.
  JOURNAL   Bull. Chem. Soc. Jpn. 28 (1955) 666-668.
REFERENCE   3
  AUTHORS   Roy, A.B.
  TITLE     The synthesis and hydrolysis of sulfate esters.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 22 (1960) 205-235.
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.3
            ExPASy - ENZYME nomenclature database: 3.1.6.3
            ExplorEnz - The Enzyme Database: 3.1.6.3
            ERGO genome analysis and discovery system: 3.1.6.3
            BRENDA, the Enzyme Database: 3.1.6.3
            CAS: 9025-61-0
///
ENTRY       EC 3.1.6.4                  Enzyme
NAME        N-acetylgalactosamine-6-sulfatase;
            chondroitin sulfatase;
            chondroitinase;
            galactose-6-sulfate sulfatase;
            acetylgalactosamine 6-sulfatase;
            N-acetylgalactosamine-6-sulfate sulfatase;
            N-acetylgalactosamine 6-sulfatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     N-acetyl-D-galactosamine-6-sulfate 6-sulfohydrolase
REACTION    Hydrolysis of the 6-sulfate groups of the N-acetyl-D-galactosamine
            6-sulfate units of chondroitin sulfate and of the D-galactose
            6-sulfate units of keratan sulfate [RN:R07806]
ALL_REAC    R07806(G)
REFERENCE   1  [PMID:6939689]
  AUTHORS   Epstein EH Jr, Leventhal ME.
  TITLE     Steroid sulfatase of human leukocytes and epidermis and the
            diagnosis of recessive X-linked ichthyosis.
  JOURNAL   J. Clin. Invest. 67 (1981) 1257-62.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:6213226]
  AUTHORS   Glossl J, Kresse H.
  TITLE     Impaired degradation of keratan sulphate by Morquio A fibroblasts.
  JOURNAL   Biochem. J. 203 (1982) 335-8.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:7213753]
  AUTHORS   Lim CT, Horwitz AL.
  TITLE     Purification and properties of human N-acetylgalactosamine-6-sulfate
            sulfatase.
  JOURNAL   Biochim. Biophys. Acta. 657 (1981) 344-55.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:6814909]
  AUTHORS   Sorensen SH, Noren O, Sjostrom H, Danielsen EM.
  TITLE     Amphiphilic pig intestinal microvillus maltase/glucoamylase.
            Structure and specificity.
  JOURNAL   Eur. J. Biochem. 126 (1982) 559-68.
  ORGANISM  pig [GN:ssc]
REFERENCE   5  [PMID:6809361]
  AUTHORS   Yutaka T, Okada S, Kato T, Inui K, Yabuuhi H.
  TITLE     Galactose 6-sulfate sulfatase activity in Morquio syndrome.
  JOURNAL   Clin. Chim. Acta. 122 (1982) 169-80.
  ORGANISM  shark
PATHWAY     PATH: map00531  Glycosaminoglycan degradation
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01132  N-acetylgalactosamine-6-sulfatase
GENES       HSA: 2588(GALNS)
            MMU: 50917(Galns)
            CFA: 489661(GALNS)
            SSC: 397000(GALNS)
            GGA: 415848(GALNS)
            XLA: 495239(LOC495239)
            SPU: 579130(LOC579130)
            RBA: RB11123(aslA) RB1456 RB4787 RB7560(GALNS) RB7879(GALNS)
            AVA: Ava_4240
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.4
            ExPASy - ENZYME nomenclature database: 3.1.6.4
            ExplorEnz - The Enzyme Database: 3.1.6.4
            ERGO genome analysis and discovery system: 3.1.6.4
            BRENDA, the Enzyme Database: 3.1.6.4
            CAS: 9025-60-9
///
ENTRY       EC 3.1.6.5        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
COMMENT     Deleted entry: sinigrin sulfohydrolase; myrosulfatase (EC 3.1.6.5
            created 1961, deleted 1964)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.5
            ExPASy - ENZYME nomenclature database: 3.1.6.5
            ExplorEnz - The Enzyme Database: 3.1.6.5
            ERGO genome analysis and discovery system: 3.1.6.5
            BRENDA, the Enzyme Database: 3.1.6.5
///
ENTRY       EC 3.1.6.6                  Enzyme
NAME        choline-sulfatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     choline-sulfate sulfohydrolase
REACTION    choline sulfate + H2O = choline + sulfate [RN:R01028]
ALL_REAC    R01028
SUBSTRATE   choline sulfate [CPD:C00919];
            H2O [CPD:C00001]
PRODUCT     choline [CPD:C00114];
            sulfate [CPD:C00059]
REFERENCE   1
  AUTHORS   Takebe, I.
  TITLE     Isolation and characterization of a new enzyme choline sulfatase.
  JOURNAL   J. Biochem. (Tokyo) 50 (1961) 245-255.
  ORGANISM  Pseudomonas nitroreducens
ORTHOLOGY   KO: K01133  choline-sulfatase
GENES       ANI: AN5449.2
            AFM: AFUA_6G13440
            AOR: AO090003000469
            PAE: PA0031(betC)
            PAU: PA14_00380(betC)
            PAP: PSPA7_0032(betC)
            PPU: PP_0077(betC)
            PST: PSPTO_0165
            PSB: Psyr_0029
            PSP: PSPPH_0030(betC)
            PFL: PFL_0031(betC)
            PFO: Pfl_0026
            PEN: PSEEN0034(betC)
            NOC: Noc_0194
            REU: Reut_B5764
            BMA: BMAA0484(betC)
            BMV: BMASAVP1_0697(betC)
            BML: BMA10299_0993(betC)
            BMN: BMA10247_A1966(betC)
            BXE: Bxe_B1573
            BUR: Bcep18194_B0587 Bcep18194_B2021
            BCN: Bcen_3296
            BCH: Bcen2424_5072
            BAM: Bamb_4484
            BPS: BPSS0560
            BPM: BURPS1710b_A2121(betC)
            BPL: BURPS1106A_A0753
            BPD: BURPS668_A0841
            BTE: BTH_II1855
            BPA: BPP0475
            BBR: BB0475
            MLO: mll7612
            SME: SMc00127(betC)
            ATU: Atu4648(betC)
            ATC: AGR_L_469
            RET: RHE_PE00324(betC)
            RLE: pRL110429(betC)
            BME: BMEII0110
            SIL: SPO1083(betC-1) SPO2214(betC-2)
            SIT: TM1040_3133
            RSP: RSP_0594
            RDE: RD1_2022(betC-1)
            RBA: RB6781
            HWA: HQ3464A(aslA)
            NPH: NP0946A
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.6
            ExPASy - ENZYME nomenclature database: 3.1.6.6
            ExplorEnz - The Enzyme Database: 3.1.6.6
            ERGO genome analysis and discovery system: 3.1.6.6
            BRENDA, the Enzyme Database: 3.1.6.6
            CAS: 9025-59-6
///
ENTRY       EC 3.1.6.7                  Enzyme
NAME        cellulose-polysulfatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     cellulose-sulfate sulfohydrolase
REACTION    Hydrolysis of the 2- and 3-sulfate groups of the polysulfates of
            cellulose and charonin
REFERENCE   1
  AUTHORS   Takahashi, N. and Egami, F.
  TITLE     Hydrolysis of polysaccharide sulphate esters by a sulphatase
            preparation from Charonia lampas.
  JOURNAL   Biochem. J. 80 (1961) 384-386.
  ORGANISM  Charonia lampas
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.7
            ExPASy - ENZYME nomenclature database: 3.1.6.7
            ExplorEnz - The Enzyme Database: 3.1.6.7
            ERGO genome analysis and discovery system: 3.1.6.7
            BRENDA, the Enzyme Database: 3.1.6.7
            CAS: 9025-58-5
///
ENTRY       EC 3.1.6.8                  Enzyme
NAME        cerebroside-sulfatase;
            arylsulfatase A;
            cerebroside sulfate sulfatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     cerebroside-3-sulfate 3-sulfohydrolase
REACTION    a cerebroside 3-sulfate + H2O = a cerebroside + sulfate [RN:R04856
            R06280]
ALL_REAC    R04856 R06280(G)
SUBSTRATE   cerebroside 3-sulfate [CPD:C06125];
            H2O [CPD:C00001]
PRODUCT     cerebroside [CPD:C02686];
            sulfate [CPD:C00059]
COMMENT     Hydrolyses galactose-3-sulfate residues in a number of lipids. Also
            hydrolyses ascorbate 2-sulfate and many phenol sulfates.
REFERENCE   1  [PMID:5829234]
  AUTHORS   Mehl E, Jatzkewitz H.
  TITLE     [A cerebrosidesulfatase from swine kidney]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 339 (1964) 260-76.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:13772]
  AUTHORS   Roy AB.
  TITLE     Sulphatases, lysosomes and disease.
  JOURNAL   Aust. J. Exp. Biol. Med. Sci. 54 (1976) 111-35.
  ORGANISM  pig [GN:ssc], human [GN:hsa]
PATHWAY     PATH: map00600  Sphingolipid metabolism
ORTHOLOGY   KO: K01134  arylsulfatase A
GENES       HSA: 410(ARSA)
            MMU: 11883(Arsa)
            CFA: 474457(ARSA)
            SSC: 396973(AS-A)
            GGA: 426863(ARSA)
            SPU: 574839(LOC574839)
            NOC: Noc_0740
            SME: SMa1683
            RLE: pRL110221
            RBA: RB10116(arsA) RB12325 RB12432 RB409 RB4784(aslA) RB4815
                 RB6873 RB6956 RB7481(arsA) RB7995(arsA) RB8078(arsA)
                 RB9192(arsA) RB9755(arsA)
            HMA: rrnAC0858
STRUCTURES  PDB: 1AUK  1E1Z  1E2S  1E33  1E3C  1N2K  1N2L  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.8
            ExPASy - ENZYME nomenclature database: 3.1.6.8
            ExplorEnz - The Enzyme Database: 3.1.6.8
            ERGO genome analysis and discovery system: 3.1.6.8
            BRENDA, the Enzyme Database: 3.1.6.8
            CAS: 9068-68-2
///
ENTRY       EC 3.1.6.9                  Enzyme
NAME        chondro-4-sulfatase;
            chondroitin-4-sulfatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine-4-su
            lfate 4-sulfohydrolase
REACTION    4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine
            4-sulfate + H2O =
            4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine +
            sulfate [RN:R03517]
ALL_REAC    R03517
SUBSTRATE   4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine
            4-sulfate [CPD:C04864];
            H2O [CPD:C00001]
PRODUCT     4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine
            [CPD:C01310];
            sulfate [CPD:C00059]
COMMENT     Also acts on the saturated analogue but not on higher
            oligosaccharides, nor any 6-sulfates.
REFERENCE   1  [PMID:5595107]
  AUTHORS   Held E, Buddecke E.
  TITLE     [Studies on the chemistry of the arterial wall, XI. Demonstration,
            purification and properties of a chondroitin-4-sulfatase from bovine
            aorta]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 348 (1967) 1047-60.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:13772]
  AUTHORS   Roy AB.
  TITLE     Sulphatases, lysosomes and disease.
  JOURNAL   Aust. J. Exp. Biol. Med. Sci. 54 (1976) 111-35.
REFERENCE   3  [PMID:5647268]
  AUTHORS   Yamagata T, Saito H, Habuchi O, Suzuki S.
  TITLE     Purification and properties of bacterial chondroitinases and
            chondrosulfatases.
  JOURNAL   J. Biol. Chem. 243 (1968) 1523-35.
  ORGANISM  Proteus vulgaris
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.9
            ExPASy - ENZYME nomenclature database: 3.1.6.9
            ExplorEnz - The Enzyme Database: 3.1.6.9
            ERGO genome analysis and discovery system: 3.1.6.9
            BRENDA, the Enzyme Database: 3.1.6.9
            CAS: 9045-75-4
///
ENTRY       EC 3.1.6.10                 Enzyme
NAME        chondro-6-sulfatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine-6-su
            lfate 6-sulfohydrolase
REACTION    4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine
            6-sulfate + H2O =
            4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine +
            sulfate [RN:R03518]
ALL_REAC    R03518
SUBSTRATE   4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine
            6-sulfate [CPD:C04865];
            H2O [CPD:C00001]
PRODUCT     4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine
            [CPD:C01310];
            sulfate [CPD:C00059]
COMMENT     Also acts on the saturated analogue and N-acetyl-D-galactosamine
            4,6-disulfate, but not higher oligosaccharides, nor any 4-sulfate
REFERENCE   1  [PMID:5647268]
  AUTHORS   Yamagata T, Saito H, Habuchi O, Suzuki S.
  TITLE     Purification and properties of bacterial chondroitinases and
            chondrosulfatases.
  JOURNAL   J. Biol. Chem. 243 (1968) 1523-35.
  ORGANISM  Proteus vulgaris
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.10
            ExPASy - ENZYME nomenclature database: 3.1.6.10
            ExplorEnz - The Enzyme Database: 3.1.6.10
            ERGO genome analysis and discovery system: 3.1.6.10
            BRENDA, the Enzyme Database: 3.1.6.10
            CAS: 9045-76-5
///
ENTRY       EC 3.1.6.11                 Enzyme
NAME        disulfoglucosamine-6-sulfatase;
            N-sulfoglucosamine-6-sulfatase;
            6,N-disulfoglucosamine 6-O-sulfohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     N,6-O-disulfo-D-glucosamine 6-sulfohydrolase
REACTION    N,6-O-disulfo-D-glucosamine + H2O = N-sulfo-D-glucosamine + sulfate
            [RN:R03216]
ALL_REAC    R03216
SUBSTRATE   N,6-O-disulfo-D-glucosamine [CPD:C03789];
            H2O [CPD:C00001]
PRODUCT     N-sulfo-D-glucosamine [CPD:C01075];
            sulfate [CPD:C00059]
COMMENT     May be identical with EC 3.1.6.14 N-acetylglucosamine-6-sulfatase.
REFERENCE   1  [PMID:5775690]
  AUTHORS   Dietrich CP.
  TITLE     Enzymic degradation of heparin. A sulphamidase and a sulphoesterase
            from Flavobacterium heparinum.
  JOURNAL   Biochem. J. 111 (1969) 91-5.
  ORGANISM  Flavobacterium heparinum
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.11
            ExPASy - ENZYME nomenclature database: 3.1.6.11
            ExplorEnz - The Enzyme Database: 3.1.6.11
            ERGO genome analysis and discovery system: 3.1.6.11
            BRENDA, the Enzyme Database: 3.1.6.11
            CAS: 37288-32-7
///
ENTRY       EC 3.1.6.12                 Enzyme
NAME        N-acetylgalactosamine-4-sulfatase;
            chondroitinsulfatase;
            chondroitinase;
            arylsulfatase B;
            acetylgalactosamine 4-sulfatase;
            N-acetylgalactosamine 4-sulfate sulfohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     N-acetyl-D-galactosamine-4-sulfate 4-sulfohydrolase
REACTION    Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine
            4-sulfate units of chondroitin sulfate and dermatan sulfate
            [RN:R07823]
ALL_REAC    R07823(G)
COMMENT     Acts also on N-acetylglucosamine 4-sulfate.
REFERENCE   1  [PMID:976430]
  AUTHORS   Farooqui AA.
  TITLE     The desulphation of hexosamine sulphates by arylsulphatase B.
  JOURNAL   Experientia. 32 (1976) 1242-4.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:738706]
  AUTHORS   Gorham SD, Cantz M.
  TITLE     Arylsulphatase B, an exo-sulphatase for chondroitin 4-sulphate
            tetrasaccharide.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 359 (1978) 1811-4.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:7370276]
  AUTHORS   Tsuji M, Nakanishi Y, Habuchi H, Ishihara K, Suzuki S.
  TITLE     The common identity of UDP-N-acetylgalactosamine 4-sulfatase,
            nitrocatechol sulfatase (arylsulfatase), and chondroitin
            4-sulfatase.
  JOURNAL   Biochim. Biophys. Acta. 612 (1980) 373-83.
  ORGANISM  chicken [GN:gga], cow [GN:bta]
PATHWAY     PATH: map00531  Glycosaminoglycan degradation
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01135  arylsulfatase B
GENES       HSA: 411(ARSB)
            MMU: 11881(Arsb)
            CFA: 610364(ARSB)
            SPU: 583464(LOC583464)
            RBA: RB1475(arsB) RB198 RB348 RB5417
STRUCTURES  PDB: 1FSU  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.12
            ExPASy - ENZYME nomenclature database: 3.1.6.12
            ExplorEnz - The Enzyme Database: 3.1.6.12
            ERGO genome analysis and discovery system: 3.1.6.12
            BRENDA, the Enzyme Database: 3.1.6.12
            CAS: 55354-43-3
///
ENTRY       EC 3.1.6.13                 Enzyme
NAME        iduronate-2-sulfatase;
            chondroitinsulfatase;
            idurono-2-sulfatase;
            iduronide-2-sulfate sulfatase;
            L-iduronosulfatase;
            L-idurono sulfate sulfatase;
            iduronate sulfatase;
            sulfo-L-iduronate sulfatase;
            L-iduronate 2-sulfate sulfatase;
            sulfoiduronate sulfohydrolase;
            2-sulfo-L-iduronate 2-sulfatase;
            iduronate-2-sulfate sulfatase;
            iduronate sulfate sulfatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     L-iduronate-2-sulfate 2-sulfohydrolase
REACTION    Hydrolysis of the 2-sulfate groups of the L-iduronate 2-sulfate
            units of dermatan sulfate, heparan sulfate and heparin [RN:R07812
            R07821]
ALL_REAC    R07812(G) R07821(G)
REFERENCE   1  [PMID:6816283]
  AUTHORS   Archer IM, Harper PS, Wusteman FS.
  TITLE     Multiple forms of iduronate 2-sulphate sulphatase in human tissues
            and body fluids.
  JOURNAL   Biochim. Biophys. Acta. 708 (1982) 134-40.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:4269173]
  AUTHORS   Bach G, Eisenberg F Jr, Cantz M, Neufeld EF.
  TITLE     The defect in the Hunter syndrome: deficiency of sulfoiduronate
            sulfatase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 70 (1973) 2134-8.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:6945876]
  AUTHORS   Di Natale P, Ronsisvalle L.
  TITLE     Identification and partial characterization of two enzyme forms of
            iduronate sulfatase from human placenta.
  JOURNAL   Biochim. Biophys. Acta. 661 (1981) 106-11.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:6950934]
  AUTHORS   Yutaka T, Fluharty AL, Stevens RL, Kihara H.
  TITLE     Purification and some properties of human liver iduronate sulfatase.
  JOURNAL   J. Biochem. (Tokyo). 91 (1982) 433-41.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00531  Glycosaminoglycan degradation
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01136  iduronate 2-sulfatase
GENES       HSA: 3423(IDS)
            MCC: 700892(IDS)
            MMU: 15931(Ids)
            CFA: 492194(IDS)
            GGA: 422392(IDS)
            RBA: RB10612 RB110 RB11127(ids) RB2085(betC) RB2254 RB2707 RB3755
                 RB5424 RB763
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.13
            ExPASy - ENZYME nomenclature database: 3.1.6.13
            ExplorEnz - The Enzyme Database: 3.1.6.13
            ERGO genome analysis and discovery system: 3.1.6.13
            BRENDA, the Enzyme Database: 3.1.6.13
            CAS: 50936-59-9
///
ENTRY       EC 3.1.6.14                 Enzyme
NAME        N-acetylglucosamine-6-sulfatase;
            chondroitinsulfatase;
            O,N-disulfate O-sulfohydrolase;
            acetylglucosamine 6-sulfatase;
            N-acetylglucosamine 6-sulfate sulfatase;
            acetylglucosamine 6-sulfatase;
            2-acetamido-2-deoxy-D-glucose 6-sulfate sulfatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     N-acetyl-D-glucosamine-6-sulfate 6-sulfohydrolase
REACTION    Hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine
            6-sulfate units of heparan sulfate and keratan sulfate [RN:R07808
            R07819]
ALL_REAC    R07808(G) R07819(G)
COMMENT     May be identical with EC 3.1.6.11 disulfoglucosamine-6-sulfatase.
REFERENCE   1  [PMID:762121]
  AUTHORS   Basner R, Kresse H, von Figura K.
  TITLE     N-Acetylglucosamine-6-sulfate sulfatase from human urine.
  JOURNAL   J. Biol. Chem. 254 (1979) 1151-8.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:6458607]
  AUTHORS   Kresse H, Fuchs W, Glossl J, Holtfrerich D, Gilberg W.
  TITLE     Liberation of N-acetylglucosamine-6-sulfate by human
            beta-N-acetylhexosaminidase A.
  JOURNAL   J. Biol. Chem. 256 (1981) 12926-32.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:6451222]
  AUTHORS   Weissmann B, Chao H, Chow P.
  TITLE     A glucosamine O,N-disulfate O-sulfohydrolase with a probable role in
            mammalian catabolism of heparan sulfate.
  JOURNAL   Biochem. Biophys. Res. Commun. 97 (1980) 827-33.
  ORGANISM  rat [GN:rno], cow [GN:bta]
PATHWAY     PATH: map00531  Glycosaminoglycan degradation
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01137  N-acetylglucosamine-6-sulfatase
GENES       HSA: 2799(GNS)
            PTR: 467054(GNS)
            RNO: 299825(Gns)
            CFA: 474429(GNS)
            GGA: 417829(GNS)
            VFI: VFA1007
            FRA: Francci3_2189
            SEN: SACE_4791
            RBA: RB200 RB406 RB4880 RB5282 RB8596(mdsA) RB973
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.14
            ExPASy - ENZYME nomenclature database: 3.1.6.14
            ExplorEnz - The Enzyme Database: 3.1.6.14
            ERGO genome analysis and discovery system: 3.1.6.14
            BRENDA, the Enzyme Database: 3.1.6.14
            CAS: 65666-34-4
///
ENTRY       EC 3.1.6.15                 Enzyme
NAME        N-sulfoglucosamine-3-sulfatase;
            chondroitinsulfatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     N-sulfo-3-sulfoglucosamine 3-sulfohydrolase
REACTION    Hydrolysis of the 3-sulfate groups of the N-sulfo-D-glucosamine
            3-O-sulfate units of heparin
COMMENT     The enzyme from Flavobacterium heparinum also hydrolyses
            N-acetyl-D-glucosamine 3-O-sulfate; the mammalian enzyme acts only
            on the disulfated residue.
REFERENCE   1  [PMID:3987694]
  AUTHORS   Bruce JS, McLean MW, Long WF, Williamson FB.
  TITLE     Flavobacterium heparinum 3-O-sulphatase for N-substituted
            glucosamine 3-O-sulphate.
  JOURNAL   Eur. J. Biochem. 148 (1985) 359-65.
  ORGANISM  Flavobacterium heparinum
REFERENCE   2  [PMID:7396957]
  AUTHORS   Leder IG.
  TITLE     A novel 3-O sulfatase from human urine acting on
            methyl-2-deoxy-2-sulfamino-alphs-D-glucopyranoside 3-sulfate.
  JOURNAL   Biochem. Biophys. Res. Commun. 94 (1980) 1183-9.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map01032  Glycan structures - degradation
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.15
            ExPASy - ENZYME nomenclature database: 3.1.6.15
            ExplorEnz - The Enzyme Database: 3.1.6.15
            ERGO genome analysis and discovery system: 3.1.6.15
            BRENDA, the Enzyme Database: 3.1.6.15
///
ENTRY       EC 3.1.6.16                 Enzyme
NAME        monomethyl-sulfatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     monomethyl-sulfate sulfohydrolase
REACTION    monomethyl sulfate + H2O = methanol + sulfate [RN:R01145]
ALL_REAC    R01145
SUBSTRATE   monomethyl sulfate [CPD:C02704];
            H2O [CPD:C00001]
PRODUCT     methanol [CPD:C00132];
            sulfate [CPD:C00059]
COMMENT     Highly specific; does not act on monoethyl sulfate, monoisopropyl
            sulfate or monododecyl sulfate.
REFERENCE   1  [PMID:6641899]
  AUTHORS   Ghisalba O, Kuenzi M.
  TITLE     Biodegradation and utilization of monomethyl sulfate by specialized
            methylotrophs.
  JOURNAL   Experientia. 39 (1983) 1257-63.
  ORGANISM  Hyphomicrobium sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.16
            ExPASy - ENZYME nomenclature database: 3.1.6.16
            ExplorEnz - The Enzyme Database: 3.1.6.16
            ERGO genome analysis and discovery system: 3.1.6.16
            BRENDA, the Enzyme Database: 3.1.6.16
///
ENTRY       EC 3.1.6.17                 Enzyme
NAME        D-lactate-2-sulfatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     (S)-2-O-sulfolactate 2-sulfohydrolase
REACTION    (S)-2-O-sulfolactate + H2O = (S)-lactate + sulfate [RN:R01448]
ALL_REAC    R01448
SUBSTRATE   (S)-2-O-sulfolactate [CPD:C02914];
            H2O [CPD:C00001]
PRODUCT     (S)-lactate [CPD:C00186];
            sulfate [CPD:C00059]
COMMENT     Highly specific.
REFERENCE   1  [PMID:6497859]
  AUTHORS   Crescenzi AM, Dodgson KS, White GF.
  TITLE     Purification and some properties of the D-lactate-2-sulphatase of
            Pseudomonas syringae GG.
  JOURNAL   Biochem. J. 223 (1984) 487-94.
  ORGANISM  Pseudomonas syringae
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.17
            ExPASy - ENZYME nomenclature database: 3.1.6.17
            ExplorEnz - The Enzyme Database: 3.1.6.17
            ERGO genome analysis and discovery system: 3.1.6.17
            BRENDA, the Enzyme Database: 3.1.6.17
            CAS: 93586-05-1
///
ENTRY       EC 3.1.6.18                 Enzyme
NAME        glucuronate-2-sulfatase;
            glucurono-2-sulfatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Sulfuric-ester hydrolases
SYSNAME     polysaccharide-2-O-sulfo-D-glucuronate 2-sulfohydrolase
REACTION    Hydrolysis of the 2-sulfate groups of the 2-O-sulfo-D-glucuronate
            residues of chondroitin sulfate, heparin and heparitin sulfate
            [RN:R07817]
ALL_REAC    R07817(G)
COMMENT     Does not act on iduronate 2-sulfate residues (cf. EC 3.1.6.13
            iduronate-2-sulfatase)
REFERENCE   1  [PMID:4019466]
  AUTHORS   Shaklee PN, Glaser JH, Conrad HE.
  TITLE     A sulfatase specific for glucuronic acid 2-sulfate residues in
            glycosaminoglycans.
  JOURNAL   J. Biol. Chem. 260 (1985) 9146-9.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00531  Glycosaminoglycan degradation
            PATH: map01032  Glycan structures - degradation
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.6.18
            ExPASy - ENZYME nomenclature database: 3.1.6.18
            ExplorEnz - The Enzyme Database: 3.1.6.18
            ERGO genome analysis and discovery system: 3.1.6.18
            BRENDA, the Enzyme Database: 3.1.6.18
            CAS: 98597-45-6
///
ENTRY       EC 3.1.7.1                  Enzyme
NAME        prenyl-diphosphatase;
            prenyl-pyrophosphatase;
            prenol pyrophosphatase;
            prenylphosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Diphosphoric-monoester hydrolases
SYSNAME     prenyl-diphosphate diphosphohydrolase
REACTION    prenyl diphosphate + H2O = prenol + diphosphate [RN:R03541]
ALL_REAC    R03541
SUBSTRATE   prenyl diphosphate [CPD:C00235];
            H2O [CPD:C00001]
PRODUCT     prenol [CPD:C01390];
            diphosphate [CPD:C00013]
COMMENT     Farnesyl diphosphate is the best substrate tested to date.
REFERENCE   1  [PMID:4288361]
  AUTHORS   Tsai SC, Gaylor JL.
  TITLE     Testicular sterols. V. Preparation and partial purification of a
            microsomal prenol pyrophosphate pyrophosphohydrolase.
  JOURNAL   J. Biol. Chem. 241 (1966) 4043-50.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.7.1
            ExPASy - ENZYME nomenclature database: 3.1.7.1
            ExplorEnz - The Enzyme Database: 3.1.7.1
            ERGO genome analysis and discovery system: 3.1.7.1
            BRENDA, the Enzyme Database: 3.1.7.1
            CAS: 37288-33-8
///
ENTRY       EC 3.1.7.2                  Enzyme
NAME        guanosine-3',5'-bis(diphosphate) 3'-diphosphatase;
            guanosine-3',5'-bis(diphosphate) 3'-pyrophosphatase;
            PpGpp-3'-pyrophosphohydrolase;
            PpGpp phosphohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Diphosphoric-monoester hydrolases
SYSNAME     guanosine-3',5'-bis(diphosphate) 3'-diphosphohydrolase
REACTION    guanosine 3',5'-bis(diphosphate) + H2O = guanosine 5'-diphosphate +
            diphosphate [RN:R00336]
ALL_REAC    R00336
SUBSTRATE   guanosine 3',5'-bis(diphosphate) [CPD:C01228];
            H2O [CPD:C00001]
PRODUCT     guanosine 5'-diphosphate [CPD:C00035];
            diphosphate [CPD:C00013]
REFERENCE   1  [PMID:365225]
  AUTHORS   Heinemeyer EA, Richter D.
  TITLE     Characterization of the guanosine 5'-triphosphate 3'-diphosphate and
            guanosine 5'-diphosphate 3'-diphosphate degradation reaction
            catalyzed by a specific pyrophosphorylase from Escherichia coli.
  JOURNAL   Biochemistry. 17 (1978) 5368-72.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:114395]
  AUTHORS   Richter D, Fehr S, Harder R.
  TITLE     The guanosine 3',5'-bis(diphosphate) (ppGpp) cycle. Comparison of
            synthesis and degradation of guanosine 3',5'-bis(diphosphate) in
            various bacterial systems.
  JOURNAL   Eur. J. Biochem. 99 (1979) 57-64.
  ORGANISM  Escherichia coli [GN:eco], Bacillus stearothermophilus, Bacillus
            subtilis [GN:bsu], Bacillus brevis
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01139  guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase
GENES       CGR: CAGL0G07755g
            ECO: b3650(spoT)
            ECJ: JW3625(spoT)
            ECE: Z5076(spoT)
            ECS: ECs4525
            ECC: c4475(spoT)
            ECI: UTI89_C4195(spoT)
            ECP: ECP_3748
            ECV: APECO1_2811(spoT)
            ECW: EcE24377A_4153(spoT)
            ECX: EcHS_A3861(spoT)
            STY: STY4050(spoT)
            STT: t3776(spoT)
            SPT: SPA3594(spoT)
            SEC: SC3666(spoT)
            STM: STM3742(spoT)
            YPE: YPO0038(spoT)
            YPK: y0103(spoT)
            YPM: YP_0039(spoT)
            YPA: YPA_3504
            YPN: YPN_3812
            YPS: YPTB0035(spoT)
            YPI: YpsIP31758_0039(spoT)
            SFL: SF3690(spoT)
            SFX: S4079(spoT)
            SFV: SFV_3879(spoT)
            SSN: SSON_3755(spoT)
            SBO: SBO_3727(spoT)
            SDY: SDY_4082(spoT)
            ECA: ECA0038(spoT)
            PLU: plu0272(spoT)
            SGL: SG2223
            SPE: Spro_4869
            HIT: NTHI2052(spoT)
            HDU: HD1924(spoT)
            HSO: HS_1455(spoT)
            PMU: PM0920(spoT)
            MSU: MS1736(spoT)
            APL: APL_1825(spoT)
            ASU: Asuc_1024
            XFA: XF0352
            XFT: PD1707(spoT)
            XCC: XCC3247(spoT)
            XCB: XC_0956
            XCV: XCV3510(spoT)
            XAC: XAC3393(spoT)
            XOO: XOO1149(spoT)
            XOM: XOO_1046(XOO1046)
            VCH: VC2710
            VCO: VC0395_A2282(spoT)
            VVU: VV1_0852
            VVY: VV0241
            VPA: VP0159
            VFI: VF0104
            PPR: PBPRA0189
            PAE: PA5338(spoT)
            PAU: PA14_70470(spoT)
            PPU: PP_5302(spoT)
            PST: PSPTO_0073(spoT)
            PSB: Psyr_0209
            PSP: PSPPH_0197(spoT)
            PFL: PFL_6063(spoT)
            PEN: PSEEN5447(spoT)
            PAR: Psyc_1725(spoT)
            ACI: ACIAD3326
            SON: SO_0359(spoT)
            SBM: Shew185_0351
            ILO: IL2380(spoT)
            CPS: CPS_4973(spoT)
            PHA: PSHAa2793(spoT)
            PAT: Patl_0349
            CBU: CBU_0303(spoT)
            CBD: COXBU7E912_1778(spoT)
            LPN: lpg2009(spoT)
            LPF: lpl1985(spoT)
            LPP: lpp1990(spoT)
            MCA: MCA2023(spoT)
            FTU: FTT0808(spoT)
            FTF: FTF0808(spoT)
            FTW: FTW_0605
            FTH: FTH_1376(spoT2)
            FTA: FTA_1501
            HCH: HCH_06313
            ABO: ABO_0176
            AHA: AHA_0039
            VOK: COSY_0471(spoT)
            NME: NMB1659
            NMA: NMA1917a(spoT)
            NMC: NMC1577(spoT)
            NGO: NGO1308
            CVI: CV_3768(spoT)
            RSO: RSc2153(spoT)
            BMA: BMA2094
            BMV: BMASAVP1_A0817
            BML: BMA10299_A2650
            BMN: BMA10247_1962
            BUR: Bcep18194_C6634
            BPS: BPSL2561(spoT)
            BPM: BURPS1710b_3047(spoT)
            BPL: BURPS1106A_3013
            BPD: BURPS668_2947
            BTE: BTH_I1588
            BPE: BP1576(spoT)
            BPA: BPP3007(spoT)
            BBR: BB2973(spoT)
            MPT: Mpe_A2721
            MMS: mma_1326(spoT)
            AZO: azo3951(spoT)
            HPY: HP0775(spoT)
            HPA: HPAG1_0760
            HHE: HH0831(spoT)
            WSU: WS0240(spoT)
            CJE: Cj1272c(spoT)
            CJR: CJE1408
            CJU: C8J_1216(spoT)
            ABU: Abu_0645(spoT)
            NIS: NIS_0760
            SUN: SUN_1745
            SAT: SYN_00904 SYN_01901 SYN_03611
            PUB: SAR11_1058
            MLO: mlr7755
            MES: Meso_0946
            SME: SMc02659(relA)
            ATU: Atu1030
            ATC: AGR_C_1896
            RET: RHE_CH01385(relA)
            RLE: RL1506(relA)
            BME: BMEI1296
            BMF: BAB1_0672
            BMS: BR0652
            BMB: BruAb1_0669
            BJA: bll5065
            BRA: BRADO1039 BRADO4468(relA)
            BBT: BBta_4687(relA) BBta_7010
            BHE: BH05040(spoT)
            BQU: BQ04230(spoT)
            CCR: CC_1553
            SIL: SPO3203
            RSP: RSP_1670(spoT)
            RDE: RD1_1359(spoT)
            ZMO: ZMO0086
            MGM: Mmc1_2468
            SPZ: M5005_Spy_1686(relA)
            SPH: MGAS10270_Spy1755(relA)
            SPI: MGAS10750_Spy1780(relA)
            SPJ: MGAS2096_Spy1709(relA)
            SPK: MGAS9429_Spy1689(relA)
            SPA: M6_Spy1694
            SPB: M28_Spy1674(relA)
            MPN: MPN397(spoT)
            MPE: MYPE5280(spot)
            MGA: MGA_0950(spoT)
            UUR: UU283(spoT)
            CGB: cg1861(rel)
            FNU: FN1482
            BGA: BG0196(spoT)
            BAF: BAPKO_0200(spoT)
            SYN: slr1325(spoT)
            SYW: SYNW2324(spoT)
            SYC: syc0179_c
            SYF: Synpcc7942_1377
            SYR: SynRCC307_2235(spoT)
            SYX: SynWH7803_2342(spoT)
            CYA: CYA_1944
            CYB: CYB_1543
            TEL: tll0584
            GVI: glr2748
            ANA: all1549
            PMA: Pro0217(spoT)
            PMM: PMM0191(spoT)
            PMT: PMT2111(spoT)
            PMB: A9601_02091(spoT)
            PMC: P9515_02201(spoT)
            PMF: P9303_28061(spoT)
            PMG: P9301_02111(spoT)
            PMH: P9215_02091(spoT)
            PME: NATL1_02671(spoT)
            SRU: SRU_1062(spoT)
            CHU: CHU_2390(spoT)
            TTH: TTC1355
            TTJ: TTHA1717
            AAE: aq_844(spoT)
STRUCTURES  PDB: 1VJ7  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.7.2
            ExPASy - ENZYME nomenclature database: 3.1.7.2
            ExplorEnz - The Enzyme Database: 3.1.7.2
            ERGO genome analysis and discovery system: 3.1.7.2
            BRENDA, the Enzyme Database: 3.1.7.2
            CAS: 70457-12-4
///
ENTRY       EC 3.1.7.3                  Enzyme
NAME        monoterpenyl-diphosphatase;
            bornyl pyrophosphate hydrolase;
            monoterpenyl-pyrophosphatase
CLASS       Hydrolases;
            Acting on ester bonds;
            Diphosphoric-monoester hydrolases
SYSNAME     monoterpenyl-diphosphate diphosphohydrolase
REACTION    monoterpenyl diphosphate + H2O = monoterpenol + diphosphate
            [RN:R03016]
ALL_REAC    R03016
SUBSTRATE   monoterpenyl diphosphate [CPD:C03517];
            H2O [CPD:C00001]
PRODUCT     monoterpenol [CPD:C00863];
            diphosphate [CPD:C00013]
COMMENT     A group of enzymes with varying specificity for the monoterpenol
            moiety. One has the highest activity on sterically hindered
            compounds such as (+)-bornyl diphosphate; another has highest
            activity on the diphosphates of primary allylic alcohols such as
            geraniol.
REFERENCE   1  [PMID:42357]
  AUTHORS   Croteau R, Karp F.
  TITLE     Biosynthesis of monoterpenes: hydrolysis of bornyl pyrophosphate, an
            essential step in camphor biosynthesis, and hydrolysis of geranyl
            pyrophosphate, the acyclic precursor of camphor, by enzymes from
            sage (Salvia officinalis).
  JOURNAL   Arch. Biochem. Biophys. 198 (1979) 523-32.
  ORGANISM  Salvia officinalis
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.7.3
            ExPASy - ENZYME nomenclature database: 3.1.7.3
            ExplorEnz - The Enzyme Database: 3.1.7.3
            ERGO genome analysis and discovery system: 3.1.7.3
            BRENDA, the Enzyme Database: 3.1.7.3
///
ENTRY       EC 3.1.8.1                  Enzyme
NAME        aryldialkylphosphatase;
            organophosphate hydrolase;
            paraoxonase;
            A-esterase;
            aryltriphosphatase;
            organophosphate esterase;
            esterase B1;
            esterase E4;
            paraoxon esterase;
            pirimiphos-methyloxon esterase;
            OPA anhydrase;
            organophosphorus hydrolase;
            phosphotriesterase;
            paraoxon hydrolase;
            OPH;
            organophosphorus acid anhydrase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-triester hydrolases
SYSNAME     aryltriphosphate dialkylphosphohydrolase
REACTION    an aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl
            alcohol [RN:R03979]
ALL_REAC    R03979;
            (other) R05421 R05548
SUBSTRATE   aryl dialkyl phosphate [CPD:C03254];
            H2O [CPD:C00001]
PRODUCT     dialkyl phosphate [CPD:C02534];
            aryl alcohol [CPD:C01891]
COFACTOR    Divalent cation [CPD:C00572]
INHIBITOR   Chelating agent [CPD:C00917]
COMMENT     Acts on organophosphorus compounds (such as paraoxon) including
            esters of phosphonic and phosphinic acids. Inhibited by chelating
            agents; requires divalent cations for activity. Previously regarded
            as identical with EC 3.1.1.2 arylesterase.
REFERENCE   1  [PMID:13032041]
  AUTHORS   ALDRIDGE WN.
  TITLE     Serum esterases.  I.  Two types of esterase (A and B) hydrolysing
            p-nitrophenyl acetate, propionate and butyrate, and a method for
            their determination.
  JOURNAL   Biochem. J. 53 (1953) 110-7.
  ORGANISM  rat [GN:rno], rabbit, horse
REFERENCE   2  [PMID:5047702]
  AUTHORS   Bosmann HB.
  TITLE     Membrane marker enzymes. Characterization of an arylesterase of
            guinea pig cerebral cortex utilizing p-nitrophenyl acetate as
            substrate.
  JOURNAL   Biochim. Biophys. Acta. 276 (1972) 180-91.
  ORGANISM  guinea pig
REFERENCE   3  [PMID:2822017]
  AUTHORS   Mackness MI, Thompson HM, Hardy AR, Walker CH.
  TITLE     Distinction between 'A'-esterases and arylesterases. Implications
            for esterase classification.
  JOURNAL   Biochem. J. 245 (1987) 293-6.
  ORGANISM  rat [GN:rno], rabbit, human [GN:hsa], mouse [GN:mmu], sheep, goat,
            cow [GN:bta], cat, Meles taxus
REFERENCE   4
  AUTHORS   Main, A.R.
  TITLE     The differentiation of the A-type esterases in sheep serum.
  JOURNAL   Biochem. J. 75 (1960) 188-195.
  ORGANISM  sheep
REFERENCE   5
  AUTHORS   In: Reiner, E., Aldridge, W.N. and Hoskin, C.G. (Eds.), Enzymes
            Hydrolysing Organophosphorus Compounds, Ellis Horwood, Chichester,
            UK, 1989.
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
ORTHOLOGY   KO: K01140  aryldialkylphosphatase
GENES       HSA: 5444(PON1) 5445(PON2) 5446(PON3)
            PTR: 463547(PON1) 463548(PON3) 463549(PON2)
            MMU: 18979(Pon1) 269823(Pon3) 330260(Pon2)
            RNO: 296851(Pon2) 84024(Pon1)
            CFA: 403855(PON2)
            BTA: 281417(PON2)
            SSC: 733674(PON3)
            GGA: 395830(PON2)
            SPU: 582780(LOC582780)
            ECI: UTI89_C3877(yhfV)
            CTC: CTC00933
            MBO: Mb0235c(php)
            MBB: BCG_0267c(php)
            MMC: Mmcs_0224
            MKM: Mkms_0234
            MJL: Mjls_0214
            RXY: Rxyl_2340
STRUCTURES  PDB: 1EYW  1EZ2  1HZY  1I0B  1I0D  1JGM  1P6B  1P6C  1P9E  1QW7  
                 1V04  2D2G  2D2H  2D2J  2OB3  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.8.1
            ExPASy - ENZYME nomenclature database: 3.1.8.1
            ExplorEnz - The Enzyme Database: 3.1.8.1
            ERGO genome analysis and discovery system: 3.1.8.1
            UM-BBD (Biocatalysis/Biodegradation Database): 3.1.8.1
            BRENDA, the Enzyme Database: 3.1.8.1
            CAS: 117698-12-1
///
ENTRY       EC 3.1.8.2                  Enzyme
NAME        diisopropyl-fluorophosphatase;
            DFPase;
            tabunase;
            somanase;
            organophosphorus acid anhydrolase;
            organophosphate acid anhydrase;
            OPA anhydrase;
            diisopropylphosphofluoridase;
            dialkylfluorophosphatase;
            diisopropyl phosphorofluoridate hydrolase;
            isopropylphosphorofluoridase;
            diisopropylfluorophosphonate dehalogenase
CLASS       Hydrolases;
            Acting on ester bonds;
            Phosphoric-triester hydrolases
SYSNAME     diisopropyl-fluorophosphate fluorohydrolase
REACTION    diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride
            [RN:R01533]
ALL_REAC    R01533
SUBSTRATE   diisopropyl fluorophosphate [CPD:C00202];
            H2O [CPD:C00001]
PRODUCT     diisopropyl phosphate [CPD:C03113];
            fluoride [CPD:C00742]
COFACTOR    Divalent cation [CPD:C00572]
INHIBITOR   Chelating agent [CPD:C00917]
COMMENT     Acts on phosphorus anhydride bonds (such as phosphorus-halide and
            phosphorus-cyanide) in organophosphorus compounds (including 'nerve
            gases'). Inhibited by chelating agents; requires divalent cations.
            Related to EC 3.1.8.1 aryldialkylphosphatase.
REFERENCE   1
  AUTHORS   Augustinsson, K.-B. and Heimburger, G.
  TITLE     Enzymatic hydrolysis of organophosphorus compounds. I. Occurrence of
            enzymes hydrolysing dimethyl-amido-ethoxy-phosphoryl cyanide
            (Tabun).
  JOURNAL   Acta Chem. Scand. 8 (1954) 753-761.
  ORGANISM  rabbit
REFERENCE   2
  AUTHORS   Augustinsson, K.-B. and Heimburger, G.
  TITLE     Enzymatic hydrolysis of organophosphorus compounds. II. Analysis of
            reaction products in experiments with Tabun and some properties of
            blood plasma tabunase.
  JOURNAL   Acta Chem. Scand. 8 (1954) 762-767.
  ORGANISM  rabbit
REFERENCE   3
  AUTHORS   Augustinsson, K.-B. and Heimburger, G.
  TITLE     Enzymatic hydrolysis of organophosphorus compounds. IV. Specificity
            studies.
  JOURNAL   Acta Chem. Scand. 8 (1954) 1533-1541.
  ORGANISM  rabbit
REFERENCE   4  [PMID:13479457]
  AUTHORS   COHEN JA, WARRINGA MG.
  TITLE     Purification and properties of dialkylfluorophosphatase.
  JOURNAL   Biochim. Biophys. Acta. 26 (1957) 29-39.
  ORGANISM  pig [GN:ssc]
REFERENCE   5
  AUTHORS   Mounter, L.A.
  TITLE     Enzymic hydrolysis of organophosphorus compounds.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 541-550.
REFERENCE   6
  AUTHORS   In: Reiner, E., Aldridge, W.N. and Hoskin, C.G. (Eds.), Enzymes
            Hydrolysing Organophosphorus Compounds, Ellis Horwood, Chichester,
            UK, 1989.
STRUCTURES  PDB: 1E1A  1PJX  2GVU  2GVV  2GVW  2GVX  2IAO  2IAP  2IAQ  2IAR  
                 2IAS  2IAT  2IAU  2IAV  2IAW  2IAX  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.8.2
            ExPASy - ENZYME nomenclature database: 3.1.8.2
            ExplorEnz - The Enzyme Database: 3.1.8.2
            ERGO genome analysis and discovery system: 3.1.8.2
            BRENDA, the Enzyme Database: 3.1.8.2
            CAS: 9032-18-2
///
ENTRY       EC 3.1.11.1                 Enzyme
NAME        exodeoxyribonuclease I;
            Escherichia coli exonuclease I;
            E. coli exonuclease I;
            exonuclease I
CLASS       Hydrolases;
            Acting on ester bonds;
            Exodeoxyribonucleases producing 5'-phosphomonoesters
REACTION    Exonucleolytic cleavage in the 3'- to 5'-direction to yield
            nucleoside 5'-phosphates
COMMENT     Preference for single-stranded DNA. The Escherichia coli enzyme
            hydrolyses glucosylated DNA.
REFERENCE   1  [PMID:71298]
  AUTHORS   Blakesley RW, Dodgson JB, Nes IF, Wells RD.
  TITLE     Duplex regions in &quot;single-stranded&quot; phiX174 DNA are
            cleaved by a restriction endonuclease from Haemophilus aegyptius.
  JOURNAL   J. Biol. Chem. 252 (1977) 7300-6.
  ORGANISM  Haemophilus aegyptius
REFERENCE   2
  AUTHORS   Kelley, R.B., Atkinson, M.R., Huberman, J.A. and Kornberg, A.
  TITLE     Excision of thymine dimers and other mismatched sequences by DNA
            polymerases of Escherichia coli.
  JOURNAL   Nature 224 (1969) 495-501.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Lehman, I.R. and Nussbaum, A.L.
  TITLE     The deoxyribonucleases of Escherichia coli. V. On the specificity of
            exonuclease I (phosphodiesterase).
  JOURNAL   J. Biol. Chem. 239 (1964) 2628-2636.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01141  exodeoxyribonuclease I
GENES       DME: Dmel_CG10387(tos)
            PIC: PICST_33450(EXO1)
            ECO: b2011(sbcB)
            ECJ: JW1993(sbcB)
            ECE: Z3173(sbcB)
            ECS: ECs2813
            ECC: c2539(sbcB)
            ECI: UTI89_C2285(sbcB)
            ECP: ECP_2055
            ECV: APECO1_1109(sbcB)
            ECW: EcE24377A_2302(sbcB)
            ECX: EcHS_A2149(sbcB)
            STY: STY2276(sbcB)
            STT: t0807(sbcB)
            SPT: SPA0804(sbcB)
            SEC: SC2077(sbcB)
            STM: STM2067(sbcB)
            YPE: YPO1558(sbcB)
            YPK: y2610(sbcB)
            YPM: YP_1446(sbcB)
            YPA: YPA_0853
            YPN: YPN_2422
            YPP: YPDSF_1418
            YPS: YPTB1569(sbcB)
            YPI: YpsIP31758_2420(sbcB)
            SFL: SF2070(sbcB)
            SFX: S2193(sbcB)
            SFV: SFV_2070(sbcB)
            SSN: SSON_2081(sbcB)
            SBO: SBO_0835(sbcB)
            SDY: SDY_2231(sbcB)
            ECA: ECA2565(sbcB)
            PLU: plu2847(sbcB)
            BUC: BU555(sbcB)
            BAS: BUsg537(sbcB)
            BAB: bbp503(sbcB)
            BCC: BCc_364(sbcB)
            SGL: SG1132
            ENT: Ent638_2627
            SPE: Spro_3214
            BFL: Bfl461(sbcB)
            BPN: BPEN_476(sbcB)
            HIT: NTHI1780(sbcB)
            HIP: CGSHiEE_04490(sbcB)
            HIQ: CGSHiGG_00695(sbcB)
            HDU: HD1412(sbcB)
            HSO: HS_0872(sbcB)
            PMU: PM0611(sbcB)
            MSU: MS1081(sbcB)
            APL: APL_0673(sbcB)
            ASU: Asuc_1400
            XFA: XF2022
            XFT: PD0793(sbcB)
            XCC: XCC1551(sbcB)
            XCB: XC_2683
            XCV: XCV1640(sbcB)
            XAC: XAC1599(sbcB)
            XOO: XOO2430(sbcB)
            XOM: XOO_2307(XOO2307)
            VCH: VC1234
            VCO: VC0395_A0855(sbcB)
            VVU: VV1_2792
            VVY: VV1472
            VPA: VP1301
            VFI: VF1482
            PPR: PBPRA1693(sbcB)
            PAE: PA4316(sbcB)
            PAU: PA14_56080(sbcB)
            PPU: PP_1365(sbcB)
            PPF: Pput_4359
            PST: PSPTO_4316(sbcB)
            PSB: Psyr_4020
            PSP: PSPPH_4026(sbcB)
            PFL: PFL_4788(sbcB)
            PFO: Pfl_4438
            PEN: PSEEN1150(sbcB)
            PMY: Pmen_3314
            SON: SO_2790(sbcB)
            SDN: Sden_2287
            SFR: Sfri_1638
            SAZ: Sama_1973
            SBL: Sbal_1695
            SBM: Shew185_1680
            SLO: Shew_1611
            SPC: Sputcn32_1569
            SSE: Ssed_2617
            SPL: Spea_2487
            SHE: Shewmr4_2410
            SHM: Shewmr7_2480
            SHN: Shewana3_2572
            SHW: Sputw3181_2530
            ILO: IL1370(sbcB)
            CPS: CPS_2014(sbcB)
            PHA: PSHAa1255(sbcB)
            PAT: Patl_2172
            SDE: Sde_2394
            PIN: Ping_2436
            MAQ: Maqu_2602
            CBU: CBU_1363
            MCA: MCA2382(sbcB)
            FTU: FTT1200c(sbcB)
            FTF: FTF1200c(sbcB)
            FTL: FTL_0744
            FTH: FTH_0746(sbcB)
            FTN: FTN_1177(sbcB)
            HCH: HCH_05002
            CSA: Csal_3024
            MMW: Mmwyl1_2380
            AHA: AHA_1899
            RMA: Rmag_0946
            VOK: COSY_0846(sbcB)
            CVI: CV_1329(sbcB)
            RSO: RSc3125(sbcB)
            RFR: Rfer_2072
            POL: Bpro_2939
            PNA: Pnap_1935
            AAV: Aave_3236
            AJS: Ajs_1838
            VEI: Veis_0266
            MPT: Mpe_A1360
            HAR: HEAR0585(sbcB)
            MMS: mma_0562(sbcB)
            NEU: NE0663(sbcB) NE0671(sbcB)
            NET: Neut_1887
            PUB: SAR11_0483(sbcB)
            PLA: Plav_1822
            BJA: bll0068
            RPE: RPE_2473
STRUCTURES  PDB: 1FXX  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.11.1
            ExPASy - ENZYME nomenclature database: 3.1.11.1
            ExplorEnz - The Enzyme Database: 3.1.11.1
            ERGO genome analysis and discovery system: 3.1.11.1
            BRENDA, the Enzyme Database: 3.1.11.1
///
ENTRY       EC 3.1.11.2                 Enzyme
NAME        exodeoxyribonuclease III;
            Escherichia coli exonuclease III;
            E. coli exonuclease III;
            endoribonuclease III
CLASS       Hydrolases;
            Acting on ester bonds;
            Exodeoxyribonucleases producing 5'-phosphomonoesters
REACTION    Exonucleolytic cleavage in the 3'- to 5'-direction to yield
            nucleoside 5'-phosphates
COMMENT     Preference for double-stranded DNA. Has endonucleolytic activity
            near apurinic sites on DNA.
REFERENCE   1  [PMID:5824576]
  AUTHORS   Lindahl T, Gally JA, Edelman GM.
  TITLE     Properties of deoxyribonuclease 3 from mammalian tissues.
  JOURNAL   J. Biol. Chem. 244 (1969) 5014-9.
  ORGANISM  rabbit
REFERENCE   2
  AUTHORS   Richardson, C.C. and Kornberg, A.
  TITLE     A deoxyribonucleic acid phosphatase-exonuclease from Escherichia
            coli. I. Purification of the enzyme and characterization of the
            phosphatase activity.
  JOURNAL   J. Biol. Chem. 239 (1964) 242-250.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Richardson, C.C., Lehman, I.R. and Kornberg, A.
  TITLE     A deoxyribonucleic acid phosphatase-exonuclease from Escherichia
            coli. II. Characterization of the exonuclease activity.
  JOURNAL   J. Biol. Chem. 239 (1964) 251-258.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01142  exodeoxyribonuclease III
GENES       HSA: 11277(TREX1)
            MMU: 22040(Trex1)
            CFA: 484778(LOC484778)
            BTA: 282099(TREX1)
            AFM: AFUA_3G06180
            ECU: ECU06_1360
            TET: TTHERM_00794600
            EHI: 213.t00004
            ECO: b1749(xthA)
            ECJ: JW1738(xthA)
            ECE: Z2781(xthA)
            ECS: ECs2455
            ECC: c2150(xthA)
            ECI: UTI89_C1945(xthA)
            ECP: ECP_1695
            ECV: APECO1_818(xthA)
            ECW: EcE24377A_1972(xth)
            ECX: EcHS_A1833(xth)
            STY: STY1812(xthA)
            STT: t1181(xthA)
            SPT: SPA1542(xthA)
            SEC: SC1324(xthA)
            STM: STM1302(xthA)
            YPE: YPO2168(xthA)
            YPK: y2153(xthA)
            YPM: YP_1968(xthA)
            YPA: YPA_1525
            YPN: YPN_1634
            YPS: YPTB2094(xthA)
            YPI: YpsIP31758_1976(xth)
            SFL: SF1477(xthA)
            SFX: S1594(xthA)
            SFV: SFV_1471(xthA)
            SSN: SSON_1408(xthA)
            SBO: SBO_1341(xthA)
            SDY: SDY_1527(xthA)
            ECA: ECA2335(xthA)
            PLU: plu2549(xthA)
            WBR: WGLp371(xthA)
            SGL: SG1363
            BFL: Bfl435(xthA)
            BPN: BPEN_449(xthA)
            HIT: NTHI0049(xthA)
            HIP: CGSHiEE_03130
            HIQ: CGSHiGG_02705
            HDU: HD1718(xthA)
            HSO: HS_0836(xthA)
            PMU: PM0691
            MSU: MS1048(xthA)
            APL: APL_0977(xthA)
            XFA: XF0164 XF1933
            XFT: PD0128(exoA) PD0864(xthA)
            XCC: XCC1998(xthA2) XCC3846(exoA) XCC4046(xthA1)
            XCB: XC_2186 XC_3930
            XCV: XCV2081(xthA1) XCV4015(exoA) XCV4270(xthA2)
            XAC: XAC2030(xthA2) XAC3902(exoA) XAC4171(xthA1)
            XOO: XOO0509(exoA) XOO4550(xthA1)
            XOM: XOO_0475(XOO0475) XOO_4286(XOO4286)
            VCH: VC1860
            VCO: VC0395_A1451(xth)
            VVU: VV1_2106
            VVY: VV2334
            VPA: VP1003
            VFI: VF1583
            PPR: PBPRA2737
            PAE: PA2545(xthA) PA4172 PA5332(crc)
            PAU: PA14_31650(xthA) PA14_70390(crc)
            PAP: PSPA7_0921(xth2) PSPA7_2692(xth1)
            PPU: PP_2707 PP_2890(xthA) PP_5292(crc)
            PST: PSPTO_0079 PSPTO_2747(xthA)
            PSB: Psyr_0215 Psyr_2476
            PSP: PSPPH_0203 PSPPH_2634(xth)
            PFL: PFL_3928(xth) PFL_6057
            PFO: Pfl_1868 Pfl_3649 Pfl_5545
            PEN: PSEEN2076(xthA) PSEEN5437
            PAR: Psyc_1199(xthA)
            PCR: Pcryo_1192
            ACI: ACIAD3526(crc)
            SON: SO_3037(xth)
            SDN: Sden_1465
            SFR: Sfri_1420
            SHE: Shewmr4_1447
            SHM: Shewmr7_1513
            SHN: Shewana3_1503
            ILO: IL1451(xthA)
            CPS: CPS_3173(xth)
            PHA: PSHAa1339(xthA)
            PAT: Patl_2648
            SDE: Sde_1995 Sde_3671
            MAQ: Maqu_1490
            CBU: CBU_0297(xth)
            CBD: COXBU7E912_1784(xth)
            LPN: lpg0648(xth) lpg0649(xthA1)
            LPF: lpl0684(exoA) lpl0685(xthA)
            LPP: lpp0702(exoA) lpp0703(xthA)
            MCA: MCA0321(xth-1) MCA3070(xth-2)
            FTU: FTT0959c(xthA)
            FTF: FTF0959c(xthA)
            FTW: FTW_0858(xthA)
            FTL: FTL_1244
            FTH: FTH_1221(xthA)
            FTA: FTA_1317(xth)
            FTN: FTN_0838(xthA)
            TCX: Tcr_2052
            NOC: Noc_0209
            AEH: Mlg_2782
            HCH: HCH_02757(xth) HCH_06339
            CSA: Csal_1621 Csal_3205
            ABO: ABO_1485(xthA)
            AHA: AHA_2958(xth)
            DNO: DNO_0431(xth-1) DNO_0917(xth-2)
            VOK: COSY_0892(xthA)
            NME: NMB0399 NMB2082
            NMA: NMA0348 NMA2086(xthA)
            NMC: NMC1768(xthA)
            NGO: NGO1561 NGO1994
            CVI: CV_0877(xthA) CV_4247(exoA)
            RSO: RSc0140(RS01010) RSc1593(xthA)
            REU: Reut_A1297
            REH: H16_A0223 H16_A1368
            RME: Rmet_0149 Rmet_1189 Rmet_4910
            BMA: BMA0167(xth-1) BMA1738(xth-2)
            BMV: BMASAVP1_A2247(xth) BMASAVP1_A2780(xth-1)
            BML: BMA10299_A2299(xth-1) BMA10299_A3071(xth-2)
            BMN: BMA10247_1520(xth) BMA10247_2379(xth-1)
            BXE: Bxe_A1526 Bxe_A4393 Bxe_B2221
            BUR: Bcep18194_A5454
            BCN: Bcen_5932
            BCH: Bcen2424_2145
            BAM: Bamb_2182
            BPS: BPSL0191 BPSL2315
            BPM: BURPS1710b_0371(xth) BURPS1710b_2765(xth-2)
            BPL: BURPS1106A_0186(xth) BURPS1106A_2687(xth)
            BPD: BURPS668_0175(xth) BURPS668_2631(xth)
            BTE: BTH_I0151(xth-1) BTH_I1847(xth-2)
            BPE: BP0369 BP2110
            BPA: BPP1422 BPP4061
            BBR: BB2496 BB4534
            RFR: Rfer_2983 Rfer_3929
            POL: Bpro_0216 Bpro_1820 Bpro_3424
            PNA: Pnap_2776
            MPT: Mpe_A0089 Mpe_A2071
            HAR: HEAR2385
            MMS: mma_0190(xthA1) mma_2444(xthA2)
            NEU: NE0023(xthA1) NE2192(xthA2)
            NET: Neut_0211 Neut_0691
            NMU: Nmul_A0224 Nmul_A2418
            EBA: ebA1134(xthA) ebA3323(xthA2)
            AZO: azo2880 azo3664(xthA2)
            DAR: Daro_0123 Daro_3648
            TBD: Tbd_0254 Tbd_2435
            MFA: Mfla_0172 Mfla_2484
            HPY: HP1526(lexA)
            HPA: HPAG1_1389
            HHE: HH0928(lexA)
            HAC: Hac_0003(exoA)
            CJE: Cj0255c
            CJR: CJE0305(xth)
            CJJ: CJJ81176_0282(xth)
            CJU: C8J_0232(xth)
            CJD: JJD26997_0254(xth)
            CFF: CFF8240_1722(xth)
            CCV: CCV52592_0089(xth)
            CHA: CHAB381_1629(xth)
            CCO: CCC13826_1799(xth)
            ABU: Abu_0821(xth)
            NIS: NIS_1148(xthA)
            SUN: SUN_0644(xthA)
            GSU: GSU1539(xth)
            PCA: Pcar_2379
            DVU: DVU3259(xth)
            DDE: Dde_0551
            LIP: LI0839(xthA)
            BBA: Bd3524 Bd3670(exoA)
            DPS: DP2416(exoA)
            ADE: Adeh_0431
            AFW: Anae109_4139
            MXA: MXAN_3970(xth) MXAN_5178(xth)
            SAT: SYN_00429
            SFU: Sfum_2331
            RPR: RP260 RP676
            RTY: RT0251(xthA1) RT0671(xthA2)
            RCO: RC0346(xthA1) RC1028(xthA2)
            RFE: RF_0250(xth2) RF_1021(xth1)
            RBE: RBE_0205(xth2) RBE_0258(xth1)
            RCM: A1E_01495
            OTS: OTBS_1662(xth1) OTBS_1807(xth1) OTBS_2114(xth1)
            WOL: WD1001(xth)
            WBM: Wbm0729
            AMA: AM591(xthA2)
            APH: APH_0471 APH_0505(xth)
            ERU: Erum3810(exoA)
            ERW: ERWE_CDS_03930(xthA)
            ERG: ERGA_CDS_03890(xthA)
            ECN: Ecaj_0371
            ECH: ECH_0675(xth)
            NSE: NSE_0415(xth)
            PUB: SAR11_0967(xthA)
            MLO: mll2070 mll4241 mlr1096
            MES: Meso_1085 Meso_1686 Meso_3233
            SME: SMb20689(xthA4) SMc00956(xthA1) SMc02077(xthA2)
                 SMc03818(xthA3)
            ATU: Atu1714 Atu2761 Atu5048
            ATC: AGR_C_3151 AGR_C_5007(xthA1) AGR_pAT_63
            RET: RHE_CH00732 RHE_CH01731(xthA1) RHE_CH01815(xthA2)
                 RHE_CH03970(xthA3)
            RLE: RL1832(exoA) RL2038(xthA) RL4561(xthA)
            BME: BMEI0068 BMEI1093
            BMF: BAB1_0892(xth-1) BAB1_2004
            BMS: BR0873(xth-1) BR2004(xth-2)
            BMB: BruAb1_0885(xth-1) BruAb1_1979(xth-2)
            BOV: BOV_0864(xth) BOV_1927(xth-2)
            BJA: bll4069 blr0618 blr4761
            BRA: BRADO0181 BRADO3288 BRADO4062(xthA2)
            BBT: BBta_0179 BBta_3799 BBta_4438(xthA2)
            RPA: RPA0281(xthA1) RPA2861(xthA2) RPA3307(xthA3)
            RPB: RPB_0379 RPB_2758 RPB_2898
            RPC: RPC_0278 RPC_1207 RPC_2496
            RPD: RPD_0442 RPD_0579 RPD_2804
            RPE: RPE_0396 RPE_2622 RPE_3647
            NWI: Nwi_0085 Nwi_1810
            NHA: Nham_0092 Nham_1755
            BHE: BH10570(xthA1) BH15490(xthA2)
            BQU: BQ08290(xthA1) BQ12410(xthA2)
            BBK: BARBAKC583_0095(xth1) BARBAKC583_0660(xth2)
                 BARBAKC583_0692(xth3)
            CCR: CC_2011 CC_3706
            SIL: SPO2509(xth) SPO3425
            SIT: TM1040_0053 TM1040_0897
            RSP: RSP_0848(xthA1) RSP_2657(xthA) RSP_3423(xthA1)
            JAN: Jann_0421 Jann_2815
            RDE: RD1_0041(xth) RD1_3171(xth)
            MMR: Mmar10_1920 Mmar10_2948
            HNE: HNE_1935(xth) HNE_3549
            ZMO: ZMO1401 ZMO1699(ex3)
            NAR: Saro_0156 Saro_3190
            SAL: Sala_2180 Sala_2671
            ELI: ELI_11970 ELI_12950
            GOX: GOX1750 GOX2271
            GBE: GbCGDNIH1_1263 GbCGDNIH1_2002
            RRU: Rru_A1784 Rru_A3696
            MAG: amb0018 amb2533
            MGM: Mmc1_2467
            ABA: Acid345_1993
            BSU: BG10046(exoA)
            BAN: BA3868(exoA)
            BAR: GBAA3868(exoA)
            BAA: BA_4343
            BAT: BAS3584
            BCE: BC3739
            BCZ: BCZK3496(exoA)
            BTK: BT9727_3484(exoA)
            BCL: ABC1955(exoA)
            OIH: OB0511
            LMO: lmo1782
            LMF: LMOf2365_1807(exoA)
            LIN: lin1894
            LWE: lwe1800(exoA)
            LLA: L198056(exoA)
            LLC: LACR_0841
            LLM: llmg_1765(exoA)
            SPY: SPy_0412(exoA)
            SPZ: M5005_Spy_0339(exoA) M5005_Spy_1691
            SPM: spyM18_0461
            SPG: SpyM3_0296(exoA)
            SPS: SPs1561
            SPH: MGAS10270_Spy0338(exoA)
            SPI: MGAS10750_Spy0337(exoA)
            SPJ: MGAS2096_Spy0359(exoA)
            SPK: MGAS9429_Spy0342(exoA)
            SPF: SpyM51520(exoA)
            SPA: M6_Spy0365 M6_Spy1697
            SPB: M28_Spy0327(exoA) M28_Spy1677
            SPN: SP_1845
            SPR: spr1660(exoA)
            SPD: SPD_1626(xth)
            SAG: SAG1563(exoA)
            SAN: gbs1616
            SAK: SAK_1581(xth)
            SMU: SMU.1649(exoA)
            STC: str1550(exoA)
            STL: stu1550(exoA)
            SSA: SSA_1706(exoA)
            SGO: SGO_1531(xth)
            LPL: lp_0812(exoA)
            LJO: LJ0036 LJ0609
            LAC: LBA0056(exoA) LBA1699(exoA)
            LSA: LSA1338(exoA)
            LSL: LSL_1490(xthA)
            LDB: Ldb0092(exoA)
            LBU: LBUL_0075
            LBR: LVIS_0679
            LCA: LSEI_1002
            LGA: LGAS_0034
            LRE: Lreu_1090
            EFA: EF2735(exoA)
            OOE: OEOE_1659
            CAC: CAC0222(exoA)
            CPE: CPE1174(exoA)
            CPF: CPF_1377(xth)
            CPR: CPR_1192(xth)
            CTC: CTC01610
            CDF: CD1341(exoA)
            CBO: CBO1480(exoA)
            CBA: CLB_1504(xth)
            CBH: CLC_1516(xth)
            CBF: CLI_1563(xth)
            DSY: DSY4691
            TTE: TTE2226(xthA)
            MTU: Rv0427c(xthA)
            MTC: MT0442(xth)
            MBO: Mb0435c(xthA)
            MBB: BCG_0466c(xthA)
            MPA: MAP3916c(xthA)
            MAV: MAV_4727(xth)
            MSM: MSMEG_0829(xth) MSMEG_1656(xth)
            MGI: Mflv_4873
            MMC: Mmcs_0567
            CGL: NCgl0641(cgl0671) NCgl2645(cgl2741)
            CGB: cg0773 cg3036(xthA)
            CEF: CE0689 CE2579
            CDI: DIP0633 DIP2047
            CJK: jk0259(xthA) jk1691(exoA)
            NFA: nfa53030(xthA) nfa9310
            RHA: RHA1_ro00291
            SCO: SCO3174(SCE87.25c) SCO6341(SC3A7.09)
            SMA: SAV1966(xthA) SAV3628(exoA)
            TWH: TWT444(xthA) TWT685 TWT744
            TWS: TW323(xthA1) TW704 TW756(xthA1)
            LXX: Lxx04460 Lxx23390(xthA)
            CMI: CMM_0475(xthB) CMM_0966(xthA)
            AAU: AAur_0464(xth) AAur_1236(xth)
            PAC: PPA1898
            TFU: Tfu_0258
            FRA: Francci3_1180
            SEN: SACE_3393
            BLO: BL1391
            FNU: FN0047
            RBA: RB8161(exoA)
            BGA: BG0542(exoA)
            BAF: BAPKO_0559(exoA)
            TPA: TP0125
            TDE: TDE1734(xth)
            LIL: LA2516(exoA)
            LIC: LIC11452
            LBJ: LBJ_1669(xthA)
            LBL: LBL_1888(xthA)
            SYN: sll1854(xthA)
            SYW: SYNW1807
            SYC: syc1503_d(xthA)
            SYF: Synpcc7942_2607
            SYD: Syncc9605_0661
            SYE: Syncc9902_1699
            SYG: sync_2056(xth)
            SYR: SynRCC307_1646(xthA)
            SYX: SynWH7803_1819(xthA)
            CYA: CYA_0466(xth)
            CYB: CYB_0231(xth)
            TEL: tlr1785
            GVI: glr0140
            ANA: all5306
            AVA: Ava_2559
            PMA: Pro0483(xthA)
            PMM: PMM0484(xthA)
            PMT: PMT1294(xthA)
            PMN: PMN2A_1817
            PMI: PMT9312_0485
            PMB: A9601_05401(xthA)
            PMC: P9515_05481(xthA)
            PMF: P9303_06981(xthA)
            PMG: P9301_05111(xthA)
            PMH: P9215_05661(xthA)
            PME: NATL1_01631 NATL1_05411(xthA)
            TER: Tery_3564
            BTH: BT_0630
            BFR: BF2560
            BFS: BF2585(exoA)
            PGI: PG0269(xth)
            CHU: CHU_2061(xthA) CHU_3497
            GFO: GFO_3536(exoA)
            FPS: FP0062(xth)
            CTE: CT2136(xth)
            DRA: DR_0354
            DGE: Dgeo_0461 Dgeo_2484
            MMP: MMP1012(exoA)
            MAC: MA2077
            MBA: Mbar_A3242
            MMA: MM_3148
            MSI: Msm_1479
            TAC: Ta1506m
            TVO: TVN0046
            PTO: PTO0627
            RCI: RCIX1223(xthA)
            SSO: SSO2290
            STO: ST1910
            SAI: Saci_0129
STRUCTURES  PDB: 1AKO  1Y97  2IOC  2JC5  2O4G  2O4I  2OA8  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.11.2
            ExPASy - ENZYME nomenclature database: 3.1.11.2
            ExplorEnz - The Enzyme Database: 3.1.11.2
            ERGO genome analysis and discovery system: 3.1.11.2
            BRENDA, the Enzyme Database: 3.1.11.2
///
ENTRY       EC 3.1.11.3                 Enzyme
NAME        exodeoxyribonuclease (lambda-induced);
            lambda exonuclease;
            phage lambda-induced exonuclease;
            Escherichia coli exonuclease IV;
            E. coli exonuclease IV;
            exodeoxyribonuclease IV;
            exonuclease IV
CLASS       Hydrolases;
            Acting on ester bonds;
            Exodeoxyribonucleases producing 5'-phosphomonoesters
REACTION    Exonucleolytic cleavage in the 5'- to 3'-direction to yield
            nucleoside 5'-phosphates
COMMENT     Preference for double-stranded DNA. Does not attack single-strand
            breaks.
REFERENCE   1  [PMID:5256235]
  AUTHORS   Lindahl T, Gally JA, Edelman GM.
  TITLE     Deoxyribonuclease IV: a new exonuclease from mammalian tissues.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 62 (1969) 597-603.
  ORGANISM  rabbit
REFERENCE   2  [PMID:6017737]
  AUTHORS   Little JW.
  TITLE     An exonuclease induced by bacteriophage lambda. II. Nature of the
            enzymatic reaction.
  JOURNAL   J. Biol. Chem. 242 (1967) 679-86.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01143  exodeoxyribonuclease (lambda-induced)
GENES       ECO: b0539(ybcC)
            ECJ: JW0526(ybcC)
            ECS: ECs1174
            ECI: UTI89_C1275
            ECV: APECO1_221
            ECW: EcE24377A_0804(exo)
            STY: STY1016(exo)
            STT: t1924(exo)
            ENT: Ent638_1002
            PHA: PSHAa2757(polA)
            HAR: HEAR2308
STRUCTURES  PDB: 1AVQ  1EXN  1UT5  1UT8  1XO1  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.11.3
            ExPASy - ENZYME nomenclature database: 3.1.11.3
            ExplorEnz - The Enzyme Database: 3.1.11.3
            ERGO genome analysis and discovery system: 3.1.11.3
            BRENDA, the Enzyme Database: 3.1.11.3
            CAS: 37367-70-7
///
ENTRY       EC 3.1.11.4                 Enzyme
NAME        exodeoxyribonuclease (phage SP3-induced);
            phage SP3 DNase;
            DNA 5'-dinucleotidohydrolase;
            deoxyribonucleate 5'-dinucleotidase;
            deoxyribonucleic 5'-dinucleotidohydrolase;
            bacteriophage SP3 deoxyribonuclease;
            deoxyribonucleate 5'-dinucleotidase
CLASS       Hydrolases;
            Acting on ester bonds;
            Exodeoxyribonucleases producing 5'-phosphomonoesters
REACTION    Exonucleolytic cleavage in the 5'- to 3'-direction to yield
            nucleoside 5'-phosphates
COMMENT     Preference for single-stranded DNA.
REFERENCE   1  [PMID:4968633]
  AUTHORS   Trilling DM, Aposhian HV.
  TITLE     Sequential cleavage of dinucleotides from DNA by phage Sp3 DNAse.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 60 (1968) 214-21.
  ORGANISM  bacteriophage SP3
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.11.4
            ExPASy - ENZYME nomenclature database: 3.1.11.4
            ExplorEnz - The Enzyme Database: 3.1.11.4
            ERGO genome analysis and discovery system: 3.1.11.4
            BRENDA, the Enzyme Database: 3.1.11.4
///
ENTRY       EC 3.1.11.5                 Enzyme
NAME        exodeoxyribonuclease V;
            Escherichia coli exonuclease V;
            E. coli exonuclease V;
            gene recBC endoenzyme;
            RecBC deoxyribonuclease;
            gene recBC DNase;
            exonuclease V;
            gene recBCD enzymes
CLASS       Hydrolases;
            Acting on ester bonds;
            Exodeoxyribonucleases producing 5'-phosphomonoesters
REACTION    Exonucleolytic cleavage (in the presence of ATP) in either 5'- to
            3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides
COFACTOR    ATP [CPD:C00002]
COMMENT     Preference for double-stranded DNA. Possesses DNA-dependent ATPase
            activity. Acts endonucleolytically on single-stranded circular DNA.
REFERENCE   1  [PMID:319095]
  AUTHORS   Eichler DC, Lehman IR.
  TITLE     On the role of ATP in phosphodiester bond hydrolysis catalyzed by
            the recBC deoxyribonuclease of Escherichia coli.
  JOURNAL   J. Biol. Chem. 252 (1977) 499-503.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4552016]
  AUTHORS   Goldmark PJ, Linn S.
  TITLE     Purification and properties of the recBC DNase of Escherichia coli
            K-12.
  JOURNAL   J. Biol. Chem. 247 (1972) 1849-60.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4916924]
  AUTHORS   Oishi M.
  TITLE     An ATP-dependent deoxyribonuclease from Escherichia coli with a
            possible role in genetic recombination.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 64 (1969) 1292-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:4332130]
  AUTHORS   Wright M, Buttin G, Hurwitz J.
  TITLE     The isolation and characterization from Escherichia coli of an
            adenosine triphosphate-dependent deoxyribonuclease directed by rec
            B, C genes.
  JOURNAL   J. Biol. Chem. 246 (1971) 6543-55.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01144  exodeoxyribonuclease V
            KO: K03581  exodeoxyribonuclease V alpha subunit
            KO: K03582  exodeoxyribonuclease V beta subunit
            KO: K03583  exodeoxyribonuclease V gamma subunit
GENES       UMA: UM05203.1
            ECO: b2819(recD) b2820(recB) b2822(recC)
            ECJ: JW2787(recD) JW2788(recB) JW2790(recC)
            ECE: Z4136(recD) Z4137(recB) Z4139(recC)
            ECS: ECs3676 ECs3677 ECs3679
            ECC: c3413(recD) c3414(recB) c3416(recC)
            ECI: UTI89_C3220(recD) UTI89_C3221(recB) UTI89_C3223(recC)
            ECP: ECP_2831 ECP_2832 ECP_2834
            ECV: APECO1_3683(recC) APECO1_3685(recB) APECO1_3686(recD)
            ECW: EcE24377A_3139(recD) EcE24377A_3140(recB)
                 EcE24377A_3142(recC)
            ECX: EcHS_A2965(recD) EcHS_A2966(recB) EcHS_A2968(recC)
            STY: STY3131(recD) STY3132(recB) STY3134(recC)
            STT: t2901(recD) t2902(recB) t2904(recC)
            SPT: SPA2858(recD) SPA2859(recB) SPA2861(recC)
            SEC: SC2931(recD) SC2932(recB) SC2934(recC)
            STM: STM2993(recD) STM2994(recB) STM2996(recC)
            YPE: YPO1018(recC) YPO1020(recB) YPO1021(recD)
            YPK: y3163(recD) y3164(recB) y3166(recC)
            YPM: YP_2881(recC) YP_2883(recB) YP_2884(recD)
            YPA: YPA_0490 YPA_0492 YPA_0493
            YPN: YPN_2980 YPN_2981 YPN_2983
            YPP: YPDSF_1694 YPDSF_1695 YPDSF_1697
            YPS: YPTB3024(recD) YPTB3025(recB) YPTB3027(recC)
            YPI: YpsIP31758_0989(recC) YpsIP31758_0991(recB)
                 YpsIP31758_0992(recD)
            SFL: SF2830(recD) SF2831(recB) SF2833(recC)
            SFX: S3027(recD) S3028(recB) S3030(recC)
            SFV: SFV_2897(recD) SFV_2898(recB) SFV_2900(recC)
            SSN: SSON_2976(recD) SSON_2977(recB) SSON_2979(recC)
            SBO: SBO_2709(recD) SBO_2710(recB) SBO_2712(recC)
            SDY: SDY_3036(recD) SDY_3037(recB) SDY_3039(recC)
            ECA: ECA0993(recC) ECA0995(recB) ECA0996(recD)
            PLU: plu0630(recC) plu0632(recB) plu0633(recD)
            BUC: BU453(recC) BU454(recB) BU455(recD)
            BAS: BUsg438(recC) BUsg439(recB) BUsg440(recD)
            BAB: bbp403(recC) bbp404(recB) bbp405(recD)
            BCC: BCc_281(recC) BCc_282(recB) BCc_283(recD)
            WBR: WGLp265(recC) WGLp266(recB)
            SGL: SG1972 SG1973 SG1975
            ENT: Ent638_3262
            KPN: KPN_03228(recD) KPN_03229(recB) KPN_03231(recC)
            SPE: Spro_3813
            BFL: Bfl266(recC) Bfl267(recD) Bfl268(recB)
            BPN: BPEN_274(recC) BPEN_275(recD) BPEN_276(recB)
            HIN: HI0942(recC) HI1321(recB) HI1322(recD)
            HIT: NTHI1113(recC) NTHI1644(recB) NTHI1646(recD)
            HDU: HD0186(recC) HD0626(recD) HD1076(recB)
            HSO: HS_0268(recC) HS_0928(recD) HS_0929(recB)
            PMU: PM0516(recB) PM0517(recD) PM0961(recC)
            MSU: MS0728(recC) MS1098(recD) MS1099(recB)
            APL: APL_0253(recD) APL_0370(recB) APL_1884(recC)
            ASU: Asuc_1183
            XFA: XF0422 XF0423 XF0425
            XFT: PD1651(recD) PD1652(recB) PD1653(recC)
            XCC: XCC4198(recD) XCC4199(recB) XCC4200(recC)
            XCB: XC_4287 XC_4288 XC_4289
            XCV: XCV4441(recD) XCV4442(recB) XCV4443(recC)
            XAC: XAC4335(recD) XAC4336(recB) XAC4337(recC)
            XOO: XOO4469(recD) XOO4470(recB) XOO4471(recC)
            XOM: XOO_4212(XOO4212) XOO_4213(XOO4213) XOO_4214(XOO4214)
            VCH: VC2319 VC2320 VC2322
            VCO: VC0395_A1903(recD) VC0395_A1904(recB) VC0395_A1905(recC)
            VVU: VV1_1795 VV1_1796 VV1_1797
            VVY: VV2613 VV2614 VV2615
            VPA: VP2373 VP2374 VP2375 VPA1266
            VFI: VF0581 VF0582 VF0583
            PPR: PBPRA1815 PBPRA2997 PBPRA2998 PBPRA2999
            PAE: PA4283(recD) PA4284(recB) PA4285(recC)
            PAU: PA14_55660(recD) PA14_55670(recB) PA14_55690(recC)
            PAP: PSPA7_4850(recD) PSPA7_4851(recB) PSPA7_4852(recC)
            PPU: PP_4672(recD) PP_4673(recB) PP_4674(recC)
            PPF: Pput_4536
            PST: PSPTO_0776(recC) PSPTO_0777(recB) PSPTO_0778(recD)
            PSB: Psyr_0680 Psyr_0681 Psyr_0682
            PSP: PSPPH_0694(recC) PSPPH_0695(recB) PSPPH_0696(recD)
            PFL: PFL_0740(recC) PFL_0741(recB) PFL_0742(recD)
            PFO: Pfl_0688 Pfl_0689 Pfl_0690
            PEN: PSEEN0691(recC) PSEEN0692(recB) PSEEN0693(recD)
            PMY: Pmen_1987
            PAR: Psyc_1126(recD) Psyc_1127(recB) Psyc_1128(recC)
            PCR: Pcryo_1290 Pcryo_1291 Pcryo_1292
            PRW: PsycPRwf_1211
            ACI: ACIAD0397(recC) ACIAD0398(recB) ACIAD0399(recD)
            SON: SO_2147(recD) SO_2148(recB) SO_2149(recC)
            SDN: Sden_2351 Sden_2352 Sden_2353
            SFR: Sfri_2533 Sfri_2534 Sfri_2535
            SAZ: Sama_1900 Sama_1901 Sama_1902
            SBL: Sbal_2278 Sbal_2279 Sbal_2280
            SBM: Shew185_2046
            SLO: Shew_2129 Shew_2130 Shew_2131
            SPC: Sputcn32_2112
            SSE: Ssed_1935
            SPL: Spea_2421
            SHE: Shewmr4_1773 Shewmr4_1774 Shewmr4_1775
            SHM: Shewmr7_1851 Shewmr7_1852 Shewmr7_1853
            SHN: Shewana3_2245 Shewana3_2246 Shewana3_2247 Shewana3_2919
            SHW: Sputw3181_1900 Sputw3181_1901 Sputw3181_1902
            ILO: IL2530(recD) IL2531(recB) IL2532(recC)
            CPS: CPS_0188 CPS_2767(recD) CPS_2768(recB) CPS_2769(recC)
            PHA: PSHAa1857(recD) PSHAa1858(recB) PSHAa1859(recC)
            PAT: Patl_1756 Patl_1757 Patl_1758
            PIN: Ping_1458 Ping_1459 Ping_1460
            MAQ: Maqu_0010 Maqu_0011 Maqu_0012
            MCA: MCA0690(recC) MCA0691(recB) MCA0692(recD)
            FTU: FTT1393c(recD) FTT1394c(recB) FTT1397c(recC)
            FTF: FTF1393c(recD) FTF1394c(recB) FTF1397c(recC)
            FTW: FTW_0491(recC) FTW_0494(recB) FTW_0495(recD)
            FTL: FTL_0666 FTL_0669 FTL_0670
            FTH: FTH_0668(recC) FTH_0672(recB) FTH_0673(recD)
            FTA: FTA_0701(recC) FTA_0704(recB) FTA_0705(recD)
            FTN: FTN_1356(recD) FTN_1357(recB) FTN_1359(recC) FTN_1580
            NOC: Noc_0995
            AEH: Mlg_0803 Mlg_0804 Mlg_0805
            HHA: Hhal_1269 Hhal_1270 Hhal_1271
            HCH: HCH_00222(recD) HCH_00223(recB) HCH_00224(recC)
            CSA: Csal_1168 Csal_1169 Csal_1170
            ABO: ABO_1818(recC) ABO_1819(recB) ABO_1820(recD)
            MMW: Mmwyl1_3231
            AHA: AHA_3974(recD) AHA_3975(recB) AHA_3976(recC)
            DNO: DNO_0251(recC) DNO_0408(recD)
            BCI: BCI_0545(recC) BCI_0546(recB) BCI_0547(recD)
            NME: NMB0785 NMB1233 NMB1720
            NMA: NMA0995(recB) NMA1401(recD) NMA1974(recC)
            NMC: NMC0737(recB) NMC1638(recC)
            NGO: NGO0370 NGO0771 NGO1369
            CVI: CV_4073(recD) CV_4076(recB) CV_4077(recC)
            BMA: BMA1768(recD) BMA1769(recB) BMA1769.1(recC)
            BMV: BMASAVP1_A1188(recC) BMASAVP1_A1189(recB)
                 BMASAVP1_A1190(recD)
            BML: BMA10299_A0679(recD) BMA10299_A0680(recB)
                 BMA10299_A0681(recC)
            BMN: BMA10247_0471(recC) BMA10247_0472(recB) BMA10247_0473(recD)
            BXE: Bxe_A2837 Bxe_A2838 Bxe_A2839
            BVI: Bcep1808_1126 Bcep1808_6232
            BUR: Bcep18194_A4322 Bcep18194_A4323 Bcep18194_A4324
            BCN: Bcen_0734 Bcen_0735
            BCH: Bcen2424_1214 Bcen2424_1215 Bcen2424_1216
            BAM: Bamb_1097 Bamb_1098 Bamb_1099
            BPS: BPSL1282 BPSL1283 BPSL1284
            BPM: BURPS1710b_1520(recB) BURPS1710b_1521(recD)
            BPL: BURPS1106A_1389(recC) BURPS1106A_1390(recB)
                 BURPS1106A_1391(recD)
            BPD: BURPS668_1385(recC) BURPS668_1386(recB) BURPS668_1387(recD)
            BTE: BTH_I2850 BTH_I2851(recB) BTH_I2852(recC)
            POL: Bpro_1706
            NET: Neut_1355 Neut_1356 Neut_1357
            EBA: ebA2722(recD) ebA2723(recB) ebA2724(recC)
            AZO: azo3850(recD) azo3851(recB) azo3858(recC)
            HPA: HPAG1_1502
            TDN: Tmden_1852
            ABU: Abu_1382(recD) Abu_2069
            GSU: GSU1533(recC) GSU1534(recB) GSU1535(recD)
            GME: Gmet_1892 Gmet_1893 Gmet_1894
            GUR: Gura_0578
            PPD: Ppro_0186 Ppro_1864 Ppro_2148 Ppro_2149 Ppro_2150
            DVU: DVU0895
            DVL: Dvul_2089
            DDE: Dde_0906 Dde_1922 Dde_2725
            LIP: LI0287(recD)
            DPS: DP1343 DP1344 DP1345
            SAT: SYN_01037 SYN_02551 SYN_02552 SYN_02553
            SFU: Sfum_1909
            OTS: OTBS_0395(recD)
            ERU: Erum6250(recB)
            ERW: ERWE_CDS_06560(recB)
            ECN: Ecaj_0629
            MLO: mll1421
            MES: Meso_1491
            SME: SMc01414
            ATU: Atu2026
            ATC: AGR_C_3671
            RET: RHE_CH00026 RHE_CH00726(traAch) RHE_CH02771(recD)
                 RHE_PA00159(traAa) RHE_PD00170(traAd)
            RLE: RL0026 RL0772(traA) RL3224 pRL70086(traA)
            BME: BMEI0619
            BMF: BAB1_1406
            BMS: BR1387
            BMB: BruAb1_1383
            BJA: blr7041(edrN)
            RPA: RPA1273 RPA2215
            RPB: RPB_1281
            RPC: RPC_0955
            RPD: RPD_3837
            RPE: RPE_0975 RPE_2475
            NWI: Nwi_0594
            NHA: Nham_0686 Nham_2841
            BHE: BH10910
            BQU: BQ08560
            SIL: SPO0373
            SIT: TM1040_3101
            RSP: RSP_0959
            RDE: RD1_0452 RD1_1640
            SAL: Sala_0157 Sala_0158
            GOX: GOX0681
            ACR: Acry_3273 Acry_3541
            MGM: Mmc1_3380
            BSU: BG13789(yrrC)
            BAN: BA4622
            BAR: GBAA4622
            BAA: BA_5063
            BAT: BAS4289
            BCE: BC4389
            BCA: BCE_4477
            BCZ: BCZK4137(recD)
            BCY: Bcer98_3106
            BTK: BT9727_4126(recD)
            BTL: BALH_3976(recD)
            BLI: BL02037(yrrC)
            BLD: BLi02873(yrrC)
            BCL: ABC1588
            BPU: BPUM_2389(recD)
            OIH: OB2012
            GKA: GK2561
            SAU: SA1447
            SAV: SAV1619
            SAM: MW1569
            SAR: SAR1698
            SAS: SAS1555
            SAC: SACOL1674
            SAB: SAB1490c
            SAA: SAUSA300_1576
            SAO: SAOUHSC_01723
            SEP: SE1302
            SER: SERP1183
            SHA: SH1300
            SSP: SSP1142
            LMO: lmo1509
            LMF: LMOf2365_1528
            LIN: lin1544
            LWE: lwe1522
            LLA: L180415(recD)
            LLC: LACR_1903
            LLM: llmg_1922(recD)
            SPY: SPy_1844
            SPZ: M5005_Spy_1566(recD)
            SPM: spyM18_1908
            SPG: SpyM3_1593(recD)
            SPS: SPs0274
            SPH: MGAS10270_Spy1633(recD)
            SPI: MGAS10750_Spy1625(recD)
            SPJ: MGAS2096_Spy1591(recD)
            SPK: MGAS9429_Spy1571(recD)
            SPA: M6_Spy1578
            SPB: M28_Spy1554(recD)
            SPN: SP_0401
            SPR: spr0363(recD)
            SAG: SAG1724
            SAN: gbs1769
            SAK: SAK_1732
            SMU: SMU.1875
            STC: str1767(recD)
            STL: stu1767(recD)
            SSA: SSA_0350(recD)
            LPL: lp_2168(recD)
            LJO: LJ0989
            LAC: LBA0825
            LSA: LSA0805(recD)
            LSL: LSL_0728(recD)
            LDB: Ldb0758(recD)
            LBU: LBUL_0691
            LBR: LVIS_1431
            LCA: LSEI_1295 LSEI_2082
            EFA: EF2663
            OOE: OEOE_1106
            CAC: CAC1143(recD) CAC2854(recD)
            CPE: CPE2175(recD)
            CPF: CPF_2433
            CPR: CPR_2143
            CTC: CTC00322
            CNO: NT01CX_0515
            CTH: Cthe_2249 Cthe_3190
            AMT: Amet_0722
            CHY: CHY_1815
            SWO: Swol_2085
            CSC: Csac_0197
            TTE: TTE0489(recD) TTE2109(recD2)
            MPU: MYPU_7820(recD)
            MMY: MSC_0512(recD) MSC_0649(recD)
            MMO: MMOB0930(recD) MMOB0960(recD)
            MSY: MS53_0617(recD)
            MCP: MCAP_0455
            MFL: Mfl322
            MTU: Rv0629c(recD) Rv0630c(recB) Rv0631c(recC)
            MTC: MT0657(recD) MT0658(recB) MT0659(recC)
            MBO: Mb0645c(recD) Mb0646c(recBb) Mb0647c(recBa) Mb0648c(recC)
            MBB: BCG_0675c(recD) BCG_0677c(recBa) BCG_0678c(recC)
            MPA: MAP4091c(recD) MAP4092c MAP4093c MAP4094c(recC)
            MAV: MAV_4542(recC) MAV_4543(recB) MAV_4544(recD)
            MSM: MSMEG_1325(recD) MSMEG_1327(recB) MSMEG_1328(recC)
            MUL: MUL_0707(recD)
            MVA: Mvan_1208
            MGI: Mflv_5131
            MMC: Mmcs_0897 Mmcs_0900 Mmcs_0901
            MKM: Mkms_0914
            MJL: Mjls_0903
            NFA: nfa25450(recC) nfa25460(recB) nfa25470(recD)
            RHA: RHA1_ro01836 RHA1_ro01837 RHA1_ro01838(recC)
            SCO: SCO2737(SCC57A.08c)
            SMA: SAV5329(recD)
            PAC: PPA1315 PPA1316 PPA1317
            NCA: Noca_0253
            TFU: Tfu_1753
            FRA: Francci3_1552 Francci3_2646
            FAL: FRAAL2853 FRAAL4186
            KRA: Krad_0994
            SEN: SACE_3353
            CTR: CT033(recD_1) CT639(recB) CT640(recC) CT652(recD_2)
            CTA: CTA_0035(recD_1) CTA_0694(recB) CTA_0695(recC)
                 CTA_0707(recD_2)
            CMU: TC0007 TC0008 TC0021 TC0302
            CPN: CPn0123(recD_1) CPn0737(recC) CPn0738(recB) CPn0752(recD_2)
            CPA: CP0007 CP0008 CP0650 CP1120
            CPJ: CPj0123(recD_1) CPj0737(recC) CPj0738(recB) CPj0752(recD_2)
            CPT: CpB0124 CpB0765 CpB0767 CpB0780(recD)
            CCA: CCA00007(recB) CCA00008(recC) CCA00650 CCA01005(recD)
            CAB: CAB007 CAB008 CAB621 CAB975(recD)
            CFE: CF0007(recD1) CF0361(recD2) CF0997 CF0999(recB)
            PCU: pc0008(recC) pc0009(recB) pc0010(recD) pc0689(recD)
            BBU: BB0632(recD) BB0633(recB) BB0634(recC)
            BGA: BG0654(recD) BG0655(recB) BG0656(recC)
            BAF: BAPKO_0675(recD) BAPKO_0676(recB) BAPKO_0677(recC)
            LIL: LA0965(recC) LA0966(recB) LA0967(recD)
            LIC: LIC12685(recD) LIC12686(recB)
            LBJ: LBJ_0683(recD) LBJ_0684(recB) LBJ_0685(recC)
            LBL: LBL_2394(recC) LBL_2395(recB) LBL_2396(recD)
            SYW: SYNW0744 SYNW0914(recC) SYNW0917(recB) SYNW0918(recD)
            SYD: Syncc9605_1650 Syncc9605_1651 Syncc9605_1653 Syncc9605_1924
            SYE: Syncc9902_0741 Syncc9902_1409 Syncc9902_1410 Syncc9902_1411
            SYG: sync_0993 sync_1053(recD) sync_1054(recB) sync_1055(recC)
            SYR: SynRCC307_1555(recC) SynRCC307_1556(recB)
                 SynRCC307_1557(recD)
            SYX: SynWH7803_1507(recC) SynWH7803_1508(recB)
                 SynWH7803_1509(recD)
            GVI: glr0629
            ANA: all7071
            AVA: Ava_B0243
            PMA: Pro1090(recC) Pro1092(recB) Pro1093(recD)
            PMM: PMM1102(recD) PMM1103(recB) PMM1105(recC)
            PMT: PMT1085(recD) PMT1086(recB) PMT1089(recC) PMT1107
            PMN: PMN2A_0643 PMN2A_0645 PMN2A_0646 PMN2A_0679
            PMI: PMT9312_1113 PMT9312_1116
            PMB: A9601_12081(recD) A9601_12091(recB) A9601_12111(recC)
            PMC: P9515_11931(recD) P9515_11941(recB) P9515_11961(recC)
            PMF: P9303_09351 P9303_09591(recC) P9303_09621(recB)
                 P9303_09631(recD)
            PMG: P9301_12091(recD) P9301_12101(recB) P9301_12121(recC)
            PMH: P9215_12381(recD) P9215_12391(recB)
            PME: NATL1_14751(recC) NATL1_14771(recB) NATL1_14781(recD)
                 NATL1_15131
            BTH: BT_3982
            BFR: BF0750
            BFS: BF0679
            PGI: PG1303
            SRU: SRU_0919
            CHU: CHU_2314(recD) CHU_2665(uvrD)
            CTE: CT1068(recC) CT1069(recB) CT1070(recD) CT1402
            CCH: Cag_0763 Cag_0769 Cag_0770 Cag_0847
            CPH: Cpha266_0838 Cpha266_1400 Cpha266_1401 Cpha266_1402
            PVI: Cvib_0913 Cvib_1272
            PLT: Plut_0996 Plut_0997 Plut_0998 Plut_1462
            DRA: DR_1902
            DGE: Dgeo_0826
            AAE: aq_388
            MJA: MJ1519(recD)
STRUCTURES  PDB: 1W36  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.11.5
            ExPASy - ENZYME nomenclature database: 3.1.11.5
            ExplorEnz - The Enzyme Database: 3.1.11.5
            ERGO genome analysis and discovery system: 3.1.11.5
            BRENDA, the Enzyme Database: 3.1.11.5
///
ENTRY       EC 3.1.11.6                 Enzyme
NAME        exodeoxyribonuclease VII;
            Escherichia coli exonuclease VII;
            E. coli exonuclease VII;
            endodeoxyribonuclease VII;
            exonuclease VII
CLASS       Hydrolases;
            Acting on ester bonds;
            Exodeoxyribonucleases producing 5'-phosphomonoesters
REACTION    Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction
            to yield nucleoside 5'-phosphates
COMMENT     Preference for single-stranded DNA.
REFERENCE   1  [PMID:4602029]
  AUTHORS   Chase JW, Richardson CC.
  TITLE     Exonuclease VII of Escherichia coli. Purification and properties.
  JOURNAL   J. Biol. Chem. 249 (1974) 4545-52.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4602030]
  AUTHORS   Chase JW, Richardson CC.
  TITLE     Exonuclease VII of Escherichia coli. Mechanism of action.
  JOURNAL   J. Biol. Chem. 249 (1974) 4553-61.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01145  exodeoxyribonuclease VII
            KO: K03601  exodeoxyribonuclease VII large subunit
            KO: K03602  exodeoxyribonuclease VII small subunit
GENES       ECO: b0422(xseB) b2509(xseA)
            ECJ: JW0412(xseB) JW2493(xseA)
            ECE: Z0525(xseB) Z3773(xseA)
            ECS: ECs0476 ECs3371
            ECC: c0533(xseB) c3028(xseA)
            ECI: UTI89_C0445(xseB) UTI89_C2827(xseA)
            ECP: ECP_0481 ECP_2511
            ECV: APECO1_4017(xseA)
            ECW: EcE24377A_0453(xseB)
            ECX: EcHS_A0493(xseB) EcHS_A2660(xseA)
            STY: STY0463(xseB) STY2753(xseA)
            STT: t0345(xseA) t2439(xseB)
            SPT: SPA0355(xseA) SPA2299(xseB)
            SEC: SC0465(xseB) SC2510(xseA)
            STM: STM0424(xseB) STM2512(xseA)
            YPE: YPO2872(xseA) YPO3175(xseB)
            YPK: y1010(xseB) y1361(xseA)
            YPM: YP_0756(xseB) YP_2738(xseA)
            YPA: YPA_2313 YPA_2669
            YPN: YPN_0913 YPN_1266
            YPP: YPDSF_2217
            YPS: YPTB0941(xseB) YPTB2834(xseA)
            YPI: YpsIP31758_1193(xseA) YpsIP31758_3110(xseB)
            YEN: YE1080(xseA)
            SFL: SF0359(xseB) SF2555(xseA)
            SFX: S0367(xseB) S2727(xseA)
            SFV: SFV_0387(xseB) SFV_2556(xseA)
            SSN: SSON_0399(xseB) SSON_2591(xseA)
            SBO: SBO_0316(xseB) SBO_2533(xseA)
            SDY: SDY_0308(xseB) SDY_2705(xseA)
            ECA: ECA1133(xseB) ECA3210(xseA)
            PLU: plu2714(xseA) plu3885(xseB)
            SGL: SG0658 SG1750
            ENT: Ent638_3000
            SPE: Spro_3597
            HIN: HI0397(xseA) HI1437(xseB)
            HIT: NTHI0518(xseA) NTHI1693(xseB)
            HIP: CGSHiEE_01015(xseA) CGSHiEE_04790
            HIQ: CGSHiGG_01075 CGSHiGG_05165(xseA)
            HDU: HD1323(xseB)
            HSO: HS_0903(xseB) HS_1216(xseA)
            PMU: PM0168(xseA) PM0534(xseB)
            MSU: MS0560(xseA) MS1061(xseB)
            APL: APL_0806(xseB) APL_0817(xseA)
            ASU: Asuc_1776
            XFA: XF0660 XF0755
            XFT: PD1513(xseB) PD1901(xseA)
            XCC: XCC2303(xseA) XCC2599(xseB)
            XCB: XC_1517 XC_1812
            XCV: XCV2607(xseA) XCV2915(xseB)
            XAC: XAC2410(xseA) XAC2761(xseB)
            XOO: XOO2737(xseA) XOO3298(xseB)
            XOM: XOO_2582(XOO2582) XOO_3121(XOO3121)
            VCH: VC0766 VC0891
            VCO: VC0395_A0294(xseA) VC0395_A0414(xseB)
            VVU: VV1_0313 VV1_0420
            VVY: VV0774 VV0870
            VPA: VP0615 VP0688
            VFI: VF0636 VF0713
            PPR: PBPRA0779(xseA) PBPRA0807(xseB)
            PAE: PA3777(xseA) PA4042(xseB)
            PAU: PA14_11570(xseB) PA14_15230(xseA)
            PAP: PSPA7_1059(xseB) PSPA7_1339(xseA)
            PPU: PP_0529(xseB) PP_1027(xseA)
            PPF: Pput_1067
            PST: PSPTO_0700(xseB) PSPTO_1446(xseA)
            PSB: Psyr_0606 Psyr_1259
            PSP: PSPPH_0601(xseB) PSPPH_1331(xseA)
            PFL: PFL_4944(xseA) PFL_5508(xseB)
            PFO: Pfl_4592 Pfl_5005
            PEN: PSEEN0602 PSEEN4397(xseA)
            PMY: Pmen_3490
            PAR: Psyc_1291
            PCR: Pcryo_1091
            PRW: PsycPRwf_1369
            SON: SO_3294(xseA)
            SDN: Sden_1268 Sden_2569
            SFR: Sfri_1136 Sfri_2788
            SAZ: Sama_2360
            SBL: Sbal_2985
            SBM: Shew185_3000
            SLO: Shew_1296
            SPC: Sputcn32_2647
            SSE: Ssed_3125
            SPL: Spea_1312
            SHE: Shewmr4_1233 Shewmr4_2729
            SHM: Shewmr7_1304 Shewmr7_2802
            SHN: Shewana3_1234 Shewana3_2899
            SHW: Sputw3181_1360
            ILO: IL2012(xseA) IL2136(xseB)
            CPS: CPS_1090(xseB) CPS_4244(xseA)
            PHA: PSHAa0647(xseA) PSHAa2364(xseB)
            PAT: Patl_1321 Patl_3121
            SDE: Sde_0198 Sde_1458 Sde_3220
            PIN: Ping_2951
            MAQ: Maqu_1729
            CBU: CBU_0468(xseB) CBU_1243(xseA)
            CBD: COXBU7E912_1327(xseA) COXBU7E912_1610(xseB)
            LPN: lpg0826(xseA) lpg2329(xseB)
            LPF: lpl0857(xseA) lpl2249(xseB)
            LPP: lpp0888(xseA) lpp2277(xseB)
            MCA: MCA0819(xseB) MCA1818(xseA)
            FTU: FTT1190c(xseA)
            FTF: FTF1190c(xseA)
            FTW: FTW_1239(xseA)
            FTL: FTL_0754
            FTH: FTH_0757(xseA)
            FTN: FTN_1168(xseA)
            TCX: Tcr_1209
            NOC: Noc_0612 Noc_2036
            AEH: Mlg_0693 Mlg_0946
            HHA: Hhal_1683
            HCH: HCH_04944(xseA) HCH_05864(xseB)
            CSA: Csal_0718
            ABO: ABO_1852(xseA) ABO_2164(xseB)
            MMW: Mmwyl1_4149
            AHA: AHA_1983(xseA)
            ASA: ASA_1863(xseA)
            RMA: Rmag_0750
            VOK: COSY_0444(xseB) COSY_0695(xseA)
            NME: NMB0262 NMB1363
            NMA: NMA1575(xseA) NMA2225(xseB)
            NMC: NMC0256(xseB)
            NGO: NGO0655 NGO1734
            CVI: CV_2475(recJ) CV_2690(xseB) CV_3564(xseA)
            RSO: RSc2223(xseB) RSc2527(xseA)
            REU: Reut_A0596 Reut_A0880
            REH: H16_A0609(xseA) H16_A2734
            RME: Rmet_0538 Rmet_2617
            BMA: BMA2272(xseA) BMAA0328(xseB)
            BMV: BMASAVP1_1510(xseB) BMASAVP1_A0567(xseA)
            BML: BMA10299_1704(xseB) BMA10299_A1044(xseA)
            BMN: BMA10247_2149(xseA) BMA10247_A0362(xseB)
            BXE: Bxe_A0768 Bxe_B2829
            BVI: Bcep1808_2637 Bcep1808_6808
            BUR: Bcep18194_A5875 Bcep18194_B2213
            BCN: Bcen_1932 Bcen_4488
            BCH: Bcen2424_2544 Bcen2424_3877
            BAM: Bamb_2592 Bamb_3248
            BPS: BPSL0879 BPSS1764(xseB)
            BPM: BURPS1710b_1084(xseA) BURPS1710b_A0844(xseB)
            BPL: BURPS1106A_0932(xseA) BURPS1106A_A2394(xseB)
            BPD: BURPS668_0929(xseA) BURPS668_A2536(xseB)
            BTE: BTH_I0743 BTH_II0612
            PNU: Pnuc_0287
            BPE: BP2762(xseA) BP2800(xseB)
            BPA: BPP2462(xseB) BPP2566(xseA)
            BBR: BB1910(xseB) BB2011(xseA)
            RFR: Rfer_2877 Rfer_3152
            POL: Bpro_1745 Bpro_2946
            PNA: Pnap_1926 Pnap_4878
            AAV: Aave_2567
            AJS: Ajs_2302
            VEI: Veis_4890
            MPT: Mpe_A2482 Mpe_A2633
            HAR: HEAR0277 HEAR2497(xseA)
            MMS: mma_0329(xseB) mma_2585(xseA)
            NEU: NE1159(xseB) NE1172(xseA)
            NET: Neut_1510
            NMU: Nmul_A0234 Nmul_A1030
            EBA: ebA5078(xseA) ebA5815(recJ)
            AZO: azo1200(xseB) azo1467(xseA)
            DAR: Daro_3059 Daro_3211
            TBD: Tbd_0881 Tbd_1511
            MFA: Mfla_1863 Mfla_2131
            HPY: HP0259(xseA)
            HPJ: jhp0243(xseA)
            HPA: HPAG1_0261
            HHE: HH1732(xseA)
            HAC: Hac_1349(xseA) Hac_1742(xseB)
            WSU: WS0566
            TDN: Tmden_0681
            CJE: Cj0325(xseA)
            CJR: CJE0370(xseA)
            CJJ: CJJ81176_0347(xseA)
            CJU: C8J_0302(xseA)
            CJD: JJD26997_1634(xseA)
            CFF: CFF8240_0255(xseA)
            CCV: CCV52592_0981 CCV52592_1675(xseA)
            CHA: CHAB381_1293(xseA)
            CCO: CCC13826_0519
            ABU: Abu_0425(xseA)
            NIS: NIS_0427(xseA) NIS_1275
            SUN: SUN_1789(xseB) SUN_1966(xseA)
            GSU: GSU1766(xseB) GSU1767(xseA)
            GME: Gmet_1848 Gmet_1936
            GUR: Gura_1890
            PCA: Pcar_1669 Pcar_1670
            PPD: Ppro_0178 Ppro_1869 Ppro_2406
            DVU: DVU1346(xseA) DVU1348(xseB)
            DVL: Dvul_1722
            DDE: Dde_2202 Dde_2204
            LIP: LI0405(xseA)
            BBA: Bd0197(xseA) Bd0198(xseB)
            DPS: DP1945 DP2698
            ADE: Adeh_1093
            AFW: Anae109_1132
            MXA: MXAN_4646(xseB) MXAN_4647(xseA)
            SAT: SYN_02458 SYN_02459
            SFU: Sfum_1415 Sfum_1416
            RPR: RP350(xseB) RP675(xseA)
            RTY: RT0339(xseB) RT0669(xseA)
            RCO: RC0475(xseB) RC1026(xseA)
            RFE: RF_0253(xseA) RF_0557(xseB)
            RBE: RBE_0208(xseA) RBE_0766(xseB)
            RAK: A1C_02625 A1C_05220(xseA)
            RBO: A1I_04940 A1I_06785(xseA)
            RCM: A1E_04480(xseA)
            RRI: A1G_02690 A1G_05650(xseA)
            OTS: OTBS_1046(xseB) OTBS_1915(xseA)
            AMA: AM094 AM1327(xseA)
            APH: APH_0079(xseB) APH_1322(xseA)
            ERU: Erum0370(xseA) Erum0371 Erum0372 Erum7560(xseB)
            ERW: ERWE_CDS_00240(xseA) ERWE_CDS_00260(xseA)
                 ERWE_CDS_07960(xseB)
            ERG: ERGA_CDS_00240(xseA) ERGA_CDS_00250(xseA)
                 ERGA_CDS_07870(xseB)
            ECN: Ecaj_0029 Ecaj_0790
            ECH: ECH_0056 ECH_0214
            MLO: mll6896 msr7470
            MES: Meso_0182 Meso_0733
            PLA: Plav_0620
            SME: SMc00378 SMc00970
            SMD: Smed_3498
            ATU: Atu0269(xseA) Atu0747(xseB)
            ATC: AGR_C_1356 AGR_C_461(xseA)
            RET: RHE_CH00276(xseA) RHE_CH00916
            RLE: RL0282(xseA) RL0976(xseB)
            BME: BMEI1503 BMEII0527
            BMF: BAB1_0457(xseB) BAB2_0475
            BMS: BR0431(xseB) BRA0764(xseA)
            BMB: BruAb1_0453(xseB) BruAb2_0468(xseA)
            BOV: BOV_0438(xseB) BOV_A0712(xseA)
            OAN: Oant_2996
            BJA: blr7507 bsl2652
            BRA: BRADO2164(xseB) BRADO6092
            BBT: BBta_1695 BBta_2480(xseB)
            RPA: RPA0953(xseB) RPA1161(xseA)
            RPB: RPB_1859 RPB_4459
            RPC: RPC_1150 RPC_4621
            RPD: RPD_4105 RPD_4304
            RPE: RPE_1068 RPE_4617
            NWI: Nwi_0634 Nwi_2553
            NHA: Nham_0779 Nham_3174
            BHE: BH04340(xseB) BH12220(xseA)
            BQU: BQ03530(xseB) BQ09610(xseA)
            BBK: BARBAKC583_0399(xseB) BARBAKC583_1034(xseA)
            XAU: Xaut_1413
            CCR: CC_2070 CC_2246
            SIL: SPO0249(xseB) SPO1344(xseA)
            SIT: TM1040_1945 TM1040_2922
            RSP: RSP_1136(xseB) RSP_1845(xseA)
            RSH: Rsph17029_0494
            RSQ: Rsph17025_0634
            JAN: Jann_0090 Jann_3300
            RDE: RD1_0550(xseB) RD1_1929(xseA)
            PDE: Pden_4028
            MMR: Mmar10_0628 Mmar10_0846
            HNE: HNE_0920(xseA) HNE_1840(xseB)
            ZMO: ZMO0300(xseA) ZMO0856(xseB)
            NAR: Saro_0171 Saro_2254
            SAL: Sala_2195 Sala_3105
            SWI: Swit_3148
            ELI: ELI_05570 ELI_12710
            GOX: GOX0250 GOX0510 GOX1729
            GBE: GbCGDNIH1_0219 GbCGDNIH1_2298
            ACR: Acry_1331
            RRU: Rru_A0159 Rru_A2617
            MAG: amb0212 amb2902
            MGM: Mmc1_1050 Mmc1_1052
            ABA: Acid345_0279 Acid345_3427
            SUS: Acid_0298
            BSU: BG11712(xseA) BG11713(xseB)
            BHA: BH2782 BH2783
            BAN: BA4403(xseB) BA4404(xseA)
            BAR: GBAA4403(xseB) GBAA4404(xseA)
            BAA: BA_4855 BA_4856
            BAT: BAS4083 BAS4084
            BCE: BC4178 BC4179
            BCA: BCE_4252(xseB) BCE_4253(xseA)
            BCZ: BCZK3932(xseB) BCZK3933(xseA)
            BCY: Bcer98_2873
            BTK: BT9727_3921(xseB) BT9727_3922(xseA)
            BTL: BALH_3787(xseB) BALH_3788(xseA)
            BLI: BL01525(xseB) BL01526(xseA)
            BLD: BLi02600(yqiC) BLi02601(yqiB)
            BCL: ABC2464(xseB) ABC2465(xseA)
            BAY: RBAM_022630(xseA)
            BPU: BPUM_2161(xseB) BPUM_2162(xseA)
            OIH: OB1878 OB1879
            GKA: GK2394 GK2395
            SAU: SA1353 SA1354
            SAV: SAV1522 SAV1523
            SAM: MW1475 MW1476
            SAR: SAR1600 SAR1601
            SAS: SAS1461 SAS1462
            SAC: SACOL1567(xseB) SACOL1568(xseA)
            SAB: SAB1395c SAB1396c
            SAA: SAUSA300_1471(xseB) SAUSA300_1472(xseA)
            SAO: SAOUHSC_01619 SAOUHSC_01620
            SAJ: SaurJH9_1582
            SAH: SaurJH1_1615
            SEP: SE1203 SE1204
            SER: SERP1083(xseB) SERP1084(xseA)
            SHA: SH1392 SH1393
            SSP: SSP1231 SSP1232
            LMO: lmo1361 lmo1362
            LMF: LMOf2365_1378(xseA) LMOf2365_1379(xseB)
            LIN: lin1398 lin1399
            LWE: lwe1376(xseA) lwe1377
            LLA: L0254(xseA) L0255(xseB)
            LLC: LACR_0922 LACR_0923
            LLM: llmg_1691(xseB) llmg_1692(xseA)
            SPY: SPy_1499(xseB) SPy_1500(xseA)
            SPZ: M5005_Spy_1232(xseB) M5005_Spy_1233
            SPM: spyM18_1517 spyM18_1518
            SPG: SpyM3_1155(xseB) SpyM3_1156(xseA)
            SPS: SPs0706 SPs0707
            SPH: MGAS10270_Spy1248(xseB) MGAS10270_Spy1249
            SPI: MGAS10750_Spy1339(xseB) MGAS10750_Spy1340
            SPJ: MGAS2096_Spy1250(xseB) MGAS2096_Spy1251
            SPK: MGAS9429_Spy1226(xseB) MGAS9429_Spy1227
            SPF: SpyM50620(xseA) SpyM50621(xseB)
            SPA: M6_Spy1252 M6_Spy1253
            SPB: M28_Spy1171(xseB) M28_Spy1172
            SPN: SP_1206 SP_1207
            SPR: spr1088(xseB) spr1089(xseA)
            SPD: SPD_1066(xseB) SPD_1067(xseA)
            SAG: SAG0496(xseA) SAG0497(xseB)
            SAN: gbs0542 gbs0543
            SAK: SAK_0597(xseA) SAK_0598(xseB)
            SMU: SMU.580 SMU.581
            STC: str1217(xseB) str1218(xseA)
            STL: stu1217(xseB) stu1218(xseA)
            STE: STER_1184
            SSA: SSA_0674(xseA) SSA_0675(xseB)
            SSU: SSU05_1656
            SSV: SSU98_1666
            SGO: SGO_0693(xseA) SGO_0694(xseB)
            LPL: lp_1600(xseA) lp_1601(xseB)
            LJO: LJ1548 LJ1549
            LAC: LBA1330(xseB) LBA1331(xseA)
            LSA: LSA0677(xseA) LSA0678(xseB)
            LSL: LSL_0534(xseA) LSL_0535(xseB)
            LDB: Ldb1423(xseB) Ldb1424(xseA)
            LBU: LBUL_1318 LBUL_1319
            LBR: LVIS_0976 LVIS_0977
            LCA: LSEI_1637 LSEI_1638
            LGA: LGAS_0752
            LRE: Lreu_1183
            PPE: PEPE_0818
            EFA: EF0979(xseA) EF0980(xseB)
            OOE: OEOE_1236 OEOE_1237
            LME: LEUM_1604
            STH: STH1845 STH1846
            CAC: CAC2081(xseB) CAC2082(xseA)
            CPE: CPE1821(xseB) CPE1822(xseA)
            CPF: CPF_2075(xseB) CPF_2076(xseA)
            CPR: CPR_1789(xseB) CPR_1790(xseA)
            CTC: CTC01578
            CNO: NT01CX_1980(xseA) NT01CX_1981(xseB)
            CTH: Cthe_0833
            CDF: CD1203(xseA) CD1204(xseB)
            CBO: CBO1884(xseB) CBO1885(xseA)
            CBA: CLB_1821(xseB) CLB_1822(xseA)
            CBH: CLC_1828(xseB) CLC_1829(xseA)
            CBF: CLI_1948(xseB) CLI_1949(xseA)
            CBE: Cbei_1703
            CKL: CKL_1228(xseA) CKL_1229(xseB)
            AMT: Amet_2503
            CHY: CHY_1989(xseB) CHY_1990(xseA)
            DSY: DSY2352 DSY2353
            DRM: Dred_1072
            SWO: Swol_0567
            CSC: Csac_2122
            TTE: TTE1294(xseA) TTE1295(xseB)
            MTA: Moth_1514 Moth_1515
            MMY: MSC_0100(xseB) MSC_0101(xseA)
            MCP: MCAP_0056 MCAP_0057(xseA)
            MFL: Mfl330 Mfl331
            MTU: Rv1107c(xseB) Rv1108c(xseA)
            MTC: MT1138(xseB) MT1139(xseA)
            MBO: Mb1137c(xseB) Mb1138c(xseA)
            MBB: BCG_1167c(xseB) BCG_1168c(xseA)
            MLE: ML1940(xseA) ML1941(xseB)
            MPA: MAP2686(xseA) MAP2687(xseB)
            MAV: MAV_1227(xseB) MAV_1228(xseA)
            MSM: MSMEG_5226(xseA) MSMEG_5227(xseB)
            MVA: Mvan_4633
            MGI: Mflv_2077
            MMC: Mmcs_4107 Mmcs_4108
            MKM: Mkms_4183
            MJL: Mjls_4338
            CGL: NCgl0980(cgl1024) NCgl0981(cgl1025)
            CGB: cg1162(xseB) cg1163(xseA)
            CEF: CE1077 CE1078
            CDI: DIP0941(xseB) DIP0942(xseA)
            CJK: jk1450(xseA) jk1451(xseB)
            NFA: nfa47970(xseA) nfa47980(xseB)
            RHA: RHA1_ro05867 RHA1_ro05868
            SCO: SCO5055(SCK7.28c) SCO5056(SCK7.29c)
            SMA: SAV3211(xseA) SAV3212(xseB)
            TWH: TWT643(xseA) TWT644(xseB)
            TWS: TW665(xseA) TW666(xseB)
            LXX: Lxx16750(xseA) Lxx16770(xseB)
            ART: Arth_2835
            AAU: AAur_2810(xseA) AAur_2812(xseB)
            PAC: PPA0568 PPA0569
            NCA: Noca_1074
            TFU: Tfu_0467 Tfu_0468
            FRA: Francci3_3879 Francci3_3880
            FAL: FRAAL6148(xseB) FRAAL6149(xseA)
            ACE: Acel_1875
            KRA: Krad_1122
            SEN: SACE_0935(xseB) SACE_0937(xseA)
            STP: Strop_0878
            BLO: BL1750(xseB) BL1751(xseA)
            BAD: BAD_1217(xseA)
            FNU: FN1066 FN1328
            RBA: RB2146(xseB) RB3598(xseA)
            CTR: CT329(xseA)
            CTA: CTA_0356(xseA) CTA_0357(xseB)
            CMU: TC0605 TC0606
            CPN: CPn1062(xseA)
            CPA: CP0787 CP0788
            CPJ: CPj1062(xseA)
            CPT: CpB1104 CpB1105
            CCA: CCA00306(xseB) CCA00307(xseA)
            CAB: CAB303(xseB) CAB304(xseA)
            CFE: CF0696(xseA) CF0697(xseB)
            PCU: pc0620(xseB) pc0621(xseA)
            TDE: TDE1017(xseA) TDE2066(xseB)
            LIL: LA2356(xseA) LA2357(xseB)
            LIC: LIC11590 LIC11591(xseA)
            LBJ: LBJ_1273(xseB) LBJ_1274(xseA)
            LBL: LBL_1498(xseB) LBL_1499(xseA)
            SYW: SYNW2181 SYNW2182
            SYC: syc1046_c syc1145_c(xseA)
            SYF: Synpcc7942_0368 Synpcc7942_0472
            SYD: Syncc9605_2324 Syncc9605_2325
            SYE: Syncc9902_0366 Syncc9902_0367
            SYG: sync_2530(xseA) sync_2531
            SYR: SynRCC307_0367(xseB) SynRCC307_0368(xseA)
            SYX: SynWH7803_2193(xseA) SynWH7803_2194(xseB)
            CYA: CYA_1975(xseB) CYA_1976(xseA)
            CYB: CYB_0088(xseA) CYB_0089(xseB)
            ANA: all1774(xseA) asl1773(xseB)
            AVA: Ava_0262 Ava_0263
            PMA: Pro0111(xseA) Pro0112(xseB)
            PMT: PMT1641(xseA) PMT1642
            PMN: PMN2A_1460 PMN2A_1461
            PMF: P9303_02381(xseA)
            PME: NATL1_01621(xseA) NATL1_01631
            BTH: BT_3890 BT_3891
            BFR: BF3998 BF3999
            BFS: BF3773 BF3774
            PGI: PG1128(xseA) PG1433
            SRU: SRU_0735(xseB) SRU_0738(xseA)
            CHU: CHU_3316 CHU_3317(xseA)
            FJO: Fjoh_3775
            CTE: CT1828(xseA) CT2214(xseB)
            CCH: Cag_0321 Cag_1872
            CPH: Cpha266_2078
            PVI: Cvib_0405
            PLT: Plut_0164 Plut_0340
            RRS: RoseRS_3173
            RCA: Rcas_2900
            DRA: DR_0186
            DGE: Dgeo_0148
            TMA: TM1768 TM1769
            TPT: Tpet_1056
            TME: Tmel_1916
            FNO: Fnod_1569
            MMP: MMP0731 MMP0732(xseA)
            MMQ: MmarC5_0850
            MMZ: MmarC7_1753
            MVN: Mevan_1603
            MBU: Mbur_1514 Mbur_1515
            MTP: Mthe_1309
            MHU: Mhun_3008 Mhun_3009
            MEM: Memar_1979
            MBN: Mboo_1893
            MSI: Msm_0001
            HMA: pNG6094(xseA1) pNG6095(exoVIIA) rrnB0041(xseA2)
                 rrnB0042(exoVIIB)
            HWA: HQ2032A(xseAs) HQ2033A(xseAl)
STRUCTURES  PDB: 1VP7  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.11.6
            ExPASy - ENZYME nomenclature database: 3.1.11.6
            ExplorEnz - The Enzyme Database: 3.1.11.6
            ERGO genome analysis and discovery system: 3.1.11.6
            BRENDA, the Enzyme Database: 3.1.11.6
///
ENTRY       EC 3.1.13.1                 Enzyme
NAME        exoribonuclease II;
            ribonuclease II;
            ribonuclease Q;
            BN ribonuclease;
            Escherichia coli exo-RNase II;
            RNase II;
            exoribonuclease;
            5'-exoribonuclease
CLASS       Hydrolases;
            Acting on ester bonds;
            Exoribonucleases producing 5'-phosphomonoesters
REACTION    Exonucleolytic cleavage in the 3'- to 5'-direction to yield
            nucleoside 5'-phosphates
COMMENT     Preference for single-stranded RNA. The enzyme processes 3'-terminal
            extra-nucleotides of monomeric tRNA precursors, following the action
            of EC 3.1.26.5 ribonuclease P.
REFERENCE   1  [PMID:4867942]
  AUTHORS   Nossal NG, Singer MF.
  TITLE     The processive degradation of individual polyribonucleotide chains.
            I. Escherichia coli ribonuclease II.
  JOURNAL   J. Biol. Chem. 243 (1968) 913-22.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:364422]
  AUTHORS   Schmidt FJ, McClain WH.
  TITLE     An Escherichia coli ribonuclease which removes an extra nucleotide
            from a biosynthetic intermediate of bacteriophage T4 proline
            transfer RNA.
  JOURNAL   Nucleic. Acids. Res. 5 (1978) 4129-39.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:350582]
  AUTHORS   Shimura Y, Sakano H, Nagawa F.
  TITLE     Specific ribonucleases involved in processing of tRNA precursors of
            Escherichia coli. Partial purification and some properties.
  JOURNAL   Eur. J. Biochem. 86 (1978) 267-81.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:5805304]
  AUTHORS   Sporn MB, Lazarus HM, Smith JM, Henderson WR.
  TITLE     Studies on nuclear exoribonucleases. 3. Isolation and properties of
            the enzyme from normal and malignant tissues of the mouse.
  JOURNAL   Biochemistry. 8 (1969) 1698-706.
  ORGANISM  mouse [GN:mmu]
ORTHOLOGY   KO: K01147  exoribonuclease II
GENES       HSA: 3669(ISG20)
            MMU: 57444(Isg20)
            CFA: 488729(ISG20)
            SSC: 448855(ISG20)
            OSA: 4327498
            PIC: PICST_86849(DIS3)
            TET: TTHERM_00047440
            ECO: b1286(rnb)
            ECJ: JW1279(rnb)
            ECE: Z2514(rnb)
            ECS: ECs1859
            ECC: c1757(rnb)
            ECI: UTI89_C1559(rnb)
            ECP: ECP_1340
            ECV: APECO1_445(rnb)
            ECW: EcE24377A_1491(rnb)
            ECX: EcHS_A1399(rnb)
            STY: STY1350(rnb)
            STT: t1615(rnb)
            SPT: SPA1175(rnb)
            SEC: SC1696(rnb)
            STM: STM1702(rnb)
            YPE: YPO2235(rnb)
            YPK: y2077(rnb)
            YPM: YP_2034(rnb)
            YPA: YPA_1595
            YPN: YPN_1704
            YPP: YPDSF_0899 YPDSF_3594
            YPS: YPTB2157(rnb)
            YPI: YpsIP31758_1904(rnb)
            SFL: SF1291(rnb)
            SFX: S1373(rnb)
            SFV: SFV_1300(rnb)
            SSN: SSON_1854(rnb)
            SBO: SBO_1776(rnb)
            SDY: SDY_1366(rnb)
            ECA: ECA1963(rnb)
            PLU: plu2384(rnb)
            BUC: BU266(rnb)
            BAS: BUsg256(rnb)
            BAB: bbp247(rnb)
            BCC: BCc_168(rnb)
            SGL: SG1514
            ENT: Ent638_0362 Ent638_2180
            SPE: Spro_0438 Spro_2638
            HIT: NTHI2041(rnb)
            HIP: CGSHiEE_03395
            HIQ: CGSHiGG_02410
            HDU: HD1264(rnb)
            HSO: HS_0151(rnr) HS_0661(rnb)
            PMU: PM0181(rnb)
            MSU: MS1468(vacB)
            APL: APL_0757(rnb)
            ASU: Asuc_1066 Asuc_2063
            VCH: VCA0805
            VCO: VC0395_0429(rnb)
            VVU: VV2_0146
            VVY: VVA0656
            VPA: VPA0607
            VFI: VFA0383
            PPR: PBPRB0426
            PPF: Pput_4760
            PFO: Pfl_0532
            PEN: PSEEN4933(rnr)
            PMY: Pmen_0643
            PCR: Pcryo_2420
            PRW: PsycPRwf_2237
            SDN: Sden_0511
            SFR: Sfri_3355
            SAZ: Sama_3067
            SBL: Sbal_3647
            SBM: Shew185_0707
            SLO: Shew_3289
            SPC: Sputcn32_0749
            SSE: Ssed_0752
            SPL: Spea_3590
            SHE: Shewmr4_3264
            SHM: Shewmr7_0683
            SHN: Shewana3_0697
            SHW: Sputw3181_3426
            PHA: PSHAa2480(rnr)
            PAT: Patl_0994 Patl_3785
            SDE: Sde_1054 Sde_1120
            PIN: Ping_2270 Ping_3417
            MAQ: Maqu_2388 Maqu_3792
            FTU: FTT0257
            FTF: FTF0257
            FTL: FTL_0138 FTL_0556
            FTH: FTH_0130
            FTN: FTN_0133
            TCX: Tcr_1490
            NOC: Noc_2897
            AEH: Mlg_0580
            HHA: Hhal_0659
            CSA: Csal_0886 Csal_1225
            MMW: Mmwyl1_1407
            AHA: AHA_0554(rnb)
            BCI: BCI_0297(rnb)
            RMA: Rmag_0530
            REU: Reut_A2072
            REH: H16_A1310(rbn) H16_B0870 H16_B2572
            RME: Rmet_2092
            BMA: BMA2495
            BVI: Bcep1808_1510
            BUR: Bcep18194_A3694 Bcep18194_A4688
            BCN: Bcen_0129 Bcen_1066
            BCH: Bcen2424_0612 Bcen2424_1546
            BAM: Bamb_0513 Bamb_1447
            BPS: BPSL2977
            BPM: BURPS1710b_3494
            BTE: BTH_I1170
            PNU: Pnuc_1271
            RFR: Rfer_1422 Rfer_1976 Rfer_3411
            POL: Bpro_1089 Bpro_2700 Bpro_2925
            PNA: Pnap_2438 Pnap_4011
            AAV: Aave_2988
            AJS: Ajs_2568
            VEI: Veis_1425
            HAR: HEAR1277(rnr) HEAR2755
            NET: Neut_0498 Neut_1619
            NMU: Nmul_A1953
            AZO: azo0939(vacB) azo1818 azo3062(brkB) azo3165
            MFA: Mfla_1234 Mfla_1626
            TDN: Tmden_0543
            GSU: GSU1485
            GUR: Gura_2699
            PPD: Ppro_1172
            DVU: DVU3207
            DVL: Dvul_0774
            DDE: Dde_0173 Dde_2598
            LIP: LI0199 LI0594(rnb)
            BBA: Bd0423(vacB)
            DPS: DP1688
            ADE: Adeh_2432
            AFW: Anae109_1447
            SFU: Sfum_0728
            PLA: Plav_2830
            SME: SMc00734
            SMD: Smed_0931
            RET: RHE_CH03787
            OAN: Oant_3672
            RPB: RPB_2418
            RPC: RPC_2238
            RPD: RPD_3034
            RPE: RPE_3380
            NWI: Nwi_1713
            NHA: Nham_2438
            XAU: Xaut_3864
            SIT: TM1040_2994
            RSH: Rsph17029_2787
            RSQ: Rsph17025_0050
            JAN: Jann_0356
            RDE: RD1_0183(rnr)
            PDE: Pden_2853
            ZMO: ZMO1096(rnr)
            NAR: Saro_1948
            SAL: Sala_1231
            SWI: Swit_4048
            ACR: Acry_0037
            ABA: Acid345_3965
            SUS: Acid_5242 Acid_5497
            BAN: BA5334(vacB)
            BAR: GBAA5334(vacB)
            BAA: BA_0194
            BAT: BAS4956
            BCE: BC5129
            BCA: BCE_5232(vacB)
            BCZ: BCZK4818(vacB)
            BCY: Bcer98_3673
            BTK: BT9727_4808(vacB)
            GKA: GK3044
            SAJ: SaurJH9_0805
            SAH: SaurJH1_0821
            LMF: LMOf2365_2422
            LLA: L0323(vacB1)
            LLC: LACR_1015
            SPH: MGAS10270_Spy0415
            SPI: MGAS10750_Spy0427
            SPJ: MGAS2096_Spy0433
            SPK: MGAS9429_Spy0413
            SPA: M6_Spy0441
            SPB: M28_Spy0402
            SPN: SP_0975
            SPR: spr0878(rnr)
            SMU: SMU.1607(vacB)
            STC: str0625(rnr)
            STL: stu0625(rnr)
            LRE: Lreu_0394
            EFA: EF2617(vacB)
            CPE: CPE1296(rnr)
            CTC: CTC00384
            CTH: Cthe_0146
            CBE: Cbei_0633
            AMT: Amet_3572
            CHY: CHY_0289(rnr)
            SWO: Swol_0280
            CSC: Csac_1321
            MTA: Moth_0273
            MPU: MYPU_3510(vacB)
            MHJ: MHJ_0033(vacB)
            MHP: MHP7448_0037(vacB)
            MSY: MS53_0301(vacB)
            RHA: RHA1_ro08585 RHA1_ro08613
            RXY: Rxyl_1604
            FNU: FN0608
            CTR: CT397(vacB)
            CTA: CTA_0432(vacB)
            CMU: TC0676
            CPN: CPn0504(vacB)
            CPA: CP0249
            CPJ: CPj0504(vacB)
            CPT: CpB0525
            CCA: CCA00240
            CAB: CAB236
            CFE: CF0766(vacB)
            PCU: pc1048(vacB)
            TPA: TP0805
            TDE: TDE1371
            SYN: sll1290(rnb) sll1910(zam)
            SYW: SYNW1224
            SYC: syc0425_c(rnb) syc2184_d(zam)
            SYF: Synpcc7942_1124
            SYD: Syncc9605_1336
            SYE: Syncc9902_1138
            SYG: sync_1336
            CYA: CYA_1213
            CYB: CYB_2552
            TEL: tlr0652
            GVI: gll1448 gll1616
            ANA: all4450 alr1240(zam)
            AVA: Ava_0549 Ava_1322
            PMM: PMM0868
            PMT: PMT0741
            PMB: A9601_09941
            PMC: P9515_09491
            PMF: P9303_14771
            PMG: P9301_09921
            PME: NATL1_10141
            TER: Tery_1511 Tery_3730
            CHU: CHU_0462(rnr)
            FJO: Fjoh_1017
            CCH: Cag_0752
            CPH: Cpha266_1962
            PVI: Cvib_0574
            PLT: Plut_0521
            DRA: DR_0020
            DGE: Dgeo_0032 Dgeo_0460
            TTH: TTC0554 TTC1171
            TTJ: TTHA0910
            TPT: Tpet_0207
            TME: Tmel_1513
            FNO: Fnod_0181
            MMA: MM_0544
            MHU: Mhun_1145
            RCI: RCIX2731(rnb)
STRUCTURES  PDB: 2ID0  2IX0  2IX1  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.13.1
            ExPASy - ENZYME nomenclature database: 3.1.13.1
            ExplorEnz - The Enzyme Database: 3.1.13.1
            ERGO genome analysis and discovery system: 3.1.13.1
            BRENDA, the Enzyme Database: 3.1.13.1
///
ENTRY       EC 3.1.13.2                 Enzyme
NAME        exoribonuclease H;
            retroviral reverse transcriptase RNaseH
CLASS       Hydrolases;
            Acting on ester bonds;
            Exoribonucleases producing 5'-phosphomonoesters
REACTION    Exonucleolytic cleavage to 5'-phosphomonoester oligonucleotides in
            both 5'- to 3'- and 3'- to 5'- directions
COMMENT     Attacks RNA in duplex with DNA strand. Found in certain oncorna
            viruses and animal cells.
REFERENCE   1  [PMID:46925]
  AUTHORS   Verma IM.
  TITLE     Studies on reverse transcriptase of RNA tumor viruses III.
            Properties of purified Moloney murine leukemia virus DNA polymerase
            and associated RNase H.
  JOURNAL   J. Virol. 15 (1975) 843-54.
  ORGANISM  Moloney murine leukemia virus
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.13.2
            ExPASy - ENZYME nomenclature database: 3.1.13.2
            ExplorEnz - The Enzyme Database: 3.1.13.2
            ERGO genome analysis and discovery system: 3.1.13.2
            BRENDA, the Enzyme Database: 3.1.13.2
///
ENTRY       EC 3.1.13.3                 Enzyme
NAME        oligonucleotidase;
            oligoribonuclease
CLASS       Hydrolases;
            Acting on ester bonds;
            Exoribonucleases producing 5'-phosphomonoesters
REACTION    Exonucleolytic cleavage of oligonucleotides to yield nucleoside
            5'-phosphates
COMMENT     Also hydrolyses NAD+ to NMN and AMP.
REFERENCE   1  [PMID:4294333]
  AUTHORS   Futai M, Mizuno D.
  TITLE     A new phosphodiesterase forming nucleoside 5'-monophosphate from rat
            liver. Its partial purification and substrate specificity for
            nicotinamide adenine dinucleotide and oligonucleotides.
  JOURNAL   J. Biol. Chem. 242 (1967) 5301-7.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K05981  
GENES       CVI: CV_2368(orn)
            MMS: mma_0852
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.13.3
            ExPASy - ENZYME nomenclature database: 3.1.13.3
            ExplorEnz - The Enzyme Database: 3.1.13.3
            ERGO genome analysis and discovery system: 3.1.13.3
            BRENDA, the Enzyme Database: 3.1.13.3
            CAS: 37288-23-6
///
ENTRY       EC 3.1.13.4                 Enzyme
NAME        poly(A)-specific ribonuclease;
            3'-exoribonuclease;
            2',3'-exoribonuclease
CLASS       Hydrolases;
            Acting on ester bonds;
            Exoribonucleases producing 5'-phosphomonoesters
REACTION    Exonucleolytic cleavage of poly(A) to 5'-AMP
COMMENT     Cleaves poly(A) in either the single- or double-stranded form.
REFERENCE   1  [PMID:6246077]
  AUTHORS   Schroder HC, Zahn RK, Dose K, Muller WE.
  TITLE     Purification and characterization of a poly(A)-specific
            exoribonuclease from calf thymus.
  JOURNAL   J. Biol. Chem. 255 (1980) 4535-8.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K01148  poly(A)-specific ribonuclease
GENES       HSA: 5073(PARN)
            PTR: 453936(PARN)
            MMU: 74108(Parn)
            CFA: 479839(PARN)
            GGA: 416423(RCJMB04_20e14)
            XLA: 394409(parn-A)
            DRE: 394063(zgc:56067)
            OSA: 4336101
            SCE: YGL094C(PAN2) YKL025C(PAN3)
            AGO: AGOS_ACR172W AGOS_AFL055W
            CAL: CaO19_4010(CaO19.4010)
            CGR: CAGL0H03025g
            AFM: AFUA_2G04650
            TET: TTHERM_00008800
            TCR: 504427.200
STRUCTURES  PDB: 2A1R  2A1S  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.13.4
            ExPASy - ENZYME nomenclature database: 3.1.13.4
            ExplorEnz - The Enzyme Database: 3.1.13.4
            ERGO genome analysis and discovery system: 3.1.13.4
            BRENDA, the Enzyme Database: 3.1.13.4
///
ENTRY       EC 3.1.13.5                 Enzyme
NAME        ribonuclease D;
            RNase D
CLASS       Hydrolases;
            Acting on ester bonds;
            Exoribonucleases producing 5'-phosphomonoesters
REACTION    Exonucleolytic cleavage that removes extra residues from the
            3'-terminus of tRNA to produce 5'-mononucleotides
COMMENT     Requires divalent cations for activity (Mg2+, Mn2+ or Co2+).
            Alteration of the 3'-terminal base has no effect on the rate of
            hydrolysis whereas modification of the 3'-terminal sugar has a major
            effect. tRNA terminating with a 3'-phosphate is completely inactive
            [3]. This enzyme can convert a tRNA precursor into a mature tRNA
            [2].
REFERENCE   1  [PMID:342522]
  AUTHORS   Ghosh RK, Deutscher MP.
  TITLE     Identification of an Escherichia coli nuclease acting on
            structurally altered transfer RNA molecules.
  JOURNAL   J. Biol. Chem. 253 (1978) 997-1000.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:6263885]
  AUTHORS   Cudny H, Zaniewski R, Deutscher MP.
  TITLE     Escherichia coli RNase D. Purification and structural
            characterization of a putative processing nuclease.
  JOURNAL   J. Biol. Chem. 256 (1981) 5627-32.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:6263886]
  AUTHORS   Cudny H, Zaniewski R, Deutscher MP.
  TITLE     Escherichia coli RNase D. Catalytic properties and substrate
            specificity.
  JOURNAL   J. Biol. Chem. 256 (1981) 5633-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:2828310]
  AUTHORS   Zhang JR, Deutscher MP.
  TITLE     Cloning, characterization, and effects of overexpression of the
            Escherichia coli rnd gene encoding RNase D.
  JOURNAL   J. Bacteriol. 170 (1988) 522-7.
  ORGANISM  Escherichia coli [GN:eco]
GENES       PAP: PSPA7_4097(rnd)
            BOV: BOV_0744(rnd)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.13.5
            ExPASy - ENZYME nomenclature database: 3.1.13.5
            ExplorEnz - The Enzyme Database: 3.1.13.5
            ERGO genome analysis and discovery system: 3.1.13.5
            BRENDA, the Enzyme Database: 3.1.13.5
///
ENTRY       EC 3.1.14.1                 Enzyme
NAME        yeast ribonuclease
CLASS       Hydrolases;
            Acting on ester bonds;
            Exoribonucleases producing 3'-phosphomonoesters
REACTION    Exonucleolytic cleavage to nucleoside 3'-phosphates
COMMENT     Similar enzyme: RNase U4.
REFERENCE   1
  AUTHORS   Otaka, Y., Uchida, T. and Sakai, T.
  TITLE     Purification and properties of ribonuclease from yeast.
  JOURNAL   J. Biochem (Tokyo) 54 (1963) 322-327.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.14.1
            ExPASy - ENZYME nomenclature database: 3.1.14.1
            ExplorEnz - The Enzyme Database: 3.1.14.1
            ERGO genome analysis and discovery system: 3.1.14.1
            BRENDA, the Enzyme Database: 3.1.14.1
///
ENTRY       EC 3.1.15.1                 Enzyme
NAME        venom exonuclease;
            venom phosphodiesterase
CLASS       Hydrolases;
            Acting on ester bonds;
            Exonucleases that are active with either ribo- or deoxyribonucleic
            acids and produce 5'-phosphomonoesters
REACTION    Exonucleolytic cleavage in the 3'- to 5'- direction to yield
            nucleoside 5'-phosphates
COMMENT     Preference for single-stranded substrate.
REFERENCE   1
  AUTHORS   Laskowski, M.
  TITLE     , Sr. Pancreatic deoxyribonuclease I.
  JOURNAL   In: Cantoni, G.L. and Davies, D.R. (Eds.), Procedures in Nucleic
            Acid Research, Procedures in Nucleic Acid Research, New York, 1966,
            p. 85-101.
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.15.1
            ExPASy - ENZYME nomenclature database: 3.1.15.1
            ExplorEnz - The Enzyme Database: 3.1.15.1
            ERGO genome analysis and discovery system: 3.1.15.1
            BRENDA, the Enzyme Database: 3.1.15.1
            CAS: 9025-82-5
///
ENTRY       EC 3.1.16.1                 Enzyme
NAME        spleen exonuclease;
            3'-exonuclease;
            spleen phosphodiesterase;
            3'-nucleotide phosphodiesterase;
            phosphodiesterase II
CLASS       Hydrolases;
            Acting on ester bonds;
            Exonucleases that are active with either ribo- or deoxyribonucleic
            acids and produce 3'-phosphomonoesters
REACTION    Exonucleolytic cleavage in the 5'- to 3'-direction to yield
            nucleoside 3'-phosphates
COMMENT     Preference for single-stranded substrate.
REFERENCE   1
  AUTHORS   Bernardi, A. and Bernardi, G.
  TITLE     Spleen acid nuclease.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 4, Academic Press,
            New York, 1971, p. 329-336.
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.16.1
            ExPASy - ENZYME nomenclature database: 3.1.16.1
            ExplorEnz - The Enzyme Database: 3.1.16.1
            ERGO genome analysis and discovery system: 3.1.16.1
            BRENDA, the Enzyme Database: 3.1.16.1
            CAS: 9068-54-6
///
ENTRY       EC 3.1.21.1                 Enzyme
NAME        deoxyribonuclease I;
            pancreatic DNase;
            DNase;
            thymonuclease, dornase;
            dornava;
            dornavac;
            pancreatic deoxyribonuclease;
            pancreatic dornase;
            deoxyribonuclease (pancreatic);
            pancreatic DNase;
            DNAase;
            deoxyribonucleic phosphatase;
            DNase I;
            alkaline deoxyribonuclease;
            alkaline DNase;
            endodeoxyribonuclease I;
            DNA depolymerase;
            Escherichia coli endonuclease I;
            deoxyribonuclease A;
            DNA endonuclease;
            DNA nuclease
CLASS       Hydrolases;
            Acting on ester bonds;
            Endodeoxyribonucleases producing 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage to 5'-phosphodinucleotide and
            5'-phosphooligonucleotide end-products
COMMENT     Preference for double-stranded DNA.
REFERENCE   1  [PMID:16433437]
  AUTHORS   Privat A.
  TITLE     [Pathophysiology and treatment of spinal cord injury]
  JOURNAL   Bull. Acad. Natl. Med. 189 (2005) 1109-17; discussion 1117-8.
REFERENCE   2
  AUTHORS   Kunitz, M.
  TITLE     Isolation of crystalline deoxyribonuclease from beef pancreas.
  JOURNAL   Science 108 (1948) 19-20.
  ORGANISM  cow [GN:bta]
REFERENCE   3
  AUTHORS   Laskowski, M.
  TITLE     , Sr. Venom exonuclease.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 4, Academic Press,
            New York, 1971, p. 313-328.
ORTHOLOGY   KO: K01150  deoxyribonuclease I
GENES       HSA: 1773(DNASE1)
            MMU: 13419(Dnase1)
            RNO: 25633(Dnase1)
            CFA: 403413(DNASE1)
            BTA: 282217(DNASE1)
            SSC: 397051(DNASE1)
            GGA: 395725(DNASE1)
            ECO: b2945(endA)
            ECJ: JW2912(endA)
            ECE: Z4290(endA)
            ECS: ECs3821
            ECC: c3531(endA)
            ECI: UTI89_C0121(usp) UTI89_C3334(endA)
            ECP: ECP_2939
            ECV: APECO1_3576(endA)
            ECW: EcE24377A_3288(endA)
            ECX: EcHS_A3103(endA)
            STY: STY3246(endA)
            STT: t3005(endA)
            SPT: SPA2956(endA)
            SEC: SC3033(endA)
            STM: STM3093(endA)
            YPE: YPO0933(endA)
            YPK: y3316(endA)
            YPM: YP_3510(endA)
            YPA: YPA_0333
            YPN: YPN_3129
            YPP: YPDSF_0583
            YPS: YPTB0150(pys2) YPTB0152(pys2) YPTB3205(endA)
            YPI: YpsIP31758_0839(endA)
            SFL: SF2936(endA)
            SFX: S3140(endA)
            SFV: SFV_2999(endA)
            SSN: SSON_3099(endA)
            SBO: SBO_3045(endA)
            SDY: SDY_3127(endA)
            BUC: BU409(endA)
            BAB: bbp369(endA)
            ENT: Ent638_3349
            SPE: Spro_4024
            VCH: VC0470
            VVU: VV1_1533
            VVY: VV2866
            VPA: VP2609
            VFI: VF0437
            PPR: PBPRA3136(endA)
            PAE: PA1150(pys2) PA2749(endA)
            PAU: PA14_28570(endA)
            PPU: PP_2451(endA-1)
            PPF: Pput_2383 Pput_3242
            PST: PSPTO_2364(endA)
            PSB: Psyr_2148
            PSP: PSPPH_2122(endA)
            PFL: PFL_2097(endA)
            PFO: Pfl_1915
            PEN: PSEEN1949(endA)
            PMY: Pmen_1350
            SON: SO_0833(endA)
            SDN: Sden_2973
            SFR: Sfri_0544
            SAZ: Sama_0576
            SBL: Sbal_3525
            SBM: Shew185_0810 Shew185_4415
            SLO: Shew_3223
            SPC: Sputcn32_3160
            SSE: Ssed_3971
            SPL: Spea_0601
            SHE: Shewmr4_0691
            SHM: Shewmr7_3331
            SHN: Shewana3_3443
            SHW: Sputw3181_0783 Sputw3181_1149
            PHA: PSHAa2879(endA)
            PIN: Ping_2580
            HCH: HCH_05359
            ABO: ABO_2097(endA)
            AHA: AHA_3126
            CVI: CV_0628 CV_1988(endA)
            BPM: BURPS1710b_2716(tatD)
            BPE: BP2566
            BPA: BPP2613
            BBR: BB2056
            PNA: Pnap_0624 Pnap_4374
            NET: Neut_2534 Neut_2614
            EBA: ebA6514(tatD)
            CJR: CJE0256(dns)
            LIP: LI0181
            DPS: DP0291
            MGM: Mmc1_1309 Mmc1_2065 Mmc1_2835
            BPU: BPUM_2907(end1)
            LLM: llmg_0168
            SPZ: M5005_Spy_1169(spd3) M5005_Spy_1415(sdaD2)
                 M5005_Spy_1738(spd)
            SPH: MGAS10270_Spy0598 MGAS10270_Spy0852(spd3)
                 MGAS10270_Spy1807(spd)
            SPI: MGAS10750_Spy0622 MGAS10750_Spy0888(spd3)
                 MGAS10750_Spy1832(spd)
            SPJ: MGAS2096_Spy0602(spd3) MGAS2096_Spy1441(sdaD2)
                 MGAS2096_Spy1771 MGAS2096_Spy1772(spd)
            SPK: MGAS9429_Spy0594(spd1) MGAS9429_Spy1417(sdaD2)
                 MGAS9429_Spy1747(spd)
            SPF: SpyM51702(sdbII)
            SPA: M6_Spy1541 M6_Spy1739
            RBA: RB9212(dnl1)
STRUCTURES  PDB: 1DNK  1EMV  1FR2  1FSJ  1V14  1V15  2A3Z  2A40  2A41  2A42  
                 2D1K  2DNJ  2G7E  2G7F  2GYK  2GZF  3DNI  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.21.1
            ExPASy - ENZYME nomenclature database: 3.1.21.1
            ExplorEnz - The Enzyme Database: 3.1.21.1
            ERGO genome analysis and discovery system: 3.1.21.1
            BRENDA, the Enzyme Database: 3.1.21.1
            CAS: 9003-98-9
///
ENTRY       EC 3.1.21.2                 Enzyme
NAME        deoxyribonuclease IV (phage-T4-induced);
            endodeoxyribonuclease IV (phage T4-induced);
            E. coli endonuclease IV;
            endodeoxyribonuclease;
            redoxyendonuclease;
            deoxriboendonuclease;
            Escherichia coli endonuclease II;
            endonuclease II;
            DNA-adenine-transferase
CLASS       Hydrolases;
            Acting on ester bonds;
            Endodeoxyribonucleases producing 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products
COMMENT     Preference for single-stranded DNA.
REFERENCE   1  [PMID:4895219]
  AUTHORS   Friedberg EC, Goldthwait DA.
  TITLE     Endonuclease II of E. coli. I. Isolation and purification.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 62 (1969) 934-40.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4981786]
  AUTHORS   Friedberg EC, Hadi SM, Goldthwait DA.
  TITLE     Endonuclease II of Escherichia coli. II. Enzyme properties and
            studies on the degradation of alkylated and native deoxyribonucleic
            acid.
  JOURNAL   J. Biol. Chem. 244 (1969) 5879-89.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4944066]
  AUTHORS   Hadi SM, Goldthwait DA.
  TITLE     Endonuclease II of Escherichia coli. Degradation of partially
            depurinated deoxyribonucleic acid.
  JOURNAL   Biochemistry. 10 (1971) 4986-93.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:4310836]
  AUTHORS   Sadowski PD, Hurwitz J.
  TITLE     Enzymatic breakage of deoxyribonucleic acid. I. Purification and
            properties of endonuclease II from T4 phage-infected Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 244 (1969) 6182-91.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01151  deoxyribonuclease IV
GENES       ECU: ECU11_1550i
            ECO: b2159(nfo)
            ECJ: JW2146(nfo)
            ECE: Z3416(nfo)
            ECS: ECs3051
            ECC: c2694(nfo)
            ECI: UTI89_C2434(nfo)
            ECP: ECP_2199
            ECV: APECO1_4393(yeiH)
            ECW: EcE24377A_2456(nfo)
            ECX: EcHS_A2295
            STY: STY2438(nfo)
            STT: t0652(nfo)
            SPT: SPA0648(nfo)
            SEC: SC2219(nfo)
            STM: STM2203(nfo)
            YPE: YPO1306(nfo)
            YPK: y2879(nfo)
            YPM: YP_1286(nfo)
            YPA: YPA_1023
            YPN: YPN_2673
            YPP: YPDSF_2391
            YPS: YPTB1337(nfo)
            YPI: YpsIP31758_2675(nfo)
            SFL: SF2244(nfo)
            SFX: S2373(nfo)
            SFV: SFV_2234(nfo)
            SSN: SSON_2215(nfo)
            SBO: SBO_2168(nfo)
            SDY: SDY_2107(nfo)
            ECA: ECA2726(nfo)
            PLU: plu2857(nfo)
            BUC: BU137(nfo)
            BAS: BUsg130(nfo)
            BAB: bbp128(nfo)
            BCC: BCc_087(nfo)
            ENT: Ent638_2760
            SPE: Spro_3227
            HDU: HD1062(nfo)
            APL: APL_0358(nfo)
            VCH: VC2360
            VCO: VC0395_A1939(nfo)
            VVU: VV1_0541
            VVY: VV0654
            VPA: VP0498
            VFI: VF2114
            PPR: PBPRA0557
            SLO: Shew_1083
            SSE: Ssed_1179
            SPL: Spea_1070
            AEH: Mlg_1735
            HHA: Hhal_1668
            AHA: AHA_2097
            BCI: BCI_0392(nfo)
            BPM: BURPS1710b_A2610
            WSU: WS1754
            TDN: Tmden_1835
            CFF: CFF8240_1670
            CCV: CCV52592_1487
            CHA: CHAB381_0245
            ABU: Abu_2221(nfo)
            NIS: NIS_0286(nfo)
            SUN: SUN_2249(nfo)
            GSU: GSU0529(nfo)
            GME: Gmet_2994
            GUR: Gura_3914
            PCA: Pcar_3071
            PPD: Ppro_0453
            DVU: DVU1224(nfo)
            DVL: Dvul_1834
            DDE: Dde_2402
            DPS: DP0053
            ADE: Adeh_1050
            AFW: Anae109_1100
            SAT: SYN_01340
            SFU: Sfum_0659
            MGM: Mmc1_1936
            ABA: Acid345_1326
            SUS: Acid_5984
            BSU: BG11665(yqfS)
            BHA: BH1386
            BAN: BA4508(nfo)
            BAR: GBAA4508(nfo)
            BAA: BA_4956
            BAT: BAS4186
            BCE: BC4282
            BCA: BCE_4364
            BCZ: BCZK4034(nfo)
            BCY: Bcer98_3012
            BTK: BT9727_4024(nfo)
            BTL: BALH_3877(nfo)
            BLI: BL03699(nfo)
            BLD: BLi02692(yqfS)
            BCL: ABC1698
            BPU: BPUM_2246
            OIH: OB1938(nfo)
            GKA: GK2474
            SAU: SA1386
            SAV: SAV1557
            SAM: MW1509
            SAR: SAR1634
            SAS: SAS1495
            SAC: SACOL1614(nfo)
            SAB: SAB1429c
            SAA: SAUSA300_1517
            SAO: SAOUHSC_01658
            SAJ: SaurJH9_1615
            SAH: SaurJH1_1649
            SEP: SE1244
            SER: SERP1123(nfo)
            SHA: SH1359
            SSP: SSP1199
            LMO: lmo1449
            LMF: LMOf2365_1468(nfo)
            LIN: lin1487
            LWE: lwe1465(nfo)
            LPL: lp_1976(nfo)
            LSA: LSA0868(nfo)
            LBR: LVIS_0742
            LCA: LSEI_1523
            EFA: EF1736(nfo)
            STH: STH459
            CAC: CAC1632
            CPE: CPE1079
            CTC: CTC01745
            CNO: NT01CX_2317
            CDF: CD0560(nfo)
            CBE: Cbei_0552
            CHY: CHY_1757(nfo)
            DSY: DSY2560 DSY3714
            TTE: TTE1276(nfo)
            MTA: Moth_1124
            MPN: MPN328(nfo)
            MPU: MYPU_6210(nfo)
            MPE: MYPE1190(nfo)
            MGA: MGA_1293(nfo)
            MMY: MSC_0105(nfo)
            MMO: MMOB5480(nfo)
            MHY: mhp065(nfo)
            MHJ: MHJ_0058(nfo)
            MHP: MHP7448_0062(nfo)
            MSY: MS53_0125(nfo)
            MCP: MCAP_0060
            UUR: UU306(nfo)
            POY: PAM454(nfo)
            AYW: AYWB_317(nfo)
            MFL: Mfl333
            MTU: Rv0670(end)
            MTC: MT0699
            MBO: Mb0689(end)
            MBB: BCG_0719(end)
            MLE: ML1889
            MPA: MAP4132(end)
            MVA: Mvan_1261
            MGI: Mflv_5093
            MMC: Mmcs_0972
            MKM: Mkms_0990
            MJL: Mjls_1000
            NFA: nfa46690
            RHA: RHA1_ro01891
            SCO: SCO2111(SC6E10.05)
            SMA: SAV6091(nfo)
            PAC: PPA2235
            NCA: Noca_3090 Noca_4666
            TFU: Tfu_1956
            ACE: Acel_0985
            SEN: SACE_7353(end)
            STP: Strop_3254
            BLO: BL0757
            RXY: Rxyl_1147
            CTR: CT625(nfo)
            CTA: CTA_0678(nfo)
            CMU: TC0914
            CPN: CPn0732(nfo)
            CPA: CP0014
            CPJ: CPj0732(nfo)
            CPT: CpB0760
            CCA: CCA00012(nfo)
            CAB: CAB012
            CFE: CF0993(mviN)
            PCU: pc0345(nfo)
            BTH: BT_4651
            BFR: BF1241
            BFS: BF1191(nfo)
            CTE: CT0316(nfo)
            CCH: Cag_0528
            CPH: Cpha266_1981
            PVI: Cvib_0479
            PLT: Plut_0428
            DET: DET0392
            DEH: cbdb_A340
            RRS: RoseRS_0614
            RCA: Rcas_0549
            TTH: TTC0482
            TTJ: TTHA0834
            AAE: aq_1629(nfo)
            TMA: TM0362
            TPT: Tpet_0556
            TME: Tmel_1402
            FNO: Fnod_0947
            MJA: MJ0133
            MMP: MMP1678(nfo)
            MAC: MA3548
            MBA: Mbar_A2341
            MMA: MM_0460
            MBU: Mbur_2015
            MTP: Mthe_0406
            MHU: Mhun_1782
            MEM: Memar_0638
            MBN: Mboo_0654
            MST: Msp_0992(nfo)
            MSI: Msm_0963
            HAL: VNG0183G(xthA)
            HMA: rrnAC0265(apl) rrnAC2015(xthA)
            HWA: HQ1417A(nfo)
            NPH: NP5118A
            TAC: Ta0891
            TVO: TVN0971
            PTO: PTO0616 PTO1066
            PAB: PAB1103
            PFU: PF0258
            TKO: TK0170
            RCI: RRC305(nfo)
            APE: APE_2104.1
            SSO: SSO2156
            STO: ST2148
            SAI: Saci_0015
            PAI: PAE3257
            NEQ: NEQ077a
STRUCTURES  PDB: 1FZR  1M0D  1M0I  1QTW  1QUM  1XP3  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.21.2
            ExPASy - ENZYME nomenclature database: 3.1.21.2
            ExplorEnz - The Enzyme Database: 3.1.21.2
            ERGO genome analysis and discovery system: 3.1.21.2
            BRENDA, the Enzyme Database: 3.1.21.2
///
ENTRY       EC 3.1.21.3                 Enzyme
NAME        type I site-specific deoxyribonuclease;
            type I restriction enzyme;
            deoxyribonuclease (ATP- and S-adenosyl-L-methionine-dependent);
            restriction-modification system;
            deoxyribonuclease (adenosine triphosphate-hydrolyzing);
            adenosine triphosphate-dependent deoxyribonuclease;
            ATP-dependent DNase;
            type 1 site-specific deoxyribonuclease
CLASS       Hydrolases;
            Acting on ester bonds;
            Endodeoxyribonucleases producing 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage of DNA to give random double-stranded
            fragments with terminal 5'-phosphates; ATP is simultaneously
            hydrolysed
COFACTOR    S-Adenosyl-L-methionine [CPD:C00019]
COMMENT     This is a large group of enzymes which, together with those now
            listed as EC 3.1.21.4 (type II site-specific deoxyribonuclease) and
            EC 3.1.21.5 (type III site-specific deoxyribonuclease), were
            previously listed separately in sub-subclasses EC 3.1.23 and EC
            3.1.24. They have an absolute requirement for ATP (or dATP) and
            S-adenosyl-L-methionine. They recognize specific short DNA sequences
            and cleave at sites remote from the recognition sequence. They are
            multifunctional proteins that also catalyse the reactions of EC
            2.1.1.72 [site-specific DNA-methyltransferase (adenine-specific)]
            and EC 2.1.1.37
REFERENCE   1  [PMID:2159140]
  AUTHORS   Roberts RJ.
  TITLE     Restriction enzymes and their isoschizomers.
  JOURNAL   Nucleic. Acids. Res. 18 Suppl (1990) 2331-65.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01152  type I restriction enzyme
            KO: K01153  type I restriction enzyme, R subunit
            KO: K01154  type I restriction enzyme, S subunit
GENES       PIC: PICST_88383(ADD1.2)
            EHI: 213.t00003
            ECO: b4348(hsdS) b4350(hsdR)
            ECJ: JW4311(hsdS) JW4313(hsdR)
            ECE: Z5948
            ECS: ECs5308
            ECC: c5425
            ECI: UTI89_C5050(hsdS) UTI89_C5053(hsdR)
            ECP: ECP_4678
            ECV: APECO1_2076(hsdR)
            STY: STY4881(hsdS) STY4884(hsdR)
            STT: t4574(hsdS) t4576(hsdR)
            SPT: SPA4345(hsdS) SPA4347(hsdR)
            STM: STM4524(hsdS) STM4526(hsdR)
            YPS: YPTB0535 YPTB0536 YPTB3879
            SFL: SF4366
            SFV: SFV_4367
            SBO: SBO_4158
            ECA: ECA3122(hsdR)
            PLU: plu4320(hsdS) plu4322(hsdR)
            SPE: Spro_4084
            HIN: HI0216(hsdS) HI1285(hsdR) HI1286(hsdS)
            HIT: NTHI0192(hsdS1) NTHI0193(hsdR1) NTHI0315(hsdS2)
                 NTHI0318(hsdR2) NTHI1839(hsdS3) NTHI1843(hsdR3)
            HSO: HS_0556(hsdS) HS_0559(hsdR)
            PMU: PM1538(hsdA) PM1541(hsdR)
            MSU: MS2170(hsdS) MS2171(hsdR)
            APL: APL_0634(hsdS3) APL_0636(hsdR3) APL_1196
            XFA: XF0296 XF2721 XF2722 XF2725 XF2726 XF2739 XF2741
            XFT: PD2070(hsdR) PD2071(hsdS) PD2074(hsdR) PD2075(hsdS)
            XCC: XCC0462(hsdR) XCC0463 XCC2905
            XCB: XC_0476 XC_0477 XC_1204 XC_3180 XC_3181
            XCV: XCV0509(hsdR1) XCV0510(hsdS1) XCV1193(hsdS2) XCV1194(hsdR2)
            XAC: XAC2898(hsdR) XAC2899
            XOO: XOO3452 XOO3461(hsdR-2) XOO3464
            XOM: XOO_3254(XOO3254) XOO_3257(XOO3257) XOO_3260(XOO3260)
                 XOO_3266(XOO3266) XOO_3269(XOO3269)
            VCH: VC1765 VC1768
            VVU: VV1_2037
            VVY: VV0265 VV0813 VV2204
            VPA: VP0395
            VFI: VFA0538 VFA0539
            PPR: PBPRA0883 PBPRA0886(hsdR) PBPRA1804
            PAE: PA2732 PA2734
            PAP: PSPA7_6047
            PPU: PP_4740(hsdR)
            PST: PSPTO_1087 PSPTO_1089
            PSP: PSPPH_0104 PSPPH_0106
            PAR: Psyc_0416 Psyc_0424 Psyc_0878 Psyc_0881(hsdR)
            PCR: Pcryo_0948 Pcryo_0951 Pcryo_1360 Pcryo_1362
            ACI: ACIAD3430 ACIAD3431
            SON: SO_0380(hsdR-1) SO_0382(hsdS-1) SO_4264(hsdS-2)
                 SO_4267(hsdR-2)
            SFR: Sfri_1956 Sfri_2605
            SBL: Sbal_0775
            SPC: Sputcn32_2912
            SHM: Shewmr7_2867
            SHN: Shewana3_2026 Shewana3_2028 Shewana3_2960 Shewana3_2963
                 Shewana3_3790 Shewana3_3793 Shewana3_4163 Shewana3_4164
                 Shewana3_4241 Shewana3_4244
            ILO: IL0643(hsdS) IL0644
            PHA: PSHAa2091(hsdR) PSHAa2093(hsdS)
            MAQ: Maqu_3386
            MCA: MCA0274 MCA0277 MCA0836 MCA0838 MCA1893
            FTH: FTH_0955 FTH_1650(isftu1)
            FTN: FTN_0285 FTN_0707 FTN_0710 FTN_1154 FTN_1155
            TCX: Tcr_0333 Tcr_0334
            NOC: Noc_0448(hsdR) Noc_1205 Noc_1804(hsdR) Noc_1808 Noc_2688
                 Noc_2689 Noc_2909 Noc_3028
            AEH: Mlg_0504
            HCH: HCH_05026(hsdR)
            CSA: Csal_0087
            ABO: ABO_1829(hsdS) ABO_1832(hsdR)
            DNO: DNO_0220(hsdR) DNO_0222(hsdS)
            NME: NMB0835
            NGO: NGO0404 NGO0407 NGO0697
            RSO: RSc3394(RS05975)
            BXE: Bxe_A0222 Bxe_A0223
            BVI: Bcep1808_0004
            BPS: BPSL0945 BPSL0947
            BTE: BTH_I2740
            RFR: Rfer_0028 Rfer_0030 Rfer_1060 Rfer_1062 Rfer_1366 Rfer_1367
                 Rfer_4007 Rfer_4010
            POL: Bpro_1941 Bpro_1944
            PNA: Pnap_4782
            VEI: Veis_3013 Veis_3131
            MPT: Mpe_A0006 Mpe_A0011 Mpe_A2995
            NEU: NE0382(hsdR) NE0384 NE2448 NE2496 NE2499(hsdR) NE2526 NE2527
            NET: Neut_0537
            EBA: ebA2610(hsdS) ebA2612(hsdR) p2A45(hsdR_2)
            AZO: azo0007(hsdS) azo0010(hsdR)
            DAR: Daro_1308(hsdR)
            TBD: Tbd_2685
            MFA: Mfla_1175 Mfla_1215 Mfla_1216 Mfla_2606 Mfla_2607
            HPY: HP0462(hsdS) HP0464(hsdR) HP0790(prrB) HP0846(hsdR)
                 HP0848(hsdS) HP1383 HP1402(hsdR) HP1404(hsdS)
            HPJ: jhp0414(hsdS_1a) jhp0726(hsdS_4) jhp0784(hsdR_2)
                 jhp0785(hsdS_2) jhp1422(hsdS_3a) jhp1424(hsdR_3)
            HPA: HPAG1_0437 HPAG1_0439 HPAG1_0440 HPAG1_0775 HPAG1_0831
                 HPAG1_0832 HPAG1_1462 HPAG1_1466
            HHE: HH1418
            HAC: Hac_1107(hsdR_fragment_1) Hac_1109(hsdR_fragment_3)
                 Hac_1110(hsdR_fragment_4) Hac_1113(hsdS)
            WSU: WS1129(hsdR)
            TDN: Tmden_0948
            CJE: Cj1549c Cj1551c
            CJJ: CJJ81176_1534
            CJD: JJD26997_1853
            CFF: CFF8240_0988
            CCV: CCV52592_1475
            CCO: CCC13826_1410
            NIS: NIS_1703
            PCA: Pcar_0897 Pcar_2923 Pcar_2924
            PPD: Ppro_1854
            DVU: DVU1703
            DDE: Dde_1859 Dde_1860 Dde_2496 Dde_2499 Dde_2869 Dde_2870
                 Dde_3424 Dde_3425
            BBA: Bd3694(hsdR) Bd3695(hsdS)
            ADE: Adeh_2327 Adeh_2328
            SAT: SYN_00495 SYN_00497
            RFE: RF_0918 RF_0919
            RBE: RBE_0402
            SME: SMc02292(hsdR) SMc02295(hsdS)
            RLE: RL1097(hsdS) RL1100(hsdR) pRL110099(hsdS) pRL110101(hsdR)
            BME: BMEII0449 BMEII0450
            BMF: BAB2_0395(hsdR) BAB2_0396(hsdS)
            BMS: BRA0841(hsdS) BRA0842(hsdR)
            BMB: BruAb2_0389(hsdR) BruAb2_0390(hsdS)
            RPB: RPB_3053
            RPC: RPC_3653
            NWI: Nwi_0270 Nwi_1255
            CCR: CC_0621 CC_0623
            SIL: SPO2734(hsdS) SPO2735(hsdR)
            SIT: TM1040_3537 TM1040_3549
            RSP: RSP_3543
            RDE: RD1_2234 RD1_2235 RD1_4054 RD1_4055(hsdR)
            MMR: Mmar10_0160
            HNE: HNE_2539
            GOX: GOX2567 GOX2568
            MGM: Mmc1_0132 Mmc1_0134
            ABA: Acid345_3755 Acid345_3757
            BCE: BC4456 BC4457 BC4458
            BCA: BCE_0840 BCE_0842
            BLI: BL02331 BL02332 BL02388
            BLD: BLi00745 BLi00746 BLi04315
            GKA: GK0346 GK1381 GK1382 GK2905
            SAU: SA0189(hsdR) SA0392(hsdS)
            SAV: SAV0195(hsdR) SAV0432(hsdS)
            SAM: MW0169(hsdR)
            SAR: SAR0196 SAR0434 SAR1898
            SAS: SAS0025 SAS0026 SAS0170
            SAC: SACOL0180 SACOL0477
            SAB: SAB0135
            SAA: SAUSA300_0196(hsdR) SAUSA300_0406
            SAO: SAOUHSC_00162 SAOUHSC_00398
            SAJ: SaurJH9_0180
            SAH: SaurJH1_0185
            SER: SERP2474(hsdR)
            SHA: SH0062(hsdR) SH0118
            SSP: SSP0052 SSP0054
            LIN: lin0521
            LWE: lwe0477(hsdR)
            LLA: L0308(hsdR) L0310(hsdS)
            LLM: llmg_0658(hsdR) llmg_0660(hsdS)
            SPY: SPy_1904(hsdR) SPy_1905(hsdS)
            SPZ: M5005_Spy_1621(hsdR) M5005_Spy_1622(hsdS)
            SPM: spyM18_1974(hsdR) spyM18_1975(hsdS)
            SPG: SpyM3_1642(hsdR) SpyM3_1643(hsdS)
            SPS: SPs1642 SPs1643
            SPH: MGAS10270_Spy1689(hsdR)
            SPI: MGAS10750_Spy1676(hsdR) MGAS10750_Spy1677(hsdS)
            SPJ: MGAS2096_Spy1645(hsdR) MGAS2096_Spy1646(hsdS)
            SPK: MGAS9429_Spy1624(hsdR) MGAS9429_Spy1625(hsdS)
            SPF: SpyM51597
            SPA: M6_Spy1629 M6_Spy1630
            SPB: M28_Spy1610(hsdR) M28_Spy1611(hsdS)
            SPN: SP_0510 SP_0892
            SPR: spr0446(hsdS) spr0448(hsdS) spr0450(hsdR) spr0792(hsdR)
            SMU: SMU.897
            STC: str0705(hsdR1) str0708(hsdS1) str0851 str1660
            STL: stu0705(hsdR1) stu0708(hsdS1) stu0850 stu0851
            SGO: SGO_0554(hsdR) SGO_0557 SGO_0923
            LPL: lp_0938(hsdR) lp_0940(hsdS1)
            LSL: LSL_0915(hsdS) LSL_0920(hsdR)
            LDB: Ldb1051(hsdR) Ldb1053(hsdS1) Ldb1055(hsdS2)
            LCA: LSEI_2095
            STH: STH1908 STH1909
            CPF: CPF_2596(hsdR) CPF_2598(hsdS)
            CNO: NT01CX_2406(hsdR) NT01CX_2407
            CBO: CBO0682(hsdR)
            CKL: CKL_2595 CKL_2596 CKL_2597
            CHY: CHY_0832(hsdR)
            SWO: Swol_0516 Swol_2256
            MTA: Moth_1670
            MPN: MPN089(hsdS) MPN343(H91_orf330) MPN345(hsdR) MPN347(hsdR)
                 MPN507(P02_orf363V) MPN615(hsdS)
            MPU: MYPU_0770(hsdR) MYPU_0780(hsdR) MYPU_0830(hsdS)
                 MYPU_4310(hsdS) MYPU_4320(hsdR) MYPU_4340(hsdS)
                 MYPU_6760(hsdS) MYPU_6770(hsdR) MYPU_6790(hsdS)
            MPE: MYPE8220(hsdR) MYPE8230(hsdR)
            MGA: MGA_0541(hsdR)
            MMO: MMOB2830(hsdR) MMOB2850(hsdS) MMOB2870(hsdS)
            UUR: UU095(hsdR) UU096(hsdS-1) UU097(hsdS-2) UU099(hsdS-3)
            MAV: MAV_3649 MAV_5024
            MMC: Mmcs_0023 Mmcs_0024
            CEF: CE0049 CE0050 CE0258 CE2329
            CDI: DIP2312 DIP2313
            CJK: jk0898(hsdS1) jk0899(hsdR1) jk1251(hsdR2) jk1253(hsdS2)
            NFA: nfa27650(hsdR)
            RHA: RHA1_ro11152(hsdS) RHA1_ro11153(hsdR)
            ART: Arth_0986
            FRA: Francci3_0193 Francci3_0194 Francci3_4011 Francci3_4012
            FAL: FRAAL1375 FRAAL1376 FRAAL3318(hsdS) FRAAL4993 FRAAL4994
            SEN: SACE_0868
            BLO: BL1783(hsdS) BL1785(hsdR)
            RBA: RB10767(hsdS) RB10770(hsdR) RB11371(hsdR) RB11377(hsdS)
                 RB11407(hsdR) RB11622 RB11643(hsdS)
            TDE: TDE0366(hsdR-1) TDE0368 TDE2747(hsdR-2)
            LIL: LA3198(prrB) LA3200
            LIC: LIC10929 LIC10931
            LBJ: LBJ_0302
            LBL: LBL_2774
            SYW: SYNW1659
            SYC: syc0483_c syc0484_c
            SYF: Synpcc7942_1064 Synpcc7942_1065
            TEL: tll2229 tll2230
            ANA: all2687 alr0509 alr0510 alr3473 alr3618 alr4602 alr4604
                 asr4605
            AVA: Ava_1156 Ava_3267 Ava_3273 Ava_3502
            TER: Tery_2422
            BTH: BT_4517 BT_4535 BT_4540
            BFS: BF1079 BF1457 BF1836(hsdR)
            SRU: SRU_1102
            CHU: CHU_2936(hsdR) CHU_2939(hsdS) CHU_3349(hsdR) CHU_3351(hsdS)
                 CHU_3352(hsdS)
            GFO: GFO_0680 GFO_2587
            FJO: Fjoh_4396
            CTE: CT0679(hsdS-1) CT1878(hsdR)
            CCH: Cag_0810 Cag_1124(hsdR) Cag_1523
            DEH: cbdb_A105 cbdb_A106
            DGE: Dgeo_2012 Dgeo_2016
            MJA: MJ0124m MJ0130m MJ1214 MJ1218 MJ1531 MJECL40 MJECL41
            MVN: Mevan_0082
            MAC: MA2106 MA2122 MA2415(hsdS) MA2418(hsdR)
            MBA: Mbar_A1014 Mbar_A1015 Mbar_A2662 Mbar_A3274
            MMA: MM_0430 MM_0431 MM_1661 MM_2204 MM_2292 MM_2293 MM_2705
                 MM_2733 MM_2739 MM_2976 MM_2978 MM_3141
            MBU: Mbur_0509 Mbur_1213 Mbur_1218 Mbur_1841 Mbur_1842
            MHU: Mhun_2781
            MST: Msp_0477 Msp_0484
            HAL: VNG0107G(rmeS) VNG0108G(rmeR)
            PTO: PTO0076 PTO0077
            PAB: PAB2150 PAB2154
            RCI: RCIX1320(hsdS-2) RCIX1321(hsdR-2) RCIX971(hsdR-1)
                 RCIX972(hsdS-1) RCIX974(hsdS-3)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.21.3
            ExPASy - ENZYME nomenclature database: 3.1.21.3
            ExplorEnz - The Enzyme Database: 3.1.21.3
            ERGO genome analysis and discovery system: 3.1.21.3
            BRENDA, the Enzyme Database: 3.1.21.3
            CAS: 37263-09-5
///
ENTRY       EC 3.1.21.4                 Enzyme
NAME        type II site-specific deoxyribonuclease;
            type II restriction enzyme
CLASS       Hydrolases;
            Acting on ester bonds;
            Endodeoxyribonucleases producing 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage of DNA to give specific double-stranded
            fragments with terminal 5'-phosphates
COFACTOR    Magnesium [CPD:C00305]
COMMENT     This is a large group of enzymes which, together with those now
            listed as EC 3.1.21.3 (type 1 site-specific deoxyribonuclease) and
            EC 3.1.21.5.
REFERENCE   1  [PMID:2159140]
  AUTHORS   Roberts RJ.
  TITLE     Restriction enzymes and their isoschizomers.
  JOURNAL   Nucleic. Acids. Res. 18 Suppl (1990) 2331-65.
  ORGANISM  Haemophilus influenzae
ORTHOLOGY   KO: K01155  type II restriction enzyme
GENES       SPE: Spro_0571
            HIN: HI0512(hindIIR) HI1040(ureF) HI1393(hindIIIR)
            HIT: NTHI1786(haeIIR)
            PAR: Psyc_0143(dpnC)
            PCR: Pcryo_0153 Pcryo_2495
            PRW: PsycPRwf_0124
            CPS: CPS_3626(mutH)
            PAT: Patl_0726
            FTA: FTA_1961 FTA_1962
            NME: NMB0726 NMB1032(nlaIVR) NMB1289 NMB1896(dpnC)
            NMA: NMA1499
            VEI: Veis_0524 Veis_3517
            HPY: HP0091(hsdR) HP1209(iceA) HP1366(MBOIIR)
            HPJ: jhp1442
            HPA: HPAG1_1150 HPAG1_1151
            HAC: Hac_0188 Hac_0305
            TDN: Tmden_0128 Tmden_1839
            SFU: Sfum_2533
            SUS: Acid_1688
            SPN: SP_1221 SP_1222 SP_1850
            SPR: spr1101(spnII-interrupted-C) spr1102(spnII-interrupted-N)
                 spr1285 spr1286 spr1665(dpnC)
            SSA: SSA_1716
            CTH: Cthe_1512
            MMY: MSC_0185 MSC_0215(sau96I-like)
            MMO: MMOB3440(dpnII)
            STP: Strop_0105
            ANA: all3631(avaIR)
            PMM: PMM0384(spnII-interrupted-C)
            TER: Tery_4526
            BFR: BF2023
            BFS: BF2077
            CHU: CHU_2648(mutS)
            FPS: FP2273(hpaIIR)
            CCH: Cag_0333
            CPH: Cpha266_1502 Cpha266_1908 Cpha266_2523
            DEB: DehaBAV1_0080
            RRS: RoseRS_1242
            RCA: Rcas_0408 Rcas_4037
            TME: Tmel_0307 Tmel_1481
            MJA: MJ0600
            MMA: MM_0156
            MBN: Mboo_2338
            MST: Msp_0144
STRUCTURES  PDB: 1AZ0  1AZ3  1AZ4  1B94  1B95  1B96  1B97  1BAM  1BGB  1BHM  
                 1BSS  1BSU  1BUA  1CFR  1D02  1DC1  1DMU  1EO3  1EO4  1EON  
                 1EOO  1EOP  1ERI  1ESG  1EV7  1EYU  1F0O  1FIU  1H56  1IAW  
                 1K0Z  1KC6  1KNV  1NA6  1NI0  1PVI  1PVU  1QC9  1RV5  1RVA  
                 1RVB  1RVC  1RVE  1SA3  1SDO  1STX  1SUZ  1SX5  1SX8  1TW8  
                 1TX3  1VRR  1WTD  1WTE  1XHU  1XHV  1YFI  1YNM  2AUD  2B0D  
                 2B0E  2BAM  2C1L  2EZV  2F03  2FKC  2FKH  2FL3  2FLC  2FOK  
                 2GE5  2GIE  2GIG  2GIH  2GII  2GIJ  2IXS  2PVI  2RVE  3BAM  
                 4RVE  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.21.4
            ExPASy - ENZYME nomenclature database: 3.1.21.4
            ExplorEnz - The Enzyme Database: 3.1.21.4
            ERGO genome analysis and discovery system: 3.1.21.4
            BRENDA, the Enzyme Database: 3.1.21.4
///
ENTRY       EC 3.1.21.5                 Enzyme
NAME        type III site-specific deoxyribonuclease;
            type III restriction enzyme;
            restriction-modification system
CLASS       Hydrolases;
            Acting on ester bonds;
            Endodeoxyribonucleases producing 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage of DNA to give specific double-stranded
            fragments with terminal 5'-phosphates
COFACTOR    ATP [CPD:C00002];
            S-Adenosyl-L-methionine [CPD:C00019]
COMMENT     This is a large group of enzymes which, together with those now
            listed as EC 3.1.21.3 (type 1 site-specific deoxyribonuclease) and
            EC 3.1.21.4 (type II site-specific deoxyribonuclease), were
            previously listed separately in sub-subclasses EC 3.1.23 and EC
            3.1.24. They have an absolute requirement for ATP but do not
            hydrolyse it; S-adenosy-L-methionine stimulates the reaction, but is
            not absolutely required. They recognize specific, short DNA
            sequences and cleave a short distance away from the recognition
            sequence. These enzymes exist as complexes with enzymes of similar
            specificity listed under EC 2.1.1.72 [site-specific
            DNA-methyltransferase (adenine-specific)] or EC 2.1.1.73
REFERENCE   1  [PMID:2159140]
  AUTHORS   Roberts RJ.
  TITLE     Restriction enzymes and their isoschizomers.
  JOURNAL   Nucleic. Acids. Res. 18 Suppl (1990) 2331-65.
  ORGANISM  Haemophilus influenzae
ORTHOLOGY   KO: K01156  type III restriction enzyme
GENES       ECC: c5372
            STT: t0871
            SPT: SPA2365(res)
            SEC: SC0399(res)
            STM: STM0358.S(res)
            HIN: HI1055
            HIT: NTHI1216(res)
            HDU: HD1690
            PMU: PM0699
            MSU: MS1027
            APL: APL_0812(res)
            PIN: Ping_2486
            FTU: FTT1579c
            FTF: FTF1579c
            FTL: FTL_0528
            FTH: FTH_0531(res)
            FTN: FTN_1487
            NOC: Noc_2927
            NME: NMB1260
            NMA: NMA1466 NMA1591
            NMC: NMC1193
            NGO: NGO0545 NGO0546
            BMA: BMA2673
            BMV: BMASAVP1_A3281
            BML: BMA10299_A1846
            BMN: BMA10247_2706
            BUR: Bcep18194_A3212
            BCN: Bcen_0043
            BCH: Bcen2424_0027
            BAM: Bamb_0019
            BPS: BPSL0043
            BPM: BURPS1710b_0260(res)
            BPL: BURPS1106A_0047
            BPD: BURPS668_0047
            BTE: BTH_I0042
            BBR: BB0913
            AAV: Aave_0162
            VEI: Veis_3485
            HPY: HP0592(res) HP1521(res)
            HPJ: jhp1410(res_2)
            HPA: HPAG1_1394
            HAC: Hac_0009(res) Hac_1418(res) Hac_1720
            SUN: SUN_0583
            PCA: Pcar_2729
            PPD: Ppro_0236
            DDE: Dde_1742
            SAT: SYN_01824
            MES: Meso_0544
            MGM: Mmc1_0790
            BCA: BCE_1019
            LLC: LACR_2573
            LSL: LSL_1759
            LBR: LVIS_1621
            LCA: LSEI_0585
            CPF: CPF_0362
            CTH: Cthe_0518
            CKL: CKL_3239 CKL_3240
            SWO: Swol_1547
            MMO: MMOB4610
            FNU: FN0417
            BFR: BF1142
            BFS: BF1057
            GFO: GFO_1535(res)
            FPS: FP2167
            CTE: CT0911(res)
            DET: DET1114
            MST: Msp_0473
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.21.5
            ExPASy - ENZYME nomenclature database: 3.1.21.5
            ExplorEnz - The Enzyme Database: 3.1.21.5
            ERGO genome analysis and discovery system: 3.1.21.5
            BRENDA, the Enzyme Database: 3.1.21.5
///
ENTRY       EC 3.1.21.6                 Enzyme
NAME        CC-preferring endodeoxyribonuclease;
            Streptomyces glaucescens exocytoplasmic dodeoxyribonuclease
CLASS       Hydrolases;
            Acting on ester bonds;
            Endodeoxyribonucleases producing 5'-phosphomonoesters
REACTION    endonucleolytic cleavage to give 5'-phosphooligonucleotide
            end-products, with a preference for cleavage within the sequence CC
COMMENT     Prefers CC sites in double-stranded circular and linear DNA. Greater
            affinity for double-stranded than single-stranded DNA. Produces
            nicks, generating double-stranded fragments with 5'- and/or
            3'-protruding single-stranded tails. Requires magnesium ions for
            activity. The endonuclease from Chlorella-like green algae infected
            with NYs-1 virus 4[1] may be the same enzyme.
REFERENCE   1  [PMID:3186439]
  AUTHORS   Xia YN, Morgan R, Schildkraut I, Van Etten JL.
  TITLE     A site-specific single strand endonuclease activity induced by NYs-1
            virus infection of a Chlorella-like green alga.
  JOURNAL   Nucleic. Acids. Res. 16 (1988) 9477-87.
  ORGANISM  NYs-1 virus
REFERENCE   2  [PMID:1533367]
  AUTHORS   Aparicio JF, Freije JM, Lopez-Otin C, Cal S, Sanchez J.
  TITLE     A Streptomyces glaucescens endodeoxyribonuclease which shows a
            strong preference for CC dinucleotide.
  JOURNAL   Eur. J. Biochem. 205 (1992) 695-9.
  ORGANISM  Streptomyces glaucescens
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.21.6
            ExPASy - ENZYME nomenclature database: 3.1.21.6
            ExplorEnz - The Enzyme Database: 3.1.21.6
            ERGO genome analysis and discovery system: 3.1.21.6
            BRENDA, the Enzyme Database: 3.1.21.6
///
ENTRY       EC 3.1.21.7                 Enzyme
NAME        deoxyribonuclease V;
            endodeoxyribonuclease V;
            DNase V;
            Escherichia coli endodeoxyribonuclease V
CLASS       Hydrolases;
            Acting on ester bonds;
            Endodeoxyribonucleases producing 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage at apurinic or apyrimidinic sites to
            products with a 5'-phosphate
COMMENT     Previously classified erroneously as EC 3.1.22.3.
REFERENCE   1  [PMID:14159]
  AUTHORS   Gates FT 3rd, Linn S.
  TITLE     Endonuclease V of Escherichia coli.
  JOURNAL   J. Biol. Chem. 252 (1977) 1647-53.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K05982  deoxyribonuclease V
GENES       ATH: AT4G31150
            TBR: Tb10.6k15.3890
            TCR: 510187.80
            LMA: LmjF36.2330
            EHI: 492.t00004
            ECO: b3998(nfi)
            ECJ: JW5547(nfi)
            ECE: Z5574(nfi)
            ECS: ECs4921
            ECC: c4955(nfi)
            ECI: UTI89_C3821(nfi)
            ECP: ECP_4211
            ECV: APECO1_2477(nfi)
            ECW: EcE24377A_4541(nfi)
            ECX: EcHS_A4232
            STY: STY3717(nfi)
            STT: t3463(nfi)
            SPT: SPA4005(nfi)
            SEC: SC4049(nfi)
            STM: STM4168(nfi)
            YPE: YPO3733(nfi)
            YPK: y0497(nfi)
            YPM: YP_3096(nfi)
            YPA: YPA_3606
            YPN: YPN_0232
            YPP: YPDSF_3731
            YPS: YPTB0295(nfi)
            YPI: YpsIP31758_3848(nfi)
            SFL: SF4070(nfi)
            SFX: S3665(nfi)
            SFV: SFV_4070(nfi)
            SSN: SSON_4171(nfi)
            SBO: SBO_4019(nfi)
            SDY: SDY_3728(nfi)
            ECA: ECA0236(nfi)
            PLU: plu0490(nfi)
            SGL: SG0139
            ENT: Ent638_0211
            SPE: Spro_0288
            XFA: XF1892
            XFT: PD0899(nfi)
            XCC: XCC2713(nfi)
            XCB: XC_1403
            XCV: XCV3030(nfi)
            XAC: XAC2875(nfi)
            XOO: XOO1459(nfi)
            XOM: XOO_1361(XOO1361)
            PMY: Pmen_0899
            SDE: Sde_3125 Sde_3689
            MCA: MCA0045
            NOC: Noc_0217
            AEH: Mlg_2526
            CSA: Csal_1151
            GUR: Gura_0261
            PCA: Pcar_0602
            MXA: MXAN_1503(nfi)
            SAT: SYN_01952
            SFU: Sfum_0258
            BSU: BG12516(ywqL)
            BTK: BT9727_3063
            CAC: CAC0363
            CBE: Cbei_2626 Cbei_4370
            NFA: nfa45770
            SCO: SCO6726(SC5F2A.09)
            SMA: SAV1684
            TFU: Tfu_1400
            SEN: SACE_1342
            STP: Strop_3777
            RXY: Rxyl_2425
            PCU: pc0623(nfi)
            GVI: glr4243
            ANA: all4085
            AVA: Ava_0819
            SRU: SRU_2800(nfi)
            DET: DET0569(nfi)
            DEH: cbdb_A542(nfi)
            DEB: DehaBAV1_0543
            RRS: RoseRS_2758
            RCA: Rcas_2382
            TTH: TTC0982
            TTJ: TTHA1347
            AAE: aq_548
            TMA: TM1865
            TPT: Tpet_0932
            TME: Tmel_1562
            FNO: Fnod_0350
            MTP: Mthe_1279
            MEM: Memar_1932
            MKA: MK1435(nfi)
            AFU: AF0129
            HAL: VNG0363G(nfi)
            HMA: rrnAC0676(nfi)
            HWA: HQ1234A(nfi)
            NPH: NP1158A(nfi)
            PHO: PH0661
            PAB: PAB0916(nfi)
            PFU: PF0987
            TKO: TK0906
            RCI: RRC272(nfi)
            APE: APE_0506
            SSO: SSO2454(nfi)
            STO: ST0581
            SAI: Saci_0544
            MSE: Msed_1366
            PAI: PAE0684
            TPE: Tpen_0682
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.21.7
            ExPASy - ENZYME nomenclature database: 3.1.21.7
            ExplorEnz - The Enzyme Database: 3.1.21.7
            ERGO genome analysis and discovery system: 3.1.21.7
            BRENDA, the Enzyme Database: 3.1.21.7
            CAS: 61970-03-4
///
ENTRY       EC 3.1.22.1                 Enzyme
NAME        deoxyribonuclease II;
            DNase II;
            pancreatic DNase II;
            deoxyribonucleate 3'-nucleotidohydrolase;
            DNase II;
            pancreatic DNase II;
            acid deoxyribonuclease;
            acid DNase
CLASS       Hydrolases;
            Acting on ester bonds;
            Endodeoxyribonucleases producing 3'-phosphomonoesters
REACTION    Endonucleolytic cleavage to nucleoside 3'-phosphates and
            3'-phosphooligonucleotide end-products
COMMENT     Preference for double-stranded DNA.
REFERENCE   1
  AUTHORS   Bernardi, G.
  TITLE     Spleen acid deoxyribonuclease.
  JOURNAL   In: Cantoni, G.L. and Davies, D.R. (Eds.), Procedures in Nucleic
            Acid Research, Procedures in Nucleic Acid Research, New York, 1966,
            p. 102-121.
ORTHOLOGY   KO: K01158  deoxyribonuclease II
GENES       HSA: 1777(DNASE2) 58511(DNASE2B)
            PTR: 469369(DNASE2B)
            MMU: 13423(Dnase2a) 56629(Dnase2b)
            RNO: 59296(Dnase2b)
            CFA: 476697(DNASE2) 479973(DNASE2B)
            BTA: 282218(DNASE2)
            SSC: 397398(DNASE2)
            GGA: 424540(DNASE2B)
            XTR: 496759(dnase2b)
            SPU: 582395(LOC582395)
            DME: Dmel_CG7780(DNaseII)
            CEL: C07B5.5(nuc-1)
            TET: TTHERM_00028670 TTHERM_00028680 TTHERM_00028710
                 TTHERM_00122420
            BPM: BURPS1710b_A1091
            CMI: CMM_1896
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.22.1
            ExPASy - ENZYME nomenclature database: 3.1.22.1
            ExplorEnz - The Enzyme Database: 3.1.22.1
            ERGO genome analysis and discovery system: 3.1.22.1
            BRENDA, the Enzyme Database: 3.1.22.1
            CAS: 9025-64-3
///
ENTRY       EC 3.1.22.2                 Enzyme
NAME        Aspergillus deoxyribonuclease K1;
            Aspergillus DNase K1
CLASS       Hydrolases;
            Acting on ester bonds;
            Endodeoxyribonucleases producing 3'-phosphomonoesters
REACTION    Endonucleolytic cleavage to nucleoside 3'-phosphates and
            3'-phosphooligonucleotide end-products
COMMENT     Preference for single-stranded DNA.
REFERENCE   1  [PMID:4303413]
  AUTHORS   Kato M, Ikeda Y.
  TITLE     On the deoxyribonucleases, K1 and K2, isolated from mycelia of
            Aspergillus oryzae. I. Isolation and purification of DNases K1 and
            K2.
  JOURNAL   J. Biochem. (Tokyo). 64 (1968) 321-8.
  ORGANISM  Aspergillus oryzae [GN:aor]
REFERENCE   2
  AUTHORS   Shishido, K., Kato, M. and Ikeda, Y.
  TITLE     Isolation of thymidylic acid-rich fragments from double-stranded
            deoxyribonucleic acids.
  JOURNAL   J. Biochem. (Tokyo) 65 (1968) 479-481.
  ORGANISM  Aspergillus oryzae [GN:aor]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.22.2
            ExPASy - ENZYME nomenclature database: 3.1.22.2
            ExplorEnz - The Enzyme Database: 3.1.22.2
            ERGO genome analysis and discovery system: 3.1.22.2
            BRENDA, the Enzyme Database: 3.1.22.2
///
ENTRY       EC 3.1.22.3       Obsolete  Enzyme
NAME        Transferred to 3.1.21.7
CLASS       Hydrolases;
            Acting on ester bonds;
            Endodeoxyribonucleases producing 3'-phosphomonoesters
COMMENT     Transferred entry: now EC 3.1.21.7 deoxyribonuclease V (EC 3.1.22.3
            created 1978, deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.22.3
            ExPASy - ENZYME nomenclature database: 3.1.22.3
            ExplorEnz - The Enzyme Database: 3.1.22.3
            ERGO genome analysis and discovery system: 3.1.22.3
            BRENDA, the Enzyme Database: 3.1.22.3
///
ENTRY       EC 3.1.22.4                 Enzyme
NAME        crossover junction endodeoxyribonuclease;
            Hje endonuclease;
            Holliday junction endonuclease CCE1;
            Holliday junction resolvase;
            Holliday junction-cleaving endonuclease;
            Holliday junction-resolving endoribonuclease;
            RusA Holliday junction resolvase;
            RusA endonuclease;
            RuvC endonuclease;
            SpCCe1 Holliday junction resolvase;
            crossover junction endoribonuclease;
            cruciform-cutting endonuclease;
            endo X3;
            endonuclease RuvC;
            endonuclease VII;
            endonuclease X3;
            resolving enzyme CCE1
CLASS       Hydrolases;
            Acting on ester bonds;
            Endodeoxyribonucleases producing 3'-phosphomonoesters
REACTION    Endonucleolytic cleavage at a junction such as a reciprocal
            single-stranded crossover between two homologous DNA duplexes
            (Holliday junction)
COMMENT     The enzyme from Saccharomyces cerevisiae has no endonuclease or
            exonuclease activity on single-stranded or double-stranded DNA
            molecules that do not contain Holliday junctions.
REFERENCE   1  [PMID:9308179]
  AUTHORS   Oldfield C, Pogrebinsky O, Simmonds J, Olson ES, Kulpa CF.
  TITLE     Elucidation of the metabolic pathway for dibenzothiophene
            desulphurization by Rhodococcus sp. strain IGTS8 (ATCC 53968).
  JOURNAL   Microbiology. 143 ( Pt 9) (1997) 2961-73.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:8824253]
  AUTHORS   Shida T, Iwasaki H, Saito A, Kyogoku Y, Shinagawa H.
  TITLE     Analysis of substrate specificity of the RuvC holliday junction
            resolvase with synthetic Holliday junctions.
  JOURNAL   J. Biol. Chem. 271 (1996) 26105-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:9135161]
  AUTHORS   Shah R, Cosstick R, West SC.
  TITLE     The RuvC protein dimer resolves Holliday junctions by a dual
            incision mechanism that involves base-specific contacts.
  JOURNAL   EMBO. J. 16 (1997) 1464-72.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:10471285]
  AUTHORS   Fogg JM, Schofield MJ, White MF, Lilley DM.
  TITLE     Sequence and functional-group specificity for cleavage of DNA
            junctions by RuvC of Escherichia coli.
  JOURNAL   Biochemistry. 38 (1999) 11349-58.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:12499561]
  AUTHORS   Middleton CL, Parker JL, Richard DJ, White MF, Bond CS.
  TITLE     Crystallization and preliminary X-ray diffraction studies of Hje, a
            HolliDay junction resolving enzyme from Sulfolobus solfataricus.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 59 (2003) 171-3.
  ORGANISM  Sulfolobus solfataricus [GN:sso]
ORTHOLOGY   KO: K01159  crossover junction endodeoxyribonuclease
            KO: K05983  
GENES       DME: Dmel_CG3026(mus81)
            ECO: b1863(ruvC)
            ECJ: JW1852(ruvC)
            ECE: Z2915(ruvC)
            ECS: ECs2573
            ECC: c2277(ruvC)
            ECI: UTI89_C2067(ruvC)
            ECP: ECP_1807
            ECV: APECO1_913(ruvC)
            ECW: EcE24377A_0821(rusA) EcE24377A_2093(ruvC)
            ECX: EcHS_A0300(rusA) EcHS_A1956(ruvC)
            STY: STY2106(ruvC)
            STT: t0979(ruvC)
            SPT: SPA0971(ruvC)
            SEC: SC1906(ruvC)
            STM: STM1898(ruvC)
            YPE: YPO2056(ruvC)
            YPK: y2254(ruvC)
            YPM: YP_1899(ruvC)
            YPA: YPA_1438
            YPN: YPN_1533
            YPP: YPDSF_1066
            YPS: YPTB2039(ruvC)
            YPI: YpsIP31758_2032(ruvC)
            SFL: SF1873(ruvC)
            SFX: S1939(ruvC)
            SFV: SFV_1865(ruvC)
            SSN: SSON_1278(ruvC)
            SBO: SBO_1186(ruvC)
            SDY: SDY_1150(ruvC)
            ECA: ECA2493(ruvC)
            PLU: plu2110(ruvC)
            WBR: WGLp114(ruvC)
            SGL: SG1260
            ENT: Ent638_2431
            KPN: KPN_02377(ruvC)
            SPE: Spro_2778
            HIN: HI0314(ruvC)
            HIT: NTHI0432(ruvC)
            HIP: CGSHiEE_01485(ruvC) CGSHiEE_01500(ruvB)
            HDU: HD0593(ruvC)
            HSO: HS_0509(ruvC)
            PMU: PM0978(ruvC)
            MSU: MS0711(ruvC)
            APL: APL_1153(ruvC)
            ASU: Asuc_1801
            XFA: XF1905
            XFT: PD0886(ruvC)
            XCC: XCC3026(ruvC)
            XCB: XC_1132
            XCV: XCV3281(ruvC)
            XAC: XAC3150(ruvC)
            XOO: XOO1660(ruvC)
            XOM: XOO_1544(XOO1544)
            VCH: VC1847(ruvC)
            VCO: VC0395_A1438(ruvC)
            VVU: VV1_2157(ruvC)
            VVY: VV2287(ruvC)
            VPA: VP1048(ruvC)
            VFI: VF0950
            PPR: PBPRA1114(ruvC)
            PAE: PA0965(ruvC)
            PAU: PA14_51800(ruvC)
            PAP: PSPA7_4543(ruvC)
            PPU: PP_1215(ruvC)
            PPF: Pput_1244
            PST: PSPTO_3979(ruvC)
            PSB: Psyr_1408(ruvC)
            PSP: PSPPH_3774(ruvC)
            PFL: PFL_4765(ruvC)
            PFO: Pfl_4409(ruvC)
            PEN: PSEEN4094(ruvC)
            PMY: Pmen_1270
            PAR: Psyc_0699(ruvC)
            PCR: Pcryo_0671
            PRW: PsycPRwf_1433
            ACI: ACIAD2041(ruvC)
            SON: SO_2431(ruvC)
            SDN: Sden_1885
            SFR: Sfri_2182
            SAZ: Sama_1841
            SBL: Sbal_2040
            SBM: Shew185_2305
            SLO: Shew_2077
            SSE: Ssed_2032
            SPL: Spea_2364
            SHE: Shewmr4_1900
            SHM: Shewmr7_2078
            SHN: Shewana3_1955
            SHW: Sputw3181_2071
            ILO: IL1087(ruvC)
            CPS: CPS_2115(ruvC)
            PHA: PSHAa1877(ruvC)
            PAT: Patl_2946
            SDE: Sde_2535
            PIN: Ping_0716
            MAQ: Maqu_1706
            CBU: CBU_1567(ruvC)
            CBD: COXBU7E912_0421(ruvC)
            LPN: lpg1287(ruvC)
            LPF: lpl1250(ruvC)
            LPP: lpp1250(ruvC)
            MCA: MCA1221(ruvC)
            FTU: FTT0656(ruvC)
            FTF: FTF0656(ruvC)
            FTW: FTW_1072(ruvC)
            FTL: FTL_0930
            FTH: FTH_0909(ruvC) FTH_0911(ruvA) FTH_1052(ruvB) FTH_1192
            FTA: FTA_0980(ruvC)
            FTN: FTN_1027(ruvC)
            TCX: Tcr_0892
            NOC: Noc_0138(ruvC)
            AEH: Mlg_2493
            HHA: Hhal_2211
            HCH: HCH_04924(ruvC)
            CSA: Csal_1846
            ABO: ABO_0751(ruvC)
            MMW: Mmwyl1_2188
            AHA: AHA_1301(ruvC)
            DNO: DNO_1178(ruvC)
            BCI: BCI_0314(ruvC)
            NME: NMB1419
            NMA: NMA1631(ruvC)
            NMC: NMC1352(ruvC)
            NGO: NGO0153(ruvC)
            CVI: CV_4225(ruvC)
            RSO: RSc0503(ruvC)
            REU: Reut_A0486(ruvC)
            REH: H16_A0500(ruvC)
            RME: Rmet_0426
            BMA: BMA2355(ruvC)
            BMV: BMASAVP1_A0268(ruvC)
            BML: BMA10299_A1130(ruvC)
            BMN: BMA10247_2534(ruvC)
            BXE: Bxe_A0617
            BUR: Bcep18194_A3776(ruvC)
            BCN: Bcen_0207
            BCH: Bcen2424_0690
            BAM: Bamb_0583
            BPS: BPSL2897(ruvC)
            BPM: BURPS1710b_3405(ruvC)
            BPL: BURPS1106A_3399(ruvC)
            BPD: BURPS668_3364(ruvC)
            BTE: BTH_I1249(ruvC)
            BPE: BP3417(ruvC)
            BPA: BPP3567(ruvC)
            BBR: BB4002(ruvC)
            RFR: Rfer_3417
            POL: Bpro_1083
            MPT: Mpe_A0482
            HAR: HEAR0256(ruvC)
            MMS: mma_0309(ruvC)
            NEU: NE0211(ruvC)
            NET: Neut_0282
            NMU: Nmul_A2721(ruvC)
            EBA: ebA3657(ruvC)
            AZO: azo0571(ruvC)
            DAR: Daro_4063(ruvC)
            TBD: Tbd_2214(ruvC)
            MFA: Mfla_2354
            HPY: HP0877(ruvC)
            HPJ: jhp0811(ruvC)
            HPA: HPAG1_0860
            HHE: HH1111(ruvC)
            HAC: Hac_1242(ruvC)
            WSU: WS2229(ruvC)
            TDN: Tmden_2104
            CJE: Cj1731c(ruvC)
            CJR: CJE1897(ruvC)
            CJJ: CJJ81176_0026(ruvC)
            CJU: C8J_1630(ruvC)
            CJD: JJD26997_2104(ruvC)
            CFF: CFF8240_1822(ruvC)
            CCV: CCV52592_2057(ruvC)
            CHA: CHAB381_1794(ruvC)
            CCO: CCC13826_1854(ruvC)
            ABU: Abu_2335(ruvC)
            GSU: GSU1075(ruvC)
            GME: Gmet_0744
            GUR: Gura_1415
            PCA: Pcar_2336(ruvC)
            PPD: Ppro_2672
            DVU: DVU2258(ruvC)
            DDE: Dde_2324(ruvC)
            LIP: LI0268(ruvC)
            ADE: Adeh_0951
            AFW: Anae109_0992
            MXA: MXAN_4973(ruvC)
            SAT: SYN_02973
            SFU: Sfum_0995
            RPR: RP119(ruvC)
            RTY: RT0017(ruvC)
            RCO: RC0159(ruvC)
            RFE: RF_1173(ruvC)
            RBE: RBE_1178(ruvC)
            RAK: A1C_00880(ruvC) A1C_02910(ruvB)
            RBO: A1I_01390(ruvC) A1I_03990(ruvB)
            RCM: A1E_00630(ruvC)
            RRI: A1G_00915(ruvC) A1G_03025(ruvB)
            OTS: OTBS_1638(ruvC)
            WOL: WD0142(ruvC)
            WBM: Wbm0697(ruvC)
            AMA: AM1299(ruvC)
            APH: APH_0018(ruvC)
            ERU: Erum0160(ruvC)
            ERW: ERWE_CDS_00030(ruvC)
            ERG: ERGA_CDS_00030(ruvC)
            ECN: Ecaj_0008(ruvC)
            ECH: ECH_0028(ruvC)
            NSE: NSE_0955(ruvC)
            PUB: SAR11_0593(ruvC)
            MLO: mll3901(ruvC)
            MES: Meso_3179
            PLA: Plav_2115
            SME: SMc03967(ruvC)
            SMD: Smed_2639
            ATU: Atu3724(ruvC)
            ATC: AGR_L_2221(ruvC)
            RET: RHE_CH03478(ruvC)
            RLE: RL3986(ruvC)
            BME: BMEI0332
            BMF: BAB1_1716
            BMS: BR1704(ruvC)
            BMB: BruAb1_1689(ruvC)
            BOV: BOV_1647(ruvC)
            OAN: Oant_1211
            BJA: blr1535(ruvC)
            BRA: BRADO1144(ruvC)
            BBT: BBta_6909(ruvC)
            RPA: RPA1099(ruvC)
            RPB: RPB_4272(ruvC)
            RPC: RPC_4806
            RPD: RPD_4170
            RPE: RPE_4770
            NWI: Nwi_2726(ruvC)
            NHA: Nham_3523
            BHE: BH14910(ruvC)
            BQU: BQ11890(ruvC)
            BBK: BARBAKC583_0151(ruvC)
            XAU: Xaut_3065
            CCR: CC_3238
            SIL: SPO3117(ruvC)
            SIT: TM1040_2373
            RSP: RSP_0556(ruvC)
            RSH: Rsph17029_2208
            RSQ: Rsph17025_1230
            JAN: Jann_0964
            RDE: RD1_2088(ruvC)
            PDE: Pden_0696
            MMR: Mmar10_2424
            HNE: HNE_0145(ruvC)
            ZMO: ZMO0154(ruvC)
            NAR: Saro_0421
            SAL: Sala_0336
            SWI: Swit_2141
            ELI: ELI_14520
            GOX: GOX1680
            GBE: GbCGDNIH1_1098
            ACR: Acry_2906
            RRU: Rru_A1087
            MAG: amb3219
            MGM: Mmc1_0478
            ABA: Acid345_3618
            BPU: BPUM_2378(yrrK) BPUM_2415(ruvB) BPUM_2416(ruvA)
            STH: STH1159(ruvC)
            CDF: CD2807(ruvC)
            AMT: Amet_2337
            CHY: CHY_1524(ruvC)
            DSY: DSY2468
            SWO: Swol_1433
            CSC: Csac_1564
            TTE: TTE1178(ruvC)
            MTA: Moth_1702(ruvC)
            MTU: Rv2594c(ruvC)
            MTC: MT2671(ruvC)
            MBO: Mb2625c(ruvC)
            MBB: BCG_2617c(ruvC)
            MLE: ML0481(ruvC)
            MPA: MAP1036(ruvC)
            MAV: MAV_3475(ruvC)
            MSM: MSMEG_2943(ruvC)
            MMC: Mmcs_2265
            CGL: NCgl1598(ruvC)
            CGB: cg1871(ruvC)
            CEF: CE1775(rubC)
            CDI: DIP1377(ruvC)
            CJK: jk1056(ruvC)
            NFA: nfa36970(ruvC)
            RHA: RHA1_ro06892(ruvC)
            SCO: SCO1520(ruvC)
            SMA: SAV6833(ruvC)
            TWH: TWT267(ruvC)
            TWS: TW503(ruvC)
            LXX: Lxx10760(ruvC)
            CMI: CMM_1816(ruvC)
            AAU: AAur_2299(ruvC)
            PAC: PPA1158
            TFU: Tfu_2095(ruvC)
            FRA: Francci3_1369(ruvC)
            FAL: FRAAL2139(ruvC)
            KRA: Krad_3056
            SEN: SACE_2021(rubC)
            STP: Strop_1808
            BLO: BL0727(ruvC)
            BAD: BAD_0803(ruvC)
            RXY: Rxyl_1322
            FNU: FN0214(ruvC)
            RBA: RB4673(ruvC)
            CTR: CT502(ruvC)
            CTA: CTA_0550(ruvC)
            CMU: TC0789
            CPN: CPn0621(ruvC)
            CPA: CP0126
            CPJ: CPj0621(ruvC)
            CPT: CpB0647(ruvC)
            CCA: CCA00119(ruvC)
            CAB: CAB118(ruvC)
            CFE: CF0887(ruvC)
            PCU: pc0019(ruvC)
            TPA: TP0517
            TDE: TDE1864(ruvC)
            LIL: LA0723(ruvC)
            LIC: LIC12885(ruvC)
            LBJ: LBJ_0544(ruvC)
            LBL: LBL_2536(ruvC)
            SYN: sll0896(ruvC)
            SYW: SYNW0715(ruvC)
            SYC: syc0740_d(ruvC)
            SYF: Synpcc7942_0798
            SYD: Syncc9605_1953
            SYE: Syncc9902_0712
            SYG: sync_0961(ruvC)
            SYR: SynRCC307_0728(ruvC)
            SYX: SynWH7803_1601(ruvC)
            CYA: CYA_1905(ruvC)
            CYB: CYB_0493(ruvC)
            TEL: tlr1137(ruvC)
            GVI: gll3300(ruvC)
            ANA: all2297(ruvC)
            AVA: Ava_0115(ruvC)
            PMA: Pro1147(ruvC)
            PMM: PMM1054(ruvC)
            PMT: PMT1136(ruvC)
            PMN: PMN2A_0699(ruvC)
            PMI: PMT9312_1065
            PMB: A9601_11591(ruvC)
            PMC: P9515_11451(ruvC)
            PMF: P9303_08941(ruvC)
            PMG: P9301_11601(ruvC)
            PMH: P9215_11891(ruvC)
            PME: NATL1_15331(ruvC)
            TER: Tery_3620
            BTH: BT_1664(ruvC)
            BFR: BF3262(ruvC)
            BFS: BF3101(ruvC)
            PGI: PG1324(ruvC)
            SRU: SRU_2668(ruvC)
            CHU: CHU_2183(ruvC)
            GFO: GFO_0072(ruvC)
            FJO: Fjoh_1377
            FPS: FP0209(ruvC)
            CTE: CT1664(ruvC)
            CCH: Cag_0164(ruvC)
            PLT: Plut_1642(ruvC)
            DET: DET0443(ruvC)
            DEH: cbdb_A399(ruvC)
            DEB: DehaBAV1_0420
            RRS: RoseRS_4363
            RCA: Rcas_0719
            DRA: DR_0440
            DGE: Dgeo_0327
            TTH: TTC0725(ruvC)
            TTJ: TTHA1090
            TMA: TM0575
            TPT: Tpet_0343
            TME: Tmel_1038
            FNO: Fnod_1720
            MHU: Mhun_0890
            RCI: RCIX2628(ruvC)
STRUCTURES  PDB: 1EN7  1HJR  1IPI  2FCO  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.22.4
            ExPASy - ENZYME nomenclature database: 3.1.22.4
            ExplorEnz - The Enzyme Database: 3.1.22.4
            ERGO genome analysis and discovery system: 3.1.22.4
            BRENDA, the Enzyme Database: 3.1.22.4
            CAS: 99676-43-4
///
ENTRY       EC 3.1.22.5                 Enzyme
NAME        deoxyribonuclease X;
            Escherichia coli endodeoxyribonuclease;
            Escherichia coli endodeoxyribonuclease X
CLASS       Hydrolases;
            Acting on ester bonds;
            Endodeoxyribonucleases producing 3'-phosphomonoesters
REACTION    Endonucleolytic cleavage of supercoiled plasma DNA to linear DNA
            duplexes
INHIBITOR   ATP [CPD:C00002];
            AMP [CPD:C00020];
            Single-stranded DNA [CPD:C00271]
COMMENT     Preference for supercoiled DNA; little activity on linear
            double-stranded DNA. Inhibited by single-stranded DNA, ATP and AMP.
REFERENCE   1
  AUTHORS   Ghosh, S. and DasGupta, U.
  TITLE     Studies with endonuclease X: a new deoxyendonuclease of E. coli that
            preferentially cleaves supercoiled plasmid DNA.
  JOURNAL   Curr. Trends Life Sci. 12 (1984) 79-88.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.22.5
            ExPASy - ENZYME nomenclature database: 3.1.22.5
            ExplorEnz - The Enzyme Database: 3.1.22.5
            ERGO genome analysis and discovery system: 3.1.22.5
            BRENDA, the Enzyme Database: 3.1.22.5
            CAS: 97002-82-9
///
ENTRY       EC 3.1.23.1       Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease AluI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.1 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.1
            ExPASy - ENZYME nomenclature database: 3.1.23.1
            ExplorEnz - The Enzyme Database: 3.1.23.1
            ERGO genome analysis and discovery system: 3.1.23.1
            BRENDA, the Enzyme Database: 3.1.23.1
///
ENTRY       EC 3.1.23.2       Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease AsuI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.2 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.2
            ExPASy - ENZYME nomenclature database: 3.1.23.2
            ExplorEnz - The Enzyme Database: 3.1.23.2
            ERGO genome analysis and discovery system: 3.1.23.2
            BRENDA, the Enzyme Database: 3.1.23.2
///
ENTRY       EC 3.1.23.3       Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease AvaI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.3 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.3
            ExPASy - ENZYME nomenclature database: 3.1.23.3
            ExplorEnz - The Enzyme Database: 3.1.23.3
            ERGO genome analysis and discovery system: 3.1.23.3
            BRENDA, the Enzyme Database: 3.1.23.3
///
ENTRY       EC 3.1.23.4       Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease AvaII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.4 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.4
            ExPASy - ENZYME nomenclature database: 3.1.23.4
            ExplorEnz - The Enzyme Database: 3.1.23.4
            ERGO genome analysis and discovery system: 3.1.23.4
            BRENDA, the Enzyme Database: 3.1.23.4
///
ENTRY       EC 3.1.23.5       Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease BalI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.5 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.5
            ExPASy - ENZYME nomenclature database: 3.1.23.5
            ExplorEnz - The Enzyme Database: 3.1.23.5
            ERGO genome analysis and discovery system: 3.1.23.5
            BRENDA, the Enzyme Database: 3.1.23.5
///
ENTRY       EC 3.1.23.6       Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease BamHI. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.6 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.6
            ExPASy - ENZYME nomenclature database: 3.1.23.6
            ExplorEnz - The Enzyme Database: 3.1.23.6
            ERGO genome analysis and discovery system: 3.1.23.6
            BRENDA, the Enzyme Database: 3.1.23.6
///
ENTRY       EC 3.1.23.7       Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease BbvI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.7 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.7
            ExPASy - ENZYME nomenclature database: 3.1.23.7
            ExplorEnz - The Enzyme Database: 3.1.23.7
            ERGO genome analysis and discovery system: 3.1.23.7
            BRENDA, the Enzyme Database: 3.1.23.7
///
ENTRY       EC 3.1.23.8       Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease BclI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.8 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.8
            ExPASy - ENZYME nomenclature database: 3.1.23.8
            ExplorEnz - The Enzyme Database: 3.1.23.8
            ERGO genome analysis and discovery system: 3.1.23.8
            BRENDA, the Enzyme Database: 3.1.23.8
///
ENTRY       EC 3.1.23.9       Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease BglI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.9 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.9
            ExPASy - ENZYME nomenclature database: 3.1.23.9
            ExplorEnz - The Enzyme Database: 3.1.23.9
            ERGO genome analysis and discovery system: 3.1.23.9
            BRENDA, the Enzyme Database: 3.1.23.9
///
ENTRY       EC 3.1.23.10      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease BglII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.10 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.10
            ExPASy - ENZYME nomenclature database: 3.1.23.10
            ExplorEnz - The Enzyme Database: 3.1.23.10
            ERGO genome analysis and discovery system: 3.1.23.10
            BRENDA, the Enzyme Database: 3.1.23.10
///
ENTRY       EC 3.1.23.11      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease BpuI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.11 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.11
            ExPASy - ENZYME nomenclature database: 3.1.23.11
            ExplorEnz - The Enzyme Database: 3.1.23.11
            ERGO genome analysis and discovery system: 3.1.23.11
            BRENDA, the Enzyme Database: 3.1.23.11
///
ENTRY       EC 3.1.23.12      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease DpnI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.12 created 1978,
            modified 1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.12
            ExPASy - ENZYME nomenclature database: 3.1.23.12
            ExplorEnz - The Enzyme Database: 3.1.23.12
            ERGO genome analysis and discovery system: 3.1.23.12
            BRENDA, the Enzyme Database: 3.1.23.12
///
ENTRY       EC 3.1.23.13      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease EcoRI. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.13 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.13
            ExPASy - ENZYME nomenclature database: 3.1.23.13
            ExplorEnz - The Enzyme Database: 3.1.23.13
            ERGO genome analysis and discovery system: 3.1.23.13
            BRENDA, the Enzyme Database: 3.1.23.13
///
ENTRY       EC 3.1.23.14      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease EcoRII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.14 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.14
            ExPASy - ENZYME nomenclature database: 3.1.23.14
            ExplorEnz - The Enzyme Database: 3.1.23.14
            ERGO genome analysis and discovery system: 3.1.23.14
            BRENDA, the Enzyme Database: 3.1.23.14
///
ENTRY       EC 3.1.23.15      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HaeI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.15 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.15
            ExPASy - ENZYME nomenclature database: 3.1.23.15
            ExplorEnz - The Enzyme Database: 3.1.23.15
            ERGO genome analysis and discovery system: 3.1.23.15
            BRENDA, the Enzyme Database: 3.1.23.15
///
ENTRY       EC 3.1.23.16      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HaeII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.16 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.16
            ExPASy - ENZYME nomenclature database: 3.1.23.16
            ExplorEnz - The Enzyme Database: 3.1.23.16
            ERGO genome analysis and discovery system: 3.1.23.16
            BRENDA, the Enzyme Database: 3.1.23.16
///
ENTRY       EC 3.1.23.17      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HaeIII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.17 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.17
            ExPASy - ENZYME nomenclature database: 3.1.23.17
            ExplorEnz - The Enzyme Database: 3.1.23.17
            ERGO genome analysis and discovery system: 3.1.23.17
            BRENDA, the Enzyme Database: 3.1.23.17
///
ENTRY       EC 3.1.23.18      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HgaI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.18 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.18
            ExPASy - ENZYME nomenclature database: 3.1.23.18
            ExplorEnz - The Enzyme Database: 3.1.23.18
            ERGO genome analysis and discovery system: 3.1.23.18
            BRENDA, the Enzyme Database: 3.1.23.18
///
ENTRY       EC 3.1.23.19      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HhaI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.19 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.19
            ExPASy - ENZYME nomenclature database: 3.1.23.19
            ExplorEnz - The Enzyme Database: 3.1.23.19
            ERGO genome analysis and discovery system: 3.1.23.19
            BRENDA, the Enzyme Database: 3.1.23.19
///
ENTRY       EC 3.1.23.20      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HindII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.20 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.20
            ExPASy - ENZYME nomenclature database: 3.1.23.20
            ExplorEnz - The Enzyme Database: 3.1.23.20
            ERGO genome analysis and discovery system: 3.1.23.20
            BRENDA, the Enzyme Database: 3.1.23.20
///
ENTRY       EC 3.1.23.21      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HindIII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.21 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.21
            ExPASy - ENZYME nomenclature database: 3.1.23.21
            ExplorEnz - The Enzyme Database: 3.1.23.21
            ERGO genome analysis and discovery system: 3.1.23.21
            BRENDA, the Enzyme Database: 3.1.23.21
///
ENTRY       EC 3.1.23.22      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HinfI. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.22 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.22
            ExPASy - ENZYME nomenclature database: 3.1.23.22
            ExplorEnz - The Enzyme Database: 3.1.23.22
            ERGO genome analysis and discovery system: 3.1.23.22
            BRENDA, the Enzyme Database: 3.1.23.22
///
ENTRY       EC 3.1.23.23      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HpaI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.23 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.23
            ExPASy - ENZYME nomenclature database: 3.1.23.23
            ExplorEnz - The Enzyme Database: 3.1.23.23
            ERGO genome analysis and discovery system: 3.1.23.23
            BRENDA, the Enzyme Database: 3.1.23.23
///
ENTRY       EC 3.1.23.24      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HpaII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.24 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.24
            ExPASy - ENZYME nomenclature database: 3.1.23.24
            ExplorEnz - The Enzyme Database: 3.1.23.24
            ERGO genome analysis and discovery system: 3.1.23.24
            BRENDA, the Enzyme Database: 3.1.23.24
///
ENTRY       EC 3.1.23.25      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HphI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.25 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.25
            ExPASy - ENZYME nomenclature database: 3.1.23.25
            ExplorEnz - The Enzyme Database: 3.1.23.25
            ERGO genome analysis and discovery system: 3.1.23.25
            BRENDA, the Enzyme Database: 3.1.23.25
///
ENTRY       EC 3.1.23.26      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease KpnI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.26 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.26
            ExPASy - ENZYME nomenclature database: 3.1.23.26
            ExplorEnz - The Enzyme Database: 3.1.23.26
            ERGO genome analysis and discovery system: 3.1.23.26
            BRENDA, the Enzyme Database: 3.1.23.26
///
ENTRY       EC 3.1.23.27      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease MboI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.27 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.27
            ExPASy - ENZYME nomenclature database: 3.1.23.27
            ExplorEnz - The Enzyme Database: 3.1.23.27
            ERGO genome analysis and discovery system: 3.1.23.27
            BRENDA, the Enzyme Database: 3.1.23.27
///
ENTRY       EC 3.1.23.28      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease MboII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.28 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.28
            ExPASy - ENZYME nomenclature database: 3.1.23.28
            ExplorEnz - The Enzyme Database: 3.1.23.28
            ERGO genome analysis and discovery system: 3.1.23.28
            BRENDA, the Enzyme Database: 3.1.23.28
///
ENTRY       EC 3.1.23.29      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease MnlI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.29 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.29
            ExPASy - ENZYME nomenclature database: 3.1.23.29
            ExplorEnz - The Enzyme Database: 3.1.23.29
            ERGO genome analysis and discovery system: 3.1.23.29
            BRENDA, the Enzyme Database: 3.1.23.29
///
ENTRY       EC 3.1.23.30      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease PfaI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.30 created 1978,
            modified 1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.30
            ExPASy - ENZYME nomenclature database: 3.1.23.30
            ExplorEnz - The Enzyme Database: 3.1.23.30
            ERGO genome analysis and discovery system: 3.1.23.30
            BRENDA, the Enzyme Database: 3.1.23.30
///
ENTRY       EC 3.1.23.31      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease PstI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.31 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.31
            ExPASy - ENZYME nomenclature database: 3.1.23.31
            ExplorEnz - The Enzyme Database: 3.1.23.31
            ERGO genome analysis and discovery system: 3.1.23.31
            BRENDA, the Enzyme Database: 3.1.23.31
///
ENTRY       EC 3.1.23.32      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease PvuI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.32 created 1978,
            modified 1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.32
            ExPASy - ENZYME nomenclature database: 3.1.23.32
            ExplorEnz - The Enzyme Database: 3.1.23.32
            ERGO genome analysis and discovery system: 3.1.23.32
            BRENDA, the Enzyme Database: 3.1.23.32
///
ENTRY       EC 3.1.23.33      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease PvuII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.33 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.33
            ExPASy - ENZYME nomenclature database: 3.1.23.33
            ExplorEnz - The Enzyme Database: 3.1.23.33
            ERGO genome analysis and discovery system: 3.1.23.33
            BRENDA, the Enzyme Database: 3.1.23.33
///
ENTRY       EC 3.1.23.34      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease SacI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.34 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.34
            ExPASy - ENZYME nomenclature database: 3.1.23.34
            ExplorEnz - The Enzyme Database: 3.1.23.34
            ERGO genome analysis and discovery system: 3.1.23.34
            BRENDA, the Enzyme Database: 3.1.23.34
///
ENTRY       EC 3.1.23.35      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease SacII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.35 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.35
            ExPASy - ENZYME nomenclature database: 3.1.23.35
            ExplorEnz - The Enzyme Database: 3.1.23.35
            ERGO genome analysis and discovery system: 3.1.23.35
            BRENDA, the Enzyme Database: 3.1.23.35
///
ENTRY       EC 3.1.23.36      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease SacIII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.36 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.36
            ExPASy - ENZYME nomenclature database: 3.1.23.36
            ExplorEnz - The Enzyme Database: 3.1.23.36
            ERGO genome analysis and discovery system: 3.1.23.36
            BRENDA, the Enzyme Database: 3.1.23.36
///
ENTRY       EC 3.1.23.37      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease SalI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.37 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.37
            ExPASy - ENZYME nomenclature database: 3.1.23.37
            ExplorEnz - The Enzyme Database: 3.1.23.37
            ERGO genome analysis and discovery system: 3.1.23.37
            BRENDA, the Enzyme Database: 3.1.23.37
///
ENTRY       EC 3.1.23.38      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease SgrI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.38 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.38
            ExPASy - ENZYME nomenclature database: 3.1.23.38
            ExplorEnz - The Enzyme Database: 3.1.23.38
            ERGO genome analysis and discovery system: 3.1.23.38
            BRENDA, the Enzyme Database: 3.1.23.38
///
ENTRY       EC 3.1.23.39      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease TaqI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.39 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.39
            ExPASy - ENZYME nomenclature database: 3.1.23.39
            ExplorEnz - The Enzyme Database: 3.1.23.39
            ERGO genome analysis and discovery system: 3.1.23.39
            BRENDA, the Enzyme Database: 3.1.23.39
///
ENTRY       EC 3.1.23.40      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease TaqII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.40 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.40
            ExPASy - ENZYME nomenclature database: 3.1.23.40
            ExplorEnz - The Enzyme Database: 3.1.23.40
            ERGO genome analysis and discovery system: 3.1.23.40
            BRENDA, the Enzyme Database: 3.1.23.40
///
ENTRY       EC 3.1.23.41      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease XbaI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.41 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.41
            ExPASy - ENZYME nomenclature database: 3.1.23.41
            ExplorEnz - The Enzyme Database: 3.1.23.41
            ERGO genome analysis and discovery system: 3.1.23.41
            BRENDA, the Enzyme Database: 3.1.23.41
///
ENTRY       EC 3.1.23.42      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease XhoI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.42 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.42
            ExPASy - ENZYME nomenclature database: 3.1.23.42
            ExplorEnz - The Enzyme Database: 3.1.23.42
            ERGO genome analysis and discovery system: 3.1.23.42
            BRENDA, the Enzyme Database: 3.1.23.42
///
ENTRY       EC 3.1.23.43      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease XhoII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.43 created 1978,
            modified 1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.43
            ExPASy - ENZYME nomenclature database: 3.1.23.43
            ExplorEnz - The Enzyme Database: 3.1.23.43
            ERGO genome analysis and discovery system: 3.1.23.43
            BRENDA, the Enzyme Database: 3.1.23.43
///
ENTRY       EC 3.1.23.44      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease XmaI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.44 created 1978,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.44
            ExPASy - ENZYME nomenclature database: 3.1.23.44
            ExplorEnz - The Enzyme Database: 3.1.23.44
            ERGO genome analysis and discovery system: 3.1.23.44
            BRENDA, the Enzyme Database: 3.1.23.44
///
ENTRY       EC 3.1.23.45      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease XniI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.45 created 1978,
            modified 1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.45
            ExPASy - ENZYME nomenclature database: 3.1.23.45
            ExplorEnz - The Enzyme Database: 3.1.23.45
            ERGO genome analysis and discovery system: 3.1.23.45
            BRENDA, the Enzyme Database: 3.1.23.45
///
ENTRY       EC 3.1.23.46      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease AimI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.46 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.46
            ExPASy - ENZYME nomenclature database: 3.1.23.46
            ExplorEnz - The Enzyme Database: 3.1.23.46
            ERGO genome analysis and discovery system: 3.1.23.46
            BRENDA, the Enzyme Database: 3.1.23.46
///
ENTRY       EC 3.1.23.47      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease AccI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.47 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.47
            ExPASy - ENZYME nomenclature database: 3.1.23.47
            ExplorEnz - The Enzyme Database: 3.1.23.47
            ERGO genome analysis and discovery system: 3.1.23.47
            BRENDA, the Enzyme Database: 3.1.23.47
///
ENTRY       EC 3.1.23.48      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease AccII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.48 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.48
            ExPASy - ENZYME nomenclature database: 3.1.23.48
            ExplorEnz - The Enzyme Database: 3.1.23.48
            ERGO genome analysis and discovery system: 3.1.23.48
            BRENDA, the Enzyme Database: 3.1.23.48
///
ENTRY       EC 3.1.23.49      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease AtuAI. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.49 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.49
            ExPASy - ENZYME nomenclature database: 3.1.23.49
            ExplorEnz - The Enzyme Database: 3.1.23.49
            ERGO genome analysis and discovery system: 3.1.23.49
            BRENDA, the Enzyme Database: 3.1.23.49
///
ENTRY       EC 3.1.23.50      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease AtuBVI. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.50 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.50
            ExPASy - ENZYME nomenclature database: 3.1.23.50
            ExplorEnz - The Enzyme Database: 3.1.23.50
            ERGO genome analysis and discovery system: 3.1.23.50
            BRENDA, the Enzyme Database: 3.1.23.50
///
ENTRY       EC 3.1.23.51      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease AcaI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.51 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.51
            ExPASy - ENZYME nomenclature database: 3.1.23.51
            ExplorEnz - The Enzyme Database: 3.1.23.51
            ERGO genome analysis and discovery system: 3.1.23.51
            BRENDA, the Enzyme Database: 3.1.23.51
///
ENTRY       EC 3.1.23.52      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease AcyI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.52 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.52
            ExPASy - ENZYME nomenclature database: 3.1.23.52
            ExplorEnz - The Enzyme Database: 3.1.23.52
            ERGO genome analysis and discovery system: 3.1.23.52
            BRENDA, the Enzyme Database: 3.1.23.52
///
ENTRY       EC 3.1.23.53      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease AosI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.53 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.53
            ExPASy - ENZYME nomenclature database: 3.1.23.53
            ExplorEnz - The Enzyme Database: 3.1.23.53
            ERGO genome analysis and discovery system: 3.1.23.53
            BRENDA, the Enzyme Database: 3.1.23.53
///
ENTRY       EC 3.1.23.54      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease AsuII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.54 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.54
            ExPASy - ENZYME nomenclature database: 3.1.23.54
            ExplorEnz - The Enzyme Database: 3.1.23.54
            ERGO genome analysis and discovery system: 3.1.23.54
            BRENDA, the Enzyme Database: 3.1.23.54
///
ENTRY       EC 3.1.23.55      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease AvaIII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.55 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.55
            ExPASy - ENZYME nomenclature database: 3.1.23.55
            ExplorEnz - The Enzyme Database: 3.1.23.55
            ERGO genome analysis and discovery system: 3.1.23.55
            BRENDA, the Enzyme Database: 3.1.23.55
///
ENTRY       EC 3.1.23.56      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease AvrII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.56 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.56
            ExPASy - ENZYME nomenclature database: 3.1.23.56
            ExplorEnz - The Enzyme Database: 3.1.23.56
            ERGO genome analysis and discovery system: 3.1.23.56
            BRENDA, the Enzyme Database: 3.1.23.56
///
ENTRY       EC 3.1.23.57      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease BceI4579. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease. Assumed to be the same as
            endodeoxyribonuclease Bce4579I (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.23.57 created
            1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.57
            ExPASy - ENZYME nomenclature database: 3.1.23.57
            ExplorEnz - The Enzyme Database: 3.1.23.57
            ERGO genome analysis and discovery system: 3.1.23.57
            BRENDA, the Enzyme Database: 3.1.23.57
///
ENTRY       EC 3.1.23.58      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease Bce1229. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease. Assumed to be the same as
            endodeoxyribonuclease Bce1229I (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.23.58 created
            1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.58
            ExPASy - ENZYME nomenclature database: 3.1.23.58
            ExplorEnz - The Enzyme Database: 3.1.23.58
            ERGO genome analysis and discovery system: 3.1.23.58
            BRENDA, the Enzyme Database: 3.1.23.58
///
ENTRY       EC 3.1.23.59      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease Bme899. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease. Assumed to be the same as
            endodeoxyribonuclease Bme899I (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.23.59 created
            1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.59
            ExPASy - ENZYME nomenclature database: 3.1.23.59
            ExplorEnz - The Enzyme Database: 3.1.23.59
            ERGO genome analysis and discovery system: 3.1.23.59
            BRENDA, the Enzyme Database: 3.1.23.59
///
ENTRY       EC 3.1.23.60      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease Bme205. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease. Assumed to be the same as
            endodeoxyribonuclease Bme205I (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.23.60 created
            1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.60
            ExPASy - ENZYME nomenclature database: 3.1.23.60
            ExplorEnz - The Enzyme Database: 3.1.23.60
            ERGO genome analysis and discovery system: 3.1.23.60
            BRENDA, the Enzyme Database: 3.1.23.60
///
ENTRY       EC 3.1.23.61      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease BmeI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.61 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.61
            ExPASy - ENZYME nomenclature database: 3.1.23.61
            ExplorEnz - The Enzyme Database: 3.1.23.61
            ERGO genome analysis and discovery system: 3.1.23.61
            BRENDA, the Enzyme Database: 3.1.23.61
///
ENTRY       EC 3.1.23.62      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease Bsp1286. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease. Assumed to be the same as
            endodeoxyribonuclease Bsp1286I (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.23.62 created
            1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.62
            ExPASy - ENZYME nomenclature database: 3.1.23.62
            ExplorEnz - The Enzyme Database: 3.1.23.62
            ERGO genome analysis and discovery system: 3.1.23.62
            BRENDA, the Enzyme Database: 3.1.23.62
///
ENTRY       EC 3.1.23.63      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease BstAI. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.63 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.63
            ExPASy - ENZYME nomenclature database: 3.1.23.63
            ExplorEnz - The Enzyme Database: 3.1.23.63
            ERGO genome analysis and discovery system: 3.1.23.63
            BRENDA, the Enzyme Database: 3.1.23.63
///
ENTRY       EC 3.1.23.64      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease BstEI. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.64 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.64
            ExPASy - ENZYME nomenclature database: 3.1.23.64
            ExplorEnz - The Enzyme Database: 3.1.23.64
            ERGO genome analysis and discovery system: 3.1.23.64
            BRENDA, the Enzyme Database: 3.1.23.64
///
ENTRY       EC 3.1.23.65      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease BstEIII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.65 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.65
            ExPASy - ENZYME nomenclature database: 3.1.23.65
            ExplorEnz - The Enzyme Database: 3.1.23.65
            ERGO genome analysis and discovery system: 3.1.23.65
            BRENDA, the Enzyme Database: 3.1.23.65
///
ENTRY       EC 3.1.23.66      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease BstPI. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.66 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.66
            ExPASy - ENZYME nomenclature database: 3.1.23.66
            ExplorEnz - The Enzyme Database: 3.1.23.66
            ERGO genome analysis and discovery system: 3.1.23.66
            BRENDA, the Enzyme Database: 3.1.23.66
///
ENTRY       EC 3.1.23.67      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease BsuM. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease. Assumed to be the same as
            endodeoxyribonuclease BsuMI (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.23.67 created
            1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.67
            ExPASy - ENZYME nomenclature database: 3.1.23.67
            ExplorEnz - The Enzyme Database: 3.1.23.67
            ERGO genome analysis and discovery system: 3.1.23.67
            BRENDA, the Enzyme Database: 3.1.23.67
///
ENTRY       EC 3.1.23.68      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease Bsu6633. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease. The name was misprinted in
            supplement 3 of the 1978 edition. Assumed to be the same as
            endodeoxyribonuclease Bsu6633I (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.23.68 created
            1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.68
            ExPASy - ENZYME nomenclature database: 3.1.23.68
            ExplorEnz - The Enzyme Database: 3.1.23.68
            ERGO genome analysis and discovery system: 3.1.23.68
            BRENDA, the Enzyme Database: 3.1.23.68
///
ENTRY       EC 3.1.23.69      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease Bsu1145. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease. Assumed to be the same as
            endodeoxyribonuclease Bsu1145I (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.23.69 created
            1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.69
            ExPASy - ENZYME nomenclature database: 3.1.23.69
            ExplorEnz - The Enzyme Database: 3.1.23.69
            ERGO genome analysis and discovery system: 3.1.23.69
            BRENDA, the Enzyme Database: 3.1.23.69
///
ENTRY       EC 3.1.23.70      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease Bsu1192. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease. Assumed to be the same as
            endodeoxyribonuclease Bsu1192I or see Bsu1192II (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.23.70 created
            1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.70
            ExPASy - ENZYME nomenclature database: 3.1.23.70
            ExplorEnz - The Enzyme Database: 3.1.23.70
            ERGO genome analysis and discovery system: 3.1.23.70
            BRENDA, the Enzyme Database: 3.1.23.70
///
ENTRY       EC 3.1.23.71      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease Bsu1193. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease. Assumed to be the same as
            endodeoxyribonuclease Bsu1193I (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.23.71 created
            1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.71
            ExPASy - ENZYME nomenclature database: 3.1.23.71
            ExplorEnz - The Enzyme Database: 3.1.23.71
            ERGO genome analysis and discovery system: 3.1.23.71
            BRENDA, the Enzyme Database: 3.1.23.71
///
ENTRY       EC 3.1.23.72      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease Bsu1231. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease. Not found in
            http://rebase.neb.com/rebase/rebase.html (EC 3.1.23.72 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.72
            ExPASy - ENZYME nomenclature database: 3.1.23.72
            ExplorEnz - The Enzyme Database: 3.1.23.72
            ERGO genome analysis and discovery system: 3.1.23.72
            BRENDA, the Enzyme Database: 3.1.23.72
///
ENTRY       EC 3.1.23.73      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease Bsu1259. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease. Assumed to be the same as
            endodeoxyribonuclease Bsu1259I (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.23.73 created
            1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.73
            ExPASy - ENZYME nomenclature database: 3.1.23.73
            ExplorEnz - The Enzyme Database: 3.1.23.73
            ERGO genome analysis and discovery system: 3.1.23.73
            BRENDA, the Enzyme Database: 3.1.23.73
///
ENTRY       EC 3.1.23.74      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease ClaI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.74 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.74
            ExPASy - ENZYME nomenclature database: 3.1.23.74
            ExplorEnz - The Enzyme Database: 3.1.23.74
            ERGO genome analysis and discovery system: 3.1.23.74
            BRENDA, the Enzyme Database: 3.1.23.74
///
ENTRY       EC 3.1.23.75      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease CauII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.75 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.75
            ExPASy - ENZYME nomenclature database: 3.1.23.75
            ExplorEnz - The Enzyme Database: 3.1.23.75
            ERGO genome analysis and discovery system: 3.1.23.75
            BRENDA, the Enzyme Database: 3.1.23.75
///
ENTRY       EC 3.1.23.76      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease CviI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.76 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.76
            ExPASy - ENZYME nomenclature database: 3.1.23.76
            ExplorEnz - The Enzyme Database: 3.1.23.76
            ERGO genome analysis and discovery system: 3.1.23.76
            BRENDA, the Enzyme Database: 3.1.23.76
///
ENTRY       EC 3.1.23.77      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease DdeI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.77 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.77
            ExPASy - ENZYME nomenclature database: 3.1.23.77
            ExplorEnz - The Enzyme Database: 3.1.23.77
            ERGO genome analysis and discovery system: 3.1.23.77
            BRENDA, the Enzyme Database: 3.1.23.77
///
ENTRY       EC 3.1.23.78      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease EclI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.78 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.78
            ExPASy - ENZYME nomenclature database: 3.1.23.78
            ExplorEnz - The Enzyme Database: 3.1.23.78
            ERGO genome analysis and discovery system: 3.1.23.78
            BRENDA, the Enzyme Database: 3.1.23.78
///
ENTRY       EC 3.1.23.79      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease EcaI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.79 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.79
            ExPASy - ENZYME nomenclature database: 3.1.23.79
            ExplorEnz - The Enzyme Database: 3.1.23.79
            ERGO genome analysis and discovery system: 3.1.23.79
            BRENDA, the Enzyme Database: 3.1.23.79
///
ENTRY       EC 3.1.23.80      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease EcoRI'. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease. Assumed to be the same as
            endodeoxyribonuclease EcoRI' (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.23.80 created
            1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.80
            ExPASy - ENZYME nomenclature database: 3.1.23.80
            ExplorEnz - The Enzyme Database: 3.1.23.80
            ERGO genome analysis and discovery system: 3.1.23.80
            BRENDA, the Enzyme Database: 3.1.23.80
///
ENTRY       EC 3.1.23.81      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease Fnu48I. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.81 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.81
            ExPASy - ENZYME nomenclature database: 3.1.23.81
            ExplorEnz - The Enzyme Database: 3.1.23.81
            ERGO genome analysis and discovery system: 3.1.23.81
            BRENDA, the Enzyme Database: 3.1.23.81
///
ENTRY       EC 3.1.23.82      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease Fnu4H. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease. Assumed to be the same as
            endodeoxyribonuclease Fnu4HI (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.23.82 created
            1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.82
            ExPASy - ENZYME nomenclature database: 3.1.23.82
            ExplorEnz - The Enzyme Database: 3.1.23.82
            ERGO genome analysis and discovery system: 3.1.23.82
            BRENDA, the Enzyme Database: 3.1.23.82
///
ENTRY       EC 3.1.23.83      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HapI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.83 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.83
            ExPASy - ENZYME nomenclature database: 3.1.23.83
            ExplorEnz - The Enzyme Database: 3.1.23.83
            ERGO genome analysis and discovery system: 3.1.23.83
            BRENDA, the Enzyme Database: 3.1.23.83
///
ENTRY       EC 3.1.23.84      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease Hin1056II. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.84 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.84
            ExPASy - ENZYME nomenclature database: 3.1.23.84
            ExplorEnz - The Enzyme Database: 3.1.23.84
            ERGO genome analysis and discovery system: 3.1.23.84
            BRENDA, the Enzyme Database: 3.1.23.84
///
ENTRY       EC 3.1.23.85      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HinfIII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.85 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.85
            ExPASy - ENZYME nomenclature database: 3.1.23.85
            ExplorEnz - The Enzyme Database: 3.1.23.85
            ERGO genome analysis and discovery system: 3.1.23.85
            BRENDA, the Enzyme Database: 3.1.23.85
///
ENTRY       EC 3.1.23.86      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HgiAI. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.86 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.86
            ExPASy - ENZYME nomenclature database: 3.1.23.86
            ExplorEnz - The Enzyme Database: 3.1.23.86
            ERGO genome analysis and discovery system: 3.1.23.86
            BRENDA, the Enzyme Database: 3.1.23.86
///
ENTRY       EC 3.1.23.87      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HgiCI. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.87 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.87
            ExPASy - ENZYME nomenclature database: 3.1.23.87
            ExplorEnz - The Enzyme Database: 3.1.23.87
            ERGO genome analysis and discovery system: 3.1.23.87
            BRENDA, the Enzyme Database: 3.1.23.87
///
ENTRY       EC 3.1.23.88      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HgiDI. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.88 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.88
            ExPASy - ENZYME nomenclature database: 3.1.23.88
            ExplorEnz - The Enzyme Database: 3.1.23.88
            ERGO genome analysis and discovery system: 3.1.23.88
            BRENDA, the Enzyme Database: 3.1.23.88
///
ENTRY       EC 3.1.23.89      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease HgiEII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.89 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.89
            ExPASy - ENZYME nomenclature database: 3.1.23.89
            ExplorEnz - The Enzyme Database: 3.1.23.89
            ERGO genome analysis and discovery system: 3.1.23.89
            BRENDA, the Enzyme Database: 3.1.23.89
///
ENTRY       EC 3.1.23.90      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease MstI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.90 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.90
            ExPASy - ENZYME nomenclature database: 3.1.23.90
            ExplorEnz - The Enzyme Database: 3.1.23.90
            ERGO genome analysis and discovery system: 3.1.23.90
            BRENDA, the Enzyme Database: 3.1.23.90
///
ENTRY       EC 3.1.23.91      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease MstII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.91 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.91
            ExPASy - ENZYME nomenclature database: 3.1.23.91
            ExplorEnz - The Enzyme Database: 3.1.23.91
            ERGO genome analysis and discovery system: 3.1.23.91
            BRENDA, the Enzyme Database: 3.1.23.91
///
ENTRY       EC 3.1.23.92      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease MglI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.92 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.92
            ExPASy - ENZYME nomenclature database: 3.1.23.92
            ExplorEnz - The Enzyme Database: 3.1.23.92
            ERGO genome analysis and discovery system: 3.1.23.92
            BRENDA, the Enzyme Database: 3.1.23.92
///
ENTRY       EC 3.1.23.93      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease MglII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.93 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.93
            ExPASy - ENZYME nomenclature database: 3.1.23.93
            ExplorEnz - The Enzyme Database: 3.1.23.93
            ERGO genome analysis and discovery system: 3.1.23.93
            BRENDA, the Enzyme Database: 3.1.23.93
///
ENTRY       EC 3.1.23.94      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease MnoII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.94 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.94
            ExPASy - ENZYME nomenclature database: 3.1.23.94
            ExplorEnz - The Enzyme Database: 3.1.23.94
            ERGO genome analysis and discovery system: 3.1.23.94
            BRENDA, the Enzyme Database: 3.1.23.94
///
ENTRY       EC 3.1.23.95      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease MnnIII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.95 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.95
            ExPASy - ENZYME nomenclature database: 3.1.23.95
            ExplorEnz - The Enzyme Database: 3.1.23.95
            ERGO genome analysis and discovery system: 3.1.23.95
            BRENDA, the Enzyme Database: 3.1.23.95
///
ENTRY       EC 3.1.23.96      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease MviI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.96 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.96
            ExPASy - ENZYME nomenclature database: 3.1.23.96
            ExplorEnz - The Enzyme Database: 3.1.23.96
            ERGO genome analysis and discovery system: 3.1.23.96
            BRENDA, the Enzyme Database: 3.1.23.96
///
ENTRY       EC 3.1.23.97      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease MviII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.97 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.97
            ExPASy - ENZYME nomenclature database: 3.1.23.97
            ExplorEnz - The Enzyme Database: 3.1.23.97
            ERGO genome analysis and discovery system: 3.1.23.97
            BRENDA, the Enzyme Database: 3.1.23.97
///
ENTRY       EC 3.1.23.98      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease OxaII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.98 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.98
            ExPASy - ENZYME nomenclature database: 3.1.23.98
            ExplorEnz - The Enzyme Database: 3.1.23.98
            ERGO genome analysis and discovery system: 3.1.23.98
            BRENDA, the Enzyme Database: 3.1.23.98
///
ENTRY       EC 3.1.23.99      Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease PaeR7. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease. Assumed to be the same as
            endodeoxyribonuclease PaeR7I (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.23.99 created
            1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.99
            ExPASy - ENZYME nomenclature database: 3.1.23.99
            ExplorEnz - The Enzyme Database: 3.1.23.99
            ERGO genome analysis and discovery system: 3.1.23.99
            BRENDA, the Enzyme Database: 3.1.23.99
///
ENTRY       EC 3.1.23.100     Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease RspI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.100 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.100
            ExPASy - ENZYME nomenclature database: 3.1.23.100
            ExplorEnz - The Enzyme Database: 3.1.23.100
            ERGO genome analysis and discovery system: 3.1.23.100
            BRENDA, the Enzyme Database: 3.1.23.100
///
ENTRY       EC 3.1.23.101     Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease RsaI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.101 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.101
            ExPASy - ENZYME nomenclature database: 3.1.23.101
            ExplorEnz - The Enzyme Database: 3.1.23.101
            ERGO genome analysis and discovery system: 3.1.23.101
            BRENDA, the Enzyme Database: 3.1.23.101
///
ENTRY       EC 3.1.23.102     Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease SmaI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.102 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.102
            ExPASy - ENZYME nomenclature database: 3.1.23.102
            ExplorEnz - The Enzyme Database: 3.1.23.102
            ERGO genome analysis and discovery system: 3.1.23.102
            BRENDA, the Enzyme Database: 3.1.23.102
///
ENTRY       EC 3.1.23.103     Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease SspI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.103 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.103
            ExPASy - ENZYME nomenclature database: 3.1.23.103
            ExplorEnz - The Enzyme Database: 3.1.23.103
            ERGO genome analysis and discovery system: 3.1.23.103
            BRENDA, the Enzyme Database: 3.1.23.103
///
ENTRY       EC 3.1.23.104     Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease SnaI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.104 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.104
            ExPASy - ENZYME nomenclature database: 3.1.23.104
            ExplorEnz - The Enzyme Database: 3.1.23.104
            ERGO genome analysis and discovery system: 3.1.23.104
            BRENDA, the Enzyme Database: 3.1.23.104
///
ENTRY       EC 3.1.23.105     Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease SfaNI. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.105 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.105
            ExPASy - ENZYME nomenclature database: 3.1.23.105
            ExplorEnz - The Enzyme Database: 3.1.23.105
            ERGO genome analysis and discovery system: 3.1.23.105
            BRENDA, the Enzyme Database: 3.1.23.105
///
ENTRY       EC 3.1.23.106     Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease SalII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.106 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.106
            ExPASy - ENZYME nomenclature database: 3.1.23.106
            ExplorEnz - The Enzyme Database: 3.1.23.106
            ERGO genome analysis and discovery system: 3.1.23.106
            BRENDA, the Enzyme Database: 3.1.23.106
///
ENTRY       EC 3.1.23.107     Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease SauI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.107 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.107
            ExPASy - ENZYME nomenclature database: 3.1.23.107
            ExplorEnz - The Enzyme Database: 3.1.23.107
            ERGO genome analysis and discovery system: 3.1.23.107
            BRENDA, the Enzyme Database: 3.1.23.107
///
ENTRY       EC 3.1.23.108     Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease SphI. Now EC 3.1.21.4, type
            II site-specific deoxyribonuclease (EC 3.1.23.108 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.108
            ExPASy - ENZYME nomenclature database: 3.1.23.108
            ExplorEnz - The Enzyme Database: 3.1.23.108
            ERGO genome analysis and discovery system: 3.1.23.108
            BRENDA, the Enzyme Database: 3.1.23.108
///
ENTRY       EC 3.1.23.109     Obsolete  Enzyme
NAME        Transferred to 3.1.21.4
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases: cleavage is sequence specific
            (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease XmaIII. Now EC 3.1.21.4,
            type II site-specific deoxyribonuclease (EC 3.1.23.109 created 1982,
            deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.23.109
            ExPASy - ENZYME nomenclature database: 3.1.23.109
            ExplorEnz - The Enzyme Database: 3.1.23.109
            ERGO genome analysis and discovery system: 3.1.23.109
            BRENDA, the Enzyme Database: 3.1.23.109
///
ENTRY       EC 3.1.24.1       Obsolete  Enzyme
NAME        Transferred to 3.1.21.3
CLASS       Hydrolases;
            Acting on ester bonds;
            Site specific endodeoxyribonucleases: cleavage is not sequence
            specific (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease EcoB. Now EC 3.1.21.3, type
            I site-specific deoxyribonuclease. Assumed to be the same as
            endodeoxyribonuclease EcoBI (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.24.1 created 1978,
            modified 1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.24.1
            ExPASy - ENZYME nomenclature database: 3.1.24.1
            ExplorEnz - The Enzyme Database: 3.1.24.1
            ERGO genome analysis and discovery system: 3.1.24.1
            BRENDA, the Enzyme Database: 3.1.24.1
///
ENTRY       EC 3.1.24.2       Obsolete  Enzyme
NAME        Transferred to 3.1.21.3
CLASS       Hydrolases;
            Acting on ester bonds;
            Site specific endodeoxyribonucleases: cleavage is not sequence
            specific (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease EcoK. Now EC 3.1.21.3, type
            I site-specific deoxyribonuclease. Assumed to be the same as
            endodeoxyribonuclease EcoKI (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.24.2 created 1978,
            modified 1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.24.2
            ExPASy - ENZYME nomenclature database: 3.1.24.2
            ExplorEnz - The Enzyme Database: 3.1.24.2
            ERGO genome analysis and discovery system: 3.1.24.2
            BRENDA, the Enzyme Database: 3.1.24.2
///
ENTRY       EC 3.1.24.3       Obsolete  Enzyme
NAME        Transferred to 3.1.21.5
CLASS       Hydrolases;
            Acting on ester bonds;
            Site specific endodeoxyribonucleases: cleavage is not sequence
            specific (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease EcoPI. Now EC 3.1.21.5,
            type III site-specific deoxyribonuclease. The name is misprinted in
            supplement 3 of the 1978 edition. (EC 3.1.24.3 created 1978,
            modified 1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.24.3
            ExPASy - ENZYME nomenclature database: 3.1.24.3
            ExplorEnz - The Enzyme Database: 3.1.24.3
            ERGO genome analysis and discovery system: 3.1.24.3
            BRENDA, the Enzyme Database: 3.1.24.3
///
ENTRY       EC 3.1.24.4       Obsolete  Enzyme
NAME        Transferred to 3.1.21.5
CLASS       Hydrolases;
            Acting on ester bonds;
            Site specific endodeoxyribonucleases: cleavage is not sequence
            specific (deleted sub-subclass)
COMMENT     Transferred entry: endodeoxyribonuclease EcoP15. Now EC 3.1.21.5,
            type III site-specific deoxyribonuclease. Assumed to be the same as
            endodeoxyribonuclease EcoP15I (see
            http://rebase.neb.com/rebase/rebase.html) (EC 3.1.24.4 created 1978,
            modified 1982, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.24.4
            ExPASy - ENZYME nomenclature database: 3.1.24.4
            ExplorEnz - The Enzyme Database: 3.1.24.4
            ERGO genome analysis and discovery system: 3.1.24.4
            BRENDA, the Enzyme Database: 3.1.24.4
///
ENTRY       EC 3.1.25.1                 Enzyme
NAME        deoxyribonuclease (pyrimidine dimer);
            endodeoxyribonuclease (pyrimidine dimer);
            endodeoxyribonuclease (pyrimidine dimer);
            bacteriophage T4 endodeoxyribonuclease V;
            T4 endonuclease V
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases that are specific for altered
            bases
REACTION    Endonucleolytic cleavage near pyrimidine dimers to products with
            5'-phosphate
COMMENT     Acts on a damaged strand, 5' from the damaged site.
REFERENCE   1
  AUTHORS   Braun, A.G., Radman, M. and Grossman, L.
  TITLE     Enzymic repair of DNA: sites of hydrolysis by the Escherichia coli
            endonuclease specific for pyrimidine dimers (corendonuclease II).
  JOURNAL   Biochemistry 15 (1976) 4116-4120.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:330526]
  AUTHORS   Riazuddin S, Grossman L.
  TITLE     Micrococcus luteus correndonucleases. II. Mechanism of action of two
            endonucleases specific for DNA containing pyrimidine dimers.
  JOURNAL   J. Biol. Chem. 252 (1977) 6287-93.
  ORGANISM  Micrococcus luteus
ORTHOLOGY   KO: K01161  deoxyribonuclease (pyrimidine dimer)
GENES       BME: BMEII0653
            BMF: BAB2_0621
            BMS: BRA0621
            BOV: BOV_A0583
            BLD: BLi02698
            PMA: Pro1489
            PMF: P9303_13661
            PTO: PTO1429
STRUCTURES  PDB: 1ENI  1ENJ  1ENK  1VAS  2END  2FCC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.25.1
            ExPASy - ENZYME nomenclature database: 3.1.25.1
            ExplorEnz - The Enzyme Database: 3.1.25.1
            ERGO genome analysis and discovery system: 3.1.25.1
            BRENDA, the Enzyme Database: 3.1.25.1
            CAS: 66143-22-4
///
ENTRY       EC 3.1.25.2       Obsolete  Enzyme
NAME        Transferred to 4.2.99.18
CLASS       Hydrolases;
            Acting on ester bonds;
            Site-specific endodeoxyribonucleases that are specific for altered
            bases
COMMENT     Transferred entry: now EC 4.2.99.18, DNA-(apurinic or apyrimidinic
            site) lyase (EC 3.1.25.2 created 1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.25.2
            ExPASy - ENZYME nomenclature database: 3.1.25.2
            ExplorEnz - The Enzyme Database: 3.1.25.2
            ERGO genome analysis and discovery system: 3.1.25.2
            BRENDA, the Enzyme Database: 3.1.25.2
///
ENTRY       EC 3.1.26.1                 Enzyme
NAME        Physarum polycephalum ribonuclease
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage to 5'-phosphomonoester
REFERENCE   1  [PMID:5817397]
  AUTHORS   Hiramaru M, Uchida T, Egami F.
  TITLE     Studies on two nucleases and a ribonuclease from Physarum
            polycephalum. Purification and mode of action.
  JOURNAL   J. Biochem. (Tokyo). 65 (1969) 701-8.
  ORGANISM  Physarum polycephalum
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.26.1
            ExPASy - ENZYME nomenclature database: 3.1.26.1
            ExplorEnz - The Enzyme Database: 3.1.26.1
            ERGO genome analysis and discovery system: 3.1.26.1
            BRENDA, the Enzyme Database: 3.1.26.1
            CAS: 9001-99-4
///
ENTRY       EC 3.1.26.2                 Enzyme
NAME        ribonuclease alpha;
            2'-O-methyl RNase
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage to 5'-phosphomonoester
COMMENT     Specific for O-methylated RNA.
REFERENCE   1  [PMID:6022850]
  AUTHORS   Norton J, Roth JS.
  TITLE     A ribonuclease specific for 2'-O-methylated ribonucleic acid.
  JOURNAL   J. Biol. Chem. 242 (1967) 2029-34.
  ORGANISM  Anacystis nidulans
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.26.2
            ExPASy - ENZYME nomenclature database: 3.1.26.2
            ExplorEnz - The Enzyme Database: 3.1.26.2
            ERGO genome analysis and discovery system: 3.1.26.2
            BRENDA, the Enzyme Database: 3.1.26.2
///
ENTRY       EC 3.1.26.3                 Enzyme
NAME        ribonuclease III;
            RNase III;
            ribonuclease 3
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage to a 5'-phosphomonoester
COMMENT     This is an endoribonuclease that cleaves double-stranded RNA
            molecules [4]. The cleavage can be either a single-stranded nick or
            double-stranded break in the RNA, depending in part upon the degree
            of base-pairing in the region of the cleavage site [5]. Specificity
            is conferred by negative determinants, i.e., the presence of certain
            Watson-Crick base-pairs at specific positions that strongly inhibit
            cleavage [6]. RNase III is involved in both rRNA processing and mRNA
            processing and decay.
REFERENCE   1  [PMID:4592261]
  AUTHORS   Crouch RJ.
  TITLE     Ribonuclease 3 does not degrade deoxyribonucleic acid-ribonucleic
            acid hybrids.
  JOURNAL   J. Biol. Chem. 249 (1974) 1314-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:6248530]
  AUTHORS   Rech J, Cathala G, Jeanteur P.
  TITLE     Isolation and characterization of a ribonuclease activity specific
            for double-stranded RNA (RNase D) from Krebs II ascites cells.
  JOURNAL   J. Biol. Chem. 255 (1980) 6700-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4865702]
  AUTHORS   Robertson HD, Webster RE, Zinder ND.
  TITLE     Purification and properties of ribonuclease III from Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 243 (1968) 82-91.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:10690408]
  AUTHORS   Grunberg-Manago M.
  TITLE     Messenger RNA stability and its role in control of gene expression
            in bacteria and phages.
  JOURNAL   Annu. Rev. Genet. 33 (1999) 193-227.
  ORGANISM  Escherichia coli [GN:eco], Rhodobacter capsulatus, Bacillus subtilis
            [GN:bsu], Salmonella typhimurium, Coxiella burnetii [GN:cbu]
REFERENCE   5
  AUTHORS   Court, D.
  TITLE     RNA processing and degradation by RNase III in control of mRNA
            stability.
  JOURNAL   In: Belasco, J.G. and Brawerman, G. (Eds.), Control of Messenger RNA
            Stability, Academic Press, New York, 1993, p. 71-116.
REFERENCE   6  [PMID:9391043]
  AUTHORS   Zhang K, Nicholson AW.
  TITLE     Regulation of ribonuclease III processing by double-helical sequence
            antideterminants.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 13437-41.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01162  ribonuclease III
            KO: K03684  ribonuclease D
            KO: K03685  ribonuclease III
GENES       HSA: 29102(RNASEN)
            PTR: 471576(RNASEN)
            MMU: 14000(Rnasen)
            CFA: 479375(RNASEN)
            GGA: 420911(RNASEN)
            DME: Dmel_CG8730
            CEL: F26E4.10(drsh-1)
            OSA: 4325844
            SCE: YMR239C(RNT1)
            AGO: AGOS_AFR538C
            PIC: PICST_30953 PICST_68661(RRP6)
            CAL: CaO19_3796(CaO19.3796)
            CGR: CAGL0M05159g
            SPO: SPBC119.11c(pac1)
            AFM: AFUA_3G03050 AFUA_5G04440
            DDI: DDB_0231869(drnB)
            ECO: b1804(rnd) b2567(rnc)
            ECJ: JW1793(rnd) JW2551(rnc)
            ECE: Z2847(rnd) Z3848(rnc)
            ECS: ECs2513 ECs3433
            ECC: c2208(rnd) c3091(rnc)
            ECI: UTI89_C1998(rnd) UTI89_C2888(rnc)
            ECP: ECP_1747 ECP_2569
            ECV: APECO1_3964(rnc) APECO1_862(rnd)
            ECW: EcE24377A_2853(rnc)
            ECX: EcHS_A2722(rnc)
            STY: STY1947(rnd) STY2827(rnc)
            STT: t0277(rnc) t1060(rnd)
            SPT: SPA0284(rnc) SPA1056(rnd)
            SEC: SC1810(rnd) SC2576(rnc)
            STM: STM1817(rnd) STM2581(rnc)
            YPE: YPO2075(rnd) YPO2718(rnc)
            YPK: y1297(rnc) y2235(rnd)
            YPM: YP_1918(rnd) YP_2522(rnc)
            YPA: YPA_1458 YPA_2452
            YPN: YPN_1206 YPN_1552
            YPP: YPDSF_1046 YPDSF_1553
            YPS: YPTB2058(rnd) YPTB2890(rnc)
            YPI: YpsIP31758_1136(rnc) YpsIP31758_2013(rnd)
            YEN: YE1017(rnc)
            SFL: SF1424(rnd) SF2629(rnc)
            SFX: S1539(rnd) S2802(rnc)
            SFV: SFV_1425(rnd) SFV_2630(rnc)
            SSN: SSON_1357(rnd) SSON_2691(rnc)
            SBO: SBO_1284(rnd) SBO_2595(rnc)
            SDY: SDY_1708(rnd) SDY_2808(rnc)
            ECA: ECA2371(rnd) ECA3278(rnc)
            PLU: plu2135(rnd) plu3340(rnc)
            BUC: BU258(rnc)
            BAS: BUsg249(rnc)
            BAB: bbp239(rnc)
            BCC: BCc_163(rnc)
            WBR: WGLp196(rnc)
            SGL: SG1333 SG1787
            ENT: Ent638_3054
            SPE: Spro_3669
            BFL: Bfl540(rnc)
            BPN: BPEN_560(rnc)
            HIN: HI0014(rnc) HI0390(rnd)
            HIT: NTHI0019(rnc) NTHI0511(rnd)
            HIP: CGSHiEE_03240(rnc)
            HDU: HD1478(rnd) HD1606(rnc)
            HSO: HS_0736(rnd) HS_1240(rnc)
            PMU: PM0061(rnc) PM0706(rnd)
            MSU: MS0368(rnc) MS1357(rnd)
            APL: APL_0543(rnc) APL_0616(rnd)
            ASU: Asuc_0580
            XFA: XF0751 XF2246
            XFT: PD1290(rnc) PD1904(rnd)
            XCC: XCC1273(rnc) XCC2306(rnD)
            XCB: XC_1809 XC_2968
            XCV: XCV1376(rncS) XCV2611(rnd)
            XAC: XAC1325(rnc) XAC2413(rnD)
            XOO: XOO1855(rnc) XOO2742(rnD)
            XOM: XOO_1751(XOO1751) XOO_2586(XOO2586)
            VCH: VC1984 VC2461
            VCO: VC0395_A1569(rnd) VC0395_A2039(rnc)
            VVU: VV1_0135 VV1_1565
            VVY: VV1054 VV2831
            VPA: VP0871 VP2572
            VFI: VF1707 VF2087
            PPR: PBPRA1076(rnd) PBPRA3089(rnc)
            PAE: PA0770(rnc) PA1294(rnd)
            PAU: PA14_47460(rnd) PA14_54330(rnc)
            PAP: PSPA7_4749(rnc)
            PPU: PP_1433(rnc) PP_4591(rnd)
            PPF: Pput_0048 Pput_4288
            PST: PSPTO_3922(rnd) PSPTO_4217(rnc)
            PSB: Psyr_1563 Psyr_3951
            PSP: PSPPH_1547(rnd) PSPPH_3948(rnc)
            PFL: PFL_1071(rncS) PFL_1495(rnd)
            PFO: Pfl_0994 Pfl_1388
            PEN: PSEEN4035(rnd) PSEEN4290(rnc)
            PMY: Pmen_1475
            PAR: Psyc_0333(rnc) Psyc_0795(rnd)
            PCR: Pcryo_0367 Pcryo_0801
            PRW: PsycPRwf_0374
            ACI: ACIAD2310(rnd) ACIAD2581(rnc)
            SON: SO_1348(rnc) SO_2580(rnd)
            SDN: Sden_1626 Sden_2766
            SFR: Sfri_1734 Sfri_2929
            SAZ: Sama_0880
            SBL: Sbal_1201
            SBM: Shew185_1245
            SLO: Shew_1054
            SPC: Sputcn32_1159
            SSE: Ssed_1148
            SPL: Spea_1037
            SHE: Shewmr4_2176 Shewmr4_2848
            SHM: Shewmr7_2253 Shewmr7_2930
            SHN: Shewana3_2385 Shewana3_3026
            SHW: Sputw3181_3005
            ILO: IL0810(rnc) IL1826(rnd)
            CPS: CPS_3518(rnd) CPS_4122(rnc)
            PHA: PSHAa0732(rnc) PSHAb0503(rnd)
            PAT: Patl_2803 Patl_3149
            SDE: Sde_1338 Sde_2243
            PIN: Ping_0640 Ping_1668
            MAQ: Maqu_2245
            CBU: CBU_1503
            CBD: COXBU7E912_0481(rnc)
            LPN: lpg1869(rnc)
            LPF: lpl1831(rnc)
            LPP: lpp1834(rnc)
            MCA: MCA1463(rnc) MCA2378(rnd)
            FTU: FTT0776c(rnd) FTT1555c(rnc)
            FTF: FTF0776c(rnd) FTF1555c(rnc)
            FTW: FTW_0372(rnc) FTW_1462
            FTL: FTL_0554 FTL_1449
            FTH: FTH_0555(rnc) FTH_1411(rnd)
            FTA: FTA_0587(rnc)
            FTN: FTN_0679(rnd) FTN_1463(rnc)
            TCX: Tcr_0734 Tcr_1582
            NOC: Noc_2458
            AEH: Mlg_1347
            HHA: Hhal_0034
            HCH: HCH_01800(rnc) HCH_02616(rnd)
            CSA: Csal_1461 Csal_1631
            ABO: ABO_1631(rnc) ABO_1768(rnd)
            MMW: Mmwyl1_1246
            AHA: AHA_0800(rnc) AHA_2205(rnd)
            DNO: DNO_0692(rnc) DNO_1123(rnd)
            BCI: BCI_0281(rnc)
            RMA: Rmag_0614
            VOK: COSY_0566(rnc)
            NME: NMB0686
            NMA: NMA0888(rnc)
            NMC: NMC0637(rnc)
            NGO: NGO0259
            CVI: CV_2066(rnc)
            RSO: RSc1063(rnc)
            REU: Reut_A2252
            RME: Rmet_2418
            BMA: BMA0543
            BMV: BMASAVP1_A2466(rnc)
            BMN: BMA10247_1789(rnc)
            BXE: Bxe_A1085
            BVI: Bcep1808_1053
            BUR: Bcep18194_A4246
            BCN: Bcen_0654
            BCH: Bcen2424_1134
            BAM: Bamb_1010
            BPS: BPSL2429(rnc)
            BPM: BURPS1710b_2895(rnc)
            BPL: BURPS1106A_2840(rnc)
            BPD: BURPS668_2779(rnc)
            BTE: BTH_I1730
            PNU: Pnuc_0406
            BPE: BP2431(rnc)
            BPA: BPP3295(rnc)
            BBR: BB3746(rnc)
            RFR: Rfer_1743
            POL: Bpro_3635
            PNA: Pnap_3061
            AAV: Aave_1196
            AJS: Ajs_3267
            VEI: Veis_3238
            MPT: Mpe_A0650
            HAR: HEAR2063
            MMS: mma_1370(rnc)
            NEU: NE2324(rnc)
            NET: Neut_1778
            NMU: Nmul_A1753
            EBA: ebA5539(rnc)
            AZO: azo1642(rnc)
            DAR: Daro_2029
            TBD: Tbd_2086
            MFA: Mfla_0863 Mfla_1007
            HPY: HP0662(rnc)
            HPJ: jhp0607(rnc)
            HPA: HPAG1_0538 HPAG1_0647
            HHE: HH0699(rnc)
            HAC: Hac_0847(rnc)
            WSU: WS1899(rnc)
            TDN: Tmden_2024
            CJE: Cj1635c(rnc)
            CJR: CJE1807(rnc)
            CJJ: CJJ81176_1626(rnc)
            CJU: C8J_1537(rnc)
            CJD: JJD26997_1995(rnc)
            CFF: CFF8240_1742(rnc)
            CCV: CCV52592_2065(rnc) CCV52592_2115
            CHA: CHAB381_1613(rnc)
            ABU: Abu_1613(rnc)
            NIS: NIS_0215(rnc)
            SUN: SUN_2259(rnc)
            GSU: GSU0443 GSU2228(rnc)
            GME: Gmet_2317 Gmet_3389
            GUR: Gura_3152
            PCA: Pcar_0323 Pcar_1403
            PPD: Ppro_1778
            DVU: DVU1440(rnc)
            DVL: Dvul_1639
            DDE: Dde_1708
            LIP: LI0571(rnc)
            BBA: Bd1941(rncS)
            DPS: DP1245 DP2797
            ADE: Adeh_1602 Adeh_1650
            AFW: Anae109_2159
            MXA: MXAN_3762(rnc) MXAN_5981
            SAT: SYN_00796 SYN_02700
            SFU: Sfum_0414 Sfum_0876
            RPR: RP117(rnc) RP422 RP462(rnd)
            RTY: RT0019(rnc) RT0408(rnd1) RT0449(rnd2)
            RCO: RC0157(rncS) RC0587(rnd2) RC0696(rnd)
            RFE: RF_0653(rnd2) RF_0809(rnd) RF_1176(rnc)
            RBE: RBE_0690(rnd) RBE_0748(rnd2) RBE_1181(rnc)
            RAK: A1C_00870(rnc)
            RBO: A1I_01375(rnc)
            RCM: A1E_00590(rnc) A1E_03245
            RRI: A1G_00905(rnc)
            OTS: OTBS_0265(rnd) OTBS_1703(rnc)
            WOL: WD0186 WD0878 WD1240
            WBM: Wbm0099 Wbm0258 Wbm0609
            AMA: AM1015(rnd) AM1069(rnc) AM151(rnd)
            APH: APH_0137 APH_1098 APH_1149(rnc)
            ERU: Erum6950 Erum7870 Erum8070(rnc)
            ERW: ERWE_CDS_07300(rnd) ERWE_CDS_08320(rnd) ERWE_CDS_08540(rnc)
            ERG: ERGA_CDS_07220(rnd) ERGA_CDS_08220(rnd) ERGA_CDS_08450(rnc)
            ECN: Ecaj_0703 Ecaj_0816 Ecaj_0847
            ECH: ECH_0300 ECH_1011 ECH_1054(rnc)
            NSE: NSE_0529 NSE_0918(rnc)
            PUB: SAR11_0498(rnd) SAR11_1053(rnc)
            MLO: mll3296 mll8354 mlr7765
            MES: Meso_0950 Meso_1121 Meso_3984
            PLA: Plav_2874
            SME: SMc00342 SMc00622(rnd) SMc02652(rnc)
            SMD: Smed_0682
            ATU: Atu1035(rnc) Atu1151(rnd) Atu4108(rnd)
            ATC: AGR_C_1906 AGR_C_2134 AGR_L_1490
            RET: RHE_CH00095(rnd1) RHE_CH01390(rnc) RHE_CH01495(rnd2)
            RLE: RL0104 RL1511(rnc) RL1603(rnd)
            BME: BMEI1203 BMEI1287 BMEI1828
            BMF: BAB1_0117 BAB1_0681(rnc) BAB1_0774
            BMS: BR0120 BR0661(rnc) BR0750(rnd)
            BMB: BruAb1_0117 BruAb1_0678(rncS) BruAb1_0767(rnd)
            BOV: BOV_0654(rnc)
            OAN: Oant_2627
            BJA: bll4135(rnd) bll5061(rnc) blr0719
            BRA: BRADO3356(rnd) BRADO4463(rnc)
            BBT: BBta_3861(rnd) BBta_4683(rnc)
            RPA: RPA0046 RPA2697 RPA3045(rnd)
            RPB: RPB_0659 RPB_2494 RPB_2612
            RPC: RPC_0419 RPC_2334 RPC_2640
            RPD: RPD_0174 RPD_2651 RPD_2949
            RPE: RPE_0426 RPE_3022 RPE_3278
            NWI: Nwi_0171 Nwi_1589 Nwi_1918
            NHA: Nham_0179 Nham_2112 Nham_2251
            BHE: BH02530(rnd1) BH05090(rnc) BH09800(rnd2)
            BQU: BQ02390(rnd1) BQ04280(rnc) BQ07560(rnd2)
            BBK: BARBAKC583_0473(rnc) BARBAKC583_0869(rnd)
            XAU: Xaut_3881
            CCR: CC_1560 CC_1704 CC_3603
            SIL: SPO0083 SPO2167(rnd) SPO3198(rnc)
            SIT: TM1040_0027 TM1040_1474 TM1040_2559
            RSP: RSP_1152(rnd) RSP_1675(rnc) RSP_1971(rnd)
            RSH: Rsph17029_0308 Rsph17029_0679
            RSQ: Rsph17025_2571
            JAN: Jann_0522 Jann_1838
            RDE: RD1_0367 RD1_1366(rnc) RD1_2254(rnd)
            PDE: Pden_0419 Pden_1890
            MMR: Mmar10_0109 Mmar10_1252 Mmar10_1571
            HNE: HNE_0877(rnc) HNE_2258(rnd)
            ZMO: ZMO0278(rnd) ZMO0714(rnd) ZMO1375(rnc)
            NAR: Saro_1337 Saro_1807 Saro_3251
            SAL: Sala_1213 Sala_1752 Sala_2343
            SWI: Swit_0209
            ELI: ELI_03960 ELI_04840 ELI_12160
            GOX: GOX0625 GOX1810 GOX1847
            GBE: GbCGDNIH1_0211 GbCGDNIH1_0701 GbCGDNIH1_0992
            ACR: Acry_0250
            RRU: Rru_A1852 Rru_A2073
            MAG: amb2258 amb2836 amb3932
            MGM: Mmc1_0327 Mmc1_0907
            ABA: Acid345_3854
            SUS: Acid_1804
            BSU: BG11537(rncS)
            BHA: BH2489(rncS)
            BAN: BA3987(rncS)
            BAR: GBAA3987(rncS)
            BAA: BA_4458
            BAT: BAS3700
            BCE: BC3847
            BCA: BCE_3891(rncS)
            BCZ: BCZK3608(rncS) BCZK3609(acpA)
            BCY: Bcer98_2501
            BTK: BT9727_3590(rncS)
            BTL: BALH_3480
            BLI: BL02317(rnc)
            BLD: BLi01814(rnc)
            BCL: ABC2299(rncS)
            BAY: RBAM_015760(rnc)
            BPU: BPUM_0080(yazC) BPUM_1492(rnc)
            OIH: OB1526
            GKA: GK1192
            GTN: GTNG_1045
            SAU: SA1076(rnc)
            SAV: SAV1233(rnc)
            SAM: MW1116(rnc)
            SAR: SAR1209
            SAS: SAS1167
            SAC: SACOL1248(rnc)
            SAB: SAB1097
            SAA: SAUSA300_1126(rnc)
            SAO: SAOUHSC_01203
            SAJ: SaurJH9_1292
            SAH: SaurJH1_1317
            SEP: SE0908
            SER: SERP0799(rnc)
            SHA: SH1681(rnc)
            SSP: SSP1536
            LMO: lmo1805(rncS)
            LMF: LMOf2365_1832
            LIN: lin1919(rncS)
            LWE: lwe1824(rncS)
            LLA: L0326(rnc)
            LLC: LACR_0862
            LLM: llmg_1753(rnc) llmg_2039
            SPY: SPy_0531(acpA)
            SPZ: M5005_Spy_0438(rncS)
            SPM: spyM18_0597(rnc)
            SPG: SpyM3_0375(acpA)
            SPS: SPs1478
            SPH: MGAS10270_Spy0439(acpA)
            SPI: MGAS10750_Spy0458(acpA)
            SPJ: MGAS2096_Spy0457(acpA)
            SPK: MGAS9429_Spy0437(acpA)
            SPF: SpyM51426(acpA)
            SPA: M6_Spy0472
            SPB: M28_Spy0426(rncS)
            SPN: SP_1248
            SPR: spr1127(rncS)
            SPD: SPD_1105(rnc)
            SAG: SAG0723(rnc)
            SAN: gbs0745
            SAK: SAK_0849(rnc)
            SMU: SMU.1514(rnc)
            STC: str1296(rncS)
            STL: stu1296(rncS)
            STE: STER_1272
            SSA: SSA_1561(rncS)
            SSU: SSU05_1191
            SSV: SSU98_1208
            SGO: SGO_0783(rnc)
            LPL: lp_1631(rnc)
            LJO: LJ1521
            LAC: LBA1297
            LSA: LSA0707(rncS)
            LSL: LSL_0625(rnc)
            LDB: Ldb1380(rnc)
            LBU: LBUL_1287
            LBR: LVIS_0952
            LCA: LSEI_1607
            LGA: LGAS_0780
            LRE: Lreu_1159
            PPE: PEPE_0842
            EFA: EF3097(rnc)
            OOE: OEOE_0453
            LME: LEUM_1565
            STH: STH1453
            CAC: CAC1748(rncS) CAC1909(rnd)
            CPE: CPE1718(rncS)
            CPF: CPF_1972(rnc)
            CPR: CPR_1690(rnc)
            CTC: CTC01243
            CNO: NT01CX_2219
            CTH: Cthe_0931
            CDF: CD1248(rnc)
            CBA: CLB_2319(rnc)
            CBH: CLC_2303(rnc)
            CBF: CLI_2511(rnc)
            CBE: Cbei_1170
            AMT: Amet_2752
            CHY: CHY_1444(rnc)
            DSY: DSY2656
            DRM: Dred_2069
            PTH: PTH_1738(rnc)
            SWO: Swol_0773
            CSC: Csac_0268 Csac_1057 Csac_1608
            TTE: TTE1469(rnc)
            MTA: Moth_0951
            MGE: MG_367(rnc)
            MPN: MPN545(rnc)
            MPU: MYPU_1630(rnc)
            MPE: MYPE3650(rnc)
            MGA: MGA_0180(rnc)
            MMY: MSC_0479(rnc)
            MMO: MMOB4110(rnc)
            MHY: mhp412(rnc)
            MHJ: MHJ_0411(rnc)
            MHP: MHP7448_0398(rnc)
            MSY: MS53_0675(rncS)
            MCP: MCAP_0492
            UUR: UU205(rnc)
            POY: PAM608(rnc)
            AYW: AYWB_143(rnc)
            MFL: Mfl231
            MTU: Rv2681 Rv2925c(rnc)
            MTC: MT2755 MT2995(rnc)
            MBO: Mb2700 Mb2950c(rnc)
            MBB: BCG_2947c(rnc)
            MLE: ML1040 ML1659(rnc)
            MPA: MAP2802 MAP2995c(rnc)
            MAV: MAV_3783(rnc)
            MSM: MSMEG_2418(rnc) MSMEG_2778
            MVA: Mvan_2171
            MGI: Mflv_4192
            MMC: Mmcs_1949
            MKM: Mkms_1995
            MJL: Mjls_1929
            CGL: NCgl1826(cgl1901) NCgl1994(rncS)
            CGB: cg2081(rnd) cg2273(rnc)
            CEF: CE1795 CE1976
            CDI: DIP1396 DIP1544(rnc)
            CJK: jk1077(rnd) jk1206(rnc)
            NFA: nfa37400(rnd) nfa41840(rnc)
            RHA: RHA1_ro06522 RHA1_ro06854
            SCO: SCO5572(SC7A1.16) SCO6028(SC1C3.16c)
            SMA: SAV2231(rnd) SAV2665(rnc)
            TWH: TWT394(rnd) TWT562(rnc)
            TWS: TW199(rnc) TW376
            LXX: Lxx09780(rnc) Lxx10490
            CMI: CMM_1358(rncA)
            ART: Arth_2501
            PAC: PPA1063 PPA1452
            NCA: Noca_3281
            TFU: Tfu_0651 Tfu_1901
            FRA: Francci3_1331 Francci3_3601
            FAL: FRAAL2098 FRAAL5804(rnc)
            ACE: Acel_1574
            KRA: Krad_1376
            SEN: SACE_1832 SACE_6100(rnc)
            STP: Strop_1287
            BLO: BL0295(rncS) BL0948
            BAD: BAD_0989 BCD_0222(rncS)
            RXY: Rxyl_1384
            FNU: FN0152
            RBA: RB4925 RB5689(rnd)
            CTR: CT297(rnc)
            CTA: CTA_0319(rnc)
            CMU: TC0570
            CPN: CPn0054(rnc)
            CPA: CP0721
            CPJ: CPj0054(rnc)
            CPT: CpB0055
            CCA: CCA00342(rnc)
            CAB: CAB334(rnc)
            CFE: CF0664(rnc)
            PCU: pc0274(rnc)
            BBU: BB0705(rnc)
            BGA: BG0727(rnc)
            BAF: BAPKO_0748(rnc)
            TPA: TP0809
            TDE: TDE1027(rnc)
            LIL: LA2917 LA4091 LB084
            LIC: LIC11141 LIC13263(rnD) LIC20066(rnC)
            LBJ: LBJ_0193(rnd) LBJ_2111(rnc) LBJ_2281
            LBL: LBL_0826 LBL_0940(rnc) LBL_2890(rnd)
            SYN: sll0320(rnd) slr0346(rnc) slr1646(rnc)
            SYW: SYNW0152(rnc) SYNW2036(rnd)
            SYC: syc0851_c(rnd) syc2441_c(rnc)
            SYF: Synpcc7942_0678 Synpcc7942_1645
            SYD: Syncc9605_0149 Syncc9605_0407
            SYE: Syncc9902_0179 Syncc9902_1922
            SYG: sync_0200(rnc)
            SYR: SynRCC307_0137(rnc) SynRCC307_2079(rnd)
            SYX: SynWH7803_0204(rnc) SynWH7803_0465(rnd)
            CYA: CYA_0804(rnc) CYA_1113
            CYB: CYB_0755(rnc) CYB_1361
            TEL: tlr1083
            GVI: gll3123 glr2648(rnc) glr3747
            ANA: all1697 all3791 all4107 alr0280
            AVA: Ava_0668 Ava_0797 Ava_1914 Ava_3081
            PMA: Pro1740(rnd) Pro1762(rnc)
            PMM: PMM1584(rnd) PMM1603(rnc)
            PMT: PMT1703(rnd) PMT1949(rnc)
            PMN: PMN2A_1157 PMN2A_1179
            PMI: PMT9312_1676 PMT9312_1696
            PMB: A9601_17921(rnd) A9601_18131(rnc) A9601_18181(acpP)
            PMC: P9515_17711(rnd) P9515_17911(rnc) P9515_17961(acpP)
            PMF: P9303_22631(rnd) P9303_26001(rnc) P9303_26061(acpP)
            PMG: P9301_17761(rnd) P9301_17961(rnc) P9301_18011(acpP)
            PMH: P9215_18771(rnc)
            PME: NATL1_20321(rnd) NATL1_20541(rnc) NATL1_20601(acpP)
            TER: Tery_1105 Tery_2144
            BTH: BT_3357
            BFR: BF0218
            BFS: BF0177
            PGI: PG1763(rnc)
            SRU: SRU_1343(rnc)
            CHU: CHU_1396(rnc)
            GFO: GFO_3384
            FJO: Fjoh_1139
            FPS: FP0202(rnc)
            CTE: CT2119(rnc)
            CCH: Cag_1659
            CPH: Cpha266_2495
            PVI: Cvib_0195
            PLT: Plut_0128
            DET: DET1025(rnc)
            DEH: cbdb_A994(rnc)
            DEB: DehaBAV1_0908
            RRS: RoseRS_3414 RoseRS_4602
            RCA: Rcas_0380 Rcas_1513
            AAE: aq_946(rnc)
            TMA: TM1102
            TPT: Tpet_1641
            TME: Tmel_1604
            FNO: Fnod_1081
            MMP: MMP1526(rncS)
            MMQ: MmarC5_0049
            MMZ: MmarC7_0774
            MVN: Mevan_0839
            MHU: Mhun_1116
            MEM: Memar_0367
            MSI: Msm_0176
STRUCTURES  PDB: 1I4S  1JFZ  1O0W  1RC5  1RC7  1T4N  1T4O  1YT3  1YYK  1YYO  
                 1YYW  1YZ9  2A11  2EZ6  2FFL  2QVW  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.26.3
            ExPASy - ENZYME nomenclature database: 3.1.26.3
            ExplorEnz - The Enzyme Database: 3.1.26.3
            ERGO genome analysis and discovery system: 3.1.26.3
            BRENDA, the Enzyme Database: 3.1.26.3
            CAS: 78413-14-6
///
ENTRY       EC 3.1.26.4                 Enzyme
NAME        calf thymus ribonuclease H;
            endoribonuclease H (calf thymus);
            RNase H;
            RNA*DNA hybrid ribonucleotidohydrolase;
            hybrid ribonuclease;
            hybridase;
            hybridase (ribonuclease H);
            ribonuclease H;
            hybrid nuclease
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage to 5'-phosphomonoester
COMMENT     Acts on RNA-DNA hybrids.
REFERENCE   1  [PMID:4709937]
  AUTHORS   Haberkern RC, Cantoni GL.
  TITLE     Studies on a calf thymus ribonuclease specific for ribonucleic
            acid-deoxyribonucleic acid hybrids.
  JOURNAL   Biochemistry. 12 (1973) 2389-95.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:4516197]
  AUTHORS   Stavrianopoulos JG, Chargaff E.
  TITLE     Purification and properties of ribonuclease H of calf thymus.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 70 (1973) 1959-63.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K01163  ribonuclease H
            KO: K03469  ribonuclease HI
            KO: K03470  ribonuclease HII
            KO: K03471  ribonuclease HIII
GENES       HSA: 10535(RNASEH2A) 246243(RNASEH1)
            PTR: 455752(RNASEH2A)
            MMU: 19819(Rnaseh1) 69724(Rnaseh2a)
            RNO: 298933(Rnaseh1)
            CFA: 475648(RNASEH1) 484925(RNASEH2A)
            GGA: 395848(RNASEH1)
            XLA: 414644(MGC81203)
            XTR: 394751(rnaseh2a)
            DRE: 393195(rnaseh2a) 436932(rnaseh1)
            SPU: 577358(LOC577358) 584833(LOC584833) 759796(LOC759796)
            DME: Dmel_CG13690 Dmel_CG8729(rnh1)
            CEL: C04F12.9(rnh-1.3) T13H5.7(rnh-2)
            ATH: AT2G25100
            OSA: 4349811
            CME: CMK297C CMT626C
            SCE: YMR234W(RNH1) YNL072W(RNH201)
            AGO: AGOS_ABL017C AGOS_AER363W
            PIC: PICST_31007 PICST_84962
            CAL: CaO19_5614(CaO19.5614)
            CGR: CAGL0J04246g CAGL0J10208g
            SPO: SPAC4G9.02 SPBC336.06c(rnh1)
            ANI: AN5114.2 AN5188.2
            AFM: AFUA_1G07180 AFUA_1G07600 AFUA_1G10020
            AOR: AO090012000971 AO090012001012
            CNE: CNA03470 CNI02520
            UMA: UM06131.1
            ECU: ECU03_0670
            DDI: DDBDRAFT_0184459 DDBDRAFT_0218016
            PFA: PFF1150w
            CHO: Chro.40245
            TAN: TA19790
            TPV: TP01_0041
            TET: TTHERM_00142290
            TBR: Tb10.70.2140 Tb10.70.2470 Tb927.7.4930
            TCR: 503891.70 505939.60 506351.40 508661.50
            LMA: LmjF06.0290
            EHI: 36.t00028
            ECO: b0183(rnhB) b0214(rnhA)
            ECJ: JW0178(rnhB) JW0204(rnhA)
            ECE: Z0195(rnhB) Z0239(rnhA)
            ECS: ECs0185 ECs0210
            ECC: c0220(rnhB) c0251(rnhA)
            ECI: UTI89_C0198(rnhB) UTI89_C0233(rnhA)
            ECP: ECP_0191 ECP_0220
            ECV: APECO1_1776(rnhA) APECO1_1804(rnhB)
            ECW: EcE24377A_0187(rnhB) EcE24377A_0219(rnhA)
            ECX: EcHS_A0181(lpxD) EcHS_A0185(rnhB) EcHS_A0219(rnhA)
            STY: HCM2.0109c STY0253(rnhB) STY0284(rnhA)
            STT: t0231(rnhB) t2602(rnhA)
            SPT: SPA0237(rnhB) SPA2506(rnhA)
            SEC: SC0230(rnhB) SC0259(rnhA)
            STM: STM0230(rnhB) STM0263(rnhA)
            YPE: YPO1058(rnhB) YPO1081(rnhA)
            YPK: y3095(rnhA) y3121(rnhB)
            YPM: YP_2768(rnhA) YP_2792(rnhB)
            YPA: YPA_0534 YPA_0559
            YPN: YPN_2917 YPN_2942
            YPP: YPDSF_1654
            YPS: YPTB2965(rnhA) YPTB2989(rnhB)
            YPI: YpsIP31758_1027(rnhB)
            SFL: SF0173(rnhB) SF0201(rnhA)
            SFX: S0176(rnhB) S0208(rnhA)
            SFV: SFV_0166(rnhB) SFV_0199(rnhA)
            SSN: SSON_0195(rnhB) SSON_0228(rnhA)
            SBO: SBO_0171(rnhB) SBO_0203(rnhA)
            SDY: SDY_0199(rnhB) SDY_0233(rnhA)
            ECA: ECA1045(rnhB) ECA3340
            PLU: plu0686(rnhB) plu0942(rnhA)
            BAS: BUsg239(rnhA)
            BAB: bbp229(rnhA)
            WBR: WGLp068(rnhA)
            SGL: SG0591 SG1929
            ENT: Ent638_0721
            KPN: KPN_00196(rnhB)
            SPE: Spro_0911 Spro_3776
            BFL: Bfl224(rnhA) Bfl285(rnhB)
            BPN: BPEN_231(rnhA) BPEN_293(rnhB)
            HIN: HI0138(rnh) HI1059(rnhB)
            HIT: NTHI0224(rnhA) NTHI1219(rnhB)
            HIP: CGSHiEE_02595(rnhA)
            HIQ: CGSHiGG_08925(rnhB)
            HDU: HD1026(rnhB) HD1206(rnhA)
            HSO: HS_0604(rnhA) HS_1357(rnhB)
            PMU: PM0107(rnh) PM1998(rnhB)
            MSU: MS0423(rnhB) MS1571(rnhA)
            APL: APL_0129(rnhB) APL_0423(rnhA)
            ASU: Asuc_1892
            XFA: XF1041 XF2158
            XFT: PD0321(rnhB) PD1218(rnhA)
            XCC: XCC0987(rnhA) XCC1359(rnhB)
            XCB: XC_2879 XC_3256
            XCV: XCV1089(rnhA) XCV1464(rnhB)
            XAC: XAC1089(rnhA) XAC1407(rnhB)
            XOO: XOO1041(rnhA) XOO1963(rnhB)
            XOM: XOO_0940(XOO0940) XOO_1853(XOO1853)
            VCH: VC0498 VC2234 VC2246
            VCO: VC0395_A1826(rnhA) VC0395_A1837(rnhB)
            VVU: VV1_1874 VV1_1886
            VVY: VV0516 VV0806 VV2254 VV2530 VV2543
            VPA: VP2293 VP2304 VPA0440
            VFI: VF1936 VF1948 VFA0524
            PPR: PBPRA1876 PBPRA2918 PBPRA2954
            PAE: PA1815(rnhA) PA3642(rnhB)
            PAU: PA14_17230(rnhB) PA14_41060(rnhA)
            PPU: PP_1605(rnhB) PP_4142(rnhA)
            PPF: Pput_1723 Pput_4172
            PST: PSPTO_1548(rnhB) PSPTO_3712(rnhA)
            PSB: Psyr_1357 Psyr_1763
            PSP: PSPPH_1712(rnhA) PSPPH_3826(rnhB)
            PFL: PFL_1190(rnhB) PFL_3297(rnhA)
            PFO: Pfl_1115 Pfl_2186
            PEN: PSEEN3559(rnhA) PSEEN4206(rnhB)
            PMY: Pmen_3039 Pmen_4263
            PAR: Psyc_0833(dnaQ) Psyc_0912
            PCR: Pcryo_1505
            PRW: PsycPRwf_0923
            ACI: ACIAD1137(rnhA-dnaQ) ACIAD1248(rnhB)
            SON: SO_1643(rnhB) SO_2560(rnhA)
            SDN: Sden_0758 Sden_1568 Sden_2019
            SFR: Sfri_1284 Sfri_2205 Sfri_3175
            SAZ: Sama_1153
            SBL: Sbal_1464
            SBM: Shew185_1459 Shew185_2014
            SLO: Shew_2621
            SPC: Sputcn32_1362
            SSE: Ssed_1992 Ssed_3147
            SPL: Spea_2403 Spea_2871
            SHE: Shewmr4_2158 Shewmr4_2627
            SHM: Shewmr7_2235 Shewmr7_2694
            SHN: Shewana3_2366 Shewana3_2801
            SHW: Sputw3181_2741
            ILO: IL1670(rnhB) IL1694(rnhA)
            CPS: CPS_1569(rnhB) CPS_1701(rnhA)
            PHA: PSHAa1964(rnhA) PSHAa2016(rnhB)
            PAT: Patl_1263 Patl_2365
            SDE: Sde_0066 Sde_2583
            PIN: Ping_2962
            MAQ: Maqu_1534 Maqu_2534
            CBU: CBU_0316 CBU_1339(rnhB)
            CBD: COXBU7E912_1428(rnhB)
            LPN: lpg1373(rnhB) lpg1383(rnhA)
            LPF: lpl1324(rnhB) lpl1334(rnhA)
            LPP: lpp1327(rnhB) lpp1338(rnhA)
            MCA: MCA0719(rnhA) MCA2443(rnhB)
            FTU: FTT0590(rnhA) FTT1278c(rnhB)
            FTF: FTF0590(rnhA) FTF1278c(rnhB)
            FTW: FTW_0562(rnhB)
            FTL: FTL_0854 FTL_1182
            FTH: FTH_0843(rnhA) FTH_1158(rnhB)
            FTA: FTA_1248(rnhB)
            FTN: FTN_1089(rnhA) FTN_1293(rnhB)
            TCX: Tcr_0928 Tcr_1272
            NOC: Noc_2022 Noc_2815
            AEH: Mlg_1850 Mlg_1992
            HHA: Hhal_1454
            HCH: HCH_02527(rnhA) HCH_05237
            CSA: Csal_0577 Csal_1942
            ABO: ABO_1157(rnhB) ABO_1224(rnhA)
            MMW: Mmwyl1_1286 Mmwyl1_1704 Mmwyl1_3648
            AHA: AHA_1187(rnhB) AHA_1568(rnhA)
            DNO: DNO_0687(rnhB)
            BCI: BCI_0474(rnhA)
            RMA: Rmag_0374
            VOK: COSY_0352(rnhA)
            NME: NMB0192 NMB1618
            NMA: NMA0075(rnhB) NMA1817(rnhA)
            NMC: NMC0183(rnhB) NMC1544(rnhA)
            NGO: NGO1162 NGO1789(rnhB)
            CVI: CV_1256(rnhA) CV_2210(rnhB)
            RSO: RSc1418(rnhB) RSc1513(rnhA)
            REU: Reut_A1867 Reut_A2189
            REH: H16_A2041(rnhB) H16_A2466(rnhA)
            RME: Rmet_1449 Rmet_2208
            BMA: BMA0763(rnhA) BMA1541(rnhB)
            BMV: BMASAVP1_A1273(rnhA) BMASAVP1_A2041(rnhB)
            BML: BMA10299_A0596(rnhA) BMA10299_A3270(rnhB)
            BMN: BMA10247_0556(rnhA) BMA10247_1313(rnhB)
            BXE: Bxe_A1251 Bxe_A1696
            BVI: Bcep1808_1911
            BUR: Bcep18194_A4427 Bcep18194_A5315
            BCN: Bcen_0804 Bcen_6072
            BCH: Bcen2424_1285 Bcen2424_2005
            BAM: Bamb_1162 Bamb_2038
            BPS: BPSL1342(rnhA) BPSL2145(rnhB)
            BPM: BURPS1710b_1600(rnhA) BURPS1710b_2568(rnhB)
            BPL: BURPS1106A_1496(rnhA) BURPS1106A_2478(rnhB)
            BPD: BURPS668_1466(rnhA) BURPS668_2422(rnhB)
            BTE: BTH_I2041(rnhB) BTH_I2790(rnhA)
            PNU: Pnuc_1024 Pnuc_1437
            BPE: BP1433(rnhB) BP3211(rnhA)
            BPA: BPP1541(rnhB) BPP3834(rnhA)
            BBR: BB2619(rnhB) BB4278(rnhA)
            RFR: Rfer_1464 Rfer_2002
            POL: Bpro_2281 Bpro_2681
            PNA: Pnap_1680 Pnap_1772
            AAV: Aave_1837 Aave_2653
            AJS: Ajs_1745 Ajs_2571
            VEI: Veis_0593 Veis_1452
            MPT: Mpe_A1966 Mpe_A2527 Mpe_B0154
            HAR: HEAR1349(rnhB)
            MMS: mma_1211(rnhA) mma_2044(rnhB)
            NEU: NE0140(rnhA) NE1707(rnhB)
            NET: Neut_2024 Neut_2176
            NMU: Nmul_A0668 Nmul_A1619
            EBA: ebA6003(rnhB) ebA6458(rnhA)
            AZO: azo0772(rnhA1) azo1895(rnhB) azo2055(rnhA2)
            DAR: Daro_1593 Daro_1756
            TBD: Tbd_0799 Tbd_1663
            MFA: Mfla_1479 Mfla_1516
            HPY: HP0661(rnhA) HP1323(rnhB)
            HPJ: jhp0606(rnhA) jhp1243(rnhB)
            HPA: HPAG1_0646 HPAG1_1268
            HHE: HH0006(rnhB) HH0698(rnhA)
            HAC: Hac_0132(rnhB) Hac_0846(rnhA)
            WSU: WS1718(rnhB) WS1900(rnhA)
            TDN: Tmden_0280 Tmden_2025
            CJE: Cj0010c(rnhB) Cj1636c(rnhA)
            CJR: CJE0009(rnhB) CJE1808(rnhA)
            CJJ: CJJ81176_0036(rnhB)
            CJU: C8J_0009(rnhB) C8J_1538(rnhA)
            CJD: JJD26997_0010(rnhB)
            CFF: CFF8240_0016(rnhB)
            CCV: CCV52592_0405 CCV52592_1765(rnhB)
            CHA: CHAB381_0430(rnhB)
            CCO: CCC13826_0342(rnhB)
            ABU: Abu_1488(rnhA) Abu_1627(rnhB)
            NIS: NIS_0214(rnhA) NIS_0218(rnhB)
            SUN: SUN_2258(rnhA) SUN_2262(rnhB)
            GSU: GSU0649(rnhB) GSU2071(rnhA)
            GME: Gmet_0935 Gmet_2865
            GUR: Gura_1220 Gura_2851 Gura_3757
            PCA: Pcar_0204 Pcar_2218
            PPD: Ppro_1092
            DVU: DVU0689(rnhA) DVU0834(rnhB)
            DVL: Dvul_2147
            DDE: Dde_1094 Dde_2941
            LIP: LI0222(rplS) LI0756(rnh)
            BBA: Bd2116(rnhB) Bd2138(rnhA) Bd3131(rnhA)
            DPS: DP0910 DP2806
            ADE: Adeh_0278 Adeh_2077
            AFW: Anae109_0302
            MXA: MXAN_2265(rnhA) MXAN_2574(rnhB) MXAN_5728(rnhA)
            SAT: SYN_00291 SYN_00771
            SFU: Sfum_0852 Sfum_3003 Sfum_3045
            RPR: RP202(rnhB) RP726(rnhA)
            RTY: RT0192(rnhB) RT0713(rnhA)
            RCO: RC0264(rnhB) RC1108(rnhA)
            RFE: RF_0180(rnhA) RF_1061(rnhB)
            RBE: RBE_0366(rnhA) RBE_0511(rnhB)
            RAK: A1C_01485(rnhB) A1C_05880(rnhA)
            RBO: A1I_02935(rnhB)
            RCM: A1E_01050(rnhB) A1E_01125(rnhA)
            RRI: A1G_01510(rnhB) A1G_06145(rnhA)
            OTS: OTBS_0859(rnhB) OTBS_1582(rnhA)
            WOL: WD0304(rnhA) WD1103(rnhB)
            WBM: Wbm0305 Wbm0642
            AMA: AM126(rnhA) AM264(rnhB)
            APH: APH_0109(rnhA) APH_1022(rnhB)
            ERU: Erum1760(rnhB) Erum7260(rnhA)
            ERW: ERWE_CDS_01750(rnhB) ERWE_CDS_07640(rnhA)
            ERG: ERGA_CDS_01700(rnhB) ERGA_CDS_07560(rnhA)
            ECN: Ecaj_0173 Ecaj_0761
            ECH: ECH_0263(rnhA) ECH_0946(rnhB)
            NSE: NSE_0667(rnhA) NSE_0701(rnhB)
            PUB: SAR11_0108(rnhB) SAR11_0126(rnhA)
            MLO: mll7416 mlr7504
            MES: Meso_0703 Meso_0750
            PLA: Plav_0684 Plav_0703
            SME: SMc00018(rnhA1) SMc00867(rnhB) SMc02327(rnhA2)
            SMD: Smed_0451 Smed_0529
            ATU: Atu0720(rnhB) Atu0776
            ATC: AGR_C_1307 AGR_C_1417
            RET: RHE_CH00868(rnhB) RHE_CH00963(rnhA)
            RLE: RL0930 RL1032(rnhA) RL2672(rnhA)
            BME: BMEI1457 BMEI1542
            BMF: BAB1_0415(rnhB) BAB1_0503(rnhA)
            BMS: BR0386(rnhB) BR0477(rnhA)
            BMB: BruAb1_0411(rnhB) BruAb1_0499(rnhA)
            BOV: BOV_0398(rnhB)
            OAN: Oant_0507
            BJA: blr1316 blr2521(rnhB)
            BRA: BRADO2017(rnhB) BRADO6586(rnhA)
            BBT: BBta_0950(rnhA) BBta_2343(rnhB)
            RPA: RPA1034(rnh2) RPA4269
            RPB: RPB_1081 RPB_1342
            RPC: RPC_4076 RPC_4361
            RPD: RPD_1208 RPD_4028
            RPE: RPE_4128 RPE_4424
            NWI: Nwi_2598 Nwi_2687
            NHA: Nham_3221 Nham_3743
            BHE: BH04230(rnhB) BH04430(rnhA)
            BQU: BQ03420(rnhB) BQ03620(rnhA)
            BBK: BARBAKC583_0388(rnhB) BARBAKC583_0409(rnhA)
            XAU: Xaut_1101 Xaut_1266 Xaut_2357
            CCR: CC_0379 CC_3365
            SIL: SPO3212(rnhA) SPO3452(rnhB)
            SIT: TM1040_2573 TM1040_2650
            RSP: RSP_0867(rnhA) RSP_1470(rnhB)
            RSH: Rsph17029_0120
            RSQ: Rsph17025_0067 Rsph17025_0154
            JAN: Jann_0391 Jann_0502
            RDE: RD1_0300(rnhB) RD1_1351(rnhA)
            PDE: Pden_2102
            MMR: Mmar10_2192 Mmar10_2217
            HNE: HNE_0945(rnhA) HNE_2755(rnhB)
            ZMO: ZMO1004(rnhB) ZMO1601(rnhA)
            NAR: Saro_1085 Saro_1839
            SAL: Sala_0963 Sala_1134
            SWI: Swit_4574
            ELI: ELI_01550 ELI_02270
            GOX: GOX0177 GOX0345
            GBE: GbCGDNIH1_1858 GbCGDNIH1_1877
            ACR: Acry_0639
            RRU: Rru_A3054 Rru_A3209
            MAG: amb0762 amb3989
            MGM: Mmc1_0508 Mmc1_2115
            ABA: Acid345_2878
            SUS: Acid_2565
            BSU: BG12324(rnhC) BG12666(rnhB)
            BHA: BH2475(rnh)
            BAN: BA1623(rnhA) BA1626 BA3975(rnhB) BA4798(rnh)
            BAR: GBAA1623(rnhA) GBAA1626 GBAA3975(rnhB) GBAA4798(rnh)
            BAA: BA_2140 BA_2143 BA_4445 BA_5224
            BAT: BAS1507 BAS1510 BAS3688 BAS4451
            BCE: BC1597 BC1600 BC3835 BC4556
            BCA: BCE_1714(rnhA) BCE_1717 BCE_3879(rnhB) BCE_4682(rnh)
            BCZ: BCZK1469(rnhA) BCZK3596(rnhB) BCZK4300(rnh)
            BCY: Bcer98_2489 Bcer98_3244
            BTK: BT9727_1479(rnhA) BT9727_3578(rnhB) BT9727_4289(rnh)
            BTL: BALH_4139(rnhC)
            BLI: BL00302(rnhC) BL01288(rnhB)
            BLD: BLi01826(rnhB) BLi03009(rnhC)
            BCL: ABC2014 ABC2284(rnhB)
            BAY: RBAM_015890(rnhB)
            BPU: BPUM_1504(rnhB) BPUM_1935(rnhA) BPUM_2520(rnhC)
            OIH: OB1540(rnh) OB2128
            GKA: GK1205 GK1351 GK2697
            SAU: SA0987 SA1087(rnhB)
            SAV: SAV1140 SAV1244(rnhB)
            SAM: MW1023 MW1127(rnhB)
            SAR: SAR1113 SAR1220(rnhB)
            SAS: SAS1074 SAS1178
            SAC: SACOL1150(rnhC) SACOL1261(rnhB)
            SAB: SAB1004c SAB1108
            SAA: SAUSA300_1039(rnhC) SAUSA300_1137(rnhB)
            SAO: SAOUHSC_01095 SAOUHSC_01215
            SAJ: SaurJH9_1199 SaurJH9_1303
            SAH: SaurJH1_1221 SaurJH1_1328
            SEP: SE0833 SE0922
            SER: SERP0723(rnhC) SERP0812(rnhB)
            SHA: SH1669(rnhB) SH1821
            SSP: SSP1522 SSP1655
            LMO: lmo1228(rnhC) lmo1273(rnhB)
            LMF: LMOf2365_1237 LMOf2365_1291(rnhB) LMOf2365_1909(rnhA)
            LIN: lin1191(rnhC) lin1312(rnhB)
            LWE: lwe1183 lwe1290(rnhB) lwe1899(rnhA)
            LLA: L0320(rnhB) L132875(rnhA)
            LLC: LACR_1415 LACR_2587
            LLM: llmg_1176(rnhB) llmg_2549(rnhA)
            SPY: SPy_1162(rnh) SPy_1841
            SPZ: M5005_Spy_0883(rnhB) M5005_Spy_1564
            SPM: spyM18_1122(rnhB) spyM18_1906
            SPG: SpyM3_0818(rnh) SpyM3_1591
            SPS: SPs0276 SPs1019
            SPH: MGAS10270_Spy0997 MGAS10270_Spy1631
            SPI: MGAS10750_Spy1032 MGAS10750_Spy1623
            SPJ: MGAS2096_Spy0957 MGAS2096_Spy1589
            SPK: MGAS9429_Spy1001 MGAS9429_Spy1569
            SPF: SpyM50286 SpyM50907(rnh)
            SPA: M6_Spy0879 M6_Spy1576
            SPB: M28_Spy0857(rnhB) M28_Spy1552
            SPN: SP_0403 SP_1156
            SPR: spr0365(rnhB) spr1044(rnh)
            SPD: SPD_1020(rnhB)
            SAG: SAG1012(rnhB) SAG1722(rnhC)
            SAN: gbs1047 gbs1767
            SAK: SAK_1107(rnhB) SAK_1730(rnhC)
            SMU: SMU.1873(rnh3) SMU.994(rnh)
            STC: str0894(rnhA) str1765(rnhB)
            STL: stu0894(rnhA) stu1765(rnhB)
            SSA: SSA_0352(rnhC) SSA_1188(rnh)
            SGO: SGO_1201(rnhB)
            LPL: lp_1853(rnhB) lp_2593(rnh)
            LJO: LJ0098 LJ1106
            LAC: LBA0121 LBA0979
            LSA: LSA0391(rnhC) LSA0993(rnhB)
            LSL: LSL_0415(rnhA) LSL_0718(rnhB) LSL_0840
            LDB: Ldb0176(rnhA1) Ldb1275(rnhB)
            LBU: LBUL_0152 LBUL_1192
            LBR: LVIS_0796 LVIS_0836 LVIS_1930
            LCA: LSEI_1398 LSEI_1462 LSEI_2646
            LGA: LGAS_0096
            LRE: Lreu_0777
            PPE: PEPE_0304
            EFA: EF1267(rnhC) EF1653(rnhB)
            OOE: OEOE_1019
            STH: STH1474 STH2029 STH2922
            CAC: CAC1762(rnh)
            CPE: CPE1706(rnh)
            CPF: CPF_1960(rnhB)
            CPR: CPR_1436 CPR_1678(rnhB)
            CTC: CTC01255
            CNO: NT01CX_2206
            CTH: Cthe_0761
            CDF: CD1262(rnhB)
            CBO: CBO0402(rnh)
            CBA: CLB_0424(rnhA) CLB_2305(rnhB)
            CBH: CLC_0439(rnhA) CLC_2289(rnhB)
            CBF: CLI_0477(rnhA) CLI_2497(rnhB)
            CBE: Cbei_1182
            AMT: Amet_2740
            CHY: CHY_0852(rnhA) CHY_1426(rnhB)
            DSY: DSY2589
            DRM: Dred_0914 Dred_2047
            SWO: Swol_1478 Swol_2115
            CSC: Csac_2151
            TTE: TTE1362(rnhA) TTE1451(rnhB)
            MTA: Moth_0619 Moth_0976
            MPU: MYPU_3000(rnhB)
            MPE: MYPE10220(rnhB)
            MMY: MSC_0328(rnh) MSC_0430(rnhB)
            MMO: MMOB1230(rnhB) MMOB6240(rnhB)
            MHY: mhp613(rnhB)
            MHJ: MHJ_0593(rnhB)
            MHP: MHP7448_0593(rnhB)
            MSY: MS53_0619(rnhB)
            MCP: MCAP_0319 MCAP_0542
            UUR: UU397(rnhB)
            MFL: Mfl537
            MTU: Rv2902c(rnhB)
            MTC: MT2970(rnhB)
            MBO: Mb2926c(rnhB)
            MBB: BCG_2923c(rnhB)
            MLE: ML1611(rnhB)
            MPA: MAP2970c(rnhB)
            MAV: MAV_3757(rnhB)
            MSM: MSMEG_2442 MSMEG_5562(rnhA)
            MVA: Mvan_2194
            MGI: Mflv_4168
            MMC: Mmcs_1972 Mmcs_4350
            MKM: Mkms_2018
            MJL: Mjls_1952
            CGL: NCgl1957(rnhB)
            CGB: cg2230(rnhB)
            CEF: CE1925
            CDI: DIP1515(rnhB)
            CJK: jk1182(rnhB)
            NFA: nfa41450(rnhB) nfa56240(rnhA)
            RHA: RHA1_ro02274 RHA1_ro06544
            SCO: SCO5812 SCO7284(rnhA)
            SMA: SAV1138(rnhA) SAV2453(rnh)
            TWH: TWT239(rnhA)
            TWS: TW531(rnhA)
            LXX: Lxx14810(rnhB)
            CMI: CMM_0874(rnhA)
            ART: Arth_2476
            PAC: PPA1433 PPA1729
            NCA: Noca_3253
            TFU: Tfu_2145
            FRA: Francci3_3588
            FAL: FRAAL3840(rnhA) FRAAL5787(rnhB)
            ACE: Acel_1554
            KRA: Krad_1405
            SEN: SACE_6047(rnhB) SACE_6195(rnhA)
            STP: Strop_1312
            BLO: BL0276 BL1624(rnh)
            BAD: BAD_0234
            RXY: Rxyl_0795 Rxyl_1393
            FNU: FN1371
            RBA: RB10271(rnH) RB2637(rnhA)
            CTR: CT008(rnhB_1) CT029(rnhB_2)
            CTA: CTA_0009(rnhC) CTA_0031(rnhB)
            CMU: TC0276 TC0298
            CPN: CPn0119(rnhB_1) CPn1068(rnhB_2)
            CPA: CP0654 CP0782
            CPJ: CPj0119(rnhB_1) CPj1068(rnhB_2)
            CPT: CpB0120 CpB1112
            CCA: CCA00293(rnhC) CCA00654(rnhB)
            CAB: CAB291(rnhC) CAB625(rnhB)
            CFE: CF0357(rnhB1) CF0709(rnhB2)
            PCU: pc0658(rnh) pc0679(rnhB)
            BBU: BB0046(rnhB)
            BGA: BG0045(rnhB)
            BAF: BAPKO_0046(rnhB)
            TPA: TP0353
            TDE: TDE1547(rnhB) TDE2570(rnhA)
            LIL: LA2386
            LIC: LIC11560(rnhB)
            LBJ: LBJ_1431(rnhB)
            LBL: LBL_1655(rnhB)
            SYN: slr0080(rnhA) slr1130(rhnB)
            SYW: SYNW2144(rnhB) SYNW2338(rnhA)
            SYC: syc0661_c(rnhB) syc1913_d(rnhA)
            SYF: Synpcc7942_0879 Synpcc7942_2183
            SYD: Syncc9605_0314 Syncc9605_2466
            SYE: Syncc9902_2028 Syncc9902_2151
            SYG: sync_0375(rnhB) sync_2722(rnhA)
            SYR: SynRCC307_2176(rnhB) SynRCC307_2354(rnhA)
            SYX: SynWH7803_0373(rnhB) SynWH7803_2369(rnhA)
            CYA: CYA_0798(rnhA) CYA_0822(rnhB)
            CYB: CYB_1340(rnhA) CYB_1824(rnhB)
            TEL: tll0663(rhnB) tlr0299(rnhA)
            GVI: gll3612(rnhA) glr1507(rnhA)
            ANA: alr0142 alr4332
            AVA: Ava_1282 Ava_1511
            PMA: Pro0226(rnhA) Pro1658(rnhB)
            PMM: PMM0200(rnhA) PMM1502
            PMT: PMT1788 PMT2093(rnhA)
            PMN: PMN2A_1068 PMN2A_1567
            PMI: PMT9312_0202 PMT9312_1594
            PMB: A9601_02181(rnhA) A9601_17051(rnhB)
            PMC: P9515_02291(rnhA) P9515_16821(rnhB)
            PMF: P9303_23711(rnhB) P9303_27831(rnhA)
            PMG: P9301_02201(rnhA) P9301_16931(rnhB)
            PMH: P9215_17701(rnhB)
            PME: NATL1_02761(rnhA) NATL1_19431(rnhB)
            TER: Tery_0482 Tery_1584
            BTH: BT_3412
            BFR: BF0290
            BFS: BF0239(rnhB)
            PGI: PG0736(rnhB)
            SRU: SRU_2372(rnhB)
            CHU: CHU_2706(rnhA) CHU_2825(rnhB)
            GFO: GFO_2923(rnhB) GFO_3380(rnhA)
            FJO: Fjoh_1135 Fjoh_1923
            FPS: FP0198(rnhA) FP1200(rnhB)
            CTE: CT1612(rnhA) CT2261(rnhB)
            CCH: Cag_1744(rnhA) Cag_1993
            CPH: Cpha266_0038
            PVI: Cvib_0015
            PLT: Plut_0011 Plut_1607(rnhA)
            DET: DET0780(rnhB)
            DEH: cbdb_A756(rnhB)
            DEB: DehaBAV1_0706
            RRS: RoseRS_1014 RoseRS_2783
            RCA: Rcas_1189 Rcas_2563
            DRA: DR_0899 DR_1949
            DGE: Dgeo_1623 Dgeo_1969
            TTH: TTC1191 TTC1788
            TTJ: TTHA0198 TTHA1556
            AAE: aq_1768 aq_1955(rnhB)
            TMA: TM0915
            TPT: Tpet_0012
            TME: Tmel_1910
            FNO: Fnod_1335
            MJA: MJ0135
            MMP: MMP1374(RNase_HII)
            MMQ: MmarC5_0204
            MMZ: MmarC7_0619
            MAE: Maeo_0608
            MVN: Mevan_0684
            MAC: MA1959
            MBA: Mbar_A2753
            MMA: MM_2814(hhI)
            MBU: Mbur_0450
            MTP: Mthe_0780
            MHU: Mhun_1216
            MEM: Memar_0504
            MBN: Mboo_1943
            MTH: MTH1023
            MST: Msp_0551 Msp_1395(rnhB)
            MSI: Msm_0979
            MKA: MK0186(rnhB)
            AFU: AF0621(rnhB)
            HAL: VNG1984G(rnh)
            HMA: pNG7077(rnh) rrnAC3216(rnhB)
            HWA: HQ1228A(rnhA) HQ3096A(rnhB)
            NPH: NP2392A(rnhB)
            TAC: Ta1458
            TVO: TVN0133
            PTO: PTO1263
            PHO: PH1650
            PAB: PAB0352(rnhB)
            PFU: PF1781
            TKO: TK0805
            RCI: RCIX928(rnh)
            APE: APE_0496.1
            IHO: Igni_1437
            HBU: Hbut_0844
            SSO: SSO2384(rnhB)
            STO: ST0519
            SAI: Saci_0958
            MSE: Msed_0661
            PAI: PAE1216(rnhB)
            PIS: Pisl_1305
            PAS: Pars_0312
            TPE: Tpen_0899
            NEQ: NEQ063
STRUCTURES  PDB: 1EKE  1F21  1G15  1GOA  1GOB  1GOC  1I39  1I3A  1IO2  1JL1  
                 1JL2  1JXB  1KVA  1KVB  1KVC  1LAV  1LAW  1O1W  1Q94  1QHK  
                 1RBR  1RBS  1RBT  1RBU  1RBV  1RCH  1RDA  1RDB  1RDC  1RDD  
                 1RIL  1RNH  1TFR  1UAX  1WSE  1WSF  1WSG  1WSH  1WSI  1WSJ  
                 1X1P  1ZBF  1ZBI  1ZBL  2D0A  2D0B  2D0C  2DFE  2DFF  2DFH  
                 2E4L  2EHG  2ETJ  2G8F  2G8H  2G8I  2G8K  2G8U  2G8V  2G8W  
                 2HB5  2IHN  2RN2  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.26.4
            ExPASy - ENZYME nomenclature database: 3.1.26.4
            ExplorEnz - The Enzyme Database: 3.1.26.4
            ERGO genome analysis and discovery system: 3.1.26.4
            BRENDA, the Enzyme Database: 3.1.26.4
            CAS: 9050-76-4
///
ENTRY       EC 3.1.26.5                 Enzyme
NAME        ribonuclease P;
            RNase P
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from
            tRNA precursor
COMMENT     An RNA-containing enzyme, essential for tRNA processing; generates
            5'-termini or mature tRNA molecules.
REFERENCE   1  [PMID:1099089]
  AUTHORS   Bikoff EK, Gefter ML.
  TITLE     In vitro synthesis of transfer RNA. I. Purification of required
            components.
  JOURNAL   J. Biol. Chem. 250 (1975) 6240-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:1099090]
  AUTHORS   Bikoff EK, LaRue BF, Gefter ML.
  TITLE     In vitro synthesis of transfer RNA. II. Identification of required
            enzymatic activities.
  JOURNAL   J. Biol. Chem. 250 (1975) 6248-55.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4560501]
  AUTHORS   Robertson HD, Altman S, Smith JD.
  TITLE     Purification and properties of a specific Escherichia coli
            ribonuclease which cleaves a tyrosine transfer ribonucleic acid
            presursor.
  JOURNAL   J. Biol. Chem. 247 (1972) 5243-51.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01164  ribonuclease P
            KO: K03536  ribonuclease P protein component
            KO: K03537  ribonuclease P subunit P14
            KO: K03538  ribonuclease P subunit P29
            KO: K03539  ribonuclease P subunit Rpp30
            KO: K03540  ribonuclease P subunit RPR2
GENES       HSA: 10556(RPP30) 10557(RPP38) 10775(POP4) 10799(RPP40)
                 10940(POP1) 11102(RPP14) 79897(RPP21)
            PTR: 452309(POP5) 463608(POP7) 464303(POP1) 466016(RPP38)
                 466155(RPP30)
            MMU: 117109(Pop5) 208366(Rpp40) 54364(Rpp30) 66161(Pop4)
                 67053(Rpp14) 67676(Rpp21) 67724(Pop1)
            RNO: 117241(Pop5_predicted) 292831(Pop4) 361020(Rpp14_predicted)
            CFA: 474824(RPP21) 477515(POP5) 477763(RPP30) 478709(RPP40)
                 481978(POP1) 489832(POP7) 612732(POP4) 612771(RPP14)
            GGA: 415753(POP4) 416064(RPP14) 416973(POP5) 420876(RPP40)
                 423795(RPP30) 768362(POP4)
            XLA: 447458(MGC81617) 494740(LOC494740)
            XTR: 448235(MGC88946)
            DRE: 541421(pop5)
            SPU: 579025(LOC579025) 579142(LOC579142) 753068(LOC753068)
            DME: Dmel_CG11606(Rpp30) Dmel_CG14057 Dmel_CG33082
            CEL: C15C6.4
            ATH: AT1G25250(ATIDD16) AT5G59980
            OSA: 4335406 4351650
            CME: CMI187C CMM152C CMR143C
            SCE: YBR257W(POP4) YHR062C(RPP1) YIR015W(RPR2) YML091C(RPM2)
                 YNL221C(POP1)
            AGO: AGOS_AAL046C AGOS_AAR014C AGOS_ABL187C AGOS_ADL357C
                 AGOS_ADR362C AGOS_AFR610W
            PIC: PICST_34257(RPM2) PICST_59359(POP4) PICST_61322
                 PICST_83026(POP1) PICST_83666(POP5)
            CAL: CaO19.1029 CaO19.2404
            CGR: CAGL0D03740g CAGL0I06380g CAGL0I09152g CAGL0K05049g
                 CAGL0M11836g
            SPO: SPAC3A12.04c SPBC1105.16c SPBC1703.01c
            ANI: AN2437.2 AN8691.2
            AFM: AFUA_5G11150 AFUA_6G02270 AFUA_8G04820
            AOR: AO090005000665 AO090120000111
            UMA: UM01144.1 UM02526.1 UM03124.1 UM03277.1
            DDI: DDBDRAFT_0187984 DDBDRAFT_0188805 DDBDRAFT_0219669
                 DDB_0232069(drpp30) DDB_0233114(pop1)
            PFA: MAL13P1.153
            CPV: cgd3_800 cgd6_1040
            CHO: Chro.30109 Chro.60134
            TAN: TA06385 TA09545
            TPV: TP01_0916 TP01_1174
            TET: TTHERM_01005330
            EHI: 94.t00035
            ECO: b3704(rnpA)
            ECJ: JW3681(rnpA)
            ECE: Z5195(rnpA)
            ECS: ECs4639
            ECC: c4628(rnpA)
            ECI: UTI89_C4255(rnpA)
            ECP: ECP_3905
            ECV: APECO1_27542(rnpA)
            ECW: EcE24377A_4214(rnpA)
            ECX: EcHS_A3917(rnpA)
            STY: STY3939(rnpA)
            STT: t3679(rnpA)
            SPT: SPA3684(rnpA)
            SEC: SC3758(rnpA)
            STM: STM3840(rnpA)
            YPE: YPO4101(rnpA)
            YPK: y4115(rnpA)
            YPM: YP_4008(rnpA)
            YPA: YPA_4145
            YPN: YPN_3957
            YPS: YPTB3946(rnpA)
            YPI: YpsIP31758_4155(rnpA)
            SFL: SF3760(rnpA)
            SFX: S4011(rnpA)
            SFV: SFV_3808(rnpA)
            SSN: SSON_3654(rnpA)
            SBO: SBO_3673(rnpA)
            SDY: SDY_4186(rnpA)
            ECA: ECA4444(rnpA)
            PLU: plu4908(rnpA)
            BUC: BU014(rnpA)
            BAS: BUsg014(rnpA)
            BAB: bbp014(rnpA)
            BCC: BCc_006(rnpA)
            SGL: SG2431
            BFL: Bfl014(rnpA)
            BPN: BPEN_013(rnpA)
            HIN: HI0999(rnpA)
            HIT: NTHI1173(rnpA)
            HIP: CGSHiEE_06975(rnpA)
            HIQ: CGSHiGG_08595(rnpA)
            HDU: HD0752(rnpA)
            HSO: HS_0135(rnpA)
            PMU: PM1163(rnpA)
            MSU: MS0483(rnpA)
            APL: APL_1939(rnpA)
            XFA: XF2781
            XFT: PD2122(rnpA)
            XCC: XCC4241(rnpA)
            XCB: XC_4331
            XCV: XCV4486(rnpA)
            XAC: XAC4373(rnpA)
            XOO: XOO4637(rnpA)
            XOM: XOO_4371(XOO4371)
            VCH: VC0006
            VCO: VC0395_A2513(rnpA)
            VVU: VV1_1005
            VVY: VV0004
            VPA: VP0004
            VFI: VF0004
            PPR: PBPRA0004(rnpA)
            PAE: PA5569(rn)
            PAU: PA14_73420(rnpA)
            PAP: PSPA7_6370(rnpA)
            PPU: PP_0008(rnpA)
            PST: PSPTO_5614(rnpA)
            PSB: Psyr_5136
            PSP: PSPPH_5222(rnpA)
            PFO: Pfl_5745
            PEN: PSEEN5558(rnpA)
            PAR: Psyc_2146(rnpA)
            PCR: Pcryo_0001
            ACI: ACIAD3683(rnpA)
            SON: SO_0006(rnpA)
            SDN: Sden_3777
            SFR: Sfri_4065
            SAZ: Sama_0011
            SBL: Sbal_4382
            SLO: Shew_3868
            SHE: Shewmr4_3942
            SHM: Shewmr7_4034
            SHN: Shewana3_0008
            SHW: Sputw3181_4094
            ILO: IL2639(rnpA)
            CPS: CPS_5052(rnpA)
            PHA: PSHAa3025(rnpA)
            PAT: Patl_4314
            PIN: Ping_3609
            MAQ: Maqu_3897
            CBU: CBU_1918(rnpA)
            CBD: COXBU7E912_0203(rnpA)
            LPN: lpg3004(rnpA)
            LPF: lpl2932(rnpA)
            LPP: lpp3076(rnpA)
            MCA: MCA3035(rnpA)
            FTU: FTT0235c(rnpA)
            FTF: FTF0235c(rnpA)
            FTL: FTL_0176
            FTH: FTH_0170(rnpA)
            FTN: FTN_0075(rnpA)
            TCX: Tcr_2198
            NOC: Noc_3088
            AEH: Mlg_2883
            HCH: HCH_10034(rnpA)
            CSA: Csal_3317
            ABO: ABO_2754(rnpA)
            AHA: AHA_4283(rnpA)
            DNO: DNO_0951(rnpA)
            BCI: BCI_0134(rnpA)
            RMA: Rmag_1038
            VOK: COSY_0939(rnpA)
            NME: NMB1905
            NMA: NMA0550(rnpA)
            NMC: NMC0318(rnpA)
            NGO: NGO2181
            CVI: CV_4406(rnpA)
            RSO: RSc0002(rnpA)
            REU: Reut_A3462
            REH: H16_A3746
            RME: Rmet_3615
            BMA: BMA3399(rnpA)
            BMV: BMASAVP1_A2846(rnpA)
            BML: BMA10299_A2239(rnpA)
            BMN: BMA10247_3552(rnpA)
            BXE: Bxe_A4464
            BUR: Bcep18194_A6522
            BCN: Bcen_2551
            BCH: Bcen2424_3165
            BAM: Bamb_3217
            BPS: BPSL0076(rnpA)
            BPM: BURPS1710b_0302(rnpA)
            BPL: BURPS1106A_0105(rnpA)
            BPD: BURPS668_0091(rnpA)
            BTE: BTH_I3237
            BPE: BP0493(rnpA)
            BPA: BPP4403(rnpA)
            BBR: BB4991(rnpA)
            MPT: Mpe_A3827
            MMS: mma_3696(rnpA)
            NEU: NE0389(rnpA)
            NET: Neut_2152
            NMU: Nmul_A2778
            EBA: ebB90(rnpA)
            AZO: azo3991
            DAR: Daro_4203
            MFA: Mfla_2760
            HPY: HP1448(rnpA)
            HPJ: jhp1341(rnpA)
            HPA: HPAG1_1374
            HHE: HH0115(rnpA)
            HAC: Hac_0171(rnpA)
            TDN: Tmden_0522
            CJE: Cj0960c(rnpA)
            CJR: CJE1040(rnpA)
            CJJ: CJJ81176_0983(rnpA)
            CJU: C8J_0902(rnpA)
            CJD: JJD26997_0821(rnpA)
            CFF: CFF8240_0552(rnpA)
            CCV: CCV52592_1829
            CHA: CHAB381_0650
            SUN: SUN_1572
            PCA: Pcar_3145
            DVU: DVU1075(rnpA)
            DDE: Dde_2396
            LIP: LI1069(rnpA)
            BBA: Bd3913(rnpA)
            DPS: DP0854
            ADE: Adeh_4360
            MXA: MXAN_7511(rnpA)
            SAT: SYN_01012
            SFU: Sfum_2595
            RPR: RP611(rnpA)
            RTY: RT0599(rnpA)
            RCO: RC0937(rnpA)
            RFE: RF_0347(rnpA)
            RBE: RBE_0867(rnpA)
            RAK: A1C_04775(rnpA)
            RBO: A1I_02565(rnpA)
            RCM: A1E_01735(rnpA)
            RRI: A1G_05155(rnpA)
            OTS: OTBS_0256(rnpA)
            WBM: Wbm0692
            AMA: AM881
            APH: APH_0308(rnpA)
            ERU: Erum5800(rnpA)
            ERW: ERWE_CDS_06100
            ERG: ERGA_CDS_06010
            ECN: Ecaj_0584
            ECH: ECH_0439
            NSE: NSE_0857(rnpA)
            PUB: SAR11_0468
            MLO: mlr4810
            MES: Meso_0375
            SME: SMc01720(rnpA)
            ATU: Atu0385(rnpA)
            RET: RHE_CH00438(rnpA)
            RLE: RL0454
            BME: BMEII0276
            BMF: BAB2_0985(rnpA)
            BMS: BRA1022(rnpA)
            BMB: BruAb2_0962(rnpA)
            BOV: BOV_A0963(rnpA)
            BJA: blr8097(rnpA)
            BRA: BRADO0783(rnpA)
            BBT: BBta_7325(rnpA)
            RPA: RPA0633(rnpA)
            RPB: RPB_0684
            RPC: RPC_0818
            RPD: RPD_0068
            RPE: RPE_0643
            NWI: Nwi_3075
            NHA: Nham_3704
            BHE: BH12400(rnpA)
            BQU: BQ09770(rnpA)
            BBK: BARBAKC583_1047(rnpA)
            CCR: CC_0768
            SIL: SPO0537
            SIT: TM1040_0312
            RSP: RSP_1060(rnpA)
            JAN: Jann_0641
            RDE: RD1_1459(rnpA)
            HNE: HNE_0413(rnpA)
            ZMO: ZMO1625(rnpA)
            NAR: Saro_0576
            SAL: Sala_0006
            ELI: ELI_10645
            GOX: GOX1826
            GBE: GbCGDNIH1_0724
            RRU: Rru_A3337
            MAG: amb4354
            MGM: Mmc1_3759
            ABA: Acid345_0219
            BSU: BG10063(rnpA)
            BHA: BH4065(rnpA)
            BAN: BA5737(rnpA)
            BAR: GBAA5737(rnpA)
            BAA: BA_0594
            BAT: BAS5340
            BCE: BC5489
            BCA: BCE_5638(rnpA)
            BCZ: BCZK5184(rnpA)
            BTK: BT9727_5168(rnpA)
            BTL: BALH_4994(rnpA)
            BLI: BL00113(rnpA)
            BLD: BLi04378(rnpA)
            BCL: ABC4120(rnpA)
            BAY: RBAM_038150(rnpA)
            BPU: BPUM_3736(rnpA)
            OIH: OB3495(rnpA)
            GKA: GK3497(rnpA)
            SAU: SA2502(rnpA)
            SAV: SAV2713(rnpA)
            SAM: MW2631(rnpA)
            SAR: SAR2799(rnpA)
            SAS: SAS2595
            SAC: SACOL2739(rnpA)
            SAB: SAB2589c(rnpA)
            SAA: SAUSA300_2647(rnpA)
            SAO: SAOUHSC_03054
            SEP: SE2418
            SER: SERP0002(rnpA)
            SHA: SH2677(rnpA)
            SSP: SSP2445
            LMO: lmo2855(rnpA)
            LMF: LMOf2365_2845(rnpA)
            LIN: lin2987(rnpA)
            LWE: lwe2778(rnpA)
            LLA: L131443(rnpA)
            LLC: LACR_0129
            LLM: llmg_0142
            SPY: SPy_0246(rnpA)
            SPZ: M5005_Spy_0207(rnpA)
            SPM: spyM18_0228(rnpA)
            SPG: SpyM3_0175(rnpA)
            SPS: SPs0180
            SPH: MGAS10270_Spy0207(fasX)
            SPI: MGAS10750_Spy0202(fasX)
            SPJ: MGAS2096_Spy0222(fasX)
            SPK: MGAS9429_Spy0208(fasX)
            SPF: SpyM50187(rnpA)
            SPA: M6_Spy0238
            SPB: M28_Spy0201(rnpA)
            SPN: SP_2042
            SPR: spr1853(rnpA)
            SPD: SPD_1851(rnpA)
            SAG: SAG0408(rnpA)
            SAN: gbs0443
            SAK: SAK_0481(rnpA)
            SMU: SMU.336(rnpA)
            STC: str1811(rnpA)
            STL: stu1811(rnpA)
            STE: STER_1790
            SSA: SSA_2140(rnpA)
            SSU: SSU05_2015
            SSV: SSU98_2017
            SGO: SGO_0178(rnpA)
            LPL: lp_3688(rnpA)
            LJO: LJ1857
            LAC: LBA1978(rnpA)
            LSA: LSA1885(rnpA)
            LSL: LSL_1737(rnpA)
            LDB: Ldb2217(rnpA)
            LBU: LBUL_2038
            LBR: LVIS_2313
            LCA: LSEI_2908
            EFA: EF3332(rnpA)
            OOE: OEOE_1863
            STH: STH3340
            CAC: CAC3738(rnpA)
            CPE: CPE2659(rnpA)
            CPF: CPF_2996(rnpA)
            CPR: CPR_2673(rnpA)
            CNO: NT01CX_0869(rnpA)
            CDF: CD3679(rnpA)
            CBO: CBO3647(rnpA)
            CBA: CLB_3740(rnpA)
            CBH: CLC_3646(rnpA)
            CBF: CLI_3892(rnpA)
            CKL: CKL_3925(rnpA)
            CHY: CHY_0002(rnpA)
            DSY: DSY5059(rnpA)
            SWO: Swol_2576
            TTE: TTE2801(rnpA)
            MGE: MG_465(rnpA)
            MPN: MPN681(rnpA)
            MPU: MYPU_1530(rnpA)
            MPE: MYPE10410(rnpA)
            MGA: MGA_0630(rnpA)
            MMY: MSC_1067(rnpA)
            MMO: MMOB6310(rnpA)
            MHJ: MHJ_0675(rnpA)
            MHP: MHP7448_0677(rnpA)
            MSY: MS53_0600(rnpA)
            MCP: MCAP_0869(rnpA)
            UUR: UU603(rnpA)
            POY: PAM248(rnpA)
            AYW: AYWB_473(rnpA)
            MFL: Mfl682
            MTU: Rv3923c(rnpA)
            MTC: MT4041(rnpA)
            MBO: Mb3954c(rnpA)
            MBB: BCG_0029c(rnpA_2) BCG_3981c(rnpA_1)
            MLE: ML2712(rnpA)
            MPA: MAP4349c(rnpA)
            MAV: MAV_5312(rnpA)
            MSM: MSMEG_6945(rnpA)
            MMC: Mmcs_5412
            CGL: NCgl2992(rnpA)
            CGB: cg3431(rnpA)
            CEF: CE2946
            CDI: DIP2381(rnpA)
            CJK: jk2103(rnpA)
            NFA: nfa56720(rnpA)
            RHA: RHA1_ro03664
            SCO: SCO3881(rnpA)
            SMA: SAV4314(rnpA)
            TWH: TWT807
            TWS: TW817(rnpA)
            CMI: CMM_2977(rnpA)
            PAC: PPA2352
            TFU: Tfu_3116
            FRA: Francci3_4547
            FAL: FRAAL6883(rnpA)
            SEN: SACE_7396(rnpA)
            BLO: BL0642a(rnpA)
            BAD: BAD_1630(rnpA)
            RXY: Rxyl_3215
            FNU: FN0002
            RBA: RB7431(rnpA)
            CTR: CT784(rnpA)
            CTA: CTA_0854(rnpA)
            CMU: TC0167
            CPN: CPn0934(rnpA)
            CPA: CP0927
            CPJ: CPj0934(rnpA)
            CPT: CpB0967
            CCA: CCA00835(rnpA)
            CAB: CAB804
            CFE: CF0178(rnpA)
            BBU: BB0441(rnpA)
            BGA: BG0448(rnpA)
            BAF: BAPKO_0463(rnpA)
            TPA: TP0950a
            TDE: TDE2399(rnpA)
            SYN: slr1469(rnpA)
            SYW: SYNW1888(rnpA)
            SYC: syc0072_d(rnpA)
            SYF: Synpcc7942_1615
            SYD: Syncc9605_0579
            SYE: Syncc9902_1785
            SYG: sync_2097
            SYR: SynRCC307_0639
            SYX: SynWH7803_1899(rnpA)
            CYA: CYA_2904(rnpA)
            CYB: CYB_2941(rnpA)
            GVI: glr1475(rnpA)
            ANA: alr3413
            AVA: Ava_3433(rnpA)
            PMA: Pro1300(rnpA)
            PMM: PMM1184(rnpA)
            PMT: PMT1369(rnpA)
            PMN: PMN2A_0803
            PMI: PMT9312_1285
            PMB: A9601_13771(rnpA)
            PMC: P9515_13561(rnpA)
            PMF: P9303_06111(rnpA)
            PMG: P9301_13851(rnpA)
            PME: NATL1_16581(rnpA)
            TER: Tery_4708
            BTH: BT_3227
            BFR: BF0065
            BFS: BF0076
            PGI: PG0201(rnpA)
            CHU: CHU_0097(rnpA)
            GFO: GFO_3318(rnpA)
            FPS: FP2376(rnpA)
            CTE: CT0004
            CCH: Cag_2032(rnpA)
            PLT: Plut_2131(rnpA)
            DET: DET1042(rnpA)
            DEH: cbdb_A1017(rnpA)
            DRA: DR_2151
            DGE: Dgeo_1567
            TTH: TTC0077
            TTJ: TTHA0444 TTHA0445
            TMA: TM1463
            MJA: MJ0464 MJ0494 MJ0962 MJ1139
            MMP: MMP0430 MMP0921 MMP1407
            MMQ: MmarC5_1207
            MMZ: MmarC7_1427
            MAE: Maeo_1310
            MVN: Mevan_1415
            MAC: MA0290 MA1080 MA1781(rnpB) MA1782(rnpA)
            MBA: Mbar_A0102 Mbar_A1272 Mbar_A2501 Mbar_A2502
            MMA: MM_1556 MM_2132 MM_2618 MM_2619
            MBU: Mbur_0009 Mbur_0194 Mbur_0195 Mbur_1510
            MTP: Mthe_1366 Mthe_1720
            MHU: Mhun_2245 Mhun_2280 Mhun_3013
            MTH: MTH11 MTH1618 MTH687 MTH688
            MST: Msp_0592(rnp4) Msp_0900(rnp1) Msp_1245(rnp3) Msp_1246(rnp2)
            MSI: Msm_0246 Msm_0247 Msm_0711 Msm_0753
            MKA: MK0387(RPP30) MK0846(POP4_1) MK1216(POP4_2) MK1622(RPR2)
            AFU: AF0109 AF0489 AF1917 AF2317
            HAL: VNG0599C VNG1699C
            HMA: rrnAC1175(rpp14) rrnAC1177(rnp30)
            HWA: HQ1513A(rnp3) HQ1515A(rnp2) HQ2501A(rnp4) HQ2834A(rnpA)
            NPH: NP3726A(rnp3) NP3736A(rnp2) NP4480A(rnp4)
            TAC: Ta0176m Ta1263a(POP4)
            TVO: TVN0279 TVN0333
            PHO: PH1481 PH1601 PH1771 PH1877
            PAB: PAB0385 PAB0467 PAB1136 PAB2126
            PFU: PF1378 PF1613 PF1816 PF1914
            TKO: TK0031 TK1450 TK1533 TK1767
            RCI: RCIX2119(rnp3) RCIX2120(rnp2) RCIX2552(rnp1) RCIX609(rnp4)
            APE: APE_0362 APE_1092.1 APE_1450.1(rnp3)
            SSO: SSO2225
            STO: ST2130
            SAI: Saci_0033
STRUCTURES  PDB: 1A6F  1D6T  1NZ0  1OQK  1TS9  1TSF  1V76  1V77  1X0T  2AV5  
                 2CZV  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.26.5
            ExPASy - ENZYME nomenclature database: 3.1.26.5
            ExplorEnz - The Enzyme Database: 3.1.26.5
            ERGO genome analysis and discovery system: 3.1.26.5
            BRENDA, the Enzyme Database: 3.1.26.5
///
ENTRY       EC 3.1.26.6                 Enzyme
NAME        ribonuclease IV;
            endoribonuclease IV;
            poly(A)-specific ribonuclease
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage of poly(A) to fragments terminated by
            3'-hydroxy and 5'-phosphate groups
COMMENT     Forms oligonucleotides with an average chain length of 10.
REFERENCE   1  [PMID:1009928]
  AUTHORS   Muller WE.
  TITLE     Endoribonuclease IV. A poly(A)-specific ribonuclease from chick
            oviduct. 1. Purification of the enzyme.
  JOURNAL   Eur. J. Biochem. 70 (1976) 241-8.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:1009929]
  AUTHORS   Muller WE, Seibert G, Steffen R, Zahn RK.
  TITLE     Endoribonuclease IV. 2. Further investigation on the specificity.
  JOURNAL   Eur. J. Biochem. 70 (1976) 249-58.
  ORGANISM  Coturnix japonica
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.26.6
            ExPASy - ENZYME nomenclature database: 3.1.26.6
            ExplorEnz - The Enzyme Database: 3.1.26.6
            ERGO genome analysis and discovery system: 3.1.26.6
            BRENDA, the Enzyme Database: 3.1.26.6
            CAS: 61536-76-3
///
ENTRY       EC 3.1.26.7                 Enzyme
NAME        ribonuclease P4
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage of RNA, removing 3'-extranucleotides from
            tRNA precursor
REFERENCE   1  [PMID:109442]
  AUTHORS   Sekiya T, Contreras R, Takeya T, Khorana HG.
  TITLE     Total synthesis of a tyrosine suppressor transfer RNA gene. XVII.
            Transcription, in vitro, of the synthetic gene and processing of the
            primary transcript to transfer RNA.
  JOURNAL   J. Biol. Chem. 254 (1979) 5802-16.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.26.7
            ExPASy - ENZYME nomenclature database: 3.1.26.7
            ExplorEnz - The Enzyme Database: 3.1.26.7
            ERGO genome analysis and discovery system: 3.1.26.7
            BRENDA, the Enzyme Database: 3.1.26.7
///
ENTRY       EC 3.1.26.8                 Enzyme
NAME        ribonuclease M5;
            RNase M5;
            5S ribosomal maturation nuclease;
            5S ribosomal RNA maturation endonuclease
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage of RNA, removing 21 and 42 nucleotides,
            respectively, from the 5'- and 3'-termini of a 5S-rRNA precursor
COMMENT     Converts the 5S-rRNA precursor from Bacillus subtilis into 5S-rRNA,
            with 5'-phosphate and 3'-hydroxy groups.
REFERENCE   1  [PMID:402365]
  AUTHORS   Sogin ML, Pace B, Pace NR.
  TITLE     Partial purification and properties of a ribosomal RNA maturation
            endonuclease from Bacillus subtilis.
  JOURNAL   J. Biol. Chem. 252 (1977) 1350-7.
  ORGANISM  Bacillus subtilis [GN:bsu]
ORTHOLOGY   KO: K05985  ribonuclease M5
GENES       BSU: BG10104(rnmV)
            BHA: BH0056
            BAN: BA0038
            BAR: GBAA0038
            BAA: BA_0628
            BAT: BAS0039
            BCE: BC0045
            BCA: BCE_0038
            BCZ: BCZK0036(rnmV)
            BTK: BT9727_0036(rnmV)
            BTL: BALH_0036(rnmV)
            BLI: BL00530(rnmV)
            BCL: ABC0069(rnmV)
            BPU: BPUM_0025(rnmV)
            OIH: OB0049
            SAU: SA0450
            SAV: SAV0492
            SAM: MW0447
            SAR: SAR0493
            SAS: SAS0449
            SAB: SAB0441
            SAA: SAUSA300_0469
            SAO: SAOUHSC_00463
            SEP: SE2291
            SHA: SH2519
            SSP: SSP2264
            LMO: lmo0187
            LMF: LMOf2365_0198
            LIN: lin0226
            LLA: L88730(ygiK)
            LLC: LACR_0717
            LLM: llmg_1883
            SPY: SPy_0261
            SPZ: M5005_Spy_0221
            SPM: spyM18_0244
            SPG: SpyM3_0189
            SPS: SPs0194
            SPH: MGAS10270_Spy0221
            SPI: MGAS10750_Spy0216
            SPJ: MGAS2096_Spy0239
            SPK: MGAS9429_Spy0222
            SPF: SpyM50200
            SPA: M6_Spy0253
            SPB: M28_Spy0215
            SPN: SP_1990
            SPR: spr1804
            SPD: SPD_1787
            SAG: SAG1781
            SAN: gbs1824
            SAK: SAK_1803
            SMU: SMU.342
            STC: str1800
            STL: stu1800
            STE: STER_1773
            SSA: SSA_2125
            SSU: SSU05_2010
            SSV: SSU98_2012
            LPL: lp_0457
            LJO: LJ0204
            LAC: LBA0215
            LSA: LSA1656
            LSL: LSL_0228 LSL_1398
            LDB: Ldb0344
            LBU: LBUL_0299
            LBR: LVIS_0457
            LCA: LSEI_2594
            LGA: LGAS_0207
            PPE: PEPE_0268
            EFA: EF0935
            OOE: OEOE_1550
            LME: LEUM_1614
            CAC: CAC2987
            CPE: CPE2518
            CTC: CTC00246
            DSY: DSY0134
            MGE: MG_057
            MPE: MYPE9440
            MGA: MGA_0346
            MMY: MSC_0003
            MCP: MCAP_0003
            UUR: UU194
            MFL: Mfl004
            FNU: FN0039
            BBU: BB0626
            BGA: BG0646
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.26.8
            ExPASy - ENZYME nomenclature database: 3.1.26.8
            ExplorEnz - The Enzyme Database: 3.1.26.8
            ERGO genome analysis and discovery system: 3.1.26.8
            BRENDA, the Enzyme Database: 3.1.26.8
            CAS: 62253-00-3
///
ENTRY       EC 3.1.26.9                 Enzyme
NAME        ribonuclease [poly-(U)-specific];
            ribonuclease (uracil-specific);
            uracil-specific endoribonuclease;
            uracil-specific RNase
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage of poly(U) to fragments terminated by
            3'-hydroxy and 5'-phosphate groups
COMMENT     Forms oligonucleotides with chain lengths of 6 to 12.
REFERENCE   1  [PMID:6227485]
  AUTHORS   Bachmann M, Trautmann F, Messer R, Zahn RK, Meyer zum Buschenfelde
            KH, Muller WE.
  TITLE     Association of a polyuridylate-specific endoribonuclease with small
            nuclear ribonucleo-proteins which had been isolated by affinity
            chromatography using antibodies from a patient with systemic lupus
            erythematosus.
  JOURNAL   Eur. J. Biochem. 136 (1983) 447-51.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.26.9
            ExPASy - ENZYME nomenclature database: 3.1.26.9
            ExplorEnz - The Enzyme Database: 3.1.26.9
            ERGO genome analysis and discovery system: 3.1.26.9
            BRENDA, the Enzyme Database: 3.1.26.9
///
ENTRY       EC 3.1.26.10                Enzyme
NAME        ribonuclease IX;
            poly(U)- and poly(C)-specific endoribonuclease
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage of poly(U) or poly(C) to fragments
            terminated by 3'-hydroxy and 5'-phosphate groups
COMMENT     Acts on poly(U) and poly(C), with a higher affinity for poly(C), but
            does not act on poly(A) or poly(G).
REFERENCE   1  [PMID:3569265]
  AUTHORS   Sideris DC, Fragoulis EG.
  TITLE     Purification and characterization of a ribonuclease specific for
            poly(U) and poly(C) from the larvae of Ceratitis capitata.
  JOURNAL   Eur. J. Biochem. 164 (1987) 309-15.
  ORGANISM  Ceratitis capitata
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.26.10
            ExPASy - ENZYME nomenclature database: 3.1.26.10
            ExplorEnz - The Enzyme Database: 3.1.26.10
            ERGO genome analysis and discovery system: 3.1.26.10
            BRENDA, the Enzyme Database: 3.1.26.10
            CAS: 9001-99-4
///
ENTRY       EC 3.1.26.11                Enzyme
NAME        tRNase Z;
            3 tRNase;
            tRNA 3 endonuclease;
            RNase Z;
            3' tRNase
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 5'-phosphomonoesters
REACTION    endonucleolytic cleavage of RNA, removing extra 3' nucleotides from
            tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group
            is left at the tRNA terminus and a 5'-phosphoryl group is left at
            the trailer molecule
COMMENT     No cofactor requirements. An homologous enzyme to that found in
            Arabidopsis thaliana has been found in Methanococcus janaschii.
REFERENCE   1  [PMID:12032089]
  AUTHORS   Schiffer S, Rosch S, Marchfelder A.
  TITLE     Assigning a function to a conserved group of proteins: the tRNA
            3'-processing enzymes.
  JOURNAL   EMBO. J. 21 (2002) 2769-77.
  ORGANISM  Arabidopsis thaliana [GN:ath], Methano coccus janaschii
REFERENCE   2  [PMID:10684660]
  AUTHORS   Mayer M, Schiffer S, Marchfelder A.
  TITLE     tRNA 3' processing in plants: nuclear and mitochondrial activities
            differ.
  JOURNAL   Biochemistry. 39 (2000) 2096-105.
  ORGANISM  Solanum tuberosum [GN:estu], Triticum aestivum [GN:etae]
REFERENCE   3  [PMID:11444972]
  AUTHORS   Schiffer S, Helm M, Theobald-Dietrich A, Giege R, Marchfelder A.
  TITLE     The plant tRNA 3' processing enzyme has a broad substrate spectrum.
  JOURNAL   Biochemistry. 40 (2001) 8264-72.
  ORGANISM  Solanum tuberosum [GN:estu], Triticum aestivum [GN:etae]
REFERENCE   4  [PMID:9419337]
  AUTHORS   Kunzmann A, Brennicke A, Marchfelder A.
  TITLE     5' end maturation and RNA editing have to precede tRNA 3' processing
            in plant mitochondria.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 108-13.
  ORGANISM  Solanum tuberosum [GN:estu]
REFERENCE   5  [PMID:11252717]
  AUTHORS   Morl M, Marchfelder A.
  TITLE     The final cut. The importance of tRNA 3'-processing.
  JOURNAL   EMBO. Rep. 2 (2001) 17-20.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], rat [GN:rno], human [GN:hsa]
REFERENCE   6  [PMID:14749326]
  AUTHORS   Minagawa A, Takaku H, Takagi M, Nashimoto M.
  TITLE     A novel endonucleolytic mechanism to generate the CCA 3' termini of
            tRNA molecules in Thermotoga maritima.
  JOURNAL   J. Biol. Chem. 279 (2004) 15688-97.
  ORGANISM  Thermotoga maritima [GN:tma]
REFERENCE   7  [PMID:12711671]
  AUTHORS   Takaku H, Minagawa A, Takagi M, Nashimoto M.
  TITLE     A candidate prostate cancer susceptibility gene encodes tRNA 3'
            processing endoribonuclease.
  JOURNAL   Nucleic. Acids. Res. 31 (2003) 2272-8.
  ORGANISM  pig [GN:ssc], human [GN:hsa]
ORTHOLOGY   KO: K00784  ribonuclease Z
GENES       HSA: 55520(ELAC1) 60528(ELAC2)
            PTR: 450109(ELAC2)
            MMU: 114615(Elac1) 68626(Elac2)
            RNO: 282826(Elac2)
            CFA: 476197(ELAC1) 489511(ELAC2)
            GGA: 417313(ELAC2)
            SPU: 578654(LOC578654) 583893(LOC583893)
            DME: Dmel_CG3298(JhI-1)
            ATH: AT3G16260
            CME: CMO192C
            SCE: YKR079C(TRZ1)
            AGO: AGOS_ADR212C
            PIC: PICST_65151
            CAL: CaO19_5425(CaO19.5425)
            CGR: CAGL0G02167g
            SPO: SPAC1D4.10
            AFM: AFUA_1G16470
            AOR: AO090005001063
            UMA: UM03648.1
            DDI: DDBDRAFT_0189002 DDBDRAFT_0202976
            PFA: PF14_0620
            CHO: Chro.70186
            TET: TTHERM_00721700 TTHERM_01125320 TTHERM_01412060
            EHI: 22.t00045
            ECO: b2268(elaC)
            ECJ: JW2263(elaC)
            ECE: Z3528(elaC)
            ECS: ECs3156
            ECC: c2812(elaC)
            ECI: UTI89_C2552(elaC)
            ECP: ECP_2312
            ECV: APECO1_4293(elaC)
            ECW: EcE24377A_2565(rnz)
            ECX: EcHS_A2414(rnz)
            STY: STY2544
            STT: t0550
            SPT: SPA0550(elaC)
            SEC: SC2313(elaC)
            STM: STM2313(elaC)
            SFL: SF2347(elaC)
            SFX: S2481(elaC)
            SFV: SFV_2339(elaC)
            SSN: SSON_2329(elaC)
            SBO: SBO_2305(elaC)
            SDY: SDY_2464(elaC)
            ENT: Ent638_2818
            PPU: PP_4033
            PPF: Pput_1805
            PEN: PSEEN2683
            PCR: Pcryo_1720
            PRW: PsycPRwf_1808
            MAQ: Maqu_2169
            AHA: AHA_1197
            SUN: SUN_1447
            ADE: Adeh_0401
            AFW: Anae109_4169
            MXA: MXAN_0663(rnz)
            SFU: Sfum_0439
            RET: RHE_PE00054
            RLE: pRL110071
            BJA: blr3882
            BRA: BRADO1465
            BBT: BBta_2705 BBta_3742
            BSU: BG11740(yqjK)
            BHA: BH1713
            BAN: BA4364
            BAR: GBAA4364
            BAA: BA_4820
            BAT: BAS4049
            BCE: BC4138
            BCA: BCE_4210
            BCZ: BCZK3895
            BTK: BT9727_3887
            BLI: BL05258(rnz)
            BLD: BLi02554(yqjK)
            BCL: ABC2047
            BAY: RBAM_022150(rnz)
            BPU: BPUM_2115(rnz)
            OIH: OB1856
            GKA: GK2333
            SAU: SA1335
            SAV: SAV1504
            SAM: MW1458
            SAR: SAR1581
            SAS: SAS1444
            SAC: SACOL1548
            SAB: SAB1365c
            SAA: SAUSA300_1453
            SAO: SAOUHSC_01598
            SAJ: SaurJH9_1561
            SAH: SaurJH1_1592
            SEP: SE1187
            SER: SERP1066
            SHA: SH1412
            SSP: SSP1249
            LMO: lmo1977
            LMF: LMOf2365_2000
            LIN: lin2084
            LWE: lwe1996
            LLA: L18686(ygbG)
            LLC: LACR_0654
            LLM: llmg_0412(vicX) llmg_0604
            SPY: SPy_0924
            SPZ: M5005_Spy_0725(elaC)
            SPM: spyM18_0981
            SPG: SpyM3_0637
            SPS: SPs1215
            SPH: MGAS10270_Spy0784(elaC)
            SPI: MGAS10750_Spy0819(elaC)
            SPJ: MGAS2096_Spy0797(elaC)
            SPK: MGAS9429_Spy0782(elaC)
            SPF: SpyM51082(rnz)
            SPA: M6_Spy0751
            SPB: M28_Spy0705(elaC)
            SPN: SP_0674
            SPR: spr0591
            SPD: SPD_0586(rnz)
            SAG: SAG1210
            SAN: gbs1282
            SAK: SAK_1296(rnz)
            SMU: SMU.1474c
            STC: str1226(elaC)
            STL: stu1226(elaC)
            SSA: SSA_1430(elaC)
            LPL: lp_2090
            LJO: LJ1073
            LAC: LBA0949
            LSA: LSA1043(rnz)
            LSL: LSL_1093
            LDB: Ldb0820
            LBU: LBUL_0749
            LBR: LVIS_1379
            LCA: LSEI_1353
            EFA: EF1691
            OOE: OEOE_1071
            CAC: CAC1584
            CPE: CPE1363
            CPF: CPF_1613(rnz)
            CPR: CPR_1360(rnz)
            CTC: CTC02190
            CDF: CD2539(elaC)
            CBA: CLB_1400(rnz)
            CBH: CLC_1411(rnz)
            CBF: CLI_1472(rnz)
            CBE: Cbei_1740
            CKL: CKL_2411(rnz)
            MAV: MAV_1774
            MSM: MSMEG_1776 MSMEG_4568
            MVA: Mvan_5799
            NFA: nfa48890
            SCO: SCO2547(SCC77.14c)
            SMA: SAV5576
            ART: Arth_2340
            TFU: Tfu_1526
            KRA: Krad_4220
            STP: Strop_0914
            CTR: CT346(elaC)
            CTA: CTA_0375(elaC)
            CMU: TC0625
            CPN: CPn0025(atsA)
            CPA: CP0751
            CPJ: CPj0025(atsA)
            CPT: CpB0029
            CCA: CCA00317
            CAB: CAB313
            CFE: CF0686(atsA)
            PCU: pc0459(elaC)
            BBU: BB0755
            BGA: BG0777
            BAF: BAPKO_0800
            TPA: TP0819
            TDE: TDE1951
            SYN: slr0050(ycf56)
            SYW: SYNW0538
            SYC: syc2084_d(ycf56)
            SYF: Synpcc7942_2011
            SYD: Syncc9605_2145
            SYE: Syncc9902_0532
            SYG: sync_2249
            SYR: SynRCC307_1839(rnz)
            SYX: SynWH7803_1976(rnz)
            CYA: CYA_1654(rnz)
            CYB: CYB_1636(rnz)
            TEL: tll0915(ycf56)
            GVI: glr4119(ycf56)
            ANA: alr5152
            AVA: Ava_2117 Ava_2403
            PMA: Pro1430(elaC)
            PMM: PMM1349
            PMT: PMT1426
            PMN: PMN2A_0920
            PMI: PMT9312_1447
            PMB: A9601_15501(elaC)
            PMC: P9515_15101(elaC)
            PMF: P9303_05331(elaC)
            PMG: P9301_15351(elaC)
            PMH: P9215_15781(elaC)
            PME: NATL1_17761(elaC)
            TER: Tery_0641
            BTH: BT_4346
            BFR: BF1044
            BFS: BF0960
            PGI: PG0739
            SRU: SRU_2164(rnz)
            CHU: CHU_1914
            FJO: Fjoh_4543
            FPS: FP1705(rnz)
            DRA: DR_0270
            DGE: Dgeo_1607
            MJA: MJ1502
            MMP: MMP0906
            MMQ: MmarC5_0713
            MMZ: MmarC7_0153
            MAE: Maeo_0727
            MVN: Mevan_0015
            MAC: MA3031
            MBA: Mbar_A1789
            MMA: MM_0306
            MBU: Mbur_2102
            MTP: Mthe_0927
            MHU: Mhun_1716
            MEM: Memar_1554
            MBN: Mboo_1591
            MTH: MTH1831
            MST: Msp_0411(rnz)
            MKA: MK1033
            AFU: AF0939
            HAL: VNG2239C
            HMA: rrnAC2500
            HWA: HQ2036A(elaC) HQ2927A(elaC) HQ3403A(elaC)
            NPH: NP2254A
            TAC: Ta1155
            TVO: TVN1230
            PTO: PTO1273
            PHO: PH1151
            PAB: PAB0728
            PFU: PF1345
            TKO: TK1114
            RCI: RCIX719(rnz)
            APE: APE_1836.1
            SMR: Smar_1236
            IHO: Igni_1037
            HBU: Hbut_0223
            SSO: SSO1043
            STO: ST0948
            SAI: Saci_1284
            PAI: PAE3218
            PAS: Pars_1383
            NEQ: NEQ064
STRUCTURES  PDB: 1WW1  1Y44  2CBN  2E7Y  2FK6  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.26.11
            ExPASy - ENZYME nomenclature database: 3.1.26.11
            ExplorEnz - The Enzyme Database: 3.1.26.11
            ERGO genome analysis and discovery system: 3.1.26.11
            BRENDA, the Enzyme Database: 3.1.26.11
            CAS: 98148-84-6
///
ENTRY       EC 3.1.27.1                 Enzyme
NAME        ribonuclease T2;
            ribonuclease II;
            base-non-specific ribonuclease;
            nonbase-specific RNase;
            RNase (non-base specific);
            non-base specific ribonuclease;
            nonspecific RNase;
            RNase Ms;
            RNase M;
            RNase II;
            Escherichia coli ribonuclease II;
            ribonucleate nucleotido-2'-transferase (cyclizing);
            acid ribonuclease;
            RNAase CL;
            Escherichia coli ribonuclease I' ribonuclease PP2;
            ribonuclease N2;
            ribonuclease M;
            acid RNase;
            ribonnuclease (non-base specific);
            ribonuclease (non-base specific);
            RNase T2;
            ribonuclease PP3;
            ribonucleate 3'-oligonucleotide hydrolase;
            RNase II;
            ribonuclease U4
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 3'-phosphomonoesters
REACTION    Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and
            3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
REFERENCE   1  [PMID:3732273]
  AUTHORS   Garcia-Segura JM, Orozco MM, Fominaya JM, Gavilanes JG.
  TITLE     Purification, molecular and enzymic characterization of an acid
            RNase from the insect Ceratitis capitata.
  JOURNAL   Eur. J. Biochem. 158 (1986) 367-72.
  ORGANISM  Ceratitis capitata
REFERENCE   2
  AUTHORS   Heppel, L.A.
  TITLE     Pig liver nuclei ribonuclease.
  JOURNAL   In: Cantoni, G.L. and Davies, D.R. (Eds.), Procedures in Nucleic
            Acid Research, Procedures in Nucleic Acid Research, New York, 1966,
            p. 31-36.
REFERENCE   3
  AUTHORS   Reddi, K.K. and Mauser, L.J.
  TITLE     Studies on the formation of tobacco mosaic virus ribonucleic acid.
            VI. Mode of degradation of host ribonucleic acid to ribonucleosides
            and their conversion to ribonucleoside 5'-phosphates.
  JOURNAL   Proc. Natl. Acad. Sci. USA 53 (1965) 607-613.
  ORGANISM  Nicotiana tabacum
REFERENCE   4  [PMID:6048969]
  AUTHORS   Uchida T, Egami F.
  TITLE     The specificity of ribonuclease T2.
  JOURNAL   J. Biochem. (Tokyo). 61 (1967) 44-53.
  ORGANISM  Aspergillus oryzae [GN:aor]
ORTHOLOGY   KO: K01166  ribonuclease T2
GENES       SPU: 589920(LOC589920)
            ATH: AT1G14220 AT2G39780(RNS2)
            OSA: 4325103 4345656
            SCE: YPL123C(RNY1)
            AGO: AGOS_ACR156W
            KLA: KLLA0D06567g
            DHA: DEHA0G21208g
            CAL: CaO19_11408(CaO19.11408)
            CGR: CAGL0J06820g
            ANI: AN4874.2
            AFM: AFUA_3G11220
            AOR: AO090005001044
            UMA: UM03023.1
            DDI: DDB_0230141(ddiA)
            TET: TTHERM_00125450 TTHERM_00222300 TTHERM_00264790
                 TTHERM_00784550
            EHI: 346.t00008
            NIS: NIS_1545
            BRA: BRADO6051
            BBT: BBta_1732
            RPE: RPE_1409
            NWI: Nwi_2529
            NHA: Nham_3150
            RSP: RSP_0715
STRUCTURES  PDB: 1BK7  1BOL  1DIX  1IQQ  1J1F  1J1G  1UCA  1UCC  1UCD  1UCG  
                 1V9H  1VCZ  1VD1  1VD3  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.27.1
            ExPASy - ENZYME nomenclature database: 3.1.27.1
            ExplorEnz - The Enzyme Database: 3.1.27.1
            ERGO genome analysis and discovery system: 3.1.27.1
            BRENDA, the Enzyme Database: 3.1.27.1
            CAS: 37278-25-4
///
ENTRY       EC 3.1.27.2                 Enzyme
NAME        Bacillus subtilis ribonuclease;
            Proteus mirabilis RNase;
            ribonucleate nucleotido-2'-transferase (cyclizing)
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 3'-phosphomonoesters
REACTION    Endonucleolytic cleavage to 2',3'-cyclic nucleotides
REFERENCE   1
  AUTHORS   Nishimura, H. and Maruo, B.
  TITLE     Intracellular ribonuclease from Bacillus subtilis.
  JOURNAL   Biochim. Biophys. Acta 40 (1960) 355-357.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   2  [PMID:4962137]
  AUTHORS   Yamasaki M, Arima K.
  TITLE     Regulation of intracellular ribonuclease of Bacillus subtilis by ATP
            and ADP.
  JOURNAL   Biochim. Biophys. Acta. 139 (1967) 202-4.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   3  [PMID:4981632]
  AUTHORS   Yamasaki M, Arima K.
  TITLE     Intracellular ribonuclease of Bacillus subtilis; specific inhibition
            by ATP and dATP.
  JOURNAL   Biochem. Biophys. Res. Commun. 37 (1969) 430-6.
  ORGANISM  Bacillus subtilis [GN:bsu]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.27.2
            ExPASy - ENZYME nomenclature database: 3.1.27.2
            ExplorEnz - The Enzyme Database: 3.1.27.2
            ERGO genome analysis and discovery system: 3.1.27.2
            BRENDA, the Enzyme Database: 3.1.27.2
///
ENTRY       EC 3.1.27.3                 Enzyme
NAME        ribonuclease T1;
            guanyloribonuclease;
            Aspergillus oryzae ribonuclease;
            RNase N1;
            RNase N2;
            ribonuclease N3;
            ribonuclease U1;
            ribonuclease F1;
            ribonuclease Ch;
            ribonuclease PP1;
            ribonuclease SA;
            RNase F1;
            ribonuclease C2;
            binase;
            RNase Sa;
            guanyl-specific RNase;
            RNase G;
            RNase T1;
            ribonuclease guaninenucleotido-2'-transferase (cyclizing);
            ribonuclease N3;
            ribonuclease N1
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 3'-phosphomonoesters
REACTION    Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and
            3'-phosphooligonucleotides ending in Gp with 2',3'-cyclic phosphate
            intermediates
COMMENT     Formerly EC 2.7.7.26 and EC 3.1.4.8.
REFERENCE   1  [PMID:5348588]
  AUTHORS   Kasai K, Uchida T, Egami F, Yoshida K, Nomoto M.
  TITLE     Purification and crystallization of ribonuclease N1 from Neurospora
            crassa.
  JOURNAL   J. Biochem. (Tokyo). 66 (1969) 389-96.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2
  AUTHORS   Takahashi, K.
  TITLE     The structure and function of ribonuclease T1. I. Chromatographic
            purification and properties of ribonuclease T1.
  JOURNAL   J. Biochem. (Tokyo) 49 (1961) 1-8.
ORTHOLOGY   KO: K01167  ribonuclease T1
GENES       AFM: AFUA_4G03230
            RSO: RSc2766(RS00088)
            RME: Rmet_2986
            BMA: BMA2476
            BMV: BMASAVP1_A0395
            BML: BMA10299_A1255
            BMN: BMA10247_3310
            BXE: Bxe_A0559
            BUR: Bcep18194_A3714
            BCN: Bcen_0149
            BCH: Bcen2424_0632
            BAM: Bamb_0533
            BPS: BPSL2958
            BPM: BURPS1710b_3473
            BPL: BURPS1106A_3475
            BPD: BURPS668_3438
            BTE: BTH_I1190
            HAR: HEAR2477
            MMS: mma_2572
            PAC: PPA0730
            SEN: SACE_6105
STRUCTURES  PDB: 1AY7  1B20  1B21  1B27  1B2M  1B2S  1B2U  1B2X  1B2Z  1B3S  
                 1BIR  1BOX  1BU4  1BVI  1C54  1CH0  1DET  1FUS  1FUT  1FYS  
                 1FZU  1G02  1GMP  1GMQ  1GMR  1GOU  1GOV  1GOY  1GSP  1HYF  
                 1HZ1  1I0V  1I0X  1I2E  1I2F  1I2G  1I3F  1I3I  1I70  1I8V  
                 1IYY  1LNI  1LOV  1LOW  1LOY  1LRA  1MGR  1MGW  1Q9E  1RCK  
                 1RCL  1RDS  1RGA  1RGC  1RGE  1RGF  1RGG  1RGH  1RGK  1RGL  
                 1RHL  1RLS  1RN1  1RN4  1RNT  1RSN  1T2H  1T2I  1TRP  1TRQ  
                 1TTO  1UCI  1UCJ  1UCK  1UCL  1YGW  1YNV  1ZGX  2AAD  2AAE  
                 2BU4  2C4B  2GSP  2HOH  2RNT  3BIR  3BU4  3GSP  3HOH  3RNT  
                 4BIR  4BU4  4GSP  4HOH  4RNT  5BIR  5BU4  5GSP  5HOH  5RNT  
                 6GSP  6RNT  7GSP  7RNT  8RNT  9RNT  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.27.3
            ExPASy - ENZYME nomenclature database: 3.1.27.3
            ExplorEnz - The Enzyme Database: 3.1.27.3
            ERGO genome analysis and discovery system: 3.1.27.3
            BRENDA, the Enzyme Database: 3.1.27.3
            CAS: 9026-12-4
///
ENTRY       EC 3.1.27.4                 Enzyme
NAME        ribonuclease U2;
            purine specific endoribonuclease;
            ribonuclease U3;
            RNase U3;
            RNase U2;
            purine-specific ribonuclease;
            purine-specific RNase;
            Pleospora RNase;
            Trichoderma koningi RNase III;
            ribonuclease (purine)
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 3'-phosphomonoesters
REACTION    Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and
            3'-phosphooligonucleotides ending in Ap or Gp with 2',3'-cyclic
            phosphate intermediates
REFERENCE   1
  AUTHORS   Glitz, D.G. and Dekker, C.A.
  TITLE     Studies on a ribonuclease from Ustilago sphaerogena. I. Purification
            and properties of the enzyme.
  JOURNAL   Biochemistry 3 (1964) 1391-1399.
  ORGANISM  Ustilago sphaerogena
REFERENCE   2
  AUTHORS   Glitz, D.G. and Dekker, C.A.
  TITLE     Studies on a ribonuclease from Ustilago sphaerogena. II. Specificity
            of the enzyme.
  JOURNAL   Biochemistry 3 (1964) 1399-1406.
  ORGANISM  Ustilago sphaerogena
REFERENCE   3
  AUTHORS   Uchida, T. and Egami, F. Microbial ribonucleases with special
            reference to RNases T1, T 2, N
  TITLE     1, and U2.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 4, Academic Press,
            New York, 1971, p. 205-250.
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.27.4
            ExPASy - ENZYME nomenclature database: 3.1.27.4
            ExplorEnz - The Enzyme Database: 3.1.27.4
            ERGO genome analysis and discovery system: 3.1.27.4
            BRENDA, the Enzyme Database: 3.1.27.4
            CAS: 37205-57-5
///
ENTRY       EC 3.1.27.5                 Enzyme
NAME        pancreatic ribonuclease;
            RNase;
            RNase I;
            RNase A;
            pancreatic RNase;
            ribonuclease I;
            endoribonuclease I;
            ribonucleic phosphatase;
            alkaline ribonuclease;
            ribonuclease;
            gene S glycoproteins;
            Ceratitis capitata alkaline ribonuclease;
            SLSG glycoproteins;
            gene S locus-specific glycoproteins;
            S-genotype-asssocd. glycoproteins;
            ribonucleate 3'-pyrimidino-oligonucleotidohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 3'-phosphomonoesters
REACTION    Endonucleolytic cleavage to nucleoside 3'-phosphates and
            3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic
            phosphate intermediates
REFERENCE   1
  AUTHORS   Anfinsen, C.B. and White, F.H., Jr.
  TITLE     The ribonucleases: occurrence, structure, and properties.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 5, Academic Press, New York, 1961, p. 95-122.
REFERENCE   2  [PMID:14247667]
  AUTHORS   BEARD JR, RAZZELL WE.
  TITLE     PURIFICATION OF ALKALINE RIBONUCLEASE II FROM MITOCHONDRIAL AND
            SOLUBLE FRACTIONS OF LIVER.
  JOURNAL   J. Biol. Chem. 239 (1964) 4186-93.
  ORGANISM  pig [GN:ssc], rat [GN:rno], cow [GN:bta]
REFERENCE   3
  AUTHORS   Cannistraro, V.J. and Kennell, D.
  TITLE     Purification and characterization of ribonuclease M and mRNA
            degradation in Escherichia coli.
  JOURNAL   Int. J. Biochem. 181 (1989) 363-370.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01168  pancreatic ribonuclease
GENES       HSA: 6035(RNASE1) 6036(RNASE2)
            PTR: 465207(RNASE1)
            MCC: 704676(RNASE1)
            MMU: 19752(Rnase1)
            CFA: 475395(RNASE1)
            BTA: 282340(RNASE1)
STRUCTURES  PDB: 11BA  11BG  1A2W  1A5P  1A5Q  1AFK  1AFL  1AFU  1AQP  1B6V  
                 1BC4  1BEL  1BZQ  1C0B  1C0C  1DFJ  1DY5  1DZA  1E21  1EIC  
                 1EID  1EIE  1EOS  1EOW  1F0V  1FEV  1FS3  1GQV  1GV7  1H8X  
                 1HI2  1HI3  1HI4  1HI5  1IZP  1IZQ  1IZR  1J7Z  1J80  1J81  
                 1J82  1JN4  1JS0  1JVT  1JVU  1JVV  1K2A  1KF2  1KF3  1KF4  
                 1KF5  1KF7  1KF8  1KH8  1KM8  1KM9  1LSQ  1M07  1N1X  1N3Z  
                 1O0F  1O0H  1O0M  1O0N  1O0O  1QHC  1QWQ  1R3M  1R5C  1R5D  
                 1RAR  1RAS  1RAT  1RBB  1RBC  1RBD  1RBE  1RBF  1RBG  1RBH  
                 1RBI  1RBJ  1RBN  1RBW  1RBX  1RCA  1RCN  1RHA  1RHB  1RNC  
                 1RND  1RNM  1RNN  1RNO  1RNQ  1RNU  1RNV  1RNW  1RNX  1RNY  
                 1RNZ  1ROB  1RPF  1RPG  1RPH  1RRA  1RSM  1RTA  1RTB  1RUV  
                 1SRN  1TQ9  1U1B  1UN3  1UN4  1UN5  1W4O  1W4P  1W4Q  1WBU  
                 1XPS  1XPT  1Y92  1Y94  1YMN  1YMR  1YMW  1Z3L  1Z3M  1Z3P  
                 1Z6D  1Z6S  1Z7X  2AAS  2APQ  2BEX  2BLP  2BLZ  2BWK  2BWL  
                 2BZZ  2C01  2C02  2C05  2E0J  2E0L  2E0M  2E0O  2E33  2G4W  
                 2G4X  2G8Q  2G8R  2J4T  2P49  2P4A  2Q4G  2QCA  2RAT  2RLN  
                 2RNS  3RAT  3RN3  3RSD  3RSK  3RSP  3SRN  4RAT  4RSD  4RSK  
                 4SRN  5RAT  5RSA  6RAT  6RSA  7RAT  7RSA  8RAT  8RSA  9RAT  
                 9RSA  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.27.5
            ExPASy - ENZYME nomenclature database: 3.1.27.5
            ExplorEnz - The Enzyme Database: 3.1.27.5
            ERGO genome analysis and discovery system: 3.1.27.5
            BRENDA, the Enzyme Database: 3.1.27.5
            CAS: 9001-99-4
///
ENTRY       EC 3.1.27.6                 Enzyme
NAME        Enterobacter ribonuclease
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 3'-phosphomonoesters
REACTION    Endonucleolytic cleavage to nucleoside 3'-phosphates and
            3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
COMMENT     Preference for cleavage at CpA. Homopolymers of A, U or G are not
            hydrolysed.
REFERENCE   1  [PMID:5432809]
  AUTHORS   Levy CC, Goldman P.
  TITLE     Residue specificity of a ribonuclease which hydrolyzes polycytidylic
            acid.
  JOURNAL   J. Biol. Chem. 245 (1970) 3257-62.
  ORGANISM  Enterobacter sp.
REFERENCE   2  [PMID:4719125]
  AUTHORS   Marotta CA, Levy CC, Weissman SM, Varricchio F.
  TITLE     Preferred sites of digestion of a ribonuclease from Enterobacter sp.
            in the sequence analysis of Bacillus stearothermophilus 5S
            ribonucleic acid.
  JOURNAL   Biochemistry. 12 (1973) 2901-4.
  ORGANISM  Enterobacter sp.
ORTHOLOGY   KO: K01169  ribonuclease I (enterobacter ribonuclease)
GENES       ECO: b0611(rna)
            ECJ: JW0603(rna)
            ECE: Z0755(rna)
            ECS: ECs0650
            ECC: c0699(rna)
            ECI: UTI89_C0613(rna)
            ECP: ECP_0642
            ECV: APECO1_1440(rna)
            ECW: EcE24377A_0633(rna)
            ECX: EcHS_A0662(rna)
            STY: STY0666(rna)
            STT: t2250(rna)
            SPT: SPA2117(rna)
            STM: STM0617(rna)
            SFL: SF0529(rna)
            SFX: S0535(rna)
            SFV: SFV_0564(rna)
            SSN: SSON_0563(rna)
            SBO: SBO_0476(rna)
            CVI: CV_0956(rna) CV_0960(rnsA)
            BUR: Bcep18194_B0733
            BTE: BTH_II1789
            RET: RHE_CH02874(ypch00990)
            RLE: RL3334(rna)
            GOX: GOX2020
STRUCTURES  PDB: 2PQX  2PQY  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.27.6
            ExPASy - ENZYME nomenclature database: 3.1.27.6
            ExplorEnz - The Enzyme Database: 3.1.27.6
            ERGO genome analysis and discovery system: 3.1.27.6
            BRENDA, the Enzyme Database: 3.1.27.6
///
ENTRY       EC 3.1.27.7                 Enzyme
NAME        ribonuclease F;
            ribonuclease F (E. coli)
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 3'-phosphomonoesters
REACTION    Endonucleolytic cleavage of RNA precursor into two, leaving
            5'-hydroxy and 3'-phosphate groups
REFERENCE   1  [PMID:6179777]
  AUTHORS   Gurevitz M, Watson N, Apirion D.
  TITLE     A cleavage site of ribonuclease F. A putative processing
            endoribonuclease from Escherichia coli.
  JOURNAL   Eur. J. Biochem. 124 (1982) 553-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:6277308]
  AUTHORS   Watson N, Apirion D.
  TITLE     Ribonuclease F, a putative processing endoribonuclease from
            Escherichia coli.
  JOURNAL   Biochem. Biophys. Res. Commun. 103 (1981) 543-51.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.27.7
            ExPASy - ENZYME nomenclature database: 3.1.27.7
            ExplorEnz - The Enzyme Database: 3.1.27.7
            ERGO genome analysis and discovery system: 3.1.27.7
            BRENDA, the Enzyme Database: 3.1.27.7
            CAS: 80498-18-6
///
ENTRY       EC 3.1.27.8                 Enzyme
NAME        ribonuclease V;
            endoribonuclease V
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 3'-phosphomonoesters
REACTION    Hydrolysis of poly(A), forming oligoribonucleotides and ultimately
            3'-AMP
COMMENT     Also hydrolyses poly(U).
REFERENCE   1  [PMID:6246098]
  AUTHORS   Schroder HC, Dose K, Zahn RK, Muller WE.
  TITLE     Isolation and characterization of the novel polyadenylate- and
            polyuridylate-degrading acid endoribonuclease V from calf thymus.
  JOURNAL   J. Biol. Chem. 255 (1980) 5108-12.
  ORGANISM  cow [GN:bta]
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.27.8
            ExPASy - ENZYME nomenclature database: 3.1.27.8
            ExplorEnz - The Enzyme Database: 3.1.27.8
            ERGO genome analysis and discovery system: 3.1.27.8
            BRENDA, the Enzyme Database: 3.1.27.8
            CAS: 74505-36-5
///
ENTRY       EC 3.1.27.9                 Enzyme
NAME        tRNA-intron endonuclease;
            transfer ribonucleate intron endoribonuclease;
            tRNA splicing endonuclease;
            splicing endonuclease;
            tRNATRPintron endonuclease;
            transfer splicing endonuclease
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 3'-phosphomonoesters
REACTION    Endonucleolytic cleavage of pre-tRNA, producing 5'-hydroxy and
            2',3'-cyclic phosphate termini, and specifically removing the intron
COMMENT     The enzyme catalyses the final stage in the maturation of tRNA
            molecules.
REFERENCE   1  [PMID:3937725]
  AUTHORS   Attardi DG, Margarit I, Tocchini-Valentini GP.
  TITLE     Structural alterations in mutant precursors of the yeast tRNALeu3
            gene which behave as defective substrates for a highly purified
            splicing endoribonuclease.
  JOURNAL   EMBO. J. 4 (1985) 3289-97.
  ORGANISM  Xenopus laevis
REFERENCE   2  [PMID:6186398]
  AUTHORS   Peebles CL, Gegenheimer P, Abelson J.
  TITLE     Precise excision of intervening sequences from precursor tRNAs by a
            membrane-associated yeast endonuclease.
  JOURNAL   Cell. 32 (1983) 525-36.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:2470486]
  AUTHORS   Thompson LD, Brandon LD, Nieuwlandt DT, Daniels CJ.
  TITLE     Transfer RNA intron processing in the halophilic archaebacteria.
  JOURNAL   Can. J. Microbiol. 35 (1989) 36-42.
  ORGANISM  Halobacterium volcanii
REFERENCE   4  [PMID:3192521]
  AUTHORS   Thompson LD, Daniels CJ.
  TITLE     A tRNA(Trp) intron endonuclease from Halobacterium volcanii. Unique
            substrate recognition properties.
  JOURNAL   J. Biol. Chem. 263 (1988) 17951-9.
  ORGANISM  Halobacterium volcanii
ORTHOLOGY   KO: K01170  tRNA-intron endonuclease
GENES       HSA: 80746(TSEN2)
            MMU: 381802(Tsen2)
            RNO: 312649(Tsen2)
            CFA: 484651(TSEN2)
            GGA: 415965(RCJMB04_24m3)
            XLA: 444131(MGC80553)
            DME: Dmel_CG31812
            ATH: AT3G45590(ATSEN1)
            OSA: 4341203 4350867
            CME: CMN231C
            SCE: YAR008W(SEN34) YLR105C(SEN2) YMR059W(SEN15) YPL083C(SEN54)
            AGO: AGOS_ADR135W AGOS_AFL012C AGOS_AGR073C
            PIC: PICST_38031
            CGR: CAGL0G00748g CAGL0M11594g
            SPO: SPBC19C7.07c
            AFM: AFUA_5G04010 AFUA_5G11140
            AOR: AO090026000731 AO090102000604
            CNE: CNC05820
            UMA: UM02403.1
            DDI: DDBDRAFT_0204993
            PFA: PF14_0514
            EHI: 11.t00018 26.t00013 26.t00017
            MMP: MMP1132(endA)
            MMQ: MmarC5_0452
            MMZ: MmarC7_0384
            MAE: Maeo_1014
            MVN: Mevan_0454
            MAC: MA3624(endA)
            MBA: Mbar_A0349
            MMA: MM_0512
            MBU: Mbur_1040
            MHU: Mhun_1733
            MST: Msp_0652(endA)
            MSI: Msm_0217
            MKA: MK0341(SEN2_1)
            HAL: VNG2210G(endA)
            HMA: rrnAC2964(endA)
            HWA: HQ1047A(endA)
            NPH: NP0444A(endA)
            TAC: Ta1191
            TVO: TVN0400
            PTO: PTO0518
            PHO: PH0295
            PAB: PAB1099(endA)
            PFU: PF0266
            TKO: TK2215
            RCI: RRC215(endA)
            APE: APE_0685 APE_1646.1
            SSO: SSO0439
            STO: ST0358
            SAI: Saci_0858
            MSE: Msed_2217
            PAI: PAE2269
            NEQ: NEQ205
STRUCTURES  PDB: 1R0V  1R11  1RLV  2CV8  2GJW  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.27.9
            ExPASy - ENZYME nomenclature database: 3.1.27.9
            ExplorEnz - The Enzyme Database: 3.1.27.9
            ERGO genome analysis and discovery system: 3.1.27.9
            BRENDA, the Enzyme Database: 3.1.27.9
            CAS: 117444-13-0
///
ENTRY       EC 3.1.27.10                Enzyme
NAME        rRNA endonuclease;
            alpha-sarcin
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases producing 3'-phosphomonoesters
REACTION    Hydrolysis of the phosphodiester linkage between guanosine and
            adenosine residues at one specific position in 28S rRNA from rat
            ribosomes
COMMENT     Also acts on bacterial rRNA.
REFERENCE   1  [PMID:3288622]
  AUTHORS   Endo Y, Tsurugi K.
  TITLE     The RNA N-glycosidase activity of ricin A-chain. The characteristics
            of the enzymatic activity of ricin A-chain with ribosomes and with
            rRNA.
  JOURNAL   J. Biol. Chem. 263 (1988) 8735-9.
REFERENCE   2  [PMID:3288622]
  AUTHORS   Endo Y, Tsurugi K.
  TITLE     The RNA N-glycosidase activity of ricin A-chain. The characteristics
            of the enzymatic activity of ricin A-chain with ribosomes and with
            rRNA.
  JOURNAL   J. Biol. Chem. 263 (1988) 8735-9.
ORTHOLOGY   KO: K01171  rRNA endonuclease
STRUCTURES  PDB: 1DE3  1R4Y  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.27.10
            ExPASy - ENZYME nomenclature database: 3.1.27.10
            ExplorEnz - The Enzyme Database: 3.1.27.10
            ERGO genome analysis and discovery system: 3.1.27.10
            BRENDA, the Enzyme Database: 3.1.27.10
            CAS: 1407-48-3
///
ENTRY       EC 3.1.30.1                 Enzyme
NAME        Aspergillus nuclease S1;
            endonuclease S1 (Aspergillus);
            single-stranded-nucleate endonuclease;
            deoxyribonuclease S1;
            deoxyribonuclease S1;
            nuclease S1;
            Neurospora crassa single-strand specific endonuclease;
            S1 nuclease;
            single-strand endodeoxyribonuclease;
            single-stranded DNA specific endonuclease;
            single-strand-specific endodeoxyribonuclease;
            single strand-specific DNase;
            Aspergillus oryzae S1 nuclease
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases that are active with either ribo- or
            deoxyribonucleic acids and produce 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage to 5'-phosphomononucleotide and
            5'-phosphooligonucleotide end-products
REFERENCE   1  [PMID:4287053]
  AUTHORS   Ando T.
  TITLE     A nuclease specific for heat-denatured DNA in isolated from a
            product of Aspergillus oryzae.
  JOURNAL   Biochim. Biophys. Acta. 114 (1966) 158-68.
  ORGANISM  Aspergillus oryzae [GN:aor]
REFERENCE   2  [PMID:5123563]
  AUTHORS   Sutton WD.
  TITLE     A crude nuclease preparation suitable for use in DNA reassociation
            experiments.
  JOURNAL   Biochim. Biophys. Acta. 240 (1971) 522-31.
  ORGANISM  Aspergillus oryzae [GN:aor]
REFERENCE   3  [PMID:4691350]
  AUTHORS   Vogt VM.
  TITLE     Purification and further properties of single-strand-specific
            nuclease from Aspergillus oryzae.
  JOURNAL   Eur. J. Biochem. 33 (1973) 192-200.
  ORGANISM  Aspergillus oryzae [GN:aor]
ORTHOLOGY   KO: K05986  
GENES       TET: TTHERM_00088120
            TBR: Tb927.6.2890
            XCC: XCC3198
            XCB: XC_0908
            XCV: XCV3473
            XAC: XAC3356
            XOO: XOO1197
            XOM: XOO_1092(XOO1092)
            HCH: HCH_03919
            GOX: GOX2101
            LIL: LA2250
            LIC: LIC11687
STRUCTURES  PDB: 1AK0  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.30.1
            ExPASy - ENZYME nomenclature database: 3.1.30.1
            ExplorEnz - The Enzyme Database: 3.1.30.1
            ERGO genome analysis and discovery system: 3.1.30.1
            BRENDA, the Enzyme Database: 3.1.30.1
            CAS: 37288-25-8
///
ENTRY       EC 3.1.30.2                 Enzyme
NAME        Serratia marcescens nuclease;
            endonuclease (Serratia marcescens);
            barley nuclease;
            plant nuclease I;
            nucleate endonuclease
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases that are active with either ribo- or
            deoxyribonucleic acids and produce 5'-phosphomonoesters
REACTION    Endonucleolytic cleavage to 5'-phosphomononucleotide and
            5'-phosphooligonucleotide end-products
COMMENT     Hydrolyses double- or single-stranded substrate.
REFERENCE   1  [PMID:4319109]
  AUTHORS   Mikulski AJ, Laskowski M Sr.
  TITLE     Mung bean nuclease I. 3. Purification procedure and (3') omega
            monophosphatase activity.
  JOURNAL   J. Biol. Chem. 245 (1970) 5026-31.
  ORGANISM  Vigna radiata
REFERENCE   2
  AUTHORS   Stevens, A. and Hilmoe, R.J.
  TITLE     Studies on a nuclease from Azotobacter agilis. I. Isolation and mode
            of action.
  JOURNAL   J. Biol. Chem. 235 (1960) 3016-3022.
  ORGANISM  Azotobacter agilis
REFERENCE   3
  AUTHORS   Stevens, A. and Hilmoe, R.J.
  TITLE     Studies on a nuclease from Azotobacter agilis. II. Hydrolysis of
            ribonucleic and deoxyribonucleic acids.
  JOURNAL   J. Biol. Chem. 235 (1960) 3023-3027.
  ORGANISM  Azotobacter agilis
REFERENCE   4  [PMID:4296679]
  AUTHORS   Wechter WJ, Mikulski AJ, Laskowski M Sr.
  TITLE     Gradation of specificity with regard to sugar among nucleases.
  JOURNAL   Biochem. Biophys. Res. Commun. 30 (1968) 318-22.
  ORGANISM  Vigna radiata
ORTHOLOGY   KO: K05987  
GENES       CNE: CNE03360
            YEN: YE2923(nuc)
            SPE: Spro_1810
            PAT: Patl_0573
STRUCTURES  PDB: 1G8T  1QAE  1QL0  1SMN  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.30.2
            ExPASy - ENZYME nomenclature database: 3.1.30.2
            ExplorEnz - The Enzyme Database: 3.1.30.2
            ERGO genome analysis and discovery system: 3.1.30.2
            BRENDA, the Enzyme Database: 3.1.30.2
            CAS: 9025-65-4
///
ENTRY       EC 3.1.31.1                 Enzyme
NAME        micrococcal nuclease;
            spleen endonuclease;
            thermonuclease;
            nuclease T;
            micrococcal endonuclease;
            nuclease T';
            staphylococcal nuclease;
            spleen phosphodiesterase;
            Staphylococcus aureus nuclease;
            Staphylococcus aureus nuclease B;
            ribonucleate (deoxynucleate) 3'-nucleotidohydrolase
CLASS       Hydrolases;
            Acting on ester bonds;
            Endoribonucleases that are active with either ribo- or
            deoxyribonucleic acids and produce 3'-phosphomonoesters
REACTION    Endonucleolytic cleavage to nucleoside 3'-phosphates and
            3'-phosphooligonucleotide end-products
COMMENT     Hydrolyses double- or single-stranded substrate.
REFERENCE   1
  AUTHORS   Alexander, M., Heppel, L.A. and Hurwitz, J.
  TITLE     The purification and properties of micrococcal nuclease.
  JOURNAL   J. Biol. Chem. 236 (1961) 3014-3019.
  ORGANISM  Micrococcus pyogenes
REFERENCE   2
  AUTHORS   Anfinsen, C.B., Cuatrecasas, P. and Taniuchi, H.
  TITLE     Staphylococcal nuclease, chemical properties and catalysis.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 4, Academic Press,
            New York, 1971, p. 177-204.
REFERENCE   3
  AUTHORS   Reddi, K.K.
  TITLE     Micrococcal nuclease.
  JOURNAL   Methods Enzymol. 12A (1967) 257-262.
  ORGANISM  Micrococcus pyogenes, Staphylococcus aureus
REFERENCE   4  [PMID:5922962]
  AUTHORS   Sulkowski E, Laskowski M Sr.
  TITLE     Phosphatase-free crystalline micrococcal nuclease.
  JOURNAL   J. Biol. Chem. 241 (1966) 4386-8.
  ORGANISM  Micrococcus pyogenes
ORTHOLOGY   KO: K01174  micrococcal nuclease
GENES       NOC: Noc_1218 Noc_1464
            HAR: HEAR3042(nuc)
            CJE: Cj0979c
            PCA: Pcar_2433
            DDE: Dde_2354
            RLE: pRL80118
            BSU: BG13573(yokF)
            BAR: GBAA_pXO1_0211
            BAA: BXA0211
            SAU: SA0746 SA1160(nuc)
            SAV: SAV0815(nuc) SAV1324(nuc)
            SAM: MW0769 MW1211(nuc)
            SAR: SAR0847(nuc) SAR1334(nucI)
            SAS: SAS0756 SAS1264
            SAC: SACOL0860(nuc) SACOL1357
            SAB: SAB0748(nuc) SAB1182(nucI)
            SAA: SAUSA300_0776(nuc) SAUSA300_1222(nuc)
            SAO: SAOUHSC_00818 SAOUHSC_01316
            SAJ: SaurJH9_0816 SaurJH9_1385
            SAH: SaurJH1_0832 SaurJH1_1412
            SEP: SE1004
            SER: SERP0891
            SHA: SH1583(nuc)
            SSP: SSP1444
            EFA: EF0511(nuc-1) EF_B0045(nuc-2)
            CHY: CHY_1644(nucH1) CHY_1699(nucH2)
            MPU: MYPU_1390
            MMO: MMOB1270(nuc)
            MHJ: MHJ_0262
            MHP: MHP7448_0270
            MSY: MS53_0110
            CGL: NCgl1779(cgl1853)
            AAU: AAur_pTC10086
            CYA: CYA_1940
            CYB: CYB_0109(nucH)
            ANA: all2918
            AVA: Ava_0982 Ava_2776 Ava_B0290
            AAE: aq_710(nucI)
            MJA: MJ1439
            MMP: MMP1201
            PAB: PAB0704
            PFU: PF1298
STRUCTURES  PDB: 1A2T  1A2U  1A3T  1A3U  1A3V  1AEX  1ENA  1ENC  1EQV  1EY0  
                 1EY4  1EY5  1EY6  1EY7  1EY8  1EY9  1EYA  1EYC  1EYD  1EZ6  
                 1EZ8  1F2M  1F2Y  1F2Z  1IHZ  1II3  1JOK  1JOO  1JOQ  1JOR  
                 1KDA  1KDB  1KDC  1NSN  1NUC  1RKN  1SNC  1SND  1SNM  1SNO  
                 1SNP  1SNQ  1STA  1STB  1STG  1STH  1STN  1STY  1SYB  1SYC  
                 1SYD  1SYE  1SYF  1SYG  1TQO  1TR5  1TT2  1U9R  2ENB  2EXZ  
                 2EY1  2EY2  2EY5  2EY6  2EYF  2EYH  2EYJ  2EYL  2EYM  2EYO  
                 2EYP  2F0D  2F0E  2F0F  2F0G  2F0H  2F0I  2F0J  2F0K  2F0L  
                 2F0M  2F0N  2F0O  2F0P  2F0Q  2F0S  2F0T  2F0U  2F0V  2F0W  
                 2F3V  2F3W  2FXY  2FXZ  2GSI  2NUC  2OXP  2PQE  2SNM  2SOB  
                 3NUC  5NUC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.1.31.1
            ExPASy - ENZYME nomenclature database: 3.1.31.1
            ExplorEnz - The Enzyme Database: 3.1.31.1
            ERGO genome analysis and discovery system: 3.1.31.1
            BRENDA, the Enzyme Database: 3.1.31.1
            CAS: 9013-53-0
///
ENTRY       EC 3.1.-.-                  Enzyme
CLASS       Hydrolases;
            Acting on ester bonds
REACTION    D-glycero-D-manno-Heptose 1,7-bisphosphate + H2O <=>
            D-glycero-D-manno-Heptose 1-phosphate + Orthophosphate [RN:R05647]
SUBSTRATE   D-glycero-D-manno-Heptose 1,7-bisphosphate [CPD:C11472];
            H2O [CPD:C00001]
PRODUCT     D-glycero-D-manno-Heptose 1-phosphate [CPD:C07838];
            Orthophosphate [CPD:C00009]
///
ENTRY       EC 3.2.1.1                  Enzyme
NAME        alpha-amylase;
            glycogenase;
            alpha amylase, alpha-amylase;
            endoamylase;
            Taka-amylase A
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,4-alpha-D-glucan glucanohydrolase
REACTION    Endohydrolysis of 1,4-alpha-D-glucosidic linkages in polysaccharides
            containing three or more 1,4-alpha-linked D-glucose units
ALL_REAC    (other) R02108 R06209(G)
COMMENT     Acts on starch, glycogen and related polysaccharides and
            oligosaccharides in a random manner; reducing groups are liberated
            in the alpha-configuration. The term 'alpha'' relates to the initial
            anomeric configuration of the free sugar group released and not to
            the configuration of the linkage hydrolysed.
REFERENCE   1
  AUTHORS   Fischer, E.H. and Stein, E.A.
  TITLE     alpha-Amylases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 313-343.
REFERENCE   2
  AUTHORS   Manners, D.J.
  TITLE     Enzymic synthesis and degradation of starch and glycogen.
  JOURNAL   Adv. Carbohydr. Chem. 17 (1962) 371-430.
REFERENCE   3
  AUTHORS   Schwimmer, S. and Balls, A.K.
  TITLE     Isolation and properties of crystalline alpha-amylase from
            germinated barley.
  JOURNAL   J. Biol. Chem. 179 (1949) 1063-1074.
  ORGANISM  Hordeum vulgare [GN:ehvu]
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01176  alpha-amylase
            KO: K07405  alpha-amylase
GENES       HSA: 276(AMY1A) 277(AMY1B) 278(AMY1C) 279(AMY2A) 280(AMY2B)
                 84569(LYZL1)
            PTR: 450382(LYZL1) 469397(AMY1A)
            MMU: 11722(Amy1) 11723(Amy2)
            RNO: 24203(Amy1)
            CFA: 480825(LOC480825)
            SSC: 397397(AMY2B)
            GGA: 414139(AMY1A) 414140(AMY2A)
            XLA: 379600(MGC64337)
            XTR: 493323(MGC89676)
            DRE: 393400(zgc:66313)
            SPU: 577578(LOC577578) 577636(LOC577636)
            DME: Dmel_CG17876(Amy-d) Dmel_CG18730(Amy-p) Dmel_CG8221
            ATH: AT4G25000(AMY1)
            OSA: 4330832 4342055 4345812
            SPO: SPAC23D3.14c SPBC16A3.13
            ANI: AN2018.2 AN3402.2
            AFM: AFUA_1G15150 AFUA_2G00710 AFUA_2G13460 AFUA_4G10130
            AOR: AO090005001193 AO090023000944
            ANG: An05g02100(amyA) An11g03340 An12g06930(amyA)
            CNE: CNE03480 CNK02760
            DDI: DDB_0214924(amyA)
            TET: TTHERM_00312180 TTHERM_00411610
            EHI: 24.t00041
            ECO: b1927(amyA) b3571(malS)
            ECJ: JW1912(amyA) JW3543(malS)
            ECE: Z3017(amyA) Z4996(malS)
            ECS: ECs2666 ECs4454
            ECC: c2342(amyA) c4392(malS)
            ECI: UTI89_C2128(amyA) UTI89_C4113(malS)
            ECP: ECP_1861 ECP_3675
            ECV: APECO1_2879(malS) APECO1_968(amyA)
            ECW: EcE24377A_2162(amyA) EcE24377A_4068(malS)
            ECX: EcHS_A2027 EcHS_A3774
            STY: STY2171(amyA) STY4134(malS)
            STT: t0914(amyA) t3855(malS)
            SPT: SPA0907(amyA) SPA3515(malS)
            SEC: SC1967(amyA) SC3599(malS)
            STM: STM1963(amyA) STM3664(malS)
            YPE: YPO4080(malS)
            YPK: y4097(malS)
            YPM: YP_3989(malS)
            YPA: YPA_3005
            YPN: YPN_3724
            YPS: YPTB3909(malS)
            YPI: YpsIP31758_4138(malS)
            YEN: YE1962(amyA)
            SFL: SF1970(amyA) SF3615(malS)
            SFX: S2066(amyA) S4154(malS)
            SFV: SFV_1971(amyA) SFV_3969(malS)
            SSN: SSON_1983(amyA)
            SBO: SBO_1079(amyA) SBO_3579(malS)
            SDY: SDY_1088(amyA)
            MSU: MS2071(amyA)
            XCC: XCC0748(amy)
            XCB: XC_3487
            XCV: XCV0849 XCV0850
            XAC: XAC0798(amy)
            VCH: VCA0250 VCA0860
            VCO: VC0395_0377(malS) VC0395_0979(amy1)
            VVU: VV2_0400 VV2_0903 VV2_1622
            VVY: VVA0433 VVA0960 VVA1376
            VPA: VP0020 VPA0461 VPA0999 VPA1616
            VFI: VF0017 VF1132
            PPR: PBPRA1292 PBPRB0404
            SDN: Sden_1800
            CPS: CPS_3370
            PAT: Patl_2859
            SDE: Sde_0563 Sde_0573
            LPN: lpg1669 lpg1671
            LPF: lpl1634 lpl1636
            LPP: lpp1641 lpp1643
            HCH: HCH_00439
            AHA: AHA_0837 AHA_1215 AHA_1304
            BUR: Bcep18194_C7028
            NEU: NE2032(amyA)
            DAR: Daro_0583
            DDE: Dde_0415
            LIP: LI0331(amyA)
            BBA: Bd1224(amy)
            SAT: SYN_00295 SYN_00687 SYN_00880 SYN_02854
            ATU: Atu3914(amyA)
            ATC: AGR_L_1863
            RPA: RPA3642
            NHA: Nham_1466
            RRU: Rru_A0507 Rru_A1604
            BSU: BG10473(amyE)
            BHA: BH0413
            BAN: BA3551(amyS)
            BAR: GBAA3551(amyS)
            BAA: BA_4041
            BAT: BAS3291
            BCE: BC3482
            BTK: BT9727_3261(amyS)
            BLI: BL00499
            BLD: BLi00656
            BCL: ABC1611
            BAY: RBAM_003280
            GKA: GK0707 GK3181
            LLA: L128692(amyY) L77437(amyL)
            LLC: LACR_1849
            LLM: llmg_0743(amyY)
            SPZ: M5005_Spy_1065(amyA)
            SPN: SP_1382
            SPR: spr0247(pulA) spr1239(amy)
            SPD: SPD_1215(amy)
            SAG: SAG0708
            SAN: gbs0681
            SAK: SAK_0834
            SMU: SMU.1590(amyA)
            STC: str1542(amyL)
            STL: stu1542(amyL)
            SSA: SSA_0453 SSA_1024(amy)
            SGO: SGO_1075
            LPL: lp_0025(amy1) lp_0179(amy2)
            LSL: LSL_1289(amyA)
            CAC: CA_P0168(amyA)
            MPU: MYPU_6320(amyC)
            CGL: NCgl1178(cgl1225)
            CGB: cg1382(glgE)
            CDI: DIP1066
            SMA: SAV5981(amyA4)
            PAC: PPA0592
            STP: Strop_2001
            RBA: RB2160 RB5200
            ANA: alr2190
            BTH: BT_4690
            BFR: BF3209
            BFS: BF3048
            PGI: PG1683
            CHU: CHU_0801 CHU_0959(amyA) CHU_2409(amyA)
            GFO: GFO_2141
            TMA: TM1650 TM1840
            MJA: MJ1611
            MMP: MMP1291
            MMQ: MmarC5_0302
            MMZ: MmarC7_0536
            MAE: Maeo_0011
            MVN: Mevan_0601
            MAC: MA4052 MA4053
            MBA: Mbar_A0537 Mbar_A0538
            MMA: MM_0861 MM_0862
            MBU: Mbur_0437
            MTP: Mthe_0255
            MHU: Mhun_0836
            MEM: Memar_1267
            MBN: Mboo_1537
            TAC: Ta0339m
            TVO: TVN0431
            PTO: PTO1240
            PHO: PH0193
            PAB: PAB0118(amyA)
            PFU: PF0272
            TKO: TK1809
            RCI: RCIX1323(amyA)
            SMR: Smar_1389
            SSO: SSO0988
            STO: ST0817
            SAI: Saci_1200
            MSE: Msed_1418
            PAI: PAE3428
            PIS: Pisl_0969
            PCL: Pcal_1039
            PAS: Pars_1879
            TPE: Tpen_0135
STRUCTURES  PDB: 1AMY  1AQH  1AQM  1AVA  1B0I  1B2Y  1BAG  1BG9  1BLI  1BPL  
                 1BSI  1BVN  1C8Q  1CLV  1CPU  1DHK  1E3X  1E3Z  1E40  1E43  
                 1EH9  1EHA  1G94  1G9H  1HNY  1HT6  1HVX  1HX0  1IZJ  1IZK  
                 1JAE  1JD7  1JD9  1JFH  1JI1  1JXJ  1JXK  1KB3  1KBB  1KBK  
                 1KGU  1KGW  1KGX  1KXH  1KXQ  1KXT  1KXV  1L0P  1MFU  1MFV  
                 1MWO  1MXD  1MXG  1NM9  1OB0  1OSE  1P6W  1PIF  1PIG  1PPI  
                 1Q4N  1RP8  1RP9  1RPK  1SMD  1TMQ  1U2Y  1U30  1U33  1UA3  
                 1UA7  1UD2  1UD3  1UD4  1UD5  1UD6  1UD8  1UH2  1UH3  1UH4  
                 1VAH  1VB9  1VIW  1VJS  1W9X  1WO2  1WZA  1XCW  1XCX  1XD0  
                 1XD1  1XGZ  1XH0  1XH1  1XH2  1XV8  1Z32  2AAA  2B5D  2BHU  
                 2BHY  2BHZ  2BXY  2BXZ  2BY0  2BY1  2BY2  2BY3  2CPU  2D0F  
                 2D0G  2D0H  2DIE  2GJP  2GJR  2GUY  2GVY  2TAA  3CPU  6TAA  
                 7TAA  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.1
            ExPASy - ENZYME nomenclature database: 3.2.1.1
            ExplorEnz - The Enzyme Database: 3.2.1.1
            ERGO genome analysis and discovery system: 3.2.1.1
            BRENDA, the Enzyme Database: 3.2.1.1
            CAS: 9000-90-2
///
ENTRY       EC 3.2.1.2                  Enzyme
NAME        beta-amylase;
            saccharogen amylase;
            glycogenase;
            beta amylase, beta-amylase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,4-alpha-D-glucan maltohydrolase
REACTION    Hydrolysis of 1,4-alpha-D-glucosidic linkages in polysaccharides so
            as to remove successive maltose units from the non-reducing ends of
            the chains
ALL_REAC    (other) R02112 R06159(G)
COMMENT     Acts on starch, glycogen and related polysaccharides and
            oligosaccharides producing beta-maltose by an inversion. The term
            'beta'' relates to the initial anomeric configuration of the free
            sugar group released and not to the configuration of the linkage
            hydrolysed.
REFERENCE   1
  AUTHORS   Balls, A.K., Walden, M.K. and Thompson, R.R.
  TITLE     A crystalline beta-amylase from sweet potatoes.
  JOURNAL   J. Biol. Chem. 173 (1948) 9-19.
  ORGANISM  sweet potato
REFERENCE   2
  AUTHORS   French, D.
  TITLE     beta-Amylases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 345-368.
REFERENCE   3
  AUTHORS   Manners, D.J.
  TITLE     Enzymic synthesis and degradation of starch and glycogen.
  JOURNAL   Adv. Carbohydr. Chem. 17 (1962) 371-430.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01177  beta-amylase
GENES       ATH: AT4G17090(CT-BMY)
            OSA: 4349417
            EHI: 1.t00074 1.t00075
            CBO: CBO1203
            CBA: CLB_1233(amyB)
            CBH: CLC_1245(amyB)
            CBF: CLI_1286(amyB)
STRUCTURES  PDB: 1B1Y  1B90  1B9Z  1BFN  1BTC  1BYA  1BYB  1BYC  1BYD  1FA2  
                 1ITC  1J0Y  1J0Z  1J10  1J11  1J12  1J18  1Q6C  1Q6D  1Q6E  
                 1Q6F  1Q6G  1UKO  1UKP  1V3H  1V3I  1VEM  1VEN  1VEO  1VEP  
                 1WDP  1WDQ  1WDR  1WDS  2DQX  5BCA  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.2
            ExPASy - ENZYME nomenclature database: 3.2.1.2
            ExplorEnz - The Enzyme Database: 3.2.1.2
            ERGO genome analysis and discovery system: 3.2.1.2
            BRENDA, the Enzyme Database: 3.2.1.2
            CAS: 9000-91-3
///
ENTRY       EC 3.2.1.3                  Enzyme
NAME        glucan 1,4-alpha-glucosidase;
            glucoamylase;
            amyloglucosidase;
            gamma-amylase;
            lysosomal alpha-glucosidase;
            acid maltase;
            exo-1,4-alpha-glucosidase;
            glucose amylase;
            gamma-1,4-glucan glucohydrolase;
            acid maltase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,4-alpha-D-glucan glucohydrolase
REACTION    Hydrolysis of terminal 1,4-linked alpha-D-glucose residues
            successively from non-reducing ends of the chains with release of
            beta-D-glucose
ALL_REAC    (other) R01790 R01791 R06199(G)
COMMENT     Most forms of the enzyme can rapidly hydrolyse
            1,6-alpha-D-glucosidic bonds when the next bond in the sequence is
            1,4, and some preparations of this enzyme hydrolyse 1,6- and
            1,3-alpha-D-glucosidic bonds in other polysaccharides. This entry
            covers all such enzymes acting on polysaccharides more rapidly than
            on oligosaccharides. EC 3.2.1.20 alpha-glucosidase, from mammalian
            intestine, can catalyse similar reactions.
REFERENCE   1
  AUTHORS   French, D. and Knapp, D.W.
  TITLE     The maltase of Clostridium acetobutylicum.
  JOURNAL   J. Biol. Chem. 187 (1950) 463-471.
  ORGANISM  Clostridium acetobutylicum [GN:cac]
REFERENCE   2  [PMID:4286143]
  AUTHORS   Brown BI, Brown DH.
  TITLE     The subcellular distribution of enzymes in type II glycogenosis and
            the occurrence of an oligo-alpha-1,4-glucan glucohydrolase in human
            tissues.
  JOURNAL   Biochim. Biophys. Acta. 110 (1965) 124-33.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:4313883]
  AUTHORS   Jeffrey PL, Brown DH, Brown BI.
  TITLE     Studies of lysosomal alpha-glucosidase. I. Purification and
            properties of the rat liver enzyme.
  JOURNAL   Biochemistry. 9 (1970) 1403-15.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:4743896]
  AUTHORS   Kelly JJ, Alpers DH.
  TITLE     Properties of human intestinal glucoamylase.
  JOURNAL   Biochim. Biophys. Acta. 315 (1973) 113-22.
  ORGANISM  human [GN:hsa]
REFERENCE   5
  AUTHORS   Miller, K.D. and Copeland, W.H.
  TITLE     A blood trans-alpha-glucosylase.
  JOURNAL   Biochim. Biophys. Acta 22 (1956) 193-194.
REFERENCE   6
  AUTHORS   Tsujisaka, Y., Fukimoto, J. and Yamamoto, T.
  TITLE     Specificity of crystalline saccharogenic amylase of moulds.
  JOURNAL   Nature 181 (1958) 770-771.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01178  glucoamylase
GENES       HSA: 8972(MGAM)
            PTR: 463790(MGAM)
            SPU: 592667(LOC592667)
            SCE: YDL037C(BSC1) YIL099W(SGA1) YIR019C(MUC1)
            AGO: AGOS_ADL225W
            PIC: PICST_28187(WSC3) PICST_30325(MUC1.11) PICST_33726(SGA1)
                 PICST_56703(CGA1)
            CGR: CAGL0G02717g
            SPO: SPBC14C8.05c
            ANI: AN7402.2
            AFM: AFUA_2G00690 AFUA_4G10140
            AOR: AO090003000321 AO090010000746
            ANG: An03g06550(glaA)
            CNE: CNE02630 CNE03700
            UMA: UM04064.1
            EHI: 120.t00008
            SDN: Sden_2004
            SFR: Sfri_1775
            SAZ: Sama_1656
            SBL: Sbal_2348 Sbal_2349
            SBM: Shew185_2337
            SLO: Shew_1873
            SHE: Shewmr4_1869
            SHM: Shewmr7_2109
            SHN: Shewana3_1924
            SDE: Sde_0600
            LPN: lpg0422
            LPF: lpl0465
            LPP: lpp0489
            CVI: CV_3490
            REH: H16_A0429
            BPS: BPSS0144
            BPM: BURPS1710b_3662 BURPS1710b_A1658
            BTE: BTH_II0213
            AZO: azo2310(palZ)
            SMD: Smed_5985
            RET: RHE_PF00442(ypf00234)
            RLE: RL2956
            BBT: BBta_p0098
            NHA: Nham_0995
            GBE: GbCGDNIH1_1316
            RRU: Rru_A3302
            ABA: Acid345_2807
            SEN: SACE_6308 SACE_7136
            AVA: Ava_4198
            CHU: CHU_0399
            RCA: Rcas_2590
            DGE: Dgeo_0725
            MMP: MMP1292
            MAC: MA1190 MA4050
            MBA: Mbar_A0540 Mbar_A1916
            MMA: MM_0864 MM_2225 MM_2226
            MBU: Mbur_0526
            HMA: rrnAC2353(cga-2)
            TAC: Ta0342
            TVO: TVN0428
            PTO: PTO0365 PTO0598 PTO1492
            RCI: RCIX1035
            SSO: SSO0990 SSO2473
            STO: ST0815 ST2017
            SAI: Saci_1198
STRUCTURES  PDB: 1AC0  1ACZ  1AGM  1AYX  1DOG  1GAH  1GAI  1GLM  1KUL  1KUM  
                 1LF6  1LF9  2F6D  2FBA  3GLY  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.3
            ExPASy - ENZYME nomenclature database: 3.2.1.3
            ExplorEnz - The Enzyme Database: 3.2.1.3
            ERGO genome analysis and discovery system: 3.2.1.3
            BRENDA, the Enzyme Database: 3.2.1.3
            CAS: 9032-08-0
///
ENTRY       EC 3.2.1.4                  Enzyme
NAME        cellulase;
            endo-1,4-beta-D-glucanase;
            beta-1,4-glucanase;
            beta-1,4-endoglucan hydrolase;
            celluase A;
            cellulosin AP;
            endoglucanase D;
            alkali cellulase;
            cellulase A 3;
            celludextrinase;
            9.5 cellulase;
            avicelase;
            pancellase SS
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,4-(1,3;1,4)-beta-D-glucan 4-glucanohydrolase
REACTION    Endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose,
            lichenin and cereal beta-D-glucans
ALL_REAC    (other) R02886 R06200(G)
COMMENT     Will also hydrolyse 1,4-linkages in beta-D-glucans also containing
            1,3-linkages.
REFERENCE   1  [PMID:14025219]
  AUTHORS   DATTA PK, HANSON KR, WHITAKER DR.
  TITLE     Improved procedures for preparation and characterization of
            Myrothecium cellulase. 3. Molecular weight, amino acid composition,
            terminal residues, and other properties.
  JOURNAL   Can. J. Biochem. Physiol. 41 (1963) 697-705.
REFERENCE   2
  AUTHORS   Larner, J.
  TITLE     Other glucosidases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 369-378.
REFERENCE   3
  AUTHORS   Myers, F.L. and Northcote, D.H.
  TITLE     Partial purification and some properties of a cellulase from Helix
            pomatia.
  JOURNAL   Biochem. J. 71 (1959) 749-756.
  ORGANISM  Helix pomatia
REFERENCE   4
  AUTHORS   Nishizawa, K. and Hashimoto, Y.
  TITLE     Cellulose splitting enzymes. VI. Difference in the specificities of
            cellulase and beta-glucosidase from Irpex lacteus.
  JOURNAL   Arch. Biochem. Biophys. 81 (1959) 211-222.
  ORGANISM  Irpex lacteus
REFERENCE   5
  AUTHORS   Whitaker, D.R., Hanson, K.R. and Datta, P.K.
  TITLE     Improved procedures for preparation and characterization of
            myrothecium cellulase. 2. Purification procedures.
  JOURNAL   Can. J. Biochem. Physiol. 41 (1963) 671-696.
REFERENCE   6
  AUTHORS   Hatfield, R. and Nevins, D.J.
  TITLE     Purification and properties of an endoglucanase isolated from the
            cell walls of Zea mays seedlings.
  JOURNAL   Carbohydr. Res. 148 (1986) 265-278.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   7
  AUTHORS   Hatfield, R. and Nevins, D.J.
  TITLE     Hydrolytic activity and substrate specificity of an endoglucanase
            from Zea mays seedling cell walls.
  JOURNAL   Plant Physiol. 83 (1987) 203-207.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   8
  AUTHORS   Inohue, M., Hayashgi, K. and Nevins, D.J.
  TITLE     Polypeptide characteristics and immunological properties of exo- and
            endoglucanases purified from maize coleoptile cell walls.
  JOURNAL   J. Plant Physiol. 154 (1999) 334-340.
  ORGANISM  Zea mays [GN:ezma]
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01179  endoglucanase
GENES       ATH: AT3G43860 AT4G39000 AT4G39010
            OSA: 4330912 4334029 4335944 4347660
            ANI: AN1285.2
            AFM: AFUA_3G03870 AFUA_5G01830 AFUA_6G01800 AFUA_6G07480
                 AFUA_7G01540 AFUA_7G06740
            AOR: AO090003001342
            ANG: An07g08950(eglB) An14g02760(eglA)
            CNE: CNH00790
            DDI: DDB_0215351(celA) DDB_0230001
            ECO: b3531(bcsC)
            ECJ: JW3499(bcsZ)
            ECE: Z4946(yhjM)
            ECS: ECs4411
            ECC: c4343(yhjM)
            ECI: UTI89_C4063(yhjM)
            ECP: ECP_3631
            ECV: APECO1_2917(bcsZ)
            ECW: EcE24377A_4019(bcsZ)
            STY: STY4183(yhjM)
            STT: t3900(yhjM)
            SPT: SPA3473(yhjM)
            SEC: SC3551(bcsC)
            STM: STM3617
            YPK: y3831
            YPA: YPA_3825
            YPN: YPN_3647
            YPP: YPDSF_3364
            YPS: YPTB3837
            YPI: YpsIP31758_4070(bcsZ)
            YEN: YE4072A(bcsZ)
            SFX: S4204(yhjM)
            SFV: SFV_3557(yhjM)
            SSN: SSON_3860(yhjM)
            SBO: SBO_3530(yhjM)
            ECA: ECA1981(celV) ECA4373(bcsZ)
            ENT: Ent638_3928 Ent638_3936
            SPE: Spro_0150
            XFA: XF2708
            XFT: PD2061(egl)
            XCC: XCC0026(egl) XCC0027(egl) XCC0028(egl) XCC2387(egl2)
                 XCC3521(engXCA)
            XCB: XC_0026 XC_0027 XC_0028 XC_0639 XC_1727
            XCV: XCV0029(egl1) XCV0031(egl2) XCV0033(egl3) XCV0358
                 XCV0670(engXCA) XCV2704(egl4) XCV3641(bcsZ)
            XAC: XAC0028(egl) XAC0029(egl) XAC0030(egl) XAC0612(engXCA)
                 XAC2522(egl2) XAC3516
            XOO: XOO0281(egl) XOO0282(egl) XOO0283(egl) XOO4019(engXCA)
            XOM: XOO_0253(XOO0253) XOO_0254(XOO0254) XOO_0255(XOO0255)
                 XOO_3789(XOO3789)
            VFI: VFA0882
            PPR: PBPRA1722
            PPU: PP_2637
            PPF: Pput_2138
            PST: PSPTO_1029(wssD)
            PHA: PSHAa2164(bcsZ)
            PAT: Patl_1404
            SDE: Sde_0636 Sde_2490 Sde_2636 Sde_3237 Sde_3239
            CVI: CV_2676(bscZ)
            RSO: RSp0162(egl)
            REU: Reut_B3526
            RME: Rmet_2251
            BMA: BMAA1589(bcsC)
            BXE: Bxe_B2042
            BVI: Bcep1808_1350
            BUR: Bcep18194_A4526
            BCN: Bcen_0898
            BCH: Bcen2424_1380
            BAM: Bamb_1259
            BPS: BPSS1581(bcsZ)
            BPM: BURPS1710b_A0632(bcsZ)
            BTE: BTH_II0792
            PNU: Pnuc_1167
            AAV: Aave_2102
            AZO: azo2236(eglA)
            GSU: GSU2196
            GME: Gmet_2294
            PCA: Pcar_1216
            MXA: MXAN_4837(celA)
            SMD: Smed_5210
            RET: RHE_CH00072 RHE_CH00228(egl) RHE_CH01544(celC)
            RLE: RL0081 RL0236 RL1648(celY)
            BME: BMEII0724
            BJA: blr3367
            RPA: RPA4584
            RSP: RSP_0157
            RSH: Rsph17029_1976
            RSQ: Rsph17025_0964
            MMR: Mmar10_2725
            ZMO: ZMO1086(celA)
            ACR: Acry_0570
            SUS: Acid_2606 Acid_4467
            BSU: BG10437(bglC)
            BCZ: BCZK2421(choA) pE33L466_0086(celCCC)
            BCY: Bcer98_3257
            BLI: BL01471(bglC)
            BLD: BLi01880 BLi01882 BLi02088(bglC)
            BCL: ABC3362
            BAY: RBAM_018100(bglC)
            BPU: BPUM_1558(bglC)
            OIH: OB2238 OB2332
            SAB: SAB1605c SAB2338c
            SAJ: SaurJH9_2482
            SAH: SaurJH1_2531
            LLM: llmg_1166 llmg_1167
            STH: STH1079 STH1080 STH1081
            CAC: CAC0214 CAC0215
            CNO: NT01CX_0791(celM) NT01CX_0793
            CTH: Cthe_0040
            CDF: CD2546 CD3446(celM)
            AMT: Amet_2620 Amet_2621
            DSY: DSY1620 DSY1621 DSY1622
            CSC: Csac_0678 Csac_1079
            TTE: TTE0359 TTE0441(frvX) TTE0442(frvX2) TTE0443(frvX3)
            UUR: UU280(celM)
            AYW: AYWB_658(ysdC)
            MTU: Rv1089A(celA2a) Rv1090(celA2b)
            MTC: MT0067(celA)
            MBO: Mb0063(celA1) Mb1119(celA2a) Mb1120(celA2b)
            MBB: BCG_0093(celA1) BCG_1149(celA2a) BCG_1150(celA2b)
            MAV: MAV_0326
            MSM: MSMEG_6752
            MUL: MUL_0371 MUL_2210
            MVA: Mvan_3505 Mvan_5837
            MGI: Mflv_1003 Mflv_3001
            MMC: Mmcs_5301
            MKM: Mkms_5390
            MJL: Mjls_5680
            CMI: CMM_2443(celB) pCM1_0020(celA)
            NCA: Noca_3501 Noca_4617
            TFU: Tfu_1627 Tfu_2176
            FAL: FRAAL4955(celA1) FRAAL4956(celA2)
            ACE: Acel_0135
            KRA: Krad_4622
            SEN: SACE_4004(bglC) SACE_6060(celA)
            RBA: RB5256 RB8541(celM)
            SYN: slr0897
            SYG: sync_1467 sync_2705
            CHU: CHU_1401(cel) CHU_1655(cel) CHU_1842(cel) CHU_2103(cel)
                 CHU_2802(bglC)
            FJO: Fjoh_4946
            CCH: Cag_0339
            PLT: Plut_0993
            DRA: DR_0229
            DGE: Dgeo_1994
            AAE: aq_1401(celY)
            TMA: TM1048 TM1049 TM1050 TM1524 TM1751 TM1752
            TPT: Tpet_1702
            TME: Tmel_0097
            FNO: Fnod_1077
            MJA: MJ0555
            MMP: MMP1116
            MMQ: MmarC5_0468
            MMZ: MmarC7_0368
            MAE: Maeo_0709
            MVN: Mevan_0441
            MAC: MA3849
            MBA: Mbar_A0214
            MMA: MM_0673
            MBU: Mbur_0712
            MEM: Memar_1505
            MSI: Msm_0134
            MKA: MK0383
            AFU: AF1795(celM)
            HAL: VNG1498G(celM)
            HMA: rrnAC0799(cdlM)
            HWA: HQ2923A(celM)
            NPH: NP4306A(celM)
            PHO: PH1171
            PAB: PAB0437 PAB0632(celB-like)
            PFU: PF1547
            TKO: TK0781
            SMR: Smar_0057
            HBU: Hbut_1154
            PAI: PAE1385
            PIS: Pisl_1432
            PCL: Pcal_0842
            PAS: Pars_0452
            TPE: Tpen_0002 Tpen_0177
STRUCTURES  PDB: 1A39  1A3H  1AIW  1CEC  1CEM  1CEN  1CEO  1CLC  1CX1  1DAQ  
                 1DAV  1DYM  1DYS  1E5J  1ECE  1EDG  1EG1  1EGZ  1F9D  1F9O  
                 1FAE  1FBO  1FBW  1FCE  1G01  1G0C  1G87  1G9G  1G9J  1GA2  
                 1GU3  1GZJ  1H0B  1H11  1H1N  1H2J  1H5V  1H8V  1HD5  1HF6  
                 1IA6  1IA7  1IS9  1J83  1J84  1JS4  1K72  1KFG  1KS4  1KS5  
                 1KS8  1KSC  1KSD  1KWF  1L1Y  1L2A  1L8F  1LF1  1NLR  1OA2  
                 1OA3  1OA4  1OA7  1OA9  1OCQ  1OJI  1OJJ  1OJK  1OLQ  1OLR  
                 1OVW  1QHZ  1QI0  1QI2  1TF4  1TML  1TVN  1TVP  1ULO  1ULP  
                 1UT9  1UU4  1UU5  1UU6  1UWW  1V0A  1VJZ  1VRX  1W2U  1W3K  
                 1W3L  1WC2  1WZZ  2A39  2A3H  2BOD  2BOE  2BOF  2BOG  2BV9  
                 2BVD  2BW8  2BWA  2BWC  2CIP  2CIT  2CKR  2CKS  2DEP  2E0P  
                 2E4T  2EEX  2EJ1  2ENG  2EO7  2EQD  2JEM  2JEN  2NLR  2OVW  
                 2UWA  2UWB  2UWC  2V38  2V3G  3A3H  3ENG  3OVW  3TF4  4A3H  
                 4ENG  4OVW  4TF4  5A3H  6A3H  7A3H  8A3H  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.4
            ExPASy - ENZYME nomenclature database: 3.2.1.4
            ExplorEnz - The Enzyme Database: 3.2.1.4
            ERGO genome analysis and discovery system: 3.2.1.4
            BRENDA, the Enzyme Database: 3.2.1.4
            CAS: 9012-54-8
///
ENTRY       EC 3.2.1.5        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
COMMENT     Deleted entry: licheninase (EC 3.2.1.5 created 1961, deleted 1964)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.5
            ExPASy - ENZYME nomenclature database: 3.2.1.5
            ExplorEnz - The Enzyme Database: 3.2.1.5
            ERGO genome analysis and discovery system: 3.2.1.5
            BRENDA, the Enzyme Database: 3.2.1.5
///
ENTRY       EC 3.2.1.6                  Enzyme
NAME        endo-1,3(4)-beta-glucanase;
            endo-1,3-beta-D-glucanase;
            laminarinase;
            laminaranase;
            beta-1,3-glucanase;
            beta-1,3-1,4-glucanase;
            endo-1,3-beta-glucanase;
            endo-beta-1,3(4)-glucanase;
            endo-beta-1,3-1,4-glucanase;
            endo-beta-(1->3)-D-glucanase;
            endo-1,3-1,4-beta-D-glucanase;
            endo-beta-(1-3)-D-glucanase;
            endo-beta-1,3-glucanase IV;
            endo-1,3-beta-D-glucanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,3-(1,3;1,4)-beta-D-glucan 3(4)-glucanohydrolase
REACTION    Endohydrolysis of 1,3- or 1,4-linkages in beta-D-glucans when the
            glucose residue whose reducing group is involved in the linkage to
            be hydrolysed is itself substituted at C-3
COMMENT     Substrates include laminarin, lichenin and cereal D-glucans;
            different from EC 3.2.1.52 beta-N-acetylhexosaminidase.
REFERENCE   1  [PMID:5354264]
  AUTHORS   Barras DR, Stone BA.
  TITLE     Beta-1,3-glucan hydrolases from Euglena gracilis. I. The nature of
            the hydrolases.
  JOURNAL   Biochim. Biophys. Acta. 191 (1969) 329-41.
  ORGANISM  Euglena gracilis
REFERENCE   2  [PMID:5354265]
  AUTHORS   Barras DR, Stone BA.
  TITLE     Beta-1,3-glucan hydrolases from Euglena gracilis. II. Purification
            and properties of the beta-1,3-glucan exo-hydrolase.
  JOURNAL   Biochim. Biophys. Acta. 191 (1969) 342-53.
  ORGANISM  Euglena gracilis
REFERENCE   3
  AUTHORS   Cunningham, L.W. and Manners, D.J.
  TITLE     Enzymic degradation of lichenin.
  JOURNAL   Biochem. J. 80 (1961) 42.
REFERENCE   4
  AUTHORS   Reese, E.T. and Mandels, M.
  TITLE     beta-D-1,3-Glucanases in fungi.
  JOURNAL   Can. J. Microbiol. 5 (1959) 173-185.
  ORGANISM  Rhizopus arrhizus, Triticum aestivum [GN:etae], Hordeum vulgare
            [GN:ehvu], Secale cereale, marine algae
REFERENCE   5  [PMID:5500926]
  AUTHORS   Sova VV, Elyakova LA, Vaskovsky VE.
  TITLE     Purification and some properties of beta-1,3-glucan glucanohydrolase
            from the crystalline style of bivalvia, Spisula sachalinensis.
  JOURNAL   Biochim. Biophys. Acta. 212 (1970) 111-5.
  ORGANISM  Spisula sachalinensis
ORTHOLOGY   KO: K01180  endo-1,3(4)-beta-glucanase
GENES       AFM: AFUA_1G04260 AFUA_1G05290 AFUA_3G03080 AFUA_4G13360
                 AFUA_5G02280 AFUA_5G13990 AFUA_5G14030 AFUA_6G14540
            PFA: PFL0285w
            BCL: ABC2683 ABC2776
            OIH: OB2143
            HWA: HQ2923A(celM)
            NPH: NP4306A(celM)
STRUCTURES  PDB: 1UP4  1UP6  1UP7  2CL2  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.6
            ExPASy - ENZYME nomenclature database: 3.2.1.6
            ExplorEnz - The Enzyme Database: 3.2.1.6
            ERGO genome analysis and discovery system: 3.2.1.6
            BRENDA, the Enzyme Database: 3.2.1.6
            CAS: 62213-14-3
///
ENTRY       EC 3.2.1.7                  Enzyme
NAME        inulinase;
            inulase;
            indoinulinase;
            endo-inulinase;
            exoinulinase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     2,1-beta-D-fructan fructanohydrolase
REACTION    Endohydrolysis of 2,1-beta-D-fructosidic linkages in inulin
REFERENCE   1
  AUTHORS   Adams, M., Richtmyer, N.K. and Hudson, C.S.
  TITLE     Some enzymes present in highly purified invertase preparations; a
            contribution to the study of fructofuranosidases, galactosidases,
            glucosidases and mannosidases.
  JOURNAL   J. Am. Chem. Soc. 65 (1943) 1369-1380.
  ORGANISM  Aspergillus niger
GENES       ANG: An11g03200(inuA)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.7
            ExPASy - ENZYME nomenclature database: 3.2.1.7
            ExplorEnz - The Enzyme Database: 3.2.1.7
            ERGO genome analysis and discovery system: 3.2.1.7
            BRENDA, the Enzyme Database: 3.2.1.7
            CAS: 9025-67-6
///
ENTRY       EC 3.2.1.8                  Enzyme
NAME        endo-1,4-beta-xylanase;
            endo-(1->4)-beta-xylan 4-xylanohydrolase;
            endo-1,4-xylanase;
            xylanase;
            beta-1,4-xylanase;
            endo-1,4-xylanase;
            endo-beta-1,4-xylanase;
            endo-1,4-beta-D-xylanase;
            1,4-beta-xylan xylanohydrolase;
            beta-xylanase;
            beta-1,4-xylan xylanohydrolase;
            endo-1,4-beta-xylanase;
            beta-D-xylanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,4-beta-D-xylan xylanohydrolase
REACTION    Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans
REFERENCE   1  [PMID:14403433]
  AUTHORS   HOWARD BH, JONES G, PURDOM MR.
  TITLE     The pentosanases of some rumen bacteria.
  JOURNAL   Biochem. J. 74 (1960) 173-80.
  ORGANISM  Triticum aestivum [GN:etae]
REFERENCE   2
  AUTHORS   Whistler, R.L. and Masek, E.
  TITLE     Enzymatic hydolysis of xylan.
  JOURNAL   J. Am. Chem. Soc. 77 (1955) 1241-1243.
  ORGANISM  Aspergillus foetidus
ORTHOLOGY   KO: K01181  endo-1,4-beta-xylanase
GENES       PIC: PICST_35732(XYN1)
            ANI: AN1818.2
            AFM: AFUA_3G00320 AFUA_3G00470 AFUA_4G09480 AFUA_6G12210
                 AFUA_6G13610
            AOR: AO090103000423 AO090701000887
            ANG: An03g00940(xynA)
            UMA: UM03411.1 UM06350.1
            ECI: UTI89_C4270(yieL)
            XCC: XCC4115(xynA) XCC4118(xynB)
            XCB: XC_4207 XC_4210
            XCV: XCV4355(xynA) XCV4358(xynB2) XCV4360(xynB3)
            XAC: XAC4249(xynA) XAC4252(xynB) XAC4254(xynB)
            XOO: XOO4428 XOO4429
            XOM: XOO_4171(XOO4171) XOO_4172(XOO4172)
            PSB: Psyr_4508
            PSP: PSPPH_4536
            PAT: Patl_2657
            SDE: Sde_2633 Sde_2934
            ATU: Atu2371(xynA)
            ATC: AGR_C_4304
            RET: RHE_CH03212(pssT1)
            RLE: RL3642
            BJA: bll2241(xynA)
            RPC: RPC_0668
            CCR: CC_2803 CC_3042
            SUS: Acid_2681 Acid_4394
            BSU: BG10808(xynA)
            BHA: BH0899 BH2120
            BAY: RBAM_018150(xynD) RBAM_033790(xynA)
            BPU: BPUM_1748(xynD)
            LSL: LSL_1486(aes)
            CBE: Cbei_3041
            CSC: Csac_0696 Csac_2405 Csac_2408
            MUL: MUL_0371 MUL_2210
            SCO: SCO0105(SCJ11.34c) SCO0674(xysA)
            SMA: SAV4984
            CMI: CMM_1673(xysA) CMM_1674(xysB)
            TFU: Tfu_1213 Tfu_2791 Tfu_2923
            ACE: Acel_0372
            KRA: Krad_0550 Krad_1068 Krad_2548
            RBA: RB10416(xynB) RB3550 RB4024 RB5243(xynB) RB8823(xynE)
                 RB9136(xlnC) RB9911
            SYC: syc0155_d
            SYF: Synpcc7942_1400
            ANA: alr4448
            AVA: Ava_1373
            CHU: CHU_2105(xynT)
            FJO: Fjoh_1996 Fjoh_2079 Fjoh_3866
            TMA: TM0061 TM0070
            TPT: Tpet_0854 Tpet_0863
STRUCTURES  PDB: 1AXK  1B30  1B31  1B3V  1B3W  1B3X  1B3Y  1B3Z  1BCX  1BG4  
                 1BK1  1BVV  1C5H  1C5I  1CLX  1E0V  1E0W  1E0X  1E5B  1E5C  
                 1E5N  1E8R  1ENX  1EXP  1F5J  1GKK  1GKL  1GMM  1GNY  1GOK  
                 1GOM  1GOO  1GOQ  1GOR  1H12  1H13  1H14  1H1A  1H4G  1H4H  
                 1HEH  1HEJ  1HIX  1HIZ  1HV0  1HV1  1I1W  1I1X  1I82  1I8A  
                 1I8U  1IGO  1ISV  1ISW  1ISX  1ISY  1ISZ  1IT0  1JJF  1JT2  
                 1K42  1K45  1K6A  1KNL  1KNM  1M4W  1MC9  1N82  1NOF  1NQ6  
                 1O8P  1O8S  1OD8  1OHZ  1PVX  1QH6  1QH7  1QLD  1R85  1R86  
                 1R87  1RED  1REE  1REF  1T6E  1T6G  1TA3  1TE1  1TUX  1UKR  
                 1UQY  1UQZ  1UR1  1UR2  1US2  1US3  1UXX  1V0K  1V0L  1V0M  
                 1V0N  1V6U  1V6V  1V6W  1V6X  1V6Y  1VBR  1VBU  1W0N  1W2P  
                 1W2V  1W32  1W3H  1WB4  1WB5  1WB6  1XAS  1XBD  1XNB  1XNC  
                 1XND  1XNK  1XW2  1XWQ  1XWT  1XXN  1XYF  1XYN  1XYO  1XYP  
                 1XYS  1XYZ  1YNA  2A8Z  2B42  2B45  2B46  2B4F  2BNJ  2BVV  
                 2C1F  2CCL  2D1Z  2D20  2D22  2D23  2D24  2D97  2D98  2DCJ  
                 2DCK  2DCY  2DCZ  2DEP  2DFB  2DFC  2F6B  2F8Q  2FGL  2G3I  
                 2G3J  2G4F  2XBD  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.8
            ExPASy - ENZYME nomenclature database: 3.2.1.8
            ExplorEnz - The Enzyme Database: 3.2.1.8
            ERGO genome analysis and discovery system: 3.2.1.8
            BRENDA, the Enzyme Database: 3.2.1.8
            CAS: 9025-57-4
///
ENTRY       EC 3.2.1.9        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
COMMENT     Deleted entry: amylopectin-1,6-glucosidase (EC 3.2.1.9 created 1961,
            deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.9
            ExPASy - ENZYME nomenclature database: 3.2.1.9
            ExplorEnz - The Enzyme Database: 3.2.1.9
            ERGO genome analysis and discovery system: 3.2.1.9
            BRENDA, the Enzyme Database: 3.2.1.9
///
ENTRY       EC 3.2.1.10                 Enzyme
NAME        oligo-1,6-glucosidase;
            limit dextrinase (erroneous);
            isomaltase;
            sucrase-isomaltase;
            exo-oligo-1,6-glucosidase;
            dextrin 6alpha-glucanohydrolase;
            alpha-limit dextrinase;
            dextrin 6-glucanohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     oligosaccharide alpha-1,6-glucohydrolase
REACTION    Hydrolysis of 1,6-alpha-D-glucosidic linkages in some
            oligosaccharides produced from starch and glycogen by
            internal_xref(ec_num(3,2,1,1)) (alpha-amylase), and in isomaltose
ALL_REAC    (other) R01718 R01791 R06080(G) R06199(G)
COMMENT     This enzyme, like EC 3.2.1.33 (amylo-alpha-1,6-glucosidase), can
            release an alpha-1->6-linked glucose, whereas the shortest chain
            that can be released by EC 3.2.1.41 (pullulanase), EC 3.2.1.142
            (limit dextrinase), and EC 3.2.1.68 (isoamylase) is maltose. It also
            hydrolyses isomaltulose (palatinose), isomaltotriose and panose, but
            has no action on glycogen or phosphorylase limit dextrin. The enzyme
            from intestinal mucosa is a single polypeptide chain that also
            catalyses the reaction of EC 3.2.1.48 (sucrose alpha-glucosidase).
            Differs from EC 3.2.1.33 (amylo-alpha-1,6-glucosidase) in its
            preference for short-chain substrates and in its not requiring the
            6-glucosylated residue to be at a branch point, i.e. linked at both
            C-1 and C-4.
REFERENCE   1  [PMID:291933]
  AUTHORS   Hauri HP, Quaroni A, Isselbacher KJ.
  TITLE     Biogenesis of intestinal plasma membrane: posttranslational route
            and cleavage of sucrase-isomaltase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 5183-6.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:7002920]
  AUTHORS   Sjostrom H, Noren O, Christiansen L, Wacker H, Semenza G.
  TITLE     A fully active, two-active-site, single-chain sucrase.isomaltase
            from pig small intestine. Implications for the biosynthesis of a
            mammalian integral stalked membrane protein.
  JOURNAL   J. Biol. Chem. 255 (1980) 11332-8.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:6479163]
  AUTHORS   Rodriguez IR, Taravel FR, Whelan WJ.
  TITLE     Characterization and function of pig intestinal sucrase-isomaltase
            and its separate subunits.
  JOURNAL   Eur. J. Biochem. 143 (1984) 575-82.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01182  oligo-1,6-glucosidase
GENES       HSA: 6476(SI)
            PTR: 470988(SI)
            MMU: 69983(2010204N08Rik)
            RNO: 497756(Si)
            CFA: 488141(SI)
            EHI: 258.t00009 337.t00007
            VVU: VV2_0256
            VVY: VVA0760
            PPR: PBPRB0410(dexA)
            NMU: Nmul_A1251
            RET: RHE_CH03282(malL)
            BSU: BG12421(malL) BG12762(ycdG)
            BHA: BH2903
            BAN: BA4231(malL)
            BAR: GBAA4231(malL)
            BAA: BA_4692
            BAT: BAS3924
            BCE: BC4015
            BCA: BCE_4066(malL)
            BCZ: BCZK3772(malL)
            BTK: BT9727_3756(malL)
            BTL: BALH_3635(malL)
            BLI: BL00491(malL)
            BLD: BLi00664(malL)
            BAY: RBAM_003100(ycdG)
            OIH: OB2556
            SHA: SH0072(malL)
            LMO: lmo0184
            LMF: LMOf2365_0195(malL-1) LMOf2365_0270(malL-2)
            LIN: lin0223
            LWE: lwe0225(malL)
            LLA: L128693(dexA)
            LLM: llmg_0741(dexA)
            LPL: lp_3627(agl6)
            LJO: LJ0743
            LSL: LSL_1712
            LCA: LSEI_0406
            LGA: LGAS_0518
            OOE: OEOE_0040
            CDF: CD0468(malL)
            CBO: CBO1604(malL)
            CKL: CKL_1598(malL)
            MPU: MYPU_1030 MYPU_6330
            MSY: MS53_0108
            BLO: BL1526(agl)
            BAD: BAD_1571(agl)
            RBA: RB2986
            TDE: TDE0107
            LIL: LA1466
STRUCTURES  PDB: 1UOK  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.10
            ExPASy - ENZYME nomenclature database: 3.2.1.10
            ExplorEnz - The Enzyme Database: 3.2.1.10
            ERGO genome analysis and discovery system: 3.2.1.10
            BRENDA, the Enzyme Database: 3.2.1.10
            CAS: 9032-15-9
///
ENTRY       EC 3.2.1.11                 Enzyme
NAME        dextranase;
            dextran hydrolase;
            endodextranase;
            dextranase DL 2;
            DL 2;
            endo-dextranase;
            alpha-D-1,6-glucan-6-glucanohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,6-alpha-D-glucan 6-glucanohydrolase
REACTION    Endohydrolysis of 1,6-alpha-D-glucosidic linkages in dextran
REFERENCE   1  [PMID:13651134]
  AUTHORS   BAILEY RW, CLARKE RT.
  TITLE     A bacterial dextranase.
  JOURNAL   Biochem. J. 72 (1959) 49-54.
  ORGANISM  Lactobacillus bifidus
REFERENCE   2
  AUTHORS   Deuel, H. and Stutz, E.
  TITLE     Pectic substances and pectic enzymes.
  JOURNAL   Adv. Enzymol. Relat. Areas Mol. Biol. 20 (1958) 341-382.
REFERENCE   3
  AUTHORS   Fischer, E.H. and Stein, E.A.
  TITLE     Cleavage of O- and S-glycosidic bonds (survey).
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 301-312.
REFERENCE   4
  AUTHORS   Rozenfel'd, E.L. and Lukomskaya, I.S.
  TITLE     [The hydrolysis of 1:6 bonds of dextran by animal tissues.].
  JOURNAL   Biokhimiya 21 (1956) 412-415.
ORTHOLOGY   KO: K05988  
GENES       SMU: SMU.2042(dexA)
STRUCTURES  PDB: 1OGM  1OGO  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.11
            ExPASy - ENZYME nomenclature database: 3.2.1.11
            ExplorEnz - The Enzyme Database: 3.2.1.11
            ERGO genome analysis and discovery system: 3.2.1.11
            BRENDA, the Enzyme Database: 3.2.1.11
            CAS: 9025-70-1
///
ENTRY       EC 3.2.1.12       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
COMMENT     Deleted entry: cycloheptaglucanase. Now included with EC 3.2.1.54
            cyclomaltodextrinase (EC 3.2.1.12 created 1961, deleted 1976)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.12
            ExPASy - ENZYME nomenclature database: 3.2.1.12
            ExplorEnz - The Enzyme Database: 3.2.1.12
            ERGO genome analysis and discovery system: 3.2.1.12
            BRENDA, the Enzyme Database: 3.2.1.12
///
ENTRY       EC 3.2.1.13       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
COMMENT     Deleted entry: cyclohexaglucanase. Now included with EC 3.2.1.54
            cyclomaltodextrinase (EC 3.2.1.13 created 1961, deleted 1976)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.13
            ExPASy - ENZYME nomenclature database: 3.2.1.13
            ExplorEnz - The Enzyme Database: 3.2.1.13
            ERGO genome analysis and discovery system: 3.2.1.13
            BRENDA, the Enzyme Database: 3.2.1.13
///
ENTRY       EC 3.2.1.14                 Enzyme
NAME        chitinase;
            chitodextrinase;
            1,4-beta-poly-N-acetylglucosaminidase;
            poly-beta-glucosaminidase;
            beta-1,4-poly-N-acetyl glucosamidinase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     poly[1,4-(N-acetyl-beta-D-glucosaminide)] glycanohydrolase
REACTION    Random hydrolysis of N-acetyl-beta-D-glucosaminide 1,4-beta-linkages
            in chitin and chitodextrins
ALL_REAC    (other) R01206 R02334 R06081(G) R06082(G)
INHIBITOR   Allosamidine [CPD:C05346]
COMMENT     Some chitinases also display the activity defined in EC 3.2.1.17
            lysozyme.
REFERENCE   1
  AUTHORS   Fischer, E.H. and Stein, E.A.
  TITLE     Cleavage of O- and S-glycosidic bonds (survey).
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 301-312.
REFERENCE   2
  AUTHORS   Tracey, M.V.
  TITLE     Chitinase in some basidiomycetes.
  JOURNAL   Biochem. J. 61 (1955) 579-586.
  ORGANISM  Lycoperdon sp.
REFERENCE   3
  AUTHORS   Zechmeister, L. and Toth, G.
  TITLE     Chromatographic adsorption of the enzymes of emulsin which act on
            chitins.
  JOURNAL   Enzymologia 7 (1939) 165-169.
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K01183  chitinase
GENES       HSA: 1118(CHIT1) 27159(CHIA)
            MMU: 71884(Chit1) 81600(Chia)
            CFA: 479904(CHIA)
            BTA: 282645(CHIA)
            GGA: 395072(CHIA)
            XLA: 444170(MGC80644)
            XTR: 448265(chit1)
            DRE: 322420(zgc:65788)
            DME: Dmel_CG1780(Idgf4) Dmel_CG18140(Cht3) Dmel_CG2054(Cht2)
                 Dmel_CG3986(Cht4) Dmel_CG4472(Idgf1) Dmel_CG4475(Idgf2)
                 Dmel_CG4559(Idgf3) Dmel_CG5154(Idgf5) Dmel_CG5210(Chit)
            CEL: C04F6.3(cht-1)
            ATH: AT3G12500(ATHCHIB) AT3G54420(ATEP3) AT5G24090
            OSA: 4323899 4324117 4325067 4329920 4336263 4336265 4338718
                 4338719
            SCE: YLR286C(CTS1)
            PIC: PICST_31390(CHT4) PICST_48142(CHT2) PICST_68871(CHT3)
                 PICST_91537(CHT1)
            CGR: CAGL0A02904g CAGL0M09779g
            AFM: AFUA_1G00310 AFUA_1G02800 AFUA_3G07110 AFUA_3G07160
                 AFUA_3G11280 AFUA_5G01400 AFUA_5G03530 AFUA_5G03760
                 AFUA_5G03850 AFUA_5G03960 AFUA_5G06840 AFUA_6G09310
                 AFUA_6G09780 AFUA_6G13720 AFUA_7G05140 AFUA_7G08490
                 AFUA_8G00700 AFUA_8G01410
            AOR: AO090003000464 AO090023000367
            PFA: PFL2510w
            TET: TTHERM_00196530 TTHERM_00527400 TTHERM_00569420
                 TTHERM_00794490 TTHERM_01433580
            EHI: 128.t00013
            ECO: b3338(chiA)
            ECJ: JW3300(chiA)
            ECC: c4109(chiA)
            ECI: UTI89_C1846(ydhO) UTI89_C3793(yheB)
            ECV: APECO1_3115(yheB)
            ECX: EcHS_A3533(chiA)
            SSN: SSON_1501(ydhO)
            SPE: Spro_0137 Spro_3476
            VCH: VC1952 VCA0027
            VCO: VC0395_0106(chiA-2) VC0395_0638
            VVU: VV1_1833 VV2_1217
            VVY: VV2578 VVA0044 VVA0045
            VPA: VP2338 VPA0055
            VFI: VF0655 VF0986 VF1598
            PSP: PSPPH_0470
            PFL: PFL_2091
            PEN: PSEEN2568(chiC)
            SDN: Sden_2136 Sden_3140
            SBL: Sbal_2491 Sbal_3083
            SHE: Shewmr4_2805
            SHM: Shewmr7_2888
            SHN: Shewana3_2984
            SDE: Sde_3870 Sde_3982
            FTU: FTT1768c
            FTF: FTF1768c
            FTL: FTL_0093
            FTH: FTH_0088
            FTN: FTN_1744(chiB)
            HCH: HCH_00869
            AHA: AHA_0977 AHA_3440
            CVI: CV_4240
            BUR: Bcep18194_A4818
            BCN: Bcen_1190
            BCH: Bcen2424_1670
            BAM: Bamb_1428 Bamb_1569
            BPM: BURPS1710b_2109(chiC)
            BTE: BTH_I2402
            MXA: MXAN_4534 MXAN_6008
            BHA: BH0916
            BAN: BA0385 BA3854(chi36)
            BAR: GBAA0385 GBAA3854(chi36)
            BAA: BA_0961 BA_4327
            BAT: BAS0371 BAS3571
            BCE: BC0429 BC3725
            BCA: BCE_0497 BCE_3753(chi36)
            BCZ: BCZK0359(chiA) BCZK3483(chiA) pE33L466_0276(chbA)
            BTK: BT9727_0362(chiA) BT9727_3469(chiA)
            BTL: BALH_0385(chiA) BALH_2510(chb)
            BLI: BL01685(yvbX)
            BLD: BLi00338 BLi00339
            BCL: ABC0646
            OIH: OB0791
            SAA: SAUSA300_0964
            LMF: LMOf2365_0123(chiB)
            LWE: lwe0093
            LLM: llmg_2199(chiC)
            LBR: LVIS_1777
            CPR: CPR_0949
            CBO: CBO1057(chiD) CBO2832
            CBA: CLB_1097
            CBH: CLC_1109
            CBF: CLI_1149
            MTU: Rv1987
            MBO: Mb2009
            MVA: Mvan_3505
            MGI: Mflv_3001
            MMC: Mmcs_3355
            MKM: Mkms_3417
            MJL: Mjls_3366
            ART: Arth_1229
            TFU: Tfu_0580
            ACE: Acel_2033
            SEN: SACE_3887(chiC) SACE_5287(chiC) SACE_6557 SACE_6558
            STP: Strop_4405
            CTA: CTA_0134(ydhO)
            SRU: SRU_2812
STRUCTURES  PDB: 1CNS  1CTN  1D2K  1DXJ  1E6Z  1ED7  1EDQ  1EHN  1EIB  1FFQ  
                 1FFR  1GOI  1GPF  1H0G  1H0I  1HKI  1HKJ  1HKK  1HKM  1HVQ  
                 1ITX  1K85  1K9T  1KFW  1KQY  1KQZ  1KR0  1KR1  1LL4  1LL6  
                 1LL7  1LLO  1NH6  1O6I  1OGB  1OGG  1RD6  1UR8  1UR9  1W1P  
                 1W1T  1W1V  1W1Y  1W9P  1W9U  1W9V  1WAW  1WB0  1WNO  1WVU  
                 1WVV  1X6L  1X6N  2A3A  2A3B  2A3C  2A3E  2CJL  2CWR  2CZN  
                 2D49  2DBT  2DKV  2DSK  2HVM  2IUZ  2UY2  2UY3  2UY4  2UY5  
                 2Z37  2Z38  2Z39  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.14
            ExPASy - ENZYME nomenclature database: 3.2.1.14
            ExplorEnz - The Enzyme Database: 3.2.1.14
            ERGO genome analysis and discovery system: 3.2.1.14
            BRENDA, the Enzyme Database: 3.2.1.14
            CAS: 9001-06-3
///
ENTRY       EC 3.2.1.15                 Enzyme
NAME        polygalacturonase;
            pectin depolymerase;
            pectinase;
            endopolygalacturonase;
            pectolase;
            pectin hydrolase;
            pectin polygalacturonase;
            endo-polygalacturonase;
            poly-alpha-1,4-galacturonide glycanohydrolase;
            endogalacturonase;
            endo-D-galacturonase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     poly(1,4-alpha-D-galacturonide) glycanohydrolase
REACTION    Random hydrolysis of 1,4-alpha-D-galactosiduronic linkages in
            pectate and other galacturonans
ALL_REAC    (other) R01982 R02360 R06201(G) R06239(G)
REFERENCE   1
  AUTHORS   Deuel, H. and Stutz, E.
  TITLE     Pectic substances and pectic enzymes.
  JOURNAL   Adv. Enzymol. Relat. Areas Mol. Biol. 20 (1958) 341-382.
REFERENCE   2
  AUTHORS   Lineweaver, H. and Jansen, E.F.
  TITLE     Pectic enzymes.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 267-295.
REFERENCE   3  [PMID:13159344]
  AUTHORS   McCREADY RM, SEEGMILLER CG.
  TITLE     Action of pectic enzymes on oligogalacturonic acids and some of
            their derivatives.
  JOURNAL   Arch. Biochem. Biophys. 50 (1954) 440-50.
  ORGANISM  Aspergillus niger
REFERENCE   4
  AUTHORS   Mill, P.J. and Tuttobello, R.
  TITLE     The pectic enzymes of Aspergillus niger. 2. Endopolygalacturonase.
  JOURNAL   Biochem. J. 79 (1961) 57-64.
  ORGANISM  Aspergillus niger
REFERENCE   5
  AUTHORS   Phaff, H.J. and Demain, A.L.
  TITLE     The unienzymatic nature of yeast polygalacturonase.
  JOURNAL   J. Biol. Chem. 218 (1956) 875-884.
  ORGANISM  Aspergillus niger
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01184  polygalacturonase
GENES       ATH: AT3G59850
            SCE: YJR153W(PGU1)
            AGO: AGOS_ADR327W
            ANI: AN4372.2 AN6656.2
            AFM: AFUA_1G17220 AFUA_4G13920 AFUA_8G01970
            AOR: AO090005000186 AO090023000161 AO090023000401
            ANG: An01g11520(pgaI) An01g14670(pgaE) An02g04900(pgaB)
                 An05g02440(pgaC) An09g03260(pgaD) An12g00950(rhgA)
                 An15g05370(pgaII) An16g06990(pgaA)
            UMA: UM02510.1
            ECA: ECA1095(pehA)
            XFT: PD1485(pglA)
            XCC: XCC2266(pglA) XCC3459(peh-1)
            XCB: XC_0705 XC_1849
            XCV: XCV0722(pgl) XCV2571
            XAC: XAC0661(peh-1) XAC2374(pglA)
            XOO: XOO2699(pglA)
            XOM: XOO_2545(XOO2545) XOO_3737(XOO3737)
            PST: PSPTO_3960(pglA)
            PSP: PSPPH_1530 PSPPH_A0006 PSPPH_A0072
            RSO: RSp0880(pglA)
            LXX: Lxx07750(pglA)
STRUCTURES  PDB: 1BHE  1CZF  1IA5  1IB4  1K5C  1KCC  1KCD  1NHC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.15
            ExPASy - ENZYME nomenclature database: 3.2.1.15
            ExplorEnz - The Enzyme Database: 3.2.1.15
            ERGO genome analysis and discovery system: 3.2.1.15
            BRENDA, the Enzyme Database: 3.2.1.15
            CAS: 9032-75-1
///
ENTRY       EC 3.2.1.16       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
COMMENT     Deleted entry: alginase (EC 3.2.1.16 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.16
            ExPASy - ENZYME nomenclature database: 3.2.1.16
            ExplorEnz - The Enzyme Database: 3.2.1.16
            ERGO genome analysis and discovery system: 3.2.1.16
            BRENDA, the Enzyme Database: 3.2.1.16
///
ENTRY       EC 3.2.1.17                 Enzyme
NAME        lysozyme;
            muramidase;
            globulin G;
            mucopeptide glucohydrolase;
            globulin G1;
            N,O-diacetylmuramidase;
            lysozyme g;
            L-7001;
            1,4-N-acetylmuramidase;
            mucopeptide N-acetylmuramoylhydrolase;
            PR1-lysozyme
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     peptidoglycan N-acetylmuramoylhydrolase
REACTION    Hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and
            N-acetyl-D-glucosamine residues in a peptidoglycan and between
            N-acetyl-D-glucosamine residues in chitodextrins
COMMENT     cf. also EC 3.2.1.14 chitinase.
REFERENCE   1  [PMID:4382801]
  AUTHORS   Blake CC, Johnson LN, Mair GA, North AC, Phillips DC, Sarma VR.
  TITLE     Crystallographic studies of the activity of hen egg-white lysozyme.
  JOURNAL   Proc. R. Soc. Lond. B. Biol. Sci. 167 (1967) 378-88.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:4382800]
  AUTHORS   Blake CC, Mair GA, North AC, Phillips DC, Sarma VR.
  TITLE     On the conformation of the hen egg-white lysozyme molecule.
  JOURNAL   Proc. R. Soc. Lond. B. Biol. Sci. 167 (1967) 365-77.
  ORGANISM  chicken [GN:gga]
REFERENCE   3
  AUTHORS   Jolles, P.
  TITLE     Lysozyme.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 431-445.
ORTHOLOGY   KO: K01185  lysozyme
GENES       HSA: 4069(LYZ)
            PTR: 450190(LYZ)
            MMU: 17105(Lyzs) 17110(Lyz)
            RNO: 25211(Lyz)
            CFA: 474442(LYZ)
            BTA: 281287(LYZ1) 281289(LYZ3) 777776(LYS)
            SSC: 397685(LYZ)
            GGA: 396218(LYZ)
            XTR: 448362(MGC89221)
            DME: Dmel_CG1165(LysS) Dmel_CG1179(LysB) Dmel_CG1180(LysE)
                 Dmel_CG7798 Dmel_CG9111(LysC) Dmel_CG9116(LysP)
                 Dmel_CG9118(LysD) Dmel_CG9120(LysX)
            TET: TTHERM_00024350 TTHERM_00024410 TTHERM_00083410
                 TTHERM_00083420 TTHERM_00666790 TTHERM_01243480
                 TTHERM_01250150
            ECO: b1554(ydfQ) b3338(chiA)
            ECJ: JW0544(ybcS) JW3300(chiA)
            ECE: Z0960
            ECS: ECs0819
            ECC: c1436 c1562(ybcS) c3180 c4109(chiA)
            ECI: UTI89_C1303(ybcS1) UTI89_C1490 UTI89_C2660 UTI89_C3793(yheB)
                 UTI89_C5112(ybcS2)
            ECP: ECP_1160
            ECV: APECO1_1029 APECO1_2033(ydfQ) APECO1_242(ybcS2)
                 APECO1_3115(yheB) APECO1_392 APECO1_4196 APECO1_514
            ECW: EcE24377A_0827
            ECX: EcHS_A0304 EcHS_A0931 EcHS_A1644 EcHS_A3533(chiA)
            STY: STY2044 STY4620(nucD2)
            STT: t4314(nucD)
            SPT: SPA2575(nucD)
            SEC: SC0986(lycV) SC2614(lycV)
            STM: STM1028
            YPE: YPO2098
            YPN: YPN_1570
            YPS: YPTB1755 YPTB1805
            YPI: YpsIP31758_2206
            YEN: YE1840
            SFV: SFV_0212 SFV_0279 SFV_0726(ybcS) SFV_2706
            SSN: SSON_0733 SSON_2437 SSON_2783(ybcS)
            SBO: SBO_0765 SBO_1924
            SGL: SG0728 SG1559 SG1671 SG1681
            ENT: Ent638_2248 Ent638_2609
            SPE: Spro_0884 Spro_1899
            HIT: NTHI1880
            ASU: Asuc_0036 Asuc_1839
            XFA: XF2314
            XFT: PD1113
            XAC: XAC1063(p13)
            PAP: PSPA7_0693 PSPA7_5063
            PPF: Pput_0663 Pput_3808
            PMY: Pmen_0969 Pmen_1620
            PRW: PsycPRwf_0480 PsycPRwf_1572
            ACI: ACIAD0226
            SON: SO_0659
            SDN: Sden_3256
            SBM: Shew185_1086 Shew185_1708
            SSE: Ssed_2633 Ssed_3499
            SPL: Spea_2503 Spea_3166
            PHA: PSHAa1967(mltD)
            CBU: CBU_1031
            CBD: COXBU7E912_1015
            MCA: MCA2680
            MMW: Mmwyl1_2303 Mmwyl1_3611
            AHA: AHA_2050
            CVI: CV_0727 CV_1253(mltD) CV_1609(mltB) CV_2034(sltY)
                 CV_2611(slt) CV_3759(mltA)
            RSO: RSc0883(RS04859) RSc3192(RS02409)
            REH: H16_B1313
            BAM: Bamb_4258
            BPM: BURPS1710b_1695
            BTE: BTH_I1920
            MMS: mma_2788
            NEU: NE2534
            ABU: Abu_1520
            GUR: Gura_0881
            DDE: Dde_3421
            AFW: Anae109_0059 Anae109_0212 Anae109_1958 Anae109_3442
            RCO: RC1298
            PLA: Plav_2164
            SMD: Smed_2613
            RET: RHE_CH01113(ypch00360)
            RLE: RL3328 RL3920
            BME: BMEI0562 BMEII0782
            OAN: Oant_1237
            BBK: BARBAKC583_0240 BARBAKC583_1057
            XAU: Xaut_1985
            RSQ: Rsph17025_1573
            SWI: Swit_0061
            ACR: Acry_0164 Acry_2719
            MAG: amb1525
            BCE: BC3441
            BCY: Bcer98_0916 Bcer98_1014 Bcer98_2541
            SAJ: SaurJH9_1256
            SAH: SaurJH1_1281
            LLA: L68758(acmA)
            SPH: MGAS10270_Spy0722(mur1-1) MGAS10270_Spy0723(mur1-2)
            SPI: MGAS10750_Spy0754(mur1-1) MGAS10750_Spy0755(mur1-2)
            SPJ: MGAS2096_Spy0734(mur1-1) MGAS2096_Spy0735(mur1-2)
            SPK: MGAS9429_Spy0718(mur1-1) MGAS9429_Spy0719(mur1-2)
                 MGAS9429_Spy0849
            SPR: spr1431(lytC)
            LPL: lp_1138(acm1) lp_1158(lys) lp_2645(acm2) lp_3093
            LSA: LSA1538 LSA1788
            LSL: LSL_0296 LSL_0304 LSL_0797 LSL_0805 LSL_1310
            LRE: Lreu_0574 Lreu_0929 Lreu_1521
            OOE: OEOE_1199
            CAC: CAC0554(lyc)
            CPE: CPE0382
            CNO: NT01CX_2099
            CBE: Cbei_0516 Cbei_1595
            AMT: Amet_2796 Amet_3173
            CSC: Csac_1928 Csac_1959
            PAC: PPA1662
            KRA: Krad_3188
            SEN: SACE_0675 SACE_0704 SACE_3764 SACE_7138
            STP: Strop_3201
            SYG: sync_1433 sync_1864
            ANA: alr1167
            AVA: Ava_4421
            FJO: Fjoh_2620
            CCH: Cag_0702
            DEB: DehaBAV1_1186
            RRS: RoseRS_0254
            RCA: Rcas_0282
            TPT: Tpet_0458 Tpet_1802
            TME: Tmel_0919 Tmel_0989
            FNO: Fnod_1102
            MMZ: MmarC7_0252
            MVN: Mevan_0337
STRUCTURES  PDB: 107L  108L  109L  110L  111L  112L  113L  114L  115L  118L  
                 119L  120L  122L  123L  125L  126L  127L  128L  129L  130L  
                 131L  132L  133L  134L  135L  137L  138L  139L  140L  141L  
                 142L  143L  144L  145L  146L  147L  148L  149L  150L  151L  
                 152L  153L  154L  155L  156L  157L  158L  159L  160L  161L  
                 162L  163L  164L  165L  166L  167L  168L  169L  170L  171L  
                 172L  173L  174L  175L  176L  177L  178L  179L  180L  181L  
                 182L  183L  184L  185L  186L  187L  188L  189L  190L  191L  
                 192L  195L  196L  197L  198L  199L  1A2Y  1AKI  1AT5  1AT6  
                 1AZF  1B0D  1B2K  1B5U  1B5V  1B5W  1B5X  1B5Y  1B5Z  1B6I  
                 1B7L  1B7M  1B7N  1B7O  1B7P  1B7Q  1B7R  1BB3  1BB4  1BB5  
                 1BB6  1BB7  1BGI  1BHZ  1BVK  1BVX  1BWH  1BWI  1BWJ  1C10  
                 1C43  1C45  1C46  1C60  1C61  1C62  1C63  1C64  1C65  1C66  
                 1C67  1C68  1C69  1C6A  1C6B  1C6C  1C6D  1C6E  1C6F  1C6G  
                 1C6H  1C6I  1C6J  1C6K  1C6L  1C6M  1C6N  1C6P  1C6Q  1C6T  
                 1C7P  1CJ6  1CJ7  1CJ8  1CJ9  1CKC  1CKD  1CKF  1CKG  1CKH  
                 1CTW  1CU0  1CU2  1CU3  1CU5  1CU6  1CUP  1CUQ  1CV0  1CV1  
                 1CV3  1CV4  1CV5  1CV6  1CVK  1CX6  1CX7  1D2W  1D2Y  1D3F  
                 1D3J  1D3M  1D3N  1D6P  1D6Q  1D9U  1D9W  1DI3  1DI4  1DI5  
                 1DKJ  1DKK  1DPW  1DPX  1DQJ  1DYA  1DYB  1DYC  1DYD  1DYE  
                 1DYF  1DYG  1DZB  1E8L  1EL1  1EPY  1EQ4  1EQ5  1EQE  1F0W  
                 1F10  1FBI  1FDL  1FLQ  1FLU  1FLW  1FLY  1FN5  1G06  1G07  
                 1G0G  1G0J  1G0K  1G0L  1G0M  1G0P  1G0Q  1G1V  1G1W  1G7H  
                 1G7I  1G7J  1G7L  1G7M  1GAY  1GAZ  1GB0  1GB2  1GB3  1GB5  
                 1GB6  1GB7  1GB8  1GB9  1GBO  1GBS  1GBW  1GBX  1GBY  1GBZ  
                 1GD6  1GDW  1GDX  1GE0  1GE1  1GE2  1GE3  1GE4  1GEV  1GEZ  
                 1GF0  1GF3  1GF4  1GF5  1GF6  1GF7  1GF8  1GF9  1GFA  1GFE  
                 1GFG  1GFH  1GFJ  1GFK  1GFR  1GFT  1GFU  1GFV  1GHL  1GPQ  
                 1GWD  1GXV  1GXX  1H09  1H6M  1H87  1HC0  1HEL  1HEM  1HEN  
                 1HEO  1HEP  1HEQ  1HER  1HEW  1HF4  1HHL  1HNL  1HSW  1HSX  
                 1HVQ  1I22  1I56  1I6S  1IC4  1IC5  1IC7  1IEE  1IIZ  1INU  
                 1IO5  1IOC  1IOQ  1IOR  1IOS  1IP1  1IP2  1IP3  1IP4  1IP5  
                 1IP6  1IP7  1IR7  1IR8  1IR9  1IVM  1IWT  1IWU  1IWV  1IWW  
                 1IWX  1IWY  1IWZ  1IX0  1IY3  1IY4  1J1O  1J1P  1J1X  1JA2  
                 1JA4  1JA6  1JA7  1JEF  1JFX  1JIS  1JIT  1JIY  1JJ0  1JJ1  
                 1JJ3  1JKA  1JKB  1JKC  1JKD  1JPO  1JQU  1JSE  1JSF  1JTM  
                 1JTN  1JTO  1JTP  1JTT  1JUG  1JWR  1K28  1KIP  1KIQ  1KIR  
                 1KNI  1KQY  1KQZ  1KR0  1KR1  1KS3  1KW5  1KW7  1KXW  1KXX  
                 1KXY  1KY0  1KY1  1L00  1L01  1L02  1L03  1L04  1L05  1L06  
                 1L07  1L08  1L09  1L0J  1L0K  1L10  1L11  1L12  1L13  1L14  
                 1L15  1L16  1L17  1L18  1L19  1L20  1L21  1L22  1L23  1L24  
                 1L25  1L26  1L27  1L28  1L29  1L30  1L31  1L32  1L33  1L34  
                 1L35  1L36  1L37  1L38  1L39  1L40  1L41  1L42  1L43  1L44  
                 1L45  1L46  1L47  1L48  1L49  1L50  1L51  1L52  1L53  1L54  
                 1L55  1L56  1L57  1L58  1L59  1L60  1L61  1L62  1L63  1L64  
                 1L65  1L66  1L67  1L68  1L69  1L70  1L71  1L72  1L73  1L74  
                 1L75  1L76  1L77  1L79  1L80  1L81  1L82  1L83  1L84  1L85  
                 1L86  1L87  1L88  1L89  1L90  1L91  1L92  1L93  1L94  1L95  
                 1L96  1L97  1L98  1L99  1LAA  1LCN  1LGU  1LGW  1LGX  1LHH  
                 1LHI  1LHJ  1LHK  1LHL  1LHM  1LI2  1LI3  1LI6  1LJ3  1LJ4  
                 1LJE  1LJF  1LJG  1LJH  1LJI  1LJJ  1LJK  1LJN  1LKR  1LKS  
                 1LLH  1LLO  1LMA  1LMC  1LMN  1LMO  1LMP  1LMQ  1LMT  1LOZ  
                 1LPI  1LPY  1LSA  1LSB  1LSC  1LSD  1LSE  1LSF  1LSM  1LSN  
                 1LSP  1LSY  1LSZ  1LW9  1LWG  1LWK  1LYO  1LYS  1LYY  1LYZ  
                 1LZ1  1LZ4  1LZ5  1LZ6  1LZ8  1LZ9  1LZA  1LZB  1LZC  1LZD  
                 1LZE  1LZG  1LZH  1LZN  1LZR  1LZS  1LZT  1LZY  1MEL  1MII  
                 1N4F  1NBY  1NBZ  1NDG  1NDM  1NHB  1OBA  1OP9  1OUA  1OUB  
                 1OUC  1OUD  1OUE  1OUF  1OUG  1OUH  1OUI  1OUJ  1OV5  1OV7  
                 1OVH  1OVJ  1OVK  1OWY  1OWZ  1OYU  1P2C  1P2L  1P2R  1P36  
                 1P37  1P3N  1P46  1P56  1P5C  1P64  1P6Y  1P7S  1PDL  1PQD  
                 1PQI  1PQJ  1PQK  1PQM  1PQO  1PS5  1QIO  1QQY  1QS5  1QS9  
                 1QSB  1QSQ  1QT3  1QT4  1QT5  1QT6  1QT7  1QT8  1QTB  1QTC  
                 1QTD  1QTH  1QTK  1QTV  1QTZ  1QUD  1QUG  1QUH  1QUO  1RCM  
                 1RE2  1REM  1REX  1REY  1REZ  1RFP  1RI8  1RJC  1SF4  1SF6  
                 1SF7  1SFB  1SFG  1SQ2  1SSW  1SSY  1SWY  1SWZ  1SX2  1SX7  
                 1T3P  1T6H  1T6V  1T8A  1T8F  1T8G  1T97  1TAY  1TBY  1TCY  
                 1TDY  1TEW  1TLA  1UA6  1UAC  1UBZ  1UC0  1UCO  1UIA  1UIB  
                 1UIC  1UID  1UIE  1UIF  1UIG  1UIH  1UUZ  1V7S  1V7T  1VAT  
                 1VAU  1VDP  1VDQ  1VDS  1VDT  1VED  1W08  1W6Z  1WQM  1WQN  
                 1WQO  1WQP  1WQQ  1WQR  1WTH  1WTM  1WTN  1XEI  1XEJ  1XEK  
                 1XEP  1XFP  1XFT  1XGP  1XGQ  1XJT  1XJU  1YAM  1YAN  1YAO  
                 1YAP  1YAQ  1YIK  1YIL  1YKX  1YKY  1YKZ  1YL0  1YL1  1YQV  
                 1Z55  1ZMY  1ZUR  1ZV5  1ZVH  1ZVY  1ZWN  1ZYT  200L  201L  
                 205L  206L  207L  208L  209L  210L  211L  212L  213L  214L  
                 215L  216L  217L  218L  219L  220L  221L  222L  223L  224L  
                 225L  226L  227L  228L  229L  230L  231L  232L  233L  234L  
                 235L  236L  237L  238L  239L  240L  241L  242L  243L  244L  
                 245L  246L  247L  248L  249L  250L  251L  252L  253L  254L  
                 255L  256L  257L  258L  259L  260L  261L  262L  2A4T  2A6U  
                 2A7D  2A7F  2ANV  2ANX  2AUB  2B5Z  2B6T  2B6W  2B6X  2B6Y  
                 2B6Z  2B70  2B72  2B73  2B74  2B75  2B7W  2B7X  2BLX  2BLY  
                 2BPU  2BQA  2BQB  2BQC  2BQD  2BQE  2BQF  2BQG  2BQH  2BQI  
                 2BQJ  2BQK  2BQL  2BQM  2BQN  2BQO  2C8O  2C8P  2CDS  2CGI  
                 2CUU  2CWI  2D4I  2D4J  2D4K  2D6B  2D91  2DQA  2DQC  2DQD  
                 2DQE  2DQF  2DQG  2DQH  2DQI  2DQJ  2EPE  2F2N  2F2Q  2F30  
                 2F32  2F47  2F4A  2F4G  2FBB  2FBD  2G4P  2G4Q  2GV0  2H5Z  
                 2H9J  2H9K  2HEA  2HEB  2HEC  2HED  2HEE  2HEF  2HS7  2HS9  
                 2HSO  2HTX  2HU1  2HU3  2HUB  2HUK  2HUL  2HUM  2HVM  2I25  
                 2I26  2I6Z  2IGC  2IHL  2IXU  2IXV  2J8F  2J8G  2L78  2LHM  
                 2LYM  2LYO  2LYZ  2LZ2  2LZH  2LZM  2LZT  2MEA  2MEB  2MEC  
                 2MED  2MEE  2MEF  2MEG  2MEH  2MEI  2NTG  2NTH  2NW0  2NWD  
                 2O4W  2O79  2O7A  2OE4  2OE7  2OE9  2OEA  2OTY  2OTZ  2OU0  
                 2OU8  2OU9  2Q9D  2Q9E  2VB1  2YVB  3HFM  3LHM  3LYM  3LYO  
                 3LYT  3LYZ  3LZ2  3LZM  3LZT  4LYM  4LYO  4LYT  4LYZ  4LZM  
                 4LZT  5LYM  5LYT  5LYZ  5LZM  6LYT  6LYZ  6LZM  7LYZ  7LZM  
                 8LYZ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.17
            ExPASy - ENZYME nomenclature database: 3.2.1.17
            ExplorEnz - The Enzyme Database: 3.2.1.17
            ERGO genome analysis and discovery system: 3.2.1.17
            BRENDA, the Enzyme Database: 3.2.1.17
            CAS: 9001-63-2
///
ENTRY       EC 3.2.1.18                 Enzyme
NAME        exo-alpha-sialidase;
            neuraminidase;
            sialidase;
            alpha-neuraminidase;
            acetylneuraminidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     acetylneuraminyl hydrolase
REACTION    Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic
            linkages of terminal sialic acid residues in oligosaccharides,
            glycoproteins, glycolipids, colominic acid and synthetic substrates
ALL_REAC    (other) R03491 R04018 R04634 R04650 R05115 R05117 R05996(G)
            R05998(G) R05999(G) R06012(G) R06147(G) R06253(G)
INHIBITOR   2-Deoxy-2,3-dehydro-N-acetylneuraminic acid [CPD:C04580]
COMMENT     The enzyme does not act on 4-O-acetylated sialic acids.
            endo-alpha-Sialidase activity is listed as EC 3.2.1.129,
            endo-alpha-sialidase. See also EC 4.2.2.15 anhydrosialidase.
REFERENCE   1  [PMID:6762816]
  AUTHORS   Schauer R.
  TITLE     Chemistry, metabolism, and biological functions of sialic acids.
  JOURNAL   Adv. Carbohydr. Chem. Biochem. 40 (1982) 131-234.
REFERENCE   2  [PMID:1883340]
  AUTHORS   Cabezas JA.
  TITLE     Some questions and suggestions on the type references of the
            official nomenclature (IUB) for sialidase(s) and endosialidase.
  JOURNAL   Biochem. J. 278 ( Pt 1) (1991) 311-2.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00511  N-Glycan degradation
            PATH: map00600  Sphingolipid metabolism
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01186  neuraminidase
GENES       HSA: 10825(NEU3) 129807(NEU4) 4758(NEU1) 4759(NEU2)
            MMU: 18010(Neu1) 23956(Neu2) 241159(Neu4) 50877(Neu3)
            RNO: 117185(Neu3) 24591(Neu1) 29204(Neu2)
            CFA: 481717(NEU1) 485195(NEU3) 486166(NEU2) 609668(LOC609668)
            BTA: 281349(NEU3)
            XLA: 444511(MGC81958)
            SPU: 583431(LOC583431) 585449(LOC585449) 764416(LOC764416)
            PIC: PICST_3402(HYR6.2) PICST_3529(HYR6.3) PICST_61722(HYR6.4)
            AFM: AFUA_4G13800
            TBR: Tb927.7.6850 Tb927.7.7480
            STM: STM0928(nanH)
            PMU: PM0663 PM1000
            VCH: VC1784
            VCO: VC0395_A1381(nanH)
            SPL: Spea_1515
            PHA: PSHAb0159
            BXE: Bxe_B2278
            BBA: Bd2821 Bd3647
            RET: RHE_PB00030
            RLE: pRL90099
            SUS: Acid_0193
            SPN: SP_1326 SP_1687
            SPR: spr1531(nanB) spr1536(nanA)
            SPD: SPD_1499(nanB) SPD_1504(nanA)
            CPE: CPE0553(nanJ) CPE0725(nanI)
            CTC: CTC00453
            CGL: NCgl1495(cgl1556)
            CGB: cg1756(nanH)
            CDI: DIP0330
            SCO: SCO6557(SC4B5.07c)
            SMA: SAV5934
            ART: Arth_0189 Arth_0543
            PAC: PPA0684 PPA0685 PPA1560
            SEN: SACE_1663
            RBA: RB3353
            BTH: BT_0455
            BFR: BF3936
            BFS: BF3709
            HMA: pNG5066
STRUCTURES  PDB: 1A14  1A4G  1A4Q  1B9S  1B9T  1B9V  1BJI  1DIL  1DIM  1E8T  
                 1E8U  1E8V  1EUR  1EUS  1EUT  1EUU  1F8B  1F8C  1F8D  1F8E  
                 1INF  1ING  1INH  1INV  1INW  1INX  1INY  1IVB  1IVC  1IVD  
                 1IVE  1IVF  1IVG  1KIT  1L7F  1L7G  1L7H  1MR5  1MS0  1MS1  
                 1MS3  1MS4  1MS5  1MS8  1MS9  1MWE  1MZ5  1MZ6  1N1S  1N1T  
                 1N1V  1N1Y  1NCA  1NCB  1NCC  1NCD  1NMA  1NMB  1NMC  1NN2  
                 1NNA  1NNB  1NNC  1NSB  1NSC  1NSD  1S0I  1S0J  1SLI  1SLL  
                 1SNT  1SO7  1USR  1USX  1V0Z  1V2I  1V3B  1V3C  1V3D  1V3E  
                 1VCJ  1VCU  1W1X  1W20  1W21  1W8N  1W8O  1WCQ  1WCS  1XOE  
                 1XOG  1Z4V  1Z4W  1Z4X  1Z4Y  1Z4Z  1Z50  2A75  2AEP  2AGS  
                 2AH2  2B8H  2BAT  2BER  2BF6  2BZD  2C4A  2C4L  2CML  2F0Z  
                 2F10  2F11  2F12  2F13  2F24  2F25  2F26  2F27  2F28  2F29  
                 2FHR  2HT5  2HT7  2HT8  2HTQ  2HTR  2HTU  2QWA  2QWB  2QWC  
                 2QWD  2QWE  2QWF  2QWG  2QWH  2QWI  2QWJ  2QWK  2SIL  2SIM  
                 2SLI  3NN9  3SIL  3SLI  4NN9  4SLI  5NN9  6NN9  7NN9  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.18
            ExPASy - ENZYME nomenclature database: 3.2.1.18
            ExplorEnz - The Enzyme Database: 3.2.1.18
            ERGO genome analysis and discovery system: 3.2.1.18
            BRENDA, the Enzyme Database: 3.2.1.18
            CAS: 9001-67-6
///
ENTRY       EC 3.2.1.19       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
COMMENT     Deleted entry: heparinase (EC 3.2.1.19 created 1961, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.19
            ExPASy - ENZYME nomenclature database: 3.2.1.19
            ExplorEnz - The Enzyme Database: 3.2.1.19
            ERGO genome analysis and discovery system: 3.2.1.19
            BRENDA, the Enzyme Database: 3.2.1.19
///
ENTRY       EC 3.2.1.20                 Enzyme
NAME        alpha-glucosidase;
            maltase;
            glucoinvertase;
            glucosidosucrase;
            maltase-glucoamylase;
            alpha-glucopyranosidase;
            glucosidoinvertase;
            alpha-D-glucosidase;
            alpha-glucoside hydrolase;
            alpha-1,4-glucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     alpha-D-glucoside glucohydrolase
REACTION    Hydrolysis of terminal, non-reducing 1,4-linked alpha-D-glucose
            residues with release of alpha-D-glucose
ALL_REAC    (other) R00028 R00801 R00802 R01101 R06084(G) R06087(G) R06088(G)
            R06091(G)
INHIBITOR   Castanospermine [CPD:C02256]
COMMENT     This single entry covers a group of enzymes whose specificity is
            directed mainly towards the exohydrolysis of 1,4-alpha-glucosidic
            linkages, and that hydrolyse oligosaccharides rapidly, relative to
            polysaccharide, which are hydrolysed relatively slowly, or not at
            all. The intestinal enzyme also hydrolyses polysaccharides,
            catalysing the reactions of EC 3.2.1.3 glucan 1,4-alpha-glucosidase
            and, more slowly, hydrolyses 1,6-alpha-D-glucose links.
REFERENCE   1  [PMID:5466143]
  AUTHORS   Bruni CB, Sica V, Auricchio F, Covelli I.
  TITLE     Further kinetic and structural characterization of the lysosomal
            alpha-D-glucoside glucohydrolase from cattle liver.
  JOURNAL   Biochim. Biophys. Acta. 212 (1970) 470-7.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:29602]
  AUTHORS   Flanagan PR, Forstner GG.
  TITLE     Purification of rat intestinal maltase/glucoamylase and its
            anomalous dissociation either by heat or by low pH.
  JOURNAL   Biochem. J. 173 (1978) 553-63.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Larner, J.
  TITLE     Other glucosidases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 369-378.
REFERENCE   4  [PMID:4792946]
  AUTHORS   Sivakami S, Radhakrishnan AN.
  TITLE     Purification of rabbit intestinal glucoamylase by affinity
            chromatography on Sephadex G-200.
  JOURNAL   Indian. J. Biochem. Biophys. 10 (1973) 283-4.
  ORGANISM  rabbit
REFERENCE   5  [PMID:6814909]
  AUTHORS   Sorensen SH, Noren O, Sjostrom H, Danielsen EM.
  TITLE     Amphiphilic pig intestinal microvillus maltase/glucoamylase.
            Structure and specificity.
  JOURNAL   Eur. J. Biochem. 126 (1982) 559-68.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00052  Galactose metabolism
            PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01187  alpha-glucosidase
GENES       HSA: 2548(GAA) 2595(GANC) 8972(MGAM)
            PTR: 453361(GANC) 454940(GAA)
            MMU: 14387(Gaa)
            RNO: 367562(Gaa)
            CFA: 483352(GAA)
            BTA: 280798(GAA)
            GGA: 416462(GAA) 417691(LOC417691)
            SPU: 592667(LOC592667)
            DME: Dmel_CG11669 Dmel_CG14476 Dmel_CG14934 Dmel_CG14935
                 Dmel_CG6453 Dmel_CG8693 Dmel_CG8694(LvpD) Dmel_CG8695(LvpL)
                 Dmel_CG8696(LvpH)
            CEL: D2096.3
            ATH: AT3G45940 AT5G11720
            OSA: 4341824 4341833
            SCE: YBR299W(MAL32) YGR287C YGR292W(MAL12) YIL172C YJL216C
                 YJL221C(FSP2) YOL157C
            PIC: PICST_29292(MAL9) PICST_42120(MAL6) PICST_85073(ROT2)
            SPO: SPAC922.02c SPAPB24D3.10c SPBC1683.07
            ANI: AN2017.2 AN3504.2 AN7345.2
            AFM: AFUA_1G06560 AFUA_1G16250 AFUA_4G10150 AFUA_8G07070
            AOR: AO090003001209 AO090005001084 AO090023000288 AO090038000471
                 AO090103000129
            ANG: An04g06920(aglU)
            CNE: CNF00610 CNH01310 CNN00140
            UMA: UM03692.1
            DDI: DDBDRAFT_0190556
            TET: TTHERM_00013800 TTHERM_00013890 TTHERM_00013900
                 TTHERM_00181060 TTHERM_00463650
            TBR: Tb10.05.0080
            LMA: LmjF18.0090
            EHI: 154.t00005 25.t00013
            ECO: b0403(malZ)
            ECJ: JW0393(malZ)
            ECE: Z0501(malZ)
            ECS: ECs0453
            ECC: c0513(malZ)
            ECI: UTI89_C0425(malZ)
            ECP: ECP_0462
            ECV: APECO1_1607(malZ)
            ECW: EcE24377A_0433(malZ)
            ECX: EcHS_A0473
            STY: STY0439(malZ)
            STT: t2462(malZ)
            SPT: SPA2322(malZ)
            SEC: SC0443(malZ)
            STM: STM0401(malZ)
            YPE: YPO0848 YPO3200(malZ)
            YPK: y0983(malZ) y3233
            YPM: YP_0732(malZ) YP_3545
            YPA: YPA_0422 YPA_2693
            YPN: YPN_0889 YPN_3050
            YPS: YPTB0922(malZ) YPTB3093
            YPI: YpsIP31758_3131(malZ)
            SFL: SF0340(malZ)
            SFX: S0348(malZ)
            SFV: SFV_0368(malZ)
            SSN: SSON_0380(malZ) SSON_0800
            ECA: ECA1968
            SPE: Spro_3598
            MSU: MS0539
            APL: APL_1021
            ASU: Asuc_0149
            XCC: XCC2468(aglA) XCC2471(aglA) XCC3163(susB)
            XCB: XC_1002 XC_1642 XC_1645
            XCV: XCV2800 XCV2803(aglA) XCV3431
            XAC: XAC2599(aglA) XAC2602(aglA) XAC3313(susB)
            VVU: VV1_2227
            VVY: VV2128
            VPA: VP2077
            PPR: PBPRA1726
            SON: SO_2213
            SDN: Sden_2002 Sden_2028
            SFR: Sfri_1777 Sfri_1788
            SHN: Shewana3_1931 Shewana3_2311
            CPS: CPS_0983 CPS_0984
            PHA: PSHAa1351 PSHAa1357 PSHAa2848
            PAT: Patl_2338
            SDE: Sde_0590 Sde_0601 Sde_2360
            MCA: MCA0942
            HCH: HCH_00205 HCH_00480 HCH_04150
            CSA: Csal_0261
            AHA: AHA_4149
            BUR: Bcep18194_B1872
            BCH: Bcen2424_4158
            BAM: Bamb_3565
            EBA: ebA583
            BBA: Bd2279(malA)
            MLO: mll5109 mlr7593
            MES: Meso_3687
            SME: SMc01532 SMc03064(aglA)
            ATU: Atu0594(aglA) Atu2295(aglA)
            ATC: AGR_C_1051 AGR_C_4169
            RET: RHE_CH00699(aglA) RHE_CH03095(ypch01078)
            RLE: RL0748(aglA) RL3542(aglA)
            BJA: blr0901(aglA)
            BRA: BRADO4392
            RPE: RPE_4865
            CCR: CC_2285
            SIT: TM1040_3304 TM1040_3867
            RSP: RSP_1370
            JAN: Jann_3112
            RDE: RD1_2326(aglA)
            GOX: GOX1342
            RRU: Rru_A2294
            ABA: Acid345_0387 Acid345_0650 Acid345_0921
            BCE: BC0413
            BCZ: BCZK0343
            BTK: BT9727_0347
            BTL: BALH_0369
            BLI: BL00280
            BLD: BLi02117 BLi03301(yugT)
            BCL: ABC0298
            GKA: GK0615
            SAR: SAR1584(malA)
            SAS: SAS1447
            SAC: SACOL1551(malA)
            SAB: SAB1368c(malA)
            SAA: SAUSA300_1456
            SAO: SAOUHSC_01601
            SER: SERP1070(malA)
            SHA: SH1408(malA)
            SSP: SSP1246
            LMO: lmo0183
            LMF: LMOf2365_0194
            LIN: lin0222
            LLC: LACR_1848
            LLM: llmg_0744(agl) llmg_1869(apu)
            LPL: lp_0174(agl1) lp_0189(agl2) lp_0193(agl3) lp_3220(agl4)
                 lp_3534(agl5) lp_3627(agl6)
            LJO: LJ0211 LJ0569
            LAC: LBA1365 LBA1812 LBA1872
            LBR: LVIS_0137 LVIS_0309 LVIS_2180
            LCA: LSEI_0980 LSEI_2102
            LGA: LGAS_0214
            LRE: Lreu_1017
            CPE: CPE2076 CPE2339
            CPF: CPF_2333
            CPR: CPR_2334
            CNO: NT01CX_0968
            CBE: Cbei_1443 Cbei_4653 Cbei_4655
            TTE: TTE0006 TTE1934
            MMY: MSC_0162(xylS) MSC_0748(aglA)
            MMO: MMOB3970(algA)
            MTU: Rv2471(aglA)
            MTC: MT0134 MT2547
            MBO: Mb2498(aglA)
            MBB: BCG_2491(aglA)
            MPA: MAP2292 MAP3528
            MSM: MSMEG_4696
            CGB: cg2529(treS)
            CDI: DIP0532
            NFA: nfa13150
            RHA: RHA1_ro01389 RHA1_ro04274
            SCO: SCO1394(SC1A8A.14) SCO2228(aglA) SCO3780(SCH63.27)
                 SCO7010(aglA)
            SMA: SAV1724(aglA1) SAV5980(aglA2) SAV6307(treA) SAV6969
            PAC: PPA1630 PPA2332
            TFU: Tfu_0833
            FRA: Francci3_1150
            FAL: FRAAL1845(aglA)
            SEN: SACE_1330 SACE_1668(aglA) SACE_3274(aglA) SACE_4257(aglA)
                 SACE_6260(aglA)
            BLO: BL0529(aglA)
            RXY: Rxyl_2099
            RBA: RB10507
            LIL: LA2944
            LIC: LIC11117(malZ)
            CYA: CYA_2306
            CYB: CYB_1375
            GVI: gll0197 glr1535
            ANA: alr4773 alr5331
            TER: Tery_4624
            BTH: BT_3086
            BFR: BF1397
            BFS: BF1332
            CHU: CHU_0803(malZ)
            GFO: GFO_2998
            FJO: Fjoh_2746 Fjoh_4430
            DRA: DR_0723 DR_1375
            DGE: Dgeo_0475 Dgeo_0672
            TTH: TTC0107 TTC1283 TT_P0221
            TTJ: TTHA0481 TTHA1647 TTHB033
            TMA: TM0434 TM0752 TM1068 TM1834
            TME: Tmel_1611
            FNO: Fnod_1570
            HMA: rrnAC0224(aglA1)
            PTO: PTO0092
            SSO: SSO3051(malA)
            STO: ST2525
            SAI: Saci_1160(malA)
            MSE: Msed_0911
            PAI: PAE1968
            PIS: Pisl_1794
            PCL: Pcal_0917
            PAS: Pars_2044
STRUCTURES  PDB: 1G7P  1OBB  1VAD  2D73  2G3M  2G3N  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.20
            ExPASy - ENZYME nomenclature database: 3.2.1.20
            ExplorEnz - The Enzyme Database: 3.2.1.20
            ERGO genome analysis and discovery system: 3.2.1.20
            BRENDA, the Enzyme Database: 3.2.1.20
            CAS: 9001-42-7
///
ENTRY       EC 3.2.1.21                 Enzyme
NAME        beta-glucosidase;
            gentiobiase;
            cellobiase;
            emulsin;
            elaterase;
            aryl-beta-glucosidase;
            beta-D-glucosidase;
            beta-glucoside glucohydrolase;
            arbutinase;
            amygdalinase;
            p-nitrophenyl beta-glucosidase;
            primeverosidase;
            amygdalase;
            limarase;
            salicilinase;
            beta-1,6-glucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     beta-D-glucoside glucohydrolase
REACTION    Hydrolysis of terminal, non-reducing beta-D-glucose residues with
            release of beta-D-glucose
ALL_REAC    (other) R00026 R02887 R03527 R04949 R04998 R06077(G) R06092(G)
COMMENT     Wide specificity for beta-D-glucosides. Some examples also hydrolyse
            one or more of the following: beta-D-galactosides,
            alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides.
REFERENCE   1  [PMID:2503402]
  AUTHORS   Chinchetru MA, Cabezas JA, Calvo P.
  TITLE     Purification and characterization of a broad specificity
            beta-glucosidase from sheep liver.
  JOURNAL   Int. J. Biochem. 21 (1989) 469-76.
  ORGANISM  sheep
REFERENCE   2  [PMID:13230003]
  AUTHORS   CONCHIE J.
  TITLE     Beta-Glucosidase from rumen liquor; preparation, assay and kinetics
            of action.
  JOURNAL   Biochem. J. 58 (1954) 552-60.
  ORGANISM  sheep, Aspergillus oryzae [GN:aor]
REFERENCE   3  [PMID:13719334]
  AUTHORS   DAHLQVIST A.
  TITLE     Pig intestinal beta-glucosidase activities. I. Relation to
            beta-galactosidase (lactase).
  JOURNAL   Biochim. Biophys. Acta. 50 (1961) 55-61.
REFERENCE   4  [PMID:13907157]
  AUTHORS   HEYWORTH R, WALKER PG.
  TITLE     Almond-emulsin beta-D-glucosidase and beta-D-galactosidase.
  JOURNAL   Biochem. J. 83 (1962) 331-5.
  ORGANISM  sweet-almond
REFERENCE   5
  AUTHORS   Larner, J.
  TITLE     Other glucosidases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 369-378.
REFERENCE   6  [PMID:235305]
  AUTHORS   Sano K, Amemura A, Harada T.
  TITLE     Purification and properties of a beta-1,6-clucosidase from
            Flavobacterium.
  JOURNAL   Biochim. Biophys. Acta. 377 (1975) 410-20.
  ORGANISM  Flavobacterium sp.
PATHWAY     PATH: map00460  Cyanoamino acid metabolism
            PATH: map00500  Starch and sucrose metabolism
            PATH: map00940  Phenylpropanoid biosynthesis
ORTHOLOGY   KO: K01188  beta-glucosidase
            KO: K05349  beta-glucosidase
            KO: K05350  beta-glucosidase
GENES       HSA: 2629(GBA) 57733(GBA3)
            CFA: 488857(GBA3)
            XLA: 447502(MGC82041)
            CEL: C50F7.10
            ATH: AT1G02640(BXL2) AT1G26560 AT2G44450 AT2G44480 AT3G18080
                 AT3G47000 AT3G47050 AT5G42260 AT5G44640
            OSA: 4324050 4332041 4333841 4336146 4338560
            PIC: PICST_1541(BGL1) PICST_34123(BGL5) PICST_37797(BGL4)
                 PICST_41452(BGL2) PICST_51227(BGL6) PICST_61725(BGL3)
                 PICST_65767(BGL7) PICST_89784(SUN4)
            SPO: SPAC1002.13c(psu1) SPBC1683.04
            ANI: AN0812.2 AN7396.2
            AFM: AFUA_1G05770 AFUA_1G14710 AFUA_1G16400 AFUA_1G17410
                 AFUA_3G00230 AFUA_5G07080 AFUA_5G07190 AFUA_6G03570
                 AFUA_6G08700 AFUA_6G11910 AFUA_6G12010 AFUA_7G06140
                 AFUA_8G02100 AFUA_8G06970
            AOR: AO090003000497 AO090010000034 AO090011000140 AO090012000135
                 AO090701000244 AO090701000841
            ANG: An18g03570(bgl1)
            CNE: CNE05170
            EHI: 55.t00001
            ECO: b2132(bglX)
            ECJ: JW2120(bglX)
            ECE: Z3381(bglX)
            ECS: ECs3019
            ECC: c2663(bglX)
            ECI: UTI89_C2406(bglX)
            ECP: ECP_2171
            ECV: APECO1_4417(bglX)
            ECW: EcE24377A_2421(bglX)
            ECX: EcHS_A2267(bglX)
            STY: STY2396(bglX) STY4009
            STT: t0689(bglX) t3743
            SPT: SPA0685(bglX) SPA3625
            SEC: SC2182(bglX) SC3695(bglA)
            STM: STM2166(bglX) STM3775
            YPE: YPO0616 YPO2803(bglB)
            YPK: y1128 y3562
            YPM: YP_1160(bglB) YP_2934(bglX2)
            YPA: YPA_2548 YPA_3174
            YPN: YPN_0479 YPN_1038
            YPP: YPDSF_0401
            YPS: YPTB1055(bglB) YPTB3439
            YEN: YE2103(arbB)
            SFL: SF2217(bglX)
            SFX: S2346(bglX)
            SFV: SFV_2208(bglX)
            SSN: SSON_2189(bglX)
            SBO: SBO_1012(bglX)
            SDY: SDY_2156(bglX)
            ECA: ECA2790(bglX) ECA3646(celH) ECA4387(bglH) ECA4407
            ENT: Ent638_0036 Ent638_2731
            KPN: KPN_02568(bglX)
            SPE: Spro_0836 Spro_4221
            XFA: XF0439 XF0845
            XFT: PD1640(bglX) PD1829(xylA)
            XCC: XCC1090(bglX) XCC1404(bglS) XCC1775(celD) XCC2892
                 XCC3814(bglX) XCC4106
            XCB: XC_1217 XC_2461 XC_2834 XC_3159 XC_3886 XC_4197
            XCV: XCV1505(bglS) XCV3211 XCV3988(bglX) XCV4337
            XAC: XAC1448(bglS) XAC1793(celD) XAC3076 XAC3869(bglX) XAC4231
            XOO: XOO1779 XOO2352(bglS) XOO2356(celD) XOO4123(bglX) XOO4423
            XOM: XOO_1682(XOO1682) XOO_2234(XOO2234) XOO_2238(XOO2238)
                 XOO_3899(XOO3899) XOO_4166(XOO4166)
            VVU: VV2_1287
            VVY: VVA0128
            PPR: PBPRA0461 PBPRB2006(bglB)
            PAE: PA1726(bglX)
            PAU: PA14_42230(bglX)
            PAP: PSPA7_2629 PSPA7_3580
            PPU: PP_1403(bglX)
            PST: PSPTO_3318 PSPTO_4290(bglX)
            PSB: Psyr_1781 Psyr_3153 Psyr_3993
            PSP: PSPPH_4000(bglX)
            PFL: PFL_1351(bglX)
            PFO: Pfl_1297
            PEN: PSEEN4339(bglX)
            PMY: Pmen_3237
            PSA: PST_2726(bglX)
            SDN: Sden_2605 Sden_2607
            SFR: Sfri_1307 Sfri_1316 Sfri_1318
            SAZ: Sama_1402
            SBL: Sbal_1131 Sbal_1133
            SBM: Shew185_1183
            CPS: CPS_2379 CPS_3706(abG) CPS_3739(bglX) CPS_3740
            PAT: Patl_0825 Patl_3730
            SDE: Sde_0245 Sde_1394 Sde_1487 Sde_2674 Sde_3603
            MCA: MCA1578(bgl)
            HCH: HCH_06825 HCH_06907
            MMW: Mmwyl1_4295
            AHA: AHA_2091 AHA_2689
            CVI: CV_1272(bglB)
            RME: Rmet_3995
            BML: BMA10299_1911
            BXE: Bxe_B2084
            BVI: Bcep1808_4765
            BUR: Bcep18194_B1822 Bcep18194_C6710
            BCN: Bcen_1802 Bcen_4171
            BCH: Bcen2424_2414 Bcen2424_4195
            BAM: Bamb_2459 Bamb_3266 Bamb_3617 Bamb_4300
            BPS: BPSS1657(bglB)
            BPM: BURPS1710b_1239(bglB) BURPS1710b_1240(bglB) BURPS1710b_A0720
            BTE: BTH_II0723(bglB)
            RFR: Rfer_1102 Rfer_1111 Rfer_1113
            DPS: DP2448(bglA)
            AFW: Anae109_3267
            MXA: MXAN_6303(bglA) MXAN_6555
            RPR: RP706
            RTY: RT0701
            RCO: RC1086
            RFE: RF_0203
            RBE: RBE_0182
            SME: SMc03160
            SMD: Smed_2786
            ATU: Atu4485(bgl)
            ATC: AGR_L_770
            RET: RHE_CH03640(bglSch) RHE_PD00043 RHE_PF00473(bglSf)
            RLE: RL4168(abg) pRL120344
            OAN: Oant_2765
            BJA: bll6177 blr1365(bgl) blr4657
            BRA: BRADO1577 BRADO3844
            BBT: BBta_4086 BBta_6477
            RPA: RPA1736(bglA)
            RPB: RPB_3627
            RPC: RPC_1611
            RPD: RPD_1840
            RPE: RPE_4619
            CCR: CC_0797 CC_0968 CC_1105 CC_1756 CC_2052 CC_2136
            SIT: TM1040_3309
            RSP: RSP_2874
            RSH: Rsph17029_1520
            RSQ: Rsph17025_1146
            JAN: Jann_1944
            RDE: RD1_2318(bglA)
            MMR: Mmar10_2726 Mmar10_2729
            NAR: Saro_1611 Saro_1729 Saro_2419
            SAL: Sala_1014 Sala_1019 Sala_1511
            RRU: Rru_A3299
            MAG: amb0219 amb2230
            ABA: Acid345_0530 Acid345_2378 Acid345_3246 Acid345_4061
            SUS: Acid_6936
            BSU: BG10935(bglH) BG11181(yckE) BG12193(ydhP)
            BHA: BH0596(gblH) BH1908 BH1923(bglA) BH3918
            BCZ: BCZK0860(bglH)
            BLI: BL00115(ydhP) BL00212(bglH) BL01718 BL01920 BL01946 BL02680
            BLD: BLi00387(yckE) BLi02560(ydhP) BLi03544 BLi04168 BLi04199
                 BLi04214(bglH)
            BCL: ABC0315 ABC0484 ABC1454 ABC3792(bglH)
            BAY: RBAM_036350(bglH)
            BPU: BPUM_3538 BPUM_3565(bglH) BPUM_3643
            OIH: OB0779 OB2763
            GKA: GK1856 GK2337 GK3214
            LMO: lmo0018 lmo0261 lmo0271 lmo0300 lmo0319 lmo0372 lmo0574
                 lmo0917 lmo1729 lmo2761 lmo2771 lmo2781
            LMF: LMOf2365_0021 LMOf2365_0277 LMOf2365_0291 LMOf2365_0321
                 LMOf2365_0337(bglH-1) LMOf2365_0388 LMOf2365_0603
                 LMOf2365_0939(bglH-2) LMOf2365_1753(bglX-1) LMOf2365_2751
                 LMOf2365_2772(bglX-2)
            LIN: lin0017 lin0288 lin0297 lin0328 lin0344 lin0391 lin0583
                 lin0918 lin1840 lin2904
            LWE: lwe0230 lwe0245 lwe0275 lwe0328 lwe0540 lwe1746 lwe2708
                 lwe2727(bglX-2)
            LLA: L119614(ypcA) L179659(bglS) L32812(yidC) L89194(bglH)
            LLC: LACR_0184 LACR_1473 LACR_1544 LACR_1586
            LLM: llmg_0190(bglS) llmg_0959 llmg_0960 llmg_1004 llmg_1046(bglH)
                 llmg_1456(bglX) llmg_1738
            SPY: SPy_1328(bglA.2) SPy_1599
            SPZ: M5005_Spy_1085(bglA.2) M5005_Spy_1313
            SPM: spyM18_1338(bglA) spyM18_1605
            SPG: SpyM3_1007(bglA.2) SpyM3_1293
            SPS: SPs0568 SPs0852
            SPH: MGAS10270_Spy1141(bglA2) MGAS10270_Spy1429
            SPI: MGAS10750_Spy1178(bglA2) MGAS10750_Spy1422
            SPJ: MGAS2096_Spy1086(bglA2) MGAS2096_Spy1333
            SPK: MGAS9429_Spy1128(bglA2) MGAS9429_Spy1307
            SPA: M6_Spy1054 M6_Spy1331
            SPB: M28_Spy1066(bglA.2) M28_Spy1354
            SPN: SP_0265 SP_2021
            SPR: spr0244(bglA) spr1833(bgl2)
            SPD: SPD_0277(bglA-1)
            SSA: SSA_1149
            SSU: SSU05_2147
            SSV: SSU98_2149
            SGO: SGO_1759
            LPL: lp_0906(pbg2) lp_3629(bgl)
            LJO: LJ0544 LJ0736
            LAC: LBA1366 LBA1574(bglH) LBA1706
            LSA: LSA1169 LSA1531
            LBR: LVIS_1961
            LCA: LSEI_0448 LSEI_0700
            LGA: LGAS_0397
            EFA: EF1020 EF1238 EF1243 EF1606
            STH: STH954
            CAC: CAC0385 CAC1075 CAC1084 CAC1405(bglA) CA_P0010(bglA)
            CPE: CPE2309
            CPR: CPR_2295 CPR_2603
            CTH: Cthe_0212
            CBE: Cbei_1477 Cbei_3814 Cbei_4566
            CSC: Csac_0586 Csac_1089
            TTE: TTE0338(bglB) TTE0358(bglB2)
            MPE: MYPE4550(bglH) MYPE4560(bglH)
            MMY: MSC_0840(bgl)
            MFL: Mfl011 Mfl012 Mfl425
            MTU: Rv0186 Rv0237(lpqI)
            MTC: MT0195 MT0251
            MBO: Mb0192(bglS) Mb0243(lpqI)
            MBB: BCG_0223(bglS)
            MLE: ML2569
            MPA: MAP3625(bglS) MAP3688(lpqI)
            MSM: MSMEG_2556 MSMEG_5142 MSMEG_5144
            CGL: NCgl0311(cgl0317) NCgl2754(cgl2852)
            CGB: cg0385(bglS')
            CEF: CE0329 CE2670
            CDI: DIP2172
            CJK: jk0169 jk0930
            NFA: nfa26190 nfa29580 nfa34000 nfa54650
            RHA: RHA1_ro01034(bglA) RHA1_ro02947
            SCO: SCO0293(SC5G9.02) SCO0458(SCF51A.36) SCO1059(SCG22.05)
                 SCO2531(SCC117.04) SCO2798(2SCC13.06) SCO6604(SC1F2.01)
                 SCO7031(SC1H10.20) SCO7558(SC5F1.12)
            SMA: SAV1801(bglC1) SAV2708 SAV4982(xynB2) SAV5253(bglC2)
                 SAV5598(bglC3)
            CMI: CMM_1041(bglK) CMM_2249(bglL)
            ART: Arth_3149
            AAU: AAur_0085(bglA) AAur_0658 AAur_2950(bglA)
            PAC: PPA0992
            NCA: Noca_3263 Noca_3917 Noca_4587
            TFU: Tfu_0937 Tfu_1607 Tfu_1629
            ACE: Acel_0133 Acel_1659
            KRA: Krad_3961
            SEN: SACE_0732(eryBI) SACE_1247(bglC3) SACE_1284(bglSf)
                 SACE_4101(bglA) SACE_5452(bglB2)
            STP: Strop_0326 Strop_2958
            BLO: BL1757(bglX)
            BAD: BAD_1194 BAD_1197(bglX) BAD_1611
            RXY: Rxyl_2046
            TDE: TDE1882
            SYN: sll1538(bgl)
            SYW: SYNW2208
            SYC: syc1159_d(bgl)
            SYF: Synpcc7942_0354
            SYD: Syncc9605_2351
            SYE: Syncc9902_0340
            SYR: SynRCC307_0280
            TEL: tll1043
            GVI: gll0417
            PMA: Pro0133(cglX)
            PMT: PMT1964
            PMF: P9303_26161
            PME: NATL1_01861
            BTH: BT_1780 BT_1872 BT_3300 BT_3314 BT_3567 BT_4714
            BFR: BF0330 BF0392 BF0841 BF4372
            BFS: BF0278 BF0339 BF0766 BF4170(bglX)
            CHU: CHU_0013(nagA) CHU_2268(bglX) CHU_2273(bglX) CHU_3577(bglX)
                 CHU_3784(bglX) CHU_3811(blgA)
            GFO: GFO_0367(bglX) GFO_3467(bglX)
            FJO: Fjoh_3521 Fjoh_3874 Fjoh_4857
            RRS: RoseRS_3614
            RCA: Rcas_0521
            DGE: Dgeo_2862
            TTH: TT_P0042
            TTJ: TTHB087
            TMA: TM0025 TM0076
            TPT: Tpet_0848 Tpet_0952
            TME: Tmel_1638
            FNO: Fnod_1530
            HMA: rrnAC0173(bglX-1) rrnAC1113(bglX-2)
            PHO: PH0366
            PFU: PF0442
            TKO: TK1827
            RCI: LRC258(bglX)
            SSO: SSO3032
            PAI: PAE1736
STRUCTURES  PDB: 1BGA  1BGG  1CBG  1E1E  1E1F  1E4I  1E4L  1E4N  1E55  1E56  
                 1GNX  1H49  1HXJ  1NP2  1OD0  1OIF  1OIM  1OIN  1QOX  1TR1  
                 1UYQ  1UZ1  1V02  1V03  1V08  1VFF  1W3J  2CBU  2CBV  2CER  
                 2CES  2CET  2DGA  2E3Z  2E40  2E9L  2E9M  2J75  2J77  2J78  
                 2J79  2J7B  2J7C  2J7D  2J7E  2J7F  2J7G  2J7H  2JAL  2JFE  
                 2JIE  2O9P  2O9R  2O9T  2Z1S  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.21
            ExPASy - ENZYME nomenclature database: 3.2.1.21
            ExplorEnz - The Enzyme Database: 3.2.1.21
            ERGO genome analysis and discovery system: 3.2.1.21
            BRENDA, the Enzyme Database: 3.2.1.21
            CAS: 9001-22-3
///
ENTRY       EC 3.2.1.22                 Enzyme
NAME        alpha-galactosidase;
            melibiase;
            alpha-D-galactosidase;
            alpha-galactosidase A;
            alpha-galactoside galactohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     alpha-D-galactoside galactohydrolase
REACTION    Hydrolysis of terminal, non-reducing alpha-D-galactose residues in
            alpha-D-galactosides, including galactose oligosaccharides,
            galactomannans and galactohydrolase
ALL_REAC    (other) R01101 R01103 R01104 R01194 R01329 R02926 R03618 R03634
            R04019 R04470 R05549 R05961(G) R06002(G) R06070(G) R06091(G)
            R06093(G) R06094(G) R06096(G) R06142(G) R06152(G)
COMMENT     Also hydrolyses alpha-D-fucosides.
REFERENCE   1  [PMID:5418105]
  AUTHORS   Suzuki H, Li SC, Li YT.
  TITLE     Alpha-galactosidase from Mortierella vinacea. Crystallization and
            properties.
  JOURNAL   J. Biol. Chem. 245 (1970) 781-6.
  ORGANISM  Mortierella vinacea
REFERENCE   2  [PMID:976079]
  AUTHORS   Vidershain GIa, Beier EM.
  TITLE     [Interrelation of alpha-D-fucosidase and alpha-D-galactosidase
            activities in man and animals]
  JOURNAL   Dokl. Akad. Nauk. SSSR. 231 (1976) 486-8.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00052  Galactose metabolism
            PATH: map00561  Glycerolipid metabolism
            PATH: map00600  Sphingolipid metabolism
            PATH: map00603  Glycosphingolipid biosynthesis - globoseries
ORTHOLOGY   KO: K01189  alpha-galactosidase
            KO: K07406  alpha-galactosidase
            KO: K07407  alpha-galactosidase
GENES       HSA: 2717(GLA)
            MMU: 11605(Gla)
            CFA: 480988(GLA)
            GGA: 422188(GLA)
            ATH: AT3G56310
            OSA: 4344290
            CME: CMG050C
            SCE: YBR184W
            SPO: SPAC869.07c
            ANI: AN7624.2
            AFM: AFUA_1G01200 AFUA_4G03580 AFUA_5G02130 AFUA_5G13830
                 AFUA_8G01100 AFUA_8G01130
            AOR: AO090003001305
            ANG: An02g11150(aglB) An06g00170(aglA) An09g00260(aglC)
                 An09g00270(aglC)
            TET: TTHERM_00043770 TTHERM_01181990
            ECO: b4119(melA)
            ECJ: JW4080(melA)
            ECE: Z5721(melA)
            ECS: ECs5101
            ECC: c5124(melA)
            ECI: UTI89_C1705(yddW) UTI89_C4713(melA)
            ECP: ECP_4362
            ECV: APECO1_2332(melA)
            ECW: EcE24377A_3380(rafA) EcE24377A_4673(melA)
            ECX: EcHS_A4360
            STY: STY4497(melA)
            STT: t4205(melA)
            SPT: SPA4116(melA)
            SEC: SC4177(melA)
            STM: STM4298(melA)
            YPE: YPO1581(rafA)
            YPK: y2582
            YPM: YP_1469(galA)
            YPA: YPA_0878
            YPN: YPN_2398
            YPS: YPTB1608(rafA)
            YPI: YpsIP31758_2395(agaN)
            SFL: SF4104(melA)
            SFX: S3626(melA)
            SFV: SFV_4111(melA)
            SSN: SSON_4294(melA)
            SBO: SBO_4146(melA)
            SDY: SDY_4092(melA)
            ECA: ECA0754(rafA)
            ENT: Ent638_1710
            MSU: MS1227(galA)
            VCH: VC1690
            VVU: VV1_2890 VV2_1330
            VVY: VV1379 VVA0166
            VPA: VP1163
            VFI: VFA0301
            PPR: PBPRB0018 PBPRB0258
            PAT: Patl_3687
            SDE: Sde_1593
            AHA: AHA_1897
            BPS: BPSS2081
            BPM: BURPS1710b_A1181(rafA)
            BPL: BURPS1106A_A2815(rafA)
            MLO: mlr6443 mlr6450
            SME: SMb21643(agaL2) SMb21648(agaL1)
            ATU: Atu4660(melA) Atu4665(melA)
            ATC: AGR_L_436 AGR_L_446
            RET: RHE_PE00089(agaL1) RHE_PE00094(agaL2)
            RLE: pRL110242 pRL110247 pRL120256(melA)
            BRA: BRADO2867
            RPA: RPA0378(melA)
            RPB: RPB_0445
            SIT: TM1040_3486
            RDE: RD1_2865(rafA)
            NAR: Saro_1878
            ELI: ELI_03515
            MAG: amb2735
            ABA: Acid345_1677
            SUS: Acid_0705 Acid_1588 Acid_2820
            BSU: BG12615(melA)
            BHA: BH2223 BH2228(melA)
            BLI: BL01356(melA)
            BLD: BLi01143(melA)
            BCL: ABC0412 ABC0732(melA)
            BAY: RBAM_027220
            BPU: BPUM_1750
            GKA: GK2152
            GTN: GTNG_2088
            SPN: SP_1898
            SPR: spr1713(aga)
            SPD: SPD_1678(aga)
            SAK: SAK_0535
            SMU: SMU.877(agaL)
            SSA: SSA_0419 SSA_1002
            SSU: SSU05_0172
            SSV: SSU98_0174
            LPL: lp_3485(melA)
            LJO: LJ0261
            LAC: LBA1438(melA)
            LSA: LSA1795(melA)
            LSL: LSL_1010(galA)
            LBR: LVIS_1758
            LCA: LSEI_1036 LSEI_2079
            LGA: LGAS_0257
            PPE: PEPE_0513
            OOE: OEOE_1781
            LME: LEUM_0882
            CPE: CPE0374(aga) CPE0512(agaN)
            CPF: CPF_0491
            CPR: CPR_0475(aga)
            MSM: MSMEG_0514
            SCO: SCO0274(SCF85.02) SCO0541(SCF11.21)
            SMA: SAV1082(agaB1) SAV1475(agaB2) SAV1641(agaB3)
            AAU: AAur_3362(rafA)
            PAC: PPA2057
            FAL: FRAAL4014(melA)
            SEN: SACE_3139(agaB2) SACE_7065(agaB2)
            BLO: BL1518(aga)
            BAD: BAD_1576(aga)
            TDE: TDE1453
            LIL: LA2918(galA)
            LIC: LIC11140(galA)
            LBJ: LBJ_2282
            LBL: LBL_0825
            BTH: BT_2851 BT_3065 BT_3131
            BFR: BF0287 BF0550 BF1485 BF4391
            BFS: BF0233 BF0498 BF1418 BF4189
            FJO: Fjoh_4947
            DGE: Dgeo_2828
            TTH: TT_P0072
            TTJ: TTHB115
            TMA: TM1192
            TPE: Tpen_1511
STRUCTURES  PDB: 1R46  1R47  1SZN  1T0O  1UAS  1ZY9  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.22
            ExPASy - ENZYME nomenclature database: 3.2.1.22
            ExplorEnz - The Enzyme Database: 3.2.1.22
            ERGO genome analysis and discovery system: 3.2.1.22
            BRENDA, the Enzyme Database: 3.2.1.22
            CAS: 9025-35-8
///
ENTRY       EC 3.2.1.23                 Enzyme
NAME        beta-galactosidase;
            lactase (ambiguous);
            beta-lactosidase;
            maxilact;
            hydrolact;
            beta-D-lactosidase;
            S 2107;
            lactozym;
            trilactase;
            beta-D-galactanase;
            oryzatym;
            sumiklat
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     beta-D-galactoside galactohydrolase
REACTION    Hydrolysis of terminal non-reducing beta-D-galactose residues in
            beta-D-galactosides
ALL_REAC    (other) R01105 R01678 R01679 R03355 R03616 R04633 R04783 R05112
            R05994(G) R06010(G) R06098(G) R06099(G) R06111(G) R06144(G)
            R06202(G) R07807(G)
COMMENT     Some enzymes in this group hydrolyse alpha-L-arabinosides; some
            animal enzymes also hydrolyse beta-D-fucosides and
            beta-D-glucosides; cf. EC 3.2.1.108 lactase.
REFERENCE   1  [PMID:5389663]
  AUTHORS   Blakely JA, MacKenzie SL.
  TITLE     Purification and properties of a beta-hexosidase from Sporobolomyces
            singularis.
  JOURNAL   Can. J. Biochem. 47 (1969) 1021-5.
  ORGANISM  Sporobolomyces singularis
REFERENCE   2
  AUTHORS   Kuby, S.A. and Lardy, H.A.
  TITLE     Purification and kinetics of beta-D-galactosidase from Escherichia
            coli, strain K-12.
  JOURNAL   J. Am. Chem. Soc. 75 (1953) 890-896.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:418065]
  AUTHORS   Kuo CH, Wells WW.
  TITLE     beta-Galactosidase from rat mammary gland. Its purification,
            properties, and role in the biosynthesis of
            6beta-O-D-galactopyranosyl myo-inositol.
  JOURNAL   J. Biol. Chem. 253 (1978) 3550-6.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:13426167]
  AUTHORS   LANDMAN OE.
  TITLE     Properties and induction of beta-galactosidase in Bacillus
            megaterium.
  JOURNAL   Biochim. Biophys. Acta. 23 (1957) 558-69.
  ORGANISM  Bacillus megaterium
REFERENCE   5
  AUTHORS   Llanillo, M., Perez, N. and Cabezas, J.A.
  TITLE     beta-Galactosidase and beta-glucosidase activities of the same
            enzyme from rabbit liver.
  JOURNAL   Int. J. Biochem. 8 (1977) 557-564.
  ORGANISM  rabbit
REFERENCE   6  [PMID:14943665]
  AUTHORS   MONOD J, COHN M.
  TITLE     [Biosynthesis induced by enzymes; enzymatic adaptation.]
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 13 (1952) 67-119.
REFERENCE   7
  AUTHORS   Wallenfels, K. and Malhotra, O.P.
  TITLE     In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 409-430.
REFERENCE   8  [PMID:5822067]
  AUTHORS   Asp NG, Dahlqvist A, Koldovsky O.
  TITLE     Human small-intestinal beta-galactosidases. Separation and
            characterization of one lactase and one hetero beta-galactosidase.
  JOURNAL   Biochem. J. 114 (1969) 351-9.
PATHWAY     PATH: map00052  Galactose metabolism
            PATH: map00511  N-Glycan degradation
            PATH: map00531  Glycosaminoglycan degradation
            PATH: map00561  Glycerolipid metabolism
            PATH: map00600  Sphingolipid metabolism
            PATH: map00604  Glycosphingolipid biosynthesis - ganglioseries
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01190  beta-galactosidase
GENES       HSA: 2720(GLB1) 3938(LCT)
            MMU: 12091(Glb1) 226413(Lct)
            RNO: 116569(Lct) 316033(Glb1_predicted)
            CFA: 403873(GLB1) 483898(LCT)
            GGA: 420720(RCJMB04_5i4)
            SPU: 587532(LOC587532)
            DME: Dmel_CG3132(Ect3) Dmel_CG9092(Gal)
            CEL: T19B10.3(beta-galactosidase)
            ATH: AT3G52840
            OSA: 4325748 4339457
            CME: CMP078C
            PIC: PICST_30036(LAC4)
            ANI: AN3201.2 AN6388.2
            AFM: AFUA_1G14170 AFUA_1G16700 AFUA_3G00380 AFUA_5G14090
                 AFUA_5G14550 AFUA_6G06660
            AOR: AO090012000389 AO090120000158
            DDI: DDBDRAFT_0188784
            TET: TTHERM_00321550 TTHERM_00321600 TTHERM_00321640
            ECO: b0344(lacZ) b3076(ebgA)
            ECJ: JW0335(lacZ) JW5511(ebgA)
            ECE: Z0440(lacZ) Z4429(ebgA)
            ECS: ECs0397 ECs3958
            ECC: c0459(lacZ) c3833(ebgA)
            ECI: UTI89_C0371(lacZ) UTI89_C3516(ebgA) UTI89_C3517(ebgC)
            ECP: ECP_0417 ECP_3167
            ECV: APECO1_1649(lacZ) APECO1_3340(ebgA)
            ECW: EcE24377A_0368(lacZ) EcE24377A_3543(ebgA)
            ECX: EcHS_A0408(lacZ) EcHS_A3258(ebgA)
            YPE: YPO0852(bgaB) YPO1654(lacZ)
            YPK: y1817(lacZ) y3237
            YPM: YP_1785(lacZ) YP_3549(bgaB)
            YPA: YPA_0418 YPA_1868
            YPN: YPN_1975 YPN_3054
            YPS: YPTB2415(lacZ) YPTB3097(bgaB)
            YPI: YpsIP31758_1629(lacZ)
            SFL: SF3116(ebgA)
            SFX: S3323(ebgA)
            SFV: SFV_3117(ebgA)
            SSN: SSON_0299(lacZ) SSON_3215(ebgA)
            SBO: SBO_2935(ebgA)
            SDY: SDY_0378(lacZ)
            ECA: ECA1490(lacZ) ECA3179(pbg)
            MSU: MS0749(lacZ) MS0806(lacZ)
            APL: APL_0997(lacZ)
            XFA: XF0840
            XFT: PD1833(bga)
            XCC: XCC1256(bga) XCC2895(bga) XCC4116
            XCB: XC_1214 XC_2985 XC_4208
            XCV: XCV1359 XCV3214(bga1) XCV4356(bga2)
            XAC: XAC1308(bga) XAC3084(bga) XAC4250
            XOO: XOO1769(bga) XOO3923(lacZ)
            XOM: XOO_1670(XOO1670) XOO_3703(XOO3703)
            VCO: VC0395_A1917(lacZ)
            VVU: VV1_1767 VV2_1327
            VVY: VV2642 VVA0165
            VPA: VP2403
            VFI: VFA0347
            PPR: PBPRA2084 PBPRB0034
            SLO: Shew_3269
            PAT: Patl_0821 Patl_2144 Patl_4065
            SDE: Sde_2935 Sde_3882
            PIN: Ping_2019
            MMW: Mmwyl1_2015 Mmwyl1_2734
            AHA: AHA_0205 AHA_4101
            BVI: Bcep1808_1284 Bcep1808_3827
            BCN: Bcen_4877 Bcen_5202
            BCH: Bcen2424_3288 Bcen2424_5657
            BAM: Bamb_4931 Bamb_6327
            PLA: Plav_1938
            SME: SMb20966(lacZ2) SMb21655(lacZ1)
            RET: RHE_CH02656(lacZ1) RHE_CH03705(lacZ2)
            RLE: RL3107(bgaB) RL3801 RL4248(lacZ)
            SIT: TM1040_3492
            JAN: Jann_3830
            RDE: RD1_2869(bgaT)
            ZMO: ZMO0904(bga)
            SAL: Sala_1017
            ELI: ELI_03710
            ABA: Acid345_0901 Acid345_4484
            SUS: Acid_4396 Acid_4607 Acid_7597
            BSU: BG12439(lacA) BG12860(yesZ)
            BHA: BH2022(lacA) BH2723 BH3701
            BCZ: pE33L466_0350(bgaC)
            BLI: BL00264(lacA) BL01749 BL03780(yesZ)
            BLD: BLi00447 BLi01382(yesZ) BLi04277(lacA)
            BCL: ABC1405 ABC3516(lacA)
            BPU: BPUM_3617(lacA)
            SSP: SSP0105
            LLA: L0025(lacZ)
            SPZ: M5005_Spy_1304(lacZ)
            SPH: MGAS10270_Spy1419(lacZ)
            SPI: MGAS10750_Spy1413(lacZ)
            SPJ: MGAS2096_Spy1324(lacZ)
            SPK: MGAS9429_Spy1298(lacZ)
            SPA: M6_Spy1322
            SPB: M28_Spy1345(lacZ)
            SPN: SP_0060 SP_0648
            SPR: spr0059(bgaC) spr0565(bgaA)
            SPD: SPD_0065(bgaC)
            STC: str1397(lacZ)
            STL: stu1397(lacZ)
            SSA: SSA_0053 SSA_0271
            SGO: SGO_0043 SGO_1486
            LPL: lp_3469(lacA) lp_3483(lacL) lp_3484(lacM)
            LJO: LJ0738 LJ0854 LJ0855 LJ0858
            LAC: LBA1364(lacA) LBA1462(lacZ) LBA1467(lacL) LBA1468(lacM)
            LSA: LSA1710(lacM) LSA1711(lacL)
            LSL: LSL_0376(lacZ)
            LDB: Ldb1201(lacZ)
            LBU: LBUL_1114
            LBR: LVIS_2258 LVIS_2259
            LCA: LSEI_0384
            LRE: Lreu_1085
            PPE: PEPE_0204
            EFA: EF0813 EF1805 EF1851 EF2709
            OOE: OEOE_1044
            CPE: CPE0167(pbg) CPE0771(bgaL) CPE0831(bgaL)
            CPF: CPF_0160 CPF_0766 CPF_1221(lacZ) CPF_1474(lacZ)
            CPR: CPR_0156 CPR_0750
            CBE: Cbei_1232
            CSC: Csac_1018
            TTE: TTE0061
            SCO: SCO3479(SCE65.15c) SCO5689(SC5H4.13) SCO6347(SC3A7.15)
                 SCO6457(SC9B5.24) SCO7407(SC6D11.03c)
            SMA: SAV1027(bga1) SAV1325(bga2) SAV1451(bga3) SAV1760(bga4)
                 SAV2095(bga5) SAV2573(bga6)
            CMI: CMM_0102(bglH) CMM_0355(bgaA) CMM_2109(lacZ) CMM_2700(bgaB)
            ART: Arth_3325
            AAU: AAur_2821(bgaC)
            PAC: PPA1700 PPA1819
            TFU: Tfu_1615
            KRA: Krad_0412 Krad_3970
            SEN: SACE_0306(bga) SACE_1940(lacZ2) SACE_5154(bga2)
                 SACE_6726(lacZ)
            BLO: BL0259(bgaB) BL0978(lacZ) BL1168(bga)
            BAD: BAD_1402 BAD_1582 BAD_1603 BAD_1605
            RBA: RB3405
            LIL: LA0035
            LIC: LIC10031(lacZ)
            BTH: BT_0993 BT_1626 BT_3340 BT_4050 BT_4241
            BFR: BF0192 BF0929 BF3244 BF3375 BF4019
            BFS: BF0029 BF0157 BF0851 BF3084 BF3205 BF3793
            PGI: PG0665(lacZ-1)
            GFO: GFO_1699(lacZ) GFO_1738(lacZ)
            FJO: Fjoh_2038 Fjoh_4102
            RRS: RoseRS_2714
            RCA: Rcas_2493
            DGE: Dgeo_2829
            TTH: TT_P0220 TT_P0222
            TTJ: TTHB032 TTHB034
            TMA: TM0310 TM1193 TM1195
            TPT: Tpet_0607 Tpet_1557
            FNO: Fnod_0419
            TAC: Ta1323
            TVO: TVN0685
            PTO: PTO1259 PTO1453
            PHO: PH0501 PH0511
            PAB: PAB1349 PAB1740 PAB2376(bgaL)
            PFU: PF0073 PF0356 PF0363
            TKO: TK1754 TK1761
            SSO: SSO3019(lacS)
            STO: ST0773
            SAI: Saci_1849(bgaS)
STRUCTURES  PDB: 1BGL  1BGM  1DP0  1F49  1F4A  1F4H  1GHO  1GOW  1JYN  1JYV  
                 1JYW  1JYX  1JYY  1JYZ  1JZ0  1JZ1  1JZ2  1JZ3  1JZ4  1JZ5  
                 1JZ6  1JZ7  1JZ8  1KWG  1KWK  1PX3  1PX4  1TG7  1UWI  1UWQ  
                 1UWR  1UWS  1UWT  1UWU  1XC6  1YQ2  2CEQ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.23
            ExPASy - ENZYME nomenclature database: 3.2.1.23
            ExplorEnz - The Enzyme Database: 3.2.1.23
            ERGO genome analysis and discovery system: 3.2.1.23
            BRENDA, the Enzyme Database: 3.2.1.23
            CAS: 9031-11-2
///
ENTRY       EC 3.2.1.24                 Enzyme
NAME        alpha-mannosidase;
            alpha-D-mannosidase;
            p-nitrophenyl-alpha-mannosidase;
            alpha-D-mannopyranosidase;
            1,2-alpha-mannosidase;
            1,2-alpha-D-mannosidase;
            exo-alpha-mannosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     alpha-D-mannoside mannohydrolase
REACTION    Hydrolysis of terminal, non-reducing alpha-D-mannose residues in
            alpha-D-mannosides
COMMENT     Also hydrolyses alpha-D-lyxosides and heptopyranosides with the same
            configuration at C-2, C-3 and C-4 as mannose.
REFERENCE   1  [PMID:5905120]
  AUTHORS   Li YT.
  TITLE     Presence of alpha-D-mannosidic linkage in glycoproteins. Liberation
            of d-mannose from various glycoproteins by alpha-mannosidase
            isolated from jack bean meal.
  JOURNAL   J. Biol. Chem. 241 (1966) 1010-2.
  ORGANISM  jack bean
REFERENCE   2  [PMID:6428944]
  AUTHORS   Winchester B.
  TITLE     Role of alpha-D-mannosidases in the biosynthesis and catabolism of
            glycoproteins.
  JOURNAL   Biochem. Soc. Trans. 12 (1984) 522-4.
PATHWAY     PATH: map00511  N-Glycan degradation
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01191  alpha-mannosidase
GENES       HSA: 23324(MAN2B2) 4123(MAN2C1) 4125(MAN2B1)
            MMU: 17159(Man2b1) 17160(Man2b2) 73744(Man2c1)
            RNO: 246136(Man2c1)
            CFA: 484932(MAN2B1) 488779(LOC488779) 611620(LOC611620)
            BTA: 282272(MAN2B1)
            SSC: 396847(MAN2B2)
            GGA: 415306(RCJMB04_18f23) 422859(MAN2B2)
            XLA: 431951(MGC83821)
            SPU: 583500(LOC583500) 756277(LOC756277)
            DME: Dmel_CG4606
            CEL: F55D10.1(Alpha-mannosidase)
            ATH: AT3G26720 AT5G66150
            SCE: YGL156W(AMS1)
            AGO: AGOS_AGR385C
            PIC: PICST_35546(MLN1) PICST_83621(AMS1) PICST_84949(MNS1)
            CGR: CAGL0E05148g
            SPO: SPAC513.05
            ANI: AN2936.2
            AFM: AFUA_3G08200
            AOR: AO090005001458
            CNE: CNA06750
            UMA: UM00557.1
            DDI: DDB_0201569(manA) DDB_0231611(manG)
            TCR: 506407.10
            SBO: SBO_1171
            RET: RHE_PF00487(ypf00255)
            RLE: pRL120348(ams1)
            JAN: Jann_2057
            ABA: Acid345_3122
            BHA: BH0791
            BPU: BPUM_0216
            GKA: GK1902
            LMO: lmo2015
            LMF: LMOf2365_0421 LMOf2365_2038 LMOf2365_2040
            LIN: lin2123
            LWE: lwe2034 lwe2035
            SPZ: M5005_Spy_1317
            SPH: MGAS10270_Spy1433
            SPI: MGAS10750_Spy1426
            SPJ: MGAS2096_Spy1338
            SPK: MGAS9429_Spy1311
            SPA: M6_Spy1335
            SPB: M28_Spy1358
            CPE: CPE0856 CPE2080
            CPF: CPF_2337
            CPR: CPR_1405 CPR_2049
            SCO: SCO0948(SCM11.03c)
            SMA: SAV1753(ama1) SAV7277(ama2)
            CMI: CMM_0347(manX) CMM_1259
            PAC: PPA0062 PPA1459
            SEN: SACE_3737(ama2)
            BLO: BL1327 BL1328
            BAD: BAD_1238
            RXY: Rxyl_0070 Rxyl_2051
            SYN: slr0323(ams1)
            SYW: SYNW0267
            SYC: syc2388_d(ams1)
            SYF: Synpcc7942_1703
            SYD: Syncc9605_0261
            SYE: Syncc9902_2083
            SYG: sync_0308
            TEL: tll0290
            GVI: glr0080
            ANA: all0848
            AVA: Ava_4452
            PMT: PMT1839(ams1)
            PMF: P9303_24641
            TER: Tery_3192
            BTH: BT_3774
            BFR: BF0339
            BFS: BF0287
            RRS: RoseRS_1434
            RCA: Rcas_2851
            TMA: TM1851
            FNO: Fnod_0811
            TVO: TVN0209
            PTO: PTO0091
            SSO: SSO3006
            STO: ST1008
STRUCTURES  PDB: 1FO2  1FO3  1O7D  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.24
            ExPASy - ENZYME nomenclature database: 3.2.1.24
            ExplorEnz - The Enzyme Database: 3.2.1.24
            ERGO genome analysis and discovery system: 3.2.1.24
            BRENDA, the Enzyme Database: 3.2.1.24
            CAS: 9025-42-7
///
ENTRY       EC 3.2.1.25                 Enzyme
NAME        beta-mannosidase;
            mannanase;
            mannase;
            beta-D-mannosidase;
            beta-mannoside mannohydrolase;
            exo-beta-D-mannanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     beta-D-mannoside mannohydrolase
REACTION    Hydrolysis of terminal, non-reducing beta-D-mannose residues in
            beta-D-mannosides
REFERENCE   1
  AUTHORS   Adams, M., Richtmyer, N.K. and Hudson, C.S.
  TITLE     Some enzymes present in highly purified invertase preparations; a
            contribution to the study of fructofuranosidases, galactosidases,
            glucosidases and mannosidases.
  JOURNAL   J. Am. Chem. Soc. 65 (1943) 1369-1380.
  ORGANISM  Hordeum vulgare [GN:ehvu]
REFERENCE   2  [PMID:4743897]
  AUTHORS   Bartholomew BA, Perry AL.
  TITLE     The properties of synovial fluid beta-mannosidase activity.
  JOURNAL   Biochim. Biophys. Acta. 315 (1973) 123-7.
  ORGANISM  human [GN:hsa]
REFERENCE   3
  AUTHORS   Deuel, H., Lewuenberger, R. and Huber, G.
  TITLE     Uber den enzymatischen Abbau von Carubin, dem Galaktomannan aus
            Ceratonia siliqua L.
  JOURNAL   Helv. Chim. Acta 33 (1950) 942-946.
  ORGANISM  Ceratonia siliqua
REFERENCE   4  [PMID:14165949]
  AUTHORS   HYLIN JW, SAWAI K.
  TITLE     THE ENZYMATIC HYDROLYSIS OF LEUCAENA GLAUCA GALACTOMANNAN. ISOLATION
            OF CRYSTALLINE GALACTOMANNAN DEPOLYMERASE.
  JOURNAL   J. Biol. Chem. 239 (1964) 990-2.
  ORGANISM  Leucaena glauca
PATHWAY     PATH: map00511  N-Glycan degradation
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01192  beta-mannosidase
GENES       HSA: 4126(MANBA)
            MMU: 110173(Manba)
            CFA: 487883(MANBA)
            BTA: 281909(MANBA)
            GGA: 422712(MANBA)
            XLA: 447024(manba)
            DRE: 393128(manba)
            SPU: 593854(LOC593854)
            DME: Dmel_CG12582
            CEL: C33G3.4(beta-mannosidase)
            PIC: PICST_29300(MAN2) PICST_43820(BMS1)
            ANI: AN1742.2
            AFM: AFUA_6G08840
            AOR: AO090001000556 AO090005000740
            ANG: An11g06540(mndA)
            UMA: UM05229.1
            DDI: DDBDRAFT_0217722
            XFA: XF0846
            XFT: PD1828
            XCC: XCC2891
            XCB: XC_1218
            XCV: XCV3210(manB)
            XAC: XAC3075
            XOO: XOO1780
            XOM: XOO_1683(XOO1683)
            VVU: VV2_1361
            VVY: VVA0201
            VPA: VPA0357
            VFI: VFA0106
            PPR: PBPRA0480
            REH: H16_B0016
            BXE: Bxe_A2529
            BVI: Bcep1808_4779
            BUR: Bcep18194_B1808 Bcep18194_C7540
            BCN: Bcen_4156
            BCH: Bcen2424_4210
            BAM: Bamb_3633
            SME: SMc04255(manB)
            SMD: Smed_1724
            ATU: Atu1523(manA)
            ATC: AGR_C_2809
            RET: RHE_CH00480(manB1) RHE_CH02457(manB2) RHE_CH04047(manB3)
            RLE: RL2792 RL4593
            SCO: SCO6232(SC2H4.14)
            PAC: PPA1033
            TFU: Tfu_0915
            BTH: BT_0458
            BFR: BF1733
            BFS: BF1810(bmnA)
            PGI: PG0032
            RRS: RoseRS_1576
            RCA: Rcas_2644
            TMA: TM1624
STRUCTURES  PDB: 2JE8  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.25
            ExPASy - ENZYME nomenclature database: 3.2.1.25
            ExplorEnz - The Enzyme Database: 3.2.1.25
            ERGO genome analysis and discovery system: 3.2.1.25
            BRENDA, the Enzyme Database: 3.2.1.25
            CAS: 9025-43-8
///
ENTRY       EC 3.2.1.26                 Enzyme
NAME        beta-fructofuranosidase;
            invertase;
            saccharase;
            glucosucrase;
            beta-h-fructosidase;
            beta-fructosidase;
            invertin;
            sucrase;
            maxinvert L 1000;
            fructosylinvertase;
            alkaline invertase;
            acid invertase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     beta-D-fructofuranoside fructohydrolase
REACTION    Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues
            in beta-D-fructofuranosides
ALL_REAC    (other) R00802 R02410 R03635 R03921 R06088(G) R06100(G) R06101(G)
            R06102(G)
COMMENT     Substrates include sucrose; also catalyses fructotransferase
            reactions.
REFERENCE   1
  AUTHORS   Myrback, K.
  TITLE     Invertases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 379-396.
REFERENCE   2  [PMID:4963242]
  AUTHORS   Neumann NP, Lampen JO.
  TITLE     Purification and properties of yeast invertase.
  JOURNAL   Biochemistry. 6 (1967) 468-75.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00052  Galactose metabolism
            PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01193  beta-fructofuranosidase
GENES       ATH: AT1G12240(ATBETAFRUCT4/VAC-INV) AT1G62660 AT2G36190(ATCWINV4)
                 AT3G13790(ATBFRUCT1/ATCWINV1)
            OSA: 4324001 4328018 4329561 4334025 4336515 4337312
            SCE: YIL162W(SUC2)
            AGO: AGOS_AFR529W
            SPO: SPAC8E11.01c SPCC191.11(inv1)
            AFM: AFUA_2G01240 AFUA_5G00480 AFUA_6G05000
            AOR: AO090701000400
            ANG: An08g11070(suc1) An12g08280(inu1)
            CNE: CNK00060
            UMA: UM03605.1
            LMA: LmjF04.0310 LmjF23.0870 LmjF23.0880 LmjF27.2340
            ECE: Z3625
            ECS: ECs3243
            ECP: ECP_2388 ECP_2753
            ECW: EcE24377A_3382(rafD)
            YEN: YE0551(scrB)
            SFL: SF2430
            SFX: S2470
            SFV: SFV_2422
            SSN: SSON_2454
            SDY: SDY_2558
            ECA: ECA0361(scrB)
            SPE: Spro_2082
            PMU: PM1848(scrB)
            MSU: MS0909(sacC)
            APL: APL_2033(scrB)
            VCH: VCA0655
            VCO: VC0395_0599(cscA)
            PST: PSPTO_0885
            PSB: Psyr_0758
            PSP: PSPPH_5192(scrB)
            PFL: PFL_3237(scrB)
            FTU: FTT1644
            FTF: FTF1644
            FTL: FTL_0053
            FTN: FTN_0058
            AHA: AHA_2978
            RSO: RSp1284(scrB)
            ATU: Atu0944(cscA)
            ATC: AGR_C_1721
            RET: RHE_PE00354(ype00178) RHE_PF00050(cscA)
            RLE: pRL120559
            ZMO: ZMO0375(sacC) ZMO0942(invA)
            BSU: BG10596(sacA)
            BHA: BH1858(sacA)
            BAN: BA0753(scrB)
            BAR: GBAA0753(scrB)
            BAA: BA_1337
            BAT: BAS0717
            BCE: BC0774
            BTK: BT9727_0667(scrB)
            BTL: BALH_0689(scrB)
            BLI: BL01929(sacAB) BL03892(sacAA)
            BLD: BLi04016(sacA) BLi04178
            BCL: ABC1455(sacA) ABC3115 ABC3765
            BAY: RBAM_035280(sacA)
            BPU: BPUM_3451(sacA)
            GKA: GK3443
            SAU: SA1846(scrB)
            SAV: SAV2041(scrB)
            SAM: MW1965(scrB)
            SAR: SAR2128(scrB)
            SAS: SAS1946
            SAC: SACOL2029(cscA)
            SAB: SAB1925c(scrB)
            SAA: SAUSA300_1994(scrB)
            SAO: SAOUHSC_02268
            SEP: SE1640
            SER: SERP1495(cscA)
            SHA: SH0991(scrB)
            SSP: SSP0837
            SPY: SPy_1816(scrB)
            SPZ: M5005_Spy_1543(scrB)
            SPM: spyM18_1882
            SPG: SpyM3_1570(scrB)
            SPS: SPs0297
            SPH: MGAS10270_Spy1610(scrB)
            SPI: MGAS10750_Spy1602(scrB)
            SPJ: MGAS2096_Spy1568(scrB)
            SPK: MGAS9429_Spy1547(scrB)
            SPF: SpyM50307(scrB)
            SPA: M6_Spy1532
            SPB: M28_Spy1530(scrB)
            SPN: SP_1724 SP_1795
            SPR: spr1568(scrB) spr1617(sacA)
            SPD: SPD_1534(scrB) SPD_1582
            SAG: SAG1691(scrB)
            SAN: gbs1735
            SAK: SAK_1703(scrB)
            SMU: SMU.1843(scrB)
            STC: str1735(scrB)
            STL: stu1735(scrB)
            SSA: SSA_0455(scrB)
            SGO: SGO_1302 SGO_1858
            LPL: lp_0187(sacA)
            LJO: LJ0518
            LAC: LBA0400(scrB) LBA0505(bfrA)
            LSA: LSA1793(scrB)
            LSL: LSL_0065(scrB)
            LCA: LSEI_2104
            LGA: LGAS_0399
            EFA: EF1603(scrB-1) EFA0069(scrB-2)
            CAC: CAC0425(sacA)
            CPE: CPE1532(sacA)
            CPF: CPF_1783
            CDF: CD1805(sacA)
            CBE: Cbei_3877
            MMO: MMOB4650(scrB)
            MFL: Mfl515 Mfl526
            CGL: NCgl1071(cgl1116) NCgl2554(cgl2643)
            CGB: cg1267 cg2927(scrB)
            CEF: CE1173
            CDI: DIP0989
            CJK: jk1385
            BLO: BL0105(cscA)
            BAD: BAD_1150(cscA)
            SYX: SynWH7803_0536
            TMA: TM1414
            TPT: Tpet_1379
            HMA: rrnAC1479(scrB)
STRUCTURES  PDB: 1UYP  1W2T  2AC1  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.26
            ExPASy - ENZYME nomenclature database: 3.2.1.26
            ExplorEnz - The Enzyme Database: 3.2.1.26
            ERGO genome analysis and discovery system: 3.2.1.26
            BRENDA, the Enzyme Database: 3.2.1.26
            CAS: 9001-57-4
///
ENTRY       EC 3.2.1.27       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
COMMENT     Deleted entry: alpha-1,3-glucosidase (EC 3.2.1.27 created 1961,
            deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.27
            ExPASy - ENZYME nomenclature database: 3.2.1.27
            ExplorEnz - The Enzyme Database: 3.2.1.27
            ERGO genome analysis and discovery system: 3.2.1.27
            BRENDA, the Enzyme Database: 3.2.1.27
///
ENTRY       EC 3.2.1.28                 Enzyme
NAME        alpha,alpha-trehalase;
            trehalase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     alpha,alpha-trehalose glucohydrolase
REACTION    alpha,alpha-trehalose + H2O = 2 D-glucose [RN:R00010 R06103]
ALL_REAC    R00010 R06103(G)
SUBSTRATE   alpha,alpha-trehalose [CPD:C01083];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031]
REFERENCE   1  [PMID:13525386]
  AUTHORS   KALF GF, RIEDER SV.
  TITLE     The purification and properties of trehalase.
  JOURNAL   J. Biol. Chem. 230 (1958) 691-8.
  ORGANISM  Galleria mellonella
REFERENCE   2
  AUTHORS   Myrback, K. and Ortenblad, B.
  TITLE     Trehalose und Hefe. II. Trehalasewirkung von Hefepraparaten.
  JOURNAL   Biochem. Z. 291 (1937) 61-69.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01194  alpha,alpha-trehalase
GENES       HSA: 11181(TREH)
            PTR: 466800(TREH)
            CFA: 489380(TREH)
            SPU: 580425(LOC580425)
            DME: Dmel_CG9364(Treh)
            CEL: C23H3.7(trehalase) F57B10.7(tre-1) T05A12.2(tre-2)
                 W05E10.4(trehalase)
            ATH: AT4G24040(ATTRE1)
            CME: CMH100C CMN097C
            SCE: YBR001C(NTH2) YDR001C(NTH1) YPR026W(ATH1)
            AGO: AGOS_AER001C AGOS_AGL271W
            PIC: PICST_64968(NTH2) PICST_80169(ATH1)
            CGR: CAGL0K05137g CAGL0M10439g
            SPO: SPBC660.07
            ANI: AN5635.2
            AFM: AFUA_4G13530
            AOR: AO090009000215
            CNE: CNB02790 CNG00690
            ECU: ECU02_1370
            DDI: DDBDRAFT_0185541
            ECO: b1197(treA) b3519(treF)
            ECJ: JW1186(treA) JW3487(treF)
            ECE: Z1968(treA) Z4932(treF)
            ECS: ECs4399
            ECC: c1654(treA) c4330(treF)
            ECI: UTI89_C1389(treA) UTI89_C4051(treF)
            ECP: ECP_1245 ECP_3619
            ECV: APECO1_2929(treF) APECO1_314(treA)
            ECW: EcE24377A_1343(treA) EcE24377A_4007(treF)
            ECX: EcHS_A1301(treA) EcHS_A3722(treF)
            STY: STY4200(treF)
            STT: t3914(treF)
            SPT: SPA1077(treA) SPA3459(treF)
            SEC: SC1789(treA) SC3537(treF)
            STM: STM1796(treA) STM3603(treF)
            SFL: SF1200(treA) SF3550(treF)
            SFX: S1284(treA) S4217(treF)
            SFV: SFV_1211(treA) SFV_3570(treF)
            SSN: SSON_3567(treF)
            SBO: SBO_3518(treF)
            SDY: SDY_1246(treA)
            SGL: SG1886
            ENT: Ent638_2355 Ent638_3914
            XCC: XCC3529(treA)
            XCB: XC_0631
            XCV: XCV0660(treA)
            XAC: XAC0604(treA)
            XOO: XOO4030(treA)
            XOM: XOO_3799(XOO3799)
            PAE: PA2416(treA)
            PAU: PA14_33450(treA)
            PAP: PSPA7_2843
            SFR: Sfri_3506
            PAT: Patl_1825
            CBU: CBU_1346
            CBD: COXBU7E912_1435(treA)
            LPF: lpl1841
            LPP: lpp1844
            FTL: FTL_1150 FTL_1151
            FTN: FTN_1328(treA)
            RSO: RSp0277(treA)
            REH: H16_B2096(treA)
            BMA: BMAA1166
            BML: BMA10299_0075
            BMN: BMA10247_A1543
            BVI: Bcep1808_5353
            BUR: Bcep18194_B0851
            BCN: Bcen_3502
            BCH: Bcen2424_4864
            BAM: Bamb_4237
            BPS: BPSS0671
            BPM: BURPS1710b_A2235(treA)
            BPL: BURPS1106A_A0908
            BPD: BURPS668_A0995
            BTE: BTH_II1752
            AAV: Aave_0217 Aave_2117
            ABA: Acid345_0922
            GKA: GK1678
            MBO: Mb2029(otsB1)
            MBB: BCG_2023(otsB1)
            FAL: FRAAL6634(pgcM)
            ANA: all0166(treH)
            AVA: Ava_1426
            GFO: GFO_0755(treA)
            FJO: Fjoh_1262
STRUCTURES  PDB: 2JF4  2JG0  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.28
            ExPASy - ENZYME nomenclature database: 3.2.1.28
            ExplorEnz - The Enzyme Database: 3.2.1.28
            ERGO genome analysis and discovery system: 3.2.1.28
            BRENDA, the Enzyme Database: 3.2.1.28
            CAS: 9025-52-9
///
ENTRY       EC 3.2.1.29       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
COMMENT     Deleted entry: chitobiase. Now included with EC 3.2.1.52,
            beta-N-acetylhexosaminidase (EC 3.2.1.29 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.29
            ExPASy - ENZYME nomenclature database: 3.2.1.29
            ExplorEnz - The Enzyme Database: 3.2.1.29
            ERGO genome analysis and discovery system: 3.2.1.29
            BRENDA, the Enzyme Database: 3.2.1.29
///
ENTRY       EC 3.2.1.30       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
COMMENT     Deleted entry: beta-D-acetylglucosaminidase. Now included with EC
            3.2.1.52, beta-N-acetylhexosaminidase (EC 3.2.1.30 created 1961,
            deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.30
            ExPASy - ENZYME nomenclature database: 3.2.1.30
            ExplorEnz - The Enzyme Database: 3.2.1.30
            ERGO genome analysis and discovery system: 3.2.1.30
            BRENDA, the Enzyme Database: 3.2.1.30
///
ENTRY       EC 3.2.1.31                 Enzyme
NAME        beta-glucuronidase;
            beta-glucuronide glucuronohydrolase glucuronidase;
            exo-beta-D-glucuronidase;
            ketodase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     beta-D-glucuronoside glucuronosohydrolase
REACTION    a beta-D-glucuronoside + H2O = D-glucuronate + an alcohol
            [RN:R01478]
ALL_REAC    R01478;
            (other) R04979 R07818(G)
SUBSTRATE   beta-D-glucuronoside [CPD:C03033];
            H2O [CPD:C00001]
PRODUCT     D-glucuronate [CPD:C00191];
            alcohol [CPD:C00069]
REFERENCE   1
  AUTHORS   Diez, T. and Cabezas, J.A.
  TITLE     Properties of two molecular forms of beta-glucuronidase from the
            mollusc Littorina littorea L.
  JOURNAL   Eur. J. Biochem. 93 (1978) 301-311.
  ORGANISM  Littorina littorea
REFERENCE   2  [PMID:13271452]
  AUTHORS   DOYLE ML, KATZMAN PA, DOISY EA.
  TITLE     Production and properties of bacterial beta-glucuronidase.
  JOURNAL   J. Biol. Chem. 217 (1955) 921-30.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:14376216]
  AUTHORS   FISHMAN WH.
  TITLE     Not Available
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 16 (1955) 361-409.
REFERENCE   4
  AUTHORS   Levvy, G.A. and Marsh, C.A.
  TITLE     beta-Glucuronidase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 397-407.
REFERENCE   5
  AUTHORS   Wakabayashi, M. and Fishman, W.H.
  TITLE     The comparative ability of beta-glucuronidase preparations (liver,
            Escherichia coli, Helix pomatia, and Patella vulgata) to hydrolyze
            certain steroid glucosiduronic acids.
  JOURNAL   J. Biol. Chem. 236 (1961) 996-1001.
  ORGANISM  Escherichia coli [GN:eco], Helix pomatia, Patella vulgata, cow
            [GN:bta]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00500  Starch and sucrose metabolism
            PATH: map00531  Glycosaminoglycan degradation
            PATH: map00860  Porphyrin and chlorophyll metabolism
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01195  beta-glucuronidase
GENES       HSA: 2990(GUSB)
            PTR: 463443(GUSB)
            MMU: 110006(Gusb)
            RNO: 24434(Gusb)
            CFA: 403831(GUSB)
            GGA: 427823(RCJMB04_28l23)
            SPU: 575689(LOC575689)
            DME: Dmel_CG2135
            CEL: Y105E8B.9
            ANI: AN5361.2
            AOR: AO090038000009
            ECO: b1617(uidA)
            ECJ: JW1609(uidA)
            ECE: Z2621m
            ECC: c2009(uidA)
            ECI: UTI89_C1805(uidA)
            ECP: ECP_1561
            ECV: APECO1_700(uidA)
            ECW: EcE24377A_1825(uidA)
            ECX: EcHS_A1692(uidA)
            SFL: SF1640(uidA)
            SFX: S1771(uidA)
            SFV: SFV_1633(uidA)
            SSN: SSON_1543(uidA)
            HSO: HS_1330(uidA)
            SDE: Sde_2632
            SIT: TM1040_3871
            ABA: Acid345_0579
            SHA: SH2645
            SPH: MGAS10270_Spy1174
            SAG: SAG0698
            SAN: gbs0671
            SAK: SAK_0824
            LBR: LVIS_0138
            CPE: CPE0147(bglR)
            CEF: CE2379
            AAU: AAur_0068
            PAC: PPA2333
            FJO: Fjoh_2082
            TMA: TM1062
            TPT: Tpet_0490 Tpet_1689
            SSO: SSO3036(gusB)
STRUCTURES  PDB: 1BHG  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.31
            ExPASy - ENZYME nomenclature database: 3.2.1.31
            ExplorEnz - The Enzyme Database: 3.2.1.31
            ERGO genome analysis and discovery system: 3.2.1.31
            BRENDA, the Enzyme Database: 3.2.1.31
            CAS: 9001-45-0
///
ENTRY       EC 3.2.1.32                 Enzyme
NAME        xylan endo-1,3-beta-xylosidase;
            xylanase;
            endo-1,3-beta-xylanase;
            endo-1,3-xylanase;
            1,3-beta-xylanase;
            endo-1,3-beta-xylanase;
            1,3-xylanase;
            beta-1,3-xylanase;
            endo-beta-1,3-xylanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,3-beta-D-xylan xylanohydrolase
REACTION    Random hydrolysis of 1,3-beta-D-glycosidic linkages in
            1,3-beta-D-xylans
REFERENCE   1
  AUTHORS   Aoki, T., Araki, T. and Kitamikado, M.
  TITLE     Purification and characterization of an endo-beta-1,3-xylanase from
            Vibrio species.
  JOURNAL   Nippon Suisan Gakkaishi 54 (1988) 277-281.
  ORGANISM  Vibrio sp.
REFERENCE   2
  AUTHORS   Chen, W.P., Matsuo, M. and Tsuneo, Y.
  TITLE     Purification and some properties of beta-1,3-xylanase from
            Aspergillus terreus A-07.
  JOURNAL   Agric. Biol. Chem. 50 (1986) 1183-1194.
  ORGANISM  Aspergillus terreus
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.32
            ExPASy - ENZYME nomenclature database: 3.2.1.32
            ExplorEnz - The Enzyme Database: 3.2.1.32
            ERGO genome analysis and discovery system: 3.2.1.32
            BRENDA, the Enzyme Database: 3.2.1.32
            CAS: 9025-55-2
///
ENTRY       EC 3.2.1.33                 Enzyme
NAME        amylo-alpha-1,6-glucosidase;
            amylo-1,6-glucosidase;
            dextrin 6-alpha-D-glucosidase;
            amylopectin 1,6-glucosidase;
            dextrin-1,6-glucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     glycogen phosphorylase-limit dextrin alpha-1,6-glucohydrolase
REACTION    Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen
            phosphorylase limit dextrin
ALL_REAC    (other) R02109 R06158(G)
COMMENT     This enzyme hydrolyses an unsubstituted (1->4)-linked glucose chain.
            The enzyme activity found in mammals and yeast is in a polypeptide
            chain containing two active centres. The other activity is similar
            to that of EC 2.4.1.25 (4-alpha-glucanotransferase), which acts on
            the glycogen phosphorylase limit dextrin chains to expose the single
            glucose residues, which the 6-alpha-glucosidase activity can then
            hydrolyse. Together, these two activities constitute the glycogen
            debranching system.
REFERENCE   1
  AUTHORS   Brown, D.H. and Brown, B.I.
  TITLE     Enzymes of glycogen debranching: Amylo-1,6-glucosidase (I) and
            oligo-1,4->1,4-glucanotransferase (II).
  JOURNAL   Methods Enzymol. 8 (1966) 515-524.
  ORGANISM  rabbit
REFERENCE   2  [PMID:5424210]
  AUTHORS   Lee EY, Carter JH, Nielsen LD, Fischer EH.
  TITLE     Purification and properties of yeast
            amylo-1,6-glucosidase--oligo-1,4 leads to 1,4-glucantransferase.
  JOURNAL   Biochemistry. 9 (1970) 2347-55.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:5805288]
  AUTHORS   Nelson TE, Kolb E, Larner J.
  TITLE     Purification and properties of rabbit muscle
            amylo-1,6-glucosidase-oligo-1,4-1,4-transferase.
  JOURNAL   Biochemistry. 8 (1969) 1419-28.
  ORGANISM  rabbit
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01196  amylo-1,6-glucosidase
GENES       HSA: 178(AGL)
            PTR: 469392(AGL)
            MMU: 77559(Agl)
            GGA: 424474(AGL)
            CEL: R06A4.8
            SCE: YPR184W(GDB1)
            AGO: AGOS_AEL276C
            CGR: CAGL0G09977g
            AFM: AFUA_1G02140
            AOR: AO090005000884
            CNE: CNJ03090
            UMA: UM03949.1
            DDI: DDBDRAFT_0219237
            CPV: cgd6_880
            EHI: 77.t00009
            VFI: VF2048
            BML: BMA10299_0038
            BMN: BMA10247_A1583
            BXE: Bxe_B1135
            BCH: Bcen2424_4932
            BPL: BURPS1106A_1910 BURPS1106A_A0852
            BPD: BURPS668_1897 BURPS668_A0945
            RPE: RPE_1189
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.33
            ExPASy - ENZYME nomenclature database: 3.2.1.33
            ExplorEnz - The Enzyme Database: 3.2.1.33
            ERGO genome analysis and discovery system: 3.2.1.33
            BRENDA, the Enzyme Database: 3.2.1.33
            CAS: 9012-47-9
///
ENTRY       EC 3.2.1.34       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
COMMENT     Deleted entry: chondroitinase. Now included with EC 3.2.1.35
            hyalurononglucosaminidase (EC 3.2.1.34 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.34
            ExPASy - ENZYME nomenclature database: 3.2.1.34
            ExplorEnz - The Enzyme Database: 3.2.1.34
            ERGO genome analysis and discovery system: 3.2.1.34
            BRENDA, the Enzyme Database: 3.2.1.34
///
ENTRY       EC 3.2.1.35                 Enzyme
NAME        hyaluronoglucosaminidase;
            hyaluronidase;
            hyaluronoglucosidase;
            chondroitinase;
            chondroitinase I
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     hyaluronate 4-glycanohydrolase
REACTION    Random hydrolysis of 1->4-linkages between
            N-acetyl-beta-D-glucosamine and D-glucuronate residues in
            hyaluronate
ALL_REAC    (other) R07824(G) R07825(G)
COMMENT     Also hydrolyses 1,4-beta-D-glycosidic linkages between
            N-acetyl-galactosamine or N-acetylgalactosamine sulfate and
            glucuronic acid in chondroitin, chondroitin 4- and 6-sulfates, and
            dermatan.
REFERENCE   1
  AUTHORS   Meyer, K., Hoffman, P. and Linker, A.
  TITLE     Hyaluronidases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 447-460.
REFERENCE   2
  AUTHORS   Rapport, M.M., Myer, K. and Linker, A.
  TITLE     Analysis of the products formed on hydrolysis of hyaluronic acid by
            testicular hyaluronidase.
  JOURNAL   J. Am. Chem. Soc. 73 (1951) 2416-2420.
  ORGANISM  human [GN:hsa]
REFERENCE   3
  AUTHORS   Weissmann, B.
  TITLE     The transglycosylative action of testicular hyaluronidase.
  JOURNAL   J. Biol. Chem. 216 (1955) 783-794.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00531  Glycosaminoglycan degradation
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01197  hyaluronoglucosaminidase
GENES       HSA: 3373(HYAL1) 6677(SPAM1) 8692(HYAL2)
            PTR: 472498(SPAM1)
            MMU: 15586(Hyal1) 15587(Hyal2) 20690(Spam1)
            RNO: 367166(Hyal1) 64468(Hyal2)
            CFA: 475211(SPAM1) 484760(HYAL2) 608602(HYAL1)
            BTA: 281838(HYAL2) 353352(SPAM1)
            SSC: 397074(SPAM-1) 404697(HYAL2) 404698(HYAL1)
            GGA: 415908(HYAL2) 417749(SPAM1) 426739(HYAL1)
            XLA: 380470(hyal2)
            SPU: 584769(LOC584769)
            SPY: SPy_0701(hylP1)
            SPZ: M5005_Spy_1314(hyl) M5005_Spy_1423
            SPM: spyM18_0770(hylP)
            SPG: SpyM3_1214(hylP.4)
            SPS: SPs0648
            SPH: MGAS10270_Spy0590 MGAS10270_Spy1310 MGAS10270_Spy1430(hyl)
            SPI: MGAS10750_Spy0615 MGAS10750_Spy1285 MGAS10750_Spy1423(hyl)
            SPJ: MGAS2096_Spy0593 MGAS2096_Spy1334(hyl) MGAS2096_Spy1449
            SPK: MGAS9429_Spy0586 MGAS9429_Spy0843 MGAS9429_Spy1308(hyl)
                 MGAS9429_Spy1425
            SPF: SpyM50680
            SPA: M6_Spy0059 M6_Spy0993 M6_Spy1203 M6_Spy1332 M6_Spy1348
                 M6_Spy1550
            SPB: M28_Spy1233 M28_Spy1355(hyl)
            CPE: CPE0191(nagH)
            CPF: CPF_0184(nagH)
STRUCTURES  PDB: 1FCQ  1FCU  1FCV  2ATM  2CBI  2CBJ  2J88  2PE4  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.35
            ExPASy - ENZYME nomenclature database: 3.2.1.35
            ExplorEnz - The Enzyme Database: 3.2.1.35
            ERGO genome analysis and discovery system: 3.2.1.35
            BRENDA, the Enzyme Database: 3.2.1.35
            CAS: 37326-33-3
///
ENTRY       EC 3.2.1.36                 Enzyme
NAME        hyaluronoglucuronidase;
            hyaluronidase;
            glucuronoglucosaminoglycan hyaluronate lyase;
            orgelase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     hyaluronate 3-glycanohydrolase
REACTION    Random hydrolysis of 1,3-linkages between beta-D-glucuronate and
            N-acetyl-D-glucosamine residues in hyaluronate
REFERENCE   1
  AUTHORS   Linker, A., Meyer, K. and Hoffman, P.
  TITLE     The production of hyaluronate oligosaccharides by leech
            hyaluronidase and alkali.
  JOURNAL   J. Biol. Chem. 235 (1960) 924-927.
  ORGANISM  leech
REFERENCE   2
  AUTHORS   Meyer, K., Hoffman, P. and Linker, A.
  TITLE     Hyaluronidases.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 447-460.
GENES       SYR: SynRCC307_0447
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.36
            ExPASy - ENZYME nomenclature database: 3.2.1.36
            ExplorEnz - The Enzyme Database: 3.2.1.36
            ERGO genome analysis and discovery system: 3.2.1.36
            BRENDA, the Enzyme Database: 3.2.1.36
            CAS: 37288-34-9
///
ENTRY       EC 3.2.1.37                 Enzyme
NAME        xylan 1,4-beta-xylosidase;
            xylobiase;
            beta-xylosidase;
            exo-1,4-beta-xylosidase;
            beta-D-xylopyranosidase;
            beta-xylosidase;
            beta-xylosidase;
            exo-1,4-xylosidase;
            exo-1,4-beta-D-xylosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,4-beta-D-xylan xylohydrolase
REACTION    Hydrolysis of 1,4-beta-D-xylans, to remove successive D-xylose
            residues from the non-reducing termini
ALL_REAC    (other) R01433 R06203(G)
COMMENT     Also hydrolyses xylobiose. Some other exoglycosidase activities have
            been found associated with this enzyme in sheep liver.
REFERENCE   1  [PMID:2503402]
  AUTHORS   Chinchetru MA, Cabezas JA, Calvo P.
  TITLE     Purification and characterization of a broad specificity
            beta-glucosidase from sheep liver.
  JOURNAL   Int. J. Biochem. 21 (1989) 469-76.
REFERENCE   2  [PMID:14403433]
  AUTHORS   HOWARD BH, JONES G, PURDOM MR.
  TITLE     The pentosanases of some rumen bacteria.
  JOURNAL   Biochem. J. 74 (1960) 173-80.
  ORGANISM  Butyrivibrio sp.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
            PATH: map00520  Nucleotide sugars metabolism
ORTHOLOGY   KO: K01198  xylan 1,4-beta-xylosidase
GENES       AFM: AFUA_1G01230 AFUA_2G13190 AFUA_7G06110 AFUA_8G04710
            ANG: An01g09960(xlnD)
            ECO: b0271(yagH)
            ECJ: JW0264(yagH)
            XCC: XCC1178(xylB) XCC3975(xynB) XCC4064 XCC4105(xylB)
            XCB: XC_3064 XC_4065 XC_4154 XC_4196
            XCV: XCV0150(xylB1) XCV1325 XCV4148(xynB1) XCV4281(xylB2)
                 XCV4336(xylB3)
            XAC: XAC1275(xylB) XAC4058(xynB) XAC4183 XAC4230(xylB)
            XOO: XOO4422(xylB)
            XOM: XOO_4165(XOO4165) XOO_4277(XOO4277)
            MMW: Mmwyl1_3059
            SME: SMc04247
            RET: RHE_CH02453(xynA)
            RLE: RL2788 RL4418(xynB)
            CCR: CC_0989 CC_2357 CC_2802
            BSU: BG11987(xynB)
            BHA: BH1068 BH3683(xynB)
            BLI: BL03023(xynBB)
            BLD: BLi00864(xynB)
            BCL: ABC0554(xynB) ABC1148
            BAY: RBAM_017330(xynB) RBAM_025570(xsa)
            BPU: BPUM_1831(xynB)
            OIH: OB2087 OB3125
            GTN: GTNG_1758
            LLA: L0234(xynB)
            LLM: llmg_1320
            LBR: LVIS_0375 LVIS_2285
            CAC: CAC3452(xynD)
            CBE: Cbei_3047
            CSC: Csac_2409
            SMA: SAV1453(xynB1)
            CMI: CMM_0103(bglI)
            AAU: AAur_1139
            BAD: BAD_0428(xynB)
STRUCTURES  PDB: 1PX8  1UHV  1Y7B  1YI7  1YIF  2BFG  2BS9  2EXH  2EXI  2EXJ  
                 2EXK  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.37
            ExPASy - ENZYME nomenclature database: 3.2.1.37
            ExplorEnz - The Enzyme Database: 3.2.1.37
            ERGO genome analysis and discovery system: 3.2.1.37
            BRENDA, the Enzyme Database: 3.2.1.37
            CAS: 9025-53-0
///
ENTRY       EC 3.2.1.38                 Enzyme
NAME        beta-D-fucosidase;
            beta-fucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     beta-D-fucoside fucohydrolase
REACTION    Hydrolysis of terminal non-reducing beta-D-fucose residues in
            beta-D-fucosides
REFERENCE   1  [PMID:6413126]
  AUTHORS   Chinchetru MA, Cabezas JA, Calvo P.
  TITLE     Characterization and kinetics of beta-D-gluco/fuco/galactosidase
            from sheep liver.
  JOURNAL   Comp. Biochem. Physiol. B. 75 (1983) 719-28.
  ORGANISM  sheep
REFERENCE   2  [PMID:2503402]
  AUTHORS   Chinchetru MA, Cabezas JA, Calvo P.
  TITLE     Purification and characterization of a broad specificity
            beta-glucosidase from sheep liver.
  JOURNAL   Int. J. Biochem. 21 (1989) 469-76.
  ORGANISM  sheep
REFERENCE   3  [PMID:6811346]
  AUTHORS   Rodriguez JA, Cabezas JA, Calvo P.
  TITLE     beta-Fucosidase, beta-glucosidase and beta-galactosidase activities
            associated in bovine liver.
  JOURNAL   Int. J. Biochem. 14 (1982) 695-8.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:4782520]
  AUTHORS   Wiederschain GY, Prokopenkov AA.
  TITLE     Beta-D-galactosidase and beta-D-fucosidase of pig kidney.
  JOURNAL   Arch. Biochem. Biophys. 158 (1973) 539-43.
  ORGANISM  pig [GN:ssc]
REFERENCE   5  [PMID:6789883]
  AUTHORS   Wiederschain GYa, Beyer EM, Klyashchitsky BA, Shashkov AS.
  TITLE     Specificity patterns of different types of human fucosidase.
            Recognition of a certain region of the pyranose ring in sugars by
            the enzymes.
  JOURNAL   Biochim. Biophys. Acta. 659 (1981) 434-44.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.38
            ExPASy - ENZYME nomenclature database: 3.2.1.38
            ExplorEnz - The Enzyme Database: 3.2.1.38
            ERGO genome analysis and discovery system: 3.2.1.38
            BRENDA, the Enzyme Database: 3.2.1.38
            CAS: 9025-34-7
///
ENTRY       EC 3.2.1.39                 Enzyme
NAME        glucan endo-1,3-beta-D-glucosidase;
            endo-1,3-beta-glucanase;
            laminarinase;
            laminaranase;
            oligo-1,3-glucosidase;
            endo-1,3-beta-glucanase;
            callase;
            beta-1,3-glucanase;
            kitalase;
            1,3-beta-D-glucan 3-glucanohydrolase;
            endo-(1,3)-beta-D-glucanase;
            (1->3)-beta-glucan 3-glucanohydrolase;
            endo-1,3-beta-D-glucanase;
            endo-1,3-beta-glucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,3-beta-D-glucan glucanohydrolase
REACTION    Hydrolysis of 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans
ALL_REAC    (other) R00308 R06204(G)
COMMENT     Different from EC 3.2.1.6 endo-1,3(4)-beta-glucanase. Very limited
            action on mixed-link (1,3-1,4-)-beta-D-glucans. Hydrolyses
            laminarin, paramylon and pachyman.
REFERENCE   1
  AUTHORS   Chesters, C.G.C. and Bull, A.T.
  TITLE     The enzymic degradation of laminarin. 2. The multicomponent nature
            of fungal laminarinases.
  JOURNAL   Biochem. J. 86 (1963) 31-38.
  ORGANISM  Penicillium stipitatum, Streptomyces sp., Trichoderma viride,
            Myrothecium verrucaria
REFERENCE   2
  AUTHORS   Reese, E.T. and Mandels, M.
  TITLE     beta-D-1,3-Glucanases in fungi.
  JOURNAL   Can. J. Microbiol. 5 (1959) 173-185.
  ORGANISM  Aspergillus niger
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01199  glucan endo-1,3-beta-D-glucosidase
GENES       ATH: AT3G57260(BGL2)
            TET: TTHERM_00243770 TTHERM_00637420 TTHERM_00956460
                 TTHERM_00956480
            SFR: Sfri_1319
            SAZ: Sama_1396
            SDE: Sde_3121
            PIN: Ping_0554
            RLE: RL3815
            MMR: Mmar10_0247
            NAR: Saro_1608
            SAL: Sala_0919
            RHA: RHA1_ro05769 RHA1_ro05771
            FJO: Fjoh_2435
            FNO: Fnod_0286 Fnod_1600
STRUCTURES  PDB: 1GHS  2CYG  2HYK  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.39
            ExPASy - ENZYME nomenclature database: 3.2.1.39
            ExplorEnz - The Enzyme Database: 3.2.1.39
            ERGO genome analysis and discovery system: 3.2.1.39
            BRENDA, the Enzyme Database: 3.2.1.39
            CAS: 9025-37-0
///
ENTRY       EC 3.2.1.40                 Enzyme
NAME        alpha-L-rhamnosidase;
            alpha-L-rhamnosidase T;
            alpha-L-rhamnosidase N
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     alpha-L-rhamnoside rhamnohydrolase
REACTION    Hydrolysis of terminal non-reducing alpha-L-rhamnose residues in
            alpha-L-rhamnosides
REFERENCE   1  [PMID:5855461]
  AUTHORS   Rosenfeld EL, Wiederschein GY.
  TITLE     The metabolism of L-rhamnose in animal tissues.
  JOURNAL   Bull. Soc. Chim. Biol. (Paris). 47 (1965) 1433-40.
  ORGANISM  pig [GN:ssc]
ORTHOLOGY   KO: K05989  
GENES       RET: RHE_PC00040
            RLE: pRL100260
            BCZ: BCZK2019(ramA)
            BTK: BT9727_2019(ramA)
            LPL: lp_3471(ram1) lp_3473(ram2)
            RHA: RHA1_ro03902
            CMI: CMM_0105(ramA)
            ART: Arth_1840
            RBA: RB700(ramA)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.40
            ExPASy - ENZYME nomenclature database: 3.2.1.40
            ExplorEnz - The Enzyme Database: 3.2.1.40
            ERGO genome analysis and discovery system: 3.2.1.40
            BRENDA, the Enzyme Database: 3.2.1.40
            CAS: 37288-35-0
///
ENTRY       EC 3.2.1.41                 Enzyme
NAME        pullulanase;
            limit dextrinase (erroneous);
            amylopectin 6-glucanohydrolase;
            bacterial debranching enzyme;
            debranching enzyme;
            alpha-dextrin endo-1,6-alpha-glucosidase;
            R-enzyme
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     pullulan alpha-1,6-glucanohydrolase
REACTION    Hydrolysis of (1->6)-linked maltotriose units] and in amylopectin
            and glycogen, and the alpha- and beta-limit dextrins of amylopectin
            and glycogen
COMMENT     Different from EC 3.2.1.142 (limit dextrinase) in its action on
            glycogen, and its rate of hydrolysis of limit dextrins. Its action
            on amylopectin is complete. Maltose is the smallest sugar that it
            can release from an alpha-(1->6)-linkage.
REFERENCE   1
  AUTHORS   Lee, E.Y.C. and Whelan, W.J.
  TITLE     Glycogen and starch debranching enzymes.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 5, Academic Press,
            New York, 1972, p. 191-234.
REFERENCE   2
  AUTHORS   Bender, H. and Wallenfels, K.
  TITLE     Pullulanase (an amylopectin and glycogen debranching enzyme) from
            Aerobacter aerogenes.
  JOURNAL   Methods Enzymol. 8 (1966) 555-559.
  ORGANISM  Aerobacter aerogenes
REFERENCE   3
  AUTHORS   Manners, D.J.
  TITLE     Observations on the specificity and nomenclature of starch
            debranching enzymes.
  JOURNAL   J. Appl. Glycosci. 44 (1997) 83-85.
ORTHOLOGY   KO: K01200  pullulanase
GENES       AFM: AFUA_2G03230
            VCO: VC0395_A2273
            PAT: Patl_1941
            FTU: FTT0412c(pulB)
            FTF: FTF0412c(pulB)
            FTW: FTW_1661(pulA)
            FTL: FTL_0482
            FTH: FTH_0480(pul)
            FTN: FTN_0512(glgX)
            AHA: AHA_0628
            REH: H16_B1560(pulA)
            AZO: azo1794(glgX)
            BBA: Bd1228(amyX)
            ABA: Acid345_2329
            BSU: BG12566(amyX)
            BHA: BH3264(amyX)
            BAN: BA2728 BA4953
            BAR: GBAA2728 GBAA4953
            BAA: BA_3251 BA_5371
            BAT: BAS2542 BAS4597
            BCE: BC2734
            BCA: BCE_2761 BCE_4844
            BCZ: BCZK2463(pulA) BCZK4452(amyX)
            BTK: BT9727_2498(pulA) BT9727_4434(amyX)
            BTL: BALH_2451(pulA) BALH_4277(amyX)
            BLI: BL00040(amyX)
            OIH: OB0405
            LLA: L102412(apu)
            SPZ: M5005_Spy_1679 M5005_Spy_1680(pulA)
            SPH: MGAS10270_Spy1749(pulA)
            SPI: MGAS10750_Spy1774(pulA)
            SPJ: MGAS2096_Spy1703(pulA)
            SPK: MGAS9429_Spy1681(pulA) MGAS9429_Spy1683
            SPA: M6_Spy1688
            SPB: M28_Spy1668(pulA)
            SPN: SP_1118
            SPR: spr1025(pulI)
            SPD: SPD_1002(pulA)
            SAG: SAG0852
            SAN: gbs0870
            SAK: SAK_0975(pulA)
            SMU: SMU.1541(pulA)
            SSA: SSA_0453 SSA_1482(pulI) SSA_2268(pulA)
            SGO: SGO_0099(pulA-2) SGO_1388(pulA-1)
            LAC: LBA0686 LBA1710(amyX)
            CAC: CAC2679
            CPE: CPE1552(pulA) CPE1587(pulB)
            CPF: CPF_1803(pulA) CPF_1839
            CPR: CPR_0084 CPR_1522 CPR_1558
            CNO: NT01CX_0439(pulA)
            MPU: MYPU_6440(pulA)
            MMO: MMOB4000(pulA)
            MHY: mhp605
            MHJ: MHJ_0587(pulA)
            MHP: MHP7448_0587(pulA)
            BAD: BAD_0708(pulA)
            BTH: BT_4689
            DRA: DR_0405
            TTH: TTC1198
            TMA: TM1845
            PFU: PF1108
STRUCTURES  PDB: 2FGZ  2FH6  2FH8  2FHB  2FHC  2FHF  2J71  2J72  2J73  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.41
            ExPASy - ENZYME nomenclature database: 3.2.1.41
            ExplorEnz - The Enzyme Database: 3.2.1.41
            ERGO genome analysis and discovery system: 3.2.1.41
            BRENDA, the Enzyme Database: 3.2.1.41
            CAS: 9075-68-7
///
ENTRY       EC 3.2.1.42                 Enzyme
NAME        GDP-glucosidase;
            guanosine diphosphoglucosidase;
            guanosine diphosphate D-glucose glucohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     GDP-glucose glucohydrolase
REACTION    GDP-glucose + H2O = D-glucose + GDP [RN:R00337]
ALL_REAC    R00337
SUBSTRATE   GDP-glucose [CPD:C00394];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031];
            GDP [CPD:C00035]
REFERENCE   1  [PMID:5963308]
  AUTHORS   Sonnino S, Carminatti H, Cabib E.
  TITLE     Guanosine diphosphate D-glucose glucohydrolase.
  JOURNAL   Arch. Biochem. Biophys. 116 (1966) 26-33.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.42
            ExPASy - ENZYME nomenclature database: 3.2.1.42
            ExplorEnz - The Enzyme Database: 3.2.1.42
            ERGO genome analysis and discovery system: 3.2.1.42
            BRENDA, the Enzyme Database: 3.2.1.42
            CAS: 37288-36-1
///
ENTRY       EC 3.2.1.43                 Enzyme
NAME        beta-L-rhamnosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     beta-L-rhamnoside rhamnohydrolase
REACTION    Hydrolysis of terminal, non-reducing beta-L-rhamnose residues in
            beta-L-rhamnosides
REFERENCE   1
  AUTHORS   Barker, S.A., Somers, P.J. and Stacey, M.
  TITLE     Arrangement of the L-rhamnose units in Diplococcus pneumoniae type
            II polysaccharide.
  JOURNAL   Carbohydr. Res. 1 (1965) 106-115.
  ORGANISM  Klebsiella aerogenes
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.43
            ExPASy - ENZYME nomenclature database: 3.2.1.43
            ExplorEnz - The Enzyme Database: 3.2.1.43
            ERGO genome analysis and discovery system: 3.2.1.43
            BRENDA, the Enzyme Database: 3.2.1.43
            CAS: 37288-37-2
///
ENTRY       EC 3.2.1.44                 Enzyme
NAME        fucoidanase;
            alpha-L-fucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     poly(1,2-alpha-L-fucoside-4-sulfate) glycanohydrolase
REACTION    Endohydrolysis of 1,2-alpha-L-fucoside linkages in fucoidan without
            release of sulfate
REFERENCE   1
  AUTHORS   Thanassi, N.M. and Nakada, H.I.
  TITLE     Enzymic degradation of fucoidan by enzymes from the hepatopancreas
            of abalone, Halotus species.
  JOURNAL   Arch. Biochem. Biophys. 118 (1967) 172-177.
  ORGANISM  Halotus sp., rat [GN:rno], cow [GN:bta]
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.44
            ExPASy - ENZYME nomenclature database: 3.2.1.44
            ExplorEnz - The Enzyme Database: 3.2.1.44
            ERGO genome analysis and discovery system: 3.2.1.44
            BRENDA, the Enzyme Database: 3.2.1.44
            CAS: 37288-38-3
///
ENTRY       EC 3.2.1.45                 Enzyme
NAME        glucosylceramidase;
            psychosine hydrolase;
            glucosphingosine glucosylhydrolase;
            GlcCer-beta-glucosidase;
            beta-D-glucocerebrosidase;
            glucosylcerebrosidase;
            beta-glucosylceramidase;
            ceramide glucosidase;
            glucocerebrosidase;
            glucosylsphingosine beta-glucosidase;
            glucosylsphingosine beta-D-glucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     D-glucosyl-N-acylsphingosine glucohydrolase
REACTION    D-glucosyl-N-acylsphingosine + H2O = D-glucose + N-acylsphingosine
            [RN:R01498]
ALL_REAC    R01498
SUBSTRATE   D-glucosyl-N-acylsphingosine [CPD:C01190];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031];
            N-acylsphingosine [CPD:C00195]
COMMENT     Also acts on glucosylsphingosine (cf. EC 3.2.1.62
            glycosylceramidase).
REFERENCE   1
  AUTHORS   Brady, R.O., Kanfer, J.N. and Shapiro, D.
  TITLE     The metabolism of glucocerebrosides. I. Preparation and properties
            of a glucocerebroside-cleaving enzyme from spleen tissue.
  JOURNAL   J. Biol. Chem. 240 (1966) 39-43.
REFERENCE   2  [PMID:3967661]
  AUTHORS   Vaccaro AM, Muscillo M, Suzuki K.
  TITLE     Characterization of human glucosylsphingosine glucosyl hydrolase and
            comparison with glucosylceramidase.
  JOURNAL   Eur. J. Biochem. 146 (1985) 315-21.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00600  Sphingolipid metabolism
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01201  glucosylceramidase
GENES       HSA: 2629(GBA)
            MMU: 14466(Gba)
            SSC: 449572(GBA)
            XLA: 447570(MGC84284)
            CEL: C33C12.3(glucosylceramidase) C33C12.8(glucosylceramidase)
                 Y4C6B.6
            AFM: AFUA_8G07120
            STM: STM4426(srfJ)
            PLU: plu2272
            XCC: XCC1077(srfJ)
            XCB: XC_3172
            XCV: XCV1202
            XAC: XAC1176(srfJ)
            CPS: CPS_3714
            SDE: Sde_2994
            BPL: BURPS1106A_1087
            RFR: Rfer_1106
            CCR: CC_1757
            ABA: Acid345_4153
            SUS: Acid_2638
            LBR: LVIS_2226
            CSC: Csac_2513
            TTE: TTE2349
            SMA: SAV2709
            SEN: SACE_4785
            BAD: BAD_1208
            BTH: BT_3312
STRUCTURES  PDB: 1OGS  1Y7V  2F61  2J25  2NSX  2NT0  2NT1  2V3D  2V3E  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.45
            ExPASy - ENZYME nomenclature database: 3.2.1.45
            ExplorEnz - The Enzyme Database: 3.2.1.45
            ERGO genome analysis and discovery system: 3.2.1.45
            BRENDA, the Enzyme Database: 3.2.1.45
            CAS: 37228-64-1
///
ENTRY       EC 3.2.1.46                 Enzyme
NAME        galactosylceramidase;
            cerebroside galactosidase;
            galactocerebroside.beta-galactosidase;
            galactosylcerebrosidase;
            galactocerebrosidase;
            ceramide galactosidase;
            galactocerebroside galactosidase;
            galactosylceramide.beta-galactosidase;
            cerebroside beta-galactosidase;
            galactosylceramidase I;
            beta-galactosylceramidase;
            galactocerebroside-beta-D-galactosidase;
            lactosylceramidase I;
            beta-galactocerebrosidase;
            lactosylceramidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     D-galactosyl-N-acylsphingosine galactohydrolase
REACTION    D-galactosyl-N-acylsphingosine + H2O = D-galactose +
            N-acylsphingosine [RN:R01502]
ALL_REAC    R01502 > R03617
SUBSTRATE   D-galactosyl-N-acylsphingosine [CPD:C02686];
            H2O [CPD:C00001]
PRODUCT     D-galactose [CPD:C00124];
            N-acylsphingosine [CPD:C00195]
COMMENT     cf. EC 3.2.1.62 glycosylceramidase.
REFERENCE   1  [PMID:5320641]
  AUTHORS   Brady RO, Gal AE, Kanfer JN, Bradley RM.
  TITLE     The metabolism of glucocerebrosides. 3. Purification and properties
            of a glucosyl- and galactosylceramide-cleaving enzyme from rat
            intestinal tissue.
  JOURNAL   J. Biol. Chem. 240 (1965) 3766-70.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00600  Sphingolipid metabolism
ORTHOLOGY   KO: K01202  galactosylceramidase
GENES       HSA: 2581(GALC)
            MMU: 14420(Galc)
            CFA: 403916(GALC)
            DRE: 406385(zgc:56444)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.46
            ExPASy - ENZYME nomenclature database: 3.2.1.46
            ExplorEnz - The Enzyme Database: 3.2.1.46
            ERGO genome analysis and discovery system: 3.2.1.46
            BRENDA, the Enzyme Database: 3.2.1.46
            CAS: 9027-89-8
///
ENTRY       EC 3.2.1.47                 Enzyme
NAME        galactosylgalactosylglucosylceramidase;
            trihexosyl ceramide galactosidase;
            ceramide trihexosidase;
            ceramidetrihexoside alpha-galactosidase;
            trihexosylceramide alpha-galactosidase;
            ceramidetrihexosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     D-galactosyl-D-galactosyl-D-glucosyl-N-acylsphingosine
            galactohydrolase
REACTION    D-galactosyl-D-galactosyl-D-glucosyl-N-acylsphingosine + H2O =
            D-galactose + lactosyl-N-acylsphingosine [RN:R03487 R06136]
ALL_REAC    R03487 R06136(G)
SUBSTRATE   D-galactosyl-D-galactosyl-D-glucosyl-N-acylsphingosine [CPD:C04753];
            H2O [CPD:C00001]
PRODUCT     D-galactose [CPD:C00124];
            lactosyl-N-acylsphingosine [CPD:C01290]
REFERENCE   1  [PMID:6020428]
  AUTHORS   Brady RO, Gal AE, Bradley RM, Martensson E.
  TITLE     The metabolism of ceramide trihexosides. I. Purification and
            properties of an enzyme that cleaves the terminal galactose molecule
            of galactosylgalactosylglucosylceramide.
  JOURNAL   J. Biol. Chem. 242 (1967) 1021-6.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.47
            ExPASy - ENZYME nomenclature database: 3.2.1.47
            ExplorEnz - The Enzyme Database: 3.2.1.47
            ERGO genome analysis and discovery system: 3.2.1.47
            BRENDA, the Enzyme Database: 3.2.1.47
            CAS: 9023-01-2
///
ENTRY       EC 3.2.1.48                 Enzyme
NAME        sucrose alpha-glucosidase;
            sucrose alpha-glucohydrolase;
            sucrase;
            sucrase-isomaltase;
            sucrose.alpha.-glucohydrolase;
            intestinal sucrase;
            sucrase(invertase)
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     sucrose-alpha-D-glucohydrolase
REACTION    Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type
            action
ALL_REAC    (other) R00802 R06088(G)
COMMENT     This enzyme is isolated from intestinal mucosa as a single
            polypeptide chain that also displays activity towards isomaltose (EC
            3.2.1.10 oligo-1,6-glucosidase).
REFERENCE   1  [PMID:807575]
  AUTHORS   Conklin KA, Yamashiro KM, Gray GM.
  TITLE     Human intestinal sucrase-isomaltase. Identification of free sucrase
            and isomaltase and cleavage of the hybrid into active distinct
            subunits.
  JOURNAL   J. Biol. Chem. 250 (1975) 5735-41.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:291933]
  AUTHORS   Hauri HP, Quaroni A, Isselbacher KJ.
  TITLE     Biogenesis of intestinal plasma membrane: posttranslational route
            and cleavage of sucrase-isomaltase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 5183-6.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:5073761]
  AUTHORS   Kolinska J, Kraml J.
  TITLE     Separation and characterization of sucrose-isomaltase and of
            glucoamylase of rat intestine.
  JOURNAL   Biochim. Biophys. Acta. 284 (1972) 235-47.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:1182172]
  AUTHORS   Sigrist H, Ronner P, Semenza G.
  TITLE     A hydrophobic form of the small-intestinal sucrase-isomaltase
            complex.
  JOURNAL   Biochim. Biophys. Acta. 406 (1975) 433-46.
  ORGANISM  rabbit
REFERENCE   5  [PMID:7002920]
  AUTHORS   Sjostrom H, Noren O, Christiansen L, Wacker H, Semenza G.
  TITLE     A fully active, two-active-site, single-chain sucrase.isomaltase
            from pig small intestine. Implications for the biosynthesis of a
            mammalian integral stalked membrane protein.
  JOURNAL   J. Biol. Chem. 255 (1980) 11332-8.
  ORGANISM  pig [GN:ssc]
REFERENCE   6  [PMID:5804876]
  AUTHORS   Takesue Y.
  TITLE     Purification and properties of rabbit intestinal sucrase.
  JOURNAL   J. Biochem. (Tokyo). 65 (1969) 545-52.
  ORGANISM  rabbit
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01203  sucrase-isomaltase
GENES       HSA: 6476(SI)
            MMU: 69983(2010204N08Rik)
            RNO: 497756(Si)
            CFA: 488141(SI)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.48
            ExPASy - ENZYME nomenclature database: 3.2.1.48
            ExplorEnz - The Enzyme Database: 3.2.1.48
            ERGO genome analysis and discovery system: 3.2.1.48
            BRENDA, the Enzyme Database: 3.2.1.48
            CAS: 37288-39-4
///
ENTRY       EC 3.2.1.49                 Enzyme
NAME        alpha-N-acetylgalactosaminidase;
            alpha-acetylgalactosaminidase;
            N-acetyl-alpha-D-galactosaminidase;
            N-acetyl-alpha-galactosaminidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     alpha-N-acetyl-D-galactosaminide N-acetylgalactosaminohydrolase
REACTION    Hydrolysis of terminal non-reducing N-acetyl-D-galactosamine
            residues in N-acetyl-alpha-D-galactosaminides
ALL_REAC    (other) R04183 R05966(G)
COMMENT     Splits N-acetylgalactosaminyl groups from O-3 of Ser and Thr.
REFERENCE   1  [PMID:6006833]
  AUTHORS   Tuppy H, Staudenbauer WL.
  TITLE     The action on soluble blood group A substances of an
            alpha-N-acetylgalactosaminidase from Helix pomatia.
  JOURNAL   Biochemistry. 5 (1966) 1742-7.
  ORGANISM  Helix pomatia
REFERENCE   2  [PMID:5785223]
  AUTHORS   Weissmann B, Hinrichsen DF.
  TITLE     Mammalian alpha-acetylgalactosaminidase. Occurrence, partial
            purification, and action on linkages in submaxillary mucins.
  JOURNAL   Biochemistry. 8 (1969) 2034-43.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:5348072]
  AUTHORS   Werries E, Wollek E, Gottschalk A, Buddecke E.
  TITLE     Separation of N-acetyl-alpha-glucosaminidase and
            N-acetyl-alpha-galactosaminidase from ox spleen. Cleavage of the
            O-glycosidic linkage between carbohydrate and polypeptide in ovine
            and bovine submaxillary glycoprotein by
            N-acetyl-alpha-galactosaminidase.
  JOURNAL   Eur. J. Biochem. 10 (1969) 445-9.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00603  Glycosphingolipid biosynthesis - globoseries
ORTHOLOGY   KO: K01204  alpha-N-acetylgalactosaminidase
GENES       HSA: 4668(NAGA)
            PTR: 470279(NAGA)
            GGA: 396547(NAGA)
            TET: TTHERM_00136050
STRUCTURES  PDB: 1KTB  1KTC  2IXA  2IXB  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.49
            ExPASy - ENZYME nomenclature database: 3.2.1.49
            ExplorEnz - The Enzyme Database: 3.2.1.49
            ERGO genome analysis and discovery system: 3.2.1.49
            BRENDA, the Enzyme Database: 3.2.1.49
            CAS: 9075-63-2
///
ENTRY       EC 3.2.1.50                 Enzyme
NAME        alpha-N-acetylglucosaminidase;
            alpha-acetylglucosaminidase;
            N-acetyl-alpha-D-glucosaminidase;
            N-acetyl-alpha-glucosaminidase;
            alpha-D-2-acetamido-2-deoxyglucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     alpha-N-acetyl-D-glucosaminide N-acetylglucosaminohydrolase
REACTION    Hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues
            in N-acetyl-alpha-D-glucosaminides
ALL_REAC    (other) R07816(G)
COMMENT     Hydrolyses UDP-N-acetylglucosamine.
REFERENCE   1  [PMID:411658]
  AUTHORS   von Figura K.
  TITLE     Human alpha-N-acetylglucosaminidase. 1. Purification and properties.
  JOURNAL   Eur. J. Biochem. 80 (1977) 523-33.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:923593]
  AUTHORS   von Figura K.
  TITLE     Human alpha-n-acetylglucosaminidase. 2. Activity towards natural
            substrates and multiple recognition forms.
  JOURNAL   Eur. J. Biochem. 80 (1977) 535-42.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:4291567]
  AUTHORS   Weissmann B, Rowin G, Marshall J, Friederici D.
  TITLE     Mammalian alpha-acetylglucosaminidase. Enzymic properties, tissue
            distribution, and intracellular localization.
  JOURNAL   Biochemistry. 6 (1967) 207-14.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:5348072]
  AUTHORS   Werries E, Wollek E, Gottschalk A, Buddecke E.
  TITLE     Separation of N-acetyl-alpha-glucosaminidase and
            N-acetyl-alpha-galactosaminidase from ox spleen. Cleavage of the
            O-glycosidic linkage between carbohydrate and polypeptide in ovine
            and bovine submaxillary glycoprotein by
            N-acetyl-alpha-galactosaminidase.
  JOURNAL   Eur. J. Biochem. 10 (1969) 445-9.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00531  Glycosaminoglycan degradation
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01205  alpha-N-acetylglucosaminidase
GENES       HSA: 4669(NAGLU)
            PTR: 468265(NAGLU)
            CFA: 490965(NAGLU)
            GGA: 771195(NAGLU)
            SPU: 580105(LOC580105)
            DME: Dmel_CG13397
            CEL: K09E4.4
            ATH: AT5G13690
            OSA: 4337231
            AFM: AFUA_2G09410
            AOR: AO090010000111
            DDI: DDBDRAFT_0184151
            FJO: Fjoh_3128
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.50
            ExPASy - ENZYME nomenclature database: 3.2.1.50
            ExplorEnz - The Enzyme Database: 3.2.1.50
            ERGO genome analysis and discovery system: 3.2.1.50
            BRENDA, the Enzyme Database: 3.2.1.50
            CAS: 37288-40-7
///
ENTRY       EC 3.2.1.51                 Enzyme
NAME        alpha-L-fucosidase;
            alpha-fucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     alpha-L-fucoside fucohydrolase
REACTION    an alpha-L-fucoside + H2O = L-fucose + an alcohol [RN:R03162]
ALL_REAC    R03162
SUBSTRATE   alpha-L-fucoside [CPD:C02475];
            H2O [CPD:C00001]
PRODUCT     L-fucose [CPD:C01019];
            alcohol [CPD:C00069]
REFERENCE   1
  AUTHORS   Levvy, G.A. and McAllan, A.
  TITLE     Mammalian fucosidases. 2. alpha-L-Fucosidase.
  JOURNAL   Biochem. J. 80 (1961) 435-439.
  ORGANISM  mouse [GN:mmu], rat [GN:rno], pig [GN:ssc], cow [GN:bta]
REFERENCE   2  [PMID:7458]
  AUTHORS   Reglero A, Cabezas JA.
  TITLE     Glycosidases of molluscs. Purification and properties of
            alpha-L-fucosidase from Chamelea gallina L.
  JOURNAL   Eur. J. Biochem. 66 (1976) 379-87.
  ORGANISM  Chamelea gallina
REFERENCE   3  [PMID:5672520]
  AUTHORS   Tanaka K, Nakano T, Noguchi S, Pigman W.
  TITLE     Purification of alpha-L-fucosidase of abalone livers.
  JOURNAL   Arch. Biochem. Biophys. 126 (1968) 624-33.
  ORGANISM  Haliotis gigantea
PATHWAY     PATH: map00511  N-Glycan degradation
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01206  alpha-L-fucosidase
GENES       HSA: 2517(FUCA1) 2519(FUCA2)
            PTR: 463039(FUCA2) 469222(FUCA1)
            MMU: 66848(Fuca2) 71665(Fuca1)
            RNO: 24375(Fuca)
            CFA: 403929(FUCA1) 484016(FUCA2)
            GGA: 419687(FUCA1)
            XLA: 398801(MGC68702)
            XTR: 496744(LOC496744)
            DRE: 335494(fuca1)
            SPU: 592142(LOC592142)
            CEL: W03G11.3
            DDI: DDBDRAFT_0202938 DDB_0185016(alfA)
            HSO: HS_0435(alfA)
            XFA: XF0106 XF2714
            XFT: PD0080 PD2066(fucA1)
            XCC: XCC1251 XCC2888(fucA1)
            XCB: XC_1221 XC_2990
            XCV: XCV1357 XCV3207(fucA1)
            XAC: XAC1306 XAC3072(fucA1)
            XOO: XOO1783(fucA1) XOO1835
            XOM: XOO_1686(XOO1686) XOO_1731(XOO1731)
            PAT: Patl_0823 Patl_0831
            RET: RHE_PF00304(ypf00150)
            RLE: pRL100274 pRL120678
            CCR: CC_0795
            HNE: HNE_0383
            ABA: Acid345_0902
            SUS: Acid_2655 Acid_3464 Acid_4210 Acid_7109
            SPN: SP_2146
            SPR: spr1954
            SGO: SGO_0150(fucA1)
            LCA: LSEI_1818 LSEI_2750
            CPE: CPE0324 CPE1876
            CPR: CPR_1843
            CSC: Csac_1340
            SCO: SCO0279(SCF85.07)
            SMA: SAV1752
            PAC: PPA0607 PPA2070
            KRA: Krad_3569
            SEN: SACE_1317
            RBA: RB5816(fucA)
            BTH: BT_1625 BT_1842 BT_3665
            BFR: BF1720 BF3243 BF3420
            BFS: BF1796 BF3083 BF3242
            PGI: PG1750
            GFO: GFO_1710(fucA)
            FJO: Fjoh_2028 Fjoh_2040
            RRS: RoseRS_2814 RoseRS_3943
            RCA: Rcas_2554 Rcas_3615
            TMA: TM0306
            TPT: Tpet_0611
            SSO: SSO11867(fucA1) SSO3060(fucA1)
STRUCTURES  PDB: 1HL8  1HL9  1ODU  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.51
            ExPASy - ENZYME nomenclature database: 3.2.1.51
            ExplorEnz - The Enzyme Database: 3.2.1.51
            ERGO genome analysis and discovery system: 3.2.1.51
            BRENDA, the Enzyme Database: 3.2.1.51
            CAS: 9037-65-4
///
ENTRY       EC 3.2.1.52                 Enzyme
NAME        beta-N-acetylhexosaminidase;
            hexosaminidase;
            beta-acetylaminodeoxyhexosidase;
            N-acetyl-beta-D-hexosaminidase;
            N-acetyl-beta-hexosaminidase;
            beta-hexosaminidase;
            beta-acetylhexosaminidinase;
            beta-D-N-acetylhexosaminidase;
            beta-N-acetyl-D-hexosaminidase;
            beta-N-acetylglucosaminidase;
            hexosaminidase A;
            N-acetylhexosaminidase;
            beta-D-hexosaminidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     beta-N-acetyl-D-hexosaminide N-acetylhexosaminohydrolase
REACTION    Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues
            in N-acetyl-beta-D-hexosaminides
ALL_REAC    (other) R00022 R03492 R04184 R04586 R05963(G) R06001(G) R06004(G)
            R06141(G) R07809(G) R07810(G)
COMMENT     Acts on N-acetylglucosides and N-acetylgalactosides.
REFERENCE   1  [PMID:2529847]
  AUTHORS   Cabezas JA.
  TITLE     Some comments on the type references of the official nomenclature
            (IUB) for beta-N-acetylglucosaminidase, beta-N-acetylhexosaminidase
            and beta-N-acetylgalactosaminidase.
  JOURNAL   Biochem. J. 261 (1989) 1059-60.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:33660]
  AUTHORS   Calvo P, Reglero A, Cabezas JA.
  TITLE     Purification and properties of beta-N-acetylhexosaminidase from the
            mollusc Helicella ericetorum Muller.
  JOURNAL   Biochem. J. 175 (1978) 743-50.
  ORGANISM  Helicella ericetorum
REFERENCE   3  [PMID:6055190]
  AUTHORS   Frohwein YZ, Gatt S.
  TITLE     Isolation of beta-N-acetylhexosaminidase,
            beta-N-acetylglucosaminidase, and beta-N-acetylgalactosaminidase
            from calf brain.
  JOURNAL   Biochemistry. 6 (1967) 2775-82.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:5506280]
  AUTHORS   Li SC, Li YT.
  TITLE     Studies on the glycosidases of jack bean meal. 3. Crystallization
            and properties of beta-N-acetylhexosaminidase.
  JOURNAL   J. Biol. Chem. 245 (1970) 5153-60.
  ORGANISM  jack bean
PATHWAY     PATH: map00511  N-Glycan degradation
            PATH: map00530  Aminosugars metabolism
            PATH: map00531  Glycosaminoglycan degradation
            PATH: map00603  Glycosphingolipid biosynthesis - globoseries
            PATH: map00604  Glycosphingolipid biosynthesis - ganglioseries
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01207  beta-N-acetylhexosaminidase
GENES       HSA: 3073(HEXA) 3074(HEXB)
            MMU: 15211(Hexa) 15212(Hexb)
            RNO: 294673(Hexb)
            CFA: 487633(HEXA)
            SSC: 396958(HEXB)
            GGA: 415320(RCJMB04_30g17)
            DME: Dmel_CG1318(Hexo1) Dmel_CG1787(Hexo2) Dmel_CG8824(fdl)
            CEL: T14F9.3
            ATH: AT1G05590 AT3G55260
            OSA: 4337620 4343697
            PIC: PICST_77156(BHA1)
            CAL: CaO19.6673(hex1)
            ANI: AN1502.2 AN2870.2
            AFM: AFUA_2G00640 AFUA_3G11780 AFUA_8G05020
            AOR: AO090003000741 AO090005000639
            CNE: CNF03620
            DDI: DDBDRAFT_0204822 DDBDRAFT_0219249 DDB_0191256(nagA)
            TET: TTHERM_00191450 TTHERM_01068140
            EHI: 125.t00018 16.t00041 231.t00004
            ECO: b1107(nagZ)
            ECJ: JW1093(nagZ)
            ECE: Z1746(ycfO)
            ECS: ECs1485
            ECC: c1380(nagZ)
            ECP: ECP_1099
            ECV: APECO1_188(nagZ)
            ECW: EcE24377A_1229(nagZ)
            ECX: EcHS_A1230
            STY: STY1249
            STT: t1711
            SPT: SPA1642(ycfO)
            SEC: SC1159(nagZ)
            STM: STM1209(nagZ)
            YPE: YPO1615(ycfO)
            YPK: y1775
            YPM: YP_1082(chb) YP_2239(bglX1)
            YPA: YPA_1907 YPA_2464
            YPN: YPN_1119 YPN_2014
            YPP: YPDSF_2621
            YPS: YPTB1123 YPTB2449(ycfO)
            YPI: YpsIP31758_1592(nagZ) YpsIP31758_2903(chb)
            YEN: YE2974(chb)
            SFL: SF1111(ycfO)
            SFX: S1191(ycfO)
            SFV: SFV_1127(ycfO)
            SSN: SSON_1127(ycfO)
            SBO: SBO_1954(ycfO)
            SDY: SDY_2043(ycfO)
            ECA: ECA1813(nagZ) ECA4161
            PLU: plu1324(chb) plu2822(nagZ)
            SGL: SG1953
            ENT: Ent638_0442
            SPE: Spro_0536 Spro_1232
            HIN: HI0959(exoII)
            HIT: NTHI1132(nagZ)
            HIP: CGSHiEE_07165
            HIQ: CGSHiGG_08380
            HDU: HD0542(nagZ)
            HSO: HS_1132(nagZ)
            PMU: PM0071
            MSU: MS0396(bglX)
            APL: APL_1111(nagZ)
            ASU: Asuc_0211
            XFA: XF0847 XF2355
            XFT: PD1383(exoII) PD1827(nahA)
            XCC: XCC1283(nagZ) XCC2890(nahA)
            XCB: XC_1219 XC_2958
            XCV: XCV1386 XCV3209(nahA)
            XAC: XAC1334(nagZ) XAC3074(nahA)
            XOO: XOO1781(nahA) XOO1867(nagZ)
            XOM: XOO_1684(XOO1684) XOO_1762(XOO1762)
            VCH: VC0613 VC0692 VC2217
            VCO: VC0395_A0142(chb-1) VC0395_A0223(nagZ) VC0395_A1809(chb-2)
            VVU: VV1_0241 VV1_0496 VV1_1666 VV2_0591
            VVY: VV0700 VV0942 VV2741 VVA1141
            VPA: VP0545 VP0755 VP2486
            VFI: VF0037 VF2146 VFA0493 VFA1010
            PPR: PBPRA0518(chb) PBPRA1033 PBPRA1268 PBPRB0828
            PAE: PA3005
            PAU: PA14_25195(nagZ)
            PPU: PP_2145(nagZ)
            PST: PSPTO_3507(nagZ)
            PSB: Psyr_3281
            PSP: PSPPH_3201(nagZ)
            PFL: PFL_1951
            PFO: Pfl_3870
            PEN: PSEEN3718
            PAR: Psyc_0281
            PCR: Pcryo_0308
            PRW: PsycPRwf_0314
            ACI: ACIAD0551(nagZ)
            ACB: A1S_0492
            SON: SO_2250(nagZ) SO_3509(hex)
            SDN: Sden_0553 Sden_1945
            SFR: Sfri_2401
            SAZ: Sama_0943
            SBL: Sbal_1405
            SBM: Shew185_1143 Shew185_1396
            SLO: Shew_1115
            SPC: Sputcn32_1075
            SSE: Ssed_1211
            SPL: Spea_1100
            SHE: Shewmr4_2936
            SHM: Shewmr7_3018
            SHN: Shewana3_2293 Shewana3_3115
            SHW: Sputw3181_3090
            ILO: IL0915
            CPS: CPS_1025 CPS_3960(nagZ1) CPS_4609(nagZ2)
            PHA: PSHAb0065(nagZ)
            PAT: Patl_1716
            SDE: Sde_1790 Sde_3037 Sde_3271
            CBU: CBU_1077(nagZ)
            CBD: COXBU7E912_1179(nagZ)
            LPF: lpl1199
            MCA: MCA1984
            FTU: FTT0928c
            FTF: FTF0928c
            FTL: FTL_1282
            FTH: FTH_1254
            TCX: Tcr_1296
            NOC: Noc_2183
            AEH: Mlg_1327
            HHA: Hhal_1261
            HCH: HCH_02679 HCH_04791
            CSA: Csal_2067
            ABO: ABO_1018(nagZ)
            AHA: AHA_1528 AHA_3100
            DNO: DNO_0021
            RMA: Rmag_0318
            NME: NMB0530
            NMA: NMA0708
            NMC: NMC0469
            NGO: NGO0135
            CVI: CV_1493 CV_2073
            RSO: RSc0769(RS05085) RSc1068(RS04135)
            REU: Reut_A2247
            REH: H16_A2550
            RME: Rmet_2413
            BMA: BMA0548 BMA3173
            BXE: Bxe_A1090
            BVI: Bcep1808_1058 Bcep1808_2924
            BUR: Bcep18194_A4251 Bcep18194_A6150
            BCN: Bcen_0659 Bcen_2206
            BCH: Bcen2424_1139 Bcen2424_2820
            BAM: Bamb_1015 Bamb_2880
            BPS: BPSL0500 BPSL2015 BPSL2424
            BPM: BURPS1710b_0725(bcc1) BURPS1710b_1807(cht60)
                 BURPS1710b_2889(nagZ)
            BTE: BTH_I0451 BTH_I1735 BTH_I2668
            BPE: BP2080(nagZ)
            BPA: BPP1764(nagZ)
            BBR: BB3344(nagZ)
            RFR: Rfer_1754
            POL: Bpro_3630
            AAV: Aave_1200
            AJS: Ajs_3261
            VEI: Veis_2346
            MPT: Mpe_A0655
            HAR: HEAR2058(nagZ)
            MMS: mma_1375
            NEU: NE2320
            NET: Neut_1774
            NMU: Nmul_A1761
            EBA: ebA5547(nagZ)
            AZO: azo0701(nagZ1) azo1647(nagZ2)
            DAR: Daro_2034
            TBD: Tbd_0727
            MFA: Mfla_1845
            TDN: Tmden_2069
            ABU: Abu_1035
            SUN: SUN_0984
            PCA: Pcar_1318
            DDE: Dde_2559
            BBA: Bd0146(bglX2) Bd3895
            ADE: Adeh_4264
            SFU: Sfum_2523
            PUB: SAR11_0972
            MLO: mll1089
            PLA: Plav_3024
            SME: SMb21160(hexA) SMc02071
            SMD: Smed_1160 Smed_4653
            ATU: Atu1709 Atu2596
            ATC: AGR_C_3141 AGR_C_4704
            RET: RHE_CH01820(ypch00608) RHE_CH03686(hexA)
                 RHE_PE00333(ype00169) RHE_PE00391
            RLE: RL2043(nagZ) RL4222(exoI) RL4489 pRL110439 pRL110511
            BME: BMEI1087
            BMF: BAB1_0898
            BMS: BR0879
            BMB: BruAb1_0891
            OAN: Oant_2348
            BJA: bll4754
            BRA: BRADO3953 BRADO4050
            BBT: BBta_4322 BBta_4420
            RPA: RPA2852
            RPB: RPB_2748
            RPC: RPC_2510
            RPD: RPD_2793
            RPE: RPE_2693
            NWI: Nwi_1805
            NHA: Nham_1760
            XAU: Xaut_4411
            CCR: CC_0447 CC_2006
            SIL: SPO2502
            SIT: TM1040_0905 TM1040_2739
            RSP: RSP_2941
            RSH: Rsph17029_1586
            RSQ: Rsph17025_0904
            JAN: Jann_1509
            RDE: RD1_3163(nagZ)
            PDE: Pden_1868
            MMR: Mmar10_0601 Mmar10_1912
            HNE: HNE_2048(nagZ)
            ZMO: ZMO1171
            NAR: Saro_1091 Saro_2417
            SAL: Sala_1140
            SWI: Swit_3933
            ELI: ELI_01580
            GOX: GOX0580
            GBE: GbCGDNIH1_1258
            ACR: Acry_0951
            RRU: Rru_A1777
            MGM: Mmc1_1631
            ABA: Acid345_1990 Acid345_2735 Acid345_3493 Acid345_4564
            SUS: Acid_3086 Acid_6569
            BSU: BG10455(lytD) BG10832(ybbD)
            BHA: BH0675
            BLI: BL02465(lytD) BL02716(ybbD)
            BLD: BLi00187(ybbD) BLi03821(lytD)
            BCL: ABC3126
            BAY: RBAM_002150(ybbD)
            BPU: BPUM_3233(lytD)
            OIH: OB0270 OB1299 OB3206
            SHA: SH2654
            LLA: L100350(yejJ)
            LLC: LACR_0523
            LLM: llmg_0494(nagZ)
            SPH: MGAS10270_Spy1164 MGAS10270_Spy1165 MGAS10270_Spy1166
                 MGAS10270_Spy1167
            SPN: SP_0057
            SPR: spr0057(strH) spr1949
            SPD: SPD_0063(strH)
            SAG: SAG0705
            SAN: gbs0678
            SAK: SAK_0831
            SSA: SSA_1065 SSA_1144
            SGO: SGO_0405
            LPL: lp_3645
            LSL: LSL_1568
            LCA: LSEI_0291
            STH: STH2498 STH300
            CAC: CAC0182
            CPE: CPE0266 CPE1364
            CPF: CPF_0259
            DSY: DSY4234
            TTE: TTE0215(bglX) TTE0241(bglX2)
            MVA: Mvan_0256
            MGI: Mflv_0415
            MMC: Mmcs_0229
            MKM: Mkms_0239
            MJL: Mjls_0219
            CGB: cg3158(nagA2)
            RHA: RHA1_ro05196
            SCO: SCO0534(SCF11.14) SCO2758(nagA) SCO2786(hexA)
                 SCO2943(SCE59.02c)
            SMA: SAV5134(nagZ3) SAV5268(nagZ4) SAV5302(nagZ5)
            LXX: Lxx18650
            ART: Arth_2890
            AAU: AAur_0928(nahA) AAur_4089(nahA)
            PAC: PPA0066 PPA2164
            TFU: Tfu_2486
            FAL: FRAAL0843 FRAAL0882
            ACE: Acel_0072
            SEN: SACE_0363(nagA) SACE_3851(hexA)
            STP: Strop_3430
            RXY: Rxyl_0629
            RBA: RB4561
            BGA: BG0002
            LIL: LA2561(nagZ)
            SYG: sync_2563
            CYB: CYB_2338
            ANA: all1831
            AVA: Ava_4847
            PMN: PMN2A_1481
            TER: Tery_3725
            BTH: BT_0459 BT_0460 BT_1051 BT_1627 BT_3178 BT_4337 BT_4394
                 BT_4681
            BFR: BF1036 BF1734 BF1736 BF2136 BF3246 BF4250
            BFS: BF0953 BF1811(nahB) BF1813(nahC) BF2193 BF3085 BF4059
            PGI: PG0043(nahA)
            SRU: SRU_0368(chb)
            CHU: CHU_0470(nagZ)
            FJO: Fjoh_0674 Fjoh_2039 Fjoh_4556 Fjoh_4808
            CTE: CT0090
            CCH: Cag_1657 Cag_1972
            PVI: Cvib_1697
            PLT: Plut_0125 Plut_2055
            DRA: DR_1333
            DGE: Dgeo_1079
            TMA: TM0809
            PTO: PTO0020
STRUCTURES  PDB: 1C7S  1C7T  1HP4  1HP5  1JAK  1M01  1M03  1M04  1NOU  1NOW  
                 1NP0  1O7A  1QBA  1QBB  1TR9  1Y65  1YHT  2CHN  2CHO  2GJX  
                 2GK1  2J47  2J4G  2JIW  2OXN  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.52
            ExPASy - ENZYME nomenclature database: 3.2.1.52
            ExplorEnz - The Enzyme Database: 3.2.1.52
            ERGO genome analysis and discovery system: 3.2.1.52
            BRENDA, the Enzyme Database: 3.2.1.52
            CAS: 9027-52-5
///
ENTRY       EC 3.2.1.53                 Enzyme
NAME        beta-N-acetylgalactosaminidase;
            N-acetyl-beta-galactosaminidase;
            N-acetyl-beta-D-galactosaminidase;
            beta-acetylgalactosaminidase;
            beta-D-N-acetylgalactosaminidase;
            N-acetylgalactosaminidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     beta-N-acetyl-D-galactosaminide N-acetylgalactosaminohydrolase
REACTION    Hydrolysis of terminal non-reducing N-acetyl-D-galactosamine
            residues in N-acetyl-beta-D-galactosaminides
REFERENCE   1  [PMID:6055190]
  AUTHORS   Frohwein YZ, Gatt S.
  TITLE     Isolation of beta-N-acetylhexosaminidase,
            beta-N-acetylglucosaminidase, and beta-N-acetylgalactosaminidase
            from calf brain.
  JOURNAL   Biochemistry. 6 (1967) 2775-82.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:5069351]
  AUTHORS   Hooghwinkel GJ, Veltkamp WA, Overdijk B, Lisman JJ.
  TITLE     Electrophoretic separation of  -N-acetylhexosaminidases of human and
            bovine brain and liver and of Tay-Sachs brain tissue.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 353 (1972) 839-41.
  ORGANISM  cow [GN:bta], human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.53
            ExPASy - ENZYME nomenclature database: 3.2.1.53
            ExplorEnz - The Enzyme Database: 3.2.1.53
            ERGO genome analysis and discovery system: 3.2.1.53
            BRENDA, the Enzyme Database: 3.2.1.53
            CAS: 9054-43-7
///
ENTRY       EC 3.2.1.54                 Enzyme
NAME        cyclomaltodextrinase;
            cycloheptaglucanase;
            cyclohexaglucanase;
            cyclodextrinase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     cyclomaltodextrin dextrin-hydrolase (decyclizing)
REACTION    cyclomaltodextrin + H2O = linear maltodextrin [RN:R03122 R06160]
ALL_REAC    R03122 R06160(G)
SUBSTRATE   cyclomaltodextrin [CPD:C00973];
            H2O [CPD:C00001]
PRODUCT     linear maltodextrin [CPD:C01935]
COMMENT     Also hydrolyses linear maltodextrin.
REFERENCE   1  [PMID:4922856]
  AUTHORS   DePinto JA, Campbell LL.
  TITLE     Purification and properties of the cyclodextrinase of Bacillus
            macerans.
  JOURNAL   Biochemistry. 7 (1968) 121-5.
  ORGANISM  Bacillus macerans
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01208  cyclomaltodextrinase
GENES       VFI: VF2049
            OIH: OB2561
            SPZ: M5005_Spy_1066(amyB)
            SPH: MGAS10270_Spy1122(amyB)
            SPI: MGAS10750_Spy1159(amyB)
            LSL: LSL_0067(amyB) LSL_1295
            CGL: NCgl0853(cgl0889)
            CGB: cg1012
            FAL: FRAAL2309
            AVA: Ava_2017
STRUCTURES  PDB: 1EA9  1H3G  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.54
            ExPASy - ENZYME nomenclature database: 3.2.1.54
            ExplorEnz - The Enzyme Database: 3.2.1.54
            ERGO genome analysis and discovery system: 3.2.1.54
            BRENDA, the Enzyme Database: 3.2.1.54
            CAS: 37288-41-8
///
ENTRY       EC 3.2.1.55                 Enzyme
NAME        alpha-N-arabinofuranosidase;
            arabinosidase;
            alpha-arabinosidase;
            alpha-L-arabinosidase;
            alpha-arabinofuranosidase;
            polysaccharide alpha-L-arabinofuranosidase;
            alpha-L-arabinofuranoside hydrolase;
            L-arabinosidase;
            alpha-L-arabinanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     alpha-L-arabinofuranoside arabinofuranohydrolase
REACTION    Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
            residues in alpha-L-arabinosides
ALL_REAC    (other) R01762 R06205(G)
COMMENT     The enzyme acts on alpha-L-arabinofuranosides, alpha-L-arabinans
            containing (1,3)- and/or (1,5)-linkages, arabinoxylans and
            arabinogalactans. Some beta-galactosidases (EC 3.2.1.23) and
            beta-D-fucosidases (EC 3.2.1.38) also hydrolyse
            alpha-L-arabinosides.
REFERENCE   1  [PMID:5452669]
  AUTHORS   Kaji A, Tagawa K.
  TITLE     Purification, crystallization and amino acid composition of
            alpha-L-arabinofuranosidase from Aspergillus niger.
  JOURNAL   Biochim. Biophys. Acta. 207 (1970) 456-64.
  ORGANISM  Aspergillus niger
REFERENCE   2  [PMID:5143344]
  AUTHORS   Kaji A, Yoshihara O.
  TITLE     Properties of purified  -L-arabinofuranosidase from Corticium
            rolfsii.
  JOURNAL   Biochim. Biophys. Acta. 250 (1971) 367-71.
  ORGANISM  Corticium rolfsii
REFERENCE   3
  AUTHORS   Tagawa, K. and Kaji, A.
  TITLE     Preparation of L-arabinose-containing polysaccharides and the action
            of an alpha-L-arabinofuranosidase on these polysaccharides.
  JOURNAL   Carbohydr. Res. 11 (1969) 293-301.
  ORGANISM  Aspergillus niger
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
ORTHOLOGY   KO: K01209  alpha-N-arabinofuranosidase
GENES       ANI: AN1277.2
            AFM: AFUA_1G09900 AFUA_2G15160
            ANG: An01g00330(abfA) An03g00960(axhA) An15g02300(abfB)
            CNE: CNH00030
            UMA: UM00837.1
            ENT: Ent638_0457 Ent638_0656 Ent638_2996
            SPE: Spro_4015
            XCC: XCC1178(xylB) XCC1191 XCC4105(xylB)
            XCB: XC_3051 XC_3064 XC_4196
            XCV: XCV1325 XCV1335 XCV4336(xylB3)
            XAC: XAC1275(xylB) XAC1286 XAC4230(xylB)
            XOO: XOO1317 XOO4422(xylB)
            XOM: XOO_1211(XOO1211) XOO_4165(XOO4165)
            SPC: Sputcn32_2050 Sputcn32_2053 Sputcn32_2055
            SHE: Shewmr4_1990 Shewmr4_1991
            SHM: Shewmr7_1983 Shewmr7_1984
            SHN: Shewana3_2077 Shewana3_2078
            SHW: Sputw3181_1957 Sputw3181_1959 Sputw3181_1962
            PAT: Patl_0842 Patl_3728
            SDE: Sde_0598 Sde_0777 Sde_0787 Sde_0791 Sde_0822 Sde_1655
                 Sde_1767
            CSA: Csal_1143
            MMW: Mmwyl1_2712
            VEI: Veis_3457
            MLO: mll3591
            SME: SMb20924(abfA)
            SMD: Smed_1710 Smed_5583
            ATU: Atu3104
            ATC: AGR_L_3408
            RET: RHE_PE00195(ype00096)
            RLE: pRL110282(abfA)
            CCR: CC_1422 CC_2802
            ABA: Acid345_0328 Acid345_0753
            SUS: Acid_2094 Acid_2100 Acid_2120 Acid_2992 Acid_3644 Acid_3748
                 Acid_5647 Acid_7260
            BSU: BG11900(abfA) BG11985(xsa)
            BHA: BH1861(abfA) BH1874(xsa)
            BLI: BL00345(abfA)
            BLD: BLi03021(abfA)
            BCL: ABC0397(abfA) ABC1148 ABC3371(xsa)
            BAY: RBAM_025780
            BPU: BPUM_2508
            OIH: OB2087
            LLM: llmg_1608
            LBR: LVIS_1750 LVIS_2221
            CTH: Cthe_2548
            CBE: Cbei_2360 Cbei_4126 Cbei_4972 Cbei_4973
            AMT: Amet_3317
            CSC: Csac_1561
            SCO: SCO2431(abfA) SCO5932(abfB)
            SMA: SAV5743(abfA)
            CMI: CMM_2435(abfA2)
            ART: Arth_0226
            AAU: AAur_0205(abfA) AAur_0688(abfA)
            PAC: PPA2308
            TFU: Tfu_1616
            KRA: Krad_0962 Krad_1037 Krad_3567
            BLO: BL0544(abfA1) BL1166(abfA2) BL1611(abfA3)
            BAD: BAD_1205(xsa)
            RBA: RB8073(abf2)
            BTH: BT_0348
            GFO: GFO_0690(arfA) GFO_0695
            FJO: Fjoh_1118 Fjoh_1998 Fjoh_2025 Fjoh_3113
            RRS: RoseRS_3514
            RCA: Rcas_0598
            TMA: TM0281
            TPT: Tpet_0631 Tpet_0633
STRUCTURES  PDB: 1PZ2  1PZ3  1QW8  1QW9  1WD3  1WD4  2C7F  2C8N  2D43  2D44  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.55
            ExPASy - ENZYME nomenclature database: 3.2.1.55
            ExplorEnz - The Enzyme Database: 3.2.1.55
            ERGO genome analysis and discovery system: 3.2.1.55
            BRENDA, the Enzyme Database: 3.2.1.55
            CAS: 9067-74-7
///
ENTRY       EC 3.2.1.56                 Enzyme
NAME        glucuronosyl-disulfoglucosamine glucuronidase;
            glycuronidase;
            3-D-glucuronsyl-2-N,6-disulfo-beta-D-glucosamine glucuronohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     3-D-glucuronsyl-N2,6-disulfo-beta-D-glucosamine glucuronohydrolase
REACTION    3-D-glucuronosyl-N2,6-disulfo-beta-D-glucosamine + H2O =
            D-glucuronate + N2,6-disulfo-D-glucosamine [RN:R04512 R06143]
ALL_REAC    R04512 R06143(G)
SUBSTRATE   3-D-glucuronosyl-N2,6-disulfo-beta-D-glucosamine [CPD:C04674];
            H2O [CPD:C00001]
PRODUCT     D-glucuronate [CPD:C00191];
            N2,6-disulfo-D-glucosamine [CPD:C03789]
REFERENCE   1  [PMID:5785227]
  AUTHORS   Dietrich CP.
  TITLE     Enzymic degradation of heparin. A glucosaminidase and a
            glycuronidase from Flavobacterium heparinum.
  JOURNAL   Biochemistry. 8 (1969) 2089-94.
  ORGANISM  Flavobacterium heparinum
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.56
            ExPASy - ENZYME nomenclature database: 3.2.1.56
            ExplorEnz - The Enzyme Database: 3.2.1.56
            ERGO genome analysis and discovery system: 3.2.1.56
            BRENDA, the Enzyme Database: 3.2.1.56
            CAS: 37288-42-9
///
ENTRY       EC 3.2.1.57                 Enzyme
NAME        isopullulanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     pullulan 4-glucanohydrolase (isopanose-forming)
REACTION    Hydrolysis of pullulan to isopanose (6-alpha-maltosylglucose)
COMMENT     The enzyme has practically no action on starch. Panose
            (4-alpha-isomaltosylglucose) is hydrolysed to isomaltose and
            glucose. cf. EC 3.2.1.41 (pullulanase) and EC 3.2.1.135
            (neopullulanase).
REFERENCE   1
  AUTHORS   Sakano, Y., Masuda, N. and Kobayashi, T.
  TITLE     Hydrolysis of pullulan by a novel enzyme from Aspergillus niger.
  JOURNAL   Agric. Biol. Chem. 35 (1971) 971-973.
  ORGANISM  Aspergillus niger
STRUCTURES  PDB: 1WMR  1X0C  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.57
            ExPASy - ENZYME nomenclature database: 3.2.1.57
            ExplorEnz - The Enzyme Database: 3.2.1.57
            ERGO genome analysis and discovery system: 3.2.1.57
            BRENDA, the Enzyme Database: 3.2.1.57
            CAS: 37288-43-0
///
ENTRY       EC 3.2.1.58                 Enzyme
NAME        glucan 1,3-beta-glucosidase;
            exo-1,3-beta-glucosidase;
            beta-1,3-glucan exo-hydrolase;
            exo (1->3)-glucanohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,3-beta-glucan glucohydrolase
REACTION    Successive hydrolysis of beta-D-glucose units from the non-reducing
            ends of 1,3-beta-D-glucans, releasing alpha-glucose
ALL_REAC    (other) R03115 R06078(G)
COMMENT     Acts on oligosaccharides, but very slowly on laminaribiose.
REFERENCE   1  [PMID:5354264]
  AUTHORS   Barras DR, Stone BA.
  TITLE     Beta-1,3-glucan hydrolases from Euglena gracilis. I. The nature of
            the hydrolases.
  JOURNAL   Biochim. Biophys. Acta. 191 (1969) 329-41.
  ORGANISM  Euglena gracilis
REFERENCE   2  [PMID:5354265]
  AUTHORS   Barras DR, Stone BA.
  TITLE     Beta-1,3-glucan hydrolases from Euglena gracilis. II. Purification
            and properties of the beta-1,3-glucan exo-hydrolase.
  JOURNAL   Biochim. Biophys. Acta. 191 (1969) 342-53.
  ORGANISM  Euglena gracilis
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01210  glucan 1,3-beta-glucosidase
GENES       OSA: 4338201
            SCE: YDR261C(EXG2) YGR282C(BGL2) YLR300W(EXG1) YOR190W(SPR1)
            AGO: AGOS_AAR146W AGOS_AEL220C
            PIC: PICST_28554(BOT2) PICST_57025(SCW4.2) PICST_57399(EXG1)
                 PICST_61452(EXG3) PICST_74722(SCW4) PICST_78873(EXG2)
                 PICST_89695(SCW4.1)
            CAL: CaO19_2990(CaO19.2990)
            CGR: CAGL0G00220g CAGL0G09515g CAGL0I00484g CAGL0M08756g
            YLI: YALI0F05390g(EXG1)
            SPO: SPAC12B10.11 SPAC26H5.08c SPBC1105.05
            ANI: AN4052.2 AN7533.2
            AFM: AFUA_1G03600 AFUA_1G11460 AFUA_1G14450 AFUA_2G00430
                 AFUA_3G07520 AFUA_6G09250 AFUA_6G11980 AFUA_6G13270
            AOR: AO090001000604 AO090003000990 AO090038000279
            CNE: CNE03150 CNN00660
            UMA: UM00235.1 UM06078.1
            PEN: PSEEN1452
            AZO: azo1284(ndvC) azo2311(spr1)
            BRA: BRADO3754 BRADO3757
            BBT: BBta_4171 BBta_4173
STRUCTURES  PDB: 1CZ1  1EQC  1EQP  1EX1  1H4P  1IEQ  1IEV  1IEW  1IEX  1J8V  
                 1LQ2  1X38  1X39  2PB1  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.58
            ExPASy - ENZYME nomenclature database: 3.2.1.58
            ExplorEnz - The Enzyme Database: 3.2.1.58
            ERGO genome analysis and discovery system: 3.2.1.58
            BRENDA, the Enzyme Database: 3.2.1.58
            CAS: 9073-49-8
///
ENTRY       EC 3.2.1.59                 Enzyme
NAME        glucan endo-1,3-alpha-glucosidase;
            endo-1,3-alpha-glucanase;
            mutanase;
            endo-(1->3)-alpha-glucanase;
            cariogenase;
            cariogenanase;
            endo-1,3-alpha-D-glucanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,3(1,3;1,4)-alpha-D-glucan 3-glucanohydrolase
REACTION    Endohydrolysis of 1,3-alpha-D-glucosidic linkages in isolichenin,
            pseudonigeran and nigeran
COMMENT     Products from pseudonigeran (1,3-alpha-D-glucan) are nigerose and
            alpha-D-glucose.
REFERENCE   1  [PMID:5388595]
  AUTHORS   Hasegawa S, Nordin JH.
  TITLE     Enzymes that hydrolyze fungal cell wall polysaccharides. I.
            Purification and properties of an endo-alpha-D-(1-3)-glucanase from
            Trichoderma.
  JOURNAL   J. Biol. Chem. 244 (1969) 5460-70.
  ORGANISM  Trichoderma viride, Aspergillus niger
ORTHOLOGY   KO: K08254  glucan endo-1,3-alpha-glucosidase
GENES       SPO: SPAC14C4.09(agn1) SPBC646.06c
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.59
            ExPASy - ENZYME nomenclature database: 3.2.1.59
            ExplorEnz - The Enzyme Database: 3.2.1.59
            ERGO genome analysis and discovery system: 3.2.1.59
            BRENDA, the Enzyme Database: 3.2.1.59
            CAS: 9075-84-7
///
ENTRY       EC 3.2.1.60                 Enzyme
NAME        glucan 1,4-alpha-maltotetraohydrolase;
            exo-maltotetraohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,4-alpha-D-glucan maltotetraohydrolase
REACTION    Hydrolysis of 1,4-alpha-D-glucosidic linkages in amylaceous
            polysaccharides, to remove successive maltotetraose residues from
            the non-reducing chain ends
COMMENT     Compare EC 3.2.1.2 beta-amylase, which removes successive maltose
            residues, and EC 3.2.1.98 (glucan 1,4-alpha-maltohexaosidase) and EC
            3.2.1.116 (glucan 1,4-alpha-maltotriohydrolase).
REFERENCE   1
  AUTHORS   Nakakuki, T., Azuma, K. and Kainuma, K.
  TITLE     Action patterns of various exo-amylases and the anomeric
            configurations of their products.
  JOURNAL   Carbohydr. Res. 128 (1984) 297-310.
  ORGANISM  Pseudomonas stutzeri, Streptomyces griseus, Aerobacter aerogenes
REFERENCE   2  [PMID:5123132]
  AUTHORS   Robyt JF, Ackerman RJ.
  TITLE     Isolation, purification, and characterization of a
            maltotetraose-producing amylase from Pseudomonas stutzeri.
  JOURNAL   Arch. Biochem. Biophys. 145 (1971) 105-14.
  ORGANISM  Pseudomonas stutzeri
GENES       PMY: Pmen_3136
STRUCTURES  PDB: 1GCY  1JDA  1JDC  1JDD  1QI3  1QI4  1QI5  2AMG  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.60
            ExPASy - ENZYME nomenclature database: 3.2.1.60
            ExplorEnz - The Enzyme Database: 3.2.1.60
            ERGO genome analysis and discovery system: 3.2.1.60
            BRENDA, the Enzyme Database: 3.2.1.60
            CAS: 37288-44-1
///
ENTRY       EC 3.2.1.61                 Enzyme
NAME        mycodextranase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,3-1,4-alpha-D-glucan 4-glucanohydrolase
REACTION    Endohydrolysis of 1,4-alpha-D-glucosidic linkages in alpha-D-glucans
            containing both 1,3- and 1,4-bonds
COMMENT     Products are nigerose and 4-alpha-D-nigerosylglucose. No hydrolysis
            of alpha-D-glucans containing only 1,3- or 1,4-bonds.
REFERENCE   1  [PMID:5652425]
  AUTHORS   Tung KK, Nordin JH.
  TITLE     Structure of the tetrasaccharide produced by the hydrolysis of
            nigeran by the enzyme mycodextranase.
  JOURNAL   Biochim. Biophys. Acta. 158 (1968) 154-6.
  ORGANISM  Penicillium melinii
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.61
            ExPASy - ENZYME nomenclature database: 3.2.1.61
            ExplorEnz - The Enzyme Database: 3.2.1.61
            ERGO genome analysis and discovery system: 3.2.1.61
            BRENDA, the Enzyme Database: 3.2.1.61
            CAS: 9047-04-5
///
ENTRY       EC 3.2.1.62                 Enzyme
NAME        glycosylceramidase;
            phlorizin hydrolase;
            phloretin-glucosidase;
            glycosyl ceramide glycosylhydrolase;
            cerebrosidase;
            phloridzin beta-glucosidase;
            lactase-phlorizin hydrolase;
            phloridzin glucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     glycosyl-N-acylsphingosine glycohydrolase
REACTION    glycosyl-N-acylsphingosine + H2O = N-acylsphingosine + a sugar
            [RN:R01501]
ALL_REAC    R01501
SUBSTRATE   glycosyl-N-acylsphingosine [CPD:C03701];
            H2O [CPD:C00001]
PRODUCT     N-acylsphingosine [CPD:C00195];
            sugar [CPD:C11477]
COMMENT     Broad specificity [cf. EC 3.2.1.45 (glucosylceramidase) and EC
            3.2.1.46 (galactosylceramidase)]. Also hydrolyses phlorizin to
            phloretin and glucose. The intestinal enzyme is a complex that also
            catalyses the reaction of EC 3.2.1.108 lactase.
REFERENCE   1  [PMID:4752949]
  AUTHORS   Leese HJ, Semenza G.
  TITLE     On the identity between the small intestinal enzymes phlorizin
            hydrolase and glycosylceramidase.
  JOURNAL   J. Biol. Chem. 248 (1973) 8170-3.
  ORGANISM  rat [GN:rno], hamster, human [GN:hsa]
REFERENCE   2  [PMID:5082068]
  AUTHORS   Lorenz-Meyer H, Blum AL, Haemmerli HP, Semenza G.
  TITLE     A second enzyme defect in acquired lactase deficiency: lack of
            small-intestinal phlorizin-hydrolase.
  JOURNAL   Eur. J. Clin. Invest. 2 (1972) 326-31.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:5774775]
  AUTHORS   Malathi P, Crane RK.
  TITLE     Phlorizin hydrolase: a beta-glucosidase of hamster intestinal brush
            border membrane.
  JOURNAL   Biochim. Biophys. Acta. 173 (1969) 245-56.
  ORGANISM  hamster
ORTHOLOGY   KO: K01211  glycosylceramidase
GENES       HSA: 3938(LCT)
            MMU: 226413(Lct)
            RNO: 116569(Lct)
            CFA: 483898(LCT)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.62
            ExPASy - ENZYME nomenclature database: 3.2.1.62
            ExplorEnz - The Enzyme Database: 3.2.1.62
            ERGO genome analysis and discovery system: 3.2.1.62
            BRENDA, the Enzyme Database: 3.2.1.62
            CAS: 9033-10-7
///
ENTRY       EC 3.2.1.63                 Enzyme
NAME        1,2-alpha-L-fucosidase;
            almond emulsin fucosidase;
            alpha-(1->2)-L-fucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     2-alpha-L-fucopyranosyl-beta-D-galactoside fucohydrolase
REACTION    methyl-2-alpha-L-fucopyranosyl-beta-D-galactoside + H2O = L-fucose +
            methyl beta-D-galactoside [RN:R04270 R06118]
ALL_REAC    R04270 R06118(G)
SUBSTRATE   methyl-2-alpha-L-fucopyranosyl-beta-D-galactoside [CPD:C04698];
            H2O [CPD:C00001]
PRODUCT     L-fucose [CPD:C01019];
            methyl beta-D-galactoside [CPD:C03619]
COMMENT     Highly specific for non-reducing terminal L-fucose residues linked
            to D-galactose residues by a 1,2-alpha-linkage. Not identical with
            EC 3.2.1.111 1,3-alpha-L-fucosidase.
REFERENCE   1  [PMID:5460888]
  AUTHORS   Bahl OP.
  TITLE     Glycosidases of aspergillus niger. II. Purification and general
            properties of 1,2-alpha-L-fucosidase.
  JOURNAL   J. Biol. Chem. 245 (1970) 299-304.
  ORGANISM  Aspergillus niger
REFERENCE   2  [PMID:18111]
  AUTHORS   Ogata-Arakawa M, Muramatsu T, Kobata A.
  TITLE     alpha-L-fucosidases from almond emulsin: characterization of the two
            enzymes with different specificities.
  JOURNAL   Arch. Biochem. Biophys. 181 (1977) 353-8.
  ORGANISM  Aspergillus niger, Bacillus fulminans, Clostridium perfringens,
            almond
REFERENCE   3  [PMID:7458]
  AUTHORS   Reglero A, Cabezas JA.
  TITLE     Glycosidases of molluscs. Purification and properties of
            alpha-L-fucosidase from Chamelea gallina L.
  JOURNAL   Eur. J. Biochem. 66 (1976) 379-87.
  ORGANISM  Chamelea gallina
STRUCTURES  PDB: 2EAB  2EAC  2EAD  2EAE  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.63
            ExPASy - ENZYME nomenclature database: 3.2.1.63
            ExplorEnz - The Enzyme Database: 3.2.1.63
            ERGO genome analysis and discovery system: 3.2.1.63
            BRENDA, the Enzyme Database: 3.2.1.63
            CAS: 37288-45-2
///
ENTRY       EC 3.2.1.64                 Enzyme
NAME        2,6-beta-fructan 6-levanbiohydrolase;
            beta-2,6-fructan-6-levanbiohydrolase;
            2,6-beta-D-fructan 6-levanbiohydrolase;
            levanbiose-producing levanase;
            2,6-beta-D-fructan 6-beta-D-fructofuranosylfructohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     2,6-beta-D-fructofuranan 6-(beta-D-fructosyl)-D-fructose-hydrolase
REACTION    Hydrolysis of 2,6-beta-D-fructofuranan, to remove successive
            disaccharide residues as levanbiose, i.e.
            6-(beta-D-fructofuranosyl)-D-fructose, from the end of the chain
REFERENCE   1
  AUTHORS   Avigad, G. and Zelikson, R.
  TITLE     Cleavage of fructans to levanbiose by a specific hydrolase.
  JOURNAL   Bull. Res. Counc. Isr. 11 (1963) 253-257.
REFERENCE   2  [PMID:10618232]
  AUTHORS   Saito K, Kondo K, Kojima I, Yokota A, Tomita F.
  TITLE     Purification and characterization of 2,6-beta-D-fructan
            6-levanbiohydrolase from Streptomyces exfoliatus F3-2.
  JOURNAL   Appl. Environ. Microbiol. 66 (2000) 252-6.
  ORGANISM  Streptomyces exfoliatus
REFERENCE   3  [PMID:12586402]
  AUTHORS   Saito K, Oda Y, Tomita F, Yokota A.
  TITLE     Molecular cloning of the gene for 2,6-beta-D-fructan
            6-levanbiohydrolase from Streptomyces exfoliatus F3-2.
  JOURNAL   FEMS. Microbiol. Lett. 218 (2003) 265-70.
  ORGANISM  Streptomyces exfoliatus
REFERENCE   4  [PMID:12095678]
  AUTHORS   Song EK, Kim H, Sung HK, Cha J.
  TITLE     Cloning and characterization of a levanbiohydrolase from
            Microbacterium laevaniformans ATCC 15953.
  JOURNAL   Gene. 291 (2002) 45-55.
  ORGANISM  Microbacterium laevaniformans
REFERENCE   5  [PMID:10334957]
  AUTHORS   Jung Kang E, Lee SO, Lee JD, Lee TH.
  TITLE     Purification and characterization of a levanbiose-producing levanase
            from Pseudomonas sp. No. 43.
  JOURNAL   Biotechnol. Appl. Biochem. 29 ( Pt 3) (1999) 263-8.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.64
            ExPASy - ENZYME nomenclature database: 3.2.1.64
            ExplorEnz - The Enzyme Database: 3.2.1.64
            ERGO genome analysis and discovery system: 3.2.1.64
            BRENDA, the Enzyme Database: 3.2.1.64
            CAS: 37288-46-3
///
ENTRY       EC 3.2.1.65                 Enzyme
NAME        levanase;
            levan hydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     2,6-beta-D-fructan fructanohydrolase
REACTION    Random hydrolysis of 2,6-beta-D-fructofuranosidic linkages in
            2,6-beta-D-fructans (levans) containing more than 3 fructose units
ALL_REAC    (other) R05624 R06206(G)
REFERENCE   1
  AUTHORS   Avigad, G. and Bauer, S.
  TITLE     Fructan hydrolases.
  JOURNAL   Methods Enzymol. 8 (1966) 621-628.
  ORGANISM  Arthrobacter sp.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01212  levanase
GENES       AFM: AFUA_5G00530
            PAT: Patl_3823
            BMA: BMAA0465(sacC)
            BMV: BMASAVP1_0715(sacC)
            BML: BMA10299_1011(sacC)
            BMN: BMA10247_A1985(sacC)
            BVI: Bcep1808_4835
            BCN: Bcen_4097
            BCH: Bcen2424_4269
            BAM: Bamb_3697
            BPS: BPSS0542
            BPM: BURPS1710b_A2101(sacC)
            BPL: BURPS1106A_A0733(sacC)
            BPD: BURPS668_A0821(sacC)
            BTE: BTH_II1873
            NAR: Saro_1884
            GOX: GOX1010
            ABA: Acid345_3886
            BSU: BG10320(sacC)
            BLD: BLi02827(sacC)
            BCL: ABC3116
            SSA: SSA_2023
            ART: Arth_0054 Arth_0404 Arth_0425 Arth_3796
            SEN: SACE_2277(sacC)
            RBA: RB12360
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.65
            ExPASy - ENZYME nomenclature database: 3.2.1.65
            ExplorEnz - The Enzyme Database: 3.2.1.65
            ERGO genome analysis and discovery system: 3.2.1.65
            BRENDA, the Enzyme Database: 3.2.1.65
            CAS: 9041-11-6
///
ENTRY       EC 3.2.1.66                 Enzyme
NAME        quercitrinase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     quercitrin 3-L-rhamnohydrolase
REACTION    quercitrin + H2O = L-rhamnose + quercetin [RN:R02436]
ALL_REAC    R02436
SUBSTRATE   quercitrin [CPD:C01750];
            H2O [CPD:C00001]
PRODUCT     L-rhamnose [CPD:C00507];
            quercetin [CPD:C00389]
COMMENT     Quercitrin is quercetin 3-L-rhamnoside.
REFERENCE   1
  AUTHORS   Westlake, D.W.S.
  TITLE     Microbiological degradation of quercitrin.
  JOURNAL   Can. J. Microbiol. 9 (1963) 211-220.
  ORGANISM  Aspergillus flavus
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.66
            ExPASy - ENZYME nomenclature database: 3.2.1.66
            ExplorEnz - The Enzyme Database: 3.2.1.66
            ERGO genome analysis and discovery system: 3.2.1.66
            BRENDA, the Enzyme Database: 3.2.1.66
            CAS: 37288-47-4
///
ENTRY       EC 3.2.1.67                 Enzyme
NAME        galacturan 1,4-alpha-galacturonidase;
            exopolygalacturonase;
            poly(galacturonate) hydrolase;
            exo-D-galacturonase;
            exo-D-galacturonanase;
            exopoly-D-galacturonase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     poly(1,4-alpha-D-galacturonide) galacturonohydrolase
REACTION    (1,4-alpha-D-galacturonide)n + H2O = (1,4-alpha-D-galacturonide)n-1
            + D-galacturonate [RN:R04320 R06201]
ALL_REAC    R04320 R06201(G);
            (other) R01982 R07413
SUBSTRATE   (1,4-alpha-D-galacturonide)n [CPD:C03816];
            H2O [CPD:C00001]
PRODUCT     (1,4-alpha-D-galacturonide)n-1 [CPD:C03816];
            D-galacturonate [CPD:C00333]
REFERENCE   1  [PMID:5661621]
  AUTHORS   Hasegawa S, Nagel CW.
  TITLE     Isolation of an oligogalacturonate hydrolase from a Bacillus specie.
  JOURNAL   Arch. Biochem. Biophys. 124 (1968) 513-20.
  ORGANISM  Bacillus sp.
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01213  galacturan 1,4-alpha-galacturonidase
GENES       ATH: AT1G02790(PGA4) AT3G07850
            AFM: AFUA_8G02630 AFUA_8G06890
            RLE: pRL120688
            CSC: Csac_0361
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.67
            ExPASy - ENZYME nomenclature database: 3.2.1.67
            ExplorEnz - The Enzyme Database: 3.2.1.67
            ERGO genome analysis and discovery system: 3.2.1.67
            BRENDA, the Enzyme Database: 3.2.1.67
            CAS: 9045-35-6
///
ENTRY       EC 3.2.1.68                 Enzyme
NAME        isoamylase;
            debranching enzyme
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     glycogen alpha-1,6-glucanohydrolase
REACTION    Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen,
            amylopectin and their beta-limit dextrins
COMMENT     Also readily hydrolyses amylopectin. Differs from EC 3.2.1.41
            (pullulanase) and EC 3.2.1.142 (limit dextrinase) by its inability
            to hydrolyse pullulan, and by limited action on alpha-limit
            dextrins. Maltose is the smallest sugar it can release from an
            alpha-(1->6)-linkage.
REFERENCE   1  [PMID:5456995]
  AUTHORS   Yokobayashi K, Misaki A, Harada T.
  TITLE     Purification and properties of Pseudomonas isoamylase.
  JOURNAL   Biochim. Biophys. Acta. 212 (1970) 458-69.
  ORGANISM  Pseudomonas sp.
ORTHOLOGY   KO: K01214  isoamylase
GENES       CME: CMI294C
            VFI: VFA0801
            NOC: Noc_1740(glgX)
            BUR: Bcep18194_C7031(glgX)
            NWI: Nwi_1206(glgX)
            GBE: GbCGDNIH1_0916 GbCGDNIH1_2172
            RRU: Rru_A2577
            GKA: GK2827
            SSA: SSA_2268(pulA)
            RHA: RHA1_ro06450
            FAL: FRAAL2118(iam)
            FNU: FN0799
            CTA: CTA_0046(glgX)
            PMB: A9601_15221(glgX)
            PMC: P9515_14831(glgX)
            PMF: P9303_05691(glgX)
            PMG: P9301_15081(glgX)
            PME: NATL1_17491(glgX)
STRUCTURES  PDB: 1BF2  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.68
            ExPASy - ENZYME nomenclature database: 3.2.1.68
            ExplorEnz - The Enzyme Database: 3.2.1.68
            ERGO genome analysis and discovery system: 3.2.1.68
            BRENDA, the Enzyme Database: 3.2.1.68
            CAS: 9067-73-6
///
ENTRY       EC 3.2.1.69       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
COMMENT     Deleted entry: amylopectin 6-glucanohydrolase. Now included with EC
            3.2.1.41 pullulanase (EC 3.2.1.69 created 1972, deleted 1976)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.69
            ExPASy - ENZYME nomenclature database: 3.2.1.69
            ExplorEnz - The Enzyme Database: 3.2.1.69
            ERGO genome analysis and discovery system: 3.2.1.69
            BRENDA, the Enzyme Database: 3.2.1.69
///
ENTRY       EC 3.2.1.70                 Enzyme
NAME        glucan 1,6-alpha-glucosidase;
            exo-1,6-beta-glucosidase;
            glucodextrinase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     glucan alpha-1,6-D-glucohydrolase
REACTION    Hydrolysis of (1->6)-alpha-D-glucosidic linkages in
            (1->6)-alpha-D-glucans and derived oligosaccharides
COMMENT     Hydrolysis is accompanied by inversion at C-1, so that new reducing
            ends are released in the beta-configuration. Dextrans and
            isomaltosaccharides are hydrolysed, as is isomaltose, but very
            slowly. The enzyme from some sources also possesses the activity of
            EC 3.2.1.59 (glucan endo-1,3-alpha-glucosidase).
REFERENCE   1
  AUTHORS   Ohya, T., Sawai, T., Uemura, S. and Abe, K.
  TITLE     Some catalytic properties of an exo-1,6-alpha-glucosidase
            (glucodextranase) from Arthrobacter globiformis I42.
  JOURNAL   Agric. Biol. Chem. 42 (1978) 571-577.
  ORGANISM  Arthrobacter globiformis
REFERENCE   2
  AUTHORS   Sawai, T., Yamaki, T. and Ohya, T.
  TITLE     Preparation and some properties of Arthrobacter globiformis
            exo-1,6-alpha-glucosidase.
  JOURNAL   Agric. Biol. Chem. 40 (1976) 1293-1299.
  ORGANISM  Arthrobacter globiformis
REFERENCE   3  [PMID:4356399]
  AUTHORS   Walker GJ, Pulkownik A.
  TITLE     Degradation of dextrans by an alpha-1,6-glucan glucohydrolase from
            Streptococcus mitis.
  JOURNAL   Carbohydr. Res. 29 (1973) 1-14.
  ORGANISM  Streptococcus mitis
ORTHOLOGY   KO: K01215  glucan 1,6-alpha-glucosidase
GENES       AFM: AFUA_2G11620 AFUA_7G06380
            VFI: VFA0731
            LLA: L124628(dexB)
            LLC: LACR_1851
            SPY: SPy_1973(dexB)
            SPZ: M5005_Spy_1681(dexB)
            SPM: spyM18_2039
            SPG: SpyM3_1695(dexB)
            SPS: SPs1697
            SPH: MGAS10270_Spy1750(dexB)
            SPI: MGAS10750_Spy1775(dexB)
            SPJ: MGAS2096_Spy1704(dexB)
            SPK: MGAS9429_Spy1684(dexB)
            SPF: SpyM51652(dexB)
            SPA: M6_Spy1689
            SPB: M28_Spy1669(dexB)
            SPN: SP_0342
            SPR: spr0310(dexB)
            SPD: SPD_0311(dexB)
            SAG: SAG1924(dexB)
            SAN: gbs1911
            SAK: SAK_1883(dexB)
            SMU: SMU.883(dexB)
            LPL: lp_3641(dexB)
            LJO: LJ0220
            LAC: LBA0264
            LSA: LSA1791(dexB)
            LGA: LGAS_0222
            EFA: EF1348
            MPU: MYPU_4630(dexB)
            MMO: MMOB3610(dexB)
            MCP: MCAP_0191
STRUCTURES  PDB: 1UG9  1ULV  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.70
            ExPASy - ENZYME nomenclature database: 3.2.1.70
            ExplorEnz - The Enzyme Database: 3.2.1.70
            ERGO genome analysis and discovery system: 3.2.1.70
            BRENDA, the Enzyme Database: 3.2.1.70
            CAS: 37288-48-5
///
ENTRY       EC 3.2.1.71                 Enzyme
NAME        glucan endo-1,2-beta-glucosidase;
            endo-1,2-beta-glucanase;
            beta-D-1,2-glucanase;
            endo-(1->2)-beta-D-glucanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,2-beta-D-glucan glucanohydrolase
REACTION    Random hydrolysis of 1,2-glucosidic linkages in 1,2-beta-D-glucans
REFERENCE   1
  AUTHORS   Reese, E.T., Parrish, F.W. and Mandels, M.
  TITLE     beta-D-1,2-Glucanases in fungi.
  JOURNAL   Can. J. Microbiol. 7 (1961) 309-317.
  ORGANISM  Aspergillus auratus, Aspergillus aureolus, Aspergillus
            quadricinctus, Aspergillus sydowi, Aspergillus unguis, Beauveria
            bassiana, Fusarium oxysporum, Penicillium brefeldianum, Penicillium
            funiculosum, Penicillium melinii, Penicillium parvum, Penicillium
            quadrilineatum, Penicillium verruculosum
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.71
            ExPASy - ENZYME nomenclature database: 3.2.1.71
            ExplorEnz - The Enzyme Database: 3.2.1.71
            ERGO genome analysis and discovery system: 3.2.1.71
            BRENDA, the Enzyme Database: 3.2.1.71
            CAS: 37288-49-6
///
ENTRY       EC 3.2.1.72                 Enzyme
NAME        xylan 1,3-beta-xylosidase;
            1,3-beta-D-xylosidase, exo-1,3-beta-xylosidase;
            beta-1,3'-xylanase;
            exo-beta-1,3'-xylanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,3-beta-D-xylan xylohydrolase
REACTION    Hydrolysis of successive xylose residues from the non-reducing
            termini of 1,3-beta-D-xylans
REFERENCE   1
  AUTHORS   Fukui, S., Suzuki, T., Kitahara, K. and Miwa, T.
  TITLE     beta-1,3'-Xylanase.
  JOURNAL   J. Gen. Appl. Microbiol. 6 (1960) 270-282.
  ORGANISM  Chaetomium globosum
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.72
            ExPASy - ENZYME nomenclature database: 3.2.1.72
            ExplorEnz - The Enzyme Database: 3.2.1.72
            ERGO genome analysis and discovery system: 3.2.1.72
            BRENDA, the Enzyme Database: 3.2.1.72
            CAS: 37288-50-9
///
ENTRY       EC 3.2.1.73                 Enzyme
NAME        licheninase;
            lichenase;
            beta-(1->4)-D-glucan 4-glucanohydrolase;
            1,3;
            1,4-beta-glucan endohydrolase;
            1,3;
            1,4-beta-glucan 4-glucanohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,3-1,4-beta-D-glucan 4-glucanohydrolase
REACTION    Hydrolysis of 1,4-beta-D-glucosidic linkages in beta-D-glucans
            containing 1,3- and 1,4-bonds
COMMENT     Acts on lichenin and cereal beta-D-glucans, but not on
            beta-D-glucans containing only 1,3- or 1,4-bonds.
REFERENCE   1
  AUTHORS   Barras, D.R., Moore, A.E. and Stone, B.A.
  TITLE     Enzyme-substrate relations among beta-glucan hydrolases.
  JOURNAL   Adv. Chem. Ser. 95 (1969) 105-138.
ORTHOLOGY   KO: K01216  licheninase
GENES       PIC: PICST_25832(CRH1)
            CPS: CPS_3723(bglA)
            MMW: Mmwyl1_3714
            RSH: Rsph17029_1209
            BSU: BG10476(bglS)
            BAY: RBAM_036190(bglS)
            BPU: BPUM_0463(bglS)
            SSA: SSA_0182
            RBA: RB5011
            BFR: BF4251
            BFS: BF4060
            SRU: SRU_2844
            CHU: CHU_1727(cel)
            FJO: Fjoh_1022
STRUCTURES  PDB: 1AJK  1AJO  1AQ0  1AXK  1BYH  1CPM  1CPN  1GBG  1GHR  1GLH  
                 1MAC  1MVE  1U0A  1ZM1  2AYH  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.73
            ExPASy - ENZYME nomenclature database: 3.2.1.73
            ExplorEnz - The Enzyme Database: 3.2.1.73
            ERGO genome analysis and discovery system: 3.2.1.73
            BRENDA, the Enzyme Database: 3.2.1.73
            CAS: 37288-51-0
///
ENTRY       EC 3.2.1.74                 Enzyme
NAME        glucan 1,4-beta-glucosidase;
            exo-1,4-beta-glucosidase;
            exocellulase;
            exo-beta-1,4-glucosidase;
            exo-beta-1,4-glucanase;
            beta-1,4-beta-glucanase;
            beta-glucosidase;
            exo-1,4-beta-glucanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,4-beta-D-glucan glucohydrolase
REACTION    Hydrolysis of 1,4-linkages in 1,4-beta-D-glucans, to remove
            successive glucose units
ALL_REAC    (other) R00306 R01444 R03801 R03802 R05141 R05142 R06104(G)
            R06105(G) R06106(G) R06107(G) R06108(G) R06109(G)
COMMENT     Acts on 1,4-beta-D-glucans and related oligosaccharides. Cellobiose
            is hydrolysed, but very slowly.
REFERENCE   1
  AUTHORS   Barras, D.R., Moore, A.E. and Stone, B.A.
  TITLE     Enzyme-substrate relations among beta-glucan hydrolases.
  JOURNAL   Adv. Chem. Ser. 95 (1969) 105-138.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
GENES       XCV: XCV1823(celD)
            SEN: SACE_6502(celD)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.74
            ExPASy - ENZYME nomenclature database: 3.2.1.74
            ExplorEnz - The Enzyme Database: 3.2.1.74
            ERGO genome analysis and discovery system: 3.2.1.74
            BRENDA, the Enzyme Database: 3.2.1.74
            CAS: 37288-52-1
///
ENTRY       EC 3.2.1.75                 Enzyme
NAME        glucan endo-1,6-beta-glucosidase;
            endo-1,6-beta-glucanase;
            beta-1->6)-beta-D-glucanase;
            beta-1,6-glucanase-pustulanase;
            beta-1,6-glucan hydrolase;
            beta-1,6-glucan 6-glucanohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,6-beta-D-glucan glucanohydrolase
REACTION    Random hydrolysis of 1,6-linkages in 1,6-beta-D-glucans
COMMENT     Acts on lutean, pustulan and 1,6-oligo-beta-D-glucosides.
REFERENCE   1  [PMID:14491003]
  AUTHORS   REESE ET, PARRISH FW, MANDELS M.
  TITLE     Beta-d-1, 6-Glucanases in fungi.
  JOURNAL   Can. J. Microbiol. 8 (1962) 327-34.
  ORGANISM  Aspergillus aureolus, Aspergillus quadricinctus, Aspergillus unguis,
            Aspergillus versicolor, Beauveria bassiana, Fusarium roseum,
            Penicillium brefeldianum, Penicillium digitatum, Penicillium
            ehrlichii, Penicillium funiculosum, Penicillium herquei, Penicillium
            janthinellum, Penicillium javanicum, Penicillium nigricans,
            Penicillium ochro-chloron, Penicillium oxolicum, Penicillium parvum,
            Penicillium spinulosum, Poria cocos, Trichoderma viride, Trichoderma
            lignorum
GENES       FJO: Fjoh_1566 Fjoh_1905
            FNO: Fnod_0296
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.75
            ExPASy - ENZYME nomenclature database: 3.2.1.75
            ExplorEnz - The Enzyme Database: 3.2.1.75
            ERGO genome analysis and discovery system: 3.2.1.75
            BRENDA, the Enzyme Database: 3.2.1.75
            CAS: 37278-39-0
///
ENTRY       EC 3.2.1.76                 Enzyme
NAME        L-iduronidase;
            alpha-L-iduronidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     glycosaminoglycan alpha-L-iduronohydrolase
REACTION    Hydrolysis of unsulfated alpha-L-iduronosidic linkages in dermatan
            sulfate
ALL_REAC    (other) R07813(G) R07822(G)
REFERENCE   1  [PMID:4993544]
  AUTHORS   Matalon R, Cifonelli JA, Dorfman A.
  TITLE     L-iduronidase in cultured human fibroblasts and liver.
  JOURNAL   Biochem. Biophys. Res. Commun. 42 (1971) 340-5.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:30407]
  AUTHORS   Rome LH, Garvin AJ, Neufeld EF.
  TITLE     Human kidney alpha-L-iduronidase: purification and characterization.
  JOURNAL   Arch. Biochem. Biophys. 189 (1978) 344-53.
  ORGANISM  human [GN:hsa]
REFERENCE   3
  AUTHORS   Srivastava, R.M., Hudson, N., Seymour, F.R. and Weissman, B.
  TITLE     Preparation of (aryl alpha-L-idopyranosid)uronic acids.
  JOURNAL   Carbohydr. Res. 60 (1978) 315-326.
PATHWAY     PATH: map00531  Glycosaminoglycan degradation
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01217  L-iduronidase
GENES       HSA: 3425(IDUA)
            MMU: 15932(Idua)
            GGA: 427294(RCJMB04_31l23)
            SPU: 592184(LOC592184)
            RLE: pRL100282
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.76
            ExPASy - ENZYME nomenclature database: 3.2.1.76
            ExplorEnz - The Enzyme Database: 3.2.1.76
            ERGO genome analysis and discovery system: 3.2.1.76
            BRENDA, the Enzyme Database: 3.2.1.76
            CAS: 9073-56-7
///
ENTRY       EC 3.2.1.77                 Enzyme
NAME        mannan 1,2-(1,3)-alpha-mannosidase;
            exo-1,2-1,3-alpha-mannosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,2-1,3-alpha-D-mannan mannohydrolase
REACTION    Hydrolysis of 1,2- and 1,3-linkages in yeast mannan, releasing
            mannose
ALL_REAC    (other) R01331(G) R05816 R06150(G) R06151(G)
COMMENT     A 1,6-alpha-D-mannan backbone remains after action on yeast mannan.
            This is further attacked, but slowly.
REFERENCE   1  [PMID:5769177]
  AUTHORS   Jones GH, Ballou CE.
  TITLE     Studies on the structure of yeast mannan. I. Purification and some
            properties of an alpha-mannosidase from an arthrobacter species.
  JOURNAL   J. Biol. Chem. 244 (1969) 1043-51.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:5814027]
  AUTHORS   Jones GH, Ballou CE.
  TITLE     Studies on the structure of yeast mannan. II. Mode of action of the
            Arthrobacter alpha-mannosidase on yeast mannan.
  JOURNAL   J. Biol. Chem. 244 (1969) 1052-9.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.77
            ExPASy - ENZYME nomenclature database: 3.2.1.77
            ExplorEnz - The Enzyme Database: 3.2.1.77
            ERGO genome analysis and discovery system: 3.2.1.77
            BRENDA, the Enzyme Database: 3.2.1.77
            CAS: 37288-53-2
///
ENTRY       EC 3.2.1.78                 Enzyme
NAME        mannan endo-1,4-beta-mannosidase;
            endo-1,4-beta-mannanase;
            endo-beta-1,4-mannase;
            beta-mannanase B;
            beta-1, 4-mannan 4-mannanohydrolase;
            endo-beta-mannanase;
            beta-D-mannanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,4-beta-D-mannan mannanohydrolase
REACTION    Random hydrolysis of 1,4-beta-D-mannosidic linkages in mannans,
            galactomannans and glucomannans
ALL_REAC    (other) R01332 R06207(G)
REFERENCE   1
  AUTHORS   Eriksson, A.F.V.
  TITLE     Purification and characterisation of a fungal beta-mannanase.
  JOURNAL   Acta Chem. Scand. 22 (1968) 1924-1934.
  ORGANISM  Aspergillus niger
REFERENCE   2
  AUTHORS   Reese, E.T.
  TITLE     beta-Mannanases of fungi.
  JOURNAL   Can. J. Microbiol. 11 (1965) 167-183.
  ORGANISM  Paecilomyces variotii, Penicillium funiculosum, Penicillium
            wortmanni, Penicillium verruculosum, Penicillium ochro-chloron,
            Fusicoccum sp., Aspergillus luchuensis, Aspergillus giganteus,
            Paecilomyces variotii
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K01218  mannan endo-1,4-beta-mannosidase
GENES       XCC: XCC1778
            XCB: XC_2458
            XCV: XCV1826
            XAC: XAC1796
            SDE: Sde_3691
            BSU: BG12197(ydhT)
            BCL: ABC0320
            BAY: RBAM_035930(ydhT)
            BPU: BPUM_1561
            CSC: Csac_0663
            RHA: RHA1_ro03572
            BFR: BF0846
            BFS: BF0771(manA)
            FJO: Fjoh_2729 Fjoh_4957
STRUCTURES  PDB: 1BQC  1GVY  1GW1  1J9Y  1ODZ  1PMH  1PMJ  1QNO  1QNP  1QNQ  
                 1QNR  1QNS  1R7O  1RH9  1WKY  2BVT  2BVY  2C0H  2MAN  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.78
            ExPASy - ENZYME nomenclature database: 3.2.1.78
            ExplorEnz - The Enzyme Database: 3.2.1.78
            ERGO genome analysis and discovery system: 3.2.1.78
            BRENDA, the Enzyme Database: 3.2.1.78
            CAS: 37288-54-3
///
ENTRY       EC 3.2.1.79       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
COMMENT     Deleted entry: alpha-L-arabinofuranoside hydrolase. Now included
            with EC 3.2.1.55 alpha-N-arabinofuranosidase (EC 3.2.1.79 created
            1972, deleted 1976)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.79
            ExPASy - ENZYME nomenclature database: 3.2.1.79
            ExplorEnz - The Enzyme Database: 3.2.1.79
            ERGO genome analysis and discovery system: 3.2.1.79
            BRENDA, the Enzyme Database: 3.2.1.79
///
ENTRY       EC 3.2.1.80                 Enzyme
NAME        fructan beta-fructosidase;
            exo-beta-D-fructosidase;
            exo-beta-fructosidase;
            polysaccharide beta-fructofuranosidase;
            fructan exohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     beta-D-fructan fructohydrolase
REACTION    Hydrolysis of terminal, non-reducing 2,1- and 2,6-linked
            beta-D-fructofuranose residues in fructans
ALL_REAC    (other) R00879 R06208(G)
COMMENT     Hydrolyses inulin and levan, and also sucrose.
REFERENCE   1  [PMID:5244285]
  AUTHORS   DaCosta T, Gibbons RJ.
  TITLE     Hydrolysis of levan by human plaque streptococci.
  JOURNAL   Arch. Oral. Biol. 13 (1968) 609-17.
  ORGANISM  Streptococcus salivarius
REFERENCE   2  [PMID:4045423]
  AUTHORS   Jacques NJ, Morrey-Jones JG, Walker GJ.
  TITLE     Inducible and constitutive formation of fructanase in batch and
            continuous cultures of Streptococcus mutans.
  JOURNAL   J. Gen. Microbiol. 131 (1985) 1625-33.
  ORGANISM  Streptococcus mutans [GN:smu]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K03332  fructan beta-fructosidase
GENES       SMU: SMU.78(fruA)
            SSA: SSA_2023
            SGO: SGO_0385
STRUCTURES  PDB: 1ST8  1Y4W  1Y9G  1Y9M  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.80
            ExPASy - ENZYME nomenclature database: 3.2.1.80
            ExplorEnz - The Enzyme Database: 3.2.1.80
            ERGO genome analysis and discovery system: 3.2.1.80
            BRENDA, the Enzyme Database: 3.2.1.80
            CAS: 37288-56-5
///
ENTRY       EC 3.2.1.81                 Enzyme
NAME        beta-agarase;
            agarase (ambiguous);
            AgaA;
            AgaB;
            endo-beta-agarase;
            agarose 3-glycanohydrolase (incorrect)
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     agarose 4-glycanohydrolase
REACTION    Hydrolysis of 1,4-beta-D-galactosidic linkages in agarose, giving
            the tetramer as the predominant product
COMMENT     Also acts on porphyran, but more slowly [1]. This enzyme cleaves the
            beta-(1->4) linkages of agarose in a random manner with retention of
            the anomeric-bond configuration, producing beta-anomers that give
            rise progressively to alpha-anomers when mutarotation takes place
            [6]. The end products of hydrolysis are neoagarotetraose and
            neoagarohexaose in the case of AgaA from the marine bacterium
            Zobellia galactanivorans, and neoagarotetraose and neoagarobiose in
            the case of AgaB [6].
REFERENCE   1  [PMID:5386190]
  AUTHORS   Duckworth M, Turvey JR.
  TITLE     The action of a bacterial agarase on agarose, porphyran and
            alkali-treated porphyran.
  JOURNAL   Biochem. J. 113 (1969) 687-92.
  ORGANISM  Cytophaga sp.
REFERENCE   2  [PMID:12970344]
  AUTHORS   Allouch J, Jam M, Helbert W, Barbeyron T, Kloareg B, Henrissat B,
            Czjzek M.
  TITLE     The three-dimensional structures of two beta-agarases.
  JOURNAL   J. Biol. Chem. 278 (2003) 47171-80.
  ORGANISM  Zobellia galactanivorans
REFERENCE   3  [PMID:15170112]
  AUTHORS   Ohta Y, Nogi Y, Miyazaki M, Li Z, Hatada Y, Ito S, Horikoshi K.
  TITLE     Enzymatic properties and nucleotide and amino acid sequences of a
            thermostable beta-agarase from the novel marine isolate, JAMB-A94.
  JOURNAL   Biosci. Biotechnol. Biochem. 68 (2004) 1073-81.
  ORGANISM  Microbulbifer salipaludis
REFERENCE   4  [PMID:15088129]
  AUTHORS   Ohta Y, Hatada Y, Nogi Y, Miyazaki M, Li Z, Akita M, Hidaka Y, Goda
            S, Ito S, Horikoshi K.
  TITLE     Enzymatic properties and nucleotide and amino acid sequences of a
            thermostable beta-agarase from a novel species of deep-sea
            Microbulbifer.
  JOURNAL   Appl. Microbiol. Biotechnol. 64 (2004) 505-14.
  ORGANISM  Microbulbifer elongataus, Microbulbifer salipaludis, Microbulbifer
            elongataus, Microbulbifer hydrolyticus
REFERENCE   5  [PMID:8517750]
  AUTHORS   Sugano Y, Terada I, Arita M, Noma M, Matsumoto T.
  TITLE     Purification and characterization of a new agarase from a marine
            bacterium, Vibrio sp. strain JT0107.
  JOURNAL   Appl. Environ. Microbiol. 59 (1993) 1549-54.
  ORGANISM  Undaria pinnatiJida, Laminaria sp., Vibrio sp.
REFERENCE   6  [PMID:15456406]
  AUTHORS   Jam M, Flament D, Allouch J, Potin P, Thion L, Kloareg B, Czjzek M,
            Helbert W, Michel G, Barbeyron T.
  TITLE     The endo-beta-agarases AgaA and AgaB from the marine bacterium
            Zobellia galactanivorans: two paralogue enzymes with different
            molecular organizations and catalytic behaviours.
  JOURNAL   Biochem. J. 385 (2005) 703-13.
  ORGANISM  Zobellia galactanivorans
ORTHOLOGY   KO: K01219  agarase
GENES       PPF: Pput_1162
            PAT: Patl_1904 Patl_1971 Patl_2341 Patl_2640 Patl_2642
            SDE: Sde_1175 Sde_1176 Sde_2644 Sde_2650 Sde_2655
            RPB: RPB_3029
            RPD: RPD_2419
            RPE: RPE_4620
            SCO: SCO3471(dagA)
            RBA: RB3421(agrA)
STRUCTURES  PDB: 1O4Y  1O4Z  1URX  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.81
            ExPASy - ENZYME nomenclature database: 3.2.1.81
            ExplorEnz - The Enzyme Database: 3.2.1.81
            ERGO genome analysis and discovery system: 3.2.1.81
            BRENDA, the Enzyme Database: 3.2.1.81
            CAS: 37288-57-6
///
ENTRY       EC 3.2.1.82                 Enzyme
NAME        exo-poly-alpha-galacturonosidase;
            exopolygalacturonosidase;
            exopolygalacturanosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
REACTION    Hydrolysis of pectic acid from the non-reducing end, releasing
            digalacturonate
REFERENCE   1  [PMID:5661621]
  AUTHORS   Hasegawa S, Nagel CW.
  TITLE     Isolation of an oligogalacturonate hydrolase from a Bacillus specie.
  JOURNAL   Arch. Biochem. Biophys. 124 (1968) 513-20.
  ORGANISM  Bacillus sp.
REFERENCE   2
  AUTHORS   Hatanaka, C. and Ozawa, J.
  TITLE     Enzymic degradation of pectic acid. XIII. New exopolygalacturonase
            producing digalacturonic acid from pectic acid.
  JOURNAL   J. Agric. Chem. Soc. Jpn.. 43 (1968) 764-772.
REFERENCE   3
  AUTHORS   Hatanaka, C. and Ozawa, J.
  TITLE     Enzymic degradation of pectic acid. XIII. New exopolygalacturonase
            producing digalacturonic acid from pectic acid.
  JOURNAL   J. Agric. Chem. Soc. Jpn. 15 (1971) 47.
GENES       YEN: YE0164(pehX)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.82
            ExPASy - ENZYME nomenclature database: 3.2.1.82
            ExplorEnz - The Enzyme Database: 3.2.1.82
            ERGO genome analysis and discovery system: 3.2.1.82
            BRENDA, the Enzyme Database: 3.2.1.82
            CAS: 37288-58-7
///
ENTRY       EC 3.2.1.83                 Enzyme
NAME        kappa-carrageenase;
            kappa-carrageenan 4-beta-D-glycanohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     kappa-carrageenan 4-beta-D-glycanohydrolase
            (configuration-retaining)
REACTION    Endohydrolysis of 1,4-beta-D-linkages between D-galactose 4-sulfate
            and 3,6-anhydro-D-galactose in kappa-carrageenans
COMMENT     The main products of hydrolysis are neocarrabiose-sulfate and
            neocarratetraose-sulfate [5]. Unlike EC 3.2.1.157
            (iota-carrageenase), but similar to EC 3.2.1.81 (beta-agarase), this
            enzyme proceeds with retention of the anomeric configuration.
REFERENCE   1  [PMID:5972647]
  AUTHORS   Weigl J, Yaphe W.
  TITLE     The enzymic hydrolysis of carrageenan by Pseudomonas carrageenovora:
            purification of a kappa-carrageenase.
  JOURNAL   Can. J. Microbiol. 12 (1966) 939-47.
  ORGANISM  Pseudomonas carrageenovora
REFERENCE   2  [PMID:1915370]
  AUTHORS   Potin P, Sanseau A, Le Gall Y, Rochas C, Kloareg B.
  TITLE     Purification and characterization of a new kappa-carrageenase from a
            marine Cytophaga-like bacterium.
  JOURNAL   Eur. J. Biochem. 201 (1991) 241-7.
  ORGANISM  Delesseria sanguinea
REFERENCE   3  [PMID:7737202]
  AUTHORS   Potin P, Richard C, Barbeyron T, Henrissat B, Gey C, Petillot Y,
            Forest E, Dideberg O, Rochas C, Kloareg B.
  TITLE     Processing and hydrolytic mechanism of the cgkA-encoded
            kappa-carrageenase of Alteromonas carrageenovora.
  JOURNAL   Eur. J. Biochem. 228 (1995) 971-5.
  ORGANISM  Alteromonas carrageenovora
REFERENCE   4  [PMID:10089334]
  AUTHORS   Michel G, Barbeyron T, Flament D, Vernet T, Kloareg B, Dideberg O.
  TITLE     Expression, purification, crystallization and preliminary x-ray
            analysis of the kappa-carrageenase from Pseudoalteromonas
            carrageenovora.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 55 (1999) 918-20.
  ORGANISM  Pseudomonas carrageenovora
REFERENCE   5  [PMID:11435116]
  AUTHORS   Michel G, Chantalat L, Duee E, Barbeyron T, Henrissat B, Kloareg B,
            Dideberg O.
  TITLE     The kappa-carrageenase of P. carrageenovora features a tunnel-shaped
            active site: a novel insight in the evolution of Clan-B glycoside
            hydrolases.
  JOURNAL   Structure. 9 (2001) 513-25.
  ORGANISM  Pseudomonas carrageenovora
ORTHOLOGY   KO: K05990  
GENES       RBA: RB2702
STRUCTURES  PDB: 1DYP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.83
            ExPASy - ENZYME nomenclature database: 3.2.1.83
            ExplorEnz - The Enzyme Database: 3.2.1.83
            ERGO genome analysis and discovery system: 3.2.1.83
            BRENDA, the Enzyme Database: 3.2.1.83
            CAS: 37288-59-8
///
ENTRY       EC 3.2.1.84                 Enzyme
NAME        glucan 1,3-alpha-glucosidase;
            exo-1,3-alpha-glucanase;
            glucosidase II
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,3-alpha-D-glucan 3-glucohydrolase
REACTION    Hydrolysis of terminal 1,3-alpha-D-glucosidic links in
            1,3-alpha-D-glucans
ALL_REAC    (other) R05980(G) R05981(G)
COMMENT     Does not act on nigeran.
REFERENCE   1  [PMID:4622000]
  AUTHORS   Zonneveld BJ.
  TITLE     A new type of enzyme, and exo-splitting  -1,3 glucanase from
            non-induced cultures of Aspergillus nidulans.
  JOURNAL   Biochim. Biophys. Acta. 258 (1972) 541-7.
  ORGANISM  Aspergillus nidulans [GN:ani]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K05546  alpha 1,3-glucosidase
GENES       HSA: 23193(GANAB)
            PTR: 451258(GANAB)
            MMU: 14376(Ganab)
            RNO: 293721(Ganab_predicted)
            CFA: 483784(GANAB)
            BTA: 540155(LOC540155)
            SSC: 396938(G2AN)
            OSA: 4332068
            SCE: YBR229C(ROT2)
            AGO: AGOS_AAR173C
            CAL: CaO19_974(CaO19.974)
            CGR: CAGL0K06963g
            SPO: SPAC1002.03c
            ANI: AN8217.2
            AFM: AFUA_5G03500
            AOR: AO090102000559
            CNE: CNB05150
            DDI: DDB_0191113(modA)
            ENT: Ent638_1312
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.84
            ExPASy - ENZYME nomenclature database: 3.2.1.84
            ExplorEnz - The Enzyme Database: 3.2.1.84
            ERGO genome analysis and discovery system: 3.2.1.84
            BRENDA, the Enzyme Database: 3.2.1.84
            CAS: 9073-99-8
///
ENTRY       EC 3.2.1.85                 Enzyme
NAME        6-phospho-beta-galactosidase;
            phospho-beta-galactosidase;
            beta-D-phosphogalactoside galactohydrolase;
            phospho-beta-D-galactosidase;
            6-phospho-beta-D-galactosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     6-phospho-beta-D-galactoside 6-phosphogalactohydrolase
REACTION    a 6-phospho-beta-D-galactoside + H2O = 6-phospho-D-galactose + an
            alcohol [RN:R03255]
ALL_REAC    R03255 > R03256 R06110(G)
SUBSTRATE   6-phospho-beta-D-galactoside [CPD:C03847];
            H2O [CPD:C00001]
PRODUCT     6-phospho-D-galactose [CPD:C01113];
            alcohol [CPD:C00069]
REFERENCE   1  [PMID:5447434]
  AUTHORS   Hengstenberg W, Penberthy WK, Morse ML.
  TITLE     Purification of the staphylococcal 6-phospho-beta-D-- galactosidase.
  JOURNAL   Eur. J. Biochem. 14 (1970) 27-32.
  ORGANISM  Staphylococcus aureus
PATHWAY     PATH: map00052  Galactose metabolism
ORTHOLOGY   KO: K01220  6-phospho-beta-galactosidase
GENES       SAU: SA1991(lacG)
            SAV: SAV2189(lacG)
            SAM: MW2115(lacG)
            SAR: SAR2280(lacG)
            SAS: SAS2090
            SAC: SACOL2180(lacG)
            SAB: SAB2070c(lacG)
            SAA: SAUSA300_2149(lacG)
            SAO: SAOUHSC_02449
            SAJ: SaurJH9_2220
            SAH: SaurJH1_2259
            SEP: SE1781
            SER: SERP1789(lacG)
            SHA: SH0848(lacG)
            LLC: LACR_D39
            SPY: SPy_1916(lacG)
            SPZ: M5005_Spy_1632(lacG)
            SPM: spyM18_1984
            SPG: SpyM3_1653(lacG)
            SPS: SPs1651
            SPH: MGAS10270_Spy1701(lacG)
            SPI: MGAS10750_Spy1729(lacG)
            SPJ: MGAS2096_Spy1657(lacG)
            SPK: MGAS9429_Spy1635(lacG)
            SPF: SpyM51607(lacG)
            SPA: M6_Spy1641
            SPB: M28_Spy1622(lacG)
            SPN: SP_0477 SP_1184
            SPR: spr0424(lacG) spr1069(lacG)
            SPD: SPD_0427(lacG-1) SPD_1046(lacG-2)
            SAN: gbs1329
            SMU: SMU.1490(lacG)
            SSA: SSA_1692(lacG)
            SSU: SSU05_1036
            SSV: SSU98_1048
            SGO: SGO_1512(lacG)
            LCA: LSEI_A04
            LGA: LGAS_0344 LGAS_0502
            CAC: CAC2963(lacG)
STRUCTURES  PDB: 1PBG  2PBG  3PBG  4PBG  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.85
            ExPASy - ENZYME nomenclature database: 3.2.1.85
            ExplorEnz - The Enzyme Database: 3.2.1.85
            ERGO genome analysis and discovery system: 3.2.1.85
            BRENDA, the Enzyme Database: 3.2.1.85
            CAS: 37237-42-6
///
ENTRY       EC 3.2.1.86                 Enzyme
NAME        6-phospho-beta-glucosidase;
            phospho-beta-glucosidase A;
            phospho-beta-glucosidase;
            phosphocellobiase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     6-phospho-beta-D-glucosyl-(1,4)-D-glucose glucohydrolase
REACTION    6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H2O = D-glucose +
            D-glucose 6-phosphate [RN:R00839 R06112]
ALL_REAC    R00839 R06112(G);
            (other) R05133 R05134
SUBSTRATE   6-phospho-beta-D-glucosyl-(1,4)-D-glucose [CPD:C04534];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031];
            D-glucose 6-phosphate [CPD:C00092]
COMMENT     Also hydrolyses several other phospho-beta-D-glucosides, but not
            their non-phosphorylated forms.
REFERENCE   1  [PMID:4624114]
  AUTHORS   Palmer RE, Anderson RL.
  TITLE     Cellobiose metabolism in Aerobacter aerogenes. 3. Cleavage of
            cellobiose monophosphate by a phospho- -glucosidase.
  JOURNAL   J. Biol. Chem. 247 (1972) 3420-3.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
ORTHOLOGY   KO: K01221  6-phospho-beta-glucosidase
            KO: K01222  6-phospho-beta-glucosidase
            KO: K01223  6-phospho-beta-glucosidase
GENES       ECO: b1734(celF) b2716(ascB) b2901(bglA) b3721(bglB)
            ECJ: JW1723(chbF) JW2686(ascB) JW2869(bglA) JW3658(glvG)
                 JW3699(bglB)
            ECE: Z2764(celF) Z4024(ascB) Z4239(bglA) Z5177
            ECS: ECs2440 ECs3572 ECs3773 ECs4622
            ECC: c1955 c2133(celF) c3482(bglA) c4643(bglB)
            ECI: UTI89_C1752 UTI89_C1927(celF) UTI89_C3078(ascB)
                 UTI89_C3287(bglA) UTI89_C4272(bglB)
            ECP: ECP_1516 ECP_1680 ECP_2677 ECP_2895 ECP_3920
            ECV: APECO1_2740(bglB) APECO1_3626(bglA) APECO1_3810(ascB)
                 APECO1_650(bglA) APECO1_803(celF)
            ECW: EcE24377A_1955(chbF) EcE24377A_3001(ascB)
                 EcE24377A_3228(bglA)
            ECX: EcHS_A1816(chbF) EcHS_A2852 EcHS_A3060(bglA)
            STY: STY1797(celF) STY3207(bglA)
            STT: t1195(celF) t2969(bglA)
            SPT: SPA1528(celF) SPA2919(bglA)
            SEC: SC1337(celF) SC2992(bglA)
            STM: STM1316(celF) STM3051(bglA)
            YPE: YPO0166 YPO1254(bglA)
            YPK: y2932(bglA) y3950(celF)
            YPM: YP_0886(bglA)
            YPA: YPA_0969 YPA_3303
            YPN: YPN_2722 YPN_3898
            YPP: YPDSF_2439
            YPS: YPTB1290(bglA) YPTB3735
            YPI: YpsIP31758_2729 YpsIP31758_3951(celF)
            YEN: YE1257(ascB) YE1417(bglA)
            SFL: SF1494(celF) SF2887(bglA)
            SFX: S1611(celF) S3086(bglA) S4038(bglB)
            SFV: SFV_1486(celF) SFV_2789(ascB) SFV_2949(bglA) SFV_3786(bglB)
            SSN: SSON_1424(celF) SSON_1595 SSON_2860(ascB) SSON_3054(bglA)
            SBO: SBO_2802(ascB) SBO_3091(bglA)
            SDY: SDY_2912(ascB) SDY_4168
            ECA: ECA0662 ECA1451 ECA1871(arbB) ECA2166(ascB) ECA4432(bglA)
            PLU: plu0582(bglB) plu2273(bglA) plu2757(celF)
            XAC: XAC3081(celF)
            VCH: VC1284 VC1558
            VCO: VC0395_A0903(celF) VC0395_A1165(bglA)
            VVU: VV1_1485 VV2_1050
            VVY: VV2898 VVA1565
            VPA: VP2634 VPA0180 VPA1695
            VFI: VF0605
            PPR: PBPRA0497
            SME: SMb21463
            RET: RHE_PE00094(agaL2)
            BSU: BG11203(bglA) BG11350(licH)
            BHA: BH0183(licH) BH0912
            BAN: BA5441(celF)
            BAR: GBAA5441(celF)
            BAA: BA_0294
            BAT: BAS5056
            BCE: BC3759 BC3760 BC5209
            BCA: BCE_5318(celF)
            BCZ: BCZK4901(celF)
            BTK: BT9727_4886(celF)
            BTL: BALH_4701(celF)
            BLI: BL01803 BL02335 BL03844(licH)
            BLD: BLi00335 BLi00749 BLi04086(licH)
            BCL: ABC0643 ABC3669(licH)
            BAY: RBAM_019360(bglA) RBAM_035760(licH)
            BPU: BPUM_0667(licH1) BPUM_2118(ydhP) BPUM_3503(licH2)
                 BPUM_3662(bglA)
            OIH: OB0811(licH) OB2273
            GKA: GK3212
            SAU: SA0256(bglA)
            SAV: SAV0266(bglA)
            SAM: MW0242(bglA)
            SAR: SAR0264(bglA)
            SAS: SAS0243
            SAC: SACOL0251(bglA)
            SAB: SAB0205(bglA)
            SAA: SAUSA300_0260(bglA)
            SAO: SAOUHSC_00236
            SSP: SSP0125
            LMO: lmo0521 lmo0536 lmo0739
            LMF: LMOf2365_0550 LMOf2365_0565 LMOf2365_2761(bglA)
            LIN: lin0526 lin0540 lin2454
            LWE: lwe0293 lwe0482 lwe0496 lwe2718(bglA)
            LLA: L121426(yrcA) L22116(bglA)
            LLC: LACR_0469 LACR_1637
            LLM: llmg_0441(bglA) llmg_0751(ascB) llmg_1455(bglA2)
            SPY: SPy_0574(bglA)
            SPZ: M5005_Spy_0476(bglA)
            SPM: spyM18_0642
            SPG: SpyM3_0405(bglA.1)
            SPS: SPs1450
            SPH: MGAS10270_Spy0470(bglA)
            SPI: MGAS10750_Spy0498(bglA)
            SPJ: MGAS2096_Spy0489(bglA)
            SPK: MGAS9429_Spy0468(bglA)
            SPF: SpyM51384(bglA)
            SPA: M6_Spy0500
            SPB: M28_Spy0457(bglA)
            SPN: SP_0303 SP_0578
            SPR: spr0276(bglA) spr0506(bglH)
            SPD: SPD_0503(bglA-2)
            SAG: SAG0791(bglA) SAG1103(ascB)
            SAN: gbs0811 gbs1170
            SAK: SAK_0916 SAK_1188
            SMU: SMU.1102(ascB) SMU.1601(bgl) SMU.985(bglA)
            STC: str1064 str1065 str1066 str1067 str1630 str1631
            STL: stu1064 stu1065 stu1066 stu1067 stu1630 stu1631
            SSA: SSA_0383(bglA) SSA_0395
            SGO: SGO_0285(pbg) SGO_0297 SGO_1582
            LPL: lp_0440(pbg1) lp_1401(pbg3) lp_2777(pbg4) lp_2778(pbg5)
                 lp_3011(pbg6) lp_3132(pbg7) lp_3512(pbg8) lp_3525(pbg9)
                 lp_3526(pbg10)
            LJO: LJ0182 LJ0188 LJ0194
            LAC: LBA0225 LBA0726 LBA0874 LBA0881 LBA0885
            LBU: LBUL_0258
            LBR: LVIS_0465
            LCA: LSEI_1104 LSEI_1778 LSEI_2191
            LGA: LGAS_0185 LGAS_0190 LGAS_0196
            PPE: PEPE_0106 PEPE_1776
            EFA: EF0271 EF0272 EF0291 EF1411
            OOE: OEOE_0340 OEOE_0341
            LME: LEUM_0927
            STH: STH2450
            CAC: CAC0743 CAC1408 CAC3426(glvG)
            CDF: CD0389(bglA) CD2882(celF) CD3079(ascB) CD3095(bglA1)
                 CD3096(ascB1) CD3115(bglA2) CD3124(ascB2) CD3130(acsB3)
                 CD3136(bglA3)
            CBO: CBO0882(ascB) CBO3360(celF)
            CBE: Cbei_4036 Cbei_4670 Cbei_4805
            TTE: TTE0337(celF)
            MFL: Mfl430
            MSM: MSMEG_0502
            SCO: SCO2661(SC6D10.04) SCO6670(SC5A7.20)
            SMA: SAV1754(bglA1) SAV5380(bglA2)
            CMI: CMM_0348(bglY)
            AAU: AAur_2890
            PAC: PPA0061
            TFU: Tfu_2768
            SEN: SACE_1589
            TMA: TM1281
STRUCTURES  PDB: 1S6Y  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.86
            ExPASy - ENZYME nomenclature database: 3.2.1.86
            ExplorEnz - The Enzyme Database: 3.2.1.86
            ERGO genome analysis and discovery system: 3.2.1.86
            BRENDA, the Enzyme Database: 3.2.1.86
            CAS: 37205-51-9
///
ENTRY       EC 3.2.1.87                 Enzyme
NAME        capsular-polysaccharide endo-1,3-alpha-galactosidase;
            polysaccharide depolymerase;
            capsular polysaccharide galactohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     Aerobacter-capsular-polysaccharide galactohydrolase
REACTION    Random hydrolysis of 1,3-alpha-D-galactosidic linkages in Aerobacter
            aerogenes capsular polysaccharide
COMMENT     Hydrolyses the galactosyl-alpha-1,3-D-galactose linkages only in the
            complex substrate, bringing about depolymerization.
REFERENCE   1  [PMID:5096084]
  AUTHORS   Yurewicz EC, Ghalambor MA, Duckworth DH, Heath EC.
  TITLE     Catalytic and molecular properties of a phage-induced capsular
            polysaccharide depolymerase.
  JOURNAL   J. Biol. Chem. 246 (1971) 5607-16.
  ORGANISM  Aerobacter aerogenes
REFERENCE   2  [PMID:4328830]
  AUTHORS   Yurewicz EC, Ghalambor MA, Heath EC.
  TITLE     The structure of Aerobacter aerogenes capsular polysaccharide.
  JOURNAL   J. Biol. Chem. 246 (1971) 5596-606.
  ORGANISM  Aerobacter aerogenes
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.87
            ExPASy - ENZYME nomenclature database: 3.2.1.87
            ExplorEnz - The Enzyme Database: 3.2.1.87
            ERGO genome analysis and discovery system: 3.2.1.87
            BRENDA, the Enzyme Database: 3.2.1.87
            CAS: 62213-16-5
///
ENTRY       EC 3.2.1.88                 Enzyme
NAME        beta-L-arabinosidase;
            vicianosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     beta-L-arabinoside arabinohydrolase
REACTION    a beta-L-arabinoside + H2O = L-arabinose + an alcohol [RN:R01760]
ALL_REAC    R01760
SUBSTRATE   beta-L-arabinoside [CPD:C02761];
            H2O [CPD:C00001]
PRODUCT     L-arabinose [CPD:C00259];
            alcohol [CPD:C00069]
REFERENCE   1  [PMID:4699248]
  AUTHORS   Dey PM.
  TITLE     Beta-L-arabinosidase from Cajanus indicus: a new enzyme.
  JOURNAL   Biochim. Biophys. Acta. 302 (1973) 393-8.
  ORGANISM  Cajanus indicus
GENES       BAY: RBAM_012120(ganA)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.88
            ExPASy - ENZYME nomenclature database: 3.2.1.88
            ExplorEnz - The Enzyme Database: 3.2.1.88
            ERGO genome analysis and discovery system: 3.2.1.88
            BRENDA, the Enzyme Database: 3.2.1.88
            CAS: 39361-63-2
///
ENTRY       EC 3.2.1.89                 Enzyme
NAME        arabinogalactan endo-1,4-beta-galactosidase;
            endo-1,4-beta-galactanase;
            galactanase;
            arabinogalactanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     arabinogalactan 4-beta-D-galactanohydrolase
REACTION    Endohydrolysis of 1,4-beta-D-galactosidic linkages in
            arabinogalactans
REFERENCE   1
  AUTHORS   Emi, S. and Yamamoto, T.
  TITLE     Purification and properties of several galactanases of Bacillus
            subtilis var. amylosacchariticus.
  JOURNAL   Agric. Biol. Chem. 36 (1972) 1945-1954.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   2  [PMID:823153]
  AUTHORS   Labavitch JM, Freeman LE, Albersheim P.
  TITLE     Structure of plant cell walls. Purification and characterization of
            a beta-1,4-galactanase which degrades a structural component of the
            primary cell walls of dicots.
  JOURNAL   J. Biol. Chem. 251 (1976) 5904-10.
  ORGANISM  Bacillus subtilis [GN:bsu]
ORTHOLOGY   KO: K01224  arabinogalactan endo-1,4-beta-galactosidase
GENES       ANI: AN5727.2
            AFM: AFUA_1G06910
            AOR: AO090001000492
            YPE: YPO0853
            YPK: y3238
            YPM: YP_3550
            YPA: YPA_0417
            YPN: YPN_3055
            YPP: YPDSF_0660
            YPS: YPTB3098
            ECA: ECA3178
            XCC: XCC1257(galA) XCC3624(galA)
            XCB: XC_0587 XC_2984
            XCV: XCV0610(ganA) XCV1360
            XAC: XAC1309(galA)
            SDE: Sde_0683 Sde_2827 Sde_3710
            BCN: Bcen_4875
            BCH: Bcen2424_3290
            BAM: Bamb_6329
            BSU: BG12440(yvfO)
            BHA: BH2023
            BLI: BL00263(yvfO)
            BLD: BLi04276(yvfO)
            BCL: ABC3517
            BPU: BPUM_3616(yvfO)
            CAC: CAC2570(ganA)
            MPE: MYPE6320
            SMA: SAV1324
            BLO: BL0257(yvfO)
            BTH: BT_4668
            TMA: TM1201
            TPT: Tpet_1555
STRUCTURES  PDB: 1FHL  1FOB  1HJQ  1HJS  1HJU  1R8L  1UR0  1UR4  2CCR  2GFT  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.89
            ExPASy - ENZYME nomenclature database: 3.2.1.89
            ExplorEnz - The Enzyme Database: 3.2.1.89
            ERGO genome analysis and discovery system: 3.2.1.89
            BRENDA, the Enzyme Database: 3.2.1.89
            CAS: 58182-40-4
///
ENTRY       EC 3.2.1.90       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
COMMENT     Deleted entry: arabinogalactan endo-1,3-beta-galactosidase. The
            enzyme was not sufficiently characterized to warrant an EC number.
            (EC 3.2.1.90 created 1976, deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.90
            ExPASy - ENZYME nomenclature database: 3.2.1.90
            ExplorEnz - The Enzyme Database: 3.2.1.90
            ERGO genome analysis and discovery system: 3.2.1.90
            BRENDA, the Enzyme Database: 3.2.1.90
///
ENTRY       EC 3.2.1.91                 Enzyme
NAME        cellulose 1,4-beta-cellobiosidase;
            exo-cellobiohydrolase;
            beta-1,4-glucan cellobiohydrolase;
            beta-1,4-glucan cellobiosylhydrolase;
            1,4-beta-glucan cellobiosidase;
            exoglucanase;
            avicelase;
            CBH 1;
            C1 cellulase;
            cellobiohydrolase I;
            cellobiohydrolase;
            exo-beta-1,4-glucan cellobiohydrolase;
            1,4-beta-D-glucan cellobiohydrolase;
            cellobiosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,4-beta-D-glucan cellobiohydrolase
REACTION    Hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose and
            cellotetraose, releasing cellobiose from the non-reducing ends of
            the chains
ALL_REAC    (other) R02886 R06200(G)
REFERENCE   1  [PMID:4738092]
  AUTHORS   Berghem LE, Pettersson LG.
  TITLE     The mechanism of enzymatic cellulose degradation. Purification of a
            cellulolytic enzyme from Trichoderma viride active on highly ordered
            cellulose.
  JOURNAL   Eur. J. Biochem. 37 (1973) 21-30.
  ORGANISM  Trichoderma viride
REFERENCE   2  [PMID:235428]
  AUTHORS   Eriksson KE, Pettersson B.
  TITLE     Extracellular enzyme system utilized by the fungus Sporotrichum
            pulverulentum (Chrysosporium lignorum) for the breakdown of
            cellulose. 3. Purification and physico-chemical characterization of
            an exo-1,4-beta-glucanase.
  JOURNAL   Eur. J. Biochem. 51 (1975) 213-8.
  ORGANISM  Sporotrichum pulverulentum
REFERENCE   3  [PMID:5076675]
  AUTHORS   Halliwell G, Griffin M, Vincent R.
  TITLE     The role of component C 1  in cellulolytic systems.
  JOURNAL   Biochem. J. 127 (1972) 43P.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01225  cellulose 1,4-beta-cellobiosidase
GENES       ANG: An01g11660(cbhB) An07g09330(cbhA)
            RSO: RS03897(RSp0583)
            ABU: Abu_1002
            BPU: BPUM_1559(celB)
            CTH: Cthe_0040 Cthe_0071 Cthe_1235
            CSC: Csac_1078 Csac_1079 Csac_2410
            MUL: MUL_0371 MUL_2210
            TFU: Tfu_1627 Tfu_2176
            KRA: Krad_3823
            STP: Strop_2951
STRUCTURES  PDB: 1AZ6  1AZH  1AZJ  1AZK  1BVW  1CB2  1CBH  1CEL  1DY4  1EGN  
                 1EXG  1EXH  1EXP  1FH7  1FH8  1FH9  1FHD  1GPI  1GZ1  1H46  
                 1HGW  1HGY  1J01  1OC5  1OC6  1OC7  1OCB  1OCJ  1OCN  1Q2B  
                 1Q2E  1Q9H  1QJW  1QK0  1QK2  1RQ5  1Z3T  1Z3V  1Z3W  2BVW  
                 2CBH  2CEL  2EXO  2HIS  2XYL  3CBH  3CEL  4CEL  5CEL  6CEL  
                 7CEL  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.91
            ExPASy - ENZYME nomenclature database: 3.2.1.91
            ExplorEnz - The Enzyme Database: 3.2.1.91
            ERGO genome analysis and discovery system: 3.2.1.91
            BRENDA, the Enzyme Database: 3.2.1.91
            CAS: 37329-65-0
///
ENTRY       EC 3.2.1.92                 Enzyme
NAME        peptidoglycan beta-N-acetylmuramidase;
            exo-beta-N-acetylmuramidase;
            exo-beta-acetylmuramidase;
            beta-2-acetamido-3-O-(D-1-carboxyethyl)-2-deoxy-D-glucoside
            acetamidodeoxyglucohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     peptidoglycan beta-N-acetylmuramoylexohydrolase
REACTION    Hydrolysis of terminal, non-reducing N-acetylmuramic residues
REFERENCE   1  [PMID:6281]
  AUTHORS   del Rio LA, Berkeley RC.
  TITLE     Exo-beta-N-acetylmuramidase--a novel hexosaminidase. Production by
            Bacillus subtilis B, purification and characterization.
  JOURNAL   Eur. J. Biochem. 65 (1976) 3-12.
  ORGANISM  Bacillus subtilis [GN:bsu]
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.92
            ExPASy - ENZYME nomenclature database: 3.2.1.92
            ExplorEnz - The Enzyme Database: 3.2.1.92
            ERGO genome analysis and discovery system: 3.2.1.92
            BRENDA, the Enzyme Database: 3.2.1.92
            CAS: 52219-03-1
///
ENTRY       EC 3.2.1.93                 Enzyme
NAME        alpha,alpha-phosphotrehalase;
            phosphotrehalase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     alpha,alpha-trehalose-6-phosphate phosphoglucohydrolase
REACTION    alpha,alpha-trehalose 6-phosphate + H2O = D-glucose + D-glucose
            6-phosphate [RN:R00837 R06113]
ALL_REAC    R00837 R06113(G)
SUBSTRATE   alpha,alpha'-trehalose 6-phosphate [CPD:C00689];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031];
            D-glucose 6-phosphate [CPD:C00092]
REFERENCE   1  [PMID:4369400]
  AUTHORS   Bhumiratana A, Anderson RL, Costilow RN.
  TITLE     Trehalose metabolism by Bacillus popilliae.
  JOURNAL   J. Bacteriol. 119 (1974) 484-93.
  ORGANISM  Bacillus popilliae
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01226  trehalose-6-phosphate hydrolase
GENES       AFM: AFUA_3G07380
            ECO: b4239(treC)
            ECJ: JW4198(treC)
            ECE: Z5849(treC)
            ECS: ECs5216
            ECC: c5338(treC)
            ECI: UTI89_C4843(treC)
            ECP: ECP_4488
            ECV: APECO1_2153(treC)
            ECW: EcE24377A_4811(treC)
            ECX: EcHS_A4493(treC)
            STY: STY4793(treC)
            STT: t4488(treC)
            SPT: SPA4254(treC)
            SEC: SC4309(treC)
            STM: STM4453(treC)
            YPE: YPO3696(treC)
            YPK: y0167(treC)
            YPM: YP_3848(treC)
            YPA: YPA_3709
            YPN: YPN_3476
            YPS: YPTB3537(treC)
            YPI: YpsIP31758_0430(treC)
            SFL: SF4251(treC)
            SFX: S4513(treC)
            SFV: SFV_4252(treC)
            SSN: SSON_4420(treC)
            SBO: SBO_4207(treC)
            SDY: SDY_4258(treC)
            ECA: ECA3014(treC)
            PLU: plu3287(treC)
            MSU: MS1236(amyA)
            VCH: VC0911
            VCO: VC0395_A0433(treC)
            VVU: VV1_0288
            VVY: VV0896
            VPA: VP0711
            PPR: PBPRA1225
            PAP: PSPA7_3104
            PFL: PFL_4933(treC)
            AHA: AHA_3172 AHA_3823(treC)
            CVI: CV_3299(treC)
            BSU: BG11010(treA)
            BHA: BH0872(treA)
            BAN: BA0632(treC)
            BAR: GBAA0632(treC)
            BAA: BA_1215
            BAT: BAS0599
            BCE: BC0632
            BCA: BCE_0700(treC)
            BCZ: BCZK0543(treC)
            BTK: BT9727_0543(treC)
            BTL: BALH_0569(treC)
            BLI: BL03069(treA)
            BLD: BLi00797(treA)
            BCL: ABC1264(treA)
            BAY: RBAM_007980(treA)
            BPU: BPUM_0729(treA)
            GKA: GK1746(treA)
            SAU: SA0433
            SAV: SAV0475
            SAM: MW0429
            SAR: SAR0474
            SAS: SAS0432
            SAC: SACOL0517
            SAB: SAB0424
            SAA: SAUSA300_0449(treC)
            SAO: SAOUHSC_00438
            SHA: SH2537
            SSP: SSP2281
            LMO: lmo0862 lmo1254
            LMF: LMOf2365_0879(treC-1) LMOf2365_1271(treC-2)
            LIN: lin0855 lin1222
            LWE: lwe1273
            SPZ: M5005_Spy_1783(dexS)
            SPH: MGAS10270_Spy1850(dexS)
            SPI: MGAS10750_Spy1875(dexS)
            SPJ: MGAS2096_Spy1816(dexS)
            SPK: MGAS9429_Spy1794(dexS)
            SPF: SpyM51742(treA)
            SPA: M6_Spy1782
            SPB: M28_Spy1767(dexS)
            SPD: SPD_1663(treC)
            SAK: SAK_0258
            SSA: SSA_1751(dexS)
            LPL: lp_0263(treA)
            LJO: LJ0758
            LAC: LBA1014(treC)
            LSA: LSA1199(treC)
            LSL: LSL_1514(treC)
            LCA: LSEI_0630
            LGA: LGAS_0533
            PPE: PEPE_1806
            CPE: CPE0562
            CPF: CPF_0542(treC)
            CDF: CD3091(treA)
            CBO: CBO1988(treA)
            CBA: CLB_1928(treC)
            CBH: CLC_1934(treC)
            CBF: CLI_2054(treC)
            MMO: MMOB0630(treC)
            MFL: Mfl499
            CHU: CHU_2602(treC)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.93
            ExPASy - ENZYME nomenclature database: 3.2.1.93
            ExplorEnz - The Enzyme Database: 3.2.1.93
            ERGO genome analysis and discovery system: 3.2.1.93
            BRENDA, the Enzyme Database: 3.2.1.93
            CAS: 54576-93-1
///
ENTRY       EC 3.2.1.94                 Enzyme
NAME        glucan 1,6-alpha-isomaltosidase;
            exo-isomaltohydrolase;
            isomalto-dextranase;
            isomaltodextranase;
            G2-dextranase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,6-alpha-D-glucan isomaltohydrolase
REACTION    Hydrolysis of 1,6-alpha-D-glucosidic linkages in polysaccharides, to
            remove successive isomaltose units from the non-reducing ends of the
            chains
COMMENT     Optimum activity is on those 1,6-alpha-D-glucans containing 6, 7 and
            8 glucose units; those containing 3, 4 and 5 glucose units are
            hydrolysed at slower rates.
REFERENCE   1  [PMID:4826536]
  AUTHORS   Sawai T, Toriyama K, Yano K.
  TITLE     A bacterial dextranase releasing only isomaltose from dextrans.
  JOURNAL   J. Biochem. (Tokyo). 75 (1974) 105-12.
  ORGANISM  Achromobacter sp.
REFERENCE   2
  AUTHORS   Sawai, T. and Niwa, Y.
  TITLE     Transisomaltosylation activity of a bacterial isomaltodextranase.
  JOURNAL   Agric. Biol. Chem. 39 (1975) 1077-1083.
GENES       FJO: Fjoh_4436
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.94
            ExPASy - ENZYME nomenclature database: 3.2.1.94
            ExplorEnz - The Enzyme Database: 3.2.1.94
            ERGO genome analysis and discovery system: 3.2.1.94
            BRENDA, the Enzyme Database: 3.2.1.94
            CAS: 56467-68-6
///
ENTRY       EC 3.2.1.95                 Enzyme
NAME        dextran 1,6-alpha-isomaltotriosidase;
            exo-isomaltotriohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,6-alpha-D-glucan isomaltotriohydrolase
REACTION    Hydrolysis of 1,6-alpha-D-glucosidic linkages in dextrans, to remove
            successive isomaltotriose units from the non-reducing ends of the
            chains
REFERENCE   1  [PMID:4210084]
  AUTHORS   Sugiura M, Ito A, Yamaguchi T.
  TITLE     Studies on dextranase. II. New exo-dextranase from Brevibacterium
            fuscum var. Dextranlyticum.
  JOURNAL   Biochim. Biophys. Acta. 350 (1974) 61-70.
  ORGANISM  Brevibacterium fuscum
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.95
            ExPASy - ENZYME nomenclature database: 3.2.1.95
            ExplorEnz - The Enzyme Database: 3.2.1.95
            ERGO genome analysis and discovery system: 3.2.1.95
            BRENDA, the Enzyme Database: 3.2.1.95
            CAS: 72561-11-6
///
ENTRY       EC 3.2.1.96                 Enzyme
NAME        mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase;
            N,N'-diacetylchitobiosyl beta-N-acetylglucosaminidase;
            endo-beta-N-acetylglucosaminidase;
            mannosyl-glycoprotein endo-beta-N-acetylglucosamidase;
            di-N-acetylchitobiosyl beta-N-acetylglucosaminidase;
            endo-beta-acetylglucosaminidase;
            endo-beta-(1->4)-N-acetylglucosaminidase;
            mannosyl-glycoprotein 1,4-N-acetamidodeoxy-beta-D-glycohydrolase;
            endoglycosidase S;
            endo-N-acetyl-beta-D-glucosaminidase;
            endo-N-acetyl-beta-glucosaminidase;
            endo-beta-N-acetylglucosaminidase D;
            endo-beta-N-acetylglucosaminidase F;
            endo-beta-N-acetylglucosaminidase H;
            endo-beta-N-acetylglucosaminidase L;
            glycopeptide-D-mannosyl-4-N-(N-acetyl-D-glucosaminyl)2-asparagine
            1,4-N-acetyl-beta-glucosaminohydrolase;
            endoglycosidase H
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine
            1,4-N-acetyl-beta-glucosaminohydrolase
REACTION    Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose
            glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-
            structure. One N-acetyl-D-glucosamine residue remains attached to
            the protein; the rest of the oligosaccharide is released intact
COMMENT     A group of related enzymes.
REFERENCE   1
  AUTHORS   Chien, S., Weinburg, R., Li, S. and Li, Y.
  TITLE     Endo-beta-N-acetylglucosaminidase from fig latex.
  JOURNAL   Biochem. Biophys. Res. Commun. 76 (1977) 317-323.
  ORGANISM  fig
REFERENCE   2  [PMID:4152561]
  AUTHORS   Koide N, Muramatsu T.
  TITLE     Endo-beta-N-acetylglucosaminidase acting on carbohydrate moieties of
            glycoproteins. Purification and properties of the enzyme from
            Diplococcus pneumoniae.
  JOURNAL   J. Biol. Chem. 249 (1974) 4897-904.
  ORGANISM  Diplococcus pneumoniae
REFERENCE   3  [PMID:486141]
  AUTHORS   Pierce RJ, Spik G, Montreuil J.
  TITLE     Cytosolic location of an endo-N-acetyl-beta-D-glucosaminidase
            activity in rat liver and kidney.
  JOURNAL   Biochem. J. 180 (1979) 673-76.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:7378051]
  AUTHORS   Pierce RJ, Spik G, Montreuil J.
  TITLE     Demonstration and cytosolic location of an
            endo-N-acetyl-beta-D-glucosaminidase activity towards an
            asialo-N-acetyl-lactosaminic-type substrate in rat liver.
  JOURNAL   Biochem. J. 185 (1980) 261-4.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:389]
  AUTHORS   Tai T, Yamashita K, Ogata-Arakawa M, Koide N, Muramatsu T, Iwashita
            S, Inoue Y, Kobata A.
  TITLE     Structural studies of two ovalbumin glycopeptides in relation to the
            endo-beta-N-acetylglucosaminidase specificity.
  JOURNAL   J. Biol. Chem. 250 (1975) 8569-75.
  ORGANISM  Diplococcus pneumoniae, Streptomyces griseus
REFERENCE   6  [PMID:4204553]
  AUTHORS   Tarentino AL, Plummer TH Jr, Maley F.
  TITLE     The release of intact oligosaccharides from specific glycoproteins
            by endo-beta-N-acetylglucosaminidase H.
  JOURNAL   J. Biol. Chem. 249 (1974) 818-24.
  ORGANISM  Streptomyces griseus
PATHWAY     PATH: map00511  N-Glycan degradation
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01227  mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
GENES       HSA: 64772(FLJ21865)
            PIC: PICST_32069(HEX1)
            TBR: Tb09.160.2050
            BCL: ABC3097
            SAU: SA0905(atl)
            SAV: SAV1052
            SAM: MW0936(atl)
            SAR: SAR1026(atl)
            SAS: SAS0988
            SAC: SACOL1062(atl)
            SAB: SAB0919c(atl)
            SAA: SAUSA300_0955(atl)
            SAO: SAOUHSC_00994
            SAJ: SaurJH9_0363 SaurJH9_0909 SaurJH9_1112 SaurJH9_1827
                 SaurJH9_2330
            SAH: SaurJH1_0372 SaurJH1_0927 SaurJH1_1135 SaurJH1_1862
                 SaurJH1_2373
            SEP: SE0750
            SER: SERP0636(atlE)
            SHA: SH1911(atl)
            SSP: SSP1741
            LLM: llmg_0280(acmA) llmg_1087(acmC) llmg_2165(acmB)
            SPZ: M5005_Spy_1540(endoS)
            SPH: MGAS10270_Spy1607(endoS)
            SPI: MGAS10750_Spy1599(endoS)
            SPJ: MGAS2096_Spy1565(endoS)
            SPK: MGAS9429_Spy1544(endoS)
            SPF: SpyM50309
            SPA: M6_Spy1530
            SPB: M28_Spy1527(endoS)
            SPN: SP_0965
            SPR: spr0867(lytB)
            SPD: SPD_0853(lytB) SPD_1403(lytC)
            LPL: lp_0182
            LBR: LVIS_1883
            OOE: OEOE_0144
            CNO: NT01CX_0726
            CBA: CLB_3142
            CBH: CLC_3015
            CBF: CLI_3171
            PAC: PPA0990
            CHU: CHU_1472(flgJ)
STRUCTURES  PDB: 1C3F  1C8X  1C8Y  1C90  1C91  1C92  1C93  1EDT  1EOK  1EOM  
                 2EBN  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.96
            ExPASy - ENZYME nomenclature database: 3.2.1.96
            ExplorEnz - The Enzyme Database: 3.2.1.96
            ERGO genome analysis and discovery system: 3.2.1.96
            BRENDA, the Enzyme Database: 3.2.1.96
            CAS: 37278-88-9
///
ENTRY       EC 3.2.1.97                 Enzyme
NAME        glycopeptide alpha-N-acetylgalactosaminidase;
            endo-alpha-N-acetylgalactosaminidase;
            endo-alpha-acetylgalactosaminidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     D-galactosyl-N-acetyl-alpha-D-galactosamine
            D-galactosyl-N-acetyl-galactosaminohydrolase
REACTION    Hydrolysis of terminal
            D-galactosyl-N-acetyl-alpha-D-galactosaminidic residues from a
            variety of glycopeptides and glycoproteins
COMMENT     The aglycone may be serine or threonine.
REFERENCE   1  [PMID:7253]
  AUTHORS   Bhavanandan VP, Umemoto J, Davidson EA.
  TITLE     Characterization of an endo-alpha-N-acetyl galactosaminidase from
            Diplococcus pneumoniae.
  JOURNAL   Biochem. Biophys. Res. Commun. 70 (1976) 738-45.
  ORGANISM  Diplococcus pneumoniae
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.97
            ExPASy - ENZYME nomenclature database: 3.2.1.97
            ExplorEnz - The Enzyme Database: 3.2.1.97
            ERGO genome analysis and discovery system: 3.2.1.97
            BRENDA, the Enzyme Database: 3.2.1.97
            CAS: 59793-96-3
///
ENTRY       EC 3.2.1.98                 Enzyme
NAME        glucan 1,4-alpha-maltohexaosidase;
            exo-maltohexaohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,4-alpha-D-glucan maltohexaohydrolase
REACTION    Hydrolysis of 1,4-alpha-D-glucosidic linkages in amylaceous
            polysaccharides, to remove successive maltohexaose residues from the
            non-reducing chain ends
COMMENT     cf. EC 3.2.1.3 glucan 1,4-alpha-glucosidase, which removes
            successive glucose residues; EC 3.2.1.2 beta-amylase, which removes
            successive maltose residues; EC 3.2.1.116 glucan
            1,4-alpha-maltotriohydrolase, which removes successive maltotriose
            units and EC 3.2.1.60 glucan 1,4-alpha-maltotetraohydrolase, which
            removes successive maltotetraose residues. The products have the
            alpha-configuration.
REFERENCE   1  [PMID:1094]
  AUTHORS   Kainuma K, Wako K, Kobayashi S, Nogami A, Suzuki S.
  TITLE     Purification and some properties of a novel maltohexaose-producing
            exo-amylase from Aerobacter aerogenes.
  JOURNAL   Biochim. Biophys. Acta. 410 (1975) 333-46.
  ORGANISM  Aerobacter aerogenes
REFERENCE   2
  AUTHORS   Nakakuki, T., Azuma, K. and Kainuma, K.
  TITLE     Action patterns of various exo-amylases and the anomeric
            configurations of their products.
  JOURNAL   Carbohydr. Res. 128 (1984) 297-310.
  ORGANISM  Aerobacter aerogenes
GENES       ENT: Ent638_2526
STRUCTURES  PDB: 1WP6  1WPC  2D3L  2D3N  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.98
            ExPASy - ENZYME nomenclature database: 3.2.1.98
            ExplorEnz - The Enzyme Database: 3.2.1.98
            ERGO genome analysis and discovery system: 3.2.1.98
            BRENDA, the Enzyme Database: 3.2.1.98
            CAS: 72561-12-7
///
ENTRY       EC 3.2.1.99                 Enzyme
NAME        arabinan endo-1,5-alpha-L-arabinosidase;
            endo-1,5-alpha-L-arabinanase;
            endo-alpha-1,5-arabanase;
            endo-arabanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,5-alpha-L-arabinan 1,5-alpha-L-arabinanohydrolase
REACTION    Endohydrolysis of 1,5-alpha-arabinofuranosidic linkages in
            1,5-arabinans
COMMENT     Also acts on beet arabinan, but more slowly.
REFERENCE   1  [PMID:1096]
  AUTHORS   Kaji A, Saheki T.
  TITLE     Endo-arabinanase from Bacillus subtilis F-11.
  JOURNAL   Biochim. Biophys. Acta. 410 (1975) 354-60.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   2
  AUTHORS   Weinstein, L. and Albersheim, P.
  TITLE     Structure of plant cell walls. IX. Purification and partial
            characterization of a wall-degrading endo-arabinase and an
            arabinosidase from Bacillus subtilis.
  JOURNAL   Plant Physiol. 63 (1979) 425-432.
  ORGANISM  Bacillus subtilis [GN:bsu]
GENES       ANG: An09g01190(abnA)
            SPC: Sputcn32_2051
            SHM: Shewmr7_1980
            SHW: Sputw3181_1961
            RHA: RHA1_ro05391
            KRA: Krad_0078
            GFO: GFO_0691(abnA) GFO_0694(abnA)
STRUCTURES  PDB: 1GYD  1GYE  1GYH  1UV4  1WL7  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.99
            ExPASy - ENZYME nomenclature database: 3.2.1.99
            ExplorEnz - The Enzyme Database: 3.2.1.99
            ERGO genome analysis and discovery system: 3.2.1.99
            BRENDA, the Enzyme Database: 3.2.1.99
            CAS: 75432-96-1
///
ENTRY       EC 3.2.1.100                Enzyme
NAME        mannan 1,4-mannobiosidase;
            1,4-beta-D-mannan mannobiohydrolase;
            exo-beta-mannanase;
            exo-1,4-beta-mannobiohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,4-beta-D-mannan mannobiohydrolase
REACTION    Hydrolysis of 1,4-beta-D-mannosidic linkages in 1,4-beta-D-mannans,
            to remove successive mannobiose residues from the non-reducing chain
            ends
REFERENCE   1  [PMID:7096283]
  AUTHORS   Araki T, Kitamikado M.
  TITLE     Purification and characterization of a novel exo-beta-mannanase from
            Aeromonas sp. F-25.
  JOURNAL   J. Biochem. (Tokyo). 91 (1982) 1181-6.
  ORGANISM  Aeromonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.100
            ExPASy - ENZYME nomenclature database: 3.2.1.100
            ExplorEnz - The Enzyme Database: 3.2.1.100
            ERGO genome analysis and discovery system: 3.2.1.100
            BRENDA, the Enzyme Database: 3.2.1.100
            CAS: 81811-49-6
///
ENTRY       EC 3.2.1.101                Enzyme
NAME        mannan endo-1,6-alpha-mannosidase;
            exo-1,6-beta-mannanase;
            endo-alpha-1->6-D-mannanase;
            endo-1,6-beta-mannanase;
            mannan endo-1,6-beta-mannosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,6-alpha-D-mannan mannanohydrolase
REACTION    Random hydrolysis of 1,6-alpha-D-mannosidic linkages in unbranched
            1,6-mannans
REFERENCE   1  [PMID:811665]
  AUTHORS   Nakajima T, Maitra SK, Ballou CE.
  TITLE     An endo-alpha1 leads to 6-D-mannanase from a soil bacterium.
            Purification, properties, and mode of action.
  JOURNAL   J. Biol. Chem. 251 (1976) 174-81.
  ORGANISM  Arthrobacter sp.
REFERENCE   2  [PMID:10637300]
  AUTHORS   Brigance WT, Barlowe C, Graham TR.
  TITLE     Organization of the yeast Golgi complex into at least four
            functionally distinct compartments.
  JOURNAL   Mol. Biol. Cell. 11 (2000) 171-82.
  ORGANISM  Bacillus circulans
REFERENCE   3  [PMID:4612041]
  AUTHORS   Nakajima T, Ballou CE.
  TITLE     Structure of the linkage region between the polysaccharide and
            protein parts of Saccharomyces cerevisiae mannan.
  JOURNAL   J. Biol. Chem. 249 (1974) 7685-94.
  ORGANISM  Arthrobacter sp.
ORTHOLOGY   KO: K08257  mannan endo-1,6-alpha-mannosidase
GENES       SCE: YKL046C(DCW1) YMR238W(DFG5)
            AGO: AGOS_ABR060W AGOS_AFR530W
            PIC: PICST_82260(DCW1)
            CAL: CaO19_2075(CaO19.2075)
            CGR: CAGL0L01727g CAGL0M05049g
            SPO: SPBC1198.06c SPCC970.02
            ANI: AN2825.2
            AFM: AFUA_4G00620
            AOR: AO090003001408
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.101
            ExPASy - ENZYME nomenclature database: 3.2.1.101
            ExplorEnz - The Enzyme Database: 3.2.1.101
            ERGO genome analysis and discovery system: 3.2.1.101
            BRENDA, the Enzyme Database: 3.2.1.101
            CAS: 98148-86-8
///
ENTRY       EC 3.2.1.102                Enzyme
NAME        blood-group-substance endo-1,4-beta-galactosidase;
            endo-beta-galactosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     blood-group-substance 1,4-beta-D-galactanohydrolase
REACTION    Endohydrolysis of 1,4-beta-D-galactosidic linkages in blood group A
            and B substances
COMMENT     Hydrolyses the 1,4-beta-D-galactosyl linkages adjacent to a
            1,3-alpha-D-galactosyl or N-acetylgalactosaminyl residues and a
            1,2-alpha-D-fucosyl residue.
REFERENCE   1  [PMID:135762]
  AUTHORS   Fukuda MN, Matsumura G.
  TITLE     Endo-beta-galactosidase of Escherichia freundii. Purification and
            endoglycosidic action on keratan sulfates, oligosaccharides, and
            blood group active glycoprotein.
  JOURNAL   J. Biol. Chem. 251 (1976) 6218-25.
  ORGANISM  Escherichia freundii
REFERENCE   2  [PMID:234443]
  AUTHORS   Nakazawa K, Suzuki S.
  TITLE     Purification of Keratan Sulfate-endogalactosidase and its action on
            keratan sulfates of different origin.
  JOURNAL   J. Biol. Chem. 250 (1975) 912-7.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:6459]
  AUTHORS   Takasaki S, Kobata A.
  TITLE     Purification and characterization of an endo-beta-galactosidase
            produced by Diplococcus pneumoniae.
  JOURNAL   J. Biol. Chem. 251 (1976) 3603-9.
  ORGANISM  Diplococcus pneumoniae
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.102
            ExPASy - ENZYME nomenclature database: 3.2.1.102
            ExplorEnz - The Enzyme Database: 3.2.1.102
            ERGO genome analysis and discovery system: 3.2.1.102
            BRENDA, the Enzyme Database: 3.2.1.102
            CAS: 52720-51-1
///
ENTRY       EC 3.2.1.103                Enzyme
NAME        keratan-sulfate endo-1,4-beta-galactosidase;
            endo-beta-galactosidase;
            keratan sulfate endogalactosidase;
            keratanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     keratan-sulfate 1,4-beta-D-galactanohydrolase
REACTION    Endohydrolysis of 1,4-beta-D-galactosidic linkages in keratan
            sulfate [RN:R07805]
ALL_REAC    R07805(G)
COMMENT     Hydrolyses the 1,4-beta-D-galactosyl linkages adjacent to
            1,3-alpha-D-N-acetyl-glucosaminyl residues. Also acts on some
            non-sulfated oligosaccharides, but only acts on blood group
            substances when the 1,2-linked fucosyl residues have been removed
            (cf. EC 3.2.1.102 blood-group-substance
            endo-1,4-beta-galactosidase).
REFERENCE   1  [PMID:135762]
  AUTHORS   Fukuda MN, Matsumura G.
  TITLE     Endo-beta-galactosidase of Escherichia freundii. Purification and
            endoglycosidic action on keratan sulfates, oligosaccharides, and
            blood group active glycoprotein.
  JOURNAL   J. Biol. Chem. 251 (1976) 6218-25.
  ORGANISM  Escherichia freundii
PATHWAY     PATH: map00531  Glycosaminoglycan degradation
            PATH: map01032  Glycan structures - degradation
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.103
            ExPASy - ENZYME nomenclature database: 3.2.1.103
            ExplorEnz - The Enzyme Database: 3.2.1.103
            ERGO genome analysis and discovery system: 3.2.1.103
            BRENDA, the Enzyme Database: 3.2.1.103
            CAS: 55072-01-0
///
ENTRY       EC 3.2.1.104                Enzyme
NAME        steryl-beta-glucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     cholesteryl-beta-D-glucoside glucohydrolase
REACTION    cholesteryl-beta-D-glucoside + H2O = D-glucose + cholesterol
            [RN:R01460]
ALL_REAC    R01460
SUBSTRATE   cholesteryl-beta-D-glucoside [CPD:C03855];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031];
            cholesterol [CPD:C00187]
COMMENT     Acts on glucosides of cholesterol and sitosterol, but not on some
            related sterols such as coprostanol.
REFERENCE   1
  AUTHORS   Kalinowska, M. and Wojciechowski, Z.A.
  TITLE     Purification and some properties of steryl beta-D-glucoside
            hydrolase from Sinapis alba seedlings.
  JOURNAL   Phytochemistry 17 (1978) 1533-1537.
  ORGANISM  Sinapis alba
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.104
            ExPASy - ENZYME nomenclature database: 3.2.1.104
            ExplorEnz - The Enzyme Database: 3.2.1.104
            ERGO genome analysis and discovery system: 3.2.1.104
            BRENDA, the Enzyme Database: 3.2.1.104
            CAS: 69494-88-8
///
ENTRY       EC 3.2.1.105                Enzyme
NAME        3alpha(S)-strictosidine beta-glucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     strictosidine beta-D-glucohydrolase
REACTION    strictosidine + H2O = D-glucose + strictosidine aglycone [RN:R03820]
ALL_REAC    R03820
SUBSTRATE   strictosidine [CPD:C03470];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031];
            strictosidine aglycone [CPD:C03309]
COMMENT     Does not act on a number of closely related glycosides.
            Strictosidine is a precursor of indole alkaloids.
REFERENCE   1  [PMID:6768587]
  AUTHORS   Hemscheidt T, Zenk MH.
  TITLE     Glucosidases involved in indole alkaloid biosynthesis of
            Catharanthus cell cultures.
  JOURNAL   FEBS. Lett. 110 (1980) 187-91.
  ORGANISM  Catharunthus roseus
REFERENCE   2  [PMID:15680242]
  AUTHORS   Barleben L, Ma X, Koepke J, Peng G, Michel H, Stockigt J.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            analysis of strictosidine glucosidase, an enzyme initiating
            biosynthetic pathways to a unique diversity of indole alkaloid
            skeletons.
  JOURNAL   Biochim. Biophys. Acta. 1747 (2005) 89-92.
  ORGANISM  Rauvolfia serpentina
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.105
            ExPASy - ENZYME nomenclature database: 3.2.1.105
            ExplorEnz - The Enzyme Database: 3.2.1.105
            ERGO genome analysis and discovery system: 3.2.1.105
            BRENDA, the Enzyme Database: 3.2.1.105
            CAS: 73379-57-4
///
ENTRY       EC 3.2.1.106                Enzyme
NAME        mannosyl-oligosaccharide glucosidase;
            Glc3Man9NAc2 oligosaccharide glucosidase;
            trimming glucosidase I
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     mannosyl-oligosaccharide glucohydrolase
REACTION    Exohydrolysis of the non-reducing terminal glucose residues in the
            mannosyl-oligosaccharide Glc3Man9GlcNAc2
ALL_REAC    (other) R05979(G)
COMMENT     Also acts, more slowly, on the corresponding glycolipids and
            glycopeptides. Involved in the formation of high-mannose and complex
            glycoproteins.
REFERENCE   1  [PMID:7358674]
  AUTHORS   Elting JJ, Chen WW, Lennarz WJ.
  TITLE     Characterization of a glucosidase involved in an initial step in the
            processing of oligosaccharide chains.
  JOURNAL   J. Biol. Chem. 255 (1980) 2325-31.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:479161]
  AUTHORS   Grinna LS, Robbins PW.
  TITLE     Glycoprotein biosynthesis. Rat liver microsomal glucosidases which
            process oligosaccharides.
  JOURNAL   J. Biol. Chem. 254 (1979) 8814-8.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:7014569]
  AUTHORS   Kilker RD Jr, Saunier B, Tkacz JS, Herscovics A.
  TITLE     Partial purification from Saccharomyces cerevisiae of a soluble
            glucosidase which removes the terminal glucose from the
            oligosaccharide Glc3Man9GlcNAc2.
  JOURNAL   J. Biol. Chem. 256 (1981) 5299-603.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4  [PMID:7358666]
  AUTHORS   Grinna LS, Robbins PW.
  TITLE     Substrate specificities of rat liver microsomal glucosidases which
            process glycoproteins.
  JOURNAL   J. Biol. Chem. 255 (1980) 2255-8.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:7356331]
  AUTHORS   Michael JM, Kornfeld S.
  TITLE     Partial purification and characterization of the glucosidases
            involved in the processing of asparagine-linked oligosaccharides.
  JOURNAL   Arch. Biochem. Biophys. 199 (1980) 249-58.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K01228  mannosyl-oligosaccharide glucosidase
GENES       HSA: 7841(GCS1)
            MMU: 57377(Gcs1)
            RNO: 78947(Gcs1)
            CFA: 483104(LOC483104)
            DRE: 567913(zgc:158312)
            DME: Dmel_CG1597
            CEL: F13H10.4
            ATH: AT1G24320
            OSA: 4327748
            CME: CMF070C
            SCE: YGL027C(CWH41)
            AGO: AGOS_AFR483C
            PIC: PICST_39865(CWH41)
            CGR: CAGL0A01452g
            SPO: SPAC6G10.09
            ANI: AN6606.2
            AFM: AFUA_6G04210
            AOR: AO090701000141
            DDI: DDBDRAFT_0206405
            TET: TTHERM_00636930
            TCR: 510895.9 511015.10 511805.10
            LMA: LmjF28.2200
            ECI: UTI89_C3520(ygjK)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.106
            ExPASy - ENZYME nomenclature database: 3.2.1.106
            ExplorEnz - The Enzyme Database: 3.2.1.106
            ERGO genome analysis and discovery system: 3.2.1.106
            BRENDA, the Enzyme Database: 3.2.1.106
            CAS: 78413-07-7
///
ENTRY       EC 3.2.1.107                Enzyme
NAME        protein-glucosylgalactosylhydroxylysine glucosidase;
            2-O-alpha-D-glucopyranosyl-5-O-alpha-D-galactopyranosylhydroxy-L-
            lysine glucohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     protein-alpha-D-glucosyl-1,2-beta-D-galactosyl-L-hydroxylysine
            glucohydrolase
REACTION    protein alpha-D-glucosyl-1,2-beta-D-galactosyl-L-hydroxylysine + H2O
            = D-glucose + protein beta-D-galactosyl-L-hydroxylysine [RN:R04503]
ALL_REAC    R04503
SUBSTRATE   protein alpha-D-glucosyl-1,2-beta-D-galactosyl-L-hydroxylysine
            [CPD:C04817];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031];
            protein beta-D-galactosyl-L-hydroxylysine [CPD:C04542]
COMMENT     Requires free, positively charged epsilon-amino group of
            hydroxylysine.
REFERENCE   1  [PMID:385589]
  AUTHORS   Hamazaki H, Hotta K.
  TITLE     Purification and characterization of an alpha-glucosidase specific
            for hydroxylysine-linked disaccharide of collagen.
  JOURNAL   J. Biol. Chem. 254 (1979) 9682-7.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:7460918]
  AUTHORS   Hamazaki H, Hotta K.
  TITLE     Enzymatic hydrolysis of disaccharide unit of collagen. Isolation of
            2-O-alpha-D-glucopyranosyl-O-beta-D-galactopyranosyl-hydroxylysine
            glucohydrolase from rat spleens.
  JOURNAL   Eur. J. Biochem. 111 (1980) 587-91.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:385599]
  AUTHORS   Sternberg M, Spiro RG.
  TITLE     Studies on the catabolism of the hydroxylysine-linked disaccharide
            units of basement membranes and collagens. Isolation and
            characterization of a rat kidney alpha-glucosidase of high
            specificity.
  JOURNAL   J. Biol. Chem. 254 (1979) 10329-36.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.107
            ExPASy - ENZYME nomenclature database: 3.2.1.107
            ExplorEnz - The Enzyme Database: 3.2.1.107
            ERGO genome analysis and discovery system: 3.2.1.107
            BRENDA, the Enzyme Database: 3.2.1.107
            CAS: 72829-45-9
///
ENTRY       EC 3.2.1.108                Enzyme
NAME        lactase;
            lactase-phlorizin hydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     lactose galactohydrolase
REACTION    lactose + H2O = D-galactose + D-glucose [RN:R01100 R06114]
ALL_REAC    R01100 R06114(G) > R01678 R06098(G)
SUBSTRATE   lactose [CPD:C00243];
            H2O [CPD:C00001]
PRODUCT     D-galactose [CPD:C00124];
            D-glucose [CPD:C00031]
COMMENT     The enzyme from intestinal mucosa is isolated as a complex that also
            catalyses the reaction of EC 3.2.1.62 glycosylceramidase. cf. EC
            3.2.1.33 amylo-alpha-1,6-glucosidase.
REFERENCE   1  [PMID:5082068]
  AUTHORS   Lorenz-Meyer H, Blum AL, Haemmerli HP, Semenza G.
  TITLE     A second enzyme defect in acquired lactase deficiency: lack of
            small-intestinal phlorizin-hydrolase.
  JOURNAL   Eur. J. Clin. Invest. 2 (1972) 326-31.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:810166]
  AUTHORS   Ramaswamy S, Radhakrishnan AN.
  TITLE     Lactase-phlorizin hydrolase complex from monkey small intestine.
            Purification, properties and evidence for two catalytic sites.
  JOURNAL   Biochim. Biophys. Acta. 403 (1975) 446-55.
  ORGANISM  monkey
REFERENCE   3  [PMID:5010299]
  AUTHORS   Schlegel-Haueter S, Hore P, Kerry KR, Semenza G.
  TITLE     The preparation of lactase and glucoamylase of rat small intestine.
  JOURNAL   Biochim. Biophys. Acta. 258 (1972) 506-19.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:6814489]
  AUTHORS   Skovbjerg H, Noren O, Sjostrom H, Danielsen EM, Enevoldsen BS.
  TITLE     Further characterization of intestinal lactase/phlorizin hydrolase.
  JOURNAL   Biochim. Biophys. Acta. 707 (1982) 89-97.
  ORGANISM  pig [GN:ssc]
REFERENCE   5  [PMID:6786877]
  AUTHORS   Skovbjerg H, Sjostrom H, Noren O.
  TITLE     Purification and characterisation of amphiphilic lactase/phlorizin
            hydrolase from human small intestine.
  JOURNAL   Eur. J. Biochem. 114 (1981) 653-61.
  ORGANISM  human [GN:hsa]
REFERENCE   6  [PMID:5822067]
  AUTHORS   Asp NG, Dahlqvist A, Koldovsky O.
  TITLE     Human small-intestinal beta-galactosidases. Separation and
            characterization of one lactase and one hetero beta-galactosidase.
  JOURNAL   Biochem. J. 114 (1969) 351-9.
PATHWAY     PATH: map00052  Galactose metabolism
ORTHOLOGY   KO: K01229  lactase
GENES       HSA: 3938(LCT)
            MMU: 226413(Lct)
            RNO: 116569(Lct)
            CFA: 483898(LCT)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.108
            ExPASy - ENZYME nomenclature database: 3.2.1.108
            ExplorEnz - The Enzyme Database: 3.2.1.108
            ERGO genome analysis and discovery system: 3.2.1.108
            BRENDA, the Enzyme Database: 3.2.1.108
            CAS: 9031-11-2
///
ENTRY       EC 3.2.1.109                Enzyme
NAME        endogalactosaminidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     galactosaminoglycan glycanohydrolase
REACTION    Endohydrolysis of 1,4-alpha-D-galactosaminidic linkages in
            poly(D-galactosamine)
REFERENCE   1  [PMID:3271]
  AUTHORS   Reissig JL, Lai WH, Glasgow JE.
  TITLE     An endogalactosaminidase from Streptomyces griseus.
  JOURNAL   Can. J. Biochem. 53 (1975) 1237-49.
  ORGANISM  Streptomyces griseus
REFERENCE   2
  AUTHORS   Tamura, J., Takagi, H. and Kadowaki, K.
  TITLE     Purification and some properties of the endo
            alpha-1,4-polygalactosaminidase from Pseudomonas sp.
  JOURNAL   Agric. Biol. Chem. 52 (1988) 2475-2484.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.109
            ExPASy - ENZYME nomenclature database: 3.2.1.109
            ExplorEnz - The Enzyme Database: 3.2.1.109
            ERGO genome analysis and discovery system: 3.2.1.109
            BRENDA, the Enzyme Database: 3.2.1.109
            CAS: 59088-26-5
///
ENTRY       EC 3.2.1.110                Enzyme
NAME        mucinaminylserine mucinaminidase;
            endo-alpha-N-acetylgalactosaminidase;
            endo-alpha-N-acetyl-D-galactosaminidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     D-galactosyl-3-(N-acetyl-beta-D-galactosaminyl)-L-serine
            mucinaminohydrolase
REACTION    D-galactosyl-3-(N-acetyl-beta-D-galactosaminyl)-L-serine + H2O =
            D-galactosyl-3-N-acetyl-beta-D-galactosamine + L-serine [RN:R04527
            R06140]
ALL_REAC    R04527 R06140(G)
SUBSTRATE   D-galactosyl-3-(N-acetyl-beta-D-galactosaminyl)-L-serine
            [CPD:C04776];
            H2O [CPD:C00001]
PRODUCT     D-galactosyl-3-N-acetyl-beta-D-galactosamine [CPD:C04610];
            L-serine [CPD:C00065]
REFERENCE   1  [PMID:7253]
  AUTHORS   Bhavanandan VP, Umemoto J, Davidson EA.
  TITLE     Characterization of an endo-alpha-N-acetyl galactosaminidase from
            Diplococcus pneumoniae.
  JOURNAL   Biochem. Biophys. Res. Commun. 70 (1976) 738-45.
  ORGANISM  Diplococcus pneumoniae
REFERENCE   2  [PMID:9374]
  AUTHORS   Endo Y, Kobata A.
  TITLE     Partial purification and characterization of an
            endo-alpha-N-acetylgalactosaminidase from the culture of medium of
            Diplococcus pneumoniae.
  JOURNAL   J. Biochem. (Tokyo). 80 (1976) 1-8.
  ORGANISM  Diplococcus pneumoniae
REFERENCE   3  [PMID:21877]
  AUTHORS   Umemoto J, Bhavanandan VP, Davidson EA.
  TITLE     Purification and properties of an
            endo-alpha-N-acetyl-D-galactosaminidase from Diplococcus pneumoniae.
  JOURNAL   J. Biol. Chem. 252 (1977) 8609-14.
  ORGANISM  Diplococcus pneumoniae
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.110
            ExPASy - ENZYME nomenclature database: 3.2.1.110
            ExplorEnz - The Enzyme Database: 3.2.1.110
            ERGO genome analysis and discovery system: 3.2.1.110
            BRENDA, the Enzyme Database: 3.2.1.110
            CAS: 59793-96-3
///
ENTRY       EC 3.2.1.111                Enzyme
NAME        1,3-alpha-L-fucosidase;
            almond emulsin fucosidase I
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     3-alpha-L-fucosyl-N-acetylglucosaminyl-glycoprotein fucohydrolase
REACTION    Hydrolysis of 1,3-linkages between alpha-L-fucose and
            N-acetylglucosamine residues in glycoproteins
COMMENT     Not identical with EC 3.2.1.63 1,2-alpha-L-fucosidase.
REFERENCE   1  [PMID:7085666]
  AUTHORS   Imber MJ, Glasgow LR, Pizzo SV.
  TITLE     Purification of an almond emulsin fucosidase on Cibacron
            blue-sepharose and demonstration of its activity toward
            fucose-containing glycoproteins.
  JOURNAL   J. Biol. Chem. 257 (1982) 8205-10.
  ORGANISM  almond
REFERENCE   2  [PMID:18111]
  AUTHORS   Ogata-Arakawa M, Muramatsu T, Kobata A.
  TITLE     alpha-L-fucosidases from almond emulsin: characterization of the two
            enzymes with different specificities.
  JOURNAL   Arch. Biochem. Biophys. 181 (1977) 353-8.
  ORGANISM  almond
REFERENCE   3  [PMID:443810]
  AUTHORS   Yoshima H, Takasaki S, Ito-Mega S, Kobata A.
  TITLE     Purification of almond emulsin alpha-L-fucosidase I by affinity
            chromatography.
  JOURNAL   Arch. Biochem. Biophys. 194 (1979) 394-8.
  ORGANISM  almond
PATHWAY     PATH: map01032  Glycan structures - degradation
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.111
            ExPASy - ENZYME nomenclature database: 3.2.1.111
            ExplorEnz - The Enzyme Database: 3.2.1.111
            ERGO genome analysis and discovery system: 3.2.1.111
            BRENDA, the Enzyme Database: 3.2.1.111
            CAS: 83061-50-1
///
ENTRY       EC 3.2.1.112                Enzyme
NAME        2-deoxyglucosidase;
            2-deoxy-alpha-glucosidase;
            2-deoxy-alpha-D-glucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     2-deoxy-alpha-D-glucoside deoxyglucohydrolase
REACTION    a 2-deoxy-alpha-D-glucoside + H2O = 2-deoxy-D-glucose + an alcohol
            [RN:R02588]
ALL_REAC    R02588
SUBSTRATE   2-deoxy-alpha-D-glucoside [CPD:C03573];
            H2O [CPD:C00001]
PRODUCT     2-deoxy-D-glucose [CPD:C00586];
            alcohol [CPD:C00069]
REFERENCE   1  [PMID:6468386]
  AUTHORS   Canellakis ZN, Bondy PK, May JA Jr, Myers-Robfogel MK, Sartorelli
            AC.
  TITLE     Identification of a glycosidase activity with apparent specificity
            for 2-deoxy-D-glucose in glycosidic linkage.
  JOURNAL   Eur. J. Biochem. 143 (1984) 159-63.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.112
            ExPASy - ENZYME nomenclature database: 3.2.1.112
            ExplorEnz - The Enzyme Database: 3.2.1.112
            ERGO genome analysis and discovery system: 3.2.1.112
            BRENDA, the Enzyme Database: 3.2.1.112
            CAS: 92480-05-2
///
ENTRY       EC 3.2.1.113                Enzyme
NAME        mannosyl-oligosaccharide 1,2-alpha-mannosidase;
            mannosidase 1A;
            mannosidase 1B;
            1,2-alpha-mannosidase;
            exo-alpha-1,2-mannanase;
            mannose-9 processing alpha-mannosidase;
            glycoprotein processing mannosidase I;
            mannosidase I;
            Man9-mannosidase;
            ManI
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,2-alpha-mannosyl-oligosaccharide alpha-D-mannohydrolase
REACTION    Hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in
            the oligo-mannose oligosaccharide Man9(GlcNAc)2
ALL_REAC    (other) R05982(G) R06722(G)
COMMENT     Involved in the synthesis of glycoproteins.
REFERENCE   1  [PMID:500665]
  AUTHORS   Tabas I, Kornfeld S.
  TITLE     Purification and characterization of a rat liver Golgi
            alpha-mannosidase capable of processing asparagine-linked
            oligosaccharides.
  JOURNAL   J. Biol. Chem. 254 (1979) 11655-63.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:7061502]
  AUTHORS   Tulsiani DR, Hubbard SC, Robbins PW, Touster O.
  TITLE     alpha-D-Mannosidases of rat liver Golgi membranes. Mannosidase II is
            the GlcNAcMAN5-cleaving enzyme in glycoprotein biosynthesis and
            mannosidases Ia and IB are the enzymes converting Man9 precursors to
            Man5 intermediates.
  JOURNAL   J. Biol. Chem. 257 (1982) 3660-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map00513  High-mannose type N-glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K01230  mannosyl-oligosaccharide alpha-1,2-mannosidase
GENES       HSA: 10905(MAN1A2) 11253(MAN1B1) 4121(MAN1A1) 57134(MAN1C1)
            PTR: 457159(MAN1A2)
            MMU: 17155(Man1a) 17156(Man1a2) 227619(Man1b1) 230815(Man1c1)
            RNO: 294410(Man1a_predicted) 295319(Man1a2_predicted)
                 362625(Man1c1_predicted) 499751(RGD1563595_predicted)
            CFA: 476275(MAN1A1) 478178(MAN1C1) 480667(MAN1B1) 483141(MAN1A2)
            SSC: 396919(MAN1A)
            GGA: 417296(MAN1B1) 418265(MAN1A2) 419588(MAN1C1) 421726(MAN1A1)
            XLA: 446337(man1a2) 447291(MGC78858)
            DRE: 556237(DKEY-61L1.3)
            SPU: 592701(LOC592701)
            DME: Dmel_CG11874 Dmel_CG31040(Cog7) Dmel_CG32684(alpha-Man-I)
            CEL: ZC410.3(Man(9)-alpha-mannosidase)
            ATH: AT1G30000
            OSA: 4336917 4338088
            CME: CMF045C
            SCE: YJR131W(MNS1)
            AGO: AGOS_AER165W
            PIC: PICST_84949(MNS1)
            CGR: CAGL0M00528g
            ANI: AN0787.2 AN5748.2
            AFM: AFUA_1G14560 AFUA_4G10070 AFUA_6G06790 AFUA_6G12360
                 AFUA_7G02290
            AOR: AO090003000057 AO090003000476
            CNE: CNE04550
            DDI: DDBDRAFT_0190008
STRUCTURES  PDB: 1DL2  1FMI  1G6I  1HCU  1KKT  1KRE  1KRF  1NXC  1X9D  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.113
            ExPASy - ENZYME nomenclature database: 3.2.1.113
            ExplorEnz - The Enzyme Database: 3.2.1.113
            ERGO genome analysis and discovery system: 3.2.1.113
            BRENDA, the Enzyme Database: 3.2.1.113
            CAS: 9068-25-1
///
ENTRY       EC 3.2.1.114                Enzyme
NAME        mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase;
            mannosidase II;
            exo-1,3-1,6-alpha-mannosidase;
            alpha-D-mannosidase II;
            alpha-mannosidase II;
            alpha1-3,6-mannosidase;
            GlcNAc transferase I-dependent alpha1,3[alpha1,6]mannosidase;
            Golgi alpha-mannosidase II;
            ManII;
            1,3(1,6)-alpha-D-mannosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,3-(1,6-)mannosyl-oligosaccharide alpha-D-mannohydrolase
REACTION    Hydrolysis of the terminal 1,3- and 1,6-linked alpha-D-mannose
            residues in the mannosyl-oligosaccharide Man5(GlcNAc)3
ALL_REAC    (other) R05984(G)
COMMENT     Involved in the synthesis of glycoproteins.
REFERENCE   1  [PMID:6445359]
  AUTHORS   Harpaz N, Schachter H.
  TITLE     Control of glycoprotein synthesis. Processing of asparagine-linked
            oligosaccharides by one or more rat liver Golgi alpha-D-mannosidases
            dependent on the prior action of UDP-N-acetylglucosamine:
            alpha-D-mannoside beta 2-N-acetylglucosaminyltransferase I.
  JOURNAL   J. Biol. Chem. 255 (1980) 4894-902.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:7061502]
  AUTHORS   Tulsiani DR, Hubbard SC, Robbins PW, Touster O.
  TITLE     alpha-D-Mannosidases of rat liver Golgi membranes. Mannosidase II is
            the GlcNAcMAN5-cleaving enzyme in glycoprotein biosynthesis and
            mannosidases Ia and IB are the enzymes converting Man9 precursors to
            Man5 intermediates.
  JOURNAL   J. Biol. Chem. 257 (1982) 3660-8.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:863880]
  AUTHORS   Tulsiani DR, Opheim DJ, Touster O.
  TITLE     Purification and characterization of alpha-D-mannosidase from rat
            liver golgi membranes.
  JOURNAL   J. Biol. Chem. 252 (1977) 3227-33.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:15721331]
  AUTHORS   Athanasopoulos VI, Niranjan K, Rastall RA.
  TITLE     The production, purification and characterisation of two novel
            alpha-D-mannosidases from Aspergillus phoenicis.
  JOURNAL   Carbohydr. Res. 340 (2005) 609-17.
PATHWAY     PATH: map00510  N-Glycan biosynthesis
            PATH: map01030  Glycan structures - biosynthesis 1
ORTHOLOGY   KO: K01231  alpha-mannosidase II
GENES       HSA: 4124(MAN2A1)
            PTR: 461982(MAN2A1)
            MMU: 140481(Man2a2) 17158(Man2a1)
            RNO: 308757(Man2a2_predicted)
            CFA: 488745(MAN2A2) 488878(MAN2A1)
            BTA: 527449(LOC527449)
            GGA: 415585(MAN2A2)
            XLA: 443991(MGC80473)
            XTR: 448465(man2a2)
            DRE: 561043(LOC561043)
            SPU: 579104(LOC579104)
            DME: Dmel_CG18802(alpha-Man-II)
            CEL: F58H1.1(alpha-mannosidase)
            ATH: AT5G14950(ATGMII/GMII)
            OSA: 4340636
            TET: TTHERM_00227830 TTHERM_00230960 TTHERM_00629960
                 TTHERM_00629970 TTHERM_00630020 TTHERM_00630030
STRUCTURES  PDB: 1HTY  1HWW  1HXK  1PS3  1QWN  1QWU  1QX1  1R33  1R34  1TQS  
                 1TQT  1TQU  1TQV  1TQW  2ALW  2F18  2F1A  2F1B  2F7O  2F7P  
                 2F7Q  2F7R  2FYV  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.114
            ExPASy - ENZYME nomenclature database: 3.2.1.114
            ExplorEnz - The Enzyme Database: 3.2.1.114
            ERGO genome analysis and discovery system: 3.2.1.114
            BRENDA, the Enzyme Database: 3.2.1.114
            CAS: 82047-77-6
///
ENTRY       EC 3.2.1.115                Enzyme
NAME        branched-dextran exo-1,2-alpha-glucosidase;
            dextran 1,2-alpha-glucosidase;
            dextran alpha-1,2 debranching enzyme
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,2-alpha-D-glucosyl-branched-dextran 2-glucohydrolase
REACTION    Hydrolysis of 1,2-alpha-D-glucosidic linkages at the branch points
            of dextrans and related polysaccharides, producing free D-glucose
COMMENT     Does not hydrolyse disaccharides or oligosaccharides containing
            linear 1,2-alpha-glucosidic linkages.
REFERENCE   1
  AUTHORS   Mitsuishi, Y., Kobayashi, M. and Matsuda, K.
  TITLE     Dextran alpha-1,2-debranching enzyme from Flavobacterium sp. M-73:
            its production and purification.
  JOURNAL   Agric. Biol. Chem. 43 (1979) 2283-2290.
  ORGANISM  Flavobacterium sp.
REFERENCE   2  [PMID:7407800]
  AUTHORS   Mitsuishi Y, Kobayashi M, Matsuda K.
  TITLE     Dextran alpha-(1 yields 2)-debranching enzyme from Flavobacterium
            Sp. M-73. Properties and mode of action.
  JOURNAL   Carbohydr. Res. 83 (1980) 303-13.
  ORGANISM  Flavobacterium sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.115
            ExPASy - ENZYME nomenclature database: 3.2.1.115
            ExplorEnz - The Enzyme Database: 3.2.1.115
            ERGO genome analysis and discovery system: 3.2.1.115
            BRENDA, the Enzyme Database: 3.2.1.115
            CAS: 72840-94-9
///
ENTRY       EC 3.2.1.116                Enzyme
NAME        glucan 1,4-alpha-maltotriohydrolase;
            exo-maltotriohydrolase;
            maltotriohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,4-alpha-D-glucan maltotriohydrolase
REACTION    Hydrolysis of 1,4-alpha-D-glucosidic linkages in amylaceous
            polysaccharides, to remove successive maltotriose residues from the
            non-reducing chain ends
COMMENT     Cf. EC 3.2.1.2 (beta-amylase), EC 3.2.1.60 (glucan
            1,4-alpha-maltotetraohydrolase) and EC 3.2.1.98 (glucan
            1,4-alpha-maltohexaosidase). The products have the
            alpha-configuration.
REFERENCE   1
  AUTHORS   Nakakuki, T., Azuma, K. and Kainuma, K.
  TITLE     Action patterns of various exo-amylases and the anomeric
            configurations of their products.
  JOURNAL   Carbohydr. Res. 128 (1984) 297-310.
  ORGANISM  Streptomyces griseus
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.116
            ExPASy - ENZYME nomenclature database: 3.2.1.116
            ExplorEnz - The Enzyme Database: 3.2.1.116
            ERGO genome analysis and discovery system: 3.2.1.116
            BRENDA, the Enzyme Database: 3.2.1.116
            CAS: 91273-84-6
///
ENTRY       EC 3.2.1.117                Enzyme
NAME        amygdalin beta-glucosidase;
            amygdalase;
            amygdalinase;
            amygdalin hydrolase;
            amygdalin glucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     amygdalin beta-D-glucohydrolase
REACTION    (R)-amygdalin + H2O = (R)-prunasin + D-glucose [RN:R02985]
ALL_REAC    R02985
SUBSTRATE   (R)-amygdalin [CPD:C01982];
            H2O [CPD:C00001]
PRODUCT     (R)-prunasin [CPD:C00844];
            D-glucose [CPD:C00031]
COMMENT     Highly specific; does not act on prunasin, linamarin, gentiobiose or
            cellobiose (cf. EC 3.2.1.21 beta-glucosidase).
REFERENCE   1
  AUTHORS   Kuroki, G., Lizotte, P.A. and Poulton, J.E.
  TITLE     L-beta-Glycosidases from Prunus serotina EHRH and Davallia
            trichomanoides.
  JOURNAL   Z. Natursforsch. C: Biosci. 39 (1984) 232-239.
  ORGANISM  Prunus serotina
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.117
            ExPASy - ENZYME nomenclature database: 3.2.1.117
            ExplorEnz - The Enzyme Database: 3.2.1.117
            ERGO genome analysis and discovery system: 3.2.1.117
            BRENDA, the Enzyme Database: 3.2.1.117
            CAS: 51683-43-3
///
ENTRY       EC 3.2.1.118                Enzyme
NAME        prunasin beta-glucosidase;
            prunasin hydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     prunasin beta-D-glucohydrolase
REACTION    (R)-prunasin + H2O = D-glucose + mandelonitrile [RN:R02558]
ALL_REAC    R02558
SUBSTRATE   (R)-prunasin [CPD:C00844];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031];
            mandelonitrile [CPD:C00561]
COMMENT     Highly specific; does not act on amygdalin, linamarin or
            gentiobiose. (cf. EC 3.2.1.21 beta-glucosidase).
REFERENCE   1
  AUTHORS   Kuroki, G., Lizotte, P.A. and Poulton, J.E.
  TITLE     L-beta-Glycosidases from Prunus serotina EHRH and Davallia
            trichomanoides.
  JOURNAL   Z. Natursforsch. C: Biosci. 39 (1984) 232-239.
  ORGANISM  Prunus serotina
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.118
            ExPASy - ENZYME nomenclature database: 3.2.1.118
            ExplorEnz - The Enzyme Database: 3.2.1.118
            ERGO genome analysis and discovery system: 3.2.1.118
            BRENDA, the Enzyme Database: 3.2.1.118
            CAS: 9023-41-0
///
ENTRY       EC 3.2.1.119                Enzyme
NAME        vicianin beta-glucosidase;
            vicianin hydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     (R)-vicianin beta-D-glucohydrolase
REACTION    (R)-vicianin + H2O = mandelonitrile + vicianose [RN:R03642]
ALL_REAC    R03642
SUBSTRATE   (R)-vicianin [CPD:C01870];
            H2O [CPD:C00001]
PRODUCT     mandelonitrile [CPD:C00561];
            vicianose [CPD:C01625]
COMMENT     Also hydrolyses, more slowly, (R)-amygdalin and (R)-prunasin, but
            not gentiobiose, linamarin or cellobiose.
REFERENCE   1
  AUTHORS   Kuroki, G., Lizotte, P.A. and Poulton, J.E.
  TITLE     L-beta-Glycosidases from Prunus serotina EHRH and Davallia
            trichomanoides.
  JOURNAL   Z. Natursforsch. C: Biosci. 39 (1984) 232-239.
  ORGANISM  Davallia trichomanoides
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.119
            ExPASy - ENZYME nomenclature database: 3.2.1.119
            ExplorEnz - The Enzyme Database: 3.2.1.119
            ERGO genome analysis and discovery system: 3.2.1.119
            BRENDA, the Enzyme Database: 3.2.1.119
            CAS: 91608-93-4
///
ENTRY       EC 3.2.1.120                Enzyme
NAME        oligoxyloglucan beta-glycosidase;
            isoprimeverose-producing oligoxyloglucan hydrolase;
            oligoxyloglucan hydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     oligoxyloglucan xyloglucohydrolase
REACTION    Hydrolysis of 1,4-beta-D-glucosidic links in oligoxyloglucans so as
            to remove successive isoprimeverose (i.e.
            alpha-xylo-1,6-beta-D-glucosyl-) residues from the non-reducing
            chain ends
REFERENCE   1  [PMID:4019436]
  AUTHORS   Kato Y, Matsushita J, Kubodera T, Matsuda K.
  TITLE     A novel enzyme producing isoprimeverose from oligoxyloglucans of
            Aspergillus oryzae.
  JOURNAL   J. Biochem. (Tokyo). 97 (1985) 801-10.
  ORGANISM  Aspergillus oryzae [GN:aor]
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.120
            ExPASy - ENZYME nomenclature database: 3.2.1.120
            ExplorEnz - The Enzyme Database: 3.2.1.120
            ERGO genome analysis and discovery system: 3.2.1.120
            BRENDA, the Enzyme Database: 3.2.1.120
            CAS: 97162-80-6
///
ENTRY       EC 3.2.1.121                Enzyme
NAME        polymannuronate hydrolase;
            polymannuronic acid polymerase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     poly(mannuronide) mannuronohydrolase
REACTION    Endohydrolysis of the D-mannuronide linkages of polymannuronate
COMMENT     Does not act on alginic acid, which is a copolymer of
            polymannuronate.
REFERENCE   1  [PMID:3935048]
  AUTHORS   Dunne WM Jr, Buckmire FL.
  TITLE     Partial purification and characterization of a polymannuronic acid
            depolymerase produced by a mucoid strain of Pseudomonas aeruginosa
            isolated from a patient with cystic fibrosis.
  JOURNAL   Appl. Environ. Microbiol. 50 (1985) 562-7.
  ORGANISM  Pseudomonas aeruginosa
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.121
            ExPASy - ENZYME nomenclature database: 3.2.1.121
            ExplorEnz - The Enzyme Database: 3.2.1.121
            ERGO genome analysis and discovery system: 3.2.1.121
            BRENDA, the Enzyme Database: 3.2.1.121
            CAS: 99283-64-4
///
ENTRY       EC 3.2.1.122                Enzyme
NAME        maltose-6'-phosphate glucosidase;
            phospho-alpha-glucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     maltose-6'-phosphate 6-phosphoglucohydrolase
REACTION    maltose 6'-phosphate + H2O = D-glucose + D-glucose 6-phosphate
            [RN:R00838 R06115]
ALL_REAC    R00838 R06115(G);
            (other) R00837 R06113(G)
SUBSTRATE   maltose 6'-phosphate [CPD:C02995];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031];
            D-glucose 6-phosphate [CPD:C00092]
COMMENT     Hydrolyses a variety of 6-phospho-D-glucosides, including maltose
            6-phosphate, alpha,alpha-trehalose 6-phosphate, sucrose 6-phosphate
            and p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate (as a
            chromogenic substrate). The enzyme is activated by FeII, MnII, CoII
            and NiII. It is rapidly inactivated in air.
REFERENCE   1  [PMID:7730284]
  AUTHORS   Thompson J, Gentry-Weeks CR, Nguyen NY, Folk JE, Robrish SA.
  TITLE     Purification from Fusobacterium mortiferum ATCC 25557 of a
            6-phosphoryl-O-alpha-D-glucopyranosyl:6-phosphoglucohydrolase that
            hydrolyzes maltose 6-phosphate and related
            phospho-alpha-D-glucosides.
  JOURNAL   J. Bacteriol. 177 (1995) 2505-12.
  ORGANISM  Fusobacterium mortiferum
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01232  maltose-6'-phosphate glucosidase
GENES       ECX: EcHS_A3893(glvA)
            YEN: YE3198(aglB)
            ECA: ECA1847(aglB) ECA3226
            PLU: plu1988(malH)
            AHA: AHA_0115
            BSU: BG11839(glvA)
            BLI: BL03017(glvA)
            BLD: BLi00855(malA)
            BCL: ABC2078 ABC3581(glvA)
            BAY: RBAM_008360(glvA)
            BPU: BPUM_0661(glvA)
            LAC: LBA1689(malH)
            LCA: LSEI_0369 LSEI_2684
            CAC: CAC0533(glvA)
            CPE: CPE0199(malH)
            CDF: CD0864 CD1338(glvG)
            CBO: CBO0278(glvA1) CBO0289(glvA2)
            CBA: CLB_0311(glvA-1) CLB_0322(glvA-2) CLB_0333(glvA-3)
            CBH: CLC_0326(glvA-1) CLC_0337(glvA-2) CLC_0348(glvA-3)
            CBF: CLI_0340(glvA-1) CLI_0351(glvA-2) CLI_0362(glvA-3)
STRUCTURES  PDB: 1U8X  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.122
            ExPASy - ENZYME nomenclature database: 3.2.1.122
            ExplorEnz - The Enzyme Database: 3.2.1.122
            ERGO genome analysis and discovery system: 3.2.1.122
            BRENDA, the Enzyme Database: 3.2.1.122
            CAS: 98445-08-0
///
ENTRY       EC 3.2.1.123                Enzyme
NAME        endoglycosylceramidase;
            endoglycoceramidase;
            EGCase;
            glycosyl-N-acetyl-sphingosine 1,1-beta-D-glucanohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     oligoglycosylglucosylceramide glycohydrolase
REACTION    oligoglycosylglucosylceramide + H2O = ceramide +
            oligoglycosylglucose [RN:R04118 R06157]
ALL_REAC    R04118 R06157(G);
            (other) R06283(G)
SUBSTRATE   oligoglycosylglucosylceramide [CPD:C03956];
            H2O [CPD:C00001]
PRODUCT     ceramide [CPD:C00195];
            oligoglycosylglucose [CPD:C03018]
COMMENT     An enzyme from Rhodococcus sp. that degrades various acidic and
            neutral glycosphingolipids to oligosaccharides and ceramides, by
            cleaving a glucosyl bond. Does not act on monoglycosylceramides. cf.
            EC 3.2.1.62 glycosylceramidase.
REFERENCE   1  [PMID:3771534]
  AUTHORS   Ito M, Yamagata T.
  TITLE     A novel glycosphingolipid-degrading enzyme cleaves the linkage
            between the oligosaccharide and ceramide of neutral and acidic
            glycosphingolipids.
  JOURNAL   J. Biol. Chem. 261 (1986) 14278-82.
  ORGANISM  Rhodococcus sp.
ORTHOLOGY   KO: K05991  
GENES       AFM: AFUA_5G00550
            TET: TTHERM_00283470
            PAC: PPA0644 PPA2106
            SEN: SACE_3752
STRUCTURES  PDB: 2OSW  2OSX  2OSY  2OYK  2OYL  2OYM  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.123
            ExPASy - ENZYME nomenclature database: 3.2.1.123
            ExplorEnz - The Enzyme Database: 3.2.1.123
            ERGO genome analysis and discovery system: 3.2.1.123
            BRENDA, the Enzyme Database: 3.2.1.123
            CAS: 105503-61-5
///
ENTRY       EC 3.2.1.124                Enzyme
NAME        3-deoxy-2-octulosonidase;
            2-keto-3-deoxyoctonate hydrolase;
            octulosylono hydrolase;
            octulofuranosylono hydrolase;
            octulopyranosylonohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     capsular-polysaccharide 3-deoxy-D-manno-2-octulosonohydrolase
REACTION    Endohydrolysis of the beta-ketopyranosidic linkages of
            3-deoxy-D-manno-2-octulosonate in capsular polysaccharides
COMMENT     The enzyme from a bacteriophage catalyses the depolymerization of
            capsular polysaccharides containing 3-deoxy-2-octulosonide in the
            cell wall of Escherichia coli.
REFERENCE   1  [PMID:3707579]
  AUTHORS   Altmann F, Kwiatkowski B, Stirm S, Marz L, Unger FM.
  TITLE     A bacteriophage-associated glycanase cleaving beta-pyranosidic
            linkages of 3-deoxy-D-manno-2-octulosonic acid (KDO).
  JOURNAL   Biochem. Biophys. Res. Commun. 136 (1986) 329-35.
  ORGANISM  Bacteriophage PHI20
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.124
            ExPASy - ENZYME nomenclature database: 3.2.1.124
            ExplorEnz - The Enzyme Database: 3.2.1.124
            ERGO genome analysis and discovery system: 3.2.1.124
            BRENDA, the Enzyme Database: 3.2.1.124
            CAS: 103171-48-8
///
ENTRY       EC 3.2.1.125                Enzyme
NAME        raucaffricine beta-glucosidase;
            raucaffricine beta-D-glucosidase;
            raucaffricine glucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     raucaffricine beta-D-glucohydrolase
REACTION    raucaffricine + H2O = D-glucose + vomilenine [RN:R03703]
ALL_REAC    R03703
SUBSTRATE   raucaffricine [CPD:C02074];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031];
            vomilenine [CPD:C01761]
COMMENT     Highly specific; some other ajmalan glucoside alkaloids are
            hydrolysed, but more slowly.
REFERENCE   1  [PMID:16517320]
  AUTHORS   Lee BI, Min KD, Choi HS, Kim JB, Kim ST.
  TITLE     Arthroscopic anterior cruciate ligament reconstruction with the
            tibial-remnant preserving technique using a hamstring graft.
  JOURNAL   Arthroscopy. 22 (2006) 340.e1-7.
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.125
            ExPASy - ENZYME nomenclature database: 3.2.1.125
            ExplorEnz - The Enzyme Database: 3.2.1.125
            ERGO genome analysis and discovery system: 3.2.1.125
            BRENDA, the Enzyme Database: 3.2.1.125
            CAS: 102925-37-1
///
ENTRY       EC 3.2.1.126                Enzyme
NAME        coniferin beta-glucosidase;
            coniferin-hydrolyzing beta-glucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     coniferin beta-D-glucosidase
REACTION    coniferin + H2O = D-glucose + coniferol [RN:R02595]
ALL_REAC    R02595;
            (other) R03604 R04006
SUBSTRATE   coniferin [CPD:C00761];
            H2O [CPD:C00001]
PRODUCT     D-glucose [CPD:C00031];
            coniferol [CPD:C00590]
COMMENT     Also hydrolyses syringin, 4-cinnamyl alcohol beta-glucoside and,
            more slowly, some other aryl beta-glycosides. A plant cell-wall
            enzyme involved in the biosynthesis of lignin.
REFERENCE   1  [PMID:25181]
  AUTHORS   Hosel W, Surholt E, Borgmann E.
  TITLE     Characterization of beta-glucosidase isoenzymes possibly involved in
            lignification from chick pea (Cicer arietinum L.) cell suspension
            cultures.
  JOURNAL   Eur. J. Biochem. 84 (1978) 487-92.
  ORGANISM  Cicer arietinum
REFERENCE   2  [PMID:27355]
  AUTHORS   Marcinowski S, Grisebach H.
  TITLE     Enzymology of lignification. Cell-wall bound beta-glucosidase for
            coniferin from spruce (Picea abies) seedlings.
  JOURNAL   Eur. J. Biochem. 87 (1978) 37-44.
  ORGANISM  Picea abies
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.126
            ExPASy - ENZYME nomenclature database: 3.2.1.126
            ExplorEnz - The Enzyme Database: 3.2.1.126
            ERGO genome analysis and discovery system: 3.2.1.126
            BRENDA, the Enzyme Database: 3.2.1.126
            CAS: 83869-30-1
///
ENTRY       EC 3.2.1.127                Enzyme
NAME        1,6-alpha-L-fucosidase;
            alpha-L-fucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,6-L-fucosyl-N-acetyl-D-glucosaminylglycopeptide fucohydrolase
REACTION    Hydrolysis of 1,6-linkages between alpha-L-fucose and
            N-acetyl-D-glucosamine in glycopeptides such as immunoglobulin G
            glycopeptide and fucosyl-asialo-agalacto-fetuin
COMMENT     The enzyme from Aspergillus niger does not act on 1,2-, 1,3-, or
            1,4-L-fucosyl linkages.
REFERENCE   1  [PMID:2423086]
  AUTHORS   Yazawa S, Madiyalakan R, Chawda RP, Matta KL.
  TITLE     alpha-L-fucosidase from aspergillus niger: demonstration of a novel
            alpha-L-(1----6)-fucosidase acting on glycopeptides.
  JOURNAL   Biochem. Biophys. Res. Commun. 136 (1986) 563-9.
  ORGANISM  Aspergillus niger
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.127
            ExPASy - ENZYME nomenclature database: 3.2.1.127
            ExplorEnz - The Enzyme Database: 3.2.1.127
            ERGO genome analysis and discovery system: 3.2.1.127
            BRENDA, the Enzyme Database: 3.2.1.127
            CAS: 102925-35-9
///
ENTRY       EC 3.2.1.128                Enzyme
NAME        glycyrrhizinate beta-glucuronidase;
            glycyrrhizin beta-hydrolase;
            glycyrrhizin hydrolase;
            glycyrrhizinic acid hydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     glycyrrhizinate glucuronosylhydrolase
REACTION    glycyrrhizinate + H2O = 1,2-beta-D-glucuronosyl-D-glucuronate +
            glycyrrhetinate [RN:R03906]
ALL_REAC    R03906
SUBSTRATE   glycyrrhizinate [CPD:C02284];
            H2O [CPD:C00001]
PRODUCT     1,2-beta-D-glucuronosyl-D-glucuronate [CPD:C04354];
            glycyrrhetinate [CPD:C02283]
COMMENT     The enzyme from Aspergillus niger is specific for the hydrolysis of
            the triterpenoid glycoside glycyrrhizinate from roots of Glycyrrhiza
            sp.
REFERENCE   1
  AUTHORS   Muro, T., Kuramoto, T., Imoto, K. and Okada, S.
  TITLE     Purification and some properties of glycyrrhizinic acid hydrolase
            from Aspergillus niger GRM3.
  JOURNAL   Agric. Biol. Chem. 50 (1986) 687-692.
  ORGANISM  Aspergillus niger
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.128
            ExPASy - ENZYME nomenclature database: 3.2.1.128
            ExplorEnz - The Enzyme Database: 3.2.1.128
            ERGO genome analysis and discovery system: 3.2.1.128
            BRENDA, the Enzyme Database: 3.2.1.128
            CAS: 102484-56-0
///
ENTRY       EC 3.2.1.129                Enzyme
NAME        endo-alpha-sialidase;
            endo-N-acylneuraminidase;
            endoneuraminidase;
            endo-N-acetylneuraminidase;
            poly(alpha-2,8-sialosyl) endo-N-acetylneuraminidase;
            poly(alpha-2,8-sialoside) alpha-2,8-sialosylhydrolase;
            endosialidase;
            endo-N
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     polysialoside (2->8)-alpha-sialosylhydrolase
REACTION    Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or
            poly(sialic) acids
COMMENT     Although the name endo-N-acetylneuraminidase has also been used for
            this enzyme, this is misleading since its activity is not restricted
            to acetylated substrates. An exo-alpha-sialidase activity is listed
            as EC 3.2.1.18 exo-alpha-sialidase. See also EC 4.2.2.15
            anhydrosialidase.
REFERENCE   1  [PMID:3968060]
  AUTHORS   Finne J, Makela PH.
  TITLE     Cleavage of the polysialosyl units of brain glycoproteins by a
            bacteriophage endosialidase. Involvement of a long oligosaccharide
            segment in molecular interactions of polysialic acid.
  JOURNAL   J. Biol. Chem. 260 (1985) 1265-70.
  ORGANISM  bacteriophage PK1A
REFERENCE   2  [PMID:3546309]
  AUTHORS   Hallenbeck PC, Vimr ER, Yu F, Bassler B, Troy FA.
  TITLE     Purification and properties of a bacteriophage-induced
            endo-N-acetylneuraminidase specific for poly-alpha-2,8-sialosyl
            carbohydrate units.
  JOURNAL   J. Biol. Chem. 262 (1987) 3553-61.
  ORGANISM  bacteriophage K1F
REFERENCE   3  [PMID:3142874]
  AUTHORS   Kitajima K, Inoue S, Inoue Y, Troy FA.
  TITLE     Use of a bacteriophage-derived endo-N-acetylneuraminidase and an
            equine antipolysialyl antibody to characterize the polysialyl
            residues in salmonid fish egg polysialoglycoproteins. Substrate and
            immunospecificity studies.
  JOURNAL   J. Biol. Chem. 263 (1988) 18269-76.
  ORGANISM  bacteriophage PK1A
REFERENCE   4  [PMID:7109038]
  AUTHORS   Kwiatkowski B, Boschek B, Thiele H, Stirm S.
  TITLE     Endo-N-acetylneuraminidase associated with bacteriophage particles.
  JOURNAL   J. Virol. 43 (1982) 697-704.
  ORGANISM  bacteriophage PHI1.2
REFERENCE   5  [PMID:2778882]
  AUTHORS   Pelkonen S, Pelkonen J, Finne J.
  TITLE     Common cleavage pattern of polysialic acid by bacteriophage
            endosialidases of different properties and origins.
  JOURNAL   J. Virol. 63 (1989) 4409-16.
  ORGANISM  bacteriophage PK1A, bacteriophage PK1E
REFERENCE   6  [PMID:3894684]
  AUTHORS   Tomlinson S, Taylor PW.
  TITLE     Neuraminidase associated with coliphage E that specifically
            depolymerizes the Escherichia coli K1 capsular polysaccharide.
  JOURNAL   J. Virol. 55 (1985) 374-8.
  ORGANISM  bacteriophage E
REFERENCE   7  [PMID:1883340]
  AUTHORS   Cabezas JA.
  TITLE     Some questions and suggestions on the type references of the
            official nomenclature (IUB) for sialidase(s) and endosialidase.
  JOURNAL   Biochem. J. 278 ( Pt 1) (1991) 311-2.
PATHWAY     PATH: map01032  Glycan structures - degradation
STRUCTURES  PDB: 1V0E  1V0F  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.129
            ExPASy - ENZYME nomenclature database: 3.2.1.129
            ExplorEnz - The Enzyme Database: 3.2.1.129
            ERGO genome analysis and discovery system: 3.2.1.129
            BRENDA, the Enzyme Database: 3.2.1.129
            CAS: 91195-87-8
///
ENTRY       EC 3.2.1.130                Enzyme
NAME        glycoprotein endo-alpha-1,2-mannosidase;
            glucosylmannosidase;
            endo-alpha-D-mannosidase;
            endo-alpha-mannosidase;
            endomannosidase;
            glucosyl mannosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     glycoprotein glucosylmannohydrolase
REACTION    Hydrolysis of the terminal alpha-D-glucosyl-(1,3)-D-mannosyl unit
            from the GlcMan9(GlcNAc)2 oligosaccharide component of the
            glycoprotein produced in the Golgi membrane
COMMENT     Involved in the synthesis of glycoproteins.
REFERENCE   1  [PMID:3818665]
  AUTHORS   Lubas WA, Spiro RG.
  TITLE     Golgi endo-alpha-D-mannosidase from rat liver, a novel N-linked
            carbohydrate unit processing enzyme.
  JOURNAL   J. Biol. Chem. 262 (1987) 3775-81.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:2407194]
  AUTHORS   Tulsiani DR, Coleman VD, Touster O.
  TITLE     Asparagine-linked glycoprotein biosynthesis in rat brain:
            identification of glucosidase I, glucosidase II, and and
            endomannosidase (glucosyl mannosidase).
  JOURNAL   Arch. Biochem. Biophys. 277 (1990) 114-21.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.130
            ExPASy - ENZYME nomenclature database: 3.2.1.130
            ExplorEnz - The Enzyme Database: 3.2.1.130
            ERGO genome analysis and discovery system: 3.2.1.130
            BRENDA, the Enzyme Database: 3.2.1.130
            CAS: 108022-16-8
///
ENTRY       EC 3.2.1.131                Enzyme
NAME        xylan alpha-1,2-glucuronosidase;
            1,2-alpha-glucuronidase;
            alpha-(1->2)-glucuronidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     xylan alpha-D-1,2-(4-O-methyl)glucuronohydrolase
REACTION    Hydrolysis of alpha-D-1,2-(4-O-methyl)glucuronosyl links in the main
            chain of hardwood xylans
REFERENCE   1
  AUTHORS   Ishihara, M. and Shimizu, K.
  TITLE     alpha-(1->2)-Glucuronidase in the enzymatic saccharification of
            hardwood xylan .1. Screening of alpha-glucuronidase producing fungi.
  JOURNAL   Mokuzai Gakkaishi 34 (1988) 58-64.
  ORGANISM  Tyromyces palustris, Trichoderma aureoviride, Trichoderma hamatum,
            Trichoderma harzianum, Trichoderma koningii, Trichoderma
            longibrachiatum, Trichoderma viride, Trichoderma sp., Agaricus
            bisporus, Laetiporus sulphureus var. miniatus, Pleurotus ostreatus,
            Polyporus versicolor
GENES       ANG: An14g05800(aguA)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.131
            ExPASy - ENZYME nomenclature database: 3.2.1.131
            ExplorEnz - The Enzyme Database: 3.2.1.131
            ERGO genome analysis and discovery system: 3.2.1.131
            BRENDA, the Enzyme Database: 3.2.1.131
            CAS: 114921-73-2
///
ENTRY       EC 3.2.1.132                Enzyme
NAME        chitosanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     chitosan N-acetylglucosaminohydrolase
REACTION    Endohydrolysis of beta-1,4-linkages between D-glucosamine residues
            in a partly acetylated chitosan
ALL_REAC    (other) R02833 R06175(G)
COMMENT     A whole spectrum of chitosanases are now known (for more details,
            see http://pages.usherbrooke.ca/rbrzezinski/). They can hydrolyse
            various types of links in chitosan. The only constant property is
            the endohydrolysis of GlcN-GlcN links, which is common to all known
            chitosanases. One known chitosanase is limited to this link
            recognition [4], while the majority can also recognize GlcN-GlcNAc
            links or GlcNAc-GlcN links but not both. They also do not recognize
            GlcNAc-GlcNAc links in partly acetylated chitosan.
REFERENCE   1
  AUTHORS   Fenton, D.M. and Eveleigh, D.E.
  TITLE     Purification and mode of action of a chitosanase from Penicillium
            islandicum.
  JOURNAL   J. Gen. Microbiol. 126 (1981) 151-165.
  ORGANISM  Penicillium islandicum
REFERENCE   2  [PMID:10521473]
  AUTHORS   Saito J, Kita A, Higuchi Y, Nagata Y, Ando A, Miki K.
  TITLE     Crystal structure of chitosanase from Bacillus circulans MH-K1 at
            1.6-A resolution and its substrate recognition mechanism.
  JOURNAL   J. Biol. Chem. 274 (1999) 30818-25.
  ORGANISM  Bacillus circulans
REFERENCE   3  [PMID:1368330]
  AUTHORS   Izume M, Nagae S, Kawagishi H, Mitsutomi M, Ohtakara A.
  TITLE     Action pattern of Bacillus sp. no. 7-M chitosanase on partially
            N-acetylated chitosan.
  JOURNAL   Biosci. Biotechnol. Biochem. 56 (1992) 448-53.
  ORGANISM  Bacillus sp.
REFERENCE   4  [PMID:8564542]
  AUTHORS   Marcotte EM, Monzingo AF, Ernst SR, Brzezinski R, Robertus JD.
  TITLE     X-ray structure of an anti-fungal chitosanase from streptomyces
            N174.
  JOURNAL   Nat. Struct. Biol. 3 (1996) 155-62.
  ORGANISM  Streptomyces sp.
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K01233  chitosanase
GENES       AFM: AFUA_3G14980 AFUA_4G01290 AFUA_6G00500 AFUA_8G00930
            CVI: CV_3931
            BSU: BG11923(csn)
STRUCTURES  PDB: 1QGI  1V5C  1V5D  2D05  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.132
            ExPASy - ENZYME nomenclature database: 3.2.1.132
            ExplorEnz - The Enzyme Database: 3.2.1.132
            ERGO genome analysis and discovery system: 3.2.1.132
            BRENDA, the Enzyme Database: 3.2.1.132
            CAS: 51570-20-8
///
ENTRY       EC 3.2.1.133                Enzyme
NAME        glucan 1,4-alpha-maltohydrolase;
            maltogenic alpha-amylase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,4-alpha-D-glucan alpha-maltohydrolase
REACTION    hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides
            so as to remove successive alpha-maltose residues from the
            non-reducing ends of the chains
COMMENT     Acts on starch and related polysaccharides and oligosaccharides. The
            product is alpha-maltose; cf. EC 3.2.1.2 beta-amylase.
REFERENCE   1
  AUTHORS   Diderichsen, B. and Christiansen, L.
  TITLE     Cloning of a maltogenic alpha-amylase from Bacillus
            stearothermophilus.
  JOURNAL   FEMS Microbiol. Lett. 56 (1988) 53-59.
  ORGANISM  Bacillus stearothermophilus
REFERENCE   2
  AUTHORS   Outtrup, H. and Norman, B.E.
  TITLE     Properties and application of a thermostable maltogenic amylase
            produced by a strain of Bacillus modified by recombinant-DNA
            techniques.
  JOURNAL   Starke 36 (1984) 405-411.
ORTHOLOGY   KO: K05992  
GENES       VFI: VF2049
            BLD: BLi00658
            SPZ: M5005_Spy_1066(amyB)
            SPH: MGAS10270_Spy1122(amyB)
            SPI: MGAS10750_Spy1159(amyB)
            LPL: lp_2757
            LSL: LSL_0067(amyB) LSL_1295
STRUCTURES  PDB: 1QHO  1QHP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.133
            ExPASy - ENZYME nomenclature database: 3.2.1.133
            ExplorEnz - The Enzyme Database: 3.2.1.133
            ERGO genome analysis and discovery system: 3.2.1.133
            BRENDA, the Enzyme Database: 3.2.1.133
            CAS: 160611-47-2
///
ENTRY       EC 3.2.1.134                Enzyme
NAME        difructose-anhydride synthase;
            inulobiose hydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     bis-D-fructose 2',1:2,1'-dianhydride fructohydrolase
REACTION    bis-D-fructose 2',1:2,1'-dianhydride + H2O = inulobiose [RN:R03685
            R06161]
ALL_REAC    R03685 R06161(G)
SUBSTRATE   bis-D-fructose 2',1:2,1'-dianhydride [CPD:C04333];
            H2O [CPD:C00001]
PRODUCT     inulobiose [CPD:C01711]
COMMENT     Produces difructose anhydride by the reverse reaction of partial
            hydrolysis, forming an alpha-fructosidic linkage.
REFERENCE   1
  AUTHORS   Matsuyama, T. and Tanaka, K.
  TITLE     On the enzyme of Aspergillus fumigatus producing difructose
            anhydride I from inulobiose.
  JOURNAL   Agric. Biol. Chem. 53 (1989) 831-832.
  ORGANISM  Aspergillus fumigatus [GN:afm]
REFERENCE   2  [PMID:6757245]
  AUTHORS   Matsuyama T, Tanaka K, Mashiko M, Kanamoto M.
  TITLE     Enzymic formation of di-D-fructose 1,2'; 2,1' dianhydride from
            inulobiose by Aspergillus fumigatus.
  JOURNAL   J. Biochem. (Tokyo). 92 (1982) 1325-8.
  ORGANISM  Aspergillus fumigatus [GN:afm]
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.134
            ExPASy - ENZYME nomenclature database: 3.2.1.134
            ExplorEnz - The Enzyme Database: 3.2.1.134
            ERGO genome analysis and discovery system: 3.2.1.134
            BRENDA, the Enzyme Database: 3.2.1.134
            CAS: 121479-55-8
///
ENTRY       EC 3.2.1.135                Enzyme
NAME        neopullulanase;
            pullulanase II
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     pullulan 4-D-glucanohydrolase (panose-forming)
REACTION    Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose)
COMMENT     cf. EC 3.2.1.41 (pullulanase ) and EC 3.2.1.57 (isopullulanase).
REFERENCE   1  [PMID:2914851]
  AUTHORS   Imanaka T, Kuriki T.
  TITLE     Pattern of action of Bacillus stearothermophilus neopullulanase on
            pullulan.
  JOURNAL   J. Bacteriol. 171 (1989) 369-74.
  ORGANISM  Bacillus stearothermophilus
ORTHOLOGY   KO: K01234  neopullulanase
GENES       VFI: VF2049
            PHA: PSHAa1354 PSHAa1355
            BCE: BC4014
            BCZ: BCZK3771(nplT)
            BTL: BALH_3634(nplT)
            LMF: LMOf2365_2160(nplT)
            LWE: lwe2146
            LLC: LACR_1852
            LLM: llmg_0740(dexC)
            SPZ: M5005_Spy_1066(amyB)
            SPH: MGAS10270_Spy1122(amyB)
            SPI: MGAS10750_Spy1159(amyB)
            SPB: M28_Spy1047(amyB)
            SPR: spr0948(nplT)
            SPD: SPD_0927(nplT)
            SSA: SSA_1457(dexB)
            SGO: SGO_1351
            LJO: LJ0212
            LAC: LBA1871
            LSL: LSL_0067(amyB) LSL_1295
            LGA: LGAS_0215
            CPR: CPR_0789
            SYN: sll0842(nplT)
            SYW: SYNW1952
            SYG: sync_0570
            GVI: glr3646
            ANA: alr4646
            PMT: PMT0192
            PMF: P9303_21691
            SRU: SRU_2743
            DGE: Dgeo_0611
STRUCTURES  PDB: 1BVZ  1G1Y  1J0H  1J0I  1J0J  1J0K  1JF5  1JF6  1JI2  1JIB  
                 1JL8  1VFK  1VFM  1VFO  1VFU  1WZK  1WZL  1WZM  2D2O  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.135
            ExPASy - ENZYME nomenclature database: 3.2.1.135
            ExplorEnz - The Enzyme Database: 3.2.1.135
            ERGO genome analysis and discovery system: 3.2.1.135
            BRENDA, the Enzyme Database: 3.2.1.135
            CAS: 119632-58-5
///
ENTRY       EC 3.2.1.136                Enzyme
NAME        glucuronoarabinoxylan endo-1,4-beta-xylanase;
            feraxan endoxylanase;
            feraxanase;
            endoarabinoxylanase;
            glucuronoxylan xylohydrolase;
            glucuronoxylanase;
            glucuronoxylan xylanohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     glucuronoarabinoxylan 1,4-beta-D-xylanohydrolase
REACTION    Endohydrolysis of 1,4-beta-D-xylosyl links in some
            glucuronoarabinoxylans
COMMENT     High activity towards feruloylated arabinoxylans from cereal plant
            cell walls.
REFERENCE   1
  AUTHORS   Nishitani, K. and Nevins, D.J.
  TITLE     Enzymic analysis of feruloylated arabinoxylans (Feraxan) derived
            from Zea mays cell walls. I. Purification of novel enzymes capable
            of dissociating Feraxan fragments from Zea mays coleoptile cell
            wall.
  JOURNAL   Plant Physiol. 87 (1988) 883-890.
  ORGANISM  Bacillus subtilis [GN:bsu]
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.136
            ExPASy - ENZYME nomenclature database: 3.2.1.136
            ExplorEnz - The Enzyme Database: 3.2.1.136
            ERGO genome analysis and discovery system: 3.2.1.136
            BRENDA, the Enzyme Database: 3.2.1.136
            CAS: 123609-77-8
///
ENTRY       EC 3.2.1.137                Enzyme
NAME        mannan exo-1,2-1,6-alpha-mannosidase;
            exo-1,2-1,6-alpha-mannosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,2-1,6-alpha-D-mannan D-mannohydrolase
REACTION    Hydrolysis of 1,2-alpha-D- and 1,6-alpha-D- linkages in yeast
            mannan, releasing D-mannose
ALL_REAC    (other) R01331(G) R05816 R06149(G) R06150(G)
COMMENT     Mannose residues linked alpha-D-1,3- are also released, but very
            slowly.
REFERENCE   1
  AUTHORS   Takegawa, K., Miki, S., Jikibara, T. and Iwahara, S.
  TITLE     Purification and characterization of exo-alpha-D-mannosidase from a
            Cellulomonas sp.
  JOURNAL   Biochim. Biophys. Acta 991 (1989) 431-437.
  ORGANISM  Cellulomonas sp.
PATHWAY     PATH: map00051  Fructose and mannose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.137
            ExPASy - ENZYME nomenclature database: 3.2.1.137
            ExplorEnz - The Enzyme Database: 3.2.1.137
            ERGO genome analysis and discovery system: 3.2.1.137
            BRENDA, the Enzyme Database: 3.2.1.137
            CAS: 123175-72-4
///
ENTRY       EC 3.2.1.138      Obsolete  Enzyme
NAME        Transferred to 4.2.2.15
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
COMMENT     Transferred entry: now EC 4.2.2.15 anhydrosialidase. (EC 3.2.1.138
            created 1992, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.138
            ExPASy - ENZYME nomenclature database: 3.2.1.138
            ExplorEnz - The Enzyme Database: 3.2.1.138
            ERGO genome analysis and discovery system: 3.2.1.138
            BRENDA, the Enzyme Database: 3.2.1.138
///
ENTRY       EC 3.2.1.139                Enzyme
NAME        alpha-glucuronidase;
            alpha-glucosiduronase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     alpha-D-glucosiduronate glucuronohydrolase
REACTION    an alpha-D-glucuronoside + H2O = an alcohol + D-glucuronate
            [RN:R01480]
ALL_REAC    R01480
SUBSTRATE   alpha-D-glucuronoside [CPD:C06370];
            H2O [CPD:C00001]
PRODUCT     alcohol [CPD:C00069];
            D-glucuronate [CPD:C00191]
COMMENT     Considerable differences in the specificities of the enzymes from
            different fungi for alpha-D-glucosiduronates have been reported.
            Activity is also found in the snail.
REFERENCE   1
  AUTHORS   Puls, J.
  TITLE     alpha-Glucuronidases in the hydrolysis of wood xylans.
  JOURNAL   In: Visser, J., Kusters van Someren, M.A., Beldman, G. and Voragen,
            A.G.J. (Eds.), Xylans and Xylanases, Elsevier, Amsterdam, 1992, p.
            213-224.
REFERENCE   2
  AUTHORS   Uchida, H., Nanri, T., Kawabata, Y., Kusakabe, I., Murakami, K.
  TITLE     Purification and characterization of intracellular
            alpha-glucuronidase from Aspergillus niger.
  JOURNAL   Biosci. Biotechnol. Biochem. 56 (1992) 1608-1615.
  ORGANISM  Aspergillus niger
ORTHOLOGY   KO: K01235  alpha-glucuronidase
GENES       ANI: AN9286.2
            AFM: AFUA_5G14380
            AOR: AO090026000127
            XCC: XCC4102(aguA)
            XCB: XC_4193
            XCV: XCV4333(aguA)
            XAC: XAC4227(aguA)
            XOO: XOO4419(aguA)
            XOM: XOO_4162(XOO4162)
            SDE: Sde_1025
            CCR: CC_2811
            ABA: Acid345_0963
            SUS: Acid_2666
            BHA: BH1061
            BCL: ABC0555
            LLM: llmg_1169(aguA)
            CSC: Csac_2689
            SMA: SAV1450
            BTH: BT_2622
            FJO: Fjoh_1993
            TMA: TM0055
            TPT: Tpet_0869
STRUCTURES  PDB: 1GQI  1GQJ  1GQK  1GQL  1H41  1K9D  1K9E  1K9F  1L8N  1MQP  
                 1MQQ  1MQR  1VJT  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.139
            ExPASy - ENZYME nomenclature database: 3.2.1.139
            ExplorEnz - The Enzyme Database: 3.2.1.139
            ERGO genome analysis and discovery system: 3.2.1.139
            BRENDA, the Enzyme Database: 3.2.1.139
            CAS: 37259-81-7
///
ENTRY       EC 3.2.1.140                Enzyme
NAME        lacto-N-biosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     oligosaccharide lacto-N-biosylhydrolase
REACTION    (1) beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc +
            H2O = beta-D-Gal-(1->3)-D-GlcNAc + beta-D-Gal-(1->4)-D-Glc;
            (2) lacto-N-tetraose + H2O = lacto-N-biose + lactose
ALL_REAC    (other) R05166 R06116(G)
SUBSTRATE   beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc;
            H2O [CPD:C00001];
            lacto-N-tetraose [CPD:C06371]
PRODUCT     beta-D-Gal-(1->3)-D-GlcNAc [CPD:C06372];
            beta-D-Gal-(1->4)-D-Glc [CPD:C06373];
            lacto-N-biose [CPD:C06372];
            lactose [CPD:C00243]
COMMENT     The enzyme from Streptomyces specifically hydrolyses the terminal
            lacto-N-biosyl residue (beta-D-Gal-(1->3)-D-GlcNAc) from the
            non-reducing end of oligosaccharides with the structure
            beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->R).
            Lacto-N-hexaose
            (beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->3)-beta-D-Glc
            NAc-(1->3)-beta-D-Gal-(1->4)-D-Glc) is hydrolysed to form first
            lacto-N-tetraose plus lacto-N-biose, with the subsequent formation
            of lactose. Oligosaccharides in which the non-reducing terminal Gal
            or the penultimate GlcNAc are replaced by fucose or sialic acid are
            not substrates. Asialo GM1 tetraose
            (beta-D-Gal-(1->3)-beta-D-GalNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc) is
            hydrolysed very slowly, but lacto-N-neotetraose
            (beta-D-Gal-(1->4)-beta-D-GalNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc) is
            not a substrate
REFERENCE   1  [PMID:1528855]
  AUTHORS   Sano M, Hayakawa K, Kato I.
  TITLE     An enzyme releasing lacto-N-biose from oligosaccharides.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 8512-6.
  ORGANISM  Streptomyces sp.
REFERENCE   2  [PMID:7689556]
  AUTHORS   Sano M, Hayakawa K, Kato I.
  TITLE     Purification and characterization of an enzyme releasing
            lacto-N-biose from oligosaccharides with type 1 chain.
  JOURNAL   J. Biol. Chem. 268 (1993) 18560-6.
  ORGANISM  Streptomyces sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.140
            ExPASy - ENZYME nomenclature database: 3.2.1.140
            ExplorEnz - The Enzyme Database: 3.2.1.140
            ERGO genome analysis and discovery system: 3.2.1.140
            BRENDA, the Enzyme Database: 3.2.1.140
            CAS: 146359-52-6
///
ENTRY       EC 3.2.1.141                Enzyme
NAME        4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase;
            malto-oligosyltrehalose trehalohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     4-alpha-D-[(1->4)-alpha-D-glucano]trehalose glucanohydrolase
            (trehalose-producing)
REACTION    hydrolysis of alpha-(1->4)-D-glucosidic linkage in
            4-alpha-D-[(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose
            and alpha-(1->4)-D-glucan
REFERENCE   1  [PMID:8534970]
  AUTHORS   Maruta K, Nakada T, Kubota M, Chaen H, Sugimoto T, Kurimoto M,
            Tsujisaka Y.
  TITLE     Formation of trehalose from maltooligosaccharides by a novel
            enzymatic system.
  JOURNAL   Biosci. Biotechnol. Biochem. 59 (1995) 1829-34.
  ORGANISM  Arthrobacter sp.
REFERENCE   2  [PMID:8611745]
  AUTHORS   Nakada T, Maruta K, Mitsuzumi H, Kubota M, Chaen H, Sugimoto T,
            Kurimoto M, Tsujisaka Y.
  TITLE     Purification and characterization of a novel enzyme, maltooligosyl
            trehalose trehalohydrolase, from Arthrobacter sp. Q36.
  JOURNAL   Biosci. Biotechnol. Biochem. 59 (1995) 2215-8.
  ORGANISM  Arthrobacter sp.
REFERENCE   3  [PMID:9063974]
  AUTHORS   Nakada T, Ikegami S, Chaen H, Kubota M, Fukuda S, Sugimoto T,
            Kurimoto M, Tsujisaka Y.
  TITLE     Purification and characterization of thermostable maltooligosyl
            trehalose trehalohydrolase from the thermoacidophilic
            archaebacterium Sulfolobus acidocaldarius.
  JOURNAL   Biosci. Biotechnol. Biochem. 60 (1996) 267-70.
  ORGANISM  Sulfolobus acidocaldarius [GN:sai]
ORTHOLOGY   KO: K01236  maltooligosyltrehalose trehalohydrolase
GENES       XCC: XCC0410
            XCB: XC_0423
            XCV: XCV0453
            XAC: XAC0427
            XOO: XOO0114
            XOM: XOO_0064(XOO0064)
            PAP: PSPA7_3142(treZ)
            PPU: PP_4051
            PPF: Pput_1792
            PSB: Psyr_2993
            PSP: PSPPH_2247(treZ)
            PFL: PFL_2886(treZ)
            PEN: PSEEN2053
            RSO: RS05186(RSp0237)
            BMA: BMA0818
            BXE: Bxe_B2865
            BUR: Bcep18194_B2247 Bcep18194_C7030
            BCH: Bcen2424_6495
            BPS: BPSL2078
            BPM: BURPS1710b_1735(treZ)
            BPL: BURPS1106A_1564(treZ)
            BPD: BURPS668_1541(treZ)
            RFR: Rfer_2157
            AZO: azo1798(treZ)
            MFA: Mfla_1417
            DDE: Dde_0999
            AFW: Anae109_3802
            MXA: MXAN_0541(treZ)
            RET: RHE_CH03279
            BRA: BRADO5819
            BBT: BBta_6325
            RPE: RPE_1273
            NWI: Nwi_1205
            GBE: GbCGDNIH1_0749
            RRU: Rru_A2295
            SUS: Acid_0218
            MTA: Moth_1809
            MTU: Rv1562c(treZ)
            MTC: MT1613(treZ)
            MBO: Mb1588c(treZ)
            MPA: MAP1268c(glgZ)
            MAV: MAV_3212(treZ)
            MSM: MSMEG_3184(treZ)
            MMC: Mmcs_3082
            CGL: NCgl2045(cgl2125)
            CGB: cg2333(treZ)
            CEF: CE2025
            CJK: jk0773(treZ)
            NFA: nfa18050
            RHA: RHA1_ro01062
            CMI: CMM_1430(treZ)
            AAU: AAur_2895(treZ)
            FRA: Francci3_1347
            FAL: FRAAL2116(treZ)
            CYA: CYA_0184(treZ)
            CYB: CYB_2529(treZ)
            AVA: Ava_1428
            SRU: SRU_0659(treZ)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.141
            ExPASy - ENZYME nomenclature database: 3.2.1.141
            ExplorEnz - The Enzyme Database: 3.2.1.141
            ERGO genome analysis and discovery system: 3.2.1.141
            BRENDA, the Enzyme Database: 3.2.1.141
            CAS: 170780-50-4
///
ENTRY       EC 3.2.1.142                Enzyme
NAME        limit dextrinase;
            R-enzyme;
            amylopectin-1,6-glucosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     dextrin alpha-1,6-glucanohydrolase
REACTION    Hydrolysis of (1->6)-alpha-D-glucosidic linkages in alpha- and
            beta-limit dextrins of amylopectin and glycogen, and in amylopectin
            and pullulan
COMMENT     Plant enzymes with little or no action on glycogen. Action on
            amylopectin is incomplete, but action on alpha-limit dextrins is
            complete. Maltose is the smallest sugar it can release from an
            alpha-(1->6)-linkage.
REFERENCE   1
  AUTHORS   Gordon, R.W., Manners, D.J. and Stark, J.R.
  TITLE     The limit dextrinase of the broad bean (Vicia faba).
  JOURNAL   Carbohydr. Res. 42 (1975) 125-134.
  ORGANISM  Vicia faba
REFERENCE   2
  AUTHORS   Manners, D.J.
  TITLE     Observations on the specificity and nomenclature of starch
            debranching enzymes.
  JOURNAL   J. Appl. Glycosci. 44 (1997) 83-85.
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.142
            ExPASy - ENZYME nomenclature database: 3.2.1.142
            ExplorEnz - The Enzyme Database: 3.2.1.142
            ERGO genome analysis and discovery system: 3.2.1.142
            BRENDA, the Enzyme Database: 3.2.1.142
///
ENTRY       EC 3.2.1.143                Enzyme
NAME        poly(ADP-ribose) glycohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
REACTION    hydrolyses poly(ADP-ribose) at glycosidic (1"-2') linkage of
            ribose-ribose bond to produce free ADP-ribose
COMMENT     Specific to (1"-2') linkage of ribose-ribose bond of
            poly(ADP-ribose).
REFERENCE   1  [PMID:4331388]
  AUTHORS   Miwa M, Sugimura T.
  TITLE     Splitting of the ribose-ribose linkage of poly(adenosine
            diphosphate-robose) by a calf thymus extract.
  JOURNAL   J. Biol. Chem. 246 (1971) 6362-4.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:9115250]
  AUTHORS   Lin W, Ame JC, Aboul-Ela N, Jacobson EL, Jacobson MK.
  TITLE     Isolation and characterization of the cDNA encoding bovine
            poly(ADP-ribose) glycohydrolase.
  JOURNAL   J. Biol. Chem. 272 (1997) 11895-901.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K07759  poly(ADP-ribose) glycohydrolase
GENES       HSA: 8505(PARG)
            MMU: 26430(Parg)
            RNO: 83507(Parg)
            CFA: 477749(PARG)
            BTA: 281377(PARG)
            GGA: 423617(PARG)
            DRE: 796446(zgc:92867)
            DME: Dmel_CG2864(Parg)
            CEL: H23L24.5(glycohydrolase)
            OSA: 4334754
            TET: TTHERM_00006460 TTHERM_00030590 TTHERM_00052040
                 TTHERM_00052350
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.143
            ExPASy - ENZYME nomenclature database: 3.2.1.143
            ExplorEnz - The Enzyme Database: 3.2.1.143
            ERGO genome analysis and discovery system: 3.2.1.143
            BRENDA, the Enzyme Database: 3.2.1.143
///
ENTRY       EC 3.2.1.144                Enzyme
NAME        3-deoxyoctulosonase;
            alpha-Kdo-ase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     3-deoxyoctulosonyl-lipopolysaccharide hydrolase
REACTION    3-deoxyoctulosonyl-lipopolysaccharide + H2O = 3-deoxyoctulosonic
            acid + lipopolysaccharide [RN:R06054]
ALL_REAC    R06054
SUBSTRATE   3-deoxyoctulosonyl-lipopolysaccharide [CPD:C06744];
            H2O [CPD:C00001]
PRODUCT     3-deoxyoctulosonic acid [CPD:C01187];
            lipopolysaccharide [CPD:C00338]
COMMENT     Releases Kdo (alpha- and beta-linked 3-deoxy-D-manno-octulosonic
            acid) from different lipopolysaccharides, including Re-LPS from
            Escherichia coli and Salmonella, Rd-LPS from S. minnesota, and
            de-O-acyl-re-LPS. 4-Methylumbelliferyl-alpha-Kdo (alpha-Kdo-OMec) is
            also a substrate.
REFERENCE   1  [PMID:9334217]
  AUTHORS   Li YT, Wang LX, Pavlova NV, Li SC, Lee YC.
  TITLE     alpha-KDOase activity in oyster and synthesis of alpha- and
            beta-4-methylumbelliferyl ketosides of 3-deoxy-D-manno-octulosonic
            acid.
  JOURNAL   J. Biol. Chem. 272 (1997) 26419-24.
  ORGANISM  Crassostrea virginica
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.144
            ExPASy - ENZYME nomenclature database: 3.2.1.144
            ExplorEnz - The Enzyme Database: 3.2.1.144
            ERGO genome analysis and discovery system: 3.2.1.144
            BRENDA, the Enzyme Database: 3.2.1.144
///
ENTRY       EC 3.2.1.145                Enzyme
NAME        galactan 1,3-beta-galactosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     galactan (1->3)-beta-D-galactosidase
REACTION    Hydrolysis of terminal, non-reducing beta-D-galactose residues in
            (1->3)-beta-D-galactopyranans
COMMENT     This enzyme removes not only free galactose, but also 6-glycosylated
            residues, e.g., (1->6)-beta-D-galactobiose, and galactose bearing
            oligosaccharide chains on O-6. Hence, it releases branches from
            [arabino-galacto-(1->6)]-(1->3)-beta-D-galactans.
REFERENCE   1  [PMID:2158993]
  AUTHORS   Tsumuraya Y, Mochizuki N, Hashimoto Y, Kovac P.
  TITLE     Purification of an exo-beta-(1----3)-D-galactanase of Irpex lacteus
            (Polyporus tulipiferae) and its action on arabinogalactan-proteins.
  JOURNAL   J. Biol. Chem. 265 (1990) 7207-15.
  ORGANISM  Irpex lacteus
REFERENCE   2  [PMID:7805066]
  AUTHORS   Pellerin P, Brillouet JM.
  TITLE     Purification and properties of an exo-(1--&gt;3)-beta-D-galactanase
            from Aspergillus niger.
  JOURNAL   Carbohydr. Res. 264 (1994) 281-91.
  ORGANISM  Aspergillus niger
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.145
            ExPASy - ENZYME nomenclature database: 3.2.1.145
            ExplorEnz - The Enzyme Database: 3.2.1.145
            ERGO genome analysis and discovery system: 3.2.1.145
            BRENDA, the Enzyme Database: 3.2.1.145
///
ENTRY       EC 3.2.1.146                Enzyme
NAME        beta-galactofuranosidase;
            exo-beta-galactofuranosidase;
            exo-beta-D-galactofuranosidase;
            beta-D-galactofuranosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     beta-D-galactofuranoside hydrolase
REACTION    Hydrolysis of terminal non-reducing beta-D-galactofuranosides,
            releasing galactose
COMMENT     The enzyme from Helminthosporium sacchari detoxifies
            helminthosporoside, a bis(digalactosyl)terpene produced by this
            fungus, by releasing its four molecules of bound galactose.
REFERENCE   1  [PMID:863879]
  AUTHORS   Rietschel-Berst M, Jentoft NH, Rick PD, Pletcher C, Fang F, Gander
            JE.
  TITLE     Extracellular exo-beta-galactofuranosidase from Penicillium
            charlesii: isolation, purification, and properties.
  JOURNAL   J. Biol. Chem. 252 (1977) 3219-26.
  ORGANISM  Penicillium charlesii
REFERENCE   2
  AUTHORS   Daley, L.S. and Strobel, G.A.
  TITLE     beta-Galactofuranosidase activity in Helminthosporium sacchari and
            its relationship to the production of helminthosporoside.
  JOURNAL   Plant Sci. Lett. 30 (1983) 145-154.
  ORGANISM  Helminthosporium sacchari
REFERENCE   3  [PMID:2502527]
  AUTHORS   Cousin MA, Notermans S, Hoogerhout P, Van Boom JH.
  TITLE     Detection of beta-galactofuranosidase production by Penicillium and
            Aspergillus species using 4-nitrophenyl beta-D-galactofuranoside.
  JOURNAL   J. Appl. Bacteriol. 66 (1989) 311-7.
  ORGANISM  Penicillium funiculosum, Penicillium islandicum, Penicillium rubrum,
            Penicillium tardum, Aspergillus spp.
REFERENCE   4  [PMID:10573856]
  AUTHORS   Miletti LC, Marino C, Marino K, de Lederkremer RM, Colli W, Alves
            MJ.
  TITLE     Immobilized 4-aminophenyl 1-thio-beta-D-galactofuranoside as a
            matrix for affinity purification of an
            exo-beta-D-galactofuranosidase.
  JOURNAL   Carbohydr. Res. 320 (1999) 176-82.
  ORGANISM  Penicillium fellutanum
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.146
            ExPASy - ENZYME nomenclature database: 3.2.1.146
            ExplorEnz - The Enzyme Database: 3.2.1.146
            ERGO genome analysis and discovery system: 3.2.1.146
            BRENDA, the Enzyme Database: 3.2.1.146
///
ENTRY       EC 3.2.1.147                Enzyme
NAME        thioglucosidase;
            myrosinase;
            sinigrinase;
            sinigrase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     thioglucoside glucohydrolase
REACTION    a thioglucoside + H2O = a sugar + a thiol [RN:R01237]
ALL_REAC    R01237;
            (other) R04094
SUBSTRATE   thioglucoside [CPD:C02085];
            H2O [CPD:C00001]
PRODUCT     sugar [CPD:C11477];
            thiol [CPD:C00145]
COMMENT     Has a wide specificity for thioglycosides.
REFERENCE   1
  AUTHORS   Goodman, I., Fouts, J.R., Bresnick, E., Menegas, R. and Hitchings,
            G.H.
  TITLE     A mammalian thioglucosidase.
  JOURNAL   Science 130 (1959) 450-451.
REFERENCE   2
  AUTHORS   Pigman, W.W.
  TITLE     Action of almond emulsin on the phenyl glucosides of synthetic
            sugars and on beta-thiophenyl d-glucoside.
  JOURNAL   J. Res. Nat. Bur. Stand. 26 (1941) 197-204.
  ORGANISM  almond
PATHWAY     PATH: map00380  Tryptophan metabolism
ORTHOLOGY   KO: K01237  myrosinase
GENES       ATH: AT2G44460 AT2G44470 AT2G44490(PEN2)
            REH: H16_A0250
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.147
            ExPASy - ENZYME nomenclature database: 3.2.1.147
            ExplorEnz - The Enzyme Database: 3.2.1.147
            ERGO genome analysis and discovery system: 3.2.1.147
            BRENDA, the Enzyme Database: 3.2.1.147
            CAS: 9025-38-1
///
ENTRY       EC 3.2.1.148      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
COMMENT     Deleted entry: was transferred to EC 3.13.1.2,
            5-deoxyribos-5-ylhomocysteinase, which has since been deleted. The
            activity is most probably attributable to EC 4.4.1.21,
            S-ribosylhomocysteine lyase (EC 3.2.1.148 created 1972 as EC
            3.3.1.3, transferred 2001 to EC 3.2.1.148, deleted 2004)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.148
            ExPASy - ENZYME nomenclature database: 3.2.1.148
            ExplorEnz - The Enzyme Database: 3.2.1.148
            ERGO genome analysis and discovery system: 3.2.1.148
            BRENDA, the Enzyme Database: 3.2.1.148
///
ENTRY       EC 3.2.1.149                Enzyme
NAME        beta-primeverosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranoside
            6-O-(beta-D-xylosyl)-beta-D-glucohydrolase
REACTION    a 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranoside + H2O =
            6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranose + an alcohol
            [RN:R05788]
ALL_REAC    R05788
SUBSTRATE   6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranoside [CPD:C11531];
            H2O [CPD:C00001]
PRODUCT     6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranose [CPD:C11535];
            alcohol [CPD:C00069]
COMMENT     The enzyme is responsible for the formation of the alcoholic aroma
            in oolong and black tea. In addition to beta-primeverosides [i.e.
            6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranosides], it also
            hydrolyses 6-O-(beta-D-apiofuranosyl)-beta-D-glucopyranosides and,
            less rapidly, beta-vicianosides and
            6-O-(alpha-L-arabinofuranosyl)-beta-D-glucopyranosides, but not
            beta-glucosides. Geranyl-, linaloyl-, benzyl- and p-nitrophenol
            glycosides are all hydrolysed.
REFERENCE   1
  AUTHORS   Ijima, Y., Ogawa, K., Watanabe, N., Usui, T., Ohnishi-Kameyama, M.,
            Nagata, T. and Sakata, K.
  TITLE     Characterization of beta-primeverosidase, being concerned with
            alcoholic aroma formation in tea leaves to be processed into black
            tea, and preliminary observations on its substrate specificity.
  JOURNAL   J. Agric. Food Chem. 46 (1998) 1712-1718.
  ORGANISM  Camellia sinensis
REFERENCE   2
  AUTHORS   Ogawa, K., Ijima, Y., Guo, W., Watanabe, N., Usui, T., Dong, S.,
            Tong, Q. and Sakata, K.
  TITLE     Purification of a beta-primeverosidase concerned with alcoholic
            aroma formation in tea leaves (cv. Shuxian) to be processed to
            oolong tea.
  JOURNAL   J. Agric. Food Chem. 45 (1997) 877-882.
  ORGANISM  Camellia sinensis
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.149
            ExPASy - ENZYME nomenclature database: 3.2.1.149
            ExplorEnz - The Enzyme Database: 3.2.1.149
            ERGO genome analysis and discovery system: 3.2.1.149
            BRENDA, the Enzyme Database: 3.2.1.149
///
ENTRY       EC 3.2.1.150                Enzyme
NAME        oligoxyloglucan reducing-end-specific cellobiohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     oligoxyloglucan reducing-end cellobiohydrolase
REACTION    Hydrolysis of cellobiose from the reducing end of xyloglucans
            consisting of a beta-1,4-linked glucan carrying alpha-D-xylosyl
            groups on O-6 of the glucose residues. To be a substrate, the first
            residue must be unsubstituted, the second residue may bear a xylosyl
            group, whether further glycosylated or not, and the third residue,
            which becomes the new terminus by the action of the enzyme, is
            preferably xylosylated, but this xylose residue must not be further
            substituted.
COMMENT     The enzyme is found in the fungus Geotrichum sp. M128. The substrate
            is a hemicellulose found in plant cell walls.
REFERENCE   1  [PMID:12374797]
  AUTHORS   Yaoi K, Mitsuishi Y.
  TITLE     Purification, characterization, cloning, and expression of a novel
            xyloglucan-specific glycosidase, oligoxyloglucan reducing
            end-specific cellobiohydrolase.
  JOURNAL   J. Biol. Chem. 277 (2002) 48276-81.
  ORGANISM  Geotrichum sp.
STRUCTURES  PDB: 1SQJ  2EBS  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.150
            ExPASy - ENZYME nomenclature database: 3.2.1.150
            ExplorEnz - The Enzyme Database: 3.2.1.150
            ERGO genome analysis and discovery system: 3.2.1.150
            BRENDA, the Enzyme Database: 3.2.1.150
///
ENTRY       EC 3.2.1.151                Enzyme
NAME        xyloglucan-specific endo-beta-1,4-glucanase;
            XEG;
            xyloglucan endo-beta-1,4-glucanase;
            xyloglucanase;
            xyloglucanendohydrolase;
            XH;
            1,4-beta-D-glucan glucanohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     [(1->6)-alpha-D-xylo]-(1->4)-beta-D-glucan glucanohydrolase
REACTION    xyloglucan + H2O = xyloglucan oligosaccharides
SUBSTRATE   xyloglucan [CPD:C00807];
            H2O [CPD:C00001]
PRODUCT     xyloglucan oligosaccharides
COMMENT     The enzyme from Aspergillus aculeatus is specific for xyloglucan and
            does not hydrolyse other cell-wall components. The reaction involves
            endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with
            retention of the beta-configuration of the glycosyl residues.
REFERENCE   1  [PMID:9884411]
  AUTHORS   Pauly M, Andersen LN, Kauppinen S, Kofod LV, York WS, Albersheim P,
            Darvill A.
  TITLE     A xyloglucan-specific endo-beta-1,4-glucanase from Aspergillus
            aculeatus: expression cloning in yeast, purification and
            characterization of the recombinant enzyme.
  JOURNAL   Glycobiology. 9 (1999) 93-100.
  ORGANISM  Aspergillus aculeatus
REFERENCE   2  [PMID:15541296]
  AUTHORS   Grishutin SG, Gusakov AV, Markov AV, Ustinov BB, Semenova MV,
            Sinitsyn AP.
  TITLE     Specific xyloglucanases as a new class of polysaccharide-degrading
            enzymes.
  JOURNAL   Biochim. Biophys. Acta. 1674 (2004) 268-81.
  ORGANISM  Aspergillus japonicus, Chrysosporium lucknowense, Trichoderma reesei
STRUCTURES  PDB: 2CN2  2CN3  2E0P  2E4T  2EEX  2EJ1  2EO7  2EQD  2JEM  2JEN  
                 2JEP  2JEQ  2UWA  2UWB  2UWC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.151
            ExPASy - ENZYME nomenclature database: 3.2.1.151
            ExplorEnz - The Enzyme Database: 3.2.1.151
            ERGO genome analysis and discovery system: 3.2.1.151
            BRENDA, the Enzyme Database: 3.2.1.151
///
ENTRY       EC 3.2.1.152                Enzyme
NAME        mannosylglycoprotein endo-beta-mannosidase;
            endo-beta-mannosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
REACTION    Hydrolysis of the
            alpha-D-mannosyl-(1->6)-beta-D-mannosyl-(1->4)-beta-D-N-
            acetylglucosaminyl-(1->4)-beta-D-N-acetylglucosaminyl sequence of
            glycoprotein to alpha-D-mannosyl-(1->6)-D-mannose and
            beta-D-N-acetylglucosaminyl-(1->4)-beta-D-N-acetylglucosaminyl
            sequences
COMMENT     The substrate group is a substituent on N-4 of an asparagine residue
            in the glycoprotein. The mannose residue at the non-reducing end of
            the sequence may carry further alpha-D-mannosyl groups on O-3 or
            O-6, but such a substituent on O-3 of the beta-D-mannosyl group
            prevents the action of the enzyme. The enzyme was obtained from the
            lily, Lilium longiflorum.
REFERENCE   1  [PMID:15247239]
  AUTHORS   Ishimizu T, Sasaki A, Okutani S, Maeda M, Yamagishi M, Hase S.
  TITLE     Endo-beta-mannosidase, a plant enzyme acting on N-glycan:
            purification, molecular cloning, and characterization.
  JOURNAL   J. Biol. Chem. 279 (2004) 38555-62.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   2  [PMID:9990135]
  AUTHORS   Sasaki A, Yamagishi M, Mega T, Norioka S, Natsuka S, Hase S.
  TITLE     Partial purification and characterization of a novel
            endo-beta-mannosidase acting on N-linked sugar chains from Lilium
            longflorum thumb.
  JOURNAL   J. Biochem. (Tokyo). 125 (1999) 363-7.
  ORGANISM  Lilium longflorum
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.152
            ExPASy - ENZYME nomenclature database: 3.2.1.152
            ExplorEnz - The Enzyme Database: 3.2.1.152
            ERGO genome analysis and discovery system: 3.2.1.152
            BRENDA, the Enzyme Database: 3.2.1.152
///
ENTRY       EC 3.2.1.153                Enzyme
NAME        fructan beta-(2,1)-fructosidase;
            beta-(2-1)-D-fructan fructohydrolase;
            beta-(2-1)fructan exohydrolase;
            inulinase;
            1-FEH II;
            1-fructan exohydrolase;
            1-FEH w1;
            1-FEH w2;
            beta-(2-1)-linkage-specific fructan-beta-fructosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     beta-(2,1)-D-fructan fructohydrolase
REACTION    Hydrolysis of terminal, non-reducing 2,1-linked
            beta-D-fructofuranose residues in fructans
COMMENT     Possesses one of the activities of EC 3.2.1.80, fructan
            beta-fructosidase. While the best substrates are the inulin-type
            fructans, such as 1-kestose
            (beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl
            alpha-D-glucopyranoside) and 1,1-nystose
            (beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl-(2->1)-beta-D-
            fructofuranosyl alpha-D-glucopyranoside), some (but not all)
            levan-type fructans can also be hydrolysed, but more slowly [see EC
            3.2.1.154, fructan beta-(2,6)-fructosidase]. Sucrose, while being a
            very poor substrate, can substantially inhibit enzyme activity in
            some cases.
REFERENCE   1  [PMID:16526094]
  AUTHORS   Foucher AL, McIntosh A, Douce G, Wastling J, Tait A, Turner CM.
  TITLE     A proteomic analysis of arsenical drug resistance in Trypanosoma
            brucei.
  JOURNAL   Proteomics. 6 (2006) 2726-32.
REFERENCE   2  [PMID:12586886]
  AUTHORS   Van Den Ende W, Clerens S, Vergauwen R, Van Riet L, Van Laere A,
            Yoshida M, Kawakami A.
  TITLE     Fructan 1-exohydrolases. beta-(2,1)-trimmers during graminan
            biosynthesis in stems of wheat? Purification, characterization, mass
            mapping, and cloning of two fructan 1-exohydrolase isoforms.
  JOURNAL   Plant. Physiol. 131 (2003) 621-31.
  ORGANISM  Triticum aestivum [GN:etae]
STRUCTURES  PDB: 2ADD  2ADE  2AEY  2AEZ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.153
            ExPASy - ENZYME nomenclature database: 3.2.1.153
            ExplorEnz - The Enzyme Database: 3.2.1.153
            ERGO genome analysis and discovery system: 3.2.1.153
            BRENDA, the Enzyme Database: 3.2.1.153
///
ENTRY       EC 3.2.1.154                Enzyme
NAME        fructan beta-(2,6)-fructosidase;
            beta-(2-6)-fructan exohydrolase;
            levanase;
            6-FEH
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     beta-(2,6)-D-fructan fructohydrolase
REACTION    Hydrolysis of terminal, non-reducing 2,6-linked
            beta-D-fructofuranose residues in fructans
COMMENT     Possesses one of the activities of EC 3.2.1.80, fructan
            beta-fructosidase. While the best substrates are the levan-type
            fructans such as 6-kestotriose
            (beta-D-fructofuranosyl-(2->6)-beta-D-fructofuranosyl
            alpha-D-glucopyranoside) and 6,6-kestotetraose
            (beta-D-fructofuranosyl-(2->6)-beta-D-fructofuranosyl-(2->6)-beta-D-
            fructofuranosyl alpha-D-glucopyranoside), some (but not all)
            inulin-type fructans can also be hydrolysed, but more slowly (cf. EC
            3.2.1.153, fructan beta-(2,1)-fructosidase). Sucrose, while being a
            very poor substrate, can substantially inhibit enzyme activity in
            some cases.
REFERENCE   1
  AUTHORS   Marx, S.P., Nosberger, J. and Frehner, M.
  TITLE     Hydrolysis of fructan in grasses: A beta-(2-6)-linkage specific
            fructan-beta-fructosidase from stubble of Lolium perenne.
  JOURNAL   New Phytol. 135 (1997) 279-290.
  ORGANISM  Lolium perenne
REFERENCE   2  [PMID:14617070]
  AUTHORS   Van den Ende W, De Coninck B, Clerens S, Vergauwen R, Van Laere A.
  TITLE     Unexpected presence of fructan 6-exohydrolases (6-FEHs) in
            non-fructan plants: characterization, cloning, mass mapping and
            functional analysis of a novel &quot;cell-wall invertase-like&quot;
            specific 6-FEH from sugar beet (Beta vulgaris L.).
  JOURNAL   Plant. J. 36 (2003) 697-710.
  ORGANISM  Beta vulgaris
REFERENCE   3  [PMID:8742337]
  AUTHORS   Henson CA, Livingston DP 3rd.
  TITLE     Purification and characterization of an oat fructan exohydrolase
            that preferentially hydrolyzes beta-2,6-fructans.
  JOURNAL   Plant. Physiol. 110 (1996) 639-44.
  ORGANISM  Avena sativa
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.154
            ExPASy - ENZYME nomenclature database: 3.2.1.154
            ExplorEnz - The Enzyme Database: 3.2.1.154
            ERGO genome analysis and discovery system: 3.2.1.154
            BRENDA, the Enzyme Database: 3.2.1.154
///
ENTRY       EC 3.2.1.155                Enzyme
NAME        xyloglucan-specific exo-beta-1,4-glucanase;
            Cel74A
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     [(1->6)-alpha-D-xylo]-(1->4)-beta-D-glucan exo-glucohydrolase
REACTION    xyloglucan + H2O = xyloglucan oligosaccharides (exohydrolysis of
            1,4-beta-D-glucosidic linkages in xyloglucan)
SUBSTRATE   xyloglucan [CPD:C00807];
            H2O [CPD:C00001]
PRODUCT     xyloglucan oligosaccharides (exohydrolysis of 1,4-beta-D-glucosidic
            linkages in xyloglucan)
COMMENT     The enzyme from Chrysosporium lucknowense is an endoglucanase, i.e.
            acquires the specificity of EC 3.2.1.151, xyloglucan-specific
            endo-beta-1,4-glucanase, when it acts on linear substrates without
            bulky substituents on the polymeric backbone (e.g.
            carboxymethylcellulose). However, it switches to an exoglucanase
            mode of action when bulky side chains are present (as in the case of
            xyloglucan). The enzyme can also act on barley beta-glucan, but more
            slowly.
REFERENCE   1  [PMID:15541296]
  AUTHORS   Grishutin SG, Gusakov AV, Markov AV, Ustinov BB, Semenova MV,
            Sinitsyn AP.
  TITLE     Specific xyloglucanases as a new class of polysaccharide-degrading
            enzymes.
  JOURNAL   Biochim. Biophys. Acta. 1674 (2004) 268-81.
  ORGANISM  Aspergillus japonicus, Chrysosporium lucknowense, Trichoderma reesei
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.155
            ExPASy - ENZYME nomenclature database: 3.2.1.155
            ExplorEnz - The Enzyme Database: 3.2.1.155
            ERGO genome analysis and discovery system: 3.2.1.155
            BRENDA, the Enzyme Database: 3.2.1.155
///
ENTRY       EC 3.2.1.156                Enzyme
NAME        oligosaccharide reducing-end xylanase;
            Rex;
            reducing end xylose-releasing exo-oligoxylanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose reducing-end
            xylanase
REACTION    Hydrolysis of 1,4-beta-D-xylose residues from the reducing end of
            oligosaccharides
COMMENT     The enzyme acts rapidly on the beta-anomer of
            beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose, leaving the new
            reducing end in the alpha configuration. It also acts on longer
            oligosaccharides that have this structure at their reducing ends.
            The penultimate residue must be xylose, but replacing either of the
            other two residues with glucose merely slows the rate greatly.
REFERENCE   1  [PMID:15491996]
  AUTHORS   Honda Y, Kitaoka M.
  TITLE     A family 8 glycoside hydrolase from Bacillus halodurans C-125
            (BH2105) is a reducing end xylose-releasing exo-oligoxylanase.
  JOURNAL   J. Biol. Chem. 279 (2004) 55097-103.
  ORGANISM  Bacillus halodurans [GN:bha]
REFERENCE   2  [PMID:15718242]
  AUTHORS   Fushinobu S, Hidaka M, Honda Y, Wakagi T, Shoun H, Kitaoka M.
  TITLE     Structural basis for the specificity of the reducing end
            xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125.
  JOURNAL   J. Biol. Chem. 280 (2005) 17180-6.
  ORGANISM  Bacillus halodurans [GN:bha]
STRUCTURES  PDB: 1WU4  1WU5  1WU6  2DRO  2DRQ  2DRR  2DRS  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.156
            ExPASy - ENZYME nomenclature database: 3.2.1.156
            ExplorEnz - The Enzyme Database: 3.2.1.156
            ERGO genome analysis and discovery system: 3.2.1.156
            BRENDA, the Enzyme Database: 3.2.1.156
            CAS: 879497-03-7
///
ENTRY       EC 3.2.1.157                Enzyme
NAME        iota-carrageenase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     iota-carrageenan 4-beta-D-glycanohydrolase (configuration-inverting)
REACTION    Endohydrolysis of 1,4-beta-D-linkages between D-galactose 4-sulfate
            and 3,6-anhydro-D-galactose-2-sulfate in iota-carrageenans
COMMENT     The main products of hydrolysis are iota-neocarratetraose sulfate
            and iota-neocarrahexaose sulfate. iota-Neocarraoctaose is the
            shortest substrate oligomer that can be cleaved. Unlike EC 3.2.1.81,
            beta-agarase and EC 3.2.1.83, kappa-carrageenase, this enzyme
            proceeds with inversion of the anomeric configuration.
            iota-Carrageenan differs from kappa-carrageenan by possessing a
            sulfo group on O-2 of the 3,6-anhydro-D-galactose residues, in
            addition to that present in the kappa-compound on O-4 of the
            D-galactose residues.
REFERENCE   1  [PMID:10934194]
  AUTHORS   Barbeyron T, Michel G, Potin P, Henrissat B, Kloareg B.
  TITLE     iota-Carrageenases constitute a novel family of glycoside
            hydrolases, unrelated to that of kappa-carrageenases.
  JOURNAL   J. Biol. Chem. 275 (2000) 35499-505.
  ORGANISM  Zobellia galactanovorans, Alteromonas fortis
REFERENCE   2  [PMID:11493601]
  AUTHORS   Michel G, Chantalat L, Fanchon E, Henrissat B, Kloareg B, Dideberg
            O.
  TITLE     The iota-carrageenase of Alteromonas fortis. A beta-helix
            fold-containing enzyme for the degradation of a highly polyanionic
            polysaccharide.
  JOURNAL   J. Biol. Chem. 276 (2001) 40202-9.
  ORGANISM  Alteromonas fortis
REFERENCE   3  [PMID:14623184]
  AUTHORS   Michel G, Helbert W, Kahn R, Dideberg O, Kloareg B.
  TITLE     The structural bases of the processive degradation of
            iota-carrageenan, a main cell wall polysaccharide of red algae.
  JOURNAL   J. Mol. Biol. 334 (2003) 421-33.
  ORGANISM  Alteromonas fortis
STRUCTURES  PDB: 1H80  1KTW  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.157
            ExPASy - ENZYME nomenclature database: 3.2.1.157
            ExplorEnz - The Enzyme Database: 3.2.1.157
            ERGO genome analysis and discovery system: 3.2.1.157
            BRENDA, the Enzyme Database: 3.2.1.157
///
ENTRY       EC 3.2.1.158                Enzyme
NAME        alpha-agarase;
            agarase (ambiguous);
            agaraseA33
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     agarose 3-glycanohydrolase
REACTION    Endohydrolysis of 1,3-alpha-L-galactosidic linkages in agarose,
            yielding agarotetraose as the major product
COMMENT     Requires Ca2+. The enzyme from Thalassomonas sp. can use agarose,
            agarohexaose and neoagarohexaose as substrate. The products of
            agarohexaose hydrolysis are dimers and tetramers, with agarotetraose
            being the predominant product, whereas hydrolysis of neoagarohexaose
            gives rise to two types of trimer. While the enzyme can also
            hydrolyse the highly sulfated agarose porphyran very efficiently, it
            cannot hydrolyse the related compounds kappa-carrageenan (see EC
            3.2.1.83) and iota-carrageenan (see EC 3.2.1.157) [2]. See also EC
            3.2.1.81, beta-agarase.
REFERENCE   1  [PMID:8513809]
  AUTHORS   Potin P, Richard C, Rochas C, Kloareg B.
  TITLE     Purification and characterization of the alpha-agarase from
            Alteromonas agarlyticus (Cataldi) comb. nov., strain GJ1B.
  JOURNAL   Eur. J. Biochem. 214 (1993) 599-607.
  ORGANISM  Alteromonas agarlyticus
REFERENCE   2  [PMID:15902469]
  AUTHORS   Ohta Y, Hatada Y, Miyazaki M, Nogi Y, Ito S, Horikoshi K.
  TITLE     Purification and characterization of a novel alpha-agarase from a
            Thalassomonas sp.
  JOURNAL   Curr. Microbiol. 50 (2005) 212-6.
  ORGANISM  Thalassomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.158
            ExPASy - ENZYME nomenclature database: 3.2.1.158
            ExplorEnz - The Enzyme Database: 3.2.1.158
            ERGO genome analysis and discovery system: 3.2.1.158
            BRENDA, the Enzyme Database: 3.2.1.158
///
ENTRY       EC 3.2.1.159                Enzyme
NAME        alpha-neoagaro-oligosaccharide hydrolase;
            alpha-neoagarooligosaccharide hydrolase;
            alpha-NAOS hydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     alpha-neoagaro-oligosaccharide 3-glycohydrolase
REACTION    Hydrolysis of the 1,3-alpha-L-galactosidic linkages of
            neoagaro-oligosaccharides that are smaller than a hexamer, yielding
            3,6-anhydro-L-galactose and D-galactose
COMMENT     When neoagarohexaose is used as a substrate, the oligosaccharide is
            cleaved at the non-reducing end to produce 3,6-anhydro-L-galactose
            and agaropentaose, which is further hydrolysed to agarobiose and
            agarotriose. With neoagarotetraose as substrate, the products are
            predominantly agarotriose and 3,6-anhydro-L-galactose. In Vibrio sp.
            the actions of EC 3.2.1.81, beta-agarase and EC 3.2.1.159 can be
            used to degrade agarose to 3,6-anhydro-L-galactose and D-galactose.
REFERENCE   1  [PMID:7961439]
  AUTHORS   Sugano Y, Kodama H, Terada I, Yamazaki Y, Noma M.
  TITLE     Purification and characterization of a novel enzyme,
            alpha-neoagarooligosaccharide hydrolase (alpha-NAOS hydrolase), from
            a marine bacterium, Vibrio sp. strain JT0107.
  JOURNAL   J. Bacteriol. 176 (1994) 6812-8.
  ORGANISM  Vibrio sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.159
            ExPASy - ENZYME nomenclature database: 3.2.1.159
            ExplorEnz - The Enzyme Database: 3.2.1.159
            ERGO genome analysis and discovery system: 3.2.1.159
            BRENDA, the Enzyme Database: 3.2.1.159
///
ENTRY       EC 3.2.1.160      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
COMMENT     Deleted entry: xyloglucan-specific exo-beta-1,4-glucanase. The
            enzyme was shown to be identical to EC 3.2.1.155,
            xyloglucan-specific exo-beta-1,4-glucanase, during the public-review
            process so was withdrawn before being made official. (EC 3.2.1.160
            created 2006, deleted 2006)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.160
            ExPASy - ENZYME nomenclature database: 3.2.1.160
            ExplorEnz - The Enzyme Database: 3.2.1.160
            ERGO genome analysis and discovery system: 3.2.1.160
            BRENDA, the Enzyme Database: 3.2.1.160
///
ENTRY       EC 3.2.1.161                Enzyme
NAME        beta-apiosyl-beta-glucosidase;
            isoflavonoid-7-O-beta[D-apiosyl-(1->6)-beta-D-glucoside]
            disaccharidase;
            isoflavonoid 7-O-beta-apiosyl-glucoside beta-glucosidase;
            furcatin hydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     7-[beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranosyloxy]isoflavonoid
            beta-D-apiofuranosyl-(1->6)-D-glucohydrolase
REACTION    7-[beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranosyloxy]isoflavonoid
            + H2O = a 7-hydroxyisoflavonoid +
            beta-D-apiofuranosyl-(1->6)-D-glucose
SUBSTRATE   7-[beta-D-apiofuranosyl-(1->6)-beta-D-
            glucopyranosyloxy]isoflavonoid;
            H2O [CPD:C00001]
PRODUCT     7-hydroxyisoflavonoid;
            beta-D-apiofuranosyl-(1->6)-D-glucose
COMMENT     The enzyme from the tropical tree Dalbergia nigrescens Kurz belongs
            in glycosyl hydrolase family 1. The enzyme removes disaccharides
            from the natural substrates dalpatein
            7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside and
            7-hydroxy-2',4',5',6-tetramethoxy-7-O-beta-D-apiofuranosyl-(1->6)-be
            ta-D-glucopyranoside (dalnigrein
            7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside) although it
            can also remove a single glucose residue from isoflavonoid
            7-O-glucosides [2]. Daidzin and genistin are also substrates.
REFERENCE   1  [PMID:240725]
  AUTHORS   Hosel W, Barz W.
  TITLE     Beta-Glucosidases from Cicer arietinum L. Purification and
            Properties of isoflavone-7-O-glucoside-specific beta-glucosidases.
  JOURNAL   Eur. J. Biochem. 57 (1975) 607-16.
  ORGANISM  Cicer arietinum
REFERENCE   2  [PMID:16098548]
  AUTHORS   Chuankhayan P, Hua Y, Svasti J, Sakdarat S, Sullivan PA, Ketudat
            Cairns JR.
  TITLE     Purification of an isoflavonoid 7-O-beta-apiosyl-glucoside
            beta-glycosidase and its substrates from Dalbergia nigrescens Kurz.
  JOURNAL   Phytochemistry. 66 (2005) 1880-9.
  ORGANISM  Dalbergia nigrescens
REFERENCE   3  [PMID:14976214]
  AUTHORS   Ahn YO, Mizutani M, Saino H, Sakata K.
  TITLE     Furcatin hydrolase from Viburnum furcatum Blume is a novel
            disaccharide-specific acuminosidase in glycosyl hydrolase family 1.
  JOURNAL   J. Biol. Chem. 279 (2004) 23405-14.
  ORGANISM  Viburnum furcatum
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.161
            ExPASy - ENZYME nomenclature database: 3.2.1.161
            ExplorEnz - The Enzyme Database: 3.2.1.161
            ERGO genome analysis and discovery system: 3.2.1.161
            BRENDA, the Enzyme Database: 3.2.1.161
///
ENTRY       EC 3.2.1.162                Enzyme
NAME        lambda-carrageenase;
            endo-beta-1,4-carrageenose 2,6,2'-trisulfate-hydrolase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
REACTION    Endohydrolysis of beta-1,4-linkages in the backbone of
            lambda-carrageenan, resulting in the tetrasaccharide
            alpha-D-Galp2,6S2-(1->3)-beta-D-Galp2S-(1->4)-alpha-D-Galp2,6S2-(1-
            >3)-D-Galp2S
COMMENT     The enzyme from Pseudoalteromonas sp. is specific for
            lambda-carrageenan. iota-Carrageenan (see EC 3.2.1.157,
            iota-carrageenase), kappa-carrageenan (see EC 3.2.1.83,
            kappa-carrageenase), agarose and porphyran are not substrates.
REFERENCE   1  [PMID:16926183]
  AUTHORS   Ohta Y, Hatada Y.
  TITLE     A novel enzyme, lambda-carrageenase, isolated from a deep-sea
            bacterium.
  JOURNAL   J. Biochem. (Tokyo). 140 (2006) 475-81.
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.162
            ExPASy - ENZYME nomenclature database: 3.2.1.162
            ExplorEnz - The Enzyme Database: 3.2.1.162
            ERGO genome analysis and discovery system: 3.2.1.162
            BRENDA, the Enzyme Database: 3.2.1.162
///
ENTRY       EC 3.2.1.163                Enzyme
NAME        1,6-alpha-D-mannosidase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
SYSNAME     1,6-alpha-mannosyl alpha-D-mannohydrolase
REACTION    Hydrolysis of the 1,6-linked alpha-D-mannose residues in
            alpha-D-Manp-(1->6)-D-Manp
COMMENT     The enzyme is specific for (1->6)-linked mannobiose and has no
            activity towards any other linkages, or towards
            p-nitrophenyl-alpha-D-mannopyranoside or baker's yeast mannan. It is
            strongly inhibited by Mn2+ but does not require Ca2+ or any other
            metal cofactor for activity.
REFERENCE   1  [PMID:15721331]
  AUTHORS   Athanasopoulos VI, Niranjan K, Rastall RA.
  TITLE     The production, purification and characterisation of two novel
            alpha-D-mannosidases from Aspergillus phoenicis.
  JOURNAL   Carbohydr. Res. 340 (2005) 609-17.
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.163
            ExPASy - ENZYME nomenclature database: 3.2.1.163
            ExplorEnz - The Enzyme Database: 3.2.1.163
            ERGO genome analysis and discovery system: 3.2.1.163
            BRENDA, the Enzyme Database: 3.2.1.163
///
ENTRY       EC 3.2.1.164                Enzyme
NAME        galactan endo-1,6-beta-galactosidase;
            endo-1,6-beta-galactanase;
            endo-beta-(1->6)-galactanase
CLASS       Hydrolases;
            Glycosylases;
            Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
            compounds
REACTION    Endohydrolysis of 1,6-beta-D-galactosidic linkages in
            arabinogalactan proteins and 1,3:1,6-beta-galactans to yield
            galactose and beta-(1->6)-galactaobiose as the final products
COMMENT     The enzyme specifically hydrolyses
            1,6-beta-D-galactooligosaccharides with a degree of polymerization
            (DP) higher than 3, and their acidic derivatives with
            4-O-methylglucosyluronate or glucosyluronate groups at the
            non-reducing terminals [2]. 1,3-beta-D- and 1,4-beta-D-galactosyl
            residues cannot act as substrates. The enzyme can also hydrolyse
            alpha-L-arabinofuranosidase-treated arabinogalactan protein (AGP)
            extracted from radish roots [2,3]. AGPs are thought to be involved
            in many physiological events, such as cell division, cell expansion
            and cell death [3].
REFERENCE   1
  AUTHORS   Brillouet, J.-M., Williams, P. and Moutounet, M.
  TITLE     Purification and some properties of a novel
            endo-beta-(1->6)-D-galactanase from Aspergillus niger.
  JOURNAL   Agric. Biol. Chem. 55 (1991) 1565-1571.
REFERENCE   2  [PMID:12543554]
  AUTHORS   Okemoto K, Uekita T, Tsumuraya Y, Hashimoto Y, Kasama T.
  TITLE     Purification and characterization of an
            endo-beta-(1--&gt;6)-galactanase from Trichoderma viride.
  JOURNAL   Carbohydr. Res. 338 (2003) 219-30.
REFERENCE   3  [PMID:14565843]
  AUTHORS   Kotake T, Kaneko S, Kubomoto A, Haque MA, Kobayashi H, Tsumuraya Y.
  TITLE     Molecular cloning and expression in Escherichia coli of a
            Trichoderma viride endo-beta-(1--&gt;6)-galactanase gene.
  JOURNAL   Biochem. J. 377 (2004) 749-55.
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.1.164
            ExPASy - ENZYME nomenclature database: 3.2.1.164
            ExplorEnz - The Enzyme Database: 3.2.1.164
            ERGO genome analysis and discovery system: 3.2.1.164
            BRENDA, the Enzyme Database: 3.2.1.164
///
ENTRY       EC 3.2.1.-                  Enzyme
CLASS       Hydrolases;
            Glycosidases;
            Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds
REACTION    (1) D-Glucosamine + D-Glucosaminide <=> D-Glucosaminide + H2O
            [RN:R01966];
            (2) Pentosans + H2O <=> Pentosans + D-Xylose [RN:R04937];
            (3) Pentosans + H2O <=> Pentosans + L-Arabinose [RN:R04938];
            (4) D-Glucosamine + Chitosan(n) <=> Chitosan(n+1) + H2O [RN:R06225];
            (5) (+)-7-Isojasmonic acid CoA + H2O <=> CoA + (+)-7-Isojasmonic
            acid [RN:R07902]
SUBSTRATE   D-Glucosamine [CPD:C00329];
            D-Glucosaminide [CPD:C06023];
            Pentosans [CPD:C06016];
            H2O [CPD:C00001];
            Chitosan [GL:G10536]
PRODUCT     D-Glucosaminide [CPD:C06023];
            H2O [CPD:C00001];
            Pentosans [CPD:C06016];
            D-Xylose [CPD:C00181];
            L-Arabinose [CPD:C00259];
            Chitosan [GL:G10536]
///
ENTRY       EC 3.2.2.1                  Enzyme
NAME        purine nucleosidase;
            nucleosidase;
            purine beta-ribosidase;
            purine nucleoside hydrolase;
            purine ribonucleosidase;
            ribonucleoside hydrolase;
            nucleoside hydrolase;
            N-ribosyl purine ribohydrolase;
            nucleosidase g;
            N-D-ribosylpurine ribohydrolase;
            inosine-adenosine-guanosine preferring nucleoside hydrolase;
            purine-specific nucleoside N-ribohydrolase;
            IAG-nucleoside hydrolase;
            IAG-NH
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     purine-nucleoside ribohydrolase
REACTION    a purine nucleoside + H2O = D-ribose + a purine base [RN:R02341]
ALL_REAC    R02341 > R01245 R01677 R01770 R02143;
            (other) R01273
SUBSTRATE   purine nucleoside [CPD:C01736];
            H2O [CPD:C00001]
PRODUCT     D-ribose [CPD:C00121];
            purine base
COMMENT     The enzyme from the bacterium Ochrobactrum anthropi specifically
            catalyses the irreversible N-riboside hydrolysis of purine
            nucleosides. Pyrimidine nucleosides, purine and pyrimidine
            nucleotides, NAD+, NADP+ and nicotinaminde mononucleotide are not
            substrates [6].
REFERENCE   1  [PMID:12999785]
  AUTHORS   HEPPEL LA, HILMOE RJ.
  TITLE     [Phosphorolysis and hydrolysis of purine ribosides by enzymes from
            yeast.]
  JOURNAL   J. Biol. Chem. 198 (1952) 683-94.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2
  AUTHORS   Kalckar, H.M.
  TITLE     Biosynthetic aspects of nucleosides and nucleic acids.
  JOURNAL   Pubbl. Staz. Zool. (Napoli) (1951) 87-103.
REFERENCE   3
  AUTHORS   Takagi, Y. and Horecker, B.L.
  TITLE     Purification and properties of a bacterial riboside hydrolyase.
  JOURNAL   J. Biol. Chem. 225 (1956) 77-86.
  ORGANISM  Lactobacillus pentmus, Lactobacillus delbrueckii
REFERENCE   4
  AUTHORS   Tarr, H.L.A.
  TITLE     Fish muscle riboside hydrolases.
  JOURNAL   Biochem. J. 59 (1955) 386-391.
  ORGANISM  Ophiodon elonatus, Sebastodes sp.
REFERENCE   5  [PMID:8702965]
  AUTHORS   Parkin DW.
  TITLE     Purine-specific nucleoside N-ribohydrolase from Trypanosoma brucei
            brucei. Purification, specificity, and kinetic mechanism.
  JOURNAL   J. Biol. Chem. 271 (1996) 21713-9.
  ORGANISM  Trypanosoma brucei [GN:tbr]
REFERENCE   6  [PMID:11282633]
  AUTHORS   Ogawa J, Takeda S, Xie SX, Hatanaka H, Ashikari T, Amachi T, Shimizu
            S.
  TITLE     Purification, characterization, and gene cloning of purine
            nucleosidase from Ochrobactrum anthropi.
  JOURNAL   Appl. Environ. Microbiol. 67 (2001) 1783-7.
  ORGANISM  Ochrobactrum anthropi
REFERENCE   7  [PMID:11854281]
  AUTHORS   Versees W, Decanniere K, Van Holsbeke E, Devroede N, Steyaert J.
  TITLE     Enzyme-substrate interactions in the purine-specific nucleoside
            hydrolase from Trypanosoma vivax.
  JOURNAL   J. Biol. Chem. 277 (2002) 15938-46.
  ORGANISM  Trypanosoma vivax
REFERENCE   8  [PMID:15909995]
  AUTHORS   Mazumder-Shivakumar D, Bruice TC.
  TITLE     Computational study of IAG-nucleoside hydrolase: determination of
            the preferred ground state conformation and the role of active site
            residues.
  JOURNAL   Biochemistry. 44 (2005) 7805-17.
  ORGANISM  Trypanosoma vivax
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K01239  purine nucleosidase
GENES       XLA: 379157(MGC52875)
            SPO: SPBC1683.06c
            DDI: DDB_0231227(iunH)
            TET: TTHERM_00666430 TTHERM_00766410
            TBR: Tb927.3.2960 Tb927.7.4570
            TCR: 508153.640 510315.10
            LMA: LmjF29.2800
            EHI: 42.t00042
            ECO: b0030(rihC)
            ECJ: JW0028(rihC)
            ECE: Z0035(yaaF)
            ECS: ECs0033
            ECI: UTI89_C0032(yaaF)
            ECP: ECP_0028
            ECV: APECO1_1953(rihC)
            STY: STY0060(yaaF)
            STT: t0053(yaaF)
            SPT: SPA0052(yaaF)
            SEC: SC0045(rihC)
            STM: STM0051(rihC)
            SFL: SF0027(yaaF)
            SFX: S0029(yaaF)
            SFV: SFV_0024(yaaF)
            SSN: SSON_0035(yaaF)
            SBO: SBO_0029(yaaF)
            SDY: SDY_0052(yaaF)
            ECA: ECA4423
            PLU: plu4289(iunH)
            ENT: Ent638_1178
            KPN: KPN_00025(rihC)
            SPE: Spro_4396
            PMU: PM1767(iunH)
            XCC: XCC3237
            XCB: XC_0946
            XCV: XCV3507(iunH)
            XAC: XAC3390
            XOO: XOO1152
            XOM: XOO_1049(XOO1049)
            PAE: PA0143
            PAU: PA14_01760(nuh)
            PPU: PP_2460
            PST: PSPTO_2373
            PSB: Psyr_2157
            PSP: PSPPH_2131 PSPPH_2471
            PFL: PFL_2107
            PFO: Pfl_1925
            PEN: PSEEN1958
            ACI: ACIAD2386(iunH)
            SDN: Sden_0940
            SFR: Sfri_4026
            SBL: Sbal_0660
            SBM: Shew185_3647
            SLO: Shew_0697
            SPC: Sputcn32_3178
            SSE: Ssed_1049
            SHE: Shewmr4_3306
            SHM: Shewmr7_0647
            SHN: Shewana3_3476
            SHW: Sputw3181_0765
            AHA: AHA_1466
            ASA: ASA_2899
            RSO: RSc2548(RS00727)
            BUR: Bcep18194_B0386
            BCN: Bcen_3104
            BCH: Bcen2424_5263
            BAM: Bamb_4624
            DDE: Dde_0760
            MLO: mll3190 mlr2009
            SME: SMc01105
            ATU: Atu0374(iunH)
            ATC: AGR_C_654
            RET: RHE_CH00366(iunH1)
            RLE: RL0383(iunH) RL2825 RL3882(iunH) pRL120178
            BME: BMEII0088
            BMF: BAB2_0005
            BMS: BRA0006(iunH)
            BMB: BruAb2_0006(iunH)
            BOV: BOV_A0003(iunH)
            SIL: SPO2470(iunH)
            SIT: TM1040_0934
            RSP: RSP_2914
            RSH: Rsph17029_1558
            RSQ: Rsph17025_1107
            JAN: Jann_1804
            RDE: RD1_3134
            PDE: Pden_4001
            GOX: GOX0947
            GBE: GbCGDNIH1_1340
            BAN: BA2400 BA2888 BA3606 BA5338
            BAR: GBAA2400 GBAA2888 GBAA3606 GBAA5338
            BAA: BA_0199 BA_2897 BA_3408 BA_4098
            BAT: BAS2236 BAS2693 BAS4961
            BCE: BC2331 BC2683 BC2889 BC3552 BC5134
            BCA: BCE_2927 BCE_3566
            BCZ: BCZK2156(iunH) BCZK2619(iunH) BCZK3260 BCZK4823
            BTK: BT9727_2170(iunH) BT9727_2642(iunH) BT9727_3310 BT9727_4813
            BTL: BALH_2595(iunH) BALH_3191(iunH) BALH_4626(iunH)
            BLI: BL02627
            BLD: BLi00740
            BCL: ABC3205 ABC3550 ABC3998
            BPU: BPUM_0649 BPUM_3604
            SAB: SAB2155c
            SAJ: SaurJH9_0228
            SAH: SaurJH1_0234
            SEP: SE0755
            SER: SERP0642
            SHA: SH1905
            SSP: SSP1735
            SAG: SAG0528
            SAN: gbs0574
            SAK: SAK_0679
            SMU: SMU.1865(mutY)
            LPL: lp_0363 lp_2591 lp_2825
            LJO: LJ0799
            LAC: LBA0591(iunH) LBA0865
            LSA: LSA0252(iunH1) LSA0533(iunH2) LSA0830(iunH3)
            LSL: LSL_0819(uRH) LSL_1528(uRH)
            LDB: Ldb0532 Ldb0815
            LBU: LBUL_0473 LBUL_0745
            LBR: LVIS_0403 LVIS_1816 LVIS_2069
            LGA: LGAS_0558
            LRE: Lreu_0877
            PPE: PEPE_0161
            EFA: EF1921 EF2587
            OOE: OEOE_0154 OEOE_1461
            LME: LEUM_0797
            CPF: CPF_2260
            CPR: CPR_1971
            CTC: CTC00577
            CDF: CD1682(iunH)
            DSY: DSY3527
            CGL: NCgl1309(cgl1364) NCgl2736(cgl2835)
            CGB: cg1543(iunH3) cg3137(iunH1)
            CGT: cgR_1429
            CEF: CE1482
            CDI: DIP1753(iunH)
            CJK: jk0233(iunH1) jk2078(iunH2)
            RHA: RHA1_ro00276 RHA1_ro07236(iunH)
            ART: Arth_0081
            PAC: PPA2076
            TFU: Tfu_2581
            SEN: SACE_0339 SACE_3233
            BLO: BL1770
            BAD: BAD_1486(iunH2)
            RBA: RB417(iunH)
            CYA: CYA_1903
            CYB: CYB_0491
            ANA: alr3202 alr3285
            AVA: Ava_3071 Ava_3900 Ava_4938
            TER: Tery_3465
            DRA: DR_0403
            DGE: Dgeo_1652
            HMA: rrnAC0226(iunH2) rrnAC0987(mutY)
            HWA: HQ2498A(iunH)
            SSO: SSO0505(iunH-1) SSO2243(iunH-2)
            STO: ST0803 ST2115
            SAI: Saci_0047 Saci_1187(iunH)
STRUCTURES  PDB: 1EZR  1HOZ  1HP0  1KIC  1KIE  1MAS  1R4F  2C40  2FF1  2FF2  
                 2MAS  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.1
            ExPASy - ENZYME nomenclature database: 3.2.2.1
            ExplorEnz - The Enzyme Database: 3.2.2.1
            ERGO genome analysis and discovery system: 3.2.2.1
            BRENDA, the Enzyme Database: 3.2.2.1
            CAS: 9025-44-9
///
ENTRY       EC 3.2.2.2                  Enzyme
NAME        inosine nucleosidase;
            inosinase;
            inosine-guanosine nucleosidase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     inosine ribohydrolase
REACTION    inosine + H2O = D-ribose + hypoxanthine [RN:R01770]
ALL_REAC    R01770
SUBSTRATE   inosine [CPD:C00294];
            H2O [CPD:C00001]
PRODUCT     D-ribose [CPD:C00121];
            hypoxanthine [CPD:C00262]
REFERENCE   1  [PMID:13376622]
  AUTHORS   KOCH AL.
  TITLE     Some enzymes of nucleoside metabolism of Escherichia coli.
  JOURNAL   J. Biol. Chem. 223 (1956) 535-49.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Tarr, H.L.A.
  TITLE     Fish muscle riboside hydrolases.
  JOURNAL   Biochem. J. 59 (1955) 386-391.
PATHWAY     PATH: map00230  Purine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.2
            ExPASy - ENZYME nomenclature database: 3.2.2.2
            ExplorEnz - The Enzyme Database: 3.2.2.2
            ERGO genome analysis and discovery system: 3.2.2.2
            BRENDA, the Enzyme Database: 3.2.2.2
            CAS: 9030-95-9
///
ENTRY       EC 3.2.2.3                  Enzyme
NAME        uridine nucleosidase;
            uridine hydrolase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     uridine ribohydrolase
REACTION    uridine + H2O = D-ribose + uracil [RN:R01080]
ALL_REAC    R01080
SUBSTRATE   uridine [CPD:C00299];
            H2O [CPD:C00001]
PRODUCT     D-ribose [CPD:C00121];
            uracil [CPD:C00106]
REFERENCE   1
  AUTHORS   Carter, C.E.
  TITLE     Partial purification of a non-phosphorylytic uridine nucleosidase
            from yeast.
  JOURNAL   J. Am. Chem. Soc. 73 (1951) 1508-1510.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K01240  uridine nucleosidase
GENES       PIC: PICST_60105(URH1)
            TBR: Tb10.61.2910
            TCR: 511277.330
            LMA: LmjF18.0480
            LPL: lp_3615
STRUCTURES  PDB: 1EMH  1EMJ  1EUG  1FLZ  1OKB  1SSP  1UDG  1UDH  1UDI  1UGH  
                 1UUG  1YUO  2BOO  2C53  2C56  2EUG  2J8X  2SSP  2UUG  3EUG  
                 4EUG  4SKN  5EUG  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.3
            ExPASy - ENZYME nomenclature database: 3.2.2.3
            ExplorEnz - The Enzyme Database: 3.2.2.3
            ERGO genome analysis and discovery system: 3.2.2.3
            BRENDA, the Enzyme Database: 3.2.2.3
            CAS: 9025-47-2
///
ENTRY       EC 3.2.2.4                  Enzyme
NAME        AMP nucleosidase;
            adenylate nucleosidase;
            adenosine monophosphate nucleosidase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     AMP phosphoribohydrolase
REACTION    AMP + H2O = D-ribose 5-phosphate + adenine [RN:R00182]
ALL_REAC    R00182
SUBSTRATE   AMP [CPD:C00020];
            H2O [CPD:C00001]
PRODUCT     D-ribose 5-phosphate [CPD:C00117];
            adenine [CPD:C00147]
REFERENCE   1
  AUTHORS   Hurwitz, J., Heppel, L.A. and Horecker, B.L.
  TITLE     The enzymatic cleavage of adenylic acid to adenine and ribose
            5-phosphate.
  JOURNAL   J. Biol. Chem. 226 (1957) 525-540.
  ORGANISM  Azotobacter vinelandii
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01241  AMP nucleosidase
GENES       ECO: b1982(amn)
            ECJ: JW1963(amn)
            ECE: Z3139(amn)
            ECS: ECs2779
            ECC: c2444(amn)
            ECI: UTI89_C2195(amn)
            ECP: ECP_1955
            ECV: APECO1_1068(amn)
            ECW: EcE24377A_2264(amn)
            ECX: EcHS_A2105
            STY: STY2211(amn)
            STT: t0868(amn)
            SPT: SPA0864(amn)
            SEC: SC2017(amn)
            STM: STM2009(amn)
            YPE: YPO2288(amn)
            YPK: y2119(amn)
            YPM: YP_2074(amn)
            YPA: YPA_1637
            YPN: YPN_1749
            YPP: YPDSF_0855
            YPS: YPTB2211(amn)
            YPI: YpsIP31758_1846(amn)
            SFL: SF2053(amn)
            SFX: S2160(amn)
            SFV: SFV_2053(amn)
            SSN: SSON_2047(amn)
            SDY: SDY_2253(amn)
            ECA: ECA1547(amn)
            ENT: Ent638_2572
            SPE: Spro_3127
            PAE: PA3970(amn)
            PAU: PA14_12490
            PAP: PSPA7_1138(amn)
            PPU: PP_4779
            PPF: Pput_4655
            PST: PSPTO_4795
            PSB: Psyr_4337
            PSP: PSPPH_4379(amn)
            PFL: PFL_5424(amn)
            PFO: Pfl_4942
            PEN: PSEEN4799(amn)
            PMY: Pmen_3750
            RSO: RSp0214(amn)
            REU: Reut_B5425
            REH: H16_B0070(amn)
            RME: Rmet_5885
            BMA: BMAA0309(amn)
            BMV: BMASAVP1_1489(amn)
            BML: BMA10299_1685(amn)
            BMN: BMA10247_A0341(amn)
            BXE: Bxe_B2838
            BVI: Bcep1808_4245
            BUR: Bcep18194_B2227
            BCN: Bcen_4496
            BCH: Bcen2424_3869
            BAM: Bamb_3237
            BPS: BPSS1777(amn)
            BPM: BURPS1710b_A0857(amn)
            BPL: BURPS1106A_A2416(amn)
            BPD: BURPS668_A2553(amn)
            BTE: BTH_II0602(amn)
            BPE: BP1583(amn)
            BPA: BPP3000(amn)
            BBR: BB2966(amn)
            RFR: Rfer_3569
            POL: Bpro_0642
            PNA: Pnap_3545
            AAV: Aave_4246
            AJS: Ajs_3709
            VEI: Veis_1155
            MPT: Mpe_A3401
            AZO: azo0116(amn)
            PCA: Pcar_2626
            BBA: Bd1233(amn)
            MLO: mll7714
            MES: Meso_0916
            SME: SMc02386(amn)
            SMD: Smed_0658
            ATU: Atu1006(amn)
            ATC: AGR_C_1849
            RET: RHE_CH01327(amn)
            RLE: RL1478(amn)
            BME: BMEI1318
            BMF: BAB1_0647(amn)
            BMS: BR0623(amn)
            BMB: BruAb1_0642(amn)
            BOV: BOV_0622(amn)
            OAN: Oant_2656
            BJA: bll7912(amn)
            BRA: BRADO2347(amn)
            BBT: BBta_2704(amn)
            NHA: Nham_0980
            CCR: CC_0264
            SIL: SPO3745(amn)
            SIT: TM1040_2800
            RSP: RSP_1387
            RSH: Rsph17029_0054
            RSQ: Rsph17025_2794
            JAN: Jann_0337
            RDE: RD1_0604(amn)
            PDE: Pden_0404
            MMR: Mmar10_0408
            HNE: HNE_1294(amn)
            NAR: Saro_1413
            SAL: Sala_0167
            SWI: Swit_2669
            ELI: ELI_07375
            CGL: NCgl0094(cgl0095)
            CGB: cg0124(amn)
            CEF: CE0099
            CTR: CT751(amn)
            CTA: CTA_0820(amn)
            CMU: TC0132
            CPN: CPn0894(amn)
            CPA: CP0972
            CPJ: CPj0894(amn)
            CPT: CpB0925
            CCA: CCA00874
            CAB: CAB840
            CFE: CF0142(amn)
            BFR: BF2395
            CHU: CHU_1998(amn)
STRUCTURES  PDB: 1T8R  1T8S  1T8W  1T8Y  2GUW  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.4
            ExPASy - ENZYME nomenclature database: 3.2.2.4
            ExplorEnz - The Enzyme Database: 3.2.2.4
            ERGO genome analysis and discovery system: 3.2.2.4
            BRENDA, the Enzyme Database: 3.2.2.4
            CAS: 9025-45-0
///
ENTRY       EC 3.2.2.5                  Enzyme
NAME        NAD+ nucleosidase;
            NADase;
            DPNase;
            DPN hydrolase;
            NAD hydrolase;
            diphosphopyridine nucleosidase;
            nicotinamide adenine dinucleotide nucleosidase;
            NAD glycohydrolase;
            NAD nucleosidase;
            nicotinamide adenine dinucleotide glycohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     NAD+ glycohydrolase
REACTION    NAD+ + H2O = ADP-ribose + nicotinamide [RN:R00102]
ALL_REAC    R00102;
            (other) R00119
SUBSTRATE   NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     ADP-ribose [CPD:C00301];
            nicotinamide [CPD:C00153]
COMMENT     This enzyme can also hydrolyse NADP+ to yield phospho-ADP-ribose and
            nicotinamide, but more slowly.
REFERENCE   1  [PMID:13276383]
  AUTHORS   HOFMANN EC, RAPOPORT S.
  TITLE     [DPN- and TPN-specific nucleosidases in erythrocytes.]
  JOURNAL   Biochim. Biophys. Acta. 18 (1955) 296.
REFERENCE   2  [PMID:5672131]
  AUTHORS   Nakazawa K, Ueda K, Honjo T, Yoshihara K, Nishizuka Y, Hayaishi O.
  TITLE     Nicotinamide adenine dinucleotide glycohydrolases and poly adenosine
            diphosphate ribose synthesis in rat liver.
  JOURNAL   Biochem. Biophys. Res. Commun. 32 (1968) 143-9.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:240831]
  AUTHORS   Ueda K, Fukushima M, Okayama H, Hayaishi O.
  TITLE     Nicotinamide adenine dinucleotide glycohydrolase from rat liver
            nuclei. Isolation and characterization of a new enzyme.
  JOURNAL   J. Biol. Chem. 250 (1975) 7541-6.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:11866528]
  AUTHORS   Yamamoto-Katayama S, Ariyoshi M, Ishihara K, Hirano T, Jingami H,
            Morikawa K.
  TITLE     Crystallographic studies on human BST-1/CD157 with ADP-ribosyl
            cyclase and NAD glycohydrolase activities.
  JOURNAL   J. Mol. Biol. 316 (2002) 711-23.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
            PATH: map04020  Calcium signaling pathway
ORTHOLOGY   KO: K01242  NAD+ nucleosidase
GENES       HSA: 683(BST1) 952(CD38)
            PTR: 461126(BST1) 745433(CD38)
            MMU: 12182(Bst1) 12494(Cd38)
            RNO: 25668(Cd38) 81506(Bst1)
            CFA: 403756(CD38) 488820(BST1)
            BTA: 327677(CD38) 616757(LOC616757)
            GGA: 422827(CD38) 422828(BST1)
            XTR: 496666(LOC496666)
            SPU: 580868(LOC580868)
            SPZ: M5005_Spy_0139(nga)
            SPH: MGAS10270_Spy0141(nga)
            SPI: MGAS10750_Spy0145(nga)
            SPJ: MGAS2096_Spy0146(nga)
            SPK: MGAS9429_Spy0141(nga)
            SPF: SpyM50134(nga)
            SPA: M6_Spy0186
            SPB: M28_Spy0137(nga)
STRUCTURES  PDB: 1ISF  1ISG  1ISH  1ISI  1ISJ  1ISM  1LBE  1R0S  1R12  1R15  
                 1R16  1YH3  1ZVM  2EF1  2HCT  2I65  2I66  2I67  2O3Q  2O3R  
                 2O3S  2O3T  2O3U  2PGJ  2PGL  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.5
            ExPASy - ENZYME nomenclature database: 3.2.2.5
            ExplorEnz - The Enzyme Database: 3.2.2.5
            ERGO genome analysis and discovery system: 3.2.2.5
            BRENDA, the Enzyme Database: 3.2.2.5
            CAS: 9032-65-9
///
ENTRY       EC 3.2.2.6                  Enzyme
NAME        NAD(P)+ nucleosidase;
            nicotinamide adenine dinucleotide (phosphate) nucleosidase;
            triphosphopyridine nucleotidase;
            NAD(P) nucleosidase;
            NAD(P)ase;
            nicotinamide adenine dinucleotide (phosphate) glycohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     NAD(P)+ glycohydrolase
REACTION    NAD(P)+ + H2O = ADP-ribose(P) + nicotinamide [RN:R00102 R00119]
ALL_REAC    R00102 R00119
SUBSTRATE   NAD+ [CPD:C00003];
            NADP+ [CPD:C00006];
            H2O [CPD:C00001]
PRODUCT     ADP-ribose [CPD:C00301];
            nicotinamide [CPD:C00153]
COMMENT     Also catalyses transfer of ADP-ribose(P) residues.
REFERENCE   1  [PMID:13319302]
  AUTHORS   ALIVISATOS SG, WOOLLEY DW.
  TITLE     Solubilization and purification of the diphosphopyridine
            nucleotidase from beef spleen.
  JOURNAL   J. Biol. Chem. 219 (1956) 823-32.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:13034774]
  AUTHORS   ZATMAN LJ, KAPLAN NO, COLOWICK SP.
  TITLE     Inhibition of spleen diphosphopyridine nucleotidase by nicotinamide,
            an exchange reaction.
  JOURNAL   J. Biol. Chem. 200 (1953) 197-212.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   3
  AUTHORS   Zatman, L.J., Kaplan, N.O., Colowick, S.P. and Ciotti, M.M.
  TITLE     Formation of the isonicotinic acid hydrazide analog of DPN.
  JOURNAL   J. Am. Chem. Soc. 75 (1953) 3293-3294.
  ORGANISM  Neurospora crassa [GN:dncr]
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.6
            ExPASy - ENZYME nomenclature database: 3.2.2.6
            ExplorEnz - The Enzyme Database: 3.2.2.6
            ERGO genome analysis and discovery system: 3.2.2.6
            BRENDA, the Enzyme Database: 3.2.2.6
            CAS: 9025-46-1
///
ENTRY       EC 3.2.2.7                  Enzyme
NAME        adenosine nucleosidase;
            adenosinase;
            N-ribosyladenine ribohydrolase;
            adenosine hydrolase;
            ANase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     adenosine ribohydrolase
REACTION    adenosine + H2O = D-ribose + adenine [RN:R01245]
ALL_REAC    R01245
SUBSTRATE   adenosine [CPD:C00212];
            H2O [CPD:C00001]
PRODUCT     D-ribose [CPD:C00121];
            adenine [CPD:C00147]
COMMENT     Also acts on adenosine N-oxide.
REFERENCE   1  [PMID:14085386]
  AUTHORS   MAZELIS M, CREVELING RK.
  TITLE     AN ADENOSINE HYDROLASE FROM BRUSSELS SPROUTS.
  JOURNAL   J. Biol. Chem. 238 (1963) 3358-61.
  ORGANISM  brussels sprouts
PATHWAY     PATH: map00230  Purine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.7
            ExPASy - ENZYME nomenclature database: 3.2.2.7
            ExplorEnz - The Enzyme Database: 3.2.2.7
            ERGO genome analysis and discovery system: 3.2.2.7
            BRENDA, the Enzyme Database: 3.2.2.7
            CAS: 9075-41-6
///
ENTRY       EC 3.2.2.8                  Enzyme
NAME        ribosylpyrimidine nucleosidase;
            N-ribosylpyrimidine nucleosidase;
            pyrimidine nucleosidase;
            N-ribosylpyrimidine ribohydrolase;
            pyrimidine nucleoside hydrolase;
            RihB;
            YeiK;
            nucleoside ribohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     pyrimidine-nucleoside ribohydrolase
REACTION    a pyrimidine nucleoside + H2O = D-ribose + a pyrimidine base
            [RN:R02172]
ALL_REAC    R02172 > R02137;
            (other) R01245 R01677 R01770
SUBSTRATE   pyrimidine nucleoside [CPD:C03169];
            H2O [CPD:C00001]
PRODUCT     D-ribose [CPD:C00121];
            pyrimidine base [CPD:C00396]
COMMENT     Also hydrolyses purine D-ribonucleosides, but much more slowly. 2'-,
            3'- and 5'-deoxynucleosides are not substrates [3].
REFERENCE   1  [PMID:12325375]
  AUTHORS   Terada M, Tatibana M, Hayaishi O.
  TITLE     Purification and properties of nucleoside hydrolase from Pseudomonas
            fluorescens.
  JOURNAL   J. Biol. Chem. 242 (1967) 5578-85.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   2  [PMID:11027694]
  AUTHORS   Petersen C, Moller LB.
  TITLE     The RihA, RihB, and RihC ribonucleoside hydrolases of Escherichia
            coli. Substrate specificity, gene expression, and regulation.
  JOURNAL   J. Biol. Chem. 276 (2001) 884-94.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:14993681]
  AUTHORS   Giabbai B, Degano M.
  TITLE     Cloning, purification, crystallization and X-ray analysis of the
            Escherichia coli pyrimidine nucleoside hydrolase YeiK.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 60 (2004) 524-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:15130467]
  AUTHORS   Giabbai B, Degano M.
  TITLE     Crystal structure to 1.7 a of the Escherichia coli pyrimidine
            nucleoside hydrolase YeiK, a novel candidate for cancer gene
            therapy.
  JOURNAL   Structure. 12 (2004) 739-49.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K10213  ribosylpyrimidine nucleosidase
GENES       ECO: b2162(rihB)
            ECJ: JW2149(rihB)
            ECE: Z3419(yeiK)
            ECS: ECs3054
            ECC: c2696(yeiK)
            ECI: UTI89_C2436(yeiK)
            ECP: ECP_2202
            ECV: APECO1_43912(rihB)
            SFL: SF2247(yeiK)
            SFX: S2376(yeiK)
            SFV: SFV_2237(yeiK)
            SSN: SSON_2218(yeiK)
            SBO: SBO_2165(yeiK)
            SDY: SDY_2104(yeiK)
            LBR: LVIS_2188
STRUCTURES  PDB: 1Q8F  1YOE  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.8
            ExPASy - ENZYME nomenclature database: 3.2.2.8
            ExplorEnz - The Enzyme Database: 3.2.2.8
            ERGO genome analysis and discovery system: 3.2.2.8
            BRENDA, the Enzyme Database: 3.2.2.8
            CAS: 37288-60-1
///
ENTRY       EC 3.2.2.9                  Enzyme
NAME        adenosylhomocysteine nucleosidase;
            S-adenosylhomocysteine hydrolase (ambiguous);
            S-adenosylhomocysteine nucleosidase;
            5'-methyladenosine nucleosidase;
            S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase;
            AdoHcy/MTA nucleosidase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     S-adenosyl-L-homocysteine homocysteinylribohydrolase
REACTION    S-adenosyl-L-homocysteine + H2O =
            S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine [RN:R00194]
ALL_REAC    R00194;
            (other) R01401
SUBSTRATE   S-adenosyl-L-homocysteine [CPD:C00021];
            H2O [CPD:C00001]
PRODUCT     S-(5-deoxy-D-ribos-5-yl)-L-homocysteine [CPD:C03539];
            adenine [CPD:C00147]
COMMENT     Also acts on S-methyl-5'-thioadenosine to give adenine and
            S-methyl-5-thioribose (cf. EC 3.2.2.16, methylthioadenosine
            nucleosidase).
REFERENCE   1
  AUTHORS   Duerre, J.A.
  TITLE     A hydrolytic nucleosidase acting on S-adenosylhomocysteine and on
            5-methylthioadenosine.
  JOURNAL   J. Biol. Chem. 237 (1962) 3737-3741.
  ORGANISM  Aerobacter aerogenes
REFERENCE   2  [PMID:782530]
  AUTHORS   Ferro AJ, Barrett A, Shapiro SK.
  TITLE     Kinetic properties and the effect of substrate analogues on
            5'-methylthioadenosine nucleosidase from Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 438 (1976) 487-94.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K01243  S-adenosylhomocysteine nucleosidase
GENES       TET: TTHERM_00085560
            EHI: 91.t00029
            ECO: b0159(pfs)
            ECJ: JW0155(pfs)
            ECE: Z0170(pfs)
            ECS: ECs0163
            ECC: c0195(pfs)
            ECI: UTI89_C0175(mtn)
            ECP: ECP_0169
            ECV: APECO1_1826
            ECW: EcE24377A_0164(mtnN)
            ECX: EcHS_A0163
            STY: STY0229(pfs)
            STT: t0208(mtn)
            SPT: SPA0213(mtn)
            SEC: SC0207(pfs)
            STM: STM0207(pfs)
            YPE: YPO3384(mtn)
            YPK: y0805(pfs)
            YPM: YP_0301(mtn)
            YPA: YPA_2883
            YPN: YPN_0707
            YPS: YPTB0747(mtn)
            YPI: YpsIP31758_3325(mtnN)
            SFL: SF0151(pfs)
            SFX: S0154(pfs)
            SFV: SFV_0144(pfs)
            SSN: SSON_0171(pfs)
            SBO: SBO_0148(pfs)
            SDY: SDY_0175(pfs)
            ECA: ECA3303(mtn)
            PLU: plu0906(mtnA)
            BUC: BU210(pfs)
            BAS: BUsg204(pfs)
            BAB: bbp192(pfs)
            WBR: WGLp436(pfs)
            SGL: SG0503
            SPE: Spro_0787
            HIN: HI1216(pfs)
            HIT: NTHI1389(mtnA)
            HIP: CGSHiEE_05975
            HIQ: CGSHiGG_09830
            HDU: HD1898(mtn)
            HSO: HS_1473(pfs)
            PMU: PM0194(pfs)
            MSU: MS1537(pfs)
            APL: APL_1637(mtn)
            ASU: Asuc_1510
            VCH: VC2379
            VVU: VV1_0558
            VVY: VV0635
            VPA: VP0479 VPA1089
            VFI: VF2128
            PPR: PBPRA0538(pfs)
            PPU: PP_3254
            ACI: ACIAD0773
            SON: SO_1322(pfs)
            SDN: Sden_2801
            SFR: Sfri_2966
            SAZ: Sama_0855
            SBL: Sbal_1176
            SBM: Shew185_1220
            SPC: Sputcn32_1134
            SSE: Ssed_1115
            SPL: Spea_1001
            SHM: Shewmr7_2956
            SHN: Shewana3_3052
            SHW: Sputw3181_3030
            CPS: CPS_4743
            PHA: PSHAa0547(mtnN)
            PAT: Patl_0518
            FTU: FTT0397(mtn)
            FTF: FTF0397(mtn)
            FTW: FTW_1677(mtnN)
            FTL: FTL_0463
            FTH: FTH_0460
            FTA: FTA_0491(mtnN)
            FTN: FTN_0493(mtn)
            TCX: Tcr_2130
            CSA: Csal_2050
            MMW: Mmwyl1_4313
            AHA: AHA_0953(mtnN-1) AHA_1706(mtnN-2)
            BCI: BCI_0224(pfs)
            NME: NMB0767
            NMA: NMA0978(pfs)
            NMC: NMC0720(pfs)
            NGO: NGO0345
            RSO: RSc3374(pfs)
            REU: Reut_A3041
            REH: H16_A3337(pfs)
            RME: Rmet_3198
            BMA: BMA0929
            BMV: BMASAVP1_A1462(mtnN)
            BML: BMA10299_A0420(mtnN)
            BMN: BMA10247_0743(mtnN)
            BPS: BPSL1978
            BPM: BURPS1710b_1848(mtnN)
            BPL: BURPS1106A_1693(mtnN)
            BPD: BURPS668_1671(mtnN)
            BTE: BTH_I2631
            BPA: BPP0208
            BBR: BB0212
            PNA: Pnap_3796
            MPT: Mpe_A3574
            HAR: HEAR3422(mtnN)
            NET: Neut_1886
            HPY: HP0089(pfs)
            HPJ: jhp0082
            HPA: HPAG1_0090
            HHE: HH1283
            HAC: Hac_1516
            WSU: WS0528(pfs)
            TDN: Tmden_1392
            CJE: Cj0117(pfs)
            CJR: CJE0112(mtnA)
            CJJ: CJJ81176_0152(mtnA)
            CJU: C8J_0110(pfs)
            CJD: JJD26997_0124(mtnA)
            CFF: CFF8240_1515(mtnN)
            CCV: CCV52592_1748(mtnN) CCV52592_1786
            CHA: CHAB381_0698(mtnN)
            CCO: CCC13826_0092 CCC13826_0927(mtnN)
            ABU: Abu_1585(pfs)
            NIS: NIS_1209(pfs)
            SUN: SUN_1755(pfs)
            GSU: GSU0453(pfs)
            PCA: Pcar_3117
            BBA: Bd0846 Bd2653(pfs)
            DPS: DP0328 DP0528 DP1546
            PUB: SAR11_1212(pfs)
            MLO: mlr6947
            MES: Meso_0494
            SME: SMc00395(pfs)
            ATU: Atu0282(pfs)
            ATC: AGR_C_482
            RET: RHE_CH00298(pfs)
            BME: BMEII0888
            BMF: BAB2_0843
            BMS: BRA0360
            BMB: BruAb2_0822
            NHA: Nham_3696
            CCR: CC_2266
            NAR: Saro_3294
            GBE: GbCGDNIH1_2407
            RRU: Rru_A0061
            ABA: Acid345_1742
            BSU: BG13800(yrrU)
            BHA: BH1279 BH3238(pfs)
            BAN: BA2564 BA4602
            BAR: GBAA2564 GBAA4602
            BAA: BA_3069 BA_5043
            BAT: BAS2388 BAS4270
            BCE: BC2503 BC4368
            BCA: BCE_2567 BCE_2638 BCE_4456
            BCZ: BCZK2305(pfs) BCZK2595 BCZK4118(mtnA)
            BCY: Bcer98_3086
            BTK: BT9727_1702(pfs) BT9727_2344(pfs) BT9727_2625(pfs)
                 BT9727_2626(pfs) BT9727_4107(mtnA)
            BTL: BALH_2989(mtn) BALH_3959(mtnN)
            BLI: BL02020(mtn)
            BLD: BLi02855(mtn)
            BCL: ABC1603(mthA)
            BAY: RBAM_024370
            BPU: BPUM_2362
            OIH: OB2000
            GKA: GK2542
            SAU: SA1427(pfs)
            SAV: SAV1599(pfs)
            SAM: MW1550(pfS)
            SAR: SAR1676(pfs)
            SAS: SAS1536
            SAC: SACOL1655(mtn)
            SAB: SAB1471c
            SAA: SAUSA300_1558(mtnN)
            SAO: SAOUHSC_01702
            SAJ: SaurJH9_1656
            SAH: SaurJH1_1691
            SEP: SE1285
            SER: SERP1166(mtn)
            SHA: SH1316(pfs)
            SSP: SSP1159
            LMO: lmo1494
            LMF: LMOf2365_1513
            LIN: lin1529
            LWE: lwe1507(pfs)
            LLA: L132777(pfs)
            LLC: LACR_2076
            LLM: llmg_2073(pfs)
            SPY: SPy_0447(pfs)
            SPZ: M5005_Spy_0365(pfs)
            SPM: spyM18_0490(pfs)
            SPG: SpyM3_0315(pfs)
            SPS: SPs1542
            SPH: MGAS10270_Spy0368(pfs)
            SPI: MGAS10750_Spy0367(pfs)
            SPJ: MGAS2096_Spy0384(pfs)
            SPK: MGAS9429_Spy0368(pfs)
            SPF: SpyM51500(mtn)
            SPA: M6_Spy0389
            SPB: M28_Spy0354(pfs)
            SPN: SP_0991
            SPR: spr0894(pfs)
            SPD: SPD_0877(mtnN)
            SAG: SAG1535(pfs)
            SAN: gbs1591
            SAK: SAK_1558(pfs)
            SMU: SMU.1632(pfs)
            STC: str0566(pfs)
            STL: stu0566(pfs)
            LPL: lp_2181(mtn)
            LJO: LJ0983
            LAC: LBA0820
            LSA: LSA0776(pfs)
            LSL: LSL_0859(pfs)
            LBU: LBUL_0685
            LBR: LVIS_1437
            LCA: LSEI_1288
            LRE: Lreu_0602
            PPE: PEPE_1175
            EFA: EF2694(pfs)
            CAC: CAC2117(pfs)
            CPE: CPE0056(mtn) CPE1050
            CPF: CPF_0063(mtnN) CPF_1305(mtnN)
            CPR: CPR_0066(mtnN)
            CTC: CTC01619
            CDF: CD2611(mtnN)
            CBO: CBO1471(mtn)
            CBA: CLB_1496(mtnN)
            CBH: CLC_1508(mtnN)
            CBF: CLI_1555(mtnN)
            CBE: Cbei_4917
            AMT: Amet_2799
            MPU: MYPU_3360(pfs)
            MPE: MYPE5210(pfs)
            MGA: MGA_0051(pfs)
            MMY: MSC_0443(pfs)
            MMO: MMOB2770(pfs)
            MHY: mhp473
            MHJ: MHJ_0472(pfs)
            MHP: MHP7448_0475(pfs)
            MCP: MCAP_0528
            MFL: Mfl372
            MTU: Rv0091(mtn)
            MTC: MT0100
            MBO: Mb0094(mtn)
            MBB: BCG_0124(mtn)
            MSM: MSMEG_1753(mtnN)
            CGL: NCgl2704(cgl2802)
            CGB: cg3102
            CEF: CE2636
            CDI: DIP2131
            PAC: PPA1093
            BLO: BL0318(pfs)
            FNU: FN1015
            BBU: BBI06(pfs)
            BAF: BAPKO_0384(pfs-1) BAPKO_0619(pfs-2)
            TPA: TP0170
            TDE: TDE0105
            SYW: SYNW0169(pfs)
            CYA: CYA_1636(mtnN)
            CYB: CYB_1283(mtnN)
            PMG: P9301_14421(pfs)
            PMH: P9215_14761
            BTH: BT_4451
            BFR: BF3598
            BFS: BF3401
            PGI: PG0497(mtn)
            SRU: SRU_1556(mtnN)
            CHU: CHU_2004(pfs)
            DRA: DR_1451
            DGE: Dgeo_0776
            TTH: TTC1185
            TTJ: TTHA1550
            TMA: TM1129
            TPT: Tpet_1616
            TME: Tmel_0485
            FNO: Fnod_0825
STRUCTURES  PDB: 1JYS  1NC1  1NC3  1Y6Q  1Y6R  1Z5N  1Z5O  1Z5P  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.9
            ExPASy - ENZYME nomenclature database: 3.2.2.9
            ExplorEnz - The Enzyme Database: 3.2.2.9
            ERGO genome analysis and discovery system: 3.2.2.9
            BRENDA, the Enzyme Database: 3.2.2.9
            CAS: 9055-10-1
///
ENTRY       EC 3.2.2.10                 Enzyme
NAME        pyrimidine-5'-nucleotide nucleosidase;
            pyrimidine nucleotide N-ribosidase;
            Pyr5N
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     pyrimidine-5'-nucleotide phosphoribo(deoxyribo)hydrolase
REACTION    a pyrimidine 5'-nucleotide + H2O = D-ribose 5-phosphate + a
            pyrimidine base [RN:R02171]
ALL_REAC    R02171 > R00510
SUBSTRATE   pyrimidine 5'-nucleotide [CPD:C03536];
            H2O [CPD:C00001]
PRODUCT     D-ribose 5-phosphate [CPD:C00117];
            pyrimidine base [CPD:C00396]
COMMENT     Also acts on dUMP, dTMP and dCMP.
REFERENCE   1
  AUTHORS   Imada, A.
  TITLE     Degradation of pyrimidine nucleotides by enzyme systems of
            Streptomyces. II. Pyrimidine 5'-nucleotide phosphoribo(deoxyribo)
            hydrolase of Streptomyces virginiae.
  JOURNAL   J. Gen. Appl. Microbiol. 13 (1967) 267-278.
  ORGANISM  Streptomyces virginiae
REFERENCE   2
  AUTHORS   Imada, A., Kuno, M. and Igarasi, S.
  TITLE     Degradation of pyrimidine nucleotides by enzyme systems of
            Streptomyces. I. Ribose-5-phosphate formation from pyrimidine
            nucleotides.
  JOURNAL   J. Gen. Appl. Microbiol. 13 (1967) 255-265.
  ORGANISM  Streptomyces sp.
PATHWAY     PATH: map00240  Pyrimidine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.10
            ExPASy - ENZYME nomenclature database: 3.2.2.10
            ExplorEnz - The Enzyme Database: 3.2.2.10
            ERGO genome analysis and discovery system: 3.2.2.10
            BRENDA, the Enzyme Database: 3.2.2.10
            CAS: 9023-31-8
///
ENTRY       EC 3.2.2.11                 Enzyme
NAME        beta-aspartyl-N-acetylglucosaminidase;
            beta-aspartylacetylglucosaminidase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     1-beta-aspartyl-N-acetyl-D-glucosaminylamine L-asparaginohydrolase
REACTION    1-beta-aspartyl-N-acetyl-D-glucosaminylamine + H2O = L-asparagine +
            N-acetyl-D-glucosamine [RN:R01266]
ALL_REAC    R01266
SUBSTRATE   1-beta-aspartyl-N-acetyl-D-glucosaminylamine [CPD:C04540];
            H2O [CPD:C00001]
PRODUCT     L-asparagine [CPD:C00152];
            N-acetyl-D-glucosamine [CPD:C00140]
REFERENCE   1
  AUTHORS   Eylar, E.H. and Murakami, M.
  TITLE     beta-Aspartyl-N-acetylglucosaminidase from epididymis.
  JOURNAL   Methods Enzymol. 8 (1966) 597-600.
  ORGANISM  sheep
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.11
            ExPASy - ENZYME nomenclature database: 3.2.2.11
            ExplorEnz - The Enzyme Database: 3.2.2.11
            ERGO genome analysis and discovery system: 3.2.2.11
            BRENDA, the Enzyme Database: 3.2.2.11
            CAS: 9027-31-0
///
ENTRY       EC 3.2.2.12                 Enzyme
NAME        inosinate nucleosidase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     5'-inosinate phosphoribohydrolase
REACTION    5'-inosinate + H2O = D-ribose 5-phosphate + hypoxanthine [RN:R01128]
ALL_REAC    R01128
SUBSTRATE   5'-inosinate [CPD:C00130];
            H2O [CPD:C00001]
PRODUCT     D-ribose 5-phosphate [CPD:C00117];
            hypoxanthine [CPD:C00262]
REFERENCE   1
  AUTHORS   Kuninaka, A.
  TITLE     5'-Inosinic acid-N-ribosidase in Aspergillus.
  JOURNAL   Koso Kagaka Shinojiumu 12 (1957) 65-69.
  ORGANISM  Aspergillus sp.
PATHWAY     PATH: map00230  Purine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.12
            ExPASy - ENZYME nomenclature database: 3.2.2.12
            ExplorEnz - The Enzyme Database: 3.2.2.12
            ERGO genome analysis and discovery system: 3.2.2.12
            BRENDA, the Enzyme Database: 3.2.2.12
            CAS: 37288-61-2
///
ENTRY       EC 3.2.2.13                 Enzyme
NAME        1-methyladenosine nucleosidase;
            1-methyladenosine hydrolase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     1-methyladenosine ribohydrolase
REACTION    1-methyladenosine + H2O = 1-methyladenine + D-ribose [RN:R03885]
ALL_REAC    R03885
SUBSTRATE   1-methyladenosine [CPD:C02494];
            H2O [CPD:C00001]
PRODUCT     1-methyladenine [CPD:C02216];
            D-ribose [CPD:C00121]
REFERENCE   1
  AUTHORS   Tarr, H.L.A.
  TITLE     1-Methyladenosine hydrolase of starfish (Pisaster ochraceous).
  JOURNAL   J. Fish Res. Board Can. 30 (1973) 1861-1866.
  ORGANISM  Pisaster ochraceous
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.13
            ExPASy - ENZYME nomenclature database: 3.2.2.13
            ExplorEnz - The Enzyme Database: 3.2.2.13
            ERGO genome analysis and discovery system: 3.2.2.13
            BRENDA, the Enzyme Database: 3.2.2.13
            CAS: 37367-71-8
///
ENTRY       EC 3.2.2.14                 Enzyme
NAME        NMN nucleosidase;
            NMNase;
            nicotinamide mononucleotide nucleosidase;
            nicotinamide mononucleotidase;
            NMN glycohydrolase;
            NMNGhase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     nicotinamide-nucleotide phosphoribohydrolase
REACTION    nicotinamide D-ribonucleotide + H2O = D-ribose 5-phosphate +
            nicotinamide [RN:R01270]
ALL_REAC    R01270
SUBSTRATE   nicotinamide D-ribonucleotide [CPD:C00455];
            H2O [CPD:C00001]
PRODUCT     D-ribose 5-phosphate [CPD:C00117];
            nicotinamide [CPD:C00153]
REFERENCE   1  [PMID:4342726]
  AUTHORS   Andreoli AJ, Okita TW, Bloom R, Grover TA.
  TITLE     The pyridine nucleotide cycle: presence of a nicotinamide
            mononucleotide-specific glycohydrolase in Escherichia coli.
  JOURNAL   Biochem. Biophys. Res. Commun. 49 (1972) 264-9.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.14
            ExPASy - ENZYME nomenclature database: 3.2.2.14
            ExplorEnz - The Enzyme Database: 3.2.2.14
            ERGO genome analysis and discovery system: 3.2.2.14
            BRENDA, the Enzyme Database: 3.2.2.14
            CAS: 37237-49-3
///
ENTRY       EC 3.2.2.15                 Enzyme
NAME        DNA-deoxyinosine glycosylase;
            DNA(hypoxanthine) glycohydrolase;
            deoxyribonucleic acid glycosylase;
            hypoxanthine-DNA glycosylase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     DNA-deoxyinosine deoxyribohydrolase
REACTION    Hydrolyses DNA and polynucleotides, releasing free hypoxanthine
REFERENCE   1  [PMID:98523]
  AUTHORS   Karran P, Lindahl T.
  TITLE     Enzymatic excision of free hypoxanthine from polydeoxynucleotides
            and DNA containing deoxyinosine monophosphate residues.
  JOURNAL   J. Biol. Chem. 253 (1978) 5877-9.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.15
            ExPASy - ENZYME nomenclature database: 3.2.2.15
            ExplorEnz - The Enzyme Database: 3.2.2.15
            ERGO genome analysis and discovery system: 3.2.2.15
            BRENDA, the Enzyme Database: 3.2.2.15
            CAS: 68247-62-1
///
ENTRY       EC 3.2.2.16                 Enzyme
NAME        methylthioadenosine nucleosidase;
            5'-methylthioadenosine nucleosidase;
            MTA nucleosidase;
            MeSAdo nucleosidase;
            methylthioadenosine methylthioribohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     S-methyl-5'-thioadenosine adeninehyrolase
REACTION    S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine
            [RN:R01401]
ALL_REAC    R01401
SUBSTRATE   S-methyl-5'-thioadenosine [CPD:C00170];
            H2O [CPD:C00001]
PRODUCT     S-methyl-5-thio-D-ribose [CPD:C03089];
            adenine [CPD:C00147]
COMMENT     Does not act on S-adenosylhomocysteine. cf. EC 3.2.2.9
            adenosylhomocysteine nucleosidase.
REFERENCE   1  [PMID:6783408]
  AUTHORS   Guranowski AB, Chiang PK, Cantoni GL.
  TITLE     5'-Methylthioadenosine nucleosidase. Purification and
            characterization of the enzyme from Lupinus luteus seeds.
  JOURNAL   Eur. J. Biochem. 114 (1981) 293-9.
  ORGANISM  Lupinus luteus
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K01244  5'-methylthioadenosine nucleosidase
GENES       ECO: b0159(pfs)
            ECJ: JW0155(pfs)
            ECE: Z0170(pfs)
            ECS: ECs0163
            ECC: c0195(pfs)
            ECI: UTI89_C0175(mtn)
            ECP: ECP_0169
            ECV: APECO1_1826
            ECW: EcE24377A_0164(mtnN)
            ECX: EcHS_A0163
            STY: STY0229(pfs)
            STT: t0208(mtn)
            SPT: SPA0213(mtn)
            SEC: SC0207(pfs)
            STM: STM0207(pfs)
            YPE: YPO3384(mtn)
            YPK: y0805(pfs)
            YPM: YP_0301(mtn)
            YPA: YPA_2883
            YPN: YPN_0707
            YPS: YPTB0747(mtn)
            YPI: YpsIP31758_3325(mtnN)
            SFL: SF0151(pfs)
            SFX: S0154(pfs)
            SFV: SFV_0144(pfs)
            SSN: SSON_0171(pfs)
            SBO: SBO_0148(pfs)
            SDY: SDY_0175(pfs)
            ECA: ECA3303(mtn)
            PLU: plu0906(mtnA)
            BUC: BU210(pfs)
            BAS: BUsg204(pfs)
            BAB: bbp192(pfs)
            WBR: WGLp436(pfs)
            SGL: SG0503
            HIN: HI1216(pfs)
            HIT: NTHI1389(mtnA)
            HDU: HD1898(mtn)
            HSO: HS_1473(pfs)
            PMU: PM0194(pfs)
            MSU: MS1537(pfs)
            APL: APL_1637(mtn)
            VCH: VC2379
            VVU: VV1_0558
            VVY: VV0635
            VPA: VP0479 VPA1089
            VFI: VF2128
            PPR: PBPRA0538(pfs)
            PPU: PP_3254
            ACI: ACIAD0773
            SON: SO_1322(pfs)
            SDN: Sden_2801
            SFR: Sfri_2966
            SLO: Shew_1027
            SHE: Shewmr4_2874
            SHM: Shewmr7_2956
            SHN: Shewana3_3052
            CPS: CPS_4743
            PHA: PSHAa0547(mtnN)
            PAT: Patl_0518
            PIN: Ping_0920
            FTU: FTT0397(mtn)
            FTF: FTF0397(mtn)
            FTW: FTW_1677(mtnN)
            FTL: FTL_0463
            FTH: FTH_0460
            FTA: FTA_0491(mtnN)
            FTN: FTN_0493(mtn)
            TCX: Tcr_2130
            NOC: Noc_1319
            AHA: AHA_0953(mtnN-1) AHA_1706(mtnN-2)
            BCI: BCI_0224(pfs)
            NME: NMB0767
            NMA: NMA0978(pfs)
            NMC: NMC0720(pfs)
            NGO: NGO0345
            RSO: RSc3374(pfs)
            REU: Reut_A3041
            RME: Rmet_3198
            BMA: BMA0929
            BMV: BMASAVP1_A1462(mtnN)
            BML: BMA10299_A0420(mtnN)
            BMN: BMA10247_0743(mtnN)
            BXE: Bxe_A1338
            BVI: Bcep1808_1405
            BUR: Bcep18194_A4587
            BCN: Bcen_0961
            BCH: Bcen2424_1443
            BAM: Bamb_1323
            BPS: BPSL1978
            BPM: BURPS1710b_1848(mtnN)
            BPL: BURPS1106A_1693(mtnN)
            BPD: BURPS668_1671(mtnN)
            BTE: BTH_I2631
            BPA: BPP0208
            BBR: BB0212
            POL: Bpro_4542
            AAV: Aave_4573
            AJS: Ajs_3949
            VEI: Veis_4426
            HAR: HEAR3422(mtnN)
            NET: Neut_1886
            HPY: HP0089(pfs)
            HPJ: jhp0082
            HPA: HPAG1_0090
            HHE: HH1283
            HAC: Hac_1516
            WSU: WS0528(pfs)
            TDN: Tmden_1392
            CJE: Cj0117(pfs)
            CJR: CJE0112(mtnA)
            CJJ: CJJ81176_0152(mtnA)
            CJU: C8J_0110(pfs)
            CJD: JJD26997_0124(mtnA)
            CFF: CFF8240_1515(mtnN)
            CCV: CCV52592_1748(mtnN)
            CHA: CHAB381_0698(mtnN)
            CCO: CCC13826_0927(mtnN)
            ABU: Abu_1585(pfs)
            NIS: NIS_1209(pfs)
            SUN: SUN_1755(pfs)
            GSU: GSU0453(pfs)
            PCA: Pcar_3117
            BBA: Bd0846 Bd2653(pfs)
            DPS: DP0328 DP0528 DP1546
            PUB: SAR11_1212(pfs)
            MLO: mlr6947
            MES: Meso_0494
            SME: SMc00395(pfs)
            ATU: Atu0282(pfs)
            ATC: AGR_C_482
            RET: RHE_CH00298(pfs)
            BME: BMEII0888
            BMF: BAB2_0843
            BMS: BRA0360
            BMB: BruAb2_0822
            NWI: Nwi_3067
            NHA: Nham_3696
            CCR: CC_2266
            NAR: Saro_3294
            GBE: GbCGDNIH1_2407
            ABA: Acid345_1742
            BSU: BG13800(yrrU)
            BHA: BH1279 BH3238(pfs)
            BAN: BA2564 BA4602
            BAR: GBAA2564 GBAA4602
            BAA: BA_3069 BA_5043
            BAT: BAS2388 BAS4270
            BCE: BC2503 BC4368
            BCA: BCE_2567 BCE_2638 BCE_4456
            BCZ: BCZK2305(pfs) BCZK2595 BCZK4118(mtnA)
            BTK: BT9727_2344(pfs) BT9727_2626(pfs) BT9727_4107(mtnA)
            BTL: BALH_2989(mtn) BALH_3959(mtnN)
            BLI: BL02020(mtn)
            BLD: BLi02855(mtn)
            BCL: ABC1603(mthA)
            OIH: OB2000
            GKA: GK2542
            SAU: SA1427(pfs)
            SAV: SAV1599(pfs)
            SAM: MW1550(pfS)
            SAR: SAR1676(pfs)
            SAS: SAS1536
            SAC: SACOL1655(mtn)
            SAB: SAB1471c
            SAA: SAUSA300_1558(mtnN)
            SAO: SAOUHSC_01702
            SEP: SE1285
            SER: SERP1166(mtn)
            SHA: SH1316(pfs)
            SSP: SSP1159
            LMO: lmo1494
            LMF: LMOf2365_1513
            LIN: lin1529
            LLA: L132777(pfs)
            LLC: LACR_2076
            SPY: SPy_0447(pfs)
            SPZ: M5005_Spy_0365(pfs)
            SPM: spyM18_0490(pfs)
            SPG: SpyM3_0315(pfs)
            SPS: SPs1542
            SPH: MGAS10270_Spy0368(pfs)
            SPI: MGAS10750_Spy0367(pfs)
            SPJ: MGAS2096_Spy0384(pfs)
            SPK: MGAS9429_Spy0368(pfs)
            SPA: M6_Spy0389
            SPB: M28_Spy0354(pfs)
            SPN: SP_0991
            SPR: spr0894(pfs)
            SPD: SPD_0877(mtnN)
            SAG: SAG1535(pfs)
            SAN: gbs1591
            SAK: SAK_1558(pfs)
            SMU: SMU.1632(pfs)
            STC: str0566(pfs)
            STL: stu0566(pfs)
            SSA: SSA_1639(pfs)
            LPL: lp_2181(mtn)
            LJO: LJ0983
            LAC: LBA0820
            LSA: LSA0776(pfs)
            LSL: LSL_0859(pfs)
            LDB: Ldb0752(pfs)
            LBU: LBUL_0685
            LBR: LVIS_1437
            LCA: LSEI_1288
            PPE: PEPE_1175
            EFA: EF2694(pfs)
            CAC: CAC2117(pfs)
            CPE: CPE0056(mtn) CPE1050
            CPF: CPF_0063(mtnN) CPF_1305(mtnN)
            CPR: CPR_0066(mtnN)
            CTC: CTC01619
            CDF: CD2611(mtnN)
            CBO: CBO1471(mtn)
            CBA: CLB_1496(mtnN)
            CBH: CLC_1508(mtnN)
            CBF: CLI_1555(mtnN)
            MPU: MYPU_3360(pfs)
            MPE: MYPE5210(pfs)
            MGA: MGA_0051(pfs)
            MMY: MSC_0443(pfs)
            MMO: MMOB2770(pfs)
            MHY: mhp473
            MHJ: MHJ_0472(pfs)
            MHP: MHP7448_0475(pfs)
            MCP: MCAP_0528
            MFL: Mfl372
            MTU: Rv0091(mtn)
            MTC: MT0100
            MBO: Mb0094(mtn)
            MBB: BCG_0124(mtn)
            MSM: MSMEG_1753(mtnN)
            CGL: NCgl2704(cgl2802)
            CGB: cg3102
            CEF: CE2636
            CDI: DIP2131
            PAC: PPA1093
            BLO: BL0318(pfs)
            FNU: FN1015
            BBU: BBI06(pfs)
            BAF: BAPKO_0384(pfs-1) BAPKO_0619(pfs-2)
            TPA: TP0170
            TDE: TDE0105
            SYW: SYNW0169(pfs)
            SYD: Syncc9605_0164
            SYE: Syncc9902_0194
            CYA: CYA_1636(mtnN)
            CYB: CYB_1283(mtnN)
            PMG: P9301_14421(pfs)
            PMH: P9215_14761
            BTH: BT_4451
            BFR: BF3598
            BFS: BF3401
            PGI: PG0497(mtn)
            SRU: SRU_1556(mtnN)
            CHU: CHU_2004(pfs)
            DRA: DR_1451
            TTH: TTC1185
            TTJ: TTHA1550
            TMA: TM1129
STRUCTURES  PDB: 1NC1  1NC3  1Y6Q  1Y6R  1ZOS  2H8G  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.16
            ExPASy - ENZYME nomenclature database: 3.2.2.16
            ExplorEnz - The Enzyme Database: 3.2.2.16
            ERGO genome analysis and discovery system: 3.2.2.16
            BRENDA, the Enzyme Database: 3.2.2.16
            CAS: 50812-28-7
///
ENTRY       EC 3.2.2.17                 Enzyme
NAME        deoxyribodipyrimidine endonucleosidase;
            pyrimidine dimer DNA-glycosylase;
            endonuclease V;
            deoxyribonucleate pyrimidine dimer glycosidase;
            pyrimidine dimer DNA glycosylase;
            T4-induced UV endonuclease;
            PD-DNA glycosylase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     deoxy-D-ribocyclobutadipyrimidine polynucleotidodeoxyribohydrolase
REACTION    Cleaves the N-glycosidic bond between the 5'-pyrimidine residue in
            cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose
            residue
REFERENCE   1  [PMID:6248789]
  AUTHORS   Haseltine WA, Gordon LK, Lindan CP, Grafstrom RH, Shaper NL,
            Grossman L.
  TITLE     Cleavage of pyrimidine dimers in specific DNA sequences by a
            pyrimidine dimer DNA-glycosylase of M. luteus.
  JOURNAL   Nature. 285 (1980) 634-41.
  ORGANISM  Micrococcus luteus
STRUCTURES  PDB: 1I1Z  1I20  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.17
            ExPASy - ENZYME nomenclature database: 3.2.2.17
            ExplorEnz - The Enzyme Database: 3.2.2.17
            ERGO genome analysis and discovery system: 3.2.2.17
            BRENDA, the Enzyme Database: 3.2.2.17
            CAS: 75302-33-9
///
ENTRY       EC 3.2.2.18       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
COMMENT     Deleted entry: glycopeptide N-glycosidase. Now included with EC
            3.5.1.52, peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase
            (EC 3.2.2.18 created 1984, deleted 1989)
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.18
            ExPASy - ENZYME nomenclature database: 3.2.2.18
            ExplorEnz - The Enzyme Database: 3.2.2.18
            ERGO genome analysis and discovery system: 3.2.2.18
            BRENDA, the Enzyme Database: 3.2.2.18
///
ENTRY       EC 3.2.2.19                 Enzyme
NAME        [protein ADP-ribosylarginine] hydrolase;
            ADP-ribose-L-arginine cleavage enzyme;
            ADP-ribosylarginine hydrolase;
            Nomega-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase;
            protein-omega-N-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     protein-Nomega-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase
REACTION    (1) protein-Nomega-(ADP-D-ribosyl)-L-arginine + H2O = ADP-ribose +
            protein-L-arginine [RN:R07626];
            (2) Nomega-(ADP-D-ribosyl)-L-arginine + H2O = ADP-ribose +
            L-arginine [RN:R01886]
ALL_REAC    R01886 R07626
SUBSTRATE   protein-Nomega-(ADP-D-ribosyl)-L-arginine;
            H2O [CPD:C00001];
            Nomega-(ADP-D-ribosyl)-L-arginine
PRODUCT     ADP-ribose [CPD:C00301];
            protein-L-arginine [CPD:C00613];
            L-arginine [CPD:C00062]
COMMENT     The enzyme will remove ADP-ribose from arginine residues in
            ADP-ribosylated proteins.
REFERENCE   1  [PMID:2994036]
  AUTHORS   Moss J, Jacobson MK, Stanley SJ.
  TITLE     Reversibility of arginine-specific mono(ADP-ribosyl)ation:
            identification in erythrocytes of an ADP-ribose-L-arginine cleavage
            enzyme.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 5603-7.
  ORGANISM  turkey, rabbit, chicken [GN:gga]
REFERENCE   2  [PMID:1375222]
  AUTHORS   Moss J, Stanley SJ, Nightingale MS, Murtagh JJ Jr, Monaco L, Mishima
            K, Chen HC, Williamson KC, Tsai SC.
  TITLE     Molecular and immunological characterization of ADP-ribosylarginine
            hydrolases.
  JOURNAL   J. Biol. Chem. 267 (1992) 10481-8.
  ORGANISM  turkey, rabbit, rat [GN:rno], mouse [GN:mmu], cow [GN:bta], guinea
            pig
REFERENCE   3  [PMID:10358013]
  AUTHORS   Konczalik P, Moss J.
  TITLE     Identification of critical, conserved vicinal aspartate residues in
            mammalian and bacterial ADP-ribosylarginine hydrolases.
  JOURNAL   J. Biol. Chem. 274 (1999) 16736-40.
  ORGANISM  Rhodospirillum rubrum [GN:rru]
REFERENCE   4  [PMID:8349667]
  AUTHORS   Takada T, Iida K, Moss J.
  TITLE     Cloning and site-directed mutagenesis of human ADP-ribosylarginine
            hydrolase.
  JOURNAL   J. Biol. Chem. 268 (1993) 17837-43.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:8678289]
  AUTHORS   Ohno T, Tsuchiya M, Osago H, Hara N, Jidoi J, Shimoyama M.
  TITLE     Detection of arginine-ADP-ribosylated protein using recombinant
            ADP-ribosylarginine hydrolase.
  JOURNAL   Anal. Biochem. 231 (1995) 115-22.
  ORGANISM  mouse [GN:mmu], cow [GN:bta]
ORTHOLOGY   KO: K01245  ADP-ribosylarginine hydrolase
GENES       HSA: 141(ADPRH)
            PTR: 470893(ADPRH)
            MMU: 11544(Adprh)
            RNO: 25371(Adprh)
            CFA: 487995(ADPRH)
            XLA: 432184(MGC82502) 495095(LOC495095)
            XTR: 493544(adprh)
            SPU: 576531(LOC576531) 577960(LOC577960)
            DDI: DDBDRAFT_0188511
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.19
            ExPASy - ENZYME nomenclature database: 3.2.2.19
            ExplorEnz - The Enzyme Database: 3.2.2.19
            ERGO genome analysis and discovery system: 3.2.2.19
            BRENDA, the Enzyme Database: 3.2.2.19
            CAS: 98668-52-1
///
ENTRY       EC 3.2.2.20                 Enzyme
NAME        DNA-3-methyladenine glycosylase I;
            deoxyribonucleate 3-methyladenine glycosidase I;
            3-methyladenine DNA glycosylase I;
            DNA-3-methyladenine glycosidase I
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     alkylated-DNA glycohydrolase (releasing methyladenine and
            methylguanine)
REACTION    Hydrolysis of alkylated DNA, releasing 3-methyladenine
COMMENT     Involved in the removal of alkylated bases from DNA in Escherichia
            coli (cf. EC 2.1.1.63 methylated-DNA---[protein]-cysteine
            S-methyltransferase).
REFERENCE   1  [PMID:7040984]
  AUTHORS   Evensen G, Seeberg E.
  TITLE     Adaptation to alkylation resistance involves the induction of a DNA
            glycosylase.
  JOURNAL   Nature. 296 (1982) 773-5.
REFERENCE   2  [PMID:7040983]
  AUTHORS   Karran P, Hjelmgren T, Lindahl T.
  TITLE     Induction of a DNA glycosylase for N-methylated purines is part of
            the adaptive response to alkylating agents.
  JOURNAL   Nature. 296 (1982) 770-3.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:7041972]
  AUTHORS   Thomas L, Yang CH, Goldthwait DA.
  TITLE     Two DNA glycosylases in Escherichia coli which release primarily
            3-methyladenine.
  JOURNAL   Biochemistry. 21 (1982) 1162-9.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01246  DNA-3-methyladenine glycosylase I
GENES       ATH: AT1G75090
            OSA: 4331957
            PIC: PICST_58778(MAG1)
            ECO: b3549(tag)
            ECJ: JW3518(tag)
            ECE: Z4974(tag)
            ECS: ECs4434
            ECC: c4367(tag)
            ECI: UTI89_C4089(tag)
            ECV: APECO1_2899(tag)
            ECW: EcE24377A_4044(tag)
            ECX: EcHS_A3749(tag)
            STY: STY4160(tag)
            STT: t3877(tag)
            SPT: SPA3494(tag)
            SEC: SC3574(tag)
            STM: STM3642(tag)
            YPE: YPO4074(tag)
            YPK: y4091(tag)
            YPM: YP_3984(tag)
            YPA: YPA_3010
            YPN: YPN_3719
            YPP: YPDSF_0021
            YPS: YPTB3914(tag)
            YPI: YpsIP31758_4132(tag)
            SFL: SF3582(tag)
            SFX: S4186(tag)
            SFV: SFV_3539(tag)
            SSN: SSON_3841(tag)
            SBO: SBO_3551(tag)
            SDY: SDY_4353(tag)
            ECA: ECA0082(tag)
            PLU: plu0292(tag)
            SGL: SG1137
            ENT: Ent638_0175
            SPE: Spro_0064
            HIT: NTHI0774(tag)
            PMU: PM1601(tagI)
            MSU: MS2356(tag)
            APL: APL_1931(tagI)
            ASU: Asuc_0297
            XCC: XCC2750(tag)
            XCB: XC_1363
            XCV: XCV2171 XCV3064(tag)
            XAC: XAC2919(tag)
            XOO: XOO1423(tag)
            XOM: XOO_1306(XOO1306)
            VCH: VC1672
            VCO: VC0395_A1277(tag)
            VVU: VV1_2873
            VVY: VV1398
            VPA: VP1179
            VFI: VFA0815
            PAE: PA0010(tag)
            PAU: PA14_00110(tag)
            PPU: PP_0062(tag)
            PPF: Pput_0078
            PST: PSPTO_0183(tag)
            PSB: Psyr_0013
            PSP: PSPPH_0013(tag)
            PFL: PFL_0015(tag)
            PFO: Pfl_0011
            PEN: PSEEN0018(tag)
            PMY: Pmen_0015
            ACI: ACIAD3611(tag)
            SON: SO_0016(tag)
            SDN: Sden_0010
            SFR: Sfri_0008
            SAZ: Sama_0027
            SBL: Sbal_0014
            SBM: Shew185_0010
            SLO: Shew_0011
            SPC: Sputcn32_0008
            SSE: Ssed_0016
            SPL: Spea_0008
            SHE: Shewmr4_0010
            SHM: Shewmr7_0010
            SHN: Shewana3_0018
            SHW: Sputw3181_0008
            ILO: IL0007(tag)
            CPS: CPS_2351(tag)
            PHA: PSHAa0788(tag)
            PAT: Patl_0010
            SDE: Sde_0555
            MAQ: Maqu_0153
            CBU: CBU_0383(tag)
            CBD: COXBU7E912_1686(tag)
            LPN: lpg0618(tag)
            LPF: lpl0656(tag)
            LPP: lpp0672(tag)
            MCA: MCA0358(tag)
            FTN: FTN_0673(tag)
            HCH: HCH_02047(tag) HCH_03236
            CSA: Csal_0684
            ABO: ABO_0010(tag)
            MMW: Mmwyl1_0147 Mmwyl1_3559
            AHA: AHA_0129
            NME: NMB1673
            NMA: NMA1931(tag)
            NMC: NMC1591(tag)
            NGO: NGO1322
            CVI: CV_1945(tag)
            RSO: RSp0666(tag)
            REU: Reut_A3242
            REH: H16_A3558(tag)
            RME: Rmet_3404
            BMA: BMA2871(tag)
            BMV: BMASAVP1_A3446(tag)
            BML: BMA10299_A1673(tag)
            BMN: BMA10247_3104(tag)
            BXE: Bxe_A0106
            BVI: Bcep1808_0203
            BUR: Bcep18194_A3347
            BCN: Bcen_2862
            BCH: Bcen2424_0245
            BAM: Bamb_0158
            BPS: BPSL3317(tag)
            BPM: BURPS1710b_0088(tag)
            BPL: BURPS1106A_3948(tag)
            BPD: BURPS668_3867(tag)
            BTE: BTH_I3193
            BPE: BP2838
            BPA: BPP3707
            BBR: BB4153
            POL: Bpro_3540
            AAV: Aave_0775
            AJS: Ajs_0457
            MPT: Mpe_A0097
            HAR: HEAR0071(tag)
            MMS: mma_0077(tag)
            AZO: azo3621(tag)
            DAR: Daro_1887
            MFA: Mfla_0491
            WSU: WS0781
            CFF: CFF8240_0211
            CCV: CCV52592_0983
            CCO: CCC13826_0711(tag)
            GSU: GSU0567(tag)
            GUR: Gura_3518
            PPD: Ppro_3581
            DVU: DVU0356(tag)
            DVL: Dvul_2628
            DDE: Dde_3701
            DPS: DP0164
            ADE: Adeh_2154
            AFW: Anae109_4052
            SAT: SYN_00331
            RTY: RT0340(mpg)
            PUB: SAR11_0186(tag)
            MLO: mlr6925
            MES: Meso_0359
            PLA: Plav_0747
            SME: SMc00923(tag)
            SMD: Smed_0399
            ATU: Atu0670(tag)
            ATC: AGR_C_1200
            RET: RHE_CH00815(tag)
            RLE: RL0871(tag)
            BME: BMEII1058
            BMF: BAB2_0179(tag)
            BMS: BRA0185(tag)
            BMB: BruAb2_0180(tag)
            OAN: Oant_3015
            BJA: bll2553(tag)
            BRA: BRADO2046(tag)
            BBT: BBta_2374(tag)
            RPA: RPA1067(tag)
            RPB: RPB_1116
            RPC: RPC_4332
            RPD: RPD_1237
            RPE: RPE_4391
            NWI: Nwi_2705
            NHA: Nham_4020
            BHE: BH12210(tag)
            BQU: BQ09600(tag)
            XAU: Xaut_1417
            CCR: CC_0382
            SIL: SPO1900(tag)
            SIT: TM1040_1922
            RSP: RSP_0744
            RSH: Rsph17029_2400
            RSQ: Rsph17025_2464
            JAN: Jann_0495
            RDE: RD1_3392(tag)
            PDE: Pden_2024
            MMR: Mmar10_0810
            HNE: HNE_0860(tag)
            ZMO: ZMO0377(tag) ZMO1677(mutY)
            SWI: Swit_4680
            RRU: Rru_A1573
            MAG: amb2574
            SUS: Acid_0536
            BCL: ABC0755
            OIH: OB0533
            SAU: SA1489(tag)
            SAV: SAV1664(tag)
            SAM: MW1608(tag)
            SAR: SAR1744(tag)
            SAS: SAS1593
            SAC: SACOL1711
            SAB: SAB1525(tag)
            SAA: SAUSA300_1612(tag)
            SAO: SAOUHSC_01768
            SAJ: SaurJH9_1722
            SAH: SaurJH1_1756
            SEP: SE1340
            SER: SERP1229
            SHA: SH1262(tag)
            SSP: SSP1100
            LMO: lmo1639
            LMF: LMOf2365_1661(tag)
            LIN: lin1680
            LWE: lwe1655(tag)
            LLA: L0289(tag)
            LLC: LACR_1224
            SPY: SPy_2118(tag)
            SPZ: M5005_Spy_1801(tag)
            SPM: spyM18_2176(tag)
            SPG: SpyM3_1802(tag)
            SPS: SPs1800
            SPH: MGAS10270_Spy1869(tag)
            SPI: MGAS10750_Spy1893(tag)
            SPJ: MGAS2096_Spy1834(tag)
            SPK: MGAS9429_Spy1812(tag)
            SPF: SpyM51760(tag)
            SPA: M6_Spy1800
            SPB: M28_Spy1785(tag)
            SPN: SP_0180
            SPR: spr0166(tag)
            SPD: SPD_0171(tag)
            SAG: SAG2095(tag)
            SAN: gbs2049
            SAK: SAK_2034(tag)
            SMU: SMU.2087(tagI)
            STL: stu0057(tag)
            STE: STER_0075
            SSA: SSA_2133 SSA_2253(tag)
            SSU: SSU05_0061
            SSV: SSU98_0062
            SGO: SGO_2049(tagI)
            LPL: lp_0296(tag1) lp_3020(tag2) lp_3293(tag3)
            LJO: LJ0697
            LAC: LBA0155
            LSA: LSA0039(tag1) LSA1323(tag2)
            LSL: LSL_1082
            LBR: LVIS_1958 LVIS_1965
            LCA: LSEI_0431 LSEI_2212
            LGA: LGAS_0477
            LRE: Lreu_1297
            EFA: EF0278(tag-1) EF3050(tag-2)
            OOE: OEOE_0312
            STH: STH2658
            CBE: Cbei_2823
            DSY: DSY3485
            TTE: TTE0091(tag)
            MPE: MYPE3200
            MFL: Mfl277
            MTU: Rv1210(tagA)
            MTC: MT1248(tag)
            MBO: Mb1242(tagA)
            MBB: BCG_1270(tagA)
            MLE: ML1066(tagA)
            MPA: MAP2567c(tagA)
            MSM: MSMEG_5082(tag)
            MVA: Mvan_4506
            MGI: Mflv_2189
            MMC: Mmcs_4003
            MKM: Mkms_4077
            MJL: Mjls_4233
            CGL: NCgl0142(cgl0145) NCgl2739(cgl2837)
            CGB: cg0182(tagA2) cg3140(tagA1)
            CEF: CE2657
            CDI: DIP0134
            CJK: jk0074(tagA)
            NFA: nfa47230(tag)
            RHA: RHA1_ro05971
            SCO: SCO5143(SCP8.06)
            SMA: SAV3121(tagA)
            LXX: Lxx07090(tagI)
            CMI: CMM_1172(tag)
            ART: Arth_0014
            NCA: Noca_0664
            TFU: Tfu_0498
            FRA: Francci3_0687
            FAL: FRAAL1196(tag)
            ACE: Acel_1837
            KRA: Krad_0999
            SEN: SACE_1027(tag) SACE_6025(tagA1)
            STP: Strop_0705
            BLO: BL0979(tag)
            RBA: RB5226(tag)
            PCU: pc1338(tag)
            LIL: LA3832
            LIC: LIC13064(tag)
            BTH: BT_2400
            BFR: BF3930
            BFS: BF3704(tag)
            GFO: GFO_3040
            FJO: Fjoh_1605
            FPS: FP2354(tag)
            MBU: Mbur_0590
STRUCTURES  PDB: 1F4R  1F6O  1LMZ  1NKU  1P7M  2JG6  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.20
            ExPASy - ENZYME nomenclature database: 3.2.2.20
            ExplorEnz - The Enzyme Database: 3.2.2.20
            ERGO genome analysis and discovery system: 3.2.2.20
            BRENDA, the Enzyme Database: 3.2.2.20
            CAS: 89287-37-6
///
ENTRY       EC 3.2.2.21                 Enzyme
NAME        DNA-3-methyladenine glycosylase II;
            deoxyribonucleate 3-methyladenine glycosidase II;
            3-methyladenine DNA glycosylase II;
            DNA-3-methyladenine glycosidase II;
            AlkA
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     alkylated-DNA glycohydrolase (releasing methyladenine and
            methylguanine)
REACTION    Hydrolysis of alkylated DNA, releasing 3-methyladenine,
            3-methylguanine, 7-methylguanine and 7-methyladenine
COMMENT     Involved in the removal of alkylated bases from DNA in Escherichia
            coli (cf. EC 2.1.1.63 methylated-DNA---[protein]-cysteine
            S-methyltransferase).
REFERENCE   1  [PMID:7040984]
  AUTHORS   Evensen G, Seeberg E.
  TITLE     Adaptation to alkylation resistance involves the induction of a DNA
            glycosylase.
  JOURNAL   Nature. 296 (1982) 773-5.
REFERENCE   2  [PMID:7040983]
  AUTHORS   Karran P, Hjelmgren T, Lindahl T.
  TITLE     Induction of a DNA glycosylase for N-methylated purines is part of
            the adaptive response to alkylating agents.
  JOURNAL   Nature. 296 (1982) 770-3.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:352392]
  AUTHORS   Riazuddin S, Lindahl T.
  TITLE     Properties of 3-methyladenine-DNA glycosylase from Escherichia coli.
  JOURNAL   Biochemistry. 17 (1978) 2110-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:7041972]
  AUTHORS   Thomas L, Yang CH, Goldthwait DA.
  TITLE     Two DNA glycosylases in Escherichia coli which release primarily
            3-methyladenine.
  JOURNAL   Biochemistry. 21 (1982) 1162-9.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01247  DNA-3-methyladenine glycosylase II
GENES       HSA: 4350(MPG)
            MMU: 268395(Mpg)
            RNO: 24561(Mpg)
            CFA: 611597(MPG)
            GGA: 416648(MPG)
            ATH: AT3G12040
            OSA: 4330890
            SCE: YER142C(MAG1)
            AGO: AGOS_AFR011W
            SPO: SPAPB24D3.04c(mag1) SPBC23G7.11
            ECU: ECU05_1590
            PFA: PF14_0639
            CPV: cgd8_5410
            CHO: Chro.80616
            TET: TTHERM_01079170
            ECO: b2068(alkA)
            ECJ: JW2053(alkA)
            ECE: Z3237(alkA)
            ECS: ECs2877
            ECC: c2595(alkA)
            ECI: UTI89_C2344(alkA)
            ECP: ECP_2108
            ECV: APECO1_1159(alkA)
            ECW: EcE24377A_2361(alkA)
            ECX: EcHS_A2209
            STY: STY2337(alkA)
            STT: t0748(alkA)
            SPT: SPA0742(alkA)
            SEC: SC2127(alkA)
            STM: STM2124(alkA)
            YPE: YPO1834
            YPK: y2473
            YPM: YP_1558(alkA)
            YPA: YPA_1210
            YPN: YPN_2289
            YPS: YPTB1708
            SFL: SF2133(alkA)
            SFX: S2258(alkA)
            SFV: SFV_2131(alkA)
            SSN: SSON_2121(alkA)
            SBO: SBO_0895(alkA)
            SDY: SDY_2194(alkA)
            ECA: ECA0907
            PLU: plu0155
            ENT: Ent638_2682
            XFA: XF1326
            XFT: PD0572(alkA)
            XCC: XCC1131
            XCB: XC_3112
            XCV: XCV1264(alkA)
            XAC: XAC1232
            XOO: XOO3524
            XOM: XOO_3330(XOO3330)
            VCO: VC0395_0222
            PAE: PA1686(alkA)
            PAU: PA14_42700(alkA)
            PAP: PSPA7_3585(alkA)
            PPU: PP_0705
            PPF: Pput_0738
            PSB: Psyr_3366
            PSP: PSPPH_3286
            PFL: PFL_2661 PFL_4632(alkA)
            PFO: Pfl_2156
            PEN: PSEEN0843
            CBD: COXBU7E912_1144(mpg)
            LPF: lpl2036
            NOC: Noc_0079
            ABO: ABO_1413
            CVI: CV_3195(alkA)
            RSO: RSc1168(RS04576) RSc2569(alkA)
            REU: Reut_A1123
            REH: H16_B2551(alkA)
            RME: Rmet_1086 Rmet_3766
            BMA: BMA0116(alkA) BMA1655
            BMV: BMASAVP1_A2158 BMASAVP1_A2835(alkA)
            BML: BMA10299_A2250(alkA) BMA10299_A3157
            BMN: BMA10247_2324(alkA)
            BXE: Bxe_A1627
            BUR: Bcep18194_A4930 Bcep18194_A5383 Bcep18194_A6105
                 Bcep18194_A6507
            BCN: Bcen_2161 Bcen_6000
            BCH: Bcen2424_2077 Bcen2424_2775 Bcen2424_3151
            BAM: Bamb_2112 Bamb_3204
            BPS: BPSL0101 BPSL2242
            BPM: BURPS1710b_0323(alkA) BURPS1710b_2680
            BPL: BURPS1106A_0133(alkA)
            BPD: BURPS668_0117(alkA)
            BTE: BTH_I0086 BTH_I1942
            BPE: BP1909
            BPA: BPP1021 BPP2284
            BBR: BB1235 BB1736
            RFR: Rfer_1350
            POL: Bpro_2864
            MPT: Mpe_A2455
            HAR: HEAR1287 HEAR2927
            MMS: mma_2107
            NEU: NE0981
            NMU: Nmul_A1213
            EBA: ebA7191(alkA)
            AZO: azo1833(alkA)
            DAR: Daro_0843
            TBD: Tbd_2436
            MFA: Mfla_1299
            MXA: MXAN_1556
            RFE: RF_0560(mpg)
            OTS: OTBS_2169(mpg)
            WOL: WD1110(mpg)
            MLO: mll3478
            MES: Meso_3025
            SME: SMc00736
            ATU: Atu3588(alkA)
            ATC: AGR_L_2478
            RET: RHE_CH03785(alkA)
            RLE: RL4312
            BME: BMEI0382
            BMF: BAB1_1661
            BMS: BR1646
            BMB: BruAb1_1634
            BJA: bll1371(alkA)
            RPA: RPA2586(3mg) RPA4755
            RPB: RPB_0813
            RPC: RPC_4886
            RPD: RPD_0924
            RPE: RPE_4855
            NWI: Nwi_0747 Nwi_1438
            CCR: CC_2201
            SIL: SPO2127
            SIT: TM1040_1157
            RSP: RSP_2381 RSP_2727
            RDE: RD1_3176
            HNE: HNE_3393
            SWI: Swit_0547
            GOX: GOX0961
            GBE: GbCGDNIH1_1341 GbCGDNIH1_1806
            ACR: Acry_2635
            RRU: Rru_A3357
            ABA: Acid345_0702 Acid345_4712
            SUS: Acid_6307
            BSU: BG10165(alkA) BG12912(yfjP)
            BHA: BH1749
            BAN: BA3871(alkA)
            BAR: GBAA3871(alkA)
            BAA: BA_1003 BA_4346
            BAT: BAS0413 BAS3587
            BCE: BC0468 BC3742
            BCA: BCE_0541 BCE_3774(alkA)
            BCZ: BCZK0399(alkA) BCZK0774(alkA) BCZK3499(alkA)
            BCY: Bcer98_0411 Bcer98_0703
            BTK: BT9727_0403(alkA) BT9727_0773(alkA) BT9727_3487(alkA)
            BTL: BALH_0424(alkA)
            BLI: BL03090(yfjP)
            BLD: BLi00831(yfjP)
            BCL: ABC3152(alkA)
            BPU: BPUM_0752
            GKA: GK0428
            SSP: SSP0289
            CBE: Cbei_0072
            DSY: DSY2079
            DRM: Dred_1635
            MPU: MYPU_0950(ogt)
            MSM: MSMEG_4925
            RHA: RHA1_ro02327
            RXY: Rxyl_1215
            RBA: RB4998(alkA)
            LIL: LA0281 LA1370(mag1)
            LIC: LIC10238 LIC12362(alkA)
            SYN: slr0231
            GVI: gll2018
            CCH: Cag_1802
            CPH: Cpha266_2098
            PVI: Cvib_0387
            PLT: Plut_0321
            DRA: DR_2584
            DGE: Dgeo_0107
            TTH: TTC1654
            TTJ: TTHA0329
            MEM: Memar_0903
            HAL: VNG1311G(alkA)
            HMA: rrnAC1088(alkA)
            NPH: NP4170A
            PAB: PAB1530(alkA)
            PFU: PF0511
            TKO: TK0345
            APE: APE_0275.1
STRUCTURES  PDB: 1BNK  1DIZ  1EWN  1MPG  1PVS  2JHJ  2JHN  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.21
            ExPASy - ENZYME nomenclature database: 3.2.2.21
            ExplorEnz - The Enzyme Database: 3.2.2.21
            ERGO genome analysis and discovery system: 3.2.2.21
            BRENDA, the Enzyme Database: 3.2.2.21
            CAS: 89287-38-7
///
ENTRY       EC 3.2.2.22                 Enzyme
NAME        rRNA N-glycosylase;
            ribosomal ribonucleate N-glycosidase;
            nigrin b;
            RNA N-glycosidase;
            rRNA N-glycosidase;
            ricin;
            momorcochin-S;
            Mirabilis antiviral protein;
            momorcochin-S;
            gelonin;
            saporins
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     rRNA N-glycohydrolase
REACTION    Hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat
            ribosomes
COMMENT     Ricin A-chain and related toxins show this activity. Naked rRNA is
            attacked more slowly than rRNA in intact ribosomes. Naked rRNA from
            Escherichia coli is cleaved at a corresponding position.
REFERENCE   1  [PMID:3288622]
  AUTHORS   Endo Y, Tsurugi K.
  TITLE     The RNA N-glycosidase activity of ricin A-chain. The characteristics
            of the enzymatic activity of ricin A-chain with ribosomes and with
            rRNA.
  JOURNAL   J. Biol. Chem. 263 (1988) 8735-9.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:3288622]
  AUTHORS   Endo Y, Tsurugi K.
  TITLE     The RNA N-glycosidase activity of ricin A-chain. The characteristics
            of the enzymatic activity of ricin A-chain with ribosomes and with
            rRNA.
  JOURNAL   J. Biol. Chem. 263 (1988) 8735-9.
  ORGANISM  rat [GN:rno]
STRUCTURES  PDB: 1AHA  1AHB  1AHC  1BR5  1BR6  1BRY  1D6A  1DM0  1F8Q  1FMP  
                 1GIK  1GIS  1GIU  1HWM  1HWN  1HWO  1HWP  1IFS  1IFT  1IFU  
                 1IL3  1IL4  1IL5  1IL9  1J1M  1J1Q  1J1R  1J1S  1J4G  1LLN  
                 1LP8  1LPC  1LPD  1M2T  1MOM  1NIO  1NLI  1OBS  1OBT  1ONK  
                 1OQL  1PC8  1QD2  1QI7  1R4P  1R4Q  1RL0  1RTC  1RZO  1TCS  
                 1UQ4  1UQ5  1YF8  1ZAM  1ZB0  1ZB2  2AAI  2B7U  2G5X  2GA4  
                 2Q3N  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.22
            ExPASy - ENZYME nomenclature database: 3.2.2.22
            ExplorEnz - The Enzyme Database: 3.2.2.22
            ERGO genome analysis and discovery system: 3.2.2.22
            BRENDA, the Enzyme Database: 3.2.2.22
            CAS: 113756-12-0
///
ENTRY       EC 3.2.2.23                 Enzyme
NAME        DNA-formamidopyrimidine glycosylase;
            Fapy-DNA glycosylase;
            deoxyribonucleate glycosidase;
            2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase;
            2,6-diamino-4-hydroxy-5(N-methyl)formamidopyrimidine-DNA
            glycosylase;
            formamidopyrimidine-DNA glycosylase;
            DNA-formamidopyrimidine glycosidase;
            Fpg protein
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     DNA glycohydrolase
            [2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimide releasing]
REACTION    Hydrolysis of DNA containing ring-opened 7-methylguanine residues,
            releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
COMMENT     May play a significant role in processes leading to recovery from
            mutagenesis and/or cell death by alkylating agents. Also involved in
            the GO system responsible for removing an oxidatively damaged form
            of guanine (7,8-dihydro-8-oxoguanine) from DNA.
REFERENCE   1  [PMID:3319582]
  AUTHORS   Boiteux S, O'Connor TR, Laval J.
  TITLE     Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and
            sequencing of the fpg structural gene and overproduction of the
            protein.
  JOURNAL   EMBO. J. 6 (1987) 3177-83.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01248  formamidopyrimidine-DNA glycosylase
GENES       DME: Dmel_CG1795
            ANI: AN3629.2
            AFM: AFUA_4G11930
            AOR: AO090003001022
            PFA: PFI0835c
            ECO: b3635(mutM)
            ECJ: JW3610(mutM)
            ECE: Z5059(mutM)
            ECS: ECs4510
            ECC: c4459(mutM)
            ECI: UTI89_C4178(mutM)
            ECP: ECP_3733
            ECV: APECO1_2824(mutM)
            ECW: EcE24377A_4136(mutM)
            ECX: EcHS_A3844
            STY: STY4068(mutM)
            STT: t3792(mutM)
            SPT: SPA3578(mutM)
            SEC: SC3649(mutM)
            STM: STM3726(mutM)
            YPE: YPO0052(mutM)
            YPK: y0090(mutM)
            YPM: YP_0053(mutM)
            YPA: YPA_3490
            YPN: YPN_3798
            YPP: YPDSF_3853
            YPS: YPTB0049(mutM)
            YPI: YpsIP31758_0064(mutM)
            YEN: YE0066(fpg)
            SFL: SF3674(mutM)
            SFX: S4094(mutM)
            SFV: SFV_3894(mutM)
            SSN: SSON_3772(mutM)
            SBO: SBO_3637(mutM)
            SDY: SDY_4065(mutM)
            ECA: ECA0148(mutM)
            PLU: plu4857(mutM)
            SGL: SG2206
            ENT: Ent638_0104
            KPN: KPN_03975(mutM)
            SPE: Spro_4839
            HIN: HI0946(fpg)
            HIT: NTHI1118(mutM)
            HIP: CGSHiEE_07245
            HDU: HD0710(mutM)
            HSO: HS_0146(mutM)
            PMU: PM1145(fpg)
            MSU: MS1944(nei)
            APL: APL_1990(mutM)
            ASU: Asuc_0016
            XFA: XF0071 XF0170
            XFT: PD0053(mutM) PD0138(mutM)
            XCC: XCC3527 XCC4147(mutM)
            XCB: XC_0633 XC_4239
            XCV: XCV0662 XCV4390(mutM)
            XAC: XAC0606 XAC4286(mutM)
            XOO: XOO0299(mutM)
            XOM: XOO_0270(XOO0270)
            VCH: VC0221
            VCO: VC0395_A2602(mutM)
            VVU: VV1_0821
            VVY: VV0289
            VPA: VP0189
            VFI: VF0130
            PPR: PBPRA0206
            PAE: PA0357(mutM)
            PAU: PA14_04670(mutM)
            PAP: PSPA7_0450(mutM)
            PPU: PP_5125(mutM)
            PPF: Pput_4999
            PST: PSPTO_0414(mutM)
            PSB: Psyr_4761
            PSP: PSPPH_4792(mutM)
            PFL: PFL_5870(mutM)
            PFO: Pfl_5351
            PEN: PSEEN0287(mutM)
            PMY: Pmen_4197
            PAR: Psyc_0342(fpg)
            PCR: Pcryo_0376
            PRW: PsycPRwf_0382
            ACI: ACIAD0707(mutM)
            SON: SO_4726(mutM)
            SDN: Sden_0210
            SFR: Sfri_3924
            SAZ: Sama_0117
            SBL: Sbal_0075
            SBM: Shew185_4324
            SLO: Shew_3690
            SPC: Sputcn32_3886
            SSE: Ssed_0117
            SPL: Spea_4104
            SHE: Shewmr4_3881
            SHM: Shewmr7_3974
            SHN: Shewana3_4084
            SHW: Sputw3181_0067
            ILO: IL0245(mutM)
            CPS: CPS_0212(mutM)
            PHA: PSHAa0447(mutM)
            PAT: Patl_0051
            SDE: Sde_3681
            PIN: Ping_0053
            MAQ: Maqu_3749
            LPN: lpg0557(mutM)
            LPF: lpl0599(mutM)
            LPP: lpp0616(mutM)
            MCA: MCA3072(mutM)
            FTU: FTT0693c(mutM)
            FTF: FTF0693c(mutM)
            FTW: FTW_1550(mutM)
            FTL: FTL_1543
            FTH: FTH_1493(mutM)
            FTA: FTA_1627(mutM)
            FTN: FTN_0603(mutM)
            TCX: Tcr_1921
            NOC: Noc_2648
            AEH: Mlg_2649
            HHA: Hhal_2311
            HCH: HCH_00567(mutM1) HCH_02013(mutM2)
            CSA: Csal_2969
            ABO: ABO_2583(mutM)
            MMW: Mmwyl1_0631
            AHA: AHA_0164(mutM)
            DNO: DNO_1135(mutM)
            BCI: BCI_0177(mutM)
            RMA: Rmag_0332
            VOK: COSY_0314(mutM)
            NME: NMB1295
            NMA: NMA1505(fpg)
            NMC: NMC1232(fpg)
            NGO: NGO0610
            CVI: CV_4062(mutM)
            RSO: RSc0399(mutM)
            REU: Reut_A0346
            REH: H16_A0377
            RME: Rmet_0293
            BMA: BMA3115(mutM)
            BMV: BMASAVP1_A0083(mutM)
            BML: BMA10299_A1507(mutM)
            BMN: BMA10247_2935(mutM)
            BXE: Bxe_A4129
            BVI: Bcep1808_2903
            BUR: Bcep18194_A6128
            BCN: Bcen_2184
            BCH: Bcen2424_2798
            BAM: Bamb_2858
            BPS: BPSL0526(mutM)
            BPM: BURPS1710b_0758(mutM)
            BPL: BURPS1106A_0590(mutM)
            BPD: BURPS668_0574(mutM)
            BTE: BTH_I0479(mutM)
            PNU: Pnuc_1917
            BPE: BP3129(mutM)
            BPA: BPP0813(mutM)
            BBR: BB0897(mutM)
            RFR: Rfer_1656
            POL: Bpro_1297
            PNA: Pnap_0903
            AAV: Aave_3606
            AJS: Ajs_0899
            VEI: Veis_0955
            MPT: Mpe_A3233
            HAR: HEAR2889(mutM)
            MMS: mma_3124
            NEU: NE2552(mutM)
            NET: Neut_2512
            NMU: Nmul_A0582
            EBA: ebA1401(mutM)
            AZO: azo0759(mutM)
            DAR: Daro_3726
            TBD: Tbd_0383
            MFA: Mfla_0686
            GSU: GSU0997(mutM)
            GME: Gmet_1206
            GUR: Gura_3674
            PCA: Pcar_1864
            PPD: Ppro_3608
            DVU: DVU3256(mutM)
            DVL: Dvul_0133
            DDE: Dde_0542
            LIP: LI0637(mutM)
            BBA: Bd2176(fpg)
            DPS: DP0913
            ADE: Adeh_0277 Adeh_3929
            AFW: Anae109_0299 Anae109_0505
            MXA: MXAN_5932(mutM)
            SAT: SYN_00204
            RCO: RC1038(mutM)
            RFE: RF_0242(mutM)
            RBE: RBE_0247(mutM)
            WOL: WD1158(mutM)
            WBM: Wbm0589
            AMA: AM771(fpg)
            APH: APH_0411(mutM)
            ERU: Erum4330(mutM)
            ERW: ERWE_CDS_04520(mutM)
            ERG: ERGA_CDS_04450(mutM)
            ECH: ECH_0602(mutM)
            PUB: SAR11_0408(mutM)
            MLO: mll5585
            MES: Meso_4100
            PLA: Plav_3659
            SME: SMc01154(fpg)
            SMD: Smed_3573
            ATU: Atu0321(mutM)
            ATC: AGR_C_561
            RET: RHE_CH00355(fpg)
            RLE: RL0372(mutM)
            BME: BMEI1946
            BMF: BAB1_2184
            BMS: BR2183(mutM)
            BMB: BruAb1_2156(mutM)
            BOV: BOV_2096(mutM)
            OAN: Oant_0716
            BJA: blr0762
            BRA: BRADO0074(mutM)
            BBT: BBta_0080(mutM)
            RPA: RPA0084(mutM)
            RPB: RPB_0619
            RPC: RPC_0377
            RPD: RPD_0212
            RPE: RPE_0471
            NWI: Nwi_0040
            NHA: Nham_0048 Nham_1004
            BHE: BH02510(mutM)
            BQU: BQ02370(mutM)
            BBK: BARBAKC583_1221(mutM)
            XAU: Xaut_3307
            CCR: CC_3707
            SIL: SPO0146(mutM)
            SIT: TM1040_3029
            RSP: RSP_1339
            RSH: Rsph17029_0008
            RSQ: Rsph17025_2592
            JAN: Jann_4210
            RDE: RD1_0204(mutM)
            PDE: Pden_4512
            MMR: Mmar10_3076
            HNE: HNE_3274(mutM)
            ZMO: ZMO1187(mutM)
            NAR: Saro_0596
            SAL: Sala_3187
            SWI: Swit_4885
            ELI: ELI_10555
            GOX: GOX2500
            GBE: GbCGDNIH1_0159
            ACR: Acry_1723
            RRU: Rru_A3799
            MAG: amb0632
            MGM: Mmc1_1621
            ABA: Acid345_0380 Acid345_0985 Acid345_3866
            SUS: Acid_2844 Acid_3463 Acid_6700
            BSU: BG12628(mutM)
            BHA: BH3152(mutM)
            BAN: BA4830(mutM)
            BAR: GBAA4830(mutM)
            BAA: BA_5254
            BAT: BAS4481
            BCE: BC4586
            BCA: BCE_4717(mutM)
            BCZ: BCZK4327(mutM)
            BCY: Bcer98_3271
            BTK: BT9727_4316(mutM)
            BTL: BALH_4170(mutM)
            BLI: BL00393(mutM)
            BLD: BLi03056(mutM)
            BCL: ABC2708(mutM)
            BAY: RBAM_026120
            BPU: BPUM_2550
            OIH: OB2162(mutM)
            GKA: GK2728
            SAU: SA1512
            SAV: SAV1689
            SAM: MW1632
            SAR: SAR1768
            SAS: SAS1617
            SAC: SACOL1736(fpg)
            SAB: SAB1548c
            SAA: SAUSA300_1635(mutM)
            SAO: SAOUHSC_01796
            SAJ: SaurJH9_1746
            SAH: SaurJH1_1780
            SEP: SE1366
            SER: SERP1253(fpg)
            SHA: SH1235
            SSP: SSP1076
            LMO: lmo1564(mutM)
            LMF: LMOf2365_1586(mutM)
            LIN: lin1599(mutM)
            LWE: lwe1577(mutM)
            LLA: L0271(mutM)
            LLC: LACR_0399
            LLM: llmg_0373(fpg)
            SPY: SPy_0497(fpg)
            SPZ: M5005_Spy_0408(fpg)
            SPM: spyM18_0555
            SPG: SpyM3_0347(fpg)
            SPS: SPs1507
            SPH: MGAS10270_Spy0409(fpg)
            SPI: MGAS10750_Spy0421(fpg)
            SPJ: MGAS2096_Spy0427(fpg)
            SPK: MGAS9429_Spy0407(fpg)
            SPF: SpyM51461(fpg)
            SPA: M6_Spy0434
            SPB: M28_Spy0396(fpg)
            SPN: SP_0970
            SPR: spr0872(mutM)
            SPD: SPD_0858(mutM)
            SAG: SAG1489(mutM)
            SAN: gbs1554
            SAK: SAK_1519(mutM)
            SMU: SMU.1614(fpg)
            STC: str0620(mutM)
            STL: stu0620(mutM)
            SSA: SSA_1607(mutM)
            SGO: SGO_0715(mutM)
            LPL: lp_1509(fpg)
            LJO: LJ1650
            LAC: LBA1549(mutM)
            LSA: LSA1405(fpg)
            LSL: LSL_0489(nei)
            LDB: Ldb1511(fpg)
            LBU: LBUL_1406
            LBR: LVIS_1041
            LCA: LSEI_1708
            LRE: Lreu_1246
            EFA: EF0879(fpg)
            OOE: OEOE_0675
            STH: STH849
            CHY: CHY_1649(mutM)
            DSY: DSY1341 DSY4101
            DRM: Dred_1598
            SWO: Swol_2016
            MTA: Moth_1840
            MGE: MG_498(mutM)
            MPN: MPN380(fpg)
            MPU: MYPU_3100(fpg)
            MPE: MYPE2000(fpg)
            MGA: MGA_1053(nei)
            MMY: MSC_0682(fpg)
            MMO: MMOB3720(fpg)
            MHY: mhp595(fpg)
            MHJ: MHJ_0579(fpg)
            MHP: MHP7448_0578(fpg)
            MSY: MS53_0448(fpg)
            MCP: MCAP_0635(mutM)
            UUR: UU413(fpg)
            POY: PAM674(nei)
            AYW: AYWB_067(nei)
            MFL: Mfl581
            MTU: Rv0944 Rv2924c(fpg)
            MTC: MT0970 MT2994(fpg-2)
            MBO: Mb0969 Mb2949c(fpg)
            MBB: BCG_0998 BCG_2946c(fpg)
            MLE: ML1658(fpg)
            MPA: MAP0889 MAP2994c(fpg)
            MAV: MAV_3782(mutM)
            MSM: MSMEG_2419(mutM) MSMEG_5545
            MVA: Mvan_1631 Mvan_2172 Mvan_4883
            MGI: Mflv_1852 Mflv_4191
            MMC: Mmcs_1265 Mmcs_1950 Mmcs_4336
            MKM: Mkms_1282 Mkms_1996 Mkms_4422
            MJL: Mjls_1291 Mjls_1930 Mjls_4716
            CGL: NCgl0813(cgl0847) NCgl1993(cgl2073) NCgl2898(cgl3000)
            CGB: cg2272(mutM1) cg3328(mutM2)
            CEF: CE1975
            CDI: DIP1543
            CJK: jk1205(mutM)
            NFA: nfa41830(mutM) nfa50200
            RHA: RHA1_ro01377 RHA1_ro02246 RHA1_ro06270 RHA1_ro06523
            SCO: SCO0945(SCM10.34c) SCO5573(SC7A1.17)
            SMA: SAV2664(mutM1) SAV7289(mutM2)
            LXX: Lxx00140(mutM) Lxx09800(mutM)
            ART: Arth_1539 Arth_2500
            AAU: AAur_2469(mutM)
            PAC: PPA1451 PPA1623
            NCA: Noca_0157 Noca_3280
            TFU: Tfu_0652
            FRA: Francci3_3600
            FAL: FRAAL0303 FRAAL5723(end8) FRAAL5802(mutM) FRAAL6736(mutM)
            ACE: Acel_1573
            KRA: Krad_0158 Krad_1377
            SEN: SACE_0114(mutM) SACE_4713(mutM) SACE_5875(end8)
                 SACE_6099(mutM)
            STP: Strop_1288
            RXY: Rxyl_1786 Rxyl_2433 Rxyl_2550
            RBA: RB12746(mutM) RB7569(mutM)
            PCU: pc0892(mutM)
            SYN: slr1689(mutM)
            SYW: SYNW1961(FPG)
            SYC: syc0230_c(fpg)
            SYF: Synpcc7942_1323
            SYD: Syncc9605_0492
            SYE: Syncc9902_1843
            SYG: sync_0561(mutM)
            SYR: SynRCC307_0450(mutM)
            SYX: SynWH7803_0539(mutM)
            CYA: CYA_0203(mutM)
            CYB: CYB_1244(mutM)
            TEL: tll1566(fpg)
            GVI: gll3407(fpg)
            ANA: alr4320
            AVA: Ava_1271
            PMA: Pro0370(nei)
            PMM: PMM0328(FPG)
            PMT: PMT0186(FPG)
            PMN: PMN2A_1705
            PMI: PMT9312_0334
            PMB: A9601_03541(mutM)
            PMC: P9515_03601(mutM)
            PMF: P9303_21761(mutM)
            PMG: P9301_03551(mutM)
            PMH: P9215_03541
            PME: NATL1_04201(mutM)
            TER: Tery_1015
            BTH: BT_2359 BT_4488
            SRU: SRU_0462(mutM)
            GFO: GFO_3213(mutM)
            DET: DET1389(mutM)
            DEH: cbdb_A1344(mutM)
            DEB: DehaBAV1_1198
            RRS: RoseRS_1946
            RCA: Rcas_3836
            DRA: DR_0493
            DGE: Dgeo_0442
            TTH: TTC1454(mutM)
            TTJ: TTHA1806
            RCI: RCIX276(mutM)
STRUCTURES  PDB: 1K82  1KFV  1NNJ  1PJI  1PJJ  1PM5  1TDZ  1XC8  2F5N  2F5O  
                 2F5P  2F5Q  2F5S  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.23
            ExPASy - ENZYME nomenclature database: 3.2.2.23
            ExplorEnz - The Enzyme Database: 3.2.2.23
            ERGO genome analysis and discovery system: 3.2.2.23
            BRENDA, the Enzyme Database: 3.2.2.23
            CAS: 78783-53-6
///
ENTRY       EC 3.2.2.24                 Enzyme
NAME        ADP-ribosyl-[dinitrogen reductase] hydrolase;
            azoferredoxin glycosidase;
            azoferredoxin-activating enzymes;
            dinitrogenase reductase-activating glycohydrolase;
            ADP-ribosyl glycohydrolase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     ADP-D-ribosyl-[dinitrogen reductase] ADP-ribosylhydrolase
REACTION    ADP-D-ribosyl-[dinitrogen reductase] = ADP-D-ribose + [dinitrogen
            reductase] [RN:R03446]
ALL_REAC    R03446
SUBSTRATE   ADP-D-ribosyl-[dinitrogen reductase] [CPD:C01253]
PRODUCT     ADP-D-ribose [CPD:C01882];
            [dinitrogen reductase] [CPD:C03315]
COMMENT     Together with EC 2.4.2.37 NAD+---dinitrogen-reductase
            ADP-D-ribosyltransferase, , this enzyme controls the level of
            activity of EC 1.18.6.1 nitrogenase.
REFERENCE   1  [PMID:2506427]
  AUTHORS   Fitzmaurice WP, Saari LL, Lowery RG, Ludden PW, Roberts GP.
  TITLE     Genes coding for the reversible ADP-ribosylation system of
            dinitrogenase reductase from Rhodospirillum rubrum.
  JOURNAL   Mol. Gen. Genet. 218 (1989) 340-7.
  ORGANISM  Rhodospirillum rubrum [GN:rru]
GENES       SPE: Spro_3018
            PPF: Pput_1073
            BUR: Bcep18194_B1119
            PNA: Pnap_4684
            AZO: azo0530(draG1) azo2644(draG2)
            GSU: GSU2800(draG)
            GUR: Gura_1208
            PCA: Pcar_2093
            PPD: Ppro_3462
            AFW: Anae109_3034
            NAR: Saro_0259
            RBA: RB11217
            AVA: Ava_5053
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.24
            ExPASy - ENZYME nomenclature database: 3.2.2.24
            ExplorEnz - The Enzyme Database: 3.2.2.24
            ERGO genome analysis and discovery system: 3.2.2.24
            BRENDA, the Enzyme Database: 3.2.2.24
            CAS: 125626-63-3
///
ENTRY       EC 3.2.2.25                 Enzyme
NAME        N-methyl nucleosidase;
            7-methylxanthosine nucleosidase;
            N-MeNase;
            N-methyl nucleoside hydrolase;
            methylpurine nucleosidase
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing N-glycosyl compounds
SYSNAME     7-methylxanthosine ribohydrolase
REACTION    7-methylxanthosine + H2O = 7-methylxanthine + D-ribose [RN:R07918]
ALL_REAC    R07918
SUBSTRATE   7-methylxanthosine [CPD:C16352];
            H2O [CPD:C00001]
PRODUCT     7-methylxanthine [CPD:C16353];
            D-ribose [CPD:C00121]
COMMENT     The enzyme preferentially hydrolyses 3- and 7-methylpurine
            nucleosides, such as 3-methylxanthosine, 3-methyladenosine and
            7-methylguanosine. Hydrolysis of 7-methylxanthosine to form
            7-methylxanthine is the second step in the caffeine-biosynthesis
            pathway.
REFERENCE   1
  AUTHORS   Negishi, O., Ozawa, T. and Imagawa, H.
  TITLE     N-Methyl nucleosidase from tea leaves.
  JOURNAL   Agric. Biol. Chem. 52 (1988) 169-175.
PATHWAY     PATH: map00232  Caffeine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.2.25
            ExPASy - ENZYME nomenclature database: 3.2.2.25
            ExplorEnz - The Enzyme Database: 3.2.2.25
            ERGO genome analysis and discovery system: 3.2.2.25
            BRENDA, the Enzyme Database: 3.2.2.25
///
ENTRY       EC 3.2.3.1        Obsolete  Enzyme
NAME        Transferred to 3.2.1.147
CLASS       Hydrolases;
            Glycosylases;
            Hydrolysing S-glycosyl compounds (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.2.1.147 thioglucosidase (EC 3.2.3.1
            created 1972, deleted 2001)
STRUCTURES  PDB: 1DWA  1DWF  1DWG  1DWH  1DWI  1DWJ  1E4M  1E6Q  1E6S  1E6X  
                 1E70  1E71  1E72  1E73  1MYR  1W9B  1W9D  1WCG  
DBLINKS     IUBMB Enzyme Nomenclature: 3.2.3.1
            ExPASy - ENZYME nomenclature database: 3.2.3.1
            ExplorEnz - The Enzyme Database: 3.2.3.1
            ERGO genome analysis and discovery system: 3.2.3.1
            BRENDA, the Enzyme Database: 3.2.3.1
///
ENTRY       EC 3.3.1.1                  Enzyme
NAME        adenosylhomocysteinase;
            S-adenosylhomocysteine synthase;
            S-adenosylhomocysteine hydrolase (ambiguous);
            adenosylhomocysteine hydrolase;
            S-adenosylhomocysteinase;
            SAHase;
            AdoHcyase
CLASS       Hydrolases;
            Acting on ether bonds;
            Thioether and trialkylsulfonium hydrolases
SYSNAME     S-adenosyl-L-homocysteine hydrolase
REACTION    S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
            [RN:R00192]
ALL_REAC    R00192;
            (other) R04936
SUBSTRATE   S-adenosyl-L-homocysteine [CPD:C00021];
            H2O [CPD:C00001]
PRODUCT     L-homocysteine [CPD:C00155];
            adenosine [CPD:C00212]
COMMENT     The enzyme contains one tightly bound NAD+ per subunit. This appears
            to bring about a transient oxidation at C-3' of the
            5'-deoxyadenosine residue, thus labilizing the thioether bond [2]
            (for mechanism, click here), cf. EC 5.5.1.4, inositol-3-phosphate
            synthase.
REFERENCE   1  [PMID:13641268]
  AUTHORS   DE LA HABA G, CANTONI GL.
  TITLE     The enzymatic synthesis of S-adenosyl-L-homocysteine from adenosine
            and homocysteine.
  JOURNAL   J. Biol. Chem. 234 (1959) 603-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:762125]
  AUTHORS   Palmer JL, Abeles RH.
  TITLE     The mechanism of action of S-adenosylhomocysteinase.
  JOURNAL   J. Biol. Chem. 254 (1979) 1217-26.
PATHWAY     PATH: map00271  Methionine metabolism
            PATH: map00450  Selenoamino acid metabolism
ORTHOLOGY   KO: K01251  adenosylhomocysteinase
GENES       HSA: 191(AHCY) 23382(KIAA0828)
            MMU: 229709(Ahcyl1) 269378(Ahcy) 74340(4631427C17Rik)
            RNO: 29443(Ahcy)
            CFA: 475197(LOC475197) 477198(AHCY) 611790(AHCYL1)
            SSC: 497050(AHCY)
            GGA: 419146(AHCY) 419803(RCJMB04_10b17)
            XLA: 446493(MGC79134) 447361(MGC84148) 447640(MGC86404)
                 503682(sahh)
            DRE: 282675(ahcyl1) 387530(ahcy) 394240(ahcyl2)
            SPU: 574714(LOC574714) 592592(LOC592592)
            DME: Dmel_CG11654(Ahcy13) Dmel_CG8956(Ahcy89E) Dmel_CG9977
            CEL: K02F2.2
            ATH: AT3G23810(SAHH2)
            OSA: 4350455
            CME: CMB157C
            SCE: YER043C(SAH1)
            AGO: AGOS_AFR243C
            PIC: PICST_76463(SAH1)
            CGR: CAGL0C02189g
            SPO: SPBC8D2.18c
            ANI: AN1263.2
            AFM: AFUA_1G10130
            AOR: AO090038000417
            CNE: CND00240
            UMA: UM03734.1
            DDI: DDB_0191108(sahA)
            PFA: PFE1050w
            CPV: cgd3_80
            CHO: Chro.30017
            TAN: TA05430
            TPV: TP03_0160
            TBR: Tb11.01.1350
            TCR: 511229.50 511589.200
            LMA: LmjF36.3910
            EHI: 140.t00011 150.t00003
            SPE: Spro_1351
            XFA: XF1037
            XFT: PD0319(ahcY)
            XCC: XCC0752(sahH)
            XCB: XC_3482
            XCV: XCV0856(sahH)
            XAC: XAC0804(sahH)
            XOO: XOO3798(sahH)
            XOM: XOO_3579(XOO3579)
            PAE: PA0432(sahH)
            PAU: PA14_05620(sahH)
            PAP: PSPA7_0532(ahcY)
            PPF: Pput_4849
            PST: PSPTO_5068(ahcY)
            PSB: Psyr_0460
            PSP: PSPPH_0451(ahcY)
            PFL: PFL_5798(ahcY)
            PFO: Pfl_5280
            PEN: PSEEN5037(sahH)
            PMY: Pmen_0449
            PAR: Psyc_0968(ahcY)
            PCR: Pcryo_1448
            PRW: PsycPRwf_0915
            ACI: ACIAD2282(sahH)
            ACB: A1S_2334
            SPL: Spea_3401
            ILO: IL0485
            SDE: Sde_0469
            MAQ: Maqu_3043
            CBU: CBU_2031(ahcY)
            CBD: COXBU7E912_2132(ahcY)
            LPN: lpg2021(ahcY) lpg2172
            LPF: lpl1998(sahH)
            LPP: lpp2003(sahH) lpp2110
            MCA: MCA0138(ahcY)
            NOC: Noc_2679
            AEH: Mlg_2263
            HHA: Hhal_0050 Hhal_1675
            HCH: HCH_01532(ahcY) HCH_06377
            ABO: ABO_2618(ahcY)
            RMA: Rmag_0739
            VOK: COSY_0684(ahcY)
            CVI: CV_0965(ahcY)
            RSO: RSc0093(ahcY)
            REU: Reut_A0213
            REH: H16_A0244(ahcY)
            RME: Rmet_0170
            BMA: BMA2842(ahcY)
            BMV: BMASAVP1_A3417(ahcY)
            BML: BMA10299_A1701(ahcY)
            BMN: BMA10247_3134(ahcY)
            BXE: Bxe_A0178
            BVI: Bcep1808_0232
            BUR: Bcep18194_A3375
            BCN: Bcen_2835
            BCH: Bcen2424_0272
            BAM: Bamb_0186
            BPS: BPSL3290(ahcY)
            BPM: BURPS1710b_0057(ahcY)
            BPL: BURPS1106A_3919(ahcY)
            BPD: BURPS668_3838(ahcY)
            BTE: BTH_I3165(ahcY)
            PNU: Pnuc_2002
            BPE: BP3068(acyH)
            BPA: BPP0195(acyH)
            BBR: BB0198(acyH)
            RFR: Rfer_0652
            POL: Bpro_4132
            PNA: Pnap_0489
            AAV: Aave_4060
            AJS: Ajs_0618
            VEI: Veis_0656
            MPT: Mpe_A3286
            HAR: HEAR2950(sahH)
            MMS: mma_3196
            NEU: NE0660(ahcY)
            NET: Neut_1892
            NMU: Nmul_A2540
            EBA: ebA1874(ahcY)
            AZO: azo0587(acyH)
            DAR: Daro_0186
            TBD: Tbd_2519
            MFA: Mfla_0193
            GSU: GSU1875(ahcY)
            GME: Gmet_1294
            GUR: Gura_3005
            PCA: Pcar_1924
            PPD: Ppro_0041
            DVU: DVU0607(ahcY)
            DVL: Dvul_2347
            DDE: Dde_3134
            LIP: LI0670(ahcY)
            BBA: Bd1339(ahcY)
            ADE: Adeh_0156
            AFW: Anae109_0161
            MXA: MXAN_6516(ahcY)
            SAT: SYN_00416
            SFU: Sfum_0366
            PUB: SAR11_0197(ahcY)
            MLO: mll5088
            MES: Meso_3576
            PLA: Plav_0117
            SME: SMc02755(ahcY)
            SMD: Smed_3247
            ATU: Atu0029(ahcY)
            ATC: AGR_C_46
            RET: RHE_CH00031(ahcY)
            RLE: RL0031 RL0860
            BME: BMEI2029
            BMF: BAB1_2099(ahcY)
            BMS: BR2097(ahcY)
            BMB: BruAb1_2072(ahcY)
            BOV: BOV_2015(ahcY)
            OAN: Oant_0822
            BJA: bll5944(ahcY)
            BRA: BRADO5238(ahcY)
            BBT: BBta_5698(ahcY)
            RPA: RPA4015(ahcY)
            RPB: RPB_1589
            RPC: RPC_4153
            RPD: RPD_1597
            RPE: RPE_4203
            NWI: Nwi_2377
            NHA: Nham_2752
            BHE: BH00310(ahcY)
            BQU: BQ00290(ahcY)
            XAU: Xaut_0186
            CCR: CC_0257
            SIL: SPO3861(ahcY)
            SIT: TM1040_2835
            RSP: RSP_1514(ahcY)
            RSH: Rsph17029_0166
            RSQ: Rsph17025_2964
            JAN: Jann_1579 Jann_4074
            RDE: RD1_0465(ahcY)
            PDE: Pden_2682
            MMR: Mmar10_2440
            HNE: HNE_0788(ahcY)
            ZMO: ZMO0182(ahcY)
            NAR: Saro_2003
            SAL: Sala_0163
            SWI: Swit_2674
            ELI: ELI_05040
            GOX: GOX1078
            GBE: GbCGDNIH1_0064
            ACR: Acry_1228
            RRU: Rru_A3444
            MAG: amb4391
            MGM: Mmc1_3331
            ABA: Acid345_3662
            SUS: Acid_5273
            STH: STH1697
            CTH: Cthe_1200
            CHY: CHY_1440(ahcY)
            DSY: DSY1889
            DRM: Dred_2063
            SWO: Swol_1128
            CSC: Csac_1467
            MTA: Moth_0706
            MTU: Rv3248c(sahH)
            MTC: MT3346(ahcY)
            MBO: Mb3276c(sahH)
            MBB: BCG_3277c(sahH)
            MLE: ML0771(sahH)
            MPA: MAP3362c(sahH)
            MAV: MAV_4211(ahcY)
            MVA: Mvan_1746
            MGI: Mflv_4717
            MMC: Mmcs_1336
            MKM: Mkms_1354
            MJL: Mjls_1372
            CGL: NCgl0719(cgl0752)
            CGB: cg0860(sahH)
            CEF: CE0767
            CDI: DIP0692(ahcY)
            CJK: jk1637(sahH)
            NFA: nfa46130
            RHA: RHA1_ro06322(ahcY)
            SCO: SCO3023(sahH)
            SMA: SAV5053(sahH)
            CMI: CMM_1038(ahcY)
            ART: Arth_1198
            AAU: AAur_1316(ahcY)
            NCA: Noca_1432
            TFU: Tfu_2505
            FRA: Francci3_4092 Francci3_4454
            FAL: FRAAL1283(ahcY) FRAAL6781(ahcY)
            ACE: Acel_0468
            KRA: Krad_3838
            SEN: SACE_3897(sahH) SACE_6450(sahH)
            STP: Strop_0966
            RXY: Rxyl_0228 Rxyl_1998
            RBA: RB6285(sahH)
            LIL: LB106
            LIC: LIC20083(ahcY)
            LBJ: LBJ_4089(sahH)
            LBL: LBL_4105(sahH)
            SYN: sll1234(ahcY)
            SYW: SYNW0119(ahcY)
            SYC: syc0906_c(ahcY)
            SYF: Synpcc7942_0618
            SYD: Syncc9605_0102
            SYE: Syncc9902_0146
            SYG: sync_0108(ahcY)
            SYR: SynRCC307_0106(ahcY)
            SYX: SynWH7803_0169(ahcY)
            CYA: CYA_0709(ahcY)
            CYB: CYB_1751(ahcY)
            TEL: tll2390
            GVI: glr3183
            ANA: alr1414
            AVA: Ava_3963
            PMA: Pro1786(SAM1)
            PMM: PMM1625(ahcY)
            PMT: PMT0138(ahcY)
            PMN: PMN2A_1202
            PMI: PMT9312_1718
            PMB: A9601_18351(sam1)
            PMC: P9515_18141(sam1)
            PMF: P9303_01751(sam1)
            PMG: P9301_18171(sam1)
            PME: NATL1_20771(sam1)
            TER: Tery_2623
            BTH: BT_2797
            BFR: BF4468
            BFS: BF4263(sahH)
            SRU: SRU_1139(ahcY)
            CHU: CHU_0610(sahH)
            GFO: GFO_3067(ahcY)
            FJO: Fjoh_1579
            FPS: FP0189(ahcY)
            CTE: CT0721(sahH)
            CCH: Cag_1548
            CPH: Cpha266_0921
            PVI: Cvib_1122
            PLT: Plut_0671
            DET: DET0513(ahcY)
            DEH: cbdb_A477(ahcY)
            DEB: DehaBAV1_0489
            RRS: RoseRS_0488
            RCA: Rcas_0159
            AAE: aq_1180(sahH)
            TMA: TM0172
            TPT: Tpet_0753
            TME: Tmel_1765
            FNO: Fnod_0136
            MMP: MMP0920(ahcY)
            MMQ: MmarC5_0727
            MMZ: MmarC7_0167
            MAE: Maeo_0674
            MVN: Mevan_0213
            MAC: MA1275(ahcY2)
            MBA: Mbar_A3251
            MMA: MM_2278
            MBU: Mbur_1181
            MTP: Mthe_1004
            MHU: Mhun_0956
            MLA: Mlab_0916
            MEM: Memar_0646
            MBN: Mboo_0660
            MST: Msp_1085(ahcY)
            MSI: Msm_0727
            MKA: MK0368
            AFU: AF0886(ahcY-1) AF2000(ahcY-2)
            HAL: VNG2251G(achY)
            HMA: rrnAC2840(ahcY)
            HWA: HQ3414A(achY)
            NPH: NP0968A
            TAC: Ta0469
            TVO: TVN0986
            PTO: PTO1270
            PAB: PAB1372(ahcY)
            PFU: PF0343
            TKO: TK0028
            RCI: RRC46(ahcY)
            APE: APE_0624.1
            SMR: Smar_0929
            IHO: Igni_0040
            HBU: Hbut_1132
            SSO: SSO0755(ahcY)
            STO: ST0342
            SAI: Saci_0646(ahcY)
            MSE: Msed_2257
            PAI: PAE3140
            PIS: Pisl_0516
            PCL: Pcal_1787
            PAS: Pars_1679
            TPE: Tpen_0617
STRUCTURES  PDB: 1A7A  1B3R  1D4F  1K0U  1KY4  1KY5  1LI4  1V8B  1XWF  2H5L  
DBLINKS     IUBMB Enzyme Nomenclature: 3.3.1.1
            ExPASy - ENZYME nomenclature database: 3.3.1.1
            ExplorEnz - The Enzyme Database: 3.3.1.1
            ERGO genome analysis and discovery system: 3.3.1.1
            BRENDA, the Enzyme Database: 3.3.1.1
            CAS: 9025-54-1
///
ENTRY       EC 3.3.1.2                  Enzyme
NAME        adenosylmethionine hydrolase;
            S-adenosylmethionine cleaving enzyme;
            methylmethionine-sulfonium-salt hydrolase;
            adenosylmethionine lyase
CLASS       Hydrolases;
            Acting on ether bonds;
            Thioether and trialkylsulfonium hydrolases
SYSNAME     S-adenosyl-L-methionine hydrolase
REACTION    S-adenosyl-L-methionine + H2O = L-homoserine + methylthioadenosine
            [RN:R00175]
ALL_REAC    R00175
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019];
            H2O [CPD:C00001]
PRODUCT     L-homoserine [CPD:C00263];
            methylthioadenosine [CPD:C00170]
COMMENT     Also hydrolyses methylmethionine sulfonium salt to dimethyl sulfide
            and homoserine.
REFERENCE   1  [PMID:5849106]
  AUTHORS   Mazelis M, Levin B, Mallinson N.
  TITLE     Decomposition of methyl methionine sulfonium salts by a bacterial
            enzyme.
  JOURNAL   Biochim. Biophys. Acta. 105 (1965) 106-14.
DBLINKS     IUBMB Enzyme Nomenclature: 3.3.1.2
            ExPASy - ENZYME nomenclature database: 3.3.1.2
            ExplorEnz - The Enzyme Database: 3.3.1.2
            ERGO genome analysis and discovery system: 3.3.1.2
            BRENDA, the Enzyme Database: 3.3.1.2
            CAS: 37288-62-3
///
ENTRY       EC 3.3.1.3        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on ether bonds;
            Thioether and trialkylsulfonium hydrolases
COMMENT     Deleted entry: was transferred to EC 3.2.1.148,
            ribosylhomocysteinase, which has since been deleted. The activity is
            most probably attributable to EC 4.4.1.21, S-ribosylhomocysteine
            lyase. (EC 3.3.1.3 created 1972, deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 3.3.1.3
            ExPASy - ENZYME nomenclature database: 3.3.1.3
            ExplorEnz - The Enzyme Database: 3.3.1.3
            ERGO genome analysis and discovery system: 3.3.1.3
            BRENDA, the Enzyme Database: 3.3.1.3
///
ENTRY       EC 3.3.2.1                  Enzyme
NAME        isochorismatase;
            2,3-dihydro-2,3-dihydroxybenzoate synthase;
            2,3-dihydroxy-2,3-dihydrobenzoate synthase;
            2,3-dihydroxy-2,3-dihydrobenzoic synthase
CLASS       Hydrolases;
            Acting on ether bonds;
            Ether hydrolases
SYSNAME     isochorismate pyruvate-hydrolase
REACTION    isochorismate + H2O = 2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
            [RN:R03037]
ALL_REAC    R03037
SUBSTRATE   isochorismate [CPD:C00885];
            H2O [CPD:C00001]
PRODUCT     2,3-dihydroxy-2,3-dihydrobenzoate [CPD:C04171];
            pyruvate [CPD:C00022]
REFERENCE   1  [PMID:4306838]
  AUTHORS   Young IG, Gibson F.
  TITLE     Regulation of the enzymes involved in the biosynthesis of
            2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia
            coli.
  JOURNAL   Biochim. Biophys. Acta. 177 (1969) 401-11.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map01053  Biosynthesis of siderophore group nonribosomal
                            peptides
ORTHOLOGY   KO: K01252  enterobactin isochorismatase
            KO: K04777  vibriobactin-specific isochorismatase
            KO: K04779  isochorismatase
            KO: K05993  isochorismatase
GENES       AFM: AFUA_2G09355
            ECO: b0595(entB)
            ECJ: JW0587(entB)
            ECE: Z0737(entB)
            ECS: ECs0634
            ECC: c0682(entB)
            ECI: UTI89_C0597(entB)
            ECP: ECP_0627
            ECV: APECO1_1454(entB)
            ECW: EcE24377A_0615(entB)
            ECX: EcHS_A0646(entB)
            STY: STY0641(entB)
            STT: t2271(entB)
            SPT: SPA2137(entB)
            SEC: SC0628(entB)
            STM: STM0597(entB)
            SFL: SF0509(entB)
            SFX: S0515(entB)
            SFV: SFV_0543(entB)
            SSN: SSON_0546(entB)
            SBO: SBO_0456(entB)
            SDY: SDY_0526(entB)
            ECA: ECA0479(entB) ECA2702(ehpB)
            PLU: plu2728(entB)
            ENT: Ent638_1127
            SPE: Spro_3419
            VCH: VC0771
            VCO: VC0395_A0300(vibB)
            VVU: VV2_0838
            VVY: VVA1304
            PPR: PBPRB1822
            PSP: PSPPH_0909 PSPPH_1848
            PEN: PSEEN1524 PSEEN2254
            ACI: ACIAD2775(entB) ACIAD3473
            SHE: Shewmr4_1153
            SHM: Shewmr7_1224
            SHN: Shewana3_1154
            SDE: Sde_3398
            HCH: HCH_06565
            MMW: Mmwyl1_1623 Mmwyl1_1633
            AHA: AHA_0970 AHA_2477
            CVI: CV_1483(entB)
            RME: Rmet_5659
            BMA: BMAA0508
            BXE: Bxe_A1712 Bxe_B2021
            BUR: Bcep18194_A3602 Bcep18194_B1272 Bcep18194_B1569
            BCN: Bcen_2589 Bcen_3796 Bcen_3819
            BCH: Bcen2424_0515 Bcen2424_4549 Bcen2424_4572
            BAM: Bamb_0419 Bamb_1688
            BPS: BPSL3069 BPSS2153
            BPM: BURPS1710b_3597 BURPS1710b_A1005 BURPS1710b_A1265(entB)
            BPD: BURPS668_3584
            BTE: BTH_I2926 BTH_II2229
            SUN: SUN_0927
            MXA: MXAN_3644
            RET: RHE_PE00110 RHE_PE00112 RHE_PF00312(ypf00158)
            RLE: pRL100352 pRL100355 pRL120673
            BME: BMEII0079
            BMF: BAB2_0013
            BMS: BRA0014(entB)
            BMB: BruAb2_0014(entB)
            BOV: BOV_A0011(entB)
            BRA: BRADO2402 BRADO4247 BRADO5128 BRADO5505
            BBT: BBta_2755 BBta_4623 BBta_5596 BBta_5987
            RPC: RPC_4714
            JAN: Jann_3001
            PDE: Pden_2383
            ZMO: ZMO0758(dhbB) ZMO1887(entB)
            GOX: GOX2578
            RRU: Rru_A0757 Rru_A2717
            ABA: Acid345_2306
            BSU: BG11241(dhbB)
            BAN: BA1382 BA1620 BA2371(dhbB) BA2963 BA4482
            BAR: GBAA1382 GBAA1620 GBAA2371(dhbB) GBAA2963 GBAA4482
            BAA: BA_2137 BA_2865 BA_3470 BA_4929
            BAT: BAS1280 BAS1504 BAS2207 BAS2752 BAS4160
            BCE: BC1365 BC1594 BC2305 BC2947 BC4255
            BCA: BCE_1711 BCE_2401(dhbB) BCE_4338
            BCZ: BCZK0283 BCZK1254 BCZK1466 BCZK2130(entB) BCZK2680 BCZK4009
            BCY: Bcer98_1757
            BTK: BT9727_1252 BT9727_1476 BT9727_2146(entB) BT9727_2701
                 BT9727_3999
            BTL: BALH_0302 BALH_1432 BALH_2939(dhbB)
            BLI: BL04023(dhbB)
            BLD: BLi03899(dhbB)
            BCL: ABC0969
            BAY: RBAM_029020
            OIH: OB0025 OB0957(dhbB)
            SAC: SACOL0172(entB)
            SAA: SAUSA300_0189(entB)
            LLC: LACR_2347
            LLM: llmg_1538
            SPI: MGAS10750_Spy0259
            LSA: LSA0183 LSA1852
            LCA: LSEI_2755
            CKL: CKL_2496(phzA)
            MSM: MSMEG_4618
            CJK: jk1821(dhbB)
            RHA: RHA1_ro02318
            TFU: Tfu_1870
            FAL: FRAAL6302(dhbB) FRAAL6406
            SEN: SACE_1113 SACE_3852(dhbB) SACE_5166
            TTH: TTC1655
            TTJ: TTHA0328
            MMA: MM_1907
            HAL: VNG2537G(entB)
            HMA: rrnAC2100(entB1)
            HWA: HQ1060A(entB) HQ2280A(entB)
            NPH: NP1170A(entB_2) NP1274A(entB_1)
            TAC: Ta0454
            TVO: TVN0771
            PTO: PTO0118 PTO0621 PTO0671
            RCI: RCIX277(entB)
            APE: APE_2350.1
            SSO: SSO2455(entB-like2)
            STO: ST0582
            SAI: Saci_0543
            PAI: PAE3001
STRUCTURES  PDB: 1NF8  1NF9  2FQ1  
DBLINKS     IUBMB Enzyme Nomenclature: 3.3.2.1
            ExPASy - ENZYME nomenclature database: 3.3.2.1
            ExplorEnz - The Enzyme Database: 3.3.2.1
            ERGO genome analysis and discovery system: 3.3.2.1
            BRENDA, the Enzyme Database: 3.3.2.1
            CAS: 37288-64-5
///
ENTRY       EC 3.3.2.2                  Enzyme
NAME        alkenylglycerophosphocholine hydrolase;
            lysoplasmalogenase
CLASS       Hydrolases;
            Acting on ether bonds;
            Ether hydrolases
SYSNAME     1-(1-alkenyl)-sn-glycero-3-phosphocholine aldehydohydrolase
REACTION    1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O = an aldehyde +
            sn-glycero-3-phosphocholine [RN:R02745]
ALL_REAC    R02745
SUBSTRATE   1-(1-alkenyl)-sn-glycero-3-phosphocholine [CPD:C04517];
            H2O [CPD:C00001]
PRODUCT     aldehyde [CPD:C00071];
            sn-glycero-3-phosphocholine [CPD:C00670]
REFERENCE   1  [PMID:3753461]
  AUTHORS   Arthur G, Page L, Mock T, Choy PC.
  TITLE     The catabolism of plasmenylcholine in the guinea pig heart.
  JOURNAL   Biochem. J. 236 (1986) 475-80.
  ORGANISM  guinea pig
REFERENCE   2
  AUTHORS   Ellingson, J.S. and Lands, W.E.M.
  TITLE     Phospholipid reactivation of plasmalogen metabolism.
  JOURNAL   Lipids 3 (1968) 111-120.
REFERENCE   3
  AUTHORS   Warner, H.R. and Lands, W.E.M.
  TITLE     The metabolism of plasmalogen: enzymatic hydrolysis of the vinyl
            ether.
  JOURNAL   J. Biol. Chem. 236 (1961) 2404-2409.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00565  Ether lipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.3.2.2
            ExPASy - ENZYME nomenclature database: 3.3.2.2
            ExplorEnz - The Enzyme Database: 3.3.2.2
            ERGO genome analysis and discovery system: 3.3.2.2
            BRENDA, the Enzyme Database: 3.3.2.2
            CAS: 37288-65-6
///
ENTRY       EC 3.3.2.3        Obsolete  Enzyme
NAME        Transferred to 3.3.2.9 and 3.3.2.10
CLASS       Hydrolases;
            Acting on ether bonds;
            Ether hydrolases
COMMENT     Transferred entry: epoxide hydrolase. Now known to comprise two
            enzymes, microsomal epoxide hydrolase (EC 3.3.2.9) and soluble
            epoxide hydrolase (EC 3.3.2.10). (EC 3.3.2.3 created 1978, modified
            1999, deleted 2006)
GENES       REH: H16_A1767 H16_A1793
            FAL: FRAAL0555 FRAAL1691 FRAAL2594 FRAAL3740 FRAAL5461
STRUCTURES  PDB: 1CQZ  1CR6  1EHY  1EK1  1EK2  1QO7  1S8O  1VJ5  1ZD2  1ZD3  
                 1ZD4  1ZD5  2CJP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.3.2.3
            ExPASy - ENZYME nomenclature database: 3.3.2.3
            ExplorEnz - The Enzyme Database: 3.3.2.3
            ERGO genome analysis and discovery system: 3.3.2.3
            UM-BBD (Biocatalysis/Biodegradation Database): 3.3.2.3
            BRENDA, the Enzyme Database: 3.3.2.3
///
ENTRY       EC 3.3.2.4                  Enzyme
NAME        trans-epoxysuccinate hydrolase;
            trans-epoxysuccinate hydratase;
            tartrate epoxydase
CLASS       Hydrolases;
            Acting on ether bonds;
            Ether hydrolases
SYSNAME     trans-2,3-epoxysuccinate hydrolase
REACTION    trans-2,3-epoxysuccinate + H2O = meso-tartrate [RN:R02547]
ALL_REAC    R02547
SUBSTRATE   trans-2,3-epoxysuccinate [CPD:C03548];
            H2O [CPD:C00001]
PRODUCT     meso-tartrate [CPD:C00552]
COMMENT     Acts on both optical isomers of the substrate.
REFERENCE   1  [PMID:5782001]
  AUTHORS   Allen RH, Jakoby WB.
  TITLE     Tartaric acid metabolism. IX. Synthesis with tartrate epoxidase.
  JOURNAL   J. Biol. Chem. 244 (1969) 2078-84.
  ORGANISM  Pseudomonas putida [GN:ppu], Aspergillus fumigatus [GN:afm]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.3.2.4
            ExPASy - ENZYME nomenclature database: 3.3.2.4
            ExplorEnz - The Enzyme Database: 3.3.2.4
            ERGO genome analysis and discovery system: 3.3.2.4
            BRENDA, the Enzyme Database: 3.3.2.4
            CAS: 37290-73-6
///
ENTRY       EC 3.3.2.5                  Enzyme
NAME        alkenylglycerophosphoethanolamine hydrolase
CLASS       Hydrolases;
            Acting on ether bonds;
            Ether hydrolases
SYSNAME     1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine aldehydohydrolase
REACTION    1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O = an aldehyde +
            sn-glycero-3-phosphoethanolamine [RN:R03415]
ALL_REAC    R03415
SUBSTRATE   1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine [CPD:C04635];
            H2O [CPD:C00001]
PRODUCT     aldehyde [CPD:C00071];
            sn-glycero-3-phosphoethanolamine [CPD:C01233]
REFERENCE   1  [PMID:7239443]
  AUTHORS   Gunawan J, Debuch H.
  TITLE     Liberation of free aldehyde from
            1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine (lysoplasmalogen) by
            rat liver microsomes.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 362 (1981) 445-52.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00565  Ether lipid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.3.2.5
            ExPASy - ENZYME nomenclature database: 3.3.2.5
            ExplorEnz - The Enzyme Database: 3.3.2.5
            ERGO genome analysis and discovery system: 3.3.2.5
            BRENDA, the Enzyme Database: 3.3.2.5
            CAS: 78413-08-8
///
ENTRY       EC 3.3.2.6                  Enzyme
NAME        leukotriene-A4 hydrolase;
            LTA4 hydrolase;
            LTA4H;
            leukotriene A4 hydrolase
CLASS       Hydrolases;
            Acting on ether bonds;
            Ether hydrolases
SYSNAME     (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate
            hydrolase
REACTION    (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O =
            (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate
            [RN:R03057]
ALL_REAC    R03057
SUBSTRATE   (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate
            [CPD:C00909];
            H2O [CPD:C00001]
PRODUCT     (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate
            [CPD:C02165]
COMMENT     This is a bifunctional zinc metalloprotease that displays both
            epoxide hydrolase and aminopeptidase activities [4,6]. It
            preferentially cleaves tripeptides at an arginyl bond, with
            dipeptides and tetrapeptides being poorer substrates [6] (see EC
            3.4.11.6, aminopeptidase B). It also converts leukotriene A4 into
            leukotriene B4, unlike EC 3.2.2.10, soluble epoxide hydrolase, which
            converts leukotriene A4 into 5,6-dihydroxy-7,9,11,14-icosatetraenoic
            acid [3,4]. In vertebrates, five epoxide-hydrolase enzymes have been
            identified to date: EC 3.3.2.6 (leukotriene A4 hydrolase), EC
            3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal
            epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC
            3.3.2.11 (cholesterol-5,6-oxide hydrolase) [3].
REFERENCE   1  [PMID:3995081]
  AUTHORS   Evans JF, Dupuis P, Ford-Hutchinson AW.
  TITLE     Purification and characterisation of leukotriene A4 hydrolase from
            rat neutrophils.
  JOURNAL   Biochim. Biophys. Acta. 840 (1985) 43-50.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:3654641]
  AUTHORS   Minami M, Ohno S, Kawasaki H, Radmark O, Samuelsson B, Jornvall H,
            Shimizu T, Seyama Y, Suzuki K.
  TITLE     Molecular cloning of a cDNA coding for human leukotriene A4
            hydrolase. Complete primary structure of an enzyme involved in
            eicosanoid synthesis.
  JOURNAL   J. Biol. Chem. 262 (1987) 13873-6.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:3009453]
  AUTHORS   Haeggstrom J, Meijer J, Radmark O.
  TITLE     Leukotriene A4. Enzymatic conversion into
            5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid by mouse liver
            cytosolic epoxide hydrolase.
  JOURNAL   J. Biol. Chem. 261 (1986) 6332-7.
  ORGANISM  mouse [GN:mmu]
REFERENCE   4  [PMID:15748653]
  AUTHORS   Newman JW, Morisseau C, Hammock BD.
  TITLE     Epoxide hydrolases: their roles and interactions with lipid
            metabolism.
  JOURNAL   Prog. Lipid. Res. 44 (2005) 1-51.
  ORGANISM  rat [GN:rno], human [GN:hsa], mouse [GN:mmu], Saccharomyces
            cerevisiae [GN:sce], Xenopus laevis
REFERENCE   5  [PMID:11154734]
  AUTHORS   Fretland AJ, Omiecinski CJ.
  TITLE     Epoxide hydrolases: biochemistry and molecular biology.
  JOURNAL   Chem. Biol. Interact. 129 (2000) 41-59.
  ORGANISM  human [GN:hsa]
REFERENCE   6  [PMID:8157657]
  AUTHORS   Orning L, Gierse JK, Fitzpatrick FA.
  TITLE     The bifunctional enzyme leukotriene-A4 hydrolase is an arginine
            aminopeptidase of high efficiency and specificity.
  JOURNAL   J. Biol. Chem. 269 (1994) 11269-73.
  ORGANISM  human [GN:hsa], mouse [GN:mmu]
REFERENCE   7  [PMID:3038871]
  AUTHORS   Ohishi N, Izumi T, Minami M, Kitamura S, Seyama Y, Ohkawa S, Terao
            S, Yotsumoto H, Takaku F, Shimizu T.
  TITLE     Leukotriene A4 hydrolase in the human lung. Inactivation of the
            enzyme with leukotriene A4 isomers.
  JOURNAL   J. Biol. Chem. 262 (1987) 10200-5.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00590  Arachidonic acid metabolism
ORTHOLOGY   KO: K01254  leukotriene-A4 hydrolase
GENES       HSA: 4048(LTA4H)
            PTR: 452145(LTA4H)
            MMU: 16993(Lta4h)
            RNO: 299732(Lta4h)
            CFA: 482611(LTA4H)
            BTA: 507130(LTA4H)
            GGA: 417918(LTA4H)
            XLA: 432332(MGC78867)
            XTR: 448745(lta4h)
            DRE: 406575(lta4h)
            SPU: 592555(LOC592555)
            CEL: ZC416.6(protease)
            ATH: AT5G13520
            OSA: 4334583
            SCE: YNL045W
            AGO: AGOS_ADL233W
            PIC: PICST_76777(LKA4) PICST_82220(LTA4)
            CGR: CAGL0G01430g
            SPO: SPCC1322.05c
            ANI: AN5812.2
            AFM: AFUA_2G07520
            AOR: AO090011000940
            CNE: CNE04600
            DDI: DDB_0191291(lkhA)
            TET: TTHERM_00579060 TTHERM_00579070
            PHA: PSHAa2915
STRUCTURES  PDB: 1GW6  1H19  1HS6  1SQM  
DBLINKS     IUBMB Enzyme Nomenclature: 3.3.2.6
            ExPASy - ENZYME nomenclature database: 3.3.2.6
            ExplorEnz - The Enzyme Database: 3.3.2.6
            ERGO genome analysis and discovery system: 3.3.2.6
            BRENDA, the Enzyme Database: 3.3.2.6
            CAS: 90119-07-6
///
ENTRY       EC 3.3.2.7                  Enzyme
NAME        hepoxilin-epoxide hydrolase;
            hepoxilin epoxide hydrolase;
            hepoxylin hydrolase;
            hepoxilin A3 hydrolase
CLASS       Hydrolases;
            Acting on ether bonds;
            Ether hydrolases
SYSNAME     (5Z,9E,14Z)-(8xi,11R,12S)-11,12-epoxy-8-hydroxyicosa-5,9,14-trienoat
            e hydrolase
REACTION    (5Z,9E,14Z)-(8xi,11R,12S)-11,12-epoxy-8-hydroxyicosa-5,9,14-
            trienoate + H2O =
            (5Z,9E,14Z)-(8xi,11xi,12S)-8,11,12-trihydroxyicosa-5,9,14-trienoate
            [RN:R04609]
ALL_REAC    R04609;
            (other) R07036
SUBSTRATE   (5Z,9E,14Z)-(8xi,11R,12S)-11,12-epoxy-8-hydroxyicosa-5,9,14-
            trienoate [CPD:C04849];
            H2O [CPD:C00001]
PRODUCT     (5Z,9E,14Z)-(8xi,11xi,12S)-8,11,12-trihydroxyicosa-5,9,14-trienoate
            [CPD:C04843]
COMMENT     Converts hepoxilin A3 into trioxilin A3. Highly specific for the
            substrate, having only slight activity with other epoxides such as
            leukotriene A4 and styrene oxide [2]. Hepoxilin A3 is an
            hydroxy-epoxide derivative of arachidonic acid that is formed via
            the 12-lipoxygenase pathway [2]. It is probable that this enzyme
            plays a modulatory role in inflammation, vascular physiology,
            systemic glucose metabolism and neurological function [4]. In
            vertebrates, five epoxide-hydrolase enzymes have been identified to
            date: EC 3.3.2.6 (leukotriene-A4 hydrolase), EC 3.3.2.7
            (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide
            hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC 3.3.2.11
            (cholesterol 5,6-oxide hydrolase) [3].
REFERENCE   1  [PMID:3348791]
  AUTHORS   Pace-Asciak CR.
  TITLE     Formation and metabolism of hepoxilin A3 by the rat brain.
  JOURNAL   Biochem. Biophys. Res. Commun. 151 (1988) 493-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:2722835]
  AUTHORS   Pace-Asciak CR, Lee WS.
  TITLE     Purification of hepoxilin epoxide hydrolase from rat liver.
  JOURNAL   J. Biol. Chem. 264 (1989) 9310-3.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:11154734]
  AUTHORS   Fretland AJ, Omiecinski CJ.
  TITLE     Epoxide hydrolases: biochemistry and molecular biology.
  JOURNAL   Chem. Biol. Interact. 129 (2000) 41-59.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:15748653]
  AUTHORS   Newman JW, Morisseau C, Hammock BD.
  TITLE     Epoxide hydrolases: their roles and interactions with lipid
            metabolism.
  JOURNAL   Prog. Lipid. Res. 44 (2005) 1-51.
  ORGANISM  rat [GN:rno], human [GN:hsa], Balanus amphitrite, Elminius modestus
PATHWAY     PATH: map00590  Arachidonic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.3.2.7
            ExPASy - ENZYME nomenclature database: 3.3.2.7
            ExplorEnz - The Enzyme Database: 3.3.2.7
            ERGO genome analysis and discovery system: 3.3.2.7
            BRENDA, the Enzyme Database: 3.3.2.7
            CAS: 122096-98-4
///
ENTRY       EC 3.3.2.8                  Enzyme
NAME        limonene-1,2-epoxide hydrolase;
            limonene oxide hydrolase
CLASS       Hydrolases;
            Acting on ether bonds;
            Ether hydrolases
SYSNAME     limonene-1,2-epoxide hydrolase
REACTION    limonene-1,2-epoxide + H2O = limonene-1,2-diol [RN:R05784]
ALL_REAC    R05784
SUBSTRATE   limonene-1,2-epoxide [CPD:C07271];
            H2O [CPD:C00001]
PRODUCT     limonene-1,2-diol [CPD:C07276]
COMMENT     Involved in the monoterpene degradation pathway of the actinomycete
            Rhodococcus erythropolis. Enzyme hydrolyses several alicyclic and
            1-methyl-substituted epoxides, such as 1-methylcyclohexene oxide,
            indene oxide and cyclohexene oxide. It differs from the previously
            described epoxide hydrolases [EC 3.3.2.4 (trans-epoxysuccinate
            hydrolase), EC 3.3.2.6 (leukotriene-A4 hydrolase) and EC 3.3.2.7
            (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide
            hydrolase) and EC 3.3.2.10 (soluble epoxide hydrolase)] as it is not
            inhibited by 2-bromo-4'-nitroacetophenone, diethyl dicarbonate,
            4-fluorochalcone oxide or 1,10-phenanthroline.
REFERENCE   1  [PMID:9748436]
  AUTHORS   van der Werf MJ, Overkamp KM, de Bont JA.
  TITLE     Limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis DCL14
            belongs to a novel class of epoxide hydrolases.
  JOURNAL   J. Bacteriol. 180 (1998) 5052-7.
  ORGANISM  Rhodococcus erythropolis
REFERENCE   2  [PMID:9827564]
  AUTHORS   Barbirato F, Verdoes JC, de Bont JA, van der Werf MJ.
  TITLE     The Rhodococcus erythropolis DCL14 limonene-1,2-epoxide hydrolase
            gene encodes an enzyme belonging to a novel class of epoxide
            hydrolases.
  JOURNAL   FEBS. Lett. 438 (1998) 293-6.
  ORGANISM  Rhodococcus erythropolis
PATHWAY     PATH: map00903  Limonene and pinene degradation
ORTHOLOGY   KO: K10533  limonene-1,2-epoxide hydrolase
GENES       MBB: BCG_2754(ephG)
            FAL: FRAAL3429
STRUCTURES  PDB: 1NU3  1NWW  2BNG  
DBLINKS     IUBMB Enzyme Nomenclature: 3.3.2.8
            ExPASy - ENZYME nomenclature database: 3.3.2.8
            ExplorEnz - The Enzyme Database: 3.3.2.8
            ERGO genome analysis and discovery system: 3.3.2.8
            UM-BBD (Biocatalysis/Biodegradation Database): 3.3.2.8
            BRENDA, the Enzyme Database: 3.3.2.8
///
ENTRY       EC 3.3.2.9                  Enzyme
NAME        microsomal epoxide hydrolase;
            epoxide hydratase (ambiguous);
            microsomal epoxide hydratase (ambiguous);
            epoxide hydrase;
            microsomal epoxide hydrase;
            arene-oxide hydratase (ambiguous);
            benzo[a]pyrene-4,5-oxide hydratase;
            benzo(a)pyrene-4,5-epoxide hydratase;
            aryl epoxide hydrase (ambiguous);
            cis-epoxide hydrolase;
            mEH
CLASS       Hydrolases;
            Acting on ether bonds;
            Ether hydrolases
SYSNAME     cis-stilbene-oxide hydrolase
REACTION    cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol
            [RN:R07627]
ALL_REAC    R07627;
            (other) R07013 R07014 R07027 R07071 R07072 R07082
SUBSTRATE   cis-stilbene oxide [CPD:C16014];
            H2O [CPD:C00001]
PRODUCT     (+)-(1R,2R)-1,2-diphenylethane-1,2-diol [CPD:C16015]
COMMENT     This is a key hepatic enzyme that is involved in the metabolism of
            numerous xenobiotics, such as 1,3-butadiene oxide, styrene oxide and
            the polycyclic aromatic hydrocarbon benzo[a]pyrene 4,5-oxide
            [5---7]. In a series of oxiranes with a lipophilic substituent of
            sufficient size (styrene oxides), monosubstituted as well as 1,1-
            and cis-1,2-disubstituted oxiranes serve as substrates or inhibitors
            of the enzyme. However, trans-1,2-disubstituted, tri-and
            tetra-substituted oxiranes are not substrates [9]. The reaction
            involves the formation of an hydroxyalkyl---enzyme intermediate
            [10]. In vertebrates, five epoxide-hydrolase enzymes have been
            identified to date: EC 3.3.2.6 (leukotriene-A4 hydrolase), EC
            3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal
            epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC
            3.3.2.11 (cholesterol-5,6-oxide hydrolase) [7].
REFERENCE   1
  AUTHORS   Jakoby, W.B. and Fjellstedt, T.A.
  TITLE     Epoxidases.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 7, Academic Press,
            New York, 1972, p. 199-212.
REFERENCE   2  [PMID:240858]
  AUTHORS   Lu AY, Ryan D, Jerina DM, Daly JW, Levin W.
  TITLE     Liver microsomal expoxide hydrase. Solubilization, purification, and
            characterization.
  JOURNAL   J. Biol. Chem. 250 (1975) 8283-8.
  ORGANISM  guinea pig, human [GN:hsa], rat [GN:rno]
REFERENCE   3  [PMID:4463951]
  AUTHORS   Oesch F.
  TITLE     Purification and specificity of a human microsomal epoxide
            hydratase.
  JOURNAL   Biochem. J. 139 (1974) 77-88.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:4998715]
  AUTHORS   Oesch F, Daly J.
  TITLE     Solubilization, purification, and properties of a hepatic epoxide
            hydrase.
  JOURNAL   Biochim. Biophys. Acta. 227 (1971) 692-7.
  ORGANISM  guinea pig
REFERENCE   5  [PMID:7986671]
  AUTHORS   Bellucci G, Chiappe C, Ingrosso G.
  TITLE     Kinetics and stereochemistry of the microsomal epoxide
            hydrolase-catalyzed hydrolysis of cis-stilbene oxides.
  JOURNAL   Chirality. 6 (1994) 577-82.
  ORGANISM  rabbit
REFERENCE   6  [PMID:15822179]
  AUTHORS   Morisseau C, Hammock BD.
  TITLE     Epoxide hydrolases: mechanisms, inhibitor designs, and biological
            roles.
  JOURNAL   Annu. Rev. Pharmacol. Toxicol. 45 (2005) 311-33.
  ORGANISM  human [GN:hsa], rat [GN:rno]
REFERENCE   7  [PMID:11154734]
  AUTHORS   Fretland AJ, Omiecinski CJ.
  TITLE     Epoxide hydrolases: biochemistry and molecular biology.
  JOURNAL   Chem. Biol. Interact. 129 (2000) 41-59.
  ORGANISM  rat [GN:rno]
REFERENCE   8  [PMID:4584115]
  AUTHORS   Oesch F.
  TITLE     Mammalian epoxide hydrases: inducible enzymes catalysing the
            inactivation of carcinogenic and cytotoxic metabolites derived from
            aromatic and olefinic compounds.
  JOURNAL   Xenobiotica. 3 (1973) 305-40.
REFERENCE   9  [PMID:8199297]
  AUTHORS   Lacourciere GM, Armstrong RN.
  TITLE     Microsomal and soluble epoxide hydrolases are members of the same
            family of C-X bond hydrolase enzymes.
  JOURNAL   Chem. Res. Toxicol. 7 (1994) 121-4.
  ORGANISM  rat [GN:rno]
REFERENCE   10 [PMID:15748653]
  AUTHORS   Newman JW, Morisseau C, Hammock BD.
  TITLE     Epoxide hydrolases: their roles and interactions with lipid
            metabolism.
  JOURNAL   Prog. Lipid. Res. 44 (2005) 1-51.
  ORGANISM  human [GN:hsa], rat [GN:rno]
PATHWAY     PATH: map00980  Metabolism of xenobiotics by cytochrome P450
ORTHOLOGY   KO: K01253  microsomal epoxide hydrolase
GENES       HSA: 2052(EPHX1)
            MMU: 13849(Ephx1)
            RNO: 25315(Ephx1)
            CFA: 480113(EPHX1)
            SSC: 397639(EPHX1)
            GGA: 421321(EPHX1) 421447(LOC421447)
            XLA: 432100(MGC82277)
            DRE: 394043(zgc:56126)
            DME: Dmel_CG15102(Jheh2)
            CEL: W01A11.1
            PIC: PICST_38202(SEH1)
            ANI: AN3017.2
            AFM: AFUA_1G12880 AFUA_2G14860 AFUA_4G07410 AFUA_5G08810
                 AFUA_7G06650
            AOR: AO090005001384
            CNE: CNN02220
            UMA: UM05464.1
            BUR: Bcep18194_C7708
            MMS: mma_3333
            ABU: Abu_1144
            PUB: SAR11_0803(ephX1)
            RET: RHE_PF00546
            RLE: RL1848 pRL120297
            BRA: BRADO0927 BRADO1897 BRADO2514 BRADO3825
            BBT: BBta_2211 BBta_2860 BBta_4104 BBta_5344 BBta_7125
            HNE: HNE_2052
            GBE: GbCGDNIH1_0516 GbCGDNIH1_1779
            BCL: ABC1387
            MBB: BCG_1185(ephC) BCG_1977(ephB) BCG_3200c(mesTb)
                 BCG_3201c(mesTa) BCG_3728(ephE)
            MSM: MSMEG_0182 MSMEG_6858
            AAU: AAur_pTC10054
            FRA: Francci3_2199
            SEN: SACE_3441
DBLINKS     IUBMB Enzyme Nomenclature: 3.3.2.9
            ExPASy - ENZYME nomenclature database: 3.3.2.9
            ExplorEnz - The Enzyme Database: 3.3.2.9
            ERGO genome analysis and discovery system: 3.3.2.9
            BRENDA, the Enzyme Database: 3.3.2.9
///
ENTRY       EC 3.3.2.10                 Enzyme
NAME        soluble epoxide hydrolase;
            epoxide hydrase (ambiguous);
            epoxide hydratase (ambiguous);
            arene-oxide hydratase (ambiguous);
            aryl epoxide hydrase (ambiguous);
            trans-stilbene oxide hydrolase;
            sEH;
            cytosolic epoxide hydrolase
CLASS       Hydrolases;
            Acting on ether bonds;
            Ether hydrolases
SYSNAME     epoxide hydrolase
REACTION    an epoxide + H2O = a glycol [RN:R02822]
ALL_REAC    R02822 > R05842 R07108 R07109 R07110 R07111
SUBSTRATE   epoxide [CPD:C00722];
            H2O [CPD:C00001]
PRODUCT     glycol [CPD:C15588]
COMMENT     Catalyses the hydrolysis of trans-substituted epoxides, such as
            trans-stilbene oxide, as well as various aliphatic epoxides derived
            from fatty-acid metabolism [7]. It is involved in the metabolism of
            arachidonic epoxides (epoxyicosatrienoic acids; EETs) and linoleic
            acid epoxides. The EETs, which are endogenous chemical mediators,
            act at the vascular, renal and cardiac levels to regulate blood
            pressure [4,5]. The enzyme from mammals is a bifunctional enzyme:
            the C-terminal domain exhibits epoxide-hydrolase activity and the
            N-terminal domain has the activity of EC 3.1.3.76, lipid-phosphate
            phosphatase [1,2]. Like EC 3.3.2.9, microsomal epoxide hydrolase, it
            is probable that the reaction involves the formation of an
            hydroxyalkyl---enzyme intermediate [4,6]. The enzyme can also use
            leukotriene A4, the substrate of EC 3.3.2.6, leukotriene-A4
            hydrolase, but it forms 5,6-dihydroxy-7,9,11,14-icosatetraenoic acid
            rather than leukotriene B4 as the product [9,10]. In vertebrates,
            five epoxide-hydrolase enzymes have been identified to date: EC
            3.3.2.6 (leukotriene-A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide
            hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase), EC 3.3.2.10
            (soluble epoxide hydrolase) and EC 3.3.2.11 (cholesterol 5,6-oxide
            hydrolase) [7].
REFERENCE   1  [PMID:12574510]
  AUTHORS   Newman JW, Morisseau C, Harris TR, Hammock BD.
  TITLE     The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional
            enzyme with novel lipid phosphate phosphatase activity.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 1558-63.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:12574508]
  AUTHORS   Cronin A, Mowbray S, Durk H, Homburg S, Fleming I, Fisslthaler B,
            Oesch F, Arand M.
  TITLE     The N-terminal domain of mammalian soluble epoxide hydrolase is a
            phosphatase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 1552-7.
  ORGANISM  human [GN:hsa], mouse [GN:mmu]
REFERENCE   3  [PMID:4584115]
  AUTHORS   Oesch F.
  TITLE     Mammalian epoxide hydrases: inducible enzymes catalysing the
            inactivation of carcinogenic and cytotoxic metabolites derived from
            aromatic and olefinic compounds.
  JOURNAL   Xenobiotica. 3 (1973) 305-40.
REFERENCE   4  [PMID:15822179]
  AUTHORS   Morisseau C, Hammock BD.
  TITLE     Epoxide hydrolases: mechanisms, inhibitor designs, and biological
            roles.
  JOURNAL   Annu. Rev. Pharmacol. Toxicol. 45 (2005) 311-33.
  ORGANISM  human [GN:hsa], mouse [GN:mmu], rat [GN:rno]
REFERENCE   5  [PMID:11090543]
  AUTHORS   Yu Z, Xu F, Huse LM, Morisseau C, Draper AJ, Newman JW, Parker C,
            Graham L, Engler MM, Hammock BD, Zeldin DC, Kroetz DL.
  TITLE     Soluble epoxide hydrolase regulates hydrolysis of vasoactive
            epoxyeicosatrienoic acids.
  JOURNAL   Circ. Res. 87 (2000) 992-8.
  ORGANISM  human [GN:hsa], mouse [GN:mmu], rat [GN:rno]
REFERENCE   6
  AUTHORS   Lacourciere, G.M. and Armstrong, R.N.
  TITLE     The catalytic mechanism of microsomal epoxide hydrolase involves an
            ester intermediate.
  JOURNAL   J. Am. Chem. Soc. 115 (1993) 10466-10456.
REFERENCE   7  [PMID:11154734]
  AUTHORS   Fretland AJ, Omiecinski CJ.
  TITLE     Epoxide hydrolases: biochemistry and molecular biology.
  JOURNAL   Chem. Biol. Interact. 129 (2000) 41-59.
  ORGANISM  rat [GN:rno]
REFERENCE   8  [PMID:7840649]
  AUTHORS   Zeldin DC, Wei S, Falck JR, Hammock BD, Snapper JR, Capdevila JH.
  TITLE     Metabolism of epoxyeicosatrienoic acids by cytosolic epoxide
            hydrolase: substrate structural determinants of asymmetric
            catalysis.
  JOURNAL   Arch. Biochem. Biophys. 316 (1995) 443-51.
  ORGANISM  rat [GN:rno]
REFERENCE   9  [PMID:3009453]
  AUTHORS   Haeggstrom J, Meijer J, Radmark O.
  TITLE     Leukotriene A4. Enzymatic conversion into
            5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid by mouse liver
            cytosolic epoxide hydrolase.
  JOURNAL   J. Biol. Chem. 261 (1986) 6332-7.
  ORGANISM  mouse [GN:mmu]
REFERENCE   10 [PMID:15748653]
  AUTHORS   Newman JW, Morisseau C, Hammock BD.
  TITLE     Epoxide hydrolases: their roles and interactions with lipid
            metabolism.
  JOURNAL   Prog. Lipid. Res. 44 (2005) 1-51.
  ORGANISM  human [GN:hsa], mouse [GN:mmu], rat [GN:rno], Glycine max [GN:egma],
            Arabidopsis thaliana [GN:ath], Solanum tuberosum [GN:estu],
            Nicotiana tabacum, Brassica napus [GN:ebna], Ananas comosus,
            Euphorbia lagascae, Oryza sativa [GN:eosa], Citrus jambhiri,
            spinach, Malus pumila, Ricinus communis, Vicia sativa, Zea mays
            [GN:ezma], Triticum aestivum [GN:etae], celery, rainbow trout,
            Oryzias latipes, Pimphales promelas, Stenotomus chrysops, rabbit,
            guinea pig, hamster, pig [GN:ssc], horse, monkey, baboon
PATHWAY     PATH: map00590  Arachidonic acid metabolism
            PATH: map00625  Tetrachloroethene degradation
ORTHOLOGY   KO: K08726  soluble epoxide hydrolase
GENES       HSA: 2053(EPHX2)
            PTR: 464074(EPHX2)
            MMU: 13850(Ephx2)
            RNO: 65030(Ephx2)
            CFA: 477373(EPHX2)
            BTA: 511716(MGC139743)
            SSC: 414425(LOC414425)
            GGA: 421999(EPHX2)
            XLA: 447032(ephx2)
            XTR: 448759(ephx2)
            SPU: 590472(LOC590472)
            UMA: UM04063.1
            RPA: RPA2773
            RPB: RPB_2677
            CCR: CC_1229
            MTC: MT3719
            MBO: Mb1973(ephB)
            MSM: MSMEG_6106
            RBA: RB4968(ephA)
            CYA: CYA_0481
            CYB: CYB_0349
DBLINKS     IUBMB Enzyme Nomenclature: 3.3.2.10
            ExPASy - ENZYME nomenclature database: 3.3.2.10
            ExplorEnz - The Enzyme Database: 3.3.2.10
            ERGO genome analysis and discovery system: 3.3.2.10
            BRENDA, the Enzyme Database: 3.3.2.10
///
ENTRY       EC 3.3.2.11                 Enzyme
NAME        cholesterol-5,6-oxide hydrolase;
            cholesterol-epoxide hydrolase;
            ChEH
CLASS       Hydrolases;
            Acting on ether bonds;
            Ether hydrolases
SYSNAME     5,6alpha-epoxy-5alpha-cholestan-3beta-ol hydrolase
REACTION    (1) 5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O =
            cholestane-3beta,5alpha,6beta-triol [RN:R07597];
            (2) 5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O =
            cholestane-3beta,5alpha,6beta-triol [RN:R04792]
ALL_REAC    R04792 R07597
SUBSTRATE   5,6alpha-epoxy-5alpha-cholestan-3beta-ol [CPD:C15992];
            H2O [CPD:C00001];
            5,6beta-epoxy-5beta-cholestan-3beta-ol [CPD:C05418]
PRODUCT     cholestane-3beta,5alpha,6beta-triol
COMMENT     The enzyme appears to work equally well with either epoxide as
            substrate [3]. The product is a competitive inhibitor of the
            reaction. In vertebrates, five epoxide-hydrolase enzymes have been
            identified to date: EC 3.3.2.6 (leukotriene-A4 hydrolase), EC
            3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal
            epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC
            3.3.2.11 (cholesterol 5,6-oxide hydrolase) [3].
REFERENCE   1  [PMID:6401984]
  AUTHORS   Levin W, Michaud DP, Thomas PE, Jerina DM.
  TITLE     Distinct rat hepatic microsomal epoxide hydrolases catalyze the
            hydration of cholesterol 5,6 alpha-oxide and certain xenobiotic
            alkene and arene oxides.
  JOURNAL   Arch. Biochem. Biophys. 220 (1983) 485-94.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6690087]
  AUTHORS   Oesch F, Timms CW, Walker CH, Guenthner TM, Sparrow A, Watabe T,
            Wolf CR.
  TITLE     Existence of multiple forms of microsomal epoxide hydrolases with
            radically different substrate specificities.
  JOURNAL   Carcinogenesis. 5 (1984) 7-9.
  ORGANISM  rat [GN:rno], rabbit
REFERENCE   3  [PMID:3941086]
  AUTHORS   Sevanian A, McLeod LL.
  TITLE     Catalytic properties and inhibition of hepatic cholesterol-epoxide
            hydrolase.
  JOURNAL   J. Biol. Chem. 261 (1986) 54-9.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:11154734]
  AUTHORS   Fretland AJ, Omiecinski CJ.
  TITLE     Epoxide hydrolases: biochemistry and molecular biology.
  JOURNAL   Chem. Biol. Interact. 129 (2000) 41-59.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:15748653]
  AUTHORS   Newman JW, Morisseau C, Hammock BD.
  TITLE     Epoxide hydrolases: their roles and interactions with lipid
            metabolism.
  JOURNAL   Prog. Lipid. Res. 44 (2005) 1-51.
  ORGANISM  rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 3.3.2.11
            ExPASy - ENZYME nomenclature database: 3.3.2.11
            ExplorEnz - The Enzyme Database: 3.3.2.11
            ERGO genome analysis and discovery system: 3.3.2.11
            BRENDA, the Enzyme Database: 3.3.2.11
///
ENTRY       EC 3.3.2.-                  Enzyme
CLASS       Hydrolases;
            Acting on ether bonds;
            Ether hydrolases
REACTION    (1) 5,6beta-Epoxy-5beta-cholestane <=> 5alpha-Cholestan-5,6beta-diol
            [RN:R04791];
            (2) Cholesterol-5alpha,6beta-epoxide + H2O <=>
            3beta,5alpha,6beta-Cholestanetriol [RN:R04793];
            (3) 5,6beta-Epoxy-5alpha-cholestane <=>
            5alpha-Cholestan-5,6beta-diol [RN:R04794];
            (4) Phenanthrene-9,10-oxide + H2O <=>
            trans-9(S),10(S)-Dihydrodiolphenanthrene [RN:R05658];
            (5) 5,6-Epoxytetraene + H2O <=> Lipoxin A4 [RN:R07031];
            (6) 5,6-Epoxytetraene + H2O <=> Lipoxin B4 [RN:R07032];
            (7) Hepoxilin B3 + H2O <=> Trioxilin B3 [RN:R07037];
            (8) 12(13)-EpOME + H2O <=> 12,13-DHOME [RN:R07121];
            (9) 9(10)-EpOME + H2O <=> 9,10-DHOME [RN:R07122]
SUBSTRATE   5,6beta-Epoxy-5beta-cholestane [CPD:C05417];
            Cholesterol-5beta,6beta-epoxide [CPD:C05418];
            H2O [CPD:C00001];
            Cholesterol-5alpha,6beta-epoxide [CPD:C05419];
            5,6beta-Epoxy-5alpha-cholestane [CPD:C05423];
            Phenanthrene-9,10-oxide [CPD:C11429];
            5,6-Epoxytetraene [CPD:C14815];
            Hepoxilin B3 [CPD:C14810];
            12(13)-EpOME [CPD:C14826];
            9(10)-EpOME [CPD:C14825]
PRODUCT     5alpha-Cholestan-5,6beta-diol [CPD:C05424];
            3beta,5alpha,6beta-Cholestanetriol [CPD:C05425];
            trans-9(S),10(S)-Dihydrodiolphenanthrene [CPD:C11428];
            Lipoxin A4 [CPD:C06314];
            Lipoxin B4 [CPD:C06315];
            Trioxilin B3 [CPD:C14811];
            12,13-DHOME [CPD:C14829];
            9,10-DHOME [CPD:C14828]
///
ENTRY       EC 3.4.1.1        Obsolete  Enzyme
NAME        Transferred to 3.4.11.1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            alpha-Amino-acyl-peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.11.1, leucyl aminopeptidase (EC
            3.4.1.1 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.1.1
            ExPASy - ENZYME nomenclature database: 3.4.1.1
            ExplorEnz - The Enzyme Database: 3.4.1.1
            ERGO genome analysis and discovery system: 3.4.1.1
            BRENDA, the Enzyme Database: 3.4.1.1
///
ENTRY       EC 3.4.1.2        Obsolete  Enzyme
NAME        Transferred to 3.4.11.2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            alpha-Amino-acyl-peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.11.2, membrane alanyl aminopeptidase
            (EC 3.4.1.2 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.1.2
            ExPASy - ENZYME nomenclature database: 3.4.1.2
            ExplorEnz - The Enzyme Database: 3.4.1.2
            ERGO genome analysis and discovery system: 3.4.1.2
            BRENDA, the Enzyme Database: 3.4.1.2
///
ENTRY       EC 3.4.1.3        Obsolete  Enzyme
NAME        Transferred to 3.4.11.4
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            alpha-Amino-acyl-peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.11.4, tripeptide aminopeptidase (EC
            3.4.1.3 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.1.3
            ExPASy - ENZYME nomenclature database: 3.4.1.3
            ExplorEnz - The Enzyme Database: 3.4.1.3
            ERGO genome analysis and discovery system: 3.4.1.3
            BRENDA, the Enzyme Database: 3.4.1.3
///
ENTRY       EC 3.4.1.4        Obsolete  Enzyme
NAME        Transferred to 3.4.11.5
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            alpha-Amino-acyl-peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.11.5, prolyl aminopeptidase (EC
            3.4.1.4 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.1.4
            ExPASy - ENZYME nomenclature database: 3.4.1.4
            ExplorEnz - The Enzyme Database: 3.4.1.4
            ERGO genome analysis and discovery system: 3.4.1.4
            BRENDA, the Enzyme Database: 3.4.1.4
///
ENTRY       EC 3.4.2.1        Obsolete  Enzyme
NAME        Transferred to 3.4.17.1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl-amino-acid hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.17.1, carboxypeptidase A (EC 3.4.2.1
            created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.2.1
            ExPASy - ENZYME nomenclature database: 3.4.2.1
            ExplorEnz - The Enzyme Database: 3.4.2.1
            ERGO genome analysis and discovery system: 3.4.2.1
            BRENDA, the Enzyme Database: 3.4.2.1
///
ENTRY       EC 3.4.2.2        Obsolete  Enzyme
NAME        Transferred to 3.4.17.2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl-amino-acid hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.17.2, carboxypeptidase B (EC 3.4.2.2
            created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.2.2
            ExPASy - ENZYME nomenclature database: 3.4.2.2
            ExplorEnz - The Enzyme Database: 3.4.2.2
            ERGO genome analysis and discovery system: 3.4.2.2
            BRENDA, the Enzyme Database: 3.4.2.2
///
ENTRY       EC 3.4.2.3        Obsolete  Enzyme
NAME        Transferred to 3.4.17.4
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl-amino-acid hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.17.4, Gly-Xaa carboxypeptidase (EC
            3.4.2.3 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.2.3
            ExPASy - ENZYME nomenclature database: 3.4.2.3
            ExplorEnz - The Enzyme Database: 3.4.2.3
            ERGO genome analysis and discovery system: 3.4.2.3
            BRENDA, the Enzyme Database: 3.4.2.3
///
ENTRY       EC 3.4.3.1        Obsolete  Enzyme
NAME        Transferred to 3.4.13.18
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.13.18, cytosol nonspecific dipeptidase
            (EC 3.4.3.1 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.3.1
            ExPASy - ENZYME nomenclature database: 3.4.3.1
            ExplorEnz - The Enzyme Database: 3.4.3.1
            ERGO genome analysis and discovery system: 3.4.3.1
            BRENDA, the Enzyme Database: 3.4.3.1
///
ENTRY       EC 3.4.3.2        Obsolete  Enzyme
NAME        Transferred to 3.4.13.18
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.13.18, cytosol nonspecific dipeptidase
            (EC 3.4.3.2 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.3.2
            ExPASy - ENZYME nomenclature database: 3.4.3.2
            ExplorEnz - The Enzyme Database: 3.4.3.2
            ERGO genome analysis and discovery system: 3.4.3.2
            BRENDA, the Enzyme Database: 3.4.3.2
///
ENTRY       EC 3.4.3.3        Obsolete  Enzyme
NAME        Transferred to 3.4.13.3
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.13.3, Xaa-His dipeptidase (EC 3.4.3.3
            created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.3.3
            ExPASy - ENZYME nomenclature database: 3.4.3.3
            ExplorEnz - The Enzyme Database: 3.4.3.3
            ERGO genome analysis and discovery system: 3.4.3.3
            BRENDA, the Enzyme Database: 3.4.3.3
///
ENTRY       EC 3.4.3.4        Obsolete  Enzyme
NAME        Transferred to 3.4.13.5
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.13.5, Xaa-methyl-His dipeptidase (EC
            3.4.3.4 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.3.4
            ExPASy - ENZYME nomenclature database: 3.4.3.4
            ExplorEnz - The Enzyme Database: 3.4.3.4
            ERGO genome analysis and discovery system: 3.4.3.4
            BRENDA, the Enzyme Database: 3.4.3.4
///
ENTRY       EC 3.4.3.5        Obsolete  Enzyme
NAME        Transferred to 3.4.11.2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.11.2, membrane alanyl aminopeptidase
            (EC 3.4.3.5 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.3.5
            ExPASy - ENZYME nomenclature database: 3.4.3.5
            ExplorEnz - The Enzyme Database: 3.4.3.5
            ERGO genome analysis and discovery system: 3.4.3.5
            BRENDA, the Enzyme Database: 3.4.3.5
///
ENTRY       EC 3.4.3.6        Obsolete  Enzyme
NAME        Transferred to 3.4.13.18
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.13.18, cytosol nonspecific dipeptidase
            (EC 3.4.3.6 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.3.6
            ExPASy - ENZYME nomenclature database: 3.4.3.6
            ExplorEnz - The Enzyme Database: 3.4.3.6
            ERGO genome analysis and discovery system: 3.4.3.6
            BRENDA, the Enzyme Database: 3.4.3.6
///
ENTRY       EC 3.4.3.7        Obsolete  Enzyme
NAME        Transferred to 3.4.13.9
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.13.9, Xaa-Pro dipeptidase (EC 3.4.3.7
            created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.3.7
            ExPASy - ENZYME nomenclature database: 3.4.3.7
            ExplorEnz - The Enzyme Database: 3.4.3.7
            ERGO genome analysis and discovery system: 3.4.3.7
            BRENDA, the Enzyme Database: 3.4.3.7
///
ENTRY       EC 3.4.4.1        Obsolete  Enzyme
NAME        Transferred to 3.4.23.1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.23.1, pepsin A (EC 3.4.4.1 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.1
            ExPASy - ENZYME nomenclature database: 3.4.4.1
            ExplorEnz - The Enzyme Database: 3.4.4.1
            ERGO genome analysis and discovery system: 3.4.4.1
            BRENDA, the Enzyme Database: 3.4.4.1
///
ENTRY       EC 3.4.4.2        Obsolete  Enzyme
NAME        Transferred to 3.4.23.2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.23.2, pepsin B (EC 3.4.4.2 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.2
            ExPASy - ENZYME nomenclature database: 3.4.4.2
            ExplorEnz - The Enzyme Database: 3.4.4.2
            ERGO genome analysis and discovery system: 3.4.4.2
            BRENDA, the Enzyme Database: 3.4.4.2
///
ENTRY       EC 3.4.4.3        Obsolete  Enzyme
NAME        Transferred to 3.4.23.4
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.23.4, chymosin (EC 3.4.4.3 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.3
            ExPASy - ENZYME nomenclature database: 3.4.4.3
            ExplorEnz - The Enzyme Database: 3.4.4.3
            ERGO genome analysis and discovery system: 3.4.4.3
            BRENDA, the Enzyme Database: 3.4.4.3
///
ENTRY       EC 3.4.4.4        Obsolete  Enzyme
NAME        Transferred to 3.4.21.4
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.21.4, trypsin (EC 3.4.4.4 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.4
            ExPASy - ENZYME nomenclature database: 3.4.4.4
            ExplorEnz - The Enzyme Database: 3.4.4.4
            ERGO genome analysis and discovery system: 3.4.4.4
            BRENDA, the Enzyme Database: 3.4.4.4
///
ENTRY       EC 3.4.4.5        Obsolete  Enzyme
NAME        Transferred to 3.4.21.1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.21.1 chymotrypsin (EC 3.4.4.5 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.5
            ExPASy - ENZYME nomenclature database: 3.4.4.5
            ExplorEnz - The Enzyme Database: 3.4.4.5
            ERGO genome analysis and discovery system: 3.4.4.5
            BRENDA, the Enzyme Database: 3.4.4.5
///
ENTRY       EC 3.4.4.6        Obsolete  Enzyme
NAME        Transferred to 3.4.21.1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.21.1, chymotrypsin (EC 3.4.4.6 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.6
            ExPASy - ENZYME nomenclature database: 3.4.4.6
            ExplorEnz - The Enzyme Database: 3.4.4.6
            ERGO genome analysis and discovery system: 3.4.4.6
            BRENDA, the Enzyme Database: 3.4.4.6
///
ENTRY       EC 3.4.4.7        Obsolete  Enzyme
NAME        Transferred to 3.4.21.36 and 3.4.21.37
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: elastase. Now covered by EC 3.4.21.36, pancreatic
            elastase and EC 3.4.21.37, leukocyte elastase (EC 3.4.4.7 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.7
            ExPASy - ENZYME nomenclature database: 3.4.4.7
            ExplorEnz - The Enzyme Database: 3.4.4.7
            ERGO genome analysis and discovery system: 3.4.4.7
            BRENDA, the Enzyme Database: 3.4.4.7
///
ENTRY       EC 3.4.4.8        Obsolete  Enzyme
NAME        Transferred to 3.4.21.9
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.21.9, enteropeptidase (EC 3.4.4.8
            created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.8
            ExPASy - ENZYME nomenclature database: 3.4.4.8
            ExplorEnz - The Enzyme Database: 3.4.4.8
            ERGO genome analysis and discovery system: 3.4.4.8
            BRENDA, the Enzyme Database: 3.4.4.8
///
ENTRY       EC 3.4.4.9        Obsolete  Enzyme
NAME        Transferred to 3.4.14.1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.14.1, dipeptidyl-peptidase I (EC
            3.4.4.9 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.9
            ExPASy - ENZYME nomenclature database: 3.4.4.9
            ExplorEnz - The Enzyme Database: 3.4.4.9
            ERGO genome analysis and discovery system: 3.4.4.9
            BRENDA, the Enzyme Database: 3.4.4.9
///
ENTRY       EC 3.4.4.10       Obsolete  Enzyme
NAME        Transferred to 3.4.22.2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.22.2, papain (EC 3.4.4.10 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.10
            ExPASy - ENZYME nomenclature database: 3.4.4.10
            ExplorEnz - The Enzyme Database: 3.4.4.10
            ERGO genome analysis and discovery system: 3.4.4.10
            BRENDA, the Enzyme Database: 3.4.4.10
///
ENTRY       EC 3.4.4.11       Obsolete  Enzyme
NAME        Transferred to 3.4.22.6
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.22.6, chymopapain (EC 3.4.4.11 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.11
            ExPASy - ENZYME nomenclature database: 3.4.4.11
            ExplorEnz - The Enzyme Database: 3.4.4.11
            ERGO genome analysis and discovery system: 3.4.4.11
            BRENDA, the Enzyme Database: 3.4.4.11
///
ENTRY       EC 3.4.4.12       Obsolete  Enzyme
NAME        Transferred to 3.4.22.3
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.22.3, ficain (EC 3.4.4.12 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.12
            ExPASy - ENZYME nomenclature database: 3.4.4.12
            ExplorEnz - The Enzyme Database: 3.4.4.12
            ERGO genome analysis and discovery system: 3.4.4.12
            BRENDA, the Enzyme Database: 3.4.4.12
///
ENTRY       EC 3.4.4.13       Obsolete  Enzyme
NAME        Transferred to 3.4.21.5
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.21.5, thrombin (EC 3.4.4.13 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.13
            ExPASy - ENZYME nomenclature database: 3.4.4.13
            ExplorEnz - The Enzyme Database: 3.4.4.13
            ERGO genome analysis and discovery system: 3.4.4.13
            BRENDA, the Enzyme Database: 3.4.4.13
///
ENTRY       EC 3.4.4.14       Obsolete  Enzyme
NAME        Transferred to 3.4.21.7
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.21.7, plasmin (EC 3.4.4.14 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.14
            ExPASy - ENZYME nomenclature database: 3.4.4.14
            ExplorEnz - The Enzyme Database: 3.4.4.14
            ERGO genome analysis and discovery system: 3.4.4.14
            BRENDA, the Enzyme Database: 3.4.4.14
///
ENTRY       EC 3.4.4.15       Obsolete  Enzyme
NAME        Transferred to 3.4.23.15
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.23.15, renin (EC 3.4.4.15 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.15
            ExPASy - ENZYME nomenclature database: 3.4.4.15
            ExplorEnz - The Enzyme Database: 3.4.4.15
            ERGO genome analysis and discovery system: 3.4.4.15
            BRENDA, the Enzyme Database: 3.4.4.15
///
ENTRY       EC 3.4.4.16       Obsolete  Enzyme
NAME        Transferred to 3.4.21.62 and 3.4.21.63 and 3.4.21.64 and 3.4.21.65
            and 3.4.21.66 and 3.4.21.67
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now covered by the microbial serine proteinases
            EC 3.4.21.62 (subtilisin), EC 3.4.21.63 (oryzin), EC 3.4.21.64
            (endopeptidase K), EC 3.4.21.65 (thermomycolin), EC 3.4.21.66
            (thermitase) and EC 3.4.21.67 (ndopeptidase So) (EC 3.4.4.16 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.16
            ExPASy - ENZYME nomenclature database: 3.4.4.16
            ExplorEnz - The Enzyme Database: 3.4.4.16
            ERGO genome analysis and discovery system: 3.4.4.16
            BRENDA, the Enzyme Database: 3.4.4.16
///
ENTRY       EC 3.4.4.17       Obsolete  Enzyme
NAME        Transferred to 3.4.23.20 and 3.4.23.21 and 3.4.23.22 and 3.4.23.23
            and 3.4.23.24 and 3.4.23.25 and 3.4.23.26 and 3.4.21.103 and
            3.4.23.28 and 3.4.23.29 and 3.4.23.30
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now covered by the microbial aspartic proteinases
            EC 3.4.23.20 (penicillopepsin), EC 3.4.23.21 (rhizopuspepsin), EC
            3.4.23.22 (endothiapepsin), EC 3.4.23.23 (mucorpepsin), EC 3.4.23.24
            (candidapepsin), EC 3.4.23.25 (saccharopepsin), EC 3.4.23.26
            (rhodotorulapepsin), EC 3.4.21.103 (physarolisin), EC 3.4.23.28
            (acrocylindropepsin), EC 3.4.23.29 (polyporopepsin) and EC 3.4.23.30
            (pycnoporopepsin) (EC 3.4.4.17 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.17
            ExPASy - ENZYME nomenclature database: 3.4.4.17
            ExplorEnz - The Enzyme Database: 3.4.4.17
            ERGO genome analysis and discovery system: 3.4.4.17
            BRENDA, the Enzyme Database: 3.4.4.17
///
ENTRY       EC 3.4.4.18       Obsolete  Enzyme
NAME        Transferred to 3.4.22.10
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.22.10, streptopain (EC 3.4.4.18
            created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.18
            ExPASy - ENZYME nomenclature database: 3.4.4.18
            ExplorEnz - The Enzyme Database: 3.4.4.18
            ERGO genome analysis and discovery system: 3.4.4.18
            BRENDA, the Enzyme Database: 3.4.4.18
///
ENTRY       EC 3.4.4.19       Obsolete  Enzyme
NAME        Transferred to 3.4.24.3
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.24.3, microbial collagenase (EC
            3.4.4.19 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.19
            ExPASy - ENZYME nomenclature database: 3.4.4.19
            ExplorEnz - The Enzyme Database: 3.4.4.19
            ERGO genome analysis and discovery system: 3.4.4.19
            BRENDA, the Enzyme Database: 3.4.4.19
///
ENTRY       EC 3.4.4.20       Obsolete  Enzyme
NAME        Transferred to 3.4.22.8
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.22.8, clostripain (EC 3.4.4.20 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.20
            ExPASy - ENZYME nomenclature database: 3.4.4.20
            ExplorEnz - The Enzyme Database: 3.4.4.20
            ERGO genome analysis and discovery system: 3.4.4.20
            BRENDA, the Enzyme Database: 3.4.4.20
///
ENTRY       EC 3.4.4.21       Obsolete  Enzyme
NAME        Transferred to 3.4.21.34 and 3.4.21.35
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.21.34, plasma kallikrein and EC
            3.4.21.35, tissue kallikrein (EC 3.4.4.21 created 1965, deleted
            1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.21
            ExPASy - ENZYME nomenclature database: 3.4.4.21
            ExplorEnz - The Enzyme Database: 3.4.4.21
            ERGO genome analysis and discovery system: 3.4.4.21
            BRENDA, the Enzyme Database: 3.4.4.21
///
ENTRY       EC 3.4.4.22       Obsolete  Enzyme
NAME        Transferred to 3.4.23.3
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.23.3, gastricsin (EC 3.4.4.22 created
            1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.22
            ExPASy - ENZYME nomenclature database: 3.4.4.22
            ExplorEnz - The Enzyme Database: 3.4.4.22
            ERGO genome analysis and discovery system: 3.4.4.22
            BRENDA, the Enzyme Database: 3.4.4.22
///
ENTRY       EC 3.4.4.23       Obsolete  Enzyme
NAME        Transferred to 3.4.23.5
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.4.23.5, cathepsin D (EC 3.4.4.23 created
            1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.23
            ExPASy - ENZYME nomenclature database: 3.4.4.23
            ExplorEnz - The Enzyme Database: 3.4.4.23
            ERGO genome analysis and discovery system: 3.4.4.23
            BRENDA, the Enzyme Database: 3.4.4.23
///
ENTRY       EC 3.4.4.24       Obsolete  Enzyme
NAME        Transferred to 3.4.22.32 and 3.4.22.33
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Transferred entry: now covered by EC 3.4.22.32, stem bromelain and
            EC 3.4.22.33, fruit bromelain (EC 3.4.4.24 created 1965, deleted
            1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.24
            ExPASy - ENZYME nomenclature database: 3.4.4.24
            ExplorEnz - The Enzyme Database: 3.4.4.24
            ERGO genome analysis and discovery system: 3.4.4.24
            BRENDA, the Enzyme Database: 3.4.4.24
///
ENTRY       EC 3.4.4.25       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl peptide hydrolases (deleted sub-subclass)
COMMENT     Deleted entry: Streptomyces alkalophilic keratinase (EC 3.4.4.25
            created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.4.25
            ExPASy - ENZYME nomenclature database: 3.4.4.25
            ExplorEnz - The Enzyme Database: 3.4.4.25
            ERGO genome analysis and discovery system: 3.4.4.25
            BRENDA, the Enzyme Database: 3.4.4.25
///
ENTRY       EC 3.4.11.1                 Enzyme
NAME        leucyl aminopeptidase;
            leucine aminopeptidase;
            leucyl peptidase;
            peptidase S;
            cytosol aminopeptidase;
            cathepsin III;
            L-leucine aminopeptidase;
            leucinaminopeptidase;
            leucinamide aminopeptidase;
            FTBL proteins;
            proteinates FTBL;
            aminopeptidase II;
            aminopeptidase III;
            aminopeptidase I
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of an N-terminal amino acid, Xaa!Yaa-, in which Xaa is
            preferably Leu, but may be other amino acids including Pro although
            not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl
            esters are also readily hydrolysed, but rates on arylamides are
            exceedingly low
COFACTOR    Zinc [CPD:C00038]
INHIBITOR   Amastatin [CPD:C01552]
EFFECTOR    Heavy metal ion [CPD:C02285]
COMMENT     A zinc enzyme isolated from pig kidney and cattle lens; activated by
            heavy metal ions. Type example of peptidase family M17.
REFERENCE   1
  AUTHORS   Himmelhoch, S.R.
  TITLE     Leucine aminopeptidase from swine kidney.
  JOURNAL   Methods Enzymol. 19 (1970) 508-513.
  ORGANISM  pig [GN:ssc]
REFERENCE   2
  AUTHORS   Delange, R.J. and Smith, E.L.
  TITLE     Leucine aminopeptidase and other N-terminal exopeptidases.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 3, Academic Press,
            New York, 1971, p. 81-118.
REFERENCE   3  [PMID:7417261]
  AUTHORS   van Loon-Klaassen LA, Cuypers HT, van Westreenen H, de Jong WW,
            Bloemendal H.
  TITLE     The primary structure of bovine lens leucine aminopeptidase.
            Complete amino acid sequence of the N-terminal cyanogen bromide
            fragment and site of limited tryptic digestion.
  JOURNAL   Biochem. Biophys. Res. Commun. 95 (1980) 334-41.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K01255  leucyl aminopeptidase
GENES       HSA: 51056(LAP3)
            PTR: 461132(LAP3)
            MMU: 66988(Lap3)
            RNO: 289668(Lap3)
            CFA: 479081(LAP3)
            GGA: 425306(RCJMB04_15i13)
            XLA: 414652(MGC81140)
            XTR: 496537(lap3)
            DRE: 562854(lap3)
            DME: Dmel_CG13340 Dmel_CG32351 Dmel_CG4439
                 Dmel_CG7340(granny-smith) Dmel_CG9285(Dip-B)
            CEL: W07G4.4 ZK353.6(lap-1)
            ATH: AT2G24200 AT4G30910 AT4G30920
            OSA: 4330998 4352123
            CME: CMI185C
            SPO: SPAC13A11.05
            UMA: UM03308.1
            ECU: ECU10_1770i
            DDI: DDB_0231024(lap)
            PFA: PF14_0439
            CPV: cgd5_2600
            CHO: Chro.50116
            TAN: TA09045
            TPV: TP04_0561
            TET: TTHERM_00263380
            TBR: Tb927.8.3060
            TCR: 509859.40 510515.60
            LMA: LmjF23.0950
            ECO: b4260(pepA)
            ECJ: JW4217(pepA)
            ECE: Z5872(pepA)
            ECS: ECs5237
            ECC: c5360(pepA)
            ECI: UTI89_C4866(pepA)
            ECP: ECP_4509
            ECV: APECO1_2134(pepA)
            ECW: EcE24377A_4832(pepA)
            ECX: EcHS_A4516
            STY: STY4816
            STT: t4512
            SPT: SPA4278(pepA)
            SEC: SC4333(pepA)
            STM: STM4477(pepA)
            YPE: YPO3441(pepA)
            YPK: y0746(pepA)
            YPM: YP_0643(pepA)
            YPA: YPA_2942
            YPN: YPN_0647
            YPP: YPDSF_3251
            YPS: YPTB0531(pepA)
            YPI: YpsIP31758_3543(pepA)
            YEN: YE0500(carP)
            SFL: SF4229(pepA)
            SFX: S4490(pepA)
            SFV: SFV_4233(pepA)
            SSN: SSON_4445(pepA)
            SBO: SBO_4180(pepA)
            SDY: SDY_4284(pepA)
            ECA: ECA0404(pepA)
            PLU: plu4481(pepA)
            BUC: BU367(pepA)
            BAS: BUsg355(pepA)
            BAB: bbp332(pepA)
            WBR: WGLp459(pepA)
            SGL: SG2109
            ENT: Ent638_2983 Ent638_3648
            KPN: KPN_04665(pepA)
            SPE: Spro_0562 Spro_2848
            BFL: Bfl035(pepA)
            BPN: BPEN_035(pepA)
            HIN: HI1705(pepA)
            HIT: NTHI2013(pepA)
            HIP: CGSHiEE_03515
            HIQ: CGSHiGG_02300
            HDU: HD0555(pepA)
            HSO: HS_0516(pepA)
            PMU: PM0195(pepA)
            MSU: MS1550(pepB)
            APL: APL_1101(pepA)
            ASU: Asuc_0952
            XFA: XF0138 XF0280
            XFT: PD0106(pepA) PD0226(pepA)
            XCC: XCC0649(pepA) XCC3904
            XCB: XC_3585 XC_3992
            XCV: XCV3681(pepA) XCV4080(pepA2)
            XAC: XAC3556(pepA) XAC3987
            XOO: XOO0450 XOO0834(pepA)
            XOM: XOO_0413(XOO0413) XOO_0760(XOO0760)
            VCH: VC2501
            VCO: VC0395_A2083(pepA)
            VVU: VV1_1476
            VVY: VV2907
            VPA: VP2644
            VFI: VF0413
            PPR: PBPRA0484
            PAE: PA3831(pe)
            PAU: PA14_14470(pepA)
            PPU: PP_0980(pepA)
            PPF: Pput_1018
            PST: PSPTO_1271(pepA)
            PSB: Psyr_1091(pepA)
            PSP: PSPPH_1157(pepA)
            PFL: PFL_1066(pepA)
            PFO: Pfl_0989
            PEN: PSEEN4443(pepA)
            PMY: Pmen_3527
            PAR: Psyc_0043(pepA)
            PCR: Pcryo_0051
            PRW: PsycPRwf_0053
            ACI: ACIAD0253(pepA)
            SON: SO_0959(pepA-1) SO_1117 SO_1368(pepA-2)
            SDN: Sden_0871
            SFR: Sfri_0924 Sfri_0963
            SAZ: Sama_0616 Sama_0795
            SBL: Sbal_0850 Sbal_3109
            SBM: Shew185_3119 Shew185_3514
            SLO: Shew_0939 Shew_1677
            SPC: Sputcn32_0897 Sputcn32_1178
            SSE: Ssed_1014 Ssed_1488
            SPL: Spea_0388 Spea_0910 Spea_2759
            SHE: Shewmr4_0802 Shewmr4_0949 Shewmr4_2827
            SHM: Shewmr7_0987 Shewmr7_2909 Shewmr7_3221
            SHN: Shewana3_0951 Shewana3_3006 Shewana3_3324
            SHW: Sputw3181_2986 Sputw3181_3275
            ILO: IL1948(pepA)
            CPS: CPS_0740(pepA) CPS_4956
            PHA: PSHAa1484 PSHAa2388 PSHAa2423(pepA) PSHAb0302
            PAT: Patl_3562
            SDE: Sde_1372
            PIN: Ping_0395
            MAQ: Maqu_0961
            CBU: CBU_0572
            LPN: lpg2631(pepA) lpg2634
            LPF: lpl2556(pepA) lpl2559
            LPP: lpp2684(pepA) lpp2687
            MCA: MCA2099(pepA)
            FTU: FTT1094c FTT1318c(pepA)
            FTF: FTF1094c FTF1318c(pepA)
            FTL: FTL_1108 FTL_1479
            FTH: FTH_1081 FTH_1433(pepA)
            FTN: FTN_0660(pepA) FTN_0780(pepB)
            TCX: Tcr_1748
            NOC: Noc_0289
            AEH: Mlg_0558
            HHA: Hhal_0681
            HCH: HCH_01931
            CSA: Csal_2918
            ABO: ABO_0495(pepA)
            MMW: Mmwyl1_4007
            AHA: AHA_2386 AHA_3700(pepA)
            DNO: DNO_1151
            BCI: BCI_0287(pepA)
            RMA: Rmag_0211
            VOK: COSY_0207(pepA)
            NMA: NMA1758(pepA)
            NMC: NMC1489(pepA)
            NGO: NGO1227
            CVI: CV_2914(pepA)
            RSO: RSc2415(pepA)
            REU: Reut_A2683(pepA)
            REH: H16_A2990
            RME: Rmet_2807
            BMA: BMA0672(pepA)
            BMV: BMASAVP1_A2339(pepA)
            BML: BMA10299_A2947(pepA)
            BMN: BMA10247_1653(pepA)
            BXE: Bxe_A3638
            BVI: Bcep1808_2549
            BUR: Bcep18194_A5797(pepA)
            BCN: Bcen_1855
            BCH: Bcen2424_2466
            BAM: Bamb_2515
            BPS: BPSL0965(pepA)
            BPM: BURPS1710b_1176(pepA)
            BPL: BURPS1106A_1022(pepA)
            BPD: BURPS668_1015(pepA)
            BTE: BTH_I0823
            PNU: Pnuc_0623
            BPE: BP2421(pepA)
            BPA: BPP3285(pepA)
            BBR: BB3736(pepA)
            RFR: Rfer_2116
            POL: Bpro_2408
            PNA: Pnap_2169
            AAV: Aave_3162
            AJS: Ajs_1921
            VEI: Veis_4922
            MPT: Mpe_A1942
            HAR: HEAR2401(pepA)
            MMS: mma_2461
            NEU: NE0441 NE0569
            NET: Neut_0599 Neut_1022
            NMU: Nmul_A0746 Nmul_A1961
            EBA: ebA7174
            AZO: azo2904(pepA)
            DAR: Daro_2961 Daro_3082
            TBD: Tbd_0580 Tbd_0656
            MFA: Mfla_0222 Mfla_2073
            HPY: HP0570
            HPJ: jhp0517(pepA)
            HPA: HPAG1_0549
            HHE: HH1372(pepA)
            HAC: Hac_1442(pepA)
            WSU: WS1353(pepA)
            TDN: Tmden_1120
            CJE: Cj0929(pepA)
            CJR: CJE1007
            CJU: C8J_0866(pepA)
            CFF: CFF8240_1167
            CCV: CCV52592_1317
            CHA: CHAB381_1046
            CCO: CCC13826_0528
            ABU: Abu_0702(pepA)
            NIS: NIS_0704
            SUN: SUN_0651
            GSU: GSU0332(pepA)
            GME: Gmet_3361
            GUR: Gura_4252
            PCA: Pcar_0200
            DVU: DVU0415(pepA)
            DVL: Dvul_2519
            DDE: Dde_0568
            LIP: LI0686(pepA)
            BBA: Bd2554(pepA) Bd3755(pepA)
            DPS: DP2604
            ADE: Adeh_4097
            AFW: Anae109_0328
            MXA: MXAN_4963
            SAT: SYN_02170
            SFU: Sfum_2081
            RPR: RP142(pepA)
            RTY: RT0131(pepA)
            RCO: RC0184(pepA)
            RFE: RF_1143(pepA)
            RBE: RBE_0351(pepA)
            RAK: A1C_01025
            RBO: A1I_06015
            RCM: A1E_00740
            RRI: A1G_01050
            OTS: OTBS_1135(pepA)
            WOL: WD0054(pepA)
            WBM: Wbm0630
            AMA: AM956(pepA)
            APH: APH_0231(pepA)
            ERU: Erum6380(pepA)
            ERW: ERWE_CDS_06690(pepA)
            ERG: ERGA_CDS_06600(pepA)
            ECN: Ecaj_0642
            ECH: ECH_0369(pepA)
            NSE: NSE_0475(pepA)
            PUB: SAR11_0716(pepA)
            MLO: mll0602 mlr5606 mlr7868
            MES: Meso_1756 Meso_3953
            PLA: Plav_0242 Plav_3337
            SME: SMc00585(pepA) SMc02825
            SMD: Smed_0766 Smed_3359
            ATU: Atu0214 Atu1110(pepA)
            ATC: AGR_C_2055 AGR_C_368
            RET: RHE_CH00213(ypch00075) RHE_CH01456(pepA)
            RLE: RL0222 RL1571(pepA)
            BME: BMEI1261 BMEI1948
            BMF: BAB1_0710 BAB1_2182
            BMS: BR0689 BR2181
            BMB: BruAb1_0708 BruAb1_2154
            OAN: Oant_0730 Oant_2600
            BJA: bll1431 blr4108(pepA)
            BRA: BRADO1011 BRADO3328
            BBT: BBta_3832 BBta_7039
            RPA: RPA3060 RPA3685
            RPB: RPB_1777 RPB_2481
            RPC: RPC_2314 RPC_3720
            RPD: RPD_2965 RPD_3527
            RPE: RPE_3291 RPE_3758
            NWI: Nwi_0294 Nwi_1676
            NHA: Nham_0384 Nham_2339
            BHE: BH02040(pepA)
            BQU: BQ01920(pepA)
            BBK: BARBAKC583_1264
            XAU: Xaut_0281 Xaut_1462
            CCR: CC_0977 CC_1692 CC_2937
            SIL: SPO2453(pepA) SPO3717
            SIT: TM1040_0950 TM1040_3455
            RSP: RSP_1379 RSP_2899
            RSH: Rsph17029_0047 Rsph17029_1543
            RSQ: Rsph17025_0038 Rsph17025_1122
            JAN: Jann_0106 Jann_1815
            RDE: RD1_0314(pepA) RD1_3118(pepA)
            PDE: Pden_0903 Pden_2707 Pden_4634
            MMR: Mmar10_0428 Mmar10_1227
            HNE: HNE_2244(pepA) HNE_2273 HNE_3007
            ZMO: ZMO0806(pepA) ZMO1309(pepA)
            NAR: Saro_0890 Saro_1112
            SAL: Sala_0713 Sala_1761 Sala_2389
            SWI: Swit_0098 Swit_0412
            ELI: ELI_01680 ELI_08880
            GOX: GOX0293 GOX1918
            GBE: GbCGDNIH1_0317 GbCGDNIH1_2202
            ACR: Acry_0419 Acry_1204
            RRU: Rru_A0138 Rru_A0454 Rru_A2173
            MAG: amb3676 amb4107
            MGM: Mmc1_2676
            ABA: Acid345_2102
            SUS: Acid_1288
            BSU: BG13970(yuiE)
            BHA: BH3401
            BAN: BA5155(pepA)
            BAR: GBAA5155(pepA)
            BAA: BA_0028
            BAT: BAS4792
            BCE: BC4921(pepA)
            BCA: BCE_5060(pepA)
            BCZ: BCZK4653(pepA)
            BCY: Bcer98_3532
            BTK: BT9727_4633(pepA)
            BTL: BALH_4461(pepA)
            BLI: BL05323(pepA)
            BLD: BLi03387(yuiE)
            BCL: ABC2920(pepA)
            BPU: BPUM_2866
            GKA: GK2140 GK2947(pepA)
            SAU: SA0803(ampA)
            SAV: SAV0942(ampA)
            SAM: MW0824(ampA)
            SAR: SAR0904(pepA)
            SAS: SAS0812
            SAC: SACOL0945
            SAB: SAB0808
            SAA: SAUSA300_0845(ampA)
            SAO: SAOUHSC_00879
            SAJ: SaurJH9_0942
            SAH: SaurJH1_0961
            SEP: SE0636
            SER: SERP0528
            SHA: SH2009(ampA)
            SSP: SSP1833
            STH: STH1774
            CPE: CPE2501
            CPF: CPF_2824
            CPR: CPR_2510(pepA)
            CTC: CTC01012 CTC01866
            CDF: CD1300(pepA)
            CBE: Cbei_2737
            AMT: Amet_4616
            MGE: MG_391
            MPN: MPN572(D02_orf445)
            MPU: MYPU_3750(pepA) MYPU_7260(pepA)
            MPE: MYPE8950
            MGA: MGA_0114(pepB)
            MMY: MSC_0163(pepA) MSC_0235(pepA)
            MMO: MMOB1740(pepA) MMOB4630(pepA)
            MHY: mhp462(pepA)
            MHJ: MHJ_0461(pepA)
            MHP: MHP7448_0464(pepA)
            MSY: MS53_0153(pepA-1) MS53_0154(pepA)
            MCP: MCAP_0157(pepA1) MCAP_0195(pepA2)
            UUR: UU507(ampL)
            MFL: Mfl070
            MTU: Rv2213(pepB)
            MTC: MT2269(pepA)
            MBO: Mb2236(pepB)
            MBB: BCG_2229(pepB)
            MLE: ML0864(pepA)
            MPA: MAP1953(pepB)
            MAV: MAV_2279
            MSM: MSMEG_4281
            MVA: Mvan_3575
            MGI: Mflv_2938
            MMC: Mmcs_3310
            MKM: Mkms_3372
            MJL: Mjls_3321
            CGL: NCgl2124(cgl2205)
            CGB: cg2419(pepB)
            CEF: CE2096
            CDI: DIP1637
            CJK: jk0709(pepB) jk1387(pepA)
            NFA: nfa16920
            RHA: RHA1_ro01149
            SCO: SCO2179(SC5F7.22)
            SMA: SAV6025
            TWH: TWT501(pepB)
            TWS: TW261
            LXX: Lxx10160(pep)
            CMI: CMM_1643(pepA)
            ART: Arth_1613
            PAC: PPA0694
            NCA: Noca_1207 Noca_2306
            TFU: Tfu_0503 Tfu_0995
            FRA: Francci3_3133 Francci3_3836
            FAL: FRAAL5149(pepA) FRAAL6095(pepA)
            ACE: Acel_0937 Acel_1834
            KRA: Krad_1149 Krad_3276
            SEN: SACE_1030(pepA) SACE_1642(pepB)
            STP: Strop_3317
            RXY: Rxyl_1124
            FNU: FN1906
            RBA: RB12107(pepA)
            CTR: CT045(pepA)
            CTA: CTA_0049(pepA)
            CMU: TC0315
            CPN: CPn0385(pepA)
            CPA: CP0370
            CPJ: CPj0385(pepA)
            CPT: CpB0397
            CCA: CCA00411(pepA)
            CAB: CAB397
            CFE: CF0597(pepA)
            PCU: pc1103(pepA)
            TDE: TDE0300
            LIL: LA3441(pepA)
            LIC: LIC10733(pepA)
            LBJ: LBJ_0821(pepB)
            LBL: LBL_2260(pepB)
            SYN: sll2001(lap)
            SYW: SYNW0562
            SYC: syc0360_d
            SYF: Synpcc7942_1190
            SYD: Syncc9605_2108
            SYE: Syncc9902_0561
            SYG: sync_2208
            SYR: SynRCC307_1809(pepA)
            SYX: SynWH7803_1951(pepA)
            TEL: tlr1745
            GVI: glr2611
            ANA: alr0237
            AVA: Ava_2727
            PMA: Pro1413(pepB)
            PMM: PMM1332
            PMT: PMT1407
            PMN: PMN2A_0903
            PMI: PMT9312_1430
            PMB: A9601_15321(pepB)
            PMC: P9515_14931(pepB)
            PMF: P9303_05571(pepB)
            PMG: P9301_15181(pepB)
            PMH: P9215_15611
            PME: NATL1_17591(pepB)
            TER: Tery_0069
            CTE: CT1180(pepA)
            CCH: Cag_0823
            CPH: Cpha266_1537
            PVI: Cvib_0947
            PLT: Plut_0954
            DET: DET1030
            DEH: cbdb_A1001(pepA)
            DEB: DehaBAV1_0913
            RRS: RoseRS_0699
            RCA: Rcas_0295
            DRA: DR_0717
            TTH: TTC1729
            TTJ: TTHA0256
            AAE: aq_2099(pepA)
            HWA: HQ1074A(pepB) HQ3641A(pepB)
            APE: APE_2450.1
            SMR: Smar_0166
            IHO: Igni_0738
            NEQ: NEQ412
STRUCTURES  PDB: 1BLL  1BPM  1BPN  1GYT  1LAM  1LAN  1LAP  1LCP  2EWB  2HB6  
                 2HC9  2J9A  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.1
            ExPASy - ENZYME nomenclature database: 3.4.11.1
            ExplorEnz - The Enzyme Database: 3.4.11.1
            ERGO genome analysis and discovery system: 3.4.11.1
            BRENDA, the Enzyme Database: 3.4.11.1
            CAS: 9001-61-0
///
ENTRY       EC 3.4.11.2                 Enzyme
NAME        membrane alanyl aminopeptidase;
            microsomal aminopeptidase;
            aminopeptidase M;
            aminopeptidase N;
            particle-bound aminopeptidase;
            amino-oligopeptidase;
            alanine aminopeptidase;
            membrane aminopeptidase I;
            pseudo leucine aminopeptidase;
            alanyl aminopeptidase;
            alanine-specific aminopeptidase;
            cysteinylglycine dipeptidase;
            cysteinylglycinase;
            L-alanine aminopeptidase;
            CD13
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of an N-terminal amino acid, Xaa!Yaa- from a peptide, amide
            or arylamide. Xaa is preferably Ala, but may be most amino acids
            including Pro (slow action). When a terminal hydrophobic residue is
            followed by a prolyl residue, the two may be released as an intact
            Xaa-Pro dipeptide
ALL_REAC    (other) R00899 R04951
COFACTOR    Manganese [CPD:C00034];
            Zinc [CPD:C00038]
COMMENT     A zinc enzyme, not activated by heavy metal ions. Type example of
            peptidase family M1.
REFERENCE   1  [PMID:5938934]
  AUTHORS   Wachsmuth ED, Fritze I, Pfleiderer G.
  TITLE     An aminopeptidase occurring in pig kidney. I. An improved method of
            preparation. Physical and enzymic properties.
  JOURNAL   Biochemistry. 5 (1966) 169-74.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:931983]
  AUTHORS   Kim YS, Brophy EJ.
  TITLE     Rat intestinal brush border membrane peptidases. I. Solubilization,
            purification, and physicochemical properties of two different forms
            of the enzyme.
  JOURNAL   J. Biol. Chem. 251 (1976) 3199-205.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:873921]
  AUTHORS   Gray GM, Santiago NA.
  TITLE     Intestinal surface amino-oligopeptidases. I. Isolation of two weight
            isomers and their subunits from rat brush border.
  JOURNAL   J. Biol. Chem. 252 (1977) 4922-8.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:357150]
  AUTHORS   Sjostrom H, Noren O, Jeppesen L, Staun M, Svensson B, Christiansen
            L.
  TITLE     Purification of different amphiphilic forms of a microvillus
            aminopeptidase from pig small intestine using immunoadsorbent
            chromatography.
  JOURNAL   Eur. J. Biochem. 88 (1978) 503-11.
  ORGANISM  pig [GN:ssc]
REFERENCE   5  [PMID:6105876]
  AUTHORS   Feracci H, Maroux S.
  TITLE     Rabbit intestinal aminopeptidase N. Purification and molecular
            properties.
  JOURNAL   Biochim. Biophys. Acta. 599 (1980) 448-63.
  ORGANISM  rabbit
PATHWAY     PATH: map00480  Glutathione metabolism
            PATH: map04614  Renin-angiotensin system
            PATH: map04640  Hematopoietic cell lineage
ORTHOLOGY   KO: K01256  membrane alanyl aminopeptidase
GENES       HSA: 290(ANPEP)
            PTR: 467758(ANPEP)
            MMU: 16790(Anpep)
            RNO: 81641(Anpep)
            CFA: 403913(ANPEP)
            BTA: 404191(ANPEP)
            SSC: 397520(ANPEP)
            GGA: 395667(ANPEP)
            XLA: 495476(LOC495476)
            DRE: 100006595(LOC100006595)
            SPU: 578352(APN)
            DME: Dmel_CG11956(SP1029) Dmel_CG14516 Dmel_CG5518(sda)
                 Dmel_CG7653
            CEL: T07F10.1
            OSA: 4346337
            CME: CMF182C
            PIC: PICST_31787(APE2.1)
            CPV: cgd8_3430
            CHO: Chro.80395
            TAN: TA20910
            TPV: TP01_0397
            TET: TTHERM_00569330 TTHERM_00786960 TTHERM_00786970
            ECO: b0932(pepN)
            ECJ: JW0915(pepN)
            ECE: Z1280(pepN)
            ECS: ECs1015
            ECC: c1075(pepN)
            ECI: UTI89_C1004(pepN)
            ECP: ECP_0944
            ECV: APECO1_44(pepN)
            ECW: EcE24377A_1033(pepN)
            ECX: EcHS_A1041
            STY: STY1078(pepN)
            STT: t1863(pepN)
            SPT: SPA1793(pepN)
            SEC: SC1010(pepN)
            STM: STM1057(pepN)
            YPE: YPO1414(pepN)
            YPK: y2756(pepN)
            YPM: YP_1179(pepN)
            YPA: YPA_0709
            YPN: YPN_2563
            YPP: YPDSF_2281
            YPS: YPTB1438(pepN)
            YPI: YpsIP31758_2556(pepN)
            YEN: YE1567(pepN)
            SFL: SF0929(pepN)
            SFX: S0993(pepN)
            SFV: SFV_0934(pepN)
            SSN: SSON_0935(pepN)
            SBO: SBO_2223(pepN)
            SDY: SDY_2325(pepN)
            ECA: ECA2539(pepN)
            PLU: plu1755(pepN)
            SGL: SG1017
            ENT: Ent638_1451
            KPN: KPN_00968(pepN)
            HIN: HI1614(pepN)
            HIT: NTHI1428(pepN)
            HDU: HD0976(pepN)
            HSO: HS_0884(pepN)
            PMU: PM0618(pepN)
            MSU: MS1034(pepN)
            APL: APL_1340(pepN)
            XCC: XCC1054(pepN)
            XCB: XC_3192
            XCV: XCV1179(pepN2)
            XAC: XAC1159(pepN)
            XOO: XOO0916(pepN)
            XOM: XOO_0841(XOO0841)
            VCH: VC1494
            VCO: VC0395_A1102(pepN)
            VVU: VV1_2641
            VVY: VV1650
            VPA: VP1604
            VFI: VF1282
            PPR: PBPRA1764
            PAE: PA3083(pepN)
            PAU: PA14_24270(pepN)
            PAP: PSPA7_2055(pepN)
            PPU: PP_2017(pepN)
            PST: PSPTO_3788(pepN)
            PSB: Psyr_1690
            PSP: PSPPH_3595(pepN)
            PFL: PFL_3281(pepN)
            PFO: Pfl_2200
            PEN: PSEEN1713(pepN)
            PMY: Pmen_2939
            PAR: Psyc_0909(pepN)
            PCR: Pcryo_1508
            ACI: ACIAD2008(pepN)
            SON: SO_1059 SO_2600(pepN)
            SDN: Sden_1723 Sden_2915
            SFR: Sfri_2227 Sfri_3244
            SBL: Sbal_2446
            SLO: Shew_1803
            SPC: Sputcn32_2201
            SHE: Shewmr4_1674 Shewmr4_3040
            SHM: Shewmr7_0932 Shewmr7_1749
            SHN: Shewana3_0897 Shewana3_1779
            SHW: Sputw3181_1808
            ILO: IL1277(pepN_1)
            CPS: CPS_2808(pepN)
            PHA: PSHAa1676(pepN)
            PAT: Patl_1996
            SDE: Sde_0760 Sde_1737
            PIN: Ping_2344
            MAQ: Maqu_2067
            CBU: CBU_0338(pepN)
            CBD: COXBU7E912_1741(pepN)
            LPN: lpg1497(pepN) lpg2809(pepN)
            LPF: lpl1529 lpl2724(pepN)
            LPP: lpp1454 lpp2855(pepN)
            MCA: MCA0774(pepN)
            FTU: FTT1793c(pepN)
            FTF: FTF1793c(pepN)
            FTL: FTL_1956
            FTH: FTH_1873(pepN)
            FTA: FTA_2070(pepN)
            FTN: FTN_1768(pepN)
            TCX: Tcr_1485
            NOC: Noc_1314
            AEH: Mlg_1592
            HHA: Hhal_0120
            HCH: HCH_04587(pepN)
            CSA: Csal_2521
            ABO: ABO_0998(pepN)
            AHA: AHA_2290(pepN)
            DNO: DNO_0019
            NME: NMB1416
            NMA: NMA1627(pepN)
            NMC: NMC1347(pepN)
            NGO: NGO0158
            CVI: CV_1176(pepN)
            RSO: RSc2125(pepN)
            REU: Reut_A2443
            REH: H16_A1000(pepN)
            RME: Rmet_0876
            BMA: BMA0466(pepN) BMA2818
            BMV: BMASAVP1_A2614(pepN)
            BML: BMA10299_A0986(pepN)
            BMN: BMA10247_0161(pepN)
            BXE: Bxe_A0923
            BUR: Bcep18194_A3582 Bcep18194_A4126
            BCN: Bcen_0536 Bcen_2613
            BCH: Bcen2424_0492 Bcen2424_1015
            BAM: Bamb_0397 Bamb_0878
            BPS: BPSL2544 BPSL3089
            BPM: BURPS1710b_3028(pepN) BURPS1710b_3622(pepN)
            BPL: BURPS1106A_2983(pepN)
            BPD: BURPS668_2922(pepN)
            BTE: BTH_I1608 BTH_I2945
            BPE: BP0869(pepN)
            BPA: BPP2483(pepN)
            BBR: BB1930(pepN)
            RFR: Rfer_2703
            POL: Bpro_1587
            MPT: Mpe_A2774
            HAR: HEAR0571(pepN)
            MMS: mma_0553
            NEU: NE0626(pepN)
            NET: Neut_0418
            EBA: ebA7122(pepN)
            AZO: azo3147(pepN)
            DAR: Daro_3676
            TBD: Tbd_0899
            MFA: Mfla_1238
            TDN: Tmden_0620
            CCO: CCC13826_1263
            GSU: GSU0304(pepN)
            PCA: Pcar_1649
            BBA: Bd2521(pepN)
            DPS: DP2164
            SFU: Sfum_0739
            MLO: mll7701
            MES: Meso_0906
            SME: SMc02370(pepN)
            ATU: Atu0984(pepN)
            ATC: AGR_C_1803
            RET: RHE_CH01298(pepN)
            RLE: RL1446(pepN)
            BME: BMEI1324
            BMF: BAB1_0641(pepN)
            BMS: BR0617(pepN)
            BMB: BruAb1_0636(pepN)
            BOV: BOV_0616(pepN)
            BHE: BH04840(pepN)
            BQU: BQ04040(pepN)
            BBK: BARBAKC583_0439(pepN)
            CCR: CC_2481
            SIL: SPO2841(pepN)
            SIT: TM1040_0706
            RSP: RSP_1982
            JAN: Jann_1872
            RDE: RD1_3327(pepN) RD1_4194(pepN)
            HNE: HNE_2911(pepN)
            ZMO: ZMO1345(pepN) ZMO1776(pepN)
            NAR: Saro_0443 Saro_3270
            SAL: Sala_0475
            ELI: ELI_13625
            GOX: GOX2144
            GBE: GbCGDNIH1_0675
            MGM: Mmc1_1919
            LLA: L102360(pepN)
            LLC: LACR_0341
            LLM: llmg_0319(pepN)
            SPY: SPy_1239(pepN)
            SPZ: M5005_Spy_0949(pepN)
            SPM: spyM18_1188(pepN)
            SPG: SpyM3_0875(pepN)
            SPS: SPs1075
            SPH: MGAS10270_Spy1063(pepN)
            SPI: MGAS10750_Spy1098(pepN)
            SPJ: MGAS2096_Spy1008(pepN)
            SPK: MGAS9429_Spy1052(pepN)
            SPF: SpyM50849(lap)
            SPA: M6_Spy0938
            SPB: M28_Spy0921(pepN)
            SPN: SP_0797
            SPR: spr0706(pepN)
            SPD: SPD_0700(pepN)
            SAG: SAG0986(pepN)
            SAN: gbs1021
            SAK: SAK_1081(pepN)
            SMU: SMU.1132(pepN)
            STC: str1007(pepN)
            STL: stu1007(pepN)
            SSA: SSA_0955(pepN) SSA_0994
            SGO: SGO_1069
            LPL: lp_0937(pepN)
            LJO: LJ1584
            LAC: LBA1849(pepN)
            LSA: LSA0226(pepN)
            LSL: LSL_1745(pepN)
            LDB: Ldb2080(pepN)
            LBU: LBUL_1922
            LBR: LVIS_1756
            LCA: LSEI_0470
            LGA: LGAS_0715
            LRE: Lreu_1883
            PPE: PEPE_0417
            OOE: OEOE_1058
            LME: LEUM_0504
            MTU: Rv2467(pepN)
            MTC: MT2542(pepN)
            MBO: Mb2494(pepN)
            MBB: BCG_2487(pepN)
            MLE: ML1486
            MPA: MAP2287(pepD)
            MAV: MAV_1704(pepN)
            MSM: MSMEG_4690(pepN)
            MMC: Mmcs_3605
            CGL: NCgl2340(cgl2426)
            CGB: cg2662(pepN)
            CEF: CE2320
            CDI: DIP1798
            CJK: jk0539(pepN)
            NFA: nfa13180
            RHA: RHA1_ro01382 RHA1_ro01938
            SCO: SCO2018(SC7H2.32c) SCO2635(SC8E4A.05) SCO2643(pepN)
            SMA: SAV5395(pepN1) SAV5411(pepN2) SAV6212
            TWH: TWT399(pepD)
            TWS: TW371(pepN)
            LXX: Lxx08760(pepN)
            AAU: AAur_2130(pepN) AAur_2388(pepN)
            PAC: PPA1627 PPA1979
            TFU: Tfu_2204
            FRA: Francci3_0968 Francci3_1160
            FAL: FRAAL1858
            SEN: SACE_1339
            BLO: BL1191(pepN)
            BAD: BAD_1295(pepN)
            LIL: LA1080(pepN)
            LIC: LIC12591(pepN)
            LBJ: LBJ_2310(pepN)
            LBL: LBL_0797(pepN)
            SYW: SYNW0756(pepN)
            SYD: Syncc9605_1912
            SYE: Syncc9902_0754
            SYG: sync_1009(pepN)
            SYR: SynRCC307_0767(pepN)
            SYX: SynWH7803_1555(pepN)
            AVA: Ava_0316
            PMM: PMM1002(pepN)
            PMT: PMT1052(pepN)
            PMN: PMN2A_0671
            PMI: PMT9312_1011
            PMB: A9601_10901(pepN)
            PMC: P9515_10861(pepN)
            PMF: P9303_10001(pepN)
            PMG: P9301_10751 P9301_10901(pepN)
            PMH: P9215_11191
            PME: NATL1_15041(pepN)
            TER: Tery_0295
            BFR: BF0674
            BFS: BF0600
            CHU: CHU_0163(pepN) CHU_0576(pepN) CHU_1442(pepN)
            MAC: MA1605(pepN)
            MBA: Mbar_A2053
            MMA: MM_0279
            MBU: Mbur_0032
STRUCTURES  PDB: 2DQ6  2DQM  2GTQ  2HPO  2HPT  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.2
            ExPASy - ENZYME nomenclature database: 3.4.11.2
            ExplorEnz - The Enzyme Database: 3.4.11.2
            ERGO genome analysis and discovery system: 3.4.11.2
            BRENDA, the Enzyme Database: 3.4.11.2
            CAS: 9054-63-1
///
ENTRY       EC 3.4.11.3                 Enzyme
NAME        cystinyl aminopeptidase;
            cystyl-aminopeptidase;
            oxytocinase;
            cystine aminopeptidase;
            L-cystine aminopeptidase;
            oxytocin peptidase;
            vasopresssinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of an N-terminal amino acid, Cys!Xaa-, in which the
            half-cystine residue is involved in a disulfide loop, notably in
            oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl
            arylamides exceed that for the cystinyl derivative, however [4]
COFACTOR    Zinc [CPD:C00038]
COMMENT     A zinc-containing sialoglycoprotein in peptidase family M1 (membrane
            alanyl aminopeptidase family)
REFERENCE   1  [PMID:6041057]
  AUTHORS   Sjoholm I.
  TITLE     Biochemical studies on oxytocin and oxytocinase.
  JOURNAL   Acta. Pharm. Suec. 4 (1967) 81-96.
  ORGANISM  human [GN:hsa], ,
REFERENCE   2  [PMID:4292447]
  AUTHORS   Sjoholm I, Yman L.
  TITLE     Degradation of oxytocin, lysine-vasopressin, angiotensin II and
            angiotensin-II-amide by oxytocinase (cystine aminopeptidase).
  JOURNAL   Acta. Pharm. Suec. 4 (1967) 65-76.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:5421622]
  AUTHORS   Yman L.
  TITLE     Studies on human serum aminopeptidases. Some properties of
            oxytocinase, human serum aminopeptidase A and leucine aminopeptidase
            and their purification from retroplacental serum.
  JOURNAL   Acta. Pharm. Suec. 7 (1970) 75-86.
  ORGANISM  human [GN:hsa]
REFERENCE   4
  AUTHORS   Sakura, H., Lin, T.Y., Doi, M., Mizutani, S. and Kawashima, Y.
  TITLE     Purification and properties of oxytocinase, a metalloenzyme.
  JOURNAL   Biochem. Int. 2 (1981) 173-179.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04614  Renin-angiotensin system
ORTHOLOGY   KO: K01257  cystinyl aminopeptidase
GENES       HSA: 4012(LNPEP)
            PTR: 461960(LNPEP)
            MMU: 240028(Lnpep)
            RNO: 171105(Lnpep)
            CFA: 488896(LNPEP)
            BTA: 521633(LOC521633)
            GGA: 427279(LNPEP)
            XLA: 495293(LOC495293)
            DRE: 322814(zgc:66103)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.3
            ExPASy - ENZYME nomenclature database: 3.4.11.3
            ExplorEnz - The Enzyme Database: 3.4.11.3
            ERGO genome analysis and discovery system: 3.4.11.3
            BRENDA, the Enzyme Database: 3.4.11.3
            CAS: 9031-41-8
///
ENTRY       EC 3.4.11.4                 Enzyme
NAME        tripeptide aminopeptidase;
            tripeptidase;
            aminotripeptidase;
            aminoexotripeptidase;
            lymphopeptidase;
            imidoendopeptidase;
            peptidase B;
            alanine-phenylalanine-proline arylamidase;
            peptidase T
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of the N-terminal residue from a tripeptide
ALL_REAC    (other) R00494
COFACTOR    Zinc [CPD:C00038]
COMMENT     A zinc enzyme, widely distributed in mammalian tissues.
REFERENCE   1  [PMID:109082]
  AUTHORS   Doumeng C, Maroux S.
  TITLE     Aminotripeptidase, a cytosol enzyme from rabbit intestinal mucosa.
  JOURNAL   Biochem. J. 177 (1979) 801-8.
  ORGANISM  rabbit
REFERENCE   2  [PMID:7126601]
  AUTHORS   Sachs L, Marks N.
  TITLE     A highly specific aminotripeptidase of rat brain cytosol. Substrate
            specificity and effects of inhibitors.
  JOURNAL   Biochim. Biophys. Acta. 706 (1982) 229-38.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00480  Glutathione metabolism
ORTHOLOGY   KO: K01258  tripeptide aminopeptidase
GENES       ECO: b1127(pepT)
            ECJ: JW1113(pepT)
            ECE: Z1832(pepT)
            ECS: ECs1572
            ECC: c1479(pepT)
            ECI: UTI89_C1256(pepT)
            ECP: ECP_1122
            ECV: APECO1_209(pepT)
            ECW: EcE24377A_1290(pepT)
            ECX: EcHS_A1247
            STY: STY1267(pepT)
            STT: t1693(pepT)
            SPT: SPA1623(pepT)
            SEC: SC1178(pepT)
            STM: STM1227(pepT)
            YPE: YPO1631(pepT)
            YPK: y1791(pepT)
            YPM: YP_1761(pepT)
            YPA: YPA_1893 YPA_3367
            YPN: YPN_2000 YPN_3223
            YPP: YPDSF_1817
            YPS: YPTB2437(pepT)
            SFL: SF1129(pepT)
            SFX: S1209(pepT)
            SFV: SFV_1145(pepT)
            SSN: SSON_1145(pepT)
            SBO: SBO_1912(pepT)
            SDY: SDY_2025(pepT)
            ECA: ECA2448(pepT)
            PLU: plu2810(pepT)
            ENT: Ent638_1640 Ent638_1976
            SPE: Spro_2009 Spro_3359
            HIN: HI1348(pepT)
            HIT: NTHI1818(pepT)
            HIP: CGSHiEE_04270
            HIQ: CGSHiGG_00390
            PMU: PM0265(pepT)
            MSU: MS0815(pepD)
            ASU: Asuc_1747
            VCH: VCA0180
            VVU: VV2_0532
            VVY: VVA1081
            VPA: VPA1193
            VFI: VF1060 VFA0004 VFA0253
            PPR: PBPRA1848
            SLO: Shew_3250
            SSE: Ssed_4006
            SPL: Spea_2943
            AHA: AHA_1612(pepT)
            CCV: CCV52592_2106
            CCO: CCC13826_0644
            BBA: Bd2900(pepT)
            SMD: Smed_5042 Smed_5411
            RET: RHE_PE00254(pepT)
            RLE: pRL110369(pepT)
            OAN: Oant_4406
            BJA: blr4926(pepT)
            BRA: BRADO4189(pepT)
            BBT: BBta_4565(pepT)
            RPA: RPA2954(pepT)
            RPB: RPB_2569
            RPC: RPC_2396
            RPD: RPD_2890
            RPE: RPE_2516
            NWI: Nwi_1893
            NHA: Nham_2224
            SIL: SPO3830(pepT)
            SIT: TM1040_0648
            BSU: BG11842(pepT)
            BAN: BA3872(pepT-1)
            BAR: GBAA3872(pepT-1)
            BAA: BA_4347
            BAT: BAS3588
            BCE: BC3743
            BCA: BCE_3775(pepT)
            BCZ: BCZK3500(pepT)
            BCY: Bcer98_2411
            BTK: BT9727_3488(pepT)
            BLI: BL01918(pepT)
            BLD: BLi04177(pepT)
            BCL: ABC0714(pepT)
            BAY: RBAM_022210(yqjE)
            OIH: OB0531
            GKA: GK1762(pepT)
            SAU: SA0698(pepT)
            SAV: SAV0743(pepT)
            SAM: MW0705(pepT)
            SAR: SAR0797(pepT)
            SAS: SAS0708
            SAC: SACOL0806(pepT)
            SAB: SAB0695c(pepT)
            SAA: SAUSA300_0727(pepT)
            SAO: SAOUHSC_00757
            SAJ: SaurJH9_0767
            SAH: SaurJH1_0784
            SEP: SE0525
            SER: SERP0410(pepT)
            SHA: SH2148(pepT)
            SSP: SSP1973
            LMO: lmo1780
            LMF: LMOf2365_1805(pepT)
            LIN: lin1892
            LWE: lwe1798(pepT)
            LLA: L60596(pepT)
            SPY: SPy_0799(pepT)
            SPZ: M5005_Spy_0614(pepT)
            SPM: spyM18_0861(pepT)
            SPG: SpyM3_0533(pepT)
            SPS: SPs1321
            SPH: MGAS10270_Spy0669(pepT)
            SPI: MGAS10750_Spy0701(pepT)
            SPJ: MGAS2096_Spy0679(pepT)
            SPK: MGAS9429_Spy0669(pepT)
            SPA: M6_Spy0631
            SPB: M28_Spy0593(pepT)
            SPN: SP_1008
            SPR: spr0913(pepT)
            SPD: SPD_0894(pepT)
            SAG: SAG1389(pepT)
            SAN: gbs1459
            SAK: SAK_1422(pepT)
            SMU: SMU.691(pepT)
            STC: str1139(pepT)
            STL: stu1139(pepT)
            SSA: SSA_1326(pepT)
            LPL: lp_1904(pepT)
            LJO: LJ1303
            LAC: LBA1190(pepT) LBA1515(pepT)
            LSA: LSA0888(pepT)
            LSL: LSL_0848(pepD)
            LDB: Ldb0371(pepT2) Ldb1217(pepT1)
            LBU: LBUL_0326 LBUL_1126
            LBR: LVIS_0761
            LRE: Lreu_0748
            EFA: EF1382(pepT-1)
            OOE: OEOE_0998
            STH: STH1610
            CAC: CAC0476(pepT)
            CPE: CPE0025(pepT)
            CPF: CPF_0029(pepT)
            CPR: CPR_0029(pepT)
            CBA: CLB_0480(pepT)
            CBH: CLC_0513(pepT)
            CBF: CLI_0524(pepT)
            CBE: Cbei_2428
            DSY: DSY2060
            TTE: TTE1808(pepD)
            FNU: FN0733
            RBA: RB7375(pepT)
            TDE: TDE0925(pepT)
            BTH: BT_4583
            BFR: BF1302
            BFS: BF1289(pepT)
            PGI: PG0445(pepT)
            GFO: GFO_2523(pepT)
            FJO: Fjoh_2205
            FPS: FP1919(pepT)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.4
            ExPASy - ENZYME nomenclature database: 3.4.11.4
            ExplorEnz - The Enzyme Database: 3.4.11.4
            ERGO genome analysis and discovery system: 3.4.11.4
            BRENDA, the Enzyme Database: 3.4.11.4
            CAS: 9056-26-2
///
ENTRY       EC 3.4.11.5                 Enzyme
NAME        prolyl aminopeptidase;
            proline aminopeptidase;
            Pro-X aminopeptidase;
            cytosol aminopeptidase V;
            proline iminopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of N-terminal proline from a peptide
ALL_REAC    (other) R00135
COFACTOR    Manganese [CPD:C00034]
COMMENT     A Mn2+-requiring enzyme present in the cytosol of mammalian and
            microbial cells. In contrast to the mammalian form, the bacterial
            form of the enzyme (type example of peptidase family S33) hydrolyses
            both polyproline and prolyl-2-naphthylamide. The mammalian enzyme,
            which is not specific for prolyl bonds, is possibly identical with
            EC 3.4.11.1, leucyl aminopeptidase."
REFERENCE   1
  AUTHORS   Sarid, S., Berger, A. and Katchalski, E.
  TITLE     Proline iminopeptidase. II. Purification and comparison with
            iminopeptidase (prolinase).
  JOURNAL   J. Biol. Chem. 237 (1962) 2207-2212.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4803482]
  AUTHORS   Nordwig A, Mayer H.
  TITLE     The cleavage of prolyl peptides by kidney peptidases. Detection of a
            new peptidase capable of removing N-terminal proline.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 354 (1973) 380-3.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:2373079]
  AUTHORS   Turzynski A, Mentlein R.
  TITLE     Prolyl aminopeptidase from rat brain and kidney. Action on peptides
            and identification as leucyl aminopeptidase.
  JOURNAL   Eur. J. Biochem. 190 (1990) 509-15.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K01259  proline iminopeptidase
GENES       HSA: 51056(LAP3)
            PTR: 461132(LAP3)
            MMU: 66988(Lap3)
            RNO: 289668(Lap3)
            CFA: 479081(LAP3)
            GGA: 425306(RCJMB04_15i13)
            XLA: 414652(MGC81140)
            XTR: 496537(lap3)
            ATH: AT2G24200 AT4G30910 AT4G30920
            OSA: 4339305 4352123
            CME: CMA107C CMS385C
            PIC: PICST_48996(PAP2)
            AFM: AFUA_2G05000
            ANG: An11g04730(papA)
            DDI: DDBDRAFT_0187236
            TET: TTHERM_00049020 TTHERM_00433870 TTHERM_00760600
            YPE: YPO1781(pip)
            YPK: y2526
            YPM: YP_1612(pip)
            YPA: YPA_1156
            YPN: YPN_2342
            YPP: YPDSF_1342
            YPS: YPTB1657(pip)
            YPI: YpsIP31758_2344(pip)
            PLU: plu2691(pip)
            SPE: Spro_1940
            ASU: Asuc_0740
            XFA: XF1510
            XFT: PD0727(pip)
            XCC: XCC0836(pip) XCC2817
            XCB: XC_1296 XC_3394
            XCV: XCV0945(pip) XCV3134(pip)
            XAC: XAC0909(pip) XAC2987
            XOO: XOO1269 XOO3642(pip)
            XOM: XOO_1168(XOO1168) XOO_3441(XOO3441)
            VFI: VFA0792
            PAE: PA5080
            PAU: PA14_67110(pap)
            PAP: PSPA7_5819(pip)
            PPU: PP_5028(pip)
            PPF: Pput_4902
            PST: PSPTO_5164(pip)
            PSB: Psyr_0375
            PSP: PSPPH_0357(pip) PSPPH_4239
            PFL: PFL_0411(pip)
            PFO: Pfl_0371
            PEN: PSEEN5092(pip)
            SON: SO_4400
            SPL: Spea_3908
            SHE: Shewmr4_0317
            SHM: Shewmr7_3707
            SHN: Shewana3_0312
            CPS: CPS_0863(pip1) CPS_3964(pip2)
            PAT: Patl_3951
            SDE: Sde_0552
            PIN: Ping_0253
            MAQ: Maqu_0771
            LPN: lpg1843(pip)
            LPF: lpl1808
            LPP: lpp1807
            MCA: MCA1737(pip)
            FTN: FTN_1731(pip)
            TCX: Tcr_0168
            NOC: Noc_0712
            HCH: HCH_01038(pip)
            ABO: ABO_2257(pip)
            AHA: AHA_2386 AHA_3475
            NME: NMB0927
            NMA: NMA1122(pip)
            NMC: NMC0905(pip)
            NGO: NGO0949
            RSO: RS04709(RSp0196)
            REU: Reut_B3492
            REH: H16_B1053(pap) H16_B2515(pip)
            RME: Rmet_4027
            BMA: BMAA1876(pip)
            BMV: BMASAVP1_0886(pip)
            BML: BMA10299_1173(pip)
            BMN: BMA10247_A2151(pip)
            BXE: Bxe_B2466
            BVI: Bcep1808_4676 Bcep1808_6559
            BUR: Bcep18194_A4280 Bcep18194_B1183 Bcep18194_B1463
                 Bcep18194_B1929 Bcep18194_B2393 Bcep18194_B2445
                 Bcep18194_B2956
            BCN: Bcen_3244 Bcen_4251
            BCH: Bcen2424_4115 Bcen2424_5124
            BAM: Bamb_3526 Bamb_6163
            BPS: BPSS0201(pip)
            BPM: BURPS1710b_A1728
            BPL: BURPS1106A_A0279(pip)
            BPD: BURPS668_A0373(pip)
            BTE: BTH_II2193
            BPE: BP3691
            BPA: BPP0504
            BBR: BB0509
            RFR: Rfer_0089
            POL: Bpro_1603
            PNA: Pnap_1088
            MPT: Mpe_A2584
            HAR: HEAR1383 HEAR3357
            MMS: mma_3579
            NEU: NE2295
            NET: Neut_2133
            AZO: azo1185(pip)
            DAR: Daro_1031 Daro_1698
            TBD: Tbd_0887
            MFA: Mfla_2315
            BBA: Bd3480(pip)
            MXA: MXAN_6006(pip)
            MLO: mlr7803
            PLA: Plav_0503
            SME: SMc02547(pip1)
            SMD: Smed_0717
            ATU: Atu1069(pip)
            ATC: AGR_C_1974
            RET: RHE_CH01420(pipch1) RHE_CH02208(pipch2) RHE_PB00088(pipb1)
                 RHE_PB00090(pipb2)
            RLE: RL1539(pip) RL2538(pip) pRL100270 pRL90179(pepI)
                 pRL90181(pip)
            BME: BMEI1608
            BMF: BAB1_0344(pip)
            BMS: BR0314(pip)
            BMB: BruAb1_0340(pip)
            BOV: BOV_0330(pip)
            OAN: Oant_3085
            BJA: bll4403(pip) blr6740(pip)
            BRA: BRADO4325 BRADO5798(pip) BRADO6453
            BBT: BBta_1192 BBta_5020 BBta_5500 BBta_6305(pip)
            RPA: RPA3630
            RPB: RPB_1894
            RPC: RPC_3668
            RPD: RPD_3473
            RPE: RPE_3706
            CCR: CC_1227
            SIL: SPO0066(pip)
            SIT: TM1040_2907
            RSP: RSP_1174(pip)
            RSH: Rsph17029_2836
            RSQ: Rsph17025_2767
            JAN: Jann_0299
            RDE: RD1_0391(pip)
            PDE: Pden_2590
            MMR: Mmar10_1122 Mmar10_2011
            HNE: HNE_2930(pip)
            SAL: Sala_2006
            SWI: Swit_0937 Swit_4410
            ELI: ELI_06495
            GBE: GbCGDNIH1_0167
            ACR: Acry_1042
            RRU: Rru_A0084 Rru_A2180
            MAG: amb0597
            SUS: Acid_6970
            BAN: BA2217
            BAR: GBAA2217
            BAA: BA_2719
            BAT: BAS2061
            BCE: BC2171 BC2337 BC4663
            BCA: BCE_1173 BCE_2247 BCE_4805
            BCZ: BCZK1692 BCZK2000(pip) BCZK3858 BCZK4415
            BTK: BT9727_2001(pip) BT9727_4398
            BTL: BALH_0955(pip) BALH_1656(pip) BALH_1978(pip) BALH_4246
            BCL: ABC1243 ABC1974
            OIH: OB1045
            SAA: SAUSA300_0601 SAUSA300_0604
            LLM: llmg_1830(menX)
            SSA: SSA_0934
            LPL: lp_0088(pepI) lp_0853(pepR1) lp_2919(pepR2)
            LJO: LJ0054
            LAC: LBA0092 LBA1658 LBA1957(pepL)
            LSA: LSA0133(pepR)
            LDB: Ldb1896(pepIP) Ldb1909(pepPN)
            LBU: LBUL_1775
            LBR: LVIS_1783 LVIS_2232
            LCA: LSEI_0750 LSEI_1988
            LGA: LGAS_0052
            LRE: Lreu_1648
            PPE: PEPE_0379
            OOE: OEOE_0576
            CDF: CD3041(pepI)
            CBO: CBO2031(pepIP)
            CBA: CLB_1972(pepIP)
            CBH: CLC_1977(pepIP)
            CBF: CLI_2096(pepIP)
            MGE: MG_020(pip)
            MPN: MPN022(pip)
            MPE: MYPE8330(pip)
            MTU: Rv0840c(pip)
            MTC: MT0862(pip)
            MBO: Mb0863c(pip)
            MBB: BCG_0892c(pip)
            MSM: MSMEG_2681
            MGI: Mflv_5441
            CGB: cg0684(papA)
            NFA: nfa16480
            RHA: RHA1_ro01171 RHA1_ro03520
            SCO: SCO1989(SC7H2.03c)
            SMA: SAV875(pip)
            LXX: Lxx21800(pip)
            CMI: CMM_0804(pipA) CMM_0817(pipB)
            AAU: AAur_2073(pip)
            PAC: PPA0932 PPA2174
            TFU: Tfu_2349
            FRA: Francci3_2191
            FAL: FRAAL0535(pip)
            SEN: SACE_2704(pip)
            STP: Strop_2620 Strop_2777
            BAD: BAD_0607(pap)
            FNU: FN0752
            TDE: TDE2776(pip)
            CYA: CYA_2804(pip)
            CYB: CYB_0956(pip)
            GVI: gll1435
            ANA: alr1270
            AVA: Ava_2994 Ava_3602 Ava_4415
            PMM: PMM0356
            PMN: PMN2A_0523
            PMI: PMT9312_0360
            PMB: A9601_03911
            PMC: P9515_03961
            PMG: P9301_03901
            PME: NATL1_12631
            TER: Tery_3860
            GFO: GFO_0839(pip) GFO_0853(pip)
            FJO: Fjoh_1984
            DGE: Dgeo_0193
            TTH: TTC1457
            TTJ: TTHA1809
            TAC: Ta0830
            TVO: TVN0910
            SSO: SSO3115
            SAI: Saci_1940(pip) Saci_1942
STRUCTURES  PDB: 1AZW  1MT3  1MTZ  1MU0  1QTR  1WM1  1X2B  1X2E  1XQV  1XQW  
                 1XQX  1XQY  1XRL  1XRM  1XRN  1XRO  1XRP  1XRQ  1XRR  2J9A  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.5
            ExPASy - ENZYME nomenclature database: 3.4.11.5
            ExplorEnz - The Enzyme Database: 3.4.11.5
            ERGO genome analysis and discovery system: 3.4.11.5
            BRENDA, the Enzyme Database: 3.4.11.5
            CAS: 9025-40-5
///
ENTRY       EC 3.4.11.6                 Enzyme
NAME        aminopeptidase B;
            arylamidase II;
            arginine aminopeptidase;
            arginyl aminopeptidase;
            Cl--activated arginine aminopeptidase;
            cytosol aminopeptidase IV;
            L-arginine aminopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of N-terminal Arg and Lys from oligopeptides when P1' is not
            Pro. Also acts on arylamides of Arg and Lys
COFACTOR    Zinc [CPD:C00038];
            Cl- [CPD:C00698]
COMMENT     Cytosolic or membrane-associated enzyme from mammalian tissues,
            activated by chloride ions and low concentrations of thiol
            compounds. This is one of the activities of the bifunctional enzyme
            EC 3.3.2.6 (membrane alanyl aminopeptidase family) [4,5].
REFERENCE   1  [PMID:6434344]
  AUTHORS   Gainer H, Russell JT, Loh YP.
  TITLE     An aminopeptidase activity in bovine pituitary secretory vesicles
            that cleaves the N-terminal arginine from beta-lipotropin60-65.
  JOURNAL   FEBS. Lett. 175 (1984) 135-9.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:8344358]
  AUTHORS   Belhacene N, Mari B, Rossi B, Auberger P.
  TITLE     Characterization and purification of T lymphocyte aminopeptidase B:
            a putative marker of T cell activation.
  JOURNAL   Eur. J. Immunol. 23 (1993) 1948-55.
  ORGANISM  rabbit
REFERENCE   3  [PMID:7672445]
  AUTHORS   Cadel S, Pierotti AR, Foulon T, Creminon C, Barre N, Segretain D,
            Cohen P.
  TITLE     Aminopeptidase-B in the rat testes: isolation, functional properties
            and cellular localization in the seminiferous tubules.
  JOURNAL   Mol. Cell. Endocrinol. 110 (1995) 149-60.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:8940051]
  AUTHORS   Fukasawa KM, Fukasawa K, Kanai M, Fujii S, Harada M.
  TITLE     Molecular cloning and expression of rat liver aminopeptidase B.
  JOURNAL   J. Biol. Chem. 271 (1996) 30731-5.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:9096329]
  AUTHORS   Cadel S, Foulon T, Viron A, Balogh A, Midol-Monnet S, Noel N, Cohen
            P.
  TITLE     Aminopeptidase B from the rat testis is a bifunctional enzyme
            structurally related to leukotriene-A4 hydrolase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 2963-8.
  ORGANISM  rat [GN:rno]
REFERENCE   6  [PMID:8157657]
  AUTHORS   Orning L, Gierse JK, Fitzpatrick FA.
  TITLE     The bifunctional enzyme leukotriene-A4 hydrolase is an arginine
            aminopeptidase of high efficiency and specificity.
  JOURNAL   J. Biol. Chem. 269 (1994) 11269-73.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K01260  aminopeptidase B
GENES       HSA: 6051(RNPEP)
            PTR: 469638(RNPEP)
            MMU: 215615(Rnpep)
            RNO: 81761(Rnpep)
            CFA: 490236(RNPEP)
            GGA: 421165(RNPEP)
            XLA: 447741(MGC82089)
            XTR: 407876(rnpep)
            DRE: 437014(rnpep)
            SPU: 588993(LOC588993)
            TET: TTHERM_00637080
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.6
            ExPASy - ENZYME nomenclature database: 3.4.11.6
            ExplorEnz - The Enzyme Database: 3.4.11.6
            ERGO genome analysis and discovery system: 3.4.11.6
            BRENDA, the Enzyme Database: 3.4.11.6
            CAS: 9073-92-1
///
ENTRY       EC 3.4.11.7                 Enzyme
NAME        glutamyl aminopeptidase;
            aminopeptidase A;
            aspartate aminopeptidase;
            angiotensinase A;
            glutamyl peptidase;
            Ca2+-activated glutamate aminopeptidase;
            membrane aminopeptidase II;
            antigen BP-1/6C3 of mouse B lymphocytes;
            L-aspartate aminopeptidase;
            angiotensinase A2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of N-terminal glutamate (and to a lesser extent aspartate)
            from a peptide
COFACTOR    Zinc [CPD:C00038];
            Calcium [CPD:C00076]
COMMENT     Ca2+-activated and generally membrane-bound. A zinc-metallopeptidase
            in family M1 (membrane alanyl aminopeptidase family)
REFERENCE   1
  AUTHORS   Glenner, G.G., McMillan, P.J. and Folk, J.E.
  TITLE     A mammalian peptidase specific for the hydrolysis of N-terminal
            alpha-L-glutamyl and aspartyl residues.
  JOURNAL   Nature 194 (1962) 867.
  ORGANISM  guinea pig, human [GN:hsa], rat [GN:rno]
REFERENCE   2  [PMID:508862]
  AUTHORS   Chulkova TM, Orekhovich VN.
  TITLE     [Molecular structure of aminopeptidase A from bovine kidney]
  JOURNAL   Biokhimiia. 44 (1979) 1539-41.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:7011318]
  AUTHORS   Danielsen EM, Noren O, Sjostrom H, Ingram J, Kenny AJ.
  TITLE     Proteins of the kidney microvillar membrane. Aspartate
            aminopeptidase: purification by immunoadsorbent chromatography and
            properties of the detergent- and proteinase-solubilized forms.
  JOURNAL   Biochem. J. 189 (1980) 591-603.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:7448199]
  AUTHORS   Tobe H, Kojima F, Aoyagi T, Umezawa H.
  TITLE     Purification by affinity chromatography using amastatin and
            properties of aminopeptidase A from pig kidney.
  JOURNAL   Biochim. Biophys. Acta. 613 (1980) 459-68.
  ORGANISM  pig [GN:ssc]
REFERENCE   5  [PMID:1689065]
  AUTHORS   Wu Q, Lahti JM, Air GM, Burrows PD, Cooper MD.
  TITLE     Molecular cloning of the murine BP-1/6C3 antigen: a member of the
            zinc-dependent metallopeptidase family.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 993-7.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map04614  Renin-angiotensin system
ORTHOLOGY   KO: K01261  glutamyl aminopeptidase
GENES       HSA: 2028(ENPEP)
            PTR: 461437(ENPEP)
            MMU: 13809(Enpep)
            RNO: 64017(Enpep)
            CFA: 478517(ENPEP)
            BTA: 504350(ENPEP)
            SSC: 397080(ENPEP)
            GGA: 428771(ENPEP)
            DME: Dmel_CG32473
            PIC: PICST_65905(APE2.2)
            AFM: AFUA_5G04330
            BCY: Bcer98_3359
            BPU: BPUM_2633(ytoP)
            SAC: SACOL1795(pepA1) SACOL2463(pepA2)
            SAA: SAUSA300_1691
            SAJ: SaurJH9_1800
            SAH: SaurJH1_1835
            SER: SERP1305(pepA)
            SHA: SH1177
            LLA: L193909(pepA)
            LLC: LACR_0433
            LLM: llmg_0403(pepA)
            SPY: SPy_0115(pepA)
            SPZ: M5005_Spy_0097(pepA)
            SPM: spyM18_0115
            SPG: SpyM3_0089(pepA)
            SPS: SPs0090
            SPH: MGAS10270_Spy0099(pepA)
            SPI: MGAS10750_Spy0104(pepA)
            SPJ: MGAS2096_Spy0100(pepA)
            SPK: MGAS9429_Spy0098(pepA)
            SPF: SpyM50095(pepA)
            SPA: M6_Spy0145
            SPB: M28_Spy0095(pepA)
            SPN: SP_1865
            SPR: spr1682(pepA)
            SPD: SPD_1647(pepA)
            SAG: SAG0174(pepA)
            SAN: gbs0172
            SAK: SAK_0240(pepA)
            SMU: SMU.1973(pepA)
            STC: str1851(pepA)
            STL: stu1851(pepA)
            SSA: SSA_0209(pepA)
            SGO: SGO_1898
            EFA: EF3037(pepA)
            CDF: CD2152
            CBO: CBO0213
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.7
            ExPASy - ENZYME nomenclature database: 3.4.11.7
            ExplorEnz - The Enzyme Database: 3.4.11.7
            ERGO genome analysis and discovery system: 3.4.11.7
            BRENDA, the Enzyme Database: 3.4.11.7
            CAS: 9074-83-3
///
ENTRY       EC 3.4.11.8       Obsolete  Enzyme
NAME        Transferred to 3.4.19.3
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
COMMENT     Transferred entry: now EC 3.4.19.3 pyroglutamyl-peptidase I (EC
            3.4.11.8 created 1972, deleted 1981)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.8
            ExPASy - ENZYME nomenclature database: 3.4.11.8
            ExplorEnz - The Enzyme Database: 3.4.11.8
            ERGO genome analysis and discovery system: 3.4.11.8
            BRENDA, the Enzyme Database: 3.4.11.8
///
ENTRY       EC 3.4.11.9                 Enzyme
NAME        Xaa-Pro aminopeptidase;
            proline aminopeptidase;
            aminopeptidase P;
            aminoacylproline aminopeptidase;
            X-Pro aminopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of any N-terminal amino acid, including proline, that is
            linked to proline, even from a dipeptide or tripeptide
COFACTOR    Manganese [CPD:C00034];
            Cobalt [CPD:C00175]
COMMENT     A Mn2+-dependent, generally membrane-bound enzyme present in both
            mammalian and bacterial cells. In peptidase family M24 (methionyl
            aminopeptidase family)
REFERENCE   1  [PMID:4878817]
  AUTHORS   Yaron A, Mlynar D.
  TITLE     Aminopeptidase-P.
  JOURNAL   Biochem. Biophys. Res. Commun. 32 (1968) 658-63.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Yaron, A. and Berger, A.
  TITLE     Aminopeptidase-P.
  JOURNAL   Methods Enzymol. 19 (1970) 522-534.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:6749499]
  AUTHORS   Fleminger G, Carmel A, Goldenberg D, Yaron A.
  TITLE     Fluorogenic substrates for bacterial aminopeptidase P and its
            analogs detected in human serum and calf lung.
  JOURNAL   Eur. J. Biochem. 125 (1982) 609-15.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:3627107]
  AUTHORS   Orawski AT, Susz JP, Simmons WH.
  TITLE     Aminopeptidase P from bovine lung: solubilization, properties, and
            potential role in bradykinin degradation.
  JOURNAL   Mol. Cell. Biochem. 75 (1987) 123-32.
  ORGANISM  cow [GN:bta]
REFERENCE   5  [PMID:2139778]
  AUTHORS   Hooper NM, Hryszko J, Turner AJ.
  TITLE     Purification and characterization of pig kidney aminopeptidase P. A
            glycosyl-phosphatidylinositol-anchored ectoenzyme.
  JOURNAL   Biochem. J. 267 (1990) 509-15.
  ORGANISM  pig [GN:ssc]
ORTHOLOGY   KO: K01262  X-Pro aminopeptidase
GENES       HSA: 7511(XPNPEP1) 7512(XPNPEP2)
            PTR: 450726(XPNPEP1) 458859(XPNPEP3) 465852(XPNPEP2)
            MMU: 170745(Xpnpep2) 170750(Xpnpep1)
            RNO: 170751(Xpnpep1)
            CFA: 486880(XPNPEP1) 492124(XPNPEP2)
            BTA: 504822(LOC504822) 513156(XPNPEP1) 539202(LOC539202)
            SSC: 445538(XPNPEP2)
            GGA: 418002(XPNPEP3) 423886(XPNPEP1)
            XLA: 414716(MGC83093) 446780(MGC80423)
            DRE: 394007(zgc:63528) 406253(xpnpep1)
            SPU: 581095(LOC581095) 589972(LOC589972)
            DME: Dmel_CG6291(ApepP) Dmel_CG9581
            CEL: R119.2(peptidase) W03G9.4(aminopeptidase)
            ATH: AT4G36760(ATAPP1)
            OSA: 4342685 4350667
            CME: CMC096C
            PIC: PICST_75738(XPA1)
            CGR: CAGL0G03971g
            ANI: AN1780.2 AN7730.2
            AFM: AFUA_1G07720 AFUA_5G08050
            AOR: AO090001000597 AO090701000720
            CNE: CNK02680
            UMA: UM01270.1 UM03733.1
            DDI: DDBDRAFT_0188915 DDBDRAFT_0218347
            PFA: PF14_0517
            TAN: TA10245
            TET: TTHERM_00624780
            TBR: Tb927.3.2090
            TCR: 503991.20 507081.110
            LMA: LmjF02.0040
            EHI: 254.t00003
            ECO: b2908(pepP)
            ECJ: JW2876(pepP)
            ECE: Z4245(pepP)
            ECS: ECs3779
            ECC: c3490(pepP)
            ECI: UTI89_C3294(pepP)
            ECP: ECP_2901
            ECV: APECO1_3620(pepB)
            ECW: EcE24377A_3236(pepP)
            ECX: EcHS_A3067
            STY: STY3214(pepP)
            STT: t2976(pepP)
            SPT: SPA2926(pepP)
            SEC: SC2999(pepP)
            STM: STM3058(pepP)
            YPE: YPO0910(pepP)
            YPK: y3297(pepP)
            YPM: YP_3607(pepP2)
            YPA: YPA_0357
            YPN: YPN_3109
            YPS: YPTB3185(pepP)
            YPI: YpsIP31758_0860(pepP)
            SFL: SF2894(pepP)
            SFX: S3093(pepP)
            SFV: SFV_2956(pepP)
            SSN: SSON_3061(pepP)
            SBO: SBO_3084(pepP)
            SDY: SDY_3173(pepP)
            ECA: ECA0459(pepP)
            PLU: plu3601(pepP)
            WBR: WGLp432(pepP)
            SGL: SG2005
            HIT: NTHI0980(pepP)
            HDU: HD1418(pepP)
            HSO: HS_0682(pepP)
            PMU: PM1724(pepP)
            MSU: MS0479(pepP)
            APL: APL_0663(pepP)
            XFA: XF2009
            XFT: PD0803(pepP)
            XCC: XCC3259(pepP)
            XCB: XC_0905
            XCV: XCV3522(pepP)
            XAC: XAC3405(pepP)
            XOO: XOO1133(pepP)
            XOM: XOO_1029(XOO1029)
            VCH: VC0067
            VCO: VC0395_A2447
            VVU: VV1_0958
            VVY: VV3201
            VPA: VP3021
            VFI: VF0038
            PPR: PBPRA0111
            PAE: PA5224(pepP)
            PAU: PA14_69000(pepP)
            PPU: PP_2238 PP_5200(pepP)
            PST: PSPTO_3437 PSPTO_5223(pepP)
            PSB: Psyr_0321 Psyr_3219
            PSP: PSPPH_0306(pepP) PSPPH_3138
            PFL: PFL_4151 PFL_5968
            PFO: Pfl_3911 Pfl_5434
            PEN: PSEEN3528 PSEEN5315(pepP)
            PCR: Pcryo_2273
            ACI: ACIAD1126(pepP)
            SON: SO_1388
            SDN: Sden_0887
            SFR: Sfri_3047
            SHN: Shewana3_2986
            ILO: IL2098(pepP)
            CPS: CPS_1271(pepP)
            PHA: PSHAa0562(pepP)
            PAT: Patl_3502
            SDE: Sde_3513
            CBU: CBU_0073
            LPN: lpg0077(pepP)
            LPF: lpl0079(pepP)
            LPP: lpp0091(pepP)
            MCA: MCA2770(pepP)
            TCX: Tcr_1559
            NOC: Noc_2579
            HCH: HCH_01070
            CSA: Csal_0024 Csal_2924
            ABO: ABO_2600(pepP)
            AHA: AHA_0563
            VOK: COSY_0118(pepP)
            CVI: CV_0130 CV_2796 CV_3122(pepP)
            RSO: RSc0509(pepP)
            REU: Reut_A0492
            REH: H16_B0923(pepP)
            RME: Rmet_0432 Rmet_5054
            BMA: BMA2360(pepP) BMAA0507
            BMV: BMASAVP1_A0274(pepP)
            BML: BMA10299_A1135(pepP)
            BMN: BMA10247_2540(pepP)
            BXE: Bxe_A0440 Bxe_A0623
            BUR: Bcep18194_A3601 Bcep18194_A3781 Bcep18194_A6376
            BCN: Bcen_0211
            BCH: Bcen2424_0514 Bcen2424_0695 Bcen2424_3029
            BAM: Bamb_0418 Bamb_0588 Bamb_3074
            BPS: BPSL1247 BPSL2892 BPSL3070
            BPM: BURPS1710b_1478 BURPS1710b_3399(pepP) BURPS1710b_3598
            BPL: BURPS1106A_3394(pepP)
            BPD: BURPS668_3358(pepP)
            BTE: BTH_I1254 BTH_I2888 BTH_I2927
            BPE: BP2391 BP3411
            BPA: BPP3256 BPP3561
            BBR: BB3707 BB3996
            RFR: Rfer_0086
            POL: Bpro_4829
            MPT: Mpe_A0254
            HAR: HEAR0363(pepP)
            MMS: mma_0414
            NEU: NE2147(pepP)
            NET: Neut_2095
            NMU: Nmul_A0128
            EBA: ebA1146(pepP)
            AZO: azo2890(pepP)
            DAR: Daro_3662
            TBD: Tbd_2334
            MFA: Mfla_2146
            HPY: HP1037
            HPJ: jhp0387(pepQ)
            HPA: HPAG1_0410
            HHE: HH0944
            HAC: Hac_1141
            WSU: WS1644(pepQ)
            TDN: Tmden_1524
            GME: Gmet_0982
            PCA: Pcar_2129
            DVU: DVU0296
            DDE: Dde_0217
            LIP: LI0314(pepP) LI0823(pepQ)
            BBA: Bd0202(pepP) Bd1372(pepP)
            ADE: Adeh_3287
            MXA: MXAN_0463(pepP) MXAN_2026(pepP) MXAN_2861(dmpA)
            SAT: SYN_01652 SYN_03148
            RFE: RF_0840(pepP)
            RBE: RBE_0916(pepP)
            WOL: WD1008
            WBM: Wbm0612
            APH: APH_0353
            PUB: SAR11_0015(pepP)
            MLO: mlr1535
            MES: Meso_1994
            SME: SMc01885
            ATU: Atu2070
            ATC: AGR_C_3749
            RET: RHE_CH02827(ypch00974)
            RLE: RL3284
            BME: BMEI0591
            BMF: BAB1_1437
            BMS: BR1418
            BMB: BruAb1_1413
            BOV: BOV_1374
            BJA: blr6589
            BRA: BRADO5647
            BBT: BBta_6160
            RPA: RPA3515
            RPB: RPB_2010
            RPC: RPC_3291
            RPD: RPD_3379
            RPE: RPE_2123
            NWI: Nwi_2368
            NHA: Nham_2747
            BHE: BH11110
            BQU: BQ08750
            CCR: CC_1525
            SIL: SPO2857
            SIT: TM1040_0641
            RSP: RSP_1975
            RDE: RD1_3341
            HNE: HNE_0381
            ZMO: ZMO0491(pepP)
            NAR: Saro_0152 Saro_0438
            SAL: Sala_2994
            ELI: ELI_11900
            GOX: GOX2387
            GBE: GbCGDNIH1_2193
            RRU: Rru_A2865
            MAG: amb0738
            MGM: Mmc1_3486
            ABA: Acid345_3224 Acid345_4208
            BSU: BG11708(yqhT)
            BAN: BA1901
            BAR: GBAA1901
            BAA: BA_2405
            BAT: BAS1763
            BCE: BC1828
            BCA: BCE_1982
            BCZ: BCZK1712(pepP)
            BTK: BT9727_1740(pepP)
            BTL: BALH_1682(pepP)
            BLI: BL01543(yqhT)
            BLD: BLi02617(yqhT)
            SHA: SH1386
            LMO: lmo1354
            LMF: LMOf2365_1371
            LIN: lin1391
            LWE: lwe1369
            LLA: L90422(pepP)
            LLC: LACR_0719
            LLM: llmg_1881(pepP)
            SPY: SPy_1824(pepP)
            SPM: spyM18_1889(pepP)
            SPG: SpyM3_1576(pepP)
            SPS: SPs0291
            SPH: MGAS10270_Spy0424(pepQ)
            SPI: MGAS10750_Spy0436(pepQ)
            SPJ: MGAS2096_Spy0442(pepQ)
            SPK: MGAS9429_Spy0422(pepQ)
            SPN: SP_0187
            SPR: spr0172(pepP)
            SAN: gbs1751
            SMU: SMU.1850(pepP)
            STC: str1742(pepP)
            STL: stu1742(pepP)
            SSA: SSA_0449(pepP)
            SGO: SGO_1864
            LPL: lp_1595(pepP)
            LSL: LSL_0419(pepQ)
            LDB: Ldb1429(pepP)
            LBU: LBUL_1324
            LBR: LVIS_0982
            LCA: LSEI_1643
            LGA: LGAS_0747
            EFA: EF0973(pepQ-1)
            CPE: CPE2530
            CPF: CPF_2854(pepP)
            CPR: CPR_2539(pepP)
            CTC: CTC01592
            CNO: NT01CX_0615 NT01CX_1472
            CBO: CBO0542(pepP)
            CBA: CLB_0581(pepP)
            CBH: CLC_0465(pepP)
            CBF: CLI_0620(pepP)
            CHY: CHY_1873(pepP)
            DSY: DSY1708 DSY4692
            TTE: TTE1280(pepP)
            MPN: MPN470(pepX)
            MPU: MYPU_4880(pepP)
            MPE: MYPE3910(pepP)
            MGA: MGA_0104(pepP)
            MHY: mhp680(pepP)
            MHJ: MHJ_0659(pepP)
            MHP: MHP7448_0659(pepP)
            MSY: MS53_0149(pepP)
            UUR: UU532(pepP)
            POY: PAM245(pepP)
            CGB: cg1826(pepQ)
            CJK: jk1029(pepQ)
            SCO: SCO1352(2SCG61.34c) SCO3970(SCBAC25E3.07c)
            SMA: SAV4230(pepP)
            TWH: TWT522(pepQ)
            TWS: TW238
            LXX: Lxx09170(pepP)
            CMI: CMM_0805(pepP1) CMM_1189(pepP2)
            ART: Arth_2788
            AAU: AAur_2773(pepP)
            PAC: PPA0650
            NCA: Noca_1364
            TFU: Tfu_1744
            FRA: Francci3_3497
            FAL: FRAAL5689(pepP)
            ACE: Acel_0669
            KRA: Krad_1161
            STP: Strop_3058
            BLO: BL1350(pepP)
            BAD: BAD_1089(pepP)
            FNU: FN0453
            RBA: RB8547
            CTR: CT574(pepP)
            CMU: TC0863
            CPN: CPn0813(pepP)
            CPA: CP1058
            CPJ: CPj0813(pepP)
            CPT: CpB0842
            CCA: CCA00950
            CAB: CAB919
            CFE: CF0064(pepP)
            LIL: LA2687(pepP)
            LIC: LIC11313(pepP)
            LBJ: LBJ_1022(pepP)
            LBL: LBL_2012(pepP)
            SYN: sll0136(pepP)
            SYW: SYNW0506(pepP)
            SYC: syc1429_c(pepP)
            SYF: Synpcc7942_0075
            SYD: Syncc9605_2176
            SYE: Syncc9902_0500
            SYG: sync_2290
            SYR: SynRCC307_1866(pepP)
            SYX: SynWH7803_2005(pepP)
            CYA: CYA_1706
            CYB: CYB_1026
            TEL: tll2265
            GVI: glr0093
            ANA: all0266 alr1946
            AVA: Ava_2777
            PMA: Pro1595(pepP)
            PMM: PMM1442(pepP)
            PMT: PMT1456(pepP)
            PMN: PMN2A_0973
            PMI: PMT9312_1535
            PMB: A9601_16441(pepP)
            PMC: P9515_16211(pepP)
            PMF: P9303_04951(pepP)
            PMG: P9301_16321(pepP)
            PMH: P9215_17101
            PME: NATL1_18411(pepP)
            TER: Tery_4599
            BFR: BF4360
            BFS: BF4027 BF4158
            SRU: SRU_1497 SRU_1805(pepP)
            CHU: CHU_3034(pepP)
            GFO: GFO_0851(pepP) GFO_3143(pepP)
            FPS: FP0153(pepP)
            CTE: CT1608(pepP)
            DEH: cbdb_A671
            TTH: TTC0703 TTC1273
            TTJ: TTHA1068
            TMA: TM0042
            MAC: MA0213(pepQ2)
            MBA: Mbar_A1315
            MMA: MM_0974 MM_1500
            MBU: Mbur_1619
            MHU: Mhun_2340
            MTH: MTH981
            MKA: MK0223(pepP)
            HAL: VNG1233G(pepQ2)
            HMA: rrnAC0322(pepQ)
            HWA: HQ1363A(pepQ) HQ3353A(pepQ)
            NPH: NP3076A(pepQ)
            RCI: RRC18(pepP)
STRUCTURES  PDB: 1A16  1JAW  1M35  1N51  1W2M  1W7V  1WBQ  1WL6  1WL9  1WLR  
                 2BH3  2BHA  2BHB  2BHC  2BHD  2BN7  2BWS  2BWT  2BWU  2BWV  
                 2BWW  2BWX  2BWY  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.9
            ExPASy - ENZYME nomenclature database: 3.4.11.9
            ExplorEnz - The Enzyme Database: 3.4.11.9
            ERGO genome analysis and discovery system: 3.4.11.9
            BRENDA, the Enzyme Database: 3.4.11.9
            CAS: 37288-66-7
///
ENTRY       EC 3.4.11.10                Enzyme
NAME        bacterial leucyl aminopeptidase;
            Aeromonas proteolytica aminopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of an N-terminal amino acid, preferentially leucine, but not
            glutamic or aspartic acids
COFACTOR    Zinc [CPD:C00038]
COMMENT     A zinc enzyme. Forms of the enzyme have been isolated from Aeromonas
            proteolytica, Escherichia coli and Staphylococcus thermophilus.
            Examples are known from peptidase families M17 and M28 (of leucyl
            aminopeptidase and aminopeptidase Y, respectively)
REFERENCE   1  [PMID:4961737]
  AUTHORS   Prescott JM, Wilkes SH.
  TITLE     Aeromonas aminopeptidase: purification and some general properties.
  JOURNAL   Arch. Biochem. Biophys. 117 (1966) 328-36.
  ORGANISM  Aeromonas proteolytica
REFERENCE   2  [PMID:4920230]
  AUTHORS   Dick AJ, Matheson AT, Wang JH.
  TITLE     A ribosomal-bound aminopeptidase in Escherichia coli B: purification
            and properties.
  JOURNAL   Can. J. Biochem. 48 (1970) 1181-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4749719]
  AUTHORS   Rabier D, Desmazeaud MJ.
  TITLE     [Inventory of different intracellular peptidase activities in
            Streptococcus thermophilus. Purification and properties of a
            dipeptide hydrolase and an aminopeptidase]
  JOURNAL   Biochimie. 55 (1973) 389-404.
ORTHOLOGY   KO: K05994  bacterial leucyl aminopeptidase
GENES       ANI: AN7035.2
            AFM: AFUA_4G04210
            AOR: AO090206000073
            VCH: VCA0813
            VCO: VC0395_0421
            HCH: HCH_03015
            AHA: AHA_3051
            CVI: CV_0056
            BMA: BMAA0487
            BUR: Bcep18194_B0596
            BCN: Bcen_3301
            BCH: Bcen2424_5067
            BAM: Bamb_4476
            BPS: BPSS0563
            BPM: BURPS1710b_A2124(apAC)
            BTE: BTH_II1852
            MXA: MXAN_5166
STRUCTURES  PDB: 1AMP  1CP6  1FT7  1IGB  1LOK  1RTQ  1TXR  1XRY  2ANP  2DEA  
                 2IQ6  2PRQ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.10
            ExPASy - ENZYME nomenclature database: 3.4.11.10
            ExplorEnz - The Enzyme Database: 3.4.11.10
            ERGO genome analysis and discovery system: 3.4.11.10
            BRENDA, the Enzyme Database: 3.4.11.10
            CAS: 37288-67-8
///
ENTRY       EC 3.4.11.11      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
COMMENT     Deleted entry: aminopeptidase (EC 3.4.11.11 created 1978, deleted
            1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.11
            ExPASy - ENZYME nomenclature database: 3.4.11.11
            ExplorEnz - The Enzyme Database: 3.4.11.11
            ERGO genome analysis and discovery system: 3.4.11.11
            BRENDA, the Enzyme Database: 3.4.11.11
///
ENTRY       EC 3.4.11.12      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
COMMENT     Deleted entry: thermophilic aminopeptidase (EC 3.4.11.12 created
            1978, deleted 1997)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.12
            ExPASy - ENZYME nomenclature database: 3.4.11.12
            ExplorEnz - The Enzyme Database: 3.4.11.12
            ERGO genome analysis and discovery system: 3.4.11.12
            BRENDA, the Enzyme Database: 3.4.11.12
///
ENTRY       EC 3.4.11.13                Enzyme
NAME        clostridial aminopeptidase;
            Clostridium histolyticum aminopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of any N-terminal amino acid, including proline and
            hydroxyproline, but no cleavage of Xaa-Pro-
COFACTOR    Manganese [CPD:C00034];
            Cobalt [CPD:C00175]
COMMENT     A secreted enzyme from Clostridium histolyticum, requiring Mn2+ or
            Co2+
REFERENCE   1  [PMID:4631895]
  AUTHORS   Kessler E, Yaron A.
  TITLE     A novel aminopeptidase from Clostridium histolyticum.
  JOURNAL   Biochem. Biophys. Res. Commun. 50 (1973) 405-12.
  ORGANISM  Clostridium histolyticum
REFERENCE   2  [PMID:4318]
  AUTHORS   Kessler E, Yaron A.
  TITLE     An extracellular aminopeptidase from Clostridium histolyticum.
  JOURNAL   Eur. J. Biochem. 63 (1976) 271-87.
  ORGANISM  Clostridium histolyticum
REFERENCE   3  [PMID:13266]
  AUTHORS   Kessler E, Yaron A.
  TITLE     Extracellular aminopeptidase from Clostridium histolyticum.
  JOURNAL   Methods. Enzymol. 45 (1976) 544-52.
  ORGANISM  Clostridium histolyticum
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.13
            ExPASy - ENZYME nomenclature database: 3.4.11.13
            ExplorEnz - The Enzyme Database: 3.4.11.13
            ERGO genome analysis and discovery system: 3.4.11.13
            BRENDA, the Enzyme Database: 3.4.11.13
            CAS: 59680-69-2
///
ENTRY       EC 3.4.11.14                Enzyme
NAME        cytosol alanyl aminopeptidase;
            arylamidase;
            aminopolypeptidase;
            thiol-activated aminopeptidase;
            human liver aminopeptidase;
            puromycin-sensitive aminopeptidase;
            soluble alanyl aminopeptidase;
            cytosol aminopeptidase III;
            alanine aminopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of an N-terminal amino acid, preferentially alanine, from a
            wide range of peptides, amides and arylamides
COFACTOR    Zinc [CPD:C00038];
            Cobalt [CPD:C00175]
COMMENT     A puromycin-sensitive, Co2+-activated zinc-sialoglycoprotein that is
            generally cytosolic. Multiple forms are widely distributed in
            mammalian tissues and body fluids. In peptidase family M1 (membrane
            alanyl aminopeptidase family)
REFERENCE   1  [PMID:4841062]
  AUTHORS   Starnes WL, Behal FJ.
  TITLE     A human liver aminopeptidase. The amino acid and carbohydrate
            content, and some physical properties of a sialic acid containing
            glycoprotein.
  JOURNAL   Biochemistry. 13 (1974) 3221-7.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:698181]
  AUTHORS   Kao YJ, Starnes WL, Behal FJ.
  TITLE     Human kidney alanine aminopeptidase: physical and kinetic properties
            of a sialic acid containing glycoprotein.
  JOURNAL   Biochemistry. 17 (1978) 2990-4.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:6108169]
  AUTHORS   Sidorowicz W, Hsia WC, Maslej-Zownir O, Behal FJ.
  TITLE     Multiple molecular forms of human alanine aminopeptidase:
            immunochemical properties.
  JOURNAL   Clin. Chim. Acta. 107 (1980) 245-56.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01263  cytosol alanyl aminopeptidase
GENES       TBR: Tb927.7.6270
            TCR: 506513.110 511051.70
            LMA: LmjF17.0140
            EHI: 242.t00016
            XCC: XCC3168(pepN)
            XCB: XC_0997
            XCV: XCV3437(pepN3)
            XAC: XAC3318(pepN)
            XOO: XOO3393(pepN)
            XOM: XOO_3194(XOO3194)
            PAT: Patl_1912
            DNO: DNO_0201(pepT-1) DNO_1350(pepT-2)
            BCZ: BCZK3898(pepT)
            BTK: BT9727_3891(pepT)
            BTL: BALH_3758(pepT)
            SAB: SAB1385c
            SAO: SAOUHSC_01606
            LLC: LACR_1996
            LLM: llmg_1994(pepT)
            SPF: SpyM51192(pepT)
            SGO: SGO_1312(pepT)
            LJO: LJ0645
            EFA: EF3080(pepT-2)
            CNO: NT01CX_0717(pepT)
            CDF: CD1046(pepT)
            CBO: CBO0438(pepT)
STRUCTURES  PDB: 1VIX  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.14
            ExPASy - ENZYME nomenclature database: 3.4.11.14
            ExplorEnz - The Enzyme Database: 3.4.11.14
            ERGO genome analysis and discovery system: 3.4.11.14
            BRENDA, the Enzyme Database: 3.4.11.14
            CAS: 243859-94-1
///
ENTRY       EC 3.4.11.15                Enzyme
NAME        aminopeptidase Y;
            aminopeptidase Co;
            aminopeptidase (cobalt-activated);
            lysyl aminopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Preferentially, release of N-terminal lysine
COFACTOR    Cobalt [CPD:C00175]
INHIBITOR   Manganese [CPD:C00034];
            Zinc [CPD:C00038]
COMMENT     Requires Co2+; inhibited by Zn2+ and Mn2+. An enzyme best known from
            Saccharomyces cerevisiae that hydrolyses Lys-NHPhNO2 and, more
            slowly, Arg-NHPhNO2. Type example of peptidase family M28
REFERENCE   1  [PMID:6758786]
  AUTHORS   Achstetter T, Ehmann C, Wolf DH.
  TITLE     Aminopeptidase Co, a new yeast peptidase.
  JOURNAL   Biochem. Biophys. Res. Commun. 109 (1982) 341-7.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:8175799]
  AUTHORS   Yasuhara T, Nakai T, Ohashi A.
  TITLE     Aminopeptidase Y, a new aminopeptidase from Saccharomyces
            cerevisiae. Purification, properties, localization, and processing
            by protease B.
  JOURNAL   J. Biol. Chem. 269 (1994) 13644-50.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:8175800]
  AUTHORS   Nishizawa M, Yasuhara T, Nakai T, Fujiki Y, Ohashi A.
  TITLE     Molecular cloning of the aminopeptidase Y gene of Saccharomyces
            cerevisiae. Sequence analysis and gene disruption of a new
            aminopeptidase.
  JOURNAL   J. Biol. Chem. 269 (1994) 13651-5.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K01264  aminopeptidase Y
GENES       SCE: YBR286W(APE3)
            AGO: AGOS_ADR123W
            PIC: PICST_89245(APE3.1)
            CAL: CaO19.3591
            CGR: CAGL0G07623g
            ANI: AN3918.2
            AFM: AFUA_2G00220
            AOR: AO090012000110
            PMY: Pmen_3548
            SSA: SSA_0955(pepN)
            MVA: Mvan_0715 Mvan_0716
            MGI: Mflv_0189 Mflv_0190
            MKM: Mkms_0565 Mkms_0566
            MJL: Mjls_0543 Mjls_0544
            STP: Strop_1408
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.15
            ExPASy - ENZYME nomenclature database: 3.4.11.15
            ExplorEnz - The Enzyme Database: 3.4.11.15
            ERGO genome analysis and discovery system: 3.4.11.15
            BRENDA, the Enzyme Database: 3.4.11.15
///
ENTRY       EC 3.4.11.16                Enzyme
NAME        Xaa-Trp aminopeptidase;
            aminopeptidase W;
            aminopeptidase X-Trp;
            X-Trp aminopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of a variety of N-terminal residues (especially glutamate
            and leucine) from peptides, provided tryptophan (or at least
            phenylalanine or tyrosine) is the penultimate residue. Also acts on
            Glu!Trp, Leu!Trp and a number of other dipeptides
COMMENT     A glycoprotein containing Zn2+, from renal and intestinal brush
            border membranes
REFERENCE   1  [PMID:4062876]
  AUTHORS   Gee NS, Kenny AJ.
  TITLE     Proteins of the kidney microvillar membrane. The 130 kDa protein in
            pig kidney, recognized by monoclonal antibody GK5C1, is an
            ectoenzyme with aminopeptidase activity.
  JOURNAL   Biochem. J. 230 (1985) 753-64.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:2890346]
  AUTHORS   Gee NS, Kenny AJ.
  TITLE     Proteins of the kidney microvillar membrane. Enzymic and molecular
            properties of aminopeptidase W.
  JOURNAL   Biochem. J. 246 (1987) 97-102.
  ORGANISM  pig [GN:ssc]
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.16
            ExPASy - ENZYME nomenclature database: 3.4.11.16
            ExplorEnz - The Enzyme Database: 3.4.11.16
            ERGO genome analysis and discovery system: 3.4.11.16
            BRENDA, the Enzyme Database: 3.4.11.16
            CAS: 137010-33-4
///
ENTRY       EC 3.4.11.17                Enzyme
NAME        tryptophanyl aminopeptidase;
            tryptophan aminopeptidase;
            L-tryptophan aminopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Preferential release of N-terminal tryptophan
COFACTOR    Manganese [CPD:C00034]
COMMENT     From Trichosporon cutaneum. Also acts on L-tryptophanamide. Requires
            Mn2+
REFERENCE   1
  AUTHORS   Iwayama, A., Kimura, T., Adachi, O. and Ameyama, M.
  TITLE     Crystallization and characterization of a novel aminopeptidase from
            Trichosporon cutaneum.
  JOURNAL   Agric. Biol. Chem. 47 (1983) 2483-2493.
  ORGANISM  Trichosporon cutaneum
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.17
            ExPASy - ENZYME nomenclature database: 3.4.11.17
            ExplorEnz - The Enzyme Database: 3.4.11.17
            ERGO genome analysis and discovery system: 3.4.11.17
            BRENDA, the Enzyme Database: 3.4.11.17
            CAS: 76689-19-5
///
ENTRY       EC 3.4.11.18                Enzyme
NAME        methionyl aminopeptidase;
            methionine aminopeptidase;
            peptidase M;
            L-methionine aminopeptidase;
            MAP
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of N-terminal amino acids, preferentially methionine, from
            peptides and arylamides
COMMENT     Membrane-bound enzyme present in both prokaryotes and eukaryotes.
            Type example of peptidase family M24. Releases methionine from
            nascent peptides
REFERENCE   1  [PMID:4110013]
  AUTHORS   Yoshida A, Lin M.
  TITLE     NH 2 -terminal formylmethionine- and NH 2 -terminal
            methionine-cleaving enzymes in rabbits.
  JOURNAL   J. Biol. Chem. 247 (1972) 952-7.
  ORGANISM  rabbit
REFERENCE   2  [PMID:2985590]
  AUTHORS   Tsunasawa S, Stewart JW, Sherman F.
  TITLE     Amino-terminal processing of mutant forms of yeast iso-1-cytochrome
            c. The specificities of methionine aminopeptidase and
            acetyltransferase.
  JOURNAL   J. Biol. Chem. 260 (1985) 5382-91.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:3937747]
  AUTHORS   Freitas JO Jr, Termignoni C, Guimaraes JA.
  TITLE     Microsomal methionine aminopeptidase: properties of the
            detergent-solubilized enzyme.
  JOURNAL   Int. J. Biochem. 17 (1985) 1285-91.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:3027045]
  AUTHORS   Ben-Bassat A, Bauer K, Chang SY, Myambo K, Boosman A, Chang S.
  TITLE     Processing of the initiation methionine from proteins: properties of
            the Escherichia coli methionine aminopeptidase and its gene
            structure.
  JOURNAL   J. Bacteriol. 169 (1987) 751-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:3141408]
  AUTHORS   Roderick SL, Matthews BW.
  TITLE     Crystallization of methionine aminopeptidase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 263 (1988) 16531.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01265  methionyl aminopeptidase
GENES       HSA: 10988(METAP2) 23173(METAP1) 254042(MAP1D)
            PTR: 452141(METAP2) 461392(METAP1)
            MMU: 56307(Metap2) 66559(Metapl1) 75624(Metap1)
            RNO: 295500(Metap1_predicted) 311748(Metapl1_predicted)
                 498869(RGD1560341_predicted) 64370(Metap2)
            CFA: 475429(METAP2) 487871(LOC487871) 488399(LOC488399)
            BTA: 404150(METAP2) 516540(MGC152490) 533042(MAP1D)
            GGA: 417912(METAP2) 422704(RCJMB04_24o19) 424150(LOC424150)
            XLA: 379465(MGC64362) 380164(metap2) 443662(LOC443662)
            XTR: 496944(metap1) 548869(LOC548869)
            DRE: 323452(metap2) 503783(metap1) 554090(zgc:110461)
            SPU: 576778(LOC576778) 578258(LOC578258) 579158(LOC579158)
                 582111(LOC582111) 586566(LOC586566)
            DME: Dmel_CG13630 Dmel_CG4008(und) Dmel_CG5188
            CEL: Y116A8A.9(map-2) Y37E11AL.7(map-1)
            ATH: AT1G13270(MAP1C)
            OSA: 4330811 4336948 4343067 4349075
            CME: CMP247C CMT169C CMT395C
            SCE: YBL091C(MAP2) YLR244C(MAP1)
            AGO: AGOS_AGL122W
            PIC: PICST_31342 PICST_64750(MAP1)
            CGR: CAGL0G03641g CAGL0G08250g
            SPO: SPBC14C8.03 SPBC3E7.10
            ANI: AN0369.2 AN4404.2 AN5055.2 AN5199.2
            AFM: AFUA_2G01750 AFUA_2G16820 AFUA_4G06930 AFUA_6G07330
                 AFUA_8G00410 AFUA_8G00460
            AOR: AO090005001568 AO090113000045 AO090120000238
            CNE: CNB04150 CNG02860
            ECU: ECU10_0750
            DDI: DDBDRAFT_0205763 DDBDRAFT_0206394
            PFA: MAL8P1.140 PF10_0150 PF14_0261 PF14_0327 PFE1360c
            CPV: cgd1_2700 cgd2_2480
            CHO: Chro.10305 Chro.20263
            TAN: TA07050 TA09495 TA10075 TA18485
            TPV: TP03_0462 TP03_0593 TP04_0063 TP04_0770
            TET: TTHERM_00016600 TTHERM_00624400 TTHERM_00624430
                 TTHERM_00703440 TTHERM_01004930
            TBR: Tb10.61.1210 Tb10.70.6620
            TCR: 504111.20 506457.10 507031.120 509693.50
            LMA: LmjF19.0550 LmjF21.0840
            EHI: 159.t00001
            ECO: b0168(map)
            ECJ: JW0163(map)
            ECE: Z0178(map)
            ECS: ECs0170
            ECC: c0203(map)
            ECI: UTI89_C0182(map)
            ECP: ECP_0176
            ECV: APECO1_1819(map)
            ECW: EcE24377A_0171(map)
            ECX: EcHS_A0170
            STY: STY0238(map)
            STT: t0216(map)
            SPT: SPA0221(map)
            SEC: SC0215(map)
            STM: STM0215(map)
            YPE: YPO1043(ampM) YPO3337(map)
            YPK: y0852(map) y3138(map)
            YPM: YP_0350(map) YP_2808(ampM)
            YPA: YPA_0517 YPA_2807
            YPN: YPN_0756 YPN_2958
            YPS: YPTB0794(map) YPTB3004(ampM)
            YPI: YpsIP31758_1012(map1) YpsIP31758_3273(map2)
            SFL: SF0158(map)
            SFX: S0161(map)
            SFV: SFV_0151(map)
            SSN: SSON_0180(map)
            SBO: SBO_0156(map)
            SDY: SDY_0184(map)
            ECA: ECA1030(map)
            PLU: plu0671(map)
            BUC: BU230(map)
            BAS: BUsg224(map)
            BAB: bbp212(map)
            BCC: BCc_141(map)
            WBR: WGLp393(map)
            SGL: SG1944
            BFL: Bfl270(map)
            BPN: BPEN_278(map)
            HIT: NTHI2027(map)
            HIP: CGSHiEE_03440
            HIQ: CGSHiGG_02350
            HDU: HD0248(map)
            HSO: HS_0828(map)
            PMU: PM0459(map)
            MSU: MS1306(map)
            APL: APL_2030(map)
            XFA: XF0111
            XFT: PD0085(map)
            XCC: XCC1382(map)
            XCB: XC_2856
            XCV: XCV1485(map) XCV3894(map)
            XAC: XAC1428(map) XAC3782(map)
            XOO: XOO1983(map)
            XOM: XOO_1874(XOO1874)
            VCH: VC2261
            VCO: VC0395_A1852(map)
            VVU: VV1_1858
            VVY: VV2558
            VPA: VP2319
            VFI: VF1963
            PPR: PBPRA2969
            PAE: PA2748 PA3657(map)
            PAU: PA14_17050(map) PA14_28590(mapB)
            PAP: PSPA7_1482(map2) PSPA7_2495(map1)
            PPU: PP_1590(map)
            PST: PSPTO_1533(map-1) PSPTO_2362(map-2)
            PSB: Psyr_1342 Psyr_2146
            PSP: PSPPH_2120(map1) PSPPH_3841(map2)
            PFL: PFL_1175(map) PFL_3100(map)
            PFO: Pfl_1100 Pfl_3245
            PEN: PSEEN1415 PSEEN4221(map)
            PAR: Psyc_0396(map)
            PCR: Pcryo_0442
            ACI: ACIAD1987(map) ACIAD2271(map)
            SON: SO_1627(map)
            SDN: Sden_1553
            SFR: Sfri_1269
            SHE: Shewmr4_0884 Shewmr4_2642
            SHM: Shewmr7_2709 Shewmr7_3138
            SHN: Shewana3_2816 Shewana3_3230
            ILO: IL0846(map)
            CPS: CPS_1550(map)
            PHA: PSHAa2037(map)
            PAT: Patl_1248 Patl_1471
            SDE: Sde_2321 Sde_2601
            PIN: Ping_3003
            MAQ: Maqu_2549
            CBU: CBU_1388(map)
            CBD: COXBU7E912_0605(map)
            LPN: lpg0157(map-1) lpg1719(map)
            LPF: lpl0221 lpl1683
            LPP: lpp0221 lpp1684
            MCA: MCA0566(map)
            FTU: FTT0393(map)
            FTF: FTF0393(map)
            FTW: FTW_1681(map)
            FTL: FTL_0459
            FTH: FTH_0456(map)
            FTA: FTA_0486(map)
            FTN: FTN_0490(map)
            TCX: Tcr_1286
            NOC: Noc_0807
            AEH: Mlg_1864
            HHA: Hhal_1467
            HCH: HCH_03504(map1) HCH_05254(map2)
            CSA: Csal_0562
            ABO: ABO_1142(map)
            AHA: AHA_1172(map)
            DNO: DNO_0724(map)
            BCI: BCI_0526(map)
            CRP: CRP_019
            VOK: COSY_0369(map)
            NME: NMB2093
            NMA: NMA0337(map)
            NMC: NMC2073(map)
            NGO: NGO1983
            CVI: CV_2334(map2) CV_2397(map1)
            RSO: RSc1403(map)
            REU: Reut_A1882
            REH: H16_A2056(map)
            RME: Rmet_1434
            BMA: BMA1556(map-1) BMA1618(map-2)
            BMV: BMASAVP1_A2058(map-1) BMASAVP1_A2119(map-2)
            BML: BMA10299_A3195(map-2) BMA10299_A3253(map-1)
            BMN: BMA10247_1330(map-1) BMA10247_1393(map-2)
            BXE: Bxe_A1680 Bxe_A3427 Bxe_B0269
            BUR: Bcep18194_A4261 Bcep18194_A5330
            BCN: Bcen_0670 Bcen_6057
            BCH: Bcen2424_1149 Bcen2424_2020
            BAM: Bamb_1027 Bamb_2053
            BPS: BPSL2160(map) BPSL2212(map2)
            BPM: BURPS1710b_2584(map) BURPS1710b_2644(map)
            BPL: BURPS1106A_2495(map) BURPS1106A_2557(map)
            BPD: BURPS668_2438(map) BURPS668_2504(map)
            BTE: BTH_I1973(map-1) BTH_I2026(map-2)
            PNU: Pnuc_1452
            BPE: BP1418(map)
            BPA: BPP1526(map)
            BBR: BB2604(map)
            RFR: Rfer_0852 Rfer_2421
            POL: Bpro_2587
            PNA: Pnap_1820 Pnap_4816
            AAV: Aave_3100
            AJS: Ajs_2293
            VEI: Veis_3610
            MPT: Mpe_A1760
            HAR: HEAR1334(map)
            MMS: mma_0791 mma_2059
            NEU: NE0275(map)
            NET: Neut_0307
            NMU: Nmul_A2632
            EBA: ebA5984(map)
            AZO: azo1910(map)
            DAR: Daro_1740 Daro_2485
            TBD: Tbd_0784
            MFA: Mfla_0106 Mfla_1531
            HPY: HP1299
            HPA: HPAG1_1244
            HHE: HH1398(map)
            HAC: Hac_0155(map)
            WSU: WS1697(MAP)
            TDN: Tmden_0306
            CJE: Cj1651c(map)
            CJR: CJE1823(map)
            CJJ: CJJ81176_1642(map)
            CJU: C8J_1553(map)
            CJD: JJD26997_2012(map)
            CFF: CFF8240_0054(map)
            CHA: CHAB381_0104(map)
            CCO: CCC13826_1756(map)
            ABU: Abu_0772(map)
            NIS: NIS_0243(map)
            SUN: SUN_2341(map)
            GSU: GSU2835(map)
            GME: Gmet_0648
            PCA: Pcar_0723
            DVU: DVU1324(map)
            DDE: Dde_2236
            LIP: LI0978(map)
            BBA: Bd0649(map) Bd1338(map)
            DPS: DP1146 DP2240
            ADE: Adeh_1405 Adeh_1924
            MXA: MXAN_6714(map) MXAN_7084(map)
            SAT: SYN_01596
            SFU: Sfum_1577
            RPR: RP824
            RTY: RT0812(map)
            RCO: RC1276(map)
            RFE: RF_1309(map)
            RBE: RBE_0156(map)
            RAK: A1C_06395
            RBO: A1I_07100
            RCM: A1E_05355
            RRI: A1G_07020
            OTS: OTBS_1354(map)
            WOL: WD0167(map)
            WBM: Wbm0112
            AMA: AM1086(map)
            APH: APH_1199(map)
            ERU: Erum8160(map) Erum8161
            ERW: ERWE_CDS_08640(map)
            ERG: ERGA_CDS_08550(map)
            ECN: Ecaj_0856
            ECH: ECH_1064(map)
            NSE: NSE_0337(map)
            PUB: SAR11_1136(map)
            MLO: mlr0954
            MES: Meso_1455
            PLA: Plav_1552
            SME: SMb21002(map2) SMc00298(map1)
            SMD: Smed_1458 Smed_4508
            ATU: Atu1606(map) Atu2306(map)
            ATC: AGR_C_2957 AGR_C_4195
            RET: RHE_CH01849(map1) RHE_CH03116(map2)
            RLE: RL2069(map) RL3560(map)
            BME: BMEI0719
            BMF: BAB1_1300(map)
            BMS: BR1282(map)
            BMB: BruAb1_1283(map)
            BOV: BOV_1245(map)
            OAN: Oant_1910
            BJA: bll4871(map) blr8170(map)
            BRA: BRADO0719(map)
            BBT: BBta_7381(map)
            RPA: RPA0387(map)
            RPB: RPB_0058
            RPC: RPC_0578
            RPD: RPD_0155
            RPE: RPE_0094
            NWI: Nwi_0336
            NHA: Nham_0431
            BHE: BH08350(map)
            BQU: BQ06230(map)
            BBK: BARBAKC583_0829(map)
            CCR: CC_2677
            SIL: SPO3761(map)
            SIT: TM1040_2469
            RSP: RSP_0923(map1)
            RSH: Rsph17029_2582
            JAN: Jann_0285
            RDE: RD1_0949(map)
            PDE: Pden_3118 Pden_4919
            MMR: Mmar10_1044
            HNE: HNE_0953(map1) HNE_1332(map2)
            ZMO: ZMO1348(map)
            NAR: Saro_1110
            SAL: Sala_0378
            ELI: ELI_01690
            GOX: GOX0606
            GBE: GbCGDNIH1_1653
            ACR: Acry_1492
            RRU: Rru_A0733
            MAG: amb1603
            MGM: Mmc1_3022
            ABA: Acid345_1248 Acid345_1327
            SUS: Acid_7194
            BSU: BG10447(map) BG12942(yflG)
            BHA: BH0156(map)
            BAN: BA0132(maP-1) BA1590(maP-2) BA5601(maP-3)
            BAR: GBAA0132(maP-1) GBAA1590(maP-2) GBAA5601(maP-3)
            BAA: BA_0458 BA_0715 BA_2107
            BAT: BAS0132 BAS1474 BAS5204
            BCE: BC0153 BC1568 BC5356
            BCA: BCE_0132(map) BCE_1695(map) BCE_5486(map)
            BCZ: BCZK0126(map) BCZK1447(map) BCZK5054(map)
            BCY: Bcer98_3875
            BTK: BT9727_0128(map) BT9727_1446(map) BT9727_5038(map)
            BTL: BALH_0130(map) BALH_1416(map) BALH_4854(map)
            BLI: BL01029(map) BL03102
            BLD: BLi00155(map) BLi00792(yflG)
            BCL: ABC0172(map) ABC0743 ABC3950
            BAY: RBAM_001630 RBAM_007890(yflG)
            BPU: BPUM_0124 BPUM_0719(yflG)
            OIH: OB1116(map) OB3394
            GKA: GK0128 GK1833
            GTN: GTNG_1723
            SAU: SA1704(map)
            SAV: SAV1888(map)
            SAM: MW1828(map)
            SAR: SAR1978
            SAS: SAS1810
            SAC: SACOL1946
            SAB: SAB1820c
            SAA: SAUSA300_1869(map)
            SAO: SAOUHSC_02102
            SEP: SE1573
            SER: SERP1426(map)
            SHA: SH1064(map)
            SSP: SSP0905
            LMO: lmo1709
            LMF: LMOf2365_1733(map)
            LIN: lin1821
            LWE: lwe1729
            LLA: L883(pepM)
            LLC: LACR_0631
            LLM: llmg_0577(pepM)
            SPY: SPy_1354(map)
            SPZ: M5005_Spy_1103(map)
            SPM: spyM18_1366(map)
            SPG: SpyM3_1029(map)
            SPS: SPs0831
            SPH: MGAS10270_Spy1160(map)
            SPI: MGAS10750_Spy1202(map)
            SPJ: MGAS2096_Spy1165(map)
            SPK: MGAS9429_Spy1147(map)
            SPF: SpyM50756
            SPA: M6_Spy1075
            SPB: M28_Spy1095(map)
            SPN: SP_1084
            SPR: spr0992(map)
            SPD: SPD_0970(map)
            SAG: SAG0846(map)
            SAN: gbs0864
            SAK: SAK_0969(map)
            SMU: SMU.1556(ampM)
            STC: str1557(pepM)
            STL: stu1557(pepM)
            STE: STER_1516
            SSA: SSA_1491(map)
            SSU: SSU05_1617
            SSV: SSU98_1628
            SGO: SGO_1397(map)
            LPL: lp_0257(pepM)
            LJO: LJ1595
            LAC: LBA0623(ampM)
            LSA: LSA1515(pepM)
            LSL: LSL_1269(map)
            LDB: Ldb0556(pepM)
            LBU: LBUL_0496
            LBR: LVIS_1919 LVIS_2007
            LCA: LSEI_1088
            LGA: LGAS_0700
            LRE: Lreu_1385
            PPE: PEPE_0375
            EFA: EF2200(map)
            OOE: OEOE_1699
            LME: LEUM_1437
            STH: STH2575
            CAC: CAC3111
            CPE: CPE1382(map) CPE2383(map)
            CPF: CPF_1635(map) CPF_2692(map)
            CPR: CPR_1375(map) CPR_2377(map)
            CTC: CTC02582
            CNO: NT01CX_0188 NT01CX_1137
            CDF: CD0092(map1) CD1596(map2)
            CBO: CBO3459(map1) CBO3576(map2)
            CBA: CLB_3515(map-1) CLB_3657(map-2)
            CBH: CLC_3403(map-1) CLC_3555(map-2)
            CBF: CLI_3641(map-1) CLI_3796(map-2)
            CKL: CKL_0246(map1) CKL_2791(map2)
            CHY: CHY_2288(map)
            DSY: DSY0493 DSY2339
            DRM: Dred_0236
            SWO: Swol_1733 Swol_2311
            CSC: Csac_2266
            TTE: TTE2270(map)
            MTA: Moth_2438
            MGE: MG_172(map)
            MPN: MPN186(map)
            MPU: MYPU_5660(map)
            MPE: MYPE9960(map)
            MGA: MGA_0745(map)
            MMY: MSC_0724(map)
            MMO: MMOB2560(map)
            MHY: mhp209(map)
            MHJ: MHJ_0169(map)
            MHP: MHP7448_0173(map)
            MSY: MS53_0579(map)
            MCP: MCAP_0675(map)
            UUR: UU252(map)
            POY: PAM222(map)
            AYW: AYWB_500(map)
            MFL: Mfl145
            MTU: Rv0734(mapA) Rv2861c(mapB)
            MTC: MT0758(map-1) MT2929(map-2)
            MBO: Mb0755(mapA) Mb2886c(mapB)
            MBB: BCG_0784(mapA) BCG_2883c(mapB)
            MLE: ML1576(mapB) ML1831(mapA)
            MPA: MAP2934c(map) MAP4200(map')
            MAV: MAV_3721(map) MAV_4432(map)
            MSM: MSMEG_1485(map) MSMEG_2587(map) MSMEG_5050(map)
                 MSMEG_5683(map)
            MMC: Mmcs_1048 Mmcs_2050 Mmcs_3065
            CGL: NCgl0534(cgl0558) NCgl1932(cgl2007)
            CGB: cg0649(map1) cg2198(map2)
            CEF: CE0566 CE1901
            CDI: DIP0542(mapA) DIP1496(mapB)
            CJK: jk1159(mapB) jk1764(mapA)
            NFA: nfa31320 nfa40890(map) nfa7960
            RHA: RHA1_ro01746 RHA1_ro04072 RHA1_ro06155 RHA1_ro06604
            SCO: SCO2266(map3) SCO4724(map) SCO6409(map2)
            SMA: SAV1956(map1) SAV1974(map2) SAV4948(map3) SAV5931(map4)
            TWH: TWT259(map)
            TWS: TW511(map)
            LXX: Lxx09980(ampM) Lxx14830(map) Lxx20120(map)
            CMI: CMM_1371(mapA1) CMM_2596(mapA2)
            AAU: AAur_0976(map) AAur_1728(map) AAur_2402(map) AAur_2927(map)
            PAC: PPA0661 PPA1833
            NCA: Noca_3883
            TFU: Tfu_0968 Tfu_2624
            FRA: Francci3_0604
            FAL: FRAAL1104(map) FRAAL3739(map)
            ACE: Acel_0328
            SEN: SACE_2816(map) SACE_3598(map2) SACE_5989(map) SACE_6811
            STP: Strop_3773
            BLO: BL1732(map)
            BAD: BAD_0459(map)
            RXY: Rxyl_2133
            FNU: FN1297
            RBA: RB3478(map)
            CTR: CT851(map)
            CTA: CTA_0928(map)
            CMU: TC0240
            CPN: CPn1009(map)
            CPA: CP0844
            CPJ: CPj1009(map)
            CPT: CpB1046
            CCA: CCA00752(map)
            CAB: CAB720
            CFE: CF0262(map)
            PCU: pc0546(map) pc0780(map1)
            BGA: BG0106(map)
            BAF: BAPKO_0106(map)
            TPA: TP0842
            TDE: TDE1733(map)
            LIL: LA2457
            LIC: LIC11500(map)
            LBJ: LBJ_1458(map)
            LBL: LBL_1682(map)
            SYN: sll0555(map-3) slr0786(map-1) slr0918(map-2)
            SYW: SYNW1822(map)
            SYC: syc1660_d(map)
            SYF: Synpcc7942_2446
            SYD: Syncc9605_0645
            SYE: Syncc9902_1714
            SYG: sync_2170(map)
            SYR: SynRCC307_1662(map)
            SYX: SynWH7803_1832(map)
            CYA: CYA_0844(map-1) CYA_1158(map-2)
            CYB: CYB_2149(map-1) CYB_2617(map-2)
            TEL: tll0424
            GVI: gll2411 glr0412
            ANA: all1019 alr4150
            AVA: Ava_0754 Ava_3676
            PMA: Pro0475(map)
            PMM: PMM0477(map)
            PMT: PMT1305(map)
            PMN: PMN2A_1809
            PMI: PMT9312_0477
            PMB: A9601_05321(map)
            PMC: P9515_05401(map)
            PMF: P9303_06841(map)
            PMG: P9301_05021(map)
            PMH: P9215_05581
            PME: NATL1_05331(map)
            TER: Tery_0402 Tery_4490
            BTH: BT_0638 BT_2706
            BFR: BF2551 BF4160
            BFS: BF2576 BF3982(map)
            PGI: PG1917(map)
            SRU: SRU_1055(map)
            CHU: CHU_2358(map) CHU_3141(map)
            GFO: GFO_0411(map)
            FJO: Fjoh_0158 Fjoh_1762
            FPS: FP0419(map)
            CTE: CT2168(map)
            CCH: Cag_1830
            PLT: Plut_0202
            DET: DET0496(map)
            DEH: cbdb_A460(map)
            DEB: DehaBAV1_0473
            DRA: DR_1311
            DGE: Dgeo_1284 Dgeo_1914
            TTH: TTC1306
            TTJ: TTHA1670
            AAE: aq_076(map)
            TMA: TM1478
            TPT: Tpet_1314
            TME: Tmel_0975
            FNO: Fnod_1116
            MMP: MMP1444
            MMQ: MmarC5_0134
            MMZ: MmarC7_0689
            MAE: Maeo_0870
            MVN: Mevan_0755
            MAC: MA0212(map)
            MBA: Mbar_A1316
            MMA: MM_1499
            MBU: Mbur_1620
            MTP: Mthe_0656
            MHU: Mhun_2339
            MEM: Memar_2090
            MBN: Mboo_0487
            MST: Msp_1496(map)
            MSI: Msm_1120
            MKA: MK0613(map)
            HAL: VNG1866G(map)
            HMA: rrnAC3421(map)
            HWA: HQ3208A(map)
            NPH: NP3190A(map)
            TAC: Ta1439
            TVO: TVN0103
            PTO: PTO1091
            PHO: PH0628
            PAB: PAB1434(map)
            PFU: PF0541
            TKO: TK1183
            RCI: RCIX2452(map-1) RRC16(map-2)
            APE: APE_1114.1
            SMR: Smar_0892
            IHO: Igni_0295
            HBU: Hbut_0885
            SSO: SSO0098
            STO: ST1419
            SAI: Saci_1513
            MSE: Msed_2126
            PAI: PAE2116
            PIS: Pisl_0959
            PCL: Pcal_1051
            PAS: Pars_1013
            TPE: Tpen_0680
            NEQ: NEQ399
STRUCTURES  PDB: 1B59  1B6A  1BN5  1BOA  1C21  1C22  1C23  1C24  1C27  1KQ0  
                 1KQ9  1MAT  1O0X  1QXW  1QXY  1QXZ  1QZY  1R58  1R5G  1R5H  
                 1WKM  1XGM  1XGN  1XGO  1XNZ  1Y1N  1YJ3  1YVM  1YW7  1YW8  
                 1YW9  2ADU  2B3H  2B3K  2B3L  2BB7  2DFI  2EVC  2EVM  2EVO  
                 2G6P  2GA2  2GG0  2GG2  2GG3  2GG5  2GG7  2GG8  2GG9  2GGB  
                 2GGC  2GTX  2GU4  2GU5  2GU6  2GU7  2GZ5  2MAT  2NQ6  2NQ7  
                 2NW5  2OAZ  3MAT  4MAT  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.18
            ExPASy - ENZYME nomenclature database: 3.4.11.18
            ExplorEnz - The Enzyme Database: 3.4.11.18
            ERGO genome analysis and discovery system: 3.4.11.18
            BRENDA, the Enzyme Database: 3.4.11.18
            CAS: 61229-81-0
///
ENTRY       EC 3.4.11.19                Enzyme
NAME        D-stereospecific aminopeptidase;
            D-aminopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of an N-terminal D-amino acid from a peptide, Xaa!Yaa-, in
            which Xaa is preferably D-Ala, D-Ser or D-Thr. D-Amino acid amides
            and methyl esters also are hydrolysed, as is glycine amide
COMMENT     Known from the bacterium Ochrobactrum anthropi. In peptidase family
            S12 (D-Ala-D-Ala carboxypeptidase family) [2]
REFERENCE   1  [PMID:2760064]
  AUTHORS   Asano Y, Nakazawa A, Kato Y, Kondo K.
  TITLE     Properties of a novel D-stereospecific aminopeptidase from
            Ochrobactrum anthropi.
  JOURNAL   J. Biol. Chem. 264 (1989) 14233-9.
  ORGANISM  Ochrobactrum anthropi
REFERENCE   2  [PMID:1540587]
  AUTHORS   Asano Y, Kato Y, Yamada A, Kondo K.
  TITLE     Structural similarity of D-aminopeptidase to carboxypeptidase DD and
            beta-lactamases.
  JOURNAL   Biochemistry. 31 (1992) 2316-28.
  ORGANISM  Ochrobactrum anthropi
ORTHOLOGY   KO: K01266  D-aminopeptidase
GENES       AFM: AFUA_3G03710
            AOR: AO090138000075
            PAE: PA1486
            PAU: PA14_45210
            PPU: PP_3844
            PFO: Pfl_3533
            PEN: PSEEN2881
            CSA: Csal_1047
            RSO: RSc1383(RS04666)
            REU: Reut_A1923(dmpA)
            REH: H16_A2097(dmpA)
            RME: Rmet_1411
            BMA: BMAA0592
            BXE: Bxe_A0839
            BUR: Bcep18194_B1864(dmpA)
            BCN: Bcen_4200
            BCH: Bcen2424_4166
            BPS: BPSS1303(dmpA)
            BPM: BURPS1710b_A0321(dmpA)
            BPL: BURPS1106A_A1764
            BTE: BTH_II1116 BTH_II1650
            BPE: BP2393
            BPA: BPP3258
            BBR: BB3709
            RFR: Rfer_3106
            POL: Bpro_0136
            ADE: Adeh_2448
            MXA: MXAN_4096(dmpA)
            MLO: mlr2477
            SME: SMa0095
            ATU: Atu2510
            ATC: AGR_C_4562
            RLE: RL0230
            BME: BMEII0741
            BMF: BAB2_0708
            BMS: BRA0531
            BMB: BruAb2_0693
            BOV: BOV_A0889
            RPB: RPB_3687(dmpA)
            RPD: RPD_1773
            RPE: RPE_1644
            SIL: SPO3135
            SIT: TM1040_2667
            JAN: Jann_0772
            RDE: RD1_0100
            ABA: Acid345_0995
            OIH: OB0850
            GKA: GK0323
            LBU: LBUL_0553
            DSY: DSY1931
            TTE: TTE1085(dmpA)
            MSM: MSMEG_1507 MSMEG_2092
            MMC: Mmcs_5206
            SRU: SRU_1933
            PHO: PH0078
            PAB: PAB0045
            PFU: PF1924
            TKO: TK0160
STRUCTURES  PDB: 1EI5  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.19
            ExPASy - ENZYME nomenclature database: 3.4.11.19
            ExplorEnz - The Enzyme Database: 3.4.11.19
            ERGO genome analysis and discovery system: 3.4.11.19
            BRENDA, the Enzyme Database: 3.4.11.19
            CAS: 57534-78-8
///
ENTRY       EC 3.4.11.20                Enzyme
NAME        aminopeptidase Ey
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Differs from other aminopeptidases in broad specificity for amino
            acids in the P1 position and the ability to hydrolyse peptides of
            four or five residues that contain Pro in the P1' position
COMMENT     A zinc glycoprotein in peptidase family M1 (membrane alanyl
            aminopeptidase family), composed of two 150 kDa subunits. From the
            plasma fraction of hen egg yolk
REFERENCE   1
  AUTHORS   Ichishima, E., Yamagata, Y., Chiba, H., Sawaguchi, K. and Tanaka, T.
  TITLE     Soluble and bound forms of aminopeptidase in hens egg-yolk.
  JOURNAL   Agric. Biol. Chem. 53 (1989) 1867-1872.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:7684960]
  AUTHORS   Tanaka T, Ichishima E.
  TITLE     Substrate specificity of aminopeptidase Ey from hen's (Gallus
            domesticus) egg yolk.
  JOURNAL   Comp. Biochem. Physiol. B. 105 (1993) 105-10.
  ORGANISM  chicken [GN:gga]
REFERENCE   3  [PMID:8288037]
  AUTHORS   Tanaka T, Ichishima E.
  TITLE     Molecular properties of aminopeptidase Ey as a zinc-metalloenzyme.
  JOURNAL   Int. J. Biochem. 25 (1993) 1681-8.
  ORGANISM  chicken [GN:gga]
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.20
            ExPASy - ENZYME nomenclature database: 3.4.11.20
            ExplorEnz - The Enzyme Database: 3.4.11.20
            ERGO genome analysis and discovery system: 3.4.11.20
            BRENDA, the Enzyme Database: 3.4.11.20
            CAS: 9031-94-1
///
ENTRY       EC 3.4.11.21                Enzyme
NAME        aspartyl aminopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of an N-terminal aspartate or glutamate from a peptide, with
            a preference for aspartate
COMMENT     Aminoacyl-arylamides are poor substrates. This is an abundant
            cytosolic enzyme in mammalian cells, in peptidase family M18 of
            aminopeptidase I
REFERENCE   1  [PMID:6854330]
  AUTHORS   Kelly JA, Neidle EL, Neidle A.
  TITLE     An aminopeptidase from mouse brain cytosol that cleaves N-terminal
            acidic amino acid residues.
  JOURNAL   J. Neurochem. 40 (1983) 1727-34.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:9632644]
  AUTHORS   Wilk S, Wilk E, Magnusson RP.
  TITLE     Purification, characterization, and cloning of a cytosolic aspartyl
            aminopeptidase.
  JOURNAL   J. Biol. Chem. 273 (1998) 15961-70.
  ORGANISM  rabbit
ORTHOLOGY   KO: K01267  aspartyl aminopeptidase
GENES       HSA: 23549(DNPEP)
            PTR: 459964(DNPEP)
            MMU: 13437(Dnpep)
            RNO: 301529(Dnpep)
            CFA: 478922(DNPEP)
            BTA: 506882(DNPEP)
            GGA: 424200(RCJMB04_20m7)
            XLA: 443951(MGC80319) 495491(LOC495491)
            XTR: 548780(dnpep)
            DRE: 393122(zgc:55944) 564492(LOC564492)
            CEL: F01F1.9
            ATH: AT5G04710 AT5G60160
            OSA: 4324011 4351851
            CME: CMG039C
            SCE: YHR113W
            PIC: PICST_75911(DNP1)
            CGR: CAGL0I01298g
            SPO: SPAC4F10.02
            ANI: AN2966.2
            AFM: AFUA_3G08290
            AOR: AO090005001447
            CNE: CND02950
            PFA: PFI1570c
            CPV: cgd3_3610
            CHO: Chro.30408
            TBR: Tb927.3.3410
            EHI: 10.t00011 217.t00007
            PPF: Pput_3989
            PFL: PFL_4383
            PFO: Pfl_1690
            PMY: Pmen_1231
            SDE: Sde_2231
            PIN: Ping_1777
            MAQ: Maqu_1042
            AEH: Mlg_0439
            HCH: HCH_04958
            CSA: Csal_1520
            MMW: Mmwyl1_2884
            NET: Neut_1358
            TDN: Tmden_0913
            DVL: Dvul_0481
            CDF: CD0329
            CBO: CBO3338
            CBE: Cbei_4774
            CKL: CKL_0085(apeB)
            MSM: MSMEG_5828
            MVA: Mvan_5121
            MGI: Mflv_1628
            MMC: Mmcs_4550
            MKM: Mkms_4638
            MJL: Mjls_4933
            ART: Arth_4128
            FNU: FN0775
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.21
            ExPASy - ENZYME nomenclature database: 3.4.11.21
            ExplorEnz - The Enzyme Database: 3.4.11.21
            ERGO genome analysis and discovery system: 3.4.11.21
            BRENDA, the Enzyme Database: 3.4.11.21
///
ENTRY       EC 3.4.11.22                Enzyme
NAME        aminopeptidase I;
            aminopeptidase III;
            aminopeptidase yscI;
            leucine aminopeptidase IV;
            yeast aminopeptidase I
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of an N-terminal amino acid, preferably a neutral or
            hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor
            substrates
COMMENT     A 640-kDa, dodecameric enzyme best known as the major vacuolar
            aminopeptidase of yeast, Saccharomyces cervisiae, in which species
            it was first given the name aminopeptidase I (one), amongst others.
            Activity is stimulated by both Zn2+ and Cl- ions. Type example of
            peptidase family M18
REFERENCE   1
  AUTHORS   Johnson, M.J.
  TITLE     Isolation and properties of a pure yeast polypeptidase.
  JOURNAL   J. Biol. Chem. 137 (1941) 575-586.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:5147]
  AUTHORS   Metz G, Rohm KH.
  TITLE     Yeast aminopeptidase I. Chemical composition and catalytic
            properties.
  JOURNAL   Biochim. Biophys. Acta. 429 (1976) 933-49.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:2651436]
  AUTHORS   Chang YH, Smith JA.
  TITLE     Molecular cloning and sequencing of genomic DNA encoding
            aminopeptidase I from Saccharomyces cerevisiae.
  JOURNAL   J. Biol. Chem. 264 (1989) 6979-83.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4  [PMID:8601598]
  AUTHORS   Oda MN, Scott SV, Hefner-Gravink A, Caffarelli AD, Klionsky DJ.
  TITLE     Identification of a cytoplasm to vacuole targeting determinant in
            aminopeptidase I.
  JOURNAL   J. Cell. Biol. 132 (1996) 999-1010.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K01268  aminopeptidase I
GENES       SCE: YKL103C(LAP4)
            AGO: AGOS_ABL035C
            CGR: CAGL0K08536g
            TET: TTHERM_00011120 TTHERM_00355360 TTHERM_00355370
            MXA: MXAN_2382
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.22
            ExPASy - ENZYME nomenclature database: 3.4.11.22
            ExplorEnz - The Enzyme Database: 3.4.11.22
            ERGO genome analysis and discovery system: 3.4.11.22
            BRENDA, the Enzyme Database: 3.4.11.22
            CAS: 9031-94-1
///
ENTRY       EC 3.4.11.23                Enzyme
NAME        PepB aminopeptidase;
            Salmonella enterica serovar Typhimurium peptidase B
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aminopeptidases
REACTION    Release of an N-terminal amino acid, Xaa, from a peptide or
            arylamide. Xaa is preferably Glu or Asp but may be other amino
            acids, including Leu, Met, His, Cys and Gln
COMMENT     A 270-kDa protein composed of six 46.3-kDa subunits. The pH optimum
            is in the alkaline range and activity is stimulated by KCl. In
            peptidase family M17.
REFERENCE   1  [PMID:10852868]
  AUTHORS   Mathew Z, Knox TM, Miller CG.
  TITLE     Salmonella enterica serovar typhimurium peptidase B is a leucyl
            aminopeptidase with specificity for acidic amino acids.
  JOURNAL   J. Bacteriol. 182 (2000) 3383-93.
  ORGANISM  Salmonella enterica
ORTHOLOGY   KO: K07751  PepB aminopeptidase
GENES       ECO: b2523(pepB)
            ECJ: JW2507(pepB)
            ECE: Z3790(pepB)
            ECS: ECs3389
            ECC: c3048(pepB)
            ECI: UTI89_C2845(pepB)
            ECP: ECP_2528
            ECV: APECO1_4001(pepB)
            ECW: EcE24377A_2807(pepB)
            ECX: EcHS_A2674
            STY: STY2782(yfhI)
            STT: t0320(yfhI)
            SPT: SPA0330(yfhI)
            SEC: SC2531(pepB)
            STM: STM2536(pepB)
            YPE: YPO2889(pepB)
            YPK: y1342(pepB)
            YPM: YP_2566(pepB)
            YPA: YPA_2330
            YPN: YPN_1248
            YPP: YPDSF_2234
            YPS: YPTB2852(pepB)
            YPI: YpsIP31758_1175(pepB)
            SFL: SF2570(pepB)
            SFX: S2742(pepB)
            SFV: SFV_2571(pepB)
            SSN: SSON_2605(pepB)
            SBO: SBO_2547(pepB)
            SDY: SDY_2719(pepB)
            ECA: ECA3230(pepB)
            PLU: plu3276(pepB)
            SGL: SG1768
            ENT: Ent638_3020
            SPE: Spro_3620
            HIT: NTHI1038(pepB)
            HIP: CGSHiEE_07720
            HIQ: CGSHiGG_07915
            HDU: HD1169(pepB)
            HSO: HS_0388(pepB)
            PMU: PM1029(pepB)
            MSU: MS0667(pepB)
            APL: APL_0388(pepB)
            ASU: Asuc_0833
            VCH: VC0755
            VVU: VV1_0431
            VVY: VV0762
            VPA: VP0603
            VFI: VF0624
            PPR: PBPRA0757 PBPRA0758(pepB)
            SON: SO_0876(pepB)
            SDN: Sden_3168
            SFR: Sfri_3274
            SAZ: Sama_0782
            SBL: Sbal_3488
            SBM: Shew185_0851
            SLO: Shew_3127
            SPC: Sputcn32_3126
            SSE: Ssed_3897
            SPL: Spea_0700
            SHE: Shewmr4_0732
            SHM: Shewmr7_3290
            SHN: Shewana3_3402
            SHW: Sputw3181_0817
            ILO: IL2248(pepB)
            PHA: PSHAa0608(pepB)
            PAT: Patl_3939
            PIN: Ping_1331
            AHA: AHA_1753(pepB) AHA_1754
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.11.23
            ExPASy - ENZYME nomenclature database: 3.4.11.23
            ExplorEnz - The Enzyme Database: 3.4.11.23
            ERGO genome analysis and discovery system: 3.4.11.23
            BRENDA, the Enzyme Database: 3.4.11.23
            CAS: 928346-44-5
///
ENTRY       EC 3.4.12.1       Obsolete  Enzyme
NAME        Transferred to 3.4.16.5 and 3.4.16.6
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidylamino-acid hydrolases or acylamino-acid hydrolases (deleted
            sub-subclass)
COMMENT     Transferred entry: now EC 3.4.16.5, carboxypeptidase C and EC
            3.4.16.6, carboxypeptidase D (EC 3.4.12.1 created 1972, deleted
            1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.12.1
            ExPASy - ENZYME nomenclature database: 3.4.12.1
            ExplorEnz - The Enzyme Database: 3.4.12.1
            ERGO genome analysis and discovery system: 3.4.12.1
            BRENDA, the Enzyme Database: 3.4.12.1
///
ENTRY       EC 3.4.12.2       Obsolete  Enzyme
NAME        Transferred to 3.4.17.1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidylamino-acid hydrolases or acylamino-acid hydrolases (deleted
            sub-subclass)
COMMENT     Transferred entry: now EC 3.4.17.1, carboxypeptidase A (EC 3.4.12.2
            created 1972, deleted 1978)
STRUCTURES  PDB: 1PCA  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.12.2
            ExPASy - ENZYME nomenclature database: 3.4.12.2
            ExplorEnz - The Enzyme Database: 3.4.12.2
            ERGO genome analysis and discovery system: 3.4.12.2
            BRENDA, the Enzyme Database: 3.4.12.2
///
ENTRY       EC 3.4.12.3       Obsolete  Enzyme
NAME        Transferred to 3.4.17.2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidylamino-acid hydrolases or acylamino-acid hydrolases (deleted
            sub-subclass)
COMMENT     Transferred entry: now EC 3.4.17.2, carboxypeptidase B (EC 3.4.12.3
            created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.12.3
            ExPASy - ENZYME nomenclature database: 3.4.12.3
            ExplorEnz - The Enzyme Database: 3.4.12.3
            ERGO genome analysis and discovery system: 3.4.12.3
            BRENDA, the Enzyme Database: 3.4.12.3
///
ENTRY       EC 3.4.12.4       Obsolete  Enzyme
NAME        Transferred to 3.4.16.2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidylamino-acid hydrolases or acylamino-acid hydrolases (deleted
            sub-subclass)
COMMENT     Transferred entry: now EC 3.4.16.2, lysosomal Pro-Xaa
            carboxypeptidase (EC 3.4.12.4 created 1972, modified 1976, deleted
            1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.12.4
            ExPASy - ENZYME nomenclature database: 3.4.12.4
            ExplorEnz - The Enzyme Database: 3.4.12.4
            ERGO genome analysis and discovery system: 3.4.12.4
            BRENDA, the Enzyme Database: 3.4.12.4
///
ENTRY       EC 3.4.12.5       Obsolete  Enzyme
NAME        Transferred to 3.5.1.28
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidylamino-acid hydrolases or acylamino-acid hydrolases (deleted
            sub-subclass)
COMMENT     Transferred entry: now EC 3.5.1.28, N-acetylmuramoyl-L-alanine
            amidase (EC 3.4.12.5 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.12.5
            ExPASy - ENZYME nomenclature database: 3.4.12.5
            ExplorEnz - The Enzyme Database: 3.4.12.5
            ERGO genome analysis and discovery system: 3.4.12.5
            BRENDA, the Enzyme Database: 3.4.12.5
///
ENTRY       EC 3.4.12.6       Obsolete  Enzyme
NAME        Transferred to 3.4.17.8
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidylamino-acid hydrolases or acylamino-acid hydrolases (deleted
            sub-subclass)
COMMENT     Transferred entry: now EC 3.4.17.8, muramoyl-pentapeptidase
            carboxypeptidase (EC 3.4.12.6 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.12.6
            ExPASy - ENZYME nomenclature database: 3.4.12.6
            ExplorEnz - The Enzyme Database: 3.4.12.6
            ERGO genome analysis and discovery system: 3.4.12.6
            BRENDA, the Enzyme Database: 3.4.12.6
///
ENTRY       EC 3.4.12.7       Obsolete  Enzyme
NAME        Transferred to 3.4.17.3
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidylamino-acid hydrolases or acylamino-acid hydrolases (deleted
            sub-subclass)
COMMENT     Transferred entry: now EC 3.4.17.3, lysine carboxypeptidase (EC
            3.4.12.7 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.12.7
            ExPASy - ENZYME nomenclature database: 3.4.12.7
            ExplorEnz - The Enzyme Database: 3.4.12.7
            ERGO genome analysis and discovery system: 3.4.12.7
            BRENDA, the Enzyme Database: 3.4.12.7
///
ENTRY       EC 3.4.12.8       Obsolete  Enzyme
NAME        Transferred to 3.4.17.4
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidylamino-acid hydrolases or acylamino-acid hydrolases (deleted
            sub-subclass)
COMMENT     Transferred entry: now EC 3.4.17.4, Gly-Xaa carboxypeptidase (EC
            3.4.12.8 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.12.8
            ExPASy - ENZYME nomenclature database: 3.4.12.8
            ExplorEnz - The Enzyme Database: 3.4.12.8
            ERGO genome analysis and discovery system: 3.4.12.8
            BRENDA, the Enzyme Database: 3.4.12.8
///
ENTRY       EC 3.4.12.9       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidylamino-acid hydrolases or acylamino-acid hydrolases (deleted
            sub-subclass)
COMMENT     Deleted entry: aspartate carboxypeptidase (EC 3.4.12.9 created 1972,
            deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.12.9
            ExPASy - ENZYME nomenclature database: 3.4.12.9
            ExplorEnz - The Enzyme Database: 3.4.12.9
            ERGO genome analysis and discovery system: 3.4.12.9
            BRENDA, the Enzyme Database: 3.4.12.9
///
ENTRY       EC 3.4.12.10      Obsolete  Enzyme
NAME        Transferred to 3.4.19.9
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidylamino-acid hydrolases or acylamino-acid hydrolases (deleted
            sub-subclass)
COMMENT     Transferred entry: now EC 3.4.19.9, gamma-glutamyl hydrolase (EC
            3.4.12.10 created 1972, modified 1976, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.12.10
            ExPASy - ENZYME nomenclature database: 3.4.12.10
            ExplorEnz - The Enzyme Database: 3.4.12.10
            ERGO genome analysis and discovery system: 3.4.12.10
            BRENDA, the Enzyme Database: 3.4.12.10
///
ENTRY       EC 3.4.12.11      Obsolete  Enzyme
NAME        Transferred to 3.4.17.6
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidylamino-acid hydrolases or acylamino-acid hydrolases (deleted
            sub-subclass)
COMMENT     Transferred entry: now EC 3.4.17.6, alanine carboxypeptidase (EC
            3.4.12.11 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.12.11
            ExPASy - ENZYME nomenclature database: 3.4.12.11
            ExplorEnz - The Enzyme Database: 3.4.12.11
            ERGO genome analysis and discovery system: 3.4.12.11
            BRENDA, the Enzyme Database: 3.4.12.11
///
ENTRY       EC 3.4.12.12      Obsolete  Enzyme
NAME        Transferred to 3.4.16.5 and 3.4.16.6
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidylamino-acid hydrolases or acylamino-acid hydrolases (deleted
            sub-subclass)
COMMENT     Transferred entry: now EC 3.4.16.5, carboxypeptidase C and EC
            3.4.16.6, carboxypeptidase D (EC 3.4.12.12 created 1972, deleted
            1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.12.12
            ExPASy - ENZYME nomenclature database: 3.4.12.12
            ExplorEnz - The Enzyme Database: 3.4.12.12
            ERGO genome analysis and discovery system: 3.4.12.12
            BRENDA, the Enzyme Database: 3.4.12.12
///
ENTRY       EC 3.4.12.13      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidylamino-acid hydrolases or acylamino-acid hydrolases (deleted
            sub-subclass)
COMMENT     Deleted entry: gamma-glutamylglutamate carboxypeptidase (EC
            3.4.12.13 created 1975, modified 1976, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.12.13
            ExPASy - ENZYME nomenclature database: 3.4.12.13
            ExplorEnz - The Enzyme Database: 3.4.12.13
            ERGO genome analysis and discovery system: 3.4.12.13
            BRENDA, the Enzyme Database: 3.4.12.13
///
ENTRY       EC 3.4.13.1       Obsolete  Enzyme
NAME        Transferred to 3.4.13.18
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
COMMENT     Transferred entry: now EC 3.4.13.18 cytosol nonspecific dipeptidase
            (EC 3.4.13.1 created 1972, deleted 1978 [transferred to EC
            3.4.13.11, deleted 1992])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.1
            ExPASy - ENZYME nomenclature database: 3.4.13.1
            ExplorEnz - The Enzyme Database: 3.4.13.1
            ERGO genome analysis and discovery system: 3.4.13.1
            BRENDA, the Enzyme Database: 3.4.13.1
///
ENTRY       EC 3.4.13.2       Obsolete  Enzyme
NAME        Transferred to 3.4.13.18
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
COMMENT     Transferred entry: now EC 3.4.13.18 cytosol nonspecific dipeptidase
            (EC 3.4.13.2 created 1972, deleted 1978 [transferred to EC
            3.4.13.11, deleted 1992])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.2
            ExPASy - ENZYME nomenclature database: 3.4.13.2
            ExplorEnz - The Enzyme Database: 3.4.13.2
            ERGO genome analysis and discovery system: 3.4.13.2
            BRENDA, the Enzyme Database: 3.4.13.2
///
ENTRY       EC 3.4.13.3                 Enzyme
NAME        Xaa-His dipeptidase;
            aminoacylhistidine dipeptidase;
            carnosinase;
            homocarnosinase;
            dipeptidase M;
            X-His dipeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
REACTION    Hydrolysis of Xaa!His dipeptides
ALL_REAC    (other) R01166 R01992
COFACTOR    Manganese [CPD:C00034];
            Zinc [CPD:C00038]
INHIBITOR   EDTA [CPD:C00284]
EFFECTOR    Thiol [CPD:C00145]
COMMENT     A mammalian cytosolic enzyme that also acts on anserine and
            homocarnosine (but not on homoanserine), and to a lesser extent on
            some other aminoacyl-L-histidine dipeptides. Activated by thiols;
            inhibited by metal-chelating agents. This enzyme in peptidase family
            M25 may be identical with EC 3.4.13.18, cytosol nonspecific
            dipeptidase.
REFERENCE   1
  AUTHORS   Hanson, H.T. and Smith, E.L.
  TITLE     Carnosinase: an enzyme of swine kidney.
  JOURNAL   J. Biol. Chem. 179 (1949) 789-801.
  ORGANISM  pig [GN:ssc]
REFERENCE   2
  AUTHORS   Rosenberg, A.
  TITLE     The activation of carnosinase by divalent ions.
  JOURNAL   Biochim. Biophys. Acta 45 (1960) 297-316.
REFERENCE   3  [PMID:21630]
  AUTHORS   Lenney JF, Kan SC, Siu K, Sugiyama GH.
  TITLE     Homocarnosinase: a hog kidney dipeptidase with a broader specificity
            than carnosinase.
  JOURNAL   Arch. Biochem. Biophys. 184 (1977) 257-66.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:2378680]
  AUTHORS   Lenney JF.
  TITLE     Separation and characterization of two carnosine-splitting cytosolic
            dipeptidases from hog kidney (carnosinase and non-specific
            dipeptidase).
  JOURNAL   Biol. Chem. Hoppe. Seyler. 371 (1990) 433-40.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00252  Alanine and aspartate metabolism
            PATH: map00340  Histidine metabolism
            PATH: map00410  beta-Alanine metabolism
ORTHOLOGY   KO: K01270  aminoacylhistidine dipeptidase
GENES       EHI: 11.t00017 129.t00006 26.t00016
            ECO: b0237(pepD)
            ECJ: JW0227(pepD)
            ECE: Z0298(pepD)
            ECS: ECs0264
            ECC: c0383(pepD)
            ECI: UTI89_C0277(pepD)
            ECP: ECP_0266
            ECV: APECO1_1732(pepD)
            ECW: EcE24377A_0269(pepD)
            ECX: EcHS_A0264
            STY: STY0361(pepD)
            STT: t2534(pepD)
            SPT: SPA2439(pepD)
            SEC: SC0317(pepD)
            STM: STM0316(pepD)
            YPE: YPO3230(pepD)
            YPK: y0960(pepD)
            YPM: YP_0703(pepD1)
            YPA: YPA_2720
            YPN: YPN_0865
            YPP: YPDSF_2857
            YPS: YPTB0897(pepD)
            YPI: YpsIP31758_3156(pepD)
            SFL: SF0285(pepD)
            SFX: S0306(pepD)
            SFV: SFV_0293(pepD)
            SSN: SSON_0279(pepD)
            SBO: SBO_0243(pepD)
            SDY: SDY_0480(pepD)
            ECA: ECA3467(pepD)
            PLU: plu1240(pepD)
            SGL: SG0597
            ENT: Ent638_0763
            SPE: Spro_0963
            HIT: NTHI0797(pepD)
            HDU: HD1832(pepD)
            HSO: HS_0004(pepD)
            PMU: PM1368(pepD)
            MSU: MS2118(pepD)
            APL: APL_0254(pepD)
            ASU: Asuc_0178
            VCH: VC2279
            VCO: VC0395_A1869(pepD)
            VVU: VV1_0333
            VVY: VV0852
            VPA: VP0671
            VFI: VF0736
            PPR: PBPRA0833
            PRW: PsycPRwf_1035
            ACI: ACIAD2220(pepD)
            SON: SO_1115(pepD)
            SDN: Sden_1011
            SFR: Sfri_0962
            SAZ: Sama_1565 Sama_2519
            SBL: Sbal_0940
            SBM: Shew185_2660 Shew185_3422
            SLO: Shew_2160 Shew_2852
            SPC: Sputcn32_0954
            SSE: Ssed_2691 Ssed_3421
            SPL: Spea_3091
            SHE: Shewmr4_0948 Shewmr4_2301
            SHM: Shewmr7_0986 Shewmr7_2371
            SHN: Shewana3_0950 Shewana3_1692 Shewana3_2491
            SHW: Sputw3181_3222
            CPS: CPS_0180(pepD)
            PIN: Ping_0894
            HCH: HCH_00218(pepD)
            CSA: Csal_2957
            MMW: Mmwyl1_2361
            AHA: AHA_3426(pepD)
            CVI: CV_2694(pepD)
            RSO: RSc1302(pepV)
            AZO: azo1259(pepD)
            DAR: Daro_1720
            CJR: CJE1062(pepD)
            CJJ: CJJ81176_0999(pepD)
            CJU: C8J_0919(pepD)
            CJD: JJD26997_0809(pepD)
            ABU: Abu_1305(pepD)
            NIS: NIS_0557(pepD)
            SUN: SUN_1808(pepD)
            ADE: Adeh_2079
            AFW: Anae109_1744
            ABA: Acid345_1504
            BAN: BA2498(pepD)
            BAR: GBAA2498(pepD)
            BAA: BA_2989
            BAT: BAS2319
            BCE: BC2439
            BCA: BCE_2527(pepD)
            BCZ: BCZK2240(pepD) BCZK4454
            BCY: Bcer98_1800
            BTK: BT9727_2284(pepD)
            BTL: BALH_4279
            GKA: GK2831
            SAJ: SaurJH9_1806
            SAH: SaurJH1_1841
            SPZ: M5005_Spy_0793 M5005_Spy_1271
            SPH: MGAS10270_Spy0906 MGAS10270_Spy1286
            SPI: MGAS10750_Spy0941 MGAS10750_Spy1378
            SPJ: MGAS2096_Spy0864 MGAS2096_Spy1290
            SPK: MGAS9429_Spy0907 MGAS9429_Spy1265
            SPF: SpyM50976(pepV)
            SPA: M6_Spy0810 M6_Spy1292
            SPB: M28_Spy0767 M28_Spy1209
            LSA: LSA0424(pepV)
            LSL: LSL_0447
            LDB: Ldb1746(pepV)
            LBR: LVIS_2032
            LCA: LSEI_0813
            LGA: LGAS_0439
            CPE: CPE2148(pepD) CPE2251(pepD)
            CPF: CPF_2403(pepD) CPF_2512(pepD)
            CPR: CPR_2115(pepD) CPR_2216(pepD)
            CTC: CTC01945 CTC02317
            CNO: NT01CX_0660
            CTH: Cthe_3149
            CDF: CD0708(pepD)
            CBO: CBO2867(pepD)
            CBA: CLB_1412(pepD-1) CLB_2172(pepD-2) CLB_2833(pepD-3)
            CBH: CLC_1423(pepD-1) CLC_2155(pepD-2) CLC_2766(pepD-3)
            CBF: CLI_1484(pepD-1) CLI_2281(pepD-2) CLI_2923(pepD-3)
            CBE: Cbei_0486
            AYW: AYWB_431(pepD)
            FNU: FN1277 FN1408 FN1804
            BGA: BG0621(pepD)
            BAF: BAPKO_0641(pepD)
            TDE: TDE2228
            BTH: BT_1615 BT_4045
            BFR: BF0780 BF3239
            BFS: BF0708 BF3079(pepD)
            PGI: PG0137(pepD-1) PG0537(pepD-2)
            GFO: GFO_0785(pepD)
            FJO: Fjoh_2400
            FPS: FP1929(pepD)
            CTE: CT1058(pepD)
            CPH: Cpha266_1680
            PLT: Plut_0525
            MAC: MA2653
            MBA: Mbar_A3039
            MMA: MM_2749
STRUCTURES  PDB: 1LFW  2QYV  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.3
            ExPASy - ENZYME nomenclature database: 3.4.13.3
            ExplorEnz - The Enzyme Database: 3.4.13.3
            ERGO genome analysis and discovery system: 3.4.13.3
            BRENDA, the Enzyme Database: 3.4.13.3
            CAS: 9027-21-8
///
ENTRY       EC 3.4.13.4                 Enzyme
NAME        Xaa-Arg dipeptidase;
            aminoacyl-lysine dipeptidase;
            N2-(4-amino-butyryl)-L-lysine hydrolase;
            X-Arg dipeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
REACTION    Preferential hydrolysis of Xaa!Arg, Xaa!Lys or Xaa!ornithine
            dipeptides
ALL_REAC    (other) R00911 R03935
COMMENT     Widely distributed in mammals
REFERENCE   1  [PMID:5436646]
  AUTHORS   Kumon A, Matsuoka Y, Kakimoto Y, Nakajima T, Sano I.
  TITLE     A peptidase that hydrolyzes Na-(gamma-aminobutyryl)lysine.
  JOURNAL   Biochim. Biophys. Acta. 200 (1970) 466-74.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00410  beta-Alanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.4
            ExPASy - ENZYME nomenclature database: 3.4.13.4
            ExplorEnz - The Enzyme Database: 3.4.13.4
            ERGO genome analysis and discovery system: 3.4.13.4
            BRENDA, the Enzyme Database: 3.4.13.4
            CAS: 37288-72-5
///
ENTRY       EC 3.4.13.5                 Enzyme
NAME        Xaa-methyl-His dipeptidase;
            anserinase;
            aminoacyl-methylhistidine dipeptidase;
            acetylhistidine deacetylase;
            N-acetylhistidine deacetylase;
            alpha-N-acetyl-L-histidine aminohydrolase;
            X-methyl-His dipeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
REACTION    Hydrolysis of anserine (beta-alanyl!Npi-methyl-L-histidine),
            carnosine, homocarnosine, glycyl!leucine and other dipeptides with
            broad specificity
ALL_REAC    (other) R03288
REFERENCE   1  [PMID:14363188]
  AUTHORS   JONES NR.
  TITLE     The free amino acids of fish; 1-methylhistidine and beta-alanine
            liberation by skeletal muscle anserinase of codling (Gadus
            callarias).
  JOURNAL   Biochem. J. 60 (1955) 81-7.
  ORGANISM  Gadus callarias
REFERENCE   2  [PMID:6067033]
  AUTHORS   Baslow MH, Lenney JF.
  TITLE     Alpha-N-acetyl-L-histidine amidohydrolase activity from the brain of
            the skipjack tuna Katsuwonus pelamis.
  JOURNAL   Can. J. Biochem. 45 (1967) 337-40.
  ORGANISM  Katsuwonus pelamis
REFERENCE   3  [PMID:318374]
  AUTHORS   Lenney JF, Baslow MH, Sugiyama GH.
  TITLE     Similarity of tuna N-acetylhistidine deacetylase and cod fish
            anserinase.
  JOURNAL   Comp. Biochem. Physiol. B. 61 (1978) 253-8.
  ORGANISM  Katsuwonus pelamis
PATHWAY     PATH: map00340  Histidine metabolism
            PATH: map00410  beta-Alanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.5
            ExPASy - ENZYME nomenclature database: 3.4.13.5
            ExplorEnz - The Enzyme Database: 3.4.13.5
            ERGO genome analysis and discovery system: 3.4.13.5
            BRENDA, the Enzyme Database: 3.4.13.5
            CAS: 9027-38-7
///
ENTRY       EC 3.4.13.6       Obsolete  Enzyme
NAME        Transferred to 3.4.11.2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
COMMENT     Transferred entry: now EC 3.4.11.2 membrane alanyl aminopeptidase
            (EC 3.4.13.6 created 1961 as EC 3.4.3.5, transferred 1972 to EC
            3.4.13.6)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.6
            ExPASy - ENZYME nomenclature database: 3.4.13.6
            ExplorEnz - The Enzyme Database: 3.4.13.6
            ERGO genome analysis and discovery system: 3.4.13.6
            BRENDA, the Enzyme Database: 3.4.13.6
///
ENTRY       EC 3.4.13.7                 Enzyme
NAME        Glu-Glu dipeptidase;
            alpha-glutamyl-glutamate dipeptidase;
            glutamylglutamic arylamidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
REACTION    Hydrolysis of the Glu!Glu dipeptide
COMMENT     It is unclear whether the specificity of this enzyme extends to
            other alpha-glutamyl dipeptides
REFERENCE   1  [PMID:5726892]
  AUTHORS   Pratt AG, Crawford EJ, Friedkin M.
  TITLE     The hydrolysis of mono-, di-, and triglutamate derivatives of folic
            acid with bacterial enzymes.
  JOURNAL   J. Biol. Chem. 243 (1968) 6367-72.
  ORGANISM  Flavobacterium polyglutamicum
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.7
            ExPASy - ENZYME nomenclature database: 3.4.13.7
            ExplorEnz - The Enzyme Database: 3.4.13.7
            ERGO genome analysis and discovery system: 3.4.13.7
            BRENDA, the Enzyme Database: 3.4.13.7
            CAS: 37288-73-6
///
ENTRY       EC 3.4.13.8       Obsolete  Enzyme
NAME        Transferred to 3.4.13.18
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
COMMENT     Transferred entry: now EC 3.4.13.18 cytosol nonspecific dipeptidase
            (EC 3.4.13.8 created 1961 as EC 3.4.3.6, transferred 1972 to EC
            3.4.13.8)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.8
            ExPASy - ENZYME nomenclature database: 3.4.13.8
            ExplorEnz - The Enzyme Database: 3.4.13.8
            ERGO genome analysis and discovery system: 3.4.13.8
            BRENDA, the Enzyme Database: 3.4.13.8
///
ENTRY       EC 3.4.13.9                 Enzyme
NAME        Xaa-Pro dipeptidase;
            prolidase;
            imidodipeptidase;
            proline dipeptidase;
            peptidase D;
            gamma-peptidase;
            X-Pro dipeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
REACTION    Hydrolysis of Xaa!Pro dipeptides; also acts on
            aminoacyl-hydroxyproline analogs. No action on Pro-Pro
COFACTOR    Manganese [CPD:C00034]
EFFECTOR    Thiol [CPD:C00145]
COMMENT     A Mn2+-activated enzyme, in peptidase family M24 (methionyl
            aminopeptidase family); cytosolic from most animal tissues.
REFERENCE   1  [PMID:13398404]
  AUTHORS   DAVIS NC, SMITH EL.
  TITLE     Purification and some properties of prolidase of swine kidney.
  JOURNAL   J. Biol. Chem. 224 (1957) 261-75.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:4778946]
  AUTHORS   Sjostrom H, Noren O, Josefsson L.
  TITLE     Purification and specificity of pig intestinal prolidase.
  JOURNAL   Biochim. Biophys. Acta. 327 (1973) 457-70.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:4435812]
  AUTHORS   Baksi K, Radhakrishnan AN.
  TITLE     Purification and properties of prolidase (imidodipeptidase) from
            monkey small intestine.
  JOURNAL   Indian. J. Biochem. Biophys. 11 (1974) 7-11.
  ORGANISM  monkey
REFERENCE   4  [PMID:6853481]
  AUTHORS   Browne P, O'Cuinn G.
  TITLE     The purification and characterization of a proline dipeptidase from
            guinea pig brain.
  JOURNAL   J. Biol. Chem. 258 (1983) 6147-54.
  ORGANISM  guinea pig
ORTHOLOGY   KO: K01271  X-Pro dipeptidase
GENES       HSA: 5184(PEPD)
            PTR: 455933(PEPD)
            MMU: 18624(Pepd)
            RNO: 292808(Pepd)
            CFA: 476493(PEPD)
            BTA: 615158(PEPD)
            GGA: 415776(RCJMB04_10d1)
            XLA: 379515(MGC64570)
            XTR: 493456(pepd)
            DRE: 337498(pepd)
            SPU: 581659(LOC581659)
            DME: Dmel_CG5663(Dip-C)
            CEL: K12C11.1
            ATH: AT4G29490
            OSA: 4328771
            SCE: YFR006W
            AGO: AGOS_AGR008W
            PIC: PICST_62767
            CGR: CAGL0F02233g CAGL0L09185g
            ANI: AN5810.2
            AFM: AFUA_1G14920 AFUA_2G07500
            AOR: AO090005001240 AO090011000942
            CNE: CNE02200
            DDI: DDBDRAFT_0190220
            TET: TTHERM_00281000 TTHERM_00445980
            TBR: Tb09.211.4330
            TCR: 510655.120
            LMA: LmjF35.2350
            EHI: 4.t00122 60.t00014
            ECO: b3847(pepQ)
            ECJ: JW3823(pepQ)
            ECE: Z5369(pepQ)
            ECS: ECs4775
            ECC: c4794(pepQ)
            ECI: UTI89_C4432(pepQ)
            ECP: ECP_4060
            ECV: APECO1_2610(pepQ)
            ECW: EcE24377A_4366(pepQ)
            ECX: EcHS_A4070
            STY: STY3576(pepQ)
            STT: t3314(pepQ)
            SPT: SPA3824(pepQ)
            SEC: SC3881(pepQ)
            STM: STM3984(pepQ)
            YPE: YPO3765(pepQ)
            YPK: y0465(pepQ)
            YPM: YP_3283(pepQ)
            YPA: YPA_3435
            YPN: YPN_0199
            YPS: YPTB0268(pepQ)
            YPI: YpsIP31758_0284(pepQ)
            SFL: SF3923(pepQ)
            SFX: S3829(pepQ)
            SFV: SFV_3653(pepQ)
            SSN: SSON_4020(pepQ)
            SBO: SBO_3859(pepQ)
            SDY: SDY_3898(pepQ)
            ECA: ECA0209(pepQ)
            PLU: plu4401(pepQ)
            SGL: SG0118
            APL: APL_0091(pepQ)
            XFA: XF0220
            XFT: PD0177(pepQ)
            XCC: XCC2409(pepQ) XCC3257(pepQ)
            XCB: XC_0966 XC_1703
            XCV: XCV2742 XCV3520(pepQ)
            XAC: XAC2545(pepQ) XAC3403(pepQ)
            XOO: XOO1137(pepQ) XOO3135(pepQ)
            XOM: XOO_1034(XOO1034) XOO_2977(XOO2977)
            PAE: PA4498
            PAU: PA14_58375
            PPU: PP_4432
            PFL: PFL_5299(pepQ)
            SON: SO_0022(pepQ)
            SDN: Sden_0016 Sden_0888
            SFR: Sfri_0014 Sfri_3046
            SAZ: Sama_0033
            SBL: Sbal_0022
            SLO: Shew_0020
            SPC: Sputcn32_0014
            SHE: Shewmr4_0019
            SHM: Shewmr7_0017
            SHN: Shewana3_0025
            SHW: Sputw3181_0014
            ILO: IL0013(pepQ) IL0630
            CPS: CPS_0013(pepQ) CPS_1459
            PHA: PSHAa0013(pepQ) PSHAb0215
            PAT: Patl_0199 Patl_3777
            SDE: Sde_1643
            TCX: Tcr_0221
            NOC: Noc_2608
            HCH: HCH_06289 HCH_07017
            AHA: AHA_0141(pepQ)
            CVI: CV_2454(pepQ)
            REU: Reut_B4498 Reut_B5472
            REH: H16_A0506(pepQ)
            BXE: Bxe_C0063
            BUR: Bcep18194_B2694
            BCH: Bcen2424_6167
            HPA: HPAG1_1428
            CCV: CCV52592_1794
            CCO: CCC13826_0804(pepQ)
            NIS: NIS_0431
            SUN: SUN_1039
            GSU: GSU1105(pepQ-1) GSU2021(pepQ-2)
            DDE: Dde_0811 Dde_1305
            SAT: SYN_01769
            PUB: SAR11_0853 SAR11_1338(y4tM)
            MLO: mlr7141 mlr9012
            SME: SMb20434
            ATU: Atu4112 Atu4757(pepQ) Atu5477
            ATC: AGR_L_1483 AGR_L_248 AGR_pAT_704
            RET: RHE_CH03021(ypch01052) RHE_PF00180(ypf00080)
            RLE: RL3466 pRL100271 pRL120054
            BME: BMEI0485 BMEI0924
            BMF: BAB1_1547
            BMS: BR1062(pepQ) BR1531
            BMB: BruAb1_1520
            BRA: BRADO6608
            BBT: BBta_0928
            SIL: SPO1140
            SIT: TM1040_1921
            RSP: RSP_3444
            JAN: Jann_0850
            RDE: RD1_3472(pepQ) RD1_3474
            MMR: Mmar10_2407
            GOX: GOX0543(pepQ)
            GBE: GbCGDNIH1_1040
            BSU: BG13326(ykvY)
            BHA: BH1739 BH3179(pepQ)
            BAN: BA4014 BA4861(pepQ-2)
            BAR: GBAA4014 GBAA4861(pepQ-2)
            BAA: BA_4485 BA_5282
            BAT: BAS3727 BAS4508
            BCE: BC3875 BC4198 BC4614
            BCA: BCE_3921 BCE_4271(pepQ) BCE_4748(pepQ)
            BCZ: BCZK3635(pepQ) BCZK3951(pepQ) BCZK4355(pepQ)
            BTK: BT9727_3617(pepQ) BT9727_3940(pepQ) BT9727_4344(pepQ)
            BTL: BALH_3507(pepQ) BALH_3804(pepQ) BALH_4195(pepQ)
            BLI: BL03561
            BLD: BLi01594(ykvY)
            BCL: ABC0020 ABC2483 ABC2732
            OIH: OB2187 OB2829 OB2950
            GKA: GK2751
            GTN: GTNG_2676
            SAU: SA1530
            SAV: SAV1708
            SAM: MW1651
            SAR: SAR1786
            SAS: SAS1635
            SAC: SACOL1588 SACOL1756(pepQ)
            SAB: SAB1402c SAB1567
            SAA: SAUSA300_1491 SAUSA300_1654
            SAO: SAOUHSC_01626 SAOUHSC_01816
            SAJ: SaurJH9_1764
            SEP: SE1383
            SER: SERP1094 SERP1271(pepQ)
            SHA: SH1217
            SSP: SSP1059
            LMO: lmo1578
            LMF: LMOf2365_1600(pepQ)
            LIN: lin1613
            LWE: lwe1591
            LLA: L96847(pepQ)
            LLC: LACR_1813
            LLM: llmg_0774(pepQ)
            SPY: SPy_0513(pepQ)
            SPZ: M5005_Spy_0423(pepQ) M5005_Spy_1328 M5005_Spy_1549
            SPM: spyM18_0571(pepQ)
            SPG: SpyM3_0361(pepQ)
            SPS: SPs1492
            SPH: MGAS10270_Spy1444 MGAS10270_Spy1616
            SPI: MGAS10750_Spy1437 MGAS10750_Spy1608
            SPJ: MGAS2096_Spy1349 MGAS2096_Spy1574
            SPK: MGAS9429_Spy1553
            SPF: SpyM50301 SpyM51447(pepQ)
            SPA: M6_Spy0450 M6_Spy1374 M6_Spy1538
            SPB: M28_Spy0411(pepQ) M28_Spy1369 M28_Spy1536
            SPN: SP_1591
            SPR: spr1445(pepQ)
            SPD: SPD_1418(pepQ)
            SAG: SAG0706(pepQ)
            SAN: gbs0679
            SAK: SAK_0832(pepQ)
            SMU: SMU.1592(pepQ)
            STC: str0629(pepQ)
            STL: stu0629(pepQ)
            STE: STER_0678
            SSA: SSA_1577(pepQ)
            SSU: SSU05_1373
            SSV: SSU98_1388
            SGO: SGO_0771(pepQ)
            LPL: lp_2258(pepQ)
            LJO: LJ0490
            LAC: LBA0430 LBA1336(pepP)
            LSA: LSA0414(pepQ)
            LSL: LSL_1084(pepQ)
            LDB: Ldb1594(pepQ1) Ldb1700(pepZ)
            LBU: LBUL_1474
            LBR: LVIS_1204
            LCA: LSEI_0808
            LGA: LGAS_0435
            LRE: Lreu_0549
            PPE: PEPE_1251
            EFA: EF1743(pepQ-2)
            OOE: OEOE_0574
            LME: LEUM_0543
            STH: STH1865 STH828
            CAC: CAC2788
            CPE: CPE2497
            CPF: CPF_2820
            CPR: CPR_2506
            CNO: NT01CX_1669
            CDF: CD2347 CD2485
            CBO: CBO2030(pepQ)
            CBA: CLB_1971(pepQ)
            CBH: CLC_1976(pepQ)
            CBF: CLI_2095(pepQ)
            CKL: CKL_1215(pepQ)
            MMY: MSC_0357(pepQ)
            MMO: MMOB5500(pepQ)
            MCP: MCAP_0341
            MFL: Mfl379
            MSM: MSMEG_2494
            CGB: cg1681(pepE)
            RHA: RHA1_ro00832 RHA1_ro07144(pepQ) RHA1_ro10433
            AAU: AAur_3432
            SEN: SACE_2074(pepQ) SACE_2279
            FNU: FN1949
            CTA: CTA_0624(pepP)
            BGA: BG0438
            AVA: Ava_4366
            TER: Tery_3411
            BTH: BT_2522
            CCH: Cag_1740
            PLT: Plut_1603
            DRA: DR_1246
            DGE: Dgeo_1087
            TMA: TM1713
            MJA: MJ0806
            MMP: MMP1204
            MST: Msp_1153(pepQ)
            TAC: Ta1037
            TVO: TVN0558
            PTO: PTO0981
            PHO: PH1149
            PAB: PAB1637(pepQ-2)
            PFU: PF1343
            TKO: TK0967
            APE: APE_0526.1
            HBU: Hbut_0451
            SSO: SSO0363(pepQ)
            STO: ST1384
            SAI: Saci_1480(pepQ)
            PAI: PAE2025
STRUCTURES  PDB: 1PV9  1WY2  2IW2  2OKN  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.9
            ExPASy - ENZYME nomenclature database: 3.4.13.9
            ExplorEnz - The Enzyme Database: 3.4.13.9
            ERGO genome analysis and discovery system: 3.4.13.9
            BRENDA, the Enzyme Database: 3.4.13.9
            CAS: 9025-32-5
///
ENTRY       EC 3.4.13.10      Obsolete  Enzyme
NAME        Transferred to 3.4.19.5
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
COMMENT     Transferred entry: now EC 3.4.19.5 beta-aspartyl-peptidase (EC
            3.4.13.10 created 1972, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.10
            ExPASy - ENZYME nomenclature database: 3.4.13.10
            ExplorEnz - The Enzyme Database: 3.4.13.10
            ERGO genome analysis and discovery system: 3.4.13.10
            BRENDA, the Enzyme Database: 3.4.13.10
///
ENTRY       EC 3.4.13.11      Obsolete  Enzyme
NAME        Transferred to 3.4.13.19
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
COMMENT     Transferred entry: now EC 3.4.13.19 membrane dipeptidase (EC
            3.4.13.11 created 1972, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.11
            ExPASy - ENZYME nomenclature database: 3.4.13.11
            ExplorEnz - The Enzyme Database: 3.4.13.11
            ERGO genome analysis and discovery system: 3.4.13.11
            BRENDA, the Enzyme Database: 3.4.13.11
///
ENTRY       EC 3.4.13.12                Enzyme
NAME        Met-Xaa dipeptidase;
            methionyl dipeptidase;
            dipeptidase M;
            Met-X dipeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
REACTION    Hydrolysis of Met!Xaa dipeptides
ALL_REAC    (other) R00657
COFACTOR    Manganese [CPD:C00034]
COMMENT     A Mn2+-activated Escherichia coli enzyme with thiol dependence
REFERENCE   1  [PMID:4567782]
  AUTHORS   Brown JL.
  TITLE     Purification and properties of dipeptidase M from Escherichia coli
            B.
  JOURNAL   J. Biol. Chem. 248 (1973) 409-16.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00271  Methionine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.12
            ExPASy - ENZYME nomenclature database: 3.4.13.12
            ExplorEnz - The Enzyme Database: 3.4.13.12
            ERGO genome analysis and discovery system: 3.4.13.12
            BRENDA, the Enzyme Database: 3.4.13.12
            CAS: 37341-91-6
///
ENTRY       EC 3.4.13.13      Obsolete  Enzyme
NAME        Transferred to 3.4.13.3
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
COMMENT     Transferred entry: now EC 3.4.13.3, X-His dipeptidase (EC 3.4.13.13
            created 1981, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.13
            ExPASy - ENZYME nomenclature database: 3.4.13.13
            ExplorEnz - The Enzyme Database: 3.4.13.13
            ERGO genome analysis and discovery system: 3.4.13.13
            BRENDA, the Enzyme Database: 3.4.13.13
///
ENTRY       EC 3.4.13.14      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
COMMENT     Deleted entry: gamma-glutamyldipeptidase (EC 3.4.13.14 created 1989,
            deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.14
            ExPASy - ENZYME nomenclature database: 3.4.13.14
            ExplorEnz - The Enzyme Database: 3.4.13.14
            ERGO genome analysis and discovery system: 3.4.13.14
            BRENDA, the Enzyme Database: 3.4.13.14
///
ENTRY       EC 3.4.13.15      Obsolete  Enzyme
NAME        Transferred to 3.4.13.18
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
COMMENT     Transferred entry: now EC 3.4.13.18 cytosol nonspecific dipeptidase
            (EC 3.4.13.15 created 1989, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.15
            ExPASy - ENZYME nomenclature database: 3.4.13.15
            ExplorEnz - The Enzyme Database: 3.4.13.15
            ERGO genome analysis and discovery system: 3.4.13.15
            BRENDA, the Enzyme Database: 3.4.13.15
///
ENTRY       EC 3.4.13.16      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
COMMENT     Deleted entry: aspartylphenylalanine dipeptidase (EC 3.4.13.16
            created 1989, deleted 1992)
STRUCTURES  PDB: 2BPV  2BPW  2BPX  2BPY  2BPZ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.16
            ExPASy - ENZYME nomenclature database: 3.4.13.16
            ExplorEnz - The Enzyme Database: 3.4.13.16
            ERGO genome analysis and discovery system: 3.4.13.16
            BRENDA, the Enzyme Database: 3.4.13.16
///
ENTRY       EC 3.4.13.17                Enzyme
NAME        non-stereospecific dipeptidase;
            peptidyl-D-amino acid hydrolase;
            D-(or L-)aminoacyl-dipeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
REACTION    Hydrolysis of dipeptides containing either D- or L-amino acids or
            both
COMMENT     A digestive enzyme of cephalopods
REFERENCE   1  [PMID:6444201]
  AUTHORS   D'Aniello A, Strazzullo L.
  TITLE     Peptidyl-D-amino acid hydrolase from Loligo vulgaris Lam.
            Purification and characterization.
  JOURNAL   J. Biol. Chem. 259 (1984) 4237-43.
  ORGANISM  Loligo vulgaris
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.17
            ExPASy - ENZYME nomenclature database: 3.4.13.17
            ExplorEnz - The Enzyme Database: 3.4.13.17
            ERGO genome analysis and discovery system: 3.4.13.17
            BRENDA, the Enzyme Database: 3.4.13.17
            CAS: 90371-43-0
///
ENTRY       EC 3.4.13.18                Enzyme
NAME        cytosol nonspecific dipeptidase;
            N2-beta-alanylarginine dipeptidase;
            glycyl-glycine dipeptidase;
            glycyl-leucine dipeptidase;
            iminodipeptidase;
            peptidase A;
            Pro-X dipeptidase;
            prolinase;
            prolyl dipeptidase;
            prolylglycine dipeptidase;
            iminodipeptidase;
            prolinase;
            L-prolylglycine dipeptidase;
            prolylglycine dipeptidase;
            diglycinase;
            Gly-Leu hydrolase;
            glycyl-L-leucine dipeptidase;
            glycyl-L-leucine hydrolase;
            glycyl-L-leucine peptidase;
            L-amino-acyl-L-amino-acid hydrolase;
            glycylleucine peptidase;
            glycylleucine hydrolase;
            glycylleucine dipeptide hydrolase;
            non-specific dipeptidase;
            human cytosolic non-specific dipeptidase;
            glycyl-L-leucine hydrolase;
            glycyl-glycine dipeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
REACTION    Hydrolysis of dipeptides, preferentially hydrophobic dipeptides
            including prolyl amino acids
COFACTOR    Zinc [CPD:C00038]
INHIBITOR   L-Leucine [CPD:C00123]
EFFECTOR    Manganese [CPD:C00034];
            Dithiothreitol [CPD:C00265]
COMMENT     A zinc enzyme with broad specificity, varying somewhat with source
            species. Activated and stabilized by dithiothreitol and Mn2+.
            Inhibited by bestatin and leucine.
REFERENCE   1
  AUTHORS   Bauer, K.
  TITLE     Cytosol non-specific dipeptidase.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Academic Press, London, 1998, p.
            1520-1522.
ORTHOLOGY   KO: K01272  cytosol nonspecific dipeptidase
GENES       LLM: llmg_0260(pepDA) llmg_0943(pepDB)
            SMU: SMU.1303c
            SSA: SSA_0356
            LAC: LBA0035 LBA0235 LBA0236 LBA1294 LBA1837
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.18
            ExPASy - ENZYME nomenclature database: 3.4.13.18
            ExplorEnz - The Enzyme Database: 3.4.13.18
            ERGO genome analysis and discovery system: 3.4.13.18
            BRENDA, the Enzyme Database: 3.4.13.18
            CAS: 9025-31-4
///
ENTRY       EC 3.4.13.19                Enzyme
NAME        membrane dipeptidase;
            renal dipeptidase;
            dehydropeptidase I (DPH I);
            dipeptidase;
            aminodipeptidase;
            dipeptide hydrolase;
            dipeptidyl hydrolase;
            nonspecific dipeptidase;
            glycosyl-phosphatidylinositol-anchored renal dipeptidase;
            MDP
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
REACTION    Hydrolysis of dipeptides
COFACTOR    Zinc [CPD:C00038]
INHIBITOR   Cilastatin [CPD:C01675]
COMMENT     A membrane-bound, zinc enzyme with broad specificity. Abundant in
            the kidney cortex. Inhibited by bestatin and cilastatin. Type
            example of peptidase family M19.
REFERENCE   1  [PMID:5961612]
  AUTHORS   Campbell BJ, Lin YC, Davis RV, Ballew E.
  TITLE     The purification and properties of a particulate renal dipeptidase.
  JOURNAL   Biochim. Biophys. Acta. 118 (1966) 371-86.
REFERENCE   2
  AUTHORS   Campbell, B.J.
  TITLE     Renal dipeptidase.
  JOURNAL   Methods Enzymol. 19 (1970) 722-729.
REFERENCE   3  [PMID:7125632]
  AUTHORS   Kropp H, Sundelof JG, Hajdu R, Kahan FM.
  TITLE     Metabolism of thienamycin and related carbapenem antibiotics by the
            renal dipeptidase, dehydropeptidase.
  JOURNAL   Antimicrob. Agents. Chemother. 22 (1982) 62-70.
  ORGANISM  mouse [GN:mmu], rat [GN:rno], rabbit, dog [GN:cfa], monkey,
            chimpanzee [GN:ptr]
REFERENCE   4  [PMID:2137335]
  AUTHORS   Hooper NM, Keen JN, Turner AJ.
  TITLE     Characterization of the glycosyl-phosphatidylinositol-anchored human
            renal dipeptidase reveals that it is more extensively glycosylated
            than the pig enzyme.
  JOURNAL   Biochem. J. 265 (1990) 429-33.
  ORGANISM  pig [GN:ssc]
ORTHOLOGY   KO: K01273  membrane dipeptidase
GENES       HSA: 1800(DPEP1)
            MMU: 13479(Dpep1)
            RNO: 94199(Dpep1)
            CFA: 479611(DPEP1)
            BTA: 514685(MGC126924)
            SSC: 397196(DPEP1)
            SPU: 578328(LOC578328) 592585(LOC592585)
            DME: Dmel_CG6154
            SPO: SPAC3A11.10c SPCC965.12
            ANI: AN0224.2
            AFM: AFUA_6G09650
            AOR: AO090001000042 AO090023000428 AO090023000540
            CNE: CNC05890
            UMA: UM01942.1
            XCC: XCC4228
            XCB: XC_4317
            XCV: XCV3130 XCV4474
            XAC: XAC2984 XAC4362
            XOO: XOO4622
            PPF: Pput_0329
            PEN: PSEEN3220
            PMY: Pmen_0497
            PHA: PSHAa2910
            PAT: Patl_3688
            MMW: Mmwyl1_2726
            DNO: DNO_0073
            RSO: RS02031(RSp0056)
            REU: Reut_B4821
            BMA: BMAA0472
            BXE: Bxe_B1584
            BVI: Bcep1808_3422
            BUR: Bcep18194_B0572
            BCN: Bcen_3284
            BCH: Bcen2424_5084
            BAM: Bamb_4496
            BPS: BPSS0548
            BPM: BURPS1710b_A2108
            BTE: BTH_II1867
            VEI: Veis_4050
            ADE: Adeh_3815
            MLO: mll3679
            PLA: Plav_3591
            SMD: Smed_3733
            ATU: Atu2519
            ATC: AGR_C_4575
            RET: RHE_CH03991(ypch01411)
            RLE: RL4652
            BME: BMEII0626
            BMF: BAB2_0586
            BMS: BRA0654
            BMB: BruAb2_0572
            XAU: Xaut_0861
            SIL: SPO1542
            SIT: TM1040_0039
            RSP: RSP_0802
            RSQ: Rsph17025_0377
            RDE: RD1_2067
            NAR: Saro_0805
            SAL: Sala_2312
            ELI: ELI_09665
            GOX: GOX2272
            GBE: GbCGDNIH1_2365
            ACR: Acry_3086
            ABA: Acid345_1522 Acid345_2579
            SUS: Acid_3699 Acid_4390
            BAN: BA3911
            BAR: GBAA3911
            BAA: BA_4381
            BAT: BAS3624
            BCE: BC3775
            BCA: BCE_3810
            BCZ: BCZK3534
            BCY: Bcer98_2427
            BTK: BT9727_3516
            BLD: BLi01922
            BCL: ABC2143
            OIH: OB2692
            GKA: GK1300
            LWE: lwe2411
            CPE: CPE1928
            CPR: CPR_1894
            CTC: CTC00571
            CTH: Cthe_0756
            CBE: Cbei_2397
            AMT: Amet_0477 Amet_3077
            DSY: DSY1937
            DRM: Dred_1915
            MSM: MSMEG_3731
            SCO: SCO3058(SCBAC19G2.13c)
            KRA: Krad_1837
            SEN: SACE_4049
            CTA: CTA_0145
            SRU: SRU_0920
            RRS: RoseRS_3883
            RCA: Rcas_3312
            TTH: TTC1181
            PTO: PTO0633
            SSO: SSO1864
            STO: ST1063
            SAI: Saci_1691
STRUCTURES  PDB: 1ITQ  1ITU  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.19
            ExPASy - ENZYME nomenclature database: 3.4.13.19
            ExplorEnz - The Enzyme Database: 3.4.13.19
            ERGO genome analysis and discovery system: 3.4.13.19
            BRENDA, the Enzyme Database: 3.4.13.19
            CAS: 9031-99-6
///
ENTRY       EC 3.4.13.20                Enzyme
NAME        beta-Ala-His dipeptidase;
            serum carnosinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
REACTION    Preferential hydrolysis of the beta-Ala!His dipeptide (carnosine),
            and also anserine, Xaa!His dipeptides and other dipeptides including
            homocarnosine
ALL_REAC    (other) R01166 R03286
COFACTOR    Citrate [CPD:C00158];
            Cadmium [CPD:C01413]
COMMENT     Present in the serum of humans and higher primates, but not in the
            serum of other mammals. Activated by Cd2+ and citrate. Belongs in
            peptidase family M20.
REFERENCE   1  [PMID:7116644]
  AUTHORS   Lenney JF, George RP, Weiss AM, Kucera CM, Chan PW, Rinzler GS.
  TITLE     Human serum carnosinase: characterization, distinction from cellular
            carnosinase, and activation by cadmium.
  JOURNAL   Clin. Chim. Acta. 123 (1982) 221-31.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:1903095]
  AUTHORS   Jackson MC, Kucera CM, Lenney JF.
  TITLE     Purification and properties of human serum carnosinase.
  JOURNAL   Clin. Chim. Acta. 196 (1991) 193-205.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00340  Histidine metabolism
            PATH: map00410  beta-Alanine metabolism
ORTHOLOGY   KO: K05604  beta-Ala-His dipeptidase
GENES       HSA: 84735(CNDP1)
            PTR: 455474(CNDP1)
            MMU: 338403(Cndp1)
            RNO: 307212(Cndp1)
            CFA: 476165(CNDP1)
            GGA: 421012(CNDP1)
            XLA: 398917(MGC68563)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.20
            ExPASy - ENZYME nomenclature database: 3.4.13.20
            ExplorEnz - The Enzyme Database: 3.4.13.20
            ERGO genome analysis and discovery system: 3.4.13.20
            BRENDA, the Enzyme Database: 3.4.13.20
            CAS: 9027-21-8
///
ENTRY       EC 3.4.13.21                Enzyme
NAME        dipeptidase E;
            aspartyl dipeptidase;
            peptidase E;
            PepE gene product (Salmonella typhimurium)
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
REACTION    Dipeptidase E catalyses the hydrolysis of dipeptides Asp!Xaa. It
            does not act on peptides with N-terminal Glu, Asn or Gln, nor does
            it cleave isoaspartyl peptides
COMMENT     A free carboxy group is not absolutely required in the substrate
            since Asp-Phe-NH2 and Asp-Phe-OMe are hydrolysed somewhat more
            slowly than dipeptides with free C-termini. No peptide larger than a
            C-blocked dipeptide is known to be a substrate. Asp-NH-Np is
            hydrolysed and is a convenient substrate for routine assay. The
            enzyme is most active near pH 7.0, and is not inhibited by
            di-isopropylfluorophosphate or phenylmethanesulfonyl fluoride.
            Belongs in peptidase family S51.
REFERENCE   1  [PMID:11106384]
  AUTHORS   Hakansson K, Wang AH, Miller CG.
  TITLE     The structure of aspartyl dipeptidase reveals a unique fold with a
            Ser-His-Glu catalytic triad.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 14097-102.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:10762256]
  AUTHORS   Lassy RA, Miller CG.
  TITLE     Peptidase E, a peptidase specific for N-terminal aspartic
            dipeptides, is a serine hydrolase.
  JOURNAL   J. Bacteriol. 182 (2000) 2536-43.
  ORGANISM  Salmonella enterica serovar Typhimurium
ORTHOLOGY   KO: K05995  dipeptidase E
GENES       GGA: 424109(LOC424109)
            XLA: 378550(aad-a)
            XTR: 549202(dpepe)
            DME: Dmel_CG2200
            TBR: Tb11.01.4450
            LMA: LmjF09.0600
            ECO: b4021(pepE)
            ECJ: JW3981(pepE)
            ECE: Z5612(pepE)
            ECS: ECs4939
            ECC: c4980(pepE)
            ECI: UTI89_C4581(pepE)
            ECP: ECP_4232
            ECV: APECO1_2454(pepE)
            ECW: EcE24377A_4565(pepE)
            ECX: EcHS_A4257
            STY: STY4407(pepE)
            STT: t4117(pepE)
            SPT: SPA4028(pepE)
            SEC: SC4069(pepE)
            STM: STM4190(pepE)
            SFL: SF4087(pepE)
            SFX: S3643(pepE)
            SFV: SFV_4092(pepE)
            SSN: SSON_4192(pepE)
            SBO: SBO_4042(pepE)
            SPE: Spro_0257
            HIN: HI0587(pepE)
            HIT: NTHI0738(pepE)
            HIP: CGSHiEE_00035
            HSO: HS_1245(pepE)
            PMU: PM0454(pepE)
            APL: APL_0871(pepE)
            ASU: Asuc_1062
            VFI: VFA1068
            PPR: PBPRA2559
            SON: SO_2730(pepE)
            SDN: Sden_2131
            SFR: Sfri_1567
            SAZ: Sama_1442
            SBL: Sbal_2558
            SBM: Shew185_2596
            SPC: Sputcn32_2335
            SSE: Ssed_2771
            SHE: Shewmr4_2352
            SHM: Shewmr7_2424
            SHN: Shewana3_2513
            SHW: Sputw3181_1673
            PAT: Patl_1809
            AHA: AHA_3293(pepE)
            REU: Reut_B5540
            REH: H16_A2300(pepE1) H16_B0135(pepE2)
            BUR: Bcep18194_B2319
            AAV: Aave_4364
            VEI: Veis_3298
            WSU: WS1597
            CCV: CCV52592_2072
            BAN: BA1774
            BAR: GBAA1774
            BAA: BA_2282
            BAT: BAS1643
            BCE: BC1717
            BCA: BCE_1847
            BCZ: BCZK1592(pepE)
            BTK: BT9727_1622(pepE)
            BLI: BL00475
            BLD: BLi02841
            LMO: lmo0363
            LMF: LMOf2365_0382
            LIN: lin0382
            LLC: LACR_1589
            LPL: lp_1574
            TTE: TTE2723(pepE)
            CGL: NCgl0448(cgl0464)
            CGB: cg0550
            CJK: jk1275
            SCO: SCO0575(SC5G5.07)
            PAC: PPA1579
            SEN: SACE_1952
            FNU: FN1116
            ANA: alr7184
            GFO: GFO_2729(pepE)
            FJO: Fjoh_1768
            FPS: FP2130(pepE)
            DRA: DR_1070
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.21
            ExPASy - ENZYME nomenclature database: 3.4.13.21
            ExplorEnz - The Enzyme Database: 3.4.13.21
            ERGO genome analysis and discovery system: 3.4.13.21
            BRENDA, the Enzyme Database: 3.4.13.21
///
ENTRY       EC 3.4.13.22                Enzyme
NAME        D-Ala-D-Ala dipeptidase;
            D-alanyl-D-alanine dipeptidase;
            vanX D-Ala-D-Ala dipeptidase;
            VanX
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidases
REACTION    D-Ala-D-Ala + H2O = 2 D-Ala [RN:R07651]
ALL_REAC    R07651
SUBSTRATE   D-Ala-D-Ala [CPD:C00993];
            H2O [CPD:C00001]
PRODUCT     D-Ala [CPD:C00133]
COMMENT     A Zn2+-dependent enzyme [4]. The enzyme protects Enterococcus
            faecium from the antibiotic vancomycin, which can bind to the
            -D-Ala-D-Ala sequence at the C-terminus of the peptidoglycan
            pentapeptide (see diagram). This enzyme reduces the availability of
            the free dipeptide D-Ala-D-Ala, which is the precursor for this
            pentapeptide sequence, allowing D-Ala-(R)-lactate (for which
            vancomycin has much less affinity) to be added to the cell wall
            instead [2,3]. The enzyme is stereospecific, as L-Ala-L-Ala,
            D-Ala-L-Ala and L-Ala-D-Ala are not substrates [2]. Belongs in
            peptidase family M15.
REFERENCE   1  [PMID:7854121]
  AUTHORS   Reynolds PE, Depardieu F, Dutka-Malen S, Arthur M, Courvalin P.
  TITLE     Glycopeptide resistance mediated by enterococcal transposon Tn1546
            requires production of VanX for hydrolysis of D-alanyl-D-alanine.
  JOURNAL   Mol. Microbiol. 13 (1994) 1065-70.
  ORGANISM  Enterococcus faecium [GN:efa]
REFERENCE   2  [PMID:7873524]
  AUTHORS   Wu Z, Wright GD, Walsh CT.
  TITLE     Overexpression, purification, and characterization of VanX, a D-,
            D-dipeptidase which is essential for vancomycin resistance in
            Enterococcus faecium BM4147.
  JOURNAL   Biochemistry. 34 (1995) 2455-63.
  ORGANISM  Enterococcus faecium [GN:efa]
REFERENCE   3  [PMID:9265630]
  AUTHORS   McCafferty DG, Lessard IA, Walsh CT.
  TITLE     Mutational analysis of potential zinc-binding residues in the active
            site of the enterococcal D-Ala-D-Ala dipeptidase VanX.
  JOURNAL   Biochemistry. 36 (1997) 10498-505.
REFERENCE   4  [PMID:9702193]
  AUTHORS   Bussiere DE, Pratt SD, Katz L, Severin JM, Holzman T, Park CH.
  TITLE     The structure of VanX reveals a novel amino-dipeptidase involved in
            mediating transposon-based vancomycin resistance.
  JOURNAL   Mol. Cell. 2 (1998) 75-84.
  ORGANISM  Enterococcus faecium [GN:efa]
REFERENCE   5  [PMID:11881895]
  AUTHORS   Tan AL, Loke P, Sim TS.
  TITLE     Molecular cloning and functional characterisation of VanX, a
            D-alanyl-D-alanine dipeptidase from Streptomyces coelicolor A3(2).
  JOURNAL   Res. Microbiol. 153 (2002) 27-32.
  ORGANISM  Streptomyces coelicolor [GN:sco]
REFERENCE   6  [PMID:17017774]
  AUTHORS   Matthews ML, Periyannan G, Hajdin C, Sidgel TK, Bennett B, Crowder
            MW.
  TITLE     Probing the reaction mechanism of the D-ala-D-ala dipeptidase, VanX,
            by using stopped-flow kinetic and rapid-freeze quench EPR studies on
            the Co(II)-substituted enzyme.
  JOURNAL   J. Am. Chem. Soc. 128 (2006) 13050-1.
  ORGANISM  Enterococcus faecium [GN:efa]
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.13.22
            ExPASy - ENZYME nomenclature database: 3.4.13.22
            ExplorEnz - The Enzyme Database: 3.4.13.22
            ERGO genome analysis and discovery system: 3.4.13.22
            BRENDA, the Enzyme Database: 3.4.13.22
///
ENTRY       EC 3.4.14.1                 Enzyme
NAME        dipeptidyl-peptidase I;
            cathepsin C;
            dipeptidyl aminopeptidase I;
            dipeptidyl transferase;
            cathepsin C;
            dipeptidyl transferase;
            dipeptide arylamidase I;
            DAP I
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidyl-peptidases and tripeptidyl-peptidases
REACTION    Release of an N-terminal dipeptide, Xaa-Yaa!Zaa-, except when Xaa is
            Arg or Lys, or Yaa or Zaa is Pro
EFFECTOR    Chloride [CPD:C00115]
COMMENT     A Cl--dependent, lysosomal cysteine-type peptidase maximally active
            at acidic pH. Also polymerizes dipeptide amides, arylamides and
            esters at neutral pH. In peptidase family C1 (papain family).
REFERENCE   1
  AUTHORS   Planta, R.J., Gorter, J. and Gruber, M.
  TITLE     The catalytic properties of cathepsin C.
  JOURNAL   Biochim. Biophys. Acta 89 (1964) 511-519.
REFERENCE   2  [PMID:5961281]
  AUTHORS   Metroione RM, Neves AG, Fruton JS.
  TITLE     Purification and properties of dipeptidyl transferase (Cathepsin C).
  JOURNAL   Biochemistry. 5 (1966) 1597-604.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:4306035]
  AUTHORS   McDonald JK, Zeitman BB, Reilly TJ, Ellis S.
  TITLE     New observations on the substrate specificity of cathepsin C
            (dipeptidyl aminopeptidase I). Including the degradation of
            beta-corticotropin and other peptide hormones.
  JOURNAL   J. Biol. Chem. 244 (1969) 2693-709.
  ORGANISM  rat [GN:rno], cow [GN:bta]
REFERENCE   4
  AUTHORS   McDonald, J.K. and Schwabe, C.
  TITLE     Intracellular exopeptidases.
  JOURNAL   In: Barrett, A.J. (Ed.), Proteinases in Mammalian Cells and Tissues,
            North-Holland Publishing Co., Amsterdam, 1977, p. 311-391.
ORTHOLOGY   KO: K01275  cathepsin C
GENES       HSA: 1075(CTSC)
            PTR: 451469(CTSC)
            MMU: 13032(Ctsc)
            RNO: 25423(Ctsc)
            CFA: 403458(CTSC) 478608(CTSC)
            BTA: 352958(CTSC)
            GGA: 419014(CTSC)
            XLA: 380203(ctsc)
            XTR: 407938(LOC407938)
            DRE: 368704(ctsc)
            SPU: 586157(LOC586157) 761822(LOC761822)
            PFA: PFL2290w
            CHO: Chro.40239
            TAN: TA04105 TA15665
            TPV: TP03_0357
            TET: TTHERM_00102770 TTHERM_00502690
STRUCTURES  PDB: 1JQP  1K3B  2DJF  2DJG  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.14.1
            ExPASy - ENZYME nomenclature database: 3.4.14.1
            ExplorEnz - The Enzyme Database: 3.4.14.1
            ERGO genome analysis and discovery system: 3.4.14.1
            BRENDA, the Enzyme Database: 3.4.14.1
            CAS: 9032-68-2
///
ENTRY       EC 3.4.14.2                 Enzyme
NAME        dipeptidyl-peptidase II;
            dipeptidyl aminopeptidase II;
            dipeptidyl arylamidase II;
            carboxytripeptidase;
            dipeptidyl peptidase II;
            dipeptidyl arylamidase II;
            DAP II;
            dipeptidyl(amino)peptidase II;
            dipeptidylarylamidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidyl-peptidases and tripeptidyl-peptidases
REACTION    Release of an N-terminal dipeptide, Xaa-Yaa!, preferentially when
            Yaa is Ala or Pro. Substrates are oligopeptides, preferentially
            tripeptides
COMMENT     A lysosomal serine-type peptidase in family S28 (Pro-X
            carboxypeptidase family); maximally active at acidic pH
REFERENCE   1  [PMID:4969969]
  AUTHORS   McDonald JK, Leibach FH, Grindeland RE, Ellis S.
  TITLE     Purification of  dipeptidyl aminopeptidase II (dipeptidyl
            arylamidase II) of the anterior pituitary gland. Peptidase and
            dipeptide esterase activities.
  JOURNAL   J. Biol. Chem. 243 (1968) 4143-50.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   McDonald, J.K. and Schwabe, C.
  TITLE     Intracellular exopeptidases.
  JOURNAL   In: Barrett, A.J. (Ed.), Proteinases in Mammalian Cells and Tissues,
            North-Holland Publishing Co., Amsterdam, 1977, p. 311-391.
ORTHOLOGY   KO: K01276  dipeptidyl-peptidase II
GENES       HSA: 29952(DPP7)
            PTR: 473101(DPP7)
            MMU: 83768(Dpp7)
            RNO: 83799(Dpp7)
            CFA: 607003(DPP7)
            GGA: 417297(DPP7)
            DRE: 503737(zgc:113564)
            SPU: 592836(LOC592836)
            TET: TTHERM_00028690 TTHERM_00028700 TTHERM_00035670
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.14.2
            ExPASy - ENZYME nomenclature database: 3.4.14.2
            ExplorEnz - The Enzyme Database: 3.4.14.2
            ERGO genome analysis and discovery system: 3.4.14.2
            BRENDA, the Enzyme Database: 3.4.14.2
            CAS: 76199-23-0
///
ENTRY       EC 3.4.14.3       Obsolete  Enzyme
NAME        Transferred to 3.4.19.1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidyl-peptidases and tripeptidyl-peptidases
COMMENT     Transferred entry: now EC 3.4.19.1 acylaminoacyl-peptidase (EC
            3.4.14.3 created 1978, deleted 1981)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.14.3
            ExPASy - ENZYME nomenclature database: 3.4.14.3
            ExplorEnz - The Enzyme Database: 3.4.14.3
            ERGO genome analysis and discovery system: 3.4.14.3
            BRENDA, the Enzyme Database: 3.4.14.3
///
ENTRY       EC 3.4.14.4                 Enzyme
NAME        dipeptidyl-peptidase III;
            dipeptidyl aminopeptidase III;
            dipeptidyl arylamidase III;
            enkephalinase B;
            red cell angiotensinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidyl-peptidases and tripeptidyl-peptidases
REACTION    Release of an N-terminal dipeptide from a peptide comprising four or
            more residues, with broad specificity. Also acts on dipeptidyl
            2-naphthylamides.
COMMENT     A cytosolic peptidase that is active at neutral pH. It has broad
            activity on peptides, although it is highly selective for
            Arg-Arg-2-naphthylamide, at pH 9.2. Active in the hydrolysis of
            enkephalins. A metallopeptidase, the type example of peptidase
            family M49.
REFERENCE   1
  AUTHORS   McDonald, J.K.
  TITLE     Dipeptidyl-peptidase III.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Handbook of Proteolytic Enzymes,
            London, 1998, p. 536-538.
REFERENCE   2  [PMID:10387075]
  AUTHORS   Fukasawa K, Fukasawa KM, Iwamoto H, Hirose J, Harada M.
  TITLE     The HELLGH motif of rat liver dipeptidyl peptidase III is involved
            in zinc coordination and the catalytic activity of the enzyme.
  JOURNAL   Biochemistry. 38 (1999) 8299-303.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K01277  dipeptidyl-peptidase III
GENES       HSA: 10072(DPP3)
            MMU: 75221(Dpp3)
            RNO: 114591(Dpp3)
            CFA: 476011(DPP3)
            BTA: 510200(DPP3)
            XLA: 394413(dpp3-a) 446491(dpp3)
            DRE: 322527(dpp3)
            SPU: 582874(LOC582874)
            DME: Dmel_CG7415(DppIII)
            CEL: F02E9.9
            SCE: YOL057W
            AGO: AGOS_AER229C
            PIC: PICST_88224(DPP3)
            CGR: CAGL0C05093g
            ANI: AN4321.2
            AFM: AFUA_4G06140
            AOR: AO090023000980
            DDI: DDBDRAFT_0217197
            TET: TTHERM_00011440 TTHERM_00313320
            LMA: LmjF05.0960
            EHI: 58.t00023
            BTH: BT_1846
            BFR: BF3425
            BFS: BF3247
            PGI: PG0317
            GFO: GFO_0057
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.14.4
            ExPASy - ENZYME nomenclature database: 3.4.14.4
            ExplorEnz - The Enzyme Database: 3.4.14.4
            ERGO genome analysis and discovery system: 3.4.14.4
            BRENDA, the Enzyme Database: 3.4.14.4
            CAS: 77464-87-0
///
ENTRY       EC 3.4.14.5                 Enzyme
NAME        dipeptidyl-peptidase IV;
            dipeptidyl aminopeptidase IV;
            Xaa-Pro-dipeptidyl-aminopeptidase;
            Gly-Pro naphthylamidase;
            postproline dipeptidyl aminopeptidase IV;
            lymphocyte antigen CD26;
            glycoprotein GP110;
            dipeptidyl peptidase IV;
            glycylproline aminopeptidase;
            glycylproline aminopeptidase;
            X-prolyl dipeptidyl aminopeptidase;
            pep X;
            leukocyte antigen CD26;
            glycylprolyl dipeptidylaminopeptidase;
            dipeptidyl-peptide hydrolase;
            glycylprolyl aminopeptidase;
            dipeptidyl-aminopeptidase IV;
            DPP IV/CD26;
            amino acyl-prolyl dipeptidyl aminopeptidase;
            T cell triggering molecule Tp103;
            X-PDAP
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidyl-peptidases and tripeptidyl-peptidases
REACTION    Release of an N-terminal dipeptide, Xaa-Yaa!Zaa-, from a
            polypeptide, preferentially when Yaa is Pro, provided Zaa is neither
            Pro nor hydroxyproline
INHIBITOR   L-Pro-L-boroPro [CPD:C02292]
COMMENT     A homodimer. An integral protein of the plasma membrane of
            lymphocytes and other mammalian cells, in peptidase family S9
            (prolyl oligopeptidase family). The reaction is similar to that of
            the unrelated EC 3.4.14.11 Xaa-Pro dipeptidyl-peptidase of
            lactococci
REFERENCE   1  [PMID:1352704]
  AUTHORS   Misumi Y, Hayashi Y, Arakawa F, Ikehara Y.
  TITLE     Molecular cloning and sequence analysis of human dipeptidyl
            peptidase IV, a serine proteinase on the cell surface.
  JOURNAL   Biochim. Biophys. Acta. 1131 (1992) 333-6.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:8102366]
  AUTHORS   David F, Bernard AM, Pierres M, Marguet D.
  TITLE     Identification of serine 624, aspartic acid 702, and histidine 734
            as the catalytic triad residues of mouse dipeptidyl-peptidase IV
            (CD26). A member of a novel family of nonclassical serine
            hydrolases.
  JOURNAL   J. Biol. Chem. 268 (1993) 17247-52.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:7845210]
  AUTHORS   Ikehara Y, Ogata S, Misumi Y.
  TITLE     Dipeptidyl-peptidase IV from rat liver.
  JOURNAL   Methods. Enzymol. 244 (1994) 215-27.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K01278  dipeptidyl-peptidase 4
            KO: K08655  dipeptidyl-peptidase 8
            KO: K08656  dipeptidyl-peptidase 9
GENES       HSA: 1803(DPP4) 54878(DPP8) 91039(DPP9)
            PTR: 453518(DPP8) 459689(DPP4)
            MMU: 13482(Dpp4) 224897(Dpp9) 74388(Dpp8)
            RNO: 25253(Dpp4) 301130(LOC301130) 315758(Dpp8_predicted)
            CFA: 478767(DPP4) 485033(DPP9) 487605(DPP8)
            BTA: 281122(DPP4) 536604(LOC536604)
            SSC: 397492(DPPIV)
            GGA: 420159(DPP9) 424187(RCJMB04_29g21) 427512(DPP8)
            XLA: 397888(LOC397888) 443772(MGC81313)
            XTR: 548987(dpp4)
            DRE: 556437(LOC556437) 571728(LOC571728)
            SPU: 576891(LOC576891)
            DME: Dmel_CG11034 Dmel_CG32145(ome)
            ATH: AT5G24260
            OSA: 4329059
            ANI: AN6438.2
            AFM: AFUA_3G07850 AFUA_4G09320
            AOR: AO090023000602
            DDI: DDBDRAFT_0205566
            XCC: XCC3961
            XCB: XC_4051
            XCV: XCV4136
            XAC: XAC4046
            XOO: XOO0398
            XOM: XOO_0361(XOO0361)
            SON: SO_3990
            SDN: Sden_2985
            SFR: Sfri_0532
            SHE: Shewmr4_0650
            SHM: Shewmr7_3372
            SHN: Shewana3_0649
            ILO: IL2328
            CPS: CPS_1104
            PHA: PSHAa2386 PSHAb0005
            PAT: Patl_3968
            GUR: Gura_1624
            ADE: Adeh_1335
            MXA: MXAN_0515(dpp4) MXAN_1682 MXAN_6038
            CCR: CC_2154
            MMR: Mmar10_2106
            HNE: HNE_1217
            NAR: Saro_1409
            ELI: ELI_07440
            GOX: GOX1461
            ABA: Acid345_0056
            BAD: BAD_0045
            RBA: RB1225(dpp4)
            GVI: gll3871
            BTH: BT_4193
            BFR: BF0977
            BFS: BF0899
            PGI: PG0503(dpp)
            SRU: SRU_0572
            MHU: Mhun_0346
STRUCTURES  PDB: 1J2E  1N1M  1NU6  1NU8  1ORV  1ORW  1PFQ  1R9M  1R9N  1RWQ  
                 1TK3  1TKR  1U8E  1W1I  1WCY  1X70  2AJ8  2AJB  2AJC  2AJD  
                 2AJL  2BGN  2BGR  2BUA  2BUB  2BUC  2FJP  2G5P  2G5T  2G63  
                 2GBF  2GBG  2GBI  2HHA  2I03  2I3Z  2I78  2IIT  2IIV  2OAE  
                 2OAG  2OGZ  2OPH  2OQI  2OQV  2P8S  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.14.5
            ExPASy - ENZYME nomenclature database: 3.4.14.5
            ExplorEnz - The Enzyme Database: 3.4.14.5
            ERGO genome analysis and discovery system: 3.4.14.5
            BRENDA, the Enzyme Database: 3.4.14.5
            CAS: 54249-88-6
///
ENTRY       EC 3.4.14.6                 Enzyme
NAME        dipeptidyl-dipeptidase;
            dipeptidyl tetrapeptide hydrolase;
            dipeptidyl ligase;
            tetrapeptide dipeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidyl-peptidases and tripeptidyl-peptidases
REACTION    Preferential release of dipeptides from a tetrapeptide, e.g.
            Ala-Gly!Ala-Gly. Acts more slowly on Ala-Ala!Ala-Ala and
            Gly-Gly!Gly-Gly
COMMENT     A thiol-activated peptidase from cabbage (Brassica oleracea).
            Tetrapeptides are formed from Ala-Ala, Gly-Gly, Ala-Gly and Gly-Ala
REFERENCE   1
  AUTHORS   Eng, F.W.H.T.
  TITLE     Dipeptidyl tetrapeptide hydrolase, a new enzyme with dipeptidyl
            ligase activity.
  JOURNAL   Can. J. Biochem. Cell. Biol. 62 (1984) 516-528.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.14.6
            ExPASy - ENZYME nomenclature database: 3.4.14.6
            ExplorEnz - The Enzyme Database: 3.4.14.6
            ERGO genome analysis and discovery system: 3.4.14.6
            BRENDA, the Enzyme Database: 3.4.14.6
            CAS: 91608-92-3
///
ENTRY       EC 3.4.14.7       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidyl-peptidases and tripeptidyl-peptidases
COMMENT     Deleted entry: tetralysine endopeptidase (EC 3.4.14.7 created 1989,
            deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.14.7
            ExPASy - ENZYME nomenclature database: 3.4.14.7
            ExplorEnz - The Enzyme Database: 3.4.14.7
            ERGO genome analysis and discovery system: 3.4.14.7
            BRENDA, the Enzyme Database: 3.4.14.7
///
ENTRY       EC 3.4.14.8       Obsolete  Enzyme
NAME        Transferred to 3.4.14.10
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidyl-peptidases and tripeptidyl-peptidases
COMMENT     Transferred entry: now EC 3.4.14.10 tripeptidyl-peptidase II (EC
            3.4.14.8 created 1989, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.14.8
            ExPASy - ENZYME nomenclature database: 3.4.14.8
            ExplorEnz - The Enzyme Database: 3.4.14.8
            ERGO genome analysis and discovery system: 3.4.14.8
            BRENDA, the Enzyme Database: 3.4.14.8
///
ENTRY       EC 3.4.14.9                 Enzyme
NAME        tripeptidyl-peptidase I;
            tripeptidyl aminopeptidase;
            tripeptidyl peptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidyl-peptidases and tripeptidyl-peptidases
REACTION    Release of an N-terminal tripeptide from a polypeptide, but also has
            endopeptidase activity.
INHIBITOR   Isoflurophate [CPD:C00202]
COMMENT     A lysosomal enzyme that is active at acidic pH. Deficient in
            classical late-infantile neuronal ceroid lipofuscinosis brain
            tissue. Belongs in peptidase family S53. Formerly included in EC
            3.4.14.8.
REFERENCE   1  [PMID:10349869]
  AUTHORS   Ezaki J, Tanida I, Kanehagi N, Kominami E.
  TITLE     A lysosomal proteinase, the late infantile neuronal ceroid
            lipofuscinosis gene (CLN2) product, is essential for degradation of
            a hydrophobic protein, the subunit c of ATP synthase.
  JOURNAL   J. Neurochem. 72 (1999) 2573-82.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:9989235]
  AUTHORS   Rawlings ND, Barrett AJ.
  TITLE     Tripeptidyl-peptidase I is apparently the CLN2 protein absent in
            classical late-infantile neuronal ceroid lipofuscinosis.
  JOURNAL   Biochim. Biophys. Acta. 1429 (1999) 496-500.
  ORGANISM  human [GN:hsa], rat [GN:rno]
REFERENCE   3  [PMID:10679303]
  AUTHORS   Ezaki J, Takeda-Ezaki M, Oda K, Kominami E.
  TITLE     Characterization of endopeptidase activity of tripeptidyl
            peptidase-I/CLN2 protein which is deficient in classical late
            infantile neuronal ceroid lipofuscinosis.
  JOURNAL   Biochem. Biophys. Res. Commun. 268 (2000) 904-8.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:10617131]
  AUTHORS   Junaid MA, Wu G, Pullarkat RK.
  TITLE     Purification and characterization of bovine brain lysosomal
            pepstatin-insensitive proteinase, the gene product deficient in the
            human late-infantile neuronal ceroid lipofuscinosis.
  JOURNAL   J. Neurochem. 74 (2000) 287-94.
  ORGANISM  cow [GN:bta]
REFERENCE   5  [PMID:11054422]
  AUTHORS   Lin L, Sohar I, Lackland H, Lobel P.
  TITLE     The human CLN2 protein/tripeptidyl-peptidase I is a serine protease
            that autoactivates at acidic pH.
  JOURNAL   J. Biol. Chem. 276 (2001) 2249-55.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01279  tripeptidyl-peptidase I
GENES       HSA: 1200(TPP1)
            PTR: 450999(TPP1)
            MMU: 12751(Tpp1)
            RNO: 83534(Tpp1)
            CFA: 485337(TPP1)
            BTA: 515575(TPP1)
            XLA: 414505(MGC83094)
            ANI: AN7159.2
            AFM: AFUA_4G03490 AFUA_6G10250
            UMA: UM06118.1
            DDI: DDBDRAFT_0190668
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.14.9
            ExPASy - ENZYME nomenclature database: 3.4.14.9
            ExplorEnz - The Enzyme Database: 3.4.14.9
            ERGO genome analysis and discovery system: 3.4.14.9
            BRENDA, the Enzyme Database: 3.4.14.9
            CAS: 151662-36-1
///
ENTRY       EC 3.4.14.10                Enzyme
NAME        tripeptidyl-peptidase II;
            tripeptidyl aminopeptidase;
            tripeptidyl peptidase;
            tripeptidyl aminopeptidase II;
            tripeptidyl peptidase II;
            TPP
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidyl-peptidases and tripeptidyl-peptidases
REACTION    Release of an N-terminal tripeptide from a polypeptide
COMMENT     A cytosolic enzyme in peptidase family S8 (subtilisin family).
            Active at neutral pH. Inhibited by diisopropyl fluorophosphate.
            Formerly included in EC 3.4.14.8
REFERENCE   1  [PMID:6352701]
  AUTHORS   Balow RM, Ragnarsson U, Zetterqvist O.
  TITLE     Tripeptidyl aminopeptidase in the extralysosomal fraction of rat
            liver.
  JOURNAL   J. Biol. Chem. 258 (1983) 11622-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:3511062]
  AUTHORS   Balow RM, Tomkinson B, Ragnarsson U, Zetterqvist O.
  TITLE     Purification, substrate specificity, and classification of
            tripeptidyl peptidase II.
  JOURNAL   J. Biol. Chem. 261 (1986) 2409-17.
  ORGANISM  rat [GN:rno], human [GN:hsa]
REFERENCE   3  [PMID:1691635]
  AUTHORS   Tomkinson B, Zetterqvist O.
  TITLE     Immunological cross-reactivity between human tripeptidyl peptidase
            II and fibronectin.
  JOURNAL   Biochem. J. 267 (1990) 149-54.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01280  tripeptidyl-peptidase II
GENES       HSA: 7174(TPP2)
            PTR: 452645(TPP2)
            MMU: 22019(Tpp2)
            RNO: 81815(Tpp2)
            BTA: 526052(MGC157323)
            GGA: 428020(TPP2)
            XLA: 443806(MGC83244)
            DRE: 564757(LOC564757)
            SPU: 583848(LOC583848)
            DME: Dmel_CG3991(TppII)
            CEL: F21H12.6
            OSA: 4330237
            SPO: SPAP8A3.12c
            UMA: UM00517.1
            STP: Strop_0881
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.14.10
            ExPASy - ENZYME nomenclature database: 3.4.14.10
            ExplorEnz - The Enzyme Database: 3.4.14.10
            ERGO genome analysis and discovery system: 3.4.14.10
            BRENDA, the Enzyme Database: 3.4.14.10
            CAS: 101149-94-4
///
ENTRY       EC 3.4.14.11                Enzyme
NAME        Xaa-Pro dipeptidyl-peptidase;
            X-prolyl dipeptidyl aminopeptidase;
            PepX;
            X-prolyl dipeptidyl peptidase;
            X-Pro dipeptidyl-peptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidyl-peptidases and tripeptidyl-peptidases
REACTION    Hydrolyses Xaa-Pro! bonds to release unblocked, N-terminal
            dipeptides from substrates including Ala-Pro!p-nitroanilide and
            (sequentially) Tyr-Pro!Phe-Pro!Gly-Pro!Ile
COMMENT     The intracellular enzyme from Lactococcus lactis (190-kDa) is the
            type example of peptidase family S15. The reaction is similar to
            that catalysed by dipeptidyl-peptidase IV of animals
REFERENCE   1
  AUTHORS   Zevaco, C., Monnet, V. and Gripon, J.-C.
  TITLE     Intracellular X-prolyl dipeptidyl peptidase from Lactococcus lactis
            spp. lactis: purification and properties.
  JOURNAL   J. Appl. Bacteriol. 68 (1990) 357-366.
  ORGANISM  Lactococcus lactis
REFERENCE   2  [PMID:7765315]
  AUTHORS   Meyer-Barton EC, Klein JR, Imam M, Plapp R.
  TITLE     Cloning and sequence analysis of the
            X-prolyl-dipeptidyl-aminopeptidase gene (pepX) from Lactobacillus
            delbruckii ssp. lactis DSM7290.
  JOURNAL   Appl. Microbiol. Biotechnol. 40 (1993) 82-9.
  ORGANISM  Lactobacillus delbruckii
REFERENCE   3  [PMID:7765768]
  AUTHORS   Habibi-Najafi MB, Lee BH.
  TITLE     Purification and characterization of X-prolyl dipeptidyl peptidase
            from Lactobacillus casei subsp. casei LLG.
  JOURNAL   Appl. Microbiol. Biotechnol. 42 (1994) 280-6.
  ORGANISM  Lactobacillus casei [GN:lca]
REFERENCE   4  [PMID:7710078]
  AUTHORS   Chich JF, Gripon JC, Ribadeau-Dumas B.
  TITLE     Preparation of bacterial X-prolyl dipeptidyl aminopeptidase and its
            stabilization by organic cosolvents.
  JOURNAL   Anal. Biochem. 224 (1995) 245-9.
  ORGANISM  Lactococcus lactis
REFERENCE   5
  AUTHORS   Chich, J.-F., Chapot-Chartier, M.P., Ribadeau-Dumas, B. and Gripon,
            J.-C.
  TITLE     Identification of the active site serine of the X-prolyl
            aminopeptidase from Lactococcus lactis.
  JOURNAL   FEBS Lett. 314 (1995) 139-142.
  ORGANISM  Lactococcus lactis
ORTHOLOGY   KO: K01281  X-Pro dipeptidyl-peptidase
GENES       PIC: PICST_84390(DAP2)
            XCV: XCV0642
            BVI: Bcep1808_3448
            BUR: Bcep18194_B0505
            BCN: Bcen_3229
            BCH: Bcen2424_5138
            BAM: Bamb_4532
            BPS: BPSS0654 BPSS1992
            BPM: BURPS1710b_A1100(pepX) BURPS1710b_A2222(pepX)
            BTE: BTH_II0380
            BRA: BRADO1420
            ZMO: ZMO0700(pepX) ZMO1408(pepX)
            BAN: BA2860
            BAR: GBAA2860
            BAA: BA_3381
            BAT: BAS2667
            BCE: BC2861
            BCA: BCE_2891
            BCZ: BCZK2588(pepX)
            BTK: BT9727_2618(pepX)
            LLA: L118079(pepXP)
            LLC: LACR_2342
            LLM: llmg_2328(pepXP)
            SPY: SPy_1858(pepXP)
            SPZ: M5005_Spy_1577(pepXP)
            SPM: spyM18_1922
            SPG: SpyM3_1603(pepXP)
            SPS: SPs0264
            SPH: MGAS10270_Spy1644(pepXP)
            SPI: MGAS10750_Spy1635(pepXP)
            SPJ: MGAS2096_Spy1602(pepXP)
            SPK: MGAS9429_Spy1582(pepXP)
            SPF: SpyM50273(pepXP)
            SPA: M6_Spy1588
            SPB: M28_Spy1565(pepXP)
            SPN: SP_0894
            SPR: spr0794(pepXP)
            SPD: SPD_0787(pepX)
            SAG: SAG1736(pepX)
            SAN: gbs1781
            SAK: SAK_1744(pepX)
            SMU: SMU.395(pepX)
            STC: str1672(pepXP)
            STL: stu1672(pepXP)
            SSA: SSA_0328(pepXP)
            SGO: SGO_0234(pepX) SGO_1415
            LPL: lp_0857(pepX)
            LJO: LJ1585
            LAC: LBA1373(pepX)
            LSA: LSA0643(pepX)
            LSL: LSL_1534
            LDB: Ldb1455(pepX)
            LBU: LBUL_1351
            LBR: LVIS_1782
            LCA: LSEI_1651
            LGA: LGAS_0712
            LRE: Lreu_1647
            PPE: PEPE_0380
            OOE: OEOE_1411
            LME: LEUM_0506
            SMA: SAV1674
            SEN: SACE_1771(pepX) SACE_6505
            RBA: RB2081 RB9674(pepX)
            SRU: SRU_2821
            FPS: FP1112(pepX2) FP2339(pepX1)
STRUCTURES  PDB: 1LNS  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.14.11
            ExPASy - ENZYME nomenclature database: 3.4.14.11
            ExplorEnz - The Enzyme Database: 3.4.14.11
            ERGO genome analysis and discovery system: 3.4.14.11
            BRENDA, the Enzyme Database: 3.4.14.11
            CAS: 54249-88-6
///
ENTRY       EC 3.4.14.12                Enzyme
NAME        Xaa-Xaa-Pro tripeptidyl-peptidase;
            prolyltripeptidyl amino peptidase;
            prolyl tripeptidyl peptidase;
            prolyltripeptidyl aminopeptidase;
            PTP-A;
            TPP
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Dipeptidyl-peptidases and tripeptidyl-peptidases
REACTION    Hydrolysis of Xaa-Xaa-Pro!Yaa- releasing the N-terminal tripeptide
            of a peptide with Pro as the third residue (position P1) and where
            Yaa is not proline
COMMENT     This cell-surface-associated serine exopeptidase is found in the
            Gram-negative, anaerobic bacterium Porphyromonas gingivalis, which
            has been implicated in adult periodontal disease [1]. The enzyme
            releases the N-terminal tripeptide of peptides, such as
            interleukin-6. It has an absolute requirement for a proline residue
            at the P1 position but is completely inactivated by a proline
            residue at the P1' position [1]. The size of the peptide does not
            affect the rate of reaction [1].
REFERENCE   1  [PMID:10092598]
  AUTHORS   Banbula A, Mak P, Bugno M, Silberring J, Dubin A, Nelson D, Travis
            J, Potempa J.
  TITLE     Prolyl tripeptidyl peptidase from Porphyromonas gingivalis. A novel
            enzyme with possible pathological implications for the development
            of periodontitis.
  JOURNAL   J. Biol. Chem. 274 (1999) 9246-52.
  ORGANISM  Porphyromonas gingivalis [GN:pgi]
REFERENCE   2  [PMID:12620636]
  AUTHORS   Fujimura S, Ueda O, Shibata Y, Hirai K.
  TITLE     Isolation and properties of a tripeptidyl peptidase from a
            periodontal pathogen Prevotella nigrescens.
  JOURNAL   FEMS. Microbiol. Lett. 219 (2003) 305-9.
  ORGANISM  Prevotella nigrescens
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.14.12
            ExPASy - ENZYME nomenclature database: 3.4.14.12
            ExplorEnz - The Enzyme Database: 3.4.14.12
            ERGO genome analysis and discovery system: 3.4.14.12
            BRENDA, the Enzyme Database: 3.4.14.12
///
ENTRY       EC 3.4.15.1                 Enzyme
NAME        peptidyl-dipeptidase A;
            angiotensin I-converting enzyme;
            kininase II;
            dipeptidyl carboxypeptidase I;
            peptidase P;
            carboxycathepsin;
            dipeptide hydrolase;
            peptidyl dipeptidase;
            angiotensin converting enzyme;
            kininase II;
            angiotensin I-converting enzyme;
            carboxycathepsin;
            dipeptidyl carboxypeptidase;
            peptidyl dipeptidase I;
            peptidyl-dipeptide hydrolase;
            peptidyldipeptide hydrolase;
            endothelial cell peptidyl dipeptidase;
            ACE;
            peptidyl dipeptidase-4;
            peptidyl dipeptidase A;
            PDH;
            peptidyl dipeptide hydrolase;
            DCP
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl-dipeptidases
REACTION    Release of a C-terminal dipeptide, oligopeptide!Xaa-Yaa, when Xaa is
            not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of
            angiotensin I to angiotensin II, with increase in vasoconstrictor
            activity, but no action on angiotensin II
COFACTOR    Zinc [CPD:C00038]
INHIBITOR   (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(mercaptomethyl)-1-oxoprolyl]g
            lycine [CPD:C01313];
            (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(mercaptomethyl)-1-oxoprolyl]-
            (S)-alanine [CPD:C01314];
            (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(acetylthio)methyl-1-oxoprolyl
            ]glycine benzyl ester [CPD:C01315];
            (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(acetylthio)methyl-1-oxoprolyl
            ]-(S)-alanine benzyl ester [CPD:C01316]
EFFECTOR    Chloride [CPD:C00115]
COMMENT     A Cl--dependent, zinc glycoprotein that is generally membrane-bound.
            A potent inhibitor is captopril. Important in elevation of blood
            pressure, through formation of angiotensin II (vasoconstrictor) and
            destruction of bradykinin (vasodilator). Two molecular forms exist
            in mammalian tissues, a widely-distributed somatic form of 150- to
            180-kDa that contains two non-identical catalytic sites, and a
            testicular form of 90- to 100-kDa that contains only a single
            catalytic site. Type example of peptidase family M2
REFERENCE   1  [PMID:2849100]
  AUTHORS   Soubrier F, Alhenc-Gelas F, Hubert C, Allegrini J, John M, Tregear
            G, Corvol P.
  TITLE     Two putative active centers in human angiotensin I-converting enzyme
            revealed by molecular cloning.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 9386-90.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:2554286]
  AUTHORS   Ehlers MR, Fox EA, Strydom DJ, Riordan JF.
  TITLE     Molecular cloning of human testicular angiotensin-converting enzyme:
            the testis isozyme is identical to the C-terminal half of
            endothelial angiotensin-converting enzyme.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 7741-5.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:1320019]
  AUTHORS   Wei L, Clauser E, Alhenc-Gelas F, Corvol P.
  TITLE     The two homologous domains of human angiotensin I-converting enzyme
            interact differently with competitive inhibitors.
  JOURNAL   J. Biol. Chem. 267 (1992) 13398-405.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:7674927]
  AUTHORS   Corvol P, Williams TA, Soubrier F.
  TITLE     Peptidyl dipeptidase A: angiotensin I-converting enzyme.
  JOURNAL   Methods. Enzymol. 248 (1995) 283-305.
PATHWAY     PATH: map04614  Renin-angiotensin system
ORTHOLOGY   KO: K01283  peptidyl-dipeptidase A
GENES       HSA: 1636(ACE)
            PTR: 449567(ACE)
            MMU: 11421(Ace)
            RNO: 24310(Ace)
            CFA: 403837(ACE) 610668(ACE)
            BTA: 509484(ACE)
            SSC: 613133(ACE)
            GGA: 419953(ACE)
            DRE: 565980(LOC565980)
            SPU: 593528(LOC593528)
            DME: Dmel_CG10142(Ance-5) Dmel_CG10593(Acer) Dmel_CG16869(Ance-2)
                 Dmel_CG17988(Ance-3) Dmel_CG8196(Ance-4) Dmel_CG8827(Ance)
            CEL: C42D8.5(acn-1)
            XCC: XCC1116
            XCB: XC_3130
            XCV: XCV1249
            XAC: XAC1217
            XOO: XOO3539
            XOM: XOO_3345(XOO3345)
            SON: SO_2494
            SDN: Sden_2117
            SFR: Sfri_1887
            SAZ: Sama_1817
            SBL: Sbal_2246
            SBM: Shew185_2125
            SLO: Shew_2053
            SSE: Ssed_2057
            SPL: Spea_2340
            SHE: Shewmr4_2051
            SHM: Shewmr7_1924
            SHN: Shewana3_2002 Shewana3_2156
            CPS: CPS_1585
            ADE: Adeh_2024
            AFW: Anae109_1785
            MXA: MXAN_3581
            MMR: Mmar10_1467
            HNE: HNE_1947
            SAL: Sala_0456
            SWI: Swit_2667
            ELI: ELI_07405
            ABA: Acid345_4468
            SUS: Acid_4844
            GVI: gll3143
STRUCTURES  PDB: 1DTD  1J36  1J37  1J38  1O86  1O8A  2C6F  2C6N  2IUL  2IUX  
                 2OC2  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.15.1
            ExPASy - ENZYME nomenclature database: 3.4.15.1
            ExplorEnz - The Enzyme Database: 3.4.15.1
            ERGO genome analysis and discovery system: 3.4.15.1
            BRENDA, the Enzyme Database: 3.4.15.1
            CAS: 9015-82-1
///
ENTRY       EC 3.4.15.2       Obsolete  Enzyme
NAME        Transferred to 3.4.19.2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl-dipeptidases
COMMENT     Transferred entry: now EC 3.4.19.2 peptidyl-glycinamidase (EC
            3.4.15.2 created 1978, deleted 1981)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.15.2
            ExPASy - ENZYME nomenclature database: 3.4.15.2
            ExplorEnz - The Enzyme Database: 3.4.15.2
            ERGO genome analysis and discovery system: 3.4.15.2
            BRENDA, the Enzyme Database: 3.4.15.2
///
ENTRY       EC 3.4.15.3       Obsolete  Enzyme
NAME        Transferred to 3.4.15.5
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl-dipeptidases
COMMENT     Transferred entry: now EC 3.4.15.5 peptidyl-dipeptidase Dcp (EC
            3.4.15.3 created 1981, modified 1989, deleted 1996)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.15.3
            ExPASy - ENZYME nomenclature database: 3.4.15.3
            ExplorEnz - The Enzyme Database: 3.4.15.3
            ERGO genome analysis and discovery system: 3.4.15.3
            BRENDA, the Enzyme Database: 3.4.15.3
///
ENTRY       EC 3.4.15.4                 Enzyme
NAME        peptidyl-dipeptidase B;
            dipeptidyl carboxyhydrolase;
            atriopeptin convertase;
            atrial di-(tri)peptidyl carboxyhydrolase;
            peptidyldipeptidase B;
            atrial dipeptidyl carboxyhydrolase;
            atrial peptide convertase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl-dipeptidases
REACTION    Release of a C-terminal dipeptide or exceptionally a tripeptide
COFACTOR    Zinc [CPD:C00038]
COMMENT     A membrane-bound, zinc metallopeptidase located in mammalian atrial,
            but not ventricular, myocytes. Although it is capable of converting
            the 126-residue atriopeptin III directly to atriopeptin I by
            releasing a C-terminal tripeptide Phe-Arg-Tyr, it is generally
            restricted to the release of dipeptides. In contrast to
            peptidyl-dipeptidase A (EC 3.4.15.1) it displays no Cl- dependence
            and shows no action on angiotensin I. Conversely,
            peptidyl-dipeptidase A is unable to release Phe-Arg from the
            C-terminus of atriopeptin II
REFERENCE   1  [PMID:6385859]
  AUTHORS   Harris RB, Wilson IB.
  TITLE     Atrial tissue contains a metallo dipeptidyl carboxyhydrolase not
            present in ventricular tissue: partial purification and
            characterization.
  JOURNAL   Arch. Biochem. Biophys. 233 (1984) 667-75.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:2999723]
  AUTHORS   Harris RB, Wilson IB.
  TITLE     Conversion of atriopeptin II to atriopeptin I by atrial dipeptidyl
            carboxy hydrolase.
  JOURNAL   Peptides. 6 (1985) 393-6.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:3146555]
  AUTHORS   Soler DF, Harris RB.
  TITLE     Continuous fluorogenic substrates for atrial dipeptidyl
            carboxyhydrolase. Importance of Ser in the P1 position.
  JOURNAL   Int. J. Pept. Protein. Res. 32 (1988) 35-40.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:2501770]
  AUTHORS   Soler DF, Harris RB.
  TITLE     Atrial dipeptidyl carboxyhydrolase is a zinc-metallo proteinase
            which possesses tripeptidyl carboxyhydrolase activity.
  JOURNAL   Peptides. 10 (1989) 63-8.
  ORGANISM  cow [GN:bta]
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.15.4
            ExPASy - ENZYME nomenclature database: 3.4.15.4
            ExplorEnz - The Enzyme Database: 3.4.15.4
            ERGO genome analysis and discovery system: 3.4.15.4
            BRENDA, the Enzyme Database: 3.4.15.4
            CAS: 147014-93-5
///
ENTRY       EC 3.4.15.5                 Enzyme
NAME        peptidyl-dipeptidase Dcp;
            dipeptidyl carboxypeptidase (Dcp);
            dipeptidyl carboxypeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl-dipeptidases
REACTION    Hydrolysis of unblocked, C-terminal dipeptides from oligopeptides,
            with broad specificity. Does not hydrolyse bonds in which P1' is
            Pro, or both P1 and P1' are Gly
COMMENT     Known from Escherichia coli and Salmonella typhimurium. A zinc
            metallopeptidase in peptidase family M3 (thimet oligopeptidase
            family). Ac-Ala!Ala-Ala is a good test substrate [3]. Inhibited by
            captopril, as is peptidyl-dipeptidase A. Formerly EC 3.4.15.3, and
            included in EC 3.4.15.1, peptidyl-dipeptidase A."
REFERENCE   1  [PMID:13271]
  AUTHORS   Yaron A.
  TITLE     Dipeptidyl carboxypeptidase from Escherichia coli.
  JOURNAL   Methods. Enzymol. 45 (1976) 599-610.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:8226676]
  AUTHORS   Henrich B, Becker S, Schroeder U, Plapp R.
  TITLE     dcp gene of Escherichia coli: cloning, sequencing, transcript
            mapping, and characterization of the gene product.
  JOURNAL   J. Bacteriol. 175 (1993) 7290-300.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:7674945]
  AUTHORS   Conlin CA, Miller CG.
  TITLE     Dipeptidyl carboxypeptidase and oligopeptidase A from Escherichia
            coli and Salmonella typhimurium.
  JOURNAL   Methods. Enzymol. 248 (1995) 567-79.
  ORGANISM  Escherichia coli [GN:eco], Salmonella typhimurium
ORTHOLOGY   KO: K01284  peptidyl-dipeptidase Dcp
GENES       LMA: LmjF02.0740 LmjF27.2660
            ECO: b1538(dcp)
            ECJ: JW1531(dcp)
            ECE: Z2160(dcp)
            ECS: ECs2147
            ECC: c1964(dcp)
            ECI: UTI89_C1761(dcp)
            ECP: ECP_1522
            ECW: EcE24377A_1747(dcp)
            ECX: EcHS_A1628
            STY: STY1549(dcp)
            STT: t1433(dcp)
            SPT: SPA1343(dcp)
            SEC: SC1529(dcp)
            STM: STM1512(dcp)
            SFL: SF1557(dcp)
            SFX: S1682(dcp)
            SFV: SFV_1552(dcp)
            SSN: SSON_1590(dcp)
            SBO: SBO_1612(dcp)
            SDY: SDY_1587(dcp)
            ENT: Ent638_1940
            SPE: Spro_2306
            XFA: XF1944
            XFT: PD0856(dcp)
            XCC: XCC0230(dcp) XCC1412(dcp)
            XCB: XC_0240 XC_2826
            XCV: XCV0255(dcp2) XCV1513(dcp)
            XAC: XAC0249(dcp) XAC1456(dcp)
            XOO: XOO0344(dcp) XOO2340(dcp)
            XOM: XOO_0316(XOO0316) XOO_2220(XOO2220) XOO_2221(XOO2221)
            SON: SO_3142(dcp-1) SO_3564(dcp-2)
            SDN: Sden_1597 Sden_3306
            SFR: Sfri_2334 Sfri_3613
            SAZ: Sama_1172 Sama_1564
            SBL: Sbal_2627 Sbal_2629 Sbal_2844
            SBM: Shew185_2661 Shew185_2664 Shew185_2863
            SLO: Shew_2161 Shew_2212 Shew_2581
            SPC: Sputcn32_1612 Sputcn32_2508
            SSE: Ssed_1448 Ssed_2692
            SPL: Spea_1857 Spea_2852
            SHE: Shewmr4_1355 Shewmr4_1525 Shewmr4_2302
            SHM: Shewmr7_1420 Shewmr7_1592 Shewmr7_2372
            SHN: Shewana3_1408 Shewana3_1586 Shewana3_2492
            SHW: Sputw3181_1500 Sputw3181_2410
            ILO: IL1691(dcp)
            CPS: CPS_4267(dcp)
            PHA: PSHAa2184(dcp)
            PAT: Patl_1586 Patl_2786
            DNO: DNO_1351(dcpA) DNO_1352(dcpB)
            CVI: CV_3380(dcp1) CV_3381(dcp2)
            RFR: Rfer_1048
            BBA: Bd3171(dcp)
            ADE: Adeh_3108
            MXA: MXAN_2286(dcp)
            MLO: mlr4139
            MES: Meso_0127
            SME: SMc04403(dcp)
            SMD: Smed_3177
            ATU: Atu2664(dcp)
            ATC: AGR_C_4829
            RLE: RL4507(dcp)
            BME: BMEII0416
            BMF: BAB2_0358(dcp)
            BMS: BRA0878(dcp)
            BMB: BruAb2_0354(dcp)
            BOV: BOV_A0823(dcp)
            OAN: Oant_3302
            BJA: bll7756(dcp)
            BRA: BRADO6258(dcp)
            BBT: BBta_1351(dcp)
            RPA: RPA0872
            RPB: RPB_4545
            RPC: RPC_4839
            RPD: RPD_0858
            RPE: RPE_4804
            NWI: Nwi_0926
            NHA: Nham_3417
            BHE: BH01720(dcp)
            CCR: CC_3702
            SIL: SPO0414
            SIT: TM1040_0465
            RSP: RSP_0596
            RSH: Rsph17029_2249
            RSQ: Rsph17025_0514
            JAN: Jann_0912
            RDE: RD1_1203(dcp)
            PDE: Pden_1944
            MMR: Mmar10_0143
            HNE: HNE_3288(dcp)
            SAL: Sala_3161
            ELI: ELI_07930
            GOX: GOX2134
            CGL: NCgl2219(cgl2301)
            CGB: cg2527(dcp)
            CEF: CE2203
            CDI: DIP1728
            CJK: jk0594(dcp)
            NFA: nfa20170
            CMI: CMM_1468(dcpA)
            ART: Arth_2313
            KRA: Krad_3616
            RBA: RB7940(dcp)
            BTH: BT_2834 BT_4262
            BFR: BF0966 BF3181
            BFS: BF0884(dcp) BF3021
            PGI: PG0758(dcp-1) PG1789(dcp-2)
            GFO: GFO_1952(dcp)
            FJO: Fjoh_1608
            FPS: FP1364(dcp1) FP1883(dcp2)
STRUCTURES  PDB: 1Y79  2GBC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.15.5
            ExPASy - ENZYME nomenclature database: 3.4.15.5
            ExplorEnz - The Enzyme Database: 3.4.15.5
            ERGO genome analysis and discovery system: 3.4.15.5
            BRENDA, the Enzyme Database: 3.4.15.5
            CAS: 9015-82-1
///
ENTRY       EC 3.4.15.6                 Enzyme
NAME        cyanophycinase;
            cyanophycin degrading enzyme;
            beta-Asp-Arg hydrolysing enzyme;
            CGPase;
            CphB;
            CphE;
            cyanophycin granule polypeptidase;
            extracellular CGPase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Peptidyl-dipeptidases
REACTION    [L-Asp(4-L-Arg)]n + H2O = [L-Asp(4-L-Arg)]n-1 + L-Asp(4-L-Arg)
SUBSTRATE   [L-Asp(4-L-Arg)]n;
            H2O [CPD:C00001]
PRODUCT     [L-Asp(4-L-Arg)]n-1;
            L-Asp(4-L-Arg)
COMMENT     The enzyme is highly specific for the branched polypeptide
            cyanophycin and does not hydrolyse poly-L-aspartate or
            poly-L-arginine [3]. A serine-type exopeptidase that belongs in
            peptidase family S51.
REFERENCE   1  [PMID:16000772]
  AUTHORS   Obst M, Krug A, Luftmann H, Steinbuchel A.
  TITLE     Degradation of cyanophycin by Sedimentibacter hongkongensis strain
            KI and Citrobacter amalonaticus strain G Isolated from an anaerobic
            bacterial consortium.
  JOURNAL   Appl. Environ. Microbiol. 71 (2005) 3642-52.
REFERENCE   2  [PMID:11986309]
  AUTHORS   Obst M, Oppermann-Sanio FB, Luftmann H, Steinbuchel A.
  TITLE     Isolation of cyanophycin-degrading bacteria, cloning and
            characterization of an extracellular cyanophycinase gene (cphE) from
            Pseudomonas anguilliseptica strain BI. The cphE gene from P.
            anguilliseptica BI encodes a cyanophycinhydrolyzing enzyme.
  JOURNAL   J. Biol. Chem. 277 (2002) 25096-105.
REFERENCE   3  [PMID:10429200]
  AUTHORS   Richter R, Hejazi M, Kraft R, Ziegler K, Lockau W.
  TITLE     Cyanophycinase, a peptidase degrading the cyanobacterial reserve
            material multi-L-arginyl-poly-L-aspartic acid (cyanophycin):
            molecular cloning of the gene of Synechocystis sp. PCC 6803,
            expression in Escherichia coli, and biochemical characterization of
            the purified enzyme.
  JOURNAL   Eur. J. Biochem. 263 (1999) 163-9.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.15.6
            ExPASy - ENZYME nomenclature database: 3.4.15.6
            ExplorEnz - The Enzyme Database: 3.4.15.6
            ERGO genome analysis and discovery system: 3.4.15.6
            BRENDA, the Enzyme Database: 3.4.15.6
            CAS: 131554-16-0
///
ENTRY       EC 3.4.16.1       Obsolete  Enzyme
NAME        Transferred to 3.4.16.6
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine-type carboxypeptidases
COMMENT     Transferred entry: now EC 3.4.16.6 carboxypeptidase D (EC 3.4.16.1
            created 1972 as EC 3.4.12.1 and EC 3.4.21.13, both transferred 1978
            to EC 3.4.16.1, deleted 1993)
STRUCTURES  PDB: 1WHS  1WHT  3SC2  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.16.1
            ExPASy - ENZYME nomenclature database: 3.4.16.1
            ExplorEnz - The Enzyme Database: 3.4.16.1
            ERGO genome analysis and discovery system: 3.4.16.1
            BRENDA, the Enzyme Database: 3.4.16.1
///
ENTRY       EC 3.4.16.2                 Enzyme
NAME        lysosomal Pro-Xaa carboxypeptidase;
            angiotensinase C;
            lysosomal carboxypeptidase C;
            peptidylprolylamino acid carboxypeptidase;
            aminoacylproline carboxypeptidase;
            prolyl carboxypeptidase;
            carboxypeptidase P;
            proline-specific carboxypeptidase P;
            PCP;
            lysosomal Pro-Xaa carboxypeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine-type carboxypeptidases
REACTION    Cleavage of a -Pro!Xaa bond to release a C-terminal amino acid
INHIBITOR   Isoflurophate [CPD:C00202]
COMMENT     A lysosomal peptidase active at acidic pH that inactivates
            angiotensin II. Inhibited by diisopropyl fluorophosphate. In
            peptidase family S28 (Pro-X carboxypeptidase family).
REFERENCE   1  [PMID:6991912]
  AUTHORS   Walter R, Simmons WH, Yoshimoto T.
  TITLE     Proline specific endo- and exopeptidases.
  JOURNAL   Mol. Cell. Biochem. 30 (1980) 111-27.
  ORGANISM  human [GN:hsa], pig [GN:ssc]
REFERENCE   2  [PMID:7341916]
  AUTHORS   Odya CE, Erdos EG.
  TITLE     Human prolylcarboxypeptidase.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 460-6.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01285  lysosomal Pro-X carboxypeptidase
GENES       HSA: 5547(PRCP)
            PTR: 451453(PRCP)
            MMU: 72461(Prcp)
            RNO: 293118(Prcp_predicted)
            CFA: 476788(PRCP)
            BTA: 534927(MGC134276)
            DRE: 436967(zgc:91816)
            SPU: 578398(LOC578398)
            DME: Dmel_CG2493
            OSA: 4325498 4341667
            DDI: DDBDRAFT_0188558
            TET: TTHERM_01018340 TTHERM_01085520
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.16.2
            ExPASy - ENZYME nomenclature database: 3.4.16.2
            ExplorEnz - The Enzyme Database: 3.4.16.2
            ERGO genome analysis and discovery system: 3.4.16.2
            BRENDA, the Enzyme Database: 3.4.16.2
            CAS: 9075-64-3
///
ENTRY       EC 3.4.16.3       Obsolete  Enzyme
NAME        Transferred to 3.4.16.5
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine-type carboxypeptidases
COMMENT     Transferred entry: Now included with EC 3.4.16.5, carboxypeptidase C
            (EC 3.4.16.3 created 1972 as EC 3.4.12.12, transferred 1978 to EC
            3.4.16.3, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.16.3
            ExPASy - ENZYME nomenclature database: 3.4.16.3
            ExplorEnz - The Enzyme Database: 3.4.16.3
            ERGO genome analysis and discovery system: 3.4.16.3
            BRENDA, the Enzyme Database: 3.4.16.3
///
ENTRY       EC 3.4.16.4                 Enzyme
NAME        serine-type D-Ala-D-Ala carboxypeptidase;
            DD-peptidase;
            D-alanyl-D-alanine-carboxypeptidase;
            D-alanyl-D-alanine-cleaving-peptidase;
            D-alanyl-D-alanine-cleaving peptidase;
            DD-transpeptidase;
            D-alanine carboxypeptidase;
            DD-carboxypeptidase;
            D-alanyl carboxypeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine-type carboxypeptidases
REACTION    Preferential cleavage: (Ac)2-L-Lys-D-Ala!D-Ala. Also
            transpeptidation of peptidyl-alanyl moieties that are N-acyl
            substituents of D-alanine
INHIBITOR   Penicillin [CPD:C00395];
            beta-Lactam antibiotics [CPD:C03438]
COMMENT     A membrane-bound, bacterial enzyme inhibited by penicillin and other
            beta-lactam antibiotics, which acylate the active site serine.
            Examples are known from peptidase families S11, S12 and S13.
            Distinct from EC 3.4.17.14, zinc D-Ala-D-Ala carboxypeptidase
REFERENCE   1  [PMID:6597561]
  AUTHORS   Ghuysen JM, Frere JM, Leyh-Bouille M, Nguyen-Disteche M, Coyette J,
            Dusart J, Joris B, Duez C, Dideberg O, Charlier P, et al.
  TITLE     Bacterial wall peptidoglycan, DD-peptidases and beta-lactam
            antibiotics.
  JOURNAL   Scand. J. Infect. Dis. Suppl. 42 (1984) 17-37.
REFERENCE   2  [PMID:3888533]
  AUTHORS   Frere JM, Joris B.
  TITLE     Penicillin-sensitive enzymes in peptidoglycan biosynthesis.
  JOURNAL   Crit. Rev. Microbiol. 11 (1985) 299-396.
ORTHOLOGY   KO: K01286  D-alanyl-D-alanine carboxypeptidase
            KO: K07258  D-alanyl-D-alanine carboxypeptidase (penicillin binding
                        protein 5/6)
            KO: K07259  D-alanyl-D-alanine carboxypeptidase /
                        D-alanyl-D-alanine-endopeptidase (penicillin binding
                        protein 4)
            KO: K07260  D-alanyl-D-alanine carboxypeptidase
GENES       UMA: UM00660.1
            DDI: DDBDRAFT_0168572
            TET: TTHERM_00355840 TTHERM_00732760 TTHERM_00923230
                 TTHERM_01284710
            ECO: b0632(dacA) b0839(dacC) b2010(dacD) b3182(dacB)
            ECJ: JW0627(dacA) JW0823(dacC) JW3149(dacB)
            ECE: Z0777(dacA) Z1066(dacC) Z3171(dacD) Z4544(dacB)
            ECS: ECs0670 ECs0919 ECs2812 ECs4061
            ECC: c0722(dacA) c0924(dacC) c2538(dacD) c3939(dacB)
            ECI: UTI89_C0634(dacA) UTI89_C0842(dacC) UTI89_C3615(dacB)
            ECP: ECP_0662 ECP_0853 ECP_2054 ECP_3269
            ECV: APECO1_1254(dacC) APECO1_1423(dacA) APECO1_3250(dacB)
            ECW: EcE24377A_0657(dacA) EcE24377A_0910(dacC)
                 EcE24377A_2301(dacD) EcE24377A_3667(dacB)
            ECX: EcHS_A0900 EcHS_A2148 EcHS_A3374
            STY: STY0688(dacA) STY0896(dacC) STY2268(yeeC) STY3479
            STT: t2033(dacC) t2230(dacA) t3217
            SPT: SPA1899(dacC) SPA2097(dacA) SPA3167(dacB)
            SEC: SC0666(dacA) SC0857(dacC) SC2071(dacD) SC3238(dacB)
            STM: STM0637(dacA) STM0863(dacC) STM2062(dacD) STM3300(dacB)
            YPE: YPO1320(dacC) YPO2601(dacA) YPO3054 YPO3506(dacB)
            YPK: y0678(dacB) y1175(dacA) y1426 y2864(dacC)
            YPM: YP_0577(dacB) YP_1112(dacA) YP_1272(dacC) YP_2676(vanY)
            YPA: YPA_0056 YPA_1037 YPA_2245 YPA_2498
            YPN: YPN_1086 YPN_1331 YPN_2659 YPN_3250
            YPP: YPDSF_2376 YPDSF_2652 YPDSF_3555
            YPS: YPTB0470(dacB) YPTB1094(dacA) YPTB1351(dacC) YPTB2776
            YPI: YpsIP31758_3606(dacB)
            YEN: YE1471(dacC)
            SFL: SF0649(dacA) SF0789(dacC) SF3222(dacB)
            SFX: S0671(dacA) S3440(dacB)
            SFV: SFV_0694(dacA) SFV_3212(dacB)
            SSN: SSON_0586(dacA) SSON_2080(dacD) SSON_3330(dacB)
            SBO: SBO_0496(dacA) SBO_3200(dacB)
            SDY: SDY_0554(dacA) SDY_0841(dacC) SDY_2233(dacD) SDY_3363(dacB)
            ECA: ECA0694(dacD) ECA1290 ECA1300(dacA) ECA2686(dacC)
            PLU: plu1294(dacA) plu1573(dacC) plu2723 plu4539(dacB)
            WBR: WGLp174(dacA)
            SGL: SG0795 SG0921 SG1719
            ENT: Ent638_1167 Ent638_1330 Ent638_2578 Ent638_3616
            KPN: KPN_00871(dacC)
            SPE: Spro_0479 Spro_1198 Spro_1628 Spro_2636
            HIN: HI0029(dacA) HI1330(dacB)
            HIT: NTHI0036(dacA) NTHI0181 NTHI1655(dacB)
            HIP: CGSHiEE_04965
            HDU: HD0641 HD2016(dacA)
            HSO: HS_0318(dacA) HS_0579
            PMU: PM0716(dacB) PM1021 PM1927(dacA)
            MSU: MS0675(vanY) MS0960(dacB) MS1829(dacC)
            APL: APL_0420(pbpG) APL_0945(dacB) APL_1596(dacA) APL_1872
            ASU: Asuc_0700 Asuc_1456
            XFA: XF0881 XF1614 XF2230
            XFT: PD1277(dacC) PD1799
            XCC: XCC1132 XCC3456(dacC)
            XCB: XC_0708 XC_3111
            XCV: XCV0725(dacC) XCV1265
            XAC: XAC0664(dacC) XAC1233
            XOO: XOO3523 XOO3956(dacC)
            XOM: XOO_3329(XOO3329) XOO_3734(XOO3734)
            VCH: VC0632 VC0947 VC2153 VCA0270
            VCO: VC0395_0960(dacA-2) VC0395_A0161(dacB) VC0395_A0470(dacA-1)
            VVU: VV1_0281 VV1_1685 VV1_1915 VV2_1681
            VVY: VV0903 VV2501 VV2721 VVA0500
            VPA: VP0719 VP2270 VP2468 VPA1296 VPA1594
            VFI: VF0474 VF0745 VF1915
            PPR: PBPRA0599 PBPRA0843 PBPRA1842 PBPRA2893 PBPRB0791
            PAE: PA3047 PA3999(dacC)
            PAU: PA14_12100(dacC) PA14_24690(dacB)
            PAP: PSPA7_2091(dacB)
            PPU: PP_2098(dacB) PP_4803(dacA)
            PPF: Pput_4678
            PST: PSPTO_2314(dacB) PSPTO_4821
            PSB: Psyr_2111 Psyr_4361
            PSP: PSPPH_2081(dacB) PSPPH_4402
            PFL: PFL_1880(dacB) PFL_5448
            PFO: Pfl_1790 Pfl_4966
            PEN: PSEEN3770(dacB) PSEEN4822(dacC)
            PMY: Pmen_0066 Pmen_3008 Pmen_3794
            PAR: Psyc_0687(dacC)
            PCR: Pcryo_0436 Pcryo_0658
            PRW: PsycPRwf_1758
            ACI: ACIAD1184 ACIAD1225(dacC)
            SON: SO_1164(dacA-1) SO_2394(dacB) SO_2472
            SDN: Sden_0851 Sden_1778 Sden_1813
            SFR: Sfri_0695 Sfri_1764 Sfri_1920
            SAZ: Sama_1744 Sama_2592
            SBL: Sbal_2078 Sbal_3279
            SBM: Shew185_2271 Shew185_3321
            SLO: Shew_1962 Shew_2939 Shew_3053
            SPC: Sputcn32_2034 Sputcn32_2873
            SSE: Ssed_2291 Ssed_3489
            SPL: Spea_2082 Spea_3153
            SHE: Shewmr4_0987 Shewmr4_1932
            SHM: Shewmr7_1052 Shewmr7_2044
            SHN: Shewana3_0991 Shewana3_1911 Shewana3_1985
            SHW: Sputw3181_1030 Sputw3181_1979
            ILO: IL0957(dacA) IL1456
            CPS: CPS_1712(dacA) CPS_3180
            PHA: PSHAa1022(dacA) PSHAa1330
            PAT: Patl_1556 Patl_2193 Patl_2539
            SDE: Sde_3337 Sde_3368
            PIN: Ping_3027 Ping_3293
            MAQ: Maqu_2196 Maqu_2410
            CBU: CBU_0009(dacB) CBU_1261
            CBD: COXBU7E912_0134(dacB)
            LPN: lpg1118 lpg1470 lpg1509 lpg1910 lpg2589(dacB) lpg2919
            LPF: lpl1123 lpl1517 lpl1874 lpl2512
            LPP: lpp1119 lpp1426 lpp1466 lpp1885 lpp2642
            MCA: MCA0105 MCA2619
            FTU: FTT1029(dacD) FTT1039(dacB)
            FTF: FTF1029(dacD) FTF1039(dacB1)
            FTW: FTW_0936 FTW_0948(dacB1) FTW_0992 FTW_1514(dacB2)
            FTL: FTL_1004 FTL_1046 FTL_1060
            FTH: FTH_1025(dacB) FTH_1036
            FTA: FTA_1106(dacB1) FTA_1593(dacB2)
            FTN: FTN_0907 FTN_0917 FTN_0967(vanY)
            TCX: Tcr_0793 Tcr_1635
            NOC: Noc_2632
            AEH: Mlg_0176 Mlg_1692
            HHA: Hhal_1012
            HCH: HCH_05839
            CSA: Csal_0150 Csal_1549 Csal_2931
            ABO: ABO_1959(dacA) ABO_1965(dacB)
            MMW: Mmwyl1_2844
            AHA: AHA_1477 AHA_2624(dacB) AHA_3259
            DNO: DNO_0129(dacB) DNO_0899
            BCI: BCI_0641(dacB)
            RMA: Rmag_0470
            VOK: COSY_0433
            NME: NMB0877 NMB1797
            NMA: NMA0665 NMA1095
            NMC: NMC0818
            NGO: NGO0107 NGO0443
            CVI: CV_1125(dacB) CV_3094(dacC)
            RSO: RSc0327(dac) RSc0584(RS04879)
            REU: Reut_A0280 Reut_A0564
            REH: H16_A0302(dac) H16_A1386
            RME: Rmet_0225 Rmet_0508
            BMA: BMA0058 BMA0307(dacB) BMAA1081
            BMV: BMASAVP1_A0224 BMASAVP1_A0602(dacB)
            BML: BMA10299_A1369 BMA10299_A2436(dacB)
            BMN: BMA10247_0050(dacB) BMA10247_3192
            BXE: Bxe_A0698 Bxe_A4218
            BVI: Bcep1808_2734 Bcep1808_2989
            BUR: Bcep18194_A5950 Bcep18194_A6236 Bcep18194_B1275
                 Bcep18194_C7182
            BCN: Bcen_2008 Bcen_2278
            BCH: Bcen2424_2619 Bcen2424_2893
            BAM: Bamb_2666 Bamb_2943 Bamb_6304
            BPS: BPSL0408 BPSL0805 BPSS1239
            BPM: BURPS1710b_0620(dac) BURPS1710b_1009(dacB)
                 BURPS1710b_A0238(dac)
            BPL: BURPS1106A_0458 BURPS1106A_0849(dacB)
            BPD: BURPS668_0438 BURPS668_0844(dacB)
            BTE: BTH_I0380 BTH_I0672
            BPE: BP0102 BP1051
            BPA: BPP0166 BPP1148
            BBR: BB0168 BB1364
            RFR: Rfer_0191 Rfer_0920 Rfer_3801
            POL: Bpro_0250 Bpro_4622
            PNA: Pnap_0197 Pnap_3847
            AAV: Aave_0332
            AJS: Ajs_0272
            VEI: Veis_1254
            MPT: Mpe_A0300 Mpe_A0311
            HAR: HEAR0634 HEAR0817(pbpG) HEAR1504 HEAR1716 HEAR2999(dacC)
            MMS: mma_0600 mma_3248
            NEU: NE0053 NE1485(dac)
            NET: Neut_0223 Neut_0761
            NMU: Nmul_A1991 Nmul_A2367
            EBA: ebA2281 ebA3044
            AZO: azo0180(dacC) azo3656(dacB)
            DAR: Daro_0291 Daro_0423
            TBD: Tbd_0101 Tbd_0266 Tbd_0647
            MFA: Mfla_0378 Mfla_2497
            WSU: WS0721
            ABU: Abu_0114(dacA)
            GUR: Gura_4141
            DVU: DVU2655 DVU3196
            DVL: Dvul_0599
            DDE: Dde_0064
            LIP: LI0914(dacC)
            BBA: Bd2044(dacA) Bd3244(dacB)
            DPS: DP2814
            ADE: Adeh_3807
            AFW: Anae109_3925
            MXA: MXAN_1070(dacB)
            SAT: SYN_02260
            SFU: Sfum_1305 Sfum_2719 Sfum_2754
            RPR: RP389(dacF)
            RTY: RT0377(dacF)
            RCO: RC0536(dacF)
            RFE: RF_0609(dacF)
            RBE: RBE_0931(dacF)
            WOL: WD0098
            WBM: Wbm0290
            AMA: AM1091
            APH: APH_1214
            ERU: Erum8220(dacF)
            ERW: ERWE_CDS_08710(dacF)
            ERG: ERGA_CDS_08610(dacF)
            ECN: Ecaj_0859
            ECH: ECH_1067
            PUB: SAR11_0998(dacC)
            MLO: mll0426 mll3581 mlr0666 mlr4960
            MES: Meso_0634 Meso_1371 Meso_1580 Meso_3057
            PLA: Plav_2796 Plav_3109
            SME: SMc00068 SMc00683 SMc00996 SMc01188(dac)
            SMD: Smed_0506 Smed_1040 Smed_1293 Smed_2572
            ATU: Atu1499(dac) Atu1505(dac) Atu2321 Atu3634(dacF)
            ATC: AGR_C_2763 AGR_C_2773 AGR_C_4221(dacF) AGR_L_2387(dacF)
            RET: RHE_CH00944(dacF1) RHE_CH02161(dac) RHE_CH02211(ypch00722)
                 RHE_CH02344 RHE_CH03832(dacF2)
            RLE: RL1016 RL2477(dacF) RL2541 RL2656 RL4363(dacC)
            BME: BMEI0035 BMEI0814 BMEI0913 BMEI0914 BMEI0990 BMEII0350
            BMF: BAB1_1010 BAB1_1094 BAB1_1193 BAB1_2037
            BMS: BR0991 BR1072 BR1172 BR2036
            BMB: BruAb1_0997 BruAb1_1077 BruAb1_1178 BruAb1_2011 BruAb2_0286
            BOV: BOV_0959 BOV_1129
            OAN: Oant_0902 Oant_2019 Oant_2076 Oant_2155
            BJA: bll1320 bll4519(dac) blr5156
            BRA: BRADO2994 BRADO3826 BRADO4549
            BBT: BBta_4103 BBta_4777 BBta_5173
            RPA: RPA2774 RPA3150 RPA4266
            RPB: RPB_1345 RPB_2393 RPB_2678
            RPC: RPC_2702 RPC_3328 RPC_4073
            RPD: RPD_1324 RPD_2714 RPD_3058
            RPE: RPE_1708 RPE_2864 RPE_3407
            NWI: Nwi_1465 Nwi_1699 Nwi_2682
            NHA: Nham_2011 Nham_2420 Nham_3735
            BHE: BH06160(dacA1) BH08450(dacA2) BH16300(dacA3)
            BQU: BQ06120(dacA1) BQ07070(dacA2) BQ13220(dacA3)
            XAU: Xaut_1925 Xaut_4324 Xaut_4539
            CCR: CC_2161
            SIL: SPO0451(dacB) SPO2739 SPO3658
            SIT: TM1040_2259 TM1040_2536 TM1040_3590
            RSP: RSP_0550 RSP_0582 RSP_0688 RSP_3246
            RSH: Rsph17029_2201 Rsph17029_2343
            RSQ: Rsph17025_0542 Rsph17025_1237
            JAN: Jann_1278 Jann_3631 Jann_3849
            RDE: RD1_1244(dacB) RD1_1278(dacA) RD1_3465(dacC)
            PDE: Pden_1757 Pden_2143
            MMR: Mmar10_1283 Mmar10_1455
            HNE: HNE_0402(dacB) HNE_1025 HNE_1814
            ZMO: ZMO1089(dacC)
            NAR: Saro_1942
            SAL: Sala_1256
            SWI: Swit_0483 Swit_1363
            ELI: ELI_06210
            GOX: GOX0019 GOX0607 GOX1238
            GBE: GbCGDNIH1_1072 GbCGDNIH1_1651
            ACR: Acry_0248 Acry_2838
            RRU: Rru_A0132 Rru_A1704 Rru_A2113
            MAG: amb1118 amb2451
            MGM: Mmc1_0042 Mmc1_1471
            ABA: Acid345_4495
            SUS: Acid_1026
            BSU: BG10074(dacA) BG10295(dacF) BG10527(dacB) BG10969(dacC)
                 BG13538(yodJ)
            BHA: BH0021(dacA) BH1535(dacF) BH1573 BH1810 BH2877(dacB)
            BAN: BA0009(dacA) BA1286 BA1490 BA1743 BA1950 BA2070 BA2526 BA2559
                 BA3033(adP-2) BA4297(dacF) BA4750 BA5104 BA5252 BA5639
            BAR: GBAA0009(dacA) GBAA1286 GBAA1490 GBAA1743 GBAA1950 GBAA2070
                 GBAA2526 GBAA2559 GBAA3033(adP-2) GBAA4297(dacF) GBAA4750
                 GBAA5104 GBAA5252 GBAA5639
            BAA: BA_0115 BA_0495 BA_0604 BA_1815 BA_2013 BA_2255 BA_2452
                 BA_2566(vanY) BA_3020(vanY) BA_3542 BA_4756 BA_5181(vanY)
                 BA_5522(vanY)
            BAT: BAS0012 BAS1190 BAS1379 BAS1617 BAS1810 BAS1923 BAS2349
                 BAS2382 BAS2819 BAS3986 BAS4410 BAS4743 BAS4878 BAS5240
            BCE: BC0014 BC1277 BC1469 BC1690 BC1951 BC2052 BC2448 BC2496
                 BC3013 BC3119 BC3307 BC4075 BC4514 BC4847 BC5005 BC5389
            BCA: BCE_0010(dacA) BCE_1388 BCE_1594 BCE_1820 BCE_2034 BCE_2141
                 BCE_2529(dacA) BCE_2562 BCE_3069(adP) BCE_4145(dacF) BCE_4641
                 BCE_5008 BCE_5147 BCE_5518
            BCZ: BCZK0010(dacA) BCZK1171(dacF) BCZK1351(dacB) BCZK1569
                 BCZK1767(dacA) BCZK1875 BCZK2051 BCZK2266 BCZK2300(dacA)
                 BCZK2409 BCZK2755(adp) BCZK2860(adp) BCZK2932(pbp)
                 BCZK3832(dacF) BCZK4261(dacF) BCZK4603(vanY) BCZK4735(vanY)
                 BCZK5087
            BCY: Bcer98_0009 Bcer98_0998 Bcer98_1193 Bcer98_1490 Bcer98_1813
                 Bcer98_2774 Bcer98_3599 Bcer98_3910
            BTK: BT9727_0010(dacA) BT9727_1169(dacF) BT9727_1352(dacB)
                 BT9727_1578 BT9727_1784(dacA) BT9727_1885 BT9727_2053
                 BT9727_2339(dacA) BT9727_2769(adp) BT9727_3816(dacF)
                 BT9727_4249(dacF) BT9727_4581(vanY) BT9727_4720(vanY)
                 BT9727_5070
            BTL: BALH_0010(dacA) BALH_1139(dacF) BALH_1325(dacB)
                 BALH_1727(dacA) BALH_1829 BALH_2246(dacA) BALH_2271
                 BALH_2300(dacA) BALH_2918(vanY) BALH_2998(adp) BALH_3693(dacF)
                 BALH_4098(dacF) BALH_4414(vanY) BALH_4548(vanY)
                 BALH_4888(pbp4)
            BLI: BL00775(dacF) BL01438(yodJ) BL01881(dacB) BL01997(dacC)
                 BL02352(dacA) BL05330
            BLD: BLi00015(dacA) BLi02133(dacC) BLi02284(yodJ) BLi02465(dacB)
                 BLi02498(dacF) BLi03478
            BCL: ABC0012(dacA) ABC0801 ABC1175 ABC1792(dacF) ABC1828(dacB)
                 ABC2694(dacC)
            BAY: RBAM_000130 RBAM_002160(ybbE) RBAM_019410(yodJ) RBAM_021330
                 RBAM_021590
            BPU: BPUM_0505 BPUM_1807 BPUM_1883(yodJ) BPUM_2052 BPUM_2079
            OIH: OB0011 OB0530 OB1342 OB1826(dacB) OB1842(dacF) OB3145
            GKA: GK0010 GK1581 GK2286 GK2311
            GTN: GTNG_0010
            SAU: SA0598(pbp4)
            SAV: SAV0642(pbp4)
            SAM: MW0604(pbp4)
            SAR: SAR0652(pbp4)
            SAS: SAS0608
            SAC: SACOL0033(mecA) SACOL0699(pbp4)
            SAB: SAB0592c(pbp4)
            SAA: SAUSA300_0032(mecA) SAUSA300_0629(pbp4)
            SAO: SAOUHSC_00646
            SAJ: SaurJH9_0665
            SAH: SaurJH1_0680
            SEP: SE0034 SE0035
            SER: SERP2521(mecA)
            SHA: SH0186 SH0303 SH2254(pbp4)
            SSP: SSP0884 SSP2077
            LMO: lmo1855 lmo2754
            LMF: LMOf2365_1883 LMOf2365_2742
            LIN: lin1969 lin2897
            LWE: lwe1874 lwe2701
            LLA: L139168(dacA) L175147(dacB)
            LLC: LACR_1023 LACR_2600
            LLM: llmg_1578(dacB) llmg_2560(dacA)
            SPY: SPy_0292(dacA) SPy_1093 SPy_1765
            SPZ: M5005_Spy_0247 M5005_Spy_0248(dacA2) M5005_Spy_0383
                 M5005_Spy_0817(dacA1) M5005_Spy_1502
            SPM: spyM18_0279 spyM18_0280(dacA) spyM18_1051 spyM18_1835
            SPG: SpyM3_0213 SpyM3_0214(dacA) SpyM3_0755 SpyM3_1535
            SPS: SPs0219 SPs0220 SPs0331 SPs0956
            SPH: MGAS10270_Spy0247 MGAS10270_Spy0248(dacA2)
                 MGAS10270_Spy0933(dacA1) MGAS10270_Spy1570
            SPI: MGAS10750_Spy0244 MGAS10750_Spy0245(dacA2)
                 MGAS10750_Spy0968(dacA1) MGAS10750_Spy1562
            SPJ: MGAS2096_Spy0266 MGAS2096_Spy0267 MGAS2096_Spy0268
                 MGAS2096_Spy0269(dacA2) MGAS2096_Spy0891(dacA1)
                 MGAS2096_Spy1530
            SPK: MGAS9429_Spy0249 MGAS9429_Spy0250(dacA2)
                 MGAS9429_Spy0936(dacA1) MGAS9429_Spy1504
            SPF: SpyM50225 SpyM50226 SpyM50343
            SPA: M6_Spy0278 M6_Spy0279 M6_Spy0815 M6_Spy1496
            SPB: M28_Spy0242 M28_Spy0243(dacA2) M28_Spy0369 M28_Spy0794(dacA1)
                 M28_Spy1491
            SPN: SP_0629 SP_0872
            SPR: spr0554 spr0776(dacA)
            SPD: SPD_0767(dacC)
            SAG: SAG0093 SAG0146 SAG0147
            SAN: gbs0092 gbs0142 gbs0143
            SAK: SAK_0143 SAK_0204 SAK_0205
            SMU: SMU.253(dacA) SMU.75
            STC: str0078 str0080(dacA1) str0116(dacB)
            STL: stu0080(dacA1) stu0116(dacB)
            STE: STER_0113
            SSA: SSA_0747(dacA) SSA_1277 SSA_1366 SSA_1951(pbp3) SSA_2014
            SSU: SSU05_1870
            SSV: SSU98_1874
            SGO: SGO_0393 SGO_0843 SGO_1585 SGO_1717(pbp3)
            LPL: lp_1010(dacB) lp_1171(pbpX1) lp_1278(dacA2) lp_2021(pbpX2)
                 lp_3189(dacA1)
            LJO: LJ0685
            LAC: LBA1603(vanY)
            LSA: LSA0101 LSA0279(dacA)
            LSL: LSL_0075(dacC) LSL_1532(dacC)
            LDB: Ldb1555(dacA)
            LBU: LBUL_1444
            LBR: LVIS_0271 LVIS_0571 LVIS_1825 LVIS_1826 LVIS_2055
            LCA: LSEI_0221 LSEI_1805
            LGA: LGAS_0465
            LRE: Lreu_1540 Lreu_1842
            PPE: PEPE_1715
            EFA: EF2297(vanYB) EF3129
            OOE: OEOE_0719 OEOE_1065
            LME: LEUM_0292
            STH: STH1075 STH1585 STH1815 STH2021 STH2375 STH2587
            CAC: CAC0993(dacF) CAC1267(dacB) CAC2057 CAC2063(dacF) CAC3297
            CPE: CPE1379 CPE1801(dacB) CPE1806(dacF) CPE1976(dacF)
                 CPE2121(dacF)
            CPF: CPF_1631 CPF_2056 CPF_2061(dacF) CPF_2231 CPF_2376(dacF)
            CPR: CPR_1371 CPR_1770 CPR_1775 CPR_1943 CPR_2088
            CTC: CTC00981 CTC01525 CTC01530 CTC02051
            CNO: NT01CX_0071 NT01CX_1621 NT01CX_2026 NT01CX_2036
            CTH: Cthe_0272 Cthe_0679 Cthe_1171 Cthe_1231 Cthe_1899 Cthe_3179
            CDF: CD0515 CD1291(dacF) CD2498 CD2504 CD3601
            CBO: CBO0609 CBO1033 CBO1853(dacB) CBO1859(dacF) CBO2979
            CBA: CLB_1789(dacB) CLB_1795(dacF)
            CBH: CLC_1796(dacB) CLC_1802(dacF)
            CBF: CLI_1855(dacB) CLI_1861(dacF)
            CBE: Cbei_0519 Cbei_0941 Cbei_1874 Cbei_1879
            CKL: CKL_0025 CKL_0887(dacA1) CKL_1253(dacA2) CKL_1458(dacA3)
            AMT: Amet_2319 Amet_2528 Amet_2643 Amet_3427
            CHY: CHY_1147 CHY_1962 CHY_2101
            DSY: DSY1096 DSY2305 DSY2507 DSY3708
            DRM: Dred_0649 Dred_1102 Dred_1234 Dred_1606 Dred_2952
            SWO: Swol_0612 Swol_0909
            CSC: Csac_1744 Csac_1820 Csac_1845
            TTE: TTE0925(dacC) TTE1314(dacC2) TTE1328(dacC3)
            MTA: Moth_1058 Moth_1357 Moth_1499
            MTU: Rv2911(dacB2) Rv3330(dacB1) Rv3627c
            MTC: MT2979(dacB) MT3433 MT3729
            MBO: Mb2935(dacB2) Mb3363(dacB1) Mb3651c
            MBB: BCG_2932(dacB2) BCG_3400(dacB1)
            MLE: ML0211 ML0691
            MPA: MAP0436 MAP2979(dacB) MAP3448
            MAV: MAV_0529(dacB)
            MSM: MSMEG_2433 MSMEG_6113(dacB)
            MVA: Mvan_1562 Mvan_2184 Mvan_3027
            MGI: Mflv_4179 Mflv_4869
            MMC: Mmcs_0342 Mmcs_1216 Mmcs_1962 Mmcs_4094 Mmcs_4778 Mmcs_5360
            MKM: Mkms_1233 Mkms_2008 Mkms_4170 Mkms_5451
            MJL: Mjls_1243 Mjls_1942 Mjls_4325 Mjls_5738
            CGL: NCgl0650(cgl0680) NCgl2606(cgl2699)
            CGB: cg0060(pbpA) cg0782(dac) cg2199(pbp) cg2987(dacB)
            CEF: CE0699 CE2545
            CDI: DIP0637 DIP2005
            CJK: jk0275(pbp4)
            NFA: nfa13570 nfa3860 nfa9380
            RHA: RHA1_ro00199 RHA1_ro02598 RHA1_ro04401 RHA1_ro06243
                 RHA1_ro06929
            SCO: SCO3408(SCE9.15c) SCO3811(dacA) SCO4847(SC5G8.15c)
                 SCO6131(SC9B2.18c) SCO7050(SC4G1.16c)
            SMA: SAV1311(dacA) SAV3413(dacB) SAV4379(dacD) SAV4662(dacE)
                 SAV5913(dacF)
            TWH: TWT327(dacB)
            TWS: TW444
            LXX: Lxx04140(pbp) Lxx11900(pbpA)
            CMI: CMM_0931(pbpE) CMM_2067(dacB)
            ART: Arth_2647 Arth_3436
            AAU: AAur_0131(dacB)
            PAC: PPA0257
            TFU: Tfu_2903
            FRA: Francci3_0664 Francci3_4311
            FAL: FRAAL1173 FRAAL6585
            ACE: Acel_0200 Acel_0393
            KRA: Krad_0368 Krad_1969 Krad_2625
            SEN: SACE_5713(dacC) SACE_6587
            STP: Strop_2043 Strop_2464 Strop_2475 Strop_3984
            BLO: BL1679
            BAD: BAD_0407
            RXY: Rxyl_2298 Rxyl_2970
            FNU: FN0060
            CTR: CT551(dacC)
            CTA: CTA_0601(dacC)
            CMU: TC0839
            CPN: CPn0672(dacF)
            CPA: CP0075
            CPJ: CPj0672(dacF)
            CPT: CpB0698(dacB)
            CCA: CCA00067
            CAB: CAB069
            CFE: CF0937(dacF)
            PCU: pc0394(dac)
            BBU: BB0582 BB0605(dacA)
            BGA: BG0594 BG0618(dacA)
            BAF: BAPKO_0613 BAPKO_0638(dacA)
            TPA: TP0221 TP0800(dacC)
            TDE: TDE0633 TDE0979
            LIL: LA3947
            LIC: LIC13152(dac)
            LBJ: LBJ_0406
            LBL: LBL_2671
            SYN: sll0777 slr0646(dacB) slr0804(dacB) slr1924
            SYW: SYNW1098 SYNW1250(dacB)
            SYC: syc2160_c(dacB) syc2418_c(vanY)
            SYF: Synpcc7942_1672 Synpcc7942_1934
            SYD: Syncc9605_1241 Syncc9605_1367
            SYE: Syncc9902_1111 Syncc9902_1238
            SYG: sync_1283 sync_1364
            SYR: SynRCC307_1194(dacB)
            SYX: SynWH7803_1266(dacB)
            CYA: CYA_0032 CYA_0671
            CYB: CYB_1058 CYB_2287
            TEL: tll0932 tll1375
            GVI: glr0698 glr2377
            ANA: all3702 alr1666
            AVA: Ava_0669 Ava_2656 Ava_3580
            PMA: Pro0833(vanY) Pro0951(dacB)
            PMM: PMM0761 PMM0885(dacB)
            PMT: PMT0576 PMT0720(dacB)
            PMN: PMN2A_0165 PMN2A_0325
            PMI: PMT9312_0769 PMT9312_0915
            PMB: A9601_09761(dacB)
            PMC: P9515_09671(dacB)
            PMF: P9303_14981(dacB) P9303_16751(vanY)
            PMG: P9301_09741(dacB)
            PME: NATL1_07971 NATL1_09981(dacB)
            TER: Tery_4167 Tery_4445
            BTH: BT_3187
            BFR: BF0025
            BFS: BF0024(dacB)
            PGI: PG1422(dacB)
            SRU: SRU_1078(dacB) SRU_1748(dacB)
            CHU: CHU_1364(dacB)
            GFO: GFO_2757(dacB)
            CTE: CT1265(dacA)
            CCH: Cag_1081
            CPH: Cpha266_1420
            PVI: Cvib_0747
            PLT: Plut_0916
            RCA: Rcas_2208
            DRA: DR_0176
            DGE: Dgeo_0147
            MAC: MA1969
            PTO: PTO0015
STRUCTURES  PDB: 1CEF  1CEG  1ES2  1ES3  1ES4  1ES5  1ESI  1HD8  1HVB  1IKG  
                 1IKI  1J9M  1MPL  1NJ4  1NZO  1NZU  1PW1  1PW8  1PWC  1PWD  
                 1PWG  1SCW  1SDE  1SDN  1SKF  1W5D  1W79  1W8Q  1W8Y  1XP4  
                 1YQS  1Z6F  2BCF  2EX2  2EX6  2EX8  2EX9  2EXA  2EXB  3PTE  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.16.4
            ExPASy - ENZYME nomenclature database: 3.4.16.4
            ExplorEnz - The Enzyme Database: 3.4.16.4
            ERGO genome analysis and discovery system: 3.4.16.4
            BRENDA, the Enzyme Database: 3.4.16.4
            CAS: 9077-67-2
///
ENTRY       EC 3.4.16.5                 Enzyme
NAME        carboxypeptidase C;
            carboxypeptidase Y;
            serine carboxypeptidase I;
            cathepsin A;
            lysosomal protective protein;
            deamidase;
            lysosomal carboxypeptidase A;
            phaseolin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine-type carboxypeptidases
REACTION    Release of a C-terminal amino acid with broad specificity
INHIBITOR   Isoflurophate [CPD:C00202];
            Thiol-blocking reagent [CPD:C00648]
COMMENT     A carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl
            fluorophosphate, and sensitive to thiol-blocking reagents (reviewed
            in [1]). Widely distributed in eukaryotes. Type example of peptidase
            family S10.
REFERENCE   1
  AUTHORS   Breddam, K.
  TITLE     Serine carboxypeptidases. A review.
  JOURNAL   Carlsberg Res. Commun. 51 (1986) 83-128.
REFERENCE   2  [PMID:3028649]
  AUTHORS   Valls LA, Hunter CP, Rothman JH, Stevens TH.
  TITLE     Protein sorting in yeast: the localization determinant of yeast
            vacuolar carboxypeptidase Y resides in the propeptide.
  JOURNAL   Cell. 48 (1987) 887-97.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:1737744]
  AUTHORS   Jackman HL, Morris PW, Deddish PA, Skidgel RA, Erdos EG.
  TITLE     Inactivation of endothelin I by deamidase (lysosomal protective
            protein).
  JOURNAL   J. Biol. Chem. 267 (1992) 2872-5.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:1487525]
  AUTHORS   Miller JJ, Changaris DG, Levy RS.
  TITLE     Purification, subunit structure and inhibitor profile of cathepsin
            A.
  JOURNAL   J. Chromatogr. 627 (1992) 153-62.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map04614  Renin-angiotensin system
ORTHOLOGY   KO: K01287  carboxypeptidase C
GENES       HSA: 5476(CTSA)
            PTR: 458290(CTSA)
            MMU: 19025(Ctsa)
            RNO: 296370(Ppgb)
            CFA: 611146(CTSA)
            BTA: 518169(CTSA)
            GGA: 428163(RCJMB04_25l7)
            XLA: 494810(LOC494810)
            XTR: 734066(LOC734066)
            DRE: 321818(zgc:65802)
            SPU: 594128(LOC594128)
            CEL: F41C3.5
            ATH: AT1G11080(SCPL31) AT4G12910(SCPL20)
            OSA: 4328060 4335479 4351908
            SCE: YBR139W YMR297W(PRC1)
            AGO: AGOS_AGL328C
            PIC: PICST_36810 PICST_78088(KEX1)
            CGR: CAGL0M13651g
            SPO: SPAC19G12.10c(pcy1)
            ANI: AN5442.2
            AFM: AFUA_3G12210 AFUA_5G14610 AFUA_6G13540
            AOR: AO090103000332
            CNE: CNF03760
            UMA: UM01886.1
            DDI: DDBDRAFT_0184133
            TET: TTHERM_00249550 TTHERM_00249560 TTHERM_00249570
                 TTHERM_00249680 TTHERM_00249710 TTHERM_00249800
                 TTHERM_00448920 TTHERM_00448930 TTHERM_00448980
                 TTHERM_00927190 TTHERM_00927200 TTHERM_00927210
                 TTHERM_00927220 TTHERM_01141610
            TBR: Tb10.70.7080 Tb10.70.7090 Tb10.70.7100
            TCR: 508671.20 509695.210 509695.220 509695.230
            LMA: LmjF18.0450
STRUCTURES  PDB: 1CPY  1IVY  1WPX  1YSC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.16.5
            ExPASy - ENZYME nomenclature database: 3.4.16.5
            ExplorEnz - The Enzyme Database: 3.4.16.5
            ERGO genome analysis and discovery system: 3.4.16.5
            BRENDA, the Enzyme Database: 3.4.16.5
            CAS: 9046-67-7
///
ENTRY       EC 3.4.16.6                 Enzyme
NAME        carboxypeptidase D;
            cereal serine carboxypeptidase II;
            Saccharomyces cerevisiae KEX1 gene product;
            carboxypeptidase Kex1;
            gene KEX1 serine carboxypeptidase;
            KEX1 carboxypeptidase;
            KEX1 proteinase;
            KEX1DELTAp;
            CPDW-II
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine-type carboxypeptidases
REACTION    Preferential release of a C-terminal arginine or lysine residue
INHIBITOR   Isoflurophate [CPD:C00202];
            Thiol-blocking reagent [CPD:C00648]
COMMENT     A carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl
            fluorophosphate, and sensitive to thiol-blocking reagents (reviewed
            in [1]). In peptidase family S10 (carboxypeptidase C family).
REFERENCE   1
  AUTHORS   Breddam, K.
  TITLE     Serine carboxypeptidases. A review.
  JOURNAL   Carlsberg Res. Commun. 51 (1986) 83-128.
REFERENCE   2
  AUTHORS   Breddam, K., Sorensen, S.B. and Svendsen, I.
  TITLE     Primary structure and enzymatic properties of carboxypeptidase II
            from wheat bran.
  JOURNAL   Carlsberg Res. Commun. 52 (1987) 297-311.
  ORGANISM  Triticum aestivum [GN:etae]
REFERENCE   3  [PMID:3301004]
  AUTHORS   Dmochowska A, Dignard D, Henning D, Thomas DY, Bussey H.
  TITLE     Yeast KEX1 gene encodes a putative protease with a carboxypeptidase
            B-like function involved in killer toxin and alpha-factor precursor
            processing.
  JOURNAL   Cell. 50 (1987) 573-84.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4  [PMID:1390755]
  AUTHORS   Liao DI, Breddam K, Sweet RM, Bullock T, Remington SJ.
  TITLE     Refined atomic model of wheat serine carboxypeptidase II at 2.2-A
            resolution.
  JOURNAL   Biochemistry. 31 (1992) 9796-812.
  ORGANISM  Triticum aestivum [GN:etae]
ORTHOLOGY   KO: K01288  carboxypeptidase D
GENES       ATH: AT2G24000(SCPL22) AT2G24010(SCPL23) AT3G52000(SCPL36)
                 AT3G52010(SCPL37) AT3G52020(SCPL39) AT3G63470(SCPL40)
                 AT4G30610(BRS1) AT4G30810(SCPL29) AT5G23210(SCPL34)
            OSA: 4330073 4330996 4335700 4340344 4344152
            SCE: YGL203C(KEX1)
            AGO: AGOS_AFR549W
            CGR: CAGL0G01232g
            SPO: SPBC16G5.09
            ANI: AN1384.2 AN2555.2
            AFM: AFUA_1G08940 AFUA_2G03510 AFUA_5G01200 AFUA_5G07330
                 AFUA_8G04120
            AOR: AO090005001632 AO090010000534
            ANG: An07g08030(pepF)
            CNE: CND01720 CNE00660
            UMA: UM01888.1 UM03465.1 UM03947.1
            DDI: DDB_0229903
            TET: TTHERM_00312150 TTHERM_00617770 TTHERM_00617790
STRUCTURES  PDB: 1AC5  1BCR  1BCS  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.16.6
            ExPASy - ENZYME nomenclature database: 3.4.16.6
            ExplorEnz - The Enzyme Database: 3.4.16.6
            ERGO genome analysis and discovery system: 3.4.16.6
            BRENDA, the Enzyme Database: 3.4.16.6
            CAS: 153967-26-1
///
ENTRY       EC 3.4.17.1                 Enzyme
NAME        carboxypeptidase A;
            carboxypolypeptidase;
            pancreatic carboxypeptidase A;
            tissue carboxypeptidase A
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Release of a C-terminal amino acid, but little or no action with
            -Asp, -Glu, -Arg, -Lys or -Pro
COFACTOR    Zinc [CPD:C00038]
COMMENT     A zinc enzyme formed from procarboxypeptidase A. Isolated from
            cattle, pig and dogfish pancreas, and other sources including mast
            cells [3] and skeletal muscle [4]. Type example of peptidase family
            M14.
REFERENCE   1
  AUTHORS   Petra, P.H.
  TITLE     Bovine procarboxypeptidase and carboxypeptidase A.
  JOURNAL   Methods Enzymol. 19 (1970) 460-503.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:5140186]
  AUTHORS   Reeck GR, Walsh KA, Neurath H.
  TITLE     Isolation and characterization of carboxypeptidases A and B from
            activated pancreatic juice.
  JOURNAL   Biochemistry. 10 (1971) 4690-8.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:7371832]
  AUTHORS   Everitt MT, Neurath H.
  TITLE     Rat peritoneal mast cell carboxypeptidase: localization,
            purification, and enzymatic properties.
  JOURNAL   FEBS. Lett. 110 (1980) 292-6.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:7018567]
  AUTHORS   Bodwell JE, Meyer WL.
  TITLE     Purification and characterization of carboxypeptidase A from rat
            skeletal muscle.
  JOURNAL   Biochemistry. 20 (1981) 2767-77.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map04614  Renin-angiotensin system
ORTHOLOGY   KO: K01290  carboxypeptidase A
            KO: K08779  carboxypeptidase A1
            KO: K08780  carboxypeptidase A3
            KO: K08781  carboxypeptidase A5
            KO: K08782  carboxypeptidase A6
GENES       HSA: 1357(CPA1) 1359(CPA3) 57094(CPA6) 93979(CPA5)
            PTR: 471081(CPA3) 472786(CPA6)
            MMU: 109697(Cpa1) 12873(Cpa3) 329093(Cpa6) 74649(Cpa5)
            RNO: 24269(Cpa1) 312913(Cpa6_predicted) 408212(Cpa5) 54242(Cpa3)
            CFA: 475192(CPA1) 482257(CPA5) 485707(CPA3) 486983(CPA6)
            BTA: 286762(CPA1) 511416(MGC152081) 528454(LOC528454)
            SSC: 397476(PCPA1)
            GGA: 395276(CPA1) 420171(CPA6)
            XLA: 379614(MGC64526) 379903(cpa6) 495367(LOC495367)
            DRE: 246092(cpa5)
            DME: Dmel_CG12374 Dmel_CG33935(mei-217) Dmel_CG4399(east)
                 Dmel_CG6806(Lsp2)
            AZO: azo2294
            PMB: A9601_05111
            PMC: P9515_05181
            PMF: P9303_06571
            PMG: P9301_04801
            PME: NATL1_05101
STRUCTURES  PDB: 1ARL  1ARM  1BAV  1CBX  1CPS  1CPX  1EE3  1ELL  1ELM  1F57  
                 1HDQ  1HDU  1HEE  1IY7  1JQG  1M4L  1PYT  1YME  1ZLH  2ABZ  
                 2CTB  2CTC  3CPA  4CPA  5CPA  6CPA  7CPA  8CPA  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.1
            ExPASy - ENZYME nomenclature database: 3.4.17.1
            ExplorEnz - The Enzyme Database: 3.4.17.1
            ERGO genome analysis and discovery system: 3.4.17.1
            BRENDA, the Enzyme Database: 3.4.17.1
            CAS: 11075-17-5
///
ENTRY       EC 3.4.17.2                 Enzyme
NAME        carboxypeptidase B;
            protaminase;
            pancreatic carboxypeptidase B;
            tissue carboxypeptidase B;
            peptidyl-L-lysine [L-arginine]hydrolase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Preferential release of a C-terminal lysine or arginine amino acid
COFACTOR    Zinc [CPD:C00038]
COMMENT     A zinc enzyme formed from procarboxypeptidase B. Isolated from
            cattle, pig and dogfish pancreas and other sources, including skin
            fibroblasts [3] and adrenal medulla [4]. In peptidase family M14
            (carboxypeptidase A family).
REFERENCE   1
  AUTHORS   Folk, J.E.
  TITLE     Carboxypeptidase B (porcine pancreas).
  JOURNAL   Methods Enzymol. 19 (1970) 504-508.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:1009123]
  AUTHORS   Brodrick JW, Geokas MC, Largman C.
  TITLE     Human carboxypeptidase B. II. Purification of the enzyme from
            pancreatic tissue and comparison with the enzymes present in
            pancreatic secretion.
  JOURNAL   Biochim. Biophys. Acta. 452 (1976) 468-81.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:40714]
  AUTHORS   Butterworth J, Duncan JJ.
  TITLE     Carboxypeptidase B activity of cultured skin fibroblasts and
            relationship to cystic fibrosis.
  JOURNAL   Clin. Chim. Acta. 97 (1979) 39-43.
  ORGANISM  rat [GN:rno], cow [GN:bta]
REFERENCE   4  [PMID:6130442]
  AUTHORS   Wallace EF, Evans CJ, Jurik SM, Mefford IN, Barchas JD.
  TITLE     Carboxypeptidase B activity from adrenal medulla--is it involved in
            the processing of proenkephalin?
  JOURNAL   Life. Sci. 31 (1982) 1793-6.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K01291  carboxypeptidase B
GENES       HSA: 1360(CPB1)
            PTR: 460763(CPB1)
            MMU: 76703(Cpb1)
            RNO: 24271(Cpb1)
            CFA: 403512(CPB1)
            SSC: 397341(CPB1)
            GGA: 424888(CPB1)
            XLA: 495368(LOC495368)
            DRE: 322412(cpb1)
STRUCTURES  PDB: 1CPB  1KWM  1PBA  1Z5R  1ZG7  1ZG8  1ZG9  1ZLI  2C1C  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.2
            ExPASy - ENZYME nomenclature database: 3.4.17.2
            ExplorEnz - The Enzyme Database: 3.4.17.2
            ERGO genome analysis and discovery system: 3.4.17.2
            BRENDA, the Enzyme Database: 3.4.17.2
            CAS: 9025-24-5
///
ENTRY       EC 3.4.17.3                 Enzyme
NAME        lysine carboxypeptidase;
            carboxypeptidase N;
            arginine carboxypeptidase;
            kininase I;
            anaphylatoxin inactivator;
            plasma carboxypeptidase B;
            creatine kinase conversion factor;
            bradykinase;
            kininase Ia;
            hippuryllysine hydrolase;
            bradykinin-decomposing enzyme;
            protaminase;
            CPase N;
            creatinine kinase convertase;
            peptidyl-L-lysine(-L-arginine) hydrolase;
            CPN
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Release of a C-terminal basic amino acid, preferentially lysine
COFACTOR    Zinc [CPD:C00038]
COMMENT     A zinc enzyme found in plasma. Inactivates bradykinin and
            anaphylatoxins in blood plasma. In peptidase family M14
            (carboxypeptidase A family).
REFERENCE   1  [PMID:7341915]
  AUTHORS   Plummer TH Jr, Erdos EG.
  TITLE     Human plasma carboxypeptidase N.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 442-9.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:6750606]
  AUTHORS   Levin Y, Skidgel RA, Erdos EG.
  TITLE     Isolation and characterization of the subunits of human plasma
            carboxypeptidase N (kininase i).
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 79 (1982) 4618-22.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:3074547]
  AUTHORS   Skidgel RA.
  TITLE     Basic carboxypeptidases: regulators of peptide hormone activity.
  JOURNAL   Trends. Pharmacol. Sci. 9 (1988) 299-304.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01292  carboxypeptidase N
GENES       HSA: 1369(CPN1) 1370(CPN2)
            PTR: 450672(CPN1)
            MMU: 93721(Cpn1)
            RNO: 365466(Cpn1)
            CFA: 477795(CPN1)
            BTA: 536753(MGC128810)
            GGA: 769143(CPN1)
            XLA: 398791(MGC68490)
            XTR: 548472(MGC107957)
            DRE: 337172(cpn1)
STRUCTURES  PDB: 2NSM  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.3
            ExPASy - ENZYME nomenclature database: 3.4.17.3
            ExplorEnz - The Enzyme Database: 3.4.17.3
            ERGO genome analysis and discovery system: 3.4.17.3
            BRENDA, the Enzyme Database: 3.4.17.3
            CAS: 9013-89-2
///
ENTRY       EC 3.4.17.4                 Enzyme
NAME        Gly-Xaa carboxypeptidase;
            glycine carboxypeptidase;
            carboxypeptidase a;
            carboxypeptidase S;
            peptidase alpha;
            yeast carboxypeptidase;
            Gly-X carboxypeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Release of a C-terminal amino acid from a peptide in which glycine
            is the penultimate amino acid, e.g. Z-Gly!Leu
COMMENT     From yeast. In peptidase family M20 (glutamate carboxypeptidase
            family).
REFERENCE   1  [PMID:4961236]
  AUTHORS   Felix F, Brouillet N.
  TITLE     [Purification and properties of 2 peptidases from baker's yeast]
  JOURNAL   Biochim. Biophys. Acta. 122 (1966) 127-44.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:352726]
  AUTHORS   Wolf DH, Ehmann C.
  TITLE     Carboxypetidase S from yeast: regulation of its activity during
            vegetative growth and differentiation.
  JOURNAL   FEBS. Lett. 91 (1978) 59-62.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K01293  Gly-Xaa carboxypeptidase
GENES       SCE: YJL172W(CPS1)
            AGO: AGOS_AEL132W
            PIC: PICST_28659 PICST_34371(CPS1)
            CGR: CAGL0C00319g
            SPO: SPAC24C9.08
            ANI: AN4810.2
            AOR: AO090020000288
            CNE: CNB04480 CNL06270
            UMA: UM05897.1
            BRA: BRADO0276
            RPA: RPA0412(CPS1)
            RPE: RPE_0045
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.4
            ExPASy - ENZYME nomenclature database: 3.4.17.4
            ExplorEnz - The Enzyme Database: 3.4.17.4
            ERGO genome analysis and discovery system: 3.4.17.4
            BRENDA, the Enzyme Database: 3.4.17.4
            CAS: 9025-25-6
///
ENTRY       EC 3.4.17.5       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
COMMENT     Deleted entry: aspartate carboxypeptidase (EC 3.4.17.5 created 1972
            as EC 3.4.12.9, transferred 1978 to EC 3.4.17.5, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.5
            ExPASy - ENZYME nomenclature database: 3.4.17.5
            ExplorEnz - The Enzyme Database: 3.4.17.5
            ERGO genome analysis and discovery system: 3.4.17.5
            BRENDA, the Enzyme Database: 3.4.17.5
///
ENTRY       EC 3.4.17.6                 Enzyme
NAME        alanine carboxypeptidase;
            N-benzoyl-L-alanine-amidohydrolase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Release of a C-terminal alanine from a peptide or a variety of
            pteroyl or acyl groups
COMMENT     From soil bacteria. The enzyme from Corynebacterium equi also
            hydrolyses N-benzoylglycine and N-benzoyl-L-aminobutyric acid.
REFERENCE   1  [PMID:5806587]
  AUTHORS   Levy CC, Goldman P.
  TITLE     Bacterial peptidases. 3. An enzyme specific for N-acyl linkages to
            alanine.
  JOURNAL   J. Biol. Chem. 244 (1969) 4467-72.
  ORGANISM  soil bacterium
REFERENCE   2
  AUTHORS   Miyagawa, E., Takahiro, H. and Yoshinobu, M.
  TITLE     Purification and properties of N-benzoyl-L-alanine amidohydrolase
            from Corynebacterium equii.
  JOURNAL   Agric. Biol. Chem. 50 (1986) 1527-1531.
  ORGANISM  Corynebacterium equii
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.6
            ExPASy - ENZYME nomenclature database: 3.4.17.6
            ExplorEnz - The Enzyme Database: 3.4.17.6
            ERGO genome analysis and discovery system: 3.4.17.6
            BRENDA, the Enzyme Database: 3.4.17.6
            CAS: 37288-70-3
///
ENTRY       EC 3.4.17.7       Obsolete  Enzyme
NAME        Transferred to 3.5.1.28
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
COMMENT     Transferred entry: now EC 3.5.1.28, N-acetylmuramoyl-L-alanine
            amidase (EC 3.4.17.7 created 1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.7
            ExPASy - ENZYME nomenclature database: 3.4.17.7
            ExplorEnz - The Enzyme Database: 3.4.17.7
            ERGO genome analysis and discovery system: 3.4.17.7
            BRENDA, the Enzyme Database: 3.4.17.7
///
ENTRY       EC 3.4.17.8                 Enzyme
NAME        muramoylpentapeptide carboxypeptidase;
            D-alanine carboxypeptidase I;
            DD-carboxypeptidase;
            D-alanine carboxypeptidase;
            D-alanyl-D-alanine carboxypeptidase;
            D-alanine-D-alanine-carboxypeptidase;
            carboxypeptidase D-alanyl-D-alanine;
            carboxypeptidase I;
            UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase;
            D-alanyl-D-alanine peptidase;
            DD-peptidase;
            penicillin binding protein 5;
            PBP5;
            PdcA;
            VanY
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Cleavage of the bond
            UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-
            alanyl!D-alanine [RN:R04611]
ALL_REAC    R04611
INHIBITOR   Penicillin [CPD:C00395];
            Cephalosporin [CPD:C00875]
EFFECTOR    Divalent metal [CPD:C02148]
COMMENT     A bacterial enzyme that requires a divalent cation for activity.
            Does not cleave the C-terminal D-alanine from the product of the
            above reaction,
            UDP-N-acetyl-muramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-
            alanine. Competitively inhibited by penicillins and cephalosporins.
REFERENCE   1  [PMID:4871206]
  AUTHORS   Izaki K, Strominger JL.
  TITLE     Biosynthesis of the peptidoglycan of bacterial cell walls. XIV.
            Purification and properties of two D-alanine carboxypeptidases from
            Escherichia coli.
  JOURNAL   J. Biol. Chem. 243 (1968) 3193-201.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00550  Peptidoglycan biosynthesis
GENES       ECO: b0376(ampH)
STRUCTURES  PDB: 1LBU  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.8
            ExPASy - ENZYME nomenclature database: 3.4.17.8
            ExplorEnz - The Enzyme Database: 3.4.17.8
            ERGO genome analysis and discovery system: 3.4.17.8
            BRENDA, the Enzyme Database: 3.4.17.8
            CAS: 9077-67-2
///
ENTRY       EC 3.4.17.9       Obsolete  Enzyme
NAME        Transferred to 3.4.17.4
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
COMMENT     Transferred entry: Now included with EC 3.4.17.4, Gly-Xaa
            carboxypeptidase (EC 3.4.17.9 created 1981, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.9
            ExPASy - ENZYME nomenclature database: 3.4.17.9
            ExplorEnz - The Enzyme Database: 3.4.17.9
            ERGO genome analysis and discovery system: 3.4.17.9
            BRENDA, the Enzyme Database: 3.4.17.9
///
ENTRY       EC 3.4.17.10                Enzyme
NAME        carboxypeptidase E;
            carboxypeptidase H;
            enkephalin convertase;
            cobalt-stimulated chromaffin granule carboxypeptidase;
            insulin granule-associated carboxypeptidase;
            enkephalin convertase;
            membrane-bound carboxypeptidase;
            carboxypeptidase E;
            enkephalin-precursor endopeptidase;
            enkephalin precursor carboxypeptidase;
            peptidyl-L-lysine(-L-arginine) hydrolase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Release of C-terminal arginine or lysine residues from polypeptides
COFACTOR    Zinc [CPD:C00038]
INHIBITOR   EDTA [CPD:C00284];
            1,10-Phenanthroline [CPD:C00604]
EFFECTOR    Cobalt [CPD:C00175]
COMMENT     A zinc enzyme, activated by Co2+. Inhibited by 1,10-phenanthroline
            and other chelating agents. pH optimum 5.6. Located in storage
            granules of secretory cells, and active in processing of protein
            hormones and bioactive peptides. In peptidase family M14
            (carboxypeptidase A family).
REFERENCE   1  [PMID:10206965]
  AUTHORS   Qian Y, Varlamov O, Fricker LD.
  TITLE     Glu300 of rat carboxypeptidase E is essential for enzymatic activity
            but not substrate binding or routing to the regulated secretory
            pathway.
  JOURNAL   J. Biol. Chem. 274 (1999) 11582-6.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Fricker, L.D.
  TITLE     Carboxypeptidase E/H.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Academic Press, London, 1998, p.
            1341-1344.
REFERENCE   3
  AUTHORS   Fricker, L.D.
  TITLE     Methods for studying carboxypeptidase E.
  JOURNAL   Methods Neurosci. 23 (1995) 237-250.
REFERENCE   4  [PMID:2334405]
  AUTHORS   Manser E, Fernandez D, Loo L, Goh PY, Monfries C, Hall C, Lim L.
  TITLE     Human carboxypeptidase E. Isolation and characterization of the
            cDNA, sequence conservation, expression and processing in vitro.
  JOURNAL   Biochem. J. 267 (1990) 517-25.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:2897826]
  AUTHORS   Fricker LD.
  TITLE     Carboxypeptidase E.
  JOURNAL   Annu. Rev. Physiol. 50 (1988) 309-21.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map04940  Type I diabetes mellitus
ORTHOLOGY   KO: K01294  carboxypeptidase E
GENES       HSA: 1363(CPE)
            PTR: 461592(CPE)
            MMU: 12876(Cpe)
            RNO: 25669(Cpe)
            CFA: 475492(CPE)
            BTA: 280753(CPE)
            GGA: 422424(CPE)
            DRE: 407979(zgc:85981)
            SPU: 757239(LOC757239)
            CEL: F01D4.4(egl-21)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.10
            ExPASy - ENZYME nomenclature database: 3.4.17.10
            ExplorEnz - The Enzyme Database: 3.4.17.10
            ERGO genome analysis and discovery system: 3.4.17.10
            BRENDA, the Enzyme Database: 3.4.17.10
            CAS: 81876-95-1
///
ENTRY       EC 3.4.17.11                Enzyme
NAME        glutamate carboxypeptidase;
            carboxypeptidase G;
            carboxypeptidase G1;
            carboxypeptidase G2;
            glutamyl carboxypeptidase;
            N-pteroyl-L-glutamate hydrolase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Release of C-terminal glutamate residues from a wide range of
            N-acylating moieties, including peptidyl, aminoacyl, benzoyl,
            benzyloxycarbonyl, folyl and pteroyl groups
COFACTOR    Zinc [CPD:C00038]
COMMENT     A zinc enzyme produced by pseudomonads, Flavobacterium sp. and
            Acinetobacter sp. Its ability to hydrolyse pteroyl-L-glutamate
            (folic acid) has led to its use as a folate-depleting, antitumour
            agent. Type example of peptidase family M20
REFERENCE   1  [PMID:5237864]
  AUTHORS   Goldman P, Levy CC.
  TITLE     Carboxypeptidase G: purification and properties.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 58 (1967) 1299-306.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:5129727]
  AUTHORS   McCullough JL, Chabner BA, Bertino JR.
  TITLE     Purification and properties of carboxypeptidase G 1 .
  JOURNAL   J. Biol. Chem. 246 (1971) 7207-13.
  ORGANISM  Pseudomonas stutzeri
REFERENCE   3  [PMID:26657]
  AUTHORS   Albrecht AM, Boldizsar E, Hutchison DJ.
  TITLE     Carboxypeptidase displaying differential velocity in hydrolysis of
            methotrexate, 5-methyltetrahydrofolic acid, and leucovorin.
  JOURNAL   J. Bacteriol. 134 (1978) 506-13.
  ORGANISM  Flavobacterium sp.
REFERENCE   4  [PMID:3838935]
  AUTHORS   Sherwood RF, Melton RG, Alwan SM, Hughes P.
  TITLE     Purification and properties of carboxypeptidase G2 from Pseudomonas
            sp. strain RS-16. Use of a novel triazine dye affinity method.
  JOURNAL   Eur. J. Biochem. 148 (1985) 447-53.
  ORGANISM  Pseudomonas sp.
ORTHOLOGY   KO: K01295  glutamate carboxypeptidase
GENES       PMU: PM0932
            VVU: VV2_0898
            VVY: VVA1372
            VPA: VPA1611
            VFI: VFA0930
            PPR: PBPRA2427
            PAE: PA2787(cpg2)
            PST: PSPTO_2120 PSPTO_2570
            PSB: Psyr_1915 Psyr_2261
            PSP: PSPPH_1871
            LPN: lpg1705
            LPF: lpl1664
            LPP: lpp1670
            AHA: AHA_1483
            RSO: RSc3093(RS00546)
            REU: Reut_B4369
            RME: Rmet_0024 Rmet_4870
            BPE: BP3295
            BPA: BPP4129
            BBR: BB4599
            NIS: NIS_0890
            SUN: SUN_1051
            ADE: Adeh_0170
            AFW: Anae109_0179
            BJA: bll0789 bll3749 blr5597 blr7006
            BRA: BRADO2922 BRADO6431
            BBT: BBta_1203 BBta_5255
            RPA: RPA1217
            RPB: RPB_1225
            RPC: RPC_1198
            RPD: RPD_4023
            SIL: SPO1215
            BHA: BH0352
            BCL: ABC1036
            NFA: nfa24270
            SEN: SACE_4623 SACE_4710
            SRU: SRU_0454
            DRA: DR_2493
            DGE: Dgeo_0366
            TTH: TTC1334
            TTJ: TTHA1698
            TMA: TM0129
            NPH: NP5372A(cxp_2)
            PTO: PTO0575
STRUCTURES  PDB: 1CG2  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.11
            ExPASy - ENZYME nomenclature database: 3.4.17.11
            ExplorEnz - The Enzyme Database: 3.4.17.11
            ERGO genome analysis and discovery system: 3.4.17.11
            BRENDA, the Enzyme Database: 3.4.17.11
            CAS: 9074-87-7
///
ENTRY       EC 3.4.17.12                Enzyme
NAME        carboxypeptidase M;
            CPM
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Cleavage of C-terminal arginine or lysine residues from polypeptides
COMMENT     A membrane-bound enzyme optimally active at neutral pH. In peptidase
            family M14 (carboxypeptidase A family)
REFERENCE   1  [PMID:3074547]
  AUTHORS   Skidgel RA.
  TITLE     Basic carboxypeptidases: regulators of peptide hormone activity.
  JOURNAL   Trends. Pharmacol. Sci. 9 (1988) 299-304.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:2775217]
  AUTHORS   Deddish PA, Skidgel RA, Erdos EG.
  TITLE     Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M
            at low pH. Similarity to carboxypeptidase H (enkephalin convertase).
  JOURNAL   Biochem. J. 261 (1989) 289-91.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:2914904]
  AUTHORS   Skidgel RA, Davis RM, Tan F.
  TITLE     Human carboxypeptidase M. Purification and characterization of a
            membrane-bound carboxypeptidase that cleaves peptide hormones.
  JOURNAL   J. Biol. Chem. 264 (1989) 2236-41.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01296  carboxypeptidase M
GENES       HSA: 1368(CPM)
            MMU: 70574(Cpm)
            RNO: 314855(Cpm_predicted)
            GGA: 417843(CPM)
            TET: TTHERM_00725980
STRUCTURES  PDB: 1UWY  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.12
            ExPASy - ENZYME nomenclature database: 3.4.17.12
            ExplorEnz - The Enzyme Database: 3.4.17.12
            ERGO genome analysis and discovery system: 3.4.17.12
            BRENDA, the Enzyme Database: 3.4.17.12
            CAS: 120038-28-0
///
ENTRY       EC 3.4.17.13                Enzyme
NAME        muramoyltetrapeptide carboxypeptidase;
            carboxypeptidase IIW;
            carboxypeptidase II;
            lysyl-D-alanine carboxypeptidase;
            L-lysyl-D-alanine carboxypeptidase;
            LD-carboxypeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Hydrolysis of the bond:
            N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-
            L-lysyl!D-alanine
INHIBITOR   Thiol-blocking reagent [CPD:C00648]
EFFECTOR    Manganese [CPD:C00034];
            Calcium [CPD:C00076]
COMMENT     Variants are known from various microorganisms. Involved in
            peptidoglycan synthesis, catalysing both decarboxylation and
            transpeptidation. Stimulated by divalent cations such as Mg2+ and
            Ca2+, but not by Zn2+. Inhibited by thiol-blocking reagents, but
            unaffected by penicillin
REFERENCE   1  [PMID:109439]
  AUTHORS   DasGupta H, Fan DP.
  TITLE     Purification and characterization of a
            carboxypeptidase-transpeptidase of Bacillus megaterium acting on the
            tetrapeptide moiety of the peptidoglycan.
  JOURNAL   J. Biol. Chem. 254 (1979) 5672-83.
  ORGANISM  Bacillus megaterium
REFERENCE   2  [PMID:6754695]
  AUTHORS   Rousset A, Nguyen-Disteche M, Minck R, Ghuysen JM.
  TITLE     Penicillin-binding proteins and carboxypeptidase/transpeptidase
            activities in Proteus vulgaris P18 and its penicillin-induced stable
            L-forms.
  JOURNAL   J. Bacteriol. 152 (1982) 1042-8.
  ORGANISM  Proteus vulgaris
REFERENCE   3  [PMID:3521530]
  AUTHORS   Metz R, Henning S, Hammes WP.
  TITLE     LD-carboxypeptidase activity in Escherichia coli. II. Isolation,
            purification and characterization of the enzyme from E. coli K 12.
  JOURNAL   Arch. Microbiol. 144 (1986) 181-6.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01297  muramoyltetrapeptide carboxypeptidase
GENES       ECO: b1192(ldcA)
            ECJ: JW1181(ldcA)
            ECE: Z1955
            ECS: ECs1688
            ECC: c1641(ldcA)
            ECI: UTI89_C1378(ldcA)
            ECP: ECP_1235
            ECV: APECO1_304(ldcA)
            ECW: EcE24377A_1337(ldcA)
            ECX: EcHS_A1296(ldcA)
            STY: STY1928
            STT: t1077
            SPT: SPA1073(ycgQ)
            SEC: SC1793(ycgQ)
            STM: STM1800(ycgQ)
            SFL: SF1182(ldcA)
            SFX: S1271
            SFV: SFV_1201
            SSN: SSON_1185
            SBO: SBO_1879
            SDY: SDY_1232
            ENT: Ent638_2360
            PPU: PP_4799
            PFL: PFL_5444
            PFO: Pfl_4962
            PEN: PSEEN4818
            PCR: Pcryo_0859
            PRW: PsycPRwf_1821
            NME: NMB1620
            NMA: NMA1819
            NGO: NGO1274
            CVI: CV_2304(mccF)
            RSO: RSc1452(RS03855)
            REU: Reut_A1845
            REH: H16_A1922(mccF)
            RME: Rmet_1574
            BMA: BMA1513(ldcA)
            BMV: BMASAVP1_A2012(ldcA)
            BML: BMA10299_A3298(ldcA)
            BMN: BMA10247_1284(ldcA)
            BXE: Bxe_A1921
            BVI: Bcep1808_1892
            BUR: Bcep18194_A5282 Bcep18194_C7092
            BCN: Bcen_6110
            BCH: Bcen2424_1967
            BAM: Bamb_1955
            BPS: BPSL2122
            BPM: BURPS1710b_2537(ldcA)
            BPL: BURPS1106A_2436(ldcA) BURPS1106A_A2525
            BPD: BURPS668_2393(ldcA)
            BTE: BTH_I2063
            PNU: Pnuc_1415
            BPE: BP1166(ldcA) BP1701(ldcA)
            BPA: BPP1600(ldcA) BPP3073(ldcA)
            BBR: BB2677(ldcA) BB3036(ldcA)
            RFR: Rfer_2285
            POL: Bpro_2448
            PNA: Pnap_1996
            AAV: Aave_3081
            AJS: Ajs_2281
            VEI: Veis_4303
            MPT: Mpe_A1749
            HAR: HEAR1384(ldcA)
            MMS: mma_2002(ldcA)
            SAT: SYN_01084
            RTY: RT0390(ldcA)
            RBE: RBE_0581(mccF)
            OTS: OTBS_0277(mccF)
            BTL: BALH_1226(ldcA)
            BCL: ABC0781
            SSA: SSA_2339
            CPR: CPR_2453
            CNO: NT01CX_0768
            MTA: Moth_0711
            AVA: Ava_4290 Ava_4926
            PMB: A9601_05111
            PMC: P9515_05181
            PMF: P9303_06571
            PMG: P9301_04801
            PMH: P9215_05351(ldcA)
            PME: NATL1_05101
            BFS: BF4140
            CHU: CHU_3416
            GFO: GFO_2758(ldcA)
            CTE: CT2236
            CCH: Cag_2016
            CPH: Cpha266_0047
            PVI: Cvib_0023
            PLT: Plut_0019
            PTO: PTO0247
STRUCTURES  PDB: 1S2J  1ZRS  2AUM  2AUN  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.13
            ExPASy - ENZYME nomenclature database: 3.4.17.13
            ExplorEnz - The Enzyme Database: 3.4.17.13
            ERGO genome analysis and discovery system: 3.4.17.13
            BRENDA, the Enzyme Database: 3.4.17.13
            CAS: 60063-80-1
///
ENTRY       EC 3.4.17.14                Enzyme
NAME        zinc D-Ala-D-Ala carboxypeptidase;
            Zn2+ G peptidase, D-alanyl-D-alanine hydrolase;
            D-alanyl-D-alanine-cleaving carboxypeptidase;
            DD-carboxypeptidase;
            G enzyme;
            DD-carboxypeptidase-transpeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Cleavage of the bond: (Ac)2-L-lysyl-D-alanyl!D-alanine
EFFECTOR    Zinc [CPD:C00038]
COMMENT     A zinc enzyme. Catalyzes carboxypeptidation but not transpeptidation
            reactions involved in bacterial cell wall metabolism. Weakly
            inhibited by beta-lactams. In peptidase family M15. Distinct from EC
            3.4.16.4, serine-type D-Ala-D-Ala carboxypeptidase.
REFERENCE   1  [PMID:7121588]
  AUTHORS   Dideberg O, Charlier P, Dive G, Joris B, Frere JM, Ghuysen JM.
  TITLE     Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving
            carboxypeptidase at 2.5 A resolution.
  JOURNAL   Nature. 299 (1982) 469-70.
  ORGANISM  Streptomyces albus
REFERENCE   2  [PMID:6825689]
  AUTHORS   Joris B, Van Beeumen J, Casagrande F, Gerday C, Frere JM, Ghuysen
            JM.
  TITLE     The complete amino acid sequence of the Zn2+-containing
            D-alanyl-D-alanine-cleaving carboxypeptidase of streptomyces albus
            G.
  JOURNAL   Eur. J. Biochem. 130 (1983) 53-69.
  ORGANISM  Streptomyces albus
REFERENCE   3  [PMID:6597561]
  AUTHORS   Ghuysen JM, Frere JM, Leyh-Bouille M, Nguyen-Disteche M, Coyette J,
            Dusart J, Joris B, Duez C, Dideberg O, Charlier P, et al.
  TITLE     Bacterial wall peptidoglycan, DD-peptidases and beta-lactam
            antibiotics.
  JOURNAL   Scand. J. Infect. Dis. Suppl. 42 (1984) 17-37.
ORTHOLOGY   KO: K08640  zinc D-Ala-D-Ala carboxypeptidase
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.14
            ExPASy - ENZYME nomenclature database: 3.4.17.14
            ExplorEnz - The Enzyme Database: 3.4.17.14
            ERGO genome analysis and discovery system: 3.4.17.14
            BRENDA, the Enzyme Database: 3.4.17.14
            CAS: 213189-85-6
///
ENTRY       EC 3.4.17.15                Enzyme
NAME        carboxypeptidase A2;
            CPA2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Similar to that of carboxypeptidase A
            (internal_xref(ec_num(3,4,17,1))), but with a preference for bulkier
            C-terminal residues
COMMENT     Isolated from rat pancreas but not present in cattle pancreas. In
            peptidase family M14 (carboxypeptidase A family)
REFERENCE   1  [PMID:5500406]
  AUTHORS   Dehm P, Nordwig A.
  TITLE     The cleavage of prolyl peptides by kidney peptidases. Isolation of a
            microsomal carboxypeptidase from swine kidney.
  JOURNAL   Eur. J. Biochem. 17 (1970) 372-7.
  ORGANISM  pig [GN:ssc]
ORTHOLOGY   KO: K01298  carboxypeptidase A2
GENES       HSA: 1358(CPA2)
            MMU: 232680(Cpa2)
            RNO: 296959(Cpa2_predicted)
            CFA: 475193(CPA2)
            GGA: 416682(CPA2)
            DRE: 431764(zgc:91794)
            CEL: Y18H1A.9
            UMA: UM05109.1
STRUCTURES  PDB: 1AYE  1O6X  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.15
            ExPASy - ENZYME nomenclature database: 3.4.17.15
            ExplorEnz - The Enzyme Database: 3.4.17.15
            ERGO genome analysis and discovery system: 3.4.17.15
            BRENDA, the Enzyme Database: 3.4.17.15
            CAS: 181186-98-1
///
ENTRY       EC 3.4.17.16                Enzyme
NAME        membrane Pro-Xaa carboxypeptidase;
            carboxypeptidase P;
            microsomal carboxypeptidase;
            membrane Pro-X carboxypeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Release of a C-terminal residue other than proline, by preferential
            cleavage of a prolyl bond
COMMENT     One of the renal brush border exopeptidases
REFERENCE   1  [PMID:5500406]
  AUTHORS   Dehm P, Nordwig A.
  TITLE     The cleavage of prolyl peptides by kidney peptidases. Isolation of a
            microsomal carboxypeptidase from swine kidney.
  JOURNAL   Eur. J. Biochem. 17 (1970) 372-7.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:486090]
  AUTHORS   Booth AG, Hubbard LM, Kenny AJ.
  TITLE     Proteins of the kidney microvillar membrane. Immunoelectrophoretic
            analysis of the membrane hydrolases: identification and resolution
            of the detergent- and proteinase-solubilized forms.
  JOURNAL   Biochem. J. 179 (1979) 397-405.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:4038259]
  AUTHORS   Hedeager-Sorensen S, Kenny AJ.
  TITLE     Proteins of the kidney microvillar membrane. Purification and
            properties of carboxypeptidase P from pig kidneys.
  JOURNAL   Biochem. J. 229 (1985) 251-7.
  ORGANISM  pig [GN:ssc]
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.16
            ExPASy - ENZYME nomenclature database: 3.4.17.16
            ExplorEnz - The Enzyme Database: 3.4.17.16
            ERGO genome analysis and discovery system: 3.4.17.16
            BRENDA, the Enzyme Database: 3.4.17.16
            CAS: 9075-64-3
///
ENTRY       EC 3.4.17.17                Enzyme
NAME        tubulinyl-Tyr carboxypeptidase;
            carboxypeptidase-tubulin;
            soluble carboxypeptidase;
            tubulin-tyrosine carboxypeptidase;
            tubulin carboxypeptidase;
            tubulinyltyrosine carboxypeptidase;
            tyrosinotubulin carboxypeptidase;
            tyrosyltubulin carboxypeptidase;
            TTCPase;
            brain I carboxypeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Cleavage of the -Glu!Tyr bond to release the C-terminal tyrosine
            residue from the native tyrosinated tubulin. Inactive on Z-Glu-Tyr
COMMENT     Active at neutral pH, from brain
REFERENCE   1  [PMID:7452228]
  AUTHORS   Argarana CE, Barra HS, Caputto R.
  TITLE     Tubulinyl-tyrosine carboxypeptidase from chicken brain: properties
            and partial purification.
  JOURNAL   J. Neurochem. 34 (1980) 114-8.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:6114100]
  AUTHORS   Kumar N, Flavin M.
  TITLE     Preferential action of a brain detyrosinolating carboxypeptidase on
            polymerized tubulin.
  JOURNAL   J. Biol. Chem. 256 (1981) 7678-86.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:6862022]
  AUTHORS   Arce CA, Barra HS.
  TITLE     Association of tubulinyl-tyrosine carboxypeptidase with
            microtubules.
  JOURNAL   FEBS. Lett. 157 (1983) 75-8.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.17
            ExPASy - ENZYME nomenclature database: 3.4.17.17
            ExplorEnz - The Enzyme Database: 3.4.17.17
            ERGO genome analysis and discovery system: 3.4.17.17
            BRENDA, the Enzyme Database: 3.4.17.17
            CAS: 73050-23-4
///
ENTRY       EC 3.4.17.18                Enzyme
NAME        carboxypeptidase T;
            CPT
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Releases a C-terminal residue, which may be hydrophobic or
            positively charged
COMMENT     Known from Thermoactinomyces vulgaris. In peptidase family M14
            (carboxypeptidase A family)
REFERENCE   1  [PMID:6424730]
  AUTHORS   Osterman AL, Stepanov VM, Rudenskaia GN, Khodova OM, Tsaplina IA.
  TITLE     [Carboxypeptidase T--intracellular carboxypeptidase of
            Thermoactinomycetes--a distant analog of animal carboxypeptidase]
  JOURNAL   Biokhimiia. 49 (1984) 292-301.
  ORGANISM  Thermoactinomyces sp.
REFERENCE   2  [PMID:1936254]
  AUTHORS   Smulevitch SV, Osterman AL, Galperina OV, Matz MV, Zagnitko OP,
            Kadyrov RM, Tsaplina IA, Grishin NV, Chestukhina GG, Stepanov VM.
  TITLE     Molecular cloning and primary structure of Thermoactinomyces
            vulgaris carboxypeptidase T. A metalloenzyme endowed with dual
            substrate specificity.
  JOURNAL   FEBS. Lett. 291 (1991) 75-8.
  ORGANISM  Thermoactinomyces vulgaris
REFERENCE   3  [PMID:1521526]
  AUTHORS   Teplyakov A, Polyakov K, Obmolova G, Strokopytov B, Kuranova I,
            Osterman A, Grishin N, Smulevitch S, Zagnitko O, Galperina O, et al.
  TITLE     Crystal structure of carboxypeptidase T from Thermoactinomyces
            vulgaris.
  JOURNAL   Eur. J. Biochem. 208 (1992) 281-8.
  ORGANISM  Thermoactinomyces vulgaris
ORTHOLOGY   KO: K05996  carboxypeptidase T
GENES       BBA: Bd3234(cpt)
            SMA: SAV3266
            SEN: SACE_5779(cpt) SACE_5780
STRUCTURES  PDB: 1OBR  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.18
            ExPASy - ENZYME nomenclature database: 3.4.17.18
            ExplorEnz - The Enzyme Database: 3.4.17.18
            ERGO genome analysis and discovery system: 3.4.17.18
            BRENDA, the Enzyme Database: 3.4.17.18
            CAS: 89623-65-4
///
ENTRY       EC 3.4.17.19                Enzyme
NAME        carboxypeptidase Taq
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Release of a C-terminal amino acid with broad specificity, except
            for -Pro
COMMENT     A 56-kDa enzyme from Thermus aquaticus. Most active at 80_degree_ C.
            Type example of peptidase family M32
REFERENCE   1  [PMID:1369078]
  AUTHORS   Lee SH, Minagawa E, Taguchi H, Matsuzawa H, Ohta T, Kaminogawa S,
            Yamauchi K.
  TITLE     Purification and characterization of a thermostable carboxypeptidase
            (carboxypeptidase Taq) from Thermus aquaticus YT-1.
  JOURNAL   Biosci. Biotechnol. Biochem. 56 (1992) 1839-44.
  ORGANISM  Thermus aquaticus
REFERENCE   2  [PMID:7765282]
  AUTHORS   Lee SH, Taguchi H, Yoshimura E, Minagawa E, Kaminogawa S, Ohta T,
            Matsuzawa H.
  TITLE     Carboxypeptidase Taq, a thermostable zinc enzyme, from Thermus
            aquaticus YT-1: molecular cloning, sequencing, and expression of the
            encoding gene in Escherichia coli.
  JOURNAL   Biosci. Biotechnol. Biochem. 58 (1994) 1490-5.
  ORGANISM  Thermus aquaticus
ORTHOLOGY   KO: K01299  carboxypeptidase Taq
GENES       TBR: Tb11.02.0100
            TCR: 504045.60 504153.160
            LMA: LmjF13.0090 LmjF33.2540
            YPE: YPO2310
            YPK: y2141
            YPM: YP_2097
            YPA: YPA_1658
            YPN: YPN_1772
            YPP: YPDSF_0834
            YPS: YPTB2232
            ENT: Ent638_1916
            SPE: Spro_2592
            VCH: VC1414
            VCO: VC0395_A1024
            VVU: VV1_2698
            VVY: VV1592
            VPA: VP1744
            VFI: VF1457
            PPR: PBPRA1843
            SON: SO_1375
            SDN: Sden_0880 Sden_0882
            SAZ: Sama_0802
            SBL: Sbal_3102
            SBM: Shew185_3112
            SLO: Shew_0947
            SSE: Ssed_1020
            SPL: Spea_0916
            SHE: Shewmr4_2819
            SHM: Shewmr7_2902
            SHN: Shewana3_2999
            PIN: Ping_1034
            LPN: lpg1146
            LPF: lpl1152
            LPP: lpp1148
            FTL: FTL_0100
            FTH: FTH_0094
            FTN: FTN_1738
            MMW: Mmwyl1_2751
            AHA: AHA_1048
            CVI: CV_1292(ctaQ)
            RFR: Rfer_3175
            NMU: Nmul_A2170
            AZO: azo3546(ctaQ)
            AFW: Anae109_0129
            MXA: MXAN_5988
            SFU: Sfum_1978
            RTY: RT0172
            RCO: RC0228
            RFE: RF_1090 RF_1091
            RBE: RBE_1100
            OTS: OTBS_0471
            WOL: WD1257
            WBM: Wbm0153
            AMA: AM853
            APH: APH_0339
            ERU: Erum5610
            ERW: ERWE_CDS_05880
            ERG: ERGA_CDS_05790
            ECN: Ecaj_0562
            ECH: ECH_0464
            MLO: mlr3932
            PLA: Plav_0676
            XAU: Xaut_4189
            SIL: SPO2053
            SIT: TM1040_1334
            RSP: RSP_3832(cxp)
            RSH: Rsph17029_3525
            RSQ: Rsph17025_3812
            JAN: Jann_2431 Jann_4120
            RDE: RD1_2727(cxp)
            PDE: Pden_3700
            GBE: GbCGDNIH1_2252
            ACR: Acry_2162
            RRU: Rru_A3232
            MAG: amb4113
            BSU: BG11458(ypwA)
            BHA: BH2149
            BAN: BA1587
            BAR: GBAA1587
            BAA: BA_2104
            BAT: BAS1471
            BCE: BC1566
            BCA: BCE_1693
            BCZ: BCZK1444
            BCY: Bcer98_1301
            BTK: BT9727_1443
            BTL: BALH_1413
            BLI: BL00681(ypwA)
            BLD: BLi02349(ypwA)
            BCL: ABC1995
            BAY: RBAM_020270(ypwA)
            BPU: BPUM_1945(ypwA)
            GKA: GK1545
            LMO: lmo1886
            LMF: LMOf2365_1915
            LIN: lin1999
            LWE: lwe1905
            EFA: EF1153
            POY: PAM187 PAM188
            AYW: AYWB_532
            RXY: Rxyl_1098
            FNU: FN0061
            RBA: RB1579
            PCU: pc0630
            LIL: LA4322
            LIC: LIC13464
            LBJ: LBJ_2980
            LBL: LBL_0085
            SYW: SYNW1789
            SYD: Syncc9605_0676
            SYE: Syncc9902_1685
            SYG: sync_2040
            SYR: SynRCC307_0897
            SYX: SynWH7803_1803
            PMA: Pro0492
            PMM: PMM0493(cxp)
            PMT: PMT1279(cxp)
            PMN: PMN2A_1826
            PMI: PMT9312_0494
            PMC: P9515_05571
            PMF: P9303_07181
            PMG: P9301_05201
            PME: NATL1_05501
            TER: Tery_3995
            SRU: SRU_2485
            RRS: RoseRS_1549
            RCA: Rcas_2306
            DRA: DR_2423
            DGE: Dgeo_0334
            TTH: TTC1715
            TTJ: TTHA0270
            TME: Tmel_0528
            FNO: Fnod_0588
            HAL: VNG2616G(cxp)
            HMA: rrnAC2092(cxp)
            NPH: NP0944A(cxp_1)
            PHO: PH0465
            PAB: PAB1320
            PFU: PF0456
            TKO: TK1840
            APE: APE_1775.1
            SMR: Smar_1598
            SSO: SSO3105
            STO: ST1650
            SAI: Saci_1661(taq)
            MSE: Msed_0344
            PAI: PAE0885
            PIS: Pisl_1143
            PCL: Pcal_0069
            PAS: Pars_0104
            NEQ: NEQ042
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.19
            ExPASy - ENZYME nomenclature database: 3.4.17.19
            ExplorEnz - The Enzyme Database: 3.4.17.19
            ERGO genome analysis and discovery system: 3.4.17.19
            BRENDA, the Enzyme Database: 3.4.17.19
///
ENTRY       EC 3.4.17.20                Enzyme
NAME        carboxypeptidase U;
            arginine carboxypeptidase;
            carboxypeptidase R;
            plasma carboxypeptidase B (misleading, since the term
            carboxypeptidase B is used for other enzymes);
            thrombin-activatable fibrinolysis inhibitor
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Release of C-terminal Arg and Lys from a polypeptide
COFACTOR    Zinc [CPD:C00038]
COMMENT     Pro-carboxypeptidase U in (human) plasma is activated by thrombin or
            plasmin during clotting to form the unstable carboxypeptidase U,
            with activity similar to that of the more stable lysine
            carboxypeptidase, except that no preference is shown for Lys over
            Arg. A zinc enzyme, in peptidase family M14 (carboxypeptidase A
            family)
REFERENCE   1  [PMID:1939207]
  AUTHORS   Eaton DL, Malloy BE, Tsai SP, Henzel W, Drayna D.
  TITLE     Isolation, molecular cloning, and partial characterization of a
            novel carboxypeptidase B from human plasma.
  JOURNAL   J. Biol. Chem. 266 (1991) 21833-8.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:8130654]
  AUTHORS   Shinohara T, Sakurada C, Suzuki T, Takeuchi O, Campbell W, Ikeda S,
            Okada N, Okada H.
  TITLE     Pro-carboxypeptidase R cleaves bradykinin following activation.
  JOURNAL   Int. Arch. Allergy. Immunol. 103 (1994) 400-4.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:8195249]
  AUTHORS   Wang W, Hendriks DF, Scharpe SS.
  TITLE     Carboxypeptidase U, a plasma carboxypeptidase with high affinity for
            plasminogen.
  JOURNAL   J. Biol. Chem. 269 (1994) 15937-44.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:7727441]
  AUTHORS   Tan AK, Eaton DL.
  TITLE     Activation and characterization of procarboxypeptidase B from human
            plasma.
  JOURNAL   Biochemistry. 34 (1995) 5811-6.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:8916945]
  AUTHORS   Broze GJ Jr, Higuchi DA.
  TITLE     Coagulation-dependent inhibition of fibrinolysis: role of
            carboxypeptidase-U and the premature lysis of clots from hemophilic
            plasma.
  JOURNAL   Blood. 88 (1996) 3815-23.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01300  carboxypeptidase B2 (plasma, carboxypeptidase U)
GENES       HSA: 1361(CPB2)
            PTR: 452582(CPB2)
            MMU: 56373(Cpb2)
            RNO: 113936(Cpb2)
            CFA: 608910(CPB2)
            BTA: 508222(MGC137155)
            GGA: 418851(CPB2)
            XTR: 595005(MGC108395)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.20
            ExPASy - ENZYME nomenclature database: 3.4.17.20
            ExplorEnz - The Enzyme Database: 3.4.17.20
            ERGO genome analysis and discovery system: 3.4.17.20
            BRENDA, the Enzyme Database: 3.4.17.20
            CAS: 156621-18-0
///
ENTRY       EC 3.4.17.21                Enzyme
NAME        glutamate carboxypeptidase II;
            N-acetylated-gamma-linked-acidic dipeptidase (NAALADase);
            folate hydrolase;
            prostate-specific membrane antigen;
            pteroylpoly-gamma-glutamate carboxypeptidase;
            microsomal gamma-glutamyl carboxypeptidase;
            pteroylpolyglutamate hydrolase;
            folylpolyglutamate hydrolase;
            pteroylpoly-gamma-glutamate hydrolase;
            pteroylpolygammaglutamyl hydrolase;
            pteroylpolyglutamate hydrolase;
            pteroylpolyglutamic acid hydrolase;
            PSM antigen;
            acetylaspartylglutamate dipeptidase;
            NAALA dipeptidase;
            rat NAAG peptidase;
            mGCP;
            membrane glutamate carboxypeptidase;
            N-acetylated-alpha-linked-amino dipeptidase;
            prostrate-specific membrane antigen;
            N-Acetylated alpha-linked acidic dipeptidase;
            PSMA
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Release of an unsubstituted, C-terminal glutamyl residue, typically
            from Ac-Asp-Glu or folylpoly-gamma-glutamates
EFFECTOR    Metal [CPD:C00050]
COMMENT     A metallo-carboxypeptidase that is predominantly expressed as a
            membrane-bound enzyme of 94-100 kDa , but also exists in a soluble
            form. Hydrolyses alpha-peptide bonds in Ac-Asp-Glu, Asp-Glu, and
            Glu-Glu, but also gamma-glutamyl bonds in gamma-Glu-Glu, and
            folylpoly-gamma-glutamates. With folylpoly-gamma-glutamates, shows
            processive carboxypeptidase activity to produce pteroylmonoglutamate
            [4]. Does not hydrolyse Ac-beta-Asp-Glu. Known inhibitors:
            quisqualic acid, Ac-beta-Asp-Glu, and
            2-phosphonomethyl-pentanedioate. In peptidase family M28 of Vibrio
            leucyl aminopeptidase. The release of C-terminal glutamate from
            folylpoly-gamma-glutamates is also catalysed by EC 3.4.17.11
            (glutamate carboxypeptidase) and EC 3.4.19.9 (gamma-Glu-X
            carboxypeptidase).
REFERENCE   1  [PMID:9123729]
  AUTHORS   Heston WD.
  TITLE     Characterization and glutamyl preferring carboxypeptidase function
            of prostate specific membrane antigen: a novel folate hydrolase.
  JOURNAL   Urology. 49 (1997) 104-12.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:9187245]
  AUTHORS   Rawlings ND, Barrett AJ.
  TITLE     Structure of membrane glutamate carboxypeptidase.
  JOURNAL   Biochim. Biophys. Acta. 1339 (1997) 247-52.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:9685395]
  AUTHORS   Halsted CH, Ling EH, Luthi-Carter R, Villanueva JA, Gardner JM,
            Coyle JT.
  TITLE     Folylpoly-gamma-glutamate carboxypeptidase from pig jejunum.
            Molecular characterization and relation to glutamate
            carboxypeptidase II.
  JOURNAL   J. Biol. Chem. 273 (1998) 20417-24.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:9501243]
  AUTHORS   Luthi-Carter R, Berger UV, Barczak AK, Enna M, Coyle JT.
  TITLE     Isolation and expression of a rat brain cDNA encoding glutamate
            carboxypeptidase II.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 3215-20.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K01301  glutamate carboxypeptidase II
GENES       HSA: 10003(NAALAD2) 10004(NAALADL1) 2346(FOLH1)
            PTR: 451475(LOC451475)
            MMU: 381204(Naaladl1) 53320(Folh1) 72560(Naalad2)
            RNO: 300384(Naalad2_predicted) 83568(Naaladl1) 85309(Folh1)
            CFA: 476775(LOC476775) 483751(NAALADL1) 485139(NAALAD2)
            BTA: 505865(MGC152047) 506692(LOC506692)
            SSC: 397677(FOLH1)
            GGA: 419010(NAALAD2)
            XTR: 594947(MGC69500)
            DRE: 393247(zgc:56429)
            SPU: 579656(LOC579656)
            ATH: AT3G54720(AMP1)
            OSA: 4326550
            CME: CMT078C
            PIC: PICST_33956(VPS70) PICST_72031(GCP1)
            ANI: AN4018.2
            AOR: AO090003000972
            ABA: Acid345_2466 Acid345_2819 Acid345_2823
            SUS: Acid_4582
            RHA: RHA1_ro02185
            SEN: SACE_0204 SACE_6113
STRUCTURES  PDB: 1Z8L  2C6C  2C6G  2C6P  2CIJ  2JBJ  2JBK  2OOT  2OR4  2PVV  
                 2PVW  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.21
            ExPASy - ENZYME nomenclature database: 3.4.17.21
            ExplorEnz - The Enzyme Database: 3.4.17.21
            ERGO genome analysis and discovery system: 3.4.17.21
            BRENDA, the Enzyme Database: 3.4.17.21
            CAS: 111070-04-3
///
ENTRY       EC 3.4.17.22                Enzyme
NAME        metallocarboxypeptidase D;
            carboxypeptidase D (cattle, human, mouse, rat);
            gp180 (duck)
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metallocarboxypeptidases
REACTION    Releases C-terminal Arg and Lys from polypeptides
COFACTOR    Zinc [CPD:C00038]
COMMENT     Activated by Co2+; inhibited by guanidinoethylmercaptosuccinic acid.
            Large molecule (180 kDa) because of presence of three copies of
            metallopeptidase domain. The product of the silver gene (Drosophila)
            is similar. A zinc metallopeptidase in peptidase family M14
            (carboxypeptidase A family)
REFERENCE   1  [PMID:9525948]
  AUTHORS   Eng FJ, Novikova EG, Kuroki K, Ganem D, Fricker LD.
  TITLE     gp180, a protein that binds duck hepatitis B virus particles, has
            metallocarboxypeptidase D-like enzymatic activity.
  JOURNAL   J. Biol. Chem. 273 (1998) 8382-8.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:7559630]
  AUTHORS   Song L, Fricker LD.
  TITLE     Purification and characterization of carboxypeptidase D, a novel
            carboxypeptidase E-like enzyme, from bovine pituitary.
  JOURNAL   J. Biol. Chem. 270 (1995) 25007-13.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:8910535]
  AUTHORS   Song L, Fricker LD.
  TITLE     Tissue distribution and characterization of soluble and
            membrane-bound forms of metallocarboxypeptidase D.
  JOURNAL   J. Biol. Chem. 271 (1996) 28884-9.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K07752  carboxypeptidase D
GENES       HSA: 1362(CPD)
            MMU: 12874(Cpd)
            RNO: 25306(Cpd)
            CFA: 480636(CPD)
            GGA: 417590(CPD)
            DRE: 563008(LOC563008)
            SPU: 593440(LOC593440)
            DME: Dmel_CG4122(svr)
            CEL: F59A3.1(carboxypeptidase)
            OSA: 4340100
            DDI: DDBDRAFT_0219394
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.17.22
            ExPASy - ENZYME nomenclature database: 3.4.17.22
            ExplorEnz - The Enzyme Database: 3.4.17.22
            ERGO genome analysis and discovery system: 3.4.17.22
            BRENDA, the Enzyme Database: 3.4.17.22
            CAS: 153967-26-1
///
ENTRY       EC 3.4.18.1                 Enzyme
NAME        cathepsin X;
            cathepsin B2;
            cysteine-type carboxypeptidase;
            cathepsin IV;
            cathepsin Z;
            acid carboxypeptidase;
            lysosomal carboxypeptidase B
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine-type carboxypeptidases
REACTION    Release of C-terminal amino acid residues with broad specificity,
            but lacks action on C-terminal proline. Shows weak endopeptidase
            activity
COMMENT     Cathepsin X is a lysosomal cysteine peptidase of family C1 (papain
            family). The pH optimum is dependent on the substrate and is 5.0 for
            the carboxypeptidase activity. Unstable above pH 7.0. Compound E-64,
            leupeptin and antipain are inhibitors, but not cystatin C. Cathepsin
            X is ubiquitously distributed in mammalian tissues. The propeptide
            is extremely short (38 amino acid residues) and the proenzyme is
            catalytically active. Human gene locus: 20q13.
REFERENCE   1  [PMID:9642240]
  AUTHORS   Santamaria I, Velasco G, Pendas AM, Fueyo A, Lopez-Otin C.
  TITLE     Cathepsin Z, a novel human cysteine proteinase with a short
            propeptide domain and a unique chromosomal location.
  JOURNAL   J. Biol. Chem. 273 (1998) 16816-23.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:9738465]
  AUTHORS   Nagler DK, Menard R.
  TITLE     Human cathepsin X: a novel cysteine protease of the papain family
            with a very short proregion and unique insertions.
  JOURNAL   FEBS. Lett. 434 (1998) 135-9.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:9642240]
  AUTHORS   Santamaria I, Velasco G, Pendas AM, Fueyo A, Lopez-Otin C.
  TITLE     Cathepsin Z, a novel human cysteine proteinase with a short
            propeptide domain and a unique chromosomal location.
  JOURNAL   J. Biol. Chem. 273 (1998) 16816-23.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:577]
  AUTHORS   McDonald JK, Ellis S.
  TITLE     On the substrate specificity of cathepsins B1 and B2 including a new
            fluorogenic substrate for cathepsin B1.
  JOURNAL   Life. Sci. 17 (1975) 1269-76.
  ORGANISM  cow [GN:bta]
REFERENCE   5  [PMID:1122298]
  AUTHORS   Otto K, Riesenkonig H.
  TITLE     Improved purification of cathepsin B1 and cathepsin B2.
  JOURNAL   Biochim. Biophys. Acta. 379 (1975) 462-75.
  ORGANISM  cow [GN:bta]
REFERENCE   6  [PMID:4429705]
  AUTHORS   Ninjoor V, Taylor SL, Tappel AL.
  TITLE     Purification and characterization of rat liver lysosomal cathepsin
            B2.
  JOURNAL   Biochim. Biophys. Acta. 370 (1974) 308-21.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K08568  cathepsin X
GENES       HSA: 1522(CTSZ)
            MMU: 64138(Ctsz)
            RNO: 252929(Ctsz)
            CFA: 611983(CTSZ)
            BTA: 404187(CTSZ)
            GGA: 419311(CTSZ)
            XLA: 432187(MGC82409)
            DRE: 450022(zgc:103420)
            SPU: 583170(LOC583170)
            CEL: F32B5.8(cpz-1)
            DDI: DDBDRAFT_0185484
STRUCTURES  PDB: 1EF7  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.18.1
            ExPASy - ENZYME nomenclature database: 3.4.18.1
            ExplorEnz - The Enzyme Database: 3.4.18.1
            ERGO genome analysis and discovery system: 3.4.18.1
            BRENDA, the Enzyme Database: 3.4.18.1
            CAS: 37217-21-3
///
ENTRY       EC 3.4.19.1                 Enzyme
NAME        acylaminoacyl-peptidase;
            acylamino-acid-releasing enzyme;
            N-acylpeptide hydrolase;
            N-formylmethionine (fMet) aminopeptidase;
            alpha-N-acylpeptide hydrolase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Omega peptidases
REACTION    Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus
            of a polypeptide
INHIBITOR   Isoflurophate [CPD:C00202]
COMMENT     Active at neutral pH. Several variants of this enzyme exist; the
            human erythrocyte enzyme is relatively specific for removal of
            N-acetylalanine from peptides. Displays dipeptidyl-peptidase
            activity on glycyl-peptides, perhaps as a result of mis-recognition
            of the glycyl residue as an uncharged N-acyl group. Inhibited by
            diisopropyl fluorophosphate. In peptidase family S9 (prolyl
            oligopeptidase family).
REFERENCE   1  [PMID:1137989]
  AUTHORS   Tsunasawa S, Narita K, Ogata K.
  TITLE     Purification and properties of acylamino acid-releasing enzyme from
            rat liver.
  JOURNAL   J. Biochem. (Tokyo). 77 (1975) 89-102.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:477668]
  AUTHORS   Unger T, Nagelschmidt M, Struck H.
  TITLE     N-Acetylaminoacyl-p-nitranilidase from human placenta. Purification
            and some properties.
  JOURNAL   Eur. J. Biochem. 97 (1979) 205-11.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:3305492]
  AUTHORS   Kobayashi K, Smith JA.
  TITLE     Acyl-peptide hydrolase from rat liver. Characterization of enzyme
            reaction.
  JOURNAL   J. Biol. Chem. 262 (1987) 11435-45.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K01303  acylaminoacyl-peptidase
GENES       HSA: 327(APEH)
            PTR: 460376(APEH)
            MMU: 235606(Apeh)
            RNO: 24206(Apeh)
            CFA: 476622(APEH)
            BTA: 514666(MGC139504)
            SSC: 396961(APEH)
            GGA: 415926(RCJMB04_19g24)
            DRE: 321028(apeh)
            CEL: R11E3.8(dpf-5)
            ATH: AT4G14570
            OSA: 4348626
            CME: CMT228C
            DDI: DDBDRAFT_0184409
            CPV: cgd5_4370
            CHO: Chro.50405
            TET: TTHERM_00449000 TTHERM_00449010 TTHERM_00856550
            ECI: UTI89_C1599
            ILO: IL0039
            PHA: PSHAa0132 PSHAa1986
            BRA: BRADO3729
            BCE: BC0192
            BCL: ABC2617
            BAY: RBAM_029340(yuxL)
            OIH: OB1081
            GKA: GK0961
            LSL: LSL_1001
            LDB: Ldb1011
            LBR: LVIS_2137
            ACE: Acel_2009
            FNU: FN1128
            SRU: SRU_2034
            TTH: TTC1241
            APE: APE_1547.1 APE_1832 APE_2290.1
            SMR: Smar_0411
STRUCTURES  PDB: 1VE6  1VE7  2HU5  2HU7  2HU8  2QZP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.19.1
            ExPASy - ENZYME nomenclature database: 3.4.19.1
            ExplorEnz - The Enzyme Database: 3.4.19.1
            ERGO genome analysis and discovery system: 3.4.19.1
            BRENDA, the Enzyme Database: 3.4.19.1
            CAS: 73562-30-8
///
ENTRY       EC 3.4.19.2                 Enzyme
NAME        peptidyl-glycinamidase;
            carboxyamidase;
            peptidyl carboxy-amidase;
            peptidyl-aminoacylamidase;
            carboxamidopeptidase;
            peptidyl amino acid amide hydrolase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Omega peptidases
REACTION    Cleavage of C-terminal glycinamide from polypeptides
INHIBITOR   Isoflurophate [CPD:C00202]
COMMENT     Inactivates vasopressin and oxytocin by splitting off glycinamide.
            Also cleaves ester substrates of trypsin and chymotrypsin. Although
            glycinamide is by far the preferred leaving group, other
            aminoacylamides may also be released, e.g. phenylalaninamide. The
            toad skin enzyme is inhibited by diisopropyl fluorophosphate.
REFERENCE   1
  AUTHORS   Fruhaufova, L., Suska-Brezezinska, E., Barth, T. and Rychlik, I.
  TITLE     Rat liver enzyme inactivating oxytocin and its deamino-carba
            analogues.
  JOURNAL   Coll. Czech. Chem. Commun. 38 (1973) 2793-2798.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:1122284]
  AUTHORS   Nardacci NJ, Mukhopadhyay S, Campbell BJ.
  TITLE     Partial purification and characterization of the antidiuretic
            hormone-inactivating enzyme from renal plasma membranes.
  JOURNAL   Biochim. Biophys. Acta. 377 (1975) 146-57.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:6766314]
  AUTHORS   Simmons WH, Walter R.
  TITLE     Carboxamidopeptidase: purification and characterization of a
            neurohypophyseal hormone inactivating peptidase from toad skin.
  JOURNAL   Biochemistry. 19 (1980) 39-48.
  ORGANISM  frog
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.19.2
            ExPASy - ENZYME nomenclature database: 3.4.19.2
            ExplorEnz - The Enzyme Database: 3.4.19.2
            ERGO genome analysis and discovery system: 3.4.19.2
            BRENDA, the Enzyme Database: 3.4.19.2
            CAS: 94047-14-0
///
ENTRY       EC 3.4.19.3                 Enzyme
NAME        pyroglutamyl-peptidase I;
            5-oxoprolyl-peptidase;
            pyrase;
            pyroglutamate aminopeptidase;
            pyroglutamyl aminopeptidase;
            L-pyroglutamyl peptide hydrolase;
            pyrrolidone-carboxyl peptidase;
            pyrrolidone-carboxylate peptidase;
            pyrrolidonyl peptidase;
            L-pyrrolidonecarboxylate peptidase;
            pyroglutamidase;
            pyrrolidonecarboxylyl peptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Omega peptidases
REACTION    Release of an N-terminal pyroglutamyl group from a polypeptide, the
            second amino acid generally not being Pro
INHIBITOR   Thiol-blocking reagent [CPD:C00648]
COMMENT     A cysteine peptidase, known from bacteria, plants and animals. The
            enzyme from bacterial sources is used in protein sequencing, and is
            the type example of peptidase family C15.
REFERENCE   1
  AUTHORS   Tsuru, D., Nakamura, K., Yoshimoto, T. and Fujiwara, K.
  TITLE     Pyroglutamyl-peptidase from Bacillus amyloliquefaciens. An improved
            purification method and some properties of the enzyme.
  JOURNAL   Biochim. Biophys. Acta 791 (1984) 117-122.
  ORGANISM  Bacillus amyloliquefaciens
REFERENCE   2  [PMID:7824521]
  AUTHORS   Awade AC, Cleuziat P, Gonzales T, Robert-Baudouy J.
  TITLE     Pyrrolidone carboxyl peptidase (Pcp): an enzyme that removes
            pyroglutamic acid (pGlu) from pGlu-peptides and pGlu-proteins.
  JOURNAL   Proteins. 20 (1994) 34-51.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:8529900]
  AUTHORS   Patti JM, Schneider A, Garza N, Boles JO.
  TITLE     Isolation and characterization of pcp, a gene encoding a pyrrolidone
            carboxyl peptidase in Staphylococcus aureus.
  JOURNAL   Gene. 166 (1995) 95-9.
  ORGANISM  Staphylococcus aureus
REFERENCE   4  [PMID:8655512]
  AUTHORS   Le Saux O, Gonzales T, Robert-Baudouy J.
  TITLE     Mutational analysis of the active site of Pseudomonas fluorescens
            pyrrolidone carboxyl peptidase.
  JOURNAL   J. Bacteriol. 178 (1996) 3308-13.
  ORGANISM  Pseudomonas fluorescens
ORTHOLOGY   KO: K01304  pyroglutamyl-peptidase
GENES       HSA: 54858(PGPEP1)
            MMU: 66522(Pgpep1)
            RNO: 290648(Pgpep1)
            CFA: 484823(PGPEP1)
            BTA: 615089(LOC615089)
            GGA: 420127(PGPEP1)
            XTR: 448426(pgpep1)
            DRE: 553547(zgc:109902)
            SPU: 581828(LOC581828)
            DME: Dmel_CG32147
            UMA: UM02263.1
            TET: TTHERM_00349070 TTHERM_00527300
            TBR: Tb927.4.2670
            TCR: 506635.60
            LMA: LmjF34.2000
            YPE: YPO2703(pcp)
            YPK: y1280
            YPM: YP_2507(pcp1)
            YPA: YPA_2436
            YPN: YPN_1191
            YPP: YPDSF_1568
            YPS: YPTB2905(pcp)
            YPI: YpsIP31758_1120(pcp)
            ECA: ECA1354(pcp)
            PLU: plu4303(pcp) plu4418
            SGL: SG1848
            ENT: Ent638_1219
            SPE: Spro_1260 Spro_2993
            VVU: VV2_1257
            VVY: VVA0085
            VPA: VPA0587
            VFI: VF1370
            SAZ: Sama_0018
            PHA: PSHAa1441
            FTU: FTT0296(pcp)
            FTF: FTF0296(pcp)
            FTW: FTW_1789(pcp)
            FTL: FTL_0207
            FTH: FTH_0202(pcp)
            FTA: FTA_0223(pcp)
            FTN: FTN_0211(pcp)
            CVI: CV_3176(pcp1)
            RSO: RSc2165(pcp1) RSp0259(pcp2)
            REU: Reut_A0092
            REH: H16_A0129(pcp)
            RME: Rmet_0067
            RFR: Rfer_0871
            POL: Bpro_1512
            BBA: Bd0879(pcp)
            BJA: bll3047
            BRA: BRADO2676
            BBT: BBta_3018
            RPA: RPA1828
            RPB: RPB_3543
            RPC: RPC_1753
            RPD: RPD_1921
            RPE: RPE_1845
            NWI: Nwi_2241
            NHA: Nham_2644
            SWI: Swit_0885
            ACR: Acry_2286
            BSU: BG10873(pcp)
            BHA: BH3631(pcp)
            BAN: BA3090(pcP)
            BAR: GBAA3090(pcP)
            BAA: BA_3595
            BAT: BAS2875
            BCE: BC3063
            BCA: BCE_3116(pcp)
            BCZ: BCZK2805(pcp)
            BCY: Bcer98_2056
            BTK: BT9727_2844(pcp)
            BTL: BALH_2757
            BLI: BL02514(pcp)
            BLD: BLi03263(pcp)
            BCL: ABC3089(pcp)
            BAY: RBAM_002960
            OIH: OB2539
            SAU: SA2482(pcp)
            SAV: SAV2690(pcp)
            SAM: MW2610(pcp)
            SAR: SAR2772(pcp)
            SAS: SAS2576
            SAC: SACOL2714(pcp)
            SAB: SAB2566(pcp)
            SAA: SAUSA300_2623(pcp)
            SAO: SAOUHSC_03025
            SAJ: SaurJH9_2714
            SAH: SaurJH1_2771
            SEP: SE0261
            SER: SERP2317(pcp)
            SHA: SH0293(pcp)
            SSP: SSP0471
            LLC: LACR_C27
            LLM: llmg_0663(pcp)
            SPY: SPy_0506(pcp)
            SPZ: M5005_Spy_0417(pcp)
            SPM: spyM18_0565(pcp)
            SPG: SpyM3_0355(pcp)
            SPS: SPs1498
            SPH: MGAS10270_Spy0418(pcp)
            SPI: MGAS10750_Spy0430(pcp)
            SPJ: MGAS2096_Spy0436(pcp)
            SPK: MGAS9429_Spy0416(pcp)
            SPF: SpyM51453(pcp)
            SPA: M6_Spy0444
            SPB: M28_Spy0405(pcp)
            SPN: SP_0860 SP_2060
            SPR: spr0762(pcp) spr1871 spr1872
            SPD: SPD_0753(pcp)
            LJO: LJ1798
            LAC: LBA0186
            LDB: Ldb1175(pcp)
            LBU: LBUL_1093
            LBR: LVIS_1994
            LCA: LSEI_0206
            LGA: LGAS_1832
            EFA: EF0401(pcp)
            CPE: CPE1425
            CPF: CPF_1678(pcp)
            CPR: CPR_1413(pcp)
            CDF: CD1676(pcp)
            TTE: TTE0678(pcp) TTE1612(pcp2)
            MTU: Rv0319(pcp)
            MTC: MT0334(pcp)
            MBO: Mb0327(pcp)
            MBB: BCG_0359(pcp)
            SCO: SCO0438(pcp)
            ART: Arth_1486
            AAU: AAur_1621(pcp)
            BLO: BL0323(pcp)
            BAD: BAD_0270(pcp)
            FNU: FN1728
            RBA: RB3898(pcp)
            TDE: TDE0175(pcp)
            GVI: glr2409
            ANA: alr1369
            AVA: Ava_4016
            RRS: RoseRS_1774
            RCA: Rcas_2052
            DRA: DR_0490
            DGE: Dgeo_0441
            TTH: TTC0531
            TTJ: TTHA0888
            TME: Tmel_0762
            FNO: Fnod_0998
            PHO: PH0596
            PAB: PAB1419
            PFU: PF1299
            TKO: TK1835
            HBU: Hbut_1614
            SSO: SSO1465(pcp) SSO1607(pcp-like)
            SAI: Saci_1780(pcp)
            TPE: Tpen_1586
STRUCTURES  PDB: 1A2Z  1AUG  1IOF  1IOI  1IU8  1X10  1X12  1Z8T  1Z8W  1Z8X  
                 2DF5  2EBJ  2EO8  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.19.3
            ExPASy - ENZYME nomenclature database: 3.4.19.3
            ExplorEnz - The Enzyme Database: 3.4.19.3
            ERGO genome analysis and discovery system: 3.4.19.3
            BRENDA, the Enzyme Database: 3.4.19.3
            CAS: 9075-21-2
///
ENTRY       EC 3.4.19.4       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Omega peptidases
COMMENT     Deleted entry: N-Acetylmethionylpeptide peptidase (EC 3.4.19.4
            created 1989, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.19.4
            ExPASy - ENZYME nomenclature database: 3.4.19.4
            ExplorEnz - The Enzyme Database: 3.4.19.4
            ERGO genome analysis and discovery system: 3.4.19.4
            BRENDA, the Enzyme Database: 3.4.19.4
///
ENTRY       EC 3.4.19.5                 Enzyme
NAME        beta-aspartyl-peptidase;
            beta-aspartyl dipeptidase;
            beta-aspartyl peptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Omega peptidases
REACTION    Cleavage of a beta-linked Asp residue from the N-terminus of a
            polypeptide
COMMENT     Other isopeptide bonds, e.g. gamma-glutamyl and beta-alanyl, are not
            hydrolysed. A mammalian, cytosolic enzyme.
REFERENCE   1
  AUTHORS   Haley, E.E.
  TITLE     beta-Aspartyl peptidase from rat liver.
  JOURNAL   Methods Enzymol. 19 (1970) 737-741.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K01305  beta-aspartyl-peptidase
GENES       ECO: b4328(iadA)
            ECJ: JW4291(iadA)
            ECE: Z5927(iadA)
            ECS: ECs5286
            ECC: c5408(iadA)
            ECI: UTI89_C5038(iadA)
            ECP: ECP_4664
            ECW: EcE24377A_4927(iadA)
            ECX: EcHS_A4556
            STY: STY4868(iadA)
            STT: t4562(iadA)
            SPT: SPA4332(iadA)
            SEC: SC4367(iadA)
            STM: STM4512(iadA)
            SFL: SF4190(iadA)
            SFX: S4446(iadA)
            SFV: SFV_4198(iadA)
            SBO: SBO_4379(iadA)
            VVU: VV2_1131
            VFI: VF1509
            PPR: PBPRA1536
            CPS: CPS_1869(iadA)
            CSA: Csal_1115
            CCV: CCV52592_0185(iadA)
            CCO: CCC13826_0178(iadA) CCC13826_0552(iadA)
            BHA: BH1129
            CPE: CPE2356
            CPF: CPF_2665(iadA)
            CPR: CPR_2351(iadA)
            DSY: DSY1818
            SWO: Swol_1352
            TTE: TTE0837
STRUCTURES  PDB: 1SEO  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.19.5
            ExPASy - ENZYME nomenclature database: 3.4.19.5
            ExplorEnz - The Enzyme Database: 3.4.19.5
            ERGO genome analysis and discovery system: 3.4.19.5
            BRENDA, the Enzyme Database: 3.4.19.5
            CAS: 37288-74-7
///
ENTRY       EC 3.4.19.6                 Enzyme
NAME        pyroglutamyl-peptidase II;
            thyroliberinase;
            pyroglutamyl aminopeptidase II;
            , thyrotropin-releasing factor pyroglutamate aminopeptidase;
            pyroglutamate aminopeptidase II;
            pyroglutamyl peptidase II;
            thyroliberin-hydrolyzing pyroglutamate aminopeptidase;
            thyrotropin-releasing hormone-degrading pyroglutamate
            aminopeptidase;
            thyrotropin-releasing hormone-degrading peptidase;
            TRH aminopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Omega peptidases
REACTION    Release of the N-terminal pyroglutamyl group from pGlu!His-Xaa
            tripeptides and pGlu!His-Xaa-Gly tetrapeptides
INHIBITOR   Metal chelator [CPD:C02169]
COMMENT     Highly specific for thyrotropin releasing hormone
            (pyroglutamyl-histidyl-prolylamide). Will not cleave the
            pyroglutamyl-histidyl bond of luteinizing hormone releasing hormone.
            Found in serum and brain. Inhibited by metal chelators. In peptidase
            family M1 (membrane alanyl aminopeptidase family)
REFERENCE   1  [PMID:115687]
  AUTHORS   Bauer K, Nowak P.
  TITLE     Characterization of a thyroliberin-degrading serum enzyme catalyzing
            the hydrolysis of thyroliberin at the pyroglutamyl-histidine bond.
  JOURNAL   Eur. J. Biochem. 99 (1979) 239-46.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:2862039]
  AUTHORS   O'Connor B, O'Cuinn G.
  TITLE     Purification of and kinetic studies on a narrow specificity
            synaptosomal membrane pyroglutamate aminopeptidase from guinea-pig
            brain.
  JOURNAL   Eur. J. Biochem. 150 (1985) 47-52.
  ORGANISM  guinea pig
REFERENCE   3
  AUTHORS   Wilk, S. and Wilk, E.K.
  TITLE     Pyroglutamyl peptidase II, a thyrotropin releasing hormone degrading
            enzyme: purification and specificity studies of the rabbit brain
            enzyme.
  JOURNAL   Neurochem. Int. 15 (1989) 81-89.
  ORGANISM  rabbit
ORTHOLOGY   KO: K01306  pyroglutamyl-peptidase II
GENES       HSA: 29953(TRHDE)
            PTR: 467071(TRHDE)
            MMU: 237553(Trhde)
            RNO: 366894(Trhde)
            BTA: 509809(LOC509809)
            GGA: 427868(TRHDE)
            DRE: 562409(LOC562409)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.19.6
            ExPASy - ENZYME nomenclature database: 3.4.19.6
            ExplorEnz - The Enzyme Database: 3.4.19.6
            ERGO genome analysis and discovery system: 3.4.19.6
            BRENDA, the Enzyme Database: 3.4.19.6
            CAS: 60063-88-9
///
ENTRY       EC 3.4.19.7                 Enzyme
NAME        N-formylmethionyl-peptidase;
            (fMet)-releasing enzyme;
            formylmethionine aminopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Omega peptidases
REACTION    Release of an N-terminal, formyl-methionyl residue from a
            polypeptide
INHIBITOR   Heavy metal [CPD:C01815]
EFFECTOR    Chloride [CPD:C00115]
COMMENT     Highly specific for N-formylmethionyl peptides. Will not cleave
            methionyl peptides or N-formyl derivatives of amino acids other than
            methionine. Isolated from rat liver. Inhibited by heavy metals and
            activated by Cl-
REFERENCE   1  [PMID:7437450]
  AUTHORS   Suda H, Yamamoto K, Aoyagi T, Umezawa H.
  TITLE     Purification and properties of N-formylmethionine aminopeptidase
            from rat liver.
  JOURNAL   Biochim. Biophys. Acta. 616 (1980) 60-7.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.19.7
            ExPASy - ENZYME nomenclature database: 3.4.19.7
            ExplorEnz - The Enzyme Database: 3.4.19.7
            ERGO genome analysis and discovery system: 3.4.19.7
            BRENDA, the Enzyme Database: 3.4.19.7
            CAS: 76106-80-4
///
ENTRY       EC 3.4.19.8       Obsolete  Enzyme
NAME        Transferred to 3.4.17.21
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Omega peptidases
COMMENT     Transferred entry: now EC 3.4.17.21 glutamate carboxypeptidase II
            (EC 3.4.19.8 created 1992, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.19.8
            ExPASy - ENZYME nomenclature database: 3.4.19.8
            ExplorEnz - The Enzyme Database: 3.4.19.8
            ERGO genome analysis and discovery system: 3.4.19.8
            BRENDA, the Enzyme Database: 3.4.19.8
///
ENTRY       EC 3.4.19.9                 Enzyme
NAME        gamma-glutamyl hydrolase;
            conjugase;
            folate conjugase;
            lysosomal gamma-glutamyl carboxypeptidase;
            gamma-Glu-X carboxypeptidase;
            pteroyl-poly-gamma-glutamate hydrolase;
            carboxypeptidase G;
            folic acid conjugase;
            poly(gamma-glutamic acid) endohydrolase;
            polyglutamate hydrolase;
            poly(glutamic acid) hydrolase II;
            pteroylpoly-gamma-glutamyl hydrolase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Omega peptidases
REACTION    Hydrolysis of a gamma-glutamyl bond
ALL_REAC    (other) R04242
COMMENT     A lysosomal or secreted, thiol-dependent peptidase, most active at
            acidic pH. Commonly studied with folylpoly-gamma-glutamate as
            substrate, with which the initial cleavage may release glutamate or
            poly-gamma-glutamate of two or more residues, according to the
            species of origin of the enzyme. Final products are
            pteroyl-alpha-glutamate (folic acid) and free glutamate. Highly
            specific for the gamma-glutamyl bond, but not for the C-terminal
            amino acid (leaving group). Action on gamma-glutamyl bonds is
            independent of an N-terminal pteroyl moiety, but it is not known
            whether an N-terminal gamma-Glu residue can be hydrolysed. Type
            example of peptidase family C26.
REFERENCE   1
  AUTHORS   McGuire, J.J. and Coward, J.K.
  TITLE     Pteroylpolyglutamates: biosynthesis, degradation and function.
  JOURNAL   In: Blakley, R.L. and Benkovic, S.J. (Eds.), Folates and Pterins,
            John Wiley and Sons, New York, 1984, p. 135-191.
REFERENCE   2  [PMID:8343522]
  AUTHORS   Wang Y, Nimec Z, Ryan TJ, Dias JA, Galivan J.
  TITLE     The properties of the secreted gamma-glutamyl hydrolases from H35
            hepatoma cells.
  JOURNAL   Biochim. Biophys. Acta. 1164 (1993) 227-35.
  ORGANISM  human [GN:hsa], rat [GN:rno], cow [GN:bta], chicken [GN:gga]
REFERENCE   3  [PMID:7565632]
  AUTHORS   Yao R, Rhee MS, Galivan J.
  TITLE     Effects of gamma-glutamyl hydrolase on folyl and
            antifolylpolyglutamates in cultured H35 hepatoma cells.
  JOURNAL   Mol. Pharmacol. 48 (1995) 505-11.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:8816764]
  AUTHORS   Yao R, Schneider E, Ryan TJ, Galivan J.
  TITLE     Human gamma-glutamyl hydrolase: cloning and characterization of the
            enzyme expressed in vitro.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 10134-8.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:8621474]
  AUTHORS   Yao R, Nimec Z, Ryan TJ, Galivan J.
  TITLE     Identification, cloning, and sequencing of a cDNA coding for rat
            gamma-glutamyl hydrolase.
  JOURNAL   J. Biol. Chem. 271 (1996) 8525-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K01307  gamma-glutamyl hydrolase
GENES       HSA: 8836(GGH)
            PTR: 464204(GGH)
            MMU: 14590(Ggh)
            RNO: 25455(Ggh)
            CFA: 477896(GGH)
            BTA: 525303(LOC525303)
            GGA: 421144(GGH)
            XLA: 444589(MGC84044)
            XTR: 594986(ggh)
            DRE: 406624(ggh)
            SPU: 582718(LOC582718)
            DME: Dmel_CG32155
            ATH: AT1G78670(ATGGH3) AT1G78680(ATGGH2)
            OSA: 4339329
            DDI: DDBDRAFT_0187001 DDBDRAFT_0188389
            TET: TTHERM_00030360 TTHERM_00130000 TTHERM_00321670
                 TTHERM_00449200 TTHERM_00819530 TTHERM_01027470
                 TTHERM_01156850
STRUCTURES  PDB: 1L9X  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.19.9
            ExPASy - ENZYME nomenclature database: 3.4.19.9
            ExplorEnz - The Enzyme Database: 3.4.19.9
            ERGO genome analysis and discovery system: 3.4.19.9
            BRENDA, the Enzyme Database: 3.4.19.9
            CAS: 9074-87-7
///
ENTRY       EC 3.4.19.10      Obsolete  Enzyme
NAME        Transferred to 3.5.1.28
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Omega peptidases
COMMENT     Transferred entry: now EC 3.5.1.28, N-acetylmuramoyl-L-alanine
            amidase (EC 3.4.19.10 created 1972 as EC 3.4.12.5, transferred 1978
            to EC 3.4.17.7, transferred 1992 to EC 3.4.19.10, deleted 1997)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.19.10
            ExPASy - ENZYME nomenclature database: 3.4.19.10
            ExplorEnz - The Enzyme Database: 3.4.19.10
            ERGO genome analysis and discovery system: 3.4.19.10
            BRENDA, the Enzyme Database: 3.4.19.10
///
ENTRY       EC 3.4.19.11                Enzyme
NAME        gamma-D-glutamyl-meso-diaminopimelate peptidase;
            endopeptidase I;
            gamma-D-glutamyldiaminopimelate endopeptidase;
            gamma-D-glutamyl-L-meso-diaminopimelate peptidoglycan hydrolase;
            gamma-glutamyl-L-meso-diaminopimelyl endopeptidase;
            gamma-D-glutamyl-meso-diaminopimelate endopeptidase;
            gamma-D-glutamyl-meso-diaminopimelic peptidoglycan hydrolase;
            gamma-D-glutamyl-meso-diaminopimelic endopeptidase;
            gamma-D-glutamyl-meso-D-aminopimelic endopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Omega peptidases
REACTION    Hydrolysis of gamma-D-glutamyl bonds to the L-terminus (position 7)
            of meso-diaminopimelic acid (meso-A2pm) in
            7-(L-Ala-gamma-D-Glu)-meso-A2pm and
            7-(L-Ala-gamma-D-Glu)-7-(D-Ala)-meso-A2pm. It is required that the
            D-terminal amino and carboxy groups of meso-A2pm are unsubstituted
COMMENT     A 45-kDa metallopeptidase from Bacillus sphaericus, the substrates
            being components of the bacterial spore wall. A member of peptidase
            family M14 (carboxypeptidase A family). Endopeptidase II has similar
            activity, but differs in cellular location, molecular mass and
            catalytic mechanism [3]
REFERENCE   1  [PMID:849747]
  AUTHORS   Arminjon F, Guinand M, Vacheron MJ, Michel G.
  TITLE     Specificity profiles of the membrane-bound
            gamma-D-glutamyl-(L)meso-diaminopimelateendopeptidase and
            LD-carboxypeptidase from Bacillus sphaericus 9602.
  JOURNAL   Eur. J. Biochem. 73 (1977) 557-65.
  ORGANISM  Bacillus sphaericus
REFERENCE   2  [PMID:3922755]
  AUTHORS   Garnier M, Vacheron MJ, Guinand M, Michel G.
  TITLE     Purification and partial characterization of the extracellular
            gamma-D-glutamyl-(L)meso-diaminopimelate endopeptidase I, from
            Bacillus sphaericus NCTC 9602.
  JOURNAL   Eur. J. Biochem. 148 (1985) 539-43.
  ORGANISM  Bacillus sphaericus
REFERENCE   3  [PMID:8503890]
  AUTHORS   Hourdou ML, Guinand M, Vacheron MJ, Michel G, Denoroy L, Duez C,
            Englebert S, Joris B, Weber G, Ghuysen JM.
  TITLE     Characterization of the sporulation-related
            gamma-D-glutamyl-(L)meso-diaminopimelic-acid-hydrolysing peptidase I
            of Bacillus sphaericus NCTC 9602 as a member of the metallo(zinc)
            carboxypeptidase A family. Modular design of the protein.
  JOURNAL   Biochem. J. 292 ( Pt 2) (1993) 563-70.
  ORGANISM  Bacillus sphaericus
ORTHOLOGY   KO: K01308  g-D-glutamyl-meso-diaminopimelate peptidase
GENES       BSU: BG11687(yqgT)
            BHA: BH1603
            BLI: BL01578(yqgT)
            BLD: BLi02657(yqgT)
            OIH: OB1731
            GKA: GK2441
            STH: STH1567
            CTC: CTC00595
            CBO: CBO1374
            CKL: CKL_0988
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.19.11
            ExPASy - ENZYME nomenclature database: 3.4.19.11
            ExplorEnz - The Enzyme Database: 3.4.19.11
            ERGO genome analysis and discovery system: 3.4.19.11
            BRENDA, the Enzyme Database: 3.4.19.11
            CAS: 62572-28-5
///
ENTRY       EC 3.4.19.12                Enzyme
NAME        ubiquitinyl hydrolase 1;
            ubiquitin C-terminal hydrolase;
            yeast ubiquitin hydrolase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Omega peptidases
REACTION    Thiol-dependent hydrolysis of ester, thioester, amide, peptide and
            isopeptide bonds formed by the C-terminal Gly of ubiquitin (a
            76-residue protein attached to proteins as an intracellular
            targeting signal)
COMMENT     Links to polypeptides smaller than 60 residues are hydrolysed more
            readily than those to larger polypeptides. Isoforms exist with
            quantitatively different specificities, amongst the best known being
            UCH-L1 and UCH-L3, which are major proteins of the brain of mammals
            [1]. Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by
            aminoacetaldehyde). Ubiquitinyl hydrolase 1 is the type example of
            peptidase family C12, with a similar protein fold to papain and
            catalytic amino acids Cys, His and Asp. There is a separate family
            (C19) of enzymes that also hydrolyse ubiquitinyl bonds, and it is
            thought that all the ubiquitinyl hydrolases are also ubiquitin
            thiolesterases (EC 3.1.2.15)
REFERENCE   1  [PMID:9233788]
  AUTHORS   Johnston SC, Larsen CN, Cook WJ, Wilkinson KD, Hill CP.
  TITLE     Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8
            A resolution.
  JOURNAL   EMBO. J. 16 (1997) 3787-96.
  ORGANISM  human [GN:hsa]
REFERENCE   2
  AUTHORS   Wilkinson, K.D.
  TITLE     Ubiquitin C-terminal hydrolase.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Academic Press, London, 1998, p.
            470-472.
PATHWAY     PATH: map01510  Neurodegenerative Disorders
            PATH: map05020  Parkinson's disease
ORTHOLOGY   KO: K01309  ubiquitinyl hydrolase 1
            KO: K05609  ubiquitin carboxyl-terminal hydrolase L3
            KO: K05610  ubiquitin carboxyl-terminal hydrolase L5
            KO: K05611  ubiquitin carboxyl-terminal hydrolase L1
            KO: K08588  ubiquitin carboxyl-terminal hydrolase BAP1
GENES       HSA: 51377(UCHL5) 7345(UCHL1) 7347(UCHL3) 8314(BAP1)
            PTR: 460426(BAP1) 461185(UCHL1)
            MMU: 104416(Bap1) 22223(Uchl1) 50933(Uchl3) 56207(Uchl5)
                 93841(Uchl4)
            RNO: 114094(Uchl3) 29545(Uchl1) 306257(Bap1_predicted)
                 360853(Uchl5)
            CFA: 476947(UCHL3) 478958(UCHL5) 479098(UCHL1) 484737(BAP1)
            BTA: 282110(UCHL5) 514394(UCHL1) 520170(UCHL3)
            SSC: 396637(UCHL1)
            GGA: 395626(UCHL3) 415944(RCJMB04_11f19) 424359(UCHL5)
                 770302(UCHL1)
            XLA: 495025(LOC495025)
            XTR: 493568(bap1) 496780(uchl1)
            DRE: 325119(uchl1) 406357(zgc:85615) 558885(LOC558885)
            SPU: 576462(LOC576462) 577834(LOC577834)
            DME: Dmel_CG3431(Uch-L3) Dmel_CG4265(Uch) Dmel_CG8445
            CEL: C08B11.7(thiolesterase)
            ATH: AT4G17510
            OSA: 4337328
            CME: CMO018C CMQ026C
            SCE: YJR099W(YUH1)
            AGO: AGOS_AGL314C
            PIC: PICST_41797(YUH1) PICST_65784
            ANI: AN7491.2
            AFM: AFUA_1G15920 AFUA_2G05590
            AOR: AO090001000670 AO090005001099
            CNE: CNA01690
            UMA: UM01905.1
            DDI: DDBDRAFT_0205083
            PFA: PF11_0177 PF14_0576
            CPV: cgd8_3200
            CHO: Chro.80372
            TET: TTHERM_00245080
            TBR: Tb11.02.2800 Tb11.03.0890
            TCR: 419703.20 510945.10
            LMA: LmjF24.0420
STRUCTURES  PDB: 1XD3  2ETL  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.19.12
            ExPASy - ENZYME nomenclature database: 3.4.19.12
            ExplorEnz - The Enzyme Database: 3.4.19.12
            ERGO genome analysis and discovery system: 3.4.19.12
            BRENDA, the Enzyme Database: 3.4.19.12
            CAS: 86480-67-3
///
ENTRY       EC 3.4.21.1                 Enzyme
NAME        chymotrypsin;
            chymotrypsins A and B;
            alpha-chymar ophth;
            avazyme;
            chymar;
            chymotest;
            enzeon;
            quimar;
            quimotrase;
            alpha-chymar;
            alpha-chymotrypsin A;
            alpha-chymotrypsin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage: Tyr!, Trp!, Phe!, Leu!
INHIBITOR   Tos-Phe-CH2Cl [CPD:C02088]
COMMENT     Chymotrypsin A is formed from cattle and pig chymotrypsinogen A,
            several iso-forms being produced according to the number of bonds
            hydrolysed in the precursor. Chymotrypsin B (formerly listed as EC
            3.4.4.6), formed from chymotrypsinogen B, is homologous with
            chymotrypsin A. Enzymes with specificity similar to that of
            chymotrypsins A and B have been isolated from many species. In
            peptidase family S1 (trypsin family)
REFERENCE   1
  AUTHORS   Wilcox, P.E.
  TITLE     Chymotrypsinogens - chymotrypsins.
  JOURNAL   Methods Enzymol. 19 (1970) 64-108.
  ORGANISM  cow [GN:bta], pig [GN:ssc]
REFERENCE   2
  AUTHORS   Blow, D.M.
  TITLE     Structure and mechanism of chymotrypsin.
  JOURNAL   Acc. Chem. Res. 9 (1976) 145-152.
  ORGANISM  mammalian
REFERENCE   3  [PMID:6768556]
  AUTHORS   Bauer CA.
  TITLE     Active centers of alpha-chymotrypsin and of Streptomyces griseus
            proteases 1 and 3. S2-P2 enzyme-substrate interactions.
  JOURNAL   Eur. J. Biochem. 105 (1980) 565-70.
  ORGANISM  Streptomyces griseus
REFERENCE   4
  AUTHORS   Polgar, L.
  TITLE     Structure and function of serine proteases.
  JOURNAL   In: Neuberger, A. and Brocklehurst, K. (Eds.), New Comprehensive
            Biochemistry: Hydrolytic Enzymes, vol. 16, Elsevier, Amsterdam,
            1987, p. 159-200.
REFERENCE   5  [PMID:2917002]
  AUTHORS   Tomita N, Izumoto Y, Horii A, Doi S, Yokouchi H, Ogawa M, Mori T,
            Matsubara K.
  TITLE     Molecular cloning and nucleotide sequence of human pancreatic
            prechymotrypsinogen cDNA.
  JOURNAL   Biochem. Biophys. Res. Commun. 158 (1989) 569-75.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01310  chymotrypsin
GENES       HSA: 1504(CTRB1) 440387(CTRB2)
            MMU: 66473(Ctrb1)
            RNO: 24291(Ctrb)
            CFA: 479649(CTRB1) 479650(CTRB2) 610373(LOC610373)
            BTA: 504241(LOC504241)
            XLA: 379495(MGC64534) 379607(MGC64417) 444360(MGC82838)
            XTR: 496968(ctrl) 548358(ctrb1)
            DRE: 322451(ctrb1) 562139(LOC562139)
            DME: Dmel_CG31362(Jon99Ciii) Dmel_CG6298(Jon74E) Dmel_CG6457(yip7)
                 Dmel_CG6467(Jon65Aiv) Dmel_CG7170(Jon66Cii)
                 Dmel_CG8579(Jon44E) Dmel_CG8869(Jon25Bii)
STRUCTURES  PDB: 1AB9  1ACB  1AFQ  1CA0  1CBW  1CHO  1DLK  1EQ9  1EX3  1GCD  
                 1GCT  1GG6  1GGD  1GHA  1GHB  1GL0  1GL1  1GMC  1GMD  1GMH  
                 1HJA  1K2I  1KDQ  1MTN  1N8O  1OXG  1P2M  1P2N  1P2O  1P2Q  
                 1T7C  1T8L  1T8M  1T8N  1T8O  1VGC  1YPH  2CHA  2GCH  2GCT  
                 2GMT  2JET  2P8O  2VGC  3GCH  3GCT  3VGC  4CHA  4GCH  4VGC  
                 5CHA  5GCH  6CHA  6GCH  7GCH  8GCH  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.1
            ExPASy - ENZYME nomenclature database: 3.4.21.1
            ExplorEnz - The Enzyme Database: 3.4.21.1
            ERGO genome analysis and discovery system: 3.4.21.1
            BRENDA, the Enzyme Database: 3.4.21.1
            CAS: 9004-07-3
///
ENTRY       EC 3.4.21.2                 Enzyme
NAME        chymotrypsin C
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage: Leu!, Tyr!, Phe!, Met!, Trp!, Gln!, Asn!
COMMENT     Formed from pig chymotrypsinogen C, and from cattle subunit II of
            procarboxypeptidase A. Reacts more readily with Tos-Leu-CH2Cl than
            Tos-Phe-CH2Cl in contrast to chymotrypsin. In peptidase family S1
            (trypsin family)
REFERENCE   1  [PMID:5792601]
  AUTHORS   Peanasky RJ, Gratecos D, Baratti J, Rovery M.
  TITLE     Mode of activation of N-terminal sequence of subunit II in bovine
            procarboxypeptidase A and of porcine chymotrypsinogen C.
  JOURNAL   Biochim. Biophys. Acta. 181 (1969) 82-92.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   Folk, J.E.
  TITLE     Chymotrypsin C (porcine pancreas).
  JOURNAL   Methods Enzymol. 19 (1970) 109-112.
  ORGANISM  cow [GN:bta], pig [GN:ssc]
REFERENCE   3
  AUTHORS   Wilcox, P.E.
  TITLE     Chymotrypsinogens - chymotrypsins.
  JOURNAL   Methods Enzymol. 19 (1970) 64-108.
  ORGANISM  pig [GN:ssc]
ORTHOLOGY   KO: K01311  chymotrypsin C
GENES       HSA: 11330(CTRC)
            MMU: 76701(Ctrc)
            RNO: 362653(Ctrc)
            CFA: 478220(CTRC)
            BTA: 514047(LOC514047)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.2
            ExPASy - ENZYME nomenclature database: 3.4.21.2
            ExplorEnz - The Enzyme Database: 3.4.21.2
            ERGO genome analysis and discovery system: 3.4.21.2
            BRENDA, the Enzyme Database: 3.4.21.2
            CAS: 9036-09-3
///
ENTRY       EC 3.4.21.3                 Enzyme
NAME        metridin;
            Metridium proteinase A;
            sea anemone protease A;
            sea anemone proteinase A
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage: Tyr!, Phe!, Leu!; little action on Trp-!
COMMENT     Digestive enzyme from the sea anemone Metridium senile.
REFERENCE   1  [PMID:4389140]
  AUTHORS   Gibson D, Dixon GH.
  TITLE     Chymotrypsin-like proteases from the sea anemone, Metridium senile.
  JOURNAL   Nature. 222 (1969) 753-6.
  ORGANISM  Metridium senile
REFERENCE   2  [PMID:4150616]
  AUTHORS   Stevenson KJ, Gibson D, Dixon GH.
  TITLE     Amino acid analyses of chymotrypsin-like proteases from the sea
            anemone (Metridium senile).
  JOURNAL   Can. J. Biochem. 52 (1974) 93-100.
  ORGANISM  Metridium senile
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.3
            ExPASy - ENZYME nomenclature database: 3.4.21.3
            ExplorEnz - The Enzyme Database: 3.4.21.3
            ERGO genome analysis and discovery system: 3.4.21.3
            BRENDA, the Enzyme Database: 3.4.21.3
            CAS: 37288-75-8
///
ENTRY       EC 3.4.21.4                 Enzyme
NAME        trypsin;
            alpha-trypsin;
            beta-trypsin;
            cocoonase;
            parenzyme;
            parenzymol;
            tryptar;
            trypure;
            pseudotrypsin;
            tryptase;
            tripcellim;
            sperm receptor hydrolase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage: Arg!, Lys!
INHIBITOR   Tos-Lys-CH2Cl [CPD:C00896];
            Tos-Arg-CH2Cl [CPD:C02087]
COMMENT     The single polypeptide chain cattle beta-trypsin is formed from
            trypsinogen by cleavage of one peptide bond. Further peptide bond
            cleavages produce alpha and other iso-forms. Isolated as multiple
            cationic and anionic trypsins [5] from the pancreas of many
            vertebrates and from lower species including crayfish, insects
            (cocoonase) and microorganisms (Streptomyces griseus) [3]. Type
            example of peptidase family S1.
REFERENCE   1
  AUTHORS   Huber, R. and Bode, W.
  TITLE     Structural basis of the activation and action of trypsin.
  JOURNAL   Acc. Chem. Res. 11 (1978) 114-122.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   Walsh, K.A.
  TITLE     Trypsinogens and trypsins of various species.
  JOURNAL   Methods Enzymol. 19 (1970) 41-63.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:6442164]
  AUTHORS   Read RJ, Brayer GD, Jurasek L, James MN.
  TITLE     Critical evaluation of comparative model building of Streptomyces
            griseus trypsin.
  JOURNAL   Biochemistry. 23 (1984) 6570-5.
  ORGANISM  Streptomyces griseus
REFERENCE   4  [PMID:3643848]
  AUTHORS   Fiedler F.
  TITLE     Effects of secondary interactions on the kinetics of peptide and
            peptide ester hydrolysis by tissue kallikrein and trypsin.
  JOURNAL   Eur. J. Biochem. 163 (1987) 303-12.
  ORGANISM  cow [GN:bta]
REFERENCE   5  [PMID:3112218]
  AUTHORS   Jelinek DF, Lipsky PE.
  TITLE     Comparative activation requirements of human peripheral blood,
            spleen, and lymph node B cells.
  JOURNAL   J. Immunol. 139 (1987) 1005-13.
  ORGANISM  human [GN:hsa]
REFERENCE   6
  AUTHORS   Polgar, L.
  TITLE     Structure and function of serine proteases.
  JOURNAL   In: Neuberger, A. and Brocklehurst, K. (Eds.), New Comprehensive
            Biochemistry: Hydrolytic Enzymes, vol. 16, Elsevier, Amsterdam,
            1987, p. 159-200.
REFERENCE   7  [PMID:2326201]
  AUTHORS   Tani T, Kawashima I, Mita K, Takiguchi Y.
  TITLE     Nucleotide sequence of the human pancreatic trypsinogen III cDNA.
  JOURNAL   Nucleic. Acids. Res. 18 (1990) 1631.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04080  Neuroactive ligand-receptor interaction
ORTHOLOGY   KO: K01312  trypsin
GENES       HSA: 5644(PRSS1) 5645(PRSS2) 5646(PRSS3)
            MMU: 435889(1810049H19Rik) 436522(Try10)
            RNO: 24691(Prss1) 25052(Prss2) 286960(LOC286960)
                 362347(Prss3_predicted)
            CFA: 475521(PRSS3)
            BTA: 282603(TRYP8)
            GGA: 396344(PRSS2) 396345(PRSS3) 768632(LOC768632)
                 768663(LOC768663)
            XLA: 379460(MGC64344)
            XTR: 496623(LOC496623) 496627(LOC496627) 548509(MGC108396)
            DRE: 65223(try)
            DME: Dmel_CG1102(MP1) Dmel_CG12350 Dmel_CG12351(deltaTry)
                 Dmel_CG12385(thetaTry) Dmel_CG12386(etaTry)
                 Dmel_CG12387(zetaTry) Dmel_CG18211(betaTry)
                 Dmel_CG18444(alphaTry) Dmel_CG18681(epsilonTry)
                 Dmel_CG2045(Ser7) Dmel_CG30031 Dmel_CG3066(Sp7)
                 Dmel_CG4316(Sb) Dmel_CG4812(Ser8) Dmel_CG4821(Tequila)
                 Dmel_CG6367(psh) Dmel_CG7754(iotaTry) Dmel_CG9564(Try29F)
            ANI: AN2366.2
            BBA: Bd0564 Bd2630
            MXA: MXAN_5435
            SMA: SAV2443
STRUCTURES  PDB: 1A0J  1AKS  1AMH  1AN1  1ANB  1ANC  1AND  1ANE  1AQ7  1AUJ  
                 1AVW  1AVX  1AZ8  1BJU  1BJV  1BRA  1BRB  1BRC  1BTP  1BTW  
                 1BTX  1BTY  1BTZ  1BZX  1C1N  1C1O  1C1P  1C1Q  1C1R  1C1S  
                 1C1T  1C2D  1C2E  1C2F  1C2G  1C2H  1C2I  1C2J  1C2K  1C2L  
                 1C2M  1C5P  1C5Q  1C5R  1C5S  1C5T  1C5U  1C5V  1C9P  1C9T  
                 1CE5  1CO7  1D6R  1DPO  1EB2  1EJA  1EJM  1EPT  1EZS  1EZU  
                 1EZX  1F0T  1F0U  1F2S  1F5R  1F7Z  1FMG  1FN6  1FN8  1FNI  
                 1FY4  1FY5  1FY8  1G36  1G3B  1G3C  1G3D  1G3E  1G9I  1GBT  
                 1GDN  1GDQ  1GDU  1GHZ  1GI0  1GI1  1GI2  1GI3  1GI4  1GI5  
                 1GI6  1GJ6  1H4W  1H9H  1H9I  1HJ8  1HJ9  1J14  1J15  1J16  
                 1J17  1J8A  1JIR  1JRS  1JRT  1K1I  1K1J  1K1L  1K1M  1K1N  
                 1K1O  1K1P  1K9O  1LDT  1LQE  1MAX  1MAY  1MBQ  1MCT  1MTS  
                 1MTU  1MTV  1MTW  1N6X  1N6Y  1NC6  1NTP  1O2H  1O2I  1O2J  
                 1O2K  1O2L  1O2M  1O2N  1O2O  1O2P  1O2Q  1O2R  1O2S  1O2T  
                 1O2U  1O2V  1O2W  1O2X  1O2Y  1O2Z  1O30  1O31  1O32  1O33  
                 1O34  1O35  1O36  1O37  1O38  1O39  1O3A  1O3B  1O3C  1O3D  
                 1O3E  1O3F  1O3G  1O3H  1O3I  1O3J  1O3K  1O3L  1O3M  1O3N  
                 1O3O  1OPH  1OS8  1OSS  1OX1  1OYQ  1P2I  1P2J  1P2K  1PPC  
                 1PPE  1PPH  1PPZ  1PQ5  1PQ7  1PQ8  1PQA  1QA0  1QB1  1QB6  
                 1QB9  1QBN  1QBO  1QL7  1QL8  1QL9  1QQU  1RXP  1S0Q  1S0R  
                 1S5S  1S6F  1S6H  1S81  1S82  1S83  1S84  1S85  1SBW  1SFI  
                 1SGT  1SLU  1SLV  1SLW  1SLX  1SMF  1TAB  1TAW  1TFX  1TIO  
                 1TLD  1TNG  1TNH  1TNI  1TNJ  1TNK  1TNL  1TPA  1TPO  1TPP  
                 1TRM  1TRN  1TRY  1TX7  1TX8  1UHB  1UTJ  1UTK  1UTL  1UTM  
                 1UTN  1UTO  1UTP  1UTQ  1V2J  1V2K  1V2L  1V2M  1V2N  1V2O  
                 1V2P  1V2Q  1V2R  1V2S  1V2T  1V2U  1V2V  1V2W  1V6D  1XUF  
                 1XUG  1XUH  1XUI  1XUJ  1XUK  1XVM  1XVO  1Y3U  1Y3V  1Y3W  
                 1Y3X  1Y3Y  1Y59  1Y5A  1Y5B  1Y5U  1YF4  1YKT  1YLC  1YLD  
                 1YP9  1YYY  1Z7K  1ZR0  2A31  2A32  2A7H  2AGE  2AGG  2AGI  
                 2AH4  2AYW  2BLV  2BLW  2BTC  2BY5  2BY6  2BY7  2BY8  2BY9  
                 2BYA  2BZA  2CMY  2D8W  2F3C  2F91  2FI3  2FI4  2FI5  2FMJ  
                 2FTL  2FTM  2FX4  2FX6  2G51  2G52  2G55  2G5N  2G5V  2G8T  
                 2ILN  2J9N  2OTV  2OXS  2PLX  2PTC  2PTN  2STA  2STB  2TBS  
                 2TIO  2TLD  2TRM  2UUY  3BTD  3BTE  3BTF  3BTG  3BTH  3BTK  
                 3BTM  3BTQ  3BTT  3BTW  3PTB  3PTN  3TGI  3TGJ  3TGK  5PTP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.4
            ExPASy - ENZYME nomenclature database: 3.4.21.4
            ExplorEnz - The Enzyme Database: 3.4.21.4
            ERGO genome analysis and discovery system: 3.4.21.4
            BRENDA, the Enzyme Database: 3.4.21.4
            CAS: 9002-07-7
///
ENTRY       EC 3.4.21.5                 Enzyme
NAME        thrombin;
            fibrinogenase;
            thrombase;
            thrombofort;
            topical;
            thrombin-C;
            tropostasin;
            activated blood-coagulation factor II;
            blood-coagulation factor IIa;
            factor IIa;
            E thrombin;
            beta-thrombin;
            gamma-thrombin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage of Arg!Gly bonds in fibrinogen to form fibrin and
            release fibrinopeptides A and B
INHIBITOR   Benzamidine [CPD:C01784];
            D-Phe-Pro-Arg-CH2Cl [CPD:C02828];
            Nalpha-(2-naphthyl-sulfonyl-glycyl)-D-p-amidinopheyl-alanylpiperadin
            e [CPD:C04863];
            Argatroban [CPD:C04931]
COMMENT     Formed from prothrombin. More selective than trypsin and plasmin. In
            peptidase family S1 (trypsin family).
REFERENCE   1
  AUTHORS   Baughman, D.J.
  TITLE     Thrombin assay.
  JOURNAL   Methods Enzymol. 19 (1970) 145-157.
REFERENCE   2
  AUTHORS   Magnusson, S.
  TITLE     Bovine prothrombin and thrombin.
  JOURNAL   Methods Enzymol. 19 (1970) 157-184.
  ORGANISM  cow [GN:bta]
REFERENCE   3
  AUTHORS   Miller, K.D.
  TITLE     Horse prothrombin.
  JOURNAL   Methods Enzymol. 19 (1970) 140-145.
  ORGANISM  horse
REFERENCE   4  [PMID:1011989]
  AUTHORS   Lundblad RL, Kingdon HS, Mann KG.
  TITLE     Thrombin.
  JOURNAL   Methods. Enzymol. 45 (1976) 156-76.
REFERENCE   5  [PMID:1011988]
  AUTHORS   Mann KG.
  TITLE     Prothrombin.
  JOURNAL   Methods. Enzymol. 45 (1976) 123-56.
REFERENCE   6  [PMID:367103]
  AUTHORS   Davie EW, Fujikawa K, Kurachi K, Kisiel W.
  TITLE     The role of serine proteases in the blood coagulation cascade.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 48 (1979) 277-318.
REFERENCE   7  [PMID:6370301]
  AUTHORS   Cho K, Tanaka T, Cook RR, Kisiel W, Fujikawa K, Kurachi K, Powers
            JC.
  TITLE     Active-site mapping of bovine and human blood coagulation serine
            proteases using synthetic peptide 4-nitroanilide and thio ester
            substrates.
  JOURNAL   Biochemistry. 23 (1984) 644-50.
  ORGANISM  cow [GN:bta], human [GN:hsa]
REFERENCE   8  [PMID:6326805]
  AUTHORS   MacGillivray RT, Davie EW.
  TITLE     Characterization of bovine prothrombin mRNA and its translation
            product.
  JOURNAL   Biochemistry. 23 (1984) 1626-34.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map04080  Neuroactive ligand-receptor interaction
            PATH: map04610  Complement and coagulation cascades
            PATH: map04810  Regulation of actin cytoskeleton
ORTHOLOGY   KO: K01313  coagulation factor II (thrombin)
GENES       HSA: 2147(F2)
            PTR: 451158(F2)
            MMU: 14061(F2)
            RNO: 29251(F2)
            BTA: 280685(F2)
            GGA: 395306(F2)
            XLA: 446352(lpa)
            XTR: 548514(f2)
            DRE: 325881(f2)
STRUCTURES  PDB: 1A0H  1A2C  1A3B  1A3E  1A46  1A4W  1A5G  1A61  1ABI  1ABJ  
                 1AD8  1AE8  1AFE  1AHT  1AI8  1AIX  1AVG  1AWF  1AWH  1AY6  
                 1B5G  1B7X  1BA8  1BB0  1BBR  1BCU  1BHX  1BMM  1BMN  1BTH  
                 1C1U  1C1V  1C1W  1C4U  1C4V  1C4Y  1C5L  1C5N  1C5O  1CA8  
                 1D3D  1D3P  1D3Q  1D3T  1D4P  1D6W  1D9I  1DE7  1DIT  1DOJ  
                 1DWB  1DWC  1DWD  1DWE  1DX5  1E0F  1EB1  1EOJ  1EOL  1ETR  
                 1ETS  1ETT  1FPC  1FPH  1G30  1G32  1G37  1GHV  1GHW  1GHX  
                 1GHY  1GJ4  1GJ5  1H8D  1H8I  1HAG  1HAH  1HAI  1HAO  1HAP  
                 1HBT  1HDT  1HGT  1HRT  1HUT  1HXE  1HXF  1ID5  1IHS  1IHT  
                 1JMO  1JWT  1K21  1K22  1KTS  1KTT  1LHC  1LHD  1LHE  1LHF  
                 1LHG  1MH0  1MKW  1MKX  1MU6  1MU8  1MUE  1NL1  1NL2  1NM6  
                 1NO9  1NRN  1NRO  1NRP  1NRQ  1NRR  1NRS  1NT1  1NU7  1NU9  
                 1NY2  1NZQ  1O0D  1O2G  1O5G  1OOK  1OYT  1P8V  1PPB  1QBV  
                 1QHR  1QJ1  1QJ6  1QJ7  1RD3  1RIW  1SB1  1SFQ  1SG8  1SGI  
                 1SHH  1SL3  1SR5  1T4U  1T4V  1TA2  1TA6  1TB6  1TBQ  1TBR  
                 1TBZ  1THP  1THR  1THS  1TMB  1TMT  1TMU  1TOC  1TOM  1TQ0  
                 1TQ7  1TWX  1UCY  1UMA  1UVS  1UVT  1UVU  1VIT  1VZQ  1W7G  
                 1WAY  1WBG  1XM1  1XMN  1YCP  1YPE  1YPG  1YPJ  1YPK  1YPL  
                 1YPM  1Z71  1Z8I  1Z8J  1ZGI  1ZGV  1ZRB  2A0Q  2A1D  2A2X  
                 2A45  2AFQ  2ANK  2ANM  2B5T  2BDY  2BVR  2BVS  2BVX  2BXT  
                 2BXU  2C8W  2C8X  2C8Y  2C8Z  2C90  2C93  2CF8  2CF9  2CN0  
                 2FEQ  2FES  2GDE  2GP9  2H9T  2HGT  2HPP  2HPQ  2HWL  2JH0  
                 2JH5  2JH6  2PGB  2PGQ  2SPT  2THF  2UUF  2UUJ  2UUK  3HAT  
                 3HTC  4HTC  4THN  5GDS  7KME  8KME  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.5
            ExPASy - ENZYME nomenclature database: 3.4.21.5
            ExplorEnz - The Enzyme Database: 3.4.21.5
            ERGO genome analysis and discovery system: 3.4.21.5
            BRENDA, the Enzyme Database: 3.4.21.5
            CAS: 9002-04-4
///
ENTRY       EC 3.4.21.6                 Enzyme
NAME        coagulation factor Xa;
            thrombokinase;
            prothrombase;
            prothrombinase;
            activated blood-coagulation factor X;
            autoprothrombin C;
            thromboplastin;
            plasma thromboplastin;
            factor Xa;
            activated Stuart-Prower factor;
            activated factor X
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage of Arg!Thr and then Arg!Ile bonds in prothrombin
            to form thrombin
COMMENT     Formed from the proenzyme factor X by limited proteolysis. In
            peptidase family S1 (trypsin family). Scutelarin (EC 3.4.21.60) has
            similar specificity
REFERENCE   1  [PMID:1012041]
  AUTHORS   Fujikawa K, Davie EW.
  TITLE     Bovine factor X (Stuart factor).
  JOURNAL   Methods. Enzymol. 45 (1976) 89-95.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:1012042]
  AUTHORS   Jesty J, Nemerson Y.
  TITLE     The activation of bovine coagulation factor X.
  JOURNAL   Methods. Enzymol. 45 (1976) 95-107.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:367103]
  AUTHORS   Davie EW, Fujikawa K, Kurachi K, Kisiel W.
  TITLE     The role of serine proteases in the blood coagulation cascade.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 48 (1979) 277-318.
REFERENCE   4  [PMID:6996572]
  AUTHORS   Jackson CM, Nemerson Y.
  TITLE     Blood coagulation.
  JOURNAL   Annu. Rev. Biochem. 49 (1980) 765-811.
REFERENCE   5  [PMID:6871167]
  AUTHORS   McMullen BA, Fujikawa K, Kisiel W, Sasagawa T, Howald WN, Kwa EY,
            Weinstein B.
  TITLE     Complete amino acid sequence of the light chain of human blood
            coagulation factor X: evidence for identification of residue 63 as
            beta-hydroxyaspartic acid.
  JOURNAL   Biochemistry. 22 (1983) 2875-84.
  ORGANISM  human [GN:hsa]
REFERENCE   6  [PMID:6370301]
  AUTHORS   Cho K, Tanaka T, Cook RR, Kisiel W, Fujikawa K, Kurachi K, Powers
            JC.
  TITLE     Active-site mapping of bovine and human blood coagulation serine
            proteases using synthetic peptide 4-nitroanilide and thio ester
            substrates.
  JOURNAL   Biochemistry. 23 (1984) 644-50.
  ORGANISM  cow [GN:bta], human [GN:hsa]
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01314  coagulation factor X
GENES       HSA: 2159(F10)
            PTR: 452679(F10)
            MMU: 14058(F10)
            RNO: 29243(F10)
            CFA: 476993(F10)
            BTA: 280787(F10)
            GGA: 395876(F10)
            XLA: 398778(MGC68454)
            XTR: 548445(MGC107878)
            DRE: 282670(f10)
STRUCTURES  PDB: 1C5M  1EZQ  1F0R  1F0S  1FAX  1FJS  1G2L  1G2M  1IOD  1IOE  
                 1IQE  1IQF  1IQG  1IQH  1IQI  1IQJ  1IQK  1IQL  1IQM  1IQN  
                 1KIG  1KSN  1KYE  1LPG  1LPK  1LPZ  1LQD  1MQ5  1MQ6  1NFU  
                 1NFW  1NFX  1NFY  1P0S  1V3X  1WHE  1WHF  1WU1  1XKA  1XKB  
                 1Z6E  2BMG  2BOH  2BOK  2BQ6  2BQ7  2BQW  2CJI  2D1J  2FZZ  
                 2G00  2GD4  2H9E  2J2U  2J34  2J38  2J4I  2J94  2J95  2P3U  
                 2P93  2P94  2P95  2PR3  2Q1J  2UWL  2UWO  2UWP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.6
            ExPASy - ENZYME nomenclature database: 3.4.21.6
            ExplorEnz - The Enzyme Database: 3.4.21.6
            ERGO genome analysis and discovery system: 3.4.21.6
            BRENDA, the Enzyme Database: 3.4.21.6
            CAS: 9002-05-5
///
ENTRY       EC 3.4.21.7                 Enzyme
NAME        plasmin;
            fibrinase;
            fibrinolysin;
            actase;
            serum tryptase;
            thrombolysin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage: Lys! > Arg!; higher selectivity than trypsin.
            Converts fibrin into soluble products
COMMENT     Formed from plasminogen by proteolysis which results in multiple
            forms of the active plasmin. In peptidase family S1 (trypsin
            family).
REFERENCE   1  [PMID:138065]
  AUTHORS   Castellino FJ, Sodetz JM.
  TITLE     Rabbit plasminogen and plasmin isozymes.
  JOURNAL   Methods. Enzymol. 45 (1976) 273-86.
  ORGANISM  rabbit
REFERENCE   2  [PMID:6210827]
  AUTHORS   Castellino FJ, Powell JR.
  TITLE     Human plasminogen.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 365-78.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:6210828]
  AUTHORS   Robbins KC, Summaria L, Wohl RC.
  TITLE     Human plasmin.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 379-87.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01315  plasminogen
GENES       HSA: 5340(PLG)
            PTR: 463117(PLG)
            MCC: 703891(PLG)
            MMU: 18815(Plg)
            RNO: 85253(Plg)
            CFA: 403602(PLG)
            BTA: 280897(PLG)
            GGA: 421580(PLG)
            DRE: 322691(plg)
            SPU: 593482(LOC593482)
            NMC: NMC0651(iga)
            BBA: Bd0994(splA)
STRUCTURES  PDB: 1B2I  1BML  1BUI  1CEA  1CEB  1DDJ  1HPJ  1HPK  1I5K  1KI0  
                 1KRN  1L4D  1L4Z  1PMK  1RJX  2DOH  2DOI  5HPG  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.7
            ExPASy - ENZYME nomenclature database: 3.4.21.7
            ExplorEnz - The Enzyme Database: 3.4.21.7
            ERGO genome analysis and discovery system: 3.4.21.7
            BRENDA, the Enzyme Database: 3.4.21.7
            CAS: 9001-90-5
///
ENTRY       EC 3.4.21.8       Obsolete  Enzyme
NAME        Transferred to 3.4.21.34 and 3.4.21.35
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Transferred entry: now EC 3.4.21.34 (plasma kallikrein) and EC
            3.4.21.35 (tissue kallikrein) (EC 3.4.21.8 created 1972, deleted
            1981)
STRUCTURES  PDB: 2KAI  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.8
            ExPASy - ENZYME nomenclature database: 3.4.21.8
            ExplorEnz - The Enzyme Database: 3.4.21.8
            ERGO genome analysis and discovery system: 3.4.21.8
            BRENDA, the Enzyme Database: 3.4.21.8
///
ENTRY       EC 3.4.21.9                 Enzyme
NAME        enteropeptidase;
            enterokinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Activation of trypsinogen by selective cleavage of Lys6!Ile bond
COMMENT     Is not inhibited by protein inhibitors of trypsin. In peptidase
            family S1 (trypsin family).
REFERENCE   1  [PMID:2658218]
  AUTHORS   Light A, Janska H.
  TITLE     Enterokinase (enteropeptidase): comparative aspects.
  JOURNAL   Trends. Biochem. Sci. 14 (1989) 110-2.
  ORGANISM  human [GN:hsa], pig [GN:ssc], cow [GN:bta]
ORTHOLOGY   KO: K01316  protease, serine, 7 (enterokinase)
GENES       HSA: 5651(PRSS7)
            MMU: 19146(Prss7)
            RNO: 288291(Prss7_predicted)
            CFA: 487700(PRSS7)
            BTA: 282009(PRSS7)
            SSC: 397152(PRSS7)
            GGA: 427967(PRSS7)
STRUCTURES  PDB: 1EKB  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.9
            ExPASy - ENZYME nomenclature database: 3.4.21.9
            ExplorEnz - The Enzyme Database: 3.4.21.9
            ERGO genome analysis and discovery system: 3.4.21.9
            BRENDA, the Enzyme Database: 3.4.21.9
            CAS: 9014-74-8
///
ENTRY       EC 3.4.21.10                Enzyme
NAME        acrosin;
            acrosomal proteinase;
            acrozonase;
            alpha-acrosin;
            beta-acrosin;
            upsilon-acrosin;
            acrosomal protease;
            acrosin amidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage: Arg!, Lys!
INHIBITOR   Tripsin inhibitor [CPD:C02597]
COMMENT     Occurs in spermatozoa; formed from proacrosin by limited
            proteolysis. Inhibited by naturally occurring trypsin inhibitors. In
            peptidase family S1 (trypsin family)
REFERENCE   1  [PMID:7043204]
  AUTHORS   Muller-Esterl W, Fritz H.
  TITLE     Sperm Acrosin.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 621-32.
REFERENCE   2  [PMID:2500154]
  AUTHORS   Skoog MT, Mehdi S, Wiseman JS, Bey P.
  TITLE     The specificity of two proteinases that cleave adjacent to arginine,
            C1 esterase and acrosin, for peptide p-nitroanilide substrates.
  JOURNAL   Biochim. Biophys. Acta. 996 (1989) 89-94.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:2114285]
  AUTHORS   Keime S, Adham IM, Engel W.
  TITLE     Nucleotide sequence and exon-intron organization of the human
            proacrosin gene.
  JOURNAL   Eur. J. Biochem. 190 (1990) 195-200.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01317  acrosin
GENES       HSA: 49(ACR)
            PTR: 458950(ACR)
            MMU: 11434(Acr)
            RNO: 24163(Acr)
            CFA: 606765(ACR)
            BTA: 280711(ACR)
            SSC: 397098(ACR)
            AVA: Ava_1781 Ava_4160
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.10
            ExPASy - ENZYME nomenclature database: 3.4.21.10
            ExplorEnz - The Enzyme Database: 3.4.21.10
            ERGO genome analysis and discovery system: 3.4.21.10
            BRENDA, the Enzyme Database: 3.4.21.10
            CAS: 9068-57-9
///
ENTRY       EC 3.4.21.11      Obsolete  Enzyme
NAME        Transferred to 3.4.21.37
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Transferred entry: now EC 3.4.21.37 leukocyte elastase (EC 3.4.21.11
            created 1972, deleted 1981)
STRUCTURES  PDB: 1HAX  1HAY  1HAZ  1HB0  1QIX  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.11
            ExPASy - ENZYME nomenclature database: 3.4.21.11
            ExplorEnz - The Enzyme Database: 3.4.21.11
            ERGO genome analysis and discovery system: 3.4.21.11
            BRENDA, the Enzyme Database: 3.4.21.11
///
ENTRY       EC 3.4.21.12                Enzyme
NAME        alpha-lytic endopeptidase;
            myxobacter alpha-lytic proteinase;
            alpha-lytic proteinase;
            alpha-lytic protease;
            Mycobacterium sorangium alpha-lytic proteinase;
            Myxobacter 495 alpha-lytic proteinase;
            alpha-lytic proteinase;
            Myxobacter alpha-lytic proteinase;
            Mycobacterium sorangium alpha-lytic proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage: Ala!, Val! in bacterial cell walls, elastin
            and other proteins
COMMENT     From the myxobacterium Lysobacter enzymogenes. In peptidase family
            S1 (trypsin family)
REFERENCE   1  [PMID:5482494]
  AUTHORS   Olson MO, Nagabhushan N, Dzwiniel M, Smillie LB, Whitaker DR.
  TITLE     Priaary structure of alpha-lytic protease: a bacterial homologue of
            the pancreatic serine proteases.
  JOURNAL   Nature. 228 (1970) 438-42.
REFERENCE   2
  AUTHORS   Polgar, L.
  TITLE     Structure and function of serine proteases.
  JOURNAL   In: Neuberger, A. and Brocklehurst, K. (Eds.), New Comprehensive
            Biochemistry: Hydrolytic Enzymes, vol. 16, Elsevier, Amsterdam,
            1987, p. 159-200.
REFERENCE   3  [PMID:3053694]
  AUTHORS   Epstein DM, Wensink PC.
  TITLE     The alpha-lytic protease gene of Lysobacter enzymogenes. The
            nucleotide sequence predicts a large prepro-peptide with homology to
            pro-peptides of other chymotrypsin-like enzymes.
  JOURNAL   J. Biol. Chem. 263 (1988) 16586-90.
  ORGANISM  Lysobacter enzymogenes
REFERENCE   4  [PMID:2611204]
  AUTHORS   Bone R, Frank D, Kettner CA, Agard DA.
  TITLE     Structural analysis of specificity: alpha-lytic protease complexes
            with analogues of reaction intermediates.
  JOURNAL   Biochemistry. 28 (1989) 7600-9.
  ORGANISM  Lysobacter enzymogenes
STRUCTURES  PDB: 1BOQ  1GBA  1GBB  1GBC  1GBD  1GBE  1GBF  1GBH  1GBI  1GBJ  
                 1GBK  1GBL  1GBM  1P01  1P02  1P03  1P04  1P05  1P06  1P09  
                 1P10  1P11  1P12  1QQ4  1QRW  1QRX  1SSX  1TAL  2ALP  2H5C  
                 2H5D  2LPR  2ULL  3LPR  5LPR  6LPR  7LPR  8LPR  9LPR  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.12
            ExPASy - ENZYME nomenclature database: 3.4.21.12
            ExplorEnz - The Enzyme Database: 3.4.21.12
            ERGO genome analysis and discovery system: 3.4.21.12
            BRENDA, the Enzyme Database: 3.4.21.12
            CAS: 37288-76-9
///
ENTRY       EC 3.4.21.13      Obsolete  Enzyme
NAME        Transferred to 3.4.16.6
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Transferred entry: now EC 3.4.16.6 carboxypeptidase D (EC 3.4.21.13
            created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.13
            ExPASy - ENZYME nomenclature database: 3.4.21.13
            ExplorEnz - The Enzyme Database: 3.4.21.13
            ERGO genome analysis and discovery system: 3.4.21.13
            BRENDA, the Enzyme Database: 3.4.21.13
///
ENTRY       EC 3.4.21.14      Obsolete  Enzyme
NAME        Transferred to 3.4.21.67
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Transferred entry: now EC 3.4.21.67 endopeptidase So (EC 3.4.21.14
            created 1961 as EC 3.4.4.16, transferred 1972 to EC 3.4.21.14,
            modified 1986, deleted 1992)
STRUCTURES  PDB: 1MEE  1S01  1S02  1SBT  1ST2  1YJA  1YJB  1YJC  2PRK  2SBT  
                 2SIC  2SNI  2ST1  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.14
            ExPASy - ENZYME nomenclature database: 3.4.21.14
            ExplorEnz - The Enzyme Database: 3.4.21.14
            ERGO genome analysis and discovery system: 3.4.21.14
            BRENDA, the Enzyme Database: 3.4.21.14
///
ENTRY       EC 3.4.21.15      Obsolete  Enzyme
NAME        Transferred to 3.4.21.63
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Transferred entry: now EC 3.4.21.63, oryzin (EC 3.4.21.15 created
            1972, deleted 1978 (transferred to EC 3.4.21.14, deleted 1992))
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.15
            ExPASy - ENZYME nomenclature database: 3.4.21.15
            ExplorEnz - The Enzyme Database: 3.4.21.15
            ERGO genome analysis and discovery system: 3.4.21.15
            BRENDA, the Enzyme Database: 3.4.21.15
///
ENTRY       EC 3.4.21.16      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Deleted entry: Alternaria serine proteinase (EC 3.4.21.16 created
            1972, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.16
            ExPASy - ENZYME nomenclature database: 3.4.21.16
            ExplorEnz - The Enzyme Database: 3.4.21.16
            ERGO genome analysis and discovery system: 3.4.21.16
            BRENDA, the Enzyme Database: 3.4.21.16
///
ENTRY       EC 3.4.21.17      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Deleted entry: Arthrobacter serine proteinase (EC 3.4.21.17 created
            1972, deleted 1978 [transferred to EC 3.4.21.14, deleted 1992])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.17
            ExPASy - ENZYME nomenclature database: 3.4.21.17
            ExplorEnz - The Enzyme Database: 3.4.21.17
            ERGO genome analysis and discovery system: 3.4.21.17
            BRENDA, the Enzyme Database: 3.4.21.17
///
ENTRY       EC 3.4.21.18      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Deleted entry: Tenebrio alpha-proteinase (EC 3.4.21.18 created 1972
            [EC 3.4.99.24 created 1972, incorporated 1978], deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.18
            ExPASy - ENZYME nomenclature database: 3.4.21.18
            ExplorEnz - The Enzyme Database: 3.4.21.18
            ERGO genome analysis and discovery system: 3.4.21.18
            BRENDA, the Enzyme Database: 3.4.21.18
///
ENTRY       EC 3.4.21.19                Enzyme
NAME        glutamyl endopeptidase;
            V8 proteinase;
            endoproteinase Glu-C;
            staphylococcal serine proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage: Glu!, Asp!
COMMENT     From Staphylococcus aureus strain V8. In appropriate buffer the
            specificity is restricted to Glu!. In peptidase family S1 (trypsin
            family)
REFERENCE   1  [PMID:1012010]
  AUTHORS   Drapeau GR.
  TITLE     Protease from Staphyloccus aureus.
  JOURNAL   Methods. Enzymol. 45 (1976) 469-75.
  ORGANISM  Staphyloccus aureus
REFERENCE   2  [PMID:96922]
  AUTHORS   Drapeau GR.
  TITLE     The primary structure of staphylococcal protease.
  JOURNAL   Can. J. Biochem. 56 (1978) 534-44.
  ORGANISM  Streptomyces griseus
REFERENCE   3  [PMID:3306605]
  AUTHORS   Carmona C, Gray GL.
  TITLE     Nucleotide sequence of the serine protease gene of Staphylococcus
            aureus, strain V8.
  JOURNAL   Nucleic. Acids. Res. 15 (1987) 6757.
  ORGANISM  Staphyloccus aureus
ORTHOLOGY   KO: K01318  glutamyl endopeptidase
GENES       MLO: mll3306
            BCE: BC0789
            BLI: BL01804(mpr)
            BLD: BLi00340(mpr)
            SAU: SA0901(sspA)
            SAV: SAV1048(sspA)
            SAM: MW0932(sspA)
            SAR: SAR1022(sspA)
            SAS: SAS0984
            SAC: SACOL1057(sspA)
            SAB: SAB0915c(sspA)
            SAA: SAUSA300_0951(sspA) SAUSA300_1753(splF) SAUSA300_1754(splE)
                 SAUSA300_1755(splD) SAUSA300_1756(splC) SAUSA300_1757(splB)
                 SAUSA300_1758(splA)
            SAO: SAOUHSC_00988 SAOUHSC_01935 SAOUHSC_01936 SAOUHSC_01938
                 SAOUHSC_01942
            SAJ: SaurJH9_1107
            SAH: SaurJH1_1130
            SEP: SE1543
            SER: SERP1397(sspA)
            SSP: SSP0282
            CTC: CTC00612
            RBA: RB4269
STRUCTURES  PDB: 1QY6  1WCZ  1ZYO  2O8L  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.19
            ExPASy - ENZYME nomenclature database: 3.4.21.19
            ExplorEnz - The Enzyme Database: 3.4.21.19
            ERGO genome analysis and discovery system: 3.4.21.19
            BRENDA, the Enzyme Database: 3.4.21.19
            CAS: 137010-42-5
///
ENTRY       EC 3.4.21.20                Enzyme
NAME        cathepsin G;
            chymotrypsin-like proteinase;
            neutral proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Specificity similar to chymotrypsin C
COMMENT     From azurophil granules of polymorphonuclear leukocytes. In
            peptidase family S1 (trypsin family)
REFERENCE   1  [PMID:7341917]
  AUTHORS   Barrett AJ.
  TITLE     Cathepsin G.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 561-5.
REFERENCE   2  [PMID:4016099]
  AUTHORS   Tanaka T, Minematsu Y, Reilly CF, Travis J, Powers JC.
  TITLE     Human leukocyte cathepsin G. Subsite mapping with 4-nitroanilides,
            chemical modification, and effect of possible cofactors.
  JOURNAL   Biochemistry. 24 (1985) 2040-7.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:2569462]
  AUTHORS   Hohn PA, Popescu NC, Hanson RD, Salvesen G, Ley TJ.
  TITLE     Genomic organization and chromosomal localization of the human
            cathepsin G gene.
  JOURNAL   J. Biol. Chem. 264 (1989) 13412-9.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04080  Neuroactive ligand-receptor interaction
            PATH: map04614  Renin-angiotensin system
ORTHOLOGY   KO: K01319  cathepsin G
GENES       HSA: 1511(CTSG)
            PTR: 467413(CTSG)
            MMU: 13035(Ctsg)
            RNO: 290257(Ctsg_predicted)
            CFA: 608543(CTSG)
            BTA: 505658(LOC505658)
            GGA: 426049(CTSG)
STRUCTURES  PDB: 1AU8  1CGH  1KYN  1T32  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.20
            ExPASy - ENZYME nomenclature database: 3.4.21.20
            ExplorEnz - The Enzyme Database: 3.4.21.20
            ERGO genome analysis and discovery system: 3.4.21.20
            BRENDA, the Enzyme Database: 3.4.21.20
            CAS: 56645-49-9
///
ENTRY       EC 3.4.21.21                Enzyme
NAME        coagulation factor VIIa;
            blood-coagulation factor VIIa;
            activated blood coagulation factor VII
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage of Arg!Ile bond in factor X to form factor Xa
INHIBITOR   Isoflurophate [CPD:C00202]
COMMENT     Formed from the precursor factor VII. The cattle enzyme is more
            readily inhibited by diisopropyl fluorophosphate than the human [1].
            In peptidase family S1 (trypsin family)
REFERENCE   1  [PMID:4510277]
  AUTHORS   Nemerson Y, Esnouf MP.
  TITLE     Activation of a proteolytic system by a membrane lipoprotein:
            mechanism of action of tissue factor.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 70 (1973) 310-4.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:367103]
  AUTHORS   Davie EW, Fujikawa K, Kurachi K, Kisiel W.
  TITLE     The role of serine proteases in the blood coagulation cascade.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 48 (1979) 277-318.
REFERENCE   3  [PMID:6996572]
  AUTHORS   Jackson CM, Nemerson Y.
  TITLE     Blood coagulation.
  JOURNAL   Annu. Rev. Biochem. 49 (1980) 765-811.
REFERENCE   4
  AUTHORS   Broze, G.J., Jr. and Majerus, P.W.
  TITLE     Human factor VII.
  JOURNAL   Methods Enzymol. 80 (1981) 228-237.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01320  coagulation factor VII
GENES       HSA: 2155(F7)
            PTR: 452678(MCF2L)
            MMU: 14068(F7)
            RNO: 260320(F7)
            CFA: 607661(F7)
            BTA: 617960(F7)
            GGA: 395086(F7)
            XLA: 444394(MGC82927)
            DRE: 114423(f7)
STRUCTURES  PDB: 1BF9  1CVW  1DAN  1DVA  1FAK  1JBU  1KLI  1KLJ  1O5D  1QFK  
                 1W0Y  1W2K  1W7X  1W8B  1WQV  1WSS  1WTG  1WUN  1WV7  1YGC  
                 1Z6J  2A2Q  2AEI  2AER  2B7D  2B8O  2BZ6  2C4F  2F9B  2FIR  
                 2FLR  2PUQ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.21
            ExPASy - ENZYME nomenclature database: 3.4.21.21
            ExplorEnz - The Enzyme Database: 3.4.21.21
            ERGO genome analysis and discovery system: 3.4.21.21
            BRENDA, the Enzyme Database: 3.4.21.21
            CAS: 65312-43-8
///
ENTRY       EC 3.4.21.22                Enzyme
NAME        coagulation factor IXa;
            activated Christmas factor;
            blood-coagulation factor IXa;
            activated blood-coagulation factor IX;
            autoprothrombin II;
            blood platelet cofactor II;
            activated blood coagulation factor XI
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage of Arg!Ile bond in factor X to form factor Xa
COMMENT     A chymotrypsin homologue, and one of the gamma-carboxyglutamic
            acid-containing blood coagulation factors. The proenzyme factor IX
            is activated by factor XIa. In peptidase family S1 (trypsin family)
REFERENCE   1  [PMID:1012029]
  AUTHORS   Fujikawa K, Davie EW.
  TITLE     Bovine factor IX (Christmas factor).
  JOURNAL   Methods. Enzymol. 45 (1976) 74-83.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:367103]
  AUTHORS   Davie EW, Fujikawa K, Kurachi K, Kisiel W.
  TITLE     The role of serine proteases in the blood coagulation cascade.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 48 (1979) 277-318.
REFERENCE   3  [PMID:6412750]
  AUTHORS   Link RP, Castellino FJ.
  TITLE     Kinetic comparison of bovine blood coagulation factors IXa alpha and
            IXa beta toward bovine factor X.
  JOURNAL   Biochemistry. 22 (1983) 4033-41.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:6370301]
  AUTHORS   Cho K, Tanaka T, Cook RR, Kisiel W, Fujikawa K, Kurachi K, Powers
            JC.
  TITLE     Active-site mapping of bovine and human blood coagulation serine
            proteases using synthetic peptide 4-nitroanilide and thio ester
            substrates.
  JOURNAL   Biochemistry. 23 (1984) 644-50.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01321  coagulation factor IX (Christmas factor)
GENES       HSA: 2158(F9)
            PTR: 465887(F9)
            MMU: 14071(F9)
            RNO: 24946(F9)
            CFA: 404015(F9)
            BTA: 280688(F9)
            GGA: 374258(F9)
            XTR: 496659(f9)
STRUCTURES  PDB: 1CFI  1J34  1J35  1MGX  1PFX  1X7A  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.22
            ExPASy - ENZYME nomenclature database: 3.4.21.22
            ExplorEnz - The Enzyme Database: 3.4.21.22
            ERGO genome analysis and discovery system: 3.4.21.22
            BRENDA, the Enzyme Database: 3.4.21.22
            CAS: 37316-87-3
///
ENTRY       EC 3.4.21.23      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Deleted entry: Vipera russelli proteinase (EC 3.4.21.23 created
            1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.23
            ExPASy - ENZYME nomenclature database: 3.4.21.23
            ExplorEnz - The Enzyme Database: 3.4.21.23
            ERGO genome analysis and discovery system: 3.4.21.23
            BRENDA, the Enzyme Database: 3.4.21.23
///
ENTRY       EC 3.4.21.24      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Deleted entry: red cell neutral endopeptidase (EC 3.4.21.24 created
            1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.24
            ExPASy - ENZYME nomenclature database: 3.4.21.24
            ExplorEnz - The Enzyme Database: 3.4.21.24
            ERGO genome analysis and discovery system: 3.4.21.24
            BRENDA, the Enzyme Database: 3.4.21.24
///
ENTRY       EC 3.4.21.25                Enzyme
NAME        cucumisin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins with broad specificity
COMMENT     From the sarcocarp of the musk melon (Cucumis melo). In peptidase
            family S8 (subtilisin family). Other endopeptidases from plants,
            which are less well characterized but presumably of serine-type,
            include euphorbain from Euphorbia cerifera [6], solanain from
            horse-nettle Solanum elaeagnifolium [1], hurain from Hura crepitans
            [2] and tabernamontanain from Tabernamontana grandiflora [3].
REFERENCE   1
  AUTHORS   Greenberg, D.M. and Winnick, T.
  TITLE     Plant proteases. I. Activation-inhibition reactions.
  JOURNAL   J. Biol. Chem. 135 (1940) 761-773.
REFERENCE   2
  AUTHORS   Jaffe, W.G.
  TITLE     Hurain, a new plant protease from Hura crepitans.
  JOURNAL   J. Biol. Chem. 149 (1943) 1-7.
  ORGANISM  Hura crepitans
REFERENCE   3
  AUTHORS   Jaffe, W.G.
  TITLE     A new vegetable proteolytic enzyme of the papain class.
  JOURNAL   Rev. Brasil Biol. 3 (1943) 149-157.
REFERENCE   4  [PMID:5423]
  AUTHORS   Kaneda M, Tominaga N.
  TITLE     Isolation and characterization of a proteinase from the sarcocarp of
            melon fruit.
  JOURNAL   J. Biochem. (Tokyo). 78 (1975) 1287-96.
  ORGANISM  Cucumis melo
REFERENCE   5  [PMID:6427203]
  AUTHORS   Kaneda M, Ohmine H, Yonezawa H, Tominaga N.
  TITLE     Amino acid sequence around the reactive serine of cucumisin from
            melon fruit.
  JOURNAL   J. Biochem. (Tokyo). 95 (1984) 825-9.
  ORGANISM  Cucumis melo
REFERENCE   6
  AUTHORS   Lynn, K.R. and Clevette-Radford, N.A.
  TITLE     Two proteases from the latex of Elaeophorbia drupifera.
  JOURNAL   Phytochemistry 24 (1985) 2843-2845.
  ORGANISM  Elaeophorbia drupifera
REFERENCE   7
  AUTHORS   Kaneda, N., Minematsu, Y., Powers, J.C. and Tominaga, N.
  TITLE     Specificity of cucumisin in hydrolysis of peptide thiobenzyl esters.
  JOURNAL   Agric. Biol. Chem. 50 (1986) 1075-1076.
  ORGANISM  Cucumis melo
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.25
            ExPASy - ENZYME nomenclature database: 3.4.21.25
            ExplorEnz - The Enzyme Database: 3.4.21.25
            ERGO genome analysis and discovery system: 3.4.21.25
            BRENDA, the Enzyme Database: 3.4.21.25
            CAS: 82062-89-3
///
ENTRY       EC 3.4.21.26                Enzyme
NAME        prolyl oligopeptidase;
            post-proline cleaving enzyme;
            proline-specific endopeptidase;
            post-proline endopeptidase;
            proline endopeptidase;
            endoprolylpeptidase;
            prolyl endopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of ---Pro! and to a lesser extent ---Ala! in
            oligopeptides
COMMENT     Found in vertebrates, plants and Flavobacterium. Generally
            cytosolic, commonly activated by thiol compounds. Type example of
            peptidase family S9.
REFERENCE   1  [PMID:708698]
  AUTHORS   Walter R, Yoshimoto T.
  TITLE     Postproline cleaving enzyme: kinetic studies of size and
            stereospecificity of its active site.
  JOURNAL   Biochemistry. 17 (1978) 4139-44.
  ORGANISM  sheep
REFERENCE   2  [PMID:3539636]
  AUTHORS   Nomura K.
  TITLE     Specificity of prolyl endopeptidase.
  JOURNAL   FEBS. Lett. 209 (1986) 235-7.
  ORGANISM  rat [GN:rno], Fravobacterium sp.
REFERENCE   3  [PMID:2851585]
  AUTHORS   Moriyama A, Nakanishi M, Sasaki M.
  TITLE     Porcine muscle prolyl endopeptidase and its endogenous substrates.
  JOURNAL   J. Biochem. (Tokyo). 104 (1988) 112-7.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:1900195]
  AUTHORS   Rennex D, Hemmings BA, Hofsteenge J, Stone SR.
  TITLE     cDNA cloning of porcine brain prolyl endopeptidase and
            identification of the active-site seryl residue.
  JOURNAL   Biochemistry. 30 (1991) 2195-203.
  ORGANISM  pig [GN:ssc]
ORTHOLOGY   KO: K01322  prolyl oligopeptidase
GENES       HSA: 5550(PREP)
            PTR: 462903(PREP)
            MMU: 19072(Prep)
            RNO: 83471(Prep)
            CFA: 481945(PREP)
            BTA: 286818(PREP)
            SSC: 445540(PREP)
            GGA: 421785(PREP)
            XLA: 399432(PREP)
            XTR: 394797(prep)
            DRE: 553791(zgc:110670)
            SPU: 584505(LOC584505)
            DME: Dmel_CG2528 Dmel_CG5355
            ATH: AT1G20380
            OSA: 4326161 4336657
            CNE: CNJ00580
            DDI: DDB_0185041(dpoA)
            TBR: Tb10.6k15.2520
            TCR: 506247.230
            LMA: LmjF36.6750
            SPE: Spro_2232
            VVU: VV2_0795
            VVY: VVA1259
            VPA: VPA0468 VPA1496
            VFI: VF1122 VFA0660
            SON: SO_2753
            SDN: Sden_2940
            SFR: Sfri_3635
            SAZ: Sama_1757 Sama_2091
            SBL: Sbal_1741
            SBM: Shew185_1737 Shew185_2255
            SLO: Shew_1522
            SPC: Sputcn32_1602 Sputcn32_2098
            SSE: Ssed_1852
            SPL: Spea_2569 Spea_3588
            SHE: Shewmr4_2104 Shewmr4_2373
            SHM: Shewmr7_1870 Shewmr7_2445
            SHN: Shewana3_2229 Shewana3_2536
            SHW: Sputw3181_1914 Sputw3181_2420
            ILO: IL0145
            CPS: CPS_0086 CPS_3511
            PHA: PSHAa1273
            PAT: Patl_2782
            AHA: AHA_0767
            DNO: DNO_1338(ptrB)
            NMA: NMA0579
            NMC: NMC0342
            CVI: CV_4306(preP)
            BUR: Bcep18194_A5455
            BPM: BURPS1710b_A0367(ptrB) BURPS1710b_A1761
            MXA: MXAN_2016(pep) MXAN_5460
            RTY: RT0165(ppcE)
            RFE: RF_1104 RF_1105
            MLO: mll1209
            RLE: RL1575
            BRA: BRADO6844
            BBT: BBta_0699
            RPE: RPE_1599
            MMR: Mmar10_0018
            HNE: HNE_0034
            NAR: Saro_2524 Saro_2525
            SAL: Sala_1978
            SWI: Swit_1324
            GOX: GOX0700
            GBE: GbCGDNIH1_1175
            ABA: Acid345_0615 Acid345_4142
            SUS: Acid_6251
            BCZ: BCZK0158
            BTL: BALH_0163
            MSM: MSMEG_0899
            MVA: Mvan_0785
            MGI: Mflv_0127
            MMC: Mmcs_0623
            MKM: Mkms_0636
            MJL: Mjls_0616
            CGL: NCgl0333(cgl0340)
            CGB: cg0410
            CEF: CE0354
            CDI: DIP0364
            RHA: RHA1_ro02141
            TFU: Tfu_1856 Tfu_2212
            ACE: Acel_1604
            KRA: Krad_3530
            SEN: SACE_1333
            RBA: RB12337
            TDE: TDE1195
            CYA: CYA_2555
            CYB: CYB_2532
            GVI: gll0625 gll0681 glr3271
            ANA: all2533
            AVA: Ava_0462
            TER: Tery_3157
            GFO: GFO_3350
            FJO: Fjoh_1313 Fjoh_5032
            CTE: CT1301
            CPH: Cpha266_1010
            PVI: Cvib_1063
            PLT: Plut_0781
            DRA: DR_2503
            PTO: PTO1489
            PHO: PH1262
            PAB: PAB0762
            PFU: PF0825
            TKO: TK0423
            STO: ST0002
STRUCTURES  PDB: 1E5T  1E8M  1E8N  1H2W  1H2X  1H2Y  1H2Z  1O6F  1O6G  1QFM  
                 1QFS  1UOO  1UOP  1UOQ  1VZ2  1VZ3  1YR2  2BKL  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.26
            ExPASy - ENZYME nomenclature database: 3.4.21.26
            ExplorEnz - The Enzyme Database: 3.4.21.26
            ERGO genome analysis and discovery system: 3.4.21.26
            BRENDA, the Enzyme Database: 3.4.21.26
            CAS: 72162-84-6
///
ENTRY       EC 3.4.21.27                Enzyme
NAME        coagulation factor XIa;
            blood-coagulation factor XIa;
            activated blood-coagulation factor XI;
            activated plasma thromboplastin antecedent
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage of Arg!Ala and Arg!Val bonds in factor IX to form
            factor IXa
COMMENT     In peptidase family S1 (trypsin family), and one of the
            gamma-carboxyglutamic acid-containing blood coagulation factors. The
            proenzyme factor XI is activated by factor XIIa
REFERENCE   1
  AUTHORS   Kurachi, K. and Davie, E.W.
  TITLE     Human factor XI (plasma thromboplastin antecedent).
  JOURNAL   Methods Enzymol. 80 (1981) 211-220.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:6370301]
  AUTHORS   Cho K, Tanaka T, Cook RR, Kisiel W, Fujikawa K, Kurachi K, Powers
            JC.
  TITLE     Active-site mapping of bovine and human blood coagulation serine
            proteases using synthetic peptide 4-nitroanilide and thio ester
            substrates.
  JOURNAL   Biochemistry. 23 (1984) 644-50.
  ORGANISM  human [GN:hsa], cow [GN:bta]
REFERENCE   3  [PMID:3636155]
  AUTHORS   Fujikawa K, Chung DW, Hendrickson LE, Davie EW.
  TITLE     Amino acid sequence of human factor XI, a blood coagulation factor
            with four tandem repeats that are highly homologous with plasma
            prekallikrein.
  JOURNAL   Biochemistry. 25 (1986) 2417-24.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01323  coagulation factor XI
GENES       HSA: 2160(F11)
            MMU: 109821(F11)
            BTA: 407998(F11)
STRUCTURES  PDB: 1XX9  1XXD  1XXF  1ZHM  1ZHP  1ZHR  1ZJD  1ZLR  1ZMJ  1ZML  
                 1ZMN  1ZOM  1ZPB  1ZPC  1ZPZ  1ZRK  1ZSJ  1ZSK  1ZSL  1ZTJ  
                 1ZTK  1ZTL  2F83  2FDA  2J8J  2J8L  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.27
            ExPASy - ENZYME nomenclature database: 3.4.21.27
            ExplorEnz - The Enzyme Database: 3.4.21.27
            ERGO genome analysis and discovery system: 3.4.21.27
            BRENDA, the Enzyme Database: 3.4.21.27
            CAS: 37203-61-5
///
ENTRY       EC 3.4.21.28      Obsolete  Enzyme
NAME        Transferred to 3.4.21.74
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Transferred entry: now EC 3.4.21.74 venombin A (EC 3.4.21.28 created
            1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.28
            ExPASy - ENZYME nomenclature database: 3.4.21.28
            ExplorEnz - The Enzyme Database: 3.4.21.28
            ERGO genome analysis and discovery system: 3.4.21.28
            BRENDA, the Enzyme Database: 3.4.21.28
///
ENTRY       EC 3.4.21.29      Obsolete  Enzyme
NAME        Transferred to 3.4.21.74
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Transferred entry: now EC 3.4.21.74 venombin A (EC 3.4.21.29 created
            1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.29
            ExPASy - ENZYME nomenclature database: 3.4.21.29
            ExplorEnz - The Enzyme Database: 3.4.21.29
            ERGO genome analysis and discovery system: 3.4.21.29
            BRENDA, the Enzyme Database: 3.4.21.29
///
ENTRY       EC 3.4.21.30      Obsolete  Enzyme
NAME        Transferred to 3.4.21.74
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Transferred entry: now EC 3.4.21.74 venombin A (EC 3.4.21.30 created
            1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.30
            ExPASy - ENZYME nomenclature database: 3.4.21.30
            ExplorEnz - The Enzyme Database: 3.4.21.30
            ERGO genome analysis and discovery system: 3.4.21.30
            BRENDA, the Enzyme Database: 3.4.21.30
///
ENTRY       EC 3.4.21.31      Obsolete  Enzyme
NAME        Transferred to 3.4.21.73
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Transferred entry: now EC 3.4.21.73 u-plasminogen activator (EC
            3.4.21.31 created 1972 as EC 3.4.99.26, transferred 1978 to EC
            3.4.21.31, deleted 1992)
STRUCTURES  PDB: 1TPK  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.31
            ExPASy - ENZYME nomenclature database: 3.4.21.31
            ExplorEnz - The Enzyme Database: 3.4.21.31
            ERGO genome analysis and discovery system: 3.4.21.31
            BRENDA, the Enzyme Database: 3.4.21.31
///
ENTRY       EC 3.4.21.32                Enzyme
NAME        brachyurin;
            Uca pugilator collagenolytic proteinase;
            crab protease I;
            crab protease II
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins, with broad specificity for peptide bonds.
            Native collagen is cleaved about 75% of the length of the molecule
            from the N-terminus. Low activity on small molecule substrates of
            both trypsin and chymotrypsin
INHIBITOR   Tos-Lys-CH2Cl [CPD:C00896]
COMMENT     From hepatopancreas of the fiddler crab, Uca pugilator. In peptidase
            family S1 (trypsin family). Other serine endopeptidases that degrade
            collagen, but are not listed separately here, include a second
            endopeptidase from Uca pugilator [4], digestive enzymes from other
            decapod crustacea [5,6], and an enzyme from the fungus Entomophthora
            coronata [1].
REFERENCE   1  [PMID:219780]
  AUTHORS   Hurion N, Fromentin H, Keil B.
  TITLE     Specificity of the collagenolytic enzyme from the fungus
            Entomophthora coronata: comparison with the bacterial collagenase
            from Achromobacter iophagus.
  JOURNAL   Arch. Biochem. Biophys. 192 (1979) 438-45.
  ORGANISM  Uca pugilator
REFERENCE   2
  AUTHORS   Grant, G.A., Eisen, A.Z. and Bradshaw, R.A.
  TITLE     Collagenolytic protease from fiddler crab (Uca pugilator).
  JOURNAL   Methods Enzymol. 80 (1981) 722-734.
  ORGANISM  Uca pugilator
REFERENCE   3  [PMID:6756469]
  AUTHORS   Welgus HG, Grant GA, Jeffrey JJ, Eisen AZ.
  TITLE     Substrate specificity of the collagenolytic serine protease from Uca
            pugilator: studies with collagenous substrates.
  JOURNAL   Biochemistry. 21 (1982) 5183-9.
  ORGANISM  Uca pugilator
REFERENCE   4  [PMID:6305411]
  AUTHORS   Welgus HG, Grant GA.
  TITLE     Degradation of collagen substrates by a trypsin-like serine protease
            from the fiddler crab Uca pugilator.
  JOURNAL   Biochemistry. 22 (1983) 2228-33.
  ORGANISM  Uca pugilator
REFERENCE   5  [PMID:2154979]
  AUTHORS   Klimova OA, Borukhov SI, Solovyeva NI, Balaevskaya TO, Strongin AYa.
  TITLE     The isolation and properties of collagenolytic proteases from crab
            hepatopancreas.
  JOURNAL   Biochem. Biophys. Res. Commun. 166 (1990) 1411-20.
  ORGANISM  Uca pugilator
REFERENCE   6  [PMID:1963309]
  AUTHORS   Lu PJ, Liu HC, Tsai IH.
  TITLE     The midgut trypsins of shrimp (Penaeus monodon). High efficiency
            toward native protein substrates including collagens.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 371 (1990) 851-9.
  ORGANISM  Penaeus monodon
STRUCTURES  PDB: 1AZZ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.32
            ExPASy - ENZYME nomenclature database: 3.4.21.32
            ExplorEnz - The Enzyme Database: 3.4.21.32
            ERGO genome analysis and discovery system: 3.4.21.32
            BRENDA, the Enzyme Database: 3.4.21.32
///
ENTRY       EC 3.4.21.33      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Deleted entry: Entomophthora collagenolytic proteinase (EC 3.4.21.33
            created 1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.33
            ExPASy - ENZYME nomenclature database: 3.4.21.33
            ExplorEnz - The Enzyme Database: 3.4.21.33
            ERGO genome analysis and discovery system: 3.4.21.33
            BRENDA, the Enzyme Database: 3.4.21.33
///
ENTRY       EC 3.4.21.34                Enzyme
NAME        plasma kallikrein;
            serum kallikrein;
            kininogenin;
            kallikrein I;
            kallikrein II;
            kininogenase;
            kallikrein;
            callicrein;
            glumorin;
            padreatin;
            padutin;
            kallidinogenase;
            bradykininogenase;
            panceatic kallikrein;
            onokrein P;
            dilminal D;
            depot-Padutin;
            urokallikrein;
            urinary kallikrein
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage of some Arg! and Lys! bonds, including Lys!Arg
            and Arg!Ser in (human) kininogen to release bradykinin
COMMENT     Formed from plasma prokallikrein (Fletcher factor) by factor XIIa.
            Activates coagulation factors XII, VII and plasminogen. Selective
            for Arg > Lys in P1, in small molecule substrates.
REFERENCE   1  [PMID:6918767]
  AUTHORS   Heimark RL, Davie EW.
  TITLE     Bovine and human plasma prekallikrein.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 157-72.
  ORGANISM  human [GN:hsa], cow [GN:bta]
REFERENCE   2  [PMID:6976185]
  AUTHORS   McRae BJ, Kurachi K, Heimark RL, Fujikawa K, Davie EW, Powers JC.
  TITLE     Mapping the active sites of bovine thrombin, factor IXa, factor Xa,
            factor XIa, factor XIIa, plasma kallikrein, and trypsin with amino
            acid and peptide thioesters: development of new sensitive
            substrates.
  JOURNAL   Biochemistry. 20 (1981) 7196-206.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:3237096]
  AUTHORS   Silverberg M, Kaplan AP.
  TITLE     Prekallikrein.
  JOURNAL   Methods. Enzymol. 163 (1988) 85-95.
REFERENCE   4  [PMID:2598771]
  AUTHORS   Seidah NG, Ladenheim R, Mbikay M, Hamelin J, Lutfalla G, Rougeon F,
            Lazure C, Chretien M.
  TITLE     The cDNA structure of rat plasma kallikrein.
  JOURNAL   DNA. 8 (1989) 563-74.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:2534361]
  AUTHORS   Tsuda Y, Teno N, Okada Y, Wanaka K, Bohgaki M, Hijikata-Okunomiya A,
            Okamoto U, Naito T, Okamoto S.
  TITLE     Synthesis of tripeptide chloromethyl ketones and examination of
            their inhibitory effects on plasmin and plasma kallikrein.
  JOURNAL   Chem. Pharm. Bull. (Tokyo). 37 (1989) 3108-11.
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01324  plasma kallikrein
GENES       HSA: 3818(KLKB1)
            PTR: 471375(KLKB1)
            MMU: 16621(Klkb1)
            RNO: 25048(Klkb1)
            CFA: 475624(KLKB1)
            BTA: 533547(KLKB1)
            SSC: 397144(KLKB1)
            GGA: 422723(F11)
            XLA: 446603(klkb1)
STRUCTURES  PDB: 2ANW  2ANY  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.34
            ExPASy - ENZYME nomenclature database: 3.4.21.34
            ExplorEnz - The Enzyme Database: 3.4.21.34
            ERGO genome analysis and discovery system: 3.4.21.34
            BRENDA, the Enzyme Database: 3.4.21.34
///
ENTRY       EC 3.4.21.35                Enzyme
NAME        tissue kallikrein;
            glandular kallikrein;
            pancreatic kallikrein;
            submandibular kallikrein;
            submaxillary kallikrein;
            kidney kallikrein;
            urinary kallikrein;
            kallikrein;
            salivary kallikrein;
            kininogenin;
            kininogenase;
            callicrein;
            glumorin;
            padreatin;
            padutin;
            kallidinogenase;
            bradykininogenase;
            depot-padutin;
            urokallikrein;
            dilminal D;
            onokrein P
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage of Arg! bonds in small molecule substrates.
            Highly selective action to release kallidin (lysyl-bradykinin) from
            kininogen involves hydrolysis of Met! or Leu!. The rat enzyme is
            unusual in liberating bradykinin directly from autologous kininogens
            by cleavage at two Arg! bonds [5]
COMMENT     Formed from tissue prokallikrein by activation with trypsin. In
            peptidase family S1 (trypsin family). A large number of tissue
            kallikrein-related sequences have been reported for rats [16] and
            mice [7], though fewer seem to exist in other mammals. The few that
            have been isolated and tested on substrates include mouse
            gamma-renin (EC 3.4.21.54), submandibular proteinase A [2,15],
            epidermal growth-factor-binding protein, nerve growth factor
            gamma-subunit, rat tonin [3,4,9], submaxillary proteinases A and B
            [10], T-kininogenase [18], kallikreins k7 and k8 [17] and human
            prostate-specific antigen (gamma-seminoprotein, [6])
REFERENCE   1  [PMID:7043199]
  AUTHORS   Fiedler F, Fink E, Tschesche H, Fritz H.
  TITLE     Porcine glandular kallikreins.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 493-532.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:6295764]
  AUTHORS   Anundi H, Ronne H, Peterson PA, Rask L.
  TITLE     Partial amino-acid sequence of the epidermal growth-factor-binding
            protein.
  JOURNAL   Eur. J. Biochem. 129 (1982) 365-71.
REFERENCE   3  [PMID:6295383]
  AUTHORS   Pesquero JL, Boschcov P, Oliveira MC, Paiva AC.
  TITLE     Effect of substrate size on tonin activity.
  JOURNAL   Biochem. Biophys. Res. Commun. 108 (1982) 1441-6.
REFERENCE   4  [PMID:6043136]
  AUTHORS   Schack P.
  TITLE     Fractionation of proteolytic enzymes of dried papaya latex.
            Isolation and preliminary characterization of a new proteolytic
            enzyme.
  JOURNAL   C. R. Trav. Lab. Carlsberg. 36 (1967) 67-83.
  ORGANISM  papaya
REFERENCE   5  [PMID:3844939]
  AUTHORS   Kato H, Enjyoji K, Miyata T, Hayashi I, Oh-ishi S, Iwanaga S.
  TITLE     Demonstration of arginyl-bradykinin moiety in rat HMW kininogen:
            direct evidence for liberation of bradykinin by rat glandular
            kallikreins.
  JOURNAL   Biochem. Biophys. Res. Commun. 127 (1985) 289-95.
  ORGANISM  rat [GN:rno]
REFERENCE   6  [PMID:3691800]
  AUTHORS   Akiyama K, Nakamura T, Iwanaga S, Hara M.
  TITLE     The chymotrypsin-like activity of human prostate-specific antigen,
            gamma-seminoprotein.
  JOURNAL   FEBS. Lett. 225 (1987) 168-72.
  ORGANISM  human [GN:hsa]
REFERENCE   7  [PMID:3036794]
  AUTHORS   Evans BA, Drinkwater CC, Richards RI.
  TITLE     Mouse glandular kallikrein genes. Structure and partial sequence
            analysis of the kallikrein gene locus.
  JOURNAL   J. Biol. Chem. 262 (1987) 8027-34.
  ORGANISM  mouse [GN:mmu]
REFERENCE   8  [PMID:3643848]
  AUTHORS   Fiedler F.
  TITLE     Effects of secondary interactions on the kinetics of peptide and
            peptide ester hydrolysis by tissue kallikrein and trypsin.
  JOURNAL   Eur. J. Biochem. 163 (1987) 303-12.
REFERENCE   9  [PMID:2821276]
  AUTHORS   Fujinaga M, James MN.
  TITLE     Rat submaxillary gland serine protease, tonin. Structure solution
            and refinement at 1.8 A resolution.
  JOURNAL   J. Mol. Biol. 195 (1987) 373-96.
  ORGANISM  rat [GN:rno]
REFERENCE   10 [PMID:3844939]
  AUTHORS   Kato H, Enjyoji K, Miyata T, Hayashi I, Oh-ishi S, Iwanaga S.
  TITLE     Demonstration of arginyl-bradykinin moiety in rat HMW kininogen:
            direct evidence for liberation of bradykinin by rat glandular
            kallikreins.
  JOURNAL   Biochem. Biophys. Res. Commun. 127 (1985) 289-95.
  ORGANISM  rat [GN:rno]
REFERENCE   11 [PMID:3237072]
  AUTHORS   Bailey GS.
  TITLE     Rat pancreas kallikrein.
  JOURNAL   Methods. Enzymol. 163 (1988) 115-28.
  ORGANISM  rat [GN:rno]
REFERENCE   12 [PMID:2611215]
  AUTHORS   Blaber M, Isackson PJ, Marsters JC Jr, Burnier JP, Bradshaw RA.
  TITLE     Substrate specificities of growth factor associated kallikreins of
            the mouse submandibular gland.
  JOURNAL   Biochemistry. 28 (1989) 7813-9.
  ORGANISM  mouse [GN:mmu]
REFERENCE   13 [PMID:3070295]
  AUTHORS   Chao J, Chao L.
  TITLE     Rat urinary kallikrein.
  JOURNAL   Methods. Enzymol. 163 (1988) 128-43.
  ORGANISM  rat [GN:rno]
REFERENCE   14 [PMID:2975076]
  AUTHORS   Zakrevskaia SF.
  TITLE     [Effectiveness of outpatient dental care for the schoolchildren of
            Arkhangelsk]
  JOURNAL   Stomatologiia. (Mosk). 67 (1988) 62-3.
REFERENCE   15 [PMID:2523317]
  AUTHORS   Bertrand R, Derancourt J, Kassab R.
  TITLE     Selective cleavage at lysine of the 50 kDa-20 kDa connector loop
            segment of skeletal myosin S-1 by endoproteinase Arg-C.
  JOURNAL   FEBS. Lett. 246 (1989) 171-6.
REFERENCE   16 [PMID:2708383]
  AUTHORS   Wines DR, Brady JM, Pritchett DB, Roberts JL, MacDonald RJ.
  TITLE     Organization and expression of the rat kallikrein gene family.
  JOURNAL   J. Biol. Chem. 264 (1989) 7653-62.
  ORGANISM  rat [GN:rno]
REFERENCE   17 [PMID:2194829]
  AUTHORS   Elmoujahed A, Gutman N, Brillard M, Gauthier F.
  TITLE     Substrate specificity of two kallikrein family gene products
            isolated from the rat submaxillary gland.
  JOURNAL   FEBS. Lett. 265 (1990) 137-40.
  ORGANISM  rat [GN:rno]
REFERENCE   18 [PMID:2303430]
  AUTHORS   Xiong W, Chen LM, Chao J.
  TITLE     Purification and characterization of a kallikrein-like
            T-kininogenase.
  JOURNAL   J. Biol. Chem. 265 (1990) 2822-7.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K01325  tissue kallikrein
GENES       HSA: 3816(KLK1) 3817(KLK2)
            MMU: 13646(Klk1b22) 13648(Klk1b9) 16612(Klk1) 16613(Klk1b11)
                 16616(Klk1b21) 16617(Klk1b24) 16618(Klk1b26) 16622(Klk1b5)
                 16623(Klk1b1) 16624(Klk1b8) 18050(Klk1b3)
            RNO: 24523(Klk7) 24594(Ngfg) 24841(Ton) 292855(Klk12)
                 292866(Klk6_predicted)
            CFA: 403942(KLK1)
            BTA: 493738(KLK1)
            SSC: 431673(KLK1)
            AHA: AHA_3330
STRUCTURES  PDB: 1AO5  1HIA  1SGF  1SPJ  2PKA  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.35
            ExPASy - ENZYME nomenclature database: 3.4.21.35
            ExplorEnz - The Enzyme Database: 3.4.21.35
            ERGO genome analysis and discovery system: 3.4.21.35
            BRENDA, the Enzyme Database: 3.4.21.35
///
ENTRY       EC 3.4.21.36                Enzyme
NAME        pancreatic elastase;
            pancreatopeptidase E;
            pancreatic elastase I;
            elastase;
            elaszym;
            serine elastase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins, including elastin. Preferential cleavage:
            Ala!
COMMENT     Formed by activation of proelastase from mammalian pancreas by
            trypsin. In peptidase family S1 (trypsin family). Formerly included
            in EC 3.4.21.11
REFERENCE   1
  AUTHORS   Shotton, D.M.
  TITLE     Elastase.
  JOURNAL   Methods Enzymol. 19 (1970) 113-140.
REFERENCE   2  [PMID:6380580]
  AUTHORS   Harper JW, Cook RR, Roberts CJ, McLaughlin BJ, Powers JC.
  TITLE     Active site mapping of the serine proteases human leukocyte
            elastase, cathepsin G, porcine pancreatic elastase, rat mast cell
            proteases I and II. Bovine chymotrypsin A alpha, and Staphylococcus
            aureus protease V-8 using tripeptide thiobenzyl ester substrates.
  JOURNAL   Biochemistry. 23 (1984) 2995-3002.
  ORGANISM  human [GN:hsa], rat [GN:rno], pig [GN:ssc]
REFERENCE   3  [PMID:3646943]
  AUTHORS   Kawashima I, Tani T, Shimoda K, Takiguchi Y.
  TITLE     Characterization of pancreatic elastase II cDNAs: two elastase II
            mRNAs are expressed in human pancreas.
  JOURNAL   DNA. 6 (1987) 163-72.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:2909256]
  AUTHORS   Bieth JG, Dirrig S, Jung ML, Boudier C, Papamichael E, Sakarellos C,
            Dimicoli JL.
  TITLE     Investigation of the active center of rat pancreatic elastase.
  JOURNAL   Biochim. Biophys. Acta. 994 (1989) 64-74.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:2655701]
  AUTHORS   Bode W, Meyer E Jr, Powers JC.
  TITLE     Human leukocyte and porcine pancreatic elastase: X-ray crystal
            structures, mechanism, substrate specificity, and mechanism-based
            inhibitors.
  JOURNAL   Biochemistry. 28 (1989) 1951-63.
  ORGANISM  human [GN:hsa], pig [GN:ssc]
ORTHOLOGY   KO: K01326  pancreatic elastase I
GENES       HSA: 1990(ELA1)
            MMU: 109901(Ela1)
            RNO: 24331(Ela1)
            CFA: 403515(ELA1)
            BTA: 281139(ELA1)
            SSC: 396766(ELS1)
            GGA: 425200(ELA1)
            XLA: 398300(LOC398300)
            XTR: 496993(LOC496993)
            DRE: 445282(zgc:92041)
STRUCTURES  PDB: 1B0E  1BMA  1BTU  1C1M  1E34  1E35  1E36  1E37  1E38  1EAI  
                 1EAS  1EAT  1EAU  1ELA  1ELB  1ELC  1ELD  1ELE  1ELF  1ELG  
                 1ELT  1ESA  1ESB  1EST  1FLE  1FZZ  1GVK  1GWA  1H9L  1HV7  
                 1INC  1JIM  1L0Z  1L1G  1LKA  1LKB  1LVY  1MCV  1MMJ  1NES  
                 1OKX  1QGF  1QNJ  1QR3  1UO6  1UVO  1UVP  2A7C  2A7J  2BB4  
                 2BD2  2BD3  2BD4  2BD5  2BD7  2BD8  2BD9  2BDA  2BDB  2BDC  
                 2BLO  2BLQ  2CV3  2D26  2DE8  2DE9  2EST  2FO9  2FOA  2FOB  
                 2FOC  2FOD  2FOE  2FOF  2FOG  2FOH  2G4T  2G4U  2H1U  2OQU  
                 3EST  4EST  5EST  6EST  7EST  8EST  9EST  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.36
            ExPASy - ENZYME nomenclature database: 3.4.21.36
            ExplorEnz - The Enzyme Database: 3.4.21.36
            ERGO genome analysis and discovery system: 3.4.21.36
            BRENDA, the Enzyme Database: 3.4.21.36
            CAS: 9004-06-2
///
ENTRY       EC 3.4.21.37                Enzyme
NAME        leukocyte elastase;
            lysosomal elastase;
            neutrophil elastase;
            polymorphonuclear leukocyte elastase;
            elastase;
            elaszym;
            serine elastase;
            lysosomal elastase;
            granulocyte elastase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins, including elastin. Preferential cleavage
            Val! > Ala!
COMMENT     Differs from pancreatic elastase in specificity on synthetic
            substrates and in inhibitor sensitivity. In peptidase family S1
            (trypsin family). Formerly included in EC 3.4.21.11
REFERENCE   1  [PMID:7043201]
  AUTHORS   Barrett AJ.
  TITLE     Leukocyte elastase.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 581-8.
REFERENCE   2  [PMID:6380580]
  AUTHORS   Harper JW, Cook RR, Roberts CJ, McLaughlin BJ, Powers JC.
  TITLE     Active site mapping of the serine proteases human leukocyte
            elastase, cathepsin G, porcine pancreatic elastase, rat mast cell
            proteases I and II. Bovine chymotrypsin A alpha, and Staphylococcus
            aureus protease V-8 using tripeptide thiobenzyl ester substrates.
  JOURNAL   Biochemistry. 23 (1984) 2995-3002.
  ORGANISM  human [GN:hsa], rat [GN:rno], cow [GN:bta], Staphylococcus aureus
REFERENCE   3  [PMID:3646070]
  AUTHORS   Stein RL, Strimpler AM, Hori H, Powers JC.
  TITLE     Catalysis by human leukocyte elastase: mechanistic insights into
            specificity requirements.
  JOURNAL   Biochemistry. 26 (1987) 1301-5.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:2655701]
  AUTHORS   Bode W, Meyer E Jr, Powers JC.
  TITLE     Human leukocyte and porcine pancreatic elastase: X-ray crystal
            structures, mechanism, substrate specificity, and mechanism-based
            inhibitors.
  JOURNAL   Biochemistry. 28 (1989) 1951-63.
  ORGANISM  human [GN:hsa], pig [GN:ssc]
ORTHOLOGY   KO: K01327  leukocyte elastase
GENES       HSA: 1991(ELA2)
            MMU: 50701(Ela2)
            RNO: 299606(Ela2_predicted)
            CFA: 442980(ELA2)
            XTR: 448597(ela2)
STRUCTURES  PDB: 1B0F  1H1B  1HNE  1PPF  1PPG  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.37
            ExPASy - ENZYME nomenclature database: 3.4.21.37
            ExplorEnz - The Enzyme Database: 3.4.21.37
            ERGO genome analysis and discovery system: 3.4.21.37
            BRENDA, the Enzyme Database: 3.4.21.37
            CAS: 9004-06-2
///
ENTRY       EC 3.4.21.38                Enzyme
NAME        coagulation factor XIIa;
            Hageman factor (activated);
            blood-coagulation factor XIIf;
            activated beta blood-coagulation factor XII;
            prealbumin activator;
            Hageman factor beta-fragment;
            Hageman factor fragment HFf;
            blood-coagulation factor XIIabeta;
            prekallikrein activator;
            kallikreinogen activator
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage of Arg!Ile bonds in factor VII to form factor
            VIIa and factor XI to form factor XIa
COMMENT     Also activates plasminogen and plasma prokallikrein. Formed from the
            proenzyme, factor XII, by plasma kallikrein or factor XIIa. In
            peptidase family S1 (trypsin family)
REFERENCE   1  [PMID:6918768]
  AUTHORS   Fujikawa K, Davie EW.
  TITLE     Human factor XII (Hageman factor).
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 198-211.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:6370301]
  AUTHORS   Cho K, Tanaka T, Cook RR, Kisiel W, Fujikawa K, Kurachi K, Powers
            JC.
  TITLE     Active-site mapping of bovine and human blood coagulation serine
            proteases using synthetic peptide 4-nitroanilide and thio ester
            substrates.
  JOURNAL   Biochemistry. 23 (1984) 644-50.
  ORGANISM  human [GN:hsa], cow [GN:bta]
REFERENCE   3  [PMID:3011063]
  AUTHORS   Que BG, Davie EW.
  TITLE     Characterization of a cDNA coding for human factor XII (Hageman
            factor).
  JOURNAL   Biochemistry. 25 (1986) 1525-8.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:3237089]
  AUTHORS   Fujikawa K.
  TITLE     Bovine Hageman factor and its fragments.
  JOURNAL   Methods. Enzymol. 163 (1988) 54-68.
  ORGANISM  cow [GN:bta]
REFERENCE   5  [PMID:3237092]
  AUTHORS   Silverberg M, Kaplan AP.
  TITLE     Human Hageman factor and its fragments.
  JOURNAL   Methods. Enzymol. 163 (1988) 68-80.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01328  coagulation factor XII (Hageman factor)
GENES       HSA: 2161(F12)
            PTR: 462304(F12)
            MMU: 58992(F12)
            RNO: 306761(F12)
            CFA: 489090(F12)
            BTA: 280789(F12)
            SSC: 397474(F12)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.38
            ExPASy - ENZYME nomenclature database: 3.4.21.38
            ExplorEnz - The Enzyme Database: 3.4.21.38
            ERGO genome analysis and discovery system: 3.4.21.38
            BRENDA, the Enzyme Database: 3.4.21.38
            CAS: 75216-42-1
///
ENTRY       EC 3.4.21.39                Enzyme
NAME        chymase;
            mast cell protease I;
            skeletal muscle protease;
            skin chymotryptic proteinase;
            mast cell serine proteinase, chymase;
            skeletal muscle (SK) protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage: Phe! > Tyr! > Trp! > Leu!
COMMENT     In mast cell granules. In peptidase family S1 (trypsin family)
REFERENCE   1  [PMID:7043202]
  AUTHORS   Woodbury RG, Everitt MT, Neurath H.
  TITLE     Mast cell proteases.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 588-609.
REFERENCE   2  [PMID:3893542]
  AUTHORS   Powers JC, Tanaka T, Harper JW, Minematsu Y, Barker L, Lincoln D,
            Crumley KV, Fraki JE, Schechter NM, Lazarus GG, et al.
  TITLE     Mammalian chymotrypsin-like enzymes. Comparative reactivities of rat
            mast cell proteases, human and dog skin chymases, and human
            cathepsin G with peptide 4-nitroanilide substrates and with peptide
            chloromethyl ketone and sulfonyl fluoride inhibitors.
  JOURNAL   Biochemistry. 24 (1985) 2048-58.
  ORGANISM  rat [GN:rno], human [GN:hsa], dog [GN:cfa]
REFERENCE   3  [PMID:2425663]
  AUTHORS   Johnson LA, Moon KE, Eisenberg M.
  TITLE     Purification to homogeneity of the human skin chymotryptic
            proteinase &quot;chymase&quot;.
  JOURNAL   Anal. Biochem. 155 (1986) 358-64.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04614  Renin-angiotensin system
ORTHOLOGY   KO: K01329  chymase
GENES       HSA: 1215(CMA1)
            MMU: 17228(Cma1)
            RNO: 25627(Cma1)
            CFA: 490628(CMA1)
STRUCTURES  PDB: 1KLT  1NN6  1PJP  1T31  2HVX  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.39
            ExPASy - ENZYME nomenclature database: 3.4.21.39
            ExplorEnz - The Enzyme Database: 3.4.21.39
            ERGO genome analysis and discovery system: 3.4.21.39
            BRENDA, the Enzyme Database: 3.4.21.39
            CAS: 97501-92-3
///
ENTRY       EC 3.4.21.40      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Deleted entry: submandibular proteinase A (EC 3.4.21.40 created
            1981, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.40
            ExPASy - ENZYME nomenclature database: 3.4.21.40
            ExplorEnz - The Enzyme Database: 3.4.21.40
            ERGO genome analysis and discovery system: 3.4.21.40
            BRENDA, the Enzyme Database: 3.4.21.40
///
ENTRY       EC 3.4.21.41                Enzyme
NAME        complement subcomponent C_overbar_1r_;
            activated complement C1r;
            C_overbar_1r_ esterase;
            activated complement C1r
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage of Lys(or Arg)!Ile bond in complement
            subcomponent C1s to form C_overbar_1s_
            (internal_xref(ec_num(3,4,21,42)))
COMMENT     Activated from proenzyme C_overbar_1r_ in plasma during activation
            of the complement system by the "classical" route. In peptidase
            family S1 (trypsin family)
REFERENCE   1  [PMID:6281620]
  AUTHORS   Sim RB.
  TITLE     The human complement system serine proteases C1r and C1s and their
            proenzymes.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 26-42.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:3021205]
  AUTHORS   Leytus SP, Kurachi K, Sakariassen KS, Davie EW.
  TITLE     Nucleotide sequence of the cDNA coding for human complement C1r.
  JOURNAL   Biochemistry. 25 (1986) 4855-63.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:3052276]
  AUTHORS   Muller-Eberhard HJ.
  TITLE     Molecular organization and function of the complement system.
  JOURNAL   Annu. Rev. Biochem. 57 (1988) 321-47.
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01330  complement component 1, r subcomponent
GENES       HSA: 715(C1R)
            PTR: 466939(C1R)
            MMU: 50909(C1r)
            RNO: 312705(C1r)
            CFA: 477707(C1R)
            BTA: 511581(C1R)
            GGA: 418295(C1R)
STRUCTURES  PDB: 1APQ  1MD7  1MD8  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.41
            ExPASy - ENZYME nomenclature database: 3.4.21.41
            ExplorEnz - The Enzyme Database: 3.4.21.41
            ERGO genome analysis and discovery system: 3.4.21.41
            BRENDA, the Enzyme Database: 3.4.21.41
            CAS: 80295-69-8
///
ENTRY       EC 3.4.21.42                Enzyme
NAME        complement subcomponent C_overbar_1s_;
            C1 esterase;
            activated complement C1s;
            complement C_overbar_1r_
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Cleavage of Arg!Ala bond in complement component C4 to form C4a and
            C4b, and Lys(or Arg)!Lys bond in complement component C2 to form C2a
            and C2b: the "classical" pathway C3 convertase
COMMENT     Activated from proenzyme C1s in plasma by complement subcomponent
            C_overbar_1r_ . In peptidase family S1 (trypsin family)
REFERENCE   1  [PMID:6281620]
  AUTHORS   Sim RB.
  TITLE     The human complement system serine proteases C1r and C1s and their
            proenzymes.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 26-42.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:3500856]
  AUTHORS   Mackinnon CM, Carter PE, Smyth SJ, Dunbar B, Fothergill JE.
  TITLE     Molecular cloning of cDNA for human complement component C1s. The
            complete amino acid sequence.
  JOURNAL   Eur. J. Biochem. 169 (1987) 547-53.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:3052276]
  AUTHORS   Muller-Eberhard HJ.
  TITLE     Molecular organization and function of the complement system.
  JOURNAL   Annu. Rev. Biochem. 57 (1988) 321-47.
REFERENCE   4  [PMID:2500154]
  AUTHORS   Skoog MT, Mehdi S, Wiseman JS, Bey P.
  TITLE     The specificity of two proteinases that cleave adjacent to arginine,
            C1 esterase and acrosin, for peptide p-nitroanilide substrates.
  JOURNAL   Biochim. Biophys. Acta. 996 (1989) 89-94.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01331  complement component 1, s subcomponent
GENES       HSA: 716(C1S)
            PTR: 451808(C1S)
            MMU: 317677(EG317677) 50908(C1s)
            RNO: 192262(C1s)
            CFA: 486714(C1S)
            SSC: 397274(C1S)
            GGA: 418294(RCJMB04_11h6)
STRUCTURES  PDB: 1ELV  1NZI  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.42
            ExPASy - ENZYME nomenclature database: 3.4.21.42
            ExplorEnz - The Enzyme Database: 3.4.21.42
            ERGO genome analysis and discovery system: 3.4.21.42
            BRENDA, the Enzyme Database: 3.4.21.42
            CAS: 80295-70-1
///
ENTRY       EC 3.4.21.43                Enzyme
NAME        classical-complement-pathway C3/C5 convertase;
            C3 convertase;
            C_overbar_42_;
            C4b,2a;
            C5 convertase;
            C_overbar_423_;
            C4b,2a,3b;
            C42;
            C5 convertase;
            C423;
            C4b,2a,3b;
            complement C.hivin.4.hivin2;
            complement C3 convertase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage of Arg!Ser bond in complement component C3
            alpha-chain to form C3a and C3b, and Arg! bond in complement
            component C5 alpha-chain to form C5a and C5b
COMMENT     A complex of complement fragments C4b, C2a and C2b. C2a contains the
            active site, C2b the site for C4b binding. C2a and C2b are formed by
            cleavage of proenzyme C2 by complement subcomponent C_overbar_1s_.
            Cleavage of C5 requires complement fragment C3b which binds C5 and
            renders it susceptible to cleavage by the C4b,2a complex. Includes
            former EC 3.4.21.44. Complement component C2a is in peptidase family
            S1 (trypsin family)
REFERENCE   1  [PMID:7043188]
  AUTHORS   Kerr MA.
  TITLE     Human factor B.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 102-12.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:3052276]
  AUTHORS   Muller-Eberhard HJ.
  TITLE     Molecular organization and function of the complement system.
  JOURNAL   Annu. Rev. Biochem. 57 (1988) 321-47.
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01332  complement component 2
GENES       HSA: 717(C2)
            MMU: 12263(C2)
            RNO: 24231(C2)
            BTA: 515440(C2)
            PLA: Plav_0014
STRUCTURES  PDB: 1HZF  2I6Q  2I6S  2ODP  2ODQ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.43
            ExPASy - ENZYME nomenclature database: 3.4.21.43
            ExplorEnz - The Enzyme Database: 3.4.21.43
            ERGO genome analysis and discovery system: 3.4.21.43
            BRENDA, the Enzyme Database: 3.4.21.43
            CAS: 56626-15-4
///
ENTRY       EC 3.4.21.44      Obsolete  Enzyme
NAME        Transferred to 3.4.21.43
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Transferred entry: now EC 3.4.21.43 classical-complement-pathway
            C3/C5 convertase (EC 3.4.21.44 created 1981, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.44
            ExPASy - ENZYME nomenclature database: 3.4.21.44
            ExplorEnz - The Enzyme Database: 3.4.21.44
            ERGO genome analysis and discovery system: 3.4.21.44
            BRENDA, the Enzyme Database: 3.4.21.44
///
ENTRY       EC 3.4.21.45                Enzyme
NAME        complement factor I;
            complement component C3b inactivator;
            C3b inactivator;
            C3b/C4b inactivator;
            C3bINA;
            complement C3b/C4b inactivator;
            complement C4b inactivator;
            conglutinogen-activating factor C;
            complement C3b inactivator;
            factor I;
            complement C4bi
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Inactivates complement subcomponents C3b, iC3b and C4b by
            proteolytic cleavage
COFACTOR    Factor H [CPD:C01491];
            C4b-binding protein [CPD:C02815];
            Complement receptor CR1 [CPD:C03382]
COMMENT     Cleavage of complement subcomponent C3b requires its binding to
            cofactor factor H or complement receptor CR1; cleavage of iC3b
            requires complement receptor CR1; cleavage of C4b requires
            C4b-binding protein. In peptidase family S1 (trypsin family)
REFERENCE   1  [PMID:7391570]
  AUTHORS   Nagasawa S, Ichihara C, Stroud RM.
  TITLE     Cleavage of C4b by C3b inactivator: production of a nicked form of
            C4b, C4b', as an intermediate cleavage product of C4b by C3b
            inactivator.
  JOURNAL   J. Immunol. 125 (1980) 578-82.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:6210825]
  AUTHORS   Crossley LG.
  TITLE     C3b inactivator and beta 1H.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 112-24.
REFERENCE   3  [PMID:3052276]
  AUTHORS   Muller-Eberhard HJ.
  TITLE     Molecular organization and function of the complement system.
  JOURNAL   Annu. Rev. Biochem. 57 (1988) 321-47.
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01333  complement factor I
GENES       HSA: 3426(CFI)
            PTR: 471271(CFI)
            MMU: 12630(Cfi)
            RNO: 79126(Cfi)
            CFA: 478515(CFI)
            BTA: 513197(MGC128240)
            GGA: 428773(CFI)
            XLA: 379108(MGC53615)
            XTR: 613100(mgc107998)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.45
            ExPASy - ENZYME nomenclature database: 3.4.21.45
            ExplorEnz - The Enzyme Database: 3.4.21.45
            ERGO genome analysis and discovery system: 3.4.21.45
            BRENDA, the Enzyme Database: 3.4.21.45
            CAS: 80295-66-5
///
ENTRY       EC 3.4.21.46                Enzyme
NAME        complement factor D;
            C3 proactivator convertase;
            properdin factor D esterase;
            factor D;
            factor D (complement)
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage of Arg!Lys bond in complement factor B when in
            complex with complement subcomponent C3b or with cobra venom factor
COMMENT     A component of the alternative pathway of complement activation.
            This reaction is analogous to the activation of complement component
            C2 by complement subcomponent C_overbar_1s_. In peptidase family S1
            (trypsin family)
REFERENCE   1  [PMID:6918766]
  AUTHORS   Reid KB, Johnson DM, Gagnon J, Phohaska R.
  TITLE     Preparation of human factor D of the alternative pathway of
            complement.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 134-43.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:3052276]
  AUTHORS   Muller-Eberhard HJ.
  TITLE     Molecular organization and function of the complement system.
  JOURNAL   Annu. Rev. Biochem. 57 (1988) 321-47.
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01334  component factor D
GENES       HSA: 1675(CFD)
            PTR: 455533(CFD)
            MMU: 11537(Cfd)
            RNO: 54249(Cfd)
            CFA: 485095(CFD)
            BTA: 505647(DF)
            XLA: 494791(ami)
            XTR: 394945(df)
            DRE: 553553(zgc:109940)
STRUCTURES  PDB: 1BIO  1DFP  1DIC  1DST  1DSU  1FDP  1HFD  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.46
            ExPASy - ENZYME nomenclature database: 3.4.21.46
            ExplorEnz - The Enzyme Database: 3.4.21.46
            ERGO genome analysis and discovery system: 3.4.21.46
            BRENDA, the Enzyme Database: 3.4.21.46
            CAS: 37213-56-2
///
ENTRY       EC 3.4.21.47                Enzyme
NAME        alternative-complement-pathway C3/C5 convertase;
            complement component C3/C5 convertase (alternative);
            proenzyme factor B;
            properdin factor B;
            C3 proactivator;
            glycine-rich beta-glycoprotein;
            heat-labile factor;
            C3 convertase;
            C3b,Bb,CVF,Bb,C5 convertase;
            (C3b)n,Bb;
            complement C 3(C 5) convertase (amplification);
            alternative complement pathway C3(C5) convertase;
            C5 convertase;
            CVF,Bb;
            (CVF)-dependent glycine-rich-beta-glucoprotein;
            cobra venom factor-dependent C3 convertase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Cleavage of Arg!Ser bond in complement component C3 alpha-chain to
            yield C3a and C3b, and Arg! bond in complement component C5
            alpha-chain to yield C5a and C5b
COMMENT     A bimolecular complex of complement fragment Bb with either C3b or
            cobra venom factor; Bb contains the active site. Bb is formed by
            cleavage of proenzyme factor B by factor D. Cleavage of complement
            component C5 requires additional C3b which binds C5 and renders it
            susceptible to cleavage by C3b,Bb complex. C3b,Bb is stabilized in
            plasma by factor P. Complement factor B is in peptidase family S1
            (trypsin family)
REFERENCE   1  [PMID:7043188]
  AUTHORS   Kerr MA.
  TITLE     Human factor B.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 102-12.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:6323161]
  AUTHORS   Morley BJ, Campbell RD.
  TITLE     Internal homologies of the Ba fragment from human complement
            component Factor B, a class III MHC antigen.
  JOURNAL   EMBO. J. 3 (1984) 153-7.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:3052276]
  AUTHORS   Muller-Eberhard HJ.
  TITLE     Molecular organization and function of the complement system.
  JOURNAL   Annu. Rev. Biochem. 57 (1988) 321-47.
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01335  component factor B
GENES       HSA: 629(CFB)
            PTR: 494140(CFB)
            MMU: 14962(Cfb)
            RNO: 294257(Cfb)
            CFA: 474853(CFB)
            BTA: 514076(MGC137125)
            DRE: 30604(cfb)
            SPU: 373308(Bf)
STRUCTURES  PDB: 1Q0P  1RRK  1RS0  1RTK  2OK5  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.47
            ExPASy - ENZYME nomenclature database: 3.4.21.47
            ExplorEnz - The Enzyme Database: 3.4.21.47
            ERGO genome analysis and discovery system: 3.4.21.47
            BRENDA, the Enzyme Database: 3.4.21.47
            CAS: 80295-67-6
///
ENTRY       EC 3.4.21.48                Enzyme
NAME        cerevisin;
            yeast proteinase B;
            proteinase yscB;
            baker's yeast proteinase B;
            brewer's yeast proteinase;
            peptidase beta
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt >
            Ac-Tyr-OEt. Does not hydrolyze peptide amides
INHIBITOR   Isoflurophate [CPD:C00202];
            Hg [CPD:C01319];
            p-Chloromercuribenzoate [CPD:C03444]
COMMENT     From Saccharomyces cerevisiae (baker's yeast, brewer's yeast). In
            peptidase family S8 (subtilisin family), but contains a Cys residue
            near the active site His, and is inhibited by mercurials. Proteinase
            ycaB is a similar enzyme from the yeast Candida albicans [3]
REFERENCE   1  [PMID:4961236]
  AUTHORS   Felix F, Brouillet N.
  TITLE     [Purification and properties of 2 peptidases from baker's yeast]
  JOURNAL   Biochim. Biophys. Acta. 122 (1966) 127-44.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:7028121]
  AUTHORS   Kominami E, Hoffschulte H, Leuschel L, Maier K, Holzer H.
  TITLE     The substrate specificity of proteinase B from baker's yeast.
  JOURNAL   Biochim. Biophys. Acta. 661 (1981) 136-41.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:3539100]
  AUTHORS   Farley PC, Shepherd MG, Sullivan PA.
  TITLE     The purification and properties of yeast proteinase B from Candida
            albicans.
  JOURNAL   Biochem. J. 236 (1986) 177-84.
  ORGANISM  Candida albicans [GN:cal]
REFERENCE   4  [PMID:3325823]
  AUTHORS   Moehle CM, Tizard R, Lemmon SK, Smart J, Jones EW.
  TITLE     Protease B of the lysosomelike vacuole of the yeast Saccharomyces
            cerevisiae is homologous to the subtilisin family of serine
            proteases.
  JOURNAL   Mol. Cell. Biol. 7 (1987) 4390-9.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K01336  cerevisin
GENES       SCE: YEL060C(PRB1)
            AGO: AGOS_ACR012C
            PIC: PICST_78783(PRB2)
            CAL: CaO19.2242
            CGR: CAGL0B03619g
            AFM: AFUA_5G09210
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.48
            ExPASy - ENZYME nomenclature database: 3.4.21.48
            ExplorEnz - The Enzyme Database: 3.4.21.48
            ERGO genome analysis and discovery system: 3.4.21.48
            BRENDA, the Enzyme Database: 3.4.21.48
            CAS: 37288-81-6
///
ENTRY       EC 3.4.21.49                Enzyme
NAME        hypodermin C;
            Hypoderma collagenase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins including native collagen at !Ala bond
            leaving an N-terminal (75%) and a C-terminal (25%) fragment
COMMENT     From the larva of a warble fly, Hypoderma lineatum. Little action on
            small molecule substrates of trypsin, chymotrypsin, elastase or
            microbial collagenases. In peptidase family S1 (trypsin family)
REFERENCE   1  [PMID:230030]
  AUTHORS   Lecroisey A, Boulard C, Keil B.
  TITLE     Chemical and enzymatic characterization of the collagenase from the
            insect Hypoderma lineatum.
  JOURNAL   Eur. J. Biochem. 101 (1979) 385-93.
  ORGANISM  Hypoderma lineatum
REFERENCE   2  [PMID:2995028]
  AUTHORS   Lecroisey A, Keil B.
  TITLE     Specificity of the collagenase from the insect Hypoderma lineatum.
  JOURNAL   Eur. J. Biochem. 152 (1985) 123-30.
  ORGANISM  Hypoderma lineatum
REFERENCE   3  [PMID:3034899]
  AUTHORS   Lecroisey A, Gilles AM, De Wolf A, Keil B.
  TITLE     Complete amino acid sequence of the collagenase from the insect
            Hypoderma lineatum.
  JOURNAL   J. Biol. Chem. 262 (1987) 7546-51.
  ORGANISM  Hypoderma lineatum
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.49
            ExPASy - ENZYME nomenclature database: 3.4.21.49
            ExplorEnz - The Enzyme Database: 3.4.21.49
            ERGO genome analysis and discovery system: 3.4.21.49
            BRENDA, the Enzyme Database: 3.4.21.49
            CAS: 122191-36-0
///
ENTRY       EC 3.4.21.50                Enzyme
NAME        lysyl endopeptidase;
            Achromobacter proteinase I (also see Comment);
            Achromobacter lyticus alkaline proteinase I;
            protease I;
            achromopeptidase;
            lysyl bond specific proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage: Lys!, including -Lys!Pro-
COMMENT     From Achromobacter lyticus [6]. Enzymes with similar specificity are
            produced by Lysobacter enzymogenes (Endoproteinase Lys-C; [3]) and
            Pseudomonas aeruginosa (Ps-1; [4]). In peptidase family S1 (trypsin
            family)
REFERENCE   1  [PMID:6791693]
  AUTHORS   Masaki T, Tanabe M, Nakamura K, Soejima M.
  TITLE     Studies on a new proteolytic enzyme from A chromobacter lyticus
            M497-1. I. Purification and some enzymatic properties.
  JOURNAL   Biochim. Biophys. Acta. 660 (1981) 44-50.
  ORGANISM  Achromobacter lyticus
REFERENCE   2  [PMID:6168293]
  AUTHORS   Masaki T, Fujihashi T, Nakamura K, Soejima M.
  TITLE     Studies on a new proteolytic enzyme from Achromobacter lyticus
            M497-1. II. specificity and inhibition studies of Achromobacter
            protease I.
  JOURNAL   Biochim. Biophys. Acta. 660 (1981) 51-5.
  ORGANISM  Achromobacter lyticus
REFERENCE   3  [PMID:6359954]
  AUTHORS   Jekel PA, Weijer WJ, Beintema JJ.
  TITLE     Use of endoproteinase Lys-C from Lysobacter enzymogenes in protein
            sequence analysis.
  JOURNAL   Anal. Biochem. 134 (1983) 347-54.
  ORGANISM  Lysobacter enzymogenes
REFERENCE   4  [PMID:3090046]
  AUTHORS   Elliott BW Jr, Cohen C.
  TITLE     Isolation and characterization of a lysine-specific protease from
            Pseudomonas aeruginosa.
  JOURNAL   J. Biol. Chem. 261 (1986) 11259-65.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   5
  AUTHORS   Ohara, T., Makino, K., Shinagawa, H., Nakata, A., Norioka, S. and
            Sakiyama, F.
  TITLE     Cloning, nucleotide sequence, and expression of Achromobacter
            protease I gene.
  JOURNAL   J. Biol. Chem. 264 (1989) 20625-2063.
  ORGANISM  Achromobacter lyticus
REFERENCE   6  [PMID:2492988]
  AUTHORS   Tsunasawa S, Masaki T, Hirose M, Soejima M, Sakiyama F.
  TITLE     The primary structure and structural characteristics of
            Achromobacter lyticus protease I, a lysine-specific serine protease.
  JOURNAL   J. Biol. Chem. 264 (1989) 3832-9.
  ORGANISM  Achromobacter lyticus
ORTHOLOGY   KO: K01337  lysyl endopeptidase
GENES       PAP: PSPA7_0919
            SRU: SRU_1622
STRUCTURES  PDB: 1ARB  1ARC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.50
            ExPASy - ENZYME nomenclature database: 3.4.21.50
            ExplorEnz - The Enzyme Database: 3.4.21.50
            ERGO genome analysis and discovery system: 3.4.21.50
            BRENDA, the Enzyme Database: 3.4.21.50
            CAS: 123175-82-6
///
ENTRY       EC 3.4.21.51      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Deleted entry: Leukocyte-membrane neutral endopeptidase (EC
            3.4.21.51 created 1984, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.51
            ExPASy - ENZYME nomenclature database: 3.4.21.51
            ExplorEnz - The Enzyme Database: 3.4.21.51
            ERGO genome analysis and discovery system: 3.4.21.51
            BRENDA, the Enzyme Database: 3.4.21.51
///
ENTRY       EC 3.4.21.52      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Deleted entry: Cathepsin R (EC 3.4.21.52 created 1981 as EC
            3.4.99.33, transferred 1984 to EC 3.4.21.52, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.52
            ExPASy - ENZYME nomenclature database: 3.4.21.52
            ExplorEnz - The Enzyme Database: 3.4.21.52
            ERGO genome analysis and discovery system: 3.4.21.52
            BRENDA, the Enzyme Database: 3.4.21.52
///
ENTRY       EC 3.4.21.53                Enzyme
NAME        endopeptidase La;
            ATP-dependent serine proteinase;
            lon proteinase;
            protease La;
            proteinase La;
            ATP-dependent lon proteinase;
            ATP-dependent protease La;
            Escherichia coli proteinase La;
            Escherichia coli serine proteinase La;
            gene lon protease;
            gene lon proteins;
            PIM1 protease;
            PIM1 proteinase;
            serine protease La
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins in presence of ATP
INHIBITOR   Vanadate [CPD:C00754]
COMMENT     Product of the lon gene in Escherichia coli. ATP hydrolysis is
            linked with peptide bond hydrolysis; vanadate inhibits both
            reactions. Type example of peptidase family S16. A similar enzyme
            occurs in animal mitochondria
REFERENCE   1  [PMID:6749845]
  AUTHORS   Desautels M, Goldberg AL.
  TITLE     Demonstration of an ATP-dependent, vanadate-sensitive endoprotease
            in the matrix of rat liver mitochondria.
  JOURNAL   J. Biol. Chem. 257 (1982) 11673-9.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:7040380]
  AUTHORS   Larimore FS, Waxman L, Goldberg AL.
  TITLE     Studies of the ATP-dependent proteolytic enzyme, protease La, from
            Escherichia coli.
  JOURNAL   J. Biol. Chem. 257 (1982) 4187-95.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:3042779]
  AUTHORS   Chin DT, Goff SA, Webster T, Smith T, Goldberg AL.
  TITLE     Sequence of the lon gene in Escherichia coli. A heat-shock gene
            which encodes the ATP-dependent protease La.
  JOURNAL   J. Biol. Chem. 263 (1988) 11718-28.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01338  ATP-dependent Lon protease
GENES       HSA: 83752(LONP2)
            PTR: 465152(LONP2)
            MMU: 66887(Lonp2)
            RNO: 291922(RGD1305466)
            CFA: 478137(LONP2)
            BTA: 541085(MGC128838)
            GGA: 415740(LONP2)
            DRE: 494030(lonp2)
            ATH: AT5G47040
            OSA: 4347683
            ANI: AN0122.2
            AFM: AFUA_5G11750
            AOR: AO090120000293
            CNE: CND03860
            DDI: DDBDRAFT_0204395
            TET: TTHERM_00101500 TTHERM_00649120
            ECO: b0439(lon)
            ECJ: JW0429(lon)
            ECE: Z0545(lon)
            ECS: ECs0493
            ECC: c0555(lon)
            ECI: UTI89_C0467(lon)
            ECP: ECP_0500
            ECV: APECO1_1572(lon)
            ECW: EcE24377A_0475(lon)
            ECX: EcHS_A0516(lon)
            STY: STY0492(lon)
            STT: t2410(lon)
            SPT: SPA2272(lon)
            SEC: SC0492(lon)
            STM: STM0450(lon) STM4491
            YPE: YPO3155(lon)
            YPK: y1029(lon)
            YPM: YP_0776(lon)
            YPA: YPA_2650
            YPN: YPN_0935
            YPP: YPDSF_2791
            YPS: YPTB0961(lon)
            YPI: YpsIP31758_3090(lon)
            SFL: SF0384(lon)
            SFX: S0390(lon)
            SFV: SFV_0413(lon)
            SSN: SSON_0422(lon)
            SBO: SBO_0333(lon)
            SDY: SDY_0293(lon)
            ECA: ECA1150(lon)
            PLU: plu3867(lon)
            BUC: BU477(lon)
            BAS: BUsg461(lon)
            BAB: bbp421(lon)
            BCC: BCc_295(lon)
            WBR: WGLp153(lon)
            SGL: SG0673
            ENT: Ent638_0906
            KPN: KPN_00401(lon)
            SPE: Spro_1097
            BFL: Bfl299(lon)
            BPN: BPEN_307(lon)
            HIT: NTHI0593(lon)
            HDU: HD1149(lon)
            HSO: HS_0489(lon) HS_0858
            PMU: PM1978(lon)
            MSU: MS1844(lon)
            APL: APL_0376(lon)
            ASU: Asuc_0768
            XFA: XF1189
            XFT: PD0474(lon)
            XCC: XCC0977(lon)
            XCB: XC_3263
            XCV: XCV1083(lon)
            XAC: XAC1080(lon)
            XOO: XOO1035(lon)
            XOM: XOO_0934(XOO0934)
            VCH: VC1920
            VCO: VC0395_A1510(lon)
            VVU: VV1_0020 VV1_0021
            VVY: VV1106
            VPA: VP0919
            VFI: VF0798 VF1293
            PPR: PBPRA2635
            PAE: PA0779 PA1803(lon)
            PAU: PA14_41220(lon)
            PAP: PSPA7_3494(lon2) PSPA7_4740(lon1)
            PPU: PP_2302(lon-2)
            PPF: Pput_3467 Pput_4278
            PST: PSPTO_3724(lon-1)
            PSB: Psyr_1749 Psyr_3944
            PSP: PSPPH_1700(lon1) PSPPH_3941(lon2)
            PFL: PFL_3985(lon) PFL_4923(lon)
            PFO: Pfl_3695 Pfl_4579
            PEN: PSEEN1870(lon)
            PMY: Pmen_1223 Pmen_2052
            PAR: Psyc_1659(lon)
            PCR: Pcryo_1899
            PRW: PsycPRwf_1979
            ACI: ACIAD1115(lon)
            SON: SO_1796(lon)
            SDN: Sden_2493
            SFR: Sfri_2594
            SAZ: Sama_1226
            SBL: Sbal_1606
            SBM: Shew185_1595
            SLO: Shew_2506
            SPC: Sputcn32_1492
            SSE: Ssed_1543
            SPL: Spea_2679
            SHE: Shewmr4_2493
            SHM: Shewmr7_2561
            SHN: Shewana3_2659
            SHW: Sputw3181_2609
            ILO: IL1003(lon)
            CPS: CPS_3783(lon)
            PHA: PSHAa2060(lon)
            PAT: Patl_3134
            SDE: Sde_1610 Sde_2752
            PIN: Ping_1467
            MAQ: Maqu_1838 Maqu_3332
            CBU: CBU_0740(lon)
            CBD: COXBU7E912_0754(lon)
            LPN: lpg1859(lon)
            LPF: lpl1823(lon)
            LPP: lpp1827(lon)
            MCA: MCA0531(lon)
            FTU: FTT0626(lon)
            FTF: FTF0626(lon)
            FTW: FTW_1103(lon)
            FTL: FTL_0894
            FTH: FTH_0879(lon)
            FTA: FTA_0945(lon)
            FTN: FTN_1055(lon)
            TCX: Tcr_1179 Tcr_1548
            NOC: Noc_1387 Noc_1674
            AEH: Mlg_2286
            HHA: Hhal_0601
            HCH: HCH_01256(lon1) HCH_02162(lon2)
            CSA: Csal_2044 Csal_2665
            ABO: ABO_1195(lon-1) ABO_1212
            MMW: Mmwyl1_1725 Mmwyl1_3488
            AHA: AHA_2013(lon)
            DNO: DNO_0227(lon)
            BCI: BCI_0263(lon)
            RMA: Rmag_0208
            VOK: COSY_0205(lon)
            NME: NMB1231
            NMA: NMA1398(lon)
            NMC: NMC1131(lon)
            NGO: NGO0775(lon)
            CVI: CV_2555(lon)
            RSO: RSc1713(lon)
            REU: Reut_A1382
            REH: H16_A1485(lon)
            RME: Rmet_1883
            BMA: BMA1463(lon)
            BMV: BMASAVP1_A1955(lon)
            BML: BMA10299_A3350(lon)
            BMN: BMA10247_1230(lon)
            BXE: Bxe_A2293 Bxe_A4335
            BVI: Bcep1808_1853
            BUR: Bcep18194_A5222 Bcep18194_A6396
            BCN: Bcen_6158
            BCH: Bcen2424_1921
            BAM: Bamb_1909 Bamb_3094
            BPS: BPSL1405(lon)
            BPM: BURPS1710b_0433(lon1) BURPS1710b_2479(lon)
            BPL: BURPS1106A_2363(lon)
            BPD: BURPS668_2321(lon)
            BTE: BTH_I0216 BTH_I2122(lon)
            PNU: Pnuc_0936
            BPE: BP1777(lon)
            BPA: BPP1033(lon) BPP2008(lon)
            BBR: BB1248(lon) BB2256(lon)
            RFR: Rfer_1556 Rfer_3006
            POL: Bpro_0925 Bpro_2032 Bpro_5032
            PNA: Pnap_0819 Pnap_2955
            AAV: Aave_1457
            AJS: Ajs_1211
            VEI: Veis_4373
            MPT: Mpe_A1294
            HAR: HEAR1750(lon)
            MMS: mma_1533(lon)
            NEU: NE0033(lon) NE1278(lonA)
            NET: Neut_0201 Neut_0970
            NMU: Nmul_A2097 Nmul_A2338
            EBA: ebA4973(lon) ebA5250
            AZO: azo2069 azo3813
            DAR: Daro_1716
            TBD: Tbd_1252 Tbd_1675
            MFA: Mfla_1411
            HPY: HP1379(lon)
            HPA: HPAG1_1325
            HHE: HH0845(lon)
            HAC: Hac_0059(lon)
            WSU: WS1972
            TDN: Tmden_0414
            CJE: Cj1073c(lon)
            CJR: CJE1216(lon)
            CJJ: CJJ81176_1091(lon)
            CJU: C8J_1014(lon)
            CJD: JJD26997_0650(lon)
            CFF: CFF8240_1060(lon)
            CCV: CCV52592_1589(lon)
            CHA: CHAB381_0549(lon)
            CCO: CCC13826_1730 CCC13826_1958(lon)
            ABU: Abu_0592(lon)
            NIS: NIS_1348(lon)
            SUN: SUN_1906(lon)
            GSU: GSU0923(loN-1) GSU1790(loN-2) GSU2105 GSU3193(loN-3)
            GME: Gmet_1871 Gmet_2544 Gmet_3214
            GUR: Gura_0691 Gura_1246 Gura_1917
            PCA: Pcar_0027 Pcar_0591 Pcar_1687 Pcar_1982
            PPD: Ppro_2604 Ppro_3207
            DVU: DVU1191 DVU1337(lon)
            DVL: Dvul_0092 Dvul_1732 Dvul_1866
            DDE: Dde_2218 Dde_2444
            LIP: LI0148(lon) LI0796(lon)
            BBA: Bd2144(lon) Bd2218(lon) Bd3749(lon) Bd3876(lon)
            DPS: DP0130 DP2536 DP2921 DP2922
            ADE: Adeh_1707 Adeh_3231 Adeh_3350
            AFW: Anae109_2098 Anae109_3418
            MXA: MXAN_2017(lon) MXAN_3993(lon)
            SAT: SYN_00783 SYN_01156 SYN_02756 SYN_02787
            SFU: Sfum_0098 Sfum_0715
            RPR: RP450
            RTY: RT0437(lon)
            RCO: RC0629(lon)
            RFE: RF_0692(lon)
            RBE: RBE_0797(lon1)
            OTS: OTBS_0855(lon)
            WOL: WD0317(lon)
            WBM: Wbm0551
            AMA: AM311(lon)
            APH: APH_0968(lon)
            ERU: Erum2020(lon)
            ERW: ERWE_CDS_02040(lon)
            ERG: ERGA_CDS_01990(lon)
            ECN: Ecaj_0204
            ECH: ECH_0899(lon)
            NSE: NSE_0347(lon)
            PUB: SAR11_0882(lon)
            MLO: mlr8476
            MES: Meso_1171
            PLA: Plav_3230
            SME: SMc01905(lon)
            SMD: Smed_0874
            ATU: Atu1261(lon)
            ATC: AGR_C_2329
            RET: RHE_CH01589(lon)
            RLE: RL1690(lon)
            BME: BMEI0876 BMEII0402
            BMF: BAB1_1130
            BMS: BR1106(lon)
            BMB: BruAb1_1112(lon)
            BOV: BOV_1065(lon)
            OAN: Oant_2204
            BJA: bll4942(lon) blr6174(lon)
            BRA: BRADO3111 BRADO4196(lon)
            BBT: BBta_3560 BBta_4570(lon) BBta_7794(lon)
            RPA: RPA2959(lon)
            RPB: RPB_2565
            RPC: RPC_2394
            RPD: RPD_2892
            RPE: RPE_2512
            NWI: Nwi_0074 Nwi_1897
            NHA: Nham_2227
            BHE: BH05900(lon1)
            BQU: BQ05060(lon1)
            BBK: BARBAKC583_0548(lon)
            XAU: Xaut_3593
            CCR: CC_1960
            SIL: SPO2613(lon)
            SIT: TM1040_0775
            RSP: RSP_2806(lon)
            RSH: Rsph17029_1493
            RSQ: Rsph17025_1158
            JAN: Jann_2518
            RDE: RD1_0038(lonD) RD1_2950(lon)
            PDE: Pden_3609
            MMR: Mmar10_1340
            HNE: HNE_0977(lon)
            ZMO: ZMO0376(lon)
            NAR: Saro_1361
            SAL: Sala_0798
            SWI: Swit_0390 Swit_1146
            ELI: ELI_03690
            GOX: GOX0085 GOX0763
            GBE: GbCGDNIH1_1305
            ACR: Acry_0919
            RRU: Rru_A1552
            MAG: amb2047 amb2790
            MGM: Mmc1_0534 Mmc1_3640
            ABA: Acid345_1558 Acid345_2051
            SUS: Acid_2027 Acid_7055
            BSU: BG10338(lonA)
            BHA: BH3050(lonA)
            BAN: BA4702(loN)
            BAR: GBAA4702(loN)
            BAA: BA_5141
            BAT: BAS4367
            BCE: BC4477
            BCA: BCE_4561(lon)
            BCZ: BCZK3685(lon) BCZK4214(lonA) BCZK4215(lonB)
            BCY: Bcer98_3184 Bcer98_3185
            BTK: BT9727_4203(lonA) BT9727_4204(lonB)
            BTL: BALH_4063(lonA)
            BLI: BL00621(lonA)
            BLD: BLi02950(lonA)
            BCL: ABC2634(lonA)
            BAY: RBAM_025260(lonA)
            OIH: OB2076
            GKA: GK2650
            SPZ: M5005_Spy_1266
            SPH: MGAS10270_Spy1281
            SPI: MGAS10750_Spy1373
            SPJ: MGAS2096_Spy1285
            SPK: MGAS9429_Spy1260
            SPB: M28_Spy1204
            LSL: LSL_0662(lon)
            STH: STH3316 STH361
            CAC: CAC0456(lonA) CAC2637(lonA) CAC3716(lonB)
            CPE: CPE1390(lonA)
            CPF: CPF_1644(lon)
            CPR: CPR_1382(lon) CPR_2649
            CTC: CTC00113 CTC01644 CTC02372
            CNO: NT01CX_0368 NT01CX_0890
            CTH: Cthe_0082 Cthe_2742
            CDF: CD3301(lon)
            CBO: CBO3228(lonA)
            CBA: CLB_3265(lon)
            CBH: CLC_3139(lon)
            CBF: CLI_3367(lon)
            CBE: Cbei_1254 Cbei_1329 Cbei_1330
            CKL: CKL_1179 CKL_3349(lon)
            AMT: Amet_1072
            CHY: CHY_0040 CHY_0330(lon) CHY_2651
            DSY: DSY0680 DSY3195 DSY5030
            DRM: Dred_2559 Dred_3302
            SWO: Swol_1653 Swol_2488 Swol_2534
            CSC: Csac_1506
            TTE: TTE0627(lon)
            MTA: Moth_0133 Moth_0531 Moth_2236
            MGE: MG_239(lon)
            MPN: MPN332(lon)
            MPU: MYPU_5190(lon)
            MPE: MYPE6910(lon)
            MGA: MGA_1299(lon)
            MMY: MSC_0454(lon)
            MMO: MMOB2680(lonA)
            MHY: mhp541(lon)
            MHJ: MHJ_0525(lon)
            MHP: MHP7448_0524(lon)
            MSY: MS53_0312(lon)
            MCP: MCAP_0516(lon)
            UUR: UU348(lon)
            POY: PAM448(lon)
            AYW: AYWB_333(lon)
            MFL: Mfl404
            MPA: MAP1584c
            MSM: MSMEG_3582(lon)
            MVA: Mvan_3064
            MGI: Mflv_3336
            MMC: Mmcs_2775
            MKM: Mkms_2819
            MJL: Mjls_2802
            NFA: nfa56180
            RHA: RHA1_ro02353
            SCO: SCO5285(lon)
            SMA: SAV2966(lonA)
            NCA: Noca_3988
            FRA: Francci3_1042 Francci3_1047
            FAL: FRAAL1764(lon)
            FNU: FN2014
            RBA: RB3431(lon)
            CTR: CT344(lon)
            CTA: CTA_0373(lon)
            CMU: TC0623
            CPN: CPn0027(lon)
            CPA: CP0749
            CPJ: CPj0027(lon)
            CPT: CpB0031
            CCA: CCA00319(lon)
            CAB: CAB315
            CFE: CF0684(lon)
            PCU: pc0462(lon)
            BBU: BB0253(lon-1) BB0613(lon-2)
            BGA: BG0256(lon-1) BG0629(lon-2)
            BAF: BAPKO_0263(lon-1) BAPKO_0649(lon-2)
            TPA: TP0016 TP0524
            TDE: TDE0670(lon)
            LIL: LA2412 LA3596(lon)
            LIC: LIC10608(lon) LIC11537
            LBJ: LBJ_0462(lon) LBJ_1454
            LBL: LBL_1678 LBL_2617(lon)
            SYN: sll0195
            SYW: SYNW2140
            SYC: syc0658_d(lon)
            SYF: Synpcc7942_0882
            SYD: Syncc9605_0318
            SYE: Syncc9902_2024
            SYG: sync_0379
            CYA: CYA_1906
            CYB: CYB_0494
            TEL: tlr2461
            GVI: glr3968
            ANA: all4335
            AVA: Ava_1285
            PMA: Pro1662
            PMM: PMM1506
            PMT: PMT1784
            PMN: PMN2A_1072
            PMB: A9601_17091
            PMC: P9515_16861
            PMF: P9303_23671
            PMG: P9301_16971
            PME: NATL1_19471
            BTH: BT_0836 BT_0837
            BFR: BF2304
            BFS: BF2393(lon)
            PGI: PG0620(lon)
            CHU: CHU_2992(lon)
            GFO: GFO_1853(lon)
            FJO: Fjoh_2754
            FPS: FP1714(lon)
            RRS: RoseRS_1469 RoseRS_1605 RoseRS_2778 RoseRS_3815
            RCA: Rcas_0994 Rcas_2169 Rcas_2557 Rcas_3439
            DRA: DR_0349 DR_1974
            DGE: Dgeo_0427 Dgeo_2153
            TTH: TTC0418 TTC0746 TTC1975
            TTJ: TTHA0770 TTHA1111
            AAE: aq_242(lon)
            TMA: TM1633
            TPT: Tpet_1158
            TME: Tmel_1493
            FNO: Fnod_0407
            MMP: MMP1186(lon)
            MAC: MA0752 MA1862(lonA) MA2364
            MBA: Mbar_A2576
            MMA: MM_0164 MM_1913 MM_3118
            MHU: Mhun_1077 Mhun_1532 Mhun_1906
            MEM: Memar_0097
            MBN: Mboo_0143 Mboo_2391
            MTH: MTH892
            MST: Msp_1328(lon)
            HMA: rrnAC1914(lon)
            TAC: Ta0098
            TVO: TVN0155
            PTO: PTO1235
            RCI: RCIX438(lonB)
            PAI: PAE0243
STRUCTURES  PDB: 1QZM  1RR9  1RRE  1X37  1Z0B  1Z0C  1Z0E  1Z0G  1Z0T  1Z0V  
                 1Z0W  2ANE  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.53
            ExPASy - ENZYME nomenclature database: 3.4.21.53
            ExplorEnz - The Enzyme Database: 3.4.21.53
            ERGO genome analysis and discovery system: 3.4.21.53
            BRENDA, the Enzyme Database: 3.4.21.53
            CAS: 79818-35-2
///
ENTRY       EC 3.4.21.54                Enzyme
NAME        gamma-renin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Cleavage of the Leu!Leu bond in synthetic tetradecapeptide renin
            substrate (horse), to produce angiotensin I, but not active on
            natural angiotensinogen, unlike renin
            (internal_xref(ec_num(3,4,23,15))). Also hydrolyses
            Bz-Arg-p-nitroanilide
COMMENT     A member of the tissue kallikrein family, from submandibular glands
            of male mice. In peptidase family S1 (trypsin family)
REFERENCE   1  [PMID:6337154]
  AUTHORS   Poe M, Wu JK, Florance JR, Rodkey JA, Bennett CD, Hoogsteen K.
  TITLE     Purification and properties of renin and gamma-renin from the mouse
            submaxillary gland.
  JOURNAL   J. Biol. Chem. 258 (1983) 2209-16.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:3288617]
  AUTHORS   Drinkwater CC, Evans BA, Richards RI.
  TITLE     Sequence and expression of mouse gamma-renin.
  JOURNAL   J. Biol. Chem. 263 (1988) 8565-8.
  ORGANISM  mouse [GN:mmu]
ORTHOLOGY   KO: K01339  g-renin
GENES       MMU: 16615(Klk1b16)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.54
            ExPASy - ENZYME nomenclature database: 3.4.21.54
            ExplorEnz - The Enzyme Database: 3.4.21.54
            ERGO genome analysis and discovery system: 3.4.21.54
            BRENDA, the Enzyme Database: 3.4.21.54
            CAS: 85270-20-8
///
ENTRY       EC 3.4.21.55                Enzyme
NAME        venombin AB;
            gabonase;
            okinaxobin II;
            Bitis gabonica venom serine proteinase;
            afaacytin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage at Arg! bonds in fibrinogen to form fibrin and
            release fibrinopeptides A and B
COMMENT     From the venom of the Gaboon viper Bitis gabonica. Activates Factor
            XIII. Not inhibited by antithrombin III/heparin or hirudin, unlike
            EC 3.4.21.5, thrombin
REFERENCE   1  [PMID:3522580]
  AUTHORS   Pirkle H, Theodor I, Miyada D, Simmons G.
  TITLE     Thrombin-like enzyme from the venom of Bitis gabonica. Purification,
            properties, and coagulant actions.
  JOURNAL   J. Biol. Chem. 261 (1986) 8830-5.
  ORGANISM  Bitis gabonica
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.55
            ExPASy - ENZYME nomenclature database: 3.4.21.55
            ExplorEnz - The Enzyme Database: 3.4.21.55
            ERGO genome analysis and discovery system: 3.4.21.55
            BRENDA, the Enzyme Database: 3.4.21.55
            CAS: 104003-74-9
///
ENTRY       EC 3.4.21.56      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Deleted entry: Euphorbain (EC 3.4.21.56 created 1972 as EC 3.4.99.7,
            transferred 1989 to EC 3.4.21.56, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.56
            ExPASy - ENZYME nomenclature database: 3.4.21.56
            ExplorEnz - The Enzyme Database: 3.4.21.56
            ERGO genome analysis and discovery system: 3.4.21.56
            BRENDA, the Enzyme Database: 3.4.21.56
///
ENTRY       EC 3.4.21.57                Enzyme
NAME        leucyl endopeptidase;
            plant Leu-proteinase;
            leucine-specific serine proteinase;
            leucine endopeptidase;
            spinach serine proteinase (leucine specific);
            spinach leucine-specific serine proteinase;
            Leu-proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins. Preferential cleavage: Leu! in small
            molecule substrates
COMMENT     From leaves of the spinach plant (Spinacia oleracea)
REFERENCE   1
  AUTHORS   Aducci, P., Ascenzi, P., Pierini, M. and Ballio, A.
  TITLE     Purification and characterization of Leu-proteinase, the leucine
            specific serine proteinase from spinach (Spinacia oleracea L.)
            leaves.
  JOURNAL   Plant Physiol. 81 (1986) 812-816.
  ORGANISM  spinach
REFERENCE   2
  AUTHORS   Aducci, P., Ascenzi, P. and Ballio, A.
  TITLE     Esterolytic properties of leucine-proteinase, the leucine-specific
            serine proteinase from spinach (Spinacia oleracea L.).
  JOURNAL   Plant Physiol. 82 (1986) 591-593.
  ORGANISM  spinach
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.57
            ExPASy - ENZYME nomenclature database: 3.4.21.57
            ExplorEnz - The Enzyme Database: 3.4.21.57
            ERGO genome analysis and discovery system: 3.4.21.57
            BRENDA, the Enzyme Database: 3.4.21.57
            CAS: 136396-22-0
///
ENTRY       EC 3.4.21.58      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Deleted entry: prohormone serine proteinase (EC 3.4.21.58 created
            1989, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.58
            ExPASy - ENZYME nomenclature database: 3.4.21.58
            ExplorEnz - The Enzyme Database: 3.4.21.58
            ERGO genome analysis and discovery system: 3.4.21.58
            BRENDA, the Enzyme Database: 3.4.21.58
///
ENTRY       EC 3.4.21.59                Enzyme
NAME        tryptase;
            mast cell tryptase;
            mast cell protease II;
            skin tryptase;
            lung tryptase;
            pituitary tryptase;
            mast cell neutral proteinase;
            mast cell tryptase;
            mast cell neutral proteinase;
            mast cell serine proteinase II;
            mast cell proteinase II;
            mast cell serine proteinase tryptase;
            rat mast cell protease II;
            tryptase M
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage: Arg!, Lys!, but with more restricted
            specificity than trypsin
COMMENT     Occurs as a tetrameric molecule with high affinity for heparin, in
            mast cell granules. In peptidase family S1 (trypsin family). Not
            inhibited by alpha1-proteinase inhibitor or alpha2-macroglobulin
REFERENCE   1  [PMID:6358206]
  AUTHORS   Tanaka T, McRae BJ, Cho K, Cook R, Fraki JE, Johnson DA, Powers JC.
  TITLE     Mammalian tissue trypsin-like enzymes. Comparative reactivities of
            human skin tryptase, human lung tryptase, and bovine trypsin with
            peptide 4-nitroanilide and thioester substrates.
  JOURNAL   J. Biol. Chem. 258 (1983) 13552-7.
  ORGANISM  human [GN:hsa], cow [GN:bta]
REFERENCE   2  [PMID:3890754]
  AUTHORS   Kido H, Fukusen N, Katunuma N.
  TITLE     Chymotrypsin- and trypsin-type serine proteases in rat mast cells:
            properties and functions.
  JOURNAL   Arch. Biochem. Biophys. 239 (1985) 436-43.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:3543004]
  AUTHORS   Cromlish JA, Seidah NG, Marcinkiewicz M, Hamelin J, Johnson DA,
            Chretien M.
  TITLE     Human pituitary tryptase: molecular forms, NH2-terminal sequence,
            immunocytochemical localization, and specificity with prohormone and
            fluorogenic substrates.
  JOURNAL   J. Biol. Chem. 262 (1987) 1363-73.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:3140898]
  AUTHORS   Harvima IT, Schechter NM, Harvima RJ, Fraki JE.
  TITLE     Human skin tryptase: purification, partial characterization and
            comparison with human lung tryptase.
  JOURNAL   Biochim. Biophys. Acta. 957 (1988) 71-80.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:2187193]
  AUTHORS   Vanderslice P, Ballinger SM, Tam EK, Goldstein SM, Craik CS, Caughey
            GH.
  TITLE     Human mast cell tryptase: multiple cDNAs and genes reveal a
            multigene serine protease family.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 3811-5.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01340  tryptase
GENES       HSA: 23430(TPSD1) 64499(TPSB2) 7177(TPSAB1)
            PTR: 468084(LOC468084)
            MMU: 17229(Tpsb2) 17230(Tpsab1)
            RNO: 29268(Mcpt6) 54271(Tpsab1)
            CFA: 490080(LOC490080)
            BTA: 281545(TPSB1)
            SSC: 397389(PMCT7)
            BBA: Bd1043
STRUCTURES  PDB: 1A0L  1LTO  2BM2  2F9N  2F9O  2F9P  2FPZ  2FS8  2FS9  2FWW  
                 2FXR  2GDD  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.59
            ExPASy - ENZYME nomenclature database: 3.4.21.59
            ExplorEnz - The Enzyme Database: 3.4.21.59
            ERGO genome analysis and discovery system: 3.4.21.59
            BRENDA, the Enzyme Database: 3.4.21.59
            CAS: 97501-93-4
///
ENTRY       EC 3.4.21.60                Enzyme
NAME        scutelarin;
            taipan activator;
            Oxyuranus scutellatus prothrombin-activating proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage of Arg!Thr and Arg!Ile in prothrombin to form
            thrombin and two inactive fragments
EFFECTOR    Calcium [CPD:C00076];
            Phospholipid [CPD:C00865]
COMMENT     From the venom of the Taipan snake (Oxyuranus scutellatus). Converts
            prothrombin to thrombin in the absence of coagulation Factor Va, and
            is potentiated by phospholipid and Ca2+. Specificity is similar to
            that of Factor Xa. Binds Ca2+ via gamma-carboxyglutamic acid
            residues. Similar enzymes are known from the venom of other
            Australian elapid snakes Pseudonaja textilis textilis, Oxyuranus
            microlepidotus and Demansia nuchalis affinis
REFERENCE   1  [PMID:6986908]
  AUTHORS   Walker FJ, Owen WG, Esmon CT.
  TITLE     Characterization of the prothrombin activator from the venom of
            Oxyuranus scutellatus scutellatus (taipan venom).
  JOURNAL   Biochemistry. 19 (1980) 1020-3.
  ORGANISM  Oxyuranus scutellatus
REFERENCE   2  [PMID:3531198]
  AUTHORS   Speijer H, Govers-Riemslag JW, Zwaal RF, Rosing J.
  TITLE     Prothrombin activation by an activator from the venom of Oxyuranus
            scutellatus (Taipan snake).
  JOURNAL   J. Biol. Chem. 261 (1986) 13258-67.
  ORGANISM  Oxyuranus scutellatus
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.60
            ExPASy - ENZYME nomenclature database: 3.4.21.60
            ExplorEnz - The Enzyme Database: 3.4.21.60
            ERGO genome analysis and discovery system: 3.4.21.60
            BRENDA, the Enzyme Database: 3.4.21.60
            CAS: 93389-45-8
///
ENTRY       EC 3.4.21.61                Enzyme
NAME        kexin;
            yeast KEX2 protease;
            proteinase yscF;
            prohormone-processing endoprotease;
            paired-basic endopeptidase;
            yeast cysteine proteinase F (misleading);
            paired-basic endopeptidase;
            andrenorphin-Gly-generating enzyme;
            endoproteinase Kex2p;
            gene KEX2 dibasic proteinase;
            Kex 2p proteinase;
            Kex2 endopeptidase;
            Kex2 endoprotease;
            Kex2 endoproteinase;
            Kex2 protease;
            proteinase Kex2p;
            Kex2-like precursor protein processing endoprotease;
            prohormone-processing KEX2 proteinase;
            prohormone-processing proteinase;
            proprotein convertase;
            protease KEX2;
            Kex2 proteinase;
            Kex2-like endoproteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Cleavage of -Lys-Arg! and -Arg-Arg! bonds to process yeast
            alpha-factor pheromone and killer toxin precursors
COFACTOR    Calcium [CPD:C00076]
INHIBITOR   p-Mercuribenzoate [CPD:C00985]
COMMENT     A Ca2+-activated peptidase of peptidase family S8, containing Cys
            near the active site His, and inhibited by p-mercuribenzoate.
            Similar enzymes occur in mammals.
REFERENCE   1  [PMID:6430565]
  AUTHORS   Julius D, Brake A, Blair L, Kunisawa R, Thorner J.
  TITLE     Isolation of the putative structural gene for the
            lysine-arginine-cleaving endopeptidase required for processing of
            yeast prepro-alpha-factor.
  JOURNAL   Cell. 37 (1984) 1075-89.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:3894003]
  AUTHORS   Achstetter T, Wolf DH.
  TITLE     Hormone processing and membrane-bound proteinases in yeast.
  JOURNAL   EMBO. J. 4 (1985) 173-7.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:2845974]
  AUTHORS   Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H.
  TITLE     Yeast KEX2 genes encodes an endopeptidase homologous to
            subtilisin-like serine proteases.
  JOURNAL   Biochem. Biophys. Res. Commun. 156 (1988) 246-54.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4  [PMID:2646633]
  AUTHORS   Fuller RS, Brake A, Thorner J.
  TITLE     Yeast prohormone processing enzyme (KEX2 gene product) is a
            Ca2+-dependent serine protease.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 1434-8.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   5  [PMID:2845974]
  AUTHORS   Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H.
  TITLE     Yeast KEX2 genes encodes an endopeptidase homologous to
            subtilisin-like serine proteases.
  JOURNAL   Biochem. Biophys. Res. Commun. 156 (1988) 246-54.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K01341  kexin
GENES       SCE: YNL238W(KEX2)
            AGO: AGOS_ABL203W
            PIC: PICST_14973
            AFM: AFUA_4G12970
            ANG: An01g08530(kexB)
            AVA: Ava_4009
STRUCTURES  PDB: 1OT5  1R64  2ID4  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.61
            ExPASy - ENZYME nomenclature database: 3.4.21.61
            ExplorEnz - The Enzyme Database: 3.4.21.61
            ERGO genome analysis and discovery system: 3.4.21.61
            BRENDA, the Enzyme Database: 3.4.21.61
            CAS: 99676-46-7
///
ENTRY       EC 3.4.21.62                Enzyme
NAME        subtilisin;
            alcalase;
            alcalase 0.6L;
            alcalase 2.5L;
            ALK-enzyme;
            bacillopeptidase A;
            bacillopeptidase B;
            Bacillus subtilis alkaline proteinase bioprase;
            bioprase AL 15;
            bioprase APL 30;
            colistinase;
            (see also comments);
            subtilisin J;
            subtilisin S41;
            subtilisin Sendai;
            subtilisin GX;
            subtilisin E;
            subtilisin BL;
            genenase I;
            esperase;
            maxatase;
            alcalase;
            thermoase PC 10;
            protease XXVII;
            thermoase;
            superase;
            subtilisin DY;
            subtilopeptidase;
            SP 266;
            savinase 8.0L;
            savinase 4.0T;
            kazusase;
            protease VIII;
            opticlean;
            Bacillus subtilis alkaline proteinase;
            protin A 3L;
            savinase;
            savinase 16.0L;
            savinase 32.0 L EX;
            orientase 10B;
            protease S
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins with broad specificity for peptide bonds, and
            a preference for a large uncharged residue in P1. Hydrolyses peptide
            amides
COMMENT     Subtilisin is a serine endopeptidase, type example of peptidase
            family S8. It contains no cysteine residues (although these are
            found in homologous enzymes). Species variants include subtilisin
            BPN' (also subtilisin B, subtilopeptidase B, subtilopeptidase C,
            Nagarse, Nagarse proteinase, subtilisin Novo, bacterial proteinase
            Novo) and subtilisin Carlsberg (subtilisin A, subtilopeptidase A,
            alcalase Novo). Similar enzymes are produced by various Bacillus
            subtilis strains and other Bacillus species [1,3]
REFERENCE   1
  AUTHORS   Ottesen, M. and Svendsen, I.
  TITLE     The subtilisins.
  JOURNAL   Methods Enzymol. 19 (1970) 199-215.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   2
  AUTHORS   Markland, F.S. and Smith, E.L.
  TITLE     Subtilisins: primary structure, chemical and physical properties.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 3, Academic Press,
            New York, 1971, p. 561-608.
REFERENCE   3  [PMID:6221910]
  AUTHORS   Tang H.
  TITLE     [The use of single-dose total body irradiation before bone marrow
            transplantation in treatment of leukemia]
  JOURNAL   Zhonghua. Fang. She. Xue. Za. Zhi. 16 (1982) 296-300.
REFERENCE   4  [PMID:3927935]
  AUTHORS   Nedkov P, Oberthur W, Braunitzer G.
  TITLE     Determination of the complete amino-acid sequence of subtilisin DY
            and its comparison with the primary structures of the subtilisins
            BPN', Carlsberg and amylosacchariticus.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 366 (1985) 421-30.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   5  [PMID:3108260]
  AUTHORS   Ikemura H, Takagi H, Inouye M.
  TITLE     Requirement of pro-sequence for the production of active subtilisin
            E in Escherichia coli.
  JOURNAL   J. Biol. Chem. 262 (1987) 7859-64.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   6
  AUTHORS   Polgar, L.
  TITLE     Structure and function of serine proteases.
  JOURNAL   In: Neuberger, A. and Brocklehurst, K. (Eds.), New Comprehensive
            Biochemistry: Hydrolytic Enzymes, vol. 16, Elsevier, Amsterdam,
            1987, p. 159-200.
ORTHOLOGY   KO: K01342  subtilisin
GENES       DME: Dmel_CG7169(S1P)
            OSA: 4334194
            ANG: An09g03780(pepD)
            PFA: PFE0370c
            PEN: PSEEN4433
            CPS: CPS_0751
            DNO: DNO_0603(aprV5)
            AZO: azo1237(subC)
            GSU: GSU2075
            GME: Gmet_0931
            RLE: RL1858
            BRA: BRADO0807
            RDE: RD1_4002(apr)
            BSU: BG10190(aprE)
            BHA: BH0684(alp) BH0855
            BLI: BL01111(kerA)
            BLD: BLi01109
            BCL: ABC0761(aprE)
            BAY: RBAM_010500
            BPU: BPUM_0972
            MTA: Moth_2027
            MPU: MYPU_6550
            MHJ: MHJ_0085
            RHA: RHA1_ro08410
            SEN: SACE_7133(aprE)
            RBA: RB841
            AVA: Ava_2018 Ava_4060
STRUCTURES  PDB: 1A2Q  1AF4  1AK9  1AQN  1AU9  1AV7  1AVT  1BE6  1BE8  1BFK  
                 1BFU  1BH6  1C3L  1C9J  1C9M  1C9N  1CSE  1DUI  1GCI  1GNS  
                 1GNV  1IAV  1JEA  1LW6  1MPT  1NDQ  1NDU  1OYV  1Q5P  1R0R  
                 1SBC  1SBH  1SBI  1SBN  1SCA  1SCB  1SCD  1SCJ  1SCN  1SIB  
                 1SPB  1ST3  1SUA  1SUB  1SUC  1SUD  1SUE  1SUP  1SVN  1TK2  
                 1TM1  1TM3  1TM4  1TM5  1TM7  1TMG  1TO1  1TO2  1UBN  1V5I  
                 1VSB  1Y1K  1Y33  1Y34  1Y3B  1Y3C  1Y3D  1Y3F  1Y48  1Y4A  
                 1Y4D  1YU6  2E1P  2GKO  2SEC  3SIC  3VSB  5SIC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.62
            ExPASy - ENZYME nomenclature database: 3.4.21.62
            ExplorEnz - The Enzyme Database: 3.4.21.62
            ERGO genome analysis and discovery system: 3.4.21.62
            BRENDA, the Enzyme Database: 3.4.21.62
            CAS: 9014-01-1
///
ENTRY       EC 3.4.21.63                Enzyme
NAME        oryzin;
            Aspergillus alkaline proteinase;
            aspergillopeptidase B;
            API 21;
            aspergillopepsin B;
            aspergillopepsin F;
            Aspergillus candidus alkaline proteinase;
            Aspergillus flavus alkaline proteinase;
            Aspergillus melleus semi-alkaline proteinase;
            Aspergillus oryzae alkaline proteinase;
            Aspergillus parasiticus alkaline proteinase;
            Aspergillus serine proteinase;
            Aspergillus sydowi alkaline proteinase;
            Aspergillus soya alkaline proteinase;
            Aspergillus melleus alkaline proteinase;
            Aspergillus sulphureus alkaline proteinase;
            prozyme;
            P 5380;
            kyorinase;
            seaprose S;
            semi-alkaline protease;
            sumizyme MP;
            prozyme 10;
            onoprose;
            onoprose SA;
            protease P;
            promelase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt >
            Ac-Tyr-OEt. Does not hydrolyze peptide amides
COMMENT     A peptidase of family S8 (subtilisin family), not containing
            cysteine, that is the predominant extracellular alkaline
            endopeptidase of the mold Aspergillus oryzae. Identical or closely
            related enzymes are produced by A. flavus and A. sojae [2,3,4]
REFERENCE   1
  AUTHORS   Nakagawa, Y.
  TITLE     Alkaline proteinases from Aspergillus.
  JOURNAL   Methods Enzymol. 19 (1970) 581-591.
  ORGANISM  Aspergillus sojae, Aspergillus sydowii , Aspergillus flavus,
            Aspergillus oryzae [GN:aor]
REFERENCE   2
  AUTHORS   Hayashi, K. and Terada, M.
  TITLE     Some characteristics of hydrolysis of synthetic substrates and
            proteins by the alkaline proteases from Aspergillus sojae.
  JOURNAL   Agric. Biol. Chem. 36 (1972) 1755-1765.
  ORGANISM  Aspergillus sojae
REFERENCE   3  [PMID:4623338]
  AUTHORS   Turkova J, Mikes O, Hayashi K, Danno G, Polgar L.
  TITLE     Alkaline proteinases of the genus Aspergillus.
  JOURNAL   Biochim. Biophys. Acta. 257 (1972) 257-63.
  ORGANISM  Aspergillus sojae, Aspergillus flavus, Aspergillus oryzae [GN:aor],
            Aspergillus sulphureus
REFERENCE   4  [PMID:4441086]
  AUTHORS   Morihara K, Oka T, Tsuzuki H.
  TITLE     Comparative study of various serine alkaline proteinases from
            microorganisms. Esterase activity against N-acylated peptide ester
            substrates.
  JOURNAL   Arch. Biochem. Biophys. 165 (1974) 72-9.
  ORGANISM  Aspergillus melleus, Streptomyces fradiae
REFERENCE   5  [PMID:4859351]
  AUTHORS   Spadari S, Subramanian AR, Kalnitsky G.
  TITLE     Highly restricted specificity of the serine proteinase
            aspergillopeptidase B.
  JOURNAL   Biochim. Biophys. Acta. 359 (1974) 267-72.
  ORGANISM  Aspergillus oryzae [GN:aor]
GENES       AFM: AFUA_4G11800
            VCO: VC0395_A2570(prlC)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.63
            ExPASy - ENZYME nomenclature database: 3.4.21.63
            ExplorEnz - The Enzyme Database: 3.4.21.63
            ERGO genome analysis and discovery system: 3.4.21.63
            BRENDA, the Enzyme Database: 3.4.21.63
            CAS: 9074-07-1
///
ENTRY       EC 3.4.21.64                Enzyme
NAME        peptidase K;
            Tritirachium alkaline proteinase;
            Tritirachium album serine proteinase;
            proteinase K;
            Tritirachium album proteinase K;
            endopeptidase K
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of keratin, and of other proteins with subtilisin-like
            specificity. Hydrolyses peptide amides
COMMENT     From the mold Tritirachium album Limber. A peptidase of family S8
            (subtilisin family) containing two disulfide bridges and one free
            Cys near the active site His. Formerly included in EC 3.4.21.14
REFERENCE   1  [PMID:4373242]
  AUTHORS   Ebeling W, Hennrich N, Klockow M, Metz H, Orth HD, Lang H.
  TITLE     Proteinase K from Tritirachium album Limber.
  JOURNAL   Eur. J. Biochem. 47 (1974) 91-7.
  ORGANISM  Tritirachium album
REFERENCE   2
  AUTHORS   Morihara, K. and Tsuzuki, H.
  TITLE     Specificity of proteinase K from Tritirachium album Limber for
            synthetic peptides.
  JOURNAL   Agric. Biol. Chem. 39 (1975) 1489-1492.
  ORGANISM  Tritirachium album
REFERENCE   3  [PMID:943367]
  AUTHORS   Kraus E, Kiltz HH, Femfert UF.
  TITLE     The specificity of proteinase K against oxidized insulin B chain.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 357 (1976) 233-7.
  ORGANISM  Tritirachium album
REFERENCE   4
  AUTHORS   Jany, K.-D., Lederer, G. and Mayer, B.
  TITLE     Amino acid sequence of proteinase K from the mold Tritirachium album
            Limber.
  JOURNAL   FEBS Lett. 199 (1986) 139-144.
  ORGANISM  Tritirachium album
REFERENCE   5  [PMID:2184432]
  AUTHORS   Betzel C, Teplyakov AV, Harutyunyan EH, Saenger W, Wilson KS.
  TITLE     Thermitase and proteinase K: a comparison of the refined
            three-dimensional structures of the native enzymes.
  JOURNAL   Protein. Eng. 3 (1990) 161-72.
STRUCTURES  PDB: 1BJR  1CNM  1EGQ  1HT3  1IC6  1OYO  1P7V  1P7W  1PEK  1PFG  
                 1PJ8  1PTK  2DP4  2DQK  2DUJ  2G4V  2HD4  2HPZ  2ID8  2PKC  
                 2PQ2  2PWA  2PWB  2PYZ  3PRK  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.64
            ExPASy - ENZYME nomenclature database: 3.4.21.64
            ExplorEnz - The Enzyme Database: 3.4.21.64
            ERGO genome analysis and discovery system: 3.4.21.64
            BRENDA, the Enzyme Database: 3.4.21.64
            CAS: 39450-01-6
///
ENTRY       EC 3.4.21.65                Enzyme
NAME        thermomycolin;
            thermomycolase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Rather nonspecific hydrolysis of proteins. Preferential cleavage:
            Ala!, Tyr!, Phe! in small molecule substrates
COMMENT     A peptidase of family S8 (subtilisin family) from the thermophilic
            fungus Malbranchea pulchella var. sulfurea containing Cys, but not
            inhibited by p-mercuribenzoate. Very thermostable. Formerly included
            in EC 3.4.21.14
REFERENCE   1  [PMID:1012007]
  AUTHORS   Gaucher GM, Stevenson KJ.
  TITLE     Thermomycolin.
  JOURNAL   Methods. Enzymol. 45 (1976) 415-33.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.65
            ExPASy - ENZYME nomenclature database: 3.4.21.65
            ExplorEnz - The Enzyme Database: 3.4.21.65
            ERGO genome analysis and discovery system: 3.4.21.65
            BRENDA, the Enzyme Database: 3.4.21.65
            CAS: 52233-31-5
///
ENTRY       EC 3.4.21.66                Enzyme
NAME        thermitase;
            thermophilic Streptomyces serine proteinase;
            Thermoactinomyces vulgaris serine proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins, including collagen
INHIBITOR   p-Mercuribenzoate [CPD:C00985]
COMMENT     A peptidase of family S8 (subtilisin family) from Thermoactinomyces
            vulgaris containing a single Cys, near the active site His, and
            inhibited by p-mercuribenzoate. The N-terminal extension of the
            polypeptide chain relative to subtilisin contributes to Ca2+-binding
            and the high thermostability. The amino acid composition and
            properties of the thermostable enzyme from Streptomyces rectus var.
            proteolyticus (formerly included in EC 3.4.21.14) are closely
            similar [1,2]
REFERENCE   1  [PMID:4711613]
  AUTHORS   Mizusawa K, Yoshida F.
  TITLE     Thermophilic Streptomyces alkaline proteinase. II. The role of a
            sulfhydryl group and the conformational stability.
  JOURNAL   J. Biol. Chem. 248 (1973) 4417-23.
  ORGANISM  Streptomyces rectus
REFERENCE   2  [PMID:4373436]
  AUTHORS   Borgia P, Campbell LL.
  TITLE     Properties of two homologous alkaline proteases from Streptomyces
            rectus.
  JOURNAL   J. Bacteriol. 120 (1974) 1109-15.
  ORGANISM  Streptomyces rectus
REFERENCE   3  [PMID:7051706]
  AUTHORS   Kleine R.
  TITLE     Properties of thermitase, a thermostable serine protease from
            Thermoactinomyces vulgaris.
  JOURNAL   Acta. Biol. Med. Ger. 41 (1982) 89-102.
  ORGANISM  Thermoactinomyces vulgaris
REFERENCE   4
  AUTHORS   Meloun, B., Baudy, M., Kostka, V., Hausdorf, G., Frommel, C. and
            Hohne, W.E.
  TITLE     Complete primary structure of thermitase from Thermoactinomyces
            vulgaris and its structural features related to the subtilisin-type
            proteinases.
  JOURNAL   FEBS Lett. 183 (1985) 195-200.
  ORGANISM  Thermoactinomyces vulgaris
REFERENCE   5  [PMID:2196375]
  AUTHORS   Teplyakov AV, Kuranova IP, Harutyunyan EH, Vainshtein BK, Frommel C,
            Hohne WE, Wilson KS.
  TITLE     Crystal structure of thermitase at 1.4 A resolution.
  JOURNAL   J. Mol. Biol. 214 (1990) 261-79.
  ORGANISM  Thermoactinomyces vulgaris
ORTHOLOGY   KO: K08651  thermitase
GENES       NOC: Noc_0787
            BUR: Bcep18194_B1283
            BBT: BBta_6385
            BCE: BC2316
            BTK: BT9727_2155
            AVA: Ava_0365 Ava_3522 Ava_4226
STRUCTURES  PDB: 1TEC  1THM  2TEC  3TEC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.66
            ExPASy - ENZYME nomenclature database: 3.4.21.66
            ExplorEnz - The Enzyme Database: 3.4.21.66
            ERGO genome analysis and discovery system: 3.4.21.66
            BRENDA, the Enzyme Database: 3.4.21.66
            CAS: 69772-87-8
///
ENTRY       EC 3.4.21.67                Enzyme
NAME        endopeptidase So;
            E. coli cytoplasmic proteinase;
            proteinase So;
            Escherichia coli serine proteinase So
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins, but not Bz-Tyr-OEt,
            Ac-Phe-beta-naphthylester, or Bz-Arg-OEt
INHIBITOR   Tos-Ph-CH2Cl [CPD:C01964]
COMMENT     An Escherichia coli cytoplasmic endopeptidase formerly included in
            EC 3.4.21.14. Inhibited by Tos-Phe-CH2Cl, but not by Tos-Lys-CH2Cl
REFERENCE   1  [PMID:7043205]
  AUTHORS   Goldberg AL, Swamy KH, Chung CH, Larimore FS.
  TITLE     Proteases in Escherichia coli.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 680-702.
REFERENCE   2  [PMID:6339474]
  AUTHORS   Chung CH, Goldberg AL.
  TITLE     Purification and characterization of protease So, a cytoplasmic
            serine protease in Escherichia coli.
  JOURNAL   J. Bacteriol. 154 (1983) 231-8.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.67
            ExPASy - ENZYME nomenclature database: 3.4.21.67
            ExplorEnz - The Enzyme Database: 3.4.21.67
            ERGO genome analysis and discovery system: 3.4.21.67
            BRENDA, the Enzyme Database: 3.4.21.67
            CAS: 81611-83-8
///
ENTRY       EC 3.4.21.68                Enzyme
NAME        t-plasminogen activator;
            tissue plasminogen activator;
            plasminogen activator, tissue-type;
            tissue-type plasminogen activator;
            tPA;
            t-PA
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Specific cleavage of Arg!Val bond in plasminogen to form plasmin
EFFECTOR    Fibrin [CPD:C00290]
COMMENT     A peptidase of family S1 (trypsin family) from a wide variety of
            mammalian tissues, especially endothelial cells. Secreted as a
            single chain precursor which is cleaved to a two-chain form by
            plasmin. Activity is considerably enhanced by fibrin. Formerly
            included in EC 3.4.21.31 and EC 3.4.99.26
REFERENCE   1  [PMID:6337343]
  AUTHORS   Pennica D, Holmes WE, Kohr WJ, Harkins RN, Vehar GA, Ward CA,
            Bennett WF, Yelverton E, Seeburg PH, Heyneker HL, Goeddel DV, Collen
            D.
  TITLE     Cloning and expression of human tissue-type plasminogen activator
            cDNA in E. coli.
  JOURNAL   Nature. 301 (1983) 214-21.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:3148826]
  AUTHORS   Loskutoff DJ, Schleef RR.
  TITLE     Plasminogen activators and their inhibitors.
  JOURNAL   Methods. Enzymol. 163 (1988) 293-302.
REFERENCE   3  [PMID:2962643]
  AUTHORS   Petersen LC, Johannessen M, Foster D, Kumar A, Mulvihill E.
  TITLE     The effect of polymerised fibrin on the catalytic activities of
            one-chain tissue-type plasminogen activator as revealed by an
            analogue resistant to plasmin cleavage.
  JOURNAL   Biochim. Biophys. Acta. 952 (1988) 245-54.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:3148827]
  AUTHORS   Verheijen JH.
  TITLE     Tissue-type plasminogen activator and fast-acting plasminogen
            activator inhibitor in plasma.
  JOURNAL   Methods. Enzymol. 163 (1988) 302-9.
REFERENCE   5  [PMID:2496643]
  AUTHORS   Gerard RD, Meidell RS.
  TITLE     Regulation of tissue plasminogen activator expression.
  JOURNAL   Annu. Rev. Physiol. 51 (1989) 245-62.
REFERENCE   6
  AUTHORS   Collen, D., Lijnen, H. R. and Verstraete, M.
  TITLE     The fibrinolytic system and its disorders.
  JOURNAL   In: Handin, R.I., Lux, S.E. and Stossel, J.P. (Eds.), Blood:
            Principles and Practice of Hematology, 2nd ed., J.B.Lippincott
            Company, Philadelphia, 1990.
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01343  tissue plasminogen activator
GENES       HSA: 5327(PLAT)
            PTR: 472748(PLAT)
            MMU: 18791(Plat)
            RNO: 25692(Plat)
            CFA: 482840(PLAT)
            BTA: 281407(PLAT)
            SSC: 397121(PLAT)
            GGA: 426791(PLAT)
            TET: TTHERM_00571860
            PLA: Plav_1463
            SMD: Smed_2924
            OAN: Oant_1103
            BBT: BBta_1433
            XAU: Xaut_2078
            RSQ: Rsph17025_2203
            SWI: Swit_0621
            ACR: Acry_1679
STRUCTURES  PDB: 1A5H  1A5I  1BDA  1PK2  1PML  1RTF  1TPG  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.68
            ExPASy - ENZYME nomenclature database: 3.4.21.68
            ExplorEnz - The Enzyme Database: 3.4.21.68
            ERGO genome analysis and discovery system: 3.4.21.68
            BRENDA, the Enzyme Database: 3.4.21.68
            CAS: 139639-23-9
///
ENTRY       EC 3.4.21.69                Enzyme
NAME        protein C (activated);
            blood-coagulation factor XIVa;
            activated blood coagulation factor XIV;
            activated protein C;
            autoprothrombin II-A;
            protein Ca;
            APC;
            GSAPC
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Degradation of blood coagulation factors Va and VIIIa
COMMENT     A peptidase of family S1 (trypsin family), one of the
            gamma-carboxyglutamic acid-containing coagulation factors. Formed
            from protein C, the proenzyme that circulates in plasma, by the
            action of a complex of thrombin with thrombomodulin, or by serine
            endopeptidases present in several snake venoms
REFERENCE   1  [PMID:3029867]
  AUTHORS   Esmon CT.
  TITLE     The regulation of natural anticoagulant pathways.
  JOURNAL   Science. 235 (1987) 1348-52.
REFERENCE   2  [PMID:8917439]
  AUTHORS   Dejgaard K, Leffers H.
  TITLE     Characterisation of the nucleic-acid-binding activity of KH domains.
            Different properties of different domains.
  JOURNAL   Eur. J. Biochem. 241 (1996) 425-31.
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01344  protein C (activated)
GENES       HSA: 5624(PROC)
            PTR: 459593(PROC)
            MMU: 19123(Proc)
            RNO: 25268(Proc)
            CFA: 476104(PROC)
            BTA: 281428(PROC)
            SSC: 396954(PROC)
            GGA: 395085(PROC)
            XLA: 380116(proc)
            XTR: 548476(MGC107972)
            DRE: 393327(zgc:63987)
STRUCTURES  PDB: 1AUT  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.69
            ExPASy - ENZYME nomenclature database: 3.4.21.69
            ExplorEnz - The Enzyme Database: 3.4.21.69
            ERGO genome analysis and discovery system: 3.4.21.69
            BRENDA, the Enzyme Database: 3.4.21.69
            CAS: 42617-41-4
///
ENTRY       EC 3.4.21.70                Enzyme
NAME        pancreatic endopeptidase E;
            cholesterol-binding proteinase;
            proteinase E;
            cholesterol-binding serine proteinase;
            pancreatic protease E;
            pancreatic proteinase E;
            cholesterol-binding pancreatic proteinase;
            CBPP;
            pancreas E proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage: Ala!. Does not hydrolyse elastin
COMMENT     A peptidase of family S1 (trypsin family) from pancreatic juice.
            Unlike elastases, has an acidic pI. Binds cholesterol
REFERENCE   1  [PMID:234742]
  AUTHORS   Mallory PA, Travis J.
  TITLE     Human pancreatic enzymes: purification and characterization of a
            nonelastolytic enzyme, protease E. resembling elastase.
  JOURNAL   Biochemistry. 14 (1975) 722-30.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:3477287]
  AUTHORS   Shen WF, Fletcher TS, Largman C.
  TITLE     Primary structure of human pancreatic protease E determined by
            sequence analysis of the cloned mRNA.
  JOURNAL   Biochemistry. 26 (1987) 3447-52.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01345  pancreatic endopeptidase E
GENES       HSA: 10136(ELA3A) 23436(ELA3B)
            PTR: 456491(ELA3B)
            MMU: 67868(Ela3)
            RNO: 298567(Ela3b_predicted)
            CFA: 478196(ELA3B)
            BTA: 281752(ELA3B)
            XLA: 447029(ela3b)
            XTR: 496902(ela3b)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.70
            ExPASy - ENZYME nomenclature database: 3.4.21.70
            ExplorEnz - The Enzyme Database: 3.4.21.70
            ERGO genome analysis and discovery system: 3.4.21.70
            BRENDA, the Enzyme Database: 3.4.21.70
            CAS: 68073-27-8
///
ENTRY       EC 3.4.21.71                Enzyme
NAME        pancreatic elastase II;
            pancreatic elastase 2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage: Leu!, Met! and Phe!. Hydrolyses elastin
COMMENT     A peptidase of family S1 (trypsin family) formed by activation of
            proelastase II from mammalian pancreas by trypsin. Usually, only one
            of the pancreatic elastases (see also EC 3.4.21.36) is expressed in
            a given species; human pancreatic elastase is of type II
REFERENCE   1  [PMID:3427074]
  AUTHORS   Fletcher TS, Shen WF, Largman C.
  TITLE     Primary structure of human pancreatic elastase 2 determined by
            sequence analysis of the cloned mRNA.
  JOURNAL   Biochemistry. 26 (1987) 7256-61.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:2834346]
  AUTHORS   Shirasu Y, Yoshida H, Matsuki S, Takemura K, Ikeda N, Shimada Y,
            Ozawa T, Mikayama T, Iijima H, Ishida A, et al.
  TITLE     Molecular cloning and expression in Escherichia coli of a cDNA
            encoding human pancreatic elastase 2.
  JOURNAL   J. Biochem. (Tokyo). 102 (1987) 1555-63.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01346  pancreatic elastase II
GENES       HSA: 51032(ELA2B) 63036(ELA2A)
            PTR: 469129(ELA2A)
            MMU: 13706(RP23-395H4.4)
            RNO: 24332(Ela2)
            BTA: 282687(Ela2)
            SSC: 397197(ELA2)
            XLA: 444404(MGC82963)
            DRE: 334304(zgc:63744)
            VFI: VFA0273
STRUCTURES  PDB: 1BRU  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.71
            ExPASy - ENZYME nomenclature database: 3.4.21.71
            ExplorEnz - The Enzyme Database: 3.4.21.71
            ERGO genome analysis and discovery system: 3.4.21.71
            BRENDA, the Enzyme Database: 3.4.21.71
            CAS: 75603-19-9
///
ENTRY       EC 3.4.21.72                Enzyme
NAME        IgA-specific serine endopeptidase;
            IgA protease;
            IgA proteinase;
            IgA-specific proteinase;
            immunoglobulin A protease;
            immunoglobulin A proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Cleavage of immunoglobulin A molecules at certain Pro! bonds in the
            hinge region. No small molecule substrates are known
COMMENT     Species variants differing slightly in specificity are secreted by
            Gram-negative bacteria Neisseria gonorrhoeae and Haemophilus
            influenzae. Type example of peptidase family S6. Some other
            bacterial endopeptidases with similar specificity are of metallo-
            type (see EC 3.4.24.13, IgA-specific metalloendopeptidase)
REFERENCE   1  [PMID:6416146]
  AUTHORS   Plaut AG.
  TITLE     The IgA1 proteases of pathogenic bacteria.
  JOURNAL   Annu. Rev. Microbiol. 37 (1983) 603-22.
REFERENCE   2  [PMID:2105953]
  AUTHORS   Bachovchin WW, Plaut AG, Flentke GR, Lynch M, Kettner CA.
  TITLE     Inhibition of IgA1 proteinases from Neisseria gonorrhoeae and
            Hemophilus influenzae by peptide prolyl boronic acids.
  JOURNAL   J. Biol. Chem. 265 (1990) 3738-43.
  ORGANISM  Neisseria gonorrhoeae [GN:ngo], Hemophilus influenzae
ORTHOLOGY   KO: K01347  IgA-specific serine endopeptidase
GENES       ECI: UTI89_C2514(yfaL)
            HIT: NTHI0354(hap) NTHI1164(iga1)
            NME: NMB0700
            NMA: NMA0457(iga2) NMA0905(iga)
            NMC: NMC1959(iga2)
            NGO: NGO0275 NGO2105
            LLM: llmg_0877
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.72
            ExPASy - ENZYME nomenclature database: 3.4.21.72
            ExplorEnz - The Enzyme Database: 3.4.21.72
            ERGO genome analysis and discovery system: 3.4.21.72
            BRENDA, the Enzyme Database: 3.4.21.72
            CAS: 55127-02-1
///
ENTRY       EC 3.4.21.73                Enzyme
NAME        u-plasminogen activator;
            urokinase;
            urinary plasminogen activator;
            cellular plasminogen activator;
            urokinase-type plasminogen activator;
            double-chain urokinase-type plasminogen activator;
            two-chain urokinase-type plasminogen activator;
            urokinase plasminogen activator;
            uPA;
            u-PA;
            abbokinase;
            urinary esterase A
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Specific cleavage of Arg!Val bond in plasminogen to form plasmin
COMMENT     Formed from the inactive precursor by action of plasmin or plasma
            kallikrein. Differs in structure from t-plasminogen activator (EC
            3.4.21.68), and does not bind to fibrin. In peptidase family S1
            (trypsin family). Formerly included in EC 3.4.21.31 and EC 3.4.99.26
REFERENCE   1  [PMID:6210826]
  AUTHORS   Lottenberg R, Christensen U, Jackson CM, Coleman PL.
  TITLE     Assay of coagulation proteases using peptide chromogenic and
            fluorogenic substrates.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 341-61.
REFERENCE   2  [PMID:3148826]
  AUTHORS   Loskutoff DJ, Schleef RR.
  TITLE     Plasminogen activators and their inhibitors.
  JOURNAL   Methods. Enzymol. 163 (1988) 293-302.
REFERENCE   3  [PMID:3143380]
  AUTHORS   Saksela O, Rifkin DB.
  TITLE     Cell-associated plasminogen activation: regulation and physiological
            functions.
  JOURNAL   Annu. Rev. Cell. Biol. 4 (1988) 93-126.
REFERENCE   4
  AUTHORS   Collen, D., Lijnen, H. R. and Verstraete, M.
  TITLE     The fibrinolytic system and its disorders.
  JOURNAL   In: Handin, R.I., Lux, S.E. and Stossel, J.P. (Eds.), Blood:
            Principles and Practice of Hematology, 2nd ed., J.B.Lippincott
            Company, Philadelphia, 1990.
REFERENCE   5  [PMID:1969415]
  AUTHORS   Lijnen HR, Van Hoef B, Nelles L, Collen D.
  TITLE     Plasminogen activation with single-chain urokinase-type plasminogen
            activator (scu-PA). Studies with active site mutagenized plasminogen
            (Ser740----Ala) and plasmin-resistant scu-PA (Lys158----Glu).
  JOURNAL   J. Biol. Chem. 265 (1990) 5232-6.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K01348  urokinase plasminogen activator
GENES       HSA: 5328(PLAU)
            MMU: 18792(Plau)
            RNO: 25619(Plau)
            CFA: 403426(PLAU)
            BTA: 281408(PLAU)
            SSC: 396985(PLAU)
            GGA: 396424(PLAU)
STRUCTURES  PDB: 1C5W  1C5X  1C5Y  1C5Z  1EJN  1F5K  1F5L  1F92  1FV9  1GI7  
                 1GI8  1GI9  1GJ7  1GJ8  1GJ9  1GJA  1GJB  1GJC  1GJD  1LMW  
                 1O3P  1O5A  1O5B  1O5C  1OWD  1OWE  1OWH  1OWI  1OWJ  1OWK  
                 1SC8  1SQA  1SQO  1SQT  1U6Q  1VJ9  1VJA  2FD6  2I9A  2I9B  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.73
            ExPASy - ENZYME nomenclature database: 3.4.21.73
            ExplorEnz - The Enzyme Database: 3.4.21.73
            ERGO genome analysis and discovery system: 3.4.21.73
            BRENDA, the Enzyme Database: 3.4.21.73
            CAS: 9039-53-6
///
ENTRY       EC 3.4.21.74                Enzyme
NAME        venombin A;
            alpha-fibrinogenase;
            habutobin;
            zinc metalloproteinase Cbfib1.1;
            zinc metalloproteinase Cbfib1.2;
            zinc metalloproteinase Cbfib2;
            ancrod;
            (see also Comments)Comments: A somewhat thrombin-like enzyme from
            venoms of snakes of the viper/rattlesnake group. Species variants of
            the enzyme include ancrod from Agkistrodon rhodostoma (Malayan pit
            viper) (formerly EC 3.4.21.28) [1], batroxobin from Bothrops atrox
            (South American pit viper) (formerly EC 3.4.21.29) [2,5] and
            crotalase from Crotalus adamanteus (Eastern diamondback rattlesnake)
            (formerly EC 3.4.21.30) [3,4]. In peptidase family S1 (trypsin
            family). Does not require activation by Ca2+
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage of Arg! bond in fibrinogen, to form fibrin, and
            release fibrinopeptide A. The specificity of further degradation of
            fibrinogen varies with species origin of the enzyme
REFERENCE   1  [PMID:1011992]
  AUTHORS   Nolan C, Hall LS, Barlow GH.
  TITLE     Ancrod, the coagulating enzyme from Malayan pit viper (Agkistrodon
            rhodostoma) venom.
  JOURNAL   Methods. Enzymol. 45 (1976) 205-13.
  ORGANISM  Agkistrodon rhodostoma
REFERENCE   2  [PMID:1011993]
  AUTHORS   Stocker K, Barlow GH.
  TITLE     The coagulant enzyme from Bothrops atrox venom (batroxobin).
  JOURNAL   Methods. Enzymol. 45 (1976) 214-23.
  ORGANISM  Bothrops atrox
REFERENCE   3  [PMID:2934864]
  AUTHORS   Simmons G, Bundalian M, Theodor I, Martinoli J, Pirkle H.
  TITLE     Action of crotalase, an enzyme with thrombin-like and
            kallikrein-like specificities, on tripeptide nitroanilide
            derivatives.
  JOURNAL   Thromb. Res. 40 (1985) 555-61.
  ORGANISM  Crotalus adamanteus
REFERENCE   4  [PMID:2934864]
  AUTHORS   Simmons G, Bundalian M, Theodor I, Martinoli J, Pirkle H.
  TITLE     Action of crotalase, an enzyme with thrombin-like and
            kallikrein-like specificities, on tripeptide nitroanilide
            derivatives.
  JOURNAL   Thromb. Res. 40 (1985) 555-61.
  ORGANISM  Crotalus adamanteus
REFERENCE   5  [PMID:3163691]
  AUTHORS   Itoh N, Tanaka N, Funakoshi I, Kawasaki T, Mihashi S, Yamashina I.
  TITLE     Organization of the gene for batroxobin, a thrombin-like snake venom
            enzyme. Homology with the trypsin/kallikrein gene family.
  JOURNAL   J. Biol. Chem. 263 (1988) 7628-31.
STRUCTURES  PDB: 2AIP  2AIQ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.74
            ExPASy - ENZYME nomenclature database: 3.4.21.74
            ExplorEnz - The Enzyme Database: 3.4.21.74
            ERGO genome analysis and discovery system: 3.4.21.74
            BRENDA, the Enzyme Database: 3.4.21.74
            CAS: 146240-35-9
///
ENTRY       EC 3.4.21.75                Enzyme
NAME        furin;
            prohormone convertase;
            dibasic processing enzyme;
            PACE;
            paired basic amino acid cleaving enzyme;
            paired basic amino acid converting enzyme;
            serine proteinase PACE;
            PC1;
            SPC3;
            proprotein convertase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Release of mature proteins from their proproteins by cleavage of
            -Arg-Xaa-Yaa-Arg! bonds, where Xaa can by any amino acid and Yaa is
            Arg or Lys. Releases albumin, complement component C3 and von
            Willebrand factor from their respective precursors
COMMENT     One of a group of peptidases in peptidase family S8 (subtilisin
            family) that is structurally and functionally similar to kexin. All
            are activated by Ca2+, contain Cys near the active site His, and are
            inhibited by p-mercuribenzoate. At least three related enzymes are
            recognized in mammals: PC2, PC3 and PC4, which have somewhat
            different specificities
REFERENCE   1  [PMID:2094803]
  AUTHORS   van de Ven WJ, Voorberg J, Fontijn R, Pannekoek H, van den Ouweland
            AM, van Duijnhoven HL, Roebroek AJ, Siezen RJ.
  TITLE     Furin is a subtilisin-like proprotein processing enzyme in higher
            eukaryotes.
  JOURNAL   Mol. Biol. Rep. 14 (1990) 265-75.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:1843280]
  AUTHORS   Van de Ven WJ, Creemers JW, Roebroek AJ.
  TITLE     Furin: the prototype mammalian subtilisin-like proprotein-processing
            enzyme. Endoproteolytic cleavage at paired basic residues of
            proproteins of the eukaryotic secretory pathway.
  JOURNAL   Enzyme. 45 (1991) 257-70.
  ORGANISM  human [GN:hsa], mouse [GN:mmu]
REFERENCE   3  [PMID:1587790]
  AUTHORS   Hatsuzawa K, Murakami K, Nakayama K.
  TITLE     Molecular and enzymatic properties of furin, a Kex2-like
            endoprotease involved in precursor cleavage at Arg-X-Lys/Arg-Arg
            sites.
  JOURNAL   J. Biochem. (Tokyo). 111 (1992) 296-301.
  ORGANISM  mouse [GN:mmu]
REFERENCE   4
  AUTHORS   Seidah, N.G. and Chretien, M.
  TITLE     Proprotein and prohormone convertases of the subtilisin family:
            recent developments and future perspectives.
  JOURNAL   Trends Endocrinol. Metab. 3 (1992) 133-140.
  ORGANISM  human [GN:hsa], mouse [GN:mmu]
REFERENCE   5  [PMID:1429684]
  AUTHORS   Steiner DF, Smeekens SP, Ohagi S, Chan SJ.
  TITLE     The new enzymology of precursor processing endoproteases.
  JOURNAL   J. Biol. Chem. 267 (1992) 23435-8.
  ORGANISM  human [GN:hsa], mouse [GN:mmu]
ORTHOLOGY   KO: K01349  furin
GENES       HSA: 5045(FURIN)
            PTR: 453652(FURIN)
            MMU: 18550(Furin)
            RNO: 54281(Pcsk3)
            CFA: 488746(FURIN)
            BTA: 281374(FURIN)
            GGA: 395457(FURIN)
            XLA: 397747(LOC397747)
            SPU: 574878(LOC574878)
            DME: Dmel_CG10772(Fur1) Dmel_CG18734(Fur2)
            AVA: Ava_2140
STRUCTURES  PDB: 1P8J  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.75
            ExPASy - ENZYME nomenclature database: 3.4.21.75
            ExplorEnz - The Enzyme Database: 3.4.21.75
            ERGO genome analysis and discovery system: 3.4.21.75
            BRENDA, the Enzyme Database: 3.4.21.75
            CAS: 141760-45-4
///
ENTRY       EC 3.4.21.76                Enzyme
NAME        myeloblastin;
            leukocyte proteinase 3;
            leukocyte proteinase 4;
            Wegener's granulomatosis autoantigen;
            proteinase PR-3;
            proteinase-3;
            PMNL proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins, including elastin, by preferential cleavage:
            -Ala! > -Val!
COMMENT     From polymorphonuclear leukocyte granules. In peptidase family S1
            (trypsin family). Not inhibited by secretory leukocyte proteinase
            inhibitor
REFERENCE   1  [PMID:1681549]
  AUTHORS   Labbaye C, Musette P, Cayre YE.
  TITLE     Wegener autoantigen and myeloblastin are encoded by a single mRNA.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 9253-6.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:2033050]
  AUTHORS   Rao NV, Wehner NG, Marshall BC, Gray WR, Gray BH, Hoidal JR.
  TITLE     Characterization of proteinase-3 (PR-3), a neutrophil serine
            proteinase. Structural and functional properties.
  JOURNAL   J. Biol. Chem. 266 (1991) 9540-8.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:1445363]
  AUTHORS   Brubaker MJ, Groutas WC, Hoidal JR, Rao NV.
  TITLE     Human neutrophil proteinase 3: mapping of the substrate binding site
            using peptidyl thiobenzyl esters.
  JOURNAL   Biochem. Biophys. Res. Commun. 188 (1992) 1318-24.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:1551417]
  AUTHORS   Kam CM, Kerrigan JE, Dolman KM, Goldschmeding R, Von dem Borne AE,
            Powers JC.
  TITLE     Substrate and inhibitor studies on proteinase 3.
  JOURNAL   FEBS. Lett. 297 (1992) 119-23.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01350  myeloblastin
GENES       HSA: 5657(PRTN3)
            MMU: 19152(Prtn3)
            RNO: 314615(Prtn3_predicted)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.76
            ExPASy - ENZYME nomenclature database: 3.4.21.76
            ExplorEnz - The Enzyme Database: 3.4.21.76
            ERGO genome analysis and discovery system: 3.4.21.76
            BRENDA, the Enzyme Database: 3.4.21.76
            CAS: 128028-50-2
///
ENTRY       EC 3.4.21.77                Enzyme
NAME        semenogelase;
            prostate-specific antigen;
            alpha-seminoprotein;
            seminin;
            P-30 antigen;
            antigen (human clone HPSA-1 prostate-specific protein moiety
            reduced);
            gamma-seminoglycoprotein (human protein moiety reduced);
            gamma-SM;
            antigen PSA (human prostate-specific);
            human glandular kallikrein;
            antigen PSA (human clone 5P1 protein moiety reduced)
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage: -Tyr!
COMMENT     A peptidase of family S1 (trypsin family) from seminal plasma.
            Slowly inhibited by alpha1-antichymotrypsin
REFERENCE   1  [PMID:2467258]
  AUTHORS   Digby M, Zhang XY, Richards RI.
  TITLE     Human prostate specific antigen (PSA) gene: structure and linkage to
            the kallikrein-like gene, hGK-1.
  JOURNAL   Nucleic. Acids. Res. 17 (1989) 2137.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:1702714]
  AUTHORS   Christensson A, Laurell CB, Lilja H.
  TITLE     Enzymatic activity of prostate-specific antigen and its reactions
            with extracellular serine proteinase inhibitors.
  JOURNAL   Eur. J. Biochem. 194 (1990) 755-63.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map05215  Prostate cancer
ORTHOLOGY   KO: K01351  semenogelase
GENES       HSA: 354(KLK3)
            PTR: 493182(KLK3)
            MCC: 719444(LOC719444)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.77
            ExPASy - ENZYME nomenclature database: 3.4.21.77
            ExplorEnz - The Enzyme Database: 3.4.21.77
            ERGO genome analysis and discovery system: 3.4.21.77
            BRENDA, the Enzyme Database: 3.4.21.77
            CAS: 110157-83-0
///
ENTRY       EC 3.4.21.78                Enzyme
NAME        granzyme A;
            CTLA3;
            HuTPS;
            T-cell associated protease 1;
            cytotoxic T lymphocyte serine protease;
            TSP-1;
            T-cell derived serine proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins, including fibronectin, type IV collagen and
            nucleolin. Preferential cleavage: -Arg!, -Lys! > > -Phe! in small
            molecule substrates
COMMENT     From cytotoxic T lymphocyte granules. In peptidase family S1
            (trypsin family). The human enzyme does not cleave Phe!-
REFERENCE   1  [PMID:3545816]
  AUTHORS   Simon MM, Hoschutzky H, Fruth U, Simon HG, Kramer MD.
  TITLE     Purification and characterization of a T cell specific serine
            proteinase (TSP-1) from cloned cytolytic T lymphocytes.
  JOURNAL   EMBO. J. 5 (1986) 3267-74.
  ORGANISM  ouse [GN:mmu]
REFERENCE   2  [PMID:3257574]
  AUTHORS   Gershenfeld HK, Hershberger RJ, Shows TB, Weissman IL.
  TITLE     Cloning and chromosomal assignment of a human cDNA encoding a T
            cell- and natural killer cell-specific trypsin-like serine protease.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 1184-8.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:1998680]
  AUTHORS   Odake S, Kam CM, Narasimhan L, Poe M, Blake JT, Krahenbuhl O,
            Tschopp J, Powers JC.
  TITLE     Human and murine cytotoxic T lymphocyte serine proteases: subsite
            mapping with peptide thioester substrates and inhibition of enzyme
            activity and cytolysis by isocoumarins.
  JOURNAL   Biochemistry. 30 (1991) 2217-27.
  ORGANISM  human [GN:hsa], ouse [GN:mmu]
PATHWAY     PATH: map04080  Neuroactive ligand-receptor interaction
ORTHOLOGY   KO: K01352  granzyme A
GENES       HSA: 3001(GZMA)
            PTR: 461873(GZMA)
            MMU: 14938(Gzma)
            RNO: 266708(Gzma)
            CFA: 487207(GZMA)
            BTA: 407178(gzmA) 539093(MGC157236)
            GGA: 395108(GZMA)
            XLA: 379554(MGC69002)
STRUCTURES  PDB: 1OP8  1ORF  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.78
            ExPASy - ENZYME nomenclature database: 3.4.21.78
            ExplorEnz - The Enzyme Database: 3.4.21.78
            ERGO genome analysis and discovery system: 3.4.21.78
            BRENDA, the Enzyme Database: 3.4.21.78
            CAS: 143180-73-8
///
ENTRY       EC 3.4.21.79                Enzyme
NAME        granzyme B;
            CTLA1;
            CCPII;
            cytotoxic cell proteinase-1;
            granzyme G;
            granzyme H;
            CCP1 proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage: -Asp! > > -Asn! > -Met!, -Ser!
COMMENT     From cytotoxic T lymphocyte granules. In peptidase family S1
            (trypsin family)
REFERENCE   1  [PMID:2953813]
  AUTHORS   Schmid J, Weissmann C.
  TITLE     Induction of mRNA for a serine protease and a
            beta-thromboglobulin-like protein in mitogen-stimulated human
            leukocytes.
  JOURNAL   J. Immunol. 139 (1987) 250-6.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:1998680]
  AUTHORS   Odake S, Kam CM, Narasimhan L, Poe M, Blake JT, Krahenbuhl O,
            Tschopp J, Powers JC.
  TITLE     Human and murine cytotoxic T lymphocyte serine proteases: subsite
            mapping with peptide thioester substrates and inhibition of enzyme
            activity and cytolysis by isocoumarins.
  JOURNAL   Biochemistry. 30 (1991) 2217-27.
  ORGANISM  human [GN:hsa], mouse [GN:mmu]
REFERENCE   3  [PMID:1985927]
  AUTHORS   Poe M, Blake JT, Boulton DA, Gammon M, Sigal NH, Wu JK, Zweerink HJ.
  TITLE     Human cytotoxic lymphocyte granzyme B. Its purification from
            granules and the characterization of substrate and inhibitor
            specificity.
  JOURNAL   J. Biol. Chem. 266 (1991) 98-103.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04650  Natural killer cell mediated cytotoxicity
            PATH: map04940  Type I diabetes mellitus
ORTHOLOGY   KO: K01353  granzyme B
GENES       HSA: 3002(GZMB)
            MMU: 14939(Gzmb)
            RNO: 171528(Gzmb)
            CFA: 490630(GZMB)
            BTA: 281731(GZMB) 508646(LOC508646)
STRUCTURES  PDB: 1FQ3  1IAU  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.79
            ExPASy - ENZYME nomenclature database: 3.4.21.79
            ExplorEnz - The Enzyme Database: 3.4.21.79
            ERGO genome analysis and discovery system: 3.4.21.79
            BRENDA, the Enzyme Database: 3.4.21.79
            CAS: 143180-74-9
///
ENTRY       EC 3.4.21.80                Enzyme
NAME        streptogrisin A;
            Streptomyces griseus protease A;
            protease A;
            proteinase A;
            Streptomyces griseus proteinase A;
            Streptomyces griseus serine proteinase 3;
            Streptomyces griseus serine proteinase A
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins with specificity similar to chymotrypsin
COMMENT     From Streptomyces griseus. A component of Pronase, in family S1
            (trypsin family). Not inhibited by Tos-Phe-CH2Cl or ovomucoid
REFERENCE   1  [PMID:5575653]
  AUTHORS   Johnson P, Smillie LB.
  TITLE     The disulfide bridge sequences of a serine protease of wide
            specificity from Streptomyces griseus.
  JOURNAL   Can. J. Biochem. 49 (1971) 548-62.
  ORGANISM  Streptomyces griseus
REFERENCE   2  [PMID:119870]
  AUTHORS   Sielecki AR, Hendrickson WA, Broughton CG, Delbaere LT, Brayer GD,
            James MN.
  TITLE     Protein structure refinement: Streptomyces griseus serine protease A
            at 1.8 A resolution.
  JOURNAL   J. Mol. Biol. 134 (1979) 781-804.
  ORGANISM  Streptomyces griseus
REFERENCE   3  [PMID:6783761]
  AUTHORS   James MN, Sielecki AR, Brayer GD, Delbaere LT, Bauer CA.
  TITLE     Structures of product and inhibitor complexes of Streptomyces
            griseus protease A at 1.8 A resolution. A model for serine protease
            catalysis.
  JOURNAL   J. Mol. Biol. 144 (1980) 43-88.
  ORGANISM  Streptomyces griseus
REFERENCE   4  [PMID:3892018]
  AUTHORS   Delbaere LT, Brayer GD.
  TITLE     The 1.8 A structure of the complex between chymostatin and
            Streptomyces griseus protease A. A model for serine protease
            catalytic tetrahedral intermediates.
  JOURNAL   J. Mol. Biol. 183 (1985) 89-103.
  ORGANISM  Streptomyces griseus
REFERENCE   5  [PMID:3112129]
  AUTHORS   Henderson G, Krygsman P, Liu CJ, Davey CC, Malek LT.
  TITLE     Characterization and structure of genes for proteases A and B from
            Streptomyces griseus.
  JOURNAL   J. Bacteriol. 169 (1987) 3778-84.
  ORGANISM  Streptomyces griseus
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.80
            ExPASy - ENZYME nomenclature database: 3.4.21.80
            ExplorEnz - The Enzyme Database: 3.4.21.80
            ERGO genome analysis and discovery system: 3.4.21.80
            BRENDA, the Enzyme Database: 3.4.21.80
            CAS: 55326-50-6
///
ENTRY       EC 3.4.21.81                Enzyme
NAME        streptogrisin B;
            Streptomyces griseus protease B;
            pronase B;
            serine proteinase B;
            Streptomyces griseus proteinase B;
            Streptomyces griseus proteinase 1;
            Streptomyces griseus serine proteinase B
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins with trypsin-like specificity
COMMENT     From Streptomyces griseus. A component of Pronase, in peptidase
            family S1 (trypsin family), distinct from Streptomyces trypsin
REFERENCE   1  [PMID:4899581]
  AUTHORS   Jurasek L, Fackre D, Smillie LB.
  TITLE     Remarkable homology about the disulfide bridges of a trypsin-like
            enzyme from Streptomyces griseus.
  JOURNAL   Biochem. Biophys. Res. Commun. 37 (1969) 99-105.
  ORGANISM  Streptomyces griseus
REFERENCE   2  [PMID:6750612]
  AUTHORS   Fujinaga M, Read RJ, Sielecki A, Ardelt W, Laskowski M Jr, James MN.
  TITLE     Refined crystal structure of the molecular complex of Streptomyces
            griseus protease B, a serine protease, with the third domain of the
            ovomucoid inhibitor from turkey.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 79 (1982) 4868-72.
  ORGANISM  Streptomyces griseus
REFERENCE   3  [PMID:6414511]
  AUTHORS   Read RJ, Fujinaga M, Sielecki AR, James MN.
  TITLE     Structure of the complex of Streptomyces griseus protease B and the
            third domain of the turkey ovomucoid inhibitor at 1.8-A resolution.
  JOURNAL   Biochemistry. 22 (1983) 4420-33.
  ORGANISM  Streptomyces griseus
REFERENCE   4  [PMID:3112129]
  AUTHORS   Henderson G, Krygsman P, Liu CJ, Davey CC, Malek LT.
  TITLE     Characterization and structure of genes for proteases A and B from
            Streptomyces griseus.
  JOURNAL   J. Bacteriol. 169 (1987) 3778-84.
  ORGANISM  Streptomyces griseus
REFERENCE   5  [PMID:2494344]
  AUTHORS   Greenblatt HM, Ryan CA, James MN.
  TITLE     Structure of the complex of Streptomyces griseus proteinase B and
            polypeptide chymotrypsin inhibitor-1 from Russet Burbank potato
            tubers at 2.1 A resolution.
  JOURNAL   J. Mol. Biol. 205 (1989) 201-28.
  ORGANISM  Streptomyces griseus
STRUCTURES  PDB: 1CSO  1CT0  1CT2  1CT4  1DS2  1SGD  1SGE  1SGN  1SGP  1SGQ  
                 1SGR  1SGY  2GKV  2NU0  2NU1  2NU2  2NU3  2NU4  2SGD  2SGE  
                 2SGF  2SGP  2SGQ  3SGQ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.81
            ExPASy - ENZYME nomenclature database: 3.4.21.81
            ExplorEnz - The Enzyme Database: 3.4.21.81
            ERGO genome analysis and discovery system: 3.4.21.81
            BRENDA, the Enzyme Database: 3.4.21.81
            CAS: 55071-87-9
///
ENTRY       EC 3.4.21.82                Enzyme
NAME        glutamyl endopeptidase II;
            GluSGP
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage: -Glu! > > -Asp! . Preference for Pro or Leu
            at P2 and Phe at P3. Cleavage of -Glu!Asp- and -Glu!Pro- bonds is
            slow
COMMENT     From Streptomyces griseus. A peptidase of family S1 (trypsin
            family). Inhibited by [Leu18->Glu]-modified turkey ovomucoid third
            domain
REFERENCE   1  [PMID:3149277]
  AUTHORS   Yoshida N, Tsuruyama S, Nagata K, Hirayama K, Noda K, Makisumi S.
  TITLE     Purification and characterization of an acidic amino acid specific
            endopeptidase of Streptomyces griseus obtained from a commercial
            preparation (Pronase).
  JOURNAL   J. Biochem. (Tokyo). 104 (1988) 451-6.
  ORGANISM  Streptomyces griseus
REFERENCE   2  [PMID:1674942]
  AUTHORS   Komiyama T, Bigler TL, Yoshida N, Noda K, Laskowski M Jr.
  TITLE     Replacement of P1 Leu18 by Glu18 in the reactive site of turkey
            ovomucoid third domain converts it into a strong inhibitor of
            Glu-specific Streptomyces griseus proteinase (GluSGP).
  JOURNAL   J. Biol. Chem. 266 (1991) 10727-30.
  ORGANISM  Streptomyces griseus
REFERENCE   3  [PMID:1794975]
  AUTHORS   Nagata K, Yoshida N, Ogata F, Araki M, Noda K.
  TITLE     Subsite mapping of an acidic amino acid-specific endopeptidase from
            Streptomyces griseus, GluSGP, and protease V8.
  JOURNAL   J. Biochem. (Tokyo). 110 (1991) 859-62.
  ORGANISM  Streptomyces griseus
REFERENCE   4  [PMID:1959600]
  AUTHORS   Svendsen I, Jensen MR, Breddam K.
  TITLE     The primary structure of the glutamic acid-specific protease of
            Streptomyces griseus.
  JOURNAL   FEBS. Lett. 292 (1991) 165-7.
  ORGANISM  Streptomyces griseus
REFERENCE   5  [PMID:1587264]
  AUTHORS   Breddam K, Meldal M.
  TITLE     Substrate preferences of glutamic-acid-specific endopeptidases
            assessed by synthetic peptide substrates based on intramolecular
            fluorescence quenching.
  JOURNAL   Eur. J. Biochem. 206 (1992) 103-7.
  ORGANISM  Streptomyces griseus, Staphyllococcus aureus, Bacillus licheniformis
STRUCTURES  PDB: 1HPG  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.82
            ExPASy - ENZYME nomenclature database: 3.4.21.82
            ExplorEnz - The Enzyme Database: 3.4.21.82
            ERGO genome analysis and discovery system: 3.4.21.82
            BRENDA, the Enzyme Database: 3.4.21.82
            CAS: 137010-42-5
///
ENTRY       EC 3.4.21.83                Enzyme
NAME        oligopeptidase B;
            protease II;
            Escherichia coli alkaline proteinase II;
            protease II
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of -Arg!, -Lys! bonds in oligopeptides, even when P1'
            residue is proline
COMMENT     Known from Escherichia coli. Inhibited by Tos-Lys-CH2Cl. In
            peptidase family S9 (prolyl oligopeptidase family)
REFERENCE   1  [PMID:1769955]
  AUTHORS   Kanatani A, Masuda T, Shimoda T, Misoka F, Lin XS, Yoshimoto T,
            Tsuru D.
  TITLE     Protease II from Escherichia coli: sequencing and expression of the
            enzyme gene and characterization of the expressed enzyme.
  JOURNAL   J. Biochem. (Tokyo). 110 (1991) 315-20.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01354  oligopeptidase B
GENES       ATH: AT1G50380
            OSA: 4342148
            TAN: TA08065
            TPV: TP04_0365
            TET: TTHERM_00243670
            TBR: Tb11.52.0003
            TCR: 503995.50 511557.10
            LMA: LmjF09.0770
            ECO: b1845(ptrB)
            ECJ: JW1834(ptrB)
            ECE: Z2896(ptrB)
            ECS: ECs2555
            ECC: c2255 c2256(ptrB)
            ECI: UTI89_C2047(ptrB)
            ECP: ECP_1789
            ECW: EcE24377A_2073(prtB)
            ECX: EcHS_A1936
            STY: STY2085(opdB)
            STT: t0998(opdB)
            SPT: SPA0990(opdB)
            SEC: SC1884(ptrB)
            STM: STM1879(ptrB)
            YPE: YPO1780(ptrB)
            YPK: y2527(ptrB)
            YPM: YP_1613(ptrB)
            YPA: YPA_1152
            YPN: YPN_2343
            YPP: YPDSF_1343
            YPS: YPTB1656(ptrB)
            YPI: YpsIP31758_2346(ptrB)
            SFL: SF1856(ptrB)
            SFX: S1921(ptrB)
            SFV: SFV_1847(ptrB)
            SSN: SSON_1303(ptrB)
            SDY: SDY_1131(ptrB)
            ECA: ECA2476(ptrB)
            PLU: plu2716(ptrB)
            SGL: SG1273
            ENT: Ent638_2416
            SPE: Spro_1937 Spro_3467
            XFA: XF1479
            XFT: PD0696(ptrB)
            XCC: XCC3502(ptrB)
            XCB: XC_0659
            XCV: XCV0687(ptrB)
            XAC: XAC0631(ptrB)
            XOO: XOO3999(ptrB)
            XOM: XOO_3770(XOO3770)
            VCH: VCA0063
            VCO: VC0395_0075(ptrB)
            VVU: VV2_1548
            VVY: VVA0361
            VPA: VPA0167 VPA1467
            VFI: VFA0333
            PPR: PBPRB0979
            PAE: PA1304
            PPU: PP_4583
            PPF: Pput_1306
            PST: PSPTO_3911
            PSB: Psyr_1574
            PSP: PSPPH_1558
            PFL: PFL_1507
            PFO: Pfl_1399
            PEN: PSEEN4025
            PMY: Pmen_1781
            SON: SO_0144(ptrB)
            SAZ: Sama_0144
            SBL: Sbal_4218
            SBM: Shew185_0135
            SLO: Shew_0039
            SPC: Sputcn32_0135
            SSE: Ssed_4371
            SPL: Spea_0132
            SHE: Shewmr4_0136
            SHM: Shewmr7_0130
            SHN: Shewana3_0135
            SHW: Sputw3181_3937
            ILO: IL0074(ptrB)
            CPS: CPS_3026(ptrB1) CPS_4644(ptrB2)
            PHA: PSHAa0069(ptrB) PSHAa2955(ptrB)
            PIN: Ping_0633
            AEH: Mlg_1577
            HHA: Hhal_1376
            CSA: Csal_1464
            AHA: AHA_0348 AHA_1662
            BBA: Bd3175(ptrB)
            RPR: RP281
            RTY: RT0272(ptrB)
            RCO: RC0377(ptrB)
            RFE: RF_0454(ptrB)
            RBE: RBE_1023 RBE_1024
            OTS: OTBS_0350(ptrB)
            PUB: SAR11_0180(ptrB)
            MLO: mll7643
            MES: Meso_0862
            PLA: Plav_0844
            SME: SMc00114(ptrB)
            SMD: Smed_0599
            ATU: Atu0897(ptrB)
            ATC: AGR_C_1636
            RET: RHE_CH01226(ptrB)
            RLE: RL1360(ptrB)
            BME: BMEI1365
            BMF: BAB1_0593
            BMS: BR0568(ptrB)
            BMB: BruAb1_0590(ptrB)
            BOV: BOV_0569(ptrB)
            OAN: Oant_2691
            BJA: blr0376(ptrB)
            BRA: BRADO6986
            BBT: BBta_0542
            RPA: RPA1570
            RPB: RPB_3959
            RPC: RPC_1332
            RPD: RPD_3717
            RPE: RPE_1366
            NWI: Nwi_2471
            NHA: Nham_2902
            BHE: BH04620(ptrB)
            BQU: BQ03810(ptrB)
            XAU: Xaut_2839
            CCR: CC_0936
            MMR: Mmar10_0878
            HNE: HNE_2146(ptrB)
            ZMO: ZMO0490(ptrB)
            NAR: Saro_0437
            SAL: Sala_2995
            SWI: Swit_1423
            ELI: ELI_11895
            GOX: GOX0727
            ACR: Acry_2766
            ABA: Acid345_2328
            SUS: Acid_3709
            SPN: SP_1343
            SPR: spr1204(ptrB)
            MTU: Rv0781(ptrBa) Rv0782(ptrBb)
            MTC: MT0805(ptrB)
            MBO: Mb0804(ptrB)
            MBB: BCG_0833(ptrB)
            MLE: ML2226(ptrB)
            MPA: MAP0615(ptrBa)
            MAV: MAV_0727
            MSM: MSMEG_5839
            MVA: Mvan_5137
            MGI: Mflv_1617
            MMC: Mmcs_4559
            MKM: Mkms_4647
            MJL: Mjls_4942
            CGL: NCgl2507(cgl2596)
            CGB: cg2873(ptrB)
            CEF: CE2486
            CDI: DIP1926
            CJK: jk0351(ptrB)
            NFA: nfa5630
            RHA: RHA1_ro04818
            TWH: TWT493(ptrB)
            TWS: TW269(ptrB)
            LXX: Lxx02110(ptrB)
            CMI: CMM_2114(ptrB)
            ART: Arth_3230
            NCA: Noca_2979
            STP: Strop_4105
            BLO: BL1219(ptrB)
            BAD: BAD_1342(ptrB)
            TDE: TDE2140(ptrB)
            GVI: glr0129
            ANA: alr3911
            AVA: Ava_1786
            GFO: GFO_1795(ptrB)
            FJO: Fjoh_2556
            FPS: FP0870(ptrB)
            RRS: RoseRS_1579
            RCA: Rcas_2641
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.83
            ExPASy - ENZYME nomenclature database: 3.4.21.83
            ExplorEnz - The Enzyme Database: 3.4.21.83
            ERGO genome analysis and discovery system: 3.4.21.83
            BRENDA, the Enzyme Database: 3.4.21.83
            CAS: 57657-67-7
///
ENTRY       EC 3.4.21.84                Enzyme
NAME        limulus clotting factor _overbar_C_;
            factor C;
            limulus factor C
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage of -Arg103!Ser- and -Ile124!Ile- bonds in limulus
            clotting factor B to form factor _overbar_B_. Cleavage of -Pro-Arg!
            bonds in synthetic substrates
COMMENT     From the hemocyte granules of the horseshoe crabs Limulus and
            Tachypleus. Factor C is activated by Gram-negative bacterial
            lipopolysaccharides and chymotrypsin. Inhibited by antithrombin III.
            In peptidase family S1 (trypsin family)
REFERENCE   1  [PMID:3512266]
  AUTHORS   Nakamura T, Morita T, Iwanaga S.
  TITLE     Lipopolysaccharide-sensitive serine-protease zymogen (factor C)
            found in Limulus hemocytes. Isolation and characterization.
  JOURNAL   Eur. J. Biochem. 154 (1986) 511-21.
  ORGANISM  Limulus polyphemus, Tachypleus tridentatus
REFERENCE   2  [PMID:2007602]
  AUTHORS   Muta T, Miyata T, Misumi Y, Tokunaga F, Nakamura T, Toh Y, Ikehara
            Y, Iwanaga S.
  TITLE     Limulus factor C. An endotoxin-sensitive serine protease zymogen
            with a mosaic structure of complement-like, epidermal growth
            factor-like, and lectin-like domains.
  JOURNAL   J. Biol. Chem. 266 (1991) 6554-61.
  ORGANISM  Limulus sp.
REFERENCE   3  [PMID:2016264]
  AUTHORS   Tokunaga F, Nakajima H, Iwanaga S.
  TITLE     Further studies on lipopolysaccharide-sensitive serine protease
            zymogen (factor C): its isolation from Limulus polyphemus hemocytes
            and identification as an intracellular zymogen activated by
            alpha-chymotrypsin, not by trypsin.
  JOURNAL   J. Biochem. (Tokyo). 109 (1991) 150-7.
  ORGANISM  Limulus polyphemus, Tachypleus tridentatus
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.84
            ExPASy - ENZYME nomenclature database: 3.4.21.84
            ExplorEnz - The Enzyme Database: 3.4.21.84
            ERGO genome analysis and discovery system: 3.4.21.84
            BRENDA, the Enzyme Database: 3.4.21.84
            CAS: 115743-27-6
///
ENTRY       EC 3.4.21.85                Enzyme
NAME        limulus clotting factor _overbar_B_
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage of -Arg98!Ile- bond in limulus proclotting enzyme
            to form active clotting enzyme
COMMENT     From the hemocyte granules of the horseshoe crabs Limulus and
            Tachypleus. Factor B is activated by limulus clotting factor
            _overbar_C_. In peptidase family S1 (trypsin family)
REFERENCE   1  [PMID:3519594]
  AUTHORS   Nakamura T, Horiuchi T, Morita T, Iwanaga S.
  TITLE     Purification and properties of intracellular clotting factor, factor
            B, from horseshoe crab (Tachypleus tridentatus) hemocytes.
  JOURNAL   J. Biochem. (Tokyo). 99 (1986) 847-57.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.85
            ExPASy - ENZYME nomenclature database: 3.4.21.85
            ExplorEnz - The Enzyme Database: 3.4.21.85
            ERGO genome analysis and discovery system: 3.4.21.85
            BRENDA, the Enzyme Database: 3.4.21.85
            CAS: 848851-53-6
///
ENTRY       EC 3.4.21.86                Enzyme
NAME        limulus clotting enzyme;
            clotting enzyme
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage of -Arg18! and -Arg47! bonds in coagulogen to
            form coagulin and fragments
COMMENT     From the hemocyte granules of horseshoe crabs Limulus and
            Tachypleus. Proclotting enzyme is activated by limulus clotting
            factor . In peptidase family S1 (trypsin family)
REFERENCE   1  [PMID:2266134]
  AUTHORS   Muta T, Hashimoto R, Miyata T, Nishimura H, Toh Y, Iwanaga S.
  TITLE     Proclotting enzyme from horseshoe crab hemocytes. cDNA cloning,
            disulfide locations, and subcellular localization.
  JOURNAL   J. Biol. Chem. 265 (1990) 22426-33.
  ORGANISM  Tachypleus tridentatus
REFERENCE   2  [PMID:2016264]
  AUTHORS   Tokunaga F, Nakajima H, Iwanaga S.
  TITLE     Further studies on lipopolysaccharide-sensitive serine protease
            zymogen (factor C): its isolation from Limulus polyphemus hemocytes
            and identification as an intracellular zymogen activated by
            alpha-chymotrypsin, not by trypsin.
  JOURNAL   J. Biochem. (Tokyo). 109 (1991) 150-7.
  ORGANISM  Limulus polyphemus, Tachypleus tridentatus
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.86
            ExPASy - ENZYME nomenclature database: 3.4.21.86
            ExplorEnz - The Enzyme Database: 3.4.21.86
            ERGO genome analysis and discovery system: 3.4.21.86
            BRENDA, the Enzyme Database: 3.4.21.86
///
ENTRY       EC 3.4.21.87      Obsolete  Enzyme
NAME        Transferred to 3.4.23.49
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
COMMENT     Transferred entry: now EC 3.4.23.49, omptin. The enzyme is not a
            serine protease, as thought previously, but an aspartate protease.
            (EC 3.4.21.87 created 1993, deleted 2006)
STRUCTURES  PDB: 1I78  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.87
            ExPASy - ENZYME nomenclature database: 3.4.21.87
            ExplorEnz - The Enzyme Database: 3.4.21.87
            ERGO genome analysis and discovery system: 3.4.21.87
            BRENDA, the Enzyme Database: 3.4.21.87
///
ENTRY       EC 3.4.21.88                Enzyme
NAME        repressor LexA;
            LexA repressor
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of Ala84!Gly bond in repressor LexA
COMMENT     RecA protein and single-stranded DNA are required for activity,
            which is attributed to a Ser/Lys dyad [2]. The LexA protein
            represses the SOS regulon, which regulates the genes involved in DNA
            repair. In the presence of single-stranded DNA, the RecA protein
            interacts with repressor LexA, causing it to undergo an
            autocatalytic cleavage which disrupts the DNA-binding part of the
            repressor, and inactivates it. The consequent derepression of the
            SOS regulon leads to DNA repair. This peptidase activity of LexA was
            previously attributed to the RecA protein. Type example of peptidase
            family S24
REFERENCE   1  [PMID:7013987]
  AUTHORS   Horii T, Ogawa T, Ogawa H.
  TITLE     Nucleotide sequence of the lexA gene of E. coli.
  JOURNAL   Cell. 23 (1981) 689-97.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:3108885]
  AUTHORS   Slilaty SN, Little JW.
  TITLE     Lysine-156 and serine-119 are required for LexA repressor cleavage:
            a possible mechanism.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 3987-91.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:8513500]
  AUTHORS   Kim B, Little JW.
  TITLE     LexA and lambda Cl repressors as enzymes: specific cleavage in an
            intermolecular reaction.
  JOURNAL   Cell. 73 (1993) 1165-73.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:7845214]
  AUTHORS   Little JW, Kim B, Roland KL, Smith MH, Lin LL, Slilaty SN.
  TITLE     Cleavage of LexA repressor.
  JOURNAL   Methods. Enzymol. 244 (1994) 266-84.
ORTHOLOGY   KO: K01356  repressor LexA
GENES       ECO: b4043(lexA)
            ECJ: JW4003(lexA)
            ECE: Z5642(lexA)
            ECS: ECs5026
            ECC: c5014(lexA)
            ECI: UTI89_C4613(lexA)
            ECP: ECP_4261
            ECV: APECO1_2426(lexA)
            ECW: EcE24377A_4596(lexA)
            ECX: EcHS_A4283(lexA)
            STY: STY4433(lexA)
            STT: t4143(lexA)
            SPT: SPA4054(lexA)
            SEC: SC4116(lexA)
            STM: STM4237(lexA)
            YPE: YPO0314(lexA)
            YPK: y0572(lexA)
            YPM: YP_0470(lexA1)
            YPA: YPA_3970
            YPN: YPN_3355
            YPP: YPDSF_3657
            YPS: YPTB0370(lexA)
            YPI: YpsIP31758_3770(lexA)
            SFL: SF4162(lexA)
            SFX: S3569(lexA)
            SFV: SFV_4170(lexA)
            SSN: SSON_4223(lexA)
            SBO: SBO_4074(lexA)
            SDY: SDY_4531(lexA)
            ECA: ECA0630(lexA)
            PLU: plu4374(lexA)
            SGL: SG2141
            ENT: Ent638_0247
            SPE: Spro_4460
            HIN: HI0749(lexA)
            HIT: NTHI0905(lexA)
            HIP: CGSHiEE_08360
            HIQ: CGSHiGG_07240
            HDU: HD0545(lexA)
            HSO: HS_0386(lexA)
            PMU: PM1181(lexA)
            MSU: MS0744(lexA)
            APL: APL_1108(lexA)
            ASU: Asuc_0877
            XFA: XF0122
            XFT: PD0092(lexA)
            XCC: XCC1098(lexA) XCC1721(lexA)
            XCB: XC_2510(lexA) XC_3151
            XCV: XCV1223(lexA1) XCV1772(lexA2)
            XAC: XAC1196(lexA) XAC1739(lexA)
            XOO: XOO2942(lexA) XOO3442(lexA)
            XOM: XOO_2794(XOO2794) XOO_3242(XOO3242)
            VCH: VC0092
            VCO: VC0395_A2423(lexA)
            VVU: VV1_1166
            VVY: VV0123
            VPA: VP2945
            VFI: VF2442
            PPR: PBPRA0165
            PAE: PA3007(lexA)
            PAU: PA14_25160(lexA)
            PAP: PSPA7_2152(lexA)
            PPU: PP_2143(lexA-1) PP_3116(lexA-2)
            PPF: Pput_2601 Pput_3599
            PST: PSPTO_2792(lexA-1) PSPTO_3510(lexA-2)
            PSB: Psyr_2520 Psyr_3283
            PSP: PSPPH_2677(lexA1) PSPPH_3203(lexA2)
            PFL: PFL_1949(lexA) PFL_3700(lexA)
            PFO: Pfl_3152 Pfl_3872(lexA)
            PEN: PSEEN2412 PSEEN3721(lexA)
            PMY: Pmen_1587
            SON: SO_4603(lexA)
            SDN: Sden_3515
            SFR: Sfri_0260
            SAZ: Sama_3481
            SBL: Sbal_0156
            SBM: Shew185_4178
            SLO: Shew_0127
            SPC: Sputcn32_3780
            SSE: Ssed_0200
            SPL: Spea_3997
            SHE: Shewmr4_3789
            SHM: Shewmr7_3862
            SHN: Shewana3_3989
            SHW: Sputw3181_0135
            ILO: IL0262(lexA)
            CPS: CPS_0237(lexA)
            PHA: PSHAa2873(lexA)
            PAT: Patl_4247
            SDE: Sde_1787
            PIN: Ping_0108
            MAQ: Maqu_2007
            LPP: lpp1039
            MCA: MCA2167(lexA)
            TCX: Tcr_1234
            AEH: Mlg_1096
            HHA: Hhal_1741
            HCH: HCH_02068(lexA)
            CSA: Csal_0696 Csal_2070
            ABO: ABO_1009(lexA)
            MMW: Mmwyl1_2117
            AHA: AHA_0183(lexA)
            CVI: CV_2332(umuD)
            RSO: RSc1304(lexA)
            REU: Reut_A2008
            REH: H16_A2281(lexA)
            RME: Rmet_1981
            BMA: BMA1211(lexA)
            BMV: BMASAVP1_A1699(lexA)
            BML: BMA10299_A0356(lexA)
            BMN: BMA10247_0805(lexA)
            BXE: Bxe_A2471
            BVI: Bcep1808_1552
            BUR: Bcep18194_A4738
            BCN: Bcen_1120
            BCH: Bcen2424_1600
            BAM: Bamb_1496
            BPS: BPSL1840(lexA)
            BPM: BURPS1710b_2012(lexA)
            BPL: BURPS1106A_1859(lexA)
            BPD: BURPS668_1845(lexA)
            BTE: BTH_I2481(lexA)
            PNU: Pnuc_0418
            BPE: BP1794(lexA)
            BPA: BPP2023(lexA)
            BBR: BB2271(lexA)
            RFR: Rfer_2994
            POL: Bpro_2954
            PNA: Pnap_1918
            AAV: Aave_2558
            AJS: Ajs_2310
            VEI: Veis_4912
            MPT: Mpe_A1866
            HAR: HEAR2163(lexA)
            MMS: mma_1300(lexA)
            EBA: ebA3086(lexA)
            AZO: azo2064(lexA)
            DAR: Daro_1939
            TBD: Tbd_1483
            MFA: Mfla_1781
            HPA: HPAG1_0151
            GSU: GSU0041(lexA-1) GSU1617(lexA-2)
            GME: Gmet_1439
            GUR: Gura_1142
            PCA: Pcar_1739
            PPD: Ppro_0192 Ppro_1572 Ppro_1901
            DDE: Dde_0893 Dde_1932
            BBA: Bd3511(lexA)
            ADE: Adeh_1701
            AFW: Anae109_2104
            MXA: MXAN_4446(lexA)
            SFU: Sfum_0927 Sfum_3779
            RBE: RBE_0006(lexA)
            PUB: SAR11_0921(lexA)
            MLO: mlr0626
            MES: Meso_1642
            PLA: Plav_3178
            SME: SMc01183(lexA)
            SMD: Smed_1353
            ATU: Atu1395(lexA)
            ATC: AGR_C_2577(lexA)
            RET: RHE_CH01928(lexA)
            RLE: RL2236(lexA)
            BME: BMEI0840
            BMF: BAB1_1167(lexA)
            BMS: BR1144(lexA)
            BMB: BruAb1_1150(lexA)
            BOV: BOV_1104(lexA)
            OAN: Oant_2045
            BJA: blr4826(lexA)
            BRA: BRADO4120(lexA) BRADO5340
            BBT: BBta_4496(lexA) BBta_5832
            RPA: RPA2903(lexA)
            RPB: RPB_2809
            RPC: RPC_2454
            RPD: RPD_2839
            RPE: RPE_2571
            NWI: Nwi_1841
            NHA: Nham_1729
            BHE: BH08420(lexA)
            BQU: BQ06160(lexA)
            XAU: Xaut_4371
            CCR: CC_1902(lexA)
            SIL: SPO2154(lexA)
            SIT: TM1040_1135
            RSP: RSP_1997(lexA)
            RSH: Rsph17029_0707
            RSQ: Rsph17025_3094
            JAN: Jann_1874
            RDE: RD1_3216(lexA)
            PDE: Pden_2142
            MMR: Mmar10_1398
            HNE: HNE_1786(lexA)
            ZMO: ZMO0199(lexA)
            NAR: Saro_2029
            SAL: Sala_0832
            SWI: Swit_3216
            ELI: ELI_06530
            GOX: GOX2276
            GBE: GbCGDNIH1_0816
            ACR: Acry_2883
            RRU: Rru_A1898
            MAG: amb2866
            MGM: Mmc1_2084
            ABA: Acid345_0581
            SUS: Acid_1496
            BSU: BG10678(lexA)
            BHA: BH2356(lexA)
            BAN: BA3754(lexA)
            BAR: GBAA3754(lexA)
            BAA: BA_4235
            BAT: BAS3479
            BCE: BC3690 BC3704 BCp0006
            BCA: BCE_3727(lexA)
            BCZ: BCZK3395(lexA)
            BCY: Bcer98_2344
            BTK: BT9727_3444(lexA)
            BLI: BL00127(lexA)
            BLD: BLi02032(lexA)
            BCL: ABC2167(lexA)
            BAY: RBAM_017650(lexA)
            OIH: OB1669(lexA)
            GKA: GK1328
            SAU: SA1174(lexA)
            SAV: SAV1339(lexA)
            SAM: MW1226(lexA)
            SAR: SAR1349(dinR)
            SAS: SAS1279
            SAC: SACOL1374(lexA)
            SAB: SAB1197c(dinR)
            SAA: SAUSA300_1237(lexA)
            SAO: SAOUHSC_01333
            SAJ: SaurJH9_1400
            SAH: SaurJH1_1427
            SEP: SE1022
            SER: SERP0909(lexA)
            SHA: SH1568(lexA)
            SSP: SSP1418
            LMO: lmo1302
            LMF: LMOf2365_1320(lexA)
            LIN: lin1340
            LWE: lwe1317(lexA)
            LPL: lp_2063(lexA)
            LJO: LJ1508
            LAC: LBA1280(lexA)
            LSA: LSA1275(lexA)
            LSL: LSL_0540(lexA)
            LDB: Ldb1356(lexA)
            LBU: LBUL_1265
            LCA: LSEI_0730
            LGA: LGAS_0793
            LRE: Lreu_0677
            PPE: PEPE_0870
            EFA: EF1579(lexA)
            OOE: OEOE_0970
            LME: LEUM_1204
            STH: STH1736(lexA)
            CAC: CAC1832(lexA)
            CPE: CPE1161(lexA)
            CPF: CPF_1364(lexA)
            CPR: CPR_1177(lexA)
            CTC: CTC01298(lexA)
            CNO: NT01CX_2111(lexA)
            CTH: Cthe_0773
            CDF: CD1931(dinR)
            CBO: CBO1795(dinR)
            CBA: CLB_1729(lexA)
            CBH: CLC_1737(lexA)
            CBF: CLI_1789(lexA)
            CBE: Cbei_2561 Cbei_2575
            CKL: CKL_1579(lexA)
            AMT: Amet_2535
            CHY: CHY_1378(lexA)
            DSY: DSY1577
            DRM: Dred_1873
            SWO: Swol_1008
            CSC: Csac_2042
            MTA: Moth_1120
            MTU: Rv2720(lexA)
            MTC: MT2793(lexA)
            MBO: Mb2739(lexA)
            MBB: BCG_2733(lexA)
            MLE: ML1003(lexA)
            MPA: MAP2836(lexA)
            MAV: MAV_3614(lexA)
            MSM: MSMEG_2740(lexA)
            MVA: Mvan_2441
            MGI: Mflv_3956
            MMC: Mmcs_2168
            MKM: Mkms_2214
            MJL: Mjls_2157
            CGL: NCgl1855(cgl1930)
            CGB: cg2114(lexA) cg2141(recA)
            CEF: CE1823
            CDI: DIP1426(lexA)
            CJK: jk1106(lexA)
            NFA: nfa38000(lexA) nfa52180
            RHA: RHA1_ro00572 RHA1_ro06788
            SCO: SCO5803(lexA)
            SMA: SAV2463(lexA)
            LXX: Lxx15880(lexA)
            CMI: CMM_2018(lexA)
            ART: Arth_1468
            AAU: AAur_1602(lexA)
            PAC: PPA1023
            NCA: Noca_3817
            TFU: Tfu_2152
            FRA: Francci3_3510
            FAL: FRAAL5703(lexA)
            ACE: Acel_1479
            KRA: Krad_1506
            SEN: SACE_1736(recA) SACE_1760 SACE_2836(lexA)
            STP: Strop_1451
            BLO: BL1310(lexA)
            BAD: BAD_1115(lexA)
            FNU: FN1589
            RBA: RB7437(lexA)
            PCU: pc1269(lexA)
            LIL: LA1447(lexA)
            LIC: LIC12305(lexA)
            LBJ: LBJ_1985(lexA)
            LBL: LBL_1071(lexA)
            SYN: sll1626(lexA)
            SYW: SYNW1582
            SYD: Syncc9605_0929
            SYE: Syncc9902_1481
            SYG: sync_0831(lexA)
            SYR: SynRCC307_1756(lexA)
            SYX: SynWH7803_1680(lexA)
            GVI: gll0709
            ANA: alr4908(lexA)
            AVA: Ava_2198
            PMA: Pro1336(lexA)
            PMM: PMM1262(lexA)
            PMT: PMT0380
            PMN: PMN2A_0828
            PMI: PMT9312_1356
            PMB: A9601_14611(lexA)
            PMC: P9515_14231(lexA)
            PMF: P9303_19141(lexA)
            PMG: P9301_14471(lexA)
            PMH: P9215_14871(lexA)
            PME: NATL1_16801(lexA)
            SRU: SRU_0551 SRU_1177(lexA)
            DET: DET1640(lexA)
            DEH: cbdb_A1740(lexA)
            DEB: DehaBAV1_1384
            RRS: RoseRS_0427
            RCA: Rcas_1071
            DRA: DR_A0344
            TMA: TM1082
            TPT: Tpet_1662
            TME: Tmel_1184
            FNO: Fnod_0793
STRUCTURES  PDB: 1JHC  1JHE  1JHF  1JHH  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.88
            ExPASy - ENZYME nomenclature database: 3.4.21.88
            ExplorEnz - The Enzyme Database: 3.4.21.88
            ERGO genome analysis and discovery system: 3.4.21.88
            BRENDA, the Enzyme Database: 3.4.21.88
            CAS: 84721-00-6
///
ENTRY       EC 3.4.21.89                Enzyme
NAME        signal peptidase I;
            leader peptidase I;
            signal proteinase;
            Escherichia coli leader peptidase;
            eukaryotic signal peptidase;
            eukaryotic signal proteinase;
            leader peptidase;
            leader peptide hydrolase;
            leader proteinase;
            signal peptidase;
            pilin leader peptidase;
            SPC;
            prokaryotic signal peptidase;
            prokaryotic leader peptidase;
            HOSP;
            prokaryotic signal proteinase;
            propeptidase;
            PuIO prepilin peptidase;
            signal peptide hydrolase;
            signal peptide peptidase;
            signalase;
            bacterial leader peptidase 1;
            pilin leader peptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Cleavage of hydrophobic, N-terminal signal or leader sequences from
            secreted and periplasmic proteins
COMMENT     Present in the inner membrane of Escherichia coli. Unaffected by
            inhibitors of most serine peptidases, but site-directed mutagenesis
            implicates a Ser/Lys catalytic dyad in activity [1,3]. Hydrolyses a
            single bond -Ala!Ala- in M13 phage procoat protein, producing free
            signal peptide and coat protein. Formerly included in EC 3.4.99.36.
            Eukaryote signal peptidases that may have somewhat different
            specificity are known from the endoplasmic reticulum membrane [4]
            and mitochondrial inner membrane [2]. Type example of peptidase
            family S26
REFERENCE   1  [PMID:8394311]
  AUTHORS   Black MT.
  TITLE     Evidence that the catalytic activity of prokaryote leader peptidase
            depends upon the operation of a serine-lysine catalytic dyad.
  JOURNAL   J. Bacteriol. 175 (1993) 4957-61.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Nunnari, J., Fox, T.D. and Walter, P.
  TITLE     A mitochondrial protease with two catalytic subunits of
            nonoverlapping specificities.
  JOURNAL   Science 262 (1993) 1997-2004.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:8262975]
  AUTHORS   Tschantz WR, Sung M, Delgado-Partin VM, Dalbey RE.
  TITLE     A serine and a lysine residue implicated in the catalytic mechanism
            of the Escherichia coli leader peptidase.
  JOURNAL   J. Biol. Chem. 268 (1993) 27349-54.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:7845216]
  AUTHORS   Lively MO, Newsome AL, Nusier M.
  TITLE     Eukaryote microsomal signal peptidases.
  JOURNAL   Methods. Enzymol. 244 (1994) 301-14.
REFERENCE   5  [PMID:7845215]
  AUTHORS   Tschantz WR, Dalbey RE.
  TITLE     Bacterial leader peptidase 1.
  JOURNAL   Methods. Enzymol. 244 (1994) 285-301.
ORTHOLOGY   KO: K03100  signal peptidase I
GENES       HSA: 157708(SEC11B) 23478(SEC11A) 90701(SEC11C)
            PTR: 453607(SEC11A)
            MMU: 56529(Sec11a) 66286(Sec11c)
            RNO: 266758(Sec11l3) 65166(Sec11l1)
            CFA: 404003(SEC11C) 404004(SEC11A)
            BTA: 282078(SPC18)
            GGA: 415334(SEC11A) 426850(SEC11C)
            XLA: 379448(MGC64284) 447023(MGC82823)
            XTR: 394740(MGC76332) 448712(sec11c)
            SPU: 581228(LOC581228)
            DME: Dmel_CG2358(Spase18-21)
            CEL: Y54E10BR.5
            ATH: AT1G06870 AT1G52600 AT2G30440 AT3G15710 AT3G24590
            OSA: 4328965 4334222 4338334 4340738
            CME: CMS130C
            SCE: YIR022W(SEC11)
            AGO: AGOS_ADR158W
            PIC: PICST_36729(SEC11)
            CAL: CaO19_3259(CaO19.3259)
            CGR: CAGL0F06721g
            SPO: SPBC1685.03
            ANI: AN3126.2
            AFM: AFUA_3G12840
            AOR: AO090012000838
            CNE: CNJ00480
            UMA: UM00481.1
            ECU: ECU02_0760
            DDI: DDBDRAFT_0167012
            PFA: MAL13P1.167
            TAN: TA18300
            TPV: TP03_0804
            TET: TTHERM_01093560
            TBR: Tb927.5.3220
            TCR: 507809.74
            LMA: LmjF08.0450
            EHI: 92.t00019
            ECO: b2568(lepB)
            ECJ: JW2552(lepB)
            ECE: Z3850(lepB)
            ECS: ECs3434
            ECC: c3092(lepB)
            ECI: UTI89_C2890(lepB)
            ECP: ECP_2570
            ECV: APECO1_3963(lepB)
            ECW: EcE24377A_2854(lepB)
            ECX: EcHS_A2723(lepB)
            STY: STY2828(lepB)
            STT: t0275(lepB)
            SPT: SPA0283(lepB)
            SEC: SC2577(lepB)
            STM: STM2582(lepB)
            YPE: YPO2717(lepB)
            YPK: y1296(lepB)
            YPM: YP_2521(lepB)
            YPA: YPA_2451
            YPN: YPN_1205
            YPP: YPDSF_1554
            YPS: YPTB2891(lepB)
            YPI: YpsIP31758_1135(lepB)
            YEN: YE1016(lepB)
            SFL: SF2630(lepB)
            SFX: S2803(lepB)
            SFV: SFV_2631(lepB)
            SSN: SSON_2692(lepB)
            SBO: SBO_2596(lepB)
            SDY: SDY_2809(lepB)
            ECA: ECA3279(lepB)
            PLU: plu3341(lepB)
            BUC: BU259(lepB)
            BAS: BUsg250(lepB)
            BAB: bbp240(lepB)
            BCC: BCc_164(lepB)
            WBR: WGLp195(lepB)
            SGL: SG1788
            ENT: Ent638_3055
            SPE: Spro_3670
            BFL: Bfl541(lepB)
            BPN: BPEN_561(lepB)
            HIN: HI0015(lepB)
            HIT: NTHI0020(lepB)
            HDU: HD1607(lepB)
            HSO: HS_1241(lepB)
            PMU: PM0062(lepB)
            MSU: MS0370(lepB)
            APL: APL_0542(lepB)
            ASU: Asuc_0579
            XFA: XF2244
            XFT: PD1288(lepB)
            XCC: XCC1271(lepB)
            XCB: XC_2970
            XCV: XCV1374(lepB)
            XAC: XAC1323(lepB)
            XOO: XOO1853(lepB)
            XOM: XOO_1749(XOO1749)
            VCH: VC2462
            VCO: VC0395_A2040(lepB)
            VVU: VV1_1564
            VVY: VV2832
            VPA: VP2573
            VFI: VF2088
            PPR: PBPRA3090
            PAE: PA0768(lepB) PA1303
            PAU: PA14_54350(lepB)
            PAP: PSPA7_4088(lepB2) PSPA7_4751(lepB1)
            PPU: PP_1432(lepB)
            PPF: Pput_4289
            PST: PSPTO_4219(lepB)
            PSB: Psyr_3953
            PSP: PSPPH_3950(lepB)
            PFL: PFL_1070(lepB)
            PFO: Pfl_0993
            PEN: PSEEN4291(lepB)
            PMY: Pmen_1473
            PAR: Psyc_0331(lepB)
            PCR: Pcryo_0365
            PRW: PsycPRwf_0373
            ACI: ACIAD2583(lepB)
            SON: SO_1347(lepB) SO_2924
            SDN: Sden_2462 Sden_2767
            SFR: Sfri_2930
            SAZ: Sama_0879
            SBL: Sbal_1200 Sbal_2685
            SBM: Shew185_1244 Shew185_1516 Shew185_2706
            SLO: Shew_0362 Shew_1053
            SPC: Sputcn32_1158
            SSE: Ssed_1147
            SPL: Spea_0134 Spea_1036
            SHE: Shewmr4_1481 Shewmr4_2849
            SHM: Shewmr7_1546 Shewmr7_2931
            SHN: Shewana3_1540 Shewana3_3027
            SHW: Sputw3181_3006
            ILO: IL0811(lepB)
            CPS: CPS_0009(lepB1) CPS_1803(lepB2) CPS_4123(lepB3)
            PHA: PSHAa0731(lepB) PSHAa1310
            PAT: Patl_2309 Patl_3150
            SDE: Sde_0576 Sde_2245
            PIN: Ping_0639
            MAQ: Maqu_2247
            CBU: CBU_1099(lepB-1) CBU_1504(lepB-2)
            CBD: COXBU7E912_0480(lepB2) COXBU7E912_1201(lepB1)
            LPN: lpg1871(lepB-1)
            LPF: lpl1833(lepB)
            LPP: lpp1836(lepB)
            MCA: MCA1465(lepB)
            FTU: FTT1556c(lepB)
            FTF: FTF1556c(lepB)
            FTW: FTW_0371(lepB)
            FTL: FTL_0553
            FTH: FTH_0554(lepB)
            FTA: FTA_0586(lepB)
            FTN: FTN_1464(lepB)
            TCX: Tcr_0733
            NOC: Noc_2460
            AEH: Mlg_1345
            HHA: Hhal_0035
            HCH: HCH_01798(lepB)
            CSA: Csal_1630
            ABO: ABO_1633(lepB)
            MMW: Mmwyl1_1245
            AHA: AHA_0799(lepB)
            DNO: DNO_0693(lepB)
            BCI: BCI_0282(lepB)
            RMA: Rmag_0621
            VOK: COSY_0574(lepB)
            NME: NMB0765
            NMA: NMA0976(lepB)
            NMC: NMC0718(lepB)
            NGO: NGO0343
            CVI: CV_2064(lepB) CV_3687
            RSO: RSc1061(lepB) RSc1716(RS02906)
            REU: Reut_A2254
            REH: H16_A2557(lepB)
            RME: Rmet_2420
            BMA: BMA0542(lepB)
            BMV: BMASAVP1_A2467(lepB)
            BML: BMA10299_A2814(lepB)
            BMN: BMA10247_1790(lepB)
            BXE: Bxe_A1084 Bxe_A2510
            BVI: Bcep1808_1052 Bcep1808_6971
            BUR: Bcep18194_A4245
            BCN: Bcen_0653
            BCH: Bcen2424_1133
            BAM: Bamb_1009
            BPS: BPSL2430(lepB)
            BPM: BURPS1710b_2896(lepB)
            BPL: BURPS1106A_2841
            BPD: BURPS668_2780
            BTE: BTH_I1729
            PNU: Pnuc_0405
            BPE: BP2432(lep)
            BPA: BPP3296(lep)
            BBR: BB3747(lep)
            RFR: Rfer_1741
            POL: Bpro_3637
            PNA: Pnap_3063
            AAV: Aave_1194
            AJS: Ajs_3269
            VEI: Veis_3240
            MPT: Mpe_A0648
            HAR: HEAR2065(lepB)
            NEU: NE2326(lepB)
            NET: Neut_1780
            NMU: Nmul_A1752
            EBA: ebA5536(lepB)
            AZO: azo1640(lepB)
            DAR: Daro_2027
            TBD: Tbd_2088
            MFA: Mfla_0861 Mfla_1005
            HPY: HP0576(lepB)
            HPJ: jhp0523(lepB)
            HPA: HPAG1_0555
            HHE: HH1367(lepB)
            HAC: Hac_1436(lepB)
            WSU: WS1346(lepP)
            TDN: Tmden_1114
            CJE: Cj0856(lepP)
            CJR: CJE0943(lepB)
            CJJ: CJJ81176_0872(lepB)
            CJU: C8J_0803(lepP)
            CJD: JJD26997_1005(lepB)
            CFF: CFF8240_1173(lepB)
            CCV: CCV52592_0800(lepB)
            CHA: CHAB381_1037(lepB)
            CCO: CCC13826_0831(lepB)
            ABU: Abu_0636(lepP)
            NIS: NIS_0710(lepB)
            SUN: SUN_0664(lepB)
            GSU: GSU1267(lepB)
            GME: Gmet_1767
            GUR: Gura_2504 Gura_3501
            PCA: Pcar_1617
            PPD: Ppro_2330
            DVU: DVU0704(lepB)
            DVL: Dvul_2260
            DDE: Dde_2816
            LIP: LI0923(lepB)
            BBA: Bd0852(lepB) Bd0853(lepB) Bd0854(lepB)
            DPS: DP0107
            ADE: Adeh_1615 Adeh_4158
            AFW: Anae109_2196
            MXA: MXAN_3509(lepB)
            SAT: SYN_01527
            SFU: Sfum_0536 Sfum_0598
            RPR: RP116(lepB)
            RTY: RT0020(lepB)
            RCO: RC0156(lepB)
            RFE: RF_1177(lepB)
            RBE: RBE_1182(lepB)
            OTS: OTBS_1702(lepB)
            WOL: WD0893(lepB)
            WBM: Wbm0760
            AMA: AM708(lepB)
            APH: APH_0802(lepB)
            ERU: Erum3720(sipF)
            ERW: ERWE_CDS_03840(lepB)
            ERG: ERGA_CDS_03800(lepB)
            ECN: Ecaj_0362
            ECH: ECH_0690(lepB)
            NSE: NSE_0784(lepB)
            PUB: SAR11_1054(sipF)
            MLO: mlr7763
            MES: Meso_0949
            PLA: Plav_2873
            SME: SMc02653(lepB)
            SMD: Smed_0681
            ATU: Atu1034(sipf)
            ATC: AGR_C_1904
            RET: RHE_CH01389(lepB)
            RLE: RL1510(sipS)
            BME: BMEI1288
            BMF: BAB1_0680
            BMS: BR0660
            BMB: BruAb1_0677
            BOV: BOV_0653(lepB)
            OAN: Oant_2628
            BJA: bll1167(sipS) bll5062(sipF) bll5628
            BRA: BRADO2889(lepB) BRADO4464(lepB) BRADO6713(lepB1)
            BBT: BBta_0824(lepB1) BBta_4684(lepB)
            RPA: RPA0824(lepB1) RPA2696(lepB2)
            RPB: RPB_2611 RPB_4593
            RPC: RPC_2639 RPC_4784
            RPD: RPD_2650
            RPE: RPE_3023
            NWI: Nwi_1919
            NHA: Nham_0252 Nham_2252
            BHE: BH05080(lebB)
            BQU: BQ04270(lebB)
            BBK: BARBAKC583_0472(lepB)
            XAU: Xaut_3880
            CCR: CC_1559 CC_2150
            SIL: SPO3199(lepB)
            SIT: TM1040_2560
            RSP: RSP_1674
            RSH: Rsph17029_0307
            RSQ: Rsph17025_2572
            JAN: Jann_0521
            RDE: RD1_1365(lepB)
            PDE: Pden_0420
            MMR: Mmar10_0838
            HNE: HNE_1842(lepB)
            ZMO: ZMO1710(lepB)
            NAR: Saro_0909 Saro_1808
            SAL: Sala_1214 Sala_1410
            SWI: Swit_3871
            ELI: ELI_02705 ELI_04845
            GOX: GOX0871 GOX1809
            GBE: GbCGDNIH1_0991
            ACR: Acry_0249
            RRU: Rru_A1853
            MAG: amb2257
            MGM: Mmc1_0906
            ABA: Acid345_2191 Acid345_3855 Acid345_3856
            SUS: Acid_0799 Acid_1171 Acid_2207 Acid_4552 Acid_4838
            BSU: BG10515(sipS) BG11223(sipU) BG11696(sipW) BG11977(sipT)
                 BG12674(sipV)
            BHA: BH1030(sipV) BH2130(sipW)
            BAN: BA1140(sipT) BA1287(sipW) BA3086 BA3099(sipU) BA3977(sipS-2)
            BAR: GBAA1140(sipT) GBAA1287(sipW) GBAA3086 GBAA3099(sipU)
                 GBAA3977(sipS-2) GBAA_pXO2_0073
            BAA: BA_0989 BA_1687 BA_1816 BA_3591 BA_3602 BXB0073
            BAT: BAS0400 BAS1059 BAS1191 BAS2871 BAS2884 BAS3690
            BCE: BC0456 BC1136 BC1278 BC2621 BC3060 BC3070 BC3837
            BCA: BCE_0528(SpaseI) BCE_1243(sipT) BCE_1389(sipW) BCE_3112
                 BCE_3123(sipU) BCE_3881(sipS)
            BCZ: BCZK0388(sipS) BCZK1037(sipT) BCZK1172(sigW) BCZK2801(sipP)
                 BCZK2812(sipU) BCZK3598(sipS) pE33L466_0206(lepB)
            BCY: Bcer98_0400 Bcer98_0858 Bcer98_2064 Bcer98_2491
            BTK: BT9727_0392(sip) BT9727_1039(sipT) BT9727_1170(sigW)
                 BT9727_2841(sipP) BT9727_2851(sipU) BT9727_3580(sipS)
            BTL: BALH_0413(sipS) BALH_2764
            BLI: BL00487(sipS) BL01092(sipV) BL01564(sipW) BL01607(sipT)
            BLD: BLi00675(sipS) BLi01122(sipV) BLi01655(sipT) BLi02638(sipW)
            BCL: ABC0753(sipW) ABC1475(sipV) ABC2286(sipS)
            BAY: RBAM_010710(sipV) RBAM_014150(sipT) RBAM_021440(sipS)
                 RBAM_022950(sipW)
            BPU: BPUM_0840(sipP) BPUM_1337(sipT)
            OIH: OB0800 OB1180 OB1301 OB1390(sipS) OB1538 OB2526
            GKA: GK0680 GK1203
            SAU: SA0825(spsA) SA0826(spsB)
            SAV: SAV0964(spsA) SAV0965(spsB)
            SAM: MW0846(spsA) MW0847(spsB)
            SAR: SAR0926(spsA) SAR0927(spsB)
            SAS: SAS0834 SAS0835
            SAC: SACOL0968(spsA) SACOL0969(spsB)
            SAB: SAB0833(spsA) SAB0834(spsB)
            SAA: SAUSA300_0867(spsA) SAUSA300_0868(spsB)
            SAO: SAOUHSC_00902 SAOUHSC_00903
            SAJ: SaurJH9_0965
            SAH: SaurJH1_0984
            SEP: SE0660 SE0662 SE2397
            SER: SERP0024 SERP0552(spsA) SERP0553(spsB)
            SHA: SH1985(spsB) SH1986(spsA) SH2662(sipB)
            SSP: SSP1810 SSP1811
            LMO: lmo1269 lmo1270 lmo1271
            LMF: LMOf2365_1287 LMOf2365_1288 LMOf2365_1289
            LIN: lin1308 lin1309 lin1310
            LWE: lwe1286(sipX) lwe1287(sipY) lwe1288(sipZ)
            LLA: L0337(sipL)
            LLC: LACR_2588
            LLM: llmg_2550(sipL)
            SPY: SPy_0127 SPy_1281(sipC) SPy_1842(spi)
            SPZ: M5005_Spy_0108 M5005_Spy_0987(sipC) M5005_Spy_1565(spi)
            SPM: spyM18_0127(lepA) spyM18_1229 spyM18_1907(lepB)
            SPG: SpyM3_0099 SpyM3_0911(sipC) SpyM3_1592(spi)
            SPS: SPs0101(lepA) SPs0275 SPs1110
            SPH: MGAS10270_Spy1101(sipC) MGAS10270_Spy1632(spi)
            SPI: MGAS10750_Spy1137(sipC) MGAS10750_Spy1624(spi)
            SPJ: MGAS2096_Spy0114 MGAS2096_Spy1047(sipC) MGAS2096_Spy1590(spi)
            SPK: MGAS9429_Spy0112 MGAS9429_Spy1091(sipC) MGAS9429_Spy1570(spi)
            SPF: SpyM50285(spi) SpyM50814(sipC)
            SPA: M6_Spy0974 M6_Spy1577
            SPB: M28_Spy0108 M28_Spy0959(sipC) M28_Spy1553(spi)
            SPN: SP_0402
            SPR: spr0364(spi)
            SPD: SPD_0367(lepB)
            SAG: SAG0942 SAG1723
            SAN: gbs0932 gbs1768
            SAK: SAK_1038(lepB) SAK_1443(lepB) SAK_1731(lepB)
            SMU: SMU.1188(lepB) SMU.1874(lepC)
            STC: str1140(sipB) str1766(sipA)
            STL: stu1140(sipB) stu1766(sipA)
            SSA: SSA_0351(spi) SSA_0849(sip)
            LPL: lp_2862(sip1) lp_2863(sip2) lp_3675(sip3)
            LJO: LJ1291 LJ1511
            LAC: LBA1909
            LSA: LSA0096(sipA1) LSA0995(sipA2)
            LSL: LSL_0876(lepB)
            LDB: Ldb1215(lepB)
            LBU: LBUL_1124
            LBR: LVIS_0282 LVIS_2298
            LCA: LSEI_0254
            LGA: LGAS_0790
            EFA: EF0854 EF1111 EF1678 EF3073
            OOE: OEOE_1861
            STH: STH1180 STH1472 STH2445 STH381
            CAC: CAC1760 CAC2646(sipS)
            CPE: CPE0315(sipS) CPE0430(sipS) CPE0514 CPE0597(sipS)
                 CPE1553(sipS) CPE2295(lepW)
            CPF: CPF_0312 CPF_0432(lepB) CPF_0493(sipW) CPF_0578 CPF_1804
                 CPF_2579
            CPR: CPR_0427 CPR_0480 CPR_0564 CPR_1523 CPR_2281(sipW)
            CTC: CTC01253
            CNO: NT01CX_0388(lepB) NT01CX_1339(lepB)
            CTH: Cthe_0350
            CDF: CD0554(sip2) CD0555(sip2)
            CBO: CBO0574
            CBA: CLB_0615(lepB-1) CLB_2307(lepB-2)
            CBH: CLC_0630(lepB-1) CLC_2291(lepB-2)
            CBF: CLI_0654(lepB-1) CLI_2499(lepB-2)
            CKL: CKL_2852
            AMT: Amet_3647
            CHY: CHY_1360(lepB)
            DSY: DSY1580 DSY2118 DSY2591 DSY4475
            DRM: Dred_2049
            SWO: Swol_1149
            CSC: Csac_1711
            TTE: TTE0024(lepB)
            MTA: Moth_0972
            MPU: MYPU_6300(sipS)
            MGA: MGA_1091(lepB)
            MHY: mhp028
            MHJ: MHJ_0022(sipS)
            MHP: MHP7448_0026(sipS)
            MSY: MS53_0040(sipS)
            MTU: Rv2903c(lepB)
            MTC: MT2971(lepB)
            MBO: Mb2927c(lepB)
            MBB: BCG_2924c(lepB)
            MLE: ML1612
            MPA: MAP2971c(lepB)
            MAV: MAV_3758(lepB)
            MSM: MSMEG_2441(lepB)
            MVA: Mvan_2193
            MGI: Mflv_4169
            MMC: Mmcs_1971
            MKM: Mkms_2017
            MJL: Mjls_1951
            CGL: NCgl1958(cgl2034)
            CGB: cg2232(lepB)
            CEF: CE1926 CE2634
            CDI: DIP1516
            CJK: jk1183
            NFA: nfa41460
            RHA: RHA1_ro06543(lepB)
            SCO: SCO5596(sip1) SCO5597(sip2) SCO5598(sip3) SCO5599(sip4)
            SMA: SAV2636 SAV2637 SAV2638 SAV2639
            TWH: TWT456(lepB)
            TWS: TW309(sipS)
            LXX: Lxx18070(lepB) Lxx21130(lepB)
            CMI: CMM_1247(sipX) CMM_1374(lepB)
            AAU: AAur_3230(lepB)
            PAC: PPA1434
            TFU: Tfu_0667
            FRA: Francci3_3589
            FAL: FRAAL5788
            ACE: Acel_1556
            SEN: SACE_6048(lepB)
            STP: Strop_1310
            BLO: BL0277(lepB) BL0779(sipY)
            RXY: Rxyl_0250
            FNU: FN0370
            RBA: RB5154(lepB) RB5837
            CTR: CT020(lepB)
            CTA: CTA_0022(lepB)
            CMU: TC0289
            CPN: CPn0110(lepB)
            CPA: CP0664
            CPJ: CPj0110(lepB)
            CPT: CpB0111
            CCA: CCA00663
            CAB: CAB633
            CFE: CF0348(lepB)
            PCU: pc0496(lepB)
            BBU: BB0030(lepB-1) BB0031(lepB-2) BB0263(lepB-3)
            BGA: BG0030(lepB-1) BG0031(lepB-2) BG0266(lepB-3)
            BAF: BAPKO_0029(lepB-1) BAPKO_0030(lepB-2) BAPKO_0273(lepB-3)
            TPA: TP0185 TP0926
            TDE: TDE1313 TDE1465 TDE2219
            LIL: LA1712(sipA) LA2788(lepB) LA3754(sipC)
            LIC: LIC10478(lepB) LIC11233 LIC12086(sipA)
            LBJ: LBJ_1224 LBJ_1764(lepB-2) LBJ_2554(lepB-1)
            LBL: LBL_0558(lepB-1) LBL_1275 LBL_1983(lepB-2)
            SYN: sll0716(lepB1) slr1377(lepB2)
            SYW: SYNW0996(lepB) SYNW1765(lepB)
            SYC: syc1032_d(lepB) syc1041_d
            SYF: Synpcc7942_0478 Synpcc7942_0487
            SYD: Syncc9605_0699 Syncc9605_1121
            SYE: Syncc9902_1335 Syncc9902_1659
            SYG: sync_1525(lepB) sync_2014
            SYR: SynRCC307_0869(lepB) SynRCC307_1139(lepB)
            SYX: SynWH7803_0628(lepB) SynWH7803_1020(lepB)
            CYA: CYA_2275(lepB)
            CYB: CYB_0452(lepB)
            TEL: tlr0405 tlr1822
            GVI: glr2023 glr2481 glr3215
            ANA: alr2304 alr2975
            AVA: Ava_0121 Ava_0931
            PMA: Pro0513(lepB) Pro1055(lepB)
            PMM: PMM0513(lepB) PMM0606(lepB)
            PMT: PMT0407(lepB) PMT1254(lepB)
            PMN: PMN2A_0042 PMN2A_1846
            PMI: PMT9312_0514 PMT9312_0606
            PMB: A9601_05701 A9601_06621
            PMC: P9515_05771 P9515_06711
            PMF: P9303_07511 P9303_18791
            PMG: P9301_05401 P9301_06321
            PMH: P9215_05951(lepB)
            PME: NATL1_05711 NATL1_06621
            TER: Tery_1310 Tery_2178
            BTH: BT_0667 BT_3318 BT_3319
            BFR: BF0180 BF0181
            BFS: BF0145 BF0146
            PGI: PG2000 PG2001(lepB)
            SRU: SRU_0407(lepB)
            CHU: CHU_2564(lepB) CHU_2565(lepB)
            GFO: GFO_0802(lepB)
            FPS: FP1127(lepB)
            CTE: CT1450(lepB)
            CCH: Cag_0491
            CPH: Cpha266_1858
            PVI: Cvib_1281
            PLT: Plut_1470
            DET: DET1192(lepB)
            DEH: cbdb_A1107(lepB)
            DEB: DehaBAV1_1003
            RCA: Rcas_3523
            DRA: DR_1321 DR_1427 DR_1737
            DGE: Dgeo_1649
            TTH: TTC1003
            TTJ: TTHA1368
            AAE: aq_955(lepB)
            TMA: TM1572
            MJA: MJ0260
            MMP: MMP0387
            MAC: MA0036(sec11)
            MBA: Mbar_A1004
            MMA: MM_1344
            MBU: Mbur_1734
            MHU: Mhun_2411
            MTH: MTH1448
            MST: Msp_1575
            MSI: Msm_1232
            MKA: MK1031(lepB)
            AFU: AF1655 AF1657(spc21) AF1791(sec11) AF2078
            HAL: VNG2416G(sec11)
            HMA: rrnAC2712(sec11a) rrnAC2713(sec11b)
            HWA: HQ1595A(lepW)
            NPH: NP0484A(sec11)
            TAC: Ta0151m Ta0378
            TVO: TVN0221
            PTO: PTO0924 PTO1349
            PHO: PH0563 PH0590
            PAB: PAB0966 PAB0983
            PFU: PF0313 PF0326
            TKO: TK1703 TK2037
            APE: APE_1796.1
            SSO: SSO0916
            STO: ST1209 ST1554
            SAI: Saci_1380
            PAI: PAE0264
STRUCTURES  PDB: 1KN9  1T7D  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.89
            ExPASy - ENZYME nomenclature database: 3.4.21.89
            ExplorEnz - The Enzyme Database: 3.4.21.89
            ERGO genome analysis and discovery system: 3.4.21.89
            BRENDA, the Enzyme Database: 3.4.21.89
            CAS: 65979-36-4
///
ENTRY       EC 3.4.21.90                Enzyme
NAME        togavirin;
            Sindbis virus protease;
            Sindbis virus core protein;
            NsP2 proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Autocatalytic release of the core protein from the N-terminus of the
            togavirus structural polyprotein by hydrolysis of a -Trp!Ser- bond
COMMENT     Known from the Sindbis and Semliki forest togaviruses. Once
            released, the core protein does not retain catalytic activity.
            Togavirin is the type example of peptidase family S3 and has a
            similar tertiary structure to chymotrypsin [3]
REFERENCE   1  [PMID:3052288]
  AUTHORS   Krausslich HG, Wimmer E.
  TITLE     Viral proteinases.
  JOURNAL   Annu. Rev. Biochem. 57 (1988) 701-54.
REFERENCE   2  [PMID:1448929]
  AUTHORS   Strauss EG, De Groot RJ, Levinson R, Strauss JH.
  TITLE     Identification of the active site residues in the nsP2 proteinase of
            Sindbis virus.
  JOURNAL   Virology. 191 (1992) 932-40.
  ORGANISM  Sindbis virus
REFERENCE   3  [PMID:8450538]
  AUTHORS   Tong L, Wengler G, Rossmann MG.
  TITLE     Refined structure of Sindbis virus core protein and comparison with
            other chymotrypsin-like serine proteinase structures.
  JOURNAL   J. Mol. Biol. 230 (1993) 228-47.
  ORGANISM  Sindbis virus
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.90
            ExPASy - ENZYME nomenclature database: 3.4.21.90
            ExplorEnz - The Enzyme Database: 3.4.21.90
            ERGO genome analysis and discovery system: 3.4.21.90
            BRENDA, the Enzyme Database: 3.4.21.90
            CAS: 37259-58-8
///
ENTRY       EC 3.4.21.91                Enzyme
NAME        flavivirin;
            Yellow fever virus (flavivirus) protease;
            NS2B-3 proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective hydrolysis of -Xaa-Xaa!Yaa- bonds in which each of the Xaa
            can be either Arg or Lys and Yaa can be either Ser or Ala
COMMENT     Known from classical flaviviruses (yellow fever, dengue fever). The
            functional viral peptidase is part of the NS2B protein. Catalytic
            His, Asp and Ser residues are arranged as in chymotrypsin, but
            flavivrin is the type example of peptidase family S7
REFERENCE   1  [PMID:2174669]
  AUTHORS   Chambers TJ, Hahn CS, Galler R, Rice CM.
  TITLE     Flavivirus genome organization, expression, and replication.
  JOURNAL   Annu. Rev. Microbiol. 44 (1990) 649-88.
REFERENCE   2  [PMID:1531368]
  AUTHORS   Cahour A, Falgout B, Lai CJ.
  TITLE     Cleavage of the dengue virus polyprotein at the NS3/NS4A and
            NS4B/NS5 junctions is mediated by viral protease NS2B-NS3, whereas
            NS4A/NS4B may be processed by a cellular protease.
  JOURNAL   J. Virol. 66 (1992) 1535-42.
  ORGANISM  Dengue virus
REFERENCE   3  [PMID:8445732]
  AUTHORS   Lin C, Amberg SM, Chambers TJ, Rice CM.
  TITLE     Cleavage at a novel site in the NS4A region by the yellow fever
            virus NS2B-3 proteinase is a prerequisite for processing at the
            downstream 4A/4B signalase site.
  JOURNAL   J. Virol. 67 (1993) 2327-35.
  ORGANISM  Yellow fever virus
STRUCTURES  PDB: 1YKS  2FOM  2FP7  2IJO  2QEQ  2V8O  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.91
            ExPASy - ENZYME nomenclature database: 3.4.21.91
            ExplorEnz - The Enzyme Database: 3.4.21.91
            ERGO genome analysis and discovery system: 3.4.21.91
            BRENDA, the Enzyme Database: 3.4.21.91
            CAS: 154215-26-6
///
ENTRY       EC 3.4.21.92                Enzyme
NAME        endopeptidase Clp;
            endopeptidase Ti;
            caseinolytic protease;
            protease Ti;
            ATP-dependent Clp protease;
            endopeptidase Ti;
            caseinolytic protease;
            ClpP;
            Clp protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of proteins to small peptides in the presence of ATP and
            Mg2+. alpha-Casein is the usual test substrate. In the absence of
            ATP, only oligopeptides shorter than five residues are hydrolysed
            (such as succinyl-Leu-Tyr!NHMec; and Leu-Tyr-Leu!Tyr-Trp, in which
            cleavage of the -Tyr!Leu- and -Tyr!Trp bonds also occurs)
COMMENT     An enzyme from bacteria that contains subunits of two types, ClpP,
            with peptidase activity, and ClpA, with ATPase activity. The ClpAP
            complex, which displays ATP-dependent endopeptidase activity, has
            the composition (ClpP14ClpA6)2 [4]. ClpP is the type example of
            peptidase family S14
REFERENCE   1  [PMID:2186030]
  AUTHORS   Gottesman S, Clark WP, Maurizi MR.
  TITLE     The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA
            and identification of a Clp-specific substrate.
  JOURNAL   J. Biol. Chem. 265 (1990) 7886-93.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:2197275]
  AUTHORS   Maurizi MR, Clark WP, Katayama Y, Rudikoff S, Pumphrey J, Bowers B,
            Gottesman S.
  TITLE     Sequence and structure of Clp P, the proteolytic component of the
            ATP-dependent Clp protease of Escherichia coli.
  JOURNAL   J. Biol. Chem. 265 (1990) 12536-45.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:7845217]
  AUTHORS   Maurizi MR, Thompson MW, Singh SK, Kim SH.
  TITLE     Endopeptidase Clp: ATP-dependent Clp protease from Escherichia coli.
  JOURNAL   Methods. Enzymol. 244 (1994) 314-31.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:7623377]
  AUTHORS   Kessel M, Maurizi MR, Kim B, Kocsis E, Trus BL, Singh SK, Steven AC.
  TITLE     Homology in structural organization between E. coli ClpAP protease
            and the eukaryotic 26 S proteasome.
  JOURNAL   J. Mol. Biol. 250 (1995) 587-94.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01358  ATP-dependent Clp protease, protease subunit
GENES       HSA: 8192(CLPP)
            PTR: 455637(CLPP)
            MMU: 53895(Clpp)
            RNO: 301117(LOC301117)
            CFA: 611738(CLPP)
            BTA: 535981(CLPP)
            XLA: 496087(LOC496087)
            DRE: 553713(zgc:112333)
            SPU: 581816(LOC581816)
            DME: Dmel_CG5045
            CEL: ZK970.2
            ATH: AT1G11750(CLPP6) AT1G12410(CLPR2) AT4G17040 AT5G23140(CLPP2)
            OSA: 4324049 4325168 4330071 4332615 4333096 4336449 4340044
            CME: CML155C CMQ045C CMS440C
            ANI: AN2972.2
            AFM: AFUA_3G08330
            AOR: AO090005001444
            CNE: CNN01350
            PFA: MAL3P2.31 PF14_0063 PF14_0348
            TAN: TA05070 TA09390 TA09910 TA16975
            TPV: TP01_1041 TP04_0168 TP04_0800
            ECO: b0437(clpP)
            ECJ: JW0427(clpP)
            ECE: Z0542(clpP)
            ECS: ECs0491
            ECC: c0553(clpP)
            ECI: UTI89_C0465(clpP) UTI89_C3197
            ECP: ECP_0498
            ECV: APECO1_1574(clpP)
            ECW: EcE24377A_0473(clpP)
            ECX: EcHS_A0514(clpP)
            STY: STY0490(clpP)
            STT: t2412(clpP)
            SPT: SPA2274(clpP)
            SEC: SC0490(clpP)
            STM: STM0448(clpP)
            YPE: YPO3157(clpP)
            YPK: y1027(clpP)
            YPM: YP_0774(clpP)
            YPA: YPA_2652
            YPN: YPN_0933
            YPP: YPDSF_2793
            YPS: YPTB0959(clpP)
            YPI: YpsIP31758_3092(clpP)
            SFL: SF0382(clpP)
            SFX: S0388(clpP)
            SFV: SFV_0411(clpP)
            SSN: SSON_0420(clpP)
            SBO: SBO_0331(clpP)
            SDY: SDY_0295(clpP)
            ECA: ECA1148(clpP)
            PLU: plu3869(clpP)
            BUC: BU475(clpP)
            BAS: BUsg459(clpP)
            BAB: bbp419(clpP)
            BCC: BCc_293(clpP)
            WBR: WGLp155(clpP)
            SGL: SG0671
            ENT: Ent638_0489 Ent638_0904
            KPN: KPN_00399(clpP)
            SPE: Spro_1095 Spro_1978
            BFL: Bfl246(clpP)
            BPN: BPEN_253(clpP)
            HIT: NTHI0844(clpP)
            HIP: CGSHiEE_08555(clpP)
            HIQ: CGSHiGG_06885(clpP)
            HDU: HD0221(clpP)
            HSO: HS_1432(clpP)
            PMU: PM1976(clpP)
            MSU: MS1847(clpP)
            APL: APL_1280(clpP)
            ASU: Asuc_0766
            XFA: XF1187
            XFT: PD0472(clpP)
            XCC: XCC0975(clpP)
            XCB: XC_3265
            XCV: XCV1081(clpP)
            XAC: XAC1078(clpP)
            XOO: XOO1033(clpP)
            XOM: XOO_0932(XOO0932)
            VCH: VC1922
            VCO: VC0395_A1512(clpP)
            VVU: VV1_0023
            VVY: VV1104
            VPA: VP0917
            VFI: VF0796
            PPR: PBPRA2637
            PAE: PA1801(clpP) PA3326
            PAU: PA14_21030 PA14_41240(clpP)
            PAP: PSPA7_1794 PSPA7_3110 PSPA7_3496(clpP)
            PPU: PP_2300(clpP)
            PPF: Pput_3469
            PST: PSPTO_3726(clpP-2)
            PSB: Psyr_1747(clpP)
            PSP: PSPPH_1698(clpP)
            PFL: PFL_3987(clpP)
            PFO: Pfl_3697(clpP)
            PEN: PSEEN1868(clpP)
            PMY: Pmen_2050
            PAR: Psyc_1941(clpP)
            PCR: Pcryo_2234
            PRW: PsycPRwf_0306
            ACI: ACIAD0534(clpP)
            SON: SO_1794(clpP)
            SDN: Sden_2495
            SFR: Sfri_2596
            SAZ: Sama_1224
            SBL: Sbal_1604
            SBM: Shew185_1593
            SLO: Shew_2508
            SPC: Sputcn32_1490
            SSE: Ssed_1541
            SPL: Spea_2681
            SHE: Shewmr4_2495
            SHM: Shewmr7_2563
            SHN: Shewana3_2661
            SHW: Sputw3181_2611
            ILO: IL1005(clpP)
            CPS: CPS_3785(clpP)
            PHA: PSHAa2062(clpP)
            PAT: Patl_3136
            SDE: Sde_1608
            PIN: Ping_1465
            MAQ: Maqu_1840
            CBU: CBU_0738(clpP)
            CBD: COXBU7E912_0752(clpP)
            LPN: lpg1861(clpP)
            LPF: lpl1825(clpP)
            LPP: lpp1829(clpP)
            MCA: MCA0242(clpP-1) MCA0529(clpP-2)
            FTU: FTT0624(clpP)
            FTF: FTF0624(clpP)
            FTW: FTW_1105(clpP)
            FTL: FTL_0892
            FTH: FTH_0089(clpB) FTH_0877(clpP) FTH_0878(clpX)
            FTA: FTA_0943(clpP)
            FTN: FTN_1057(clpP)
            TCX: Tcr_1177
            NOC: Noc_1676
            AEH: Mlg_2288
            HHA: Hhal_0603
            HCH: HCH_02158(clpP1) HCH_02373(clpP2)
            CSA: Csal_2046
            ABO: ABO_1210(clpP)
            MMW: Mmwyl1_1723
            AHA: AHA_2011(clpP)
            DNO: DNO_0229(clpP)
            BCI: BCI_0265(clpP)
            CRP: CRP_072
            RMA: Rmag_0205
            VOK: COSY_0203(clpP)
            NME: NMB1312
            NMA: NMA1525(clpP)
            NMC: NMC1248(clpP)
            NGO: NGO0593
            CVI: CV_1944(clpB) CV_2557(clpX) CV_2558(clpP) CV_3965
            RSO: RSc1711(clpP)
            REU: Reut_A1380
            REH: H16_A1483(clpP)
            RME: Rmet_1885
            BMA: BMA1465(clpP)
            BMV: BMASAVP1_A1957(clpP)
            BML: BMA10299_A3348(clpP)
            BMN: BMA10247_1232(clpP)
            BXE: Bxe_A0776 Bxe_A2295
            BVI: Bcep1808_1855
            BUR: Bcep18194_A5224 Bcep18194_B1167
            BCN: Bcen_6156
            BCH: Bcen2424_1923
            BAM: Bamb_1911
            BPS: BPSL1403(clpP)
            BPM: BURPS1710b_2481(clpP)
            BPL: BURPS1106A_2365(clpP)
            BPD: BURPS668_2323(clpP)
            BTE: BTH_I2120(clpP) BTH_I2958 BTH_II1046
            PNU: Pnuc_0934
            BPE: BP1775(clpP)
            BPA: BPP2006(clpP)
            BBR: BB2254(clpP)
            RFR: Rfer_1554
            POL: Bpro_2030
            PNA: Pnap_2957
            AAV: Aave_1459
            AJS: Ajs_1209
            VEI: Veis_0360 Veis_4371
            MPT: Mpe_A1292
            HAR: HEAR1752(clpP)
            NEU: NE0031(clpP)
            NET: Neut_0203
            NMU: Nmul_A2340
            EBA: ebA4970(clpP)
            AZO: azo1132(clpA) azo1870 azo2071(clpP)
            DAR: Daro_1718(clpP)
            TBD: Tbd_1677
            MFA: Mfla_1409
            HPY: HP0794
            HPJ: jhp0730(clpP)
            HPA: HPAG1_0031 HPAG1_0490 HPAG1_0779 HPAG1_1320
            HHE: HH0567(clpP)
            HAC: Hac_0916(clpP)
            WSU: WS2210(clpP)
            TDN: Tmden_2036
            CJE: Cj0192c(clpP)
            CJR: CJE0185(clpP)
            CJJ: CJJ81176_0223(clpP)
            CJU: C8J_0181(clpP)
            CJD: JJD26997_0202(clpP)
            CFF: CFF8240_1692(clpP)
            CCV: CCV52592_1499(clpP)
            CHA: CHAB381_0017(clpP)
            CCO: CCC13826_1781(clpP) CCC13826_2175
            ABU: Abu_1701(clpP)
            NIS: NIS_0165(clpP)
            SUN: SUN_0012(clpP)
            GSU: GSU1792(clpP)
            GME: Gmet_1873
            GUR: Gura_1915
            PCA: Pcar_1689(clpP)
            PPD: Ppro_1183
            DVU: DVU1335(clpP)
            DVL: Dvul_1734
            DDE: Dde_2220
            LIP: LI0794(clpP)
            BBA: Bd3754(clpP)
            DPS: DP2538(clpP)
            ADE: Adeh_3353
            AFW: Anae109_3421
            MXA: MXAN_2014(clpP) MXAN_6438(clpP)
            SAT: SYN_02785
            SFU: Sfum_0100
            RPR: RP520
            RTY: RT0507(clpP)
            RCO: RC0746(clpP)
            RFE: RF_0772(clpP)
            RBE: RBE_0411(clpP)
            RAK: A1C_04235(clpP)
            RCM: A1E_02570(clpP)
            RRI: A1G_04200(clpP)
            OTS: OTBS_1350(clpP)
            WOL: WD0319(clpP)
            WBM: Wbm0553
            AMA: AM309(clpP) AM949(clpB)
            APH: APH_0970(clpP)
            ERU: Erum2000(clpP) Erum4660(clpA)
            ERW: ERWE_CDS_02020(clpP)
            ERG: ERGA_CDS_01970(clpP)
            ECN: Ecaj_0202
            ECH: ECH_0901(clpP)
            NSE: NSE_0752(clpP)
            PUB: SAR11_0880(clpP)
            MLO: mlr0748 mlr8472
            MES: Meso_1169 Meso_1531
            PLA: Plav_0006 Plav_3232
            SME: SMc01903(clpP1) SMc02720(clpP2) SMc03841(clpP3)
            SMD: Smed_0872 Smed_2289 Smed_3078
            ATU: Atu1258(clpP) Atu1627(clpP) Atu2270(clpP)
            ATC: AGR_C_2324(clpP) AGR_C_3003(clpP) AGR_C_4125
            RET: RHE_CH01414(clpP1) RHE_CH01587(clpP2) RHE_CH03069(clpP3)
            RLE: RL1170(clpP) RL1688(clpP) RL3515(clpP)
            BME: BMEI0874
            BMF: BAB1_1132(clpP)
            BMS: BR1109(clpP)
            BMB: BruAb1_1115(clpP)
            BOV: BOV_1068(clpP)
            OAN: Oant_0480 Oant_2206
            BJA: bll4944(clpP) blr0611(clpP)
            BRA: BRADO0526(clpP) BRADO4197(clpX) BRADO4198(clpP)
            BBT: BBta_4571(clpX) BBta_4573(clpP) BBta_6597
            RPA: RPA2961(clpP)
            RPB: RPB_2563
            RPC: RPC_2392
            RPD: RPD_2894
            RPE: RPE_2510
            NWI: Nwi_1543 Nwi_1899
            NHA: Nham_2229
            BHE: BH05880(clpP)
            BQU: BQ05040(clpP)
            BBK: BARBAKC583_0546(clpP)
            XAU: Xaut_3591
            CCR: CC_1963
            SIL: SPO1003(clpP)
            SIT: TM1040_1527
            RSP: RSP_0197(clpP)
            RSH: Rsph17029_1830
            RSQ: Rsph17025_1448
            JAN: Jann_2808
            RDE: RD1_2858(clpP)
            PDE: Pden_0017 Pden_1265
            MMR: Mmar10_1338
            HNE: HNE_0542 HNE_2087(clpP)
            ZMO: ZMO0405(clpA) ZMO0948(clpP) ZMO0949(clpX) ZMO1424(clpB)
            NAR: Saro_3055
            SAL: Sala_2742
            SWI: Swit_0593
            ELI: ELI_01135
            GOX: GOX0087 GOX1520
            GBE: GbCGDNIH1_1307
            ACR: Acry_0917 Acry_2158
            RRU: Rru_A1550
            MAG: amb2792
            MGM: Mmc1_3642
            ABA: Acid345_1560
            SUS: Acid_3900
            BSU: BG19016(clpP)
            BHA: BH3118 BH3564(clpP)
            BAN: BA2788(clpP-1) BA5380(clpP-2)
            BAR: GBAA2788(clpP-1) GBAA5380(clpP-2)
            BAA: BA_0238 BA_3310
            BAT: BAS2599(clpP) BAS5000(clpP)
            BCE: BC2793 BC5152
            BCA: BCE_0399(clpP) BCE_2819(clpP) BCE_5254(clpP)
            BCZ: BCZK2518(clpP) BCZK4844(clpP)
            BCY: Bcer98_1910 Bcer98_3694
            BTK: BT9727_2551(clpP) BT9727_4829(clpP)
            BTL: BALH_2505(clpP) BALH_4642(clpP)
            BLI: BL03605(clpP) BL05355
            BLD: BLi03710(clpP) BLi03890
            BCL: ABC0035 ABC3026(clpP)
            BAY: RBAM_031850(clpP)
            BPU: BPUM_1583(clpP1) BPUM_3102(clpP2)
            OIH: OB2456
            GKA: GK3062
            SAU: SA0723(clpP)
            SAV: SAV0768(clpP)
            SAM: MW0730(clpP)
            SAR: SAR0823(clpP)
            SAS: SAS0733
            SAC: SACOL0833(clpP)
            SAB: SAB0722(clpP)
            SAA: SAUSA300_0752(clpP)
            SAO: SAOUHSC_00790
            SAJ: SaurJH9_0793
            SAH: SaurJH1_0809
            SEP: SE0551
            SER: SERP0436(clpP)
            SHA: SH2121(clpP)
            SSP: SSP1923
            LMO: lmo1138 lmo2468(clpP)
            LMF: LMOf2365_1146(clpP-1) LMOf2365_2441(clpP-2)
            LIN: lin1103 lin2612(clpP)
            LWE: lwe1097 lwe2417(clpP)
            LLA: L72391(clpP)
            LLC: LACR_0700
            LLM: llmg_0638(clpP)
            SPY: SPy_0395(clpP)
            SPZ: M5005_Spy_0328(clpP)
            SPM: spyM18_0446(clpP)
            SPG: SpyM3_0287(clpP.1)
            SPS: SPs1572
            SPH: MGAS10270_Spy0324(clpP) MGAS10270_Spy0577
            SPI: MGAS10750_Spy0324(clpP) MGAS10750_Spy0602
            SPJ: MGAS2096_Spy0347(clpP) MGAS2096_Spy1642
            SPK: MGAS9429_Spy0328(clpP) MGAS9429_Spy0573
            SPF: SpyM51284 SpyM51530(clpP)
            SPA: M6_Spy0354 M6_Spy1007 M6_Spy1139
            SPB: M28_Spy0317(clpP)
            SPN: SP_0746
            SPR: spr0656(clpP)
            SPD: SPD_0650(clpP)
            SAG: SAG1585(clpP)
            SAN: gbs1634(clpP)
            SAK: SAK_0747 SAK_1600(clpP)
            SMU: SMU.1672(clpP)
            STC: str0356(clpP)
            STL: stu0356(clpP)
            SSA: SSA_1731(clpP)
            SGO: SGO_1632(clpP)
            LPL: lp_0786(clpP)
            LJO: LJ0869
            LAC: LBA0694(clpP)
            LSA: LSA0531(clpP)
            LSL: LSL_0284(clpP) LSL_0785(clpP) LSL_1168(clpP)
            LDB: Ldb0624(clpP)
            LBU: LBUL_0559
            LBR: LVIS_0654
            LCA: LSEI_0963
            LRE: Lreu_0389
            EFA: EF0771(clpP)
            OOE: OEOE_0570
            STH: STH358 STH914
            CAC: CAC2640(clpP)
            CPE: CPE1393(clpP)
            CPF: CPF_1647(clpP) CPF_1931(clpP)
            CPR: CPR_1385(clpP) CPR_1649(clpP) CPR_C0013(clpP)
            CTC: CTC01283 CTC02375
            CNO: NT01CX_0371(clpP)
            CTH: Cthe_2740
            CDF: CD3305(clpP1) CD3351(clpP2)
            CBO: CBO3231(clpP)
            CBA: CLB_2272(clpP-1) CLB_3268(clpP-2)
            CBH: CLC_2255(clpP-1) CLC_3142(clpP-2)
            CBF: CLI_2464(clpP-1) CLI_3370(clpP-2)
            CBE: Cbei_1327 Cbei_4002
            CKL: CKL_3351(clpP)
            AMT: Amet_1067
            CHY: CHY_0325(clpP)
            DSY: DSY1974 DSY3354
            DRM: Dred_2562
            SWO: Swol_1656
            CSC: Csac_0879
            TTE: TTE0625(clpP)
            MTA: Moth_0528 Moth_1071(clpP)
            MTU: Rv2460c(clpP2) Rv2461c(clpP1)
            MTC: MT2535(clpP-1) MT2536(clpP-2)
            MBO: Mb2487c(clpP2) Mb2488c(clpP1)
            MBB: BCG_2480c(clpP2) BCG_2481c(clpP1)
            MLE: ML1479(clpP2) ML1480(clpP)
            MPA: MAP2280c(clpP2) MAP2281c(clpP)
            MAV: MAV_1713(clpP) MAV_1714(clpP)
            MSM: MSMEG_4672(clpP) MSMEG_4673(clpP)
            MVA: Mvan_4039 Mvan_4040
            MGI: Mflv_2588 Mflv_2589
            MMC: Mmcs_3577 Mmcs_3578
            MKM: Mkms_3650 Mkms_3651
            MJL: Mjls_3582 Mjls_3583
            CGL: NCgl2327(cgl2411) NCgl2328(cgl2412)
            CGB: cg2644(clpP2) cg2645(clpP1)
            CEF: CE2311 CE2312
            CDI: DIP1791(clpP2) DIP1792(clpP1)
            CJK: jk0544(clpP1) jk0545(clpP2)
            NFA: nfa11710(clp3) nfa11720(clp4) nfa13330(clpP1) nfa13340(clpP2)
            RHA: RHA1_ro01371 RHA1_ro01372 RHA1_ro01525 RHA1_ro01526
                 RHA1_ro11334
            SCO: SCO1238(2SCG1.13) SCO2618(clpP2) SCO2619(clpP1)
                 SCO7280(clpP4) SCO7281(clpP3)
            SMA: SAV1146(clpP4) SAV1147(clpP5) SAV5447(clpP1) SAV5448(clpP2)
                 SAV7101(clpP3)
            TWH: TWT480(clpP2) TWT481(clpP1)
            TWS: TW283(clpP1) TW284(clpP2)
            LXX: Lxx07850(clpP) Lxx07860(clpP)
            CMI: CMM_1464(clpP1) CMM_1465(clpP2)
            ART: Arth_2404 Arth_2405
            AAU: AAur_2382(clpP)
            PAC: PPA1572 PPA1573
            NCA: Noca_2736 Noca_2737 Noca_3476 Noca_3477
            TFU: Tfu_2193 Tfu_2194
            FRA: Francci3_1205 Francci3_1206 Francci3_2773 Francci3_2774
            FAL: FRAAL1910(clpP1) FRAAL1911(clpP2) FRAAL4269(clpP)
                 FRAAL4270(clpP)
            ACE: Acel_0737 Acel_0738
            KRA: Krad_3516 Krad_3517 Krad_4258 Krad_4259
            SEN: SACE_1360 SACE_1361
            STP: Strop_0695 Strop_3498 Strop_3499
            BLO: BL0944(clpP2) BL0945(clp1)
            BAD: BAD_0587(clp1) BAD_0588(clpP2)
            RXY: Rxyl_1537
            FNU: FN2016
            RBA: RB10826(clpP) RB10829(clpP)
            CTR: CT431(clpP_1) CT706(clpP_2)
            CTA: CTA_0471(clpP_1) CTA_0767(clpP_2)
            CMU: TC0079 TC0715
            CPN: CPn0520(clpP_1) CPn0847(clpP_2)
            CPA: CP0233 CP1022
            CPJ: CPj0520(clpP_1) CPj0847(clpP_2)
            CPT: CpB0541(clp) CpB0876
            CCA: CCA00225(clpP-2) CCA00920(clpP-1)
            CAB: CAB222(clpP1) CAB888(clpP)
            CFE: CF0094(clpP2) CF0781(clpP1)
            PCU: pc0443(clpP) pc1376(clpP)
            BBU: BB0611(clpP-1) BB0757(clpP-2)
            BGA: BG0627(clpP-1) BG0779(clpP-2)
            BAF: BAPKO_0647(clpP-1) BAPKO_0804(clpP-2)
            TPA: TP0507 TP1041
            TDE: TDE1672(clpP-1) TDE2388(clpP-2)
            LIL: LA1953(clpP1) LA2559(clpP2)
            LIC: LIC11417(clpP) LIC11951
            LBJ: LBJ_1084(clpP-1) LBJ_1559(clpP-2)
            LBL: LBL_1141(clpP-1) LBL_1783(clpP-2)
            SYN: sll0534(clpP2) slr0164(clpP4) slr0165(clpP3) slr0542(clpP1)
            SYW: SYNW0064(clpP2) SYNW1301(clpP1) SYNW1648(clpP4)
                 SYNW1649(clpP3)
            SYC: syc0012_c(clpP) syc1572_d(clpP) syc1573_d(clpP)
                 syc1584_c(clpP)
            SYF: Synpcc7942_1554 Synpcc7942_2525 Synpcc7942_2537
                 Synpcc7942_2538
            SYD: Syncc9605_0065 Syncc9605_0840 Syncc9605_0841 Syncc9605_1440
            SYE: Syncc9902_0062 Syncc9902_1059 Syncc9902_1548 Syncc9902_1549
            SYG: sync_0065(clpP-1) sync_0726 sync_0727(clpP-2)
                 sync_1418(clpP-3)
            SYR: SynRCC307_0066(clpP) SynRCC307_0595(clpP)
                 SynRCC307_0596(clpP) SynRCC307_1404(clpP)
            SYX: SynWH7803_0070(clpP) SynWH7803_1214(clpP)
                 SynWH7803_1763(clpP) SynWH7803_1764(clpP)
            CYA: CYA_0657 CYA_0659 CYA_1193(clpP)
            CYB: CYB_0608(clpP-1) CYB_0610(clpP) CYB_2581(clpP-2)
            TEL: tll1759(clpP3) tlr0509(clpP1) tlr1071(clpP2)
            GVI: gll3766(clpP) gll3767(clpP)
            ANA: all4357(clpP) all4358(clpP) alr1238(clpP) alr3683(clpP)
            AVA: Ava_0547 Ava_1305 Ava_1306 Ava_3604
            PMA: Pro0920(clpP) Pro1387(clpP) Pro1388(clpP) Pro1816(clpP)
            PMM: PMM0742(clpP1) PMM1313(clpP4) PMM1314(clpP3) PMM1656(clpP2)
            PMT: PMT0062(clpP2) PMT0314(clpP3) PMT0315(clpP4) PMT0676(clpP1)
            PMN: PMN2A_0292 PMN2A_0879 PMN2A_0880 PMN2A_1254
            PMI: PMT9312_0750 PMT9312_1410 PMT9312_1411 PMT9312_1748
            PMB: A9601_02251(clpB2) A9601_06361(clpB) A9601_08031
                 A9601_11941(clpC) A9601_15121 A9601_15131 A9601_18651
                 A9601_18661(clpX)
            PMC: P9515_02361(clpB2) P9515_06451(clpB) P9515_08421
                 P9515_11791(clpC) P9515_14741 P9515_14751 P9515_18461
                 P9515_18471(clpX)
            PMF: P9303_00681(clpX) P9303_00691 P9303_09911(clpC) P9303_15461
                 P9303_18321(clpB) P9303_20021 P9303_20031 P9303_27741(clpB2)
            PMG: P9301_02271(clpB2) P9301_06061(clpB) P9301_08021
                 P9301_11951(clpC) P9301_14991 P9301_15001 P9301_18461
                 P9301_18471(clpX)
            PMH: P9215_19291(clpP)
            PME: NATL1_02831(clpB2) NATL1_06361(clpB) NATL1_09641
                 NATL1_14921(clpC) NATL1_17341 NATL1_17351 NATL1_21251
                 NATL1_21261(clpX)
            TER: Tery_0585 Tery_1246 Tery_1247 Tery_1514
            BTH: BT_3842
            BFR: BF4078
            BFS: BF3894(clpP)
            PGI: PG0418(clpP)
            SRU: SRU_1439(clpP) SRU_2674
            CHU: CHU_1079(clpA) CHU_1465(sms)
            GFO: GFO_0223(clpP) GFO_0418(clpP)
            FJO: Fjoh_1702
            FPS: FP2085(clpP)
            CTE: CT1553(clpP)
            CCH: Cag_0389
            CPH: Cpha266_2030
            PVI: Cvib_0441
            PLT: Plut_0385(clpP)
            DET: DET0710(clpP)
            DEH: cbdb_A666(clpP)
            DEB: DehaBAV1_0645
            RRS: RoseRS_1553 RoseRS_3662
            RCA: Rcas_1476 Rcas_3404
            DRA: DR_1972(clpP)
            DGE: Dgeo_2151
            TTH: TTC0250
            TTJ: TTHA0615
            AAE: aq_1339(clpP)
            TMA: TM0695
            TPT: Tpet_0235
            TME: Tmel_0984
            FNO: Fnod_1107
STRUCTURES  PDB: 1TG6  1TYF  1Y7O  1YG6  1YG8  2C8T  2CBY  2CE3  2F6I  2FZS  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.92
            ExPASy - ENZYME nomenclature database: 3.4.21.92
            ExplorEnz - The Enzyme Database: 3.4.21.92
            ERGO genome analysis and discovery system: 3.4.21.92
            BRENDA, the Enzyme Database: 3.4.21.92
            CAS: 110910-59-3
///
ENTRY       EC 3.4.21.93                Enzyme
NAME        proprotein convertase 1;
            prohormone convertase 3;
            neuroendocrine convertase 1;
            PC1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Release of protein hormones, neuropeptides and renin from their
            precursors, generally by hydrolysis of -Lys-Arg! bonds
COMMENT     A Ca2+-dependent enzyme, maximally active at about pH 5.5.
            Substrates include pro-opiomelanocortin, prorenin, proenkephalin,
            prodynorphin, prosomatostatin and proinsulin. Unlike prohormone
            convertase 2, does not hydrolyse
            proluteinizing-hormone-releasing-hormone. Unusually, processing of
            prodynorphin occurs at a bond in which P2 is Thr. Present in the
            regulated secretory pathway of neuroendocrine cells, commonly acting
            co-operatively with prohormone convertase 2. In peptidase family S8
            (subtilisin family)
REFERENCE   1  [PMID:2169760]
  AUTHORS   Seidah NG, Gaspar L, Mion P, Marcinkiewicz M, Mbikay M, Chretien M.
  TITLE     cDNA sequence of two distinct pituitary proteins homologous to Kex2
            and furin gene products: tissue-specific mRNAs encoding candidates
            for pro-hormone processing proteinases.
  JOURNAL   DNA. Cell. Biol. 9 (1990) 415-24.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:1988934]
  AUTHORS   Smeekens SP, Avruch AS, LaMendola J, Chan SJ, Steiner DF.
  TITLE     Identification of a cDNA encoding a second putative prohormone
            convertase related to PC2 in AtT20 cells and islets of Langerhans.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 340-4.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:1429684]
  AUTHORS   Steiner DF, Smeekens SP, Ohagi S, Chan SJ.
  TITLE     The new enzymology of precursor processing endoproteases.
  JOURNAL   J. Biol. Chem. 267 (1992) 23435-8.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:7845206]
  AUTHORS   Seidah NG, Chretien M.
  TITLE     Pro-protein convertases of subtilisin/kexin family.
  JOURNAL   Methods. Enzymol. 244 (1994) 175-88.
REFERENCE   5  [PMID:7741698]
  AUTHORS   Jean F, Basak A, DiMaio J, Seidah NG, Lazure C.
  TITLE     An internally quenched fluorogenic substrate of prohormone
            convertase 1 and furin leads to a potent prohormone convertase
            inhibitor.
  JOURNAL   Biochem. J. 307 ( Pt 3) (1995) 689-95.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01359  proprotein convertase subtilisin/kexin type 1
GENES       HSA: 5122(PCSK1)
            PTR: 461740(PCSK1)
            MMU: 18548(Pcsk1)
            RNO: 25204(Pcsk1)
            CFA: 479149(PCSK1)
            BTA: 281967(PCSK1)
            SSC: 397103(PC1/3)
STRUCTURES  PDB: 1KN6  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.93
            ExPASy - ENZYME nomenclature database: 3.4.21.93
            ExplorEnz - The Enzyme Database: 3.4.21.93
            ERGO genome analysis and discovery system: 3.4.21.93
            BRENDA, the Enzyme Database: 3.4.21.93
            CAS: 99676-46-7
///
ENTRY       EC 3.4.21.94                Enzyme
NAME        proprotein convertase 2;
            neuroendocrine convertase 2;
            PC2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Release of protein hormones and neuropeptides from their precursors,
            generally by hydrolysis of -Lys-Arg! bonds
COMMENT     A Ca2+-dependent enzyme, maximally active at about pH 5.5.
            Specificity is broader than that of prohormone convertase 1.
            Substrates include pro-opiomelanocortin, proenkephalin,
            prodynorphin, proglucagon, proinsulin and
            proluteinizing-hormone-releasing-hormone. Does not hydrolyse
            prorenin or prosomatostatin, however. Unusually, processing of
            prodynorphin occurs at a bond in which P2 is Thr. Present in the
            regulated secretory pathway of neuroendocrine cells, commonly acting
            co-operatively with prohormone convertase 1. In peptidase family S8
            (subtilisin family)
REFERENCE   1  [PMID:2169760]
  AUTHORS   Seidah NG, Gaspar L, Mion P, Marcinkiewicz M, Mbikay M, Chretien M.
  TITLE     cDNA sequence of two distinct pituitary proteins homologous to Kex2
            and furin gene products: tissue-specific mRNAs encoding candidates
            for pro-hormone processing proteinases.
  JOURNAL   DNA. Cell. Biol. 9 (1990) 415-24.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:2154467]
  AUTHORS   Smeekens SP, Steiner DF.
  TITLE     Identification of a human insulinoma cDNA encoding a novel mammalian
            protein structurally related to the yeast dibasic processing
            protease Kex2.
  JOURNAL   J. Biol. Chem. 265 (1990) 2997-3000.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:8159732]
  AUTHORS   Rouille Y, Westermark G, Martin SK, Steiner DF.
  TITLE     Proglucagon is processed to glucagon by prohormone convertase PC2 in
            alpha TC1-6 cells.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 3242-6.
  ORGANISM  human [GN:hsa], mouse [GN:mmu]
REFERENCE   4  [PMID:7845206]
  AUTHORS   Seidah NG, Chretien M.
  TITLE     Pro-protein convertases of subtilisin/kexin family.
  JOURNAL   Methods. Enzymol. 244 (1994) 175-88.
ORTHOLOGY   KO: K01360  proprotein convertase subtilisin/kexin type 2
GENES       HSA: 5126(PCSK2)
            PTR: 458106(PCSK2)
            MMU: 18549(Pcsk2)
            RNO: 25121(Pcsk2)
            CFA: 485757(PCSK2)
            BTA: 281968(PCSK2)
            SSC: 445533(PC2)
            GGA: 395136(PCSK2)
            XLA: 373675(pcsk2-A) 444586(MGC84034)
            SPU: 579017(LOC579017)
            DME: Dmel_CG6438(amon)
            CEL: C51E3.7(egl-3)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.94
            ExPASy - ENZYME nomenclature database: 3.4.21.94
            ExplorEnz - The Enzyme Database: 3.4.21.94
            ERGO genome analysis and discovery system: 3.4.21.94
            BRENDA, the Enzyme Database: 3.4.21.94
            CAS: 130960-94-0
///
ENTRY       EC 3.4.21.95                Enzyme
NAME        snake venom factor V activator
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Fully activates human clotting factor V by a single cleavage at the
            Trp-Tyr-Leu-Arg1545!Ser-Asn-Asn-Gly bond. Cattle, but not rabbit,
            factor V is cleaved, and no other proteins of the clotting system
            are attacked. Esterase activity is observed on Bz-Arg- OEt and
            Tos-Arg- OMe, and amidase activity on Phe-pipecolyl-Arg-NHPhNO2
INHIBITOR   Isoflurophate [CPD:C00202]
REFERENCE   1  [PMID:7043192]
  AUTHORS   Kisiel W, Canfield WM.
  TITLE     Snake venom proteases that activate blood-coagulation factor V.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 275-85.
REFERENCE   2  [PMID:3053712]
  AUTHORS   Tokunaga F, Nagasawa K, Tamura S, Miyata T, Iwanaga S, Kisiel W.
  TITLE     The factor V-activating enzyme (RVV-V) from Russell's viper venom.
            Identification of isoproteins RVV-V alpha, -V beta, and -V gamma and
            their complete amino acid sequences.
  JOURNAL   J. Biol. Chem. 263 (1988) 17471-81.
  ORGANISM  Vipera russelli
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.95
            ExPASy - ENZYME nomenclature database: 3.4.21.95
            ExplorEnz - The Enzyme Database: 3.4.21.95
            ERGO genome analysis and discovery system: 3.4.21.95
            BRENDA, the Enzyme Database: 3.4.21.95
            CAS: 471269-12-2
///
ENTRY       EC 3.4.21.96                Enzyme
NAME        lactocepin;
            CEP;
            extracellular lactococcal proteinase;
            lactococcal cell wall-associated proteinase;
            lactococcal cell envelope-associated proteinase;
            lactococcal proteinase;
            PrtP
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Endopeptidase activity with very broad specificity, although some
            subsite preferences have been noted, e.g. large hydrophobic residues
            in the P1 and P4 positions, and Pro in the P2 position [1,2]. Best
            known for its action on caseins, although it has been shown to
            hydrolyse hemoglobin and oxidized insulin B chain
COMMENT     Associated with the cell envelope of Lactococcus lactis and attached
            via a C-terminal membrane anchor sequence. Responsible for the
            hydrolysis of casein in milk and the provision of peptides essential
            to cell growth. Important in cheese making and the production of
            lactic casein, being required for rapid growth to high cell
            densities with concomitant production of adequate levels of lactic
            acid. Specificity differences between lactocepins from different
            starter strains may be partly responsible for imparting different
            flavour qualities to cheese [4]. In peptidase family S8 (subtilisin
            family)
REFERENCE   1  [PMID:1367552]
  AUTHORS   Visser S, Robben AJ, Slangen CJ.
  TITLE     Specificity of a cell-envelope-located proteinase (PIII-type) from
            Lactococcus lactis subsp. cremoris AM1 in its action on bovine
            beta-casein.
  JOURNAL   Appl. Microbiol. Biotechnol. 35 (1991) 477-83.
  ORGANISM  Lactococcus lactis
REFERENCE   2  [PMID:1592148]
  AUTHORS   Monnet V, Ley JP, Gonzalez S.
  TITLE     Substrate specificity of the cell envelope-located proteinase of
            Lactococcus lactis subsp. lactis NCDO 763.
  JOURNAL   Int. J. Biochem. 24 (1992) 707-18.
  ORGANISM  Lactococcus lactis
REFERENCE   3  [PMID:8285671]
  AUTHORS   Exterkate FA, Alting AC, Bruinenberg PG.
  TITLE     Diversity of cell envelope proteinase specificity among strains of
            Lactococcus lactis and its relationship to charge characteristics of
            the substrate-binding region.
  JOURNAL   Appl. Environ. Microbiol. 59 (1993) 3640-7.
  ORGANISM  Lactococcus lactis
REFERENCE   4  [PMID:8398214]
  AUTHORS   Pritchard GG, Coolbear T.
  TITLE     The physiology and biochemistry of the proteolytic system in lactic
            acid bacteria.
  JOURNAL   FEMS. Microbiol. Rev. 12 (1993) 179-206.
  ORGANISM  Lactococcus lactis
ORTHOLOGY   KO: K01361  lactocepin
GENES       OIH: OB2932
            LLC: LACR_C42
            SPY: SPy_0416(prtS)
            SPZ: M5005_Spy_0341
            SPM: spyM18_0464
            SPG: SpyM3_0298(prtS)
            SPS: SPs1559
            SPH: MGAS10270_Spy0340(spyCEP)
            SPI: MGAS10750_Spy0339
            SPJ: MGAS2096_Spy0361(spyCEP)
            SPK: MGAS9429_Spy0344(spyCEP)
            SPF: SpyM51518(cspA)
            SPA: M6_Spy0367
            SPB: M28_Spy0329(prtS)
            SAG: SAG2053
            SAN: gbs2008
            SAK: SAK_1991(cspA)
            LJO: LJ1840
            LAC: LBA1235
            LDB: Ldb1189(prtB)
            LBU: LBUL_1105
            LCA: LSEI_2270
            CPF: CPF_1123
            CPR: CPR_0968(prtP)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.96
            ExPASy - ENZYME nomenclature database: 3.4.21.96
            ExplorEnz - The Enzyme Database: 3.4.21.96
            ERGO genome analysis and discovery system: 3.4.21.96
            BRENDA, the Enzyme Database: 3.4.21.96
            CAS: 205510-58-3
///
ENTRY       EC 3.4.21.97                Enzyme
NAME        assemblin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Cleaves -Ala!Ser- and -Ala!Ala- bonds in the scaffold protein
COMMENT     Involved in the breakdown of the scaffold protein during the late
            stages of assembly of the herpes-virus virion. Inhibited by
            diisopropyl fluorophosphate. Type example of peptidase family S21.
            Catalytic residues are His, Ser, His, a combination not known for
            any other peptidase, and the protein fold also is unique. Known from
            herpes viruses of several types, cytomegalovirus, Epstein-Barr virus
            and human herpesvirus 3
REFERENCE   1  [PMID:8797829]
  AUTHORS   Chen P, Tsuge H, Almassy RJ, Gribskov CL, Katoh S, Vanderpool DL,
            Margosiak SA, Pinko C, Matthews DA, Kan CC.
  TITLE     Structure of the human cytomegalovirus protease catalytic domain
            reveals a novel serine protease fold and catalytic triad.
  JOURNAL   Cell. 86 (1996) 835-43.
  ORGANISM  human cytomegalovirus
REFERENCE   2
  AUTHORS   Darke, P.L.
  TITLE     Herpesvirus assemblin.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Academic Press, London, 1998, p.
            470-472.
STRUCTURES  PDB: 1ID4  1IEC  1IED  1IEF  1IEG  1JQ6  1JQ7  1NJT  1NJU  1NKK  
                 1NKM  1O6E  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.97
            ExPASy - ENZYME nomenclature database: 3.4.21.97
            ExplorEnz - The Enzyme Database: 3.4.21.97
            ERGO genome analysis and discovery system: 3.4.21.97
            BRENDA, the Enzyme Database: 3.4.21.97
            CAS: 139691-88-6
///
ENTRY       EC 3.4.21.98                Enzyme
NAME        hepacivirin;
            Cpro-2;
            hepatitis C virus NS3 serine proteinase;
            NS3-4A serine proteinase complex
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of four peptide bonds in the viral precursor polyprotein,
            commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and
            Ser or Ala in P1'
COMMENT     Encoded by the genome of the viruses of the hepatitis C group, and
            contributes to the maturation of the precursor polyproteins. The
            enzyme is greatly activated by binding of the 54-residue NS4A
            'cofactor' protein also derived from the viral polyprotein. Type
            example of peptidase family S29. The crystallographic structure
            shows a chymotrypsin-like fold
REFERENCE   1  [PMID:8861917]
  AUTHORS   Kim JL, Morgenstern KA, Lin C, Fox T, Dwyer MD, Landro JA, Chambers
            SP, Markland W, Lepre CA, O'Malley ET, Harbeson SL, Rice CM, Murcko
            MA, Caron PR, Thomson JA.
  TITLE     Crystal structure of the hepatitis C virus NS3 protease domain
            complexed with a synthetic NS4A cofactor peptide.
  JOURNAL   Cell. 87 (1996) 343-55.
  ORGANISM  Hepatitis C virus
REFERENCE   2
  AUTHORS   Rice, C.M.
  TITLE     Hepatitis C virus polyprotein peptidase.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Academic Press, London, 1998, p.
            272-277.
STRUCTURES  PDB: 1JR6  1N64  1ONB  1RGQ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.98
            ExPASy - ENZYME nomenclature database: 3.4.21.98
            ExplorEnz - The Enzyme Database: 3.4.21.98
            ERGO genome analysis and discovery system: 3.4.21.98
            BRENDA, the Enzyme Database: 3.4.21.98
            CAS: 149885-80-3
///
ENTRY       EC 3.4.21.99                Enzyme
NAME        spermosin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolyses arginyl bonds, preferably with Pro in the P2 position
COMMENT     The enzyme from the ascidian (Prochordate) Halocynthia roretzi is
            localised in the sperm head, and released during sperm activation. A
            proline-rich region is involved in binding to the vitelline coat of
            the egg. Belongs in peptidase family S1 (trypsin family).
REFERENCE   1  [PMID:6365918]
  AUTHORS   Sawada H, Yokosawa H, Ishii S.
  TITLE     Purification and characterization of two types of trypsin-like
            enzymes from sperm of the ascidian (Prochordata) Halocynthia
            roretzi. Evidence for the presence of spermosin, a novel
            acrosin-like enzyme.
  JOURNAL   J. Biol. Chem. 259 (1984) 2900-4.
  ORGANISM  Halocynthia roretzi
REFERENCE   2  [PMID:6381175]
  AUTHORS   Sawada H, Yokosawa H, Someno T, Saino T, Ishii S.
  TITLE     Evidence for the participation of two sperm proteases, spermosin and
            acrosin, in fertilization of the ascidian, Halocynthia roretzi:
            inhibitory effects of leupeptin analogs on enzyme activities and
            fertilization.
  JOURNAL   Dev. Biol. 105 (1984) 246-9.
  ORGANISM  Halocynthia roretzi
REFERENCE   3  [PMID:8670234]
  AUTHORS   Sawada H, Iwasaki K, Kihara-Negishi F, Ariga H, Yokosawa H.
  TITLE     Localization, expression, and the role in fertilization of
            spermosin, an ascidian sperm trypsin-like protease.
  JOURNAL   Biochem. Biophys. Res. Commun. 222 (1996) 499-504.
  ORGANISM  Halocynthia roretzi
REFERENCE   4  [PMID:8914083]
  AUTHORS   Sawada H, Someno T.
  TITLE     Substrate specificity of ascidian sperm trypsin-like proteases,
            spermosin and acrosin.
  JOURNAL   Mol. Reprod. Dev. 45 (1996) 240-3.
  ORGANISM  Halocynthia roretzi
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.99
            ExPASy - ENZYME nomenclature database: 3.4.21.99
            ExplorEnz - The Enzyme Database: 3.4.21.99
            ERGO genome analysis and discovery system: 3.4.21.99
            BRENDA, the Enzyme Database: 3.4.21.99
///
ENTRY       EC 3.4.21.100               Enzyme
NAME        sedolysin;
            Pseudomonas sp. pepstatin-insensitive carboxyl proteinase;
            pseudomonapepsin;
            pseudomonalisin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolysis of the B chain of insulin at -Glu13!Ala-, -Leu15!Tyr- and
            -Phe25!Tyr-, and angiotensin I at -Tyr4!Ile-. A good synthetic
            substrate is Lys-Pro-Ile-Glu-Phe!Phe(NO2)-Arg-Leu.
COMMENT     An enzyme secreted by Pseudomonas sp. No. 101. Optimum pH is 4. It
            is distinguished from xanthomonapepsin by its insensitivity to EPNP
            and from scytalidopepsin B by this property and by its unrelated
            amino-acid sequence. Inhibited by tyrostatin, a peptide aldehyde
            [2]. Type example of peptidase family S53.
REFERENCE   1  [PMID:3548827]
  AUTHORS   Oda K, Sugitani M, Fukuhara K, Murao S.
  TITLE     Purification and properties of a pepstatin-insensitive carboxyl
            proteinase from a gram-negative bacterium.
  JOURNAL   Biochim. Biophys. Acta. 923 (1987) 463-9.
REFERENCE   2  [PMID:1562589]
  AUTHORS   Oda K, Nakatani H, Dunn BM.
  TITLE     Substrate specificity and kinetic properties of
            pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. No.
            101.
  JOURNAL   Biochim. Biophys. Acta. 1120 (1992) 208-14.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:11323721]
  AUTHORS   Wlodawer A, Li M, Dauter Z, Gustchina A, Uchida K, Oyama H, Dunn BM,
            Oda K.
  TITLE     Carboxyl proteinase from Pseudomonas defines a novel family of
            subtilisin-like enzymes.
  JOURNAL   Nat. Struct. Biol. 8 (2001) 442-6.
  ORGANISM  Pseudomonas sp.
REFERENCE   4  [PMID:12673349]
  AUTHORS   Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K.
  TITLE     Structural and enzymatic properties of the sedolisin family of
            serine-carboxyl peptidases.
  JOURNAL   Acta. Biochim. Pol. 50 (2003) 81-102.
  ORGANISM  Pseudomonas sp.
ORTHOLOGY   KO: K05998  pseudomonalisin
GENES       CVI: CV_1965 CV_1968
            BUR: Bcep18194_B0370 Bcep18194_B2163 Bcep18194_B2199
            BCN: Bcen_4443 Bcen_4475
            BCH: Bcen2424_3891
            BAM: Bamb_3301
            BPS: BPSS1734
            BPM: BURPS1710b_2563 BURPS1710b_A0811(scpB)
            BPL: BURPS1106A_A2358
            BPD: BURPS668_A2497 BURPS668_A2829
            BTE: BTH_II0646
STRUCTURES  PDB: 1NLU  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.100
            ExPASy - ENZYME nomenclature database: 3.4.21.100
            ExplorEnz - The Enzyme Database: 3.4.21.100
            ERGO genome analysis and discovery system: 3.4.21.100
            BRENDA, the Enzyme Database: 3.4.21.100
///
ENTRY       EC 3.4.21.101               Enzyme
NAME        xanthomonalisin;
            Xanthomonas aspartic proteinase;
            xanthomonapepsin;
            sedolisin-B
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Cleavage of casein
INHIBITOR   1,2-Epoxy-3-(p-Nitrophenoxy)propane [CPD:C04274]
COMMENT     Secreted by the bacterium Xanthomonas sp. Belongs in peptidase
            family S53.
REFERENCE   1
  AUTHORS   Oda, K., Nakazima, T., Terashita, T., Suzuki, K. and Murao, S.
  TITLE     Purification and properties of an S-PI(pepstatin Ac)-insensitive
            carboxyl proteinase from a Xanthomonas sp. bacterium.
  JOURNAL   Agric. Biol. Chem. 51 (1987) 3073-3080.
  ORGANISM  Xanthomonas sp.
REFERENCE   2  [PMID:12673349]
  AUTHORS   Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K.
  TITLE     Structural and enzymatic properties of the sedolisin family of
            serine-carboxyl peptidases.
  JOURNAL   Acta. Biochim. Pol. 50 (2003) 81-102.
  ORGANISM  Pseudomonas sp.
ORTHOLOGY   KO: K05999  xanthomonalisin
GENES       CVI: CV_1965 CV_1968
            BMA: BMAA0093
            BUR: Bcep18194_B1564
            BPS: BPSS1973
            BPM: BURPS1710b_A1080
            BTE: BTH_I2356 BTH_II0399
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.101
            ExPASy - ENZYME nomenclature database: 3.4.21.101
            ExplorEnz - The Enzyme Database: 3.4.21.101
            ERGO genome analysis and discovery system: 3.4.21.101
            BRENDA, the Enzyme Database: 3.4.21.101
            CAS: 113356-29-9
///
ENTRY       EC 3.4.21.102               Enzyme
NAME        C-terminal processing peptidase;
            CtpA gene product (Synechocystis sp.);
            photosystem II D1 protein processing peptidase;
            protease Re;
            tail-specific protease;
            Tsp protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    The enzyme shows specific recognition of a C-terminal tripeptide,
            Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is
            preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves
            at a variable distance from the C-terminus. A typical cleavage is
            -Ala-Ala!Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant
            chloroplast, the enzyme removes the C-terminal extension of the D1
            polypeptide of photosystem II
COMMENT     Proteolytic processing of the D1 protein of photosystem II is
            necessary to allow the light-driven assembly of the tetranuclear
            manganese cluster, which is responsible for photosynthetic water
            oxidation. The recognition of the substrate is mediated by a PDZ
            domain, a small protein module that promotes protein-protein
            interactions by binding to internal or C-terminal sequences of their
            partner proteins. Type example of peptidase family S41.
REFERENCE   1
  AUTHORS   Keiler, K.C. and Sauer, R.T.
  TITLE     Tsp protease.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Handbook of Proteolytic Enzymes,
            London, 1998, p. 460-461.
REFERENCE   2  [PMID:10715137]
  AUTHORS   Beebe KD, Shin J, Peng J, Chaudhury C, Khera J, Pei D.
  TITLE     Substrate recognition through a PDZ domain in tail-specific
            protease.
  JOURNAL   Biochemistry. 39 (2000) 3149-55.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:10966643]
  AUTHORS   Liao DI, Qian J, Chisholm DA, Jordan DB, Diner BA.
  TITLE     Crystal structures of the photosystem II D1 C-terminal processing
            protease.
  JOURNAL   Nat. Struct. Biol. 7 (2000) 749-53.
  ORGANISM  Scenedesmus obliquus
ORTHOLOGY   KO: K03797  carboxyl-terminal processing protease
GENES       OSA: 4340883
            CME: CMT227C
            ECO: b1830(prc)
            ECJ: JW1819(prc)
            ECE: Z2877(prc)
            ECS: ECs2540
            ECC: c2239(prc)
            ECI: UTI89_C2031(prc)
            ECP: ECP_1774
            ECV: APECO1_885(prc)
            ECW: EcE24377A_2059(prc)
            ECX: EcHS_A1921
            STY: STY1976(prc)
            STT: t1033(prc)
            SPT: SPA1028(prc)
            SEC: SC1841(prc)
            STM: STM1845(prc)
            YPE: YPO1705(prc)
            YPK: y1867(prc)
            YPM: YP_1730(prc)
            YPA: YPA_1816
            YPN: YPN_1925
            YPP: YPDSF_1743
            YPS: YPTB2376(prc)
            YPI: YpsIP31758_1672(prc)
            SFL: SF1395(prc)
            SFX: S1511(prc)
            SFV: SFV_1399(prc)
            SSN: SSON_1331(prc)
            SBO: SBO_1245(prc)
            SDY: SDY_1978(prc)
            ECA: ECA2459(prc)
            PLU: plu2682(prc)
            SGL: SG1316
            ENT: Ent638_2400
            SPE: Spro_2119
            HIN: HI1668(prc)
            HIT: NTHI1969(prc)
            HIP: CGSHiEE_03735
            HIQ: CGSHiGG_02065
            HDU: HD1010(prc)
            HSO: HS_1071(prc)
            PMU: PM0269(prc)
            MSU: MS0821(prc)
            APL: APL_0120(prc)
            ASU: Asuc_1084
            XFA: XF1823 XF1854 XF2704
            XFT: PD1042(prc) PD2057(ctpA)
            XCC: XCC0021(ctp) XCC3450(prc)
            XCB: XC_0021 XC_0714
            XCV: XCV0024(ctp) XCV0730(prc)
            XAC: XAC0023(ctp) XAC0669(prc)
            XOO: XOO3950(prc) XOO4586(ctp)
            XOM: XOO_3727(XOO3727) XOO_4322(XOO4322)
            VCH: VC1496 VCA0045
            VVU: VV1_2643
            VVY: VV1647
            VPA: VP1606
            VFI: VF1280
            PPR: PBPRA1921
            PAE: PA3257(prc) PA5134
            PAU: PA14_21880(tsp) PA14_67810(ctpA)
            PPU: PP_1719(prc) PP_5058
            PPF: Pput_4000 Pput_4931
            PST: PSPTO_3885(prc) PSPTO_5329
            PSB: Psyr_1599 Psyr_4887
            PSP: PSPPH_1587(prc) PSPPH_4918
            PFL: PFL_0368(prc) PFL_4394
            PFO: Pfl_0331 Pfl_1679
            PEN: PSEEN0378(ctpA) PSEEN1431
            PMY: Pmen_1321 Pmen_4248
            PAR: Psyc_0282(prc) Psyc_0702
            PCR: Pcryo_0309 Pcryo_0674
            PRW: PsycPRwf_0315 PsycPRwf_1430
            ACI: ACIAD0257 ACIAD0552(prc)
            SON: SO_0047 SO_2601
            SDN: Sden_1722 Sden_3700
            SFR: Sfri_2228
            SAZ: Sama_0058 Sama_1585
            SBL: Sbal_2447 Sbal_4334
            SBM: Shew185_0041 Shew185_2440
            SLO: Shew_1802 Shew_3808
            SPC: Sputcn32_0038 Sputcn32_2202
            SSE: Ssed_2483 Ssed_4472
            SPL: Spea_1935 Spea_4219
            SHE: Shewmr4_0043 Shewmr4_1673
            SHM: Shewmr7_0041 Shewmr7_1748
            SHN: Shewana3_0049 Shewana3_1778
            SHW: Sputw3181_1807 Sputw3181_4040
            ILO: IL1274(prc)
            CPS: CPS_2810(prc)
            PHA: PSHAa0364 PSHAa1678(prc)
            PAT: Patl_1993
            SDE: Sde_0492 Sde_1994
            PIN: Ping_2187
            MAQ: Maqu_2491 Maqu_3168
            CBU: CBU_1538
            LPN: lpg0499
            LPF: lpl0537
            LPP: lpp0561
            MCA: MCA2533
            TCX: Tcr_1781
            NOC: Noc_0030
            AEH: Mlg_1593 Mlg_2568
            HHA: Hhal_0121 Hhal_1210
            HCH: HCH_01350 HCH_02184(prc)
            CSA: Csal_0044 Csal_1519
            ABO: ABO_2276(ctpA)
            MMW: Mmwyl1_0725 Mmwyl1_2885
            AHA: AHA_2291(prc)
            RMA: Rmag_0620
            NME: NMB1332
            NMA: NMA1546
            NGO: NGO0572
            CVI: CV_3354(prc)
            RSO: RSc0352(RS03319)
            REU: Reut_A0303
            RME: Rmet_0250
            BMA: BMA3209
            BXE: Bxe_A4182
            BVI: Bcep1808_2958
            BUR: Bcep18194_A3806 Bcep18194_A6187
            BCN: Bcen_2244
            BCH: Bcen2424_2858
            BAM: Bamb_2913
            BPS: BPSL0442
            BPM: BURPS1710b_0661(ctpA)
            BTE: BTH_I0415
            PNU: Pnuc_1949
            BPE: BP0609(ctpA)
            BPA: BPP0297(ctpA)
            BBR: BB0300(ctpA)
            RFR: Rfer_1308
            POL: Bpro_0885
            PNA: Pnap_0926
            AAV: Aave_3859
            AJS: Ajs_3506
            VEI: Veis_0035
            MPT: Mpe_A1084
            HAR: HEAR2977(ctpA)
            MMS: mma_3224
            NEU: NE1782
            NET: Neut_0917
            NMU: Nmul_A1119
            DAR: Daro_0608 Daro_2146
            TBD: Tbd_2392
            MFA: Mfla_0383
            HPY: HP1350
            HPJ: jhp1269(prc)
            HPA: HPAG1_1297
            HHE: HH1618
            HAC: Hac_0279(ctpA)
            WSU: WS0608
            TDN: Tmden_0492
            CJE: Cj0511
            CJR: CJE0618(ctpA)
            CJJ: CJJ81176_0539(ctpA)
            CJU: C8J_0475
            CJD: JJD26997_1420(ctpA)
            CCV: CCV52592_2006
            CHA: CHAB381_0848
            ABU: Abu_2120(ctpA)
            GSU: GSU0969(ctpA-1) GSU1772(ctpA-2)
            GME: Gmet_1853 Gmet_2713
            GUR: Gura_1500 Gura_1935
            PCA: Pcar_1658 Pcar_1673
            PPD: Ppro_2409
            DVU: DVU2336
            DVL: Dvul_0923
            DDE: Dde_1437
            LIP: LI1123(prc)
            BBA: Bd0169(ctpA) Bd0967(prc)
            DPS: DP2556 DP3077
            ADE: Adeh_0669 Adeh_3796
            AFW: Anae109_0713 Anae109_3916
            MXA: MXAN_5808
            SAT: SYN_02024
            SFU: Sfum_3063
            RPR: RP228(ctp)
            RTY: RT0220(ctp)
            RCO: RC0310(ctp)
            RFE: RF_0989(ctp)
            RBE: RBE_0229(ctp)
            MLO: mll4000
            MES: Meso_3451
            PLA: Plav_1472
            SME: SMc03783(ctpA)
            SMD: Smed_3016
            ATU: Atu2774(ctpA)
            ATC: AGR_C_5034
            RET: RHE_CH04078(ctpA)
            RLE: RL4692(ctpA) pRL120279(prc)
            BME: BMEI0214
            BMF: BAB1_1845
            BMS: BR1837
            BMB: BruAb1_1816
            OAN: Oant_1062 Oant_4122
            BJA: bll4822(ctpA) blr0434(ctpA)
            BRA: BRADO0425(ctpA) BRADO4113(ctpA)
            BBT: BBta_0414(ctpA) BBta_4487(ctpA)
            RPA: RPA0169(ctpA)
            RPB: RPB_0258
            RPC: RPC_0166
            RPD: RPD_0566
            RPE: RPE_0271
            NWI: Nwi_0449
            NHA: Nham_0525
            BHE: BH01630(ctpA)
            BQU: BQ01530(ctpA)
            BBK: BARBAKC583_0324(ctpA)
            XAU: Xaut_2072
            CCR: CC_2028 CC_3435
            SIL: SPO3812
            SIT: TM1040_2755
            RSP: RSP_0932(ctpA)
            RSH: Rsph17029_2591
            RSQ: Rsph17025_2983
            JAN: Jann_0381
            RDE: RD1_0333(ctpA)
            PDE: Pden_2508
            MMR: Mmar10_2796
            HNE: HNE_3209
            ZMO: ZMO1667(ctpA)
            NAR: Saro_0055
            SAL: Sala_0574
            SWI: Swit_2547
            ELI: ELI_13245
            GOX: GOX0332 GOX1262
            GBE: GbCGDNIH1_0802 GbCGDNIH1_1714
            ACR: Acry_0038 Acry_0903
            RRU: Rru_A1232 Rru_A3204
            MAG: amb0303
            MGM: Mmc1_3509
            ABA: Acid345_2676 Acid345_4232
            SUS: Acid_1207 Acid_2796 Acid_5257 Acid_6221
            BSU: BG11794(ctpA)
            BHA: BH3599
            BAN: BA5414
            BAR: GBAA5414
            BAA: BA_0271
            BAT: BAS5032
            BCE: BC5184
            BCA: BCE_5288
            BCZ: BCZK4877
            BCY: Bcer98_3721
            BTK: BT9727_4862
            BTL: BALH_4678
            BLI: BL01439(ctpA)
            BLD: BLi02281(ctpA)
            BCL: ABC3062
            OIH: OB2490
            SAU: SA1253(ctpA)
            SAV: SAV1420(ctpA)
            SAM: MW1310(ctpA)
            SAR: SAR1432
            SAS: SAS1363
            SAC: SACOL1455
            SAB: SAB1275c
            SAO: SAOUHSC_01427
            SAJ: SaurJH9_1480
            SAH: SaurJH1_1509
            SEP: SE1113
            SER: SERP0996
            SHA: SH1486(ctpA)
            SSP: SSP1319
            LMO: lmo1851
            LMF: LMOf2365_1879
            LIN: lin1965
            LWE: lwe1870(ctpA)
            LPL: lp_1864(ctpA)
            LJO: LJ1104
            LCA: LSEI_1395
            EFA: EF1679
            STH: STH142 STH60
            CAC: CAC0499
            CPE: CPE0301
            CPF: CPF_0298
            CPR: CPR_0293
            CTC: CTC02507
            CNO: NT01CX_1272
            CTH: Cthe_1857 Cthe_1930
            CDF: CD3455
            CBE: Cbei_4866
            AMT: Amet_0177 Amet_4128
            CHY: CHY_0170
            DSY: DSY3259 DSY4862
            DRM: Dred_1600 Dred_3070
            SWO: Swol_0168 Swol_0248 Swol_1732
            CSC: Csac_0592 Csac_2341
            TTE: TTE1974(prc)
            MTA: Moth_0247
            SCO: SCO2967(SCE59.26c)
            SMA: SAV5106
            ACE: Acel_1729
            RXY: Rxyl_0877
            FNU: FN1205
            RBA: RB12148(prc) RB7408(ctpA)
            CTR: CT441(tsp)
            CTA: CTA_0481(tsp)
            CMU: TC0725
            CPN: CPn0555(tsp)
            CPA: CP0197
            CPJ: CPj0555(tsp)
            CPT: CpB0577
            CCA: CCA00187
            CAB: CAB183
            CFE: CF0819(tsp)
            PCU: pc0214(tsp) pc0246(tsp)
            BBU: BB0359(ctp)
            BGA: BG0359(ctp)
            BAF: BAPKO_0367(ctp)
            TPA: TP0277
            LIL: LA1449
            LIC: LIC12303
            LBJ: LBJ_1983(prc-2)
            LBL: LBL_1069(prc-2)
            SYN: slr0008(ctpA) slr0257(ctpB) slr1751(prc)
            SYW: SYNW1175
            SYC: syc0818_d syc1004_d(ctpB) syc1772_d(ctpA)
            SYF: Synpcc7942_0516 Synpcc7942_0712 Synpcc7942_2330
            SYD: Syncc9605_0484 Syncc9605_1299
            SYE: Syncc9902_1178 Syncc9902_1850
            SYG: sync_0548 sync_1675
            SYR: SynRCC307_0444(ctp) SynRCC307_1463(ctpA)
            SYX: SynWH7803_0532(ctp) SynWH7803_1476(ctpA)
            CYA: CYA_1795(prc-1) CYA_2818(prc-2)
            CYB: CYB_0822(prc-1) CYB_1628(prc-2)
            TEL: tll1406 tlr1607(ctpA)
            GVI: gll3102
            ANA: all1738 all2500 all3420
            AVA: Ava_0299 Ava_0432 Ava_0814 Ava_3440
            PMA: Pro1014(prc)
            PMM: PMM0677
            PMT: PMT0776
            PMN: PMN2A_0110 PMN2A_1701
            PMI: PMT9312_0330 PMT9312_0677
            PMB: A9601_03481 A9601_07321
            PMC: P9515_03561 P9515_07501
            PMF: P9303_14351 P9303_21861
            PMG: P9301_03501 P9301_07301
            PME: NATL1_04161 NATL1_07361
            TER: Tery_1138 Tery_2406 Tery_4518
            BTH: BT_2798 BT_3035 BT_4259
            BFR: BF4374 BF4547
            BFS: BF4172 BF4335
            PGI: PG0235 PG1060
            SRU: SRU_0779(prc)
            CHU: CHU_0098(prc) CHU_0632(prc) CHU_0689(ctpA)
            FJO: Fjoh_0529 Fjoh_0972 Fjoh_1430 Fjoh_2561
            FPS: FP0463 FP2345(prc)
            CTE: CT1054(prc) CT2258(ctpA-2)
            CCH: Cag_0729 Cag_0813 Cag_1991
            CPH: Cpha266_0042 Cpha266_1304 Cpha266_1328 Cpha266_1529
            PVI: Cvib_0018 Cvib_0940
            PLT: Plut_0014 Plut_0961 Plut_1022
            DEB: DehaBAV1_0346
            RRS: RoseRS_0582 RoseRS_3039
            RCA: Rcas_2135 Rcas_4069
            DRA: DR_1308 DR_1491 DR_1551
            DGE: Dgeo_0277 Dgeo_1216 Dgeo_1479
            TTH: TTC0929
            TTJ: TTHA1296
            AAE: aq_797(prc)
            TMA: TM0747
            TPT: Tpet_0182
            TME: Tmel_0224
            FNO: Fnod_1693
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.102
            ExPASy - ENZYME nomenclature database: 3.4.21.102
            ExplorEnz - The Enzyme Database: 3.4.21.102
            ERGO genome analysis and discovery system: 3.4.21.102
            BRENDA, the Enzyme Database: 3.4.21.102
            CAS: 113356-29-9
///
ENTRY       EC 3.4.21.103               Enzyme
NAME        physarolisin;
            Dictyostelium discoideum aspartic proteinase;
            Dictyostelium discoideum aspartic proteinase E;
            Physarum flavicomum aspartic proteinase;
            Physarum polycephalum acid proteinase;
            Physarum aspartic proteinase;
            physaropepsin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Milk clotting activity. Preferential cleavage of Gly8!Ser in B chain
            of insulin most rapidly, followed by Leu11!Val, Cys(SO3H)19!Gly and
            Phe24!Phe. No action on Ac-Phe-Tyr(I)2.
INHIBITOR   Methyl 2-diazoacetamidohexanoate [CPD:C04130]
COMMENT     Belongs in peptidase family S53. From the slime mold Physarum
            polycephalum. Is not inhibited by pepstatin, but is blocked by
            methyl 2-diazoacetamidohexanoate. Closely similar enzymes are found
            in Dictyostelium discoideum and P. flavicomum. Formerly included in
            EC 3.4.23.6.
REFERENCE   1
  AUTHORS   Henney, H.R. and Tavana, G.
  TITLE     Purification and some properties of an intracellular acid (carboxyl)
            proteinase from differentiating haploid cells of Physarum
            flavicomum.
  JOURNAL   Exp. Mycol. 6 (1982) 161-170.
  ORGANISM  Physarum flavicomum
REFERENCE   2
  AUTHORS   Murakami-Murofushi, K., Hiratsuka, A. and Ohta, J.
  TITLE     A novel acid protease from haploid amoebae of Physarum polycephalum,
            and its changes during mating and subsequent differentiation into
            diploid plasmodia.
  JOURNAL   Cell Struct. Funct. 9 (1984) 311-315.
  ORGANISM  Physarum polycephalum
REFERENCE   3
  AUTHORS   North, M.J. and Whyte, A.
  TITLE     Purification and characterization of two acid proteinases from
            Dictyostelium discoideum.
  JOURNAL   J. Gen. Microbiol. 130 (1984) 123-134.
  ORGANISM  Dictyostelium discoideum [GN:ddi]
REFERENCE   4  [PMID:12673349]
  AUTHORS   Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K.
  TITLE     Structural and enzymatic properties of the sedolisin family of
            serine-carboxyl peptidases.
  JOURNAL   Acta. Biochim. Pol. 50 (2003) 81-102.
  ORGANISM  Physarum polycephalum
REFERENCE   5  [PMID:12589815]
  AUTHORS   Nishii W, Ueki T, Miyashita R, Kojima M, Kim YT, Sasaki N,
            Murakami-Murofushi K, Takahashi K.
  TITLE     Structural and enzymatic characterization of physarolisin (formerly
            physaropepsin) proves that it is a unique serine-carboxyl
            proteinase.
  JOURNAL   Biochem. Biophys. Res. Commun. 301 (2003) 1023-9.
  ORGANISM  Physarum polycephalum
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.103
            ExPASy - ENZYME nomenclature database: 3.4.21.103
            ExplorEnz - The Enzyme Database: 3.4.21.103
            ERGO genome analysis and discovery system: 3.4.21.103
            BRENDA, the Enzyme Database: 3.4.21.103
            CAS: 94949-28-7
///
ENTRY       EC 3.4.21.104               Enzyme
NAME        mannan-binding lectin-associated serine protease-2;
            MASP-2;
            MASP2;
            MBP-associated serine protease-2;
            mannose-binding lectin-associated serine protease-2;
            p100;
            mannan-binding lectin-associated serine peptidase 2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Selective cleavage after Arg223 in complement component C2
            (-Ser-Leu-Gly-Arg!Lys-Ile-Gln-Ile) and after Arg76 in complement
            component C4 (-Gly-Leu-Gln-Arg!Ala-Leu-Glu-Ile)
COMMENT     Mannan-binding lectin (MBL) recognizes patterns of neutral
            carbohydrates, such as mannose and N-acetylglucosamine, on a wide
            range of microbial surfaces and is able to initiate activation of
            the lectin pathway of complement [7]. This enzyme displays
            C_overbar_1s_-like esterolytic activity (cf. EC 3.4.21.42,
            complement subcomponent C_overbar_1s_). It also cleaves C4 and C2
            with efficiencies that are relatively higher than those of EC
            3.4.21.42 [3]. Belongs in peptidase family S1A.
REFERENCE   1  [PMID:1460414]
  AUTHORS   Matsushita M, Fujita T.
  TITLE     Activation of the classical complement pathway by mannose-binding
            protein in association with a novel C1s-like serine protease.
  JOURNAL   J. Exp. Med. 176 (1992) 1497-502.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:9087411]
  AUTHORS   Thiel S, Vorup-Jensen T, Stover CM, Schwaeble W, Laursen SB, Poulsen
            K, Willis AC, Eggleton P, Hansen S, Holmskov U, Reid KB, Jensenius
            JC.
  TITLE     A second serine protease associated with mannan-binding lectin that
            activates complement.
  JOURNAL   Nature. 386 (1997) 506-10.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:11527969]
  AUTHORS   Rossi V, Cseh S, Bally I, Thielens NM, Jensenius JC, Arlaud GJ.
  TITLE     Substrate specificities of recombinant mannan-binding
            lectin-associated serine proteases-1 and -2.
  JOURNAL   J. Biol. Chem. 276 (2001) 40880-7.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:12538697]
  AUTHORS   Ambrus G, Gal P, Kojima M, Szilagyi K, Balczer J, Antal J, Graf L,
            Laich A, Moffatt BE, Schwaeble W, Sim RB, Zavodszky P.
  TITLE     Natural substrates and inhibitors of mannan-binding
            lectin-associated serine protease-1 and -2: a study on recombinant
            catalytic fragments.
  JOURNAL   J. Immunol. 170 (2003) 1374-82.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:15364579]
  AUTHORS   Harmat V, Gal P, Kardos J, Szilagyi K, Ambrus G, Vegh B, Naray-Szabo
            G, Zavodszky P.
  TITLE     The structure of MBL-associated serine protease-2 reveals that
            identical substrate specificities of C1s and MASP-2 are realized
            through different sets of enzyme-substrate interactions.
  JOURNAL   J. Mol. Biol. 342 (2004) 1533-46.
  ORGANISM  human [GN:hsa]
REFERENCE   6  [PMID:15060079]
  AUTHORS   Chen CB, Wallis R.
  TITLE     Two mechanisms for mannose-binding protein modulation of the
            activity of its associated serine proteases.
  JOURNAL   J. Biol. Chem. 279 (2004) 26058-65.
  ORGANISM  human [GN:hsa]
REFERENCE   7  [PMID:15728497]
  AUTHORS   Teillet F, Dublet B, Andrieu JP, Gaboriaud C, Arlaud GJ, Thielens
            NM.
  TITLE     The two major oligomeric forms of human mannan-binding lectin:
            chemical characterization, carbohydrate-binding properties, and
            interaction with MBL-associated serine proteases.
  JOURNAL   J. Immunol. 174 (2005) 2870-7.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04610  Complement and coagulation cascades
ORTHOLOGY   KO: K03993  mannan-binding lectin serine protease 2
GENES       HSA: 10747(MASP2)
            MMU: 17175(Masp2)
            RNO: 64459(Masp2)
            BTA: 505819(LOC505819)
            GGA: 407089(MASP2)
            XTR: 496446(masp2)
            DRE: 560277(LOC560277)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.104
            ExPASy - ENZYME nomenclature database: 3.4.21.104
            ExplorEnz - The Enzyme Database: 3.4.21.104
            ERGO genome analysis and discovery system: 3.4.21.104
            BRENDA, the Enzyme Database: 3.4.21.104
///
ENTRY       EC 3.4.21.105               Enzyme
NAME        rhomboid protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Cleaves type-1 transmembrane domains using a catalytic dyad composed
            of serine and histidine that are contributed by different
            transmembrane domains
COMMENT     These endopeptidases are multi-spanning membrane proteins. Their
            catalytic site is embedded within the membrane and they cleave
            type-1 transmembrane domains. A catalytic dyad is involved in
            proteolysis rather than a catalytic triad, as was thought previously
            [14]. They are important for embryo development in Drosophila
            melanogaster. Rhomboid is a key regulator of EGF receptor signalling
            and is responsible for cleaving Spitz, the main ligand of the
            Drosophila EGF receptor pathway. Belongs in peptidase family S54.
            Parasite-encoded rhomboid enzymes are also important for invasion of
            host cells by Toxoplasma and the malaria parasite. Rhomboids are
            widely conserved from bacteria to archaea to humans [9,13].
REFERENCE   1  [PMID:15684070]
  AUTHORS   Urban S, Wolfe MS.
  TITLE     Reconstitution of intramembrane proteolysis in vitro reveals that
            pure rhomboid is sufficient for catalysis and specificity.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 1883-8.
  ORGANISM  Providencia stuartii, Drosophila sp.
REFERENCE   2  [PMID:15753289]
  AUTHORS   Brossier F, Jewett TJ, Sibley LD, Urban S.
  TITLE     A spatially localized rhomboid protease cleaves cell surface
            adhesins essential for invasion by Toxoplasma.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 4146-51.
  ORGANISM  Toxoplasma gondii
REFERENCE   3  [PMID:15096522]
  AUTHORS   Herlan M, Bornhovd C, Hell K, Neupert W, Reichert AS.
  TITLE     Alternative topogenesis of Mgm1 and mitochondrial morphology depend
            on ATP and a functional import motor.
  JOURNAL   J. Cell. Biol. 165 (2004) 167-73.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4  [PMID:15047175]
  AUTHORS   Pascall JC, Brown KD.
  TITLE     Intramembrane cleavage of ephrinB3 by the human rhomboid family
            protease, RHBDL2.
  JOURNAL   Biochem. Biophys. Res. Commun. 317 (2004) 244-52.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:14732705]
  AUTHORS   Sik A, Passer BJ, Koonin EV, Pellegrini L.
  TITLE     Self-regulated cleavage of the mitochondrial intramembrane-cleaving
            protease PARL yields Pbeta, a nuclear-targeted peptide.
  JOURNAL   J. Biol. Chem. 279 (2004) 15323-9.
  ORGANISM  Drosophila sp.
REFERENCE   6  [PMID:12820957]
  AUTHORS   Urban S, Freeman M.
  TITLE     Substrate specificity of rhomboid intramembrane proteases is
            governed by helix-breaking residues in the substrate transmembrane
            domain.
  JOURNAL   Mol. Cell. 11 (2003) 1425-34.
  ORGANISM  Toxoplasma gondii
REFERENCE   7  [PMID:12707284]
  AUTHORS   Herlan M, Vogel F, Bornhovd C, Neupert W, Reichert AS.
  TITLE     Processing of Mgm1 by the rhomboid-type protease Pcp1 is required
            for maintenance of mitochondrial morphology and of mitochondrial
            DNA.
  JOURNAL   J. Biol. Chem. 278 (2003) 27781-8.
  ORGANISM  human [GN:hsa]
REFERENCE   8  [PMID:12774122]
  AUTHORS   McQuibban GA, Saurya S, Freeman M.
  TITLE     Mitochondrial membrane remodelling regulated by a conserved rhomboid
            protease.
  JOURNAL   Nature. 423 (2003) 537-41.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   9  [PMID:12620104]
  AUTHORS   Koonin EV, Makarova KS, Rogozin IB, Davidovic L, Letellier MC,
            Pellegrini L.
  TITLE     The rhomboids: a nearly ubiquitous family of intramembrane serine
            proteases that probably evolved by multiple ancient horizontal gene
            transfers.
  JOURNAL   Genome. Biol. 4 (2003) R19.
  ORGANISM  Providencia stuartii, Drosophila sp.
REFERENCE   10 [PMID:12200155]
  AUTHORS   Urban S, Freeman M.
  TITLE     Intramembrane proteolysis controls diverse signalling pathways
            throughout evolution.
  JOURNAL   Curr. Opin. Genet. Dev. 12 (2002) 512-8.
  ORGANISM  Drosophila sp.
REFERENCE   11 [PMID:12225666]
  AUTHORS   Urban S, Schlieper D, Freeman M.
  TITLE     Conservation of intramembrane proteolytic activity and substrate
            specificity in prokaryotic and eukaryotic rhomboids.
  JOURNAL   Curr. Biol. 12 (2002) 1507-12.
  ORGANISM  Providencia stuartii
REFERENCE   12 [PMID:12169630]
  AUTHORS   Urban S, Lee JR, Freeman M.
  TITLE     A family of Rhomboid intramembrane proteases activates all
            Drosophila membrane-tethered EGF ligands.
  JOURNAL   EMBO. J. 21 (2002) 4277-86.
  ORGANISM  Drosophila sp.
REFERENCE   13 [PMID:11672525]
  AUTHORS   Urban S, Lee JR, Freeman M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases.
  JOURNAL   Cell. 107 (2001) 173-82.
  ORGANISM  human [GN:hsa]
REFERENCE   14 [PMID:15616571]
  AUTHORS   Lemberg MK, Menendez J, Misik A, Garcia M, Koth CM, Freeman M.
  TITLE     Mechanism of intramembrane proteolysis investigated with purified
            rhomboid proteases.
  JOURNAL   EMBO. J. 24 (2005) 464-72.
REFERENCE   15 [PMID:17051161]
  AUTHORS   Wang Y, Zhang Y, Ha Y.
  TITLE     Crystal structure of a rhomboid family intramembrane protease.
  JOURNAL   Nature. 444 (2006) 179-80.
ORTHOLOGY   KO: K02857  rhomboid-related protein 1/2/3
            KO: K09650  rhomboid-like protein
GENES       HSA: 162494(RHBDL3) 54933(RHBDL2) 55486(PARL) 9028(RHBDL1)
            PTR: 453801(RHBDL1) 460877(PARL)
            MMU: 214951(Rhbdl1) 246104(Rhbdl3) 381038(Parl)
            RNO: 117025(Rhbdl1) 287556(Rhbdl4_predicted) 287979(Psarl)
                 298512(Rhbdl2_predicted)
            CFA: 482466(RHBDL2) 488100(PARL) 490092(RHBDL1) 491155(RHBDL3)
            BTA: 514191(PSARL) 514943(MGC148990) 535623(LOC535623)
            GGA: 417411(RHBDL3) 424767(PARL) 429205(RHBDL1)
            XLA: 444640(MGC84162) 495156(LOC495156)
            XTR: 549275(rhbdl2)
            DRE: 394179(rhbdl2) 541485(zgc:112986) 550128(rhbdl3)
            SPU: 576709(LOC576709) 580619(LOC580619)
            DME: Dmel_CG1004(rho) Dmel_CG33166(stet) Dmel_CG8972(rho-7)
            CEL: F26F4.3(rom-1) Y54E10A.14(rom-5)
            CME: CMP210C
            SCE: YGR101W(PCP1)
            AGO: AGOS_AAR092W
            PIC: PICST_6645
            CAL: CaO19_1643(CaO19.1643)
            CGR: CAGL0G07799g
            ANI: AN1372.2
            AFM: AFUA_1G09150
            AOR: AO090005001606
            CNE: CNG04190
            UMA: UM04721.1
            DDI: DDBDRAFT_0184385
STRUCTURES  PDB: 2GQC  2NR9  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.105
            ExPASy - ENZYME nomenclature database: 3.4.21.105
            ExplorEnz - The Enzyme Database: 3.4.21.105
            ERGO genome analysis and discovery system: 3.4.21.105
            BRENDA, the Enzyme Database: 3.4.21.105
///
ENTRY       EC 3.4.21.106               Enzyme
NAME        hepsin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Cleavage after basic amino-acid residues, with Arg strongly
            preferred to Lys
COMMENT     This type-II membrane-associated serine peptidase has been
            implicated in cell growth and development [1,3]. The enzyme has been
            shown to activate blood coagulation factor VII by cleavage of the
            Arg152!Ile153 peptide bound in BHK cells, thus indicating a possible
            role in the initiation of blood coagulation [2]. There is no
            cleavage after aromatic or aliphatic residues [1]. The occupancy of
            the S2 site is an absolute requirement for catalysis and a basic
            residue at that site is preferred to an aliphatic residue. The
            nature of the residue at S3 also affects hydrolysis, with Gln being
            much more favourable than Ala [1]. Belongs in peptidase family S1A.
REFERENCE   1  [PMID:9003440]
  AUTHORS   Zhukov A, Hellman U, Ingelman-Sundberg M.
  TITLE     Purification and characterization of hepsin from rat liver
            microsomes.
  JOURNAL   Biochim. Biophys. Acta. 1337 (1997) 85-95.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:7814421]
  AUTHORS   Kazama Y, Hamamoto T, Foster DC, Kisiel W.
  TITLE     Hepsin, a putative membrane-associated serine protease, activates
            human factor VII and initiates a pathway of blood coagulation on the
            cell surface leading to thrombin formation.
  JOURNAL   J. Biol. Chem. 270 (1995) 66-72.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:8346233]
  AUTHORS   Torres-Rosado A, O'Shea KS, Tsuji A, Chou SH, Kurachi K.
  TITLE     Hepsin, a putative cell-surface serine protease, is required for
            mammalian cell growth.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 7181-5.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.106
            ExPASy - ENZYME nomenclature database: 3.4.21.106
            ExplorEnz - The Enzyme Database: 3.4.21.106
            ERGO genome analysis and discovery system: 3.4.21.106
            BRENDA, the Enzyme Database: 3.4.21.106
///
ENTRY       EC 3.4.21.107               Enzyme
NAME        peptidase Do;
            DegP;
            DegP protease;
            HtrA;
            high temperature requirement protease A;
            HrtA heat shock protein;
            protease Do;
            Do protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Acts on substrates that are at least partially unfolded. The
            cleavage site P1 residue is normally between a pair of hydrophobic
            residues, such as Val!Val
COMMENT     This serine endopeptidase is essential for the clearance of
            denatured or aggregated proteins from the inner-membrane and
            periplasmic space in Escherichia coli. Natural substrates of the
            enzyme include colicin A lysis protein, pilin subunits and MalS from
            E. coli [3]. The enzyme has weak peptidase activity with casein and
            other non-native substrates [3]. The peptidase acts as a chaperone
            at low temperatures but switches to a peptidase (heat shock protein)
            at higher temperatures [1,6]. Molecular chaperones and peptidases
            control the folded state of proteins by recognizing hydrophobic
            stretches of polypeptide that become exposed by misfolding or
            unfolding. They then bind these hydrophobic substrates to prevent
            aggregation or assist in protein refolding. If attempts at refolding
            fail, then irreversibly damaged proteins are degraded by peptidases
            such as this enzyme [6]. Belongs in peptidase family S1C.
REFERENCE   1  [PMID:2180903]
  AUTHORS   Lipinska B, Zylicz M, Georgopoulos C.
  TITLE     The HtrA (DegP) protein, essential for Escherichia coli survival at
            high temperatures, is an endopeptidase.
  JOURNAL   J. Bacteriol. 172 (1990) 1791-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:2025286]
  AUTHORS   Seol JH, Woo SK, Jung EM, Yoo SJ, Lee CS, Kim KJ, Tanaka K, Ichihara
            A, Ha DB, Chung CH.
  TITLE     Protease Do is essential for survival of Escherichia coli at high
            temperatures: its identity with the htrA gene product.
  JOURNAL   Biochem. Biophys. Res. Commun. 176 (1991) 730-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:12270835]
  AUTHORS   Jones CH, Dexter P, Evans AK, Liu C, Hultgren SJ, Hruby DE.
  TITLE     Escherichia coli DegP protease cleaves between paired hydrophobic
            residues in a natural substrate: the PapA pilin.
  JOURNAL   J. Bacteriol. 184 (2002) 5762-71.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:6347072]
  AUTHORS   Swamy KH, Chung CH, Goldberg AL.
  TITLE     Isolation and characterization of protease do from Escherichia coli,
            a large serine protease containing multiple subunits.
  JOURNAL   Arch. Biochem. Biophys. 224 (1983) 543-54.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:9383148]
  AUTHORS   Pallen MJ, Wren BW.
  TITLE     The HtrA family of serine proteases.
  JOURNAL   Mol. Microbiol. 26 (1997) 209-21.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:11919638]
  AUTHORS   Krojer T, Garrido-Franco M, Huber R, Ehrmann M, Clausen T.
  TITLE     Crystal structure of DegP (HtrA) reveals a new protease-chaperone
            machine.
  JOURNAL   Nature. 416 (2002) 455-9.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K04771  serine protease Do
GENES       ECO: b0161(degP)
            ECJ: JW0157(degP)
            ECE: Z0173(htrA)
            ECS: ECs0165
            ECC: c0197(htrA)
            ECI: UTI89_C0177(degP)
            ECP: ECP_0171
            ECV: APECO1_1824(htrA)
            STY: STY0231(htrA)
            STT: t0210(htrA)
            SPT: SPA0215(htrA)
            SEC: SC0209(htrA)
            STM: STM0209(htrA)
            YPE: YPO3382(gsrA)
            YPK: y0807(htrA)
            YPM: YP_0303(gsrA)
            YPA: YPA_2881
            YPN: YPN_0709
            YPS: YPTB0749(htrA)
            SFL: SF0153(htrA)
            SFX: S0156(htrA)
            SFV: SFV_0146(htrA)
            SSN: SSON_0174(htrA)
            SBO: SBO_0150(htrA)
            SDY: SDY_0178(htrA)
            ECA: ECA3301(degP)
            BUC: BU228(htrA)
            BAS: BUsg222(htrA)
            BAB: bbp210(htrA)
            SGL: SG0505
            HDU: HD0260(degP)
            PMU: PM0734(htrA)
            XFA: XF0285
            XFT: PD0231(htrA)
            XOO: XOO0059(htrA)
            XOM: XOO_0115(XOO0115)
            VCH: VC0566
            VVY: VV0591
            VPA: VP0433
            VFI: VF2225
            CPS: CPS_4346(degP)
            CBU: CBU_0755(htrA)
            LPN: lpg1331(htrA)
            LPF: lpl1284(htrA)
            LPP: lpp1285(htrA)
            MCA: MCA2343(htrA)
            NMU: Nmul_A0510
            HPJ: jhp0405(htrA)
            HPA: HPAG1_0428
            HAC: Hac_1123(htrA)
            CJE: Cj1228c(htrA)
            CJR: CJE1363(htrA)
            RLE: RL1877
            BJA: blr5235(degP)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.107
            ExPASy - ENZYME nomenclature database: 3.4.21.107
            ExplorEnz - The Enzyme Database: 3.4.21.107
            ERGO genome analysis and discovery system: 3.4.21.107
            BRENDA, the Enzyme Database: 3.4.21.107
///
ENTRY       EC 3.4.21.108               Enzyme
NAME        HtrA2 peptidase;
            high temperature requirement protein A2;
            HtrA2;
            Omi stress-regulated endoprotease;
            serine proteinase OMI;
            HtrA2 protease;
            OMI/HtrA2 protease;
            HtrA2/Omi;
            Omi/HtrA2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Cleavage of non-polar aliphatic amino-acids at the P1 position, with
            a preference for Val, Ile and Met. At the P2 and P3 positions, Arg
            is selected most strongly with a secondary preference for other
            hydrophilic residues
COMMENT     This enzyme is upregulated in mammalian cells in response to stress
            induced by both heat shock and tunicamycin treatment [4]. It can
            induce apoptosis in a caspase-independent manner through its
            peptidase activity and in a caspase-dependent manner by disrupting
            the interaction between caspase and the inhibitor of apoptosis (IAP)
            [3]. Belongs in peptidase family S1C.
REFERENCE   1  [PMID:12835328]
  AUTHORS   Srinivasula SM, Gupta S, Datta P, Zhang Z, Hegde R, Cheong N,
            Fernandes-Alnemri T, Alnemri ES.
  TITLE     Inhibitor of apoptosis proteins are substrates for the mitochondrial
            serine protease Omi/HtrA2.
  JOURNAL   J. Biol. Chem. 278 (2003) 31469-72.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:10873535]
  AUTHORS   Savopoulos JW, Carter PS, Turconi S, Pettman GR, Karran EH, Gray CW,
            Ward RV, Jenkins O, Creasy CL.
  TITLE     Expression, purification, and functional analysis of the human
            serine protease HtrA2.
  JOURNAL   Protein. Expr. Purif. 19 (2000) 227-34.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:14512424]
  AUTHORS   Martins LM, Turk BE, Cowling V, Borg A, Jarrell ET, Cantley LC,
            Downward J.
  TITLE     Binding specificity and regulation of the serine protease and PDZ
            domains of HtrA2/Omi.
  JOURNAL   J. Biol. Chem. 278 (2003) 49417-27.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:10971580]
  AUTHORS   Gray CW, Ward RV, Karran E, Turconi S, Rowles A, Viglienghi D,
            Southan C, Barton A, Fantom KG, West A, Savopoulos J, Hassan NJ,
            Clinkenbeard H, Hanning C, Amegadzie B, Davis JB, Dingwall C, Livi
            GP, Creasy CL.
  TITLE     Characterization of human HtrA2, a novel serine protease involved in
            the mammalian cellular stress response.
  JOURNAL   Eur. J. Biochem. 267 (2000) 5699-710.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:11967569]
  AUTHORS   Li W, Srinivasula SM, Chai J, Li P, Wu JW, Zhang Z, Alnemri ES, Shi
            Y.
  TITLE     Structural insights into the pro-apoptotic function of mitochondrial
            serine protease HtrA2/Omi.
  JOURNAL   Nat. Struct. Biol. 9 (2002) 436-41.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K08669  HtrA serine peptidase 2
GENES       HSA: 27429(HTRA2)
            MMU: 64704(Htra2)
            RNO: 297376(Prss25)
            CFA: 475782(LOC475782)
            BTA: 523039(MGC155015)
            DRE: 561604(LOC561604)
STRUCTURES  PDB: 2PZD  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.108
            ExPASy - ENZYME nomenclature database: 3.4.21.108
            ExplorEnz - The Enzyme Database: 3.4.21.108
            ERGO genome analysis and discovery system: 3.4.21.108
            BRENDA, the Enzyme Database: 3.4.21.108
///
ENTRY       EC 3.4.21.109               Enzyme
NAME        matriptase;
            serine protease 14;
            membrane-type serine protease 1;
            MT-SP1;
            prostamin;
            serine protease TADG-15;
            tumor-associated differentially-expressed gene 15 protein;
            ST14;
            breast cancer 80 kDa protease;
            epithin;
            serine endopeptidase SNC19
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Cleaves various synthetic substrates with Arg or Lys at the P1
            position and prefers small side-chain amino acids, such as Ala and
            Gly, at the P2 position
COMMENT     This trypsin-like integral-membrane serine peptidase has been
            implicated in breast cancer invasion and metastasis [1,2]. The
            enzyme can activate hepatocyte growth factor/scattering factor
            (HGF/SF) by cleavage of the two-chain form at an Arg residue to give
            active alpha- and beta-HGF, but It does not activate plasminogen,
            which shares high homology with HGF [1]. The enzyme can also
            activate urokinase plasminogen activator (uPA), which initiates the
            matrix-degrading peptidase cascade [1,2]. Belongs in peptidase
            family S1A.
REFERENCE   1  [PMID:10962009]
  AUTHORS   Lee SL, Dickson RB, Lin CY.
  TITLE     Activation of hepatocyte growth factor and urokinase/plasminogen
            activator by matriptase, an epithelial membrane serine protease.
  JOURNAL   J. Biol. Chem. 275 (2000) 36720-5.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:10373424]
  AUTHORS   Lin CY, Anders J, Johnson M, Sang QA, Dickson RB.
  TITLE     Molecular cloning of cDNA for matriptase, a matrix-degrading serine
            protease with trypsin-like activity.
  JOURNAL   J. Biol. Chem. 274 (1999) 18231-6.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K08670  suppressor of tumorigenicity protein 14
GENES       HSA: 6768(ST14)
            MMU: 19143(St14)
            RNO: 114093(St14)
            CFA: 489278(ST14)
            GGA: 419731(ST14)
            XLA: 394363(st14-a)
            XTR: 448647(MGC89623)
            DRE: 678603(zgc:136950)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.109
            ExPASy - ENZYME nomenclature database: 3.4.21.109
            ExplorEnz - The Enzyme Database: 3.4.21.109
            ERGO genome analysis and discovery system: 3.4.21.109
            BRENDA, the Enzyme Database: 3.4.21.109
///
ENTRY       EC 3.4.21.110               Enzyme
NAME        C5a peptidase;
            streptococcal C5a peptidase;
            ScpA;
            ScpB;
            SCPA
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    The primary cleavage site is at His67!Lys68 in human C5a with a
            minor secondary cleavage site at Ala58!Ser59
COMMENT     This enzyme is a surface-associated subtilisin-like serine peptidase
            with very specific substrate specificity. Virulent strains of
            streptococci, including Streptococcus pyogenes, can evade human
            detection and phagocytosis by destroying the complement chemotaxin
            C5a. Cleavage of human C5a by this enzyme reduces the ability of C5a
            to bind receptors on the surface of polymorphonuclear neutrophil
            leukocytes (PMNLs) and thereby abolishes its chemotactic properties
            [1,4]. Belongs in peptidase family S8A.
REFERENCE   1  [PMID:3906656]
  AUTHORS   Wexler DE, Chenoweth DE, Cleary PP.
  TITLE     Mechanism of action of the group A streptococcal C5a inactivator.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 8144-8.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:1996961]
  AUTHORS   Bohnsack JF, Mollison KW, Buko AM, Ashworth JC, Hill HR.
  TITLE     Group B streptococci inactivate complement component C5a by enzymic
            cleavage at the C-terminus.
  JOURNAL   Biochem. J. 273 ( Pt 3) (1991) 635-40.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:1452354]
  AUTHORS   Cleary PP, Prahbu U, Dale JB, Wexler DE, Handley J.
  TITLE     Streptococcal C5a peptidase is a highly specific endopeptidase.
  JOURNAL   Infect. Immun. 60 (1992) 5219-23.
  ORGANISM  Streptococcus pyogenes
REFERENCE   4  [PMID:12354115]
  AUTHORS   Anderson ET, Wetherell MG, Winter LA, Olmsted SB, Cleary PP, Matsuka
            YV.
  TITLE     Processing, stability, and kinetic parameters of C5a peptidase from
            Streptococcus pyogenes.
  JOURNAL   Eur. J. Biochem. 269 (2002) 4839-51.
  ORGANISM  Streptococcus pyogenes
REFERENCE   5  [PMID:10809707]
  AUTHORS   Stafslien DK, Cleary PP.
  TITLE     Characterization of the streptococcal C5a peptidase using a
            C5a-green fluorescent protein fusion protein substrate.
  JOURNAL   J. Bacteriol. 182 (2000) 3254-8.
  ORGANISM  Streptococcus pyogenes
REFERENCE   6  [PMID:16565520]
  AUTHORS   Terao Y, Yamaguchi M, Hamada S, Kawabata S.
  TITLE     Multifunctional glyceraldehyde-3-phosphate dehydrogenase of
            Streptococcus pyogenes is essential for evasion from neutrophils.
  JOURNAL   J. Biol. Chem. 281 (2006) 14215-23.
  ORGANISM  Streptococcus pyogenes
ORTHOLOGY   KO: K08652  C5a peptidase
GENES       SPY: SPy_2010(scpA)
            SPZ: M5005_Spy_1715(scpA)
            SPM: spyM18_2074(scpA)
            SPG: SpyM3_1726(scpA)
            SPS: SPs1724
            SPH: MGAS10270_Spy1782(scpA)
            SPI: MGAS10750_Spy1807(scpA)
            SPJ: MGAS2096_Spy1744(scpA)
            SPK: MGAS9429_Spy1720(scpA)
            SPA: M6_Spy1718
            SPB: M28_Spy1700(scpA)
            SAN: gbs1308(scpB)
            SAK: SAK_1320(scpB)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.110
            ExPASy - ENZYME nomenclature database: 3.4.21.110
            ExplorEnz - The Enzyme Database: 3.4.21.110
            ERGO genome analysis and discovery system: 3.4.21.110
            BRENDA, the Enzyme Database: 3.4.21.110
///
ENTRY       EC 3.4.21.111               Enzyme
NAME        aqualysin 1;
            caldolysin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Exhibits low specificity towards esters of amino acids with small
            hydrophobic or aromatic residues at the P1 position
COMMENT     This enzyme from the extreme thermophile, Thermus aquaticus, is an
            alkaline serine peptidase. It has three subsites, S1, S2, and S3, in
            the substrate binding site. The preferred amino acids at the S1 site
            are Ala and Phe, at the S2 site are Ala and norleucine and at the S3
            site are Phe and Ile [3]. These specificities are similar to those
            of EC 3.4.21.64 (peptidase K) and EC 3.4.21.62 (subtilisin BPN')
            [3]. The enzyme displays broad specificity for cleavage of insulin
            B-chain and hydrolyses elastin substrates such as
            succinyl-(Ala)n-p-nitroanilide (n = 1,2,3) and some peptide esters
            [1,3]. Belongs in peptidase family S8A.
REFERENCE   1  [PMID:3162211]
  AUTHORS   Matsuzawa H, Tokugawa K, Hamaoki M, Mizoguchi M, Taguchi H, Terada
            I, Kwon ST, Ohta T.
  TITLE     Purification and characterization of aqualysin I (a thermophilic
            alkaline serine protease) produced by Thermus aquaticus YT-1.
  JOURNAL   Eur. J. Biochem. 171 (1988) 441-7.
  ORGANISM  Thermus aquaticus
REFERENCE   2  [PMID:9882104]
  AUTHORS   Tanaka T, Matsuzawa H, Kojima S, Kumagai I, Miura K, Ohta T.
  TITLE     P1 specificity of aqualysin I (a subtilisin-type serine protease)
            from Thermus aquaticus YT-1, using P1-substituted derivatives of
            Streptomyces subtilisin inhibitor.
  JOURNAL   Biosci. Biotechnol. Biochem. 62 (1998) 2035-8.
  ORGANISM  Thermus aquaticus
REFERENCE   3
  AUTHORS   Tanaka, T., Matsuzawa, H. and Ohta, T.
  TITLE     Substrate specificity of aqualysin I, a bacterial thermophilic
            alkaline serine protease from Thermus aquaticus YT-1: Comparison
            with proteinase K, subtilisin BPN' and subtilisin Carlsberg.
  JOURNAL   Biosci. Biotechnol. Biochem. 62 (1998) 2161-2165.
  ORGANISM  Thermus aquaticus
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.111
            ExPASy - ENZYME nomenclature database: 3.4.21.111
            ExplorEnz - The Enzyme Database: 3.4.21.111
            ERGO genome analysis and discovery system: 3.4.21.111
            BRENDA, the Enzyme Database: 3.4.21.111
///
ENTRY       EC 3.4.21.112               Enzyme
NAME        site-1 protease;
            mammalian subtilisin/kexin isozyme 1;
            membrane-bound transcription factor site-1 protease;
            proprotein convertase SKI-1;
            proprotein convertase SKI-1/S1PPS1;
            S1P endopeptidase;
            S1P protease;
            site-1 peptidase;
            site-1 protease;
            SKI-1;
            SREBP proteinase;
            SREBP S1 protease;
            SREBP-1 proteinase;
            SREBP-2 proteinase;
            sterol regulatory element-binding protein proteinase;
            sterol regulatory element-binding protein site 1 protease;
            sterol-regulated luminal protease;
            subtilase SKI-1;
            subtilase SKI-1/S1P;
            subtilisin/kexin-isozyme 1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Processes precursors containing basic and hydrophobic/aliphatic
            residues at P4 and P2, respectively, with a relatively relaxed
            acceptance of amino acids at P1 and P3
COMMENT     Cleaves sterol regulatory element-binding proteins (SREBPs) and
            thereby initiates a process by which the active fragments of the
            SREBPs translocate to the nucleus and activate genes controlling the
            synthesis and uptake of cholesterol and unsaturated fatty acids into
            the bloodstream [1]. The enzyme also processes pro-brain-derived
            neurotrophic factor and undergoes autocatalytic activation in the
            endoplasmic reticulum through sequential cleavages [5]. The enzyme
            can also process the unfolded protein response stress factor ATF6 at
            an Arg-His-Lys-Lys! site [4,8], and the envelope glycoprotein of the
            highly infectious Lassa virus [5,8] and Crimean Congo hemorrhagic
            fever virus at Arg-Arg-Lys-Lys! [7,8]. Belongs in peptidase family
            S8A.
REFERENCE   1  [PMID:10428864]
  AUTHORS   Espenshade PJ, Cheng D, Goldstein JL, Brown MS.
  TITLE     Autocatalytic processing of site-1 protease removes propeptide and
            permits cleavage of sterol regulatory element-binding proteins.
  JOURNAL   J. Biol. Chem. 274 (1999) 22795-804.
  ORGANISM  hamster, human [GN:hsa]
REFERENCE   2  [PMID:10428865]
  AUTHORS   Cheng D, Espenshade PJ, Slaughter CA, Jaen JC, Brown MS, Goldstein
            JL.
  TITLE     Secreted site-1 protease cleaves peptides corresponding to luminal
            loop of sterol regulatory element-binding proteins.
  JOURNAL   J. Biol. Chem. 274 (1999) 22805-12.
  ORGANISM  hamster
REFERENCE   3  [PMID:10644685]
  AUTHORS   Toure BB, Munzer JS, Basak A, Benjannet S, Rochemont J, Lazure C,
            Chretien M, Seidah NG.
  TITLE     Biosynthesis and enzymatic characterization of human SKI-1/S1P and
            the processing of its inhibitory prosegment.
  JOURNAL   J. Biol. Chem. 275 (2000) 2349-58.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:11163209]
  AUTHORS   Ye J, Rawson RB, Komuro R, Chen X, Dave UP, Prywes R, Brown MS,
            Goldstein JL.
  TITLE     ER stress induces cleavage of membrane-bound ATF6 by the same
            proteases that process SREBPs.
  JOURNAL   Mol. Cell. 6 (2000) 1355-64.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:11606739]
  AUTHORS   Lenz O, ter Meulen J, Klenk HD, Seidah NG, Garten W.
  TITLE     The Lassa virus glycoprotein precursor GP-C is proteolytically
            processed by subtilase SKI-1/S1P.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 12701-5.
  ORGANISM  hamster, human [GN:hsa], rat [GN:rno], mouse [GN:mmu]
REFERENCE   6  [PMID:11943176]
  AUTHORS   Basak A, Chretien M, Seidah NG.
  TITLE     A rapid fluorometric assay for the proteolytic activity of SKI-1/S1P
            based on the surface glycoprotein of the hemorrhagic fever Lassa
            virus.
  JOURNAL   FEBS. Lett. 514 (2002) 333-9.
REFERENCE   7  [PMID:12885882]
  AUTHORS   Vincent MJ, Sanchez AJ, Erickson BR, Basak A, Chretien M, Seidah NG,
            Nichol ST.
  TITLE     Crimean-Congo hemorrhagic fever virus glycoprotein proteolytic
            processing by subtilase SKI-1.
  JOURNAL   J. Virol. 77 (2003) 8640-9.
  ORGANISM  human [GN:hsa]
REFERENCE   8
  AUTHORS   Seidah, N.G. and Chretien, M.
  TITLE     Proprotein convertase SKI-1/S1P.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, 2nd ed., vol. 2, Elsevier, London,
            2004, p. 1845-1847.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.112
            ExPASy - ENZYME nomenclature database: 3.4.21.112
            ExplorEnz - The Enzyme Database: 3.4.21.112
            ERGO genome analysis and discovery system: 3.4.21.112
            BRENDA, the Enzyme Database: 3.4.21.112
///
ENTRY       EC 3.4.21.113               Enzyme
NAME        pestivirus NS3 polyprotein peptidase;
            border disease virus NS3 endopeptidase;
            BDV NS3 endopeptidase;
            bovine viral diarrhea virus NS3 endopeptidase;
            BVDV NS3 endopeptidase;
            classical swine fever virus NS3 endopeptidase;
            CSFV NS3 endopeptidase;
            p80
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Leu is conserved at position P1 for all four cleavage sites. Alanine
            is found at position P1' of the NS4A-NS4B cleavage site, whereas
            serine is found at position P1' of the NS3-NS4A, NS4B-NS5A and
            NS5A-NS5B cleavage sites
COMMENT     The polyprotein of noncytopathogenic pestiviruses is cleaved co- and
            post-translationally into at least 11 proteins (Npro, C, Erns, E1,
            E2, p7, NS2-3, NS4A, NS4B, NS5A, and NS5B) [2]. The genomes of
            cytopathogenic pestivirus strains express at least one additional
            protein, called NS3 (p80) [2]. This enzyme, which resides in the
            N-terminal region of NS3 (nonstructural protein 3), is essential for
            generation of its own C-terminus and for processing of the
            downstream cleavage sites, leading to the release of the pestivirus
            nonstructural proteins NS4A, NS4B, NS5A and NS5B [1,2]. Belongs in
            peptidase family S31.
REFERENCE   1  [PMID:1651596]
  AUTHORS   Wiskerchen M, Collett MS.
  TITLE     Pestivirus gene expression: protein p80 of bovine viral diarrhea
            virus is a proteinase involved in polyprotein processing.
  JOURNAL   Virology. 184 (1991) 341-50.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:9188613]
  AUTHORS   Tautz N, Elbers K, Stoll D, Meyers G, Thiel HJ.
  TITLE     Serine protease of pestiviruses: determination of cleavage sites.
  JOURNAL   J. Virol. 71 (1997) 5415-22.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:9188600]
  AUTHORS   Xu J, Mendez E, Caron PR, Lin C, Murcko MA, Collett MS, Rice CM.
  TITLE     Bovine viral diarrhea virus NS3 serine proteinase: polyprotein
            cleavage sites, cofactor requirements, and molecular model of an
            enzyme essential for pestivirus replication.
  JOURNAL   J. Virol. 71 (1997) 5312-22.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:10915606]
  AUTHORS   Tautz N, Kaiser A, Thiel HJ.
  TITLE     NS3 serine protease of bovine viral diarrhea virus: characterization
            of active site residues, NS4A cofactor domain, and protease-cofactor
            interactions.
  JOURNAL   Virology. 273 (2000) 351-63.
  ORGANISM  cow [GN:bta]
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.113
            ExPASy - ENZYME nomenclature database: 3.4.21.113
            ExplorEnz - The Enzyme Database: 3.4.21.113
            ERGO genome analysis and discovery system: 3.4.21.113
            BRENDA, the Enzyme Database: 3.4.21.113
///
ENTRY       EC 3.4.21.114               Enzyme
NAME        equine arterivirus serine peptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Cleavage of (Glu/Gln)!(Gly/Ser/Ala) in arterivirus replicase
            translation products ORF1a and ORF1ab
COMMENT     In the equine arterivirus (EAV), the replicase gene is translated
            into open reading frame 1a (ORF1a) and ORF1ab polyproteins. This
            enzyme is the main viral proteinase and processes five cleavage
            sites in the ORF1a protein and three in the ORF1b-encoded part of
            the ORF1ab protein to yield nonstructural proteins (nsp5-nsp12) [3].
            It combines the catalytic system of a chymotrypsin-like serine
            peptidase (His-Asp-Ser catalytic triad) with the substrate
            specificity of a 3C-like serine peptidase (Glu or Gln) at the P1
            position and a small amino-acid residue (Gly, Ser or Ala) at the P1'
            position [1]. Cleavage of ORF1ab by this enzyme is essential for
            viral replication [2]. Belongs in peptidase family S32.
REFERENCE   1  [PMID:8617757]
  AUTHORS   Snijder EJ, Wassenaar AL, van Dinten LC, Spaan WJ, Gorbalenya AE.
  TITLE     The arterivirus nsp4 protease is the prototype of a novel group of
            chymotrypsin-like enzymes, the 3C-like serine proteases.
  JOURNAL   J. Biol. Chem. 271 (1996) 4864-71.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:9971783]
  AUTHORS   van Dinten LC, Rensen S, Gorbalenya AE, Snijder EJ.
  TITLE     Proteolytic processing of the open reading frame 1b-encoded part of
            arterivirus replicase is mediated by nsp4 serine protease and Is
            essential for virus replication.
  JOURNAL   J. Virol. 73 (1999) 2027-37.
  ORGANISM  hamster, rabbit
REFERENCE   3  [PMID:12163505]
  AUTHORS   Barrette-Ng IH, Ng KK, Mark BL, Van Aken D, Cherney MM, Garen C,
            Kolodenko Y, Gorbalenya AE, Snijder EJ, James MN.
  TITLE     Structure of arterivirus nsp4. The smallest chymotrypsin-like
            proteinase with an alpha/beta C-terminal extension and alternate
            conformations of the oxyanion hole.
  JOURNAL   J. Biol. Chem. 277 (2002) 39960-6.
  ORGANISM  human [GN:hsa], Streptomyces griseus
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.114
            ExPASy - ENZYME nomenclature database: 3.4.21.114
            ExplorEnz - The Enzyme Database: 3.4.21.114
            ERGO genome analysis and discovery system: 3.4.21.114
            BRENDA, the Enzyme Database: 3.4.21.114
///
ENTRY       EC 3.4.21.115               Enzyme
NAME        infectious pancreatic necrosis birnavirus Vp4 peptidase;
            infectious pancreatic necrosis virus protease;
            IPNV Vp4 protease;
            IPNV Vp4 peptidase;
            NS protease;
            NS-associated protease;
            Vp4 protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Cleaves the (Ser/Thr)-Xaa-Ala!(Ser/Ala)-Gly motif in the polyprotein
            NH2-pVP2-VP4-VP3-COOH of infectious pancreatic necrosis virus at the
            pVP2-VP4 and VP4-VP3 junctions
COMMENT     Infectious pancreatic necrosis virus (IPNV) is a birnavirus that
            causes an acute, contagious disease in young salmonid fish [2]. As
            with most viruses that infect eukaryotic cells, the proteolytic
            processing of viral precursor proteins is a crucial step in the life
            cycle of this virus [2]. pVP2 is converted into VP2 by cleavage near
            the carboxy end of pVP2. This cleavage is most likely due to
            host-cell proteases rather than VP4 [2,3]. Differs from most serine
            peptidases in not having the catalytic triad Ser-His-Asp [2].
            Belongs in peptidase family S50.
REFERENCE   1  [PMID:2219718]
  AUTHORS   Manning DS, Leong JC.
  TITLE     Expression in Escherichia coli of the large genomic segment of
            infectious pancreatic necrosis virus.
  JOURNAL   Virology. 179 (1990) 16-25.
  ORGANISM  infectious pancreatic necrosis virus
REFERENCE   2  [PMID:10666235]
  AUTHORS   Petit S, Lejal N, Huet JC, Delmas B.
  TITLE     Active residues and viral substrate cleavage sites of the protease
            of the birnavirus infectious pancreatic necrosis virus.
  JOURNAL   J. Virol. 74 (2000) 2057-66.
  ORGANISM  infectious pancreatic necrosis virus
REFERENCE   3
  AUTHORS   Dobos, P.
  TITLE     The molecular biology of infectious pancreatic necrosis virus
            (IPNV).
  JOURNAL   Annu. Rev. Fish Dis. 5 (1995) 25-54.
  ORGANISM  infectious pancreatic necrosis virus
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.115
            ExPASy - ENZYME nomenclature database: 3.4.21.115
            ExplorEnz - The Enzyme Database: 3.4.21.115
            ERGO genome analysis and discovery system: 3.4.21.115
            BRENDA, the Enzyme Database: 3.4.21.115
///
ENTRY       EC 3.4.21.116               Enzyme
NAME        SpoIVB peptidase;
            sporulation factor IV B protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Self-cleaves Val52!Asn53, Ala62!Phe63 and Val74!Thr75 at the
            N-terminus of SpoIVB
COMMENT     This enzyme plays a central role in a regulatory checkpoint (the
            sigmaK checkpoint), which coordinates gene expression during the
            later stages of spore formation in Bacillus subtilis [1,3]. The
            enzyme activates proteolytic processing of a sporulation-specific
            sigma factor, pro-sigmaK, to its mature and active form, sigmaK, by
            self-cleavage [1,3]. The enzyme is also subject to secondary
            proteolysis, which presumably inactivates SpoIVB [3]. The enzyme is
            also essential for the formation of heat-resistant spores. Belongs
            in peptidase family S55.
REFERENCE   1  [PMID:10931284]
  AUTHORS   Wakeley PR, Dorazi R, Hoa NT, Bowyer JR, Cutting SM.
  TITLE     Proteolysis of SpolVB is a critical determinant in signalling of
            Pro-sigmaK processing in Bacillus subtilis.
  JOURNAL   Mol. Microbiol. 36 (2000) 1336-48.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   2  [PMID:11418578]
  AUTHORS   Hoa NT, Brannigan JA, Cutting SM.
  TITLE     The PDZ domain of the SpoIVB serine peptidase facilitates multiple
            functions.
  JOURNAL   J. Bacteriol. 183 (2001) 4364-73.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   3  [PMID:11741860]
  AUTHORS   Hoa NT, Brannigan JA, Cutting SM.
  TITLE     The Bacillus subtilis signaling protein SpoIVB defines a new family
            of serine peptidases.
  JOURNAL   J. Bacteriol. 184 (2002) 191-9.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   4  [PMID:12940997]
  AUTHORS   Dong TC, Cutting SM.
  TITLE     SpoIVB-mediated cleavage of SpoIVFA could provide the intercellular
            signal to activate processing of Pro-sigmaK in Bacillus subtilis.
  JOURNAL   Mol. Microbiol. 49 (2003) 1425-34.
  ORGANISM  Bacillus subtilis [GN:bsu]
ORTHOLOGY   KO: K06399  stage IV sporulation protein B
GENES       BSU: BG10311(spoIVB)
            BHA: BH2775(spoIVB)
            BAN: BA4396(spoIVB)
            BAR: GBAA4396(spoIVB)
            BAA: BA_4849
            BAT: BAS4077
            BCE: BC4172
            BCA: BCE_4245(spoIVB)
            BCZ: BCZK3926(spoIVB)
            BTK: BT9727_3915(spoIVB)
            BTL: BALH_3781(spoIVB)
            BLI: BL01519(spoIVB)
            BLD: BLi02594(spoIVB)
            BCL: ABC2458(spoIVB)
            OIH: OB1873(spoIVB)
            GKA: GK2388(spoIVB)
            STH: STH1833(spoIVB)
            CAC: CAC2072
            CPE: CPE1814
            CPF: CPF_2068
            CPR: CPR_1782(spoIVB)
            CTC: CTC01570
            CNO: NT01CX_1988
            CHY: CHY_1979
            DSY: DSY2342
            SWO: Swol_0589
            TTE: TTE1303
            MTA: Moth_1506
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.116
            ExPASy - ENZYME nomenclature database: 3.4.21.116
            ExplorEnz - The Enzyme Database: 3.4.21.116
            ERGO genome analysis and discovery system: 3.4.21.116
            BRENDA, the Enzyme Database: 3.4.21.116
///
ENTRY       EC 3.4.21.117               Enzyme
NAME        stratum corneum chymotryptic enzyme;
            kallikrein 7;
            SCCE;
            KLK7;
            PRSS6;
            hK7
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Cleavage of proteins with aromatic side chains in the P1 position
COMMENT     This enzyme has wide substrate specificity, being able to degrade
            heat-denatured bovine casein and the alpha-chain of native human
            fibrinogen. It cleaves the B chain of bovine insulin at Leu6!Cya7,
            Tyr16!Leu17, Phe25!Tyr26 and Tyr26!Thr27 [1]. It is thought to play
            a role in the desquamation (skin-shedding) of the outer layer of
            skin, the stratum corneum, by degrading intercellular cohesive
            structures [1,2]. Belongs in peptidase family S1A.
REFERENCE   1  [PMID:7794273]
  AUTHORS   Skytt A, Stromqvist M, Egelrud T.
  TITLE     Primary substrate specificity of recombinant human stratum corneum
            chymotryptic enzyme.
  JOURNAL   Biochem. Biophys. Res. Commun. 211 (1995) 586-9.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:8393902]
  AUTHORS   Egelrud T.
  TITLE     Purification and preliminary characterization of stratum corneum
            chymotryptic enzyme: a proteinase that may be involved in
            desquamation.
  JOURNAL   J. Invest. Dermatol. 101 (1993) 200-4.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:8034709]
  AUTHORS   Hansson L, Stromqvist M, Backman A, Wallbrandt P, Carlstein A,
            Egelrud T.
  TITLE     Cloning, expression, and characterization of stratum corneum
            chymotryptic enzyme. A skin-specific human serine proteinase.
  JOURNAL   J. Biol. Chem. 269 (1994) 19420-6.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:10974542]
  AUTHORS   Yousef GM, Scorilas A, Magklara A, Soosaipillai A, Diamandis EP.
  TITLE     The KLK7 (PRSS6) gene, encoding for the stratum corneum chymotryptic
            enzyme is a new member of the human kallikrein gene family - genomic
            characterization, mapping, tissue expression and hormonal
            regulation.
  JOURNAL   Gene. 254 (2000) 119-28.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:15191543]
  AUTHORS   Vasilopoulos Y, Cork MJ, Murphy R, Williams HC, Robinson DA, Duff
            GW, Ward SJ, Tazi-Ahnini R.
  TITLE     Genetic association between an AACC insertion in the 3'UTR of the
            stratum corneum chymotryptic enzyme gene and atopic dermatitis.
  JOURNAL   J. Invest. Dermatol. 123 (2004) 62-6.
  ORGANISM  human [GN:hsa], mouse [GN:mmu]
ORTHOLOGY   KO: K08668  kallikrein 7 (chymotryptic, stratum corneum)
GENES       HSA: 5650(KLK7)
            PTR: 468973(KLK7)
            MMU: 23993(Klk7)
            RNO: 292852(Klk7_predicted)
            CFA: 611780(KLK7)
            BTA: 506380(KLK7)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.117
            ExPASy - ENZYME nomenclature database: 3.4.21.117
            ExplorEnz - The Enzyme Database: 3.4.21.117
            ERGO genome analysis and discovery system: 3.4.21.117
            BRENDA, the Enzyme Database: 3.4.21.117
///
ENTRY       EC 3.4.21.118               Enzyme
NAME        kallikrein 8;
            KLK8;
            PRSS19;
            human kallikrein 8;
            hK8;
            mK8;
            ovasin;
            tumor-associated differentially expressed gene 14;
            TADG-14;
            NP;
            neuropsin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Cleavage of amide substrates following the basic amino acids Arg or
            Lys at the P1 position, with a preference for Arg over Lys
COMMENT     The enzyme is activated by removal of an N-terminal prepropeptide
            [2,4]. The highest amidolytic activity is observed using
            Boc-Val-Pro-Arg!7-amido-4-methylcoumarin, which is a substrate of
            alpha-thrombin [2,4]. Substrates lacking basic amino acids in the P1
            position are not cleaved [4]. The enzyme degrades casein,
            fibronectin, gelatin, collagen type IV, fibrinogen, and
            high-molecular-mass kininogen [3] and is associated with diseases
            such as ovarian cancer and Alzheimer's disease [4]. Belongs in
            peptidase family S1A.
REFERENCE   1  [PMID:7623137]
  AUTHORS   Chen ZL, Yoshida S, Kato K, Momota Y, Suzuki J, Tanaka T, Ito J,
            Nishino H, Aimoto S, Kiyama H, et al.
  TITLE     Expression and activity-dependent changes of a novel limbic-serine
            protease gene in the hippocampus.
  JOURNAL   J. Neurosci. 15 (1995) 5088-97.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:9556608]
  AUTHORS   Shimizu C, Yoshida S, Shibata M, Kato K, Momota Y, Matsumoto K,
            Shiosaka T, Midorikawa R, Kamachi T, Kawabe A, Shiosaka S.
  TITLE     Characterization of recombinant and brain neuropsin, a
            plasticity-related serine protease.
  JOURNAL   J. Biol. Chem. 273 (1998) 11189-96.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:16337200]
  AUTHORS   Rajapakse S, Ogiwara K, Takano N, Moriyama A, Takahashi T.
  TITLE     Biochemical characterization of human kallikrein 8 and its possible
            involvement in the degradation of extracellular matrix proteins.
  JOURNAL   FEBS. Lett. 579 (2005) 6879-84.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:16800733]
  AUTHORS   Kishi T, Cloutier SM, Kundig C, Deperthes D, Diamandis EP.
  TITLE     Activation and enzymatic characterization of recombinant human
            kallikrein 8.
  JOURNAL   Biol. Chem. 387 (2006) 723-31.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K08650  kallikrein 8 (neuropsin/ovasin)
GENES       HSA: 11202(KLK8)
            PTR: 456239(KLK8)
            MMU: 259277(Klk8)
            RNO: 308565(Klk8)
            CFA: 484352(KLK8)
            BTA: 618438(LOC618438)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.118
            ExPASy - ENZYME nomenclature database: 3.4.21.118
            ExplorEnz - The Enzyme Database: 3.4.21.118
            ERGO genome analysis and discovery system: 3.4.21.118
            BRENDA, the Enzyme Database: 3.4.21.118
///
ENTRY       EC 3.4.21.119               Enzyme
NAME        kallikrein 13;
            KLK13;
            kallikrein mK13;
            mGK-13;
            mK13;
            mKLK13;
            prorenin converting enzyme 1;
            PRECE-1;
            prorenin-converting enzyme;
            PRECE;
            proteinase P
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Hydrolyses mouse Ren2 protein (a species of prorenin present in the
            submandibular gland) on the carboxy side of the arginine residue at
            the Lys-Arg! pair in the N-terminus, to yield mature renin
COMMENT     The enzyme is specific for prorenin from the mouse submandibular
            gland, as prorenin from the mouse kidney (Ren1) and human prorenin
            are not substrates [1]. Site-directed mutagenesis studies have shown
            that the enzyme will also cleave prorenin when Lys-Arg is replaced
            by Arg-Arg or Gln-Arg but the rate of reaction is much slower when
            Lys-Lys is used. This enzyme is also able to process
            pro-interleukin-1beta (pro-IL-1beta) in mouse submandibular gland to
            form IL-1beta [4]. Belongs in peptidase family S1A.
REFERENCE   1  [PMID:2250008]
  AUTHORS   Nakayama K, Kim WS, Nakagawa T, Nagahama M, Murakami K.
  TITLE     Substrate specificity of prorenin converting enzyme of mouse
            submandibular gland. Analysis using site-directed mutagenesis.
  JOURNAL   J. Biol. Chem. 265 (1990) 21027-31.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:2180937]
  AUTHORS   Kim WS, Hatsuzawa K, Ishizuka Y, Hashiba K, Murakami K, Nakayama K.
  TITLE     A processing enzyme for prorenin in mouse submandibular gland.
            Purification and characterization.
  JOURNAL   J. Biol. Chem. 265 (1990) 5930-3.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:9507064]
  AUTHORS   Kikkawa Y, Yamanaka N, Tada J, Kanamori N, Tsumura K, Hosoi K.
  TITLE     Prorenin processing and restricted endoproteolysis by mouse tissue
            kallikrein family enzymes (mK1, mK9, mK13, and mK22).
  JOURNAL   Biochim. Biophys. Acta. 1382 (1998) 55-64.
  ORGANISM  mouse [GN:mmu]
REFERENCE   4  [PMID:16423834]
  AUTHORS   Yao C, Karabasil MR, Purwanti N, Li X, Akamatsu T, Kanamori N, Hosoi
            K.
  TITLE     Tissue kallikrein mK13 is a candidate processing enzyme for the
            precursor of interleukin-1beta in the submandibular gland of mice.
  JOURNAL   J. Biol. Chem. 281 (2006) 7968-76.
  ORGANISM  mouse [GN:mmu]
ORTHOLOGY   KO: K09462  glandular kallikrein 13
GENES       MMU: 13647(Egfbp2)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.119
            ExPASy - ENZYME nomenclature database: 3.4.21.119
            ExplorEnz - The Enzyme Database: 3.4.21.119
            ERGO genome analysis and discovery system: 3.4.21.119
            BRENDA, the Enzyme Database: 3.4.21.119
///
ENTRY       EC 3.4.21.120               Enzyme
NAME        oviductin;
            oviductal protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Serine endopeptidases
REACTION    Preferential cleavage at Gly-Ser-Arg373! of glycoprotein gp43 in
            Xenopus laevis coelemic egg envelope to yield gp41
COMMENT     The egg envelope of the South African clawed frog (Xenopus laevis)
            is modified during transit of the egg through the pars rectus
            oviduct, changing the egg envelope from an unfertilizable form to a
            fertilizable form. This process involves the conversion of
            glycoprotein gp43 to gp41 (ZPC) by the pars recta protease
            oviductin. It is thought that the enzymatically active protease
            molecule comprises the N-terminal protease domain coupled to two
            C-terminal CUB domains, which are related to the mammalian
            spermadhesin molecules implicated in mediating sperm-envelope
            interactions [2]. The enzyme is also found in the Japanese toad
            (Bufo japonicus) [3]. Belongs in peptidase family S1.
REFERENCE   1  [PMID:1581303]
  AUTHORS   Hardy DM, Hedrick JL.
  TITLE     Oviductin. Purification and properties of the oviductal protease
            that processes the molecular weight 43,000 glycoprotein of the
            Xenopus laevis egg envelope.
  JOURNAL   Biochemistry. 31 (1992) 4466-72.
REFERENCE   2  [PMID:10084976]
  AUTHORS   Lindsay LL, Wieduwilt MJ, Hedrick JL.
  TITLE     Oviductin, the Xenopus laevis oviductal protease that processes egg
            envelope glycoprotein gp43, increases sperm binding to envelopes,
            and is translated as part of an unusual mosaic protein composed of
            two protease and several CUB domains.
  JOURNAL   Biol. Reprod. 60 (1999) 989-95.
REFERENCE   3  [PMID:11846486]
  AUTHORS   Hiyoshi M, Takamune K, Mita K, Kubo H, Sugimoto Y, Katagiri C.
  TITLE     Oviductin, the oviductal protease that mediates gamete interaction
            by affecting the vitelline coat in Bufo japonicus: its molecular
            cloning and analyses of expression and posttranslational activation.
  JOURNAL   Dev. Biol. 243 (2002) 176-84.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.21.120
            ExPASy - ENZYME nomenclature database: 3.4.21.120
            ExplorEnz - The Enzyme Database: 3.4.21.120
            ERGO genome analysis and discovery system: 3.4.21.120
            BRENDA, the Enzyme Database: 3.4.21.120
///
ENTRY       EC 3.4.22.1                 Enzyme
NAME        cathepsin B;
            cathepsin B1 (obsolete);
            cathepsin II
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Hydrolysis of proteins with broad specificity for peptide bonds.
            Preferentially cleaves -Arg-Arg! bonds in small molecule substrates
            (thus differing from cathepsin L). In addition to being an
            endopeptidase, shows peptidyl-dipeptidase activity, liberating
            C-terminal dipeptides
COMMENT     An intracellular (lysosomal) enzyme in peptidase family C1 (papain
            family)
REFERENCE   1  [PMID:7458901]
  AUTHORS   Bond JS, Barrett AJ.
  TITLE     Degradation of fructose-1,6-bisphosphate aldolase by cathepsin B.
  JOURNAL   Biochem. J. 189 (1980) 17-25.
  ORGANISM  rabbit
REFERENCE   2  [PMID:7043200]
  AUTHORS   Barrett AJ, Kirschke H.
  TITLE     Cathepsin B, Cathepsin H, and cathepsin L.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 535-61.
REFERENCE   3  [PMID:3312190]
  AUTHORS   Polgar L, Csoma C.
  TITLE     Dissociation of ionizing groups in the binding cleft inversely
            controls the endo- and exopeptidase activities of cathepsin B.
  JOURNAL   J. Biol. Chem. 262 (1987) 14448-53.
REFERENCE   4
  AUTHORS   Barrett, A.J., Buttle, D.J. and Mason, R.W.
  TITLE     Lysosomal cysteine proteinases.
  JOURNAL   ISI Atlas of Science. Biochemistry 1 (1988) 256-260.
REFERENCE   5  [PMID:3342870]
  AUTHORS   Kirschke H, Wikstrom P, Shaw E.
  TITLE     Active center differences between cathepsins L and B: the S1 binding
            region.
  JOURNAL   FEBS. Lett. 228 (1988) 128-30.
PATHWAY     PATH: map04612  Antigen processing and presentation
ORTHOLOGY   KO: K01363  cathepsin B
GENES       HSA: 1508(CTSB)
            PTR: 463993(CTSB)
            MMU: 13030(Ctsb)
            RNO: 64529(Ctsb)
            CFA: 486077(CTSB)
            BTA: 281105(CTSB)
            GGA: 396329(CTSB)
            XLA: 379257(MGC53360) 380102(cg10992)
            XTR: 394833(MGC75969)
            DRE: 394030(zgc:55862) 406645(ctsba)
            SPU: 582922(LOC582922)
            DME: Dmel_CG10992
            CEL: C52E4.1(cpr-1) F36D3.9(cpr-2) T10H4.12(cpr-3)
            TET: TTHERM_00079660 TTHERM_00079670 TTHERM_00083480
                 TTHERM_00083500 TTHERM_00641150
STRUCTURES  PDB: 1CPJ  1CSB  1CTE  1GMY  1HUC  1ITO  1MIR  1PBH  1QDQ  1SP4  
                 1THE  2DC6  2DC7  2DC8  2DC9  2DCA  2DCB  2DCC  2DCD  2IPP  
                 2PBH  3PBH  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.1
            ExPASy - ENZYME nomenclature database: 3.4.22.1
            ExplorEnz - The Enzyme Database: 3.4.22.1
            ERGO genome analysis and discovery system: 3.4.22.1
            BRENDA, the Enzyme Database: 3.4.22.1
            CAS: 9047-22-7
///
ENTRY       EC 3.4.22.2                 Enzyme
NAME        papain;
            papayotin;
            summetrin;
            velardon;
            papaine;
            Papaya peptidase I
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Hydrolysis of proteins with broad specificity for peptide bonds, but
            preference for an amino acid bearing a large hydrophobic side chain
            at the P2 position. Does not accept Val in P1'
COMMENT     Type example of peptidase family C1 from latex of the papaya (Carica
            papaya) fruit. Inhibited by compound E-64 and proteins of the
            cystatin family.
REFERENCE   1  [PMID:3889350]
  AUTHORS   Kamphuis IG, Drenth J, Baker EN.
  TITLE     Thiol proteases. Comparative studies based on the high-resolution
            structures of papain and actinidin, and on amino acid sequence
            information for cathepsins B and H, and stem bromelain.
  JOURNAL   J. Mol. Biol. 182 (1985) 317-29.
  ORGANISM  Carica papaya, Actinidia chinensis
REFERENCE   2
  AUTHORS   Menard, R. and Storer, A.C.
  TITLE     Papain.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Academic Press, London, 1998, p.
            555-557.
ORTHOLOGY   KO: K06000  papain
GENES       PFA: PFI0135c
STRUCTURES  PDB: 1CVZ  1KHP  1KHQ  1PAD  1PIP  1POP  1PPD  1STF  2CIO  2PAD  
                 4PAD  5PAD  6PAD  9PAP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.2
            ExPASy - ENZYME nomenclature database: 3.4.22.2
            ExplorEnz - The Enzyme Database: 3.4.22.2
            ERGO genome analysis and discovery system: 3.4.22.2
            BRENDA, the Enzyme Database: 3.4.22.2
            CAS: 9001-73-4
///
ENTRY       EC 3.4.22.3                 Enzyme
NAME        ficain;
            ficin;
            debricin;
            higueroxyl delabarre
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Similar to that of papain
COMMENT     The major proteolytic component of the latex of fig, Ficus glabrata.
            Cysteine endopeptidases with similar properties are present in other
            members of the large genus Ficus. In peptidase family C1 (papain
            family).
REFERENCE   1
  AUTHORS   Liener, I.E. and Friedenson, B.
  TITLE     Ficin.
  JOURNAL   Methods Enzymol. 19 (1970) 261-273.
  ORGANISM  Ficus glabrata, Ficus carica, Ficus anthelmintica
REFERENCE   2
  AUTHORS   Brocklehurst, K., Willenbrock, F. and Salih, E.
  TITLE     Cysteine proteinases.
  JOURNAL   In: Neuberger, A. and Brocklehurst, K. (Eds.), New Comprehensive
            Biochemistry: Hydrolytic Enzymes, Elsevier, Amsterdam, 1987, p.
            39-158.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.3
            ExPASy - ENZYME nomenclature database: 3.4.22.3
            ExplorEnz - The Enzyme Database: 3.4.22.3
            ERGO genome analysis and discovery system: 3.4.22.3
            BRENDA, the Enzyme Database: 3.4.22.3
            CAS: 9001-33-6
///
ENTRY       EC 3.4.22.4       Obsolete  Enzyme
NAME        Transferred to 3.4.22.32 and 3.4.22.33
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
COMMENT     Transferred entry: now EC 3.4.22.32 (stem bromelain) and EC
            3.4.22.33 (fruit bromelain) (EC 3.4.22.4 created 1972, deleted 1992
            [EC 3.4.22.5 created 1972, incorporated 1978])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.4
            ExPASy - ENZYME nomenclature database: 3.4.22.4
            ExplorEnz - The Enzyme Database: 3.4.22.4
            ERGO genome analysis and discovery system: 3.4.22.4
            BRENDA, the Enzyme Database: 3.4.22.4
///
ENTRY       EC 3.4.22.5       Obsolete  Enzyme
NAME        Transferred to 3.4.22.32 and 3.4.22.33
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
COMMENT     Transferred entry: now EC 3.4.22.32 (stem bromelain) and EC
            3.4.22.33 (fruit bromelain) (EC 3.4.22.5 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.5
            ExPASy - ENZYME nomenclature database: 3.4.22.5
            ExplorEnz - The Enzyme Database: 3.4.22.5
            ERGO genome analysis and discovery system: 3.4.22.5
            BRENDA, the Enzyme Database: 3.4.22.5
///
ENTRY       EC 3.4.22.6                 Enzyme
NAME        chymopapain;
            chymopapain A;
            chymopapain B;
            chymopapain S
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Similar to that of papain
COMMENT     The major endopeptidase of papaya (Carica papaya) latex. It has
            multiple chromatographic forms. In peptidase family C1 (papain
            family).
REFERENCE   1
  AUTHORS   Brocklehurst, K., Willenbrock, F. and Salih, E.
  TITLE     Cysteine proteinases.
  JOURNAL   In: Neuberger, A. and Brocklehurst, K. (Eds.), New Comprehensive
            Biochemistry: Hydrolytic Enzymes, Elsevier, Amsterdam, 1987, p.
            39-158.
REFERENCE   2  [PMID:2500950]
  AUTHORS   Jacquet A, Kleinschmidt T, Schnek AG, Looze Y, Braunitzer G.
  TITLE     The thiol proteinases from the latex of Carica papaya L. III. The
            primary structure of chymopapain.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 370 (1989) 425-34.
  ORGANISM  Carica papaya
REFERENCE   3  [PMID:2085414]
  AUTHORS   Buttle DJ, Dando PM, Coe PF, Sharp SL, Shepherd ST, Barrett AJ.
  TITLE     The preparation of fully active chymopapain free of contaminating
            proteinases.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 371 (1990) 1083-8.
  ORGANISM  Carica papaya
STRUCTURES  PDB: 1PCI  1YAL  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.6
            ExPASy - ENZYME nomenclature database: 3.4.22.6
            ExplorEnz - The Enzyme Database: 3.4.22.6
            ERGO genome analysis and discovery system: 3.4.22.6
            BRENDA, the Enzyme Database: 3.4.22.6
            CAS: 9001-09-6
///
ENTRY       EC 3.4.22.7                 Enzyme
NAME        asclepain
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Similar to that of papain
COMMENT     From the latex of milkweed, Asclepias syriaca. It has multiple
            forms, and is in peptidase family C1 (papain family)
REFERENCE   1  [PMID:36921]
  AUTHORS   Brockbank WJ, Lynn KR.
  TITLE     Purification and preliminary characterization of two asclepains from
            the latex of Asclepias syriaca L. (milkweed).
  JOURNAL   Biochim. Biophys. Acta. 578 (1979) 13-22.
  ORGANISM  Asclepias syriaca
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.7
            ExPASy - ENZYME nomenclature database: 3.4.22.7
            ExplorEnz - The Enzyme Database: 3.4.22.7
            ERGO genome analysis and discovery system: 3.4.22.7
            BRENDA, the Enzyme Database: 3.4.22.7
            CAS: 37288-80-5
///
ENTRY       EC 3.4.22.8                 Enzyme
NAME        clostripain;
            clostridiopeptidase B;
            clostridium histolyticum proteinase B;
            alpha-clostridipain;
            clostridiopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Preferential cleavage: Arg!, including Arg!Pro, but not Lys-
COFACTOR    Calcium [CPD:C00076]
INHIBITOR   EDTA [CPD:C00284];
            N2-Acylated Arg-CH2Cl [CPD:C03151];
            N2-Acylated Lys-CH2Cl [CPD:C03152]
COMMENT     From the bacterium Clostridium histolyticum. It requires Ca2+ ions
            and is inhibited by EDTA. Type example of peptidase family C11.
REFERENCE   1  [PMID:927173]
  AUTHORS   Mitchell WM.
  TITLE     Cleavage at arginine residues by clostripain.
  JOURNAL   Methods. Enzymol. 47 (1977) 165-70.
REFERENCE   2  [PMID:762145]
  AUTHORS   Gilles AM, Imhoff JM, Keil B.
  TITLE     alpha-Clostripain. Chemical characterization, activity, and thiol
            content of the highly active form of clostripain.
  JOURNAL   J. Biol. Chem. 254 (1979) 1462-8.
  ORGANISM  Clostridium histolyticum
REFERENCE   3  [PMID:6391922]
  AUTHORS   Gilles AM, Lecroisey A, Keil B.
  TITLE     Primary structure of alpha-clostripain light chain.
  JOURNAL   Eur. J. Biochem. 145 (1984) 469-76.
  ORGANISM  Clostridium histolyticum
ORTHOLOGY   KO: K08587  clostripain
GENES       CPE: CPE0846
            CPF: CPF_0840(cloSI)
            CPR: CPR_0833(cloSI)
            CNO: NT01CX_1195
            CBO: CBO1920(closI)
            CBA: CLB_1857(cloSI)
            CBH: CLC_1864(cloSI)
            CBF: CLI_1984(cloSI)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.8
            ExPASy - ENZYME nomenclature database: 3.4.22.8
            ExplorEnz - The Enzyme Database: 3.4.22.8
            ERGO genome analysis and discovery system: 3.4.22.8
            BRENDA, the Enzyme Database: 3.4.22.8
            CAS: 9028-00-6
///
ENTRY       EC 3.4.22.9       Obsolete  Enzyme
NAME        Transferred to 3.4.21.48
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
COMMENT     Transferred entry: now EC 3.4.21.48 cerevisin (EC 3.4.22.9 created
            1972, deleted 1981)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.9
            ExPASy - ENZYME nomenclature database: 3.4.22.9
            ExplorEnz - The Enzyme Database: 3.4.22.9
            ERGO genome analysis and discovery system: 3.4.22.9
            BRENDA, the Enzyme Database: 3.4.22.9
///
ENTRY       EC 3.4.22.10                Enzyme
NAME        streptopain;
            Streptococcus peptidase A;
            streptococcal cysteine proteinase;
            Streptococcus protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Preferential cleavage with hydrophobic residues at P2, P1 and P1'
COMMENT     From the bacterium, group A Streptococcus. Formed from the proenzyme
            by limited proteolysis. Type example of peptidase family C10.
REFERENCE   1
  AUTHORS   Elliott, S.D. and Liu, T.-Y.
  TITLE     Streptococcal proteinase.
  JOURNAL   Methods Enzymol. 19 (1970) 252-261.
  ORGANISM  Streptococcus sp.
REFERENCE   2
  AUTHORS   Liu, T.-Y. and Elliott, S.D.
  TITLE     Streptococcal proteinase.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., Academic Press, New
            York, 1971, p. 609-647.
REFERENCE   3  [PMID:1270417]
  AUTHORS   Tai JY, Kortt AA, Liu TY, Elliott SD.
  TITLE     Primary structure of streptococcal proteinase. III. Isolation of
            cyanogen bromide peptides: complete covalent structure of the
            polypeptide chain.
  JOURNAL   J. Biol. Chem. 251 (1976) 1955-9.
  ORGANISM  Streptococcus sp.
REFERENCE   4  [PMID:6381494]
  AUTHORS   Lo SS, Fraser BA, Liu TY.
  TITLE     The mixed disulfide in the zymogen of streptococcal proteinase.
            Characterization and implication for its biosynthesis.
  JOURNAL   J. Biol. Chem. 259 (1984) 11041-5.
  ORGANISM  Streptococcus sp.
ORTHOLOGY   KO: K01364  streptopain
GENES       SPY: SPy_2039(speB)
            SPZ: M5005_Spy_1735(speB)
            SPM: spyM18_2099(speB)
            SPG: SpyM3_1742(speB)
            SPS: SPs1739
            SPH: MGAS10270_Spy1803(speB)
            SPI: MGAS10750_Spy1828(speB)
            SPJ: MGAS2096_Spy1767(speB)
            SPK: MGAS9429_Spy1743(speB)
            SPF: SpyM51698(speB)
            SPA: M6_Spy1735
            SPB: M28_Spy1721(speB)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.10
            ExPASy - ENZYME nomenclature database: 3.4.22.10
            ExplorEnz - The Enzyme Database: 3.4.22.10
            ERGO genome analysis and discovery system: 3.4.22.10
            BRENDA, the Enzyme Database: 3.4.22.10
            CAS: 9025-51-8
///
ENTRY       EC 3.4.22.11      Obsolete  Enzyme
NAME        Transferred to 3.4.24.56
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
COMMENT     Transferred entry: now EC 3.4.24.56 insulysin (EC 3.4.22.11 created
            1976, deleted 1978 [transferred to EC 3.4.99.45, deleted 1993])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.11
            ExPASy - ENZYME nomenclature database: 3.4.22.11
            ExplorEnz - The Enzyme Database: 3.4.22.11
            ERGO genome analysis and discovery system: 3.4.22.11
            BRENDA, the Enzyme Database: 3.4.22.11
///
ENTRY       EC 3.4.22.12      Obsolete  Enzyme
NAME        Transferred to 3.4.19.9
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
COMMENT     Transferred entry: now EC 3.4.19.9, gamma-glutamyl hydrolase (EC
            3.4.22.12 created 1978, deleted 1992)
STRUCTURES  PDB: 1FO6  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.12
            ExPASy - ENZYME nomenclature database: 3.4.22.12
            ExplorEnz - The Enzyme Database: 3.4.22.12
            ERGO genome analysis and discovery system: 3.4.22.12
            BRENDA, the Enzyme Database: 3.4.22.12
///
ENTRY       EC 3.4.22.13      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
COMMENT     Deleted entry: staphylococcal cysteine proteinase (EC 3.4.22.13
            created 1978, modified 1981, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.13
            ExPASy - ENZYME nomenclature database: 3.4.22.13
            ExplorEnz - The Enzyme Database: 3.4.22.13
            ERGO genome analysis and discovery system: 3.4.22.13
            BRENDA, the Enzyme Database: 3.4.22.13
///
ENTRY       EC 3.4.22.14                Enzyme
NAME        actinidain;
            actinidin;
            Actinidia anionic protease;
            proteinase A2 of Actinidia chinensis
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Similar to that of papain
COMMENT     From the kiwi fruit or Chinese gooseberry (Actinidia chinensis). In
            peptidase family C1 (papain family)
REFERENCE   1  [PMID:7002215]
  AUTHORS   Baker EN, Boland MJ, Calder PC, Hardman MJ.
  TITLE     The specificity of actinidin and its relationship to the structure
            of the enzyme.
  JOURNAL   Biochim. Biophys. Acta. 616 (1980) 30-4.
REFERENCE   2  [PMID:3889350]
  AUTHORS   Kamphuis IG, Drenth J, Baker EN.
  TITLE     Thiol proteases. Comparative studies based on the high-resolution
            structures of papain and actinidin, and on amino acid sequence
            information for cathepsins B and H, and stem bromelain.
  JOURNAL   J. Mol. Biol. 182 (1985) 317-29.
  ORGANISM  Carica papaya, Actinidia chinensis
REFERENCE   3
  AUTHORS   Baker, E.N. and Drenth, J.
  TITLE     The thiol proteases: stucture and mechanism.
  JOURNAL   In: Jurnak, F.A. and McPherson, A. (Eds.), Biological Macromolecules
            and Assemblies: Active Sites of Enzymes, vol. 3, John Wiley and
            Sons, New York, 1987, p. 314-368.
GENES       TET: TTHERM_00879230 TTHERM_00881410 TTHERM_01359470
                 TTHERM_02592230
STRUCTURES  PDB: 1AEC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.14
            ExPASy - ENZYME nomenclature database: 3.4.22.14
            ExplorEnz - The Enzyme Database: 3.4.22.14
            ERGO genome analysis and discovery system: 3.4.22.14
            BRENDA, the Enzyme Database: 3.4.22.14
            CAS: 39279-27-1
///
ENTRY       EC 3.4.22.15                Enzyme
NAME        cathepsin L;
            Aldrichina grahami cysteine proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Similar to that of papain. As compared to cathepsin B, cathepsin L
            exhibits higher activity towards protein substrates, but has little
            activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity
INHIBITOR   E-64 [CPD:C01341];
            Leupeptin [CPD:C01591];
            Z-Phe-Phe-CHN2 [CPD:C02202]
COMMENT     A lysosomal enzyme in peptidase family C1 (papain family) that is
            readily inhibited by the diazomethane inhibitor Z-Phe-Phe-CHN2 or
            the epoxide inhibitor E-64
REFERENCE   1  [PMID:7043200]
  AUTHORS   Barrett AJ, Kirschke H.
  TITLE     Cathepsin B, Cathepsin H, and cathepsin L.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 535-61.
REFERENCE   2
  AUTHORS   Barrett, A.J., Buttle, D.J. and Mason, R.W.
  TITLE     Lysosomal cysteine proteinases.
  JOURNAL   ISI Atlas of Science. Biochemistry 1 (1988) 256-260.
REFERENCE   3  [PMID:2835398]
  AUTHORS   Joseph LJ, Chang LC, Stamenkovich D, Sukhatme VP.
  TITLE     Complete nucleotide and deduced amino acid sequences of human and
            murine preprocathepsin L. An abundant transcript induced by
            transformation of fibroblasts.
  JOURNAL   J. Clin. Invest. 81 (1988) 1621-9.
  ORGANISM  human [GN:hsa], mouse [GN:mmu]
REFERENCE   4  [PMID:3342870]
  AUTHORS   Kirschke H, Wikstrom P, Shaw E.
  TITLE     Active center differences between cathepsins L and B: the S1 binding
            region.
  JOURNAL   FEBS. Lett. 228 (1988) 128-30.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map04612  Antigen processing and presentation
ORTHOLOGY   KO: K01365  cathepsin L
GENES       HSA: 1514(CTSL1)
            MMU: 13039(Ctsl)
            RNO: 25697(Ctsl)
            BTA: 281108(CTSL)
            SSC: 396926(CTSL2)
            GGA: 427466(CTSL1)
            XLA: 447313(MGC81823)
            XTR: 448179(MGC69486)
            DRE: 30443(ctsl1b) 321453(ctsl1a)
            SPU: 575070(LOC575070) 575142(LOC575142)
            DME: Dmel_CG6692(Cp1)
            CEL: T03E6.7(cpl-1)
            DDI: DDBDRAFT_0203746 DDB_0214998(cprB) DDB_0220784(cprC)
            TET: TTHERM_00013200 TTHERM_00079380 TTHERM_00079450
                 TTHERM_00079550 TTHERM_00161130 TTHERM_00320290
                 TTHERM_00494530 TTHERM_00628610 TTHERM_00629950
                 TTHERM_00802340 TTHERM_00874750 TTHERM_00881370
                 TTHERM_01256490 TTHERM_01256520 TTHERM_01276400
                 TTHERM_01359480
STRUCTURES  PDB: 1CJL  1CS8  1ICF  1MHW  2NQD  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.15
            ExPASy - ENZYME nomenclature database: 3.4.22.15
            ExplorEnz - The Enzyme Database: 3.4.22.15
            ERGO genome analysis and discovery system: 3.4.22.15
            BRENDA, the Enzyme Database: 3.4.22.15
            CAS: 60616-82-2
///
ENTRY       EC 3.4.22.16                Enzyme
NAME        cathepsin H;
            cathepsin B3;
            benzoylarginine-naphthylamide (BANA) hydrolase (obsolete);
            cathepsin Ba, aleurain;
            N-benzoylarginine-beta-naphthylamide hydrolase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Hydrolysis of proteins, acting as an aminopeptidase (notably,
            cleaving Arg! bonds) as well as an endopeptidase
COMMENT     Present in lysosomes of mammalian cells. In peptidase family C1
            (papain family)
REFERENCE   1  [PMID:7043200]
  AUTHORS   Barrett AJ, Kirschke H.
  TITLE     Cathepsin B, Cathepsin H, and cathepsin L.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 535-61.
REFERENCE   2  [PMID:3663163]
  AUTHORS   Bromme D, Bescherer K, Kirschke H, Fittkau S.
  TITLE     Enzyme-substrate interactions in the hydrolysis of peptides by
            cathepsins B and H from rat liver.
  JOURNAL   Biochem. J. 245 (1987) 381-5.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:2849458]
  AUTHORS   Fuchs R, Machleidt W, Gassen HG.
  TITLE     Molecular cloning and sequencing of a cDNA coding for mature human
            kidney cathepsin H.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 369 (1988) 469-75.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01366  cathepsin H
GENES       HSA: 1512(CTSH)
            MMU: 13036(Ctsh)
            RNO: 25425(Ctsh)
            CFA: 479065(CTSH)
            BTA: 510524(CTSH)
            SSC: 396969(CTSH)
            GGA: 770109(CTSH)
            DRE: 324818(ctsh)
            TET: TTHERM_00075840 TTHERM_00079580 TTHERM_00079610
                 TTHERM_00079620 TTHERM_00079630 TTHERM_00079640
                 TTHERM_00079650 TTHERM_00735230 TTHERM_00874740
                 TTHERM_00878210 TTHERM_00879270 TTHERM_00895720
                 TTHERM_00908100 TTHERM_00909100 TTHERM_00910100
                 TTHERM_00911100 TTHERM_01001420 TTHERM_01008660
                 TTHERM_01028740 TTHERM_01028750 TTHERM_01354260
                 TTHERM_01354270
STRUCTURES  PDB: 1NB3  1NB5  8PCH  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.16
            ExPASy - ENZYME nomenclature database: 3.4.22.16
            ExplorEnz - The Enzyme Database: 3.4.22.16
            ERGO genome analysis and discovery system: 3.4.22.16
            BRENDA, the Enzyme Database: 3.4.22.16
            CAS: 60748-73-4
///
ENTRY       EC 3.4.22.17      Obsolete  Enzyme
NAME        Transferred to 3.4.22.53
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
COMMENT     Transferred entry: now EC 3.4.22.53 calpain-2 (EC 3.4.22.17 created
            1981 [EC 3.4.24.5 created 1978, part incorporated 1989], deleted
            2003)
GENES       DME: Dmel_CG1391(sol) Dmel_CG3692(CalpC) Dmel_CG7563(CalpA)
STRUCTURES  PDB: 1AJ5  1ALV  1ALW  1DF0  1DVI  1KFU  1KFX  1KXR  1MDW  1NX0  
                 1NX1  1NX2  1NX3  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.17
            ExPASy - ENZYME nomenclature database: 3.4.22.17
            ExplorEnz - The Enzyme Database: 3.4.22.17
            ERGO genome analysis and discovery system: 3.4.22.17
            BRENDA, the Enzyme Database: 3.4.22.17
///
ENTRY       EC 3.4.22.18      Obsolete  Enzyme
NAME        Transferred to 3.4.21.26
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
COMMENT     Transferred entry: now EC 3.4.21.26 prolyl oligopeptidase (EC
            3.4.22.18 created 1981, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.18
            ExPASy - ENZYME nomenclature database: 3.4.22.18
            ExplorEnz - The Enzyme Database: 3.4.22.18
            ERGO genome analysis and discovery system: 3.4.22.18
            BRENDA, the Enzyme Database: 3.4.22.18
///
ENTRY       EC 3.4.22.19      Obsolete  Enzyme
NAME        Transferred to 3.4.24.15
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
COMMENT     Transferred entry: now EC 3.4.24.15 thimet oligopeptidase (EC
            3.4.22.19 created 1989, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.19
            ExPASy - ENZYME nomenclature database: 3.4.22.19
            ExplorEnz - The Enzyme Database: 3.4.22.19
            ERGO genome analysis and discovery system: 3.4.22.19
            BRENDA, the Enzyme Database: 3.4.22.19
///
ENTRY       EC 3.4.22.20      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
COMMENT     Deleted entry: dinorphin-converting enzyme (EC 3.4.22.20 created
            1989, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.20
            ExPASy - ENZYME nomenclature database: 3.4.22.20
            ExplorEnz - The Enzyme Database: 3.4.22.20
            ERGO genome analysis and discovery system: 3.4.22.20
            BRENDA, the Enzyme Database: 3.4.22.20
///
ENTRY       EC 3.4.22.21      Obsolete  Enzyme
NAME        Transferred to 3.4.25.1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
COMMENT     Transferred entry: now EC 3.4.25.1, proteasome endopeptidase complex
            (EC 3.4.22.21 created 1989, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.21
            ExPASy - ENZYME nomenclature database: 3.4.22.21
            ExplorEnz - The Enzyme Database: 3.4.22.21
            ERGO genome analysis and discovery system: 3.4.22.21
            BRENDA, the Enzyme Database: 3.4.22.21
///
ENTRY       EC 3.4.22.22      Obsolete  Enzyme
NAME        Transferred to 3.4.24.37
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
COMMENT     Transferred entry: now EC 3.4.24.37 saccharolysin (EC 3.4.22.22
            created 1989, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.22
            ExPASy - ENZYME nomenclature database: 3.4.22.22
            ExplorEnz - The Enzyme Database: 3.4.22.22
            ERGO genome analysis and discovery system: 3.4.22.22
            BRENDA, the Enzyme Database: 3.4.22.22
///
ENTRY       EC 3.4.22.23      Obsolete  Enzyme
NAME        Transferred to 3.4.21.61
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
COMMENT     Transferred entry: now EC 3.4.21.61 kexin (EC 3.4.22.23 created
            1989, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.23
            ExPASy - ENZYME nomenclature database: 3.4.22.23
            ExplorEnz - The Enzyme Database: 3.4.22.23
            ERGO genome analysis and discovery system: 3.4.22.23
            BRENDA, the Enzyme Database: 3.4.22.23
///
ENTRY       EC 3.4.22.24                Enzyme
NAME        cathepsin T
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Interconversion of the three forms of tyrosine aminotransferase, EC
            2.6.1.5
COMMENT     Degrades azocasein and denatured hemoglobin; the only native protein
            on which it has been shown to act is tyrosine aminotransferase
REFERENCE   1  [PMID:7248311]
  AUTHORS   Gohda E, Pitot HC.
  TITLE     Purification and characterization of a new thiol proteinase from rat
            kidney.
  JOURNAL   Biochim. Biophys. Acta. 659 (1981) 114-22.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:6780567]
  AUTHORS   Gohda E, Pitot HC.
  TITLE     A new thiol proteinase from rat liver.
  JOURNAL   J. Biol. Chem. 256 (1981) 2567-72.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:2885716]
  AUTHORS   Pitot HC, Gohda E.
  TITLE     Cathepsin T.
  JOURNAL   Methods. Enzymol. 142 (1987) 279-89.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.24
            ExPASy - ENZYME nomenclature database: 3.4.22.24
            ExplorEnz - The Enzyme Database: 3.4.22.24
            ERGO genome analysis and discovery system: 3.4.22.24
            BRENDA, the Enzyme Database: 3.4.22.24
            CAS: 77464-86-9
///
ENTRY       EC 3.4.22.25                Enzyme
NAME        glycyl endopeptidase;
            papaya peptidase B;
            papaya proteinase IV;
            glycine-specific proteinase;
            chymopapain;
            Papaya proteinase 4;
            PPIV;
            chymopapain M
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Preferential cleavage: Gly!, in proteins and small molecule
            substrates
COMMENT     From the papaya plant, Carica papaya. Not inhibited by chicken
            cystatin, unlike most other homologues of papain, but in peptidase
            family C1 (papain family)
REFERENCE   1  [PMID:7018581]
  AUTHORS   Polgar L.
  TITLE     Isolation of highly active papaya peptidases A and B from commercial
            chymopapain.
  JOURNAL   Biochim. Biophys. Acta. 658 (1981) 262-9.
REFERENCE   2  [PMID:2505761]
  AUTHORS   Buttle DJ, Kembhavi AA, Sharp SL, Shute RE, Rich DH, Barrett AJ.
  TITLE     Affinity purification of the novel cysteine proteinase papaya
            proteinase IV, and papain from papaya latex.
  JOURNAL   Biochem. J. 261 (1989) 469-76.
  ORGANISM  Carica papaya
REFERENCE   3  [PMID:2591528]
  AUTHORS   Ritonja A, Buttle DJ, Rawlings ND, Turk V, Barrett AJ.
  TITLE     Papaya proteinase IV amino acid sequence.
  JOURNAL   FEBS. Lett. 258 (1989) 109-12.
  ORGANISM  Carica papaya
REFERENCE   4  [PMID:1690669]
  AUTHORS   Buttle DJ, Ritonja A, Dando PM, Abrahamson M, Shaw EN, Wikstrom P,
            Turk V, Barrett AJ.
  TITLE     Interactions of papaya proteinase IV with inhibitors.
  JOURNAL   FEBS. Lett. 262 (1990) 58-60.
  ORGANISM  Carica papaya
REFERENCE   5  [PMID:1690669]
  AUTHORS   Buttle DJ, Ritonja A, Dando PM, Abrahamson M, Shaw EN, Wikstrom P,
            Turk V, Barrett AJ.
  TITLE     Interactions of papaya proteinase IV with inhibitors.
  JOURNAL   FEBS. Lett. 262 (1990) 58-60.
  ORGANISM  Carica papaya
STRUCTURES  PDB: 1GEC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.25
            ExPASy - ENZYME nomenclature database: 3.4.22.25
            ExplorEnz - The Enzyme Database: 3.4.22.25
            ERGO genome analysis and discovery system: 3.4.22.25
            BRENDA, the Enzyme Database: 3.4.22.25
            CAS: 92228-52-9
///
ENTRY       EC 3.4.22.26                Enzyme
NAME        cancer procoagulant
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Specific cleavage of Arg!Ile bond in Factor X to form Factor Xa
COMMENT     Apparently produced only by malignant and fetal cells
REFERENCE   1  [PMID:3935163]
  AUTHORS   Falanga A, Gordon SG.
  TITLE     Isolation and characterization of cancer procoagulant: a cysteine
            proteinase from malignant tissue.
  JOURNAL   Biochemistry. 24 (1985) 5558-67.
  ORGANISM  rabbit
REFERENCE   2  [PMID:2772865]
  AUTHORS   Falanga A, Shaw E, Donati MB, Consonni R, Barbui T, Gordon S.
  TITLE     Inhibition of cancer procoagulant by peptidyl diazomethyl ketones
            and peptidyl sulfonium salts.
  JOURNAL   Thromb. Res. 54 (1989) 389-98.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.26
            ExPASy - ENZYME nomenclature database: 3.4.22.26
            ExplorEnz - The Enzyme Database: 3.4.22.26
            ERGO genome analysis and discovery system: 3.4.22.26
            BRENDA, the Enzyme Database: 3.4.22.26
            CAS: 109456-80-6
///
ENTRY       EC 3.4.22.27                Enzyme
NAME        cathepsin S
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Similar to cathepsin L, but with much less activity on
            Z-Phe-Arg!NHMec, and more activity on the Z-Val-Val-Arg! compound
COMMENT     A lysosomal cysteine endopeptidase that is unusual amongst such
            enzymes for its stability to neutral pH. In peptidase family C1
            (papain family)
REFERENCE   1  [PMID:1182153]
  AUTHORS   Turnsek T, Kregar I, Lebez D.
  TITLE     Acid sulphydryl protease from calf lymph nodes.
  JOURNAL   Biochim. Biophys. Acta. 403 (1975) 514-20.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:2604727]
  AUTHORS   Bromme D, Steinert A, Friebe S, Fittkau S, Wiederanders B, Kirschke
            H.
  TITLE     The specificity of bovine spleen cathepsin S. A comparison with rat
            liver cathepsins L and B.
  JOURNAL   Biochem. J. 264 (1989) 475-81.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:2690828]
  AUTHORS   Kirschke H, Wiederanders B, Bromme D, Rinne A.
  TITLE     Cathepsin S from bovine spleen. Purification, distribution,
            intracellular localization and action on proteins.
  JOURNAL   Biochem. J. 264 (1989) 467-73.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map04612  Antigen processing and presentation
ORTHOLOGY   KO: K01368  cathepsin S
GENES       HSA: 1520(CTSS)
            PTR: 457277(CTSS)
            MMU: 13040(Ctss)
            RNO: 50654(Ctss)
            CFA: 403400(CTSS)
            BTA: 327711(CTSS)
            GGA: 425657(RCJMB04_1f23)
            XLA: 380516(ctss-a) 446505(ctss-b)
            XTR: 448203(ctss)
            DRE: 554157(zgc:112226)
STRUCTURES  PDB: 1GLO  1MS6  1NPZ  1NQC  2C0Y  2F1G  2FQ9  2FRA  2FRQ  2FUD  
                 2FYE  2G6D  2G7Y  2H7J  2HH5  2HHN  2HXZ  2OP3  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.27
            ExPASy - ENZYME nomenclature database: 3.4.22.27
            ExplorEnz - The Enzyme Database: 3.4.22.27
            ERGO genome analysis and discovery system: 3.4.22.27
            BRENDA, the Enzyme Database: 3.4.22.27
            CAS: 71965-46-3
///
ENTRY       EC 3.4.22.28                Enzyme
NAME        picornain 3C;
            picornavirus endopeptidase 3C;
            poliovirus protease 3C;
            rhinovirus protease 3C;
            foot-and-mouth protease 3C;
            poliovirus proteinase 3C;
            rhinovirus proteinase 3C;
            coxsackievirus 3C proteinase;
            foot-and-mouth-disease virus proteinase 3C;
            3C protease;
            3C proteinase;
            cysteine proteinase 3C;
            hepatitis A virus 3C proteinase;
            protease 3C;
            tomato ringspot nepovirus 3C-related protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Selective cleavage of Gln!Gly bond in the poliovirus polyprotein. In
            other picornavirus reactions Glu may be substituted for Gln, and Ser
            or Thr for Gly
COMMENT     From entero-, rhino-, aphto- and cardioviruses. Larger than the
            homologous virus picornain 2A. Type example of peptidase family C3
REFERENCE   1  [PMID:3016701]
  AUTHORS   Ivanoff LA, Towatari T, Ray J, Korant BD, Petteway SR Jr.
  TITLE     Expression and site-specific mutagenesis of the poliovirus 3C
            protease in Escherichia coli.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 5392-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:3186696]
  AUTHORS   Bazan JF, Fletterick RJ.
  TITLE     Viral cysteine proteases are homologous to the trypsin-like family
            of serine proteases: structural and functional implications.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 7872-6.
  ORGANISM  Staphylococcus aureus, Streptomyces griseus
REFERENCE   3  [PMID:3052288]
  AUTHORS   Krausslich HG, Wimmer E.
  TITLE     Viral proteinases.
  JOURNAL   Annu. Rev. Biochem. 57 (1988) 701-54.
REFERENCE   4  [PMID:2846872]
  AUTHORS   Nicklin MJ, Harris KS, Pallai PV, Wimmer E.
  TITLE     Poliovirus proteinase 3C: large-scale expression, purification, and
            specific cleavage activity on natural and synthetic substrates in
            vitro.
  JOURNAL   J. Virol. 62 (1988) 4586-93.
  ORGANISM  Escherichia coli [GN:eco]
STRUCTURES  PDB: 1L1N  2A4O  2B0F  2BHG  2CXV  2H6M  2H9H  2HAL  2IJD  2IN2  
                 2J92  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.28
            ExPASy - ENZYME nomenclature database: 3.4.22.28
            ExplorEnz - The Enzyme Database: 3.4.22.28
            ERGO genome analysis and discovery system: 3.4.22.28
            BRENDA, the Enzyme Database: 3.4.22.28
            CAS: 97162-88-4
///
ENTRY       EC 3.4.22.29                Enzyme
NAME        picornain 2A;
            picornavirus endopeptidase 2A;
            poliovirus protease 2A;
            rhinovirus protease 2A;
            2A protease;
            2A proteinase;
            protease 2A;
            proteinase 2Apro;
            picornaviral 2A proteinase;
            Y-G proteinase 2A;
            poliovirus proteinase 2A;
            poliovirus protease 2Apro;
            picornaviral 2A proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Selective cleavage of Tyr!Gly bond in picornavirus polyprotein
COMMENT     From entero-, rhino-, aphto- and cardioviruses. Smaller than the
            homologous picornain 3C, which is also in peptidase family C3
            (picornain 3C family)
REFERENCE   1  [PMID:3186696]
  AUTHORS   Bazan JF, Fletterick RJ.
  TITLE     Viral cysteine proteases are homologous to the trypsin-like family
            of serine proteases: structural and functional implications.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 7872-6.
  ORGANISM  Staphylococcus aureus, Streptomyces griseus
REFERENCE   2  [PMID:2831385]
  AUTHORS   Konig H, Rosenwirth B.
  TITLE     Purification and partial characterization of poliovirus protease 2A
            by means of a functional assay.
  JOURNAL   J. Virol. 62 (1988) 1243-50.
REFERENCE   3  [PMID:3052288]
  AUTHORS   Krausslich HG, Wimmer E.
  TITLE     Viral proteinases.
  JOURNAL   Annu. Rev. Biochem. 57 (1988) 701-54.
STRUCTURES  PDB: 1Z8R  2HRV  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.29
            ExPASy - ENZYME nomenclature database: 3.4.22.29
            ExplorEnz - The Enzyme Database: 3.4.22.29
            ERGO genome analysis and discovery system: 3.4.22.29
            BRENDA, the Enzyme Database: 3.4.22.29
            CAS: 103406-62-8
///
ENTRY       EC 3.4.22.30                Enzyme
NAME        caricain;
            papaya peptidase A;
            papaya peptidase II;
            papaya proteinase ;
            papaya proteinase III;
            papaya proteinase 3;
            proteinase omega;
            papaya proteinase A;
            chymopapain S;
            Pp
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Hydrolysis of proteins with broad specificity for peptide bonds,
            similar to those of papain and chymopapain
COMMENT     From papaya plant, Carica papaya. In peptidase family C1 (papain
            family)
REFERENCE   1  [PMID:6043136]
  AUTHORS   Schack P.
  TITLE     Fractionation of proteolytic enzymes of dried papaya latex.
            Isolation and preliminary characterization of a new proteolytic
            enzyme.
  JOURNAL   C. R. Trav. Lab. Carlsberg. 36 (1967) 67-83.
  ORGANISM  Carica papaya
REFERENCE   2  [PMID:240390]
  AUTHORS   Robinson GW.
  TITLE     Isolation and characterization of papaya peptidase A from commercial
            chymopapain.
  JOURNAL   Biochemistry. 14 (1975) 3695-700.
  ORGANISM  Carica papaya
REFERENCE   3  [PMID:6383350]
  AUTHORS   Polgar L.
  TITLE     Problems of classification of papaya latex proteinases.
  JOURNAL   Biochem. J. 221 (1984) 555-6.
  ORGANISM  Carica papaya
REFERENCE   4  [PMID:4015629]
  AUTHORS   Brocklehurst K, Salih E, McKee R, Smith H.
  TITLE     Fresh non-fruit latex of Carica papaya contains papain, multiple
            forms of chymopapain A and papaya proteinase omega.
  JOURNAL   Biochem. J. 228 (1985) 525-7.
  ORGANISM  Carica papaya
REFERENCE   5  [PMID:3919769]
  AUTHORS   Zucker S, Buttle DJ, Nicklin MJ, Barrett AJ.
  TITLE     The proteolytic activities of chymopapain, papain, and papaya
            proteinase III.
  JOURNAL   Biochim. Biophys. Acta. 828 (1985) 196-204.
  ORGANISM  Carica papaya
REFERENCE   6  [PMID:3063283]
  AUTHORS   Dubois T, Kleinschmidt T, Schnek AG, Looze Y, Braunitzer G.
  TITLE     The thiol proteinases from the latex of Carica papaya L. II. The
            primary structure of proteinase omega.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 369 (1988) 741-54.
  ORGANISM  Carica papaya
STRUCTURES  PDB: 1MEG  1PPO  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.30
            ExPASy - ENZYME nomenclature database: 3.4.22.30
            ExplorEnz - The Enzyme Database: 3.4.22.30
            ERGO genome analysis and discovery system: 3.4.22.30
            BRENDA, the Enzyme Database: 3.4.22.30
            CAS: 39307-22-7
///
ENTRY       EC 3.4.22.31                Enzyme
NAME        ananain;
            stem bromelain;
            fruit bromelain
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Hydrolysis of proteins with broad specificity for peptide bonds.
            Best reported small molecule substrate Bz-Phe-Val-Arg!NHMec, but
            broader specificity than fruit bromelain
COMMENT     From stem of pineapple plant, Ananas comosus. Differs from stem and
            fruit bromelains in being inhibited by chicken cystatin. In
            peptidase family C1 (papain family)
REFERENCE   1  [PMID:3196029]
  AUTHORS   Rowan AD, Buttle DJ, Barrett AJ.
  TITLE     Ananain: a novel cysteine proteinase found in pineapple stem.
  JOURNAL   Arch. Biochem. Biophys. 267 (1988) 262-70.
  ORGANISM  Ananas comosus
REFERENCE   2  [PMID:2327970]
  AUTHORS   Rowan AD, Buttle DJ, Barrett AJ.
  TITLE     The cysteine proteinases of the pineapple plant.
  JOURNAL   Biochem. J. 266 (1990) 869-75.
  ORGANISM  Ananas comosus
GENES       TET: TTHERM_00079600 TTHERM_00881320 TTHERM_00881330
                 TTHERM_00881420 TTHERM_00945300
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.31
            ExPASy - ENZYME nomenclature database: 3.4.22.31
            ExplorEnz - The Enzyme Database: 3.4.22.31
            ERGO genome analysis and discovery system: 3.4.22.31
            BRENDA, the Enzyme Database: 3.4.22.31
            CAS: 119129-70-3
///
ENTRY       EC 3.4.22.32                Enzyme
NAME        stem bromelain;
            bromelain;
            pineapple stem bromelain
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Broad specificity for cleavage of proteins, but strong preference
            for Z-Arg-Arg!NHMec amongst small molecule substrates
COMMENT     The most abundant of the cysteine endopeptidases of the stem of the
            pineapple plant, Ananas comosus. Distinct from the bromelain found
            in the pineapple fruit (EC 3.4.22.33). Scarcely inhibited by chicken
            cystatin and also very slowly inactivated by E-64. In peptidase
            family C1 (papain family).
REFERENCE   1
  AUTHORS   Brocklehurst, K., Willenbrock, F. and Salih, E.
  TITLE     Cysteine proteinases.
  JOURNAL   In: Neuberger, A. and Brocklehurst, K. (Eds.), New Comprehensive
            Biochemistry: Hydrolytic Enzymes, Elsevier, Amsterdam, 1987, p.
            39-158.
REFERENCE   2  [PMID:3196029]
  AUTHORS   Rowan AD, Buttle DJ, Barrett AJ.
  TITLE     Ananain: a novel cysteine proteinase found in pineapple stem.
  JOURNAL   Arch. Biochem. Biophys. 267 (1988) 262-70.
  ORGANISM  Ananas comosus
REFERENCE   3  [PMID:2714443]
  AUTHORS   Ritonja A, Rowan AD, Buttle DJ, Rawlings ND, Turk V, Barrett AJ.
  TITLE     Stem bromelain: amino acid sequence and implications for weak
            binding of cystatin.
  JOURNAL   FEBS. Lett. 247 (1989) 419-24.
  ORGANISM  Ananas comosus
REFERENCE   4  [PMID:2327970]
  AUTHORS   Rowan AD, Buttle DJ, Barrett AJ.
  TITLE     The cysteine proteinases of the pineapple plant.
  JOURNAL   Biochem. J. 266 (1990) 869-75.
  ORGANISM  Ananas comosus
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.32
            ExPASy - ENZYME nomenclature database: 3.4.22.32
            ExplorEnz - The Enzyme Database: 3.4.22.32
            ERGO genome analysis and discovery system: 3.4.22.32
            BRENDA, the Enzyme Database: 3.4.22.32
            CAS: 37189-34-7
///
ENTRY       EC 3.4.22.33                Enzyme
NAME        fruit bromelain;
            juice bromelain;
            ananase;
            bromelase;
            bromelin;
            extranase;
            juice bromelain;
            pinase;
            pineapple enzyme;
            traumanase;
            fruit bromelain FA2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Hydrolysis of proteins with broad specificity for peptide bonds.
            Bz-Phe-Val-Arg!NHMec is a good synthetic substrate, but there is no
            action on Z-Arg-Arg-NHMec (c.f. stem bromelain)
COMMENT     From the pineapple plant, Ananas comosus. Scarcely inhibited by
            chicken cystatin. Another cysteine endopeptidase, with similar
            action on small molecule substrates, pinguinain, is obtained from
            the related plant, Bromelia pinguin, but pinguinain differs from
            fruit bromelain in being inhibited by chicken cystatin [4].
REFERENCE   1  [PMID:4127920]
  AUTHORS   Sasaki M, Kato T, Iida S.
  TITLE     Antigenic determinant common to four kinds of thiol proteases of
            plant origin.
  JOURNAL   J. Biochem. (Tokyo). 74 (1973) 635-7.
REFERENCE   2  [PMID:956152]
  AUTHORS   Yamada F, Takahashi N, Murachi T.
  TITLE     Purification and characterization of a proteinase from pineapple
            fruit, fruit bromelain FA2.
  JOURNAL   J. Biochem. (Tokyo). 79 (1976) 1223-34.
  ORGANISM  Ananas comosus
REFERENCE   3  [PMID:4044551]
  AUTHORS   Ota S, Muta E, Katahira Y, Okamoto Y.
  TITLE     Reinvestigation of fractionation and some properties of the
            proteolytically active components of stem and fruit bromelains.
  JOURNAL   J. Biochem. (Tokyo). 98 (1985) 219-28.
REFERENCE   4  [PMID:2327970]
  AUTHORS   Rowan AD, Buttle DJ, Barrett AJ.
  TITLE     The cysteine proteinases of the pineapple plant.
  JOURNAL   Biochem. J. 266 (1990) 869-75.
  ORGANISM  Ananas comosus
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.33
            ExPASy - ENZYME nomenclature database: 3.4.22.33
            ExplorEnz - The Enzyme Database: 3.4.22.33
            ERGO genome analysis and discovery system: 3.4.22.33
            BRENDA, the Enzyme Database: 3.4.22.33
            CAS: 9001-00-7
///
ENTRY       EC 3.4.22.34                Enzyme
NAME        legumain;
            asparaginyl endopeptidase;
            citvac;
            proteinase B (ambiguous);
            hemoglobinase (ambiguous);
            PRSC1 gene product (Homo sapiens);
            vicilin peptidohydrolase;
            bean endopeptidase;
            vicilin peptidohydrolase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Hydrolysis of proteins and small molecule substrates at -Asn!Xaa-
            bonds
COMMENT     Best known from legume seeds, the trematode Schistosoma mansoni and
            mammalian lysosomes. Not inhibited by compound E-64. Type example of
            peptidase family C13
REFERENCE   1
  AUTHORS   Hara-Nishimura, I.
  TITLE     Asparaginyl endopeptidase.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Academic Press, London, 1998, p.
            746-749.
REFERENCE   2
  AUTHORS   Dalton, J.P. and Brindley, P.J.
  TITLE     Schistosome legumain.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Academic Press, London, 1998, p.
            749-754.
REFERENCE   3  [PMID:9891971]
  AUTHORS   Chen JM, Rawlings ND, Stevens RA, Barrett AJ.
  TITLE     Identification of the active site of legumain links it to caspases,
            clostripain and gingipains in a new clan of cysteine endopeptidases.
  JOURNAL   FEBS. Lett. 441 (1998) 361-5.
  ORGANISM  human [GN:hsa], mouse [GN:mmu]
PATHWAY     PATH: map04612  Antigen processing and presentation
ORTHOLOGY   KO: K01369  legumain
GENES       HSA: 5641(LGMN)
            PTR: 453118(LGMN)
            RNO: 63865(Lgmn)
            CFA: 480232(LGMN)
            BTA: 281281(LGMN)
            GGA: 423418(LGMN)
            XLA: 379601(MGC64351)
            XTR: 448252(lgmn)
            DRE: 406625(lgmn)
            CEL: T28H10.3
            ATH: AT3G20210(DELTA-VPE)
            PFA: PF11_0298
            TET: TTHERM_00066890 TTHERM_00066900 TTHERM_00415590
                 TTHERM_00415600
            MHU: Mhun_0488
            MBN: Mboo_1489
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.34
            ExPASy - ENZYME nomenclature database: 3.4.22.34
            ExplorEnz - The Enzyme Database: 3.4.22.34
            ERGO genome analysis and discovery system: 3.4.22.34
            BRENDA, the Enzyme Database: 3.4.22.34
            CAS: 149371-18-6
///
ENTRY       EC 3.4.22.35                Enzyme
NAME        histolysain;
            histolysin;
            histolysin;
            Entamoeba histolytica cysteine proteinase;
            amebapain;
            Entamoeba histolytica cysteine protease;
            Entamoeba histolytica neutral thiol proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Hydrolysis of proteins, including basement membrane collagen and
            azocasein. Preferential cleavage: Arg-Arg! in small molecule
            substrates including Z-Arg-Arg!NHMec
COMMENT     From the protozoan, Entamoeba histolytica. In peptidase family C1
            (papain family)
REFERENCE   1  [PMID:2860002]
  AUTHORS   Lushbaugh WB, Hofbauer AF, Pittman FE.
  TITLE     Entamoeba histolytica: purification of cathepsin B.
  JOURNAL   Exp. Parasitol. 59 (1985) 328-36.
  ORGANISM  Entamoeba histolytica [GN:ehi]
REFERENCE   2  [PMID:2898937]
  AUTHORS   Luaces AL, Barrett AJ.
  TITLE     Affinity purification and biochemical characterization of
            histolysin, the major cysteine proteinase of Entamoeba histolytica.
  JOURNAL   Biochem. J. 250 (1988) 903-9.
  ORGANISM  Entamoeba histolytica [GN:ehi]
ORTHOLOGY   KO: K08570  histolysain
GENES       EHI: 12.t00005 242.t00001 79.t00025
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.35
            ExPASy - ENZYME nomenclature database: 3.4.22.35
            ExplorEnz - The Enzyme Database: 3.4.22.35
            ERGO genome analysis and discovery system: 3.4.22.35
            BRENDA, the Enzyme Database: 3.4.22.35
            CAS: 92228-52-9
///
ENTRY       EC 3.4.22.36                Enzyme
NAME        caspase-1;
            interleukin 1beta-converting enzyme;
            protease VII;
            protease A;
            interleukin 1beta precursor proteinase;
            interleukin 1 converting enzyme;
            interleukin 1beta-converting endopeptidase;
            interleukin-1beta convertase;
            interleukin-1beta converting enzyme;
            interleukin-1beta precursor proteinase;
            prointerleukin 1beta protease;
            precursor interleukin-1beta converting enzyme;
            pro-interleukin 1beta proteinase;
            ICE
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Strict requirement for an Asp residue at position P1 and has a
            preferred cleavage sequence of Tyr-Val-Ala-Asp!
COMMENT     From mammalian monocytes. This enzyme is part of the family of
            inflammatory caspases, which also includes caspase-4 (EC 3.4.22.57)
            and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC
            3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains
            a caspase-recruitment domain (CARD) in its N-terminal prodomain,
            which plays a role in procaspase activation [6,7]. Cleaves
            pro-interleukin-1beta (pro-IL-1beta) to form mature IL-1beta, a
            potent mediator of inflammation. Also activates the proinflammatory
            cytokine, IL-18, which is also known as interferon-gamma-inducing
            factor [6]. Inhibited by Ac-Tyr-Val-Ala-Asp-CHO. Caspase-11 plays a
            critical role in the activation of caspase-1 in mice, whereas
            caspase-4 enhances its activation in humans [7]. Belongs in
            peptidase family C14.
REFERENCE   1  [PMID:1919001]
  AUTHORS   Howard AD, Kostura MJ, Thornberry N, Ding GJ, Limjuco G, Weidner J,
            Salley JP, Hogquist KA, Chaplin DD, Mumford RA, et al.
  TITLE     IL-1-converting enzyme requires aspartic acid residues for
            processing of the IL-1 beta precursor at two distinct sites and does
            not cleave 31-kDa IL-1 alpha.
  JOURNAL   J. Immunol. 147 (1991) 2964-9.
  ORGANISM  human [GN:hsa], mouse [GN:mmu]
REFERENCE   2  [PMID:1574116]
  AUTHORS   Thornberry NA, Bull HG, Calaycay JR, Chapman KT, Howard AD, Kostura
            MJ, Miller DK, Molineaux SM, Weidner JR, Aunins J, et al.
  TITLE     A novel heterodimeric cysteine protease is required for
            interleukin-1 beta processing in monocytes.
  JOURNAL   Nature. 356 (1992) 768-74.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:7845238]
  AUTHORS   Thornberry NA.
  TITLE     Interleukin-1 beta converting enzyme.
  JOURNAL   Methods. Enzymol. 244 (1994) 615-31.
REFERENCE   4  [PMID:8861900]
  AUTHORS   Alnemri ES, Livingston DJ, Nicholson DW, Salvesen G, Thornberry NA,
            Wong WW, Yuan J.
  TITLE     Human ICE/CED-3 protease nomenclature.
  JOURNAL   Cell. 87 (1996) 171.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:9054418]
  AUTHORS   Margolin N, Raybuck SA, Wilson KP, Chen W, Fox T, Gu Y, Livingston
            DJ.
  TITLE     Substrate and inhibitor specificity of interleukin-1 beta-converting
            enzyme and related caspases.
  JOURNAL   J. Biol. Chem. 272 (1997) 7223-8.
  ORGANISM  Caenorhabditis elegans [GN:cel]
REFERENCE   6  [PMID:15163405]
  AUTHORS   Martinon F, Tschopp J.
  TITLE     Inflammatory caspases: linking an intracellular innate immune system
            to autoinflammatory diseases.
  JOURNAL   Cell. 117 (2004) 561-74.
REFERENCE   7  [PMID:11104820]
  AUTHORS   Chang HY, Yang X.
  TITLE     Proteases for cell suicide: functions and regulation of caspases.
  JOURNAL   Microbiol. Mol. Biol. Rev. 64 (2000) 821-46.
PATHWAY     PATH: map01510  Neurodegenerative Disorders
            PATH: map05040  Huntington's disease
            PATH: map05050  Dentatorubropallidoluysian atrophy (DRPLA)
ORTHOLOGY   KO: K01370  caspase 1, apoptosis-related cysteine protease
                        (interleukin 1, beta, convertase)
GENES       HSA: 834(CASP1)
            PTR: 451519(CASP1)
            MMU: 12362(Casp1)
            RNO: 25166(Casp1)
            SSC: 397319(CASP1)
            GGA: 395764(CASP1)
            AFM: AFUA_1G06700 AFUA_3G14140
STRUCTURES  PDB: 1BMQ  1IBC  1ICE  1M72  1RWK  1RWM  1RWN  1RWO  1RWP  1RWV  
                 1RWW  1RWX  1SC1  1SC3  1SC4  2FQQ  2H48  2HBQ  2HBR  2HBY  
                 2HBZ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.36
            ExPASy - ENZYME nomenclature database: 3.4.22.36
            ExplorEnz - The Enzyme Database: 3.4.22.36
            ERGO genome analysis and discovery system: 3.4.22.36
            BRENDA, the Enzyme Database: 3.4.22.36
            CAS: 122191-40-6
///
ENTRY       EC 3.4.22.37                Enzyme
NAME        gingipain R;
            Arg-gingipain;
            gingipain-1;
            argingipain;
            Arg-gingivain-55 proteinase;
            Arg-gingivain-70 proteinase;
            Arg-gingivain-75 proteinase;
            arginine-specific cysteine protease;
            arginine-specific gingipain;
            arginine-specific gingivain;
            RGP-1;
            RGP
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Hydrolysis of proteins and small molecule substrates, with a
            preference for Arg in P1
COMMENT     A secreted endopeptidase from the bacterium Porphyromonas
            gingivalis. Strongly activated by glycine [1], and stabilized by
            Ca2+. Precursor molecule contains a hemagglutinin domain [2,3].
            Misleadingly described in some literature as "trypsin-like", being a
            cysteine peptidase, type example of family C25
REFERENCE   1  [PMID:1527017]
  AUTHORS   Chen Z, Potempa J, Polanowski A, Wikstrom M, Travis J.
  TITLE     Purification and characterization of a 50-kDa cysteine proteinase
            (gingipain) from Porphyromonas gingivalis.
  JOURNAL   J. Biol. Chem. 267 (1992) 18896-901.
  ORGANISM  Porphyromonas gingivalis [GN:pgi]
REFERENCE   2  [PMID:7857299]
  AUTHORS   Kirszbaum L, Sotiropoulos C, Jackson C, Cleal S, Slakeski N,
            Reynolds EC.
  TITLE     Complete nucleotide sequence of a gene prtR of Porphyromonas
            gingivalis W50 encoding a 132 kDa protein that contains an
            arginine-specific thiol endopeptidase domain and a haemagglutinin
            domain.
  JOURNAL   Biochem. Biophys. Res. Commun. 207 (1995) 424-31.
  ORGANISM  Porphyromonas gingivalis [GN:pgi]
REFERENCE   3  [PMID:7836351]
  AUTHORS   Pavloff N, Potempa J, Pike RN, Prochazka V, Kiefer MC, Travis J,
            Barr PJ.
  TITLE     Molecular cloning and structural characterization of the
            Arg-gingipain proteinase of Porphyromonas gingivalis. Biosynthesis
            as a proteinase-adhesin polyprotein.
  JOURNAL   J. Biol. Chem. 270 (1995) 1007-10.
  ORGANISM  Porphyromonas gingivalis [GN:pgi]
ORTHOLOGY   KO: K08589  gingipain R
GENES       PGI: PG0506(prtRII)
STRUCTURES  PDB: 1CVR  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.37
            ExPASy - ENZYME nomenclature database: 3.4.22.37
            ExplorEnz - The Enzyme Database: 3.4.22.37
            ERGO genome analysis and discovery system: 3.4.22.37
            BRENDA, the Enzyme Database: 3.4.22.37
            CAS: 159745-71-8
///
ENTRY       EC 3.4.22.38                Enzyme
NAME        cathepsin K;
            cathepsin O and cathepsin X (both misleading, having been used for
            other enzymes);
            cathepsin O2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Broad proteolytic activity. With small-molecule substrates and
            inhibitors, the major determinant of specificity is P2, which is
            preferably Leu, Met > Phe, and not Arg
COMMENT     Prominently expressed in mammalian osteoclasts, and believed to play
            a role in bone resorption. In peptidase family C1 (papain family)
REFERENCE   1  [PMID:7818555]
  AUTHORS   Inaoka T, Bilbe G, Ishibashi O, Tezuka K, Kumegawa M, Kokubo T.
  TITLE     Molecular cloning of human cDNA for cathepsin K: novel cysteine
            proteinase predominantly expressed in bone.
  JOURNAL   Biochem. Biophys. Res. Commun. 206 (1995) 89-96.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:8647860]
  AUTHORS   Bossard MJ, Tomaszek TA, Thompson SK, Amegadzie BY, Hanning CR,
            Jones C, Kurdyla JT, McNulty DE, Drake FH, Gowen M, Levy MA.
  TITLE     Proteolytic activity of human osteoclast cathepsin K. Expression,
            purification, activation, and substrate identification.
  JOURNAL   J. Biol. Chem. 271 (1996) 12517-24.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:8670136]
  AUTHORS   Bromme D, Klaus JL, Okamoto K, Rasnick D, Palmer JT.
  TITLE     Peptidyl vinyl sulphones: a new class of potent and selective
            cysteine protease inhibitors: S2P2 specificity of human cathepsin O2
            in comparison with cathepsins S and L.
  JOURNAL   Biochem. J. 315 ( Pt 1) (1996) 85-9.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:9033588]
  AUTHORS   Zhao B, Janson CA, Amegadzie BY, D'Alessio K, Griffin C, Hanning CR,
            Jones C, Kurdyla J, McQueney M, Qiu X, Smith WW, Abdel-Meguid SS.
  TITLE     Crystal structure of human osteoclast cathepsin K complex with E-64.
  JOURNAL   Nat. Struct. Biol. 4 (1997) 109-11.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:9033587]
  AUTHORS   McGrath ME, Klaus JL, Barnes MG, Bromme D.
  TITLE     Crystal structure of human cathepsin K complexed with a potent
            inhibitor.
  JOURNAL   Nat. Struct. Biol. 4 (1997) 105-9.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01371  cathepsin K
GENES       HSA: 1513(CTSK)
            PTR: 457278(CTSK)
            MMU: 13038(Ctsk)
            RNO: 29175(Ctsk)
            CFA: 608843(CTSK)
            BTA: 513038(CTSK)
            SSC: 397569(CTSK)
            GGA: 395818(LOC395818)
            XTR: 448216(ctsk)
            DRE: 550475(ctsk)
            SPU: 758756(LOC758756)
            DME: Dmel_CG4847 Dmel_CG8947(26-29-p)
STRUCTURES  PDB: 1ATK  1AU0  1AU2  1AU3  1AU4  1AYU  1AYV  1AYW  1BGO  1BY8  
                 1MEM  1NL6  1NLJ  1Q6K  1SNK  1TU6  1U9V  1U9W  1U9X  1VSN  
                 1YK7  1YK8  1YT7  2ATO  2AUX  2AUZ  2BDL  2F7D  2FTD  7PCK  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.38
            ExPASy - ENZYME nomenclature database: 3.4.22.38
            ExplorEnz - The Enzyme Database: 3.4.22.38
            ERGO genome analysis and discovery system: 3.4.22.38
            BRENDA, the Enzyme Database: 3.4.22.38
            CAS: 94716-09-3
///
ENTRY       EC 3.4.22.39                Enzyme
NAME        adenain
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Cleaves proteins of the adenovirus and its host cell at two
            consensus sites: -Yaa-Xaa-Gly-Gly!Xaa- and -Yaa-Xaa-Gly-Xaa!Gly- (in
            which Yaa is Met, Ile or Leu, and Xaa is any amino acid)
COMMENT     A cysteine endopeptidase from adenoviruses, the type example of
            peptidase family C5, with a protein fold unlike that known for any
            other peptidase [2]. Activity is greatly stimulated by the binding
            to the enzyme of an 11-residue peptide from the adenovirus capsid
            protein pre-VI at a site separate from the active site [1]
REFERENCE   1  [PMID:8422686]
  AUTHORS   Webster A, Hay RT, Kemp G.
  TITLE     The adenovirus protease is activated by a virus-coded
            disulphide-linked peptide.
  JOURNAL   Cell. 72 (1993) 97-104.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:8617222]
  AUTHORS   Ding J, McGrath WJ, Sweet RM, Mangel WF.
  TITLE     Crystal structure of the human adenovirus proteinase with its 11
            amino acid cofactor.
  JOURNAL   EMBO. J. 15 (1996) 1778-83.
  ORGANISM  human [GN:hsa]
REFERENCE   3
  AUTHORS   Weber, J.M.
  TITLE     Adenovirus protease.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Academic Press, London, 1998, p.
            741-743.
STRUCTURES  PDB: 1NLN  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.39
            ExPASy - ENZYME nomenclature database: 3.4.22.39
            ExplorEnz - The Enzyme Database: 3.4.22.39
            ERGO genome analysis and discovery system: 3.4.22.39
            BRENDA, the Enzyme Database: 3.4.22.39
            CAS: 369652-03-9
///
ENTRY       EC 3.4.22.40                Enzyme
NAME        bleomycin hydrolase;
            aminopeptidase C (Lactococcus lactis) [4]
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by
            hydrolysis of a carboxyamide bond of beta-aminoalanine, but also
            shows general aminopeptidase activity. The specificity varies
            somewhat with source, but amino acid arylamides of Met, Leu and Ala
            are preferred [1]
REFERENCE   1  [PMID:8639621]
  AUTHORS   Bromme D, Rossi AB, Smeekens SP, Anderson DC, Payan DG.
  TITLE     Human bleomycin hydrolase: molecular cloning, sequencing, functional
            expression, and enzymatic characterization.
  JOURNAL   Biochemistry. 35 (1996) 6706-14.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:9151954]
  AUTHORS   Adachi H, Tsujimoto M, Fukasawa M, Sato Y, Arai H, Inoue K,
            Nishimura T.
  TITLE     cDNA cloning and expression of chicken aminopeptidase H, possessing
            endopeptidase as well as aminopeptidase activity.
  JOURNAL   Eur. J. Biochem. 245 (1997) 283-8.
  ORGANISM  chicken [GN:gga]
REFERENCE   3  [PMID:9546396]
  AUTHORS   Zheng W, Johnston SA, Joshua-Tor L.
  TITLE     The unusual active site of Gal6/bleomycin hydrolase can act as a
            carboxypeptidase, aminopeptidase, and peptide ligase.
  JOURNAL   Cell. 93 (1998) 103-9.
REFERENCE   4  [PMID:9546047]
  AUTHORS   Mistou MY, Gripon JC.
  TITLE     Catalytic properties of the cysteine aminopeptidase PepC, a
            bacterial bleomycin hydrolase.
  JOURNAL   Biochim. Biophys. Acta. 1383 (1998) 63-70.
  ORGANISM  Lactococcus lactis
ORTHOLOGY   KO: K01372  bleomycin hydrolase
GENES       HSA: 642(BLMH)
            PTR: 454555(BLMH)
            MMU: 104184(Blmh)
            RNO: 287552(Blmh)
            CFA: 480635(BLMH)
            BTA: 504483(LOC504483)
            GGA: 395996(BLMH)
            XTR: 448747(blmh)
            DRE: 336541(blmh)
            SPU: 752414(LOC752414)
            DME: Dmel_CG1440
            SCE: YNL239W(LAP3)
            AGO: AGOS_ABL204W
            CGR: CAGL0J07568g
            ANI: AN6399.2
            AOR: AO090005000599
            UMA: UM01232.1
            BBA: Bd1649(pepC)
            LMO: lmo2338(pepC)
            LMF: LMOf2365_2308
            LIN: lin2432(pepC)
            LWE: lwe2290
            LLA: L130687(pepC)
            LLC: LACR_2073
            LLM: llmg_2069(pepC)
            SPY: SPy_1651(pepC)
            SPZ: M5005_Spy_1356(pepC)
            SPM: spyM18_1662(pepC)
            SPG: SpyM3_1391(pepC)
            SPS: SPs0471
            SPH: MGAS10270_Spy1473(pepC)
            SPI: MGAS10750_Spy1465(pepC)
            SPJ: MGAS2096_Spy1378(pepC)
            SPK: MGAS9429_Spy1352(pepC)
            SPF: SpyM50435(pepC)
            SPA: M6_Spy1402
            SPB: M28_Spy1397(pepC)
            SPN: SP_0281
            SPR: spr0258(pepC)
            SPD: SPD_0261(pepC)
            SAG: SAG0297(pepC)
            SAN: gbs0287(pepC)
            SAK: SAK_0369(pepC)
            SMU: SMU.466(pepC)
            STC: str0229(pepC)
            STL: stu0229(pepC)
            STE: STER_0276
            SSA: SSA_1861(pepC)
            SSU: SSU05_1709
            SSV: SSU98_1721
            LPL: lp_0601(pepC1)
            LJO: LJ0395 LJ0716 LJ0719
            LAC: LBA0343
            LSA: LSA1686(pepC1N) LSA1687(pepC1C) LSA1688(pepC2)
            LSL: LSL_1253(pepC)
            LDB: Ldb1730(pepC)
            LBU: LBUL_1604
            LBR: LVIS_0572
            LCA: LSEI_2328 LSEI_2329
            LGA: LGAS_0334
            LRE: Lreu_0297 Lreu_1881
            PPE: PEPE_1507
            EFA: EF0302(pepC)
            OOE: OEOE_0461
            LME: LEUM_1760
            MPE: MYPE9890(pepC) MYPE9900(pepC)
            MGA: MGA_0100(pepC) MGA_0101(pepC)
            BLO: BL0173(pepC1) BL0321(pepC2)
            BAD: BAD_0272(pepC2) BAD_0964(pepC1)
            TPA: TP0112
            BTH: BT_1161
            BFR: BF2010
            BFS: BF2064
            PGI: PG1605(pepC)
            FPS: FP2369(pepC)
STRUCTURES  PDB: 2DZY  2DZZ  2E01  2E02  2E03  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.40
            ExPASy - ENZYME nomenclature database: 3.4.22.40
            ExplorEnz - The Enzyme Database: 3.4.22.40
            ERGO genome analysis and discovery system: 3.4.22.40
            BRENDA, the Enzyme Database: 3.4.22.40
            CAS: 53096-17-6
///
ENTRY       EC 3.4.22.41                Enzyme
NAME        cathepsin F
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    The recombinant enzyme cleaves synthetic substrates with Phe and Leu
            (better than Val) in P2, with high specificity constant (kcat/Km)
            comparable to that of cathepsin L
COMMENT     Cathepsin F is a lysosomal cysteine endopeptidase of family C1
            (papain family), most active at pH 5.9. The enzyme is unstable at
            neutral pH values and is inhibited by compound E-64. Cathepsin F is
            expressed in most tissues of human, mouse and rat. Human gene locus:
            11q13.1-13.3
REFERENCE   1  [PMID:10318784]
  AUTHORS   Santamaria I, Velasco G, Pendas AM, Paz A, Lopez-Otin C.
  TITLE     Molecular cloning and structural and functional characterization of
            human cathepsin F, a new cysteine proteinase of the papain family
            with a long propeptide domain.
  JOURNAL   J. Biol. Chem. 274 (1999) 13800-9.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:10198209]
  AUTHORS   Nagler DK, Sulea T, Menard R.
  TITLE     Full-length cDNA of human cathepsin F predicts the presence of a
            cystatin domain at the N-terminus of the cysteine protease zymogen.
  JOURNAL   Biochem. Biophys. Res. Commun. 257 (1999) 313-8.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:10362521]
  AUTHORS   Wex T, Levy B, Wex H, Bromme D.
  TITLE     Human cathepsins F and W: A new subgroup of cathepsins.
  JOURNAL   Biochem. Biophys. Res. Commun. 259 (1999) 401-7.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:9822672]
  AUTHORS   Wang B, Shi GP, Yao PM, Li Z, Chapman HA, Bromme D.
  TITLE     Human cathepsin F. Molecular cloning, functional expression, tissue
            localization, and enzymatic characterization.
  JOURNAL   J. Biol. Chem. 273 (1998) 32000-8.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01373  cathepsin F
GENES       MMU: 56464(Ctsf)
            RNO: 361704(Ctsf)
            CFA: 476010(CTSF)
            BTA: 509715(MGC140519)
            DRE: 565588(zgc:153093)
            CEL: F41E6.6(tag-196)
            TET: TTHERM_00016590
STRUCTURES  PDB: 1M6D  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.41
            ExPASy - ENZYME nomenclature database: 3.4.22.41
            ExplorEnz - The Enzyme Database: 3.4.22.41
            ERGO genome analysis and discovery system: 3.4.22.41
            BRENDA, the Enzyme Database: 3.4.22.41
///
ENTRY       EC 3.4.22.42                Enzyme
NAME        cathepsin O
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    The recombinant human enzyme hydrolyses synthetic endopeptidase
            substrates including Z-Phe-Arg-NHMec and Z-Arg-Arg-NHMec
COMMENT     Cathepsin O is a lysosomal cysteine peptidase of family C1 (papain
            family). The recombinant human enzyme is catalytically active at pH
            6.0 and is inhibited by compound E-64. Cathepsin O is ubiquitously
            expressed in human tissues and the human gene locus is 4q31-32
REFERENCE   1  [PMID:9790772]
  AUTHORS   Santamaria I, Pendas AM, Velasco G, Lopez-Otin C.
  TITLE     Genomic structure and chromosomal localization of the human
            cathepsin O gene (CTSO).
  JOURNAL   Genomics. 53 (1998) 231-4.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:7929457]
  AUTHORS   Velasco G, Ferrando AA, Puente XS, Sanchez LM, Lopez-Otin C.
  TITLE     Human cathepsin O. Molecular cloning from a breast carcinoma,
            production of the active enzyme in Escherichia coli, and expression
            analysis in human tissues.
  JOURNAL   J. Biol. Chem. 269 (1994) 27136-42.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01374  cathepsin O
GENES       HSA: 1519(CTSO)
            PTR: 461567(CTSO)
            MMU: 229445(Ctso)
            CFA: 482665(CTSO)
            BTA: 616804(LOC616804)
            GGA: 422410(RCJMB04_1m17)
            DRE: 567333(LOC567333)
            SPU: 593754(LOC593754)
            TET: TTHERM_00102770
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.42
            ExPASy - ENZYME nomenclature database: 3.4.22.42
            ExplorEnz - The Enzyme Database: 3.4.22.42
            ERGO genome analysis and discovery system: 3.4.22.42
            BRENDA, the Enzyme Database: 3.4.22.42
///
ENTRY       EC 3.4.22.43                Enzyme
NAME        cathepsin V;
            Cathepsin L2;
            cathepsin U
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    The recombinant enzyme hydrolyses proteins (serum albumin, collagen)
            and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec >
            Z-Val-Arg-NHMec)
COMMENT     Cathepsin V is a human lysosomal cysteine endopeptidase of family C1
            (papain family) that is maximally active at pH 5.7 and unstable at
            neutral pH. Compound E-64, leupeptin and chicken cystatin are
            inhibitors. Human cathepsin V shows expression restricted to thymus,
            testis, corneal epithelium and some colon and breast carcinomas.
            Human gene locus: 9q22.2
REFERENCE   1  [PMID:10029531]
  AUTHORS   Bromme D, Li Z, Barnes M, Mehler E.
  TITLE     Human cathepsin V functional expression, tissue distribution,
            electrostatic surface potential, enzymatic characterization, and
            chromosomal localization.
  JOURNAL   Biochemistry. 38 (1999) 2377-85.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:9727401]
  AUTHORS   Adachi W, Kawamoto S, Ohno I, Nishida K, Kinoshita S, Matsubara K,
            Okubo K.
  TITLE     Isolation and characterization of human cathepsin V: a major
            proteinase in corneal epithelium.
  JOURNAL   Invest. Ophthalmol. Vis. Sci. 39 (1998) 1789-96.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:9563472]
  AUTHORS   Santamaria I, Velasco G, Cazorla M, Fueyo A, Campo E, Lopez-Otin C.
  TITLE     Cathepsin L2, a novel human cysteine proteinase produced by breast
            and colorectal carcinomas.
  JOURNAL   Cancer. Res. 58 (1998) 1624-30.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01375  cathepsin V
GENES       HSA: 1515(CTSL2)
            CFA: 403708(CTSL2)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.43
            ExPASy - ENZYME nomenclature database: 3.4.22.43
            ExplorEnz - The Enzyme Database: 3.4.22.43
            ERGO genome analysis and discovery system: 3.4.22.43
            BRENDA, the Enzyme Database: 3.4.22.43
///
ENTRY       EC 3.4.22.44                Enzyme
NAME        nuclear-inclusion-a endopeptidase;
            potyvirus NIa protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Hydrolyses glutaminyl bonds, and activity is further restricted by
            preferences for the amino acids in P6 - P1' that vary with the
            species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln!(Ser or Gly) for
            the enzyme from tobacco etch virus. The natural substrate is the
            viral polyprotein, but other proteins and oligopeptides containing
            the appropriate consensus sequence are also cleaved.
COMMENT     The potyviruses cause diseases in plants, and inclusion bodies
            appear in the host cell nuclei; protein a of the inclusion bodies is
            the endopeptidase. The enzyme finds practical use when encoded in
            vectors for the artificial expression of recombinant fusion
            proteins, since it can confer on them the capacity for autolytic
            cleavage. It is also reported that transgenic plants expressing the
            enzyme are resistant to viral infection. Type example of peptidase
            family C4.
REFERENCE   1
  AUTHORS   Fellers, J.P., Collins, G.B. and Hunt, A.G.
  TITLE     The NIa-proteinase of different plant potyviruses provides specific
            resistance to viral infection.
  JOURNAL   Crop Sci. 38 (1998) 1309-1319.
REFERENCE   2
  AUTHORS   Kim, D.-H. and Choi, K.Y.
  TITLE     Potyvirus NIa protease.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Academic Press, London, 1998, p.
            721-723.
REFERENCE   3  [PMID:9648226]
  AUTHORS   Takahashi T, Nakanishi M, Yao Y, Uyeda I, Serizawa N.
  TITLE     Direct formation of human interleukin-11 by cis-acting system of
            plant virus protease in Escherichia coli.
  JOURNAL   Biosci. Biotechnol. Biochem. 62 (1998) 953-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:8955037]
  AUTHORS   Kim DH, Hwang DC, Kang BH, Lew J, Han J, Song BD, Choi KY.
  TITLE     Effects of internal cleavages and mutations in the C-terminal region
            of NIa protease of turnip mosaic potyvirus on the catalytic
            activity.
  JOURNAL   Virology. 226 (1996) 183-90.
GENES       BUR: Bcep18194_C7264
STRUCTURES  PDB: 1Q31  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.44
            ExPASy - ENZYME nomenclature database: 3.4.22.44
            ExplorEnz - The Enzyme Database: 3.4.22.44
            ERGO genome analysis and discovery system: 3.4.22.44
            BRENDA, the Enzyme Database: 3.4.22.44
///
ENTRY       EC 3.4.22.45                Enzyme
NAME        helper-component proteinase;
            HC-Pro
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Hydrolyses a Gly!Gly bond at its own C-terminus, commonly in the
            sequence -Tyr-Xaa-Val-Gly!Gly, in the processing of the potyviral
            polyprotein
COMMENT     Known from many potyviruses. The helper component-proteinase of the
            tobacco etch virus is a multifunctional protein with several known
            activities: the N-terminal region is required for aphid transmission
            and efficient genome amplification, the central region is required
            for long-distance movement in plants, and the C-terminal domain has
            cysteine endopeptidase activity. Type example of peptidase family
            C6.
REFERENCE   1  [PMID:7747479]
  AUTHORS   Kasschau KD, Carrington JC.
  TITLE     Requirement for HC-Pro processing during genome amplification of
            tobacco etch potyvirus.
  JOURNAL   Virology. 209 (1995) 268-73.
  ORGANISM  Nicotiana tabacum
REFERENCE   2
  AUTHORS   Verchot, J.
  TITLE     Potyvirus helper component proteinase.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Handbook of Proteolytic Enzymes,
            London, 1998, p. 677-679.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.45
            ExPASy - ENZYME nomenclature database: 3.4.22.45
            ExplorEnz - The Enzyme Database: 3.4.22.45
            ERGO genome analysis and discovery system: 3.4.22.45
            BRENDA, the Enzyme Database: 3.4.22.45
///
ENTRY       EC 3.4.22.46                Enzyme
NAME        L-peptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Autocatalytically cleaves itself from the polyprotein of the
            foot-and-mouth disease virus by hydrolysis of a Lys!Gly bond, but
            then cleaves host cell initiation factor eIF-4G at bonds -Gly!Arg-
            and -Lys!Arg-
COMMENT     Best known from foot-and-mouth disease virus, but occurs in other
            aphthoviruses and cardioviruses. Destruction of initiation factor
            eIF-4G has the effect of shutting off host-cell protein synthesis
            while allowing synthesis of viral proteins to continue. The tertiary
            structure reveals a distant relationship to papain and, consistent
            with this, compound E-64 is inhibitory. Type example of peptidase
            family C28.
REFERENCE   1  [PMID:7609064]
  AUTHORS   Piccone ME, Zellner M, Kumosinski TF, Mason PW, Grubman MJ.
  TITLE     Identification of the active-site residues of the L proteinase of
            foot-and-mouth disease virus.
  JOURNAL   J. Virol. 69 (1995) 4950-6.
REFERENCE   2  [PMID:11183785]
  AUTHORS   Guarne A, Hampoelz B, Glaser W, Carpena X, Tormo J, Fita I, Skern T.
  TITLE     Structural and biochemical features distinguish the foot-and-mouth
            disease virus leader proteinase from other papain-like enzymes.
  JOURNAL   J. Mol. Biol. 302 (2000) 1227-40.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.46
            ExPASy - ENZYME nomenclature database: 3.4.22.46
            ExplorEnz - The Enzyme Database: 3.4.22.46
            ERGO genome analysis and discovery system: 3.4.22.46
            BRENDA, the Enzyme Database: 3.4.22.46
///
ENTRY       EC 3.4.22.47                Enzyme
NAME        gingipain K;
            Lys-gingipain;
            PrtP proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Endopeptidase with strict specificity for lysyl bonds
COMMENT     Activity is stimulated by glycine. Known from the bacterium
            Porphyromonas gingivalis and contributes to the pathogenicity of the
            organism. In peptidase family C25.
REFERENCE   1  [PMID:8276827]
  AUTHORS   Pike R, McGraw W, Potempa J, Travis J.
  TITLE     Lysine- and arginine-specific proteinases from Porphyromonas
            gingivalis. Isolation, characterization, and evidence for the
            existence of complexes with hemagglutinins.
  JOURNAL   J. Biol. Chem. 269 (1994) 406-11.
  ORGANISM  Porphyromonas gingivalis [GN:pgi]
REFERENCE   2  [PMID:12438376]
  AUTHORS   Curtis MA, Aduse Opoku J, Rangarajan M, Gallagher A, Sterne JA, Reid
            CR, Evans HE, Samuelsson B.
  TITLE     Attenuation of the virulence of Porphyromonas gingivalis by using a
            specific synthetic Kgp protease inhibitor.
  JOURNAL   Infect. Immun. 70 (2002) 6968-75.
  ORGANISM  Porphyromonas gingivalis [GN:pgi]
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.47
            ExPASy - ENZYME nomenclature database: 3.4.22.47
            ExplorEnz - The Enzyme Database: 3.4.22.47
            ERGO genome analysis and discovery system: 3.4.22.47
            BRENDA, the Enzyme Database: 3.4.22.47
///
ENTRY       EC 3.4.22.48                Enzyme
NAME        staphopain;
            staphylopain
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Broad endopeptidase action on proteins including elastin, but rather
            limited hydrolysis of small-molecule substrates. Assays are
            conveniently made with hemoglobin, casein or Z-Phe-Arg-NHMec as
            substrate
COMMENT     Known from species of Staphylococcus. Type example of peptidase
            family C47.
REFERENCE   1
  AUTHORS   Hofmann, B., Hecht, H.J., Kiess, M. and Schomburg, D.
  TITLE     Crystal structure of a thiol proteinase from Staphylococcus aureus
            V8 in the E-64 inhibitor complex.
  JOURNAL   Acta Crystallogr. Sect. A (Suppl.) 49 (1993) 102.
  ORGANISM  Staphylococcus aureus
REFERENCE   2
  AUTHORS   Potempa, J., Dubin, A. and Travis, J.
  TITLE     Staphylopain.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Handbook of Proteolytic Enzymes,
            London, 1998, p. 669-671.
REFERENCE   3  [PMID:11767947]
  AUTHORS   Dubin G, Chmiel D, Mak P, Rakwalska M, Rzychon M, Dubin A.
  TITLE     Molecular cloning and biochemical characterisation of proteases from
            Staphylococcus epidermidis.
  JOURNAL   Biol. Chem. 382 (2001) 1575-82.
  ORGANISM  Staphylococcus epidermidis
ORTHOLOGY   KO: K08258  staphopain
GENES       SAU: SA1725
            SAV: SAV1909
            SAM: MW1850
            SAR: SAR2001
            SAS: SAS1832
            SAC: SACOL1970(sspB2)
            SAB: SAB1845
            SAA: SAUSA300_0950(sspB) SAUSA300_1890
            SAO: SAOUHSC_02127
            SAH: SaurJH1_1129 SaurJH1_1998
            SEP: SE0184
            SER: SERP2390(sspB)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.48
            ExPASy - ENZYME nomenclature database: 3.4.22.48
            ExplorEnz - The Enzyme Database: 3.4.22.48
            ERGO genome analysis and discovery system: 3.4.22.48
            BRENDA, the Enzyme Database: 3.4.22.48
///
ENTRY       EC 3.4.22.49                Enzyme
NAME        separase;
            separin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    All bonds known to be hydrolysed by this endopeptidase have arginine
            in P1 and an acidic residue in P4. P6 is often occupied by an acidic
            residue or by an hydroxy-amino-acid residue, the phosphorylation of
            which enhances cleavage
COMMENT     In both budding yeast and human cells, cleavage of the cohesin
            subunit Scc1 by separase is required for sister chromatid separation
            in mitosis. Budding yeast separase is also known to cleave the Rec8
            subunit of a meiotic cohesin complex and the kinetochore protein
            Slk19. Type example of peptidase family C50.
REFERENCE   1  [PMID:12194817]
  AUTHORS   Waizenegger I, Gimenez-Abian JF, Wernic D, Peters JM.
  TITLE     Regulation of human separase by securin binding and autocleavage.
  JOURNAL   Curr. Biol. 12 (2002) 1368-78.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04110  Cell cycle
            PATH: map04111  Cell cycle - yeast
ORTHOLOGY   KO: K02365  separase
GENES       HSA: 9700(ESPL1)
            MMU: 105988(Espl1)
            RNO: 315330(Espl1_predicted)
            CFA: 607879(ESPL1)
            BTA: 506740(ESPL1)
            GGA: 425536(ESPL1)
            DRE: 568818(LOC568818)
            SPU: 576865(LOC576865)
            DME: Dmel_CG10583(Sse)
            CEL: Y47G6A.12(sep-1)
            OSA: 4330866
            CME: CMD159C
            SCE: YGR098C(ESP1)
            AGO: AGOS_AAR089C
            PIC: PICST_28228(ESP1)
            CGR: CAGL0G03223g
            SPO: SPCC5E4.04(cut1)
            ANI: AN8783.2
            AFM: AFUA_5G09710
            AOR: AO090005000276
            CNE: CNB00660
            ECU: ECU07_0350
            DDI: DDBDRAFT_0188839
            CPV: cgd7_2760
            CHO: Chro.70313
            TBR: Tb927.1.3120
            TCR: 507837.10 508405.80
            LMA: LmjF20.1680
            EHI: 182.t00017
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.49
            ExPASy - ENZYME nomenclature database: 3.4.22.49
            ExplorEnz - The Enzyme Database: 3.4.22.49
            ERGO genome analysis and discovery system: 3.4.22.49
            BRENDA, the Enzyme Database: 3.4.22.49
///
ENTRY       EC 3.4.22.50                Enzyme
NAME        V-cath endopeptidase;
            AcNPV protease;
            BmNPV protease;
            NPV protease;
            baculovirus cathepsin;
            nucleopolyhedrosis virus protease;
            viral cathepsin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Endopeptidase of broad specificity, hydrolyzing substrates of both
            cathepsin L and cathepsin B
COMMENT     In peptidase family C1. Contributes to the liquefaction of the
            tissues of the insect host in the late stages of infection by the
            baculovirus.
REFERENCE   1  [PMID:7730794]
  AUTHORS   Slack JM, Kuzio J, Faulkner P.
  TITLE     Characterization of v-cath, a cathepsin L-like proteinase expressed
            by the baculovirus Autographa californica multiple nuclear
            polyhedrosis virus.
  JOURNAL   J. Gen. Virol. 76 ( Pt 5) (1995) 1091-8.
  ORGANISM  Autographa californica
REFERENCE   2  [PMID:9400597]
  AUTHORS   Hawtin RE, Zarkowska T, Arnold K, Thomas CJ, Gooday GW, King LA,
            Kuzio JA, Possee RD.
  TITLE     Liquefaction of Autographa californica nucleopolyhedrovirus-infected
            insects is dependent on the integrity of virus-encoded chitinase and
            cathepsin genes.
  JOURNAL   Virology. 238 (1997) 243-53.
  ORGANISM  Autographa californica
GENES       TET: TTHERM_00102770 TTHERM_00925850 TTHERM_00925870
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.50
            ExPASy - ENZYME nomenclature database: 3.4.22.50
            ExplorEnz - The Enzyme Database: 3.4.22.50
            ERGO genome analysis and discovery system: 3.4.22.50
            BRENDA, the Enzyme Database: 3.4.22.50
///
ENTRY       EC 3.4.22.51                Enzyme
NAME        cruzipain;
            congopain;
            cruzain;
            evansain;
            trypanopain
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Broad endopeptidase specificity similar to that of cathepsin L
COMMENT     In peptidase family C1. Is located in the digestive vacuoles of the
            parasitic trypanosome and contributes to the nutrition of the
            organism by digestion of host proteins.
REFERENCE   1  [PMID:11472258]
  AUTHORS   Jose Cazzulo J, Stoka V, Turk V.
  TITLE     The major cysteine proteinase of Trypanosoma cruzi: a valid target
            for chemotherapy of Chagas disease.
  JOURNAL   Curr. Pharm. Des. 7 (2001) 1143-56.
  ORGANISM  Trypanosoma cruzi [GN:tcr]
ORTHOLOGY   KO: K08571  cruzipain
GENES       TCR: 507297.10 508595.50 509429.329 510889.261
STRUCTURES  PDB: 1U9Q  2OQZ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.51
            ExPASy - ENZYME nomenclature database: 3.4.22.51
            ExplorEnz - The Enzyme Database: 3.4.22.51
            ERGO genome analysis and discovery system: 3.4.22.51
            BRENDA, the Enzyme Database: 3.4.22.51
///
ENTRY       EC 3.4.22.52                Enzyme
NAME        calpain-1;
            mu-calpain;
            calcium-activated neutral protease I
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Broad endopeptidase specificity
COMMENT     In peptidase family C2. Requires Ca2+ at micromolar concentrations
            for activity. Cytosolic in animal cells. The active enzyme molecule
            is a heterodimer in which the large subunit contains the peptidase
            unit, and the small subunit is also a component of EC 3.4.22.53,
            calpain-2.
REFERENCE   1  [PMID:12014988]
  AUTHORS   Dutt P, Spriggs CN, Davies PL, Jia Z, Elce JS.
  TITLE     Origins of the difference in Ca2+ requirement for activation of mu-
            and m-calpain.
  JOURNAL   Biochem. J. 367 (2002) 263-9.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map04210  Apoptosis
ORTHOLOGY   KO: K01367  calpain-1
GENES       HSA: 823(CAPN1)
            PTR: 451317(CAPN1)
            MMU: 12333(Capn1)
            RNO: 29153(Capn1)
            CFA: 483745(CAPN1)
            BTA: 281661(CAPN1)
            SSC: 397027(CAPN1)
            GGA: 396240(CAPN1) 693249(LOC693249)
            XLA: 380177(capn1)
            XTR: 541455(CAPN1)
            DRE: 393417(capn1a) 406768(zgc:55262)
            AFM: AFUA_6G07970
            TET: TTHERM_00051890 TTHERM_00196650 TTHERM_00387030
                 TTHERM_00885870 TTHERM_00898290 TTHERM_00979860
                 TTHERM_01084250 TTHERM_01261780
STRUCTURES  PDB: 1QXP  1TL9  1TLO  1ZCM  2ARY  2G8E  2G8J  2NQA  2NQG  2NQI  
                 2P0R  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.52
            ExPASy - ENZYME nomenclature database: 3.4.22.52
            ExplorEnz - The Enzyme Database: 3.4.22.52
            ERGO genome analysis and discovery system: 3.4.22.52
            BRENDA, the Enzyme Database: 3.4.22.52
            CAS: 78990-62-2
///
ENTRY       EC 3.4.22.53                Enzyme
NAME        calpain-2;
            calcium-activated neutral protease II;
            m-calpain;
            milli-calpain
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Broad endopeptidase specificity
COMMENT     Type example of peptidase family C2. Requires Ca2+ at millimolar
            concentrations for activity. Cytosolic in animal cells. The active
            enzyme molecule is a heterodimer in which the large subunit contains
            the peptidase unit, and the small subunit is also a component of EC
            3.4.22.52, calpain-1.
REFERENCE   1  [PMID:10639123]
  AUTHORS   Strobl S, Fernandez-Catalan C, Braun M, Huber R, Masumoto H,
            Nakagawa K, Irie A, Sorimachi H, Bourenkow G, Bartunik H, Suzuki K,
            Bode W.
  TITLE     The crystal structure of calcium-free human m-calpain suggests an
            electrostatic switch mechanism for activation by calcium.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 588-92.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:12014988]
  AUTHORS   Dutt P, Spriggs CN, Davies PL, Jia Z, Elce JS.
  TITLE     Origins of the difference in Ca2+ requirement for activation of mu-
            and m-calpain.
  JOURNAL   Biochem. J. 367 (2002) 263-9.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map04210  Apoptosis
            PATH: map04510  Focal adhesion
ORTHOLOGY   KO: K03853  calpain-2
GENES       HSA: 824(CAPN2)
            MMU: 12334(Capn2)
            RNO: 29154(Capn2)
            CFA: 480118(CAPN2)
            BTA: 281662(CAPN2)
            GGA: 395963(CAPN2)
            XLA: 399075(MGC68474)
            XTR: 448035(capn2)
            DRE: 550505(zgc:112420)
            TET: TTHERM_01108610
STRUCTURES  PDB: 1U5I  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.53
            ExPASy - ENZYME nomenclature database: 3.4.22.53
            ExplorEnz - The Enzyme Database: 3.4.22.53
            ERGO genome analysis and discovery system: 3.4.22.53
            BRENDA, the Enzyme Database: 3.4.22.53
            CAS: 78990-62-2
///
ENTRY       EC 3.4.22.54                Enzyme
NAME        calpain-3;
            p94;
            calpain p94;
            CAPN3;
            muscle calpain;
            calpain 3;
            calcium-activated neutral proteinase 3;
            muscle-specific calcium-activated neutral protease 3;
            CANP 3;
            calpain L3
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Broad endopeptidase activity
COMMENT     This Ca2+-dependent enzyme is found in skeletal muscle and is
            genetically linked to limb girdle muscular dystrophy type 2A [1,4].
            The enzyme is activated by autoproteolytic cleavage of insertion
            sequence 1 (IS1), which allows substrates and inhibitors gain access
            to the active site [4]. Substrates include the protein itself [3,4]
            and connectin/titin [2,5]. Belongs in peptidase family C2.
REFERENCE   1  [PMID:2555341]
  AUTHORS   Sorimachi H, Imajoh-Ohmi S, Emori Y, Kawasaki H, Ohno S, Minami Y,
            Suzuki K.
  TITLE     Molecular cloning of a novel mammalian calcium-dependent protease
            distinct from both m- and mu-types. Specific expression of the mRNA
            in skeletal muscle.
  JOURNAL   J. Biol. Chem. 264 (1989) 20106-11.
REFERENCE   2  [PMID:8537379]
  AUTHORS   Sorimachi H, Kinbara K, Kimura S, Takahashi M, Ishiura S, Sasagawa
            N, Sorimachi N, Shimada H, Tagawa K, Maruyama K, et al.
  TITLE     Muscle-specific calpain, p94, responsible for limb girdle muscular
            dystrophy type 2A, associates with connectin through IS2, a
            p94-specific sequence.
  JOURNAL   J. Biol. Chem. 270 (1995) 31158-62.
REFERENCE   3  [PMID:12482600]
  AUTHORS   Rey MA, Davies PL.
  TITLE     The protease core of the muscle-specific calpain, p94, undergoes
            Ca2+-dependent intramolecular autolysis.
  JOURNAL   FEBS. Lett. 532 (2002) 401-6.
REFERENCE   4  [PMID:16533054]
  AUTHORS   Garcia Diaz BE, Gauthier S, Davies PL.
  TITLE     Ca2+ dependency of calpain 3 (p94) activation.
  JOURNAL   Biochemistry. 45 (2006) 3714-22.
REFERENCE   5  [PMID:16627476]
  AUTHORS   Ono Y, Torii F, Ojima K, Doi N, Yoshioka K, Kawabata Y, Labeit D,
            Labeit S, Suzuki K, Abe K, Maeda T, Sorimachi H.
  TITLE     Suppressed disassembly of autolyzing p94/CAPN3 by N2A
            connectin/titin in a genetic reporter system.
  JOURNAL   J. Biol. Chem. 281 (2006) 18519-31.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.54
            ExPASy - ENZYME nomenclature database: 3.4.22.54
            ExplorEnz - The Enzyme Database: 3.4.22.54
            ERGO genome analysis and discovery system: 3.4.22.54
            BRENDA, the Enzyme Database: 3.4.22.54
///
ENTRY       EC 3.4.22.55                Enzyme
NAME        caspase-2;
            ICH-1;
            NEDD-2;
            caspase-2L;
            caspase-2S;
            neural precursor cell expressed developmentally down-regulated
            protein 2;
            CASP-2;
            NEDD2 protein
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Strict requirement for an Asp residue at P1, with Asp316 being
            essential for proteolytic activity and has a preferred cleavage
            sequence of Val-Asp-Val-Ala-Asp!
COMMENT     Caspase-2 is an initiator caspase, as are caspase-8 (EC 3.4.22.61),
            caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.64) [6]. Contains
            a caspase-recruitment domain (CARD) in its N-terminal prodomain,
            which plays a role in procaspase activation [6]. Two forms of
            caspase-2 with antagonistic effects exist: caspase-2L induces
            programmed cell death and caspase-2S suppresses cell death [2,3,5].
            Caspase-2 is activated by caspase-3 (EC 3.4.22.56), or by a
            caspase-3-like protease. Activation involves cleavage of the
            N-terminal prodomain, followed by self-proteolysis between the large
            and small subunits of pro-caspase-2 and further proteolysis into
            smaller fragments [3]. Proteolysis occurs at Asp residues and the
            preferred substrate for this enzyme is a pentapeptide rather than a
            tetrapeptide [5]. Apart from itself, the enzyme can cleave
            golgin-16, which is present in the Golgi complex and has a cleavage
            site that is unique for caspase-2 [4,5]. alphaII-Spectrin, a
            component of the membrane cytoskeleton, is a substrate of the large
            isoform of pro-caspase-2 (caspase-2L) but not of the short isoform
            (caspase-2S). Belongs in peptidase family C14.
REFERENCE   1  [PMID:7958843]
  AUTHORS   Kumar S, Kinoshita M, Noda M, Copeland NG, Jenkins NA.
  TITLE     Induction of apoptosis by the mouse Nedd2 gene, which encodes a
            protein similar to the product of the Caenorhabditis elegans cell
            death gene ced-3 and the mammalian IL-1 beta-converting enzyme.
  JOURNAL   Genes. Dev. 8 (1994) 1613-26.
REFERENCE   2  [PMID:8087842]
  AUTHORS   Wang L, Miura M, Bergeron L, Zhu H, Yuan J.
  TITLE     Ich-1, an Ice/ced-3-related gene, encodes both positive and negative
            regulators of programmed cell death.
  JOURNAL   Cell. 78 (1994) 739-50.
REFERENCE   3  [PMID:9261102]
  AUTHORS   Li H, Bergeron L, Cryns V, Pasternack MS, Zhu H, Shi L, Greenberg A,
            Yuan J.
  TITLE     Activation of caspase-2 in apoptosis.
  JOURNAL   J. Biol. Chem. 272 (1997) 21010-7.
REFERENCE   4  [PMID:10791974]
  AUTHORS   Mancini M, Machamer CE, Roy S, Nicholson DW, Thornberry NA,
            Casciola-Rosen LA, Rosen A.
  TITLE     Caspase-2 is localized at the Golgi complex and cleaves golgin-160
            during apoptosis.
  JOURNAL   J. Cell. Biol. 149 (2000) 603-12.
REFERENCE   5  [PMID:15865942]
  AUTHORS   Zhivotovsky B, Orrenius S.
  TITLE     Caspase-2 function in response to DNA damage.
  JOURNAL   Biochem. Biophys. Res. Commun. 331 (2005) 859-67.
REFERENCE   6  [PMID:11104820]
  AUTHORS   Chang HY, Yang X.
  TITLE     Proteases for cell suicide: functions and regulation of caspases.
  JOURNAL   Microbiol. Mol. Biol. Rev. 64 (2000) 821-46.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.55
            ExPASy - ENZYME nomenclature database: 3.4.22.55
            ExplorEnz - The Enzyme Database: 3.4.22.55
            ERGO genome analysis and discovery system: 3.4.22.55
            BRENDA, the Enzyme Database: 3.4.22.55
///
ENTRY       EC 3.4.22.56                Enzyme
NAME        caspase-3;
            CPP32;
            apopain;
            yama protein
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Strict requirement for an Asp residue at positions P1 and P4. It has
            a preferred cleavage sequence of Asp-Xaa-Xaa-Asp! with a hydrophobic
            amino-acid residue at P2 and a hydrophilic amino-acid residue at P3,
            although Val or Ala are also accepted at this position
COMMENT     Caspase-3 is an effector/executioner caspase, as are caspase-6 (EC
            3.4.22.59) and caspase-7 (EC 3.4.22.60) [5]. These caspases are
            responsible for the proteolysis of the majority of cellular
            polypeptides [e.g. poly(ADP-ribose) polymerase (PARP)], which leads
            to the apoptotic phenotype [3,5]. Procaspase-3 can be activated by
            caspase-1 (EC 3.4.22.36), caspase-8 (EC 3.4.22.61), caspase-9 (EC
            3.4.22.62) and caspase-10 (EC 3.4.22.63) as well as by the serine
            protease granzyme B [1]. Caspase-3 can activate procaspase-2 (EC
            3.4.22.55) [2]. Activation occurs by inter-domain cleavage followed
            by removal of the N-terminal prodomain [6]. Although
            Asp-Glu-(Val/Ile)-Asp is thought to be the preferred cleavage
            sequence, the enzyme can accommodate different residues at P2 and P3
            of the substrate [4]. Like caspase-2, a hydrophobic residue at P5 of
            caspase-3 leads to more efficient hydrolysis, e.g.
            (Val/Leu)-Asp-Val-Ala-Asp! is a better substrate than
            Asp-Val-Ala-Asp! . This is not the case for caspase-7 [4]. Belongs
            in peptidase family C14.
REFERENCE   1  [PMID:11123933]
  AUTHORS   Krebs JF, Srinivasan A, Wong AM, Tomaselli KJ, Fritz LC, Wu JC.
  TITLE     Heavy membrane-associated caspase 3: identification, isolation, and
            characterization.
  JOURNAL   Biochemistry. 39 (2000) 16056-63.
REFERENCE   2  [PMID:9261102]
  AUTHORS   Li H, Bergeron L, Cryns V, Pasternack MS, Zhu H, Shi L, Greenberg A,
            Yuan J.
  TITLE     Activation of caspase-2 in apoptosis.
  JOURNAL   J. Biol. Chem. 272 (1997) 21010-7.
REFERENCE   3
  AUTHORS   Nicholson, D. and Thornberry, N.A.
  TITLE     Caspase-3 and caspase-7.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, 2nd ed., Elsevier, London, 2004, p.
            1298-1302.
REFERENCE   4  [PMID:16781734]
  AUTHORS   Fang B, Boross PI, Tozser J, Weber IT.
  TITLE     Structural and kinetic analysis of caspase-3 reveals role for s5
            binding site in substrate recognition.
  JOURNAL   J. Mol. Biol. 360 (2006) 654-66.
REFERENCE   5  [PMID:11104820]
  AUTHORS   Chang HY, Yang X.
  TITLE     Proteases for cell suicide: functions and regulation of caspases.
  JOURNAL   Microbiol. Mol. Biol. Rev. 64 (2000) 821-46.
REFERENCE   6  [PMID:8665848]
  AUTHORS   Martin SJ, Amarante-Mendes GP, Shi L, Chuang TH, Casiano CA, O'Brien
            GA, Fitzgerald P, Tan EM, Bokoch GM, Greenberg AH, Green DR.
  TITLE     The cytotoxic cell protease granzyme B initiates apoptosis in a
            cell-free system by proteolytic processing and activation of the
            ICE/CED-3 family protease, CPP32, via a novel two-step mechanism.
  JOURNAL   EMBO. J. 15 (1996) 2407-16.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.56
            ExPASy - ENZYME nomenclature database: 3.4.22.56
            ExplorEnz - The Enzyme Database: 3.4.22.56
            ERGO genome analysis and discovery system: 3.4.22.56
            BRENDA, the Enzyme Database: 3.4.22.56
///
ENTRY       EC 3.4.22.57                Enzyme
NAME        caspase-4;
            ICErelII;
            ICErel-II;
            Ich-2;
            transcript X;
            TX;
            TX protease;
            caspase 4;
            CASP-4
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Strict requirement for Asp at the P1 position. It has a preferred
            cleavage sequence of Tyr-Val-Ala-Asp! but also cleaves at
            Asp-Glu-Val-Asp!
COMMENT     This enzyme is part of the family of inflammatory caspases, which
            also includes caspase-1 (EC 3.4.22.36) and caspase-5 (EC 3.4.22.58)
            in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and
            caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in
            its N-terminal prodomain, which plays a role in procaspase
            activation [3,5,6]. The enzyme is able to cleave itself and the p30
            caspase-1 precursor, but, unlike caspase-1, it is very inefficient
            at generating mature interleukin-1beta (IL-1beta) from pro-IL-1beta
            [1,4]. Both this enzyme and caspase-5 can cleave pro-caspase-3 to
            release the small subunit (p12) but not the large subunit (p17) [3].
            The caspase-1 inhibitor Ac-Tyr-Val-Ala-Asp-CHO can also inhibit this
            enzyme, but more slowly [4]. Belongs in peptidase family C14.
REFERENCE   1  [PMID:7743998]
  AUTHORS   Faucheu C, Diu A, Chan AW, Blanchet AM, Miossec C, Herve F,
            Collard-Dutilleul V, Gu Y, Aldape RA, Lippke JA, et al.
  TITLE     A novel human protease similar to the interleukin-1 beta converting
            enzyme induces apoptosis in transfected cells.
  JOURNAL   EMBO. J. 14 (1995) 1914-22.
REFERENCE   2  [PMID:7797510]
  AUTHORS   Kamens J, Paskind M, Hugunin M, Talanian RV, Allen H, Banach D, Bump
            N, Hackett M, Johnston CG, Li P, et al.
  TITLE     Identification and characterization of ICH-2, a novel member of the
            interleukin-1 beta-converting enzyme family of cysteine proteases.
  JOURNAL   J. Biol. Chem. 270 (1995) 15250-6.
REFERENCE   3  [PMID:16465268]
  AUTHORS   Kamada S, Funahashi Y, Tsujimoto Y.
  TITLE     Caspase-4 and caspase-5, members of the ICE/CED-3 family of cysteine
            proteases, are CrmA-inhibitable proteases.
  JOURNAL   Cell. Death. Differ. 4 (1997) 473-8.
REFERENCE   4  [PMID:9578463]
  AUTHORS   Fassy F, Krebs O, Rey H, Komara B, Gillard C, Capdevila C, Yea C,
            Faucheu C, Blanchet AM, Miossec C, Diu-Hercend A.
  TITLE     Enzymatic activity of two caspases related to
            interleukin-1beta-converting enzyme.
  JOURNAL   Eur. J. Biochem. 253 (1998) 76-83.
REFERENCE   5  [PMID:15163405]
  AUTHORS   Martinon F, Tschopp J.
  TITLE     Inflammatory caspases: linking an intracellular innate immune system
            to autoinflammatory diseases.
  JOURNAL   Cell. 117 (2004) 561-74.
REFERENCE   6  [PMID:11104820]
  AUTHORS   Chang HY, Yang X.
  TITLE     Proteases for cell suicide: functions and regulation of caspases.
  JOURNAL   Microbiol. Mol. Biol. Rev. 64 (2000) 821-46.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.57
            ExPASy - ENZYME nomenclature database: 3.4.22.57
            ExplorEnz - The Enzyme Database: 3.4.22.57
            ERGO genome analysis and discovery system: 3.4.22.57
            BRENDA, the Enzyme Database: 3.4.22.57
///
ENTRY       EC 3.4.22.58                Enzyme
NAME        caspase-5;
            ICErel-III;
            Ich-3;
            ICH-3 protease;
            transcript Y;
            TY;
            CASP-5
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Strict requirement for Asp at the P1 position. It has a preferred
            cleavage sequence of Tyr-Val-Ala-Asp! but also cleaves at
            Asp-Glu-Val-Asp!
COMMENT     This enzyme is part of the family of inflammatory caspases, which
            also includes caspase-1 (EC 3.4.22.36) and caspase-4 (EC 3.4.22.57)
            in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and
            caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in
            its N-terminal prodomain, which plays a role in procaspase
            activation [3,5,6]. The enzyme is able to cleave itself and the p30
            caspase-1 precursor, but is very inefficient at generating mature
            interleukin-1beta (IL-1beta) from pro-IL-1beta [1,4]. Both this
            enzyme and caspase-4 can cleave pro-caspase-3 to release the small
            subunit (p12) but not the large subunit (p17) [3]. Unlike caspase-4,
            this enzyme can be induced by lipopolysaccharide [3]. Belongs in
            peptidase family C14.
REFERENCE   1  [PMID:8617266]
  AUTHORS   Faucheu C, Blanchet AM, Collard-Dutilleul V, Lalanne JL, Diu-Hercend
            A.
  TITLE     Identification of a cysteine protease closely related to
            interleukin-1 beta-converting enzyme.
  JOURNAL   Eur. J. Biochem. 236 (1996) 207-13.
REFERENCE   2  [PMID:16465268]
  AUTHORS   Kamada S, Funahashi Y, Tsujimoto Y.
  TITLE     Caspase-4 and caspase-5, members of the ICE/CED-3 family of cysteine
            proteases, are CrmA-inhibitable proteases.
  JOURNAL   Cell. Death. Differ. 4 (1997) 473-8.
REFERENCE   3  [PMID:10986288]
  AUTHORS   Lin XY, Choi MS, Porter AG.
  TITLE     Expression analysis of the human caspase-1 subfamily reveals
            specific regulation of the CASP5 gene by lipopolysaccharide and
            interferon-gamma.
  JOURNAL   J. Biol. Chem. 275 (2000) 39920-6.
REFERENCE   4  [PMID:9578463]
  AUTHORS   Fassy F, Krebs O, Rey H, Komara B, Gillard C, Capdevila C, Yea C,
            Faucheu C, Blanchet AM, Miossec C, Diu-Hercend A.
  TITLE     Enzymatic activity of two caspases related to
            interleukin-1beta-converting enzyme.
  JOURNAL   Eur. J. Biochem. 253 (1998) 76-83.
REFERENCE   5  [PMID:15163405]
  AUTHORS   Martinon F, Tschopp J.
  TITLE     Inflammatory caspases: linking an intracellular innate immune system
            to autoinflammatory diseases.
  JOURNAL   Cell. 117 (2004) 561-74.
REFERENCE   6  [PMID:11104820]
  AUTHORS   Chang HY, Yang X.
  TITLE     Proteases for cell suicide: functions and regulation of caspases.
  JOURNAL   Microbiol. Mol. Biol. Rev. 64 (2000) 821-46.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.58
            ExPASy - ENZYME nomenclature database: 3.4.22.58
            ExplorEnz - The Enzyme Database: 3.4.22.58
            ERGO genome analysis and discovery system: 3.4.22.58
            BRENDA, the Enzyme Database: 3.4.22.58
///
ENTRY       EC 3.4.22.59                Enzyme
NAME        caspase-6;
            CASP-6;
            apoptotic protease Mch-2;
            Mch2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Strict requirement for Asp at position P1 and has a preferred
            cleavage sequence of Val-Glu-His-Asp!
COMMENT     Caspase-6 is an effector/executioner caspase, as are caspase-3 (EC
            3.4.22.56) and caspase-7 (EC 3.4.22.60) [2]. These caspases are
            responsible for the proteolysis of the majority of cellular
            polypeptides [e.g. poly(ADP-ribose) polymerase (PARP)], which leads
            to the apoptotic phenotype [2]. Caspase-6 can cleave its prodomain
            to produce mature caspase-6, which directly activates caspase-8 (EC
            3.4.22.61) and leads to the release of cytochrome c from the
            mitochondria. The release of cytochrome c is an essential component
            of the intrinsic apoptosis pathway [1]. The enzyme can also cleave
            and inactivate lamins, the intermediate filament scaffold proteins
            of the nuclear envelope, leading to nuclear fragmentation in the
            final phases of apoptosis [2,4,5,6]. Belongs in peptidase family
            C14.
REFERENCE   1  [PMID:12232792]
  AUTHORS   Cowling V, Downward J.
  TITLE     Caspase-6 is the direct activator of caspase-8 in the cytochrome
            c-induced apoptosis pathway: absolute requirement for removal of
            caspase-6 prodomain.
  JOURNAL   Cell. Death. Differ. 9 (2002) 1046-56.
REFERENCE   2  [PMID:11104820]
  AUTHORS   Chang HY, Yang X.
  TITLE     Proteases for cell suicide: functions and regulation of caspases.
  JOURNAL   Microbiol. Mol. Biol. Rev. 64 (2000) 821-46.
REFERENCE   3  [PMID:12049625]
  AUTHORS   Kang BH, Ko E, Kwon OK, Choi KY.
  TITLE     The structure of procaspase 6 is similar to that of active mature
            caspase 6.
  JOURNAL   Biochem. J. 364 (2002) 629-34.
REFERENCE   4  [PMID:16518869]
  AUTHORS   Lee SC, Chan J, Clement MV, Pervaiz S.
  TITLE     Functional proteomics of resveratrol-induced colon cancer cell
            apoptosis: caspase-6-mediated cleavage of lamin A is a major
            signaling loop.
  JOURNAL   Proteomics. 6 (2006) 2386-94.
REFERENCE   5  [PMID:12089322]
  AUTHORS   MacLachlan TK, El-Deiry WS.
  TITLE     Apoptotic threshold is lowered by p53 transactivation of caspase-6.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 9492-7.
REFERENCE   6  [PMID:8710882]
  AUTHORS   Takahashi A, Alnemri ES, Lazebnik YA, Fernandes-Alnemri T, Litwack
            G, Moir RD, Goldman RD, Poirier GG, Kaufmann SH, Earnshaw WC.
  TITLE     Cleavage of lamin A by Mch2 alpha but not CPP32: multiple
            interleukin 1 beta-converting enzyme-related proteases with distinct
            substrate recognition properties are active in apoptosis.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 8395-400.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.59
            ExPASy - ENZYME nomenclature database: 3.4.22.59
            ExplorEnz - The Enzyme Database: 3.4.22.59
            ERGO genome analysis and discovery system: 3.4.22.59
            BRENDA, the Enzyme Database: 3.4.22.59
///
ENTRY       EC 3.4.22.60                Enzyme
NAME        caspase-7;
            CASP-7;
            ICE-like apoptotic protease 3;
            ICE-LAP3;
            apoptotic protease Mch-3;
            Mch3;
            CMH-1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Strict requirement for an Asp residue at position P1 and has a
            preferred cleavage sequence of Asp-Glu-Val-Asp!
COMMENT     Caspase-7 is an effector/executioner caspase, as are caspase-3 (EC
            3.4.22.56) and caspase-6 (EC 3.4.22.59) [1]. These caspases are
            responsible for the proteolysis of the majority of cellular
            polypeptides [e.g. poly(ADP-ribose) polymerase (PARP)], which leads
            to the apoptotic phenotype [2]. Although a hydrophobic residue at P5
            of caspase-2 (EC 3.4.22.55) and caspase-3 leads to more efficient
            hydrolysis, the amino-acid residue at this location in caspase-7 has
            no effect [3]. Caspase-7 is activated by the initiator caspases
            [caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10
            (EC 3.4.22.63)]. Removal of the N-terminal prodomain occurs before
            cleavage in the linker region between the large and small subunits
            [4]. Belongs in peptidase family C14.
REFERENCE   1  [PMID:11104820]
  AUTHORS   Chang HY, Yang X.
  TITLE     Proteases for cell suicide: functions and regulation of caspases.
  JOURNAL   Microbiol. Mol. Biol. Rev. 64 (2000) 821-46.
REFERENCE   2
  AUTHORS   Nicholson, D. and Thornberry, N.A.
  TITLE     Caspase-3 and caspase-7.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, 2nd ed., Elsevier, London, 2004, p.
            1298-1302.
REFERENCE   3  [PMID:16781734]
  AUTHORS   Fang B, Boross PI, Tozser J, Weber IT.
  TITLE     Structural and kinetic analysis of caspase-3 reveals role for s5
            binding site in substrate recognition.
  JOURNAL   J. Mol. Biol. 360 (2006) 654-66.
REFERENCE   4  [PMID:12824163]
  AUTHORS   Denault JB, Salvesen GS.
  TITLE     Human caspase-7 activity and regulation by its N-terminal peptide.
  JOURNAL   J. Biol. Chem. 278 (2003) 34042-50.
STRUCTURES  PDB: 2QL5  2QL7  2QL9  2QLB  2QLF  2QLJ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.60
            ExPASy - ENZYME nomenclature database: 3.4.22.60
            ExplorEnz - The Enzyme Database: 3.4.22.60
            ERGO genome analysis and discovery system: 3.4.22.60
            BRENDA, the Enzyme Database: 3.4.22.60
///
ENTRY       EC 3.4.22.61                Enzyme
NAME        caspase-8;
            FLICE, FADD-like ICE;
            MACH;
            MORT1-associated CED-3 homolog;
            Mch5;
            mammalian Ced-3 homolog 5;
            CASP-8;
            ICE-like apoptotic protease 5;
            FADD-homologous ICE/CED-3-like protease;
            apoptotic cysteine protease;
            apoptotic protease Mch-5;
            CAP4
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Strict requirement for Asp at position P1 and has a preferred
            cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp!(Gly/Ser/Ala)
COMMENT     Caspase-8 is an initiator caspase, as are caspase-2 (EC 3.4.22.55),
            caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63) [1].
            Caspase-8 is the apical activator of the extrinsic (death receptor)
            apoptosis pathway, triggered by death receptor ligation [2]. It
            contains two tandem death effector domains (DEDs) in its N-terminal
            prodomain, and these play a role in procaspase activation [1]. This
            enzyme is linked to cell surface death receptors such as Fas [1,5].
            When Fas is aggregated by the Fas ligand, procaspase-8 is recruited
            to the death receptor where it is activated [1]. The enzyme has a
            preference for Glu at P3 and prefers small residues, such as Gly,
            Ser and Ala, at the P1' position. It has very broad P4 specificity,
            tolerating substrates with Asp, Val or Leu in this position [2,3,4].
            Endogenous substrates for caspase-8 include procaspase-3, the
            pro-apoptotic Bcl-2 family member Bid, RIP, PAK2 and the caspase-8
            activity modulator FLIPL [4,5]. Belongs in peptidase family C14.
REFERENCE   1  [PMID:11104820]
  AUTHORS   Chang HY, Yang X.
  TITLE     Proteases for cell suicide: functions and regulation of caspases.
  JOURNAL   Microbiol. Mol. Biol. Rev. 64 (2000) 821-46.
REFERENCE   2  [PMID:8681376]
  AUTHORS   Boldin MP, Goncharov TM, Goltsev YV, Wallach D.
  TITLE     Involvement of MACH, a novel MORT1/FADD-interacting protease, in
            Fas/APO-1- and TNF receptor-induced cell death.
  JOURNAL   Cell. 85 (1996) 803-15.
REFERENCE   3  [PMID:8681377]
  AUTHORS   Muzio M, Chinnaiyan AM, Kischkel FC, O'Rourke K, Shevchenko A, Ni J,
            Scaffidi C, Bretz JD, Zhang M, Gentz R, Mann M, Krammer PH, Peter
            ME, Dixit VM.
  TITLE     FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited
            to the CD95 (Fas/APO-1) death--inducing signaling complex.
  JOURNAL   Cell. 85 (1996) 817-27.
REFERENCE   4
  AUTHORS   Salvesen, G.S. and Boatright, K.M.
  TITLE     Caspase-8.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, 2nd ed., Elsevier, London, 2004, p.
            1293-1296.
REFERENCE   5  [PMID:16186808]
  AUTHORS   Fischer U, Stroh C, Schulze-Osthoff K.
  TITLE     Unique and overlapping substrate specificities of caspase-8 and
            caspase-10.
  JOURNAL   Oncogene. 25 (2006) 152-9.
REFERENCE   6  [PMID:10964557]
  AUTHORS   Blanchard H, Donepudi M, Tschopp M, Kodandapani L, Wu JC, Grutter
            MG.
  TITLE     Caspase-8 specificity probed at subsite S(4): crystal structure of
            the caspase-8-Z-DEVD-cho complex.
  JOURNAL   J. Mol. Biol. 302 (2000) 9-16.
REFERENCE   7  [PMID:15209560]
  AUTHORS   Boatright KM, Deis C, Denault JB, Sutherlin DP, Salvesen GS.
  TITLE     Activation of caspases-8 and -10 by FLIP(L).
  JOURNAL   Biochem. J. 382 (2004) 651-7.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.61
            ExPASy - ENZYME nomenclature database: 3.4.22.61
            ExplorEnz - The Enzyme Database: 3.4.22.61
            ERGO genome analysis and discovery system: 3.4.22.61
            BRENDA, the Enzyme Database: 3.4.22.61
///
ENTRY       EC 3.4.22.62                Enzyme
NAME        caspase-9;
            CASP-9;
            ICE-like apoptotic protease 6;
            ICE-LAP6;
            apoptotic protease Mch-6;
            apoptotic protease-activating factor 3;
            APAF-3
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Strict requirement for an Asp residue at position P1 and with a
            marked preference for His at position P2. It has a preferred
            cleavage sequence of Leu-Gly-His-Asp!Xaa
COMMENT     Caspase-9 is an initiator caspase, as are caspase -2 (EC 3.4.22.55),
            caspase-8 (EC 3.4.22.61) and caspase-10 (EC 3.4.22.63) [1].
            Caspase-9 contains a caspase-recruitment domain (CARD) in its
            N-terminal prodomain, which plays a role in procaspase activation
            [1]. An alternatively spliced version of caspase-9 also exists,
            caspase-9S, that inhibits apoptosis, similar to the situation found
            with caspase-2 [1]. Phosphorylation of caspase-9 from some species
            by Akt, a serine-threonine protein kinase, inhibits caspase activity
            in vitro and caspase activation in vivo [1]. The activity of
            caspase-9 is increased dramatically upon association with the
            apoptosome but the enzyme can be activated without proteolytic
            cleavage [2,3]. Procaspase-3 is the enzyme's physiological substrate
            [2]. Belongs in peptidase family C14.
REFERENCE   1  [PMID:11104820]
  AUTHORS   Chang HY, Yang X.
  TITLE     Proteases for cell suicide: functions and regulation of caspases.
  JOURNAL   Microbiol. Mol. Biol. Rev. 64 (2000) 821-46.
REFERENCE   2  [PMID:16630893]
  AUTHORS   Yin Q, Park HH, Chung JY, Lin SC, Lo YC, da Graca LS, Jiang X, Wu H.
  TITLE     Caspase-9 holoenzyme is a specific and optimal procaspase-3
            processing machine.
  JOURNAL   Mol. Cell. 22 (2006) 259-68.
REFERENCE   3  [PMID:12620239]
  AUTHORS   Boatright KM, Renatus M, Scott FL, Sperandio S, Shin H, Pedersen IM,
            Ricci JE, Edris WA, Sutherlin DP, Green DR, Salvesen GS.
  TITLE     A unified model for apical caspase activation.
  JOURNAL   Mol. Cell. 11 (2003) 529-41.
REFERENCE   4
  AUTHORS   Salvesen, G.S. and Boatright, K.M.
  TITLE     Caspase-9.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, 2nd ed., Elsevier, London, 2004, p.
            1296-1298.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.62
            ExPASy - ENZYME nomenclature database: 3.4.22.62
            ExplorEnz - The Enzyme Database: 3.4.22.62
            ERGO genome analysis and discovery system: 3.4.22.62
            BRENDA, the Enzyme Database: 3.4.22.62
///
ENTRY       EC 3.4.22.63                Enzyme
NAME        caspase-10;
            FLICE2, Mch4;
            CASP-10;
            ICE-like apoptotic protease 4;
            apoptotic protease Mch-4;
            FAS-associated death domain protein interleukin-1beta-converting
            enzyme 2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Strict requirement for Asp at position P1 and has a preferred
            cleavage sequence of Leu-Gln-Thr-Asp!Gly
COMMENT     Caspase-10 is an initiator caspase, as are caspase-2 (EC 3.4.22.44),
            caspase-8 (EC 3.4.22.61) and caspase-9 (EC 3.4.22.62) [1]. Like
            caspase-8, caspase-10 contains two tandem death effector domains
            (DEDs) in its N-terminal prodomain, and these play a role in
            procaspase activation [1]. The enzyme has many overlapping
            substrates in common with caspase-8, such as RIP (the cleavage of
            which impairs NF-kappaB survival signalling and starts the
            cell-death process) and PAK2 (associated with some of the
            morphological features of apoptosis, such as cell rounding and
            apoptotic body formation) [2]. Bid, a Bcl2 protein, can be cleaved
            by caspase-3 (EC 3.4.22.56), caspase-8 and caspase-10 at
            Lys-Gln-Thr-Asp! to yield the pro-apoptotic p15 fragment. The p15
            fragment is N-myristoylated and enhances the release of cytochrome c
            from mitochondria (which, in turn, initiatiates the intrinsic
            apoptosis pathway). Bid can be further cleaved by caspase-10 and
            granzyme B but not by caspase-3 or caspase-8 at Ile-Glu-Thr-Asp! to
            yield a p13 fragment that is not N-myristoylated [2]. Belongs in
            peptidase family C14.
REFERENCE   1  [PMID:11104820]
  AUTHORS   Chang HY, Yang X.
  TITLE     Proteases for cell suicide: functions and regulation of caspases.
  JOURNAL   Microbiol. Mol. Biol. Rev. 64 (2000) 821-46.
REFERENCE   2  [PMID:16186808]
  AUTHORS   Fischer U, Stroh C, Schulze-Osthoff K.
  TITLE     Unique and overlapping substrate specificities of caspase-8 and
            caspase-10.
  JOURNAL   Oncogene. 25 (2006) 152-9.
REFERENCE   3  [PMID:12884866]
  AUTHORS   Shikama Y, Yamada M, Miyashita T.
  TITLE     Caspase-8 and caspase-10 activate NF-kappaB through RIP, NIK and
            IKKalpha kinases.
  JOURNAL   Eur. J. Immunol. 33 (2003) 1998-2006.
REFERENCE   4  [PMID:15209560]
  AUTHORS   Boatright KM, Deis C, Denault JB, Sutherlin DP, Salvesen GS.
  TITLE     Activation of caspases-8 and -10 by FLIP(L).
  JOURNAL   Biochem. J. 382 (2004) 651-7.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.63
            ExPASy - ENZYME nomenclature database: 3.4.22.63
            ExplorEnz - The Enzyme Database: 3.4.22.63
            ERGO genome analysis and discovery system: 3.4.22.63
            BRENDA, the Enzyme Database: 3.4.22.63
///
ENTRY       EC 3.4.22.64                Enzyme
NAME        caspase-11;
            CASP-11
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Strict requirement for Asp at the P1 position and has a preferred
            cleavage sequence of (Ile/Leu/Val/Phe)-Gly-His-Asp!
COMMENT     This murine enzyme is part of the family of inflammatory caspases,
            which also includes caspase-1 (EC 3.4.22.36), caspase-4 (EC
            3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-12,
            caspase-13 and caspase-14 in mice. Contains a caspase-recruitment
            domain (CARD) in its N-terminal prodomain, which plays a role in
            procaspase activation. Like caspase-5, but unlike caspase-4, this
            enzyme can be induced by lipopolysaccharide [1]. This enzyme not
            only activates caspase-1, which is required for the maturation of
            proinflammatory cytokines such as interleukin-1beta (IL-1beta) and
            IL-18, but it also activates caspase-3 (EC 3.4.22.56), which leads
            to cellular apoptosis under pathological conditions [1,2]. Belongs
            in peptidase family C14.
REFERENCE   1  [PMID:10791975]
  AUTHORS   Kang SJ, Wang S, Hara H, Peterson EP, Namura S, Amin-Hanjani S,
            Huang Z, Srinivasan A, Tomaselli KJ, Thornberry NA, Moskowitz MA,
            Yuan J.
  TITLE     Dual role of caspase-11 in mediating activation of caspase-1 and
            caspase-3 under pathological conditions.
  JOURNAL   J. Cell. Biol. 149 (2000) 613-22.
REFERENCE   2  [PMID:11684090]
  AUTHORS   Hur J, Kim SY, Kim H, Cha S, Lee MS, Suk K.
  TITLE     Induction of caspase-11 by inflammatory stimuli in rat astrocytes:
            lipopolysaccharide induction through p38 mitogen-activated protein
            kinase pathway.
  JOURNAL   FEBS. Lett. 507 (2001) 157-62.
REFERENCE   3  [PMID:9491891]
  AUTHORS   Wang S, Miura M, Jung YK, Zhu H, Li E, Yuan J.
  TITLE     Murine caspase-11, an ICE-interacting protease, is essential for the
            activation of ICE.
  JOURNAL   Cell. 92 (1998) 501-9.
REFERENCE   4  [PMID:16670335]
  AUTHORS   Endo M, Mori M, Akira S, Gotoh T.
  TITLE     C/EBP homologous protein (CHOP) is crucial for the induction of
            caspase-11 and the pathogenesis of lipopolysaccharide-induced
            inflammation.
  JOURNAL   J. Immunol. 176 (2006) 6245-53.
REFERENCE   5  [PMID:11104820]
  AUTHORS   Chang HY, Yang X.
  TITLE     Proteases for cell suicide: functions and regulation of caspases.
  JOURNAL   Microbiol. Mol. Biol. Rev. 64 (2000) 821-46.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.64
            ExPASy - ENZYME nomenclature database: 3.4.22.64
            ExplorEnz - The Enzyme Database: 3.4.22.64
            ERGO genome analysis and discovery system: 3.4.22.64
            BRENDA, the Enzyme Database: 3.4.22.64
///
ENTRY       EC 3.4.22.65                Enzyme
NAME        peptidase 1 (mite);
            allergen Der f 1;
            allergen Der p 1;
            antigen Der p 1;
            antigen Eur m 1;
            antigen Pso o 1;
            major mite fecal allergen Der p 1;
            Der p 1;
            Der f 1;
            Eur m 1;
            endopeptidase 1 (mite)
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Broad endopeptidase specificity
COMMENT     This enzyme, derived from the house dust mite, is a major component
            of the allergic immune response [2]. The substrate specificity of
            this enzyme is not altogether clear. It cleaves the low-affinity IgE
            receptor CD23 at Glu298!Ser299 and Ser155!Ser156 [1]. It also
            cleaves the pulmonary structural proteins occludin and claudin at
            Leu!Leu, Asp!Leu and at Gly!Thr bonds [1,2]. It can also cleave the
            alpha subunit of the interleukin-2 (IL-2) receptor (CD25) [4]. Using
            a positional scanning combinatorial library, it was found that the
            major substrate-specificity determinant is for Ala in the P2
            position [3]. The enzyme shows only a slight preference for basic
            amino acids in the P1 and P3 positions and a preference for
            aliphatic amino acids such as Ile, Pro, Val, Leu and norleucine in
            the P4 position [3]. Belongs in peptidase family C1A.
REFERENCE   1
  AUTHORS   Meighan, P. and Pirzad, R.
  TITLE     Mite endopeptidase 1.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, 2nd ed., Elsevier, London, 2004, p.
            1187-1189.
REFERENCE   2  [PMID:8660343]
  AUTHORS   Kalsheker NA, Deam S, Chambers L, Sreedharan S, Brocklehurst K,
            Lomas DA.
  TITLE     The house dust mite allergen Der p1 catalytically inactivates alpha
            1-antitrypsin by specific reactive centre loop cleavage: a mechanism
            that promotes airway inflammation and asthma.
  JOURNAL   Biochem. Biophys. Res. Commun. 221 (1996) 59-61.
REFERENCE   3  [PMID:15489163]
  AUTHORS   Harris J, Mason DE, Li J, Burdick KW, Backes BJ, Chen T, Shipway A,
            Van Heeke G, Gough L, Ghaemmaghami A, Shakib F, Debaene F,
            Winssinger N.
  TITLE     Activity profile of dust mite allergen extract using substrate
            libraries and functional proteomic microarrays.
  JOURNAL   Chem. Biol. 11 (2004) 1361-72.
REFERENCE   4  [PMID:9432986]
  AUTHORS   Schulz O, Sewell HF, Shakib F.
  TITLE     Proteolytic cleavage of CD25, the alpha subunit of the human T cell
            interleukin 2 receptor, by Der p 1, a major mite allergen with
            cysteine protease activity.
  JOURNAL   J. Exp. Med. 187 (1998) 271-5.
REFERENCE   5  [PMID:9893750]
  AUTHORS   Schulz O, Sewell HF, Shakib F.
  TITLE     A sensitive fluorescent assay for measuring the cysteine protease
            activity of Der p 1, a major allergen from the dust mite
            Dermatophagoides pteronyssinus.
  JOURNAL   Mol. Pathol. 51 (1998) 222-4.
REFERENCE   6  [PMID:15707969]
  AUTHORS   Takai T, Kato T, Sakata Y, Yasueda H, Izuhara K, Okumura K, Ogawa H.
  TITLE     Recombinant Der p 1 and Der f 1 exhibit cysteine protease activity
            but no serine protease activity.
  JOURNAL   Biochem. Biophys. Res. Commun. 328 (2005) 944-52.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.65
            ExPASy - ENZYME nomenclature database: 3.4.22.65
            ExplorEnz - The Enzyme Database: 3.4.22.65
            ERGO genome analysis and discovery system: 3.4.22.65
            BRENDA, the Enzyme Database: 3.4.22.65
///
ENTRY       EC 3.4.22.67                Enzyme
NAME        zingipain;
            ginger protease;
            GP-I;
            GP-II;
            ginger protease II (Zingiber officinale);
            zingibain
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Cysteine endopeptidases
REACTION    Preferential cleavage of peptides with a proline residue at the P2
            position
COMMENT     This enzyme is found in ginger (Zingiber officinale) rhizome and is
            a member of the papain family. GP-II contains two glycosylation
            sites. The enzyme is inhibited by some divalent metal ions, such as
            Hg2+, Cu2+, Cd2+ and Zn2+ [2]. Belongs in peptidase family C1.
REFERENCE   1  [PMID:10691991]
  AUTHORS   Choi KH, Laursen RA.
  TITLE     Amino-acid sequence and glycan structures of cysteine proteases with
            proline specificity from ginger rhizome Zingiber officinale.
  JOURNAL   Eur. J. Biochem. 267 (2000) 1516-26.
REFERENCE   2  [PMID:7873561]
  AUTHORS   Ohtsuki K, Taguchi K, Sato K, Kawabata M.
  TITLE     Purification of ginger proteases by DEAE-Sepharose and isoelectric
            focusing.
  JOURNAL   Biochim. Biophys. Acta. 1243 (1995) 181-4.
REFERENCE   3  [PMID:10512617]
  AUTHORS   Choi KH, Laursen RA, Allen KN.
  TITLE     The 2.1 A structure of a cysteine protease with proline specificity
            from ginger rhizome, Zingiber officinale.
  JOURNAL   Biochemistry. 38 (1999) 11624-33.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.22.67
            ExPASy - ENZYME nomenclature database: 3.4.22.67
            ExplorEnz - The Enzyme Database: 3.4.22.67
            ERGO genome analysis and discovery system: 3.4.22.67
            BRENDA, the Enzyme Database: 3.4.22.67
///
ENTRY       EC 3.4.23.1                 Enzyme
NAME        pepsin A;
            pepsin;
            lactated pepsin;
            pepsin fortior;
            fundus-pepsin;
            elixir lactate of pepsin;
            P I;
            lactated pepsin elixir;
            P II;
            pepsin R;
            pepsin D
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Preferential cleavage: hydrophobic, preferably aromatic, residues in
            P1 and P1' positions. Cleaves Phe1!Val, Gln4!His, Glu13!Ala,
            Ala14!Leu, Leu15!Tyr, Tyr16!Leu, Gly23!Phe, Phe24!Phe and Phe25!Tyr
            bonds in the B chain of insulin
INHIBITOR   Methyl 2-diazoacetamidohexonate [CPD:C01223]
COMMENT     The predominant endopeptidase in the gastric juice of vertebrates,
            formed from pepsinogen A by limited proteolysis. Human pepsin A
            occurs in five molecular forms. Pig pepsin D [1,2] is
            unphosphorylated pepsin A. Type example of peptidase family A1.
REFERENCE   1  [PMID:4167464]
  AUTHORS   Lee D, Ryle AP.
  TITLE     Pepsinogen D. A fourth proteolytic zymogen from pig gastric mucosa.
  JOURNAL   Biochem. J. 104 (1967) 735-41.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:4860638]
  AUTHORS   Lee D, Ryle AP.
  TITLE     Pepsin D. A minor component of commercial pepsin preparations.
  JOURNAL   Biochem. J. 104 (1967) 742-8.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:6795036]
  AUTHORS   Foltmann B.
  TITLE     Gastric proteinases--structure, function, evolution and mechanism of
            action.
  JOURNAL   Essays. Biochem. 17 (1981) 52-84.
REFERENCE   4  [PMID:3941737]
  AUTHORS   James MN, Sielecki AR.
  TITLE     Molecular structure of an aspartic proteinase zymogen, porcine
            pepsinogen, at 1.8 A resolution.
  JOURNAL   Nature. 319 (1986) 33-8.
  ORGANISM  pig [GN:ssc]
REFERENCE   5
  AUTHORS   Fruton, J.S.
  TITLE     Aspartyl proteinases.
  JOURNAL   In: Neuberger, A. and Brocklehurst, K. (Eds.), New Comprehensive
            Biochemistry: Hydrolytic Enzymes, vol. 16, Elsevier, Amsterdam,
            1987, p. 1-38.
REFERENCE   6  [PMID:3546346]
  AUTHORS   Tang J, Wong RN.
  TITLE     Evolution in the structure and function of aspartic proteases.
  JOURNAL   J. Cell. Biochem. 33 (1987) 53-63.
  ORGANISM  pig [GN:ssc], human [GN:hsa], monkey, cow [GN:bta]
REFERENCE   7  [PMID:3139029]
  AUTHORS   Pohl J, Dunn BM.
  TITLE     Secondary enzyme-substrate interactions: kinetic evidence for ionic
            interactions between substrate side chains and the pepsin active
            site.
  JOURNAL   Biochemistry. 27 (1988) 4827-34.
  ORGANISM  pig [GN:ssc]
ORTHOLOGY   KO: K06002  pepsin A
GENES       HSA: 5222(PGA5) 643834(PGA3) 643847(PGA4)
            MMU: 58803(Pga5)
            RNO: 60372(Pga5)
            CFA: 403711(PGA5) 483802(LOC483802)
            BTA: 414350(pga)
            SSC: 396892(LOC396892)
            GGA: 395691(PGA5)
            PFA: PF08_0108
            TAN: TA02750
            TPV: TP03_0306
            TET: TTHERM_00046380 TTHERM_00433600 TTHERM_00971740
                 TTHERM_01128620
STRUCTURES  PDB: 1AM5  1F34  1FLH  1PSA  1PSN  1PSO  1YX9  3PEP  4PEP  5PEP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.1
            ExPASy - ENZYME nomenclature database: 3.4.23.1
            ExplorEnz - The Enzyme Database: 3.4.23.1
            ERGO genome analysis and discovery system: 3.4.23.1
            BRENDA, the Enzyme Database: 3.4.23.1
            CAS: 9001-75-6
///
ENTRY       EC 3.4.23.2                 Enzyme
NAME        pepsin B;
            parapepsin I;
            pig gelatinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Degradation of gelatin; little activity on hemoglobin. Specificity
            on B chain of insulin more restricted than that of pepsin A; does
            not cleave at Phe1-Val, Gln4-His or Gly23-Phe
COMMENT     Formed from pig pepsinogen B. In peptidase family A1 (pepsin A
            family)
REFERENCE   1
  AUTHORS   Ryle, A.P.
  TITLE     The porcine pepsins and pepsinogens.
  JOURNAL   Methods Enzymol. 19 (1970) 316-336.
  ORGANISM  pig [GN:ssc]
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.2
            ExPASy - ENZYME nomenclature database: 3.4.23.2
            ExplorEnz - The Enzyme Database: 3.4.23.2
            ERGO genome analysis and discovery system: 3.4.23.2
            BRENDA, the Enzyme Database: 3.4.23.2
            CAS: 9025-48-3
///
ENTRY       EC 3.4.23.3                 Enzyme
NAME        gastricsin;
            pepsin C;
            pig parapepsin II;
            parapepsin II
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    More restricted specificity than pepsin A, but shows preferential
            cleavage at Tyr! bonds. High activity on hemoglobin
COMMENT     Formed from progastricsin, apparently in the gastric juice of most
            vertebrates. In addition to the fundus, progastricsin is also
            secreted in antrum and proximal duodenum. Seminal plasma contains a
            zymogen that is immunologically identical with progastricsin [6]. In
            peptidase family A1 (pepsin A family).
REFERENCE   1
  AUTHORS   Ryle, A.P.
  TITLE     The porcine pepsins and pepsinogens.
  JOURNAL   Methods Enzymol. 19 (1970) 316-336.
  ORGANISM  pig [GN:ssc]
REFERENCE   2
  AUTHORS   Tang, J.
  TITLE     Gastricsin and pepsin.
  JOURNAL   Methods Enzymol. 19 (1970) 406-421.
  ORGANISM  human [GN:hsa], pig [GN:ssc]
REFERENCE   3  [PMID:6795036]
  AUTHORS   Foltmann B.
  TITLE     Gastric proteinases--structure, function, evolution and mechanism of
            action.
  JOURNAL   Essays. Biochem. 17 (1981) 52-84.
REFERENCE   4  [PMID:6816595]
  AUTHORS   Foltmann B, Jensen AL.
  TITLE     Human progastricsin. Analysis of intermediates during activation
            into gastricsin and determination of the amino acid sequence of the
            propart.
  JOURNAL   Eur. J. Biochem. 128 (1982) 63-70.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:6800788]
  AUTHORS   Martin P, Trieu-Cuot P, Collin JC, Ribadeau Dumas B.
  TITLE     Purification and characterization of bovine gastricsin.
  JOURNAL   Eur. J. Biochem. 122 (1982) 31-9.
  ORGANISM  cow [GN:bta]
REFERENCE   6  [PMID:6432332]
  AUTHORS   Reid WA, Vongsorasak L, Svasti J, Valler MJ, Kay J.
  TITLE     Identification of the acid proteinase in human seminal fluid as a
            gastricsin originating in the prostate.
  JOURNAL   Cell. Tissue. Res. 236 (1984) 597-600.
  ORGANISM  human [GN:hsa]
REFERENCE   7  [PMID:3335549]
  AUTHORS   Hayano T, Sogawa K, Ichihara Y, Fujii-Kuriyama Y, Takahashi K.
  TITLE     Primary structure of human pepsinogen C gene.
  JOURNAL   J. Biol. Chem. 263 (1988) 1382-5.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01377  gastricsin
GENES       HSA: 5225(PGC)
            PTR: 462684(PGC)
            MMU: 109820(Pgc)
            RNO: 24864(Pgc)
            CFA: 403552(PGC) 611675(LOC611675)
            BTA: 514502(LOC514502)
            GGA: 395690(PGC)
            XTR: 594991(pgc)
            TET: TTHERM_01053070
STRUCTURES  PDB: 1AVF  1HTR  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.3
            ExPASy - ENZYME nomenclature database: 3.4.23.3
            ExplorEnz - The Enzyme Database: 3.4.23.3
            ERGO genome analysis and discovery system: 3.4.23.3
            BRENDA, the Enzyme Database: 3.4.23.3
            CAS: 9012-71-9
///
ENTRY       EC 3.4.23.4                 Enzyme
NAME        chymosin;
            rennin (but this should be avoided since it leads to confusion with
            renin)
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Broad specificity similar to that of pepsin A. Clots milk by
            cleavage of a single Ser-Phe105!Met-Ala bond in kappa-chain of
            casein
COMMENT     Neonatal gastric enzyme with high milk clotting and weak general
            proteolytic activity, formed from prochymosin. Found among mammals
            with postnatal uptake of immunoglobulins. In peptidase family
            A1(pepsin A family)
REFERENCE   1  [PMID:5330666]
  AUTHORS   Foltmann B.
  TITLE     A review on prorennin and rennin.
  JOURNAL   C. R. Trav. Lab. Carlsberg. 35 (1966) 143-231.
REFERENCE   2  [PMID:6283469]
  AUTHORS   Harris TJ, Lowe PA, Lyons A, Thomas PG, Eaton MA, Millican TA, Patel
            TP, Bose CC, Carey NH, Doel MT.
  TITLE     Molecular cloning and nucleotide sequence of cDNA coding for calf
            preprochymosin.
  JOURNAL   Nucleic. Acids. Res. 10 (1982) 2177-87.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:3128264]
  AUTHORS   Visser S, Slangen CJ, van Rooijen PJ.
  TITLE     Peptide substrates for chymosin (rennin). Interaction sites in
            kappa-casein-related sequences located outside the
            (103-108)-hexapeptide region that fits into the enzyme's active-site
            cleft.
  JOURNAL   Biochem. J. 244 (1987) 553-8.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K01378  chymosin
GENES       MMU: 229697(Gm131)
            CFA: 490112(LOC490112)
            BTA: 529879(CYM)
STRUCTURES  PDB: 1CMS  1CZI  2HB3  3CMS  4CMS  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.4
            ExPASy - ENZYME nomenclature database: 3.4.23.4
            ExplorEnz - The Enzyme Database: 3.4.23.4
            ERGO genome analysis and discovery system: 3.4.23.4
            BRENDA, the Enzyme Database: 3.4.23.4
            CAS: 9001-98-3
///
ENTRY       EC 3.4.23.5                 Enzyme
NAME        cathepsin D
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Specificity similar to, but narrower than, that of pepsin A. Does
            not cleave the Gln4-His bond in B chain of insulin
INHIBITOR   Methyl 2-diazoacetamidohexonate [CPD:C01223]
COMMENT     Occurs intracellularly, in lysosomes. A zymogen form is known [4].
            In peptidase family A1 (pepsin A family).
REFERENCE   1
  AUTHORS   Barrett, A.J.
  TITLE     Cathepsin D and other carboxyl proteinases.
  JOURNAL   In: Barrett, A.J. (Ed.), Proteinases in Mammalian Cells and Tissues,
            North-Holland Publishing Co., Amsterdam, 1977, p. 209-248.
REFERENCE   2  [PMID:7341918]
  AUTHORS   Takahashi T, Tang J.
  TITLE     Cathepsin D from porcine and bovine spleen.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 565-81.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:3927292]
  AUTHORS   Faust PL, Kornfeld S, Chirgwin JM.
  TITLE     Cloning and sequence analysis of cDNA for human cathepsin D.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 4910-4.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:2512908]
  AUTHORS   Conner GE.
  TITLE     Isolation of procathepsin D from mature cathepsin D by pepstatin
            affinity chromatography. Autocatalytic proteolysis of the zymogen
            form of the enzyme.
  JOURNAL   Biochem. J. 263 (1989) 601-4.
  ORGANISM  cow [GN:bta], pig [GN:ssc]
ORTHOLOGY   KO: K01379  cathepsin D
GENES       HSA: 1509(CTSD)
            MMU: 13033(Ctsd)
            RNO: 171293(Ctsd)
            CFA: 483662(CTSD)
            BTA: 282883(CTSD)
            SSC: 494568(CTSD)
            GGA: 396090(CTSD)
            XLA: 443721(LOC443721) 443829(MGC82347)
            XTR: 394561(ctsd)
            DRE: 65225(ctsd)
            DME: Dmel_CG1548
            CME: CMN194C
            AFM: AFUA_4G07040
            DDI: DDB_0215012(ctsD)
            TET: TTHERM_00037350 TTHERM_00052190 TTHERM_00082230
                 TTHERM_00112980 TTHERM_00112990 TTHERM_00128320
                 TTHERM_00321680
STRUCTURES  PDB: 1LYA  1LYB  1LYW  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.5
            ExPASy - ENZYME nomenclature database: 3.4.23.5
            ExplorEnz - The Enzyme Database: 3.4.23.5
            ERGO genome analysis and discovery system: 3.4.23.5
            BRENDA, the Enzyme Database: 3.4.23.5
            CAS: 9025-26-7
///
ENTRY       EC 3.4.23.6       Obsolete  Enzyme
NAME        Transferred to 3.4.23.30
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
COMMENT     Transferred entry: now EC 3.4.23.30 pycnoporopepsin (EC 3.4.23.6
            created 1961 as EC 3.4.4.17, transferred 1972 to EC 3.4.23.6,
            modified 1981, deleted 1992 [EC 3.4.23.7, EC 3.4.23.8, EC 3.4.23.9,
            EC 3.4.23.10, EC 3.4.99.1, EC 3.4.99.15 and EC 3.4.99.25 all created
            1972 and incorporated 1978])
STRUCTURES  PDB: 1ER8  1UH7  1UH8  1UH9  2APR  2ER0  2ER6  2ER7  2ER9  3APR  
                 3ER3  3ER5  4APR  4ER1  4ER2  4ER4  5APR  5ER1  5ER2  6APR  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.6
            ExPASy - ENZYME nomenclature database: 3.4.23.6
            ExplorEnz - The Enzyme Database: 3.4.23.6
            ERGO genome analysis and discovery system: 3.4.23.6
            BRENDA, the Enzyme Database: 3.4.23.6
///
ENTRY       EC 3.4.23.7       Obsolete  Enzyme
NAME        Transferred to 3.4.23.20
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
COMMENT     Transferred entry: now EC 3.4.23.20 penicillopepsin (EC 3.4.23.7
            created 1972, modified 1981, deleted 1978 [transferred to EC
            3.4.23.6, deleted 1992])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.7
            ExPASy - ENZYME nomenclature database: 3.4.23.7
            ExplorEnz - The Enzyme Database: 3.4.23.7
            ERGO genome analysis and discovery system: 3.4.23.7
            BRENDA, the Enzyme Database: 3.4.23.7
///
ENTRY       EC 3.4.23.8       Obsolete  Enzyme
NAME        Transferred to 3.4.23.25
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
COMMENT     Transferred entry: now EC 3.4.23.25 saccharopepsin (EC 3.4.23.8
            created 1972, modified 1981, deleted 1978 [transferred to EC
            3.4.23.6, deleted 1992])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.8
            ExPASy - ENZYME nomenclature database: 3.4.23.8
            ExplorEnz - The Enzyme Database: 3.4.23.8
            ERGO genome analysis and discovery system: 3.4.23.8
            BRENDA, the Enzyme Database: 3.4.23.8
///
ENTRY       EC 3.4.23.9       Obsolete  Enzyme
NAME        Transferred to 3.4.23.21
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
COMMENT     Transferred entry: now EC 3.4.23.21 rhizopuspepsin (EC 3.4.23.9
            created 1972, modified 1981, deleted 1978 [transferred to EC
            3.4.23.6, deleted 1992])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.9
            ExPASy - ENZYME nomenclature database: 3.4.23.9
            ExplorEnz - The Enzyme Database: 3.4.23.9
            ERGO genome analysis and discovery system: 3.4.23.9
            BRENDA, the Enzyme Database: 3.4.23.9
///
ENTRY       EC 3.4.23.10      Obsolete  Enzyme
NAME        Transferred to 3.4.23.22
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
COMMENT     Transferred entry: now EC 3.4.23.22 endothiapepsin (EC 3.4.23.10
            created 1972, modified 1981, deleted 1978 [transferred to EC
            3.4.23.6, deleted 1992])
STRUCTURES  PDB: 4APE  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.10
            ExPASy - ENZYME nomenclature database: 3.4.23.10
            ExplorEnz - The Enzyme Database: 3.4.23.10
            ERGO genome analysis and discovery system: 3.4.23.10
            BRENDA, the Enzyme Database: 3.4.23.10
///
ENTRY       EC 3.4.23.11      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
COMMENT     Deleted entry: thyroid aspartic proteinase (EC 3.4.23.11 created
            1978, modified 1981, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.11
            ExPASy - ENZYME nomenclature database: 3.4.23.11
            ExplorEnz - The Enzyme Database: 3.4.23.11
            ERGO genome analysis and discovery system: 3.4.23.11
            BRENDA, the Enzyme Database: 3.4.23.11
///
ENTRY       EC 3.4.23.12                Enzyme
NAME        nepenthesin;
            Nepenthes aspartic proteinase;
            Nepenthes acid proteinase;
            nepenthacin;
            nepenthasin;
            aspartyl endopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Similar to pepsin, but also cleaves on either side of Asp and at
            Lys!Arg
COMMENT     From the insectivorous plants Nepenthes spp. (secretions) and
            Drosera peltata (ground-up leaves). Aspartic endopeptidases are
            probably present in many other plants, including Lotus [3] and
            sorghum [2]. In peptidase family A1 (pepsin A family)
REFERENCE   1  [PMID:5354017]
  AUTHORS   Amagase S, Nakayama S, Tsugita A.
  TITLE     Acid protease in Nepenthes. II. Study on the specificity of
            nepenthesin.
  JOURNAL   J. Biochem. (Tokyo). 66 (1969) 431-9.
  ORGANISM  Nepenthes sp.
REFERENCE   2  [PMID:5486576]
  AUTHORS   Garg GK, Virupaksha TK.
  TITLE     Acid protease from germinated sorghum. 2. Substrate specificity with
            synthetic peptides and ribonuclease A.
  JOURNAL   Eur. J. Biochem. 17 (1970) 13-8.
REFERENCE   3
  AUTHORS   Shinano, S. and Fukushima, K.
  TITLE     Studies on lotus seed protease. Part III. Some physicochemical and
            enzymic properties.
  JOURNAL   Agric. Biol. Chem. 35 (1971) 1488-1494.
  ORGANISM  Nepenthes sp.
REFERENCE   4  [PMID:5069751]
  AUTHORS   Amagase S.
  TITLE     Digestive enzymes in insectivorous plants. 3. Acid proteases in the
            genus Nepenthes and Drosera peltata.
  JOURNAL   J. Biochem. (Tokyo). 72 (1972) 73-81.
  ORGANISM  Nepenthes sp., Drosera peltata
REFERENCE   5  [PMID:4436292]
  AUTHORS   Takahashi K, Chang W, Ko J.
  TITLE     Specific inhibition of acid proteases from brain, kidney, skeletal
            muscle, and insectivorous plants by diazoacetyl-DL-norleucine methyl
            ester and by pepstatin.
  JOURNAL   J. Biochem. (Tokyo). 76 (1974) 897-9.
  ORGANISM  Nepenthes macferlanei
REFERENCE   6  [PMID:16526095]
  AUTHORS   Coiras M, Camafeita E, Urena T, Lopez JA, Caballero F, Fernandez B,
            Lopez-Huertas MR, Perez-Olmeda M, Alcami J.
  TITLE     Modifications in the human T cell proteome induced by intracellular
            HIV-1 Tat protein expression.
  JOURNAL   Proteomics. 6 Suppl 1 (2006) S63-73.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.12
            ExPASy - ENZYME nomenclature database: 3.4.23.12
            ExplorEnz - The Enzyme Database: 3.4.23.12
            ERGO genome analysis and discovery system: 3.4.23.12
            BRENDA, the Enzyme Database: 3.4.23.12
            CAS: 9073-80-7
///
ENTRY       EC 3.4.23.13      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
COMMENT     Deleted entry: Lotus aspartic proteinase (EC 3.4.23.13 created 1978,
            modified 1981, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.13
            ExPASy - ENZYME nomenclature database: 3.4.23.13
            ExplorEnz - The Enzyme Database: 3.4.23.13
            ERGO genome analysis and discovery system: 3.4.23.13
            BRENDA, the Enzyme Database: 3.4.23.13
///
ENTRY       EC 3.4.23.14      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
COMMENT     Deleted entry: sorghum aspartic proteinase (EC 3.4.23.14 created
            1978, modified 1981, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.14
            ExPASy - ENZYME nomenclature database: 3.4.23.14
            ExplorEnz - The Enzyme Database: 3.4.23.14
            ERGO genome analysis and discovery system: 3.4.23.14
            BRENDA, the Enzyme Database: 3.4.23.14
///
ENTRY       EC 3.4.23.15                Enzyme
NAME        renin;
            angiotensin-forming enzyme;
            angiotensinogenase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Cleavage of Leu! bond in angiotensinogen to generate angiotensin I
COMMENT     Formed from prorenin in plasma and kidney. In peptidase family A1
            (pepsin A family).
REFERENCE   1  [PMID:16012]
  AUTHORS   Inagami T, Murakami K.
  TITLE     Pure Renin. Isolation from hog kidney and characterization.
  JOURNAL   J. Biol. Chem. 252 (1977) 2978-83.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:7043197]
  AUTHORS   Slater EE.
  TITLE     Renin.
  JOURNAL   Methods. Enzymol. 80 Pt C (1981) 427-42.
REFERENCE   3  [PMID:2785652]
  AUTHORS   Sussman S, Holt L, Dent CW, Flay BR, Graham JW, Hansen WB, Johnson
            CA.
  TITLE     Activity involvement, risk-taking, demographic variables, and other
            drug use: prediction of trying smokeless tobacco.
  JOURNAL   NCI. Monogr.  (1989) 57-62.
REFERENCE   4  [PMID:2493678]
  AUTHORS   Sielecki AR, Hayakawa K, Fujinaga M, Murphy ME, Fraser M, Muir AK,
            Carilli CT, Lewicki JA, Baxter JD, James MN.
  TITLE     Structure of recombinant human renin, a target for
            cardiovascular-active drugs, at 2.5 A resolution.
  JOURNAL   Science. 243 (1989) 1346-51.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04614  Renin-angiotensin system
ORTHOLOGY   KO: K01380  renin
GENES       HSA: 5972(REN)
            PTR: 469651(REN)
            MMU: 19701(Ren1) 19702(Ren2)
            RNO: 24715(Ren1)
            CFA: 403838(REN)
            BTA: 511831(LOC511831)
            DRE: 405786(ren)
STRUCTURES  PDB: 1BBS  1RNE  1SMR  2BKS  2BKT  2FS4  2G1N  2G1O  2G1R  2G1S  
                 2G1Y  2G20  2G21  2G22  2G24  2G26  2G27  2I4Q  2IKO  2IKU  
                 2IL2  2REN  2V0Z  2V10  2V11  2V12  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.15
            ExPASy - ENZYME nomenclature database: 3.4.23.15
            ExplorEnz - The Enzyme Database: 3.4.23.15
            ERGO genome analysis and discovery system: 3.4.23.15
            BRENDA, the Enzyme Database: 3.4.23.15
            CAS: 9015-94-5
///
ENTRY       EC 3.4.23.16                Enzyme
NAME        HIV-1 retropepsin;
            human immunodeficiency virus type 1 protease;
            gag protease;
            HIV aspartyl protease;
            HIV proteinase;
            retroproteinase;
            HIV-1 protease;
            HIV-2 protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Specific for a P1 residue that is hydrophobic, and P1' variable, but
            often Pro
COMMENT     Present in human immunodeficiency virus type 1. Contributes to the
            maturation of the viral particle, and is a target of antiviral
            drugs. Active enzyme is a dimer of identical 11-kDa subunits.
            Similar enzymes occur in other retroviruses [1]. Type example of
            peptidase family A2
REFERENCE   1
  AUTHORS   Kuo, L.C. and Shafer, J.A.
  TITLE     (eds) Retroviral Proteases.
  JOURNAL   Methods Enzymol. 241 (1994) 1-431.
  ORGANISM  human [GN:hsa]
REFERENCE   2
  AUTHORS   Dunn, B.M.
  TITLE     Human immunodeficiency virus 1 retropepsin.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Academic Press, London, 1998, p.
            919-928.
ORTHOLOGY   KO: K06003  
STRUCTURES  PDB: 1A30  1A8G  1A8K  1A94  1AID  1AJV  1AJX  1AXA  1AZ5  1B11  
                 1B6J  1B6K  1B6L  1B6M  1B6P  1BDL  1BDQ  1BDR  1BV7  1BV9  
                 1BVE  1BVG  1BWA  1BWB  1D4H  1D4I  1D4J  1D4K  1D4L  1D4S  
                 1D4Y  1DAZ  1DMP  1DW6  1EBK  1EBW  1EBY  1EBZ  1EC0  1EC1  
                 1EC2  1EC3  1F7A  1FEJ  1FF0  1FFF  1FFI  1FG6  1FG8  1FGC  
                 1FIV  1FMB  1FQX  1G2K  1G35  1G6L  1HPO  1HVH  1HWR  1HXB  
                 1HXW  1IIQ  1IZH  1IZI  1JLD  1K1T  1K1U  1K2B  1K2C  1K6C  
                 1K6P  1K6T  1K6V  1KJ4  1KJ7  1KJF  1KJG  1KJH  1KZK  1LV1  
                 1LZQ  1M0B  1MER  1MES  1MET  1MEU  1MRW  1MRX  1MSM  1MSN  
                 1MT7  1MT8  1MT9  1MTB  1MTR  1MUI  1N49  1NH0  1NPA  1NPV  
                 1NPW  1ODW  1ODX  1ODY  1PRO  1Q94  1Q9P  1QBR  1QBS  1QBT  
                 1QBU  1RL8  1RPI  1RQ9  1RV7  1SDT  1SDU  1SDV  1SGU  1SH9  
                 1SP5  1T3R  1T7I  1T7J  1T7K  1TCW  1TCX  1TSQ  1TSU  1TW7  
                 1U8G  1VIJ  1VIK  1W5V  1W5W  1W5X  1W5Y  1XL2  1XL5  1YTG  
                 1YTH  1YTI  1YTJ  1Z1H  1Z1R  1Z8C  1ZBG  1ZJ7  1ZLF  1ZP8  
                 1ZPA  1ZPK  1ZSF  1ZSR  1ZTZ  2A1E  2A4F  2AID  2AOC  2AOD  
                 2AOE  2AOF  2AOG  2AOH  2AOI  2AOJ  2AQU  2AVM  2AVO  2AVQ  
                 2AVS  2AVV  2AZ8  2AZ9  2AZB  2AZC  2BB9  2BBB  2BQV  2CEJ  
                 2CEM  2CEN  2F3K  2F80  2F81  2F8G  2FDD  2FDE  2FGU  2FGV  
                 2FIV  2FMB  2FNS  2FNT  2FXD  2FXE  2G69  2HAH  2HB2  2HB4  
                 2HC0  2HS1  2HS2  2I4D  2I4U  2I4V  2I4W  2I4X  2IDW  2IEN  
                 2IEO  2JO0  2NMW  2NMY  2NMZ  2NNK  2NNP  2NPH  2NXD  2NXL  
                 2NXM  2O40  2P3A  2P3B  2P3C  2P3D  2PC0  2UPJ  3AID  3FIV  
                 3TLH  3UPJ  4FIV  4UPJ  5FIV  5UPJ  6FIV  6UPJ  7UPJ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.16
            ExPASy - ENZYME nomenclature database: 3.4.23.16
            ExplorEnz - The Enzyme Database: 3.4.23.16
            ERGO genome analysis and discovery system: 3.4.23.16
            BRENDA, the Enzyme Database: 3.4.23.16
            CAS: 144114-21-6
///
ENTRY       EC 3.4.23.17                Enzyme
NAME        pro-opiomelanocortin converting enzyme;
            prohormone converting enzyme;
            pro-opiomelanocortin-converting enzyme;
            proopiomelanocortin proteinase;
            PCE
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Cleavage at paired basic residues in certain prohormones, either
            between them, or on the carboxyl side
COMMENT     A 70 kDa membrane-bound enzyme isolated from cattle pituitary
            secretory vesicle.
REFERENCE   1  [PMID:2987247]
  AUTHORS   Loh YP, Parish DC, Tuteja R.
  TITLE     Purification and characterization of a paired basic residue-specific
            pro-opiomelanocortin converting enzyme from bovine pituitary
            intermediate lobe secretory vesicles.
  JOURNAL   J. Biol. Chem. 260 (1985) 7194-205.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:3017955]
  AUTHORS   Loh YP.
  TITLE     Kinetic studies on the processing of human beta-lipotropin by bovine
            pituitary intermediate lobe pro-opiomelanocortin-converting enzyme.
  JOURNAL   J. Biol. Chem. 261 (1986) 11949-55.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:2553692]
  AUTHORS   Estivariz FE, Birch NP, Loh YP.
  TITLE     Generation of Lys-gamma 3-melanotropin from pro-opiomelanocortin
            1-77 by a bovine intermediate lobe secretory vesicle
            membrane-associated aspartic protease and purified
            pro-opiomelanocortin converting enzyme.
  JOURNAL   J. Biol. Chem. 264 (1989) 17796-801.
  ORGANISM  cow [GN:bta]
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.17
            ExPASy - ENZYME nomenclature database: 3.4.23.17
            ExplorEnz - The Enzyme Database: 3.4.23.17
            ERGO genome analysis and discovery system: 3.4.23.17
            BRENDA, the Enzyme Database: 3.4.23.17
            CAS: 80891-34-5
///
ENTRY       EC 3.4.23.18                Enzyme
NAME        aspergillopepsin I;
            Aspergillus acid protease;
            Aspergillus acid proteinase;
            Aspergillus aspartic proteinase;
            Aspergillus awamori acid proteinase;
            Aspergillus carboxyl proteinase;
            (see also Comments);
            carboxyl proteinase;
            Aspergillus kawachii aspartic proteinase;
            Aspergillus saitoi acid proteinase;
            pepsin-type aspartic proteinase;
            Aspergillus niger acid proteinase;
            sumizyme AP;
            proctase P;
            denapsin;
            denapsin XP 271;
            proctase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Hydrolysis of proteins with broad specificity. Generally favours
            hydrophobic residues in P1 and P1', but also accepts Lys in P1,
            which leads to activation of trypsinogen. Does not clot milk
COMMENT     Found in a variety of Aspergillus species (imperfect fungi):
            Aspergillus awamori (awamorin, aspergillopepsin A: [8]), A. foetidus
            (aspergillopepsin F: [6]), A. fumigatus [7], A. kawachii [9], A.
            niger (proteinase B, proctase B: [2,4]), A. oryzae (trypsinogen
            kinase: [3,10]), A. saitoi (aspergillopeptidase A: [10]), and A.
            sojae [5,10]. In peptidase family A1 (pepsin A family). Formerly
            included in EC 3.4.23.6
REFERENCE   1  [PMID:4565799]
  AUTHORS   Kovaleva GG, Shimanskaya MP, Stepanov VM.
  TITLE     The site of diazoacetyl inhibitor attachment to acid proteinase of
            Aspergillus awamori--an analog of penicillopepsin and pepsin.
  JOURNAL   Biochem. Biophys. Res. Commun. 49 (1972) 1075-81.
  ORGANISM  Aspergillus awamori
REFERENCE   2  [PMID:4593189]
  AUTHORS   Morihara K, Oka T.
  TITLE     Comparative specificity of microbial acid proteinases for synthetic
            peptides. 3. Relationship with their trypsinogen activating ability.
  JOURNAL   Arch. Biochem. Biophys. 157 (1973) 561-72.
REFERENCE   3  [PMID:239702]
  AUTHORS   Davidson R, Gertler A, Hofmann T.
  TITLE     Aspergillus oryzae acid proteinase. Purification and properties, and
            formation of pi-chymotrypsin.
  JOURNAL   Biochem. J. 147 (1975) 45-53.
  ORGANISM  Aspergillus oryzae [GN:aor]
REFERENCE   4  [PMID:12156]
  AUTHORS   Chang WJ, Horiuchi S, Takahashi K, Yamasaki M, Yamada Y.
  TITLE     The structure and function of acid proteases. VI. Effects of acid
            protease-specific inhibitors on the acid proteases from Aspergillus
            niger var. macrosporus.
  JOURNAL   J. Biochem. (Tokyo). 80 (1976) 975-81.
  ORGANISM  Aspergillus niger
REFERENCE   5  [PMID:21699]
  AUTHORS   Tanaka N, Takeuchi M, Ichishima E.
  TITLE     Purification of an acid proteinase from Aspergillus saitoi and
            determination of peptide bond specificity.
  JOURNAL   Biochim. Biophys. Acta. 485 (1977) 406-16.
  ORGANISM  Aspergillus saitoi
REFERENCE   6
  AUTHORS   Ostoslavskaya, V.I., Kotlova, E.K., Stepanov, V.M., Rudenskaya,
            G.H., Baratova, L.A. and Belyanova, L.P.
  TITLE     Aspergillopepsin F-A carboxylic proteinase from Aspergillus
            foetidus.
  JOURNAL   Bioorg. Khim. 5 (1976) 595-603.
  ORGANISM  Aspergillus foetidus
REFERENCE   7  [PMID:7024192]
  AUTHORS   Panneerselvam M, Dhar SC.
  TITLE     Studies on the peptide bond specificity and the essential groups of
            an acid proteinase from Aspergillus fumigatus.
  JOURNAL   Ital. J. Biochem. 30 (1981) 207-16.
  ORGANISM  Aspergillus foetidus
REFERENCE   8
  AUTHORS   Ostoslavskaya, V.I., Revina, L.P., Kotlova, E.K., Surova, I.A.,
            Levin, E.D., Timokhima, E.A. and Stepanov, V.M.
  TITLE     The primary structure of aspergillopepsin A, aspartic proteinase
            from Aspergillus awamori. IV. Amino acid sequence of the enzyme.
  JOURNAL   Bioorg. Khim. 12 (1986) 1030-1047.
REFERENCE   9
  AUTHORS   Yagi, F., Fan, J., Tadera, K. and Kobayashi, A.
  TITLE     Purification and characterization of carboxyl proteinase from
            Aspergillus kawachii.
  JOURNAL   Agric. Biol. Chem. 50 (1986) 1029-1033.
  ORGANISM  Aspergillus kawachii
REFERENCE   10
  AUTHORS   Majima, E., Oda, K., Murao, S. and Ichishima, E.
  TITLE     Comparative study on the specificities of several fungal aspartic
            and acidic proteinases towards the tetradecapeptide of a renin
            substrate.
  JOURNAL   Agric. Biol. Chem. 52 (1988) 787-793.
ORTHOLOGY   KO: K06004  aspergillopepsin I
GENES       ANI: AN6888.2
            AFM: AFUA_2G15950 AFUA_3G01220 AFUA_5G13300
            AOR: AO090120000474
            ANG: An14g04710(pepA)
STRUCTURES  PDB: 1IBQ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.18
            ExPASy - ENZYME nomenclature database: 3.4.23.18
            ExplorEnz - The Enzyme Database: 3.4.23.18
            ERGO genome analysis and discovery system: 3.4.23.18
            BRENDA, the Enzyme Database: 3.4.23.18
            CAS: 9025-49-4
///
ENTRY       EC 3.4.23.19                Enzyme
NAME        aspergillopepsin II;
            proteinase A;
            proctase A;
            Aspergillus niger var. macrosporus aspartic proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Preferential cleavage in B chain of insulin: Asn3!Gln, Gly13!Ala,
            Tyr26!Thr
COMMENT     Isolated from Aspergillus niger var. macrosporus, distinct from
            proteinase B (see aspergillopepsin I) in specificity and
            insensitivity to pepstatin. In peptidase family A4 (scytalidopepsin
            B family). Formerly included in EC 3.4.23.6
REFERENCE   1  [PMID:12156]
  AUTHORS   Chang WJ, Horiuchi S, Takahashi K, Yamasaki M, Yamada Y.
  TITLE     The structure and function of acid proteases. VI. Effects of acid
            protease-specific inhibitors on the acid proteases from Aspergillus
            niger var. macrosporus.
  JOURNAL   J. Biochem. (Tokyo). 80 (1976) 975-81.
  ORGANISM  Aspergillus niger
REFERENCE   2  [PMID:1268233]
  AUTHORS   Iio K, Yamasaki M.
  TITLE     Specificity of acid proteinase A from Aspergillus niger var.
            macrosporus towards B-chain of performic acid oxidized bovine
            insulin.
  JOURNAL   Biochim. Biophys. Acta. 429 (1976) 912-24.
  ORGANISM  Aspergillus niger
GENES       ANG: An01g00530(proctase-A)
STRUCTURES  PDB: 1Y43  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.19
            ExPASy - ENZYME nomenclature database: 3.4.23.19
            ExplorEnz - The Enzyme Database: 3.4.23.19
            ERGO genome analysis and discovery system: 3.4.23.19
            BRENDA, the Enzyme Database: 3.4.23.19
            CAS: 9025-49-4
///
ENTRY       EC 3.4.23.20                Enzyme
NAME        penicillopepsin;
            peptidase A;
            Penicillium janthinellum aspartic proteinase;
            acid protease A;
            Penicillium citrinum acid proteinase;
            Penicillium cyclopium acid proteinase;
            Penicillium expansum acid proteinase;
            Penicillium janthinellum acid proteinase;
            Penicillium expansum aspartic proteinase;
            Penicillium aspartic proteinase;
            Penicillium caseicolum aspartic proteinase;
            Penicillium roqueforti acid proteinase;
            Penicillium duponti aspartic proteinase;
            Penicillium citrinum aspartic proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Hydrolysis of proteins with broad specificity similar to that of
            pepsin A, preferring hydrophobic residues at P1 and P1', but also
            cleaving Gly20!Glu in the B chain of insulin. Clots milk, and
            activates trypsinogen
COMMENT     From the imperfect fungus Penicillium janthinellum. In peptidase
            family A1 (pepsin A family). Closely related enzymes have been
            isolated from P. roqueforti [2] and P. duponti [3].
REFERENCE   1  [PMID:4946839]
  AUTHORS   Mains G, Takahashi M, Sodek J, Hofmann T.
  TITLE     The specificity of penicillopepsin.
  JOURNAL   Can. J. Biochem. 49 (1971) 1134-49.
REFERENCE   2  [PMID:4790849]
  AUTHORS   Zevaco C, Hermier J, Gripon JC.
  TITLE     [Proteolytic system in Penicillium roqueforti. 2. Purification and
            properties of acid protease]
  JOURNAL   Biochimie. 55 (1973) 1353-60.
  ORGANISM  Penicillium roqueforti
REFERENCE   3  [PMID:2287]
  AUTHORS   Emi S, Myers DV, Iacobucci GA.
  TITLE     Purification and properties of the thermostable acid protease of
            Penicillium duponti.
  JOURNAL   Biochemistry. 15 (1976) 842-8.
  ORGANISM  Penicillium duponti
REFERENCE   4  [PMID:1012008]
  AUTHORS   Hofmann T.
  TITLE     Penicillopepsin.
  JOURNAL   Methods. Enzymol. 45 (1976) 434-52.
REFERENCE   5  [PMID:323722]
  AUTHORS   Hsu IN, Delbaere LT, James MN, Hofmann T.
  TITLE     Penicillopepsin from Penicillium janthinellum crystal structure at
            2.8 A and sequence homology with porcine pepsin.
  JOURNAL   Nature. 266 (1977) 140-5.
  ORGANISM  Penicillium janthinellum
STRUCTURES  PDB: 1APT  1APU  1APV  1APW  1BXO  1BXQ  1PPK  1PPL  1PPM  2WEA  
                 2WEB  2WEC  2WED  3APP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.20
            ExPASy - ENZYME nomenclature database: 3.4.23.20
            ExplorEnz - The Enzyme Database: 3.4.23.20
            ERGO genome analysis and discovery system: 3.4.23.20
            BRENDA, the Enzyme Database: 3.4.23.20
            CAS: 9074-08-2
///
ENTRY       EC 3.4.23.21                Enzyme
NAME        rhizopuspepsin;
            Rhizopus aspartic proteinase;
            neurase;
            Rhizopus acid protease;
            Rhizopus acid proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Hydrolysis of proteins with broad specificity similar to that of
            pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk
            and activates trypsinogen. Does not cleave Gln4-His, but does cleave
            His10!Leu and Val12!Glu in B chain of insulin
COMMENT     From the zygomycete fungus Rhizopus chinensis. A similar
            endopeptidase is found in R. niveus [2]. In peptidase family A1
            (pepsin A family).
REFERENCE   1
  AUTHORS   Tsuru, D., Hattori, A., Tsuji, H., Yamamoto, T. and Fukumoto, J.
  TITLE     Studies on mold proteases. Part II. Substrate specificity of acid
            protease of Rhizopus chinensis.
  JOURNAL   Agric. Biol. Chem. 33 (1969) 1419-1426.
  ORGANISM  Rhizopus chinensis
REFERENCE   2
  AUTHORS   Kurono, Y., Chidimatsu, M., Horikoshi, K. and Ikeda, Y.
  TITLE     Isolation of a protease from a Rhizopus product.
  JOURNAL   Agric. Biol. Chem. 35 (1971) 1668-1675.
  ORGANISM  Rhizopus sp.
REFERENCE   3  [PMID:6751894]
  AUTHORS   Ohtsuru M, Tang J, Delaney R.
  TITLE     Purification and characterization of rhizopuspepsin isozymes from a
            liquid culture of Rhizopus chinensis.
  JOURNAL   Int. J. Biochem. 14 (1982) 925-32.
  ORGANISM  Rhizopus chinensis
REFERENCE   4  [PMID:3313384]
  AUTHORS   Suguna K, Padlan EA, Smith CW, Carlson WD, Davies DR.
  TITLE     Binding of a reduced peptide inhibitor to the aspartic proteinase
            from Rhizopus chinensis: implications for a mechanism of action.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 7009-13.
  ORGANISM  Rhizopus chinensis
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.21
            ExPASy - ENZYME nomenclature database: 3.4.23.21
            ExplorEnz - The Enzyme Database: 3.4.23.21
            ERGO genome analysis and discovery system: 3.4.23.21
            BRENDA, the Enzyme Database: 3.4.23.21
            CAS: 9074-09-3
///
ENTRY       EC 3.4.23.22                Enzyme
NAME        endothiapepsin;
            Endothia aspartic proteinase;
            Endothia acid proteinase;
            Endothia parasitica acid proteinase;
            Endothia parasitica aspartic proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Hydrolysis of proteins with specificity similar to that of pepsin A;
            prefers hydrophobic residues at P1 and P1', but does not cleave
            Ala14-Leu in the B chain of insulin or Z-Glu-Tyr. Clots milk
COMMENT     From the ascomycete Endothia parasitica. In peptidase family A1
            (pepsin A family).
REFERENCE   1
  AUTHORS   Whitaker, J.R.
  TITLE     Protease of Endothia parasitica.
  JOURNAL   Methods Enzymol. 19 (1970) 436-445.
  ORGANISM  Endothia parasitica
REFERENCE   2  [PMID:4552802]
  AUTHORS   Williams DC, Witaker JR, Caldwell PV.
  TITLE     Hydrolysis of peptide bonds of the oxidized B-chain of insulin by
            Endothia parasitica protease.
  JOURNAL   Arch. Biochem. Biophys. 149 (1972) 52-61.
  ORGANISM  Endothia parasitica
REFERENCE   3  [PMID:3305016]
  AUTHORS   Barkholt V.
  TITLE     Amino acid sequence of endothiapepsin. Complete primary structure of
            the aspartic protease from Endothia parasitica.
  JOURNAL   Eur. J. Biochem. 167 (1987) 327-38.
  ORGANISM  Endothia parasitica
REFERENCE   4  [PMID:3119339]
  AUTHORS   Cooper J, Foundling S, Hemmings A, Blundell T, Jones DM, Hallett A,
            Szelke M.
  TITLE     The structure of a synthetic pepsin inhibitor complexed with
            endothiapepsin.
  JOURNAL   Eur. J. Biochem. 169 (1987) 215-21.
STRUCTURES  PDB: 1EED  1ENT  1EPL  1EPM  1EPN  1EPO  1EPP  1EPQ  1EPR  1GKT  
                 1GVT  1GVU  1GVV  1GVW  1GVX  1OD1  1OEW  1OEX  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.22
            ExPASy - ENZYME nomenclature database: 3.4.23.22
            ExplorEnz - The Enzyme Database: 3.4.23.22
            ERGO genome analysis and discovery system: 3.4.23.22
            BRENDA, the Enzyme Database: 3.4.23.22
            CAS: 37205-60-0
///
ENTRY       EC 3.4.23.23                Enzyme
NAME        mucorpepsin;
            Mucor rennin;
            Mucor aspartic proteinase;
            Mucor acid proteinase;
            Mucor acid protease;
            Mucor miehei aspartic proteinase;
            Mucor miehei aspartic protease;
            Mucor aspartic proteinase;
            Mucor pusillus emporase;
            Fromase 100;
            Mucor pusillus rennin;
            Fromase 46TL;
            Mucor miehei rennin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Hydrolysis of proteins, favouring hydrophobic residues at P1 and
            P1'. Clots milk. Does not accept Lys at P1, and hence does not
            activate trypsinogen
COMMENT     Isolated from the zygomycete fungi Mucor pusillus and M. miehei. The
            two species variants show 83% sequence identity and are
            immunologically crossreactive. In peptidase family A1 (pepsin A
            family). Formerly included in EC 3.4.23.6
REFERENCE   1
  AUTHORS   Arima, K., Yu, J. and Iwasaki, S.
  TITLE     Milk-clotting enzyme from Mucor pusillus var. lindt.
  JOURNAL   Methods Enzymol. 19 (1970) 446-459.
  ORGANISM  Mucor pusillus
REFERENCE   2
  AUTHORS   Ottesen, M. and Rickert, W.
  TITLE     The acid protease of Mucor miehei.
  JOURNAL   Methods Enzymol. 19 (1970) 459-460.
  ORGANISM  Mucor miehei
REFERENCE   3  [PMID:4573298]
  AUTHORS   Sternberg M.
  TITLE     Bond specificity, active site and milk clotting mechanism of the
            Mucor miehei protease.
  JOURNAL   Biochim. Biophys. Acta. 285 (1972) 383-92.
  ORGANISM  Mucor miehei
REFERENCE   4
  AUTHORS   Oka, T., Ishino, K., Tsuzuki, H., Morihara, K. and Arima, K.
  TITLE     On the specificity of a rennin-like enzyme from Mucor pusillus.
  JOURNAL   Agric. Biol. Chem. 37 (1973) 1177-1184.
  ORGANISM  Mucor pusillus
REFERENCE   5  [PMID:3042459]
  AUTHORS   Baudys M, Foundling S, Pavlik M, Blundell T, Kostka V.
  TITLE     Protein chemical characterization of Mucor pusillus aspartic
            proteinase. Amino acid sequence homology with the other aspartic
            proteinases, disulfide bond arrangement and site of carbohydrate
            attachment.
  JOURNAL   FEBS. Lett. 235 (1988) 271-4.
  ORGANISM  Mucor pusillus
STRUCTURES  PDB: 1E5O  1E80  1E81  1E82  1MPP  2ASI  2RMP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.23
            ExPASy - ENZYME nomenclature database: 3.4.23.23
            ExplorEnz - The Enzyme Database: 3.4.23.23
            ERGO genome analysis and discovery system: 3.4.23.23
            BRENDA, the Enzyme Database: 3.4.23.23
            CAS: 148465-73-0
///
ENTRY       EC 3.4.23.24                Enzyme
NAME        candidapepsin;
            Candida albicans aspartic proteinase;
            Candida albicans carboxyl proteinase;
            Candida albicans secretory acid proteinase;
            Candida olea acid proteinase;
            Candida aspartic proteinase;
            Candida olea aspartic proteinase;
            Candida albicans aspartic proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Preferential cleavage at the carboxyl of hydrophobic amino acids,
            but fails to cleave Leu15-Tyr, Tyr16-Leu and Phe24-Phe of insulin B
            chain. Activates trypsinogen, and degrades keratin
INHIBITOR   Pepstatin [CPD:C00773]
COMMENT     This endopeptidase from the imperfect yeast Candida albicans is
            inhibited by pepstatin, but not by methyl 2-diazoacetamidohexanoate
            or 1,2-epoxy-3-(p-nitrophenoxy)propane. In peptidase family A1
            (pepsin A family). Formerly included in EC 3.4.23.6
REFERENCE   1  [PMID:5729955]
  AUTHORS   Remold H, Fasold H, Staib F.
  TITLE     Purification and characterization of a proteolytic enzyme from
            Candida albicans.
  JOURNAL   Biochim. Biophys. Acta. 167 (1968) 399-406.
  ORGANISM  Candida albicans [GN:cal]
REFERENCE   2  [PMID:7018586]
  AUTHORS   Ruchel R.
  TITLE     Properties of a purified proteinase from the yeast Candida albicans.
  JOURNAL   Biochim. Biophys. Acta. 659 (1981) 99-113.
  ORGANISM  Candida albicans [GN:cal]
REFERENCE   3  [PMID:6203988]
  AUTHORS   Negi M, Tsuboi R, Matsui T, Ogawa H.
  TITLE     Isolation and characterization of proteinase from Candida albicans:
            substrate specificity.
  JOURNAL   J. Invest. Dermatol. 83 (1984) 32-6.
  ORGANISM  Candida albicans [GN:cal]
REFERENCE   4  [PMID:2646602]
  AUTHORS   Lott TJ, Page LS, Boiron P, Benson J, Reiss E.
  TITLE     Nucleotide sequence of the Candida albicans aspartyl proteinase
            gene.
  JOURNAL   Nucleic. Acids. Res. 17 (1989) 1779.
  ORGANISM  Candida albicans [GN:cal]
ORTHOLOGY   KO: K06005  
GENES       PIC: PICST_73446(APR1)
STRUCTURES  PDB: 1EAG  1J71  1ZAP  2H6S  2H6T  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.24
            ExPASy - ENZYME nomenclature database: 3.4.23.24
            ExplorEnz - The Enzyme Database: 3.4.23.24
            ERGO genome analysis and discovery system: 3.4.23.24
            BRENDA, the Enzyme Database: 3.4.23.24
            CAS: 69458-91-9
///
ENTRY       EC 3.4.23.25                Enzyme
NAME        saccharopepsin;
            yeast endopeptidase A;
            Saccharomyces aspartic proteinase;
            aspartic proteinase yscA;
            proteinase A;
            proteinase yscA;
            yeast proteinase A;
            Saccharomyces cerevisiae aspartic proteinase A;
            yeast proteinase A;
            PRA
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Hydrolysis of proteins with broad specificity for peptide bonds.
            Cleaves -Leu-Leu!Val-Tyr bond in a synthetic substrate. Does not act
            on esters of Tyr or Arg
COMMENT     Located in the vacuole of the baker's yeast (Saccharomyces
            cerevisiae) cell. In peptidase family A1 (pepsin A family).
REFERENCE   1
  AUTHORS   Hata, T., Hayashi, R. and Dot, E.
  TITLE     Purification of yeast proteinases. Part III. Isolation and
            physicochemical properties of yeast proteinase A and C.
  JOURNAL   Agric. Biol. Chem. 31 (1967) 357-367.
REFERENCE   2  [PMID:7002931]
  AUTHORS   Meussdoerffer F, Tortora P, Holzer H.
  TITLE     Purification and properties of proteinase A from yeast.
  JOURNAL   J. Biol. Chem. 255 (1980) 12087-93.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:3023936]
  AUTHORS   Ammerer G, Hunter CP, Rothman JH, Saari GC, Valls LA, Stevens TH.
  TITLE     PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a
            vacuolar enzyme required for processing of vacuolar precursors.
  JOURNAL   Mol. Cell. Biol. 6 (1986) 2490-9.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K01381  saccharopepsin
GENES       SCE: YPL154C(PEP4)
            AGO: AGOS_ACR144W
            CGR: CAGL0M02211g
            ANI: AN2903.2
            AFM: AFUA_3G11400
            AOR: AO090003000693
            CNE: CNA05650
            UMA: UM04926.1
STRUCTURES  PDB: 1DP5  1DPJ  1FMU  1FMX  1FQ4  1FQ5  1FQ6  1FQ7  1FQ8  1G0V  
                 2JXR  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.25
            ExPASy - ENZYME nomenclature database: 3.4.23.25
            ExplorEnz - The Enzyme Database: 3.4.23.25
            ERGO genome analysis and discovery system: 3.4.23.25
            BRENDA, the Enzyme Database: 3.4.23.25
            CAS: 37228-80-1
///
ENTRY       EC 3.4.23.26                Enzyme
NAME        rhodotorulapepsin;
            Rhodotorula aspartic proteinase;
            Cladosporium acid protease;
            Cladosporium acid proteinase;
            Paecilomyces proteinase;
            Cladosporium aspartic proteinase;
            Paecilomyces proteinase;
            Rhodotorula glutinis aspartic proteinase;
            Rhodotorula glutinis acid proteinase;
            Rhodotorula glutinis aspartic proteinase II;
            Rhodotorula acid proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Specificity similar to that of pepsin A. Cleaves Z-Lys!Ala-Ala-Ala
            and activates trypsinogen
COMMENT     From the imperfect yeast Rhodotorula glutinis. Somewhat similar
            enzymes have been isolated from the imperfect yeast-like organism
            Cladosporium sp. [4,6] and the imperfect fungus Paecilomyces varioti
            [1,2].
REFERENCE   1
  AUTHORS   Sawada, J.
  TITLE     Studies on the acid-protease of Paecilomyces varioti Bainier
            TPR-220. Part I. Crystallization of the acid-protease of
            Paecilomyces varioti Bainier TPR-220.
  JOURNAL   Agric. Biol. Chem. 27 (1963) 677-683.
  ORGANISM  Paecilomyces varioti
REFERENCE   2
  AUTHORS   Sawada, J.
  TITLE     The acid-protease of Paecilomyces varioti. III. The specificity of
            the crystalline acid-protease on synthetic substrates.
  JOURNAL   Agric. Biol. Chem. 28 (1964) 869-875.
  ORGANISM  Paecilomyces varioti
REFERENCE   3
  AUTHORS   Kamada, M., Oda, K. and Murao, S.
  TITLE     The purification of the extracellular acid protease of Rhodotorula
            glutinis K-24 and its general properties.
  JOURNAL   Agric. Biol. Chem. 36 (1972) 1095-1101.
  ORGANISM  Rhodotorula glutinis
REFERENCE   4
  AUTHORS   Murao, S., Funakoshi, S. and Oda, K.
  TITLE     Purification, crystallization and some enzymatic properties of acid
            protease of Cladosporium sp. No. 45-2.
  JOURNAL   Agric. Biol. Chem. 36 (1972) 1327-1333.
  ORGANISM  Cladosporium sp.
REFERENCE   5
  AUTHORS   Oda, K., Kamada, M. and Murao, S.
  TITLE     Some physicochemical properties and substrate specificity of acid
            protease of Rhodotorula glutinis K-24.
  JOURNAL   Agric. Biol. Chem. 36 (1972) 1103-1108.
  ORGANISM  Rhodotorula glutinis
REFERENCE   6
  AUTHORS   Oda, K., Funakoshi, S. and Murao, S.
  TITLE     Some physicochemical properties and substrate specificity of acid
            protease isolated from Cladosporium sp. No. 45-2.
  JOURNAL   Agric. Biol. Chem. 37 (1973) 1723-1729.
  ORGANISM  Cladosporium sp.
REFERENCE   7  [PMID:10290]
  AUTHORS   Takahashi K, Chang WJ.
  TITLE     The structure and function of acid proteases. V. Comparative studies
            on the specific inhibition of acid proteases by
            diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy)
            propane and pepstatin.
  JOURNAL   J. Biochem. (Tokyo). 80 (1976) 497-506.
REFERENCE   8
  AUTHORS   Majima, E., Oda, K., Murao, S. and Ichishima, E.
  TITLE     Comparative study on the specificities of several fungal aspartic
            and acidic proteinases towards the tetradecapeptide of a renin
            substrate.
  JOURNAL   Agric. Biol. Chem. 52 (1988) 787-793.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.26
            ExPASy - ENZYME nomenclature database: 3.4.23.26
            ExplorEnz - The Enzyme Database: 3.4.23.26
            ERGO genome analysis and discovery system: 3.4.23.26
            BRENDA, the Enzyme Database: 3.4.23.26
            CAS: 37259-59-9
///
ENTRY       EC 3.4.23.27      Obsolete  Enzyme
NAME        Transferred to 3.4.21.103
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
COMMENT     Transferred entry: now EC 3.4.21.103 physarolisin (EC 3.4.23.27
            created 1992 (EC 3.4.23.6 created 1992 (EC 3.4.23.6 created 1961 as
            EC 3.4.4.17, transferred 1972 to EC 3.4.23.6, modified 1981 [EC
            3.4.23.7, EC 3.4.23.8, EC 3.4.23.9, EC 3.4.23.10, EC 3.4.99.1, EC
            3.4.99.15 and EC 3.4.99.25 all created 1972 and incorporated 1978],
            part incorporated 1992), deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.27
            ExPASy - ENZYME nomenclature database: 3.4.23.27
            ExplorEnz - The Enzyme Database: 3.4.23.27
            ERGO genome analysis and discovery system: 3.4.23.27
            BRENDA, the Enzyme Database: 3.4.23.27
///
ENTRY       EC 3.4.23.28                Enzyme
NAME        acrocylindropepsin;
            Acrocylindrium proteinase;
            Acrocylindrium acid proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Preference for hydrophobic residues at P1 and P1'. Action on the B
            chain of insulin is generally similar to that of pepsin A, but it
            also cleaves Leu6!Cys(SO3H), Glu21!Arg and Asn3!Gln, although not
            Gln4-His
COMMENT     From the imperfect fungus Acrocylindrium sp. Has a very low pH
            optimum on casein of 2.0. In peptidase family A1 (pepsin A family).
REFERENCE   1
  AUTHORS   Uchino, F., Kurono, Y. and Doi, S.
  TITLE     Purification and some properties of crystalline acid protease from
            Acrocylindrium sp.
  JOURNAL   Agric. Biol. Chem. 31 (1967) 428-434.
  ORGANISM  Acrocylindrium sp.
REFERENCE   2
  AUTHORS   Ichihara, S. and Uchino, F.
  TITLE     The specificity of acid proteinase from Acrocylindrium.
  JOURNAL   Agric. Biol. Chem. 39 (1975) 423-428.
  ORGANISM  Acrocylindrium sp.
REFERENCE   3  [PMID:10290]
  AUTHORS   Takahashi K, Chang WJ.
  TITLE     The structure and function of acid proteases. V. Comparative studies
            on the specific inhibition of acid proteases by
            diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy)
            propane and pepstatin.
  JOURNAL   J. Biochem. (Tokyo). 80 (1976) 497-506.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.28
            ExPASy - ENZYME nomenclature database: 3.4.23.28
            ExplorEnz - The Enzyme Database: 3.4.23.28
            ERGO genome analysis and discovery system: 3.4.23.28
            BRENDA, the Enzyme Database: 3.4.23.28
            CAS: 37288-84-9
///
ENTRY       EC 3.4.23.29                Enzyme
NAME        polyporopepsin;
            Polyporus aspartic proteinase;
            Irpex lacteus aspartic proteinase;
            Irpex lacteus carboxyl proteinase B
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Milk clotting activity, broad specificity, but fails to cleave
            Leu15-Tyr or Tyr16-Leu of insulin B chain
COMMENT     From the basidiomycete Polyporus tulipiferae (formerly Irpex
            lacteus). In peptidase family A1 (pepsin A family)
REFERENCE   1
  AUTHORS   Kobayashi, H., Kusakabe, I. and Murakami, K.
  TITLE     Substrate specificity of a carboxyl proteinase from Irpex lacteus.
  JOURNAL   Agric. Biol. Chem. 47 (1983) 1921-1923.
  ORGANISM  Irpex lacteus
REFERENCE   2
  AUTHORS   Kobayashi, H., Sekibata, S., Shibuya, H., Yoshida, S., Kusakabe, I.
            and Murakami, K.
  TITLE     Cloning and sequence analysis of cDNA for Irpex lacteus aspartic
            proteinase.
  JOURNAL   Agric. Biol. Chem. 53 (1989) 1927-1933.
  ORGANISM  Irpex lacteus
STRUCTURES  PDB: 1WKR  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.29
            ExPASy - ENZYME nomenclature database: 3.4.23.29
            ExplorEnz - The Enzyme Database: 3.4.23.29
            ERGO genome analysis and discovery system: 3.4.23.29
            BRENDA, the Enzyme Database: 3.4.23.29
            CAS: 61573-73-7
///
ENTRY       EC 3.4.23.30                Enzyme
NAME        pycnoporopepsin;
            proteinase Ia;
            Pycnoporus coccineus aspartic proteinase;
            Trametes acid proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Similar to pepsin A, but narrower, cleaving only three bonds in the
            B chain of insulin: Ala14!Leu, Tyr16!Leu, and Phe24!Phe
COMMENT     From the basidiomycete Pycnoporus sanguineus, formerly known as P.
            coccineus and Trametes sanguinea. Formerly included in EC 3.4.23.6
REFERENCE   1
  AUTHORS   Tomoda, K. and Shimazono, H.
  TITLE     Acid protease produced by Trametes sanguinea a wood-destroying
            fungus. Part I. Purification and crystallization of the enzyme.
  JOURNAL   Agric. Biol. Chem. 28 (1964) 770-773.
  ORGANISM  Trametes sanguinea
REFERENCE   2
  AUTHORS   Tsuru, D., Hattori, A., Tsuji, H., Yamamoto, T. and Fukumoto, J.
  TITLE     Studies on mold proteases. Part II. Substrate specificity of acid
            protease of Rhizopus chinensis.
  JOURNAL   Agric. Biol. Chem. 33 (1969) 1419-1426.
  ORGANISM  Rhizopus chinensis
REFERENCE   3
  AUTHORS   Ichishima, E., Kumagai, H. and Tomoda, K.
  TITLE     Substrate specificity of carboxyl proteinase from Pycnoporus
            coccineus, a wood-deteriorating fungus.
  JOURNAL   Curr. Microbiol. 3 (1980) 333-337.
  ORGANISM  Pycnoporus coccineus
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.30
            ExPASy - ENZYME nomenclature database: 3.4.23.30
            ExplorEnz - The Enzyme Database: 3.4.23.30
            ERGO genome analysis and discovery system: 3.4.23.30
            BRENDA, the Enzyme Database: 3.4.23.30
            CAS: 77967-78-3
///
ENTRY       EC 3.4.23.31                Enzyme
NAME        scytalidopepsin A;
            Scytalidium aspartic proteinase A;
            Scytalidium lignicolum aspartic proteinase;
            Scytalidium lignicolum aspartic proteinase A-2;
            Scytalidium lignicolum aspartic proteinase A-I;
            Scytalidium lignicolum aspartic proteinase C;
            Scytalidium lignicolum carboxyl proteinase;
            Scytalidium lignicolum acid proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Hydrolysis of proteins with specificity similar to that of pepsin A,
            but also cleaves Cys(SO3H)7!Gly and Leu17!Val in the B chain of
            insulin
COMMENT     Isolated from the imperfect fungus Scytalidium lignicolum. Not
            inhibited by pepstatin-Ac, methyl 2-diazoacetamidohexanoate or
            1,2-epoxy-3-(p-nitrophenyl)propane. A related enzyme from the same
            organism, proteinase C, is also insensitive to these inhibitors and
            has Mr = 406,000 [3]
REFERENCE   1
  AUTHORS   Oda, K. and Murao, S.
  TITLE     Purification and some enzymatic properties of acid protease A and B
            of Scytalidium lignicolum ATCC 24568.
  JOURNAL   Agric. Biol. Chem. 38 (1974) 2435-2444.
  ORGANISM  Scytalidium lignicolum
REFERENCE   2
  AUTHORS   Oda, K. and Murao, S.
  TITLE     Action of Scytalidium lignicolum acid proteases on insulin B-chain.
  JOURNAL   Agric. Biol. Chem. 40 (1976) 1221-1225.
  ORGANISM  Scytalidium lignicolum
REFERENCE   3
  AUTHORS   Oda, K., Torishima, H. and Murao, S.
  TITLE     Purification and characterization of acid proteinase C of
            Scytalidium lignicolum ATCC 24568.
  JOURNAL   Agric. Biol. Chem. 50 (1986) 651-658.
  ORGANISM  Scytalidium lignicolum
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.31
            ExPASy - ENZYME nomenclature database: 3.4.23.31
            ExplorEnz - The Enzyme Database: 3.4.23.31
            ERGO genome analysis and discovery system: 3.4.23.31
            BRENDA, the Enzyme Database: 3.4.23.31
            CAS: 42613-34-3
///
ENTRY       EC 3.4.23.32                Enzyme
NAME        scytalidopepsin B;
            Scytalidium aspartic proteinase B;
            Ganoderma lucidum carboxyl proteinase;
            Ganoderma lucidum aspartic proteinase;
            Scytalidium lignicolum aspartic proteinase B;
            SLB
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Hydrolysis of proteins with broad specificity, cleaving Phe24!Phe,
            but not Leu15-Tyr and Phe25-Tyr in the B chain of insulin
COMMENT     A second endopeptidase from Scytalidium lignicolum (see
            scytalidopepsin A) that is insensitive to pepstatin and methyl
            2-diazoacetamidohexanoate. 1,2-Epoxy-3-(p-nitrophenoxy)propane
            reacts with Glu53, which replaces one of the aspartic residues at
            the active centre. One of the smallest aspartic endopeptidases
            active as the monomer, with Mr 22,000. Similarly inhibitor-resistant
            endopeptidases are found in the basidiomycetes Lentinus edodes [1]
            and Ganoderma lucidum [3], and in Polyporus tulipiferae [4], a
            second endopeptidase distinct from polyporopepsin, but these are of
            typical aspartic endopeptidase size, Mr about 36,000. Type example
            of peptidase family G1.
REFERENCE   1
  AUTHORS   Terashita, T., Oda, K., Kono, M. and Murao, S.
  TITLE     Streptomyces pepsin inhibitor-insensitive carboxyl proteinase from
            Lentinus edodes.
  JOURNAL   Agric. Biol. Chem. 45 (1981) 1937-1943.
  ORGANISM  Lentinus edodes
REFERENCE   2
  AUTHORS   Maita, T., Nagata, S., Matsuda, G., Maruta, S., Oda, K., Murao, S.
            and Tsuru, D.
  TITLE     Complete amino acid sequence of Scytalidium lignicolum acid protease
            B.
  JOURNAL   J. Biochem. (Tokyo) 95 (1984) 465-473.
  ORGANISM  Scytalidium lignicolum
REFERENCE   3  [PMID:6370989]
  AUTHORS   Maita T, Nagata S, Matsuda G, Maruta S, Oda K, Murao S, Tsuru D.
  TITLE     Complete amino acid sequence of Scytalidium lignicolum acid protease
            B.
  JOURNAL   J. Biochem. (Tokyo). 95 (1984) 465-75.
  ORGANISM  Scytalidium lignicolum
REFERENCE   4
  AUTHORS   Kobayashi, H., Kusakabe, I. and Murakami, K.
  TITLE     Purification and characterization of a pepstatin-insensitive
            carboxyl proteinase from Polyporus tulipiferae (Irpex lacteus).
  JOURNAL   Agric. Biol. Chem. 49 (1985) 2393-2397.
  ORGANISM  Polyporus tulipiferae (Irpex lacteus)
REFERENCE   5  [PMID:3519605]
  AUTHORS   Tsuru D, Shimada S, Maruta S, Yoshimoto T, Oda K, Murao S, Miyata T,
            Iwanaga S.
  TITLE     Isolation and amino acid sequence of a peptide containing an
            epoxide-reactive residue from the thermolysin-digest of Scytalidium
            lignicolum acid protease B.
  JOURNAL   J. Biochem. (Tokyo). 99 (1986) 1537-9.
  ORGANISM  Scytalidium lignicolum
STRUCTURES  PDB: 1S2B  1S2K  2IFR  2IFW  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.32
            ExPASy - ENZYME nomenclature database: 3.4.23.32
            ExplorEnz - The Enzyme Database: 3.4.23.32
            ERGO genome analysis and discovery system: 3.4.23.32
            BRENDA, the Enzyme Database: 3.4.23.32
            CAS: 104781-89-7
///
ENTRY       EC 3.4.23.33      Obsolete  Enzyme
NAME        Transferred to 3.4.21.101
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
COMMENT     Transferred entry: now EC 3.4.21.101, xanthomonalisin (EC 3.4.23.33
            created 1992, deleted 2001)
STRUCTURES  PDB: 1KDV  1KDY  1KDZ  1KE1  1KE2  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.33
            ExPASy - ENZYME nomenclature database: 3.4.23.33
            ExplorEnz - The Enzyme Database: 3.4.23.33
            ERGO genome analysis and discovery system: 3.4.23.33
            BRENDA, the Enzyme Database: 3.4.23.33
///
ENTRY       EC 3.4.23.34                Enzyme
NAME        cathepsin E;
            slow-moving proteinase;
            erythrocyte membrane aspartic proteinase;
            SMP;
            erythrocyte membrane aspartic proteinase;
            EMAP;
            non-pepsin proteinase;
            cathepsin D-like acid proteinase;
            cathepsin E-like acid proteinase;
            cathepsin D-type proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Similar to cathepsin D, but slightly broader specificity
COMMENT     Found in stomach, spleen, erythrocyte membrane; not lysosomal.
            Pro-cathepsin E is an 86 kDa disulfide-linked dimer; activation or
            reduction produces monomer. In peptidase family A1 (pepsin A family)
REFERENCE   1  [PMID:3741628]
  AUTHORS   Lapresle C, Puizdar V, Porchon-Bertolotto C, Joukoff E, Turk V.
  TITLE     Structural differences between rabbit cathepsin E and cathepsin D.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 367 (1986) 523-6.
  ORGANISM  rabbit
REFERENCE   2  [PMID:3058036]
  AUTHORS   Yonezawa S, Fujii K, Maejima Y, Tamoto K, Mori Y, Muto N.
  TITLE     Further studies on rat cathepsin E: subcellular localization and
            existence of the active subunit form.
  JOURNAL   Arch. Biochem. Biophys. 267 (1988) 176-83.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:3058118]
  AUTHORS   Jupp RA, Richards AD, Kay J, Dunn BM, Wyckoff JB, Samloff IM,
            Yamamoto K.
  TITLE     Identification of the aspartic proteinases from human erythrocyte
            membranes and gastric mucosa (slow-moving proteinase) as
            catalytically equivalent to cathepsin E.
  JOURNAL   Biochem. J. 254 (1988) 895-8.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:2674141]
  AUTHORS   Azuma T, Pals G, Mohandas TK, Couvreur JM, Taggart RT.
  TITLE     Human gastric cathepsin E. Predicted sequence, localization to
            chromosome 1, and sequence homology with other aspartic proteinases.
  JOURNAL   J. Biol. Chem. 264 (1989) 16748-53.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01382  cathepsin E
GENES       HSA: 1510(CTSE)
            PTR: 457677(CTSE)
            MMU: 13034(Ctse)
            RNO: 25424(Ctse)
            CFA: 488577(CTSE)
            GGA: 771791(CTSE)
            DME: Dmel_CG13374(pcl)
            TPV: TP03_0056
            TET: TTHERM_00011710 TTHERM_00202810 TTHERM_01053050
                 TTHERM_01128610 TTHERM_01128630 TTHERM_01128640
STRUCTURES  PDB: 1TZS  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.34
            ExPASy - ENZYME nomenclature database: 3.4.23.34
            ExplorEnz - The Enzyme Database: 3.4.23.34
            ERGO genome analysis and discovery system: 3.4.23.34
            BRENDA, the Enzyme Database: 3.4.23.34
            CAS: 110910-42-4
///
ENTRY       EC 3.4.23.35                Enzyme
NAME        barrierpepsin;
            barrier proteinase;
            Bar proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Selective cleavage of -Leu6!Lys- bond in the pheromone alpha-mating
            factor
COMMENT     A secreted endopeptidase known from baker's yeast (Saccharomyces
            cerevisiae). In peptidase family A1 (pepsin A family)
REFERENCE   1  [PMID:3124102]
  AUTHORS   MacKay VL, Welch SK, Insley MY, Manney TR, Holly J, Saari GC, Parker
            ML.
  TITLE     The Saccharomyces cerevisiae BAR1 gene encodes an exported protein
            with homology to pepsin.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 55-9.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:1812704]
  AUTHORS   MacKay VL, Armstrong J, Yip C, Welch S, Walker K, Osborn S, Sheppard
            P, Forstrom J.
  TITLE     Characterization of the Bar proteinase, an extracellular enzyme from
            the yeast Saccharomyces cerevisiae.
  JOURNAL   Adv. Exp. Med. Biol. 306 (1991) 161-72.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K01383  barrierpepsin
GENES       SCE: YIL015W(BAR1)
            AGO: AGOS_AGR240W
            CGR: CAGL0J02288g
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.35
            ExPASy - ENZYME nomenclature database: 3.4.23.35
            ExplorEnz - The Enzyme Database: 3.4.23.35
            ERGO genome analysis and discovery system: 3.4.23.35
            BRENDA, the Enzyme Database: 3.4.23.35
            CAS: 152060-38-3
///
ENTRY       EC 3.4.23.36                Enzyme
NAME        signal peptidase II;
            premurein-leader peptidase;
            prolipoprotein signal peptidase;
            leader peptidase II;
            premurein leader proteinase;
            leader peptidase II
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Release of signal peptides from bacterial membrane prolipoproteins
            including murein prolipoprotein. Hydrolyses
            -Xaa-Yaa-Zaa!(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic
            (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have
            small, neutral sidechains
INHIBITOR   Pepstatin [CPD:C00773];
            Globomycin [CPD:C01700]
COMMENT     An 18-kDa enzyme present in bacterial inner membranes. Inhibited by
            pepstatin and the antibiotic globomycin. Type example of peptidase
            family A8.
REFERENCE   1  [PMID:2202720]
  AUTHORS   Dev IK, Ray PH.
  TITLE     Signal peptidases and signal peptide hydrolases.
  JOURNAL   J. Bioenerg. Biomembr. 22 (1990) 271-90.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:1544479]
  AUTHORS   Zhao XJ, Wu HC.
  TITLE     Nucleotide sequence of the Staphylococcus aureus signal peptidase II
            (lsp) gene.
  JOURNAL   FEBS. Lett. 299 (1992) 80-4.
  ORGANISM  Staphylococcus aureus
REFERENCE   3  [PMID:7674920]
  AUTHORS   Sankaran K, Wu HC.
  TITLE     Bacterial prolipoprotein signal peptidase.
  JOURNAL   Methods. Enzymol. 248 (1995) 169-80.
ORTHOLOGY   KO: K03101  signal peptidase II
GENES       ECO: b0027(lspA)
            ECJ: JW0025(lspA)
            ECE: Z0031(lspA)
            ECS: ECs0030
            ECC: c0031(lspA)
            ECI: UTI89_C0029(lspA)
            ECP: ECP_0025
            ECV: APECO1_1956(lspA)
            ECW: EcE24377A_0027(lspA)
            ECX: EcHS_A0029(lspA)
            STY: STY0056(lspA)
            STT: t0049(lspA)
            SPT: SPA0048(lspA)
            SEC: SC0041(lspA)
            STM: STM0047(lspA)
            YPE: YPO0476(lspA)
            YPK: y3699(lspA)
            YPM: YP_3704(fkpB)
            YPA: YPA_4069
            YPN: YPN_0348
            YPP: YPDSF_3156
            YPS: YPTB0618(lspA)
            YPI: YpsIP31758_3459(lspA)
            YEN: YE0617(b0027)
            SFL: SF0023(lspA)
            SFX: S0026(lspA)
            SFV: SFV_0021(lspA)
            SSN: SSON_0032(lspA)
            SBO: SBO_0026(lspA)
            SDY: SDY_0049(lspA)
            ECA: ECA3875(lspA)
            PLU: plu0592(lspA)
            BUC: BU148(lspA)
            BAS: BUsg141(lspA)
            BAB: bbp138(lspA)
            BCC: BCc_164(lepB)
            WBR: WGLp293(lspA)
            SGL: SG0415
            ENT: Ent638_0585
            SPE: Spro_0699
            BFL: Bfl119(lspA)
            BPN: BPEN_123(lspA)
            HIN: HI1006(lspA)
            HIT: NTHI1181(lspA)
            HIP: CGSHiEE_06960(lspA)
            HIQ: CGSHiGG_08630(lspA)
            HDU: HD0063(lspA)
            HSO: HS_0185(lspA)
            PMU: PM1663(lspA)
            MSU: MS1750(lspA)
            APL: APL_1519(lspA)
            ASU: Asuc_1875
            XFA: XF2417
            XFT: PD1436(lspA)
            XCC: XCC1156(lspA)
            XCB: XC_3086
            XCV: XCV1291(lspA)
            XAC: XAC1255(lspA)
            XOO: XOO1627(lspA)
            XOM: XOO_1513(XOO1513)
            VCH: VC0683
            VCO: VC0395_A0215(lspA)
            VVU: VV1_0506
            VVY: VV0688
            VPA: VP0535
            VFI: VF0468
            PPR: PBPRA0592
            PAE: PA4559(ls)
            PAU: PA14_60360(lspA)
            PAP: PSPA7_5199(lspA)
            PPU: PP_0604(lspA)
            PPF: Pput_0645
            PST: PSPTO_0807(lspA)
            PSB: Psyr_0711
            PSP: PSPPH_0722(lspA)
            PFL: PFL_5320(lspA)
            PFO: Pfl_4851
            PEN: PSEEN2363 PSEEN4691(lspA)
            PMY: Pmen_0954
            PAR: Psyc_0363(lspA)
            PCR: Pcryo_0401 Pcryo_1352
            PRW: PsycPRwf_1893
            ACI: ACIAD0021(lspA)
            ACB: A1S_0019
            SON: SO_3531(lspA)
            SDN: Sden_2722
            SFR: Sfri_2889
            SAZ: Sama_0925
            SBL: Sbal_1055
            SBM: Shew185_1122
            SLO: Shew_1100
            SPC: Sputcn32_0196 Sputcn32_0222 Sputcn32_1060
            SSE: Ssed_1195
            SPL: Spea_1084
            SHE: Shewmr4_2956
            SHM: Shewmr7_3038
            SHN: Shewana3_1036 Shewana3_3135 Shewana3_4320
            SHW: Sputw3181_0415 Sputw3181_0440 Sputw3181_0519 Sputw3181_3105
            ILO: IL0633 IL1127(lspA)
            CPS: CPS_1183(lspA)
            PHA: PSHAa0919(lspA)
            PAT: Patl_3177
            SDE: Sde_2565
            PIN: Ping_3270
            MAQ: Maqu_0863 Maqu_0889 Maqu_1404 Maqu_1409 Maqu_3274
            CBU: CBU_0397(lspA)
            CBD: COXBU7E912_1671(lspA)
            LPN: lpg0938(lspA)
            LPF: lpl0969(lspA)
            LPP: lpp1000(lspA)
            MCA: MCA2254(lspA)
            FTU: FTT0914c(lspA)
            FTF: FTF0914c(lspA)
            FTW: FTW_1265(lspA)
            FTL: FTL_0435
            FTH: FTH_0427(lspA)
            FTA: FTA_0456(lspA)
            FTN: FTN_0440(lspA)
            TCX: Tcr_0496
            NOC: Noc_2276
            AEH: Mlg_0853
            HHA: Hhal_1835
            HCH: HCH_05932(lspA)
            CSA: Csal_0482
            ABO: ABO_0460 ABO_1369(lspA)
            AHA: AHA_0683(lspA)
            DNO: DNO_0084(lspA)
            BCI: BCI_0557(lspA)
            RMA: Rmag_0652
            VOK: COSY_0599(lspA)
            NME: NMB1832
            NMA: NMA0623(lsp)
            NMC: NMC0384(lsp)
            NGO: NGO0071
            CVI: CV_3568(lspA)
            RSO: RSc2459(lspA)
            REU: Reut_A2746
            REH: H16_A3047(lspA)
            RME: Rmet_2304 Rmet_2886
            BMA: BMA2243(lspA)
            BMV: BMASAVP1_A2659(lspA)
            BML: BMA10299_A1034(lspA)
            BMN: BMA10247_2113(lspA)
            BXE: Bxe_A0806 Bxe_A1105 Bxe_A1119 Bxe_A2904 Bxe_B1606 Bxe_B2910
                 Bxe_C0390 Bxe_C0884
            BVI: Bcep1808_2591
            BUR: Bcep18194_A5845
            BCN: Bcen_1902
            BCH: Bcen2424_2513
            BAM: Bamb_2560
            BPS: BPSL0905(lspA)
            BPM: BURPS1710b_1121(lspA)
            BPL: BURPS1106A_0970(lspA)
            BPD: BURPS668_0966(lspA)
            BTE: BTH_I0769(lspA)
            PNU: Pnuc_1741
            BPE: BP1752(lspA)
            BPA: BPP1983(lspA)
            BBR: BB2171(lspA)
            RFR: Rfer_1431
            POL: Bpro_3850
            PNA: Pnap_3230
            AAV: Aave_3451
            AJS: Ajs_3400 Ajs_3473
            VEI: Veis_2110
            MPT: Mpe_A3047
            HAR: HEAR0520(lspAA) HEAR0844(lspAB) HEAR1544(lspAC)
            MMS: mma_0827(lspA)
            NEU: NE1148(lspA)
            NET: Neut_1438
            NMU: Nmul_A2655
            EBA: ebA4447(lspA)
            AZO: azo1204(lspA)
            DAR: Daro_2630 Daro_3045
            TBD: Tbd_1858
            MFA: Mfla_2207
            HPY: HP0074(lspA)
            HPJ: jhp0069(lspA)
            HPA: HPAG1_0075
            HHE: HH1780(lspA)
            HAC: Hac_1530(lspA)
            WSU: WS0819(lspA)
            TDN: Tmden_2038
            CJE: Cj0361(lspA)
            CJR: CJE0410(lspA)
            CJJ: CJJ81176_0384(lspA)
            CJU: C8J_0337(lspA)
            CJD: JJD26997_1596(lspA)
            CFF: CFF8240_1716(lspA)
            CCV: CCV52592_0743(lspA)
            CHA: CHAB381_1790(lspA)
            CCO: CCC13826_1808(lspA) CCC13826_2148(lspA)
            ABU: Abu_0080(lspA)
            NIS: NIS_0107(lspA)
            SUN: SUN_0066
            GSU: GSU3135(lspA)
            GME: Gmet_0352
            PCA: Pcar_2454
            PPD: Ppro_3597
            DVU: DVU1928(lspA)
            DDE: Dde_2143
            LIP: LI1052(lsp)
            BBA: Bd3365(lspA)
            DPS: DP2551
            ADE: Adeh_0013
            MXA: MXAN_0368(lspA) MXAN_0369(lspA) MXAN_3930(lspA)
                 MXAN_3944(lspA)
            SAT: SYN_01453
            SFU: Sfum_0123 Sfum_3566
            RPR: RP408(lspA)
            RTY: RT0394(lspA)
            RCO: RC0558(lspA)
            RFE: RF_0632(lspA)
            RBE: RBE_0886(lspA)
            RAK: A1C_03040(lspA)
            RBO: A1I_02465(lspA)
            RRI: A1G_03150(lspA)
            OTS: OTBS_2043(lspA)
            WOL: WD0760(lspA)
            WBM: Wbm0417
            AMA: AM1081(lspA)
            APH: APH_1160(lspA)
            ERU: Erum8120(lspA)
            ERW: ERWE_CDS_08600(lspA)
            ERG: ERGA_CDS_08510(lspA)
            ECN: Ecaj_0852
            ECH: ECH_1060(lspA)
            NSE: NSE_0915(lspA)
            PUB: SAR11_0157(lspA)
            MLO: mlr3211
            MES: Meso_3678 Meso_4211
            SME: SMc01129(lspA)
            ATU: Atu0342(lspA)
            ATC: AGR_C_596
            RET: RHE_CH00392(lpsA)
            RLE: RL0410(lspA)
            BME: BMEI1799
            BMF: BAB1_0148(lspA)
            BMS: BR0149(lspA)
            BMB: BruAb1_0145(lspA)
            BOV: BOV_0144(lspA)
            BJA: blr7482
            BRA: BRADO6068(lspA)
            BBT: BBta_1715(lspA)
            RPA: RPA4376(lspA)
            RPB: RPB_4181
            RPC: RPC_1394
            RPD: RPD_4037
            RPE: RPE_1415
            NWI: Nwi_2543
            NHA: Nham_3163
            BHE: BH00100(lspA)
            BQU: BQ00090(lspA)
            BBK: BARBAKC583_1375(lspA)
            CCR: CC_0700
            SIL: SPO3373(lspA)
            SIT: TM1040_0092
            RSP: RSP_1099(lspA)
            JAN: Jann_4043
            RDE: RD1_0656(lspA)
            MMR: Mmar10_0614 Mmar10_2334
            HNE: HNE_0850(lspA1) HNE_1728(lspA2)
            ZMO: ZMO0324(lspA)
            NAR: Saro_3258
            SAL: Sala_2356
            ELI: ELI_04470 ELI_13545
            GOX: GOX1250
            GBE: GbCGDNIH1_0465
            RRU: Rru_A2967
            MAG: amb0835
            MGM: Mmc1_2146
            ABA: Acid345_1860
            SUS: Acid_5352
            BSU: BG11793(lsp)
            BHA: BH2543(lsp)
            BAN: BA4032(lspA)
            BAR: GBAA4032(lspA)
            BAA: BA_4503
            BAT: BAS3744
            BCE: BC3893
            BCA: BCE_3938(lspA)
            BCZ: BCZK3652(lspA)
            BTK: BT9727_3635(lspA)
            BLI: BL02269(lspA)
            BLD: BLi01765(lspA)
            BCL: ABC2340(lsp)
            BAY: RBAM_015280(lspA)
            OIH: OB1485
            GKA: GK1145
            SAU: SA1039(lsp)
            SAV: SAV1196(lsp)
            SAM: MW1079(lsp)
            SAR: SAR1172(lspA)
            SAS: SAS1130
            SAC: SACOL1208(lspA)
            SAB: SAB1060(lspA)
            SAA: SAUSA300_1089(lspA)
            SAO: SAOUHSC_01162
            SEP: SE0871
            SER: SERP0762(lspA)
            SHA: SH1718(lsp)
            SSP: SSP1576
            LMO: lmo1101 lmo1844(lsp)
            LMF: LMOf2365_1872(lspA)
            LIN: lin1958(lsp)
            LWE: lwe1863(lspA)
            LLA: L0335(lspA)
            LLC: LACR_1081
            LLM: llmg_1525(pA)
            SPY: SPy_0826(lsp)
            SPZ: M5005_Spy_0637(lsp)
            SPM: spyM18_0888(lspA)
            SPG: SpyM3_0556(lsp)
            SPS: SPs1298
            SPH: MGAS10270_Spy0693(lsp)
            SPI: MGAS10750_Spy0726(lsp)
            SPJ: MGAS2096_Spy0703(lsp)
            SPK: MGAS9429_Spy0692(lsp)
            SPF: SpyM51170(lsp)
            SPA: M6_Spy0655
            SPB: M28_Spy0617(lsp)
            SPN: SP_0928
            SPR: spr0829(lspA)
            SPD: SPD_0819(lspA)
            SAG: SAG1366(lspA)
            SAN: gbs1436
            SAK: SAK_1399(lspA)
            SMU: SMU.853(lspA)
            STC: str0521(lspA)
            STL: stu0521(lspA)
            SSA: SSA_1069(lspA)
            SGO: SGO_1089(lspA)
            LPL: lp_1780(lspA)
            LJO: LJ1187
            LAC: LBA1152(lspA)
            LSA: LSA0948(lspA)
            LSL: LSL_0825(lspA)
            LDB: Ldb1021(lsp)
            LBU: LBUL_0929
            LBR: LVIS_0833
            LCA: LSEI_1459
            EFA: EF1723(lspA)
            STH: STH1242
            CAC: CAC2115(lspA)
            CPE: CPE2244
            CPR: CPR_0074
            CTC: CTC01615
            CNO: NT01CX_0177 NT01CX_1951(lspA)
            CDF: CD2597(lspA)
            CBO: CBO1475(lspA)
            CBA: CLB_1500(lspA)
            CBH: CLC_1512(lspA)
            CBF: CLI_1559(lspA)
            CHY: CHY_1506(lspA)
            DSY: DSY2866
            SWO: Swol_1287
            TTE: TTE1539(lspA)
            MTA: Moth_0868
            MGE: MG_210(lspa)
            MPN: MPN293(lsp)
            MPU: MYPU_6680(lsp)
            MPE: MYPE1320(lsp)
            MGA: MGA_0997(lspA)
            MMY: MSC_0584(lsp)
            MMO: MMOB3530(lspA)
            MHY: mhp032(lspA)
            MHJ: MHJ_0027(lsp)
            MHP: MHP7448_0031(lsp)
            MSY: MS53_0557
            MCP: MCAP_0394(lspA)
            UUR: UU314(lspA)
            MFL: Mfl388
            MTU: Rv1539(lspA)
            MTC: MT1591(lspA)
            MBO: Mb1566(lspA)
            MBB: BCG_1591(lspA)
            MLE: ML1199(lspA)
            MPA: MAP1250(lspA)
            MAV: MAV_3231(lspA)
            MSM: MSMEG_3174
            MVA: Mvan_2773
            MGI: Mflv_3640
            MMC: Mmcs_3093
            MKM: Mkms_3153
            MJL: Mjls_3113
            CGL: NCgl2058(cgl2139)
            CGB: cg2347(lspA)
            CEF: CE2033
            CDI: DIP1584
            CJK: jk0765(lspA)
            NFA: nfa17880(lspA) pnf1340
            RHA: RHA1_ro01073
            SCO: SCO2074(SC4A10.07c)
            SMA: SAV6132
            TWH: TWT512(lpsA)
            TWS: TW250(lspA)
            LXX: Lxx15175(lspA)
            CMI: CMM_2058(lspA)
            ART: Arth_4208 Arth_4308 Arth_4429 Arth_4477
            AAU: AAur_1719(lspA) AAur_pTC10187(lspA) AAur_pTC20032(lspA)
            PAC: PPA0767
            TFU: Tfu_1122
            FRA: Francci3_1425
            FAL: FRAAL2208(lspA)
            SEN: SACE_5824(lspA)
            BLO: BL0122(lspA)
            BAD: BAD_1132(lspA)
            RXY: Rxyl_2818
            FNU: FN0068
            RBA: RB10374(lspA)
            CTR: CT408(lspA)
            CTA: CTA_0443(lspA)
            CMU: TC0688
            CPN: CPn0535(lspA)
            CPA: CP0217
            CPJ: CPj0535(lspA)
            CPT: CpB0556
            CCA: CCA00210(lspA)
            CAB: CAB205
            CFE: CF0797(lspA)
            PCU: pc1797(lspA)
            BBU: BB0469(lsp)
            BGA: BG0482(lsp)
            BAF: BAPKO_0498(lsp)
            TPA: TP0978
            TDE: TDE2615(lspA)
            LIL: LA1336(lspA)
            LIC: LIC12389(lspA)
            LBJ: LBJ_2262(lspA)
            LBL: LBL_0845(lspA)
            SYN: slr1366(lspA)
            SYW: SYNW1079
            SYC: syc2365_d(lspA)
            SYF: Synpcc7942_1726
            SYD: Syncc9605_1211
            SYE: Syncc9902_1258
            SYG: sync_1561(lspA)
            SYR: SynRCC307_1289(lspA)
            SYX: SynWH7803_1340(lspA)
            CYA: CYA_1533(lspA)
            CYB: CYB_0541(lspA)
            TEL: tlr2420
            GVI: glr0072
            ANA: alr4577
            AVA: Ava_2475(lspA)
            PMA: Pro1032(lspA)
            PMM: PMM0915
            PMT: PMT0595
            PMN: PMN2A_0146
            PMI: PMT9312_0885
            PMB: A9601_09461(lspA)
            PMC: P9515_09981(lspA)
            PMF: P9303_16531(lspA)
            PMH: P9215_09761(lspA)
            PME: NATL1_07781(lspA)
            TER: Tery_3531
            BTH: BT_0808
            BFR: BF2277
            BFS: BF2369
            PGI: PG1598
            SRU: SRU_0404(lspA)
            CHU: CHU_3677(lspA)
            GFO: GFO_1205 GFO_3180(lspA)
            FPS: FP0219(lspA)
            CTE: CT1810(lspA)
            CCH: Cag_1346
            PLT: Plut_0482
            DET: DET1374(lspA)
            DEH: cbdb_A1327(lspA)
            DRA: DR_2388
            DGE: Dgeo_2249 Dgeo_2580
            TTH: TTC1963
            TTJ: TTHA0043
            AAE: aq_1837(lsp)
            TMA: TM0463
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.36
            ExPASy - ENZYME nomenclature database: 3.4.23.36
            ExplorEnz - The Enzyme Database: 3.4.23.36
            ERGO genome analysis and discovery system: 3.4.23.36
            BRENDA, the Enzyme Database: 3.4.23.36
            CAS: 171715-14-3
///
ENTRY       EC 3.4.23.37      Obsolete  Enzyme
NAME        Transferred to 3.4.21.100
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
COMMENT     Transferred entry: now EC 3.4.21.100, pseudomonalisin (EC 3.4.23.37
            created 1995)
STRUCTURES  PDB: 1GA1  1GA4  1GA6  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.37
            ExPASy - ENZYME nomenclature database: 3.4.23.37
            ExplorEnz - The Enzyme Database: 3.4.23.37
            ERGO genome analysis and discovery system: 3.4.23.37
            BRENDA, the Enzyme Database: 3.4.23.37
///
ENTRY       EC 3.4.23.38                Enzyme
NAME        plasmepsin I;
            aspartic hemoglobinase I;
            PFAPG;
            malaria aspartic hemoglobinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Hydrolysis of the -Phe33!Leu- bond in the alpha-chain of hemoglobin,
            leading to denaturation of the molecule
COMMENT     Known from the malaria organism, Plasmodium. About 37 kDa. In
            peptidase family A1 (pepsin A family), closest to cathepsin D and
            renin in structure. Inhibited by pepstatin. Formerly included in EC
            3.4.23.6
REFERENCE   1  [PMID:2007860]
  AUTHORS   Goldberg DE, Slater AF, Beavis R, Chait B, Cerami A, Henderson GB.
  TITLE     Hemoglobin degradation in the human malaria pathogen Plasmodium
            falciparum: a catabolic pathway initiated by a specific aspartic
            protease.
  JOURNAL   J. Exp. Med. 173 (1991) 961-9.
  ORGANISM  Plasmodium falciparum [GN:pfa]
REFERENCE   2  [PMID:8313875]
  AUTHORS   Francis SE, Gluzman IY, Oksman A, Knickerbocker A, Mueller R, Bryant
            ML, Sherman DR, Russell DG, Goldberg DE.
  TITLE     Molecular characterization and inhibition of a Plasmodium falciparum
            aspartic hemoglobinase.
  JOURNAL   EMBO. J. 13 (1994) 306-17.
  ORGANISM  Plasmodium falciparum [GN:pfa]
REFERENCE   3  [PMID:8163662]
  AUTHORS   Gluzman IY, Francis SE, Oksman A, Smith CE, Duffin KL, Goldberg DE.
  TITLE     Order and specificity of the Plasmodium falciparum hemoglobin
            degradation pathway.
  JOURNAL   J. Clin. Invest. 93 (1994) 1602-8.
  ORGANISM  Plasmodium falciparum [GN:pfa]
ORTHOLOGY   KO: K06007  plasmepsin I
GENES       PFA: PF14_0076
            TET: TTHERM_00106950
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.38
            ExPASy - ENZYME nomenclature database: 3.4.23.38
            ExplorEnz - The Enzyme Database: 3.4.23.38
            ERGO genome analysis and discovery system: 3.4.23.38
            BRENDA, the Enzyme Database: 3.4.23.38
            CAS: 180189-87-1
///
ENTRY       EC 3.4.23.39                Enzyme
NAME        plasmepsin II;
            aspartic hemoglobinase II;
            PFAPD
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Hydrolysis of the bonds linking certain hydrophobic residues in
            hemoglobin or globin. Also cleaves the small molecule substrates
            such as Ala-Leu-Glu-Arg-Thr-Phe!Phe(NO2)-Ser-Phe-Pro-Thr [3]
COMMENT     Known from the malaria organism, Plasmodium. About 37 kDa. In
            peptidase family A1 (pepsin A family), and is 73% identical in
            sequence to plasmepsin I. Inhibited by pepstatin. Formerly included
            in EC 3.4.23.6
REFERENCE   1  [PMID:7935597]
  AUTHORS   Dame JB, Reddy GR, Yowell CA, Dunn BM, Kay J, Berry C.
  TITLE     Sequence, expression and modeled structure of an aspartic proteinase
            from the human malaria parasite Plasmodium falciparum.
  JOURNAL   Mol. Biochem. Parasitol. 64 (1994) 177-90.
  ORGANISM  Plasmodium falciparum [GN:pfa]
REFERENCE   2  [PMID:8163662]
  AUTHORS   Gluzman IY, Francis SE, Oksman A, Smith CE, Duffin KL, Goldberg DE.
  TITLE     Order and specificity of the Plasmodium falciparum hemoglobin
            degradation pathway.
  JOURNAL   J. Clin. Invest. 93 (1994) 1602-8.
  ORGANISM  Plasmodium falciparum [GN:pfa]
REFERENCE   3  [PMID:7925966]
  AUTHORS   Hill J, Tyas L, Phylip LH, Kay J, Dunn BM, Berry C.
  TITLE     High level expression and characterisation of Plasmepsin II, an
            aspartic proteinase from Plasmodium falciparum.
  JOURNAL   FEBS. Lett. 352 (1994) 155-8.
  ORGANISM  Plasmodium falciparum [GN:pfa]
ORTHOLOGY   KO: K06008  plasmepsin II
GENES       PFA: PF14_0077
STRUCTURES  PDB: 1LEE  1LF2  1LF3  1LF4  1M43  1ME6  1PFZ  1SME  1W6H  1W6I  
                 1XDH  1XE5  1XE6  2BJU  2IGX  2IGY  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.39
            ExPASy - ENZYME nomenclature database: 3.4.23.39
            ExplorEnz - The Enzyme Database: 3.4.23.39
            ERGO genome analysis and discovery system: 3.4.23.39
            BRENDA, the Enzyme Database: 3.4.23.39
            CAS: 159447-18-4
///
ENTRY       EC 3.4.23.40                Enzyme
NAME        phytepsin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and
            P1', but also cleaves -Phe!Asp- and -Asp!Asp- bonds in 2S albumin
            from plant seeds
COMMENT     Known particularly from barley grain, but present in other plants
            also. In peptidase family A1 (pepsin A family), but structurally
            distinct in containing an internal region of about 100 amino acids
            not generally present in the family
REFERENCE   1  [PMID:1722454]
  AUTHORS   Runeberg-Roos P, Tormakangas K, Ostman A.
  TITLE     Primary structure of a barley-grain aspartic proteinase. A plant
            aspartic proteinase resembling mammalian cathepsin D.
  JOURNAL   Eur. J. Biochem. 202 (1991) 1021-7.
  ORGANISM  Hordeum vulgare [GN:ehvu]
REFERENCE   2  [PMID:7763475]
  AUTHORS   Kervinen J, Sarkkinen P, Kalkkinen N, Mikola L, Saarma M.
  TITLE     Hydrolytic specificity of the barley grain aspartic proteinase.
  JOURNAL   Phytochemistry. 32 (1993) 799-803.
  ORGANISM  Hordeum vulgare [GN:ehvu]
REFERENCE   3  [PMID:7556174]
  AUTHORS   Asakura T, Watanabe H, Abe K, Arai S.
  TITLE     Rice aspartic proteinase, oryzasin, expressed during seed ripening
            and germination, has a gene organization distinct from those of
            animal and microbial aspartic proteinases.
  JOURNAL   Eur. J. Biochem. 232 (1995) 77-83.
  ORGANISM  Oryza sativa [GN:eosa]
REFERENCE   4  [PMID:8540324]
  AUTHORS   Kervinen J, Tormakangas K, Runeberg-Roos P, Guruprasad K, Blundell
            T, Teeri TH.
  TITLE     Structure and possible function of aspartic proteinases in barley
            and other plants.
  JOURNAL   Adv. Exp. Med. Biol. 362 (1995) 241-54.
  ORGANISM  Hordeum vulgare [GN:ehvu]
ORTHOLOGY   KO: K08245  phytepsin
GENES       ATH: AT1G11910 AT1G62290 AT4G04460
STRUCTURES  PDB: 1QDM  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.40
            ExPASy - ENZYME nomenclature database: 3.4.23.40
            ExplorEnz - The Enzyme Database: 3.4.23.40
            ERGO genome analysis and discovery system: 3.4.23.40
            BRENDA, the Enzyme Database: 3.4.23.40
            CAS: 78169-47-8
///
ENTRY       EC 3.4.23.41                Enzyme
NAME        yapsin 1;
            yeast aspartic protease 3;
            Yap3 gene product (Saccharomyces cerevisiae)
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Hydrolyses various precursor proteins with Arg or Lys in P1, and
            commonly Arg or Lys also in P2. The P3 amino acid is usually
            non-polar, but otherwise additional basic amino acids are favourable
            in both non-prime and prime positions
COMMENT     In peptidase family A1 of pepsin, and weakly inhibited by pepstatin.
            Can partially substitute for kexin in a deficient strain of yeast.
            The homologous product of the Mkc7 gene (Saccharomyces cerevisiae)
            has similar catalytic activity and has been termed yapsin 2 [2]
REFERENCE   1  [PMID:8626758]
  AUTHORS   Cawley NX, Chen HC, Beinfeld MC, Loh YP.
  TITLE     Specificity and kinetic studies on the cleavage of various
            prohormone mono- and paired-basic residue sites by yeast aspartic
            protease 3.
  JOURNAL   J. Biol. Chem. 271 (1996) 4168-76.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2
  AUTHORS   Fuller, R.S.
  TITLE     Yapsin 2.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Academic Press, London, 1998, p.
            908-909.
REFERENCE   3  [PMID:9485427]
  AUTHORS   Olsen V, Guruprasad K, Cawley NX, Chen HC, Blundell TL, Loh YP.
  TITLE     Cleavage efficiency of the novel aspartic protease yapsin 1 (Yap3p)
            enhanced for substrates with arginine residues flanking the P1 site:
            correlation with electronegative active-site pockets predicted by
            molecular modeling.
  JOURNAL   Biochemistry. 37 (1998) 2768-77.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K06009  yapsin 1
GENES       SCE: YDR144C(MKC7) YLR120C(YPS1)
            AGO: AGOS_AGL192W
            PIC: PICST_68459
            CGR: CAGL0M04191g
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.41
            ExPASy - ENZYME nomenclature database: 3.4.23.41
            ExplorEnz - The Enzyme Database: 3.4.23.41
            ERGO genome analysis and discovery system: 3.4.23.41
            BRENDA, the Enzyme Database: 3.4.23.41
            CAS: 205132-58-7
///
ENTRY       EC 3.4.23.42                Enzyme
NAME        thermopsin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Similar in specificity to pepsin A preferring bulky hydrophobic
            amino acids in P1 and P1'
INHIBITOR   Pepstatin [CPD:C00773]
COMMENT     From the thermophilic archeaon Sulfolobus acidocaldarius. Maximally
            active at pH 2 and 90 _degree_C. Weakly inhibited by pepstatin but
            shows no sequence similarity to pepsin. Type example of peptidase
            family A5.
REFERENCE   1  [PMID:7674919]
  AUTHORS   Lin X, Tang J.
  TITLE     Thermopsin.
  JOURNAL   Methods. Enzymol. 248 (1995) 156-68.
ORTHOLOGY   KO: K01385  thermopsin
GENES       PTO: PTO0161 PTO1487
            SSO: SSO1886 SSO2037 SSO2194
            SAI: Saci_1534 Saci_1714(thpS) Saci_2170
            MSE: Msed_1018 Msed_1230 Msed_1460
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.42
            ExPASy - ENZYME nomenclature database: 3.4.23.42
            ExplorEnz - The Enzyme Database: 3.4.23.42
            ERGO genome analysis and discovery system: 3.4.23.42
            BRENDA, the Enzyme Database: 3.4.23.42
            CAS: 126125-05-1
///
ENTRY       EC 3.4.23.43                Enzyme
NAME        prepilin peptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Typically cleaves a -Gly!Phe- bond to release an N-terminal, basic
            peptide of 5-8 residues from type IV prepilin, and then N-methylates
            the new N-terminal amino group, the methyl donor being
            S-adenosyl-L-methionine
COMMENT     Many species of bacteria carry pili on their cell surfaces. These
            are virulence determinants in pathogenic strains, and are assembled
            biosynthetically from type IV prepilin subunits. Before assembly,
            the prepilin molecules require proteolytic processing, which is done
            by the prepilin peptidase. Prepilin peptidase and its homologues
            play a central role not only in type IV pilus biogenesis but also in
            transport of macromolecules across cell membranes. Although both
            peptide-bond hydrolysis and N-methylation are catalysed by the same
            molecule, the methylation can be inhibited without affecting
            peptidase activity, and it is believed that the enzyme has two
            separate catalytic sites. Type example of peptidase family A24.
REFERENCE   1  [PMID:9224881]
  AUTHORS   Lory S, Strom MS.
  TITLE     Structure-function relationship of type-IV prepilin peptidase of
            Pseudomonas aeruginosa--a review.
  JOURNAL   Gene. 192 (1997) 117-21.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   2  [PMID:10625704]
  AUTHORS   LaPointe CF, Taylor RK.
  TITLE     The type 4 prepilin peptidases comprise a novel family of aspartic
            acid proteases.
  JOURNAL   J. Biol. Chem. 275 (2000) 1502-10.
  ORGANISM  Vibrio cholerae [GN:vch]
PATHWAY     PATH: map03090  Type II secretion system
ORTHOLOGY   KO: K02236  leader peptidase (prepilin peptidase) /
                        N-methyltransferase
            KO: K02278  prepilin peptidase CpaA
            KO: K02464  general secretion pathway protein O
            KO: K02506  leader peptidase HopD
            KO: K02654  leader peptidase (prepilin peptidase) /
                        N-methyltransferase
            KO: K06010  
GENES       ECO: b2972(pppA) b3335(gspO)
            ECJ: JW2939(pppA) JW3297(gspO)
            ECE: Z4693(hopD)
            ECS: ECs4188
            ECC: c4106(hofD)
            ECI: UTI89_C3388(pppA) UTI89_C3790(hofD)
            ECV: APECO1_3117(hofD) APECO1_3455(pppA)
            ECX: EcHS_A3529(gspO)
            STY: STY4356(hopD)
            STT: t4063(hopD)
            SPT: SPA3308(hopD)
            SEC: SC3376(hopD)
            STM: STM3442(hopD)
            YPE: YPO0806
            YPK: y3195
            YPM: YP_2850(pppA1)
            YPA: YPA_0463
            YPN: YPN_3010
            YPP: YPDSF_0703
            YPS: YPTB3055
            YEN: YE3499 YE3574(yst1O)
            SFL: SF3354(hopD)
            SFV: SFV_3341(hopD)
            ECA: ECA0787 ECA3098(outO)
            PLU: plu1733
            SPE: Spro_4241
            HIN: HI0296(hopD)
            HIT: NTHI0406(pilD)
            HDU: HD1126
            HSO: HS_0458(pilD)
            PMU: PM0087(hopD)
            MSU: MS0360(pppA)
            APL: APL_0877(apfD)
            XFA: XF2537
            XFT: PD1922(pilD)
            XCC: XCC3101(pilD)
            XCB: XC_1056
            XCV: XCV3355(pilD)
            XAC: XAC3243(pilD)
            XOO: XOO1584(pilD)
            XOM: XOO_1466(XOO1466)
            VCH: VC0839(tcpJ) VC2426(pilD)
            VVU: VV1_1623 VV1_1746
            VVY: VV2663 VV2781
            VPA: VP2422 VP2526
            VFI: VF2188
            PPR: PBPRA3203(pilD)
            PAE: PA4528(pilD)
            PAU: PA14_58770(pilD)
            PPU: PP_0632(pilD)
            PPF: Pput_0673
            PST: PSPTO_0924(pilD)
            PSB: Psyr_0796
            PSP: PSPPH_0818(pilD)
            PFL: PFL_5289(pilD)
            PFO: Pfl_4822
            PEN: PSEEN4668(pilD)
            PMY: Pmen_0773
            PAR: Psyc_0062(pilD)
            PCR: Pcryo_0067
            ACI: ACIAD0360(pilD)
            SON: SO_0414(pilD)
            SDN: Sden_3391
            SFR: Sfri_3785
            SAZ: Sama_0367
            SBL: Sbal_3921
            SBM: Shew185_3944
            SLO: Shew_3440
            SPC: Sputcn32_3425
            SSE: Ssed_0423
            SPL: Spea_0411
            SHE: Shewmr4_0418
            SHM: Shewmr7_3607
            SHN: Shewana3_0417
            SHW: Sputw3181_0514
            ILO: IL0450(pulO)
            CPS: CPS_4449(pilD)
            PHA: PSHAa0380(pilD)
            PAT: Patl_3342
            SDE: Sde_0861
            PIN: Ping_3325
            MAQ: Maqu_2683
            CBU: CBU_0153(pilD)
            LPN: lpg1524(pilD)
            LPF: lpl1502(pilD)
            LPP: lpp1481(pilD)
            MCA: MCA2094(pilD)
            FTU: FTT0683c(pilD)
            FTF: FTF0683c(pilD)
            FTL: FTL_0959
            FTH: FTH_0937(pulO)
            FTN: FTN_1000(pilD)
            TCX: Tcr_1391
            NOC: Noc_0310
            AEH: Mlg_2081
            HHA: Hhal_2022
            HCH: HCH_05280
            CSA: Csal_2176
            ABO: ABO_0612(pilD)
            AHA: AHA_3871(gspO)
            NME: NMB0332
            NMA: NMA2156(pilD)
            NGO: NGO1670(pilD)
            CVI: CV_3826
            RSO: RSc0657(cpaA1) RSc2827(pilD) RSp1091(cpaA2)
            REU: Reut_A2641 Reut_A2962 Reut_B5406
            REH: H16_A0720(cpaA1) H16_A3257(pilD) H16_B0182(cpaA2)
            RME: Rmet_0650 Rmet_3110
            BMA: BMA1293 BMA2533(pilD)
            BXE: Bxe_A0502 Bxe_A2801
            BVI: Bcep1808_0551
            BUR: Bcep18194_A3661 Bcep18194_A4658 Bcep18194_B2059
                 Bcep18194_C7204
            BCN: Bcen_0094 Bcen_1038 Bcen_5501
            BCH: Bcen2424_0576 Bcen2424_1518 Bcen2424_6787
            BAM: Bamb_0479 Bamb_1400 Bamb_3419
            BPS: BPSL1820 BPSL1898 BPSL3010(gspO) BPSS2187
            BPM: BURPS1710b_1938 BURPS1710b_2038 BURPS1710b_3529
                 BURPS1710b_A1308(cpaA1)
            BTE: BTH_I1134(pilD) BTH_I2461 BTH_I2545 BTH_II2265
            BPE: BP3818
            BPA: BPP3962
            BBR: BB0792(gspO) BB4435
            RFR: Rfer_0790 Rfer_2904
            POL: Bpro_0843 Bpro_2546
            PNA: Pnap_0768
            AAV: Aave_3682
            AJS: Ajs_0803
            VEI: Veis_3921
            MPT: Mpe_A0507(pilD) Mpe_B0304
            HAR: HEAR2791(pilD)
            MMS: mma_2998
            NEU: NE0597(pilD)
            NET: Neut_1044
            NMU: Nmul_A2131 Nmul_A2362
            EBA: ebA3718 ebA4343(pilD)
            AZO: azo3236(pilD)
            DAR: Daro_0637
            TBD: Tbd_2368(pilD)
            MFA: Mfla_2225
            WSU: WS0674
            TDN: Tmden_0996
            CJE: Cj0825
            CJR: CJE0912
            CJU: C8J_0772
            ABU: Abu_2201
            GSU: GSU2043(pilD)
            GME: Gmet_0959
            PCA: Pcar_1745 Pcar_2139
            PPD: Ppro_0800 Ppro_0982
            DVU: DVU1263(pppA) DVU2117
            DDE: Dde_2358
            BBA: Bd0862(pilD)
            DPS: DP1537 DP3017
            ADE: Adeh_0637 Adeh_2830
            MXA: MXAN_5779(gspO)
            SFU: Sfum_0214 Sfum_1491
            PUB: SAR11_0065(pilD)
            MLO: mll6828 mlr5594
            MES: Meso_0610 Meso_4094
            SME: SMa1578(cpaA2) SMc04113(cpaA1)
            ATU: Atu0223(ctpB)
            ATC: AGR_C_382(cpaA)
            RET: RHE_CH00203(cpaA)
            RLE: RL0212(cpaA) pRL110566
            BJA: bll1441(ctpB) blr3491 blr6023
            BRA: BRADO6338
            BBT: BBta_1288
            RPA: RPA3676
            RPB: RPB_1786
            RPC: RPC_3012 RPC_3711
            RPD: RPD_3518
            RPE: RPE_2668 RPE_3749
            NWI: Nwi_0303
            NHA: Nham_0731
            CCR: CC_0184 CC_2947(cpaA)
            SIL: SPO3095
            SIT: TM1040_2354
            RSP: RSP_1900
            JAN: Jann_0989
            MMR: Mmar10_0417
            HNE: HNE_2653(gspO) HNE_3016
            NAR: Saro_1081 Saro_1526 Saro_2305
            SAL: Sala_0326 Sala_1131 Sala_2766
            ELI: ELI_01530(cpaA)
            RRU: Rru_A0108
            MAG: amb3739
            MGM: Mmc1_0021
            ABA: Acid345_1591
            BSU: BG10323(comC)
            BHA: BH3035(comC)
            BAN: BA1318(comC)
            BAR: GBAA1318(comC)
            BAA: BA_1844
            BAT: BAS1219(comC)
            BCE: BC1306
            BCA: BCE_1419(comC)
            BCZ: BCZK1199(comC)
            BTK: BT9727_1197(comC)
            BLI: BL00633(comC)
            BLD: BLi02936(comC)
            BCL: ABC2619(comC)
            BAY: RBAM_025120(comC)
            OIH: OB0617
            GKA: GK2625
            SAU: SA1486
            SAV: SAV1661
            SAM: MW1605
            SAR: SAR1741
            SAS: SAS1590
            SAC: SACOL1708
            SAB: SAB1522c
            SAA: SAUSA300_1609
            SAO: SAOUHSC_01764
            SEP: SE1337
            SER: SERP1226
            SHA: SH1265
            SSP: SSP1104
            LMO: lmo1550(comC)
            LMF: LMOf2365_1570
            LIN: lin1585(comC)
            LWE: lwe1563
            LLA: L0332(comC)
            LLC: LACR_2312
            LLM: llmg_2304(comC)
            SPY: SPy_1532
            SPM: spyM18_1549
            SPG: SpyM3_1183
            SPS: SPs0679
            SPA: M6_Spy1281
            SPB: M28_Spy1199
            SPN: SP_1808
            SPR: spr1628(pilD)
            SAG: SAG0469
            SAN: gbs0516
            SAK: SAK_0571
            SMU: SMU.539c
            STC: str0722(pilD)
            STL: stu0722(pilD)
            SSA: SSA_0642(pilD) SSA_2302
            LPL: lp_1023
            LJO: LJ0334
            LAC: LBA0286
            LSA: LSA1771
            LGA: LGAS_0286
            EFA: EF3236
            STH: STH1951
            CAC: CAC2784
            CPE: CPE2287
            CTC: CTC02411(pilD)
            CHY: CHY_0634(pilD)
            DSY: DSY0061 DSY2382
            TTE: TTE1266(pppA)
            MTA: Moth_1550
            SCO: SCO4549(SCD16A.34c)
            SMA: SAV4824
            FRA: Francci3_3210
            FAL: FRAAL5248
            LIC: LIC12423(pilD)
            LBJ: LBJ_1030
            LBL: LBL_2004
            SYN: slr1120(pilD)
            SYW: SYNW0787
            SYC: syc2159_d(pilD)
            SYF: Synpcc7942_1935
            SYG: sync_1709(gspO)
            CYA: CYA_1318(gspO)
            CYB: CYB_0909(gspO)
            TEL: tll0476(pilD)
            GVI: glr2433(pilD)
            ANA: alr1315(pilD)
            AVA: Ava_2985
            PMA: Pro0860(pulO)
            PMT: PMT0533
            PMI: PMT9312_1186
            PMF: P9303_17321
            PMG: P9301_06881
            TER: Tery_2683
            DET: DET1362
            DEH: cbdb_A1313
            DRA: DR_2065
            DGE: Dgeo_0374
            TTH: TTC1716(pilD)
            TTJ: TTHA0269
            AAE: aq_1601(pilD)
            TMA: TM1696
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.43
            ExPASy - ENZYME nomenclature database: 3.4.23.43
            ExplorEnz - The Enzyme Database: 3.4.23.43
            ERGO genome analysis and discovery system: 3.4.23.43
            BRENDA, the Enzyme Database: 3.4.23.43
///
ENTRY       EC 3.4.23.44                Enzyme
NAME        nodavirus endopeptidase;
            Black Beetle virus endopeptidase;
            Flock House virus endopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Hydrolysis of an asparaginyl bond involved in the maturation of the
            structural protein of the virus, typically -Asn!Ala- or -Asn!Phe-
COMMENT     A single aspartic residue is critical for activity, and inhibition
            by EDTA indicates that a metal ion is also important. The enzyme is
            known from several nodaviruses that are pathogens of insects. Type
            example of peptidase family A6, and structurally related to the
            tetravirus endopeptidase in family A21, although in that family, the
            catalytic residue is thought to be Glu.
REFERENCE   1  [PMID:8175803]
  AUTHORS   Zlotnick A, Reddy VS, Dasgupta R, Schneemann A, Ray WJ Jr, Rueckert
            RR, Johnson JE.
  TITLE     Capsid assembly in a family of animal viruses primes an
            autoproteolytic maturation that depends on a single aspartic acid
            residue.
  JOURNAL   J. Biol. Chem. 269 (1994) 13680-4.
  ORGANISM  black beetle virus, Flock House virus
REFERENCE   2
  AUTHORS   Johnson, J.E. and Schneemann, A.
  TITLE     Nodavirus endopeptidase.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Handbook of Proteolytic Enzymes,
            London, 1998, p. 964-967.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.44
            ExPASy - ENZYME nomenclature database: 3.4.23.44
            ExplorEnz - The Enzyme Database: 3.4.23.44
            ERGO genome analysis and discovery system: 3.4.23.44
            BRENDA, the Enzyme Database: 3.4.23.44
///
ENTRY       EC 3.4.23.45                Enzyme
NAME        memapsin 1;
            beta-secretase;
            beta-site Alzheimer's amyloid precursor protein cleaving enzyme 2
            (BACE2);
            ASP1;
            Down region aspartic protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Broad endopeptidase specificity. Cleaves
            Glu-Val-Asn-Leu!Asp-Ala-Glu-Phe in the Swedish variant of
            Alzheimer's amyloid precursor protein
COMMENT     Can cleave beta-amyloid precursor protein to form the amyloidogenic
            beta-peptide that is implicated in the pathology of Alzheimer's
            disease, but is not significantly expressed in human brain. In
            peptidase family A1, but is atypical in containing a C-terminal
            membrane-spanning domain.
REFERENCE   1  [PMID:12093293]
  AUTHORS   Turner RT 3rd, Loy JA, Nguyen C, Devasamudram T, Ghosh AK, Koelsch
            G, Tang J.
  TITLE     Specificity of memapsin 1 and its implications on the design of
            memapsin 2 (beta-secretase) inhibitor selectivity.
  JOURNAL   Biochemistry. 41 (2002) 8742-6.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map05010  Alzheimer's disease
ORTHOLOGY   KO: K07747  beta-site APP-cleaving enzyme 2 (memapsin 1)
GENES       HSA: 25825(BACE2)
            MMU: 56175(Bace2)
            RNO: 288227(Bace2)
            CFA: 478418(BACE2)
            BTA: 534774(LOC534774)
            GGA: 418526(BACE2)
            XLA: 380307(bace2)
STRUCTURES  PDB: 2EWY  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.45
            ExPASy - ENZYME nomenclature database: 3.4.23.45
            ExplorEnz - The Enzyme Database: 3.4.23.45
            ERGO genome analysis and discovery system: 3.4.23.45
            BRENDA, the Enzyme Database: 3.4.23.45
///
ENTRY       EC 3.4.23.46                Enzyme
NAME        memapsin 2;
            beta-secretase;
            beta-site Alzheimer's amyloid precursor protein cleaving enzyme 1
            (BACE1)
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Broad endopeptidase specificity. Cleaves
            Glu-Val-Asn-Leu!Asp-Ala-Glu-Phe in the Swedish variant of
            Alzheimer's amyloid precursor protein
COMMENT     Suggested to be the major "beta-secretase" responsible for the
            cleavage of the beta-amyloid precursor protein to form the
            amyloidogenic beta-peptide that is implicated in the pathology of
            Alzheimer's disease. In peptidase family A1 but is atypical in
            containing a C-terminal membrane-spanning domain.
REFERENCE   1  [PMID:11513577]
  AUTHORS   Turner RT 3rd, Koelsch G, Hong L, Castanheira P, Ermolieff J, Ghosh
            AK, Tang J.
  TITLE     Subsite specificity of memapsin 2 (beta-secretase): implications for
            inhibitor design.
  JOURNAL   Biochemistry. 40 (2001) 10001-6.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:12206667]
  AUTHORS   Hong L, Turner RT 3rd, Koelsch G, Shin D, Ghosh AK, Tang J.
  TITLE     Crystal structure of memapsin 2 (beta-secretase) in complex with an
            inhibitor OM00-3.
  JOURNAL   Biochemistry. 41 (2002) 10963-7.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map05010  Alzheimer's disease
ORTHOLOGY   KO: K04521  beta-site APP-cleaving enzyme 1 (memapsin 2)
GENES       HSA: 23621(BACE1)
            PTR: 451573(BACE1)
            MMU: 23821(Bace1)
            RNO: 29392(Bace1)
            CFA: 489390(BACE1)
            BTA: 614333(BACE1)
            GGA: 419768(BACE1)
            DRE: 403005(zgc:77409)
            SPU: 585631(LOC585631)
STRUCTURES  PDB: 1SGZ  1TQF  1W50  1W51  1XN2  1XN3  1XS7  1YM2  1YM4  2B8L  
                 2B8V  2F3E  2F3F  2FDP  2G94  2HIZ  2HM1  2IQG  2IRZ  2IS0  
                 2OAH  2OF0  2OHK  2OHL  2OHM  2OHN  2OHP  2OHQ  2OHR  2OHS  
                 2OHT  2OHU  2P4J  2P83  2P8H  2PH6  2Q11  2Q15  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.46
            ExPASy - ENZYME nomenclature database: 3.4.23.46
            ExplorEnz - The Enzyme Database: 3.4.23.46
            ERGO genome analysis and discovery system: 3.4.23.46
            BRENDA, the Enzyme Database: 3.4.23.46
///
ENTRY       EC 3.4.23.47                Enzyme
NAME        HIV-2 retropepsin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Endopeptidase for which the P1 residue is preferably hydrophobic
COMMENT     In peptidase family A2. Responsible for the post-translational
            processing of the human immunodeficiency virus polyprotein.
REFERENCE   1  [PMID:2015912]
  AUTHORS   Tozser J, Blaha I, Copeland TD, Wondrak EM, Oroszlan S.
  TITLE     Comparison of the HIV-1 and HIV-2 proteinases using oligopeptide
            substrates representing cleavage sites in Gag and Gag-Pol
            polyproteins.
  JOURNAL   FEBS. Lett. 281 (1991) 77-80.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:7929352]
  AUTHORS   Chen Z, Li Y, Chen E, Hall DL, Darke PL, Culberson C, Shafer JA, Kuo
            LC.
  TITLE     Crystal structure at 1.9-A resolution of human immunodeficiency
            virus (HIV) II protease complexed with L-735,524, an orally
            bioavailable inhibitor of the HIV proteases.
  JOURNAL   J. Biol. Chem. 269 (1994) 26344-8.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.47
            ExPASy - ENZYME nomenclature database: 3.4.23.47
            ExplorEnz - The Enzyme Database: 3.4.23.47
            ERGO genome analysis and discovery system: 3.4.23.47
            BRENDA, the Enzyme Database: 3.4.23.47
///
ENTRY       EC 3.4.23.48                Enzyme
NAME        plasminogen activator Pla
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Converts human Glu-plasminogen to plasmin by cleaving the Arg560!Val
            peptide bond that is also hydrolysed by the mammalian u-plasminogen
            activator and t-plasminogen activator. Also cleaves arginyl bonds in
            other proteins
COMMENT     In peptidase family A26. From the bacterium Yersinia pestis that
            causes plague.
REFERENCE   1  [PMID:11401715]
  AUTHORS   Kukkonen M, Lahteenmaki K, Suomalainen M, Kalkkinen N, Emody L, Lang
            H, Korhonen TK.
  TITLE     Protein regions important for plasminogen activation and
            inactivation of alpha2-antiplasmin in the surface protease Pla of
            Yersinia pestis.
  JOURNAL   Mol. Microbiol. 40 (2001) 1097-111.
  ORGANISM  Yersinia pestis
ORTHOLOGY   KO: K08566  plasminogen activator
GENES       YPE: YPO1231(pla2) YPPCP1.07(pla)
            YPM: YP_0910(pla2) YP_pPCP08(pla)
            YPA: YPA_0944 YPA_PCP0005
            YPN: YPN_2748 YPN_PCP0005
            YPP: YPDSF_2465
            ENT: Ent638_1900
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.48
            ExPASy - ENZYME nomenclature database: 3.4.23.48
            ExplorEnz - The Enzyme Database: 3.4.23.48
            ERGO genome analysis and discovery system: 3.4.23.48
            BRENDA, the Enzyme Database: 3.4.23.48
///
ENTRY       EC 3.4.23.49                Enzyme
NAME        omptin;
            protease VII;
            protease A;
            gene ompT proteins;
            ompT protease;
            protein a;
            Pla;
            protease VII;
            protease A;
            OmpT
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Aspartic endopeptidases
REACTION    Has a virtual requirement for Arg in the P1 position and a slightly
            less stringent preference for this residue in the P1' position,
            which can also contain Lys, Gly or Val.
COMMENT     A product of the ompT gene of Escherichia coli, and associated with
            the outer membrane. Omptin shows a preference for cleavage between
            consecutive basic amino acids, but is capable of cleavage when P1'
            is a non-basic residue [5,7]. Belongs in peptidase family A26.
REFERENCE   1  [PMID:3278297]
  AUTHORS   Grodberg J, Lundrigan MD, Toledo DL, Mangel WF, Dunn JJ.
  TITLE     Complete nucleotide sequence and deduced amino acid sequence of the
            ompT gene of Escherichia coli K-12.
  JOURNAL   Nucleic. Acids. Res. 16 (1988) 1209.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:3056908]
  AUTHORS   Sugimura K, Nishihara T.
  TITLE     Purification, characterization, and primary structure of Escherichia
            coli protease VII with specificity for paired basic residues:
            identity of protease VII and OmpT.
  JOURNAL   J. Bacteriol. 170 (1988) 5625-32.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:1603076]
  AUTHORS   Hanke C, Hess J, Schumacher G, Goebel W.
  TITLE     Processing by OmpT of fusion proteins carrying the HlyA transport
            signal during secretion by the Escherichia coli hemolysin transport
            system.
  JOURNAL   Mol. Gen. Genet. 233 (1992) 42-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4
  AUTHORS   Dekker, N.
  TITLE     Omptin.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, 2nd ed., Elsevier, London, 2004, p.
            212-216.
REFERENCE   5  [PMID:11566868]
  AUTHORS   Vandeputte-Rutten L, Kramer RA, Kroon J, Dekker N, Egmond MR, Gros
            P.
  TITLE     Crystal structure of the outer membrane protease OmpT from
            Escherichia coli suggests a novel catalytic site.
  JOURNAL   EMBO. J. 20 (2001) 5033-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:11576541]
  AUTHORS   Kramer RA, Vandeputte-Rutten L, de Roon GJ, Gros P, Dekker N, Egmond
            MR.
  TITLE     Identification of essential acidic residues of outer membrane
            protease OmpT supports a novel active site.
  JOURNAL   FEBS. Lett. 505 (2001) 426-30.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   7  [PMID:15317797]
  AUTHORS   McCarter JD, Stephens D, Shoemaker K, Rosenberg S, Kirsch JF,
            Georgiou G.
  TITLE     Substrate specificity of the Escherichia coli outer membrane
            protease OmpT.
  JOURNAL   J. Bacteriol. 186 (2004) 5919-25.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01355  omptin
GENES       ECO: b0565(ompT)
            ECJ: JW0554(ompT)
            ECE: Z1931
            ECS: ECs1663
            ECC: c0652(ompT)
            ECI: UTI89_C0566(ompT)
            ECP: ECP_0597
            ECV: APECO1_1482(ompT)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.23.49
            ExPASy - ENZYME nomenclature database: 3.4.23.49
            ExplorEnz - The Enzyme Database: 3.4.23.49
            ERGO genome analysis and discovery system: 3.4.23.49
            BRENDA, the Enzyme Database: 3.4.23.49
            CAS: 150770-86-8
///
ENTRY       EC 3.4.24.1                 Enzyme
NAME        atrolysin A;
            Crotalus atrox metalloendopeptidase a;
            hemorrhagic toxin a;
            Crotalus atrox alpha-proteinase;
            Crotalus atrox proteinase;
            bothropasin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of Asn3!Gln, His5!Leu, His10!Leu, Ala14!Leu and Tyr16!Leu
            in insulin B chain; removes C-terminal Leu from small peptides
COMMENT     A hemorrhagic endopeptidase of 68 kDa, one of six hemorrhagic toxins
            in the venom of western diamondback rattlesnake. The 60 kDa
            hemorrhagic toxin 1 of Crotalus ruber ruber shows identical
            specificity [2]. In peptidase family M12 (astacin family). Related
            metalloendopeptidases from rattlesnake venoms are EC 3.4.24.41
            (atrolysin B), EC 3.4.24.42 (atrolysin C), EC 3.4.24.43 (atroxase),
            EC 3.4.24.44 (atrolysin E), EC 3.4.24.45 (atrolysin F), EC 3.4.24.46
            (adamalysin), EC 3.4.24.47 (horrilysin), and EC 3.4.24.48
            (ruberlysin)
REFERENCE   1  [PMID:210790]
  AUTHORS   Bjarnason JB, Tu AT.
  TITLE     Hemorrhagic toxins from Western diamondback rattlesnake (Crotalus
            atrox) venom: isolation and characterization of five toxins and the
            role of zinc in hemorrhagic toxin e.
  JOURNAL   Biochemistry. 17 (1978) 3395-404.
  ORGANISM  Crotalus atrox
REFERENCE   2  [PMID:2949699]
  AUTHORS   Mori N, Nikai T, Sugihara H, Tu AT.
  TITLE     Biochemical characterization of hemorrhagic toxins with
            fibrinogenase activity isolated from Crotalus ruber ruber venom.
  JOURNAL   Arch. Biochem. Biophys. 253 (1987) 108-21.
  ORGANISM  Crotalus ruber ruber
REFERENCE   3  [PMID:3060135]
  AUTHORS   Bjarnason JB, Hamilton D, Fox JW.
  TITLE     Studies on the mechanism of hemorrhage production by five
            proteolytic hemorrhagic toxins from Crotalus atrox venom.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 369 Suppl (1988) 121-9.
  ORGANISM  Crotalus atrox
REFERENCE   4
  AUTHORS   Bjarnason, J.B. and Fox, J.W.
  TITLE     Hemorrhagic toxins from snake venoms.
  JOURNAL   J. Toxicol. Toxin Rev. (1989) 121-209.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.1
            ExPASy - ENZYME nomenclature database: 3.4.24.1
            ExplorEnz - The Enzyme Database: 3.4.24.1
            ERGO genome analysis and discovery system: 3.4.24.1
            BRENDA, the Enzyme Database: 3.4.24.1
            CAS: 37288-82-7
///
ENTRY       EC 3.4.24.2       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
COMMENT     Deleted entry: Sepia proteinase (EC 3.4.24.2 created 1972, deleted
            1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.2
            ExPASy - ENZYME nomenclature database: 3.4.24.2
            ExplorEnz - The Enzyme Database: 3.4.24.2
            ERGO genome analysis and discovery system: 3.4.24.2
            BRENDA, the Enzyme Database: 3.4.24.2
///
ENTRY       EC 3.4.24.3                 Enzyme
NAME        microbial collagenase;
            Clostridium histolyticum collagenase;
            clostridiopeptidase A;
            collagenase A;
            collagenase I;
            Achromobacter iophagus collagenase;
            collagenase;
            aspergillopeptidase C;
            nucleolysin;
            azocollase;
            metallocollagenase;
            soycollagestin;
            Clostridium histolyticum proteinase A;
            clostridiopeptidase II;
            MMP-8;
            clostridiopeptidase I;
            collagen peptidase;
            collagen protease;
            collagenase MMP-1;
            metalloproteinase-1;
            kollaza;
            matrix metalloproteinase-1;
            MMP-1;
            matrix metalloproteinase-8;
            matirx metalloproteinase-18;
            interstitial collagenase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Digestion of native collagen in the triple helical region at !Gly
            bonds. With synthetic peptides, a preference is shown for Gly at P3
            and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg
            at P3'
COMMENT     Six species of metalloendopeptidase acting on native collagen can be
            isolated from the medium of Clostridium histolyticum. Class I has
            forms alpha (68 kDa), beta (115 kDa) and gamma (79 kDa); class II
            has delta (100 kDa), epsilon (110 kDa) and zeta (125 kDa). The two
            classes are immunologically crossreactive, but have significantly
            different sequences, and different specificities such that their
            actions on collagen are complementary. The enzymes also act as
            peptidyl-tripeptidases. Variants of the enzyme have been purified
            from Bacillus cereus [10], Empedobacter collagenolyticum [4],
            Pseudomonas marinoglutinosa [1], and species of Vibrio, Vibrio B-30
            (ATCC 21250) [2] and V. alginolyticus (previously Achromobacter
            iophagus) [3,8]. Also known from Streptomyces sp. [9]. The Vibrio
            enzyme is the type example of peptidase family M9.
REFERENCE   1
  AUTHORS   Hanada, K., Mizutani, T., Yamagishi, M., Tsuji, H., Misaki, T.
            Sawada, J.
  TITLE     The isolation of collagenase and its enzymological and
            physico-chemical properties.
  JOURNAL   Agric. Biol. Chem. (1973) 1771-1781.
REFERENCE   2  [PMID:210785]
  AUTHORS   Merkel JR, Dreisbach JH.
  TITLE     Purification and characterization of a marine bacterial collagenase.
  JOURNAL   Biochemistry. 17 (1978) 2857-63.
  ORGANISM  Clostridium histolyticum
REFERENCE   3  [PMID:6250633]
  AUTHORS   Heindl MC, Fermandjian S, Keil B.
  TITLE     Circular dichroism comparative studies of two bacterial collagenases
            and thermolysin.
  JOURNAL   Biochim. Biophys. Acta. 624 (1980) 51-9.
  ORGANISM  Clostridium histolyticum, Achromobacter iophagu
REFERENCE   4  [PMID:6530724]
  AUTHORS   Waid DD, Warren RJ, Pence DB.
  TITLE     Elaeophora schneideri Wehr and Dickmans, 1935 in white-tailed deer
            from the Edwards Plateau of Texas.
  JOURNAL   J. Wildl. Dis. 20 (1984) 342-5.
REFERENCE   5  [PMID:6087888]
  AUTHORS   Bond MD, Van Wart HE.
  TITLE     Characterization of the individual collagenases from Clostridium
            histolyticum.
  JOURNAL   Biochemistry. 23 (1984) 3085-91.
  ORGANISM  Clostridium histolyticum
REFERENCE   6  [PMID:6087889]
  AUTHORS   Bond MD, Van Wart HE.
  TITLE     Relationship between the individual collagenases of Clostridium
            histolyticum: evidence for evolution by gene duplication.
  JOURNAL   Biochemistry. 23 (1984) 3092-9.
  ORGANISM  Clostridium histolyticum
REFERENCE   7  [PMID:3002445]
  AUTHORS   Van Wart HE, Steinbrink DR.
  TITLE     Complementary substrate specificities of class I and class II
            collagenases from Clostridium histolyticum.
  JOURNAL   Biochemistry. 24 (1985) 6520-6.
  ORGANISM  Clostridium histolyticum
REFERENCE   8
  AUTHORS   Tong, N.T., Tsugita, A. and Keil-Dlouha, V.
  TITLE     Purification and characterization of two high-molecular-mass forms
            of Achromobacter collagenase.
  JOURNAL   Biochim. Biophys. Acta 874 (1986) 296-304.
  ORGANISM  Vibrio alginolyticus
REFERENCE   9  [PMID:2822678]
  AUTHORS   Endo A, Murakawa S, Shimizu H, Shiraishi Y.
  TITLE     Purification and properties of collagenase from a Streptomyces
            species.
  JOURNAL   J. Biochem. (Tokyo). 102 (1987) 163-70.
  ORGANISM  Streptomyces sp.
REFERENCE   10 [PMID:3040751]
  AUTHORS   Makinen KK, Makinen PL.
  TITLE     Purification and properties of an extracellular collagenolytic
            protease produced by the human oral bacterium Bacillus cereus
            (strain Soc 67).
  JOURNAL   J. Biol. Chem. 262 (1987) 12488-95.
  ORGANISM  Bacillus cereus
ORTHOLOGY   KO: K01387  microbial collagenase
GENES       SGL: SG1493
            VCH: VC1650
            VCO: VC0395_A1256
            VVU: VV2_1146
            VVY: VVA1672
            VPA: VPA0459
            SON: SO_0639
            SAZ: Sama_1077 Sama_1517
            SBL: Sbal_3732
            SBM: Shew185_0630
            SLO: Shew_1685 Shew_2743 Shew_3732
            SSE: Ssed_0039 Ssed_3300
            SPL: Spea_0035 Spea_2754 Spea_2966
            CPS: CPS_1458 CPS_2237
            HCH: HCH_05788
            CVI: CV_1955 CV_2001 CV_3255
            BMA: BMAA0694
            BUR: Bcep18194_C6876
            BPS: BPSS0666
            BPM: BURPS1710b_A2230
            BPL: BURPS1106A_A0900 BURPS1106A_A1142(colA)
            BPD: BURPS668_A0988 BURPS668_A1216(colA)
            BTE: BTH_II1578
            MXA: MXAN_6205
            BAN: BA0555 BA3299 BA3584
            BAR: GBAA0555 GBAA3299 GBAA3584
            BAA: BA_1129 BA_3802 BA_4075
            BAT: BAS0523 BAS3060 BAS3323
            BCE: BC0556 BC2466 BC3009 BC3010 BC3161 BC3412 BC3529 BC3762
                 BC4377
            BCA: BCE_0616 BCE_3539
            BCZ: BCZK0466(colA) BCZK3238(colA) pE33L466_0145(colA)
            BCY: Bcer98_0486
            BTK: BT9727_0466(colA) BT9727_3286(colA)
            BTL: BALH_0495(colA)
            CPE: CPE0173(colA)
            CPF: CPF_0166(colA)
            CPR: CPR_0162(colA)
            CTC: pE88_34(colT)
            CNO: NT01CX_1295
            CBO: CBO1620(colA)
            CBA: CLB_1638
            CBH: CLC_1647
            CBF: CLI_1698
            SCO: SCO5912(SC10A5.17)
            SEN: SACE_3082
            LIL: LA0872(colA)
            LIC: LIC12760
            LBJ: LBJ_0742(colA)
            LBL: LBL_2336(colA)
STRUCTURES  PDB: 1NQD  1NQJ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.3
            ExPASy - ENZYME nomenclature database: 3.4.24.3
            ExplorEnz - The Enzyme Database: 3.4.24.3
            ERGO genome analysis and discovery system: 3.4.24.3
            BRENDA, the Enzyme Database: 3.4.24.3
            CAS: 9001-12-1
///
ENTRY       EC 3.4.24.4       Obsolete  Enzyme
NAME        Transferred to 3.4.24.40
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
COMMENT     Transferred entry: now EC 3.4.24.40 serralysin (EC 3.4.24.4 created
            1972 [EC 3.4.99.13 and EC 3.4.99.22 both created 1972, incorporated
            1978], deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.4
            ExPASy - ENZYME nomenclature database: 3.4.24.4
            ExplorEnz - The Enzyme Database: 3.4.24.4
            ERGO genome analysis and discovery system: 3.4.24.4
            BRENDA, the Enzyme Database: 3.4.24.4
///
ENTRY       EC 3.4.24.5       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
COMMENT     Deleted entry: lens neutral proteinase. Now included with EC
            3.4.22.53 (calpain-2) and EC 3.4.25.1 (proteasome endopeptidase
            complex) (EC 3.4.24.5 created 1978, deleted 1989)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.5
            ExPASy - ENZYME nomenclature database: 3.4.24.5
            ExplorEnz - The Enzyme Database: 3.4.24.5
            ERGO genome analysis and discovery system: 3.4.24.5
            BRENDA, the Enzyme Database: 3.4.24.5
///
ENTRY       EC 3.4.24.6                 Enzyme
NAME        leucolysin;
            Leucostoma neutral proteinase;
            Leucostoma peptidase A
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of Phe1!Val, His5!Leu, Ala14!Leu, Gly20!Glu, Gly23!Phe and
            Phe24!Phe bonds in insulin B chain as well as N-blocked dipeptides
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050];
            Calcium [CPD:C00076]
COMMENT     From the venom of the western cottonmouth moccasin snake
            (Agkistrodon piscivorus leucostoma).
REFERENCE   1  [PMID:5684005]
  AUTHORS   Wagner FW, Spiekerman AM, Prescott JM.
  TITLE     Leucostoma peptidase A. Isolation and physical properties.
  JOURNAL   J. Biol. Chem. 243 (1968) 4486-93.
  ORGANISM  Agkistrodon piscivorus leucostoma
REFERENCE   2  [PMID:4711816]
  AUTHORS   Spiekerman AM, Fredericks KK, Wagner FW, Prescott JM.
  TITLE     Leucostoma peptidase A: a metalloprotease from snake venom.
  JOURNAL   Biochim. Biophys. Acta. 293 (1973) 464-75.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.6
            ExPASy - ENZYME nomenclature database: 3.4.24.6
            ExplorEnz - The Enzyme Database: 3.4.24.6
            ERGO genome analysis and discovery system: 3.4.24.6
            BRENDA, the Enzyme Database: 3.4.24.6
            CAS: 72561-03-6
///
ENTRY       EC 3.4.24.7                 Enzyme
NAME        interstitial collagenase;
            vertebrate collagenase;
            matrix metalloproteinase 1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of the triple helix of collagen at about three-quarters of
            the length of the molecule from the N-terminus, at Gly775!Ile in the
            alpha1(I) chain. Cleaves synthetic substrates and
            alpha-macroglobulins at bonds where P1' is a hydrophobic residue
COFACTOR    Zinc [CPD:C00038]
COMMENT     The enzyme takes its name from substrates of the interstitial
            collagen group - types I, II and III, all of which are cleaved in
            the helical domain. However, alpha-macroglobulins are cleaved much
            more rapidly. The enzyme is widely distributed in vertebrate
            animals. Type example of peptidase family M10
REFERENCE   1  [PMID:3009463]
  AUTHORS   Goldberg GI, Wilhelm SM, Kronberger A, Bauer EA, Grant GA, Eisen AZ.
  TITLE     Human fibroblast collagenase. Complete primary structure and
            homology to an oncogene transformation-induced rat protein.
  JOURNAL   J. Biol. Chem. 261 (1986) 6600-5.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:3041177]
  AUTHORS   Birkedal-Hansen H.
  TITLE     Catabolism and turnover of collagens: collagenases.
  JOURNAL   Methods. Enzymol. 144 (1987) 140-71.
REFERENCE   3  [PMID:3032960]
  AUTHORS   Fields GB, Van Wart HE, Birkedal-Hansen H.
  TITLE     Sequence specificity of human skin fibroblast collagenase. Evidence
            for the role of collagen structure in determining the collagenase
            cleavage site.
  JOURNAL   J. Biol. Chem. 262 (1987) 6221-6.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:2462561]
  AUTHORS   Sottrup-Jensen L, Birkedal-Hansen H.
  TITLE     Human fibroblast collagenase-alpha-macroglobulin interactions.
            Localization of cleavage sites in the bait regions of five mammalian
            alpha-macroglobulins.
  JOURNAL   J. Biol. Chem. 264 (1989) 393-401.
  ORGANISM  human [GN:hsa], rat [GN:rno]
PATHWAY     PATH: map03320  PPAR signaling pathway
            PATH: map05219  Bladder cancer
ORTHOLOGY   KO: K01388  matrix metalloproteinase-1 (interstitial collagenase)
GENES       HSA: 4312(MMP1)
            PTR: 451510(MMP1)
            MMU: 83995(Mmp1a) 83996(Mmp1b)
            RNO: 300339(Mmp1a_predicted)
            CFA: 489428(MMP1)
            BTA: 281308(MMP1)
            GGA: 418982(MMP1)
STRUCTURES  PDB: 1AYK  1CGE  1CGF  1CGL  1FBL  1HFC  1MNC  1R77  1SU3  2AYK  
                 2CLT  2J0T  3AYK  4AYK  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.7
            ExPASy - ENZYME nomenclature database: 3.4.24.7
            ExplorEnz - The Enzyme Database: 3.4.24.7
            ERGO genome analysis and discovery system: 3.4.24.7
            BRENDA, the Enzyme Database: 3.4.24.7
            CAS: 9001-12-1
///
ENTRY       EC 3.4.24.8       Obsolete  Enzyme
NAME        Transferred to 3.4.24.3
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
COMMENT     Transferred entry: now EC 3.4.24.3 microbial collagenase (EC
            3.4.24.8 created 1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.8
            ExPASy - ENZYME nomenclature database: 3.4.24.8
            ExplorEnz - The Enzyme Database: 3.4.24.8
            ERGO genome analysis and discovery system: 3.4.24.8
            BRENDA, the Enzyme Database: 3.4.24.8
///
ENTRY       EC 3.4.24.9       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
COMMENT     Deleted entry: Trichophyton schoenleinii collagenase (EC 3.4.24.9
            created 1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.9
            ExPASy - ENZYME nomenclature database: 3.4.24.9
            ExplorEnz - The Enzyme Database: 3.4.24.9
            ERGO genome analysis and discovery system: 3.4.24.9
            BRENDA, the Enzyme Database: 3.4.24.9
///
ENTRY       EC 3.4.24.10      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
COMMENT     Deleted entry: Trichophyton mentagrophytes keratinase (EC 3.4.24.10
            created 1972 as EC 3.4.99.12, transferred 1978 to EC 3.4.24.10,
            deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.10
            ExPASy - ENZYME nomenclature database: 3.4.24.10
            ExplorEnz - The Enzyme Database: 3.4.24.10
            ERGO genome analysis and discovery system: 3.4.24.10
            BRENDA, the Enzyme Database: 3.4.24.10
///
ENTRY       EC 3.4.24.11                Enzyme
NAME        neprilysin;
            neutral endopeptidase;
            endopeptidase 24.11;
            kidney-brush-border neutral peptidase;
            enkephalinase (misleading);
            endopeptidase-2;
            CALLA (common acute lymphoblastic leukemia-associated) antigens;
            CALLA antigen;
            endopeptidase;
            membrane metalloendopeptidase;
            kidney-brush-border neutral endopeptidase;
            kidney-brush-border neutral proteinase;
            endopeptidase-2;
            CALLA glycoprotein;
            CALLA;
            common acute lymphoblastic leukemia antigen;
            CALLA glycoproteins;
            common acute lymphoblastic leukemia-associated antigens;
            neutral metallendopeptidase;
            membrane metalloendopeptidase;
            NEP;
            neutral endopeptidase 24.11;
            CD10;
            neutral endopeptidase;
            acute lymphoblastic leukemia antigen
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Preferential cleavage of polypeptides between hydrophobic residues,
            particularly with Phe or Tyr at P1'
COFACTOR    Zinc [CPD:C00038]
INHIBITOR   EDTA [CPD:C00284];
            Phosphoramidon [CPD:C00563];
            (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(mercaptomethyl)-1-oxoprolyl]g
            lycine [CPD:C01313];
            (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(mercaptomethyl)-1-oxoprolyl]-
            (S)-alanine [CPD:C01314];
            (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(acetylthio)methyl-1-oxoprolyl
            ]glycine benzyl ester [CPD:C01315];
            (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(acetylthio)methyl-1-oxoprolyl
            ]-(S)-alanine benzyl ester [CPD:C01316];
            Thiorphan [CPD:C01619]
COMMENT     A membrane-bound glycoprotein widely distributed in animal tissues.
            Inhibited by phosphoramidon and thiorphan. Common acute
            lymphoblastic leukemia antigen (CALLA). Type example of peptidase
            family M13
REFERENCE   1  [PMID:6190172]
  AUTHORS   Matsas R, Fulcher IS, Kenny AJ, Turner AJ.
  TITLE     Substance P and [Leu]enkephalin are hydrolyzed by an enzyme in pig
            caudate synaptic membranes that is identical with the endopeptidase
            of kidney microvilli.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 80 (1983) 3111-5.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:3555489]
  AUTHORS   Malfroy B, Schofield PR, Kuang WJ, Seeburg PH, Mason AJ, Henzel WJ.
  TITLE     Molecular cloning and amino acid sequence of rat enkephalinase.
  JOURNAL   Biochem. Biophys. Res. Commun. 144 (1987) 59-66.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:2971756]
  AUTHORS   Letarte M, Vera S, Tran R, Addis JB, Onizuka RJ, Quackenbush EJ,
            Jongeneel CV, McInnes RR.
  TITLE     Common acute lymphocytic leukemia antigen is identical to neutral
            endopeptidase.
  JOURNAL   J. Exp. Med. 168 (1988) 1247-53.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:2521610]
  AUTHORS   Erdos EG, Skidgel RA.
  TITLE     Neutral endopeptidase 24.11 (enkephalinase) and related regulators
            of peptide hormones.
  JOURNAL   FASEB. J. 3 (1989) 145-51.
  ORGANISM  rat [GN:rno], human [GN:hsa], rabbit
PATHWAY     PATH: map04614  Renin-angiotensin system
            PATH: map04640  Hematopoietic cell lineage
            PATH: map05010  Alzheimer's disease
ORTHOLOGY   KO: K01389  neprilysin
GENES       HSA: 4311(MME)
            PTR: 460792(MME)
            MMU: 17380(Mme)
            RNO: 24590(Mme)
            CFA: 477120(MME)
            BTA: 536741(LOC536741)
            GGA: 425031(MME)
            SPU: 580975(LOC580975)
            DME: Dmel_CG4058(Nep4) Dmel_CG6265(Nep5) Dmel_CG9761(Nep2)
            CEL: F26G1.6(Neprilysin) T05A8.4(protease)
            MVA: Mvan_0184
            MGI: Mflv_0472
            MMC: Mmcs_0157
            MKM: Mkms_0166
            MJL: Mjls_0147
            RHA: RHA1_ro05118
STRUCTURES  PDB: 1DMT  1R1H  1R1I  1R1J  1Y8J  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.11
            ExPASy - ENZYME nomenclature database: 3.4.24.11
            ExplorEnz - The Enzyme Database: 3.4.24.11
            ERGO genome analysis and discovery system: 3.4.24.11
            BRENDA, the Enzyme Database: 3.4.24.11
            CAS: 82707-54-8
///
ENTRY       EC 3.4.24.12                Enzyme
NAME        envelysin;
            sea-urchin-hatching proteinase;
            hatching enzyme;
            chorionase;
            chorion-digesting proteinase;
            chymostrypsin;
            sea urchin embryo hatching enzyme
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of proteins of the fertilization envelope and
            dimethylcasein
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050];
            Calcium [CPD:C00076]
COMMENT     A glycoprotein from various members of the class Echinoidea.
            Extracellular enzyme requiring Ca2+. In peptidase family M10
            (interstitial collagenase family)
REFERENCE   1  [PMID:1012003]
  AUTHORS   Barrett D, Edwards BF.
  TITLE     Hatching enzyme of the sea urchin Strongylocentrotus purpuratus.
  JOURNAL   Methods. Enzymol. 45 (1976) 354-73.
  ORGANISM  Strongylocentrotus purpuratus [GN:spu]
REFERENCE   2  [PMID:2925668]
  AUTHORS   Lepage T, Gache C.
  TITLE     Purification and characterization of the sea urchin embryo hatching
            enzyme.
  JOURNAL   J. Biol. Chem. 264 (1989) 4787-93.
  ORGANISM  Paracentrotus lividus
REFERENCE   3  [PMID:2167841]
  AUTHORS   Lepage T, Gache C.
  TITLE     Early expression of a collagenase-like hatching enzyme gene in the
            sea urchin embryo.
  JOURNAL   EMBO. J. 9 (1990) 3003-12.
  ORGANISM  Paracentrotus lividus
REFERENCE   4  [PMID:1711895]
  AUTHORS   Nomura K, Tanaka H, Kikkawa Y, Yamaguchi M, Suzuki N.
  TITLE     The specificity of sea urchin hatching enzyme (envelysin) places it
            in the mammalian matrix metalloproteinase family.
  JOURNAL   Biochemistry. 30 (1991) 6115-23.
  ORGANISM  Hemicentrotus pulcherrimus
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.12
            ExPASy - ENZYME nomenclature database: 3.4.24.12
            ExplorEnz - The Enzyme Database: 3.4.24.12
            ERGO genome analysis and discovery system: 3.4.24.12
            BRENDA, the Enzyme Database: 3.4.24.12
            CAS: 50812-13-0
///
ENTRY       EC 3.4.24.13                Enzyme
NAME        IgA-specific metalloendopeptidase;
            immunoglobulin A1 proteinase;
            IgA protease;
            IgA1-specific proteinase;
            IgA1 protease;
            IgA1 proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of Pro!Thr bond in the hinge region of the heavy chain of
            human IgA
INHIBITOR   EDTA [CPD:C00284]
COMMENT     A 190 kDa enzyme found in several pathogenic species of
            Streptococcus such as sanguis and pneumoniae. Type example of
            peptidase family M26. There is also an IgA-specific prolyl
            endopeptidase of the serine-type (see EC 3.4.21.72, IgA-specific
            serine endopeptidase)
REFERENCE   1  [PMID:6792682]
  AUTHORS   Kornfeld SJ, Plaut AG.
  TITLE     Secretory immunity and the bacterial IgA proteases.
  JOURNAL   Rev. Infect. Dis. 3 (1981) 521-34.
REFERENCE   2  [PMID:1987065]
  AUTHORS   Gilbert JV, Plaut AG, Wright A.
  TITLE     Analysis of the immunoglobulin A protease gene of Streptococcus
            sanguis.
  JOURNAL   Infect. Immun. 59 (1991) 7-17.
  ORGANISM  Streptococcus sanguis
REFERENCE   3  [PMID:3294181]
  AUTHORS   Gilbert JV, Plaut AG, Fishman Y, Wright A.
  TITLE     Cloning of the gene encoding streptococcal immunoglobulin A protease
            and its expression in Escherichia coli.
  JOURNAL   Infect. Immun. 56 (1988) 1961-6.
  ORGANISM  Streptococcus sanguis
ORTHOLOGY   KO: K01390  IgA-specific metalloendopeptidase
GENES       PIC: PICST_28598(RLF2) PICST_72775(SED4) PICST_85888(SSN7)
            SPN: SP_1154
            SPR: spr1042(iga)
            SPD: SPD_1018(iga)
            SSA: SSA_1106(iga)
            SGO: SGO_0408(zmpB) SGO_0942(zmpC)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.13
            ExPASy - ENZYME nomenclature database: 3.4.24.13
            ExplorEnz - The Enzyme Database: 3.4.24.13
            ERGO genome analysis and discovery system: 3.4.24.13
            BRENDA, the Enzyme Database: 3.4.24.13
            CAS: 72231-73-3
///
ENTRY       EC 3.4.24.14                Enzyme
NAME        procollagen N-endopeptidase;
            procollagen N-terminal peptidase;
            procollagen aminopeptidase;
            aminoprocollagen peptidase;
            aminoterminal procollagen peptidase;
            procollagen aminoterminal protease;
            procollagen N-terminal proteinase;
            type I/II procollagen N-proteinase;
            type III procollagen
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleaves the N-propeptide of collagen chain alpha1(I) at Pro!Gln and
            of alpha1(II) and alpha2(I) at Ala!Gln
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     Removes the propeptides of type I and II collagens prior to fibril
            assembly. Does not act on type III collagen. In peptidase family M12
            (astacin family)
REFERENCE   1  [PMID:4204204]
  AUTHORS   Kohn LD, Isersky C, Zupnik J, Lenaers A, Lee G, Lapiere CM.
  TITLE     Calf tendon procollagen peptidase: its purification and
            endopeptidase mode of action.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 71 (1974) 40-4.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:2500439]
  AUTHORS   Hojima Y, McKenzie JA, van der Rest M, Prockop DJ.
  TITLE     Type I procollagen N-proteinase from chick embryo tendons.
            Purification of a new 500-kDa form of the enzyme and identification
            of the catalytically active polypeptides.
  JOURNAL   J. Biol. Chem. 264 (1989) 11336-45.
  ORGANISM  chicken [GN:gga]
ORTHOLOGY   KO: K01391  
            KO: K08618  ADAM metallopeptidase with thrombospondin type 1 motif,
                        2
GENES       HSA: 9509(ADAMTS2)
            PTR: 462325(ADAMTS2)
            MMU: 216725(Adamts2)
            RNO: 287899(RGD1565950_predicted)
            CFA: 481453(ADAMTS2)
            BTA: 282401(ADAMTS2)
            GGA: 416291(ADAMTS2)
            DRE: 571682(LOC571682)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.14
            ExPASy - ENZYME nomenclature database: 3.4.24.14
            ExplorEnz - The Enzyme Database: 3.4.24.14
            ERGO genome analysis and discovery system: 3.4.24.14
            BRENDA, the Enzyme Database: 3.4.24.14
            CAS: 68651-94-5
///
ENTRY       EC 3.4.24.15                Enzyme
NAME        thimet oligopeptidase;
            Pz-peptidase;
            soluble metalloendopeptidase;
            endo-oligopeptidase A;
            tissue-endopeptidase degrading collagenase-synthetic-substrate
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Preferential cleavage of bonds with hydrophobic residues at P1, P2
            and P3' and a small residue at P1' in substrates of 5-15 residues
REFERENCE   1  [PMID:3244563]
  AUTHORS   Cicilini MA, Ribeiro MJ, de Oliveira EB, Mortara RA, de Camargo AC.
  TITLE     Endooligopeptidase A activity in rabbit heart: generation of
            enkephalin from enkephalin containing peptides.
  JOURNAL   Peptides. 9 (1988) 945-55.
  ORGANISM  rabbit
REFERENCE   2  [PMID:2803255]
  AUTHORS   Orlowski M, Reznik S, Ayala J, Pierotti AR.
  TITLE     Endopeptidase 24.15 from rat testes. Isolation of the enzyme and its
            specificity toward synthetic and natural peptides, including
            enkephalin-containing peptides.
  JOURNAL   Biochem. J. 261 (1989) 951-8.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:2123097]
  AUTHORS   Barrett AJ, Brown MA.
  TITLE     Chicken liver Pz-peptidase, a thiol-dependent metallo-endopeptidase.
  JOURNAL   Biochem. J. 271 (1990) 701-6.
  ORGANISM  chicken [GN:gga]
REFERENCE   4  [PMID:2261476]
  AUTHORS   Pierotti A, Dong KW, Glucksman MJ, Orlowski M, Roberts JL.
  TITLE     Molecular cloning and primary structure of rat testes
            metalloendopeptidase EC 3.4.24.15.
  JOURNAL   Biochemistry. 29 (1990) 10323-9.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:2185743]
  AUTHORS   Tisljar U, Barrett AJ.
  TITLE     Thiol-dependent metallo-endopeptidase characteristics of
            Pz-peptidase in rat and rabbit.
  JOURNAL   Biochem. J. 267 (1990) 531-3.
  ORGANISM  rabbit, rat [GN:rno]
PATHWAY     PATH: map04614  Renin-angiotensin system
ORTHOLOGY   KO: K01392  thimet oligopeptidase
GENES       HSA: 7064(THOP1)
            MMU: 50492(Thop1)
            RNO: 64517(Thop1)
            CFA: 476748(THOP1)
            BTA: 510889(THOP1)
            SSC: 397442(THOP1)
            XLA: 397806(LOC397806)
            DRE: 436628(zgc:92139)
            OSA: 4325012
            CME: CMS446C
            AFM: AFUA_7G05930
            AOR: AO090005000457
            TBR: Tb927.7.190
            TCR: 506411.10 511237.10
            LMA: LmjF26.1570
            VFI: VF1239
            SDE: Sde_2026
            MPT: Mpe_A1779
            ADE: Adeh_0397
            AFW: Anae109_4180
            OIH: OB1171 OB1216
            GKA: GK0822 GK1818
            SMU: SMU.645(pepB)
            NCA: Noca_4613
            MBN: Mboo_2053
STRUCTURES  PDB: 1S4B  2O36  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.15
            ExPASy - ENZYME nomenclature database: 3.4.24.15
            ExplorEnz - The Enzyme Database: 3.4.24.15
            ERGO genome analysis and discovery system: 3.4.24.15
            BRENDA, the Enzyme Database: 3.4.24.15
            CAS: 110639-28-6
///
ENTRY       EC 3.4.24.16                Enzyme
NAME        neurolysin;
            neurotensin endopeptidase;
            endopeptidase 24.16;
            endo-oligopeptidase B (proline-endopeptidase)
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Preferential cleavage in neurotensin: Pro10!Tyr
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     No absolute requirement for a prolyl bond: the enzyme acts on some
            peptides, such as dynorphin 1-8, that do not contain proline, and
            does not act on some others that do. In peptidase family M3 (thimet
            oligopeptidase family)
REFERENCE   1  [PMID:3525564]
  AUTHORS   Checler F, Vincent JP, Kitabgi P.
  TITLE     Purification and characterization of a novel neurotensin-degrading
            peptidase from rat brain synaptic membranes.
  JOURNAL   J. Biol. Chem. 261 (1986) 11274-81.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:3409880]
  AUTHORS   Barelli H, Vincent JP, Checler F.
  TITLE     Peripheral inactivation of neurotensin. Isolation and
            characterization of a metallopeptidase from rat ileum.
  JOURNAL   Eur. J. Biochem. 175 (1988) 481-9.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:2649078]
  AUTHORS   Checler F, Barelli H, Vincent JP.
  TITLE     Tissue distribution of a novel neurotensin-degrading
            metallopeptidase. An immunological approach using monospecific
            polyclonal antibodies.
  JOURNAL   Biochem. J. 257 (1989) 549-54.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map04614  Renin-angiotensin system
ORTHOLOGY   KO: K01393  neurolysin
GENES       HSA: 57486(NLN)
            MMU: 75805(Nln)
            RNO: 117041(Nln)
            CFA: 478081(NLN)
            BTA: 538650(NLN)
            SSC: 397646(NLN)
            GGA: 427167(NLN)
            SUS: Acid_7278
STRUCTURES  PDB: 1I1I  2O3E  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.16
            ExPASy - ENZYME nomenclature database: 3.4.24.16
            ExplorEnz - The Enzyme Database: 3.4.24.16
            ERGO genome analysis and discovery system: 3.4.24.16
            BRENDA, the Enzyme Database: 3.4.24.16
            CAS: 149371-24-4
///
ENTRY       EC 3.4.24.17                Enzyme
NAME        stromelysin 1;
            matrix metalloproteinase 3;
            proteoglycanase;
            collagenase activating protein;
            procollagenase activator;
            transin;
            MMP-3;
            neutral proteoglycanase;
            stromelysin;
            collagen-activating protein
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Preferential cleavage where P1', P2' and P3' are hydrophobic
            residues
COMMENT     An extracellular endopeptidase of vertebrate tissues homologous with
            interstitial collagenase. Digests proteoglycan, fibronectin,
            collagen types III, IV, V, IX, and activates procollagenase. In
            peptidase family M10 (interstitial collagenase family)
REFERENCE   1  [PMID:2995374]
  AUTHORS   Chin JR, Murphy G, Werb Z.
  TITLE     Stromelysin, a connective tissue-degrading metalloendopeptidase
            secreted by stimulated rabbit synovial fibroblasts in parallel with
            collagenase. Biosynthesis, isolation, characterization, and
            substrates.
  JOURNAL   J. Biol. Chem. 260 (1985) 12367-76.
  ORGANISM  rabbit
REFERENCE   2  [PMID:3095317]
  AUTHORS   Okada Y, Nagase H, Harris ED Jr.
  TITLE     A metalloproteinase from human rheumatoid synovial fibroblasts that
            digests connective tissue matrix components. Purification and
            characterization.
  JOURNAL   J. Biol. Chem. 261 (1986) 14245-55.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:2197998]
  AUTHORS   Docherty AJ, Murphy G.
  TITLE     The tissue metalloproteinase family and the inhibitor TIMP: a study
            using cDNAs and recombinant proteins.
  JOURNAL   Ann. Rheum. Dis. 49 (1990) 469-79.
REFERENCE   4  [PMID:2165861]
  AUTHORS   Emonard H, Grimaud JA.
  TITLE     Matrix metalloproteinases. A review.
  JOURNAL   Cell. Mol. Biol. 36 (1990) 131-53.
ORTHOLOGY   KO: K01394  matrix metalloproteinase-3 (stromelysin 1,
                        progelatinase)
GENES       HSA: 4314(MMP3)
            PTR: 451511(MMP3)
            MMU: 17392(Mmp3)
            RNO: 171045(Mmp3)
            CFA: 403445(MMP3)
            BTA: 281309(MMP3)
            GGA: 418981(MMP3)
STRUCTURES  PDB: 1B8Y  1BIW  1BM6  1BQO  1C3I  1C8T  1CAQ  1CIZ  1CQR  1D5J  
                 1D7X  1D8F  1D8M  1G05  1G49  1G4K  1HFS  1HY7  1OO9  1QIA  
                 1QIC  1SLM  1SLN  1UEA  1UMS  1UMT  1USN  2D1O  2SRT  2USN  
                 3USN  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.17
            ExPASy - ENZYME nomenclature database: 3.4.24.17
            ExplorEnz - The Enzyme Database: 3.4.24.17
            ERGO genome analysis and discovery system: 3.4.24.17
            BRENDA, the Enzyme Database: 3.4.24.17
            CAS: 79955-99-0
///
ENTRY       EC 3.4.24.18                Enzyme
NAME        meprin A;
            endopeptidase-2;
            meprin-a;
            meprin;
            N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase;
            PABA-peptide hydrolase;
            PPH
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of protein and peptide substrates preferentially on
            carboxyl side of hydrophobic residues
COMMENT     A membrane-bound metalloendopeptidase of rat and mouse kidney and
            intestinal brush borders, and salivary ducts. Differences from
            neprilysin (EC 3.4.24.11 (astacin family). Formerly included in EC
            3.4.24.11
REFERENCE   1  [PMID:7041888]
  AUTHORS   Beynon RJ, Shannon JD, Bond JS.
  TITLE     Purification and characterization of a metallo-endoproteinase from
            mouse kidney.
  JOURNAL   Biochem. J. 199 (1981) 591-8.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:3105525]
  AUTHORS   Butler PE, McKay MJ, Bond JS.
  TITLE     Characterization of meprin, a membrane-bound metalloendopeptidase
            from mouse kidney.
  JOURNAL   Biochem. J. 241 (1987) 229-35.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:2461706]
  AUTHORS   Stephenson SL, Kenny AJ.
  TITLE     The metabolism of neuropeptides. Hydrolysis of peptides by the
            phosphoramidon-insensitive rat kidney enzyme 'endopeptidase-2' and
            by rat microvillar membranes.
  JOURNAL   Biochem. J. 255 (1988) 45-51.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:3261961]
  AUTHORS   Sterchi EE, Naim HY, Lentze MJ, Hauri HP, Fransen JA.
  TITLE     N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: a
            metalloendopeptidase of the human intestinal microvillus membrane
            which degrades biologically active peptides.
  JOURNAL   Arch. Biochem. Biophys. 265 (1988) 105-18.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:2690825]
  AUTHORS   Barnes K, Ingram J, Kenny AJ.
  TITLE     Proteins of the kidney microvillar membrane. Structural and
            immunochemical properties of rat endopeptidase-2 and its
            immunohistochemical localization in tissues of rat and mouse.
  JOURNAL   Biochem. J. 264 (1989) 335-46.
  ORGANISM  mouse [GN:mmu], rat [GN:rno]
ORTHOLOGY   KO: K01395  meprin A, alpha
            KO: K08606  meprin A, beta
GENES       HSA: 4224(MEP1A) 4225(MEP1B)
            PTR: 462745(MEP1A) 468515(MEP1B)
            MMU: 17287(Mep1a) 17288(Mep1b)
            RNO: 25684(Mep1a) 25727(Mep1b)
            CFA: 481826(MEP1A) 490497(MEP1B)
            BTA: 540701(LOC540701)
            GGA: 421097(MEP1B) 422060(MEP1A)
            XLA: 447263(MGC86332)
            XTR: 548484(mep1a)
            DRE: 565535(mep1a.2)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.18
            ExPASy - ENZYME nomenclature database: 3.4.24.18
            ExplorEnz - The Enzyme Database: 3.4.24.18
            ERGO genome analysis and discovery system: 3.4.24.18
            BRENDA, the Enzyme Database: 3.4.24.18
            CAS: 148938-24-3
///
ENTRY       EC 3.4.24.19                Enzyme
NAME        procollagen C-endopeptidase;
            procollagen C-terminal proteinase;
            carboxyprocollagen peptidase;
            procollagen C-terminal peptidase;
            procollagen C-proteinase;
            procollagen C-terminal proteinase;
            procollagen carboxypeptidase;
            procollagen carboxy-terminal proteinase;
            procollagen peptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of the C-terminal propeptide at Ala!Asp in type I and II
            procollagens and at Arg!Asp in type III
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
EFFECTOR    Calcium [CPD:C00076]
COMMENT     A 100 kDa endopeptidase the activity of which is increased by Ca2+
            and by an enhancer glycoprotein. In peptidase family M12 (astacin
            family)
REFERENCE   1  [PMID:3905801]
  AUTHORS   Hojima Y, van der Rest M, Prockop DJ.
  TITLE     Type I procollagen carboxyl-terminal proteinase from chick embryo
            tendons. Purification and characterization.
  JOURNAL   J. Biol. Chem. 260 (1985) 15996-6003.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:2689170]
  AUTHORS   Kessler E, Adar R.
  TITLE     Type I procollagen C-proteinase from mouse fibroblasts. Purification
            and demonstration of a 55-kDa enhancer glycoprotein.
  JOURNAL   Eur. J. Biochem. 186 (1989) 115-21.
  ORGANISM  mouse [GN:mmu]
ORTHOLOGY   KO: K05502  bone morphogenetic protein 1
GENES       HSA: 649(BMP1)
            PTR: 464042(BMP1)
            MMU: 12153(Bmp1)
            RNO: 83470(Bmp1)
            CFA: 486127(BMP1)
            XLA: 397872(BMP-1)
            SPU: 373360(BMP1)
            DME: Dmel_CG6863(tok) Dmel_CG6868(tld)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.19
            ExPASy - ENZYME nomenclature database: 3.4.24.19
            ExplorEnz - The Enzyme Database: 3.4.24.19
            ERGO genome analysis and discovery system: 3.4.24.19
            BRENDA, the Enzyme Database: 3.4.24.19
            CAS: 68651-95-6
///
ENTRY       EC 3.4.24.20                Enzyme
NAME        peptidyl-Lys metalloendopeptidase;
            Armillaria mellea neutral proteinase;
            peptidyllysine metalloproteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Preferential cleavage in proteins: -Xaa!Lys- (in which Xaa may be
            Pro)
COFACTOR    Metal [CPD:C00050]
COMMENT     From the honey fungus Armillaria mellea. In peptidase family M35
            (deuterolysin family).
REFERENCE   1  [PMID:1239277]
  AUTHORS   Doonan S, Doonan HJ, Hanford R, Vernon CA, Walker JM, da Airold LP,
            Bossa F, Barra D, Carloni M, Fasella P, Riva F.
  TITLE     The primary structure of aspartate aminotransferase from pig heart
            muscle. Digestion with a proteinase having specificity for lysine
            residues.
  JOURNAL   Biochem. J. 149 (1975) 497-506.
  ORGANISM  Armillaria mellea
REFERENCE   2  [PMID:23849]
  AUTHORS   Lewis WG, Basford JM, Walton PL.
  TITLE     Specificity and inhibition studies of Armillaria mellea protease.
  JOURNAL   Biochim. Biophys. Acta. 522 (1978) 551-60.
  ORGANISM  Armillaria mellea
ORTHOLOGY   KO: K08646  peptidyl-Lys metalloendopeptidase
GENES       SDN: Sden_1380 Sden_2616
            SAZ: Sama_1205
            SLO: Shew_1243
            AHA: AHA_2713
STRUCTURES  PDB: 1G12  1GE5  1GE6  1GE7  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.20
            ExPASy - ENZYME nomenclature database: 3.4.24.20
            ExplorEnz - The Enzyme Database: 3.4.24.20
            ERGO genome analysis and discovery system: 3.4.24.20
            BRENDA, the Enzyme Database: 3.4.24.20
            CAS: 65979-41-1
///
ENTRY       EC 3.4.24.21                Enzyme
NAME        astacin;
            Astacus proteinase;
            crayfish small-molecule proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of peptide bonds in substrates containing five or more
            amino acids, preferentially with Ala in P1', and Pro in P2'
COMMENT     A 22.6 kDa digestive endopeptidase from the cardia of the crayfish
            Astacus fluviatilis. Type example of peptidase family M12.
REFERENCE   1  [PMID:7041692]
  AUTHORS   Krauhs E, Dorsam H, Little M, Zwilling R, Ponstingl H.
  TITLE     A protease from Astacus fluviatilis as an aid in protein sequencing.
  JOURNAL   Anal. Biochem. 119 (1982) 153-7.
  ORGANISM  Astacus fluviatilis
REFERENCE   2  [PMID:3548817]
  AUTHORS   Titani K, Torff HJ, Hormel S, Kumar S, Walsh KA, Rodl J, Neurath H,
            Zwilling R.
  TITLE     Amino acid sequence of a unique protease from the crayfish Astacus
            fluviatilis.
  JOURNAL   Biochemistry. 26 (1987) 222-6.
  ORGANISM  Astacus fluviatilis
REFERENCE   3  [PMID:16524858]
  AUTHORS   Fadeyev VV, Sytch J, Kalashnikov V, Rojtman A, Syrkin A, Melnichenko
            G.
  TITLE     Levothyroxine replacement therapy in patients with subclinical
            hypothyroidism and coronary artery disease.
  JOURNAL   Endocr. Pract. 12 (2006) 5-17.
REFERENCE   4  [PMID:2261483]
  AUTHORS   Stocker W, Ng M, Auld DS.
  TITLE     Fluorescent oligopeptide substrates for kinetic characterization of
            the specificity of Astacus protease.
  JOURNAL   Biochemistry. 29 (1990) 10418-25.
ORTHOLOGY   KO: K08076  astacin
GENES       CEL: 4R79.1(nas-6) C05D11.6(nas-4) C07D10.4(nas-7) C24F3.3(nas-12)
                 C26C6.3(nas-36) C34D4.9(nas-8) C37H5.9(nas-9) F09E8.6(nas-14)
                 F38E9.2(nas-39) F39D8.4(metalloprotease)
                 F40E10.1(metalloprotease) F42A10.8(nas-28) F45G2.1(nas-1)
                 F46C5.3(nas-25) F57C12.1(nas-38) F58A6.4(nas-29)
                 K03B8.1(nas-16) K03B8.2(nas-17) K03B8.3(nas-18)
                 K03B8.5(nas-19) K04E7.3(nas-33) K06A4.1(nas-3)
                 K09C8.3(metalloprotease) T02B11.7(protease) T04G9.2(nas-15)
                 T11F9.3(nas-20) T11F9.6(nas-22) T23F4.4(protease)
                 T23H4.3(nas-5) T24A11.3(toh-1) Y95B8A.1(peptidase)
            RDE: RD1_1303(nas)
STRUCTURES  PDB: 1AST  1IAA  1IAB  1IAC  1IAD  1IAE  1QJI  1QJJ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.21
            ExPASy - ENZYME nomenclature database: 3.4.24.21
            ExplorEnz - The Enzyme Database: 3.4.24.21
            ERGO genome analysis and discovery system: 3.4.24.21
            BRENDA, the Enzyme Database: 3.4.24.21
            CAS: 143179-21-9
///
ENTRY       EC 3.4.24.22                Enzyme
NAME        stromelysin 2;
            matrix metalloproteinase 10;
            transin 2;
            proteoglycanase 2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Similar to stromelysin 1, but action on collagen types III, IV and V
            is weak
COMMENT     In peptidase family M10 (interstitial collagenase family). Digests
            gelatin types I, III, IV, V, fibronectin and proteoglycan
REFERENCE   1  [PMID:3547333]
  AUTHORS   Breathnach R, Matrisian LM, Gesnel MC, Staub A, Leroy P.
  TITLE     Sequences coding for part of oncogene-induced transin are highly
            conserved in a related rat gene.
  JOURNAL   Nucleic. Acids. Res. 15 (1987) 1139-51.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:2844164]
  AUTHORS   Muller D, Quantin B, Gesnel MC, Millon-Collard R, Abecassis J,
            Breathnach R.
  TITLE     The collagenase gene family in humans consists of at least four
            members.
  JOURNAL   Biochem. J. 253 (1988) 187-92.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:2548603]
  AUTHORS   Nicholson R, Murphy G, Breathnach R.
  TITLE     Human and rat malignant-tumor-associated mRNAs encode
            stromelysin-like metalloproteinases.
  JOURNAL   Biochemistry. 28 (1989) 5195-203.
  ORGANISM  rat [GN:rno], human [GN:hsa]
ORTHOLOGY   KO: K01396  matrix metalloproteinase-10 (stromelysin 2)
GENES       HSA: 4319(MMP10)
            MMU: 17384(Mmp10)
            RNO: 117061(Mmp10)
            XTR: 594917(Mmp10)
STRUCTURES  PDB: 1Q3A  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.22
            ExPASy - ENZYME nomenclature database: 3.4.24.22
            ExplorEnz - The Enzyme Database: 3.4.24.22
            ERGO genome analysis and discovery system: 3.4.24.22
            BRENDA, the Enzyme Database: 3.4.24.22
            CAS: 140610-48-6
///
ENTRY       EC 3.4.24.23                Enzyme
NAME        matrilysin;
            matrin;
            uterine metalloendopeptidase;
            matrix metalloproteinase 7;
            putative (or punctuated) metalloproteinase-1;
            matrix metalloproteinase pump 1;
            MMP 7;
            PUMP-1 proteinase;
            PUMP;
            metalloproteinase pump-1;
            putative metalloproteinase;
            MMP
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of Ala14!Leu and Tyr16!Leu in B chain of insulin. No action
            on collagen types I, II, IV, V. Cleaves gelatin chain alpha2(I) >
            alpha1(I)
COMMENT     Found in rat uterus; at 19 kDa, the smallest member of peptidase
            family M10 (interstitial collagenase family). Similar in specificity
            to stromelysin, but more active on azocoll
REFERENCE   1  [PMID:2844164]
  AUTHORS   Muller D, Quantin B, Gesnel MC, Millon-Collard R, Abecassis J,
            Breathnach R.
  TITLE     The collagenase gene family in humans consists of at least four
            members.
  JOURNAL   Biochem. J. 253 (1988) 187-92.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:3182822]
  AUTHORS   Woessner JF Jr, Taplin CJ.
  TITLE     Purification and properties of a small latent matrix
            metalloproteinase of the rat uterus.
  JOURNAL   J. Biol. Chem. 263 (1988) 16918-25.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:2550050]
  AUTHORS   Quantin B, Murphy G, Breathnach R.
  TITLE     Pump-1 cDNA codes for a protein with characteristics similar to
            those of classical collagenase family members.
  JOURNAL   Biochemistry. 28 (1989) 5327-34.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:2253219]
  AUTHORS   Miyazaki K, Hattori Y, Umenishi F, Yasumitsu H, Umeda M.
  TITLE     Purification and characterization of extracellular matrix-degrading
            metalloproteinase, matrin (pump-1), secreted from human rectal
            carcinoma cell line.
  JOURNAL   Cancer. Res. 50 (1990) 7758-64.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04310  Wnt signaling pathway
ORTHOLOGY   KO: K01397  matrix metalloproteinase-7 (matrilysin, uterine)
GENES       HSA: 4316(MMP7)
            PTR: 451509(MMP7)
            MMU: 17393(Mmp7)
            RNO: 25335(Mmp7)
            CFA: 489432(MMP7)
            BTA: 286794(MMP7)
            GGA: 418983(MMP7)
STRUCTURES  PDB: 1MMP  1MMQ  1MMR  2DDY  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.23
            ExPASy - ENZYME nomenclature database: 3.4.24.23
            ExplorEnz - The Enzyme Database: 3.4.24.23
            ERGO genome analysis and discovery system: 3.4.24.23
            BRENDA, the Enzyme Database: 3.4.24.23
            CAS: 141256-52-2
///
ENTRY       EC 3.4.24.24                Enzyme
NAME        gelatinase A;
            72-kDa gelatinase;
            matrix metalloproteinase 2;
            type IV collagenase;
            3/4 collagenase (Obsolete);
            matrix metalloproteinase 5 (Obsolete);
            72 kDa gelatinase type A;
            collagenase IV;
            collagenase type IV;
            MMP 2;
            type IV collagen metalloproteinase;
            type IV collagenase/gelatinase;
            matrix metalloproteinase 2
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves
            the collagen-like sequence Pro-Gln-Gly!Ile-Ala-Gly-Gln
COMMENT     A secreted endopeptidase in peptidase family M10 (interstitial
            collagenase family), but possessing an additional fibronectin-like
            domain
REFERENCE   1  [PMID:2994741]
  AUTHORS   Murphy G, McAlpine CG, Poll CT, Reynolds JJ.
  TITLE     Purification and characterization of a bone metalloproteinase that
            degrades gelatin and types IV and V collagen.
  JOURNAL   Biochim. Biophys. Acta. 831 (1985) 49-58.
  ORGANISM  rabbit
REFERENCE   2  [PMID:2834383]
  AUTHORS   Collier IE, Wilhelm SM, Eisen AZ, Marmer BL, Grant GA, Seltzer JL,
            Kronberger A, He CS, Bauer EA, Goldberg GI.
  TITLE     H-ras oncogene-transformed human bronchial epithelial cells (TBE-1)
            secrete a single metalloprotease capable of degrading basement
            membrane collagen.
  JOURNAL   J. Biol. Chem. 263 (1988) 6579-87.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:2269296]
  AUTHORS   Okada Y, Morodomi T, Enghild JJ, Suzuki K, Yasui A, Nakanishi I,
            Salvesen G, Nagase H.
  TITLE     Matrix metalloproteinase 2 from human rheumatoid synovial
            fibroblasts. Purification and activation of the precursor and
            enzymic properties.
  JOURNAL   Eur. J. Biochem. 194 (1990) 721-30.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04670  Leukocyte transendothelial migration
            PATH: map04912  GnRH signaling pathway
            PATH: map05219  Bladder cancer
ORTHOLOGY   KO: K01398  matrix metalloproteinase-2 (gelatinase A)
            KO: K07761  gelatinase A
GENES       HSA: 4313(MMP2)
            PTR: 454094(MMP2)
            MMU: 17390(Mmp2)
            RNO: 81686(Mmp2)
            CFA: 403733(MMP2)
            BTA: 282872(MMP2)
            SSC: 397391(MMP-2)
            GGA: 386583(MMP2)
            XLA: 380389(mmp2)
            XTR: 548506(mmp2)
            DRE: 337179(mmp2)
            ATH: AT1G59970
STRUCTURES  PDB: 1CK7  1CXW  1EAK  1GEN  1GXD  1HOV  1J7M  1KS0  1QIB  1RTG  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.24
            ExPASy - ENZYME nomenclature database: 3.4.24.24
            ExplorEnz - The Enzyme Database: 3.4.24.24
            ERGO genome analysis and discovery system: 3.4.24.24
            BRENDA, the Enzyme Database: 3.4.24.24
            CAS: 146480-35-5
///
ENTRY       EC 3.4.24.25                Enzyme
NAME        vibriolysin;
            Aeromonas proteolytica neutral proteinase;
            aeromonolysin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Preferential cleavage of bonds with bulky hydrophobic groups in P2
            and P1'. Phe at P1' is the most favoured residue, which
            distinguished this enzyme from thermolysin
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     Thermostable enzyme from Vibrio proteolyticus (formerly Aeromonas
            proteolytica). Specificity related to, but distinct from, those of
            thermolysin and bacillolysin [1]. A zinc metallopeptidase in family
            M4 (thermolysin family). Formerly included in EC 3.4.24.4
REFERENCE   1  [PMID:2276]
  AUTHORS   Holmquist B, Vallee BL.
  TITLE     Esterase activity of zinc neutral proteases.
  JOURNAL   Biochemistry. 15 (1976) 101-7.
  ORGANISM  Aeromonas proteolytica
REFERENCE   2  [PMID:1012006]
  AUTHORS   Wilkes SH, Prescott JM.
  TITLE     Aeromonas neutral protease.
  JOURNAL   Methods. Enzymol. 45 (1976) 404-15.
REFERENCE   3  [PMID:7000005]
  AUTHORS   Bayliss ME, Wilkes SH, Prescott JM.
  TITLE     Aeromonas neutral protease: specificity toward extended substrates.
  JOURNAL   Arch. Biochem. Biophys. 204 (1980) 214-9.
  ORGANISM  Aeromonas proteolytica
REFERENCE   4  [PMID:3123480]
  AUTHORS   Wilkes SH, Bayliss ME, Prescott JM.
  TITLE     Critical ionizing groups in Aeromonas neutral protease.
  JOURNAL   J. Biol. Chem. 263 (1988) 1821-5.
  ORGANISM  Aeromonas proteolytica
REFERENCE   5  [PMID:2201689]
  AUTHORS   Diez E, Mong S.
  TITLE     Purification of a phospholipase A2 from human monocytic leukemic
            U937 cells. Calcium-dependent activation and membrane association.
  JOURNAL   J. Biol. Chem. 265 (1990) 14654-61.
ORTHOLOGY   KO: K08604  vibriolysin
GENES       VCH: VCA0865
            VVU: VV2_0974
            VVY: VVA1465
            VPA: VPA0755
            SDN: Sden_3015
            HCH: HCH_02479
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.25
            ExPASy - ENZYME nomenclature database: 3.4.24.25
            ExplorEnz - The Enzyme Database: 3.4.24.25
            ERGO genome analysis and discovery system: 3.4.24.25
            BRENDA, the Enzyme Database: 3.4.24.25
            CAS: 58500-42-8
///
ENTRY       EC 3.4.24.26                Enzyme
NAME        pseudolysin;
            Pseudomonas elastase;
            Pseudomonas aeruginosa neutral metalloproteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of proteins including elastin, collagen types III and IV,
            fibronectin and immunoglobulin A, generally with bulky hydrophobic
            group at P1'. Insulin B chain cleavage pattern identical to that of
            thermolysin, but specificity differs in other respects
REFERENCE   1
  AUTHORS   Morihara, K. and Tsuzuki, H.
  TITLE     Pseudomonas aeruginosa elastase: affinity chromatography and some
            properties as a metallo-neutral proteinase.
  JOURNAL   Agric. Biol. Chem. 39 (1975) 1123-1128.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   2  [PMID:6767718]
  AUTHORS   Nishino N, Powers JC.
  TITLE     Pseudomonas aeruginosa elastase. Development of a new substrate,
            inhibitors, and an affinity ligand.
  JOURNAL   J. Biol. Chem. 255 (1980) 3482-6.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   3  [PMID:3512431]
  AUTHORS   Dreyfus LA, Iglewski BH.
  TITLE     Purification and characterization of an extracellular protease of
            Legionella pneumophila.
  JOURNAL   Infect. Immun. 51 (1986) 736-43.
  ORGANISM  Legionella pneumophila
REFERENCE   4  [PMID:2842313]
  AUTHORS   Bever RA, Iglewski BH.
  TITLE     Molecular characterization and nucleotide sequence of the
            Pseudomonas aeruginosa elastase structural gene.
  JOURNAL   J. Bacteriol. 170 (1988) 4309-14.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   5  [PMID:2110146]
  AUTHORS   Black WJ, Quinn FD, Tompkins LS.
  TITLE     Legionella pneumophila zinc metalloprotease is structurally and
            functionally homologous to Pseudomonas aeruginosa elastase.
  JOURNAL   J. Bacteriol. 172 (1990) 2608-13.
  ORGANISM  Pseudomonas aeruginosa
ORTHOLOGY   KO: K01399  pseudolysin
GENES       PAE: PA3724(lasB)
            PAU: PA14_16250(lasB)
            LPN: lpg1655(lasB)
            LPF: lpl1620
            LPP: lpp1626
            CVI: CV_0057(lasB)
STRUCTURES  PDB: 1EZM  1U4G  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.26
            ExPASy - ENZYME nomenclature database: 3.4.24.26
            ExplorEnz - The Enzyme Database: 3.4.24.26
            ERGO genome analysis and discovery system: 3.4.24.26
            BRENDA, the Enzyme Database: 3.4.24.26
            CAS: 171715-23-4
///
ENTRY       EC 3.4.24.27                Enzyme
NAME        thermolysin;
            Bacillus thermoproteolyticus neutral proteinase;
            thermoase;
            thermoase Y10;
            TLN
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Preferential cleavage: !Leu > !Phe
REFERENCE   1  [PMID:5954368]
  AUTHORS   Ohta Y, Ogura Y, Wada A.
  TITLE     Thermostable protease from thermophilic bacteria. I.
            Thermostability, physiocochemical properties, and amino acid
            composition.
  JOURNAL   J. Biol. Chem. 241 (1966) 5919-25.
  ORGANISM  Bacillus thermoproteolyticus
REFERENCE   2  [PMID:4967801]
  AUTHORS   Morihara K, Tsuzuki H, Oka T.
  TITLE     Comparison of the specificities of various neutral proteinases from
            microorganisms.
  JOURNAL   Arch. Biochem. Biophys. 123 (1968) 572-88.
REFERENCE   3  [PMID:5823940]
  AUTHORS   Latt SA, Holmquist B, Vallee BL.
  TITLE     Thermolysin: a zinc metalloenzyme.
  JOURNAL   Biochem. Biophys. Res. Commun. 37 (1969) 333-9.
  ORGANISM  Bacillus thermoproteolyticus
REFERENCE   4  [PMID:5551628]
  AUTHORS   Desmazeaud MJ, Hermier JH.
  TITLE     [Specificity of the nuclear protease produced by Micrococcus
            caseolyticus]
  JOURNAL   Eur. J. Biochem. 19 (1971) 51-5.
  ORGANISM  Micrococcus caseolyticus
REFERENCE   5  [PMID:5004124]
  AUTHORS   Morihara K, Tsuzuki H.
  TITLE     Comparative study of various neutral proteinases from
            microorganisms: specificity with oligopeptides.
  JOURNAL   Arch. Biochem. Biophys. 146 (1971) 291-6.
REFERENCE   6
  AUTHORS   Titani, K., Hermodson, M.
  TITLE     A., Ericson, L. H., Walsh, K. A. and Neurath, H. Amino-acid sequence
            of thermolysin.
  JOURNAL   Nature New Biol. 238 (1972) 35-37.
REFERENCE   7
  AUTHORS   Matthews, B.
  TITLE     W. Structural basis of the action of thermolysin and related zinc
            peptidases.
  JOURNAL   Acc. Chem. Res. 21 (1988) 333-340.
  ORGANISM  Bacillus thermoproteolyticus
ORTHOLOGY   KO: K08603  thermolysin
GENES       BAN: BA0599
            BAR: GBAA0599
            BAT: BAS0567
            BCY: Bcer98_0515
            GKA: GK2838
            FRA: Francci3_1623
STRUCTURES  PDB: 1BQB  1FJ3  1FJO  1FJQ  1FJT  1FJU  1FJV  1FJW  1GXW  1HYT  
                 1KEI  1KJO  1KJP  1KKK  1KL6  1KR6  1KRO  1KS7  1KTO  1L3F  
                 1LNA  1LNB  1LNC  1LND  1LNE  1LNF  1NPC  1OS0  1PE5  1PE7  
                 1PE8  1QF0  1QF1  1QF2  1THL  1TLI  1TLP  1TLX  1TMN  1TRL  
                 1Y3G  1Z9G  1ZDP  2G4Z  2TLI  2TLX  2TMN  3TLI  3TMN  4TLI  
                 4TLN  4TMN  5TLI  5TLN  5TMN  6TLI  6TMN  7TLI  7TLN  8TLI  
                 8TLN  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.27
            ExPASy - ENZYME nomenclature database: 3.4.24.27
            ExplorEnz - The Enzyme Database: 3.4.24.27
            ERGO genome analysis and discovery system: 3.4.24.27
            BRENDA, the Enzyme Database: 3.4.24.27
            CAS: 9073-78-3
///
ENTRY       EC 3.4.24.28                Enzyme
NAME        bacillolysin;
            Bacillus metalloendopeptidase;
            Bacillus subtilis neutral proteinase;
            anilozyme P 10;
            Bacillus metalloproteinase;
            Bacillus neutral proteinase;
            megateriopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Similar, but not identical, to that of thermolysin
COMMENT     Variants of this enzyme have been found in species of Bacillus
            including B. subtilis [1,6], B. amyloliquefaciens [5], B. megaterium
            (megateriopeptidase, [2]), B. mesentericus [10], B. cereus [3,8,9]
            and B. stearothermophilus [7]. In peptidase family M4 (thermolysin
            family). Formerly included in EC 3.4.24.4
REFERENCE   1  [PMID:4967801]
  AUTHORS   Morihara K, Tsuzuki H, Oka T.
  TITLE     Comparison of the specificities of various neutral proteinases from
            microorganisms.
  JOURNAL   Arch. Biochem. Biophys. 123 (1968) 572-88.
REFERENCE   2  [PMID:4980359]
  AUTHORS   Millet J, Acher R.
  TITLE     [Specificity of megateriopeptidase: an amino-endopeptidase with
            hydrophobic characteristics]
  JOURNAL   Eur. J. Biochem. 9 (1969) 456-62.
REFERENCE   3  [PMID:5002444]
  AUTHORS   Feder J, Keay L, Garrett LR, Cirulis N, Moseley MH, Wildi BS.
  TITLE     Bacillus cereus neutral protease.
  JOURNAL   Biochim. Biophys. Acta. 251 (1971) 74-8.
  ORGANISM  Bacillus cereus
REFERENCE   4  [PMID:2276]
  AUTHORS   Holmquist B, Vallee BL.
  TITLE     Esterase activity of zinc neutral proteases.
  JOURNAL   Biochemistry. 15 (1976) 101-7.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   5  [PMID:6090391]
  AUTHORS   Vasantha N, Thompson LD, Rhodes C, Banner C, Nagle J, Filpula D.
  TITLE     Genes for alkaline protease and neutral protease from Bacillus
            amyloliquefaciens contain a large open reading frame between the
            regions coding for signal sequence and mature protein.
  JOURNAL   J. Bacteriol. 159 (1984) 811-9.
  ORGANISM  Bacillus amyloliquefaciens
REFERENCE   6  [PMID:6090407]
  AUTHORS   Yang MY, Ferrari E, Henner DJ.
  TITLE     Cloning of the neutral protease gene of Bacillus subtilis and the
            use of the cloned gene to create an in vitro-derived deletion
            mutation.
  JOURNAL   J. Bacteriol. 160 (1984) 15-21.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   7  [PMID:2993245]
  AUTHORS   Takagi M, Imanaka T, Aiba S.
  TITLE     Nucleotide sequence and promoter region for the neutral protease
            gene from Bacillus stearothermophilus.
  JOURNAL   J. Bacteriol. 163 (1985) 824-31.
  ORGANISM  Bacillus stearothermophilus
REFERENCE   8  [PMID:3092843]
  AUTHORS   Sidler W, Niederer E, Suter F, Zuber H.
  TITLE     The primary structure of Bacillus cereus neutral proteinase and
            comparison with thermolysin and Bacillus subtilis neutral
            proteinase.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 367 (1986) 643-57.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   9  [PMID:3127592]
  AUTHORS   Pauptit RA, Karlsson R, Picot D, Jenkins JA, Niklaus-Reimer AS,
            Jansonius JN.
  TITLE     Crystal structure of neutral protease from Bacillus cereus refined
            at 3.0 A resolution and comparison with the homologous but more
            thermostable enzyme thermolysin.
  JOURNAL   J. Mol. Biol. 199 (1988) 525-37.
  ORGANISM  Bacillus cereus
REFERENCE   10 [PMID:2302386]
  AUTHORS   Stoeva S, Kleinschmidt T, Mesrob B, Braunitzer G.
  TITLE     Primary structure of a zinc protease from Bacillus mesentericus
            strain 76.
  JOURNAL   Biochemistry. 29 (1990) 527-34.
  ORGANISM  Bacillus mesentericus
ORTHOLOGY   KO: K01400  bacillolysin
GENES       BUR: Bcep18194_B0597 Bcep18194_C7164
            BPM: BURPS1710b_A2125
            BTE: BTH_II1851
            HPA: HPAG1_0201
            BSU: BG10448(nprE)
            BCE: BC0602 BC2167 BC2506 BC2735 BC3383 BC5036
            BCA: BCE_2762
            BCZ: BCZK0511(npr) BCZK1978 BCZK2310 BCZK2464(nprE) BCZK3091(npr)
                 pE33L466_0100(npr) pE33L466_0375(npr) pE33L466_0380(npr)
            BTK: BT9727_0509(npr) BT9727_1996 BT9727_2348(npr)
                 BT9727_2499(nprE) BT9727_3170(npr)
            BTL: BALH_0539(nprE) BALH_2309 BALH_2452(nprE) BALH_2915(npr)
            BAY: RBAM_014550
            CBF: CLI_1530
            NCA: Noca_3166
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.28
            ExPASy - ENZYME nomenclature database: 3.4.24.28
            ExplorEnz - The Enzyme Database: 3.4.24.28
            ERGO genome analysis and discovery system: 3.4.24.28
            BRENDA, the Enzyme Database: 3.4.24.28
            CAS: 76774-43-1
///
ENTRY       EC 3.4.24.29                Enzyme
NAME        aureolysin;
            Staphylococcus aureus neutral proteinase;
            Staphylococcus aureus neutral protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of insulin B chain with specificity similar to that of
            thermolysin, preferring hydrophobic P1' residue. Activates the
            glutamyl endopeptidase (internal_xref(ec_num(3,4,21,19))) of
            Staphylococcus aureus
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050];
            Calcium [CPD:C00076]
COMMENT     A metalloenzyme from S. aureus earlier confused with staphylokinase
            (a non-enzymatic activator of plasminogen).
REFERENCE   1  [PMID:4632563]
  AUTHORS   Arvidson S.
  TITLE     Studies on extracellular proteolytic enzymes from Staphylococcus
            aureus. II. Isolation and characterization of an EDTA-sensitive
            protease.
  JOURNAL   Biochim. Biophys. Acta. 302 (1973) 149-57.
  ORGANISM  Staphylococcus aureus
REFERENCE   2  [PMID:823980]
  AUTHORS   Saheb SA.
  TITLE     [Purification and characterization of an extracellular protease from
            Staphylococcus aureus inhibited by EDTA]
  JOURNAL   Biochimie. 58 (1976) 793-804.
  ORGANISM  Staphylococcus aureus
REFERENCE   3  [PMID:711676]
  AUTHORS   Drapeau GR.
  TITLE     Role of metalloprotease in activation of the precursor of
            staphylococcal protease.
  JOURNAL   J. Bacteriol. 136 (1978) 607-13.
  ORGANISM  Staphylococcus aureus
REFERENCE   4  [PMID:2512988]
  AUTHORS   Potempa J, Porwit-Bobr Z, Travis J.
  TITLE     Stabilization vs. degradation of Staphylococcus aureus
            metalloproteinase.
  JOURNAL   Biochim. Biophys. Acta. 993 (1989) 301-4.
  ORGANISM  Staphylococcus aureus
ORTHOLOGY   KO: K01401  aureolysin
GENES       SAU: SA2430(aur)
            SAV: SAV2637(aur)
            SAM: MW2558(aur)
            SAR: SAR2716(aur)
            SAS: SAS2523
            SAC: SACOL2659(aur)
            SAB: SAB2512c(aur)
            SAA: SAUSA300_2572(aur)
            SAO: SAOUHSC_02971
            SEP: SE2219
            SSP: SSP1542
STRUCTURES  PDB: 1C76  1C77  1C78  1C79  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.29
            ExPASy - ENZYME nomenclature database: 3.4.24.29
            ExplorEnz - The Enzyme Database: 3.4.24.29
            ERGO genome analysis and discovery system: 3.4.24.29
            BRENDA, the Enzyme Database: 3.4.24.29
            CAS: 39335-13-2
///
ENTRY       EC 3.4.24.30                Enzyme
NAME        coccolysin;
            Streptococcus thermophilus intracellular proteinase;
            EM 19000
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Preferential cleavage: !Leu, !Phe, !Tyr, !Ala
COMMENT     A 30 kDa endopeptidase found intracellularly in S. thermophilus [1]
            and S. diacetilactis [2] and in the medium of S. faecalis [3,4]. In
            peptidase family M4 (thermolysin family). Formerly included in EC
            3.4.24.4
REFERENCE   1  [PMID:4451671]
  AUTHORS   Desmazeaud MJ.
  TITLE     [General properties and specificity of action of a neutral
            intracellular endopeptidase from Streptococcus thermophilus]
  JOURNAL   Biochimie. 56 (1974) 1173-81.
  ORGANISM  Streptococcus thermophilus
REFERENCE   2
  AUTHORS   Desmazeaud, M.J. and Zevaco, C.
  TITLE     General properties and substrate specificity of an intracellular
            neutral protease from Streptococcus diacetilactis.
  JOURNAL   Ann. Biol. Anim. Biochem. Biophys. 16 (1976) 851-868.
  ORGANISM  Streptococcus diacetilactis
REFERENCE   3  [PMID:6779709]
  AUTHORS   Smith RA, Green J, Kopper PH.
  TITLE     The purification and properties of a fibrinolytic neutral
            metalloendopeptidase from Streptococcus faecalis.
  JOURNAL   Arch. Biochem. Biophys. 202 (1980) 629-38.
  ORGANISM  Streptococcus faecalis
REFERENCE   4  [PMID:2536744]
  AUTHORS   Makinen PL, Clewell DB, An F, Makinen KK.
  TITLE     Purification and substrate specificity of a strongly hydrophobic
            extracellular metalloendopeptidase (&quot;gelatinase&quot;) from
            Streptococcus faecalis (strain 0G1-10).
  JOURNAL   J. Biol. Chem. 264 (1989) 3325-34.
  ORGANISM  Streptococcus faecalis
ORTHOLOGY   KO: K08605  coccolysin
GENES       EFA: EF1818
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.30
            ExPASy - ENZYME nomenclature database: 3.4.24.30
            ExplorEnz - The Enzyme Database: 3.4.24.30
            ERGO genome analysis and discovery system: 3.4.24.30
            BRENDA, the Enzyme Database: 3.4.24.30
            CAS: 156859-08-4
///
ENTRY       EC 3.4.24.31                Enzyme
NAME        mycolysin;
            pronase component;
            Streptomyces griseus neutral proteinase;
            actinase E;
            SGNPI
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Preferential cleavage of bonds with hydrophobic residues in P1'
INHIBITOR   Mercaptoacetyl-Phe-Leu [CPD:C03292]
COMMENT     From Streptomyces griseus, S. naraensis, and S. cacaoi. Specificity
            similar to that of thermolysin, but much more sensitive to
            inhibition by mercaptoacetyl-Phe-Leu. Little structural similarity
            to other bacterial metalloendopeptidases. Type example of peptidase
            family M5. Formerly included in EC 3.4.24.4
REFERENCE   1  [PMID:4967801]
  AUTHORS   Morihara K, Tsuzuki H, Oka T.
  TITLE     Comparison of the specificities of various neutral proteinases from
            microorganisms.
  JOURNAL   Arch. Biochem. Biophys. 123 (1968) 572-88.
REFERENCE   2  [PMID:5073323]
  AUTHORS   Hiramatsu A, Ouchi T.
  TITLE     A neutral proteinase from Streptomyces naraensis. 3. An improved
            purification and some physiochemical properties.
  JOURNAL   J. Biochem. (Tokyo). 71 (1972) 767-81.
  ORGANISM  Streptomyces naraensis
REFERENCE   3  [PMID:6413206]
  AUTHORS   Blumberg S, Tauber Z.
  TITLE     Inhibition of metalloendopeptidases by 2-mercaptoacetyl-dipeptides.
  JOURNAL   Eur. J. Biochem. 136 (1983) 151-4.
  ORGANISM  Streptomyces griseus
REFERENCE   4  [PMID:2341042]
  AUTHORS   Chang PC, Kuo TC, Tsugita A, Lee YH.
  TITLE     Extracellular metalloprotease gene of Streptomyces cacaoi:
            structure, nucleotide sequence and characterization of the cloned
            gene product.
  JOURNAL   Gene. 88 (1990) 87-95.
  ORGANISM  Streptomyces cacaoi
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.31
            ExPASy - ENZYME nomenclature database: 3.4.24.31
            ExplorEnz - The Enzyme Database: 3.4.24.31
            ERGO genome analysis and discovery system: 3.4.24.31
            BRENDA, the Enzyme Database: 3.4.24.31
            CAS: 153190-34-2
///
ENTRY       EC 3.4.24.32                Enzyme
NAME        beta-lytic metalloendopeptidase;
            Myxobacter beta-lytic proteinase;
            achromopeptidase component;
            beta-lytic metalloproteinase;
            beta-lytic protease;
            Myxobacterium sorangium beta-lytic proteinase;
            Myxobacter495 beta-lytic proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of N-acetylmuramoyl!Ala, and of the insulin B chain at
            Gly23!Phe > Val18!Cya
COMMENT     From Achromobacter lyticus and Lysobacter enzymogenes. Digests
            bacterial cell walls. Type example of peptidase family M23.
REFERENCE   1  [PMID:5880182]
  AUTHORS   Whitaker DR, Roy C, Tsai CS, Jurasek L.
  TITLE     Lytic enzymes of Sorangium sp. A comparison of the proteolytic
            properties of the alpha- and beta-lytic proteases.
  JOURNAL   Can. J. Biochem. 43 (1965) 1961-70.
  ORGANISM  Sorangium sp.
REFERENCE   2  [PMID:6034704]
  AUTHORS   Whitaker DR, Roy C.
  TITLE     Concerning the nature of the alpha- and beta-lytic proteases of
            Sorangium sp.
  JOURNAL   Can. J. Biochem. 45 (1967) 911-6.
  ORGANISM  Sorangium sp.
REFERENCE   3  [PMID:2229127]
  AUTHORS   Draganich LF, Simon MA.
  TITLE     Comparative assessment of gait after limb-salvage procedures.
  JOURNAL   J. Bone. Joint. Surg. Am. 72 (1990) 1430.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.32
            ExPASy - ENZYME nomenclature database: 3.4.24.32
            ExplorEnz - The Enzyme Database: 3.4.24.32
            ERGO genome analysis and discovery system: 3.4.24.32
            BRENDA, the Enzyme Database: 3.4.24.32
            CAS: 37288-92-9
///
ENTRY       EC 3.4.24.33                Enzyme
NAME        peptidyl-Asp metalloendopeptidase;
            endoproteinase Asp-N;
            peptidyl-Asp metalloproteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of Xaa!Asp, Xaa!Glu and Xaa!cysteic acid bonds
COFACTOR    Metal [CPD:C00050]
COMMENT     A metalloenzyme isolated from Pseudomonas fragi. Useful in protein
            sequencing applications because of its limited specificity. In
            peptidase family M72.
REFERENCE   1  [PMID:236771]
  AUTHORS   Porzio MA, Pearson AM.
  TITLE     Isolation of an extracellular neutral proteinase from Pseudomonas
            fragi.
  JOURNAL   Biochim. Biophys. Acta. 384 (1975) 235-41.
  ORGANISM  Pseudomonas fragi
REFERENCE   2  [PMID:7188696]
  AUTHORS   Drapeau GR.
  TITLE     Substrate specificity of a proteolytic enzyme isolated from a mutant
            of Pseudomonas fragi.
  JOURNAL   J. Biol. Chem. 255 (1980) 839-40.
  ORGANISM  Pseudomonas fragi
REFERENCE   3  [PMID:2669754]
  AUTHORS   Ingrosso D, Fowler AV, Bleibaum J, Clarke S.
  TITLE     Specificity of endoproteinase Asp-N (Pseudomonas fragi): cleavage at
            glutamyl residues in two proteins.
  JOURNAL   Biochem. Biophys. Res. Commun. 162 (1989) 1528-34.
  ORGANISM  Pseudomonas fragi
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.33
            ExPASy - ENZYME nomenclature database: 3.4.24.33
            ExplorEnz - The Enzyme Database: 3.4.24.33
            ERGO genome analysis and discovery system: 3.4.24.33
            BRENDA, the Enzyme Database: 3.4.24.33
            CAS: 55576-49-3
///
ENTRY       EC 3.4.24.34                Enzyme
NAME        neutrophil collagenase;
            matrix metalloproteinase 8;
            PMNL collagenase;
            MMP-8
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of interstitial collagens in the triple helical domain.
            Unlike internal_xref(ec_num(3,4,24,7)), this enzyme cleaves type III
            collagen more slowly than type I
COMMENT     Similar to interstitial collagenase in specificity, but the product
            of a different gene and highly glycosylated. Stored in the specific
            granules of neutrophil leukocytes. In peptidase family M10
            (interstitial collagenase family). Formerly included in EC 3.4.24.7
REFERENCE   1  [PMID:3038863]
  AUTHORS   Hasty KA, Jeffrey JJ, Hibbs MS, Welgus HG.
  TITLE     The collagen substrate specificity of human neutrophil collagenase.
  JOURNAL   J. Biol. Chem. 262 (1987) 10048-52.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:2164002]
  AUTHORS   Hasty KA, Pourmotabbed TF, Goldberg GI, Thompson JP, Spinella DG,
            Stevens RM, Mainardi CL.
  TITLE     Human neutrophil collagenase. A distinct gene product with homology
            to other matrix metalloproteinases.
  JOURNAL   J. Biol. Chem. 265 (1990) 11421-4.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:2159879]
  AUTHORS   Knauper V, Kramer S, Reinke H, Tschesche H.
  TITLE     Characterization and activation of procollagenase from human
            polymorphonuclear leucocytes. N-terminal sequence determination of
            the proenzyme and various proteolytically activated forms.
  JOURNAL   Eur. J. Biochem. 189 (1990) 295-300.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01402  matrix metalloproteinase-8 (neutrophil collagenase)
GENES       HSA: 4317(MMP8)
            MMU: 17394(Mmp8)
            RNO: 63849(Mmp8)
            CFA: 489429(MMP8)
STRUCTURES  PDB: 1A85  1A86  1BZS  1I73  1I76  1JAN  1JAO  1JAP  1JAQ  1JH1  
                 1JJ9  1KBC  1MMB  1ZP5  1ZS0  1ZVX  2OY2  2OY4  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.34
            ExPASy - ENZYME nomenclature database: 3.4.24.34
            ExplorEnz - The Enzyme Database: 3.4.24.34
            ERGO genome analysis and discovery system: 3.4.24.34
            BRENDA, the Enzyme Database: 3.4.24.34
            CAS: 9001-12-1
///
ENTRY       EC 3.4.24.35                Enzyme
NAME        gelatinase B;
            92-kDa gelatinase;
            matrix metalloproteinase 9;
            type V collagenase;
            92-kDa type IV collagenase;
            macrophage gelatinase;
            95 kDa type IV collagenase/gelatinase;
            collagenase IV;
            collagenase type IV;
            gelatinase MMP 9;
            MMP 9;
            matrix metalloproteinase 9;
            type IV collagen metalloproteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of gelatin types I and V and collagen types IV and V
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050];
            Calcium [CPD:C00076]
COMMENT     Similar to gelatinase A, but possesses a further domain . In
            peptidase family M10 (interstitial collagenase family)
REFERENCE   1  [PMID:3680518]
  AUTHORS   Hibbs MS, Hoidal JR, Kang AH.
  TITLE     Expression of a metalloproteinase that degrades native type V
            collagen and denatured collagens by cultured human alveolar
            macrophages.
  JOURNAL   J. Clin. Invest. 80 (1987) 1644-50.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:2551898]
  AUTHORS   Wilhelm SM, Collier IE, Marmer BL, Eisen AZ, Grant GA, Goldberg GI.
  TITLE     SV40-transformed human lung fibroblasts secrete a 92-kDa type IV
            collagenase which is identical to that secreted by normal human
            macrophages.
  JOURNAL   J. Biol. Chem. 264 (1989) 17213-21.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:2165210]
  AUTHORS   Mainardi CL, Hasty KA.
  TITLE     Secretion and glycosylation of rabbit macrophage type V collagenase.
  JOURNAL   Matrix. 10 (1990) 84-90.
  ORGANISM  rabbit
PATHWAY     PATH: map04670  Leukocyte transendothelial migration
            PATH: map05219  Bladder cancer
ORTHOLOGY   KO: K01403  matrix metalloproteinase-9 (gelatinase B)
GENES       HSA: 4318(MMP9)
            PTR: 458294(MMP9)
            MMU: 17395(Mmp9)
            RNO: 81687(Mmp9)
            CFA: 403885(MMP9)
            BTA: 282871(MMP9)
            SSC: 654325(LOC654325)
            GGA: 395387(MMP9)
            XLA: 379663(MGC69080)
            XTR: 448591(mmp9)
            DRE: 406397(mmp9)
            AVA: Ava_1873 Ava_3135
STRUCTURES  PDB: 1GKC  1GKD  1ITV  1L6J  2OVX  2OVZ  2OW0  2OW1  2OW2  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.35
            ExPASy - ENZYME nomenclature database: 3.4.24.35
            ExplorEnz - The Enzyme Database: 3.4.24.35
            ERGO genome analysis and discovery system: 3.4.24.35
            BRENDA, the Enzyme Database: 3.4.24.35
            CAS: 146480-36-6
///
ENTRY       EC 3.4.24.36                Enzyme
NAME        leishmanolysin;
            promastigote surface endopeptidase;
            glycoprotein gp63;
            Leishmania metalloproteinase;
            surface acid proteinase;
            promastigote surface protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Preference for hydrophobic residues at P1 and P1' and basic residues
            at P2' and P3'. A model nonapeptide is cleaved at
            -Ala-Tyr!Leu-Lys-Lys-
INHIBITOR   Z-Tyr-Leu-NHOH [CPD:C02203]
COMMENT     A membrane-bound glycoprotein found on the promastigote of various
            species of Leishmania protozoans. Contains consensus sequence for a
            zinc-binding site; Z-Tyr-Leu-NHOH is a strong inhibitor. The enzyme
            can activate its proenzyme by cleavage of the Val100!Val bond. An
            acid pH optimum is found with certain protein substrates. Type
            example of peptidase family M8
REFERENCE   1  [PMID:3346625]
  AUTHORS   Button LL, McMaster WR.
  TITLE     Molecular cloning of the major surface antigen of leishmania.
  JOURNAL   J. Exp. Med. 167 (1988) 724-9.
  ORGANISM  Leishmania major [GN:lma], Leishmania donovani
REFERENCE   2  [PMID:2608099]
  AUTHORS   Bouvier J, Bordier C, Vogel H, Reichelt R, Etges R.
  TITLE     Characterization of the promastigote surface protease of Leishmania
            as a membrane-bound zinc endopeptidase.
  JOURNAL   Mol. Biochem. Parasitol. 37 (1989) 235-45.
  ORGANISM  Leishmania major [GN:lma]
REFERENCE   3  [PMID:2708373]
  AUTHORS   Chaudhuri G, Chaudhuri M, Pan A, Chang KP.
  TITLE     Surface acid proteinase (gp63) of Leishmania mexicana. A
            metalloenzyme capable of protecting liposome-encapsulated proteins
            from phagolysosomal degradation by macrophages.
  JOURNAL   J. Biol. Chem. 264 (1989) 7483-9.
  ORGANISM  Leishmania mexicana
REFERENCE   4  [PMID:2271643]
  AUTHORS   Bouvier J, Schneider P, Etges R, Bordier C.
  TITLE     Peptide substrate specificity of the membrane-bound metalloprotease
            of Leishmania.
  JOURNAL   Biochemistry. 29 (1990) 10113-9.
  ORGANISM  Leishmania major [GN:lma], Leishmania amazonensis
ORTHOLOGY   KO: K01404  leishmanolysin
GENES       HSA: 89782(LMLN)
            PTR: 460976(LMLN)
            MMU: 239833(Lmln)
            RNO: 363795(Lmln_predicted)
            CFA: 609201(LMLN)
            BTA: 532564(LOC532564)
            GGA: 424264(LMLN)
            DRE: 560606(LOC560606)
            SPU: 580317(LOC580317)
            OSA: 4334001
            DDI: DDBDRAFT_0187000
            TET: TTHERM_00112760 TTHERM_00319900 TTHERM_00721820
                 TTHERM_00794340 TTHERM_00804790 TTHERM_00857790
                 TTHERM_00873660 TTHERM_00873670 TTHERM_00942690
                 TTHERM_00979910 TTHERM_00979920 TTHERM_00979930
                 TTHERM_00979940 TTHERM_00979950 TTHERM_01009860
                 TTHERM_01009870 TTHERM_01082860 TTHERM_01102690
                 TTHERM_01731490 TTHERM_02182710
            TBR: Tb11.02.5310
            TCR: 504801.20 511151.54
            LMA: LmjF31.2000
            EHI: 30.t00006
            RBA: RB11799
STRUCTURES  PDB: 1LML  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.36
            ExPASy - ENZYME nomenclature database: 3.4.24.36
            ExplorEnz - The Enzyme Database: 3.4.24.36
            ERGO genome analysis and discovery system: 3.4.24.36
            BRENDA, the Enzyme Database: 3.4.24.36
            CAS: 161052-06-8
///
ENTRY       EC 3.4.24.37                Enzyme
NAME        saccharolysin;
            proteinase yscD;
            yeast cysteine proteinase D (Misleading);
            Saccharomyces cerevisiae proteinase yscD
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of Pro!Phe and Ala!Ala bonds
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     An 83 kDa cytoplasmic thiol-dependent metalloendopeptidase from
            Saccharomyces cerevisiae. In peptidase family M3 (thimet
            oligopeptidase family).
REFERENCE   1  [PMID:3886641]
  AUTHORS   Achstetter T, Ehmann C, Wolf DH.
  TITLE     Proteinase yscD. Purification and characterization of a new yeast
            peptidase.
  JOURNAL   J. Biol. Chem. 260 (1985) 4585-90.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:3545833]
  AUTHORS   Garcia-Alvarez N, Teichert U, Wolf DH.
  TITLE     Proteinase yscD mutants of yeast. Isolation and characterization.
  JOURNAL   Eur. J. Biochem. 163 (1987) 339-46.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K01405  saccharolysin
GENES       SCE: YCL057W(PRD1)
            AGO: AGOS_AGR406C
            PIC: PICST_28404(PRD1.2) PICST_51091(PRD1.1)
            CGR: CAGL0B00418g
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.37
            ExPASy - ENZYME nomenclature database: 3.4.24.37
            ExplorEnz - The Enzyme Database: 3.4.24.37
            ERGO genome analysis and discovery system: 3.4.24.37
            BRENDA, the Enzyme Database: 3.4.24.37
            CAS: 96779-48-5
///
ENTRY       EC 3.4.24.38                Enzyme
NAME        gametolysin;
            autolysin, Chlamydomonas cell wall degrading protease;
            lysin;
            Chlamydomonas reinhardtii metalloproteinase;
            gamete lytic enzyme;
            gamete autolysin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of the proline- and hydroxyproline-rich proteins of the
            Chlamydomonas cell wall; also cleaves azocasein, gelatin and
            Leu-Trp-Met!Arg-Phe-Ala
COFACTOR    Zinc [CPD:C00038]
INHIBITOR   Phosphoramidon [CPD:C00563]
COMMENT     A glycoprotein found in the periplasmic space of Chlamydomonas
            reinhardtii gametes in a 62 kDa inactive form; decreased to 60 kDa
            upon activation. A zinc enzyme, inhibited by phosphoramidon, but
            also thiol activated. Type example of peptidase family M11
REFERENCE   1  [PMID:3319620]
  AUTHORS   Jaenicke L, Kuhne W, Spessert R, Wahle U, Waffenschmidt S.
  TITLE     Cell-wall lytic enzymes (autolysins) of Chlamydomonas reinhardtii
            are (hydroxy)proline-specific proteases.
  JOURNAL   Eur. J. Biochem. 170 (1987) 485-91.
  ORGANISM  Chlamydomonas reinhardtii
REFERENCE   2  [PMID:2910877]
  AUTHORS   Buchanan MJ, Imam SH, Eskue WA, Snell WJ.
  TITLE     Activation of the cell wall degrading protease, lysin, during sexual
            signalling in Chlamydomonas: the enzyme is stored as an inactive,
            higher relative molecular mass precursor in the periplasm.
  JOURNAL   J. Cell. Biol. 108 (1989) 199-207.
  ORGANISM  Chlamydomonas reinhardtii
REFERENCE   3
  AUTHORS   Matsuda, Y.
  TITLE     Gametolysin.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. & Woessner, J.F. (Eds.), Handbook
            of Proteolytic Enzymes, Academic Press, London, 1998, p. 1140-1143.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.38
            ExPASy - ENZYME nomenclature database: 3.4.24.38
            ExplorEnz - The Enzyme Database: 3.4.24.38
            ERGO genome analysis and discovery system: 3.4.24.38
            BRENDA, the Enzyme Database: 3.4.24.38
            CAS: 97089-74-2
///
ENTRY       EC 3.4.24.39                Enzyme
NAME        deuterolysin;
            Penicillium roqueforti protease II;
            microbial neutral proteinase II;
            acid metalloproteinase;
            neutral proteinase II;
            Penicillium roqueforti metalloproteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Preferential cleavage of bonds with hydrophobic residues in P1';
            also Asn3!Gln and Gly8!Ser bonds in insulin B chain
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     Proteolytic activity found in Penicillium roqueforti [4], P.
            caseicolum [4], Aspergillus sojae [3] and A. oryzae [1,5]. Optimum
            pH of 5 for digesting various proteins. Strong action on protamine
            and histones. Insensitive to phosphoramidon. About 20 kDa. A
            distinct Aspergillus sojae endopeptidase is larger and has a neutral
            pH optimum. Type example of peptidase family M35. Formerly included
            in EC 3.4.24.4
REFERENCE   1
  AUTHORS   Nakadai, T., Nasuno, S. and Iguchi, N.
  TITLE     Purification and properties of neutral proteinase II from
            Aspergillus oryzae.
  JOURNAL   Agric. Biol. Chem. 37 (1973) 2703-2708.
  ORGANISM  Aspergillus oryzae [GN:aor]
REFERENCE   2  [PMID:4219726]
  AUTHORS   Gripon JC, Hermier J.
  TITLE     [The proteolytic system of Penicillium roqueforti. III. -
            Purification, properties and specificity of a protease inhibited by
            E.D.T.A]
  JOURNAL   Biochimie. 56 (1974) 1323-32.
  ORGANISM  Penicillium roqueforti
REFERENCE   3
  AUTHORS   Sekine, H.
  TITLE     , Neutral proteinases I and II of Aspergillus sojae action on
            various substrates.
  JOURNAL   Agric. Biol. Chem. 40 (1976) 703-709.
  ORGANISM  Aspergillus sojae
REFERENCE   4  [PMID:6998789]
  AUTHORS   Gripon JC, Auberger B, Lenoir J.
  TITLE     Metalloproteases from Penicillium caseicolum and P. roqueforti:
            comparison of specificity and chemical characterization.
  JOURNAL   Int. J. Biochem. 12 (1980) 451-5.
  ORGANISM  Penicillium roqueforti, Penicillium caseicolum
REFERENCE   5
  AUTHORS   Vaganova, T.I., Ivanova, N.M. and Stepanov, V.M.
  TITLE     Isolation and properties of the "acid" metalloproteinase from
            Aspergillus oryzae.
  JOURNAL   Biochemistry (Moscow) 53 (1988) 1171-1178.
  ORGANISM  Aspergillus oryzae [GN:aor]
STRUCTURES  PDB: 1EB6  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.39
            ExPASy - ENZYME nomenclature database: 3.4.24.39
            ExplorEnz - The Enzyme Database: 3.4.24.39
            ERGO genome analysis and discovery system: 3.4.24.39
            BRENDA, the Enzyme Database: 3.4.24.39
            CAS: 73562-33-1
///
ENTRY       EC 3.4.24.40                Enzyme
NAME        serralysin;
            Pseudomonas aeruginosa alkaline proteinase;
            Escherichia freundii proteinase;
            Serratia marcescens extracellular proteinase;
            Serratia marcescens metalloproteinase;
            Pseudomonas aeruginosa alk. protease;
            Serratia marcescens metalloprotease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Preferential cleavage of bonds with hydrophobic residues in P1'
COMMENT     A 50 kDa extracellular endopeptidase from Pseudomonas aeruginosa
            [1,2,6], Escherichia freundii [3], Serratia marcescens [4,5,6] and
            Erwinia chrysanthemi [7]. There is broad specificity in cleavage of
            the insulin B chain, with some species variations. The pH optimum
            for digesting various proteins is about 9 - 10. In peptidase family
            M10 (interstitial collagenase family). Formerly included in EC
            3.4.24.4
REFERENCE   1  [PMID:4967801]
  AUTHORS   Morihara K, Tsuzuki H, Oka T.
  TITLE     Comparison of the specificities of various neutral proteinases from
            microorganisms.
  JOURNAL   Arch. Biochem. Biophys. 123 (1968) 572-88.
REFERENCE   2  [PMID:4199986]
  AUTHORS   Morihara K, Tsuzuki H, Oka T.
  TITLE     On the specificity of Pseudomonas aeruginosa alkaline proteinase
            with synthetic peptides.
  JOURNAL   Biochim. Biophys. Acta. 309 (1973) 414-29.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   3  [PMID:4212288]
  AUTHORS   Nakajima M, Mizusawa K, Yoshida F.
  TITLE     Purification and properties of an extracellular proteinase of
            psychrophilic Escherichia freundii.
  JOURNAL   Eur. J. Biochem. 44 (1974) 87-96.
  ORGANISM  Escherichia freundii
REFERENCE   4  [PMID:383155]
  AUTHORS   Decedue CJ, Broussard EA 2nd, Larson AD, Braymer HD.
  TITLE     Purification and characterization of the extracellular proteinase of
            Serratia marcescens.
  JOURNAL   Biochim. Biophys. Acta. 569 (1979) 293-301.
  ORGANISM  Serratia marcescens
REFERENCE   5  [PMID:6380155]
  AUTHORS   Doerr M, Traub WH.
  TITLE     Purification and characterization of two Serratia marcescens
            proteases.
  JOURNAL   Zentralbl. Bakteriol. Mikrobiol. Hyg. [A]. 257 (1984) 6-19.
  ORGANISM  Serratia marcescens
REFERENCE   6  [PMID:3016665]
  AUTHORS   Nakahama K, Yoshimura K, Marumoto R, Kikuchi M, Lee IS, Hase T,
            Matsubara H.
  TITLE     Cloning and sequencing of Serratia protease gene.
  JOURNAL   Nucleic. Acids. Res. 14 (1986) 5843-55.
  ORGANISM  Serratia marcescens
REFERENCE   7  [PMID:2211513]
  AUTHORS   Dahler GS, Barras F, Keen NT.
  TITLE     Cloning of genes encoding extracellular metalloproteases from
            Erwinia chrysanthemi EC16.
  JOURNAL   J. Bacteriol. 172 (1990) 5803-15.
  ORGANISM  Erwinia chrysanthemi
REFERENCE   8  [PMID:2123832]
  AUTHORS   Okuda K, Morihara K, Atsumi Y, Takeuchi H, Kawamoto S, Kawasaki H,
            Suzuki K, Fukushima J.
  TITLE     Complete nucleotide sequence of the structural gene for alkaline
            proteinase from Pseudomonas aeruginosa IFO 3455.
  JOURNAL   Infect. Immun. 58 (1990) 4083-8.
  ORGANISM  Pseudomonas aeruginosa
ORTHOLOGY   KO: K01406  serralysin
GENES       YPP: YPDSF_3337
            SPE: Spro_0210 Spro_2387
            PSB: Psyr_3163
            PFL: PFL_3210
            PEN: PSEEN1550(aprA)
            PMY: Pmen_4542
            SMD: Smed_5287
            RSH: Rsph17029_1872
            MMR: Mmar10_2493
            AVA: Ava_3643
STRUCTURES  PDB: 1AF0  1AKL  1G9K  1H71  1O0Q  1O0T  1OM6  1OM7  1OM8  1OMJ  
                 1SMP  1SRP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.40
            ExPASy - ENZYME nomenclature database: 3.4.24.40
            ExplorEnz - The Enzyme Database: 3.4.24.40
            ERGO genome analysis and discovery system: 3.4.24.40
            BRENDA, the Enzyme Database: 3.4.24.40
            CAS: 70851-98-8
///
ENTRY       EC 3.4.24.41                Enzyme
NAME        atrolysin B;
            Crotalus atrox metalloendopeptidase b;
            hemorrhagic toxin b;
            Ht-b
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of His5!Leu, His10!Leu, Ala14!Leu, Tyr16!Leu and Gly23!Phe
            of insulin B chain; identical to the cleavage of insulin B chain by
            atrolysin C. Also cleaves !Ser bonds in glucagon
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     From the venom of the western diamondback rattlesnake (Crotalus
            atrox). In peptidase family M12 (astacin family)
REFERENCE   1  [PMID:210790]
  AUTHORS   Bjarnason JB, Tu AT.
  TITLE     Hemorrhagic toxins from Western diamondback rattlesnake (Crotalus
            atrox) venom: isolation and characterization of five toxins and the
            role of zinc in hemorrhagic toxin e.
  JOURNAL   Biochemistry. 17 (1978) 3395-404.
  ORGANISM  Crotalus atrox
REFERENCE   2  [PMID:3060135]
  AUTHORS   Bjarnason JB, Hamilton D, Fox JW.
  TITLE     Studies on the mechanism of hemorrhage production by five
            proteolytic hemorrhagic toxins from Crotalus atrox venom.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 369 Suppl (1988) 121-9.
  ORGANISM  Crotalus atrox
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.41
            ExPASy - ENZYME nomenclature database: 3.4.24.41
            ExplorEnz - The Enzyme Database: 3.4.24.41
            ERGO genome analysis and discovery system: 3.4.24.41
            BRENDA, the Enzyme Database: 3.4.24.41
            CAS: 172306-48-8
///
ENTRY       EC 3.4.24.42                Enzyme
NAME        atrolysin C;
            Crotalus atrox metalloendopeptidase c;
            hemorrhagic toxin c and d
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of His5!Leu, His10!Leu, Ala14!Leu, Tyr16!Leu and Gly23!Phe
            bonds in B chain of insulin. With small molecule substrates prefers
            hydrophobic residue at P2' and small residue such as Ala, Gly at P1
INHIBITOR   Phosphoramidon [CPD:C00563]
COMMENT     A 24 kDa hemorrhagic endopeptidase from the venom of the western
            diamondback rattlesnake (Crotalus atrox) that digests type IV
            collagen, and exists as two forms, c and d. Phosphoramidon inhibits
            in the 0.1 mM range. In peptidase family M12 (astacin family).
            Hemorrhagic toxin-2 of C. ruber ruber has the same Mr and
            specificity and is a homologue [4,6]
REFERENCE   1  [PMID:210790]
  AUTHORS   Bjarnason JB, Tu AT.
  TITLE     Hemorrhagic toxins from Western diamondback rattlesnake (Crotalus
            atrox) venom: isolation and characterization of five toxins and the
            role of zinc in hemorrhagic toxin e.
  JOURNAL   Biochemistry. 17 (1978) 3395-404.
  ORGANISM  Crotalus atrox
REFERENCE   2  [PMID:3514216]
  AUTHORS   Fox JW, Campbell R, Beggerly L, Bjarnason JB.
  TITLE     Substrate specificities and inhibition of two hemorrhagic zinc
            proteases Ht-c and Ht-d from Crotalus atrox venom.
  JOURNAL   Eur. J. Biochem. 156 (1986) 65-72.
  ORGANISM  Crotalus atrox
REFERENCE   3  [PMID:3101740]
  AUTHORS   Bjarnason JB, Fox JW.
  TITLE     Characterization of two hemorrhagic zinc proteinases, toxin c and
            toxin d, from western diamondback rattlesnake (Crotalus atrox)
            venom.
  JOURNAL   Biochim. Biophys. Acta. 911 (1987) 356-63.
  ORGANISM  Crotalus atrox
REFERENCE   4  [PMID:2949699]
  AUTHORS   Mori N, Nikai T, Sugihara H, Tu AT.
  TITLE     Biochemical characterization of hemorrhagic toxins with
            fibrinogenase activity isolated from Crotalus ruber ruber venom.
  JOURNAL   Arch. Biochem. Biophys. 253 (1987) 108-21.
  ORGANISM  Crotalus ruber ruber
REFERENCE   5  [PMID:2745407]
  AUTHORS   Shannon JD, Baramova EN, Bjarnason JB, Fox JW.
  TITLE     Amino acid sequence of a Crotalus atrox venom metalloproteinase
            which cleaves type IV collagen and gelatin.
  JOURNAL   J. Biol. Chem. 264 (1989) 11575-83.
  ORGANISM  Crotalus atrox
REFERENCE   6  [PMID:2081731]
  AUTHORS   Takeya H, Onikura A, Nikai T, Sugihara H, Iwanaga S.
  TITLE     Primary structure of a hemorrhagic metalloproteinase, HT-2, isolated
            from the venom of Crotalus ruber ruber.
  JOURNAL   J. Biochem. (Tokyo). 108 (1990) 711-9.
  ORGANISM  Crotalus ruber ruber
STRUCTURES  PDB: 1ATL  1DTH  1HTD  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.42
            ExPASy - ENZYME nomenclature database: 3.4.24.42
            ExplorEnz - The Enzyme Database: 3.4.24.42
            ERGO genome analysis and discovery system: 3.4.24.42
            BRENDA, the Enzyme Database: 3.4.24.42
            CAS: 158886-17-0
///
ENTRY       EC 3.4.24.43                Enzyme
NAME        atroxase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of His5!Leu, Ser9!His, His10!Leu, Ala14!Leu and Tyr16!Leu
            of insulin B chain
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     A nonhemorrhagic endopeptidase from the venom of the western
            diamondback rattlesnake (Crotalus atrox) that cleaves fibrinogen. In
            peptidase family M12 (astacin family)
REFERENCE   1  [PMID:3167016]
  AUTHORS   Willis TW, Tu AT.
  TITLE     Purification and biochemical characterization of atroxase, a
            nonhemorrhagic fibrinolytic protease from western diamondback
            rattlesnake venom.
  JOURNAL   Biochemistry. 27 (1988) 4769-77.
  ORGANISM  Crotalus atrox
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.43
            ExPASy - ENZYME nomenclature database: 3.4.24.43
            ExplorEnz - The Enzyme Database: 3.4.24.43
            ERGO genome analysis and discovery system: 3.4.24.43
            BRENDA, the Enzyme Database: 3.4.24.43
            CAS: 181186-94-7
///
ENTRY       EC 3.4.24.44                Enzyme
NAME        atrolysin E;
            Crotalus atrox metalloendopeptidase e;
            hemorrhagic toxin e
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of Asn3!Gln, Ser9!His and Ala14!Leu bonds in insulin B
            chain and Tyr14!Gln and Thr8!Ser in A chain. Cleaves type IV
            collagen at Ala73!Gln in alpha1(IV) and at Gly7!Leu in alpha2(IV)
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     A 25.7 kDa hemorrhagic endopeptidase from the venom of the western
            diamondback rattlesnake (Crotalus atrox) that digests basement
            membrane components, including the triple helix of type IV collagen.
            Such action is believed to contribute to the hemorrhagic property by
            weakening capillary walls. In peptidase family M12 (astacin family)
REFERENCE   1  [PMID:210790]
  AUTHORS   Bjarnason JB, Tu AT.
  TITLE     Hemorrhagic toxins from Western diamondback rattlesnake (Crotalus
            atrox) venom: isolation and characterization of five toxins and the
            role of zinc in hemorrhagic toxin e.
  JOURNAL   Biochemistry. 17 (1978) 3395-404.
  ORGANISM  Crotalus atrox
REFERENCE   2  [PMID:6351911]
  AUTHORS   Bjarnason JB, Fox JW.
  TITLE     Proteolytic specificity and cobalt exchange of hemorrhagic toxin e,
            a zinc protease isolated from the venom of the western diamondback
            rattlesnake (Crotalus atrox).
  JOURNAL   Biochemistry. 22 (1983) 3770-8.
  ORGANISM  Crotalus atrox
REFERENCE   3  [PMID:2374521]
  AUTHORS   Baramova EN, Shannon JD, Bjarnason JB, Fox JW.
  TITLE     Identification of the cleavage sites by a hemorrhagic
            metalloproteinase in type IV collagen.
  JOURNAL   Matrix. 10 (1990) 91-7.
  ORGANISM  Crotalus atrox
STRUCTURES  PDB: 1KUF  1KUG  1KUI  1KUK  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.44
            ExPASy - ENZYME nomenclature database: 3.4.24.44
            ExplorEnz - The Enzyme Database: 3.4.24.44
            ERGO genome analysis and discovery system: 3.4.24.44
            BRENDA, the Enzyme Database: 3.4.24.44
            CAS: 172306-51-3
///
ENTRY       EC 3.4.24.45                Enzyme
NAME        atrolysin F;
            Crotalus atrox metalloendopeptidase;
            hemorrhagic toxin f;
            Crotalus atrox metalloendopeptidase f
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of Val2!Asn, Gln4!His, Leu6!Cys, His10!Leu, Ala14!Leu and
            Tyr16!Leu bonds in insulin B chain
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     A 64 kDa hemorrhagic endopeptidase from the venom of the western
            diamondback rattlesnake (Crotalus atrox) that digests the gamma
            chain of fibrinogen. Immunologically distinct from EC 3.4.24.1,
            atrolysin A.
REFERENCE   1  [PMID:6375570]
  AUTHORS   Nikai T, Mori N, Kishida M, Sugihara H, Tu AT.
  TITLE     Isolation and biochemical characterization of hemorrhagic toxin f
            from the venom of Crotalus atrox (western diamondback rattlesnake).
  JOURNAL   Arch. Biochem. Biophys. 231 (1984) 309-19.
  ORGANISM  Crotalus atrox
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.45
            ExPASy - ENZYME nomenclature database: 3.4.24.45
            ExplorEnz - The Enzyme Database: 3.4.24.45
            ERGO genome analysis and discovery system: 3.4.24.45
            BRENDA, the Enzyme Database: 3.4.24.45
            CAS: 172306-52-4
///
ENTRY       EC 3.4.24.46                Enzyme
NAME        adamalysin;
            Crotalus adamanteus metalloendopeptidase;
            proteinase I and II;
            Crotalus adamanteus venom proteinase II;
            adamalysin II
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of Phe1!Val, His5!Leu, His10!Leu, Ala14!Leu, Leu15!Tyr, and
            Tyr16!Leu of insulin B chain
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     From the venom of the eastern diamondback rattlesnake (Crotalus
            adamanteus). Two isoenzymes of approx. 24 kDa that inactivate
            alpha1-proteinase inhibitor by a single cleavage. In peptidase
            family M12 (astacin family)
REFERENCE   1  [PMID:309470]
  AUTHORS   Kurecki T, Laskowski M Sr, Kress LF.
  TITLE     Purification and some properties of two proteinases from Crotalus
            adamanteus venom that inactivate human alpha 1-proteinase inhibitor.
  JOURNAL   J. Biol. Chem. 253 (1978) 8340-5.
  ORGANISM  Crotalus adamanteus
STRUCTURES  PDB: 1IAG  2AIG  3AIG  4AIG  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.46
            ExPASy - ENZYME nomenclature database: 3.4.24.46
            ExplorEnz - The Enzyme Database: 3.4.24.46
            ERGO genome analysis and discovery system: 3.4.24.46
            BRENDA, the Enzyme Database: 3.4.24.46
            CAS: 74812-51-4
///
ENTRY       EC 3.4.24.47                Enzyme
NAME        horrilysin;
            Crotalus horridus metalloendopeptidase;
            hemorrhagic proteinase IV;
            Crotalus horridus horridus venom hemorrhagic proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of only the single bond Ala14!Leu in the insulin B chain,
            Ser12!Leu in the A chain, and Ile!Gly, Pro!Ala, and Ser!Trp in
            melittin
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     A 56 kDa hemorrhagic endopeptidase from the venom of the timber
            rattlesnake (Crotalus horridus horridus) that cleaves basement
            membrane, hide powder and fibrinogen.
REFERENCE   1  [PMID:6340728]
  AUTHORS   Civello DJ, Duong HL, Geren CR.
  TITLE     Isolation and characterization of a hemorrhagic proteinase from
            timber rattlesnake venom.
  JOURNAL   Biochemistry. 22 (1983) 749-55.
  ORGANISM  Crotalus horridus horridus
REFERENCE   2  [PMID:6340729]
  AUTHORS   Civello DJ, Moran JB, Geren CR.
  TITLE     Substrate specificity of a hemorrhagic proteinase from timber
            rattlesnake venom.
  JOURNAL   Biochemistry. 22 (1983) 755-62.
  ORGANISM  Crotalus horridus horridus
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.47
            ExPASy - ENZYME nomenclature database: 3.4.24.47
            ExplorEnz - The Enzyme Database: 3.4.24.47
            ERGO genome analysis and discovery system: 3.4.24.47
            BRENDA, the Enzyme Database: 3.4.24.47
            CAS: 84056-81-5
///
ENTRY       EC 3.4.24.48                Enzyme
NAME        ruberlysin;
            Crotalus ruber metalloendopeptidase II;
            hemorrhagic toxin II
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of His10!Leu, Ala14!Leu, Tyr16!Leu and Gly23!Phe bonds in
            the B chain of insulin; His!Pro, Pro!Phe, and Trp!Ser of angiotensin
            I; and Gly!Phe of Met enkephalin
COMMENT     A 25 kDa hemorrhagic endopeptidase from the venom of the red
            rattlesnake (Crotalus ruber ruber) that cleaves fibrinogen. In
            peptidase family M12 (astacin family)
REFERENCE   1  [PMID:2949699]
  AUTHORS   Mori N, Nikai T, Sugihara H, Tu AT.
  TITLE     Biochemical characterization of hemorrhagic toxins with
            fibrinogenase activity isolated from Crotalus ruber ruber venom.
  JOURNAL   Arch. Biochem. Biophys. 253 (1987) 108-21.
  ORGANISM  Crotalus ruber ruber
REFERENCE   2  [PMID:2081731]
  AUTHORS   Takeya H, Onikura A, Nikai T, Sugihara H, Iwanaga S.
  TITLE     Primary structure of a hemorrhagic metalloproteinase, HT-2, isolated
            from the venom of Crotalus ruber ruber.
  JOURNAL   J. Biochem. (Tokyo). 108 (1990) 711-9.
  ORGANISM  Crotalus ruber ruber
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.48
            ExPASy - ENZYME nomenclature database: 3.4.24.48
            ExplorEnz - The Enzyme Database: 3.4.24.48
            ERGO genome analysis and discovery system: 3.4.24.48
            BRENDA, the Enzyme Database: 3.4.24.48
///
ENTRY       EC 3.4.24.49                Enzyme
NAME        bothropasin;
            Bothrops jararaca venom metalloproteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of His5!Leu, His10!Leu, Ala14!Leu, Tyr16!Leu and Phe24!Phe
            in insulin B chain
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     Caseinolytic endopeptidase of jararaca snake (Bothrops jararaca)
            venom; 48 kDa. In peptidase family M12
REFERENCE   1  [PMID:6819660]
  AUTHORS   Mandelbaum FR, Reichel AP, Assakura MT.
  TITLE     Isolation and characterization of a proteolytic enzyme from the
            venom of the snake Bothrops jararaca (Jararaca).
  JOURNAL   Toxicon. 20 (1982) 955-72.
  ORGANISM  Bothrops jararaca
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.49
            ExPASy - ENZYME nomenclature database: 3.4.24.49
            ExplorEnz - The Enzyme Database: 3.4.24.49
            ERGO genome analysis and discovery system: 3.4.24.49
            BRENDA, the Enzyme Database: 3.4.24.49
            CAS: 84788-89-6
///
ENTRY       EC 3.4.24.50                Enzyme
NAME        bothrolysin;
            Bothrops metalloendopeptidase J;
            J protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of Gln4!His, Ser9!His and Ala14!Leu of insulin B chain and
            Pro!Phe of angiotensin I
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     A 22.5 kDa endopeptidase from the venom of the jararaca snake
            (Bothrops jararaca), insensitive to phosphoramidon at 0.5 mM. In
            peptidase family M12 (astacin family)
REFERENCE   1  [PMID:2781574]
  AUTHORS   Tanizaki MM, Zingali RB, Kawazaki H, Imajoh S, Yamazaki S, Suzuki K.
  TITLE     Purification and some characteristics of a zinc metalloprotease from
            the venom of Bothrops jararaca (jararaca).
  JOURNAL   Toxicon. 27 (1989) 747-55.
  ORGANISM  Bothrops jararaca
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.50
            ExPASy - ENZYME nomenclature database: 3.4.24.50
            ExplorEnz - The Enzyme Database: 3.4.24.50
            ERGO genome analysis and discovery system: 3.4.24.50
            BRENDA, the Enzyme Database: 3.4.24.50
///
ENTRY       EC 3.4.24.51                Enzyme
NAME        ophiolysin;
            Ophiophagus metalloendopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of Asn3!Gln, Gln4!His, His10!Leu, Ala14!Leu, and Tyr16!Leu
            in insulin B chain
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     A 70 kDa endopeptidase from the venom of the king cobra (Ophiophagus
            hannah)
REFERENCE   1  [PMID:3070833]
  AUTHORS   Yamakawa Y, Omori-Satoh T.
  TITLE     A protease in the venom of king cobra (Ophiophagus hannah):
            purification, characterization and substrate specificity on oxidized
            insulin B-chain.
  JOURNAL   Toxicon. 26 (1988) 1145-55.
  ORGANISM  Ophiophagus hannah
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.51
            ExPASy - ENZYME nomenclature database: 3.4.24.51
            ExplorEnz - The Enzyme Database: 3.4.24.51
            ERGO genome analysis and discovery system: 3.4.24.51
            BRENDA, the Enzyme Database: 3.4.24.51
///
ENTRY       EC 3.4.24.52                Enzyme
NAME        trimerelysin I;
            Trimeresurus metalloendopeptidase I;
            hemorrhagic proteinase HR1A;
            hemorrhagic metalloproteinase HR1A;
            metalloproteinase HR1A
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of only two bonds His10!Leu and Ala14!Leu in the insulin B
            chain
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     A 60 kDa hemorrhagic endopeptidase of pI 4.4 from the venom of the
            habu snake (Trimeresurus flavoviridis). In peptidase family M12
            (astacin family)
REFERENCE   1  [PMID:518906]
  AUTHORS   Omori-Satoh T, Sadahiro S.
  TITLE     Resolution of the major hemorrhagic component of Trimeresurus
            flavoviridis venom into two parts.
  JOURNAL   Biochim. Biophys. Acta. 580 (1979) 392-404.
  ORGANISM  Trimeresurus flavoviridis
REFERENCE   2  [PMID:3284004]
  AUTHORS   Yamakawa Y, Omori-Satoh T.
  TITLE     The sites of cleavage in oxidized insulin-B chain by a hemorrhagic
            protease derived from the venom of the habu (Trimeresurus
            flavoviridis).
  JOURNAL   Toxicon. 26 (1988) 227-31.
  ORGANISM  Trimeresurus flavoviridis
REFERENCE   3  [PMID:2398046]
  AUTHORS   Takeya H, Oda K, Miyata T, Omori-Satoh T, Iwanaga S.
  TITLE     The complete amino acid sequence of the high molecular mass
            hemorrhagic protein HR1B isolated from the venom of Trimeresurus
            flavoviridis.
  JOURNAL   J. Biol. Chem. 265 (1990) 16068-73.
  ORGANISM  Trimeresurus flavoviridis
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.52
            ExPASy - ENZYME nomenclature database: 3.4.24.52
            ExplorEnz - The Enzyme Database: 3.4.24.52
            ERGO genome analysis and discovery system: 3.4.24.52
            BRENDA, the Enzyme Database: 3.4.24.52
            CAS: 151125-16-5
///
ENTRY       EC 3.4.24.53                Enzyme
NAME        trimerelysin II;
            Trimeresurus metalloendopeptidase II;
            proteinase H2;
            H2-proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of Asn3!Gln, His10!Leu and Ala14!Leu in the insulin B
            chain, and the bond Z-Gly-Pro!Leu-Gly-Pro in a small molecule
            substrate of microbial collagenase
COMMENT     A 24 kDa nonhemorrhagic endopeptidase from the venom of the habu
            snake (Trimeresurus flavoviridis). In peptidase family M12 (astacin
            family)
REFERENCE   1  [PMID:4984550]
  AUTHORS   Takahashi T, Ohsaka A.
  TITLE     Purification and characterization of a proteinase in the venom of
            Trimeresurus flavoviridis. Complete separation of the enzyme from
            hemorrhagic activity.
  JOURNAL   Biochim. Biophys. Acta. 198 (1970) 293-307.
  ORGANISM  Trimeresurus flavoviridis
REFERENCE   2  [PMID:2777746]
  AUTHORS   Takeya H, Arakawa M, Miyata T, Iwanaga S, Omori-Satoh T.
  TITLE     Primary structure of H2-proteinase, a non-hemorrhagic
            metalloproteinase, isolated from the venom of the habu snake,
            Trimeresurus flavoviridis.
  JOURNAL   J. Biochem. (Tokyo). 106 (1989) 151-7.
  ORGANISM  Trimeresurus flavoviridis
STRUCTURES  PDB: 1WNI  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.53
            ExPASy - ENZYME nomenclature database: 3.4.24.53
            ExplorEnz - The Enzyme Database: 3.4.24.53
            ERGO genome analysis and discovery system: 3.4.24.53
            BRENDA, the Enzyme Database: 3.4.24.53
            CAS: 151125-15-4
///
ENTRY       EC 3.4.24.54                Enzyme
NAME        mucrolysin;
            Trimeresurus metalloendopeptidase A;
            mucrotoxin A
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of Ser9!His, His10!Leu, Ala14!Leu, Leu15!Tyr and Tyr16!Leu
            bonds in insulin B chain
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     A 94 kDa hemorrhagic and fibrinogenolytic endopeptidase from the
            Chinese habu snake (Trimeresurus mucrosquamatus) venom. In peptidase
            family M12 (astacin family)
REFERENCE   1  [PMID:6857709]
  AUTHORS   Sugihara H, Moriura M, Nikai T.
  TITLE     Purification and properties of a lethal, hemorrhagic protein,
            &quot;Mucrotoxin A&quot;, from the venom of the Chinese habu snake
            (Trimeresurus mucrosquamatus).
  JOURNAL   Toxicon. 21 (1983) 247-55.
  ORGANISM  Trimeresurus mucrosquamatus
REFERENCE   2  [PMID:6857709]
  AUTHORS   Sugihara H, Moriura M, Nikai T.
  TITLE     Purification and properties of a lethal, hemorrhagic protein,
            &quot;Mucrotoxin A&quot;, from the venom of the Chinese habu snake
            (Trimeresurus mucrosquamatus).
  JOURNAL   Toxicon. 21 (1983) 247-55.
  ORGANISM  Trimeresurus mucrosquamatus
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.54
            ExPASy - ENZYME nomenclature database: 3.4.24.54
            ExplorEnz - The Enzyme Database: 3.4.24.54
            ERGO genome analysis and discovery system: 3.4.24.54
            BRENDA, the Enzyme Database: 3.4.24.54
            CAS: 85898-38-0
///
ENTRY       EC 3.4.24.55                Enzyme
NAME        pitrilysin;
            Escherichia coli protease III;
            protease Pi;
            proteinase Pi;
            PTR;
            Escherichia coli metalloproteinase Pi
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Preferential cleavage of -Tyr16! Leu- and -Phe25! Tyr-bonds of
            oxidized insulin B chain. Also acts on other substrates of less than
            7 kDa such as insulin and glucagon
COFACTOR    Zinc [CPD:C00038]
INHIBITOR   EDTA [CPD:C00284];
            1,10-Phenanthroline [CPD:C00604]
COMMENT     From the periplasmic space of Escherichia coli. Inhibited by EDTA
            and 1,10-phenanthroline; not thiol-dependent. Type example of
            peptidase family M16
REFERENCE   1  [PMID:3534791]
  AUTHORS   Finch PW, Wilson RE, Brown K, Hickson ID, Emmerson PT.
  TITLE     Complete nucleotide sequence of the Escherichia coli ptr gene
            encoding protease III.
  JOURNAL   Nucleic. Acids. Res. 14 (1986) 7695-703.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:3059494]
  AUTHORS   Affholter JA, Fried VA, Roth RA.
  TITLE     Human insulin-degrading enzyme shares structural and functional
            homologies with E. coli protease III.
  JOURNAL   Science. 242 (1988) 1415-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:1570301]
  AUTHORS   Becker AB, Roth RA.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 3835-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:1733942]
  AUTHORS   Ding L, Becker AB, Suzuki A, Roth RA.
  TITLE     Comparison of the enzymatic and biochemical properties of human
            insulin-degrading enzyme and Escherichia coli protease III.
  JOURNAL   J. Biol. Chem. 267 (1992) 2414-20.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:7680857]
  AUTHORS   Anastasi A, Knight CG, Barrett AJ.
  TITLE     Characterization of the bacterial metalloendopeptidase pitrilysin by
            use of a continuous fluorescence assay.
  JOURNAL   Biochem. J. 290 ( Pt 2) (1993) 601-7.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01407  protease III
GENES       ECO: b2821(ptr)
            ECJ: JW2789(ptr)
            ECE: Z4138(ptr)
            ECS: ECs3678
            ECC: c3415(ptr)
            ECI: UTI89_C3222(ptrA)
            ECP: ECP_2833
            ECW: EcE24377A_3141(ptrA)
            ECX: EcHS_A2967
            STY: STY3133(ptr)
            STT: t2903(ptr)
            SPT: SPA2860(ptr)
            SEC: SC2933(ptr)
            STM: STM2995(ptr)
            YPE: YPO1019(ptrA)
            YPK: y3165(ptr)
            YPM: YP_2882(ptrA)
            YPA: YPA_0491
            YPN: YPN_2982
            YPS: YPTB3026(ptrA)
            YPI: YpsIP31758_0990(ptrA)
            SFL: SF2832(ptr)
            SFX: S3029(ptr)
            SFV: SFV_2899(ptr)
            SSN: SSON_2978(ptr)
            SBO: SBO_2711(ptr)
            SDY: SDY_3038(ptr)
            ECA: ECA0994(ptrA)
            PLU: plu0631(ptrA)
            SGL: SG1974
            HDU: HD0187(ptrA)
            APL: APL_1883(ptrA)
            PEN: PSEEN0399(pqqF)
            ILO: IL2336(ptr)
STRUCTURES  PDB: 1Q2L  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.55
            ExPASy - ENZYME nomenclature database: 3.4.24.55
            ExplorEnz - The Enzyme Database: 3.4.24.55
            ERGO genome analysis and discovery system: 3.4.24.55
            BRENDA, the Enzyme Database: 3.4.24.55
            CAS: 81611-78-1
///
ENTRY       EC 3.4.24.56                Enzyme
NAME        insulysin;
            insulinase;
            insulin-degrading enzyme;
            insulin protease;
            insulin proteinase;
            insulin-degrading neutral proteinase;
            insulin-specific protease;
            insulin-glucagon protease;
            metalloinsulinase;
            IDE
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Degradation of insulin, glucagon and other polypeptides. No action
            on proteins
COFACTOR    Zinc [CPD:C00038]
INHIBITOR   EDTA [CPD:C00284];
            1,10-Phenanthroline [CPD:C00604];
            Bacitracin [CPD:C01667];
            N-Ethylmaleimide [CPD:C02441]
COMMENT     A 110 kDa cytosolic enzyme, known from mammals and the fruit fly,
            Drosophila melanogaster. Inhibited by bacitracin, chelating agents
            EDTA and 1,10-phenanthroline, and by thiol-blocking reagents such as
            N-ethylmaleimide, but not by phosphoramidon. In peptidase family M16
            (pitrilysin family).
REFERENCE   1  [PMID:3061785]
  AUTHORS   Duckworth WC.
  TITLE     Insulin degradation: mechanisms, products, and significance.
  JOURNAL   Endocr. Rev. 9 (1988) 319-45.
REFERENCE   2  [PMID:2293021]
  AUTHORS   Affholter JA, Hsieh CL, Francke U, Roth RA.
  TITLE     Insulin-degrading enzyme: stable expression of the human
            complementary DNA, characterization of its protein product, and
            chromosomal mapping of the human and mouse genes.
  JOURNAL   Mol. Endocrinol. 4 (1990) 1125-35.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:1689296]
  AUTHORS   Duckworth WC, Hamel FG, Bennett R, Ryan MP, Roth RA.
  TITLE     Human red blood cell insulin-degrading enzyme and rat skeletal
            muscle insulin protease share antigenic sites and generate identical
            products from insulin.
  JOURNAL   J. Biol. Chem. 265 (1990) 2984-7.
  ORGANISM  human [GN:hsa], rat [GN:rno]
REFERENCE   4  [PMID:2126597]
  AUTHORS   Kuo WL, Gehm BD, Rosner MR.
  TITLE     Cloning and expression of the cDNA for a Drosophila
            insulin-degrading enzyme.
  JOURNAL   Mol. Endocrinol. 4 (1990) 1580-91.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:1733942]
  AUTHORS   Ding L, Becker AB, Suzuki A, Roth RA.
  TITLE     Comparison of the enzymatic and biochemical properties of human
            insulin-degrading enzyme and Escherichia coli protease III.
  JOURNAL   J. Biol. Chem. 267 (1992) 2414-20.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map05010  Alzheimer's disease
ORTHOLOGY   KO: K01408  insulysin
GENES       HSA: 3416(IDE)
            PTR: 450608(IDE)
            MMU: 15925(Ide)
            RNO: 25700(Ide)
            CFA: 477768(IDE)
            BTA: 523752(LOC523752)
            GGA: 423814(IDE)
            DRE: 561390(LOC561390)
            SPU: 591315(LOC591315)
            DME: Dmel_CG5517(Ide)
            CEL: F44E7.4(peptidase)
            ATH: AT2G41790
            OSA: 4343659
            CME: CMO219C
            ANI: AN8044.2
            AFM: AFUA_5G02010
            AOR: AO090003001317
            CNE: CNL05710
            ECU: ECU06_0750
            DDI: DDBDRAFT_0187681
            CPV: cgd2_930
            CHO: Chro.20104
            TET: TTHERM_00101300 TTHERM_00181080 TTHERM_00300360
                 TTHERM_00624110 TTHERM_00939020 TTHERM_01108740
                 TTHERM_01165230
            TBR: Tb927.8.7020
            TCR: 507389.70 509911.90
            LMA: LmjF31.3090
            VFI: VF1809
            SHE: Shewmr4_1412
            BCZ: BCZK3546
            SAA: SAUSA300_1172
            LLM: llmg_2226
            CTR: CT806(ptr)
            CTA: CTA_0878(ptr)
            CMU: TC0190
            CPN: CPn0957(ide)
            CPA: CP0903
            CPJ: CPj0957(ide)
            CPT: CpB0994
            CCA: CCA00812(ide)
            CAB: CAB782
            CFE: CF0203(ide2)
STRUCTURES  PDB: 2G47  2G48  2G49  2G54  2G56  2JBU  2JG4  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.56
            ExPASy - ENZYME nomenclature database: 3.4.24.56
            ExplorEnz - The Enzyme Database: 3.4.24.56
            ERGO genome analysis and discovery system: 3.4.24.56
            BRENDA, the Enzyme Database: 3.4.24.56
            CAS: 9013-83-6
///
ENTRY       EC 3.4.24.57                Enzyme
NAME        O-sialoglycoprotein endopeptidase;
            glycoprotease;
            glycophorin A proteinase;
            glycoproteinase;
            sialoglycoprotease;
            sialoglycoproteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of O-sialoglycoproteins; cleaves -Arg31!Asp- bond in
            glycophorin A. Does not cleave unglycosylated proteins, desialylated
            glycoproteins or glycoproteins that are only N-glycosylated
COMMENT     An enzyme secreted by the bacterium Pasteurella haemolytica.
            Inhibited by EDTA (100 mM) and 1,10-phenanthroline. Type example of
            peptidase family M22
REFERENCE   1  [PMID:1885539]
  AUTHORS   Abdullah KM, Lo RY, Mellors A.
  TITLE     Cloning, nucleotide sequence, and expression of the Pasteurella
            haemolytica A1 glycoprotease gene.
  JOURNAL   J. Bacteriol. 173 (1991) 5597-603.
  ORGANISM  Pasteurella haemolytica
REFERENCE   2  [PMID:1729196]
  AUTHORS   Abdullah KM, Udoh EA, Shewen PE, Mellors A.
  TITLE     A neutral glycoprotease of Pasteurella haemolytica A1 specifically
            cleaves O-sialoglycoproteins.
  JOURNAL   Infect. Immun. 60 (1992) 56-62.
  ORGANISM  Pasteurella haemolytica
REFERENCE   3  [PMID:1371528]
  AUTHORS   Sutherland DR, Abdullah KM, Cyopick P, Mellors A.
  TITLE     Cleavage of the cell-surface O-sialoglycoproteins CD34, CD43, CD44,
            and CD45 by a novel glycoprotease from Pasteurella haemolytica.
  JOURNAL   J. Immunol. 148 (1992) 1458-64.
  ORGANISM  Pasteurella haemolytica
ORTHOLOGY   KO: K01409  O-sialoglycoprotein endopeptidase
GENES       HSA: 55644(OSGEP)
            PTR: 473320(OSGEP)
            MMU: 66246(Osgep)
            RNO: 290028(Osgep)
            BTA: 507512(OSGEP)
            XLA: 380480(osgep)
            XTR: 548866(osgep)
            DRE: 550447(zgc:112527)
            SPU: 581023(LOC581023)
            DME: Dmel_CG4933
            CEL: Y71H2AM.1
            OSA: 4338033
            CME: CMD081C
            SCE: YKR038C(KAE1)
            AGO: AGOS_AEL316W
            PIC: PICST_57141
            CAL: CaO19_3787(CaO19.3787)
            CGR: CAGL0L03245g
            SPO: SPBC16D10.03
            ANI: AN6569.2
            AFM: AFUA_6G04510 AFUA_7G05240
            AOR: AO090701000097
            CNE: CNA03390
            UMA: UM00617.1 UM02328.1
            ECU: ECU09_0140
            DDI: DDBDRAFT_0189338
            PFA: MAL7P1.26
            TAN: TA07680
            TPV: TP04_0293
            TBR: Tb927.7.6470
            TCR: 506515.20
            LMA: LmjF31.0100
            EHI: 124.t00018
            ECO: b3064(ygjD)
            ECJ: JW3036(ygjD)
            ECE: Z4417(ygjD)
            ECS: ECs3947
            ECC: c3815(ygjD)
            ECI: UTI89_C2001(yeaZ) UTI89_C3500(ygjD)
            ECP: ECP_3154
            ECV: APECO1_3350(ygjD)
            ECW: EcE24377A_3528(gcp)
            ECX: EcHS_A3244(gcp)
            STY: STY3387
            STT: t3128
            SPT: SPA3076(gcp)
            SEC: SC3155(gcp)
            STM: STM3208(gcp)
            YPE: YPO0646(gcp)
            YPK: y3534
            YPM: YP_2961(gcp)
            YPA: YPA_3144
            YPN: YPN_0506
            YPP: YPDSF_0430
            YPS: YPTB3415(gcp)
            YPI: YpsIP31758_0556(gcp)
            SFL: SF3105(ygjD)
            SFX: S3310(ygjD)
            SFV: SFV_3104(ygjD)
            SSN: SSON_3201(ygjD)
            SBO: SBO_2922(ygjD)
            SDY: SDY_3248(ygjD)
            ECA: ECA0683(gcp)
            PLU: plu3976(gcp)
            BUC: BU058(ygjD)
            BAS: BUsg055(gcp)
            BAB: bbp055(gcp)
            BCC: BCc_037(gcp)
            WBR: WGLp471(ygjD)
            SGL: SG0254
            ENT: Ent638_3470
            SPE: Spro_4297
            BFL: Bfl059(gcp)
            BPN: BPEN_060(gcp)
            HIT: NTHI0656(gcp)
            HDU: HD0471(gcp)
            HSO: HS_0411(gcp)
            PMU: PM1238(gcp)
            MSU: MS1763(qRI7)
            APL: APL_1120(gcp)
            ASU: Asuc_2013
            XFA: XF0435
            XFT: PD1643(gcp)
            XCC: XCC3816(gcp)
            XCB: XC_3888
            XCV: XCV3990(gcp)
            XAC: XAC3871(gcp)
            XOO: XOO4125(gcp)
            XOM: XOO_3901(XOO3901)
            VCO: VC0395_A0049(gcp)
            VVU: VV1_0628
            VVY: VV0565
            VPA: VP0408
            VFI: VF2249
            PPR: PBPRA0434
            PAE: PA0580(gcp)
            PAU: PA14_07570(gcp)
            PPU: PP_0390(gcp)
            PPF: Pput_0424
            PST: PSPTO_0540(gcp)
            PSB: Psyr_4638
            PSP: PSPPH_0622(gcp)
            PFL: PFL_5660(gcp)
            PFO: Pfl_5146
            PEN: PSEEN0417(gcp)
            PMY: Pmen_4025
            PAR: Psyc_0214(ygjD)
            PCR: Pcryo_0234
            PRW: PsycPRwf_0363
            ACI: ACIAD1332
            SON: SO_1289(gcp)
            SDN: Sden_2830
            SFR: Sfri_2992
            SAZ: Sama_0827
            SBL: Sbal_1148
            SBM: Shew185_1192
            SLO: Shew_1000
            SPC: Sputcn32_1108
            SSE: Ssed_1076
            SPL: Spea_0962
            SHE: Shewmr4_2904
            SHM: Shewmr7_2986
            SHN: Shewana3_3083
            SHW: Sputw3181_3056
            ILO: IL1970
            CPS: CPS_4338(gcp)
            PHA: PSHAa2304(gcp)
            PAT: Patl_1042
            SDE: Sde_0720
            PIN: Ping_0314(gcp)
            MAQ: Maqu_0661
            CBU: CBU_1240(gcp)
            CBD: COXBU7E912_1324(gcp)
            LPN: lpg2357(gcp)
            LPF: lpl2279(gcp)
            LPP: lpp2306(gcp)
            MCA: MCA2990(gcp)
            FTU: FTT0147(gcp)
            FTF: FTF0147(gcp)
            FTL: FTL_1741
            FTH: FTH_1680(gcp)
            FTN: FTN_1565(gcp)
            TCX: Tcr_1810
            NOC: Noc_0041
            AEH: Mlg_2520
            HHA: Hhal_2327
            HCH: HCH_06270
            CSA: Csal_0973
            ABO: ABO_2059(gcp)
            MMW: Mmwyl1_1045
            AHA: AHA_0831(gcp)
            DNO: DNO_0018
            BCI: BCI_0619(gcp)
            RMA: Rmag_0980
            VOK: COSY_0878(gcp)
            NME: NMB1802
            NMA: NMA0661(gcp)
            NMC: NMC0419(gcp)
            NGO: NGO0104
            CVI: CV_2757(gcp)
            RSO: RSc2219(gcp)
            REU: Reut_A0884
            REH: H16_A2730(gcp)
            RME: Rmet_2612
            BMA: BMAA0334(gcp)
            BMV: BMASAVP1_1515(gcp)
            BML: BMA10299_1708(gcp)
            BMN: BMA10247_A0367(gcp)
            BXE: Bxe_B2825
            BVI: Bcep1808_4259
            BUR: Bcep18194_B2209
            BCN: Bcen_4484
            BCH: Bcen2424_3881
            BAM: Bamb_3252
            BPS: BPSS1760(gcp)
            BPM: BURPS1710b_A0839(gcp)
            BPL: BURPS1106A_A2389(gcp)
            BPD: BURPS668_A2531(gcp)
            BTE: BTH_II0616
            PNU: Pnuc_1702
            BPE: BP1716(gcp)
            BPA: BPP3059(gcp)
            BBR: BB3022(gcp)
            RFR: Rfer_2068
            POL: Bpro_3265
            PNA: Pnap_1416
            AAV: Aave_2151
            AJS: Ajs_2828
            VEI: Veis_1335
            MPT: Mpe_A1395
            HAR: HEAR0426
            MMS: mma_0478(gcp)
            NEU: NE0225(gcp)
            NET: Neut_0296
            NMU: Nmul_A2061
            EBA: ebA4371(gcp)
            AZO: azo3224(gcp)
            DAR: Daro_0530
            TBD: Tbd_2384
            MFA: Mfla_2326
            HPY: HP1584(gcp)
            HPA: HPAG1_1532
            HHE: HH1842(gcp)
            HAC: Hac_0281(gcp)
            WSU: WS1600
            TDN: Tmden_0131
            CJE: Cj1344c
            CJR: CJE1533(gcp)
            CJJ: CJJ81176_1343(gcp)
            CJU: C8J_1260
            CJD: JJD26997_0366(gcp)
            CFF: CFF8240_0215
            CCV: CCV52592_0591
            CHA: CHAB381_0120
            ABU: Abu_0164(gcp)
            NIS: NIS_1663
            SUN: SUN_0142
            GSU: GSU1865
            GME: Gmet_1303
            GUR: Gura_2310
            PCA: Pcar_1850
            PPD: Ppro_2493
            DVU: DVU1840
            DVL: Dvul_1322
            DDE: Dde_2068
            LIP: LI0368(ygjD)
            BBA: Bd0636(gcp) Bd3788
            DPS: DP2173
            ADE: Adeh_3687
            AFW: Anae109_3813
            MXA: MXAN_2051(gcp)
            SAT: SYN_00423
            SFU: Sfum_3311
            RPR: RP037
            RTY: RT0093(gcp)
            RCO: RC0061(gcp)
            RFE: RF_0146(gcp)
            RBE: RBE_1260(gcp)
            RCM: A1E_00175
            OTS: OTBS_1219(gcp)
            WOL: WD0699
            WBM: Wbm0217
            AMA: AM561 AM572(gcp)
            APH: APH_0626
            ERU: Erum4060(gcp)
            ERW: ERWE_CDS_04190(gcp)
            ERG: ERGA_CDS_04140(gcp)
            ECN: Ecaj_0395
            ECH: ECH_0644
            NSE: NSE_0236
            PUB: SAR11_0311(ygjD)
            MLO: mlr4224(gcp)
            MES: Meso_3203
            PLA: Plav_1348
            SME: SMc03230(gcp)
            SMD: Smed_2965
            ATU: Atu2651(gcp)
            ATC: AGR_C_4806
            RET: RHE_CH00380 RHE_CH03903(gcp)
            RLE: RL0399 RL4494(gcp)
            BME: BMEI0175 BMEI1979
            BMF: BAB1_1888(gcp) BAB1_2151
            BMS: BR1888(gcp)
            BMB: BruAb1_1865(gcp)
            BOV: BOV_1816(gcp)
            OAN: Oant_0974
            BJA: blr0567(gcp)
            BRA: BRADO0037
            BBT: BBta_0042
            RPA: RPA0255(gcp)
            RPB: RPB_0315
            RPC: RPC_0046 RPC_0464
            RPD: RPD_0470
            RPE: RPE_0065 RPE_0210
            NWI: Nwi_0011 Nwi_0470
            NHA: Nham_0561
            BHE: BH16110
            BQU: BQ13010
            XAU: Xaut_1157
            CCR: CC_0071
            SIL: SPO3854
            SIT: TM1040_2829
            RSP: RSP_1509
            RSH: Rsph17029_0161
            RSQ: Rsph17025_2914
            JAN: Jann_4080
            RDE: RD1_0470(gcp) RD1_1649
            PDE: Pden_1998
            MMR: Mmar10_0039
            HNE: HNE_0136(gcp)
            ZMO: ZMO1904
            NAR: Saro_2785
            SAL: Sala_2875
            SWI: Swit_1933
            ELI: ELI_09160
            GOX: GOX1882
            GBE: GbCGDNIH1_2425
            ACR: Acry_0129
            RRU: Rru_A3569
            MAG: amb4419
            MGM: Mmc1_0740
            ABA: Acid345_0494
            SUS: Acid_6190
            BSU: BG12202(gcp)
            BHA: BH0548
            BAN: BA0261(gcP)
            BAR: GBAA0261(gcP)
            BAA: BA_0832
            BAT: BAS0247
            BCE: BC0289
            BCA: BCE_0282(gcp)
            BCZ: BCZK0233 BCZK0235(gcp)
            BCY: Bcer98_0246
            BTK: BT9727_0233(gcp)
            BTL: BALH_0244(gcp) BALH_0246(gcp)
            BLI: BL00845(gcp)
            BLD: BLi00615(gcp)
            BCL: ABC0871(gcp)
            BPU: BPUM_0525(gcp)
            OIH: OB0648
            GKA: GK0239
            GTN: GTNG_0214
            SAU: SA1854
            SAV: SAV2049
            SAM: MW1973
            SAR: SAR2136
            SAS: SAS1954
            SAC: SACOL2038
            SAB: SAB1934c SAB1936c
            SAA: SAUSA300_2002
            SAO: SAOUHSC_02277
            SAJ: SaurJH9_2086
            SAH: SaurJH1_2123
            SEP: SE1650
            SER: SERP1661
            SHA: SH0984
            SSP: SSP0829
            LMO: lmo2075
            LMF: LMOf2365_2107
            LIN: lin2181
            LWE: lwe2096
            LLA: L93500(gcp)
            LLC: LACR_0330
            LLM: llmg_0309(gcp)
            SPY: SPy_1872
            SPZ: M5005_Spy_1591
            SPM: spyM18_1937
            SPG: SpyM3_1616(gcp)
            SPS: SPs0251
            SPH: MGAS10270_Spy1662
            SPI: MGAS10750_Spy1649
            SPJ: MGAS2096_Spy1616 MGAS2096_Spy1617
            SPK: MGAS9429_Spy1596
            SPF: SpyM50260
            SPA: M6_Spy1602
            SPB: M28_Spy1583
            SPN: SP_0129
            SPR: spr0131(gcp)
            SPD: SPD_0136
            SAG: SAG1757
            SAN: gbs1800
            SAK: SAK_1779
            SMU: SMU.387
            STC: str1770(gcp)
            STL: stu1770(gcp)
            STE: STER_1745
            SSA: SSA_0318(gcp)
            SSU: SSU05_0166
            SSV: SSU98_0169
            SGO: SGO_0221 SGO_0223
            LPL: lp_0721(gcp)
            LJO: LJ0436
            LAC: LBA0390
            LSA: LSA0351
            LSL: LSL_1216(gcp)
            LDB: Ldb1621(gcp)
            LBU: LBUL_1501
            LBR: LVIS_0612
            LCA: LSEI_2248
            LGA: LGAS_0381
            LRE: Lreu_0343
            PPE: PEPE_1472
            EFA: EF2472(gcp)
            OOE: OEOE_1399
            LME: LEUM_1775
            STH: STH1848 STH2921
            CAC: CAC0901
            CPE: CPE2232
            CPF: CPF_2496(gcp)
            CPR: CPR_2202(gcp)
            CTC: CTC02432 CTC02444
            CNO: NT01CX_0478
            CTH: Cthe_2743
            CDF: CD0152(gcp) CD1202(gcp)
            CBE: Cbei_0377
            CKL: CKL_0446(gcp)
            AMT: Amet_0808 Amet_2502
            CHY: CHY_0725(gcp) CHY_1993
            DSY: DSY2363 DSY3974
            DRM: Dred_2885
            PTH: PTH_2656(QRI7)
            SWO: Swol_1866
            CSC: Csac_2375
            TTE: TTE0538(qri7)
            MTA: Moth_1520 Moth_2157
            MGE: MG_046
            MPN: MPN059(gcp)
            MPU: MYPU_1180(gcp)
            MPE: MYPE8610(gcp)
            MGA: MGA_0129
            MMY: MSC_0083(gcp)
            MMO: MMOB1300(gcp)
            MHY: mhp656(gcp)
            MHJ: MHJ_0636(gcp)
            MHP: MHP7448_0635(gcp)
            MSY: MS53_0015(gcp)
            MCP: MCAP_0821
            UUR: UU411(gcp)
            POY: PAM579(QRI7)
            AYW: AYWB_251(qri7)
            MFL: Mfl484
            MTU: Rv3419c(gcp)
            MTC: MT3528(gcp)
            MBO: Mb3453c(gcp)
            MBB: BCG_3489c(gcp)
            MLE: ML0379(gcp)
            MPA: MAP4263(gcp)
            MSM: MSMEG_1580
            MVA: Mvan_1489
            MGI: Mflv_4929
            MMC: Mmcs_1151
            MKM: Mkms_1168
            MJL: Mjls_1178
            CGL: NCgl0569(cgl0594)
            CGB: cg0687(gcp)
            CEF: CE0599
            CDI: DIP0574
            CJK: jk1731(gcp)
            NFA: nfa8840
            SCO: SCO4752(gcp)
            SMA: SAV4974(gcp)
            TWH: TWT591(gcp)
            TWS: TW170(gcp)
            LXX: Lxx19910(gcp)
            ART: Arth_2892
            PAC: PPA1782
            NCA: Noca_3657
            TFU: Tfu_2602
            FRA: Francci3_2662
            FAL: FRAAL2797
            ACE: Acel_0360
            KRA: Krad_0403
            SEN: SACE_6723(gcp)
            STP: Strop_3851
            BLO: BL1457(gcp)
            BAD: BAD_0857(gcp)
            RXY: Rxyl_0812
            FNU: FN0549 FN0928
            RBA: RB9084
            CTR: CT197(gcp_1)
            CTA: CTA_0215(gcp) CTA_0372
            CMU: TC0470
            CPN: CPn0194(gcp_2)
            CPA: CP0573
            CPJ: CPj0194(gcp_2)
            CPT: CpB0197
            CCA: CCA00542(gcp_2)
            CAB: CAB528
            CFE: CF0466(gcp2)
            PCU: pc0818
            BGA: BG0792(gcp)
            BAF: BAPKO_0817(gcp)
            TPA: TP0680
            TDE: TDE2504(gcp)
            LIL: LA1450
            LIC: LIC12302
            LBJ: LBJ_1982
            LBL: LBL_1068
            SYN: slr0807(gcp)
            SYW: SYNW1834
            SYC: syc0299_c
            SYF: Synpcc7942_1251
            SYD: Syncc9605_0635
            SYE: Syncc9902_1727
            SYG: sync_2156(gcp)
            SYR: SynRCC307_0711(gcp)
            SYX: SynWH7803_1843(gcp)
            CYA: CYA_0297(gcp)
            CYB: CYB_2822(gcp)
            TEL: tll0502
            GVI: gll1354
            ANA: alr0110
            AVA: Ava_1479
            PMA: Pro0468(QRI7)
            PMM: PMM0470
            PMT: PMT1315
            PMN: PMN2A_1802
            PMI: PMT9312_0470
            PMB: A9601_05251(qri7)
            PMC: P9515_05341(qri7)
            PMF: P9303_06711(qri7)
            PMG: P9301_04951(qri7)
            PMH: P9215_05501(qri7)
            PME: NATL1_05251(qri7)
            TER: Tery_1635
            BTH: BT_0920
            BFR: BF2431
            BFS: BF2512
            PGI: PG1724(gcp)
            SRU: SRU_2545(gcp)
            CHU: CHU_1957(gcp)
            FJO: Fjoh_4593
            FPS: FP1616(gcp)
            CTE: CT0064(gcp)
            CCH: Cag_0109
            CPH: Cpha266_2457
            PVI: Cvib_0224
            PLT: Plut_0158
            DET: DET1426(gcp)
            DEH: cbdb_A1390(gcp)
            DEB: DehaBAV1_1234
            RRS: RoseRS_3985
            RCA: Rcas_3323
            DRA: DR_0382(gcp)
            DGE: Dgeo_1057
            TTH: TTC0008 TTC0888
            TTJ: TTHA1252
            AAE: aq_801(gcp)
            TMA: TM0145
            TPT: Tpet_0780
            TME: Tmel_0627
            FNO: Fnod_0840
            MJA: MJ1130
            MMP: MMP0415
            MMQ: MmarC5_1222
            MMZ: MmarC7_1414
            MAE: Maeo_1198
            MVN: Mevan_1404
            MAC: MA3705(gcp)
            MBA: Mbar_A0279
            MMA: MM_0602
            MBU: Mbur_1196
            MTP: Mthe_0247
            MHU: Mhun_2868
            MLA: Mlab_1694
            MEM: Memar_2247
            MBN: Mboo_0240
            MTH: MTH1425
            MST: Msp_0013
            MSI: Msm_1198
            MKA: MK1458(QRI7)
            HAL: VNG2045G(gcp)
            HMA: rrnAC2490(gcp)
            HWA: HQ1341A(gcp)
            NPH: NP5070A
            TAC: Ta0324
            TVO: TVN1276
            PTO: PTO0374
            PAB: PAB1159(gcp)
            PFU: PF0172
            TKO: TK2126
            RCI: RCIX2232(gcp-a) RCIX2234(gcp-b)
            APE: APE_1135
            SMR: Smar_0838
            IHO: Igni_0266
            SSO: SSO0434
            STO: ST0363
            SAI: Saci_0851
            MSE: Msed_2224
            PAI: PAE2430
            PIS: Pisl_1893
            PCL: Pcal_0308
            PAS: Pars_1440
            TPE: Tpen_0452
            NEQ: NEQ493
STRUCTURES  PDB: 2IVN  2IVP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.57
            ExPASy - ENZYME nomenclature database: 3.4.24.57
            ExplorEnz - The Enzyme Database: 3.4.24.57
            ERGO genome analysis and discovery system: 3.4.24.57
            BRENDA, the Enzyme Database: 3.4.24.57
            CAS: 129430-53-1
///
ENTRY       EC 3.4.24.58                Enzyme
NAME        russellysin;
            Russell's viper venom factor X activator, RVV-X;
            blood-coagulation factor X activating enzyme;
            metalloproteinase RVV-x;
            Vipera russelli proteinase;
            Russell's viper blood coagulation factor X activator;
            RVV-V
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Specifically activates several components of the blood clotting
            system, including coagulation factor X, coagulation factor IX and
            protein C by cleavage of -Arg! bonds. Has no action on insulin B
            chain
COMMENT     This enzyme from the venom of Russell's viper (Vipera russelli) of
            79 kDa comprises a heavy (59 kDa) and a heterogeneous light (18-21
            kDa) chain. Contains Ca2+ and Zn2+. The heavy chain contains the
            zinc-binding endopeptidase domain and a disintegrin. In peptidase
            family M12 (astacin family)
REFERENCE   1  [PMID:1011991]
  AUTHORS   Furie BC, Furie B.
  TITLE     Coagulant protein of Russell's viper venom.
  JOURNAL   Methods. Enzymol. 45 (1976) 191-205.
  ORGANISM  Vipera russelli
REFERENCE   2  [PMID:632245]
  AUTHORS   Lindquist PA, Fujikawa K, Davie EW.
  TITLE     Activation of bovine factor IX (Christmas factor) by factor XIa
            (activated plasma thromboplastin antecedent) and a protease from
            Russell's viper venom.
  JOURNAL   J. Biol. Chem. 253 (1978) 1902-9.
  ORGANISM  Vipera russelli
REFERENCE   3  [PMID:1629211]
  AUTHORS   Takeya H, Nishida S, Miyata T, Kawada S, Saisaka Y, Morita T,
            Iwanaga S.
  TITLE     Coagulation factor X activating enzyme from Russell's viper venom
            (RVV-X). A novel metalloproteinase with disintegrin (platelet
            aggregation inhibitor)-like and C-type lectin-like domains.
  JOURNAL   J. Biol. Chem. 267 (1992) 14109-17.
  ORGANISM  Vipera russelli
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.58
            ExPASy - ENZYME nomenclature database: 3.4.24.58
            ExplorEnz - The Enzyme Database: 3.4.24.58
            ERGO genome analysis and discovery system: 3.4.24.58
            BRENDA, the Enzyme Database: 3.4.24.58
            CAS: 79393-92-3
///
ENTRY       EC 3.4.24.59                Enzyme
NAME        mitochondrial intermediate peptidase;
            mitochondrial intermediate precursor-processing proteinase;
            MIP
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Release of an N-terminal octapeptide as second stage of processing
            of some proteins imported into the mitochondrion
COMMENT     A homologue of thimet oligopeptidase. Natural substrates are
            precursor proteins that have already been processed by mitochondrial
            processing peptidase. In peptidase family M3 (thimet oligopeptidase
            family)
REFERENCE   1  [PMID:1560019]
  AUTHORS   Isaya G, Kalousek F, Rosenberg LE.
  TITLE     Amino-terminal octapeptides function as recognition signals for the
            mitochondrial intermediate peptidase.
  JOURNAL   J. Biol. Chem. 267 (1992) 7904-10.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:1518864]
  AUTHORS   Isaya G, Kalousek F, Rosenberg LE.
  TITLE     Sequence analysis of rat mitochondrial intermediate peptidase:
            similarity to zinc metallopeptidases and to a putative yeast
            homologue.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 8317-21.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K01410  mitochondrial intermediate peptidase
GENES       HSA: 4285(MIPEP)
            MMU: 70478(Mipep)
            RNO: 81684(Mipep)
            CFA: 477338(MIPEP)
            BTA: 517531(LOC517531)
            GGA: 418942(MIPEP)
            DRE: 557349(LOC557349)
            SPU: 585883(LOC585883)
            DME: Dmel_CG7791
            CEL: Y67H2A.7
            SCE: YKL134C(OCT1)
            AGO: AGOS_AFR198W
            CGR: CAGL0D02112g
            SPO: SPAC1F3.10c
            AFM: AFUA_6G08640
            AOR: AO090001000525
            CNE: CNB02140 CNC03660
            UMA: UM02435.1
            TPV: TP01_0515
            TBR: Tb10.6k15.0490
            TCR: 504147.80
            LMA: LmjF36.4450
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.59
            ExPASy - ENZYME nomenclature database: 3.4.24.59
            ExplorEnz - The Enzyme Database: 3.4.24.59
            ERGO genome analysis and discovery system: 3.4.24.59
            BRENDA, the Enzyme Database: 3.4.24.59
            CAS: 136447-30-8
///
ENTRY       EC 3.4.24.60                Enzyme
NAME        dactylysin;
            peptide hormone inactivating endopeptidase;
            PHIE
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of peptides of at least six residues, with bulky
            hydrophobic residues in the P1' position. Shows a preference for
            hydrophobic doublets such as -Phe!Phe- and -Phe!Leu- in
            somatostatin-(1-14)-peptide and dynorphin A-(1-6)-peptide,
            respectively
COMMENT     An endopeptidase of 100 kDa secreted from the skin of the amphibian,
            Xenopus laevis (Dactyl^{e}tre du Cap). Resembles neprilysin in
            insensitivity to 1 muM captopril, but differs from it in being
            insensitive to thiorphan (1 muM) and unable to digest
            [Met5]enkephalin, [Leu5]enkephalin, oxytocin, and substance
            P-(7-11)-peptide. A similar endopeptidase is found in human
            neuroblastoma cells [2]
REFERENCE   1  [PMID:1729723]
  AUTHORS   Carvalho KM, Joudiou C, Boussetta H, Leseney AM, Cohen P.
  TITLE     A peptide-hormone-inactivating endopeptidase in Xenopus laevis skin
            secretion.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 84-8.
  ORGANISM  Xenopus laevis
REFERENCE   2  [PMID:1531011]
  AUTHORS   Delporte C, Carvalho KM, Leseney AM, Winand J, Christophe J, Cohen
            P.
  TITLE     A new metallo- endopeptidase from human neuroblastoma NB-OK-1 cells
            which inactivates atrial natriuretic peptide by selective cleavage
            at the Ser123-Phe124 bond.
  JOURNAL   Biochem. Biophys. Res. Commun. 182 (1992) 158-64.
  ORGANISM  Xenopus laevis
REFERENCE   3  [PMID:8507636]
  AUTHORS   Joudiou C, Carvalho KM, Camarao G, Boussetta H, Cohen P.
  TITLE     Characterization of the thermolysin-like cleavage of biologically
            active peptides by Xenopus laevis peptide hormone inactivating
            enzyme.
  JOURNAL   Biochemistry. 32 (1993) 5959-66.
  ORGANISM  Xenopus laevis
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.60
            ExPASy - ENZYME nomenclature database: 3.4.24.60
            ExplorEnz - The Enzyme Database: 3.4.24.60
            ERGO genome analysis and discovery system: 3.4.24.60
            BRENDA, the Enzyme Database: 3.4.24.60
            CAS: 139466-40-3
///
ENTRY       EC 3.4.24.61                Enzyme
NAME        nardilysin;
            N-arginine dibasic convertase;
            NRD-convertase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of polypeptides, preferably at -Xaa!Arg-Lys-, and less
            commonly at -Arg!Arg-Xaa-, in which Xaa is not Arg or Lys
COMMENT     Enzyme of 133 kDa from rat brain and testis. A homologue of
            pitrilysin containing the His-Phe-Leu-Glu-His zinc-binding sequence,
            and a highly acidic stretch of 71 residues. Unusually for a
            metalloendopeptidase, inhibited by bestatin, amastatin and
            N-ethylmaleimide. In peptidase family M16 (pitrilysin family)
REFERENCE   1  [PMID:3897221]
  AUTHORS   Gomez S, Gluschankof P, Morel A, Cohen P.
  TITLE     The somatostatin-28 convertase of rat brain cortex is associated
            with secretory granule membranes.
  JOURNAL   J. Biol. Chem. 260 (1985) 10541-5.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:2885328]
  AUTHORS   Gluschankof P, Gomez S, Morel A, Cohen P.
  TITLE     Enzymes that process somatostatin precursors. A novel endoprotease
            that cleaves before the arginine-lysine doublet is involved in
            somatostatin-28 convertase activity of rat brain cortex.
  JOURNAL   J. Biol. Chem. 262 (1987) 9615-20.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:8294457]
  AUTHORS   Chesneau V, Pierotti AR, Barre N, Creminon C, Tougard C, Cohen P.
  TITLE     Isolation and characterization of a dibasic selective
            metalloendopeptidase from rat testes that cleaves at the amino
            terminus of arginine residues.
  JOURNAL   J. Biol. Chem. 269 (1994) 2056-61.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:8016118]
  AUTHORS   Pierotti AR, Prat A, Chesneau V, Gaudoux F, Leseney AM, Foulon T,
            Cohen P.
  TITLE     N-arginine dibasic convertase, a metalloendopeptidase as a prototype
            of a class of processing enzymes.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 6078-82.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K01411  nardilysin
GENES       HSA: 4898(NRD1)
            PTR: 456852(NRD1)
            MMU: 230598(Nrd1)
            RNO: 25499(Nrd1)
            CFA: 475354(NRD1)
            BTA: 511254(LOC511254)
            GGA: 424635(RCJMB04_1o14)
            DRE: 565850(LOC565850)
            DME: Dmel_CG2025
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.61
            ExPASy - ENZYME nomenclature database: 3.4.24.61
            ExplorEnz - The Enzyme Database: 3.4.24.61
            ERGO genome analysis and discovery system: 3.4.24.61
            BRENDA, the Enzyme Database: 3.4.24.61
            CAS: 157906-54-2
///
ENTRY       EC 3.4.24.62                Enzyme
NAME        magnolysin;
            bovine neurosecretory granule protease cleaving
            pro-oxytocin/neurophysin;
            pro-oxytocin/neurophysin convertase;
            prooxyphysin proteinase;
            pro-oxytocin convertase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of polypeptides with Arg or Lys in P1 and P2, e.g. to
            hydrolyse pro-oxytocin at -Lys-Arg!Ala-Val-. The specificity further
            depends on the organization of a beta-turn-alpha-helix of nine or
            more residues containing the paired basic amino acids near the
            centre [3]
COMMENT     An endopeptidase of 58 kDa known from bovine pituitary
            neurosecretory granules and bovine and human corpus luteum [4,5].
            Inhibited by EDTA [1]
REFERENCE   1  [PMID:2825769]
  AUTHORS   Clamagirand C, Creminon C, Fahy C, Boussetta H, Cohen P.
  TITLE     Partial purification and functional properties of an endoprotease
            from bovine neurosecretory granules cleaving proocytocin/neurophysin
            peptides at the basic amino acid doublet.
  JOURNAL   Biochemistry. 26 (1987) 6018-23.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:3042797]
  AUTHORS   Creminon C, Rholam M, Boussetta H, Marrakchi N, Cohen P.
  TITLE     Synthetic peptide substrates as models to study a
            pro-ocytocin/neurophysin converting enzyme.
  JOURNAL   J. Chromatogr. 440 (1988) 439-48.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:2674120]
  AUTHORS   Brakch N, Boussetta H, Rholam M, Cohen P.
  TITLE     Processing endoprotease recognizes a structural feature at the
            cleavage site of peptide prohormones. The pro-ocytocin/neurophysin
            model.
  JOURNAL   J. Biol. Chem. 264 (1989) 15912-6.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:2659078]
  AUTHORS   Plevrakis I, Clamagirand C, Creminon C, Brakch N, Rholam M, Cohen P.
  TITLE     Proocytocin/neurophysin convertase from bovine neurohypophysis and
            corpus luteum secretory granules: complete purification,
            structure-function relationships, and competitive inhibitor.
  JOURNAL   Biochemistry. 28 (1989) 2705-10.
  ORGANISM  cow [GN:bta]
REFERENCE   5  [PMID:7931007]
  AUTHORS   Guillou MD, Camier M, Clamagirand C.
  TITLE     Evidence for the presence of pro-oxytocin/neurophysin-converting
            enzyme in the human ovary.
  JOURNAL   J. Endocrinol. 142 (1994) 345-52.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.62
            ExPASy - ENZYME nomenclature database: 3.4.24.62
            ExplorEnz - The Enzyme Database: 3.4.24.62
            ERGO genome analysis and discovery system: 3.4.24.62
            BRENDA, the Enzyme Database: 3.4.24.62
            CAS: 110353-43-0
///
ENTRY       EC 3.4.24.63                Enzyme
NAME        meprin B;
            meprin-b
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of proteins, including azocasein, and peptides.
            Hydrolysis of -His5!Leu-, -Leu6!Cys-, -Ala14!Leu- and -Cys19!Gly-
            bonds in insulin B chain
COMMENT     A brush border membrane-bound metalloendopeptidase known from the
            intestine of all mouse strains that have been tested, and the kidney
            of certain inbred strains. A tetramer of meprin beta subunits (in
            contrast to meprin A, which contains both alpha and beta subunits).
            Occurs in the kidney as a proenzyme that can be activated by
            trypsin. Meprin B is inhibited by both EDTA and 1,10-phenanthroline,
            but not by phosphoramidon, captopril or thiorphan. In peptidase
            family M12 (astacin family)
REFERENCE   1  [PMID:1894622]
  AUTHORS   Kounnas MZ, Wolz RL, Gorbea CM, Bond JS.
  TITLE     Meprin-A and -B. Cell surface endopeptidases of the mouse kidney.
  JOURNAL   J. Biol. Chem. 266 (1991) 17350-7.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:8407940]
  AUTHORS   Gorbea CM, Marchand P, Jiang W, Copeland NG, Gilbert DJ, Jenkins NA,
            Bond JS.
  TITLE     Cloning, expression, and chromosomal localization of the mouse
            meprin beta subunit.
  JOURNAL   J. Biol. Chem. 268 (1993) 21035-43.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:7510289]
  AUTHORS   Johnson GD, Hersh LB.
  TITLE     Expression of meprin subunit precursors. Membrane anchoring through
            the beta subunit and mechanism of zymogen activation.
  JOURNAL   J. Biol. Chem. 269 (1994) 7682-8.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:7674930]
  AUTHORS   Wolz RL, Bond JS.
  TITLE     Meprins A and B.
  JOURNAL   Methods. Enzymol. 248 (1995) 325-45.
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.63
            ExPASy - ENZYME nomenclature database: 3.4.24.63
            ExplorEnz - The Enzyme Database: 3.4.24.63
            ERGO genome analysis and discovery system: 3.4.24.63
            BRENDA, the Enzyme Database: 3.4.24.63
            CAS: 150679-52-0
///
ENTRY       EC 3.4.24.64                Enzyme
NAME        mitochondrial processing peptidase;
            processing enhancing peptidase (for one of two subunits);
            mitochondrial protein precursor-processing proteinase;
            matrix peptidase;
            matrix processing peptidase;
            matrix processing proteinase;
            mitochondrial protein precursor-processing proteinase;
            MPP
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Release of N-terminal targetting peptides from precursor proteins
            imported into the mitochondrion, typically with Arg in position P2
COFACTOR    Zinc [CPD:C00038]
COMMENT     Known from the mitochondrial matrix of fungi and mammals. Formed
            from two subunits, both homologous with pitrilysin [3], and the
            products of the MAS1 and MAS2 genes in yeast. In peptidase family
            M16 (pitrilysin family).
REFERENCE   1  [PMID:3061808]
  AUTHORS   Jensen RE, Yaffe MP.
  TITLE     Import of proteins into yeast mitochondria: the nuclear MAS2 gene
            encodes a component of the processing protease that is homologous to
            the MAS1-encoded subunit.
  JOURNAL   EMBO. J. 7 (1988) 3863-71.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:3044780]
  AUTHORS   Witte C, Jensen RE, Yaffe MP, Schatz G.
  TITLE     MAS1, a gene essential for yeast mitochondrial assembly, encodes a
            subunit of the mitochondrial processing protease.
  JOURNAL   EMBO. J. 7 (1988) 1439-47.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   3  [PMID:2025223]
  AUTHORS   Rawlings ND, Barrett AJ.
  TITLE     Homologues of insulinase, a new superfamily of
            metalloendopeptidases.
  JOURNAL   Biochem. J. 275 ( Pt 2) (1991) 389-91.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], Neurospora crassa [GN:dncr]
REFERENCE   4  [PMID:8212133]
  AUTHORS   Kalousek F, Neupert W, Omura T, Schatz G, Schmitz UK.
  TITLE     Uniform nomenclature for the mitochondrial peptidases cleaving
            precursors of mitochondrial proteins.
  JOURNAL   Trends. Biochem. Sci. 18 (1993) 249.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], Neurospora crassa [GN:dncr]
REFERENCE   5
  AUTHORS   Brunner, M. and Neupert, W.
  TITLE     Purification and characterization of the mitochondrial processing
            peptidase of Neurospora crassa.
  JOURNAL   Methods Enzymol. 248 (1994) 717-728.
  ORGANISM  Neurospora crassa [GN:dncr]
ORTHOLOGY   KO: K01412  mitochondrial processing peptidase
GENES       HSA: 23203(PMPCA) 9512(PMPCB)
            PTR: 463631(PMPCB)
            MMU: 66865(Pmpca) 73078(Pmpcb)
            RNO: 296588(Pmpca) 64198(Pmpcb)
            CFA: 475897(PMPCB) 480677(PMPCA)
            BTA: 534546(PMPCB)
            GGA: 417134(PMPCA) 417718(PMPCB)
            XLA: 432215(MGC78954) 496289(LOC496289)
            DRE: 492801(zgc:101647) 503532(zgc:110738)
            SPU: 580365(LOC580365)
            DME: Dmel_CG8728
            CEL: Y71G12B.24(mppa-1) ZC410.2(mppb-1)
            OSA: 4324473 4332040 4339368
            CME: CMK260C CMM104C
            SCE: YHR024C(MAS2) YLR163C(MAS1)
            AGO: AGOS_ACR069C AGOS_AGL138C
            PIC: PICST_36688(MAS1) PICST_49260(MAS2)
            CGR: CAGL0H02739g CAGL0J00671g
            SPO: SPBC18E5.12c SPBP23A10.15c
            ANI: AN0747.2 AN1104.2
            AFM: AFUA_1G11870 AFUA_1G14200
            AOR: AO090001000377 AO090012000436
            CNE: CNE04620 CNG00860
            UMA: UM02600.1 UM05993.1
            DDI: DDBDRAFT_0189202
            PFA: PFE1155c PFI1625c
            CPV: cgd7_2080
            CHO: Chro.50031 Chro.70239
            TAN: TA11975 TA19130
            TPV: TP02_0218
            TET: TTHERM_00463150 TTHERM_00670480
            TBR: Tb09.160.3110 Tb927.2.4110
            TCR: 506735.10 507547.30 508441.80 510155.80 511585.80
            LMA: LmjF01.0650 LmjF33.2610
            ECI: UTI89_C4059(yhjJ)
            NOC: Noc_1932 Noc_1933
            HAR: HEAR2902 HEAR2903
            PPD: Ppro_0037 Ppro_2117
            DDE: Dde_1699
            SFU: Sfum_1235
            AMA: AM117(mpp)
            APH: APH_0101
            SMD: Smed_0535
            BME: BMEI1451
            BMF: BAB1_0509
            OAN: Oant_0598
            BBT: BBta_7811
            RPE: RPE_1417 RPE_1418
            NWI: Nwi_0230 Nwi_2545 Nwi_2546
            XAU: Xaut_3525
            SIT: TM1040_2329
            RSH: Rsph17029_0481
            RSQ: Rsph17025_0621
            JAN: Jann_3148
            RDE: RD1_2142(mpp)
            SWI: Swit_1414
            ACR: Acry_1786
            RRU: Rru_A2972 Rru_A2973 Rru_A3234
            SWO: Swol_0910
            CSC: Csac_1965
            TFU: Tfu_0785
            FRA: Francci3_3554
            SYN: sll0055
            ANA: alr5125
            AVA: Ava_2341 Ava_3678 Ava_4309 Ava_4310 Ava_4370 Ava_4371
            CCH: Cag_0239
            PVI: Cvib_0338
            AAE: aq_1271(mpp)
STRUCTURES  PDB: 1HR6  1HR7  1HR8  1HR9  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.64
            ExPASy - ENZYME nomenclature database: 3.4.24.64
            ExplorEnz - The Enzyme Database: 3.4.24.64
            ERGO genome analysis and discovery system: 3.4.24.64
            BRENDA, the Enzyme Database: 3.4.24.64
            CAS: 86280-61-7
///
ENTRY       EC 3.4.24.65                Enzyme
NAME        macrophage elastase;
            metalloelastase;
            human macrophage metalloelastase (HME)
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of soluble and insoluble elastin [1]. Specific cleavages
            are also produced at -Ala14!Leu- and -Tyr16!Leu- in the B chain of
            insulin [2]
COMMENT     This enzyme is synthesized as a proenzyme of 53 kDa that is
            converted to an active form of 22 kDa. cDNA sequences have been
            obtained for the mouse [3] and human [4] enzymes. In peptidase
            family M10 (interstitial collagenase family)
REFERENCE   1  [PMID:7030312]
  AUTHORS   Banda MJ, Werb Z.
  TITLE     Mouse macrophage elastase. Purification and characterization as a
            metalloproteinase.
  JOURNAL   Biochem. J. 193 (1981) 589-605.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:7032505]
  AUTHORS   Kettner C, Shaw E, White R, Janoff A.
  TITLE     The specificity of macrophage elastase on the insulin B-chain.
  JOURNAL   Biochem. J. 195 (1981) 369-72.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:1537850]
  AUTHORS   Shapiro SD, Griffin GL, Gilbert DJ, Jenkins NA, Copeland NG, Welgus
            HG, Senior RM, Ley TJ.
  TITLE     Molecular cloning, chromosomal localization, and bacterial
            expression of a murine macrophage metalloelastase.
  JOURNAL   J. Biol. Chem. 267 (1992) 4664-71.
  ORGANISM  mouse [GN:mmu]
REFERENCE   4  [PMID:8226919]
  AUTHORS   Shapiro SD, Kobayashi DK, Ley TJ.
  TITLE     Cloning and characterization of a unique elastolytic
            metalloproteinase produced by human alveolar macrophages.
  JOURNAL   J. Biol. Chem. 268 (1993) 23824-9.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01413  matrix metalloproteinase-12 (macrophage elastase)
GENES       HSA: 4321(MMP12)
            PTR: 451512(MMP12)
            MMU: 17381(Mmp12)
            RNO: 117033(Mmp12)
            CFA: 611789(MMP12)
            BTA: 526981(LOC526981)
STRUCTURES  PDB: 1JIZ  1JK3  1OS2  1OS9  1RMZ  1ROS  1UTT  1UTZ  1Y93  1YCM  
                 1Z3J  2HU6  2OXU  2OXW  2OXZ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.65
            ExPASy - ENZYME nomenclature database: 3.4.24.65
            ExplorEnz - The Enzyme Database: 3.4.24.65
            ERGO genome analysis and discovery system: 3.4.24.65
            BRENDA, the Enzyme Database: 3.4.24.65
            CAS: 9004-06-2
///
ENTRY       EC 3.4.24.66                Enzyme
NAME        choriolysin L;
            teleost hatching enzyme (component);
            low choriolytic enzyme (LCE)
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of the inner layer of fish egg envelope. Also hydrolysis
            of casein and small molecule substrates such as
            succinyl-Leu-Leu-Val-Tyr!7-(4-methyl)coumarylamide
COMMENT     Known from the teleost fish Oryzias latipes (medaka). Efficient
            dissolution of the egg membrane requires concerted action with
            choriolysin H. A 24 kDa peptidase family M12 (astacin family)
REFERENCE   1
  AUTHORS   Yasumasu, S., Iuchi, I. and Yamagami, K.
  TITLE     Medaka hatching enzyme consists of two kinds of proteases which act
            cooperatively.
  JOURNAL   Zool. Sci. 5 (1988) 191-195.
REFERENCE   2  [PMID:2656665]
  AUTHORS   Yasumasu S, Iuchi I, Yamagami K.
  TITLE     Isolation and some properties of low choriolytic enzyme (LCE), a
            component of the hatching enzyme of the teleost, Oryzias latipes.
  JOURNAL   J. Biochem. (Tokyo). 105 (1989) 212-8.
  ORGANISM  Oryzias latipes
REFERENCE   3  [PMID:1730389]
  AUTHORS   Yasumasu S, Katow S, Hamazaki TS, Iuchi I, Yamagami K.
  TITLE     Two constituent proteases of a teleostean hatching enzyme:
            concurrent syntheses and packaging in the same secretory granules in
            discrete arrangement.
  JOURNAL   Dev. Biol. 149 (1992) 349-56.
  ORGANISM  Oryzias latipes
REFERENCE   4  [PMID:1397682]
  AUTHORS   Yasumasu S, Yamada K, Akasaka K, Mitsunaga K, Iuchi I, Shimada H,
            Yamagami K.
  TITLE     Isolation of cDNAs for LCE and HCE, two constituent proteases of the
            hatching enzyme of Oryzias latipes, and concurrent expression of
            their mRNAs during development.
  JOURNAL   Dev. Biol. 153 (1992) 250-8.
  ORGANISM  Oryzias latipes
STRUCTURES  PDB: 1WGZ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.66
            ExPASy - ENZYME nomenclature database: 3.4.24.66
            ExplorEnz - The Enzyme Database: 3.4.24.66
            ERGO genome analysis and discovery system: 3.4.24.66
            BRENDA, the Enzyme Database: 3.4.24.66
            CAS: 177529-15-6
///
ENTRY       EC 3.4.24.67                Enzyme
NAME        choriolysin H;
            teleost hatching enzyme (component);
            high choriolytic enzyme (HCE)
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of the inner layer of fish egg envelope. Also hydrolysis
            of casein and small molecule substrates such as
            succinyl-Leu-Leu-Val-Tyr!7-(4-methyl)coumarylamide
COMMENT     Known from the teleost fish Oryzias latipes (medaka). Efficient
            dissolution of the egg membrane requires concerted action with
            choriolysin L. A 25.5 kDa peptidase in family M12 (astacin family)
REFERENCE   1  [PMID:4652273]
  AUTHORS   Yamagami K.
  TITLE     Isolation of a choriolytic enzyme (hatching enzyme) of the teleost,
            Oryzias latipes.
  JOURNAL   Dev. Biol. 29 (1972) 343-8.
  ORGANISM  Oryzias latipes
REFERENCE   2  [PMID:2656664]
  AUTHORS   Yasumasu S, Iuchi I, Yamagami K.
  TITLE     Purification and partial characterization of high choriolytic enzyme
            (HCE), a component of the hatching enzyme of the teleost, Oryzias
            latipes.
  JOURNAL   J. Biochem. (Tokyo). 105 (1989) 204-11.
  ORGANISM  Oryzias latipes
REFERENCE   3  [PMID:2751672]
  AUTHORS   Yasumasu S, Katow S, Umino Y, Iuchi I, Yamagami K.
  TITLE     A unique proteolytic action of HCE, a constituent protease of a fish
            hatching enzyme: tight binding to its natural substrate, egg
            envelope.
  JOURNAL   Biochem. Biophys. Res. Commun. 162 (1989) 58-63.
  ORGANISM  Oryzias latipes
REFERENCE   4  [PMID:1397682]
  AUTHORS   Yasumasu S, Yamada K, Akasaka K, Mitsunaga K, Iuchi I, Shimada H,
            Yamagami K.
  TITLE     Isolation of cDNAs for LCE and HCE, two constituent proteases of the
            hatching enzyme of Oryzias latipes, and concurrent expression of
            their mRNAs during development.
  JOURNAL   Dev. Biol. 153 (1992) 250-8.
  ORGANISM  Oryzias latipes
REFERENCE   5  [PMID:8112467]
  AUTHORS   Lee KS, Yasumasu S, Nomura K, Iuchi I.
  TITLE     HCE, a constituent of the hatching enzymes of Oryzias latipes
            embryos, releases unique proline-rich polypeptides from its natural
            substrate, the hardened chorion.
  JOURNAL   FEBS. Lett. 339 (1994) 281-4.
  ORGANISM  Oryzias latipes
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.67
            ExPASy - ENZYME nomenclature database: 3.4.24.67
            ExplorEnz - The Enzyme Database: 3.4.24.67
            ERGO genome analysis and discovery system: 3.4.24.67
            BRENDA, the Enzyme Database: 3.4.24.67
            CAS: 177529-16-7
///
ENTRY       EC 3.4.24.68                Enzyme
NAME        tentoxilysin;
            tetanus neurotoxin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of -Gln76!Phe- bond in synaptobrevin (also known as
            neuronal vesicle-associated membrane protein, VAMP)
COMMENT     Zinc enzyme produced by Clostridium tetani. Proenzyme of 150 kDa is
            processed to disulfide-linked subunits of 100 and 50 kDa, the latter
            being responsible for the endopeptidase activity. Weakly inhibited
            by captopril, and phosphoramidon. The clostridial neurotoxins
            disable the neuroexocytosis apparatus, and have been described as
            the most toxic substances known. Tentoxilysin acts at the spinal
            inhibitory interneurons, blocking the release of various
            neurotransmitters to produce spastic paralysis. Type example of
            peptidase family M27 (tentoxilysin family)
REFERENCE   1
  AUTHORS   Fujii, N., Kimura, K., Yashiki, T., Tsuzuki, K., Moriishi, K.,
            Yokosawa, N., Syuto, B. and Oguma, K.
  TITLE     A zinc-protease specific domain in botulinum and tetanus
            neurotoxins.
  JOURNAL   Microbiol. Intern. 36 (1992) 213-220.
REFERENCE   2  [PMID:1331807]
  AUTHORS   Schiavo G, Benfenati F, Poulain B, Rossetto O, Polverino de Laureto
            P, DasGupta BR, Montecucco C.
  TITLE     Tetanus and botulinum-B neurotoxins block neurotransmitter release
            by proteolytic cleavage of synaptobrevin.
  JOURNAL   Nature. 359 (1992) 832-5.
REFERENCE   3  [PMID:1429690]
  AUTHORS   Schiavo G, Rossetto O, Santucci A, DasGupta BR, Montecucco C.
  TITLE     Botulinum neurotoxins are zinc proteins.
  JOURNAL   J. Biol. Chem. 267 (1992) 23479-83.
  ORGANISM  Clostridium botulinum
REFERENCE   4  [PMID:7527117]
  AUTHORS   Montecucco C, Schiavo G.
  TITLE     Mechanism of action of tetanus and botulinum neurotoxins.
  JOURNAL   Mol. Microbiol. 13 (1994) 1-8.
REFERENCE   5  [PMID:7674951]
  AUTHORS   Schiavo G, Montecucco C.
  TITLE     Tetanus and botulism neurotoxins: isolation and assay.
  JOURNAL   Methods. Enzymol. 248 (1995) 643-52.
ORTHOLOGY   KO: K08644  tentoxilysin
GENES       CTC: pE88_60(tetX)
STRUCTURES  PDB: 1A8D  1AF9  1DFQ  1DIW  1DLL  1FV2  1YVG  1YXW  1YYN  1Z7H  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.68
            ExPASy - ENZYME nomenclature database: 3.4.24.68
            ExplorEnz - The Enzyme Database: 3.4.24.68
            ERGO genome analysis and discovery system: 3.4.24.68
            BRENDA, the Enzyme Database: 3.4.24.68
///
ENTRY       EC 3.4.24.69                Enzyme
NAME        bontoxilysin;
            botulinum neurotoxin;
            BoNT
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Limited hydrolysis of proteins of the neuroexocytosis apparatus,
            synaptobrevin (also known as neuronal vesicle-associated membrane
            protein, VAMP), synaptosome-associated protein of 25 kDa (SNAP25) or
            syntaxin. No detected action on small molecule substrates
COMMENT     This zinc enzyme, produced by Clostridium botulinum, occurs as forms
            A-G that differ in specificity of action on the proteins of the
            neuroexocytosis apparatus [1-5]. The 150-kDa proenzymes of
            bontoxilysin are processed to disulfide-linked subunits of 100 and
            50 kDa, the latter being responsible for the endopeptidase
            activities. Weakly inhibited by captopril, and phosphoramidon.
            Toxicity is due to action at the neuromuscular junctions that blocks
            release of acetylcholine, causing flaccid paralysis, in contrast to
            the spastic paralysis caused by tentoxilysin. In peptidase family
            M27 (tentoxilysin family)
REFERENCE   1  [PMID:8226912]
  AUTHORS   Schiavo G, Rossetto O, Catsicas S, Polverino de Laureto P, DasGupta
            BR, Benfenati F, Montecucco C.
  TITLE     Identification of the nerve terminal targets of botulinum neurotoxin
            serotypes A, D, and E.
  JOURNAL   J. Biol. Chem. 268 (1993) 23784-7.
REFERENCE   2  [PMID:8243676]
  AUTHORS   Schiavo G, Santucci A, Dasgupta BR, Mehta PP, Jontes J, Benfenati F,
            Wilson MC, Montecucco C.
  TITLE     Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct
            COOH-terminal peptide bonds.
  JOURNAL   FEBS. Lett. 335 (1993) 99-103.
REFERENCE   3  [PMID:8505288]
  AUTHORS   Schiavo G, Shone CC, Rossetto O, Alexander FC, Montecucco C.
  TITLE     Botulinum neurotoxin serotype F is a zinc endopeptidase specific for
            VAMP/synaptobrevin.
  JOURNAL   J. Biol. Chem. 268 (1993) 11516-9.
REFERENCE   4  [PMID:8051110]
  AUTHORS   Schiavo G, Malizio C, Trimble WS, Polverino de Laureto P, Milan G,
            Sugiyama H, Johnson EA, Montecucco C.
  TITLE     Botulinum G neurotoxin cleaves VAMP/synaptobrevin at a single
            Ala-Ala peptide bond.
  JOURNAL   J. Biol. Chem. 269 (1994) 20213-6.
  ORGANISM  Clostridium botulinum
REFERENCE   5  [PMID:7527117]
  AUTHORS   Montecucco C, Schiavo G.
  TITLE     Mechanism of action of tetanus and botulinum neurotoxins.
  JOURNAL   Mol. Microbiol. 13 (1994) 1-8.
REFERENCE   6  [PMID:7674951]
  AUTHORS   Schiavo G, Montecucco C.
  TITLE     Tetanus and botulism neurotoxins: isolation and assay.
  JOURNAL   Methods. Enzymol. 248 (1995) 643-52.
ORTHOLOGY   KO: K06011  bontoxilysin
GENES       SAR: SAR1895
            CBO: CBO0806(atx)
            CBA: CLB_0847(ntnH) CLB_0848(boNT)
            CBH: CLC_0861(ntnH) CLC_0862(boNT)
            CBF: CLI_0850(ntnH) CLI_0851(boNT)
STRUCTURES  PDB: 1E1H  1EPW  1F31  1F82  1G9A  1G9B  1G9C  1G9D  1I1E  1S0B  
                 1S0C  1S0D  1S0E  1S0F  1S0G  1T3A  1T3C  1Z0H  1ZKW  1ZKX  
                 1ZL5  1ZL6  1ZN3  2A8A  2A97  2ETF  2FPQ  2G7K  2G7N  2G7P  
                 2G7Q  2ILP  2IMA  2IMB  2IMC  2NM1  2NP0  2NYY  2NZ9  3BTA  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.69
            ExPASy - ENZYME nomenclature database: 3.4.24.69
            ExplorEnz - The Enzyme Database: 3.4.24.69
            ERGO genome analysis and discovery system: 3.4.24.69
            BRENDA, the Enzyme Database: 3.4.24.69
///
ENTRY       EC 3.4.24.70                Enzyme
NAME        oligopeptidase A;
            68000-M signalpeptide hydrolase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of oligopeptides, with broad specificity. Gly or Ala
            commonly occur as P1 or P1' residues, but more distant residues are
            also important, as is shown by the fact that
            Z-Gly-Pro-Gly!Gly-Pro-Ala is cleaved, but not Z-(Gly)5 [4]
COMMENT     Known from Escherichia coli and Salmonella typhimurium. A zinc
            metallopeptidase, in peptidase family M3 (thimet oligopeptidase
            family), but differs from thimet oligopeptidase in lack of
            thiol-activation
REFERENCE   1  [PMID:3053642]
  AUTHORS   Novak P, Dev IK.
  TITLE     Degradation of a signal peptide by protease IV and oligopeptidase A.
  JOURNAL   J. Bacteriol. 170 (1988) 5067-75.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:1522065]
  AUTHORS   Conlin CA, Vimr ER, Miller CG.
  TITLE     Oligopeptidase A is required for normal phage P22 development.
  JOURNAL   J. Bacteriol. 174 (1992) 5869-80.
  ORGANISM  Salmonella typhimurium
REFERENCE   3  [PMID:1325967]
  AUTHORS   Conlin CA, Trun NJ, Silhavy TJ, Miller CG.
  TITLE     Escherichia coli prlC encodes an endopeptidase and is homologous to
            the Salmonella typhimurium opdA gene.
  JOURNAL   J. Bacteriol. 174 (1992) 5881-7.
  ORGANISM  Salmonella typhimurium
REFERENCE   4  [PMID:7674945]
  AUTHORS   Conlin CA, Miller CG.
  TITLE     Dipeptidyl carboxypeptidase and oligopeptidase A from Escherichia
            coli and Salmonella typhimurium.
  JOURNAL   Methods. Enzymol. 248 (1995) 567-79.
  ORGANISM  Escherichia coli [GN:eco], Salmonella typhimurium
ORTHOLOGY   KO: K01414  oligopeptidase A
GENES       SPU: 576308(LOC576308)
            DME: Dmel_CG11771
            ATH: AT5G10540 AT5G65620
            OSA: 4331244
            PIC: PICST_89481(OCT1)
            EHI: 264.t00004 286.t00005
            ECO: b3498(prlC)
            ECJ: JW3465(prlC)
            ECE: Z4898(prlC)
            ECS: ECs4370
            ECC: c4297(prlC)
            ECI: UTI89_C4017(prlC)
            ECP: ECP_3588
            ECV: APECO1_2955(prlC)
            ECW: EcE24377A_3980(prlC)
            ECX: EcHS_A3698
            STY: STY4209(prlC)
            STT: t3922(prlC)
            SPT: SPA3451(prlC)
            SEC: SC3523(opdA)
            STM: STM3594(prlC)
            YPE: YPO3975(opdA)
            YPK: y3855(prlC)
            YPM: YP_3337(opdA)
            YPA: YPA_3802
            YPN: YPN_3623
            YPP: YPDSF_3339
            YPS: YPTB3816(opdA)
            YPI: YpsIP31758_4047(prlC)
            SFL: SF3529(prlC)
            SFX: S4239(prlC)
            SFV: SFV_3510(prlC)
            SSN: SSON_3733(prlC)
            SBO: SBO_3496(prlC)
            SDY: SDY_3564(prlC)
            ECA: ECA0055(prlC)
            PLU: plu0124(opdA)
            WBR: WGLp398(prlC)
            SGL: SG0073
            ENT: Ent638_3911
            SPE: Spro_4701
            BFL: Bfl023(prlC)
            BPN: BPEN_023(prlC)
            HIN: HI0214(prlC)
            HIT: NTHI0312(prlC)
            HDU: HD0988(prlC)
            HSO: HS_0791(prlC)
            PMU: PM0680(prlC)
            MSU: MS1199(dcp)
            APL: APL_1034(prlC)
            ASU: Asuc_1588
            XFA: XF0127
            XFT: PD0097(prlC)
            XCC: XCC0580(prlC)
            XCB: XC_3653
            XCV: XCV3744(opdA)
            XAC: XAC3627(prlC)
            XOO: XOO0759(prlC)
            XOM: XOO_0689(XOO0689)
            VCH: VC0188
            VVU: VV1_1108
            VVY: VV0067
            VPA: VP0070
            VFI: VF2487
            PPR: PBPRA3544(prlC)
            PAE: PA0067(prlC)
            PAU: PA14_00790(prlC)
            PPU: PP_0096(prlC)
            PPF: Pput_0111
            PST: PSPTO_0144(prlC)
            PSB: Psyr_0045
            PSP: PSPPH_0051(prlC)
            PFL: PFL_0050(prlC)
            PFO: Pfl_0088 Pfl_0090
            PEN: PSEEN0050(prlC)
            PMY: Pmen_4461
            PAR: Psyc_0078(prlC)
            PCR: Pcryo_0084
            PRW: PsycPRwf_2240
            ACI: ACIAD3182(prlC)
            SON: SO_4699(prlC)
            SDN: Sden_3595
            SFR: Sfri_3874
            SAZ: Sama_3546
            SBL: Sbal_0124
            SBM: Shew185_4256
            SLO: Shew_3657
            SPC: Sputcn32_0087
            SSE: Ssed_0145
            SPL: Spea_4065
            SHE: Shewmr4_3842
            SHM: Shewmr7_3935
            SHN: Shewana3_4051
            SHW: Sputw3181_3978
            ILO: IL2327(prlC)
            CPS: CPS_4986(prlC)
            PHA: PSHAa0361(prlC)
            PAT: Patl_4207
            SDE: Sde_0031
            PIN: Ping_0212
            MAQ: Maqu_0054
            CBU: CBU_0039(prlC)
            CBD: COXBU7E912_0159(prlC)
            LPN: lpg0141
            LPF: lpl0141(prlC)
            LPP: lpp0156(prlC)
            MCA: MCA1253(prlC)
            FTU: FTT0899c(prlC)
            FTF: FTF0899c(prlC)
            FTL: FTL_0419
            FTH: FTH_0412(prlC)
            FTA: FTA_0442
            FTN: FTN_0425(prlC)
            TCX: Tcr_0067
            NOC: Noc_0208
            AEH: Mlg_2533
            HHA: Hhal_2397
            HCH: HCH_00043(prlC)
            CSA: Csal_0399
            ABO: ABO_0140(prlC)
            MMW: Mmwyl1_0320
            AHA: AHA_0092(prlC)
            BCI: BCI_0054(prlC)
            RMA: Rmag_0568
            VOK: COSY_0523(prlC)
            NME: NMB0214
            NMA: NMA0054(prlC)
            NMC: NMC0206(prlC)
            NGO: NGO1770
            CVI: CV_0876(prlC)
            RSO: RSc1595(prlC)
            REU: Reut_A1298
            REH: H16_A1369(dcp)
            RME: Rmet_1191
            BMA: BMA1726(prlC)
            BMV: BMASAVP1_A2235(prlC)
            BML: BMA10299_A3084(prlC)
            BMN: BMA10247_1507(prlC)
            BXE: Bxe_A1534
            BVI: Bcep1808_2221
            BUR: Bcep18194_A5447
            BCN: Bcen_5936
            BCH: Bcen2424_2141
            BAM: Bamb_2178
            BPS: BPSL2305 BPSS1175
            BPM: BURPS1710b_2750(prlC) BURPS1710b_A0141(prlC)
            BPL: BURPS1106A_2674(prlC) BURPS1106A_A1569(prlC)
            BPD: BURPS668_2618(prlC) BURPS668_A1650(prlC)
            BTE: BTH_I1860 BTH_II1232
            PNU: Pnuc_0730
            BPE: BP0989(prlC)
            BPA: BPP1458(prlC)
            BBR: BB2532(prlC)
            RFR: Rfer_2208
            POL: Bpro_2855
            PNA: Pnap_2614
            AAV: Aave_2458
            AJS: Ajs_2129
            VEI: Veis_1923
            MPT: Mpe_A2132
            HAR: HEAR0744(prlC)
            MMS: mma_0671
            NEU: NE1663(prlC)
            NET: Neut_0453
            NMU: Nmul_A2483
            EBA: ebA1131(prlC)
            AZO: azo2877(prlC)
            DAR: Daro_3646
            TBD: Tbd_2433
            MFA: Mfla_0150
            TDN: Tmden_0712
            ABU: Abu_1195(prlC)
            NIS: NIS_0533
            SUN: SUN_1683
            RET: RHE_CH03916(dcp)
            SUS: Acid_5816
            LIL: LA2625(prlC)
            LIC: LIC11361(prlC)
            LBJ: LBJ_1638
            LBL: LBL_1857
            SYN: slr0659(prlC)
            SYW: SYNW1483(opdA)
            SYC: syc2383_c(prlC)
            SYF: Synpcc7942_1708
            SYD: Syncc9605_1029
            SYE: Syncc9902_0930
            SYG: sync_1871(opdA)
            SYR: SynRCC307_0941(prlC)
            SYX: SynWH7803_0771(prlC)
            TEL: tll1181
            ANA: alr0880
            AVA: Ava_4484
            PMA: Pro1068(dcp)
            PMM: PMM0593
            PMT: PMT0428
            PMN: PMN2A_0029
            PMI: PMT9312_0593
            PMB: A9601_06491(prlC)
            PMC: P9515_06581(prlC)
            PMF: P9303_18561(prlC)
            PMG: P9301_06191(prlC)
            PMH: P9215_06751
            PME: NATL1_06491(prlC)
            TER: Tery_4649
            GFO: GFO_2871(prlC)
            FJO: Fjoh_0429
            DRA: DR_1659
            DGE: Dgeo_0948
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.70
            ExPASy - ENZYME nomenclature database: 3.4.24.70
            ExplorEnz - The Enzyme Database: 3.4.24.70
            ERGO genome analysis and discovery system: 3.4.24.70
            BRENDA, the Enzyme Database: 3.4.24.70
            CAS: 148266-37-9
///
ENTRY       EC 3.4.24.71                Enzyme
NAME        endothelin-converting enzyme 1;
            endothelin-converting enzyme;
            ECE-1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of the -Trp21!Val- bond in big endothelin to form
            endothelin 1
COMMENT     A phosphoramidon-sensitive metalloendopeptidase in peptidase family
            M13 (neprilysin family). An integral membrane protein predominantly
            of endothelial cells, which generates the potent vasoconstrictor
            endothelin 1 from its inactive precursor
REFERENCE   1  [PMID:8407980]
  AUTHORS   Takahashi M, Matsushita Y, Iijima Y, Tanzawa K.
  TITLE     Purification and characterization of endothelin-converting enzyme
            from rat lung.
  JOURNAL   J. Biol. Chem. 268 (1993) 21394-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:8034569]
  AUTHORS   Shimada K, Takahashi M, Tanzawa K.
  TITLE     Cloning and functional expression of endothelin-converting enzyme
            from rat endothelial cells.
  JOURNAL   J. Biol. Chem. 269 (1994) 18275-8.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:8062389]
  AUTHORS   Xu D, Emoto N, Giaid A, Slaughter C, Kaw S, deWit D, Yanagisawa M.
  TITLE     ECE-1: a membrane-bound metalloprotease that catalyzes the
            proteolytic activation of big endothelin-1.
  JOURNAL   Cell. 78 (1994) 473-85.
  ORGANISM  mouse [GN:mmu]
ORTHOLOGY   KO: K01415  endothelin-converting enzyme
GENES       HSA: 1889(ECE1) 9718(ECE2)
            PTR: 456594(ECE1) 471026(ECE2)
            MMU: 107522(Ece2) 230857(Ece1)
            RNO: 408243(Ece2) 94204(Ece1)
            CFA: 478654(PSMD2) 487388(ECE1)
            BTA: 281133(ECE1) 281134(ECE2)
            GGA: 395459(ECE1)
            XLA: 380070(ece1)
            DME: Dmel_CG9565(Nep3)
            CEL: F18A12.8(peptidase)
            CME: CMP249C
            ANI: AN3091.2
            AFM: AFUA_3G12420
            AOR: AO090005000726
            CNE: CNB04230
            SFR: Sfri_0842 Sfri_1958
            SAZ: Sama_0380 Sama_2615
            SBL: Sbal_0450 Sbal_0685 Sbal_3908
            SBM: Shew185_3625 Shew185_3866 Shew185_3928
            SLO: Shew_2973 Shew_3426
            SPC: Sputcn32_0791 Sputcn32_3412
            SSE: Ssed_0436 Ssed_3509 Ssed_3633
            SPL: Spea_3177 Spea_3239
            SHE: Shewmr4_0433 Shewmr4_0499 Shewmr4_3179
            SHM: Shewmr7_0787 Shewmr7_3531 Shewmr7_3594
            SHN: Shewana3_0431 Shewana3_0759
            SHW: Sputw3181_0531 Sputw3181_3384
            PHA: PSHAa1371 PSHAa2745
            PAT: Patl_3353
            ADE: Adeh_1141
            AFW: Anae109_3155
            RPD: RPD_2006
            MMR: Mmar10_0473 Mmar10_0474
            SWI: Swit_0514
            ABA: Acid345_0009 Acid345_1078 Acid345_1491 Acid345_4515
            SUS: Acid_1534 Acid_1818 Acid_2789 Acid_3743 Acid_4723
            LRE: Lreu_1797
            CBE: Cbei_0367 Cbei_4945
            ART: Arth_2227
            NCA: Noca_0131
            KRA: Krad_4429
            FJO: Fjoh_0959
            MEM: Memar_2106
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.71
            ExPASy - ENZYME nomenclature database: 3.4.24.71
            ExplorEnz - The Enzyme Database: 3.4.24.71
            ERGO genome analysis and discovery system: 3.4.24.71
            BRENDA, the Enzyme Database: 3.4.24.71
            CAS: 138238-81-0
///
ENTRY       EC 3.4.24.72                Enzyme
NAME        fibrolase;
            fibrinolytic proteinase;
            Agkistrodon contortrix contortrix metalloproteinase;
            Agkistrodon contortrix contortrix venom metalloproteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of -Ala14!Leu- in insulin B chain and -Lys413!Leu- in
            Aalpha-chain of fibrinogen
COMMENT     A 23-kDa, non-hemorrhagic enzyme from the venom of the southern
            copperhead snake (Agkistrodon contortix contortix). In peptidase
            family M12 (astacin family)
REFERENCE   1  [PMID:3232124]
  AUTHORS   Retzios AD, Markland FS Jr.
  TITLE     A direct-acting fibrinolytic enzyme from the venom of Agkistrodon
            contortrix contortrix: effects on various components of the human
            blood coagulation and fibrinolysis systems.
  JOURNAL   Thromb. Res. 52 (1988) 541-52.
  ORGANISM  Agkistrodon contortrix contortrix
REFERENCE   2  [PMID:1898066]
  AUTHORS   Guan AL, Retzios AD, Henderson GN, Markland FS Jr.
  TITLE     Purification and characterization of a fibrinolytic enzyme from
            venom of the southern copperhead snake (Agkistrodon contortrix
            contortrix).
  JOURNAL   Arch. Biochem. Biophys. 289 (1991) 197-207.
  ORGANISM  Agkistrodon contortrix contortrix
REFERENCE   3  [PMID:1304358]
  AUTHORS   Randolph A, Chamberlain SH, Chu HL, Retzios AD, Markland FS Jr,
            Masiarz FR.
  TITLE     Amino acid sequence of fibrolase, a direct-acting fibrinolytic
            enzyme from Agkistrodon contortrix contortrix venom.
  JOURNAL   Protein. Sci. 1 (1992) 590-600.
  ORGANISM  Agkistrodon contortrix contortrix
REFERENCE   4  [PMID:7719479]
  AUTHORS   Loayza SL, Trikha M, Markland FS, Riquelme P, Kuo J.
  TITLE     Resolution of isoforms of natural and recombinant fibrolase, the
            fibrinolytic enzyme from Agkistrodon contortrix contortrix snake
            venom, and comparison of their EDTA sensitivities.
  JOURNAL   J. Chromatogr. B. Biomed. Appl. 662 (1994) 227-43.
  ORGANISM  Agkistrodon contortrix contortrix
REFERENCE   5  [PMID:8085237]
  AUTHORS   Retzios AD, Markland FS.
  TITLE     Fibrinolytic enzymes from the venoms of Agkistrodon contortrix
            contortrix and Crotalus basiliscus basiliscus: cleavage site
            specificity towards the alpha-chain of fibrin.
  JOURNAL   Thromb. Res. 74 (1994) 355-67.
  ORGANISM  Agkistrodon contortrix contortrix, Crotalus basiliscus basiliscus
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.72
            ExPASy - ENZYME nomenclature database: 3.4.24.72
            ExplorEnz - The Enzyme Database: 3.4.24.72
            ERGO genome analysis and discovery system: 3.4.24.72
            BRENDA, the Enzyme Database: 3.4.24.72
            CAS: 116036-70-5
///
ENTRY       EC 3.4.24.73                Enzyme
NAME        jararhagin;
            HF2-proteinase;
            JF1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of -His10!Leu-, -Ala14!Leu-, -Tyr16!Leu-and -Phe24!Phe-
            bonds in insulin B chain
COMMENT     Hemorrhagic endopeptidase from the venom of the jararaca snake
            (Bothrops jararaca). The 52-kDa enzyme contains a disintegrin domain
            [3]. In peptidase family M12 (astacin family)
REFERENCE   1
  AUTHORS   Mandelbaum, F.R., Reichl, A.P. and Assakura, M.T.
  TITLE     Some physical and biochemical characteristics of HF2, one of the
            hemorrhagic factors in the venom of Bothrops jararaca.
  JOURNAL   In: Ohsaka, A., Hayashi, K. and Sawai, Y. (Eds.), Animal, Plant and
            Microbial Toxins, Plenum Press, New York, 1976, p. 111-121.
REFERENCE   2  [PMID:3810664]
  AUTHORS   Assakura MT, Reichl AP, Mandelbaum FR.
  TITLE     Comparison of immunological, biochemical and biophysical properties
            of three hemorrhagic factors isolated from the venom of Bothrops
            jararaca (jararaca).
  JOURNAL   Toxicon. 24 (1986) 943-6.
  ORGANISM  Bothrops jararaca
REFERENCE   3  [PMID:1385408]
  AUTHORS   Paine MJ, Desmond HP, Theakston RD, Crampton JM.
  TITLE     Purification, cloning, and molecular characterization of a high
            molecular weight hemorrhagic metalloprotease, jararhagin, from
            Bothrops jararaca venom. Insights into the disintegrin gene family.
  JOURNAL   J. Biol. Chem. 267 (1992) 22869-76.
  ORGANISM  Bothrops jararaca
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.73
            ExPASy - ENZYME nomenclature database: 3.4.24.73
            ExplorEnz - The Enzyme Database: 3.4.24.73
            ERGO genome analysis and discovery system: 3.4.24.73
            BRENDA, the Enzyme Database: 3.4.24.73
            CAS: 160477-79-2
///
ENTRY       EC 3.4.24.74                Enzyme
NAME        fragilysin;
            Bacteroides fragilis (entero)toxin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Broad proteolytic specificity, bonds hydrolysed including -Gly!Leu-,
            -Met!Leu-, -Phe!Leu-, -Cys!Leu-, Leu!Gly
COFACTOR    Zinc [CPD:C00038]
COMMENT     Thought to be a cause of diarrhoea in animals and humans. Hydrolyses
            extracellular matrix proteins, and disrupts tight junctions of
            intestinal epithelial cells. Also degrades intracellular,
            cytoskeletal proteins actin, myosin and others. In peptidase family
            M10 (interstitial collagenase family)
REFERENCE   1  [PMID:7806355]
  AUTHORS   Moncrief JS, Obiso R Jr, Barroso LA, Kling JJ, Wright RL, Van
            Tassell RL, Lyerly DM, Wilkins TD.
  TITLE     The enterotoxin of Bacteroides fragilis is a metalloprotease.
  JOURNAL   Infect. Immun. 63 (1995) 175-81.
  ORGANISM  Bacteroides fragilis
REFERENCE   2  [PMID:7558286]
  AUTHORS   Obiso RJ Jr, Lyerly DM, Van Tassell RL, Wilkins TD.
  TITLE     Proteolytic activity of the Bacteroides fragilis enterotoxin causes
            fluid secretion and intestinal damage in vivo.
  JOURNAL   Infect. Immun. 63 (1995) 3820-6.
  ORGANISM  Bacteroides fragilis
REFERENCE   3  [PMID:8557328]
  AUTHORS   Donelli G, Fabbri A, Fiorentini C.
  TITLE     Bacteroides fragilis enterotoxin induces cytoskeletal changes and
            surface blebbing in HT-29 cells.
  JOURNAL   Infect. Immun. 64 (1996) 113-9.
  ORGANISM  Bacteroides fragilis
REFERENCE   4  [PMID:8945541]
  AUTHORS   Koshy SS, Montrose MH, Sears CL.
  TITLE     Human intestinal epithelial cells swell and demonstrate actin
            rearrangement in response to the metalloprotease toxin of
            Bacteroides fragilis.
  JOURNAL   Infect. Immun. 64 (1996) 5022-8.
  ORGANISM  Bacteroides fragilis
REFERENCE   5  [PMID:9011050]
  AUTHORS   Kling JJ, Wright RL, Moncrief JS, Wilkins TD.
  TITLE     Cloning and characterization of the gene for the metalloprotease
            enterotoxin of Bacteroides fragilis.
  JOURNAL   FEMS. Microbiol. Lett. 146 (1997) 279-84.
  ORGANISM  Bacteroides fragilis
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.74
            ExPASy - ENZYME nomenclature database: 3.4.24.74
            ExplorEnz - The Enzyme Database: 3.4.24.74
            ERGO genome analysis and discovery system: 3.4.24.74
            BRENDA, the Enzyme Database: 3.4.24.74
            CAS: 188596-63-6
///
ENTRY       EC 3.4.24.75                Enzyme
NAME        lysostaphin;
            glycyl-glycine endopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolysis of the -Gly!Gly- bond in the pentaglycine inter-peptide
            link joining staphylococcal cell wall peptidoglycans
COFACTOR    Zinc [CPD:C00038]
COMMENT     A zinc-dependent, 25-kDa endopeptidase from Staphylococcus simulans.
            Lyses cells of S. aureus, in particular, by its action on the
            cross-bridges of the cell wall. Type example of peptidase family
            M23.
REFERENCE   1  [PMID:3547405]
  AUTHORS   Recsei PA, Gruss AD, Novick RP.
  TITLE     Cloning, sequence, and expression of the lysostaphin gene from
            Staphylococcus simulans.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 1127-31.
  ORGANISM  Staphylococcus simulans
REFERENCE   2  [PMID:8890152]
  AUTHORS   Baba T, Schneewind O.
  TITLE     Target cell specificity of a bacteriocin molecule: a C-terminal
            signal directs lysostaphin to the cell wall of Staphylococcus
            aureus.
  JOURNAL   EMBO. J. 15 (1996) 4789-97.
  ORGANISM  Staphylococcus aureus
REFERENCE   3  [PMID:9106216]
  AUTHORS   Thumm G, Gotz F.
  TITLE     Studies on prolysostaphin processing and characterization of the
            lysostaphin immunity factor (Lif) of Staphylococcus simulans biovar
            staphylolyticus.
  JOURNAL   Mol. Microbiol. 23 (1997) 1251-65.
  ORGANISM  Staphylococcus simulans
ORTHOLOGY   KO: K08259  lysostaphin
GENES       HAR: HEAR0247 HEAR2799
            SAU: SA0265(lytM)
            SAV: SAV0276(lytM)
            SAM: MW0252(lytM)
            SAR: SAR0273(lytM)
            SAS: SAS0252
            SAC: SACOL0263(lytM)
            SAB: SAB0215(lytM)
            SAA: SAUSA300_0270(lytM)
            SAO: SAOUHSC_00248
            SAJ: SaurJH9_0260
            SAH: SaurJH1_0267
            AVA: Ava_0183 Ava_2410 Ava_3195 Ava_4756 Ava_4929 Ava_C0210
STRUCTURES  PDB: 1QWY  2B0P  2B13  2B44  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.75
            ExPASy - ENZYME nomenclature database: 3.4.24.75
            ExplorEnz - The Enzyme Database: 3.4.24.75
            ERGO genome analysis and discovery system: 3.4.24.75
            BRENDA, the Enzyme Database: 3.4.24.75
            CAS: 9011-93-2
///
ENTRY       EC 3.4.24.76                Enzyme
NAME        flavastacin
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolyses polypeptides on the amino-side of Asp in -Xaa!Asp-. Acts
            very slowly on -Xaa!Glu
COMMENT     A zinc metalloendopeptidase in peptidase family M12 (astacin
            family), secreted by the bacterium Flavobacterium meningosepticum .
            The specificity is similar to that of EC 3.4.24.33, peptidyl-Asp
            metalloendopeptidase from Pseudomonas fragi but the two are reported
            to be structurally dissimilar
REFERENCE   1  [PMID:7771796]
  AUTHORS   Tarentino AL, Quinones G, Grimwood BG, Hauer CR, Plummer TH Jr.
  TITLE     Molecular cloning and sequence analysis of flavastacin: an
            O-glycosylated prokaryotic zinc metalloendopeptidase.
  JOURNAL   Arch. Biochem. Biophys. 319 (1995) 281-5.
  ORGANISM  Flavobacterium meningosepticum
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.76
            ExPASy - ENZYME nomenclature database: 3.4.24.76
            ExplorEnz - The Enzyme Database: 3.4.24.76
            ERGO genome analysis and discovery system: 3.4.24.76
            BRENDA, the Enzyme Database: 3.4.24.76
            CAS: 167973-66-2
///
ENTRY       EC 3.4.24.77                Enzyme
NAME        snapalysin;
            small neutral protease;
            SnpA gene product (Streptomyces lividans)
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Hydrolyses proteins with a preference for Tyr or Phe in the P1'
            position. Has no action on amino-acid p-nitroanilides
COMMENT     Type example of peptidase family M7.
REFERENCE   1
  AUTHORS   Kurisu, G., Sugimoto, A., Harada, S., Takagi, M., Imanaka, T. and
            Kai, Y.
  TITLE     Characterization of a small metalloprotease from Streptomyces
            caespitosus with high specificity to aromatic residues.
  JOURNAL   J. Ferment. Bioeng. 83 (1997) 590-592.
  ORGANISM  Streptomyces caespitosus
REFERENCE   2
  AUTHORS   Butler, M.J.
  TITLE     Snapalysin.
  JOURNAL   In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.),
            Handbook of Proteolytic Enzymes, Handbook of Proteolytic Enzymes,
            London, 1998, p. 1134-1135.
REFERENCE   3  [PMID:11132632]
  AUTHORS   Kurisu G, Kai Y, Harada S.
  TITLE     Structure of the zinc-binding site in the crystal structure of a
            zinc endoprotease from Streptomyces caespitosus at 1 A resolution.
  JOURNAL   J. Inorg. Biochem. 82 (2000) 225-8.
  ORGANISM  Streptomyces caespitosus
ORTHOLOGY   KO: K01416  snapalysin
GENES       SCO: SCO7432(mprA2)
            SMA: SAV2939 SAV4407
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.77
            ExPASy - ENZYME nomenclature database: 3.4.24.77
            ExplorEnz - The Enzyme Database: 3.4.24.77
            ERGO genome analysis and discovery system: 3.4.24.77
            BRENDA, the Enzyme Database: 3.4.24.77
///
ENTRY       EC 3.4.24.78                Enzyme
NAME        gpr endopeptidase;
            germination proteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Endopeptidase action with P4 Glu or Asp, P1 preferably Glu > Asp,
            P1' hydrophobic and P2' Ala
COMMENT     Initiates the degradation of small, acid-soluble proteins during
            spore germination in Bacillus megaterium. Type example of peptidase
            family M63.
REFERENCE   1  [PMID:10864493]
  AUTHORS   Ponnuraj K, Rowland S, Nessi C, Setlow P, Jedrzejas MJ.
  TITLE     Crystal structure of a novel germination protease from spores of
            Bacillus megaterium: structural arrangement and zymogen activation.
  JOURNAL   J. Mol. Biol. 300 (2000) 1-10.
  ORGANISM  Bacillus megaterium
ORTHOLOGY   KO: K06012  spore protease
GENES       BSU: BG10438(gpr)
            BHA: BH1340(gpr)
            BAN: BA4546(gpR)
            BAR: GBAA4546(gpR)
            BAA: BA_4993
            BAT: BAS4220
            BCE: BC4319
            BCA: BCE_4402(gpR)
            BCZ: BCZK4068(gpr)
            BCY: Bcer98_3048
            BTK: BT9727_4058(gpr)
            BTL: BALH_3910(gpr)
            BLI: BL02089(gpr)
            BLD: BLi02746(gpr)
            BCL: ABC1652(gpr)
            OIH: OB1975
            GKA: GK2511
            STH: STH1433
            CAC: CAC1275
            CPE: CPE2041(gpr)
            CPF: CPF_2298(gpr)
            CPR: CPR_2013(gpr)
            CTC: CTC02040
            CNO: NT01CX_0064
            CTH: Cthe_1038
            CDF: CD2470(gpr)
            CBO: CBO2966(gpr)
            CBE: Cbei_0822
            CKL: CKL_0895(gpr)
            AMT: Amet_3055
            CHY: CHY_1462(gpr)
            DSY: DSY2673
            DRM: Dred_2086
            SWO: Swol_0761
            CSC: Csac_2333
            TTE: TTE0946
            MTA: Moth_0926
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.78
            ExPASy - ENZYME nomenclature database: 3.4.24.78
            ExplorEnz - The Enzyme Database: 3.4.24.78
            ERGO genome analysis and discovery system: 3.4.24.78
            BRENDA, the Enzyme Database: 3.4.24.78
///
ENTRY       EC 3.4.24.79                Enzyme
NAME        pappalysin-1;
            insulin-like growth factor binding protein-4 protease;
            pregnancy-associated plasma protein-A
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleavage of the Met135!Lys bond in insulin-like growth factor
            binding protein (IGFBP)-4, and the Ser143!Lys bond in IGFBP-5
COMMENT     A 400-kDa disulfide-linked dimer. Circulates in human pregnancy
            mainly as a complex with the proform of eosinophil major basic
            protein, which acts as an inhibitor of the peptidase. The rate of
            hydrolysis of IGFBP-4 is increased about 20-fold by the presence of
            insulin-like growth factor (IGF), whereas that of IGFBP-5 is
            decreased about two-fold. In peptidase family M43.
REFERENCE   1  [PMID:10077652]
  AUTHORS   Lawrence JB, Oxvig C, Overgaard MT, Sottrup-Jensen L, Gleich GJ,
            Hays LG, Yates JR 3rd, Conover CA.
  TITLE     The insulin-like growth factor (IGF)-dependent IGF binding protein-4
            protease secreted by human fibroblasts is pregnancy-associated
            plasma protein-A.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 3149-53.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:11897673]
  AUTHORS   Chen BK, Overgaard MT, Bale LK, Resch ZT, Christiansen M, Oxvig C,
            Conover CA.
  TITLE     Molecular regulation of the IGF-binding protein-4 protease system in
            human fibroblasts: identification of a novel inducible inhibitor.
  JOURNAL   Endocrinology. 143 (2002) 1199-205.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K07762  pappalysin-1
GENES       HSA: 5069(PAPPA)
            MMU: 18491(Pappa)
            RNO: 313262(Pappa_predicted)
            CFA: 481692(PAPPA)
            BTA: 282647(PAPPA)
            GGA: 417245(PAPPA)
            DRE: 567184(LOC567184)
            SPU: 590919(LOC590919)
            ANI: AN6426.2
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.79
            ExPASy - ENZYME nomenclature database: 3.4.24.79
            ExplorEnz - The Enzyme Database: 3.4.24.79
            ERGO genome analysis and discovery system: 3.4.24.79
            BRENDA, the Enzyme Database: 3.4.24.79
///
ENTRY       EC 3.4.24.80                Enzyme
NAME        membrane-type matrix metalloproteinase-1;
            matrix metalloproteinase 14
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Endopeptidase activity. Activates progelatinase A by cleavage of the
            propeptide at Asn37!Leu. Other bonds hydrolysed include Gly35!Ile in
            the propeptide of collagenase 3, and Asn341!Phe, Asp441!Leu and
            Gln354!Thr in the aggrecan interglobular domain
COMMENT     In peptidase family M10, but, unlike most members of the family, is
            membrane-anchored. Believed to play an important role in the
            activation of progelatinase A at cell surfaces.
REFERENCE   1  [PMID:11532942]
  AUTHORS   Itoh Y, Takamura A, Ito N, Maru Y, Sato H, Suenaga N, Aoki T, Seiki
            M.
  TITLE     Homophilic complex formation of MT1-MMP facilitates proMMP-2
            activation on the cell surface and promotes tumor cell invasion.
  JOURNAL   EMBO. J. 20 (2001) 4782-93.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map04912  GnRH signaling pathway
ORTHOLOGY   KO: K07763  matrix metalloproteinase-14 (membrane-inserted)
GENES       HSA: 4323(MMP14)
            MMU: 17387(Mmp14)
            RNO: 81707(Mmp14)
            CFA: 403823(MMP14)
            BTA: 281915(MMP14)
            SSC: 397471(MT1-MMP)
            XTR: 594950(mmp14)
            DRE: 373880(mmp14b) 373882(mmp14a) 566945(LOC566945)
STRUCTURES  PDB: 1BUV  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.80
            ExPASy - ENZYME nomenclature database: 3.4.24.80
            ExplorEnz - The Enzyme Database: 3.4.24.80
            ERGO genome analysis and discovery system: 3.4.24.80
            BRENDA, the Enzyme Database: 3.4.24.80
///
ENTRY       EC 3.4.24.81                Enzyme
NAME        ADAM10 endopeptidase;
            Kuzbanian protein;
            myelin-associated disintegrin metalloproteinase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Endopeptidase of broad specificity
COMMENT     In peptidase family M12. Partially responsible for the
            "alpha-secretase" activity in brain that degrades the potentially
            harmful beta-amyloid peptide. Work with ADAM10-deficient mice
            supports a role in Notch signalling.
REFERENCE   1  [PMID:12475894]
  AUTHORS   Gutwein P, Mechtersheimer S, Riedle S, Stoeck A, Gast D, Joumaa S,
            Zentgraf H, Fogel M, Altevogt DP.
  TITLE     ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface
            and in released membrane vesicles.
  JOURNAL   FASEB. J. 17 (2003) 292-4.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map05120  Epithelial cell signaling in Helicobacter pylori
                            infection
ORTHOLOGY   KO: K06704  a disintegrin and metalloproteinase domain 10
GENES       HSA: 102(ADAM10)
            PTR: 746942(ADAM10)
            MMU: 11487(Adam10)
            RNO: 29650(Adam10)
            CFA: 478321(ADAM10)
            BTA: 282132(ADAM10)
            GGA: 374113(ADAM10)
            XTR: 733451(adam10)
            DRE: 393392(zgc:64203) 566044(LOC566044)
            SPU: 755122(LOC755122)
            DME: Dmel_CG1964(Kul) Dmel_CG7147(kuz)
            CEL: DY3.7(sup-17)
STRUCTURES  PDB: 2AO7  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.81
            ExPASy - ENZYME nomenclature database: 3.4.24.81
            ExplorEnz - The Enzyme Database: 3.4.24.81
            ERGO genome analysis and discovery system: 3.4.24.81
            BRENDA, the Enzyme Database: 3.4.24.81
///
ENTRY       EC 3.4.24.82                Enzyme
NAME        ADAMTS-4 endopeptidase;
            aggrecanase-1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Glutamyl endopeptidase; bonds cleaved include
            -Thr-Glu-Gly-Glu373!Ala-Arg-Gly-Ser- in the interglobular domain of
            mammalian aggrecan
COMMENT     In peptidase family M12. Thought to be biologically significant for
            the degradation of the aggrecan component of cartilage matrix.
REFERENCE   1  [PMID:11854269]
  AUTHORS   Westling J, Fosang AJ, Last K, Thompson VP, Tomkinson KN, Hebert T,
            McDonagh T, Collins-Racie LA, LaVallie ER, Morris EA, Sandy JD.
  TITLE     ADAMTS4 cleaves at the aggrecanase site (Glu373-Ala374) and
            secondarily at the matrix metalloproteinase site (Asn341-Phe342) in
            the aggrecan interglobular domain.
  JOURNAL   J. Biol. Chem. 277 (2002) 16059-66.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K07764  ADAM metallopeptidase with thrombospondin type 1 motif,
                        4
GENES       HSA: 9507(ADAMTS4)
            PTR: 457453(ADAMTS4)
            MMU: 240913(Adamts4)
            RNO: 66015(Adamts4)
            CFA: 488651(ADAMTS4)
            BTA: 286806(ADAMTS4)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.82
            ExPASy - ENZYME nomenclature database: 3.4.24.82
            ExplorEnz - The Enzyme Database: 3.4.24.82
            ERGO genome analysis and discovery system: 3.4.24.82
            BRENDA, the Enzyme Database: 3.4.24.82
///
ENTRY       EC 3.4.24.83                Enzyme
NAME        anthrax lethal factor endopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    lethal toxin
COMMENT     From the bacterium Bacilus anthracis that causes anthrax. One of
            three proteins that are collectively termed anthrax toxin. Cleaves
            several MAP kinase kinases near their N-termini, preventing them
            from phosphorylating the downstream mitogen-activated protein
            kinases. In peptidase family M34.
REFERENCE   1  [PMID:11700563]
  AUTHORS   Pannifer AD, Wong TY, Schwarzenbacher R, Renatus M, Petosa C,
            Bienkowska J, Lacy DB, Collier RJ, Park S, Leppla SH, Hanna P,
            Liddington RC.
  TITLE     Crystal structure of the anthrax lethal factor.
  JOURNAL   Nature. 414 (2001) 229-33.
  ORGANISM  Bacillus anthracis
ORTHOLOGY   KO: K08645  anthrax lethal factor endopeptidase
GENES       BAR: GBAA_pXO1_0172(lef)
            BAA: BXA0172(lef)
STRUCTURES  PDB: 1PWP  1PWQ  1YQY  1ZXV  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.83
            ExPASy - ENZYME nomenclature database: 3.4.24.83
            ExplorEnz - The Enzyme Database: 3.4.24.83
            ERGO genome analysis and discovery system: 3.4.24.83
            BRENDA, the Enzyme Database: 3.4.24.83
///
ENTRY       EC 3.4.24.84                Enzyme
NAME        Ste24 endopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    The peptide bond hydrolysed can be designated -C!aaX in which C is
            an S-isoprenylated cysteine residue, a is usually aliphatic and X is
            the C-terminal residue of the substrate protein, and may be any of
            several amino acids
COMMENT     Type example of peptidase family M48. One of two enzymes that can
            catalyse this processing step for mating a-factor in yeast.
            Subsequently, the S-isoprenylated cysteine residue that forms the
            new C-terminus is methyl-esterified and forms a hydrophobic
            membrane-anchor.
REFERENCE   1  [PMID:11581258]
  AUTHORS   Tam A, Schmidt WK, Michaelis S.
  TITLE     The multispanning membrane protein Ste24p catalyzes CAAX proteolysis
            and NH2-terminal processing of the yeast a-factor precursor.
  JOURNAL   J. Biol. Chem. 276 (2001) 46798-806.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K06013  STE24 endopeptidase
GENES       HSA: 10269(ZMPSTE24)
            MMU: 230709(Zmpste24)
            RNO: 313564(Zmpste24_predicted)
            CFA: 482460(ZMPSTE24)
            BTA: 538104(LOC538104)
            GGA: 419572(ZMPSTE24)
            XLA: 447784(MGC85351)
            XTR: 550009(LOC550009)
            DRE: 573028(LOC573028)
            SPU: 579174(LOC579174)
            DME: Dmel_CG9000
            ATH: AT4G01320(ATSTE24)
            OSA: 4330318
            SCE: YJR117W(STE24)
            AGO: AGOS_ABR163W
            CGR: CAGL0I08217g
            SPO: SPAC3H1.05
            AFM: AFUA_4G07590
            AOR: AO090023000816
            CNE: CND04910
            DDI: DDBDRAFT_0189115
            TAN: TA15890
            TPV: TP02_0928
            TET: TTHERM_01107240
            TCX: Tcr_0632
            NOC: Noc_0342
            RMA: Rmag_0587
            REU: Reut_A0906
            RME: Rmet_2575
            BVI: Bcep1808_0997
            BUR: Bcep18194_A4191
            BCN: Bcen_0598
            BCH: Bcen2424_1077
            BAM: Bamb_0953
            BPM: BURPS1710b_2959
            BTE: BTH_I1669
            PNU: Pnuc_0524
            RFR: Rfer_1411
            POL: Bpro_1699
            PNA: Pnap_1469
            AAV: Aave_1892
            AJS: Ajs_3347
            VEI: Veis_0323
            HAR: HEAR0875
            NET: Neut_2289
            NMU: Nmul_A0713
            MFA: Mfla_1474
            TDN: Tmden_1320
            GUR: Gura_0671
            PPD: Ppro_3199
            DDE: Dde_0070
            DPS: DP1308
            ADE: Adeh_2357
            AFW: Anae109_1511
            SFU: Sfum_1388
            NWI: Nwi_0189(htpX)
            MGM: Mmc1_0886
            ABA: Acid345_0572
            BTK: BT9727_0893
            DSY: DSY1797
            DRM: Dred_3217
            MTA: Moth_1231
            STP: Strop_3283
            SRU: SRU_0656
            CTE: CT1509
            CCH: Cag_0941
            CPH: Cpha266_1902
            PVI: Cvib_1333
            PLT: Plut_1513
            DEB: DehaBAV1_1231
            TME: Tmel_0359
            FNO: Fnod_1148
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.84
            ExPASy - ENZYME nomenclature database: 3.4.24.84
            ExplorEnz - The Enzyme Database: 3.4.24.84
            ERGO genome analysis and discovery system: 3.4.24.84
            BRENDA, the Enzyme Database: 3.4.24.84
///
ENTRY       EC 3.4.24.85                Enzyme
NAME        S2P endopeptidase
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Cleaves several transcription factors that are type-2 transmembrane
            proteins within membrane-spanning domains. Known substrates include
            sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and
            forms of the transcriptional activator ATF6. SREBP-2 is cleaved at
            the site DRSRILL483!CVLTFLCLSFNPLTSLLQWGGA, in which the
            membrane-spanning segment is underlined. The residues NP (bold), 11
            residues distal to the site of cleavage in the membrane-spanning
            domain, are important for cleavage by S2P endopeptidase. Replacement
            of either of these residues does not prevent cleavage, but there is
            no cleavage if both of these residues are replaced.
COMMENT     Type example of peptidase family M50. The transcription factors
            SREBP-1 and -2 are synthesized as precursor proteins that are
            attached to the membranes of the endoplasmic reticulum and two
            cleavages are needed to release the active factor so that it can
            move to the nucleus. This enzyme cleaves the second of these, and is
            thus the "site 2 protease", S2P.
REFERENCE   1  [PMID:10693756]
  AUTHORS   Brown MS, Ye J, Rawson RB, Goldstein JL.
  TITLE     Regulated intramembrane proteolysis: a control mechanism conserved
            from bacteria to humans.
  JOURNAL   Cell. 100 (2000) 391-8.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K07765  S2P endopeptidase
GENES       HSA: 51360(MBTPS2)
            MMU: 270669(Mbtps2)
            RNO: 302705(Mbtps2)
            CFA: 491771(LOC491771)
            BTA: 533134(MGC139715)
            GGA: 427996(MBTPS2)
            XTR: 549815(LOC549815)
            DRE: 334658(mbtps2)
            SPU: 755978(LOC755978)
            DME: Dmel_CG8988
            CEL: Y56A3A.2
            OSA: 4324173
            CME: CMB142C
            DDI: DDBDRAFT_0217735
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.85
            ExPASy - ENZYME nomenclature database: 3.4.24.85
            ExplorEnz - The Enzyme Database: 3.4.24.85
            ERGO genome analysis and discovery system: 3.4.24.85
            BRENDA, the Enzyme Database: 3.4.24.85
///
ENTRY       EC 3.4.24.86                Enzyme
NAME        ADAM 17 endopeptidase;
            TACE
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Metalloendopeptidases
REACTION    Reaction tumor necrosis factor alpha-converting enzyme
COMMENT     In peptidase family M12. In vivo, the cleavage of tumor necrosis
            factor alpha precursor releases the soluble, 17-kDa TNFalpha, which
            induces inflammation.
REFERENCE   1  [PMID:11733179]
  AUTHORS   Black RA.
  TITLE     Tumor necrosis factor-alpha converting enzyme.
  JOURNAL   Int. J. Biochem. Cell. Biol. 34 (2002) 1-5.
PATHWAY     PATH: map04330  Notch signaling pathway
            PATH: map05120  Epithelial cell signaling in Helicobacter pylori
                            infection
ORTHOLOGY   KO: K06059  a disintegrin and metalloproteinase domain 17
GENES       HSA: 6868(ADAM17)
            PTR: 459018(ADAM17)
            MMU: 11491(Adam17)
            RNO: 57027(Adam17)
            CFA: 475662(ADAM17)
            BTA: 517541(LOC517541)
            GGA: 421931(ADAM17)
            DRE: 324142(adam17a) 560657(adam17b)
            SPU: 585715(LOC585715)
            DME: Dmel_CG7908
            CEL: ZK154.7(metalloprotease)
STRUCTURES  PDB: 1ZXC  2A8H  2DDF  2FV5  2FV9  2I47  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.24.86
            ExPASy - ENZYME nomenclature database: 3.4.24.86
            ExplorEnz - The Enzyme Database: 3.4.24.86
            ERGO genome analysis and discovery system: 3.4.24.86
            BRENDA, the Enzyme Database: 3.4.24.86
///
ENTRY       EC 3.4.25.1                 Enzyme
NAME        proteasome endopeptidase complex;
            ingensin;
            macropain;
            multicatalytic endopeptidase complex;
            prosome;
            multicatalytic proteinase (complex);
            MCP;
            proteasome;
            large multicatalytic protease;
            multicatalytic proteinase;
            proteasome organelle;
            alkaline protease;
            26S protease;
            tricorn proteinase;
            tricorn protease
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Threonine endopeptidases
REACTION    Cleavage of peptide bonds with very broad specificity
INHIBITOR   Mercurial reagent [CPD:C02556];
            Inhibitor of serine endopeptidase [CPD:C04198]
COMMENT     A 20-S protein composed of 28 subunits arranged in four rings of
            seven. The outer rings are composed of alpha subunits, but the beta
            subunits forming the inner rings are responsible for peptidase
            activity. In eukaryotic organisms there are up to seven different
            types of beta subunits, three of which may carry the N-terminal
            threonine residues that are the nucleophiles in catalysis, and show
            different specificities. The molecule is barrel-shaped, and the
            active sites are on the inner surfaces. Terminal apertures restrict
            access of substrates to the active sites. There is evidence that
            catalytic subunits are replaced by others under some conditions so
            as to alter the specificity of proteolysis, perhaps optimizing it
            for the formation of antigenic peptides. A complex of the 20-S
            proteasome endopeptidase complex with a 19-S regulatory unit is the
            26-S proteasome that degrades ubiquitin-protein conjugates. Type
            example of peptidase family T1.
REFERENCE   1  [PMID:7725107]
  AUTHORS   Seemuller E, Lupas A, Stock D, Lowe J, Huber R, Baumeister W.
  TITLE     Proteasome from Thermoplasma acidophilum: a threonine protease.
  JOURNAL   Science. 268 (1995) 579-82.
  ORGANISM  Thermoplasma acidophilum [GN:tac]
REFERENCE   2  [PMID:8811196]
  AUTHORS   Coux O, Tanaka K, Goldberg AL.
  TITLE     Structure and functions of the 20S and 26S proteasomes.
  JOURNAL   Annu. Rev. Biochem. 65 (1996) 801-47.
REFERENCE   3  [PMID:9087403]
  AUTHORS   Groll M, Ditzel L, Lowe J, Stock D, Bochtler M, Bartunik HD, Huber
            R.
  TITLE     Structure of 20S proteasome from yeast at 2.4 A resolution.
  JOURNAL   Nature. 386 (1997) 463-71.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4  [PMID:9748229]
  AUTHORS   Dick TP, Nussbaum AK, Deeg M, Heinemeyer W, Groll M, Schirle M,
            Keilholz W, Stevanovic S, Wolf DH, Huber R, Rammensee HG, Schild H.
  TITLE     Contribution of proteasomal beta-subunits to the cleavage of peptide
            substrates analyzed with yeast mutants.
  JOURNAL   J. Biol. Chem. 273 (1998) 25637-46.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], human [GN:hsa]
PATHWAY     PATH: map03050  Proteasome
ORTHOLOGY   KO: K01418  proteasome
            KO: K02725  20S proteasome subunit alpha 6
            KO: K02726  20S proteasome subunit alpha 2
            KO: K02727  20S proteasome subunit alpha 7
            KO: K02728  20S proteasome subunit alpha 3
            KO: K02729  20S proteasome subunit alpha 5
            KO: K02730  20S proteasome subunit alpha 1
            KO: K02731  20S proteasome subunit alpha 4
            KO: K02732  20S proteasome subunit beta 6
            KO: K02733  20S proteasome subunit beta 10
            KO: K02734  20S proteasome subunit beta 4
            KO: K02735  20S proteasome subunit beta 3
            KO: K02736  20S proteasome subunit beta 7
            KO: K02737  20S proteasome subunit beta 5
            KO: K02738  20S proteasome subunit beta 1
            KO: K02739  20S proteasome subunit beta 2
            KO: K02740  20S proteasome subunit beta 8
            KO: K02741  20S proteasome subunit beta 9
            KO: K03432  proteasome alpha subunit
            KO: K03433  proteasome beta subunit
            KO: K06690  20S proteasome subunit alpha 8
GENES       HSA: 143471(PSMA8) 5682(PSMA1) 5683(PSMA2) 5684(PSMA3) 5685(PSMA4)
                 5686(PSMA5) 5687(PSMA6) 5688(PSMA7) 5689(PSMB1) 5690(PSMB2)
                 5691(PSMB3) 5692(PSMB4) 5693(PSMB5) 5694(PSMB6) 5695(PSMB7)
                 5696(PSMB8) 5698(PSMB9) 5699(PSMB10)
            PTR: 451040(PSMA1) 452861(PSMA6) 453569(PSMA4) 454453(PSMB6)
                 454616(LOC454616) 457293(PSMB4) 458383(PSMA7) 464723(PSMB7)
                 468505(PSMA8) 469277(PSMB2) 469795(LOC469795) 471978(TAP1)
                 472653(PSMA2) 473258(PSMB1)
            MCC: 677719(PSMB5)
            MMU: 16912(Psmb9) 16913(Psmb8) 19166(Psma2) 19167(Psma3)
                 19170(Psmb1) 19171(Psmb10) 19172(Psmb4) 19173(Psmb5)
                 19175(Psmb6) 19177(Psmb7) 26440(Psma1) 26441(Psma4)
                 26442(Psma5) 26443(Psma6) 26444(Psma7) 26445(Psmb2)
                 26446(Psmb3) 73677(Psma8)
            RNO: 24967(Psmb9) 24968(Psmb8) 291983(Psmb10) 29425(Psmb5)
                 29666(Psmb6) 29668(Psma1) 29669(Psma2) 29670(Psma3)
                 29671(Psma4) 29672(Psma5) 29673(Psma6) 29674(Psma7)
                 29675(Psmb2) 29676(Psmb3) 58854(Psmb4) 85492(Psmb7)
                 94198(Psmb1)
            CFA: 404305(PSMA7) 474865(PSMB8) 474867(PSMB9) 475040(PSMB1)
                 475132(PSMA4) 475338(PSMB2) 475848(PSMB4) 475870(PSMA2)
                 476867(PSMA1) 480246(PSMB5) 480290(PSMA6) 480338(PSMA3)
                 480537(PSMB3) 489749(PSMB10) 490123(PSMA5) 490508(PSMA8)
                 607261(LOC607261) 607466(PSMB6) 613000(LOC613000)
            BTA: 282013(PSMB8) 282328(PSMB10) 505050(PSMA7) 505176(PSMA3)
                 506203(PSMB4) 507213(PSMA6) 510069(PSMB6) 510155(PSMA5)
                 510423(PSMA4) 510593(PSMB9) 511207(MGC133789) 514237(PSMB1)
                 515503(PSMA1) 533874(MGC128032) 534640(PSMB5) 539141(PSMA2)
            SSC: 396975(LMP7) 654294(SBAB-554F3.3)
            GGA: 378915(PSMB7) 395318(PSMA7) 395874(PSMA1) 415357(PSMA4)
                 419630(PSMB2) 419997(PSMB3) 421551(PSMB1) 423326(PSMA6)
                 423542(PSMA3) 426937(RCJMB04_14i9) 429986(PSMB4)
            XLA: 379551(MGC68991) 379676(MGC68557) 379720(MGC69086)
                 379935(psma3) 380127(psmb1) 380382(psma4) 380584(psmb4)
                 394357(psma4-B) 399109(Psma7) 399279(Psma2) 399439(PSMB8)
                 431796(MGC84496) 443966(MGC80364) 444215(MGC80760)
                 446620(psma6) 447359(MGC84123) 495277(LOC495277)
                 496005(LOC496005)
            XTR: 394589(psmb1) 394668(psma7) 394718(MGC76321) 394756(psmb6)
                 445259(LMP2) 493360(TGas091k05.1) 493521(MGC90008)
                 496467(LOC496467) 496603(TGas081h10.1) 496707(psma3)
                 549136(LOC549136) 549257(psmb3)
            DRE: 171585(psma6a) 30387(psmb5) 30388(psmb6) 30665(psmb9a)
                 30666(psmb8) 326687(psma4) 403011(psma5) 406445(zgc:77139)
                 406673(psmb3) 436862(zgc:92716) 445033(zgc:92726)
                 445413(psmb1) 550499(zgc:110330) 554153(psma2)
                 564370(zgc:114044) 572683(psmb7) 573095(LOC573095)
                 64278(psmb7) 64279(psmb11) 64280(psmb10) 64281(psmb9b)
                 83917(psma6b)
            SPU: 574918(LOC574918) 575240(LOC575240) 576984(LOC576984)
                 579458(LOC579458) 581926(LOC581926) 584825(LOC584825)
                 587539(LOC587539) 588252(LOC588252) 588670(LOC588670)
                 589517(LOC589517) 591599(LOC591599) 752223(LOC752223)
                 757656(LOC757656)
            DME: Dmel_CG10938(ProsMA5) Dmel_CG11888 Dmel_CG11981 Dmel_CG12000
                 Dmel_CG12323 Dmel_CG1341 Dmel_CG13549(yip3) Dmel_CG1489
                 Dmel_CG1519(Prosalpha7) Dmel_CG16916 Dmel_CG17268 Dmel_CG17301
                 Dmel_CG17331 Dmel_CG1736 Dmel_CG18341 Dmel_CG18495(Prosalpha6)
                 Dmel_CG3329(Prosbeta2) Dmel_CG3422(Pros28.1)
                 Dmel_CG4097(Pros26) Dmel_CG4569 Dmel_CG4904(Pros35)
                 Dmel_CG5266(Pros25) Dmel_CG5648 Dmel_CG8392(l(2)05070)
                 Dmel_CG9327(Pros29) Dmel_CG9868
            CEL: C02F5.9(pbs-6) C15H11.7(pas-1) C36B1.4(pas-4) C47B2.4(pbs-2)
                 CD4.6(protease) D1054.2(pas-2) F25H2.9(pas-5) F39H11.5(pbs-7)
                 K05C4.1(pbs-5) K08D12.1(pbs-1) T20F5.2(peptidase)
                 Y110A7A.14(endopeptidase) Y38A8.2(Peptidase) ZK945.2(pas-7)
            ATH: AT1G13060(PBE1) AT1G16470(PAB1) AT1G21720(PBC1)
                 AT1G47250(PAF2) AT1G53850(PAE1) AT1G56450(PBG1)
                 AT1G77440(PBC2) AT1G79210 AT2G27020(PAG1) AT3G14290(PAE2)
                 AT3G22110(PAC1) AT3G22630(PBD1) AT3G26340 AT3G27430(PBB1)
                 AT4G14800(PBD2) AT5G35590(PAA1) AT5G42790(PAF1)
                 AT5G66140(PAD2)
            OSA: 4327357 4328215 4330075 4330861 4331828 4333000 4333803
                 4338009 4339169 4340065 4340166 4340253 4340285 4341637
                 4343187 4346117 4346245 4347507 4347573 4347710 4350922
            CME: CMD060C CME128C CMG188C CMH119C CMH154C CMK289C CML273C
                 CMN208C CMO149C CMO197C CMQ225C CMR302C CMT379C CMT477C
            SCE: YBL041W(PRE7) YER012W(PRE1) YER094C(PUP3) YFR050C(PRE4)
                 YGL011C(SCL1) YGR135W(PRE9) YGR253C(PUP2) YJL001W(PRE3)
                 YML092C(PRE8) YMR314W(PRE5) YOL038W(PRE6) YOR157C(PUP1)
                 YOR362C(PRE10) YPR103W(PRE2)
            AGO: AGOS_AAL172C AGOS_AAR012C AGOS_AAR019W AGOS_AAR119W
                 AGOS_ABR217C AGOS_ADL354W AGOS_ADR401C AGOS_AEL326C
                 AGOS_AER296W AGOS_AFR258W AGOS_AFR318W AGOS_AGL089W
                 AGOS_AGL324W AGOS_AGL336W
            PIC: PICST_36375 PICST_41423 PICST_41720 PICST_55136 PICST_55763
                 PICST_61383 PICST_62487 PICST_63922 PICST_65073(PUP1)
                 PICST_75017(RPT1) PICST_81403 PICST_82713 PICST_87371
                 PICST_89662(PRE4)
            CAL: CaO19.1336(PUP3) CaO19.3593 CaO19.6991 CaO19_350(CaO19.350)
                 CaO19_4025(CaO19.4025) CaO19_4230(CaO19.4230)
                 CaO19_5378(CaO19.5378) CaO19_7335(CaO19.7335)
                 CaO19_7605(CaO19.7605)
            CGR: CAGL0A00407g CAGL0A04719g CAGL0D03058g CAGL0F01199g
                 CAGL0F04477g CAGL0G01804g CAGL0H06105g CAGL0H07007g
                 CAGL0H09548g CAGL0I02442g CAGL0I04906g CAGL0I10406g
                 CAGL0L04312g CAGL0M14003g
            SPO: SPAC13C5.01c SPAC22F8.06 SPAC23D3.07 SPAC31A2.04c SPAC323.02c
                 SPAC4A8.13c(pts1) SPAC6G10.04c SPBC106.16 SPBC4C3.10c
                 SPBC577.10 SPBC646.16 SPCC1442.06 SPCC1795.04c SPCC63.12c
            ANI: AN1757.2 AN2085.2 AN3756.2 AN3932.2 AN4449.2 AN4457.2
                 AN4869.2 AN5783.2 AN5784.2 AN5793.2 AN5872.2 AN6547.2 AN6726.2
                 AN8054.2
            AFM: AFUA_2G04910 AFUA_2G11440 AFUA_3G11300 AFUA_4G07420
                 AFUA_4G07510 AFUA_5G02150 AFUA_6G04790 AFUA_6G06350
                 AFUA_6G06440 AFUA_6G06450 AFUA_6G08310 AFUA_6G08960
                 AFUA_7G04650 AFUA_7G05870
            AOR: AO090001000574 AO090003000005 AO090003000015 AO090003000016
                 AO090003000095 AO090003000295 AO090003000682 AO090005000157
                 AO090005000451 AO090023000824 AO090023000831 AO090026000504
                 AO090102000273 AO090701000060
            ANG: An02g07190(tbpA)
            CNE: CNA03730 CNB03070 CNB04280 CNB04850 CNB05540 CNC03530
                 CNC04990 CND01660 CNF01080 CNF01860 CNF02080 CNH01360 CNH03610
                 CNK02950
            UMA: UM00511.1 UM01275.1 UM02046.1 UM04179.1 UM05457.1 UM05652.1
                 UM05687.1 UM05860.1 UM05986.1 UM06234.1
            ECU: ECU02_0340 ECU05_0290 ECU05_1340 ECU05_1400 ECU07_1040
                 ECU07_1420 ECU08_0280 ECU08_1580 ECU08_1870 ECU09_0330
                 ECU09_0720 ECU10_0550 ECU10_1450 ECU11_1670
            DDI: DDB_0185059(psmA7) DDB_0191199(psmB6) DDB_0191264(psmA3)
                 DDB_0214953(psmA4) DDB_0214956(psmA1) DDB_0232930(psmA5)
                 DDB_0232932(psmB3) DDB_0232933(psmB7) DDB_0232934(psmB4)
                 DDB_0232935(psmA2) DDB_0232956(psmA6) DDB_0232958(psmB2)
                 DDB_0232959(psmB5)
            PFA: MAL13P1.190 MAL13P1.270 MAL1P2.08 MAL3P6.31 MAL8P1.128
                 MAL8P1.142 PF07_0112 PF10_0081 PF10_0111 PF10_0174 PF10_0298
                 PF11_0303 PF11_0314 PF13_0033 PF13_0063 PF13_0156 PF13_0282
                 PF14_0025 PF14_0632 PF14_0676 PF14_0716 PFE0915c PFF0420c
                 PFI0630w PFI1545c
            CPV: cgd2_1440 cgd2_2050 cgd2_530 cgd2_860 cgd3_2170 cgd3_2200
                 cgd3_2530 cgd4_250 cgd5_3220 cgd5_4210 cgd7_3660
            CHO: Chro.10054 Chro.20061 Chro.20097 Chro.20158 Chro.20222
                 Chro.30254 Chro.30255 Chro.30260 Chro.30293 Chro.40039
                 Chro.50050 Chro.50200 Chro.50424 Chro.70408
            TAN: TA03785 TA04595 TA06155 TA06335 TA07815 TA08070 TA10875
                 TA11345 TA11350 TA13865 TA15875 TA15900 TA18320 TA19315
                 TA20200
            TPV: TP01_0187 TP01_0874 TP01_0908 TP01_1231 TP02_0560 TP02_0927
                 TP02_0930 TP03_0293 TP03_0446 TP03_0809 TP04_0315 TP04_0366
                 TP04_0618 TP04_0827 TP04_0828
            TET: TTHERM_00030440 TTHERM_00043880 TTHERM_00106960
                 TTHERM_00147560 TTHERM_00158210 TTHERM_00379050
                 TTHERM_00470650 TTHERM_00548160 TTHERM_00633530
                 TTHERM_00666560 TTHERM_01050690
            TBR: Tb09.211.1250 Tb09.211.2590 Tb10.100.0120 Tb10.100.0170
                 Tb10.70.0790 Tb10.70.0850 Tb10.70.2490 Tb11.02.4870
                 Tb11.02.5170 Tb927.3.780 Tb927.4.430 Tb927.6.1260 Tb927.7.4420
                 Tb927.7.4790
            TCR: 416883.18 503613.20 503781.70 503891.100 504069.10 504069.53
                 504213.120 506167.40 506327.10 506779.50 506885.350 506985.30
                 507521.50 507603.40 507639.40 507775.50 508461.430 508577.160
                 509429.110 510287.30 510689.30 510729.70 511145.43 511153.140
                 511165.70 511867.50
            LMA: LmjF06.0140 LmjF11.0240 LmjF12.0030 LmjF14.0310 LmjF21.1700
                 LmjF21.1830 LmjF27.0190 LmjF28.0110 LmjF34.4340 LmjF34.4370
                 LmjF34.4400 LmjF34.4430 LmjF34.4460 LmjF34.4490 LmjF34.4520
                 LmjF35.3840 LmjF35.4850 LmjF36.0320 LmjF36.1600 LmjF36.1650
            EHI: 1.t00153 113.t00002 13.t00056 166.t00011 185.t00017
                 189.t00013 203.t00020 21.t00020 214.t00008 26.t00040
                 289.t00008 31.t00030 404.t00003 616.t00004 70.t00037 72.t00011
                 74.t00025 81.t00025 86.t00017 94.t00015
            MTU: Rv2109c(prcA) Rv2110c(prcB)
            MTC: MT2169(prcA) MT2170(prcB)
            MBO: Mb2133c(prcA) Mb2134c(prcB)
            MBB: BCG_2126c(prcA) BCG_2127c(prcB)
            MLE: ML1322(prcB) ML1323(prcA)
            MPA: MAP1834c(prcA) MAP1835c(prcB)
            MAV: MAV_2405
            MSM: MSMEG_3894 MSMEG_3895
            MUL: MUL_2330(prcA)
            MMC: Mmcs_3129 Mmcs_3130
            MKM: Mkms_3190
            NFA: nfa31710(prcA) nfa31720(prcB)
            RHA: RHA1_ro00843 RHA1_ro00844
            SCO: SCO1643(pcrA) SCO1644(prcB)
            SMA: SAV2812(prcB2) SAV6681(prcB1) SAV6682(prcA)
            ART: Arth_2177
            PAC: PPA1206 PPA1207
            TFU: Tfu_1789 Tfu_1790
            FRA: Francci3_2626 Francci3_2627
            FAL: FRAAL2873(prcB) FRAAL2874(prcA)
            ACE: Acel_1189
            SEN: SACE_2251(prcB) SACE_2252(prcA)
            MJA: MJ0591 MJ1237
            MMP: MMP0251(psmA) MMP0695(psmB)
            MMQ: MmarC5_0881 MmarC5_1422
            MMZ: MmarC7_1253 MmarC7_1722
            MAE: Maeo_0050 Maeo_0181
            MVN: Mevan_1264 Mevan_1573
            MAC: MA1779(psmA) MA3873(psmB)
            MBA: Mbar_A0194 Mbar_A2503
            MMA: MM_0694 MM_2620
            MBU: Mbur_0196 Mbur_0374
            MTP: Mthe_0083 Mthe_1365
            MHU: Mhun_0846 Mhun_2282
            MEM: Memar_1198 Memar_1678
            MBN: Mboo_1384 Mboo_1822
            MTH: MTH1202 MTH686
            MST: Msp_0282(psmB) Msp_1248(psmA)
            MSI: Msm_0245 Msm_1037
            MKA: MK0385(hslV_1) MK1228(hslV_2)
            AFU: AF0481(psmB) AF0490(psmA)
            HAL: VNG0166G(psmB) VNG0880G(psmA)
            HMA: rrnAC0442(psmA3) rrnAC1174(psmA4) rrnAC1772(psmA1)
                 rrnAC1773(psmA2)
            HWA: HQ1516A(psmA1) HQ2454A(psmA2) HQ2661A(psmB)
            NPH: NP3472A(psmB) NP3738A(psmA)
            TAC: Ta0612 Ta1288
            TVO: TVN0304 TVN0663
            PTO: PTO0686 PTO0804
            PHO: PH0245 PH1402 PH1553
            PAB: PAB0417(psmA) PAB1867 PAB2199(psmB)
            PFU: PF0159 PF1404 PF1571
            TKO: TK1429 TK1637 TK2207
            RCI: RCIX2121(psmA) RCIX2364(psmB)
            APE: APE_0507.1 APE_0521.1 APE_1449
            SMR: Smar_0856 Smar_0932 Smar_0938
            IHO: Igni_0453 Igni_0616 Igni_0980
            HBU: Hbut_0568 Hbut_1564 Hbut_1567
            SSO: SSO0278 SSO0738 SSO0766
            STO: ST0324 ST0446 ST0477
            SAI: Saci_0613(psmA) Saci_0662 Saci_0909
            MSE: Msed_0074 Msed_2052 Msed_2268
            PAI: PAE0807 PAE2215 PAE3595
            PIS: Pisl_0754 Pisl_0844 Pisl_1097
            PCL: Pcal_0021 Pcal_0936 Pcal_2008
            PAS: Pars_0055 Pars_1929 Pars_2211
            TPE: Tpen_0307 Tpen_0392 Tpen_0584
            NEQ: NEQ203 NEQ521
STRUCTURES  PDB: 1J2P  1J2Q  1Q5Q  1Q5R  1YA7  1YAR  1YAU  1Z7Q  2F16  2FAK  
                 2FNY  2GPL  2H6J  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.25.1
            ExPASy - ENZYME nomenclature database: 3.4.25.1
            ExplorEnz - The Enzyme Database: 3.4.25.1
            ERGO genome analysis and discovery system: 3.4.25.1
            BRENDA, the Enzyme Database: 3.4.25.1
            CAS: 140879-24-9
///
ENTRY       EC 3.4.99.1       Obsolete  Enzyme
NAME        Transferred to 3.4.23.28
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.23.28 acrocylindropepsin (EC 3.4.99.1
            created 1972, deleted 1978 [transferred to EC 3.4.23.6, deleted
            1992])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.1
            ExPASy - ENZYME nomenclature database: 3.4.99.1
            ExplorEnz - The Enzyme Database: 3.4.99.1
            ERGO genome analysis and discovery system: 3.4.99.1
            BRENDA, the Enzyme Database: 3.4.99.1
///
ENTRY       EC 3.4.99.2       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: agavain (EC 3.4.99.2 created 1972, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.2
            ExPASy - ENZYME nomenclature database: 3.4.99.2
            ExplorEnz - The Enzyme Database: 3.4.99.2
            ERGO genome analysis and discovery system: 3.4.99.2
            BRENDA, the Enzyme Database: 3.4.99.2
///
ENTRY       EC 3.4.99.3       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: angiotensinase (EC 3.4.99.3 created 1972, deleted
            1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.3
            ExPASy - ENZYME nomenclature database: 3.4.99.3
            ExplorEnz - The Enzyme Database: 3.4.99.3
            ERGO genome analysis and discovery system: 3.4.99.3
            BRENDA, the Enzyme Database: 3.4.99.3
///
ENTRY       EC 3.4.99.4       Obsolete  Enzyme
NAME        Transferred to 3.4.23.12
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.23.12 nepenthesin (EC 3.4.99.4 created
            1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.4
            ExPASy - ENZYME nomenclature database: 3.4.99.4
            ExplorEnz - The Enzyme Database: 3.4.99.4
            ERGO genome analysis and discovery system: 3.4.99.4
            BRENDA, the Enzyme Database: 3.4.99.4
///
ENTRY       EC 3.4.99.5       Obsolete  Enzyme
NAME        Transferred to 3.4.24.3
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.24.3 microbial collagenase (EC
            3.4.99.5 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.5
            ExPASy - ENZYME nomenclature database: 3.4.99.5
            ExplorEnz - The Enzyme Database: 3.4.99.5
            ERGO genome analysis and discovery system: 3.4.99.5
            BRENDA, the Enzyme Database: 3.4.99.5
///
ENTRY       EC 3.4.99.6       Obsolete  Enzyme
NAME        Transferred to 3.4.24.21
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.24.21 astacin (EC 3.4.99.6 created
            1972, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.6
            ExPASy - ENZYME nomenclature database: 3.4.99.6
            ExplorEnz - The Enzyme Database: 3.4.99.6
            ERGO genome analysis and discovery system: 3.4.99.6
            BRENDA, the Enzyme Database: 3.4.99.6
///
ENTRY       EC 3.4.99.7       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: euphorbain (EC 3.4.99.7 created 1972, deleted 1989)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.7
            ExPASy - ENZYME nomenclature database: 3.4.99.7
            ExplorEnz - The Enzyme Database: 3.4.99.7
            ERGO genome analysis and discovery system: 3.4.99.7
            BRENDA, the Enzyme Database: 3.4.99.7
///
ENTRY       EC 3.4.99.8       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: Gliocladium proteinase (EC 3.4.99.8 created 1972,
            deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.8
            ExPASy - ENZYME nomenclature database: 3.4.99.8
            ExplorEnz - The Enzyme Database: 3.4.99.8
            ERGO genome analysis and discovery system: 3.4.99.8
            BRENDA, the Enzyme Database: 3.4.99.8
///
ENTRY       EC 3.4.99.9       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: hurain (EC 3.4.99.9 created 1972, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.9
            ExPASy - ENZYME nomenclature database: 3.4.99.9
            ExplorEnz - The Enzyme Database: 3.4.99.9
            ERGO genome analysis and discovery system: 3.4.99.9
            BRENDA, the Enzyme Database: 3.4.99.9
///
ENTRY       EC 3.4.99.10      Obsolete  Enzyme
NAME        Transferred to 3.4.24.56
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.24.56 insulysin (EC 3.4.99.10 created
            1972, transferred 1976 to EC 3.4.22.11, transferred 1978 to EC
            3.4.99.45, transferred 1993 to EC 3.4.24.56)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.10
            ExPASy - ENZYME nomenclature database: 3.4.99.10
            ExplorEnz - The Enzyme Database: 3.4.99.10
            ERGO genome analysis and discovery system: 3.4.99.10
            BRENDA, the Enzyme Database: 3.4.99.10
///
ENTRY       EC 3.4.99.11      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: streptomyces alkalophilic keratinase (EC 3.4.99.11
            created 1965 as EC 3.4.4.25, transferred 1972 to EC 3.4.99.11,
            deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.11
            ExPASy - ENZYME nomenclature database: 3.4.99.11
            ExplorEnz - The Enzyme Database: 3.4.99.11
            ERGO genome analysis and discovery system: 3.4.99.11
            BRENDA, the Enzyme Database: 3.4.99.11
///
ENTRY       EC 3.4.99.12      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: trichophyton mentagrophytes keratinase (EC 3.4.99.12
            created 1972, deleted 1978 [transferred to EC 3.4.24.10, deleted
            1992])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.12
            ExPASy - ENZYME nomenclature database: 3.4.99.12
            ExplorEnz - The Enzyme Database: 3.4.99.12
            ERGO genome analysis and discovery system: 3.4.99.12
            BRENDA, the Enzyme Database: 3.4.99.12
///
ENTRY       EC 3.4.99.13      Obsolete  Enzyme
NAME        Transferred to 3.4.24.32
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.24.32 beta-lytic metalloendopeptidase
            (EC 3.4.99.13 created 1972, deleted 1978 [transferred to EC
            3.4.24.4, deleted 1992])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.13
            ExPASy - ENZYME nomenclature database: 3.4.99.13
            ExplorEnz - The Enzyme Database: 3.4.99.13
            ERGO genome analysis and discovery system: 3.4.99.13
            BRENDA, the Enzyme Database: 3.4.99.13
///
ENTRY       EC 3.4.99.14      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: mexicanain (EC 3.4.99.14 created 1972, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.14
            ExPASy - ENZYME nomenclature database: 3.4.99.14
            ExplorEnz - The Enzyme Database: 3.4.99.14
            ERGO genome analysis and discovery system: 3.4.99.14
            BRENDA, the Enzyme Database: 3.4.99.14
///
ENTRY       EC 3.4.99.15      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: paecilomyces proteinase (EC 3.4.99.15 created 1972,
            deleted 1978 [transferred to EC 3.4.23.6, deleted 1992])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.15
            ExPASy - ENZYME nomenclature database: 3.4.99.15
            ExplorEnz - The Enzyme Database: 3.4.99.15
            ERGO genome analysis and discovery system: 3.4.99.15
            BRENDA, the Enzyme Database: 3.4.99.15
///
ENTRY       EC 3.4.99.16      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: penicillium notatum extracellular proteinase (EC
            3.4.99.16 created 1972, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.16
            ExPASy - ENZYME nomenclature database: 3.4.99.16
            ExplorEnz - The Enzyme Database: 3.4.99.16
            ERGO genome analysis and discovery system: 3.4.99.16
            BRENDA, the Enzyme Database: 3.4.99.16
///
ENTRY       EC 3.4.99.17      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: peptidoglycan endopeptidase (EC 3.4.99.17 created
            1972, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.17
            ExPASy - ENZYME nomenclature database: 3.4.99.17
            ExplorEnz - The Enzyme Database: 3.4.99.17
            ERGO genome analysis and discovery system: 3.4.99.17
            BRENDA, the Enzyme Database: 3.4.99.17
///
ENTRY       EC 3.4.99.18      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: pinguinain (EC 3.4.99.18 created 1972, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.18
            ExPASy - ENZYME nomenclature database: 3.4.99.18
            ExplorEnz - The Enzyme Database: 3.4.99.18
            ERGO genome analysis and discovery system: 3.4.99.18
            BRENDA, the Enzyme Database: 3.4.99.18
///
ENTRY       EC 3.4.99.19      Obsolete  Enzyme
NAME        Transferred to 3.4.23.15
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.23.15 renin (EC 3.4.99.19 created
            1972, deleted 1981)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.19
            ExPASy - ENZYME nomenclature database: 3.4.99.19
            ExplorEnz - The Enzyme Database: 3.4.99.19
            ERGO genome analysis and discovery system: 3.4.99.19
            BRENDA, the Enzyme Database: 3.4.99.19
///
ENTRY       EC 3.4.99.20      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: scopulariopsis proteinase (EC 3.4.99.20 created 1972,
            deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.20
            ExPASy - ENZYME nomenclature database: 3.4.99.20
            ExplorEnz - The Enzyme Database: 3.4.99.20
            ERGO genome analysis and discovery system: 3.4.99.20
            BRENDA, the Enzyme Database: 3.4.99.20
///
ENTRY       EC 3.4.99.21      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: solanain (EC 3.4.99.21 created 1972, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.21
            ExPASy - ENZYME nomenclature database: 3.4.99.21
            ExplorEnz - The Enzyme Database: 3.4.99.21
            ERGO genome analysis and discovery system: 3.4.99.21
            BRENDA, the Enzyme Database: 3.4.99.21
///
ENTRY       EC 3.4.99.22      Obsolete  Enzyme
NAME        Transferred to 3.4.24.29
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.24.29 aureolysin (EC 3.4.99.22 created
            1972, modified 1976, deleted 1978 [transferred to EC 3.4.24.4,
            deleted 1992])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.22
            ExPASy - ENZYME nomenclature database: 3.4.99.22
            ExplorEnz - The Enzyme Database: 3.4.99.22
            ERGO genome analysis and discovery system: 3.4.99.22
            BRENDA, the Enzyme Database: 3.4.99.22
///
ENTRY       EC 3.4.99.23      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: tabernamontanain (EC 3.4.99.23 created 1972, deleted
            1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.23
            ExPASy - ENZYME nomenclature database: 3.4.99.23
            ExplorEnz - The Enzyme Database: 3.4.99.23
            ERGO genome analysis and discovery system: 3.4.99.23
            BRENDA, the Enzyme Database: 3.4.99.23
///
ENTRY       EC 3.4.99.24      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: Tenebrio alpha-proteinase (EC 3.4.99.24 created 1972,
            deleted 1978 [transferred to EC 3.4.21.18, deleted 1992])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.24
            ExPASy - ENZYME nomenclature database: 3.4.99.24
            ExplorEnz - The Enzyme Database: 3.4.99.24
            ERGO genome analysis and discovery system: 3.4.99.24
            BRENDA, the Enzyme Database: 3.4.99.24
///
ENTRY       EC 3.4.99.25      Obsolete  Enzyme
NAME        Transferred to 3.4.23.21
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.23.21 rhizopuspepsin (EC 3.4.99.25
            created 1972, deleted 1978 [transferred to EC 3.4.23.6, deleted
            1992])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.25
            ExPASy - ENZYME nomenclature database: 3.4.99.25
            ExplorEnz - The Enzyme Database: 3.4.99.25
            ERGO genome analysis and discovery system: 3.4.99.25
            BRENDA, the Enzyme Database: 3.4.99.25
///
ENTRY       EC 3.4.99.26      Obsolete  Enzyme
NAME        Transferred to 3.4.21.68
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.21.68 t-plasminogen activator (EC
            3.4.99.26 created 1972, deleted 1978 [transferred to EC 3.4.21.31,
            deleted 1992])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.26
            ExPASy - ENZYME nomenclature database: 3.4.99.26
            ExplorEnz - The Enzyme Database: 3.4.99.26
            ERGO genome analysis and discovery system: 3.4.99.26
            BRENDA, the Enzyme Database: 3.4.99.26
///
ENTRY       EC 3.4.99.27      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: Echis carinatus prothrombin-activating proteinase (EC
            3.4.99.27 created 1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.27
            ExPASy - ENZYME nomenclature database: 3.4.99.27
            ExplorEnz - The Enzyme Database: 3.4.99.27
            ERGO genome analysis and discovery system: 3.4.99.27
            BRENDA, the Enzyme Database: 3.4.99.27
///
ENTRY       EC 3.4.99.28      Obsolete  Enzyme
NAME        Transferred to 3.4.21.60
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.21.60 scutelarin (EC 3.4.99.28 created
            1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.28
            ExPASy - ENZYME nomenclature database: 3.4.99.28
            ExplorEnz - The Enzyme Database: 3.4.99.28
            ERGO genome analysis and discovery system: 3.4.99.28
            BRENDA, the Enzyme Database: 3.4.99.28
///
ENTRY       EC 3.4.99.29      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: myxobacter AL-1 proteinase I (EC 3.4.99.29 created
            1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.29
            ExPASy - ENZYME nomenclature database: 3.4.99.29
            ExplorEnz - The Enzyme Database: 3.4.99.29
            ERGO genome analysis and discovery system: 3.4.99.29
            BRENDA, the Enzyme Database: 3.4.99.29
///
ENTRY       EC 3.4.99.30      Obsolete  Enzyme
NAME        Transferred to 3.4.24.20
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.24.20 peptidyl-Lys
            metalloendopeptidase (EC 3.4.99.30 created 1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.30
            ExPASy - ENZYME nomenclature database: 3.4.99.30
            ExplorEnz - The Enzyme Database: 3.4.99.30
            ERGO genome analysis and discovery system: 3.4.99.30
            BRENDA, the Enzyme Database: 3.4.99.30
///
ENTRY       EC 3.4.99.31      Obsolete  Enzyme
NAME        Transferred to 3.4.24.15
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.24.15 thimet oligopeptidase (EC
            3.4.99.31 created 1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.31
            ExPASy - ENZYME nomenclature database: 3.4.99.31
            ExplorEnz - The Enzyme Database: 3.4.99.31
            ERGO genome analysis and discovery system: 3.4.99.31
            BRENDA, the Enzyme Database: 3.4.99.31
///
ENTRY       EC 3.4.99.32      Obsolete  Enzyme
NAME        Transferred to 3.4.24.20
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.24.20 peptidyl-Lys
            metalloendopeptidase (EC 3.4.99.32 created 1978, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.32
            ExPASy - ENZYME nomenclature database: 3.4.99.32
            ExplorEnz - The Enzyme Database: 3.4.99.32
            ERGO genome analysis and discovery system: 3.4.99.32
            BRENDA, the Enzyme Database: 3.4.99.32
///
ENTRY       EC 3.4.99.33      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: cathepsin R (EC 3.4.99.33 created 1981, deleted 1984
            [transferred to EC 3.4.21.52, deleted 1992])
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.33
            ExPASy - ENZYME nomenclature database: 3.4.99.33
            ExplorEnz - The Enzyme Database: 3.4.99.33
            ERGO genome analysis and discovery system: 3.4.99.33
            BRENDA, the Enzyme Database: 3.4.99.33
///
ENTRY       EC 3.4.99.34      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: mytilidase (EC 3.4.99.34 created 1981, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.34
            ExPASy - ENZYME nomenclature database: 3.4.99.34
            ExplorEnz - The Enzyme Database: 3.4.99.34
            ERGO genome analysis and discovery system: 3.4.99.34
            BRENDA, the Enzyme Database: 3.4.99.34
///
ENTRY       EC 3.4.99.35      Obsolete  Enzyme
NAME        Transferred to 3.4.23.36
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.23.36 signal peptidase II (EC
            3.4.99.35 created 1984, deleted 1995)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.35
            ExPASy - ENZYME nomenclature database: 3.4.99.35
            ExplorEnz - The Enzyme Database: 3.4.99.35
            ERGO genome analysis and discovery system: 3.4.99.35
            BRENDA, the Enzyme Database: 3.4.99.35
///
ENTRY       EC 3.4.99.36      Obsolete  Enzyme
NAME        Transferred to 3.4.21.89
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.21.89 signal peptidase I (EC 3.4.99.36
            created 1984, deleted 1995)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.36
            ExPASy - ENZYME nomenclature database: 3.4.99.36
            ExplorEnz - The Enzyme Database: 3.4.99.36
            ERGO genome analysis and discovery system: 3.4.99.36
            BRENDA, the Enzyme Database: 3.4.99.36
///
ENTRY       EC 3.4.99.37      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: RecA peptidase (EC 3.4.99.37 created 1989, deleted
            1992)
STRUCTURES  PDB: 1G18  1G19  1MO3  1MO4  1MO5  1MO6  1REA  2ODN  2ODW  2OE2  
                 2OEP  2OES  2OFO  2REB  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.37
            ExPASy - ENZYME nomenclature database: 3.4.99.37
            ExplorEnz - The Enzyme Database: 3.4.99.37
            ERGO genome analysis and discovery system: 3.4.99.37
            BRENDA, the Enzyme Database: 3.4.99.37
///
ENTRY       EC 3.4.99.38      Obsolete  Enzyme
NAME        Transferred to 3.4.23.17
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.23.17 pro-opiomelanocortin converting
            enzyme (EC 3.4.99.38 created 1989, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.38
            ExPASy - ENZYME nomenclature database: 3.4.99.38
            ExplorEnz - The Enzyme Database: 3.4.99.38
            ERGO genome analysis and discovery system: 3.4.99.38
            BRENDA, the Enzyme Database: 3.4.99.38
///
ENTRY       EC 3.4.99.39      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: pseudomurein endopeptidase (EC 3.4.99.39 created
            1989, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.39
            ExPASy - ENZYME nomenclature database: 3.4.99.39
            ExplorEnz - The Enzyme Database: 3.4.99.39
            ERGO genome analysis and discovery system: 3.4.99.39
            BRENDA, the Enzyme Database: 3.4.99.39
///
ENTRY       EC 3.4.99.40      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: Pro-gonadoliberin proteinase (EC 3.4.99.40 created
            1989, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.40
            ExPASy - ENZYME nomenclature database: 3.4.99.40
            ExplorEnz - The Enzyme Database: 3.4.99.40
            ERGO genome analysis and discovery system: 3.4.99.40
            BRENDA, the Enzyme Database: 3.4.99.40
///
ENTRY       EC 3.4.99.41      Obsolete  Enzyme
NAME        Transferred to 3.4.24.64
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.24.64 mitochondrial processing
            peptidase (EC 3.4.99.41 created 1989/90, deleted 1995)
GENES       TBR: Tb11.02.1480
            TCR: 509229.80
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.41
            ExPASy - ENZYME nomenclature database: 3.4.99.41
            ExplorEnz - The Enzyme Database: 3.4.99.41
            ERGO genome analysis and discovery system: 3.4.99.41
            BRENDA, the Enzyme Database: 3.4.99.41
///
ENTRY       EC 3.4.99.42      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Deleted entry: leucyllysine endopeptidase (EC 3.4.99.42 created
            1990, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.42
            ExPASy - ENZYME nomenclature database: 3.4.99.42
            ExplorEnz - The Enzyme Database: 3.4.99.42
            ERGO genome analysis and discovery system: 3.4.99.42
            BRENDA, the Enzyme Database: 3.4.99.42
///
ENTRY       EC 3.4.99.43      Obsolete  Enzyme
NAME        Transferred to 3.4.23.42
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.23.42 thermopsin (EC 3.4.99.43 created
            1992, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.43
            ExPASy - ENZYME nomenclature database: 3.4.99.43
            ExplorEnz - The Enzyme Database: 3.4.99.43
            ERGO genome analysis and discovery system: 3.4.99.43
            BRENDA, the Enzyme Database: 3.4.99.43
///
ENTRY       EC 3.4.99.44      Obsolete  Enzyme
NAME        Transferred to 3.4.24.55
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.24.55 pitrilysin (EC 3.4.99.44 created
            1992, deleted 1993)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.44
            ExPASy - ENZYME nomenclature database: 3.4.99.44
            ExplorEnz - The Enzyme Database: 3.4.99.44
            ERGO genome analysis and discovery system: 3.4.99.44
            BRENDA, the Enzyme Database: 3.4.99.44
///
ENTRY       EC 3.4.99.45      Obsolete  Enzyme
NAME        Transferred to 3.4.24.56
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.24.56 insulysin (EC 3.4.99.45 created
            1992, deleted 1993)
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.45
            ExPASy - ENZYME nomenclature database: 3.4.99.45
            ExplorEnz - The Enzyme Database: 3.4.99.45
            ERGO genome analysis and discovery system: 3.4.99.45
            BRENDA, the Enzyme Database: 3.4.99.45
///
ENTRY       EC 3.4.99.46      Obsolete  Enzyme
NAME        Transferred to 3.4.25.1
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases);
            Endopeptidases of unknown catalytic mechanism (sub-subclass is
            currently empty)
COMMENT     Transferred entry: now EC 3.4.25.1 proteasome endopeptidase complex
            (EC 3.4.99.46 created 1992, deleted 2000)
STRUCTURES  PDB: 1FNT  1G0U  1G65  1JD2  1PMA  1RYP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.4.99.46
            ExPASy - ENZYME nomenclature database: 3.4.99.46
            ExplorEnz - The Enzyme Database: 3.4.99.46
            ERGO genome analysis and discovery system: 3.4.99.46
            BRENDA, the Enzyme Database: 3.4.99.46
///
ENTRY       EC 3.4.-.-                  Enzyme
CLASS       Hydrolases;
            Acting on peptide bonds (peptidases)
REACTION    (1) N6,N6,N6-Trimethyl-L-lysine + Protein <=> Protein
            N6,N6,N6-trimethyl-L-lysine + H2O [RN:R04313];
            (2) N6-D-Biotinyl-L-lysine + Peptide <=> Holo-[carboxylase]
            [RN:R04869]
SUBSTRATE   N6,N6,N6-Trimethyl-L-lysine [CPD:C03793];
            Protein [CPD:C00017];
            N6-D-Biotinyl-L-lysine [CPD:C05552];
            Peptide [CPD:C00012]
PRODUCT     Protein N6,N6,N6-trimethyl-L-lysine [CPD:C05546];
            H2O [CPD:C00001];
            Holo-[carboxylase] [CPD:C06250]
///
ENTRY       EC 3.5.1.1                  Enzyme
NAME        asparaginase;
            asparaginase II;
            L-asparaginase;
            colaspase;
            elspar;
            leunase;
            crasnitin;
            alpha-asparaginase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     L-asparagine amidohydrolase
REACTION    L-asparagine + H2O = L-aspartate + NH3 [RN:R00485]
ALL_REAC    R00485;
            (other) R06134
SUBSTRATE   L-asparagine [CPD:C00152];
            H2O [CPD:C00001]
PRODUCT     L-aspartate [CPD:C00049];
            NH3 [CPD:C00014]
REFERENCE   1  [PMID:13426090]
  AUTHORS   HALPERN YS, GROSSOWICZ N.
  TITLE     Hydrolysis of amides by extracts from Mycobacteria.
  JOURNAL   Biochem. J. 65 (1957) 716-20.
  ORGANISM  Brucella abortus [GN:bmb], Mycobacterium phlei
REFERENCE   2
  AUTHORS   Ho, P.P.K., Frank, B.H. and Burck, P.J.
  TITLE     Crystalline L-asparaginase from Escherichia coli B.
  JOURNAL   Science 165 (1969) 510-512.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4987975]
  AUTHORS   Suld HM, Herbut PA.
  TITLE     Guinea pig serum and liver L-asparaginases. Comparison of serum and
            papain-digested liver L-asparaginases.
  JOURNAL   J. Biol. Chem. 245 (1970) 2797-801.
  ORGANISM  guinea pig
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
            PATH: map00460  Cyanoamino acid metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K01424  L-asparaginase
GENES       RNO: 246266(LOC246266)
            XLA: 444536(MGC82104)
            DME: Dmel_CG5473(SP2637) Dmel_CG7860
            ATH: AT5G08100
            OSA: 4333381
            CME: CMI015C
            SCE: YDR321W(ASP1) YLR155C(ASP3-1) YLR157C(ASP3-2) YLR158C(ASP3-3)
                 YLR160C(ASP3-4)
            AGO: AGOS_AGR357W
            PIC: PICST_30946(ASG1) PICST_39982
            CGR: CAGL0H07051g
            SPO: SPAC186.03 SPAC977.12 SPBPB8B6.05c
            ANI: AN0300.2 AN1891.2
            AFM: AFUA_1G02780 AFUA_2G04280 AFUA_3G11890 AFUA_5G02930
            AOR: AO090003000216 AO090005000816
            UMA: UM01007.1 UM04707.1
            DDI: DDB_0201640(aspA) DDB_0230992
            TCR: 504147.110 510823.80
            LMA: LmjF15.0390 LmjF36.4430
            EHI: 10.t00031 15.t00029 15.t00034 342.t00003
            ECO: b0828(ybiK) b1767(ansA) b2957(ansB)
            ECJ: JW0812(iaaA) JW1756(ansA) JW2924(ansB)
            ECE: Z1051m Z2801(ansA) Z4302(ansB)
            ECS: ECs2474 ECs3833
            ECC: c0913(ybiK) c2171(ansA) c3543(ansB)
            ECI: UTI89_C0831(ybiK) UTI89_C1963(ansA) UTI89_C3346(ansB)
            ECP: ECP_0841 ECP_1715 ECP_2951
            ECV: APECO1_1265(iaaA) APECO1_3564(ansB) APECO1_836(ansA)
            ECW: EcE24377A_1991(ansA) EcE24377A_3301(ansB)
            ECX: EcHS_A1851 EcHS_A3117
            STY: STY0886(ybiK) STY1820(ansA) STY3259(ansB)
            STT: t1173(ansA) t2042(ybiK) t3018(ansB)
            SPT: SPA1550(ansA) SPA1908(ybiK) SPA2969(ansB)
            SEC: SC0842(ybiK) SC1316(ansA) SC3046(ansB) SC3532(aspG)
            STM: STM0847(ybiK) STM1294(ansA) STM3106(ansB) STM3598
            YPE: YPO1386(ansB) YPO2161(ansA)
            YPK: y2161(ansA) y2787(ansB)
            YPM: YP_1207(ansB) YP_1961(ansA)
            YPA: YPA_0677 YPA_1518
            YPN: YPN_1627 YPN_2591
            YPP: YPDSF_0973 YPDSF_2309
            YPS: YPTB1411(ansB) YPTB2087(ansA)
            YPI: YpsIP31758_1983(ansA) YpsIP31758_2586(ansB)
            SFL: SF0778(ybiK) SF1456(ansA) SF2954(ansB)
            SFX: S0821(ybiK) S1571(ansA) S3157(ansB)
            SFV: SFV_0811(ybiK) SFV_1450(ansA) SFV_3015(ansB)
            SSN: SSON_0810(ybiK) SSON_1388(ansA) SSON_3239(ansB)
            SBO: SBO_0718(ybiK) SBO_1320(ansA) SBO_3033(ansB)
            SDY: SDY_0759(ybiK) SDY_1506(ansA) SDY_3115(ansB)
            ECA: ECA0132 ECA1102(ansB1) ECA2340(ansA) ECA4126(ansB2)
            PLU: plu1616(ansB) plu2554(ansA)
            ENT: Ent638_1322
            KPN: KPN_01203(ansA)
            SPE: Spro_2851
            HIN: HI0745(ansB)
            HIP: CGSHiEE_08385(ansB)
            HIQ: CGSHiGG_07215(ansB)
            HDU: HD0372(ansB)
            MSU: MS2050(ansB)
            APL: APL_0135(ansB) APL_0660(ansB)
            XFA: XF1093
            XFT: PD0391
            XCC: XCC0229(ansA) XCC0856(aspG)
            XCB: XC_0239 XC_3374
            XCV: XCV0254 XCV0963
            XAC: XAC0248(ansA) XAC0932(aspG)
            XOO: XOO3619(aspG)
            XOM: XOO_3421(XOO3421)
            VCH: VC1995 VC2603
            VCO: VC0395_A1580(ansA)
            VVU: VV1_1328 VV1_3135
            VVY: VV1151 VV3040
            VPA: VP2153 VP2781 VPA0374
            VFI: VF1527 VF1644(ansA)
            PPR: PBPRA2596 PBPRB1174
            PAE: PA2253(ansA)
            PAU: PA14_35440(ansA)
            PPU: PP_0495(ansB) PP_1160
            PPF: Pput_0529
            PST: PSPTO_5501(ansA)
            PSB: Psyr_5053
            PSP: PSPPH_5135(ansA)
            PFL: PFL_6140(ansA)
            PFO: Pfl_1917 Pfl_5627
            PEN: PSEEN0570
            PMY: Pmen_0136
            PAR: Psyc_1407(ansA)
            PCR: Pcryo_1567
            ACI: ACIAD0476
            SON: SO_2115 SO_2421(ansA)
            SDN: Sden_1902
            SFR: Sfri_0683 Sfri_1445 Sfri_2146
            SAZ: Sama_0299 Sama_1617 Sama_1722
            SBL: Sbal_1904 Sbal_2054 Sbal_3745
            SBM: Shew185_0619
            SLO: Shew_1940 Shew_2171
            SPC: Sputcn32_1898
            SPL: Spea_2435
            SHE: Shewmr4_1837 Shewmr4_1908
            SHM: Shewmr7_2070 Shewmr7_2140
            SHN: Shewana3_1895 Shewana3_1963
            SHW: Sputw3181_1933 Sputw3181_2110
            ILO: IL1330(ansA) IL1368
            CPS: CPS_2584(ansA) CPS_4722
            PHA: PSHAa1143(iaaA) PSHAa1408(ansA)
            PAT: Patl_0125 Patl_1544
            PIN: Ping_3394
            LPN: lpg2873
            LPF: lpl2786(asg)
            LPP: lpp2932(asg)
            FTU: FTT0464(ansB) FTT0591(ansA) FTT0803(ans)
            FTF: FTF0464(ansB) FTF0591(ansA) FTF0803(ans)
            FTW: FTW_0600 FTW_1138(ansA) FTW_1606(ansB)
            FTL: FTL_0855 FTL_1418 FTL_1600
            FTH: FTH_0844(ansA) FTH_1381(ans) FTH_1511(aspG) FTH_1546(ansB)
            FTN: FTN_0555(ansB) FTN_1088(ansA) FTN_1208(ans)
            TCX: Tcr_1235
            HCH: HCH_06648 HCH_06718
            CSA: Csal_2037
            MMW: Mmwyl1_2653 Mmwyl1_4133
            AHA: AHA_3365 AHA_3828
            VOK: COSY_0226
            NME: NMB1688
            NMA: NMA1947(ans)
            NMC: NMC1606(ans)
            NGO: NGO1339
            CVI: CV_1687(ansA) CV_4047
            RSO: RSc1306(ansB) RSc1378(RS04661)
            REU: Reut_A1928 Reut_A2007
            REH: H16_A2102(ansB)
            RME: Rmet_1406 Rmet_1980
            BMA: BMA1413 BMAA0973
            BXE: Bxe_A0834 Bxe_A2464
            BVI: Bcep1808_1806
            BUR: Bcep18194_A5182 Bcep18194_B1869
            BCN: Bcen_4205 Bcen_6197
            BCH: Bcen2424_1882 Bcen2424_4161
            BAM: Bamb_1819 Bamb_3569
            BPS: BPSL1448(ansB) BPSS1308 BPSS2060(ansA)
            BPM: BURPS1710b_2428(ansB) BURPS1710b_A0326(ansA)
            BPL: BURPS1106A_2305 BURPS1106A_A1771
            BPD: BURPS668_2265 BURPS668_A1856
            BTE: BTH_II1111
            BPE: BP2398
            BPA: BPP0006(ansB) BPP3263
            BBR: BB0006(ansB) BB3714
            RFR: Rfer_2993 Rfer_3101
            POL: Bpro_0141 Bpro_2953
            PNA: Pnap_1919
            AAV: Aave_1656
            AJS: Ajs_2309
            VEI: Veis_4589 Veis_4896
            MPT: Mpe_A1865
            HAR: HEAR1103 HEAR3462(ansB)
            MMS: mma_1624 mma_3667 mma_3688
            NMU: Nmul_A2166
            EBA: ebA3606
            AZO: azo0436 azo0438(ansB2)
            TBD: Tbd_1931
            HPY: HP0723(ansB)
            HPJ: jhp0661(ansB)
            HPA: HPAG1_0708
            HHE: HH0662(ansB)
            HAC: Hac_0948(ansB)
            WSU: WS0660(ansB)
            TDN: Tmden_0575
            CJE: Cj0029(ansA)
            CJR: CJE0029(ansA)
            CJJ: CJJ81176_0056(ansA)
            CJU: C8J_0028(ansA)
            CJD: JJD26997_0031(ansA)
            CFF: CFF8240_1025(ansB)
            CCO: CCC13826_0029
            ABU: Abu_1580
            NIS: NIS_1453
            SUN: SUN_0716 SUN_0879(ansB)
            DVU: DVU2242
            DVL: Dvul_1000
            DDE: Dde_2284
            BBA: Bd3633(aspG)
            DPS: DP0994
            ADE: Adeh_2366
            AFW: Anae109_1503
            MXA: MXAN_5198(ansA)
            ATU: Atu3044(asg) Atu3791(ansA)
            ATC: AGR_L_2084 AGR_L_3520
            RLE: RL1280(ansA)
            BME: BMEI0105 BMEI0107
            BMF: BAB1_1961 BAB1_1963
            BMS: BR1960 BR1962
            BMB: BruAb1_1936
            BJA: bll4950
            BHE: BH02060(ansA)
            BQU: BQ01940(ansA)
            CCR: CC_0097 CC_0576
            SIT: TM1040_3607
            RSP: RSP_3949(ansB)
            MMR: Mmar10_0025
            HNE: HNE_1675 HNE_3324
            ZMO: ZMO1683(ansA)
            SAL: Sala_2824
            ELI: ELI_02050
            GBE: GbCGDNIH1_0414
            RRU: Rru_A3730
            ABA: Acid345_0550
            BSU: BG10300(ansA) BG12755(yccC)
            BHA: BH1624
            BAN: BA1516(ansA-1) BA3137(ansA-2)
            BAR: GBAA1516(ansA-1) GBAA3137(ansA-2)
            BAA: BA_2038 BA_3638
            BAT: BAS1406 BAS2916
            BCE: BC1496 BC3094
            BCA: BCE_1622(ansA)
            BCZ: BCZK1377(ansA) BCZK2846(aspG)
            BTK: BT9727_1378(ansA) BT9727_2884(aspG)
            BLI: BL02224(ansZA) BL05377(ansA)
            BLD: BLi02433 BLi02777(yccC1) BLi02778(yccC2) BLi04140(ansA)
            BCL: ABC1864(ansZ)
            BAY: RBAM_003000(yccC) RBAM_021710
            BPU: BPUM_0470(yccC) BPUM_3548
            OIH: OB1808
            GKA: GK2233
            SAU: SA1310(ansA)
            SAV: SAV1479(ansA)
            SAM: MW1367(ansA)
            SAR: SAR1487
            SAS: SAS1419
            SAC: SACOL1519(ansA)
            SAB: SAB1341
            SAA: SAUSA300_1368(ansA)
            SAO: SAOUHSC_01497
            SEP: SE1167
            SER: SERP1046(ansA)
            SHA: SH1433(ansA)
            SSP: SSP1268
            LMO: lmo1940
            LMF: LMOf2365_1969(ansA)
            LIN: lin2054
            LWE: lwe1966(ansA)
            LLA: L142722(ansB)
            LLC: LACR_0779
            LLM: llmg_1823(ansB)
            SPY: SPy_1782(asnB)
            SPZ: M5005_Spy_1516(asnB)
            SPM: spyM18_1853
            SPG: SpyM3_1548(asnB)
            SPS: SPs0318
            SPH: MGAS10270_Spy1584(asnB)
            SPI: MGAS10750_Spy1576(asnB)
            SPJ: MGAS2096_Spy1543(asnB)
            SPK: MGAS9429_Spy1517(asnB)
            SPF: SpyM50329(asnB)
            SPA: M6_Spy1509
            SPB: M28_Spy1505(asnB)
            SPN: SP_1998
            SPR: spr1812(ansB)
            SAG: SAG1679
            SAN: gbs1723
            SAK: SAK_1691
            SMU: SMU.1831(aspG)
            STC: str1724(ansB)
            STL: stu1724(ansB)
            SSA: SSA_0551(ansB)
            SGO: SGO_0425(ansB)
            LPL: lp_2738
            LJO: LJ1401
            LAC: LBA1687(ansA)
            LSA: LSA0347(asnA1) LSA1693(asnA2)
            LSL: LSL_1219(ansB)
            LDB: Ldb0315(ansA)
            LBU: LBUL_0273
            LBR: LVIS_1836
            LCA: LSEI_2253
            EFA: EF1163
            OOE: OEOE_1807
            CAC: CAC1714(ansA)
            CPE: CPE1752(ansA)
            CPF: CPF_2005
            CPR: CPR_1723
            CTC: CTC01877
            CBA: CLB_2390(ansA)
            CBH: CLC_2372(ansA)
            CBF: CLI_2578(ansA)
            CBE: Cbei_2395
            DSY: DSY1908
            TTE: TTE0966(ansB)
            MTU: Rv1538c(ansA)
            MTC: MT1590(ansA)
            MBO: Mb1565c(ansA)
            MBB: BCG_1590c(ansA)
            MLE: ML1198(ansA)
            MPA: MAP1249c(ansA)
            MAV: MAV_3233
            MSM: MSMEG_3173
            CGL: NCgl2062(cgl2143)
            CGB: cg2352(ansA)
            CEF: CE2039 CE2357
            CDI: DIP1587
            CJK: jk0762(ansA)
            RHA: RHA1_ro03209(ansA) RHA1_ro04451
            CMI: CMM_1146
            AAU: AAur_3793
            PAC: PPA0367 PPA2114
            SEN: SACE_3615(ansB)
            BLO: BL1142
            BAD: BAD_0059 BAD_1173
            RXY: Rxyl_2741 Rxyl_2849
            FNU: FN0751
            RBA: RB7985(ansA)
            SYN: sll0422
            SYW: SYNW2317(yccC)
            SYD: Syncc9605_2449
            SYE: Syncc9902_2132
            SYG: sync_1200 sync_2665(ansB)
            SYR: SynRCC307_0984
            SYX: SynWH7803_1425 SynWH7803_2334(yccC)
            CYA: CYA_0931
            CYB: CYB_1038 CYB_2005
            TEL: tlr0704
            GVI: glr0035
            ANA: all3922
            AVA: Ava_1775
            TER: Tery_0258
            BTH: BT_0526 BT_2404 BT_2757
            BFR: BF0607 BF2658 BF4215
            BFS: BF0556 BF2680(ansA) BF4039(ansB)
            PGI: PG2121(ansA)
            SRU: SRU_1709(ansA) SRU_2761(asg)
            GFO: GFO_0086(ansA) GFO_0747(ybiK) GFO_3399
            FPS: FP1109 FP2291(ansA)
            RRS: RoseRS_0104 RoseRS_0748
            RCA: Rcas_0343 Rcas_4430
            DRA: DR_2353
            DGE: Dgeo_0094
            MSI: Msm_0334
            HAL: VNG1872C
            HMA: rrnAC3420(ans)
            HWA: HQ3036A(asnA)
            NPH: NP2432A
            TAC: Ta0338
            TVO: TVN0432
            PTO: PTO0425
            PHO: PH0232
            PAB: PAB0145(asnA-2) PAB2294
            PFU: PF0142 PF2047
            TKO: TK1656 TK2246
            RCI: RCIX272(ansB)
            APE: APE_2200
            SSO: SSO2350(ansA-like)
            STO: ST1827
            SAI: Saci_0402
            PAI: PAE3083
            PCL: Pcal_0144 Pcal_0970
STRUCTURES  PDB: 1AGX  1HFJ  1HFK  1HFW  1HG0  1HG1  1HO3  1IHD  1JAZ  1JJA  
                 1JN9  1JSL  1JSR  1K2X  1NNS  1O7J  1T3M  1WLS  1WNF  1WSA  
                 1ZCF  2GEZ  2GVN  2HIM  2HLN  2P2D  2P2N  3ECA  3PGA  4ECA  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.1
            ExPASy - ENZYME nomenclature database: 3.5.1.1
            ExplorEnz - The Enzyme Database: 3.5.1.1
            ERGO genome analysis and discovery system: 3.5.1.1
            BRENDA, the Enzyme Database: 3.5.1.1
            CAS: 9015-68-3
///
ENTRY       EC 3.5.1.2                  Enzyme
NAME        glutaminase;
            glutaminase I;
            L-glutaminase;
            glutamine aminohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     L-glutamine amidohydrolase
REACTION    L-glutamine + H2O = L-glutamate + NH3 [RN:R00256]
ALL_REAC    R00256;
            (other) R01579 R06134
SUBSTRATE   L-glutamine [CPD:C00064];
            H2O [CPD:C00001]
PRODUCT     L-glutamate [CPD:C00025];
            NH3 [CPD:C00014]
REFERENCE   1  [PMID:5800436]
  AUTHORS   Kung HF, Wagner C.
  TITLE     Gamma-glutamylmethylamide. A new intermediate in the metabolism of
            methylamine.
  JOURNAL   J. Biol. Chem. 244 (1969) 4136-40.
  ORGANISM  Pseudomonas sp.
REFERENCE   2
  AUTHORS   Roberts, E.
  TITLE     Glutaminase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 285-300.
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00471  D-Glutamine and D-glutamate metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K01425  glutaminase
GENES       HSA: 27165(GLS2) 2744(GLS)
            PTR: 451998(GLS2) 470606(GLS)
            MMU: 14660(Gls) 216456(Gls2)
            RNO: 192268(Gls2) 24398(Gls)
            CFA: 488448(GLS)
            GGA: 424043(RCJMB04_23e15)
            SPU: 575775(LOC575775) 758743(LOC758743)
            DME: Dmel_CG8772(nemy)
            CEL: DH11.1(glutaminase) F30F8.2(glutaminase)
            AOR: AO090010000571
            ECO: b0485(ybaS) b1524(yneH)
            ECJ: JW0474(ybaS) JW1517(yneH)
            ECE: Z0606(ybaS) Z2179(yneH)
            ECS: ECs0538 ECs2131
            ECC: c0605(ybaS) c1947(yneH)
            ECI: UTI89_C0516(ybaS) UTI89_C1743(yneH)
            ECP: ECP_0550 ECP_1508
            ECV: APECO1_1527(ybaS) APECO1_644(yneH)
            ECW: EcE24377A_0524(glsA1) EcE24377A_1724(glsA2)
            ECX: EcHS_A0564(glsA1) EcHS_A1606(glsA2)
            STT: t1446
            SPT: SPA1330(yneH)
            SEC: SC1542(yneH)
            STM: STM1525(yneH)
            YPE: YPO0949 YPO1939
            YPK: y2372 y3336
            YPM: YP_1682(glsA1) YP_3492(glsA2)
            YPA: YPA_0315 YPA_1322
            YPN: YPN_3147
            YPP: YPDSF_0565 YPDSF_1184
            YPS: YPTB1937 YPTB3221
            SFL: SF0430(ybaS) SF1569(yneH)
            SFX: S0437(ybaS) S1696(yneH)
            SFV: SFV_0458(ybaS) SFV_1583(yneH)
            SSN: SSON_0474(ybaS) SSON_1604(yneH)
            SBO: SBO_0387(ybaS)
            SDY: SDY_1631(yneH)
            PLU: plu1172
            ENT: Ent638_2007
            SPE: Spro_4040
            VCH: VC0454
            VVU: VV1_1517
            VVY: VV2882
            VPA: VP2623
            VFI: VF0423
            PPR: PBPRA3151
            PAE: PA1638
            PAU: PA14_43320(glsA)
            PPF: Pput_3197
            PST: PSPTO_2488
            PSB: Psyr_2292
            PSP: PSPPH_2883
            PFL: PFL_3159(glsA)
            PFO: Pfl_3373
            PEN: PSEEN3312
            PMY: Pmen_0139
            PCR: Pcryo_1330
            ACI: ACIAD1040
            SON: SO_3365(glsA)
            SDN: Sden_2695
            SFR: Sfri_2870
            SAZ: Sama_2487
            SBL: Sbal_3036
            SBM: Shew185_3050
            SLO: Shew_1126
            SPC: Sputcn32_2697
            SSE: Ssed_1222
            SPL: Spea_1111
            SHE: Shewmr4_1183
            SHM: Shewmr7_1254
            SHN: Shewana3_1184
            SHW: Sputw3181_1314
            ILO: IL0352
            CPS: CPS_4729(glsA)
            PHA: PSHAa2335
            PAT: Patl_2048
            SDE: Sde_2867
            LPN: lpg0241
            LPF: lpl0295
            LPP: lpp0311
            FTU: FTT0195c
            FTF: FTF0195c
            FTL: FTL_1900
            FTH: FTH_1822(glsA)
            FTA: FTA_2007
            FTN: FTN_0171(glsA)
            HCH: HCH_06987
            MMW: Mmwyl1_3795
            AHA: AHA_3480
            CVI: CV_4158
            RSO: RSp1143(glsA)
            RME: Rmet_3760
            BMA: BMAA0814(glsA)
            BML: BMA10299_0029(glsA)
            BMN: BMA10247_A1594(glsA)
            BXE: Bxe_B1127
            BVI: Bcep1808_3320
            BUR: Bcep18194_B0751
            BCN: Bcen_3428
            BCH: Bcen2424_4940
            BAM: Bamb_4370
            BPS: BPSS0628(glsA)
            BPM: BURPS1710b_A2189(glsA)
            BPL: BURPS1106A_A0842
            BPD: BURPS668_A0934
            BTE: BTH_II1788
            POL: Bpro_4370
            ABU: Abu_2331(glsA)
            SUN: SUN_0901
            MLO: mlr0211
            SME: SMc00486(glsA)
            SMD: Smed_1513
            ATU: Atu1859(glsA)
            ATC: AGR_C_3412
            RET: RHE_CH02311(glsA)
            RLE: RL2623(glsA)
            BME: BMEII0907 BMEII0908
            BMF: BAB2_0863
            BMS: BRA0340
            BMB: BruAb2_0841
            BJA: bll3935 bll4798
            BRA: BRADO3130
            BBT: BBta_3570
            RPA: RPA4211(glsA)
            RPB: RPB_1403
            RPC: RPC_1541
            RPD: RPD_1383
            XAU: Xaut_1163 Xaut_1550
            CCR: CC_0276
            RDE: RD1_2684(glsA)
            MMR: Mmar10_2917
            SWI: Swit_2796
            GOX: GOX2066
            SUS: Acid_0446 Acid_5408
            BSU: BG12753(ybgJ) BG13350(ylaM)
            BHA: BH2627 BH2717
            BAN: BA0499(glsA-1) BA3155(glsA-2)
            BAR: GBAA0499(glsA-1) GBAA3155(glsA-2)
            BAA: BA_1070 BA_3658
            BAT: BAS0471 BAS2932
            BCE: BC0481 BC3115
            BCA: BCE_0553(glsA)
            BCZ: BCZK0410(glsA) BCZK2857
            BCY: Bcer98_0426
            BTK: BT9727_0414(glsA) BT9727_2907
            BTL: BALH_0436(glsA)
            BLI: BL01786 BL02973
            BLD: BLi00274(ybgJ) BLi01700(ylaM)
            BCL: ABC0329
            BAY: RBAM_002800(ybgJ) RBAM_014690(ylaM)
            BPU: BPUM_0244(glsA1) BPUM_1374(gls)
            OIH: OB0870
            GKA: GK2125
            GTN: GTNG_2024
            LJO: LJ0713
            LGA: LGAS_0507
            LRE: Lreu_0246 Lreu_1254
            CPE: CPE0591 CPE1995
            CPF: CPF_0571 CPF_2251
            CPR: CPR_0557 CPR_1963
            CTC: CTC00566
            CDF: CD0558(glsA)
            CBO: CBO2808(glsA)
            CBA: CLB_2751
            CBH: CLC_2684
            CBF: CLI_2858
            AMT: Amet_3642
            MSM: MSMEG_3818
            MGI: Mflv_2331
            CGL: NCgl2395(cgl2482)
            CGB: cg2728(glsK)
            CEF: CE2375
            RHA: RHA1_ro06842
            SCO: SCO7049(SC4G1.15)
            SMA: SAV1314(glsA)
            CMI: CMM_0029(glsA)
            ART: Arth_3548 Arth_3926
            SEN: SACE_1670(glsA)
            FNU: FN1397
            SYN: slr2079
            TEL: tlr0598
            ANA: all2934 all4774
            AVA: Ava_0966 Ava_2446
            TER: Tery_3991
            BTH: BT_2571
            BFR: BF0455
            BFS: BF0394(glsA)
            CHU: CHU_1741(yneH)
            GFO: GFO_2730(glsA)
STRUCTURES  PDB: 1MKI  1U60  2DFW  2OSU  2PBY  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.2
            ExPASy - ENZYME nomenclature database: 3.5.1.2
            ExplorEnz - The Enzyme Database: 3.5.1.2
            ERGO genome analysis and discovery system: 3.5.1.2
            BRENDA, the Enzyme Database: 3.5.1.2
            CAS: 9001-47-2
///
ENTRY       EC 3.5.1.3                  Enzyme
NAME        omega-amidase;
            alpha-keto acid-omega-amidase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     omega-amidodicarboxylate amidohydrolase
REACTION    a monoamide of a dicarboxylic acid + H2O = a dicarboxylate + NH3
            [RN:R03804]
ALL_REAC    R03804 > R00269 R00348;
            (other) R06134
SUBSTRATE   monoamide of a dicarboxylic acid [CPD:C04131];
            H2O [CPD:C00001]
PRODUCT     dicarboxylate [CPD:C02028];
            NH3 [CPD:C00014]
COMMENT     Acts on glutaramate, succinamate and their 2-oxo derivatives.
REFERENCE   1  [PMID:14392177]
  AUTHORS   MEISTER A, LEVINTOW L, GREENFIELD RE, ABENDSCHEIN PA.
  TITLE     Hydrolysis and transfer reactions catalyzed by omega-amidase
            preparations.
  JOURNAL   J. Biol. Chem. 215 (1955) 441-60.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Meister, A., Radhakrishnan, A.N. and Buckley, S.D.
  TITLE     Enzymatic synthesis of L-pipecolic acid and L-proline.
  JOURNAL   J. Biol. Chem. 229 (1957) 789-800.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00252  Alanine and aspartate metabolism
GENES       TBR: Tb09.211.0190
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.3
            ExPASy - ENZYME nomenclature database: 3.5.1.3
            ExplorEnz - The Enzyme Database: 3.5.1.3
            ERGO genome analysis and discovery system: 3.5.1.3
            BRENDA, the Enzyme Database: 3.5.1.3
            CAS: 9025-19-8
///
ENTRY       EC 3.5.1.4                  Enzyme
NAME        amidase;
            acylamidase;
            acylase;
            amidohydrolase;
            deaminase;
            fatty acylamidase;
            N-acetylaminohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     acylamide amidohydrolase
REACTION    a monocarboxylic acid amide + H2O = a monocarboxylate + NH3
            [RN:R03909]
ALL_REAC    R03909 > R00321 R02540 R03096 R03180 R05551 R05590;
            (other) R06134
SUBSTRATE   monocarboxylic acid amide [CPD:C03620];
            H2O [CPD:C00001]
PRODUCT     monocarboxylate [CPD:C00060];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Bray, H.G., James, S.P., Raffan, I.M., Ryman, B.E. and Thorpe, W.V.
  TITLE     The fate of certain organic acids and amides in the rabbit. 7. An
            amidase of rabbit liver.
  JOURNAL   Biochem. J. 44 (1949) 618-625.
  ORGANISM  rabbit
REFERENCE   2
  AUTHORS   Bray, H.G., James, S.P., Thorpe, W.V. and Wasdell, M.R.
  TITLE     The fate of certain organic acids and amides in the rabbit. 11.
            Further observations on the hydrolysis of amides by tissue extracts.
  JOURNAL   Biochem. J. 47 (1950) 294-299.
  ORGANISM  rabbit
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00360  Phenylalanine metabolism
            PATH: map00380  Tryptophan metabolism
            PATH: map00460  Cyanoamino acid metabolism
            PATH: map00632  Benzoate degradation via CoA ligation
            PATH: map00643  Styrene degradation
ORTHOLOGY   KO: K01426  amidase
GENES       DME: Dmel_CG14704(PGRP-LB)
            SCE: YDR242W(AMD2)
            PIC: PICST_43525(AMI1) PICST_47832(AMD2) PICST_48268(AMD4)
                 PICST_87495(GTA2)
            SPO: SPBPB8B6.03
            ANI: AN8777.2
            AFM: AFUA_1G14880 AFUA_5G00470 AFUA_5G09140
            TET: TTHERM_00313830 TTHERM_00354920 TTHERM_00361370
                 TTHERM_00361380 TTHERM_00361390 TTHERM_00361400
                 TTHERM_00361450 TTHERM_00361480 TTHERM_00896080
                 TTHERM_01161020
            ECC: c2457
            ECI: UTI89_C2212
            ECP: ECP_1969
            PLU: plu3213
            SPE: Spro_4710
            PAE: PA0202 PA0704 PA3366(amiE) PA4342
            PAU: PA14_20560(amiE) PA14_55200 PA14_56450
            PPF: Pput_0653 Pput_0971 Pput_2609
            PST: PSPTO_1357(amiE) PSPTO_2421(amdA)
            PSB: Psyr_1166 Psyr_2208
            PSP: PSPPH_2976
            PEN: PSEEN2156
            PCR: Pcryo_0431
            PRW: PsycPRwf_0418
            ACI: ACIAD1618(amdA)
            SPL: Spea_2163
            MAQ: Maqu_0245 Maqu_2730 Maqu_3862
            LPN: lpg2355 lpg2852(amiC)
            LPF: lpl2277 lpl2764
            LPP: lpp2304 lpp2910
            HHA: Hhal_1003
            ABO: ABO_0120(amiC) ABO_1980(aimE) ABO_2482
            MMW: Mmwyl1_1935 Mmwyl1_3197 Mmwyl1_3206
            REU: Reut_B3768
            REH: H16_B2459(aimE)
            RME: Rmet_0495 Rmet_4787
            BMA: BMAA1320
            BXE: Bxe_C1251
            BVI: Bcep1808_0235
            BUR: Bcep18194_A3378 Bcep18194_A4134 Bcep18194_B1131
                 Bcep18194_B1550 Bcep18194_B1842 Bcep18194_B2503
                 Bcep18194_B2627 Bcep18194_C6669 Bcep18194_C7043
                 Bcep18194_C7676
            BCN: Bcen_2832 Bcen_3678 Bcen_4079 Bcen_4892
            BCH: Bcen2424_0275 Bcen2424_3272 Bcen2424_3512 Bcen2424_3612
                 Bcen2424_4287 Bcen2424_4629 Bcen2424_4689 Bcen2424_6915
            BAM: Bamb_0189 Bamb_2709 Bamb_3988 Bamb_6315 Bamb_6405
            BPS: BPSS0911
            BPM: BURPS1710b_A2509
            BTE: BTH_II0320 BTH_II0721 BTH_II1486
            PNU: Pnuc_2019
            BPE: BP1827
            BPA: BPP2879
            BBR: BB3200
            POL: Bpro_0571
            PNA: Pnap_0171
            AAV: Aave_0191
            AJS: Ajs_2586
            VEI: Veis_0311 Veis_1612 Veis_3137
            MPT: Mpe_A3614
            HAR: HEAR2119 HEAR2676 HEAR3253
            AZO: azo1956(amiD) azo2357
            DAR: Daro_1360
            MFA: Mfla_0463
            HPY: HP0294(aimE) HP1238(aimE)
            HPJ: jhp0279(amiE) jhp1159
            HPA: HPAG1_0296 HPAG1_1180
            HAC: Hac_0554(aimE) Hac_1079(aimE)
            ABU: Abu_1022(gatA)
            GUR: Gura_4324
            DVU: DVU1164(amiE)
            DVL: Dvul_2169
            ADE: Adeh_2922 Adeh_3433
            AFW: Anae109_3242 Anae109_4338
            MLO: mlr5350
            MES: Meso_2296
            PLA: Plav_0165 Plav_2598 Plav_3043
            SME: SMa1377 SMa2363 SMc03245
            SMD: Smed_5337
            RET: RHE_PB00103(ypb00060)
            RLE: pRL90204
            BME: BMEII1134
            OAN: Oant_3309
            BJA: bll0198 bll3874 blr0973 blr6144
            BRA: BRADO0324 BRADO0922 BRADO1531(amdA) BRADO2532 BRADO2587
                 BRADO2916 BRADO4071 BRADO4399 BRADO4401 BRADO4407 BRADO5789
                 BRADO5869(amiE) BRADO6818
            BBT: BBta_0309 BBta_0721 BBta_1958(amiE) BBta_2561 BBta_2877
                 BBta_2934 BBta_3796 BBta_4447 BBta_5240 BBta_5261 BBta_6296
                 BBta_7130
            RPA: RPA1700 RPA1923(aimE) RPA3440
            RPB: RPB_0940 RPB_1679 RPB_1820 RPB_2551 RPB_3629
            RPC: RPC_1671
            RPD: RPD_1043 RPD_1838 RPD_2905 RPD_4286 RPD_4294
            RPE: RPE_3704
            XAU: Xaut_3926
            RSP: RSP_3253 RSP_3526
            RSH: Rsph17029_1064 Rsph17029_3170
            RSQ: Rsph17025_2842
            JAN: Jann_1304
            PDE: Pden_3053
            HNE: HNE_1334
            SWI: Swit_0927 Swit_1621 Swit_4169
            GBE: GbCGDNIH1_1839
            ACR: Acry_2933
            RRU: Rru_A0983
            ABA: Acid345_1493 Acid345_1685
            SUS: Acid_3497 Acid_6116 Acid_7028
            BAN: BA2596 BA4149
            BAR: GBAA2596 GBAA4149
            BAA: BA_3104 BA_4617
            BAT: BAS2418 BAS3851
            BCE: BC2537 BC3939
            BCA: BCE_2616
            BCZ: BCZK2342 BCZK3699
            BTK: BT9727_2377 BT9727_3682
            GKA: GK2270
            LWE: lwe2553
            LLA: L169390(ybgE)
            OOE: OEOE_1486
            CTH: Cthe_1032
            CBE: Cbei_2128
            AMT: Amet_3388
            DRM: Dred_2341
            CSC: Csac_0909
            MTU: Rv1263(amiB2) Rv2363(amiA2) Rv2888c(amiC) Rv3175 Rv3375(amiD)
            MTC: MT1301 MT2432(nylA) MT2956 MT3264 MT3485
            MBO: Mb1294(amiB2) Mb2384(amiA2) Mb2912c(amiC) Mb3200 Mb3409(amiD)
            MBB: BCG_1322(amiB2) BCG_2377(amiA2) BCG_2909c(amiC)
                 BCG_3446(amiD)
            MLE: ML1596
            MPA: MAP2143(amiA2) MAP2509c(amiB2) MAP2954c(amiC)
            MSM: MSMEG_0485 MSMEG_1090 MSMEG_2521 MSMEG_4492
            MVA: Mvan_3824
            MGI: Mflv_2712
            MMC: Mmcs_1995 Mmcs_2705 Mmcs_3451
            MKM: Mkms_2749
            MJL: Mjls_2735
            CJK: jk0917
            NFA: nfa33260 nfa7560
            RHA: RHA1_ro00359(amdA) RHA1_ro01236 RHA1_ro02852 RHA1_ro03211
                 RHA1_ro03496 RHA1_ro04008 RHA1_ro04406 RHA1_ro04575
                 RHA1_ro04799 RHA1_ro05297 RHA1_ro10169(amiE)
            SMA: SAV7269(amiE1) SAV7345(amiE2)
            ART: Arth_1754
            AAU: AAur_pTC20148(amdA)
            TFU: Tfu_2207
            FRA: Francci3_0175
            FAL: FRAAL0331 FRAAL0363 FRAAL3665
            SEN: SACE_1914 SACE_3773 SACE_4293 SACE_5032
            RXY: Rxyl_0238 Rxyl_1701 Rxyl_1878
            LIL: LA1333(amiC)
            LIC: LIC12392(nylA)
            SYN: sll0828(nylA)
            ANA: all1235 all7525
            AVA: Ava_3674 Ava_4525
            TER: Tery_1350 Tery_4203
            SRU: SRU_0414
            PVI: Cvib_1530
            DEB: DehaBAV1_1146
            RRS: RoseRS_1254 RoseRS_2947 RoseRS_3083
            RCA: Rcas_1951 Rcas_2243 Rcas_2860
            DRA: DR_1377 DR_1625
            MEM: Memar_0772
            MBN: Mboo_0857
            NPH: NP0178A(aimE_2) NP4212A(aimE_1)
            APE: APE_0979.1
            SSO: SSO2122(gatA-3)
STRUCTURES  PDB: 2PLQ  2UXY  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.4
            ExPASy - ENZYME nomenclature database: 3.5.1.4
            ExplorEnz - The Enzyme Database: 3.5.1.4
            ERGO genome analysis and discovery system: 3.5.1.4
            UM-BBD (Biocatalysis/Biodegradation Database): 3.5.1.4
            BRENDA, the Enzyme Database: 3.5.1.4
            CAS: 9012-56-0
///
ENTRY       EC 3.5.1.5                  Enzyme
NAME        urease
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     urea amidohydrolase
REACTION    urea + H2O = CO2 + 2 NH3 [RN:R00131]
ALL_REAC    R00131;
            (other) R06134
SUBSTRATE   urea [CPD:C00086];
            H2O [CPD:C00001]
PRODUCT     CO2 [CPD:C00011];
            NH3 [CPD:C00014]
COFACTOR    Nickel [CPD:C00291]
COMMENT     A nickel protein.
REFERENCE   1
  AUTHORS   Dixon, N.E., Gazzola, C., Blakeley, R.L. and Zerner, B.
  TITLE     Metal ions in enzymes using ammonia or amides.
  JOURNAL   Science 191 (1976) 1144-1150.
  ORGANISM  jack bean
REFERENCE   2
  AUTHORS   Sumner, J.B.
  TITLE     Urease.
  JOURNAL   In: Sumner, J.B. and Myrback, K. (Eds.), The Enzymes, vol. 1,
            Academic Press, New York, 1951, p. 873-892.
REFERENCE   3
  AUTHORS   Varner, J.E.
  TITLE     Urease.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 247-256.
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00230  Purine metabolism
            PATH: map00791  Atrazine degradation
            PATH: map05120  Epithelial cell signaling in Helicobacter pylori
                            infection
ORTHOLOGY   KO: K01427  urease
            KO: K01428  urease alpha subunit
            KO: K01429  urease beta subunit
            KO: K01430  urease gamma subunit
GENES       SPU: 583434(LOC583434)
            SPO: SPAC1952.11c
            ANI: AN0431.2
            AFM: AFUA_1G04560
            AOR: AO090003000879
            CNE: CNH01900
            ECE: Z1143(ureA) Z1144(ureB) Z1145(ureC) Z1582(ureA_2)
                 Z1583(ureB_2) Z1584(ureC_2)
            ECS: ECs1322 ECs1323 ECs1324
            YPE: YPO2665(ureA) YPO2666(ureB) YPO2667(ureC)
            YPK: y1237(ureA) y1238(ureB) y1239(ureC)
            YPM: YP_2466(ureA) YP_2467(ureB) YP_2468(ureC)
            YPA: YPA_2392 YPA_2393 YPA_2394
            YPN: YPN_1149 YPN_1150 YPN_1151
            YPP: YPDSF_1609 YPDSF_1610 YPDSF_1611
            YPS: YPTB2942(ureC) YPTB2943(ureB) YPTB2944(ureA)
            YPI: YpsIP31758_1077(ureA) YpsIP31758_1078(ureB)
                 YpsIP31758_1079(ureC)
            YEN: YE0951(ureA) YE0952(ureB) YE0953(ureC)
            PLU: plu2171(ureA) plu2172(ureB) plu2173(ureC)
            ENT: Ent638_3464 Ent638_3465
            BFL: Bfl523(ureC) Bfl524(ureB) Bfl525(ureA)
            BPN: BPEN_542(ureC) BPEN_543(ureB) BPEN_544(ureA)
            HIN: HI0539(ureC) HI0540(ureB) HI0541(ureA)
            HIT: NTHI0665(ureC) NTHI0666(ureB) NTHI0667(ureA)
            APL: APL_1616(ureC) APL_1617(ureB) APL_1618(ureA)
            VFI: VF0673 VF0674 VF0675
            PAE: PA4865(ureA) PA4867(ureB) PA4868(ureC)
            PAU: PA14_64350(ureA) PA14_64370(ureB) PA14_64390(ureC)
            PAP: PSPA7_5589(ureC)
            PPU: PP_2843(ureA) PP_2844(ureB) PP_2845(ureC)
            PPF: Pput_2845 Pput_2846
            PST: PSPTO_2411 PSPTO_4891(ureA) PSPTO_4894(ureB) PSPTO_4895(ureC)
            PSB: Psyr_2197 Psyr_2198 Psyr_4432 Psyr_4435 Psyr_4436
            PSP: PSPPH_4475(ureA) PSPPH_4478(ureB) PSPPH_4479(ureC)
            PFL: PFL_0631(ureC) PFL_0632(ureB) PFL_0635(ureA)
            PFO: Pfl_0580 Pfl_0581 Pfl_0584
            PEN: PSEEN2094(ureA) PSEEN2095(ureB) PSEEN2096(ureC)
            PMY: Pmen_0693 Pmen_0695
            PCR: Pcryo_0880 Pcryo_0881 Pcryo_0882 Pcryo_0986 Pcryo_0988
            ACI: ACIAD1089(ureA) ACIAD1090(ureB) ACIAD1091(ureC)
            PHA: PSHAa1757(ureA) PSHAa1758(ureB) PSHAa1759(ureC)
            SDE: Sde_0219 Sde_0220 Sde_0221
            PIN: Ping_2992 Ping_2993
            MAQ: Maqu_2994 Maqu_2995
            NOC: Noc_2880 Noc_2881 Noc_2882
            AEH: Mlg_0182 Mlg_0183 Mlg_0184
            HCH: HCH_04521(ureA) HCH_04522(ureB) HCH_04523(ureC)
            CSA: Csal_2305 Csal_2306 Csal_2307
            ABO: ABO_2719(ureC) ABO_2720(ureB) ABO_2721(ureA)
            MMW: Mmwyl1_0954 Mmwyl1_0955 Mmwyl1_0956
            RSO: RSc2032(ureC) RSc2033(ureB) RSc2035(ureA)
            REU: Reut_A0992 Reut_A0994 Reut_A0995
            REH: H16_A1081(ureA) H16_A1083(ureB) H16_A1084(ureC)
            RME: Rmet_0958 Rmet_0960 Rmet_0961
            BMA: BMA2182(ureA) BMA2183(ureB) BMA2184(ureC)
            BMV: BMASAVP1_A0723(ureC) BMASAVP1_A0724(ureB)
                 BMASAVP1_A0725(ureA)
            BML: BMA10299_A2557(ureC) BMA10299_A2558(ureB)
                 BMA10299_A2559(ureA)
            BMN: BMA10247_2055(ureA) BMA10247_2056(ureB) BMA10247_2057(ureC)
            BXE: Bxe_A3692 Bxe_A3693 Bxe_A3694
            BVI: Bcep1808_0833 Bcep1808_0834 Bcep1808_0835
            BUR: Bcep18194_A4006 Bcep18194_A4007 Bcep18194_A4008
            BCN: Bcen_0421 Bcen_0422 Bcen_0423
            BCH: Bcen2424_0900 Bcen2424_0901 Bcen2424_0902
            BAM: Bamb_0779 Bamb_0780 Bamb_0781
            BPS: BPSL2657(ureA) BPSL2658(ureB) BPSL2659(ureC)
            BPM: BURPS1710b_3133(ureA) BURPS1710b_3134(ureAB)
                 BURPS1710b_3135(ureC)
            BPL: BURPS1106A_3110(ureA) BURPS1106A_3111(ureB)
                 BURPS1106A_3112(ureC)
            BPD: BURPS668_3074(ureA) BURPS668_3075(ureB) BURPS668_3076(ureC)
            BTE: BTH_I1496(ureC) BTH_I1497 BTH_I1498(ureA)
            PNU: Pnuc_1193 Pnuc_1194 Pnuc_1196
            BPE: BP3168(ureC) BP3169(ureB) BP3171(ureA)
            BPA: BPP3855(ureC) BPP3856(ureB) BPP3858(ureA)
            BBR: BB4323(ureC) BB4324(ureB) BB4326(ureA)
            RFR: Rfer_3399 Rfer_3400 Rfer_3402
            POL: Bpro_1350 Bpro_1351 Bpro_1352
            PNA: Pnap_0974 Pnap_0975 Pnap_0977
            AAV: Aave_3526 Aave_3528
            VEI: Veis_1726 Veis_1727 Veis_1729
            MPT: Mpe_A0667 Mpe_A0668 Mpe_A0669
            MMS: mma_1812(ureA) mma_1813(ureB) mma_1814(ureC)
            NMU: Nmul_A1239 Nmul_A1240 Nmul_A1241
            AZO: azo3504(ureC) azo3505 azo3507(ureA)
            DAR: Daro_1427 Daro_1428 Daro_1429
            MFA: Mfla_1767 Mfla_1768 Mfla_1769
            HPY: HP0072(ureB) HP0073(ureA)
            HPJ: jhp0067(ureB) jhp0068(ureA)
            HPA: HPAG1_0068 HPAG1_0070 HPAG1_0073 HPAG1_0074
            HHE: HH0407(ureA) HH0408(ureB)
            HAC: Hac_0447(ureC) Hac_0448(ureAB) Hac_1532(ureA) Hac_1533(ureC)
                 Hac_1536(ureF) Hac_1538(ureH)
            ABU: Abu_0806(ureAB) Abu_0807(ureC)
            AFW: Anae109_4048 Anae109_4049
            MLO: mll4940 mll4948 msl4944
            MES: Meso_2681 Meso_2683 Meso_2684
            SME: SMc01837(ureC) SMc01939(ureB) SMc01941(ureA)
            SMD: Smed_2386 Smed_2388
            ATU: Atu2401(ureC) Atu2405(ureB) Atu2407(ureA)
            ATC: AGR_C_4357(ureA) AGR_C_4368(ureA)
            RET: RHE_CH03305(ureC) RHE_CH03308(ureB) RHE_CH03310(ureA)
            RLE: RL3731(ureC) RL3734(ureB) RL3735(ureA)
            BME: BMEI0647 BMEI0648 BMEI0649 BMEI1652 BMEI1653 BMEI1654
            BMF: BAB1_0298(ureA-1) BAB1_0299(ureB-1) BAB1_0300(ureC-1)
                 BAB1_1376(ureA-2) BAB1_1377 BAB1_1378
            BMS: BR0268(ureA-1) BR0269(ureB-1) BR0270(ureC-1) BR1356(ureA-2)
                 BR1357(ureB-2) BR1358(ureC-2)
            BMB: BruAb1_0294(ureA-1) BruAb1_0295(ureB-1) BruAb1_0296(ureC-1)
                 BruAb1_1353(ureA-2) BruAb1_1354(ureB-2) BruAb1_1355(ureC-2)
            BOV: BOV_0282(ureA-1) BOV_0283(ureB-1) BOV_0284(ureC-1)
                 BOV_1312(ureA-2) BOV_1313(ureB-2) BOV_1314(ureC-2)
            OAN: Oant_0332 Oant_0334 Oant_2442 Oant_2443
            BJA: blr1454(ureA) blr1455(ureB) blr1457(ureC)
            BRA: BRADO1037(ureA) BRADO1038(ureB) BRADO1041(ureC)
                 BRADO4066(ureC) BRADO4067(ureAB) BRADO5863(ureC)
                 BRADO5864(ureAB)
            BBT: BBta_1961(ureAB) BBta_1962(ureC) BBta_4442(ureC)
                 BBta_4443(ureAB) BBta_7009(ureC) BBta_7011(ureB)
                 BBta_7012(ureA)
            RPA: RPA3660(ureC) RPA3662(ureB) RPA3663(ureA)
            RPB: RPB_1800 RPB_1801 RPB_1803
            RPC: RPC_3692 RPC_3695 RPC_3696
            RPD: RPD_3500 RPD_3503 RPD_3504
            RPE: RPE_3732 RPE_3734 RPE_3735
            XAU: Xaut_4155 Xaut_4156
            SIL: SPO1712(ureA) SPO1713(ureB) SPO1714(ureC)
            SIT: TM1040_0385 TM1040_0386 TM1040_0387
            RSP: RSP_0308(ureB) RSP_0309(ureA) RSP_6111(ureC)
            RSH: Rsph17029_1953 Rsph17029_1954
            RSQ: Rsph17025_0985 Rsph17025_0986
            JAN: Jann_1745 Jann_1747 Jann_1752
            RDE: RD1_3793(ureA) RD1_3795(ureB) RD1_3800(ureC)
            PDE: Pden_1209 Pden_1211
            GBE: GbCGDNIH1_2162 GbCGDNIH1_2163 GbCGDNIH1_2164
            MGM: Mmc1_1025 Mmc1_1026 Mmc1_1027
            BSU: BG11981(ureA) BG11982(ureB) BG11983(ureC)
            BHA: BH0252(ureA) BH0253(ureB) BH0254(ureC)
            BCA: BCE_3662(ureC) BCE_3663(ureB) BCE_3664(ureA)
            BAY: RBAM_033810(ureC) RBAM_033820(ureB) RBAM_033830(ureA)
            GKA: GK1930(ureC) GK1931(ureB) GK1932(ureA)
            SAU: SA2082(ureA) SA2083(ureB) SA2084(ureC)
            SAV: SAV2288(ureA) SAV2289(ureB) SAV2290(ureC)
            SAM: MW2206(ureA) MW2207(ureB) MW2208(ureC)
            SAR: SAR2372(ureA) SAR2373(ureB) SAR2374(ureC)
            SAS: SAS2178 SAS2179 SAS2180
            SAC: SACOL2280(ureA) SACOL2281(ureB) SACOL2282(ureC)
            SAB: SAB2160(ureA) SAB2161(ureB) SAB2162(ureC)
            SAA: SAUSA300_2238(ureA) SAUSA300_2239(ureB) SAUSA300_2240(ureC)
            SAO: SAOUHSC_02558 SAOUHSC_02559 SAOUHSC_02561
            SAJ: SaurJH9_2312 SaurJH9_2313
            SAH: SaurJH1_2355 SaurJH1_2356
            SEP: SE1861 SE1862 SE1863
            SER: SERP1869(ureA) SERP1870(ureB) SERP1871(ureC)
            SSP: SSP0263 SSP0264 SSP0265
            STC: str0281(ureA) str0282(ureB) str0283(ureC)
            STL: stu0281(ureA) stu0282(ureB) stu0283(ureC)
            STE: STER_0323
            CTH: Cthe_1816 Cthe_1817 Cthe_1818
            CSC: Csac_2467
            UUR: UU432(ureC) UU433(ureB) UU434(ureA)
            MTU: Rv1848(ureA) Rv1849(ureB) Rv1850(ureC)
            MTC: MT1896(ureA) MT1897(ureB) MT1898(ureC)
            MBO: Mb1879(ureA) Mb1880(ureB) Mb1881(ureC)
            MBB: BCG_1884(ureA) BCG_1885(ureB) BCG_1886(ureC)
            MSM: MSMEG_1093 MSMEG_1094(ureC) MSMEG_3625(ureC) MSMEG_3626(ureB)
                 MSMEG_3627(ureA)
            MUL: MUL_3031(ureA)
            MVA: Mvan_3082 Mvan_3083 Mvan_3084
            MGI: Mflv_1685 Mflv_3352 Mflv_3353 Mflv_3354
            MMC: Mmcs_2805 Mmcs_2806 Mmcs_2807
            MKM: Mkms_2849 Mkms_2850 Mkms_2851
            MJL: Mjls_2832 Mjls_2833 Mjls_2834
            CGL: NCgl0083(cgl0084) NCgl0084(cgl0085) NCgl0085(cgl0086)
                 NCgl0086(cgl0087) NCgl0087(cgl0088) NCgl0089(cgl0090)
            CGB: cg0113(ureA) cg0114(ureB) cg0115(ureC)
            CEF: CE0993(ureA) CE0994(ureB) CE0995(ureC)
            NFA: nfa25240(ureA) nfa25250(ureB) nfa25260(ureC)
            RHA: RHA1_ro05678(ureA) RHA1_ro05679(ureB) RHA1_ro05680(ureC)
            SCO: SCO1234(2SCG1.09c) SCO1235(2SCG1.10c) SCO1236(2SCG1.11c)
                 SCO5525(ureAB) SCO5526(ureC)
            SMA: SAV2715(ureC2) SAV2716(ureAB) SAV7104(ureA) SAV7105(ureB)
                 SAV7106(ureC1)
            ART: Arth_0241 Arth_0242 Arth_0243
            AAU: AAur_0214(ureA) AAur_0215(ureB) AAur_0216(ureC)
            FRA: Francci3_0832 Francci3_0833 Francci3_0834
            FAL: FRAAL1447(ureC) FRAAL1448(ureB) FRAAL1449(ureA)
            KRA: Krad_0835
            SEN: SACE_0634(ureA) SACE_0635(ureB) SACE_0636(ureC)
                 SACE_2526(ureC) SACE_2527(ureA) SACE_3484(ureA)
                 SACE_3485(ureC)
            SYN: sll0420(ureB) sll1750(ureC) slr1256(ureA)
            SYW: SYNW2447(ureA) SYNW2448(ureB) SYNW2449(ureC)
            SYD: Syncc9605_2625 Syncc9605_2626 Syncc9605_2627
            SYE: Syncc9902_2255 Syncc9902_2256 Syncc9902_2257
            SYG: sync_2877(ureA) sync_2878(ureB) sync_2879(ureC)
            SYR: SynRCC307_2461(ureA) SynRCC307_2462(ureB)
                 SynRCC307_2463(ureC)
            CYA: CYA_0601 CYA_0603(ureC)
            CYB: CYB_0023(ureC) CYB_2370(ureA)
            TEL: tll0330(ureB) tlr0005(ureC) tlr0981(ureA)
            ANA: alr3667 alr3668 alr3670
            AVA: Ava_3618 Ava_3620 Ava_3621
            PMM: PMM0963(ureC) PMM0964(ureB) PMM0965(ureA)
            PMT: PMT2234(ureA) PMT2235(ureB) PMT2236(ureC)
            PMN: PMN2A_1053 PMN2A_1054 PMN2A_1055
            PMI: PMT9312_0834 PMT9312_0835 PMT9312_0836
            PMB: A9601_08931(ureA) A9601_08941(ureB) A9601_08951(ureC)
            PMF: P9303_29791(ureA) P9303_29801(ureB) P9303_29811(ureC)
            PMG: P9301_08911(ureA) P9301_08921(ureB) P9301_08931(ureC)
            PME: NATL1_19241(ureA) NATL1_19251(ureB) NATL1_19261(ureC)
            TER: Tery_0746 Tery_0747 Tery_0752
            CHU: CHU_1260(ureA) CHU_1261(ureC) CHU_1262(ureF) CHU_1264(ureH)
            FJO: Fjoh_4835 Fjoh_4836 Fjoh_4837
            DRA: DR_A0318 DR_A0319
            HMA: pNG7123(ureB) pNG7124(ureC) pNG7125(ureA) pNG7129(ureF)
                 pNG7249(ureX) rrnAC3411
            HWA: HQ3625A(ureB) HQ3626A(ureA) HQ3627A(ureC)
            NPH: NP2008A(ureB) NP2010A(ureA) NP2012A(ureC)
            STO: ST1028 ST1029
            MSE: Msed_0888
STRUCTURES  PDB: 1A5K  1A5L  1A5M  1A5N  1A5O  1E9Z  1EF2  1EJR  1EJS  1EJT  
                 1EJU  1EJV  1EJW  1EJX  1FWA  1FWB  1FWC  1FWD  1FWE  1FWF  
                 1FWG  1FWH  1FWI  1FWJ  1IE7  1KRA  1KRB  1KRC  1S3T  1UBP  
                 2FVH  2KAU  2UBP  3UBP  4UBP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.5
            ExPASy - ENZYME nomenclature database: 3.5.1.5
            ExplorEnz - The Enzyme Database: 3.5.1.5
            ERGO genome analysis and discovery system: 3.5.1.5
            UM-BBD (Biocatalysis/Biodegradation Database): 3.5.1.5
            BRENDA, the Enzyme Database: 3.5.1.5
            CAS: 9002-13-5
///
ENTRY       EC 3.5.1.6                  Enzyme
NAME        beta-ureidopropionase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-carbamoyl-beta-alanine amidohydrolase
REACTION    N-carbamoyl-beta-alanine + H2O = beta-alanine + CO2 + NH3
            [RN:R00905]
ALL_REAC    R00905;
            (other) R04666 R06134
SUBSTRATE   N-carbamoyl-beta-alanine [CPD:C02642];
            H2O [CPD:C00001]
PRODUCT     beta-alanine [CPD:C00099];
            CO2 [CPD:C00011];
            NH3 [CPD:C00014]
COMMENT     The animal enzyme also acts on beta-ureidoisobutyrate.
REFERENCE   1  [PMID:13849303]
  AUTHORS   CAMPBELL LL.
  TITLE     Reductive degradation of pyrimidines. 5. Enzymatic conversion of
            N-carbamyl-beta-alanine to beta-alanine, carbon dioxide, and
            ammonia.
  JOURNAL   J. Biol. Chem. 235 (1960) 2375-8.
  ORGANISM  Clostridium uracilicum
REFERENCE   2  [PMID:13538975]
  AUTHORS   CARAVACA J, GRISOLIA S.
  TITLE     Enzymatic decarbamylation of carbamyl beta-alanine and carbamyl
            beta-aminoisobutyric acid.
  JOURNAL   J. Biol. Chem. 231 (1958) 357-65.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:6433973]
  AUTHORS   Traut TW, Loechel S.
  TITLE     Pyrimidine catabolism: individual characterization of the three
            sequential enzymes with a new assay.
  JOURNAL   Biochemistry. 23 (1984) 2533-9.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00240  Pyrimidine metabolism
            PATH: map00410  beta-Alanine metabolism
            PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K01431  beta-ureidopropionase
GENES       HSA: 51733(UPB1)
            MMU: 103149(Upb1)
            RNO: 116593(Upb1)
            CFA: 486398(UPB1)
            GGA: 416949(UPB1)
            XLA: 447326(MGC82230)
            DRE: 322660(upb1)
            SPU: 577651(LOC577651)
            DME: Dmel_CG3027(pyd3)
            CEL: F13H8.7
            OSA: 4343249
            PIC: PICST_62485(NIT2)
            CGR: CAGL0L05588g
            DDI: DDB_0185221(pyd3)
            VFI: VF0378
            PAE: PA0444
            PAU: PA14_05810(amaB)
            PPU: PP_0614 PP_4034
            PST: PSPTO_3190
            PSB: Psyr_3056
            PSP: PSPPH_0152 PSPPH_4702
            PHA: PSHAa1835
            NOC: Noc_2448
            RME: Rmet_1931
            BMA: BMAA1099(amaB-2)
            BXE: Bxe_A1427 Bxe_B2561
            BUR: Bcep18194_A4757
            BPS: BPSS1251
            BPM: BURPS1710b_0333 BURPS1710b_1308(amaB-1)
                 BURPS1710b_A0251(amaB-2)
            BTE: BTH_II1163
            BPE: BP1859(amaB) BP2301
            BPA: BPP1570(amaB) BPP2428
            BBR: BB1877 BB2648(amaB)
            POL: Bpro_0379
            MMS: mma_0662
            MLO: mll1631 mlr7938
            SME: SMc01820
            ATU: Atu2385(amaB)
            ATC: AGR_C_4327
            RET: RHE_CH03290(amaB)
            RLE: RL3716(atcC)
            BME: BMEI1643
            BMF: BAB1_0310
            BMS: BR0279
            BJA: bll2919(amaB)
            RPA: RPA1745
            SIL: SPO1781
            RSP: RSP_0184 RSP_1455
            RDE: RD1_1496
            FAL: FRAAL0165 FRAAL1415
            CCH: Cag_0942
            TTH: TTC1539
            HMA: pNG7248(amaB)
STRUCTURES  PDB: 1R3N  1R43  2V8D  2V8G  2V8H  2V8V  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.6
            ExPASy - ENZYME nomenclature database: 3.5.1.6
            ExplorEnz - The Enzyme Database: 3.5.1.6
            ERGO genome analysis and discovery system: 3.5.1.6
            BRENDA, the Enzyme Database: 3.5.1.6
            CAS: 9027-27-4
///
ENTRY       EC 3.5.1.7                  Enzyme
NAME        ureidosuccinase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-carbamoyl-L-aspartate amidohydrolase
REACTION    N-carbamoyl-L-aspartate + H2O = L-aspartate + CO2 + NH3 [RN:R00484]
ALL_REAC    R00484
SUBSTRATE   N-carbamoyl-L-aspartate [CPD:C00438];
            H2O [CPD:C00001]
PRODUCT     L-aspartate [CPD:C00049];
            CO2 [CPD:C00011];
            NH3 [CPD:C00014]
REFERENCE   1  [PMID:14353892]
  AUTHORS   LIEBERMAN I, KORNBERG A.
  TITLE     Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. III.
            Ureidosuccinase.
  JOURNAL   J. Biol. Chem. 212 (1955) 909-20.
  ORGANISM  Zymobacterium oroticum
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.7
            ExPASy - ENZYME nomenclature database: 3.5.1.7
            ExplorEnz - The Enzyme Database: 3.5.1.7
            ERGO genome analysis and discovery system: 3.5.1.7
            BRENDA, the Enzyme Database: 3.5.1.7
            CAS: 9024-81-1
///
ENTRY       EC 3.5.1.8                  Enzyme
NAME        formylaspartate deformylase;
            formylaspartic formylase (formylase I, formylase II)
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-formyl-L-aspartate amidohydrolase
REACTION    N-formyl-L-aspartate + H2O = formate + L-aspartate [RN:R00526]
ALL_REAC    R00526
SUBSTRATE   N-formyl-L-aspartate [CPD:C01044];
            H2O [CPD:C00001]
PRODUCT     formate [CPD:C00058];
            L-aspartate [CPD:C00049]
REFERENCE   1
  AUTHORS   Ohmura, E. and Hayaishi, O.
  TITLE     Enzymatic conversion of formylaspartic acid to aspartic acid.
  JOURNAL   J. Biol. Chem. 227 (1957) 181-190.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00340  Histidine metabolism
            PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.8
            ExPASy - ENZYME nomenclature database: 3.5.1.8
            ExplorEnz - The Enzyme Database: 3.5.1.8
            ERGO genome analysis and discovery system: 3.5.1.8
            BRENDA, the Enzyme Database: 3.5.1.8
            CAS: 9025-09-6
///
ENTRY       EC 3.5.1.9                  Enzyme
NAME        arylformamidase;
            kynurenine formamidase;
            formylase;
            formylkynureninase;
            formylkynurenine formamidase;
            formamidase I;
            formamidase II
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     aryl-formylamine amidohydrolase
REACTION    N-formyl-L-kynurenine + H2O = formate + L-kynurenine [RN:R01959]
ALL_REAC    R01959;
            (other) R00988 R04911
SUBSTRATE   N-formyl-L-kynurenine [CPD:C02700];
            H2O [CPD:C00001]
PRODUCT     formate [CPD:C00058];
            L-kynurenine [CPD:C00328]
COMMENT     Also acts on other aromatic formylamines.
REFERENCE   1  [PMID:14907621]
  AUTHORS   HAYAISHI O, STANIER RY.
  TITLE     The bacterial oxidation of tryptophan. III. Enzymatic activities of
            cell-free extracts from bacteria employing the aromatic pathway.
  JOURNAL   J. Bacteriol. 62 (1951) 691-709.
REFERENCE   2  [PMID:13163050]
  AUTHORS   JAKOBY WB.
  TITLE     Kynurenine formamidase from Neurospora.
  JOURNAL   J. Biol. Chem. 207 (1954) 657-63.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   3  [PMID:14794728]
  AUTHORS   MEHLER AH, KNOX WE.
  TITLE     The conversion of tryptophan to kynurenine in liver. II. The
            enzymatic hydrolysis of formylkynurenine.
  JOURNAL   J. Biol. Chem. 187 (1950) 431-8.
  ORGANISM  rabbit, rat [GN:rno]
PATHWAY     PATH: map00380  Tryptophan metabolism
            PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K01432  arylformamidase
GENES       HSA: 125061(AFMID)
            MMU: 71562(Afmid)
            GGA: 769005(AFMID)
            PAP: PSPA7_3206(kynB)
            REH: H16_A3005 H16_B1997
            BMV: BMASAVP1_A0652(kynB)
            BML: BMA10299_A2487(kynB)
            BMN: BMA10247_0100(kynB)
            BPL: BURPS1106A_0897(kynB)
            BPD: BURPS668_0894(kynB)
            RLE: pRL120604
            RDE: RD1_0928
            GFO: GFO_0068
            FPS: FP0207
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.9
            ExPASy - ENZYME nomenclature database: 3.5.1.9
            ExplorEnz - The Enzyme Database: 3.5.1.9
            ERGO genome analysis and discovery system: 3.5.1.9
            BRENDA, the Enzyme Database: 3.5.1.9
            CAS: 156229-75-3
///
ENTRY       EC 3.5.1.10                 Enzyme
NAME        formyltetrahydrofolate deformylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     10-formyltetrahydrofolate amidohydrolase
REACTION    10-formyltetrahydrofolate + H2O = formate + tetrahydrofolate
            [RN:R00944]
ALL_REAC    R00944
SUBSTRATE   10-formyltetrahydrofolate [CPD:C00234];
            H2O [CPD:C00001]
PRODUCT     formate [CPD:C00058];
            tetrahydrofolate [CPD:C00101]
REFERENCE   1
  AUTHORS   Huennekens, F.M.
  TITLE     Enzymatic deacylation of N10-formyltetrahydrofolic acid.
  JOURNAL   Fed. Proc. 16 (1957) 199.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
            PATH: map00670  One carbon pool by folate
ORTHOLOGY   KO: K01433  formyltetrahydrofolate deformylase
GENES       ATH: AT4G17360
            OSA: 4331294
            ANI: AN0495.2
            AFM: AFUA_6G11620
            AOR: AO090023000412
            UMA: UM00231.1
            ECO: b1232(purU)
            ECJ: JW1220(purU)
            ECE: Z2008(purU)
            ECS: ECs1734
            ECC: c1696(purU)
            ECI: UTI89_C1428(purU)
            ECP: ECP_1279
            ECV: APECO1_346(purU)
            ECW: EcE24377A_1381(purU)
            ECX: EcHS_A1340
            STY: STY1294(purU)
            STT: t1667(purU)
            SPT: SPA1122(purU)
            SEC: SC1751(purU)
            STM: STM1756(purU)
            YPK: y2150(purU)
            YPM: YP_1970(purU)
            YPA: YPA_1529
            YPN: YPN_1638
            YPS: YPTB2097(purU)
            YPI: YpsIP31758_1971(purU)
            SFL: SF1232(purU)
            SFX: S1318(purU)
            SFV: SFV_1245(purU)
            SSN: SSON_1947(purU)
            SBO: SBO_1837(purU)
            SDY: SDY_1284(purU)
            ECA: ECA2333(purU)
            PLU: plu2504(purU)
            WBR: WGLp370(purU)
            SGL: SG1364
            HIT: NTHI1463(purU)
            HIP: CGSHiEE_05545(purU)
            HIQ: CGSHiGG_10195(purU)
            HSO: HS_0786(purU)
            PMU: PM0873(purU)
            MSU: MS1323(purU)
            XFA: XF1831
            XFT: PD1036(purU)
            XCC: XCC0310(purU)
            XCB: XC_0322
            XCV: XCV0333(purU)
            XAC: XAC0324(purU)
            XOO: XOO4342(purU)
            XOM: XOO_4092(XOO4092)
            VCH: VC1992
            VCO: VC0395_A1577(purU)
            VVU: VV1_0143
            VVY: VV1046
            VPA: VP0864
            VFI: VF1714
            PPR: PBPRA1066 PBPRA1448(purU-2)
            PAE: PA4314(purU1) PA5420(purU2)
            PAU: PA14_56060(purU1) PA14_71530(purU2)
            PAP: PSPA7_4882(purU2) PSPA7_6208(purU1)
            PPU: PP_0327(purU-1) PP_1367(purU-2) PP_1943(purU-3)
            PST: PSPTO_0456(purU-1) PSPTO_2454(purU-2) PSPTO_4314(purU-3)
            PSB: Psyr_2226 Psyr_4018 Psyr_4717
            PSP: PSPPH_2960(purU1) PSPPH_4024(purU2) PSPPH_4755(purU3)
            PFL: PFL_4786(purU) PFL_5724(purU)
            PFO: Pfl_4436 Pfl_5203
            PEN: PSEEN1152 PSEEN5157(purU-1)
            PCR: Pcryo_1987
            ACI: ACIAD0505(purU1) ACIAD2554(purU)
            SON: SO_1624(purU)
            SDN: Sden_1549
            SFR: Sfri_1265
            SHE: Shewmr4_2647
            SHM: Shewmr7_2714
            SHN: Shewana3_2821
            CPS: CPS_2482(purU1) CPS_3620(purU2) CPS_4036(purU3)
                 CPS_4357(purU4)
            PHA: PSHAa0701(purU)
            PAT: Patl_0486
            SDE: Sde_2376
            MAQ: Maqu_1020
            FTA: FTA_1602 FTA_1603
            FTN: FTN_0629(purU)
            TCX: Tcr_1352 Tcr_2051
            NOC: Noc_1789
            AEH: Mlg_2099
            HCH: HCH_04985(purU)
            CSA: Csal_1002 Csal_2073
            ABO: ABO_1563(purU)
            AHA: AHA_1310(purU)
            CVI: CV_1926(purU)
            RSO: RSc1106(purU3) RSc1873(purU1) RSp0065(purU2)
            REU: Reut_A2211 Reut_B4812
            REH: H16_A2505 H16_B1956(purU)
            RME: Rmet_2236
            BMA: BMA3097(purU-1) BMAA0482(purU-2)
            BMV: BMASAVP1_0699(purU-2) BMASAVP1_A0066(purU-1)
            BML: BMA10299_0995(purU-2) BMA10299_A1524(purU-1)
            BMN: BMA10247_2952(purU-1) BMA10247_A1968(purU-2)
            BXE: Bxe_A4112 Bxe_B1575
            BUR: Bcep18194_A6111 Bcep18194_B0585
            BCN: Bcen_2167 Bcen_3294
            BCH: Bcen2424_2781 Bcen2424_5074
            BAM: Bamb_2841
            BPS: BPSL0543 BPSS0558
            BPM: BURPS1710b_0777(purU) BURPS1710b_A2119(purU)
            BPL: BURPS1106A_0607(purU) BURPS1106A_A0751(purU)
            BPD: BURPS668_0591(purU) BURPS668_A0839(purU)
            BTE: BTH_I0496(purU-1) BTH_II1857(purU-2)
            BPE: BP2514(purU) BP3254
            BPA: BPP3501(purU) BPP3610
            BBR: BB4045
            RFR: Rfer_0609
            POL: Bpro_0438
            MPT: Mpe_A3546
            HAR: HEAR0993(purU)
            MMS: mma_1130
            EBA: ebA3467(purU)
            AZO: azo3742(purU)
            DAR: Daro_0056
            TBD: Tbd_1977
            MFA: Mfla_2434
            HPY: HP1434(purU)
            HPA: HPAG1_1360
            HHE: HH1691(purU)
            HAC: Hac_1657(purU)
            WSU: WS1475(purU)
            TDN: Tmden_1098
            CJE: Cj0790(purU)
            CJR: CJE0881(purU)
            CJJ: CJJ81176_0811(purU)
            CJU: C8J_0741(purU)
            CJD: JJD26997_1220(purU)
            CFF: CFF8240_0822(purU)
            CCV: CCV52592_1370(purU)
            CHA: CHAB381_1249(purU)
            ABU: Abu_1077(purU)
            NIS: NIS_0729(purU)
            SUN: SUN_1704(purU)
            DVU: DVU1540(purU)
            ADE: Adeh_2012
            MES: Meso_0452
            SME: SMa2141 SMc03205(purU1) SMc04154(purU2)
            ATU: Atu2464(purU) Atu4231(purU) Atu4315(purU)
            ATC: AGR_C_4474(purU) AGR_L_1098 AGR_L_1261
            RET: RHE_CH00225(purUch) RHE_PE00417(purUe)
            RLE: RL0233(purU) pRL110553(purU)
            BME: BMEII0387
            BMF: BAB2_0326(purU)
            BMS: BRA0909(purU)
            BMB: BruAb2_0324(purU)
            BOV: BOV_A0852(purU)
            BJA: bll5955(purU)
            BRA: BRADO5257(purU)
            BBT: BBta_5709(purU)
            RPA: RPA4032(purU)
            RPB: RPB_1145 RPB_1577
            RPC: RPC_4164
            RPD: RPD_1583
            RPE: RPE_4219
            NWI: Nwi_2382
            CCR: CC_3630
            RSP: RSP_0944(purU)
            HNE: HNE_0787(purU)
            NAR: Saro_2862
            ELI: ELI_14550
            GOX: GOX2073
            RRU: Rru_A0556
            MAG: amb3572
            BSU: BG13237(purU)
            BHA: BH3265
            BLI: BL03753(purU)
            BLD: BLi01411(ykkE)
            BCL: ABC2781(purU)
            BAY: RBAM_012920(ykkE)
            BPU: BPUM_1205
            OIH: OB2693
            GKA: GK1736
            SSP: SSP0951
            MTU: Rv2964(purU)
            MTC: MT3041(purU)
            MBO: Mb2988(purU)
            MBB: BCG_2985(purU)
            MSM: MSMEG_2200(purU)
            CGL: NCgl0371(cgl0382)
            CGB: cg0457(purU)
            CEF: CE0400
            NFA: nfa52050(purU)
            RHA: RHA1_ro01818 RHA1_ro02096
            SCO: SCO4403(SC6F11.01)
            SMA: SAV3846(purU)
            LXX: Lxx19400(purU)
            CMI: CMM_2532(purU)
            AAU: AAur_0485(purU) AAur_1226(purU) AAur_3831(purU)
            PAC: PPA1739
            TFU: Tfu_2356
            FAL: FRAAL2311(purU)
            ACE: Acel_0154
            SEN: SACE_4502(purU-2) SACE_6982(purU)
            RBA: RB256(purU)
            SYN: sll0070(purU)
            SYW: SYNW2504(purU)
            SYC: syc0537_d(purU)
            SYF: Synpcc7942_1008
            SYD: Syncc9605_2671
            SYE: Syncc9902_2300
            SYG: sync_2917(purU)
            SYR: SynRCC307_2512(purU)
            SYX: SynWH7803_2509(purU)
            CYA: CYA_0760(purU)
            CYB: CYB_2447(purU)
            TEL: tll0183(purU)
            GVI: gll4325
            ANA: alr1623
            AVA: Ava_4234
            PMM: PMM1702(purU)
            PMT: PMT2253(purU)
            PMN: PMN2A_1311
            PMI: PMT9312_1795
            PMB: A9601_19121(purU)
            PMC: P9515_18931(purU)
            PMF: P9303_30021(purU)
            PMG: P9301_18931(purU)
            PMH: P9215_19751
            PME: NATL1_21841(purU)
            BTH: BT_1381
            CHU: CHU_3078(purU)
            GFO: GFO_0482(purU)
            CTE: CT1825(purU)
            PLT: Plut_0467
            DET: DET1237(purU)
            DEH: cbdb_A1158(purU)
            DRA: DR_0584
            DGE: Dgeo_1488
            TTH: TTC0957
            TTJ: TTHA1321
            AAE: aq_1818(purU)
            HAL: VNG1946G(purU)
            HMA: rrnAC3272(purU)
            HWA: HQ3129A(purU)
            NPH: NP5006A(purU)
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.10
            ExPASy - ENZYME nomenclature database: 3.5.1.10
            ExplorEnz - The Enzyme Database: 3.5.1.10
            ERGO genome analysis and discovery system: 3.5.1.10
            BRENDA, the Enzyme Database: 3.5.1.10
            CAS: 9025-08-5
///
ENTRY       EC 3.5.1.11                 Enzyme
NAME        penicillin amidase;
            penicillin acylase;
            benzylpenicillin acylase;
            novozym 217;
            semacylase;
            alpha-acylamino-beta-lactam acylhydrolase;
            ampicillin acylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     penicillin amidohydrolase
REACTION    penicillin + H2O = a carboxylate + 6-aminopenicillanate [RN:R02170]
ALL_REAC    R02170;
            (other) R04103
SUBSTRATE   penicillin [CPD:C00395];
            H2O [CPD:C00001]
PRODUCT     carboxylate [CPD:C00060];
            6-aminopenicillanate [CPD:C02954]
REFERENCE   1
  AUTHORS   Sakaguchi, K. and Murao, S.
  TITLE     A preliminary report on a new enzyme, "penicillin-amidase".
  JOURNAL   J. Agric. Chem. Soc. Jpn. 23 (1950) 411.
PATHWAY     PATH: map00311  Penicillin and cephalosporin biosynthesis
ORTHOLOGY   KO: K01434  penicillin amidase
GENES       TET: TTHERM_00898180
            SBO: SBO_4393
            SPE: Spro_3142
            XCC: XCC1392(acyII)
            XCB: XC_2845
            XCV: XCV0041 XCV0042 XCV1494
            XAC: XAC0037
            XOO: XOO1993(acyII)
            XOM: XOO_1884(XOO1884)
            PAU: PA14_03980
            PPF: Pput_1147
            PFO: Pfl_5398
            PEN: PSEEN2083 PSEEN5257
            PMY: Pmen_1414
            SDN: Sden_3735
            SAZ: Sama_3540
            SLO: Shew_2669
            SSE: Ssed_3220
            SPL: Spea_2914
            CPS: CPS_1223
            MCA: MCA3025(acyII)
            REU: Reut_A1841
            REH: H16_A1918
            RME: Rmet_1578 Rmet_5635
            BMA: BMA1038 BMAA1877
            BUR: Bcep18194_B0916
            BPS: BPSL0730 BPSL1710 BPSS0200
            BPM: BURPS1710b_0953(acyII) BURPS1710b_2163(acyII)
                 BURPS1710b_A1726
            BTE: BTH_I0631
            PNU: Pnuc_1150
            RFR: Rfer_1547
            POL: Bpro_2452
            VEI: Veis_1397 Veis_3277 Veis_4305
            MPT: Mpe_A1822
            NEU: NE1123
            NET: Neut_1415
            NMU: Nmul_A0961
            BBA: Bd2313
            ADE: Adeh_3892
            RFE: RF_1137
            BME: BMEII0211 BMEII0212
            BMB: BruAb2_1029
            OAN: Oant_1703
            SIL: SPO2078
            SIT: TM1040_1354
            RSP: RSP_2845
            RSH: Rsph17029_1448
            RSQ: Rsph17025_1495
            JAN: Jann_2327
            RDE: RD1_2752(acy)
            PDE: Pden_4002 Pden_4813
            MMR: Mmar10_1553
            HNE: HNE_0221
            SAL: Sala_2388
            GBE: GbCGDNIH1_0997
            RRU: Rru_A1840
            MAG: amb2576
            ABA: Acid345_3370
            SUS: Acid_0605 Acid_4936 Acid_5979
            BAN: BA3330
            BAR: GBAA3330
            BAA: BA_3832
            BAT: BAS3087
            BCE: BC3254
            BCA: BCE_3292
            BCZ: BCZK2980
            BTK: BT9727_3031
            OIH: OB3304 OB3305
            SAJ: SaurJH9_0259
            SAH: SaurJH1_0266
            LLA: L86424(pacB)
            STH: STH69
            CBE: Cbei_3673
            SCO: SCO3184(SCE22.01c)
            NCA: Noca_0788
            TFU: Tfu_1644
            STP: Strop_2556
            RXY: Rxyl_2001
            RBA: RB2202
            LIL: LA0330
            SYN: slr1772
            GVI: glr1988
            AVA: Ava_1773
            FPS: FP2213(pac)
            DGE: Dgeo_0269
            TTH: TTC1972
            TTJ: TTHA0024
            MSI: Msm_0986
            HMA: rrnB0229(pga-1) rrnB0230(pga-2)
            PTO: PTO1511
            SSO: SSO1460 SSO1638
            SAI: Saci_1777
            MSE: Msed_1174
            PCL: Pcal_1846
            PAS: Pars_1588
STRUCTURES  PDB: 1AI4  1AI5  1AI6  1AI7  1AJN  1AJP  1AJQ  1CP9  1E3A  1FXH  
                 1FXV  1GK0  1GK1  1GK9  1GKF  1GM7  1GM8  1GM9  1H2G  1JX9  
                 1K5Q  1K5S  1K7D  1KEC  1PNK  1PNL  1PNM  2ADV  2AE3  2AE4  
                 2AE5  2IWM  2PVA  3PVA  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.11
            ExPASy - ENZYME nomenclature database: 3.5.1.11
            ExplorEnz - The Enzyme Database: 3.5.1.11
            ERGO genome analysis and discovery system: 3.5.1.11
            BRENDA, the Enzyme Database: 3.5.1.11
            CAS: 9014-06-6
///
ENTRY       EC 3.5.1.12                 Enzyme
NAME        biotinidase;
            amidohydrolase biotinidase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     biotin-amide amidohydrolase
REACTION    biotin amide + H2O = biotin + NH3 [RN:R01076]
ALL_REAC    R01076;
            (other) R01077 R06134
SUBSTRATE   biotin amide [CPD:C01893];
            H2O [CPD:C00001]
PRODUCT     biotin [CPD:C00120];
            NH3 [CPD:C00014]
COMMENT     Also acts on biotin esters.
REFERENCE   1  [PMID:14087327]
  AUTHORS   KNAPPE J, BRUEMMER W, BIEDERBICK K.
  TITLE     [PURIFICATION AND PROPERTIES OF BIOTINIDASE FROM SWINE KIDNEY AND
            LACTOBACILLUS CASEI.]
  JOURNAL   Biochem. Z. 338 (1963) 599-613.
  ORGANISM  Lactobacillus casei [GN:lca]
REFERENCE   2
  AUTHORS   Thoma, R.W. and Peterson, W.H.
  TITLE     The enzymatic degradation of soluble bound biotin.
  JOURNAL   J. Biol. Chem. 210 (1954) 569-579.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00780  Biotin metabolism
ORTHOLOGY   KO: K01435  biotinidase
GENES       HSA: 686(BTD)
            MMU: 26363(Btd)
            RNO: 306262(Btd)
            CFA: 477059(BTD)
            GGA: 420639(BTD)
            DME: Dmel_CG32754
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.12
            ExPASy - ENZYME nomenclature database: 3.5.1.12
            ExplorEnz - The Enzyme Database: 3.5.1.12
            ERGO genome analysis and discovery system: 3.5.1.12
            BRENDA, the Enzyme Database: 3.5.1.12
            CAS: 9025-15-4
///
ENTRY       EC 3.5.1.13                 Enzyme
NAME        aryl-acylamidase;
            AAA-1;
            AAA-2;
            brain acetylcholinesterase (is associated with AAA-2);
            pseudocholinesterase (associated with arylacylamidase)
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     aryl-acylamide amidohydrolase
REACTION    an anilide + H2O = a carboxylate + aniline [RN:R01862]
ALL_REAC    R01862
SUBSTRATE   anilide [CPD:C01402];
            H2O [CPD:C00001]
PRODUCT     carboxylate [CPD:C00060];
            aniline [CPD:C00292]
COMMENT     Also acts on 4-substituted anilides.
REFERENCE   1
  AUTHORS   Nimmo-Smith, R.H.
  TITLE     Aromatic N-deacylation by chick-kidney mitochondria.
  JOURNAL   Biochem. J. 75 (1960) 284-293.
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.13
            ExPASy - ENZYME nomenclature database: 3.5.1.13
            ExplorEnz - The Enzyme Database: 3.5.1.13
            ERGO genome analysis and discovery system: 3.5.1.13
            BRENDA, the Enzyme Database: 3.5.1.13
            CAS: 9025-18-7
///
ENTRY       EC 3.5.1.14                 Enzyme
NAME        aminoacylase;
            dehydropeptidase II;
            histozyme;
            hippuricase;
            benzamidase;
            acylase I;
            hippurase;
            amido acid deacylase;
            L-aminoacylase;
            acylase;
            aminoacylase I;
            L-amino-acid acylase;
            alpha-N-acylaminoacid hydrolase;
            long acyl amidoacylase;
            short acyl amidoacylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-acyl-L-amino-acid amidohydrolase
REACTION    an N-acyl-L-amino acid + H2O = a carboxylate + an L-amino acid
            [RN:R01263]
ALL_REAC    R01263 > R00669
SUBSTRATE   N-acyl-L-amino acid [CPD:C02850];
            H2O [CPD:C00001]
PRODUCT     carboxylate [CPD:C00060];
            L-amino acid [CPD:C00151]
COMMENT     Wide specificity; also hydrolyses dehydropeptides. Used in
            separating D- and L- amino acids
REFERENCE   1  [PMID:14927637]
  AUTHORS   BIRNBAUM SM, LEVINTOW L, KINGSLEY RB, GREENSTEIN JP.
  TITLE     Specificity of amino acid acylases.
  JOURNAL   J. Biol. Chem. 194 (1952) 455-70.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:13061423]
  AUTHORS   FONES WS, LEE M.
  TITLE     Hydrolysis of N-acyl derivatives of alanine and phenylalanine by
            acylase I and carboxypeptidase.
  JOURNAL   J. Biol. Chem. 201 (1953) 847-56.
  ORGANISM  pig [GN:ssc]
REFERENCE   3
  AUTHORS   Park, R.W. and Fox, S.W.
  TITLE     An acylase system related to the utilization of benzoylamino acids
            by Lactobacillus arabinosus.
  JOURNAL   J. Biol. Chem. 235 (1960) 3193-3197.
  ORGANISM  Lactobacillus arabinosus
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K01436  aminoacylase
GENES       HSA: 95(ACY1)
            PTR: 460414(ACY1)
            MMU: 109652(Acy1)
            RNO: 300981(Acy1)
            CFA: 476602(ACY1)
            SSC: 396930(ACY1)
            XLA: 446741(acy1)
            XTR: 496883(acy1)
            DRE: 393970(zgc:55605)
            SPU: 577570(LOC577570)
            DME: Dmel_CG17109 Dmel_CG17110 Dmel_CG6465 Dmel_CG6733
            CEL: C10C5.3(aminoacylase-1) C10C5.4(aminoacylase-1)
                 C10C5.5(aminoacylase-1)
            ATH: AT1G44180 AT1G44820
            OSA: 4340457
            CME: CMA011C
            DDI: DDBDRAFT_0201767
            TET: TTHERM_00475260
            TBR: Tb927.1.3000
            TCR: 506363.70 506363.80 506363.90 506975.30 506975.40
            LMA: LmjF20.1550 LmjF20.1560 LmjF20.1570 LmjF30.1380 LmjF31.1130
            SSN: SSON_1794
            SPE: Spro_1188
            HSO: HS_1434(amaA)
            XCC: XCC3786(amaA)
            XCB: XC_3858
            XCV: XCV3964
            XOO: XOO4187(amaA)
            XOM: XOO_3956(XOO3956)
            PCR: Pcryo_1258
            SFR: Sfri_0302
            SBL: Sbal_0206
            SBM: Shew185_4131
            SHE: Shewmr4_3743
            SHM: Shewmr7_3816
            SHN: Shewana3_3941
            FTU: FTT1191
            FTF: FTF1191
            REU: Reut_A1358
            REH: H16_B0491 H16_B1209
            NIS: NIS_1768
            SUN: SUN_0171
            PPD: Ppro_2428
            DVU: DVU2568
            DVL: Dvul_0678
            DDE: Dde_2667
            SFU: Sfum_1222
            RET: RHE_CH00148(dapE1)
            RLE: RL0157 RL2009
            BME: BMEI0033 BMEI0034 BMEI1827
            OAN: Oant_2455
            RPE: RPE_1861
            RDE: RD1_2828
            SWI: Swit_4303
            GOX: GOX1176 GOX2239
            BAN: BA1392(amaA)
            BAR: GBAA1392(amaA)
            BAA: BA_1294 BA_1916
            BAT: BAS0672 BAS1289
            BCE: BC0701 BC1374 BC3664
            BCA: BCE_0775 BCE_1490(amaA) BCE_3698(hipO)
            BCZ: BCZK0616(amaA) BCZK1263(amaA) BCZK2908(amaA) BCZK3370(amaA)
            BCY: Bcer98_0594 Bcer98_1094 Bcer98_2319 Bcer98_2682
            BTK: BT9727_0616(amaA) BT9727_1261(amaA) BT9727_2973(amaA)
                 BT9727_2974 BT9727_3419
            BTL: BALH_0641(cpsA)
            BLD: BLi04023
            BCL: ABC0022 ABC1615 ABC1855 ABC2804
            BPU: BPUM_0954
            GKA: GK3242 GK3251
            SAB: SAB0042 SAB2206c
            SAA: SAUSA300_0105 SAUSA300_1291 SAUSA300_2276
            SAJ: SaurJH9_0572
            SAH: SaurJH1_0586
            LLM: llmg_0664(amd) llmg_1571(hipO2)
            LPL: lp_3044(amd)
            LDB: Ldb0265
            LCA: LSEI_2899
            CTH: Cthe_2073
            CBE: Cbei_4809
            CKL: CKL_0651(amaA)
            AMT: Amet_1192 Amet_2941 Amet_3737
            DSY: DSY3055
            MTA: Moth_1962
            MSM: MSMEG_1703
            MVA: Mvan_1612
            MGI: Mflv_4826
            MMC: Mmcs_1246
            MKM: Mkms_1263
            MJL: Mjls_1273
            RHA: RHA1_ro06260
            ART: Arth_1133
            NCA: Noca_3542
            FRA: Francci3_0694
            KRA: Krad_3950
            SEN: SACE_6534
            STP: Strop_0833
            BAD: BAD_0995
            FNU: FN0590 FN0702 FN0703 FN1063
            LIL: LA2674
            LIC: LIC11318(amaA)
            SYN: slr1653(ama)
            SYC: syc1257_c(ama)
            SYF: Synpcc7942_0256 Synpcc7942_1971
            TEL: tll2447
            GVI: glr0374
            ANA: alr4934
            AVA: Ava_1059 Ava_2218
            PMN: PMN2A_1190
            PMI: PMT9312_1706
            PME: NATL1_20651
            TER: Tery_1843 Tery_3690
            CHU: CHU_0130(ammA)
            CPH: Cpha266_1330
            RCA: Rcas_2022
            DRA: DR_1711
            DGE: Dgeo_0208
            TTH: TTC0133
            PTO: PTO0772 PTO1086
STRUCTURES  PDB: 1Q7L  1YSJ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.14
            ExPASy - ENZYME nomenclature database: 3.5.1.14
            ExplorEnz - The Enzyme Database: 3.5.1.14
            ERGO genome analysis and discovery system: 3.5.1.14
            BRENDA, the Enzyme Database: 3.5.1.14
            CAS: 9012-37-7
///
ENTRY       EC 3.5.1.15                 Enzyme
NAME        aspartoacylase;
            aminoacylase II;
            N-acetylaspartate amidohydrolase;
            acetyl-aspartic deaminase;
            acylase II
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-acyl-L-aspartate amidohydrolase
REACTION    N-acyl-L-aspartate + H2O = a carboxylate + L-aspartate [RN:R00546]
ALL_REAC    R00546 > R00488 R00526
SUBSTRATE   N-acyl-L-aspartate [CPD:C02715];
            H2O [CPD:C00001]
PRODUCT     carboxylate [CPD:C00060];
            L-aspartate [CPD:C00049]
REFERENCE   1
  AUTHORS   Birnbaum, S.M.
  TITLE     Aminoacylase. Amino acid aminoacylases I and II from hog kidney.
  JOURNAL   Methods Enzymol. 2 (1955) 115-119.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:14927637]
  AUTHORS   BIRNBAUM SM, LEVINTOW L, KINGSLEY RB, GREENSTEIN JP.
  TITLE     Specificity of amino acid acylases.
  JOURNAL   J. Biol. Chem. 194 (1952) 455-70.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
            PATH: map00340  Histidine metabolism
ORTHOLOGY   KO: K01437  aspartoacylase
GENES       HSA: 443(ASPA) 91703(ACY3)
            PTR: 451373(ACY3) 454430(ASPA)
            MMU: 11484(Aspa) 71670(Acy3)
            RNO: 79251(Aspa)
            CFA: 611064(ASPA)
            GGA: 417609(ASPA)
            PPR: PBPRB0781
            MMW: Mmwyl1_1144
            NIS: NIS_0887
            SYN: slr1705(aspA)
            SYW: SYNW1922
            SYD: Syncc9605_0517
            SYE: Syncc9902_1819
            SYG: sync_2389
            SYR: SynRCC307_0357
            ANA: alr3912
            AVA: Ava_1785
            PMA: Pro0251(aspA)
            PMM: PMM0222
            PMT: PMT1537
            PMN: PMN2A_1591
            PMI: PMT9312_0224
            PMC: P9515_02521(aspA)
            PMF: P9303_04021(aspA)
            TER: Tery_4698
STRUCTURES  PDB: 2GU2  2I3C  2Q4Z  2Q51  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.15
            ExPASy - ENZYME nomenclature database: 3.5.1.15
            ExplorEnz - The Enzyme Database: 3.5.1.15
            ERGO genome analysis and discovery system: 3.5.1.15
            BRENDA, the Enzyme Database: 3.5.1.15
            CAS: 9031-86-1
///
ENTRY       EC 3.5.1.16                 Enzyme
NAME        acetylornithine deacetylase;
            acetylornithinase;
            N-acetylornithinase;
            2-N-acetyl-L-ornithine amidohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N2-acetyl-L-ornithine amidohydrolase
REACTION    N2-acetyl-L-ornithine + H2O = acetate + L-ornithine [RN:R00669]
ALL_REAC    R00669
SUBSTRATE   N2-acetyl-L-ornithine [CPD:C00437];
            H2O [CPD:C00001]
PRODUCT     acetate [CPD:C00033];
            L-ornithine [CPD:C00077]
COMMENT     Also hydrolyses N-acetylmethionine.
REFERENCE   1  [PMID:16589307]
  AUTHORS   Vogel HJ.
  TITLE     Path of Ornithine Synthesis in Escherichia Coli.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 39 (1953) 578-83.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:13278318]
  AUTHORS   VOGEL HJ, BONNER DM.
  TITLE     Acetylornithinase of Escherichia coli:  partial purification and
            some properties.
  JOURNAL   J. Biol. Chem. 218 (1956) 97-106.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K01438  acetylornithine deacetylase
GENES       ATH: AT4G17830
            ANI: AN5749.2
            AFM: AFUA_2G00350 AFUA_6G06800
            AOR: AO090003000058
            TBR: Tb927.8.1910
            TCR: 511391.120
            LMA: LmjF07.0270
            EHI: 275.t00003 30.t00003 379.t00005
            ECO: b3957(argE)
            ECJ: JW3929(argE)
            ECE: Z5515(argE)
            ECS: ECs4886
            ECC: c4916(argE)
            ECI: UTI89_C4548(argE)
            ECP: ECP_4170
            ECW: EcE24377A_4496(argE)
            ECX: EcHS_A4191
            STY: STY3753(argE)
            STT: t3504(argE)
            SPT: SPA3958(argE)
            SEC: SC4010(argE)
            STM: STM4120(argE)
            YPE: YPO3928(argE)
            YPK: y0309(argE)
            YPM: YP_3122(argE2)
            YPA: YPA_0096
            YPN: YPN_0041
            YPP: YPDSF_3538
            YPS: YPTB0109(argE)
            YPI: YpsIP31758_0126(argE)
            SFL: SF4034(argE)
            SFX: S3712(argE)
            SFV: SFV_4026(argE)
            SSN: SSON_4130(argE)
            SBO: SBO_3976(argE)
            SDY: SDY_3792(argE)
            ECA: ECA0191(argE)
            PLU: plu4745(argE)
            BUC: BU047(argE)
            BAS: BUsg044(argE)
            SGL: SG2161
            ENT: Ent638_4029
            SPE: Spro_4782
            HDU: HD0566(argE)
            PMU: PM1117(argE)
            MSU: MS0233(argE)
            APL: APL_1085(argE)
            XFA: XF1000
            XFT: PD0292(argE)
            XCC: XCC2246(argE)
            XCB: XC_1872
            XCV: XCV2548(argE)
            XAC: XAC2349(argE)
            XOO: XOO2673(argE)
            XOM: XOO_2519(XOO2519)
            VCH: VC2645
            VCO: VC0395_A2221(argE)
            VVU: VV1_1370
            VVY: VV3003
            VPA: VP2760
            VFI: VF2307
            PAE: PA5206(argE) PA5390
            PAU: PA14_68770(argE) PA14_71180
            PAP: PSPA7_5950(argE) PSPA7_6175(argE1)
            PPU: PP_3571 PP_5186(argE)
            PST: PSPTO_0256(argE-1) PSPTO_0323(argE-2)
            PSB: Psyr_0150(argE) Psyr_0253(argE)
            PSP: PSPPH_0173 PSPPH_0241(argE1) PSPPH_5037(argE2)
            PFL: PFL_3524(argE) PFL_5942(argE)
            PFO: Pfl_3269(argE) Pfl_5420(argE)
            PEN: PSEEN2650 PSEEN5301(argE)
            PAR: Psyc_1768(argE)
            PCR: Pcryo_2049
            ACI: ACIAD3489(argE)
            SDN: Sden_0249
            SFR: Sfri_0190
            ILO: IL0611(argE)
            CPS: CPS_0459(argE1) CPS_2044(argE2)
            PHA: PSHAa2292(argE)
            PAT: Patl_0983
            SDE: Sde_0363
            PIN: Ping_0227
            LPN: lpg1164(argE)
            LPF: lpl1172
            LPP: lpp1166
            MCA: MCA2083(argE)
            NOC: Noc_2607
            AEH: Mlg_0364 Mlg_1722
            HCH: HCH_01029(argE)
            CSA: Csal_0030 Csal_1147 Csal_2386
            AHA: AHA_0592(argE)
            CVI: CV_2379(argE)
            RSO: RSc1641(argE)
            REU: Reut_A1359(argE)
            REH: H16_A1454(argE1) H16_B0459(argE2)
            RME: Rmet_1610 Rmet_1956
            BMA: BMA1493(argE)
            BMV: BMASAVP1_A1990(argE)
            BML: BMA10299_A3317(argE)
            BMN: BMA10247_1262(argE)
            BXE: Bxe_A2314 Bxe_A3463 Bxe_C0681 Bxe_C1312
            BVI: Bcep1808_1872 Bcep1808_5679
            BUR: Bcep18194_A5256 Bcep18194_C6994
            BCN: Bcen_6134
            BCH: Bcen2424_1945
            BAM: Bamb_1933 Bamb_5672
            BPS: BPSL2101
            BPM: BURPS1710b_2514(argE)
            BPL: BURPS1106A_2405(argE)
            BPD: BURPS668_2363(argE)
            BTE: BTH_I2086
            BPE: BP0655 BP3588
            BPA: BPP3324
            BBR: BB3775 BB4791
            POL: Bpro_0411 Bpro_2527
            VEI: Veis_0268
            PCA: Pcar_0275
            PPD: Ppro_0674
            DDE: Dde_2998
            ADE: Adeh_0568
            AFW: Anae109_0611
            MXA: MXAN_1012(argE)
            SAT: SYN_00326
            PUB: SAR11_1327(argE)
            MLO: mll7049 mlr7167
            SME: SMa1836(argE)
            ATU: Atu3398(argE)
            ATC: AGR_L_2847
            RET: RHE_PF00335(argE)
            RLE: pRL120633
            BJA: blr4156 blr5449
            BRA: BRADO3383 BRADO3421
            BBT: BBta_3889 BBta_4285
            RPA: RPA2325 RPA3033(argE)
            RPB: RPB_2506 RPB_3135
            RPC: RPC_2352 RPC_3457 RPC_3492
            RPD: RPD_2938
            NWI: Nwi_1351
            BBK: BARBAKC583_1338(dapE)
            CCR: CC_3631
            SIL: SPO2812(argE-1) SPO3676(argE-2)
            SIT: TM1040_0717
            RSP: RSP_0237(argE) RSP_3695(argE)
            JAN: Jann_3291
            RDE: RD1_3311(argE) RD1_4143(argE)
            PDE: Pden_3458 Pden_4976
            MMR: Mmar10_2601
            ELI: ELI_06245
            MAG: amb2375
            SUS: Acid_5456
            BSU: BG12569(argE)
            BHA: BH1059(argE)
            BAN: BA0493 BA2297
            BAR: GBAA0493 GBAA2297
            BAA: BA_1067 BA_2801
            BAT: BAS0467 BAS2142
            BCE: BC0476 BC2248
            BCA: BCE_0548 BCE_2331
            BCZ: BCZK0406(argE) BCZK2076(argE)
            BTK: BT9727_0410(argE) BT9727_2080(argE)
            BTL: BALH_0431(argE) BALH_2059(argE)
            BLI: BL01428
            BLD: BLi02296(yodQ)
            BCL: ABC0668
            BPU: BPUM_0615(yodQ)
            LLA: L0115(argE)
            LLM: llmg_0536(argE)
            LPL: lp_0488
            TTE: TTE0388(argE)
            MSM: MSMEG_3397
            RHA: RHA1_ro08464 RHA1_ro08621(argE)
            CMI: CMM_1420(argE)
            SEN: SACE_6656
            RBA: RB12133(dapE) RB9116(argE)
            CHU: CHU_3087(argE)
            GFO: GFO_2100(argE)
            MJA: MJ1497(argE)
            HMA: rrnAC0196(argE) rrnAC2095(argE)
            HWA: HQ1368A(argE)
            NPH: NP0200A NP5266A(argE)
            PAB: PAB0723(argE-like)
            PFU: PF1185
            TKO: TK0313
            RCI: RCIX906(argE)
            SSO: SSO0790(argE-1)
            SAI: Saci_2131(argE)
STRUCTURES  PDB: 2F7V  2F8H  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.16
            ExPASy - ENZYME nomenclature database: 3.5.1.16
            ExplorEnz - The Enzyme Database: 3.5.1.16
            ERGO genome analysis and discovery system: 3.5.1.16
            BRENDA, the Enzyme Database: 3.5.1.16
            CAS: 9025-12-1
///
ENTRY       EC 3.5.1.17                 Enzyme
NAME        acyl-lysine deacylase;
            epsilon-lysine acylase;
            6-N-acyl-L-lysine amidohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N6-acyl-L-lysine amidohydrolase
REACTION    N6-acyl-L-lysine + H2O = a carboxylate + L-lysine [RN:R00545]
ALL_REAC    R00545 > R00458;
            (other) R04174
SUBSTRATE   N6-acyl-L-lysine [CPD:C02444];
            H2O [CPD:C00001]
PRODUCT     carboxylate [CPD:C00060];
            L-lysine [CPD:C00047]
REFERENCE   1  [PMID:13445179]
  AUTHORS   PAIK WK, BLOCH-FRANKENTHAL L, BIRNBAUM SM, WINITZ M, GREENSTEIN JP.
  TITLE     epsilon-lysine acylase.
  JOURNAL   Arch. Biochem. Biophys. 69 (1957) 56-66.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.17
            ExPASy - ENZYME nomenclature database: 3.5.1.17
            ExplorEnz - The Enzyme Database: 3.5.1.17
            ERGO genome analysis and discovery system: 3.5.1.17
            BRENDA, the Enzyme Database: 3.5.1.17
            CAS: 9025-11-0
///
ENTRY       EC 3.5.1.18                 Enzyme
NAME        succinyl-diaminopimelate desuccinylase;
            N-succinyl-L-alpha,epsilon-diaminopimelic acid deacylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
REACTION    N-succinyl-LL-2,6-diaminoheptanedioate + H2O = succinate +
            LL-2,6-diaminoheptanedioate [RN:R02734]
ALL_REAC    R02734
SUBSTRATE   N-succinyl-LL-2,6-diaminoheptanedioate [CPD:C04421];
            H2O [CPD:C00001]
PRODUCT     succinate [CPD:C00042];
            LL-2,6-diaminoheptanedioate [CPD:C00666]
REFERENCE   1
  AUTHORS   Kindler, S.H. and Gilvarg, C.
  TITLE     N-Succinyl-L-2,6-diaminopimelic acid deacylase.
  JOURNAL   J. Biol. Chem. 235 (1960) 3532-3535.
  ORGANISM  Escherichia coli [GN:eco], Rhodopseudomonas sphaeroides, Alcaligenes
            faecalis, Azotobacter vinelandii, Micrococcus lysodeikticus
PATHWAY     PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K01439  succinyl-diaminopimelate desuccinylase
GENES       ECO: b2472(dapE)
            ECJ: JW2456(dapE)
            ECE: Z3730(dapE)
            ECS: ECs3334
            ECC: c2999(dapE)
            ECI: UTI89_C2798(dapE) UTI89_C3257(ygeY)
            ECP: ECP_2485
            ECW: EcE24377A_2751(dapE)
            ECX: EcHS_A2602
            STY: STY2721(dapE)
            STT: t0376(dapE)
            SPT: SPA0386(dapE)
            SEC: SC2478(dapE)
            STM: STM2483(dapE)
            YPE: YPO3053(dapE)
            YPK: y1427(dapE)
            YPM: YP_2675(dapE)
            YPA: YPA_2244
            YPN: YPN_1332
            YPS: YPTB2775(dapE)
            YPI: YpsIP31758_1255(dapE)
            SFL: SF2514(dapE)
            SFX: S2665(dapE)
            SFV: SFV_2516(dapE)
            SSN: SSON_2552(dapE)
            SBO: SBO_2488(dapE)
            SDY: SDY_2656(dapE)
            ECA: ECA1291(dapE)
            PLU: plu2722(dapE)
            BUC: BU095(dapE)
            BAS: BUsg087(dapE)
            BAB: bbp089(dapE)
            BCC: BCc_059(dapE)
            WBR: WGLp282(dapE)
            SGL: SG1718
            BFL: Bfl517(dapE)
            BPN: BPEN_534(dapE)
            HIT: NTHI0182(dapE)
            HIP: CGSHiEE_02835
            HIQ: CGSHiGG_03060
            HDU: HD0642(dapE)
            HSO: HS_0578(dapE)
            PMU: PM1022(dapE)
            MSU: MS0674(argE)
            APL: APL_1873(dapE)
            XFA: XF0116
            XFT: PD0088(dapE)
            XCC: XCC1387(dapE)
            XCB: XC_2851
            XCV: XCV1489(dapE)
            XAC: XAC1432(dapE)
            XOO: XOO1989(dapE)
            XOM: XOO_1880(XOO1880)
            VCH: VC2152
            VCO: VC0395_A1734(dapE)
            VVU: VV1_1916
            VVY: VV2500
            VPA: VP2269
            VFI: VF1914
            PPR: PBPRA0844
            PAE: PA1162(dapE)
            PAU: PA14_49380(dapE)
            PAP: PSPA7_4217(dapE)
            PPU: PP_1525(dapE)
            PST: PSPTO_1523(dapE)
            PSB: Psyr_1331
            PSP: PSPPH_3850(dapE)
            PFL: PFL_1165(dapE)
            PFO: Pfl_1088
            PEN: PSEEN4232(dapE)
            PAR: Psyc_0561(dapE)
            PCR: Pcryo_0549
            ACI: ACIAD0791(dapE)
            SON: SO_2471(dapE)
            SDN: Sden_1814
            SFR: Sfri_1765
            SAZ: Sama_1647
            SBL: Sbal_2367
            SLO: Shew_1862
            SHE: Shewmr4_1857
            SHM: Shewmr7_2121
            SHN: Shewana3_1912
            SHW: Sputw3181_1888
            ILO: IL1455(dapE)
            CPS: CPS_3179(dapE)
            PHA: PSHAa1331(dapE)
            PAT: Patl_2192
            SDE: Sde_2607
            MAQ: Maqu_2554
            CBU: CBU_0666(dapE)
            CBD: COXBU7E912_0676(dapE)
            LPN: lpg0887(dapE)
            LPF: lpl0918(dapE)
            LPP: lpp0948(dapE)
            MCA: MCA1553(dapE)
            TCX: Tcr_1291
            NOC: Noc_2126
            AEH: Mlg_1868
            HCH: HCH_05260(dapE)
            CSA: Csal_0557
            ABO: ABO_1137(dapE)
            AHA: AHA_1478(dapE)
            CRP: CRP_017
            VOK: COSY_0260(dapE)
            NME: NMB1530
            NMA: NMA1730(dapE)
            NMC: NMC1459(dapE)
            NGO: NGO0991
            CVI: CV_1456(dapE)
            RSO: RSc1390(dapE)
            REU: Reut_A1895
            REH: H16_A2069(dapE)
            RME: Rmet_1420
            BMA: BMA1568(dapE)
            BMV: BMASAVP1_A2071(dapE)
            BML: BMA10299_A3241(dapE)
            BMN: BMA10247_1343(dapE)
            BXE: Bxe_A1668
            BUR: Bcep18194_A5341
            BCN: Bcen_6045
            BCH: Bcen2424_2032
            BAM: Bamb_2064
            BPS: BPSL2171(dapE)
            BPM: BURPS1710b_2596(dapE)
            BPL: BURPS1106A_2507(dapE)
            BPD: BURPS668_2451(dapE)
            BTE: BTH_I2014(dapE)
            BPE: BP1763(dapE)
            BPA: BPP1994(dapE)
            BBR: BB2182(dapE)
            RFR: Rfer_2044
            POL: Bpro_1994
            MPT: Mpe_A1804
            HAR: HEAR1321(dapE)
            MMS: mma_2072
            NEU: NE0108(dapE)
            NET: Neut_2234
            NMU: Nmul_A1852
            EBA: ebA6388
            AZO: azo2007(dapE)
            DAR: Daro_1724
            TBD: Tbd_1271
            MFA: Mfla_1869
            HPY: HP0212
            HPA: HPAG1_0213
            HHE: HH1805(dapE)
            HAC: Hac_1507(dapE)
            WSU: WS0588
            TDN: Tmden_1445
            CJE: Cj1048c(dapE)
            CJR: CJE1192(dapE)
            CJJ: CJJ81176_1069(dapE)
            CJU: C8J_0989(dapE)
            CJD: JJD26997_0688(dapE)
            CFF: CFF8240_0627(dapE)
            CCV: CCV52592_0990(dapE)
            CHA: CHAB381_0240(dapE)
            CCO: CCC13826_0246(dapE)
            ABU: Abu_1150(dapE)
            NIS: NIS_1237(dapE)
            SUN: SUN_0489(dapE)
            DVU: DVU1827
            DDE: Dde_1810
            BBA: Bd0129(dapE)
            MXA: MXAN_6777
            SAT: SYN_02795
            RPR: RP874
            RTY: RT0865(dapE)
            RCO: RC1347(dapE)
            RFE: RF_1376(dapE)
            RBE: RBE_1420(dapE)
            OTS: OTBS_0555(dapE)
            WOL: WD0788(dapE)
            WBM: Wbm0568
            AMA: AM1347(dapE)
            ERU: Erum0940(dapE)
            ERW: ERWE_CDS_00910(dapE)
            ERG: ERGA_CDS_00870(dapE)
            ECN: Ecaj_0094
            ECH: ECH_0144(dapE)
            PUB: SAR11_0462(dapE)
            MLO: mlr1185 mlr4849
            MES: Meso_0389
            SME: SMc01096(dapE)
            ATU: Atu0370(dapE)
            ATC: AGR_C_647
            RET: RHE_CH00417(dapE2)
            RLE: RL0436(dapE)
            BME: BMEII0268
            BMF: BAB2_0993(dapE)
            BMS: BRA1031(dapE)
            BMB: BruAb2_0971(dapE)
            BOV: BOV_A0972(dapE)
            BJA: blr8106(dapE)
            BRA: BRADO0774(dapE)
            BBT: BBta_7333(dapE)
            RPA: RPA0624(dapE)
            RPB: RPB_0676
            RPC: RPC_0809
            RPD: RPD_0077
            RPE: RPE_0653
            NWI: Nwi_3068
            NHA: Nham_3697
            BHE: BH00520(dapE)
            BQU: BQ00460(dapE)
            BBK: BARBAKC583_1338(dapE)
            CCR: CC_0275
            SIL: SPO3332(dapE)
            SIT: TM1040_2996 TM1040_3116
            RSP: RSP_1128(dapE) RSP_1758
            JAN: Jann_0354
            RDE: RD1_0090(dapE) RD1_0185(dapE)
            MMR: Mmar10_0449
            ZMO: ZMO1632(dapE)
            NAR: Saro_0581
            SAL: Sala_2019
            ELI: ELI_10605
            GOX: GOX1832
            GBE: GbCGDNIH1_0687
            RRU: Rru_A3480
            MAG: amb3874
            MGM: Mmc1_0046
            BSU: BG13867(ytjP)
            BHA: BH3272
            BAA: BA_5374
            BAT: BAS4600
            BCE: BC4702
            BCA: BCE_4846
            BTK: BT9727_4436
            BLI: BL00035(ytjP)
            BLD: BLi03151(ytjP)
            SAU: SA1572 SA1814
            SAV: SAV1751 SAV2006
            SAM: MW1694 MW1943
            SAR: SAR1836 SAR2109
            SAS: SAS1677 SAS1926
            SAC: SACOL1801
            SAB: SAB1611c SAB1877
            SAA: SAUSA300_1976
            SAO: SAOUHSC_02244
            SAJ: SaurJH9_2064
            SAH: SaurJH1_2101
            SEP: SE0216 SE1424
            SER: SERP1310 SERP2364
            SHA: SH0132 SH1171
            SSP: SSP1012
            LMO: lmo1620
            LMF: LMOf2365_1642
            LIN: lin1661
            LLA: L59867(pepV)
            LLM: llmg_1706(pepV)
            SPR: spr0148(dapE)
            STC: str1127(pepV)
            SSA: SSA_0589(dapE)
            SGO: SGO_0459
            LPL: lp_1923(dapE1) lp_2855(dapE2)
            LSA: LSA0220_c(dapE)
            LSL: LSL_0133 LSL_1467
            LBR: LVIS_0253 LVIS_0864 LVIS_2269
            LCA: LSEI_1175
            LRE: Lreu_0190
            CAC: CAC2723
            CPE: CPE1211
            CNO: NT01CX_1079
            AMT: Amet_0039
            CHY: CHY_2216
            DSY: DSY1623
            TTE: TTE1746(argE2)
            POY: PAM290(argE)
            MTU: Rv1202(dapE)
            MTC: MT1240(dapE)
            MBO: Mb1234(dapE)
            MBB: BCG_1262(dapE)
            MLE: ML1059(dapE)
            MPA: MAP2574c(dapE)
            MAV: MAV_1349(dapE)
            MSM: MSMEG_5103(dapE)
            MMC: Mmcs_4012
            CGL: NCgl1064(cgl1109)
            CGB: cg1260(dapE)
            CEF: CE1166(dapE)
            CDI: DIP0982(dapE)
            CJK: jk1390(dapE)
            NFA: nfa47410(dapE)
            RHA: RHA1_ro05964
            SCO: SCO5139(dapE)
            SMA: SAV3125(dapE)
            LXX: Lxx09050(dapE)
            CMI: CMM_1178(dapE)
            AAU: AAur_2789(dapE)
            PAC: PPA0636
            TFU: Tfu_0495
            FRA: Francci3_3855
            FAL: FRAAL4657(dapE-like) FRAAL6123(dapE)
            SEN: SACE_1018(dapE)
            BLO: BL0875 BL1280(dapE)
            BAD: BAD_0238(dapE)
            FNU: FN0278
            RBA: RB12133(dapE)
            TDE: TDE0068
            AAE: aq_547(dapE)
            TMA: TM1666
            MJA: MJ0457
            MMP: MMP1398(dapE)
            HWA: HQ1512A(dapE)
            TAC: Ta0934m
            TVO: TVN1079
            PTO: PTO1100
            PHO: PH0265 PH1288
            PAB: PAB0581
            PFU: PF2048
            TKO: TK1466 TK1781
            APE: APE_0632.1 APE_1917
            SSO: SSO1007(argE-2) SSO1538(dapE)
            STO: ST1529 ST2549
            SAI: Saci_1645(dapE)
            PAI: PAE2335
            NEQ: NEQ511
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.18
            ExPASy - ENZYME nomenclature database: 3.5.1.18
            ExplorEnz - The Enzyme Database: 3.5.1.18
            ERGO genome analysis and discovery system: 3.5.1.18
            BRENDA, the Enzyme Database: 3.5.1.18
            CAS: 9024-94-6
///
ENTRY       EC 3.5.1.19                 Enzyme
NAME        nicotinamidase;
            nicotinamide deaminase;
            nicotinamide amidase;
            YNDase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     nicotinamide amidohydrolase
REACTION    nicotinamide + H2O = nicotinate + NH3 [RN:R01268]
ALL_REAC    R01268;
            (other) R06134
SUBSTRATE   nicotinamide [CPD:C00153];
            H2O [CPD:C00001]
PRODUCT     nicotinate [CPD:C00253];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Petrack, B., Greengard, P., Craston, A. and Sheppy, F.
  TITLE     Nicotinamide deamidase from mammalian liver.
  JOURNAL   J. Biol. Chem. 240 (1965) 1725-1730.
  ORGANISM  rabbit, rat [GN:rno], pigeon
REFERENCE   2
  AUTHORS   Sarma, D.S.R., Rajalakshmi, S. and Sarma, S.
  TITLE     Studies on the enzymes involved in nicotinamide adenine dinucleotide
            metabolism in Aspergillus niger.
  JOURNAL   Biochim. Biophys. Acta 81 (1964) 311-322.
  ORGANISM  Aspergillus niger
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K01440  nicotinamidase
GENES       SPU: 759419(LOC759419)
            SCE: YGL037C(PNC1)
            AGO: AGOS_AFR466C
            PIC: PICST_33075(PNC1)
            CGR: CAGL0A01716g
            CNE: CNA07780
            ECO: b1768(pncA)
            ECJ: JW1757(pncA)
            ECE: Z2802(ydjB)
            ECS: ECs2475
            ECC: c2172(ydjB)
            ECI: UTI89_C1964(ydjB)
            ECP: ECP_1716
            ECV: APECO1_837(ydjB)
            ECW: EcE24377A_1992(pncA)
            ECX: EcHS_A1852
            STY: STY1821(pncA)
            STT: t1172(pncA)
            SPT: SPA1551(pncA)
            SEC: SC1315(pncA)
            STM: STM1293(pncA)
            YPE: YPO2160(pncA)
            YPK: y2162
            YPM: YP_1960(pncA)
            YPA: YPA_1517
            YPN: YPN_1626
            YPP: YPDSF_0974
            YPS: YPTB2086(pncA)
            YPI: YpsIP31758_1984(pncA)
            SFL: SF1455(ydjB)
            SFX: S1570(ydjB)
            SFV: SFV_1449(ydjB)
            SSN: SSON_1387(ydjB)
            SBO: SBO_1319(ydjB)
            SDY: SDY_1505(ydjB)
            ECA: ECA2341(pncA)
            PLU: plu2555(pncA)
            ENT: Ent638_1679
            SPE: Spro_2724
            XFT: PD1310(pncA)
            VCH: VCA0712
            VCO: VC0395_0651(pncA)
            VVU: VV1_2374
            VVY: VV1967
            VPA: VPA0307
            PPR: PBPRA3449(pncA)
            PAE: PA4918
            PAU: PA14_64950(pncA)
            PST: PSPTO_3295(pncA)
            PSB: Psyr_3125
            PSP: PSPPH_3038(pncA)
            PFL: PFL_2466(pncA)
            PFO: Pfl_2887
            PEN: PSEEN2059
            ACI: ACIAD3584(pncA)
            ILO: IL0104
            PIN: Ping_1729
            LPN: lpg0271(pncA)
            LPF: lpl0323(pncA)
            LPP: lpp0345(pncA)
            FTH: FTH_0920
            NOC: Noc_0271
            AEH: Mlg_1258
            HHA: Hhal_1744
            CSA: Csal_2870
            AHA: AHA_4211
            NME: NMB2157
            NMA: NMA0244(pncA)
            NMC: NMC2135(pncA)
            NGO: NGO1933
            CVI: CV_1264(pncA)
            RSO: RSc1760(pncA)
            REU: Reut_A1406
            REH: H16_A1527(pncA)
            RME: Rmet_1854
            BMA: BMA1437(pncA)
            BMV: BMASAVP1_A1927(pncA)
            BML: BMA10299_A3377(pncA)
            BMN: BMA10247_1200(pncA)
            BVI: Bcep1808_1837
            BUR: Bcep18194_A5206
            BCN: Bcen_6174
            BCH: Bcen2424_1905
            BAM: Bamb_1893
            BPS: BPSL1425
            BPM: BURPS1710b_2454(pncA)
            BPL: BURPS1106A_2332(pncA)
            BPD: BURPS668_2293(pncA)
            BTE: BTH_I2143
            BPE: BP3506
            BPA: BPP2513
            BBR: BB1959
            RFR: Rfer_0828
            VEI: Veis_0861
            NMU: Nmul_A0906
            GSU: GSU2290
            GME: Gmet_2374
            PCA: Pcar_1461
            ADE: Adeh_1318
            AFW: Anae109_2445
            SAT: SYN_01201
            MLO: mlr4882
            SME: SMc02275(pncA)
            SMD: Smed_0199
            ATU: Atu2066(pncA)
            ATC: AGR_C_3739
            RET: RHE_CH02821(pncA)
            RLE: RL3279(pncA)
            BME: BMEI0546
            BMF: BAB1_1484
            BMS: BR1464(pncA)
            BMB: BruAb1_1459(pncA)
            OAN: Oant_1709
            BJA: bll0677(pncA) bll4549(pncA)
            BRA: BRADO2106(pncA)
            BBT: BBta_0189 BBta_2415(pncA)
            BHE: BH11400(pncA)
            BQU: BQ09020(pncA)
            XAU: Xaut_0349
            SIL: SPO0093(pncA)
            SIT: TM1040_3430
            RSP: RSP_1368(pncA)
            RSH: Rsph17029_0036
            RSQ: Rsph17025_0026
            JAN: Jann_0014
            RDE: RD1_0585(pncA)
            PDE: Pden_0851
            ACR: Acry_0085
            RRU: Rru_A3002
            MGM: Mmc1_1211
            BCZ: BCZK0017(pncA) BCZK2041(pncA)
            BTK: BT9727_2043(pncA)
            BTL: BALH_0017(pncA)
            BCL: ABC3111
            BPU: BPUM_2845
            SAB: SAB1855
            LMO: lmo2571
            LMF: LMOf2365_2544
            LIN: lin2716
            LWE: lwe2522
            SPZ: M5005_Spy_1511
            SPH: MGAS10270_Spy1579
            SPI: MGAS10750_Spy1571
            SPJ: MGAS2096_Spy1538
            SPK: MGAS9429_Spy1512
            SPA: M6_Spy1504
            SPB: M28_Spy1500
            SSA: SSA_0567
            LPL: lp_2612
            LSA: LSA1766
            LSL: LSL_1510(pncA)
            LDB: Ldb0322(pncA)
            LBR: LVIS_0241
            LCA: LSEI_2767
            CTC: CTC00699
            CBA: CLB_1171
            CBH: CLC_1183
            CBF: CLI_1220
            MMY: MSC_1020(pncA) MSC_1045(pncA)
            MCP: MCAP_0859(pncA)
            MFL: Mfl340
            MTU: Rv2043c(pncA)
            MTC: MT2103(pncA)
            MBO: Mb2069c(pncA)
            MPA: MAP1774c(pncA)
            MSM: MSMEG_6506
            MMC: Mmcs_5114
            CGL: NCgl2401(cgl2487)
            CGB: cg2734(pncA)
            CEF: CE2385
            CJK: jk1464(pncA)
            NFA: nfa10840(pncA)
            SCO: SCO2918(SCE19A.18)
            SMA: SAV5157(pncA)
            TWH: TWT692(pncA)
            TWS: TW711(pncA)
            AAU: AAur_2576
            PAC: PPA0993
            TFU: Tfu_2374
            FAL: FRAAL2123(pncA)
            SEN: SACE_1199(pncA) SACE_2641(pncA)
            BLO: BL0897(pncA)
            TPA: TP0696
            PGI: PG0678
            SRU: SRU_1457(pncA)
            GFO: GFO_3188(pncA)
            AAE: aq_994(pncA)
            TMA: TM0475
            MKA: MK0504
            HWA: HQ1060A(entB)
            NPH: NP1274A(entB_1)
            PAB: PAB1720
            PFU: PF1105(pxnC)
            TKO: TK1650
STRUCTURES  PDB: 1ILW  1IM5  2H0R  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.19
            ExPASy - ENZYME nomenclature database: 3.5.1.19
            ExplorEnz - The Enzyme Database: 3.5.1.19
            ERGO genome analysis and discovery system: 3.5.1.19
            BRENDA, the Enzyme Database: 3.5.1.19
            CAS: 9033-32-3
///
ENTRY       EC 3.5.1.20                 Enzyme
NAME        citrullinase;
            citrulline ureidase;
            citrulline hydrolase;
            L-citrulline 5-N-carbamoyldihydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     L-citrulline N5-carbamoyldihydrolase
REACTION    L-citrulline + H2O = L-ornithine + CO2 + NH3 [RN:R00665]
ALL_REAC    R00665;
            (other) R06134
SUBSTRATE   L-citrulline [CPD:C00327];
            H2O [CPD:C00001]
PRODUCT     L-ornithine [CPD:C00077];
            CO2 [CPD:C00011];
            NH3 [CPD:C00014]
REFERENCE   1  [PMID:6075416]
  AUTHORS   Hill DL, Chambers P.
  TITLE     The biosynthesis of proline by Tetrahymena pyriformis.
  JOURNAL   Biochim. Biophys. Acta. 148 (1967) 435-47.
  ORGANISM  Tetrahymena pyriformis
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.20
            ExPASy - ENZYME nomenclature database: 3.5.1.20
            ExplorEnz - The Enzyme Database: 3.5.1.20
            ERGO genome analysis and discovery system: 3.5.1.20
            BRENDA, the Enzyme Database: 3.5.1.20
            CAS: 59088-17-4
///
ENTRY       EC 3.5.1.21                 Enzyme
NAME        N-acetyl-beta-alanine deacetylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-acetyl-beta-alanine amidohydrolase
REACTION    N-acetyl-beta-alanine + H2O = acetate + beta-alanine [RN:R00909]
ALL_REAC    R00909
SUBSTRATE   N-acetyl-beta-alanine [CPD:C01073];
            H2O [CPD:C00001]
PRODUCT     acetate [CPD:C00033];
            beta-alanine [CPD:C00099]
REFERENCE   1
  AUTHORS   Fujimoto, D., Koyama, T. and Tamiya, N.
  TITLE     N-Acetyl-beta-alanine deacetylase in hog kidney.
  JOURNAL   Biochim. Biophys. Acta 167 (1968) 407-413.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00410  beta-Alanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.21
            ExPASy - ENZYME nomenclature database: 3.5.1.21
            ExplorEnz - The Enzyme Database: 3.5.1.21
            ERGO genome analysis and discovery system: 3.5.1.21
            BRENDA, the Enzyme Database: 3.5.1.21
            CAS: 37289-04-6
///
ENTRY       EC 3.5.1.22                 Enzyme
NAME        pantothenase;
            pantothenate hydrolase;
            pantothenate amidohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     (R)-pantothenate amidohydrolase
REACTION    (R)-pantothenate + H2O = (R)-pantoate + beta-alanine [RN:R02474]
ALL_REAC    R02474
SUBSTRATE   (R)-pantothenate [CPD:C00864];
            H2O [CPD:C00001]
PRODUCT     (R)-pantoate [CPD:C00522];
            beta-alanine [CPD:C00099]
REFERENCE   1  [PMID:5940928]
  AUTHORS   Nurmikko V, Salo E, Hakola H, Makinen K, Snell EE.
  TITLE     The bacterial degradation of pantothenic acid. II. Pantothenate
            hydrolase.
  JOURNAL   Biochemistry. 5 (1966) 399-402.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00770  Pantothenate and CoA biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.22
            ExPASy - ENZYME nomenclature database: 3.5.1.22
            ExplorEnz - The Enzyme Database: 3.5.1.22
            ERGO genome analysis and discovery system: 3.5.1.22
            BRENDA, the Enzyme Database: 3.5.1.22
            CAS: 9076-90-8
///
ENTRY       EC 3.5.1.23                 Enzyme
NAME        ceramidase;
            acylsphingosine deacylase;
            glycosphingolipid ceramide deacylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-acylsphingosine amidohydrolase
REACTION    N-acylsphingosine + H2O = a carboxylate + sphingosine [RN:R01493]
ALL_REAC    R01493 > R01494;
            (other) R06518 R06528
SUBSTRATE   N-acylsphingosine [CPD:C00195];
            H2O [CPD:C00001]
PRODUCT     carboxylate [CPD:C00060];
            sphingosine [CPD:C00319]
REFERENCE   1  [PMID:5775951]
  AUTHORS   Nilsson A.
  TITLE     The presence of spingomyelin- and ceramide-cleaving enzymes in the
            small intestinal tract.
  JOURNAL   Biochim. Biophys. Acta. 176 (1969) 339-47.
REFERENCE   2  [PMID:5805303]
  AUTHORS   Yavin E, Gatt S.
  TITLE     Enzymatic hydrolysis of sphingolipids. 8. Further purification and
            properties of rat brain ceramidase.
  JOURNAL   Biochemistry. 8 (1969) 1692-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00600  Sphingolipid metabolism
ORTHOLOGY   KO: K01441  N-acylsphingosine amidohydrolase
GENES       HSA: 427(ASAH1)
            PTR: 464022(ASAH1)
            MMU: 11886(Asah1)
            RNO: 84431(Asah1)
            CFA: 482897(ASAH1)
            GGA: 422727(ASAH1) 423679(ASAH2)
            DRE: 493602(asah2) 550266(zgc:110285)
            DME: Dmel_CG13969(bwa) Dmel_CG1471(CDase)
            AFM: AFUA_1G06470
            UMA: UM00367.1
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.23
            ExPASy - ENZYME nomenclature database: 3.5.1.23
            ExplorEnz - The Enzyme Database: 3.5.1.23
            ERGO genome analysis and discovery system: 3.5.1.23
            BRENDA, the Enzyme Database: 3.5.1.23
            CAS: 37289-06-8
///
ENTRY       EC 3.5.1.24                 Enzyme
NAME        choloylglycine hydrolase;
            glycocholase;
            bile salt hydrolase;
            choloyltaurine hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oylglycine
            amidohydrolase
REACTION    3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oylglycine + H2O =
            3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
            [RN:R05835]
ALL_REAC    R05835;
            (other) R02797 R03975 R03977 R04486 R04487
SUBSTRATE   3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oylglycine
            [CPD:C01921];
            H2O [CPD:C00001]
PRODUCT     3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate [CPD:C00695];
            glycine [CPD:C00037]
COMMENT     Also acts on the 3alpha,12alpha-dihydroxy-derivative, and on
            choloyl-taurine.
REFERENCE   1  [PMID:6016335]
  AUTHORS   Nair PP, Gordon M, Reback J.
  TITLE     The enzymatic cleavage of the carbon-nitrogen bond in 3-alpha,
            7-alpha, 12-alpha-trihydroxy-5-beta-cholan-24-oylglycine.
  JOURNAL   J. Biol. Chem. 242 (1967) 7-11.
  ORGANISM  Clostridium perfringens
REFERENCE   2  [PMID:10993]
  AUTHORS   Stellwag EJ, Hylemon PB.
  TITLE     Purification and characterization of bile salt hydrolase from
            Bacteroides fragilis subsp. fragilis.
  JOURNAL   Biochim. Biophys. Acta. 452 (1976) 165-76.
  ORGANISM  Bacteroides fragilis
PATHWAY     PATH: map00120  Bile acid biosynthesis
ORTHOLOGY   KO: K01442  choloylglycine hydrolase
GENES       VFI: VFA0241
            PFL: PFL_3019
            ACI: ACIAD2026
            SDN: Sden_0442
            LPN: lpg0804
            LPF: lpl0837
            LPP: lpp0866
            FTU: FTT1234
            FTF: FTF1234
            FTW: FTW_0710
            FTL: FTL_0710 FTL_1089
            FTH: FTH_0713
            FTN: FTN_1252
            BPE: BP0474
            BPA: BPP3319
            BBR: BB3770
            SUN: SUN_1118 SUN_2455
            BBA: Bd0665
            DPS: DP1182
            MLO: mlr8141
            ATU: Atu4586
            ATC: AGR_L_573
            RLE: RL1145
            BME: BMEI0543
            BMF: BAB1_1488
            BMS: BR1468
            BMB: BruAb1_1463
            RPA: RPA1879
            RPB: RPB_3497
            RPC: RPC_3412
            RPD: RPD_1956
            RPE: RPE_3554
            NWI: Nwi_0876
            XAU: Xaut_2364
            BAN: BA3898
            BAR: GBAA3898
            BAA: BA_4369
            BAT: BAS3611
            BCE: BC1015
            BCA: BCE_3801
            BCZ: pE33L466_0332
            BTK: BT9727_3508(cbaH)
            BTL: BALH_3395
            SAB: SAB0214
            SAA: SAUSA300_0269
            LMO: lmo2067
            LMF: LMOf2365_2098(cbh)
            LLM: llmg_1422(pacA)
            LPL: lp_0067(bsh2) lp_2572(bsh4) lp_3362(bsh3) lp_3536(bsh1)
            LJO: LJ0056 LJ1147 LJ1412
            LAC: LBA0892(bshA) LBA1078(bshB)
            LSA: LSA0210
            LSL: LSL_0518 LSL_1801
            LBR: LVIS_1801 LVIS_1962 LVIS_2132
            LCA: LSEI_0412
            LGA: LGAS_0054
            LRE: Lreu_0730
            EFA: EF0521
            CPE: CPE0709(cbh)
            CPF: CPF_0705 CPF_1348
            CPR: CPR_1155
            DSY: DSY3579
            MSM: MSMEG_5454
            BLO: BL0796
            BAD: BAD_0856
            SYG: sync_1125
            BFR: BF3794
            BFS: BF1508(cbh)
            CHU: CHU_2387
            MST: Msp_0760
STRUCTURES  PDB: 2BJF  2BJG  2HEZ  2HF0  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.24
            ExPASy - ENZYME nomenclature database: 3.5.1.24
            ExplorEnz - The Enzyme Database: 3.5.1.24
            ERGO genome analysis and discovery system: 3.5.1.24
            BRENDA, the Enzyme Database: 3.5.1.24
            CAS: 37289-07-9
///
ENTRY       EC 3.5.1.25                 Enzyme
NAME        N-acetylglucosamine-6-phosphate deacetylase;
            acetylglucosamine phosphate deacetylase;
            acetylaminodeoxyglucosephosphate acetylhydrolase;
            2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-acetyl-D-glucosamine-6-phosphate amidohydrolase
REACTION    N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate
            + acetate [RN:R02059]
ALL_REAC    R02059;
            (other) R05168
SUBSTRATE   N-acetyl-D-glucosamine 6-phosphate [CPD:C00357];
            H2O [CPD:C00001]
PRODUCT     D-glucosamine 6-phosphate [CPD:C00352];
            acetate [CPD:C00033]
REFERENCE   1  [PMID:4861885]
  AUTHORS   White RJ, Pasternak CA.
  TITLE     The purification and properties of N-acetylglucosamine 6-phosphate
            deacetylase from Escherichia coli.
  JOURNAL   Biochem. J. 105 (1967) 121-5.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:8987551]
  AUTHORS   Yamano N, Matsushita Y, Kamada Y, Fujishima S, Arita M.
  TITLE     Purification and characterization of N-acetylglucosamine 6-phosphate
            deacetylase with activity against N-acetylglucosamine from Vibrio
            cholerae non-O1.
  JOURNAL   Biosci. Biotechnol. Biochem. 60 (1996) 1320-3.
  ORGANISM  Vibrio cholerae [GN:vch]
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K01443  N-acetylglucosamine-6-phosphate deacetylase
            KO: K02079  N-acetylgalactosamine-6-phosphate deacetylase
GENES       HSA: 51005(AMDHD2)
            PTR: 453838(AMDHD2)
            MMU: 245847(Amdhd2)
            RNO: 302972(RGD1304601)
            CFA: 479876(AMDHD2)
            GGA: 770465(AMDHD2)
            DRE: 402981(zgc:77775)
            SPU: 577808(LOC577808) 758744(LOC758744)
            DME: Dmel_CG17065
            CEL: F59B2.3
            PIC: PICST_48829(NAG2)
            ANI: AN1428.2
            AFM: AFUA_1G00450 AFUA_8G04100
            AOR: AO090103000023
            TCR: 506507.10
            LMA: LmjF36.0040
            ECO: b0677(nagA) b3135(agaA)
            ECJ: JW0663(nagA)
            ECE: Z0824(nagA) Z4489
            ECS: ECs0707 ECs4015
            ECC: c0752(nagA) c3892
            ECI: UTI89_C0671(nagA) UTI89_C3566
            ECP: ECP_0689 ECP_3227
            ECV: APECO1_1395(nagA) APECO1_3292
            ECW: EcE24377A_0702(nagA1) EcE24377A_3617(nagA2)
            ECX: EcHS_A0721 EcHS_A3327
            STY: STY0721(nagA)
            STT: t2192(nagA)
            SPT: SPA2058(nagA)
            SEC: SC0704(nagA)
            STM: STM0683(nagA)
            YPE: YPO0838 YPO2626(nagA)
            YPK: y1201(nagA) y3223
            YPM: YP_1087(nagA1) YP_3534(nagA2)
            YPA: YPA_0432 YPA_2471
            YPN: YPN_1112 YPN_3040
            YPP: YPDSF_0676 YPDSF_2627
            YPS: YPTB1118(nagA) YPTB3082
            YPI: YpsIP31758_2910(nagA)
            SFL: SF0616(nagA) SF3172(agaA)
            SFX: S0627(nagA) S3387(agaA)
            SFV: SFV_0654(nagA)
            SSN: SSON_0631(nagA)
            SBO: SBO_0539(nagA)
            SDY: SDY_0611(nagA)
            ECA: ECA1325(nagA)
            PLU: plu1316(nagA)
            SGL: SG0815
            ENT: Ent638_1192
            SPE: Spro_1226
            BFL: Bfl322(nagA)
            BPN: BPEN_330(nagA)
            HIT: NTHI0226(nagA)
            HIP: CGSHiEE_02590(nagA)
            HDU: HD1845(nagA)
            HSO: HS_1026(nagA)
            PMU: PM0874(nagA)
            MSU: MS2204(nagA)
            APL: APL_1756(nagA)
            ASU: Asuc_1103
            XFA: XF1465
            XFT: PD0684(nagA)
            XCC: XCC3410(nagA)
            XCB: XC_0754
            XCV: XCV0771(nagA)
            XAC: XAC0715(nagA)
            XOO: XOO3915(nagA)
            XOM: XOO_3695(XOO3695)
            VCH: VC0994 VC1783
            VCO: VC0395_A0515(nagA-1) VC0395_A1380(nagA-2)
            VVU: VV1_0180 VV2_0736 VV2_1018
            VVY: VV1011 VVA1206 VVA1510
            VPA: VP0829
            VFI: VF0665 VF0807 VFA0999
            PPR: PBPRA1030 PBPRB0147(nagA) PBPRB0765 PBPRB1042
            PAE: PA3758
            PAU: PA14_15820(nagA)
            PAP: PSPA7_1360(nagA)
            PFL: PFL_1081(nagA)
            PFO: Pfl_1006
            PEN: PSEEN4380(nagA)
            SON: SO_3505(nagA)
            SDN: Sden_2704
            SAZ: Sama_0946 Sama_1198
            SBL: Sbal_1086
            SBM: Shew185_1146
            SLO: Shew_1117
            SPC: Sputcn32_1078
            SSE: Ssed_1213
            SPL: Spea_1102 Spea_1523
            SHE: Shewmr4_2531 Shewmr4_2933
            SHM: Shewmr7_2598 Shewmr7_3015
            SHN: Shewana3_2697 Shewana3_3112
            SHW: Sputw3181_3087
            CPS: CPS_1027(nagA)
            PHA: PSHAb0157(nagA)
            PAT: Patl_4174
            SDE: Sde_3040
            PIN: Ping_0489
            FTU: FTT1168c(nagA)
            FTF: FTF1168c(nagA)
            FTW: FTW_1211(nagA)
            FTL: FTL_0786
            FTH: FTH_0780(nagA)
            FTA: FTA_0831(nagA)
            FTN: FTN_1149(nagA)
            HCH: HCH_06986(nagA)
            MMW: Mmwyl1_1654
            AHA: AHA_0806(nagA-1) AHA_1525(nagA-2)
            DNO: DNO_0309(nagA)
            CVI: CV_0556(nagA)
            REH: H16_A0314(nagA)
            BMA: BMA3168.1(nagA)
            BMV: BMASAVP1_A0139(nagA)
            BML: BMA10299_A1449(nagA)
            BMN: BMA10247_2877(nagA)
            BXE: Bxe_A4155
            BVI: Bcep1808_2928
            BUR: Bcep18194_A6154
            BCN: Bcen_2211
            BCH: Bcen2424_2824
            BAM: Bamb_2884
            BPS: BPSL0496
            BPM: BURPS1710b_0721
            BPL: BURPS1106A_0552(nagA)
            BPD: BURPS668_0535(nagA)
            BTE: BTH_I0447(nagA)
            VEI: Veis_1395
            SUN: SUN_2245(nagA)
            MLO: mll4766
            MES: Meso_2863
            SME: SMc02878(nagA)
            SMD: Smed_3410
            ATU: Atu2608(nagA)
            ATC: AGR_C_4726
            RET: RHE_CH04037(nagA)
            RLE: RL4602(nagA)
            BME: BMEII0385
            BMF: BAB2_0324
            BMS: BRA0911(nagA)
            BMB: BruAb2_0322(nagA)
            BOV: BOV_A0854(nagA)
            OAN: Oant_1456
            CCR: CC_0443 CC_0534
            SIL: SPO1844(nagA)
            SIT: TM1040_3148
            RSP: RSP_1296(nagA)
            RSH: Rsph17029_2957
            RSQ: Rsph17025_2730
            JAN: Jann_1361
            RDE: RD1_1725(nagA)
            PDE: Pden_2477
            ZMO: ZMO0962(nagA)
            NAR: Saro_2414
            GOX: GOX1473
            ABA: Acid345_2780
            SUS: Acid_5572
            BSU: BG12630(nagA)
            BHA: BH0421(nagA)
            BAN: BA4274(nagA)
            BAR: GBAA4274(nagA)
            BAA: BA_4734(nagA)
            BAT: BAS3965
            BCE: BC4055
            BCA: BCE_1905(nagA) BCE_4122(nagA)
            BCZ: BCZK1640(nagA) BCZK3811(nagA)
            BCY: Bcer98_2754
            BTK: BT9727_3796(nagA)
            BTL: BALH_3671
            BLI: BL00084(nagA)
            BLD: BLi04348(nagA)
            BCL: ABC1489(nagA)
            BAY: RBAM_032200
            BPU: BPUM_3138
            OIH: OB2907(nagA)
            GKA: GK2277
            SAU: SA0656(nagA)
            SAV: SAV0701(nagA)
            SAM: MW0663(nagA)
            SAR: SAR0754
            SAS: SAS0666
            SAC: SACOL0761(nagA)
            SAB: SAB0650
            SAA: SAUSA300_0686(nagA)
            SAO: SAOUHSC_00710
            SAJ: SaurJH9_0725
            SAH: SaurJH1_0741
            SEP: SE0473
            SER: SERP0360(nagA)
            SHA: SH0276
            SSP: SSP2016
            LMO: lmo0956 lmo2108
            LMF: LMOf2365_0976(nagA-1) LMOf2365_2141(nagA-2)
            LIN: lin0955 lin2213
            LWE: lwe0938(nagA)
            LLA: L173068(nagA)
            LLC: LACR_1458
            LLM: llmg_1117(nagA)
            SPY: SPy_1694(nagA)
            SPZ: M5005_Spy_1388(nagA)
            SPM: spyM18_1705(nagA)
            SPG: SpyM3_1475(nagA)
            SPS: SPs0392
            SPH: MGAS10270_Spy1507(nagA)
            SPI: MGAS10750_Spy1500(nagA)
            SPJ: MGAS2096_Spy1412(nagA)
            SPK: MGAS9429_Spy1388(nagA)
            SPF: SpyM50402
            SPA: M6_Spy1436
            SPB: M28_Spy1431(nagA)
            SPN: SP_2056
            SPR: spr1867(nagA)
            SPD: SPD_1866(nagA)
            SAG: SAG0266(nagA)
            SAN: gbs0256
            SAK: SAK_0338(nagA)
            SMU: SMU.435
            STC: str0501(nagA)
            STL: stu0501(nagA)
            STE: STER_0537
            SSA: SSA_1893(nagA)
            SSU: SSU05_1259
            SSV: SSU98_1274
            SGO: SGO_0549(nagA)
            LPL: lp_0562(nagA)
            LJO: LJ0118
            LAC: LBA0144
            LSA: LSA1588(nagA)
            LSL: LSL_1466(nagA)
            LDB: Ldb0197(nagA)
            LBU: LBUL_0171
            LBR: LVIS_0539
            LCA: LSEI_1808
            LGA: LGAS_0116
            PPE: PEPE_1528 PEPE_1754
            EFA: EF1317(nagA-1) EF3044(nagA-2)
            OOE: OEOE_1728
            LME: LEUM_0425
            STH: STH1280 STH605
            CAC: CAC0188(nagA)
            CPE: CPE2176(nagA)
            CPF: CPF_2434(nagA)
            CPR: CPR_2144(nagA)
            CNO: NT01CX_0291(nagA)
            CTH: Cthe_2190
            CDF: CD1010(nagA) CD3453(agaA)
            CBO: CBO2834(nagA)
            CBA: CLB_2778(nagA)
            CBH: CLC_2711(nagA)
            CBF: CLI_2884(nagA)
            CBE: Cbei_4564
            AMT: Amet_4181
            TTE: TTE0232(nagA)
            MPU: MYPU_3690(nagA)
            MPE: MYPE1750(nagA)
            MMY: MSC_0533(nagA)
            MHY: mhp588(nagA)
            MHJ: MHJ_0573(nagA)
            MHP: MHP7448_0572(nagA)
            MSY: MS53_0194(nagA)
            MCP: MCAP_0438(nagA)
            MTU: Rv3332(nagA)
            MTC: MT3435(nagA)
            MBO: Mb3365(nagA)
            MBB: BCG_3402(nagA)
            MPA: MAP3450(nagA)
            MAV: MAV_4307(nagA)
            MSM: MSMEG_2119(nagA)
            MUL: MUL_1443(nagA)
            CGL: NCgl2556(cgl2645)
            CGB: cg2929(nagA1)
            CDI: DIP0520
            CJK: jk2047
            RHA: RHA1_ro01548
            SCO: SCO4284(SCD95A.17c)
            SMA: SAV3941(nagA)
            LXX: Lxx19360(nagA)
            CMI: CMM_0484(nagD)
            ART: Arth_0181 Arth_1713 Arth_3513
            AAU: AAur_2589(nagA)
            PAC: PPA0484
            NCA: Noca_4484
            TFU: Tfu_2473
            ACE: Acel_0557
            KRA: Krad_0772 Krad_2159
            SEN: SACE_7184(nagA)
            STP: Strop_0245
            BLO: BL1344(nagA)
            BAD: BAD_1602(nagA)
            RXY: Rxyl_0658
            FNU: FN1133
            RBA: RB12559(nagA) RB1356(nagA) RB977(nagA)
            BGA: BG0149(nagA)
            BAF: BAPKO_0152(nagA)
            SYW: SYNW2286
            SYC: syc1078_d(nagA)
            SYF: Synpcc7942_0440
            SYD: Syncc9605_2424
            SYE: Syncc9902_2104
            SYG: sync_2639
            SYR: SynRCC307_2264(nagA)
            SYX: SynWH7803_2305(nagA)
            TEL: tll2093
            GVI: gll0934
            ANA: all0988
            AVA: Ava_2952
            PMA: Pro0192(nagA)
            PMT: PMT2039
            PMN: PMN2A_1535
            PMF: P9303_27141(nagA)
            PME: NATL1_02421(nagA)
            TER: Tery_4474
            BTH: BT_0675 BT_0676 BT_3588
            BFR: BF2735 BF3115
            BFS: BF2752 BF2952
            FJO: Fjoh_3974
            DRA: DR_A0066
            DGE: Dgeo_2623
            TTH: TT_P0025
            TMA: TM0814
            TPT: Tpet_0114
            TME: Tmel_0694
            FNO: Fnod_0810
            HMA: rrnAC3411
            PTO: PTO0013
            SMR: Smar_1521
            SSO: SSO2673(nagA)
            STO: ST2546
            TPE: Tpen_1093
STRUCTURES  PDB: 1O12  1UN7  1YMY  1YRR  2P50  2P53  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.25
            ExPASy - ENZYME nomenclature database: 3.5.1.25
            ExplorEnz - The Enzyme Database: 3.5.1.25
            ERGO genome analysis and discovery system: 3.5.1.25
            BRENDA, the Enzyme Database: 3.5.1.25
            CAS: 9027-50-3
///
ENTRY       EC 3.5.1.26                 Enzyme
NAME        N4-(beta-N-acetylglucosaminyl)-L-asparaginase;
            aspartylglucosylamine deaspartylase;
            aspartylglucosylaminase;
            aspartylglucosaminidase;
            aspartylglycosylamine amidohydrolase;
            N-aspartyl-beta-glucosaminidase;
            glucosylamidase;
            beta-aspartylglucosylamine amidohydrolase;
            4-N-(beta-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase
REACTION    N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O =
            N-acetyl-beta-D-glucosaminylamine + L-aspartate [RN:R03421]
ALL_REAC    R03421
SUBSTRATE   N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine [CPD:C04540];
            H2O [CPD:C00001]
PRODUCT     N-acetyl-beta-D-glucosaminylamine [CPD:C01239];
            L-aspartate [CPD:C00049]
COMMENT     Acts only on asparagine-oligosaccharides containing one amino acid,
            i.e., the asparagine has free alpha-amino and alpha-carboxyl groups
            [cf. EC 3.5.1.52, peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine
            amidase]
REFERENCE   1  [PMID:5010303]
  AUTHORS   Kono M, Yamashina I.
  TITLE     Purification and properties of 4-L-aspartylglycosylamine
            amidohydrolase from hog kidney.
  JOURNAL   Biochim. Biophys. Acta. 258 (1972) 600-17.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:6061403]
  AUTHORS   Mahadevan S, Tappel AL.
  TITLE     Beta-aspartylglucosylamine amido hydrolase of rat liver and kidney.
  JOURNAL   J. Biol. Chem. 242 (1967) 4568-76.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:5778645]
  AUTHORS   Tarentino AL, Maley F.
  TITLE     The purification and properties of a beta-aspartyl
            N-acetylglucosylamine amidohydrolase from hen oviduct.
  JOURNAL   Arch. Biochem. Biophys. 130 (1969) 295-303.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00511  N-Glycan degradation
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01444  N4-(beta-N-acetylglucosaminyl)-L-asparaginase
GENES       HSA: 175(AGA)
            PTR: 461616(AGA)
            MMU: 11593(Aga)
            RNO: 290923(Aga)
            CFA: 475638(AGA)
            XLA: 496249(LOC496249)
            SPU: 593612(LOC593612)
            DME: Dmel_CG10474 Dmel_CG4372
            CEL: R04B3.2(glycosylasparaginase)
            OSA: 4336581
            XCC: XCC2914(aspG)
            XCB: XC_1195
            XCV: XCV3222
            XAC: XAC3092(aspG)
            XOO: XOO1760(aspG)
            XOM: XOO_1660(XOO1660)
            CCR: CC_2359
            CDF: CD0139
            GFO: GFO_0141
            FJO: Fjoh_2037
STRUCTURES  PDB: 1APY  1APZ  1AYY  1P4K  1P4V  2GAC  2GAW  2GL9  9GAA  9GAC  
                 9GAF  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.26
            ExPASy - ENZYME nomenclature database: 3.5.1.26
            ExplorEnz - The Enzyme Database: 3.5.1.26
            ERGO genome analysis and discovery system: 3.5.1.26
            BRENDA, the Enzyme Database: 3.5.1.26
            CAS: 9075-24-5
///
ENTRY       EC 3.5.1.27                 Enzyme
NAME        N-formylmethionylaminoacyl-tRNA deformylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-formyl-L-methionylaminoacyl-tRNA amidohydrolase
REACTION    N-formyl-L-methionylaminoacyl-tRNA + H2O = formate +
            L-methionylaminoacyl-tRNA [RN:R04268]
ALL_REAC    R04268
SUBSTRATE   N-formyl-L-methionylaminoacyl-tRNA [CPD:C04258];
            H2O [CPD:C00001]
PRODUCT     formate [CPD:C00058];
            L-methionylaminoacyl-tRNA [CPD:C03617]
REFERENCE   1  [PMID:4887858]
  AUTHORS   Livingston DM, Leder P.
  TITLE     Deformylation and protein biosynthesis.
  JOURNAL   Biochemistry. 8 (1969) 435-43.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K01445  N-formylmethionylaminoacyl-tRNA deformylase
GENES       AMA: AM1236(def)
            BAY: RBAM_014300
STRUCTURES  PDB: 1BSJ  1BSK  1LMH  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.27
            ExPASy - ENZYME nomenclature database: 3.5.1.27
            ExplorEnz - The Enzyme Database: 3.5.1.27
            ERGO genome analysis and discovery system: 3.5.1.27
            BRENDA, the Enzyme Database: 3.5.1.27
            CAS: 37289-08-0
///
ENTRY       EC 3.5.1.28                 Enzyme
NAME        N-acetylmuramoyl-L-alanine amidase;
            acetylmuramyl-L-alanine amidase;
            N-acetylmuramyl-L-alanine amidase;
            N-acylmuramyl-L-alanine amidase;
            acetylmuramoyl-alanine amidase;
            N-acetylmuramic acid L-alanine amidase;
            acetylmuramyl-alanine amidase;
            N-acetylmuramylalanine amidase;
            murein hydrolase;
            N-acetylmuramoyl-L-alanine amidase type I;
            N-acetylmuramoyl-L-alanine amidase type II
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     peptidoglycan amidohydrolase
REACTION    Hydrolyses the link between N-acetylmuramoyl residues and L-amino
            acid residues in certain cell-wall glycopeptides
ALL_REAC    (other) R04112
REFERENCE   1  [PMID:5777325]
  AUTHORS   Ghuysen JM, Dierickx L, Coyette J, Leyh-Bouille M, Guinand M,
            Campbell JN.
  TITLE     An improved technique for the preparation of Streptomyces peptidases
            and N-acetylmuramyl-l-alanine amidase active on bacterial wall
            peptidoglycans.
  JOURNAL   Biochemistry. 8 (1969) 213-22.
  ORGANISM  Streptomyces aureus
REFERENCE   2  [PMID:809432]
  AUTHORS   Herbold DR, Glaser L.
  TITLE     Interaction of N-acetylmuramic acid L-alanine amidase with cell wall
            polymers.
  JOURNAL   J. Biol. Chem. 250 (1975) 7231-8.
REFERENCE   3  [PMID:803507]
  AUTHORS   Herbold DR, Glaser L.
  TITLE     Bacillus subtilis N-acetylmuramic acid L-alanine amidase.
  JOURNAL   J. Biol. Chem. 250 (1975) 1676-82.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   4  [PMID:6126517]
  AUTHORS   Ward JB, Curtis CA, Taylor C, Buxton RS.
  TITLE     Purification and characterization of two phage PBSX-induced lytic
            enzymes of Bacillus subtilis 168: an N-acetylmuramoyl-L-alanine
            amidase and an N-acetylmuramidase.
  JOURNAL   J. Gen. Microbiol. 128 (1982) 1171-8.
  ORGANISM  Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00550  Peptidoglycan biosynthesis
ORTHOLOGY   KO: K01446  N-acetylmuramoyl-L-alanine amidase
            KO: K01447  N-acetylmuramoyl-L-alanine amidase
            KO: K01448  N-acetylmuramoyl-L-alanine amidase
            KO: K01449  N-acetylmuramoyl-L-alanine amidase
GENES       HSA: 114770(PGLYRP2)
            MMU: 57757(Pglyrp2)
            CFA: 610405(PGLYRP2)
            SSC: 396557(pPGRP-LB)
            GGA: 693263(PGRPL)
            DME: Dmel_CG11709(PGRP-SA) Dmel_CG14745(PGRP-SC2)
                 Dmel_CG14746(PGRP-SC1a) Dmel_CG32042(PGRP-LA)
                 Dmel_CG4432(PGRP-LC) Dmel_CG4437(PGRP-LF) Dmel_CG7496(PGRP-SD)
                 Dmel_CG8577(PGRP-SC1b) Dmel_CG8995(PGRP-LE)
                 Dmel_CG9681(PGRP-SB1) Dmel_CG9697(PGRP-SB2)
            ECO: b0867(ybjR) b2435(amiA) b2817(amiC) b4169(amiB)
            ECJ: JW0851(ybjR) JW2428(amiA) JW4127(amiB) JW5449(amiC)
            ECE: Z1100 Z3700(amiA) Z4134 Z5776(amiB)
            ECS: ECs0953 ECs3306 ECs3674 ECs5145
            ECC: c1000(ybjR) c2969(amiA) c3411 c5253(amiB)
            ECI: UTI89_C0118(ampD) UTI89_C0870(ybjR) UTI89_C2768(amiA)
                 UTI89_C3218(amiC) UTI89_C4769(amiB)
            ECP: ECP_0882 ECP_2456 ECP_2829 ECP_4414
            ECV: APECO1_1226(ybjR) APECO1_2222(amiB) APECO1_3688(amiC)
                 APECO1_4113(amiA)
            ECW: EcE24377A_0112(ampD) EcE24377A_0941(amiD)
                 EcE24377A_2721(amiA) EcE24377A_3137(amiC) EcE24377A_4727
            ECX: EcHS_A0114 EcHS_A0971 EcHS_A2572 EcHS_A2963 EcHS_A4411
            STY: STY0927 STY2687(amiA) STY3129 STY4715(amiB)
            STT: t0408(amiA) t2002 t2899 t4409(amiB)
            SPT: SPA0416(amiA) SPA1868(ybjR) SPA2856(amiC) SPA4175(amiB)
            SEC: SC0886(ybjR) SC2449(amiA) SC2929(amiC) SC4234(amiB)
            STM: STM0931(ybjR) STM2450(amiA) STM2991(amiC) STM4358(amiB)
            YPE: YPO0370 YPO1023 YPO1715(ybjR)
            YPK: y0627(amiB) y1877 y3161
            YPM: YP_0526(amiB) YP_1740(ampD2) YP_2827(amiC)
            YPA: YPA_0495 YPA_1806 YPA_3914
            YPN: YPN_1915 YPN_2978 YPN_3301
            YPP: YPDSF_1689 YPDSF_3604
            YPS: YPTB0422 YPTB2366(ybjR) YPTB3022
            YPI: YpsIP31758_3368(ampD)
            SFL: SF0822(ybjR) SF2488(amiA) SF2828(amiC) SF4324(amiB)
            SFX: S0863 S2636(amiA) S3025 S4592(amiB)
            SFV: SFV_0855 SFV_2487(amiA) SFV_2895 SFV_4327(amiB)
            SSN: SSON_0853 SSON_2524(amiA) SSON_2974 SSON_4354(amiB)
            SBO: SBO_0800 SBO_2460(amiA) SBO_2707 SBO_4287(amiB)
            SDY: SDY_2396 SDY_2633(amiA) SDY_3034 SDY_4420(amiB)
            ECA: ECA1000(amiC) ECA2665 ECA3937(amiB)
            PLU: plu0645(amiC) plu2790 plu4584(amiB)
            BUC: BU576(amiB)
            BAS: BUsg555(amiB)
            BAB: bbp521(amiB)
            WBR: WGLp268
            SGL: SG0100 SG0334 SG0782 SG1961
            ENT: Ent638_0352 Ent638_2956 Ent638_3260
            SPE: Spro_0428 Spro_3463 Spro_3811
            BFL: Bfl078(amiB)
            BPN: BPEN_080(amiB)
            HIN: HI0066(amiB) HI1494
            HIT: NTHI0079(amiB)
            HDU: HD0450(amiB)
            HSO: HS_1082(amiB)
            PMU: PM0903
            MSU: MS1515(amiC)
            APL: APL_1136(amiB)
            ASU: Asuc_0990
            XFA: XF0759 XF2656
            XFT: PD1898(amiC) PD2025
            XCC: XCC1539 XCC1763(amiC) XCC2299(amiC) XCC3805
            XCB: XC_1816 XC_2472 XC_2695 XC_3877
            XCV: XCV1630 XCV1812(amiC) XCV2603(amiC) XCV3978(ampD)
            XAC: XAC1589 XAC1780(amiC) XAC2406(amiC) XAC3860
            XOO: XOO2368(amiC) XOO2445 XOO2733(amiC) XOO4100
            XOM: XOO_2249(XOO2249) XOO_2318(XOO2318) XOO_2578(XOO2578)
                 XOO_3876(XOO3876)
            VCH: VC0344
            VCO: VC0395_A2755(amiB)
            VVU: VV1_1291
            VVY: VV3074
            VPA: VP2820
            VFI: VF2326
            PPR: PBPRA3353(amiB)
            PAE: PA4947(amiB) PA5485 PA5538(amiA)
            PAU: PA14_65370(amiB) PA14_72400 PA14_73040(amiA)
            PAP: PSPA7_0905
            PPU: PP_0130 PP_4897
            PPF: Pput_4773
            PST: PSPTO_0338 PSPTO_4945 PSPTO_5528
            PSB: Psyr_0265 Psyr_0569 Psyr_5077
            PSP: PSPPH_0254 PSPPH_0562 PSPPH_5159(amiC)
            PFL: PFL_0088 PFL_0563 PFL_6176(amiC)
            PFO: Pfl_0049(ampD) Pfl_0520 Pfl_5657
            PEN: PSEEN0084 PSEEN4946(amiC)
            PMY: Pmen_0632
            PAR: Psyc_0440
            PCR: Pcryo_0212
            SON: SO_0600(amiB)
            SDN: Sden_3208
            SFR: Sfri_3314
            SAZ: Sama_3028
            SBL: Sbal_0555
            SBM: Shew185_3770
            SLO: Shew_0563
            SPC: Sputcn32_3283
            SSE: Ssed_0794
            SPL: Spea_3543
            SHE: Shewmr4_0595
            SHM: Shewmr7_3435
            SHN: Shewana3_0594
            SHW: Sputw3181_0658
            ILO: IL0330(amiB)
            CPS: CPS_0322(amiB) CPS_4811(ampD)
            PHA: PSHAa0268(amiB)
            PAT: Patl_3975
            SDE: Sde_2670
            PIN: Ping_3241
            MAQ: Maqu_2772
            CBU: CBU_0379(ampD) CBU_1085
            LPN: lpg2698(amiB)
            LPF: lpl2626
            LPP: lpp2753
            MCA: MCA1296
            TCX: Tcr_1083
            NOC: Noc_0337
            AEH: Mlg_0570
            HHA: Hhal_0669
            HCH: HCH_05387
            CSA: Csal_1274 Csal_1643
            ABO: ABO_2206(amiB)
            MMW: Mmwyl1_2635
            AHA: AHA_0814 AHA_0921
            DNO: DNO_0311 DNO_1202(ampD)
            BCI: BCI_0585
            NME: NMB0456 NMB0987 NMB1085
            NMA: NMA1188 NMA1303 NMA1864 NMA2028(amiC)
            NMC: NMC1694(amiC)
            NGO: NGO1502
            CVI: CV_1309 CV_3031 CV_3822
            RSO: RSc1796(RS04196) RSc2539(amiC)
            REU: Reut_A0584
            REH: H16_A0597(amiC) H16_A3236
            RME: Rmet_0526
            BMA: BMA0365 BMA1261 BMAA0266 BMAA0751
            BMV: BMASAVP1_A0665 BMASAVP1_A3002(flgJ)
            BML: BMA10299_A2091(flgJ) BMA10299_A2500
            BMN: BMA10247_0114 BMA10247_3346(flgJ)
            BXE: Bxe_A0746 Bxe_C0344
            BVI: Bcep1808_2656
            BUR: Bcep18194_A4690 Bcep18194_A5895
            BCN: Bcen_1068 Bcen_1952
            BCH: Bcen2424_1548 Bcen2424_2563
            BAM: Bamb_1449 Bamb_2611
            BPS: BPSL0859 BPSL1872 BPSS1490 BPSS1840
            BPM: BURPS1710b_1064(amiC) BURPS1710b_1972 BURPS1710b_A0524
                 BURPS1710b_A0926(ampD)
            BTE: BTH_I0722 BTH_I2517 BTH_II0537 BTH_II0877
            PNU: Pnuc_0595
            BPE: BP0246(amiC) BP2449
            BPA: BPP3313 BPP3621(amiC)
            BBR: BB3764 BB4056(amiC)
            RFR: Rfer_3303
            POL: Bpro_3199
            PNA: Pnap_1170
            AAV: Aave_1305
            AJS: Ajs_0983
            VEI: Veis_1711
            MPT: Mpe_A2027
            HAR: HEAR0408(amiC)
            MMS: mma_0464
            NEU: NE0656(amiB)
            NET: Neut_1896
            NMU: Nmul_A2532
            EBA: ebA4451(amiC)
            AZO: azo1243 azo1779(ampD1) azo2226 azo3350(ampD2)
            DAR: Daro_3049
            TBD: Tbd_1519
            MFA: Mfla_1381
            HPY: HP0772(amiA)
            HPJ: jhp0709(amiA)
            HPA: HPAG1_0757
            HHE: HH0828(amiA)
            HAC: Hac_0641(amiA)
            WSU: WS0243(amiA)
            TDN: Tmden_0722
            CJE: Cj1269c(amiA)
            CJR: CJE1405
            CJJ: CJJ81176_1285
            CJU: C8J_1213(amiA)
            CJD: JJD26997_0456
            CCV: CCV52592_0486
            ABU: Abu_0642(amiA)
            NIS: NIS_0763
            SUN: SUN_1741 SUN_1742
            GSU: GSU1821
            GME: Gmet_1425
            GUR: Gura_2385
            PCA: Pcar_1511
            PPD: Ppro_1062
            DVU: DVU2371
            DVL: Dvul_0892
            DDE: Dde_1370
            LIP: LI1023(amiA)
            BBA: Bd0992(cwlJ) Bd2699(amiC)
            ADE: Adeh_1694 Adeh_3362
            AFW: Anae109_2111 Anae109_3426
            MXA: MXAN_3886
            SAT: SYN_00903 SYN_02145
            SFU: Sfum_0729
            RFE: RF_1384(ampD)
            OTS: OTBS_0048(ybjR)
            PUB: SAR11_0034(ybjR)
            MLO: mll1570 mlr0213
            MES: Meso_1709 Meso_2018
            PLA: Plav_3277
            SME: SMc01335(amiC) SMc01854
            SMD: Smed_0959
            ATU: Atu1340(amiA) Atu2113
            ATC: AGR_C_2473 AGR_C_3833
            RET: RHE_CH01646(amiC) RHE_CH02860(ypch00981)
            RLE: RL1742 RL3320
            BME: BMEI0565 BMEI1056
            BMF: BAB1_0931 BAB1_1462
            BMS: BR0915 BR1444
            BMB: BruAb1_0925 BruAb1_1439
            OAN: Oant_2267
            BJA: blr4306 blr6611
            BRA: BRADO3513
            BBT: BBta_4202
            RPA: RPA2451 RPA3539
            RPB: RPB_1985(ampD) RPB_3008
            RPC: RPC_2185 RPC_2853
            RPD: RPD_2443 RPD_3403
            RPE: RPE_2098 RPE_2978
            NWI: Nwi_1042 Nwi_1719
            NHA: Nham_1270 Nham_1823
            BHE: BH08710(amiB)
            BQU: BQ05880(amiB)
            BBK: BARBAKC583_0453 BARBAKC583_0904
            XAU: Xaut_4667
            CCR: CC_1876 CC_2567
            SIL: SPO2588 SPO2967
            SIT: TM1040_0866 TM1040_1916
            RSP: RSP_2272(ampD) RSP_2979(amiC)
            RSH: Rsph17029_1625
            RSQ: Rsph17025_1858
            JAN: Jann_2536
            RDE: RD1_1998 RD1_2821(amiC) RD1_4147(ampD)
            PDE: Pden_1817
            MMR: Mmar10_1297 Mmar10_2088
            HNE: HNE_0480 HNE_0674
            ZMO: ZMO0195(amiA)
            NAR: Saro_2317 Saro_3051
            SAL: Sala_1735 Sala_3173
            SWI: Swit_3847
            ELI: ELI_01195 ELI_06765
            GOX: GOX1732
            GBE: GbCGDNIH1_0282 GbCGDNIH1_0440
            ACR: Acry_2027
            RRU: Rru_A0960 Rru_A2148
            MAG: amb0859 amb3238
            MGM: Mmc1_2129
            ABA: Acid345_1153
            SUS: Acid_4586
            BSU: BG10407(lytC) BG10505(cwlA) BG10825(cwlC) BG10962(xlyA)
                 BG11172(cwlJ) BG11439(sleB) BG11514(cwlD) BG11633(cwlH)
                 BG11717(yqiI) BG12699(xlyB) BG13322(ykvT) BG13590(blyA)
                 BG13806(yrvJ)
            BHA: BH0239(cwlD) BH0810 BH0966 BH1294(cwlC) BH1631(sleB) BH2879
                 BH3510 BH3665(lytC) BH3826(cwlJ)
            BAN: BA0146(cwlD) BA1514 BA2446 BA2528 BA2594(cwlJ-1) BA2748(sleB)
                 BA2805 BA3698 BA3737 BA3767 BA3893 BA4073 BA5640(cwlJ-2)
            BAR: GBAA0146(cwlD) GBAA1514 GBAA2446 GBAA2528 GBAA2594(cwlJ-1)
                 GBAA2748(sleB) GBAA2805 GBAA3698 GBAA3737 GBAA3767 GBAA3893
                 GBAA4073 GBAA5640(cwlJ-2)
            BAA: BA_0322 BA_0496 BA_0729 BA_2036 BA_2942 BA_3022 BA_3103
                 BA_3274 BA_3326 BA_4181 BA_4218 BA_4364(lysM) BA_4544
            BAT: BAS0146 BAS1404 BAS2277 BAS2351 BAS2417 BAS2562 BAS2615
                 BAS3428 BAS3463 BAS3490 BAS3606 BAS3784 BAS5084 BAS5241
            BCE: BC0167 BC0470 BC0888 BC0902 BC1494 BC1911 BC2207 BC2536
                 BC2753 BC2822 BC2823 BC3257 BC3524 BC3637 BC3694 BC4687 BC5234
                 BC5390
            BCA: BCE_0146(cwlD) BCE_1620 BCE_2614(cwlJ) BCE_2781(sleB)
                 BCE_2848 BCE_2849 BCE_3666 BCE_3710 BCE_3795 BCE_5353
                 BCE_5519(cwlJ)
            BCZ: BCZK0139(cwlD) BCZK0777(cwlA) BCZK0800 BCZK1375
                 BCZK1628(amiB) BCZK2195 BCZK2268 BCZK2341(cwlJ) BCZK2483(sleB)
                 BCZK2532(ampD) BCZK2982(amiB) BCZK3340(cwlC) BCZK3380(cwl)
                 BCZK3381(cwl) BCZK3407(ply511) BCZK3515(cwlJ) BCZK4930
                 BCZK5088(cwlJ)
            BCY: Bcer98_0140
            BTK: BT9727_0141(cwlD) BT9727_0796 BT9727_1376 BT9727_2237
                 BT9727_2310 BT9727_2376(cwlJ) BT9727_2518(sleB)
                 BT9727_2564(ampD) BT9727_3033(amiB) BT9727_3111
                 BT9727_3389(cwlC) BT9727_3503(cwlJ) BT9727_4915
                 BT9727_5071(cwlJ)
            BTL: BALH_0143(cwlD) BALH_0788(cwlA) BALH_1920 BALH_2334(cwlJ)
                 BALH_4732 BALH_p0044(plyG)
            BLI: BL00542(xlyB) BL00686(cwlC) BL01016 BL01120(yrvJ) BL01514
                 BL01582(blyAB) BL01690(cwlJ) BL02222(sleB) BL02879
                 BL03348(lytC) BL03556
            BLD: BLi00171(cwlD) BLi00345(cwlJ) BLi01031 BLi01974(cwlC)
                 BLi02431(sleB) BLi02590(yqiI) BLi02884(yrvJ1) BLi03598(blyA)
                 BLi03808(lytC)
            BCL: ABC0192(cwlD) ABC0927(cwlC) ABC1351(xlyA) ABC1870(sleB)
                 ABC2075 ABC2541 ABC2815 ABC3920(cwlJ)
            BAY: RBAM_001790(cwlD) RBAM_012660(xlyA) RBAM_017210(cwlC)
                 RBAM_032770(lytC)
            BPU: BPUM_0144(cwlD) BPUM_1158(xlyA) BPUM_1632(cwlC)
                 BPUM_2399(blyA) BPUM_3214(lytC)
            OIH: OB0195 OB0220 OB0662 OB0854 OB1806 OB3024 OB3085 OB3141
            GKA: GK0142 GK0209 GK2231 GK3255
            SAU: SA0905(atl) SA1458(lytH)
            SAV: SAV0913 SAV1052 SAV1632(lytH)
            SAM: MW0936(atl) MW1582
            SAR: SAR1026(atl) SAR2040
            SAS: SAS0988 SAS1568 SAS1869
            SAC: SACOL1062(atl) SACOL1687
            SAB: SAB0781 SAB0919c(atl) SAB1501c SAB2183c
            SAA: SAUSA300_0955(atl) SAUSA300_1383 SAUSA300_1588(lytH)
                 SAUSA300_1923
            SAO: SAOUHSC_00994 SAOUHSC_01739 SAOUHSC_02023 SAOUHSC_02855
                 SAOUHSC_02883
            SAJ: SaurJH9_0367 SaurJH9_1080 SaurJH9_1112
            SAH: SaurJH1_0376 SaurJH1_1101 SaurJH1_1135
            SEP: SE0750 SE1313
            SER: SERP0636(atlE) SERP1194
            SHA: SH1289(lytH) SH1911(atl) SH2333
            SSP: SSP1127 SSP1741
            LMO: lmo0129 lmo1521
            LMF: LMOf2365_0147 LMOf2365_1540(ami) LMOf2365_2670
            LIN: lin0176 lin1556 lin1700 lin2374
            LWE: lwe0111 lwe1534 lwe2508(ami) lwe2639
            LLM: llmg_0509(acmD)
            SPZ: M5005_Spy_0028 M5005_Spy_0500 M5005_Spy_0663(mur1.1)
                 M5005_Spy_0664(mur1.2) M5005_Spy_1002 M5005_Spy_1501
            SPH: MGAS10270_Spy0029 MGAS10270_Spy0494 MGAS10270_Spy0845
                 MGAS10270_Spy1303 MGAS10270_Spy1569
            SPI: MGAS10750_Spy0028 MGAS10750_Spy0029 MGAS10750_Spy0519
                 MGAS10750_Spy0881 MGAS10750_Spy1561
            SPJ: MGAS2096_Spy0029 MGAS2096_Spy0511 MGAS2096_Spy1529
            SPK: MGAS9429_Spy0028 MGAS9429_Spy0490 MGAS9429_Spy1503
            SPA: M6_Spy0077 M6_Spy0521 M6_Spy0682 M6_Spy0683 M6_Spy1198
                 M6_Spy1342 M6_Spy1495
            SPB: M28_Spy0028 M28_Spy0479 M28_Spy0644(mur1.1)
                 M28_Spy0645(mur1.2) M28_Spy1490
            SPN: SP_1937
            SPR: spr1754(lytA)
            SPD: SPD_1737(lytA)
            SSA: SSA_1095(mur2) SSA_1525
            LPL: lp_1982(lytH)
            LSA: LSA0532 LSA0862 LSA1437 LSA1558 LSA1581
            LSL: LSL_0899(amiC) LSL_1516
            LBR: LVIS_0732 LVIS_0884 LVIS_1883
            LCA: LSEI_1536
            OOE: OEOE_0144 OEOE_0588
            STH: STH2593 STH2958 STH3039 STH864
            CAC: CAC0686 CAC3092
            CPE: CPE0115 CPE2367
            CPF: CPF_0111 CPF_0545 CPF_2676(cwlD)
            CPR: CPR_0113 CPR_1398 CPR_1483 CPR_2348 CPR_2361(cwlD) CPR_A0003
                 CPR_B0004
            CTC: CTC00350 CTC00491 CTC00504 CTC00515 CTC00518 CTC00520
                 CTC00521 CTC02092 CTC02570
            CNO: NT01CX_0795 NT01CX_2157
            CTH: Cthe_2498
            CDF: CD0106(cwlD)
            CBO: CBO1432 CBO1751 CBO3016 CBO3443(cwlD)
            CBA: CLB_1449 CLB_1457 CLB_3499
            CBH: CLC_1461 CLC_1469 CLC_3387
            CBF: CLI_1516 CLI_1877 CLI_3625
            AMT: Amet_0953 Amet_1886
            CHY: CHY_1756 CHY_2271 CHY_2569
            DSY: DSY0132 DSY0743 DSY1234 DSY1541 DSY3330 DSY4950
            DRM: Dred_2281 Dred_2693
            SWO: Swol_0126 Swol_2295
            CSC: Csac_1514
            TTE: TTE2217(amiC) TTE2424(amiC2) TTE2551
            MTA: Moth_0517 Moth_1272 Moth_2296
            MTU: Rv3915(cwlM)
            MTC: MT4034
            MBO: Mb3946
            MLE: ML2704
            MPA: MAP4341(cwlM)
            MAV: MAV_0385 MAV_2168 MAV_5303
            MSM: MSMEG_6281 MSMEG_6935
            MMC: Mmcs_5404
            CGL: NCgl2986(cgl3092)
            CGB: cg3424(cwlM)
            CEF: CE2935
            CDI: DIP2375
            CJK: jk2095(cwlM)
            NFA: nfa56640
            RHA: RHA1_ro03652
            FRA: Francci3_4538
            FAL: FRAAL2794 FRAAL6657 FRAAL6874(amiB)
            SEN: SACE_7386(cwlM)
            FNU: FN0164 FN1334
            CTR: CT268(amiA)
            CTA: CTA_0290(amiA)
            CMU: TC0539
            CPN: CPn0417(amiA)
            CPA: CP0337
            CPJ: CPj0417(amiA)
            CPT: CpB0433
            CCA: CCA00377
            CAB: CAB364
            CFE: CF0631(ami1)
            PCU: pc0315(amiA)
            BBU: BB0625 BB0666
            BGA: BG0689
            BAF: BAPKO_0710
            TPA: TP0247
            TDE: TDE1714
            LIL: LA0459(amiB1) LA2200(amiB2) LA3434(amiA)
            LIC: LIC10739(amiA) LIC11728
            LBJ: LBJ_1361 LBJ_2577(amiA)
            LBL: LBL_0535(amiA) LBL_1586
            SYN: slr0891(amiA) slr1744(amiA) slr1910(amiA)
            SYW: SYNW1009
            SYC: syc0816_d(amiA) syc1743_c(amiA) syc1958_d(amiA)
            SYF: Synpcc7942_0714 Synpcc7942_2134 Synpcc7942_2360
            SYD: Syncc9605_1135
            SYE: Syncc9902_1322
            SYR: SynRCC307_1157(amiC)
            SYX: SynWH7803_1036(amiC)
            CYA: CYA_2181
            CYB: CYB_0360
            TEL: tll0251 tll1774
            GVI: gll0522 glr0965
            ANA: all4998 all4999 alr0092 alr0093
            AVA: Ava_1465 Ava_1466 Ava_2268
            PMA: Pro1044(amiC)
            PMM: PMM0616
            PMT: PMT0394
            PMN: PMN2A_0053
            PMI: PMT9312_0616
            PMB: A9601_06721(amiC)
            PMC: P9515_06811(amiC)
            PMF: P9303_18931(amiC)
            PMG: P9301_06421(amiC)
            PME: NATL1_06741(amiC)
            TER: Tery_0339 Tery_4034
            BTH: BT_2141(amiA)
            BFR: BF3546 BF3823(amiA)
            BFS: BF3352 BF3615
            PGI: PG1048
            SRU: SRU_2497
            CHU: CHU_0750 CHU_1164(amiA)
            GFO: GFO_1368 GFO_1639 GFO_2754
            FPS: FP0810
            CTE: CT0054(amiB)
            CCH: Cag_0076
            CPH: Cpha266_0110
            PVI: Cvib_1713
            PLT: Plut_2072
            DRA: DR_1387 DR_1632 DR_2394 DR_2567 DR_C0013
            DGE: Dgeo_0665 Dgeo_1034
            TTH: TTC1006
            TTJ: TTHA1372
            AAE: aq_1681(amiB)
            MMA: MM_2290
STRUCTURES  PDB: 1ARO  1GVM  1H8G  1HCX  1J3G  1JWQ  1LBA  1X60  1XOV  2AR3  
                 2BGX  2BH7  2BML  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.28
            ExPASy - ENZYME nomenclature database: 3.5.1.28
            ExplorEnz - The Enzyme Database: 3.5.1.28
            ERGO genome analysis and discovery system: 3.5.1.28
            BRENDA, the Enzyme Database: 3.5.1.28
            CAS: 9013-25-6
///
ENTRY       EC 3.5.1.29                 Enzyme
NAME        2-(acetamidomethylene)succinate hydrolase;
            alpha-(N-acetylaminomethylene)succinic acid hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     2-(acetamidomethylene)succinate amidohydrolase (deaminating,
            decarboxylating)
REACTION    2-(acetamidomethylene)succinate + 2 H2O = acetate + succinate
            semialdehyde + NH3 + CO2 [RN:R01649]
ALL_REAC    R01649;
            (other) R06134
SUBSTRATE   2-(acetamidomethylene)succinate [CPD:C01215];
            H2O [CPD:C00001]
PRODUCT     acetate [CPD:C00033];
            succinate semialdehyde [CPD:C00232];
            NH3 [CPD:C00014];
            CO2 [CPD:C00011]
COMMENT     Involved in the degradation of pyridoxin in Pseudomonas.
REFERENCE   1  [PMID:3972793]
  AUTHORS   Huynh MS, Snell EE.
  TITLE     Enzymes of vitamin B6 degradation. Purification and properties of
            two N-acetylamidohydrolases.
  JOURNAL   J. Biol. Chem. 260 (1985) 2379-83.
  ORGANISM  Pseudomonas sp., Arthrobacter sp.
REFERENCE   2  [PMID:5769993]
  AUTHORS   Nyns EJ, Zach D, Snell EE.
  TITLE     The bacterial oxidation of vitamin B6. 8. Enzymatic breakdown of
            alpha-(N-acetylaminomethylene) succinic acid.
  JOURNAL   J. Biol. Chem. 244 (1969) 2601-5.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00750  Vitamin B6 metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.29
            ExPASy - ENZYME nomenclature database: 3.5.1.29
            ExplorEnz - The Enzyme Database: 3.5.1.29
            ERGO genome analysis and discovery system: 3.5.1.29
            BRENDA, the Enzyme Database: 3.5.1.29
            CAS: 37289-09-1
///
ENTRY       EC 3.5.1.30                 Enzyme
NAME        5-aminopentanamidase;
            5-aminovaleramidase;
            5-aminonorvaleramidase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     5-aminopentanamide amidohydrolase
REACTION    5-aminopentanamide + H2O = 5-aminopentanoate + NH3 [RN:R02273]
ALL_REAC    R02273;
            (other) R06134
SUBSTRATE   5-aminopentanamide [CPD:C00990];
            H2O [CPD:C00001]
PRODUCT     5-aminopentanoate [CPD:C00431];
            NH3 [CPD:C00014]
COMMENT     The enzyme from Pseudomonas putida also acts on 4-aminobutanamide
            and, more slowly, on 6-aminohexanamide.
REFERENCE   1  [PMID:5432799]
  AUTHORS   Reitz MS, Rodwell VW.
  TITLE     Delta-aminovaleramidase of Pseudomonas putida.
  JOURNAL   J. Biol. Chem. 245 (1970) 3091-6.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2  [PMID:5772467]
  AUTHORS   Takeda H, Yamamoto S, Kojima Y, Hayaishi O.
  TITLE     Studies on monooxygenases. I. General properties of crystalline
            L-lysine monooxygenase.
  JOURNAL   J. Biol. Chem. 244 (1969) 2935-41.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.30
            ExPASy - ENZYME nomenclature database: 3.5.1.30
            ExplorEnz - The Enzyme Database: 3.5.1.30
            ERGO genome analysis and discovery system: 3.5.1.30
            BRENDA, the Enzyme Database: 3.5.1.30
            CAS: 9054-60-8
///
ENTRY       EC 3.5.1.31                 Enzyme
NAME        formylmethionine deformylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-formyl-L-methionine amidohydrolase
REACTION    N-formyl-L-methionine + H2O = formate + L-methionine [RN:R00653]
ALL_REAC    R00653
SUBSTRATE   N-formyl-L-methionine [CPD:C03145];
            H2O [CPD:C00001]
PRODUCT     formate [CPD:C00058];
            L-methionine [CPD:C00073]
REFERENCE   1  [PMID:5767026]
  AUTHORS   Aronson JN, Lugay JC.
  TITLE     N-Formylmethionine deformylase from Euglena gracilis.
  JOURNAL   Biochem. Biophys. Res. Commun. 34 (1969) 311-4.
  ORGANISM  Euglena gracilis
PATHWAY     PATH: map00271  Methionine metabolism
            PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K01450  formylmethionine deformylase
GENES       CME: CME111C
            PFA: PFI0380c
            YPS: YPTB3665(def)
            VCO: VC0395_1128(def-2) VC0395_A2473(def-1)
            NMC: NMC0102(def)
            NGO: NGO1871(def)
            CVI: CV_4265(def)
            REH: H16_A2059(dmf) H16_A3700(def)
            MMS: mma_0143 mma_1680
            NEU: NE1755(def) NE1970(def)
            HHE: HH0569(def)
            WSU: WS2212(def)
            GSU: GSU0129(def-1) GSU3456(def-2)
            DVU: DVU3366(def)
            DDE: Dde_0013
            LIP: LI0767(def)
            RBE: RBE_0666(def)
            WOL: WD0165(def)
            BRA: BRADO0770(def)
            BBT: BBta_7337(def)
            GOX: GOX0123 GOX1836
            BSU: BG11933(def)
            BCA: BCE_3910(def) BCE_4023(def)
            BCZ: BCZK3626(def) BCZK3732(def)
            BTK: BT9727_3608(def) BT9727_3716(def)
            BLI: BL02297(def)
            BLD: BLi01793(def)
            BAY: RBAM_015550
            BPU: BPUM_1471
            GKA: GK1171(def)
            SAR: SAR1191(def)
            SAS: SAS1149
            SAC: SACOL1227(def2)
            SAO: SAOUHSC_01182
            LMF: LMOf2365_1072(def)
            SPD: SPD_1381(def-2)
            SGO: SGO_0321 SGO_1754
            LPL: lp_2935(def2)
            LJO: LJ1832
            LAC: LBA0060
            MCP: MCAP_0206(def)
            MBB: BCG_0468c(def)
            TDE: TDE1645(def)
            SYW: SYNW0324(def)
            PMA: Pro0081(def)
            PMM: PMM0068(def)
            PMT: PMT0384 PMT1601(def)
            PMB: A9601_00801(def)
            PMF: P9303_19041(def)
            PMG: P9301_00791(def)
            DEH: cbdb_A733(def)
            TTH: TTC1662
STRUCTURES  PDB: 1BS4  1BS5  1BS6  1BS7  1BS8  1BSZ  1DEF  1DFF  1G27  1G2A  
                 1ICJ  1JYM  1RL4  2DEF  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.31
            ExPASy - ENZYME nomenclature database: 3.5.1.31
            ExplorEnz - The Enzyme Database: 3.5.1.31
            ERGO genome analysis and discovery system: 3.5.1.31
            BRENDA, the Enzyme Database: 3.5.1.31
            CAS: 9032-86-4
///
ENTRY       EC 3.5.1.32                 Enzyme
NAME        hippurate hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-benzoylamino-acid amidohydrolase
REACTION    hippurate + H2O = benzoate + glycine [RN:R01424]
ALL_REAC    R01424
SUBSTRATE   hippurate [CPD:C01586];
            H2O [CPD:C00001]
PRODUCT     benzoate [CPD:C00180];
            glycine [CPD:C00037]
COMMENT     Acts on various N-benzoylamino acids.
REFERENCE   1  [PMID:16526097]
  AUTHORS   Tsoi E, Akmal S, Geerts L, Jeffery B, Nicolaides KH.
  TITLE     Sonographic measurement of cervical length and fetal fibronectin
            testing in threatened preterm labor.
  JOURNAL   Ultrasound. Obstet. Gynecol. 27 (2006) 368-72.
REFERENCE   2  [PMID:16526097]
  AUTHORS   Tsoi E, Akmal S, Geerts L, Jeffery B, Nicolaides KH.
  TITLE     Sonographic measurement of cervical length and fetal fibronectin
            testing in threatened preterm labor.
  JOURNAL   Ultrasound. Obstet. Gynecol. 27 (2006) 368-72.
REFERENCE   3  [PMID:3922754]
  AUTHORS   Rohrmann K, Niemann R, Buddecke E.
  TITLE     Two N-acetylgalactosaminyltransferase are involved in the
            biosynthesis of chondroitin sulfate.
  JOURNAL   Eur. J. Biochem. 148 (1985) 463-9.
PATHWAY     PATH: map00360  Phenylalanine metabolism
ORTHOLOGY   KO: K01451  hippurate hydrolase
GENES       ANI: AN7529.2
            AFM: AFUA_1G11250 AFUA_6G09600
            AOR: AO090001000612
            TET: TTHERM_00379080
            ECI: UTI89_C4556
            ECV: APECO1_2502
            ECA: ECA1004
            SGL: SG1744
            ENT: Ent638_2091
            SPE: Spro_3206
            PAU: PA14_56480
            PPF: Pput_2611
            PST: PSPTO_1882
            PSB: Psyr_3523
            PSP: PSPPH_3465
            PFO: Pfl_1291
            SDN: Sden_3487
            SFR: Sfri_3605
            SLO: Shew_2688
            SPL: Spea_2928 Spea_4074
            PAT: Patl_2787
            SDE: Sde_1645
            PIN: Ping_2027
            CBU: CBU_0362
            FTL: FTL_0753
            TCX: Tcr_0219
            CSA: Csal_1708
            MMW: Mmwyl1_2454
            CVI: CV_1884(hipO)
            RSO: RSc2871(hipO)
            REU: Reut_A0051 Reut_A3007 Reut_A3289 Reut_B4300 Reut_B5217
                 Reut_B5812
            RME: Rmet_0021 Rmet_3159 Rmet_4507 Rmet_5222
            BMA: BMAA1494(hipO-1) BMAA1941(hipO-2)
            BMV: BMASAVP1_0958(hipO-2)
            BML: BMA10299_1245(hipO-2) BMA10299_2111(hipO-1)
            BMN: BMA10247_A0794(hipO-1) BMA10247_A2220(hipO-2)
            BXE: Bxe_A0472 Bxe_A2955 Bxe_B0069 Bxe_B2175
            BVI: Bcep1808_1595 Bcep1808_3597 Bcep1808_5855 Bcep1808_6408
                 Bcep1808_6694
            BUR: Bcep18194_A4387 Bcep18194_A4797 Bcep18194_B0058
                 Bcep18194_B0252 Bcep18194_B0948 Bcep18194_B1298
                 Bcep18194_B2598 Bcep18194_C7452
            BCN: Bcen_1169 Bcen_2992 Bcen_3600 Bcen_3715 Bcen_3821 Bcen_5231
                 Bcen_6435
            BCH: Bcen2424_1649 Bcen2424_4547 Bcen2424_4653 Bcen2424_4767
                 Bcen2424_5374 Bcen2424_5628 Bcen2424_6670
            BAM: Bamb_1550 Bamb_3971 Bamb_4721 Bamb_4907 Bamb_5843 Bamb_5896
                 Bamb_6319 Bamb_6364
            BPS: BPSS0148 BPSS0271
            BPM: BURPS1710b_A1662(hipO-2) BURPS1710b_A1808(hipO-1)
            BTE: BTH_II0217
            PNU: Pnuc_0152
            BPE: BP2810
            BBR: BB4176
            RFR: Rfer_3615
            POL: Bpro_0044 Bpro_2111 Bpro_2533 Bpro_4523
            PNA: Pnap_0651 Pnap_1248
            AAV: Aave_0770 Aave_0935 Aave_2179 Aave_3677
            AJS: Ajs_0453 Ajs_0687
            VEI: Veis_1301 Veis_4256 Veis_4728 Veis_4882
            MPT: Mpe_A3092
            MMS: mma_0273(hipO1) mma_3336(hipO2)
            NMU: Nmul_A0853
            EBA: ebA5427
            AZO: azo0205(hipO1) azo1605(hipO2)
            DAR: Daro_0071
            CJE: Cj0985c(hipO)
            CJR: CJE1067(hipO)
            CJJ: CJJ81176_1004(hipO)
            CJU: C8J_0924(hipO)
            CJD: JJD26997_0803(hipO)
            DDE: Dde_3033
            ADE: Adeh_3172
            MLO: mlr3583
            SME: SMb21279 SMc00682(hipO1) SMc02256(hipO2)
            SMD: Smed_0172 Smed_2573 Smed_4612
            ATU: Atu2732(hipO) Atu3635 Atu4428 Atu4444
            ATC: AGR_C_4953 AGR_L_2386 AGR_L_849 AGR_L_879
            RET: RHE_CH03429(ypch01210) RHE_CH03833(hipO) RHE_PC00005
            RLE: RL3888(hipO) RL4364 pRL100225
            OAN: Oant_0901 Oant_3314 Oant_4353
            BJA: blr3021 blr5691
            RPA: RPA3729
            RPB: RPB_1734 RPB_2126 RPB_3086
            RPC: RPC_1193 RPC_1729
            RPD: RPD_3295 RPD_3565
            RPE: RPE_1821
            NWI: Nwi_2262
            NHA: Nham_2671 Nham_3968
            XAU: Xaut_4367
            SIL: SPO1214 SPO2468 SPO2808 SPO2809 SPO2810 SPO2811
            SIT: TM1040_0512 TM1040_0718 TM1040_0719 TM1040_0937
            RSP: RSP_2910
            RSH: Rsph17029_1555
            RSQ: Rsph17025_1110
            JAN: Jann_2343 Jann_3241 Jann_3289 Jann_4150
            RDE: RD1_3132 RD1_3310
            PDE: Pden_0186 Pden_0610 Pden_1199
            MMR: Mmar10_1822
            ZMO: ZMO0312
            NAR: Saro_2348 Saro_2932
            SAL: Sala_0940 Sala_2314
            SWI: Swit_3041 Swit_3434
            ACR: Acry_1211 Acry_1887 Acry_2229 Acry_3534
            RRU: Rru_A0984 Rru_A1813 Rru_A2871
            ABA: Acid345_1597 Acid345_2056
            BSU: BG12596(hipO)
            SAB: SAB1253
            SAJ: SaurJH9_0090 SaurJH9_1459 SaurJH9_2354
            SAH: SaurJH1_0093 SaurJH1_1488 SaurJH1_2397
            SGO: SGO_0159
            LRE: Lreu_0614
            CBE: Cbei_1386 Cbei_2229
            AMT: Amet_1622 Amet_4336
            CSC: Csac_1034
            MPE: MYPE3540
            MVA: Mvan_4743
            MGI: Mflv_1971
            MMC: Mmcs_1337
            MKM: Mkms_1355
            MJL: Mjls_1373
            CGL: NCgl2003(cgl2083)
            CGB: cg2285(hipO)
            CJK: jk0802(amiB)
            ART: Arth_3776
            NCA: Noca_3715
            TFU: Tfu_2437 Tfu_2564
            RXY: Rxyl_0180
            SYD: Syncc9605_0120
            SYE: Syncc9902_0164
            AVA: Ava_4094
            CCH: Cag_0903
            PVI: Cvib_0893
            PLT: Plut_1020
            RRS: RoseRS_1741
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.32
            ExPASy - ENZYME nomenclature database: 3.5.1.32
            ExplorEnz - The Enzyme Database: 3.5.1.32
            ERGO genome analysis and discovery system: 3.5.1.32
            BRENDA, the Enzyme Database: 3.5.1.32
            CAS: 37278-43-6
///
ENTRY       EC 3.5.1.33                 Enzyme
NAME        N-acetylglucosamine deacetylase;
            acetylaminodeoxyglucose acetylhydrolase;
            N-acetyl-D-glucosaminyl N-deacetylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-acetyl-D-glucosamine amidohydrolase
REACTION    N-acetyl-D-glucosamine + H2O = D-glucosamine + acetate [RN:R01200]
ALL_REAC    R01200
SUBSTRATE   N-acetyl-D-glucosamine [CPD:C00140];
            H2O [CPD:C00001]
PRODUCT     D-glucosamine [CPD:C00329];
            acetate [CPD:C00033]
REFERENCE   1
  AUTHORS   Roseman, S.
  TITLE     Glucosamine metabolism. I. N-Acetylglucosamine deacetylase.
  JOURNAL   J. Biol. Chem. 226 (1957) 115-123.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00530  Aminosugars metabolism
GENES       AZO: azo2324
STRUCTURES  PDB: 2C1G  2C1I  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.33
            ExPASy - ENZYME nomenclature database: 3.5.1.33
            ExplorEnz - The Enzyme Database: 3.5.1.33
            ERGO genome analysis and discovery system: 3.5.1.33
            BRENDA, the Enzyme Database: 3.5.1.33
            CAS: 9012-32-2
///
ENTRY       EC 3.5.1.34       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
COMMENT     Deleted entry: acetylhistidine deacetylase. Identical with EC
            3.4.13.5, Xaa-methyl-His dipeptidase (EC 3.5.1.34 created 1972,
            deleted 1981)
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.34
            ExPASy - ENZYME nomenclature database: 3.5.1.34
            ExplorEnz - The Enzyme Database: 3.5.1.34
            ERGO genome analysis and discovery system: 3.5.1.34
            BRENDA, the Enzyme Database: 3.5.1.34
///
ENTRY       EC 3.5.1.35                 Enzyme
NAME        D-glutaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     D-glutamine amidohydrolase
REACTION    D-glutamine + H2O = D-glutamate + NH3 [RN:R01579]
ALL_REAC    R01579;
            (other) R06134
SUBSTRATE   D-glutamine [CPD:C00819];
            H2O [CPD:C00001]
PRODUCT     D-glutamate [CPD:C00217];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Domnas, A. and Catimo, E.C.
  TITLE     The behavior of amidohydrolases and L-glutamate in synchronized
            populations of Blastocladiella emeronii.
  JOURNAL   Phytochemistry 4 (1965) 273-284.
  ORGANISM  Blastocladiella emeronii
PATHWAY     PATH: map00471  D-Glutamine and D-glutamate metabolism
            PATH: map00910  Nitrogen metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.35
            ExPASy - ENZYME nomenclature database: 3.5.1.35
            ExplorEnz - The Enzyme Database: 3.5.1.35
            ERGO genome analysis and discovery system: 3.5.1.35
            BRENDA, the Enzyme Database: 3.5.1.35
            CAS: 37289-12-6
///
ENTRY       EC 3.5.1.36                 Enzyme
NAME        N-methyl-2-oxoglutaramate hydrolase;
            5-hydroxy-N-methylpyroglutamate synthase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-methyl-2-oxoglutaramate methylamidohydrolase
REACTION    N-methyl-2-oxoglutaramate + H2O = 2-oxoglutarate + methylamine
            [RN:R01587]
ALL_REAC    R01587
SUBSTRATE   N-methyl-2-oxoglutaramate [CPD:C03623];
            H2O [CPD:C00001]
PRODUCT     2-oxoglutarate [CPD:C00026];
            methylamine [CPD:C00218]
COMMENT     In the reverse reaction, the product cyclizes non-enzymically to
            2-hydroxy-N-methyl-5-oxoproline.
REFERENCE   1  [PMID:5470822]
  AUTHORS   Hersh LB.
  TITLE     5-hydroxy-N-methylpyroglutamate synthetase. Purification and
            mechanism of action.
  JOURNAL   J. Biol. Chem. 245 (1970) 3526-35.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:5808511]
  AUTHORS   Hersh LB, Tsai L, Stadtman ER.
  TITLE     The enzymatic synthesis of 5-hydroxy-N-methylpyroglutamic acid.
  JOURNAL   J. Biol. Chem. 244 (1969) 4677-83.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.36
            ExPASy - ENZYME nomenclature database: 3.5.1.36
            ExplorEnz - The Enzyme Database: 3.5.1.36
            ERGO genome analysis and discovery system: 3.5.1.36
            BRENDA, the Enzyme Database: 3.5.1.36
            CAS: 9073-53-4
///
ENTRY       EC 3.5.1.37       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
COMMENT     Deleted entry: 4-L-aspartylglycosylamine amidohydrolase. Identical
            with EC 3.5.1.26 N4-(beta-N-acetylglucosaminyl)-L-asparaginase (EC
            3.5.1.37 created 1972, deleted 1976)
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.37
            ExPASy - ENZYME nomenclature database: 3.5.1.37
            ExplorEnz - The Enzyme Database: 3.5.1.37
            ERGO genome analysis and discovery system: 3.5.1.37
            BRENDA, the Enzyme Database: 3.5.1.37
///
ENTRY       EC 3.5.1.38                 Enzyme
NAME        glutamin-(asparagin-)ase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     L-glutamine(L-asparagine) amidohydrolase
REACTION    L-glutamine + H2O = L-glutamate + NH3 [RN:R00256]
ALL_REAC    R00256;
            (other) R00485 R00490 R01579 R06134
SUBSTRATE   L-glutamine [CPD:C00064];
            H2O [CPD:C00001]
PRODUCT     L-glutamate [CPD:C00025];
            NH3 [CPD:C00014]
COMMENT     L-Asparagine is hydrolysed at 0.8 of the rate of L-glutamine; the
            D-isomers are also hydrolysed, but more slowly.
REFERENCE   1  [PMID:5017769]
  AUTHORS   Roberts J, Holcenberg JS, Dolowy WC.
  TITLE     Isolation, crystallization, and properties of Achromobacteraceae
            glutaminase-asparaginase with antitumor activity.
  JOURNAL   J. Biol. Chem. 247 (1972) 84-90.
  ORGANISM  Achromobacferaceae sp.
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00252  Alanine and aspartate metabolism
            PATH: map00471  D-Glutamine and D-glutamate metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K05597  glutamin-(asparagin-)ase
GENES       PAE: PA1337(ansB)
            PAU: PA14_46970(ansB)
            PPU: PP_2453(ansA)
            PPF: Pput_3237
            PFL: PFL_2099(ansB)
            PEN: PSEEN1951(aspQ)
            ACI: ACIAD2088(aspQ)
            DNO: DNO_0393
            REU: Reut_A1812
            REH: H16_A1910(ansA) H16_A2280
            RME: Rmet_1583
            BXE: Bxe_B2492
            POL: Bpro_4206
            PNA: Pnap_0442
            AAV: Aave_4182
            AJS: Ajs_3863
            MPT: Mpe_A1913
            GFO: GFO_1213
STRUCTURES  PDB: 1DJO  1DJP  4PGA  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.38
            ExPASy - ENZYME nomenclature database: 3.5.1.38
            ExplorEnz - The Enzyme Database: 3.5.1.38
            ERGO genome analysis and discovery system: 3.5.1.38
            BRENDA, the Enzyme Database: 3.5.1.38
            CAS: 39335-03-0
///
ENTRY       EC 3.5.1.39                 Enzyme
NAME        alkylamidase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-methylhexanamide amidohydrolase
REACTION    N-methylhexanamide + H2O = hexanoate + methylamine [RN:R03620]
ALL_REAC    R03620
SUBSTRATE   N-methylhexanamide [CPD:C02722];
            H2O [CPD:C00001]
PRODUCT     hexanoate [CPD:C01585];
            methylamine [CPD:C00218]
COMMENT     The enzyme hydrolyses N-monosubstituted and N,N-disubstituted
            amides, and there is some activity towards primary amides. It has
            little or no activity towards short-chain substrates.
REFERENCE   1  [PMID:5141674]
  AUTHORS   Chen PR, Dauterman WC.
  TITLE     Alkylamidase of sheep liver.
  JOURNAL   Biochim. Biophys. Acta. 250 (1971) 216-23.
  ORGANISM  sheep
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.39
            ExPASy - ENZYME nomenclature database: 3.5.1.39
            ExplorEnz - The Enzyme Database: 3.5.1.39
            ERGO genome analysis and discovery system: 3.5.1.39
            BRENDA, the Enzyme Database: 3.5.1.39
            CAS: 62213-19-8
///
ENTRY       EC 3.5.1.40                 Enzyme
NAME        acylagmatine amidase;
            acylagmatine amidohydrolase;
            acylagmatine deacylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     benzoylagmatine amidohydrolase
REACTION    benzoylagmatine + H2O = benzoate + agmatine [RN:R01425]
ALL_REAC    R01425
SUBSTRATE   benzoylagmatine [CPD:C02253];
            H2O [CPD:C00001]
PRODUCT     benzoate [CPD:C00180];
            agmatine [CPD:C00179]
COMMENT     Also acts on acetylagmatine, propanoylagmatine and bleomycin B2
REFERENCE   1
  AUTHORS   Umezawa, H., Takahashi, Y., Fujii, A., Saino, T., Shirai, T. and
            Takita, T.
  TITLE     Preparation of bleomycinic acid. Hydrolysis of bleomycin B2 by a
            Fusarium acylagmatine amidohydrolase.
  JOURNAL   J. Antibiot. 26 (1974) 117-119.
  ORGANISM  Fusarium anguioides
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.40
            ExPASy - ENZYME nomenclature database: 3.5.1.40
            ExplorEnz - The Enzyme Database: 3.5.1.40
            ERGO genome analysis and discovery system: 3.5.1.40
            BRENDA, the Enzyme Database: 3.5.1.40
            CAS: 39419-74-4
///
ENTRY       EC 3.5.1.41                 Enzyme
NAME        chitin deacetylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     chitin amidohydrolase
REACTION    chitin + H2O = chitosan + acetate [RN:R02333 R06241]
ALL_REAC    R02333 R06241(G)
SUBSTRATE   chitin [CPD:C00461];
            H2O [CPD:C00001]
PRODUCT     chitosan [CPD:C00734];
            acetate [CPD:C00033]
COMMENT     Hydrolyses the N-acetamido groups of N-acetyl-D-glucosamine residues
            in chitin.
REFERENCE   1  [PMID:4826874]
  AUTHORS   Araki Y, Ito E.
  TITLE     A pathway of chitosan formation in Mucor rouxii: enzymatic
            deacetylation of chitin.
  JOURNAL   Biochem. Biophys. Res. Commun. 56 (1974) 669-75.
  ORGANISM  Mucor rouxii
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K01452  chitin deacetylase
GENES       SCE: YLR307W(CDA1) YLR308W(CDA2)
            AGO: AGOS_ADL036C
            PIC: PICST_43807(CDA2)
            AFM: AFUA_6G10430
            UMA: UM02019.1
            SPE: Spro_0916
            PPF: Pput_1582
            PMY: Pmen_2758
            MMW: Mmwyl1_0469
            BUR: Bcep18194_A5060
            HAR: HEAR2877
            SMD: Smed_4489 Smed_4618
            OAN: Oant_0449
            XAU: Xaut_3290 Xaut_3452
            RSQ: Rsph17025_3035
            ACR: Acry_1163
            BCZ: BCZK1658 BCZK1778(pdaA) BCZK1791
            BTK: BT9727_1795(pdaA) BT9727_1808
            BTL: BALH_1615 BALH_1738(pdaA) BALH_1749
            LBR: LVIS_0276
            FAL: FRAAL1746 FRAAL4911
            AVA: Ava_1295 Ava_4797
            CHU: CHU_0603 CHU_3339(yxkH)
STRUCTURES  PDB: 2IW0  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.41
            ExPASy - ENZYME nomenclature database: 3.5.1.41
            ExplorEnz - The Enzyme Database: 3.5.1.41
            ERGO genome analysis and discovery system: 3.5.1.41
            BRENDA, the Enzyme Database: 3.5.1.41
            CAS: 56379-60-3
///
ENTRY       EC 3.5.1.42                 Enzyme
NAME        nicotinamide-nucleotide amidase;
            NMN deamidase;
            nicotinamide mononucleotide deamidase;
            nicotinamide mononucleotide amidohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     nicotinamide-D-ribonucleotide amidohydrolase
REACTION    beta-nicotinamide D-ribonucleotide + H2O = beta-nicotinate
            D-ribonucleotide + NH3 [RN:R02322]
ALL_REAC    R02322;
            (other) R06134
SUBSTRATE   beta-nicotinamide D-ribonucleotide [CPD:C00455];
            H2O [CPD:C00001]
PRODUCT     beta-nicotinate D-ribonucleotide [CPD:C01185];
            NH3 [CPD:C00014]
COMMENT     Also acts more slowly on beta-nicotinamide D-ribonucleoside.
REFERENCE   1  [PMID:4144084]
  AUTHORS   Imai T.
  TITLE     Purification and properties of nicotinamide mononucleotide
            amidohydrolase from Azotobacter vinelandii.
  JOURNAL   J. Biochem. (Tokyo). 73 (1973) 139-53.
  ORGANISM  Azotobacter vinelandii
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.42
            ExPASy - ENZYME nomenclature database: 3.5.1.42
            ExplorEnz - The Enzyme Database: 3.5.1.42
            ERGO genome analysis and discovery system: 3.5.1.42
            BRENDA, the Enzyme Database: 3.5.1.42
            CAS: 37355-58-1
///
ENTRY       EC 3.5.1.43                 Enzyme
NAME        peptidyl-glutaminase;
            peptidoglutaminase I;
            peptideglutaminase;
            peptidoglutaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     peptidyl-L-glutamine amidohydrolase
REACTION    alpha-N-peptidyl-L-glutamine + H2O = alpha-N-peptidyl-L-glutamate +
            NH3 [RN:R04341]
ALL_REAC    R04341;
            (other) R06134
SUBSTRATE   alpha-N-peptidyl-L-glutamine [CPD:C03905];
            H2O [CPD:C00001]
PRODUCT     alpha-N-peptidyl-L-glutamate [CPD:C03904];
            NH3 [CPD:C00014]
COMMENT     Specific for the hydrolysis of the gamma-amide of glutamine
            substituted at the alpha-amino group, e.g., glycyl-L-glutamine,
            N-acetyl-L-glutamine and L-leucylglycyl-L-glutamine.
REFERENCE   1  [PMID:4928623]
  AUTHORS   Kikuchi M, Hayashida H, Nakano E, Sakaguchi K.
  TITLE     Peptidoglutaminase. Enzymes for selective deamidation of gamma-amide
            of peptide-bound glutamine.
  JOURNAL   Biochemistry. 10 (1971) 1222-9.
  ORGANISM  Bacillus circulans
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.43
            ExPASy - ENZYME nomenclature database: 3.5.1.43
            ExplorEnz - The Enzyme Database: 3.5.1.43
            ERGO genome analysis and discovery system: 3.5.1.43
            BRENDA, the Enzyme Database: 3.5.1.43
            CAS: 37228-70-9
///
ENTRY       EC 3.5.1.44                 Enzyme
NAME        protein-glutamine glutaminase;
            peptidoglutaminase II;
            glutaminyl-peptide glutaminase;
            destabilase;
            peptidylglutaminase II
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     protein-L-glutamine amidohydrolase
REACTION    protein L-glutamine + H2O = protein L-glutamate + NH3 [RN:R02622]
ALL_REAC    R02622;
            (other) R06134
SUBSTRATE   protein L-glutamine [CPD:C02583];
            H2O [CPD:C00001]
PRODUCT     protein L-glutamate [CPD:C00614];
            NH3 [CPD:C00014]
COMMENT     Specific for the hydrolysis of the gamma-amide of glutamine
            substituted at the carboxyl position or both the alpha-amino and
            carboxyl positions, e.g., L-glutaminylglycine and
            L-phenylalanyl-L-glutaminylglycine.
REFERENCE   1  [PMID:4928623]
  AUTHORS   Kikuchi M, Hayashida H, Nakano E, Sakaguchi K.
  TITLE     Peptidoglutaminase. Enzymes for selective deamidation of gamma-amide
            of peptide-bound glutamine.
  JOURNAL   Biochemistry. 10 (1971) 1222-9.
  ORGANISM  Bacillus circulans
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.44
            ExPASy - ENZYME nomenclature database: 3.5.1.44
            ExplorEnz - The Enzyme Database: 3.5.1.44
            ERGO genome analysis and discovery system: 3.5.1.44
            BRENDA, the Enzyme Database: 3.5.1.44
            CAS: 62213-11-0
///
ENTRY       EC 3.5.1.45       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
COMMENT     Deleted entry: urease (ATP-hydrolysing). Now listed only as EC
            6.3.4.6 urea carboxylase (EC 3.5.1.45 created 1978, deleted 1986)
STRUCTURES  PDB: 1QAZ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.45
            ExPASy - ENZYME nomenclature database: 3.5.1.45
            ExplorEnz - The Enzyme Database: 3.5.1.45
            ERGO genome analysis and discovery system: 3.5.1.45
            BRENDA, the Enzyme Database: 3.5.1.45
///
ENTRY       EC 3.5.1.46                 Enzyme
NAME        6-aminohexanoate-dimer hydrolase;
            6-aminohexanoic acid oligomer hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-(6-aminohexanoyl)-6-aminohexanoate amidohydrolase
REACTION    N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate
            [RN:R00059]
ALL_REAC    R00059
SUBSTRATE   N-(6-aminohexanoyl)-6-aminohexanoate [CPD:C01255];
            H2O [CPD:C00001]
PRODUCT     6-aminohexanoate [CPD:C02378]
COMMENT     Also hydrolyses oligomers of 6-aminohexanoate containing up to six
            residues, but more slowly; the residues are removed sequentially
            from the N-terminus.
REFERENCE   1  [PMID:7262074]
  AUTHORS   Kinoshita S, Terada T, Taniguchi T, Takene Y, Masuda S, Matsunaga N,
            Okada H.
  TITLE     Purification and characterization of 6-aminohexanoic-acid-oligomer
            hydrolase of Flavobacterium sp. Ki72.
  JOURNAL   Eur. J. Biochem. 116 (1981) 547-51.
  ORGANISM  Flavobacterium sp.
ORTHOLOGY   KO: K01453  
GENES       PEN: PSEEN1139
            PCR: Pcryo_2128
            SFR: Sfri_3124
            MAQ: Maqu_3282
            TCX: Tcr_0338
            MMW: Mmwyl1_0905
            RSO: RSc1765(RS03025)
            REU: Reut_A1411 Reut_B4421
            RME: Rmet_5283
            BUR: Bcep18194_B0204 Bcep18194_B2479
            BCN: Bcen_5414
            BCH: Bcen2424_5447
            BAM: Bamb_5936
            HAR: HEAR1491 HEAR2830(nylB)
            MMS: mma_2923
            NET: Neut_1073
            AFW: Anae109_3290
            RET: RHE_CH02865(ypch00984)
            RLE: RL3325
            BME: BMEI0945 BMEII0318 BMEII0319
            BMF: BAB2_0257
            OAN: Oant_1381
            BJA: blr3999
            BRA: BRADO0012 BRADO0335 BRADO4091 BRADO6526
            BBT: BBta_0017 BBta_0319 BBta_2408 BBta_4468
            RPD: RPD_0869
            RPE: RPE_4622
            SIT: TM1040_2807
            RDE: RD1_3903(nylB)
            NAR: Saro_0215 Saro_1793
            BAN: BA3346
            BAR: GBAA3346
            BAA: BA_3846
            BAT: BAS3101
            BCE: BC2756 BC3315
            BCA: BCE_3310
            BCZ: BCZK2485 BCZK2998
            BCY: Bcer98_2107
            BTK: BT9727_2520 BT9727_3087
            MMC: Mmcs_1974
            MKM: Mkms_2020
            MJL: Mjls_1954
            RHA: RHA1_ro03034
            AAU: AAur_3953(nylB)
            PAC: PPA1511
            MMA: MM_3157
STRUCTURES  PDB: 1WYB  1WYC  2DCF  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.46
            ExPASy - ENZYME nomenclature database: 3.5.1.46
            ExplorEnz - The Enzyme Database: 3.5.1.46
            ERGO genome analysis and discovery system: 3.5.1.46
            UM-BBD (Biocatalysis/Biodegradation Database): 3.5.1.46
            BRENDA, the Enzyme Database: 3.5.1.46
            CAS: 75216-15-8
///
ENTRY       EC 3.5.1.47                 Enzyme
NAME        N-acetyldiaminopimelate deacetylase;
            N-acetyl-L-diaminopimelic acid deacylase;
            N-acetyl-LL-diaminopimelate deacylase;
            6-N-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N6-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase
REACTION    N-acetyl-LL-2,6-diaminoheptanedioate + H2O = acetate +
            LL-2,6-diaminoheptanedioate [RN:R02733]
ALL_REAC    R02733
SUBSTRATE   N-acetyl-LL-2,6-diaminoheptanedioate [CPD:C04390];
            H2O [CPD:C00001]
PRODUCT     acetate [CPD:C00033];
            LL-2,6-diaminoheptanedioate [CPD:C00666]
REFERENCE   1
  AUTHORS   Bartlett, A.T.M. and White, P.J.
  TITLE     Species of Bacillus that make a vegetative peptidoglycan containing
            lysine lack diaminopimelate epimerase but have diaminopimelate
            dehydrogenase.
  JOURNAL   J. Gen. Microbiol. 131 (1985) 2145-2152.
REFERENCE   2
  AUTHORS   Saleh, F. and White, P.J.
  TITLE     Metabolism of DD-2,6-diaminopimelic acid by a
            diaminopimelate-requiring mutant of Bacillus megaterium.
  JOURNAL   J. Gen. Microbiol. 115 (1979) 95-100.
  ORGANISM  Bacillus megaterium
REFERENCE   3  [PMID:4962540]
  AUTHORS   Sundharadas G, Gilvarg C.
  TITLE     Biosynthesis of alpha,epsilon-diaminopimelic acid in Bacillus
            megaterium.
  JOURNAL   J. Biol. Chem. 242 (1967) 3983-4.
  ORGANISM  Bacillus megaterium
PATHWAY     PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K05823  N-acetyldiaminopimelate deacetylase
GENES       BSU: BG13302(ykuR)
            BHA: BH2668
            BAN: BA4193
            BAR: GBAA4193
            BAA: BA_4657
            BAT: BAS3890
            BCE: BC3980
            BCA: BCE_4029
            BCZ: BCZK3738
            BTK: BT9727_3722
            BLI: BL05143
            BLD: BLi01633(ykuR)
            BCL: ABC2431
            OIH: OB1403
            GKA: GK1050
            LMO: lmo1012
            LMF: LMOf2365_1033
            LIN: lin1011
            LLA: L80177(yciA)
            LLC: LACR_0294
            LLM: llmg_0292(hipO1)
            SPN: SP_2096
            SPR: spr1906(hipO)
            SMU: SMU.318
            STC: str1838(hipO3)
            STL: stu1838(hipO3)
            SSA: SSA_2173(hipO)
            LPL: lp_2263
            LAC: LBA0853
            LSL: LSL_0469
            LCA: LSEI_0096
            EFA: EF1134
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.47
            ExPASy - ENZYME nomenclature database: 3.5.1.47
            ExplorEnz - The Enzyme Database: 3.5.1.47
            ERGO genome analysis and discovery system: 3.5.1.47
            BRENDA, the Enzyme Database: 3.5.1.47
            CAS: 99193-93-8
///
ENTRY       EC 3.5.1.48                 Enzyme
NAME        acetylspermidine deacetylase;
            N8-monoacetylspermidine deacetylase;
            N8-acetylspermidine deacetylase;
            N-acetylspermidine deacetylase;
            N1-acetylspermidine amidohydrolase (incorrect);
            8-N-acetylspermidine amidohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N8-acetylspermidine amidohydrolase
REACTION    N8-acetylspermidine + H2O = acetate + spermidine [RN:R07300]
ALL_REAC    R07300;
            (other) R01916
SUBSTRATE   N8-acetylspermidine [CPD:C01029];
            H2O [CPD:C00001]
PRODUCT     acetate [CPD:C00033];
            spermidine [CPD:C00315]
COMMENT     It was initially thought that N1-acetylspermidine was the substrate
            for this deacetylase reaction [1] but this has since been disproved
            by Marchant et al. [3].
REFERENCE   1  [PMID:28089]
  AUTHORS   Libby PR.
  TITLE     Properties of an acetylspermidine deacetylase from rat liver.
  JOURNAL   Arch. Biochem. Biophys. 188 (1978) 360-3.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:708044]
  AUTHORS   Blankenship J.
  TITLE     Deacetylation of N8-acetylspermidine by subcellular fractions of rat
            tissue.
  JOURNAL   Arch. Biochem. Biophys. 189 (1978) 20-7.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:3955076]
  AUTHORS   Marchant P, Manneh VA, Blankenship J.
  TITLE     N1-acetylspermidine is not a substrate for N-acetylspermidine
            deacetylase.
  JOURNAL   Biochim. Biophys. Acta. 881 (1986) 297-9.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K01454  
GENES       PIC: PICST_34373(HOS3) PICST_81035(RPD3)
            CAL: CaO19_2834(CaO19.2834)
            AFM: AFUA_4G04290
            RET: RHE_CH00917
            RLE: RL0977
            BME: BMEI1504
            BMF: BAB1_0456
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.48
            ExPASy - ENZYME nomenclature database: 3.5.1.48
            ExplorEnz - The Enzyme Database: 3.5.1.48
            ERGO genome analysis and discovery system: 3.5.1.48
            BRENDA, the Enzyme Database: 3.5.1.48
            CAS: 67339-07-5
///
ENTRY       EC 3.5.1.49                 Enzyme
NAME        formamidase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     formamide amidohydrolase
REACTION    formamide + H2O = formate + NH3 [RN:R00524]
ALL_REAC    R00524
SUBSTRATE   formamide [CPD:C00488];
            H2O [CPD:C00001]
PRODUCT     formate [CPD:C00058];
            NH3 [CPD:C00014]
COMMENT     Also acts, more slowly, on acetamide, propanamide and butanamide.
REFERENCE   1
  AUTHORS   Clarke, P.H.
  TITLE     The aliphatic amidases of Pseudomonas aeruginosa.
  JOURNAL   Adv. Microb. Physiol. 4 (1970) 179-222.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   2
  AUTHORS   Friedich, C.G. and Mitrenga, G.
  TITLE     Utilization of aliphatic amides and formation of two different
            amidases by Alcaligenes eutrophus.
  JOURNAL   J. Gen. Microbiol. 125 (1981) 367-374.
  ORGANISM  Alcaligenes eutrophus
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K01455  formamidase
GENES       OSA: 4326894
            PIC: PICST_28914(FRM1)
            ANI: AN4577.2
            AFM: AFUA_2G02020
            AOR: AO090011000472
            PST: PSPTO_4073(fmdA)
            SDE: Sde_2970
            MAQ: Maqu_3860
            ABO: ABO_1978(fmdA)
            REH: H16_B0072(fmdA1) H16_B0473(fmdR) H16_B0476(fmdA2)
            BXE: Bxe_B1706
            BVI: Bcep1808_7168
            BCN: Bcen_3737
            BCH: Bcen2424_4631
            BPE: BP1516(fmdA)
            BPA: BPP1189(fmdA)
            BBR: BB1405(fmdA)
            POL: Bpro_0569
            MPT: Mpe_A3592
            HAR: HEAR1452
            MMS: mma_1893(fmdA)
            MFA: Mfla_1777
            DVL: Dvul_1889
            RLE: pRL100351(amiF) pRL110447
            BJA: blr0972
            BRA: BRADO6892(fmdA) BRADO7112(amiF)
            BBT: BBta_0659(fmdA)
            RPA: RPA1255(fmdA)
            RPB: RPB_1257
            RPD: RPD_3859
            RPE: RPE_4597
            RSP: RSP_3508
            RDE: RD1_1494(fmdA) RD1_3602(fmdA)
            PDE: Pden_3569
            SWI: Swit_0965
            GBE: GbCGDNIH1_1831
            GKA: GK1391
            MSM: MSMEG_0484 MSMEG_3403 MSMEG_4367 MSMEG_5335
            MMC: Mmcs_2262
            MKM: Mkms_2309
            MJL: Mjls_2301
            RHA: RHA1_ro02124 RHA1_ro03918
            SEN: SACE_1932
            RXY: Rxyl_2658 Rxyl_2662
            SYD: Syncc9605_2611 Syncc9605_2612
            HMA: pNG7060(fmdA)
            NPH: NP6204A(fmdA)
            MSE: Msed_0465
STRUCTURES  PDB: 2DYU  2DYV  2E2K  2E2L  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.49
            ExPASy - ENZYME nomenclature database: 3.5.1.49
            ExplorEnz - The Enzyme Database: 3.5.1.49
            ERGO genome analysis and discovery system: 3.5.1.49
            BRENDA, the Enzyme Database: 3.5.1.49
            CAS: 9013-59-6
///
ENTRY       EC 3.5.1.50                 Enzyme
NAME        pentanamidase;
            valeramidase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     pentanamide amidohydrolase
REACTION    pentanamide + H2O = pentanoate + NH3 [RN:R02938]
ALL_REAC    R02938
SUBSTRATE   pentanamide [CPD:C01842];
            H2O [CPD:C00001]
PRODUCT     pentanoate [CPD:C00803];
            NH3 [CPD:C00014]
COMMENT     Also acts, more slowly, on other short-chain aliphatic amides.
            Different from EC 3.5.1.49 formamidase.
REFERENCE   1
  AUTHORS   Friedich, C.G. and Mitrenga, G.
  TITLE     Utilization of aliphatic amides and formation of two different
            amidases by Alcaligenes eutrophus.
  JOURNAL   J. Gen. Microbiol. 125 (1981) 367-374.
  ORGANISM  Alcaligenes eutrophus
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.50
            ExPASy - ENZYME nomenclature database: 3.5.1.50
            ExplorEnz - The Enzyme Database: 3.5.1.50
            ERGO genome analysis and discovery system: 3.5.1.50
            BRENDA, the Enzyme Database: 3.5.1.50
            CAS: 81032-50-0
///
ENTRY       EC 3.5.1.51                 Enzyme
NAME        4-acetamidobutyryl-CoA deacetylase;
            aminobutyryl-CoA thiolesterase;
            deacetylase-thiolesterase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     4-acetamidobutanoyl-CoA amidohydrolase
REACTION    4-acetamidobutanoyl-CoA + H2O = acetate + 4-aminobutanoyl-CoA
            [RN:R04056]
ALL_REAC    R04056
SUBSTRATE   4-acetamidobutanoyl-CoA [CPD:C03357];
            H2O [CPD:C00001]
PRODUCT     acetate [CPD:C00033];
            4-aminobutanoyl-CoA [CPD:C02801]
COMMENT     The enzyme also hydrolyses 4-aminobutanoyl-CoA to aminobutanoate and
            coenzyme A.
REFERENCE   1  [PMID:6788773]
  AUTHORS   Ohsugi M, Kahn J, Hensley C, Chew S, Barker HA.
  TITLE     Metabolism of L-beta-lysine by a Pseudomonas. Purification and
            properties of a deacetylase-thiolesterase utilizing
            4-acetamidobutyryl CoA and related compounds.
  JOURNAL   J. Biol. Chem. 256 (1981) 7642-51.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.51
            ExPASy - ENZYME nomenclature database: 3.5.1.51
            ExplorEnz - The Enzyme Database: 3.5.1.51
            ERGO genome analysis and discovery system: 3.5.1.51
            BRENDA, the Enzyme Database: 3.5.1.51
///
ENTRY       EC 3.5.1.52                 Enzyme
NAME        peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase;
            glycopeptide N-glycosidase;
            glycopeptidase;
            N-oligosaccharide glycopeptidase;
            N-glycanase;
            Jack-bean glycopeptidase;
            PNGase A;
            PNGase F
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-linked-glycopeptide-(N-acetyl-beta-D-glucosaminyl)-L-asparagine
            amidohydrolase
REACTION    Hydrolysis of a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in
            which the glucosamine residue may be further glycosylated, to yield
            a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide
            containing an aspartate residue
COMMENT     Does not act on (GlcNAc)Asn, because it requires the presence of
            more than two amino-acid residues in the substrate [cf. EC 3.5.1.26,
            N4-(beta-N-acetylglucosaminyl)-L-asparaginase]. The plant enzyme was
            previously erroneously listed as EC 3.2.2.18.
REFERENCE   1  [PMID:7287707]
  AUTHORS   Plummer TH Jr, Tarentino AL.
  TITLE     Facile cleavage of complex oligosaccharides from glycopeptides by
            almond emulsin peptide: N-glycosidase.
  JOURNAL   J. Biol. Chem. 256 (1981) 10243-6.
REFERENCE   2  [PMID:901470]
  AUTHORS   Takahashi N.
  TITLE     Demonstration of a new amidase acting on glycopeptides.
  JOURNAL   Biochem. Biophys. Res. Commun. 76 (1977) 1194-201.
REFERENCE   3  [PMID:738997]
  AUTHORS   Takahashi N, Nishibe H.
  TITLE     Some characteristics of a new glycopeptidase acting on
            aspartylglycosylamine linkages.
  JOURNAL   J. Biochem. (Tokyo). 84 (1978) 1467-73.
REFERENCE   4  [PMID:4063349]
  AUTHORS   Tarentino AL, Gomez CM, Plummer TH Jr.
  TITLE     Deglycosylation of asparagine-linked glycans by
            peptide:N-glycosidase F.
  JOURNAL   Biochemistry. 24 (1985) 4665-71.
  ORGANISM  Flavobacterium meningosepticum
ORTHOLOGY   KO: K01456  
GENES       HSA: 55768(NGLY1)
            PTR: 460233(NGLY1)
            GGA: 420655(RCJMB04_17c15)
            DRE: 553627(zgc:110561)
            DME: Dmel_CG7865
            ATH: AT5G49570
            OSA: 4343301
            CGR: CAGL0H05753g
STRUCTURES  PDB: 1PGS  1PNF  1PNG  1X3W  1X3Z  2D5U  2F4M  2F4O  2G9F  2G9G  
                 2HPJ  2HPL  2I74  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.52
            ExPASy - ENZYME nomenclature database: 3.5.1.52
            ExplorEnz - The Enzyme Database: 3.5.1.52
            ERGO genome analysis and discovery system: 3.5.1.52
            BRENDA, the Enzyme Database: 3.5.1.52
            CAS: 83534-39-8
///
ENTRY       EC 3.5.1.53                 Enzyme
NAME        N-carbamoylputrescine amidase;
            carbamoylputrescine hydrolase;
            NCP
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-carbamoylputrescine amidohydrolase
REACTION    N-carbamoylputrescine + H2O = putrescine + CO2 + NH3 [RN:R01152]
ALL_REAC    R01152
SUBSTRATE   N-carbamoylputrescine [CPD:C00436];
            H2O [CPD:C00001]
PRODUCT     putrescine [CPD:C00134];
            CO2 [CPD:C00011];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Yanagisawa, H. and Suzuki, Y.
  TITLE     Preparation and properties of N-carbamylputrescine amidohydrolase
            from maize shoots.
  JOURNAL   Phytochemistry 21 (1982) 2201-2203.
  ORGANISM  Zea mays [GN:ezma]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
GENES       PAP: PSPA7_0384(aguB)
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.53
            ExPASy - ENZYME nomenclature database: 3.5.1.53
            ExplorEnz - The Enzyme Database: 3.5.1.53
            ERGO genome analysis and discovery system: 3.5.1.53
            BRENDA, the Enzyme Database: 3.5.1.53
            CAS: 85030-69-9
///
ENTRY       EC 3.5.1.54                 Enzyme
NAME        allophanate hydrolase;
            allophanate lyase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     urea-1-carboxylate amidohydrolase
REACTION    urea-1-carboxylate + H2O = 2 CO2 + 2 NH3 [RN:R00005]
ALL_REAC    R00005
SUBSTRATE   urea-1-carboxylate [CPD:C01010];
            H2O [CPD:C00001]
PRODUCT     CO2 [CPD:C00011];
            NH3 [CPD:C00014]
COMMENT     The yeast enzyme (but not that from green algae) also catalyses the
            reaction of EC 6.3.4.6, urea carboxylase, thus bringing about the
            hydrolysis of urea to CO2 and NH3 in the presence of ATP and
            bicarbonate.
REFERENCE   1
  AUTHORS   Maitz, G.S., Haas, E.M. and Castric, P.A.
  TITLE     Purification and properties of the allophanate hydrolase from
            Chlamydomonas reinhardii.
  JOURNAL   Biochim. Biophys. Acta 714 (1982) 486-491.
  ORGANISM  Chlamydomonas reinhardii
REFERENCE   2  [PMID:4556303]
  AUTHORS   Roon RJ, Levenberg B.
  TITLE     Urea amidolyase. I. Properties of the enzyme from Candida utilis.
  JOURNAL   J. Biol. Chem. 247 (1972) 4107-13.
  ORGANISM  Candida utilis
REFERENCE   3  [PMID:6124544]
  AUTHORS   Sumrada RA, Cooper TG.
  TITLE     Urea carboxylase and allophanate hydrolase are components of a
            multifunctional protein in yeast.
  JOURNAL   J. Biol. Chem. 257 (1982) 9119-27.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   4  [PMID:15796980]
  AUTHORS   Kanamori T, Kanou N, Kusakabe S, Atomi H, Imanaka T.
  TITLE     Allophanate hydrolase of Oleomonas sagaranensis involved in an
            ATP-dependent degradation pathway specific to urea.
  JOURNAL   FEMS. Microbiol. Lett. 245 (2005) 61-5.
  ORGANISM  Oleomonas sagaranensis
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00791  Atrazine degradation
ORTHOLOGY   KO: K01457  allophanate hydrolase
GENES       SCE: YBR208C(DUR1,2)
            AGO: AGOS_ADR051C
            PIC: PICST_28452(DUR1)
            CGR: CAGL0M05533g
            TET: TTHERM_00361400
            ECA: ECA1917
            HSO: HS_0025 HS_0026
            PSB: Psyr_2720
            PEN: PSEEN4016
            ACI: ACIAD2518
            PHA: PSHAa1442
            PIN: Ping_3549
            TCX: Tcr_1792
            AEH: Mlg_1917
            ABO: ABO_1892(uahA)
            CVI: CV_3170
            RSO: RSc2170(RS01429)
            REU: Reut_A0088 Reut_A2450
            REH: H16_A0124 H16_A0125 H16_B1758(alpH)
            RME: Rmet_0063
            BVI: Bcep1808_3855
            BUR: Bcep18194_A6284 Bcep18194_A6385
            BCN: Bcen_2424
            BPM: BURPS1710b_0448
            BTE: BTH_I0229
            RFR: Rfer_0126
            NET: Neut_2470
            RET: RHE_PC00188 RHE_PE00118
            RLE: RL2460 pRL100433 pRL100434
            RPE: RPE_3038
            RSP: RSP_3449
            JAN: Jann_2804
            RDE: RD1_0244
            HNE: HNE_2123 HNE_2124
            GBE: GbCGDNIH1_1744
            RRU: Rru_A1505
            SUS: Acid_0062
            BPU: BPUM_0383(kipA)
            SAJ: SaurJH9_1665
            SAH: SaurJH1_1699
            CBE: Cbei_2756
            MSM: MSMEG_2187 MSMEG_2189(atzF)
            MMC: Mmcs_1840
            MKM: Mkms_1887
            RHA: RHA1_ro06922
            CMI: CMM_0563 CMM_0564
            AAU: AAur_0186(atzF)
            TFU: Tfu_1968
            FRA: Francci3_2975
            SEN: SACE_1551(alpH) SACE_1552
            GFO: GFO_2121 GFO_2122
            TTH: TTC0624
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.54
            ExPASy - ENZYME nomenclature database: 3.5.1.54
            ExplorEnz - The Enzyme Database: 3.5.1.54
            ERGO genome analysis and discovery system: 3.5.1.54
            UM-BBD (Biocatalysis/Biodegradation Database): 3.5.1.54
            BRENDA, the Enzyme Database: 3.5.1.54
            CAS: 79121-96-3
///
ENTRY       EC 3.5.1.55                 Enzyme
NAME        long-chain-fatty-acyl-glutamate deacylase;
            long-chain aminoacylase;
            long-chain-fatty-acyl-glutamate deacylase;
            long-chain acylglutamate amidase;
            N-acyl-D-glutamate deacylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-long-chain-fatty-acyl-L-glutamate amidohydrolase
REACTION    N-long-chain-fatty-acyl-L-glutamate + H2O = a long-chain carboxylate
            + L-glutamate [RN:R02040]
ALL_REAC    R02040
SUBSTRATE   N-long-chain-fatty-acyl-L-glutamate [CPD:C04305];
            H2O [CPD:C00001]
PRODUCT     long-chain carboxylate [CPD:C00347];
            L-glutamate [CPD:C00025]
COMMENT     Does not act on acyl derivates of other amino acids. Optimum chain
            length of acyl residue is 12 to 16.
REFERENCE   1  [PMID:7096313]
  AUTHORS   Fukuda H, Iwade S, Kimura A.
  TITLE     A new enzyme: long acyl aminoacylase from Pseudomonas diminuta.
  JOURNAL   J. Biochem. (Tokyo). 91 (1982) 1731-8.
  ORGANISM  Pseudomonas diminuta
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.55
            ExPASy - ENZYME nomenclature database: 3.5.1.55
            ExplorEnz - The Enzyme Database: 3.5.1.55
            ERGO genome analysis and discovery system: 3.5.1.55
            BRENDA, the Enzyme Database: 3.5.1.55
            CAS: 82249-69-2
///
ENTRY       EC 3.5.1.56                 Enzyme
NAME        N,N-dimethylformamidase;
            dimethylformamidase;
            DMFase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N,N-dimethylformamide amidohydrolase
REACTION    N,N-dimethylformamide + H2O = dimethylamine + formate [RN:R02509]
ALL_REAC    R02509
SUBSTRATE   N,N-dimethylformamide [CPD:C03134];
            H2O [CPD:C00001]
PRODUCT     dimethylamine [CPD:C00543];
            formate [CPD:C00058]
COFACTOR    Iron [CPD:C00023]
COMMENT     An iron protein. Also acts on N-ethylformamide and
            N-methyl-formamide and, more slowly, on N,N-diethylformamide,
            N,N-dimethylacetamide and unsubstituted acyl amides.
REFERENCE   1  [PMID:3732281]
  AUTHORS   Schar HP, Holzmann W, Ramos Tombo GM, Ghisalba O.
  TITLE     Purification and characterization of N,N-dimethylformamidase from
            Pseudomonas DMF 3/3.
  JOURNAL   Eur. J. Biochem. 158 (1986) 469-75.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K03418  N,N-dimethylformamidase
GENES       BJA: blr3549 blr3932
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.56
            ExPASy - ENZYME nomenclature database: 3.5.1.56
            ExplorEnz - The Enzyme Database: 3.5.1.56
            ERGO genome analysis and discovery system: 3.5.1.56
            BRENDA, the Enzyme Database: 3.5.1.56
            CAS: 104645-73-0
///
ENTRY       EC 3.5.1.57                 Enzyme
NAME        tryptophanamidase;
            tryptophan aminopeptidase;
            L-tryptophan aminopeptidase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     L-tryptophanamide amidohydrolase
REACTION    L-tryptophanamide + H2O = L-tryptophan + NH3 [RN:R00682]
ALL_REAC    R00682
SUBSTRATE   L-tryptophanamide [CPD:C00977];
            H2O [CPD:C00001]
PRODUCT     L-tryptophan [CPD:C00078];
            NH3 [CPD:C00014]
COFACTOR    Manganese [CPD:C00034]
COMMENT     Requires Mn2+. Also acts on N-ethylformamide and L-tyrosinamide, and
            on some tryptophan dipeptides.
REFERENCE   1
  AUTHORS   Iwayama, A., Kimura, T., Adachi, O. and Ameyama, M.
  TITLE     Crystallization and characterization of a novel aminopeptidase from
            Trichosporon cutaneum.
  JOURNAL   Agric. Biol. Chem. 47 (1983) 2483-2493.
  ORGANISM  Trichosporon cutaneum
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.57
            ExPASy - ENZYME nomenclature database: 3.5.1.57
            ExplorEnz - The Enzyme Database: 3.5.1.57
            ERGO genome analysis and discovery system: 3.5.1.57
            BRENDA, the Enzyme Database: 3.5.1.57
            CAS: 76689-19-5
///
ENTRY       EC 3.5.1.58                 Enzyme
NAME        N-benzyloxycarbonylglycine hydrolase;
            benzyloxycarbonylglycine hydrolase;
            Nalpha-carbobenzoxyamino acid amidohydrolase;
            Nalpha-benzyloxycarbonyl amino acid urethane hydrolase;
            Nalpha-benzyloxycarbonyl amino acid urethane hydrolase I
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-benzyloxycarbonylglycine urethanehydrolase
REACTION    N-benzyloxycarbonylglycine + H2O = benzyl alcohol + CO2 + glycine
            [RN:R02551]
ALL_REAC    R02551
SUBSTRATE   N-benzyloxycarbonylglycine [CPD:C03710];
            H2O [CPD:C00001]
PRODUCT     benzyl alcohol [CPD:C00556];
            CO2 [CPD:C00011];
            glycine [CPD:C00037]
COFACTOR    Zinc [CPD:C00038];
            Cobalt [CPD:C00175]
COMMENT     Also acts, more slowly, on N-benzyloxycarbonylalanine, but not on
            the corresponding derivatives of other amino acids or on
            N-benzyloxycarbonylpeptides. Requires Co2+ or Zn2+. cf. EC 3.5.1.64,
            Nalpha-benzyloxycarbonylleucine hydrolase.
REFERENCE   1
  AUTHORS   Murao, S., Matsumura, E. and Kawano, T. Isolation and
            characterization of a novel enzyme, N
  TITLE     alpha-benzyloxycarbonyl amino acid urethane hydrolase, from
            Streptococcus faecalis R ATCC 8043.
  JOURNAL   Agric. Biol. Chem. 49 (1985) 967-972.
  ORGANISM  Streptococcus faecalis
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.58
            ExPASy - ENZYME nomenclature database: 3.5.1.58
            ExplorEnz - The Enzyme Database: 3.5.1.58
            ERGO genome analysis and discovery system: 3.5.1.58
            BRENDA, the Enzyme Database: 3.5.1.58
            CAS: 91930-69-7
///
ENTRY       EC 3.5.1.59                 Enzyme
NAME        N-carbamoylsarcosine amidase;
            carbamoylsarcosine amidase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-carbamoylsarcosine amidohydrolase
REACTION    N-carbamoylsarcosine + H2O = sarcosine + CO2 + NH3 [RN:R01563]
ALL_REAC    R01563
SUBSTRATE   N-carbamoylsarcosine [CPD:C01043];
            H2O [CPD:C00001]
PRODUCT     sarcosine [CPD:C00213];
            CO2 [CPD:C00011];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Deeg, R., Roeder, A., Siedel, J., Gauhl, H. and Ziegenhorn, J.
  TITLE     Process and reagent for the determination of N-carbamoylsarcosine
            with the use of a new enzyme.
  JOURNAL   Chem. Abstr. 101 (1984) 18751.
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K08687  N-carbamoylsarcosine amidase
GENES       SPE: Spro_2308
            REH: H16_A0926
            BBT: BBta_1129
            PDE: Pden_4354
            RXY: Rxyl_2747
            RCA: Rcas_3491
            HWA: HQ1060A(entB)
            NPH: NP1274A(entB_1) NP6214A(entB_3)
STRUCTURES  PDB: 1NBA  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.59
            ExPASy - ENZYME nomenclature database: 3.5.1.59
            ExplorEnz - The Enzyme Database: 3.5.1.59
            ERGO genome analysis and discovery system: 3.5.1.59
            BRENDA, the Enzyme Database: 3.5.1.59
            CAS: 92767-52-7
///
ENTRY       EC 3.5.1.60                 Enzyme
NAME        N-(long-chain-acyl)ethanolamine deacylase;
            N-acylethanolamine amidohydrolase;
            acylethanolamine amidase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-(long-chain-acyl)ethanolamine amidohydrolase
REACTION    N-(long-chain-acyl)ethanolamine + H2O = a long-chain carboxylate +
            ethanolamine [RN:R02041]
ALL_REAC    R02041
SUBSTRATE   N-(long-chain-acyl)ethanolamine [CPD:C04080];
            H2O [CPD:C00001]
PRODUCT     long-chain carboxylate [CPD:C00347];
            ethanolamine [CPD:C00189]
COMMENT     Does not act on N-acylsphingosine or N,O-diacylethanolamine.
REFERENCE   1  [PMID:4055775]
  AUTHORS   Schmid PC, Zuzarte-Augustin ML, Schmid HH.
  TITLE     Properties of rat liver N-acylethanolamine amidohydrolase.
  JOURNAL   J. Biol. Chem. 260 (1985) 14145-9.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.60
            ExPASy - ENZYME nomenclature database: 3.5.1.60
            ExplorEnz - The Enzyme Database: 3.5.1.60
            ERGO genome analysis and discovery system: 3.5.1.60
            BRENDA, the Enzyme Database: 3.5.1.60
            CAS: 99283-61-1
///
ENTRY       EC 3.5.1.61                 Enzyme
NAME        mimosinase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     mimosine amidohydrolase
REACTION    (S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O =
            3-hydroxy-4H-pyrid-4-one + L-serine [RN:R04350]
ALL_REAC    R04350
SUBSTRATE   (S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate
            [CPD:C04771];
            H2O [CPD:C00001]
PRODUCT     3-hydroxy-4H-pyrid-4-one [CPD:C03927];
            L-serine [CPD:C00065]
COMMENT     An enzyme from Leucaena leucocephala leaf, which also contains the
            toxic amino acid, mimosine.
REFERENCE   1
  AUTHORS   Tangendjaja, B., Lowry, J.B. and Wills, R.H.
  TITLE     Isolation of a mimosine degrading enzyme from Leucaena leaf.
  JOURNAL   J. Sci. Food Agric. 37 (1986) 523-526.
  ORGANISM  Leucaena leucocephala
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.61
            ExPASy - ENZYME nomenclature database: 3.5.1.61
            ExplorEnz - The Enzyme Database: 3.5.1.61
            ERGO genome analysis and discovery system: 3.5.1.61
            BRENDA, the Enzyme Database: 3.5.1.61
            CAS: 104118-49-2
///
ENTRY       EC 3.5.1.62                 Enzyme
NAME        acetylputrescine deacetylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-acetylputrescine acetylhydrolase
REACTION    N-acetylputrescine + H2O = acetate + putrescine [RN:R01156]
ALL_REAC    R01156
SUBSTRATE   N-acetylputrescine [CPD:C02714];
            H2O [CPD:C00001]
PRODUCT     acetate [CPD:C00033];
            putrescine [CPD:C00134]
COMMENT     The enzyme from Micrococcus luteus also acts on N8-acetylspermidine
            and acetylcadaverine, but more slowly.
REFERENCE   1
  AUTHORS   Suzuki, O., Ishikawa, Y., Miyazaki, K., Izu, K. and Matsumoto, T.
  TITLE     Acetylputrescine deacetylase from Micrococcus luteus K-11.
  JOURNAL   Biochim. Biophys. Acta 882 (1986) 140-142.
  ORGANISM  Micrococcus luteus
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.62
            ExPASy - ENZYME nomenclature database: 3.5.1.62
            ExplorEnz - The Enzyme Database: 3.5.1.62
            ERGO genome analysis and discovery system: 3.5.1.62
            BRENDA, the Enzyme Database: 3.5.1.62
            CAS: 103679-48-7
///
ENTRY       EC 3.5.1.63                 Enzyme
NAME        4-acetamidobutyrate deacetylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     4-acetamidobutanoate amidohydrolase
REACTION    4-acetamidobutanoate + H2O = acetate + 4-aminobutanoate [RN:R01987]
ALL_REAC    R01987;
            (other) R02276
SUBSTRATE   4-acetamidobutanoate [CPD:C02946];
            H2O [CPD:C00001]
PRODUCT     acetate [CPD:C00033];
            4-aminobutanoate [CPD:C00334]
COMMENT     Also acts on N-acetyl-beta-alanine and 5-acetamidopentanoate.
REFERENCE   1
  AUTHORS   Haywood, G.W. and Large, P.J.
  TITLE     4-Acetamidobutyrate deacetylase in the yeast Candida boidinii grown
            on putrescine or spermidine as sole nitrogen source and its probable
            role in polyamine catabolism.
  JOURNAL   J. Gen. Microbiol. 132 (1986) 7-14.
  ORGANISM  Candida boidinii
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.63
            ExPASy - ENZYME nomenclature database: 3.5.1.63
            ExplorEnz - The Enzyme Database: 3.5.1.63
            ERGO genome analysis and discovery system: 3.5.1.63
            BRENDA, the Enzyme Database: 3.5.1.63
            CAS: 102347-82-0
///
ENTRY       EC 3.5.1.64                 Enzyme
NAME        Nalpha-benzyloxycarbonylleucine hydrolase;
            benzyloxycarbonylleucine hydrolase;
            Nalpha-benzyloxycarbonyl amino acid urethane hydrolase IV;
            alpha-N-benzyloxycarbonyl-L-leucine urethanehydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     Nalpha-benzyloxycarbonyl-L-leucine urethanehydrolase
REACTION    Nalpha-benzyloxycarbonyl-L-leucine + H2O = benzyl alcohol + CO2 +
            L-leucine [RN:R02552]
ALL_REAC    R02552
SUBSTRATE   Nalpha-benzyloxycarbonyl-L-leucine;
            H2O [CPD:C00001]
PRODUCT     benzyl alcohol [CPD:C00556];
            CO2 [CPD:C00011];
            L-leucine [CPD:C00123]
COMMENT     Also acts on Nalpha-t-butoxycarbonyl-L-leucine, and, more slowly, on
            the corresponding derivatives of L-aspartate, L-methionine,
            L-glutamate and L-alanine. cf. EC 3.5.1.58
            N-benzyloxycarbonylglycine hydrolase.
REFERENCE   1
  AUTHORS   Matsumura, E., Shin, T., Murao, S., Sakaguchi, M. and Kawano, T.
  TITLE     A novel enzyme, Nalpha-benzyloxycarbonyl amino acid urethane
            hydrolase IV.
  JOURNAL   Agric. Biol. Chem. 49 (1985) 3643-3645.
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.64
            ExPASy - ENZYME nomenclature database: 3.5.1.64
            ExplorEnz - The Enzyme Database: 3.5.1.64
            ERGO genome analysis and discovery system: 3.5.1.64
            BRENDA, the Enzyme Database: 3.5.1.64
            CAS: 100630-47-5
///
ENTRY       EC 3.5.1.65                 Enzyme
NAME        theanine hydrolase;
            L-theanine amidohydrolase;
            5-N-ethyl-L-glutamine amidohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N5-ethyl-L-glutamine amidohydrolase
REACTION    N5-ethyl-L-glutamine + H2O = L-glutamate + ethylamine [RN:R02930]
ALL_REAC    R02930
SUBSTRATE   N5-ethyl-L-glutamine [CPD:C01047];
            H2O [CPD:C00001]
PRODUCT     L-glutamate [CPD:C00025];
            ethylamine [CPD:C00797]
COMMENT     Also acts on other N-alkyl-L-glutamines.
REFERENCE   1
  AUTHORS   Tsushida, T. and Takeo, T.
  TITLE     An enzyme hydrolyzing L-theanine in tea leaves.
  JOURNAL   Agric. Biol. Chem. 49 (1985) 2913-2917.
  ORGANISM  tea
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.65
            ExPASy - ENZYME nomenclature database: 3.5.1.65
            ExplorEnz - The Enzyme Database: 3.5.1.65
            ERGO genome analysis and discovery system: 3.5.1.65
            BRENDA, the Enzyme Database: 3.5.1.65
            CAS: 99533-51-4
///
ENTRY       EC 3.5.1.66                 Enzyme
NAME        2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase;
            compound B hydrolase;
            alpha-hydroxymethyl-alpha'-(N-acetylaminomethylene)succinic acid
            hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     2-(hydroxymethyl)-3-(acetamidomethylene)succinate amidohydrolase
            (deaminating, decarboxylating)
REACTION    2-(hydroxymethyl)-3-(acetamidomethylene)succinate + 2 H2O = acetate
            + 2-(hydroxymethyl)-4-oxobutanoate + NH3 + CO2 [RN:R04397]
ALL_REAC    R04397
SUBSTRATE   2-(hydroxymethyl)-3-(acetamidomethylene)succinate [CPD:C04690];
            H2O [CPD:C00001]
PRODUCT     acetate [CPD:C00033];
            2-(hydroxymethyl)-4-oxobutanoate [CPD:C04106];
            NH3 [CPD:C00014];
            CO2 [CPD:C00011]
COMMENT     Involved in the degradation of pyridoxin by Pseudomonas and
            Arthrobacter.
REFERENCE   1  [PMID:3972793]
  AUTHORS   Huynh MS, Snell EE.
  TITLE     Enzymes of vitamin B6 degradation. Purification and properties of
            two N-acetylamidohydrolases.
  JOURNAL   J. Biol. Chem. 260 (1985) 2379-83.
  ORGANISM  Pseudomonas sp., Arthrobacter sp.
PATHWAY     PATH: map00750  Vitamin B6 metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.66
            ExPASy - ENZYME nomenclature database: 3.5.1.66
            ExplorEnz - The Enzyme Database: 3.5.1.66
            ERGO genome analysis and discovery system: 3.5.1.66
            BRENDA, the Enzyme Database: 3.5.1.66
            CAS: 95829-26-8
///
ENTRY       EC 3.5.1.67                 Enzyme
NAME        4-methyleneglutaminase;
            4-methyleneglutamine deamidase;
            4-methyleneglutamine amidohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     4-methylene-L-glutamine amidohydrolase
REACTION    4-methylene-L-glutamine + H2O = 4-methylene-L-glutamate + NH3
            [RN:R02712]
ALL_REAC    R02712
SUBSTRATE   4-methylene-L-glutamine [CPD:C01109];
            H2O [CPD:C00001]
PRODUCT     4-methylene-L-glutamate [CPD:C00651];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Ibrahim, S.A., Lea, P.J. and Fowden, L.
  TITLE     Preparation and properties of 4-methyleneglutaminase from the leaves
            of peanut (Arachis hypogaea).
  JOURNAL   Phytochemistry 23 (1984) 1545-1549.
  ORGANISM  Arachis hypogaea
PATHWAY     PATH: map00660  C5-Branched dibasic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.67
            ExPASy - ENZYME nomenclature database: 3.5.1.67
            ExplorEnz - The Enzyme Database: 3.5.1.67
            ERGO genome analysis and discovery system: 3.5.1.67
            BRENDA, the Enzyme Database: 3.5.1.67
            CAS: 86855-36-9
///
ENTRY       EC 3.5.1.68                 Enzyme
NAME        N-formylglutamate deformylase;
            beta-citryl-L-glutamate hydrolase;
            formylglutamate deformylase;
            N-formylglutamate hydrolase;
            beta-citrylglutamate amidase;
            beta-citryl-L-glutamate amidohydrolase;
            beta-citryl-L-glutamate amidase;
            beta-citrylglutamate amidase;
            beta-citryl-L-glutamate-hydrolyzing enzyme
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-formyl-L-glutamate amidohydrolase
REACTION    N-formyl-L-glutamate + H2O = formate + L-glutamate [RN:R00525]
ALL_REAC    R00525
SUBSTRATE   N-formyl-L-glutamate [CPD:C01045];
            H2O [CPD:C00001]
PRODUCT     formate [CPD:C00058];
            L-glutamate [CPD:C00025]
COMMENT     The animal enzyme also acts on beta-citryl-L-glutamate and
            beta-citryl-L-glutamine.
REFERENCE   1  [PMID:3308850]
  AUTHORS   Hu L, Mulfinger LM, Phillips AT.
  TITLE     Purification and properties of formylglutamate amidohydrolase from
            Pseudomonas putida.
  JOURNAL   J. Bacteriol. 169 (1987) 4696-702.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2  [PMID:6414521]
  AUTHORS   Miyake M, Innami T, Kakimoto Y.
  TITLE     A beta-citryl-L-glutamate-hydrolysing enzyme in rat testes.
  JOURNAL   Biochim. Biophys. Acta. 760 (1983) 206-14.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00340  Histidine metabolism
            PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K01458  N-formylglutamate deformylase
GENES       YPI: YpsIP31758_2114(hutG)
            PAP: PSPA7_5824
            PFL: PFL_0410(hutG)
            CPS: CPS_4353
            PHA: PSHAa0429
            REU: Reut_A1246
            REH: H16_A1109(hutG2) H16_A1306(hutG3) H16_A3013(hutG1)
                 H16_A3649(hutG4)
            RME: Rmet_0981 Rmet_2850 Rmet_3507
            BMA: BMA0652(hutG) BMAA1476
            BMV: BMASAVP1_A2360(hutG)
            BML: BMA10299_A2925(hutG)
            BMN: BMA10247_1674(hutG)
            BXE: Bxe_A2941
            BUR: Bcep18194_B0284
            BCN: Bcen_5911
            BCH: Bcen2424_2166
            BPS: BPSL2338 BPSS0285
            BPM: BURPS1710b_2790(hutG) BURPS1710b_A1827
            BPL: BURPS1106A_2716(hutG)
            BPD: BURPS668_2660(hutG)
            BTE: BTH_I1826(hutG)
            BBR: BB4732(hutG)
            RFR: Rfer_4155
            POL: Bpro_1166 Bpro_2708
            RET: RHE_CH03574
            RLE: RL4092
            BME: BMEII0049
            BOV: BOV_A0873(hutG)
            BRA: BRADO1602 BRADO6214
            BBT: BBta_1390 BBta_6453
            RPE: RPE_0707
            SIL: SPOA0448(hutG)
            RDE: RD1_0718(hutG) RD1_1499
            HNE: HNE_2397(hutG)
            ZMO: ZMO1181(hutG)
            GOX: GOX1165 GOX2197
            GBE: GbCGDNIH1_0905
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.68
            ExPASy - ENZYME nomenclature database: 3.5.1.68
            ExplorEnz - The Enzyme Database: 3.5.1.68
            ERGO genome analysis and discovery system: 3.5.1.68
            BRENDA, the Enzyme Database: 3.5.1.68
            CAS: 97286-12-9
///
ENTRY       EC 3.5.1.69                 Enzyme
NAME        glycosphingolipid deacylase;
            glycosphingolipid ceramide deacylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     glycosphingolipid amidohydrolase
REACTION    Hydrolysis of gangliosides and neutral glycosphingolipids, releasing
            fatty acids to form the lyso-derivatives
COMMENT     Does not act on sphingolipids such as ceramide. Not identical with
            EC 3.5.1.23 ceramidase.
REFERENCE   1  [PMID:3360750]
  AUTHORS   Hirabayashi Y, Kimura M, Matsumoto M, Yamamoto K, Kadowaki S,
            Tochikura T.
  TITLE     A novel glycosphingolipid hydrolyzing enzyme, glycosphingolipid
            ceramide deacylase, which cleaves the linkage between the fatty acid
            and sphingosine base in glycosphingolipids.
  JOURNAL   J. Biochem. (Tokyo). 103 (1988) 1-4.
  ORGANISM  Nocardia sp.
ORTHOLOGY   KO: K06014  
GENES       ZMO: ZMO1395(hutG)
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.69
            ExPASy - ENZYME nomenclature database: 3.5.1.69
            ExplorEnz - The Enzyme Database: 3.5.1.69
            ERGO genome analysis and discovery system: 3.5.1.69
            BRENDA, the Enzyme Database: 3.5.1.69
            CAS: 122544-53-0
///
ENTRY       EC 3.5.1.70                 Enzyme
NAME        aculeacin-A deacylase;
            aculeacin A acylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     aculeacin-A amidohydrolase
REACTION    Hydrolysis of the amide bond in aculeacin A and related neutral
            lipopeptide antibiotics, releasing the long-chain fatty acid
            side-chain
REFERENCE   1  [PMID:2760018]
  AUTHORS   Takeshima H, Inokoshi J, Takada Y, Tanaka H, Omura S.
  TITLE     A deacylation enzyme for aculeacin A, a neutral lipopeptide
            antibiotic, from Actinoplanes utahensis: purification and
            characterization.
  JOURNAL   J. Biochem. (Tokyo). 105 (1989) 606-10.
  ORGANISM  Actinoplanes utahensis
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.70
            ExPASy - ENZYME nomenclature database: 3.5.1.70
            ExplorEnz - The Enzyme Database: 3.5.1.70
            ERGO genome analysis and discovery system: 3.5.1.70
            BRENDA, the Enzyme Database: 3.5.1.70
            CAS: 121479-50-3
///
ENTRY       EC 3.5.1.71                 Enzyme
NAME        N-feruloylglycine deacylase;
            N-feruloylglycine hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-feruloylglycine amidohydrolase
REACTION    N-feruloylglycine + H2O = ferulate + glycine [RN:R03579]
ALL_REAC    R03579
SUBSTRATE   N-feruloylglycine [CPD:C02564];
            H2O [CPD:C00001]
PRODUCT     ferulate [CPD:C01494];
            glycine [CPD:C00037]
COMMENT     Hydrolyses a range of L-amino acids from the cinnamoyl and
            substituted cinnamoyl series. Not identical with EC 3.5.1.14
            aminoacylase.
REFERENCE   1
  AUTHORS   Martens, M., Cottenie-Ruysschaert, M., Hanselaer, R., De Cooman, L.,
            CASteele, K.V. and Van Sumere, F.
  TITLE     N-Feruloylglycine amidohydrolase from barley seeds and isolated
            barley embryos.
  JOURNAL   Phytochemistry 27 (1988) 2457-2463.
  ORGANISM  Hordeum vulgare [GN:ehvu], Secale cereale
REFERENCE   2
  AUTHORS   Martens, M., Cottenie-Ruysschaert, M., Hanselaer, R., De Cooman, L.,
            CASteele, K.V. and Van Sumere, F.
  TITLE     Characteristics and specificity of purified N-feruloylglycine
            amidohydrolase from isolated barley embryos.
  JOURNAL   Phytochemistry 27 (1988) 2465-2475.
  ORGANISM  Hordeum vulgare [GN:ehvu]
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.71
            ExPASy - ENZYME nomenclature database: 3.5.1.71
            ExplorEnz - The Enzyme Database: 3.5.1.71
            ERGO genome analysis and discovery system: 3.5.1.71
            BRENDA, the Enzyme Database: 3.5.1.71
            CAS: 118731-84-3
///
ENTRY       EC 3.5.1.72                 Enzyme
NAME        D-benzoylarginine-4-nitroanilide amidase;
            benzoyl-D-arginine arylamidase;
            D-BAPA-ase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-benzoyl-D-arginine-4-nitroanilide amidohydrolase
REACTION    N-benzoyl-D-arginine-4-nitroanilide + H2O = N-benzoyl-D-arginine +
            4-nitroaniline [RN:R04113]
ALL_REAC    R04113
SUBSTRATE   N-benzoyl-D-arginine-4-nitroanilide [CPD:C04303];
            H2O [CPD:C00001]
PRODUCT     N-benzoyl-D-arginine [CPD:C03001];
            4-nitroaniline [CPD:C02126]
REFERENCE   1  [PMID:3142860]
  AUTHORS   Gofshtein-Gandman LV, Keynan A, Milner Y.
  TITLE     Bacteria of the genus Bacillus have a hydrolase stereospecific to
            the D isomer of benzoyl-arginine-p-nitroanilide.
  JOURNAL   J. Bacteriol. 170 (1988) 5895-900.
  ORGANISM  Bacillus subtilis [GN:bsu]
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.72
            ExPASy - ENZYME nomenclature database: 3.5.1.72
            ExplorEnz - The Enzyme Database: 3.5.1.72
            ERGO genome analysis and discovery system: 3.5.1.72
            BRENDA, the Enzyme Database: 3.5.1.72
            CAS: 119345-26-5
///
ENTRY       EC 3.5.1.73                 Enzyme
NAME        carnitinamidase;
            L-carnitinamidase;
            carnitine amidase;
            L-carnitine amidase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     L-carnitinamide amidohydrolase
REACTION    L-carnitinamide + H2O = L-carnitine + NH3 [RN:R01922]
ALL_REAC    R01922
SUBSTRATE   L-carnitinamide [CPD:C02290];
            H2O [CPD:C00001]
PRODUCT     L-carnitine [CPD:C00318];
            NH3 [CPD:C00014]
COMMENT     Does not act on D-carnitinamide.
REFERENCE   1
  AUTHORS   Nakayama, K., Honda, H., Ogawa, Y., Ozawa, T. and Ota, T. Method for
            producing carnitine, L-
  TITLE     carnitinamide hydrolase and method for producing same.
  JOURNAL   Chem. Abstr. 109 (1988) 22873.
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.73
            ExPASy - ENZYME nomenclature database: 3.5.1.73
            ExplorEnz - The Enzyme Database: 3.5.1.73
            ERGO genome analysis and discovery system: 3.5.1.73
            BRENDA, the Enzyme Database: 3.5.1.73
            CAS: 117444-04-9
///
ENTRY       EC 3.5.1.74                 Enzyme
NAME        chenodeoxycholoyltaurine hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     chenodeoxycholoyltaurine amidohydrolase
REACTION    chenodeoxycholoyltaurine + H2O = chenodeoxycholate + taurine
            [RN:R03977]
ALL_REAC    R03977
SUBSTRATE   chenodeoxycholoyltaurine [CPD:C05465];
            H2O [CPD:C00001]
PRODUCT     chenodeoxycholate [CPD:C02528];
            taurine [CPD:C00245]
COMMENT     Some other taurine conjugates are hydrolysed, but not glycine
            conjugates of bile acids.
REFERENCE   1  [PMID:2628421]
  AUTHORS   Kawamoto K, Horibe I, Uchida K.
  TITLE     Purification and characterization of a new hydrolase for conjugated
            bile acids, chenodeoxycholyltaurine hydrolase, from Bacteroides
            vulgatus.
  JOURNAL   J. Biochem. (Tokyo). 106 (1989) 1049-53.
  ORGANISM  Bacteroides vulgatus
PATHWAY     PATH: map00120  Bile acid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.74
            ExPASy - ENZYME nomenclature database: 3.5.1.74
            ExplorEnz - The Enzyme Database: 3.5.1.74
            ERGO genome analysis and discovery system: 3.5.1.74
            BRENDA, the Enzyme Database: 3.5.1.74
            CAS: 125752-75-2
///
ENTRY       EC 3.5.1.75                 Enzyme
NAME        urethanase;
            urethane hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     urethane amidohydrolase (decarboxylating)
REACTION    urethane + H2O = ethanol + CO2 + NH3 [RN:R02359]
ALL_REAC    R02359
SUBSTRATE   urethane [CPD:C01537];
            H2O [CPD:C00001]
PRODUCT     ethanol [CPD:C00469];
            CO2 [CPD:C00011];
            NH3 [CPD:C00014]
REFERENCE   1  [PMID:2393957]
  AUTHORS   Kobashi K, Takebe S, Sakai T.
  TITLE     Urethane-hydrolyzing enzyme from Citrobacter sp.
  JOURNAL   Chem. Pharm. Bull. (Tokyo). 38 (1990) 1326-8.
  ORGANISM  Citrobacter sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.75
            ExPASy - ENZYME nomenclature database: 3.5.1.75
            ExplorEnz - The Enzyme Database: 3.5.1.75
            ERGO genome analysis and discovery system: 3.5.1.75
            BRENDA, the Enzyme Database: 3.5.1.75
            CAS: 122007-70-9
///
ENTRY       EC 3.5.1.76                 Enzyme
NAME        arylalkyl acylamidase;
            aralkyl acylamidase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-acetylarylalkylamine amidohydrolase
REACTION    N-acetylarylalkylamine + H2O = arylalkylamine + acetate [RN:R04727]
ALL_REAC    R04727
SUBSTRATE   N-acetylarylalkylamine [CPD:C02998];
            H2O [CPD:C00001]
PRODUCT     arylalkylamine [CPD:C01890];
            acetate [CPD:C00033]
COMMENT     Identified in Pseudomonas putida. Strict specificity for N-acetyl
            arylalkylamines, including N-acetyl-2-phenylethylamine,
            N-acetyl-3-phenylpropylamine, N-acetyldopamine, N-acetyl-serotonin
            and melatonin. It also accepts arylalkyl acetates but not
            acetanilide derivatives, which are common substrates of EC 3.5.1.13,
            aryl acylamidase.
REFERENCE   1  [PMID:1396711]
  AUTHORS   Shimizu S, Ogawa J, Chung MC, Yamada H.
  TITLE     Purification and characterization of a novel enzyme, arylalkyl
            acylamidase, from Pseudomonas putida Sc2.
  JOURNAL   Eur. J. Biochem. 209 (1992) 375-82.
  ORGANISM  Pseudomonas putida [GN:ppu]
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.76
            ExPASy - ENZYME nomenclature database: 3.5.1.76
            ExplorEnz - The Enzyme Database: 3.5.1.76
            ERGO genome analysis and discovery system: 3.5.1.76
            BRENDA, the Enzyme Database: 3.5.1.76
///
ENTRY       EC 3.5.1.77                 Enzyme
NAME        N-carbamoyl-D-amino acid hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
REACTION    N-carbamoyl-D-amino acid + H2O = D-amino acid + NH3 + CO2
            [RN:R02190]
ALL_REAC    R02190
SUBSTRATE   N-carbamoyl-D-amino acid [CPD:C05226];
            H2O [CPD:C00001]
PRODUCT     D-amino acid [CPD:C00405];
            NH3 [CPD:C00014];
            CO2 [CPD:C00011]
COMMENT     Has strict stereospecificity for N-carbamoyl-D-amino acids and does
            not act upon the corresponding L-amino acids or N-formyl amino
            acids, N-carbamoyl-sarcosine, -citrulline, -allantoin and
            -ureidopropionate, which are substrates for other amidohydrolases.
REFERENCE   1  [PMID:8462543]
  AUTHORS   Ogawa J, Shimizu S, Yamada H.
  TITLE     N-carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c
            purification and characterization.
  JOURNAL   Eur. J. Biochem. 212 (1993) 685-91.
  ORGANISM  Comamonas sp.
ORTHOLOGY   KO: K01459  
GENES       RFR: Rfer_0149
            HPA: HPAG1_0311
            RET: RHE_CH03761
            RLE: RL4288
            BJA: bll7207
            BRA: BRADO0581 BRADO1782 BRADO1790 BRADO3018
            BBT: BBta_2095 BBta_2106 BBta_5123 BBta_7596
            RPE: RPE_0154
            NWI: Nwi_0384
            NHA: Nham_0479
            RDE: RD1_0395
STRUCTURES  PDB: 1ERZ  1UF4  1UF5  1UF7  1UF8  2GGK  2GGL  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.77
            ExPASy - ENZYME nomenclature database: 3.5.1.77
            ExplorEnz - The Enzyme Database: 3.5.1.77
            ERGO genome analysis and discovery system: 3.5.1.77
            BRENDA, the Enzyme Database: 3.5.1.77
            CAS: 71768-08-6
///
ENTRY       EC 3.5.1.78                 Enzyme
NAME        glutathionylspermidine amidase;
            glutathionylspermidine amidohydrolase (spermidine-forming)
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     gamma-L-glutamyl-L-cysteinyl-glycine:spermidine amidase
REACTION    glutathionylspermidine + H2O = glutathione + spermidine [RN:R01918]
ALL_REAC    R01918
SUBSTRATE   glutathionylspermidine [CPD:C05730];
            H2O [CPD:C00001]
PRODUCT     glutathione [CPD:C00051];
            spermidine [CPD:C00315]
COMMENT     Spermidine is numbered so that atom N-1 is in the amino group of the
            aminopropyl part of the molecule. The enzyme from Escherichia coli
            is bifunctional and also catalyses the glutathionylspermidine
            synthase (EC 6.3.1.8) reaction, resulting in a net hydrolysis of
            ATP.
REFERENCE   1  [PMID:7775463]
  AUTHORS   Bollinger JM Jr, Kwon DS, Huisman GW, Kolter R, Walsh CT.
  TITLE     Glutathionylspermidine metabolism in Escherichia coli. Purification,
            cloning, overproduction, and characterization of a bifunctional
            glutathionylspermidine synthetase/amidase.
  JOURNAL   J. Biol. Chem. 270 (1995) 14031-41.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00480  Glutathione metabolism
ORTHOLOGY   KO: K01460  glutathionylspermidine amidase
GENES       ECO: b2988(gss)
            ECJ: JW2956(gss)
            ECE: Z4342(gsp)
            ECS: ECs3873
            ECC: c3725(gsp)
            ECI: UTI89_C3410(gsp)
            ECP: ECP_3073
            ECV: APECO1_3433(gsp)
            ECW: EcE24377A_3455(gsp)
            ECX: EcHS_A3168(gsp)
            STY: STY3310(gsp)
            STT: t3060(gsp)
            SPT: SPA3007(gsp)
            SEC: SC3080(gsp)
            STM: STM3139(gsp)
            SFL: SF3035(gsp)
            SFX: S3236(gsp)
            SFV: SFV_3041(gsp)
            SSN: SSON_3133(gsp)
            SBO: SBO_2875(gsp)
            SDY: SDY_3085(gsp)
            MSU: MS0671(gsp)
            ASU: Asuc_0804
            PHA: PSHAa2455(gssA)
            PIN: Ping_1235
            MMW: Mmwyl1_0216
            RRU: Rru_A3723
STRUCTURES  PDB: 2IO7  2IO8  2IO9  2IOA  2IOB  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.78
            ExPASy - ENZYME nomenclature database: 3.5.1.78
            ExplorEnz - The Enzyme Database: 3.5.1.78
            ERGO genome analysis and discovery system: 3.5.1.78
            BRENDA, the Enzyme Database: 3.5.1.78
            CAS: 171040-71-4
///
ENTRY       EC 3.5.1.79                 Enzyme
NAME        phthalyl amidase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     phthalyl-amide amidohydrolase
REACTION    a phthalylamide + H2O = phthalic acid + a substituted amine
            [RN:R05167]
ALL_REAC    R05167
SUBSTRATE   phthalylamide [CPD:C06374];
            H2O [CPD:C00001]
PRODUCT     phthalic acid [CPD:C01606];
            substituted amine [CPD:C06375]
COMMENT     In the entry, "phthalyl" is used to mean "2-carboxybenzoyl". The
            enzyme from Xanthobacter agilis hydrolyses phthalylated amino acids,
            peptides, beta-lactams, aromatic and aliphatic amines. The
            substituent on nitrogen may be an alkyl group, but may also be
            complex, giving an amino acid or peptide derivative. Substitutions
            on the phthalyl ring include 6-F, 6-NH2, 3-OH, and a nitrogen in the
            aromatic ring ortho to the carboxy group attached to the amine. No
            cofactors are required
REFERENCE   1
  AUTHORS   Briggs, B.S., Kreuzman, A.J., Whitesitt, C., Yeh, W.K., Zmijewski,
            M.
  TITLE     Discovery, purification, and properties of o-phthalyl amidase from
            Xanthobacter agilis.
  JOURNAL   J. Mol. Catal., B Enzym. 2 (1996) 53-69.
  ORGANISM  Xanthobacter agilis
REFERENCE   2
  AUTHORS   Black, T.D., Briggs, B.S., Evans, R., Muth, W.L., Vangala, S.,
            Zmijewski, M.J.
  TITLE     o-Phthalyl amidase in the synthesis of Loracarbef: process
            development using this novel biocatalyst.
  JOURNAL   Biotechnol. Lett. 18 (1996) 875-880.
  ORGANISM  Xanthobacter agilis
REFERENCE   3
  AUTHORS   Costello, C., Kreuzman, A., Zmijewski, M.
  TITLE     Selective deprotection of phthalyl protected proteins.
  JOURNAL   Tetrahedron Lett. 37 (1996) 7469-7472.
  ORGANISM  Xanthobacter agilis
REFERENCE   4
  AUTHORS   Briggs, B.S., Zmijewski, M.J.
  TITLE     Enzyme from microbial source: phthalyl amidase.
  JOURNAL   Chem. Abstr. 123 (1995) 25010.
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.79
            ExPASy - ENZYME nomenclature database: 3.5.1.79
            ExplorEnz - The Enzyme Database: 3.5.1.79
            ERGO genome analysis and discovery system: 3.5.1.79
            BRENDA, the Enzyme Database: 3.5.1.79
            CAS: 169150-79-2
///
ENTRY       EC 3.5.1.80       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
COMMENT     Deleted entry: identical to EC 3.5.1.25,
            N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.80 created
            1999, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.80
            ExPASy - ENZYME nomenclature database: 3.5.1.80
            ExplorEnz - The Enzyme Database: 3.5.1.80
            ERGO genome analysis and discovery system: 3.5.1.80
            BRENDA, the Enzyme Database: 3.5.1.80
///
ENTRY       EC 3.5.1.81                 Enzyme
NAME        N-acyl-D-amino-acid deacylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-acyl-D-amino acid amidohydrolase
REACTION    N-acyl-D-amino acid + H2O = an acid + D-amino acid [RN:R02192]
ALL_REAC    R02192
SUBSTRATE   N-acyl-D-amino acid [CPD:C06378];
            H2O [CPD:C00001]
PRODUCT     acid [CPD:C00174];
            D-amino acid [CPD:C00405]
COFACTOR    Zinc [CPD:C00038]
COMMENT     The enzyme from Alcaligenes denitrificans subsp. xylosoxydans and
            Alcaligenes xylosoxydans subsp. xylosoxydans has wide specificity;
            hydrolyses N-acyl derivative of neutral D-amino acids. Used in
            separating D- and L-amino acids. Requires zinc.
REFERENCE   1  [PMID:8541651]
  AUTHORS   Wakayama M, Katsuno Y, Hayashi S, Miyamoto Y, Sakai K, Moriguchi M.
  TITLE     Cloning and sequencing of a gene encoding D-aminoacylase from
            Alcaligenes xylosoxydans subsp. xylosoxydans A-6 and expression of
            the gene in Escherichia coli.
  JOURNAL   Biosci. Biotechnol. Biochem. 59 (1995) 2115-9.
  ORGANISM  Alcaligenes xylosoxydans
REFERENCE   2  [PMID:8776758]
  AUTHORS   Wakayama M, Hayashi S, Yatsuda Y, Katsuno Y, Sakai K, Moriguchi M.
  TITLE     Overproduction of D-aminoacylase from Alcaligenes xylosoxydans
            subsp. xylosoxydans A-6 in Escherichia coli and its purification.
  JOURNAL   Protein. Expr. Purif. 7 (1996) 395-9.
  ORGANISM  Alcaligenes xylosoxydans
ORTHOLOGY   KO: K06015  
GENES       SPE: Spro_0551
            CSA: Csal_0091
            REU: Reut_B4020
            REH: H16_B0531 H16_B1123
            RME: Rmet_4772 Rmet_5093
            BMA: BMA0178
            BVI: Bcep1808_2845
            BUR: Bcep18194_A6068 Bcep18194_C7586
            BCN: Bcen_2128 Bcen_3337
            BCH: Bcen2424_2740 Bcen2424_5030
            BAM: Bamb_2790 Bamb_4439
            BPS: BPSL0630(dan)
            BPM: BURPS1710b_0837
            BTE: BTH_I0546
            RFR: Rfer_0927 Rfer_0978
            POL: Bpro_0663 Bpro_4816
            VEI: Veis_3331
            DDE: Dde_1269
            BRA: BRADO6610(dan)
            BBT: BBta_0926(dan)
            JAN: Jann_3245
            SAL: Sala_1467
            GOX: GOX1177
            ABA: Acid345_2609
            SUS: Acid_0057 Acid_0754 Acid_3623
            BCZ: BCZK4241 BCZK4242
            CDF: CD2859 CD3182
            AMT: Amet_2067
            DSY: DSY1804
            DRM: Dred_0263
            MTA: Moth_1302
            MSM: MSMEG_3787
            RHA: RHA1_ro02461 RHA1_ro02463
            KRA: Krad_1032
            SEN: SACE_2583 SACE_3585 SACE_5301
            RBA: RB2098(ndaD)
STRUCTURES  PDB: 1M7J  1RJP  1RJQ  1RJR  1RK5  1RK6  1V4Y  1V51  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.81
            ExPASy - ENZYME nomenclature database: 3.5.1.81
            ExplorEnz - The Enzyme Database: 3.5.1.81
            ERGO genome analysis and discovery system: 3.5.1.81
            BRENDA, the Enzyme Database: 3.5.1.81
            CAS: 65979-42-2
///
ENTRY       EC 3.5.1.82                 Enzyme
NAME        N-acyl-D-glutamate deacylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-acyl-D-glutamate amidohydrolase
REACTION    N-acyl-D-glutamate + H2O = a carboxylate + D-glutamate [RN:R01581]
ALL_REAC    R01581
SUBSTRATE   N-acyl-D-glutamate [CPD:C06379];
            H2O [CPD:C00001]
PRODUCT     carboxylate [CPD:C00060];
            D-glutamate [CPD:C00217]
COFACTOR    Zinc [CPD:C00038]
COMMENT     The enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans and
            Pseudomonas sp. is specific for N-acyl-D-glutamate. Requires zinc.
REFERENCE   1  [PMID:8537313]
  AUTHORS   Wakayama M, Ashika T, Miyamoto Y, Yoshikawa T, Sonoda Y, Sakai K,
            Moriguchi M.
  TITLE     Primary structure of N-acyl-D-glutamate amidohydrolase from
            Alcaligenes xylosoxydans subsp. xylosoxydans A-6.
  JOURNAL   J. Biochem. (Tokyo). 118 (1995) 204-9.
  ORGANISM  Alcaligenes xylosoxydans
REFERENCE   2  [PMID:7549100]
  AUTHORS   Wakayama M, Miura Y, Oshima K, Sakai K, Moriguchi M.
  TITLE     Metal-characterization of N-acyl-D-glutamate amidohydrolase from
            Pseudomonas sp. strain 5f-1.
  JOURNAL   Biosci. Biotechnol. Biochem. 59 (1995) 1489-92.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:8829533]
  AUTHORS   Wakayama M, Tsutsumi T, Yada H, Sakai K, Moriguchi M.
  TITLE     Chemical modification of histidine residue of N-acyl-D-Glutamate
            amidohydrolase from Pseudomonas sp. 5f-1.
  JOURNAL   Biosci. Biotechnol. Biochem. 60 (1996) 650-3.
  ORGANISM  Pseudomonas sp.
ORTHOLOGY   KO: K01461  
GENES       VVU: VV2_0594
            VVY: VVA1145
            PPR: PBPRA1272
            PST: PSPTO_5117
            PSB: Psyr_0415
            PSP: PSPPH_0405
            PFL: PFL_0775
            PFO: Pfl_0723
            RSO: RSp1187(ndeD)
            BXE: Bxe_A4058
            BPE: BP1207
            BPA: BPP1821
            BBR: BB3285
            BRA: BRADO1400
            BBT: BBta_6703
            RHA: RHA1_ro01529
            NCA: Noca_1417
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.82
            ExPASy - ENZYME nomenclature database: 3.5.1.82
            ExplorEnz - The Enzyme Database: 3.5.1.82
            ERGO genome analysis and discovery system: 3.5.1.82
            BRENDA, the Enzyme Database: 3.5.1.82
///
ENTRY       EC 3.5.1.83                 Enzyme
NAME        N-acyl-D-aspartate deacylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-acyl-D-aspartate amidohydrolase
REACTION    N-acyl-D-aspartate + H2O = a carboxylate + D-aspartate [RN:R02182]
ALL_REAC    R02182
SUBSTRATE   N-acyl-D-aspartate [CPD:C06380];
            H2O [CPD:C00001]
PRODUCT     carboxylate [CPD:C00060];
            D-aspartate [CPD:C00402]
COFACTOR    Zinc [CPD:C00038]
COMMENT     The enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans is
            specific for N-acyl-D-aspartate. Requires zinc.
REFERENCE   1  [PMID:7763985]
  AUTHORS   Moriguchi M, Sakai K, Katsuno Y, Maki T, Wakayama M.
  TITLE     Purification and characterization of novel N-acyl-D-aspartate
            amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans
            A-6.
  JOURNAL   Biosci. Biotechnol. Biochem. 57 (1993) 1145-8.
  ORGANISM  Alcaligenes xylosoxydans
REFERENCE   2
  AUTHORS   Wakayama, M., Watanabe, E., Takenaka, Y., Miyamoto, Y., Tau, Y.,
            Sakai, K., Moriguchi, M.
  TITLE     Cloning, expression and nucleotide sequence of the
            N-acyl-D-aspartate amidohydrolase gene from Alcaligenes xylosoxydans
            subsp. xylosoxydans A-6.
  JOURNAL   J. Ferment. Bioeng. 80 (1995) 311-317.
  ORGANISM  Alcaligenes xylosoxydans
GENES       REH: H16_B2124
            BPL: BURPS1106A_0674
            BPD: BURPS668_0658
            BRA: BRADO6862
            BBT: BBta_0688
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.83
            ExPASy - ENZYME nomenclature database: 3.5.1.83
            ExplorEnz - The Enzyme Database: 3.5.1.83
            ERGO genome analysis and discovery system: 3.5.1.83
            BRENDA, the Enzyme Database: 3.5.1.83
            CAS: 9031-86-1
///
ENTRY       EC 3.5.1.84                 Enzyme
NAME        biuret amidohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     biuret amidohydrolase
REACTION    biuret + H2O = urea + CO2 + NH3 [RN:R05562]
ALL_REAC    R05562;
            (other) R05563
SUBSTRATE   biuret [CPD:C06555];
            H2O [CPD:C00001]
PRODUCT     urea [CPD:C00086];
            CO2 [CPD:C00011];
            NH3 [CPD:C00014]
COMMENT     Involved in a pathway by which the herbicide atrazine,
            2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, is
            degraded in bacteria.
REFERENCE   1  [PMID:3904735]
  AUTHORS   Cook AM, Beilstein P, Grossenbacher H, Hutter R.
  TITLE     Ring cleavage and degradative pathway of cyanuric acid in bacteria.
  JOURNAL   Biochem. J. 231 (1985) 25-30.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00791  Atrazine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.84
            ExPASy - ENZYME nomenclature database: 3.5.1.84
            ExplorEnz - The Enzyme Database: 3.5.1.84
            ERGO genome analysis and discovery system: 3.5.1.84
            UM-BBD (Biocatalysis/Biodegradation Database): 3.5.1.84
            BRENDA, the Enzyme Database: 3.5.1.84
///
ENTRY       EC 3.5.1.85                 Enzyme
NAME        (S)-N-acetyl-1-phenylethylamine hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     (S)-N-acetylphenylethylamine:H2O hydrolase
REACTION    N-acetylphenylethylamine + H2O = phenylethylamine + acetate
            [RN:R07301]
ALL_REAC    R07301
SUBSTRATE   N-acetylphenylethylamine [CPD:C06746];
            H2O [CPD:C00001]
PRODUCT     phenylethylamine [CPD:C05332];
            acetate [CPD:C00033]
INHIBITOR   Phenylmethanesulfonyl fluoride [CPD:C06747]
COMMENT     Inhibited by phenylmethanesulfonyl fluoride. Some related acetylated
            compounds are hydrolysed with variable enantiomeric selectivities.
REFERENCE   1
  AUTHORS   Brunella, A., Graf, M., Kittelmann, M., Lauma, K. and Ghisalba, O.
  TITLE     Production, purification, and characterization of a highly
            enantioselective (S)-N-acetyl-1-phenylethyl amidohydrolase from
            Rhodococcus.
  JOURNAL   Appl. Microbiol. Biotechnol. 47 (1997) 515-520.
  ORGANISM  Rhodococcus equi
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.85
            ExPASy - ENZYME nomenclature database: 3.5.1.85
            ExplorEnz - The Enzyme Database: 3.5.1.85
            ERGO genome analysis and discovery system: 3.5.1.85
            BRENDA, the Enzyme Database: 3.5.1.85
            CAS: 192230-94-7
///
ENTRY       EC 3.5.1.86                 Enzyme
NAME        mandelamide amidase;
            Pseudomonas mandelamide hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     mandelamide hydrolase
REACTION    (R)-mandelamide + H2O = (R)-mandelate + NH3 [RN:R05783]
ALL_REAC    R05783
SUBSTRATE   (R)-mandelamide [CPD:C07301];
            H2O [CPD:C00001]
PRODUCT     (R)-mandelate [CPD:C01983];
            NH3 [CPD:C00014]
REFERENCE   1  [PMID:1660699]
  AUTHORS   Yamamoto K, Oishi K, Fujimatsu I, Komatsu K.
  TITLE     Production of R-(-)-mandelic acid from mandelonitrile by Alcaligenes
            faecalis ATCC 8750.
  JOURNAL   Appl. Environ. Microbiol. 57 (1991) 3028-32.
  ORGANISM  Alcaligenes faecalis
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.86
            ExPASy - ENZYME nomenclature database: 3.5.1.86
            ExplorEnz - The Enzyme Database: 3.5.1.86
            ERGO genome analysis and discovery system: 3.5.1.86
            BRENDA, the Enzyme Database: 3.5.1.86
///
ENTRY       EC 3.5.1.87                 Enzyme
NAME        N-carbamoyl-L-amino-acid hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-carbamoyl-L-amino acid amidohydrolase
REACTION    N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H2O =
            L-2-amino acid + NH3 + CO2 [RN:R05782]
ALL_REAC    R05782
SUBSTRATE   N-carbamoyl-L-2-amino acid [CPD:C11529];
            H2O [CPD:C00001]
PRODUCT     L-2-amino acid [CPD:C00151];
            NH3 [CPD:C00014];
            CO2 [CPD:C00011]
COMMENT     The enzyme has broad specificity for carbamoyl-L-amino acids,
            although it is inactive on the carbamoyl derivatives of glutamate,
            aspartate, arginine, tyrosine or tryptophan. Carbamoyl-L-valine is
            the best substrate. It is inactive on derivatives of D-amino acids,
            the substrates of EC 3.5.1.77 (N-carbamoyl-D-amino acid hydrolase),
            or on N-carbamoyl-beta-alanine, the substrate of EC 3.5.1.6
            (beta-ureidopropionase). The enzyme hydrolyses formyl derivatives
            rapidly, and acetyl derivatives very slowly. Mn2+, Ni2+ or Co2+
            enabled reactivation of enzyme that had been treated with a
            chelating agent.
REFERENCE   1  [PMID:8590654]
  AUTHORS   Ogawa J, Miyake H, Shimizu S.
  TITLE     Purification and characterization of N-carbamoyl-L-amino acid
            amidohydrolase with broad substrate specificity from Alcaligenes
            xylosoxidans.
  JOURNAL   Appl. Microbiol. Biotechnol. 43 (1995) 1039-43.
  ORGANISM  Alcaligenes xylosoxidans
ORTHOLOGY   KO: K06016  
GENES       YPA: YPA_2740
            YPN: YPN_0844
            YPP: YPDSF_2885
            ECA: ECA3490(amaB)
            SPE: Spro_0937 Spro_2555
            ASU: Asuc_1061
            XCC: XCC0284(amaB)
            XCB: XC_0294
            XCV: XCV0309
            XAC: XAC0301(amaB)
            PPF: Pput_0654 Pput_1804
            PFL: PFL_2550 PFL_3679 PFL_4137
            PAT: Patl_2051
            PIN: Ping_2423
            NOC: Noc_0781
            CSA: Csal_0031 Csal_1186
            MMW: Mmwyl1_0455 Mmwyl1_3207
            REU: Reut_A1370 Reut_A3278 Reut_B4534
            RME: Rmet_3443 Rmet_4480
            BVI: Bcep1808_1209 Bcep1808_5509 Bcep1808_6582 Bcep1808_6695
            BUR: Bcep18194_A4391 Bcep18194_B1948 Bcep18194_B2909
                 Bcep18194_B3012 Bcep18194_C6654
            BCN: Bcen_0772 Bcen_1597 Bcen_4269 Bcen_4821 Bcen_5723
            BCH: Bcen2424_1253 Bcen2424_3345 Bcen2424_4097 Bcen2424_6087
                 Bcen2424_6234
            BAM: Bamb_1132 Bamb_3508 Bamb_5903 Bamb_5967
            BPM: BURPS1710b_2180
            BPL: BURPS1106A_2039(amaB)
            BPA: BPP2133
            BBR: BB1530
            RFR: Rfer_0158 Rfer_0165
            POL: Bpro_0419 Bpro_1423 Bpro_1498 Bpro_3330
            PNA: Pnap_0354 Pnap_4022 Pnap_4068
            AAV: Aave_0970 Aave_1110 Aave_4755
            AJS: Ajs_1115
            VEI: Veis_1247 Veis_4148 Veis_4389
            CCV: CCV52592_2070
            CCO: CCC13826_0648
            SMD: Smed_2366
            RLE: RL0367(amaB) pRL120159
            OAN: Oant_0348
            BJA: bll6147
            BRA: BRADO1013 BRADO2536
            BBT: BBta_2595 BBta_2881 BBta_6028 BBta_7037
            RPB: RPB_3623
            RPC: RPC_1668
            RPD: RPD_1844
            XAU: Xaut_3289 Xaut_3376
            CCR: CC_2603
            SIT: TM1040_1498 TM1040_2689
            RSP: RSP_3446
            RSH: Rsph17029_0104 Rsph17029_1817 Rsph17029_3091
            RSQ: Rsph17025_1461 Rsph17025_2051
            JAN: Jann_2707
            RDE: RD1_3101
            PDE: Pden_1113 Pden_3434 Pden_3515 Pden_4267
            GOX: GOX1297
            GBE: GbCGDNIH1_0310
            ACR: Acry_1161 Acry_3022 Acry_3535
            SUS: Acid_0361 Acid_0364 Acid_4051
            BCL: ABC3328 ABC3483
            GKA: GK3252
            LMO: lmo0537
            CDF: CD2027
            CBO: CBO0629
            CBE: Cbei_1944
            CKL: CKL_2403(amaB)
            DSY: DSY4162 DSY4355
            MSM: MSMEG_1180
            RHA: RHA1_ro02816
            PAC: PPA2167
            NCA: Noca_4387
            TFU: Tfu_2012
            KRA: Krad_2079 Krad_4127
            SEN: SACE_6405
            STP: Strop_1109
            RXY: Rxyl_0221 Rxyl_0582 Rxyl_1854 Rxyl_2745
            RBA: RB13304(amaB)
            SYW: SYNW2452
            SYD: Syncc9605_2632
            SYE: Syncc9902_2259
            SYR: SynRCC307_1123
            DGE: Dgeo_2610
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.87
            ExPASy - ENZYME nomenclature database: 3.5.1.87
            ExplorEnz - The Enzyme Database: 3.5.1.87
            ERGO genome analysis and discovery system: 3.5.1.87
            BRENDA, the Enzyme Database: 3.5.1.87
///
ENTRY       EC 3.5.1.88                 Enzyme
NAME        peptide deformylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     formyl-L-methionyl peptide amidohydrolase
REACTION    formyl-L-methionyl peptide + H2O = formate + methionyl peptide
            [RN:R05635]
ALL_REAC    R05635
SUBSTRATE   formyl-L-methionyl peptide [CPD:C11439];
            H2O [CPD:C00001]
PRODUCT     formate [CPD:C00058];
            methionyl peptide [CPD:C11440]
COMMENT     Requires Fe(II). Also requires at least a dipeptide for an efficient
            rate of reaction. N-terminal L-methionine is a prerequisite for
            activity but the enzyme has broad specificity at other positions.
            Differs in substrate specifity from EC 3.5.1.27
            (N-formylmethionylaminoacyl-tRNA deformylase) and EC 3.5.1.31
            (formylmethionine deformylase).
REFERENCE   1  [PMID:4973445]
  AUTHORS   Adams JM.
  TITLE     On the release of the formyl group from nascent protein.
  JOURNAL   J. Mol. Biol. 33 (1968) 571-89.
  ORGANISM  Escherichia coli [GN:eco], Bacillus steurothermophilus
REFERENCE   2  [PMID:8112305]
  AUTHORS   Mazel D, Pochet S, Marliere P.
  TITLE     Genetic characterization of polypeptide deformylase, a distinctive
            enzyme of eubacterial translation.
  JOURNAL   EMBO. J. 13 (1994) 914-23.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:9374869]
  AUTHORS   Chan MK, Gong W, Rajagopalan PT, Hao B, Tsai CM, Pei D.
  TITLE     Crystal structure of the Escherichia coli peptide deformylase.
  JOURNAL   Biochemistry. 36 (1997) 13904-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:9565550]
  AUTHORS   Becker A, Schlichting I, Kabsch W, Schultz S, Wagner AF.
  TITLE     Structure of peptide deformylase and identification of the substrate
            binding site.
  JOURNAL   J. Biol. Chem. 273 (1998) 11413-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:9846875]
  AUTHORS   Becker A, Schlichting I, Kabsch W, Groche D, Schultz S, Wagner AF.
  TITLE     Iron center, substrate recognition and mechanism of peptide
            deformylase.
  JOURNAL   Nat. Struct. Biol. 5 (1998) 1053-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6
  AUTHORS   Rajagopalan, P.T.R., Yu, X.C. and Pei, D.
  TITLE     Peptide deformylase: a new type of mononuclear iron protein.
  JOURNAL   J. Am. Chem. Soc. 119 (1997) 12418-12419.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   7  [PMID:9610360]
  AUTHORS   Groche D, Becker A, Schlichting I, Kabsch W, Schultz S, Wagner AF.
  TITLE     Isolation and crystallization of functionally competent Escherichia
            coli peptide deformylase forms containing either iron or nickel in
            the active site.
  JOURNAL   Biochem. Biophys. Res. Commun. 246 (1998) 342-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   8  [PMID:10651644]
  AUTHORS   Rajagopalan PT, Grimme S, Pei D.
  TITLE     Characterization of cobalt(II)-substituted peptide deformylase:
            function of the metal ion and the catalytic residue Glu-133.
  JOURNAL   Biochemistry. 39 (2000) 779-90.
  ORGANISM  Escherichia coli [GN:eco], Thermus thermophilus
REFERENCE   9  [PMID:9888804]
  AUTHORS   Hu YJ, Wei Y, Zhou Y, Rajagopalan PT, Pei D.
  TITLE     Determination of substrate specificity for peptide deformylase
            through the screening of a combinatorial peptide library.
  JOURNAL   Biochemistry. 38 (1999) 643-50.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   10 [PMID:10373378]
  AUTHORS   Ragusa S, Mouchet P, Lazennec C, Dive V, Meinnel T.
  TITLE     Substrate recognition and selectivity of peptide deformylase.
            Similarities and differences with metzincins and thermolysin.
  JOURNAL   J. Mol. Biol. 289 (1999) 1445-57.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   11 [PMID:10931273]
  AUTHORS   Giglione C, Pierre M, Meinnel T.
  TITLE     Peptide deformylase as a target for new generation, broad spectrum
            antimicrobial agents.
  JOURNAL   Mol. Microbiol. 36 (2000) 1197-205.
  ORGANISM  Escherichia coli [GN:eco], Bacillus subtilis [GN:bsu]
REFERENCE   12
  AUTHORS   Pei, D.
  TITLE     Peptide deformylase: a target for novel antibiotics?.
  JOURNAL   Emerging Therapeutic Targets 5 (2001) 23-40.
ORTHOLOGY   KO: K01462  
GENES       HSA: 64146(PDF)
            CFA: 610955(PDF)
            XTR: 448425(TNeu035k20.1)
            SPU: 586099(LOC586099)
            ATH: AT1G15390(PDF1A)
            OSA: 4324565 4326576
            TET: TTHERM_00460620 TTHERM_01146060
            TBR: Tb11.01.6120
            TCR: 506871.100 507509.50 510579.20
            LMA: LmjF32.1300
            ECO: b3287(def)
            ECJ: JW3248(def)
            ECE: Z4657(def)
            ECS: ECs4152
            ECC: c4047(def)
            ECI: UTI89_C3731(def)
            ECP: ECP_3374
            ECV: APECO1_3160(def)
            ECW: EcE24377A_3769(def1) EcE24377A_F0040(def2)
            ECX: EcHS_A3480
            STY: STY4391(fms)
            STT: t4098(fms)
            SPT: SPA3273(fms)
            SEC: SC3342(def)
            STM: STM3406(def)
            YPE: YPO0242(def)
            YPK: y4023(def)
            YPM: YP_0240(def)
            YPA: YPA_3231
            YPN: YPN_3827
            YPP: YPDSF_0164
            YPI: YpsIP31758_3882(def)
            SFL: SF3318(def)
            SFX: S3543(def)
            SFV: SFV_3306(def)
            SSN: SSON_3427(def)
            SBO: SBO_3280(def)
            SDY: SDY_3463(def)
            ECA: ECA3999(def)
            PLU: plu4695(def)
            BUC: BU496(def)
            BAS: BUsg477(def)
            BAB: bbp439(def)
            BCC: BCc_313(def)
            WBR: WGLp496(def)
            SGL: SG2246
            ENT: Ent638_3718
            SPE: Spro_4511
            BFL: Bfl219(def)
            BPN: BPEN_226(def)
            HIN: HI0622(def)
            HIT: NTHI0725(def)
            HIP: CGSHiEE_09150(def)
            HDU: HD1889(def)
            HSO: HS_0041(def)
            PMU: PM1559(def)
            MSU: MS2201(def)
            APL: APL_1711(def)
            ASU: Asuc_0112
            XFA: XF0926
            XFT: PD1763(def)
            XCC: XCC0687(def) XCC3749(def)
            XCB: XC_3547 XC_3819
            XCV: XCV3636(def) XCV3926(def)
            XAC: XAC3510(def) XAC3801(def)
            XOO: XOO0585(def) XOO1075(def)
            XOM: XOO_0546(XOO0546) XOO_0975(XOO0975)
            VCH: VC0046 VCA0150
            VVU: VV1_1048 VV2_0863
            VVY: VV3225 VVA1334
            VPA: VP3042 VPA0784
            VFI: VF2543(def)
            PPR: PBPRA2061 PBPRA3579
            PAE: PA0019(def) PA1122
            PAU: PA14_00200(def) PA14_49870
            PAP: PSPA7_0020(def2) PSPA7_4247(def1)
            PPU: PP_0068(def-1) PP_4559(def-2)
            PPF: Pput_0084 Pput_1330
            PST: PSPTO_0177(def-1) PSPTO_1598(def-2)
            PSB: Psyr_0019(def) Psyr_3780(def)
            PSP: PSPPH_0021(def1) PSPPH_1473(def2)
            PFL: PFL_0022(def) PFL_4594(def)
            PFO: Pfl_0017 Pfl_4349
            PEN: PSEEN0025(def-1) PSEEN4003(def2)
            PMY: Pmen_0055
            PAR: Psyc_0030(def)
            PCR: Pcryo_0038
            PRW: PsycPRwf_0042
            ACI: ACIAD0211(def) ACIAD1039(def2)
            SON: SO_0032(def-1) SO_1062(def-2) SO_2530(def-3)
            SDN: Sden_0024 Sden_0898 Sden_2912
            SFR: Sfri_0024 Sfri_3241
            SAZ: Sama_0043 Sama_0639
            SBL: Sbal_0032 Sbal_0886 Sbal_2302
            SBM: Shew185_0027 Shew185_2023 Shew185_3476
            SLO: Shew_2103 Shew_3736
            SPC: Sputcn32_0024 Sputcn32_1795 Sputcn32_3013
            SSE: Ssed_0035 Ssed_2006
            SPL: Spea_0031 Spea_2387
            SHE: Shewmr4_0029 Shewmr4_2142 Shewmr4_3037
            SHM: Shewmr7_0027 Shewmr7_0937 Shewmr7_2219
            SHN: Shewana3_0035 Shewana3_0900 Shewana3_2319
            SHW: Sputw3181_0024 Sputw3181_0936 Sputw3181_2230
            ILO: IL0018(def)
            CPS: CPS_0020(def1) CPS_0407(def)
            PHA: PSHAa0023(def)
            PAT: Patl_0023 Patl_3433
            SDE: Sde_0021
            PIN: Ping_0078 Ping_3323
            MAQ: Maqu_0043
            CBU: CBU_0993(def) CBU_1879
            CBD: COXBU7E912_0110(def2) COXBU7E912_1053(def1)
            LPN: lpg0615 lpg1064 lpg2595(def)
            LPF: lpl1061 lpl2518(def)
            LPP: lpp0666 lpp1083 lpp2648(def)
            MCA: MCA1371(def) MCA2843(def-2)
            FTU: FTT0403(def1) FTT1675(def2)
            FTF: FTF0403(def1) FTF1675(def2)
            FTW: FTW_1671(def1) FTW_1942(def2)
            FTL: FTL_0074 FTL_0473
            FTH: FTH_0070(def) FTH_0470(def1)
            FTA: FTA_0082(def1) FTA_0499(def2)
            FTN: FTN_0110 FTN_0500
            TCX: Tcr_0193
            NOC: Noc_3014
            AEH: Mlg_2628
            HHA: Hhal_1409 Hhal_2323
            HCH: HCH_00030(def)
            CSA: Csal_2867
            ABO: ABO_0131(def-1)
            MMW: Mmwyl1_0017
            AHA: AHA_0258(def-1) AHA_2373(def-2)
            DNO: DNO_0156(def)
            BCI: BCI_0416(def)
            RMA: Rmag_0967
            VOK: COSY_0868(def)
            NME: NMB0110
            NMA: NMA0164(def)
            RSO: RSc0070(def) RSc1399(RS05293)
            REU: Reut_A1885(def) Reut_A3408(def)
            RME: Rmet_1429 Rmet_3565
            BMA: BMA0142(def-1) BMA1559(def-2)
            BMV: BMASAVP1_A2061(def-2) BMASAVP1_A2806(def-1)
            BML: BMA10299_A2274(def-1) BMA10299_A3250(def-2)
            BMN: BMA10247_1333(def-2) BMA10247_2352(def-1)
            BXE: Bxe_A1677 Bxe_A4416
            BVI: Bcep1808_1930 Bcep1808_3286
            BUR: Bcep18194_A5333(def) Bcep18194_A6478(def)
            BCN: Bcen_2513 Bcen_6054
            BCH: Bcen2424_2023 Bcen2424_3127
            BAM: Bamb_2056 Bamb_3182
            BPS: BPSL0121(def) BPSL2163
            BPM: BURPS1710b_0346(def) BURPS1710b_2587(def)
            BPL: BURPS1106A_0159(def) BURPS1106A_2498(def-2)
            BPD: BURPS668_0150(def) BURPS668_2441(def-2)
            BTE: BTH_I0128(def-1) BTH_I2023(def-2)
            PNU: Pnuc_1477 Pnuc_2079
            BPE: BP0039 BP0552(def)
            BPA: BPP0243(def) BPP3660
            BBR: BB0247(def) BB4095
            RFR: Rfer_2202 Rfer_3860
            POL: Bpro_2590 Bpro_4639
            PNA: Pnap_1818 Pnap_3878
            AAV: Aave_3102 Aave_4688
            AJS: Ajs_2295 Ajs_4051
            VEI: Veis_3612 Veis_4082
            MPT: Mpe_A0283 Mpe_A1813
            HAR: HEAR0118(defA) HEAR1330 HEAR1628(defB)
            NET: Neut_0392 Neut_0944
            NMU: Nmul_A0394 Nmul_A0651
            EBA: ebA62(def2) ebB91(def1)
            AZO: azo0099(def1) azo3610(def2)
            DAR: Daro_0021 Daro_2132
            TBD: Tbd_0014 Tbd_0780(def)
            MFA: Mfla_0187 Mfla_1466
            HPY: HP0793(def)
            HPJ: jhp0729(def)
            HPA: HPAG1_0778
            HAC: Hac_0915(def)
            TDN: Tmden_2034
            CJE: Cj0191c(def)
            CJR: CJE0184(def)
            CJJ: CJJ81176_0222(def)
            CJU: C8J_0180(def)
            CJD: JJD26997_0201(def)
            CFF: CFF8240_1690(def)
            CCV: CCV52592_1339 CCV52592_1501(def)
            CHA: CHAB381_0018(def)
            CCO: CCC13826_1783(def)
            ABU: Abu_1700(def)
            NIS: NIS_0166(def)
            SUN: SUN_0013
            GME: Gmet_3338
            GUR: Gura_0818 Gura_4385
            PCA: Pcar_0245
            PPD: Ppro_0514 Ppro_3513
            DVL: Dvul_0029
            BBA: Bd2759(def)
            ADE: Adeh_0725
            AFW: Anae109_0768
            MXA: MXAN_1430(def) MXAN_3395(def) MXAN_7347(def)
            SAT: SYN_01803
            SFU: Sfum_0147
            RPR: RP208(def)
            RTY: RT0197(def)
            RCO: RC0080(def3) RC0278(def) RC0674(def2)
            RFE: RF_0124(def3) RF_0324(def) RF_0730(def2)
            RBE: RBE_0560(def1) RBE_0681(def2)
            RAK: A1C_01545(def)
            RBO: A1I_03205(def)
            RCM: A1E_01200(def)
            RRI: A1G_01590(def)
            OTS: OTBS_1849(def)
            WBM: Wbm0114
            AMA: AM275
            APH: APH_1012 APH_1372(def)
            ERU: Erum0540(def1) Erum1820(def2)
            ERW: ERWE_CDS_00450(def) ERWE_CDS_01810(def)
            ERG: ERGA_CDS_00440(def) ERGA_CDS_01760(def)
            ECN: Ecaj_0043 Ecaj_0179
            ECH: ECH_0073(def) ECH_0939
            NSE: NSE_0392(def)
            PUB: SAR11_0456(def)
            MLO: mll4855
            MES: Meso_0394
            PLA: Plav_0261 Plav_2068
            SME: SMc01101(def1) SMc01262(def2)
            SMD: Smed_0054
            ATU: Atu0366(def) Atu1550(def)
            ATC: AGR_C_2856 AGR_C_640
            RET: RHE_CH00412(def1) RHE_CH02219(def2)
            RLE: RL0430(def) RL2552(def)
            BME: BMEII0264 BMEII0812
            BMF: BAB2_0782(def-1) BAB2_0997(def-2)
            BMS: BRA0454(def-1) BRA1035(def-2)
            BMB: BruAb2_0768(def) BruAb2_0975(def)
            BOV: BOV_A0976(def)
            OAN: Oant_1344 Oant_3105
            BJA: bll4005(def) bll8109(def)
            RPA: RPA0621(def)
            RPB: RPB_0673
            RPC: RPC_0803
            RPD: RPD_0081
            RPE: RPE_0656
            NWI: Nwi_3064
            NHA: Nham_3693
            BHE: BH00760(def)
            BQU: BQ00690(def)
            BBK: BARBAKC583_1319(def)
            XAU: Xaut_0628 Xaut_3305
            CCR: CC_0272
            SIL: SPO3217(def-1) SPO3218(def-2) SPO3219(def-3)
            SIT: TM1040_2578 TM1040_2579 TM1040_2580
            RSP: RSP_0872(def1) RSP_0873 RSP_0874
            RSH: Rsph17029_2532 Rsph17029_2533
            RSQ: Rsph17025_0148 Rsph17025_0149
            JAN: Jann_0466
            RDE: RD1_1337(def) RD1_1338(def)
            PDE: Pden_0646 Pden_0647
            MMR: Mmar10_0442
            HNE: HNE_0512(def)
            ZMO: ZMO0813(defA)
            NAR: Saro_2896
            SAL: Sala_0251
            SWI: Swit_4045
            ELI: ELI_02080
            GBE: GbCGDNIH1_0482 GbCGDNIH1_0693
            ACR: Acry_0374 Acry_0409
            RRU: Rru_A1044 Rru_A3350
            MGM: Mmc1_0142 Mmc1_3495
            ABA: Acid345_3916 Acid345_4287
            SUS: Acid_2746
            BSU: BG11815(ykrB)
            BHA: BH2658
            BAN: BA4005(deF-2) BA4187(deF-1)
            BAR: GBAA4005(deF-2) GBAA4187(deF-1)
            BAA: BA_4476 BA_4651
            BAT: BAS3718 BAS3884
            BCE: BC3865 BC3974
            BCY: Bcer98_2519 Bcer98_2676
            BLI: BL01629(defB)
            BLD: BLi01671(ykrB)
            BCL: ABC2423(def)
            BPU: BPUM_1352
            OIH: OB1410
            GKA: GK1057(def)
            SAU: SA0942(pdf1) SA1058
            SAV: SAV1091(pdf1) SAV1215
            SAM: MW0974(pdf1) MW1098
            SAR: SAR1065(def)
            SAS: SAS1026(def)
            SAC: SACOL1100(def)
            SAB: SAB0957c SAB1079(def)
            SAA: SAUSA300_0991(def) SAUSA300_1108(def)
            SAO: SAOUHSC_01038
            SAJ: SaurJH9_1151
            SAH: SaurJH1_1173
            SEP: SE0789 SE0890
            SER: SERP0678(def)
            SHA: SH1700 SH1861(pdf1)
            SSP: SSP1557 SSP1698
            LMO: lmo1051
            LIN: lin1043
            LWE: lwe1027
            LLA: L154885(def)
            LLC: LACR_0581
            SPY: SPy_0870(fms) SPy_1958(def)
            SPZ: M5005_Spy_0677(fms) M5005_Spy_1669(def)
            SPM: spyM18_0932(def) spyM18_2025(def)
            SPG: SpyM3_0590(fms) SpyM3_1684(def)
            SPS: SPs1263 SPs1686
            SPH: MGAS10270_Spy0735(fms) MGAS10270_Spy1737(def)
            SPI: MGAS10750_Spy0769(fms) MGAS10750_Spy1763(def)
            SPJ: MGAS2096_Spy0748(fms) MGAS2096_Spy1692(def)
            SPK: MGAS9429_Spy0732(fms) MGAS9429_Spy1670(def)
            SPF: SpyM51131(fms) SpyM51641(def)
            SPA: M6_Spy0694 M6_Spy1677(def)
            SPB: M28_Spy0657(fms) M28_Spy1657(def)
            SPN: SP_1456 SP_1549
            SPR: spr1310(fms) spr1408(def)
            SPD: SPD_1285(def)
            SAG: SAG1334 SAG1895(def)
            SAN: gbs1404 gbs1883
            SAK: SAK_1365(def) SAK_1863(def)
            SMU: SMU.143c
            STC: str0151(defB) str0431(defA)
            STL: stu0151(defB) stu0431(defA)
            SSA: SSA_0458 SSA_2061(def)
            LPL: lp_2155(def1)
            LJO: LJ0993
            LAC: LBA0830(def)
            LSA: LSA1087(def1) LSA1499(def2)
            LSL: LSL_0363(def) LSL_0649(def)
            LDB: Ldb0762(def)
            LBU: LBUL_0695
            LBR: LVIS_1411
            LCA: LSEI_1303
            LRE: Lreu_0630
            EFA: EF3066(def-1)
            OOE: OEOE_0806
            CAC: CAC1722(def) CAC2474(def)
            CPE: CPE0760(def) CPE1633(def) CPE1744(def)
            CPF: CPF_0754(def) CPF_1885(def) CPF_1997(def)
            CPR: CPR_1604(def) CPR_1715(def)
            CTC: CTC01219
            CNO: NT01CX_1650 NT01CX_2245
            CTH: Cthe_0567
            CDF: CD1756(def1) CD2585(def2)
            CBO: CBO0876(def) CBO2510 CBO2622(def)
            CBA: CLB_2234(def-1) CLB_2383(def-2) CLB_2564(def-3)
            CBH: CLC_2217(def-1) CLC_2365(def-2) CLC_2495(def-3)
            CBF: CLI_2343(def-1) CLI_2571(def-2) CLI_2686(def-3)
            CBE: Cbei_1145 Cbei_3482
            CKL: CKL_0359(def1) CKL_2653(def2) CKL_2745(def3)
            AMT: Amet_2786
            CHY: CHY_1484(def)
            DSY: DSY2694
            DRM: Dred_1591 Dred_1704
            SWO: Swol_1232
            CSC: Csac_2082
            TTE: TTE1507(def)
            MTA: Moth_0897
            MGE: MG_106(def)
            MPN: MPN245(def)
            MPU: MYPU_6890(def)
            MPE: MYPE5650(def)
            MGA: MGA_0463(def)
            MMY: MSC_0220(pdf)
            MMO: MMOB6170(def)
            MSY: MS53_0019(def)
            UUR: UU465(def)
            MFL: Mfl569
            MTU: Rv0429c(def)
            MTC: MT0444(def)
            MBO: Mb0437c(def)
            MLE: ML1929(def)
            MPA: MAP3918c(def)
            MAV: MAV_4725(def)
            MSM: MSMEG_0832(def)
            MVA: Mvan_0732
            MGI: Mflv_0175
            MMC: Mmcs_0569
            MKM: Mkms_0581
            MJL: Mjls_0559
            CGL: NCgl1539(def) NCgl2643(def)
            CGB: cg1804(def2) cg3034(def1)
            CEF: CE1720 CE2577
            CDI: DIP1323 DIP2045(def)
            CJK: jk0261(defA) jk1014(defB)
            NFA: nfa26520 nfa36090(def) nfa53010
            RHA: RHA1_ro02176 RHA1_ro02619
            SCO: SCO0883(SCM1.16) SCO1211(2SCG58.11c) SCO4560(SCD16A.23)
                 SCO5221(SC7E4.18)
            SMA: SAV3033(def1) SAV7126(def2) SAV7349(def3)
            TWH: TWT310(def)
            TWS: TW462(def)
            LXX: Lxx08610(def) Lxx15450
            CMI: CMM_1595(defA) CMM_1878(defB)
            ART: Arth_1670 Arth_2193 Arth_2436
            AAU: AAur_1821(def) AAur_2194(def) AAur_2407(def)
            PAC: PPA1525
            NCA: Noca_2441 Noca_2602
            TFU: Tfu_1726 Tfu_2433
            FRA: Francci3_0014 Francci3_2660
            FAL: FRAAL0019(def) FRAAL2799(def)
            ACE: Acel_1279
            KRA: Krad_0402 Krad_2985
            SEN: SACE_0514(def) SACE_2112(def) SACE_5920(def)
            STP: Strop_1868 Strop_2357
            BLO: BL1186 BL1502(def) BL1700(fms)
            BAD: BAD_0780(def2) BAD_1293(def1)
            RXY: Rxyl_1468
            FNU: FN1157
            RBA: RB12856(def)
            CTR: CT353(def)
            CTA: CTA_0382(def)
            CMU: TC0632
            CPN: CPn1067(def)
            CPA: CP0783
            CPJ: CPj1067(def)
            CPT: CpB1111
            CCA: CCA00311(def)
            CAB: CAB307(def)
            CFE: CF0692(def)
            PCU: pc0541(def) pc0803(def)
            BBU: BB0065(def)
            BGA: BG0064(def)
            TPA: TP0757
            LIL: LA2438
            LIC: LIC11511(def)
            LBJ: LBJ_1823(def)
            LBL: LBL_1460(def)
            SYN: slr1549(def)
            SYC: syc0213_d
            SYF: Synpcc7942_1340
            SYD: Syncc9605_2274(def)
            SYE: Syncc9902_0409(def)
            SYG: sync_2473(def)
            SYR: SynRCC307_0355(def)
            SYX: SynWH7803_2141(def) SynWH7803_2339(def)
            CYA: CYA_0120(def-1) CYA_0278(def-2)
            CYB: CYB_2132(def-1) CYB_2769(def-2)
            TEL: tlr1676
            GVI: gll2228 glr1729
            ANA: all2007 alr3079
            AVA: Ava_0830(def) Ava_5067
            PMN: PMN2A_1431(def)
            PMI: PMT9312_0070
            PMB: A9601_00801(def)
            PMC: P9515_00771(def)
            PMF: P9303_03091(def) P9303_19041(def)
            PMG: P9301_00791(def)
            PMH: P9215_00801
            PME: NATL1_01321(def)
            TER: Tery_0808 Tery_5060
            BTH: BT_0420
            BFR: BF1684
            BFS: BF1691(def)
            PGI: PG2201(def)
            SRU: SRU_1291(def)
            CHU: CHU_0693(def)
            GFO: GFO_2273(def)
            FJO: Fjoh_2532
            FPS: FP1753(def)
            CTE: CT1454(def)
            CCH: Cag_0488
            CPH: Cpha266_1861
            PVI: Cvib_1289
            PLT: Plut_1473
            DET: DET0760(def)
            DEB: DehaBAV1_0687
            RRS: RoseRS_1052
            RCA: Rcas_3475
            DRA: DR_2434
            DGE: Dgeo_2292
            AAE: aq_579(def)
            TMA: TM1661
            TPT: Tpet_1130
            TME: Tmel_0837
            FNO: Fnod_0954
STRUCTURES  PDB: 1IX1  1LM4  1LM6  1LME  1LQW  1LQY  1LRU  1LRY  1N5N  1Q1Y  
                 1S17  1SV2  1SZZ  1V3Y  1VEV  1VEY  1VEZ  1WS0  1WS1  1XEM  
                 1XEN  1XEO  1Y6H  1ZXZ  1ZY0  1ZY1  2AI7  2AI8  2AI9  2AIA  
                 2AIE  2EW5  2EW6  2EW7  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.88
            ExPASy - ENZYME nomenclature database: 3.5.1.88
            ExplorEnz - The Enzyme Database: 3.5.1.88
            ERGO genome analysis and discovery system: 3.5.1.88
            BRENDA, the Enzyme Database: 3.5.1.88
///
ENTRY       EC 3.5.1.89                 Enzyme
NAME        N-acetylglucosaminylphosphatidylinositol deacetylase;
            N-acetyl-D-glucosaminylphosphatidylinositol acetylhydrolase;
            N-acetylglucosaminylphosphatidylinositol de-N-acetylase;
            GlcNAc-PI de-N-acetylase;
            GlcNAc-PI deacetylase;
            acetylglucosaminylphosphatidylinositol deacetylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
            acetylhydrolase
REACTION    6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol +
            H2O = 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol +
            acetate [RN:R03482 R05917]
ALL_REAC    R03482 R05917(G)
SUBSTRATE   6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol;
            H2O [CPD:C00001]
PRODUCT     6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
            [CPD:C04248];
            acetate [CPD:C00033]
COMMENT     Involved in the second step of glycosylphosphatidylinositol (GPI)
            anchor formation in all eukaryotes. The enzyme appears to be
            composed of a single subunit (PIG-L in mammalian cells and GPI12 in
            yeast). In some species, the long-chain sn-1-acyl group of the
            phosphatidyl group is replaced by a long-chain alkyl or alk-1-enyl
            group.
REFERENCE   1  [PMID:2525555]
  AUTHORS   Doering TL, Masterson WJ, Englund PT, Hart GW.
  TITLE     Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of
            the trypanosome variant surface glycoprotein. Origin of the
            non-acetylated glucosamine.
  JOURNAL   J. Biol. Chem. 264 (1989) 11168-73.
  ORGANISM  Trypanosoma brucei [GN:tbr]
REFERENCE   2  [PMID:9188481]
  AUTHORS   Nakamura N, Inoue N, Watanabe R, Takahashi M, Takeda J, Stevens VL,
            Kinoshita T.
  TITLE     Expression cloning of PIG-L, a candidate
            N-acetylglucosaminyl-phosphatidylinositol deacetylase.
  JOURNAL   J. Biol. Chem. 272 (1997) 15834-40.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], rat [GN:rno]
REFERENCE   3  [PMID:10085243]
  AUTHORS   Watanabe R, Ohishi K, Maeda Y, Nakamura N, Kinoshita T.
  TITLE     Mammalian PIG-L and its yeast homologue Gpi12p are
            N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential
            in glycosylphosphatidylinositol biosynthesis.
  JOURNAL   Biochem. J. 339 ( Pt 1) (1999) 185-92.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], rat [GN:rno]
REFERENCE   4  [PMID:11432820]
  AUTHORS   Smith TK, Crossman A, Borissow CN, Paterson MJ, Dix A, Brimacombe
            JS, Ferguson MA.
  TITLE     Specificity of GlcNAc-PI de-N-acetylase of GPI biosynthesis and
            synthesis of parasite-specific suicide substrate inhibitors.
  JOURNAL   EMBO. J. 20 (2001) 3322-32.
  ORGANISM  Trypanosoma brucei [GN:tbr], human [GN:hsa]
PATHWAY     PATH: map00563  Glycosylphosphatidylinositol(GPI)-anchor
                            biosynthesis
            PATH: map01031  Glycan structures - biosynthesis 2
ORTHOLOGY   KO: K03434  N-acetylglucosaminylphosphatidylinositol deacetylase
GENES       HSA: 9487(PIGL)
            PTR: 468371(PIGL)
            MMU: 327942(Pigl)
            RNO: 192263(Pigl)
            SCE: YMR281W(GPI12)
            AGO: AGOS_ABL120W
            PIC: PICST_30247(GPI12)
            CGR: CAGL0M03047g
            SPO: SPAPB2B4.01c
            ANI: AN0049.2
            AFM: AFUA_5G12550
            AOR: AO090120000381
            CNE: CNC00580
            UMA: UM00302.1
            DDI: DDBDRAFT_0191808
            TAN: TA10880
            TPV: TP04_0615
            TET: TTHERM_00471420
            TBR: Tb11.01.3900
            TCR: 504005.20 511481.40
            LMA: LmjF09.0040
            EHI: 52.t00009
            FAL: FRAAL3175
            SEN: SACE_1008 SACE_1543
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.89
            ExPASy - ENZYME nomenclature database: 3.5.1.89
            ExplorEnz - The Enzyme Database: 3.5.1.89
            ERGO genome analysis and discovery system: 3.5.1.89
            BRENDA, the Enzyme Database: 3.5.1.89
///
ENTRY       EC 3.5.1.90                 Enzyme
NAME        adenosylcobinamide hydrolase;
            CbiZ;
            AdoCbi amidohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     adenosylcobinamide amidohydrolase
REACTION    adenosylcobinamide + H2O = adenosylcobyric acid +
            (R)-1-aminopropan-2-ol [RN:R05226]
ALL_REAC    R05226
SUBSTRATE   adenosylcobinamide;
            H2O [CPD:C00001]
PRODUCT     adenosylcobyric acid [CPD:C06507];
            (R)-1-aminopropan-2-ol [CPD:C03194]
COMMENT     Involved in the salvage pathway of cobinamide in archaea. Archaea
            convert adenosylcobinamide (AdoCbi) into adenosylcobinamide
            phosphate (AdoCbi-P) in two steps. First, the amidohydrolase
            activity of CbiZ cleaves off the aminopropanol moiety of AdoCbi
            yielding adenosylcobyric acid (AdoCby); second, AdoCby is converted
            into AdoCbi-P by the action of EC 6.3.1.10,
            adenosylcobinamide-phosphate synthase (CbiB).
REFERENCE   1  [PMID:14990804]
  AUTHORS   Woodson JD, Escalante-Semerena JC.
  TITLE     CbiZ, an amidohydrolase enzyme required for salvaging the coenzyme
            B12 precursor cobinamide in archaea.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 3591-6.
  ORGANISM  Methanosarcina mazei [GN:mma]
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K08260  adenosylcobinamide hydrolase
GENES       MAC: MA1623
            MBA: Mbar_A3636
            MMA: MM_0173
            MBU: Mbur_1001
            MHU: Mhun_2543
            MLA: Mlab_0705
            MEM: Memar_2352
            AFU: AF1400
            HAL: VNG1583C
            HMA: rrnAC1935
            HWA: HQ1406A(cbiZ)
            NPH: NP5300A
            PHO: PH0814
            PAB: PAB1708
            PFU: PF0305
            TKO: TK0846
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.90
            ExPASy - ENZYME nomenclature database: 3.5.1.90
            ExplorEnz - The Enzyme Database: 3.5.1.90
            ERGO genome analysis and discovery system: 3.5.1.90
            BRENDA, the Enzyme Database: 3.5.1.90
            CAS: 905988-16-1
///
ENTRY       EC 3.5.1.91                 Enzyme
NAME        N-substituted formamide deformylase;
            NfdA
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-benzylformamide amidohydrolase
REACTION    N-benzylformamide + H2O = formate + benzylamine [RN:R07303]
ALL_REAC    R07303
SUBSTRATE   N-benzylformamide [CPD:C15561];
            H2O [CPD:C00001]
PRODUCT     formate [CPD:C00058];
            benzylamine [CPD:C15562]
COMMENT     Zinc is a cofactor. While N-benzylformamide is the best substrate,
            the enzyme from Arthrobacter pascens can also act on the
            N-substituted formamides N-butylformamide, N-allylformamide,
            N-[2-(cyclohex-1-enyl)ethyl]formamide and
            N-(1-phenylethyl)formamide, but much more slowly. Amides of other
            acids do not act as substrates.
REFERENCE   1  [PMID:15358859]
  AUTHORS   Fukatsu H, Hashimoto Y, Goda M, Higashibata H, Kobayashi M.
  TITLE     Amine-synthesizing enzyme N-substituted formamide deformylase:
            screening, purification, characterization, and gene cloning.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 13726-31.
  ORGANISM  Arthrobacter pascens
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.91
            ExPASy - ENZYME nomenclature database: 3.5.1.91
            ExplorEnz - The Enzyme Database: 3.5.1.91
            ERGO genome analysis and discovery system: 3.5.1.91
            BRENDA, the Enzyme Database: 3.5.1.91
///
ENTRY       EC 3.5.1.92                 Enzyme
NAME        pantetheine hydrolase;
            pantetheinase;
            vanin;
            vanin-1
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     (R)-pantetheine amidohydrolase
REACTION    (R)-pantetheine + H2O = (R)-pantothenate + 2-aminoethanethiol
            [RN:R02973]
ALL_REAC    R02973
SUBSTRATE   (R)-pantetheine [CPD:C00831];
            H2O [CPD:C00001]
PRODUCT     (R)-pantothenate [CPD:C00864];
            2-aminoethanethiol [CPD:C01678]
COMMENT     The enzyme hydrolyses only one of the amide bonds of pantetheine.
            The substrate analogues phosphopantetheine and CoA are not
            substrates. The enzyme recycles pantothenate (vitamin B5) and
            produces 2-aminoethanethiol (cysteamine), a potent anti-oxidant [5].
REFERENCE   1  [PMID:440106]
  AUTHORS   Dupre S, Cavallini D.
  TITLE     Purification and properties of pantetheinase from horse kidney.
  JOURNAL   Methods. Enzymol. 62 (1979) 262-7.
  ORGANISM  horse
REFERENCE   2  [PMID:6549111]
  AUTHORS   Dupre S, Chiaraluce R, Nardini M, Cannella C, Ricci G, Cavallini D.
  TITLE     Continuous spectrophotometric assay of pantetheinase activity.
  JOURNAL   Anal. Biochem. 142 (1984) 175-81.
  ORGANISM  horse
REFERENCE   3  [PMID:10567687]
  AUTHORS   Maras B, Barra D, Dupre S, Pitari G.
  TITLE     Is pantetheinase the actual identity of mouse and human vanin-1
            proteins?
  JOURNAL   FEBS. Lett. 461 (1999) 149-52.
  ORGANISM  mouse [GN:mmu], human [GN:hsa]
REFERENCE   4  [PMID:8934567]
  AUTHORS   Aurrand-Lions M, Galland F, Bazin H, Zakharyev VM, Imhof BA, Naquet
            P.
  TITLE     Vanin-1, a novel GPI-linked perivascular molecule involved in thymus
            homing.
  JOURNAL   Immunity. 5 (1996) 391-405.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:11042271]
  AUTHORS   Pitari G, Malergue F, Martin F, Philippe JM, Massucci MT, Chabret C,
            Maras B, Dupre S, Naquet P, Galland F.
  TITLE     Pantetheinase activity of membrane-bound Vanin-1: lack of free
            cysteamine in tissues of Vanin-1 deficient mice.
  JOURNAL   FEBS. Lett. 483 (2000) 149-54.
  ORGANISM  mouse [GN:mmu]
REFERENCE   6  [PMID:11491533]
  AUTHORS   Martin F, Malergue F, Pitari G, Philippe JM, Philips S, Chabret C,
            Granjeaud S, Mattei MG, Mungall AJ, Naquet P, Galland F.
  TITLE     Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and
            encode isoforms of pantetheinase ectoenzymes.
  JOURNAL   Immunogenetics. 53 (2001) 296-306.
  ORGANISM  mouse [GN:mmu], human [GN:hsa]
REFERENCE   7  [PMID:11380987]
  AUTHORS   Pace HC, Brenner C.
  TITLE     The nitrilase superfamily: classification, structure and function.
  JOURNAL   Genome. Biol. 2 (2001) REVIEWS0001.
PATHWAY     PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K08069  pantetheine hydrolase
GENES       HSA: 8876(VNN1)
            MMU: 22361(Vnn1)
            CFA: 442973(VNN1)
            SSC: 397246(VNN1)
            GGA: 421701(VNN1)
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.92
            ExPASy - ENZYME nomenclature database: 3.5.1.92
            ExplorEnz - The Enzyme Database: 3.5.1.92
            ERGO genome analysis and discovery system: 3.5.1.92
            BRENDA, the Enzyme Database: 3.5.1.92
///
ENTRY       EC 3.5.1.93                 Enzyme
NAME        glutaryl-7-aminocephalosporanic-acid acylase;
            7beta-(4-carboxybutanamido)cephalosporanic acid acylase;
            cephalosporin C acylase;
            glutaryl-7-ACA acylase;
            CA;
            GCA;
            GA;
            cephalosporin acylase;
            glutaryl-7-aminocephalosporanic acid acylase;
            GL-7-ACA acylase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     (7R)-7-(4-carboxybutanamido)cephalosporanate amidohydrolase
REACTION    (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O =
            (7R)-7-aminocephalosporanate + glutarate [RN:R07402]
ALL_REAC    R07402
SUBSTRATE   (7R)-7-(4-carboxybutanamido)cephalosporanate [CPD:C15666];
            H2O [CPD:C00001]
PRODUCT     (7R)-7-aminocephalosporanate [CPD:C07756];
            glutarate [CPD:C00489]
COMMENT     Forms 7-aminocephalosporanic acid, a key intermediate in the
            synthesis of cephem antibiotics. It reacts only weakly with
            cephalosporin C.
REFERENCE   1  [PMID:7607251]
  AUTHORS   Ishii Y, Saito Y, Fujimura T, Sasaki H, Noguchi Y, Yamada H, Niwa M,
            Shimomura K.
  TITLE     High-level production, chemical modification and site-directed
            mutagenesis of a cephalosporin C acylase from Pseudomonas strain
            N176.
  JOURNAL   Eur. J. Biochem. 230 (1995) 773-8.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:10739919]
  AUTHORS   Kinoshita T, Tada T, Saito Y, Ishii Y, Sato A, Murata M.
  TITLE     Crystallization and preliminary X-ray analysis of cephalosporin C
            acylase from Pseudomonas sp. strain N176.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 56 ( Pt 4) (2000) 458-9.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:10972935]
  AUTHORS   Monti D, Carrea G, Riva S, Baldaro E, Frare G.
  TITLE     Characterization of an industrial biocatalyst: immobilized
            glutaryl-7-ACA acylase.
  JOURNAL   Biotechnol. Bioeng. 70 (2000) 239-44.
REFERENCE   4  [PMID:10945972]
  AUTHORS   Kwon TH, Rhee S, Lee YS, Park SS, Kim KH.
  TITLE     Crystallization and preliminary X-Ray diffraction analysis of
            glutaryl-7-aminocephalosporanic acid acylase from Pseudomonas sp.
            GK16.
  JOURNAL   J. Struct. Biol. 131 (2000) 79-81.
  ORGANISM  Pseudomonas sp.
REFERENCE   5  [PMID:11080627]
  AUTHORS   Kim Y, Yoon K, Khang Y, Turley S, Hol WG.
  TITLE     The 2.0 A crystal structure of cephalosporin acylase.
  JOURNAL   Structure. Fold. Des. 8 (2000) 1059-68.
  ORGANISM  Pseudomonas diminuta
REFERENCE   6  [PMID:11782466]
  AUTHORS   Huang X, Zeng R, Ding X, Mao X, Ding Y, Rao Z, Xie Y, Jiang W, Zhao
            G.
  TITLE     Affinity alkylation of the Trp-B4 residue of the beta -subunit of
            the glutaryl 7-aminocephalosporanic acid acylase of Pseudomonas sp.
            130.
  JOURNAL   J. Biol. Chem. 277 (2002) 10256-64.
  ORGANISM  Pseudomonas sp.
REFERENCE   7  [PMID:12680762]
  AUTHORS   Kim JK, Yang IS, Rhee S, Dauter Z, Lee YS, Park SS, Kim KH.
  TITLE     Crystal structures of glutaryl 7-aminocephalosporanic acid acylase:
            insight into autoproteolytic activation.
  JOURNAL   Biochemistry. 42 (2003) 4084-93.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00311  Penicillin and cephalosporin biosynthesis
GENES       PLA: Plav_0937
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.93
            ExPASy - ENZYME nomenclature database: 3.5.1.93
            ExplorEnz - The Enzyme Database: 3.5.1.93
            ERGO genome analysis and discovery system: 3.5.1.93
            BRENDA, the Enzyme Database: 3.5.1.93
///
ENTRY       EC 3.5.1.94                 Enzyme
NAME        gamma-glutamyl-gamma-aminobutyrate hydrolase;
            gamma-glutamyl-GABA hydrolase;
            PuuD;
            YcjL
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     4-(gamma-glutamylamino)butanoate amidohydrolase
REACTION    4-(gamma-glutamylamino)butanoate + H2O = 4-aminobutanoate +
            L-glutamate [RN:R07419]
ALL_REAC    R07419
SUBSTRATE   4-(gamma-glutamylamino)butanoate;
            H2O [CPD:C00001]
PRODUCT     4-aminobutanoate [CPD:C00334];
            L-glutamate [CPD:C00025]
COMMENT     Forms part of a novel putrescine-utilizing pathway in Escherichia
            coli, in which it has been hypothesized that putrescine is first
            glutamylated to form gamma-glutamylputrescine, which is oxidized to
            4-(gamma-glutamylamino)butanal and then to
            4-(gamma-glutamylamino)butanoate. The enzyme can also catalyse the
            reactions of EC 3.5.1.35 (D-glutaminase) and EC 3.5.1.65 (theanine
            hydrolase).
REFERENCE   1  [PMID:15590624]
  AUTHORS   Kurihara S, Oda S, Kato K, Kim HG, Koyanagi T, Kumagai H, Suzuki H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12.
  JOURNAL   J. Biol. Chem. 280 (2005) 4602-8.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K09473  gamma-glutamyl-gamma-aminobutyrate hydrolase
GENES       ECO: b1298(ycjL)
            ECJ: JW1291(puuD)
            ECE: Z2490(ycjL)
            ECS: ECs1875
            ECW: EcE24377A_1508(puuD)
            ECX: EcHS_A1413
            SFL: SF1303(ycjL)
            SFX: S1385(ycjL)
            SFV: SFV_1312(ycjL)
            SSN: SSON_1842(ycjL)
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.94
            ExPASy - ENZYME nomenclature database: 3.5.1.94
            ExplorEnz - The Enzyme Database: 3.5.1.94
            ERGO genome analysis and discovery system: 3.5.1.94
            BRENDA, the Enzyme Database: 3.5.1.94
///
ENTRY       EC 3.5.1.95                 Enzyme
NAME        N-malonylurea hydrolase;
            ureidomalonase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     3-oxo-3-ureidopropanoate amidohydrolase (urea- and malonate-forming)
REACTION    3-oxo-3-ureidopropanoate + H2O = malonate + urea [RN:R07629]
ALL_REAC    R07629
SUBSTRATE   3-oxo-3-ureidopropanoate [CPD:C15607];
            H2O [CPD:C00001]
PRODUCT     malonate [CPD:C00383];
            urea [CPD:C00086]
COMMENT     Forms part of the oxidative pyrimidine-degrading pathway in some
            microorganisms, along with EC 1.17.99.4 (uracil/thymine
            dehydrogenase) and EC 3.5.2.1 (barbiturase).
REFERENCE   1  [PMID:11485332]
  AUTHORS   Soong CL, Ogawa J, Shimizu S.
  TITLE     Novel amidohydrolytic reactions in oxidative pyrimidine metabolism:
            analysis of the barbiturase reaction and discovery of a novel
            enzyme, ureidomalonase.
  JOURNAL   Biochem. Biophys. Res. Commun. 286 (2001) 222-6.
  ORGANISM  Rhodococcus erythropolis
REFERENCE   2  [PMID:11748240]
  AUTHORS   Soong CL, Ogawa J, Sakuradani E, Shimizu S.
  TITLE     Barbiturase, a novel zinc-containing amidohydrolase involved in
            oxidative pyrimidine metabolism.
  JOURNAL   J. Biol. Chem. 277 (2002) 7051-8.
  ORGANISM  Rhodococcus erythropolis
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.95
            ExPASy - ENZYME nomenclature database: 3.5.1.95
            ExplorEnz - The Enzyme Database: 3.5.1.95
            ERGO genome analysis and discovery system: 3.5.1.95
            BRENDA, the Enzyme Database: 3.5.1.95
///
ENTRY       EC 3.5.1.96                 Enzyme
NAME        succinylglutamate desuccinylase;
            N2-succinylglutamate desuccinylase;
            SGDS;
            AstE
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
SYSNAME     N-succinyl-L-glutamate amidohydrolase
REACTION    N-succinyl-L-glutamate + H2O = succinate + L-glutamate [RN:R00411]
ALL_REAC    R00411
SUBSTRATE   N-succinyl-L-glutamate [CPD:C05931];
            H2O [CPD:C00001]
PRODUCT     succinate [CPD:C00042];
            L-glutamate [CPD:C00025]
COMMENT     Requires Co2+ for maximal activity [1]. N2-Acetylglutamate is not a
            substrate. This is the final enzyme in the arginine
            succinyltransferase (AST) pathway for the catabolism of arginine
            [1]. This pathway converts the carbon skeleton of arginine into
            glutamate, with the concomitant production of ammonia and conversion
            of succinyl-CoA into succinate and CoA. The five enzymes involved in
            this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC
            3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.11
            (acetylornithine transaminase), EC 1.2.1.71
            (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96
            (succinylglutamate desuccinylase).
REFERENCE   1  [PMID:2865249]
  AUTHORS   Vander Wauven C, Stalon V.
  TITLE     Occurrence of succinyl derivatives in the catabolism of arginine in
            Pseudomonas cepacia.
  JOURNAL   J. Bacteriol. 164 (1985) 882-6.
  ORGANISM  Pseudomonas cepacia
REFERENCE   2  [PMID:3534538]
  AUTHORS   Cunin R, Glansdorff N, Pierard A, Stalon V.
  TITLE     Biosynthesis and metabolism of arginine in bacteria.
  JOURNAL   Microbiol. Rev. 50 (1986) 314-52.
REFERENCE   3
  AUTHORS   Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V.
  TITLE     Erratum report: Biosynthesis and metabolism of arginine in bacteria.
  JOURNAL   Microbiol. Rev. 51 (1987) 178.
REFERENCE   4  [PMID:9393691]
  AUTHORS   Itoh Y.
  TITLE     Cloning and characterization of the aru genes encoding enzymes of
            the catabolic arginine succinyltransferase pathway in Pseudomonas
            aeruginosa.
  JOURNAL   J. Bacteriol. 179 (1997) 7280-90.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   5  [PMID:9696779]
  AUTHORS   Schneider BL, Kiupakis AK, Reitzer LJ.
  TITLE     Arginine catabolism and the arginine succinyltransferase pathway in
            Escherichia coli.
  JOURNAL   J. Bacteriol. 180 (1998) 4278-86.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K05526  succinylglutamate desuccinylase
GENES       ECO: b1744(astE)
            ECJ: JW1733(astE)
            ECE: Z2776(ydjS)
            ECS: ECs2450
            ECC: c2144(ydjS)
            ECI: UTI89_C1939(ydjS)
            ECP: ECP_1690
            ECV: APECO1_813(ydjS)
            ECW: EcE24377A_1966(astE)
            ECX: EcHS_A1827
            STY: STY1807(astE)
            STT: t1186(astE)
            SPT: SPA1537(astE)
            SEC: SC1328(astE)
            STM: STM1307(astE)
            YPE: YPO1966(astE)
            YPK: y2345
            YPM: YP_1711
            YPA: YPA_1348
            YPS: YPTB1963(astE)
            SFL: SF1482(ydjS)
            SFX: S1599(ydjS)
            SFV: SFV_1476(ydjS)
            SSN: SSON_1413(ydjS)
            SBO: SBO_1346(ydjS)
            SDY: SDY_1533(ydjS)
            PLU: plu3106(astE)
            VCH: VC1242
            VVU: VV1_2783
            VVY: VV1479
            VPA: VP1310
            VFI: VF1238
            PPR: PBPRA2153
            PAE: PA0901(aruE)
            PAU: PA14_52630(aruE)
            PAP: PSPA7_4614(astE)
            PPU: PP_4475(astE)
            PST: PSPTO_1838(astE)
            PSB: Psyr_3559
            PSP: PSPPH_3515(astE)
            PFL: PFL_4509(astE)
            PFO: Pfl_4279
            ACI: ACIAD1289(astE)
            SON: SO_2338(astE)
            SDN: Sden_1785
            SFR: Sfri_1934
            SHE: Shewmr4_2029
            SHM: Shewmr7_1946
            SHN: Shewana3_2132
            ILO: IL1681
            CPS: CPS_0633(astE)
            PHA: PSHAa1633
            PAT: Patl_2195
            HCH: HCH_05217(astE)
            CSA: Csal_2780
            AHA: AHA_2868
            CVI: CV_2877(astE)
            BMA: BMA0596(astE)
            BML: BMA10299_A2871(astE)
            BMN: BMA10247_1731(astE)
            BUR: Bcep18194_A4296
            BCN: Bcen_0706
            BCH: Bcen2424_1185
            BAM: Bamb_1066
            BPS: BPSL2385(astE)
            BPM: BURPS1710b_2841(astE)
            BPL: BURPS1106A_2780(astE)
            BPD: BURPS668_2722(astE)
            BTE: BTH_I1780
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.1.96
            ExPASy - ENZYME nomenclature database: 3.5.1.96
            ExplorEnz - The Enzyme Database: 3.5.1.96
            ERGO genome analysis and discovery system: 3.5.1.96
            BRENDA, the Enzyme Database: 3.5.1.96
///
ENTRY       EC 3.5.1.-                  Enzyme
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amides
REACTION    (1) Maleic acid + NH3 <=> Maleamate + H2O [RN:R03540];
            (2) UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine + H2O <=>
            UDP-3-O-(3-hydroxytetradecanoyl)-D-glucosamine + Acetate
            [RN:R04587];
            (3)
            N-(5'-Phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-D-
            ribosyl)-4-imidazolecarboxamide + H2O <=>
            5'-Phospho-D-1-ribulosylformimine +
            1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide [RN:R04655];
            (4) N2-Acetyl-L-lysine + H2O <=> L-Lysine + Acetate [RN:R06845];
            (5) N-Cyclohexylformamide + H2O <=> Cyclohexylamine + Formate
            [RN:R06940];
            (6) 3,5-Dibromo-4-hydroxybenzamide + H2O <=>
            3,5-Dibromo-4-hydroxybenzoate + NH3 [RN:R07782]
SUBSTRATE   Maleic acid [CPD:C01384];
            NH3 [CPD:C00014];
            UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine [CPD:C04738];
            H2O [CPD:C00001];
            N-(5'-Phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-D-
            ribosyl)-4-imidazolecarboxamide [CPD:C04916];
            N2-Acetyl-L-lysine [CPD:C12989];
            N-Cyclohexylformamide [CPD:C11519]
PRODUCT     Maleamate [CPD:C01596];
            H2O [CPD:C00001];
            UDP-3-O-(3-hydroxytetradecanoyl)-D-glucosamine [CPD:C06022];
            Acetate [CPD:C00033];
            5'-Phospho-D-1-ribulosylformimine [CPD:C05569];
            1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide [CPD:C04677];
            L-Lysine [CPD:C00047];
            Cyclohexylamine [CPD:C00571];
            Formate [CPD:C00058]
///
ENTRY       EC 3.5.2.1                  Enzyme
NAME        barbiturase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     barbiturate amidohydrolase (3-oxo-3-ureidopropanoate-forming)
REACTION    barbiturate + H2O = 3-oxo-3-ureidopropanoate [RN:R02139]
ALL_REAC    R02139;
            (other) R03870
SUBSTRATE   barbiturate [CPD:C00813];
            H2O [CPD:C00001]
PRODUCT     3-oxo-3-ureidopropanoate [CPD:C15607]
COMMENT     Contains zinc and is specific for barbiturate as substrate [3].
            Forms part of the oxidative pyrimidine-degrading pathway in some
            microorganisms, along with EC 1.17.99.4 (uracil/thymine
            dehydrogenase) and EC 3.5.1.95 (N-malonylurea hydrolase). It was
            previously thought that the end-products of the reaction were
            malonate and urea but this has since been disproved [2]. May be
            involved in the regulation of pyrimidine metabolism, along with EC
            2.4.2.9, uracil phosphoribosyltransferase.
REFERENCE   1  [PMID:12981104]
  AUTHORS   HAYAISHI O, KORNBERG A.
  TITLE     Metabolism of cytosine, thymine, uracil, and barbituric acid by
            bacterial enzymes.
  JOURNAL   J. Biol. Chem. 197 (1952) 717-32.
REFERENCE   2  [PMID:11485332]
  AUTHORS   Soong CL, Ogawa J, Shimizu S.
  TITLE     Novel amidohydrolytic reactions in oxidative pyrimidine metabolism:
            analysis of the barbiturase reaction and discovery of a novel
            enzyme, ureidomalonase.
  JOURNAL   Biochem. Biophys. Res. Commun. 286 (2001) 222-6.
  ORGANISM  Rhodococcus erythropolis
REFERENCE   3  [PMID:11748240]
  AUTHORS   Soong CL, Ogawa J, Sakuradani E, Shimizu S.
  TITLE     Barbiturase, a novel zinc-containing amidohydrolase involved in
            oxidative pyrimidine metabolism.
  JOURNAL   J. Biol. Chem. 277 (2002) 7051-8.
  ORGANISM  Rhodococcus erythropolis
PATHWAY     PATH: map00240  Pyrimidine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.1
            ExPASy - ENZYME nomenclature database: 3.5.2.1
            ExplorEnz - The Enzyme Database: 3.5.2.1
            ERGO genome analysis and discovery system: 3.5.2.1
            BRENDA, the Enzyme Database: 3.5.2.1
            CAS: 9025-16-5
///
ENTRY       EC 3.5.2.2                  Enzyme
NAME        dihydropyrimidinase;
            hydantoinase;
            hydropyrimidine hydrase;
            hydantoin peptidase;
            pyrimidine hydrase;
            D-hydantoinase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     5,6-dihydropyrimidine amidohydrolase
REACTION    5,6-dihydrouracil + H2O = 3-ureidopropanoate [RN:R02269]
ALL_REAC    R02269;
            (other) R03055
SUBSTRATE   5,6-dihydrouracil [CPD:C00429];
            H2O [CPD:C00001]
PRODUCT     3-ureidopropanoate [CPD:C02642]
COMMENT     Also acts on dihydrothymine and hydantoin.
REFERENCE   1  [PMID:6639068]
  AUTHORS   Brooks KP, Jones EA, Kim BD, Sander EG.
  TITLE     Bovine liver dihydropyrimidine amidohydrolase: purification,
            properties, and characterization as a zinc metalloenzyme.
  JOURNAL   Arch. Biochem. Biophys. 226 (1983) 469-83.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:15393763]
  AUTHORS   EADIE GS, BERNHEIM F, BERNHEIM ML.
  TITLE     The partial purification and properties of animal and plant
            hydantoinases.
  JOURNAL   J. Biol. Chem. 181 (1949) 449-58.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00240  Pyrimidine metabolism
            PATH: map00410  beta-Alanine metabolism
            PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K01464  dihydropyrimidinase
GENES       HSA: 1807(DPYS)
            MMU: 64705(Dpys)
            RNO: 65135(Dpys)
            GGA: 420266(DPYS)
            XLA: 495311(LOC495311)
            SPU: 579662(LOC579662)
            DME: Dmel_CG1411(CRMP)
            CEL: C47E12.8(dhp-2)
            OSA: 4327558
            ANI: AN1823.2 AN8418.2
            CNE: CNF01380
            DDI: DDB_0191172(pyd2)
            ECW: EcE24377A_3198(hyuA)
            ECX: EcHS_A3033(hyuA)
            PAE: PA0441
            PAU: PA14_05770(dhT)
            PAP: PSPA7_0543(hydA)
            PPF: Pput_1802
            PFL: PFL_2548(hydA)
            PFO: Pfl_3441
            PEN: PSEEN3253(dht)
            CPS: CPS_4055(dht)
            AHA: AHA_2164(hydA)
            REU: Reut_A0045
            REH: H16_A3075
            RME: Rmet_3886
            BXE: Bxe_A1431 Bxe_C0732
            BUR: Bcep18194_C6658
            BCN: Bcen_1593 Bcen_6385
            BCH: Bcen2424_6238 Bcen2424_6618
            BAM: Bamb_5963
            POL: Bpro_0551 Bpro_0686
            PNA: Pnap_4021
            AAV: Aave_0969
            VEI: Veis_0725 Veis_4149
            MLO: mll1629
            MES: Meso_2664
            SME: SMc01821(dht)
            SMD: Smed_2983
            ATU: Atu2386(dht)
            ATC: AGR_C_4328
            RET: RHE_CH03292(dht)
            RLE: RL3718(dht) RL4487 pRL120126
            BME: BMEI1644
            BMS: BR0278(dhT)
            BOV: BOV_0292(hydA)
            OAN: Oant_0347
            BJA: blr3295 blr3333 blr7615(dht)
            BRA: BRADO1492 BRADO1792(hyuA) BRADO6163(dht)
            BBT: BBta_2108(hyuA) BBta_6029(dht) BBta_6542
            SIL: SPO1783(hydA)
            SIT: TM1040_1497
            RSP: RSP_0183(dht) RSP_3462
            RSH: Rsph17029_1816 Rsph17029_3107
            RSQ: Rsph17025_1462 Rsph17025_2067
            JAN: Jann_1488 Jann_2705
            RDE: RD1_2404(hydA) RD1_3100(hydA)
            PDE: Pden_1112 Pden_4616
            ACR: Acry_0266
            SUS: Acid_7659
            BCL: ABC3783
            GKA: GK1423
            EFA: EF2580
            CTC: CTC01781
            CDF: CD2083 CD3178
            CBO: CBO2886
            CBA: CLB_2850(hydA-2)
            CBH: CLC_2783(hydA)
            CBF: CLI_2942(hydA)
            CBE: Cbei_1942 Cbei_1970
            CKL: CKL_2401
            AMT: Amet_4584
            DSY: DSY1806
            DRM: Dred_0261
            MTA: Moth_1997
            MSM: MSMEG_3553(hydA) MSMEG_3996(hydA) MSMEG_4012(hydA)
            SCO: SCO6415(SC1A6.04)
            SMA: SAV1949(dht)
            ART: Arth_4066
            NCA: Noca_1635
            FAL: FRAAL1416(pydB)
            KRA: Krad_4267
            SEN: SACE_3419(pydB)
            RXY: Rxyl_0219 Rxyl_0358 Rxyl_2746
            RCA: Rcas_3519
            TME: Tmel_0119
            MMA: MM_0750 MM_2253
STRUCTURES  PDB: 1GKP  1GKQ  1GKR  1NFG  1YNY  2FTW  2FTY  2FVK  2FVM  2GSE  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.2
            ExPASy - ENZYME nomenclature database: 3.5.2.2
            ExplorEnz - The Enzyme Database: 3.5.2.2
            ERGO genome analysis and discovery system: 3.5.2.2
            BRENDA, the Enzyme Database: 3.5.2.2
            CAS: 9030-74-4
///
ENTRY       EC 3.5.2.3                  Enzyme
NAME        dihydroorotase;
            carbamoylaspartic dehydrase;
            dihydroorotate hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     (S)-dihydroorotate amidohydrolase
REACTION    (S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate [RN:R01993]
ALL_REAC    R01993
SUBSTRATE   (S)-dihydroorotate [CPD:C00337];
            H2O [CPD:C00001]
PRODUCT     N-carbamoyl-L-aspartate [CPD:C00438]
REFERENCE   1
  AUTHORS   Cooper, C. and Wilson, D.W.
  TITLE     Biosynthesis of pyrimidines.
  JOURNAL   Fed. Proc. 13 (1954) 194.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:13163076]
  AUTHORS   LIEBERMAN I, KORNBERG A.
  TITLE     Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. I.
            Dihydroortic acid, ureidosuccinic acid, and
            5-carboxymethylhydantoin.
  JOURNAL   J. Biol. Chem. 207 (1954) 911-24.
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K01465  dihydroorotase
GENES       HSA: 790(CAD)
            MMU: 69719(Cad)
            CFA: 483009(CAD)
            XLA: 444548(MGC83388)
            DME: Dmel_CG18572(r) Dmel_CG6106
            CEL: D2085.1(pyr-1)
            ATH: AT4G04955(ATALN)
            OSA: 4325542
            CME: CMQ255C CMT584C
            SCE: YLR420W(URA4)
            AGO: AGOS_AER098W
            PIC: PICST_32048(URA4)
            CAL: CaO19.2360
            CGR: CAGL0J04598g
            SPO: SPAC16.03c
            ANI: AN0565.2 AN0961.2
            AFM: AFUA_8G00850
            AOR: AO090005001052
            CNE: CNA07120
            UMA: UM01521.1
            DDI: DDB_0201646(pyr1-3)
            PFA: PF14_0697
            TAN: TA11110
            TPV: TP04_0882
            TBR: Tb927.8.5630
            TCR: 506747.20 507059.70 508373.20
            LMA: LmjF16.0580
            EHI: 189.t00008
            ECO: b1062(pyrC)
            ECJ: JW1049(pyrC)
            ECE: Z1699(pyrC)
            ECS: ECs1440
            ECC: c1329(pyrC)
            ECI: UTI89_C1187(pyrC)
            ECP: ECP_1054
            ECV: APECO1_144(pyrC)
            ECW: EcE24377A_1185(pyrC)
            ECX: EcHS_A1185
            STY: STY1201(pyrC)
            STT: t1757(pyrC)
            SPT: SPA1688(pyrC)
            SEC: SC1111(pyrC)
            STM: STM1163(pyrC)
            YPE: YPO1587(pyrC)
            YPK: y1746(pyrC)
            YPM: YP_2265(pyrC)
            YPA: YPA_1940
            YPN: YPN_2042
            YPP: YPDSF_1859
            YPS: YPTB2482(pyrC)
            YPI: YpsIP31758_1567(pyrC)
            YEN: YE1625(b1062)
            SFL: SF1068(pyrC)
            SFX: S1146(pyrC)
            SFV: SFV_1084(pyrC)
            SSN: SSON_1082(pyrC)
            SBO: SBO_2002(pyrC)
            SDY: SDY_2091(pyrC)
            ECA: ECA1787(pyrC)
            PLU: plu1819(pyrC)
            BUC: BU334(pyrC)
            BAS: BUsg322(pyrC)
            WBR: WGLp087(pyrC)
            SGL: SG1051
            ENT: Ent638_1576
            SPE: Spro_1896
            XFA: XF0988
            XFT: PD0281(pyrC)
            XCC: XCC2257(pyrC)
            XCB: XC_1858
            XCV: XCV2559(pyrC)
            XAC: XAC2360(pyrC)
            XOO: XOO2683(pyrC)
            XOM: XOO_2531(XOO2531)
            VCH: VCA0925
            VCO: VC0395_0313(pyrC)
            VVU: VV2_1596
            VVY: VVA0407
            VPA: VPA0408
            VFI: VFA0412
            PPR: PBPRA2405
            PAE: PA0401 PA3527(pyrC) PA5541
            PAU: PA14_05250(pyrX) PA14_18710(pyrC) PA14_73070(pyrQ)
            PAP: PSPA7_1620(pyrC)
            PPU: PP_1086(pyrC) PP_4999
            PPF: Pput_1127
            PST: PSPTO_4157 PSPTO_5041
            PSB: Psyr_0481 Psyr_3894
            PSP: PSPPH_0472 PSPPH_3888(pyrC)
            PFL: PFL_4855(pyrC) PFL_5834(pyrC) PFL_6183
            PFO: Pfl_4519 Pfl_5315 Pfl_5663
            PEN: PSEEN1208(pyrC) PSEEN3119 PSEEN5062(pyrC')
            PMY: Pmen_1392 Pmen_4541
            PAR: Psyc_0543(pyrC) Psyc_1632(pyrC)
            PCR: Pcryo_0532 Pcryo_1865
            PRW: PsycPRwf_1660
            ACI: ACIAD1150(pyrC) ACIAD1271(pyrX) ACIAD1419
            SON: SO_3695(pyrC)
            SDN: Sden_1679
            SFR: Sfri_0589
            SAZ: Sama_2870
            SBL: Sbal_3344
            SBM: Shew185_0995
            SLO: Shew_0728
            SPC: Sputcn32_2994
            SSE: Ssed_3595
            SPL: Spea_3215
            SHE: Shewmr4_0860
            SHM: Shewmr7_3162
            SHN: Shewana3_3263
            SHW: Sputw3181_0953
            ILO: IL0362(pyrC)
            CPS: CPS_2613(pyrC) CPS_4867
            PHA: PSHAa1183(pyrC)
            PAT: Patl_0584
            SDE: Sde_2428
            PIN: Ping_2294
            MAQ: Maqu_2505
            CBU: CBU_1703(pyrC)
            CBD: COXBU7E912_0302(pyrC)
            LPN: lpg2963(pyrC)
            LPF: lpl2893(pyrC)
            LPP: lpp3035(pyrC)
            MCA: MCA2075(pyrC) MCA2332
            FTU: FTT1660c(pyrC)
            FTF: FTF1660c(pyrC)
            FTH: FTH_0032(pyrC)
            FTN: FTN_0024(pyrC)
            TCX: Tcr_1830
            NOC: Noc_0364 Noc_2521
            AEH: Mlg_0345 Mlg_0597
            HHA: Hhal_0730
            HCH: HCH_00554 HCH_04992(pyrC)
            CSA: Csal_3231
            ABO: ABO_0034(pyrC-2) ABO_1683(pyrC) ABO_1794(pyrC)
            MMW: Mmwyl1_2376
            AHA: AHA_2602
            DNO: DNO_0657(pyrC)
            BCI: BCI_0441(pyrC)
            RMA: Rmag_0015
            VOK: COSY_0015(pyrC)
            NME: NMB0682
            NMA: NMA0884(pyrC)
            NMC: NMC0633(pyrC)
            NGO: NGO0255
            CVI: CV_4330(pyrC)
            RSO: RSc0487(pyrC) RSc0679(pyrX)
            REU: Reut_A0464 Reut_A0709
            REH: H16_A0479(pyrC) H16_A2912(pyrX)
            RME: Rmet_0406 Rmet_2739
            BMA: BMA1993(pyrC') BMA2422(pyrC)
            BMV: BMASAVP1_A0338(pyrC)
            BML: BMA10299_A1199(pyrC)
            BMN: BMA10247_2609(pyrC)
            BXE: Bxe_A0602 Bxe_A3807
            BVI: Bcep1808_0641
            BUR: Bcep18194_A3762 Bcep18194_A3966
            BCN: Bcen_0192 Bcen_0386
            BCH: Bcen2424_0675 Bcen2424_0868
            BAM: Bamb_0570 Bamb_0741
            BPS: BPSL2689(pyrX) BPSL2914(pyrC)
            BPM: BURPS1710b_3166(pyrX) BURPS1710b_3425(pyrC)
            BPL: BURPS1106A_3144(pyrC) BURPS1106A_3417(pyrC)
            BPD: BURPS668_3108(pyrC) BURPS668_3382(pyrC)
            BTE: BTH_I1230(pyrC) BTH_I1466
            PNU: Pnuc_1888
            BPE: BP0322(pyrC) BP3035(pyrC)
            BPA: BPP3762(pyrC) BPP3929(pyrC)
            BBR: BB4208(pyrC) BB4402(pyrC)
            RFR: Rfer_1381 Rfer_3464
            POL: Bpro_1024
            PNA: Pnap_3451
            AAV: Aave_4319
            AJS: Ajs_3745
            VEI: Veis_1215
            MPT: Mpe_A0448 Mpe_A0709
            HAR: HEAR0229(pyrC) HEAR2736(pyrC')
            MMS: mma_0283 mma_2946
            NEU: NE0727(pyrC) NE1664(pyrX)
            NET: Neut_0452 Neut_1659
            NMU: Nmul_A0354 Nmul_A2482
            EBA: ebA1456(pyrC) ebA1760(pyrX)
            AZO: azo0873(pyrC) azo3463(pyrX)
            DAR: Daro_0506 Daro_3889
            TBD: Tbd_0109 Tbd_2583
            MFA: Mfla_2103 Mfla_2280
            HPY: HP0266(pyrC) HP0581
            HPJ: jhp0251(pyrC_1) jhp0528(pyrC_2)
            HPA: HPAG1_0268 HPAG1_0560
            HHE: HH0614(pyrC_2) HH1766(pyrC_1)
            HAC: Hac_0524(pyrC) Hac_1431(pyrC)
            WSU: WS1479(pyrC2) WS2002(pyrC)
            TDN: Tmden_0624 Tmden_0905
            CJE: Cj0259(pyrC) Cj1195c(pyrC2)
            CJR: CJE0309(pyrC) CJE1329
            CJJ: CJJ81176_0286(pyrC)
            CJU: C8J_0236(pyrC) C8J_1139
            CJD: JJD26997_1722(pyrC)
            CFF: CFF8240_1476
            CCV: CCV52592_0154
            CHA: CHAB381_0965
            CCO: CCC13826_0308
            ABU: Abu_0199(pyrC)
            NIS: NIS_1427(pyrC)
            SUN: SUN_0390(pyrC)
            GSU: GSU1272(pyrC)
            GME: Gmet_1770
            GUR: Gura_1857
            PCA: Pcar_1614
            PPD: Ppro_2528
            DVU: DVU2902(pyrC)
            DVL: Dvul_0463
            DDE: Dde_2965
            LIP: LI0819(pyrC)
            BBA: Bd2688(pyrC)
            DPS: DP0105
            ADE: Adeh_1619
            AFW: Anae109_2192
            MXA: MXAN_3511(pyrC)
            SAT: SYN_01533
            SFU: Sfum_2091
            WOL: WD0230(pyrC)
            WBM: Wbm0446(pyrC)
            AMA: AM939(pyrC)
            APH: APH_0245(pyrC)
            ERU: Erum6350(pyrC)
            ERW: ERWE_CDS_06660(pyrC)
            ERG: ERGA_CDS_06570(pyrC)
            ECN: Ecaj_0639
            ECH: ECH_0373(pyrC)
            NSE: NSE_0154(pyrC)
            PUB: SAR11_0622(pyrC2) SAR11_1081(pyrC)
            MLO: mlr0687 mlr7790
            MES: Meso_1358 Meso_1475
            PLA: Plav_2835
            SME: SMc01361 SMc02166(pyrC)
            SMD: Smed_0106
            ATU: Atu0399(pyrC) Atu1307(pyrC)
            ATC: AGR_C_2404 AGR_C_703
            RET: RHE_CH00469(pyrC) RHE_CH01641(ypch00562) RHE_CH03292(dht)
                 RHE_PE00295
            RLE: RL0493(pyrC) RL1738(pyrC) pRL110419 pRL120121
            BME: BMEI1281 BMEII0669
            BMF: BAB1_0688(pyrC-1) BAB2_0640
            BMS: BR0668(pyrC-1) BRA0600(pyrC-2)
            BMB: BruAb1_0685(pyrC-1) BruAb2_0624(pyrC-2)
            BOV: BOV_0661(pyrC-1) BOV_A0565(pyrC-2)
            OAN: Oant_2621 Oant_3667
            BJA: blr2555(pyrC) blr5100
            BRA: BRADO2048 BRADO4503(pyrC)
            BBT: BBta_2376 BBta_4726(pyrC)
            RPA: RPA1069(pyrC) RPA3118(pyr)
            RPB: RPB_2423
            RPC: RPC_2246
            RPD: RPD_3029
            RPE: RPE_3374
            NWI: Nwi_2008 Nwi_2703
            NHA: Nham_2283
            BHE: BH05160(pyrC1) BH08190(pyrC2)
            BQU: BQ04350(pyrC1) BQ06390(pyrC2)
            XAU: Xaut_3918
            CCR: CC_0388 CC_2444
            SIL: SPO0284 SPO2653
            SIT: TM1040_1776 TM1040_3072
            RSP: RSP_1003(pyrC) RSP_1930(pyrC)
            RSH: Rsph17029_0581
            RSQ: Rsph17025_0325
            JAN: Jann_1742 Jann_3905
            RDE: RD1_3235(pyrC) RD1_3429(pyr)
            PDE: Pden_4467
            HNE: HNE_2303
            ZMO: ZMO0792(pyrC) ZMO1689(pyrC)
            NAR: Saro_0935 Saro_3062
            SAL: Sala_0923 Sala_1427
            SWI: Swit_0603 Swit_2737
            ELI: ELI_01035 ELI_02850
            GOX: GOX1266 GOX1965
            GBE: GbCGDNIH1_0807 GbCGDNIH1_2291
            ACR: Acry_0732
            RRU: Rru_A3191
            MAG: amb3614
            MGM: Mmc1_0102
            ABA: Acid345_4149
            SUS: Acid_5513
            BSU: BG10714(pyrC)
            BHA: BH2538(pyrC)
            BAN: BA4027(pyrC)
            BAR: GBAA4027(pyrC)
            BAA: BA_4498
            BAT: BAS3739
            BCE: BC3888(pyrC)
            BCA: BCE_3933(pyrC)
            BCZ: BCZK3647(pyrC) BCZK4599
            BCY: Bcer98_2537
            BTK: BT9727_3630(pyrC)
            BTL: BALH_3518(pyrC)
            BLI: BL02274(pyrC)
            BLD: BLi01770(pyrC)
            BCL: ABC1407 ABC2335(pyrC)
            BAY: RBAM_015330
            BPU: BPUM_1449
            OIH: OB1489(pyrC)
            GKA: GK1150(pyrC)
            SAU: SA1044(pyrC)
            SAV: SAV1201(pyrC)
            SAM: MW1084(pyrC)
            SAR: SAR1177(pyrC)
            SAS: SAS1135(pyrC)
            SAC: SACOL1213(pyrC)
            SAB: SAB1065(pyrC)
            SAA: SAUSA300_1094(pyrC)
            SAO: SAOUHSC_01168
            SAJ: SaurJH9_1260
            SAH: SaurJH1_1285
            SEP: SE0877
            SER: SERP0767(pyrC)
            SHA: SH1713(pyrC)
            SSP: SSP1571
            LMO: lmo1837(pyrC)
            LMF: LMOf2365_1865(pyrC)
            LIN: lin1951(pyrC)
            LWE: lwe1856(pyrC)
            LLA: L81189(pyrC)
            LLC: LACR_1160
            LLM: llmg_1508(pyrC)
            SPY: SPy_0907(pyrC)
            SPZ: M5005_Spy_0709(pyrC)
            SPM: spyM18_0965(pyrC)
            SPG: SpyM3_0622(pyrC)
            SPS: SPs1231
            SPH: MGAS10270_Spy0767(pyrC)
            SPI: MGAS10750_Spy0801(pyrC)
            SPJ: MGAS2096_Spy0781(pyrC)
            SPK: MGAS9429_Spy0765(pyrC)
            SPF: SpyM51099(pyrC)
            SPA: M6_Spy0726(pyrC)
            SPB: M28_Spy0689(pyrC)
            SPN: SP_1167
            SPR: spr1053(pyrC)
            SPD: SPD_1030(pyrC)
            SAG: SAG1045(pyrC)
            SAN: gbs1080(pyrC)
            SAK: SAK_1135(pyrC)
            SMU: SMU.1214(pyrC)
            STC: str1054(pyrC)
            STL: stu1054(pyrC)
            SSA: SSA_1235(pyrC)
            SGO: SGO_1248(pyrC)
            LPL: lp_2702(pyrC)
            LJO: LJ1278
            LAC: LBA1381(pyrC)
            LSA: LSA0953(pyrC)
            LSL: LSL_0191(pyrC)
            LDB: Ldb2111(pyrC1)
            LBU: LBUL_1952
            LCA: LSEI_1454
            LRE: Lreu_0124
            EFA: EF1718(pyrC)
            OOE: OEOE_0259
            STH: STH1258
            CAC: CAC0519(pyrC)
            CPE: CPE1181(pyrC)
            CPF: CPF_1385(pyrC)
            CPR: CPR_1200(pyrC)
            CTC: CTC00927(pyrC) CTC02382
            CNO: NT01CX_0394
            CTH: Cthe_0952
            CDF: CD1526(pyrC)
            CBO: CBO3239(pyrC)
            CBA: CLB_3276(pyrC)
            CBH: CLC_3150(pyrC)
            CBF: CLI_3378(pyrC)
            CBE: Cbei_1002
            CKL: CKL_3359(pyrC)
            CHY: CHY_1501(pyrC)
            DSY: DSY2861 DSY3585 DSY4348
            DRM: Dred_1682
            SWO: Swol_1283
            CSC: Csac_1932
            TTE: TTE1533(pyrC)
            MTA: Moth_0880
            MPE: MYPE7880(pyrC)
            MTU: Rv1381(pyrC)
            MTC: MT1425(pyrC)
            MBO: Mb1416(pyrC)
            MBB: BCG_1442(pyrC)
            MLE: ML0533(pyrC)
            MPA: MAP1116(pyrC)
            MAV: MAV_3392
            MSM: MSMEG_3044
            MVA: Mvan_2661
            MGI: Mflv_3746
            MMC: Mmcs_2364
            MKM: Mkms_2411
            MJL: Mjls_2405
            CGL: NCgl1549(pyrC)
            CGB: cg1815(pyrC)
            CEF: CE1731
            CDI: DIP1333(pyrC)
            CJK: jk1024(pyrC)
            NFA: nfa36220
            RHA: RHA1_ro07149(pyrC)
            SCO: SCO1486(pyrC)
            SMA: SAV6864(pyrC)
            TWH: TWT367(pyrC)
            TWS: TW402(pyrC)
            LXX: Lxx11070(pyrC)
            CMI: CMM_1785(pyrC)
            ART: Arth_2265
            AAU: AAur_2268(pyrC)
            PAC: PPA0998
            NCA: Noca_2429
            TFU: Tfu_1055(pyrC)
            FRA: Francci3_3201
            FAL: FRAAL5237(pyrC)
            ACE: Acel_1300
            KRA: Krad_3004
            SEN: SACE_2080
            STP: Strop_1854
            BLO: BL0792(pyrC)
            BAD: BAD_0761(pyrC)
            RXY: Rxyl_1479
            FNU: FN0420
            RBA: RB10192(pyrC) RB7430(pyrC)
            TDE: TDE2107
            LIL: LA3636(pyrC)
            LIC: LIC10574(pyrC)
            LBJ: LBJ_2850
            LBL: LBL_0221
            SYN: sll1018(pyrC) slr0406(pyrC)
            SYW: SYNW1523(pyrC) SYNW1764
            SYC: syc1031_c syc1033_c(pyrC)
            SYF: Synpcc7942_0486 Synpcc7942_0488
            SYD: Syncc9605_0700 Syncc9605_0986
            SYE: Syncc9902_0892 Syncc9902_1658
            SYG: sync_1922(pyrC) sync_2013
            SYR: SynRCC307_0409(pyrC) SynRCC307_0868(pyrC)
            SYX: SynWH7803_0629(pyrC) SynWH7803_0720(pyrC)
            CYA: CYA_0178(pyrC) CYA_1664
            CYB: CYB_1021 CYB_2522(pyrC)
            TEL: tll0666 tlr1533(pyrC)
            GVI: gll3822(pyrC) glr3669(pyrC)
            ANA: all2303 alr3339
            AVA: Ava_3650
            PMA: Pro0514(pyrC) Pro0571(pyrC)
            PMM: PMM0514 PMM0569(pyrC)
            PMT: PMT0468(pyrC) PMT1253
            PMN: PMN2A_0005
            PMI: PMT9312_0569
            PMB: A9601_06251
            PMC: P9515_05781 P9515_06331
            PMF: P9303_07521 P9303_18131
            PMG: P9301_05951
            PMH: P9215_06501
            PME: NATL1_06241
            TER: Tery_2179
            BTH: BT_0250
            BFR: BF3129
            BFS: BF2965
            PGI: PG0919(pyrC)
            SRU: SRU_2198
            CHU: CHU_1007(pyrC) CHU_1793(pyrC)
            GFO: GFO_0109(pyrC) GFO_1454(pyrC)
            FJO: Fjoh_0553
            FPS: FP0164(pyrC1) FP1094(pyrC2)
            CTE: CT1042(pyrC)
            CCH: Cag_0898(pyrC)
            PLT: Plut_1013(pyrC)
            DET: DET1200(pyrC)
            DEH: cbdb_A1114(pyrC)
            DEB: DehaBAV1_1010
            RRS: RoseRS_2557 RoseRS_2862
            RCA: Rcas_1848 Rcas_2435
            DRA: DR_1106
            DGE: Dgeo_0502
            TTH: TTC0426
            TTJ: TTHA0781
            AAE: aq_806(pyrC)
            TMA: TM0335
            MMP: MMP1009(pyrC)
            MMQ: MmarC5_0585
            MMZ: MmarC7_0251
            MAE: Maeo_1111
            MVN: Mevan_0336
            MAC: MA0892(pyrC)
            MBA: Mbar_A1783
            MMA: MM_2011
            MBU: Mbur_0757
            MTP: Mthe_1113
            MEM: Memar_1019
            MST: Msp_0323(pyrC)
            MSI: Msm_0997
            MKA: MK0530(pyrC)
            HAL: VNG2533G(pyrC)
            HMA: pNG7258(pyrC) rrnAC2232(pyrC) rrnAC3411
            HWA: HQ1061A(pyrC) HQ1936A(pyrC)
            NPH: NP1706A(pyrC)
            TAC: Ta1319
            TVO: TVN0269
            PTO: PTO1424
            PAB: PAB1149(pyrC)
            PFU: PF0189
            TKO: TK1805
            RCI: RCIX288(pyrC)
            APE: APE_0261.1
            HBU: Hbut_0107
            SSO: SSO0611(pyrC)
            STO: ST1478
            SAI: Saci_1593(pyrC)
            PAI: PAE0322(pyrC)
            TPE: Tpen_1159
STRUCTURES  PDB: 1J79  1XGE  1XRF  1XRT  2E25  2EG6  2EG7  2EG8  2Z24  2Z25  
                 2Z26  2Z27  2Z28  2Z29  2Z2A  2Z2B  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.3
            ExPASy - ENZYME nomenclature database: 3.5.2.3
            ExplorEnz - The Enzyme Database: 3.5.2.3
            ERGO genome analysis and discovery system: 3.5.2.3
            BRENDA, the Enzyme Database: 3.5.2.3
            CAS: 9024-93-5
///
ENTRY       EC 3.5.2.4                  Enzyme
NAME        carboxymethylhydantoinase;
            hydantoin hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     L-5-carboxymethylhydantoin amidohydrolase
REACTION    L-5-carboxymethylhydantoin + H2O = N-carbamoyl-L-aspartate
            [RN:R02284]
ALL_REAC    R02284
SUBSTRATE   L-5-carboxymethylhydantoin [CPD:C03703];
            H2O [CPD:C00001]
PRODUCT     N-carbamoyl-L-aspartate [CPD:C00438]
REFERENCE   1  [PMID:13163076]
  AUTHORS   LIEBERMAN I, KORNBERG A.
  TITLE     Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. I.
            Dihydroortic acid, ureidosuccinic acid, and
            5-carboxymethylhydantoin.
  JOURNAL   J. Biol. Chem. 207 (1954) 911-24.
  ORGANISM  Zymobacterium oroticum
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.4
            ExPASy - ENZYME nomenclature database: 3.5.2.4
            ExplorEnz - The Enzyme Database: 3.5.2.4
            ERGO genome analysis and discovery system: 3.5.2.4
            BRENDA, the Enzyme Database: 3.5.2.4
            CAS: 9025-14-3
///
ENTRY       EC 3.5.2.5                  Enzyme
NAME        allantoinase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     (S)-allantoin amidohydrolase
REACTION    (S)-allantoin + H2O = allantoate [RN:R02425]
ALL_REAC    R02425;
            (other) R02424
SUBSTRATE   (S)-allantoin [CPD:C02350];
            H2O [CPD:C00001]
PRODUCT     allantoate [CPD:C00499]
REFERENCE   1
  AUTHORS   Florkin, M. and Duchateau-Bosson, G.
  TITLE     Microdosage photometrique de l'allantoine en solutions pures et dans
            l'urine.
  JOURNAL   Enzymologia 9 (1940) 5-9.
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01466  allantoinase
GENES       SCE: YIR027C(DAL1)
            AGO: AGOS_AER218C
            PIC: PICST_34891(ALN1)
            ANI: AN4603.2
            AFM: AFUA_2G02250
            AOR: AO090011000504
            CNE: CND00740
            DDI: DDB_0231351(allB2) DDB_0231352(allB1)
            ECO: b0512(allB)
            ECJ: JW0500(allB)
            ECE: Z0666 Z0667
            ECC: c0626(ybbX)
            ECI: UTI89_C0540(ybbX)
            ECP: ECP_0572
            ECV: APECO1_1503(allB)
            ECW: EcE24377A_0548(allB)
            ECX: EcHS_A0585
            STY: STY0571(allB)
            STT: t2338(allB)
            SPT: SPA2200(allB)
            SEC: SC0562(allB)
            STM: STM0523(allB)
            FTL: FTL_0033
            TCX: Tcr_1889
            HCH: HCH_01096(allB) HCH_01704
            RME: Rmet_1103
            BUR: Bcep18194_B0320 Bcep18194_B3013
            BCN: Bcen_3038
            BCH: Bcen2424_5328
            BPS: BPSL1681
            BPM: BURPS1710b_2181
            BPA: BPP1127
            BBR: BB1343
            POL: Bpro_1146
            NIS: NIS_1114(allB)
            SFU: Sfum_2145
            PLA: Plav_0750
            RET: RHE_CH00351
            RLE: RL0368(pucH)
            BRA: BRADO2048
            BBT: BBta_2376
            RPB: RPB_1118
            RPC: RPC_4330
            RPD: RPD_1239
            RPE: RPE_4389
            NHA: Nham_4018
            XAU: Xaut_1415
            JAN: Jann_4128
            PDE: Pden_3514
            MMR: Mmar10_0814
            RRU: Rru_A2936
            MAG: amb1265
            SUS: Acid_0362
            BSU: BG13982(pucH)
            BHA: BH2309
            BLI: BL01094(pucH)
            BLD: BLi01126(pucH)
            BCL: ABC3732(pucH)
            EFA: EF2999
            CHY: CHY_0678(allB)
            DSY: DSY4163 DSY4164
            MGI: Mflv_3169
            RHA: RHA1_ro02570
            SCO: SCO6247(SCAH10.12)
            SMA: SAV1996(pucH)
            ART: Arth_3693
            AAU: AAur_3510(allB)
            TFU: Tfu_0962
            FRA: Francci3_0839
            FAL: FRAAL1460
            KRA: Krad_2077
            SEN: SACE_6727
            RXY: Rxyl_2845
            ANA: alr5010
            AVA: Ava_0120
            TER: Tery_2177
            DRA: DR_1153
            DGE: Dgeo_2609
            HMA: rrnAC1504(tatD)
            SMR: Smar_0126
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.5
            ExPASy - ENZYME nomenclature database: 3.5.2.5
            ExplorEnz - The Enzyme Database: 3.5.2.5
            ERGO genome analysis and discovery system: 3.5.2.5
            BRENDA, the Enzyme Database: 3.5.2.5
            CAS: 9025-20-1
///
ENTRY       EC 3.5.2.6                  Enzyme
NAME        beta-lactamase;
            penicillinase;
            cephalosporinase;
            neutrapen;
            penicillin beta-lactamase;
            exopenicillinase;
            ampicillinase;
            penicillin amido-beta-lactamhydrolase;
            penicillinase I, II;
            beta-lactamase I-III;
            beta-lactamase A, B, C;
            beta-lactamase AME I;
            cephalosporin-beta-lactamase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     beta-lactam hydrolase
REACTION    a beta-lactam + H2O = a substituted beta-amino acid [RN:R03743]
ALL_REAC    R03743 > R06363
SUBSTRATE   beta-lactam [CPD:C01866];
            H2O [CPD:C00001]
PRODUCT     substituted beta-amino acid [CPD:C03806]
INHIBITOR   m-Carboxyphenyl phenylacetamidomethylphosphonate [CPD:C04684]
COMMENT     A group of enzymes of varying specificity hydrolysing beta-lactams;
            some act more rapidly on penicillins, some more rapidly on
            cephalosporins. The latter were formerly listed as EC 3.5.2.8,
            cephalosporinase.
REFERENCE   1
  AUTHORS   Citri, N.
  TITLE     Penicillinase and other beta-lactamases.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 4, Academic Press,
            New York, 1971, p. 23-46.
REFERENCE   2  [PMID:5685878]
  AUTHORS   Hennessey TD, Richmond MH.
  TITLE     The purification and some properties of a beta-lactamase
            (cephalosporinase) synthesized by Enterobactercloacae.
  JOURNAL   Biochem. J. 109 (1968) 469-73.
  ORGANISM  Enterobacter cloacae
REFERENCE   3  [PMID:4990588]
  AUTHORS   Kuwabara S.
  TITLE     Purification and properties of two extracellular beta-lactamases
            from Bacillus cereus 569-H.
  JOURNAL   Biochem. J. 118 (1970) 457-65.
  ORGANISM  Bacillus cereus
REFERENCE   4
  AUTHORS   Pollock, M.R.
  TITLE     Penicillinase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 269-278.
REFERENCE   5
  AUTHORS   Pollock, M.R., Torriani, A.-M. and Tridgell, E.G.
  TITLE     Crystalline bacterial penicillinase.
  JOURNAL   Biochem. J. 62 (1956) 387-391.
  ORGANISM  Bacillus cereus, Escherichia coli [GN:eco]
REFERENCE   6  [PMID:4731970]
  AUTHORS   Ross GW, Boulton MG.
  TITLE     Purification of beta-lactamases on QAE-sephadex.
  JOURNAL   Biochim. Biophys. Acta. 309 (1973) 430-9.
  ORGANISM  Klebsiella aerogenes
PATHWAY     PATH: map00311  Penicillin and cephalosporin biosynthesis
            PATH: map00312  beta-Lactam resistance
            PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K01467  beta-lactamase
GENES       PIC: PICST_88817(BDE99)
            TET: TTHERM_00170490
            ECO: b0376(ampH) b4150(ampC)
            ECJ: JW4111(ampC)
            ECE: Z5757(ampC)
            ECS: ECs5131
            ECC: c5238(ampC)
            ECI: UTI89_C0391(yaiH) UTI89_C4750(ampC)
            ECP: ECP_4396
            ECW: EcE24377A_4709(ampC)
            ECX: EcHS_A4394
            STY: HCM1.216(bla)
            SEC: SC018(tem-1) SC090(ampC)
            YEN: YE2019(blaA) YE2440(ampC)
            SFL: SF4308(ampC)
            SFX: S4573(ampC)
            SFV: SFV_4309(ampC)
            SSN: SSON_4336(ampC)
            SBO: SBO_4306(ampC)
            SDY: SDY_4394(ampC)
            PLU: plu0831(ampC)
            ENT: Ent638_0339
            SPE: Spro_3259
            XFA: XF1621
            XFT: PD1157(pbp)
            XCC: XCC2636 XCC2873(bla) XCC3039(bla)
            XCB: XC_1119 XC_1235 XC_1481
            XCV: XCV2113(ampC1) XCV2967(ampC2) XCV3193(ampC3) XCV3293(penP)
            XAC: XAC2806 XAC3057(bla) XAC3162(bla)
            XOO: XOO1370(bla) XOO1556 XOO1797(bla)
            XOM: XOO_1261(XOO1261) XOO_1444(XOO1444) XOO_1700(XOO1700)
            VPA: VPA0477
            VFI: VF1099
            PAE: PA4110(ampC) PA5514
            PAU: PA14_10790(ampC) PA14_72760
            PAP: PSPA7_6316
            PPU: PP_2876(ampC)
            PST: PSPTO_3594(ampC)
            PSB: Psyr_3364
            PSP: PSPPH_3284
            PFL: PFL_4054
            PFO: Pfl_3723
            PEN: PSEEN3018(ampC)
            PCR: Pcryo_1775
            ACI: ACIAD3597(ampC)
            SON: SO_0837 SO_2388
            SDN: Sden_0675 Sden_0822 Sden_3154
            SFR: Sfri_0887
            SAZ: Sama_1178
            SBL: Sbal_2086 Sbal_3522
            SBM: Shew185_0813
            SLO: Shew_3220
            SPC: Sputcn32_3157
            SSE: Ssed_3414
            SPL: Spea_2637
            SHE: Shewmr4_0694 Shewmr4_1937
            SHM: Shewmr7_2039 Shewmr7_3328
            SHN: Shewana3_1990 Shewana3_3440
            SHW: Sputw3181_0786
            CPS: CPS_0483
            PAT: Patl_4159
            MAQ: Maqu_1080
            CBD: COXBU7E912_0739(ampC)
            LPN: lpg1618 lpg2412(ampC)
            LPF: lpl1405 lpl2336
            LPP: lpp1588 lpp2481
            MCA: MCA2220
            FTU: FTT0611c FTT0681c(blaA)
            FTF: FTF0611c FTF0681c(blaA)
            FTW: FTW_1047(blaA)
            FTL: FTL_0879 FTL_0957
            FTH: FTH_0865(bla) FTH_0935(penP)
            FTN: FTN_1002(blaA) FTN_1072
            NOC: Noc_2705
            HCH: HCH_02299(penP)
            CSA: Csal_0193
            ABO: ABO_1222(bla)
            AHA: AHA_0740 AHA_3135 AHA_4258
            CVI: CV_1310(ampC) CV_3150
            RSO: RS02005(RSp0030) RSc0258(RS00693)
            REU: Reut_A0157 Reut_A1684
            REH: H16_A1195 H16_A2128(bla1) H16_B0553(bla2) H16_B0871
                 H16_B1301(ampC1) H16_B1495 H16_B1574(ampC2)
            RME: Rmet_0121 Rmet_1776 Rmet_4436
            BMA: BMAA1283(penA)
            BMV: BMASAVP1_0257(blaA)
            BML: BMA10299_0527(blaA)
            BMN: BMA10247_A1040(blaA)
            BXE: Bxe_B1593
            BVI: Bcep1808_4738 Bcep1808_5125 Bcep1808_5453
            BUR: Bcep18194_B0510 Bcep18194_B0762 Bcep18194_B1245
                 Bcep18194_B1711 Bcep18194_B2849 Bcep18194_C6892
                 Bcep18194_C7532
            BCN: Bcen_3438 Bcen_3769 Bcen_4788 Bcen_5713
            BCH: Bcen2424_3379 Bcen2424_4599 Bcen2424_4929 Bcen2424_6077
            BAM: Bamb_4029 Bamb_4360 Bamb_6103
            BPS: BPSS0946(penA) BPSS1997(oxa)
            BPM: BURPS1710b_A1106(oxa) BURPS1710b_A2553
            BPL: BURPS1106A_A1301(blaA)
            BPD: BURPS668_A1381(blaA)
            BTE: BTH_II0373(oxa) BTH_II1450
            BPA: BPP2606
            BBR: BB2049
            RFR: Rfer_3580
            POL: Bpro_4226
            AAV: Aave_2552
            AJS: Ajs_2328
            HAR: HEAR0606(blaA) HEAR1185
            NET: Neut_1060
            EBA: ebA3647
            AZO: azo0398 azo0443 azo3682
            DAR: Daro_0083
            MFA: Mfla_2477
            TDN: Tmden_0951
            CJE: Cj0299
            CJR: CJE0344
            CJU: C8J_0276
            CCV: CCV52592_0080 CCV52592_0323
            CHA: CHAB381_0736 CHAB381_1693
            CCO: CCC13826_0310 CCC13826_2205
            ABU: Abu_0558 Abu_1478
            GUR: Gura_3505
            PPD: Ppro_0184
            BBA: Bd3212
            ADE: Adeh_0354
            AFW: Anae109_2056
            MXA: MXAN_5519
            SAT: SYN_01571
            RFE: RF_1275(blaD)
            RBE: RBE_0107(blaD)
            MES: Meso_2215
            PLA: Plav_3016
            SME: SMb21600(ampC) SMc00047(bla) SMc02026
            SMD: Smed_0594 Smed_1460
            ATU: Atu3077(ampC) Atu3376(carB)
            ATC: AGR_L_2891 AGR_L_3464(ampC)
            RET: RHE_CH01220(bla) RHE_CH03194(ampC)
            RLE: RL1352 RL1606 RL3159 pRL110477
            BJA: bll0941(bla) bll5360 blr6230 blr7890
            BRA: BRADO1118 BRADO2167 BRADO2248 BRADO4063 BRADO4627(oxa5)
                 BRADO6967
            BBT: BBta_0565 BBta_2483 BBta_4439 BBta_5028(oxa5) BBta_6931
            RPA: RPA0362(penP)
            RPB: RPB_2340
            RPC: RPC_2728 RPC_3398
            RPD: RPD_0794 RPD_3124
            RPE: RPE_0911 RPE_1865 RPE_3542
            NWI: Nwi_0183 Nwi_0351
            NHA: Nham_0446
            XAU: Xaut_1441
            SIL: SPO2592
            SIT: TM1040_0211
            RSP: RSP_3749(ampC)
            RDE: RD1_0885 RD1_1522
            MMR: Mmar10_0370
            HNE: HNE_0411 HNE_2763
            ZMO: ZMO1967(blaP)
            NAR: Saro_0280
            SAL: Sala_0174
            GBE: GbCGDNIH1_0107 GbCGDNIH1_1173
            RRU: Rru_A0228
            MGM: Mmc1_0424
            ABA: Acid345_1607 Acid345_1709 Acid345_3247 Acid345_4151
            SUS: Acid_2285 Acid_6874
            BSU: BG11016(penP) BG11507(ybxI)
            BAN: BA2507(bla1) BA3500(bla2)
            BAR: GBAA2507(bla1) GBAA3500(bla2)
            BAA: BA_2997
            BAT: BAS2328 BAS3245
            BCE: BC2473 BC3440
            BCA: BCE_2539 BCE_3452(bla2)
            BCZ: BCZK0412(pbpX) BCZK0993(blaI) BCZK2247(bla) BCZK2916(pbp)
                 BCZK3155(bla) BCZK3161 BCZK3208(bla) BCZK3890
                 pE33L466_0098(pbp)
            BTK: BT9727_2291(bla) BT9727_3218(bla)
            BTL: BALH_0439(pbpX) BALH_2254 BALH_3094(bla)
            BLI: BL01642(penP)
            BLD: BLi00280(penP)
            BCL: ABC0264(penP) ABC3481
            BAY: RBAM_011860(blm) RBAM_012080
            BPU: BPUM_0155(ybbE) BPUM_2340
            OIH: OB0667 OB2793 OB3072
            SAU: SAP010(blaZ)
            SAR: SAR1831(blaZ)
            SAS: pSAS19(blaZ)
            SAA: SAUSA300_0959(fmt)
            SAJ: SaurJH9_0030 SaurJH9_2748 SaurJH9_2749
            SAH: SaurJH1_0030 SaurJH1_2825 SaurJH1_2827
            SEP: SE1608
            SER: SEA0003(blaZ-2) SERP1461(blaZ-1)
            SHA: SH1764(blaZ)
            SSP: SSP2186
            LIN: lin0199
            LWE: lwe0137
            LLC: LACR_0015
            LLM: llmg_0018
            SPZ: M5005_Spy_0010
            SPH: MGAS10270_Spy0010
            SPI: MGAS10750_Spy0010
            SPJ: MGAS2096_Spy0010
            SPK: MGAS9429_Spy0010
            SPA: M6_Spy0010
            SPB: M28_Spy0010
            SSA: SSA_1363 SSA_1481
            LPL: lp_0469(bla1) lp_2341(bla2)
            LAC: LBA1639
            LBR: LVIS_2002
            LCA: LSEI_2771
            STH: STH915
            CAC: CAC0190
            CPE: CPE1184
            CPF: CPF_1388
            CPR: CPR_1202
            CKL: CKL_2902(bla)
            MTU: Rv2068c(blaC)
            MTC: MT2128(bla)
            MBO: Mb2094c(blaC)
            MBB: BCG_2087c(blaC)
            MSM: MSMEG_2658 MSMEG_3978 MSMEG_6194
            MUL: MUL_2294(blaC)
            MVA: Mvan_2352
            MGI: Mflv_4021
            MMC: Mmcs_2102
            MKM: Mkms_2148
            MJL: Mjls_2085
            NFA: nfa23080
            RHA: RHA1_ro00175 RHA1_ro00177 RHA1_ro01701 RHA1_ro02713
                 RHA1_ro03541
            SCO: SCO3774(SCH63.21)
            SMA: SAV4452(blaA3)
            LXX: Lxx01020
            CMI: CMM_2676(blaC)
            KRA: Krad_1931
            SEN: SACE_1374(penA) SACE_3056 SACE_4081 SACE_4283(penP)
                 SACE_5313(ampC2)
            STP: Strop_1457
            RXY: Rxyl_1288
            FNU: FN1584
            LIL: LA1549
            LIC: LIC12220(blaR1)
            SYN: slr0121 slr0319(blaOXA-3)
            SYW: SYNW0718
            SYC: syc0060_d(ampC)
            SYF: Synpcc7942_1603
            SYD: Syncc9605_1950
            SYE: Syncc9902_0715
            SYG: sync_0964
            SYR: SynRCC307_0731
            CYA: CYA_0811
            CYB: CYB_1894
            TEL: tll2115
            ANA: all2480 all4822 alr4543
            AVA: Ava_0412 Ava_1408 Ava_2092
            PMA: Pro1145(penP)
            PMT: PMT1133
            PMN: PMN2A_0697
            PMF: P9303_08971(penP)
            PME: NATL1_15311(penP)
            TER: Tery_3876
            BTH: BT_4507
            BFR: BF1250
            BFS: BF1199(cepA)
            CHU: CHU_1887 CHU_3232(ampC)
            FJO: Fjoh_3485
            CCH: Cag_1938
            CPH: Cpha266_1596
            DRA: DR_0433
            DGE: Dgeo_0316
            PTO: PTO0760 PTO1203
            PAB: PAB0087(pbp)
STRUCTURES  PDB: 1A7T  1A8T  1ALQ  1AXB  1BC2  1BLC  1BLH  1BLP  1BLS  1BMC  
                 1BSG  1BT5  1BTL  1BUE  1BUL  1BVT  1BZA  1C3B  1CK3  1DD6  
                 1DDK  1DJA  1DJB  1DJC  1DXK  1DY6  1E25  1E3U  1E4D  1ERM  
                 1ERO  1ERQ  1ESU  1EWZ  1FCM  1FCN  1FCO  1FOF  1FQG  1FR1  
                 1FR6  1FSW  1FSY  1G68  1G6A  1GA0  1GA9  1GCE  1GHI  1GHM  
                 1GHP  1H5X  1H8Y  1H8Z  1HLK  1HTZ  1HZO  1I2S  1I2W  1I5Q  
                 1IEL  1IEM  1IYO  1IYP  1IYQ  1IYS  1JJE  1JJT  1JT1  1JTD  
                 1JTG  1JVJ  1JWP  1JWV  1JWZ  1K07  1K38  1K4E  1K4F  1K54  
                 1K55  1K56  1K57  1K6R  1K6S  1KDS  1KDW  1KE0  1KE3  1KE4  
                 1KGE  1KGF  1KGG  1KO2  1KO3  1KR3  1KVL  1KVM  1L0D  1L0E  
                 1L0F  1L0G  1L2S  1L9Y  1LHY  1LI0  1LI9  1LL5  1LL9  1LLB  
                 1M2X  1M40  1M6K  1MBL  1MQO  1MXO  1MY8  1N4O  1N9B  1NXY  
                 1NY0  1NYM  1NYY  1O07  1O7E  1OME  1ONG  1ONH  1PI4  1PI5  
                 1PIO  1PZO  1PZP  1Q2P  1Q2Q  1RCJ  1RGY  1RGZ  1S6R  1SHV  
                 1SML  1TDG  1TDL  1TEM  1VGN  1VM1  1W7F  1WE4  1WUO  1WUP  
                 1X8G  1X8H  1X8I  1XGI  1XGJ  1XPB  1XX2  1XXM  1Y54  1YLJ  
                 1YLP  1YLT  1YLW  1YLY  1YLZ  1YM1  1YMS  1YMX  1YT4  1ZC2  
                 1ZG4  1ZG6  1ZKJ  1ZNB  2A3U  2A49  2AIO  2B5R  2BC2  2BFK  
                 2BFL  2BFZ  2BG2  2BG6  2BG7  2BG8  2BGA  2BLM  2BLS  2BMI  
                 2CC1  2DOO  2FFY  2FHX  2FM6  2FU6  2FU7  2FU8  2FU9  2G2U  
                 2G2W  2GDN  2GFJ  2GFK  2GKL  2GMN  2H0T  2H0Y  2H10  2H5S  
                 2H6A  2HB9  2HDQ  2HDR  2HDS  2HDU  2HP5  2HP6  2HP9  2HPB  
                 2I72  2JC7  2NXA  2NYP  2NZE  2NZF  2OV5  2P74  2P9V  2Q9M  
                 2Q9N  2QDS  2QDT  2QIN  2QJS  2UYX  2ZNB  3BC2  3BLM  3BLS  
                 3ZNB  4BLM  4ZNB  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.6
            ExPASy - ENZYME nomenclature database: 3.5.2.6
            ExplorEnz - The Enzyme Database: 3.5.2.6
            ERGO genome analysis and discovery system: 3.5.2.6
            BRENDA, the Enzyme Database: 3.5.2.6
            CAS: 9073-60-3
///
ENTRY       EC 3.5.2.7                  Enzyme
NAME        imidazolonepropionase;
            4(5)-imidazolone-5(4)-propionic acid hydrolase;
            imidazolone propionic acid hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate amidohydrolase
REACTION    (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O =
            N-formimidoyl-L-glutamate + H+ [RN:R02288]
ALL_REAC    R02288
SUBSTRATE   (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate;
            H2O [CPD:C00001]
PRODUCT     N-formimidoyl-L-glutamate [CPD:C00439];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Rao, D.R. and Greenberg, D.M.
  TITLE     Studies on the enzymic decomposition of urocanic acid. IV.
            Purification and properties of 4(5)-imidazolone-5(4)-propionic acid
            hydrolase.
  JOURNAL   J. Biol. Chem. 236 (1961) 1758-1763.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   2
  AUTHORS   Snyder, S.H., Silva, O.L. and Kies, M.W.
  TITLE     The mammalian metabolism of L-histidine. IV. Purification and
            properties of imidazolone propionic acid hydrolase.
  JOURNAL   J. Biol. Chem. 236 (1961) 2996-2998.
PATHWAY     PATH: map00340  Histidine metabolism
ORTHOLOGY   KO: K01468  imidazolonepropionase
GENES       HSA: 144193(AMDHD1)
            MMU: 71761(Amdhd1)
            GGA: 417917(AMDHD1)
            XTR: 493273(MGC89894)
            SPU: 592194(LOC592194)
            STY: STY0820(hutI)
            STT: t2100(hutI)
            SPT: SPA1965(hutI)
            SEC: SC0785(hutI)
            STM: STM0787(hutI)
            YPE: YPO1972(hutI)
            YPK: y2340
            YPM: YP_1714(hutI)
            YPA: YPA_1354
            YPN: YPN_1452
            YPP: YPDSF_1151
            YPS: YPTB1966(hutI)
            YPI: YpsIP31758_2113(hutI)
            PLU: plu3197(hutI)
            ENT: Ent638_1260
            SPE: Spro_2077
            XCC: XCC1581(hutI)
            XCB: XC_2653
            XCV: XCV1679(hutI)
            XAC: XAC1638(hutI)
            XOO: XOO2396(hutI)
            XOM: XOO_2277(XOO2277)
            VCH: VC1205
            VCO: VC0395_A0825(hutI)
            VVU: VV1_2392
            VVY: VV1949
            VPA: VP1276
            VFI: VFA0453
            PPR: PBPRA2170
            PAE: PA5092(hutI)
            PAU: PA14_67250(hutI)
            PAP: PSPA7_5826(hutI)
            PPU: PP_5030(hutI)
            PPF: Pput_4904
            PST: PSPTO_5277(hutI)
            PSB: Psyr_4835
            PSP: PSPPH_4867(hutI)
            PFL: PFL_0409(hutI)
            PFO: Pfl_0367
            PEN: PSEEN5094(hutI)
            PMY: Pmen_4073
            PCR: Pcryo_1934
            PRW: PsycPRwf_0848
            SON: SO_0095(hutI)
            SDN: Sden_0081
            SFR: Sfri_3955
            SAZ: Sama_0080
            SBL: Sbal_4254
            SBM: Shew185_0095
            SLO: Shew_3759
            SPC: Sputcn32_0077
            SSE: Ssed_4449
            SPL: Spea_4171
            SHE: Shewmr4_0097
            SHM: Shewmr7_0092
            SHN: Shewana3_0098
            SHW: Sputw3181_4000
            ILO: IL2453
            CPS: CPS_0911(hutI)
            PHA: PSHAa2737(hutI)
            PAT: Patl_1019
            PIN: Ping_1032
            LPN: lpg0711(hutI)
            LPF: lpl0748(hutI)
            LPP: lpp0766(hutI)
            HCH: HCH_04169(hutI)
            MMW: Mmwyl1_3900
            AHA: AHA_0377(hutI)
            CVI: CV_0321(hutI)
            RSO: RSc2644(hutI)
            REU: Reut_A2713
            REH: H16_A3015(hutI)
            RME: Rmet_2852
            BMA: BMA0649(hutI)
            BMV: BMASAVP1_A2362(hutI)
            BML: BMA10299_A2923(hutI)
            BMN: BMA10247_1677(hutI)
            BXE: Bxe_A2943
            BVI: Bcep1808_2243
            BUR: Bcep18194_A5478
            BCN: Bcen_5909
            BCH: Bcen2424_2168
            BAM: Bamb_2207
            BPS: BPSL2340
            BPM: BURPS1710b_2792(hutI)
            BPL: BURPS1106A_2719(hutI)
            BPD: BURPS668_2663(hutI)
            BTE: BTH_I1824(hutI)
            POL: Bpro_1035
            VEI: Veis_3648
            EBA: ebA5740(hutI)
            BBA: Bd2721(hutI)
            DPS: DP2351
            ADE: Adeh_1507
            AFW: Anae109_2316
            MXA: MXAN_4345(hutI)
            SFU: Sfum_2377
            MLO: mlr8319 mlr9376
            MES: Meso_2986
            SME: SMb21166(hutI)
            SMD: Smed_4659
            ATU: Atu3934(hutI)
            ATC: AGR_L_1824
            RET: RHE_PE00073(hutI)
            RLE: pRL110206(hutI)
            BME: BMEII0368
            BMF: BAB2_0306
            BMS: BRA0929(hutI)
            BMB: BruAb2_0304(hutI)
            BOV: BOV_A0871(hutI)
            OAN: Oant_1436
            BJA: bll6243(hutI)
            BRA: BRADO1544 BRADO1603(hutI)
            BBT: BBta_6452(hutI)
            CCR: CC_0960
            SIL: SPO2191(hutI)
            SIT: TM1040_3004
            RSP: RSP_2934(hutI)
            RSH: Rsph17029_1578
            RDE: RD1_3677(hutI)
            PDE: Pden_0710
            MMR: Mmar10_1604
            HNE: HNE_2395(hutI)
            SAL: Sala_1688
            SWI: Swit_4633
            GOX: GOX1163
            ACR: Acry_1746
            RRU: Rru_A1303
            ABA: Acid345_1049
            SUS: Acid_4089 Acid_5207
            BSU: BG11100(hutI)
            BHA: BH1984(hutI)
            BAN: BA3710(hutI)
            BAR: GBAA3710(hutI)
            BAA: BA_4193
            BAT: BAS3440
            BCE: BC3650
            BCA: BCE_3678(hutI)
            BCZ: BCZK0424(hutI) BCZK3352(hutI)
            BCY: Bcer98_2310
            BTK: BT9727_3403(hutI)
            BTL: BALH_0450(hutI) BALH_3285(hutI)
            BCL: ABC3329(hutI)
            BAY: RBAM_036430(hutI)
            GKA: GK1368
            SAU: SA2121(hutI)
            SAV: SAV2330(hutI)
            SAM: MW2251(hutI)
            SAR: SAR2416(hutI)
            SAS: SAS2223
            SAC: SACOL2323(hutI)
            SAB: SAB2207c(hutI)
            SAA: SAUSA300_2277(hutI)
            SAO: SAOUHSC_02606
            SAJ: SaurJH9_2355
            SAH: SaurJH1_2398
            SSP: SSP0573
            SPY: SPy_2081(hutI)
            SPZ: M5005_Spy_1770(hutI)
            SPM: spyM18_2139(hutI)
            SPG: SpyM3_1772(hutI)
            SPS: SPs1769
            SPH: MGAS10270_Spy1836(hutI)
            SPI: MGAS10750_Spy1862(hutI)
            SPJ: MGAS2096_Spy1803(hutI)
            SPK: MGAS9429_Spy1780(hutI)
            SPF: SpyM51728(hutI)
            SPA: M6_Spy1767
            SPB: M28_Spy1754(hutI)
            SSA: SSA_0436(hutI)
            SGO: SGO_1804(hutI)
            CTC: CTC02320
            AMT: Amet_3148
            TTE: TTE0451(hutI)
            MSM: MSMEG_1182(hutI)
            NFA: nfa12340(hutI)
            RHA: RHA1_ro04641(hutI)
            SCO: SCO3070(SCE25.11c)
            SMA: SAV3493(hutI)
            ART: Arth_1313
            AAU: AAur_1464(hutI)
            PAC: PPA2169
            NCA: Noca_4385
            TFU: Tfu_0821
            FAL: FRAAL4929
            KRA: Krad_4450
            SEN: SACE_6403(hutI)
            STP: Strop_1107
            RXY: Rxyl_0585
            FNU: FN0740 FN1404
            TDE: TDE0047(hutI)
            BTH: BT_2692
            BFR: BF4146
            BFS: BF3968(hutI)
            PGI: PG0328(hutI)
            GFO: GFO_0758(hutI)
            FJO: Fjoh_4570
            FPS: FP1780(hutI)
            DRA: DR_A0148
            DGE: Dgeo_2731
            TME: Tmel_0211
            FNO: Fnod_1527
            HAL: VNG1211G(hutI)
            HMA: rrnAC1790(hutI)
            TAC: Ta0238
            TVO: TVN1357
            PTO: PTO0105
            PAS: Pars_1483
STRUCTURES  PDB: 2BB0  2G3F  2GOK  2OOF  2PUZ  2Q09  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.7
            ExPASy - ENZYME nomenclature database: 3.5.2.7
            ExplorEnz - The Enzyme Database: 3.5.2.7
            ERGO genome analysis and discovery system: 3.5.2.7
            BRENDA, the Enzyme Database: 3.5.2.7
            CAS: 9024-91-3
///
ENTRY       EC 3.5.2.8        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
COMMENT     Deleted entry: cephalosporinase. Now included with EC 3.5.2.6
            beta-lactamase (EC 3.5.2.8 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.8
            ExPASy - ENZYME nomenclature database: 3.5.2.8
            ExplorEnz - The Enzyme Database: 3.5.2.8
            ERGO genome analysis and discovery system: 3.5.2.8
            BRENDA, the Enzyme Database: 3.5.2.8
///
ENTRY       EC 3.5.2.9                  Enzyme
NAME        5-oxoprolinase (ATP-hydrolysing);
            pyroglutamase (ATP-hydrolysing);
            oxoprolinase;
            pyroglutamase;
            5-oxoprolinase;
            pyroglutamate hydrolase;
            pyroglutamic hydrolase;
            L-pyroglutamate hydrolase;
            5-oxo-L-prolinase;
            pyroglutamase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     5-oxo-L-proline amidohydrolase (ATP-hydrolysing)
REACTION    ATP + 5-oxo-L-proline + 2 H2O = ADP + phosphate + L-glutamate
            [RN:R07304]
ALL_REAC    R07304;
            (other) R00251
SUBSTRATE   ATP [CPD:C00002];
            5-oxo-L-proline [CPD:C02238];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            L-glutamate [CPD:C00025]
REFERENCE   1  [PMID:5289242]
  AUTHORS   Van der Werf P, Orlowski M, Meister A.
  TITLE     Enzymatic conversion of 5-oxo-L-proline (L-pyrrolidone carboxylate)
            to L-glutamate coupled with cleavage of adenosine triphosphate to
            adenosine diphosphate, a reaction in the  -glutamyl cycle.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 68 (1971) 2982-5.
  ORGANISM  pig [GN:ssc], sheep, human
PATHWAY     PATH: map00480  Glutathione metabolism
ORTHOLOGY   KO: K01469  5-oxoprolinase (ATP-hydrolysing)
GENES       HSA: 26873(OPLAH)
            PTR: 472891(OPLAH)
            MMU: 75475(Oplah)
            RNO: 116684(Oplah)
            CFA: 482085(LOC482085)
            BTA: 408006(5-OPase)
            SPU: 589767(LOC589767)
            ATH: AT5G37830
            CME: CMP112C
            PIC: PICST_29736(HYU1.2) PICST_81320(HYU1.1) PICST_86944(HYU1.3)
            CGR: CAGL0K00231g
            ANI: AN3972.2
            AFM: AFUA_6G14330
            AOR: AO090103000443
            DDI: DDBDRAFT_0186276
            TET: TTHERM_00006150
            TCR: 509803.40
            LMA: LmjF18.1040
            PPF: Pput_2260
            PAT: Patl_3814
            NOC: Noc_0378
            AEH: Mlg_1104 Mlg_2644
            HHA: Hhal_0734
            HCH: HCH_06431
            REU: Reut_B5473 Reut_B5474 Reut_C6223 Reut_C6263 Reut_C6264
            BXE: Bxe_C0004
            BVI: Bcep1808_4031
            BUR: Bcep18194_B1204 Bcep18194_B1206 Bcep18194_B2574
                 Bcep18194_B3096 Bcep18194_B3097
            BCH: Bcen2424_3552
            BAM: Bamb_5284
            BPE: BP1895(oplaH)
            BPA: BPP3012(oplaH)
            BBR: BB2978(oplaH)
            POL: Bpro_1781
            PNA: Pnap_1163 Pnap_1165 Pnap_1517
            AAV: Aave_3295
            AJS: Ajs_2480
            VEI: Veis_1519 Veis_1520 Veis_1833 Veis_1912 Veis_1913 Veis_2907
            MPT: Mpe_A2968
            NIS: NIS_1772
            SUN: SUN_0861 SUN_0878
            GUR: Gura_4360 Gura_4362
            MLO: mlr1573
            MES: Meso_2020
            PLA: Plav_1151 Plav_2407
            SME: SMb20023
            SMD: Smed_3306 Smed_3307 Smed_3663 Smed_3664 Smed_3717 Smed_4106
            RLE: pRL120412(hyuB)
            BME: BMEII0602
            BMF: BAB2_0559
            BMS: BRA0681
            BMB: BruAb2_0548
            OAN: Oant_3807 Oant_4581 Oant_4582
            BRA: BRADO3229
            BBT: BBta_4926
            RPB: RPB_4428 RPB_4429
            RPD: RPD_2367 RPD_2368
            RPE: RPE_3216 RPE_3217
            XAU: Xaut_3509
            CCR: CC_2369
            RSH: Rsph17029_2292 Rsph17029_2293
            JAN: Jann_2566 Jann_3764 Jann_3765 Jann_3811 Jann_3812
            PDE: Pden_0472 Pden_4352 Pden_4353 Pden_4408 Pden_4409 Pden_4973
                 Pden_4974
            MMR: Mmar10_2093
            NAR: Saro_0175 Saro_0176
            SWI: Swit_0475 Swit_0476 Swit_1718 Swit_1719 Swit_2035 Swit_2083
                 Swit_2084 Swit_3075 Swit_3648 Swit_3649 Swit_4143 Swit_4144
                 Swit_4225 Swit_4226 Swit_4343
            MGM: Mmc1_1513
            ABA: Acid345_2039 Acid345_3921
            DRM: Dred_1559 Dred_1560
            MTA: Moth_1966 Moth_1967
            MTU: Rv0266c(oplA)
            MBO: Mb0272c(oplA)
            MBB: BCG_0304c(oplA)
            MVA: Mvan_4898
            MMC: Mmcs_5242 Mmcs_5243
            MKM: Mkms_5330
            MJL: Mjls_5621 Mjls_5622
            RHA: RHA1_ro10160
            SMA: SAV6961
            ART: Arth_3641 Arth_3642
            NCA: Noca_0079 Noca_0080 Noca_1496
            FRA: Francci3_2239 Francci3_2507
            RXY: Rxyl_1695 Rxyl_1696 Rxyl_1848 Rxyl_2410 Rxyl_2411
            RBA: RB8038(OPLAH)
            SYN: slr0697
            SYF: Synpcc7942_2390
            SYD: Syncc9605_1599
            SYE: Syncc9902_1358
            SYG: sync_2245(oplaH)
            SYR: SynRCC307_1836
            SYX: SynWH7803_1973
            CYB: CYB_0961
            ANA: all4969 all4970
            AVA: Ava_2245 Ava_2246
            PMF: P9303_20111
            TER: Tery_1019
            SRU: SRU_0177
            PLT: Plut_0999
            RRS: RoseRS_2091 RoseRS_2708 RoseRS_4325
            RCA: Rcas_1778 Rcas_1968 Rcas_3492 Rcas_3493 Rcas_4426
            MAC: MA2300(oplAH)
            MBA: Mbar_A3345
            MMA: MM_2912
            MBU: Mbur_2177
            IHO: Igni_0292
            MSE: Msed_1127 Msed_1128
            PIS: Pisl_0131 Pisl_0132
            PCL: Pcal_0424 Pcal_0425
            PAS: Pars_0413 Pars_0414
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.9
            ExPASy - ENZYME nomenclature database: 3.5.2.9
            ExplorEnz - The Enzyme Database: 3.5.2.9
            ERGO genome analysis and discovery system: 3.5.2.9
            BRENDA, the Enzyme Database: 3.5.2.9
            CAS: 9075-46-1
///
ENTRY       EC 3.5.2.10                 Enzyme
NAME        creatininase;
            creatinine hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     creatinine amidohydrolase
REACTION    creatinine + H2O = creatine [RN:R01884]
ALL_REAC    R01884
SUBSTRATE   creatinine [CPD:C00791];
            H2O [CPD:C00001]
PRODUCT     creatine [CPD:C00300]
REFERENCE   1
  AUTHORS   Tsuru, D., Oka, I. and Yoshimoto, T.
  TITLE     Creatinine decomposing enzymes in Pseudomonas putida.
  JOURNAL   Agric. Biol. Chem. 40 (1976) 1011-1018.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K01470  creatinine amidohydrolase
GENES       PLU: plu3916
            TCX: Tcr_1799
            CSA: Csal_1171
            REH: H16_A1736
            BCH: Bcen2424_3253
            RFR: Rfer_3746
            POL: Bpro_4255
            DAR: Daro_0078
            GSU: GSU1722
            PCA: Pcar_1641
            MLO: mlr1298
            MES: Meso_2844
            SME: SMc02977
            ATU: Atu4503
            ATC: AGR_L_731
            RET: RHE_CH02048(ypch00659) RHE_CH03624(ypch01280)
            RLE: RL4147 pRL120303
            BME: BMEII0309
            BMF: BAB2_0247
            BMS: BRA0986
            BMB: BruAb2_0248
            BJA: blr0092
            RPA: RPA0471
            RPB: RPB_0569
            RPC: RPC_0569
            RPD: RPD_0261
            RPE: RPE_0109
            NWI: Nwi_0330
            NHA: Nham_0424
            BHE: BH12970
            BQU: BQ10260
            BBK: BARBAKC583_1108
            SIT: TM1040_3053
            JAN: Jann_1478
            RDE: RD1_0537
            HNE: HNE_3508
            GBE: GbCGDNIH1_0830
            ABA: Acid345_1632
            BHA: BH0226
            LMO: lmo2647
            LMF: LMOf2365_2619
            LIN: lin2796
            LWE: lwe2596
            CPE: CPE0757
            CPF: CPF_0751
            CPR: CPR_0738
            CTC: CTC01884
            DSY: DSY0967
            MAV: MAV_4476
            MSM: MSMEG_1425
            MMC: Mmcs_0866
            AAU: AAur_pTC20179
            FAL: FRAAL4257
            BLO: BL0014
            RXY: Rxyl_0459 Rxyl_3038 Rxyl_3150
            SYN: slr0596
            SYW: SYNW1739
            SYC: syc0049_d
            SYF: Synpcc7942_1592
            SYD: Syncc9605_0727
            SYE: Syncc9902_1636
            SYG: sync_0338 sync_1991
            SYR: SynRCC307_1587
            SYX: SynWH7803_0653
            CYA: CYA_1538
            CYB: CYB_1420
            ANA: alr1374
            AVA: Ava_4012
            PMA: Pro0531
            PMM: PMM0531
            PMT: PMT1232
            PMN: PMN2A_1862
            PMI: PMT9312_0531
            PMB: A9601_05871
            PMC: P9515_05951
            PMF: P9303_07781
            PMG: P9301_05571
            PME: NATL1_05871
            TER: Tery_0217
            TMA: TM0413
            HMA: pNG7096(camH1) pNG7341(camH2) rrnAC0223(camH3)
            HWA: HQ1805A(cre)
            NPH: NP2120A
STRUCTURES  PDB: 1J2T  1J2U  1Q3K  1V7Z  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.10
            ExPASy - ENZYME nomenclature database: 3.5.2.10
            ExplorEnz - The Enzyme Database: 3.5.2.10
            ERGO genome analysis and discovery system: 3.5.2.10
            BRENDA, the Enzyme Database: 3.5.2.10
            CAS: 9025-13-2
///
ENTRY       EC 3.5.2.11                 Enzyme
NAME        L-lysine-lactamase;
            L-alpha-aminocaprolactam hydrolase;
            L-lysinamidase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     L-lysine-1,6-lactam lactamhydrolase
REACTION    L-lysine 1,6-lactam + H2O = L-lysine [RN:R00463]
ALL_REAC    R00463
SUBSTRATE   L-lysine 1,6-lactam [CPD:C02837];
            H2O [CPD:C00001]
PRODUCT     L-lysine [CPD:C00047]
COMMENT     Also hydrolyses L-lysinamide.
REFERENCE   1  [PMID:26602]
  AUTHORS   Fukumura T, Talbot G, Misono H, Teramura Y, Kato K, Soda K.
  TITLE     Purification and properties of a novel enzyme,
            L-alpha-amino-epsilon-caprolactamase from Cryptococcus laurentii.
  JOURNAL   FEBS. Lett. 89 (1978) 298-300.
  ORGANISM  Cryptococcus laurentii
REFERENCE   2
  AUTHORS   Shvyadas, V.K., Galaev, I.Yu. and Kozlova, E.V.
  TITLE     Preparation and characterization of L-alpha-aminocaprolactam
            hydrolase from cells of Cryptococcus laurentii.
  JOURNAL   Biochemistry (Moscow) 49 (1984) 1268-1273.
  ORGANISM  Cryptococcus laurentii
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.11
            ExPASy - ENZYME nomenclature database: 3.5.2.11
            ExplorEnz - The Enzyme Database: 3.5.2.11
            ERGO genome analysis and discovery system: 3.5.2.11
            BRENDA, the Enzyme Database: 3.5.2.11
            CAS: 52652-61-6
///
ENTRY       EC 3.5.2.12                 Enzyme
NAME        6-aminohexanoate-cyclic-dimer hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     1,8-diazacyclotetradecane-2,9-dione lactamhydrolase
REACTION    1,8-diazacyclotetradecane-2,9-dione + H2O =
            N-(6-aminohexanoyl)-6-aminohexanoate [RN:R03448]
ALL_REAC    R03448
SUBSTRATE   1,8-diazacyclotetradecane-2,9-dione [CPD:C04277];
            H2O [CPD:C00001]
PRODUCT     N-(6-aminohexanoyl)-6-aminohexanoate [CPD:C01255]
COMMENT     The cyclic dimer of 6-aminohexanoate is converted to the linear
            dimer.
REFERENCE   1  [PMID:923591]
  AUTHORS   Kinoshita S, Negoro S, Muramatsu M, Bisaria VS, Sawada S, Okada H.
  TITLE     6-Aminohexanoic acid cyclic dimer hydrolase. A new cyclic amide
            hydrolase produced by Achromobacter guttatus KI74.
  JOURNAL   Eur. J. Biochem. 80 (1977) 489-95.
  ORGANISM  Achromobacter guttatus
ORTHOLOGY   KO: K01471  
GENES       PST: PSPTO_4526
            HCH: HCH_06624
            BMA: BMA2839(nylA)
            BMV: BMASAVP1_A3414(nylA)
            BML: BMA10299_A1704(nylA)
            BMN: BMA10247_3137(nylA)
            BXE: Bxe_A4331
            BPS: BPSL3287
            BPM: BURPS1710b_0054(nylA)
            BTE: BTH_I3161
            DDE: Dde_0518
            MXA: MXAN_6372(nylA)
            MLO: mlr4825
            BJA: blr7282(amiC)
            RPA: RPA2974 RPA3959
            CCR: CC_1323
            SIL: SPO2527(nylA)
            RSP: RSP_2401
            HNE: HNE_1322
            BLD: BLi00325
            BCL: ABC2593
            SMU: SMU.1218(nylA)
            MPA: MAP0581c
            MSM: MSMEG_3505 MSMEG_6673
            NFA: nfa18760 nfa28320
            SCO: SCO7601(SC7H9.13c)
            DRA: DR_0235
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.12
            ExPASy - ENZYME nomenclature database: 3.5.2.12
            ExplorEnz - The Enzyme Database: 3.5.2.12
            ERGO genome analysis and discovery system: 3.5.2.12
            UM-BBD (Biocatalysis/Biodegradation Database): 3.5.2.12
            BRENDA, the Enzyme Database: 3.5.2.12
            CAS: 60976-29-6
///
ENTRY       EC 3.5.2.13                 Enzyme
NAME        2,5-dioxopiperazine hydrolase;
            cyclo(Gly-Gly) hydrolase;
            cyclo(glycylglycine) hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     2,5-dioxopiperazine amidohydrolase
REACTION    2,5-dioxopiperazine + H2O = glycylglycine [RN:R03810]
ALL_REAC    R03810
SUBSTRATE   2,5-dioxopiperazine [CPD:C02777];
            H2O [CPD:C00001]
PRODUCT     glycylglycine [CPD:C02037]
COMMENT     Highly specific; does not hydrolyse other dioxopiperazines,
            glycylglycine, proteins or barbiturates.
REFERENCE   1
  AUTHORS   Suzuki, Y. and Uchida, K.
  TITLE     Multiple forms of alpha-glycosidase from pig duodenum.
  JOURNAL   Agric. Biol. Chem. 49 (1985) 1573-1581.
  ORGANISM  pig [GN:ssc]
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.13
            ExPASy - ENZYME nomenclature database: 3.5.2.13
            ExplorEnz - The Enzyme Database: 3.5.2.13
            ERGO genome analysis and discovery system: 3.5.2.13
            BRENDA, the Enzyme Database: 3.5.2.13
            CAS: 97599-45-6
///
ENTRY       EC 3.5.2.14                 Enzyme
NAME        N-methylhydantoinase (ATP-hydrolysing);
            N-methylhydantoin amidohydrolase;
            methylhydantoin amidase;
            N-methylhydantoin hydrolase;
            N-methylhydantoinase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     N-methylimidazolidine-2,4-dione amidohydrolase (ATP-hydrolysing)
REACTION    ATP + N-methylimidazolidine-2,4-dione + 2 H2O = ADP + phosphate +
            N-carbamoylsarcosine [RN:R03187]
ALL_REAC    R03187
SUBSTRATE   ATP [CPD:C00002];
            N-methylimidazolidine-2,4-dione [CPD:C02565];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            N-carbamoylsarcosine [CPD:C01043]
REFERENCE   1  [PMID:3827889]
  AUTHORS   Kim JM, Shimizu S, Yamada H.
  TITLE     Amidohydrolysis of N-methylhydantoin coupled with ATP hydrolysis.
  JOURNAL   Biochem. Biophys. Res. Commun. 142 (1987) 1006-12.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K01472  N-methylhydantoinase
            KO: K01473  N-methylhydantoinase A
            KO: K01474  N-methylhydantoinase B
GENES       PPU: PP_3514(hyuB) PP_3515(hyuA)
            PFL: PFL_2732 PFL_2733
            PAR: Psyc_1451
            PCR: Pcryo_1375
            ABO: ABO_0720(hyuB) ABO_2584(hyuA)
            REU: Reut_C6172
            RME: Rmet_4105
            BXE: Bxe_A1473 Bxe_A1474 Bxe_B0371 Bxe_B0372 Bxe_B2497 Bxe_C0790
                 Bxe_C0791 Bxe_C1059 Bxe_C1060
            BPE: BP0753(hyuA) BP0754(hyuB) BP0821(hyuB) BP0822(hyuA)
            BPA: BPP0316(hyuB) BPP3170 BPP3408(hyuA)
            BBR: BB0318(hyuA) BB0319(hyuB) BB3571 BB3858(hyuA) BB3859(hyuB)
            MMS: mma_0844(hyuA)
            EBA: ebA2051(hyuA) ebA2053(hyuB)
            HPA: HPAG1_0680 HPAG1_0681
            HAC: Hac_0951(hyuA)
            PCA: Pcar_3103 Pcar_3104
            BBA: Bd1059(hyuB) Bd1060(hyuA)
            MLO: mlr1573 mlr4786 mlr4788 mlr7024 mlr7025 mlr9030 mlr9031
            MES: Meso_2020
            SME: SMb20023
            ATU: Atu6022(hyuA) Atu6023(hyuB)
            ATC: AGR_pTi_62(hyuA) AGR_pTi_63(hyuB)
            RET: RHE_PE00300(ype00153)
            RLE: pRL120411(hyuA)
            BME: BMEII0602
            BMF: BAB2_0559
            BMS: BRA0681
            BMB: BruAb2_0548
            BJA: blr3326 blr3327 blr3621
            BRA: BRADO3230 BRADO5506(hyuA) BRADO5507(hyuB)
            BBT: BBta_4925 BBta_5988(hyuA) BBta_5989(hyuB)
            CCR: CC_2369
            SIL: SPO1472(hyuA) SPO1473
            RSP: RSP_0639 RSP_0640
            RDE: RD1_3584(hyuA) RD1_3585
            GOX: GOX0216 GOX0217
            BLI: BL00460 BL00462 BL01720 BL01721
            BLD: BLi00395 BLi00396 BLi01982 BLi01983 BLi01984
            GKA: GK2893 GK2894
            MSM: MSMEG_3973
            NFA: nfa21940
            RHA: RHA1_ro00479(hyuA) RHA1_ro00480(hyuB)
            SMA: SAV6961
            FRA: Francci3_2509
            GVI: gll1226 gll2098
            AAE: aq_1925(hyuB) aq_708(hyuA)
            MJA: MJ0963(hyuB) MJ0964(hyuA)
            MMA: MM_0068
            MKA: MK1048(hyuB) MK1091(hyuA_1)
            HMA: pNG7164(hyuA) pNG7165(hyuB)
            HWA: HQ2241A(hyuB) HQ2242A(hyuA)
            NPH: NP2952A(hyuB_1) NP2954A(hyuA_1) NP6216A(hyuB_2)
                 NP6218A(hyuA_2)
            TVO: TVN0811 TVN0812
            PTO: PTO0461 PTO0462
            APE: APE_1328.1 APE_1331 APE_2528.1 APE_2530.1
            SSO: SSO1662(huyB-1) SSO1663(huyA-1) SSO2008(huyA-2)
                 SSO2010(hyuB-2) SSO2934(hyuB-3) SSO2936(hyuA-3)
            STO: ST1685 ST1686
            SAI: Saci_0368(oplA) Saci_0369(oplA) Saci_2041(huyA) Saci_2042
            PAI: PAE2028(hyuB) PAE2030(hyuA)
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.14
            ExPASy - ENZYME nomenclature database: 3.5.2.14
            ExplorEnz - The Enzyme Database: 3.5.2.14
            ERGO genome analysis and discovery system: 3.5.2.14
            BRENDA, the Enzyme Database: 3.5.2.14
            CAS: 100785-00-0
///
ENTRY       EC 3.5.2.15                 Enzyme
NAME        cyanuric acid amidohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     cyanuric acid amidohydrolase
REACTION    cyanuric acid + H2O = biuret + CO2 [RN:R07305]
ALL_REAC    R07305;
            (other) R05561
SUBSTRATE   cyanuric acid [CPD:C06554];
            H2O [CPD:C00001]
PRODUCT     biuret [CPD:C06555];
            CO2 [CPD:C00011]
COMMENT     Involved in a pathway by which the herbicide atrazine,
            2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, is
            degraded in bacteria.
REFERENCE   1  [PMID:1991731]
  AUTHORS   Eaton RW, Karns JS.
  TITLE     Cloning and comparison of the DNA encoding ammelide aminohydrolase
            and cyanuric acid amidohydrolase from three s-triazine-degrading
            bacterial strains.
  JOURNAL   J. Bacteriol. 173 (1991) 1363-6.
  ORGANISM  Pseudomonas sp., Klebsiella pneumoniae
REFERENCE   2  [PMID:1846859]
  AUTHORS   Eaton RW, Karns JS.
  TITLE     Cloning and analysis of s-triazine catabolic genes from Pseudomonas
            sp. strain NRRLB-12227.
  JOURNAL   J. Bacteriol. 173 (1991) 1215-22.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00791  Atrazine degradation
ORTHOLOGY   KO: K03383  cyanuric acid amidohydrolase
GENES       RLE: pRL100353(atzD)
            BJA: blr7281(atzD)
            BRA: BRADO6319(atzD)
            BBT: BBta_1315(atzD)
            MTA: Moth_2120
            RHA: RHA1_ro05296
            NCA: Noca_1505 Noca_4270
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.15
            ExPASy - ENZYME nomenclature database: 3.5.2.15
            ExplorEnz - The Enzyme Database: 3.5.2.15
            ERGO genome analysis and discovery system: 3.5.2.15
            UM-BBD (Biocatalysis/Biodegradation Database): 3.5.2.15
            BRENDA, the Enzyme Database: 3.5.2.15
            CAS: 100785-00-0
///
ENTRY       EC 3.5.2.16                 Enzyme
NAME        maleimide hydrolase;
            imidase;
            cyclic imide hydrolase;
            cyclic-imide amidohydrolase (decyclicizing) [misprint]
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     cyclic-imide amidohydrolase (decyclizing)
REACTION    maleimide + H2O = maleamic acid [RN:R05781]
ALL_REAC    R05781
SUBSTRATE   maleimide [CPD:C07272];
            H2O [CPD:C00001]
PRODUCT     maleamic acid [CPD:C01596]
REFERENCE   1  [PMID:9030755]
  AUTHORS   Ogawa J, Soong CL, Honda M, Shimizu S.
  TITLE     Imidase, a dihydropyrimidinase-like enzyme involved in the
            metabolism of cyclic imides.
  JOURNAL   Eur. J. Biochem. 243 (1997) 322-7.
  ORGANISM  Blastobacter sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.16
            ExPASy - ENZYME nomenclature database: 3.5.2.16
            ExplorEnz - The Enzyme Database: 3.5.2.16
            ERGO genome analysis and discovery system: 3.5.2.16
            BRENDA, the Enzyme Database: 3.5.2.16
///
ENTRY       EC 3.5.2.17                 Enzyme
NAME        hydroxyisourate hydrolase;
            HIUHase;
            5-hydroxyisourate hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     5-hydroxyisourate amidohydrolase
REACTION    5-hydroxyisourate + H2O =
            5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
            [RN:R06601]
ALL_REAC    R06601
SUBSTRATE   5-hydroxyisourate [CPD:C11821];
            H2O [CPD:C00001]
PRODUCT     5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
            [CPD:C12248]
COMMENT     The reaction is the first stage in the conversion of
            5-hydroxyisourate into S-allantoin. This reaction will also occur
            spontaneously but more slowly.
REFERENCE   1  [PMID:12779339]
  AUTHORS   Raychaudhuri A, Tipton PA.
  TITLE     A familiar motif in a new context: the catalytic mechanism of
            hydroxyisourate hydrolase.
  JOURNAL   Biochemistry. 42 (2003) 6848-52.
  ORGANISM  Glycine max [GN:egma]
REFERENCE   2  [PMID:12481089]
  AUTHORS   Raychaudhuri A, Tipton PA.
  TITLE     Cloning and expression of the gene for soybean hydroxyisourate
            hydrolase. Localization and implications for function and mechanism.
  JOURNAL   Plant. Physiol. 130 (2002) 2061-8.
  ORGANISM  Glycine max [GN:egma]
REFERENCE   3  [PMID:10567345]
  AUTHORS   Sarma AD, Serfozo P, Kahn K, Tipton PA.
  TITLE     Identification and purification of hydroxyisourate hydrolase, a
            novel ureide-metabolizing enzyme.
  JOURNAL   J. Biol. Chem. 274 (1999) 33863-5.
  ORGANISM  Glycine max [GN:egma]
PATHWAY     PATH: map00230  Purine metabolism
GENES       PAP: PSPA7_3816(uraH)
            BPL: BURPS1106A_2425(uraH)
            BPD: BURPS668_2383(uraH)
            BOV: BOV_0511(uraH)
STRUCTURES  PDB: 2H1X  2H6U  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.17
            ExPASy - ENZYME nomenclature database: 3.5.2.17
            ExplorEnz - The Enzyme Database: 3.5.2.17
            ERGO genome analysis and discovery system: 3.5.2.17
            BRENDA, the Enzyme Database: 3.5.2.17
///
ENTRY       EC 3.5.2.18                 Enzyme
NAME        enamidase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
SYSNAME     6-oxo-1,4,5,6-tetrahydronicotinate amidohydrolase
REACTION    6-oxo-1,4,5,6-tetrahydronicotinate + 2 H2O = 2-formylglutarate + NH3
            [RN:R07984]
ALL_REAC    R07984
SUBSTRATE   6-oxo-1,4,5,6-tetrahydronicotinate [CPD:C04226];
            H2O [CPD:C00001]
PRODUCT     2-formylglutarate [CPD:C16159];
            NH3 [CPD:C00014]
COMMENT     Contains iron and Zn2+. Forms part of the nicotinate-fermentation
            catabolism pathway in Eubacterium barkeri. Other enzymes involved in
            this pathway are EC 1.17.1.5 (nicotinate dehydrogenase), EC 1.3.7.1
            (6-hydroxynicotinate reductase), EC 1.1.1.291
            (2-hydroxymethylglutarate dehydrogenase), EC 5.4.99.4
            (2-methyleneglutarate mutase), EC 5.3.3.6 (methylitaconate
            Delta-isomerase), EC 4.2.1.85 (dimethylmaleate hydratase) and EC
            4.1.3.32 (2,3-dimethylmalate lyase).
REFERENCE   1  [PMID:16894175]
  AUTHORS   Alhapel A, Darley DJ, Wagener N, Eckel E, Elsner N, Pierik AJ.
  TITLE     Molecular and functional analysis of nicotinate catabolism in
            Eubacterium barkeri.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 12341-6.
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.2.18
            ExPASy - ENZYME nomenclature database: 3.5.2.18
            ExplorEnz - The Enzyme Database: 3.5.2.18
            ERGO genome analysis and discovery system: 3.5.2.18
            BRENDA, the Enzyme Database: 3.5.2.18
///
ENTRY       EC 3.5.2.-                  Enzyme
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amides
REACTION    (1) Xanthine + H2O <=> 5-Ureido-4-imidazole carboxylate [RN:R02141];
            (2) N-Formiminoglycine <=> Imidazolone + H2O [RN:R04026];
            (3) N-Formimino-L-aspartate <=> 4-Imidazolone-5-acetate + H2O
            [RN:R04214];
            (4) epsilon-Caprolactam + H2O <=> 6-Aminohexanoate [RN:R05356]
SUBSTRATE   Xanthine [CPD:C00385];
            H2O [CPD:C00001];
            N-Formiminoglycine [CPD:C02718];
            N-Formimino-L-aspartate [CPD:C03409];
            epsilon-Caprolactam [CPD:C06593]
PRODUCT     5-Ureido-4-imidazole carboxylate [CPD:C05515];
            Imidazolone [CPD:C06195];
            H2O [CPD:C00001];
            4-Imidazolone-5-acetate [CPD:C05133];
            6-Aminohexanoate [CPD:C02378]
///
ENTRY       EC 3.5.3.1                  Enzyme
NAME        arginase;
            arginine amidinase;
            canavanase;
            L-arginase;
            arginine transamidinase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     L-arginine amidinohydrolase
REACTION    L-arginine + H2O = L-ornithine + urea [RN:R00551]
ALL_REAC    R00551
SUBSTRATE   L-arginine [CPD:C00062];
            H2O [CPD:C00001]
PRODUCT     L-ornithine [CPD:C00077];
            urea [CPD:C00086]
COMMENT     Also hydrolyses alpha-N-substituted L-arginines and canavanine.
REFERENCE   1  [PMID:13685626]
  AUTHORS   BACH SJ, KILLIP JD.
  TITLE     Studies on the purification and the kinetic properties of arginase
            from beef, sheep and horse liver.
  JOURNAL   Biochim. Biophys. Acta. 47 (1961) 336-43.
  ORGANISM  horse, sheep, cow [GN:bta]
REFERENCE   2  [PMID:13689647]
  AUTHORS   CABELLO J, BASILIO C, PRAJOUX V.
  TITLE     Kinetic properties of erythrocyte- and liver arginase.
  JOURNAL   Biochim. Biophys. Acta. 48 (1961) 148-52.
  ORGANISM  horse, human [GN:hsa]
REFERENCE   3
  AUTHORS   Dumitru, I.F.
  TITLE     Study of L-arginine amidinohydrolase from vegetable origin.
            Purification, crystallization and molecular weight.
  JOURNAL   Acta Vitamin. Enzymol. 27 (1973) 207-210.
REFERENCE   4
  AUTHORS   Greenberg, D.M.
  TITLE     Arginase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 4, Academic Press, New York, 1960, p. 257-267.
REFERENCE   5  [PMID:13328133]
  AUTHORS   GREENBERG DM, BAGOT AE, ROHOLT OA Jr.
  TITLE     Liver arginase.  III.  Properties of highly purified arginase.
  JOURNAL   Arch. Biochem. Biophys. 62 (1956) 446-53.
  ORGANISM  horse, rat [GN:rno]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K01476  arginase
GENES       HSA: 383(ARG1) 384(ARG2)
            PTR: 452985(ARG2)
            MMU: 11846(Arg1) 11847(Arg2)
            RNO: 29215(Arg2) 29221(Arg1)
            CFA: 480364(ARG2)
            SSC: 397115(ARG1)
            XLA: 379198(MGC53991) 380109(arg1) 397788(LOC397788)
            XTR: 448358(arg1)
            DRE: 322614(arg2)
            SPU: 586250(LOC586250) 752410(LOC752410)
            DME: Dmel_CG18104(arg)
            OSA: 4334912
            SCE: YPL111W(CAR1)
            AGO: AGOS_AGR225C
            PIC: PICST_78364(CAR1)
            CGR: CAGL0J07062g
            SPO: SPAC3H1.07(aru1) SPBP26C9.02c(car1)
            ANI: AN2901.2 AN3965.2 AN7669.2
            AFM: AFUA_3G11430
            AOR: AO090003000697 AO090011000557
            ANG: An02g07250(argA)
            CNE: CNG00550
            UMA: UM04939.1
            TBR: Tb927.8.2020
            LMA: LmjF35.1480
            EHI: 6.t00005
            XFA: XF1250
            XFT: PD0517(rocF)
            XCC: XCC3926(argI)
            XCB: XC_4015
            XCV: XCV4102(argI)
            XAC: XAC4009(argI)
            XOO: XOO0435(argI)
            XOM: XOO_0397(XOO0397)
            PSB: Psyr_2212
            PEN: PSEEN2606
            PCR: Pcryo_1794
            NOC: Noc_1712
            RSO: RSc0158(RS01028)
            REU: Reut_B4054
            RME: Rmet_3926
            BPE: BP0538
            BPA: BPP0749
            BBR: BB0835
            RFR: Rfer_3884
            POL: Bpro_4603
            MPT: Mpe_A1081
            DAR: Daro_2468
            TBD: Tbd_0069
            HPY: HP1399(rocF)
            HPA: HPAG1_1470
            HHE: HH1048(rocF)
            HAC: Hac_1761(rocF)
            PUB: SAR11_0206(speB1)
            MLO: mll6778 mlr5015
            MES: Meso_3963
            SME: SMa1711(argI2) SMc03091(argI1)
            ATU: Atu4007(arcA) Atu6018(arc)
            ATC: AGR_L_1693 AGR_pTi_56(arc)
            RET: RHE_CH03851(argI)
            RLE: RL4384(arcA)
            BME: BMEII0396
            BMF: BAB2_0337(rocF)
            BMS: BRA0900(rocF)
            BMB: BruAb2_0333(rocF)
            BOV: BOV_A0843(rocF)
            BJA: bll6122
            BRA: BRADO5323
            BBT: BBta_5811
            RPA: RPA4729(rocF)
            RPB: RPB_0842
            RPC: RPC_2929
            RPD: RPD_0950
            RPE: RPE_2678
            NWI: Nwi_0352
            NHA: Nham_0447
            SIL: SPO2119(rocF)
            SIT: TM1040_1165
            RSP: RSP_2632(argI)
            RDE: RD1_1416(arcA)
            ZMO: ZMO0432(rocF)
            ABA: Acid345_4596
            BSU: BG10932(rocF)
            BHA: BH0654 BH2984(rocF) BH3948
            BAN: BA0154(rocF)
            BAR: GBAA0154(rocF)
            BAA: BA_0735
            BAT: BAS0155
            BCE: BC0185
            BCA: BCE_0154(rocF)
            BCZ: BCZK0147(rocF)
            BTK: BT9727_0149(rocF)
            BTL: BALH_0151(rocF)
            BLI: BL01739(rocF) BL02695(rocFB)
            BLD: BLi00424(rocF) BLi00584
            BCL: ABC1426
            BAY: RBAM_037230(rocF)
            BPU: BPUM_0159(rocF)
            GKA: GK0149
            SAU: SA1968(arg)
            SAV: SAV2164(arg)
            SAM: MW2091(arg)
            SAR: SAR2255(rocF)
            SAS: SAS2066
            SAC: SACOL2154(rocF)
            SAB: SAB2044c(rocF)
            SAA: SAUSA300_2114(rocF)
            SAO: SAOUHSC_02409
            SSP: SSP0126 SSP0721
            LAC: LBA1022 LBA1572
            STH: STH2660
            CAC: CAC1054
            CTC: CTC01763
            DSY: DSY0747
            SMA: SAV1895(argI)
            LXX: Lxx06520(arg1)
            TFU: Tfu_1543
            SEN: SACE_4760(rocF)
            RXY: Rxyl_1270
            FNU: FN0501
            CHU: CHU_3637(rocF)
            DRA: DR_0651
            DGE: Dgeo_0292
            TTH: TTC1132
            TTJ: TTHA1496
            HMA: rrnAC0383(arg2) rrnAC0453(arg1)
            PTO: PTO0716
            RCI: LRC523(argI-1) RCIX2268(argI-2)
STRUCTURES  PDB: 1CEV  1D3V  1HQ5  1HQF  1HQG  1HQH  1HQX  1P8M  1P8N  1P8O  
                 1P8P  1P8Q  1P8R  1P8S  1PQ3  1R1O  1RLA  1T4P  1T4R  1T4S  
                 1T4T  1T5F  1T5G  1TA1  1TBH  1TBJ  1TBL  1WVA  1WVB  1ZPE  
                 1ZPG  2AEB  2CEV  2EF4  2EF5  2PHA  2PHO  2PLL  2RLA  3CEV  
                 3RLA  4CEV  4RLA  5CEV  5RLA  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.1
            ExPASy - ENZYME nomenclature database: 3.5.3.1
            ExplorEnz - The Enzyme Database: 3.5.3.1
            ERGO genome analysis and discovery system: 3.5.3.1
            BRENDA, the Enzyme Database: 3.5.3.1
            CAS: 9000-96-8
///
ENTRY       EC 3.5.3.2                  Enzyme
NAME        guanidinoacetase;
            glycocyaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     guanidinoacetate amidinohydrolase
REACTION    guanidinoacetate + H2O = glycine + urea [RN:R00775]
ALL_REAC    R00775
SUBSTRATE   guanidinoacetate [CPD:C00581];
            H2O [CPD:C00001]
PRODUCT     glycine [CPD:C00037];
            urea [CPD:C00086]
COFACTOR    Manganese [CPD:C00034]
COMMENT     Requires Mn2+.
REFERENCE   1  [PMID:14791411]
  AUTHORS   ROCHE J, LACOMBE G, GIRARD H.
  TITLE     [On the specificity of certain bacterial deguanidases generating
            urea and on arginindihydrolase.]
  JOURNAL   Biochim. Biophys. Acta. 6 (1950) 210-6.
REFERENCE   2
  AUTHORS   Yorifuji, T., Tamai, H. and Usami, H.
  TITLE     Purification, crystallization and properties of Mn2+ dependent
            guanidoacetate amidinohydrolase from a Pseudomonas.
  JOURNAL   Agric. Biol. Chem. 41 (1977) 959-966.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.2
            ExPASy - ENZYME nomenclature database: 3.5.3.2
            ExplorEnz - The Enzyme Database: 3.5.3.2
            ERGO genome analysis and discovery system: 3.5.3.2
            BRENDA, the Enzyme Database: 3.5.3.2
            CAS: 9024-92-4
///
ENTRY       EC 3.5.3.3                  Enzyme
NAME        creatinase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     creatine amidinohydrolase
REACTION    creatine + H2O = sarcosine + urea [RN:R01566]
ALL_REAC    R01566
SUBSTRATE   creatine [CPD:C00300];
            H2O [CPD:C00001]
PRODUCT     sarcosine [CPD:C00213];
            urea [CPD:C00086]
REFERENCE   1  [PMID:14791411]
  AUTHORS   ROCHE J, LACOMBE G, GIRARD H.
  TITLE     [On the specificity of certain bacterial deguanidases generating
            urea and on arginindihydrolase.]
  JOURNAL   Biochim. Biophys. Acta. 6 (1950) 210-6.
REFERENCE   2  [PMID:8443]
  AUTHORS   Yoshimoto T, Oka I, Tsuru D.
  TITLE     Purification, crystallization, and some properties of creatine
            amidinohydrolase from Pseudomonas putida.
  JOURNAL   J. Biochem. (Tokyo). 79 (1976) 1381-3.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K08688  creatinase
GENES       PUB: SAR11_0687(pepQ)
            SIL: SPO3327
            SIT: TM1040_2491
            RSP: RSP_1752
            RDE: RD1_0929(cln)
            AAU: AAur_3822
            RXY: Rxyl_0461
STRUCTURES  PDB: 1CHM  1KP0  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.3
            ExPASy - ENZYME nomenclature database: 3.5.3.3
            ExplorEnz - The Enzyme Database: 3.5.3.3
            ERGO genome analysis and discovery system: 3.5.3.3
            BRENDA, the Enzyme Database: 3.5.3.3
            CAS: 37340-58-2
///
ENTRY       EC 3.5.3.4                  Enzyme
NAME        allantoicase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     allantoate amidinohydrolase
REACTION    allantoate + H2O = (S)-ureidoglycolate + urea [RN:R02422]
ALL_REAC    R02422
SUBSTRATE   allantoate [CPD:C00499];
            H2O [CPD:C00001]
PRODUCT     (S)-ureidoglycolate [CPD:C00603];
            urea [CPD:C00086]
COMMENT     Also hydrolyses (R)-ureidoglycolate to glyoxylate and urea.
REFERENCE   1
  AUTHORS   Florkin, M. and Duchateau-Bosson, G.
  TITLE     Microdosage photometrique de l'allantoine en solutions pures et dans
            l'urine.
  JOURNAL   Enzymologia 9 (1940) 5-9.
REFERENCE   2  [PMID:4960174]
  AUTHORS   Trijbels F, Vogels GD.
  TITLE     Allantoicase and ureidoglycolase in Pseudomonas and Penicillium
            species.
  JOURNAL   Biochim. Biophys. Acta. 118 (1966) 387-95.
  ORGANISM  Pseudomonas sp., Penicillium sp.
REFERENCE   3  [PMID:16525953]
  AUTHORS   Hildebrand F, van Griensven M, Giannoudis P, Schreiber T, Frink M,
            Probst C, Grotz M, Krettek C, Pape HC.
  TITLE     Impact of hypothermia on the immunologic response after trauma and
            elective surgery.
  JOURNAL   Surg. Technol. Int. 14 (2005) 41-50.
REFERENCE   4
  AUTHORS   s'Gravenmade, E.J., van der Drift, C. and Vogels, G.D.
  TITLE     Hydrolysis, racemization and absolute configuration of
            ureidoglycolate, a substrate of allantoicase.
  JOURNAL   Biochim. Biophys. Acta 198 (1971) 569-582.
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01477  allantoicase
GENES       HSA: 55821(ALLC)
            PTR: 470294(ALLC)
            CFA: 475651(ALLC)
            XLA: 398942(MGC68581)
            DRE: 436989(allc)
            SPU: 576479(LOC576479)
            SCE: YIR029W(DAL2)
            AGO: AGOS_AER162C
            PIC: PICST_55822(DAL2)
            SPO: SPAC1F7.09c
            ANI: AN3104.2
            AFM: AFUA_3G12560
            DDI: DDB_0231471(allC)
            PPR: PBPRA2261
            PAE: PA1515(alc)
            PAU: PA14_44850(alc)
            PAP: PSPA7_3820(alc)
            PST: PSPTO_3668
            PSB: Psyr_1807
            PSP: PSPPH_1767
            PFL: PFL_4368
            PFO: Pfl_1704
            ACI: ACIAD3541(alc)
            CPS: CPS_4868
            HCH: HCH_01095(alc)
            RSO: RSc3274(RS02503)
            REH: H16_B2460
            BMA: BMA1505 BMA2460
            BMV: BMASAVP1_A0378 BMASAVP1_A2005
            BML: BMA10299_A1237 BMA10299_A3305
            BMN: BMA10247_1277 BMA10247_2648
            BXE: Bxe_A0569 Bxe_A1928 Bxe_B2651 Bxe_C1323
            BVI: Bcep1808_0615 Bcep1808_1886
            BUR: Bcep18194_A3733 Bcep18194_A5276
            BCN: Bcen_0164 Bcen_6116
            BCH: Bcen2424_0647 Bcen2424_1961
            BAM: Bamb_0542 Bamb_1949
            BPS: BPSL2116 BPSL2945
            BPM: BURPS1710b_2531 BURPS1710b_3459
            BPL: BURPS1106A_2430 BURPS1106A_3457
            BPD: BURPS668_2386 BURPS668_3422
            BTE: BTH_I1204 BTH_I2069
            HAR: HEAR3252(allC)
            AZO: azo1180(alc)
            SME: SMb21283
            MSM: MSMEG_5727(alc)
            MVA: Mvan_0935
            MMC: Mmcs_4781
            MKM: Mkms_4867
            MJL: Mjls_5167
            NFA: nfa52370
            RHA: RHA1_ro02572
            SCO: SCO6248(SCAH10.13)
            SMA: SAV1995
            FRA: Francci3_0840
            FAL: FRAAL1461
            SEN: SACE_6734
STRUCTURES  PDB: 1O59  1SG3  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.4
            ExPASy - ENZYME nomenclature database: 3.5.3.4
            ExplorEnz - The Enzyme Database: 3.5.3.4
            ERGO genome analysis and discovery system: 3.5.3.4
            BRENDA, the Enzyme Database: 3.5.3.4
            CAS: 9025-21-2
///
ENTRY       EC 3.5.3.5                  Enzyme
NAME        formimidoylaspartate deiminase;
            formiminoaspartate deiminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     N-formimidoyl-L-aspartate iminohydrolase
REACTION    N-formimidoyl-L-aspartate + H2O = N-formyl-L-aspartate + NH3
            [RN:R03188]
ALL_REAC    R03188;
            (other) R06138
SUBSTRATE   N-formimidoyl-L-aspartate [CPD:C03409];
            H2O [CPD:C00001]
PRODUCT     N-formyl-L-aspartate [CPD:C01044];
            NH3 [CPD:C00014]
REFERENCE   1  [PMID:13449062]
  AUTHORS   HAYAISHI O, TABOR H, HAYAISHI T.
  TITLE     N-formimino-L-aspartic acid as an intermediate in the enzymatic
            conversion of imidazoleacetic acid to formylaspartic acid.
  JOURNAL   J. Biol. Chem. 227 (1957) 161-80.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00340  Histidine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.5
            ExPASy - ENZYME nomenclature database: 3.5.3.5
            ExplorEnz - The Enzyme Database: 3.5.3.5
            ERGO genome analysis and discovery system: 3.5.3.5
            BRENDA, the Enzyme Database: 3.5.3.5
            CAS: 9025-07-4
///
ENTRY       EC 3.5.3.6                  Enzyme
NAME        arginine deiminase;
            arginine dihydrolase;
            citrulline iminase;
            L-arginine deiminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     L-arginine iminohydrolase
REACTION    L-arginine + H2O = L-citrulline + NH3 [RN:R00552]
ALL_REAC    R00552;
            (other) R06138
SUBSTRATE   L-arginine [CPD:C00062];
            H2O [CPD:C00001]
PRODUCT     L-citrulline [CPD:C00327];
            NH3 [CPD:C00014]
COMMENT     Also acts on canavanine.
REFERENCE   1  [PMID:12999797]
  AUTHORS   OGINSKY EL, GEHRIG RF.
  TITLE     The arginine dihydrolase system of Streptococcus faecalis.  II.
            Properties of arginine desimidase.
  JOURNAL   J. Biol. Chem. 198 (1952) 799-805.
  ORGANISM  Streptococcus faecalis
REFERENCE   2
  AUTHORS   Petrack, B., Sullivan, L. and Ratner, S.
  TITLE     Behavior of purified arginine desiminase from S. faecalis.
  JOURNAL   Arch. Biochem. Biophys. 69 (1957) 186-197.
  ORGANISM  Streptococcus faecalis
REFERENCE   3  [PMID:13158183]
  AUTHORS   RATNER S.
  TITLE     Urea synthesis and metabolism of arginine and citrulline.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 15 (1954) 319-87.
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K01478  arginine deiminase
GENES       ECC: c5350
            ECI: UTI89_C4857
            ECP: ECP_4500
            ECV: APECO1_2142
            STY: STY4805
            STT: t4501
            SPT: SPA4267
            SEC: SC4321(adi)
            STM: STM4467
            YEN: YE0535(arcA)
            ENT: Ent638_0452
            VCH: VC0423
            VCO: VC0395_A2842(arcA)
            VVU: VV1_1467
            VVY: VV2918
            VPA: VP2652
            VFI: VF0408
            PPR: PBPRA0477
            PAE: PA5171(arcA)
            PAU: PA14_68330(arcA)
            PAP: PSPA7_5911(arcA)
            PPU: PP_1001(arcA)
            PPF: Pput_1038
            PSB: Psyr_2684
            PFL: PFL_4635(arcA)
            PFO: Pfl_4386
            PEN: PSEEN4428(arcA)
            PMY: Pmen_1108
            HCH: HCH_05490(arcA)
            MMW: Mmwyl1_1975
            AHA: AHA_4093(arcA-2)
            DNO: DNO_1075(arcA)
            CVI: CV_3782(arcA)
            BMA: BMA1145(arcA)
            BMV: BMASAVP1_A1585(arcA)
            BML: BMA10299_A0244(arcA)
            BMN: BMA10247_0915(arcA)
            BXE: Bxe_A1877 Bxe_C0746
            BPS: BPSL1743(arcA)
            BPM: BURPS1710b_2128(arcA)
            BTE: BTH_I2384(arcA)
            MLO: mll6733
            MES: Meso_2241
            SME: SMa0693(arcA1) SMa1670(arcA2)
            SMD: Smed_5202
            OAN: Oant_4646
            BJA: bll7310
            RDE: RD1_0758(arcA)
            SUS: Acid_5795
            BCE: BC0406
            BCA: BCE_0472(arcA)
            BCY: Bcer98_0348
            BTK: BT9727_0341(arcA)
            BTL: BALH_0362(arcA)
            BLI: BL01912
            BLD: BLi04163
            SAU: SA2428(arcA)
            SAV: SAV2635(arcA)
            SAM: MW2556(arcA)
            SAR: SAR2714(arcA)
            SAS: SAS2521
            SAC: SACOL2657(arcA)
            SAB: SAB2510c(arcA)
            SAA: SAUSA300_0065(arcA) SAUSA300_2570(arcA)
            SAO: SAOUHSC_02969
            SAJ: SaurJH9_2659
            SAH: SaurJH1_2715
            SEP: SE0106 SE2217
            SER: SERP2250(arcA)
            SHA: SH0367(arcA)
            LMO: lmo0043
            LMF: LMOf2365_0052(arcA)
            LIN: lin0036
            LWE: lwe0034(arcA)
            LLA: L0329(arcA)
            LLM: llmg_2313(arcA)
            SPY: SPy_1547(sagP)
            SPZ: M5005_Spy_1275(arcA)
            SPM: spyM18_1564(arcA)
            SPG: SpyM3_1196(arcA)
            SPS: SPs0666
            SPH: MGAS10270_Spy1290(arcA)
            SPI: MGAS10750_Spy1382(arcA)
            SPJ: MGAS2096_Spy1294(arcA)
            SPK: MGAS9429_Spy1269(arcA)
            SPF: SpyM50577(arcA)
            SPA: M6_Spy1296
            SPB: M28_Spy1213(arcA)
            SPN: SP_2148
            SPR: spr1955 spr1956
            SAG: SAG2163(arcA)
            SAN: gbs2122
            SAK: SAK_2121(arcA)
            SSA: SSA_0737(sagP)
            SGO: SGO_1593(arcA)
            LSA: LSA0370(arcA)
            LBR: LVIS_2027
            LRE: Lreu_0445
            EFA: EF0104(arcA)
            OOE: OEOE_1118
            CPE: CPE0168(arcA)
            CPF: CPF_0161(arcA)
            CPR: CPR_0157(arcA)
            CBO: CBO0065(arcA1) CBO1587(arcA2)
            CBA: CLB_0101(arcA-1) CLB_1607(arcA-2)
            CBH: CLC_0113(arcA-1) CLC_1617(arcA-2)
            CBF: CLI_0122(arcA-1) CLI_1668(arcA-2)
            AMT: Amet_3161 Amet_4609
            TTE: TTE0103(arcA) TTE0531(arcA2)
            MPN: MPN304(arcA) MPN305(arcA) MPN560(arcA)
            MPE: MYPE6080(arcA)
            MGA: MGA_0105(arcA) MGA_1220(arcA)
            MMO: MMOB2230(arcA)
            MCP: MCAP_0089(arcA)
            MTU: Rv1001(arcA)
            MTC: MT1030(arcA)
            MBO: Mb1028(arcA)
            MBB: BCG_1058(arcA)
            MPA: MAP0942(arcA)
            MAV: MAV_1125(arcA)
            MSM: MSMEG_1409(arcA) MSMEG_5448(arcA)
            MVA: Mvan_1391 Mvan_4810
            MGI: Mflv_1923
            MMC: Mmcs_4276
            MKM: Mkms_4362
            MJL: Mjls_4655
            NFA: nfa32780 nfa49090
            RHA: RHA1_ro05654
            SCO: SCO0613(arcA) SCO5975(arcA2)
            SMA: SAV2320(arcA)
            PAC: PPA0583
            NCA: Noca_0166 Noca_2424
            TFU: Tfu_1993
            SEN: SACE_0131(arcA)
            STP: Strop_4517
            BGA: BG0868(arcA)
            BAF: BAPKO_0896(arcA)
            TDE: TDE0451(arcA)
            SRU: SRU_0666
            MAC: MA0792(arcA)
            MBA: Mbar_A1693
            TAC: Ta0987
            PTO: PTO1363
            SSO: SSO1148
            STO: ST1031
            MSE: Msed_0874
STRUCTURES  PDB: 1LXY  1RXX  1S9R  2A9G  2AAF  2ABR  2ACI  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.6
            ExPASy - ENZYME nomenclature database: 3.5.3.6
            ExplorEnz - The Enzyme Database: 3.5.3.6
            ERGO genome analysis and discovery system: 3.5.3.6
            BRENDA, the Enzyme Database: 3.5.3.6
            CAS: 9027-98-9
///
ENTRY       EC 3.5.3.7                  Enzyme
NAME        guanidinobutyrase;
            gamma-guanidobutyrase;
            4-guanidinobutyrate amidinobutyrase;
            gamma-guanidinobutyrate amidinohydrolase;
            G-Base;
            GBH;
            guanidinobutyrate ureahydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     4-guanidinobutanoate amidinohydrolase
REACTION    4-guanidinobutanoate + H2O = 4-aminobutanoate + urea [RN:R01990]
ALL_REAC    R01990
SUBSTRATE   4-guanidinobutanoate [CPD:C01035];
            H2O [CPD:C00001]
PRODUCT     4-aminobutanoate [CPD:C00334];
            urea [CPD:C00086]
COFACTOR    Manganese [CPD:C00034]
COMMENT     Requires Mn2+. Also acts, very slowly, on 5-guanidinopentanoate and
            6-guanidinohexanoate.
REFERENCE   1  [PMID:5862400]
  AUTHORS   Mora J, Tarrab R, Martuscelli J, Soberon G.
  TITLE     Characteristics of arginases from ureotelic and non-ureotelic
            animals.
  JOURNAL   Biochem. J. 96 (1965) 588-94.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:5936244]
  AUTHORS   Nguyen Van Thoai, Thome-Beau F, Olomucki A.
  TITLE     [Induction and specificity of enzymes of the new catabolic arginine
            pathway]
  JOURNAL   Biochim. Biophys. Acta. 115 (1966) 73-80.
  ORGANISM  Streptomyces griseus
REFERENCE   3
  AUTHORS   Yorifuji, T., Kato, M., Kobayashi, T., Ozaki, S. and Ueno, S.
  TITLE     4-Guanidinobutyrate amidinohydrolase from Pseudomonas sp ATCC 14676:
            purification to homogeneity and properties.
  JOURNAL   Agric. Biol. Chem. 44 (1980) 1127-1134.
  ORGANISM  Pseudomonas sp.
REFERENCE   4
  AUTHORS   Yorifuji, T., Kobayashi, T., Tabuchi, A., Shiritani, Y. and Yonaha,
            K.
  TITLE     Distribution of amidinohydrolases among Pseudomonas and comparative
            studies of some purified enzymes by one-dimensional peptide mapping.
  JOURNAL   Agric. Biol. Chem. 47 (1983) 2825-2830.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
GENES       RHA: RHA1_ro03527
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.7
            ExPASy - ENZYME nomenclature database: 3.5.3.7
            ExplorEnz - The Enzyme Database: 3.5.3.7
            ERGO genome analysis and discovery system: 3.5.3.7
            BRENDA, the Enzyme Database: 3.5.3.7
            CAS: 9013-69-8
///
ENTRY       EC 3.5.3.8                  Enzyme
NAME        formimidoylglutamase;
            formiminoglutamase;
            N-formiminoglutamate hydrolase;
            N-formimino-L-glutamate formiminohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     N-formimidoyl-L-glutamate formimidoylhydrolase
REACTION    N-formimidoyl-L-glutamate + H2O = L-glutamate + formamide
            [RN:R02285]
ALL_REAC    R02285
SUBSTRATE   N-formimidoyl-L-glutamate [CPD:C00439];
            H2O [CPD:C00001]
PRODUCT     L-glutamate [CPD:C00025];
            formamide [CPD:C00488]
REFERENCE   1  [PMID:4990470]
  AUTHORS   Kaminskas E, Kimhi Y, Magasanik B.
  TITLE     Urocanase and N-formimino-L-glutamate formiminohydrolase of Bacillus
            subtilis, two enzymes of the histidine degradation pathway.
  JOURNAL   J. Biol. Chem. 245 (1970) 3536-44.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   2  [PMID:5845833]
  AUTHORS   Lund P, Magasanik B.
  TITLE     N-formimino-L-glutamate formiminohydrolase of Aerobacter aerogenes.
  JOURNAL   J. Biol. Chem. 240 (1965) 4316-9.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00340  Histidine metabolism
ORTHOLOGY   KO: K01479  formiminoglutamase
GENES       TCR: 507031.90 507963.20
            STY: STY0821(hutG)
            STT: t2099(hutG)
            SPT: SPA1964(hutG)
            SEC: SC0786(hutG)
            STM: STM0788(hutG)
            YPE: YPO1971(hutG)
            YPK: y2341
            YPM: YP_1713(hutG)
            YPA: YPA_1353
            YPN: YPN_1451
            YPS: YPTB1965(hutG)
            PLU: plu3196(hutG)
            XCC: XCC1578(hutG)
            XCB: XC_2656
            XCV: XCV1677(hutG)
            XAC: XAC1636(hutG)
            XOO: XOO2399(hutG)
            XOM: XOO_2279(XOO2279)
            VCH: VC1204
            VCO: VC0395_A0824(hutG)
            VVU: VV1_2391
            VVY: VV1950
            VPA: VP1275
            VFI: VFA0452
            PPR: PBPRA2171
            PAE: PA3175 PA5091(hutG)
            PAU: PA14_23170(hutG) PA14_67240(hutG)
            PAP: PSPA7_1954
            PPU: PP_5029(hutG)
            PST: PSPTO_5278
            PSB: Psyr_4836
            PFL: PFL_0349(hutG)
            PEN: PSEEN5093(hutG)
            PCR: Pcryo_1933
            PHA: PSHAa2735(hutG)
            LPN: lpg0709
            LPF: lpl0746(hutG)
            LPP: lpp0764(hutG)
            HCH: HCH_04170(hutG)
            AHA: AHA_0378(hutG)
            CVI: CV_0322(hutG)
            RSO: RSc2645(RS04571)
            REU: Reut_A1591 Reut_A2711
            RME: Rmet_5045
            BXE: Bxe_B2046
            BBR: BB2645
            EBA: ebA5739(hutG)
            AZO: azo3002(hutG)
            BBA: Bd1812(hutG)
            MLO: mlr8322
            MES: Meso_2984
            SME: SMb21164(hutG)
            ATU: Atu3932
            ATC: AGR_L_1827
            RET: RHE_PE00071(hutG)
            RLE: pRL110204
            BME: BMEII0366
            BMF: BAB2_0304
            BMS: BRA0931(hutG)
            BMB: BruAb2_0302(hutG)
            CCR: CC_0958
            RDE: RD1_3679(hutG)
            BSU: BG11099(hutG)
            BHA: BH1985(hutG)
            BAN: BA3709(hutG)
            BAR: GBAA3709(hutG)
            BAA: BA_4192
            BAT: BAS3439
            BCA: BCE_3677(hutG)
            BCZ: BCZK3351(hutG)
            BTK: BT9727_3402(hutG)
            BTL: BALH_3284(hutG)
            BCL: ABC0371
            BAY: RBAM_036440(hutG)
            GKA: GK1365
            SAU: SA2125
            SAV: SAV2334
            SAM: MW2254
            SAR: SAR2420
            SAS: SAS2226
            SAC: SACOL2327(hutG)
            SAB: SAB2211c(hutG)
            SAA: SAUSA300_2281(hutG)
            SAO: SAOUHSC_02610
            SEP: SE1907
            SER: SERP1919(hutG)
            SHA: SH0723
            SSP: SSP0570
            SPY: SPy_2090(hutG)
            SPZ: M5005_Spy_1778(hutG)
            SPM: spyM18_2148
            SPG: SpyM3_1780(hutG)
            SPS: SPs1777
            SPH: MGAS10270_Spy1844(hutG)
            SPI: MGAS10750_Spy1870(hutG)
            SPJ: MGAS2096_Spy1811(hutG)
            SPK: MGAS9429_Spy1789(hutG)
            SPF: SpyM51736(hutG)
            SPA: M6_Spy1776
            SPB: M28_Spy1762(hutG)
            SSA: SSA_0428(hutG)
            SGO: SGO_1813(hutG)
            LCA: LSEI_1554
            CTC: CTC01812
            CEF: CE1257
            NFA: nfa12350
            RHA: RHA1_ro04640(hutG)
            AAU: AAur_0405(hutG)
            FNU: FN0662
            CHU: CHU_3062(hutG)
            GFO: GFO_0757(hutG)
            HAL: VNG1209G(hutG)
            HMA: rrnAC1789(hutG)
            PTO: PTO0106
STRUCTURES  PDB: 1XFK  2A0M  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.8
            ExPASy - ENZYME nomenclature database: 3.5.3.8
            ExplorEnz - The Enzyme Database: 3.5.3.8
            ERGO genome analysis and discovery system: 3.5.3.8
            BRENDA, the Enzyme Database: 3.5.3.8
            CAS: 9054-92-6
///
ENTRY       EC 3.5.3.9                  Enzyme
NAME        allantoate deiminase;
            allantoate amidohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     allantoate amidinohydrolase (decarboxylating)
REACTION    allantoate + H2O = ureidoglycine + NH3 + CO2 [RN:R02423]
ALL_REAC    R02423;
            (other) R05554 R06138
SUBSTRATE   allantoate [CPD:C00499];
            H2O [CPD:C00001]
PRODUCT     ureidoglycine [CPD:C02091];
            NH3 [CPD:C00014];
            CO2 [CPD:C00011]
REFERENCE   1  [PMID:5328936]
  AUTHORS   Vogels GD.
  TITLE     Reversible activation of allantoate amidohydrolase by
            acid-pretreatment and other properties of the enzyme.
  JOURNAL   Biochim. Biophys. Acta. 113 (1966) 277-91.
PATHWAY     PATH: map00230  Purine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.9
            ExPASy - ENZYME nomenclature database: 3.5.3.9
            ExplorEnz - The Enzyme Database: 3.5.3.9
            ERGO genome analysis and discovery system: 3.5.3.9
            BRENDA, the Enzyme Database: 3.5.3.9
            CAS: 37289-13-7
///
ENTRY       EC 3.5.3.10                 Enzyme
NAME        D-arginase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     D-arginine amidinohydrolase
REACTION    D-arginine + H2O = D-ornithine + urea [RN:R02458]
ALL_REAC    R02458
SUBSTRATE   D-arginine [CPD:C00792];
            H2O [CPD:C00001]
PRODUCT     D-ornithine [CPD:C00515];
            urea [CPD:C00086]
REFERENCE   1
  AUTHORS   Nadai, Y.
  TITLE     Arginase. II. Distribution and properties of D-arginase.
  JOURNAL   J. Biochem. (Tokyo) 45 (1958) 1011-1020.
  ORGANISM  pig [GN:ssc], dog [GN:cfa], toad, mouse [GN:mmu], rabbit, human
            [GN:hsa]
PATHWAY     PATH: map00472  D-Arginine and D-ornithine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.10
            ExPASy - ENZYME nomenclature database: 3.5.3.10
            ExplorEnz - The Enzyme Database: 3.5.3.10
            ERGO genome analysis and discovery system: 3.5.3.10
            BRENDA, the Enzyme Database: 3.5.3.10
            CAS: 37289-14-8
///
ENTRY       EC 3.5.3.11                 Enzyme
NAME        agmatinase;
            agmatine ureohydrolase;
            SpeB
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     agmatine amidinohydrolase
REACTION    agmatine + H2O = putrescine + urea [RN:R01157]
ALL_REAC    R01157
SUBSTRATE   agmatine [CPD:C00179];
            H2O [CPD:C00001]
PRODUCT     putrescine [CPD:C00134];
            urea [CPD:C00086]
REFERENCE   1  [PMID:4908780]
  AUTHORS   Hirshfield IN, Rosenfeld HJ, Leifer Z, Maas WK.
  TITLE     Isolation and characterization of a mutant of Escherichia coli
            blocked in the synthesis of putrescine.
  JOURNAL   J. Bacteriol. 101 (1970) 725-30.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Vicente, C. and Legaz, M.E.
  TITLE     Preparation and properties of agmatine amidinohydrolase of Evernia
            prunastri.
  JOURNAL   Physiol. Plant. 55 (1982) 335-339.
  ORGANISM  Evernia prunastri
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K01480  agmatinase
GENES       HSA: 79814(AGMAT)
            PTR: 469130(AGMAT)
            MMU: 75986(Agmat)
            RNO: 298607(Agmat)
            CFA: 487430(AGMAT)
            GGA: 373942(AGMAT)
            DRE: 556522(zgc:153353)
            SPU: 577889(LOC577889)
            AGO: AGOS_AFR048W
            PIC: PICST_32515(SPB2) PICST_55948(CAR12)
            SPO: SPAC11D3.09 SPBC8E4.03
            ANI: AN6869.2 AN7488.2
            AFM: AFUA_2G05750 AFUA_5G13180
            AOR: AO090001000694 AO090120000455
            CNE: CND03500
            UMA: UM01858.1
            ECO: b2937(speB)
            ECJ: JW2904(speB)
            ECE: Z4281(speB)
            ECS: ECs3812
            ECC: c3522(speB)
            ECI: UTI89_C3325(speB)
            ECP: ECP_2931
            ECV: APECO1_3592(speB)
            ECW: EcE24377A_3279(speB)
            ECX: EcHS_A3095(speB) EcHS_A3245(rpsU)
            STY: STY3238(speB)
            STT: t2998(speB)
            SPT: SPA2949(speB)
            SEC: SC3020(speB)
            STM: STM3078(speB)
            SFL: SF2927(speB)
            SFX: S3129(speB)
            SFV: SFV_2989(speB)
            SSN: SSON_3091(speB)
            SBO: SBO_3052(speB)
            SDY: SDY_3139(speB)
            PLU: plu3680(speB)
            SGL: SG2017
            BFL: Bfl253(speB)
            BPN: BPEN_260(speB)
            PMU: PM1381(speE)
            VCH: VCA0814
            VCO: VC0395_0420(speB)
            VVU: VV1_2355
            VVY: VV1987
            VPA: VPA0169
            VFI: VFA0839
            PAE: PA0288(speB1) PA1421(speB2)
            PAU: PA14_03770(speB1) PA14_46070(gbuA)
            PAP: PSPA7_0379(speB2) PSPA7_3918(speB1)
            PPU: PP_2196(speB) PP_4523
            PFL: PFL_0325 PFL_1574
            PFO: Pfl_1457 Pfl_2576
            PEN: PSEEN3509(speB) PSEEN3933
            PCR: Pcryo_1550
            ACI: ACIAD1299(speB)
            SDN: Sden_2278
            ILO: IL1212(speB)
            CPS: CPS_0384(speB)
            PHA: PSHAa1076(speB) PSHAb0317
            CBU: CBU_0720
            CBD: COXBU7E912_0733(speB)
            CSA: Csal_2838
            NME: NMB0469
            NMA: NMA2016(speB)
            NMC: NMC1680(speB)
            NGO: NGO1486
            CVI: CV_0490(speB)
            RSO: RSp1578(speB)
            REU: Reut_B5705
            REH: H16_A0044(speB)
            BMA: BMAA1597(speB)
            BML: BMA10299_1996(speB)
            BMN: BMA10247_A0674(speB)
            BXE: Bxe_A3438 Bxe_B0946
            BUR: Bcep18194_A4379 Bcep18194_B0366 Bcep18194_B1147
                 Bcep18194_B2787
            BCN: Bcen_3083 Bcen_3696
            BCH: Bcen2424_4672 Bcen2424_5284
            BAM: Bamb_4066 Bamb_4644
            BPS: BPSS0474(speB) BPSS1587(speB)
            BPM: BURPS1710b_A0639 BURPS1710b_A2027
            BPL: BURPS1106A_A0643(speB) BURPS1106A_A2157(speB)
            BPD: BURPS668_A0735(speB) BURPS668_A2243(speB)
            BTE: BTH_II0784 BTH_II1941
            BPE: BP1531
            BPA: BPP2778
            BBR: BB2707
            RFR: Rfer_0346 Rfer_0597
            POL: Bpro_2025
            PNA: Pnap_2635
            VEI: Veis_0334
            MPT: Mpe_A1890
            NEU: NE1147
            NET: Neut_1437 Neut_2187
            ABU: Abu_1569(speB)
            DVU: DVU0421
            DDE: Dde_0574
            BBA: Bd0356 Bd3436(speB)
            DPS: DP1391
            ADE: Adeh_2584
            MXA: MXAN_4431
            SAT: SYN_01147
            SFU: Sfum_0721
            PUB: SAR11_1329(speB)
            MLO: mll0412 mll8453 mlr4895
            MES: Meso_1162
            SME: SMc01802(speB) SMc01967(speB2)
            ATU: Atu1245(speB)
            ATC: AGR_C_2296
            RET: RHE_CH01568(speB1) RHE_CH02143(speB2)
            RLE: RL1669(speB) RL2427 RL4455(speB) pRL100366(agmaT)
            BME: BMEI0110 BMEI1170
            BMF: BAB1_0809 BAB1_1958
            BMS: BR0789 BR1957
            BMB: BruAb1_0803 BruAb1_1933
            BOV: BOV_0784(speB)
            BRA: BRADO6795
            BBT: BBta_0743
            SIL: SPO0599(speB-1) SPO0678 SPO2464(speB-2) SPO2467(speB-3)
                 SPOA0235(speB-4)
            SIT: TM1040_0938 TM1040_0939
            RSP: RSP_2909 RSP_3743(speB1)
            RSH: Rsph17029_1554
            JAN: Jann_0277 Jann_1967 Jann_2340
            RDE: RD1_2715 RD1_3130 RD1_3131
            MAG: amb1100
            MGM: Mmc1_3564
            BSU: BG12461(speB)
            BHA: BH3810
            BAN: BA5617
            BAR: GBAA5617
            BAA: BA_0473
            BAT: BAS5218
            BCE: BC5370
            BCA: BCE_5498
            BCZ: BCZK5066(speB)
            BTK: BT9727_5050(speB)
            BTL: BALH_4866(speB)
            BLI: BL03921(speB)
            BLD: BLi03973(speB)
            BCL: ABC1178 ABC3897(speB)
            BPU: BPUM_3386(speB)
            OIH: OB2551
            GKA: GK3404
            SSP: SSP2175
            STH: STH18
            CPE: CPE0551(speB)
            CPF: CPF_0530(speB)
            CPR: CPR_0516(speB)
            CKL: CKL_2407(speB)
            CHY: CHY_1620
            DSY: DSY0233
            SWO: Swol_0669
            TTE: TTE1335(speB)
            MTA: Moth_1815
            MSM: MSMEG_1072(speB) MSMEG_3535(speB) MSMEG_4374(speB)
                 MSMEG_4459(speB)
            MMC: Mmcs_2256 Mmcs_2734 Mmcs_3024 Mmcs_5283
            MKM: Mkms_2778
            MJL: Mjls_2764
            SCO: SCO2770(SCC105.01c)
            SMA: SAV5285(speB)
            TFU: Tfu_0058
            FRA: Francci3_0848
            SEN: SACE_6017(speB)
            RXY: Rxyl_2907
            SYN: sll0228(speB1) sll1077(speB2)
            SYW: SYNW1412 SYNW2422
            SYD: Syncc9605_1082 Syncc9605_2591
            SYE: Syncc9902_2230
            SYG: sync_2851(speB)
            SYR: SynRCC307_2435(speB) SynRCC307_2478(speB)
            SYX: SynWH7803_2454(speB)
            CYA: CYA_0535 CYA_0859(speB)
            CYB: CYB_1744(speB) CYB_2252
            GVI: gll3725
            ANA: alr2310
            AVA: Ava_0127
            PMA: Pro1849(speB)
            PMM: PMM1686
            PMT: PMT2214
            PMN: PMN2A_1287
            PMI: PMT9312_1779
            PMB: A9601_18961(speB)
            PMC: P9515_18771(speB)
            PMF: P9303_29511(speB)
            PMG: P9301_18771(speB)
            PMH: P9215_19591(speB)
            PME: NATL1_21591(speB)
            TER: Tery_3780
            GFO: GFO_3624(speB)
            FPS: FP2214(speB)
            DRA: DR_A0149
            DGE: Dgeo_2732
            TTH: TTC0764
            TTJ: TTHA1129
            MJA: MJ0309
            MMP: MMP1585
            MAC: MA3986
            MBA: Mbar_A0694
            MMA: MM_0923
            MBU: Mbur_1896
            MST: Msp_0415
            MSI: Msm_0876
            MKA: MK0738
            HAL: VNG1767G(speB)
            HMA: pNG7067(speB2) rrnAC1927(speB1)
            HWA: HQ3349A(speB)
            NPH: NP3022A(speD_1) NP4754A(speD_2)
            TAC: Ta1058
            TVO: TVN0538
            PAB: PAB0050(speB)
            PFU: PF1957
            TKO: TK0882
            RCI: LRC54(speB)
            APE: APE_0316.1 APE_1637.1
            HBU: Hbut_0051
            SSO: SSO0445(speB-1) SSO2732(speB-2)
            STO: ST0352
            SAI: Saci_0863 Saci_2134
            PAI: PAE2260(speB)
            NEQ: NEQ223
STRUCTURES  PDB: 1GQ6  1GQ7  1WOG  1WOH  1WOI  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.11
            ExPASy - ENZYME nomenclature database: 3.5.3.11
            ExplorEnz - The Enzyme Database: 3.5.3.11
            ERGO genome analysis and discovery system: 3.5.3.11
            BRENDA, the Enzyme Database: 3.5.3.11
            CAS: 37289-16-0
///
ENTRY       EC 3.5.3.12                 Enzyme
NAME        agmatine deiminase;
            agmatine amidinohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     agmatine iminohydrolase
REACTION    agmatine + H2O = N-carbamoylputrescine + NH3 [RN:R01416]
ALL_REAC    R01416;
            (other) R06138
SUBSTRATE   agmatine [CPD:C00179];
            H2O [CPD:C00001]
PRODUCT     N-carbamoylputrescine [CPD:C00436];
            NH3 [CPD:C00014]
COMMENT     The plant enzyme also catalyses the reactions of EC 2.1.3.3
            (ornithine carbamoyltransferase), EC 2.1.3.6 (putrescine
            carbamoyltransferase) and EC 2.7.2.2 (carbamate kinase), thus
            functioning as a putrescine synthase, converting agmatine and
            ornithine into putrescine and citrulline, respectively.
REFERENCE   1
  AUTHORS   Smith, T.A.
  TITLE     Agmatine iminohydrolase in maize.
  JOURNAL   Phytochemistry 8 (1969) 2111-2117.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   2  [PMID:6895223]
  AUTHORS   Srivenugopal KS, Adiga PR.
  TITLE     Enzymic conversion of agmatine to putrescine in Lathyrus sativus
            seedlings. Purification and properties of a multifunctional enzyme
            (putrescine synthase).
  JOURNAL   J. Biol. Chem. 256 (1981) 9532-41.
  ORGANISM  Lathyrus sativus
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K10536  agmatine deiminase
GENES       YPI: YpsIP31758_0832(aguA)
            SPE: Spro_2482
            PAP: PSPA7_0383(aguA)
            PPF: Pput_0281
            PEN: PSEEN0261(aguA)
            PMY: Pmen_0337
            SBM: Shew185_3139
            SSE: Ssed_2405
            SPL: Spea_1202
            FTA: FTA_0528
            MMW: Mmwyl1_1489
            AHA: AHA_0738
            GUR: Gura_1447
            PLA: Plav_1144 Plav_2804
            OAN: Oant_1048
            SWI: Swit_1203
            SPD: SPD_0814
            LSL: LSL_1674
            CBE: Cbei_1922
            KRA: Krad_0833
            FJO: Fjoh_3413
            RRS: RoseRS_2742
            RCA: Rcas_1823
STRUCTURES  PDB: 1VKP  2EWO  2JER  2Q3U  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.12
            ExPASy - ENZYME nomenclature database: 3.5.3.12
            ExplorEnz - The Enzyme Database: 3.5.3.12
            ERGO genome analysis and discovery system: 3.5.3.12
            BRENDA, the Enzyme Database: 3.5.3.12
            CAS: 37289-17-1
///
ENTRY       EC 3.5.3.13                 Enzyme
NAME        formimidoylglutamate deiminase;
            formiminoglutamate deiminase;
            formiminoglutamic iminohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     N-formimidoyl-L-glutamate iminohydrolase
REACTION    N-formimidoyl-L-glutamate + H2O = N-formyl-L-glutamate + NH3
            [RN:R02286]
ALL_REAC    R02286;
            (other) R06138
SUBSTRATE   N-formimidoyl-L-glutamate [CPD:C00439];
            H2O [CPD:C00001]
PRODUCT     N-formyl-L-glutamate [CPD:C01045];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Wickner, R.B. and Tabor, H.
  TITLE     N-Formimino-L-glutamate iminohydrolase (Pseudomonas sp.).
  JOURNAL   Methods Enzymol. 17B (1971) 80-84.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00340  Histidine metabolism
ORTHOLOGY   KO: K05603  formimidoylglutamate deiminase
GENES       YPI: YpsIP31758_2111(hutF)
            PAP: PSPA7_5839(hutF)
            PSP: PSPPH_0350(hutF)
            PFL: PFL_0398(hutF)
            PEN: PSEEN5100
            REH: H16_A3014(hutF)
            RME: Rmet_2851
            BMA: BMA0650(hutF)
            BMV: BMASAVP1_A2361(hutF)
            BML: BMA10299_A2924(hutF)
            BMN: BMA10247_1676(hutF)
            BAM: Bamb_2206
            BPM: BURPS1710b_2791(hutF)
            BPL: BURPS1106A_2718(hutF)
            BPD: BURPS668_2662(hutF)
            BTE: BTH_I1825(hutF)
            MXA: MXAN_1010(hutF)
            BOV: BOV_A0870(hutF)
            RSP: RSP_2933(hutF)
            RDE: RD1_3676(hutF)
            HNE: HNE_2394(hutF)
            MSM: MSMEG_1181(hutF)
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.13
            ExPASy - ENZYME nomenclature database: 3.5.3.13
            ExplorEnz - The Enzyme Database: 3.5.3.13
            ERGO genome analysis and discovery system: 3.5.3.13
            BRENDA, the Enzyme Database: 3.5.3.13
            CAS: 9054-85-7
///
ENTRY       EC 3.5.3.14                 Enzyme
NAME        amidinoaspartase;
            amidinoaspartic amidinohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     N-amidino-L-aspartate amidinohydrolase
REACTION    N-amidino-L-aspartate + H2O = L-aspartate + urea [RN:R00777]
ALL_REAC    R00777
SUBSTRATE   N-amidino-L-aspartate [CPD:C03139];
            H2O [CPD:C00001]
PRODUCT     L-aspartate [CPD:C00049];
            urea [CPD:C00086]
COMMENT     Also acts slowly on N-amidino-L-glutamate.
REFERENCE   1  [PMID:4651648]
  AUTHORS   Milstien S, Goldman P.
  TITLE     Metabolism of guanidinosuccinic acid. I. Characterization of a
            specific amidino hydrolase from Pseudomonas chlororaphis.
  JOURNAL   J. Biol. Chem. 247 (1972) 6280-3.
  ORGANISM  Pseudomonas chlororaphis
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.14
            ExPASy - ENZYME nomenclature database: 3.5.3.14
            ExplorEnz - The Enzyme Database: 3.5.3.14
            ERGO genome analysis and discovery system: 3.5.3.14
            BRENDA, the Enzyme Database: 3.5.3.14
            CAS: 37325-60-3
///
ENTRY       EC 3.5.3.15                 Enzyme
NAME        protein-arginine deiminase;
            peptidylarginine deiminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     protein-L-arginine iminohydrolase
REACTION    protein L-arginine + H2O = protein L-citrulline + NH3 [RN:R02621]
ALL_REAC    R02621
SUBSTRATE   protein L-arginine;
            H2O [CPD:C00001]
PRODUCT     protein L-citrulline [CPD:C03022];
            NH3 [CPD:C00014]
COMMENT     Also acts on N-acyl-L-arginine and, more slowly, on L-arginine
            esters.
REFERENCE   1  [PMID:7217033]
  AUTHORS   Fujisaki M, Sugawara K.
  TITLE     Properties of peptidylarginine deiminase from the epidermis of
            newborn rats.
  JOURNAL   J. Biochem. (Tokyo). 89 (1981) 257-63.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K01481  
GENES       HSA: 11240(PADI2) 23569(PADI4) 29943(PADI1) 353238(PADI6)
                 51702(PADI3)
            PTR: 469178(PADI3)
            MMU: 18599(Padi1) 18600(Padi2) 18601(Padi3) 18602(Padi4)
                 242726(Padi6)
            RNO: 29511(Padi2) 29512(Padi4) 29520(Padi3) 54282(Padi1)
            CFA: 478216(PADI3) 487413(PADI6) 487414(PADI2) 606921(PADI4)
            GGA: 395910(PADI3) 428171(PADI1) 428172(PADI2)
            XLA: 380061(padi2)
            DRE: 386792(zgc:66317)
            MXA: MXAN_6411
            TER: Tery_4936
STRUCTURES  PDB: 1WD8  1WD9  1WDA  2DEW  2DEX  2DEY  2DW5  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.15
            ExPASy - ENZYME nomenclature database: 3.5.3.15
            ExplorEnz - The Enzyme Database: 3.5.3.15
            ERGO genome analysis and discovery system: 3.5.3.15
            BRENDA, the Enzyme Database: 3.5.3.15
            CAS: 75536-80-0
///
ENTRY       EC 3.5.3.16                 Enzyme
NAME        methylguanidinase;
            methylguanidine hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     methylguanidine amidinohydrolase
REACTION    methylguanidine + H2O = methylamine + urea [RN:R01589]
ALL_REAC    R01589
SUBSTRATE   methylguanidine [CPD:C02294];
            H2O [CPD:C00001]
PRODUCT     methylamine [CPD:C00218];
            urea [CPD:C00086]
COMMENT     Acts on some other alkylguanidines, but very slowly.
REFERENCE   1  [PMID:7353662]
  AUTHORS   Nakajima M, Shirokane Y, Mizusawa K.
  TITLE     A new amidinohydrolase, methylguanidine amidinohydrolase from
            Alcaligenes sp. N-42.
  JOURNAL   FEBS. Lett. 110 (1980) 43-6.
  ORGANISM  Alcaligenes sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.16
            ExPASy - ENZYME nomenclature database: 3.5.3.16
            ExplorEnz - The Enzyme Database: 3.5.3.16
            ERGO genome analysis and discovery system: 3.5.3.16
            BRENDA, the Enzyme Database: 3.5.3.16
            CAS: 73200-93-8
///
ENTRY       EC 3.5.3.17                 Enzyme
NAME        guanidinopropionase;
            GPase;
            GPH
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     3-guanidinopropanoate amidinopropionase
REACTION    3-guanidinopropanoate + H2O = beta-alanine + urea [RN:R00913]
ALL_REAC    R00913
SUBSTRATE   3-guanidinopropanoate [CPD:C03065];
            H2O [CPD:C00001]
PRODUCT     beta-alanine [CPD:C00099];
            urea [CPD:C00086]
COFACTOR    Manganese [CPD:C00034]
COMMENT     Requires Mn2+. Also acts, more slowly, on taurocyamine and
            4-guanidinobutanoate.
REFERENCE   1
  AUTHORS   Yorifuji, T., Sugai, I., Matsumoto, H. and Tabuchi, A.
  TITLE     Characterization of 3-guanidinopropionate amidinohydrolase from
            Pseudomonas aeruginosa and a comparative study with 4-
            guanidinobutyrate amidinohydrolase from another Pseudomonas.
  JOURNAL   Agric. Biol. Chem. 46 (1982) 1361-1363.
  ORGANISM  Pseudomonas aeruginosa
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.17
            ExPASy - ENZYME nomenclature database: 3.5.3.17
            ExplorEnz - The Enzyme Database: 3.5.3.17
            ERGO genome analysis and discovery system: 3.5.3.17
            BRENDA, the Enzyme Database: 3.5.3.17
            CAS: 68821-77-2
///
ENTRY       EC 3.5.3.18                 Enzyme
NAME        dimethylargininase;
            dimethylarginine dimethylaminohydrolase;
            NG,NG-dimethylarginine dimethylaminohydrolase;
            NG,NG-dimethyl-L-arginine dimethylamidohydrolase;
            omega,omega'-di-N-methyl-L-arginine dimethylamidohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     Nomega,Nomega'-methyl-L-arginine dimethylamidohydrolase
REACTION    Nomega,Nomega'-methyl-L-arginine + H2O = dimethylamine +
            L-citrulline [RN:R02513]
ALL_REAC    R02513
SUBSTRATE   Nomega,Nomega'-methyl-L-arginine;
            H2O [CPD:C00001]
PRODUCT     dimethylamine [CPD:C00543];
            L-citrulline [CPD:C00327]
COMMENT     Also acts on Nomega-methyl-L-arginine.
REFERENCE   1  [PMID:2722865]
  AUTHORS   Ogawa T, Kimoto M, Sasaoka K.
  TITLE     Purification and properties of a new enzyme, NG,NG-dimethylarginine
            dimethylaminohydrolase, from rat kidney.
  JOURNAL   J. Biol. Chem. 264 (1989) 10205-9.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K01482  
GENES       HSA: 23564(DDAH2) 23576(DDAH1)
            MMU: 51793(Ddah2) 69219(Ddah1)
            RNO: 64157(Ddah1)
            CFA: 474846(DDAH2) 490182(DDAH1)
            GGA: 378898(DDAH1)
            XLA: 380577(ddah1) 447158(MGC85472)
            DRE: 406561(zgc:85829)
            SPU: 583809(LOC583809)
            DME: Dmel_CG1764
            SPE: Spro_2396
            LPN: lpg1657
            LPF: lpl1622
            LPP: lpp1628
            BUR: Bcep18194_B2143
            BCN: Bcen_4424
            BCH: Bcen2424_3943
            BAM: Bamb_3320
            SME: SMb21304
            SUS: Acid_1735
            SCO: SCO6718(ddaH)
            CMI: CMM_2543(ddaH)
STRUCTURES  PDB: 1H70  2C6Z  2CI1  2CI3  2CI4  2CI5  2CI6  2CI7  2JAI  2JAJ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.18
            ExPASy - ENZYME nomenclature database: 3.5.3.18
            ExplorEnz - The Enzyme Database: 3.5.3.18
            ERGO genome analysis and discovery system: 3.5.3.18
            BRENDA, the Enzyme Database: 3.5.3.18
            CAS: 123644-75-7
///
ENTRY       EC 3.5.3.19                 Enzyme
NAME        ureidoglycolate hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     (S)-ureidoglycolate amidohydrolase (decarboxylating)
REACTION    (S)-ureidoglycolate + H2O = glyoxylate + 2 NH3 + CO2 [RN:R00469]
ALL_REAC    R00469
SUBSTRATE   (S)-ureidoglycolate [CPD:C00603];
            H2O [CPD:C00001]
PRODUCT     glyoxylate [CPD:C00048];
            NH3 [CPD:C00014];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Winkler, R.G., Blevins, D.G. and Randall, D.D.
  TITLE     Ureide catabolism in soybeans. III. Ureidoglycolate amidohydrolase
            and allantoate amidohydrolase are activities of an allantoate
            degrading enzyme complex.
  JOURNAL   Plant Physiol. 86 (1988) 1084-1088.
  ORGANISM  Glycine max [GN:egma]
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01483  ureidoglycolate hydrolase
GENES       SCE: YIR032C(DAL3)
            AGO: AGOS_AGR218C
            PIC: PICST_43701(DAL3)
            SPO: SPAC19G12.04
            AFM: AFUA_8G04760
            AOR: AO090005000694
            ECO: b0505(allA)
            ECJ: JW0493(allA)
            ECE: Z0659(ybbT)
            ECS: ECs0566
            ECC: c0620(ybbT)
            ECP: ECP_0566
            ECV: APECO1_1509(allA)
            ECW: EcE24377A_0542(allA)
            ECX: EcHS_A0579
            STY: STY0563(allA)
            SPT: SPA2207(allA)
            SEC: SC0556(allA)
            STM: STM0515(allA)
            SFL: SF0444(ybbT)
            SFX: S0451(ybbT)
            SFV: SFV_0472(ybbT)
            SBO: SBO_0409(ybbT)
            SDY: SDY_0397(ybbT)
            PPR: PBPRA2260
            PAE: PA1514
            PAU: PA14_44860(allA)
            PPU: PP_4288
            PPF: Pput_1580
            PST: PSPTO_3669(allA)
            PSB: Psyr_1806
            PSP: PSPPH_1766(allA)
            PFL: PFL_4369(allA)
            PFO: Pfl_1703
            PEN: PSEEN1683(allA)
            PMY: Pmen_0302 Pmen_2760
            PCR: Pcryo_1920
            ACI: ACIAD3542(allA)
            CPS: CPS_4871(allA)
            HCH: HCH_01092(allA)
            CSA: Csal_0080
            REH: H16_B2455
            BMA: BMA1504(allA-1)
            BMV: BMASAVP1_A0376(allA) BMASAVP1_A0377 BMASAVP1_A2004(allA-1)
            BML: BMA10299_A1235(allA) BMA10299_A1236(allA-2)
                 BMA10299_A3306(allA-1)
            BMN: BMA10247_1276(allA-1) BMA10247_2646(allA) BMA10247_2647
            BXE: Bxe_A0570 Bxe_A1929
            BVI: Bcep1808_0616 Bcep1808_1885
            BUR: Bcep18194_A3734 Bcep18194_A4467 Bcep18194_A5275
            BCN: Bcen_0165 Bcen_6117
            BCH: Bcen2424_0648 Bcen2424_1960
            BAM: Bamb_0543 Bamb_1948
            BPS: BPSL2115 BPSL2944
            BPM: BURPS1710b_2530 BURPS1710b_3458
            BPL: BURPS1106A_2429(allA) BURPS1106A_3456(allA)
            BPD: BURPS668_2385(allA) BURPS668_3421(allA)
            BTE: BTH_I1205(allA) BTH_I2070
            BPA: BPP0689(allA)
            BBR: BB0696(allA)
            POL: Bpro_1402
            AZO: azo1179(allA)
            MLO: mll5130
            MES: Meso_2829
            SME: SMb20677 SMb20873(allA)
            SMD: Smed_4312 Smed_4491
            ATU: Atu1409(allA) Atu2324(allA)
            ATC: AGR_C_2603 AGR_C_4225
            RET: RHE_CH03139(allA)
            RLE: RL3584(allA)
            BME: BMEI1430
            BMF: BAB1_0531
            BMS: BR0507
            BMB: BruAb1_0529
            OAN: Oant_0694
            BRA: BRADO2841(allA)
            BBT: BBta_5333(allA)
            RPA: RPA0554
            SIL: SPO0873(allA)
            SIT: TM1040_3474
            RSP: RSP_1552
            RSH: Rsph17029_0204
            RSQ: Rsph17025_3033
            JAN: Jann_2607
            RDE: RD1_4152(allA)
            PDE: Pden_2103
STRUCTURES  PDB: 1XSQ  1XSR  1YQC  2BDR  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.19
            ExPASy - ENZYME nomenclature database: 3.5.3.19
            ExplorEnz - The Enzyme Database: 3.5.3.19
            ERGO genome analysis and discovery system: 3.5.3.19
            BRENDA, the Enzyme Database: 3.5.3.19
            CAS: 115629-07-7
///
ENTRY       EC 3.5.3.20                 Enzyme
NAME        diguanidinobutanase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     1,4-diguanidinobutane amidinohydrolase
REACTION    1,4-diguanidinobutane + H2O = agmatine + urea [RN:R01418]
ALL_REAC    R01418
SUBSTRATE   1,4-diguanidinobutane [CPD:C03047];
            H2O [CPD:C00001]
PRODUCT     agmatine [CPD:C00179];
            urea [CPD:C00086]
COMMENT     Other diguanidinoalkanes with 3 to 10 methylene groups can also act,
            but more slowly.
REFERENCE   1
  AUTHORS   Yorifuji, T., Kaneoke, M., Shimizu, E., Shiota, K. and Matsuo, R.
  TITLE     Degradation of alpha,omega-diguanidinoalkanes and a novel enzyme,
            diguanidinobutane amidohydrolase, in Pseudomonas putida.
  JOURNAL   Agric. Biol. Chem. 53 (1989) 3003-3009.
  ORGANISM  Pseudomonas putida [GN:ppu]
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.20
            ExPASy - ENZYME nomenclature database: 3.5.3.20
            ExplorEnz - The Enzyme Database: 3.5.3.20
            ERGO genome analysis and discovery system: 3.5.3.20
            BRENDA, the Enzyme Database: 3.5.3.20
            CAS: 125268-65-7
///
ENTRY       EC 3.5.3.21                 Enzyme
NAME        methylenediurea deaminase;
            methylenediurease
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     methylenediurea aminohydrolase
REACTION    (1) (1a) NH2-CO-NH-CH2-NH-CO-NH2 + H2O = N-(carboxyaminomethyl)urea
            + NH3 [RN:R05170];
            (2) (1b) N-(carboxyaminomethyl)urea = N-(aminomethyl)urea + CO2
            (spontaneous) [RN:R05171];
            (3) (1c) N-(aminomethyl)urea + H2O = N-(hydroxymethyl)urea + NH3
            (spontaneous) [RN:R05172]
ALL_REAC    R05170 R05171 R05172;
            (other) R05169
SUBSTRATE   NH2-CO-NH-CH2-NH-CO-NH2;
            H2O [CPD:C00001];
            N-(carboxyaminomethyl)urea [CPD:C06382];
            N-(aminomethyl)urea [CPD:C06383]
PRODUCT     N-(carboxyaminomethyl)urea [CPD:C06382];
            NH3 [CPD:C00014];
            N-(aminomethyl)urea [CPD:C06383];
            CO2 [CPD:C00011];
            N-(hydroxymethyl)urea [CPD:C06384]
COMMENT     The methylenediurea is hydrolysed and decarboxylated to give an
            aminated methylurea, which then spontaneously hydrolyses to
            hydroxymethylurea. The enzyme from Ochrobactrum anthropi also
            hydrolyses dimethylenetriurea and trimethylenetetraurea as well as
            ureidoglycolate, which is hydrolysed to urea and glyoxylate, and
            allantoate, which is hydrolysed to ureidoglycolate, ammonia and
            carbon dioxide.
REFERENCE   1
  AUTHORS   Jahns, T., Schepp, R., Kaltwasser, H.
  TITLE     Purification and characterisation of an enzyme from a strain of
            Ochrobactrum anthropi that degrades condensation products of urea
            and formaldehyde (ureaform).
  JOURNAL   Can. J. Microbiol. 43 (1997) 1111-1117.
  ORGANISM  Ochrobactrum anthropi
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.21
            ExPASy - ENZYME nomenclature database: 3.5.3.21
            ExplorEnz - The Enzyme Database: 3.5.3.21
            ERGO genome analysis and discovery system: 3.5.3.21
            BRENDA, the Enzyme Database: 3.5.3.21
            CAS: 205830-62-2
///
ENTRY       EC 3.5.3.22                 Enzyme
NAME        proclavaminate amidinohydrolase;
            PAH;
            proclavaminate amidino hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     amidinoproclavaminate amidinohydrolase
REACTION    amidinoproclavaminate + H2O = proclavaminate + urea [RN:R05357]
ALL_REAC    R05357
SUBSTRATE   amidinoproclavaminate [CPD:C06657];
            H2O [CPD:C00001]
PRODUCT     proclavaminate [CPD:C06658];
            urea [CPD:C00086]
COMMENT     Forms part of the pathway for the biosythesis of the beta-lactamase
            inhibitor clavulanate in Streptomyces clavuligerus. It carries out
            an intermediary reaction between the first reaction of EC
            1.14.11.21, clavaminate synthase, and the second and third reactions
            of that enzyme. Requires Mn2+.
REFERENCE   1  [PMID:1998687]
  AUTHORS   Salowe SP, Krol WJ, Iwata-Reuyl D, Townsend CA.
  TITLE     Elucidation of the order of oxidations and identification of an
            intermediate in the multistep clavaminate synthase reaction.
  JOURNAL   Biochemistry. 30 (1991) 2281-92.
  ORGANISM  Streptomyces clavuligerus
REFERENCE   2  [PMID:11472170]
  AUTHORS   Zhou J, Kelly WL, Bachmann BO, Gunsior M, Townsend CA, Solomon EI.
  TITLE     Spectroscopic studies of substrate interactions with clavaminate
            synthase 2, a multifunctional alpha-KG-dependent non-heme iron
            enzyme: correlation with mechanisms and reactivities.
  JOURNAL   J. Am. Chem. Soc. 123 (2001) 7388-98.
  ORGANISM  Streptomyces clavuligerus
REFERENCE   3  [PMID:12413541]
  AUTHORS   Townsend CA.
  TITLE     New reactions in clavulanic acid biosynthesis.
  JOURNAL   Curr. Opin. Chem. Biol. 6 (2002) 583-9.
  ORGANISM  Streptomyces clavuligerus
REFERENCE   4  [PMID:7601835]
  AUTHORS   Wu TK, Busby RW, Houston TA, McIlwaine DB, Egan LA, Townsend CA.
  TITLE     Identification, cloning, sequencing, and overexpression of the gene
            encoding proclavaminate amidino hydrolase and characterization of
            protein function in clavulanic acid biosynthesis.
  JOURNAL   J. Bacteriol. 177 (1995) 3714-20.
  ORGANISM  Streptomyces clavuligerus
PATHWAY     PATH: map00331  Clavulanic acid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.22
            ExPASy - ENZYME nomenclature database: 3.5.3.22
            ExplorEnz - The Enzyme Database: 3.5.3.22
            ERGO genome analysis and discovery system: 3.5.3.22
            BRENDA, the Enzyme Database: 3.5.3.22
///
ENTRY       EC 3.5.3.23                 Enzyme
NAME        N-succinylarginine dihydrolase;
            N2-succinylarginine dihydrolase;
            arginine succinylhydrolase;
            SADH;
            AruB;
            AstB;
            2-N-succinyl-L-arginine iminohydrolase (decarboxylating)
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
SYSNAME     N2-succinyl-L-arginine iminohydrolase (decarboxylating)
REACTION    N2-succinyl-L-arginine + 2 H2O = N2-succinyl-L-ornithine + 2 NH3 +
            CO2 [RN:R04189]
ALL_REAC    R04189
SUBSTRATE   N2-succinyl-L-arginine [CPD:C03296];
            H2O [CPD:C00001]
PRODUCT     N2-succinyl-L-ornithine [CPD:C03415];
            NH3 [CPD:C00014];
            CO2 [CPD:C00011]
COMMENT     Arginine, N2-acetylarginine and N2-glutamylarginine do not act as
            substrates [3]. This is the second enzyme in the arginine
            succinyltransferase (AST) pathway for the catabolism of arginine
            [1]. This pathway converts the carbon skeleton of arginine into
            glutamate, with the concomitant production of ammonia and conversion
            of succinyl-CoA into succinate and CoA. The five enzymes involved in
            this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC
            3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.81
            (succinylornithine transaminase), EC 1.2.1.71 (succinylglutamate
            semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate
            desuccinylase).
REFERENCE   1  [PMID:9696779]
  AUTHORS   Schneider BL, Kiupakis AK, Reitzer LJ.
  TITLE     Arginine catabolism and the arginine succinyltransferase pathway in
            Escherichia coli.
  JOURNAL   J. Bacteriol. 180 (1998) 4278-86.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:15703173]
  AUTHORS   Tocilj A, Schrag JD, Li Y, Schneider BL, Reitzer L, Matte A, Cygler
            M.
  TITLE     Crystal structure of N-succinylarginine dihydrolase AstB, bound to
            substrate and product, an enzyme from the arginine catabolic pathway
            of Escherichia coli.
  JOURNAL   J. Biol. Chem. 280 (2005) 15800-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:2865249]
  AUTHORS   Vander Wauven C, Stalon V.
  TITLE     Occurrence of succinyl derivatives in the catabolism of arginine in
            Pseudomonas cepacia.
  JOURNAL   J. Bacteriol. 164 (1985) 882-6.
  ORGANISM  Pseudomonas cepacia
REFERENCE   4  [PMID:3534538]
  AUTHORS   Cunin R, Glansdorff N, Pierard A, Stalon V.
  TITLE     Biosynthesis and metabolism of arginine in bacteria.
  JOURNAL   Microbiol. Rev. 50 (1986) 314-52.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   5  [PMID:9393691]
  AUTHORS   Itoh Y.
  TITLE     Cloning and characterization of the aru genes encoding enzymes of
            the catabolic arginine succinyltransferase pathway in Pseudomonas
            aeruginosa.
  JOURNAL   J. Bacteriol. 179 (1997) 7280-90.
  ORGANISM  Pseudomonas aeruginosa
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K01484  succinylarginine dihydrolase
GENES       ECO: b1745(astB)
            ECJ: JW1734(astB)
            ECE: Z2777
            ECS: ECs2451
            ECC: c2145
            ECI: UTI89_C1940(astB)
            ECP: ECP_1691
            ECV: APECO1_814(astB)
            ECW: EcE24377A_1967(astB)
            ECX: EcHS_A1828
            STY: STY1808(astB)
            STT: t1185(astB)
            SPT: SPA1538(astB)
            STM: STM1306(astB)
            YPE: YPO1965(astB)
            YPK: y2346
            YPA: YPA_1347
            YPS: YPTB1962(astB)
            SSN: SSON_1412
            SBO: SBO_1345
            SDY: SDY_1532
            PLU: plu3107(astB)
            VFI: VFA0847
            PPR: PBPRB0591
            PAE: PA0899(aruB)
            PAU: PA14_52660(aruB)
            PAP: PSPA7_4616(astB)
            PPU: PP_4477(astB)
            PST: PSPTO_1836(astB)
            PSB: Psyr_3561
            PSP: PSPPH_3517(astB)
            PFL: PFL_4511(astB)
            PFO: Pfl_4281
            PEN: PSEEN3878(aruB)
            ACI: ACIAD1288(astB)
            SON: SO_2706(astB)
            SDN: Sden_2329
            SFR: Sfri_2479
            SHE: Shewmr4_1584
            SHM: Shewmr7_1659
            SHN: Shewana3_1728
            ILO: IL1011(astB)
            PHA: PSHAb0177(astB)
            PAT: Patl_2357
            LPN: lpg1708(astB)
            LPF: lpl1667(astB)
            LPP: lpp1673(astB)
            HCH: HCH_01951(astB)
            CSA: Csal_2804
            AHA: AHA_3105(astB)
            CVI: CV_1500(aruB)
            BMA: BMA0595(astB)
            BXE: Bxe_A2919
            BUR: Bcep18194_A4295
            BCN: Bcen_0705
            BCH: Bcen2424_1184
            BAM: Bamb_1065
            BPS: BPSL2386(astB)
            BPM: BURPS1710b_2842(astB)
            BTE: BTH_I1779(astB)
            NMU: Nmul_A1594
            MXA: MXAN_1056(astB)
            CCR: CC_1608
            MMR: Mmar10_1855
            HNE: HNE_1993(astB)
            NAR: Saro_0882
            SAL: Sala_1941
            ELI: ELI_08925
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.3.23
            ExPASy - ENZYME nomenclature database: 3.5.3.23
            ExplorEnz - The Enzyme Database: 3.5.3.23
            ERGO genome analysis and discovery system: 3.5.3.23
            BRENDA, the Enzyme Database: 3.5.3.23
///
ENTRY       EC 3.5.3.-                  Enzyme
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In linear amidines
REACTION    5-Ureido-4-imidazole carboxylate + H2O <=> 5-Amino-4-imidazole
            carboxylate + NH3 + CO2 [RN:R04857]
SUBSTRATE   5-Ureido-4-imidazole carboxylate [CPD:C05515];
            H2O [CPD:C00001]
PRODUCT     5-Amino-4-imidazole carboxylate [CPD:C05516];
            NH3 [CPD:C00014];
            CO2 [CPD:C00011]
///
ENTRY       EC 3.5.4.1                  Enzyme
NAME        cytosine deaminase;
            isocytosine deaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     cytosine aminohydrolase
REACTION    cytosine + H2O = uracil + NH3 [RN:R00974]
ALL_REAC    R00974;
            (other) R01411 R06137
SUBSTRATE   cytosine [CPD:C00380];
            H2O [CPD:C00001]
PRODUCT     uracil [CPD:C00106];
            NH3 [CPD:C00014]
COMMENT     Also acts on 5-methylcytosine.
REFERENCE   1  [PMID:13438848]
  AUTHORS   COHEN SS, BARNER HD.
  TITLE     The conversion of 5-methyldeoxycytidine to thymidine in vitro and in
            vivo.
  JOURNAL   J. Biol. Chem. 226 (1957) 631-42.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Kream, J. and Chargaff, E.
  TITLE     On the cytosine deaminase of yeast.
  JOURNAL   J. Am. Chem. Soc. 74 (1952) 5157-5160.
  ORGANISM  Escherichia coli [GN:eco], Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K01485  cytosine deaminase
GENES       SCE: YPR062W(FCY1)
            AGO: AGOS_ADL328C
            PIC: PICST_30000(TAD3) PICST_78481(FCY1)
            CGR: CAGL0D01562g
            AFM: AFUA_1G05050
            AOR: AO090003000802
            TPV: TP03_0793
            ECO: b0337(codA)
            ECJ: JW0328(codA)
            ECE: Z0433(codA)
            ECS: ECs0390
            ECC: c0456(codA)
            ECI: UTI89_C0368(codA)
            ECP: ECP_0412
            ECV: APECO1_1652(codA)
            ECW: EcE24377A_0361(codA)
            ECX: EcHS_A0402(codA)
            STY: STY3514(codA)
            STT: t3251(codA)
            SPT: SPA3202(codA)
            SEC: SC3272(codA)
            STM: STM3334
            YPE: YPO0162(codA)
            YPK: y3946(codA)
            YPM: YP_0164(codA)
            YPA: YPA_3307
            YPN: YPN_3902
            YPS: YPTB3739(codA)
            YPI: YpsIP31758_3955(codA)
            BFL: Bfl537(yfhC)
            BPN: BPEN_557(tadA)
            PMU: PM0565
            XCC: XCC3491(codA)
            XCB: XC_0670
            XCV: XCV0694
            XAC: XAC0639(codA)
            XOO: XOO3979(codA)
            XOM: XOO_3752(XOO3752)
            VVU: VV2_0789
            VVY: VVA1255
            VPA: VPA1243
            VFI: VF0531
            PPR: PBPRB1375
            PAE: PA0437(codA)
            PAU: PA14_05690(codA)
            PPU: PP_3189(codA)
            PST: PSPTO_1602(cdd)
            PSB: Psyr_3776
            PSP: PSPPH_1477(cdd)
            PFL: PFL_4033(codA)
            PFO: Pfl_4584
            PEN: PSEEN1634 PSEEN3052(ccd) PSEEN3598
            PAR: Psyc_1496(cumB)
            SON: SO_1397
            SBL: Sbal_3077
            SBM: Shew185_3086
            SPC: Sputcn32_1204
            SHE: Shewmr4_2798
            SHM: Shewmr7_2881
            SHN: Shewana3_2977
            SHW: Sputw3181_2960
            PAT: Patl_3869
            MCA: MCA1307(cdd)
            HCH: HCH_05147
            CSA: Csal_2506
            AHA: AHA_0082(codA)
            NMA: NMA1129
            NMC: NMC0911
            RSO: RSc1594(codA)
            REU: Reut_A1846 Reut_B3993
            REH: H16_B1593(codA)
            RME: Rmet_4568
            BMA: BMAA0603(codA)
            BML: BMA10299_0864(codA)
            BMN: BMA10247_A1831(codA)
            BXE: Bxe_A1533 Bxe_C0802
            BPS: BPSS0761(codA)
            BPM: BURPS1710b_A2335(codA)
            BPL: BURPS1106A_A1034(codA)
            BPD: BURPS668_A1120(codA)
            BTE: BTH_II1639
            MMS: mma_2914(codA)
            AZO: azo3769(codA)
            DAR: Daro_2202
            TBD: Tbd_1216
            WSU: WS1357(serA)
            TDN: Tmden_1635
            PCA: Pcar_0327
            PPD: Ppro_1980
            BBA: Bd0236
            DPS: DP2354
            RTY: RT0819
            RCO: RC1285
            RFE: RF_1319
            RBE: RBE_1426
            RCM: A1E_05335
            OTS: OTBS_1716(codA)
            AMA: AM868(ssnA)
            APH: APH_0321
            ECN: Ecaj_0573
            ECH: ECH_0449
            MLO: mll1290 mlr5363
            SME: SMa2371(codA1)
            RET: RHE_CH00834(codAch1) RHE_CH02043(codAch2) RHE_PB00107(codAb)
            RLE: RL0891 pRL120308(codA) pRL90208(codA)
            BME: BMEII1040
            BMF: BAB2_0197
            BJA: bll4780 bll7276
            SIL: SPO2806
            SIT: TM1040_3052
            RSP: RSP_0341
            JAN: Jann_1474
            RDE: RD1_1293 RD1_2362(cdd)
            ZMO: ZMO0863(dcd)
            GOX: GOX0799
            BCE: BC4503
            BTL: BALH_4083
            BCL: ABC4032
            SAB: SAB0509
            SAK: SAK_0474
            LSA: LSA1212 LSA1213
            LDB: Ldb1636
            LBR: LVIS_1932
            CPE: CPE0756
            CPF: CPF_0750(codA)
            CPR: CPR_0737(codA)
            CTC: CTC00078 CTC01883
            CBO: CBO2072(codA)
            CBA: CLB_2010(codA)
            CBH: CLC_2015(codA)
            CBF: CLI_2125(codA)
            MTA: Moth_0460
            MMY: MSC_0049(codA)
            AYW: AYWB_606(codA)
            MSM: MSMEG_4687
            CGB: cg0281
            RHA: RHA1_ro05151
            SMA: SAV4806(cdd4)
            ART: Arth_0892
            AAU: AAur_1110
            NCA: Noca_4144
            TFU: Tfu_0027
            FRA: Francci3_0280
            KRA: Krad_2066
            SEN: SACE_0233 SACE_2115(codA) SACE_5196(codA)
            BLO: BL0011(codA)
            RBA: RB8824
            LIL: LA4330(codA)
            SYN: slr1237(codA)
            SYW: SYNW1638(codA)
            SYC: syc0954_d(codA)
            SYF: Synpcc7942_0568
            SYD: Syncc9605_0854
            SYE: Syncc9902_1538
            SYG: sync_0740
            SYR: SynRCC307_0961
            SYX: SynWH7803_1751(codA)
            CYA: CYA_1567 CYA_1587(codA)
            CYB: CYB_0393(codA) CYB_1063
            TEL: tlr0459
            GVI: gll2528
            ANA: all3284
            AVA: Ava_4937
            PMA: Pro1378(ssnA)
            PMM: PMM1304(codA)
            PMT: PMT0326(codA)
            PMN: PMN2A_0870
            PMI: PMT9312_1400
            PMB: A9601_09421(cumB) A9601_15031(codA)
            PMC: P9515_10011(cumB) P9515_14651(codA)
            PMF: P9303_16461(cumB) P9303_19891(codA)
            PMG: P9301_09411(cumB) P9301_14901(codA)
            PMH: P9215_15331(codA)
            PME: NATL1_07751(cumB) NATL1_17241(codA)
            CHU: CHU_0109 CHU_2245(yfhC)
            CCH: Cag_0190
            MMQ: MmarC5_0677
            MAC: MA2559
            MMA: MM_3105
            MBU: Mbur_1204
            MEM: Memar_0824
            MBN: Mboo_0945
            MSI: Msm_1386
            HWA: HQ2049A(guaD) HQ2620A(guaD) HQ3010A(guaD)
            NPH: NP0972A(guaD_1) NP4788A(guaD_3)
            RCI: RCIX2492(codA)
            SSO: SSO2770(codA)
            STO: ST2403
            SAI: Saci_1072
STRUCTURES  PDB: 1K6W  1K70  1OX7  1P6O  1R9X  1R9Y  1RA0  1RA5  1RAK  1RB7  
                 1UAQ  1YSB  1YSD  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.1
            ExPASy - ENZYME nomenclature database: 3.5.4.1
            ExplorEnz - The Enzyme Database: 3.5.4.1
            ERGO genome analysis and discovery system: 3.5.4.1
            BRENDA, the Enzyme Database: 3.5.4.1
            CAS: 9025-05-2
///
ENTRY       EC 3.5.4.2                  Enzyme
NAME        adenine deaminase;
            adenase;
            adenine aminase;
            ADase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     adenine aminohydrolase
REACTION    adenine + H2O = hypoxanthine + NH3 [RN:R01244]
ALL_REAC    R01244;
            (other) R06137
SUBSTRATE   adenine [CPD:C00147];
            H2O [CPD:C00001]
PRODUCT     hypoxanthine [CPD:C00262];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Blauch, M., Koch, F.C. and Hane, M.E.
  TITLE     A study of xanthine oxidase of rat blood.
  JOURNAL   J. Biol. Chem. 130 (1939) 471-486.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Heppel, L.A., Hurwitz, J. and Horecker, B.L.
  TITLE     Adenine deaminase of Azotobacter vinelandii.
  JOURNAL   J. Am. Chem. Soc. 79 (1957) 630-633.
  ORGANISM  Azotobacter vinelandii
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01486  adenine deaminase
GENES       ECO: b3665(ade)
            ECJ: JW3640(ade)
            ECE: Z5155(yicP)
            ECS: ECs4602
            ECC: c4589(yicP)
            ECI: UTI89_C4221(yicP)
            ECP: ECP_3871
            ECV: APECO1_2787(ade)
            ECW: EcE24377A_4173(ade)
            ECX: EcHS_A3878
            SFL: SF3796(yicP)
            SFX: S3972(yicP)
            SFV: SFV_3844(yicP)
            SSN: SSON_3619(yicP)
            SBO: SBO_3704(yicP)
            SDY: SDY_4146(yicP)
            SPE: Spro_1116
            BUR: Bcep18194_B1471
            SUN: SUN_0856(ade)
            GME: Gmet_2201
            DVU: DVU0441(ade)
            DVL: Dvul_2495
            DDE: Dde_0136
            BBA: Bd2636(yicP)
            DPS: DP1373 DP1374
            SAT: SYN_02726
            SFU: Sfum_0417
            MLO: mlr0157
            MES: Meso_1082
            SME: SMa1715(adeC3) SMa1718(adeC4) SMb21278(adeC2) SMc01533(adeC1)
            SMD: Smed_2318 Smed_4610 Smed_5275 Smed_5277
            ATU: Atu2292(adeC) Atu4426(adeC)
            ATC: AGR_C_4165 AGR_L_883
            RET: RHE_CH03094(adeC1) RHE_CH03420(adeC2)
            RLE: RL2014 RL3541(ade) RL3883(ade) RL4472(ade) pRL90169(ade)
            BME: BMEII0627
            BMF: BAB2_0587
            BMS: BRA0653(ade)
            BMB: BruAb2_0573(ade)
            BOV: BOV_A0615(ade)
            OAN: Oant_3735
            BJA: bll6142 blr3165
            BRA: BRADO2460 BRADO4947
            BBT: BBta_3118
            SIL: SPO3746(ade)
            SIT: TM1040_2799
            RSP: RSP_0985
            RSH: Rsph17029_2645
            RSQ: Rsph17025_0239
            JAN: Jann_0338 Jann_3233
            RDE: RD1_0605(ade)
            PDE: Pden_2836
            GOX: GOX1719
            BSU: BG11044(adeC) BG12829(yerA)
            BHA: BH0637 BH0640(adeC)
            BAN: BA3032
            BAR: GBAA3032
            BAA: BA_3541
            BAT: BAS2818
            BCE: BC3012
            BCZ: BCZK2753(ade)
            BTK: BT9727_2766(ade)
            BTL: BALH_4413
            BLI: BL01492(yerA) BL01613(adeC)
            BLD: BLi00711(yerA) BLi01667(adeC)
            BCL: ABC1075 ABC1077(adeC) ABC3209
            BAY: RBAM_014260
            BPU: BPUM_0617(yerA) BPUM_1348
            OIH: OB0751 OB1030(adeC)
            GKA: GK0271 GK1989 GK2098
            LMO: lmo1742(adeC)
            LMF: LMOf2365_1767(ade)
            LIN: lin1853(adeC)
            LWE: lwe1759(adeC)
            LPL: lp_3334(adeC)
            LSA: LSA0088(adeC1) LSA1670(adeC2)
            LSL: LSL_0929(adeC)
            LDB: Ldb2182(adeC)
            EFA: EF1222(ade)
            OOE: OEOE_0158 OEOE_1462
            CAC: CAC0887(adeC)
            CPE: CPE1268(adeC)
            CPF: CPF_1476
            CDF: CD1820(ade)
            CBO: CBO0294(ade)
            CBA: CLB_0338(ade)
            CBH: CLC_0353(ade)
            CBF: CLI_0367(ade)
            CBE: Cbei_1277 Cbei_1975
            AMT: Amet_4567 Amet_4574
            CHY: CHY_0689(ade1) CHY_0699(ade2)
            DSY: DSY3665
            DRM: Dred_2771
            MTA: Moth_0463
            FAL: FRAAL1454
            RXY: Rxyl_0377 Rxyl_1744
            SRU: SRU_2375(ade)
            FPS: FP1059(adeC)
            DET: DET0791(ade)
            DEH: cbdb_A769(adeC)
            DEB: DehaBAV1_0717
            DRA: DR_A0270
            DGE: Dgeo_0420
            TME: Tmel_1731
            MAE: Maeo_0932
            MAC: MA2310(adeC)
            MBA: Mbar_A3342
            MMA: MM_2910
            MBU: Mbur_0733
            MTP: Mthe_0522
            MLA: Mlab_1602 Mlab_1603
            MEM: Memar_1539
            MBN: Mboo_1575
            MST: Msp_1308(ade)
            MSI: Msm_0874
            MKA: MK0829(adeC)
            HMA: rrnAC3411
            PTO: PTO1085
            SMR: Smar_0382
STRUCTURES  PDB: 2ICS  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.2
            ExPASy - ENZYME nomenclature database: 3.5.4.2
            ExplorEnz - The Enzyme Database: 3.5.4.2
            ERGO genome analysis and discovery system: 3.5.4.2
            BRENDA, the Enzyme Database: 3.5.4.2
            CAS: 9027-68-3
///
ENTRY       EC 3.5.4.3                  Enzyme
NAME        guanine deaminase;
            guanase;
            guanine aminase;
            GAH
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     guanine aminohydrolase
REACTION    guanine + H2O = xanthine + NH3 [RN:R01676]
ALL_REAC    R01676;
            (other) R06137
SUBSTRATE   guanine [CPD:C00242];
            H2O [CPD:C00001]
PRODUCT     xanthine [CPD:C00385];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Hitchings, G.H. and Falco, E.A.
  TITLE     The identification of guanine in extracts of Girella nigricans. The
            specificity of guanase.
  JOURNAL   Proc. Natl. Acad. Sci. USA 30 (1944) 294-297.
  ORGANISM  Girella nigricans
REFERENCE   2
  AUTHORS   Kalckar, H.M.
  TITLE     Differential spectrophotometry of purine compounds by means of
            specific enzymes. III. Studies of the enzymes of purine metabolism.
  JOURNAL   J. Biol. Chem. 167 (1947) 461-475.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Rabinowitz, J.C. and Barker, H.A.
  TITLE     Purine fermentation by Clostridium cylindrosporum. II. Purine
            transformations.
  JOURNAL   J. Biol. Chem. 218 (1956) 161-173.
  ORGANISM  Clostridium cylindrosporum
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01487  guanine deaminase
GENES       HSA: 9615(GDA)
            PTR: 472950(GDA)
            MMU: 14544(Gda)
            RNO: 83585(Gda)
            CFA: 484169(GDA)
            GGA: 427253(GDA)
            XLA: 398728(LOC398728)
            DME: Dmel_CG18143
            SCE: YDL238C(GUD1)
            PIC: PICST_36448(GAH1)
            SPO: SPCC1672.03c
            ANI: AN6815.2
            AFM: AFUA_4G03770 AFUA_6G10210
            AOR: AO090011000350 AO090023000256
            CNE: CNN00990
            UMA: UM02943.1
            DDI: DDB_0230211(guaD)
            TET: TTHERM_00646860
            TBR: Tb927.5.4560
            TCR: 504431.100 507951.150
            LMA: LmjF29.0867
            EHI: 2.t00054
            ECO: b2883(guaD)
            ECJ: JW5466(guaD)
            ECE: Z4222(ygfP)
            ECS: ECs3756
            ECC: c3461(ygfP)
            ECI: UTI89_C3268(ygfP)
            ECP: ECP_2877
            ECV: APECO1_3643(ygfP)
            ECW: EcE24377A_3209(guaD)
            ECX: EcHS_A3043(guaD)
            SSN: SSON_3036
            SGL: SG1471
            VFI: VFA0969
            PPR: PBPRA1930 PBPRA2246(guaD)
            PAE: PA0134 PA1521
            PAU: PA14_01660(guaD) PA14_44770(gda1)
            PAP: PSPA7_0210(guaD2) PSPA7_3812(guaD1)
            PPU: PP_4281(gad)
            PST: PSPTO_3663(guaD)
            PSB: Psyr_1812
            PSP: PSPPH_1772(guaD)
            PFL: PFL_1886(guaD)
            PFO: Pfl_1794
            PEN: PSEEN1762(guaD)
            PCR: Pcryo_1143
            ACI: ACIAD3668(guaD)
            SPL: Spea_3243
            CPS: CPS_4872(guaD)
            PAT: Patl_2429
            LPN: lpg1985(gad)
            LPF: lpl1960
            LPP: lpp1966
            NOC: Noc_1166
            HCH: HCH_01091
            CSA: Csal_1786
            AHA: AHA_2175
            CVI: CV_0578
            RSO: RSc2099(guaD)
            REU: Reut_A2429
            REH: H16_A1013(guaD)
            RME: Rmet_0889
            BMA: BMA0463(guaD)
            BMV: BMASAVP1_A2609(guaD)
            BML: BMA10299_A0981(guaD)
            BMN: BMA10247_0166(guaD)
            BXE: Bxe_A0946
            BUR: Bcep18194_A4129 Bcep18194_B2814
            BCN: Bcen_0539
            BAM: Bamb_0881
            BPS: BPSL2541(guaD)
            BPM: BURPS1710b_3023(guaD)
            BPL: BURPS1106A_2978(guaD)
            BPD: BURPS668_2918(guaD)
            BTE: BTH_I1610
            RFR: Rfer_3295
            POL: Bpro_1496
            MPT: Mpe_A0801
            HAR: HEAR0883 HEAR1176
            MMS: mma_0504(guaD)
            EBA: ebA4668(guaD)
            AZO: azo2223(guaD)
            TDN: Tmden_1831
            ABU: Abu_0489
            MLO: mlr5142
            MES: Meso_2838
            SME: SMb20849(guaD2) SMb21293(guaD1)
            ATU: Atu2315(gda)
            ATC: AGR_C_4212
            RET: RHE_CH03130(guaD)
            RLE: RL0523 RL3577(guaD) pRL100068
            BME: BMEI1571
            BMF: BAB1_0383
            BMS: BR0354
            BMB: BruAb1_0380
            BOV: BOV_0370(guaD)
            BJA: blr3880
            BRA: BRADO1602
            BBT: BBta_6453
            CCR: CC_2616
            SIL: SPO2956
            SIT: TM1040_1905 TM1040_3479
            RSP: RSP_1896
            RDE: RD1_2008(guaD)
            ZMO: ZMO0939
            GOX: GOX0898
            RRU: Rru_A0650 Rru_A1302
            SUS: Acid_2535
            BSU: BG13240(gde)
            BLI: BL03735(guaD)
            BLD: BLi01418(guaD)
            BCL: ABC3819(gde)
            BPU: BPUM_1214(guaD)
            LBR: LVIS_1043
            LCA: LSEI_1136
            EFA: EF2431
            OOE: OEOE_1303
            CAC: CAC0282
            CTH: Cthe_2515
            CDF: CD1663(guaD)
            CBO: CBO1288(guaD)
            MSM: MSMEG_1298
            RHA: RHA1_ro03824
            AAU: AAur_1563(guaD)
            NCA: Noca_1141
            SEN: SACE_1260(guaD) SACE_6093(gde)
            AVA: Ava_1577 Ava_2029 Ava_2142
            CHU: CHU_2684(guaD)
            DRA: DR_A0180
            DGE: Dgeo_2606
            MAC: MA3407
            HWA: HQ2049A(guaD) HQ2620A(guaD) HQ3010A(guaD)
            NPH: NP0972A(guaD_1) NP4788A(guaD_3)
STRUCTURES  PDB: 1TIY  1WKQ  2I9U  2OOD  2UZ9  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.3
            ExPASy - ENZYME nomenclature database: 3.5.4.3
            ExplorEnz - The Enzyme Database: 3.5.4.3
            ERGO genome analysis and discovery system: 3.5.4.3
            BRENDA, the Enzyme Database: 3.5.4.3
            CAS: 9033-16-3
///
ENTRY       EC 3.5.4.4                  Enzyme
NAME        adenosine deaminase;
            deoxyadenosine deaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     adenosine aminohydrolase
REACTION    adenosine + H2O = inosine + NH3 [RN:R01560]
ALL_REAC    R01560;
            (other) R02556 R06137
SUBSTRATE   adenosine [CPD:C00212];
            H2O [CPD:C00001]
PRODUCT     inosine [CPD:C00294];
            NH3 [CPD:C00014]
INHIBITOR   Nebularine [CPD:C01736];
            6-Hydroxyl-1,6-dihydropurine ribonucleoside [CPD:C04583]
REFERENCE   1  [PMID:14927650]
  AUTHORS   KAPLAN NO, COLOWICK SP, CIOTTI MM.
  TITLE     Enzymatic deamination of adenosine derivatives.
  JOURNAL   J. Biol. Chem. 194 (1952) 579-91.
  ORGANISM  Aspergillus sp.
REFERENCE   2
  AUTHORS   Powell, J.F. and Hunter, J.R.
  TITLE     Adenosine deaminase and ribosidase in spores of Bacillus cereus.
  JOURNAL   Biochem. J. 62 (1956) 381-387.
  ORGANISM  Bacillus cereus
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01488  adenosine deaminase
GENES       HSA: 100(ADA)
            MMU: 11486(Ada)
            RNO: 24165(Ada)
            CFA: 477236(ADA)
            BTA: 280712(ADA)
            GGA: 415391(RCJMB04_3k8) 418160(RCJMB04_15f15) 419194(ADA)
            XLA: 444167(MGC80635)
            XTR: 496434(ada)
            DRE: 436919(ada)
            SPU: 580201(LOC580201) 586781(LOC586781)
            DME: Dmel_CG10143(Adgf-E) Dmel_CG11994(Ada) Dmel_CG5992(Adgf-A)
                 Dmel_CG5998(Adgf-B) Dmel_CG9345(Adgf-C) Dmel_CG9621(Adgf-D)
            ATH: AT4G04880
            OSA: 4344179
            CME: CMH009C
            SCE: YNL141W(AAH1)
            PIC: PICST_59156(AAH1)
            CGR: CAGL0J05984g
            SPO: SPBC1198.02 SPBC1683.02
            ANI: AN2494.2 AN6078.2
            AFM: AFUA_1G13240 AFUA_2G09150 AFUA_3G15090
            AOR: AO090011000062 AO090011000781 AO090026000211
            UMA: UM00564.1 UM01794.1
            DDI: DDB_0230171
            PFA: PF10_0289
            TET: TTHERM_00703880 TTHERM_00780760 TTHERM_00895970
                 TTHERM_01321550
            LMA: LmjF35.2160
            EHI: 103.t00019 37.t00009
            ECO: b1623(add)
            ECJ: JW1615(add)
            ECE: Z2628(add)
            ECS: ECs2331
            ECC: c2015(add)
            ECI: UTI89_C1811(add)
            ECP: ECP_1567
            ECV: APECO1_706(add)
            ECW: EcE24377A_1831(add)
            ECX: EcHS_A1698
            STY: STY1658(add)
            STT: t1331(add)
            SEC: SC1480(add)
            STM: STM1463(add)
            YPS: YPTB2180(add)
            YPI: YpsIP31758_1878(add)
            YEN: YE2009(add)
            SFL: SF1648(add)
            SFX: S1780(add)
            SFV: SFV_1640(add)
            SSN: SSON_1535(add)
            SBO: SBO_1511(add)
            SDY: SDY_1846(add)
            ECA: ECA2266(add)
            PLU: plu2362(add)
            ENT: Ent638_1825
            SPE: Spro_1204 Spro_2251
            HDU: HD0377(add)
            XCC: XCC0294(add)
            XCB: XC_0304
            XCV: XCV0317(add)
            XAC: XAC0308(add)
            VCH: VC2751
            VCO: VC0395_A2323(add)
            VVU: VV2_0468
            VVY: VVA1020
            VPA: VP0116 VPA1292
            VFI: VF0092 VF0093
            PPR: PBPRA3496 PBPRB1184 PBPRB1379
            PAE: PA0148
            PAU: PA14_01830(add)
            PAP: PSPA7_0226(add)
            PPU: PP_0591(add)
            PPF: Pput_0631 Pput_4685
            PST: PSPTO_0757(add)
            PSB: Psyr_0661
            PSP: PSPPH_4636(add)
            PFL: PFL_0719(add)
            PFO: Pfl_0671
            PEN: PSEEN0674(add)
            PMY: Pmen_3706 Pmen_3801
            PCR: Pcryo_0456
            ACI: ACIAD1245(add)
            ACB: A1S_1137
            SON: SO_4731(add)
            SDN: Sden_3627
            SFR: Sfri_0041
            SAZ: Sama_0085
            SBL: Sbal_0046
            SBM: Shew185_3314
            SLO: Shew_3721
            SPC: Sputcn32_3914
            SSE: Ssed_2715 Ssed_3482 Ssed_3524
            SPL: Spea_3146 Spea_3392
            SHE: Shewmr4_3912
            SHM: Shewmr7_4004
            SHN: Shewana3_4117
            SHW: Sputw3181_0038
            CPS: CPS_1359(add1) CPS_1979(add2)
            PHA: PSHAa0102(add)
            PAT: Patl_2222 Patl_2390 Patl_2420
            PIN: Ping_0692 Ping_1455
            LPN: lpg0580(add)
            LPF: lpl0615(add)
            LPP: lpp0631(add)
            FTU: FTT0939c(add)
            FTF: FTF0939c(add1)
            FTW: FTW_0833(add)
            FTA: FTA_1341 FTA_1342 FTA_1474
            FTN: FTN_0695(add)
            HCH: HCH_01503(add)
            CSA: Csal_1983
            MMW: Mmwyl1_1922 Mmwyl1_2851
            AHA: AHA_0273(add-1) AHA_2653(add-2)
            DNO: DNO_0579(tadA)
            RSO: RSc2098(add)
            REU: Reut_A2428
            REH: H16_A1014(add) H16_B2033
            RME: Rmet_0890
            BMA: BMA0461(add)
            BMV: BMASAVP1_A2607(add)
            BML: BMA10299_A0979(add)
            BMN: BMA10247_0168(add)
            BXE: Bxe_A0947
            BVI: Bcep1808_0939
            BUR: Bcep18194_A4131 Bcep18194_B0389
            BCN: Bcen_0541 Bcen_3107
            BCH: Bcen2424_1020 Bcen2424_5260
            BAM: Bamb_0883 Bamb_4621
            BPS: BPSL2539(add)
            BPM: BURPS1710b_3021(add)
            BPL: BURPS1106A_2976(add)
            BPD: BURPS668_2916(add)
            BTE: BTH_I1612
            BPA: BPP1038(add)
            BBR: BB1254(add)
            RFR: Rfer_3297
            POL: Bpro_1487
            PNA: Pnap_1040
            AAV: Aave_1138
            VEI: Veis_1083 Veis_2520
            MPT: Mpe_A0809
            MMS: mma_1581
            AZO: azo0236(add)
            WSU: WS0737
            GUR: Gura_2399 Gura_4130
            BBA: Bd3476(add)
            ADE: Adeh_0098 Adeh_1249
            AFW: Anae109_0100 Anae109_2517
            MXA: MXAN_1519(add)
            MLO: mll3163
            MES: Meso_3659
            SME: SMc04120(add)
            SMD: Smed_3344
            ATU: Atu0136(add)
            ATC: AGR_C_218
            RET: RHE_CH00197(add)
            RLE: RL0206
            RPC: RPC_4230
            CCR: CC_3180
            SIL: SPO2927(add)
            RSP: RSP_1597(add)
            RSH: Rsph17029_0250
            RSQ: Rsph17025_0278
            JAN: Jann_2984
            PDE: Pden_2220
            MMR: Mmar10_1236
            HNE: HNE_1938(add)
            ZMO: ZMO0655(add) ZMO0971(add)
            SAL: Sala_2009
            SWI: Swit_2485
            GOX: GOX1436
            RRU: Rru_A0766
            ABA: Acid345_0045 Acid345_3059
            SUS: Acid_7334
            BCY: Bcer98_3058
            SSP: SSP2398
            LLA: L87453(add)
            LLC: LACR_0321
            LLM: llmg_0299(add)
            SAG: SAG0538
            SAN: gbs0583
            SAK: SAK_0688(add)
            SMU: SMU.1295(add)
            STC: str0750(add)
            STL: stu0750(add)
            LJO: LJ1639
            LAC: LBA1535
            LSA: LSA0086(add)
            LDB: Ldb1463(add)
            LBU: LBUL_1358
            LBR: LVIS_0278
            LCA: LSEI_2207
            LRE: Lreu_1235
            EFA: EF0171(add)
            CAC: CAC3005(add)
            CPE: CPE2506(add)
            CPF: CPF_2829(add)
            CPR: CPR_2515(add)
            CDF: CD1747(add)
            CBO: CBO0991(add)
            CBA: CLB_1030(add)
            CBH: CLC_1043(add)
            CBF: CLI_1072(add)
            CBE: Cbei_0513
            CKL: CKL_0833(add)
            AMT: Amet_2309
            CSC: Csac_1815
            MFL: Mfl215
            MTU: Rv3313c(add)
            MBO: Mb3342c(add)
            MBB: BCG_3379c(add)
            MLE: ML0700(add)
            MPA: MAP3438c(add)
            MAV: MAV_4294(add)
            MSM: MSMEG_1676(add)
            MVA: Mvan_1592
            MGI: Mflv_4841
            MMC: Mmcs_1233
            MKM: Mkms_1250
            MJL: Mjls_1259
            CJK: jk1687(add)
            NFA: nfa9530
            RHA: RHA1_ro06027(add1) RHA1_ro06251(add2)
            SCO: SCO2546(SCC77.13c) SCO4644(add) SCO4901(2SCK8.27)
                 SCO5662(SC6A9.05) SCO7268(add)
            SMA: SAV1165(add1) SAV2595(add2) SAV3358(add3) SAV4906(add4)
                 SAV5577(add5)
            LXX: Lxx04660(add) Lxx13430(add)
            CMI: CMM_0659(addB)
            ART: Arth_0907 Arth_1145
            AAU: AAur_1117(add) AAur_1261(add)
            PAC: PPA2273
            NCA: Noca_0674 Noca_1355 Noca_3533
            TFU: Tfu_2563 Tfu_2662
            FRA: Francci3_0534 Francci3_0686 Francci3_1770 Francci3_4458
            FAL: FRAAL1027 FRAAL1195(add) FRAAL1473 FRAAL6786
            ACE: Acel_0264
            KRA: Krad_0670 Krad_1299 Krad_2063 Krad_3450 Krad_3645 Krad_3935
                 Krad_4351
            SEN: SACE_1513(add) SACE_2180(add) SACE_3230(add) SACE_3612(add)
                 SACE_6573(add)
            STP: Strop_0815 Strop_1779 Strop_3474
            TPA: TP0045
            TDE: TDE0188
            LIL: LA3783
            LIC: LIC10459(add)
            LBJ: LBJ_0617(add)
            LBL: LBL_2462(add)
            SYC: syc1695_c
            SYF: Synpcc7942_2410
            CYA: CYA_1916
            CYB: CYB_2006
            TEL: tlr1233
            GVI: glr0121
            ANA: all4418
            AVA: Ava_1344
            TER: Tery_3281
            SRU: SRU_0673(add)
            CPH: Cpha266_1916
            PLT: Plut_1524
            DEB: DehaBAV1_0003
            RRS: RoseRS_2217 RoseRS_2867
            RCA: Rcas_2430 Rcas_3366
STRUCTURES  PDB: 1A4L  1A4M  1ADD  1FKW  1FKX  1KRM  1NDV  1NDW  1NDY  1NDZ  
                 1O5R  1QXL  1UIO  1UIP  1UML  1V79  1V7A  1VFL  1W1I  1WXY  
                 1WXZ  2ADA  2AMX  2BGN  2E1W  2PGF  2PGR  2QVN  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.4
            ExPASy - ENZYME nomenclature database: 3.5.4.4
            ExplorEnz - The Enzyme Database: 3.5.4.4
            ERGO genome analysis and discovery system: 3.5.4.4
            BRENDA, the Enzyme Database: 3.5.4.4
            CAS: 9026-93-1
///
ENTRY       EC 3.5.4.5                  Enzyme
NAME        cytidine deaminase;
            cytosine nucleoside deaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     cytidine aminohydrolase
REACTION    cytidine + H2O = uridine + NH3 [RN:R01878]
ALL_REAC    R01878;
            (other) R02485 R06137
SUBSTRATE   cytidine [CPD:C00475];
            H2O [CPD:C00001]
PRODUCT     uridine [CPD:C00299];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Roberts, D.W.A.
  TITLE     The wheat leaf phosphatases. II. Pathway of hydrolysis of some
            nucleotides at pH 5.5.
  JOURNAL   J. Biol. Chem. 222 (1956) 259-270.
  ORGANISM  Triticum aestivum [GN:etae]
REFERENCE   2  [PMID:15421968]
  AUTHORS   WANG TP, SABLE HZ, LAMPEN JO.
  TITLE     Enzymatic deamination of cytosine nucleosides.
  JOURNAL   J. Biol. Chem. 184 (1950) 17-28.
  ORGANISM  rabbit
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K01489  cytidine deaminase
GENES       HSA: 57379(AICDA) 978(CDA)
            PTR: 473404(AICDA)
            MMU: 11628(Aicda) 72269(Cda)
            RNO: 399679(aicda)
            CFA: 442983(AICDA) 487393(CDA)
            BTA: 539888(AICDA)
            GGA: 418257(AICDA) 771849(CDA)
            DRE: 402979(cda) 493784(aicda)
            DME: Dmel_CG8349 Dmel_CG8360
            CEL: C47D2.2(cdd-1) F49E8.4(cdd-2)
            ATH: AT2G19570(CDA1)
            CME: CMR254C
            SCE: YLR245C(CDD1)
            AGO: AGOS_AGL123W
            PIC: PICST_39066
            SPO: SPAC1556.04c(pcd1)
            AFM: AFUA_8G02770
            CNE: CNC04940
            DDI: DDB_0230205
            TET: TTHERM_00389850
            TBR: Tb09.160.1680
            TCR: 510053.60 511321.23
            LMA: LmjF17.0360
            EHI: 14.t00001
            ECO: b2143(cdd)
            ECJ: JW2131(cdd)
            ECE: Z3398(cdd)
            ECS: ECs3035
            ECC: c2675(cdd)
            ECI: UTI89_C2416(cdd)
            ECP: ECP_2182
            ECV: APECO1_4407(cdd)
            ECW: EcE24377A_2438(cdd)
            ECX: EcHS_A2277(cdd)
            STY: STY2413(cdd)
            STT: t0672(cdd)
            SPT: SPA0668(cdd)
            SEC: SC2200(cdd)
            STM: STM2183(cdd)
            YPE: YPO1512(cdd)
            YPK: y2657(cdd)
            YPM: YP_1402(cdd)
            YPA: YPA_0807
            YPN: YPN_2467
            YPS: YPTB1527(cdd)
            YPI: YpsIP31758_2462(cdd)
            SFL: SF2228(cdd)
            SFX: S2357(cdd)
            SFV: SFV_2218(cdd)
            SSN: SSON_2199(cdd)
            SBO: SBO_0998(cdd)
            SDY: SDY_2144(cdd)
            ECA: ECA2830(cdd)
            PLU: plu1547(cdd)
            SGL: SG0968
            SPE: Spro_1568
            HIT: NTHI1816(cdd)
            HIP: CGSHiEE_04285
            HIQ: CGSHiGG_00405
            HDU: HD0979(cdd)
            HSO: HS_1257(cdd)
            PMU: PM0259(cdd)
            MSU: MS1835(cdd)
            APL: APL_1343(cdd)
            ASU: Asuc_0425
            VCH: VC1231
            VCO: VC0395_A0852(cdd)
            VVU: VV1_2379
            VVY: VV1962
            VPA: VP1298
            VFI: VF1485
            PPR: PBPRA1689
            SON: SO_2791(cdd)
            SDN: Sden_2288
            SFR: Sfri_1637
            SBM: Shew185_1679
            SSE: Ssed_2618
            SPL: Spea_2488
            SHE: Shewmr4_2411
            SHM: Shewmr7_2481
            SHN: Shewana3_2573
            CPS: CPS_1969(cdd)
            PHA: PSHAb0315(cdd)
            PAT: Patl_0790
            LPN: lpg1435(cdd)
            LPF: lpl1606
            LPP: lpp1390
            FTU: FTT1327(cdd)
            FTF: FTF1327(cdd)
            FTW: FTW_1493(cdd)
            FTL: FTL_1488
            FTH: FTH_1442(cdd)
            FTA: FTA_1573(cdd)
            FTN: FTN_0651(cdd)
            CSA: Csal_0827
            AHA: AHA_1894(cdd)
            CVI: CV_0127 CV_2570(cdd) CV_3471
            BMA: BMAA0115(cdd)
            BMV: BMASAVP1_1279(cdd)
            BMN: BMA10247_A0139(cdd)
            BXE: Bxe_B0741
            BUR: Bcep18194_C6661
            BCN: Bcen_1590
            BCH: Bcen2424_6241
            BPS: BPSS1959(cdd)
            BPM: BURPS1710b_A1065(cdd)
            BPL: BURPS1106A_A2661
            BPD: BURPS668_A2803(cdd)
            BTE: BTH_II0413(cdd)
            MPT: Mpe_A0536
            MMS: mma_2008(cumB2)
            AZO: azo1588(cumB)
            PCA: Pcar_2536
            BBA: Bd2449(cdd)
            ADE: Adeh_0620
            MXA: MXAN_5706(cdd)
            SAT: SYN_03352
            MLO: mlr3158
            MES: Meso_3655
            SME: SMc04124(cdd)
            ATU: Atu0130(cdd)
            ATC: AGR_C_209
            RET: RHE_CH00191(cdd)
            RLE: RL0200(cdd)
            RPA: RPA1101
            RPB: RPB_4270
            RPC: RPC_4804
            RPD: RPD_4168
            RPE: RPE_4768
            CCR: CC_3012
            SIL: SPO2930(cdd)
            SIT: TM1040_1572
            RSP: RSP_1594(cdd) RSP_2267
            JAN: Jann_2987
            RDE: RD1_1993 RD1_3980(cdd)
            HNE: HNE_1295(cdd)
            ZMO: ZMO0864(cdd)
            NAR: Saro_0145
            ELI: ELI_10950
            SUS: Acid_5234
            BSU: BG10477(cdd)
            BHA: BH1366(cdd)
            BAN: BA1895(cdd-1) BA2855 BA4525(cdd-2)
            BAR: GBAA1895(cdd-1) GBAA2855 GBAA4525(cdd-2)
            BAA: BA_2399 BA_3376 BA_4972
            BAT: BAS1757 BAS2661 BAS4200
            BCE: BC1823 BC4298
            BCA: BCE_1978(cdd) BCE_2885 BCE_4381(cdd)
            BCZ: BCZK1706(cdd) BCZK4048(cdd)
            BTK: BT9727_1735(cdd) BT9727_4038(cdd)
            BTL: BALH_1677(cdd) BALH_3891(cdd)
            BLI: BL03673(cdd)
            BLD: BLi02721(cdd)
            BCL: ABC1680(cdd)
            BAY: RBAM_023600(cdd)
            BPU: BPUM_1737 BPUM_2263(cdd)
            OIH: OB1751(cdd)
            GKA: GK2489
            GTN: GTNG_2426(cdd)
            SAU: SA1397(cdd)
            SAV: SAV1568(cdd)
            SAM: MW1520(cdd)
            SAR: SAR1645(cdd)
            SAS: SAS1506
            SAC: SACOL1625(cdd)
            SAB: SAB1440c(cdd)
            SAA: SAUSA300_1528(cdd)
            SAO: SAOUHSC_01670
            SEP: SE1255
            SER: SERP1135(cdd)
            SHA: SH1348(cdd)
            SSP: SSP1188
            LMO: lmo1463
            LMF: LMOf2365_1482(cdd)
            LIN: lin1500
            LWE: lwe1478(cdd)
            LLA: L62931(cdd)
            LLC: LACR_1528
            LLM: llmg_1063(cdd)
            SPY: SPy_1230(cdd)
            SPZ: M5005_Spy_0943(cdd)
            SPM: spyM18_1181(cdd)
            SPG: SpyM3_0869(cdd)
            SPS: SPs1069
            SPH: MGAS10270_Spy1057(cdd)
            SPI: MGAS10750_Spy1092(cdd) MGAS10750_Spy1706
            SPJ: MGAS2096_Spy1002(cdd)
            SPK: MGAS9429_Spy1046(cdd)
            SPF: SpyM50855(cdd)
            SPA: M6_Spy0932
            SPB: M28_Spy0915(cdd)
            SPN: SP_0844
            SPR: spr0746(cdd) spr1188(cdd)
            SPD: SPD_0738(cdd-1) SPD_1164(cdd-2)
            SAG: SAG0953(cdd)
            SAN: gbs0941
            SAK: SAK_1048(cdd)
            SMU: SMU.1122(cdd)
            STC: str0807(cdd)
            STL: stu0807(cdd)
            STE: STER_0855
            SSA: SSA_1037(cdd)
            SSU: SSU05_1084
            SSV: SSU98_1095
            SGO: SGO_0981 SGO_1081(cdd)
            LSA: LSA0335
            LDB: Ldb1252(cdd)
            LBU: LBUL_1170
            LBR: LVIS_0283
            LCA: LSEI_1516
            EFA: EF0175(cdd)
            OOE: OEOE_1731
            LME: LEUM_0443
            STH: STH533
            CAC: CAC1544 CAC2609
            CPE: CPE2016
            CPF: CPF_2273(cdd)
            CPR: CPR_1988(cdd)
            CTC: CTC02019
            CNO: NT01CX_0044
            CDF: CD2438(cdd)
            CBO: CBO0253 CBO2947(cdd)
            CBA: CLB_2910(cdd)
            CBH: CLC_2842(cdd)
            CBF: CLI_2999(cdd)
            CKL: CKL_0915(cdd)
            CHY: CHY_1553(cdd)
            DSY: DSY3106
            DRM: Dred_2480
            SWO: Swol_1562
            CSC: Csac_2319
            TTE: TTE0462(cdd)
            MTA: Moth_0599
            MGE: MG_052(cdd)
            MPN: MPN065(cdd)
            MPU: MYPU_3790(cdd)
            MPE: MYPE1060(cdd)
            MGA: MGA_0361(cdd)
            MMO: MMOB3470(cdd)
            MHY: mhp225(cdd)
            MHJ: MHJ_0153(cdd)
            MHP: MHP7448_0157(cdd)
            MSY: MS53_0388(cdd)
            UUR: UU531(cdd)
            MFL: Mfl143
            MTU: Rv3315c(cdd)
            MTC: MT3416(cdd)
            MBO: Mb3344c(cdd)
            MBB: BCG_3381c(cdd)
            MLE: ML2174(cdd)
            MPA: MAP3440c(cdd)
            MAV: MAV_4296(cdd)
            MSM: MSMEG_1673(cdd)
            MMC: Mmcs_1231 Mmcs_3453
            NFA: nfa9500
            RHA: RHA1_ro06249
            SCO: SCO4889(2SCK8.15) SCO5680(SC5H4.04c)
            SMA: SAV3366(cdd2)
            LXX: Lxx04640(cdd)
            AAU: AAur_1257(cdd)
            PAC: PPA1730
            FRA: Francci3_0684
            FAL: FRAAL0417 FRAAL1193(cdd) FRAAL2012
            SEN: SACE_6576(cdd)
            RXY: Rxyl_1507
            RBA: RB11882(cdd)
            BGA: BG0636(cdd)
            BAF: BAPKO_0656(cdd)
            TDE: TDE1931(cdd)
            LIL: LA3969
            SYW: SYNW1811
            SYD: Syncc9605_0657
            BTH: BT_1539
            BFR: BF1494
            BFS: BF1427(cdd)
            PGI: PG0030
            GFO: GFO_2890(cdd)
            FPS: FP1386(cdd)
            DRA: DR_2177
            DGE: Dgeo_1286
            TTH: TTC0383
            TTJ: TTHA0735
            TMA: TM0846
            HAL: VNG0896G(cda)
            HMA: rrnAC0446(cdd)
            HWA: HQ2646A(cdd)
            NPH: NP3512A(cdd)
            APE: APE_1038.1
            SMR: Smar_0069
            HBU: Hbut_0828
            MSE: Msed_0025
            PAI: PAE0794
            PIS: Pisl_1085
            PCL: Pcal_0011
            PAS: Pars_0045
STRUCTURES  PDB: 1AF2  1ALN  1CTT  1CTU  1JTK  1MQ0  1R5T  1UWZ  1UX0  1UX1  
                 1ZAB  2D30  2FR5  2FR6  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.5
            ExPASy - ENZYME nomenclature database: 3.5.4.5
            ExplorEnz - The Enzyme Database: 3.5.4.5
            ERGO genome analysis and discovery system: 3.5.4.5
            BRENDA, the Enzyme Database: 3.5.4.5
            CAS: 9025-06-3
///
ENTRY       EC 3.5.4.6                  Enzyme
NAME        AMP deaminase;
            adenylic acid deaminase;
            AMP aminase;
            adenylic deaminase;
            adenylate deaminase;
            5-AMP deaminase;
            adenosine 5-monophosphate deaminase;
            5-adenylate deaminase;
            adenyl deaminase;
            5-adenylic acid deaminase;
            adenosine monophosphate deaminase;
            adenylate aminohydrolase;
            adenylate desaminase;
            adenosine 5-phosphate aminohydrolase;
            5-adenylate deaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     AMP aminohydrolase
REACTION    AMP + H2O = IMP + NH3 [RN:R00181]
ALL_REAC    R00181;
            (other) R06137
SUBSTRATE   AMP [CPD:C00020];
            H2O [CPD:C00001]
PRODUCT     IMP [CPD:C00130];
            NH3 [CPD:C00014]
COMMENT     cf. EC 3.5.4.17 adenosine-phosphate deaminase.
REFERENCE   1
  AUTHORS   Kalckar, H.M.
  TITLE     Differential spectrophotometry of purine compounds by means of
            specific enzymes. III. Studies of the enzymes of purine metabolism.
  JOURNAL   J. Biol. Chem. 167 (1947) 461-475.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:13463019]
  AUTHORS   LEE YP.
  TITLE     5'-Adenylic acid deaminase. I. Isolation of the crystalline enzyme
            from rabbit skeletal muscle.
  JOURNAL   J. Biol. Chem. 227 (1957) 987-92.
  ORGANISM  rabbit
REFERENCE   3  [PMID:13463020]
  AUTHORS   LEE YP.
  TITLE     5'-Adenylic acid deaminase. II. Homogeneity and physicochemical
            properties.
  JOURNAL   J. Biol. Chem. 227 (1957) 993-8.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:13463021]
  AUTHORS   LEE YP.
  TITLE     5'-Adenylic acid deaminase. III. Properties and kinetic studies.
  JOURNAL   J. Biol. Chem. 227 (1957) 999-1007.
  ORGANISM  rabbit
REFERENCE   5  [PMID:13563464]
  AUTHORS   MENDICINO J, MUNTZ JA.
  TITLE     The activating effect of adenosine triphosphate on brain adenylic
            deaminase.
  JOURNAL   J. Biol. Chem. 233 (1958) 178-83.
  ORGANISM  dog [GN:cfa]
REFERENCE   6
  AUTHORS   Turner, D.H. and Turner, J.F.
  TITLE     Adenylic deaminase of pea seeds.
  JOURNAL   Biochem. J. 79 (1961) 143-147.
  ORGANISM  Pisum sativum
REFERENCE   7
  AUTHORS   Weil-Malherbe, W. and Green, R.H.
  TITLE     Ammonia formation in brain. 2. Brain adenylic deaminase.
  JOURNAL   Biochem. J. 61 (1955) 218-224.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01490  AMP deaminase
GENES       HSA: 270(AMPD1) 271(AMPD2) 272(AMPD3)
            MMU: 109674(Ampd2) 11717(Ampd3) 229665(Ampd1)
            RNO: 25028(Ampd1) 25095(Ampd3)
            CFA: 479913(AMPD2) 606901(AMPD1)
            GGA: 423041(AMPD3)
            DRE: 333997(ampd3) 393867(zgc:77905)
            SPU: 587814(LOC587814)
            OSA: 4344386
            CME: CMI114C
            SCE: YML035C(AMD1)
            AGO: AGOS_ABR204C
            PIC: PICST_40926(AMD1)
            CGR: CAGL0G07425g
            SPO: SPBC106.04(ada1)
            ANI: AN8872.2
            AFM: AFUA_8G02860
            AOR: AO090010000778
            CNE: CNC03570
            UMA: UM04622.1
            DDI: DDB_0191089(amdA)
            PFA: MAL13P1.146
            CPV: cgd4_1890
            CHO: Chro.40214
            TAN: TA05645
            TET: TTHERM_00171830
            TBR: Tb09.160.5250 Tb09.211.1320 Tb11.01.7390
            TCR: 410589.10 506885.390 508273.10
            LMA: LmjF04.0280 LmjF32.2550 LmjF35.4800
            EHI: 110.t00025
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.6
            ExPASy - ENZYME nomenclature database: 3.5.4.6
            ExplorEnz - The Enzyme Database: 3.5.4.6
            ERGO genome analysis and discovery system: 3.5.4.6
            BRENDA, the Enzyme Database: 3.5.4.6
            CAS: 9025-10-9
///
ENTRY       EC 3.5.4.7                  Enzyme
NAME        ADP deaminase;
            adenosine diphosphate deaminase;
            adenosinepyrophosphate deaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     ADP aminohydrolase
REACTION    ADP + H2O = IDP + NH3 [RN:R00123]
ALL_REAC    R00123;
            (other) R06137
SUBSTRATE   ADP [CPD:C00008];
            H2O [CPD:C00001]
PRODUCT     IDP [CPD:C00104];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Deutsch, A. and Nilsson, R.
  TITLE     On the dephosphorylation and deamination of adenosine triphosphate
            by actomyosin gel.
  JOURNAL   Acta Chem. Scand. 8 (1954) 1898-1906.
  ORGANISM  rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.7
            ExPASy - ENZYME nomenclature database: 3.5.4.7
            ExplorEnz - The Enzyme Database: 3.5.4.7
            ERGO genome analysis and discovery system: 3.5.4.7
            BRENDA, the Enzyme Database: 3.5.4.7
            CAS: 9027-79-6
///
ENTRY       EC 3.5.4.8                  Enzyme
NAME        aminoimidazolase;
            4-aminoimidazole hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     4-aminoimidazole aminohydrolase
REACTION    4-aminoimidazole + H2O = unidentified product + NH3
ALL_REAC    (other) R04731 R06137
SUBSTRATE   4-aminoimidazole [CPD:C05239];
            H2O [CPD:C00001]
PRODUCT     unidentified product;
            NH3 [CPD:C00014]
COFACTOR    Iron [CPD:C00023]
COMMENT     The product of the reaction is rapidly converted into
            formiminoglycine. Requires Fe2+.
REFERENCE   1
  AUTHORS   Rabinowitz, J.C. and Pricer, W.E.
  TITLE     Purine fermentation by Clostridium cylindrosporum. V.
            Formiminoglycine.
  JOURNAL   J. Biol. Chem. 222 (1956) 537-554.
  ORGANISM  Clostridium cylindrosporum
PATHWAY     PATH: map00230  Purine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.8
            ExPASy - ENZYME nomenclature database: 3.5.4.8
            ExplorEnz - The Enzyme Database: 3.5.4.8
            ERGO genome analysis and discovery system: 3.5.4.8
            BRENDA, the Enzyme Database: 3.5.4.8
            CAS: 9025-17-6
///
ENTRY       EC 3.5.4.9                  Enzyme
NAME        methenyltetrahydrofolate cyclohydrolase;
            Citrovorum factor cyclodehydrase;
            cyclohydrolase;
            formyl-methenyl-methylenetetrahydrofolate synthetase (combined)
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     5,10-methenyltetrahydrofolate 5-hydrolase (decyclizing)
REACTION    5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate
            [RN:R01655]
ALL_REAC    R01655;
            (other) R00943
SUBSTRATE   5,10-methenyltetrahydrofolate [CPD:C00445];
            H2O [CPD:C00001]
PRODUCT     10-formyltetrahydrofolate [CPD:C00234]
COMMENT     In eukaryotes, the enzyme occurs as a trifunctional enzyme that also
            has methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5) and
            formate---tetrahydrofolate ligase (EC 6.3.4.3) activity. In some
            prokaryotes, it occurs as a bifunctional enzyme that also has
            dehydrogenase (EC 1.5.1.5) activity or formimidoyltetrahydrofolate
            cyclodeaminase (EC 4.3.1.4) activity.
REFERENCE   1
  AUTHORS   Rabinowitz, J.C. and Pricer, W.E.
  TITLE     The enzymatic synthesis of N10-formyltetrahydrofolic acid and its
            role in ATP formation during formiminoglycine degradation.
  JOURNAL   J. Am. Chem. Soc. 78 (1956) 4176-4178.
  ORGANISM  Clostridium cylindrosporum, Clostridium acidi-urici
REFERENCE   2
  AUTHORS   Tabor, H. and Wyngarden, L.
  TITLE     The enzymatic formation of formiminotetrahydrofolic acid,
            5,10-methenyltetrahydrofolic acid, and 10-formyltetrahydrofolic acid
            in the metabolism of formiminoglutamic acid.
  JOURNAL   J. Biol. Chem. 234 (1959) 1830-1849.
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
            PATH: map00670  One carbon pool by folate
ORTHOLOGY   KO: K01491  methenyltetrahydrofolate cyclohydrolase
GENES       HSA: 10797(MTHFD2) 25902(MTHFD1L) 4522(MTHFD1)
            MMU: 108156(Mthfd1) 17768(Mthfd2) 270685(Mthfd1l)
            RNO: 313410(RGD1564040_predicted) 64300(Mthfd1)
            CFA: 476245(MTHFD1L)
            GGA: 423508(RCJMB04_29j22) 426126(RCJMB04_12b8)
            XLA: 380266(mthfd1) 446641(mthfd2)
            XTR: 493369(TNeu036b14.1)
            DRE: 260441(mthfd1)
            SPU: 588966(LOC588966)
            DME: Dmel_CG4067(pug)
            CEL: K07E3.3(dao-3)
            ATH: AT3G12290
            OSA: 4328117 4337829
            CME: CMR167C
            SCE: YBR084W(MIS1) YGR204W(ADE3)
            AGO: AGOS_ACL121C AGOS_AER178W
            PIC: PICST_80013(MIS1)
            CAL: CaO19_7534(CaO19.7534)
            CGR: CAGL0M01694g
            SPO: SPBC2G2.08 SPBC839.16
            CNE: CNG00590
            UMA: UM03320.1
            DDI: DDB_0230115
            TET: TTHERM_00339820
            TCR: 508207.240 509509.20 511517.60 511741.50
            LMA: LmjF26.0320 LmjF30.2600
            ECO: b0529(folD)
            ECJ: JW0518(folD)
            ECE: Z0684(folD)
            ECS: ECs0591
            ECC: c0645(folD)
            ECI: UTI89_C0559(folD)
            ECP: ECP_0590
            ECV: APECO1_1486(folD)
            ECW: EcE24377A_0570(folD)
            ECX: EcHS_A0603(folD)
            STY: STY0588(folD)
            STT: t2321(folD)
            SPT: SPA2183(folD)
            SEC: SC0581(folD)
            STM: STM0542(folD)
            YPE: YPO2824(folD)
            YPK: y1110(folD)
            YPM: YP_0855(folD)
            YPA: YPA_2565
            YPN: YPN_1020
            YPP: YPDSF_2708
            YPS: YPTB1037(folD)
            YPI: YpsIP31758_3012(folD)
            SFL: SF0460(folD)
            SFX: S0468(folD)
            SFV: SFV_0487(folD)
            SSN: SSON_0489(folD)
            SBO: SBO_0414(folD)
            SDY: SDY_0281(folD)
            ECA: ECA3149(folD)
            PLU: plu4317(folD)
            BUC: BU486(folD)
            BAS: BUsg470(folD)
            BAB: bbp430(folD)
            BCC: BCc_305(folD)
            WBR: WGLp242(folD)
            SGL: SG0706
            ENT: Ent638_0986
            BFL: Bfl305(folD)
            BPN: BPEN_313(folD)
            HIN: HI0609(folD)
            HIT: NTHI0864(folD)
            HDU: HD1108(folD)
            HSO: HS_1221(folD)
            PMU: PM1933(folD)
            MSU: MS1851(folD) MS1852(folD)
            APL: APL_0897(folD)
            ASU: Asuc_0763
            XFA: XF2431
            XFT: PD1449(folD)
            XCC: XCC2185(folD)
            XCB: XC_1933
            XCV: XCV2487(folD)
            XAC: XAC2289(folD)
            XOO: XOO2193(folD)
            XOM: XOO_2061(XOO2061)
            VCH: VC1942
            VVU: VV1_2022
            VVY: VV2391
            VPA: VP0879
            VFI: VF1770
            PPR: PBPRA2641
            PAE: PA1796(folD)
            PPU: PP_1945(folD-1) PP_2265(folD-2)
            PST: PSPTO_2453(folD-1) PSPTO_3733(folD-2)
            PSB: Psyr_1743 Psyr_2225
            PSP: PSPPH_1687(folD1) PSPPH_2961(folD2)
            PFL: PFL_3992
            PFO: Pfl_3699
            PEN: PSEEN1862(folD)
            PMY: Pmen_2048 Pmen_3458
            PAR: Psyc_0673(folD)
            PCR: Pcryo_0640
            PRW: PsycPRwf_1815
            ACI: ACIAD2553(folD) ACIAD2847(folD)
            SON: SO_1792(folD)
            SDN: Sden_2497
            SBL: Sbal_1602
            SBM: Shew185_1591
            SPC: Sputcn32_1488
            SHN: Shewana3_2663
            SHW: Sputw3181_2613
            ILO: IL1008(folD)
            CPS: CPS_3133(folD1) CPS_3791(folD2)
            PHA: PSHAa2064(folD)
            PAT: Patl_3139
            SDE: Sde_1920
            CBU: CBU_0312(folD)
            LPN: lpg1297(folD)
            LPF: lpl1260(folD)
            LPP: lpp1261(folD)
            MCA: MCA0507(fchA)
            FTU: FTT0892(folD)
            FTF: FTF0892(folD)
            FTL: FTL_0394
            FTH: FTH_0386
            FTA: FTA_0417
            FTN: FTN_0417(folD)
            TCX: Tcr_0723 Tcr_1343
            NOC: Noc_2248
            HCH: HCH_02155(folD)
            MMW: Mmwyl1_3759
            AHA: AHA_1854
            DNO: DNO_1298(folD)
            BCI: BCI_0122(folD)
            RMA: Rmag_0840
            VOK: COSY_0765(folD)
            NMA: NMA0354(folD)
            NMC: NMC2056(folD)
            NGO: NGO1999(folD)
            CVI: CV_1925(folD)
            RSO: RSc1596(folD)
            REU: Reut_A1299
            RME: Rmet_1192
            BMA: BMA1724(folD)
            BXE: Bxe_A1536
            BVI: Bcep1808_2220
            BUR: Bcep18194_A5446
            BCN: Bcen_5937
            BCH: Bcen2424_2140
            BAM: Bamb_2177
            BPS: BPSL2304(folD)
            BPM: BURPS1710b_2749(folD)
            BPL: BURPS1106A_2672(folD)
            BPD: BURPS668_2616(folD)
            BTE: BTH_I1861
            PNU: Pnuc_0731
            BPE: BP0990(folD) BP2522(folD)
            BPA: BPP1459(folD) BPP3509(folD)
            BBR: BB2533(folD)
            RFR: Rfer_2209
            POL: Bpro_2675
            PNA: Pnap_1778
            AAV: Aave_2459
            AJS: Ajs_2128
            VEI: Veis_1922
            MPT: Mpe_A3258
            HAR: HEAR0745(folD)
            NEU: NE0362(folD)
            NET: Neut_1607
            NMU: Nmul_A0357
            DAR: Daro_0448
            TBD: Tbd_0689
            MFA: Mfla_0073
            HPY: HP0577(folD)
            HPA: HPAG1_0556
            HHE: HH1366(folD)
            HAC: Hac_1435(folD)
            WSU: WS1345(folD)
            TDN: Tmden_1113
            CJE: Cj0855(folD)
            CJR: CJE0942(folD)
            CJU: C8J_0802(folD)
            CFF: CFF8240_1174
            CCV: CCV52592_0799 CCV52592_2154
            CHA: CHAB381_1036
            ABU: Abu_0637(folD)
            NIS: NIS_0711(folD)
            SUN: SUN_0665(folD)
            GSU: GSU0215(folD-1) GSU0862(folD-2)
            GME: Gmet_0247 Gmet_1162
            PCA: Pcar_2461
            PPD: Ppro_0480
            DVU: DVU0323(folD)
            DDE: Dde_0296
            LIP: LI0875
            BBA: Bd3295(folD)
            DPS: DP1901
            ADE: Adeh_1247
            MXA: MXAN_2226(folD) MXAN_3032(folD)
            SAT: SYN_02873
            SFU: Sfum_2686
            RPR: RP515(folD)
            RTY: RT0501(folD)
            RCO: RC0636(folD)
            RFE: RF_0699(folD)
            RBE: RBE_0983(folD)
            WOL: WD0555(folD)
            WBM: Wbm0073
            AMA: AM179(folD)
            APH: APH_0175(folD)
            ERU: Erum6730(folD)
            ERW: ERWE_CDS_07060(folD)
            ERG: ERGA_CDS_06980(folD)
            ECN: Ecaj_0680
            ECH: ECH_0324(folD)
            NSE: NSE_0821(folD)
            PUB: SAR11_0307(folD)
            MLO: mll6921 mlr6508
            MES: Meso_0152
            PLA: Plav_1372
            SME: SMc02604(folD1) SMc03059(folD2)
            SMD: Smed_0290 Smed_2095
            ATU: Atu0589(folD)
            ATC: AGR_C_1042(folD)
            RET: RHE_CH00694(folDch) RHE_PE00416(folDe)
            RLE: RL0743
            BME: BMEII0510
            BMF: BAB2_0457(folD)
            BMS: BRA0781(folD)
            BMB: BruAb2_0451(folD)
            BJA: bll0549(folD)
            BRA: BRADO0277(folD)
            BBT: BBta_0269(folD)
            RPA: RPA0413
            RPB: RPB_0108
            RPC: RPC_0059
            RPD: RPD_0694
            RPE: RPE_0047
            NWI: Nwi_0480
            BHE: BH03940(folD)
            BQU: BQ02960(folD)
            BBK: BARBAKC583_0297(folD)
            XAU: Xaut_4086
            CCR: CC_1217
            SIL: SPO1559 SPO1560(folD) SPO3101
            SIT: TM1040_2356
            RSP: RSP_0661
            RSQ: Rsph17025_0571
            JAN: Jann_0983
            RDE: RD1_2105(folD) RD1_4236(folD) RD1_4237(folD)
            PDE: Pden_2614 Pden_4905
            MMR: Mmar10_0051
            ZMO: ZMO0914(folD)
            NAR: Saro_3300
            SAL: Sala_3097
            SWI: Swit_0940 Swit_2064 Swit_2872
            ELI: ELI_11530
            GOX: GOX0792
            GBE: GbCGDNIH1_0051
            RRU: Rru_A0557
            MAG: amb4374
            MGM: Mmc1_3712
            ABA: Acid345_4424
            SUS: Acid_4780
            BSU: BG11711(folD)
            BHA: BH2784(folD)
            BAN: BA4405(folD)
            BAR: GBAA4405(folD)
            BAA: BA_4857
            BAT: BAS4085
            BCE: BC4180
            BCA: BCE_4254(folD)
            BCZ: BCZK3934(folD)
            BCY: Bcer98_2874
            BTK: BT9727_3923(folD)
            BTL: BALH_3789(folD)
            BLI: BL01527(folD)
            BLD: BLi02602(folD)
            BCL: ABC3388(folD)
            BPU: BPUM_2163(folD)
            OIH: OB1880(folD)
            GKA: GK2396
            SAU: SA0915(folD)
            SAV: SAV1063(folD)
            SAM: MW0946(folD)
            SAR: SAR1037(folD)
            SAS: SAS0999(folD)
            SAC: SACOL1072(folD)
            SAB: SAB0930c(folD)
            SAO: SAOUHSC_01007
            SEP: SE0761
            SER: SERP0648(folD)
            SHA: SH1894(folD)
            SSP: SSP1727
            LMO: lmo1360(folD)
            LMF: LMOf2365_1377(folD)
            LIN: lin1397(folD)
            LWE: lwe1375(folD)
            LLA: L76582(folD)
            LLC: LACR_0921
            LLM: llmg_1693(folD)
            SPY: SPy_1502(folD)
            SPZ: M5005_Spy_1234(folD)
            SPM: spyM18_1520(folD)
            SPG: SpyM3_1157(folD)
            SPS: SPs0705
            SPH: MGAS10270_Spy1250(folD)
            SPI: MGAS10750_Spy1341(folD)
            SPJ: MGAS2096_Spy1252(folD)
            SPK: MGAS9429_Spy1228(folD)
            SPF: SpyM50619(folD)
            SPA: M6_Spy1254
            SPB: M28_Spy1173(folD)
            SPN: SP_0825
            SPR: spr0729(folD)
            SPD: SPD_0721(folD)
            SAG: SAG0494(folD)
            SAN: gbs0540
            SAK: SAK_0595(folD)
            SMU: SMU.572(folD)
            STL: stu0611(folD)
            SSA: SSA_0671(folD)
            SGO: SGO_0690(folD)
            LPL: lp_1599(folD)
            LJO: LJ1215 LJ1550
            LAC: LBA1332(folD)
            LSA: LSA0676(folD)
            LSL: LSL_0533(folD)
            LDB: Ldb1425(folD)
            LBU: LBUL_1320
            LBR: LVIS_0978
            LCA: LSEI_1639
            LGA: LGAS_0751
            LRE: Lreu_1184
            PPE: PEPE_0817
            EFA: EF0978(folD)
            OOE: OEOE_0943
            STH: STH1847
            CAC: CAC2083(folD)
            CPE: CPE1823(folD)
            CPF: CPF_2077(folD)
            CPR: CPR_1791(folD)
            CTC: CTC01579
            CTH: Cthe_1093
            CDF: CD0719(fchA) CD0720(folD)
            CBO: CBO1171(fchA)
            CBA: CLB_1202(fchA)
            CBH: CLC_1214(fchA)
            CBF: CLI_1253(fchA)
            CKL: CKL_0441(fchA) CKL_0442(folD)
            CHY: CHY_0696(fchA1) CHY_1878(folD) CHY_1879(fchA2)
            DSY: DSY0606 DSY0607 DSY2356
            TTE: TTE1293(folD)
            MTA: Moth_1516
            MGE: MG_013(folD)
            MPN: MPN017(mtd1)
            MPU: MYPU_2580(folD)
            MPE: MYPE6880(folD)
            MGA: MGA_0596(folD)
            MMY: MSC_0758(folD)
            MMO: MMOB1600(folD)
            UUR: UU337(folD)
            MFL: Mfl167
            MTU: Rv3356c(folD)
            MTC: MT3464(folD)
            MBO: Mb3391c(folD)
            MBB: BCG_3428c(folD)
            MLE: ML0674(folD)
            MPA: MAP3463c(folD)
            MMC: Mmcs_1204
            CGL: NCgl0620(cgl0648)
            CGB: cg0750(folD)
            CEF: CE0659
            CDI: DIP0620(folD)
            CJK: jk1697
            NFA: nfa34300(folD)
            RHA: RHA1_ro06234(folD)
            SCO: SCO4824(folD)
            SMA: SAV3442(folD1) SAV543(folD2)
            TWH: TWT634(folD)
            TWS: TW653(folD)
            LXX: Lxx18630(folD)
            ART: Arth_1116
            AAU: AAur_0482(folD)
            PAC: PPA1743
            NCA: Noca_0641
            TFU: Tfu_2571
            FRA: Francci3_1492 Francci3_2667
            FAL: FRAAL2298(folD) FRAAL4216(folD)
            ACE: Acel_0385
            KRA: Krad_3980
            SEN: SACE_4498(folD) SACE_6651(folD)
            STP: Strop_2276 Strop_3795
            BLO: BL0993(folD)
            BAD: BAD_0673(folD)
            RXY: Rxyl_0827
            FNU: FN1488
            RBA: RB7468(folD)
            CTR: CT078(folD)
            CTA: CTA_0083(folD)
            CMU: TC0350
            CPN: CPn0335(folD)
            CPA: CP0423
            CPJ: CPj0335(folD)
            CPT: CpB0344
            CCA: CCA00448(folD)
            CAB: CAB434
            CFE: CF0559(folD)
            PCU: pc1701(folD)
            BBU: BB0026(folD)
            BGA: BG0026(folD)
            BAF: BAPKO_0025(folD)
            TPA: TP0732
            TDE: TDE0013(folD)
            LIL: LA1865(folD)
            LIC: LIC12026(folD)
            LBJ: LBJ_1651(folD)
            LBL: LBL_1870(folD)
            SYN: sll0753(folD)
            SYW: SYNW0740(folD)
            SYC: syc0759_d(folD)
            SYF: Synpcc7942_0777
            SYD: Syncc9605_1928
            SYE: Syncc9902_0737
            SYG: sync_0990
            SYR: SynRCC307_0749(folD)
            SYX: SynWH7803_1570(folD)
            CYA: CYA_1974(folD)
            CYB: CYB_0090(folD)
            TEL: tll0021(folD)
            GVI: gll1884
            ANA: alr0212
            AVA: Ava_2703
            PMA: Pro1130(folD)
            PMM: PMM1069(folD)
            PMT: PMT1110(folD)
            PMN: PMN2A_0682
            PMB: A9601_11741(folD)
            PMC: P9515_11591(folD)
            PMF: P9303_09321(folD)
            PMG: P9301_11751(folD)
            PMH: P9215_12041(folD)
            PME: NATL1_15161(folD)
            TER: Tery_4172
            BTH: BT_1607
            BFR: BF3219
            BFS: BF3058
            PGI: PG1116(folD)
            SRU: SRU_1839
            CHU: CHU_1706(clpP)
            FJO: Fjoh_0243
            FPS: FP1475(folD)
            CTE: CT0719(mtd)
            CCH: Cag_0779
            CPH: Cpha266_0997
            PVI: Cvib_0963
            PLT: Plut_0927
            DET: DET0668(folD-1) DET0702(folD-2)
            DEH: cbdb_A656(folD)
            DEB: DehaBAV1_0637
            RCA: Rcas_0735
            DRA: DR_0867
            DGE: Dgeo_0514 Dgeo_0699
            TTH: TTC0755
            TTJ: TTHA1120
            AAE: aq_1898(folD)
            TMA: TM1767
            TPT: Tpet_1055
            MAC: MA3519(folD)
            MBA: Mbar_A2315
            MMA: MM_0441
            MBU: Mbur_1814
            MTP: Mthe_1242
            MHU: Mhun_0022
            MEM: Memar_1834
            MBN: Mboo_2188
            HAL: VNG1416G(folD)
            HMA: rrnAC0996(folD1)
            HWA: HQ2790A(folD)
            NPH: NP2054A(folD)
            TAC: Ta0898
            TVO: TVN1018
            PTO: PTO1071
            PAI: PAE0220(folD)
            PCL: Pcal_1897
STRUCTURES  PDB: 1A4I  1DIA  1DIB  1DIG  2C2X  2C2Y  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.9
            ExPASy - ENZYME nomenclature database: 3.5.4.9
            ExplorEnz - The Enzyme Database: 3.5.4.9
            ERGO genome analysis and discovery system: 3.5.4.9
            BRENDA, the Enzyme Database: 3.5.4.9
            CAS: 9027-97-8
///
ENTRY       EC 3.5.4.10                 Enzyme
NAME        IMP cyclohydrolase;
            inosinicase;
            inosinate cyclohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     IMP 1,2-hydrolase (decyclizing)
REACTION    IMP + H2O =
            5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
            [RN:R01127]
ALL_REAC    R01127
SUBSTRATE   IMP [CPD:C00130];
            H2O [CPD:C00001]
PRODUCT     5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
            [CPD:C04734]
REFERENCE   1  [PMID:13502325]
  AUTHORS   FLAKS JG, ERWIN MJ, BUCHANAN JM.
  TITLE     Biosynthesis of the purines. XVIII.
            5-Amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase
            and inosinicase.
  JOURNAL   J. Biol. Chem. 229 (1957) 603-12.
  ORGANISM  pigeon, chicken [GN:gga]
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01492  IMP cyclohydrolase
GENES       HSA: 471(ATIC)
            MMU: 108147(Atic)
            RNO: 81643(Atic)
            CFA: 488513(ATIC)
            GGA: 396091(ATIC)
            XTR: 448061(atic)
            SPU: 588680(LOC588680)
            DME: Dmel_CG11089
            CME: CML194C
            SCE: YLR028C(ADE16) YMR120C(ADE17)
            AGO: AGOS_AFR213C
            SPO: SPCPB16A4.03c
            ANI: AN4464.2
            AFM: AFUA_4G07690
            AOR: AO090023000806
            CNE: CNA06790
            UMA: UM01023.1
            DDI: DDB_0230095(purH)
            ECO: b4006(purH)
            ECJ: JW3970(purH)
            ECE: Z5583(purH)
            ECS: ECs4929
            ECC: c4964(purH)
            ECI: UTI89_C3814(purH)
            ECP: ECP_4219
            ECV: APECO1_2469(purH)
            ECW: EcE24377A_4550(purH)
            ECX: EcHS_A4240
            STY: STY3709(purH)
            STT: t3455(purH)
            SPT: SPA4013(purH)
            STM: STM4176(purH)
            YPE: YPO3728(purH)
            YPK: y0502(purH)
            YPM: YP_3091(purH)
            YPA: YPA_3601
            YPN: YPN_0237
            YPP: YPDSF_3726
            YPS: YPTB0300(purH)
            YPI: YpsIP31758_3843(purH)
            SFL: SF4078(purH)
            SFX: S3657(purH)
            SFV: SFV_4078(purH)
            SSN: SSON_4179(purH)
            SBO: SBO_4027(purH)
            SDY: SDY_3720(purH)
            ECA: ECA0241(purH)
            PLU: plu0495(purH)
            BUC: BU031(purH)
            BAS: BUsg032(purH)
            BAB: bbp032(purH)
            WBR: WGLp511(purH)
            SGL: SG0143
            ENT: Ent638_0216
            SPE: Spro_0293
            BFL: Bfl555(purH)
            BPN: BPEN_575(purH)
            HIP: CGSHiEE_07600(purH)
            HDU: HD1703(purH)
            HSO: HS_1625(purH)
            PMU: PM0222(purH)
            MSU: MS1297(purH)
            APL: APL_0958(purH)
            ASU: Asuc_1147
            XFA: XF1975
            XFT: PD0828(purH)
            XCC: XCC0498(purH)
            XCB: XC_0510
            XCV: XCV0547(purH)
            XAC: XAC0513(purH)
            XOO: XOO0539(purH)
            XOM: XOO_0506(XOO0506)
            VCH: VC0276(purH)
            VVU: VV1_1227(purH)
            VVY: VV3142
            VPA: VP2896
            VFI: VF2394(purH)
            PPR: PBPRA3419
            PAE: PA4854(purH)
            PAU: PA14_64200(purH)
            PAP: PSPA7_5574(purH)
            PPU: PP_4822(purH)
            PST: PSPTO_4866(purH)
            PSB: Psyr_4406
            PSP: PSPPH_4449(purH)
            PFL: PFL_0666(purH)
            PFO: Pfl_0613
            PEN: PSEEN4863(purH)
            PMY: Pmen_0708
            PAR: Psyc_1472(purH)
            PCR: Pcryo_1651
            PRW: PsycPRwf_1624
            ACI: ACIAD2447(purH)
            SON: SO_0442(purH)
            SDN: Sden_3407
            SSE: Ssed_0444
            SHE: Shewmr4_0445
            SHM: Shewmr7_3584
            SHN: Shewana3_0441
            ILO: IL2290(purH)
            CPS: CPS_0552(purH)
            PHA: PSHAa0345(purH)
            PAT: Patl_0268
            CBU: CBU_0336(purH)
            CBD: COXBU7E912_1743(purH)
            LPN: lpg0460(purH)
            LPF: lpl0502(purH)
            LPP: lpp0526(purH)
            MCA: MCA1747(purH)
            FTU: FTT0203c(purH)
            FTF: FTF0203c(purH)
            FTW: FTW_1885(purH)
            FTH: FTH_1849(purH)
            FTA: FTA_2038(purH)
            FTN: FTN_0177(purH)
            TCX: Tcr_0439
            NOC: Noc_1048
            AEH: Mlg_0611
            HCH: HCH_06011(purH)
            CSA: Csal_2289
            ABO: ABO_2015(purH)
            AHA: AHA_0841(purH)
            BCI: BCI_0035(purH)
            VOK: COSY_0869(purH)
            NME: NMB0983
            NMA: NMA1182(purH)
            NMC: NMC0963(purH)
            NGO: NGO1466
            CVI: CV_0546(purH)
            RSO: RSc0504(purH)
            REU: Reut_A0487
            REH: H16_A0501(purH)
            RME: Rmet_0427
            BMA: BMA2356(purH)
            BMV: BMASAVP1_A0269(purH)
            BML: BMA10299_A1131(purH)
            BMN: BMA10247_2535(purH)
            BCN: Bcen_0208
            BPS: BPSL2896(purH)
            BPM: BURPS1710b_3403(purH)
            BPL: BURPS1106A_3398(purH)
            BPD: BURPS668_3363(purH)
            BTE: BTH_I1250(purH)
            PNU: Pnuc_1877
            BPE: BP3416(purH)
            BPA: BPP3566(purH)
            BBR: BB4001(purH)
            RFR: Rfer_1582
            POL: Bpro_1132
            AJS: Ajs_3584
            HAR: HEAR0255(purH)
            MMS: mma_0308
            NEU: NE0876(purH)
            NET: Neut_1210
            NMU: Nmul_A0133
            EBA: ebA1153(purH)
            AZO: azo2894(purH)
            DAR: Daro_3667
            TBD: Tbd_2458
            HHE: HH0483(purH)
            WSU: WS1885(purH)
            TDN: Tmden_0550
            CJE: Cj0953c(purH)
            CJR: CJE1033(purH)
            CJJ: CJJ81176_0976(purH)
            CJU: C8J_0895(purH)
            CJD: JJD26997_0828(purH)
            CFF: CFF8240_0558(purH)
            CCV: CCV52592_1838(purH)
            CHA: CHAB381_0670(purH)
            CCO: CCC13826_1632(purH)
            ABU: Abu_1638(purH)
            NIS: NIS_0948(purH)
            SUN: SUN_1564(purH)
            GSU: GSU0609(purH)
            GME: Gmet_2905
            PCA: Pcar_2232
            DVU: DVU3235
            LIP: LI0578(purH)
            BBA: Bd3002(purH)
            DPS: DP1614(purH)
            ADE: Adeh_2468
            AFW: Anae109_1399
            MXA: MXAN_2914(purH)
            SAT: SYN_02440
            SFU: Sfum_2760
            WOL: WD0867(purH)
            WBM: Wbm0411(purH)
            APH: APH_1207(purH)
            ERU: Erum8290(purH)
            ERW: ERWE_CDS_08780(purH)
            ERG: ERGA_CDS_08690(purH)
            ECN: Ecaj_0866
            ECH: ECH_1074(purH)
            NSE: NSE_0185(purH)
            PUB: SAR11_0319(purH)
            MLO: mlr4101
            MES: Meso_3420
            PLA: Plav_1319
            SME: SMc04088(purH)
            SMD: Smed_3189
            ATU: Atu2823(purH)
            ATC: AGR_C_5117
            RET: RHE_CH04107(purH)
            RLE: RL4722(purH)
            BME: BMEI0233
            BMF: BAB1_1824(purH)
            BMS: BR1816(purH)
            BMB: BruAb1_1796(purH)
            BOV: BOV_1749(purH)
            BJA: blr0581(purH)
            BRA: BRADO0338(purH)
            BBT: BBta_0323(purH)
            RPA: RPA0028(purH)
            RPB: RPB_0084
            RPC: RPC_0023
            RPD: RPD_0719
            RPE: RPE_0026
            NWI: Nwi_0158(purH)
            NHA: Nham_0195
            BHE: BH15970(purH)
            BQU: BQ12870(purH)
            BBK: BARBAKC583_0074(purH)
            XAU: Xaut_1732
            CCR: CC_0086
            SIL: SPO3374(purH)
            SIT: TM1040_0091
            RSP: RSP_1100(purH)
            RSH: Rsph17029_2763
            RSQ: Rsph17025_2928
            JAN: Jann_4042
            RDE: RD1_0655(purH)
            PDE: Pden_2718
            MMR: Mmar10_2928
            HNE: HNE_3372(purH)
            NAR: Saro_0106
            SAL: Sala_3123
            ELI: ELI_12540
            GOX: GOX0428
            GBE: GbCGDNIH1_1647
            ACR: Acry_0027
            MAG: amb0100
            MGM: Mmc1_3468
            ABA: Acid345_4470
            BSU: BG10710(purH)
            BHA: BH0633(purH)
            BAN: BA0298(purH)
            BAR: GBAA0298(purH)
            BAA: BA_0870
            BAT: BAS0285
            BCE: BC0333
            BCA: BCE_0327(purH)
            BCZ: BCZK0273(purH)
            BCY: Bcer98_0277
            BTK: BT9727_0270(purH)
            BTL: BALH_0292(purH)
            BLI: BL01486(purH)
            BLD: BLi00703(purH)
            BCL: ABC1034(purH)
            BPU: BPUM_0606
            OIH: OB0749(purH)
            GKA: GK0267(purH)
            SAU: SA0925(purH)
            SAV: SAV1073(purH)
            SAM: MW0956(purH)
            SAR: SAR1047(purH)
            SAS: SAS1009
            SAC: SACOL1082(purH)
            SAB: SAB0940(purH)
            SAA: SAUSA300_0975(purH)
            SAO: SAOUHSC_01017
            SAJ: SaurJH9_1133
            SAH: SaurJH1_1155
            SEP: SE0771
            SER: SERP0658(purH)
            SHA: SH1884(purH)
            SSP: SSP1717
            LMO: lmo1765(purH)
            LMF: LMOf2365_1790(purH)
            LIN: lin1877(purH)
            LWE: lwe1783(purH)
            LLA: L158710(purH)
            LLC: LACR_1605
            LLM: llmg_0994(purH)
            SPZ: M5005_Spy_0027(purH)
            SPM: spyM18_0030(purH)
            SPG: SpyM3_0024(purH)
            SPS: SPs0025
            SPH: MGAS10270_Spy0028
            SPI: MGAS10750_Spy0027
            SPJ: MGAS2096_Spy0028
            SPK: MGAS9429_Spy0027
            SPA: M6_Spy0076(purH)
            SPB: M28_Spy0027(purH)
            SPN: SP_0050
            SPR: spr0051(purH)
            SPD: SPD_0057(purH)
            SAG: SAG0030(purH)
            SAN: gbs0029
            SAK: SAK_0063(purH)
            SMU: SMU.37(purH)
            STC: str0035(purH)
            STL: stu0035(purH)
            SSA: SSA_0035(purH)
            LPL: lp_2720(purH)
            LAC: LBA1552(purH)
            LSA: LSA0662(purH)
            LSL: LSL_0670(purH)
            LDB: Ldb1436(purH)
            LBU: LBUL_1331
            LCA: LSEI_1747
            EFA: EF1778(purH)
            OOE: OEOE_1129
            STH: STH2850
            CAC: CAC1395(purH)
            CPE: CPE0686(purH)
            CPF: CPF_0677(purH)
            CPR: CPR_0675(purH)
            CTC: CTC01962(purH)
            CDF: CD0223(purH)
            CBO: CBO2873(purH)
            CBA: CLB_2838(purH)
            CBH: CLC_2771(purH)
            CBF: CLI_2931(purH)
            CBE: Cbei_1059
            CKL: CKL_2684(purH)
            AMT: Amet_0925
            CHY: CHY_1078(purH)
            DSY: DSY3927
            SWO: Swol_1775
            CSC: Csac_1992
            TTE: TTE0592(purH)
            MTA: Moth_2044
            MTU: Rv0957(purH)
            MTC: MT0984(purH)
            MBO: Mb0982(purH)
            MBB: BCG_1011(purH)
            MLE: ML0161(purH)
            MPA: MAP0903(purH)
            MAV: MAV_1081(purH)
            MSM: MSMEG_5515(purH)
            MMC: Mmcs_4319
            CGL: NCgl0827(purH)
            CGB: cg0984(purH)
            CEF: CE0937(purH)
            CDI: DIP0839(purH)
            CJK: jk1556(purH)
            NFA: nfa49860(purHJ)
            RHA: RHA1_ro05579(purH)
            SCO: SCO4814(purH)
            SMA: SAV3444(purH)
            TWH: TWT084(purH)
            TWS: TW094(purH)
            LXX: Lxx19650(purH)
            PAC: PPA1747
            TFU: Tfu_2572
            FRA: Francci3_0657
            FAL: FRAAL1162(purH)
            ACE: Acel_0384
            SEN: SACE_6664(purH)
            BLO: BL0735(purH)
            BAD: BAD_0811(purH)
            FNU: FN0982(purH)
            RBA: RB10113(purH)
            TDE: TDE1896(purH)
            LIL: LA2283(purH)
            LIC: LIC11655(purH)
            LBJ: LBJ_1329(purH)
            LBL: LBL_1554(purH)
            SYN: slr0597(purH)
            SYW: SYNW0249(purH)
            SYC: syc1119_c(purH)
            SYF: Synpcc7942_0396
            SYD: Syncc9605_0243
            SYE: Syncc9902_0272
            SYG: sync_0289(purH)
            SYR: SynRCC307_2316(purH)
            SYX: SynWH7803_0293(purH)
            CYA: CYA_2813(purH)
            CYB: CYB_2851(purH)
            TEL: tlr1547(purH)
            GVI: glr0559(purH)
            ANA: all3093(purH)
            AVA: Ava_3818(purH)
            PMA: Pro0298(purH)
            PMM: PMM0266(purH)
            PMT: PMT1857(purH)
            PMN: PMN2A_1632
            PMI: PMT9312_0268
            PMB: A9601_02881(purH)
            PMC: P9515_02991(purH)
            PMF: P9303_24851(purH)
            PMG: P9301_02891(purH)
            PMH: P9215_02901
            PME: NATL1_03441(purH)
            TER: Tery_1128
            BTH: BT_3812(purH)
            BFR: BF4101
            BFS: BF3917(purH)
            PGI: PG1397(purH)
            SRU: SRU_1639(purH)
            CHU: CHU_3309(purH)
            FJO: Fjoh_1459
            FPS: FP2416(purH)
            CTE: CT0320(purH)
            CCH: Cag_0258(purH)
            PVI: Cvib_0483
            PLT: Plut_0432
            DET: DET1417(purH)
            DEH: cbdb_A1381(purH)
            DRA: DR_0868
            DGE: Dgeo_0513
            TTH: TTC0561
            TTJ: TTHA0930
            AAE: aq_1963(purH)
            TMA: TM1249
            TPT: Tpet_1522
            TME: Tmel_1545
            FNO: Fnod_1150 Fnod_1673
            MJA: MJ0626
            MMP: MMP1310(purO)
            MMQ: MmarC5_0283
            MMZ: MmarC7_0555
            MAE: Maeo_0773
            MVN: Mevan_0620
            MAC: MA4012(purH)
            MBA: Mbar_A0571
            MMA: MM_0898
            MTP: Mthe_1644
            MTH: MTH1020
            MST: Msp_1398(purO)
            MSI: Msm_0976
            MKA: MK0087
            AFU: AF1811
            HAL: VNG0414G(purH) VNG2371C
            HMA: rrnAC0189(purH) rrnAC2659
            HWA: HQ1006A(purH)
            NPH: NP0732A(purO)
            TAC: Ta0060
            TVO: TVN0016
            PTO: PTO0745
            TKO: TK0430
            RCI: RCIX491(purO)
STRUCTURES  PDB: 1G8M  1M9N  1OZ0  1P4R  1PKX  1PL0  1THZ  2B1G  2B1I  2IU0  
                 2IU3  2NTK  2NTL  2NTM  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.10
            ExPASy - ENZYME nomenclature database: 3.5.4.10
            ExplorEnz - The Enzyme Database: 3.5.4.10
            ERGO genome analysis and discovery system: 3.5.4.10
            BRENDA, the Enzyme Database: 3.5.4.10
            CAS: 9013-81-4
///
ENTRY       EC 3.5.4.11                 Enzyme
NAME        pterin deaminase;
            acrasinase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     2-amino-4-hydroxypteridine aminohydrolase
REACTION    2-amino-4-hydroxypteridine + H2O = 2,4-dihydroxypteridine + NH3
            [RN:R02815]
ALL_REAC    R02815;
            (other) R06137
SUBSTRATE   2-amino-4-hydroxypteridine [CPD:C00715];
            H2O [CPD:C00001]
PRODUCT     2,4-dihydroxypteridine [CPD:C03212];
            NH3 [CPD:C00014]
COMMENT     The animal enzyme is specific for pterin, isoxanthopterin and
            tetrahydropterin.
REFERENCE   1  [PMID:13654299]
  AUTHORS   LEVENBERG B, HAYAISHI O.
  TITLE     A bacterial pterin deaminase.
  JOURNAL   J. Biol. Chem. 234 (1959) 955-61.
  ORGANISM  Alcaligenes metalcaligenes
REFERENCE   2  [PMID:5821022]
  AUTHORS   Rembold H, Simmersbach F.
  TITLE     Catabolism of pteridine cofactors. II. A specific pterin deaminase
            in rat liver.
  JOURNAL   Biochim. Biophys. Acta. 184 (1969) 589-96.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.11
            ExPASy - ENZYME nomenclature database: 3.5.4.11
            ExplorEnz - The Enzyme Database: 3.5.4.11
            ERGO genome analysis and discovery system: 3.5.4.11
            BRENDA, the Enzyme Database: 3.5.4.11
            CAS: 9025-04-1
///
ENTRY       EC 3.5.4.12                 Enzyme
NAME        dCMP deaminase;
            deoxycytidylate deaminase;
            deoxy-CMP-deaminase;
            deoxycytidylate aminohydrolase;
            deoxycytidine monophosphate deaminase;
            deoxycytidine-5'-phosphate deaminase;
            deoxycytidine-5'-monophosphate aminohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     dCMP aminohydrolase
REACTION    dCMP + H2O = dUMP + NH3 [RN:R01663]
ALL_REAC    R01663;
            (other) R06137
SUBSTRATE   dCMP [CPD:C00239];
            H2O [CPD:C00001]
PRODUCT     dUMP [CPD:C00365];
            NH3 [CPD:C00014]
COMMENT     Also acts on some 5-substituted dCMPs.
REFERENCE   1
  AUTHORS   Scarano, E.
  TITLE     The enzymatic deamination of 6-aminopyrimidine deoxyribonucleotides.
            I. The enzymatic deamination of deoxycytidine 5'-phosphate and of
            5-methyldeoxycytidine 5-methyldeoxycytidine 5'-phosphate.
  JOURNAL   J. Biol. Chem. 235 (1960) 706-713.
  ORGANISM  rabbit, mouse [GN:mmu], Saccharomyces cerevisiae [GN:sce],
            Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Scarano, E., Bonaduce, L. and de Petrocellis, B.
  TITLE     The enzymatic deamination of 6-aminopyrimidine deoxyribonucleotides.
            II. Purification and properties of a 6-aminopyrimidine
            deoxyribonucleoside 5'-phosphate deaminase from unfertilized eggs of
            sea urchin.
  JOURNAL   J. Biol. Chem. 235 (1960) 3556-3561.
  ORGANISM  Sphaerechinus granularis, Paracentrotus lividus
REFERENCE   3  [PMID:5002683]
  AUTHORS   Sergott RC, Debeer LJ, Bessman MJ.
  TITLE     On the regulation of a bacterial deoxycytidylate deaminase.
  JOURNAL   J. Biol. Chem. 246 (1971) 7755-8.
  ORGANISM  Lactobacillus acidophilus [GN:lac]
PATHWAY     PATH: map00240  Pyrimidine metabolism
            PATH: map03090  Type II secretion system
ORTHOLOGY   KO: K01493  dCMP deaminase
GENES       HSA: 1635(DCTD)
            PTR: 461620(DCTD)
            MMU: 320685(Dctd)
            RNO: 290741(LOC290741)
            CFA: 607328(DCTD)
            GGA: 422556(DCTD)
            XLA: 414581(MGC81193)
            SPU: 575919(LOC575919)
            DME: Dmel_CG6951
            CEL: ZK643.2
            ATH: AT3G48540
            OSA: 4326895
            CME: CMQ291C
            SCE: YHR144C(DCD1)
            AGO: AGOS_AFR023W
            PIC: PICST_34441(DCD1)
            CGR: CAGL0G05852g
            SPO: SPBC2G2.13c
            ANI: AN7429.2
            AFM: AFUA_2G06240
            AOR: AO090001000741 AO090001000742
            CNE: CNB00950
            CPV: cgd2_2780
            CHO: Chro.20294
            TET: TTHERM_00498180
            XCC: XCC0126
            XCB: XC_0132
            VCH: VCA0840
            VVU: VV2_0531
            VVY: VVA1080
            VPA: VPA1192
            VFI: VFA0917
            PPR: PBPRB1018(EBIG6842)
            SDN: Sden_0078
            SFR: Sfri_3571
            PHA: PSHAa1256
            CBU: CBU_1374
            VOK: COSY_0290
            REH: H16_B0797
            MPT: Mpe_A1200 Mpe_B0197
            TDN: Tmden_0147
            ABU: Abu_0039
            GSU: GSU1686
            GME: Gmet_1622
            GUR: Gura_2185
            PCA: Pcar_1443
            DVU: DVU1202
            DDE: Dde_2433
            BBA: Bd0085
            DPS: DP2271
            SAT: SYN_02368
            RET: RHE_CH01957
            RLE: RL2287
            BME: BMEII0619
            JAN: Jann_3746
            MAG: amb2697
            MGM: Mmc1_1393
            BSU: BG10481(comEB)
            BHA: BH1334(comEB)
            BAN: BA4552(comEB)
            BAR: GBAA4552(comEB)
            BAA: BA_4997
            BAT: BAS4224
            BCE: BC4323
            BCA: BCE_4407(comEB)
            BCZ: BCZK4072(comEB)
            BTK: BT9727_4062(comEB)
            BLI: BL02086(comEB)
            BLD: BLi02751(comEB)
            BCL: ABC1647(comEB)
            BPU: BPUM_2292(comEB)
            OIH: OB1980
            GKA: GK2516(comEB)
            SAU: SA1417(comEB)
            SAV: SAV1589(comEB)
            SAM: MW1540(comEB)
            SAR: SAR1666
            SAS: SAS1526
            SAC: SACOL1645
            SAB: SAB1461c
            SAA: SAUSA300_1548
            SAO: SAOUHSC_01692
            SEP: SE1275
            SER: SERP1156
            SHA: SH1326(comEB)
            SSP: SSP1169
            LMO: lmo1483(comEB)
            LMF: LMOf2365_1502
            LIN: lin1518(comEB)
            LWE: lwe1496(comEB)
            LLA: L155044(dcdA)
            LLC: LACR_1252
            SPY: SPy_1823(comEB)
            SPZ: M5005_Spy_1548(comEB)
            SPM: spyM18_1888
            SPG: SpyM3_1575(comEB)
            SPS: SPs0292
            SPJ: MGAS2096_Spy1573(comEB)
            SPA: M6_Spy1537
            SPB: M28_Spy1535(comEB)
            SPN: SP_0744
            SPR: spr0654(comEB)
            SAG: SAG1704
            SAN: gbs1750
            SAK: SAK_1713
            SMU: SMU.1849(comEB)
            STC: str1741(comEB)
            STL: stu1741(comEB)
            SSA: SSA_1497(comEB)
            LPL: lp_2130(comEB)
            LJO: LJ0199
            LAC: LBA0210
            LSA: LSA1070
            LSL: LSL_0679(comEB)
            LDB: Ldb0339
            LBU: LBUL_0294
            LBR: LVIS_1396
            EFA: EF2448
            STH: STH80
            CAC: CAC2876
            CPE: CPE1066
            CPF: CPF_1322
            CTC: CTC00309
            CHY: CHY_2556
            DSY: DSY4925
            SWO: Swol_2391
            TTE: TTE0148(comEB)
            MTA: Moth_2389
            MPU: MYPU_2780(dctD)
            MGA: MGA_0701(folA)
            MMY: MSC_0581(dctD)
            MMO: MMOB5300(comEB)
            MSY: MS53_0396(comEB)
            MCP: MCAP_0397
            MFL: Mfl385
            CDI: DIP0247
            PAC: PPA1950
            RXY: Rxyl_1647
            FNU: FN1902
            TPA: TP0274
            TDE: TDE2193
            BTH: BT_4260
            BFR: BF0964
            BFS: BF0882
            PGI: PG1856
            CHU: CHU_2215(dcdA)
            FPS: FP0464
            CTE: CT0746
            CCH: Cag_0622
            PLT: Plut_0726
            DET: DET0413
            DEH: cbdb_A365
            DRA: DR_2631
            TMA: TM0404
            MAC: MA0136 MA0137
            MBA: Mbar_A0853
            MMA: MM_1423 MM_2722 MM_3028
            MBU: Mbur_1985
            TAC: Ta0312
            TVO: TVN1288
            PTO: PTO0422
            PAB: PAB1975
            PFU: PF1598
            TKO: TK2257
            RCI: RCIX305
STRUCTURES  PDB: 1VQ2  2HVV  2HVW  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.12
            ExPASy - ENZYME nomenclature database: 3.5.4.12
            ExplorEnz - The Enzyme Database: 3.5.4.12
            ERGO genome analysis and discovery system: 3.5.4.12
            BRENDA, the Enzyme Database: 3.5.4.12
            CAS: 9026-92-0
///
ENTRY       EC 3.5.4.13                 Enzyme
NAME        dCTP deaminase;
            deoxycytidine triphosphate deaminase;
            5-methyl-dCTP deaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     dCTP aminohydrolase
REACTION    dCTP + H2O = dUTP + NH3 [RN:R02325]
ALL_REAC    R02325;
            (other) R00568 R06137
SUBSTRATE   dCTP [CPD:C00458];
            H2O [CPD:C00001]
PRODUCT     dUTP [CPD:C00460];
            NH3 [CPD:C00014]
REFERENCE   1  [PMID:4976547]
  AUTHORS   Tomita F, Takahashi I.
  TITLE     A novel enzyme, dCTP deaminase, found in Bacillus subtilis infected
            with phage PBS I.
  JOURNAL   Biochim. Biophys. Acta. 179 (1969) 18-27.
  ORGANISM  Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K01494  dCTP deaminase
GENES       DDI: DDB_0230112 DDB_0230132
            EHI: 8.t00003
            ECO: b2065(dcd)
            ECJ: JW2050(dcd)
            ECE: Z3233(dcd)
            ECS: ECs2872
            ECC: c2592(dcd)
            ECI: UTI89_C2341(dcd)
            ECP: ECP_2105
            ECV: APECO1_1156(dcd)
            ECW: EcE24377A_2358(dcd)
            ECX: EcHS_A2205
            STY: STY2334(dcd)
            STT: t0751(dcd)
            SPT: SPA0745(dcd)
            SEC: SC2123(dcd)
            STM: STM2121(dcd)
            YPE: YPO1525(dcd)
            YPK: y2645(dcd)
            YPM: YP_1414(dcd2)
            YPA: YPA_0819
            YPN: YPN_2455
            YPS: YPTB1537(dcd)
            YPI: YpsIP31758_2452(dcd)
            SFL: SF2129(dcd)
            SFX: S2253(dcd)
            SFV: SFV_2124(dcd)
            SSN: SSON_2118(dcd)
            SBO: SBO_0892(dcd)
            SDY: SDY_2197(dcd)
            ECA: ECA1412(dcd)
            PLU: plu1557(dcd)
            BUC: BU108(dcd)
            BAS: BUsg101(dcd)
            BAB: bbp102(dcd)
            WBR: WGLp537(dcd)
            SGL: SG0974
            HIT: NTHI0219(dcd)
            HIP: CGSHiEE_02630(dcd)
            HIQ: CGSHiGG_04540(dcd)
            HDU: HD1661(dcd)
            HSO: HS_0645(dcd)
            PMU: PM0951(dcd)
            MSU: MS1581(dcd)
            APL: APL_0835(dcd)
            XFA: XF0762
            XFT: PD1895(dcd)
            XCC: XCC2570(dcd)
            XCB: XC_1548
            XCV: XCV2892
            XAC: XAC2740(dcd)
            XOO: XOO3278(dcd)
            XOM: XOO_3103(XOO3103)
            PAE: PA3480
            PAU: PA14_19090(dcd)
            PAP: PSPA7_1646(dcd)
            PPU: PP_1100(dcd)
            PPF: Pput_1140
            PST: PSPTO_4144
            PSB: Psyr_2556 Psyr_3883
            PSP: PSPPH_1381 PSPPH_2711 PSPPH_2712(dcd1) PSPPH_4308(dcd2)
                 PSPPH_4309
            PFL: PFL_1261(dcd)
            PFO: Pfl_1202
            PMY: Pmen_1408
            PAR: Psyc_1425(dcd)
            PCR: Pcryo_1588
            PRW: PsycPRwf_1700
            ACI: ACIAD0776(dcd)
            ACB: A1S_0784
            SON: SO_2616(dcd)
            SFR: Sfri_2243
            SBL: Sbal_2462
            SBM: Shew185_2455
            SPC: Sputcn32_2217
            SHE: Shewmr4_1658
            SHM: Shewmr7_1733
            SHN: Shewana3_1763
            SHW: Sputw3181_1792
            ILO: IL0709(dcd)
            CPS: CPS_2837(dcd)
            PHA: PSHAa1319(dcd)
            PAT: Patl_1899
            SDE: Sde_2396
            MAQ: Maqu_0941
            CBU: CBU_1688
            CBD: COXBU7E912_0313(dcd)
            LPN: lpg2956(dcd)
            LPF: lpl2885(dcd)
            LPP: lpp3027(dcd)
            MCA: MCA0053
            FTU: FTT0993c(dcd)
            FTF: FTF0993c(dcd)
            FTW: FTW_0900(dcd)
            FTL: FTL_1208
            FTH: FTH_1183(dcd)
            FTA: FTA_1277(dcd)
            FTN: FTN_0873(dcd)
            TCX: Tcr_1043
            NOC: Noc_1180
            AEH: Mlg_0825
            HHA: Hhal_0713
            HCH: HCH_01900(dcd)
            CSA: Csal_2114
            ABO: ABO_1577(dcd)
            MMW: Mmwyl1_1548
            AHA: AHA_2236(dcd)
            DNO: DNO_0507
            BCI: BCI_0395(dcd)
            NME: NMB0849
            NMA: NMA1060
            NMC: NMC0789
            NGO: NGO0421
            CVI: CV_3554(dcd)
            RSO: RSc2366(dcd)
            REU: Reut_A0688
            REH: H16_A2931(dcd)
            RME: Rmet_2755
            BMA: BMA0714
            BMV: BMASAVP1_A2299(dcd)
            BML: BMA10299_A2987(dcd)
            BMN: BMA10247_1612(dcd)
            BXE: Bxe_A3478
            BVI: Bcep1808_2517
            BUR: Bcep18194_A5764
            BCN: Bcen_1822
            BCH: Bcen2424_2433
            BAM: Bamb_2480
            BPS: BPSL1002(dcd)
            BPM: BURPS1710b_1215(dcd)
            BPL: BURPS1106A_1063(dcd)
            BPD: BURPS668_1057(dcd)
            BTE: BTH_I0860(dcd)
            PNU: Pnuc_0649
            BPE: BP0185(dcd)
            BPA: BPP0760(dcd)
            BBR: BB0845(dcd)
            RFR: Rfer_3293
            POL: Bpro_1505
            PNA: Pnap_1049
            AAV: Aave_1144
            AJS: Ajs_1130
            VEI: Veis_1337
            MPT: Mpe_A1177 Mpe_B0168
            HAR: HEAR1080(dcd)
            MMS: mma_1184
            NEU: NE0623
            NET: Neut_1923
            NMU: Nmul_A1965
            EBA: ebA4412(dcd)
            AZO: azo3200(dcd)
            DAR: Daro_0577
            TBD: Tbd_2107
            MFA: Mfla_0916 Mfla_1060
            HPY: HP0372
            HPJ: jhp1009(dcd)
            HPA: HPAG1_1020
            HHE: HH0193
            HAC: Hac_0495(dcd)
            WSU: WS1071(DCD)
            CJE: Cj1292(dcd)
            CJR: CJE1484
            CJJ: CJJ81176_1309
            CJU: C8J_1235
            CFF: CFF8240_1566(dcd)
            CCV: CCV52592_0559(dcd)
            CHA: CHAB381_1552(dcd)
            CCO: CCC13826_2308(dcd)
            NIS: NIS_1646(dcd)
            SUN: SUN_0090(dcd)
            BBA: Bd2411(dcd)
            RPR: RP069
            RTY: RT0063(dcd)
            RCO: RC0099(dcd)
            RFE: RF_0054(dcd)
            RBE: RBE_1297(dcd)
            RAK: A1C_00540(dcd)
            RBO: A1I_00380(dcd)
            RCM: A1E_00330(dcd)
            RRI: A1G_00610(dcd)
            OTS: OTBS_2156(dcd)
            WOL: WD0379
            WBM: Wbm0292
            AMA: AM147(dcd)
            APH: APH_0130
            ERU: Erum6990(dcd)
            ERW: ERWE_CDS_07340(dcd)
            ERG: ERGA_CDS_07260(dcd)
            ECN: Ecaj_0707
            ECH: ECH_0296
            NSE: NSE_0964
            PUB: SAR11_0472(dcd)
            MLO: mlr5652
            MES: Meso_0097
            SME: SMc02218
            ATU: Atu0434(dcd)
            ATC: AGR_C_764
            RET: RHE_CH00524(dcd)
            RLE: RL0555
            BME: BMEI1616
            BMF: BAB1_0336
            BMS: BR0306
            BMB: BruAb1_0332
            BJA: bll5009 blr1106(dcd)
            BRA: BRADO6769(dcd)
            BBT: BBta_0769(dcd)
            RPA: RPA4765
            RPB: RPB_0792
            RPC: RPC_1525 RPC_4903
            RPD: RPD_0904
            RPE: RPE_4876
            NWI: Nwi_0140
            NHA: Nham_0218
            BHE: BH02700
            BQU: BQ02580
            BBK: BARBAKC583_1200(dcd)
            CCR: CC_2237
            SIL: SPO2498
            SIT: TM1040_0911
            RSP: RSP_2609(dcd)
            JAN: Jann_1781
            RDE: RD1_3160
            MMR: Mmar10_0492
            HNE: HNE_2673
            NAR: Saro_0146
            SAL: Sala_0762
            SWI: Swit_4050
            ELI: ELI_11475
            GOX: GOX0851
            GBE: GbCGDNIH1_1038
            ACR: Acry_1507
            RRU: Rru_A2794
            MAG: amb1527
            ABA: Acid345_1186
            BHA: BH0368
            CAC: CAC0025(dcd)
            MTU: Rv0321(dcd)
            MTC: MT0336(dcd)
            MBO: Mb0329(dcd)
            MBB: BCG_0361(dcd)
            MLE: ML2507
            MPA: MAP3820(dcd)
            MAV: MAV_4828(dcd)
            MSM: MSMEG_0678(dcd)
            MMC: Mmcs_0430
            CGL: NCgl2751(cgl2848)
            CGB: cg3155(dcd)
            CEF: CE2663
            CDI: DIP2142(dcd)
            CJK: jk0174(dcd)
            NFA: nfa54290(dcd)
            RHA: RHA1_ro05342
            SCO: SCO3678(SCH35.46)
            SMA: SAV4464(dcd)
            TWH: TWT787(dcd)
            TWS: TW796(dcd)
            LXX: Lxx23830(dcd)
            CMI: CMM_2900
            AAU: AAur_3686(dcd)
            TFU: Tfu_2932
            FRA: Francci3_4349
            FAL: FRAAL6635(dcd)
            SEN: SACE_7224(dcd)
            BLO: BL1512
            BAD: BAD_1580(dcd)
            RBA: RB3427(dcd)
            CTR: CT039(dcd)
            CTA: CTA_0042(dcd)
            CMU: TC0309
            CPN: CPn0392(dcd)
            CPA: CP0363
            CPJ: CPj0392(dcd)
            CPT: CpB0404
            CCA: CCA00404(dcd)
            CAB: CAB391(dcd)
            CFE: CF0603(dcd)
            PCU: pc0958(dcd)
            LIL: LA0072
            LIC: LIC10065(dcd)
            LBJ: LBJ_0062(dcd)
            LBL: LBL_3016(dcd)
            SYN: sll1258(dcd)
            SYW: SYNW0278(dcd)
            SYC: syc0813_d(dcd) syc2195_c(dcd)
            SYF: Synpcc7942_0717 Synpcc7942_1900
            SYD: Syncc9605_0272 Syncc9605_1883
            SYE: Syncc9902_2072
            SYG: sync_0319(dcd)
            SYR: SynRCC307_2346(dcd)
            SYX: SynWH7803_0322(dcd) SynWH7803_0949(dcd)
            CYA: CYA_1474(dcd)
            CYB: CYB_1670(dcd)
            TEL: tll0824
            GVI: gll3510
            ANA: all0066
            AVA: Ava_2668
            PMA: Pro0274(dcd)
            PMM: PMM0244(dcd)
            PMT: PMT1828(dcd)
            PMN: PMN2A_1610
            PMI: PMT9312_0246
            PMB: A9601_02661(dcd)
            PMC: P9515_02771(dcd)
            PMF: P9303_24531(dcd)
            PMG: P9301_02671(dcd)
            PME: NATL1_03221(dcd)
            SRU: SRU_1433(dcd)
            CHU: CHU_2002(dcd)
            RRS: RoseRS_4201
            RCA: Rcas_0432
            DGE: Dgeo_1880
            TTH: TTC1864
            TTJ: TTHA0130
            AAE: aq_1607(dcd)
            MHU: Mhun_1008 Mhun_2260
            MST: Msp_0604 Msp_1048(dcd)
            MSI: Msm_0402
            MKA: MK0291(dcd_1)
            HAL: VNG0245G(dtd)
            HMA: rrnAC1776(dcd2)
            HWA: HQ1278A(dcd) HQ3116A(dcd)
            NPH: NP0954A(dcd_2) NP5166A(dcd_1)
            TAC: Ta0598m
            TVO: TVN0636
            PTO: PTO0130
            PAB: PAB1164(dcd)
            PFU: PF1996
            TKO: TK1414
            APE: APE_0333.1
            IHO: Igni_0224
            HBU: Hbut_1159
            SSO: SSO0190(dcd) SSO2954(dcd-2)
            STO: ST0226 ST1632
            SAI: Saci_0789(dcD) Saci_1672
            PAI: PAE2008
            PIS: Pisl_1825
            PCL: Pcal_1021
            PAS: Pars_2075
            TPE: Tpen_0140
            NEQ: NEQ316 NEQ329
STRUCTURES  PDB: 1OGH  1PKH  1PKJ  1PKK  1XS1  1XS4  1XS6  2J4H  2J4Q  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.13
            ExPASy - ENZYME nomenclature database: 3.5.4.13
            ExplorEnz - The Enzyme Database: 3.5.4.13
            ERGO genome analysis and discovery system: 3.5.4.13
            BRENDA, the Enzyme Database: 3.5.4.13
            CAS: 37289-18-2
///
ENTRY       EC 3.5.4.14                 Enzyme
NAME        deoxycytidine deaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     deoxycytidine aminohydrolase
REACTION    deoxycytidine + H2O = deoxyuridine + NH3 [RN:R02485]
ALL_REAC    R02485;
            (other) R06137
SUBSTRATE   deoxycytidine [CPD:C00881];
            H2O [CPD:C00001]
PRODUCT     deoxyuridine [CPD:C00526];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Cohen, S.S.
  TITLE     Studies on controlling mechanisms in the metabolism of
            virus-infected bacteria.
  JOURNAL   Cold Spring Harbour Symp. Quant. Biol. 18 (1953) 221-235.
PATHWAY     PATH: map00240  Pyrimidine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.14
            ExPASy - ENZYME nomenclature database: 3.5.4.14
            ExplorEnz - The Enzyme Database: 3.5.4.14
            ERGO genome analysis and discovery system: 3.5.4.14
            BRENDA, the Enzyme Database: 3.5.4.14
            CAS: 37259-56-6
///
ENTRY       EC 3.5.4.15                 Enzyme
NAME        guanosine deaminase;
            guanosine aminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     guanosine aminohydrolase
REACTION    guanosine + H2O = xanthosine + NH3 [RN:R02145]
ALL_REAC    R02145;
            (other) R06137
SUBSTRATE   guanosine [CPD:C00387];
            H2O [CPD:C00001]
PRODUCT     xanthosine [CPD:C01762];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Isihida, Y., Shirafiji, H., Kida, M. and Yoneda, M.
  TITLE     Studies on the guanosine degrading system in bacterial cell. III.
            Preparation and properties of guanosine deaminase.
  JOURNAL   Agric. Biol. Chem. 33 (1969) 384-390.
  ORGANISM  Pseudomonas convexa
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.15
            ExPASy - ENZYME nomenclature database: 3.5.4.15
            ExplorEnz - The Enzyme Database: 3.5.4.15
            ERGO genome analysis and discovery system: 3.5.4.15
            BRENDA, the Enzyme Database: 3.5.4.15
            CAS: 9067-85-0
///
ENTRY       EC 3.5.4.16                 Enzyme
NAME        GTP cyclohydrolase I;
            GTP cyclohydrolase;
            guanosine triphosphate cyclohydrolase;
            guanosine triphosphate 8-deformylase;
            dihydroneopterin triphosphate synthase;
            GTP 8-formylhydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     GTP 7,8-8,9-dihydrolase
REACTION    GTP + H2O = formate +
            2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine
            triphosphate [RN:R00424]
ALL_REAC    R00424;
            (other) R00428 R04639 R05046 R05048
SUBSTRATE   GTP [CPD:C00044];
            H2O [CPD:C00001]
PRODUCT     formate [CPD:C00058];
            2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine
            triphosphate [CPD:C04895]
COMMENT     The reaction involves hydrolysis of two C-N bonds and isomerization
            of the pentose unit; the recyclization may be non-enzymic.
REFERENCE   1  [PMID:4296838]
  AUTHORS   Burg AW, Brown GM.
  TITLE     The biosynthesis of folic acid. 8. Purification and properties of
            the enzyme that catalyzes the production of formate from carbon atom
            8 of guanosine triphosphate.
  JOURNAL   J. Biol. Chem. 243 (1968) 2349-58.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4904679]
  AUTHORS   Wolf WA, Brown GM.
  TITLE     The biosynthesis of folic acid. X. Evidence for an Amadori
            rearrangement in the enzymatic formation of dihydroneopterin
            triphosphate from GTP.
  JOURNAL   Biochim. Biophys. Acta. 192 (1969) 468-78.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K01495  GTP cyclohydrolase I
GENES       HSA: 2643(GCH1)
            MMU: 14528(Gch1)
            RNO: 29244(Gch)
            CFA: 609393(GCH1)
            GGA: 396146(GCH1)
            XTR: 448485(gch1)
            SPU: 580182(LOC580182) 583737(LOC583737)
            DME: Dmel_CG9441(Pu)
            CEL: F32G8.6(cat-4)
            OSA: 4337297
            CME: CMF055C
            SCE: YGR267C(FOL2)
            AGO: AGOS_AGR335C
            PIC: PICST_34960(GHC1)
            CGR: CAGL0F08503g
            SPO: SPAC17A5.13
            ANI: AN8188.2
            AFM: AFUA_3G13710 AFUA_5G03140
            AOR: AO090102000517
            UMA: UM06446.1
            DDI: DDB_0191399(gchA)
            PFA: PFL1155w
            TET: TTHERM_00425960
            ECO: b2153(folE)
            ECJ: JW2140(folE)
            ECE: Z3409(folE)
            ECS: ECs3045
            ECC: c2688(folE)
            ECI: UTI89_C2427(folE)
            ECP: ECP_2193
            ECV: APECO1_4398(folE)
            ECW: EcE24377A_2449(folE)
            ECX: EcHS_A2287(folE)
            STY: STY2427(folE)
            STT: t0662(folE)
            SPT: SPA0658(folE)
            SEC: SC2209(folE)
            STM: STM2193(folE)
            YPE: YPO1505(folE)
            YPK: y2664(folE)
            YPM: YP_1395(folE)
            YPA: YPA_0800
            YPN: YPN_2474
            YPP: YPDSF_1472
            YPS: YPTB1520(folE)
            YPI: YpsIP31758_2470(folE)
            SFL: SF2238(folE)
            SFX: S2367(folE)
            SFV: SFV_2228(folE)
            SSN: SSON_2209(folE)
            SBO: SBO_2174(folE)
            SDY: SDY_2127(folE)
            ECA: ECA2711(folE)
            PLU: plu1543(folE)
            BAS: BUsg129(folE)
            WBR: WGLp317(folE)
            SGL: SG0957
            ENT: Ent638_2753
            KPN: KPN_02591(folE)
            SPE: Spro_1560
            BFL: Bfl472(folE)
            BPN: BPEN_487(folE)
            HIN: HI1447(folE)
            HIT: NTHI1683(folE)
            HIP: CGSHiEE_04840(folE)
            HIQ: CGSHiGG_01125(folE)
            HDU: HD1103(folE)
            HSO: HS_0910(folE)
            PMU: PM0693(folE)
            MSU: MS1043(folE)
            APL: APL_0903(folE)
            ASU: Asuc_1295
            XFA: XF1983
            XFT: PD0823(folE)
            XCC: XCC4166(folE)
            XCB: XC_4253
            XCV: XCV4402(folE)
            XAC: XAC4302(folE)
            XOO: XOO4600(folE)
            XOM: XOO_4336(XOO4336)
            VCH: VCA0616
            VCO: VC0395_0558(folE)
            VVU: VV2_0543
            VVY: VVA1092
            VPA: VPA1169
            VFI: VF1607(folE)
            PPR: PBPRA2009
            PAE: PA1674(folE2) PA3438(folE1)
            PAU: PA14_19630(folE1) PA14_42850(folE2)
            PAP: PSPA7_1690(folE2) PSPA7_3598(folE1)
            PPU: PP_1823(folE-1) PP_2512(folE-2)
            PPF: Pput_3207 Pput_3888
            PST: PSPTO_1182(folE-1) PSPTO_2035(folE-2)
            PSB: Psyr_1020(folE) Psyr_1845(folE)
            PSP: PSPPH_1071(folE1) PSPPH_1805(folE2)
            PFL: PFL_0949(folE) PFL_2258(folE) PFL_4355(folE)
            PFO: Pfl_0891 Pfl_1715
            PEN: PSEEN1521(folE2) PSEEN2519
            PMY: Pmen_2744 Pmen_3289
            PAR: Psyc_1044(folE2)
            PCR: Pcryo_1425
            PRW: PsycPRwf_0955
            ACI: ACIAD2470(folE2)
            SON: SO_4254(folE)
            SDN: Sden_0321
            SFR: Sfri_3162 Sfri_3834
            SAZ: Sama_0322
            SBL: Sbal_0372
            SBM: Shew185_0371
            SLO: Shew_3486
            SPC: Sputcn32_0458
            SSE: Ssed_0380
            SPL: Spea_3842
            SHE: Shewmr4_3602
            SHM: Shewmr7_0354
            SHN: Shewana3_3775
            SHW: Sputw3181_0334
            CPS: CPS_2469(folE1) CPS_2678(folE2) CPS_2930(folE3)
            PHA: PSHAa0073(folE)
            PAT: Patl_0548
            SDE: Sde_2093
            MAQ: Maqu_3782
            CBU: CBU_0795(folE)
            CBD: COXBU7E912_0863(folE)
            LPN: lpg2766(folE2)
            LPF: lpl2683(folE)
            LPP: lpp2814(folE)
            MCA: MCA1670(folE)
            FTU: FTT0951c(folE)
            FTF: FTF0951c(folE)
            FTW: FTW_0849
            FTL: FTL_1253
            FTH: FTH_1230(folE)
            FTA: FTA_1326
            FTN: FTN_0830(folE)
            NOC: Noc_1390
            AEH: Mlg_1299
            HCH: HCH_00527(folE)
            CSA: Csal_2294
            MMW: Mmwyl1_3286
            AHA: AHA_1601(folE)
            DNO: DNO_0818
            BCI: BCI_0394(folE)
            VOK: COSY_0442(folE)
            CVI: CV_1130(folE) CV_2361(mtrA)
            RSO: RSc1387(folE)
            REU: Reut_B3671
            REH: H16_B1967(folE)
            RME: Rmet_3990
            BMA: BMAA0043(folE) BMAA0727 BMAA1092
            BMV: BMASAVP1_0090 BMASAVP1_0626 BMASAVP1_1197(folE)
            BML: BMA10299_0331 BMA10299_1480(folE)
            BMN: BMA10247_A0053(folE) BMA10247_A1258 BMA10247_A1698
            BXE: Bxe_B0641
            BVI: Bcep1808_3746 Bcep1808_5901
            BUR: Bcep18194_B3132(folE)
            BCN: Bcen_5116
            BCH: Bcen2424_5743
            BAM: Bamb_5014
            BPS: BPSS0040(folE) BPSS1248 BPSS1514(folE)
            BPM: BURPS1710b_A0248(folE) BURPS1710b_A0552(folE)
                 BURPS1710b_A1549(folE)
            BPL: BURPS1106A_A0051(folE)
            BPD: BURPS668_A0064(folE) BURPS668_A1761 BURPS668_A2146
            BTE: BTH_II0043
            PNU: Pnuc_0295
            RFR: Rfer_1301
            POL: Bpro_0869
            PNA: Pnap_0912
            AAV: Aave_3631
            AJS: Ajs_0879
            VEI: Veis_1329
            MPT: Mpe_A1074
            HAR: HEAR1481(folE)
            MMS: mma_1859(folE)
            NMU: Nmul_A2419
            EBA: ebA6179(folE)
            AZO: azo2133(folE) azo3509(gch)
            TBD: Tbd_0242(folE) Tbd_0481(folE)
            HPY: HP0928(folE)
            HPJ: jhp0862(folE_1) jhp0863(folE_2)
            HPA: HPAG1_0909 HPAG1_1339
            HHE: HH1712(folE)
            HAC: Hac_1087(folE)
            WSU: WS1225(folE)
            TDN: Tmden_2086
            CJE: Cj0194(folE)
            CJR: CJE0187(folE)
            CJJ: CJJ81176_0225(folE)
            CJU: C8J_0183(folE)
            CJD: JJD26997_0204(folE)
            CFF: CFF8240_1694(folE)
            CCV: CCV52592_1496(folE)
            CHA: CHAB381_0041(folE)
            CCO: CCC13826_0284 CCC13826_1778(folE)
            ABU: Abu_1642(folE)
            NIS: NIS_0005 NIS_0163(folE)
            SUN: SUN_0009 SUN_0139
            BBA: Bd2522(folE)
            ADE: Adeh_1965
            AFW: Anae109_1888
            MXA: MXAN_2955
            RPR: RP383(folE)
            RTY: RT0371(folE)
            RCO: RC0527(folE)
            RFE: RF_0599(folE)
            RBE: RBE_0803(folE)
            RAK: A1C_02870(folE)
            RBO: A1I_05145(folE)
            RRI: A1G_02990(folE)
            AMA: AM619(folE)
            APH: APH_0706(folE) APH_0814
            ERU: Erum4000(folE)
            ERW: ERWE_CDS_04130(folE)
            ERG: ERGA_CDS_04080(folE)
            ECN: Ecaj_0389
            ECH: ECH_0651(folE)
            NSE: NSE_0587(folE)
            PUB: SAR11_1245(folE)
            MLO: mlr0922
            MES: Meso_1004
            PLA: Plav_2664
            SME: SMc01005(folE)
            SMD: Smed_1049
            ATU: Atu1749(folE)
            ATC: AGR_C_3211
            RET: RHE_CH02201(folE)
            RLE: RL2531(folE) pRL120570
            BME: BMEI0910
            BMF: BAB1_1097
            BMS: BR1075(folE)
            BMB: BruAb1_1080(folE)
            BOV: BOV_1041(folE)
            OAN: Oant_2158
            BJA: bll5522(folE)
            BRA: BRADO2613 BRADO2984(folE)
            BBT: BBta_2960 BBta_5183(folE)
            RPA: RPA3391(gch1)
            RPB: RPB_2184
            RPC: RPC_3114
            RPD: RPD_3248
            RPE: RPE_0796 RPE_2348
            NWI: Nwi_1329
            NHA: Nham_1657
            BHE: BH07690(folE)
            BQU: BQ05540(folE)
            BBK: BARBAKC583_0644(folE)
            XAU: Xaut_1649
            CCR: CC_0459
            MMR: Mmar10_2399
            HNE: HNE_1855(folE1) HNE_3203(folE2)
            ZMO: ZMO1229(folE)
            NAR: Saro_1230 Saro_2007
            SAL: Sala_1911
            SWI: Swit_0582
            ELI: ELI_05020
            GOX: GOX1537
            GBE: GbCGDNIH1_0087
            ACR: Acry_2660
            RRU: Rru_A0271 Rru_A1832
            MAG: amb4223
            ABA: Acid345_2208
            SUS: Acid_1565
            BSU: BG10277(mtrA)
            BHA: BH1646(mtrA)
            BAN: BA1532(mtrA)
            BAR: GBAA1532(mtrA)
            BAA: BA_1886 BA_2052
            BAT: BAS1421
            BCE: BC1511(folE)
            BCA: BCE_1638(folE)
            BCZ: BCZK1393(folE)
            BCY: Bcer98_1234
            BTK: BT9727_1393(folE)
            BLI: BL02786(mtrA)
            BLD: BLi02413(mtrA)
            BCL: ABC1883(folE)
            BAY: RBAM_020940
            BPU: BPUM_2009(folE)
            GKA: GK2214(folE)
            LMO: lmo1933
            LMF: LMOf2365_1962(folE)
            LIN: lin2047
            LWE: lwe1959(folE)
            LLA: L0175(folE)
            LLC: LACR_1275
            LLM: llmg_1337(folE)
            SPY: SPy_1097(folE)
            SPZ: M5005_Spy_0821(folE)
            SPM: spyM18_1059(folE)
            SPG: SpyM3_0759(folE)
            SPS: SPs0959
            SPH: MGAS10270_Spy0937(folE)
            SPI: MGAS10750_Spy0972(folE)
            SPJ: MGAS2096_Spy0895(folE)
            SPK: MGAS9429_Spy0940(folE)
            SPF: SpyM50967(folE)
            SPA: M6_Spy0819(folE)
            SPB: M28_Spy0798(folE)
            SPN: SP_0291
            SPR: spr0268(sulC)
            SPD: SPD_0271(folE)
            SAG: SAG1116(folE)
            SAN: gbs1183
            SAK: SAK_1201(folE)
            SMU: SMU.968(folE)
            STC: str1544(folE)
            STL: stu1544(folE)
            SSA: SSA_0199(folE)
            SGO: SGO_1882(folE)
            LPL: lp_3297(folE)
            LSA: LSA1100(folE)
            LDB: Ldb0247(folKE)
            LBU: LBUL_0209
            LRE: Lreu_1278
            EFA: EF3267(folE)
            STH: STH990
            CAC: CAC3626(mtrA)
            CPE: CPE1019(mtrA)
            CPF: CPF_1274(folE)
            CPR: CPR_1096(folE)
            CNO: NT01CX_0377(folE)
            CTH: Cthe_2203
            CDF: CD1449(folE)
            CBO: CBO1556(folE)
            CBA: CLB_1577(folE)
            CBH: CLC_1588(folE)
            CBF: CLI_1638(folE)
            CBE: Cbei_2540
            CKL: CKL_0958(folE)
            AMT: Amet_2160
            CHY: CHY_0955(folE)
            DSY: DSY0603 DSY1825
            DRM: Dred_1758
            SWO: Swol_1408
            TTE: TTE2371(folE)
            MTA: Moth_0408
            MTU: Rv3609c(folE)
            MTC: MT3713(folE)
            MBO: Mb3639c(folE)
            MBB: BCG_3673c(folE)
            MLE: ML0223(folE)
            MPA: MAP0449(folE)
            MAV: MAV_0543(folE)
            MSM: MSMEG_6104(folE)
            MVA: Mvan_5371
            MGI: Mflv_1417
            MMC: Mmcs_4769
            MKM: Mkms_4855
            MJL: Mjls_5155
            CGL: NCgl2602(folE)
            CGB: cg2983(folE)
            CEF: CE2541
            CDI: DIP2001(folE)
            CJK: jk0279(folE)
            NFA: nfa31470(folE2) nfa3990(folE)
            RHA: RHA1_ro04408 RHA1_ro08281 RHA1_ro10349
            SCO: SCO3403(folE)
            SMA: SAV4667(folE)
            TWH: TWT587(folE)
            TWS: TW174(folE)
            LXX: Lxx21490(folE)
            ART: Arth_0152
            AAU: AAur_0139(folE)
            PAC: PPA0261
            NCA: Noca_0445 Noca_3354 Noca_4850
            TFU: Tfu_2894(folE)
            FRA: Francci3_1748 Francci3_4315
            FAL: FRAAL2747 FRAAL6589(folE2)
            ACE: Acel_0205 Acel_1665
            KRA: Krad_0539
            SEN: SACE_0397(folE) SACE_4692(folE2)
            STP: Strop_4307
            BLO: BL1683(folE)
            BAD: BAD_0410(folE)
            RXY: Rxyl_1171
            FNU: FN0071
            RBA: RB11853(folE)
            PCU: pc0449(folE)
            LIL: LA4255(folE)
            LIC: LIC13405(folE)
            LBJ: LBJ_2937(folE)
            LBL: LBL_0126(folE)
            SYN: slr0426(folE)
            SYW: SYNW1734(folE)
            SYC: syc0054_d(folE)
            SYF: Synpcc7942_1597
            SYD: Syncc9605_0732
            SYE: Syncc9902_1631
            SYG: sync_1986(folE)
            SYR: SynRCC307_1582(folE)
            SYX: SynWH7803_0658(folE)
            CYA: CYA_2792(folE)
            CYB: CYB_0188(folE)
            TEL: tll1309(folE)
            GVI: gll1580(folE)
            ANA: all4721 alr5287
            AVA: Ava_1949(folE) Ava_2537(folE)
            PMA: Pro0537(folE) Pro1579(folE)
            PMM: PMM0536(folE)
            PMT: PMT1227(folE)
            PMN: PMN2A_1027
            PMI: PMT9312_0536
            PMB: A9601_05921(folE)
            PMC: P9515_06001(folE)
            PMF: P9303_07841(folE)
            PMG: P9301_05621(folE)
            PME: NATL1_18971(folE)
            TER: Tery_0969 Tery_4616
            BTH: BT_3931
            BFR: BF3954
            BFS: BF3727(folE)
            PGI: PG0625(folE)
            SRU: SRU_2794(folE)
            CHU: CHU_0955(folE) CHU_1059(folE) CHU_1333(folE)
            GFO: GFO_1462(folE) GFO_2740(folE)
            FJO: Fjoh_2270
            FPS: FP0597(folE2) FP0634(folE1)
            CTE: CT0781(folE)
            CCH: Cag_0372(folE)
            CPH: Cpha266_0976
            PVI: Cvib_1082
            PLT: Plut_0754(folE)
            DET: DET1204(folE)
            DEH: cbdb_A1120(folE)
            DEB: DehaBAV1_1014
            RRS: RoseRS_0705
            RCA: Rcas_0301
            DRA: DR_0036
            DGE: Dgeo_0206
            TTH: TTC1517(folE)
            TTJ: TTHA1878
            AAE: aq_239(folE)
            HMA: pNG7382(folE)
            IHO: Igni_0632
            HBU: Hbut_0868
            SSO: SSO0364(folE)
            STO: ST1385
            SAI: Saci_1481(folE)
            MSE: Msed_1611
            PAI: PAE1588
            PIS: Pisl_1636
            PCL: Pcal_0512
            PAS: Pars_2122
STRUCTURES  PDB: 1A8R  1A9C  1FB1  1FBX  1GTP  1IS7  1IS8  1N3R  1N3S  1N3T  
                 1WM9  1WPL  1WUQ  1WUR  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.16
            ExPASy - ENZYME nomenclature database: 3.5.4.16
            ExplorEnz - The Enzyme Database: 3.5.4.16
            ERGO genome analysis and discovery system: 3.5.4.16
            BRENDA, the Enzyme Database: 3.5.4.16
            CAS: 37289-19-3
///
ENTRY       EC 3.5.4.17                 Enzyme
NAME        adenosine-phosphate deaminase;
            adenylate deaminase;
            adenine nucleotide deaminase;
            adenosine (phosphate) deaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     adenosine-phosphate aminohydrolase
REACTION    5'-AMP + H2O = 5'-IMP + NH3 [RN:R00181]
ALL_REAC    R00181;
            (other) R06137
SUBSTRATE   5'-AMP [CPD:C00020];
            H2O [CPD:C00001]
PRODUCT     5'-IMP [CPD:C00130];
            NH3 [CPD:C00014]
COMMENT     Acts on 5'-AMP, ADP, ATP, NAD+ and adenosine, in decreasing order of
            activity. The bacterial enzyme also acts on the deoxy derivatives.
            cf. EC 3.5.4.6 AMP deaminase.
REFERENCE   1  [PMID:5940938]
  AUTHORS   Su JC, Li CC, Ting CC.
  TITLE     A new adenylate deaminase from red marine alga Porphyra crispata.
  JOURNAL   Biochemistry. 5 (1966) 536-43.
  ORGANISM  Porphyra crispata
REFERENCE   2  [PMID:5773435]
  AUTHORS   Yates MG.
  TITLE     A non-specific adenine nucleotide deaminase from desulfovibrio
            desulfuricans.
  JOURNAL   Biochim. Biophys. Acta. 171 (1969) 299-310.
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.17
            ExPASy - ENZYME nomenclature database: 3.5.4.17
            ExplorEnz - The Enzyme Database: 3.5.4.17
            ERGO genome analysis and discovery system: 3.5.4.17
            BRENDA, the Enzyme Database: 3.5.4.17
            CAS: 37289-20-6
///
ENTRY       EC 3.5.4.18                 Enzyme
NAME        ATP deaminase;
            adenosine triphosphate deaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     ATP aminohydrolase
REACTION    ATP + H2O = ITP + NH3 [RN:R00088]
ALL_REAC    R00088;
            (other) R06137
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ITP [CPD:C00081];
            NH3 [CPD:C00014]
REFERENCE   1  [PMID:6048966]
  AUTHORS   Chung ST, Aida K.
  TITLE     Purification and properties of ATP deaminase from Microsporum
            audouini.
  JOURNAL   J. Biochem. (Tokyo). 61 (1967) 1-9.
  ORGANISM  Microsporum audouini
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.18
            ExPASy - ENZYME nomenclature database: 3.5.4.18
            ExplorEnz - The Enzyme Database: 3.5.4.18
            ERGO genome analysis and discovery system: 3.5.4.18
            BRENDA, the Enzyme Database: 3.5.4.18
            CAS: 37289-21-7
///
ENTRY       EC 3.5.4.19                 Enzyme
NAME        phosphoribosyl-AMP cyclohydrolase;
            PRAMP-cyclohydrolase;
            phosphoribosyladenosine monophosphate cyclohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     1-(5-phospho-D-ribosyl)-AMP 1,6-hydrolase
REACTION    1-(5-phosphoribosyl)-AMP + H2O =
            1-(5-phosphoribosyl)-5-[(5-
            phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
            [RN:R04037]
ALL_REAC    R04037
SUBSTRATE   1-(5-phosphoribosyl)-AMP [CPD:C02741];
            H2O [CPD:C00001]
PRODUCT     1-(5-phosphoribosyl)-5-[(5-
            phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
            [CPD:C04896]
COMMENT     The Neurospora crassa enzyme also catalyses the reactions of EC
            1.1.1.23 (histidinol dehydrogenase) and EC 3.6.1.31
            (phosphoribosyl-ATP diphosphatase).
REFERENCE   1  [PMID:4309307]
  AUTHORS   Minson AC, Creaser EH.
  TITLE     Purification of a trifunctional enzyme, catalysing three steps of
            the histidine pathway, from Neurospora crassa.
  JOURNAL   Biochem. J. 114 (1969) 49-56.
  ORGANISM  Neurospora crassa [GN:dncr]
PATHWAY     PATH: map00340  Histidine metabolism
ORTHOLOGY   KO: K01496  phosphoribosyl-AMP cyclohydrolase
GENES       ATH: AT1G31860(AT-IE)
            OSA: 4324261
            CME: CMQ383C
            AGO: AGOS_AFR703W
            PIC: PICST_89228(HIS2)
            ECO: b2026(hisI)
            ECJ: JW2008(hisI)
            ECE: Z3188(hisI)
            ECS: ECs2827
            ECC: c2553(hisI)
            ECI: UTI89_C2299(hisI)
            ECP: ECP_2069
            ECW: EcE24377A_2317(hisIE)
            ECX: EcHS_A2165(hisIE)
            STY: STY2287(hisI)
            STT: t0795(hisI)
            SPT: SPA0793(hisI)
            SEC: SC2088(hisI)
            STM: STM2078(hisI)
            YPE: YPO1542(hisI)
            YPK: y2628(hisI)
            YPM: YP_1431(hisI)
            YPA: YPA_0837
            YPN: YPN_2438
            YPS: YPTB1555(hisI)
            YPI: YpsIP31758_2435(hisI)
            SFL: SF2088(hisIE)
            SFX: S2209(hisI)
            SFV: SFV_2086(hisI)
            SSN: SSON_2097(hisI)
            SBO: SBO_0852(hisI)
            SDY: SDY_2215(hisI)
            ECA: ECA2589(hisI)
            PLU: plu1564(hisI)
            BUC: BU106(hisI)
            BAS: BUsg099(hisI)
            BAB: bbp100(hisI)
            BCC: BCc_070(hisI)
            SGL: SG1123
            BFL: Bfl469(hisI)
            BPN: BPEN_484(hisI)
            HIT: NTHI0606(hisI)
            PMU: PM1206(hisIE)
            MSU: MS1881(hisI)
            APL: APL_2028(hisI)
            XFA: XF2213
            XFT: PD1261(hisI)
            XCC: XCC1815(hisI)
            XCB: XC_2374
            XCV: XCV1881(hisIE)
            XAC: XAC1835(hisI)
            XOO: XOO2262(hisI)
            XOM: XOO_2123(XOO2123) XOO_2125(XOO2125)
            VCH: VC1139
            VVU: VV1_2913
            VVY: VV1357
            VPA: VP1144
            VFI: VF1019
            PPR: PBPRA1085
            PAE: PA5066(hisI)
            PAU: PA14_66940(hisI)
            PPU: PP_5014(hisI)
            PPF: Pput_4888
            PST: PSPTO_5153(hisI)
            PSB: Psyr_0386
            PSP: PSPPH_0369(hisI)
            PFL: PFL_0424 PFL_6181
            PFO: Pfl_0384
            PEN: PSEEN5076(hisI)
            PMY: Pmen_0520 Pmen_4539
            PAR: Psyc_1999(hisI)
            ACI: ACIAD0380(hisIE)
            SON: SO_2067(hisI)
            SDN: Sden_1611
            SFR: Sfri_1713
            SHE: Shewmr4_1793
            SHM: Shewmr7_2184
            SHN: Shewana3_1847
            ILO: IL1841(hisI)
            CPS: CPS_3896(hisI)
            PHA: PSHAb0482(hisI)
            PAT: Patl_2888
            SDE: Sde_3222
            MAQ: Maqu_3418
            LPN: lpg1193(hisI)
            LPF: lpl1201(hisI)
            LPP: lpp1195(hisI)
            MCA: MCA2801(hisI)
            TCX: Tcr_0217
            NOC: Noc_3055
            AEH: Mlg_1201
            HHA: Hhal_1726
            HCH: HCH_01079(hisI1) HCH_10001(hisI2)
            CSA: Csal_1883
            ABO: ABO_2134(hisI)
            MMW: Mmwyl1_2431
            AHA: AHA_2186
            BCI: BCI_0398(hisI)
            RMA: Rmag_0289
            VOK: COSY_0275
            NME: NMB0627
            NMA: NMA0837(hisI)
            NGO: NGO0210
            CVI: CV_0620(hisI)
            RSO: RSc2945(hisI)
            REU: Reut_A3104
            REH: H16_A3409(hisI)
            RME: Rmet_3241
            BMA: BMA2707(hisI)
            BMV: BMASAVP1_A3246(hisI)
            BML: BMA10299_A1795(hisI)
            BMN: BMA10247_2758(hisI)
            BXE: Bxe_A0405
            BVI: Bcep1808_0411
            BUR: Bcep18194_A3530
            BCN: Bcen_2675
            BCH: Bcen2424_0432
            BAM: Bamb_0350
            BPS: BPSL3132(hisI)
            BPM: BURPS1710b_3686(hisI)
            BPL: BURPS1106A_3717(hisI)
            BPD: BURPS668_3659(hisI)
            BTE: BTH_I2986
            PNU: Pnuc_0113
            BPE: BP3774(hisI)
            BPA: BPP4273(hisI)
            BBR: BB4860(hisI)
            RFR: Rfer_2952
            POL: Bpro_0810
            PNA: Pnap_0702
            AAV: Aave_1048
            AJS: Ajs_0776
            VEI: Veis_0705
            MPT: Mpe_A0837
            HAR: HEAR3063(hisI)
            MMS: mma_3282(hisI)
            NEU: NE0642(hisI)
            NET: Neut_1910
            NMU: Nmul_A0813
            EBA: ebB39(hisI)
            AZO: azo3343(hisI)
            DAR: Daro_3378
            TBD: Tbd_1707
            MFA: Mfla_0255
            HHE: HH0449(hisI)
            WSU: WS0090
            TDN: Tmden_1875
            CJE: Cj1604(hisI)
            CJR: CJE1776(hisI)
            CJU: C8J_1505(hisI)
            CCV: CCV52592_0853
            CCO: CCC13826_1896
            ABU: Abu_0121(hisI)
            NIS: NIS_1544(hisI)
            SUN: SUN_0237
            GSU: GSU1531(hisI)
            GME: Gmet_1897
            GUR: Gura_3243
            PCA: Pcar_2024 Pcar_2683
            PPD: Ppro_2944
            DVU: DVU0113(hisI)
            DVL: Dvul_2850
            DDE: Dde_3567
            DPS: DP2639
            MXA: MXAN_4222(hisIE)
            SAT: SYN_03110
            SFU: Sfum_4056
            PUB: SAR11_1246(hisI)
            MLO: mlr0923
            MES: Meso_1003
            PLA: Plav_2663
            SME: SMc01004(hisI)
            SMD: Smed_1048
            ATU: Atu1750(hisI)
            ATC: AGR_C_3213
            RET: RHE_CH00041(hisE) RHE_CH02202(hisI)
            RLE: RL2532(hisI)
            BME: BMEI0909
            BMF: BAB1_1098
            BMS: BR1076(hisI)
            BMB: BruAb1_1081(hisI)
            BOV: BOV_1042(hisI)
            OAN: Oant_2159
            BJA: bll5521(hisI)
            BRA: BRADO2985(hisI)
            BBT: BBta_5182(hisI)
            RPA: RPA3390(his3)
            RPB: RPB_2185
            RPC: RPC_3113
            RPD: RPD_3247
            RPE: RPE_2349
            NWI: Nwi_1330
            NHA: Nham_1658
            XAU: Xaut_1648
            CCR: CC_0457
            SIL: SPO1684(hisI)
            SIT: TM1040_1394
            RSP: RSP_2627(hisI)
            RSH: Rsph17029_1284
            RSQ: Rsph17025_1163
            JAN: Jann_2501
            RDE: RD1_2607(hisI)
            PDE: Pden_1336 Pden_4080
            MMR: Mmar10_1610
            HNE: HNE_3376
            ZMO: ZMO1178(hisI)
            NAR: Saro_2107
            SAL: Sala_1540
            SWI: Swit_0577
            ELI: ELI_05885
            GOX: GOX2021
            GBE: GbCGDNIH1_0969
            ACR: Acry_2265
            RRU: Rru_A1612
            MAG: amb2307
            MGM: Mmc1_3157
            ABA: Acid345_3681
            SUS: Acid_3857
            BSU: BG12603(hisI)
            BHA: BH3577(hisI)
            BAA: BA_1951
            BAT: BAS1322
            BCE: BC1411
            BCA: BCE_1531(hisI)
            BCZ: BCZK1296(hisI)
            BCY: Bcer98_1134
            BTK: BT9727_1295(hisI)
            BLI: BL03413(hisI)
            BLD: BLi03731(hisI)
            BCL: ABC3043(hisI)
            BAY: RBAM_032070(hisI)
            BPU: BPUM_3121(hisI)
            OIH: OB0546
            GKA: GK3070
            SAU: SA2464(hisI)
            SAV: SAV2672(hisI)
            SAM: MW2591(hisI)
            SAR: SAR2754(hisIE)
            SAS: SAS2557
            SAC: SACOL2696(hisI)
            SAB: SAB2548c(hisIE)
            SAA: SAUSA300_2605(hisIE)
            SEP: SE0277
            SER: SERP2300(hisIE)
            SSP: SSP0423(hisIE)
            LMO: lmo0562
            LMF: LMOf2365_0591(hisI)
            LIN: lin0571
            LWE: lwe0528(hisI)
            LLA: L0072(hisI)
            LLC: LACR_1326
            LLM: llmg_1289(hisI)
            SMU: SMU.1263(hisI)
            SSA: SSA_1441(hisI)
            SGO: SGO_1403(hisIE)
            LPL: lp_2553(hisI)
            LCA: LSEI_1428
            STH: STH2832(hisI)
            CAC: CAC0942(hisI_1)
            CDF: CD1554(hisI)
            CBO: CBO1573(hisI)
            CBA: CLB_1593(hisI)
            CBE: Cbei_1323
            CKL: CKL_1301(hisI)
            CHY: CHY_1091(hisIE)
            DSY: DSY3907
            SWO: Swol_1764
            TTE: TTE2132(hisI)
            MTU: Rv1606(hisI)
            MTC: MT1641.1(hisI)
            MBO: Mb1632(hisI)
            MBB: BCG_1644(hisI)
            MLE: ML1264(hisI)
            MPA: MAP1300(hisI2)
            MAV: MAV_3180
            MSM: MSMEG_3212(hisIE)
            MVA: Mvan_2811
            MGI: Mflv_3606
            MMC: Mmcs_3056
            MKM: Mkms_3115
            MJL: Mjls_3072
            CGL: NCgl2012(cgl2093)
            CGB: cg2296(hisI)
            CEF: CE1993
            CDI: DIP1557(hisI)
            CJK: jk0794(hisI)
            NFA: nfa18540(hisI)
            RHA: RHA1_ro01021(hisI2)
            SCO: SCO2044(SC4G6.13c)
            SMA: SAV6170(hisI)
            LXX: Lxx11240(hisI)
            ART: Arth_1683
            AAU: AAur_1834(hisI)
            PAC: PPA1126
            NCA: Noca_3032
            TFU: Tfu_1159
            FRA: Francci3_3021
            FAL: FRAAL4973(hisI)
            ACE: Acel_1070
            KRA: Krad_2969
            SEN: SACE_5755(hisI)
            STP: Strop_3176
            BLO: BL0686(hisI)
            BAD: BAD_0788(hisI)
            RBA: RB11983(hisI)
            LIL: LA0551(hisI)
            LIC: LIC13016(hisI)
            LBJ: LBJ_0634(hisI)
            LBL: LBL_2445(hisI)
            SYN: slr0608(hisI)
            SYW: SYNW1505(hisIE)
            SYC: syc2101_d(hisIE)
            SYF: Synpcc7942_1995
            SYG: sync_1899(hisIE)
            SYR: SynRCC307_1619(hisIE)
            SYX: SynWH7803_0746(hisIE)
            CYA: CYA_0504(hisIE)
            CYB: CYB_0157(hisIE)
            TEL: tll0233(hisIE)
            GVI: glr1211(hisIE)
            ANA: all3263
            AVA: Ava_4918 Ava_B0230
            PMA: Pro0582(hisI)
            PMM: PMM0578
            PMT: PMT0453(hisI)
            PMN: PMN2A_0014(hisIE)
            PMI: PMT9312_0578
            PMB: A9601_06341(hisI)
            PMC: P9515_06431(hisI)
            PMF: P9303_18291(hisI)
            PMG: P9301_06041(hisI)
            PMH: P9215_06601(hisI)
            PME: NATL1_06341(hisI)
            TER: Tery_2490 Tery_2740
            BTH: BT_1377
            BFR: BF3052
            BFS: BF2888(hisI)
            SRU: SRU_1018
            CHU: CHU_2337(hisI)
            GFO: GFO_1757(hisIE)
            FPS: FP0953(hisIE)
            CTE: CT0463(hisI)
            CCH: Cag_0559
            CPH: Cpha266_0479
            PVI: Cvib_1481
            PLT: Plut_1696
            DET: DET1329(hisI)
            DEH: cbdb_A1276(hisI)
            DEB: DehaBAV1_1140
            DRA: DR_0733
            DGE: Dgeo_1901
            TTH: TTC1080
            TTJ: TTHA1445
            AAE: aq_1968(hisIE)
            TMA: TM1035
            MJA: MJ1430(hisIE)
            MMP: MMP0280(hisI)
            MMZ: MmarC7_1283
            MAE: Maeo_0051
            MAC: MA0908
            MBA: Mbar_A3654
            MMA: MM_2019
            MBU: Mbur_1790
            MTP: Mthe_1155
            MHU: Mhun_2051
            MEM: Memar_2006
            MBN: Mboo_1916
            MTH: MTH245
            MST: Msp_0649(hisI)
            MSI: Msm_1182
            MKA: MK1537(hisI_2)
            AFU: AF1950(hisIE)
            HAL: VNG2284G(hisJ)
            HMA: rrnAC2524(hisI2)
            HWA: HQ1022A(hisI)
            NPH: NP5154A(hisI)
            PTO: PTO1331
            PFU: PF1664
            TKO: TK0249
            RCI: RCIX21(hisI)
            IHO: Igni_0562
            SSO: SSO6227(hisI)
            STO: ST1467
            SAI: Saci_1582(hisI)
            PAI: PAE0957
            PIS: Pisl_1211
            PCL: Pcal_0131
            PAS: Pars_0158
STRUCTURES  PDB: 1ZPS  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.19
            ExPASy - ENZYME nomenclature database: 3.5.4.19
            ExplorEnz - The Enzyme Database: 3.5.4.19
            ERGO genome analysis and discovery system: 3.5.4.19
            BRENDA, the Enzyme Database: 3.5.4.19
            CAS: 37289-22-8
///
ENTRY       EC 3.5.4.20                 Enzyme
NAME        pyrithiamine deaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-methy
            lpyridinium-bromide aminohydrolase
REACTION    1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-
            methylpyridinium bromide + H2O =
            1-(4-hydroxy-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-
            methylpyridinium bromide + NH3 [RN:R04641]
ALL_REAC    R04641;
            (other) R06137
SUBSTRATE   1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-
            methylpyridinium bromide [CPD:C04905];
            H2O [CPD:C00001]
PRODUCT     1-(4-hydroxy-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-
            methylpyridinium bromide [CPD:C04908];
            NH3 [CPD:C00014]
REFERENCE   1  [PMID:5641872]
  AUTHORS   Sinha AK, Chatterjee GC.
  TITLE     Metabolism of pyrithiamine by the pyrithiamine-requiring mutant of
            Staphylococcus aureus.
  JOURNAL   Biochem. J. 107 (1968) 165-9.
  ORGANISM  Staphylococcus aureus
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.20
            ExPASy - ENZYME nomenclature database: 3.5.4.20
            ExplorEnz - The Enzyme Database: 3.5.4.20
            ERGO genome analysis and discovery system: 3.5.4.20
            BRENDA, the Enzyme Database: 3.5.4.20
            CAS: 37289-23-9
///
ENTRY       EC 3.5.4.21                 Enzyme
NAME        creatinine deaminase;
            creatinine hydrolase;
            creatinine desiminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     creatinine iminohydrolase
REACTION    creatinine + H2O = N-methylhydantoin + NH3 [RN:R02922]
ALL_REAC    R02922;
            (other) R06137
SUBSTRATE   creatinine [CPD:C00791];
            H2O [CPD:C00001]
PRODUCT     N-methylhydantoin [CPD:C02565];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Szulmajster, J.
  TITLE     Bacterial degradation of creatinine. II. Creatinine desimidase.
  JOURNAL   Biochim. Biophys. Acta 30 (1958) 154-163.
  ORGANISM  Clostridium paraputrificum
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K03365  creatinine deaminase
GENES       CGL: NCgl0075(cgl0076)
            CGB: cg0104(codA)
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.21
            ExPASy - ENZYME nomenclature database: 3.5.4.21
            ExplorEnz - The Enzyme Database: 3.5.4.21
            ERGO genome analysis and discovery system: 3.5.4.21
            BRENDA, the Enzyme Database: 3.5.4.21
            CAS: 37289-15-9
///
ENTRY       EC 3.5.4.22                 Enzyme
NAME        1-pyrroline-4-hydroxy-2-carboxylate deaminase;
            HPC deaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     1-pyrroline-4-hydroxy-2-carboxylate aminohydrolase (decyclizing)
REACTION    1-pyrroline-4-hydroxy-2-carboxylate + H2O = 2,5-dioxopentanoate +
            NH3 [RN:R02280]
ALL_REAC    R02280
SUBSTRATE   1-pyrroline-4-hydroxy-2-carboxylate [CPD:C04282];
            H2O [CPD:C00001]
PRODUCT     2,5-dioxopentanoate [CPD:C00433];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Singh, R.M.M. and Adams, E.
  TITLE     Enzymatic deamination of Delta1-pyrroline-4-hydroxy-2-carboxylate to
            2,5-dioxovalerate (alpha-ketoglutaric semialdehyde).
  JOURNAL   J. Biol. Chem. 240 (1965) 4344-4351.
  ORGANISM  Pseudomonas striata
REFERENCE   2
  AUTHORS   Singh, R.M.M. and Adams, E.
  TITLE     Isolation and identification of 2,5-dioxovalerate, an intermediate
            in the bacterial oxidation of hydroxyproline.
  JOURNAL   J. Biol. Chem. 240 (1965) 4352-4356.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00330  Arginine and proline metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.22
            ExPASy - ENZYME nomenclature database: 3.5.4.22
            ExplorEnz - The Enzyme Database: 3.5.4.22
            ERGO genome analysis and discovery system: 3.5.4.22
            BRENDA, the Enzyme Database: 3.5.4.22
            CAS: 9054-77-7
///
ENTRY       EC 3.5.4.23                 Enzyme
NAME        blasticidin-S deaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     blasticidin-S aminohydrolase
REACTION    blasticidin S + H2O = deaminohydroxyblasticidin S + NH3 [RN:R03800]
ALL_REAC    R03800;
            (other) R06137
SUBSTRATE   blasticidin S [CPD:C02010];
            H2O [CPD:C00001]
PRODUCT     deaminohydroxyblasticidin S [CPD:C03860];
            NH3 [CPD:C00014]
COMMENT     Catalyses the deamination of the cytosine moiety of the antibiotics
            blasticidin S, cytomycin and acetylblasticidin S.
REFERENCE   1  [PMID:236272]
  AUTHORS   Yamaguchi I, Shibata H, Seto H, Misato T.
  TITLE     Isolation and purification of blasticidin S deaminase from
            Aspergillus terreus.
  JOURNAL   J. Antibiot. (Tokyo). 28 (1975) 7-14.
  ORGANISM  Aspergillus terreus
ORTHOLOGY   KO: K06017  
GENES       GBE: GbCGDNIH1_1383
            BCZ: BCZK2582(bsr)
            BTL: BALH_0018 BALH_2561
STRUCTURES  PDB: 1WN5  1WN6  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.23
            ExPASy - ENZYME nomenclature database: 3.5.4.23
            ExplorEnz - The Enzyme Database: 3.5.4.23
            ERGO genome analysis and discovery system: 3.5.4.23
            BRENDA, the Enzyme Database: 3.5.4.23
            CAS: 54576-55-5
///
ENTRY       EC 3.5.4.24                 Enzyme
NAME        sepiapterin deaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     sepiapterin aminohydrolase
REACTION    sepiapterin + H2O = xanthopterin-B2 + NH3 [RN:R02974]
ALL_REAC    R02974;
            (other) R06137
SUBSTRATE   sepiapterin [CPD:C00835];
            H2O [CPD:C00001]
PRODUCT     xanthopterin-B2 [CPD:C02333];
            NH3 [CPD:C00014]
COMMENT     Also acts on isosepiapterin, but more slowly.
REFERENCE   1  [PMID:5572808]
  AUTHORS   Tsusue M.
  TITLE     Studies on sepiapterin deaminase from the silkworm, Bombyx mori.
            Purification and some properties of the enzyme.
  JOURNAL   J. Biochem. (Tokyo). 69 (1971) 781-8.
  ORGANISM  Bombyx mori [GN:dbmo]
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.24
            ExPASy - ENZYME nomenclature database: 3.5.4.24
            ExplorEnz - The Enzyme Database: 3.5.4.24
            ERGO genome analysis and discovery system: 3.5.4.24
            BRENDA, the Enzyme Database: 3.5.4.24
            CAS: 62213-22-3
///
ENTRY       EC 3.5.4.25                 Enzyme
NAME        GTP cyclohydrolase II;
            guanosine triphosphate cyclohydrolase II;
            GTP-8-formylhydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     GTP 7,8-8,9-dihydrolase (diphosphate-forming)
REACTION    GTP + 3 H2O = formate +
            2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine +
            diphosphate [RN:R00425]
ALL_REAC    R00425
SUBSTRATE   GTP [CPD:C00044];
            H2O [CPD:C00001]
PRODUCT     formate [CPD:C00058];
            2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine;
            diphosphate [CPD:C00013]
COMMENT     Two C-N bonds are hydrolysed, releasing formate, with simultaneous
            removal of the terminal diphosphate.
REFERENCE   1  [PMID:235552]
  AUTHORS   Foor F, Brown GM.
  TITLE     Purification and properties of guanosine triphosphate cyclohydrolase
            II from Escherichia coli.
  JOURNAL   J. Biol. Chem. 250 (1975) 3545-51.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00740  Riboflavin metabolism
ORTHOLOGY   KO: K01497  GTP cyclohydrolase II
GENES       ATH: AT2G22450 AT5G59750
            OSA: 4339017
            CME: CMP119C
            SCE: YBL033C(RIB1)
            AGO: AGOS_ADL296C
            PIC: PICST_30471(RIB1)
            CGR: CAGL0F04279g
            SPO: SPAP27G11.09c
            ANI: AN0670.2
            AFM: AFUA_1G13300 AFUA_2G01220
            AOR: AO090012000551
            CNE: CNA05500
            UMA: UM04826.1
            ECO: b1277(ribA)
            ECJ: JW1269(ribA)
            ECE: Z2531(ribA)
            ECS: ECs1850
            ECC: c1746(ribA)
            ECI: UTI89_C1548(ribA) UTI89_C3483(ribB)
            ECP: ECP_1330
            ECV: APECO1_437(ribA)
            ECW: EcE24377A_1479(ribA)
            ECX: EcHS_A1388(ribA)
            STY: STY1340(ribA)
            STT: t1624(ribA)
            SPT: SPA1165(ribA)
            SEC: SC1706(ribA)
            STM: STM1711(ribA)
            YPE: YPO2222(ribA)
            YPK: y2064(ribA)
            YPM: YP_2020(ribA)
            YPA: YPA_1581
            YPN: YPN_1690
            YPP: YPDSF_0912
            YPS: YPTB2144(ribA)
            YPI: YpsIP31758_1919(ribA)
            SFX: S1364(ribA)
            SFV: SFV_1290(ribA)
            SSN: SSON_1863(ribA)
            SBO: SBO_1787(ribA)
            SDY: SDY_1353(ribA)
            ECA: ECA1943(ribA)
            PLU: plu2431(ribA) plu2474
            BUC: BU271(ribA)
            BAS: BUsg261(ribA)
            BAB: bbp252(ribA)
            WBR: WGLp364(ribA)
            SGL: SG1410
            ENT: Ent638_2191
            SPE: Spro_2653
            BFL: Bfl425(ribA)
            BPN: BPEN_067(ribB) BPEN_437(ribA)
            HIN: HI0212(ribA)
            HIT: NTHI0309(ribA) NTHI0925(ribB)
            HDU: HD1163(ribAB)
            HSO: HS_1043(ribA)
            PMU: PM0677(ribA)
            MSU: MS1533(ribA)
            APL: APL_0384(ribA)
            ASU: Asuc_1502
            XFA: XF0953 XF1992
            XFT: PD0817(ribA) PD1745(ribA)
            XCC: XCC0696(ribA) XCC3740(ribA)
            XCB: XC_3538 XC_3810
            XCV: XCV0801(ribB) XCV3916
            XAC: XAC0749(ribA) XAC3792(ribA)
            XOO: XOO0594(ribA) XOO3853(ribA)
            XOM: XOO_0555(XOO0555) XOO_3632(XOO3632)
            VCH: VC1263 VC2269
            VCO: VC0395_A0882(ribA) VC0395_A1859(ribB)
            VVU: VV1_0321 VV1_2234 VV2_1180
            VVY: VV0863 VV2120 VVA0006
            VPA: VP0681 VP1921 VPA0006
            VFI: VF0702 VF1189(ribA)
            PPR: PBPRA0799 PBPRA1519 PBPRA1520 PBPRB1461
            PAE: PA4047(ribA) PA4054(ribB)
            PAU: PA14_11420(ribB) PA14_11510(ribA)
            PPU: PP_0516(ribBA-1) PP_0522(ribA) PP_3813(ribBA-2)
            PPF: Pput_0557 Pput_1956
            PST: PSPTO_0692(ribBA-1) PSPTO_0696(ribA) PSPTO_2668(ribBA-2)
            PSB: Psyr_2402 Psyr_4456(ribA) Psyr_4460
            PSP: PSPPH_2560(ribBA1) PSPPH_4501(ribA) PSPPH_4505(ribBA2)
            PFL: PFL_1034(ribA) PFL_5514(ribA) PFL_5520(ribA)
            PFO: Pfl_3240 Pfl_5011 Pfl_5017
            PEN: PSEEN0590(ribB) PSEEN0596(ribA) PSEEN3037(ribB)
            PMY: Pmen_3446 Pmen_3848
            PAR: Psyc_0093(ribB) Psyc_0220(ribA)
            PCR: Pcryo_0102 Pcryo_0244
            PRW: PsycPRwf_0410
            ACI: ACIAD3249(ribA) ACIAD3570(ribB)
            SON: SO_2831(ribA) SO_3467(ribBA)
            SDN: Sden_1146 Sden_1447
            SFR: Sfri_1037 Sfri_2438
            SAZ: Sama_1277
            SBL: Sbal_1668
            SBM: Shew185_1653
            SLO: Shew_2446
            SPC: Sputcn32_1543
            SSE: Ssed_1603
            SPL: Spea_2616
            SHE: Shewmr4_1098 Shewmr4_2438
            SHM: Shewmr7_1164 Shewmr7_2508
            SHN: Shewana3_1098 Shewana3_2600
            SHW: Sputw3181_2556
            ILO: IL1869(ribAB)
            CPS: CPS_0732(ribB) CPS_1824 CPS_4061(ribA)
            PHA: PSHAa0529(ribA) PSHAa2372(ribB)
            PAT: Patl_1313 Patl_3961
            SDE: Sde_3450 Sde_3456
            PIN: Ping_0518
            MAQ: Maqu_0844 Maqu_2439
            CBU: CBU_0647(ribA)
            CBD: COXBU7E912_0658(ribAB)
            LPN: lpg1179(ribA)
            LPF: lpl1188(ribA)
            LPP: lpp1182(ribA)
            MCA: MCA1656(ribBA) MCA2476
            FTU: FTT1673(ribA)
            FTF: FTF1673(ribA)
            FTW: FTW_1944(ribAB)
            FTL: FTL_0076
            FTH: FTH_0072(ribA)
            FTN: FTN_0112(ribAB)
            TCX: Tcr_1398
            NOC: Noc_2023
            AEH: Mlg_0377
            HHA: Hhal_0898
            HCH: HCH_05867 HCH_05955
            CSA: Csal_0115 Csal_1172 Csal_2584
            ABO: ABO_2172(dhbP)
            MMW: Mmwyl1_2026
            AHA: AHA_1807(ribA) AHA_3331
            DNO: DNO_0472(ribB)
            BCI: BCI_0300(ribA)
            VOK: COSY_0463(ribAB)
            NME: NMB1254 NMB1256
            NMA: NMA1425(ribA) NMA1429(ribB)
            NMC: NMC1155(ribA)
            NGO: NGO0704 NGO1134
            CVI: CV_2005(ribA) CV_2389(ribAB)
            RSO: RSc0713(ribAB)
            REU: Reut_A0770 Reut_A1536 Reut_B4241
            REH: H16_B1576(ribA)
            RME: Rmet_0194 Rmet_2693
            BMA: BMA2145(ribBA) BMAA1048(toxB) BMAA1349(ribA)
            BMV: BMASAVP1_0035(toxB) BMASAVP1_0332(ribA) BMASAVP1_A0764(ribBA)
            BML: BMA10299_0379(toxB) BMA10299_0610(ribA) BMA10299_A2597(ribBA)
            BMN: BMA10247_2016(ribBA) BMA10247_A0959(ribA)
                 BMA10247_A1205(toxB)
            BXE: Bxe_A0893 Bxe_B1675
            BVI: Bcep1808_5269
            BUR: Bcep18194_A4058 Bcep18194_B1027 Bcep18194_B1621
            BCN: Bcen_3636
            BCH: Bcen2424_4731
            BAM: Bamb_0818 Bamb_1629 Bamb_4122
            BPS: BPSL2626(ribB) BPSS0883(ribA) BPSS1121
            BPM: BURPS1710b_3102(ribBA) BURPS1710b_A0081(toxB)
                 BURPS1710b_A2481(ribA)
            BPL: BURPS1106A_3069(ribBA) BURPS1106A_A1220(ribA)
                 BURPS1106A_A1501
            BPD: BURPS668_3016 BURPS668_A1292(ribA) BURPS668_A1584
            BTE: BTH_I1531(ribBA) BTH_II1285 BTH_II1514(ribA)
            BPE: BP3484(ribB)
            BPA: BPP0857(ribB)
            BBR: BB0951(ribB)
            RFR: Rfer_2668
            POL: Bpro_2885
            MPT: Mpe_A2947
            HAR: HEAR0565(ribA) HEAR1036(ribB)
            MMS: mma_0548(ribA) mma_2340(ribBA)
            NEU: NE2556(ribAB)
            NET: Neut_2516
            NMU: Nmul_A0010
            EBA: ebA3120(ribA) ebA3567(ribAB)
            AZO: azo0319(ribAB) azo3765(ribA)
            DAR: Daro_3737
            TBD: Tbd_2190
            MFA: Mfla_1358 Mfla_2098
            HPY: HP0802(ribA) HP0804
            HPJ: jhp0738(ribA) jhp0740(ribBA)
            HPA: HPAG1_0787 HPAG1_0789
            HHE: HH0044(ribA) HH0208
            HAC: Hac_0920(ribA) Hac_0924(ribA)
            WSU: WS1194(ribA) WS1222(ribA)
            TDN: Tmden_0384 Tmden_1189
            CJE: Cj0572(ribA) Cj0996(ribA)
            CJR: CJE0675(ribB) CJE1076(ribA)
            CJJ: CJJ81176_1014(ribA)
            CJU: C8J_0534(ribB) C8J_0933(ribA)
            CJD: JJD26997_0793(ribA)
            CFF: CFF8240_0999 CFF8240_1575(ribA)
            CCV: CCV52592_1346(ribA)
            CHA: CHAB381_1325 CHAB381_1699(ribA)
            CCO: CCC13826_0883(ribA) CCC13826_1035 CCC13826_1413 CCC13826_1973
            ABU: Abu_1228(ribAB) Abu_1237(ribA)
            NIS: NIS_0359(ribA) NIS_0682
            SUN: SUN_1141 SUN_2088(ribA)
            GSU: GSU1690(ribA)
            GME: Gmet_1626
            GUR: Gura_2181
            PCA: Pcar_1447
            PPD: Ppro_1652
            DVU: DVU1199(ribAB)
            DVL: Dvul_1858
            DDE: Dde_2436
            LIP: LI0155(ribA)
            BBA: Bd3038(ribA)
            DPS: DP1100(ribA)
            ADE: Adeh_0508 Adeh_1663 Adeh_2740
            AFW: Anae109_2140 Anae109_2729
            MXA: MXAN_0122 MXAN_3410(ribBA) MXAN_4213(ribA)
            SAT: SYN_02371
            SFU: Sfum_1380
            WOL: WD0003(ribA) WD0653
            WBM: Wbm0278 Wbm0312
            AMA: AM1172(ribA) AM1317(ribA)
            APH: APH_1314(ribA) APH_1332(ribB)
            ERU: Erum0310 Erum0800(ribB)
            ERW: ERWE_CDS_00180(ribA) ERWE_CDS_00750(ribB)
            ERG: ERGA_CDS_00180(ribA) ERGA_CDS_00720(ribB)
            ECN: Ecaj_0023 Ecaj_0085
            ECH: ECH_0045 ECH_0134(ribB)
            NSE: NSE_0745(ribA)
            PUB: SAR11_1044(ribA)
            MLO: mlr7463
            MES: Meso_0731
            SME: SMc00008(ribA)
            ATU: Atu0753(ribA)
            ATC: AGR_C_1366
            RET: RHE_PD00121(ribA)
            RLE: RL1006(ribA) RL2726(ribA)
            BME: BMEI1505
            BMF: BAB1_0455
            BMS: BR0429(ribAB)
            BOV: BOV_0436(ribAB)
            BJA: blr2615(ribA)
            BRA: BRADO2133
            BBT: BBta_2450
            RPA: RPA1093(ribB)
            RPB: RPB_1161
            RPC: RPC_4298
            RPD: RPD_1263
            RPE: RPE_4357
            NWI: Nwi_0607
            NHA: Nham_0752
            BHE: BH04330(ribA)
            BQU: BQ03520(ribA)
            BBK: BARBAKC583_0398(ribBA)
            XAU: Xaut_2038
            CCR: CC_0887
            SIL: SPO1761 SPO3427(ribBA)
            SIT: TM1040_0050 TM1040_2129
            RSP: RSP_0757(ribBA) RSP_0846(ribA)
            RSH: Rsph17029_2504
            RSQ: Rsph17025_3129
            JAN: Jann_0416 Jann_3414
            RDE: RD1_0043(ribA) RD1_1801(ribB)
            PDE: Pden_2375
            MMR: Mmar10_1533
            HNE: HNE_2056(ribAB)
            ZMO: ZMO0474(ribB) ZMO1698(ribA)
            NAR: Saro_3191
            SAL: Sala_2672
            SWI: Swit_3789
            ELI: ELI_11975
            GOX: GOX0980
            GBE: GbCGDNIH1_1005
            ACR: Acry_2815
            RRU: Rru_A1823 Rru_A3637
            MAG: amb0020 amb2344
            MGM: Mmc1_0166
            ABA: Acid345_2148 Acid345_3140
            SUS: Acid_1908 Acid_2182
            BSU: BG10520(ribA)
            BHA: BH1556(ribA)
            BAN: BA4333(ribBA)
            BAR: GBAA4333(ribBA)
            BAA: BA_4791
            BAT: BAS4020
            BCE: BC3388 BC4111
            BCA: BCE_4181(ribBA)
            BCZ: BCZK3097(ribBA) BCZK3867(ribA) pE33L466_0153(ribA)
            BCY: Bcer98_2810
            BTK: BT9727_3853(ribA)
            BLI: BL01889(ribA)
            BLD: BLi02473(ribA)
            BCL: ABC1812(ribA)
            BAY: RBAM_021400(ribA)
            BPU: BPUM_0700 BPUM_2060(ribA) BPUM_3531(ribAB)
            OIH: OB0424 OB3214
            GKA: GK2295
            SAU: SA1587(ribA)
            SAV: SAV1769(ribA)
            SAM: MW1709(ribA)
            SAR: SAR1851(ribA)
            SAS: SAS1692
            SAC: SACOL1818(ribBA)
            SAB: SAB1626c(ribA)
            SAA: SAUSA300_1713(ribBA)
            SAO: SAOUHSC_01887
            SAJ: SaurJH9_1821
            SAH: SaurJH1_1856
            SEP: SE1439
            SER: SERP1326(ribBA)
            SHA: SH1155(ribA)
            SSP: SSP0997
            LLA: L0165(ribA)
            LLC: LACR_1074
            LLM: llmg_1530(ribA)
            SPN: SP_0176
            SPR: spr0162(ribA)
            SPD: SPD_0167(ribB)
            SAG: SAG0748(ribA)
            SAN: gbs0769
            SAK: SAK_0874(ribBA)
            LPL: lp_1437(ribA)
            LBR: LVIS_1651
            LRE: Lreu_0880
            CAC: CAC0592(ribA)
            CPE: CPE0568(ribA)
            CPF: CPF_0548(ribA)
            CPR: CPR_0532(ribA)
            CTC: CTC00673(ribA)
            CNO: NT01CX_0713
            CTH: Cthe_0106
            CDF: CD1698(ribA)
            CBO: CBO2864(ribA)
            CBA: CLB_2830(ribAB)
            CBH: CLC_2763(ribAB)
            CBF: CLI_2920(ribAB)
            CBE: Cbei_1226
            AMT: Amet_1020
            CHY: CHY_1473(ribBA)
            DSY: DSY1664(ribA)
            DRM: Dred_2091
            SWO: Swol_1220
            CSC: Csac_0792
            MTA: Moth_0917
            MMO: MMOB5970(ribA)
            MTU: Rv1415(ribA2) Rv1940(ribA1)
            MTC: MT1458 MT1990
            MBO: Mb1450(ribA2) Mb1975(ribA1)
            MBB: BCG_1476(ribA2) BCG_1979(ribA1)
            MLE: ML0559(ribA)
            MPA: MAP1140(ribA2)
            MAV: MAV_3365
            MSM: MSMEG_3072 MSMEG_3471
            MVA: Mvan_2694
            MGI: Mflv_3719
            MMC: Mmcs_2390 Mmcs_5190
            MKM: Mkms_2437
            MJL: Mjls_2431
            CGL: NCgl1533(cgl1595)
            CGB: cg1798(ribA)
            CEF: CE1714(ribA)
            CDI: DIP1317(ribA)
            CJK: jk1008(ribA)
            NFA: nfa36000(ribBA)
            RHA: RHA1_ro00258 RHA1_ro07170(ribA) RHA1_ro11048 RHA1_ro11307
            SCO: SCO1441(ribAB) SCO2687(ribA1) SCO6655(ribA2)
            SMA: SAV1791(ribA2) SAV4121(ribA3) SAV545(ribA4) SAV6904(ribA1)
            TWH: TWT689 TWT690
            TWS: TW708(ribB) TW709(ribA)
            LXX: Lxx04350(ribA)
            CMI: CMM_0961(ribAB)
            ART: Arth_1677
            PAC: PPA1750
            NCA: Noca_0866 Noca_1684 Noca_2449
            TFU: Tfu_1080
            FRA: Francci3_3186
            FAL: FRAAL5220(ribA)
            ACE: Acel_1272
            KRA: Krad_0125
            SEN: SACE_2123(ribA) SACE_2786(ribA) SACE_2884(toxB)
            STP: Strop_1877 Strop_2559
            RXY: Rxyl_1366
            FNU: FN1508
            RBA: RB12480(ribA)
            CTR: CT731(ribA)
            CTA: CTA_0793(ribA)
            CMU: TC0104
            CPN: CPn0872(ribA)
            CPA: CP0997
            CPJ: CPj0872(ribA_ribB)
            CPT: CpB0901
            CCA: CCA00895(ribA)
            CAB: CAB863(ribA)
            CFE: CF0119(ribA)
            PCU: pc0890(ribA)
            LIL: LA1147(ribA)
            LIC: LIC12534(ribA)
            LBJ: LBJ_2150(ribAB)
            LBL: LBL_2144(ribAB)
            SYN: sll1894(ribA)
            SYW: SYNW1263(ribA)
            SYC: syc0124_d(ribA)
            SYF: Synpcc7942_1432
            SYD: Syncc9605_1390
            SYE: Syncc9902_1098
            SYG: sync_1383(ribAB)
            SYR: SynRCC307_1354(ribA)
            SYX: SynWH7803_1252(ribA)
            CYA: CYA_2473(ribAB)
            CYB: CYB_2077(ribAB)
            TEL: tlr1727(ribA)
            GVI: glr0988(ribA)
            ANA: all3536
            AVA: Ava_3515
            PMA: Pro0943(ribB)
            PMM: PMM0893(ribA)
            PMT: PMT0708(ribA)
            PMN: PMN2A_0317
            PMI: PMT9312_0907
            PMB: A9601_09681(ribB)
            PMC: P9515_09751(ribB)
            PMF: P9303_15131(ribB)
            PMG: P9301_09661(ribB)
            PME: NATL1_09901(ribB)
            TER: Tery_4462
            BTH: BT_2416
            BFR: BF0594
            BFS: BF0544(ribA)
            PGI: PG0599(ribBA)
            SRU: SRU_0007(rpe) SRU_0012(ribBA)
            CHU: CHU_0931(ribA)
            GFO: GFO_2186(ribA)
            FPS: FP1589(ribBA)
            CTE: CT1591(ribBA)
            CCH: Cag_1788
            CPH: Cpha266_0600
            PVI: Cvib_1382
            PLT: Plut_1591
            DET: DET1188(ribBA)
            DEH: cbdb_A1103(ribA)
            DEB: DehaBAV1_0999
            DRA: DR_0155
            DGE: Dgeo_0302
            TTH: TTC0697(ribA)
            TTJ: TTHA1062
            AAE: aq_350(ribA)
            TMA: TM1826
            TPT: Tpet_1111
            TME: Tmel_0043
            FNO: Fnod_1417
            MTP: Mthe_1632
            AFU: AF0484(ribA-1)
            HMA: rrnAC3073(ribA)
            TAC: Ta1014m
            TVO: TVN0575
            PTO: PTO0570
            PFU: PF0064
            TKO: TK0428(ribA)
            SAI: Saci_0822
STRUCTURES  PDB: 2BZ0  2BZ1  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.25
            ExPASy - ENZYME nomenclature database: 3.5.4.25
            ExplorEnz - The Enzyme Database: 3.5.4.25
            ERGO genome analysis and discovery system: 3.5.4.25
            BRENDA, the Enzyme Database: 3.5.4.25
            CAS: 56214-35-8
///
ENTRY       EC 3.5.4.26                 Enzyme
NAME        diaminohydroxyphosphoribosylaminopyrimidine deaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine
            2-aminohydrolase
REACTION    2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + H2O =
            5-amino-6-(5-phosphoribosylamino)uracil + NH3 [RN:R03459]
ALL_REAC    R03459
SUBSTRATE   2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine;
            H2O [CPD:C00001]
PRODUCT     5-amino-6-(5-phosphoribosylamino)uracil [CPD:C01268];
            NH3 [CPD:C00014]
COMMENT     The substrate is the product of EC 3.5.4.25 GTP cyclohydrolase II.
REFERENCE   1  [PMID:30756]
  AUTHORS   Burrows RB, Brown GM.
  TITLE     Presence of Escherichia coli of a deaminase and a reductase involved
            in biosynthesis of riboflavin.
  JOURNAL   J. Bacteriol. 136 (1978) 657-67.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00740  Riboflavin metabolism
ORTHOLOGY   KO: K01498  diaminohydroxyphosphoribosylaminopyrimidine deaminase
GENES       ATH: AT3G47390 AT4G20960
            OSA: 4329349 4331409 4335087
            CME: CMS352C
            ECO: b0414(ribD)
            ECJ: JW0404(ribD)
            ECE: Z0515(ribD)
            ECS: ECs0467
            ECC: c0524(ribD)
            ECI: UTI89_C0436(ribD)
            ECP: ECP_0473
            ECV: APECO1_1596(ribD)
            ECW: EcE24377A_0445(ribD)
            ECX: EcHS_A0485(ribD)
            STY: STY0455(ribD)
            STT: t2447(ribD)
            SPT: SPA2307(ribD)
            SEC: SC0457(ribD)
            STM: STM0416(ribD)
            YPE: YPO3183(ribD)
            YPK: y1000(ribD)
            YPM: YP_0748(ribD)
            YPA: YPA_2677
            YPN: YPN_0905
            YPP: YPDSF_2818
            YPS: YPTB0934(ribD)
            YPI: YpsIP31758_3117(ribD)
            SFL: SF0351(ribD)
            SFX: S0359(ribD)
            SFV: SFV_0379(ribD)
            SSN: SSON_0391(ribD)
            SBO: SBO_0308(ribD)
            SDY: SDY_0320(ribD)
            ECA: ECA1126(ribD)
            PLU: plu3899(ribD)
            BUC: BU461(ribD1)
            BAS: BUsg445(ribD1)
            BAB: bbp408(ribD)
            WBR: WGLp462(ribD)
            SGL: SG0651
            ENT: Ent638_0882
            SPE: Spro_1072
            BFL: Bfl234(ribD)
            BPN: BPEN_240(ribD)
            HIN: HI0944(ribD)
            HIT: NTHI1115(ribD)
            HDU: HD1161(ribD)
            HSO: HS_1050(ribD)
            PMU: PM0749(ribD)
            MSU: MS1374(ribD)
            APL: APL_0382(ribD)
            ASU: Asuc_1368
            XFA: XF0950
            XFT: PD1747(ribD)
            XCC: XCC0693(ribD)
            XCB: XC_3541
            XCV: XCV0798(ribD)
            XAC: XAC0746(ribD)
            XOO: XOO3856(ribD)
            XOM: XOO_3635(XOO3635)
            VCH: VC2271
            VCO: VC0395_A1861(ribD)
            VVU: VV1_0323
            VVY: VV0861
            VPA: VP0679
            VFI: VF0700
            PPR: PBPRA0797
            PAE: PA4056(ribD)
            PAP: PSPA7_1045(ribD)
            PPU: PP_0514(ribD)
            PPF: Pput_0549
            PST: PSPTO_0690(ribD)
            PSB: Psyr_4462
            PSP: PSPPH_4507(ribD)
            PFL: PFL_5522(ribD)
            PFO: Pfl_5019(ribD)
            PEN: PSEEN0588(ribD)
            PMY: Pmen_3857
            PAR: Psyc_2141(ribD)
            PCR: Pcryo_2470
            PRW: PsycPRwf_2385
            ACI: ACIAD0247(ribD)
            SON: SO_3469(ribD)
            SDN: Sden_1144 Sden_1469
            SFR: Sfri_1035
            SAZ: Sama_1016
            SBL: Sbal_3160
            SBM: Shew185_3159
            SLO: Shew_1187
            SPC: Sputcn32_2778
            SSE: Ssed_1273
            SPL: Spea_1162
            SHE: Shewmr4_1096
            SHM: Shewmr7_1162
            SHN: Shewana3_1096
            SHW: Sputw3181_1234
            ILO: IL1870(ribD)
            CPS: CPS_0730(ribD)
            PHA: PSHAa2374(ribD)
            PAT: Patl_1311
            SDE: Sde_3458
            PIN: Ping_1440
            MAQ: Maqu_0843
            CBU: CBU_0643(ribD)
            CBD: COXBU7E912_0655(ribD)
            LPN: lpg1177(ribD)
            LPF: lpl1186(ribD)
            LPP: lpp1180(ribD)
            MCA: MCA1658(ribD)
            FTU: FTT1671(ribD)
            FTF: FTF1671(ribD)
            FTW: FTW_1946(ribD)
            FTL: FTL_0078
            FTH: FTH_0074(ribD)
            FTA: FTA_0086(ribD)
            FTN: FTN_0114(ribD)
            TCX: Tcr_1400
            NOC: Noc_2025
            AEH: Mlg_0375
            HHA: Hhal_0900
            HCH: HCH_05957(ribD)
            CSA: Csal_2585
            ABO: ABO_2174(ribD)
            AHA: AHA_3333(ribD)
            BCI: BCI_0601(ribD)
            RMA: Rmag_0800
            VOK: COSY_0726(ribD)
            NME: NMB1817
            NMA: NMA0644(ribD)
            NMC: NMC0403(ribD)
            NGO: NGO0089
            CVI: CV_1290(ribD)
            RSO: RSc0715(ribD)
            REU: Reut_A0776
            RME: Rmet_2688
            BMA: BMA2143(ribD)
            BMV: BMASAVP1_A0767(ribD)
            BML: BMA10299_A2600(ribD)
            BMN: BMA10247_2013(ribD)
            BXE: Bxe_A0895
            BVI: Bcep1808_0877
            BUR: Bcep18194_A4064 Bcep18194_A5283
            BCN: Bcen_0481
            BCH: Bcen2424_0960
            BAM: Bamb_0821
            BPS: BPSL2624(ribD) BPSS1125
            BPM: BURPS1710b_3100(ribD) BURPS1710b_A0085(ribD)
            BPL: BURPS1106A_3065(ribD) BURPS1106A_A1505(ribD)
            BPD: BURPS668_3012(ribD) BURPS668_A1588(ribD)
            BTE: BTH_I1542(ribD-1) BTH_II1281(ribD-2)
            PNU: Pnuc_0270
            BPE: BP2948
            BPA: BPP3871
            BBR: BB4344
            RFR: Rfer_2666
            POL: Bpro_2883
            PNA: Pnap_2915
            AAV: Aave_3555
            AJS: Ajs_3190
            VEI: Veis_2821
            MPT: Mpe_A2945
            HAR: HEAR1381(tadA) HEAR2372(ribD)
            NEU: NE0793(ribD)
            NET: Neut_1091
            NMU: Nmul_A0006
            EBA: ebA1045(ribD)
            AZO: azo2803(ribD)
            DAR: Daro_0605
            TBD: Tbd_2168
            MFA: Mfla_1915
            HPY: HP1505(ribG)
            HPJ: jhp1398(ribD)
            HPA: HPAG1_1407
            HHE: HH0838(ribD)
            HAC: Hac_0079(ribD)
            WSU: WS2019(ribD)
            TDN: Tmden_0679
            CJE: Cj1622(ribD)
            CJR: CJE1794
            CJJ: CJJ81176_1613(ribD)
            CJU: C8J_1524(ribD)
            CFF: CFF8240_1488(ribD)
            CCV: CCV52592_0359(ribD)
            CHA: CHAB381_0131(ribD)
            CCO: CCC13826_1500(ribD)
            ABU: Abu_2046(ribD)
            NIS: NIS_0424
            SUN: SUN_1968
            GSU: GSU1688(ribD)
            GME: Gmet_1624(ribD)
            PCA: Pcar_1445(ribD)
            PPD: Ppro_1596
            DVU: DVU1201(ribD)
            DDE: Dde_2434
            LIP: LI0157(ribD)
            BBA: Bd3542(ribD)
            DPS: DP2785(ribD)
            ADE: Adeh_2742
            AFW: Anae109_2731
            MXA: MXAN_4764(ribD)
            SAT: SYN_00578
            SFU: Sfum_1378
            WOL: WD0710(ribD)
            WBM: Wbm0026
            AMA: AM015(ribD)
            APH: APH_0037(ribD)
            ERU: Erum1140(ribD)
            ERW: ERWE_CDS_01110(ribD)
            ERG: ERGA_CDS_01070(ribD)
            ECN: Ecaj_0112
            ECH: ECH_0169(ribD)
            NSE: NSE_0499(ribD)
            MLO: mlr8405
            MES: Meso_1136
            PLA: Plav_2910
            SME: SMc01772(ribD)
            ATU: Atu1167(ribD*) Atu1168(ribD*)
            ATC: AGR_C_2159
            RET: RHE_CH01510(ribD)
            BME: BMEI1189
            BMF: BAB1_0789(ribD)
            BMS: BR0767(ribD)
            BMB: BruAb1_0783(ribD)
            BOV: BOV_0760(ribD)
            BJA: bll5031(ribD)
            BRA: BRADO4340 BRADO4428(ribD)
            BBT: BBta_4647(ribD)
            RPA: RPA2726(ribD)
            RPB: RPB_2636
            RPC: RPC_2661
            RPD: RPD_2673
            RPE: RPE_2810
            NWI: Nwi_1725
            NHA: Nham_1816
            BHE: BH07560(ribD)
            BQU: BQ05410(ribD)
            BBK: BARBAKC583_0631(ribD)
            CCR: CC_0885(ribD)
            SIL: SPO1754(ribD)
            SIT: TM1040_2135
            RSP: RSP_0393
            RSQ: Rsph17025_0844
            JAN: Jann_3421
            RDE: RD1_1799(ribD)
            PDE: Pden_1335
            MMR: Mmar10_2499
            ZMO: ZMO0476(ribD)
            NAR: Saro_2857
            SAL: Sala_2991
            ELI: ELI_00150
            GOX: GOX0978(ribD)
            RRU: Rru_A1825
            MAG: amb2341
            MGM: Mmc1_0168
            ABA: Acid345_3337
            SUS: Acid_4222
            BSU: BG10518(ribG)
            BHA: BH1554(ribG)
            BAN: BA4331(ribD)
            BAR: GBAA4331(ribD)
            BAA: BA_4789
            BAT: BAS4018(ribD)
            BCE: BC3387 BC4109
            BCA: BCE_4179(ribD)
            BCZ: BCZK3096(ribD) BCZK3865(ribD) pE33L466_0152(ribD)
            BCY: Bcer98_2808
            BTK: BT9727_3851(ribD)
            BLI: BL01891(ribD)
            BLD: BLi02475(ribD)
            BCL: ABC3987(ribG)
            BAY: RBAM_021420(ribD)
            BPU: BPUM_0703(ribD2) BPUM_3532(ribD1)
            OIH: OB0423
            GKA: GK2297
            SAU: SA1589(ribD)
            SAV: SAV1771(ribD)
            SAM: MW1711(ribD)
            SAR: SAR1853(ribD)
            SAS: SAS1694
            SAC: SACOL1820(ribD)
            SAB: SAB1628c(ribD)
            SAA: SAUSA300_1715(ribD)
            SAO: SAOUHSC_01889
            SEP: SE1441
            SER: SERP1328(ribD)
            SHA: SH1153(ribD)
            SSP: SSP0995
            LLA: L0163(ribG)
            SPN: SP_0178
            SPR: spr0164(ribD)
            SPD: SPD_0169(ribD)
            SAG: SAG0746(ribD)
            SAN: gbs0767
            SAK: SAK_0872(ribD)
            LBR: LVIS_1653
            CAC: CAC0590(ribD)
            CPE: CPE0566(ribB)
            CPF: CPF_0546(ribD)
            CPR: CPR_0530(ribD)
            CTC: CTC00671
            CTH: Cthe_0104
            CDF: CD1700(ribD)
            CBO: CBO2866(ribD)
            CBA: CLB_2832(ribD)
            CBH: CLC_2765(ribD)
            CBF: CLI_2922(ribD)
            CHY: CHY_1475(ribD)
            DSY: DSY1662(ribD)
            DRM: Dred_2093
            SWO: Swol_1222
            MTA: Moth_0915
            MTU: Rv1409(ribG)
            MTC: MT1453(ribD)
            MBO: Mb1444(ribG) Mb2690(ribD)
            MBB: BCG_1470(ribG) BCG_2684(ribD)
            MLE: ML0555(ribG)
            MPA: MAP1136(ribG)
            MAV: MAV_3368(ribD)
            MSM: MSMEG_3067(ribD)
            MVA: Mvan_2690
            MGI: Mflv_3727
            MMC: Mmcs_2386
            MKM: Mkms_2433
            MJL: Mjls_2427
            CGL: NCgl1535(cgl1597)
            CGB: cg1800(ribG)
            CEF: CE1716(ribD)
            CDI: DIP1319(ribD)
            CJK: jk1010(ribD)
            RHA: RHA1_ro07168(ribD)
            SCO: SCO2688(ribD)
            TWH: TWT687(ribG)
            TWS: TW706(ribD)
            LXX: Lxx04370(ribD)
            PAC: PPA1752
            NCA: Noca_2447
            ACE: Acel_1274
            KRA: Krad_0126
            SEN: SACE_2121(ribG) SACE_2887(ribD)
            STP: Strop_1874
            RXY: Rxyl_1364
            FNU: FN1506
            RBA: RB6126(ribD)
            CTR: CT730(ribD)
            CTA: CTA_0792(ribD)
            CMU: TC0103
            CPN: CPn0871(ribD)
            CPA: CP0998
            CPJ: CPj0871(ribD)
            CPT: CpB0900
            CCA: CCA00896(ribD)
            CAB: CAB864(ribD)
            CFE: CF0118(ribD)
            PCU: pc1042(ribD)
            LIL: LA1144(ribD1)
            LIC: LIC12536(ribD)
            LBJ: LBJ_2152(ribD)
            LBL: LBL_2146(ribD)
            SYN: slr0066(ribD)
            SYW: SYNW1590(ribD)
            SYC: syc1308_d(ribD)
            SYF: Synpcc7942_0203
            SYD: Syncc9605_0922
            SYE: Syncc9902_1486
            SYG: sync_0821(ribD)
            SYR: SynRCC307_1751(ribD)
            SYX: SynWH7803_1692(ribD)
            CYA: CYA_0386(ribD)
            CYB: CYB_1847(ribD)
            TEL: tlr2152(ribD)
            GVI: gll1250(ribD)
            ANA: all0082(ribD)
            AVA: Ava_1457
            PMA: Pro1339(ribD)
            PMM: PMM1265(ribD)
            PMT: PMT0375(ribD)
            PMN: PMN2A_0831
            PMI: PMT9312_1359
            PMB: A9601_14641
            PMC: P9515_14261
            PMF: P9303_19231
            PMG: P9301_14501
            PMH: P9215_14901(ribD)
            PME: NATL1_16841
            TER: Tery_1661
            BTH: BT_3728(ribD)
            BFR: BF0507(ribD)
            BFS: BF0452
            PGI: PG0155(ribD)
            SRU: SRU_2302(ribD)
            CHU: CHU_0203(ribD)
            GFO: GFO_0635(ribD)
            FPS: FP2025(ribD)
            CTE: CT0747(ribD)
            CCH: Cag_0623
            CPH: Cpha266_0944
            PVI: Cvib_1105
            PLT: Plut_0727
            DET: DET1190(ribD)
            DEH: cbdb_A1105(ribD)
            DEB: DehaBAV1_1001
            DRA: DR_0153
            DGE: Dgeo_0300
            TTH: TTC0699(ribD)
            TTJ: TTHA1064
            AAE: aq_138(ribD1)
            TMA: TM1828
            PFU: PF0062
            TKO: TK0424(ribD)
STRUCTURES  PDB: 2B3Z  2D5N  2G6V  2HXV  2O7P  2OBC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.26
            ExPASy - ENZYME nomenclature database: 3.5.4.26
            ExplorEnz - The Enzyme Database: 3.5.4.26
            ERGO genome analysis and discovery system: 3.5.4.26
            BRENDA, the Enzyme Database: 3.5.4.26
            CAS: 68994-19-4
///
ENTRY       EC 3.5.4.27                 Enzyme
NAME        methenyltetrahydromethanopterin cyclohydrolase;
            5,10-methenyltetrahydromethanopterin cyclohydrolase;
            N5,N10-methenyltetrahydromethanopterin cyclohydrolase;
            methenyl-H4MPT cyclohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     5,10-methenyltetrahydromethanopterin 10-hydrolase (decyclizing)
REACTION    5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O =
            5-formyl-5,6,7,8-tetrahydromethanopterin [RN:R03464]
ALL_REAC    R03464
SUBSTRATE   5,10-methenyl-5,6,7,8-tetrahydromethanopterin [CPD:C04330];
            H2O [CPD:C00001]
PRODUCT     5-formyl-5,6,7,8-tetrahydromethanopterin [CPD:C01274]
COMMENT     Methanopterin is a pterin analogue. The enzyme is involved in the
            formation of methane from CO2 in Methanobacterium
            thermoautotrophicum.
REFERENCE   1  [PMID:4062290]
  AUTHORS   Donnelly MI, Escalante-Semerena JC, Rinehart KL Jr, Wolfe RS.
  TITLE     Methenyl-tetrahydromethanopterin cyclohydrolase in cell extracts of
            Methanobacterium.
  JOURNAL   Arch. Biochem. Biophys. 242 (1985) 430-9.
  ORGANISM  Methanobacterium thermoautotrophicum [GN:mth]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K01499  methenyltetrahydromethanopterin cyclohydrolase
GENES       MCA: MCA2863
            BXE: Bxe_B2433(mch)
            MPT: Mpe_A2609
            MFA: Mfla_1658
            XAU: Xaut_1788
            GBE: GbCGDNIH1_0773
            RBA: RB6759(mch)
            MMP: MMP1191(mch)
            MMQ: MmarC5_0399
            MMZ: MmarC7_0438
            MAE: Maeo_0441
            MVN: Mevan_0507
            MAC: MA1710(mch)
            MBA: Mbar_A2233
            MMA: MM_2653
            MBU: Mbur_0653
            MTP: Mthe_0252
            MHU: Mhun_0444 Mhun_2384
            MEM: Memar_0263 Memar_0668
            MBN: Mboo_0680
            MTH: MTH773(mch)
            MST: Msp_1238(mch)
            MSI: Msm_1723
            MKA: MK0625(mch)
            HAL: VNG1686G(mch)
            HMA: rrnAC1616(mch)
            HWA: HQ2798A(mch)
            NPH: NP2634A(mch)
            RCI: LRC191(mch-1) RCIX2742(mch-2)
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.27
            ExPASy - ENZYME nomenclature database: 3.5.4.27
            ExplorEnz - The Enzyme Database: 3.5.4.27
            ERGO genome analysis and discovery system: 3.5.4.27
            UM-BBD (Biocatalysis/Biodegradation Database): 3.5.4.27
            BRENDA, the Enzyme Database: 3.5.4.27
            CAS: 99533-50-3
///
ENTRY       EC 3.5.4.28                 Enzyme
NAME        S-adenosylhomocysteine deaminase;
            adenosylhomocysteine deaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     S-adenosyl-L-homocysteine aminohydrolase
REACTION    S-adenosyl-L-homocysteine + H2O = S-inosyl-L-homocysteine + NH3
            [RN:R00193]
ALL_REAC    R00193
SUBSTRATE   S-adenosyl-L-homocysteine [CPD:C00021];
            H2O [CPD:C00001]
PRODUCT     S-inosyl-L-homocysteine [CPD:C03431];
            NH3 [CPD:C00014]
REFERENCE   1  [PMID:2592350]
  AUTHORS   Zulty JJ, Speedie MK.
  TITLE     Purification and characterization of S-adenosylhomocysteine
            deaminase from streptonigrin-producing Streptomyces flocculus.
  JOURNAL   J. Bacteriol. 171 (1989) 6840-4.
  ORGANISM  Streptomyces flocculus
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.28
            ExPASy - ENZYME nomenclature database: 3.5.4.28
            ExplorEnz - The Enzyme Database: 3.5.4.28
            ERGO genome analysis and discovery system: 3.5.4.28
            BRENDA, the Enzyme Database: 3.5.4.28
            CAS: 125149-24-8
///
ENTRY       EC 3.5.4.29                 Enzyme
NAME        GTP cyclohydrolase IIa
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     GTP 8,9-hydrolase (phosphate-forming)
REACTION    GTP + 3 H2O =
            2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one +
            2 phosphate [RN:R07306]
ALL_REAC    R07306
SUBSTRATE   GTP [CPD:C00044];
            H2O [CPD:C00001]
PRODUCT     2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one
            [CPD:C15563];
            phosphate [CPD:C00009]
COMMENT     Requires Mg2+. This enzyme catalyses the hydrolysis of the imidazole
            ring of guanosine 5'-triphosphate, N7-methylguanosine
            5'-triphosphate or inosine 5'-triphosphate. Xanthosine
            5'-triphosphate and ATP are not substrates. It also catalyses the
            hydrolysis of diphosphate to form two equivalents of phosphate.
            Unlike GTP cyclohydrolase II (EC 3.5.4.25), this enzyme does not
            release formate, but does hydrolyse the diphosphate from GTP to
            phosphate.
REFERENCE   1  [PMID:12475257]
  AUTHORS   Graham DE, Xu H, White RH.
  TITLE     A member of a new class of GTP cyclohydrolases produces
            formylaminopyrimidine nucleotide monophosphates.
  JOURNAL   Biochemistry. 41 (2002) 15074-84.
  ORGANISM  Methanococcus jannaschii [GN:mja]
ORTHOLOGY   KO: K08096  GTP cyclohydrolase IIa
GENES       MJA: MJ0145
            MMP: MMP0405(gch3)
            MMQ: MmarC5_1233
            MMZ: MmarC7_1403
            MAE: Maeo_0818
            MVN: Mevan_1393
            MTH: MTH1017
            MST: Msp_1404(gch3)
            HAL: VNG1021C
            APE: APE_1365.1
            SMR: Smar_0486
            SSO: SSO0399
            STO: ST0395
            SAI: Saci_0819
            MSE: Msed_0049
            PAI: PAE2984
            PIS: Pisl_0384
            PCL: Pcal_1123
            PAS: Pars_1351
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.29
            ExPASy - ENZYME nomenclature database: 3.5.4.29
            ExplorEnz - The Enzyme Database: 3.5.4.29
            ERGO genome analysis and discovery system: 3.5.4.29
            BRENDA, the Enzyme Database: 3.5.4.29
///
ENTRY       EC 3.5.4.30                 Enzyme
NAME        dCTP deaminase (dUMP-forming)
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
SYSNAME     dCTP aminohydrolase (dUMP-forming)
REACTION    dCTP + 2 H2O = dUMP + diphosphate + NH3 [RN:R07307]
ALL_REAC    R07307
SUBSTRATE   dCTP [CPD:C00458];
            H2O [CPD:C00001]
PRODUCT     dUMP [CPD:C00365];
            diphosphate [CPD:C00013];
            NH3 [CPD:C00014]
COMMENT     Requires Mg2+. Is highly specific for dCTP as substrate as dCMP,
            CTP, CDP, CMP, cytosine or deoxycytosine are not deaminated. While
            most bacteria require two enzymes to form dUMP from dCTP (EC
            3.5.4.13, dCTP deaminase and EC 3.6.1.23, dUTP diphosphatase), the
            archaeon Methanocaldococcus jannaschii uses a single enzyme to carry
            out both functions. This enzyme can also act as a dUTP
            diphosphatase, but more slowly.
REFERENCE   1  [PMID:12538648]
  AUTHORS   Li H, Xu H, Graham DE, White RH.
  TITLE     The Methanococcus jannaschii dCTP deaminase is a bifunctional
            deaminase and diphosphatase.
  JOURNAL   J. Biol. Chem. 278 (2003) 11100-6.
  ORGANISM  Methanococcus jannaschii [GN:mja]
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K09887  dCTP deaminase (dUMP-forming)
GENES       MJA: MJ0430(dcd)
            MMP: MMP1426(dcd)
            MMQ: MmarC5_0152
            MMZ: MmarC7_0671
            MAE: Maeo_1411
            MVN: Mevan_0737
STRUCTURES  PDB: 2HXB  2HXD  2HXE  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.4.30
            ExPASy - ENZYME nomenclature database: 3.5.4.30
            ExplorEnz - The Enzyme Database: 3.5.4.30
            ERGO genome analysis and discovery system: 3.5.4.30
            BRENDA, the Enzyme Database: 3.5.4.30
///
ENTRY       EC 3.5.4.-                  Enzyme
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In cyclic amidines
REACTION    (1) Cyromazine + H2O <=> N-Cyclopropylammeline + NH3 [RN:R06970];
            (2) N-Cyclopropylammeline + H2O <=> N-Cyclopropylammelide + NH3
            [RN:R06971];
            (3) N-Cyclopropylammelide + H2O <=> Cyanuric acid + Cyclopropylamine
            [RN:R06972]
SUBSTRATE   Cyromazine [CPD:C14147];
            H2O [CPD:C00001];
            N-Cyclopropylammeline [CPD:C14148];
            N-Cyclopropylammelide [CPD:C14149]
PRODUCT     N-Cyclopropylammeline [CPD:C14148];
            NH3 [CPD:C00014];
            N-Cyclopropylammelide [CPD:C14149];
            Cyanuric acid [CPD:C06554];
            Cyclopropylamine [CPD:C14150]
///
ENTRY       EC 3.5.5.1                  Enzyme
NAME        nitrilase;
            acetonitrilase;
            benzonitrilase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In nitriles
SYSNAME     nitrile aminohydrolase
REACTION    a nitrile + 2 H2O = a carboxylate + NH3 [RN:R00540]
ALL_REAC    R00540 > R01887 R03093 R03542 R05591 R07855
SUBSTRATE   nitrile [CPD:C00726];
            H2O [CPD:C00001]
PRODUCT     carboxylate [CPD:C00060];
            NH3 [CPD:C00014]
COMMENT     Acts on a wide range of aromatic nitriles including
            (indol-3-yl)acetonitrile, and also on some aliphatic nitriles, and
            on the corresponding acid amides. cf. EC 4.2.1.84 nitrile hydratase.
REFERENCE   1  [PMID:21655]
  AUTHORS   Harper DB.
  TITLE     Microbial metabolism of aromatic nitriles. Enzymology of C-N
            cleavage by Nocardia sp. (Rhodochrous group) N.C.I.B. 11216.
  JOURNAL   Biochem. J. 165 (1977) 309-19.
  ORGANISM  Nocardia sp.
REFERENCE   2
  AUTHORS   Thimann, K.V. and Mahadevan, S.
  TITLE     Nitrilase. I. Occurrence, preparation, and general properties of the
            enzyme.
  JOURNAL   Arch. Biochem. Biophys. 105 (1964) 133-141.
  ORGANISM  Hordeum vulgare [GN:ehvu]
REFERENCE   3  [PMID:11380987]
  AUTHORS   Pace HC, Brenner C.
  TITLE     The nitrilase superfamily: classification, structure and function.
  JOURNAL   Genome. Biol. 2 (2001) REVIEWS0001.
  ORGANISM  Caenorhabditis elegans [GN:cel], Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00380  Tryptophan metabolism
            PATH: map00460  Cyanoamino acid metabolism
            PATH: map00632  Benzoate degradation via CoA ligation
            PATH: map00643  Styrene degradation
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K01501  nitrilase
GENES       DME: Dmel_CG7067(NitFhit)
            CEL: ZK1058.6(Nitrilase)
            ATH: AT3G44300(NIT2) AT3G44320(NIT3) AT5G22300(NIT4)
            OSA: 4330076 4330077
            PIC: PICST_36697(NIT1)
            CGR: CAGL0G01210g
            ANI: AN7367.2
            AFM: AFUA_6G13450
            AOR: AO090003000470
            TBR: Tb09.160.0770
            TCR: 509979.150 510039.40
            LMA: LmjF26.2280
            ECI: UTI89_C0629(ybeM)
            PAP: PSPA7_3027
            PFL: PFL_2909
            PFO: Pfl_2571
            PEN: PSEEN1080 PSEEN3513
            PAR: Psyc_0202
            PCR: Pcryo_0222
            SSE: Ssed_0525
            SPL: Spea_2863
            PHA: PSHAa2676
            PAT: Patl_0189 Patl_2399
            NOC: Noc_2655
            AEH: Mlg_0411
            CVI: CV_2097
            RSO: RSc2658(RS04553)
            REH: H16_A1125(nit)
            RME: Rmet_0992
            BMA: BMA2336
            BXE: Bxe_A3971
            BUR: Bcep18194_A3790 Bcep18194_A3828
            BCN: Bcen_0220
            BCH: Bcen2424_0704 Bcen2424_0740
            BAM: Bamb_0595 Bamb_0633
            BPS: BPSL2837
            BPM: BURPS1710b_3333(opaA)
            BTE: BTH_I1297
            BBR: BB1116
            RFR: Rfer_0849
            POL: Bpro_3376
            PNA: Pnap_4743
            MPT: Mpe_A0244
            HAR: HEAR0861
            MMS: mma_0836 mma_2480
            NEU: NE1327
            NET: Neut_1264
            MFA: Mfla_1745
            SFU: Sfum_2312
            BJA: blr3397(nit)
            RPA: RPA4166
            JAN: Jann_3735
            MMR: Mmar10_1113
            ZMO: ZMO1207
            SWI: Swit_0987 Swit_4178
            MGM: Mmc1_1403
            CDF: CD2842
            CKL: CKL_2025
            MSM: MSMEG_5373
            RHA: RHA1_ro03332 RHA1_ro03335 RHA1_ro03530
            AAU: AAur_0337
            FAL: FRAAL1968
            RXY: Rxyl_0235
            SYF: Synpcc7942_0839
            SYR: SynRCC307_1156
            SYX: SynWH7803_1035
            PMB: A9601_06711
            PMC: P9515_06801
            PMF: P9303_18921
            PMG: P9301_06411 P9301_13131
            PME: NATL1_06731
            MMA: MM_1229
            HMA: pNG7354(nitB)
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.5.1
            ExPASy - ENZYME nomenclature database: 3.5.5.1
            ExplorEnz - The Enzyme Database: 3.5.5.1
            ERGO genome analysis and discovery system: 3.5.5.1
            UM-BBD (Biocatalysis/Biodegradation Database): 3.5.5.1
            BRENDA, the Enzyme Database: 3.5.5.1
            CAS: 9024-90-2
///
ENTRY       EC 3.5.5.2                  Enzyme
NAME        ricinine nitrilase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In nitriles
SYSNAME     ricinine aminohydrolase
REACTION    ricinine + 2 H2O = 3-carboxy-4-methoxy-N-methyl-2-pyridone + NH3
            [RN:R03593]
ALL_REAC    R03593;
            (other) R00540
SUBSTRATE   ricinine [CPD:C01526];
            H2O [CPD:C00001]
PRODUCT     3-carboxy-4-methoxy-N-methyl-2-pyridone [CPD:C04447];
            NH3 [CPD:C00014]
REFERENCE   1  [PMID:14247679]
  AUTHORS   ROBINSON WG, HOOK RH.
  TITLE     RICININE NITRILASE. I. REACTION PRODUCT AND SUBSTRATE SPECIFICITY.
  JOURNAL   J. Biol. Chem. 239 (1964) 4257-62.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:14247680]
  AUTHORS   HOOK RH, ROBINSON WG.
  TITLE     RICININE NITRILASE. II. PURIFICATION AND PROPERTIES.
  JOURNAL   J. Biol. Chem. 239 (1964) 4263-7.
REFERENCE   3  [PMID:11380987]
  AUTHORS   Pace HC, Brenner C.
  TITLE     The nitrilase superfamily: classification, structure and function.
  JOURNAL   Genome. Biol. 2 (2001) REVIEWS0001.
PATHWAY     PATH: map00910  Nitrogen metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.5.2
            ExPASy - ENZYME nomenclature database: 3.5.5.2
            ExplorEnz - The Enzyme Database: 3.5.5.2
            ERGO genome analysis and discovery system: 3.5.5.2
            BRENDA, the Enzyme Database: 3.5.5.2
            CAS: 9075-40-5
///
ENTRY       EC 3.5.5.3        Obsolete  Enzyme
NAME        Transferred to 4.2.1.104
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In nitriles
COMMENT     Transferred entry: now EC 4.2.1.104, cyanate hydratase (EC 3.5.5.3
            created 1972, deleted 1990)
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.5.3
            ExPASy - ENZYME nomenclature database: 3.5.5.3
            ExplorEnz - The Enzyme Database: 3.5.5.3
            ERGO genome analysis and discovery system: 3.5.5.3
            BRENDA, the Enzyme Database: 3.5.5.3
///
ENTRY       EC 3.5.5.4                  Enzyme
NAME        cyanoalanine nitrilase;
            beta-cyanoalanine nitrilase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In nitriles
SYSNAME     3-cyano-L-alanine aminohydrolase
REACTION    3-cyano-L-alanine + 2 H2O = L-aspartate + NH3 [RN:R00486]
ALL_REAC    R00486
SUBSTRATE   3-cyano-L-alanine [CPD:C02512];
            H2O [CPD:C00001]
PRODUCT     L-aspartate [CPD:C00049];
            NH3 [CPD:C00014]
COMMENT     L-Asparagine is formed as an intermediate.
REFERENCE   1
  AUTHORS   Yanase, H., Sakai, T. and Tonomuro, K.
  TITLE     Purification, crystallization and some properties of
            beta-cyano-L-alanine-degrading enzyme in Pseudomonas sp. 13.
  JOURNAL   Agric. Biol. Chem. 47 (1983) 473-482.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00460  Cyanoamino acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.5.4
            ExPASy - ENZYME nomenclature database: 3.5.5.4
            ExplorEnz - The Enzyme Database: 3.5.5.4
            ERGO genome analysis and discovery system: 3.5.5.4
            BRENDA, the Enzyme Database: 3.5.5.4
            CAS: 85638-44-4
///
ENTRY       EC 3.5.5.5                  Enzyme
NAME        arylacetonitrilase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In nitriles
SYSNAME     arylacetonitrile aminohydrolase
REACTION    4-chlorophenylacetonitrile + 2 H2O = 4-chlorophenylacetate + NH3
            [RN:R04140]
ALL_REAC    R04140;
            (other) R00540
SUBSTRATE   4-chlorophenylacetonitrile [CPD:C03679];
            H2O [CPD:C00001]
PRODUCT     4-chlorophenylacetate [CPD:C03077];
            NH3 [CPD:C00014]
COMMENT     Requires thiol compounds. Also hydrolyses other 4-substituted
            phenylacetonitriles, thien-2-ylacetonitrile, tolylacetonitriles,
            and, more slowly, benzyl cyanide.
REFERENCE   1
  AUTHORS   Mauger, J., Nagasawa, T. and Yamada, H.
  TITLE     Occurrence of a novel nitrilase, arylacetonitrilase, in Alcaligenes
            faecalis JM3.
  JOURNAL   Arch. Microbiol. 155 (1990) 1-6.
  ORGANISM  Alcaligenes faecalis
REFERENCE   2  [PMID:2269298]
  AUTHORS   Nagasawa T, Mauger J, Yamada H.
  TITLE     A novel nitrilase, arylacetonitrilase, of Alcaligenes faecalis JM3.
            Purification and characterization.
  JOURNAL   Eur. J. Biochem. 194 (1990) 765-72.
  ORGANISM  Alcaligenes faecalis
PATHWAY     PATH: map00460  Cyanoamino acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.5.5
            ExPASy - ENZYME nomenclature database: 3.5.5.5
            ExplorEnz - The Enzyme Database: 3.5.5.5
            ERGO genome analysis and discovery system: 3.5.5.5
            BRENDA, the Enzyme Database: 3.5.5.5
            CAS: 132053-06-6
///
ENTRY       EC 3.5.5.6                  Enzyme
NAME        bromoxynil nitrilase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In nitriles
SYSNAME     3,5-dibromo-4-hydroxybenzonitrile aminohydrolase
REACTION    3,5-dibromo-4-hydroxybenzonitrile + 2 H2O =
            3,5-dibromo-4-hydroxy-benzoate + NH3 [RN:R04349]
ALL_REAC    R04349
SUBSTRATE   3,5-dibromo-4-hydroxybenzonitrile [CPD:C04178];
            H2O [CPD:C00001]
PRODUCT     3,5-dibromo-4-hydroxy-benzoate;
            NH3 [CPD:C00014]
COMMENT     Involved in the bacterial degradation of the herbicide bromoxynil.
            Highly specific.
REFERENCE   1  [PMID:2834373]
  AUTHORS   Stalker DM, Malyj LD, McBride KE.
  TITLE     Purification and properties of a nitrilase specific for the
            herbicide bromoxynil and corresponding nucleotide sequence analysis
            of the bxn gene.
  JOURNAL   J. Biol. Chem. 263 (1988) 6310-4.
  ORGANISM  Klebsiella ozaenae
PATHWAY     PATH: map00627  1,4-Dichlorobenzene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.5.6
            ExPASy - ENZYME nomenclature database: 3.5.5.6
            ExplorEnz - The Enzyme Database: 3.5.5.6
            ERGO genome analysis and discovery system: 3.5.5.6
            UM-BBD (Biocatalysis/Biodegradation Database): 3.5.5.6
            BRENDA, the Enzyme Database: 3.5.5.6
            CAS: 157857-12-0
///
ENTRY       EC 3.5.5.7                  Enzyme
NAME        aliphatic nitrilase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In nitriles
SYSNAME     aliphatic nitrile aminohydrolase
REACTION    R-CN + 2 H2O = R-COOH + NH3 [RN:R00540]
ALL_REAC    R00540 > R05358
SUBSTRATE   R-CN [CPD:C00726];
            H2O [CPD:C00001]
PRODUCT     R-COOH [CPD:C00060];
            NH3 [CPD:C00014]
COMMENT     Preferentially hydrolyses aliphatic nitriles, some of which are
            apparently not substrates for other known nitrilases (EC 3.5.5.1).
            Substrates include crotononitrile, acrylonitrile and glutaronitrile.
REFERENCE   1  [PMID:1390687]
  AUTHORS   Kobayashi M, Yanaka N, Nagasawa T, Yamada H.
  TITLE     Primary structure of an aliphatic nitrile-degrading enzyme,
            aliphatic nitrilase, from Rhodococcus rhodochrous K22 and expression
            of its gene and identification of its active site residue.
  JOURNAL   Biochemistry. 31 (1992) 9000-7.
  ORGANISM  Rhodococcus rhodochrous
REFERENCE   2  [PMID:11380987]
  AUTHORS   Pace HC, Brenner C.
  TITLE     The nitrilase superfamily: classification, structure and function.
  JOURNAL   Genome. Biol. 2 (2001) REVIEWS0001.
PATHWAY     PATH: map00643  Styrene degradation
ORTHOLOGY   KO: K01502  aliphatic nitrilase
GENES       PLU: plu1231
            PST: PSPTO_0189
            PSB: Psyr_0007
            BXE: Bxe_A1162 Bxe_A1408
            MPT: Mpe_A0993 Mpe_A3478
            MMS: mma_3076
            RLE: RL0660 pRL80076
            BJA: bll6402
            BRA: BRADO4539(nitA)
            BBT: BBta_4766(nitA)
            RPA: RPA1563
            SIL: SPOA0114
            MSM: MSMEG_4138
            NFA: nfa32690
            SYN: sll0784(merR)
            SYW: SYNW1425
            SYC: syc0701_d(merR)
            SYD: Syncc9605_1108
            PMG: P9301_13131
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.5.7
            ExPASy - ENZYME nomenclature database: 3.5.5.7
            ExplorEnz - The Enzyme Database: 3.5.5.7
            ERGO genome analysis and discovery system: 3.5.5.7
            UM-BBD (Biocatalysis/Biodegradation Database): 3.5.5.7
            BRENDA, the Enzyme Database: 3.5.5.7
            CAS: 9024-90-2
///
ENTRY       EC 3.5.5.8                  Enzyme
NAME        thiocyanate hydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In nitriles
SYSNAME     thiocyanate aminohydrolase
REACTION    thiocyanate + 2 H2O = carbonyl sulfide + NH3 + HO- [RN:R05780]
ALL_REAC    R05780
SUBSTRATE   thiocyanate [CPD:C01755];
            H2O [CPD:C00001]
PRODUCT     carbonyl sulfide [CPD:C07331];
            NH3 [CPD:C00014];
            HO- [CPD:C01328]
COMMENT     The enzyme from Thiobacillus thioparus catalyses the first step in
            the degradation of thiocyanate.
REFERENCE   1  [PMID:9573140]
  AUTHORS   Katayama Y, Matsushita Y, Kaneko M, Kondo M, Mizuno T, Nyunoya H.
  TITLE     Cloning of genes coding for the three subunits of thiocyanate
            hydrolase of Thiobacillus thioparus THI 115 and their evolutionary
            relationships to nitrile hydratase.
  JOURNAL   J. Bacteriol. 180 (1998) 2583-9.
  ORGANISM  Thiobacillus thioparus
REFERENCE   2  [PMID:1577754]
  AUTHORS   Katayama Y, Narahara Y, Inoue Y, Amano F, Kanagawa T, Kuraishi H.
  TITLE     A thiocyanate hydrolase of Thiobacillus thioparus. A novel enzyme
            catalyzing the formation of carbonyl sulfide from thiocyanate.
  JOURNAL   J. Biol. Chem. 267 (1992) 9170-5.
  ORGANISM  Thiobacillus thioparus
GENES       LPP: lpp1219 lpp1220 lpp1221
            MVA: Mvan_1504
            MGI: Mflv_4916
            MMC: Mmcs_5258
            MKM: Mkms_5347
            MJL: Mjls_5637
            NFA: nfa20750 nfa20760 nfa20770
            RHA: RHA1_ro04428
STRUCTURES  PDB: 2DD4  2DD5  2DXB  2DXC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.5.8
            ExPASy - ENZYME nomenclature database: 3.5.5.8
            ExplorEnz - The Enzyme Database: 3.5.5.8
            ERGO genome analysis and discovery system: 3.5.5.8
            UM-BBD (Biocatalysis/Biodegradation Database): 3.5.5.8
            BRENDA, the Enzyme Database: 3.5.5.8
///
ENTRY       EC 3.5.99.1                 Enzyme
NAME        riboflavinase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In other compounds
SYSNAME     riboflavin hydrolase
REACTION    riboflavin + H2O = ribitol + lumichrome [RN:R01732]
ALL_REAC    R01732
SUBSTRATE   riboflavin [CPD:C00255];
            H2O [CPD:C00001]
PRODUCT     ribitol [CPD:C00474];
            lumichrome [CPD:C01727]
REFERENCE   1
  AUTHORS   Yanagita, T. and Foster, J.W.
  TITLE     A bacterial riboflavin hydrolase.
  JOURNAL   J. Biol. Chem. 221 (1956) 593-607.
  ORGANISM  Pseudomonas riboflavina
PATHWAY     PATH: map00740  Riboflavin metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.99.1
            ExPASy - ENZYME nomenclature database: 3.5.99.1
            ExplorEnz - The Enzyme Database: 3.5.99.1
            ERGO genome analysis and discovery system: 3.5.99.1
            BRENDA, the Enzyme Database: 3.5.99.1
            CAS: 9024-79-7
///
ENTRY       EC 3.5.99.2                 Enzyme
NAME        thiaminase;
            thiaminase II
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In other compounds
SYSNAME     thiamine hydrolase
REACTION    thiamine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine +
            5-(2-hydroxyethyl)-4-methylthiazole [RN:R02133]
ALL_REAC    R02133
SUBSTRATE   thiamine [CPD:C00378];
            H2O [CPD:C00001]
PRODUCT     4-amino-5-hydroxymethyl-2-methylpyrimidine [CPD:C01279];
            5-(2-hydroxyethyl)-4-methylthiazole [CPD:C04294]
REFERENCE   1
  AUTHORS   Fujita, A., Nose, Y. and Kuratani, K.
  TITLE     Second type of bacterial thiaminase.
  JOURNAL   J. Vitaminol. (Kyoto) 1 (1954) 1-7.
  ORGANISM  Bacillus aneurinolyticus
REFERENCE   2
  AUTHORS   Ikehata, H.
  TITLE     Purification of thiaminase II.
  JOURNAL   J. Gen. Appl. Microbiol. 6 (1960) 30-39.
  ORGANISM  Bacillus aneurinolyticus
PATHWAY     PATH: map00730  Thiamine metabolism
GENES       BCY: Bcer98_0612 Bcer98_1892
            BPU: BPUM_1094(tenA) BPUM_3574
            CBE: Cbei_2088
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.99.2
            ExPASy - ENZYME nomenclature database: 3.5.99.2
            ExplorEnz - The Enzyme Database: 3.5.99.2
            ERGO genome analysis and discovery system: 3.5.99.2
            BRENDA, the Enzyme Database: 3.5.99.2
            CAS: 9024-80-0
///
ENTRY       EC 3.5.99.3                 Enzyme
NAME        hydroxydechloroatrazine ethylaminohydrolase;
            AtzB;
            hydroxyatrazine ethylaminohydrolase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In other compounds
SYSNAME     4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine
            ethylaminohydrolase
REACTION    4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + H2O =
            N-isopropylammelide + ethylamine [RN:R05559]
ALL_REAC    R05559;
            (other) R06966
SUBSTRATE   4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine
            [CPD:C06552];
            H2O [CPD:C00001]
PRODUCT     N-isopropylammelide [CPD:C06553];
            ethylamine [CPD:C00797]
COMMENT     Involved in a pathway by which the herbicide atrazine,
            2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, is
            degraded in bacteria via N-isopropylammelide,
            2,4-dihydroxy-6-(isopropylamino)-1,3,5-triazine.
REFERENCE   1  [PMID:9055410]
  AUTHORS   Boundy-Mills KL, de Souza ML, Mandelbaum RT, Wackett LP, Sadowsky
            MJ.
  TITLE     The atzB gene of Pseudomonas sp. strain ADP encodes the second
            enzyme of a novel atrazine degradation pathway.
  JOURNAL   Appl. Environ. Microbiol. 63 (1997) 916-23.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00791  Atrazine degradation
ORTHOLOGY   KO: K03382  hydroxyatrazine ethylaminohydrolase
GENES       PPF: Pput_3132
            PFO: Pfl_3434
            PEN: PSEEN0675
            PMY: Pmen_3705
            ACI: ACIAD0761
            REU: Reut_A1294
            RME: Rmet_1186
            BXE: Bxe_A1936
            BUR: Bcep18194_A5267 Bcep18194_B0632
            BCH: Bcen2424_1956
            BAM: Bamb_1943
            BPS: BPSL2112
            BPM: BURPS1710b_2526(atzB)
            BTE: BTH_I2073
            MMS: mma_0509
            RET: RHE_PC00089
            RLE: pRL100336(atzB)
            BJA: bll6159
            BRA: BRADO1738
            BBT: BBta_1262 BBta_2050
            SIT: TM1040_1906
            RDE: RD1_2007(atzB)
            MSM: MSMEG_1297
            RHA: RHA1_ro04508(atzB)
            AAU: AAur_pTC10218(atzB)
            FRA: Francci3_0845
            SEN: SACE_1262(atzB)
            RXY: Rxyl_2838
            TME: Tmel_1728
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.99.3
            ExPASy - ENZYME nomenclature database: 3.5.99.3
            ExplorEnz - The Enzyme Database: 3.5.99.3
            ERGO genome analysis and discovery system: 3.5.99.3
            UM-BBD (Biocatalysis/Biodegradation Database): 3.5.99.3
            BRENDA, the Enzyme Database: 3.5.99.3
///
ENTRY       EC 3.5.99.4                 Enzyme
NAME        N-isopropylammelide isopropylaminohydrolase;
            AtzC
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In other compounds
SYSNAME     N-isopropylammelide isopropylaminohydrolase
REACTION    N-isopropylammelide + H2O = cyanuric acid + isopropylamine
            [RN:R05560]
ALL_REAC    R05560;
            (other) R06967
SUBSTRATE   N-isopropylammelide [CPD:C06553];
            H2O [CPD:C00001]
PRODUCT     cyanuric acid [CPD:C06554];
            isopropylamine [CPD:C06748]
COMMENT     Involved in a pathway by which the herbicide atrazine,
            2-chloro-4-(ethylamino)-6-(isopopylamino)-1,3,5-triazine, is
            degraded in bacteria via N-isopropylammelide,
            2,4-dihydroxy-6-(isopropylamino)-1,3,5-triazine.
REFERENCE   1  [PMID:9422605]
  AUTHORS   Sadowsky MJ, Tong Z, de Souza M, Wackett LP.
  TITLE     AtzC is a new member of the amidohydrolase protein superfamily and
            is homologous to other atrazine-metabolizing enzymes.
  JOURNAL   J. Bacteriol. 180 (1998) 152-8.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00791  Atrazine degradation
ORTHOLOGY   KO: K08710  N-isopropylammelide isopropylaminohydrolase
GENES       YPP: YPDSF_0089
            ENT: Ent638_3792
            SPE: Spro_4594
            ASU: Asuc_1190
            PPF: Pput_2527
            PFO: Pfl_3146 Pfl_3779
            SSE: Ssed_2803
            MMW: Mmwyl1_1583
            BXE: Bxe_A2120
            BVI: Bcep1808_4874
            BUR: Bcep18194_B0067 Bcep18194_B0068 Bcep18194_B0800
            BCN: Bcen_4038 Bcen_5236
            BCH: Bcen2424_4328 Bcen2424_5623
            BAM: Bamb_3745 Bamb_4900
            POL: Bpro_1960
            PNA: Pnap_4007
            AAV: Aave_3221
            VEI: Veis_0416 Veis_4430
            NET: Neut_1722
            SMD: Smed_5333 Smed_5791
            BRA: BRADO0862 BRADO1789
            BBT: BBta_2105 BBta_7204
            RSH: Rsph17029_1985
            RSQ: Rsph17025_0955
            JAN: Jann_1306
            PDE: Pden_1057
            ACR: Acry_0828
            RRU: Rru_A2788
            LRE: Lreu_0258
            RHA: RHA1_ro00597 RHA1_ro00599
            ART: Arth_3600
            AAU: AAur_pTC10212(atzC)
            NCA: Noca_1495
            RXY: Rxyl_0224
STRUCTURES  PDB: 2QT3  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.99.4
            ExPASy - ENZYME nomenclature database: 3.5.99.4
            ExplorEnz - The Enzyme Database: 3.5.99.4
            ERGO genome analysis and discovery system: 3.5.99.4
            UM-BBD (Biocatalysis/Biodegradation Database): 3.5.99.4
            BRENDA, the Enzyme Database: 3.5.99.4
///
ENTRY       EC 3.5.99.5                 Enzyme
NAME        2-aminomuconate deaminase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In other compounds
SYSNAME     2-aminomuconate aminohydrolase
REACTION    2-aminomuconate + H2O = 4-oxalocrotonate + NH3 [RN:R03887]
ALL_REAC    R03887
SUBSTRATE   2-aminomuconate [CPD:C02220];
            H2O [CPD:C00001]
PRODUCT     4-oxalocrotonate [CPD:C03453];
            NH3 [CPD:C00014]
COMMENT     Intermediate in the biodegradation of nitrobenzene by Pseudomonas
            pseudocaligenes JS45. The reaction is spontaneous in acid
            conditions.
REFERENCE   1  [PMID:9573204]
  AUTHORS   He Z, Spain JC.
  TITLE     A novel 2-aminomuconate deaminase in the nitrobenzene degradation
            pathway of Pseudomonas pseudoalcaligenes JS45.
  JOURNAL   J. Bacteriol. 180 (1998) 2502-6.
  ORGANISM  Pseudomonas pseudoalcaligenes
REFERENCE   2  [PMID:9471964]
  AUTHORS   He Z, Spain JC.
  TITLE     Studies of the catabolic pathway of degradation of nitrobenzene by
            Pseudomonas pseudoalcaligenes JS45: removal of the amino group from
            2-aminomuconic semialdehyde.
  JOURNAL   Appl. Environ. Microbiol. 63 (1997) 4839-43.
  ORGANISM  Pseudomonas pseudoalcaligenes
PATHWAY     PATH: map00380  Tryptophan metabolism
GENES       MXA: MXAN_0920
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.99.5
            ExPASy - ENZYME nomenclature database: 3.5.99.5
            ExplorEnz - The Enzyme Database: 3.5.99.5
            ERGO genome analysis and discovery system: 3.5.99.5
            BRENDA, the Enzyme Database: 3.5.99.5
///
ENTRY       EC 3.5.99.6                 Enzyme
NAME        glucosamine-6-phosphate deaminase;
            glucosaminephosphate isomerase;
            glucosamine-6-phosphate isomerase;
            phosphoglucosaminisomerase;
            glucosamine phosphate deaminase;
            aminodeoxyglucosephosphate isomerase;
            phosphoglucosamine isomerase
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In other compounds
SYSNAME     2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol
            isomerizing)
REACTION    D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3
            [RN:R00765]
ALL_REAC    R00765
SUBSTRATE   D-glucosamine 6-phosphate [CPD:C00352];
            H2O [CPD:C00001]
PRODUCT     D-fructose 6-phosphate [CPD:C00085];
            NH3 [CPD:C00014]
EFFECTOR    N-Acetyl-D-glucosamine 6-phosphate [CPD:C00357]
COMMENT     Isomerization of the aldose-ketose type converts the -CH(-NH2)-CH=O
            group of glucosamine 6-phosphate into -C(=NH)-CH2-OH, forming
            2-deoxy-2-imino-D-arabino-hexitol, which then hydrolyses to yield
            fructose 6-phosphate and ammonia. N-Acetyl-D-glucosamine
            6-phosphate, which is not broken down, activates the enzyme.
REFERENCE   1  [PMID:13549465]
  AUTHORS   COMB DG, ROSEMAN S.
  TITLE     Glucosamine metabolism. IV. Glucosamine-6-phosphate deaminase.
  JOURNAL   J. Biol. Chem. 232 (1958) 807-27.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Pattabiraman, T.N., Bachhawat, B.K.
  TITLE     Purification of glucosamine 6-phosphate deaminase from human brain.
  JOURNAL   Biochim. Biophys. Acta 54 (1961) 273-283.
  ORGANISM  human [GN:hsa]
REFERENCE   3
  AUTHORS   Wolfe, J.B., Britton, B.B., Nakada, H.I.
  TITLE     Glucosamine degradation by Escherichia coli. III. Isolation and
            studies of "phosphoglucosaminisomerase".
  JOURNAL   Arch. Biochem Biophys. 66 (1957) 333-339.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K01504  glucosamine-6-phosphate isomerase
            KO: K02564  glucosamine-6-phosphate isomerase
GENES       HSA: 10007(GNPDA1) 132789(GNPDA2)
            MMU: 26384(Gnpda1) 67980(Gnpda2)
            RNO: 289608(Gnpda2_predicted)
            CFA: 478043(GNPDA1)
            GGA: 416341(GNPDA1)
            XLA: 398874(MGC68593) 398943(MGC68566)
            SPU: 585301(LOC585301)
            DME: Dmel_CG6957
            CEL: T03F6.3
            PIC: PICST_62706(NAG1)
            AFM: AFUA_1G00480 AFUA_8G04070
            CNE: CNM01050
            DDI: DDBDRAFT_0206255
            TET: TTHERM_00243730
            TBR: Tb11.01.8520
            TCR: 511025.50 511531.50
            LMA: LmjF32.3260
            EHI: 86.t00021
            ECO: b0678(nagB)
            ECJ: JW0664(nagB)
            ECE: Z0825(nagB)
            ECS: ECs0708
            ECC: c0753(nagB)
            ECI: UTI89_C0672(nagB)
            ECP: ECP_0690
            ECV: APECO1_1394(nagB)
            ECW: EcE24377A_0703(nagB)
            ECX: EcHS_A0722
            STY: STY0722(nagB)
            STT: t2191(nagB)
            SPT: SPA2057(nagB)
            SEC: SC0705(nagB)
            STM: STM0684(nagB)
            YPE: YPO2627(nagB)
            YPK: y1202(nagB)
            YPM: YP_1086(nagB)
            YPA: YPA_2470
            YPN: YPN_1113
            YPS: YPTB1119(nagB)
            YPI: YpsIP31758_2909(nagB)
            SFL: SF0615(nagB)
            SFX: S0626(nagB)
            SFV: SFV_0653(nagB)
            SSN: SSON_0632(nagB)
            SBO: SBO_0540(nagB)
            SDY: SDY_0612(nagB)
            ECA: ECA1326(nagB)
            PLU: plu1317(nagB)
            SGL: SG0858
            BFL: Bfl323(nagB)
            BPN: BPEN_331(nagB)
            HIN: HI0141(nagB)
            HIT: NTHI0227(nagB)
            HIP: CGSHiEE_02580(nagB)
            HDU: HD1847(nagB)
            HSO: HS_1027(nagB)
            PMU: PM0875(nagB)
            MSU: MS2205(nagB)
            APL: APL_1755(nagB)
            XFA: XF1464
            XFT: PD0683(glmS)
            XCC: XCC3411(glmS)
            XCB: XC_0753
            XCV: XCV0770(glmS)
            XAC: XAC0714(glmS)
            XOO: XOO3917(glmS)
            XOM: XOO_3696(XOO3696)
            VCH: VCA1025
            VCO: VC0395_0216(nagB)
            VVU: VV2_1200
            VVY: VVA0028
            VPA: VPA0038
            VFI: VF2357
            PPR: PBPRA1031 PBPRB0360
            PAE: PA3759
            PAU: PA14_15810(glmS)
            PFL: PFL_1080
            PFO: Pfl_1005
            SON: SO_3506
            CPS: CPS_1008(nagB)
            PHA: PSHAb0148(nagB)
            HCH: HCH_06984(nagB)
            AHA: AHA_1526(nagB)
            CVI: CV_0557
            REH: H16_A0315(nagB)
            BMA: BMA3170
            BXE: Bxe_A4154
            BPS: BPSL0497
            BPM: BURPS1710b_0722
            BTE: BTH_I0448
            MXA: MXAN_6371(nagB)
            SFU: Sfum_2912
            MLO: mll4767
            MES: Meso_1508 Meso_2864
            SME: SMc02877
            ATU: Atu2607(glmS)
            ATC: AGR_C_4724
            RET: RHE_CH04036(glmS2)
            RLE: RL4603
            BME: BMEII0384
            BMF: BAB2_0323(nagB)
            BMS: BRA0912(nagB)
            BMB: BruAb2_0321(nagB)
            CCR: CC_0444 CC_0535
            SIL: SPO1843
            JAN: Jann_0886
            RDE: RD1_1726
            GOX: GOX1470
            MAG: amb2734
            ABA: Acid345_2909
            BSU: BG12631(nagB) BG12746(gamA)
            BHA: BH0420(nagB)
            BAN: BA4273(nagB)
            BAR: GBAA4273(nagB)
            BAA: BA_4733
            BAT: BAS3964
            BCE: BC4054
            BCA: BCE_4121(nagB)
            BCZ: BCZK3810(nagB)
            BTK: BT9727_3795(nagB)
            BLI: BL00085(nagB) BL00599(nagBA)
            BLD: BLi00726(nagB) BLi04349
            BCL: ABC1490(nagB)
            BPU: BPUM_3139
            OIH: OB0611
            GKA: GK2276
            SAU: SA0527(nagB)
            SAV: SAV0569(nagB)
            SAM: MW0524(nagB)
            SAR: SAR0573
            SAS: SAS0527
            SAC: SACOL0616(nagB)
            SAB: SAB0519
            SAA: SAUSA300_0554
            SAO: SAOUHSC_00552
            SEP: SE0340
            SER: SERP0215(nagB)
            SHA: SH0278
            SSP: SSP0235 SSP2149
            LMO: lmo0957 lmo2358
            LMF: LMOf2365_0977(nagB) LMOf2365_2328
            LIN: lin0956 lin2452
            LWE: lwe0939(nagB) lwe2301
            LLA: L14408(nagB)
            LLC: LACR_1667
            LLM: llmg_0928(nagB) llmg_2157(nagB2)
            SPY: SPy_1399(nagB)
            SPZ: M5005_Spy_1139(nagB)
            SPM: spyM18_1407(nagB)
            SPG: SpyM3_1065(nagB)
            SPS: SPs0798
            SPH: MGAS10270_Spy1209(nagB)
            SPI: MGAS10750_Spy1246(nagB)
            SPJ: MGAS2096_Spy1205(nagB)
            SPK: MGAS9429_Spy1186(nagB)
            SPF: SpyM50718(nagB)
            SPA: M6_Spy1114
            SPB: M28_Spy1133(nagB)
            SPN: SP_1415
            SPR: spr1272(nagB)
            SPD: SPD_1246(nagB)
            SAG: SAG0799(nagB)
            SAN: gbs0819
            SAK: SAK_0924(nagB)
            SMU: SMU.636
            STC: str0541(nagB)
            STL: stu0541(nagB)
            SSA: SSA_0746(nagB)
            SGO: SGO_1586(nagB)
            LPL: lp_0226(gnp)
            LJO: LJ1823
            LAC: LBA1948
            LSA: LSA0417(nagB)
            LSL: LSL_1465(nagB)
            LDB: Ldb2190(nagB)
            LBU: LBUL_2010
            LBR: LVIS_0689
            LCA: LSEI_2889
            EFA: EF0466(nagB)
            OOE: OEOE_0644
            STH: STH606
            CAC: CAC0187(nagB)
            CPE: CPE2434(nagB)
            CPF: CPF_2744(nagB)
            CPR: CPR_2431(nagB)
            CTC: CTC02631
            CNO: NT01CX_1482(nagB)
            CDF: CD1011(glmD)
            CBO: CBO2833(glmD)
            CBA: CLB_2777(nagB)
            CBH: CLC_2710(nagB)
            CBF: CLI_2883(nagB)
            DSY: DSY3827
            TTE: TTE1023(nagB)
            MPU: MYPU_3620(nagB)
            MPE: MYPE1760(nagB)
            MMY: MSC_0129(nagB) MSC_0821(nagB)
            MHY: mhp591(nagB)
            MHJ: MHJ_0576(nagB)
            MHP: MHP7448_0575(nagB)
            MSY: MS53_0193(nagB)
            MCP: MCAP_0128(nagB2) MCAP_0749(nagB1)
            MSM: MSMEG_0501 MSMEG_2118(nagB)
            CGL: NCgl2555(cgl2644)
            CGB: cg2928(nagB)
            CEF: CE2518
            CDI: DIP0521
            RHA: RHA1_ro01547
            SCO: SCO5236(nagB)
            SMA: SAV3018(gamA)
            LXX: Lxx19480(nagB)
            CMI: CMM_0354(nagB)
            AAU: AAur_2579(nagB)
            PAC: PPA0476
            SEN: SACE_0498(glmS)
            BLO: BL1343
            RXY: Rxyl_1731
            FNU: FN1143
            RBA: RB1355 RB2532(nagB) RB3340 RB3556(gpi2)
            BBU: BB0152(nagB)
            BGA: BG0150(nagB)
            BAF: BAPKO_0153(nagB)
            TDE: TDE0337(nagB)
            SYW: SYNW0540(nagB)
            SYC: syc0446_d
            SYF: Synpcc7942_1103
            SYD: Syncc9605_2143
            SYE: Syncc9902_0534
            SYG: sync_2246
            SYR: SynRCC307_1837(nagB)
            SYX: SynWH7803_1974(nagB)
            ANA: all0727
            AVA: Ava_4629
            PMT: PMT1424
            PMF: P9303_05361
            TER: Tery_2627
            BTH: BT_0258 BT_3587 BT_4127
            BFR: BF0984 BF3116
            BFS: BF0905(nagB) BF2953
            PGI: PG0803(nagB) PG1285
            SRU: SRU_2530
            CHU: CHU_1660(nagB)
            DRA: DR_A0154
            TTH: TTC1074
            TTJ: TTHA1439
STRUCTURES  PDB: 1J5X  1JT9  1NE7  2BKV  2BKX  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.99.6
            ExPASy - ENZYME nomenclature database: 3.5.99.6
            ExplorEnz - The Enzyme Database: 3.5.99.6
            ERGO genome analysis and discovery system: 3.5.99.6
            BRENDA, the Enzyme Database: 3.5.99.6
            CAS: 9013-10-9
///
ENTRY       EC 3.5.99.7                 Enzyme
NAME        1-aminocyclopropane-1-carboxylate deaminase;
            1-aminocyclopropane-1-carboxylate endolyase (deaminating)
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In other compounds
SYSNAME     1-aminocyclopropane-1-carboxylate aminohydrolase (isomerizing)
REACTION    1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
            [RN:R00997]
ALL_REAC    R00997
SUBSTRATE   1-aminocyclopropane-1-carboxylate [CPD:C01234];
            H2O [CPD:C00001]
PRODUCT     2-oxobutanoate [CPD:C00109];
            NH3 [CPD:C00014]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal 5'-phosphate enzyme. Its introduction has been used to
            make fruit ripening dependent on externally added ethylene, as it
            removes the substrate for endogenous ethylene formation.
REFERENCE   1
  AUTHORS   Honma, M. and Shimomura, T.
  TITLE     Metabolism of 1-aminocyclopropane-1-carboxylic acid.
  JOURNAL   Agric. Biol. Chem. 42 (1978) 1825-1831.
REFERENCE   2
  AUTHORS   Yao, M., Ose, T., Sugimoto, H., Horiuchi, A., Nakagawa, A.,
            Wakatsuki, S., Yokoi, D., Murakami, T., Honma, M. and Tanaka, I.
  TITLE     Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase
            from Hansenula saturnus.
  JOURNAL   J. Biol. Chem. 275 (2000) 34557-34565.
PATHWAY     PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K01505  1-aminocyclopropane-1-carboxylate deaminase
GENES       SPU: 578025(LOC578025)
            OSA: 4330881
            SPO: SPAC922.03
            AFM: AFUA_2G01030 AFUA_5G03420
            AOR: AO090701000360
            CNE: CNB00190
            ECW: EcE24377A_2153(dcyD)
            ECA: ECA1531
            PAU: PA14_24190
            PPU: PP_2009
            PST: PSPTO_3675 PSPTO_3802
            PSB: Psyr_1676 Psyr_1801
            PSP: PSPPH_1673 PSPPH_1761
            PFL: PFL_3968
            PFO: Pfl_3686
            PEN: PSEEN1704
            PAR: Psyc_1604
            PCR: Pcryo_1828
            SFR: Sfri_2321
            SPL: Spea_4164
            SHN: Shewana3_2469
            PHA: PSHAa2700(dcyD)
            PAT: Patl_0753 Patl_1784 Patl_2666
            SDE: Sde_1663 Sde_1730
            LPN: lpg1367
            LPF: lpl1318
            LPP: lpp1321
            FTH: FTH_0847
            HCH: HCH_04594
            RSO: RS05576(RSp0646)
            REH: H16_B1365(acd)
            BMA: BMAA0952
            BMV: BMASAVP1_0426
            BML: BMA10299_0218
            BMN: BMA10247_A1385
            BXE: Bxe_B1212
            BVI: Bcep1808_3930
            BUR: Bcep18194_B2860 Bcep18194_C6869
            BCN: Bcen_4794
            BCH: Bcen2424_3374
            BAM: Bamb_5155
            BPS: BPSS1324
            BPM: BURPS1710b_A0344
            BPL: BURPS1106A_A1795
            BPD: BURPS668_A1880
            BTE: BTH_II1101
            BPA: BPP4074
            BBR: BB4545
            POL: Bpro_2169 Bpro_3828
            AAV: Aave_0697 Aave_4493
            AJS: Ajs_3877
            MPT: Mpe_A3598
            DVL: Dvul_0604
            DDE: Dde_2581
            ADE: Adeh_1432
            AFW: Anae109_2397
            SFU: Sfum_1836
            MLO: mlr5932
            PLA: Plav_0934
            SMD: Smed_5532 Smed_6456
            RLE: pRL100087(acdS)
            BJA: blr0241
            BRA: BRADO3803
            BBT: BBta_4127
            RPE: RPE_2871
            XAU: Xaut_4875 Xaut_5055
            CCR: CC_2032
            SIL: SPO2657 SPOA0158
            JAN: Jann_2876
            RDE: RD1_0819 RD1_1838
            BAN: BA3236
            BCE: BC3216
            BCZ: BCZK2930
            BTK: BT9727_2992
            SSP: SSP0338
            AMT: Amet_0592
            DRM: Dred_0406 Dred_0413
            MSM: MSMEG_6740
            SCO: SCO5247(2SC7G11.09c)
            SMA: SAV1520 SAV3009
            NCA: Noca_4819 Noca_4836
            KRA: Krad_0767
            SEN: SACE_1968 SACE_2778(acd)
            LIL: LA1889
            LIC: LIC12009
            LBJ: LBJ_1506
            LBL: LBL_1730
            ANA: alr4447
            AVA: Ava_1372
            CHU: CHU_3479(yedO)
            GFO: GFO_0238
            FPS: FP1206(acdS)
            TMA: TM0225
            PHO: PH0054
            PAB: PAB2303
            PFU: PF0010
STRUCTURES  PDB: 1RQX  1TYZ  1TZ2  1TZJ  1TZK  1TZM  
DBLINKS     IUBMB Enzyme Nomenclature: 3.5.99.7
            ExPASy - ENZYME nomenclature database: 3.5.99.7
            ExplorEnz - The Enzyme Database: 3.5.99.7
            ERGO genome analysis and discovery system: 3.5.99.7
            UM-BBD (Biocatalysis/Biodegradation Database): 3.5.99.7
            BRENDA, the Enzyme Database: 3.5.99.7
            CAS: 69553-48-6
///
ENTRY       EC 3.5.99.-                 Enzyme
CLASS       Hydrolases;
            Acting on carbon-nitrogen bonds, other than peptide bonds;
            In other compounds
REACTION    (1) 2,4-Dihydroxy-6-(N'-ethyl)amino-1,3,5-triazine + H2O <=>
            Cyanuric acid + Ethylamine [RN:R05573];
            (2) Deisopropylhydroxyatrazine + H2O <=>
            2,4-Dihydroxy-6-(N'-ethyl)amino-1,3,5-triazine + NH3 [RN:R05574];
            (3) 2-Hydroxy-4,6-diamino-1,3,5-triazine + H2O <=>
            2,4-Dihydroxy-6-amino-1,3,5-triazine + NH3 [RN:R06969]
SUBSTRATE   2,4-Dihydroxy-6-(N'-ethyl)amino-1,3,5-triazine [CPD:C06558];
            H2O [CPD:C00001];
            Deisopropylhydroxyatrazine [CPD:C06557];
            2-Hydroxy-4,6-diamino-1,3,5-triazine [CPD:C08733]
PRODUCT     Cyanuric acid [CPD:C06554];
            Ethylamine [CPD:C00797];
            2,4-Dihydroxy-6-(N'-ethyl)amino-1,3,5-triazine [CPD:C06558];
            NH3 [CPD:C00014];
            2,4-Dihydroxy-6-amino-1,3,5-triazine [CPD:C08734]
///
ENTRY       EC 3.6.1.1                  Enzyme
NAME        inorganic diphosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     diphosphate phosphohydrolase
REACTION    diphosphate + H2O = 2 phosphate [RN:R00004]
ALL_REAC    R00004
SUBSTRATE   diphosphate [CPD:C00013];
            H2O [CPD:C00001]
PRODUCT     phosphate [CPD:C00009]
COFACTOR    Metal [CPD:C00050]
COMMENT     Specificity varies with the source and with the activating metal
            ion. The enzyme from some sources may be identical with EC 3.1.3.1
            (alkaline phosphatase) or EC 3.1.3.9 (glucose-6-phosphatase). A form
            of this enzyme with a molecular mass of about 90 kDa is found in
            tonoplasts of plants and fungi, where it imports protons from the
            cytosol into the vacuolar lumen.
REFERENCE   1
  AUTHORS   Bailey, K. and Webb, E.C.
  TITLE     Purification and properties of yeast pyrophosphatase.
  JOURNAL   Biochem. J. 38 (1944) 394-398.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:14898026]
  AUTHORS   KUNITZ M.
  TITLE     Crystalline inorganic pyrophosphatase isolated from baker's yeast.
  JOURNAL   J. Gen. Physiol. 35 (1952) 423-50.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Rafter, G.W.
  TITLE     Pyrophosphate metabolism in liver mitochondria.
  JOURNAL   J. Biol. Chem. 235 (1960) 2475-2477.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map00190  Oxidative phosphorylation
ORTHOLOGY   KO: K01507  inorganic pyrophosphatase
            KO: K06019  pyrophosphatase PpaX
GENES       HSA: 27068(PPA2) 5464(PPA1)
            MMU: 67895(Ppa1) 74776(Ppa2)
            CFA: 478500(PPA2) 479238(PPA1)
            BTA: 280701(PP)
            GGA: 422539(PPA2) 769424(PPA1)
            XLA: 431992(MGC81379) 444459(MGC83669)
            XTR: 496951(LOC496951)
            SPU: 588414(LOC588414)
            DME: Dmel_CG32149(RhoGAP71E) Dmel_CG4634(Nurf-38)
            ATH: AT1G01050 AT1G15690(AVP1) AT2G18230 AT2G46860 AT3G53620
                 AT4G01480
            OSA: 4324298 4325072 4326846 4329579 4330457 4330852 4331044
                 4337476 4337608 4337864 4338911 4340298 4341645
            CME: CMR255C
            SCE: YBR011C(IPP1) YMR267W(PPA2)
            AGO: AGOS_AER015C AGOS_AER283W
            PIC: PICST_55811(PPA2) PICST_83097(IPP1)
            CGR: CAGL0H02233g CAGL0H09878g
            SPO: SPAC23C11.05(ppa1) SPAC3A12.02
            ANI: AN2968.2
            AFM: AFUA_3G08380 AFUA_6G08490
            AOR: AO090005001437
            CNE: CNE00210
            ECU: ECU10_0340
            DDI: DDBDRAFT_0185935
            PFA: MAL3P6.3 PF14_0541
            CPV: cgd4_1400
            CHO: Chro.40159
            TAN: TA13735
            TET: TTHERM_00105560 TTHERM_00143770 TTHERM_00218790
                 TTHERM_00392790 TTHERM_00735340 TTHERM_00997670
            TBR: Tb927.3.2840 Tb927.4.4380
            TCR: 508153.820 508181.140 510773.20 511385.30
            LMA: LmjF03.0910 LmjF31.1220
            EHI: 302.t00006
            ECO: b4226(ppa)
            ECJ: JW4185(ppa)
            ECE: Z5837(ppa)
            ECS: ECs5204
            ECC: c5323(ppa)
            ECI: UTI89_C4831(ppa)
            ECP: ECP_4476
            ECV: APECO1_2165(ppa)
            ECW: EcE24377A_4795(ppa)
            ECX: EcHS_A4479
            STY: STY4773(ppa)
            STT: t4468(ppa)
            SPT: SPA4234(ppa)
            SEC: SC4288(ppa)
            STM: STM4414(ppa)
            YPE: YPO3521(ppa)
            YPK: y0663(ppa)
            YPM: YP_0562(ppa)
            YPA: YPA_0071
            YPN: YPN_3265
            YPP: YPDSF_3570
            YPS: YPTB0455(ppa)
            YPI: YpsIP31758_3622(ppa)
            YEN: YE0408(ppa)
            SFL: SF4264(ppa)
            SFX: S4527(ppa)
            SFV: SFV_4265(ppa)
            SSN: SSON_4408(ppa)
            SBO: SBO_4219(ppa)
            SDY: SDY_4462(ppa)
            ECA: ECA3593(ppa)
            PLU: plu4551(ppa)
            BUC: BU088(ppa)
            BAS: BUsg081(ppa)
            BAB: bbp082(ppa)
            BCC: BCc_053(ppa)
            WBR: WGLp480(ppa)
            SGL: SG0355
            ENT: Ent638_0411 Ent638_2049
            KPN: KPN_04621(ppa)
            SPE: Spro_0462
            BFL: Bfl091(ppa)
            BPN: BPEN_094(ppa)
            HIT: NTHI0214(ppa)
            HDU: HD0169(ppa)
            HSO: HS_1513(ppa)
            PMU: PM1191(ppa)
            MSU: MS2221(ppa)
            APL: APL_1899(ppa)
            ASU: Asuc_0522
            XFA: XF2171
            XFT: PD1226(ppa)
            XCC: XCC3312 XCC3314(ppa)
            XCB: XC_0851 XC_0853
            XCV: XCV3568(hppA) XCV3570(ppa)
            XAC: XAC3440 XAC3442(ppa)
            XOO: XOO0952(ppa) XOO0954
            XOM: XOO_0872(XOO0872) XOO_0874(XOO0874)
            VCH: VC1687 VC2545
            VCO: VC0395_A2123(ppa)
            VVU: VV1_0708 VV1_2888
            VVY: VV0432 VV1381
            VPA: VP0311 VP1165
            VFI: VFA0421
            PPR: PBPRA0383 PBPRA1513
            PAE: PA4031(p)
            PAU: PA14_11690(ppa)
            PAP: PSPA7_1074(ppa)
            PPU: PP_0538(ppa)
            PPF: Pput_0577
            PST: PSPTO_0722(ppa-1) PSPTO_4615(ppa-2)
            PSB: Psyr_0624 Psyr_1481
            PSP: PSPPH_2719 PSPPH_4672(ppa)
            PFL: PFL_5478(ppa)
            PFO: Pfl_4996
            PEN: PSEEN0626(ppa)
            PMY: Pmen_3829
            PAR: Psyc_1296(ppa)
            PCR: Pcryo_1083
            PRW: PsycPRwf_0971
            ACI: ACIAD0239(ppa)
            SON: SO_4190(ppaC)
            SDN: Sden_0478
            SFR: Sfri_3561
            SAZ: Sama_0598
            SBL: Sbal_3886
            SBM: Shew185_0428
            SLO: Shew_1975
            SPC: Sputcn32_0515
            SSE: Ssed_0372 Ssed_2173
            SPL: Spea_2180
            SHE: Shewmr4_3542
            SHM: Shewmr7_0413
            SHN: Shewana3_3717
            SHW: Sputw3181_3655
            ILO: IL2263(ppa)
            CPS: CPS_0391(ppaC)
            PHA: PSHAa0445(ppa)
            PAT: Patl_0140
            SDE: Sde_3364
            MAQ: Maqu_3439
            CBU: CBU_0628(ppa)
            CBD: COXBU7E912_0640(ppa)
            LPN: lpg2764(ppa)
            LPF: lpl2681(ppa)
            LPP: lpp2812(ppa)
            MCA: MCA0112(ppa) MCA1188 MCA1252(hppA)
            FTU: FTT1028c(ppa)
            FTF: FTF1028c(ppa)
            FTW: FTW_0935(ppa)
            FTL: FTL_1061
            FTH: FTH_1037(ppa)
            FTA: FTA_1120(ppa)
            FTN: FTN_0906(ppa)
            TCX: Tcr_1496
            NOC: Noc_1134 Noc_1901
            AEH: Mlg_0111 Mlg_0606
            HHA: Hhal_2005
            HCH: HCH_01060
            CSA: Csal_2281 Csal_2390
            ABO: ABO_1994(ppa)
            MMW: Mmwyl1_3224
            AHA: AHA_2987 AHA_3550(ppa)
            DNO: DNO_0198(ppa)
            BCI: BCI_0608(ppa)
            RMA: Rmag_0092 Rmag_0356
            VOK: COSY_0096 COSY_0343(ppa)
            NME: NMB0641
            NMA: NMA0851(ppa)
            NMC: NMC0584(ppa)
            NGO: NGO0223
            CVI: CV_3372(ppa)
            RSO: RSc2349(ppa)
            REU: Reut_A2613
            REH: H16_A0746(ppa)
            RME: Rmet_0678
            BMA: BMA0736(ppa)
            BMV: BMASAVP1_A2277(ppa)
            BML: BMA10299_A3007(ppa)
            BMN: BMA10247_1590(ppa)
            BXE: Bxe_A3400
            BVI: Bcep1808_2503
            BUR: Bcep18194_A5744
            BCN: Bcen_1805
            BCH: Bcen2424_2417
            BAM: Bamb_2462
            BPS: BPSL1021(ppa)
            BPM: BURPS1710b_1237(ppa) BURPS1710b_A0979(hit)
            BPL: BURPS1106A_1084(ppa)
            BPD: BURPS668_1078(ppa)
            BTE: BTH_I0878(ppa)
            PNU: Pnuc_0685 Pnuc_0686
            BPE: BP2533(ppa)
            BPA: BPP2646(ppa)
            BBR: BB2089(ppa)
            RFR: Rfer_1472 Rfer_1473
            POL: Bpro_2299 Bpro_2300
            PNA: Pnap_1701 Pnap_1702
            AAV: Aave_2668 Aave_2669
            AJS: Ajs_1757 Ajs_1758
            VEI: Veis_3002 Veis_3003
            MPT: Mpe_A2120 Mpe_A2121
            HAR: HEAR1011(ppa) HEAR2486
            MMS: mma_1146 mma_2575(rrpP)
            NEU: NE1935
            NET: Neut_0786
            NMU: Nmul_A0739 Nmul_A2093 Nmul_A2699
            EBA: ebA594 ebA7053(ppa)
            AZO: azo1358(ppa)
            DAR: Daro_1289 Daro_3203
            TBD: Tbd_1500(hppA) Tbd_1652
            MFA: Mfla_2240
            HPY: HP0620
            HPJ: jhp0564(ppa)
            HPA: HPAG1_0603
            HHE: HH1848(ppa)
            HAC: Hac_0836(ppa)
            WSU: WS1784(PPA)
            TDN: Tmden_1155
            CJE: Cj0638c(ppa)
            CJR: CJE0741(ppa)
            CJJ: CJJ81176_0666(ppa)
            CJU: C8J_0597(ppa)
            CJD: JJD26997_1361(ppa)
            CFF: CFF8240_1198(ppa)
            CCV: CCV52592_0470(ppa)
            CHA: CHAB381_0294(ppa) CHAB381_1600
            CCO: CCC13826_1978(ppa)
            ABU: Abu_0097 Abu_1578(ppa)
            NIS: NIS_0766(ppa)
            SUN: SUN_1298
            GSU: GSU2975 GSU3291(hppA)
            GME: Gmet_0503 Gmet_3239(hppA)
            GUR: Gura_0646 Gura_4157
            PCA: Pcar_1659 Pcar_2001 Pcar_3036
            PPD: Ppro_0753 Ppro_3037
            DVU: DVU1636(ppaC)
            DVL: Dvul_1498
            DDE: Dde_1778
            LIP: LI0501(ppa)
            BBA: Bd0571 Bd1715(ppa)
            DPS: DP2180
            ADE: Adeh_1282 Adeh_1780 Adeh_4099 Adeh_4307
            AFW: Anae109_2485 Anae109_4452
            MXA: MXAN_0862(ppa) MXAN_1671 MXAN_5577(ppa)
            SAT: SYN_02770 SYN_02772
            SFU: Sfum_2995 Sfum_3037
            RPR: RP589
            RTY: RT0578(ppa)
            RCO: RC0897(ppa)
            RFE: RF_0962(ppa)
            RBE: RBE_0697(ppa)
            RAK: A1C_04580
            RBO: A1I_04575
            RRI: A1G_04955
            OTS: OTBS_2146(ppa)
            WOL: WD1263(ppa)
            WBM: Wbm0583
            AMA: AM1020(ppa)
            APH: APH_1101(ppa)
            ERU: Erum7840(ppa)
            ERW: ERWE_CDS_08290(ppa)
            ERG: ERGA_CDS_08190(ppa)
            ECN: Ecaj_0819
            ECH: ECH_1014(ppa)
            NSE: NSE_0734(ppa)
            PUB: SAR11_1040(hppA)
            MLO: mll4120 mlr8418 mlr8562
            MES: Meso_1141 Meso_3230
            PLA: Plav_1376 Plav_2916
            SME: SMc01780(rrpP) SMc03239(ppa)
            SMD: Smed_0824 Smed_2974
            ATU: Atu1174(rrpP) Atu2661(ppa)
            ATC: AGR_C_2169 AGR_C_4822
            RET: RHE_CH01527(rrpP) RHE_CH03913(ppa)
            RLE: RL1634(hppA) RL4504(ppa)
            BME: BMEI0076 BMEI1185(hppA)
            BMF: BAB1_0793 BAB1_1993(ppa)
            BMS: BR0771 BR1993(ppa)
            BMB: BruAb1_0787(hppA) BruAb1_1968(ppa)
            BOV: BOV_0764 BOV_1919(ppa)
            OAN: Oant_0988 Oant_1233 Oant_2524
            BJA: bll5026(rrpP) bll7647 blr0548(ppa)
            BRA: BRADO0275(ppa) BRADO4423(hppA)
            BBT: BBta_0268(ppa) BBta_4642(hppA)
            RPA: RPA0411(ppa) RPA2731
            RPB: RPB_0106 RPB_2641
            RPC: RPC_0040 RPC_2666
            RPD: RPD_0696 RPD_2678
            RPE: RPE_0044 RPE_2815
            NWI: Nwi_0484 Nwi_1747(hppA)
            NHA: Nham_0610 Nham_2182
            BHE: BH01690(ppa)
            BQU: BQ01580(ppa)
            BBK: BARBAKC583_0329(ppa)
            XAU: Xaut_2496 Xaut_4197
            CCR: CC_0047 CC_1363(hppA)
            SIL: SPO3147(ppaC)
            SIT: TM1040_0592
            RSP: RSP_2307
            RSH: Rsph17029_0982
            RSQ: Rsph17025_2193
            JAN: Jann_3361
            RDE: RD1_3520(ppaC)
            PDE: Pden_3659
            MMR: Mmar10_0303 Mmar10_1528
            HNE: HNE_0016(ppa) HNE_1158
            ZMO: ZMO1507(ppa)
            NAR: Saro_0292 Saro_1067
            SAL: Sala_2023 Sala_3057
            SWI: Swit_2532 Swit_2772
            ELI: ELI_02570 ELI_14255
            GOX: GOX0757
            GBE: GbCGDNIH1_0199
            ACR: Acry_2488
            RRU: Rru_A0146 Rru_A1818
            MAG: amb2348 amb4486
            MGM: Mmc1_1754 Mmc1_3432
            ABA: Acid345_1918 Acid345_3968
            SUS: Acid_2857 Acid_3005 Acid_3034 Acid_5542
            BSU: BG10014(ppaC) BG14127(hprP)
            BHA: BH1604 BH3587
            BAN: BA2826(ppaC) BA5390
            BAR: GBAA2826(ppaC) GBAA5390
            BAA: BA_0248 BA_3347
            BAT: BAS2635 BAS5010
            BCE: BC2826 BC5162
            BCA: BCE_2854(ppaC) BCE_5265
            BCZ: BCZK2551(ppx) BCZK4854
            BCY: Bcer98_1924
            BTK: BT9727_2585(ppx) BT9727_4839
            BLI: BL02502(ppaC) BL03404(hprP)
            BLD: BLi03882(ppaC)
            BCL: ABC2903(ppaC) ABC3052(hprP)
            BAY: RBAM_037630
            BPU: BPUM_3708
            OIH: OB1018 OB2479
            GKA: GK2246 GK3079
            SAU: SA1735
            SAV: SAV1919
            SAM: MW1860
            SAR: SAR2012(ppaC)
            SAS: SAS1843
            SAC: SACOL1982(ppaC)
            SAB: SAB1856(ppaC)
            SAA: SAUSA300_1900(ppaC)
            SAO: SAOUHSC_02140
            SAJ: SaurJH9_1975
            SAH: SaurJH1_2009
            SEP: SE1602
            SER: SERP1455(ppaC)
            SHA: SH1034
            SSP: SSP0872
            LMO: lmo1448 lmo2481
            LMF: LMOf2365_1467(ppaC) LMOf2365_2454
            LIN: lin1486 lin2624
            LWE: lwe1464(ppaC) lwe2429
            LLA: L62663(yshC)
            LLC: LACR_0627 LACR_1998
            LLM: llmg_1996(ppa)
            SPY: SPy_0380
            SPZ: M5005_Spy_0319(ppaC)
            SPM: spyM18_0434
            SPG: SpyM3_0278
            SPS: SPs1581
            SPH: MGAS10270_Spy0314(ppaC)
            SPI: MGAS10750_Spy0313(ppaC)
            SPJ: MGAS2096_Spy0336(ppaC)
            SPK: MGAS9429_Spy0318(ppaC)
            SPF: SpyM51539(ppaC)
            SPA: M6_Spy0345
            SPB: M28_Spy0308(ppaC)
            SPN: SP_1534
            SPR: spr1389(ppaC)
            SPD: SPD_1363(ppaC)
            SAG: SAG1397(ppa)
            SAN: gbs1467
            SAK: SAK_1430(ppaC)
            SMU: SMU.1687(ppaC)
            STC: str0372(ppaC)
            STL: stu0372(ppaC)
            SSA: SSA_1748(ppx)
            SGO: SGO_1648(ppx1)
            LPL: lp_1837
            LJO: LJ1173
            LAC: LBA1125
            LSA: LSA0971(ppa)
            LSL: LSL_0833(ppa)
            LDB: Ldb0995(ppaC)
            LBU: LBUL_0902
            LBR: LVIS_0807
            LCA: LSEI_1414 LSEI_1528
            LRE: Lreu_0785
            EFA: EF1611(ppaC)
            OOE: OEOE_1028
            STH: STH2562 STH3141 STH338
            CAC: CAC2138
            CPE: CPE1977 CPE2055
            CPF: CPF_2312
            CPR: CPR_1944 CPR_2027
            CTC: CTC00383 CTC01649
            CNO: NT01CX_1416 NT01CX_1928
            CTH: Cthe_1425
            CDF: CD0333(ppaC)
            CBE: Cbei_4245 Cbei_5050
            CKL: CKL_1176(ppaC)
            AMT: Amet_1702 Amet_3574
            CHY: CHY_0286
            DSY: DSY3890 DSY4836
            DRM: Dred_2097 Dred_2985
            SWO: Swol_0602 Swol_1064
            CSC: Csac_0905
            TTE: TTE0284 TTE2216(gph) TTE2447(ppx1)
            MTA: Moth_0418 Moth_1349 Moth_2414
            MGE: MG_351(ppa)
            MPN: MPN528(ppa)
            MPU: MYPU_4700(ppa)
            MPE: MYPE4400(ppa)
            MGA: MGA_1121(ppa)
            MMY: MSC_0404(ppa)
            MMO: MMOB5210(ppa)
            MHY: mhp622(ppa)
            MHJ: MHJ_0605(ppa)
            MHP: MHP7448_0603(ppa)
            MSY: MS53_0148(ppa)
            MCP: MCAP_0581(ppa)
            UUR: UU315(ppa)
            POY: PAM145(ppa)
            AYW: AYWB_575(ppa)
            MFL: Mfl544
            MTU: Rv3628(ppa)
            MTC: MT3730(ppa)
            MBO: Mb3652(ppa)
            MBB: BCG_3686(ppa)
            MLE: ML0210(ppa)
            MPA: MAP0435c(ppa)
            MAV: MAV_0527(ppa)
            MSM: MSMEG_6114(ppa)
            MVA: Mvan_5381
            MGI: Mflv_1408
            MMC: Mmcs_4779
            MKM: Mkms_4865
            MJL: Mjls_5165
            CGL: NCgl2607(cgl2700)
            CGB: cg2988(ppa)
            CEF: CE2546
            CDI: DIP2006(ppa)
            CJK: jk0274(ppa)
            NFA: nfa3850
            RHA: RHA1_ro04400
            SCO: SCO3409(ppa) SCO3547(SCH5.10c)
            SMA: SAV4616 SAV4661(ppa)
            TWH: TWT154(ppa) TWT307(ppa)
            TWS: TW465(ppa1) TW618(ppa2)
            LXX: Lxx21530(ppa)
            ART: Arth_0146
            PAC: PPA0256
            NCA: Noca_0372 Noca_0438
            TFU: Tfu_0134 Tfu_2902
            FRA: Francci3_4304 Francci3_4310
            FAL: FRAAL6577(hppA) FRAAL6584(ppa)
            ACE: Acel_0199 Acel_1973
            KRA: Krad_0485 Krad_0526
            SEN: SACE_0375 SACE_0391(ppa)
            STP: Strop_4030 Strop_4313
            BLO: BL0389(ppa)
            BAD: BAD_1444(ppa)
            RXY: Rxyl_0826 Rxyl_2042
            FNU: FN0099 FN1824 FN2030
            RBA: RB7084(ppaC)
            CTR: CT772(ppa)
            CTA: CTA_0842(ppa)
            CMU: TC0153
            CPN: CPn0918(ppa)
            CPA: CP0948
            CPJ: CPj0918(ppa)
            CPT: CpB0950
            CCA: CCA00851(ppa)
            CAB: CAB816
            CFE: CF0165(ppa)
            LIL: LA1471 LA4040
            LIC: LIC12285(avp) LIC13223(ppa)
            LBJ: LBJ_0230 LBJ_0973
            LBL: LBL_2060 LBL_2850
            SYN: slr1622(ppa)
            SYW: SYNW1769(ppa) SYNW1788
            SYC: syc0172_d(ppa)
            SYF: Synpcc7942_1383
            SYD: Syncc9605_0677 Syncc9605_0695
            SYE: Syncc9902_1663 Syncc9902_1684
            SYG: sync_2018(ppa-1) sync_2039(ppa-2)
            SYR: SynRCC307_0873(ppa) SynRCC307_1117(ppa)
            SYX: SynWH7803_0605(ppa) SynWH7803_0624(ppa)
            CYA: CYA_0251(ppa)
            CYB: CYB_2243(ppa)
            TEL: tll1883(ppa)
            GVI: glr4227
            ANA: all3570(ppa)
            AVA: Ava_3548
            PMA: Pro0493(ppa) Pro0510(ppa)
            PMM: PMM0494(ppa) PMM0511(ppa)
            PMT: PMT1257(ppa) PMT1275(ppa)
            PMN: PMN2A_1827 PMN2A_1844
            PMI: PMT9312_0495 PMT9312_0512
            PMB: A9601_05511 A9601_05681
            PMC: P9515_05581 P9515_05751
            PMF: P9303_07251 P9303_07471
            PMG: P9301_05211 P9301_05381
            PMH: P9215_05761
            PME: NATL1_05511 NATL1_05691
            TER: Tery_1519
            BTH: BT_3411
            BFR: BF0289
            BFS: BF0235
            SRU: SRU_0812 SRU_2000(ppa) SRU_2022(ppa)
            CHU: CHU_1243(ipyR) CHU_3108(ppa)
            GFO: GFO_0296(ppa) GFO_0297(hppA) GFO_2762(ppa)
            FJO: Fjoh_1478 Fjoh_1479
            FPS: FP0339(ppa)
            CTE: CT0823(ppa)
            CCH: Cag_0443 Cag_0444 Cag_1090
            CPH: Cpha266_1182 Cpha266_1408
            PVI: Cvib_0758 Cvib_1028
            PLT: Plut_1202 Plut_1277
            DET: DET0367(ppa) DET0766 DET0784
            DEH: cbdb_A309(ppa) cbdb_A738 cbdb_A761(hppA)
            DEB: DehaBAV1_0349 DehaBAV1_0692 DehaBAV1_0710
            RRS: RoseRS_2262 RoseRS_3220
            RCA: Rcas_3559 Rcas_3708
            DRA: DR_2576
            DGE: Dgeo_0332
            TTH: TTC1600
            TTJ: TTHA1965
            AAE: aq_1547(ppa)
            TMA: TM0174 TM0587
            TPT: Tpet_0331 Tpet_0751
            TME: Tmel_1837 Tmel_1903
            FNO: Fnod_1342
            MJA: MJ0608
            MMP: MMP0219(ppaC)
            MMQ: MmarC5_1463
            MMZ: MmarC7_1219
            MAE: Maeo_0439
            MVN: Mevan_1233
            MAC: MA2676(ppa) MA3879(ppa) MA3880(ppa)
            MBA: Mbar_A0186 Mbar_A1481 Mbar_A3712
            MMA: MM_0700 MM_0701 MM_1441 MM_3283
            MBU: Mbur_0994
            MHU: Mhun_1158 Mhun_2414
            MEM: Memar_0044 Memar_0491
            MBN: Mboo_0023 Mboo_1016
            MST: Msp_0625(ppa)
            MSI: Msm_0198
            MKA: MK1450(ppa)
            AFU: AF0756(ppx1)
            HAL: VNG0259G(ipp)
            HMA: rrnAC3323(ipp)
            HWA: HQ1231A(ipp)
            NPH: NP5192A(ipp)
            TAC: Ta0399
            TVO: TVN1189
            PTO: PTO1354
            PAB: PAB1104(ppa)
            PFU: PF0257
            TKO: TK1700
            RCI: RCIX317(ppa)
            APE: APE_1692.1
            SMR: Smar_0473
            IHO: Igni_0880
            HBU: Hbut_0867
            SSO: SSO2390(ppa)
            STO: ST0524
            SAI: Saci_0955(ppa)
            MSE: Msed_0648
            PAI: PAE1771
            PIS: Pisl_1724
            PCL: Pcal_0548
            PAS: Pars_0762
            TPE: Tpen_0136
            NEQ: NEQ461
STRUCTURES  PDB: 117E  1E6A  1E9G  1FAJ  1HUJ  1HUK  1I40  1I6T  1I74  1IGP  
                 1INO  1IPW  1JFD  1K20  1K23  1M38  1MJW  1MJX  1MJY  1MJZ  
                 1OBW  1PYP  1QEZ  1SXV  1TWL  1UDE  1WCF  1WGI  1WGJ  1WPM  
                 1WPN  1WPP  1YGZ  1YPP  2AU6  2AU7  2AU8  2AU9  2AUU  2BQX  
                 2BQY  2EB0  2EIP  2ENX  2HAW  2IHP  2IK0  2IK1  2IK2  2IK4  
                 2IK6  2IK7  2IK9  2IW4  2PRD  8PRK  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.1
            ExPASy - ENZYME nomenclature database: 3.6.1.1
            ExplorEnz - The Enzyme Database: 3.6.1.1
            ERGO genome analysis and discovery system: 3.6.1.1
            BRENDA, the Enzyme Database: 3.6.1.1
            CAS: 9024-82-2
///
ENTRY       EC 3.6.1.2                  Enzyme
NAME        trimetaphosphatase;
            inorganic trimetaphosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     trimetaphosphate hydrolase
REACTION    trimetaphosphate + H2O = triphosphate [RN:R02504]
ALL_REAC    R02504
SUBSTRATE   trimetaphosphate [CPD:C02466];
            H2O [CPD:C00001]
PRODUCT     triphosphate [CPD:C00536]
REFERENCE   1  [PMID:13278311]
  AUTHORS   KORNBERG SR.
  TITLE     Tripolyphosphate and trimetaphosphate in yeast extracts.
  JOURNAL   J. Biol. Chem. 218 (1956) 23-31.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:13115420]
  AUTHORS   MEYERHOF O, SHATAS R, KAPLAN A.
  TITLE     Heat of hydrolysis of trimetaphosphate.
  JOURNAL   Biochim. Biophys. Acta. 12 (1953) 121-7.
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K01508  trimetaphosphatase
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.2
            ExPASy - ENZYME nomenclature database: 3.6.1.2
            ExplorEnz - The Enzyme Database: 3.6.1.2
            ERGO genome analysis and discovery system: 3.6.1.2
            BRENDA, the Enzyme Database: 3.6.1.2
            CAS: 9024-84-4
///
ENTRY       EC 3.6.1.3                  Enzyme
NAME        adenosinetriphosphatase;
            adenylpyrophosphatase;
            ATP monophosphatase;
            triphosphatase;
            ATPase;
            SV40 T-antigen;
            adenosine 5'-triphosphatase;
            ATP hydrolase;
            ATPase;
            complex V (mitochondrial electron transport);
            (Ca2+ + Mg2+)-ATPase;
            HCO3--ATPase;
            adenosine triphosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     ATP phosphohydrolase
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     Many enzymes previously listed under this number are now listed
            separately under EC 3.6.3 and EC 3.6.4.
REFERENCE   1  [PMID:6267987]
  AUTHORS   Geider K, Hoffmann-Berling H.
  TITLE     Proteins controlling the helical structure of DNA.
  JOURNAL   Annu. Rev. Biochem. 50 (1981) 233-60.
REFERENCE   2
  AUTHORS   Kielley, W.W.
  TITLE     Myosin adenosine triphosphatase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 5, Academic Press, New York, 1961, p. 159-168.
REFERENCE   3  [PMID:6252965]
  AUTHORS   Martin SS, Senior AE.
  TITLE     Membrane adenosine triphosphatase activities in rat pancreas.
  JOURNAL   Biochim. Biophys. Acta. 602 (1980) 401-18.
  ORGANISM  rat [GN:rno]
REFERENCE   4
  AUTHORS   Njus, D., Knoth, J. and Zallakian, M.
  TITLE     Proton-linked transport in chromaffin granules.
  JOURNAL   Curr. Top. Bioenerg. 11 (1981) 107-147.
REFERENCE   5  [PMID:6114746]
  AUTHORS   Riley MV, Peters MI.
  TITLE     The localization of the anion-sensitive ATPase activity in corneal
            endothelium.
  JOURNAL   Biochim. Biophys. Acta. 644 (1981) 251-6.
REFERENCE   6  [PMID:6269805]
  AUTHORS   Tjian R.
  TITLE     Regulation of viral transcription and DNA replication by the SV40
            large T antigen.
  JOURNAL   Curr. Top. Microbiol. Immunol. 93 (1981) 5-24.
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01509  adenosinetriphosphatase
GENES       HSA: 954(ENTPD2)
            PTR: 464883(ENTPD2)
            MMU: 12496(Entpd2) 17705(ATP6) 17706(ATP8)
            RNO: 64467(Entpd2)
            CFA: 491241(ENTPD2)
            GGA: 395797(ENTPD2)
            XTR: 407961(entpd2)
            DME: Dmel_CG1014(robl62A) Dmel_CG10181(Mdr65) Dmel_CG10210(tst)
                 Dmel_CG10279(Rm62) Dmel_CG10595(d) Dmel_CG10838(robl22E)
                 Dmel_CG11680(mle) Dmel_CG12759(Dbp45A) Dmel_CG15171(robl37BC)
                 Dmel_CG15804(Dhc62B) Dmel_CG1618(comt) Dmel_CG1666(Hlc)
                 Dmel_CG16954(Hsp60D) Dmel_CG17046(klar) Dmel_CG17632(bw)
                 Dmel_CG1842(Dhc98D) Dmel_CG18801(Ku80) Dmel_CG2173(Rs1)
                 Dmel_CG2184(Mlc2) Dmel_CG2331(TER94) Dmel_CG2412(Rad51C)
                 Dmel_CG2684(lds) Dmel_CG2759(w) Dmel_CG2830(Hsp60B)
                 Dmel_CG2969(Atet) Dmel_CG30170(bgcn) Dmel_CG31045(Mhcl)
                 Dmel_CG31069(spn-D) Dmel_CG31293(rec) Dmel_CG3158(spn-E)
                 Dmel_CG3201(Mlc-c) Dmel_CG3228(kz) Dmel_CG32604(l(1)G0007)
                 Dmel_CG3325(spn-B) Dmel_CG3327(E23) Dmel_CG3506(vas)
                 Dmel_CG3696(kis) Dmel_CG3733(Chd1) Dmel_CG3736(okr)
                 Dmel_CG3753(Marcal1) Dmel_CG3879(Mdr49) Dmel_CG4152(l(2)35Df)
                 Dmel_CG4261(Hel89B) Dmel_CG4314(st) Dmel_CG4548(XNP)
                 Dmel_CG4832(cnn) Dmel_CG4879(RecQ5) Dmel_CG4916(me31B)
                 Dmel_CG5247(Irbp) Dmel_CG5289(Pros26.4) Dmel_CG5395(nmd)
                 Dmel_CG5450(Cdlc2) Dmel_CG5501(Myo95E) Dmel_CG5695(jar)
                 Dmel_CG5772(Sur) Dmel_CG5942(brm) Dmel_CG5977(spas)
                 Dmel_CG6318(Rad51D) Dmel_CG6493(Dcr-2) Dmel_CG6539(Dhh1)
                 Dmel_CG6760(l(3)70Da) Dmel_CG6976(Myo28B1) Dmel_CG7092(Dhc16F)
                 Dmel_CG7235(Hsp60C) Dmel_CG7269(Hel25E) Dmel_CG7347(mus304)
                 Dmel_CG7487(RecQ4) Dmel_CG7595(ck) Dmel_CG7917(Nlp)
                 Dmel_CG7948(spn-A) Dmel_CG7972(mus301) Dmel_CG8019(hay)
                 Dmel_CG8103(Mi-2) Dmel_CG8523(Mdr50) Dmel_CG8571(smid)
                 Dmel_CG8625(Iswi) Dmel_CG8799(l(2)03659) Dmel_CG8937(Hsc70-1)
                 Dmel_CG9054(Ddx1) Dmel_CG9433(Xpd) Dmel_CG9594(Chd3)
                 Dmel_CG9680(Dbp73D) Dmel_CG9696(dom) Dmel_CG9748(bel)
            PIC: PICST_15102(RDH54) PICST_30157(ISW2) PICST_30672(MDL2)
                 PICST_31786(PEX6) PICST_32083(VCP1) PICST_33561(DRS2)
                 PICST_33873(MSP1) PICST_39246(ISW1.2) PICST_49179(RAD16)
                 PICST_52887(RPT5) PICST_53653(RAD54) PICST_54293(HSP78)
                 PICST_57110(FUN30) PICST_59868(MCM5) PICST_67560(DNF3)
                 PICST_71636(MCM3) PICST_71824(RPT6) PICST_75184(MCM4)
                 PICST_83690(SNF2) PICST_83848(PEX1) PICST_85147(DNF1)
                 PICST_85702(STH1) PICST_86369(SAP11) PICST_86905(SEC18)
                 PICST_87921(PRP43) PICST_88824(MOT1) PICST_90641(CHD1)
            CAL: CaO19.3593 CaO19.3761(cdc54) CaO19.4354
                 CaO19_5440(CaO19.5440)
            CGR: CAGL0H09174g CAGL0H09526g
            UMA: UM04188.1 UM04191.1
            PFA: MAL13P1.14 MAL13P1.166 MAL13P1.322 MAL3P7.12 MAL7P1.113
                 PF08_0042 PF08_0048 PF10_0294 PF11_0053 PF13_0037 PF13_0177
                 PF13_0330 PF14_0183 PF14_0185 PF14_0278 PF14_0370 PF14_0563
                 PF14_0655 PFB0445c PFB0860c PFD0245c PFD0565c PFD1060w
                 PFD1070w PFE0205w PFE0215w PFE0430w PFI0480w PFI0860c PFI0910w
                 PFL0100c PFL0560c PFL0580w PFL1310c PFL1525c PFL2010c PFL2440w
                 PFL2475w
            CPV: cgd3_280 cgd8_2770 cgd8_4620
            CHO: Chro.30042 Chro.80099 Chro.80211 Chro.80294 Chro.80323
                 Chro.80533
            TAN: TA06415 TA10885 TA14185
            TPV: TP04_0614
            TET: TTHERM_00372500 TTHERM_00688470
            EHI: 131.t00001 3.t00009 85.t00018
            ECI: UTI89_C1614(dbpA)
            SBO: SBO_0852(hisI)
            PEN: PSEEN2333(XcpR-2) PSEEN2848
            HPA: HPAG1_0365 HPAG1_1147
            FRA: Francci3_2408
            MMQ: MmarC5_1767
            RCI: RCIX1184(pan-1) RCIX2455(pan-2)
STRUCTURES  PDB: 1ATR  1ATS  1BA0  1BA1  1HJO  1HPM  1HQC  1IXR  1IXS  1KAX  
                 1KAY  1KAZ  1NGA  1NGB  1NGC  1NGD  1NGE  1NGF  1NGG  1NGH  
                 1NGI  1NGJ  1WP9  2DB3  3HSC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.3
            ExPASy - ENZYME nomenclature database: 3.6.1.3
            ExplorEnz - The Enzyme Database: 3.6.1.3
            ERGO genome analysis and discovery system: 3.6.1.3
            BRENDA, the Enzyme Database: 3.6.1.3
            CAS: 9000-83-3
///
ENTRY       EC 3.6.1.4        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
COMMENT     Deleted entry: adenosinetriphosphatase (Mg-activated). Now included
            with EC 3.6.1.3 adenosinetriphosphatase (EC 3.6.1.4 created 1961,
            deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.4
            ExPASy - ENZYME nomenclature database: 3.6.1.4
            ExplorEnz - The Enzyme Database: 3.6.1.4
            ERGO genome analysis and discovery system: 3.6.1.4
            BRENDA, the Enzyme Database: 3.6.1.4
///
ENTRY       EC 3.6.1.5                  Enzyme
NAME        apyrase;
            ATP-diphosphatase;
            adenosine diphosphatase;
            ADPase;
            ATP diphosphohydrolase [ambiguous]
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     ATP diphosphohydrolase (phosphate-forming)
REACTION    ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
ALL_REAC    R00085;
            (other) R00086 R00122 R00155 R00159 R00328 R00335 R00514 R00569
            R00719 R00961 R02092 R02095
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     AMP [CPD:C00020];
            phosphate [CPD:C00009]
COFACTOR    Calcium [CPD:C00076]
COMMENT     Requires Ca2+. Also acts on ADP, and on other nucleoside
            triphosphates and diphosphates. Most of the ecto-ATPases occurring
            on the cell surface and hydrolysing extracellular nucleoside
            triphosphates and diphosphates belong to this enzyme family. Either
            Ca2+ or Mg2+ can serve as activating ions.
REFERENCE   1
  AUTHORS   Krishman, P.S.
  TITLE     Apyrase, pyrophosphatase and metaphosphatase of Penicillium
            chrysogenum.
  JOURNAL   Arch. Biochem. Biophys. 37 (1952) 224-234.
  ORGANISM  Penicillium chrysogenum
REFERENCE   2  [PMID:16526078]
  AUTHORS   Granander J, Sott R, Hilmersson G.
  TITLE     Correlation between the 6Li,15N coupling constant and the
            coordination number at lithium.
  JOURNAL   Chemistry. 12 (2006) 4191-7.
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K01510  apyrase
GENES       HSA: 124583(CANT1) 377841(ENTPD8) 953(ENTPD1) 956(ENTPD3)
            MMU: 12495(Entpd1) 215446(Entpd3)
            RNO: 316077(Entpd3) 64519(Entpd1)
            CFA: 485604(ENTPD3) 486810(ENTPD1) 608038(CANT1)
            BTA: 282223(ENTPD1)
            SSC: 397298(CD39)
            XLA: 379060(MGC52693) 444164(MGC80631)
            XTR: 394537(cant1) 448501(entpd1)
            DRE: 406558(cant1) 445151(entpd1)
            SPU: 587808(LOC587808)
            DME: Dmel_CG5276
            SCE: YER005W(YND1)
            AGO: AGOS_ADR006W
            PIC: PICST_75213(YND1)
            CGR: CAGL0H09746g
            AFM: AFUA_5G11010
            PFA: PF14_0297
            TET: TTHERM_00684480 TTHERM_01256510
            LPN: lpg0971
            LPF: lpl1000
            LPP: lpp1033
STRUCTURES  PDB: 1S18  1S1D  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.5
            ExPASy - ENZYME nomenclature database: 3.6.1.5
            ExplorEnz - The Enzyme Database: 3.6.1.5
            ERGO genome analysis and discovery system: 3.6.1.5
            BRENDA, the Enzyme Database: 3.6.1.5
            CAS: 9000-95-7
///
ENTRY       EC 3.6.1.6                  Enzyme
NAME        nucleoside-diphosphatase;
            thiaminpyrophosphatase;
            UDPase;
            inosine diphosphatase;
            adenosine diphosphatase;
            IDPase;
            ADPase;
            adenosinepyrophosphatase;
            guanosine diphosphatase;
            guanosine 5'-diphosphatase;
            inosine 5'-diphosphatase;
            uridine diphosphatase;
            uridine 5'-diphosphatase;
            nucleoside diphosphate phosphatase;
            type B nucleoside diphosphatase;
            GDPase;
            CDPase;
            nucleoside 5'-diphosphatase;
            type L nucleoside diphosphatase;
            NDPase;
            nucleoside diphosphate phosphohydrolase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     nucleoside-diphosphate phosphohydrolase
REACTION    a nucleoside diphosphate + H2O = a nucleotide + phosphate
            [RN:R00329]
ALL_REAC    R00329 > R00155 R00328 R00961
SUBSTRATE   nucleoside diphosphate [CPD:C00454];
            H2O [CPD:C00001]
PRODUCT     nucleotide [CPD:C00215];
            phosphate [CPD:C00009]
COMMENT     Acts on IDP, GDP, UDP and also on D-ribose 5-diphosphate
REFERENCE   1  [PMID:14389272]
  AUTHORS   GIBSON DM, AYENGAR P, SANADI DR.
  TITLE     A phosphatase specific for nucleoside diphosphates.
  JOURNAL   Biochim. Biophys. Acta. 16 (1955) 536-8.
REFERENCE   2
  AUTHORS   Horecker, B.L., Hurwitz, J. and Heppel, L.A.
  TITLE     The synthesis of ribose 5-pyrophosphate and ribose 5-triphosphate.
  JOURNAL   J. Am. Chem. Soc. 79 (1957) 701-702.
  ORGANISM  Azotobacter vinehndii
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K01511  nucleoside-diphosphatase
GENES       HSA: 124583(CANT1) 955(ENTPD6) 957(ENTPD5) 9583(ENTPD4)
            PTR: 453027(ENTPD5)
            MMU: 12499(Entpd5) 67464(Entpd4) 76025(Cant1)
            RNO: 246272(Cant1) 85260(Entpd6)
            CFA: 480384(ENTPD5)
            GGA: 419531(ENTPD4) 423343(ENTPD5)
            XLA: 495422(entpd4)
            XTR: 394537(cant1)
            CEL: K08H10.4(uda-1)
            PFA: PF14_0297
            CHO: Chro.60194
            TBR: Tb927.7.1930
            EHI: 415.t00008 59.t00033
STRUCTURES  PDB: 2H2N  2H2U  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.6
            ExPASy - ENZYME nomenclature database: 3.6.1.6
            ExplorEnz - The Enzyme Database: 3.6.1.6
            ERGO genome analysis and discovery system: 3.6.1.6
            BRENDA, the Enzyme Database: 3.6.1.6
            CAS: 9027-69-4
///
ENTRY       EC 3.6.1.7                  Enzyme
NAME        acylphosphatase;
            acetylphosphatase;
            1,3-diphosphoglycerate phosphatase;
            acetic phosphatase;
            Ho 1-3;
            GP 1-3
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     acylphosphate phosphohydrolase
REACTION    an acylphosphate + H2O = a carboxylate + phosphate [RN:R00539]
ALL_REAC    R00539 > R00317 R01421 R01515
SUBSTRATE   acylphosphate;
            H2O [CPD:C00001]
PRODUCT     carboxylate [CPD:C00060];
            phosphate [CPD:C00009]
REFERENCE   1
  AUTHORS   Raijman, L., Grisolia, S. and Edelhoch, H.
  TITLE     Further purification and properties of brain acyl phosphatase.
  JOURNAL   J. Biol. Chem. 235 (1960) 2340-2342.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:4305161]
  AUTHORS   Ramponi G, Guerritore A, Treves C, Nassi P, Baccari V.
  TITLE     Horse muscle acyl phosphatase: purification and some properties.
  JOURNAL   Arch. Biochem. Biophys. 130 (1969) 362-9.
  ORGANISM  horse
REFERENCE   3  [PMID:4344156]
  AUTHORS   Ramponi G, Nassi P, Cappugi G, Treves C, Manao G.
  TITLE     Purification and some molecular properties of horse liver acyl
            phosphatase.
  JOURNAL   Biochim. Biophys. Acta. 284 (1972) 485-96.
  ORGANISM  horse
REFERENCE   4  [PMID:4313603]
  AUTHORS   Shiokawa H, Noda L.
  TITLE     Isolation and crystallization of acyl phosphatase from rabbit
            muscle.
  JOURNAL   J. Biol. Chem. 245 (1970) 669-73.
  ORGANISM  rabbit
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00620  Pyruvate metabolism
            PATH: map00632  Benzoate degradation via CoA ligation
ORTHOLOGY   KO: K01512  acylphosphatase
GENES       HSA: 97(ACYP1) 98(ACYP2)
            MMU: 66204(Acyp1) 75572(Acyp2)
            CFA: 480390(LOC480390) 609507(LOC609507)
            GGA: 421217(ACYP2) 423361(ACYP1)
            XLA: 446548(acyp1)
            SPU: 587592(LOC587592)
            DME: Dmel_CG14022 Dmel_CG16870(Acyp) Dmel_CG18505(Acyp2)
            OSA: 4340702 4340703
            CME: CMO164C
            TAN: TA16545
            TPV: TP01_1141
            TBR: Tb927.3.2030
            TCR: 504047.34
            LMA: LmjF25.1960
            ECO: b0968(yccX)
            ECJ: JW5131(yccX)
            ECE: Z1320
            ECS: ECs1052
            ECC: c1106
            ECI: UTI89_C1035
            ECP: ECP_0974
            ECV: APECO1_73(yccX)
            STY: STY1110
            STT: t1836
            SPT: SPA1767(yccX)
            SEC: SC1035(yccX)
            STM: STM1083(yccX)
            YPE: YPO1446
            YPK: y2724
            YPM: YP_1337(acyP)
            YPA: YPA_0738
            YPN: YPN_2533
            YPP: YPDSF_1528
            YPS: YPTB1464
            YEN: YE1596
            SFX: S1036
            SSN: SSON_0973
            SBO: SBO_2263
            SDY: SDY_0943
            ECA: ECA1761
            PLU: plu1785
            SGL: SG1038
            PMU: PM0396
            MSU: MS0845(acyP)
            APL: APL_0143
            XCC: XCC0862(acyP)
            XCB: XC_3368
            XCV: XCV0970
            XAC: XAC0939(acyP)
            XOO: XOO3613(acyP)
            XOM: XOO_3415(XOO3415)
            VCH: VC1355
            VCO: VC0395_A0969
            VVU: VV1_2711
            VVY: VV1550
            VPA: VP1627
            VFI: VF1502
            PPR: PBPRA2192
            PAE: PA0954
            PAU: PA14_51920
            SON: SO_2253
            SHE: Shewmr4_1728
            SHM: Shewmr7_1808
            SHN: Shewana3_2291
            CPS: CPS_2248
            SDE: Sde_3123
            MAQ: Maqu_1183
            CBU: CBU_1995
            CBD: COXBU7E912_2095
            LPN: lpg1886
            LPF: lpl1848
            LPP: lpp1853
            MCA: MCA0713
            NOC: Noc_0888
            AEH: Mlg_0522
            HCH: HCH_04535
            CSA: Csal_1839
            AHA: AHA_2230
            RSO: RSc0219(RS00651) RSc3370(RS02645)
            REU: Reut_A3029 Reut_C6189
            REH: H16_A3325(acyP)
            RME: Rmet_3184
            BMA: BMAA1957
            BMV: BMASAVP1_0974(acyP)
            BML: BMA10299_1261
            BMN: BMA10247_A2235(acyP)
            BXE: Bxe_B0023
            BUR: Bcep18194_B0110
            BCN: Bcen_5312
            BCH: Bcen2424_5548
            BAM: Bamb_4872
            BPS: BPSS2164
            BPM: BURPS1710b_A1279
            BPL: BURPS1106A_A2922(acyP)
            BPD: BURPS668_A3047(acyP)
            BTE: BTH_II2240
            BPA: BPP4395
            BBR: BB4981
            RFR: Rfer_1453
            PNA: Pnap_4846
            AZO: azo3205
            DAR: Daro_1185
            TBD: Tbd_0859
            HHE: HH0129
            SUN: SUN_1259
            GSU: GSU0889
            GME: Gmet_2729
            PCA: Pcar_2214
            DVU: DVU1192
            DDE: Dde_2164 Dde_2443
            ADE: Adeh_0694
            MXA: MXAN_5638
            SAT: SYN_02936
            SFU: Sfum_1427
            MLO: mll7735
            SME: SMb20590
            RET: RHE_CH02378(ypch00785)
            RLE: RL2696
            BJA: bsl5265
            BRA: BRADO3251
            BBT: BBta_4900
            RPA: RPA3173
            RPB: RPB_2369
            RPC: RPC_3350
            RPD: RPD_3091
            RPE: RPE_3437
            NWI: Nwi_1735
            NHA: Nham_2164
            GBE: GbCGDNIH1_0585
            RRU: Rru_A2654
            ABA: Acid345_3607
            SUS: Acid_7268
            BSU: BG12947(yflL)
            BLI: BL03100
            BLD: BLi00788(yflL)
            BCL: ABC2132
            BAY: RBAM_007840(yflL)
            BPU: BPUM_0715
            OIH: OB3253
            GKA: GK0411
            SAU: SA1236
            SAV: SAV1404
            SAM: MW1292
            SAR: SAR1416
            SAS: SAS1345
            SAC: SACOL1439
            SAB: SAB1260
            SAO: SAOUHSC_01406
            SEP: SE1087
            SER: SERP0974
            SHA: SH1507
            SSP: SSP1347
            LMO: lmo1381
            LMF: LMOf2365_1400
            LIN: lin1418
            LWE: lwe1397
            LLA: L196178(yfjC)
            LLC: LACR_0622
            LLM: llmg_0568
            SPY: SPy_0352
            SPZ: M5005_Spy_0296
            SPM: spyM18_0405
            SPG: SpyM3_0257
            SPS: SPs1602
            SPH: MGAS10270_Spy0292
            SPI: MGAS10750_Spy0291
            SPJ: MGAS2096_Spy0314
            SPK: MGAS9429_Spy0296
            SPA: M6_Spy0324
            SPB: M28_Spy0287
            SPN: SP_1974
            SPR: spr1789(acyP)
            SAG: SAG1607
            SAN: gbs1656
            SAK: SAK_1622
            SMU: SMU.1725
            STC: str0246(acyP)
            STL: stu0246(acyP)
            SSA: SSA_1791(acyP)
            LPL: lp_1554
            LJO: LJ1628
            LAC: LBA1522(acyP)
            LSA: LSA1381
            LSL: LSL_0525(acyP)
            LDB: Ldb1490
            LBU: LBUL_1386
            LBR: LVIS_1014
            LCA: LSEI_1676
            EFA: EF2401(acyP)
            CAC: CAC2830
            CPE: CPE1973
            CPF: CPF_2228
            CPR: CPR_1940
            TTE: TTE1765(acyP)
            MTA: Moth_1216
            MTU: Rv2922A(acyP)
            MTC: MT2991
            MBO: Mb2947c(acyP)
            MBB: BCG_2944c(acyP)
            MPA: MAP2991c
            MAV: MAV_3779
            MSM: MSMEG_2422
            MVA: Mvan_2174
            MMC: Mmcs_1952
            MJL: Mjls_1932
            CGL: NCgl1987(cgl2066)
            CGB: cg2266
            CEF: CE1973
            CDI: DIP1541
            NFA: nfa41730
            RHA: RHA1_ro06527(acyP)
            SCO: SCO5576(SC7A1.20)
            SMA: SAV2659(acyP)
            TFU: Tfu_0653
            FRA: Francci3_3598
            FAL: FRAAL5798
            SEN: SACE_6072(acyP)
            BLO: BL1294(acyP)
            RXY: Rxyl_0794
            RBA: RB8840
            BBU: BBB01
            BAF: BAPKO_5000
            TDE: TDE0797
            LIL: LA3975(acyP)
            LIC: LIC13178(acyP)
            LBJ: LBJ_0416(acyP)
            LBL: LBL_2661(acyP)
            SYW: SYNW0747
            SYD: Syncc9605_1921
            SYE: Syncc9902_0745
            SYG: sync_0999
            SYR: SynRCC307_0756
            SYX: SynWH7803_1564
            CYB: CYB_0710
            GVI: gsr3993
            ANA: alr0877
            AVA: Ava_4481
            SRU: SRU_2068
            CTE: CT0126
            DET: DET1027
            DEH: cbdb_A998
            DRA: DR_0929
            DGE: Dgeo_0509
            TTH: TTC0199
            TTJ: TTHA0567
            TMA: TM1564
            MAC: MA3367
            MBA: Mbar_A3282
            MMA: MM_2777
            MHU: Mhun_1211
            HMA: rrnAC1167(acyP)
            HWA: HQ1523A(acyP)
            NPH: NP3750A(acyP)
            TAC: Ta0064m
            TVO: TVN0020
            PTO: PTO0237
            PHO: PH0305a
            PAB: PAB7421(acyP)
            PFU: PF0283
            TKO: TK2031
            RCI: RCIX552(acyP)
            APE: APE_1591.1
            SSO: SSO0887
            STO: STS137
            SAI: Saci_1420
            PAI: PAE1232
STRUCTURES  PDB: 1APS  1ULR  1URR  1V3Z  1W2I  1Y9O  2ACY  2BJD  2BJE  2FHM  
                 2GV1  2HLT  2HLU  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.7
            ExPASy - ENZYME nomenclature database: 3.6.1.7
            ExplorEnz - The Enzyme Database: 3.6.1.7
            ERGO genome analysis and discovery system: 3.6.1.7
            BRENDA, the Enzyme Database: 3.6.1.7
            CAS: 9012-34-4
///
ENTRY       EC 3.6.1.8                  Enzyme
NAME        ATP diphosphatase;
            ATPase;
            ATP pyrophosphatase;
            adenosine triphosphate pyrophosphatase;
            ATP diphosphohydrolase [ambiguous]
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     ATP diphosphohydrolase (diphosphate-forming)
REACTION    ATP + H2O = AMP + diphosphate [RN:R00087]
ALL_REAC    R00087;
            (other) R00086 R00287 R00426 R00515 R00662 R00720
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013]
COMMENT     Also acts on ITP, GTP, CTP and UTP.
REFERENCE   1  [PMID:13061448]
  AUTHORS   HEPPEL LA, HILMOE RJ.
  TITLE     Mechanism of enzymatic hydrolysis of adenosinetriphosphate.
  JOURNAL   J. Biol. Chem. 202 (1953) 217-26.
  ORGANISM  Crotalus adamanteus
REFERENCE   2  [PMID:13058963]
  AUTHORS   JOHNSON M, KAYE MA, HEMS R, KREBS HA.
  TITLE     Enzymic hydrolysis of adenosine phosphates by cobra venom.
  JOURNAL   Biochem. J. 54 (1953) 625-9.
  ORGANISM  cobra
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K04765  ATP diphosphatase
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.8
            ExPASy - ENZYME nomenclature database: 3.6.1.8
            ExplorEnz - The Enzyme Database: 3.6.1.8
            ERGO genome analysis and discovery system: 3.6.1.8
            BRENDA, the Enzyme Database: 3.6.1.8
            CAS: 37289-25-1
///
ENTRY       EC 3.6.1.9                  Enzyme
NAME        nucleotide diphosphatase;
            nucleotide pyrophosphatase;
            nucleotide-sugar pyrophosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     dinucleotide nucleotidohydrolase
REACTION    a dinucleotide + H2O = 2 mononucleotides [RN:R00056]
ALL_REAC    R00056 > R00103 R00160 R03004;
            (other) R00287 R00507 R03036
SUBSTRATE   dinucleotide [CPD:C01910];
            H2O [CPD:C00001]
PRODUCT     mononucleotide [CPD:C02171]
COMMENT     Substrates include NAD+, NADP+, FAD, CoA and also ATP and ADP.
REFERENCE   1
  AUTHORS   Jacobson, J.B. and Kaplan, N.O.
  TITLE     A reduced pyridine nucleotide pyrophosphatase.
  JOURNAL   J. Biol. Chem. 226 (1957) 427-437.
  ORGANISM  pigeon
REFERENCE   2
  AUTHORS   Kornberg, A. and Pricer, W.E.
  TITLE     Nucleotide pyrophosphatase.
  JOURNAL   J. Biol. Chem. 182 (1950) 763-778.
REFERENCE   3  [PMID:5862212]
  AUTHORS   Kumar SA, Rao NA, Vaidyanathan CS.
  TITLE     Nucleotidases in plants. I. Partial purification and properties of
            the enzyme hydrolyzing flavine adenine dinucleotide from mung bean
            seedlings (Phaseolus radiatus).
  JOURNAL   Arch. Biochem. Biophys. 111 (1965) 646-52.
  ORGANISM  Phaseolus radiatus
REFERENCE   4
  AUTHORS   Swartz, M.N., Kaplan, N.O. and Lamborg, M.F.
  TITLE     A "heat-activated" diphosphopyridine nucleotide pyrophosphatase from
            Proteus vulgaris.
  JOURNAL   J. Biol. Chem. 232 (1958) 1051-1063.
  ORGANISM  Proteus vulgaris
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00500  Starch and sucrose metabolism
            PATH: map00740  Riboflavin metabolism
            PATH: map00760  Nicotinate and nicotinamide metabolism
            PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K01513  nucleotide pyrophosphatase
GENES       HSA: 5167(ENPP1) 5168(ENPP2) 5169(ENPP3)
            PTR: 463000(ENPP3) 463002(ENPP1) 464353(ENPP2)
            MCC: 705287(ENPP2) 710140(ENPP1) 710232(ENPP3)
            MMU: 18605(Enpp1) 18606(Enpp2) 209558(Enpp3)
            RNO: 54410(Enpp3) 84050(Enpp2) 85496(Enpp1)
            CFA: 482026(ENPP2)
            GGA: 420361(ENPP2) 426929(ENPP1)
            XLA: 380218(enpp2)
            AFM: AFUA_2G14770
            BUR: Bcep18194_B0352
            LPL: lp_2922(npp)
            PTO: PTO1053 PTO1526
STRUCTURES  PDB: 1NQY  1NQZ  2GSN  2GSO  2GSU  2YS0  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.9
            ExPASy - ENZYME nomenclature database: 3.6.1.9
            ExplorEnz - The Enzyme Database: 3.6.1.9
            ERGO genome analysis and discovery system: 3.6.1.9
            BRENDA, the Enzyme Database: 3.6.1.9
            CAS: 9032-64-8
///
ENTRY       EC 3.6.1.10                 Enzyme
NAME        endopolyphosphatase;
            polyphosphate depolymerase;
            metaphosphatase;
            polyphosphatase;
            polymetaphosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     polyphosphate polyphosphohydrolase
REACTION    polyphosphate + n H2O = (n+1) oligophosphate [RN:R00001]
ALL_REAC    R00001
SUBSTRATE   polyphosphate [CPD:C00890];
            H2O [CPD:C00001]
PRODUCT     oligophosphate [CPD:C02174]
COMMENT     The product contains 4 or 5 phosphate residues.
REFERENCE   1
  AUTHORS   Malmgren, H.
  TITLE     Enzymatic behavior of polymetaphosphate. V. Purification and
            specificity of the enzyme.
  JOURNAL   Acta Chem. Scand. 6 (1952) 16-26.
REFERENCE   2
  AUTHORS   Mattenheimer, H.
  TITLE     Die Substratspezifitat "anorganischer" Poly- und Metaphosphatasen.
            I. Optimale Wirkungsbedingungen fur den enzymatischen Abbau von
            Poly- und Metaphosphaten.
  JOURNAL   Hoppe-Seyler's Z. Physiol. Chem. 303 (1956) 107-114.
ORTHOLOGY   KO: K06018  
GENES       SCE: YDR452W(PPN1)
            AGO: AGOS_AER313C
            KLA: KLLA0B01606g
            PIC: PICST_47340(PPN1)
            CGR: CAGL0K06237g
            SPO: SPBC713.07c
            AFM: AFUA_1G11490
            CNE: CNE01080
            UMA: UM00882.1
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.10
            ExPASy - ENZYME nomenclature database: 3.6.1.10
            ExplorEnz - The Enzyme Database: 3.6.1.10
            ERGO genome analysis and discovery system: 3.6.1.10
            BRENDA, the Enzyme Database: 3.6.1.10
            CAS: 9024-86-6
///
ENTRY       EC 3.6.1.11                 Enzyme
NAME        exopolyphosphatase;
            metaphosphatase;
            acid phosphoanhydride phosphohydrolase;
            Gra-Pase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     polyphosphate phosphohydrolase
REACTION    (polyphosphate)n + H2O = (polyphosphate)n-1 + phosphate [RN:R03042]
ALL_REAC    R03042;
            (other) R03409
SUBSTRATE   (polyphosphate)n [CPD:C00890];
            H2O [CPD:C00001]
PRODUCT     (polyphosphate)n-1 [CPD:C00890];
            phosphate [CPD:C00009]
REFERENCE   1
  AUTHORS   Grossman, D. and Lang, K.
  TITLE     Anorganische Poly- und Metaphosphatasen sowie Polyphosphate im
            tierischen Zellkern.
  JOURNAL   Biochem. Z. 336 (1962) 351-370.
REFERENCE   2
  AUTHORS   Krishman, P.S.
  TITLE     Apyrase, pyrophosphatase and metaphosphatase of Penicillium
            chrysogenum.
  JOURNAL   Arch. Biochem. Biophys. 37 (1952) 224-234.
  ORGANISM  Penicillium chrysogenum
REFERENCE   3
  AUTHORS   Malmgren, H.
  TITLE     Enzymatic behavior of polymetaphosphate. V. Purification and
            specificity of the enzyme.
  JOURNAL   Acta Chem. Scand. 6 (1952) 16-26.
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01514  exopolyphosphatase
GENES       HSA: 58497(PRUNE)
            MMU: 229589(Prune)
            RNO: 310664(MGC93997)
            CFA: 483189(PRUNE)
            SCE: YHR201C(PPX1)
            AGO: AGOS_ABL083W
            PIC: PICST_78524(PPX1)
            CGR: CAGL0L08602g
            SPO: SPAC2F3.11
            ANI: AN3779.2
            AFM: AFUA_5G03410 AFUA_6G08350
            AOR: AO090102000550
            CNE: CNI01960
            PFA: PF14_0022
            TET: TTHERM_00500880
            TBR: Tb09.160.1950
            TCR: 504797.10 511577.110
            LMA: LmjF01.0310
            ECO: b2502(ppx) b2744(surE) b3779(gpp)
            ECJ: JW2487(ppx) JW2714(surE)
            ECE: Z3765(ppx) Z4052(surE)
            ECS: ECs3364 ECs3598
            ECC: c3020(ppx) c3311(surE)
            ECI: UTI89_C2818(ppx)
            ECP: ECP_2504
            ECV: APECO1_3779(surE) APECO1_4067(ppx)
            ECW: EcE24377A_2785(ppx) EcE24377A_3045(surE)
            ECX: EcHS_A2637 EcHS_A2688(hcaT) EcHS_A2882(surE)
            STY: STY2743(ppx) STY3052(surE)
            STT: t0355(ppx) t2828(surE)
            SPT: SPA0365(ppx) SPA2783(surE)
            SEC: SC2499(ppx) SC2859(surE)
            STM: STM2502(ppx) STM2927(surE)
            YPE: YPO2837(ppx) YPO3358(surE)
            YPK: y0831(surE) y1397(ppx)
            YPM: YP_0329(surE) YP_2704(ppx)
            YPA: YPA_2274
            YPN: YPN_1300
            YPP: YPDSF_2187
            YPS: YPTB0773(surE) YPTB2803(ppx)
            YPI: YpsIP31758_1226(ppx) YpsIP31758_3296(surE)
            SFL: SF2546(ppx) SF2767(surE)
            SFX: S2695(ppx) S2960(surE)
            SFV: SFV_2547(ppx)
            SSN: SSON_2584(ppx) SSON_2892(surE)
            SBO: SBO_2523(ppx) SBO_2776(surE)
            SDY: SDY_2691(ppx) SDY_2943(surE)
            ECA: ECA3165(ppx)
            PLU: plu0716(surE) plu2764(ppx)
            WBR: WGLp307(surE)
            SGL: SG0528 SG1737
            ENT: Ent638_2991
            HDU: HD1378(ppx)
            HSO: HS_0341(ppx)
            PMU: PM1807
            MSU: MS0287(gppA)
            APL: APL_0708(ppx)
            XFA: XF2590
            XFT: PD1967(ppx)
            XCC: XCC0960(ppx)
            XCB: XC_3275
            XCV: XCV1069(ppx)
            XAC: XAC1039(ppx)
            XOO: XOO3669(ppx)
            XOM: XOO_3466(XOO3466)
            VCH: VC0722
            VCO: VC0395_A0256(ppx)
            VVU: VV1_0465
            VVY: VV0726
            VPA: VP0572
            PPR: PBPRA0724 PBPRA0725
            PAE: PA5241(ppx)
            PAU: PA14_69220(ppx)
            PPU: PP_5216(ppx)
            PPF: Pput_4157
            PST: PSPTO_5249(ppx)
            PSB: Psyr_0294
            PSP: PSPPH_0281(ppx)
            PFL: PFL_5983(ppx)
            PFO: Pfl_5463
            PEN: PSEEN5335(ppx)
            PMY: Pmen_3024
            PAR: Psyc_0162
            PCR: Pcryo_0173
            ACI: ACIAD3036(ppx)
            SON: SO_2185(ppx)
            SFR: Sfri_0462
            SBM: Shew185_3131
            SPL: Spea_1190
            SHN: Shewana3_1756
            ILO: IL2009(ppx)
            PIN: Ping_2413
            MAQ: Maqu_0474
            MCA: MCA2123
            FTU: FTT1444c(ppx)
            FTF: FTF1444c(ppx)
            FTW: FTW_0449
            FTL: FTL_0612
            FTH: FTH_0613(ppx)
            FTN: FTN_1414(ppx)
            TCX: Tcr_1892
            NOC: Noc_2394
            HCH: HCH_00283(ppx)
            CSA: Csal_0581
            ABO: ABO_2461
            AHA: AHA_2830
            DNO: DNO_0369
            NME: NMB1467
            NMA: NMA1679(ppx)
            NGO: NGO1041
            CVI: CV_1262(ppx)
            RSO: RSc1537(ppx)
            REH: H16_A2436(ppx)
            RME: Rmet_2177
            BMA: BMA0789(ppx)
            BMV: BMASAVP1_A1301(ppx)
            BML: BMA10299_A0569(ppx)
            BMN: BMA10247_0583(ppx)
            BXE: Bxe_A1274
            BCN: Bcen_0827
            BCH: Bcen2424_1308
            BAM: Bamb_1185
            BPS: BPSL1367
            BPM: BURPS1710b_1627
            BTE: BTH_I2765
            PNU: Pnuc_1589
            BPE: BP1073(ppx)
            BPA: BPP2071(ppx)
            BBR: BB1464(ppx)
            RFR: Rfer_2032
            POL: Bpro_2249
            PNA: Pnap_2209
            AAV: Aave_2625
            AJS: Ajs_2375
            VEI: Veis_1294
            MPT: Mpe_A3006
            MMS: mma_2303
            NEU: NE1745(ppx)
            NET: Neut_1831
            NMU: Nmul_A0434
            EBA: ebA6525(ppx)
            AZO: azo1690(ppx)
            DAR: Daro_1205
            TBD: Tbd_1046
            MFA: Mfla_0131
            HPY: HP0278(gppA)
            HPJ: jhp0263(gppA)
            HPA: HPAG1_0280
            HHE: HH0984(ppx)
            HAC: Hac_0536(ppx)
            WSU: WS1910
            TDN: Tmden_0661
            CJE: Cj0353c
            CJR: CJE0402
            CJU: C8J_0330
            ABU: Abu_1823(gppA)
            NIS: NIS_0408
            SUN: SUN_1985
            GSU: GSU2559
            GME: Gmet_0880
            PCA: Pcar_1566
            BBA: Bd0061 Bd1014(ppx)
            MXA: MXAN_6322
            RPR: RP294(gppA)
            RTY: RT0285(gppA)
            RCO: RC0392(gppA)
            RFE: RF_0470(gppA)
            RBE: RBE_1019(gppA)
            MLO: mlr8346
            MES: Meso_0471 Meso_1120
            SME: SMc00810
            ATU: Atu0619(ppx)
            ATC: AGR_C_1098
            RET: RHE_CH00788(ppx1) RHE_CH01492(ppx2)
            RLE: RL0842 RL1600(ppx)
            BME: BMEI1204 BMEII0598
            BMF: BAB1_0773 BAB2_0555
            BMS: BRA0685
            BMB: BruAb1_0766 BruAb2_0544
            BJA: blr3969
            BRA: BRADO3150 BRADO3340
            BBT: BBta_3596 BBta_3848
            RPE: RPE_3273 RPE_3280
            NWI: Nwi_1593 Nwi_2151
            BHE: BH01540(ppx)
            SIL: SPO1859
            SIT: TM1040_1183 TM1040_1857
            RSP: RSP_2771
            JAN: Jann_1059 Jann_1980
            RDE: RD1_2041 RD1_3053
            MMR: Mmar10_1170 Mmar10_1251
            HNE: HNE_1801
            ZMO: ZMO0403(ppx)
            NAR: Saro_0473
            SAL: Sala_2753
            ELI: ELI_10275
            GOX: GOX1937 GOX2263
            GBE: GbCGDNIH1_0209 GbCGDNIH1_1145
            RRU: Rru_A0246 Rru_A2160
            MGM: Mmc1_0350
            ABA: Acid345_1033
            SUS: Acid_6686
            BHA: BH1393
            BAN: BA4209
            BAR: GBAA4209
            BAA: BA_4671
            BAT: BAS3904
            BCE: BC3994
            BCA: BCE_4044
            BCZ: BCZK3752(ppx)
            BTK: BT9727_3736(ppx)
            SEP: SE2033
            SER: SERP2046
            SHA: SH0588(gppA)
            SSP: SSP0434
            LPL: lp_0446(ppx1) lp_0841(ppx2) lp_0843(ppx3)
            LSL: LSL_0219(gppA)
            LDB: Ldb0522(ppx)
            LBU: LBUL_0463
            LBR: LVIS_0449 LVIS_0702 LVIS_0704
            LCA: LSEI_2615 LSEI_2617
            OOE: OEOE_1628
            CAC: CAC0621
            CPE: CPE1662
            CPF: CPF_1916
            CPR: CPR_1634
            CKL: CKL_2253(ppx1) CKL_2254(ppx2)
            DSY: DSY1021 DSY1022
            TTE: TTE2442(gppA)
            CGL: NCgl0938(cgl0977)
            CGB: cg1115(ppx2)
            CJK: jk1480(ppx2) jk1908(ppx1)
            RHA: RHA1_ro02065
            FAL: FRAAL0968
            SEN: SACE_1948
            FNU: FN0871
            RBA: RB12081
            LIL: LA2761
            LIC: LIC11257(ppx)
            SYN: sll1546(ppx)
            SYW: SYNW1846(ppx)
            SYC: syc2130_c(ppx)
            SYF: Synpcc7942_1965
            SYD: Syncc9605_0623
            SYG: sync_2143
            SYR: SynRCC307_0687(ppx)
            SYX: SynWH7803_1855(ppx)
            CYA: CYA_2432
            CYB: CYB_1493
            TEL: tll1680(ppx)
            GVI: gll0510(ppx)
            ANA: all3552
            AVA: Ava_3530
            PMA: Pro0456(gppA)
            PMM: PMM0457(ppx)
            PMT: PMT1327(ppx)
            PMN: PMN2A_1789
            PMI: PMT9312_0457
            PMB: A9601_05131(ppx)
            PMC: P9515_05201(ppx)
            PMF: P9303_06591(ppx)
            PMG: P9301_04821(ppx)
            PMH: P9215_05371
            PME: NATL1_05121(ppx)
            BTH: BT_0540
            BFR: BF2646
            BFS: BF2669
            SRU: SRU_1442(ppx)
            CHU: CHU_0316(ppx) CHU_1432
            GFO: GFO_3499(ppx)
            FPS: FP0968(ppx)
            CTE: CT1713
            CCH: Cag_0423 Cag_2019
            CPH: Cpha266_0498
            PLT: Plut_1684
            DRA: DR_A0185
            TTH: TTC0636
            AAE: aq_891(ppx)
            TMA: TM0195
            MAC: MA0083(ppx) MA2351(ppx)
            MBA: Mbar_A1198
            MMA: MM_1376
            MHU: Mhun_2990
            MSI: Msm_1423
            SSO: SSO1193
            STO: ST1544
            SAI: Saci_2018
STRUCTURES  PDB: 1T6C  1T6D  1U6Z  2FLO  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.11
            ExPASy - ENZYME nomenclature database: 3.6.1.11
            ExplorEnz - The Enzyme Database: 3.6.1.11
            ERGO genome analysis and discovery system: 3.6.1.11
            BRENDA, the Enzyme Database: 3.6.1.11
            CAS: 9024-85-5
///
ENTRY       EC 3.6.1.12                 Enzyme
NAME        dCTP diphosphatase;
            deoxycytidine-triphosphatase;
            dCTPase;
            dCTP pyrophosphatase;
            deoxycytidine triphosphatase;
            deoxy-CTPase;
            dCTPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     dCTP nucleotidohydrolase
REACTION    dCTP + H2O = dCMP + diphosphate [RN:R01668]
ALL_REAC    R01668;
            (other) R01667
SUBSTRATE   dCTP [CPD:C00458];
            H2O [CPD:C00001]
PRODUCT     dCMP [CPD:C00239];
            diphosphate [CPD:C00013]
COMMENT     Also hydrolyses dCDP to dCMP and phosphate.
REFERENCE   1
  AUTHORS   Zimmerman, S.B. and Kornberg, A.
  TITLE     Deoxycytidine di- and triphosphate cleavage by an enzyme formed in
            bacteriophage-infected Escherichia coli.
  JOURNAL   J. Biol. Chem. 236 (1961) 1480-1486.
  ORGANISM  bacteriophage T2, bacteriophage T4, bacteriophage T6
PATHWAY     PATH: map00240  Pyrimidine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.12
            ExPASy - ENZYME nomenclature database: 3.6.1.12
            ExplorEnz - The Enzyme Database: 3.6.1.12
            ERGO genome analysis and discovery system: 3.6.1.12
            BRENDA, the Enzyme Database: 3.6.1.12
            CAS: 9024-87-7
///
ENTRY       EC 3.6.1.13                 Enzyme
NAME        ADP-ribose diphosphatase;
            ADPribose pyrophosphatase;
            adenosine diphosphoribose pyrophosphatase;
            ADPR-PPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     ADP-ribose ribophosphohydrolase
REACTION    ADP-ribose + H2O = AMP + D-ribose 5-phosphate [RN:R01054]
ALL_REAC    R01054
SUBSTRATE   ADP-ribose [CPD:C00301];
            H2O [CPD:C00001]
PRODUCT     AMP [CPD:C00020];
            D-ribose 5-phosphate [CPD:C00117]
REFERENCE   1  [PMID:14028386]
  AUTHORS   DOHERTY MD, MORRISON JF.
  TITLE     The hydrolysis of adenosine diphosphate ribose by a specific
            phosphohydrolase of rabbit-muscle extracts.
  JOURNAL   Biochim. Biophys. Acta. 65 (1962) 364-6.
  ORGANISM  rabbit
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01515  ADP-ribose pyrophosphatase
GENES       HSA: 11164(NUDT5) 53343(NUDT9)
            PTR: 471246(NUDT9)
            MMU: 53893(Nudt5) 74167(Nudt9)
            RNO: 305149(Nudt9)
            CFA: 478006(NUDT5) 478469(NUDT9)
            GGA: 422587(NUDT9)
            XLA: 432263(MGC83500)
            SPU: 756760(LOC756760)
            CEL: W02G9.1(ndx-2)
            SCE: YBR111C(YSA1)
            AGO: AGOS_ADL342W
            CGR: CAGL0K07744g
            SPO: SPBP35G2.12
            ANI: AN7711.2
            AFM: AFUA_5G08240
            AOR: AO090138000061 AO090701000748
            CNE: CNC05950
            UMA: UM01764.1
            DDI: DDBDRAFT_0204862
            TAN: TA10150
            TET: TTHERM_00113100 TTHERM_00371000
            TBR: Tb11.01.1570
            EHI: 185.t00005
            ECO: b3034(yqiE)
            ECJ: JW3002(nudF)
            ECE: Z4391(yqiE)
            ECS: ECs3922
            ECC: c3780(yqiE)
            ECI: UTI89_C3468(yqiE)
            ECP: ECP_3126
            ECV: APECO1_3379(nudF)
            STY: STY3363
            STT: t3106
            SPT: SPA3054(yqiE)
            SEC: SC3129(yqiE)
            STM: STM3185(yqiE)
            YPE: YPO0664
            YPK: y3515
            YPM: YP_2979(mutT7)
            YPA: YPA_3128
            YPN: YPN_0522
            YPP: YPDSF_0446
            YPS: YPTB3399
            SFL: SF3074(yqiE)
            SFX: S3279(yqiE)
            SFV: SFV_3079(yqiE)
            SSN: SSON_3172(yqiE)
            SBO: SBO_2892(yqiE)
            SDY: SDY_3206(yqiE)
            ECA: ECA0331(nudF)
            PLU: plu3953(nudF)
            SGL: SG0267
            ENT: Ent638_3447
            SPE: Spro_4267
            HIN: HI0398
            HIT: NTHI0519(adpP)
            HSO: HS_0580(nudF)
            PMU: PM1020
            MSU: MS1694(mutT)
            APL: APL_1943
            ASU: Asuc_0841
            XFA: XF2008
            XFT: PD0804
            XCC: XCC0838
            XCB: XC_3392
            XCV: XCV0947
            XAC: XAC0911
            XOO: XOO3639
            XOM: XOO_3439(XOO3439)
            VCH: VC2435
            VVU: VV1_0610
            VVY: VV0584
            VPA: VP0426
            VFI: VF2232 VF2463
            PPR: PBPRA0451
            PAE: PA4971
            PAU: PA14_65710(aspP)
            PPU: PP_4919
            PST: PSPTO_4973
            PSB: Psyr_0547
            PSP: PSPPH_0539 PSPPH_2562(mutT2)
            PFL: PFL_0541(nudF) PFL_3331(nudF)
            PFO: Pfl_0495
            PEN: PSEEN4973
            ACI: ACIAD0275(aspP)
            SON: SO_3903
            SDN: Sden_3224
            SFR: Sfri_3331
            SAZ: Sama_3047
            SBL: Sbal_3577
            SLO: Shew_0545
            SPC: Sputcn32_0769
            SSE: Ssed_0775
            SHE: Shewmr4_3235
            SHM: Shewmr7_0754
            SHN: Shewana3_0726
            SHW: Sputw3181_3406
            ILO: IL1956
            CPS: CPS_4180(nudF)
            PHA: PSHAa2591(nudF)
            PAT: Patl_0431
            SDE: Sde_0370
            PIN: Ping_3359
            MCA: MCA1477
            TCX: Tcr_1358
            NOC: Noc_2512 Noc_2643
            HCH: HCH_05994
            ABO: ABO_2498(adpP)
            NME: NMB1064
            NMA: NMA1263
            CVI: CV_1787(mutT)
            RSO: RSc2047(RS03612)
            REU: Reut_A0976
            REH: H16_A1404
            RME: Rmet_0942
            BMA: BMA1814
            BXE: Bxe_A3199
            BUR: Bcep18194_A4044 Bcep18194_A5562
            BAM: Bamb_2272
            BPS: BPSL1226
            BPM: BURPS1710b_1451
            BPL: BURPS1106A_0371(nudF) BURPS1106A_A1477(nudF)
            BPD: BURPS668_0357(nudF) BURPS668_A1565(nudF)
            BTE: BTH_I1076
            BPE: BP1194
            BPA: BPP1810
            BBR: BB3297
            RFR: Rfer_1507
            POL: Bpro_3241
            MPT: Mpe_A1418
            HAR: HEAR1811
            MMS: mma_1477
            NEU: NE2470
            NET: Neut_2370
            NMU: Nmul_A2233
            EBA: ebA4849
            AZO: azo1410
            DAR: Daro_0963
            TBD: Tbd_0232
            MFA: Mfla_2046
            GSU: GSU3354
            GME: Gmet_0048
            PCA: Pcar_0414
            DDE: Dde_2287
            LIP: LI0940(yqiE)
            BBA: Bd3179(nudF)
            SAT: SYN_01018 SYN_02090
            RET: RHE_CH01485(ypch00514)
            RLE: RL1593(nudF) RL2595
            BJA: blr2573(nudF)
            RPA: RPA3687
            RPB: RPB_1775
            RPC: RPC_3722
            RPD: RPD_3529
            RPE: RPE_3760
            RDE: RD1_0538
            GOX: GOX0843
            RRU: Rru_A1525
            MAG: amb1307
            MGM: Mmc1_0105
            ABA: Acid345_2011
            BSU: BG11762(nudF)
            BHA: BH1524
            BAN: BA4316
            BAR: GBAA4316
            BAA: BA_4774
            BAT: BAS4004
            BCE: BC4094
            BCA: BCE_4163
            BCZ: BCZK3851(nudF) pE33L466_0258(nudF)
            BTK: BT9727_3837(nudF)
            BLI: BL05253(nudF)
            BLD: BLi02512(nudF)
            BCL: ABC0282 ABC1778(nudF)
            BAY: RBAM_021740
            BPU: BPUM_2090
            OIH: OB1851(nudF)
            GKA: GK2320
            SAU: SA1330
            SAV: SAV1499
            SAM: MW1453
            SAR: SAR1575
            SAS: SAS1439
            SAC: SACOL1542
            SAB: SAB1360c
            SAA: SAUSA300_1449
            SAO: SAOUHSC_01593
            SEP: SE1183
            SER: SERP1062
            SHA: SH1417
            SSP: SSP1253
            LMO: lmo1965
            LMF: LMOf2365_1995
            LIN: lin2079
            LWE: lwe1991
            LLA: L133761(ytfB)
            LLC: LACR_2078
            LLM: llmg_1444(mutX) llmg_2075
            SPY: SPy_0444
            SPZ: M5005_Spy_0363
            SPM: spyM18_0487
            SPG: SpyM3_0313
            SPS: SPs1544
            SPH: MGAS10270_Spy0366
            SPI: MGAS10750_Spy0365
            SPJ: MGAS2096_Spy0382
            SPK: MGAS9429_Spy0366
            SPF: SpyM51502
            SPA: M6_Spy0387
            SPB: M28_Spy0352
            SPN: SP_0989
            SPR: spr0892
            SAG: SAG1537
            SAN: gbs1593
            SAK: SAK_1560
            SMU: SMU.1634c
            STC: str0564
            STL: stu0564
            SSA: SSA_1641
            SGO: SGO_1468 SGO_1995
            LPL: lp_1790 lp_2183 lp_2762
            LJO: LJ0981
            LAC: LBA0819
            LSA: LSA0774 LSA1097 LSA1593
            LSL: LSL_0857(nudF)
            LDB: Ldb0750
            LBU: LBUL_0683
            LBR: LVIS_1439
            LCA: LSEI_1286 LSEI_1437
            EFA: EF2696
            STH: STH1825
            CPE: CPE1810
            CNO: NT01CX_2023
            CDF: CD1220(nudF)
            CBO: CBO0474 CBO1867(nudF)
            CKL: CKL_1238
            DSY: DSY2325
            TTE: TTE1310(mutT2)
            MTA: Moth_1504
            RHA: RHA1_ro00930
            FAL: FRAAL5178(nudF)
            SEN: SACE_5243(nudF)
            FNU: FN0874
            RBA: RB12441(nudF) RB6302
            SYN: sll1054 slr1134
            SYW: SYNW0218
            SYC: syc1828_d syc2286_c(mutT)
            SYF: Synpcc7942_1807 Synpcc7942_2271
            SYG: sync_0251
            CYA: CYA_2135
            CYB: CYB_0536
            TEL: tll0423 tll1450
            GVI: gll1085 gll3262 glr4330
            ANA: all3899(mutT) alr2954
            AVA: Ava_0948 Ava_1798 Ava_1823
            PMA: Pro0317
            PMM: PMM0286
            PMT: PMT1885
            PMN: PMN2A_1652
            PMI: PMT9312_0288
            PMB: A9601_03091
            PMC: P9515_03191
            PMF: P9303_25181
            PMG: P9301_03101
            PME: NATL1_03661
            BFR: BF4292
            BFS: BF4099
            SRU: SRU_2115
            DET: DET0456
            DEH: cbdb_A416(mutT)
            DRA: DR_1007
            DGE: Dgeo_1808
            TTH: TTC0160
            TTJ: TTHA0528 TTHA0863
            TMA: TM1181
            MJA: MJ1149(mutT)
            MHU: Mhun_2834
            MSI: Msm_1355
            HMA: rrnAC2153(mutT2)
            HWA: HQ2028A(nudF) HQ3084A(nudF) HQ3163A(nudF) HQ3508A(nudF)
            NPH: NP0392A(nudF_1) NP2056A NP3054A(nudF_2)
            APE: APE_1481.1(nudF) APE_2080.1(nudF)
            HBU: Hbut_0169
            SSO: SSO2167
            STO: ST2154
            SAI: Saci_0013(nudF)
            PAI: PAE0563
STRUCTURES  PDB: 1G0S  1G9Q  1GA7  1KHZ  1MK1  1MP2  1MQE  1MQW  1MR2  1Q33  
                 1QVJ  1V8I  1V8L  1V8M  1V8N  1V8R  1V8S  1V8T  1V8U  1V8V  
                 1V8W  1V8Y  1VIQ  2DSB  2DSC  2DSD  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.13
            ExPASy - ENZYME nomenclature database: 3.6.1.13
            ExplorEnz - The Enzyme Database: 3.6.1.13
            ERGO genome analysis and discovery system: 3.6.1.13
            BRENDA, the Enzyme Database: 3.6.1.13
            CAS: 9024-83-3
///
ENTRY       EC 3.6.1.14                 Enzyme
NAME        adenosine-tetraphosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     adenosine-tetraphosphate phosphohydrolase
REACTION    adenosine 5'-tetraphosphate + H2O = ATP + phosphate [RN:R00128]
ALL_REAC    R00128;
            (other) R00723
SUBSTRATE   adenosine 5'-tetraphosphate [CPD:C03483];
            H2O [CPD:C00001]
PRODUCT     ATP [CPD:C00002];
            phosphate [CPD:C00009]
COMMENT     Also acts on inosine tetraphosphate and tripolyphosphate but shows
            little or no activity with other nucleotides or polyphosphates.
REFERENCE   1  [PMID:4287215]
  AUTHORS   Small GD, Cooper C.
  TITLE     Purification and properties of nucleoside tetraphosphate hydrolase
            from rabbit muscle.
  JOURNAL   Biochemistry. 5 (1966) 14-26.
  ORGANISM  rabbit
PATHWAY     PATH: map00230  Purine metabolism
GENES       CVI: CV_2603
            BML: BMA10299_2064(bsaS)
            BMN: BMA10247_3403(fliI) BMA10247_A0744(bsaS)
            RFE: RF_0029(atpE) RF_1265(atpC) RF_1266(atpD) RF_1267(atpG)
                 RF_1268(atpA)
            RBE: RBE_0097(atpC)
            OTS: OTBS_0578(atpA)
STRUCTURES  PDB: 2V7Q  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.14
            ExPASy - ENZYME nomenclature database: 3.6.1.14
            ExplorEnz - The Enzyme Database: 3.6.1.14
            ERGO genome analysis and discovery system: 3.6.1.14
            BRENDA, the Enzyme Database: 3.6.1.14
            CAS: 37289-26-2
///
ENTRY       EC 3.6.1.15                 Enzyme
NAME        nucleoside-triphosphatase;
            nucleoside triphosphate phosphohydrolase;
            nucleoside-5-triphosphate phosphohydrolase;
            nucleoside 5-triphosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     unspecific diphosphate phosphohydrolase
REACTION    NTP + H2O = NDP + phosphate [RN:R02319]
ALL_REAC    R02319 > R00086;
            (other) R00615
SUBSTRATE   NTP [CPD:C00201];
            H2O [CPD:C00001]
PRODUCT     NDP [CPD:C00454];
            phosphate [CPD:C00009]
COMMENT     Also hydrolyses other nucleoside triphosphates, diphosphates,
            thiamine diphosphate and FAD.
REFERENCE   1  [PMID:5661608]
  AUTHORS   Brightwell R, Tappel AL.
  TITLE     Lysosomal acid pyrophosphatase and acid phosphatase.
  JOURNAL   Arch. Biochem. Biophys. 124 (1968) 333-43.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:14320490]
  AUTHORS   LEWIS M, WEISSMAN S.
  TITLE     PROPERTIES OF A SOLUBLE NUCLEOSIDE TRIPHOSPHATASE ACTIVITY IN
            MAMMALIAN LIVER.
  JOURNAL   Arch. Biochem. Biophys. 109 (1965) 490-8.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:4301913]
  AUTHORS   Matsushita S, Raacke ID.
  TITLE     Purification of nucleoside triphosphatases from pea seedling
            ribosomes.
  JOURNAL   Biochim. Biophys. Acta. 166 (1968) 707-10.
  ORGANISM  Pisum sativum
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00730  Thiamine metabolism
ORTHOLOGY   KO: K01516  nucleoside-triphosphatase
GENES       DME: Dmel_CG10662(sick) Dmel_CG1119(Gnf1) Dmel_CG12149(c12.2)
                 Dmel_CG3059(NTPase) Dmel_CG33101(Nsf2) Dmel_CG33122(cutlet)
                 Dmel_CG5313(RfC3) Dmel_CG6815(bor) Dmel_CG7833(Orc5)
            ATH: AT3G04080(ATAPY1) AT5G18280(ATAPY2)
            PIC: PICST_72696(HAM1)
            CGR: CAGL0F00429g
            UMA: UM02007.1 UM03434.1
            TET: TTHERM_01044780
            LMA: LmjF36.4630
            EHI: 226.t00008
            ECI: UTI89_C3343(yggV)
            YPI: YpsIP31758_0890
            PHA: PSHAa1144(hrpA)
            BUR: Bcep18194_A5464(hrpA)
            CCO: CCC13826_0698
            PCA: Pcar_2029
            BME: BMEI1772
            RSP: RSP_1222(ham1)
            GOX: GOX1281
            SAB: SAB1015
            LSA: LSA0406
            EFA: EF1122(rph)
            PAC: PPA1673
            TFU: Tfu_2364
            SEN: SACE_1213
            FNU: FN1851
            AVA: Ava_2368
            PMB: A9601_03021 A9601_06041
            PMC: P9515_03121 P9515_06121
            PMF: P9303_08051 P9303_25001
            PMG: P9301_03031 P9301_05741
            PME: NATL1_03591 NATL1_06021
            TTH: TTC1290
            MJA: MJ0226
            MMP: MMP0214
            MAC: MA3706
            MBA: Mbar_A0278
            MMA: MM_0603
            MBU: Mbur_1194
            MHU: Mhun_2869
            MTH: MTH1424
            MST: Msp_0011
            MKA: MK1594
            AFU: AF2237
            HAL: VNG2043G(ham1)
            HMA: rrnAC2493(ham1)
            HWA: HQ1343A(ham1)
            NPH: NP4426A(ham1)
            TAC: Ta0325
            TVO: TVN1277
            PTO: PTO0588
            PHO: PH1917
            PAB: PAB1235
            PFU: PF0249
            TKO: TK2111
            APE: APE_1138.1
            HBU: Hbut_0432
            SSO: SSO0432
            STO: ST0365
            SAI: Saci_0849
            PAI: PAE2365
STRUCTURES  PDB: 2I3B  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.15
            ExPASy - ENZYME nomenclature database: 3.6.1.15
            ExplorEnz - The Enzyme Database: 3.6.1.15
            ERGO genome analysis and discovery system: 3.6.1.15
            BRENDA, the Enzyme Database: 3.6.1.15
            CAS: 9075-51-8
///
ENTRY       EC 3.6.1.16                 Enzyme
NAME        CDP-glycerol diphosphatase;
            CDP-glycerol pyrophosphatase;
            cytidine diphosphoglycerol pyrophosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     CDP-glycerol phosphoglycerohydrolase
REACTION    CDP-glycerol + H2O = CMP + sn-glycerol 3-phosphate [RN:R00855]
ALL_REAC    R00855
SUBSTRATE   CDP-glycerol [CPD:C00513];
            H2O [CPD:C00001]
PRODUCT     CMP [CPD:C00055];
            sn-glycerol 3-phosphate [CPD:C00093]
REFERENCE   1  [PMID:14329291]
  AUTHORS   GLASER L.
  TITLE     THE SYNTHESIS OF TEICHOIC ACID. IV. ON THE REGULATION OF CYTIDINE
            5'-DIPHOSPHATEGLYCEROL CONCENTRATION.
  JOURNAL   Biochim. Biophys. Acta. 101 (1965) 6-15.
  ORGANISM  Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K01517  CDPglycerol pyrophosphatase
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.16
            ExPASy - ENZYME nomenclature database: 3.6.1.16
            ExplorEnz - The Enzyme Database: 3.6.1.16
            ERGO genome analysis and discovery system: 3.6.1.16
            BRENDA, the Enzyme Database: 3.6.1.16
            CAS: 37289-28-4
///
ENTRY       EC 3.6.1.17                 Enzyme
NAME        bis(5'-nucleosyl)-tetraphosphatase (asymmetrical);
            bis(5'-guanosyl)-tetraphosphatase;
            bis(5'-adenosyl)-tetraphosphatase;
            diguanosinetetraphosphatase (asymmetrical);
            dinucleosidetetraphosphatase (asymmetrical);
            diadenosine P1,P4-tetraphosphatase;
            dinucleoside tetraphosphatase;
            1-P,4-P-bis(5'-nucleosyl)-tetraphosphate nucleotidohydrolase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     P1,P4-bis(5'-nucleosyl)-tetraphosphate nucleotidohydrolase
REACTION    P1,P4-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP [RN:R01232]
ALL_REAC    R01232;
            (other) R00184 R00969 R02805
SUBSTRATE   P1,P4-bis(5'-guanosyl) tetraphosphate [CPD:C01261];
            H2O [CPD:C00001]
PRODUCT     GTP [CPD:C00044];
            GMP [CPD:C00144]
COMMENT     Also acts on bis(5'-xanthosyl)-tetraphosphate and, more slowly, on
            bis(5'-adenosyl)-tetraphosphate and bis(5'-uridyl)-tetraphosphate
            [cf. EC 3.6.1.41 bis(5'-nucleosyl)-tetraphosphatase (symmetrical)]
REFERENCE   1  [PMID:6309793]
  AUTHORS   Jakubowski H, Guranowski A.
  TITLE     Enzymes hydrolyzing ApppA and/or AppppA in higher plants.
            Purification and some properties of diadenosine triphosphatase,
            diadenosine tetraphosphatase, and phosphodiesterase from yellow
            lupin (Lupinus luteus) seeds.
  JOURNAL   J. Biol. Chem. 258 (1983) 9982-9.
  ORGANISM  Lupinus luteus
REFERENCE   2  [PMID:181087]
  AUTHORS   Vallejo CG, Lobaton CD, Quintanilla M, Sillero A, Sillero MA.
  TITLE     Dinucleosidasetetraphosphatase in rat liver and Artemia salina.
  JOURNAL   Biochim. Biophys. Acta. 438 (1976) 304-9.
  ORGANISM  rat [GN:rno], Artemia salina
REFERENCE   3  [PMID:4955726]
  AUTHORS   Warner AH, Finamore FJ.
  TITLE     Isolation, purification, and characterization of P1,P4-diguanosine
            5'-tetraphosphate asymmetrical-pyrophosphohydrolase from brine
            shrimp eggs.
  JOURNAL   Biochemistry. 4 (1965) 1568-75.
  ORGANISM  Artemia salina
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K01518  bis(5'-nucleosidyl)-tetraphosphatase
GENES       HSA: 318(NUDT2)
            MMU: 66401(Nudt2)
            CFA: 474746(NUDT2)
            SSC: 397577(NUDT2)
            GGA: 427399(NUDT2)
            XTR: 448765(nudt2)
            SPU: 756973(LOC756973)
            DME: Dmel_CG31713(Apf)
            PIC: PICST_42119(HNT1) PICST_56209(HNT2)
            SPO: SPCC4G3.02(aph1)
            PFA: PFE1035c
            TAN: TA05075 TA07740
            TPV: TP03_0531 TP04_0303
            ECI: UTI89_C1231(ycfF)
            VFI: VF0456
            NOC: Noc_1415
            REH: H16_A0281 H16_A3406
            AZO: azo1499
            HPA: HPAG1_0725
            RLE: pRL100341
            BME: BMEI0817 BMEI0941
            RDE: RD1_2155
            GBE: GbCGDNIH1_1715
            SPZ: M5005_Spy_0080
            SPH: MGAS10270_Spy0082 MGAS10270_Spy1539(hit)
            SPI: MGAS10750_Spy0087 MGAS10750_Spy1531(hit)
            SPJ: MGAS2096_Spy0083 MGAS2096_Spy1497(hit)
            SPA: M6_Spy0128 M6_Spy1466
            SPB: M28_Spy0078 M28_Spy1461(hit)
            SSA: SSA_1906(hit)
            SGO: SGO_0537
            LSA: LSA0628
            LSL: LSL_0477
            AYW: AYWB_104(hit)
            FNU: FN1873
            CYB: CYB_2747
            PMC: P9515_00761(hit)
            PMF: P9303_03141(hit)
            TTH: TTC1519 TTC1859
            HWA: HQ3207A(hit)
            NPH: NP5090A(hit_2)
            PTO: PTO0464
STRUCTURES  PDB: 1F3Y  1JKN  1KT9  1KTG  1XSA  1XSB  1XSC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.17
            ExPASy - ENZYME nomenclature database: 3.6.1.17
            ExplorEnz - The Enzyme Database: 3.6.1.17
            ERGO genome analysis and discovery system: 3.6.1.17
            BRENDA, the Enzyme Database: 3.6.1.17
            CAS: 37289-29-5
///
ENTRY       EC 3.6.1.18                 Enzyme
NAME        FAD diphosphatase;
            FAD pyrophosphatase;
            riboflavin adenine dinucleotide pyrophosphatase;
            flavin adenine dinucleotide pyrophosphatase;
            riboflavine adenine dinucleotide pyrophosphatase;
            flavine adenine dinucleotide pyrophosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     FAD nucleotidohydrolase
REACTION    FAD + H2O = AMP + FMN [RN:R00160]
ALL_REAC    R00160
SUBSTRATE   FAD [CPD:C00016];
            H2O [CPD:C00001]
PRODUCT     AMP [CPD:C00020];
            FMN [CPD:C00061]
COMMENT     The plant enzyme also hydrolyses NAD+ and NADH; the animal enzyme
            hydrolyses NAD+ and CoA at about half of the rate of hydrolysis of
            FAD. May be identical with EC 3.6.1.9 nucleotide diphosphatase.
REFERENCE   1  [PMID:5810832]
  AUTHORS   Ravindranath SD, Rao NA.
  TITLE     Nucleotidases in plants. 3. Effect of metabolites on the enzyme
            hydrolyzing flavine adenine dinucleotide (FAD) from Phaseolus
            radiatus.
  JOURNAL   Arch. Biochem. Biophys. 133 (1969) 54-9.
  ORGANISM  Phaseolus radiatus
REFERENCE   2  [PMID:2848456]
  AUTHORS   Shin HJ, Mego JL.
  TITLE     A rat liver lysosomal membrane flavin-adenine dinucleotide
            phosphohydrolase: purification and characterization.
  JOURNAL   Arch. Biochem. Biophys. 267 (1988) 95-103.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00740  Riboflavin metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.18
            ExPASy - ENZYME nomenclature database: 3.6.1.18
            ExplorEnz - The Enzyme Database: 3.6.1.18
            ERGO genome analysis and discovery system: 3.6.1.18
            BRENDA, the Enzyme Database: 3.6.1.18
            CAS: 37289-30-8
///
ENTRY       EC 3.6.1.19                 Enzyme
NAME        nucleoside-triphosphate diphosphatase;
            nucleoside-triphosphate pyrophosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     nucleoside-triphosphate diphosphohydrolase
REACTION    a nucleoside triphosphate + H2O = a nucleotide + diphosphate
            [RN:R01532]
ALL_REAC    R01532 > R00426 R00662 R00720 R01855 R02100 R02720 R03531
SUBSTRATE   nucleoside triphosphate [CPD:C00201];
            H2O [CPD:C00001]
PRODUCT     nucleotide [CPD:C00215];
            diphosphate [CPD:C00013]
COMMENT     May be identical with EC 3.6.1.9 nucleotide diphosphatase.
REFERENCE   1  [PMID:4310599]
  AUTHORS   Chern CJ, MacDonald AB, Morris AJ.
  TITLE     Purification and properties of a nucleoside triphosphate
            pyrophosphohydrolase from red cells of the rabbit.
  JOURNAL   J. Biol. Chem. 244 (1969) 5489-95.
  ORGANISM  rabbit
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K01519  nucleoside-triphosphate pyrophosphatase
GENES       HSA: 3704(ITPA)
            MMU: 16434(Itpa)
            TAN: TA17785
            TET: TTHERM_00041460 TTHERM_00624470
            HIP: CGSHiEE_00690(mazG)
            HIQ: CGSHiGG_05550(mazG)
            BUR: Bcep18194_A4104
            HAR: HEAR2125
            RRU: Rru_A3640
STRUCTURES  PDB: 1V7R  2CAR  2E5X  2I5D  2J4E  2Q5Z  2Q73  2Q9L  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.19
            ExPASy - ENZYME nomenclature database: 3.6.1.19
            ExplorEnz - The Enzyme Database: 3.6.1.19
            ERGO genome analysis and discovery system: 3.6.1.19
            BRENDA, the Enzyme Database: 3.6.1.19
            CAS: 9075-54-1
///
ENTRY       EC 3.6.1.20                 Enzyme
NAME        5'-acylphosphoadenosine hydrolase;
            5-phosphoadenosine hydrolase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     5'-acylphosphoadenosine acylhydrolase
REACTION    5'-acylphosphoadenosine + H2O = AMP + a carboxylate [RN:R00542]
ALL_REAC    R00542 > R00322 R01423;
            (other) R01690
SUBSTRATE   5'-acylphosphoadenosine [CPD:C03361];
            H2O [CPD:C00001]
PRODUCT     AMP [CPD:C00020];
            carboxylate [CPD:C00060]
COMMENT     Also acts on inosine and uridine compounds.
REFERENCE   1  [PMID:13651188]
  AUTHORS   KELLERMAN GM.
  TITLE     Isolation and characteristics of the enzyme acyl 5'-nucleotidase.
  JOURNAL   Biochim. Biophys. Acta. 33 (1959) 101-5.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00230  Purine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.20
            ExPASy - ENZYME nomenclature database: 3.6.1.20
            ExplorEnz - The Enzyme Database: 3.6.1.20
            ERGO genome analysis and discovery system: 3.6.1.20
            BRENDA, the Enzyme Database: 3.6.1.20
            CAS: 37289-31-9
///
ENTRY       EC 3.6.1.21                 Enzyme
NAME        ADP-sugar diphosphatase;
            ADP-sugar pyrophosphatase;
            adenosine diphosphosugar pyrophosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     ADP-sugar sugarphosphohydrolase
REACTION    ADP-sugar + H2O = AMP + alpha-D-aldose 1-phosphate [RN:R03570]
ALL_REAC    R03570 > R00951 R01885 R02677;
            (other) R00881 R01233
SUBSTRATE   ADP-sugar [CPD:C01469];
            H2O [CPD:C00001]
PRODUCT     AMP [CPD:C00020];
            alpha-D-aldose 1-phosphate [CPD:C00991]
COMMENT     Has a specificity that is distinct from that of UDP-sugar
            diphosphatase (EC 3.6.1.45).
REFERENCE   1  [PMID:5686292]
  AUTHORS   Rodriguez P, Bass ST, Hansen RG.
  TITLE     A pyrophosphatase from mammalian tissues specific for derivatives of
            ADP.
  JOURNAL   Biochim. Biophys. Acta. 167 (1968) 199-201.
  ORGANISM  cow [GN:bta], rat [GN:rno], rabbit
PATHWAY     PATH: map00051  Fructose and mannose metabolism
            PATH: map00230  Purine metabolism
            PATH: map00500  Starch and sucrose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.21
            ExPASy - ENZYME nomenclature database: 3.6.1.21
            ExplorEnz - The Enzyme Database: 3.6.1.21
            ERGO genome analysis and discovery system: 3.6.1.21
            BRENDA, the Enzyme Database: 3.6.1.21
            CAS: 37289-32-0
///
ENTRY       EC 3.6.1.22                 Enzyme
NAME        NAD+ diphosphatase;
            nicotinamide adenine dinucleotide pyrophosphatase;
            NADP+ pyrophosphatase;
            NADH pyrophosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     NAD+ phosphohydrolase
REACTION    NAD+ + H2O = AMP + NMN [RN:R00103]
ALL_REAC    R00103;
            (other) R03004
SUBSTRATE   NAD+ [CPD:C00003];
            H2O [CPD:C00001]
PRODUCT     AMP [CPD:C00020];
            NMN [CPD:C00455]
COMMENT     Also acts on NADP+, 3-acetylpyridine and the thionicotinamide
            analogues of NAD+ and NADP+.
REFERENCE   1  [PMID:4381708]
  AUTHORS   Anderson BM, Lang CA.
  TITLE     Nicotinamide-adenine dinucleotide pyrophosphatase in the growing and
            aging mosquito.
  JOURNAL   Biochem. J. 101 (1966) 392-6.
REFERENCE   2  [PMID:4405504]
  AUTHORS   Nakajima Y, Fukunaga N, Sasaki S, Usami S.
  TITLE     Purification and properties of NADP pyrophosphatase from Proteus
            vulgaris.
  JOURNAL   Biochim. Biophys. Acta. 293 (1973) 242-55.
  ORGANISM  Proteus vulgaris
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K03426  NAD diphosphatase
GENES       HSA: 83594(NUDT12)
            MMU: 67993(Nudt12)
            CFA: 488881(NUDT12)
            XLA: 495198(LOC495198)
            ECW: EcE24377A_4539(nudC)
            ECX: EcHS_A4230
            SPE: Spro_0286
            ASU: Asuc_1981
            VFI: VF2463
            CBD: COXBU7E912_1094(nudC)
            MMW: Mmwyl1_3794
            AHA: AHA_3612
            CVI: CV_2905
            REH: H16_A2761
            BRA: BRADO0761
            BBT: BBta_7348
            CTC: CTC00069
            MBO: Mb3224c(nudC)
            MBB: BCG_3224c(nudC)
            MAV: MAV_4145
            MSM: MSMEG_1946
            SEN: SACE_1091(nudC)
STRUCTURES  PDB: 2GB5  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.22
            ExPASy - ENZYME nomenclature database: 3.6.1.22
            ExplorEnz - The Enzyme Database: 3.6.1.22
            ERGO genome analysis and discovery system: 3.6.1.22
            BRENDA, the Enzyme Database: 3.6.1.22
            CAS: 37289-33-1
///
ENTRY       EC 3.6.1.23                 Enzyme
NAME        dUTP diphosphatase;
            deoxyuridine-triphosphatase;
            dUTPase;
            dUTP pyrophosphatase;
            desoxyuridine 5'-triphosphate nucleotidohydrolase;
            desoxyuridine 5'-triphosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     dUTP nucleotidohydrolase
REACTION    dUTP + H2O = dUMP + diphosphate [RN:R02100]
ALL_REAC    R02100
SUBSTRATE   dUTP [CPD:C00460];
            H2O [CPD:C00001]
PRODUCT     dUMP [CPD:C00365];
            diphosphate [CPD:C00013]
REFERENCE   1  [PMID:14085395]
  AUTHORS   BERTANI LE, HAEGGMARK A, REICHARD P.
  TITLE     ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES. II. FORMATION AND
            INTERCONVERSION OF DEOXYURIDINE PHOSPHATES.
  JOURNAL   J. Biol. Chem. 238 (1963) 3407-13.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:3025197]
  AUTHORS   Giroir LE, Deutsch WA.
  TITLE     Drosophila deoxyuridine triphosphatase. Purification and
            characterization.
  JOURNAL   J. Biol. Chem. 262 (1987) 130-4.
  ORGANISM  Escherichia coli [GN:eco], Drosophila melunogaster
REFERENCE   3  [PMID:13901467]
  AUTHORS   GREENBERG GR, SOMERVILLE RL.
  TITLE     Deoxyuridylate kinase activity and deoxyuridinetriphosphatase in
            Escherichia coli.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 48 (1962) 247-57.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:5105331]
  AUTHORS   Grindey GR, Nichol CA.
  TITLE     Mammalian deoxyuridine 5'-triphosphate pyrophosphatase.
  JOURNAL   Biochim. Biophys. Acta. 240 (1971) 180-3.
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K01520  dUTP pyrophosphatase
GENES       HSA: 1854(DUT)
            MMU: 110074(Dut)
            RNO: 497778(Dut)
            CFA: 609526(DUT)
            GGA: 769338(DUT)
            SPU: 574856(LOC574856)
            DME: Dmel_CG4584(dUTPase)
            CEL: K07A1.2(dut-1)
            ATH: AT3G46940
            OSA: 4333679
            CME: CMO126C
            SCE: YBR252W(DUT1)
            AGO: AGOS_AGR249C
            PIC: PICST_69362(DUT1)
            CGR: CAGL0L09581g
            SPO: SPAC644.05c
            ANI: AN0271.2
            AFM: AFUA_1G02890 AFUA_7G04990
            AOR: AO090005000780
            CNE: CNM01430
            UMA: UM02908.1
            ECU: ECU06_0430
            DDI: DDB_0230111
            PFA: PF11_0282
            CPV: cgd7_5170
            CHO: Chro.70577
            TAN: TA20975
            TPV: TP01_0381
            TET: TTHERM_00248320
            TBR: Tb927.7.5160
            TCR: 508175.160 509151.130
            LMA: LmjF06.0560
            EHI: 187.t00011 194.t00025 363.t00004 375.t00005
            ECO: b3640(dut)
            ECJ: JW3615(dut)
            ECE: Z5064(dut)
            ECS: ECs4515
            ECC: c4464(dut)
            ECI: UTI89_C4184(dut)
            ECP: ECP_3738
            ECV: APECO1_2821(dut)
            ECW: EcE24377A_4141(dut)
            ECX: EcHS_A3849
            STY: STY4063(dut)
            STT: t3787(dut)
            SPT: SPA3583(dut)
            SEC: SC3654(dut)
            STM: STM3731(dut)
            YPE: YPO0047(dut)
            YPK: y0094(dut)
            YPM: YP_0048(dut)
            YPA: YPA_3495
            YPN: YPN_3803
            YPP: YPDSF_3858
            YPS: YPTB0044(dut)
            YPI: YpsIP31758_0059(dut)
            YEN: YE0061(dnaS)
            SFL: SF3679(dut)
            SFX: S4089(dut)
            SFV: SFV_3890(dut)
            SSN: SSON_3766(dut)
            SBO: SBO_3642(dut)
            SDY: SDY_4070(dut)
            ECA: ECA0143(dut)
            PLU: plu4867(dut)
            BUC: BU560(dut)
            BAS: BUsg540(dut)
            BAB: bbp507(dut)
            BCC: BCc_367(dut)
            WBR: WGLp401(dut)
            SGL: SG2210
            ENT: Ent638_0099
            SPE: Spro_4844
            BFL: Bfl613(dut)
            BPN: BPEN_638(dut)
            HIN: HI0954(dut)
            HIT: NTHI1127(dut)
            HIP: CGSHiEE_07190(dut)
            HIQ: CGSHiGG_08345(dut)
            HDU: HD0734(dut)
            HSO: HS_0142(dut)
            PMU: PM1154(dut)
            MSU: MS1937(dut)
            APL: APL_1968(dut)
            ASU: Asuc_0011
            XFA: XF0150
            XFT: PD0119(dnaS)
            XCC: XCC3858(dut)
            XCB: XC_3942
            XCV: XCV4026(dut)
            XAC: XAC3913(dut)
            XOO: XOO0497(dut)
            XOM: XOO_0464(XOO0464)
            PAE: PA5321(dut)
            PAU: PA14_70260(dut)
            PPU: PP_5286(dut)
            PPF: Pput_5196
            PST: PSPTO_0084(dut)
            PSB: Psyr_0220
            PSP: PSPPH_0208(dut)
            PFL: PFL_6053(dut)
            PFO: Pfl_5541
            PEN: PSEEN5433(dut)
            PMY: Pmen_4378
            PAR: Psyc_0581(dut)
            PCR: Pcryo_0570
            PRW: PsycPRwf_1826
            ACI: ACIAD0901(dut)
            SON: SO_4250(dut)
            SDN: Sden_0324
            SFR: Sfri_3830
            SAZ: Sama_0325
            SBL: Sbal_0375
            SBM: Shew185_0374
            SLO: Shew_3483
            SPC: Sputcn32_0460
            SSE: Ssed_0383
            SPL: Spea_3839
            SHE: Shewmr4_3599
            SHM: Shewmr7_0357
            SHN: Shewana3_3772
            SHW: Sputw3181_0336
            ILO: IL0238(dut)
            PIN: Ping_0058
            MAQ: Maqu_3562
            CBU: CBU_0293(dut)
            CBD: COXBU7E912_1788(dut)
            LPN: lpg2487(dut)
            LPF: lpl2407(dut)
            LPP: lpp2551(dut)
            MCA: MCA2783(dut)
            FTU: FTT0319(dut)
            FTF: FTF0319(dut)
            FTW: FTW_1763(dut)
            FTL: FTL_0230
            FTH: FTH_0225
            FTA: FTA_0246
            FTN: FTN_0233(dut)
            TCX: Tcr_1906
            NOC: Noc_2993
            AEH: Mlg_2846
            HHA: Hhal_2298
            HCH: HCH_01022(dut)
            CSA: Csal_2982
            ABO: ABO_0212(dut)
            MMW: Mmwyl1_0622
            AHA: AHA_0158
            BCI: BCI_0182(dut)
            NME: NMB0893
            NMA: NMA1112(dut)
            NMC: NMC0833(dut)
            NGO: NGO0459
            CVI: CV_3081(dut)
            RSO: RSc2463(dut)
            REU: Reut_A2749
            REH: H16_A3049(dut)
            RME: Rmet_2889
            BMA: BMA2245(dut)
            BMV: BMASAVP1_A2661(dut)
            BML: BMA10299_A1036(dut)
            BMN: BMA10247_2115(dut)
            BXE: Bxe_A0803
            BVI: Bcep1808_2593
            BUR: Bcep18194_A5847
            BCN: Bcen_1904
            BCH: Bcen2424_2515
            BAM: Bamb_2562
            BPS: BPSL0903(dut)
            BPM: BURPS1710b_1119(dut)
            BPL: BURPS1106A_0968(dut)
            BPD: BURPS668_0964(dut)
            BTE: BTH_I0767
            PNU: Pnuc_1743
            BPE: BP2578(dut)
            BPA: BPP1976(dut)
            BBR: BB2164(dut)
            RFR: Rfer_2646
            POL: Bpro_3178
            PNA: Pnap_1188
            AAV: Aave_1329
            AJS: Ajs_1002
            VEI: Veis_2655
            MPT: Mpe_A2570 Mpe_B0284
            HAR: HEAR0842(dut)
            MMS: mma_0825
            NEU: NE1462(dut)
            NET: Neut_0784
            NMU: Nmul_A2136
            EBA: ebA837(dut)
            AZO: azo1139(dut)
            DAR: Daro_3140
            TBD: Tbd_2586
            MFA: Mfla_0313
            HPY: HP0865
            HPJ: jhp0799(dut)
            HPA: HPAG1_0848
            HHE: HH0153(dut)
            HAC: Hac_1228(dut)
            WSU: WS0800
            NIS: NIS_1015
            SUN: SUN_1566
            GSU: GSU1595(dut)
            GME: Gmet_1593
            GUR: Gura_1908
            PCA: Pcar_1563
            PPD: Ppro_2116
            DVU: DVU2348(dut)
            DVL: Dvul_0913
            DDE: Dde_1425
            LIP: LI0088(dut)
            BBA: Bd1553(dut)
            DPS: DP2607
            ADE: Adeh_1108
            AFW: Anae109_1147
            MXA: MXAN_2076(dut)
            SAT: SYN_01779
            RPR: RP399(dut)
            RTY: RT0387(dut)
            RCO: RC0546(dut)
            RFE: RF_0620(dut)
            RBE: RBE_0332(dut)
            RAK: A1C_02980(dut)
            RBO: A1I_06125(dut)
            RRI: A1G_03095(dut)
            OTS: OTBS_0580(dut)
            WOL: WD0243(dut)
            WBM: Wbm0355
            AMA: AM805(dut)
            APH: APH_0379(dut)
            ERU: Erum5190(dut)
            ERW: ERWE_CDS_05440(dut)
            ERG: ERGA_CDS_05340(dut)
            ECN: Ecaj_0527
            ECH: ECH_0501(dut)
            NSE: NSE_0957(dut)
            PUB: SAR11_0404(dut)
            MLO: mll5345
            MES: Meso_4062
            PLA: Plav_3655
            SME: SMc00461(dnaS)
            SMD: Smed_3554
            ATU: Atu0314(dut)
            ATC: AGR_C_548
            RET: RHE_CH00330(dut)
            RLE: RL0346(dut)
            BME: BMEI0358
            BMF: BAB1_1687(dut)
            BMS: BR1675(dut)
            BMB: BruAb1_1660(dut)
            BOV: BOV_1619(dut)
            OAN: Oant_1262
            BJA: bll0758(dut)
            BRA: BRADO0078(dut)
            BBT: BBta_0084(dut)
            RPA: RPA0080(dut)
            RPB: RPB_0623
            RPC: RPC_0381
            RPD: RPD_0208
            RPE: RPE_0466
            NWI: Nwi_0044
            NHA: Nham_0052
            BHE: BH14690(dut)
            BQU: BQ11670(dut)
            BBK: BARBAKC583_0178
            XAU: Xaut_0077
            CCR: CC_3713
            SIL: SPO0409(dut)
            SIT: TM1040_0461
            RSP: RSP_0598
            RSH: Rsph17029_2251
            RSQ: Rsph17025_4035
            JAN: Jann_0908
            RDE: RD1_1201(dut)
            PDE: Pden_1946
            MMR: Mmar10_3068
            HNE: HNE_3267(dut)
            ZMO: ZMO1191(dut)
            NAR: Saro_0590
            SAL: Sala_3181
            SWI: Swit_4879
            ELI: ELI_10525
            GOX: GOX2497
            GBE: GbCGDNIH1_0156
            ACR: Acry_1726
            RRU: Rru_A2791
            MAG: amb0201
            MGM: Mmc1_3419
            ABA: Acid345_1979
            SUS: Acid_0414
            BSU: BG13437(dut) BG13728(yosS)
            BAN: BA4112(dut)
            BAR: GBAA4112(dut)
            BAA: BA_4583
            BAT: BAS3821
            BCL: ABC2847
            SAV: SAV1974
            SAR: SAR2072
            SAC: SACOL0357(dut)
            SAA: SAUSA300_1949(dut)
            SAO: SAOUHSC_01552 SAOUHSC_02057
            SHA: SH2368
            LMO: lmo1691
            LMF: LMOf2365_1715
            LIN: lin1799
            LWE: lwe1709
            LLA: L181168(dut) L42912(pi335) L48154(pi221) L58858(pi120)
            LLC: LACR_0185 LACR_1122 LACR_1785 LACR_2118
            LLM: llmg_0191(dut) llmg_0816(ps325) llmg_2114(ps428)
            SPY: SPy_0235
            SPZ: M5005_Spy_0199
            SPM: spyM18_0219(dut)
            SPG: SpyM3_0166(dut)
            SPS: SPs0173
            SPH: MGAS10270_Spy0198
            SPI: MGAS10750_Spy0194
            SPJ: MGAS2096_Spy0211 MGAS2096_Spy0212
            SPK: MGAS9429_Spy0200
            SPF: SpyM50178
            SPA: M6_Spy0230
            SPB: M28_Spy0193
            SPN: SP_0021
            SPR: spr0023(dut)
            SPD: SPD_0027(dut)
            SAG: SAG0109(dut)
            SAN: gbs0108
            SAK: SAK_0160(dut)
            SMU: SMU.325
            STC: str1824(dut)
            STL: stu1824(dut)
            STE: STER_1804
            SSA: SSA_2160(dut)
            SSU: SSU05_2035
            SSV: SSU98_2036
            SGO: SGO_0169(dut)
            LPL: lp_0604(dut)
            LJO: LJ0397
            LAC: LBA0345
            LSA: LSA1684(dut)
            LSL: LSL_1251(dut)
            LDB: Ldb1728(dut)
            LBU: LBUL_1602
            LBR: LVIS_0576
            LCA: LSEI_2325
            LGA: LGAS_0335
            PPE: PEPE_1504
            EFA: EF0039
            OOE: OEOE_0316
            LME: LEUM_0156
            STH: STH1533
            CAC: CAC1210(dut) CAC1425
            CPE: CPE0678(dut) CPE1471(dut)
            CPF: CPF_0669(dut) CPF_1722(dut)
            CPR: CPR_0667(dut) CPR_1450(dut)
            CTC: CTC01210
            CNO: NT01CX_0028
            CTH: Cthe_2085
            CDF: CD2403(dut)
            CBA: CLB_1264(dut)
            CBH: CLC_1276(dut)
            CBF: CLI_1320(dut)
            CBE: Cbei_0656
            CKL: CKL_1144(dut)
            AMT: Amet_0869
            CHY: CHY_0300(dut)
            DSY: DSY2505
            DRM: Dred_0491
            SWO: Swol_0911
            CSC: Csac_1964
            TTE: TTE1384(dut)
            MPE: MYPE1000
            MGA: MGA_0994
            POY: PAM164(dut)
            AYW: AYWB_555(dut)
            MTU: Rv2697c(dut)
            MTC: MT2771(dut)
            MBO: Mb2716c(dut)
            MBB: BCG_2710c(dut)
            MLE: ML1028(dut)
            MPA: MAP2814c(dut)
            MAV: MAV_3589
            MSM: MSMEG_2765
            MVA: Mvan_2467
            MGI: Mflv_3933
            MMC: Mmcs_2191
            MKM: Mkms_2237
            MJL: Mjls_2180
            CGL: NCgl1830(cgl1905)
            CGB: cg2086(dut)
            CEF: CE1799
            CDI: DIP1400(dut)
            CJK: jk1082(dut)
            NFA: nfa37530(dut)
            RHA: RHA1_ro06829
            SCO: SCO5868(dut)
            SMA: SAV2399(dut)
            TWH: TWT487(dut)
            TWS: TW277(dut)
            LXX: Lxx10390(dut)
            ART: Arth_1636
            PAC: PPA1054
            NCA: Noca_2908
            TFU: Tfu_1935
            FRA: Francci3_1318
            FAL: FRAAL2080(dut)
            ACE: Acel_1402
            KRA: Krad_1557
            BLO: BL1438(dut)
            BAD: BAD_1003(dut)
            RXY: Rxyl_2622
            FNU: FN1028
            CTR: CT292(dut)
            CTA: CTA_0314(dut)
            CMU: TC0565
            CPN: CPn0059(dut)
            CPA: CP0716
            CPJ: CPj0059(dut)
            CPT: CpB0060
            CCA: CCA00347(dut)
            CAB: CAB338A(dut)
            CFE: CF0659(dut)
            PCU: pc0268(dut)
            TPA: TP0885
            TDE: TDE1042(dut)
            LIL: LA1119
            LIC: LIC12560(dut)
            LBJ: LBJ_2235(dut)
            LBL: LBL_2228(dut)
            GVI: glr1465
            TER: Tery_2083
            BTH: BT_3461
            BFR: BF0324
            BFS: BF0272(dut)
            PGI: PG0953(dut)
            SRU: SRU_1961(dut)
            CHU: CHU_0019(dut)
            GFO: GFO_3262
            FJO: Fjoh_1063
            FPS: FP2450(dut)
            CTE: CT1418(dut)
            CCH: Cag_1595
            CPH: Cpha266_0825
            PVI: Cvib_1236
            PLT: Plut_1418
            DET: DET0415(dut)
            DEH: cbdb_A368(dut)
            AAE: aq_220(dut)
            MJA: MJ1102(dcd)
            MMP: MMP1075(dut)
            MAC: MA0440(dcd)
            MBA: Mbar_A0752
            MMA: MM_1628
            MBU: Mbur_0910
            MTH: MTH1605
            MSI: Msm_0687
            MKA: MK1566(dcd_2)
            AFU: AF1108
            HAL: VNG2570G(dcd)
            HMA: rrnAC2159(dcd3)
            RCI: RCIX1986(dut)
            APE: APE_0069.1
STRUCTURES  PDB: 1DUC  1DUD  1DUN  1DUP  1DUT  1EU5  1EUW  1F7D  1F7K  1F7N  
                 1F7O  1F7P  1F7Q  1F7R  1MQ7  1OGH  1OGK  1OGL  1PKH  1PKJ  
                 1PKK  1RN8  1RNJ  1SEH  1SIX  1SJN  1SLH  1SM8  1SMC  1SNF  
                 1SYL  1VYQ  1W2Y  2BSY  2BT1  2CJE  2D4L  2D4M  2D4N  2HQU  
                 2HR6  2HRM  2OKB  2OKD  2OKE  2OL0  2OL1  2PY4  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.23
            ExPASy - ENZYME nomenclature database: 3.6.1.23
            ExplorEnz - The Enzyme Database: 3.6.1.23
            ERGO genome analysis and discovery system: 3.6.1.23
            BRENDA, the Enzyme Database: 3.6.1.23
            CAS: 37289-34-2
///
ENTRY       EC 3.6.1.24                 Enzyme
NAME        nucleoside phosphoacylhydrolase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     nucleoside-5'-phosphoacylate acylhydrolase
REACTION    Hydrolyses mixed phospho-anhydride bonds
COMMENT     Attacks ribonucleoside 5'-nitrophenylphosphates, but is inactive
            against phosphodiesters.
REFERENCE   1  [PMID:4318904]
  AUTHORS   Spahr PF, Gesteland RF.
  TITLE     Purification and properties of a new enzyme from Escherichia coli:
            nucleoside phosphocyl hydrolase.
  JOURNAL   Eur. J. Biochem. 12 (1970) 270-84.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.24
            ExPASy - ENZYME nomenclature database: 3.6.1.24
            ExplorEnz - The Enzyme Database: 3.6.1.24
            ERGO genome analysis and discovery system: 3.6.1.24
            BRENDA, the Enzyme Database: 3.6.1.24
            CAS: 37289-35-3
///
ENTRY       EC 3.6.1.25                 Enzyme
NAME        triphosphatase;
            inorganic triphosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     triphosphate phosphohydrolase
REACTION    triphosphate + H2O = diphosphate + phosphate [RN:R00138]
ALL_REAC    R00138
SUBSTRATE   triphosphate [CPD:C00536];
            H2O [CPD:C00001]
PRODUCT     diphosphate [CPD:C00013];
            phosphate [CPD:C00009]
REFERENCE   1
  AUTHORS   Kulaev, I.S., Konoshenko, G.I. and Umnov, A.M.
  TITLE     Localization of polyphosphatase hydolyzing polyphosphates to
            orthophosphate in subcellular structures of Neurospora crassa.
  JOURNAL   Biochemistry (Moscow) 37 (1972) 190-194.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2
  AUTHORS   Umnov, A.M., Egorov, S.N., Mansurova, S.E. and Kulaev, I.S.
  TITLE     A comparative characterisation of the polyphosphatases of Neurospora
            crassa and some other organisms.
  JOURNAL   Biochemistry (Moscow) 39 (1974) 309-312.
  ORGANISM  Neurospora crassa [GN:dncr]
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.25
            ExPASy - ENZYME nomenclature database: 3.6.1.25
            ExplorEnz - The Enzyme Database: 3.6.1.25
            ERGO genome analysis and discovery system: 3.6.1.25
            BRENDA, the Enzyme Database: 3.6.1.25
            CAS: 62213-21-2
///
ENTRY       EC 3.6.1.26                 Enzyme
NAME        CDP-diacylglycerol diphosphatase;
            cytidine diphosphodiacylglycerol pyrophosphatase;
            CDP diacylglycerol hydrolase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     CDP-diacylglycerol phosphatidylhydrolase
REACTION    CDP-diacylglycerol + H2O = CMP + phosphatidate [RN:R01797]
ALL_REAC    R01797
SUBSTRATE   CDP-diacylglycerol [CPD:C00269];
            H2O [CPD:C00001]
PRODUCT     CMP [CPD:C00055];
            phosphatidate [CPD:C00416]
REFERENCE   1  [PMID:4335869]
  AUTHORS   Raetz CR, Hirschberg CB, Dowhan W, Wickner WT, Kennedy EP.
  TITLE     A membrane-bound pyrophosphatase in Escherichia coli catalyzing the
            hydrolysis of cytidine diphosphate-diglyceride.
  JOURNAL   J. Biol. Chem. 247 (1972) 2245-7.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K01521  CDP-diacylglycerol pyrophosphatase
GENES       ECO: b3918(cdh)
            ECJ: JW3889(cdh)
            ECE: Z5463(cdh)
            ECS: ECs4843
            ECC: c4870(cdh)
            ECI: UTI89_C4502(cdh)
            ECP: ECP_4127
            ECV: APECO1_2551(cdh)
            ECW: EcE24377A_4452(cdh)
            ECX: EcHS_A4149(cdh) EcHS_A4217(rplA)
            STY: STY3800(cdh) STY3807(cdh)
            STT: t3555(cdh)
            SPT: SPA3907(cdh)
            SEC: SC3955(ushB)
            STM: STM4064(ushB)
            YPE: YPO3986(cdh)
            YPK: y3843(cdh)
            YPM: YP_3349(cdh)
            YPA: YPA_3814
            YPN: YPN_3636
            YPP: YPDSF_3352
            YPS: YPTB3826(cdh)
            SFL: SF3996(cdh)
            SFX: S3751(cdh)
            SFV: SFV_3576(cdh)
            SSN: SSON_4087(cdh)
            SBO: SBO_3935(cdh)
            ECA: ECA1560(cdh)
            ENT: Ent638_4054
            SPE: Spro_4746
            XCC: XCC1694(cdh)
            XCB: XC_2537
            CVI: CV_4315(cdh)
            REU: Reut_B4175
            REH: H16_B2144
            RME: Rmet_5614
            BXE: Bxe_B1010
            HPY: HP0871(cdh)
            HPA: HPAG1_0854
            HAC: Hac_1235(cdh)
            BBA: Bd0518(cdh)
            GOX: GOX1938
            MTU: Rv2289(cdh)
            MTC: MT2346(cdh)
            MBO: Mb2311(cdh)
            MBB: BCG_2305(cdh)
            MLE: ML1417
STRUCTURES  PDB: 2POF  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.26
            ExPASy - ENZYME nomenclature database: 3.6.1.26
            ExplorEnz - The Enzyme Database: 3.6.1.26
            ERGO genome analysis and discovery system: 3.6.1.26
            BRENDA, the Enzyme Database: 3.6.1.26
            CAS: 62213-20-1
///
ENTRY       EC 3.6.1.27                 Enzyme
NAME        undecaprenyl-diphosphatase;
            C55-isoprenyl diphosphatase;
            C55-isoprenyl pyrophosphatase;
            isoprenyl pyrophosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     undecaprenyl-diphosphate phosphohydrolase
REACTION    undecaprenyl diphosphate + H2O = undecaprenyl phosphate + phosphate
            [RN:R05627]
ALL_REAC    R05627
SUBSTRATE   undecaprenyl diphosphate [CPD:C03543];
            H2O [CPD:C00001]
PRODUCT     undecaprenyl phosphate [CPD:C00348];
            phosphate [CPD:C00009]
COMMENT     The undecaprenol involved is ditrans,octacis-undecaprenol (for
            definitions, click here).
REFERENCE   1  [PMID:4341539]
  AUTHORS   Goldman R, Strominger JL.
  TITLE     Purification and properties of C 55 -isoprenylpyrophosphate
            phosphatase from Micrococcus lysodeikticus.
  JOURNAL   J. Biol. Chem. 247 (1972) 5116-22.
  ORGANISM  Micrococcus lysodeikticus
PATHWAY     PATH: map00550  Peptidoglycan biosynthesis
ORTHOLOGY   KO: K06153  undecaprenyl-diphosphatase
GENES       ECO: b3057(bacA)
            ECJ: JW3029(bacA)
            ECE: Z4410(bacA)
            ECS: ECs3940
            ECC: c3807(bacA)
            ECI: UTI89_C3493(bacA)
            ECP: ECP_3147
            ECV: APECO1_3357(uppP)
            ECX: EcHS_A3235(uppP) EcHS_A3490(rpsD)
            STY: STY3384(bacA)
            STT: t3125(bacA)
            SPT: SPA3073(bacA)
            SEC: SC3152(bacA)
            STM: STM3205(bacA)
            YPE: YPO0649(bacA)
            YPK: y3530(bacA)
            YPM: YP_2964(bacA)
            YPA: YPA_3141
            YPN: YPN_0509
            YPS: YPTB3412(bacA)
            YPI: YpsIP31758_0559(uppP)
            SFL: SF3098(bacA)
            SFX: S3303(bacA)
            SFV: SFV_3097(bacA)
            SSN: SSON_3194(bacA)
            SBO: SBO_2913(bacA)
            ECA: ECA3589(bacA)
            PLU: plu3973(bacA)
            BUC: BU062(bacA)
            BAS: BUsg059(bacA)
            BAB: bbp058(bacA)
            WBR: WGLp473(bacA)
            SGL: SG0257
            SPE: Spro_1634 Spro_4294
            BPN: BPEN_063(bacA)
            XFA: XF1841
            XFT: PD1027(bacA)
            XCC: XCC0184(bacA)
            XCB: XC_0193
            XCV: XCV0187(uppP)
            XAC: XAC0203(bacA)
            XOO: XOO4489(bacA)
            XOM: XOO_4229(XOO4229)
            VCH: VC0526
            VVU: VV1_0623
            VVY: VV0570
            VPA: VP0413
            VFI: VF2245
            PPR: PBPRA0438
            PAE: PA1959(bacA)
            PAU: PA14_39190(bacA)
            PPU: PP_2862
            PPF: Pput_2827
            PST: PSPTO_3141
            PSB: Psyr_3008(bacA)
            PSP: PSPPH_2232
            PFL: PFL_3114(uppP)
            PFO: Pfl_2602(bacA)
            PEN: PSEEN2933(uppP)
            PMY: Pmen_2175
            PAR: Psyc_1705(bacA)
            PCR: Pcryo_1983
            PRW: PsycPRwf_0541
            ACI: ACIAD0678 ACIAD0914 ACIAD1642(bacA)
            SON: SO_1293 SO_4274
            SDN: Sden_2826
            SFR: Sfri_2988
            SAZ: Sama_0831
            SBM: Shew185_1196
            SLO: Shew_1004
            SSE: Ssed_1080
            SPL: Spea_0967
            SHE: Shewmr4_2900
            SHM: Shewmr7_2982
            SHN: Shewana3_3079
            SHW: Sputw3181_3052
            ILO: IL1437(bacA)
            CPS: CPS_4342
            PHA: PSHAa2300(uppP) PSHAb0269
            PAT: Patl_1046
            SDE: Sde_2232
            PIN: Ping_0174
            MAQ: Maqu_3641
            MCA: MCA0666
            TCX: Tcr_1816
            NOC: Noc_2835(uppP)
            AEH: Mlg_0821
            HHA: Hhal_0715
            HCH: HCH_01816
            CSA: Csal_0859
            ABO: ABO_1130(bacA)
            MMW: Mmwyl1_1258 Mmwyl1_3328
            AHA: AHA_4108
            BCI: BCI_0621
            RMA: Rmag_0439
            VOK: COSY_0409(bacA)
            NME: NMB0408
            NMA: NMA2077
            NMC: NMC1759
            NGO: NGO1547(bacA)
            CVI: CV_1327(upk) CV_1929
            RSO: RSc0701(bacA)
            REU: Reut_A0757(uppP)
            REH: H16_A2871(bacA)
            RME: Rmet_2705
            BMA: BMA2168
            BMV: BMASAVP1_1747 BMASAVP1_A0742
            BML: BMA10299_A2575
            BXE: Bxe_A0858
            BUR: Bcep18194_A4462(uppP)
            BCN: Bcen_0838
            BCH: Bcen2424_0917 Bcen2424_1319
            BAM: Bamb_1204
            BPS: BPSL1383 BPSL2643
            BPM: BURPS1710b_1713(uppP) BURPS1710b_3120
            BPL: BURPS1106A_1544
            BPD: BURPS668_1513
            BTE: BTH_I2750
            BPE: BP1904(bacA)
            BPA: BPP2279(bacA)
            BBR: BB1731(bacA)
            RFR: Rfer_1829
            POL: Bpro_3344
            PNA: Pnap_1356
            AAV: Aave_2042
            AJS: Ajs_1152
            VEI: Veis_2289
            MPT: Mpe_A1046
            NEU: NE0039(bacA)
            NET: Neut_0195
            NMU: Nmul_A2286
            EBA: ebA1726(upk)
            AZO: azo0712(uppP)
            DAR: Daro_3911(bacA)
            TBD: Tbd_2692(bacA)
            MFA: Mfla_2527
            WSU: WS1290(bacA)
            TDN: Tmden_0072
            CJE: Cj0205(bacA)
            CJR: CJE0198
            CJJ: CJJ81176_0237
            CJU: C8J_0194
            CFF: CFF8240_1235
            ABU: Abu_1908(uppP)
            GSU: GSU0387
            GME: Gmet_3133
            GUR: Gura_3622 Gura_4137
            PCA: Pcar_0646
            PPD: Ppro_3583
            DVU: DVU1660
            DVL: Dvul_1427
            DDE: Dde_1946
            LIP: LI0557(bacA)
            BBA: Bd2694(bacA)
            DPS: DP2384
            ADE: Adeh_0157
            AFW: Anae109_0163
            MXA: MXAN_6514
            SAT: SYN_02394
            SFU: Sfum_0725
            PUB: SAR11_0432(bacA)
            MLO: mll4634 mlr0116
            MES: Meso_3600
            PLA: Plav_1120
            SME: SMc00408
            SMD: Smed_3536
            ATU: Atu0294(bacA) Atu0998
            ATC: AGR_C_1833 AGR_C_505
            RET: RHE_CH00310(upk)
            RLE: RL0328
            BME: BMEII0258
            BMF: BAB2_1003
            BMS: BRA1042
            BMB: BruAb2_0982(uppP)
            OAN: Oant_1339
            BJA: blr0716
            BRA: BRADO0129(uppP)
            BBT: BBta_0223(uppP)
            RPA: RPA0044(bacA)
            RPB: RPB_0661
            RPC: RPC_0438
            RPD: RPD_0172
            RPE: RPE_0504
            NWI: Nwi_0165(uppP)
            NHA: Nham_0184
            XAU: Xaut_1807 Xaut_3383
            CCR: CC_3605
            SIL: SPO3771
            SIT: TM1040_2821
            RSP: RSP_1150(uppP)
            RSH: Rsph17029_2811
            RSQ: Rsph17025_2777
            JAN: Jann_0247
            RDE: RD1_0064(uppP)
            PDE: Pden_0491
            MMR: Mmar10_0115
            HNE: HNE_0091
            ZMO: ZMO1115(bacA)
            NAR: Saro_3184
            SAL: Sala_2137
            SWI: Swit_0660
            ELI: ELI_12065
            GOX: GOX0024
            GBE: GbCGDNIH1_0871
            ACR: Acry_0723
            RRU: Rru_A1803
            MAG: amb0523 amb1547
            MGM: Mmc1_2096
            ABA: Acid345_2082
            SUS: Acid_5064
            BSU: BG13951(yubB)
            BHA: BH0464 BH1521
            BAN: BA0283(bacA-1) BA0683 BA1403(bacA-2)
            BAR: GBAA0283(bacA-1) GBAA0683 GBAA1403(bacA-2)
            BAA: BA_0854(bacA) BA_1271(bacA) BA_1925(bacA) BA_3225(bacA)
            BAT: BAS0269 BAS0649 BAS1296 BAS2519
            BCE: BC0677 BC1384 BC2711
            BCA: BCE_0750 BCE_1502(bacA) BCE_2732
            BCZ: BCZK0254(bacA) BCZK0594(bacA) BCZK1270(bacA) BCZK2444(bacA)
            BCY: Bcer98_0572 Bcer98_1110
            BTK: BT9727_0251(bacA) BT9727_0593(bacA) BT9727_1268(bacA)
                 BT9727_2479(bacA)
            BTL: BALH_0274(bacA) BALH_2434
            BLI: BL02576(upk) BL03255(upkA)
            BLD: BLi01213 BLi03290(yubB)
            BCL: ABC1776 ABC3251
            BPU: BPUM_2782(uppP)
            OIH: OB1199
            GKA: GK0218
            SAU: SA0638(bacA)
            SAV: SAV0683(bacA)
            SAM: MW0645(bacA)
            SAR: SAR0736(bacA)
            SAS: SAS0648
            SAC: SACOL0743(bacA)
            SAB: SAB0632c(bacA)
            SAA: SAUSA300_0669
            SAO: SAOUHSC_00691
            SAJ: SaurJH9_0707
            SAH: SaurJH1_0723
            SEP: SE0454
            SER: SERP0339(bacA)
            SHA: SH2210(bacA)
            SSP: SSP2035
            LLA: L58643(bacA)
            LLC: LACR_2504
            LLM: llmg_2476(bacA)
            SPY: SPy_0280(bacA)
            SPZ: M5005_Spy_0238(uppP)
            SPM: spyM18_0268
            SPG: SpyM3_0205(bacA)
            SPS: SPs0211
            SPF: SpyM50217(bacA)
            SPA: M6_Spy0270
            SPB: M28_Spy0233(uppP)
            SPN: SP_0457
            SPR: spr0413(bacA)
            SPD: SPD_0417(bacA)
            SAG: SAG0138
            SAN: gbs0134
            SAK: SAK_0196
            SMU: SMU.244(bacA)
            STC: str0160(bacA)
            STL: stu0160(bacA)
            STE: STER_0215
            SSA: SSA_1959(bacA)
            LPL: lp_3407(bacA)
            LSA: LSA1441(bacA)
            LDB: Ldb0587(upk)
            LBU: LBUL_0523
            LCA: LSEI_0906
            EFA: EF2439
            OOE: OEOE_0848 OEOE_1821
            LME: LEUM_0133
            STH: STH2495
            CAC: CAC0501(bacA) CAC0963(bacA)
            CPE: CPE1186(bacA)
            CPF: CPF_1390
            CPR: CPR_1204
            CTC: CTC00545
            CNO: NT01CX_0158
            CTH: Cthe_2305
            CDF: CD1332(bacA1) CD2986(bacA2)
            CBE: Cbei_0997
            CKL: CKL_2312(uppP) CKL_2698
            AMT: Amet_4339
            CHY: CHY_1158
            DSY: DSY4451
            SWO: Swol_1266
            TTE: TTE0996(bacA)
            MTA: Moth_0571
            MTU: Rv2136c
            MTC: MT2194(bacA)
            MBO: Mb2160c
            MBB: BCG_2153c
            MLE: ML1297
            MPA: MAP1575c
            MAV: MAV_2853
            MUL: MUL_2366
            MVA: Mvan_3483
            MMC: Mmcs_3158
            MKM: Mkms_3220
            MJL: Mjls_3170
            CGL: NCgl1458(uppP)
            CGB: cg1710(bacA)
            CEF: CE1640(bacA)
            CDI: DIP1262(bacA)
            CJK: jk0367(uppP2) jk0957(uppP1)
            NFA: nfa29300
            RHA: RHA1_ro00881
            SCO: SCO1326(2SCG61.08) SCO7047(SC4G1.13)
            SMA: SAV1319(bacA1) SAV7021(bacA2)
            TWH: TWT315
            TWS: TW457(upk)
            ART: Arth_2167
            AAU: AAur_2168
            PAC: PPA2224
            TFU: Tfu_1838(bacA)
            FRA: Francci3_2402(bacA) Francci3_2797
            FAL: FRAAL4312
            ACE: Acel_0766
            KRA: Krad_1818
            SEN: SACE_3590(bacA)
            STP: Strop_2164
            BLO: BL0721(bacA)
            BAD: BAD_0825(bacA)
            RXY: Rxyl_1243
            FNU: FN1702
            RBA: RB7435(bacA)
            PCU: pc0471(bacA)
            BBU: BB0258(bacA)
            BGA: BG0261(bacA)
            BAF: BAPKO_0268(bacA)
            TDE: TDE0172
            LIL: LA2511
            LIC: LIC11457(bacA)
            LBJ: LBJ_1664(bacA)
            LBL: LBL_1883(bacA)
            SYN: sll0210
            SYW: SYNW2189
            SYC: syc2128_c(cacA)
            SYF: Synpcc7942_1967
            SYD: Syncc9605_2332(uppP)
            SYE: Syncc9902_0358(uppP)
            SYG: sync_2543
            SYR: SynRCC307_0306(uppP)
            SYX: SynWH7803_2201(uppP)
            CYA: CYA_0087
            CYB: CYB_2055
            TEL: tlr0737
            GVI: glr3281
            ANA: all1214
            AVA: Ava_0633(uppP)
            PMA: Pro0735(cacA)
            PMM: PMM0956(bacA)
            PMT: PMT0180(bacA)
            PMN: PMN2A_0252(bacA)
            PMI: PMT9312_0843
            PMB: A9601_09041(bacA)
            PMC: P9515_10391(bacA)
            PMF: P9303_02211(bacA)
            PMG: P9301_09021(bacA)
            PMH: P9215_09341(bacA)
            PME: NATL1_09201(bacA)
            TER: Tery_4798
            BTH: BT_3212
            BFR: BF0056
            BFS: BF0068
            PGI: PG1538
            SRU: SRU_0337
            CHU: CHU_0949(bacA)
            GFO: GFO_3037(uppP)
            FJO: Fjoh_0569
            FPS: FP2358(uppP)
            CTE: CT0329
            CCH: Cag_0482(bacA)
            CPH: Cpha266_0665
            PLT: Plut_0444(bacA)
            RRS: RoseRS_3591
            RCA: Rcas_4278
            DRA: DR_0454
            DGE: Dgeo_1051
            TTH: TTC1814
            TTJ: TTHA0172
            AAE: aq_2195(bacA)
            TMA: TM0893
            MMP: MMP1144
            MAE: Maeo_1371
            MBU: Mbur_2081
            MTH: MTH1428 MTH1429
            MST: Msp_0014(uppP)
            MSI: Msm_1201
            MKA: MK1212
            HMA: rrnAC3219(bacA)
            TKO: TK1189
            SSO: SSO1860(uppP)
            STO: ST1813
            MSE: Msed_0425
            PAI: PAE0576
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.27
            ExPASy - ENZYME nomenclature database: 3.6.1.27
            ExplorEnz - The Enzyme Database: 3.6.1.27
            ERGO genome analysis and discovery system: 3.6.1.27
            BRENDA, the Enzyme Database: 3.6.1.27
            CAS: 9077-80-9
///
ENTRY       EC 3.6.1.28                 Enzyme
NAME        thiamine-triphosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     thiamine-triphosphate phosphohydrolase
REACTION    thiamine triphosphate + H2O = thiamine diphosphate + phosphate
            [RN:R00618]
ALL_REAC    R00618
SUBSTRATE   thiamine triphosphate [CPD:C03028];
            H2O [CPD:C00001]
PRODUCT     thiamine diphosphate [CPD:C00068];
            phosphate [CPD:C00009]
REFERENCE   1  [PMID:4335862]
  AUTHORS   Hashitani Y, Cooper JR.
  TITLE     The partial purification of thiamine triphosphatase from rat brain.
  JOURNAL   J. Biol. Chem. 247 (1972) 2117-9.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00730  Thiamine metabolism
ORTHOLOGY   KO: K05307  thiamine-triphosphatase
GENES       HSA: 79178(THTPA)
            MMU: 105663(Thtpa)
            RNO: 305889(Thtpa)
            BTA: 282090(THTPA)
            SPU: 755966(LOC755966)
            CME: CMI051C
STRUCTURES  PDB: 2JMU  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.28
            ExPASy - ENZYME nomenclature database: 3.6.1.28
            ExplorEnz - The Enzyme Database: 3.6.1.28
            ERGO genome analysis and discovery system: 3.6.1.28
            BRENDA, the Enzyme Database: 3.6.1.28
            CAS: 9068-47-7
///
ENTRY       EC 3.6.1.29                 Enzyme
NAME        bis(5'-adenosyl)-triphosphatase;
            dinucleosidetriphosphatase;
            diadenosine 5,5-P1,P3-triphosphatase;
            1-P,3-P-bis(5'-adenosyl)-triphosphate adenylohydrolase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     P1,P3-bis(5'-adenosyl)-triphosphate adenylohydrolase
REACTION    P1,P3-bis(5'-adenosyl) triphosphate + H2O = ADP + AMP [RN:R00187]
ALL_REAC    R00187;
            (other) R00186
SUBSTRATE   P1,P3-bis(5'-adenosyl) triphosphate [CPD:C06197];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            AMP [CPD:C00020]
REFERENCE   1  [PMID:6309793]
  AUTHORS   Jakubowski H, Guranowski A.
  TITLE     Enzymes hydrolyzing ApppA and/or AppppA in higher plants.
            Purification and some properties of diadenosine triphosphatase,
            diadenosine tetraphosphatase, and phosphodiesterase from yellow
            lupin (Lupinus luteus) seeds.
  JOURNAL   J. Biol. Chem. 258 (1983) 9982-9.
  ORGANISM  Lupinus luteus
REFERENCE   2  [PMID:196848]
  AUTHORS   Sillero MA, Villalba R, Moreno A, Quintanilla M, Lobaton CD, Sillero
            A.
  TITLE     Dinucleosidetriphosphatase from rat liver. Purification and
            properties.
  JOURNAL   Eur. J. Biochem. 76 (1977) 331-7.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map05222  Small cell lung cancer
            PATH: map05223  Non-small cell lung cancer
ORTHOLOGY   KO: K01522  bis(5'-adenosyl)-triphosphatase
GENES       HSA: 2272(FHIT)
            MMU: 14198(Fhit)
            RNO: 60398(Fhit)
            GGA: 416071(FHIT)
            XLA: 495983(LOC495983) 496222(LOC496222)
            XTR: 448702(fhit)
            DRE: 393713(fhit)
            ATH: AT5G58240
            CME: CMC141C
            ECU: ECU10_0480
            DDI: DDBDRAFT_0167807
            TET: TTHERM_00378790
            TBR: Tb927.8.2980
            VFI: VF2463
STRUCTURES  PDB: 1FHI  2FHI  4FIT  5FIT  6FIT  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.29
            ExPASy - ENZYME nomenclature database: 3.6.1.29
            ExplorEnz - The Enzyme Database: 3.6.1.29
            ERGO genome analysis and discovery system: 3.6.1.29
            BRENDA, the Enzyme Database: 3.6.1.29
            CAS: 63951-94-0
///
ENTRY       EC 3.6.1.30                 Enzyme
NAME        m7G(5')pppN diphosphatase;
            decapase;
            m7G(5')pppN pyrophosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     7-methylguanosine-5'-triphospho-5'-polynucleotide
            7-methylguanosine-5'-phosphohydrolase
REACTION    7-methylguanosine 5'-triphospho-5'-polynucleotide + H2O =
            7-methylguanosine 5'-phosphate + polynucleotide [RN:R04368]
ALL_REAC    R04368
SUBSTRATE   7-methylguanosine 5'-triphospho-5'-polynucleotide [CPD:C04696];
            H2O [CPD:C00001]
PRODUCT     7-methylguanosine 5'-phosphate [CPD:C03998];
            polynucleotide [CPD:C00419]
REFERENCE   1  [PMID:593271]
  AUTHORS   Lavers GC.
  TITLE     Cleavage of pm7G from mRNA 5' terminal cap structures by
            pyrophosphatase activity in embryonic chick lens cells.
  JOURNAL   Mol. Biol. Rep. 3 (1977) 413-20.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:6122684]
  AUTHORS   Nuss DL, Altschuler RE, Peterson AJ.
  TITLE     Purification and characterization of the m7G(5')pppN-pyrophosphatase
            from human placenta.
  JOURNAL   J. Biol. Chem. 257 (1982) 6224-30.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:16003]
  AUTHORS   Nuss DL, Furuichi Y.
  TITLE     Characterization of the m7G(5')pppN-pyrophosphatase activity from
            HeLa cells.
  JOURNAL   J. Biol. Chem. 252 (1977) 2815-21.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.30
            ExPASy - ENZYME nomenclature database: 3.6.1.30
            ExplorEnz - The Enzyme Database: 3.6.1.30
            ERGO genome analysis and discovery system: 3.6.1.30
            BRENDA, the Enzyme Database: 3.6.1.30
            CAS: 82599-75-5
///
ENTRY       EC 3.6.1.31                 Enzyme
NAME        phosphoribosyl-ATP diphosphatase;
            phosphoribosyl-ATP pyrophosphatase;
            phosphoribosyladenosine triphosphate pyrophosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     1-(5-phosphoribosyl)-ATP diphosphohydrolase
REACTION    1-(5-phosphoribosyl)-ATP + H2O = 1-(5-phosphoribosyl)-AMP +
            diphosphate [RN:R04035]
ALL_REAC    R04035
SUBSTRATE   1-(5-phosphoribosyl)-ATP [CPD:C02739];
            H2O [CPD:C00001]
PRODUCT     1-(5-phosphoribosyl)-AMP [CPD:C02741];
            diphosphate [CPD:C00013]
COFACTOR    H+ [CPD:C00080]
COMMENT     The Neurospora crassa enzyme also catalyses the reactions of EC
            1.1.1.23 (histidinol dehydrogenase) and EC 3.5.4.19
            (phosphoribosyl-AMP cyclohydrolase).
REFERENCE   1
  AUTHORS   Smith, D.W.E. and Ames, B.N.
  TITLE     Phosphoribosyladenosine monophosphate, an intermediate in histidine
            biosynthesis.
  JOURNAL   J. Biol. Chem. 240 (1965) 3056-3063.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00340  Histidine metabolism
ORTHOLOGY   KO: K01523  phosphoribosyl-ATP pyrophosphohydrolase
GENES       ATH: AT1G31860(AT-IE)
            OSA: 4324261
            AGO: AGOS_AFR703W
            PIC: PICST_89228(HIS2)
            ECO: b2026(hisI)
            ECJ: JW2008(hisI)
            ECE: Z3188(hisI)
            ECS: ECs2827
            ECC: c2553(hisI)
            ECI: UTI89_C2299(hisI)
            ECP: ECP_2069
            ECW: EcE24377A_2317(hisIE)
            ECX: EcHS_A2165(hisIE)
            STY: STY2287(hisI)
            STT: t0795(hisI)
            SPT: SPA0793(hisI)
            SEC: SC2088(hisI)
            STM: STM2078(hisI)
            YPE: YPO1542(hisI)
            YPK: y2628(hisI)
            YPM: YP_1431(hisI)
            YPA: YPA_0837
            YPN: YPN_2438
            YPS: YPTB1555(hisI)
            YPI: YpsIP31758_2435(hisI)
            SFL: SF2088(hisIE)
            SFX: S2209(hisI)
            SFV: SFV_2086(hisI)
            SSN: SSON_2097(hisI)
            SDY: SDY_2215(hisI)
            ECA: ECA2589(hisI)
            PLU: plu1564(hisI)
            BUC: BU106(hisI)
            BAS: BUsg099(hisI)
            BAB: bbp100(hisI)
            BCC: BCc_070(hisI)
            SGL: SG1123
            BFL: Bfl469(hisI)
            BPN: BPEN_484(hisI)
            HIT: NTHI0606(hisI)
            PMU: PM1206(hisIE)
            MSU: MS1881(hisI)
            APL: APL_2028(hisI)
            XFA: XF2213
            XFT: PD1261(hisI)
            XCC: XCC1815(hisI)
            XCB: XC_2374
            XCV: XCV1881(hisIE)
            XAC: XAC1835(hisI)
            XOO: XOO2262(hisI)
            XOM: XOO_2123(XOO2123)
            VCH: VC1139
            VCO: VC0395_A0709(hisI)
            VVU: VV1_2913
            VVY: VV1357
            VPA: VP1144
            VFI: VF1019
            PPR: PBPRA1085
            PAE: PA5067(hisE)
            PAU: PA14_66950(hisE)
            PPU: PP_5015(hisE)
            PST: PSPTO_5154(hisE)
            PSB: Psyr_0385
            PSP: PSPPH_0368(hisE)
            PFL: PFL_0423(hisE)
            PFO: Pfl_0383
            PEN: PSEEN5077(hisE)
            PAR: Psyc_1999(hisI)
            ACI: ACIAD0380(hisIE)
            SON: SO_2067(hisI)
            SDN: Sden_1611
            SFR: Sfri_1713
            SHE: Shewmr4_1793
            SHM: Shewmr7_2184
            SHN: Shewana3_1847
            ILO: IL1841(hisI)
            CPS: CPS_3896(hisI)
            PHA: PSHAb0482(hisI)
            PAT: Patl_2888
            LPN: lpg1193(hisI)
            LPF: lpl1201(hisI)
            LPP: lpp1195(hisI)
            MCA: MCA2800(hisE)
            TCX: Tcr_1970
            NOC: Noc_3056
            AEH: Mlg_2613
            HCH: HCH_01078(hisE)
            CSA: Csal_0594
            ABO: ABO_2249(hisE)
            AHA: AHA_2186
            BCI: BCI_0398(hisI)
            VOK: COSY_0274(hisE)
            NME: NMB0603
            NMA: NMA0807(hisE)
            NGO: NGO0185
            CVI: CV_0621(hisE)
            RSO: RSc2944(hisE)
            REU: Reut_A3103
            REH: H16_A3408(hisE)
            RME: Rmet_3240
            BMA: BMA2706(hisE)
            BMV: BMASAVP1_A3247(hisE)
            BML: BMA10299_A1796(hisE)
            BMN: BMA10247_2757(hisE)
            BXE: Bxe_A0406
            BUR: Bcep18194_A3531(hisE)
            BCN: Bcen_2674
            BCH: Bcen2424_0433
            BAM: Bamb_0351
            BPS: BPSL3131(hisE)
            BPM: BURPS1710b_3685(hisE)
            BPL: BURPS1106A_3716(hisE)
            BPD: BURPS668_3658(hisE)
            BTE: BTH_I2985
            BPE: BP3775(hisE)
            BPA: BPP4274(hisE)
            BBR: BB4861(hisE)
            RFR: Rfer_2953
            POL: Bpro_0811
            MPT: Mpe_A0838
            HAR: HEAR3062(hisE)
            MMS: mma_3281(hisE)
            NEU: NE0641(hisE)
            NET: Neut_1911
            NMU: Nmul_A0812
            EBA: ebA1290(hisE)
            AZO: azo3342(hisE)
            DAR: Daro_3377
            TBD: Tbd_1706
            MFA: Mfla_0256
            HHE: HH0449(hisI)
            WSU: WS0090
            TDN: Tmden_1875
            CJE: Cj1604(hisI)
            CJR: CJE1776(hisI)
            CJU: C8J_1505(hisI)
            CCV: CCV52592_0853
            CCO: CCC13826_1896
            ABU: Abu_0121(hisI)
            NIS: NIS_1544(hisI)
            SUN: SUN_0237
            GSU: GSU3094
            GME: Gmet_0390
            PCA: Pcar_2683
            MXA: MXAN_4222(hisIE)
            PUB: SAR11_0328(hisE)
            MLO: mlr5018
            MES: Meso_3498
            SME: SMc02568(hisE)
            ATU: Atu0038(hisE)
            ATC: AGR_C_60
            RET: RHE_CH00041(hisE)
            RLE: RL0041
            BME: BMEI2040
            BMF: BAB1_2087(hisE)
            BMS: BR2086(hisE)
            BMB: BruAb1_2061(hisE)
            BOV: BOV_2006(hisE)
            BJA: blr0655(hisE) blr1323(his2)
            BRA: BRADO0217(hisE) BRADO6579
            BBT: BBta_0141(hisE) BBta_0957
            RPA: RPA0314(hisE) RPA4705(hisE2)
            RPB: RPB_0410 RPB_0869
            RPC: RPC_0311 RPC_0716
            RPD: RPD_0410 RPD_0979
            RPE: RPE_0365 RPE_0754
            NWI: Nwi_0121(hisE)
            NHA: Nham_0127
            CCR: CC_3738
            SIL: SPO1155(hisE)
            SIT: TM1040_2042
            RSP: RSP_2241(hisE)
            JAN: Jann_2796
            RDE: RD1_3562(hisE)
            MMR: Mmar10_1610
            HNE: HNE_0064(hisE)
            ZMO: ZMO1499(hisE)
            SAL: Sala_2380
            ELI: ELI_09550
            GOX: GOX0484
            GBE: GbCGDNIH1_2229
            RRU: Rru_A3593
            MAG: amb4530
            MGM: Mmc1_3158
            BSU: BG12603(hisI)
            BHA: BH3577(hisI)
            BAA: BA_1952
            BAT: BAS1323
            BCE: BC1412(hisE)
            BCA: BCE_1532
            BCZ: BCZK1297(hisE)
            BTK: BT9727_1296(hisE)
            BLI: BL03413(hisI)
            BLD: BLi03731(hisI)
            BCL: ABC3043(hisI)
            BPU: BPUM_3121(hisI)
            OIH: OB0546
            GKA: GK3070
            SAU: SA2464(hisI)
            SAV: SAV2672(hisI)
            SAM: MW2591(hisI)
            SAR: SAR2754(hisIE)
            SAS: SAS2557
            SAC: SACOL2696(hisI)
            SAB: SAB2548c(hisIE)
            SAA: SAUSA300_2605(hisIE)
            SEP: SE0277
            SER: SERP2300(hisIE)
            SSP: SSP0423(hisIE)
            LMO: lmo0561
            LMF: LMOf2365_0590(hisE)
            LIN: lin0570
            LWE: lwe0527(hisE)
            LLA: L0072(hisI)
            LLC: LACR_1326
            SMU: SMU.1261c
            SSA: SSA_1440
            LPL: lp_2552(hisE)
            LCA: LSEI_1427
            STH: STH2832(hisI)
            CAC: CAC0943(his_2)
            CTC: CTC00432
            CDF: CD1554(hisI)
            CBO: CBO1574(hisE)
            CBA: CLB_1594(hisE)
            CKL: CKL_1302(hisE)
            CHY: CHY_1091(hisIE)
            DSY: DSY3907
            SWO: Swol_1764
            TTE: TTE2132(hisI)
            MTU: Rv2122c(hisE)
            MTC: MT2182(hisE)
            MBO: Mb2146c(hisE)
            MBB: BCG_2139c(hisE)
            MLE: ML1309(hisE)
            MPA: MAP1847c(hisI)
            MAV: MAV_2392
            MSM: MSMEG_4181
            MMC: Mmcs_3146
            CGL: NCgl1448(hisE)
            CGB: cg1699(hisE)
            CEF: CE1635(hisE)
            CDI: DIP1257(hisE)
            CJK: jk0953(hisE)
            NFA: nfa31860(hisE)
            RHA: RHA1_ro00855(hisI)
            SCO: SCO1439(hisE)
            SMA: SAV6906(hisE)
            LXX: Lxx11210(hisE)
            CMI: CMM_1771(hisE)
            ART: Arth_1679
            AAU: AAur_1830(hisE)
            PAC: PPA1418(hisE)
            TFU: Tfu_0175
            FAL: FRAAL6591(hisE)
            SEN: SACE_2237(hisE)
            BLO: BL0752(hisE)
            BAD: BAD_0794(hisE)
            RBA: RB11983(hisI) RB5601(hisI)
            LIL: LB079(hisE)
            LIC: LIC20062(hisE)
            LBJ: LBJ_0473
            LBL: LBL_2606
            SYN: slr0608(hisI)
            SYW: SYNW1505(hisIE)
            SYC: syc2101_d(hisIE)
            SYF: Synpcc7942_1995
            SYG: sync_1899(hisIE)
            SYR: SynRCC307_1619(hisIE)
            SYX: SynWH7803_0746(hisIE)
            CYA: CYA_0504(hisIE)
            CYB: CYB_0157(hisIE)
            TEL: tll0233(hisIE)
            GVI: glr1211(hisIE)
            ANA: all3263
            AVA: Ava_4918
            PMA: Pro0582(hisI)
            PMM: PMM0578
            PMT: PMT0453(hisI)
            PMN: PMN2A_0014(hisIE)
            PMI: PMT9312_0578
            PMB: A9601_06341(hisI)
            PMC: P9515_06431(hisI)
            PMF: P9303_18291(hisI)
            PMG: P9301_06041(hisI)
            PMH: P9215_06601(hisI)
            PME: NATL1_06341(hisI)
            TER: Tery_2740
            BTH: BT_1377
            BFR: BF3052
            BFS: BF2888(hisI)
            SRU: SRU_0728
            CHU: CHU_2337(hisI)
            FPS: FP0953(hisIE)
            DRA: DR_0733
            DGE: Dgeo_1901
            TTH: TTC1080
            TTJ: TTHA1445
            AAE: aq_1968(hisIE)
            TMA: TM1035
            MJA: MJ0302(hisE)
            MMP: MMP0051(hisE)
            MAC: MA1392
            MBA: Mbar_A2166
            MMA: MM_2372
            MBU: Mbur_1885
            MTH: MTH1283
            MST: Msp_0267(hisE)
            MSI: Msm_1103
            MKA: MK0500(hisI_1)
            HAL: VNG2596G(hisI)
            HMA: rrnAC2371(hisI1)
            HWA: HQ1300A(hisE)
            NPH: NP0470A(hisE)
            PTO: PTO1331
            PFU: PF1664
            TKO: TK0249
            RCI: RCIX2673(hisE)
            SSO: SSO6223(hisE)
            STO: ST1465
            SAI: Saci_1580
            PAI: PAE0986
STRUCTURES  PDB: 1Y6X  1YVW  1YXB  2A7W  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.31
            ExPASy - ENZYME nomenclature database: 3.6.1.31
            ExplorEnz - The Enzyme Database: 3.6.1.31
            ERGO genome analysis and discovery system: 3.6.1.31
            BRENDA, the Enzyme Database: 3.6.1.31
            CAS: 69553-55-5
///
ENTRY       EC 3.6.1.32       Obsolete  Enzyme
NAME        Transferred to 3.6.4.1
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
COMMENT     Transferred entry: now EC 3.6.4.1 myosin ATPase (EC 3.6.1.32 created
            1984, deleted 2000)
STRUCTURES  PDB: 1BR1  1BR2  1BR4  1I84  1MMA  1MMD  1MMG  1MMN  1MND  1MNE  
                 2BL0  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.32
            ExPASy - ENZYME nomenclature database: 3.6.1.32
            ExplorEnz - The Enzyme Database: 3.6.1.32
            ERGO genome analysis and discovery system: 3.6.1.32
            BRENDA, the Enzyme Database: 3.6.1.32
///
ENTRY       EC 3.6.1.33       Obsolete  Enzyme
NAME        Transferred to 3.6.4.2
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
COMMENT     Transferred entry: now EC 3.6.4.2 dynein ATPase (EC 3.6.1.33 created
            1984, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.33
            ExPASy - ENZYME nomenclature database: 3.6.1.33
            ExplorEnz - The Enzyme Database: 3.6.1.33
            ERGO genome analysis and discovery system: 3.6.1.33
            BRENDA, the Enzyme Database: 3.6.1.33
///
ENTRY       EC 3.6.1.34       Obsolete  Enzyme
NAME        Transferred to 3.6.3.14
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
COMMENT     Transferred entry: now EC 3.6.3.14 H+-transporting two-sector ATPase
            (EC 3.6.1.34 created 1984, deleted 2000)
GENES       TCR: 510889.231
STRUCTURES  PDB: 1A91  1ABV  1AQT  1ATY  1B9U  1BMF  1BSH  1BSN  1C0V  1C99  
                 1COW  1D8S  1DFA  1E1Q  1E1R  1E79  1EF0  1EFR  1FS0  1FX0  
                 1H8E  1H8H  1HO8  1IJP  1JNV  1JVA  1KMH  1MAB  1NBM  1OHH  
                 1QO1  1SKY  1VDE  2CK3  2GZA  2JDI  2JIZ  2JJ1  2JJ2  2QE7  
                 2V7Q  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.34
            ExPASy - ENZYME nomenclature database: 3.6.1.34
            ExplorEnz - The Enzyme Database: 3.6.1.34
            ERGO genome analysis and discovery system: 3.6.1.34
            BRENDA, the Enzyme Database: 3.6.1.34
///
ENTRY       EC 3.6.1.35       Obsolete  Enzyme
NAME        Transferred to 3.6.3.6
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
COMMENT     Transferred entry: now EC 3.6.3.6 H+-exporting ATPase (EC 3.6.1.35
            created 1984, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.35
            ExPASy - ENZYME nomenclature database: 3.6.1.35
            ExplorEnz - The Enzyme Database: 3.6.1.35
            ERGO genome analysis and discovery system: 3.6.1.35
            BRENDA, the Enzyme Database: 3.6.1.35
///
ENTRY       EC 3.6.1.36       Obsolete  Enzyme
NAME        Transferred to 3.6.3.10
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
COMMENT     Transferred entry: now EC 3.6.3.10 H+/K+-exchanging ATPase (EC
            3.6.1.36 created 1984, deleted 2000)
STRUCTURES  PDB: 1AW0  1FVQ  1FVS  2AW0  2IYE  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.36
            ExPASy - ENZYME nomenclature database: 3.6.1.36
            ExplorEnz - The Enzyme Database: 3.6.1.36
            ERGO genome analysis and discovery system: 3.6.1.36
            BRENDA, the Enzyme Database: 3.6.1.36
///
ENTRY       EC 3.6.1.37       Obsolete  Enzyme
NAME        Transferred to 3.6.3.9
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
COMMENT     Transferred entry: now EC 3.6.3.9 Na+/K+-exchanging ATPase (EC
            3.6.1.37 created 1984, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.37
            ExPASy - ENZYME nomenclature database: 3.6.1.37
            ExplorEnz - The Enzyme Database: 3.6.1.37
            ERGO genome analysis and discovery system: 3.6.1.37
            BRENDA, the Enzyme Database: 3.6.1.37
///
ENTRY       EC 3.6.1.38       Obsolete  Enzyme
NAME        Transferred to 3.6.3.8
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
COMMENT     Transferred entry: now EC 3.6.3.8 Ca2+-transporting ATPase (EC
            3.6.1.38 created 1984, deleted 2000)
STRUCTURES  PDB: 1CFF  1IWO  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.38
            ExPASy - ENZYME nomenclature database: 3.6.1.38
            ExplorEnz - The Enzyme Database: 3.6.1.38
            ERGO genome analysis and discovery system: 3.6.1.38
            BRENDA, the Enzyme Database: 3.6.1.38
///
ENTRY       EC 3.6.1.39                 Enzyme
NAME        thymidine-triphosphatase;
            thymidine triphosphate nucleotidohydrolase;
            dTTPase;
            deoxythymidine-5'-triphosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     dTTP nucleotidohydrolase
REACTION    dTTP + H2O = dTDP + phosphate [RN:R02095]
ALL_REAC    R02095;
            (other) R00159 R02330
SUBSTRATE   dTTP [CPD:C00459];
            H2O [CPD:C00001]
PRODUCT     dTDP [CPD:C00363];
            phosphate [CPD:C00009]
COMMENT     Also acts, more slowly, on dUTP and UTP.
REFERENCE   1  [PMID:6297538]
  AUTHORS   Dahlmann N.
  TITLE     Human serum thymidine triphosphate nucleotidohydrolase: purification
            and properties of a new enzyme.
  JOURNAL   Biochemistry. 21 (1982) 6634-9.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00240  Pyrimidine metabolism
GENES       NMC: NMC0546(hisE)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.39
            ExPASy - ENZYME nomenclature database: 3.6.1.39
            ExplorEnz - The Enzyme Database: 3.6.1.39
            ERGO genome analysis and discovery system: 3.6.1.39
            BRENDA, the Enzyme Database: 3.6.1.39
            CAS: 37367-74-1
///
ENTRY       EC 3.6.1.40                 Enzyme
NAME        guanosine-5'-triphosphate,3'-diphosphate diphosphatase;
            pppGpp 5'-phosphohydrolase;
            guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase;
            guanosine 5'-triphosphate-3'-diphosphate 5'-phosphohydrolase;
            guanosine pentaphosphatase;
            guanosine pentaphosphate phosphatase;
            guanosine 5'-triphosphate 3'-diphosphate 5'-phosphatase;
            guanosine pentaphosphate phosphohydrolase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     guanosine-5'-triphosphate,3'-diphosphate 5'-phosphohydrolase
REACTION    guanosine 5'-triphosphate,3'-diphosphate + H2O = guanosine
            5'-diphosphate,3'-diphosphate + phosphate [RN:R03409]
ALL_REAC    R03409
SUBSTRATE   guanosine 5'-triphosphate,3'-diphosphate [CPD:C04494];
            H2O [CPD:C00001]
PRODUCT     guanosine 5'-diphosphate,3'-diphosphate [CPD:C01228];
            phosphate [CPD:C00009]
COMMENT     Also hydrolyses other guanosine 5'-triphosphate derivatives with at
            least one unsubstituted phosphate group on the 3'-position, but not
            GTP, ATP or adenosine 5'-triphosphate,3'-diphosphate.
REFERENCE   1  [PMID:6130093]
  AUTHORS   Hara A, Sy J.
  TITLE     Guanosine 5'-triphosphate, 3'-diphosphate 5'-phosphohydrolase.
            Purification and substrate specificity.
  JOURNAL   J. Biol. Chem. 258 (1983) 1678-83.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01524  guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase
GENES       ECO: b3779(gpp)
            ECE: Z5289(gppA)
            ECS: ECs4712
            ECC: c4699(gppA)
            ECI: UTI89_C4333(gppA)
            ECV: APECO1_2694(gppA)
            ECW: EcE24377A_4289(gppA)
            ECX: EcHS_A3995(gppA)
            STY: STY3641(gppA)
            STT: t3383(gppA)
            SPT: SPA3754(gppA)
            SEC: SC3819(gppA)
            STM: STM3913(gppA)
            YPM: YP_3175(gppA)
            YPA: YPA_0147
            YPN: YPN_0092
            YPP: YPDSF_3488
            YPS: YPTB0164
            YPI: YpsIP31758_0177(gppA)
            YEN: YE0165(gppA)
            SFL: SF3852(gppA)
            SFX: S3907(gppA)
            SFV: SFV_3725(gppA)
            SSN: SSON_3950(gppA)
            SBO: SBO_3789(gppA)
            SDY: SDY_3970(gppA)
            ECA: ECA4214(gppA)
            PLU: plu4666(gppA)
            SGL: SG2389
            ENT: Ent638_4006
            SPE: Spro_0157 Spro_3542
            ASU: Asuc_0365
            VCH: VC0304
            VCO: VC0395_A2696(gppA)
            VVU: VV1_0940
            VVY: VV3184
            VPA: VP3003
            VFI: VF0054
            PPR: PBPRA3543
            PPF: Pput_5125
            PMY: Pmen_0301
            PRW: PsycPRwf_0331
            SON: SO_0408(gppA)
            SDN: Sden_0450
            SAZ: Sama_2012 Sama_3214
            SBL: Sbal_1833 Sbal_3927
            SBM: Shew185_1820 Shew185_3950
            SLO: Shew_0340 Shew_3078
            SPC: Sputcn32_1732 Sputcn32_3431
            SSE: Ssed_4108
            SPL: Spea_0400
            SHE: Shewmr4_0412 Shewmr4_2208
            SHM: Shewmr7_2285 Shewmr7_3613
            SHN: Shewana3_0411
            SHW: Sputw3181_0508 Sputw3181_2293
            CPS: CPS_0173
            PHA: PSHAa0115(gppA)
            PAT: Patl_3323 Patl_4220
            SDE: Sde_1861
            PIN: Ping_3192
            AEH: Mlg_1871
            HHA: Hhal_0215
            MMW: Mmwyl1_3990
            AHA: AHA_0096
            REU: Reut_A2159
            BVI: Bcep1808_1261
            BUR: Bcep18194_A4451
            HAR: HEAR1096(ppx)
            HPY: HP0278(gppA)
            HPJ: jhp0263(gppA)
            HPA: HPAG1_0280
            HHE: HH0984(ppx)
            HAC: Hac_0536(ppx)
            WSU: WS1910
            TDN: Tmden_0661
            CJE: Cj0353c
            CJR: CJE0402
            CJU: C8J_0330
            NIS: NIS_0408
            SUN: SUN_1985
            RPR: RP294(gppA)
            RTY: RT0285(gppA)
            RCO: RC0392(gppA)
            RFE: RF_0470(gppA)
            RBE: RBE_1019(gppA)
            BRA: BRADO3340
            BBT: BBta_3848
            CGL: NCgl0938(cgl0977)
            FAL: FRAAL6230(gppA)
            SYE: Syncc9902_1739
            TER: Tery_0231
            AAE: aq_891(ppx)
            TMA: TM0195
STRUCTURES  PDB: 1T6C  1T6D  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.40
            ExPASy - ENZYME nomenclature database: 3.6.1.40
            ExplorEnz - The Enzyme Database: 3.6.1.40
            ERGO genome analysis and discovery system: 3.6.1.40
            BRENDA, the Enzyme Database: 3.6.1.40
            CAS: 85130-44-5
///
ENTRY       EC 3.6.1.41                 Enzyme
NAME        bis(5'-nucleosyl)-tetraphosphatase (symmetrical);
            diadenosinetetraphosphatase (symmetrical);
            dinucleosidetetraphosphatasee (symmetrical);
            symmetrical diadenosine tetraphosphate hydrolase;
            adenosine tetraphosphate phosphodiesterase;
            Ap4A hydrolase;
            bis(5'-adenosyl) tetraphosphatase;
            diadenosine tetraphosphate hydrolase;
            diadenosine polyphosphate hydrolase;
            diadenosine 5',5'''-P1,P4-tetraphosphatase;
            diadenosinetetraphosphatase (symmetrical);
            1-P,4-P-bis(5'-nucleosyl)-tetraphosphate
            nucleosidebisphosphohydrolase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     P1,P4-bis(5'-nucleosyl)-tetraphosphate nucleosidebisphosphohydrolase
REACTION    P1,P4-bis(5'-adenosyl) tetraphosphate + H2O = 2 ADP [RN:R00125]
ALL_REAC    R00125
SUBSTRATE   P1,P4-bis(5'-adenosyl) tetraphosphate [CPD:C01260];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008]
COMMENT     Also acts on bis(5'-guanosyl) tetraphosphate and bis(5'-adenosyl)
            pentaphosphate and, more slowly, on some other polyphosphates,
            forming a nucleoside bisphosphate as one product in all cases [cf.
            EC 3.6.1.17 bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)].
REFERENCE   1  [PMID:6295456]
  AUTHORS   Barnes LD, Culver CA.
  TITLE     Isolation and characterization of diadenosine
            5',5&quot;'-P1,P4-tetraphosphate pyrophosphohydrolase from Physarum
            polycephalum.
  JOURNAL   Biochemistry. 21 (1982) 6123-8.
  ORGANISM  Physarum polycephalum
REFERENCE   2  [PMID:6317672]
  AUTHORS   Guranowski A, Jakubowski H, Holler E.
  TITLE     Catabolism of diadenosine 5',5&quot;'-P1,P4-tetraphosphate in
            procaryotes. Purification and properties of diadenosine
            5',5&quot;'-P1,P4-tetraphosphate (symmetrical) pyrophosphohydrolase
            from Escherichia coli K12.
  JOURNAL   J. Biol. Chem. 258 (1983) 14784-9.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01525  bis(5'-nucleosyl)-tetraphosphatase (symmetrical)
GENES       PIC: PICST_62390(APA4)
            TBR: Tb927.8.8040
            TCR: 504411.30
            ECO: b0049(apaH)
            ECJ: JW0048(apaH)
            ECE: Z0058(apaH)
            ECS: ECs0054
            ECC: c0061(apaH)
            ECI: UTI89_C0056(apaH)
            ECP: ECP_0051
            ECV: APECO1_1933(apaH)
            ECW: EcE24377A_0053(apaH)
            ECX: EcHS_A0055
            STY: STY0103(apaH)
            STT: t0091(apaH)
            SPT: SPA0089(apaH)
            SEC: SC0083(apaH)
            STM: STM0088(apaH)
            YPE: YPO0490(apaH)
            YPK: y3685(apaH)
            YPM: YP_3689(apaH)
            YPA: YPA_4084
            YPN: YPN_0364
            YPP: YPDSF_3144
            YPS: YPTB0631(apaH)
            YPI: YpsIP31758_3446
            SFL: SF0046(apaH)
            SFX: S0048(apaH)
            SFV: SFV_0043(apaH)
            SSN: SSON_0057(apaH)
            SBO: SBO_0038(apaH)
            SDY: SDY_0074(apaH)
            ECA: ECA3861(apaH)
            PLU: plu0607(apaH)
            BUC: BU142(apaH)
            BAS: BUsg135(apaH)
            BAB: bbp132(apaH)
            WBR: WGLp021(apaH)
            SGL: SG0422
            ENT: Ent638_0598
            SPE: Spro_0722
            BFL: Bfl125(apaH)
            BPN: BPEN_129(apaH)
            HIN: HI0551(apaH)
            HIT: NTHI0679(apaH)
            HIP: CGSHiEE_00225(apaH)
            HIQ: CGSHiGG_06040(apaH)
            HDU: HD1263(apaH)
            HSO: HS_1558(apaH)
            PMU: PM1210(adaH)
            MSU: MS0631(apaH)
            APL: APL_0760(apaH)
            ASU: Asuc_0734
            XFA: XF2150
            XFT: PD1210(apaH)
            XCC: XCC0789(apaH)
            XCB: XC_3442
            XCV: XCV0898(apaH)
            XAC: XAC0861(apaH)
            XOO: XOO3750(apaH)
            XOM: XOO_3540(XOO3540)
            VCH: VC0441
            VCO: VC0395_A2859(apaH)
            VVU: VV1_0665
            VVY: VV0476
            VPA: VP0334
            VFI: VF0285
            PPR: PBPRA0400
            PAE: PA0590(a)
            PAU: PA14_07700(apaH)
            PAP: PSPA7_0734
            PPU: PP_0399(apaH)
            PPF: Pput_0433
            PST: PSPTO_0549(apaH)
            PSB: Psyr_4629(apaH)
            PSP: PSPPH_0631(apaH)
            PFL: PFL_5651(apaH)
            PFO: Pfl_5137
            PEN: PSEEN0426(apaH)
            PMY: Pmen_4015
            PAR: Psyc_0962(apaH)
            PCR: Pcryo_1455
            PRW: PsycPRwf_0908
            ACI: ACIAD3008(apaH)
            SON: SO_3641(apaH)
            SDN: Sden_2890
            SFR: Sfri_3081
            SAZ: Sama_2821
            SBL: Sbal_0975
            SBM: Shew185_1044
            SLO: Shew_0877
            SPC: Sputcn32_0987
            SSE: Ssed_0962
            SPL: Spea_0860
            SHE: Shewmr4_0903
            SHM: Shewmr7_3117
            SHN: Shewana3_3211
            SHW: Sputw3181_3180
            ILO: IL2234(apaH)
            CPS: CPS_4527
            PHA: PSHAa2637(apaH)
            PAT: Patl_3423
            SDE: Sde_0735
            PIN: Ping_1046
            MAQ: Maqu_3506
            CBU: CBU_1987(apaH)
            CBD: COXBU7E912_2085(apaH)
            LPN: lpg2926(apaH)
            LPF: lpl2853(apaH)
            LPP: lpp2993(apaH)
            MCA: MCA0159(apaH)
            FTU: FTT0470(apaH)
            FTF: FTF0470(apaH)
            FTW: FTW_1600
            FTL: FTL_1594
            FTH: FTH_1540(apaH)
            FTA: FTA_1680
            FTN: FTN_0561(apaH)
            TCX: Tcr_1658
            NOC: Noc_1345
            AEH: Mlg_0223
            HHA: Hhal_1197
            HCH: HCH_06101
            CSA: Csal_0922
            ABO: ABO_2050(apaH)
            MMW: Mmwyl1_1049
            AHA: AHA_0940
            DNO: DNO_1294(apaH)
            BCI: BCI_0562
            RMA: Rmag_0549
            VOK: COSY_0504(apaH)
            NMA: NMA0860(apaH)
            NMC: NMC0610(apaH)
            NGO: NGO0231
            CVI: CV_4067(apaH)
            RSO: RSc0681(apaH)
            REU: Reut_A0711
            RME: Rmet_2736
            BMA: BMA1991
            BMV: BMASAVP1_A0922
            BML: BMA10299_A2752
            BMN: BMA10247_1853
            BXE: Bxe_A3805
            BVI: Bcep1808_0804
            BUR: Bcep18194_A3968
            BCN: Bcen_0388
            BCH: Bcen2424_0870
            BAM: Bamb_0743
            BPS: BPSL2687(apaH)
            BPM: BURPS1710b_3164
            BPL: BURPS1106A_3142
            BPD: BURPS668_3106
            BTE: BTH_I1468
            PNU: Pnuc_0240
            BPE: BP0324(apaH)
            BPA: BPP3927(apaH)
            BBR: BB4400(apaH)
            RFR: Rfer_3027
            POL: Bpro_1518
            PNA: Pnap_3200
            AAV: Aave_1149
            AJS: Ajs_1143
            VEI: Veis_1340
            MPT: Mpe_A2854
            HAR: HEAR2734(apaH)
            MMS: mma_2944
            NEU: NE0613
            NET: Neut_1949
            NMU: Nmul_A0206
            EBA: ebA1627(apaH)
            AZO: azo0853(apaH)
            DAR: Daro_3932
            TBD: Tbd_0168
            MFA: Mfla_0467
            HPA: HPAG1_0988
            SUN: SUN_0610(apaH)
            ZMO: ZMO1498(apaH) ZMO1743(apaH)
            MGM: Mmc1_0643
            BSU: BG13145(yjbP)
            BHA: BH2845
            BLI: BL05112(yjbP)
            BLD: BLi01257(yjbP)
            OIH: OB1223
            RBA: RB13110(apaH)
            AVA: Ava_4095
            NPH: NP0728A
STRUCTURES  PDB: 2DFJ  2QJC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.41
            ExPASy - ENZYME nomenclature database: 3.6.1.41
            ExplorEnz - The Enzyme Database: 3.6.1.41
            ERGO genome analysis and discovery system: 3.6.1.41
            BRENDA, the Enzyme Database: 3.6.1.41
            CAS: 85638-48-8
///
ENTRY       EC 3.6.1.42                 Enzyme
NAME        guanosine-diphosphatase;
            GDPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     GDP phosphohydrolase
REACTION    GDP + H2O = GMP + phosphate [RN:R00328]
ALL_REAC    R00328
SUBSTRATE   GDP [CPD:C00035];
            H2O [CPD:C00001]
PRODUCT     GMP [CPD:C00144];
            phosphate [CPD:C00009]
COMMENT     Also acts on UDP but not on other nucleoside diphosphates and
            triphosphates.
REFERENCE   1  [PMID:2989286]
  AUTHORS   Raychaudhuri P, Ghosh S, Maitra U.
  TITLE     Purification and characterization of a guanosine diphosphatase
            activity from calf liver microsomal salt wash proteins.
  JOURNAL   J. Biol. Chem. 260 (1985) 8306-11.
  ORGANISM  cow [GN:bta]
ORTHOLOGY   KO: K01526  
GENES       SCE: YEL042W(GDA1)
            AGO: AGOS_AFR362C
            PIC: PICST_82228(GDA1)
            CGR: CAGL0L01243g
            SPO: SPAC824.08
            ANI: AN1082.2
            AFM: AFUA_1G12150
            AOR: AO090001000329
            CNE: CNB04810
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.42
            ExPASy - ENZYME nomenclature database: 3.6.1.42
            ExplorEnz - The Enzyme Database: 3.6.1.42
            ERGO genome analysis and discovery system: 3.6.1.42
            BRENDA, the Enzyme Database: 3.6.1.42
            CAS: 98037-56-0
///
ENTRY       EC 3.6.1.43                 Enzyme
NAME        dolichyldiphosphatase;
            dolichol diphosphatase;
            dolichyl pyrophosphatase;
            dolichyl pyrophosphate phosphatase;
            dolichyl diphosphate phosphohydrolase;
            Dol-P-P phosphohydrolase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     dolichyl-diphosphate phosphohydrolase
REACTION    dolichyl diphosphate + H2O = dolichyl phosphate + phosphate
            [RN:R01004]
ALL_REAC    R01004
SUBSTRATE   dolichyl diphosphate [CPD:C00621];
            H2O [CPD:C00001]
PRODUCT     dolichyl phosphate [CPD:C00110];
            phosphate [CPD:C00009]
REFERENCE   1
  AUTHORS   Naumov, A.V., Shabalin, Y.A., Vagabov, V.M. and Kulaev, I.S.
  TITLE     Two pathways of dephosphorylation of dolichyl diphosphate in yeasts.
  JOURNAL   Biochemistry (Moscow) 50 (1985) 551-556.
PATHWAY     PATH: map00510  N-Glycan biosynthesis
ORTHOLOGY   KO: K07252  dolichyldiphosphatase
GENES       HSA: 57171(DOLPP1)
            PTR: 464782(DOLPP1)
            MMU: 57170(Dolpp1)
            RNO: 296624(Dolpp1_predicted)
            CFA: 612827(DOLPP1)
            BTA: 504908(LOC504908)
            XTR: 549768(dolpp1)
            DRE: 474331(zgc:101585)
            SPU: 753409(LOC753409)
            ATH: AT5G03080
            OSA: 4332492
            SCE: YGR036C(CAX4)
            AGO: AGOS_ACL186W
            PIC: PICST_57488
            CGR: CAGL0K04103g
            SPO: SPBC530.12c
            ANI: AN6610.2
            AFM: AFUA_6G04240
            CNE: CNC00710
            DDI: DDBDRAFT_0167904
            TBR: Tb927.6.1820
            TCR: 511491.130
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.43
            ExPASy - ENZYME nomenclature database: 3.6.1.43
            ExplorEnz - The Enzyme Database: 3.6.1.43
            ERGO genome analysis and discovery system: 3.6.1.43
            BRENDA, the Enzyme Database: 3.6.1.43
            CAS: 73361-26-9
///
ENTRY       EC 3.6.1.44                 Enzyme
NAME        oligosaccharide-diphosphodolichol diphosphatase;
            oligosaccharide-diphosphodolichol pyrophosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     oligosaccharide-diphosphodolichol phosphodolichohydrolase
REACTION    oligosaccharide-diphosphodolichol + H2O = oligosaccharide phosphate
            + dolichyl phosphate [RN:R04272]
ALL_REAC    R04272
SUBSTRATE   oligosaccharide-diphosphodolichol [CPD:C04213];
            H2O [CPD:C00001]
PRODUCT     oligosaccharide phosphate [CPD:C03632];
            dolichyl phosphate [CPD:C00110]
REFERENCE   1  [PMID:2848504]
  AUTHORS   Belard M, Cacan R, Verbert A.
  TITLE     Characterization of an oligosaccharide-pyrophosphodolichol
            pyrophosphatase activity in yeast.
  JOURNAL   Biochem. J. 255 (1988) 235-42.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.44
            ExPASy - ENZYME nomenclature database: 3.6.1.44
            ExplorEnz - The Enzyme Database: 3.6.1.44
            ERGO genome analysis and discovery system: 3.6.1.44
            BRENDA, the Enzyme Database: 3.6.1.44
            CAS: 117698-28-9
///
ENTRY       EC 3.6.1.45                 Enzyme
NAME        UDP-sugar diphosphatase;
            nucleosidediphosphate-sugar pyrophosphatase;
            nucleosidediphosphate-sugar diphosphatase;
            UDP-sugar hydrolase;
            UDP-sugar pyrophosphatase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     UDP-sugar sugarphosphohydrolase
REACTION    UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate [RN:R03986]
ALL_REAC    R03986
SUBSTRATE   UDP-sugar [CPD:C05227];
            H2O [CPD:C00001]
PRODUCT     UMP [CPD:C00105];
            alpha-D-aldose 1-phosphate [CPD:C00991]
COMMENT     A divalent cation is required for activity. UDP-sugar is the best
            substrate, although other nucleoside-sugar diphosphates are used as
            substrates with similar Km values but much lower maximum velocities.
            Thus, this enzyme has a specificity distinct from that of ADP-sugar
            diphosphatase (EC 3.6.1.21). Some but not all enzymes of this class
            also appear to have 5'-nucleotidase (see EC 3.1.3.5) activity.
REFERENCE   1  [PMID:2548058]
  AUTHORS   Garrett AR, Johnson LA, Beacham IR.
  TITLE     Isolation, molecular characterization and expression of the ushB
            gene of Salmonella typhimurium which encodes a membrane-bound
            UDP-sugar hydrolase.
  JOURNAL   Mol. Microbiol. 3 (1989) 177-86.
  ORGANISM  Salmonella typhimurium
REFERENCE   2
  AUTHORS   Glaser, L., Melo, A., Paul, R.
  TITLE     Uridine diphosphate sugar hydrolase. Purification of enzyme and
            protein inhibitor.
  JOURNAL   J. Biol. Chem. 242 (1987) 1944-1954.
ORTHOLOGY   KO: K08077  UDP-sugar diphosphatase
GENES       HSA: 256281(NUDT14)
            MMU: 66174(Nudt14)
            CFA: 612707(NUDT14)
            AFM: AFUA_4G02960
            ECO: b0480(ushA)
            ECJ: JW0469(ushA)
            ECE: Z0599(ushA)
            ECS: ECs0533
            ECC: c0600(ushA)
            ECI: UTI89_C0508(ushA)
            ECP: ECP_0541
            ECV: APECO1_1535(ushA)
            ECW: EcE24377A_0519(ushA)
            ECX: EcHS_A0557(ushA)
            SPT: SPA2228(ushA)
            SEC: SC0536(ushA)
            STM: STM0494(ushA)
            YPI: YpsIP31758_3032(ushA)
            SFL: SF0425(ushA)
            SFX: S0432(ushA)
            SSN: SSON_0469(ushA)
            SBO: SBO_0382(ushA)
            SDY: SDY_0438(ushA)
            ECA: ECA1184(ushA)
            PLU: plu3828(ushA)
            PMU: PM1193
            MSU: MS1658(ushA)
            APL: APL_0769(ushA)
            VPA: VP1207
            SON: SO_2001(ushA)
            PHA: PSHAb0345(ushA)
            PIN: Ping_3661 Ping_3682
            CVI: CV_1743(ushA) CV_3083
            HAC: Hac_0900
            TDN: Tmden_0369
            CCV: CCV52592_0730
            CHA: CHAB381_1625
            SAT: SYN_02264
            MMO: MMOB0990(ushA)
            CGL: NCgl0322(cgl0328)
            TMA: TM1878
            HWA: HQ2723A(ushA)
            NPH: NP1854A(ushA_1) NP2590A(ushA_2)
STRUCTURES  PDB: 1HO5  1HP1  1HPU  1OI8  1OID  1OIE  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.45
            ExPASy - ENZYME nomenclature database: 3.6.1.45
            ExplorEnz - The Enzyme Database: 3.6.1.45
            ERGO genome analysis and discovery system: 3.6.1.45
            BRENDA, the Enzyme Database: 3.6.1.45
            CAS: 57127-20-5
///
ENTRY       EC 3.6.1.46       Obsolete  Enzyme
NAME        Transferred to 3.6.5.1
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
COMMENT     Transferred entry: now EC 3.6.5.1 heterotrimeric G-protein GTPase
            (EC 3.6.1.46 created 2000, deleted 2003)
STRUCTURES  PDB: 1SVK  1SVS  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.46
            ExPASy - ENZYME nomenclature database: 3.6.1.46
            ExplorEnz - The Enzyme Database: 3.6.1.46
            ERGO genome analysis and discovery system: 3.6.1.46
            BRENDA, the Enzyme Database: 3.6.1.46
///
ENTRY       EC 3.6.1.47       Obsolete  Enzyme
NAME        Transferred to 3.6.5.2
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
COMMENT     Transferred entry: Now EC 3.6.5.2, small monomeric GTPase (EC
            3.6.1.47 created 2000, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.47
            ExPASy - ENZYME nomenclature database: 3.6.1.47
            ExplorEnz - The Enzyme Database: 3.6.1.47
            ERGO genome analysis and discovery system: 3.6.1.47
            BRENDA, the Enzyme Database: 3.6.1.47
///
ENTRY       EC 3.6.1.48       Obsolete  Enzyme
NAME        Transferred to 3.6.5.3
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
COMMENT     Transferred entry: now EC 3.6.5.3 protein-synthesizing GTPase (EC
            3.6.1.48 created 2000, deleted 200)
STRUCTURES  PDB: 1OB2  2BVN  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.48
            ExPASy - ENZYME nomenclature database: 3.6.1.48
            ExplorEnz - The Enzyme Database: 3.6.1.48
            ERGO genome analysis and discovery system: 3.6.1.48
            BRENDA, the Enzyme Database: 3.6.1.48
///
ENTRY       EC 3.6.1.49       Obsolete  Enzyme
NAME        Transferred to 3.6.5.4
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
COMMENT     Transferred entry: now EC 3.6.5.4 signal-recognition-particle GTPase
            (EC 3.6.1.49 created 2000, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.49
            ExPASy - ENZYME nomenclature database: 3.6.1.49
            ExplorEnz - The Enzyme Database: 3.6.1.49
            ERGO genome analysis and discovery system: 3.6.1.49
            BRENDA, the Enzyme Database: 3.6.1.49
///
ENTRY       EC 3.6.1.50       Obsolete  Enzyme
NAME        Transferred to 3.6.5.5
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
COMMENT     Transferred entry: now EC 3.6.5.5, dynamin GTPase (EC 3.6.1.50
            created 2000, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.50
            ExPASy - ENZYME nomenclature database: 3.6.1.50
            ExplorEnz - The Enzyme Database: 3.6.1.50
            ERGO genome analysis and discovery system: 3.6.1.50
            BRENDA, the Enzyme Database: 3.6.1.50
///
ENTRY       EC 3.6.1.51       Obsolete  Enzyme
NAME        Transferred to 3.6.5.6
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
COMMENT     Transferred entry: now EC 3.6.5.6, tubulin GTPase (EC 3.6.1.51
            created 2000, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.51
            ExPASy - ENZYME nomenclature database: 3.6.1.51
            ExplorEnz - The Enzyme Database: 3.6.1.51
            ERGO genome analysis and discovery system: 3.6.1.51
            BRENDA, the Enzyme Database: 3.6.1.51
///
ENTRY       EC 3.6.1.52                 Enzyme
NAME        diphosphoinositol-polyphosphate diphosphatase;
            diphosphoinositol-polyphosphate phosphohydrolase;
            DIPP
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
SYSNAME     diphospho-myo-inositol-polyphosphate diphosphohydrolase
REACTION    diphospho-myo-inositol polyphosphate + H2O = myo-inositol
            polyphosphate + phosphate [RN:R05777]
ALL_REAC    R05777 > R05779
SUBSTRATE   diphospho-myo-inositol polyphosphate [CPD:C11524];
            H2O [CPD:C00001]
PRODUCT     myo-inositol polyphosphate [CPD:C11525];
            phosphate [CPD:C00009]
COMMENT     This enzyme hydrolyses the diphosphate bond, leaving a phospho group
            where a diphospho group had been. It can also act on bis(adenosine)
            diphosphate.
REFERENCE   1  [PMID:9822604]
  AUTHORS   Safrany ST, Caffrey JJ, Yang X, Bembenek ME, Moyer MB, Burkhart WA,
            Shears SB.
  TITLE     A novel context for the 'MutT' module, a guardian of cell integrity,
            in a diphosphoinositol polyphosphate phosphohydrolase.
  JOURNAL   EMBO. J. 17 (1998) 6599-607.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:10777568]
  AUTHORS   Caffrey JJ, Safrany ST, Yang X, Shears SB.
  TITLE     Discovery of molecular and catalytic diversity among human
            diphosphoinositol-polyphosphate phosphohydrolases. An expanding Nudt
            family.
  JOURNAL   J. Biol. Chem. 275 (2000) 12730-6.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K07766  diphosphoinositol-polyphosphate diphosphatase
GENES       HSA: 11163(NUDT4) 11165(NUDT3) 55190(NUDT11)
            MMU: 56409(Nudt3) 58242(Nudt11) 71207(Nudt4)
            RNO: 294292(Nudt3) 94267(Nudt4)
            CFA: 475425(NUDT4)
            GGA: 417897(NUDT4) 419905(NUDT3)
            XLA: 447697(MGC81536) 495434(LOC495434)
            XTR: 448180(nudt4)
            DRE: 394120(zgc:55746)
            DME: Dmel_CG6391(Aps)
STRUCTURES  PDB: 2DUK  2FVV  2Q9P  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.1.52
            ExPASy - ENZYME nomenclature database: 3.6.1.52
            ExplorEnz - The Enzyme Database: 3.6.1.52
            ERGO genome analysis and discovery system: 3.6.1.52
            BRENDA, the Enzyme Database: 3.6.1.52
///
ENTRY       EC 3.6.1.-                  Enzyme
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In phosphorus-containing anhydrides
REACTION    (1) Isomaltose + ATP + H2O <=> Isomaltose + Orthophosphate + ADP
            [RN:R01719];
            (2) UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + H2O <=> UMP +
            2,3-Bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate
            [RN:R04549];
            (3)
            2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-
            dihydropteridine + Orthophosphate <=> Dihydroneopterin phosphate +
            H2O [RN:R04621];
            (4)
            2-Amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine
            triphosphate + H2O <=> Dihydroneopterin phosphate + Pyrophosphate
            [RN:R04638];
            (5) Isomaltose + ATP + H2O <=> Isomaltose + Orthophosphate + ADP
            [RN:R06220]
SUBSTRATE   Isomaltose [CPD:C00252];
            ATP [CPD:C00002];
            H2O [CPD:C00001];
            UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine [CPD:C04652];
            2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-
            dihydropteridine [CPD:C04874];
            Orthophosphate [CPD:C00009];
            2-Amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine
            triphosphate [CPD:C04895];
            Isomaltose [GL:G01318]
PRODUCT     Isomaltose [CPD:C00252];
            Orthophosphate [CPD:C00009];
            ADP [CPD:C00008];
            UMP [CPD:C00105];
            2,3-Bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate
            [CPD:C04824];
            Dihydroneopterin phosphate [CPD:C05925];
            H2O [CPD:C00001];
            Pyrophosphate [CPD:C00013];
            Isomaltose [GL:G01318];
            ADP [GL:G11113]
///
ENTRY       EC 3.6.2.1                  Enzyme
NAME        adenylylsulfatase;
            adenosine 5-phosphosulfate sulfohydrolase;
            adenylylsulfate sulfohydrolase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In sulfonyl-containing anhydrides
SYSNAME     adenylyl-sulfate sulfohydrolase
REACTION    adenylyl sulfate + H2O = AMP + sulfate [RN:R00531]
ALL_REAC    R00531
SUBSTRATE   adenylyl sulfate [CPD:C00224];
            H2O [CPD:C00001]
PRODUCT     AMP [CPD:C00020];
            sulfate [CPD:C00059]
REFERENCE   1  [PMID:5801298]
  AUTHORS   Bailey-Wood R, Dodgson KS, Rose FA.
  TITLE     A rat liver sulphohydrolase enzyme acting on adenylyl sulphate.
  JOURNAL   Biochem. J. 112 (1969) 257-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00920  Sulfur metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.2.1
            ExPASy - ENZYME nomenclature database: 3.6.2.1
            ExplorEnz - The Enzyme Database: 3.6.2.1
            ERGO genome analysis and discovery system: 3.6.2.1
            BRENDA, the Enzyme Database: 3.6.2.1
            CAS: 37289-36-4
///
ENTRY       EC 3.6.2.2                  Enzyme
NAME        phosphoadenylylsulfatase;
            3-phosphoadenylyl sulfatase;
            3-phosphoadenosine 5-phosphosulfate sulfatase;
            PAPS sulfatase;
            3'-phosphoadenylylsulfate sulfohydrolase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            In sulfonyl-containing anhydrides
SYSNAME     3'-phosphoadenylyl-sulfate sulfohydrolase
REACTION    3'-phosphoadenylyl sulfate + H2O = adenosine 3',5'-bisphosphate +
            sulfate [RN:R00507]
ALL_REAC    R00507
SUBSTRATE   3'-phosphoadenylyl sulfate [CPD:C00053];
            H2O [CPD:C00001]
PRODUCT     adenosine 3',5'-bisphosphate [CPD:C00054];
            sulfate [CPD:C00059]
COFACTOR    Manganese [CPD:C00034]
COMMENT     Requires Mn2+.
REFERENCE   1  [PMID:13864264]
  AUTHORS   BALASUBRAMANIAN AS, BACHHAWAT BK.
  TITLE     Enzymic degradation of active sulphate.
  JOURNAL   Biochim. Biophys. Acta. 59 (1962) 389-97.
  ORGANISM  sheep
PATHWAY     PATH: map00920  Sulfur metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.2.2
            ExPASy - ENZYME nomenclature database: 3.6.2.2
            ExplorEnz - The Enzyme Database: 3.6.2.2
            ERGO genome analysis and discovery system: 3.6.2.2
            BRENDA, the Enzyme Database: 3.6.2.2
            CAS: 37289-37-5
///
ENTRY       EC 3.6.3.1                  Enzyme
NAME        phospholipid-translocating ATPase;
            Mg2+-ATPase;
            flippase;
            aminophospholipid-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (phospholipid-flipping)
REACTION    ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout
            [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            phospholipid [CPD:C00865]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            phospholipid [CPD:C00865]
COMMENT     A P-type ATPase that undergoes covalent phosphorylation during the
            transport cycle. The enzyme apparently has several activities, one
            of them being the movement of phospholipids from one membrane face
            to the other ('flippase').
REFERENCE   1  [PMID:8136700]
  AUTHORS   Morris MB, Auland ME, Xu YH, Roufogalis BD.
  TITLE     Characterization of the Mg(2+)-ATPase activity of the human
            erythrocyte membrane.
  JOURNAL   Biochem. Mol. Biol. Int. 31 (1993) 823-32.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:8839453]
  AUTHORS   Vermeulen WP, Briede JJ, Roelofsen B.
  TITLE     Manipulation of the phosphatidylethanolamine pool in the human red
            cell membrane affects its Mg2+-ATPase activity.
  JOURNAL   Mol. Membr. Biol. 13 (1996) 95-102.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:9099684]
  AUTHORS   Suzuki H, Kamakura M, Morii M, Takeguchi N.
  TITLE     The phospholipid flippase activity of gastric vesicles.
  JOURNAL   J. Biol. Chem. 272 (1997) 10429-34.
  ORGANISM  mouse [GN:mmu]
REFERENCE   4  [PMID:7971987]
  AUTHORS   Auland ME, Roufogalis BD, Devaux PF, Zachowski A.
  TITLE     Reconstitution of ATP-dependent aminophospholipid translocation in
            proteoliposomes.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 10938-42.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01530  phospholipid-translocating ATPase
GENES       HSA: 10079(ATP9A) 10396(ATP8A1) 148229(ATP8B3) 23200(ATP11B)
                 23250(ATP11A) 286410(ATP11C) 374868(ATP9B) 51761(ATP8A2)
                 5205(ATP8B1) 57194(ATP10A) 57198(ATP8B2) 57205(ATP10D)
                 79895(ATP8B4)
            PTR: 455439(ATP8B1)
            MMU: 11980(Atp8a1) 11981(Atp9a) 11982(Atp10a) 231287(Atp10d)
                 320940(Atp11c) 50769(Atp8a2) 50770(Atp11a) 50771(Atp9b)
                 54667(Atp8b2) 54670(Atp8b1) 67331(Atp8b3) 76295(Atp11b)
            RNO: 291411(LOC291411)
            CFA: 476190(ATP8B1) 476992(ATP11A) 477265(ATP9A) 478644(ATP11B)
                 481066(ATP11C) 482134(ATP10D) 487549(ATP8B4) 488691(ATP10A)
                 490447(ATP8B2) 607976(ATP8A1) 612245(ATP8B3)
            BTA: 317692(ATP8A1)
            GGA: 418685(ATP10A) 418749(ATP11A) 418936(ATP8A2) 419345(ATP9A)
                 422254(ATP11C) 422768(ATP10D) 422776(ATP8A1) 428328(ATP8B3)
            XLA: 380518(atp11a)
            XTR: 394841(atp9a)
            DRE: 568160(si:ch211-198c22.1)
            SPU: 580898(LOC580898) 594696(LOC594696)
            DME: Dmel_CG14741 Dmel_CG31729
            CEL: F02C9.3(ATPase) W09D10.2(ATPase)
            ATH: AT1G13210 AT1G17500 AT1G26130 AT1G54280 AT1G59820 AT1G68710
                 AT1G72700 AT3G13900 AT3G25610 AT3G27870 AT5G44240
            OSA: 4324268 4335557 4341328 4350436
            CME: CMR306C CMS375C
            SCE: YAL026C(DRS2) YDR093W(DNF2) YER166W(DNF1) YIL048W(NEO1)
                 YMR162C(DNF3)
            AGO: AGOS_ADL079C AGOS_ADR350W AGOS_AFL191W AGOS_AGR120C
            PIC: PICST_52414(NEO1) PICST_81178(DNF2) PICST_85147(DNF1)
            CAL: CaO19_2680(CaO19.2680) CaO19_323(CaO19.323)
                 CaO19_6778(CaO19.6778) CaO19_932(CaO19.932)
            CGR: CAGL0H04477g CAGL0L00715g CAGL0L11814g
            SPO: SPAC24B11.12c SPAC4F10.16c SPAC6C3.06c SPAC955.01c SPBC887.12
            ANI: AN2011.2 AN6112.2 AN6614.2
            AFM: AFUA_2G08850 AFUA_4G10210 AFUA_6G02070 AFUA_6G03950
            AOR: AO090003001200 AO090011000813 AO090701000148
            CNE: CNA03720 CND03980 CNH03470 CNN01890
            UMA: UM02436.1 UM03293.1
            ECU: ECU06_0930 ECU09_1440
            DDI: DDBDRAFT_0185285 DDBDRAFT_0190219 DDBDRAFT_0216656
            PFA: PFL0950c PFL1125w
            CPV: cgd3_2730
            CHO: Chro.20257 Chro.30311
            TAN: TA04770
            TPV: TP02_0772
            TET: TTHERM_00123720 TTHERM_00158340 TTHERM_00294760
                 TTHERM_00316630 TTHERM_00325570 TTHERM_00372460
                 TTHERM_00429720 TTHERM_00449540 TTHERM_00715640
                 TTHERM_00797940 TTHERM_00797960 TTHERM_00797970
                 TTHERM_00923160 TTHERM_00977610 TTHERM_00977720
                 TTHERM_00994350 TTHERM_01123860 TTHERM_01156820
                 TTHERM_01156830 TTHERM_01166280 TTHERM_01359440
            TBR: Tb11.02.0850 Tb927.4.1510 Tb927.6.3550
            TCR: 503999.100 504057.11 506941.60 509591.60 511511.60
            LMA: LmjF13.1530 LmjF30.2260 LmjF34.3220
            EHI: 191.t00016 21.t00048 309.t00009 6.t00057 8.t00012
            REH: H16_A0904
            MTU: Rv1811(mgtC)
            MBO: Mb1841(mgtC)
            MBB: BCG_1845
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.1
            ExPASy - ENZYME nomenclature database: 3.6.3.1
            ExplorEnz - The Enzyme Database: 3.6.3.1
            ERGO genome analysis and discovery system: 3.6.3.1
            BRENDA, the Enzyme Database: 3.6.3.1
///
ENTRY       EC 3.6.3.2                  Enzyme
NAME        Mg2+-importing ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (Mg2+-importing)
REACTION    ATP + H2O + Mg2+out = ADP + phosphate + Mg2+in [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            Mg2+ [CPD:C00305]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            Mg2+ [CPD:C00305]
COMMENT     A P-type ATPase that undergoes covalent phosphorylation during the
            transport cycle. This enzyme occurs in both Gram-positive and
            Gram-negative bacteria, and three types are known, designated as
            CorA, MgtA and MgtB. The CorA itself is not an ATPase but an Mg2+
            transporter.
REFERENCE   1  [PMID:7751273]
  AUTHORS   Tao T, Snavely MD, Farr SG, Maguire ME.
  TITLE     Magnesium transport in Salmonella typhimurium: mgtA encodes a P-type
            ATPase and is regulated by Mg2+ in a manner similar to that of the
            mgtB P-type ATPase.
  JOURNAL   J. Bacteriol. 177 (1995) 2654-62.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:9786860]
  AUTHORS   Smith RL, Szegedy MA, Kucharski LM, Walker C, Wiet RM, Redpath A,
            Kaczmarek MT, Maguire ME.
  TITLE     The CorA Mg2+ transport protein of Salmonella typhimurium.
            Mutagenesis of conserved residues in the third membrane domain
            identifies a Mg2+ pore.
  JOURNAL   J. Biol. Chem. 273 (1998) 28663-9.
  ORGANISM  Salmonella typhimurium
ORTHOLOGY   KO: K01531  Mg2+-importing ATPase
GENES       DDI: DDBDRAFT_0190054
            ECO: b4242(mgtA)
            ECJ: JW4201(mgtA)
            ECE: Z5853(mgtA)
            ECS: ECs5219
            ECC: c5341(mgtA)
            ECI: UTI89_C4847(mgtA)
            ECP: ECP_4492
            ECW: EcE24377A_4814(mgtA)
            ECX: EcHS_A4497
            STY: STY4023(mgtB) STY4796(mgtA)
            STT: t3755(mgtB) t4491(mgtA)
            SPT: SPA3613(mgtB)
            SEC: SC3684(mgtB) SC4312(mgtA)
            STM: STM3763(mgtB) STM4456(mgtA)
            YPE: YPO1661(mgtB)
            YPK: y1821(mgtA)
            YPM: YP_1791(mgtB)
            YPA: YPA_1860
            YPN: YPN_1969
            YPP: YPDSF_1786
            YPS: YPTB2410(mgtB)
            YPI: YpsIP31758_1633(mgtA)
            YEN: YE3776(mgtA)
            SFL: SF4248(mgtA)
            SFX: S4510(mgtA)
            SFV: SFV_4250(mgtA)
            SSN: SSON_4423(mgtA)
            SBO: SBO_4204(mgtA)
            SDY: SDY_4261(mgtA)
            ECA: ECA0435(mgtB)
            ENT: Ent638_0441
            SPE: Spro_0535
            PAE: PA4825(mgtA)
            PAU: PA14_63800(mgtA)
            PAP: PSPA7_5544(mgtA)
            PPU: PP_2645(mgtB)
            PPF: Pput_2150
            PFL: PFL_3349 PFL_4078
            PFO: Pfl_1860
            PEN: PSEEN5381(mgtA)
            ACI: ACIAD1984(mgtA)
            LPN: lpg2381(mgt)
            MCA: MCA1929
            AHA: AHA_0238(mgtA)
            CVI: CV_3100(mgtA)
            REU: Reut_A1214
            BMA: BMAA1250
            BMV: BMASAVP1_0223
            BML: BMA10299_0495
            BMN: BMA10247_A1076
            BXE: Bxe_B2642
            BUR: Bcep18194_B1281
            BCN: Bcen_3803
            BCH: Bcen2424_4565
            BPS: BPSS0973(mgtB)
            BPM: BURPS1710b_A0054 BURPS1710b_A2583(mgtA)
            BPL: BURPS1106A_A1341(mgtA)
            BPD: BURPS668_A1423(mgtA)
            BTE: BTH_II1418(mgtA)
            BBR: BB1100(mgtA)
            RFR: Rfer_0493
            VEI: Veis_0398
            HAR: HEAR2341(mgtA)
            DAR: Daro_2078
            SAT: SYN_02760
            MLO: mlr6609
            BME: BMEII0056
            BMF: BAB2_0036
            BMS: BRA0037
            BMB: BruAb2_0037
            BOV: BOV_A0033(mgtA)
            BJA: blr7053
            BCE: BC4140
            BCA: BCE_4212
            BCZ: BCZK1460
            LMO: lmo2689
            LMF: LMOf2365_2668
            LIN: lin2836
            LWE: lwe2637(mgtA)
            LLA: L85514(mgtA)
            LLC: LACR_1370
            SSA: SSA_1734
            SGO: SGO_1634
            LJO: LJ1155
            LAC: LBA0212
            LCA: LSEI_2281
            EFA: EF1304 EF1352
            CPF: CPF_1153(mgtA)
            CDF: CD3373(mgtB) CD3377(mgtA)
            CBO: CBO2869(mgtA)
            CBA: CLB_2835(mgtA)
            CBH: CLC_2768(mgtA)
            CBF: CLI_2925(mgtA)
            TTE: TTE2509(mgtA3)
            MMY: MSC_0868(mgtA) MSC_0881(mgtA) MSC_0907(mgtA)
            MCP: MCAP_0087(mgtA) MCAP_0812
            POY: PAM585(mgtA)
            AYW: AYWB_242(mgtB)
            MFL: Mfl496
            LXX: Lxx21190
            FRA: Francci3_2615
            LIL: LA2221(mgtA)
            LIC: LIC11710(mgtB)
            AVA: Ava_1904
            BTH: BT_0988
            BFR: BF0211
            BFS: BF0170(mgtA)
            CTE: CT0630(mgt)
            MBA: Mbar_A2103
            RCI: RCIX2694(mgtA)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.2
            ExPASy - ENZYME nomenclature database: 3.6.3.2
            ExplorEnz - The Enzyme Database: 3.6.3.2
            ERGO genome analysis and discovery system: 3.6.3.2
            BRENDA, the Enzyme Database: 3.6.3.2
///
ENTRY       EC 3.6.3.3                  Enzyme
NAME        Cd2+-exporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (Cd2+-exporting)
REACTION    ATP + H2O + Cd2+in = ADP + phosphate + Cd2+out [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            Cd2+ [CPD:C01413]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            Cd2+ [CPD:C01413]
COMMENT     A P-type ATPase that undergoes covalent phosphorylation during the
            transport cycle. This enzyme occurs in protozoa, fungi and plants.
REFERENCE   1  [PMID:7843081]
  AUTHORS   Silver S, Ji G.
  TITLE     Newer systems for bacterial resistances to toxic heavy metals.
  JOURNAL   Environ. Health. Perspect. 102 Suppl 3 (1994) 107-13.
  ORGANISM  Staphylococcus aureus, Bacillus firmus
REFERENCE   2  [PMID:8373163]
  AUTHORS   Tsai KJ, Linet AL.
  TITLE     Formation of a phosphorylated enzyme intermediate by the cadA
            Cd(2+)-ATPase.
  JOURNAL   Arch. Biochem. Biophys. 305 (1993) 267-70.
  ORGANISM  Bacillus subtilis [GN:bsu]
ORTHOLOGY   KO: K01532  Cd2+-exporting ATPase
GENES       ATH: AT2G19110(HMA4) AT4G30110(HMA2)
            ECO: b3469(zntA)
            ECJ: JW3434(zntA)
            ECE: Z4843(zntA)
            ECS: ECs4318
            ECC: c4262(zntA)
            ECI: UTI89_C3984(zntA)
            ECP: ECP_3562
            ECV: APECO1_2985(zntA)
            STY: STY4235
            STT: t3946
            SPT: SPA3427(zntA)
            SEC: SC3505(zntA)
            STM: STM3576(zntA)
            YPE: YPO3820
            YPK: y0410(zntA)
            YPM: YP_3228(zntA2)
            YPA: YPA_0202
            YPN: YPN_0144
            YPS: YPTB0215(ATZN)
            SFL: SF3487(zntA)
            SFX: S4276(zntA)
            SFV: SFV_3472(zntA)
            SSN: SSON_3707(zntA)
            SBO: SBO_3466(zntA)
            SDY: SDY_3620(zntA)
            ECA: ECA4352(zntA)
            PLU: plu4108(zntA)
            VCH: VC1033
            VVU: VV1_2063
            VVY: VV2378
            VPA: VP0959
            VFI: VF1522
            PPR: PBPRA1220
            PSP: PSPPH_4869
            PEN: PSEEN5232(cadA)
            LPN: lpg1010
            AHA: AHA_0629
            REU: Reut_B3972
            BUR: Bcep18194_A3304 Bcep18194_C7188
            BAM: Bamb_0114
            BPM: BURPS1710b_0150(cadA)
            BTE: BTH_I3290
            HAR: HEAR0519 HEAR1542 HEAR1592 HEAR1616
            MFA: Mfla_2550
            HPY: HP0791(cadA)
            HPJ: jhp0727(hmcT)
            HPA: HPAG1_0776
            HHE: HH0586
            HAC: Hac_0913(yvgW)
            NWI: Nwi_3134
            RRU: Rru_A1027
            SAR: SAR0723(cadA)
            LMO: lmo1100(cadA)
            LIN: pli0061
            SPZ: M5005_Spy_1167
            SPB: M28_Spy1161
            LSA: LSA0425
            FNU: FN1190
            RBA: RB4891
            AVA: Ava_1125 Ava_3859
            GFO: GFO_0024 GFO_0269 GFO_1200
            RCI: RCIX2335(cadA)
STRUCTURES  PDB: 1MWY  1MWZ  2AJ0  2AJ1  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.3
            ExPASy - ENZYME nomenclature database: 3.6.3.3
            ExplorEnz - The Enzyme Database: 3.6.3.3
            ERGO genome analysis and discovery system: 3.6.3.3
            BRENDA, the Enzyme Database: 3.6.3.3
///
ENTRY       EC 3.6.3.4                  Enzyme
NAME        Cu2+-exporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (Cu2+-exporting)
REACTION    ATP + H2O + Cu2+in = ADP + phosphate + Cu2+out [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            Cu2+ [CPD:C00070]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            Cu2+ [CPD:C00070]
COMMENT     A P-type ATPase that undergoes covalent phosphorylation during the
            transport cycle. This bacterial and mammalian enzyme exports Cu2+
            from cells. In humans, it is involved in Menkes disease and Wilson's
            disease.
REFERENCE   1  [PMID:8490659]
  AUTHORS   Vulpe C, Levinson B, Whitney S, Packman S, Gitschier J.
  TITLE     Isolation of a candidate gene for Menkes disease and evidence that
            it encodes a copper-transporting ATPase.
  JOURNAL   Nat. Genet. 3 (1993) 7-13.
REFERENCE   2  [PMID:7833924]
  AUTHORS   Petrukhin K, Lutsenko S, Chernov I, Ross BM, Kaplan JH, Gilliam TC.
  TITLE     Characterization of the Wilson disease gene encoding a P-type copper
            transporting ATPase: genomic organization, alternative splicing, and
            structure/function predictions.
  JOURNAL   Hum. Mol. Genet. 3 (1994) 1647-56.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:8151716]
  AUTHORS   Fagan MJ, Saier MH Jr.
  TITLE     P-type ATPases of eukaryotes and bacteria: sequence analyses and
            construction of phylogenetic trees.
  JOURNAL   J. Mol. Evol. 38 (1994) 57-99.
  ORGANISM  Enterococcus faecalis [GN:efa]
ORTHOLOGY   KO: K01533  Cu2+-exporting ATPase
GENES       HSA: 538(ATP7A) 540(ATP7B)
            MMU: 11977(Atp7a) 11979(Atp7b)
            RNO: 24218(Atp7b) 24941(Atp7a)
            CFA: 406185(ATP7A) 476903(ATP7B)
            BTA: 518075(LOC518075)
            GGA: 418879(ATP7B) 422333(ATP7A)
            DRE: 564924(atp7a)
            SPU: 592143(LOC592143)
            DME: Dmel_CG1886(ATP7)
            CEL: Y76A2A.2(cua-1)
            ATH: AT1G63440(HMA5) AT5G44790(RAN1)
            OSA: 4328448 4328616 4336625 4341778
            CME: CMP215C
            SCE: YBR295W(PCA1) YDR270W(CCC2)
            AGO: AGOS_ACR086C
            PIC: PICST_28495(CCC2.1) PICST_82776(CCC2.3) PICST_84044(CCC2.2)
            SPO: SPBC29A3.01
            ANI: AN3624.2
            AFM: AFUA_1G16130 AFUA_3G12740 AFUA_4G12620
            AOR: AO090009000330 AO090038000187
            UMA: UM00227.1 UM01019.1
            DDI: DDBDRAFT_0218568
            TET: TTHERM_00529920
            TBR: Tb11.47.0023
            TCR: 503703.50 511445.160
            LMA: LmjF33.2090
            ECO: b0484(copA)
            ECJ: JW0473(copA)
            ECE: Z0604(ybaR)
            ECS: ECs0537
            ECC: c0604(ybaR)
            ECI: UTI89_C0515(ybaR)
            ECP: ECP_0548 ECP_0549
            ECW: EcE24377A_0523(copA)
            ECX: EcHS_A0563(copA)
            STY: STY0544(ybaR)
            STT: t2362(ybaR)
            SPT: SPA2224(ybaR)
            SEC: SC0539(copA)
            STM: STM0498(copA)
            YPE: YPO3086(ybaR)
            YPK: y1093
            YPM: YP_0838(zntA1)
            YPA: YPA_2581
            YPN: YPN_1003
            YPS: YPTB1022(ATCU)
            YPI: YpsIP31758_3027
            SFL: SF0429(ybaR)
            SFX: S0436(ybaR)
            SFV: SFV_0457(ybaR)
            SSN: SSON_0473(ybaR)
            SBO: SBO_0386(ybaR)
            SDY: SDY_0434(ybaR)
            ECA: ECA1193(copA)
            PLU: plu3824(copA)
            SGL: SG1853
            HIN: HI0290
            HIT: NTHI0399
            PMU: PM1892
            MSU: MS0888(zntA)
            APL: APL_1265(copA)
            XCV: XCV2336(copA)
            VCH: VC2215
            VVU: VV1_0239
            VVY: VV0944
            VPA: VP0758
            VFI: VF0781 VF1304 VF1305
            PPR: PBPRA2824(copA)
            PAE: PA3920
            PAP: PSPA7_1187 PSPA7_3783
            PPU: PP_0586
            PST: PSPTO_0750
            PSB: Psyr_0654
            PSP: PSPPH_3346 PSPPH_4643
            PFL: PFL_0710
            PFO: Pfl_0661
            PEN: PSEEN0669 PSEEN1796
            PAR: Psyc_1587 Psyc_1637
            PCR: Pcryo_1777
            ACI: ACIAD2400(copA)
            SON: SO_1689
            SDN: Sden_3691
            SFR: Sfri_0212
            SHN: Shewana3_2761 Shewana3_4145
            ILO: IL0596 IL1218
            CPS: CPS_1916 CPS_1990
            PHA: PSHAa1011(copAB) PSHAa1847
            PAT: Patl_2091
            CBU: CBU_1507
            LPN: lpg0231 lpg2691
            LPF: lpl0284 lpl2618
            LPP: lpp0301 lpp2745
            MCA: MCA0805 MCA2072
            TCX: Tcr_0943 Tcr_2110
            NOC: Noc_0205 Noc_1533
            HCH: HCH_02269 HCH_06735
            CSA: Csal_3006
            ABO: ABO_2353(copA)
            AHA: AHA_2300 AHA_4222(copA)
            NME: NMB1325
            NMA: NMA1539
            NGO: NGO0579
            CVI: CV_1265(copA) CV_2042 CV_2748
            RSO: RSc3348(RS02623)
            REU: Reut_A1234 Reut_A3376 Reut_C6196
            REH: H16_A1976(copP1) H16_A1986(silP) H16_A2173(copF)
                 H16_A2321(zntA) H16_A3668(copP2) H16_B1644(cadA)
            RME: Rmet_2046 Rmet_3524
            BMA: BMA3368 BMAA1851
            BMV: BMASAVP1_0854 BMASAVP1_A3038
            BML: BMA10299_1144 BMA10299_A2054
            BMN: BMA10247_2230 BMA10247_A2119
            BUR: Bcep18194_B0162 Bcep18194_B0449 Bcep18194_B2381
            BCN: Bcen_5366
            BCH: Bcen2424_5494
            BPS: BPSS0224
            BPM: BURPS1710b_0506(silP) BURPS1710b_A1755(cueA)
            BPL: BURPS1106A_0324
            BPD: BURPS668_0311
            BTE: BTH_I0283 BTH_II2168
            BPE: BP2860
            BPA: BPP0968
            BBR: BB1180
            RFR: Rfer_0024 Rfer_1927
            POL: Bpro_4307 Bpro_4872
            MPT: Mpe_A1640(copF) Mpe_A2479 Mpe_A3535
            HAR: HEAR1562(copA) HEAR1625(kdpB) HEAR1648 HEAR3297
            NEU: NE1019(copA)
            NMU: Nmul_A2276
            EBA: ebA5128 ebA5154(copA)
            AZO: azo1355(copA) azo2956
            DAR: Daro_0711 Daro_1051 Daro_1836 Daro_2267
            TBD: Tbd_2044 Tbd_2266 Tbd_2740
            MFA: Mfla_0938 Mfla_1082
            HPY: HP1072(copA)
            HPJ: jhp0353(copA)
            HPA: HPAG1_0375
            HHE: HH0682
            HAC: Hac_1182(copA) Hac_1183(copP)
            TDN: Tmden_1223
            CJR: CJE1295
            CJJ: CJJ81176_1176
            CFF: CFF8240_1420
            CCV: CCV52592_0267 CCV52592_0531
            CHA: CHAB381_1116
            ABU: Abu_0480 Abu_0546 Abu_0711
            NIS: NIS_0505 NIS_1452
            SUN: SUN_0801 SUN_1930
            GSU: GSU2452
            GME: Gmet_2772
            PCA: Pcar_1596 Pcar_1712
            DVU: DVU2324
            DDE: Dde_0495 Dde_0498 Dde_1313
            LIP: LI1125(copA)
            BBA: Bd2224(copA)
            DPS: DP1471
            SAT: SYN_01290 SYN_02351
            MES: Meso_3893
            SME: SMa1013(actP) SMb21578(atcU2)
            ATU: Atu0937 Atu1195
            ATC: AGR_C_1708 AGR_C_2202
            RET: RHE_PE00007(actP)
            RLE: RL1871 RL1892 pRL110010 pRL110331
            BME: BMEI1730
            BMS: BR0220
            BMB: BruAb1_0215
            BOV: BOV_0212
            BRA: BRADO0147(actP)
            BBT: BBta_0206(actP) BBta_p0056(actP)
            RPD: RPD_2308
            NWI: Nwi_0911
            SIL: SPO0794 SPO3520 SPOA0365
            SIT: TM1040_2080 TM1040_2538
            RSP: RSP_0690(rdxI) RSP_2890
            RDE: RD1_1276(rdxI) RD1_2303
            HNE: HNE_1226 HNE_1483 HNE_1700
            ZMO: ZMO0915(copA)
            GOX: GOX0662
            GBE: GbCGDNIH1_2088 GbCGDNIH1_2089
            RRU: Rru_A1894 Rru_A3324
            MAG: amb1807 amb2911
            MGM: Mmc1_1003 Mmc1_2360
            BSU: BG14106(yvgX)
            BHA: BH0557
            BAN: BA3859
            BAR: GBAA3859
            BAA: BA_4334
            BAT: BAS3575
            BCE: BC3730
            BCA: BCE_3758 BCE_A0182
            BCZ: BCZK3487
            BTK: BT9727_3475
            BLI: BL01899(copA)
            BLD: BLi03553(yvgX)
            BCL: ABC0224 ABC3231
            OIH: OB1142
            GKA: GK0902
            SAU: SA2344(copA)
            SAV: SAV2557(copA)
            SAM: MW2478(copA)
            SAR: SAR2637(copA)
            SAS: SAS2443
            SAC: SACOL2572
            SAB: SAB2431(copA)
            SAA: SAUSA300_0078(copA) SAUSA300_2494
            SAO: SAOUHSC_02873
            SEP: SE2119
            SER: SERP2131
            SHA: SH0496(copA)
            SSP: SSP0297
            LMO: lmo1853
            LMF: LMOf2365_1881
            LIN: lin1967
            LWE: lwe1872(copA)
            LLA: L45966(copA)
            LLC: LACR_0891 LACR_0920
            LLM: llmg_1729(copA)
            SPY: SPy_1715(copA)
            SPZ: M5005_Spy_1405(copA)
            SPM: spyM18_1724
            SPG: SpyM3_1491(copA)
            SPS: SPs0376
            SPH: MGAS10270_Spy1526(copA)
            SPI: MGAS10750_Spy1518(copA)
            SPJ: MGAS2096_Spy1431(copA)
            SPK: MGAS9429_Spy1407(copA)
            SPF: SpyM50386(copA)
            SPA: M6_Spy1454
            SPB: M28_Spy1448(copA)
            SPD: SPD_0635
            SAG: SAG0385
            SAN: gbs0421
            SAK: SAK_0459(copA)
            SMU: SMU.426(copA)
            STC: str1585(copA)
            STL: stu1585(copA)
            SSA: SSA_0140(ctpA)
            SGO: SGO_1934
            LAC: LBA1966(copA)
            LSA: LSA1428 LSA1460(atkB)
            LSL: LSL_1704
            LBR: LVIS_0273
            EFA: EF0298
            STH: STH2616
            CAC: CAC3655
            CPE: CPE0555
            CPF: CPF_0534
            CNO: NT01CX_0757 NT01CX_2320
            CBA: CLB_1332
            CBH: CLC_1342
            CBF: CLI_1389
            CKL: CKL_0796(actP)
            CHY: CHY_0940
            DSY: DSY2564 DSY4510
            SWO: Swol_1698
            TTE: TTE2463(zntA)
            MTA: Moth_1994
            MPE: MYPE8710 MYPE8720
            UUR: UU203(copA)
            MAV: MAV_5246
            MSM: MSMEG_5014
            CGL: NCgl2859(cgl2962)
            CGB: cg3281
            CEF: CE0281
            CDI: DIP0061
            CJK: jk1429(copB)
            NFA: pnf1280 pnf1850
            RHA: RHA1_ro01231(kdpB) RHA1_ro03539 RHA1_ro11210
            CMI: CMM_1037(copA)
            AAU: AAur_4095 AAur_pTC10132 AAur_pTC10139 AAur_pTC20028
                 AAur_pTC20165
            FRA: Francci3_0490
            SEN: SACE_6088(kdpB)
            BLO: BL0409(silP)
            BAD: BAD_1301(actP)
            FNU: FN0245
            RBA: RB334
            PCU: pc0078(copA)
            TDE: TDE0008
            LIL: LA0594(atc)
            LIC: LIC12982
            LBJ: LBJ_0589
            LBL: LBL_2491
            SYG: sync_2594
            SYR: SynRCC307_0253(copA)
            SYX: SynWH7803_2245(copA)
            CYA: CYA_2372 CYA_2871
            CYB: CYB_1481 CYB_2346
            GVI: glr4047
            AVA: Ava_0992 Ava_1548 Ava_3848 Ava_4235 Ava_5064
            PMB: A9601_01481(zntA)
            PMC: P9515_01591(zntA)
            PMF: P9303_26501(zntA)
            PMG: P9301_01501(zntA)
            PMH: P9215_01481(zntA)
            PME: NATL1_02031(zntA)
            SRU: SRU_1594
            CHU: CHU_1499(copA)
            GFO: GFO_1184 GFO_1342 GFO_2935
            FJO: Fjoh_2536
            CCH: Cag_0959 Cag_1369
            PLT: Plut_1230
            DET: DET0953
            DEH: cbdb_A908
            DGE: Dgeo_2575
            TTH: TTC1371
            TTJ: TTHA1733
            MJA: MJ0968(copA)
            MAC: MA0166 MA1342
            MBA: Mbar_A0818 Mbar_A1889
            MMA: MM_1463 MM_2328
            MBU: Mbur_0612
            MSI: Msm_1153 Msm_1252
            AFU: AF0152(copB)
            HAL: VNG0700G(yvgX)
            HMA: pNG6046(copA3) pNG6056(copA2) rrnAC0504(copA4)
            NPH: NP2668A(tpa01)
            RCI: RCIX1517(copA) RRC473(copB)
            SAI: Saci_0872(actP)
STRUCTURES  PDB: 1JWW  1KQK  1KVI  1KVJ  1OPZ  1OQ3  1OQ6  1P6T  1S6O  1S6U  
                 1Y3J  1Y3K  1YJR  1YJT  1YJU  1YJV  2ARF  2EW9  2G9O  2GA7  
                 2GGP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.4
            ExPASy - ENZYME nomenclature database: 3.6.3.4
            ExplorEnz - The Enzyme Database: 3.6.3.4
            ERGO genome analysis and discovery system: 3.6.3.4
            BRENDA, the Enzyme Database: 3.6.3.4
///
ENTRY       EC 3.6.3.5                  Enzyme
NAME        Zn2+-exporting ATPase;
            Zn(II)-translocating P-type ATPase;
            P1B-type ATPase;
            AtHMA4
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (Zn2+-exporting)
REACTION    ATP + H2O + Zn2+in = ADP + phosphate + Zn2+out [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            Zn2+ [CPD:C00038]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            Zn2+ [CPD:C00038]
COMMENT     A P-type ATPase that undergoes covalent phosphorylation during the
            transport cycle. This enzyme also exports Cd2+ and Pb2+.
REFERENCE   1  [PMID:9364914]
  AUTHORS   Beard SJ, Hashim R, Membrillo-Hernandez J, Hughes MN, Poole RK.
  TITLE     Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA
            gene (o732) encodes a cation transport ATPase.
  JOURNAL   Mol. Microbiol. 25 (1997) 883-91.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:9405611]
  AUTHORS   Rensing C, Mitra B, Rosen BP.
  TITLE     The zntA gene of Escherichia coli encodes a Zn(II)-translocating
            P-type ATPase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 14326-31.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:9830000]
  AUTHORS   Rensing C, Sun Y, Mitra B, Rosen BP.
  TITLE     Pb(II)-translocating P-type ATPases.
  JOURNAL   J. Biol. Chem. 273 (1998) 32614-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:15670847]
  AUTHORS   Mills RF, Francini A, Ferreira da Rocha PS, Baccarini PJ, Aylett M,
            Krijger GC, Williams LE.
  TITLE     The plant P1B-type ATPase AtHMA4 transports Zn and Cd and plays a
            role in detoxification of transition metals supplied at elevated
            levels.
  JOURNAL   FEBS. Lett. 579 (2005) 783-91.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   5  [PMID:15475410]
  AUTHORS   Eren E, Arguello JM.
  TITLE     Arabidopsis HMA2, a divalent heavy metal-transporting P(IB)-type
            ATPase, is involved in cytoplasmic Zn2+ homeostasis.
  JOURNAL   Plant. Physiol. 136 (2004) 3712-23.
  ORGANISM  Arabidopsis thaliana [GN:ath]
ORTHOLOGY   KO: K01534  Zn2+-exporting ATPase
GENES       ATH: AT2G19110(HMA4) AT4G30110(HMA2)
            ECO: b3469(zntA)
            ECJ: JW3434(zntA)
            ECE: Z4843(zntA)
            ECS: ECs4318
            ECC: c4262(zntA)
            ECI: UTI89_C3984(zntA)
            ECP: ECP_3562
            ECV: APECO1_2985(zntA)
            STY: STY4235
            STT: t3946
            SPT: SPA3427(zntA)
            SEC: SC3505(zntA)
            STM: STM3576(zntA)
            YPE: YPO3820
            YPK: y0410(zntA)
            YPM: YP_3228(zntA2)
            YPA: YPA_0202
            YPN: YPN_0144
            YPS: YPTB0215(ATZN)
            SFL: SF3487(zntA)
            SFX: S4276(zntA)
            SFV: SFV_3472(zntA)
            SBO: SBO_3466(zntA)
            SDY: SDY_3620(zntA)
            ECA: ECA4352(zntA)
            PLU: plu4108(zntA)
            VCH: VC1033
            VVU: VV1_2063
            VVY: VV2378
            VPA: VP0959
            VFI: VF1522
            PPR: PBPRA1220
            AHA: AHA_0629
            HPY: HP0791(cadA)
            HPJ: jhp0727(hmcT)
            HHE: HH0586
            HAC: Hac_0913(yvgW)
            ABU: Abu_1859
            LIP: LI0598(zntA)
            RLE: RL4262
            BCE: BC0596
            LSL: LSL_1639
            CDF: CD0313
            CBO: CBO0478
            DSY: DSY4631
            MTA: Moth_2203
            FNU: FN0258 FN0259
            SYN: slr0798(ziaA)
            MSI: Msm_1127
            SMR: Smar_0594
STRUCTURES  PDB: 1MWY  1MWZ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.5
            ExPASy - ENZYME nomenclature database: 3.6.3.5
            ExplorEnz - The Enzyme Database: 3.6.3.5
            ERGO genome analysis and discovery system: 3.6.3.5
            BRENDA, the Enzyme Database: 3.6.3.5
///
ENTRY       EC 3.6.3.6                  Enzyme
NAME        H+-exporting ATPase;
            proton-translocating ATPase;
            yeast plasma membrane H+-ATPase;
            yeast plasma membrane ATPase;
            ATP phosphohydrolase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (H+-exporting)
REACTION    ATP + H2O + H+in = ADP + phosphate + H+out [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            H+ [CPD:C00080]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            H+ [CPD:C00080]
COFACTOR    H+ [CPD:C00080]
COMMENT     A P-type ATPase that undergoes covalent phosphorylation during the
            transport cycle. This enzyme occurs in protozoa, fungi and plants,
            and generates an electrochemical potential gradient of protons
            across the plasma membrane.
REFERENCE   1  [PMID:6461354]
  AUTHORS   Goffeau A, Slayman CW.
  TITLE     The proton-translocating ATPase of the fungal plasma membrane.
  JOURNAL   Biochim. Biophys. Acta. 639 (1981) 197-223.
REFERENCE   2  [PMID:3005867]
  AUTHORS   Serrano R, Kielland-Brandt MC, Fink GR.
  TITLE     Yeast plasma membrane ATPase is essential for growth and has
            homology with (Na+ + K+), K+- and Ca2+-ATPases.
  JOURNAL   Nature. 319 (1986) 689-93.
REFERENCE   3  [PMID:2144186]
  AUTHORS   Serrano R, Portillo F.
  TITLE     Catalytic and regulatory sites of yeast plasma membrane H(+)-ATPase
            studied by directed mutagenesis.
  JOURNAL   Biochim. Biophys. Acta. 1018 (1990) 195-9.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00190  Oxidative phosphorylation
ORTHOLOGY   KO: K01535  H+-transporting ATPase
GENES       DME: Dmel_CG1709(Vha100-1) Dmel_CG18617(Vha100-2)
                 Dmel_CG8048(Vha44)
            ATH: AT1G17260(AHA10) AT1G80660(AHA9) AT2G07560(AHA6)
                 AT2G18960(AHA1) AT2G24520(AHA5) AT3G42640(AHA8)
                 AT3G47950(AHA4) AT3G60330(AHA7) AT4G30190(AHA2)
                 AT5G57350(AHA3) AT5G62670(AHA11)
            OSA: 4324470 4331281 4331853 4333770 4337257 4338405 4342621
                 4352910
            CME: CMQ247C
            SCE: YGL008C(PMA1) YPL036W(PMA2)
            AGO: AGOS_AGL085C
            PIC: PICST_69588(CUP5) PICST_87366(PMA1)
            CGR: CAGL0A00495g
            SPO: SPAC1071.10c(pma1)
            ANI: AN4859.2
            AFM: AFUA_1G02480 AFUA_3G07640 AFUA_5G03550
            AOR: AO090005000842 AO090020000403 AO090102000565
            CNE: CNG00380 CNN01260
            UMA: UM02581.1
            DDI: DDB_0214946(patB)
            TET: TTHERM_01149330
            TBR: Tb10.389.1170 Tb10.389.1180 Tb927.5.3400
            TCR: 506649.20 511277.240
            LMA: LmjF18.1510 LmjF18.1520
            BXE: Bxe_A3829 Bxe_B1515
            NIS: NIS_0930
            SUN: SUN_1289
            GME: Gmet_3497
            DPS: DP0982
            RRU: Rru_A2263
            LCA: LSEI_0125
            RHA: RHA1_ro01842
            MJA: MJ1226(aha1)
            MAE: Maeo_0802
            MVN: Mevan_1344
            MAC: MA1678 MA2833
            MTH: MTH481 MTH482
            TAC: Ta1045
            TPE: Tpen_1427
STRUCTURES  PDB: 1MHS  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.6
            ExPASy - ENZYME nomenclature database: 3.6.3.6
            ExplorEnz - The Enzyme Database: 3.6.3.6
            ERGO genome analysis and discovery system: 3.6.3.6
            BRENDA, the Enzyme Database: 3.6.3.6
///
ENTRY       EC 3.6.3.7                  Enzyme
NAME        Na+-exporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (Na+-exporting)
REACTION    ATP + H2O + Na+in = ADP + phosphate + Na+out [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            Na+ [CPD:C01330]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            Na+ [CPD:C01330]
COMMENT     A P-type ATPase that undergoes covalent phosphorylation during the
            transport cycle. This enzyme from yeast is involved in the efflux of
            Na+, with one ion being exported per ATP hydrolysed.
REFERENCE   1  [PMID:7664728]
  AUTHORS   Wieland J, Nitsche AM, Strayle J, Steiner H, Rudolph HK.
  TITLE     The PMR2 gene cluster encodes functionally distinct isoforms of a
            putative Na+ pump in the yeast plasma membrane.
  JOURNAL   EMBO. J. 14 (1995) 3870-82.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:9224683]
  AUTHORS   Catty P, de Kerchove d'Exaerde A, Goffeau A.
  TITLE     The complete inventory of the yeast Saccharomyces cerevisiae P-type
            transport ATPases.
  JOURNAL   FEBS. Lett. 409 (1997) 325-32.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:9106203]
  AUTHORS   Cheng J, Guffanti AA, Krulwich TA.
  TITLE     A two-gene ABC-type transport system that extrudes Na+ in Bacillus
            subtilis is induced by ethanol or protonophore.
  JOURNAL   Mol. Microbiol. 23 (1997) 1107-20.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   4  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
ORTHOLOGY   KO: K01536  Na+-exporting ATPase
GENES       SCE: YDR039C(ENA2)
            CGR: CAGL0K12034g
            AFM: AFUA_2G01320 AFUA_4G09440 AFUA_6G03690
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.7
            ExPASy - ENZYME nomenclature database: 3.6.3.7
            ExplorEnz - The Enzyme Database: 3.6.3.7
            ERGO genome analysis and discovery system: 3.6.3.7
            BRENDA, the Enzyme Database: 3.6.3.7
///
ENTRY       EC 3.6.3.8                  Enzyme
NAME        Ca2+-transporting ATPase;
            sarcoplasmic reticulum ATPase;
            sarco(endo)plasmic reticulum Ca2+-ATPase;
            calcium pump;
            Ca2+-pumping ATPase;
            plasma membrane Ca-ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (Ca2+-transporting)
REACTION    ATP + H2O + Ca2+cis = ADP + phosphate + Ca2+trans [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            Ca2+ [CPD:C00076]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            Ca2+ [CPD:C00076]
COFACTOR    Calcium [CPD:C00076];
            Vanadate [CPD:C00754]
COMMENT     A P-type ATPase that undergoes covalent phosphorylation during the
            transport cycle. This enzyme family comprises three types of
            Ca2+-transporting enzymes that are found in the plasma membrane, the
            sarcoplasmic reticulum and in yeast. The first and third transport
            one ion per ATP hydrolysed, whereas the second transports two ions.
REFERENCE   1  [PMID:4238381]
  AUTHORS   Schatzmann HJ, Vincenzi FF.
  TITLE     Calcium movements across the membrane of human red cells.
  JOURNAL   J. Physiol. 201 (1969) 369-95.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:6301340]
  AUTHORS   Inesi G, Watanabe T, Coan C, Murphy A.
  TITLE     The mechanism of sarcoplasmic reticulum ATPase.
  JOURNAL   Ann. N. Y. Acad. Sci. 402 (1982) 515-34.
REFERENCE   3  [PMID:1310307]
  AUTHORS   Carafoli E.
  TITLE     The Ca2+ pump of the plasma membrane.
  JOURNAL   J. Biol. Chem. 267 (1992) 2115-8.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:9360942]
  AUTHORS   MacLennan DH, Rice WJ, Green NM.
  TITLE     The mechanism of Ca2+ transport by sarco(endo)plasmic reticulum
            Ca2+-ATPases.
  JOURNAL   J. Biol. Chem. 272 (1997) 28815-8.
PATHWAY     PATH: map04020  Calcium signaling pathway
ORTHOLOGY   KO: K01537  Ca2+-transporting ATPase
            KO: K05850  Ca2+ transporting ATPase, plasma membrane
            KO: K05853  Ca2+ transporting ATPase, sarcoplasmic/endoplasmic
                        reticulum
GENES       HSA: 27032(ATP2C1) 487(ATP2A1) 488(ATP2A2) 489(ATP2A3) 490(ATP2B1)
                 491(ATP2B2) 492(ATP2B3) 493(ATP2B4) 9914(ATP2C2)
            MMU: 11937(Atp2a1) 11938(Atp2a2) 11941(Atp2b2) 235574(Atp2c1)
                 320707(Atp2b3) 381290(Atp2b4) 53313(Atp2a3) 67972(Atp2b1)
                 69047(Atp2c2)
            RNO: 116601(Atp2a1) 170699(Atp2c1) 171496(Atp2c2) 24215(Atp2b2)
                 25391(Atp2a3) 29598(Atp2b1) 29599(Atp2b3) 29600(Atp2b4)
                 29693(Atp2a2)
            CFA: 403480(ATP2B1) 403731(ATP2B4) 403878(ATP2A2) 476535(ATP2B2)
                 479626(ATP2C2) 479797(ATP2A1) 491437(ATP2A3) 492238(ATP2B3)
            BTA: 282641(ATP2B1) 327663(ATP2C1)
            SSC: 396875(SERCA2) 397636(ATP2B1)
            GGA: 374244(ATP2B1) 395707(ATP2A3) 396446(ATP2A2) 396528(ATP2A1)
                 415958(ATP2B2) 419934(ATP2B4) 428450(ATP2C1)
            XLA: 380096(ca-p60a) 446855(atp2b3) 495440(LOC495440)
            DRE: 260440(atp2a1) 393940(atp2a2a)
            SPU: 577733(SPCA) 580345(PMCA) 581565(SERCA)
            DME: Dmel_CG11111(rdgB) Dmel_CG32451(SPoCk) Dmel_CG3725(Ca-P60A)
            CEL: R05C11.3(ATPase) Y67D8C.10(mca-3)
            ATH: AT1G07670 AT1G07810(ECA1) AT1G10130(ECA3) AT2G22950
                 AT2G41560(ACA4) AT3G21180(ACA9) AT3G22910 AT3G57330 AT3G63380
                 AT4G00900(ECA2) AT4G29900(ACA10) AT4G37640(ACA2)
            OSA: 4331984 4332447 4333451 4333998 4336912 4339199 4351449
            CME: CMM114C CMQ379C CMT241C
            SCE: YGL006W(PMC1) YGL167C(PMR1)
            AGO: AGOS_AEL301W AGOS_AFL011W
            PIC: PICST_29627(SPF1.2) PICST_33744(SPF1.3) PICST_60393(SPF1)
                 PICST_64379(PMR1) PICST_73371(ENA5) PICST_74899(ENA2)
                 PICST_81376(PMC1) PICST_85147(DNF1)
            CAL: CaO19_6070(CaO19.6070)
            CGR: CAGL0A00517g CAGL0I04312g
            SPO: SPAPB2B4.04c SPBC31E1.02c(pgak2) SPBC839.06(cta3)
            ANI: AN1189.2 AN4920.2 AN5743.2 AN7464.2
            AFM: AFUA_1G10880 AFUA_2G05860 AFUA_3G10690 AFUA_6G06740
                 AFUA_7G01030
            AOR: AO090001000706 AO090003000051 AO090003000614 AO090038000322
            CNE: CND03510 CNH02370 CNL04860 CNL04870
            UMA: UM00204.1 UM03470.1 UM04461.1
            DDI: DDB_0233095
            PFA: MAL1P1.54
            CPV: cgd7_4190
            CHO: Chro.70464
            TAN: TA13655
            TPV: TP02_0524
            TET: TTHERM_00249700 TTHERM_00249720 TTHERM_00249760
                 TTHERM_00249790 TTHERM_00249810 TTHERM_00265100
                 TTHERM_00387080 TTHERM_00463790 TTHERM_00575480
                 TTHERM_00575510 TTHERM_00666630 TTHERM_00688500
                 TTHERM_00696910 TTHERM_00913380 TTHERM_00923150
                 TTHERM_00923170 TTHERM_01084370
            TBR: Tb10.26.0290 Tb927.8.1200
            TCR: 509777.70
            LMA: LmjF04.0010 LmjF07.0630
            EHI: 133.t00029 173.t00001 429.t00006 440.t00003 55.t00037
            SPE: Spro_0841
            ASU: Asuc_0261
            PPF: Pput_4088
            PMY: Pmen_0425 Pmen_3015
            PRW: PsycPRwf_1981
            SBM: Shew185_3126
            SSE: Ssed_1300
            SPL: Spea_1195
            LPN: lpg1126
            NOC: Noc_1406 Noc_2130
            MMW: Mmwyl1_3732
            REH: H16_A2023
            HAR: HEAR1578
            NMU: Nmul_A0037 Nmul_A1648
            GUR: Gura_0219
            DDE: Dde_1893
            AFW: Anae109_0456 Anae109_3750
            SAT: SYN_00872 SYN_01009 SYN_02218 SYN_02485
            PLA: Plav_2578
            SMD: Smed_1522
            RLE: RL1869
            OAN: Oant_1986
            BBT: BBta_0672
            RPE: RPE_2585
            XAU: Xaut_4080
            RSQ: Rsph17025_2373
            SWI: Swit_0512
            ACR: Acry_1034
            BCE: BC0448
            BCY: Bcer98_2431
            SAJ: SaurJH9_1345
            SAH: SaurJH1_1371
            SPZ: M5005_Spy_0516(pacL)
            SPH: MGAS10270_Spy0510(pacL)
            SPI: MGAS10750_Spy0535(pacL)
            SPJ: MGAS2096_Spy0528(pacL)
            SPK: MGAS9429_Spy0507(pacL)
            SPA: M6_Spy0537
            SMU: SMU.723
            SSA: SSA_0866(pacL)
            LSL: LSL_1602
            LRE: Lreu_0523
            CPR: CPR_0311
            CTC: CTC01647 CTC02043
            CNO: NT01CX_0593 NT01CX_1929
            CDF: CD1824 CD2503
            CBO: CBO0532 CBO1545
            CBA: CLB_0572
            CBH: CLC_0456
            CBF: CLI_0611
            CBE: Cbei_1216
            AMT: Amet_2658
            CSC: Csac_2138
            MVA: Mvan_1651
            RHA: RHA1_ro03758
            KRA: Krad_1492
            STP: Strop_1425
            FNU: FN1021 FN1022
            CYA: CYA_1658
            CYB: CYB_1641
            AVA: Ava_1901 Ava_3392 Ava_3557 Ava_3565 Ava_4083 Ava_4087
                 Ava_4900 Ava_B0106
            BFS: BF4149
            CHU: CHU_1415(pacL)
            FJO: Fjoh_0988 Fjoh_4474
            CCH: Cag_1142
            DEB: DehaBAV1_1352
            RRS: RoseRS_3118
            RCA: Rcas_2960
            TPT: Tpet_0938
            TME: Tmel_1158
            FNO: Fnod_1291
            MMQ: MmarC5_1088
            MMZ: MmarC7_1540
            MTP: Mthe_1471
            MHU: Mhun_0342 Mhun_2663
STRUCTURES  PDB: 1KJU  1SU4  1T5S  1T5T  1VFP  1WPG  1XP5  2AGV  2BY4  2C88  
                 2C8K  2C8L  2C9M  2DQS  2EAR  2EAS  2EAT  2EAU  2O9J  2OA0  
                 2Z9R  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.8
            ExPASy - ENZYME nomenclature database: 3.6.3.8
            ExplorEnz - The Enzyme Database: 3.6.3.8
            ERGO genome analysis and discovery system: 3.6.3.8
            BRENDA, the Enzyme Database: 3.6.3.8
///
ENTRY       EC 3.6.3.9                  Enzyme
NAME        Na+/K+-exchanging ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (Na+/K+-exchanging)
REACTION    ATP + H2O + Na+in + K+out = ADP + phosphate + Na+out + K+in
            [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            Na+ [CPD:C01330];
            K+ [CPD:C00238]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            Na+ [CPD:C01330];
            K+ [CPD:C00238]
COFACTOR    Potassium [CPD:C00238];
            Magnesium [CPD:C00305];
            Sodium [CPD:C01330]
INHIBITOR   Ouabain [CPD:C01443];
            GTP-gamma-S [CPD:C01806]
COMMENT     A P-type ATPase that undergoes covalent phosphorylation during the
            transport cycle. This is a plasma membrane enzyme, ubiquitous in
            animal cells, that catalyses the efflux of three Na+ and influx of
            two K+ per ATP hydrolysed. It is involved in generating the plasma
            membrane electrical potential.
REFERENCE   1
  AUTHORS   Skou, J.C.
  TITLE     The influence of some cations on an adenosinetriphosphatase from
            peripheral nerve.
  JOURNAL   Biochim. Biophys. Acta 23 (1957) 394-401.
REFERENCE   2
  AUTHORS   Post, R.L., Sen, A.K. and Rosenthal, A.S.
  TITLE     A phosphorylated intermediate in adenosine triphosphate-dependent
            sodium and potassium transport across kidney membrane.
  JOURNAL   J. Biol. Chem. 240 (1965) 1437-1445.
  ORGANISM  guinea pig
REFERENCE   3  [PMID:2166689]
  AUTHORS   Skou JC.
  TITLE     The fourth Datta lecture. The energy coupled exchange of Na+ for K+
            across the cell membrane. The Na+, K(+)-pump.
  JOURNAL   FEBS. Lett. 268 (1990) 314-24.
ORTHOLOGY   KO: K01538  Na+/K+-exchanging ATPase
            KO: K01539  Na+/K+-exchanging ATPase alpha subunit
            KO: K01540  Na+/K+-exchanging ATPase beta subunit
GENES       HSA: 23439(ATP1B4) 476(ATP1A1) 477(ATP1A2) 478(ATP1A3) 480(ATP1A4)
                 481(ATP1B1) 482(ATP1B2) 483(ATP1B3)
            PTR: 470951(LOC470951) 746692(ATP1B3)
            MCC: 710368(ATP1A1)
            MMU: 11928(Atp1a1) 11931(Atp1b1) 11933(Atp1b3) 232975(Atp1a3)
                 67821(Atp1b4) 98660(Atp1a2)
            RNO: 24211(Atp1a1) 24212(Atp1a2) 24213(Atp1a3) 25390(Atp1b3)
                 25650(Atp1b1) 29132(Atp1a4) 84396(Atp1b4)
            CFA: 403966(ATP1B1) 403992(ATP1A1) 477098(ATP1B3) 481036(ATP1B4)
                 488636(ATP1A2) 488637(ATP1A4) 612463(ATP1A3)
            BTA: 282144(ATP1A1) 282598(ATP1A3) 532844(ATP1B3)
            SSC: 396898(ATP1B1) 397245(ATP1B4) 397481(ATP1A1)
            GGA: 396467(LOC396467) 396468(LOC396468) 396529(ATP1B1)
                 396530(ATP1A1) 396549(ATP1B3) 422365(ATP1B4)
            XLA: 380132(atp1a3) 397733(atpb-3) 398583(MGC53886)
                 398752(MGC68460) 399285(atp1a1a.1)
            XTR: 394687(atp1b3) 395044(atp1a1)
            DRE: 64267(atp1b1a) 64272(atp1b3b) 64273(atp1b1b) 64609(atp1a2a)
                 64610(atp1a3a) 64611(atp1a3b) 64612(atp1a1)
            SPU: 579450(LOC579450)
            DME: Dmel_CG17923 Dmel_CG3701 Dmel_CG5670(Atpalpha)
                 Dmel_CG8663(nrv3) Dmel_CG9258(nrv1) Dmel_CG9261(nrv2)
            CEL: B0365.3(eat-6) C01G12.8 C02E7.1 C17E4.9 F55F3.3
            PIC: PICST_60178(PMR2)
            AFM: AFUA_7G04570
            AOR: AO090005000141
            DDI: DDBDRAFT_0189650
            TET: TTHERM_00049030 TTHERM_00245100 TTHERM_00268190
                 TTHERM_00355800 TTHERM_00365390 TTHERM_00365450
                 TTHERM_00420900 TTHERM_00643550 TTHERM_00700900
                 TTHERM_00989440 TTHERM_01149330 TTHERM_01150350
                 TTHERM_01821940 TTHERM_02440130
            TCX: Tcr_1065
            DAR: Daro_1851
            PCA: Pcar_2279
            BRA: BRADO5828(kdpC) BRADO5829(kdpB) BRADO5830(kdpA)
            BBT: BBta_6336(kdpC) BBta_6337(kdpB) BBta_6338(kdpA)
            SEN: SACE_2424
            MAC: MA4378
            MBA: Mbar_A1053
            MMA: MM_1069
            MBU: Mbur_0431
STRUCTURES  PDB: 1MO7  1MO8  1Q3I  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.9
            ExPASy - ENZYME nomenclature database: 3.6.3.9
            ExplorEnz - The Enzyme Database: 3.6.3.9
            ERGO genome analysis and discovery system: 3.6.3.9
            BRENDA, the Enzyme Database: 3.6.3.9
///
ENTRY       EC 3.6.3.10                 Enzyme
NAME        H+/K+-exchanging ATPase;
            H+-K+-ATPase;
            H,K-ATPase;
            (K+ + H+)-ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (H+/K+-exchanging)
REACTION    ATP + H2O + H+in + K+out = ADP + phosphate + H+out + K+in
            [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            H+ [CPD:C00080];
            K+ [CPD:C00238]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            H+ [CPD:C00080];
            K+ [CPD:C00238]
COFACTOR    H+ [CPD:C00080];
            Potassium [CPD:C00238]
COMMENT     A P-type ATPase that undergoes covalent phosphorylation during the
            transport cycle. A gastric mucosal enzyme that catalyses the efflux
            of one H+ and the influx of one K+ per ATP hydrolysed.
REFERENCE   1  [PMID:5682852]
  AUTHORS   Sachs G, Collier RH, Shoemaker RL, Hirschowitz BI.
  TITLE     The energy source for gastric H+ secretion.
  JOURNAL   Biochim. Biophys. Acta. 162 (1968) 210-9.
  ORGANISM  frog
REFERENCE   2  [PMID:2552824]
  AUTHORS   Hersey SJ, Perez A, Matheravidathu S, Sachs G.
  TITLE     Gastric H+-K+-ATPase in situ: evidence for compartmentalization.
  JOURNAL   Am. J. Physiol. 257 (1989) G539-47.
  ORGANISM  rabbit
REFERENCE   3  [PMID:2158765]
  AUTHORS   Rabon EC, Reuben MA.
  TITLE     The mechanism and structure of the gastric H,K-ATPase.
  JOURNAL   Annu. Rev. Physiol. 52 (1990) 321-44.
PATHWAY     PATH: map00190  Oxidative phosphorylation
ORTHOLOGY   KO: K01541  H+/K+-exchanging ATPase
            KO: K01542  H+/K+-exchanging ATPase alpha polypeptide
            KO: K01543  H+/K+-exchanging ATPase beta polypeptide
            KO: K01544  H+/K+-exchanging ATPase c chain
GENES       HSA: 479(ATP12A) 495(ATP4A) 496(ATP4B)
            PTR: 452489(ATP12A)
            MMU: 11944(Atp4a) 11945(Atp4b) 192113(Atp12a)
            RNO: 171028(Atp12a) 24217(Atp4b)
            CFA: 403820(ATP12A) 404020(ATP4B) 431686(ATP4A)
            SSC: 397131(ATP4B) 397552(ATP4A)
            GGA: 386581(ATP4B) 419743(RCJMB04_25f22)
            XLA: 379283(MGC53249) 379459(MGC64342) 380512(atp12a)
            XTR: 448282(atp4b)
            PIC: PICST_60178(PMR2)
            CAL: CaO19_4328(CaO19.4328)
            AFM: AFUA_5G00730
            SPN: SP_2101
            SPR: spr0641(ctpA) spr1410(pacL) spr1911(ctpC)
            SSA: SSA_0866(pacL) SSA_2027(copA)
            SGO: SGO_0290 SGO_0291 SGO_1619
            CPE: CPE1202
            CTC: CTC00664
            CGB: cg0464(ctpA)
            CHU: CHU_1133(copA)
            MMA: MM_0910
            SSO: SSO2896
STRUCTURES  PDB: 1IWC  1IWF  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.10
            ExPASy - ENZYME nomenclature database: 3.6.3.10
            ExplorEnz - The Enzyme Database: 3.6.3.10
            ERGO genome analysis and discovery system: 3.6.3.10
            BRENDA, the Enzyme Database: 3.6.3.10
///
ENTRY       EC 3.6.3.11                 Enzyme
NAME        Cl--transporting ATPase;
            Cl--translocating ATPase;
            Cl--motive ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (Cl--importing)
REACTION    ATP + H2O + Cl-out = ADP + phosphate + Cl-in [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            Cl- [CPD:C00698]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            Cl- [CPD:C00698]
COMMENT     A P-type ATPase that undergoes covalent phosphorylation during the
            transport cycle. An animal and plant enzyme involved in the import
            of chloride anions.
REFERENCE   1  [PMID:1533790]
  AUTHORS   Ohhashi T, Katsu T, Ikeda M.
  TITLE     Improvement of reconstitution of the Cl(-)-translocating ATPase
            isolated from Acetabularia acetabulum into liposomes and several
            anion pump characteristics.
  JOURNAL   Biochim. Biophys. Acta. 1106 (1992) 165-70.
  ORGANISM  Acetabularia acetabulum
REFERENCE   2  [PMID:8953378]
  AUTHORS   Gerencser GA, Purushotham KR.
  TITLE     Reconstituted Cl- pump protein: a novel ion(Cl-)-motive ATPase.
  JOURNAL   J. Bioenerg. Biomembr. 28 (1996) 459-69.
  ORGANISM  Aplysia californica
REFERENCE   3  [PMID:8759922]
  AUTHORS   Inagaki C, Hara M, Zeng XT.
  TITLE     A Cl- pump in rat brain neurons.
  JOURNAL   J. Exp. Zool. 275 (1996) 262-8.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.11
            ExPASy - ENZYME nomenclature database: 3.6.3.11
            ExplorEnz - The Enzyme Database: 3.6.3.11
            ERGO genome analysis and discovery system: 3.6.3.11
            BRENDA, the Enzyme Database: 3.6.3.11
///
ENTRY       EC 3.6.3.12                 Enzyme
NAME        K+-transporting ATPase;
            K+-translocating Kdp-ATPase;
            multi-subunit K+-transport ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (K+-importing)
REACTION    ATP + H2O + K+out = ADP + phosphate + K+in [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            K+ [CPD:C00238]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            K+ [CPD:C00238]
COMMENT     A P-type ATPase that undergoes covalent phosphorylation during the
            transport cycle. A bacterial enzyme of di(heterotetrameric)
            structure that is involved in K+ import. The probable stoichiometry
            is one ion per ATP hydrolysed.
REFERENCE   1  [PMID:2522440]
  AUTHORS   Siebers A, Altendorf K.
  TITLE     Characterization of the phosphorylated intermediate of the
            K+-translocating Kdp-ATPase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 264 (1989) 5831-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:9858692]
  AUTHORS   Gassel M, Siebers A, Epstein W, Altendorf K.
  TITLE     Assembly of the Kdp complex, the multi-subunit K+-transport ATPase
            of Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 1415 (1998) 77-84.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K01545  K+-transporting ATPase ATPase
            KO: K01546  K+-transporting ATPase ATPase A chain
            KO: K01547  K+-transporting ATPase ATPase B chain
            KO: K01548  K+-transporting ATPase ATPase C chain
GENES       ECO: b0696(kdpC) b0697(kdpB) b0698(kdpA)
            ECJ: JW0684(kdpC) JW0685(kdpB) JW0686(kdpA)
            ECE: Z0843(kdpC) Z0844(kdpB) Z0845(kdpA)
            ECS: ECs0724 ECs0725 ECs0726
            ECC: c0781(kdpC) c0782(kdpB) c0783(kdpA)
            ECI: UTI89_C0700(kdpC) UTI89_C0701(kdpB) UTI89_C0702(kdpA)
            ECP: ECP_0715 ECP_0716 ECP_0717
            ECV: APECO1_1369(kdpA) APECO1_1370(kdpB) APECO1_1371(kdpC)
            ECW: EcE24377A_0722(kdpC) EcE24377A_0723(kdpB)
                 EcE24377A_0724(kdpA) EcE24377A_0725(kdpF)
            ECX: EcHS_A0743(kdpC) EcHS_A0744(kdpB) EcHS_A0745(kdpA)
                 EcHS_A0746(kdpF)
            STY: STY0745(kdpC) STY0746(kdpB) STY0747(kdpA)
            STT: t2169(kdpA) t2170(kdpB) t2171(kdpC)
            SPT: SPA2035(kdpA) SPA2036(kdpB) SPA2037(kdpC)
            SEC: SC0724(kdpC) SC0725(kdpB) SC0726(kdpA)
            STM: STM0704(kdpC) STM0705(kdpB) STM0706(kdpA)
            YPE: YPO2690(kdpC) YPO2691(kdpB) YPO2692(kdpA)
            YPK: y1263(kdpC) y1264(kdpB) y1265(kdpA)
            YPM: YP_2493(kdpC) YP_2494(kdpB) YP_2495(kdpA)
            YPA: YPA_2420 YPA_2421 YPA_2422
            YPN: YPN_1177 YPN_1178 YPN_1179
            YPP: YPDSF_1580 YPDSF_1582
            YPS: YPTB2916(kdpA) YPTB2917(kdpB) YPTB2918(kdpC)
            YPI: YpsIP31758_1104(kdpC) YpsIP31758_1106(kdpB)
                 YpsIP31758_1108(kdpA)
            SFL: SF0598(kdpA)
            SFX: S0609(kdpA) S0611(kdpC)
            SFV: SFV_0635(kdpA) SFV_0637(kdpC)
            SSN: SSON_0647(kdpC) SSON_0648(kdpB) SSON_0649(kdpA)
            SBO: SBO_0559(kdpB) SBO_0560(kdpA)
            SDY: SDY_0631(kdpC)
            ECA: ECA1340(kdpC) ECA1341(kdpB) ECA1342(kdpA)
            PLU: plu1418(kdpC) plu1419(kdpB) plu1420(kdpA)
            SGL: SG0327
            ENT: Ent638_1208 Ent638_1210
            KPN: KPN_00715(kdpC)
            SPE: Spro_1246 Spro_1248
            XCC: XCC0702(kdpA) XCC0703(kdpB) XCC0704(kdpC)
            XCB: XC_3530 XC_3531 XC_3532
            XCV: XCV0808(kdpA) XCV0809(kdpB) XCV0810(kdpC)
            XAC: XAC0756(kdpA) XAC0757(kdpB) XAC0758(kdpC)
            XOO: XOO3844(kdpC) XOO3845(kdpB) XOO3846(kdpA)
            XOM: XOO_3622(XOO3622) XOO_3623(XOO3623) XOO_3624(XOO3624)
            PAE: PA1633(kd) PA1634(kdpB) PA1635(kdpC)
            PAU: PA14_43370(kdpC) PA14_43380(kdpB) PA14_43400(kdpA)
            PAP: PSPA7_3638(kdpC2) PSPA7_3639(kdpB2) PSPA7_3640(kdpA2)
                 PSPA7_3712(kdpA1) PSPA7_3713(kdpB1) PSPA7_3714(kdpC1)
            PPU: PP_4159(kdpC) PP_4161(kdpA)
            PPF: Pput_1707 Pput_1709
            PST: PSPTO_2242(kdpA) PSPTO_2243(kdpB) PSPTO_2244(kdpC)
            PSB: Psyr_2047 Psyr_2048 Psyr_2049
            PSP: PSPPH_2016 PSPPH_2017(kdpA) PSPPH_2018(kdpB) PSPPH_2019
                 PSPPH_2020(kdpC)
            PFL: PFL_4295(kdpC) PFL_4296(kdpB) PFL_4297(kdpA) PFL_4571(kdpB)
                 PFL_4572(kdpC) PFL_4573(kdpA) PFL_4575(kdpF)
            PFO: Pfl_4031 Pfl_4032 Pfl_4033
            PEN: PSEEN3607(kdpC) PSEEN3608(kdpB) PSEEN3609(kdpA)
            ACI: ACIAD2976(kdpC) ACIAD2977(kdpB) ACIAD2978(kdpA)
            SPC: Sputcn32_3080 Sputcn32_3082
            SHW: Sputw3181_0862
            MCA: MCA2215(kdpC) MCA2216(kdpB) MCA2217(kdpA) MCA2218(kdpF)
            FTU: FTT1737c(kdpC) FTT1738c(kdpB)
            FTF: FTF1737c(kdpC) FTF1738c(kdpB)
            FTW: FTW_0059(kdpA) FTW_0060(kdpB) FTW_0061(kdpC)
            FTL: FTL_1880 FTL_1882 FTL_1883
            FTH: FTH_1806(kdpC) FTH_1808(kdpA)
            FTA: FTA_1990 FTA_1992(kdpA)
            FTN: FTN_1716(kdpC) FTN_1717(kdpB) FTN_1718(kdpA)
            AHA: AHA_0015(kdpC) AHA_0016(kdpB) AHA_0017(kdpA)
            CVI: CV_1597(kdpC) CV_1598(kdpB) CV_1599(kdpA)
            RSO: RSc3382(kdpA) RSc3383(kdpB) RSc3384(kdpC)
            REU: Reut_A2291 Reut_A2292 Reut_A2293
            REH: H16_B0896(kdpC) H16_B0897(kdpB) H16_B0898(kdpA)
            RME: Rmet_0038 Rmet_0039 Rmet_0040
            BMA: BMA1874(kdpC) BMA1875(kdpB) BMA1876(kdpA)
            BMV: BMASAVP1_A1083(kdpA) BMASAVP1_A1084(kdpB)
                 BMASAVP1_A1085(kdpC)
            BML: BMA10299_A0782(kdpC) BMA10299_A0783(kdpB)
                 BMA10299_A0784(kdpA)
            BMN: BMA10247_0366(kdpA) BMA10247_0367(kdpB) BMA10247_0368(kdpC)
            BXE: Bxe_A3250 Bxe_A3251 Bxe_A3252
            BVI: Bcep1808_2371 Bcep1808_2373
            BUR: Bcep18194_A5613 Bcep18194_A5614 Bcep18194_A5615
                 Bcep18194_B2382 Bcep18194_B2383
            BCN: Bcen_1674 Bcen_1675 Bcen_1676
            BCH: Bcen2424_2286 Bcen2424_2287 Bcen2424_2288
            BAM: Bamb_2324 Bamb_2325 Bamb_2326
            BPS: BPSL1171(kdpA) BPSL1172(kdpB) BPSL1173(kdpC)
            BPM: BURPS1710b_1393(kdpA) BURPS1710b_1394(kdpB)
                 BURPS1710b_1395(kdpC)
            BPL: BURPS1106A_1249(kdpA) BURPS1106A_1250(kdpB)
                 BURPS1106A_1251(kdpC)
            BPD: BURPS668_1241(kdpA) BURPS668_1242(kdpB) BURPS668_1243(kdpC)
            BTE: BTH_I1021(kdpA) BTH_I1022(kdpB) BTH_I1023(kdpC)
            PNU: Pnuc_1668 Pnuc_1670
            BPE: BP2480(kdpA) BP2481(kdpB) BP2482(kdpC)
            BPA: BPP3468(kdpA) BPP3469(kdpB) BPP3470(kdpC)
            BBR: BB3917(kdpA) BB3918(kdpB) BB3919(kdpC)
            PNA: Pnap_3602 Pnap_3604
            AAV: Aave_0355 Aave_0357
            MPT: Mpe_A2505(kdpC) Mpe_A2506(kdpB) Mpe_A2507(kdpA)
            HAR: HEAR1624(kdpC) HEAR1626(kdpA)
            MMS: mma_1821(kdpC) mma_1822(kdpB) mma_1823(kdpA)
            DAR: Daro_1085 Daro_1086 Daro_1087
            CJE: Cj0676(kdpA) Cj0677(kdpB) Cj0678(kdpC)
            CJU: C8J_0629(kdpB)
            GSU: GSU2480(kdpA) GSU2481(kdpB) GSU2482(kdpC)
            GME: Gmet_2433 Gmet_2434 Gmet_2435
            GUR: Gura_1225 Gura_1227
            DVU: DVU3337(kdpC) DVU3338(kdpB) DVU3339(kdpA) DVU3339.1(kdpF)
            DVL: Dvul_0053 Dvul_0055
            BBA: Bd1755(kdpA) Bd1757(kdpA)
            ADE: Adeh_0893 Adeh_0894 Adeh_0895
            MXA: MXAN_0163(kdpF) MXAN_0164(kdpA) MXAN_0165(kdpB)
                 MXAN_0166(kdpC)
            SFU: Sfum_2618 Sfum_2619 Sfum_2620
            MLO: mll3129 mll3130 mll3133
            PLA: Plav_1014 Plav_1015
            SME: SMa2329(kdpC) SMa2331(kdpB) SMa2333(kdpA)
            SMD: Smed_5358 Smed_5360
            ATU: Atu3788(kdpC) Atu3789(kdpB) Atu3790(kdpA)
            ATC: AGR_L_2088 AGR_L_2090 AGR_L_2092
            RET: RHE_PE00264(kdpC) RHE_PE00265(kdpB) RHE_PE00266(kdpA)
            RLE: pRL110379(kdpC) pRL110380(kdpB) pRL110381(kdpA)
            OAN: Oant_3776 Oant_3778
            BJA: bll6777(kdpC) bll6778(kdpB) bll6779(kdpA)
            RPA: RPA3002(kdpC) RPA3003(kdpB) RPA3004(kdpA)
            RPB: RPB_4645 RPB_4646 RPB_4647
            RPC: RPC_4548 RPC_4549 RPC_4550
            RPD: RPD_0662 RPD_0663 RPD_0664
            RPE: RPE_4624 RPE_4625 RPE_4626
            NHA: Nham_2992 Nham_2993 Nham_2994
            XAU: Xaut_3237 Xaut_3240
            CCR: CC_1591 CC_1592 CC_1593
            RSP: RSP_1265(kdpA) RSP_1266(kdpB) RSP_1267(kdpC)
            RSH: Rsph17029_2923 Rsph17029_2925
            SWI: Swit_1466 Swit_1468
            GBE: GbCGDNIH1_0182 GbCGDNIH1_0183 GbCGDNIH1_0184
            ACR: Acry_0708 Acry_0710 Acry_3488 Acry_3490
            RRU: Rru_A1155 Rru_A1156 Rru_A1157
            MAG: amb1909 amb1910 amb1911
            ABA: Acid345_0510 Acid345_0511 Acid345_0512
            SUS: Acid_0073 Acid_0075
            BAN: BA0739(kdpA) BA0740(kdpB) BA0741(kdpC)
            BAR: GBAA0739(kdpA) GBAA0740(kdpB) GBAA0741(kdpC)
            BAA: BA_1324 BA_1325 BA_1326(kdpC)
            BAT: BAS0703 BAS0704 BAS0705
            BCE: BC0753 BC0754 BC0755
            BCA: BCE_0809(kdpA) BCE_0810(kdpB) BCE_0811(kdpC)
            BCZ: BCZK0646(kdpA) BCZK0647(kdpB) BCZK0648(kdpC)
            BCY: Bcer98_0624 Bcer98_0626
            BTK: BT9727_0647(kdpA) BT9727_0648(kdpB) BT9727_0649(kdpC)
            BTL: BALH_0673(kdpA) BALH_0674(kdpB) BALH_0675(kdpC)
            GKA: GK3246 GK3247 GK3248
            SAU: SA0068(kdpA(SCCmec)) SA0070(kdpB(SCCmec))
                 SA0071(kdpC(SCCmec)) SA1879(kdpC) SA1880(kdpB) SA1881(kdpA)
            SAV: SAV0072 SAV0073(kdpB(SCCmec)) SAV0074(kdpC(SCCmec))
                 SAV2075(kdpC) SAV2076(kdpB) SAV2077(kdpA)
            SAM: MW1999(kdpC) MW2000(kdpB) MW2001(kdpA)
            SAR: SAR0070 SAR0071 SAR2163(kdpC) SAR2164(kdpB) SAR2165(kdpA)
            SAS: SAS1980 SAS1981 SAS1982
            SAC: SACOL2066(kdpC) SACOL2067(kdpB) SACOL2068(kdpA)
                 SACOL2069(kdpF)
            SAB: SAB1960c(kdpC) SAB1961c(kdpB) SAB1962c(kdpA)
            SAA: SAUSA300_2032(kdpC) SAUSA300_2033(kdpB) SAUSA300_2034(kdpA)
            SAO: SAOUHSC_02310 SAOUHSC_02311 SAOUHSC_02312
            SAJ: SaurJH9_0059 SaurJH9_0061 SaurJH9_2112 SaurJH9_2114
            SAH: SaurJH1_0061 SaurJH1_0063 SaurJH1_2150 SaurJH1_2152
            SER: SERP2485(kdpC) SERP2486(kdpB) SERP2487(kdpA)
            SHA: SH0033(kdpA) SH0034(kdpB) SH0035(kdpC)
            LMO: lmo2680(kdpC) lmo2681(kdpB) lmo2682(kdpA)
            LMF: LMOf2365_2660(kdpC) LMOf2365_2661(kdpB) LMOf2365_2662(kdpA)
            LIN: lin2828(kdpC) lin2829(kdpB) lin2830(kdpA) pli0052 pli0053
                 pli0055
            LWE: lwe2629(kdpC) lwe2630(kdpB) lwe2631(kdpA)
            EFA: EF0567(kdpA) EF0568(kdpB) EF0569(kdpC)
            CAC: CAC3680(kdpC) CAC3681(kdpB) CAC3682(kdpA)
            CPF: CPF_1210(kdpA) CPF_1211(kdpB) CPF_1212(kdpC)
            CDF: CD1591(kdpA) CD1592(kdpB) CD1593(kdpC)
            CKL: CKL_1471(kdpA) CKL_1472(kdpB) CKL_1473(kdpC)
            TTE: TTE2010(kdpC) TTE2011(kdpB) TTE2012(kdpA)
            MTU: Rv1029(kdpA) Rv1030(kdpB) Rv1031(kdpC)
            MTC: MT1058(kdpA) MT1059(kdpB) MT1060(kdpC)
            MBO: Mb1058(kdpA) Mb1059(kdpB) Mb1060(kdpC)
            MBB: BCG_1087(kdpA) BCG_1088(kdpB) BCG_1089(kdpC)
            MPA: MAP0997c(kdpC) MAP0998c MAP0999c MAP1000c(kdpA)
            MAV: MAV_1171(kdpC) MAV_1172(kdpB) MAV_1173(kdpA)
            MSM: MSMEG_5392(kdpA) MSMEG_5393(kdpB) MSMEG_5394
            MVA: Mvan_4759
            MMC: Mmcs_4226 Mmcs_4227 Mmcs_4228
            MKM: Mkms_4292
            MJL: Mjls_4604
            CJK: jk1269(kdpA) jk1270(kdpB) jk1271(kdpC)
            NFA: nfa15660(kdpA) nfa15670(kdpB) nfa15680(kdpC)
            RHA: RHA1_ro01230(kdpC) RHA1_ro01232(kdpA)
            SCO: SCO3716(SCH35.08) SCO3717(SCH35.07) SCO3718(SCH35.06)
            SMA: SAV917(kdpC) SAV918(kdpB) SAV919(kdpA)
            CMI: CMM_2751(kdpA) CMM_2752(kdpB) CMM_2753(kdpC)
            ART: Arth_1875 Arth_1877
            PAC: PPA0115 PPA0116 PPA0117
            FRA: Francci3_3285 Francci3_3286 Francci3_3287
            FAL: FRAAL5300(kdpC) FRAAL5301(kdpB) FRAAL5302(kdpA)
            KRA: Krad_1016 Krad_1018
            SEN: SACE_6087(kdpC) SACE_6089(kdpA)
            LIL: LA3110(kdpC) LA3111(kdpB) LA3112(kdpA)
            LIC: LIC10990(kdpA) LIC10991(kdpB) LIC10992(kdpC)
            SYN: slr1728(kdpA) slr1729(kdpB) slr1730(kdpC)
            SYC: syc2419_c(kdpC) syc2420_c(kdpB) syc2421_c(kdpA)
            SYF: Synpcc7942_1668 Synpcc7942_1669 Synpcc7942_1671
            GVI: glr0573(kdpA) glr0574(kdpB) glr0575(kdpC)
            ANA: all3151 all3153 all3154 all4243 all4245 all4246
            AVA: Ava_1192 Ava_1194 Ava_1195 Ava_3846 Ava_3849 Ava_B0204
                 Ava_B0206 Ava_B0207
            BTH: BT_2423 BT_2424 BT_2425
            BFR: BF0578 BF0579 BF0580
            BFS: BF0528(kdpA) BF0529(kdpB) BF0530(kdpC)
            CHU: CHU_1982(kdpA) CHU_1983(kdpB) CHU_1984(kdpC)
            FJO: Fjoh_1973 Fjoh_1975
            FPS: FP1690(kdpC) FP1691(kdpB) FP1692(kdpA)
            DRA: DR_B0083 DR_B0086 DR_B0087
            DGE: Dgeo_2849 Dgeo_2850 Dgeo_2851
            MBN: Mboo_0443 Mboo_0894
            HAL: VNG6176G(kdpA) VNG6177G(kdpB) VNG6178G(kdpC)
            TAC: Ta1308m Ta1309 Ta1310
            TVO: TVN0499 TVN0500 TVN0501
            PTO: PTO0155 PTO0156 PTO0157
            TPE: Tpen_1479
STRUCTURES  PDB: 1SVJ  1U7Q  2A00  2A29  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.12
            ExPASy - ENZYME nomenclature database: 3.6.3.12
            ExplorEnz - The Enzyme Database: 3.6.3.12
            ERGO genome analysis and discovery system: 3.6.3.12
            BRENDA, the Enzyme Database: 3.6.3.12
///
ENTRY       EC 3.6.3.13       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
COMMENT     Deleted entry: identical to EC 3.6.3.1, phospholipid-translocating
            ATPase (EC 3.6.3.13 created 2000, deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.13
            ExPASy - ENZYME nomenclature database: 3.6.3.13
            ExplorEnz - The Enzyme Database: 3.6.3.13
            ERGO genome analysis and discovery system: 3.6.3.13
            BRENDA, the Enzyme Database: 3.6.3.13
///
ENTRY       EC 3.6.3.14                 Enzyme
NAME        H+-transporting two-sector ATPase;
            ATP synthase;
            F1-ATPase;
            FoF1-ATPase;
            H+-transporting ATPase;
            mitochondrial ATPase;
            coupling factors (F0, F1 and CF1);
            chloroplast ATPase;
            bacterial Ca2+/Mg2+ ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (H+-transporting)
REACTION    ATP + H2O + H+in = ADP + phosphate + H+out [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            H+ [CPD:C00080]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            H+ [CPD:C00080]
COFACTOR    H+ [CPD:C00080]
COMMENT     A multisubunit non-phosphorylated ATPase that is involved in the
            transport of ions. Large enzymes of mitochondria, chloroplasts and
            bacteria with a membrane sector (Fo, Vo, Ao) and a
            cytoplasmic-compartment sector (F1, V1, A1). The F-type enzymes of
            the inner mitochondrial and thylakoid membranes act as ATP
            synthases. All of the enzymes included here operate in a rotational
            mode, where the extramembrane sector (containing 3 alpha- and 3
            beta-subunits) is connected via the delta-subunit to the membrane
            sector by several smaller subunits. Within this complex, the gamma-
            and epsilon-subunits, as well as the 9-12 c subunits rotate by
            consecutive 120_degree_ angles and perform parts of ATP synthesis.
            This movement is driven by the H+ electrochemical potential
            gradient. The V-type (in vacuoles and clathrin-coated vesicles) and
            A-type (archebacterial) enzymes have a similar structure but, under
            physiological conditions, they pump H+ rather than synthesize ATP.
REFERENCE   1  [PMID:8417777]
  AUTHORS   Boyer PD.
  TITLE     The binding change mechanism for ATP synthase--some probabilities
            and possibilities.
  JOURNAL   Biochim. Biophys. Acta. 1140 (1993) 215-50.
REFERENCE   2  [PMID:8065448]
  AUTHORS   Abrahams JP, Leslie AG, Lutter R, Walker JE.
  TITLE     Structure at 2.8 A resolution of F1-ATPase from bovine heart
            mitochondria.
  JOURNAL   Nature. 370 (1994) 621-8.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:8581162]
  AUTHORS   Blair A, Ngo L, Park J, Paulsen IT, Saier MH Jr.
  TITLE     Phylogenetic analyses of the homologous transmembrane
            channel-forming proteins of the F0F1-ATPases of bacteria,
            chloroplasts and mitochondria.
  JOURNAL   Microbiology. 142 ( Pt 1) (1996) 17-32.
REFERENCE   4  [PMID:9069291]
  AUTHORS   Noji H, Yasuda R, Yoshida M, Kinosita K Jr.
  TITLE     Direct observation of the rotation of F1-ATPase.
  JOURNAL   Nature. 386 (1997) 299-302.
PATHWAY     PATH: map00190  Oxidative phosphorylation
            PATH: map00195  Photosynthesis
            PATH: map02040  Flagellar assembly
            PATH: map03070  Type III secretion system
            PATH: map05120  Epithelial cell signaling in Helicobacter pylori
                            infection
ORTHOLOGY   KO: K01549  ATP synthase
            KO: K02107  H+-transporting ATPase
            KO: K02108  F-type H+-transporting ATPase a chain
            KO: K02109  F-type H+-transporting ATPase b chain
            KO: K02110  F-type H+-transporting ATPase c chain
            KO: K02111  F-type H+-transporting ATPase alpha chain
            KO: K02112  F-type H+-transporting ATPase beta chain
            KO: K02113  F-type H+-transporting ATPase delta chain
            KO: K02114  F-type H+-transporting ATPase epsilon chain
            KO: K02115  F-type H+-transporting ATPase gamma chain
            KO: K02117  V-type H+-transporting ATPase subunit A
            KO: K02118  V-type H+-transporting ATPase subunit B
            KO: K02119  V-type H+-transporting ATPase subunit C
            KO: K02120  V-type H+-transporting ATPase subunit D
            KO: K02121  V-type H+-transporting ATPase subunit E
            KO: K02122  V-type H+-transporting ATPase subunit F
            KO: K02123  V-type H+-transporting ATPase subunit I
            KO: K02124  V-type H+-transporting ATPase subunit K
            KO: K02125  F-type H+-transporting ATPase subunit 8
            KO: K02126  F-type H+-transporting ATPase subunit a
            KO: K02127  F-type H+-transporting ATPase subunit b
            KO: K02128  F-type H+-transporting ATPase subunit c
            KO: K02129  F-type H+-transporting ATPase subunit e
            KO: K02130  F-type H+-transporting ATPase subunit f
            KO: K02131  F-type H+-transporting ATPase subunit f6
            KO: K02132  F-type H+-transporting ATPase alpha chain
            KO: K02133  F-type H+-transporting ATPase beta chain
            KO: K02134  F-type H+-transporting ATPase delta chain
            KO: K02135  F-type H+-transporting ATPase epsilon chain
            KO: K02136  F-type H+-transporting ATPase gamma chain
            KO: K02137  F-type H+-transporting ATPase oligomycin sensitivity
                        conferral protein
            KO: K02138  F-type H+-transporting ATPase d chain
            KO: K02139  F-type H+-transporting ATPase f chain
            KO: K02140  F-type H+-transporting ATPase g chain
            KO: K02141  F-type H+-transporting ATPase h chain
            KO: K02142  F-type H+-transporting ATPase j chain
            KO: K02143  F-type H+-transporting ATPase k chain
            KO: K02144  V-type H+-transporting ATPase 54 kD subunit
            KO: K02145  V-type H+-transporting ATPase subunit A
            KO: K02146  V-type H+-transporting ATPase subunit AC39
            KO: K02147  V-type H+-transporting ATPase subunit B
            KO: K02148  V-type H+-transporting ATPase subunit C
            KO: K02149  V-type H+-transporting ATPase subunit D
            KO: K02150  V-type H+-transporting ATPase subunit E
            KO: K02151  V-type H+-transporting ATPase subunit F
            KO: K02152  V-type H+-transporting ATPase subunit G
            KO: K02153  V-type H+-transporting ATPase subunit H
            KO: K02154  V-type H+-transporting ATPase subunit I
            KO: K02155  V-type H+-transporting ATPase 16kDa proteolipid subunit
            KO: K02412  flagellum-specific ATP synthase
            KO: K03224  ATP synthase in type III secretion protein SctN
            KO: K03661  V-type H+-transporting ATPase 21kDa proteolipid subunit
            KO: K03662  V-type H+-transporting ATPase S1 subunit
GENES       HSA: 10312(TCIRG1) 10476(ATP5H) 10632(ATP5L) 127124(ATP6V1G3)
                 23545(ATP6V0A2) 245972(ATP6V0D2) 245973(ATP6V1C2) 4508(ATP6)
                 4509(ATP8) 498(ATP5A1) 506(ATP5B) 50617(ATP6V0A4) 509(ATP5C1)
                 513(ATP5D) 51382(ATP6V1D) 514(ATP5E) 515(ATP5F1) 516(ATP5G1)
                 51606(ATP6V1H) 517(ATP5G2) 518(ATP5G3) 521(ATP5I) 522(ATP5J)
                 523(ATP6V1A) 525(ATP6V1B1) 526(ATP6V1B2) 527(ATP6V0C)
                 528(ATP6V1C1) 529(ATP6V1E1) 533(ATP6V0B) 534(ATP6V1G2)
                 535(ATP6V0A1) 537(ATP6AP1) 539(ATP5O) 8992(ATP6V0E1)
                 90423(ATP6V1E2) 9114(ATP6V0D1) 9296(ATP6V1F) 9550(ATP6V1G1)
                 9551(ATP5J2)
            PTR: 450294(ATP5C1) 451943(ATP5G2) 451999(ATP5B) 452979(ATP6V1D)
                 453600(LOC453600) 454685(ATP6V0A1) 455195(ATP5G1)
                 461042(ATP5I) 464033(ATP6V1B2) 464326(ATP6V1C1)
                 466932(LOC466932) 467061(LOC467061) 469629(ATP6V1G3)
                 470584(ATP5G3) 472809(ATP6V0D2) 473030(ATP6V1G1)
                 473171(LOC473171) 473976(ATP5O) 742541(ATP5L) 807859(ATP6)
                 807862(ATP8)
            MCC: 696788(LOC696788) 698075(LOC698075) 698144(LOC698144)
                 698480(ATP5O) 698616(LOC698616) 702243(LOC702243)
                 708411(ATP5J) 713542(LOC713542) 718961(LOC718961)
            MMU: 108664(Atp6v1h) 110935(Atp6v1b1) 114143(Atp6v0b)
                 11946(Atp5a1) 11947(Atp5b) 11949(Atp5c1) 11950(Atp5f1)
                 11951(Atp5g1) 11957(Atp5j) 11958(Atp5k) 11964(Atp6v1a)
                 11966(Atp6v1b2) 11972(Atp6v0d1) 11973(Atp6v1e1) 11974(Atp6v0e)
                 11975(Atp6v0a1) 11984(Atp6v0c) 140494(Atp6v0a4)
                 21871(Atp6v0a2) 228033(Atp5g3) 240853(EG240853)
                 242341(Atp6v0d2) 27060(Tcirg1) 27425(Atp5l) 28080(Atp5o)
                 338375(Atp6v1g3) 432676(EG432676) 54411(Atp6ap1) 57423(Atp5j2)
                 66043(Atp5d) 66144(Atp6v1f) 66237(Atp6v1g2) 66290(Atp6v1g1)
                 66335(Atp6v1c1) 67126(Atp5e) 67942(Atp5g2) 68775(Atp6v1c2)
                 71679(Atp5h) 73834(Atp6v1d) 74915(Atp6v1e2) 76252(Atp6v0e2)
            RNO: 114630(Atp5g3) 116455(Atp6v0a2) 116550(Atp5c1)
                 116664(Atp6v1f) 117596(Atp6v1b2) 140608(Atp5i) 170667(Atp6v0c)
                 171082(Atp5g2) 171374(Atp5b) 171375(Atp5f1) 192241(Atp5o)
                 245958(Atp5e) 245965(Atp5d) 26196(ATP8) 26197(ATP6)
                 291969(Atp6v0d1) 293699(RGD1563463_predicted) 29754(Atp5g1)
                 297566(Atp6v1e1) 29757(Atp6v0a1) 297932(Atp6v0d2)
                 299159(Atp6v1d) 299971(Atp6v1c1) 300677(MGC72942)
                 306478(RGD1559626_predicted) 360716(Atp6v1a1_predicted)
                 362802(Atp6v1c2) 364460(RGD1565438_predicted) 641434(Atp5h)
                 65262(Atp5a1) 83615(Atp6ap1) 94170(Atp6v0e1) 94271(Atp5j)
            CFA: 403669(ATP5B) 403729(ATP6V0E1) 474433(LOC474433)
                 474628(ATP6V1B1) 474840(ATP6V1G2) 475061(ATP6V1C1)
                 475098(LOC475098) 475199(ATP6V1F) 475667(ATP6V1C2)
                 475912(LOC475912) 476756(ATP5D) 476978(LOC476978)
                 477595(ATP5G2) 477740(ATP6V1E1) 477929(ATP6V0D2)
                 478009(ATP5C1) 478252(LOC478252) 478393(ATP5J)
                 478410(LOC478410) 478807(ATP5G3) 479685(ATP6V0D1)
                 479742(LOC479742) 479877(ATP6V0C) 479901(ATP5F1)
                 480149(ATP5A1) 480360(ATP6V1D) 481359(ATP6V1E2)
                 481939(LOC481939) 482528(ATP6V0B) 482600(LOC482600)
                 482779(ATP6V0A4) 486137(ATP6V1B2) 486245(ATP6V0A2)
                 486953(ATP6V1H) 487981(ATP6V1A) 488330(LOC488330)
                 490256(ATP6V1G3) 491061(ATP5G1) 607705(ATP6V0A1)
                 608667(LOC608667) 610725(LOC610725) 610922(ATP6AP1)
                 804487(ATP8) 804488(ATP6)
            BTA: 281640(ATP5O) 281641(ATP6J) 282147(ATP6V1A) 282148(ATP6D)
                 282405(ATP6S14) 282578(ATP5A1) 282657(ATP6V1H) 282690(ATP5J)
                 282710(ATP5H) 286768(ATP6V0A1) 287017(ATP6V1E1) 327668(ATP5C1)
                 327675(ATP5B) 327687(ATP6IP1) 3283881(ATP8) 3283882(ATP6)
                 337887(ATP5G2) 338038(ATP6V0A2) 338040(ATP5I) 338053(ATP5G1)
                 338059(ATP6V1B1) 338081(ATP5D) 338082(ATP6V1B2) 338088(ATP5E)
                 338089(ATP6V1C1) 404152(ATP6V1D) 407191(LOC407191)
                 540176(ATP5G3)
            SSC: 396950(ATP5I) 397472(ATP6V1H) 445531(ATP6V1A1) 574054(ATP5G1)
                 808505(ATP8) 808506(ATP6)
            GGA: 374159(ATP5A1) 395472(TCIRG1) 395473(ATP6V0A2)
                 395474(ATP6V0A1) 395497(ATP6V1B2) 395821(ATP6V1A)
                 416495(ATP5J2) 417249(ATP6V1G1) 418162(ATP6V1E1) 418477(ATP5J)
                 418508(ATP5O) 419108(ATP5C1) 419866(ATP5F1) 419992(ATP5G1)
                 420210(ATP6V0D2) 420259(ATP6V1C1) 421939(ATP6V1C2)
                 422115(ATP5H) 423280(ATP6V1D) 424142(ATP5G3) 424349(ATP6V1G3)
                 426199(ATP6V1H) 426673(RCJMB04_6l18) 768660(LOC768660)
                 768854(ATP6V0E1) 769146(ATP5I) 769770(ATP6V0E2) 770052(ATP5L)
                 770475(ATP6V0C) 807646(ATP6) 807647(ATP8)
            XLA: 2642082(ATP8) 2642083(ATP6) 379397(MGC53399) 379457(MGC64332)
                 379616(MGC68738) 379775(cg1746) 379796(atp6a1) 379818(atp5b)
                 379892(atp6v0d1) 379986(atp6v0a1) 380128(atp6v1g1)
                 380139(atp5a1) 380173(atp5c1) 380305(vha55) 397732(LOC397732)
                 398647(MGC64475) 398852(MGC68786) 398897(MGC68661)
                 403358(MGC68592) 414718(MGC82400) 414720(MGC82276)
                 432055(MGC82361) 443873(MGC79146) 446821(MGC80578)
                 446845(MGC80692) 447080(MGC85230) 447106(MGC85306)
                 447261(MGC86324) 447565(MGC84266) 494703(LOC494703)
                 495263(LOC495263) 495264(LOC495264)
            XTR: 3283496(ATP8) 3283497(ATP6) 394488(atp6v0c) 394723(MGC75766)
                 394728(atp6v1e1) 394779(MGC75601) 394992(MGC76083)
                 407968(atp5b) 448314(MGC89120) 448533(atp6v1g1) 448663(atp5g3)
                 493238(atp6v1a) 496430(atp5h) 548977(atp6v0a2) 549161(atp5c1)
                 549169(atp5k) 549270(atp5d) 549829(atp6v1d) 594998(atp5a1)
            DRE: 140519(ATP6) 140520(ATP8) 192335(atp6v1e1) 192336(atp6v0c)
                 195824(atp6ap1) 286779(atp6v1h) 321724(atp6v0b)
                 322811(atp6v0d1) 326977(atp5l) 335025(atp6v1g1)
                 335191(zgc:109976) 335709(atp5d) 336957(atp5c1)
                 359839(atp6v1ba) 359840(atp6v1b2) 368907(atp6v1c1)
                 393675(atp5h) 393935(atp6v1d) 394110(atp6v1al)
                 394151(zgc:55970) 406599(atp5j) 436799(atp6v1f) 553755(atp5a1)
                 554135(zgc:111961) 81541(atp5g)
            SPU: 2652722(ATP6) 373259(LOC373259) 373382(LOC373382)
                 548622(LOC548622) 574666(LOC574666) 575822(LOC575822)
                 576006(LOC576006) 578290(LOC578290) 579085(LOC579085)
                 579414(LOC579414) 579751(LOC579751) 580821(LOC580821)
                 581267(LOC581267) 583818(LOC583818) 585744(LOC585744)
                 587430(LOC587430) 589143(LOC589143) 589417(LOC589417)
                 591262(LOC591262) 591328(LOC591328) 593221(LOC593221)
                 594178(LOC594178) 759060(LOC759060) 759431(LOC759431)
                 760323(LOC760323)
            DME: ATP6 ATP8 Dmel_CG1088(Vha26) Dmel_CG10897(tou)
                 Dmel_CG11154(ATPsyn-beta) Dmel_CG11589(VhaM9.7-1) Dmel_CG12403
                 Dmel_CG12602 Dmel_CG13167 Dmel_CG15552(Sox100B)
                 Dmel_CG17332(VhaSFD) Dmel_CG17369(Vha55) Dmel_CG1746
                 Dmel_CG2934 Dmel_CG2968(l(1)G0230) Dmel_CG30329
                 Dmel_CG3161(Vha16) Dmel_CG32089(Vha16-2) Dmel_CG32090
                 Dmel_CG3321 Dmel_CG3612(blw) Dmel_CG3762 Dmel_CG3897(blot)
                 Dmel_CG4029(jumu) Dmel_CG4154(Gyc88E) Dmel_CG4307(Oscp)
                 Dmel_CG4412(ATPsyn-Cf6) Dmel_CG4692 Dmel_CG5075 Dmel_CG5389
                 Dmel_CG6030(ATPsyn-d) Dmel_CG6105(l(2)06225)
                 Dmel_CG6213(Vha13) Dmel_CG6737 Dmel_CG7007 Dmel_CG7211
                 Dmel_CG7610(ATPsyn-gamma) Dmel_CG7625(VhaM9.7-2) Dmel_CG8029
                 Dmel_CG8186 Dmel_CG8189(ATPsyn-b) Dmel_CG8210(Vha14)
                 Dmel_CG8310 Dmel_CG8815(Sin3A) Dmel_CG9013 Dmel_CG9032(sun)
                 Dmel_CG9351(flfl) Dmel_CG9397(1.28)
            CEL: ATP6 C06H2.1(atp-5) C17H12.14(ATPase) C26H9A.1(vha-7)
                 C30F8.2(vha-16) C34E10.6(atp-2) C53B7.4(asg-2) F02E8.1(asb-2)
                 F20B6.2(vha-12) F32D1.2 F35G12.10(asb-1) F35H10.4(vha-5)
                 F46F11.5(vha-10) F49C12.13(vha-17) F52E1.10(ATPase)
                 F55H2.2(vha-14) F58F12.1 K07A12.3(asg-1) R04F11.2 R05D3.6
                 R10E11.2(vha-2) R10E11.8(vha-1) R53.4 T01H3.1(vha-4)
                 T14F9.1(vha-15) T26E3.7 VW02B12L.1(vha-6) Y110A7A.12(tag-300)
                 Y38F2AL.4(vha-3) Y49A3A.2(vha-13) Y55H10A.1(vha-19) Y69A2AR.18
                 ZC262.5 ZK637.8(unc-32) ZK970.4(vha-9)
            ATH: AT1G12840(DET3) AT1G15700(ATPC2) AT1G19910(AVA-P2) AT1G51650
                 AT1G64200(VHA-E3) AT1G75630(AVA-P4) AT1G76030 AT1G78900(VHA-A)
                 AT2G07698 AT2G21410 AT2G25610 AT2G28520(VHA-A1) AT2G33040
                 AT3G08560(VHA-E2) AT3G28710 AT3G28715 AT3G42050 AT3G58730
                 AT4G02620 AT4G04640(ATPC1) AT4G09650 AT4G11150(TUF) AT4G23710
                 AT4G25950(VATG3) AT4G32530 AT4G39080(VHA-A3) AT5G08670
                 AT5G08680 AT5G08690 AT5G47030 AT5G55290 ArthCp007(atpA)
                 ArthCp009(atpH) ArthCp010(atpI) ArthCp028(atpE)
                 ArthCp029(atpB) ArthMp035(atp6-1) ArthMp094(atp9)
            OSA: 3131390(atpA) 3131391(atpF) 3131392(atpH) 3131393(atpI)
                 3131461(OrsajCp031) 3131462(OrsajCp032) 4324151 4324236
                 4324550 4326699 4327166 4327412 4327660 4327731 4327833
                 4328470 4329623 4330737 4331207 4332270 4332431 4335014
                 4335236 4336883 4337176 4337284 4337563 4339122 4339546
                 4339800 4341339 4341660 4341751 4343288 4343366 4343539
                 4345078 4345839 4348305 4349180 4349890 atp1 atp6 atp9
            CME: CMC151C CMD007C CMD095C CME198C CMG004C CMH197C CMH200C
                 CMK178C CML029C CMN127C CMN223C CMO274C CMP123C CMQ010C
                 CMQ087C CMQ237C CMQ323C CMQ386C CMS332C CMS342C CMT434C
            SCE: Q0080(ATP8) Q0085(ATP6) Q0130(OLI1) YBL099W(ATP1)
                 YBR039W(ATP3) YBR127C(VMA2) YDL004W(ATP16) YDL185W(TFP1)
                 YDR298C(ATP5) YDR377W(ATP17) YEL027W(CUP5) YEL051W(VMA8)
                 YGR020C(VMA7) YHR026W(PPA1) YHR039C-A(VMA10) YJR121W(ATP2)
                 YKL016C(ATP7) YKL080W(VMA5) YLR295C(ATP14) YLR447C(VMA6)
                 YML081C-A(ATP18) YMR054W(STV1) YOL077W-A(ATP19) YOR270C(VPH1)
                 YOR332W(VMA4) YPL078C(ATP4) YPL234C(TFP3) YPL271W(ATP15)
                 YPR020W(ATP20) YPR036W(VMA13)
            AGO: AGOS_AAL065C AGOS_AAL076W AGOS_AAR130C AGOS_ABR169W
                 AGOS_ACL097C AGOS_ACL176W AGOS_ACR021W AGOS_ACR071W
                 AGOS_ACR181C AGOS_ACR203W AGOS_ADL025W AGOS_ADL380W
                 AGOS_ADR102W AGOS_ADR127W AGOS_ADR146C AGOS_ADR177C
                 AGOS_ADR358W AGOS_AEL008W AGOS_AEL074W AGOS_AEL251C
                 AGOS_AER021C AGOS_AER146C AGOS_AER163W AGOS_AFL141C
                 AGOS_AGL052W AGOS_AGL272C AGOS_AMI005W AGOS_AMI006W
                 AGOS_AMI007W
            KLA: KllafMp01(ATP9) KllafMp03(ATP6) KllafMp04(ATP8)
            PIC: PICST_30875(ATP17) PICST_32314(ATP14) PICST_35827(VMA7)
                 PICST_48891(VMA2) PICST_52299(VPH1) PICST_58102(VMA5)
                 PICST_60924(VMA4) PICST_61950(VMA10) PICST_65041(ATP20)
                 PICST_66160(VMA13) PICST_67737(VPH3) PICST_69779(ATP16)
                 PICST_71868(VMA6) PICST_75615(TFP1) PICST_77492(ATP2)
                 PICST_78422(ATP4) PICST_79036(ATP7) PICST_80851(VMA8)
                 PICST_81568(ATP18) PICST_81978(ATP5) PICST_86570(ATP1)
                 PICST_86847(PPA1) PICST_87235(TFP3) PICST_91482(ATP3)
            CAL: CaO19.1190(vph1) CaO19.364(vma6) CaO19.3757(atp20)
                 CaO19.6863(vph1) CaO19_2166(CaO19.2166) CaO19_4954(CaO19.4954)
                 CaO19_5419(CaO19.5419) CaO19_7678(CaO19.7678) CaalfMp05(ATP9)
                 CaalfMp06(ATP6)
            CGR: CAGL0A01111g CAGL0A03036g CAGL0C00649g CAGL0C02959g
                 CAGL0D04048g CAGL0E05346g CAGL0E06204g CAGL0F06347g
                 CAGL0F08987g CAGL0H00506g CAGL0H01397g CAGL0H05489g
                 CAGL0I00572g CAGL0I01562g CAGL0I03960g CAGL0I04686g
                 CAGL0J00627g CAGL0J11880g CAGL0K02409g CAGL0L05126g
                 CAGL0L09713g CAGL0M00660g CAGL0M09581g CaglfMp08(atp8)
                 CaglfMp09(atp6) CaglfMp10(atp9)
            SPO: SPAC11E3.07(vma4) SPAC14C4.14(atp1) SPAC16E8.07c SPAC17A2.03c
                 SPAC1B3.14(vma3) SPAC222.12c(atp2) SPAC23C4.11 SPAC2C4.13
                 SPAC343.05(vma1) SPAC637.05c(vma2) SPAC732.01 SPAC7D4.10
                 SPAPB2B4.05 SPBC1289.05c SPBC13E7.04 SPBC1604.07 SPBC1604.11
                 SPBC1734.13 SPBC29A10.13 SPBC31F10.15c SPBC3B9.18c SPCC1840.06
                 SPCC965.03
            ANI: AN0110.2 AN0252.2 AN0277.2 AN1195.2 AN1523.2 AN1534.2
                 AN1624.2 AN2315.2 AN3088.2 AN3168.2 AN4718.2 AN5084.2 AN5606.2
                 AN5880.2 AN6232.2 AN6287.2 AN6631.2 AN7603.2 AN8674.2 AN9107.2
                 AN9455.2
            AFM: AFUA_1G03100 AFUA_1G03510 AFUA_1G10670 AFUA_1G10810
                 AFUA_1G16280 AFUA_2G05510 AFUA_2G09310 AFUA_2G11330
                 AFUA_2G12400 AFUA_2G13240 AFUA_2G15560 AFUA_3G12370
                 AFUA_3G13390 AFUA_4G09360 AFUA_4G11300 AFUA_5G02370
                 AFUA_5G08560 AFUA_5G10550 AFUA_5G11920 AFUA_6G02090
                 AFUA_6G03810 AFUA_8G05320 AFUA_8G05440
            AOR: AO090003000607 AO090003001090 AO090005000604 AO090005000617
                 AO090005000730 AO090005000749 AO090010000482 AO090012000274
                 AO090012000797 AO090023000599 AO090026000283 AO090026000372
                 AO090026000517 AO090038000334 AO090038000352 AO090038000579
                 AO090102000349 AO090102000454 AO090120000091 AO090120000313
                 AO090701000168
            CNE: CNA02690 CNA04290 CNA05420 CNA06920 CNB00330 CNB04580
                 CNC00590 CNC00990 CNC03840 CNC05260 CNC05720 CNC06660 CND02320
                 CND03280 CNE00750 CNE02210 CNF00570 CNF01900 CNF02280 CNF02860
                 CNI01180 CNK03340
            UMA: UM00508.1 UM00621.1 UM00630.1 UM00975.1 UM01103.1 UM01618.1
                 UM02064.1 UM02782.1 UM03191.1 UM03951.1 UM04167.1 UM04345.1
                 UM04716.1 UM05090.1 UM05379.1 UM05451.1 UM05487.1 UM05503.1
                 atp6 atp8 atp9
            ECU: ECU03_0305 ECU03_0500 ECU03_1120 ECU05_0405 ECU06_0190
                 ECU07_1350 ECU08_0250 ECU08_1520 ECU09_1790 ECU10_0140
                 ECU10_1040 ECU11_1280i
            DDI: DDBDRAFT_0167520 DDBDRAFT_0167789 DDBDRAFT_0167892
                 DDBDRAFT_0184316 DDBDRAFT_0190669 DDBDRAFT_0216607
                 DDBDRAFT_0216933 DDB_0185070(vatE) DDB_0185071(vatP)
                 DDB_0185207(vatB) DDB_0185227(vatD) DDB_0191419(vatC)
                 DDB_0201563(vatA) DDB_0216215(vatM)
            PFA: MAL13P1.271 MAL13P1.47 MAL1P1.52 MAL7P1.75 PF11_0412
                 PF13_0034 PF13_0061 PF13_0065 PF13_0130 PF13_0227 PF14_0615
                 PFB0795w PFD0300c PFE0965c PFI1670c PFL1725w
            CPV: cgd1_520 cgd1_540 cgd2_250 cgd2_3960 cgd4_1470 cgd4_540
                 cgd5_3340 cgd5_530 cgd5_850 cgd7_5000 cgd8_1670 cgd8_360
                 cgd8_4790
            CHO: Chro.10062 Chro.10063 Chro.20032 Chro.20148 Chro.20149
                 Chro.20424 Chro.40070 Chro.40167 Chro.50039 Chro.50302
                 Chro.50340 Chro.60082 Chro.70559 Chro.80048 Chro.80195
                 Chro.80551
            TAN: TA02610 TA06450 TA07825 TA08420 TA08450 TA10280 TA10370
                 TA11325 TA12155 TA12310 TA13210 TA13470 TA15215 TA17420
                 TA17730 TA18615 TA19395 TA20945
            TPV: TP01_0201 TP01_0389 TP01_0929 TP02_0034 TP02_0253 TP02_0445
                 TP02_0488 TP02_0804 TP03_0033 TP03_0278 TP03_0569 TP03_0853
                 TP04_0317 TP04_0436 TP04_0441 TP04_0714 TP04_0731 TP04_0832
            TET: TTHERM_00047070 TTHERM_00052460 TTHERM_00105320
                 TTHERM_00118610 TTHERM_00161260 TTHERM_00193660
                 TTHERM_00218330 TTHERM_00266570 TTHERM_00339640
                 TTHERM_00433470 TTHERM_00529860 TTHERM_00585260
                 TTHERM_00628600 TTHERM_00653620 TTHERM_00821870
                 TTHERM_00865410 TTHERM_01005210 TepyoMp18(atp9)
            TBR: Tb10.100.0070 Tb10.100.0090 Tb10.61.2840 Tb10.70.3600
                 Tb10.70.6340 Tb10.70.7480 Tb11.01.1190 Tb11.01.3560
                 Tb11.02.2950 Tb11.02.5470 Tb927.1.3820 Tb927.3.1380
                 Tb927.4.1080 Tb927.5.1300 Tb927.5.550 Tb927.6.4990
                 Tb927.6.5050 Tb927.7.1470 Tb927.7.7420 Tb927.7.7430
                 Tb927.8.2100 Tb927.8.2310
            TCR: 467287.30 503579.70 503929.10 504069.70 504069.80 504125.40
                 504131.180 506025.50 506163.40 506375.110 506405.120
                 506529.516 506855.80 506867.20 506945.240 506945.300 506977.70
                 507517.60 507623.129 508397.10 508781.20 508821.50 508851.59
                 509017.30 509233.180 509601.70 509885.10 510395.10 510993.10
                 511001.190 511145.50 511145.60 511209.10 511589.10
            LMA: LmjF05.0500 LmjF05.0510 LmjF05.1140 LmjF07.1105 LmjF12.0520
                 LmjF18.0560 LmjF21.0740 LmjF21.1340 LmjF21.1770 LmjF21.1790
                 LmjF21.1800 LmjF23.0130 LmjF23.0340 LmjF23.1510 LmjF24.0630
                 LmjF25.1170 LmjF25.1180 LmjF26.0460 LmjF28.1160 LmjF28.2430
                 LmjF30.3600 LmjF30.3660 LmjF34.3670 LmjF35.0700 LmjF36.3100
            EHI: 101.t00011 105.t00023 111.t00022 156.t00014 161.t00001
                 18.t00032 202.t00016 204.t00009 215.t00004 289.t00003
                 417.t00001 55.t00005 79.t00005 9.t00012 9.t00013 94.t00029
            ECO: b1941(fliI) b3731(atpC) b3732(atpD) b3733(atpG) b3734(atpA)
                 b3735(atpH) b3736(atpF) b3737(atpE) b3738(atpB)
            ECJ: JW1925(fliI) JW3709(atpC) JW3710(atpD) JW3711(atpG)
                 JW3712(atpA) JW3713(atpH) JW3714(atpF) JW3715(atpE)
                 JW3716(atpB)
            ECE: Z3031(fliI) Z4194 Z5119(escN) Z5229(atpC) Z5230(atpD)
                 Z5231(atpG) Z5232(atpA) Z5233(atpH) Z5234(atpF) Z5235(atpE)
                 Z5236(atpB)
            ECS: ECs2680 ECs3730 ECs4568 ECs4673 ECs4674 ECs4675 ECs4676
                 ECs4677 ECs4678 ECs4679 ECs4680
            ECC: c2358(fliI) c4657(atpC) c4658(atpD) c4659(atpG) c4660(atpA)
                 c4662(atpH) c4664(atpF) c4665(atpE) c4666(atpB)
            ECI: UTI89_C0735(tolA) UTI89_C2141(fliI) UTI89_C4284(atpC)
                 UTI89_C4285(atpD) UTI89_C4286(atpG) UTI89_C4287(atpA)
                 UTI89_C4289(atpH) UTI89_C4291(atpF) UTI89_C4292(atpE)
                 UTI89_C4293(atpB) UTI89_C4668(gltP)
            ECP: ECP_1875 ECP_3930 ECP_3931 ECP_3932 ECP_3933 ECP_3934
                 ECP_3935 ECP_3936 ECP_3937
            ECV: APECO1_2725(atpB) APECO1_2728(atpG) APECO1_2729(atpD)
                 APECO1_980(fliI)
            ECW: EcE24377A_2174(fliI) EcE24377A_4246(atpC)
                 EcE24377A_4247(atpD) EcE24377A_4249(atpG) EcE24377A_4250(atpA)
                 EcE24377A_4251(atpH) EcE24377A_4252(atpF) EcE24377A_4253(atpE)
                 EcE24377A_4254(atpB) EcE24377A_4255(atpI)
            ECX: EcHS_A2041(fliI) EcHS_A3947 EcHS_A3948 EcHS_A3949 EcHS_A3950
                 EcHS_A3951 EcHS_A3952 EcHS_A3953 EcHS_A3954 EcHS_A3955
            STY: STY1705(ssaN) STY2180(fliI) STY3017(spaI) STY3907(atpB)
                 STY3908(atpE) STY3909(atpF) STY3910(atpH) STY3911(atpA)
                 STY3912(atpG) STY3913(atpD) STY3914(atpC)
            STT: t0905(fliI) t1283(ssaN) t2796(spaI) t3648(atpB) t3649(atpE)
                 t3650(atpF) t3651(atpH) t3652(atpA) t3653(atpG) t3654(atpD)
                 t3655(atpC)
            SPT: SPA0898(fliI) SPA1438(ssaN) SPA2752(spaI) SPA3703(atpC)
                 SPA3704(atpD) SPA3705(atpG) SPA3706(atpA) SPA3707(atpH)
                 SPA3708(atpF) SPA3709(atpE) SPA3710(atpB)
            SEC: SC1436(ssaN) SC1977(fliI) SC2826(invC) SC3776(atpC)
                 SC3777(atpD) SC3778(atpG) SC3779(atpA) SC3780(atpH)
                 SC3781(atpF) SC3782(atpL) SC3783(atpB)
            STM: STM1415(ssaN) STM1972(fliI) STM2894(invC) STM3864(atpC)
                 STM3865(atpD) STM3866(atpG) STM3867(atpA) STM3868(atpH)
                 STM3869(atpF) STM3870(atpE) STM3871(atpB)
            YPE: YPCD1.40(yscN) YPO0267 YPO0717(fliI) YPO1827(fliI)
                 YPO4120(atpC) YPO4121(atpD) YPO4122(atpG) YPO4123(atpA)
                 YPO4124(atpH) YPO4125(atpF) YPO4126(atpE) YPO4127(atpB)
            YPK: y0526(fliI) y2479(fliI) y3461(fliI) y4134(atpC) y4135(atpD)
                 y4136(atpG) y4137(atpA) y4138(atpH) y4139(atpF) y4140(atpE)
                 y4141(atpB)
            YPM: YP_0421(fliI1) YP_1565(fliI2) YP_3029(fliI3) YP_4027(atpC)
                 YP_4028(atpD) YP_4029(atpG) YP_4030(atpA) YP_4031(atpH)
                 YP_4032(atpF) YP_4033(atpE) YP_4034(atpB) YP_pCD43(yscN)
            YPA: YPA_4165 YPA_4170 YPA_4172
            YPN: YPN_3977 YPN_3982 YPN_3984
            YPP: YPDSF_3911
            YPS: YPTB0323 YPTB1700(fliI) YPTB3345(fliI) YPTB3966(atpC)
                 YPTB3967(atpD) YPTB3968(atpG) YPTB3969(atpA) YPTB3970(atpH)
                 YPTB3971(atpF) YPTB3972(atpE) YPTB3973(atpB) pYV0067
            YPI: YpsIP31758_0634(fliI2) YpsIP31758_2293(fliI1) YpsIP31758_3818
                 YpsIP31758_4175(atpC) YpsIP31758_4176(atpD)
                 YpsIP31758_4177(atpG) YpsIP31758_4178(atpA)
                 YpsIP31758_4179(atpH) YpsIP31758_4180(atpF)
                 YpsIP31758_4181(atpE) YpsIP31758_4182(atpB)
                 YpsIP31758_4183(atpI)
            YEN: YEP0024(yscN)
            SFL: SF1986(fliI) SF3811(atpC) SF3812(atpD) SF3813(atpG)
                 SF3814(atpA) SF3815(atpH) SF3816(atpF) SF3817(atpE)
                 SF3818(atpB)
            SFX: S2080(fliI) S3950(atpB) S3951(atpE) S3952(atpF) S3953(atpH)
                 S3954(atpA) S3955(atpG) S3956(atpD) S3957(atpC)
            SFV: SFV_1984(fliI) SFV_3757(atpC) SFV_3758(atpD) SFV_3759(atpG)
                 SFV_3760(atpA) SFV_3761(atpH) SFV_3762(atpF) SFV_3763(atpE)
                 SFV_3764(atpB)
            SSN: SSON_1999(fliI) SSON_3881(atpB) SSON_3882(atpE)
                 SSON_3883(atpF) SSON_3884(atpH) SSON_3885(atpA)
                 SSON_3886(atpG) SSON_3887(atpD) SSON_3888(atpC)
                 SSO_P111(spa47)
            SBO: SBO_3750(atpE) SBO_3751(atpF) SBO_3752(atpH) SBO_3753(atpA)
                 SBO_3754(atpG) SBO_3755(atpD) SBO_3756(atpC)
            SDY: SDY_4010(atpB) SDY_4011(atpE) SDY_4012(atpF) SDY_4013(atpH)
                 SDY_4014(atpA) SDY_4015(atpG) SDY_4016(atpD) SDY_4017(atpC)
                 SDY_P187(spa47)
            ECA: ECA1723(fliI) ECA2083(hrcN) ECA4511(atpC) ECA4512(atpD)
                 ECA4513(atpG) ECA4514(atpA) ECA4515(atpH) ECA4516(atpF)
                 ECA4517(atpE) ECA4518(atpB)
            PLU: plu0039(atpC) plu0040(atpD) plu0041(atpG) plu0042(atpA)
                 plu0043(atpH) plu0044(atpF) plu0045(atpE) plu0046(atpB)
                 plu1945(fliI) plu3767(sctN)
            BUC: BU002(atpB) BU003(atpE) BU004(atpF) BU005(atpH) BU006(atpA)
                 BU007(atpG) BU008(atpD) BU009(atpC) BU076(fliI)
            BAS: BUsg002(atpB) BUsg003(atpE) BUsg004(atpF) BUsg005(atpH)
                 BUsg006(atpA) BUsg007(atpG) BUsg008(atpD) BUsg009(atpC)
                 BUsg070(fliI)
            BAB: bbp002(atpB) bbp003(atpE) bbp004(atpF) bbp005(atpH)
                 bbp006(atpA) bbp007(atpG) bbp008(atpD) bbp009(atpC)
                 bbp071(fliI)
            BCC: BCc_046(fliI)
            WBR: WGLp002(atpB) WGLp003(atpE) WGLp004(atpF) WGLp005(atpH)
                 WGLp006(atpA) WGLp007(atpG) WGLp008(atpD) WGLp009(atpC)
                 WGLp057(fliI)
            SGL: SG0050 SG0565 SG1301 SG2088 SG2408 SG2409 SG2410 SG2411
                 SG2412 SG2413 SG2414 SG2415
            ENT: Ent638_4129
            KPN: KPN_04140(atpH)
            SPE: Spro_0002 Spro_0005 Spro_0006 Spro_0007
            BFL: Bfl002(atpB) Bfl003(atpE) Bfl004(atpF) Bfl005(atpH)
                 Bfl006(atpA) Bfl007(atpG) Bfl008(atpD) Bfl009(atpC)
            BPN: BPEN_002(atpB) BPEN_003(atpE) BPEN_004(atpF) BPEN_005(atpH)
                 BPEN_006(atpA) BPEN_007(atpG) BPEN_008(atpD) BPEN_009(atpC)
            HIN: HI0478(atpC) HI0479(atpD) HI0480(atpG) HI0481(atpA)
                 HI0482(atpH) HI0483(atpF) HI0484(atpE) HI0485(atpB)
            HIT: NTHI0608(atpC) NTHI0609(atpD) NTHI0610(atpG) NTHI0611(atpA)
                 NTHI0612(atpH) NTHI0613(atpF) NTHI0614(atpE) NTHI0615(atpB)
            HIP: CGSHiEE_00555 CGSHiEE_00560 CGSHiEE_00565 CGSHiEE_00570
                 CGSHiEE_00575 CGSHiEE_00580 CGSHiEE_00585 CGSHiEE_00590
            HIQ: CGSHiGG_05645(atpC) CGSHiGG_05650 CGSHiGG_05655 CGSHiGG_05660
                 CGSHiGG_05665 CGSHiGG_05670 CGSHiGG_05675 CGSHiGG_05680
                 CGSHiGG_05685
            HDU: HD0004(atpB) HD0005(atpE) HD0006(atpF) HD0007(atpH)
                 HD0008(atpA) HD0009(atpG) HD0010(atpD) HD0011(atpC)
            HSO: HS_1695(atpC) HS_1696(atpD) HS_1697(atpG) HS_1698(atpA)
                 HS_1699(atpH) HS_1700(atpF) HS_1701(atpE) HS_1702(atpB)
            PMU: PM1488(atpB) PM1489(atpE) PM1490(atpF) PM1491(atpH)
                 PM1492(atpA) PM1493(atpG) PM1494(atpD) PM1495(atpC)
            MSU: MS2345(atpC) MS2346(atpD) MS2347(atpG) MS2348(atpA)
                 MS2349(atpH) MS2350(atpF) MS2351(atpE) MS2352(atpB)
            APL: APL_1645(atpC) APL_1646(atpD) APL_1647(atpG) APL_1648(atpA)
                 APL_1649(atpH) APL_1650(atpF) APL_1651(atpE) APL_1652(atpB)
            ASU: Asuc_0327 Asuc_0328 Asuc_0329
            XFA: XF1142 XF1143 XF1144 XF1145 XF1146 XF1147 XF1148 XF1149
            XFT: PD0427(atpC) PD0428(atpD) PD0429(atpG) PD0430(atpA)
                 PD0431(atpH) PD0432(atpF) PD0433(atpE) PD0434
            XCC: XCC0548(atpB) XCC0549(atpE) XCC0550(atpF) XCC0551(atpH)
                 XCC0552(atpA) XCC0553(atpG) XCC0554(atpD) XCC0555(atpC)
                 XCC1236(hrcN) XCC1923(fliI)
            XCB: XC_2263 XC_3006 XC_3677 XC_3678 XC_3679 XC_3680 XC_3681
                 XC_3682 XC_3683 XC_3684
            XCV: XCV0432(hrcN) XCV1995(fliI) XCV3766(atpC) XCV3767(atpD)
                 XCV3768(atpG) XCV3769(atpA) XCV3770(atpH) XCV3771(atpF)
                 XCV3772(atpE) XCV3773(atpB)
            XAC: XAC0412(hrcN) XAC1951(fliI) XAC3648(atpC) XAC3649(atpD)
                 XAC3650(atpG) XAC3651(atpA) XAC3652(atpH) XAC3653(atpF)
                 XAC3654(atpE) XAC3655(atpB)
            XOO: XOO0091(hrcN) XOO0726(atpB) XOO0727(atpE) XOO0728(atpF)
                 XOO0729(atpH) XOO0730(atpA) XOO0731(atpG) XOO0732(atpD)
                 XOO0733(atpC) XOO2604(fliI)
            XOM: XOO_0085(XOO0085) XOO_0662(XOO0662) XOO_0663(XOO0663)
                 XOO_0664(XOO0664) XOO_0665(XOO0665) XOO_0666(XOO0666)
                 XOO_0667(XOO0667) XOO_0668(XOO0668) XOO_0669(XOO0669)
                 XOO_2463(XOO2463)
            VCH: VC2130(fliI) VC2763 VC2764 VC2765 VC2766 VC2767 VC2768 VC2769
                 VC2770
            VCO: VC0395_A1714(fliI) VC0395_A2523(atpE) VC0395_A2524(atpF)
                 VC0395_A2525(atpH) VC0395_A2526(atpA) VC0395_A2527(atpG)
                 VC0395_A2528(atpD) VC0395_A2529(atpC)
            VVU: VV1_1015 VV1_1016 VV1_1017 VV1_1018 VV1_1019 VV1_1020
                 VV1_1021 VV1_1022 VV1_1938
            VVY: VV2478(fliI) VV3250 VV3251 VV3252 VV3253 VV3254 VV3255 VV3256
                 VV3257
            VPA: VP1668 VP2246(fliI) VP3068 VP3069 VP3070 VP3071 VP3072 VP3073
                 VP3074 VP3075 VPA1338(yscN) VPA1533
            VFI: VF1849 VF2563 VF2564 VF2565 VF2566 VF2567 VF2568 VF2569
                 VF2570
            PPR: PBPRA0025 PBPRA0926(fliI) PBPRA3603(atpC) PBPRA3604 PBPRA3605
                 PBPRA3606 PBPRA3607 PBPRA3608 PBPRA3609 PBPRA3610 PBPRB0130
                 PBPRB0131 PBPRB0132 PBPRB0133 PBPRB0134 PBPRB0135 PBPRB0136
                 PBPRB0137(atpC)
            PAE: PA1104(fliI) PA1697 PA5553(atpC) PA5554(atpD) PA5555(atpG)
                 PA5556(at) PA5557(atpH) PA5558(atpF) PA5559(atpE) PA5560(atpB)
            PAU: PA14_42570(pscN) PA14_50100(fliI) PA14_73230(atpC)
                 PA14_73240(atpD) PA14_73250(atpG) PA14_73260(atpA)
                 PA14_73280(atpH) PA14_73290(atpF) PA14_73300(atpE)
                 PA14_73310(atpB)
            PAP: PSPA7_4267(fliI) PSPA7_6355(atpC) PSPA7_6356(atpD)
                 PSPA7_6357(atpG) PSPA7_6358(atpA) PSPA7_6359(atpH)
                 PSPA7_6360(atpF) PSPA7_6361 PSPA7_6362(atpB)
            PPU: PP_4366(fliI) PP_5412(atpC) PP_5413(atpD) PP_5414(atpG)
                 PP_5415(atpA) PP_5416(atpH) PP_5417(atpF) PP_5418(atpE)
                 PP_5419(atpB)
            PPF: Pput_5295 Pput_5296 Pput_5297
            PST: PSPTO_1400(hrcN) PSPTO_1961(fliI) PSPTO_5598(atpC)
                 PSPTO_5599(atpD) PSPTO_5600(atpG) PSPTO_5601(atpA)
                 PSPTO_5602(atpH) PSPTO_5603(atpF) PSPTO_5604(atpE)
                 PSPTO_5605(atpB)
            PSB: Psyr_1213 Psyr_3454 Psyr_5120 Psyr_5121 Psyr_5122 Psyr_5123
                 Psyr_5124 Psyr_5125 Psyr_5126 Psyr_5127
            PSP: PSPPH_1290(hrcN) PSPPH_2530 PSPPH_3380(fliI) PSPPH_5206(atpC)
                 PSPPH_5207(atpD) PSPPH_5208(atpG) PSPPH_5209(atpA)
                 PSPPH_5210(atpH) PSPPH_5211(atpF) PSPPH_5212(atpE)
                 PSPPH_5213(atpB) PSPPH_5214(atpI)
            PFL: PFL_1641(fliI) PFL_6215(atpC) PFL_6216(atpD) PFL_6217(atpG)
                 PFL_6218(atpA) PFL_6219(atpH) PFL_6220(atpF) PFL_6221(atpE)
                 PFL_6222(atpB)
            PFO: Pfl_1539 Pfl_5729 Pfl_5730 Pfl_5731 Pfl_5732 Pfl_5733
                 Pfl_5734 Pfl_5735 Pfl_5736
            PEN: PSEEN3813(fliI) PSEEN5541(atpC) PSEEN5542(atpD)
                 PSEEN5543(atpG) PSEEN5544(atpA) PSEEN5545(atpH)
                 PSEEN5546(atpF) PSEEN5547(atpE) PSEEN5549(atpB)
            PMY: Pmen_3573 Pmen_4606 Pmen_4608 Pmen_4609
            PAR: Psyc_2023(atpC) Psyc_2024(atpD) Psyc_2025(atpG)
                 Psyc_2026(atpA) Psyc_2027(atpH) Psyc_2028(atpF)
                 Psyc_2029(atpE) Psyc_2030
            PCR: Pcryo_2326 Pcryo_2329 Pcryo_2330 Pcryo_2331 Pcryo_2332
                 Pcryo_2333
            PRW: PsycPRwf_0191 PsycPRwf_0192 PsycPRwf_0749
            ACI: ACIAD0180(atpB) ACIAD0182(atpE) ACIAD0183(atpF)
                 ACIAD0184(atpH) ACIAD0185(atpA) ACIAD0186(atpG)
                 ACIAD0187(atpD) ACIAD0188(atpC)
            ACB: A1S_0150
            SON: SO_3225(fliI) SO_4746(atpC) SO_4747(atpD) SO_4748(atpG)
                 SO_4749(atpA) SO_4750(atpH) SO_4751(atpF) SO_4752(atpE)
                 SO_4753(atpB)
            SDN: Sden_3656 Sden_3751 Sden_3752 Sden_3754 Sden_3755 Sden_3756
                 Sden_3757 Sden_3758
            SFR: Sfri_3049 Sfri_3050 Sfri_3053 Sfri_3054 Sfri_3055 Sfri_3056
                 Sfri_3057 Sfri_4044 Sfri_4045 Sfri_4046 Sfri_4047 Sfri_4048
                 Sfri_4049 Sfri_4050 Sfri_4051
            SAZ: Sama_3648 Sama_3649
            SBL: Sbal_4370 Sbal_4371
            SBM: Shew185_0049 Shew185_4366 Shew185_4367 Shew185_4368
                 Shew185_4371
            SLO: Shew_3849 Shew_3850
            SSE: Ssed_4487 Ssed_4488 Ssed_4489
            SPL: Spea_4241 Spea_4242 Spea_4243
            SHE: Shewmr4_1285 Shewmr4_3924 Shewmr4_3925 Shewmr4_3926
                 Shewmr4_3927 Shewmr4_3928 Shewmr4_3929 Shewmr4_3930
                 Shewmr4_3931
            SHM: Shewmr7_1352 Shewmr7_4016 Shewmr7_4017 Shewmr7_4018
                 Shewmr7_4019 Shewmr7_4020 Shewmr7_4021 Shewmr7_4022
                 Shewmr7_4023
            SHN: Shewana3_1345 Shewana3_4129 Shewana3_4130 Shewana3_4131
                 Shewana3_4132 Shewana3_4133 Shewana3_4134 Shewana3_4135
                 Shewana3_4136
            SHW: Sputw3181_4057 Sputw3181_4058
            ILO: IL1197(fliI) IL2618(atpC) IL2619(atpD) IL2620(atpG)
                 IL2621(atpA) IL2622(atpH) IL2623(atpF) IL2624(atpE)
                 IL2625(atpB)
            CPS: CPS_0056(atpB) CPS_0057(atpE) CPS_0058(atpF) CPS_0059(atpH)
                 CPS_0060(atpA) CPS_0061(atpG) CPS_0062(atpD) CPS_0063(atpC)
                 CPS_1505(fliI)
            PHA: PSHAa0795(fliI) PSHAa3007(atpC) PSHAa3008(atpD)
                 PSHAa3009(atpG) PSHAa3010(atpA) PSHAa3011(atpH)
                 PSHAa3012(atpF) PSHAa3013(atpE) PSHAa3014(atpB)
            PAT: Patl_4294 Patl_4299 Patl_4301
            SDE: Sde_2185 Sde_3965 Sde_3968 Sde_3969 Sde_3970 Sde_3971
                 Sde_3972
            PIN: Ping_3729 Ping_3733 Ping_3734 Ping_3735
            MAQ: Maqu_3874 Maqu_3878 Maqu_3879 Maqu_3880
            CBU: CBU_1939(atpB) CBU_1940(atpE) CBU_1941(atpF) CBU_1942(atpH)
                 CBU_1943(atpA) CBU_1944(atpG) CBU_1945(atpD) CBU_1946(atpC)
            CBD: COXBU7E912_0174(atpC) COXBU7E912_0176(atpD)
                 COXBU7E912_0177(atpG) COXBU7E912_0178(atpA)
                 COXBU7E912_0179(atpH) COXBU7E912_0180(atpF)
                 COXBU7E912_0181(atpE) COXBU7E912_0182(atpB)
                 COXBU7E912_0183(atpI)
            LPN: lpg1047(atpG) lpg1048 lpg1049 lpg1050 lpg1051(atpA) lpg1053
                 lpg1054(atpD) lpg1757(fliI) lpg2981(atpC) lpg2982(atpD)
                 lpg2983(atpG) lpg2984 lpg2985(atpH) lpg2986(atpF)
                 lpg2987(atpE) lpg2988(atpB)
            LPF: lpl1721(fliI) lpl2909(atpC) lpl2910(atpD) lpl2911(atpG)
                 lpl2912(atpA) lpl2913(atpH) lpl2914(atpF) lpl2915(atpE)
                 lpl2916(atpB)
            LPP: lpp1721(fliI) lpp2328 lpp2329(atpC) lpp2331 lpp2332 lpp2333
                 lpp2334 lpp2335 lpp3052(atpC) lpp3053(atpD) lpp3054(atpG)
                 lpp3055(atpA) lpp3056(atpH) lpp3057(atpF) lpp3058(atpE)
                 lpp3059(atpB)
            MCA: MCA0006(atpB-1) MCA0007(atpE-1) MCA0008(atpF) MCA0009(atpH)
                 MCA0010(atpA-1) MCA0011(atpG-1) MCA0012(atpD-1)
                 MCA0013(atpC-1) MCA1556(atpD) MCA1557 MCA2699(atpB-2)
                 MCA2700(atpE-2) MCA2701 MCA2707(atpA-2) MCA2708(atpG-2)
                 MCA3021(atpC-2)
            FTU: FTT0058(atpB) FTT0059(atpE) FTT0060(atpF) FTT0061(atpH)
                 FTT0062(atpA) FTT0063(atpG) FTT0064(atpD) FTT0065(atpC)
            FTF: FTF0058(atpB) FTF0059(atpE) FTF0060(atpF) FTF0061(atpH)
                 FTF0062(atpA) FTF0063(atpG) FTF0064(atpD) FTF0065(atpC)
            FTW: FTW_0134(atpB) FTW_0135(atpE) FTW_0136(atpF) FTW_0137(atpH)
                 FTW_0138(atpA) FTW_0139(atpG) FTW_0140(atpD) FTW_0141(atpC)
            FTL: FTL_1794 FTL_1795 FTL_1796 FTL_1797 FTL_1798 FTL_1799
                 FTL_1800 FTL_1801
            FTH: FTH_1731(atpC) FTH_1732(atpD) FTH_1733(atpG) FTH_1734(atpA)
                 FTH_1735(atpH) FTH_1736(atpF) FTH_1737(atpE) FTH_1738(atpB)
            FTA: FTA_1901(atpC) FTA_1902(atpD) FTA_1903(atpG) FTA_1904(atpA)
                 FTA_1905(atpH) FTA_1906(atpF) FTA_1908(atpB)
            FTN: FTN_1645(atpC) FTN_1646(atpD) FTN_1647(atpG) FTN_1648(atpA)
                 FTN_1649(atpH) FTN_1650(atpF) FTN_1651(atpE) FTN_1652(atpB)
            TCX: Tcr_1439 Tcr_2164 Tcr_2165 Tcr_2166 Tcr_2167 Tcr_2168
                 Tcr_2169 Tcr_2170 Tcr_2171
            NOC: Noc_2081 Noc_2082 Noc_2083 Noc_3073 Noc_3074 Noc_3075
                 Noc_3076 Noc_3077 Noc_3078 Noc_3079 Noc_3080
            AEH: Mlg_0712 Mlg_2868 Mlg_2869 Mlg_2870 Mlg_2871 Mlg_2872
                 Mlg_2873 Mlg_2874 Mlg_2875
            HHA: Hhal_2434 Hhal_2435
            HCH: HCH_00915(atpG1) HCH_00917(atpA1) HCH_00918(atpF1)
                 HCH_00919(atpE1) HCH_00920(atpB1) HCH_00922(atpC1)
                 HCH_00923(atpD1) HCH_03268 HCH_04075(fliI1) HCH_05107(yscN)
                 HCH_05190(fliI2) HCH_07070(atpC2) HCH_07071(atpD2)
                 HCH_07072(atpG2) HCH_07073(atpA2) HCH_07075(atpH)
                 HCH_07076(atpF2) HCH_07077(atpE2) HCH_07078(atpB2)
            CSA: Csal_3283 Csal_3285 Csal_3286 Csal_3287 Csal_3288 Csal_3289
                 Csal_3290
            ABO: ABO_2725(atpC) ABO_2726(atpD) ABO_2727(atpG) ABO_2728(atpA)
                 ABO_2729(atpH) ABO_2730(atpF) ABO_2731(atpE) ABO_2732(atpB)
                 ABO_2733(atpI)
            MMW: Mmwyl1_1961 Mmwyl1_3445 Mmwyl1_4462 Mmwyl1_4463 Mmwyl1_4464
                 Mmwyl1_4481
            AHA: AHA_1368(fliI) AHA_4261(atpC) AHA_4262(atpD) AHA_4263(atpG)
                 AHA_4264(atpA) AHA_4265(atpH) AHA_4266(atpF) AHA_4267(atpE)
                 AHA_4268(atpB) AHA_4269(atpI)
            DNO: DNO_1141(atpC) DNO_1142(atpD) DNO_1143(atpG) DNO_1144(atpA)
                 DNO_1145(atpH) DNO_1146(atpF) DNO_1147(atpE) DNO_1148(atpB)
            BCI: BCI_0140(atpC) BCI_0141(atpD) BCI_0142(atpG) BCI_0143(atpA)
                 BCI_0144(atpH) BCI_0145(atpF) BCI_0146(atpE) BCI_0147(atpB)
            CRP: CRP_003 CRP_004 CRP_007 CRP_008 CRP_009
            RMA: Rmag_1044 Rmag_1050
            VOK: COSY_0944(atpC) COSY_0945(atpD) COSY_0946(atpG)
                 COSY_0947(atpA) COSY_0948(atpH) COSY_0949(atpF)
                 COSY_0950(atpE) COSY_0951(atpB)
            NME: NMB1933 NMB1934 NMB1935 NMB1936 NMB1937 NMB1938 NMB1939
                 NMB1940
            NMA: NMA0513(atpB) NMA0514(atpE) NMA0515(atpF) NMA0516(atpH)
                 NMA0517(atpA) NMA0518(atpG) NMA0519(atpD) NMA0520(atpC)
            NMC: NMC1905(atpC) NMC1906(atpD) NMC1907(atpG) NMC1908(atpA)
                 NMC1909(atpH) NMC1910(atpF) NMC1911(atpE) NMC1912(atpB)
            NGO: NGO2144 NGO2145(atpE) NGO2146(atpF) NGO2147(atpH)
                 NGO2148(atpA) NGO2149(atpG) NGO2150(atpD) NGO2151(atpC)
            CVI: CV_0666(atpB) CV_0667(atpE) CV_0668(atpF) CV_0669(atpH)
                 CV_0670(atpA) CV_0671(atpG) CV_0672(atpD) CV_0673(atpC)
                 CV_2628(invC) CV_2996(fliI2) CV_3134(fliI1)
            RSO: RSc3316(atpC1) RSc3317(atpD) RSc3318(atpG) RSc3319(atpA)
                 RSc3320(atpH) RSc3321(atpF) RSc3322(atpE) RSc3323(atpB)
                 RSp0393(fliI) RSp0810(atpC2) RSp0870(hrcN)
            REU: Reut_A3345 Reut_A3346 Reut_A3347 Reut_A3348 Reut_A3349
                 Reut_A3350 Reut_A3351 Reut_A3352
            REH: H16_A3636(atpC) H16_A3637(atpD) H16_A3638(atpG)
                 H16_A3639(atpA) H16_A3640(atpH) H16_A3641(atpF)
                 H16_A3642(atpE) H16_A3643(atpB) H16_A3644(atpI)
                 H16_B2371(fliI)
            RME: Rmet_3493 Rmet_3494 Rmet_3495 Rmet_3496 Rmet_3497 Rmet_3498
                 Rmet_3499 Rmet_3500 Rmet_5264
            BMA: BMA2951(atpB-1) BMA2952(atpE-1) BMA2953(atpF) BMA2954(atpH)
                 BMA2955(atpA-1) BMA2956(atpG) BMA2957(atpD-1) BMA2958(atpC-1)
                 BMA3278(fliI) BMAA0123(atpD-2) BMAA0124(atpC-2)
                 BMAA0127(atpB-2) BMAA0128(atpE-2) BMAA0129 BMAA0130(atpA-2)
                 BMAA0131 BMAA1540(bsaS) BMAA1637(sctN)
            BMV: BMASAVP1_1289(atpD) BMASAVP1_1291(atpC-2)
                 BMASAVP1_1294(atpB-2) BMASAVP1_1295(atpE-2) BMASAVP1_1296
                 BMASAVP1_1297(atpA-2) BMASAVP1_A2943(fliI)
                 BMASAVP1_A3354(atpC-1) BMASAVP1_A3355(atpD-1)
                 BMASAVP1_A3356(atpG) BMASAVP1_A3357(atpA-1)
                 BMASAVP1_A3358(atpH) BMASAVP1_A3359(atpF) BMASAVP1_A3360(atpE)
                 BMASAVP1_A3361(atpB)
            BML: BMA10299_A1586(atpC-1) BMA10299_A1587(atpD-1)
                 BMA10299_A1588(atpG) BMA10299_A1589(atpA-1)
                 BMA10299_A1590(atpH) BMA10299_A1591(atpF) BMA10299_A1592(atpE)
                 BMA10299_A1593(atpB) BMA10299_A2145(fliI)
            BMN: BMA10247_3009(atpB) BMA10247_3010(atpE) BMA10247_3011(atpF)
                 BMA10247_3012(atpH) BMA10247_3013(atpA-1) BMA10247_3014(atpG)
                 BMA10247_3015(atpD-1) BMA10247_3016(atpC-1)
                 BMA10247_A0147(atpD) BMA10247_A0148(atpC-2)
                 BMA10247_A0151(atpB-2) BMA10247_A0152(atpE-2) BMA10247_A0153
                 BMA10247_A0154(atpA-2)
            BXE: Bxe_A0034 Bxe_A0035 Bxe_A0036 Bxe_A0037 Bxe_A0038 Bxe_A0039
                 Bxe_A0040 Bxe_A0041 Bxe_A0163 Bxe_A1879 Bxe_A1880 Bxe_A1882
                 Bxe_A1883 Bxe_A1884 Bxe_A1885 Bxe_A1886 Bxe_A3118 Bxe_C0042
                 Bxe_C0043 Bxe_C0044 Bxe_C0045 Bxe_C0046 Bxe_C0048 Bxe_C0049
            BVI: Bcep1808_0112 Bcep1808_0116
            BUR: Bcep18194_A3282 Bcep18194_A3283 Bcep18194_A3284
                 Bcep18194_A3285 Bcep18194_A3286 Bcep18194_A3287
                 Bcep18194_A3288 Bcep18194_A3289
            BCN: Bcen_2453 Bcen_2948 Bcen_2950 Bcen_2951 Bcen_2952 Bcen_2953
                 Bcen_2954 Bcen_2955 Bcen_3492
            BCH: Bcen2424_0100 Bcen2424_0101 Bcen2424_0102 Bcen2424_0103
                 Bcen2424_0104 Bcen2424_0105 Bcen2424_0106 Bcen2424_0107
                 Bcen2424_3067 Bcen2424_4874
            BAM: Bamb_0091 Bamb_0092 Bamb_0093 Bamb_0094 Bamb_0095 Bamb_0096
                 Bamb_0097 Bamb_0098 Bamb_3112 Bamb_5851
            BPS: BPSL0227(fliI) BPSL3395(atpC) BPSL3396(atpD) BPSL3397(atpG)
                 BPSL3398(atpA) BPSL3399(atpH) BPSL3400(atpF) BPSL3401(atpE)
                 BPSL3402(atpB) BPSS1394(sctN) BPSS1541(bsaS) BPSS1627
                 BPSS1945(atpG) BPSS1946(atpA) BPSS1947 BPSS1948(atpE) BPSS1949
                 BPSS1952 BPSS1953(atpD)
            BPM: BURPS1710b_0177(atpC) BURPS1710b_0179(atpD)
                 BURPS1710b_0180(atpG) BURPS1710b_0181(atpA)
                 BURPS1710b_0182(atpH) BURPS1710b_0183(atpF)
                 BURPS1710b_0184(atpE) BURPS1710b_0185(atpB)
                 BURPS1710b_0414(fliI) BURPS1710b_A0422 BURPS1710b_A0582(bsaS)
                 BURPS1710b_A0686 BURPS1710b_A1047(atpG) BURPS1710b_A1048(atpA)
                 BURPS1710b_A1049(atpF) BURPS1710b_A1051(atpE)
                 BURPS1710b_A1052(atpB) BURPS1710b_A1055(atpC-2)
                 BURPS1710b_A1056(atpD)
            BPL: BURPS1106A_0231(fliI) BURPS1106A_4041(atpC)
                 BURPS1106A_4042(atpD) BURPS1106A_4043(atpG)
                 BURPS1106A_4044(atpA) BURPS1106A_4045(atpH)
                 BURPS1106A_4046(atpF) BURPS1106A_4047(atpE)
                 BURPS1106A_4048(atpB) BURPS1106A_A1898 BURPS1106A_A2205
                 BURPS1106A_A2645(atpA) BURPS1106A_A2647(atpE)
                 BURPS1106A_A2648(atpB) BURPS1106A_A2652(atpD)
            BPD: BURPS668_0219(fliI) BURPS668_3967(atpC) BURPS668_3968(atpD)
                 BURPS668_3969(atpG) BURPS668_3970(atpA) BURPS668_3971(atpH)
                 BURPS668_3972(atpF) BURPS668_3973(atpE) BURPS668_3974(atpB)
                 BURPS668_A0226(fliI) BURPS668_A1990 BURPS668_A2288
                 BURPS668_A2787(atpA) BURPS668_A2789(atpE) BURPS668_A2790(atpB)
                 BURPS668_A2794(atpD)
            BTE: BTH_I0197(fliI) BTH_I3307(atpC) BTH_I3308(atpD-1)
                 BTH_I3309(atpG-1) BTH_I3310(atpA-1) BTH_I3311(atpH)
                 BTH_I3312(atpF) BTH_I3313 BTH_I3314(atpB-1) BTH_II0174(fliI)
                 BTH_II0419(atpD-2) BTH_II0420 BTH_II0423(atpB-2) BTH_II0424
                 BTH_II0425 BTH_II0426(atpA-2) BTH_II0427(atpG-2)
                 BTH_II0744(sctN) BTH_II0832(bsaS)
            PNU: Pnuc_0021 Pnuc_0027
            BPE: BP1400(fliI) BP2245(bscN) BP3282(atpB) BP3283(atpE)
                 BP3284(atpF) BP3285(atpH) BP3286(atpA) BP3287(atpG)
                 BP3288(atpD) BP3289(atpC)
            BPA: BPP1507(fliI) BPP2231(bscN) BPP4134(atpC) BPP4135(atpD)
                 BPP4136(atpG) BPP4137(atpA) BPP4138(atpH) BPP4139(atpF)
                 BPP4140(atpE) BPP4141(atpB)
            BBR: BB1628(bscN) BB2585(fliI) BB4604(atpC) BB4605(atpD)
                 BB4606(atpG) BB4607(atpA) BB4608(atpH) BB4609(atpF)
                 BB4610(atpE) BB4611(atpB)
            RFR: Rfer_0105 Rfer_0106 Rfer_0107 Rfer_0109 Rfer_0110 Rfer_0111
                 Rfer_0112 Rfer_1162 Rfer_1165 Rfer_1166 Rfer_1167 Rfer_1169
            POL: Bpro_0321 Bpro_0322 Bpro_0323 Bpro_0324 Bpro_0328
            PNA: Pnap_0250 Pnap_0256
            AAV: Aave_0367 Aave_0373
            AJS: Ajs_0303 Ajs_0309
            VEI: Veis_0475
            MPT: Mpe_A0191 Mpe_A0192 Mpe_A0193 Mpe_A0194 Mpe_A0195 Mpe_A0196
                 Mpe_A0197 Mpe_A0198 Mpe_A0568(fliI)
            HAR: HEAR3404(atpC) HEAR3405(atpD) HEAR3406(atpG) HEAR3408(atpH)
                 HEAR3409(atpF) HEAR3410(atpE) HEAR3411(atpB)
            MMS: mma_1438(fliI) mma_3626 mma_3627 mma_3628 mma_3629 mma_3630
                 mma_3631 mma_3632 mma_3633
            NEU: NE0200(atpB) NE0201(atpE) NE0202(atpF) NE0203(atpH)
                 NE0204(atpA) NE0205(atpG) NE0206(atpD) NE0207(atpC)
                 NE2086(fliI)
            NET: Neut_0271 Neut_0272 Neut_0273 Neut_0274 Neut_0275 Neut_0276
                 Neut_0277 Neut_0278 Neut_0742 Neut_2013 Neut_2014 Neut_2017
                 Neut_2018 Neut_2019 Neut_2020 Neut_2021
            NMU: Nmul_A0304 Nmul_A0305 Nmul_A0306 Nmul_A0307 Nmul_A0308
                 Nmul_A0309 Nmul_A0310 Nmul_A0311 Nmul_A1348 Nmul_A1653
                 Nmul_A1655 Nmul_A1656 Nmul_A1657 Nmul_A1660
            EBA: ebA2999(atpB) ebA3000(atpE) ebA3002(atpF) ebA3003(atpH)
                 ebA3004(atpA) ebA3006(atpG) ebA3007(atpD) ebA3008(atpC)
            AZO: azo0153(atpB) azo0154(atpE) azo0156(atpH) azo0160(atpC)
                 azo2719(fliI)
            DAR: Daro_0770 Daro_4108 Daro_4109 Daro_4110 Daro_4111 Daro_4112
                 Daro_4113 Daro_4114 Daro_4115
            TBD: Tbd_1091(fliI) Tbd_1603(fliI) Tbd_2796 Tbd_2797 Tbd_2798
                 Tbd_2799 Tbd_2800 Tbd_2801 Tbd_2802 Tbd_2803
            MFA: Mfla_2743 Mfla_2744 Mfla_2745 Mfla_2746 Mfla_2747 Mfla_2748
                 Mfla_2749 Mfla_2750
            HPY: HP0828(atpB) HP1131(atpC) HP1132(atpD) HP1133(atpG)
                 HP1134(atpA) HP1135(atpH) HP1136(atpF) HP1137(atpF')
                 HP1212(atpE) HP1420(fliI)
            HPJ: jhp0767(atpB) jhp1059(atpC) jhp1060(atpD) jhp1061(atpG)
                 jhp1062(atpA) jhp1063(atpH) jhp1064(atpF) jhp1065(atpX)
                 jhp1135(atpE) jhp1315(fliI)
            HPA: HPAG1_0528 HPAG1_0604 HPAG1_0814 HPAG1_1069 HPAG1_1070
                 HPAG1_1071 HPAG1_1072 HPAG1_1073 HPAG1_1074 HPAG1_1075
                 HPAG1_1153 HPAG1_1346
            HHE: HH0424(atpF) HH0425(atpF') HH0426(atpH) HH0427(atpA)
                 HH0428(atpG) HH0429(atpD) HH0430(atpC) HH0565(fliI)
                 HH0593(atpE) HH1497(atpB)
            HAC: Hac_0106(fliI) Hac_0577(atpF') Hac_0578(atpF) Hac_0579(atpH)
                 Hac_0580(atpA) Hac_0581(atpG) Hac_0582(atpD) Hac_0583(atpC)
                 Hac_1196(atpB) Hac_1590(atpE)
            WSU: WS0318(atpB) WS0511(atpF') WS0512(atpF) WS0513(atpH)
                 WS0514(atpA) WS0515(atpG) WS0516(atpD) WS0517(atpC)
                 WS2207(fliI)
            TDN: Tmden_0429 Tmden_1339 Tmden_1402 Tmden_1403 Tmden_1404
                 Tmden_1405 Tmden_1406 Tmden_1407 Tmden_1408 Tmden_2085
            CJE: Cj0102(atpF') Cj0103(atpF) Cj0104(atpH) Cj0105(atpA)
                 Cj0106(atpG) Cj0107(atpD) Cj0108(atpC) Cj0195(fliI)
                 Cj0936(atpE) Cj1204c(atpB)
            CJR: CJE0097 CJE0098 CJE0099(atpH) CJE0100(atpA) CJE0101(atpG)
                 CJE0102(atpD) CJE0103(atpC) CJE0188(fliI) CJE1014(atpE)
                 CJE1338(atpB)
            CJJ: CJJ81176_0137 CJJ81176_0138 CJJ81176_0139(atpH)
                 CJJ81176_0140(atpA) CJJ81176_0141(atpG) CJJ81176_0142(atpD)
                 CJJ81176_0143(atpC) CJJ81176_0226(fliI) CJJ81176_0943(atpE)
                 CJJ81176_1219(atpB)
            CJU: C8J_0095(atpF') C8J_0096(atpF) C8J_0097(atpH) C8J_0098(atpA)
                 C8J_0099(atpG) C8J_0100(atpD) C8J_0101(atpC) C8J_0184(fliI)
                 C8J_0873(atpE) C8J_1147(atpB)
            CJD: JJD26997_0109 JJD26997_0110 JJD26997_0111(atpH)
                 JJD26997_0112(atpA) JJD26997_0113(atpG) JJD26997_0114(atpD)
                 JJD26997_0115(atpC) JJD26997_0205(fliI) JJD26997_0526(atpB)
                 JJD26997_0878(atpE)
            CFF: CFF8240_0771(atpB) CFF8240_1281 CFF8240_1524(atpC)
                 CFF8240_1525(atpD) CFF8240_1526(atpG) CFF8240_1527(atpA)
                 CFF8240_1528(atpH) CFF8240_1695(fliI)
            CCV: CCV52592_0790(atpB) CCV52592_0957 CCV52592_1299
                 CCV52592_1495(fliI) CCV52592_1656 CCV52592_1735(atpH)
                 CCV52592_1736(atpA) CCV52592_1737(atpG) CCV52592_1738(atpD)
                 CCV52592_1739(atpC)
            CHA: CHAB381_0646 CHAB381_0685(atpA) CHAB381_0686(atpG)
                 CHAB381_0687(atpD) CHAB381_0688(atpC) CHAB381_0723(atpB)
            CCO: CCC13826_0137(atpD) CCC13826_0159(atpB) CCC13826_0283
                 CCC13826_0914(atpH) CCC13826_0915(atpA) CCC13826_0916(atpG)
                 CCC13826_0917(atpD) CCC13826_0918(atpC) CCC13826_1502
                 CCC13826_1777(fliI)
            ABU: Abu_1289(ktrB) Abu_1594(atpC) Abu_1595(atpD) Abu_1596(atpG)
                 Abu_1597(atpA) Abu_1598(atpH) Abu_1599(atpF) Abu_1600(atpF')
                 Abu_1748(atpE) Abu_1940(fliI) Abu_2030(atpB)
            NIS: NIS_0853(atpB) NIS_1219(atpC) NIS_1220(atpD) NIS_1221(atpG)
                 NIS_1222(atpA) NIS_1223(atpH) NIS_1224 NIS_1225
            SUN: SUN_1582(atpB) SUN_1770(atpC) SUN_1771(atpD) SUN_1772(atpG)
                 SUN_1773(atpA) SUN_1774(atpH) SUN_1775(atpF) SUN_1776(atpF')
                 SUN_1883(atpE)
            GSU: GSU0108 GSU0109(atpF) GSU0110(atpH) GSU0111(atpA)
                 GSU0112(atpG) GSU0113(atpD) GSU0114(atpC) GSU0333(atpE)
                 GSU0334(atpB) GSU0413(fliI)
            GME: Gmet_3109 Gmet_3359 Gmet_3360 Gmet_3405 Gmet_3406 Gmet_3407
                 Gmet_3408 Gmet_3409 Gmet_3410 Gmet_3411
            GUR: Gura_0418 Gura_4210 Gura_4260 Gura_4261 Gura_4262
            PCA: Pcar_0015 Pcar_0016 Pcar_0944 Pcar_0945 Pcar_0946 Pcar_0947
                 Pcar_0948 Pcar_0949 Pcar_0950 Pcar_0951 Pcar_0952
                 Pcar_1189(fliI) Pcar_2989 Pcar_2990 Pcar_2993 Pcar_2994
                 Pcar_2995 Pcar_2996 Pcar_2997 Pcar_3130 Pcar_3131 Pcar_3132
                 Pcar_3133 Pcar_3134 Pcar_3135 Pcar_3136
            DVU: DVU0310(fliI) DVU0774(atpC) DVU0775(atpD) DVU0776(atpG)
                 DVU0777(atpA) DVU0778(atpH) DVU0779 DVU0780 DVU0917(atpE)
                 DVU0918(atpB) DVUA0119
            DDE: Dde_0984 Dde_0985 Dde_0986 Dde_0987 Dde_0988 Dde_0989
                 Dde_0990 Dde_2700 Dde_2701
            LIP: LI0398 LI0399(atpF) LI0400(atpE) LI0401(atpD) LI0402(atpC)
                 LI0403(atpB) LI0404(atpA) LI0540(sctN) LI0854(fliI)
                 LI1057(atpA) LI1058(atpC)
            BBA: Bd0009(atpB) Bd0010(atpE) Bd3401(fliI) Bd3896(atpC)
                 Bd3897(atpB) Bd3898(atpG) Bd3899(atpA) Bd3900(atpD)
                 Bd3902(atpF) Bd3903(atpF)
            DPS: DP0815 DP0816 DP0829(atpX) DP0830(atpF) DP0831(atpD)
                 DP0832(atpA) DP0833(atpG) DP0834(atpB) DP0835(atpE)
                 DP2659(fliI)
            ADE: Adeh_1197 Adeh_1198 Adeh_1200 Adeh_1201 Adeh_1204 Adeh_4338
                 Adeh_4339 Adeh_4340 Adeh_4347 Adeh_4351
            AFW: Anae109_2216 Anae109_4487 Anae109_4496 Anae109_4497
                 Anae109_4498
            MXA: MXAN_0402(atpB) MXAN_0403(atpE) MXAN_0404(atpF)
                 MXAN_6921(atpC) MXAN_6923(atpD) MXAN_6925(atpG)
                 MXAN_7026(atpH) MXAN_7028(atpA)
            SAT: SYN_00543 SYN_00544 SYN_00545 SYN_00546 SYN_00547 SYN_00548
                 SYN_00549 SYN_00588 SYN_01473 SYN_02098 SYN_02101 SYN_02102
                 SYN_02103 SYN_02104 SYN_02105 SYN_02965
            SFU: Sfum_1604 Sfum_1605 Sfum_2581 Sfum_2582 Sfum_2583 Sfum_2584
                 Sfum_2585 Sfum_2586 Sfum_2587
            RPR: RP020(atpF) RP021(atpX) RP022(atpE) RP023(atpB) RP800(atpC)
                 RP801(atpD) RP802(atpG) RP803(atpA) RP804(atpH)
            RTY: RT0105(atpB) RT0106(atpE) RT0107(atpX) RT0108(atpF)
                 RT0787(atpC) RT0788(atpD) RT0789(atpG) RT0790(atpA)
                 RT0791(atpH)
            RCO: RC0024(atpF) RC0025(atpX) RC0026(atpE) RC0027(atpB)
                 RC1234(atpC) RC1235(atpD) RC1236(atpG) RC1237(atpA)
                 RC1238(atpH)
            RFE: RF_0027(atpF) RF_0028(atpX) RF_0030(atpB) RF_1269(atpH)
            RBE: RBE_0092(atpH) RBE_0095(atpG) RBE_0096(atpD) RBE_1290(atpB)
                 RBE_1291(atpE) RBE_1292(atpX) RBE_1293(atpF)
            RAK: A1C_00250 A1C_00255 A1C_00260 A1C_00265 A1C_06185(atpC)
                 A1C_06190 A1C_06195 A1C_06200 A1C_06205
            RBO: A1I_00400 A1I_00405 A1I_00410 A1I_00415 A1I_07450(atpC)
                 A1I_07460 A1I_07465 A1I_07470 A1I_07475
            RCM: A1E_00085 A1E_00090 A1E_00095 A1E_00120 A1E_05100(atpC)
                 A1E_05105 A1E_05110 A1E_05115 A1E_05120
            RRI: A1G_00160 A1G_00165 A1G_00170 A1G_00175 A1G_06755(atpC)
                 A1G_06760 A1G_06765 A1G_06770 A1G_06775
            OTS: OTBS_0577(atpG) OTBS_0771
            WOL: WD0203(atpD) WD0204 WD0427(atpB) WD0428(atpE) WD0429 WD0430
                 WD0655(atpA) WD0656(atpH) WD1233(atpG)
            WBM: Wbm0314 Wbm0315 Wbm0457 Wbm0458 Wbm0459 Wbm0460 Wbm0688
                 Wbm0689 Wbm0705
            AMA: AM1110(atpB) AM1112(atpE) AM1113 AM1114 AM1116(trkH)
                 AM1174(atpA) AM1175(atpH) AM620(atpG) AM665(atpC) AM666(atpD)
            APH: APH_0493(atpC) APH_0494(atpD) APH_0707(atpG) APH_0813
                 APH_1189 APH_1190 APH_1191(atpE) APH_1192(atpB) APH_1334(atpA)
                 APH_1335(atpH)
            ERU: Erum0820(atpA) Erum0830(atpH) Erum3990(atpG) Erum4580(atpC)
                 Erum4590(atpD) Erum8360(atpB) Erum8370(atpE) Erum8380(atpF)
                 Erum8390
            ERW: ERWE_CDS_00770(atpA) ERWE_CDS_00780(atpH)
                 ERWE_CDS_04120(atpG) ERWE_CDS_04800(atpC) ERWE_CDS_04810(atpD)
                 ERWE_CDS_08870(atpB) ERWE_CDS_08880(atpE) ERWE_CDS_08890(atpX)
                 ERWE_CDS_08900
            ERG: ERGA_CDS_00740(atpA) ERGA_CDS_00750(atpH)
                 ERGA_CDS_04070(atpG) ERGA_CDS_04700(atpC) ERGA_CDS_04710(atpD)
                 ERGA_CDS_08780(atpB) ERGA_CDS_08790(atpE) ERGA_CDS_08800(atpX)
                 ERGA_CDS_08810
            ECN: Ecaj_0082 Ecaj_0083 Ecaj_0388 Ecaj_0459 Ecaj_0460 Ecaj_0872
                 Ecaj_0873 Ecaj_0874 Ecaj_0875
            ECH: ECH_0131(atpH) ECH_0132(atpA) ECH_0573(atpD) ECH_0574(atpC)
                 ECH_0652(atpG) ECH_1086(atpB) ECH_1087(atpE) ECH_1088(atpX)
                 ECH_1089(atpF)
            NSE: NSE_0131(atpA) NSE_0132(atpH) NSE_0396(atpB) NSE_0397(atpE)
                 NSE_0398(atpX) NSE_0588(atpG) NSE_0762(atpC) NSE_0763(atpD)
            PUB: SAR11_0116(atpB) SAR11_0117(atpE) SAR11_0118 SAR11_0119(atpF)
                 SAR11_0229(atpC) SAR11_0230(atpD) SAR11_0231(atpG)
                 SAR11_0232(atpA) SAR11_0233(atpH)
            MLO: mll4059 mll4060 mll4063 mll4065 mll4066 mlr2909 mlr6342
                 mlr7411 mlr7413 mlr7415 msr7412
            MES: Meso_0107 Meso_0300 Meso_0696 Meso_0697 Meso_0698 Meso_0699
                 Meso_3215 Meso_3216 Meso_3217 Meso_3218 Meso_3219
            PLA: Plav_0697 Plav_1462 Plav_1464
            SME: SMc00868(atpF) SMc00869(atpF2) SMc00870(atpE) SMc00871(atpB)
                 SMc02498(atpH) SMc02499(atpA) SMc02500(atpG) SMc02501(atpD)
                 SMc02502(atpC) SMc03025(fliI)
            SMD: Smed_0447 Smed_2923 Smed_2925
            ATU: Atu0557(fliI) Atu0714(atpA) Atu0715(atpC) Atu0716(atpB)
                 Atu0717(atpF) Atu2621(atpC) Atu2622(atpD) Atu2623(atpG)
                 Atu2624(atpA) Atu2625(atpH)
            ATC: AGR_C_1295 AGR_C_1297 AGR_C_1299 AGR_C_1301 AGR_C_4751
                 AGR_C_4754 AGR_C_4756 AGR_C_4757 AGR_C_4759 AGR_C_980
            RET: RHE_CH00656(fliI) RHE_CH00864(atpB) RHE_CH00865(atpE)
                 RHE_CH00866(atpF1) RHE_CH00867(atpF2) RHE_CH03869(atpC)
                 RHE_CH03870(atpD) RHE_CH03871(atpG) RHE_CH03872(atpA)
                 RHE_CH03873(atpH) RHE_PD00057(hrcN)
            RLE: RL0705(fliI) RL0925(atpB) RL0926(atpC) RL0927(atpG)
                 RL0928(atpF) RL4405(atpC) RL4407(atpD) RL4408(atpG)
                 RL4409(atpA) RL4410(atpH)
            BME: BMEI0248 BMEI0249 BMEI0250 BMEI0251 BMEI0252 BMEI1543
                 BMEI1544 BMEI1545 BMEI1546 BMEII1105
            BMF: BAB1_0411 BAB1_0412(atpE) BAB1_0413 BAB1_0414(atpF)
                 BAB1_1806(atpC) BAB1_1807(atpD) BAB1_1808 BAB1_1809(atpA)
                 BAB1_1810(atpH) BAB2_0129(fliI)
            BMS: BR0382(atpB) BR0383(atpE) BR0384 BR0385(atpF) BR1798(atpC)
                 BR1799(atpD) BR1800(atpG) BR1801(atpA) BR1802(atpH)
                 BRA0129(fliI)
            BMB: BruAb1_0407(atpB) BruAb1_0408(atpE) BruAb1_0409
                 BruAb1_0410(atpF) BruAb1_1778(atpC) BruAb1_1779(atpD)
                 BruAb1_1780(atpG) BruAb1_1781(atpA) BruAb1_1782(atpH)
                 BruAb2_0127(fliI)
            BOV: BOV_0394(atpB) BOV_0395(atpE) BOV_0397(atpF) BOV_1731(atpC)
                 BOV_1732(atpD) BOV_1733(atpG) BOV_1734(atpA) BOV_1735(atpH)
                 BOV_A0120
            OAN: Oant_0500 Oant_1102 Oant_1104 Oant_2514
            BJA: bll0439(atpC) bll0440(atpD) bll0441(atpG) bll0442(atpA)
                 bll0443(atpH) bll1185(atpB) bll1186(atpB') bll1188(atpA)
                 blr1816(rhcN) blr2201(fliI) blr6885(fliI) bsl1187(atpC)
            BRA: BRADO0416(atpH) BRADO0417(atpA) BRADO0418(atpG)
                 BRADO0419(atpD) BRADO0420(atpC) BRADO1498(fliI)
                 BRADO6685(atpI) BRADO6686(atpB) BRADO6687(atpE)
                 BRADO6688(atpB') BRADO6689(atpF)
            BBT: BBta_0405(atpH) BBta_0406(atpA) BBta_0407(atpG)
                 BBta_0408(atpD) BBta_0409(atpC) BBta_0843(atpF)
                 BBta_0844(atpB') BBta_0846(atpB) BBta_1435 BBta_1436 BBta_1439
                 BBta_1440(atpD) BBta_6532(fliI)
            RPA: RPA0175(atpC) RPA0176(atpD) RPA0177(atpG) RPA0178(atpA)
                 RPA0179(atpH) RPA0843(atpF1) RPA0844(atpF2) RPA0845(atpE)
                 RPA0846(atpB) RPA1633(fliI)
            RPB: RPB_0264 RPB_0265 RPB_0266 RPB_0267 RPB_0268 RPB_4571
                 RPB_4572 RPB_4573 RPB_4574
            RPC: RPC_0173 RPC_0174 RPC_0175 RPC_0176 RPC_0177 RPC_1086
                 RPC_4813 RPC_4814 RPC_4815 RPC_4816
            RPD: RPD_0556 RPD_0560 RPD_0827 RPD_0828 RPD_0829 RPD_0830
            RPE: RPE_0279 RPE_0280 RPE_0281 RPE_0282 RPE_0283 RPE_1146
                 RPE_4269 RPE_4776 RPE_4777 RPE_4778 RPE_4779
            NWI: Nwi_0235 Nwi_0236 Nwi_0237 Nwi_0238 Nwi_0429 Nwi_0430
                 Nwi_0431 Nwi_0433 Nwi_0434
            NHA: Nham_0266 Nham_0267 Nham_0268 Nham_0269 Nham_0528 Nham_0529
                 Nham_0531 Nham_0533
            BHE: BH04110(atpB) BH04120(atpE) BH04130(atpF1) BH04140(atpF2)
                 BH15310(atpC) BH15320(atpD) BH15330(atpG) BH15340(atpA)
                 BH15350(atpH)
            BQU: BQ03130(atpB) BQ03140(atpE) BQ03150(atpF1) BQ03160(atpF2)
                 BQ12220(atpC) BQ12230(atpD) BQ12240(atpG) BQ12250(atpA)
                 BQ12260(atpH)
            BBK: BARBAKC583_0111(atpH) BARBAKC583_0112(atpA)
                 BARBAKC583_0113(atpG) BARBAKC583_0114(atpD)
                 BARBAKC583_0115(atpC) BARBAKC583_0376(atpB)
                 BARBAKC583_1145(fliI)
            XAU: Xaut_1979 Xaut_2077 Xaut_2079
            CCR: CC_0365 CC_0366 CC_0367 CC_0368 CC_3040(fliI) CC_3445 CC_3447
                 CC_3448 CC_3449 CC_3450
            SIL: SPO0183(fliI) SPO3161(atpC) SPO3162(atpD) SPO3163(atpG)
                 SPO3164(atpA) SPO3165(atpH) SPO3233(atpF) SPO3234
                 SPO3235(atpE) SPO3236(atpB)
            SIT: TM1040_2085 TM1040_2089 TM1040_2591 TM1040_2592 TM1040_2593
                 TM1040_2594 TM1040_2966
            RSP: RSP_0056(fliI) RSP_1035(atpF) RSP_1036(atpX) RSP_1037(atpE)
                 RSP_1038(atpB) RSP_1332 RSP_2296(atpH) RSP_2297(atpA)
                 RSP_2298(atpG) RSP_2299(atpD) RSP_2300(atpC) RSP_3929(atpD)
                 RSP_3930(atpC-1) RSP_3933 RSP_3935(atpA) RSP_3936 RSP_7012
            RSQ: Rsph17025_2202
            JAN: Jann_0767 Jann_0768 Jann_0769 Jann_0770 Jann_1046 Jann_1050
                 Jann_4199
            RDE: RD1_0251(fliI) RD1_1321(atpI) RD1_1322(atpB) RD1_1323(atpE)
                 RD1_1324(atpX) RD1_1325(atpF) RD1_3532(atpC) RD1_3533(atpD)
                 RD1_3534(atpG) RD1_3535(atpA) RD1_3536(atpH)
            MMR: Mmar10_0670 Mmar10_2201 Mmar10_2202 Mmar10_2203 Mmar10_2204
                 Mmar10_2800 Mmar10_2802 Mmar10_2803 Mmar10_2804 Mmar10_2805
            HNE: HNE_0268(fliI) HNE_1891(atpC) HNE_1892(atpD) HNE_1893(atpG)
                 HNE_1894(atpA) HNE_1895(atpH) HNE_1919(atpB) HNE_1920(atpE)
            ZMO: ZMO0238(atpH) ZMO0239(atpA) ZMO0240(atpG) ZMO0241(atpD)
                 ZMO0242(atpC) ZMO0637(fliI) ZMO0667(atpB) ZMO0668(atpE)
                 ZMO0669(atpG) ZMO0671(atpF)
            NAR: Saro_1316 Saro_1317 Saro_1318 Saro_1319 Saro_2399 Saro_2403
            SAL: Sala_1076 Sala_1077 Sala_1078 Sala_1079 Sala_2289 Sala_2933
            SWI: Swit_0620 Swit_0622 Swit_1290 Swit_4483
            ELI: ELI_07525 ELI_07530 ELI_07535 ELI_08765 ELI_08770 ELI_08775
                 ELI_08785 ELI_08790
            GOX: GOX1110 GOX1111 GOX1112 GOX1113 GOX1310 GOX1311 GOX1312
                 GOX1313 GOX1314 GOX1694 GOX2167 GOX2168 GOX2171 GOX2172
                 GOX2173 GOX2174 GOX2175
            GBE: GbCGDNIH1_1866 GbCGDNIH1_1867 GbCGDNIH1_1868 GbCGDNIH1_1869
                 GbCGDNIH1_1870 GbCGDNIH1_2055 GbCGDNIH1_2056 GbCGDNIH1_2057
                 GbCGDNIH1_2058 GbCGDNIH1_2059
            ACR: Acry_0397 Acry_1678 Acry_1680
            RRU: Rru_A0526 Rru_A1223 Rru_A1227 Rru_A3245 Rru_A3246
            MAG: amb3993 amb3994 amb3995 amb3996 amb4138 amb4139 amb4140
                 amb4141 amb4142
            MGM: Mmc1_0272 Mmc1_3457 Mmc1_3458 Mmc1_3459 Mmc1_3460 Mmc1_3461
                 Mmc1_3674 Mmc1_3675 Mmc1_3676
            ABA: Acid345_1299 Acid345_1300 Acid345_4331 Acid345_4332
                 Acid345_4335
            SUS: Acid_0766
            BSU: BG10243(fliI) BG10815(atpB) BG10816(atpE) BG10817(atpF)
                 BG10818(atpH) BG10819(atpA) BG10820(atpG) BG10821(atpD)
                 BG10822(atpC)
            BHA: BH2455(fliI) BH3753(atpC) BH3754(atpD) BH3755(atpG)
                 BH3756(atpA) BH3757(atpH) BH3758(atpF) BH3759(atpE)
                 BH3760(atpB)
            BAN: BA1681 BA5546(atpC) BA5547(atpD) BA5548(atpG) BA5549(atpA)
                 BA5550(atpH) BA5551(atpF) BA5552(atpE) BA5553(atpB)
            BAR: GBAA1681 GBAA5546(atpC) GBAA5547(atpD) GBAA5548(atpG)
                 GBAA5549(atpA) GBAA5550(atpH) GBAA5551(atpF) GBAA5552(atpE)
                 GBAA5553(atpB)
            BAA: BA_0401 BA_0402 BA_0403 BA_0404 BA_0405 BA_0406 BA_0407
                 BA_0408 BA_2197
            BAT: BAS1563 BAS5154 BAS5155 BAS5156 BAS5157 BAS5158 BAS5159
                 BAS5160 BAS5161
            BCE: BC1647 BC5305 BC5306 BC5307 BC5308 BC5309 BC5310 BC5311
                 BC5312
            BCA: BCE_1769 BCE_5429(atpC) BCE_5430(atpD) BCE_5431(atpG)
                 BCE_5432(atpA) BCE_5433(atpH) BCE_5434(atpF) BCE_5435(atpE)
                 BCE_5436(atpB)
            BCZ: BCZK1526(fliI) BCZK4519(atpI) BCZK5004(atpC) BCZK5005(atpD)
                 BCZK5006(atpG) BCZK5007(atpA) BCZK5008(atpH) BCZK5009(atpF)
                 BCZK5010(atpE) BCZK5011(atpB) BCZK5012(atpI)
            BCY: Bcer98_1037 Bcer98_1045 Bcer98_1115 Bcer98_3826 Bcer98_3827
            BTK: BT9727_1537(fliI) BT9727_4503(atpI) BT9727_4986(atpC)
                 BT9727_4987(atpD) BT9727_4988(atpG) BT9727_4990(atpA)
                 BT9727_4991(atpH) BT9727_4992(atpF) BT9727_4993(atpE)
                 BT9727_4994(atpB) BT9727_4995(atpI)
            BTL: BALH_4807(atpC) BALH_4811(atpH) BALH_4812(atpF) BALH_4813
            BLI: BL01269(fliI) BL03994(atpB) BL03996(atpF) BL03997(atpH)
                 BL03998(atpA) BL03999(atpG) BL04000(atpD) BL04001(atpC)
            BLD: BLi01844(fliI) BLi03925(atpC) BLi03926(atpD) BLi03927(atpG)
                 BLi03928(atpA) BLi03929(atpH) BLi03930(atpF) BLi03931(atpE)
                 BLi03932(atpB)
            BCL: ABC2266(fliI) ABC3850(atpC) ABC3851(atpD) ABC3852(atpG)
                 ABC3853(atpA) ABC3854(atpH) ABC3855(atpF) ABC3856(atpE)
                 ABC3857(atpB)
            BAY: RBAM_033960
            BPU: BPUM_1522(fliI) BPUM_3325 BPUM_3326 BPUM_3327 BPUM_3328
                 BPUM_3329 BPUM_3330 BPUM_3331 BPUM_3332 BPUM_3333
            OIH: OB1558(fliI) OB2974(atpC) OB2975(atpD) OB2976(atpG)
                 OB2977(atpA) OB2978(atpH) OB2979(atpF) OB2980(atpE)
                 OB2981(atpB) OB2982(atpI)
            GKA: GK1222(fliI) GK3357 GK3358 GK3359 GK3360 GK3361 GK3362 GK3363
                 GK3364 GK3365
            GTN: GTNG_3303
            SAU: SA1904(atpC) SA1905(atpD) SA1906(atpG) SA1907(atpA)
                 SA1908(atpH) SA1909(atpF) SA1910(atpE) SA1911(atpB)
            SAV: SAV2102(atpC) SAV2103(atpD) SAV2104(atpG) SAV2105(atpA)
                 SAV2106(atpH) SAV2107(atpF) SAV2108(atpE) SAV2109(atpB)
            SAM: MW2026(atpC) MW2027(atpD) MW2028(atpG) MW2029(atpA)
                 MW2030(atpH) MW2031(atpF) MW2032(atpE) MW2033(atpB)
            SAR: SAR2190(atpC) SAR2191(atpD) SAR2192(atpG) SAR2193(atpA)
                 SAR2194(atpH) SAR2195(atpF) SAR2196(atpE) SAR2197(atpB)
            SAS: SAS2005 SAS2006 SAS2007 SAS2008 SAS2009 SAS2010 SAS2011
                 SAS2012
            SAC: SACOL2094(atpC) SACOL2095(atpD) SACOL2096(atpG)
                 SACOL2097(atpA) SACOL2098(atpH) SACOL2099(atpF)
                 SACOL2100(atpE) SACOL2101(atpB)
            SAB: SAB1986c(atpC) SAB1987c(atpD) SAB1988c(atpG) SAB1989c(atpA)
                 SAB1990c(atpH) SAB1991c(atpF) SAB1992c(atpE) SAB1993c(atpB)
            SAA: SAUSA300_2057(atpC) SAUSA300_2058(atpD) SAUSA300_2059(atpG)
                 SAUSA300_2060(atpA) SAUSA300_2061(atpH) SAUSA300_2062(atpF)
                 SAUSA300_2063(atpE) SAUSA300_2064(atpB)
            SAO: SAOUHSC_02340 SAOUHSC_02341 SAOUHSC_02343 SAOUHSC_02345
                 SAOUHSC_02346 SAOUHSC_02347 SAOUHSC_02349 SAOUHSC_02350
            SAJ: SaurJH9_1082 SaurJH9_2065 SaurJH9_2140 SaurJH9_2141
                 SaurJH9_2142
            SAH: SaurJH1_1104 SaurJH1_2102 SaurJH1_2178 SaurJH1_2179
                 SaurJH1_2180
            SEP: SE1699 SE1700 SE1701 SE1702 SE1703 SE1704 SE1705 SE1706
            SER: SERP1708(atpC) SERP1709(atpD) SERP1710(atpG) SERP1711(atpA)
                 SERP1712(atpH) SERP1713(atpF) SERP1714(atpE) SERP1715(atpB)
            SHA: SH0926(atpB) SH0927(atpE) SH0928(atpF) SH0929(atpH)
                 SH0930(atpA) SH0931(atpG) SH0932(atpD) SH0933(atpC)
            SSP: SSP0775 SSP0776 SSP0777 SSP0778 SSP0779 SSP0780 SSP0781
                 SSP0782
            LMO: lmo0088 lmo0089 lmo0090 lmo0091 lmo0092 lmo0093 lmo0716
                 lmo2528(atpC) lmo2529(atpD) lmo2530(atpG) lmo2531(atpA)
                 lmo2532(atpH) lmo2533(atpF) lmo2534(atpE) lmo2535(atpB)
            LMF: LMOf2365_0105 LMOf2365_0106 LMOf2365_0107(atpA-1)
                 LMOf2365_0108 LMOf2365_0109(atpD-1) LMOf2365_0110
                 LMOf2365_0752(fliI) LMOf2365_2501(atpC) LMOf2365_2502(atpD-2)
                 LMOf2365_2503(atpG) LMOf2365_2504(atpA-2) LMOf2365_2505(atpH)
                 LMOf2365_2506(atpF) LMOf2365_2507(atpE) LMOf2365_2508(atpB)
            LIN: lin0134 lin0135 lin0136 lin0137 lin0138 lin0139 lin0724
                 lin2672(atpC) lin2673(atpD) lin2674(atpG) lin2675(atpA)
                 lin2676(atpH) lin2677(atpF) lin2678(atpE) lin2679(atpB)
            LWE: lwe0421 lwe0422 lwe0423(atpA) lwe0424(atpG) lwe0425(atpD)
                 lwe0426(atpC) lwe0685 lwe2040 lwe2476(atpC) lwe2477(atpD)
                 lwe2478(atpG) lwe2479(atpA) lwe2480(atpH) lwe2481(atpF)
                 lwe2482(atpE) lwe2483(atpB) lwe2484(atpI)
            LLA: L10679(atpH) L11208(atpF) L11729(atpB) L11729a(atpE)
                 L5953(atpE) L6563(atpD) L8105(atpG) L8990(atpA)
            LLC: LACR_1932 LACR_1933 LACR_1934 LACR_1935 LACR_1936 LACR_1937
                 LACR_1938 LACR_1939
            LLM: llmg_1945(atpC) llmg_1946(atpD) llmg_1947(atpG)
                 llmg_1948(atpA) llmg_1949(atpH) llmg_1950(atpF)
                 llmg_1951(atpB)
            SPY: SPy_0754(atpE) SPy_0755(atpB) SPy_0756(atpF) SPy_0757(atpH)
                 SPy_0758(atpA) SPy_0759(atpG) SPy_0760(atpD) SPy_0761(atpC)
            SPZ: M5005_Spy_0575(atpE) M5005_Spy_0576(atpB)
                 M5005_Spy_0577(atpF) M5005_Spy_0578(atpH) M5005_Spy_0579(atpA)
                 M5005_Spy_0580(atpG) M5005_Spy_0581(atpD) M5005_Spy_0582(atpC)
            SPM: spyM18_0812(atpL7) spyM18_0813(atpB) spyM18_0814(atpF)
                 spyM18_0815(atpH) spyM18_0816(atpA) spyM18_0817(atpG)
                 spyM18_0818(atpD) spyM18_0819(atpE)
            SPG: SpyM3_0493 SpyM3_0494 SpyM3_0495 SpyM3_0496 SpyM3_0497
                 SpyM3_0498 SpyM3_0499 SpyM3_0500
            SPS: SPs1354 SPs1355 SPs1356 SPs1357 SPs1358 SPs1359 SPs1360
                 SPs1361
            SPH: MGAS10270_Spy0630(atpE) MGAS10270_Spy0631(atpB)
                 MGAS10270_Spy0632(atpF) MGAS10270_Spy0633(atpH)
                 MGAS10270_Spy0634(atpA) MGAS10270_Spy0635(atpG)
                 MGAS10270_Spy0636(atpD) MGAS10270_Spy0637(atpC)
            SPI: MGAS10750_Spy0659(atpE) MGAS10750_Spy0660(atpB)
                 MGAS10750_Spy0661(atpF) MGAS10750_Spy0662(atpH)
                 MGAS10750_Spy0663(atpA) MGAS10750_Spy0664(atpG)
                 MGAS10750_Spy0665(atpD) MGAS10750_Spy0666(atpC)
            SPJ: MGAS2096_Spy0637(atpE) MGAS2096_Spy0638(atpB)
                 MGAS2096_Spy0639(atpF) MGAS2096_Spy0640(atpH)
                 MGAS2096_Spy0641(atpA) MGAS2096_Spy0642(atpG)
                 MGAS2096_Spy0643(atpD) MGAS2096_Spy0644(atpC)
            SPK: MGAS9429_Spy0629(atpE) MGAS9429_Spy0630(atpB)
                 MGAS9429_Spy0631(atpF) MGAS9429_Spy0632(atpH)
                 MGAS9429_Spy0633(atpA) MGAS9429_Spy0634(atpG)
                 MGAS9429_Spy0635(atpD) MGAS9429_Spy0636(atpC)
            SPF: SpyM51226(atpC) SpyM51227(atpD) SpyM51228(atpG)
                 SpyM51229(atpA) SpyM51230(atpH) SpyM51231(atpF)
                 SpyM51232(atpB) SpyM51233(atpE)
            SPA: M6_Spy0592 M6_Spy0593 M6_Spy0594 M6_Spy0595 M6_Spy0596
                 M6_Spy0597 M6_Spy0598 M6_Spy0599
            SPB: M28_Spy0553(atpE) M28_Spy0554(atpB) M28_Spy0555(atpF)
                 M28_Spy0556(atpH) M28_Spy0557(atpA) M28_Spy0558(atpG)
                 M28_Spy0559(atpD) M28_Spy0560(atpC)
            SPN: SP_1507 SP_1508 SP_1509 SP_1510 SP_1511 SP_1512 SP_1513
                 SP_1514
            SPR: spr1359(atpC) spr1360(atpD) spr1361(atpG) spr1362(atpA)
                 spr1363(atpH) spr1364(atpF) spr1365(atpB) spr1366(atpE)
            SPD: SPD_1334(atpC) SPD_1335(atpD) SPD_1336(atpG) SPD_1337(atpA)
                 SPD_1338(atpH) SPD_1339(atpF) SPD_1340(atpB) SPD_1341(atpE)
            SAG: SAG0857(atpE) SAG0858(atpB) SAG0859(atpF) SAG0860(atpH)
                 SAG0861(atpA) SAG0862(atpG) SAG0863(atpD) SAG0864(atpC)
            SAN: gbs0875(atpE) gbs0876(atpB) gbs0877(atpF) gbs0878(atpH)
                 gbs0879(atpA) gbs0880(atpG) gbs0881(atpD) gbs0882(atpC)
            SAK: SAK_0980(atpE) SAK_0981(atpB) SAK_0982(atpF) SAK_0983(atpH)
                 SAK_0984(atpA) SAK_0985(atpG) SAK_0986(atpD) SAK_0987(atpC)
            SMU: SMU.1527(atpA) SMU.1528(atpB) SMU.1529(atpC) SMU.1530(atpD)
                 SMU.1531(atpE) SMU.1532(atpF) SMU.1533(atpG) SMU.1534(atpH)
            STC: str0478(atpE) str0479(atpB) str0480(atpF) str0481(atpH)
                 str0482(atpA) str0483(atpG) str0484(atpD) str0485(atpC)
            STL: stu0478(atpE) stu0479(atpB) stu0480(atpF) stu0481(atpH)
                 stu0482(atpA) stu0483(atpG) stu0484(atpD) stu0485(atpC)
            STE: STER_0516
            SSA: SSA_0782(uncE) SSA_0783(uncB) SSA_0784(uncF) SSA_0785(uncH)
                 SSA_0786(uncA) SSA_0787(uncG) SSA_0788(uncD) SSA_0789(uncC)
            SGO: SGO_0130(atpK) SGO_0131 SGO_0135 SGO_0137 SGO_1320(ntpJ)
                 SGO_1541(atpC) SGO_1542(atpD) SGO_1543(atpG) SGO_1544(atpA)
                 SGO_1545(atpH) SGO_1546(atpF) SGO_1547(atpB) SGO_1548(atpE)
            LPL: lp_2363(atpC) lp_2364(atpD) lp_2365(atpG) lp_2366(atpA)
                 lp_2367(atpH) lp_2368(atpF) lp_2369(atpE) lp_2370(atpB)
            LJO: LJ0934 LJ0935 LJ0936 LJ0937 LJ0938 LJ0939 LJ0940 LJ0941
            LAC: LBA0772 LBA0773 LBA0774 LBA0775 LBA0776 LBA0777 LBA0778
                 LBA0779
            LSA: LSA1125(atpC) LSA1126(atpD) LSA1127(atpG) LSA1128(atpA)
                 LSA1129(atpH) LSA1130(atpF) LSA1131(atpE) LSA1132(atpB)
            LSL: LSL_0594(atpB) LSL_0595(atpE) LSL_0596(atpF) LSL_0597(atpH)
                 LSL_0598(atpA) LSL_0599(atpG) LSL_0600(atpD) LSL_0601(atpC)
            LDB: Ldb0705(atpB) Ldb0706(atpE) Ldb0707(atpF) Ldb0708(atpH)
                 Ldb0709(atpA) Ldb0710(atpG) Ldb0711(atpD) Ldb0712(atpC)
            LBU: LBUL_0637 LBUL_0638 LBUL_0639 LBUL_0640 LBUL_0641 LBUL_0642
                 LBUL_0643 LBUL_0644
            LBR: LVIS_1278 LVIS_1279 LVIS_1280 LVIS_1281 LVIS_1282 LVIS_1283
                 LVIS_1284 LVIS_1285
            LCA: LSEI_1160 LSEI_1161 LSEI_1162 LSEI_1163 LSEI_1164 LSEI_1165
                 LSEI_1166 LSEI_1167
            LRE: Lreu_0464 Lreu_0465 Lreu_0466 Lreu_1558
            PPE: PEPE_1323
            EFA: EF1493 EF1494 EF1495 EF1496 EF1497 EF1498 EF1499 EF1500
                 EF2607(atpC) EF2608(atpD) EF2609(atpG) EF2610(atpA)
                 EF2611(atpH) EF2612(atpF) EF2613(atpE) EF2614(atpB)
            OOE: OEOE_0659 OEOE_0660 OEOE_0661 OEOE_0662 OEOE_0663 OEOE_0664
                 OEOE_0665 OEOE_0666
            LME: LEUM_1875
            STH: STH1115(mutS2) STH3000(fliI) STH85 STH86 STH87 STH88 STH89
                 STH90 STH91 STH92
            CAC: CAC2159(fliL) CAC2864(atpC) CAC2865(atpD) CAC2866(atpG)
                 CAC2867(atpA) CAC2868(atpH) CAC2869(atpF) CAC2870(atpE)
                 CAC2871(atpB)
            CPE: CPE2186(atpE) CPE2187(atpB) CPE2188(atpG) CPE2189(atpA)
                 CPE2190(atpD) CPE2191(atpF) CPE2192(atpL) CPE2193(atpI)
            CPF: CPF_1888 CPF_1889 CPF_1890 CPF_1891 CPF_1892 CPF_1893
                 CPF_1894 CPF_1895 CPF_2451(atpC) CPF_2452(atpD) CPF_2453(atpG)
                 CPF_2454(atpA) CPF_2455(atpH) CPF_2456(atpF) CPF_2457(atpE)
                 CPF_2458(atpB)
            CPR: CPR_1607 CPR_1608 CPR_1609 CPR_1610 CPR_1611 CPR_1612
                 CPR_1613 CPR_1614 CPR_2161(atpC) CPR_2162(atpD) CPR_2163(atpG)
                 CPR_2164(atpA) CPR_2165(atpH) CPR_2166(atpF) CPR_2167(atpE)
                 CPR_2168(atpB)
            CTC: CTC01673
            CNO: NT01CX_0529(atpC) NT01CX_0530(atpD) NT01CX_0531(atpG)
                 NT01CX_0532(atpA) NT01CX_0533(atpH) NT01CX_0534(atpF)
                 NT01CX_0535 NT01CX_0536(atpB) NT01CX_1642(atpI)
                 NT01CX_1643(atpK) NT01CX_1644 NT01CX_1645 NT01CX_1646
                 NT01CX_1647 NT01CX_1648(atpB) NT01CX_1649 NT01CX_1905
            CDF: CD0251(fliI) CD2956A(ntpG) CD2957(ntpC) CD2958(ntpE)
                 CD2959(ntpK) CD3467(atpC) CD3468(atpD) CD3469(atpG)
                 CD3470(atpA) CD3471(atpH) CD3472(atpF) CD3474(atpB)
            CBO: CBO0150(atpA) CBO0151(atpC) CBO0152(atpB) CBO0154(atpA)
                 CBO0156(atpD) CBO0157(atpC) CBO2625A(ntpG) CBO2626(ntpC)
                 CBO2627(ntpE) CBO2628(ntpK) CBO2659(fliI)
            CBA: CLB_0186(atpB) CLB_0187(atpE) CLB_0188(atpF) CLB_0189(atpH)
                 CLB_0190(atpA) CLB_0191(atpG) CLB_0192(atpD) CLB_0193(atpC)
                 CLB_2565 CLB_2602(fliI)
            CBH: CLC_0198(atpB) CLC_0199(atpE) CLC_0200(atpF) CLC_0201(atpH)
                 CLC_0202(atpA) CLC_0203(atpG) CLC_0204(atpD) CLC_0205(atpC)
                 CLC_2496 CLC_2534(fliI)
            CBF: CLI_0205(atpB) CLI_0206(atpE) CLI_0207(atpF) CLI_0208(atpH)
                 CLI_0209(atpA) CLI_0210(atpG) CLI_0211(atpD) CLI_0212(atpC)
                 CLI_2688 CLI_2726(fliI)
            CBE: Cbei_0416 Cbei_0417
            AMT: Amet_0351 Amet_0352 Amet_1636 Amet_2722 Amet_3310
            CHY: CHY_0996(fliI) CHY_2544(atpC) CHY_2545(atpD) CHY_2546(atpG)
                 CHY_2547(atpA) CHY_2548(atpH) CHY_2549(atpF) CHY_2550(atpE)
                 CHY_2551(atpB)
            DSY: DSY2986 DSY4911(atpC) DSY4912(atpD) DSY4913(atpG)
                 DSY4914(atpA) DSY4915(atpH) DSY4916(atpF) DSY4917(atpE)
                 DSY4918(atpB)
            PTH: PTH_2811(atpC)
            SWO: Swol_0852 Swol_2381 Swol_2382 Swol_2383 Swol_2384 Swol_2385
                 Swol_2386 Swol_2387 Swol_2388
            CSC: Csac_1260 Csac_1971 Csac_1972
            TTE: TTE0630(atpB) TTE0631(atpE) TTE0633(atpF) TTE0634(atpH)
                 TTE0635(atpA) TTE0636(atpG) TTE0637(atpD) TTE0638(atpC)
                 TTE1439(fliI)
            MTA: Moth_2377 Moth_2381 Moth_2382 Moth_2383 Moth_2384
            MGE: MG_398(atpC) MG_399(atpD) MG_400(atpG) MG_401(atpA)
                 MG_402(atpH) MG_403(atpF) MG_404(atpE) MG_405(atpB)
            MPN: MPN597(atpC) MPN598(atpD) MPN599(atpG) MPN600(atpA)
                 MPN601(atpH) MPN602(atpF) MPN603(atpE) MPN604(atpB)
            MPU: MYPU_2350(atpA) MYPU_2360(atpD) MYPU_2650(atpC)
                 MYPU_2660(atpD) MYPU_2670(atpG) MYPU_2680(atpA)
                 MYPU_2690(atpH) MYPU_2700(atpF) MYPU_2710(atpE)
                 MYPU_2720(atpB) MYPU_4490(atpA) MYPU_4500(atpD)
                 MYPU_6990(atpD) MYPU_7000(atpA)
            MPE: MYPE560(atpB) MYPE570(atpE) MYPE580(atpF) MYPE590(atpH)
                 MYPE600(atpA) MYPE610(atpG) MYPE620(atpD) MYPE630(atpC)
            MGA: MGA_0488(aptA) MGA_0491(atpD) MGA_1164(atpB) MGA_1167(atpE)
                 MGA_1168(atpF) MGA_1170(atpH) MGA_1172(atpA) MGA_1174(atpG)
                 MGA_1177(atpD) MGA_1179(atpC) MGA_1321d(atpD)
            MMY: MSC_0618(atpD) MSC_0619(atpA) MSC_0884(atpC) MSC_0885(atpD)
                 MSC_0886(atpG) MSC_0887(atpA) MSC_0888(atpH) MSC_0889(atpF)
                 MSC_0890(atpE) MSC_0891(atpB)
            MMO: MMOB1660(atpA) MMOB1670(atpD) MMOB2070(atpC) MMOB2080(atpD)
                 MMOB2090(atpG) MMOB2110(atpA) MMOB2120(atpH) MMOB2130(atpF)
                 MMOB2140(atpE) MMOB2150(atpB) MMOB2960(atpD) MMOB2970(atpA)
            MHY: mhp049(atpB) mhp050(atpE) mhp051(atpF) mhp052(atpH)
                 mhp053(atpA) mhp054(atpG) mhp055(atpD) mhp476(atpD)
                 mhp477(atpA)
            MHJ: MHJ_0043(atpB) MHJ_0044(atpE) MHJ_0045(atpF) MHJ_0046(atpH)
                 MHJ_0047(atpA-1) MHJ_0048(atpG) MHJ_0049(atpD)
                 MHJ_0475(atpD-1) MHJ_0476(atpA)
            MHP: MHP7448_0047(atpB) MHP7448_0048(atpE) MHP7448_0049(atpF)
                 MHP7448_0050(atpH) MHP7448_0051(atpA-1) MHP7448_0052(atpG)
                 MHP7448_0053(atpD) MHP7448_0479(atpA)
            MSY: MS53_0159(atpA-2) MS53_0160(atpD-2) MS53_0404(atpC)
                 MS53_0405(atpD) MS53_0406(atpG) MS53_0407(atpA)
                 MS53_0408(atpH) MS53_0409(atpF) MS53_0410(atpE)
                 MS53_0411(atpB) MS53_0464(atpD-3) MS53_0465(atpA-3)
            MCP: MCAP_0078(atpB) MCAP_0079(atpE) MCAP_0080(atpF)
                 MCAP_0081(atpH) MCAP_0082(atpA1) MCAP_0083(atpG)
                 MCAP_0084(atpD1) MCAP_0085(atpC) MCAP_0358(atpA2)
                 MCAP_0359(atpD2)
            UUR: UU053(atpA-1) UU054(atpD-1) UU128(atpC) UU129(atpD-2)
                 UU130(atpG) UU132(atpA-2) UU133(atpH-1) UU134(atpH-2)
                 UU135(atpF) UU136(atpE) UU137(atpB)
            MFL: Mfl109 Mfl110 Mfl111 Mfl112 Mfl113 Mfl114 Mfl115 Mfl116
            MTU: Rv1304(atpB) Rv1305(atpE) Rv1306(atpF) Rv1307(atpH)
                 Rv1308(atpA) Rv1309(atpG) Rv1310(atpD) Rv1311(atpC)
            MTC: MT1344(atpB) MT1345(atpE) MT1346(atpF) MT1347(atpH)
                 MT1348(atpA) MT1349(atpG) MT1350(atpD) MT1351(atpC)
            MBO: Mb1336(atpB) Mb1337(atpE) Mb1338(atpF) Mb1339(atpH)
                 Mb1340(atpA) Mb1341(atpG) Mb1342(atpD) Mb1343(atpC)
            MBB: BCG_1364(atpB) BCG_1365(atpE) BCG_1366(atpF) BCG_1367(atpH)
                 BCG_1368(atpA) BCG_1369(atpG) BCG_1370(atpD) BCG_1371(atpC)
            MLE: ML1139(atpB) ML1140(atpE) ML1141(atpF) ML1142(atpH)
                 ML1143(atpA) ML1144(atpG) ML1145(atpD) ML1146(atpC)
            MPA: MAP2450c(atpC) MAP2451c(atpD) MAP2452c(atpG) MAP2453c(atpA)
                 MAP2454c(atpH) MAP2455c(atpF) MAP2456c(atpE) MAP2457c(atpB)
            MAV: MAV_1521(atpB) MAV_1522 MAV_1523 MAV_1524 MAV_1525(atpA)
                 MAV_1526(atpG) MAV_1527(atpD) MAV_1528(atpC)
            MSM: MSMEG_4935(atpC) MSMEG_4936(atpD) MSMEG_4937(atpG)
                 MSMEG_4938(atpA) MSMEG_4939 MSMEG_4940 MSMEG_4941(atpE)
                 MSMEG_4942(atpB)
            MMC: Mmcs_3875 Mmcs_3876 Mmcs_3877 Mmcs_3878 Mmcs_3881 Mmcs_3882
            CGL: NCgl1159(cgl1206) NCgl1160(cgl1207) NCgl1161(cgl1208)
                 NCgl1162(cgl1209) NCgl1163(cgl1210) NCgl1164(cgl1211)
                 NCgl1165(cgl1212) NCgl1166(atpC)
            CGB: cg1362(atpB) cg1363(atpE) cg1364(atpF) cg1365(atpH)
                 cg1366(atpA) cg1367(atpG) cg1368(atpD) cg1369(atpC)
            CEF: CE1309(atpB) CE1310(atpE) CE1311(atpF) CE1312(atpH)
                 CE1313(atpA) CE1314(atpG) CE1315(atpB) CE1316(atpC)
            CDI: DIP1046(atpB) DIP1047(atpE) DIP1048(atpF) DIP1049(atpH)
                 DIP1050(atpA) DIP1051(atpG) DIP1052(atpD) DIP1053(atpC)
            CJK: jk1334(atpC) jk1335(atpD) jk1336(atpG) jk1337(atpA)
                 jk1338(atpH) jk1339(atpF) jk1340(atpE) jk1341(atpB)
            NFA: nfa10590(atpB) nfa10600(atpE) nfa10610(atpF) nfa10620(atpH)
                 nfa10630(atpA) nfa10640(atpG) nfa10650(atpD) nfa10660(atpC)
            RHA: RHA1_ro01471(atpC) RHA1_ro01472(atpD) RHA1_ro01473(atpG)
                 RHA1_ro01474(atpA) RHA1_ro01475 RHA1_ro01476(atpF)
                 RHA1_ro01477(atpE) RHA1_ro01478
            SCO: SCO5367(2SC6G5.11) SCO5368(2SC6G5.12) SCO5369(2SC6G5.13)
                 SCO5370(2SC6G5.14) SCO5371(2SC6G5.15) SCO5372(2SC6G5.16)
                 SCO5373(2SC6G5.17) SCO5374(2SC6G5.18)
            SMA: SAV2880(atpC) SAV2881(atpD) SAV2882(atpG) SAV2883(atpA)
                 SAV2884(atpH) SAV2885(atpF) SAV2886(atpE) SAV2887(atpB)
            TWH: TWT423(atpC) TWT424(atpD) TWT425(atpG) TWT426(atpA)
                 TWT427(atpH) TWT428(atpF) TWT429(atpE) TWT430(atpB)
            TWS: TW338(atpB) TW339(atpE) TW340(atpF) TW341(atpH) TW342(atpA)
                 TW343(atpG) TW344(atpD) TW345(atpC)
            LXX: Lxx06360(fliI) Lxx06990(atpB) Lxx07000(atpE) Lxx07010(atpF)
                 Lxx07020(atpH) Lxx07030(atpA) Lxx07040(atpG) Lxx07050(atpD)
                 Lxx07060(atpC)
            CMI: CMM_1163(atpB) CMM_1164(atpE) CMM_1165(atpF) CMM_1166(atpH)
                 CMM_1167(atpA) CMM_1168(atpG) CMM_1169(atpD) CMM_1170(atpC)
            ART: Arth_2611
            AAU: AAur_2594(atpD) AAur_2595(atpG) AAur_2596(atpA)
                 AAur_2598(atpF) AAur_2599(atpE) AAur_2600(atpB)
                 AAur_2601(atpI)
            PAC: PPA1238 PPA1239 PPA1240 PPA1241 PPA1242 PPA1243 PPA1244
                 PPA1245
            TFU: Tfu_2406 Tfu_2407 Tfu_2408 Tfu_2409 Tfu_2410 Tfu_2411
                 Tfu_2412 Tfu_2413
            FRA: Francci3_3706 Francci3_3707 Francci3_3708 Francci3_3709
                 Francci3_3710 Francci3_3711 Francci3_3712 Francci3_3713
            FAL: FRAAL5930(atpC) FRAAL5931(atpD) FRAAL5932(atpG)
                 FRAAL5933(atpA) FRAAL5934(atpH) FRAAL5935(atpF)
                 FRAAL5936(atpE) FRAAL5937(atpB)
            ACE: Acel_0647 Acel_0648 Acel_0649 Acel_0650 Acel_0651 Acel_0652
                 Acel_0653 Acel_0654
            KRA: Krad_1268 Krad_1269 Krad_4246
            SEN: SACE_5295(atpB) SACE_6279(atpC) SACE_6280(atpD)
                 SACE_6281(atpG) SACE_6282(atpA) SACE_6283(atpH)
                 SACE_6284(atpF) SACE_6285(atpE) SACE_6286(atpB)
            STP: Strop_0373 Strop_3631 Strop_3632
            BLO: BL0356(atpC) BL0357(atpD) BL0358(atpG) BL0359(atpA)
                 BL0360(atpH) BL0361 BL0362(atpE) BL0363(atpB)
            BAD: BAD_1426(atpC) BAD_1427(atpD) BAD_1428(atpG) BAD_1429(atpA)
                 BAD_1430(atpH) BAD_1431 BAD_1432(atpE) BAD_1433(atpB)
            RXY: Rxyl_1637 Rxyl_1641 Rxyl_1642 Rxyl_1643 Rxyl_1644
            FNU: FN0364
            RBA: RB10206(atpB) RB10209(atpE) RB10211(atpF) RB10213(atpD)
                 RB10215(atpA) RB10216(atpG) RB10217(atpB) RB10219(atpE)
                 RB12500(fliI) RB4906(atpD) RB4908(atpC) RB4909 RB4911(atpB)
                 RB4913 RB4915(atpF) RB4916(atpA) RB4917(atpG)
            CTR: CT304(atpK) CT305(atpI) CT306(atpD) CT307(atpB) CT308(atpA)
                 CT310(atpE) CT669(yscN) CT717(fliI)
            CTA: CTA_0328(atpD) CTA_0330(atpA) CTA_0332(atpE) CTA_0726(sctN)
                 CTA_0779(fliI)
            CMU: TC0040 TC0090 TC0578 TC0579 TC0580 TC0581 TC0582 TC0584
            CPN: CPn0086(atpE) CPn0088(atpA) CPn0089(atpB) CPn0090(atpD)
                 CPn0091(atpI) CPn0092(atpK) CPn0707(yscN) CPn0858(fliI)
            CPA: CP0039 CP0682 CP0683 CP0684 CP0685 CP0686 CP0688 CP1011
            CPJ: CPj0086(atpE) CPj0088(atpA) CPj0089(atpB) CPj0090(atpD)
                 CPj0091(atpI) CPj0092(atpK) CPj0707(yscN) CPj0858(fliI)
            CPT: CpB0086(HrpE) CpB0088 CpB0089 CpB0090 CpB0091(ntpI) CpB0092
                 CpB0734(yopN) CpB0887
            CCA: CCA00035(sctN) CCA00680(atpK) CCA00681(atpI) CCA00682
                 CCA00683(atpB) CCA00684(atpA) CCA00686 CCA00909
            CAB: CAB036 CAB650(atpK) CAB652(atpD) CAB653(atpB) CAB654(atpA)
                 CAB656 CAB877
            CFE: CF0105(fliI2) CF0325(atpE) CF0327(atpA) CF0328(atpB)
                 CF0329(atpD) CF0330(atpI) CF0331(atpK) CF0970(fliI1)
            PCU: pc1397(sctN) pc1667(atpC) pc1668(atpD) pc1669(atpG)
                 pc1670(atpA) pc1671(atpH) pc1672(atpF) pc1673(atpE)
                 pc1674(atpB)
            BBU: BB0090 BB0091 BB0092(atpD) BB0093(atpB) BB0094(atpA) BB0096
                 BB0288(fliI)
            BGA: BG0091 BG0092 BG0093(atpD) BG0094(atpB) BG0095(atpA) BG0097
                 BG0291(fliI)
            BAF: BAPKO_0091 BAPKO_0092 BAPKO_0093(atpD) BAPKO_0094(atpB)
                 BAPKO_0095(atpA) BAPKO_0097 BAPKO_0298(fliI)
            TPA: TP0402 TP0424 TP0426 TP0427 TP0428 TP0429 TP0430 TP0527
                 TP0528 TP0529 TP0530 TP0531 TP0533
            TDE: TDE1218(fliI) TDE1381(atpE) TDE1679(atpK) TDE1681(atpD)
                 TDE1682(atpB) TDE1683(atpA)
            LIL: LA2592(fliI) LA2775(atpC) LA2776(atpD) LA2778(atpG)
                 LA2779(atpA) LA2780(atpH) LA2781(atpF) LA2782(atpE)
                 LA2783(atpB)
            LIC: LIC11237(atpB) LIC11238(atpE) LIC11239(atpF) LIC11240(atpH)
                 LIC11241(atpA) LIC11242(atpG) LIC11243(atpD) LIC11244(atpC)
                 LIC11391(fliI)
            LBJ: LBJ_1054(fliI) LBJ_1751(atpC) LBJ_1752(atpD) LBJ_1753(atpG)
                 LBJ_1754(atpA) LBJ_1755(atpH) LBJ_1756(atpF) LBJ_1757(atpE)
                 LBJ_1758(atpB)
            LBL: LBL_1115(fliI) LBL_1970(atpC) LBL_1971(atpD) LBL_1972(atpG)
                 LBL_1973(atpA) LBL_1974(atpH) LBL_1975(atpF) LBL_1976(atpE)
                 LBL_1977(atpB)
            SYN: sll1322(atpI) sll1323(atpG) sll1324(atpF) sll1325(atpD)
                 sll1326(atpA) sll1327(atpC) slr1329(atpB) slr1330(atpE)
                 ssl2615(atpH)
            SYW: SYNW0489(atpI) SYNW0490(atpH) SYNW0491(atpG) SYNW0492(atpF)
                 SYNW0493(atpD) SYNW0494(atpA) SYNW0495(atpC) SYNW0511(atpE)
                 SYNW0512(atpB)
            SYC: syc1176_c(atpC) syc1177_c(atpA) syc1178_c(atpD)
                 syc1179_c(atpF) syc1180_c(atpG) syc1181_c(atpH)
                 syc1182_c(atpI) syc1786_c(atpE) syc1787_c(atpB)
            SYF: Synpcc7942_0331 Synpcc7942_0332 Synpcc7942_0333
                 Synpcc7942_0334 Synpcc7942_0335 Synpcc7942_0336
                 Synpcc7942_2315 Synpcc7942_2316
            SYD: Syncc9605_2171 Syncc9605_2172(atpC) Syncc9605_2188
                 Syncc9605_2189 Syncc9605_2190 Syncc9605_2191 Syncc9605_2192
                 Syncc9605_2193
            SYE: Syncc9902_0483 Syncc9902_0484 Syncc9902_0485 Syncc9902_0486
                 Syncc9902_0488 Syncc9902_0503(atpC) Syncc9902_0504
            SYG: sync_2284(atpD) sync_2285(atpC) sync_2312(atpG)
                 sync_2313(atpA) sync_2314(atpH) sync_2315 sync_2316
                 sync_2317(atpE) sync_2318(atpB) sync_2319
            SYR: SynRCC307_1861(atpB) SynRCC307_1862(atpE)
                 SynRCC307_1877(atpC) SynRCC307_1878(atpA) SynRCC307_1879(atpD)
                 SynRCC307_1880(atpF) SynRCC307_1881(atpG) SynRCC307_1882(atpH)
                 SynRCC307_1883(atpI)
            SYX: SynWH7803_2000(atpB) SynWH7803_2001(atpE)
                 SynWH7803_2016(atpC) SynWH7803_2017(atpA) SynWH7803_2018(atpD)
                 SynWH7803_2019(atpF) SynWH7803_2020(atpG) SynWH7803_2021(atpH)
                 SynWH7803_2022(atpI)
            CYA: CYA_0420(atpD) CYA_1542(atpC) CYA_2112(atpG) CYA_2113(atpA)
                 CYA_2114(atpH) CYA_2115(atpF) CYA_2116 CYA_2117(atpE)
                 CYA_2119(atpB)
            CYB: CYB_2222(atpC) CYB_2502(atpD) CYB_2672(atpG) CYB_2673(atpA)
                 CYB_2674(atpH) CYB_2675(atpF) CYB_2676 CYB_2677(atpE)
                 CYB_2679(atpB)
            TEL: tll0385(atpC) tlr0430(atpI) tlr0431(atpH) tlr0432(atpG)
                 tlr0433(atpF) tlr0434(atpD) tlr0435(atpA) tlr0525(atpB)
                 tlr0526(atpE)
            GVI: gll2568(atpE) gll2570(atpB) gll2905(atpA) gll2906(atpD)
                 gll2907(atpF) gll2908(atpG) gll2910(atpI) glr4315(atpC)
                 gsl2909(atpH)
            ANA: all0004(atpC) all0005(atpA) all0006(atpD) all0007(atpF)
                 all0008(atpG) all0010(atpI) all5038(atpE) all5039(atpB)
                 asl0009(atpH)
            AVA: Ava_2297 Ava_2298 Ava_2610 Ava_2611 Ava_2612 Ava_2613
                 Ava_2614 Ava_2615 Ava_2616
            PMA: Pro1591(atpD) Pro1592(atpC) Pro1603(atpG) Pro1604(atpA)
                 Pro1605(atpH) Pro1606(atpF) Pro1607(atpF) Pro1608(atpE)
                 Pro1609(atpB)
            PMM: PMM1438(atpB) PMM1439(atpC) PMM1450(atpC) PMM1451(atpA)
                 PMM1452(atpH) PMM1453(atpF) PMM1454(atpG) PMM1455
                 PMM1456(atpI)
            PMT: PMT1451(atpB) PMT1452(atpE) PMT1466(atpC) PMT1467(atpA)
                 PMT1468(atpH) PMT1469(atpF) PMT1470(atpG) PMT1471
                 PMT1472(atpI)
            PMN: PMN2A_0970 PMN2A_0971 PMN2A_0980 PMN2A_0981 PMN2A_0982
                 PMN2A_0983 PMN2A_0984 PMN2A_0985 PMN2A_0986
            PMI: PMT9312_1532 PMT9312_1543 PMT9312_1545 PMT9312_1546
                 PMT9312_1547 PMT9312_1548 PMT9312_1549
            PMB: A9601_16401(atpD) A9601_16411(atpC) A9601_16521
                 A9601_16531(atpA) A9601_16541(atpH) A9601_16551 A9601_16561
                 A9601_16571(atpE) A9601_16581(atpB)
            PMC: P9515_16171(atpD) P9515_16181(atpC) P9515_16291
                 P9515_16301(atpA) P9515_16311(atpH) P9515_16321 P9515_16331
                 P9515_16341(atpE) P9515_16351(atpB)
            PMF: P9303_03891 P9303_04781(atpB) P9303_04791 P9303_04801
                 P9303_04811 P9303_04821(atpH) P9303_04831(atpA) P9303_04841
                 P9303_05011(atpC) P9303_05021(atpD)
            PMG: P9301_16281(atpD) P9301_16291(atpC) P9301_16401
                 P9301_16411(atpA) P9301_16421(atpH) P9301_16431 P9301_16441
                 P9301_16451(atpE) P9301_16461(atpB)
            PMH: P9215_17061 P9215_17071 P9215_17181 P9215_17191 P9215_17201
                 P9215_17221 P9215_17241
            PME: NATL1_18381(atpD) NATL1_18391(atpC) NATL1_18481
                 NATL1_18491(atpA) NATL1_18501(atpH) NATL1_18511 NATL1_18521
                 NATL1_18531(atpE) NATL1_18541(atpB)
            TER: Tery_2204 Tery_3386
            BTH: BT_0711 BT_0712 BT_0714 BT_0715 BT_0716 BT_0717 BT_0718
                 BT_0719 BT_1301
            BFR: BF2171 BF2172 BF2174 BF2175 BF2176 BF2177 BF2178 BF2179
                 BF2734
            BFS: BF2227(atpD) BF2228(atpC) BF2230 BF2231(atpE) BF2232 BF2233
                 BF2234(atpA) BF2235(atpG) BF2749
            PGI: PG1801 PG1803(atpA) PG1804(atpB) PG1805(atpD)
            SRU: SRU_0911 SRU_0912(atpE) SRU_0913(atpF) SRU_0914(atpH)
                 SRU_0915(atpA) SRU_0916(atpG) SRU_2429(atpD) SRU_2430(atpC)
                 SRU_2614(fliI)
            CHU: CHU_0179(atpB) CHU_0180(atpE) CHU_0181(atpF) CHU_0182(atpH)
                 CHU_0183(atpA) CHU_0184(atpG) CHU_0336(atpD) CHU_0337(atpC)
            GFO: GFO_2532(ntpJ) GFO_3265(atpG) GFO_3266(atpA) GFO_3267(atpD)
                 GFO_3268(atpF) GFO_3269(atpE) GFO_3270(atpB) GFO_3548(atpD)
                 GFO_3549(atpC)
            FJO: Fjoh_0819 Fjoh_1059 Fjoh_1060
            FPS: FP0114(atpD) FP0115(atpC) FP2457(atpG) FP2458(atpA)
                 FP2459(atpH) FP2460(atpF) FP2461(atpE) FP2462(atpB)
            CTE: CT0018(atpH) CT0019(atpF) CT0020(atpE) CT0021(atpB-2)
                 CT1029(atpB-1) CT1032(atpC-1) CT1033(atpD-1) CT2032(atpG)
                 CT2033(atpA) CT2234(atpD-2) CT2235(atpC-2)
            CCH: Cag_0064 Cag_0065 Cag_0066 Cag_0067 Cag_0140 Cag_0141
                 Cag_2014 Cag_2015
            PLT: Plut_0020 Plut_0021 Plut_1068 Plut_1984 Plut_1985 Plut_2095
                 Plut_2096 Plut_2097 Plut_2098
            DET: DET0558(atpB) DET0559(atpE) DET0560(atpF) DET0561(atpH)
                 DET0562(atpA) DET0563(atpG) DET0564(atpD) DET0565(atpC)
            DEH: cbdb_A532(atpB) cbdb_A533(atpE) cbdb_A534(atpF)
                 cbdb_A535(atpH) cbdb_A536(atpA) cbdb_A537(atpG)
                 cbdb_A538(atpD) cbdb_A539(atpC)
            DEB: DehaBAV1_0536 DehaBAV1_0537
            RRS: RoseRS_0513 RoseRS_0514 RoseRS_2088
            RCA: Rcas_1266 Rcas_1267 Rcas_1780
            DRA: DR_0695 DR_0696 DR_0697 DR_0698 DR_0699 DR_0700 DR_0701
                 DR_0702
            DGE: Dgeo_2045 Dgeo_2048 Dgeo_2049 Dgeo_2050 Dgeo_2051 Dgeo_2052
            TTJ: TTHA1271 TTHA1272 TTHA1273 TTHA1274 TTHA1275 TTHA1276
                 TTHA1277 TTHA1278
            AAE: aq_1586(atpF1) aq_1587(atpF2) aq_1588(atpH) aq_1595(fliI)
                 aq_177(atpE) aq_179(atpB) aq_203(atpG2) aq_2038(atpD)
                 aq_2041(atpG1) aq_673(atpC) aq_679(atpA)
            TMA: TM0218 TM1609 TM1610 TM1611 TM1612 TM1613 TM1614 TM1615
                 TM1616
            TPT: Tpet_1179 Tpet_1180
            TME: Tmel_0292
            FNO: Fnod_0327
            MJA: MJ0216(atpB) MJ0217(atpA) MJ0218(atpF) MJ0219(atpC)
                 MJ0220(atpE) MJ0221 MJ0222 MJ0223 MJ0615(atpD)
            MMP: MMP1038(atpH) MMP1039(atpI) MMP1040(atpK) MMP1041(atpE)
                 MMP1042(atpC) MMP1043(atpF) MMP1044(atpA) MMP1045(atpB)
                 MMP1046(atpD)
            MMZ: MmarC7_0293 MmarC7_0296
            MAE: Maeo_0060 Maeo_0063
            MVN: Mevan_0362 Mevan_0365
            MAC: MA2433 MA2434 MA2435 MA2436 MA2437 MA2440 MA2441 MA4152(atpH)
                 MA4153(atpI) MA4154(atpC) MA4155(atpE) MA4156(atpC)
                 MA4157(atpF) MA4158(atpA) MA4159(atpB) MA4160(atpD)
            MBA: Mbar_A0378 Mbar_A0384 Mbar_A0385 Mbar_A0386 Mbar_A0387
                 Mbar_A0388 Mbar_A0389 Mbar_A0390 Mbar_A0391 Mbar_A0392
                 Mbar_A3098 Mbar_A3099 Mbar_A3101 Mbar_A3102 Mbar_A3105
                 Mbar_A3106
            MMA: MM_0778 MM_0779 MM_0780 MM_0781 MM_0782 MM_0783 MM_0784
                 MM_0785 MM_0786
            MBU: Mbur_1237 Mbur_1238 Mbur_1239 Mbur_1240 Mbur_1241 Mbur_1242
                 Mbur_1245
            MHU: Mhun_1177 Mhun_1178 Mhun_1179 Mhun_1180 Mhun_1181 Mhun_1182
                 Mhun_1183 Mhun_1184 Mhun_1185 Mhun_1757 Mhun_1760 Mhun_1761
                 Mhun_1762 Mhun_1763 Mhun_1764 Mhun_1765 Mhun_1769 Mhun_1770
                 Mhun_1771 Mhun_1773 Mhun_2766
            MTH: MTH953 MTH954 MTH955 MTH956 MTH957 MTH958 MTH959 MTH960
                 MTH961
            MSI: Msm_0433 Msm_0434 Msm_0435 Msm_0437 Msm_0438 Msm_0439
                 Msm_0440
            MKA: MK1012(ntpI) MK1013(ntpK) MK1014(ntpE) MK1015(ntpC)
                 MK1016(ntpF) MK1017(ntpA) MK1673(ntpB) MK1674(ntpD)
            AFU: AF1158 AF1159(atpI) AF1160(atpK-1) AF1162(atpK-2)
                 AF1163(atpE) AF1164(atpC) AF1165(atpF) AF1166(atpA)
                 AF1167(atpB) AF1168(atpD)
            HAL: VNG2135G(atpD) VNG2138G(atpB) VNG2139G(atpA) VNG2140G(atpF)
                 VNG2141G(atpC) VNG2142G(atpE) VNG2143G(atpK) VNG2144G(atpI)
                 VNG2146H
            HMA: rrnAC1435(atpC2) rrnAC3152(atpG) rrnAC3154(atpI)
                 rrnAC3155(atpC1) rrnAC3156(atpE) rrnAC3157(ntpC)
                 rrnAC3158(atpF) rrnAC3159(ntpA) rrnAC3160(ntpB)
                 rrnAC3162(atpD)
            HWA: HQ3242A(atpD) HQ3243A(atpB) HQ3244A(atpA) HQ3245A(atpF)
                 HQ3246A(atpC) HQ3247A(atpE) HQ3248A(atpK) HQ3249A(atpI)
                 HQ3250A(atpH)
            NPH: NP0264A(atpD) NP1018A(atpH) NP1020A(atpI) NP1022A(atpK)
                 NP1024A(atpE) NP1026A(atpC) NP1028A(atpF) NP1030A(atpA)
                 NP1032A(atpB)
            TAC: Ta0001 Ta0001z(ntpK) Ta0002 Ta0003 Ta0004 Ta0005 Ta0006
                 Ta0008
            TVO: TVN0048 TVN0049 TVN0050 TVN0051 TVN0052 TVN0053 TVN0054
                 TVN0056
            PTO: PTO0486 PTO0488 PTO0489 PTO0490 PTO0491 PTO0492 PTO0493
                 PTO0494
            PHO: PH1972 PH1974 PH1975 PH1976 PH1977 PH1978 PH1980 PH1981
                 PH1983
            PAB: PAB1179 PAB1180(atpI) PAB1181 PAB1182(atpE) PAB1183(atpC)
                 PAB1184(atpF) PAB1186(atpB) PAB2378(atpA) PAB2379(atpD)
            PFU: PF0176 PF0177 PF0178 PF0179 PF0180 PF0181 PF0182 PF0183
                 PF0184
            TKO: TK1596 TK1597 TK1598 TK1599 TK1600 TK1601 TK1602 TK1603
                 TK1604
            RCI: RCIX2025(atpI) RCIX2026(atpK) RCIX2027(atpE) RCIX2028(atpC)
                 RCIX2029(atpF) RCIX2030(atpA) RCIX2032(atpB) RCIX2034(atpD)
            APE: APE_0402.1 APE_0404.1 APE_0405.1 APE_0410.1 APE_0673.1
                 APE_2326.1
            IHO: Igni_0609
            HBU: Hbut_0782 Hbut_0783 Hbut_0784 Hbut_0787
            SSO: SSO0559(atpI) SSO0560(atpF) SSO0561(atpE) SSO0563(atpA)
                 SSO0564(atpB) SSO0566(atpD) SSO0567(atpK)
            STO: ST1433 ST1434 ST1435 ST1436 ST1437 ST1438 ST1439
            SAI: Saci_1545 Saci_1546 Saci_1547 Saci_1548(atpA) Saci_1549(atpB)
                 Saci_1550(atpD) Saci_1552
            MSE: Msed_1919
            PAI: PAE0661(atpF) PAE0662 PAE0663(atpA) PAE0754(atpC)
                 PAE0758(atpD) PAE1146(atpB) PAE1773
            NEQ: NEQ103 NEQ166 NEQ217 NEQ263 NEQ410
STRUCTURES  PDB: 1GPP  1PYV  1R5Z  1U7L  1UM2  1V9M  1VDZ  1VZS  1W0J  1W0K  
                 1WU0  2A7U  2BL2  2BO5  2C61  2CK3  2CLY  2CYD  2D00  2DB4  
                 2DM9  2DMA  2DPY  2E5T  2E5U  2E5Y  2F43  2HLD  2I4R  2JDI  
                 2JMX  2NVJ  2QAI  2R9V  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.14
            ExPASy - ENZYME nomenclature database: 3.6.3.14
            ExplorEnz - The Enzyme Database: 3.6.3.14
            ERGO genome analysis and discovery system: 3.6.3.14
            BRENDA, the Enzyme Database: 3.6.3.14
///
ENTRY       EC 3.6.3.15                 Enzyme
NAME        Na+-transporting two-sector ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (Na+-transporting)
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     A multisubunit non-phosphorylated ATPase that is involved in the
            transport of ions. An enzyme found in alkaliphilic bacteria that is
            similar to EC 3.6.3.14 (H+-transporting two-sector ATPase) where Na+
            replaces H+.
REFERENCE   1  [PMID:8144530]
  AUTHORS   Solioz M, Davies K.
  TITLE     Operon of vacuolar-type Na(+)-ATPase of Enterococcus hirae.
  JOURNAL   J. Biol. Chem. 269 (1994) 9453-9.
  ORGANISM  Enterococcus hirae
REFERENCE   2  [PMID:8157629]
  AUTHORS   Takase K, Kakinuma S, Yamato I, Konishi K, Igarashi K, Kakinuma Y.
  TITLE     Sequencing and characterization of the ntp gene cluster for
            vacuolar-type Na(+)-translocating ATPase of Enterococcus hirae.
  JOURNAL   J. Biol. Chem. 269 (1994) 11037-44.
  ORGANISM  Enterococcus hirae
REFERENCE   3  [PMID:9119076]
  AUTHORS   Rahlfs S, Muller V.
  TITLE     Sequence of subunit c of the Na(+)-translocating F1F0 ATPase of
            Acetobacterium woodii: proposal for determinants of Na+ specificity
            as revealed by sequence comparisons.
  JOURNAL   FEBS. Lett. 404 (1997) 269-71.
  ORGANISM  Acetobacterium woodii
ORTHOLOGY   KO: K01550  Na+-transporting two-sector ATPase
GENES       YPA: YPA_1203 YPA_3072 YPA_4016 YPA_4166 YPA_4167 YPA_4168
                 YPA_CD0022
            YPN: YPN_0575 YPN_2296 YPN_3401 YPN_3978 YPN_3979 YPN_3980
            YPP: YPDSF_0501 YPDSF_1297 YPDSF_3704 YPDSF_3912 YPDSF_3913
                 YPDSF_3914 YPDSF_3977
            ENT: Ent638_2532 Ent638_4130 Ent638_4131 Ent638_4132
            PPF: Pput_1501
            PMY: Pmen_2822
            PCR: Pcryo_2327 Pcryo_2328
            SDN: Sden_0056 Sden_1327 Sden_3753
            SFR: Sfri_1185
            SAZ: Sama_2294 Sama_3644 Sama_3645 Sama_3646
            SBL: Sbal_1970 Sbal_2923 Sbal_3976 Sbal_4366 Sbal_4367 Sbal_4368
            SLO: Shew_1369 Shew_3845 Shew_3846 Shew_3847
            SPC: Sputcn32_2573 Sputcn32_3473 Sputcn32_3956 Sputcn32_3957
                 Sputcn32_3958
            SHW: Sputw3181_0466 Sputw3181_1430 Sputw3181_4053 Sputw3181_4054
                 Sputw3181_4055
            PHA: PSHAa0112(rho)
            PAT: Patl_2668 Patl_2675 Patl_3044 Patl_4295 Patl_4296 Patl_4297
            SDE: Sde_3966 Sde_3967
            PIN: Ping_0463 Ping_0470 Ping_3562 Ping_3730 Ping_3731 Ping_3732
            MAQ: Maqu_1994 Maqu_3875 Maqu_3876 Maqu_3877
            NOC: Noc_2356
            HHA: Hhal_0495 Hhal_2430 Hhal_2431 Hhal_2432
            CSA: Csal_1958 Csal_3284
            RMA: Rmag_1045 Rmag_1046 Rmag_1047
            REU: Reut_B5100
            BVI: Bcep1808_0113 Bcep1808_0114 Bcep1808_0115 Bcep1808_3152
                 Bcep1808_5335 Bcep1808_5360
            BUR: Bcep18194_A5130 Bcep18194_A6416
            BCN: Bcen_2949 Bcen_3493 Bcen_3519
            BCH: Bcen2424_4847 Bcen2424_4873
            BAM: Bamb_4222
            PNU: Pnuc_0024 Pnuc_0025 Pnuc_0026
            RFR: Rfer_0108 Rfer_0553 Rfer_1161 Rfer_1168
            POL: Bpro_0325 Bpro_0326 Bpro_0327
            PNA: Pnap_0253 Pnap_0254 Pnap_0255 Pnap_2329 Pnap_2336
            AAV: Aave_0370 Aave_0371 Aave_0372 Aave_0463 Aave_4392
            AJS: Ajs_0306 Ajs_0307 Ajs_0308 Ajs_3804
            VEI: Veis_0478 Veis_0479 Veis_0480 Veis_1116
            HAR: HEAR1879(fliI) HEAR3407(atpA)
            NMU: Nmul_A1654 Nmul_A1661
            MFA: Mfla_1975
            PPD: Ppro_0604 Ppro_0605 Ppro_0606 Ppro_0845 Ppro_0851 Ppro_1505
                 Ppro_1506 Ppro_1507 Ppro_3429
            DVL: Dvul_2193 Dvul_2194 Dvul_2195 Dvul_2671 Dvul_2988
            DDE: Dde_0350
            ADE: Adeh_1202 Adeh_1203 Adeh_1391 Adeh_1596 Adeh_4348 Adeh_4349
                 Adeh_4350
            OTS: OTBS_1012(rho)
            RPB: RPB_3911
            RPC: RPC_4232
            RPD: RPD_0557 RPD_0558 RPD_0559 RPD_3671
            NWI: Nwi_0100 Nwi_0526
            NHA: Nham_0532 Nham_3370
            SIT: TM1040_2086 TM1040_2087 TM1040_2088
            RSH: Rsph17029_0001 Rsph17029_0972 Rsph17029_0973 Rsph17029_0974
                 Rsph17029_1691 Rsph17029_4097 Rsph17029_4103
            JAN: Jann_1047 Jann_1048 Jann_1049
            PDE: Pden_2109 Pden_3816 Pden_3817 Pden_3818
            NAR: Saro_2400 Saro_2401 Saro_2402
            SAL: Sala_2286 Sala_2287 Sala_2288
            RRU: Rru_A1224 Rru_A1225 Rru_A1226 Rru_A3619
            MAG: amb0628
            ABA: Acid345_1649 Acid345_4333 Acid345_4334
            SUS: Acid_0343 Acid_0463 Acid_0464 Acid_0465
            SPY: SPy_0148(ntpI) SPy_0149(ntpK) SPy_0150(ntpE) SPy_0151(ntpC)
                 SPy_0154(ntpA) SPy_0155(ntpB) SPy_0157(ntpD)
            SPZ: M5005_Spy_0126(ntpI) M5005_Spy_0127(ntpK)
                 M5005_Spy_0128(ntpE) M5005_Spy_0129(ntpC) M5005_Spy_0130(ntpF)
                 M5005_Spy_0131(ntpA) M5005_Spy_0132(ntpB) M5005_Spy_0133(ntpD)
            SPM: spyM18_0144 spyM18_0145 spyM18_0146 spyM18_0147 spyM18_0148
                 spyM18_0150 spyM18_0151 spyM18_0153
            SPG: SpyM3_0115(ntpI) SpyM3_0116(ntpK) SpyM3_0117(ntpE)
                 SpyM3_0118(ntpC) SpyM3_0119(ntpG) SpyM3_0120(ntpA)
                 SpyM3_0121(ntpB) SpyM3_0122(ntpD)
            SPS: SPs0117 SPs0118 SPs0119 SPs0120 SPs0121 SPs0122 SPs0123
                 SPs0124
            SPH: MGAS10270_Spy0128(ntpI) MGAS10270_Spy0129(ntpK)
                 MGAS10270_Spy0130(ntpE) MGAS10270_Spy0131(ntpC)
                 MGAS10270_Spy0132(ntpF) MGAS10270_Spy0133(ntpA)
                 MGAS10270_Spy0134(ntpB) MGAS10270_Spy0135(ntpD)
            SPI: MGAS10750_Spy0131(ntpI) MGAS10750_Spy0132(ntpK)
                 MGAS10750_Spy0133(ntpE) MGAS10750_Spy0134(ntpC)
                 MGAS10750_Spy0135(ntpF) MGAS10750_Spy0136(ntpA)
                 MGAS10750_Spy0137(ntpB) MGAS10750_Spy0138(ntpD)
            SPJ: MGAS2096_Spy0131(ntpI) MGAS2096_Spy0132(ntpK)
                 MGAS2096_Spy0133(ntpE) MGAS2096_Spy0134(ntpC)
                 MGAS2096_Spy0135(ntpF) MGAS2096_Spy0136(ntpA)
                 MGAS2096_Spy0137(ntpB) MGAS2096_Spy0138(ntpD)
            SPK: MGAS9429_Spy0128(ntpI) MGAS9429_Spy0129(ntpK)
                 MGAS9429_Spy0130(ntpE) MGAS9429_Spy0131(ntpC)
                 MGAS9429_Spy0132(ntpF) MGAS9429_Spy0133(ntpA)
                 MGAS9429_Spy0134(ntpB) MGAS9429_Spy0135(ntpD)
            SPF: SpyM50121(ntpI) SpyM50122(ntpK) SpyM50123(ntpE)
                 SpyM50124(ntpC) SpyM50125 SpyM50126(ntpA) SpyM50127(ntpB)
                 SpyM50128(ntpD)
            SPA: M6_Spy0173 M6_Spy0174 M6_Spy0175 M6_Spy0176 M6_Spy0177
                 M6_Spy0178 M6_Spy0179 M6_Spy0180
            SPB: M28_Spy0124(ntpI) M28_Spy0125(ntpK) M28_Spy0126(ntpE)
                 M28_Spy0127(ntpC) M28_Spy0128(ntpF) M28_Spy0129(ntpA)
                 M28_Spy0130(ntpB) M28_Spy0131(ntpD)
            SPN: SP_1315 SP_1316 SP_1317 SP_1318 SP_1319 SP_1320 SP_1321
                 SP_1322
            SSA: SSA_0085(ntpI) SSA_0086(ntpK) SSA_0087(ntpE) SSA_0088(ntpC)
                 SSA_0089(ntpG) SSA_0091(ntpA) SSA_0092(ntpB) SSA_0093(ntpD)
            SGO: SGO_0129(atpI) SGO_0136
            CPE: CPE1636(ntpD) CPE1637(ntpB) CPE1638(ntpA) CPE1639(ntpF)
                 CPE1640(ntpC) CPE1641(ntpE) CPE1642(ntpK) CPE1643(ntpI)
                 CPE1644
            CTC: CTC00993 CTC00994 CTC00995 CTC00996 CTC00997 CTC00998
                 CTC00999 CTC01000 CTC01001 CTC02326 CTC02327 CTC02328 CTC02329
                 CTC02330 CTC02331 CTC02332
            CTH: Cthe_0468 Cthe_2267 Cthe_2268 Cthe_2269 Cthe_2606 Cthe_2607
                 Cthe_2608
            CDF: CD2954(ntpD) CD2955(ntpB) CD2956(ntpA) CD2960(ntpI)
                 CD3473(atpE)
            CBO: CBO2623(ntpD) CBO2624(ntpB) CBO2625(ntpA) CBO2629(ntpI)
            CKL: CKL_3687(atpC) CKL_3688(atpD) CKL_3689(atpG) CKL_3690(atpA)
                 CKL_3691(atpH) CKL_3692(atpF) CKL_3693(atpE) CKL_3694(atpB)
                 CKL_3695(atpI)
            DRM: Dred_2405 Dred_3150 Dred_3151 Dred_3152
            MTA: Moth_0774 Moth_2378 Moth_2379 Moth_2380
            MVA: Mvan_4328 Mvan_4329 Mvan_4330
            MGI: Mflv_2316 Mflv_2317 Mflv_2318
            MKM: Mkms_3950 Mkms_3951 Mkms_3952
            MJL: Mjls_3862 Mjls_3863 Mjls_3864
            ART: Arth_2605 Arth_2606 Arth_2607
            NCA: Noca_0756 Noca_1761 Noca_1762 Noca_1763
            ACE: Acel_0844
            KRA: Krad_1653
            RXY: Rxyl_1638 Rxyl_1639 Rxyl_1640
            FNU: FN0357 FN0358 FN0359 FN0360 FN0361 FN0362 FN0363 FN1733
                 FN1734 FN1735 FN1736 FN1737 FN1738 FN1739 FN1740 FN1741 FN1742
            CTA: CTA_0326(atpK) CTA_0327(atpI) CTA_0329(atpB)
            CAB: CAB651(atpI)
            PCU: pc1676(ntpK) pc1677(ntpI) pc1678(ntpD) pc1679(atpB)
                 pc1680(ntpA) pc1682(ntpE)
            SYF: Synpcc7942_0337
            SYD: Syncc9605_2187
            SYE: Syncc9902_0489
            PMI: PMT9312_1531 PMT9312_1544
            TER: Tery_2198 Tery_2199 Tery_3385
            BTH: BT_1295 BT_1296 BT_1297 BT_1298 BT_1299
            BFR: BF2728 BF2729 BF2730 BF2731 BF2732
            BFS: BF2743 BF2744 BF2745 BF2746 BF2747
            PGI: PG1806(atpI) PG1807(atpK)
            CCH: Cag_0459(rho)
            CPH: Cpha266_0049 Cpha266_2543 Cpha266_2544
            PVI: Cvib_0025 Cvib_1627 Cvib_1628
            PLT: Plut_1063 Plut_1070
            DGE: Dgeo_2046 Dgeo_2047
            TTH: TTC0905 TTC0906 TTC0907 TTC0908 TTC0909 TTC0910 TTC0911
                 TTC0912
            TPT: Tpet_0706
            TME: Tmel_1269
            FNO: Fnod_0758
            MMQ: MmarC5_0548 MmarC5_0549
            MBU: Mbur_1243 Mbur_1244
            MTP: Mthe_1608 Mthe_1609
            MHU: Mhun_1758 Mhun_1759
            MLA: Mlab_1087
            MEM: Memar_0287 Memar_0288
            MBN: Mboo_2344 Mboo_2345
            MST: Msp_1133(ahaD) Msp_1134(ahaB) Msp_1135(ahaA) Msp_1136(ahaF)
                 Msp_1137(ahaC) Msp_1138(ahaE) Msp_1139(ahaK) Msp_1140(ahaI)
                 Msp_1141(ahaH)
            PTO: PTO0487
            SMR: Smar_1170 Smar_1171
            IHO: Igni_0679
            PIS: Pisl_0705 Pisl_1264
            PCL: Pcal_0698 Pcal_2089
            PAS: Pars_0237 Pars_2319
            TPE: Tpen_0341 Tpen_0342
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.15
            ExPASy - ENZYME nomenclature database: 3.6.3.15
            ExplorEnz - The Enzyme Database: 3.6.3.15
            ERGO genome analysis and discovery system: 3.6.3.15
            BRENDA, the Enzyme Database: 3.6.3.15
///
ENTRY       EC 3.6.3.16                 Enzyme
NAME        arsenite-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (arsenite-exporting)
REACTION    ATP + H2O + arsenitein = ADP + phosphate + arseniteout [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            arsenite [CPD:C06697]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            arsenite [CPD:C06697]
COMMENT     A multisubunit non-phosphorylated ATPase that is involved in the
            transport of ions. A bacterial enzyme that usually contains two
            subunits where one (with 12 membrane-spanning segments) forms the
            'channel' part and the other (occurring in pairs peripherally to the
            membrane) contains the ATP-binding site. Exports arsenite and
            antimonite anions.
REFERENCE   1  [PMID:2484581]
  AUTHORS   Silver S, Misra TK, Laddaga RA.
  TITLE     DNA sequence analysis of bacterial toxic heavy metal resistances.
  JOURNAL   Biol. Trace. Elem. Res. 21 (1989) 145-63.
REFERENCE   2  [PMID:1703401]
  AUTHORS   Rosen BP, Weigel U, Monticello RA, Edwards BP.
  TITLE     Molecular analysis of an anion pump: purification of the ArsC
            protein.
  JOURNAL   Arch. Biochem. Biophys. 284 (1991) 381-5.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:1703401]
  AUTHORS   Rosen BP, Weigel U, Monticello RA, Edwards BP.
  TITLE     Molecular analysis of an anion pump: purification of the ArsC
            protein.
  JOURNAL   Arch. Biochem. Biophys. 284 (1991) 381-5.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:10089335]
  AUTHORS   Zhou T, Rosen BP, Gatti DL.
  TITLE     Crystallization and preliminary x-ray analysis of the catalytic
            subunit of the ATP-dependent arsenite pump encoded by the
            Escherichia coli plasmid R773.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 55 ( Pt 4) (1999) 921-4.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01551  arsenite-transporting ATPase
GENES       MMU: 56495(Asna1)
            CFA: 476699(ASNA1)
            XLA: 444297(MGC80960)
            SPU: 592269(LOC592269)
            DME: Dmel_CG1598
            CEL: ZK637.5(ArsA)
            OSA: 4330495 4347615
            SCE: YDL100C(GET3)
            PIC: PICST_48071(ARR4)
            CAL: CaO19_2965(CaO19.2965)
            CGR: CAGL0L07304g
            SPO: SPAC1142.06
            ANI: AN2909.2
            AFM: AFUA_3G11350
            AOR: AO090003000688
            CNE: CNK02640
            UMA: UM03838.1
            DDI: DDB_0215362(arsA)
            PFA: PFD0725c
            CHO: Chro.70452
            TAN: TA05345
            TPV: TP03_0142
            TET: TTHERM_00471960
            TCR: 507763.30 510101.490
            LMA: LmjF11.0700
            EHI: 323.t00007
            ECI: UTI89_C1360(minD)
            YEN: YE3473(arsA2)
            PAR: Psyc_1121(arsA)
            PCR: Pcryo_1297
            PRW: PsycPRwf_1206
            SPC: Sputcn32_3828
            SHN: Shewana3_2343
            SHW: Sputw3181_2948
            ILO: IL0699(arsA)
            AEH: Mlg_0312 Mlg_2710
            HHA: Hhal_2193
            CSA: Csal_2005
            ABO: ABO_1301(arsA)
            AHA: AHA_1725
            BVI: Bcep1808_4680
            RFR: Rfer_3664
            PNA: Pnap_3731
            AJS: Ajs_2513
            EBA: ebA5000(arsA)
            AZO: azo2356(arsA)
            DAR: Daro_2637
            MFA: Mfla_1491
            WSU: WS1546
            GUR: Gura_1381 Gura_2829
            MXA: MXAN_4041 MXAN_4294
            RLE: RL4514(arsA)
            RRU: Rru_A1447
            MAG: amb1833
            ABA: Acid345_2410
            SUS: Acid_5915
            BHA: BH1795
            BAA: BA_0887 BA_0888
            BAT: BAS0302 BAS0303
            BCA: BCE_0346(arsA)
            BCZ: BCZK0288(arsA)
            BTK: BT9727_0285(arsA)
            BTL: BALH_0309(arsA)
            SER: SERP2428(arsA)
            SHA: SH0111
            LLM: llmg_1248(arsA)
            LBR: LVIS_B11
            STH: STH681
            CBO: CBO0755(arsA)
            CBA: CLB_0797(arsA)
            CBH: CLC_0812(arsA)
            CBF: CLI_0835(arsA)
            CBE: Cbei_2110
            AMT: Amet_0986 Amet_0987 Amet_1480 Amet_1830 Amet_1831
            DSY: DSY4152 DSY4598
            SWO: Swol_0938
            MSM: MSMEG_4250
            MVA: Mvan_3546 Mvan_5095
            MGI: Mflv_1654
            MMC: Mmcs_3279
            MKM: Mkms_3341
            MJL: Mjls_3290
            RHA: RHA1_ro01118 RHA1_ro04317
            SCO: SCO2128(SC6E10.22c)
            SMA: SAV6072
            ART: Arth_0209
            NCA: Noca_3111
            TFU: Tfu_1391
            FRA: Francci3_3094
            FAL: FRAAL5095
            SEN: SACE_1698(arsA)
            RXY: Rxyl_1314
            FNU: FN1537 FN1538
            RBA: RB9551(arsA)
            SYN: sll0086 slr1794
            SYC: syc0292_c syc2008_d
            SYF: Synpcc7942_1259 Synpcc7942_2085
            CYA: CYA_2281 CYA_2683
            CYB: CYB_0446 CYB_1135
            TEL: tll1842 tlr2251
            GVI: glr1227 glr1390
            ANA: all2244 all2700 all4481
            AVA: Ava_0069 Ava_3342 Ava_4268
            TER: Tery_0013 Tery_0875 Tery_2327
            SRU: SRU_2421
            CTE: CT0116 CT0348 CT0980 CT1939 CT1945 CT2070
            CCH: Cag_0117 Cag_0217 Cag_0221 Cag_1378 Cag_1412
            CPH: Cpha266_0213 Cpha266_0678 Cpha266_1088 Cpha266_1248
                 Cpha266_2297 Cpha266_2301
            PVI: Cvib_0328 Cvib_0332 Cvib_0505 Cvib_0783
            PLT: Plut_0070 Plut_0263 Plut_0267 Plut_0457 Plut_0696 Plut_1173
            RRS: RoseRS_0928
            RCA: Rcas_1570
            AAE: aq_343(arsA2) aq_682(arsA1)
            MJA: MJ1142(arsA)
            MMP: MMP0163(arsA)
            MMQ: MmarC5_1512
            MMZ: MmarC7_1163
            MAE: Maeo_1004
            MVN: Mevan_1168
            MTH: MTH1511
            MST: Msp_0169
            MSI: Msm_1170
            MKA: MK1680(arsA)
            HAL: VNG0365G(arsA1) VNG7123(arsA)
            HMA: rrnAC0083(arsA1) rrnAC2592(arsA3)
            HWA: HQ1035A(arsA) HQ1236A(arsA) HQ2430A(arsA)
            NPH: NP1164A(tpa07) NP1818A(tpa08)
            TAC: Ta0437
            TVO: TVN1056
            PTO: PTO1198
            TKO: TK0994
            APE: APE_2164.1 APE_2165
            SMR: Smar_0147
            IHO: Igni_1326
            PCL: Pcal_0862 Pcal_0863
            PAS: Pars_0891 Pars_0892
STRUCTURES  PDB: 1IHU  1II0  1II9  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.16
            ExPASy - ENZYME nomenclature database: 3.6.3.16
            ExplorEnz - The Enzyme Database: 3.6.3.16
            ERGO genome analysis and discovery system: 3.6.3.16
            BRENDA, the Enzyme Database: 3.6.3.16
///
ENTRY       EC 3.6.3.17                 Enzyme
NAME        monosaccharide-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (monosaccharide-importing)
REACTION    ATP + H2O + monosaccharideout = ADP + phosphate + monosaccharidein
            [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            monosaccharide [CPD:C06698]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            monosaccharide [CPD:C06698]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. Family of bacterial
            enzymes importing ribose, xylose, arabinose, galactose and
            methylgalactoside.
REFERENCE   1  [PMID:1282354]
  AUTHORS   Higgins CF.
  TITLE     ABC transporters: from microorganisms to man.
  JOURNAL   Annu. Rev. Cell. Biol. 8 (1992) 67-113.
REFERENCE   2  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   3  [PMID:9079938]
  AUTHORS   Kemner JM, Liang X, Nester EW.
  TITLE     The Agrobacterium tumefaciens virulence gene chvE is part of a
            putative ABC-type sugar transport operon.
  JOURNAL   J. Bacteriol. 179 (1997) 2452-8.
  ORGANISM  Agrobacterium tumefaciens
REFERENCE   4  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   5  [PMID:9673030]
  AUTHORS   Song S, Park C.
  TITLE     Utilization of D-ribose through D-xylose transporter.
  JOURNAL   FEMS. Microbiol. Lett. 163 (1998) 255-61.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6
  AUTHORS   Griffiths, J.K. and Sansom, C.E.
  TITLE     The Transporter Factsbook, Academic Press, San Diego, 1998.
PATHWAY     PATH: map02010  ABC transporters - General
ORTHOLOGY   KO: K02056  simple sugar transport system ATP-binding protein
            KO: K10441  ribose transport system ATP-binding protein
GENES       ECO: b1513(ego) b1900(araG) b2149(mglA) b2547(yphE) b3567(xylG)
                 b3749(rbsA) b4087(alsA) b4460(araH) b4485(ytfR)
            ECJ: JW1506(ego) JW1888(araG) JW2136(mglA) JW2531(yphE)
                 JW3539(xylG) JW3728(rbsA) JW4048(alsA) JW5752(ytfR)
            ECE: Z0417 Z2192 Z2953(araG) Z3404(mglA) Z3821(yphE) Z4992(xylG)
                 Z5250(rbsA) Z5691 Z5839
            ECS: ECs0376 ECs2120 ECs2608 ECs3041 ECs3413 ECs4450 ECs4691
                 ECs5073 ECs5206
            ECC: c2313(araG) c2683(mglA) c3069(yphE) c4016(rbsA) c4387(xylG)
                 c4677(rbsA) c5093(yjcW) c5326(ytfR)
            ECI: UTI89_C0356 UTI89_C2100(araG) UTI89_C2422(mglA)
                 UTI89_C2866(yphE) UTI89_C3693(rbsT) UTI89_C4108(xylG)
                 UTI89_C4304(rbsA) UTI89_C4682(alsA) UTI89_C4833(ytfR)
            ECP: ECP_1841 ECP_2188 ECP_2548 ECP_3345 ECP_3670 ECP_3948
                 ECP_4330 ECP_4478
            ECV: APECO1_1664 APECO1_2163(ytfR) APECO1_2363(alsA)
                 APECO1_2714(rbsA) APECO1_2882(xylG) APECO1_3186(rbsA)
                 APECO1_4402(mglA) APECO1_945(araG)
            ECW: EcE24377A_2130(araH) EcE24377A_2131(araG)
                 EcE24377A_2132(araF) EcE24377A_2444(mglA)
            ECX: EcHS_A1995 EcHS_A1996 EcHS_A1997 EcHS_A2283
            STY: STY3796 STY3896(rbsA)
            STT: t3544 t3637(rbsA)
            SPT: SPA3721(rbsA) SPA3917(ego)
            SEC: SC3795(rbsA)
            STM: STM2189(mglA) STM3882(rbsA) STM4074(ego)
            YPE: YPO0412 YPO0858 YPO0958(mglA) YPO1294 YPO1508(mglA) YPO1814
                 YPO2256(araG) YPO2500(rbsA) YPO2582 YPO3316 YPO3330 YPO3634
                 YPO3907 YPO3964 YPO4036
            YPK: y0234 y0329 y0859 y0873 y1150(rbsA) y1688(rbsA) y2097(araG)
                 y2493 y2661(mglA) y2890 y3243(rbsA) y3345 y3769 y3865(rbsA)
                 y4055(xylG)
            YPM: YP_0357(mglA1) YP_0370(mglA2) YP_1133(rbsA1) YP_1297(mglA3)
                 YP_1398(mglA4) YP_1579(mglA5) YP_2052(araG) YP_2315(rbsA2)
                 YP_3141(mglA6) YP_3327(rbsA3) YP_3398(mglA7) YP_3483(mglA8)
                 YP_3555(rbsA4) YP_3769(mglA9) YP_3913(mglA10)
            YPA: YPA_0306 YPA_0412 YPA_0803 YPA_0849 YPA_0850 YPA_1012
                 YPA_1189 YPA_1616 YPA_1995 YPA_2519 YPA_2814 YPA_2828 YPA_3647
                 YPA_3792 YPA_3873 YPA_4126
            YPN: YPN_0060 YPN_0282 YPN_0763 YPN_0777 YPN_1066 YPN_1725
                 YPN_2094 YPN_2310 YPN_2471 YPN_2684 YPN_3060 YPN_3156 YPN_3536
                 YPN_3613 YPN_3683
            YPP: YPDSF_0556 YPDSF_2672 YPDSF_3044 YPDSF_3328
            YPS: YPTB0128 YPTB0552(ego) YPTB0801 YPTB0814 YPTB1075 YPTB1326
                 YPTB1523(mglA) YPTB1687 YPTB2175(araG) YPTB2206 YPTB2536
                 YPTB3103 YPTB3230(mglA) YPTB3595 YPTB3807 YPTB3889(xylG)
            YPI: YpsIP31758_0909(rbsB1) YpsIP31758_0911(rbsC1)
                 YpsIP31758_0912(rbsA1) YpsIP31758_1507(rbsB2)
                 YpsIP31758_1508(rbsA2) YpsIP31758_1509(rbsC2)
                 YpsIP31758_1851(rbsA3) YpsIP31758_1852(rbsC3)
                 YpsIP31758_1853(rbsB3) YpsIP31758_1883(araH)
                 YpsIP31758_1884(araG) YpsIP31758_1885(araF)
                 YpsIP31758_2423(rbsA7) YpsIP31758_2424(rbsC4)
                 YpsIP31758_2971(rbsC5) YpsIP31758_2972(rbsA4)
                 YpsIP31758_2973(rbsB4) YpsIP31758_3250(rbsC6)
                 YpsIP31758_3251(rbsA5) YpsIP31758_3253(rbsB5)
                 YpsIP31758_4028(rbsB6) YpsIP31758_4029(rbsC7)
                 YpsIP31758_4030(rbsA6) YpsIP31758_4101(xylF)
            YEN: YE0009(rbsA) YE0820
            SFL: SF1583(ego) SF1946(araG) SF2234(mglA) SF2594(yphE)
                 SF3611(xylG) SF4262(ytfR)
            SFX: S1709 S2039(araG) S2363(mglA) S2766(yphE) S4158(xylG)
                 S4525(ytfR)
            SFV: SFV_1568 SFV_1943(araG) SFV_2224(mglA) SFV_2595(yphE)
                 SFV_3973(xylG) SFV_4263(ytfR)
            SSN: SSON_1218(araG) SSON_2205(mglA) SSON_2630(yphE)
                 SSON_3919(rbsA) SSON_4410(ytfR)
            SBO: SBO_1106(araG) SBO_2178(mglA) SBO_2573(yphE) SBO_3126(rbsA)
                 SBO_3575(xylG)
            SDY: SDY_1121(araG) SDY_4128 SDY_4247(ytfR)
            ECA: ECA0011(rbsA) ECA0099(xylG) ECA1460 ECA1948 ECA2272(araG)
                 ECA2719 ECA4235
            PLU: plu0056(rbsA) plu3143(lsrA)
            SGL: SG0612 SG0964
            ENT: Ent638_0289 Ent638_4115
            KPN: KPN_00598 KPN_04154(rbsA) KPN_04489
            SPE: Spro_0099 Spro_0101 Spro_1030 Spro_1565 Spro_1963 Spro_2245
                 Spro_2247 Spro_3219 Spro_3930 Spro_4227 Spro_4695 Spro_4696
                 Spro_4765 Spro_4766 Spro_4898 Spro_4899
            HIN: HI0502(rbsA) HI0823(mglA) HI1110(xylG)
            HIT: NTHI0630(rbsA) NTHI0988(mglA)
            HSO: HS_0031 HS_0051(ego) HS_0585(xylG) HS_0763(rbsA)
                 HS_0768(rbsA) HS_1580
            PMU: PM0155(rbsA_1) PM1039(mglA) PM1251(rbsA_2) PM1274 PM1326
                 PM1379
            MSU: MS0062(mglA) MS0642(mglA) MS1611(mglA)
            APL: APL_1419(mglA) APL_1670(rbsA) APL_1910(xylG)
            ASU: Asuc_0081 Asuc_0083 Asuc_0172 Asuc_0196 Asuc_0197 Asuc_0491
                 Asuc_0497 Asuc_0499 Asuc_1896
            VCH: VC1327 VCA0128
            VCO: VC0395_0009
            VVU: VV2_0062 VV2_1325
            VVY: VVA0162 VVA0569
            VPA: VPA1086 VPA1672
            VFI: VF1445(rbsA)
            PPR: PBPRA0463(xylG) PBPRB0020 PBPRB0473(mglA) PBPRB0719 PBPRB1557
                 PBPRB1871
            PAE: PA0136 PA1947(rbsA)
            PAU: PA14_39330(rbsA)
            PPU: PP_2455(rbsA) PP_2759
            PPF: Pput_3234 Pput_3236
            PST: PSPTO_0769 PSPTO_1160 PSPTO_1355 PSPTO_2368(rbsA-1)
                 PSPTO_2398(rbsA-2) PSPTO_2639 PSPTO_2995 PSPTO_3004(xylG)
                 PSPTO_3489
            PSB: Psyr_0673 Psyr_0775 Psyr_1002 Psyr_1164 Psyr_2152 Psyr_2372
                 Psyr_2571 Psyr_2876 Psyr_2885 Psyr_3264
            PSP: PSPPH_1051 PSPPH_2126(rbsA) PSPPH_2279 PSPPH_2354(xylG)
                 PSPPH_2363 PSPPH_2507 PSPPH_3184 PSPPH_4624
            PFL: PFL_0728(rbsA-1) PFL_2102(rbsA) PFL_2594
            PFO: Pfl_0681 Pfl_1920 Pfl_2301 Pfl_2338 Pfl_4140
            PEN: PSEEN1953
            ACI: ACIAD0205
            SPL: Spea_0516 Spea_0517 Spea_2283
            SHN: Shewana3_2074
            PIN: Ping_0341 Ping_2808
            HCH: HCH_01101 HCH_01167 HCH_02310 HCH_02469
            CSA: Csal_0361 Csal_1020
            MMW: Mmwyl1_1591 Mmwyl1_1858 Mmwyl1_1865 Mmwyl1_1867 Mmwyl1_1874
                 Mmwyl1_1985 Mmwyl1_1987 Mmwyl1_3108 Mmwyl1_3532 Mmwyl1_3533
                 Mmwyl1_4108 Mmwyl1_4110 Mmwyl1_4170 Mmwyl1_4188
            AHA: AHA_1903 AHA_1904 AHA_1905 AHA_2310(rbsA) AHA_4099(mglA)
            CVI: CV_2348(mglA) CV_3018(rbsA)
            RSO: RSc1016(RS04262) RSc1242(RS02750) RSc2173(RS01426)
                 RSc2757(araG) RSp1634(xylG)
            REU: Reut_A1653 Reut_A2498 Reut_B3990 Reut_B4133
            REH: H16_A0938 H16_B1498(frcA)
            RME: Rmet_0797
            BMA: BMA0914 BMA1197(rbsA) BMA2485(araG) BMAA0638 BMAA1814
            BMV: BMASAVP1_0136 BMASAVP1_A1641(rbsA)
            BML: BMA10299_0415 BMA10299_A0303(rbsA)
            BMN: BMA10247_0857(rbsA) BMA10247_A1165 BMA10247_A1811
            BXE: Bxe_A0547 Bxe_A1327 Bxe_A1938 Bxe_A3675 Bxe_A4341 Bxe_B0574
                 Bxe_B0892 Bxe_B1035 Bxe_B1372 Bxe_B1398 Bxe_B1404 Bxe_B2620
                 Bxe_B2963 Bxe_C1350
            BVI: Bcep1808_1508 Bcep1808_1559 Bcep1808_3382
            BUR: Bcep18194_A3704 Bcep18194_A4569 Bcep18194_A4683
                 Bcep18194_A4746 Bcep18194_B0046 Bcep18194_B0885
                 Bcep18194_B2370
            BCN: Bcen_0139 Bcen_0943 Bcen_1063 Bcen_1127 Bcen_3328 Bcen_3548
                 Bcen_5219 Bcen_6503
            BCH: Bcen2424_0622 Bcen2424_1425 Bcen2424_1543 Bcen2424_1607
                 Bcen2424_4819 Bcen2424_5039 Bcen2424_5640 Bcen2424_6737
            BAM: Bamb_0523 Bamb_1228 Bamb_1305 Bamb_1425 Bamb_1504 Bamb_4200
                 Bamb_4447 Bamb_4920 Bamb_6335
            BPS: BPSL1833 BPSL1993 BPSL2967(araG) BPSS0142 BPSS0255 BPSS0787
                 BPSS1032 BPSS2069
            BPM: BURPS1710b_1832 BURPS1710b_2020 BURPS1710b_2070
                 BURPS1710b_3483(araG) BURPS1710b_A0023 BURPS1710b_A1655
                 BURPS1710b_A2369(rbsA)
            BPL: BURPS1106A_1868 BURPS1106A_1921 BURPS1106A_A0197
                 BURPS1106A_A0360 BURPS1106A_A1057 BURPS1106A_A1627(araF)
            BPD: BURPS668_1855 BURPS668_1908 BURPS668_A0286 BURPS668_A0455
                 BURPS668_A1142 BURPS668_A1714
            BTE: BTH_I1180 BTH_I2340 BTH_I2343 BTH_I2434 BTH_I2474 BTH_I2646
                 BTH_II0211 BTH_II1609 BTH_II1627
            BPA: BPP2771
            BBR: BB2714
            RFR: Rfer_0437 Rfer_1901 Rfer_3129 Rfer_3166
            POL: Bpro_1483 Bpro_3205
            AAV: Aave_2253 Aave_4197
            VEI: Veis_0061 Veis_0738 Veis_2025 Veis_2046 Veis_2132 Veis_2686
                 Veis_2713 Veis_3418 Veis_3776
            MPT: Mpe_A0765 Mpe_A0803
            HPA: HPAG1_0690
            DVU: DVU1070
            DDE: Dde_0139 Dde_1510
            BBA: Bd0444(rbsA)
            DPS: DP0378 DP0681
            ADE: Adeh_1005
            MLO: mll0504 mll1002 mll1016 mll1506 mll1680 mll1722 mll1921
                 mll2146 mll3403 mll3598 mll3710 mll4176 mll4203 mll4992
                 mll5657 mll5705 mll5770 mll7012 mll7018 mll7081 mll7362
                 mll7373 mll7666 mll8568 mlr1693 mlr1891 mlr2442 mlr3154
                 mlr3336 mlr4967 mlr6802 mlr7066 mlr7286 mlr7585 mlr7627
                 mlr8214
            MES: Meso_0265 Meso_0839 Meso_1608 Meso_1693 Meso_3652 Meso_3706
            SME: SMa0072 SMa0199 SMa0216 SMa0270 SMa1421 SMa1509 SMa1998
                 SMa2127 SMa2365 SMb20017 SMb20124 SMb20317 SMb20351 SMb20485
                 SMb20503 SMb20507 SMb20622 SMb20673 SMb20713 SMb20718 SMb20855
                 SMb20894(gguA) SMb20904 SMb20930 SMb21019 SMb21344 SMb21376
                 SMb21422 SMb21588 SMc00245 SMc02020 SMc02032 SMc02169 SMc02325
                 SMc02337 SMc02773 SMc03815 SMc04127
            SMD: Smed_0103 Smed_0227 Smed_0228 Smed_0344 Smed_0914 Smed_2042
                 Smed_2442 Smed_2473 Smed_2475 Smed_3040 Smed_3126 Smed_3127
                 Smed_3229 Smed_3600 Smed_3602 Smed_3605 Smed_3637 Smed_3767
                 Smed_3819 Smed_3822 Smed_4114 Smed_4115 Smed_4262 Smed_4266
                 Smed_4317 Smed_4467 Smed_4475 Smed_4737 Smed_4738 Smed_4767
                 Smed_4910 Smed_4911 Smed_4928 Smed_5242 Smed_5264 Smed_5745
                 Smed_5834 Smed_5887
            ATU: Atu0065(frcA) Atu0127 Atu1792 Atu1898(rbsA) Atu2347(gguA)
                 Atu2819(rbsA) Atu3064 Atu3200 Atu3223 Atu3371 Atu3488 Atu3536
                 Atu3574(xylG) Atu3818(rbsA) Atu3880 Atu4032 Atu4321(rbsA)
                 Atu4370 Atu4745 Atu4843 Atu6069(rbsA)
            ATC: AGR_C_202 AGR_C_3297 AGR_C_3484 AGR_C_4264 AGR_C_5112
                 AGR_C_98(frcA) AGR_L_1081 AGR_L_1642 AGR_L_1931 AGR_L_2027
                 AGR_L_2509 AGR_L_2591 AGR_L_268 AGR_L_2683 AGR_L_2903
                 AGR_L_3184 AGR_L_3220 AGR_L_3487 AGR_L_85 AGR_L_992
                 AGR_pTi_138
            RET: RHE_CH00188 RHE_CH00467(frcA) RHE_CH00491
                 RHE_CH00613(rbsAch1) RHE_CH01212 RHE_CH01788(rbsAch2)
                 RHE_CH02081 RHE_CH02086 RHE_CH02359 RHE_CH02401(rbsAch3)
                 RHE_CH03164(gguA) RHE_CH03174(xylG) RHE_CH03190 RHE_CH03646
                 RHE_CH03694 RHE_CH03989 RHE_PB00077 RHE_PB00104 RHE_PB00123
                 RHE_PC00087 RHE_PC00147 RHE_PC00172 RHE_PC00225 RHE_PE00111
                 RHE_PE00288 RHE_PF00035 RHE_PF00216 RHE_PF00482
            RLE: RL0197 RL0491 RL0517 RL1745 RL1997 RL2372 RL2377 RL2449
                 RL2722(rbsA) RL3616 RL3626 RL3842 RL4174 RL4230 RL4654
                 pRL100338 pRL100354 pRL100394 pRL100416 pRL100463
                 pRL110412(rhaT) pRL120192 pRL120200 pRL120202 pRL120285
                 pRL120391 pRL120757 pRL80086 pRL90084(rbsA) pRL90205 pRL90224
                 pRL90246
            BME: BMEI0391 BMEI0665 BMEI1392 BMEII0085 BMEII0145 BMEII0300
                 BMEII0361 BMEII0432 BMEII0698 BMEII0982
            BMF: BAB1_0565 BAB1_1358 BAB1_1650 BAB2_0008 BAB2_0238(rbsA-4)
                 BAB2_0375(rbsA-3) BAB2_0670 BAB2_1110
            BMS: BR0542(rbsA-1) BR1339 BR1632(rbsA-2) BRA0009 BRA0266 BRA0570
                 BRA0860(rbsA-3) BRA0936 BRA0995(rbsA-4) BRA1151(xylG)
            BMB: BruAb1_0564(rbsA-1) BruAb1_1337 BruAb1_1620(rbsA-2)
                 BruAb2_0009 BruAb2_0239(rbsA-4) BruAb2_0297
                 BruAb2_0371(rbsA-3) BruAb2_0654 BruAb2_1088(xylG)
            OAN: Oant_0070 Oant_0290 Oant_0292 Oant_1415 Oant_1416 Oant_1426
                 Oant_1832 Oant_2807 Oant_2809 Oant_2840 Oant_2841 Oant_2914
                 Oant_3061 Oant_3074 Oant_3346 Oant_3407 Oant_3414 Oant_3416
                 Oant_3567 Oant_3568 Oant_4061 Oant_4064 Oant_4066 Oant_4369
                 Oant_4829
            BJA: bll2677 bll5784 blr1121 blr2270 blr3201 blr3209 blr6152
                 blr6155 blr7871
            BRA: BRADO1394(rbsA) BRADO1818(araG) BRADO1819 BRADO5633 BRADO5634
                 BRADO6756
            BBT: BBta_2138(araG) BBta_2139 BBta_4826 BBta_4828 BBta_4830
                 BBta_6154 BBta_6155
            RPA: RPA4575
            RPD: RPD_1121
            XAU: Xaut_2414
            CCR: CC_0860
            SIL: SPO0378 SPO0651 SPO0863(xylG) SPO2803 SPOA0255 SPOA0258(rbsA)
            SIT: TM1040_0370 TM1040_0496 TM1040_1188 TM1040_3095 TM1040_3176
                 TM1040_3253 TM1040_3269 TM1040_3341
            RSP: RSP_0344 RSP_0988 RSP_1178 RSP_1247 RSP_2210 RSP_2366
                 RSP_3503 RSP_3557 RSP_3688 RSP_3702 RSP_3733
            RSQ: Rsph17025_0235 Rsph17025_2619 Rsph17025_2684 Rsph17025_3351
            JAN: Jann_2595 Jann_3088
            RDE: RD1_0486 RD1_0865 RD1_1645 RD1_2211 RD1_2382 RD1_3079(rbsA)
                 RD1_4071
            PDE: Pden_1683 Pden_2159 Pden_4850
            GOX: GOX2220
            ACR: Acry_0505 Acry_1063 Acry_1139 Acry_1365 Acry_1594 Acry_1602
                 Acry_1852 Acry_1971 Acry_1973 Acry_2213 Acry_2214 Acry_2236
                 Acry_2237 Acry_2592 Acry_2601 Acry_2606 Acry_2982 Acry_2983
            RRU: Rru_A0249 Rru_A1337 Rru_A1364 Rru_A2785
            BSU: BG10879(rbsA) BG12350(yufO)
            BHA: BH2322 BH3441 BH3730(rbsA)
            BAN: BA0667(rbsA) BA2978 BA3926
            BAR: GBAA0667(rbsA) GBAA2978 GBAA3926
            BAA: BA_1255 BA_3484 BA_4398
            BAT: BAS0634 BAS2766 BAS3642
            BCE: BC0662(rbsA) BC0767 BC2963 BC3790
            BCA: BCE_0735(rbsA) BCE_3015 BCE_3825
            BCZ: BCZK0577(rbsA) BCZK2696 BCZK3550
            BCY: Bcer98_0563 Bcer98_0564
            BTK: BT9727_0578(rbsA) BT9727_2716 BT9727_3532
            BTL: BALH_0609(rbsA)
            BLI: BL01747 BL02441(rbsA)
            BLD: BLi00443 BLi03843(rbsA)
            BCL: ABC0410 ABC1090 ABC3546(rbsA)
            OIH: OB2574(rbsA) OB3387
            GKA: GK0947 GK1284 GK1880 GK1894 GK1909(araG) GK3228
            GTN: GTNG_3172
            SHA: SH0177(rbsA)
            SSP: SSP1394(rbsA)
            LMO: lmo1389
            LMF: LMOf2365_1408
            LIN: lin1426
            LWE: lwe1405
            LLA: L165279(yngE) L84240(rbsA)
            LLC: LACR_1452 LACR_1800
            LLM: llmg_0787(rbsD)
            SPY: SPy_1227
            SPZ: M5005_Spy_0941
            SPM: spyM18_1179
            SPG: SpyM3_0867
            SPS: SPs1067
            SPA: M6_Spy0930
            SPB: M28_Spy0913
            SPN: SP_0846
            SPR: spr0748(ABC-NBD)
            SAG: SAG0116(rbsA) SAG0955
            SAN: gbs0115 gbs0943
            SAK: SAK_0168(rbsA) SAK_1050
            SMU: SMU.1120
            STC: str0809
            STL: stu0809
            SSA: SSA_1039
            LAC: LBA1483(rbsA) LBA1944
            LDB: Ldb2184
            LBU: LBUL_2003
            LCA: LSEI_0308
            EFA: EF0178
            OOE: OEOE_1607
            STH: STH1235 STH2341 STH773
            CAC: CAC0703
            CPE: CPE1342 CPE1579 CPE1630(rbsA)
            CPF: CPF_1549(mglA) CPF_1882(rbsA)
            CPR: CPR_1342 CPR_1601(rbsA)
            CTC: CTC00370 CTC00861(mglA) CTC00905(rbsA) CTC02350(rbsA)
            CNO: NT01CX_0164
            CTH: Cthe_0391
            CDF: CD0301(rbsA) CD1587
            CBE: Cbei_2359 Cbei_2380 Cbei_2382 Cbei_4432 Cbei_4448 Cbei_4450
                 Cbei_4459 Cbei_4460 Cbei_4967
            AMT: Amet_0458 Amet_0588 Amet_2812 Amet_2814 Amet_2815 Amet_3797
            CHY: CHY_1535
            DSY: DSY1170
            DRM: Dred_2524
            CSC: Csac_0240 Csac_0393 Csac_0394 Csac_2504 Csac_2506 Csac_2510
            TTE: TTE0204(mglA) TTE0291(mglA2) TTE0458(mglA3) TTE0763(mglA4)
            MTA: Moth_0613 Moth_1952 Moth_2021
            MGE: MG_119(mglA)
            MPN: MPN258(yjcW)
            MPU: MYPU_3440(xylG) MYPU_6190(mglA)
            MPE: MYPE5890
            MGA: MGA_0372(mglA)
            MMY: MSC_0010(rbsA)
            MMO: MMOB0140(xylG) MMOB0370(mglA)
            MHY: mhp147(rbsA) mhp512 mhp624(mglA)
            MHJ: MHJ_0225(mglA) MHJ_0512(xylG) MHJ_0607
            MHP: MHP7448_0231(mglA) MHP7448_0514(xylG) MHP7448_0605
            MSY: MS53_0137(mglA)
            MCP: MCAP_0037
            UUR: UU015(mglA)
            MFL: Mfl668
            MSM: MSMEG_3091 MSMEG_3602 MSMEG_4170 MSMEG_6803
            CGL: NCgl0031(cgl0032) NCgl1204(cgl1252)
            CGB: cg0046 cg1411
            CEF: CE0021
            CDI: DIP0023
            CJK: jk1684
            RHA: RHA1_ro00820 RHA1_ro04085 RHA1_ro09082
            SCO: SCO0811(SCF43.22c) SCO2405(SC4A7.33) SCO2746(SCC57A.17)
                 SCO4886(2SCK8.12) SCO6010(SC7B7.07) SCO6259(SCAH10.24)
                 SCO6567(SC3F9.02) SCO6981(SC8F11.07)
            SMA: SAV1828 SAV1981 SAV2246 SAV3369 SAV5319(rbsA) SAV5702 SAV5768
                 SAV6656 SAV7153 SAV7280 SAV7416 SAV970
            TWH: TWT330
            TWS: TW441
            LXX: Lxx00320 Lxx04610(rbsA) Lxx22220(rbsA)
            ART: Arth_1825 Arth_1920
            AAU: AAur_0348(rbsB) AAur_0874(rbsA) AAur_1892
            PAC: PPA0015 PPA1733
            TFU: Tfu_1921
            FAL: FRAAL0204(rbsA) FRAAL2527
            ACE: Acel_0353 Acel_0578 Acel_0717
            KRA: Krad_1458 Krad_2944 Krad_3727
            SEN: SACE_0941(rbsA) SACE_1881 SACE_2987 SACE_5659 SACE_6228
                 SACE_6579
            BLO: BL0034 BL1692 BL1695
            RXY: Rxyl_0946 Rxyl_3003
            FNU: FN1166(mglA) FN1898
            RBA: RB3496(rbsA) RB5972(rbsA) RB9385(rbsA)
            BBU: BB0318(mglA) BB0677(mglA)
            BGA: BG0700(mglA-2)
            BAF: BAPKO_0721(mglA-2)
            TPA: TP0300 TP0321 TP0685
            TDE: TDE0952 TDE1949 TDE2216(mglA)
            CYA: CYA_1583 CYA_2437 CYA_2888
            CYB: CYB_0390 CYB_1489 CYB_1651
            GVI: glr0808
            ANA: alr5362
            AVA: Ava_2172
            TER: Tery_0800 Tery_3673
            CCH: Cag_1498
            PLT: Plut_0922
            RRS: RoseRS_2726 RoseRS_2727 RoseRS_3056
            RCA: Rcas_1881 Rcas_2116 Rcas_2668
            DRA: DR_0957
            DGE: Dgeo_1374 Dgeo_2458 Dgeo_2703 Dgeo_2855
            TTH: TTC0734 TTC0938
            TTJ: TTHA1099 TTHA1304
            TMA: TM0103 TM0115 TM0956
            TPT: Tpet_0320 Tpet_0812 Tpet_1793 Tpet_1794
            FNO: Fnod_1668
            AFU: AF0887(rbsA-1)
            HAL: VNG0901G(rbsA)
            HMA: pNG7252(rbsA) rrnAC2655(rbsA)
            HWA: HQ2451A(rbsA)
            PHO: PH1713
            PAB: PAB0303(rbsA)
            PFU: PF1696
            TKO: TK0658
            APE: APE_0063 APE_2588
            PAI: PAE3120 PAE3413
STRUCTURES  PDB: 2GX6  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.17
            ExPASy - ENZYME nomenclature database: 3.6.3.17
            ExplorEnz - The Enzyme Database: 3.6.3.17
            ERGO genome analysis and discovery system: 3.6.3.17
            BRENDA, the Enzyme Database: 3.6.3.17
///
ENTRY       EC 3.6.3.18                 Enzyme
NAME        oligosaccharide-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (disaccharide-importing)
REACTION    ATP + H2O + oligosaccharideout = ADP + phosphate + oligosaccharidein
            [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            oligosaccharide [CPD:C00930]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            oligosaccharide [CPD:C00930]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A bacterial enzyme
            that imports lactose, melibiose and raffinose.
REFERENCE   1  [PMID:1282354]
  AUTHORS   Higgins CF.
  TITLE     ABC transporters: from microorganisms to man.
  JOURNAL   Annu. Rev. Cell. Biol. 8 (1992) 67-113.
REFERENCE   2  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   3  [PMID:8336670]
  AUTHORS   Tam R, Saier MH Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria.
  JOURNAL   Microbiol. Rev. 57 (1993) 320-46.
REFERENCE   4  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   5  [PMID:1630315]
  AUTHORS   Williams SG, Greenwood JA, Jones CW.
  TITLE     Molecular analysis of the lac operon encoding the
            binding-protein-dependent lactose transport system and
            beta-galactosidase in Agrobacterium radiobacter.
  JOURNAL   Mol. Microbiol. 6 (1992) 1755-68.
  ORGANISM  Agrobacterium radiobacter
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.18
            ExPASy - ENZYME nomenclature database: 3.6.3.18
            ExplorEnz - The Enzyme Database: 3.6.3.18
            ERGO genome analysis and discovery system: 3.6.3.18
            BRENDA, the Enzyme Database: 3.6.3.18
///
ENTRY       EC 3.6.3.19                 Enzyme
NAME        maltose-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (maltose-importing)
REACTION    ATP + H2O + maltoseout = ADP + phosphate + maltosein [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            maltose [CPD:C00208]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            maltose [CPD:C00208]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. Comprises bacterial
            enzymes that import maltose and maltose oligosaccharides.
REFERENCE   1  [PMID:1282354]
  AUTHORS   Higgins CF.
  TITLE     ABC transporters: from microorganisms to man.
  JOURNAL   Annu. Rev. Cell. Biol. 8 (1992) 67-113.
REFERENCE   2  [PMID:8437518]
  AUTHORS   Dassa E, Muir S.
  TITLE     Membrane topology of MalG, an inner membrane protein from the
            maltose transport system of Escherichia coli.
  JOURNAL   Mol. Microbiol. 7 (1993) 29-38.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   4  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   5
  AUTHORS   Griffiths, J.K. and Sansom, C.E.
  TITLE     The Transporter Factsbook, Academic Press, San Diego, 1998.
PATHWAY     PATH: map02010  ABC transporters - General
ORTHOLOGY   KO: K10111  maltose/maltodextrin transport system ATP-binding
                        protein
GENES       TET: TTHERM_00850570
            ECO: b4035(malK)
            ECJ: JW3995(malK)
            ECE: Z5633(malK)
            ECS: ECs5018
            ECC: c5005(malK)
            ECI: UTI89_C4605(malK)
            ECP: ECP_4253
            ECV: APECO1_2433(malK)
            ECW: EcE24377A_4587(malK)
            ECX: EcHS_A4275
            STY: STY4426(malK)
            STT: t4136(malK)
            SPT: SPA4047(malK)
            SEC: SC4109(malK)
            STM: STM4230(malK)
            YPE: YPO0857 YPO3712(malK)
            YPK: y0031(malK) y3242
            YPM: YP_3074(malK2) YP_3554
            YPA: YPA_0032 YPA_0413
            YPN: YPN_0029 YPN_3059
            YPS: YPTB3102 YPTB3643(malK)
            YPI: YpsIP31758_0308(malK2) YpsIP31758_0913(malK1)
            SFL: SF4170(malK)
            SFX: S3561(malK)
            SFV: SFV_4179(malK)
            SSN: SSON_4213(malK)
            ECA: ECA3174(malK)
            PLU: plu0457(malK)
            MSU: MS2067(malK)
            APL: APL_1236(malK)
            VCH: VCA0946
            VVU: VV2_1584
            VVY: VVA0396
            VPA: VPA1402
            VFI: VFA0800(malK)
            PPR: PBPRB0420
            PST: PSPTO_0886(malK)
            PSB: Psyr_0759
            PSP: PSPPH_5191(malK)
            PIN: Ping_2011
            HCH: HCH_00479
            CSA: Csal_0262 Csal_2614
            AHA: AHA_1670
            BPM: BURPS1710b_A1185(malK)
            VEI: Veis_0947
            BBA: Bd1225(malK)
            SME: SMc04140
            HBU: Hbut_0308 Hbut_1466
STRUCTURES  PDB: 2AWN  2AWO  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.19
            ExPASy - ENZYME nomenclature database: 3.6.3.19
            ExplorEnz - The Enzyme Database: 3.6.3.19
            ERGO genome analysis and discovery system: 3.6.3.19
            BRENDA, the Enzyme Database: 3.6.3.19
///
ENTRY       EC 3.6.3.20                 Enzyme
NAME        glycerol-3-phosphate-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (glycerol-3-phosphate-importing)
REACTION    ATP + H2O + glycerol-3-phosphateout = ADP + phosphate +
            glycerol-3-phosphatein [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            glycerol-3-phosphate [CPD:C00093]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            glycerol-3-phosphate [CPD:C00093]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A bacterial enzyme
            that imports phosphorylated glycerol.
REFERENCE   1  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   2
  AUTHORS   Griffiths, J.K. and Sansom, C.E.
  TITLE     The Transporter Factsbook, Academic Press, San Diego, 1998.
REFERENCE   3  [PMID:1874408]
  AUTHORS   Bahl H, Burchhardt G, Wienecke A.
  TITLE     Nucleotide sequence of two Clostridium thermosulfurogenes EM1 genes
            homologous to Escherichia coli genes encoding integral membrane
            components of binding protein-dependent transport systems.
  JOURNAL   FEMS. Microbiol. Lett. 65 (1991) 83-7.
  ORGANISM  Escherichia coli [GN:eco], Clostridium thermosulfurogenes
PATHWAY     PATH: map02010  ABC transporters - General
ORTHOLOGY   KO: K05816  sn-glycerol 3-phosphate transport system ATP-binding
                        protein
GENES       ECO: b3450(ugpC)
            ECJ: JW3415(ugpC)
            ECE: Z4818(ugpC)
            ECS: ECs4296
            ECC: c4239(ugpC)
            ECI: UTI89_C3957(ugpC)
            ECP: ECP_3543
            ECV: APECO1_3009(ugpC)
            STY: STY4257(ugpC)
            STT: t3967(ugpC)
            SPT: SPA3406(ugpC)
            SEC: SC3483(ugpC)
            STM: STM3554(ugpC)
            YPE: YPO3793(ugpC)
            YPK: y0437(ugpC)
            YPM: YP_3256(ugpC)
            YPA: YPA_0231
            YPN: YPN_0171
            YPS: YPTB0241(ugpC)
            YEN: YE0244(ugpC)
            SSN: SSON_3688(ugpC)
            SBO: SBO_3446(ugpC)
            ECA: ECA4319(ugpC)
            XFA: XF1067
            XFT: PD0347(algS)
            XCC: XCC2135(ugpC)
            XCB: XC_1978
            XCV: XCV2238(ugpC)
            XAC: XAC2072(ugpC)
            XOO: XOO2313(ugpC)
            XOM: XOO_2190(XOO2190)
            VCH: VC1552
            VVU: VV1_2752
            VVY: VV1509
            PST: PSPTO_0661(ugpC)
            PSB: Psyr_4505
            PSP: PSPPH_4533(ugpC)
            PIN: Ping_2096
            LPN: lpg1729(ugpC)
            LPF: lpl1693
            LPP: lpp1694
            CSA: Csal_2735
            RSO: RSc1267(upgC)
            REU: Reut_A2049
            REH: H16_A2327
            RME: Rmet_2052
            BMA: BMA2741(ugpC)
            BMV: BMASAVP1_A3212(ugpC)
            BML: BMA10299_A1763(ugpC)
            BMN: BMA10247_2791(ugpC)
            BXE: Bxe_A0445
            BUR: Bcep18194_A3495
            BCN: Bcen_2709
            BCH: Bcen2424_0398
            BAM: Bamb_0317
            BPS: BPSL3163
            BPM: BURPS1710b_3722(ugpC) BURPS1710b_A0235
            BPL: BURPS1106A_3752(ugpC)
            BPD: BURPS668_3694(ugpC)
            BTE: BTH_I3018
            BPE: BP0122 BP1284(ugpC)
            BPA: BPP2947(ugpC) BPP4346
            BBR: BB2915(ugpC) BB4932
            RFR: Rfer_1284
            POL: Bpro_0854
            AAV: Aave_3653
            AJS: Ajs_0859 Ajs_3307
            DVU: DVU3161
            DVL: Dvul_0225
            LIP: LI0076
            MLO: mll3499 mlr8490
            SME: SMb20419(ugpC)
            ATU: Atu0308(ugpC) Atu3099(ugpC) Atu3188(ugpC) Atu5062(ugpC)
            ATC: AGR_C_533 AGR_L_3244 AGR_L_3418 AGR_pAT_82
            RET: RHE_CH02753(ugpCch1) RHE_CH03369(ugpCch2) RHE_PC00081(ugpCc)
            RLE: RL3132(ugpC) RL3804 pRL120014 pRL90110
            BME: BMEII0621
            BMF: BAB2_0582(ugpC)
            BMS: BRA0658(ugpC)
            BMB: BruAb2_0568(ugpC)
            BJA: bll0730 blr3917
            RPA: RPA0055(ugpC) RPA3471
            RPB: RPB_0650
            RPC: RPC_0408
            RPD: RPD_0183
            RPE: RPE_0436
            BHE: BH01840(ugpC)
            BQU: BQ01730(ugpC)
            BBK: BARBAKC583_0346(ugpC)
            SIL: SPO0237(upgC)
            SIT: TM1040_0852 TM1040_3217
            RSP: RSP_3287(upgC)
            RSH: Rsph17029_4019
            JAN: Jann_2078
            RDE: RD1_2936(ugpC) RD1_3572
            PDE: Pden_4187
            BHA: BH1076
            BAN: BA0566
            BAR: GBAA0566
            BAA: BA_1144
            BAT: BAS0535
            BCE: BC0567(ugpC)
            BCA: BCE_0629
            BCZ: BCZK0479
            BTK: BT9727_0477
            BTL: BALH_0506
            BCL: ABC0352
            LPL: lp_1324
            LCA: LSEI_2765
            OOE: OEOE_1456
            MTU: Rv2832c(ugpC)
            MTC: MT2898
            MBO: Mb2856c(ugpC)
            MBB: BCG_2852c(ugpC)
            CGL: NCgl1332(cgl1386)
            CGB: cg1571(ugpC)
            CEF: CE1517
            RHA: RHA1_ro05117
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.20
            ExPASy - ENZYME nomenclature database: 3.6.3.20
            ExplorEnz - The Enzyme Database: 3.6.3.20
            ERGO genome analysis and discovery system: 3.6.3.20
            BRENDA, the Enzyme Database: 3.6.3.20
///
ENTRY       EC 3.6.3.21                 Enzyme
NAME        polar-amino-acid-transporting ATPase;
            histidine permease
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (polar-amino-acid-importing)
REACTION    ATP + H2O + polar amino acidout = ADP + phosphate + polar amino
            acidin [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            polar amino acid [CPD:C06699]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            polar amino acid [CPD:C06699]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. Comprises bacterial
            enzymes that import His, Arg, Lys, Glu, Gln, Asp, ornithine,
            octopine and nopaline.
REFERENCE   1  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   2  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   3  [PMID:9346917]
  AUTHORS   Nikaido K, Liu PQ, Ames GF.
  TITLE     Purification and characterization of HisP, the ATP-binding subunit
            of a traffic ATPase (ABC transporter), the histidine permease of
            Salmonella typhimurium. Solubility, dimerization, and ATPase
            activity.
  JOURNAL   J. Biol. Chem. 272 (1997) 27745-52.
  ORGANISM  Salmonella typhimurium
REFERENCE   4  [PMID:9315727]
  AUTHORS   Walshaw DL, Lowthorpe S, East A, Poole PS.
  TITLE     Distribution of a sub-class of bacterial ABC polar amino acid
            transporter and identification of an N-terminal region involved in
            solute specificity.
  JOURNAL   FEBS. Lett. 414 (1997) 397-401.
PATHWAY     PATH: map02010  ABC transporters - General
ORTHOLOGY   KO: K02028  polar amino acid transport system ATP-binding protein
            KO: K10017  histidine transport system ATP-binding protein
GENES       ECO: b2306(hisP)
            ECJ: JW2303(hisP)
            ECE: Z3568(hisP)
            ECS: ECs3190
            ECC: c2848(hisP)
            ECI: UTI89_C2590(hisP)
            ECP: ECP_2345
            ECV: APECO1_4258(hisP)
            STY: STY1436 STY2581(hisP)
            STT: t0513(hisP) t1538
            SPT: SPA0513(hisP)
            SEC: SC1630(gltL) SC2352(hisP)
            STM: STM1635 STM2351(hisP)
            YPE: YPO0609 YPO2777(hisP) YPO3254
            YPK: y0935(glnQ) y1610(hisP) y3569
            YPM: YP_0679(glnQ1) YP_2387(hisP) YP_2927
            YPA: YPA_2065 YPA_2745 YPA_3181
            YPN: YPN_0472 YPN_0842 YPN_2170
            YPS: YPTB0869 YPTB2607(hisP) YPTB3446
            YEN: YE1321(hisP)
            SFL: SF2382(hisP)
            SFX: S2517(hisP)
            SFV: SFV_2373(hisP)
            SSN: SSON_2364(hisP)
            SBO: SBO_2343(hisP)
            SDY: SDY_2505(hisP)
            ECA: ECA0854 ECA0855 ECA2970 ECA3047(hisP) ECA3492 ECA3539 ECA4193
            PLU: plu4486
            WBR: WGLp190(gltL)
            SGL: SG0915 SG1611
            HIN: HI1078(gltL)
            HIT: NTHI1241
            HDU: HD2032
            HSO: HS_0210
            MSU: MS1275(glnQ)
            APL: APL_1603 APL_1693
            VCH: VC0008 VC1864 VCA1037
            VVU: VV1_1003 VV1_2101
            VVY: VV0006 VV2339
            VPA: VP0006 VP0998 VPA0822
            VFI: VF0006 VF1588(hisP) VFA0393
            PPR: PBPRA0005(yckI) PBPRA1477 PBPRA2742 PBPRB1263
            PAE: PA2926(hisP) PA5152
            PAU: PA14_26210(hisP)
            PPU: PP_0283 PP_3597 PP_4425 PP_4751
            PST: PSPTO_1830(hisP) PSPTO_2630 PSPTO_2778 PSPTO_3009 PSPTO_3083
                 PSPTO_4140 PSPTO_5248 PSPTO_5357
            PSB: Psyr_0295 Psyr_2506 Psyr_2890 Psyr_2965 Psyr_3567 Psyr_3878
                 Psyr_4911
            PSP: PSPPH_0282 PSPPH_1384 PSPPH_2275(glnQ2) PSPPH_2347 PSPPH_2663
                 PSPPH_3523(hisP) PSPPH_4938
            PFL: PFL_0343 PFL_1263(glnQ) PFL_2194 PFL_2284 PFL_2357(glnQ)
                 PFL_3058 PFL_3551(glnQ) PFL_5020
            PFO: Pfl_0312 Pfl_1206 Pfl_2854 Pfl_3089 Pfl_5462
            PEN: PSEEN1855 PSEEN2663 PSEEN5207
            PAR: Psyc_0294
            ACI: ACIAD3488 ACIAD3592
            SON: SO_1042
            SHN: Shewana3_0880
            PIN: Ping_2825
            CBU: CBU_0481
            LPN: lpg0493
            LPF: lpl0531
            LPP: lpp0555
            HCH: HCH_00890 HCH_05213
            ASA: ASA_2677(hisP)
            NME: NMB0789
            NMA: NMA1000
            NGO: NGO0374
            CVI: CV_0855(hisP) CV_2981
            RSO: RS00357(RSp0479) RSc2106(RS01498) RSc3408(RS01717)
            REU: Reut_A1592 Reut_A3012
            REH: H16_A0045(hisP) H16_A0811 H16_A2756 H16_A3308 H16_B1478
                 H16_B1810
            BMA: BMA0589 BMA0744 BMA2136 BMAA1218 BMAA1238(hisP) BMAA1688
            BMV: BMASAVP1_0208(hisP) BMASAVP1_A0985 BMASAVP1_A2429
            BML: BMA10299_0481(hisP) BMA10299_A2862 BMA10299_A3015
            BMN: BMA10247_1582 BMA10247_1739 BMA10247_A1091(hisP)
            BXE: Bxe_A1434 Bxe_A1502 Bxe_A2431 Bxe_A2925 Bxe_A3393 Bxe_B1061
                 Bxe_C0064 Bxe_C0396 Bxe_C0778 Bxe_C1133 Bxe_C1160
            BUR: Bcep18194_A4289 Bcep18194_A5734 Bcep18194_B2375
            BCN: Bcen_0698 Bcen_1795 Bcen_4636
            BCH: Bcen2424_1177 Bcen2424_2407 Bcen2424_3727
            BAM: Bamb_1056 Bamb_2452 Bamb_5466
            BPS: BPSL1030(hisP) BPSL2392(hisP) BPSL2617 BPSS0983(hisP)
                 BPSS0998 BPSS1671
            BPM: BURPS1710b_1245(hisP) BURPS1710b_2851(hisP) BURPS1710b_A0737
                 BURPS1710b_A2595(hisP)
            BPL: BURPS1106A_1092(hisP) BURPS1106A_2789(hisP) BURPS1106A_A1357
            BPD: BURPS668_1087(hisP)
            BTE: BTH_I0887 BTH_I1773 BTH_II1408
            BPE: BP1362 BP1510 BP1534 BP1855(glnQ)
            BPA: BPP0683 BPP1206 BPP1427 BPP1566(glnQ) BPP1975 BPP2129 BPP2703
            BBR: BB0690 BB1526 BB2163 BB2501 BB2644(glnQ) BB2795
            RFR: Rfer_0164 Rfer_0234 Rfer_0239 Rfer_0968 Rfer_1030 Rfer_2971
                 Rfer_3809 Rfer_4158
            POL: Bpro_0403 Bpro_1038 Bpro_1390 Bpro_1438 Bpro_1504 Bpro_2727
                 Bpro_3475 Bpro_3973
            PNA: Pnap_1488
            VEI: Veis_3332
            MPT: Mpe_A2883
            HPA: HPAG1_0176 HPAG1_0733 HPAG1_0922 HPAG1_1108 HPAG1_1109
                 HPAG1_1450 HPAG1_1525
            CJE: Cj0469 Cj0902(glnQ)
            CJR: CJE0519 CJE0981
            CJU: C8J_0442 C8J_0839(glnQ) C8J_0859(pebC)
            GSU: GSU0798
            DVU: DVU0388 DVU0968 DVU2343
            DDE: Dde_0184 Dde_2308 Dde_3744
            LIP: LI0127(glnQ) LI0718(glnQ)
            BBA: Bd0823(glnQ)
            DPS: DP1029
            SFU: Sfum_3901
            RPR: RP868(glnQ2)
            RTY: RT0859(glnQ)
            RCO: RC1341(glnQ)
            RFE: RF_1370(glnQ)
            RBE: RBE_1318(glnQ)
            WOL: WD0455
            MLO: mll3858 mll5204 mlr2206 mlr3801(glnQ) mlr7132 mlr9616
            MES: Meso_0039 Meso_3147 Meso_4427
            SME: SMa0083 SMa0489 SMa0508 SMa2195 SMb20427 SMb21096 SMb21138
                 SMc02260 SMc03135 SMc03894
            ATU: Atu1391 Atu1396 Atu3360 Atu3417 Atu4533 Atu4690 Atu4752
                 Atu5236 Atu5480
            ATC: AGR_C_2571 AGR_C_2580(glnQ) AGR_L_257 AGR_L_2810
                 AGR_L_2925(glnQ) AGR_L_381(glnQ) AGR_L_671 AGR_pAT_331(glnQ)
                 AGR_pAT_712
            RET: RHE_CH01462 RHE_CH02292 RHE_CH04004 RHE_PC00007 RHE_PC00159
                 RHE_PE00227 RHE_PF00159 RHE_PF00164 RHE_PF00187 RHE_PF00190
            RLE: RL1042 RL2921 RL4636 pRL100357 pRL100409 pRL110079 pRL120047
                 pRL120074 pRL120081 pRL80063
            BME: BMEI0108 BMEI0111 BMEII0599
            BMF: BAB1_1957 BAB1_1960 BAB2_0556
            BMS: BR1956 BR1959 BRA0684
            BMB: BruAb1_1932 BruAb1_1935 BruAb2_0545
            BJA: bll3978 bll6387 bll6911 bll7204 blr2226 blr3099 blr3311
                 blr4464 blr8119
            BHE: BH06340
            BQU: BQ06890
            CCR: CC_1439
            SIL: SPO1307 SPO2367 SPO2664 SPO3043(glnQ) SPOA0068
            SIT: TM1040_1711 TM1040_3040
            RSP: RSP_0371 RSP_3458 RSP_3745
            RSH: Rsph17029_0396 Rsph17029_3584
            RDE: RD1_1899 RD1_2184
            SAL: Sala_2412
            GOX: GOX1572
            BSU: BG11185(yckI) BG11729(yqiZ) BG11891(yxeO) BG12604(hisP)
            BHA: BH0172 BH1463
            BAN: BA0368 BA0857 BA4374
            BAR: GBAA0368 GBAA0857 GBAA4374
            BAA: BA_0942 BA_1437 BA_4830
            BAT: BAS0354 BAS0814 BAS4057
            BCE: BC0403(glnQ) BC0874 BC4148(artP)
            BCA: BCE_0469 BCE_0947 BCE_3546(glnQ) BCE_4223
            BCZ: BCZK0340(glnQ) BCZK0755 BCZK3903
            BTK: BT9727_0337(glnQ) BT9727_0762 BT9727_3896
            BLI: BL01510(artM) BL01827
            BLD: BLi00418(yckI) BLi02574(yqiZ)
            BCL: ABC0913
            OIH: OB0557 OB2072
            GKA: GK3455
            SAU: SA1674 SA2200
            SAV: SAV1857 SAV2412
            SAM: MW1798 MW2334
            SAR: SAR1948(glnQ) SAR2502
            SAS: SAS1780 SAS2303
            SAC: SACOL1915 SACOL2410
            SAB: SAB1791c(glnQ) SAB2292c
            SAA: SAUSA300_1807 SAUSA300_2357
            SAO: SAOUHSC_02697
            SEP: SE1540 SE1991
            SER: SERP1394 SERP2003
            SHA: SH0641 SH1105
            SSP: SSP0244 SSP0621 SSP0938
            LMO: lmo0848 lmo1739 lmo2251 lmo2346
            LMF: LMOf2365_0865 LMOf2365_1763 LMOf2365_2284 LMOf2365_2316
            LIN: lin0841 lin1850 lin2353 lin2440
            LWE: lwe0841 lwe1756 lwe2267
            LLA: L164012(yjgE) L2385(glnQ) L37916(gltQ)
            LLC: LACR_1011 LACR_1924 LACR_1977
            SPY: SPy_0276 SPy_1275 SPy_1316 SPy_1506 SPy_1657
            SPZ: M5005_Spy_0235 M5005_Spy_0983 M5005_Spy_1077(glnQ.2)
                 M5005_Spy_1237(artP) M5005_Spy_1362
            SPM: spyM18_0263 spyM18_1224 spyM18_1328(glnQ) spyM18_1524
                 spyM18_1668
            SPG: SpyM3_0202 SpyM3_0907 SpyM3_0998(glnQ) SpyM3_1160 SpyM3_1397
            SPS: SPs0208 SPs0465 SPs0702 SPs0860 SPs1106
            SPH: MGAS10270_Spy0235 MGAS10270_Spy1097
            SPI: MGAS10750_Spy0230 MGAS10750_Spy1133
            SPJ: MGAS2096_Spy0253 MGAS2096_Spy1043
            SPK: MGAS9429_Spy0237 MGAS9429_Spy1087
            SPF: SpyM50214(glnQ2) SpyM50818
            SPA: M6_Spy0267 M6_Spy1046(glnQ) M6_Spy1258 M6_Spy1408
            SPB: M28_Spy0229 M28_Spy0955 M28_Spy1058(glnQ.2) M28_Spy1176(artP)
                 M28_Spy1403
            SPN: SP_0452 SP_0709 SP_0824 SP_1242 SP_1460 SP_1501
            SPR: spr0408(glnQ) spr0535 spr0536 spr0728(glnQ) spr1121(glnQ)
                 spr1314(ABC-NDB) spr1354(glnQ)
            SPD: SPD_0411 SPD_0720 SPD_1329
            SAG: SAG0135 SAG0292 SAG0492 SAG0948 SAG1467
            SAN: gbs0131 gbs0282 gbs0538 gbs0936 gbs1534(glnQ)
            SAK: SAK_0193 SAK_0364 SAK_0593 SAK_1043 SAK_1498
            SMU: SMU.1178c SMU.241c SMU.461 SMU.568 SMU.805c SMU.936
            STC: str0158 str0606 str0876 str1502(gnlQ) str1652
            STL: stu0158 stu0606 stu0876 stu1502(gnlQ) stu1652
            STE: STER_0213 STER_0652 STER_0906
            SSA: SSA_1360 SSA_1867 SSA_1962 SSA_2097
            SSU: SSU05_0496 SSU05_0551
            SSV: SSU98_0489 SSU98_0552 SSU98_1885
            LPL: lp_0803(glnQ1) lp_2110(glnQ3) lp_2313(glnQ4) lp_3211
            LJO: LJ0086 LJ0413 LJ0787 LJ1309
            LAC: LBA0111 LBA0135(glnQ) LBA1045 LBA1673(glnQ)
            LSA: LSA0859(ls859) LSA1056 LSA1496
            LSL: LSL_0582(glnQ) LSL_1062 LSL_1540 LSL_1625
            LDB: Ldb0168 Ldb0253 Ldb1298 Ldb2199
            LBU: LBUL_0144 LBUL_0216 LBUL_0262 LBUL_1213 LBUL_2020
            LBR: LVIS_0671 LVIS_1201
            LCA: LSEI_1261 LSEI_1345 LSEI_2838 LSEI_2848 LSEI_A11
            LGA: LGAS_0085 LGAS_0359 LGAS_0545
            LRE: Lreu_0726
            PPE: PEPE_1136 PEPE_1285
            EFA: EF0246 EF0760 EF0805 EF0892 EF1120
            OOE: OEOE_0750 OEOE_1427 OEOE_1666
            LME: LEUM_0629
            STH: STH1062 STH2621 STH491
            CAC: CAC0378(glnQ) CAC0879 CAC3327 CAC3618
            CPE: CPE0602 CPE1326 CPE2092
            CPF: CPF_0583
            CTC: CTC00560(glnQ)
            CNO: NT01CX_0934
            DSY: DSY0741 DSY1209 DSY3385 DSY4278 DSY4688
            DRM: Dred_2233
            SWO: Swol_1059
            TTE: TTE0514(glnQ)
            POY: PAM488(glnQ)
            AYW: AYWB_264(artP)
            MPA: MAP0051c(gluA)
            CGL: NCgl1276(cgl1330)
            CGB: cg1502
            CEF: CE1443
            CDI: DIP1142(atrC)
            CJK: jk0806
            NFA: nfa18910
            SCO: SCO2831(SCE20.05) SCO5258(2SC7G11.20c)
            SMA: SAV2984(aotP) SAV5227 SAV6281 SAV6402 SAV6546 SAV6548 SAV7209
            PAC: PPA0600
            TFU: Tfu_0306
            SEN: SACE_1746 SACE_3965 SACE_5842 SACE_6266 SACE_7284
            BLO: BL0076(gltL) BL1176
            BAD: BAD_0472 BAD_0578 BAD_1260(yckI)
            FNU: FN0801
            CTR: CT130(glnQ)
            CTA: CTA_0137(glnQ)
            CMU: TC0406
            CPN: CPn0191(glnQ)
            CPA: CP0576
            CPJ: CPj0191(glnQ)
            CPT: CpB0194
            CCA: CCA00545(glnQ)
            CAB: CAB531
            CFE: CF0463(glnQ)
            SYN: slr1735(glnQ)
            SYW: SYNW0843
            SYD: Syncc9605_1806
            SYE: Syncc9902_0850
            SYG: sync_1186
            PMA: Pro0673
            PMT: PMT0893
            PMN: PMN2A_0611
            PMI: PMT9312_1165
            PLT: Plut_0861
            DET: DET0417
            DEH: cbdb_A369
            DRA: DR_1648 DR_2153
            TTH: TTC0795
            TTJ: TTHA1159
            TMA: TM0591
            MMP: MMP0229
            MMA: MM_1941(glnQ)
            MST: Msp_0958
            MSI: Msm_0805
            AFU: AF0680(glnQ)
            HMA: rrnAC0379(glnQ2) rrnAC1747(glnQ1)
            NPH: NP1778A(abc04a)
            APE: APE_1891.1
            PAI: PAE2001
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.21
            ExPASy - ENZYME nomenclature database: 3.6.3.21
            ExplorEnz - The Enzyme Database: 3.6.3.21
            ERGO genome analysis and discovery system: 3.6.3.21
            BRENDA, the Enzyme Database: 3.6.3.21
///
ENTRY       EC 3.6.3.22                 Enzyme
NAME        nonpolar-amino-acid-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (nonpolar-amino-acid-transporting)
REACTION    ATP + H2O + nonpolar amino acidout = ADP + phosphate + nonpolar
            amino acidin [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            nonpolar amino acid [CPD:C06700]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            nonpolar amino acid [CPD:C06700]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. Comprises bacterial
            enzymes that import Leu, Ile and Val.
REFERENCE   1  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
  ORGANISM  bacteria
REFERENCE   2  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
  ORGANISM  bacteria
REFERENCE   3
  AUTHORS   Griffiths, J.K. and Sansom, C.E.
  TITLE     The Transporter Factsbook, Academic Press, San Diego, 1998.
GENES       REH: H16_A0286 H16_A0290 H16_A0388 H16_A1078 H16_A1079 H16_A1244
                 H16_A1245 H16_A1417 H16_A1418 H16_A1523 H16_A1524 H16_A1542
                 H16_A1543 H16_A1709 H16_A2255 H16_A2256 H16_A2622(livF1)
                 H16_A2623(livG1) H16_A3026(livF2) H16_A3027(livG2) H16_A3652
                 H16_A3661 H16_A3662 H16_B0074 H16_B0501 H16_B0502 H16_B0806
                 H16_B0807 H16_B2011(livG3) H16_B2012(livF3) H16_B2039
                 H16_B2040
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.22
            ExPASy - ENZYME nomenclature database: 3.6.3.22
            ExplorEnz - The Enzyme Database: 3.6.3.22
            ERGO genome analysis and discovery system: 3.6.3.22
            BRENDA, the Enzyme Database: 3.6.3.22
///
ENTRY       EC 3.6.3.23                 Enzyme
NAME        oligopeptide-transporting ATPase;
            oligopeptide permease
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (oligopeptide-importing)
REACTION    ATP + H2O + oligopeptideout = ADP + phosphate + oligopeptidein
            [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            oligopeptide [CPD:C00098]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            oligopeptide [CPD:C00098]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A bacterial enzyme
            that imports di- and oligopeptides.
REFERENCE   1  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   2  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   3
  AUTHORS   Griffiths, J.K. and Sansom, C.E.
  TITLE     The Transporter Factsbook, Academic Press, San Diego, 1998.
REFERENCE   4  [PMID:1738314]
  AUTHORS   Pearce SR, Mimmack ML, Gallagher MP, Gileadi U, Hyde SC, Higgins CF.
  TITLE     Membrane topology of the integral membrane components, OppB and
            OppC, of the oligopeptide permease of Salmonella typhimurium.
  JOURNAL   Mol. Microbiol. 6 (1992) 47-57.
  ORGANISM  Salmonella typhimurium
GENES       REH: H16_A1303 H16_A1304 H16_A1470 H16_A1471 H16_A2952 H16_A2953
                 H16_A3294 H16_A3295 H16_B0716(dppF3) H16_B0717(dppD3)
                 H16_B1124 H16_B1125
            AZO: azo0944(nasD)
            CKL: CKL_1049(oppA1) CKL_1050(oppB) CKL_1051(oppC) CKL_1052(oppD)
                 CKL_1053(oppF)
            RHA: RHA1_ro09044 RHA1_ro09045
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.23
            ExPASy - ENZYME nomenclature database: 3.6.3.23
            ExplorEnz - The Enzyme Database: 3.6.3.23
            ERGO genome analysis and discovery system: 3.6.3.23
            BRENDA, the Enzyme Database: 3.6.3.23
///
ENTRY       EC 3.6.3.24                 Enzyme
NAME        nickel-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (nickel-importing)
REACTION    ATP + H2O + Ni2+out = ADP + phosphate + Ni2+in [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            Ni2+ [CPD:C00291]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            Ni2+ [CPD:C00291]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A bacterial enzyme
            that imports Ni2+.
REFERENCE   1  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   2  [PMID:9294450]
  AUTHORS   Hendricks JK, Mobley HL.
  TITLE     Helicobacter pylori ABC transporter: effect of allelic exchange
            mutagenesis on urease activity.
  JOURNAL   J. Bacteriol. 179 (1997) 5892-902.
  ORGANISM  Helicobacter pylori
REFERENCE   3  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   4
  AUTHORS   Griffiths, J.K. and Sansom, C.E.
  TITLE     The Transporter Factsbook, Academic Press, San Diego, 1998.
GENES       TET: TTHERM_00024080
            ECW: EcE24377A_3958(nikA) EcE24377A_3959(nikB)
                 EcE24377A_3962(nikC) EcE24377A_3963(nikD) EcE24377A_3964(nikE)
            ECX: EcHS_A3675 EcHS_A3676 EcHS_A3677 EcHS_A3678 EcHS_A3679
            PRW: PsycPRwf_1527
            MMW: Mmwyl1_0113
            CFF: CFF8240_1657
            SMD: Smed_0330
            BOV: BOV_A0750(nikE) BOV_A0752(nikC) BOV_A0753(nikB)
            BRA: BRADO1093 BRADO1094(appB) BRADO1095(oppC) BRADO1096(oppD)
                 BRADO2619
            AMT: Amet_1131 Amet_2908 Amet_4722
            CSC: Csac_1028
            DEB: DehaBAV1_0942
STRUCTURES  PDB: 1ZLQ  2NOO  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.24
            ExPASy - ENZYME nomenclature database: 3.6.3.24
            ExplorEnz - The Enzyme Database: 3.6.3.24
            ERGO genome analysis and discovery system: 3.6.3.24
            BRENDA, the Enzyme Database: 3.6.3.24
///
ENTRY       EC 3.6.3.25                 Enzyme
NAME        sulfate-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (sulfate-importing)
REACTION    ATP + H2O + sulfateout = ADP + phosphate + sulfatein [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            sulfate [CPD:C00059]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            sulfate [CPD:C00059]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A bacterial enzyme
            that imports sulfate and thiosulfate anions.
REFERENCE   1  [PMID:7608089]
  AUTHORS   Sirko A, Zatyka M, Sadowy E, Hulanicka D.
  TITLE     Sulfate and thiosulfate transport in Escherichia coli K-12: evidence
            for a functional overlapping of sulfate- and thiosulfate-binding
            proteins.
  JOURNAL   J. Bacteriol. 177 (1995) 4134-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   3  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
PATHWAY     PATH: map02010  ABC transporters - General
ORTHOLOGY   KO: K02045  sulfate transport system ATP-binding protein
            KO: K06020  sulfate-transporting ATPase
GENES       TET: TTHERM_00323060 TTHERM_00414290 TTHERM_00862740
            ECO: b2422(cysA)
            ECJ: JW2415(cysA)
            ECE: Z3687(cysA)
            ECS: ECs3293
            ECC: c2956(cysA)
            ECI: UTI89_C2755(cysA)
            ECP: ECP_2445
            ECV: APECO1_4124(cysA)
            ECW: EcE24377A_2708(cysA)
            ECX: EcHS_A2558(cysA)
            STY: STY2678(cysA)
            STT: t0417(cysA)
            SPT: SPA0425(cysA)
            SEC: SC2440(cysA)
            STM: STM2441(cysA)
            YPE: YPO3012(cysA)
            YPK: y1469(cysA)
            YPM: YP_2636(cysA)
            YPA: YPA_2201
            YPN: YPN_1371
            YPS: YPTB2732(cysA)
            YPI: YpsIP31758_1302(cysA)
            SFX: S2623(cysA)
            SFV: SFV_2475(cysA)
            SSN: SSON_2511(cysA)
            SBO: SBO_2447(cysA)
            SDY: SDY_2618(cysA)
            ECA: ECA3296(cysA)
            PLU: plu1390(cysA)
            SGL: SG1706
            BFL: Bfl511(cysA)
            BPN: BPEN_528(cysA)
            MSU: MS1261(cysA)
            APL: APL_1848(cysA)
            XFA: XF1347
            XFT: PD0591(cysA)
            XCC: XCC0943(cysA)
            XCB: XC_3292
            XCV: XCV1050(cysA)
            XAC: XAC1020(cysA)
            XOO: XOO3686(cysA)
            XOM: XOO_3482(XOO3482)
            VCH: VC0541
            VVU: VV2_0688
            PAE: PA0280(cysA)
            PPU: PP_5168(cysA)
            PST: PSPTO_0311(cysA)
            PSB: Psyr_0081
            PSP: PSPPH_0086
            PFL: PFL_0195(cysA)
            PFO: Pfl_0197
            PEN: PSEEN1099(ttg2A) PSEEN5281(cysA)
            PAR: Psyc_1074(cysA)
            ACI: ACIAD2596(cysA)
            SON: SO_3602(cysA-1) SO_4655(cysA-2)
            SHN: Shewana3_3192
            MCA: MCA1181(cysA)
            AHA: AHA_0608(cysA) AHA_3987
            BCI: BCI_0079(cysA)
            NME: NMB0879
            NMA: NMA1097(cysA)
            NGO: NGO0445
            CVI: CV_1828(cysA)
            RSO: RSc1347(cysA)
            REU: Reut_A1968
            REH: H16_A2237(cysA)
            RME: Rmet_1378
            BMA: BMA1206(cysA)
            BMV: BMASAVP1_A1695(cysA)
            BML: BMA10299_A0351(cysA)
            BMN: BMA10247_0809(cysA)
            BXE: Bxe_A2467
            BUR: Bcep18194_A3217 Bcep18194_A3402 Bcep18194_A3512
                 Bcep18194_A3518 Bcep18194_A3604 Bcep18194_A4010
                 Bcep18194_A4074 Bcep18194_A4172 Bcep18194_A4316
                 Bcep18194_A4340 Bcep18194_A4490 Bcep18194_A4560
                 Bcep18194_A4561 Bcep18194_A4706 Bcep18194_A4734(nodI)
                 Bcep18194_A4742 Bcep18194_A4781 Bcep18194_A4846
                 Bcep18194_A4998 Bcep18194_A5049 Bcep18194_A5219
                 Bcep18194_A5368 Bcep18194_A5700 Bcep18194_A5724
                 Bcep18194_A5827 Bcep18194_A6120 Bcep18194_A6159
                 Bcep18194_A6226 Bcep18194_A6242 Bcep18194_A6267
                 Bcep18194_A6346 Bcep18194_A6389 Bcep18194_A6495
                 Bcep18194_B0311 Bcep18194_B0349 Bcep18194_B0497
                 Bcep18194_B0541 Bcep18194_B0624 Bcep18194_B0675
                 Bcep18194_B0676 Bcep18194_B0724 Bcep18194_B0972
                 Bcep18194_B1249 Bcep18194_B1250 Bcep18194_B1745
                 Bcep18194_B1759 Bcep18194_B1769 Bcep18194_B1838
                 Bcep18194_B2064 Bcep18194_B2170 Bcep18194_B2533
                 Bcep18194_B3069 Bcep18194_C6716 Bcep18194_C6938
                 Bcep18194_C7103 Bcep18194_C7429 Bcep18194_C7505
                 Bcep18194_C7553 Bcep18194_C7594 Bcep18194_C7649
                 Bcep18194_C7682
            BAM: Bamb_0421 Bamb_1500
            BPS: BPSL1836(cysA)
            BPM: BURPS1710b_2017(cysA) BURPS1710b_3595
            BPL: BURPS1106A_1864(cysA)
            BPD: BURPS668_1850(cysA)
            BTE: BTH_I2477
            BPE: BP0969(cysA)
            BPA: BPP1658(cysA)
            BBR: BB3450(cysA)
            RFR: Rfer_1759
            POL: Bpro_2379
            MPT: Mpe_A0126(cysA)
            HAR: HEAR0811 HEAR0838(cysA) HEAR1420 HEAR1436 HEAR1633
                 HEAR2223(lolD) HEAR2353 HEAR2358 HEAR2454(uup) HEAR2463(braF)
                 HEAR2591(rbbA) HEAR2680 HEAR3255(livG) HEAR3309 HEAR3338
            NEU: NE0576(cysA)
            NMU: Nmul_A0503
            EBA: ebA6208(cysA)
            AZO: azo1333(cysA)
            DAR: Daro_3690
            MFA: Mfla_0609
            CCV: CCV52592_0582 CCV52592_1357 CCV52592_1977
            CHA: CHAB381_0315
            ABU: Abu_2007 Abu_2296(cysA)
            GSU: GSU1349(cysA)
            GME: Gmet_1903
            MXA: MXAN_4818(cysA)
            PUB: SAR11_0495(yhbG)
            MLO: mlr1669
            SME: SMa2067 SMb21130
            ATU: Atu0823 Atu3501
            ATC: AGR_C_1506 AGR_L_2655
            RET: RHE_CH00739(dppDch1) RHE_CH02609 RHE_PE00256
            RLE: RL3029 pRL110371
            BME: BMEI1838
            BMF: BAB1_0107
            BMS: BR0110
            BMB: BruAb1_0107
            BJA: blr1485
            BRA: BRADO1073(cysA) BRADO1409 BRADO1928
            BBT: BBta_6692 BBta_6974(cysA)
            RPA: RPA0747(cysA)
            RPB: RPB_1048
            RPC: RPC_4007
            RPD: RPD_1159
            RPE: RPE_1771
            NWI: Nwi_0174 Nwi_0292 Nwi_0458 Nwi_2757
            CCR: CC_1598
            SIT: TM1040_3330
            RSP: RSP_3696(cysA)
            RRU: Rru_A0011 Rru_A0069 Rru_A0095 Rru_A0126 Rru_A0407 Rru_A0497
                 Rru_A0585 Rru_A0788 Rru_A0803 Rru_A0843 Rru_A0863 Rru_A0864
                 Rru_A1017 Rru_A1066 Rru_A1138 Rru_A1260 Rru_A1644 Rru_A1749
                 Rru_A1792 Rru_A1920 Rru_A1921 Rru_A2011 Rru_A2048 Rru_A2104
                 Rru_A2250 Rru_A2301 Rru_A2359 Rru_A2383 Rru_A2419 Rru_A2446
                 Rru_A2498 Rru_A2748 Rru_A2804 Rru_A2909 Rru_A3014 Rru_A3130
                 Rru_A3150 Rru_A3201 Rru_A3236 Rru_A3254 Rru_A3304 Rru_A3403
                 Rru_A3414 Rru_A3453 Rru_A3510 Rru_A3651 Rru_A3664 Rru_A3688
                 Rru_A3702 Rru_A3724 Rru_A3725
            MAG: amb2012
            BHA: BH3130(cysA)
            BCE: BC1094(cysA)
            BCA: BCE_1199
            BCL: ABC1229
            LWE: lwe1990 lwe2133 lwe2158 lwe2530
            LLM: llmg_0214(rgpD) llmg_1700(choQ) llmg_1932
            SSA: SSA_1579
            SGO: SGO_2099
            CKL: CKL_1800(cysA)
            DSY: DSY2955
            MTU: Rv2397c(cysA1)
            MTC: MT2468(cysA)
            MBO: Mb2419c(cysA1)
            MPA: MAP2210c(cysA)
            MAV: MAV_1785
            MSM: MSMEG_4520 MSMEG_4530(cysA) MSMEG_6521 MSMEG_6671
            NFA: nfa14070
            RHA: RHA1_ro01270(cysA) RHA1_ro04849(cydD)
            FAL: FRAAL0081 FRAAL0330 FRAAL0586(ssuB) FRAAL0794(braG) FRAAL1346
                 FRAAL1558 FRAAL2549 FRAAL2843(livG) FRAAL3359 FRAAL3828
                 FRAAL4355(cysA) FRAAL4365(ugpC) FRAAL4807 FRAAL4975
                 FRAAL5037(livG) FRAAL5379 FRAAL5527 FRAAL6466
            LIL: LA1158
            LIC: LIC12526(cysA)
            LBJ: LBJ_2146
            LBL: LBL_2140
            SYN: slr1455(cysA)
            SYC: syc2410_d(cysA)
            SYF: Synpcc7942_1680
            CYA: CYA_0470(cysA)
            CYB: CYB_0238(cysA)
            TEL: tlr1690(cysA)
            GVI: glr2071
            ANA: all0126(cysA)
            AVA: Ava_1433 Ava_1495 Ava_1638 Ava_3020 Ava_4038 Ava_4105
                 Ava_4151 Ava_B0163
            PMB: A9601_08671(potA)
            PMC: P9515_07781(potA)
            PMF: P9303_17671(potA)
            PMG: P9301_08641(potA)
            PME: NATL1_08431(potA)
            CCH: Cag_0251 Cag_0264 Cag_0337 Cag_0479 Cag_0716 Cag_0740
                 Cag_0850 Cag_0979 Cag_1079 Cag_1444 Cag_1705
            HWA: HQ1421A(cysA)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.25
            ExPASy - ENZYME nomenclature database: 3.6.3.25
            ExplorEnz - The Enzyme Database: 3.6.3.25
            ERGO genome analysis and discovery system: 3.6.3.25
            BRENDA, the Enzyme Database: 3.6.3.25
///
ENTRY       EC 3.6.3.26                 Enzyme
NAME        nitrate-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (nitrate-importing)
REACTION    ATP + H2O + nitrateout = ADP + phosphate + nitratein [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            nitrate [CPD:C00244]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            nitrate [CPD:C00244]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A bacterial enzyme
            that imports NO3-, NO2- and OCN-.
REFERENCE   1  [PMID:7767600]
  AUTHORS   Omata T.
  TITLE     Structure, function and regulation of the nitrate transport system
            of the cyanobacterium Synechococcus sp. PCC7942.
  JOURNAL   Plant. Cell. Physiol. 36 (1995) 207-13.
  ORGANISM  Synechococcus sp.
REFERENCE   2  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   3  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   4
  AUTHORS   Griffiths, J.K. and Sansom, C.E.
  TITLE     The Transporter Factsbook, Academic Press, San Diego, 1998.
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.26
            ExPASy - ENZYME nomenclature database: 3.6.3.26
            ExplorEnz - The Enzyme Database: 3.6.3.26
            ERGO genome analysis and discovery system: 3.6.3.26
            BRENDA, the Enzyme Database: 3.6.3.26
///
ENTRY       EC 3.6.3.27                 Enzyme
NAME        phosphate-transporting ATPase;
            ABC phosphate transporter
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (phosphate-importing)
REACTION    ATP + H2O + phosphateout = ADP + phosphate + phosphatein [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            phosphate [CPD:C00009]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A bacterial enzyme
            that imports phosphate anions.
REFERENCE   1  [PMID:1447208]
  AUTHORS   Webb DC, Rosenberg H, Cox GB.
  TITLE     Mutational analysis of the Escherichia coli phosphate-specific
            transport system, a member of the traffic ATPase (or ABC) family of
            membrane transporters. A role for proline residues in transmembrane
            helices.
  JOURNAL   J. Biol. Chem. 267 (1992) 24661-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   3  [PMID:8843165]
  AUTHORS   Braibant M, Lefevre P, de Wit L, Ooms J, Peirs P, Huygen K, Wattiez
            R, Content J.
  TITLE     Identification of a second Mycobacterium tuberculosis gene cluster
            encoding proteins of an ABC phosphate transporter.
  JOURNAL   FEBS. Lett. 394 (1996) 206-12.
  ORGANISM  Mycobacterium tuberculosis
REFERENCE   4  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   5
  AUTHORS   Griffiths, J.K. and Sansom, C.E.
  TITLE     The Transporter Factsbook, Academic Press, San Diego, 1998.
PATHWAY     PATH: map02010  ABC transporters - General
ORTHOLOGY   KO: K02036  phosphate transport system ATP-binding protein
            KO: K06021  phosphate-transporting ATPase
GENES       TET: TTHERM_00006240 TTHERM_00031830 TTHERM_00033910
                 TTHERM_00037430 TTHERM_00083790 TTHERM_00243670
                 TTHERM_00265150 TTHERM_00313120 TTHERM_00550890
                 TTHERM_00592990 TTHERM_00593010 TTHERM_00593020
                 TTHERM_00630580 TTHERM_00951710 TTHERM_00951770
                 TTHERM_00951800 TTHERM_01084320 TTHERM_01151440
                 TTHERM_01151450
            ECO: b3725(pstB)
            ECJ: JW3703(pstB)
            ECE: Z5216(pstB)
            ECS: ECs4661
            ECC: c4649(pstB)
            ECP: ECP_3924
            ECV: APECO1_2736(pstB)
            ECW: EcE24377A_4236(pstB)
            ECX: EcHS_A3940
            STY: STY3929(pstB)
            STT: t3669(pstB)
            SPT: SPA3695(pstB)
            SEC: SC3768(pstB)
            STM: STM3854(pstB)
            YPE: YPO2833(pstB) YPO4114(pstB)
            YPK: y1401(pstB) y4128(pstB)
            YPM: YP_2700(pstB1) YP_4021(pstB2)
            YPA: YPA_2270 YPA_4159
            YPN: YPN_1305 YPN_3971
            YPS: YPTB2799(pstB) YPTB3960(pstB)
            YPI: YpsIP31758_1230(pstB2) YpsIP31758_4168(pstB1)
            SFL: SF3730(pstB)
            SFX: S4042(pstB)
            SFV: SFV_3782(pstB)
            SSN: SSON_3909(pstB)
            SBO: SBO_3657(pstB)
            SDY: SDY_4025(pstB)
            ECA: ECA3161(pstB) ECA4474(pstB)
            PLU: plu0217(pstB)
            SGL: SG1734 SG2420
            HIT: NTHI1777(pstB)
            PMU: PM0433(pstB)
            APL: APL_1258(pstB)
            XFA: XF2144
            XFT: PD1205(pstB)
            XCC: XCC1524(pstB)
            XCB: XC_2711
            XCV: XCV1614(pstB)
            XAC: XAC1574(pstB)
            XOO: XOO2465(pstB)
            XOM: XOO_2337(XOO2337)
            VCH: VC0726 VCA0073
            VVU: VV1_0461 VV2_1559
            VVY: VV0730 VVA0372
            VPA: VP0576 VPA1458
            VFI: VF1613(pstB) VF1983(pstB)
            PPR: PBPRA0730 PBPRA1391
            PAE: PA5366(pstB)
            PAP: PSPA7_6145(pstB)
            PPU: PP_2659 PP_5326(pstB)
            PST: PSPTO_3266(pstB-1) PSPTO_5484(pstB-2)
            PSB: Psyr_3103 Psyr_5038
            PSP: PSPPH_3015(pstB1) PSPPH_5120(pstB2)
            PFL: PFL_6116
            PFO: Pfl_5612
            PEN: PSEEN5470(pstB)
            PAR: Psyc_1929(pstB)
            ACI: ACIAD1215(pstB)
            SON: SO_1725(pstB-1) SO_4289(pstB-2)
            SDN: Sden_2582
            SFR: Sfri_1359
            SHE: Shewmr4_2558
            SHM: Shewmr7_2625
            SHN: Shewana3_2732
            ILO: IL2106(pstB)
            CPS: CPS_3640(pstB)
            PHA: PSHAa0311(pstB)
            PAT: Patl_3315
            SDE: Sde_3752
            MCA: MCA1074(pstB)
            TCX: Tcr_0539
            NOC: Noc_0581 Noc_1836 Noc_2396 Noc_2489(sufC)
            AEH: Mlg_1137
            HCH: HCH_00753(pstB)
            ABO: ABO_2682(pstB)
            AHA: AHA_2811(pstB)
            DNO: DNO_1183(pstB)
            CVI: CV_0935(pstB)
            RSO: RSc1532(pstB)
            REU: Reut_A2164
            RME: Rmet_2182
            BMA: BMA0783(pstB)
            BXE: Bxe_A1269(pstB)
            BUR: Bcep18194_A3274 Bcep18194_A3507 Bcep18194_A4271
                 Bcep18194_A4446 Bcep18194_A4998 Bcep18194_A5071
                 Bcep18194_A5368 Bcep18194_A5649(msbA) Bcep18194_A5826
                 Bcep18194_A6041 Bcep18194_A6489 Bcep18194_B0118
                 Bcep18194_B0217 Bcep18194_B0655 Bcep18194_B0834
                 Bcep18194_B1531 Bcep18194_B1868 Bcep18194_B1962
                 Bcep18194_B2299 Bcep18194_B2532 Bcep18194_C6712
                 Bcep18194_C7412 Bcep18194_C7593 Bcep18194_C7674
            BCN: Bcen_0822
            BAM: Bamb_1180
            BPS: BPSL1362(pstB)
            BPM: BURPS1710b_1621(pstB)
            BPL: BURPS1106A_1518(pstB)
            BPD: BURPS668_1488(pstB)
            BTE: BTH_I2770(pstB)
            BPE: BP1068(pstB)
            BPA: BPP2076(pstB)
            BBR: BB1469(pstB)
            RFR: Rfer_0580
            POL: Bpro_2255
            MPT: Mpe_A1275
            HAR: HEAR0490(pstB2) HEAR1372(cydD) HEAR1929 HEAR2462(braG)
                 HEAR3211(ptxA)
            NEU: NE1001(pstB)
            NMU: Nmul_A1088
            EBA: ebA4830(pstB)
            AZO: azo1393(pstB)
            DAR: Daro_3565
            TBD: Tbd_1139
            MFA: Mfla_0792
            HPA: HPAG1_0580
            WSU: WS0945(pstB)
            TDN: Tmden_1887
            CJE: Cj0616(pstB)
            CJR: CJE0719(pstB)
            CJU: C8J_0578(pstB)
            CFF: CFF8240_0183(pstB)
            CHA: CHAB381_0405(pstB)
            ABU: Abu_0089(pstB)
            GSU: GSU1096(pstB)
            GME: Gmet_2704
            PCA: Pcar_0658 Pcar_0829
            DVU: DVU1084(pstB-1)
            DDE: Dde_2386
            LIP: LI1031(pstB)
            BBA: Bd1661(pstB)
            DPS: DP1229 DP1880(pstB)
            ADE: Adeh_4003
            MXA: MXAN_4791(pstB)
            SAT: SYN_00059
            SFU: Sfum_0701 Sfum_2890
            WOL: WD0371(pstB)
            WBM: Wbm0178
            AMA: AM235(pstS) AM872(pstB)
            APH: APH_0313(pstB)
            ERU: Erum5760(pstB)
            ERW: ERWE_CDS_06050(pstB)
            ERG: ERGA_CDS_05960(pstB)
            ECN: Ecaj_0578
            ECH: ECH_0444(pstB)
            NSE: NSE_0808
            PUB: SAR11_1176(pstB)
            MLO: mll3719
            SME: SMc02142(pstB)
            ATU: Atu0423(pstB)
            ATC: AGR_C_743(pstB)
            RET: RHE_CH00512(pstB) RHE_CH02873 RHE_CH04097
            RLE: RL0545 RL1685 RL3333 RL4711
            BME: BMEI1986
            BMF: BAB1_2144(pstB)
            BMS: BR2141(pstB)
            BMB: BruAb1_2116(pstB)
            BOV: BOV_2056(pstB)
            BJA: blr1094(pstB)
            BRA: BRADO1097(oppF) BRADO5446(sufC)
            BBT: BBta_4864(oppF) BBta_5930(sufC) BBta_6951(oppF)
            RPA: RPA4777(pstB)
            RPB: RPB_0779
            RPC: RPC_4920
            RPD: RPD_0891
            RPE: RPE_4888
            NWI: Nwi_0509 Nwi_0611 Nwi_0669
            BHE: BH02460(pstB)
            BQU: BQ02330(pstB)
            BBK: BARBAKC583_1225(pstB)
            CCR: CC_0292
            SIL: SPO1951(pstB)
            SIT: TM1040_1259
            RSP: RSP_2601(pstB)
            JAN: Jann_2292
            RDE: RD1_1237 RD1_2646(pstB)
            MMR: Mmar10_0481
            HNE: HNE_2030(pstB)
            ZMO: ZMO1050(pstB)
            NAR: Saro_2279
            SAL: Sala_0823
            ELI: ELI_05410
            GOX: GOX0704(pstB)
            RRU: Rru_A0601 Rru_A0802 Rru_A0844 Rru_A0881 Rru_A0882 Rru_A1120
                 Rru_A1291 Rru_A1298 Rru_A1331 Rru_A1527 Rru_A1748 Rru_A2011
                 Rru_A2274 Rru_A2339 Rru_A2633 Rru_A3169 Rru_A3305 Rru_A3413
            MAG: amb1107 amb1372 amb4474
            MGM: Mmc1_1541
            BSU: BG11378(pstBA) BG11379(pstBB)
            BHA: BH2991
            BAN: BA4493(pstB)
            BAR: GBAA4493(pstB)
            BAA: BA_4940
            BAT: BAS4171
            BCE: BC4266(pstB)
            BCA: BCE_4349(pstB)
            BCZ: BCZK4019(pstB)
            BTK: BT9727_4009(pstB)
            BTL: BALH_3862(pstB)
            BLI: BL03714(pstBA) BL03715(pstBB)
            BLD: BLi02672(pstBB) BLi02673(pstBA)
            BCL: ABC2587(pstBB) ABC2588(pstBA)
            BAY: RBAM_023250
            BPU: BPUM_2223 BPUM_2224
            OIH: OB3133
            GKA: GK2454
            SAU: SA1218(pstB)
            SAV: SAV1386(pstB)
            SAM: MW1274(pstB)
            SAR: SAR1399
            SAS: SAS1327
            SAC: SACOL1421
            SAB: SAB1242c
            SAA: SAUSA300_1280(pstB)
            SAO: SAOUHSC_01385
            SEP: SE1067
            SER: SERP0957
            SHA: SH1525(pstB)
            SSP: SSP1364
            LMO: lmo2495 lmo2496
            LMF: LMOf2365_2468 LMOf2365_2469
            LIN: lin2638 lin2639
            LWE: lwe2443 lwe2444
            LLA: L154481(pstA) L155408(pstB)
            LLC: LACR_1877 LACR_1878
            LLM: llmg_1896(pstA) llmg_1897(pstB)
            SPY: SPy_1241(pstB) SPy_1242(pstB2)
            SPZ: M5005_Spy_0951(pstB) M5005_Spy_0952(pstB2)
            SPM: spyM18_1190(pstB1) spyM18_1191(pstB2)
            SPG: SpyM3_0877(pstB) SpyM3_0878(pstB2)
            SPS: SPs1077 SPs1078
            SPH: MGAS10270_Spy1067(pstB2)
            SPI: MGAS10750_Spy1102(pstB2)
            SPJ: MGAS2096_Spy1012(pstB2)
            SPK: MGAS9429_Spy1056(pstB2)
            SPF: SpyM50846(pstB2)
            SPA: M6_Spy0941 M6_Spy0942
            SPB: M28_Spy0924(pstB) M28_Spy0925(pstB2)
            SPN: SP_1396 SP_1397 SP_2087
            SPR: spr1253(pstB) spr1254(pstB) spr1898(pstB)
            SPD: SPD_1229 SPD_1913(pstB)
            SAG: SAG0988 SAG0989 SAG1963
            SAN: gbs1023 gbs1024 gbs1950
            SAK: SAK_1083 SAK_1084(pstB) SAK_1924(pstB)
            SMU: SMU.1134c SMU.1135(pstB)
            STC: str1004(pstB1) str1005(pstB2)
            STL: stu1004(pstB1) stu1005(pstB2)
            STE: STER_1009
            SSA: SSA_0944(pstB2) SSA_0945(pstB1)
            SSU: SSU05_1102
            SSV: SSU98_1111
            SGO: SGO_1058(pstB) SGO_1059(pstB)
            LPL: lp_0749(pstB) lp_0750(pstA)
            LJO: LJ0792 LJ0793
            LAC: LBA0364 LBA0365
            LSA: LSA0505(pstB1) LSA0506(pstB2)
            LSL: LSL_0403(pstB) LSL_0404(pstB)
            LDB: Ldb0959(pstB)
            LBU: LBUL_0870
            LBR: LVIS_0636 LVIS_0637 LVIS_1863
            LCA: LSEI_0939 LSEI_0940
            LGA: LGAS_0550 LGAS_0551
            LRE: Lreu_1565
            PPE: PEPE_0436 PEPE_0437
            EFA: EF1755 EF1756
            OOE: OEOE_0559 OEOE_0560
            LME: LEUM_0592 LEUM_0593
            STH: STH238 STH746 STH761
            CAC: CAC1708
            CPE: CPE0640
            CPF: CPF_0621(pstB)
            CTC: CTC01135(pstB)
            CDF: CD3261(phoT)
            CBO: CBO2522(phoT)
            CBA: CLB_2399(pstB)
            CBH: CLC_2381(pstB)
            CBF: CLI_2585(pstB)
            CKL: CKL_1351(pstB)
            CHY: CHY_2116(pstB)
            DSY: DSY4115
            TTE: TTE1628(pstB2)
            MTA: Moth_0114
            MGE: MG_410(pstB)
            MPN: MPN609(pstB)
            MPE: MYPE9350(pstB)
            MGA: MGA_0693(pstB)
            MMY: MSC_0487(pstB)
            MMO: MMOB0100(pstB)
            MCP: MCAP_0483(pstB)
            UUR: UU200(pstB)
            MFL: Mfl235
            MTU: Rv0820(phoT) Rv0933(pstB)
            MTC: MT0842(pstB-1) MT0960(pstB-2)
            MBO: Mb0843(phoT) Mb0958(pstBb)
            MLE: ML2189(phoT)
            MPA: MAP0654(phoT)
            MAV: MAV_0767(pstB)
            MSM: MSMEG_5779(pstB)
            CGL: NCgl2483(cgl2572)
            CGB: cg2843(pstB)
            CEF: CE2464
            CJK: jk0380(pstB)
            NFA: nfa6030(pstB)
            RHA: RHA1_ro04865(pstB)
            SCO: SCO4139(pstB) SCO6814(SC1A2.23c)
            SMA: SAV4075(pstB)
            TWH: TWT352(phoT)
            TWS: TW418
            LXX: Lxx18450(pstB)
            AAU: AAur_0198(pstB)
            PAC: PPA0338
            TFU: Tfu_2743
            FRA: Francci3_4262
            FAL: FRAAL2384 FRAAL4919 FRAAL4974 FRAAL6532(pstB)
            ACE: Acel_0094
            SEN: SACE_7096(pstB)
            BLO: BL0312(pstB)
            BAD: BAD_0281(pstB)
            RXY: Rxyl_0821
            RBA: RB7211(pstB)
            BBU: BB0218(pstB)
            BGA: BG0221(pstB)
            BAF: BAPKO_0226(pstB)
            SYN: sll0683(pstB) sll0684(pstB) slr1250(pstB)
            SYW: SYNW1272
            SYC: syc0107_c(pstB) syc1665_d(pstB)
            SYF: Synpcc7942_1450 Synpcc7942_2441
            SYD: Syncc9605_1399
            SYE: Syncc9902_1089
            SYG: sync_1392(pstB)
            CYA: CYA_1555(pstB-1) CYA_1735(pstB-2)
            CYB: CYB_1074(pstB-1) CYB_1912(pstB-2)
            TEL: tlr2167
            GVI: glr0011 glr0448
            ANA: all0907 all0908 all4572
            AVA: Ava_0048 Ava_0425(sufC) Ava_1188 Ava_1902 Ava_2398 Ava_2480
                 Ava_4147 Ava_4512 Ava_4513 Ava_4995
            PMA: Pro0596(pstB)
            PMM: PMM0725
            PMT: PMT0700
            PMN: PMN2A_0309
            PMI: PMT9312_0729
            PMB: A9601_04891(salX) A9601_07771(pstB) A9601_08111
            PMC: P9515_04961(salX) P9515_08341 P9515_08641(pstB)
                 P9515_12291(glnQ)
            PMF: P9303_06281(salX) P9303_11301(phnC) P9303_12101(glnQ)
                 P9303_15211(pstB) P9303_16611
            PMG: P9301_04581(salX) P9301_07771(pstB) P9301_08101
            PMH: P9215_08121
            PME: NATL1_04881(salX) NATL1_07861 NATL1_09821(pstB)
                 NATL1_14241(glnQ)
            TER: Tery_3540
            BTH: BT_1321
            BFR: BF2754
            BFS: BF2769(pstB)
            SRU: SRU_2296(pstB)
            CHU: CHU_3821
            FPS: FP0364(pstB)
            CTE: CT0899(pstB)
            CCH: Cag_0453 Cag_0498 Cag_0717 Cag_0849 Cag_0869 Cag_1327
                 Cag_1883
            PLT: Plut_1242
            DET: DET0141(pstB)
            DEH: cbdb_A165(pstB)
            DRA: DR_A0160
            DGE: Dgeo_0652
            TTH: TTC1723(pstB)
            TTJ: TTHA0262
            AAE: aq_1055(pstB)
            TMA: TM1261
            MJA: MJ1012(pstB)
            MMP: MMP1098(pstB)
            MAC: MA0890(pstB)
            MBA: Mbar_A1781
            MMA: MM_2009(pstB)
            MBU: Mbur_0749
            MHU: Mhun_2983
            MTH: MTH1731
            MST: Msp_0340(pstB) Msp_0343(pstS)
            MSI: Msm_0565
            MKA: MK1687(pstB)
            AFU: AF1359(pstB)
            HAL: VNG0452G(pstB2) VNG2482G(pstB1)
            HMA: rrnAC1505(pstB1) rrnAC2146(pstB2)
            HWA: HQ1468A(pstB)
            NPH: NP1984A(abc14a) NP6098A(abc15a)
            PAB: PAB0700(pstB)
            PFU: PF1008
            TKO: TK1868
            RCI: RCIX2754(pstB)
            APE: APE_0050(pstB)
            HBU: Hbut_0637
            SSO: SSO0488
            PAI: PAE1393
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.27
            ExPASy - ENZYME nomenclature database: 3.6.3.27
            ExplorEnz - The Enzyme Database: 3.6.3.27
            ERGO genome analysis and discovery system: 3.6.3.27
            BRENDA, the Enzyme Database: 3.6.3.27
///
ENTRY       EC 3.6.3.28                 Enzyme
NAME        phosphonate-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (phosphonate-transporting)
REACTION    ATP + H2O + phosphonateout = ADP + phosphate + phosphonatein
            [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            phosphonate [CPD:C06701]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            phosphonate [CPD:C06701]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A bacterial enzyme
            that imports phosphonate and organophosphate anions.
REFERENCE   1  [PMID:1335942]
  AUTHORS   Wanner BL, Metcalf WW.
  TITLE     Molecular genetic studies of a 10.9-kb operon in Escherichia coli
            for phosphonate uptake and biodegradation.
  JOURNAL   FEMS. Microbiol. Lett. 79 (1992) 133-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   3  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   4
  AUTHORS   Griffiths, J.K. and Sansom, C.E.
  TITLE     The Transporter Factsbook, Academic Press, San Diego, 1998.
GENES       ECW: EcE24377A_4659(phnC)
            ECX: EcHS_A4346
            YPI: YpsIP31758_2799(phnC)
            PAP: PSPA7_1745(phnC)
            PEN: PSEEN0993
            AHA: AHA_4214(phnC)
            REH: H16_B1868(ssuB2)
            BMV: BMASAVP1_A0323(phnC) BMASAVP1_A0326(phnE)
            BML: BMA10299_A1184(phnC) BMA10299_A1187(phnE)
            BMN: BMA10247_2593(phnC) BMA10247_2596(phnE)
            BPL: BURPS1106A_3338(phnC)
            BPD: BURPS668_3304(phnC)
            HAR: HEAR0826
            BRA: BRADO5366(phnC)
            BBT: BBta_1260 BBta_3436 BBta_5858(phnC) BBta_6355(phnC)
            RDE: RD1_1056(phnC) RD1_2403(phnC)
            BTL: BALH_3323(phnC)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.28
            ExPASy - ENZYME nomenclature database: 3.6.3.28
            ExplorEnz - The Enzyme Database: 3.6.3.28
            ERGO genome analysis and discovery system: 3.6.3.28
            BRENDA, the Enzyme Database: 3.6.3.28
///
ENTRY       EC 3.6.3.29                 Enzyme
NAME        molybdate-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (molybdate-importing)
REACTION    ATP + H2O + molybdateout = ADP + phosphate + molybdatein [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            molybdate [CPD:C06232]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            molybdate [CPD:C06232]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A bacterial enzyme
            that imports molybdate anions.
REFERENCE   1  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   2  [PMID:9325422]
  AUTHORS   Grunden AM, Shanmugam KT.
  TITLE     Molybdate transport and regulation in bacteria.
  JOURNAL   Arch. Microbiol. 168 (1997) 345-54.
  ORGANISM  Escherichia coli [GN:eco], Haemophilus influenzae, Azotobacter
            vinelandii, Rhodobacter capsulatus
REFERENCE   3  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   4
  AUTHORS   Griffiths, J.K. and Sansom, C.E.
  TITLE     The Transporter Factsbook, Academic Press, San Diego, 1998.
PATHWAY     PATH: map02010  ABC transporters - General
ORTHOLOGY   KO: K02017  molybdate transport system ATP-binding protein
            KO: K06022  molybdate-transporting ATPase
GENES       TET: TTHERM_00031790 TTHERM_00031820 TTHERM_00032880
                 TTHERM_00032890 TTHERM_00033900 TTHERM_00033910
                 TTHERM_00035440 TTHERM_00418430 TTHERM_00624590
                 TTHERM_00850570 TTHERM_00862740 TTHERM_01002630
                 TTHERM_01002640 TTHERM_01128600
            ECO: b0765(modC)
            ECJ: JW0748(modC)
            ECE: Z0935(modC)
            ECS: ECs0793
            ECC: c0842(modC)
            ECI: UTI89_C0763(modC)
            ECP: ECP_0777
            ECV: APECO1_1324(modC)
            ECW: EcE24377A_0792(modC)
            ECX: EcHS_A0819
            STY: STY0816(modC)
            STT: t2104(modC)
            SPT: SPA1969(modC)
            SEC: SC0781(modC)
            STM: STM0783(modC)
            YPE: YPO1147(modC)
            YPK: y3035(modC)
            YPM: YP_1013(modC)
            YPA: YPA_1054
            YPN: YPN_2854
            YPS: YPTB1173(modF) YPTB1178(modC)
            YPI: YpsIP31758_2848(modC)
            SFL: SF0539(modC)
            SFX: S0547(modC)
            SFV: SFV_0575(modC)
            SSN: SSON_0717(modC)
            SBO: SBO_0620(modC)
            SDY: SDY_0712(modC)
            ECA: ECA1395(modC)
            PLU: plu1478(modC)
            HIN: HI1474(sfuC) HI1691(modC)
            HIT: NTHI1998(modC)
            HIP: CGSHiEE_03590(modC)
            HIQ: CGSHiGG_02195(modC)
            HDU: HD1826(modC)
            PMU: PM0742(modC) PM1110
            MSU: MS1340(cysA)
            APL: APL_0260(modC)
            XCC: XCC3202(modC)
            XCB: XC_0912
            XCV: XCV3477(modC)
            XAC: XAC3360(modC)
            XOO: XOO1193(modC)
            XOM: XOO_1088(XOO1088)
            VCH: VCA0724
            VVU: VV2_0327
            VVY: VVA0821
            VPA: VPA0929
            VFI: VFA0292(modC)
            PPR: PBPRB1347
            PAE: PA1861(modC)
            PAU: PA14_40420(modC)
            PAP: PSPA7_3429(modC)
            PPU: PP_3830(modC)
            PST: PSPTO_2975(modC)
            PSB: Psyr_2758
            PSP: PSPPH_2403(modC)
            PFL: PFL_3414(cysA)
            PFO: Pfl_2943
            PEN: PSEEN2284(modC)
            ACI: ACIAD1899(modC)
            SON: SO_3865(modC) SO_4446
            SHE: Shewmr4_3197
            SHM: Shewmr7_0767
            SHN: Shewana3_0280 Shewana3_0741
            CPS: CPS_4641(modC)
            SDE: Sde_2847
            PIN: Ping_2164
            MAQ: Maqu_3547
            MCA: MCA1380(modC) MCA2578 MCA2836
            TCX: Tcr_1925
            NOC: Noc_1687
            HHA: Hhal_0186
            HCH: HCH_02452(modC)
            CSA: Csal_2675
            ABO: ABO_1256(modC)
            AHA: AHA_1597(modC)
            RSO: RS05462(RSp1145)
            REU: Reut_A0632
            RME: Rmet_0569
            BMA: BMAA0297(modC)
            BXE: Bxe_B2850
            BUR: Bcep18194_A4011 Bcep18194_A5932 Bcep18194_B0654
                 Bcep18194_B1962 Bcep18194_B2238
            BAM: Bamb_3226
            BPS: BPSS1788
            BPM: BURPS1710b_A0869(modC)
            BTE: BTH_II0591
            BPE: BP3093(modD)
            BPA: BPP0737(modD)
            BBR: BB0823(modD)
            RFR: Rfer_2860
            PNA: Pnap_2041
            AAV: Aave_2026
            AJS: Ajs_3126
            VEI: Veis_2886
            MPT: Mpe_A3715(modC)
            HAR: HEAR3437(modC)
            EBA: ebA2719(modC)
            AZO: azo3837(modC1) azo3842(modC2)
            DAR: Daro_2784
            TBD: Tbd_1285
            HPY: HP0475(modD)
            HPJ: jhp0427(modC)
            HPA: HPAG1_0452
            HHE: HH0657(modC)
            WSU: WS1803(modC)
            TDN: Tmden_0926
            CJE: Cj0300c(modC)
            CJR: CJE0345(modC)
            CJJ: CJJ81176_0322(modC)
            CJU: C8J_0277(modC)
            CFF: CFF8240_0360
            CCV: CCV52592_0583
            ABU: Abu_0009(modD)
            GSU: GSU2960(modC)
            GME: Gmet_0514
            PCA: Pcar_0777 Pcar_2109(modC) Pcar_2784
            DVU: DVU0180(modC)
            DDE: Dde_3520
            DPS: DP0345(modF) DP0455(modC) DP0466 DP1352
            MXA: MXAN_6643(modC)
            SFU: Sfum_3696
            MLO: mll1463(modC)
            MES: Meso_2720
            SME: SMc03198(modC)
            ATU: Atu2563(modC)
            ATC: AGR_C_4645(modC)
            RET: RHE_CH04031 RHE_CH04073(modC) RHE_PB00012
            RLE: RL1310 RL4609 RL4687 pRL90063
            BME: BMEII0003
            BMF: BAB2_0089
            BMS: BRA0090(modC)
            BMB: BruAb2_0090(modC)
            BJA: bll1780 blr6953(modC) blr8162(modC)
            BRA: BRADO1765(modC)
            BBT: BBta_2078(modC)
            RPA: RPA4715(modC)
            RPB: RPB_0859 RPB_1442
            RPC: RPC_0708
            RPD: RPD_0965
            RPE: RPE_0762
            NWI: Nwi_0292 Nwi_0338
            SIL: SPO0697(modC)
            SIT: TM1040_3662
            RSP: RSP_3869(modC)
            JAN: Jann_2468
            RDE: RD1_2915(modC) RD1_3149
            PDE: Pden_2667
            NAR: Saro_0214
            SAL: Sala_0552
            GBE: GbCGDNIH1_2124
            RRU: Rru_A0047 Rru_A0589 Rru_A0702 Rru_A0878 Rru_A1013 Rru_A1752
                 Rru_A2170 Rru_A2894
            MAG: amb3403
            MGM: Mmc1_1183
            SUS: Acid_5434
            SAU: SA2072(modC)
            SAV: SAV2277(modC)
            SAM: MW2195(modC)
            SAR: SAR2361(modC)
            SAS: SAS2167
            SAC: SACOL2270(modC)
            SAB: SAB2149c(modC)
            SAA: SAUSA300_2228(modC)
            SAO: SAOUHSC_02546
            SEP: SE1850
            SER: SERP1859(modC)
            SHA: SH0775(modC)
            SSP: SSP0634
            LMO: lmo1039
            LMF: LMOf2365_1060(modC)
            LIN: lin1031
            LWE: lwe1016
            EFA: EF1399
            STH: STH998
            DSY: DSY1140 DSY3396
            MTU: Rv1859(modC)
            MTC: MT1907
            MBO: Mb1890(modC)
            MBB: BCG_1895(modC)
            MPA: MAP1568(modC)
            MAV: MAV_2860
            MSM: MSMEG_2014
            MUL: MUL_3018(modC)
            MVA: Mvan_2536
            MMC: Mmcs_2797
            MKM: Mkms_2841
            CDI: DIP0495
            CJK: jk1593(molC)
            NFA: nfa43300
            RHA: RHA1_ro03636(modC)
            SCO: SCO3706(SCH35.18c)
            SMA: SAV1721
            ART: Arth_3746
            AAU: AAur_3533
            PAC: PPA0505
            TFU: Tfu_0326
            FRA: Francci3_3986
            SEN: SACE_0573
            SYN: sll0739(modBC)
            CYA: CYA_1846(modB)
            CYB: CYB_0398(modB)
            ANA: alr2433
            AVA: Ava_0243 Ava_B0237
            CTE: CT0450(modC) CT0668
            CCH: Cag_0415
            CPH: Cpha266_0438
            PLT: Plut_1710 Plut_1712
            DET: DET1159
            MMP: MMP0207(modC) MMP1649(modC)
            MAC: MA0323(modC) MA1235(modC) MA2282(modC) MA3903
            MBA: Mbar_A1305 Mbar_A1556
            MMA: MM_0728 MM_1578
            MBU: Mbur_1551
            MTH: MTH1469 MTH920
            MKA: MK1523
            AFU: AF1021
            TKO: TK0719
            RCI: RCIX1625(modC)
            PAI: PAE0063
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.29
            ExPASy - ENZYME nomenclature database: 3.6.3.29
            ExplorEnz - The Enzyme Database: 3.6.3.29
            ERGO genome analysis and discovery system: 3.6.3.29
            BRENDA, the Enzyme Database: 3.6.3.29
///
ENTRY       EC 3.6.3.30                 Enzyme
NAME        Fe3+-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (ferric-ion-transporting)
REACTION    ATP + H2O + Fe3+out = ADP + phosphate + Fe3+in [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            Fe3+ [CPD:C14819]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            Fe3+ [CPD:C14819]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A bacterial enzyme
            that imports ferric cations.
REFERENCE   1  [PMID:1531225]
  AUTHORS   Angerer A, Klupp B, Braun V.
  TITLE     Iron transport systems of Serratia marcescens.
  JOURNAL   J. Bacteriol. 174 (1992) 1378-87.
  ORGANISM  Serratia marcescens
REFERENCE   2  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   3  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   4  [PMID:9573125]
  AUTHORS   Khun HH, Kirby SD, Lee BC.
  TITLE     A Neisseria meningitidis fbpABC mutant is incapable of using nonheme
            iron for growth.
  JOURNAL   Infect. Immun. 66 (1998) 2330-6.
  ORGANISM  Neisseria meningitidis
PATHWAY     PATH: map02010  ABC transporters - General
ORTHOLOGY   KO: K02010  iron(III) transport system ATP-binding protein
GENES       TET: TTHERM_00919550 TTHERM_01014620 TTHERM_01151440
                 TTHERM_01358410
            ECO: b0262(afuC)
            ECJ: JW0254(afuC)
            ECE: Z0458(afuC)
            ECS: ECs0413
            YPE: YPO2960(sfuC)
            YPK: y1524(yfuC)
            YPM: YP_2586(yfuC)
            YPA: YPA_2150
            YPN: YPN_1421
            YPS: YPTB2016 YPTB2684(sfuC)
            YPI: YpsIP31758_1348(fbpC)
            ECA: ECA1468 ECA1492(afuC) ECA3139(sfuC) ECA3330
            PLU: plu0810(afuC)
            HIN: HI0099(hitC) HI0126(afuC)
            HIT: NTHI0180(hitC)
            HIQ: CGSHiGG_03235(fbpC)
            HSO: HS_0639(afuC) HS_0781(fbpC)
            PMU: PM0049(fbpC) PM0957(afuC) PM1456
            MSU: MS1587(malK)
            APL: APL_1448(afuC)
            VCH: VC0610(fbpC) VCA0602 VCA0687
            VVU: VV1_1663 VV2_1669
            VVY: VV2744 VVA0478
            VPA: VP2489 VPA0238
            VFI: VF2149
            PPR: PBPRA3182 PBPRB0373
            PAE: PA3538
            PPU: PP_1078 PP_5137
            PST: PSPTO_4165
            PSB: Psyr_3902
            PSP: PSPPH_3896
            PFL: PFL_3040(fbpC) PFL_4864 PFL_5890
            PFO: Pfl_2839 Pfl_4528 Pfl_5369
            PEN: PSEEN0267 PSEEN1200
            PAR: Psyc_1545
            SON: SO_0742
            SHN: Shewana3_3515
            ILO: IL1061(fbpC)
            CPS: CPS_1014
            PHA: PSHAa0822(ccmA) PSHAa2661(fbpC)
            PAT: Patl_1598
            NOC: Noc_2142
            HCH: HCH_01761 HCH_03087
            ABO: ABO_0717
            AHA: AHA_1935
            NMA: NMA0842(fbpC)
            NGO: NGO0215(fbpC)
            CVI: CV_1856 CV_1910
            RSO: RSc2939(RS00150)
            REU: Reut_B5873
            BMA: BMA1779 BMAA1130
            BXE: Bxe_B1837
            BUR: Bcep18194_A3948 Bcep18194_A5068 Bcep18194_A5345
                 Bcep18194_A6388 Bcep18194_B0119
            BAM: Bamb_1091
            BPS: BPSL1276 BPSS0702
            BPM: BURPS1710b_1509 BURPS1710b_A1901(phnT) BURPS1710b_A2274(potA)
            BTE: BTH_I2858 BTH_II1727
            BPE: BP1457 BP2277 BP2551
            BPA: BPP2058 BPP2451 BPP2628 BPP2982
            BBR: BB1043 BB1451 BB1899 BB2071 BB2948 BB4776
            RFR: Rfer_1595
            POL: Bpro_1148 Bpro_3218 Bpro_4695
            MPT: Mpe_A1085
            HAR: HEAR1319
            NEU: NE1031
            NMU: Nmul_A0730
            EBA: ebA2111 ebA4892
            AZO: azo2207(fbpC1) azo3826(fbpC2)
            DAR: Daro_1197
            TBD: Tbd_0988
            CJE: Cj0173c
            CJR: CJE0166
            CJU: C8J_0167
            CFF: CFF8240_0018
            PCA: Pcar_0895
            DPS: DP1394(potG)
            SFU: Sfum_2898
            WBM: Wbm0677
            APH: APH_0986
            ERU: Erum2550
            ERW: ERWE_CDS_02590(potA)
            ERG: ERGA_CDS_02550(potA)
            ECN: Ecaj_0243
            ECH: ECH_0845
            NSE: NSE_0480
            PUB: SAR11_1236(sfuA)
            MLO: mlr3498
            SME: SMb20156 SMb20363 SMb21541 SMc02068
            ATU: Atu0406(fbpA1) Atu4578 Atu4786(afuC)
            ATC: AGR_C_714 AGR_L_193 AGR_L_589
            RET: RHE_CH02124(afuC1) RHE_CH04058(sfuC)
            RLE: RL3192 RL4582(fbpC)
            BME: BMEII0567 BMEII0583 BMEII1123
            BMF: BAB2_0521 BAB2_0538
            BMS: BRA0701 BRA0718
            BMB: BruAb2_0110 BruAb2_0512 BruAb2_0529
            SIL: SPO2689
            SIT: TM1040_1801
            RSP: RSP_2539
            RDE: RD1_1061(fbpC) RD1_3260 RD1_4031
            RRU: Rru_A0767 Rru_A0982 Rru_A1497 Rru_A2273 Rru_A2360 Rru_A3169
            BHA: BH0512
            BAN: BA1734
            BAR: GBAA1734
            BAA: BA_1861 BA_1862 BA_1863 BA_2247
            BAT: BAS1236 BAS1237 BAS1610
            BCE: BC1324(phnT) BC1684
            BCA: BCE_1437 BCE_1811
            BCZ: BCZK1215 BCZK1562
            BTK: BT9727_1213 BT9727_1571
            BCL: ABC3262 ABC3649
            OIH: OB2723
            SPN: SP_0242 SP_1825
            SPR: spr0222(ABC-NBD) spr1644(ABC-NBD)
            LPL: lp_1750
            CPE: CPE0440
            CTC: CTC00276(sfuC) CTC01702
            MSM: MSMEG_3633
            CGL: NCgl0411(cgl0426)
            CGB: cg0506
            CEF: CE0446
            RHA: RHA1_ro04765 RHA1_ro07027(sfuC1) RHA1_ro07251(fepC)
                 RHA1_ro08545(sfuC2)
            AAU: AAur_0751(sufC)
            FRA: Francci3_1590
            FAL: FRAAL1420 FRAAL2622(livF) FRAAL2623 FRAAL2819(oppD)
                 FRAAL3205(ugpC) FRAAL3360(livF) FRAAL4165 FRAAL4835
                 FRAAL4836(oppD) FRAAL5387 FRAAL5769 FRAAL6832(potG)
            SEN: SACE_0413(fepC) SACE_5044
            FNU: FN0376(sfuC)
            TDE: TDE0182 TDE0375
            SYN: sll0240 sll1878(futC)
            SYW: SYNW1544(futC)
            SYC: syc0149_d
            SYF: Synpcc7942_1406
            SYD: Syncc9605_0670
            CYA: CYA_2794
            CYB: CYB_0190
            TEL: tll1492
            GVI: gll1012
            ANA: alr1384
            AVA: Ava_B0212 Ava_B0213 Ava_B0223 Ava_C0015
            PMA: Pro0881(potA)
            PMM: PMM0803(futC)
            PMT: PMT0501(futC)
            PMN: PMN2A_0211
            PMI: PMT9312_0811
            PMB: A9601_03131 A9601_08111 A9601_08671(potA)
            PMC: P9515_03231 P9515_07781(potA) P9515_08341 P9515_12291(glnQ)
            PMF: P9303_03901(malK) P9303_11301(phnC) P9303_12101(glnQ)
                 P9303_15311 P9303_16611 P9303_17671(potA)
            PMG: P9301_03141 P9301_08101 P9301_08641(potA)
            PME: NATL1_03701 NATL1_07861 NATL1_08431(potA) NATL1_14241(glnQ)
            SRU: SRU_2398
            CCH: Cag_0334 Cag_1482
            TTH: TTC1266(sfuC)
            TTJ: TTHA1630
            HAL: VNG0921G(potA1)
            HMA: rrnAC0908(potA4)
            HWA: HQ2543A(sfuC)
            NPH: NP3648A(abc24a)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.30
            ExPASy - ENZYME nomenclature database: 3.6.3.30
            ExplorEnz - The Enzyme Database: 3.6.3.30
            ERGO genome analysis and discovery system: 3.6.3.30
            BRENDA, the Enzyme Database: 3.6.3.30
///
ENTRY       EC 3.6.3.31                 Enzyme
NAME        polyamine-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (polyamine-importing)
REACTION    ATP + H2O + polyamineout = ADP + phosphate + polyaminein [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            polyamine [CPD:C06702]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            polyamine [CPD:C06702]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A bacterial enzyme
            that imports putrescine and spermidine.
REFERENCE   1  [PMID:8366082]
  AUTHORS   Kashiwagi K, Miyamoto S, Nukui E, Kobayashi H, Igarashi K.
  TITLE     Functions of potA and potD proteins in spermidine-preferential
            uptake system in Escherichia coli.
  JOURNAL   J. Biol. Chem. 268 (1993) 19358-63.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   3  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
PATHWAY     PATH: map02010  ABC transporters - General
ORTHOLOGY   KO: K02052  spermidine/putrescine transport system ATP-binding
                        protein
GENES       TET: TTHERM_00006240 TTHERM_00024080 TTHERM_00035280
                 TTHERM_00035300 TTHERM_00035360 TTHERM_00035380
                 TTHERM_00047720 TTHERM_00243670 TTHERM_00265150
                 TTHERM_00313120 TTHERM_00323060 TTHERM_00323080
                 TTHERM_00414290 TTHERM_00532790 TTHERM_00574250
                 TTHERM_00594090 TTHERM_00630580 TTHERM_00693290
                 TTHERM_00693300 TTHERM_00694300 TTHERM_00694310
                 TTHERM_00785880 TTHERM_00898300 TTHERM_00919550
                 TTHERM_01151450 TTHERM_01227870 TTHERM_01358410
                 TTHERM_01417320
            ECO: b0855(potG) b1126(potA)
            ECJ: JW1112(potA) JW5818(potG)
            ECE: Z1082(potG) Z1831(potA)
            ECS: ECs0935 ECs1571
            ECC: c0988(potG) c1477(potA)
            ECI: UTI89_C0858(potG) UTI89_C1254(potA)
            ECP: ECP_0869 ECP_1120
            ECV: APECO1_1238(potG) APECO1_208(potA) APECO1_583(ydcT)
            ECW: EcE24377A_1289(potA)
            ECX: EcHS_A1246
            STY: STY0467(phnT) STY0911(potG) STY1266(potA)
            STT: t1694(potA) t2018(potG) t2435(phnT)
            SPT: SPA1624(potA) SPA1884(potG) SPA2295(phnT)
            SEC: SC0469(phnT) SC0871(potG) SC1177(potA)
            STM: STM0428(phnT) STM0878(potG) STM1226(potA)
            YPE: YPO1332(potG) YPO2846 YPO3048
            YPK: y1388 y1432(potA) y2849(potG)
            YPM: YP_1261(potG) YP_2670 YP_2713
            YPA: YPA_0622 YPA_2239 YPA_2285
            YPN: YPN_1292 YPN_1337 YPN_2648
            YPP: YPDSF_2364
            YPS: YPTB1362(potG) YPTB2770 YPTB2812
            YEN: YE1485(potG)
            SFL: SF0809(potG) SF1128(potA)
            SFX: S0851(potG) S1208(potA)
            SFV: SFV_1144(potA)
            SSN: SSON_0840(potG) SSON_1144(potA) SSON_1696
            SBO: SBO_0789(potG) SBO_1915(potA)
            SDY: SDY_0740(potG) SDY_1733 SDY_2026(potA)
            ECA: ECA2051 ECA2450(potA) ECA2676(potG)
            SGL: SG0926
            KPN: KPN_00886(potG)
            HIN: HI1347(potA)
            HIT: NTHI1820(potA)
            HDU: HD0572(potA)
            HSO: HS_1157(potA)
            PMU: PM0264(potA)
            MSU: MS0812(malK)
            APL: APL_0280(potA)
            XCC: XCC2340(potG)
            XCB: XC_1776
            XCV: XCV2650(potG)
            XAC: XAC2472(potG)
            XOO: XOO2777(potG)
            XOM: XOO_2618(XOO2618)
            VCH: VC1428
            VVU: VV1_2604
            VVY: VV1685
            VPA: VP1336 VP1529 VPA0350
            VFI: VF1315(potA) VFA1091(sfuC)
            PPR: PBPRA1852 PBPRB0179
            PAE: PA0206 PA0302(potG) PA0603 PA3254 PA3607(potA)
            PAU: PA14_17640(potA)
            PPU: PP_0411 PP_1722 PP_3817 PP_5179(potG)
            PST: PSPTO_0489 PSPTO_0562 PSPTO_2524 PSPTO_2664 PSPTO_3882
                 PSPTO_5303(potG)
            PSB: Psyr_1602 Psyr_2335 Psyr_2398 Psyr_4615 Psyr_4692 Psyr_4863
            PSP: PSPPH_0643 PSPPH_1590 PSPPH_2556 PSPPH_2833 PSPPH_4726
                 PSPPH_4893(potG)
            PFL: PFL_0335(potA) PFL_2339(potA-1) PFL_4391(potA) PFL_5174(potA)
                 PFL_5639(potA) PFL_5924(potA-1)
            PFO: Pfl_1047 Pfl_1682 Pfl_2120 Pfl_3142 Pfl_3244 Pfl_4466
                 Pfl_5125 Pfl_5403
            PEN: PSEEN0438 PSEEN1241 PSEEN1434 PSEEN3041 PSEEN5293(potG)
            PCR: Pcryo_0239
            SON: SO_1271
            SDN: Sden_3030
            SFR: Sfri_3008
            SAZ: Sama_2641
            SBL: Sbal_1109
            SLO: Shew_0974
            SHE: Shewmr4_2917
            SHM: Shewmr7_2999
            SHN: Shewana3_3096
            SHW: Sputw3181_3069
            CPS: CPS_2039(potA) CPS_4672(potG)
            SDE: Sde_1366
            MAQ: Maqu_0341 Maqu_2136
            LPN: lpg1141
            LPF: lpl1148(potA)
            LPP: lpp1143(potA)
            MCA: MCA0872(potA)
            FTU: FTT0562(potG)
            FTF: FTF0562(potG)
            FTL: FTL_0681
            FTH: FTH_0683(potA)
            FTN: FTN_0739(potG)
            HCH: HCH_01472 HCH_02209
            AHA: AHA_4136
            NME: NMB0610
            NMA: NMA0816
            NMC: NMC0553
            NGO: NGO0192
            CVI: CV_1333(potG) CV_1678 CV_4102(potA)
            RSO: RSc1734(RS02922) RSc1794(RS04193)
            REU: Reut_B5523
            RME: Rmet_4399 Rmet_4843
            BMA: BMA1300(potG) BMA3076 BMAA0431 BMAA0856 BMAA1821
            BMV: BMASAVP1_A1787(potG)
            BML: BMA10299_A0108(potG)
            BXE: Bxe_A1951 Bxe_A3469 Bxe_A4198 Bxe_B0750 Bxe_B0939 Bxe_B1362
                 Bxe_B1511 Bxe_B1685 Bxe_B2703 Bxe_B2933
            BUR: Bcep18194_B2813
            BCN: Bcen_2383 Bcen_4728
            BCH: Bcen2424_2997
            BAM: Bamb_1674 Bamb_3044 Bamb_3296 Bamb_5376
            BPS: BPSL1300 BPSL1556(potG) BPSL1652 BPSS0248 BPSS0345
                 BPSS0466(potG) BPSS1738
            BPM: BURPS1710b_1540 BURPS1710b_2208(potA) BURPS1710b_2309(potG)
                 BURPS1710b_A0816 BURPS1710b_A1785 BURPS1710b_A2019(potG)
            BPL: BURPS1106A_A0633(potG)
            BPD: BURPS668_A0725(potG)
            BTE: BTH_I2277 BTH_I2834 BTH_II0642 BTH_II1949 BTH_II2053
            BPE: BP1930 BP2347
            BPA: BPP0903 BPP1692 BPP2304 BPP4344
            BBR: BB0996 BB1755 BB3416 BB4930
            RFR: Rfer_0353 Rfer_0593 Rfer_0889 Rfer_3223
            POL: Bpro_1011 Bpro_2023 Bpro_2096 Bpro_2913 Bpro_3887 Bpro_3947
                 Bpro_4355 Bpro_4379 Bpro_4419
            MPT: Mpe_A1904 Mpe_A3375
            HAR: HEAR3290(oppF)
            NEU: NE1870(potA)
            NMU: Nmul_A0982
            HPA: HPAG1_0700
            CJE: Cj0732
            CJR: CJE0832
            CJU: C8J_0699
            PCA: Pcar_1735
            DVU: DVU0098(potA) DVU0291
            DVL: Dvul_2864
            DDE: Dde_0213 Dde_3670
            LIP: LI0829(potA)
            BBA: Bd1419(potA)
            SFU: Sfum_3496
            PUB: SAR11_1337(potA)
            MLO: mll0232 mll1738 mll2890 mll2948 mll3065 mll6255 mll7187
                 mll8445 mlr2024 mlr2025 mlr3666 mlr4193 mlr6079 mlr6534
                 mlr6965 mlr7387 mlr7543 mlr7674 mlr9014 mlr9378
            MES: Meso_0164 Meso_2369
            SME: SMa0391 SMa0803 SMa0953 SMa1754 SMa2207 SMb20281 SMb20380
                 SMb21276(potA) SMc00771(potG) SMc01608 SMc01631 SMc01965
            ATU: Atu0610(potG) Atu2150 Atu3089 Atu4246 Atu4424 Atu5126(attA1)
                 Atu5248(potA) Atu5410 Atu5423(potG)
            ATC: AGR_C_1086 AGR_C_3896 AGR_L_1231 AGR_L_3441 AGR_L_887(potA)
                 AGR_pAT_185 AGR_pAT_353(potA) AGR_pAT_598 AGR_pAT_620
            RET: RHE_CH00715(potG) RHE_CH02893 RHE_CH02909 RHE_CH03418(potA)
                 RHE_PC00031
            RLE: RL0764 RL0984 RL2010 RL3353 RL3371 RL3881 RL4191 RL4451
                 pRL100251 pRL120141 pRL120171
            BME: BMEI0412 BMEII0193 BMEII0481
            BMF: BAB1_1627 BAB2_0428 BAB2_1065
            BMS: BR1611 BRA0112 BRA0809
            BMB: BruAb1_1598 BruAb2_0423 BruAb2_1046
            BJA: bll3287 bll6828 bll7105 bll7196 blr3544 blr5573 blr6644
            BRA: BRADO1107
            BBT: BBta_1091 BBta_6942
            RPA: RPA1479 RPA4160 RPA4650(potA)
            RPB: RPB_1454 RPB_4043
            RPC: RPC_1270 RPC_3954
            RPD: RPD_1034 RPD_1430
            RPE: RPE_4083
            NWI: Nwi_1006
            SIL: SPO1609(potA) SPO2702 SPO3468(potG) SPO3472 SPOA0382
            SIT: TM1040_0326 TM1040_0838 TM1040_2983 TM1040_2987 TM1040_3315
                 TM1040_3636
            RSP: RSP_0015 RSP_0349 RSP_1882 RSP_2159 RSP_2400 RSP_3041
                 RSP_3338 RSP_3396 RSP_3516
            RDE: RD1_0169(potG) RD1_0173 RD1_0277 RD1_2364 RD1_2409(potA)
                 RD1_2414 RD1_2427 RD1_3864 RD1_4131
            SAL: Sala_1114
            GOX: GOX1409
            MAG: amb2624
            BAN: BA1297(potA)
            BAR: GBAA1297(potA)
            BAA: BA_1824
            BAT: BAS1199
            BCE: BC1286(potA)
            BCA: BCE_1398(potA)
            BCZ: BCZK1179(potA)
            BTK: BT9727_1177(potA)
            BLI: BL01723
            BLD: BLi00398
            BCL: ABC3208
            OIH: OB3154
            GKA: GK0723
            SAU: SA0950(potA)
            SAV: SAV1099(potA)
            SAM: MW0982(potA)
            SAR: SAR1073
            SAS: SAS1034
            SAC: SACOL1108
            SAB: SAB0965
            SAA: SAUSA300_0999(potA)
            SAO: SAOUHSC_01046
            SEP: SE0797
            SER: SERP0686(potA)
            SHA: SH1853(potA)
            SSP: SSP1690
            LMO: lmo0807
            LMF: LMOf2365_0823
            LIN: lin0797
            LWE: lwe0763
            LLA: L175357(potA)
            LLC: LACR_1284
            LLM: llmg_1328(potA)
            SPY: SPy_1102(potA)
            SPZ: M5005_Spy_0826(potA)
            SPM: spyM18_1064(potA)
            SPG: SpyM3_0764(potA)
            SPS: SPs0964
            SPH: MGAS10270_Spy0942(potA)
            SPI: MGAS10750_Spy0977(potA)
            SPJ: MGAS2096_Spy0900(potA)
            SPK: MGAS9429_Spy0945(potA)
            SPA: M6_Spy0824
            SPB: M28_Spy0803(potA)
            SPN: SP_1389
            SPR: spr1246(potA)
            SPD: SPD_1221(potA)
            SAG: SAG1111(potA)
            SAN: gbs1178
            SAK: SAK_1196(potA)
            SMU: SMU.973(potA)
            STC: str1538(potA)
            STL: stu1538(potA)
            STE: STER_1496
            SSA: SSA_1048(potA)
            LPL: lp_0318(potA)
            LJO: LJ0888
            LAC: LBA0709(potA)
            LSA: LSA1363(potA)
            LSL: LSL_0113
            LDB: Ldb0647(potA1) Ldb2180(potA2)
            LBU: LBUL_0578
            LBR: LVIS_1859
            LCA: LSEI_1006
            EFA: EF1220 EF2652
            OOE: OEOE_0630 OEOE_1464
            LME: LEUM_0191
            CAC: CAC0840(potA)
            CPE: CPE1270 CPE1968(potA)
            CPF: CPF_2223(potA)
            CPR: CPR_1935
            CNO: NT01CX_1226
            CTH: Cthe_0750
            CDF: CD1024(potA)
            DSY: DSY1461
            MGE: MG_042(potA)
            MPN: MPN055(potA)
            MPU: MYPU_4250(potA)
            MPE: MYPE8570(potA)
            MGA: MGA_0135(malK)
            MMY: MSC_0224(potA)
            MMO: MMOB0480(potA)
            MHY: mhp559(potA)
            MHJ: MHJ_0544(potA)
            MHP: MHP7448_0542(potA)
            MSY: MS53_0508(potA)
            MCP: MCAP_0202
            UUR: UU107(potA)
            POY: PAM659(potA)
            AYW: AYWB_095(potA)
            MFL: Mfl511
            NFA: nfa22580
            SCO: SCO5648(SC6A9.19c) SCO5668(SC8B7.10c) SCO5923(SC10A5.28c)
            SMA: SAV2590 SAV2618
            TFU: Tfu_0280
            SEN: SACE_0983 SACE_1674
            BLO: BL0341
            RXY: Rxyl_2912
            FNU: FN1797(potA)
            PCU: pc0871(potA)
            BBU: BB0642(potA)
            BGA: BG0665(potA)
            BAF: BAPKO_0686(potA)
            TPA: TP0652
            CYA: CYA_1859(potA)
            CYB: CYB_0024 CYB_1301(potA)
            GVI: gll1404 gll4281
            AVA: Ava_2303
            TER: Tery_2805 Tery_2815
            BTH: BT_1291
            BFR: BF2723
            BFS: BF2738
            TTH: TTC0876(potA)
            TTJ: TTHA1240 TTHB175
            TMA: TM1376
            AFU: AF1608(potA)
            HAL: VNG1871G(potA2)
            HMA: pNG7347(potA1) rrnAC2870(potA2)
            HWA: HQ1431A(potA) HQ3382A(potA)
            TKO: TK0572
            APE: APE_0944.1 APE_1732
            PAI: PAE2890
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.31
            ExPASy - ENZYME nomenclature database: 3.6.3.31
            ExplorEnz - The Enzyme Database: 3.6.3.31
            ERGO genome analysis and discovery system: 3.6.3.31
            BRENDA, the Enzyme Database: 3.6.3.31
///
ENTRY       EC 3.6.3.32                 Enzyme
NAME        quaternary-amine-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (quaternary-amine-importing)
REACTION    ATP + H2O + quaternary amineout = ADP + phosphate + quaternary
            aminein [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            quaternary amine [CPD:C06703]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            quaternary amine [CPD:C06703]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A bacterial enzyme
            that imports betaine and glycine.
REFERENCE   1  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   2  [PMID:9335265]
  AUTHORS   Kempf B, Gade J, Bremer E.
  TITLE     Lipoprotein from the osmoregulated ABC transport system OpuA of
            Bacillus subtilis: purification of the glycine betaine binding
            protein and characterization of a functional lipidless mutant.
  JOURNAL   J. Bacteriol. 179 (1997) 6213-20.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   3  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
PATHWAY     PATH: map02010  ABC transporters - General
ORTHOLOGY   KO: K02000  glycine betaine/proline transport system ATP-binding
                        protein
GENES       ECO: b2677(proV)
            ECJ: JW2652(proV)
            ECE: Z3979(proV)
            ECS: ECs3540
            ECC: c3230(proV)
            ECI: UTI89_C3037(proV)
            ECP: ECP_2643
            ECV: APECO1_3844(proV)
            SPT: SPA2667(proV)
            SEC: SC2743(proV)
            STM: STM2809(proV)
            YPE: YPO2647(proV)
            YPK: y1221(proV)
            YPM: YP_2449(proV2)
            YPA: YPA_2375
            YPN: YPN_1133
            YPS: YPTB2959(proV)
            SFL: SF2705(proV)
            SFX: S2891(proV)
            SFV: SFV_2826(proV)
            SSN: SSON_2822(proV)
            SBO: SBO_2839(proV)
            SDY: SDY_2872(proV)
            MSU: MS0549(proV)
            VVU: VV2_0002
            VVY: VVA0511
            VPA: VPA1109
            PPR: PBPRB1742
            PAE: PA5094 PA5376
            PPU: PP_0294
            PST: PSPTO_0462 PSPTO_3060 PSPTO_5273
            PSB: Psyr_4711 Psyr_4831
            PSP: PSPPH_4749 PSPPH_4863
            PFL: PFL_0405 PFL_5764
            PFO: Pfl_0364 Pfl_5240
            PEN: PSEEN2603 PSEEN5190
            PCR: Pcryo_1087
            CPS: CPS_4935
            HCH: HCH_00854
            RSO: RSp0066(opuA)
            REU: Reut_B4811
            REH: H16_A0943
            BMA: BMAA0564(proV)
            BXE: Bxe_B1616
            BUR: Bcep18194_B0455 Bcep18194_B2843
            BPS: BPSS1426
            BPM: BURPS1710b_A0449 BURPS1710b_A0450(proV)
            BTE: BTH_II0966
            HPY: HP0819(proV)
            HPJ: jhp0758
            HPA: HPAG1_0805
            HAC: Hac_0722(proV)
            DDE: Dde_0673
            MXA: MXAN_2249(proV)
            PUB: SAR11_0798(proV) SAR11_1298(opuAA)
            MLO: mll2742 mll7330
            MES: Meso_2529
            SME: SMc00670(hisV) SMc02739(opuA) SMc04439
            ATU: Atu0893 Atu2279 Atu3802(proV) Atu3956 Atu4044 Atu5218(proV)
            ATC: AGR_C_1628 AGR_C_4141 AGR_L_1401GM AGR_L_1620
                 AGR_L_1796(opuAA) AGR_pAT_303(proV)
            RET: RHE_CH03087(proV) RHE_PF00394 RHE_PF00412
            RLE: RL3535 pRL100079(proV) pRL120514 pRL120532
            BME: BMEI0439 BMEII0548
            BMF: BAB1_1595 BAB2_0500
            BMS: BR1581 BRA0740
            BMB: BruAb1_1568
            SIL: SPO1132 SPO1549 SPO2443 SPOA0232(opuAA)
            RSP: RSP_2179(proV) RSP_3057 RSP_4000(proV)
            RDE: RD1_0014(opuAA) RD1_2932(opuAA)
            RRU: Rru_A1792 Rru_A2475
            BSU: BG11370(opuAA)
            BAN: BA2786(proV-2)
            BAR: GBAA2786(proV-2)
            BAA: BA_3308
            BAT: BAS2597
            BCE: BC2791
            BCA: BCE_2816(proV)
            BCZ: BCZK2516(opuAA)
            BTK: BT9727_2549(opuAA)
            BTL: BALH_2503(opuAA)
            BLI: BL01559(opuAA)
            BLD: BLi02628(opuAA)
            BCL: ABC1071(opuAA)
            OIH: OB0999 OB2944 OB3456
            SEP: SE0222
            SER: SERP2358
            SHA: SH2655
            LMO: lmo1014(gbuA)
            LMF: LMOf2365_1035
            LIN: lin1013(gbuA)
            LWE: lwe0998(gbuA) lwe0999(gbuB) lwe1000(gbuC) lwe1438 lwe1439
                 lwe1442(opuCD) lwe1443(opuCC) lwe1444(opuCB) lwe1445(opuCA)
            LLA: L74195(busAA)
            LLC: LACR_1542
            LLM: llmg_1048(busAA)
            SPZ: M5005_Spy_0157(opuAA)
            SPB: M28_Spy0155(opuAA)
            SAG: SAG1797
            SAN: gbs1839 gbs2088
            SAK: SAK_1818(proV)
            SMU: SMU.1063(opuAa)
            SSA: SSA_0386(opuAa)
            LPL: lp_0368(choQ)
            LSA: LSA1696
            LCA: LSEI_2145 LSEI_2628
            EFA: EF2641
            CTC: CTC02342
            DSY: DSY1221
            MPA: MAP0273
            RHA: RHA1_ro01162 RHA1_ro02589 RHA1_ro06003
            SCO: SCO1621(opuAA) SCO4830(SC2A6.15) SCO6062(SC9B1.09)
            SMA: SAV2185 SAV3432 SAV6715(opuAA) SAV7409
            PAC: PPA1477
            TFU: Tfu_2930
            FAL: FRAAL5387
            SEN: SACE_2225 SACE_2410 SACE_2787 SACE_6412
            BBU: BB0146(proV)
            BGA: BG0146(proV)
            BAF: BAPKO_0148(proV)
            SYW: SYNW1915
            AVA: Ava_3286
            PMT: PMT0553
            PMB: A9601_04891(salX) A9601_08111
            PMC: P9515_04961(salX) P9515_08341
            PMF: P9303_06281(salX) P9303_14301 P9303_16611 P9303_16991(proV)
            PMG: P9301_04581(salX) P9301_08101
            PME: NATL1_04881(salX) NATL1_07861
            BFR: BF3336
            BFS: BF3172(opuAA)
            SRU: SRU_0431(proV)
            MAC: MA2145(proV)
            MBA: Mbar_A2376
            MMA: MM_0040(otaA)
            MBU: Mbur_0501
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.32
            ExPASy - ENZYME nomenclature database: 3.6.3.32
            ExplorEnz - The Enzyme Database: 3.6.3.32
            ERGO genome analysis and discovery system: 3.6.3.32
            BRENDA, the Enzyme Database: 3.6.3.32
///
ENTRY       EC 3.6.3.33                 Enzyme
NAME        vitamin B12-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (vitamin B12-importing)
REACTION    ATP + H2O + vitamin B12out = ADP + phosphate + vitamin B12in
            [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            vitamin B12 [CPD:C05776]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            vitamin B12 [CPD:C05776]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A bacterial enzyme
            that imports cobalamin derivatives.
REFERENCE   1  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   2  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   3  [PMID:3528129]
  AUTHORS   Friedrich MJ, de Veaux LC, Kadner RJ.
  TITLE     Nucleotide sequence of the btuCED genes involved in vitamin B12
            transport in Escherichia coli and homology with components of
            periplasmic-binding-protein-dependent transport systems.
  JOURNAL   J. Bacteriol. 167 (1986) 928-34.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map02010  ABC transporters - General
ORTHOLOGY   KO: K06074  vitamin B12 transport system ATP-binding protein
GENES       ECO: b1709(btuD)
            ECJ: JW1699(btuD)
            ECE: Z2738(btuD)
            ECS: ECs2416
            ECC: c2105(btuD)
            ECI: UTI89_C1902(btuD)
            ECP: ECP_1657
            ECV: APECO1_784(btuC)
            ECW: EcE24377A_1928(btuD)
            ECX: EcHS_A1789(btuD)
            STY: STY1768(btuD)
            STT: t1223(btuD)
            SPT: SPA1501(btuD)
            SEC: SC1361(btuD)
            STM: STM1342(btuD)
            YPE: YPO2423(btuD)
            YPK: y1916(btuD)
            YPM: YP_2210(btuD)
            YPA: YPA_1767
            YPN: YPN_1877
            YPS: YPTB2331(btuD)
            YPI: YpsIP31758_1722(btuD)
            SFL: SF1522(btuD)
            SFX: S1639(btuD)
            SFV: SFV_1514(btuD)
            SSN: SSON_1449(btuD)
            SBO: SBO_1419(btuD)
            SDY: SDY_1804(btuD)
            ECA: ECA1834(btuD)
            PLU: plu2661(btuD)
            VCH: VC1245
            VVU: VV1_2781
            VVY: VV1481
            VPA: VP1312(btuD)
            PPR: PBPRA2151(btuD)
            AHA: AHA_2735
            BUR: Bcep18194_B0624
            RRU: Rru_A0982
STRUCTURES  PDB: 1L7V  2QI9  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.33
            ExPASy - ENZYME nomenclature database: 3.6.3.33
            ExplorEnz - The Enzyme Database: 3.6.3.33
            ERGO genome analysis and discovery system: 3.6.3.33
            BRENDA, the Enzyme Database: 3.6.3.33
///
ENTRY       EC 3.6.3.34                 Enzyme
NAME        iron-chelate-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (iron-chelate-importing)
REACTION    ATP + H2O + iron chelateout = ADP + phosphate + iron chelatein
            [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            iron chelate [CPD:C06704]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            iron chelate [CPD:C06704]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A bacterial enzyme
            that imports Fe-enterobactin, Fe-dicitrate, Fe-hydroxamate and other
            siderophores.
REFERENCE   1  [PMID:1838574]
  AUTHORS   Shea CM, McIntosh MA.
  TITLE     Nucleotide sequence and genetic organization of the ferric
            enterobactin transport system: homology to other periplasmic binding
            protein-dependent systems in Escherichia coli.
  JOURNAL   Mol. Microbiol. 5 (1991) 1415-28.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:1588908]
  AUTHORS   Koster W, Bohm B.
  TITLE     Point mutations in two conserved glycine residues within the
            integral membrane protein FhuB affect iron(III) hydroxamate
            transport.
  JOURNAL   Mol. Gen. Genet. 232 (1992) 399-407.
  ORGANISM  Escherichia coli [GN:eco], Vibrio anguillarum
REFERENCE   3  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   4  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   5  [PMID:9613584]
  AUTHORS   Mademidis A, Koster W.
  TITLE     Transport activity of FhuA, FhuC, FhuD, and FhuB derivatives in a
            system free of polar effects, and stoichiometry of components
            involved in ferrichrome uptake.
  JOURNAL   Mol. Gen. Genet. 258 (1998) 156-65.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map02010  ABC transporters - General
ORTHOLOGY   KO: K02013  iron complex transport system ATP-binding protein
GENES       TET: TTHERM_00032870
            ECO: b0151(fhuC) b0588(fepC) b4287(fecE)
            ECJ: JW0147(fhuC) JW0580(fepC) JW4247(fecE)
            ECE: Z0162(fhuC) Z0729(fepC) Z1964 Z4385 Z4919
            ECS: ECs0155 ECs0627 ECs1697 ECs3916 ECs4387
            ECC: c0186(fhuC) c0297 c0675(fepC) c1650 c2515 c3774(fepC) c4318
            ECI: UTI89_C0167(fhuC) UTI89_C0590(fepC) UTI89_C1386 UTI89_C2263
                 UTI89_C3462 UTI89_C4038
            ECP: ECP_0161 ECP_0620 ECP_1242 ECP_2033 ECP_3120 ECP_3605
            ECV: APECO1_1461(fepC) APECO1_1834(fhuC) APECO1_2942 APECO1_311
                 APECO1_3385(fepC)
            STY: STY0219(fhuC) STY0634(fepC) STY0803
            STT: t0200(fhuC) t2116 t2278(fepC)
            SPT: SPA0198(fhuC) SPA1981 SPA2144(fepC)
            SEC: SC0192(fhuC) SC0621(fepC) SC0769(fhuC)
            STM: STM0192(fhuC) STM0590(fepC) STM0771
            YPE: YPO0279(hmuV) YPO1312 YPO1345 YPO1533 YPO3392(fhuC) YPO4025
            YPK: y0539(hmuV) y0796(fhuC) y2637(ysuD) y2837 y2873(yiuC)
                 y4046(fecE)
            YPM: YP_0293(fhuC) YP_0434(hmuV) YP_1251(fepC) YP_1280(yiuC)
                 YP_1422(ysuD) YP_3388(fecE)
            YPA: YPA_0631 YPA_0827 YPA_1029 YPA_2892 YPA_4003 YPA_4116
            YPN: YPN_0698 YPN_2447 YPN_2639 YPN_2667 YPN_3388 YPN_3673
            YPS: YPTB0336(hmuV) YPTB0739(fhuC) YPTB1343 YPTB1371 YPTB1545
                 YPTB3860
            SFL: SF0143(fhuC) SF0502(fepC) SF1192
            SFX: S0146(fhuC) S0508(fepC) S1278
            SFV: SFV_0136(fhuC) SFV_0536(fepC) SFV_1207
            SSN: SSON_0163(fhuC) SSON_0539(fepC) SSON_4459(fecE)
            SBO: SBO_0140(fhuC) SBO_0449(fepC)
            SDY: SDY_0167(fhuC) SDY_0519(fepC) SDY_1240 SDY_3547(shuV)
                 SDY_4293(fecE)
            ECA: ECA1073(fecE) ECA1843(hmuV) ECA2561 ECA2806(cbrD) ECA3094
                 ECA3243 ECA3312(fhuC) ECA4254
            PLU: plu2636 plu2851 plu4450(fecE) plu4626(fepC)
            SGL: SG1540 SG1544 SGP1_0035
            HIN: HI1272 HI1470(fepC)
            PMU: PM0128(fecE) PM1080 PM1147 PM1309
            MSU: MS0794(fepC) MS1012(fepC) MS1201(fepC)
            APL: APL_0717 APL_1793 APL_2013(fhuC)
            XCC: XCC0161(ylmA)
            XCB: XC_0170
            XCV: XCV0163
            XAC: XAC0179(ylmA)
            XOO: XOO4515(ylmA)
            XOM: XOO_4254(XOO4254)
            VCH: VC0201 VC0779 VCA0230 VCA0915(hutD)
            VCO: VC0395_A2522(atpB)
            VVU: VV2_0112 VV2_1011 VV2_1609
            VVY: VVA0419 VVA0620 VVA1504
            VPA: VPA0421(hutD) VPA0660 VPA1436 VPA1652
            VFI: VF1220(hmuV) VFA0158(fhuC) VFA0783(fhuC) VFA0824
                 VFA0971(btuD)
            PPR: PBPRA1565 PBPRA2108(hutD) PBPRB1384 PBPRB1814
            PAE: PA2912 PA4158(fepC) PA4706
            PAU: PA14_62280(phuV)
            PPU: PP_2416 PP_2592 PP_4687
            PST: PSPTO_0760 PSPTO_3258 PSPTO_5561
            PSB: Psyr_0664 Psyr_2593 Psyr_3096 Psyr_5102
            PSP: PSPPH_2760(cbrD) PSPPH_3008 PSPPH_4633(fecE) PSPPH_5184
            PFL: PFL_0645 PFL_3502(hemV-1) PFL_3622 PFL_5264
            PFO: Pfl_0593 Pfl_4798
            PEN: PSEEN2494(bauE) PSEEN3066 PSEEN4720
            ACI: ACIAD0969
            SON: SO_1033 SO_3675(hmuV)
            SDN: Sden_0784 Sden_1116
            SHN: Shewana3_3241 Shewana3_3280
            ILO: IL0115(hmuV)
            CPS: CPS_1166(btuD)
            PHA: PSHAa2566(fhuC) PSHAb0066(hmuV)
            PAT: Patl_1141 Patl_1490
            SDE: Sde_3202
            TCX: Tcr_0180
            NOC: Noc_0839
            HCH: HCH_01396 HCH_03458 HCH_03795 HCH_05463 HCH_06574 HCH_06829
            ABO: ABO_2368
            NME: NMB1993
            NMA: NMA0448
            NGO: NGO2088
            CVI: CV_1487 CV_1560 CV_1793 CV_2234(fepC) CV_3899(fecE)
            RSO: RSc2398(RS02720)
            REU: Reut_A0656 Reut_A3243
            RME: Rmet_2787 Rmet_5378
            BMA: BMA0687 BMA1188 BMA2035 BMAA1830(hmuV)
            BXE: Bxe_A3500 Bxe_B0520 Bxe_B1929
            BCN: Bcen_5427
            BCH: Bcen2424_5435
            BAM: Bamb_1532 Bamb_1696 Bamb_2502 Bamb_4776
            BPS: BPSL0978 BPSL1784 BPSL2723 BPSS0240
            BPM: BURPS1710b_1190 BURPS1710b_2080 BURPS1710b_A1775(hmuV)
            BTE: BTH_I0836 BTH_I1413 BTH_I2424(fxuB) BTH_II2143
            BPE: BP0343(bhuV) BP3339
            BPA: BPP3796 BPP4189(bhuV)
            BBR: BB4241 BB4659(bhuV)
            RFR: Rfer_2619
            POL: Bpro_2772 Bpro_2780 Bpro_4777
            MPT: Mpe_A2305(fecE) Mpe_B0514
            NMU: Nmul_A0883
            EBA: ebA4020
            DAR: Daro_4032
            TBD: Tbd_2049
            MFA: Mfla_1607
            HPY: HP0888(fecE)
            HPJ: jhp0821(fecE)
            HPA: HPAG1_0593 HPAG1_0837 HPAG1_0869
            HAC: Hac_1272(fecE)
            WSU: WS1124
            TDN: Tmden_0116 Tmden_1539
            CJE: Cj1354(ceuD) Cj1616(chuC)
            CJR: CJE1543(ceuD) CJE1788
            CJU: C8J_1270(ceuD) C8J_1517(chuC)
            PCA: Pcar_0155 Pcar_0465 Pcar_3057
            DVU: DVU0648
            DDE: Dde_1624 Dde_3105
            DPS: DP0216 DP2978
            ADE: Adeh_3466
            MXA: MXAN_1321
            SFU: Sfum_0495 Sfum_2133 Sfum_2739 Sfum_2776 Sfum_3281 Sfum_3704
            MLO: mll1149 mlr8227
            MES: Meso_0136 Meso_1444
            SME: SMa1741 SMb20058 SMb21429 SMc01510(hmuV)
            ATU: Atu2458(hmuV) Atu2476 Atu3388(fecE) Atu3394(fecE)
                 Atu3691(fecE) Atu4025(fhuC) Atu5316(fepC)
            ATC: AGR_C_4465 AGR_C_4492 AGR_L_1656(fhuC) AGR_L_2292
                 AGR_L_2857(fecE) AGR_L_2867 AGR_pAT_452
            RET: RHE_CH02680 RHE_CH03271(hmuV) RHE_PE00282(fhuC) RHE_PF00271
            RLE: RL2019 RL2715 RL3050 RL3700(hmuV) pRL100328(fhuC) pRL120711
            BME: BMEI0660 BMEII0537 BMEII0604
            BMF: BAB1_1364 BAB2_0485
            BMS: BR1344 BRA0678 BRA0754
            BMB: BruAb1_1342 BruAb2_0478 BruAb2_0550
            BJA: blr7079(hmuV)
            RPA: RPA0149 RPA0722(fecE) RPA2118 RPA2310 RPA2382
            RPB: RPB_0168 RPB_0733 RPB_2698 RPB_4399
            RPC: RPC_0086 RPC_1967 RPC_1987 RPC_3609 RPC_4255
            RPD: RPD_0631 RPD_2348 RPD_2478 RPD_2923
            RPE: RPE_0528 RPE_3127 RPE_3155 RPE_3488
            NWI: Nwi_2074 Nwi_2322 Nwi_3049
            BHE: BH04930(hmuV)
            BQU: BQ04120(hmuV) BQ10330(ceuD)
            CCR: CC_1193
            SIT: TM1040_0343
            RSP: RSP_1437 RSP_2405 RSP_3222 RSP_3390 RSP_3413
            JAN: Jann_2136
            RDE: RD1_2675 RD1_3481 RD1_4191(hmuV)
            ZMO: ZMO0230(fhuC) ZMO1846
            NAR: Saro_1189
            SAL: Sala_1001
            ELI: ELI_07945
            GOX: GOX0582 GOX1012
            RRU: Rru_A0491 Rru_A3223
            BSU: BG11390(fhuC) BG12036(yclP) BG12957(yfmF) BG13370(ylmA)
                 BG14034(yusV) BG14141(yvrA)
            BHA: BH1027 BH1039 BH1081(fhuC) BH1587 BH2270 BH3292 BH3295
            BAN: BA0618 BA3864 BA4595 BA4784 BA5327 BA5629
            BAR: GBAA0618 GBAA3864 GBAA4595 GBAA4784 GBAA5327 GBAA5629
            BAA: BA_0187 BA_0485 BA_1201 BA_4339 BA_5035 BA_5212
            BAT: BAS0584 BAS3580 BAS4263 BAS4439 BAS4949 BAS5230
            BCE: BC0619(fecE) BC3735(fecE) BC4361(fhuC) BC4544(fhuC) BC5103
                 BC5381(fhuC)
            BCA: BCE_0686 BCE_3768 BCE_4448 BCE_4668 BCE_5223 BCE_5510
            BCZ: BCZK0528(fecE) BCZK3492 BCZK4111(fhuC) BCZK4289(fhuC)
                 BCZK4812 BCZK5078
            BTK: BT9727_0528(fecE) BT9727_3480 BT9727_4100(fhuC)
                 BT9727_4278(fhuC) BT9727_4792 BT9727_5061
            BLI: BL00705(fhuC) BL00718(yvrA) BL01759(yclP) BL02183(yusV)
                 BL02257
            BLD: BLi00465(yclP) BLi01752(ylmA) BLi03472(yusV) BLi03504(yvrA)
                 BLi03519(fhuC)
            BCL: ABC0683 ABC1084(fhuC) ABC1838 ABC2893 ABC3420
            OIH: OB0262 OB0450 OB0541 OB0707
            GKA: GK0194 GK1461 GK1677
            SAU: SA0602(fhuA) SA0690 SA1958
            SAV: SAV0647(fhuA) SAV0735 SAV2153
            SAM: MW0609(fhuA) MW0697 MW2079
            SAR: SAR0657(fhuA) SAR0789(sstC) SAR2241
            SAS: SAS0612 SAS0700 SAS2054
            SAC: SACOL0704 SACOL0798 SACOL2144
            SAB: SAB0596(fhuA) SAB2033c
            SAA: SAUSA300_0633(fhuA) SAUSA300_0720 SAUSA300_2103
            SAO: SAOUHSC_00652 SAOUHSC_00748 SAOUHSC_02397
            SEP: SE0421 SE0517
            SER: SERP0306 SERP0402
            SHA: SH0881 SH2158 SH2247(fhuA)
            SSP: SSP0731 SSP1982 SSP2073
            LMO: lmo1778 lmo1960(fhuC) lmo2182 lmo2429
            LMF: LMOf2365_1803 LMOf2365_1990 LMOf2365_2215 LMOf2365_2400
            LIN: lin1890 lin2074(fhuC) lin2286 lin2523
            LWE: lwe1796 lwe1986(fhuC) lwe2199 lwe2376(fhuC)
            LLA: L44550(ymeB)
            LLC: LACR_0371 LACR_1313
            SPY: SPy_0386(fhuA) SPy_1793
            SPZ: M5005_Spy_0324(fhuA) M5005_Spy_1526(fhuC)
            SPM: spyM18_0439(fhuC) spyM18_1865
            SPG: SpyM3_0283(fhuC.1) SpyM3_1558(fhuC.2)
            SPS: SPs0309 SPs1576
            SPA: M6_Spy0350 M6_Spy1519(fhuC)
            SPB: M28_Spy0313(fhuA) M28_Spy1516(fhuC)
            SPN: SP_1035 SP_1871
            SPR: spr0938(ABC-NBD) spr1686(fecE)
            SAG: SAG1008 SAG1392
            SAN: gbs1043 gbs1462
            SAK: SAK_1103 SAK_1425(fhuC)
            SMU: SMU.1695 SMU.997
            STC: str1026(fatA) str1642
            STL: stu1026(fatA) stu1642
            SSA: SSA_1579 SSA_1741 SSA_1763
            LPL: lp_1475(fecE) lp_3104(fhuC)
            LSA: LSA0400
            LBR: LVIS_0701
            EFA: EF0191 EF1639 EF3083
            STH: STH1603 STH1933 STH653
            CAC: CAC0791(hfuC) CAC1989 CAC2443
            CPE: CPE0225(fhuC) CPE0795 CPE0813(fhuC) CPE1043 CPE1215
            CTC: CTC00783(fepC) CTC00962(fecE) CTC01197(fepC) CTC01370(fepC)
            CHY: CHY_0399 CHY_1752 CHY_2191
            DSY: DSY0089 DSY0366 DSY0392 DSY1005 DSY1135 DSY1761 DSY2086
                 DSY3094 DSY3570 DSY3833 DSY3872
            TTE: TTE0374(fepC) TTE1867(fepC2)
            MTA: Moth_1423 Moth_1464
            UUR: UU069(fecE) UU435(fhuC)
            MTU: Rv3041c
            MTC: MT3126
            MBO: Mb3067c
            MLE: ML1726
            MPA: MAP3089c MAP3727
            CGL: NCgl0037(cgl0038) NCgl0380(cgl0391) NCgl0482(cgl0500)
                 NCgl0636(cgl0666) NCgl0645(cgl0675) NCgl0779(cgl0813)
                 NCgl1179(cgl1227) NCgl1566(cgl1628) NCgl2361(cgl2447)
            CGB: cg0053 cg0469 cg0589 cg0768 cg0777 cg0928 cg1383 cg1834
                 cg2688(phrA)
            CEF: CE0684 CE0693 CE0884 CE1325 CE2344 CE2675
            CDI: DIP0110(irp6C) DIP0585 DIP0628(hmuV) DIP1059 DIP1067 DIP1085
            CJK: jk0318(hmuV) jk0559(irp6C) jk1293(fetA) jk1328 jk1774(fhuA)
                 jk1806(fecA) jk1818(fepA) jk1884(feuA) jk1985(feyA)
            NFA: nfa18230 nfa24620 nfa25190 nfa29260 nfa42910
            RHA: RHA1_ro00886
            SCO: SCO0495(SCF34.14c) SCO0998(2SCG2.11) SCO1785(SCI51.25c)
                 SCO1798(SCI5.06c) SCO2274(SCC75A.20) SCO7217(SC2H12.16)
                 SCO7400(SC10G8.28c) SCO7459(SC5C11.16c)
            SMA: SAV600(fecC) SAV6480 SAV6493(fepC)
            TWH: TWT058(fepC)
            TWS: TW068
            LXX: Lxx11780 Lxx17230
            PAC: PPA0078 PPA0104 PPA0335 PPA0426 PPA0658 PPA0782 PPA0792
                 PPA1530 PPA1778
            TFU: Tfu_0139 Tfu_0336 Tfu_1494 Tfu_2384
            FRA: Francci3_3500 Francci3_4240
            FAL: FRAAL5645(fecE)
            SEN: SACE_0622(fecC) SACE_4373 SACE_5745
            BLO: BL0825
            BAD: BAD_0752
            FNU: FN0302(fecE) FN0307(fecE) FN0770(hmuV) FN0882(hmuV)
                 FN1968(hmuV)
            TDE: TDE0625 TDE0746 TDE0756 TDE1178 TDE1183 TDE2232
            LIL: LA1724
            LIC: LIC12079
            LBL: LBL_1280
            SYN: slr1318(fecE)
            SYW: SYNW1335
            SYD: Syncc9605_1483
            SYE: Syncc9902_1016
            CYA: CYA_2032
            CYB: CYB_2728
            GVI: gll0578 gll3602
            ANA: all0389 all2584 alr3241 alr4033
            AVA: Ava_2830
            PMA: Pro0888(modF)
            PMM: PMM0807
            PMT: PMT0658
            PMN: PMN2A_0217
            PMI: PMT9312_0816
            BTH: BT_1950 BT_2100
            BFR: BF2194 BF3026
            BFS: BF2248
            PGI: PG0646 PG0672
            SRU: SRU_1293 SRU_2731
            CTE: CT0412 CT0753 CT0943 CT1760(fecE)
            DET: DET0652 DET0686 DET0817 DET1176
            DEH: cbdb_A636(fepC) cbdb_A795
            DRA: DR_2590 DR_B0016 DR_B0121
            DGE: Dgeo_0023 Dgeo_0126 Dgeo_2759
            TTH: TTC0392(fecE) TT_P0177
            TTJ: TTHA0748 TTHB218
            TMA: TM0078 TM0191
            MJA: MJ0089 MJ0873
            MMP: MMP0198 MMP1183
            MAC: MA0950 MA1132 MA1198 MA1233 MA2150(fecE) MA3358 MA3453 MA3642
                 MA3676 MA3919 MA4532
            MBA: Mbar_A0297 Mbar_A0465 Mbar_A0509 Mbar_A1172 Mbar_A1872
                 Mbar_A2262 Mbar_A2394 Mbar_A2397 Mbar_A2733
            MMA: MM_0570 MM_2067
            MBU: Mbur_0496 Mbur_1049 Mbur_1095 Mbur_1545
            MHU: Mhun_0187 Mhun_0221 Mhun_0246 Mhun_0279 Mhun_0357
            MSI: Msm_1395
            AFU: AF0430(hemV-1) AF1401(hemV-3)
            HAL: VNG1371Gm(hemV2) VNG2552G(yfmF) VNG2558G(fepC)
            HMA: pNG7276(fhuG2) rrnAC3372(fecE)
            HWA: HQ1626A(hemV)
            NPH: NP3818A(abc16a)
            TAC: Ta1410
            PTO: PTO1320
            PHO: PH0791 PH1235
            PAB: PAB0678(hemV-1) PAB1536(hemV-2)
            PFU: PF0502(fecE) PF0909
            TKO: TK0708 TK2020 TK2208
            APE: APE_1055.1
            SSO: SSO0487
            STO: ST0842
            SAI: Saci_1222
            PAI: PAE2699
STRUCTURES  PDB: 1L2P  1L6T  2IHY  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.34
            ExPASy - ENZYME nomenclature database: 3.6.3.34
            ExplorEnz - The Enzyme Database: 3.6.3.34
            ERGO genome analysis and discovery system: 3.6.3.34
            BRENDA, the Enzyme Database: 3.6.3.34
///
ENTRY       EC 3.6.3.35                 Enzyme
NAME        manganese-transporting ATPase;
            ABC-type manganese permease complex
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (manganese-importing)
REACTION    ATP + H2O + Mn2+out = ADP + phosphate + Mn2+in [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            Mn2+ [CPD:C00034]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            Mn2+ [CPD:C00034]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A bacterial enzyme
            that imports Mn2+, Zn2+ and iron chelates.
REFERENCE   1  [PMID:7569321]
  AUTHORS   Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH Jr.
  TITLE     Phylogenetic analyses of the ATP-binding constituents of bacterial
            extracytoplasmic receptor-dependent ABC-type nutrient uptake
            permeases.
  JOURNAL   Res. Microbiol. 146 (1995) 271-8.
REFERENCE   2  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   3  [PMID:9767595]
  AUTHORS   Novak R, Braun JS, Charpentier E, Tuomanen E.
  TITLE     Penicillin tolerance genes of Streptococcus pneumoniae: the ABC-type
            manganese permease complex Psa.
  JOURNAL   Mol. Microbiol. 29 (1998) 1285-96.
  ORGANISM  Streptococcus pneumoniae
REFERENCE   4  [PMID:9440518]
  AUTHORS   Kolenbrander PE, Andersen RN, Baker RA, Jenkinson HF.
  TITLE     The adhesion-associated sca operon in Streptococcus gordonii encodes
            an inducible high-affinity ABC transporter for Mn2+ uptake.
  JOURNAL   J. Bacteriol. 180 (1998) 290-5.
  ORGANISM  Streptococcus gordonii
GENES       AZO: azo0642(mntA1) azo1216(mntA2)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.35
            ExPASy - ENZYME nomenclature database: 3.6.3.35
            ExplorEnz - The Enzyme Database: 3.6.3.35
            ERGO genome analysis and discovery system: 3.6.3.35
            BRENDA, the Enzyme Database: 3.6.3.35
///
ENTRY       EC 3.6.3.36                 Enzyme
NAME        taurine-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (taurine-importing)
REACTION    ATP + H2O + taurineout = ADP + phosphate + taurinein [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            taurine [CPD:C00245]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            taurine [CPD:C00245]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A bacterial enzyme
            that imports taurine.
REFERENCE   1  [PMID:8808933]
  AUTHORS   van der Ploeg JR, Weiss MA, Saller E, Nashimoto H, Saito N, Kertesz
            MA, Leisinger T.
  TITLE     Identification of sulfate starvation-regulated genes in Escherichia
            coli: a gene cluster involved in the utilization of taurine as a
            sulfur source.
  JOURNAL   J. Bacteriol. 178 (1996) 5438-46.
  ORGANISM  Escherichia coli [GN:eco]
GENES       ECO: b0366(tauB)
            ECJ: JW0358(tauB)
            ECE: Z0465(tauB)
            ECS: ECs0420
            ECC: c0473(tauB)
            ECI: UTI89_C0385(tauB)
            ECX: EcHS_A0430(tauB)
            YPE: YPO0183(tauB)
            YPK: y3964(tauB)
            YPM: YP_0182(tauB1)
            YPA: YPA_3289
            YPS: YPTB3721(tauB)
            YPI: YpsIP31758_3937(tauB)
            SFL: SF0252(tauB)
            SFX: S0273(tauB)
            SFV: SFV_0330(tauB)
            SSN: SSON_0344(tauB)
            SBO: SBO_0260(tauB)
            SDY: SDY_0504(tauB)
            ECA: ECA1530(tauB)
            PAE: PA3937
            PAU: PA14_12940
            PPU: PP_0232(tauB)
            PST: PSPTO_5320(tauB)
            PSP: PSPPH_4909(cmpC)
            PFL: PFL_0271
            PFO: Pfl_0255
            AHA: AHA_2937
            CVI: CV_2857(tauB)
            REU: Reut_A1471
            BMA: BMAA1581(tauB)
            BML: BMA10299_2018(tauB)
            BMN: BMA10247_A0696(tauB)
            BCN: Bcen_2270
            BCH: Bcen2424_2885
            BPS: BPSS1573(tauB)
            BPM: BURPS1710b_A0621(tauB)
            BPL: BURPS1106A_A2134(tauB)
            BPD: BURPS668_A2221(tauB)
            BTE: BTH_II0801
            AZO: azo2392(tauB)
            MLO: mlr4518
            SME: SMb21527(tauB)
            RET: RHE_PC00018(tauB)
            RLE: pRL100238
            BBT: BBta_1168
            RDE: RD1_0983(tauB)
            MJA: MJ0412(tauB)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.36
            ExPASy - ENZYME nomenclature database: 3.6.3.36
            ExplorEnz - The Enzyme Database: 3.6.3.36
            ERGO genome analysis and discovery system: 3.6.3.36
            BRENDA, the Enzyme Database: 3.6.3.36
///
ENTRY       EC 3.6.3.37                 Enzyme
NAME        guanine-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (guanine-importing)
REACTION    ATP + H2O + guanineout = ADP + phosphate + guaninein [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            guanine [CPD:C00242]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            guanine [CPD:C00242]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A eukaryotic enzyme
            that imports guanine and tryptophan (it contains a single
            ATP-binding site).
REFERENCE   1  [PMID:3149712]
  AUTHORS   Dreesen TD, Johnson DH, Henikoff S.
  TITLE     The brown protein of Drosophila melanogaster is similar to the white
            protein and to components of active transport complexes.
  JOURNAL   Mol. Cell. Biol. 8 (1988) 5206-15.
  ORGANISM  Drosophila melanogaster [GN:dme]
REFERENCE   2  [PMID:2503416]
  AUTHORS   Tearle RG, Belote JM, McKeown M, Baker BS, Howells AJ.
  TITLE     Cloning and characterization of the scarlet gene of Drosophila
            melanogaster.
  JOURNAL   Genetics. 122 (1989) 595-606.
  ORGANISM  Drosophila melanogaster [GN:dme]
REFERENCE   3
  AUTHORS   Griffiths, J.K. and Sansom, C.E.
  TITLE     The Transporter Factsbook, Academic Press, San Diego, 1998.
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.37
            ExPASy - ENZYME nomenclature database: 3.6.3.37
            ExplorEnz - The Enzyme Database: 3.6.3.37
            ERGO genome analysis and discovery system: 3.6.3.37
            BRENDA, the Enzyme Database: 3.6.3.37
///
ENTRY       EC 3.6.3.38                 Enzyme
NAME        capsular-polysaccharide-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (capsular-polysaccharide-exporting)
REACTION    ATP + H2O + capsular polysaccharidein = ADP + phosphate + capsular
            polysaccharideout [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            capsular polysaccharide [CPD:C06705]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            capsular polysaccharide [CPD:C06705]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. An enzyme that exports
            capsular polysaccharide from Gram-negative bacteria.
REFERENCE   1  [PMID:8302219]
  AUTHORS   Fath MJ, Kolter R.
  TITLE     ABC transporters: bacterial exporters.
  JOURNAL   Microbiol. Rev. 57 (1993) 995-1017.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:9274022]
  AUTHORS   Paulsen IT, Beness AM, Saier MH Jr.
  TITLE     Computer-based analyses of the protein constituents of transport
            systems catalysing export of complex carbohydrates in bacteria.
  JOURNAL   Microbiology. 143 ( Pt 8) (1997) 2685-99.
REFERENCE   3  [PMID:9513268]
  AUTHORS   Pigeon RP, Silver RP.
  TITLE     Analysis of the G93E mutant allele of KpsM, the membrane component
            of an ABC transporter involved in polysialic acid translocation in
            Escherichia coli K1.
  JOURNAL   FEMS. Microbiol. Lett. 156 (1997) 217-22.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   5
  AUTHORS   Griffiths, J.K. and Sansom, C.E.
  TITLE     The Transporter Factsbook, Academic Press, San Diego, 1998.
GENES       ECC: c3697(kpsT)
            PMU: PM0781(hexA)
            APL: APL_1585(cpxA)
            LPN: lpg0773
            NME: NMB0074(ctrD)
            NMA: NMA0195(ctrD)
            NMC: NMC0058(ctrD)
            BMA: BMA2304
            BMV: BMASAVP1_A0524
            BML: BMA10299_A1075
            BMN: BMA10247_2182
            BUR: Bcep18194_A3867
            BPS: BPSL2804(wzt2)
            BPD: BURPS668_3251
            BTE: BTH_I1335(bexA)
            BPE: BP1624(kpsT)
            NEU: NE1385(rkpS)
            CJE: Cj1447c(kpsT)
            CJU: C8J_1353(kpsT)
            SME: SMb20832(rkpS)
            NWI: Nwi_2153
            SIL: SPO0949(kpsT)
            SPA: M6_Spy0623
            SMU: SMU.828(rgpD)
            SSA: SSA_1507(rgpD)
            CAC: CAC2328
            SYC: syc0306_c
            MAC: MA1177
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.38
            ExPASy - ENZYME nomenclature database: 3.6.3.38
            ExplorEnz - The Enzyme Database: 3.6.3.38
            ERGO genome analysis and discovery system: 3.6.3.38
            BRENDA, the Enzyme Database: 3.6.3.38
///
ENTRY       EC 3.6.3.39                 Enzyme
NAME        lipopolysaccharide-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (lipopolysaccharide-exporting)
REACTION    ATP + H2O + lipopolysaccharidein = ADP + phosphate +
            lipopolysaccharideout [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            lipopolysaccharide [CPD:C00338]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            lipopolysaccharide [CPD:C00338]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. Enzymes of
            Gram-negative bacteria that export lipo-oligosaccharides and
            lipopolysaccharides.
REFERENCE   1  [PMID:8302219]
  AUTHORS   Fath MJ, Kolter R.
  TITLE     ABC transporters: bacterial exporters.
  JOURNAL   Microbiol. Rev. 57 (1993) 995-1017.
  ORGANISM  Rhizobium leguminosarum [GN:rle], Bradyrhizobium japonicum [GN:bja]
REFERENCE   2  [PMID:8809752]
  AUTHORS   Fernandez-Lopez M, D'Haeze W, Mergaert P, Verplancke C, Prome JC,
            Van Montagu M, Holsters M.
  TITLE     Role of nodl and nodJ in lipo-chitooligosaccharide secretion in
            Azorhizobium caulinodans and Escherichia coli.
  JOURNAL   Mol. Microbiol. 20 (1996) 993-1000.
  ORGANISM  Azorhizobium caulinodans, Escherichia coli [GN:eco]
REFERENCE   3  [PMID:9274022]
  AUTHORS   Paulsen IT, Beness AM, Saier MH Jr.
  TITLE     Computer-based analyses of the protein constituents of transport
            systems catalysing export of complex carbohydrates in bacteria.
  JOURNAL   Microbiology. 143 ( Pt 8) (1997) 2685-99.
REFERENCE   4  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.39
            ExPASy - ENZYME nomenclature database: 3.6.3.39
            ExplorEnz - The Enzyme Database: 3.6.3.39
            ERGO genome analysis and discovery system: 3.6.3.39
            BRENDA, the Enzyme Database: 3.6.3.39
///
ENTRY       EC 3.6.3.40                 Enzyme
NAME        teichoic-acid-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (teichoic-acid-exporting)
REACTION    ATP + H2O + teichoic acidin = ADP + phosphate + teichoic acidout
            [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            teichoic acid [CPD:C06707]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            teichoic acid [CPD:C06707]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. An enzyme found in
            Gram-positive bacteria that exports teichoic acid.
REFERENCE   1  [PMID:8302219]
  AUTHORS   Fath MJ, Kolter R.
  TITLE     ABC transporters: bacterial exporters.
  JOURNAL   Microbiol. Rev. 57 (1993) 995-1017.
REFERENCE   2  [PMID:7565096]
  AUTHORS   Lazarevic V, Karamata D.
  TITLE     The tagGH operon of Bacillus subtilis 168 encodes a two-component
            ABC transporter involved in the metabolism of two wall teichoic
            acids.
  JOURNAL   Mol. Microbiol. 16 (1995) 345-55.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   3  [PMID:9274022]
  AUTHORS   Paulsen IT, Beness AM, Saier MH Jr.
  TITLE     Computer-based analyses of the protein constituents of transport
            systems catalysing export of complex carbohydrates in bacteria.
  JOURNAL   Microbiology. 143 ( Pt 8) (1997) 2685-99.
REFERENCE   4
  AUTHORS   Griffiths, J.K. and Sansom, C.E.
  TITLE     The Transporter Factsbook, Academic Press, San Diego, 1998.
PATHWAY     PATH: map02010  ABC transporters - General
ORTHOLOGY   KO: K09693  teichoic acid transport system ATP-binding protein
GENES       NOC: Noc_0731 Noc_2181
            BUR: Bcep18194_A3976
            BSU: BG11191(tagH)
            BHA: BH3659(tagH)
            BAN: BA5510
            BAR: GBAA5510
            BAA: BA_0359
            BAT: BAS5118
            BCZ: BCZK4965(tagH)
            BLI: BL02460(tagH)
            BLD: BLi03814(tagH)
            BCL: ABC3365
            BAY: RBAM_032830(tagH)
            OIH: OB2923
            SAU: SA0593(tagH) SA1688
            SAV: SAV0637(tagH) SAV1871(tagH)
            SAM: MW0599(tagH) MW1811
            SAR: SAR0647(tagH) SAR1961
            SAS: SAS0603 SAS1793
            SAC: SACOL0694 SACOL1929
            SAB: SAB0587c(tagH) SAB1804c
            SAA: SAUSA300_0624(tagH) SAUSA300_1852
            SAO: SAOUHSC_00641 SAOUHSC_02009
            SAE: NWMN_0607(tagH)
            SEP: SE0411 SE1555
            SER: SERP0296 SERP1409
            SHA: SH1089(tagH) SH2259(tagH)
            SSP: SSP0922 SSP2082
            LMO: lmo1075
            LMF: LMOf2365_1092
            LIN: lin1063
            LWE: lwe1053(tagH)
            LLA: L137446(tagH)
            LLM: llmg_1623(tagH)
            LPL: lp_0344(tagH)
            LSL: LSL_0373(tagH)
            LBR: LVIS_0694
            PPE: PEPE_1606
            EFA: EF2486
            CPE: CPE0270
            CPF: CPF_0264
            CPR: CPR_0255
            SMA: SAV5080(tagH)
            AVA: Ava_3347
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.40
            ExPASy - ENZYME nomenclature database: 3.6.3.40
            ExplorEnz - The Enzyme Database: 3.6.3.40
            ERGO genome analysis and discovery system: 3.6.3.40
            BRENDA, the Enzyme Database: 3.6.3.40
///
ENTRY       EC 3.6.3.41                 Enzyme
NAME        heme-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (heme-exporting)
REACTION    ATP + H2O + hemein = ADP + phosphate + hemeout [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            heme [CPD:C00032]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            heme [CPD:C00032]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. An enzyme found in
            Gram-negative bacteria that exports heme.
REFERENCE   1  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   2  [PMID:7862087]
  AUTHORS   Jekabsons W, Schuster W.
  TITLE     orf250 encodes a second subunit of an ABC-type heme transporter in
            Oenothera mitochondria.
  JOURNAL   Mol. Gen. Genet. 246 (1995) 166-73.
  ORGANISM  Bradyrhizobium japonicum [GN:bja], Escherichia coli [GN:eco],
            Marchantia polymorpha, Daucus carota, Arabidopsis thaliana [GN:ath]
REFERENCE   3  [PMID:1850420]
  AUTHORS   Ramseier TM, Winteler HV, Hennecke H.
  TITLE     Discovery and sequence analysis of bacterial genes involved in the
            biogenesis of c-type cytochromes.
  JOURNAL   J. Biol. Chem. 266 (1991) 7793-803.
  ORGANISM  Bradyrhizobium japonicum [GN:bja]
PATHWAY     PATH: map02010  ABC transporters - General
ORTHOLOGY   KO: K02193  heme exporter ATP-binding protein CcmA
GENES       TET: TTHERM_00313120 TTHERM_00532790 TTHERM_00693290
                 TTHERM_00693300 TTHERM_00694300 TTHERM_00694310
                 TTHERM_00898300 TTHERM_01014620 TTHERM_01417320
            ECO: b2201(ccmA)
            ECJ: JW5366(ccmA)
            ECE: Z3458(ccmA)
            ECS: ECs3090
            ECC: c2738(ccmA)
            ECI: UTI89_C2479(ccmA)
            ECP: ECP_2242
            ECV: APECO1_4358(ccmA)
            STY: STY2480(ccmA1) STY3959(ccmA2)
            STT: t0610(ccmA) t3699(ccmA)
            SPT: SPA0610(ccmA) SPA3669(ccmA)
            SEC: SC2259(ccmA) SC3737(ccmA)
            STM: STM2254(ccmA) STM3819(ccmA)
            YPE: YPO2734(ccmA)
            YPK: y1567(ccmA)
            YPM: YP_2430(ccmA3)
            YPA: YPA_2110
            YPN: YPN_2213
            YPS: YPTB2649(ccmA)
            YEN: YE1263(ccmA)
            SFL: SF2285(ccmA)
            SFX: S2415(ccmA)
            SFV: SFV_2277(ccmA)
            SSN: SSON_2259(ccmA)
            SBO: SBO_2106(ccmA)
            SDY: SDY_0877(ccmA)
            ECA: ECA1882(ccmA)
            SGL: SG1637
            HIN: HI1089(ccmA)
            HIT: NTHI1253(ccmA)
            HDU: HD0786(ccmA)
            HSO: HS_0393(ccmA)
            PMU: PM0005(ccmA)
            MSU: MS0601(ccmA)
            APL: APL_1372(ccmA)
            XFA: XF2455
            XFT: PD1475(ccmA)
            XCC: XCC2219(ccmA)
            XCB: XC_1898
            XCV: XCV2522(ccmA)
            XAC: XAC2323(ccmA)
            XOO: XOO2155(ccmA)
            XOM: XOO_2024(XOO2024)
            VCH: VC2057
            VVU: VV1_1961
            VVY: VV2455
            VPA: VP2223
            VFI: VF1824
            PPR: PBPRA0948
            PAE: PA1475(ccmA)
            PAU: PA14_45380(ccmA)
            PPU: PP_4327(ccmA)
            PST: PSPTO_3635(ccmA)
            PSB: Psyr_3393(ccmA)
            PSP: PSPPH_3314(ccmA)
            PFL: PFL_1680
            PFO: Pfl_1577(ccmA)
            PEN: PSEEN3782(ccmA)
            PAR: Psyc_1829(ccmA)
            PCR: Pcryo_2113
            SON: SO_0263(ccmA)
            SDN: Sden_3569
            SFR: Sfri_0179
            SAZ: Sama_0245
            SBL: Sbal_0228
            SLO: Shew_0190
            SHE: Shewmr4_0231
            SHM: Shewmr7_0226
            SHN: Shewana3_0231
            SHW: Sputw3181_0188
            ILO: IL1106(ccmA)
            CPS: CPS_1034(ccmA)
            PAT: Patl_3256
            SDE: Sde_1866
            PIN: Ping_3024
            MAQ: Maqu_1960
            LPN: lpg0856(ccmA)
            LPF: lpl0887(ccmA)
            LPP: lpp0918(ccmA)
            MCA: MCA0954(ccmA)
            NOC: Noc_0948 Noc_1687
            AEH: Mlg_1683
            HHA: Hhal_1364
            HCH: HCH_04369(ccmA)
            ABO: ABO_0870(ccmA)
            AHA: AHA_1393(ccmA)
            RMA: Rmag_0736
            VOK: COSY_0681(ccmA)
            REU: Reut_B4766(ccmA)
            REH: H16_B0952(ccmA2)
            RME: Rmet_2385 Rmet_4060
            BXE: Bxe_C0370
            BUR: Bcep18194_A4785 Bcep18194_A5068 Bcep18194_A5785
                 Bcep18194_A6267 Bcep18194_C7226 Bcep18194_C7259
            BPA: BPP2699(ccmA)
            BBR: BB2803(ccmA)
            RFR: Rfer_0045
            PNA: Pnap_0589
            MPT: Mpe_A1215
            HAR: HEAR1373(cydC)
            NEU: NE0764(ccmA)
            NET: Neut_0063 Neut_1643
            NMU: Nmul_A1217(ccmA)
            EBA: ebA3514(ccmA)
            AZO: azo3936(ccmA)
            DAR: Daro_3991(ccmA)
            DVU: DVU1049
            DDE: Dde_1476
            LIP: LI0955(ccmA)
            RPR: RP794(ccmA)
            RTY: RT0781(ccmA)
            RCO: RC1228(ccmA)
            RFE: RF_1259(ccmA)
            RBE: RBE_0089(ccmA)
            WOL: WD0411(ccmA)
            WBM: Wbm0014
            AMA: AM144(ccmA)
            APH: APH_0125(ccmA)
            ERU: Erum7050(ccmA)
            ERW: ERWE_CDS_07400(ccmA)
            ERG: ERGA_CDS_07320(ccmA)
            ECN: Ecaj_0708
            ECH: ECH_0295
            MLO: mll4333
            MES: Meso_3358
            SME: SMc03847(ccmA)
            ATU: Atu2686(ccmA)
            ATC: AGR_C_4868
            RET: RHE_CH03945(ccmA)
            RLE: RL4537(ccmA)
            BME: BMEI1853
            BMF: BAB1_0091(ccmA)
            BMS: BR0094(ccmA)
            BMB: BruAb1_0091(ccmA)
            BJA: blr0467(ccmA)
            BRA: BRADO0392(ccmA)
            BBT: BBta_0381(ccmA)
            RPA: RPA0203(cycV)
            RPB: RPB_0292(ccmA)
            RPC: RPC_0205
            RPD: RPD_0524
            RPE: RPE_0311
            NWI: Nwi_0322(ccmA) Nwi_2153
            NHA: Nham_0409
            BHE: BH01150(ccmA)
            BQU: BQ01080(ccmA)
            CCR: CC_3668
            SIL: SPO2317(ccmA)
            SIT: TM1040_0999
            RSP: RSP_1801(ccmA)
            JAN: Jann_2647
            RDE: RD1_2547(ccmA) RD1_3149
            MMR: Mmar10_2860
            HNE: HNE_3515(ccmA)
            ZMO: ZMO0260(cycV)
            NAR: Saro_1119
            SAL: Sala_1822
            ELI: ELI_01700
            GOX: GOX1571
            GBE: GbCGDNIH1_0405
            RRU: Rru_A0040 Rru_A0047 Rru_A0117 Rru_A0878 Rru_A1013 Rru_A1527
            MAG: amb4180
            FAL: FRAAL0794(braG)
            AVA: Ava_1617 Ava_1622
            DRA: DR_0406
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.41
            ExPASy - ENZYME nomenclature database: 3.6.3.41
            ExplorEnz - The Enzyme Database: 3.6.3.41
            ERGO genome analysis and discovery system: 3.6.3.41
            BRENDA, the Enzyme Database: 3.6.3.41
///
ENTRY       EC 3.6.3.42                 Enzyme
NAME        beta-glucan-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (beta-glucan-exporting)
REACTION    ATP + H2O + beta-glucanin = ADP + phosphate + beta-glucanout
            [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            beta-glucan [CPD:C00551]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            beta-glucan [CPD:C00551]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. An enzyme found in
            Gram-negative bacteria that exports beta-glucan.
REFERENCE   1  [PMID:8302219]
  AUTHORS   Fath MJ, Kolter R.
  TITLE     ABC transporters: bacterial exporters.
  JOURNAL   Microbiol. Rev. 57 (1993) 995-1017.
  ORGANISM  Rhizobium meliloti, Agrobacterium tumefaciens
REFERENCE   2  [PMID:8544814]
  AUTHORS   Becker A, Kuster H, Niehaus K, Puhler A.
  TITLE     Extension of the Rhizobium meliloti succinoglycan biosynthesis gene
            cluster: identification of the exsA gene encoding an ABC transporter
            protein, and the exsB gene which probably codes for a regulator of
            succinoglycan biosynthesis.
  JOURNAL   Mol. Gen. Genet. 249 (1995) 487-97.
  ORGANISM  Rhizobium meliloti
REFERENCE   3  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
REFERENCE   4
  AUTHORS   Griffiths, J.K. and Sansom, C.E.
  TITLE     The Transporter Factsbook, Academic Press, San Diego, 1998.
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.42
            ExPASy - ENZYME nomenclature database: 3.6.3.42
            ExplorEnz - The Enzyme Database: 3.6.3.42
            ERGO genome analysis and discovery system: 3.6.3.42
            BRENDA, the Enzyme Database: 3.6.3.42
///
ENTRY       EC 3.6.3.43                 Enzyme
NAME        peptide-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (peptide-exporting)
REACTION    ATP + H2O + peptidein = ADP + phosphate + peptideout [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            peptide [CPD:C00012]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            peptide [CPD:C00012]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A family of enzymes
            that exports alpha-hemolysin, cyclolysin, colicin V and siderophores
            from Gram-negative bacteria, and bacteriocin, subtilin, competence
            factor and pediocin from Gram-positive bacteria.
REFERENCE   1  [PMID:8085823]
  AUTHORS   Klein C, Entian KD.
  TITLE     Genes involved in self-protection against the lantibiotic subtilin
            produced by Bacillus subtilis ATCC 6633.
  JOURNAL   Appl. Environ. Microbiol. 60 (1994) 2793-801.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   2  [PMID:8107849]
  AUTHORS   Momburg F, Roelse J, Howard JC, Butcher GW, Hammerling GJ, Neefjes
            JJ.
  TITLE     Selectivity of MHC-encoded peptide transporters from human, mouse
            and rat.
  JOURNAL   Nature. 367 (1994) 648-51.
  ORGANISM  human [GN:hsa], mouse [GN:mmu], rat [GN:rno]
REFERENCE   3  [PMID:9224868]
  AUTHORS   Binet R, Letoffe S, Ghigo JM, Delepelaire P, Wandersman C.
  TITLE     Protein secretion by Gram-negative bacterial ABC exporters--a
            review.
  JOURNAL   Gene. 192 (1997) 7-11.
  ORGANISM  Erwinia chrysanthemi
GENES       CHA: CHAB381_1446
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.43
            ExPASy - ENZYME nomenclature database: 3.6.3.43
            ExplorEnz - The Enzyme Database: 3.6.3.43
            ERGO genome analysis and discovery system: 3.6.3.43
            BRENDA, the Enzyme Database: 3.6.3.43
///
ENTRY       EC 3.6.3.44                 Enzyme
NAME        xenobiotic-transporting ATPase;
            multidrug-resistance protein;
            MDR protein;
            P-glycoprotein;
            pleiotropic-drug-resistance protein;
            PDR protein;
            steroid-transporting ATPase;
            ATP phosphohydrolase (steroid-exporting)
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (xenobiotic-exporting)
REACTION    ATP + H2O + xenobioticin = ADP + phosphate + xenobioticout
            [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            xenobiotic [CPD:C06708]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            xenobiotic [CPD:C06708]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterized by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. The enzyme from
            Gram-positive bacteria and eukaryotic cells export a number of
            drugs, with unusual specificity, covering various groups of
            unrelated substances, while ignoring some that are closely related
            structurally. Several distinct enzymes may be present in a single
            eukaryotic cell. Many of them transport glutathione---drug
            conjugates. Some also show some 'flippase'
            (phospholipid-translocating ATPase; EC 3.6.3.1) activity.
REFERENCE   1  [PMID:8725386]
  AUTHORS   Bellamy WT.
  TITLE     P-glycoproteins and multidrug resistance.
  JOURNAL   Annu. Rev. Pharmacol. Toxicol. 36 (1996) 161-83.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:8869755]
  AUTHORS   Frijters CM, Ottenhoff R, Van Wijland MJ, Van Nieuwkerk C, Groen AK,
            Oude Elferink RP.
  TITLE     Influence of bile salts on hepatic mdr2 P-glycoprotein expression.
  JOURNAL   Adv. Enzyme. Regul. 36 (1996) 351-63.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:9381978]
  AUTHORS   Keppler D, Konig J, Buchler M.
  TITLE     The canalicular multidrug resistance protein, cMRP/MRP2, a novel
            conjugate export pump expressed in the apical membrane of
            hepatocytes.
  JOURNAL   Adv. Enzyme. Regul. 37 (1997) 321-33.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:9823323]
  AUTHORS   Loe DW, Deeley RG, Cole SP.
  TITLE     Characterization of vincristine transport by the M(r) 190,000
            multidrug resistance protein (MRP): evidence for cotransport with
            reduced glutathione.
  JOURNAL   Cancer. Res. 58 (1998) 5130-6.
REFERENCE   5  [PMID:9693718]
  AUTHORS   van Veen HW, Konings WN.
  TITLE     The ABC family of multidrug transporters in microorganisms.
  JOURNAL   Biochim. Biophys. Acta. 1365 (1998) 31-6.
  ORGANISM  human [GN:hsa]
REFERENCE   6
  AUTHORS   Griffiths, J.K. and Sansom, C.E.
  TITLE     The Transporter Factsbook, Academic Press, San Diego, 1998.
REFERENCE   7  [PMID:7614555]
  AUTHORS   Prasad R, De Wergifosse P, Goffeau A, Balzi E.
  TITLE     Molecular cloning and characterization of a novel gene of Candida
            albicans, CDR1, conferring multiple resistance to drugs and
            antifungals.
  JOURNAL   Curr. Genet. 27 (1995) 320-9.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   8  [PMID:7883711]
  AUTHORS   Nagao K, Taguchi Y, Arioka M, Kadokura H, Takatsuki A, Yoda K,
            Yamasaki M.
  TITLE     bfr1+, a novel gene of Schizosaccharomyces pombe which confers
            brefeldin A resistance, is structurally related to the ATP-binding
            cassette superfamily.
  JOURNAL   J. Bacteriol. 177 (1995) 1536-43.
  ORGANISM  Schizosaccharomyces pombe [GN:spo]
REFERENCE   9  [PMID:8810273]
  AUTHORS   Mahe Y, Lemoine Y, Kuchler K.
  TITLE     The ATP binding cassette transporters Pdr5 and Snq2 of Saccharomyces
            cerevisiae can mediate transport of steroids in vivo.
  JOURNAL   J. Biol. Chem. 271 (1996) 25167-72.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
GENES       DME: Dmel_CG6214(MRP)
            ECW: EcE24377A_0484(mdlA) EcE24377A_0485(mdlB)
            ECX: EcHS_A0525 EcHS_A0526
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.44
            ExPASy - ENZYME nomenclature database: 3.6.3.44
            ExplorEnz - The Enzyme Database: 3.6.3.44
            ERGO genome analysis and discovery system: 3.6.3.44
            BRENDA, the Enzyme Database: 3.6.3.44
///
ENTRY       EC 3.6.3.45       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
COMMENT     Deleted entry: steroid-transporting ATPase. Now included with EC
            3.6.3.44, xenobiotic-transporting ATPase (EC 3.6.3.45 created 2000,
            deleted 2006)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.45
            ExPASy - ENZYME nomenclature database: 3.6.3.45
            ExplorEnz - The Enzyme Database: 3.6.3.45
            ERGO genome analysis and discovery system: 3.6.3.45
            BRENDA, the Enzyme Database: 3.6.3.45
///
ENTRY       EC 3.6.3.46                 Enzyme
NAME        cadmium-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (heavy-metal-exporting)
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A yeast enzyme that
            exports some heavy metals, especially Cd2+, from the cytosol into
            the vacuole.
REFERENCE   1  [PMID:8626454]
  AUTHORS   Li ZS, Szczypka M, Lu YP, Thiele DJ, Rea PA.
  TITLE     The yeast cadmium factor protein (YCF1) is a vacuolar glutathione
            S-conjugate pump.
  JOURNAL   J. Biol. Chem. 271 (1996) 6509-17.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.46
            ExPASy - ENZYME nomenclature database: 3.6.3.46
            ExplorEnz - The Enzyme Database: 3.6.3.46
            ERGO genome analysis and discovery system: 3.6.3.46
            BRENDA, the Enzyme Database: 3.6.3.46
///
ENTRY       EC 3.6.3.47                 Enzyme
NAME        fatty-acyl-CoA-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (fatty-acyl-CoA-transporting)
REACTION    ATP + H2O + fatty acyl CoAcis = ADP + phosphate + fatty acyl
            CoAtrans [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            fatty acyl CoAcis
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            fatty acyl CoAtrans
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. An animal and yeast
            enzyme that transports fatty acyl CoA into and out of peroxisomes.
            In humans, it is associated with Zellweger's syndrome.
REFERENCE   1  [PMID:1968461]
  AUTHORS   Kamijo K, Taketani S, Yokota S, Osumi T, Hashimoto T.
  TITLE     The 70-kDa peroxisomal membrane protein is a member of the Mdr
            (P-glycoprotein)-related ATP-binding protein superfamily.
  JOURNAL   J. Biol. Chem. 265 (1990) 4534-40.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:8670886]
  AUTHORS   Hettema EH, van Roermund CW, Distel B, van den Berg M, Vilela C,
            Rodrigues-Pousada C, Wanders RJ, Tabak HF.
  TITLE     The ABC transporter proteins Pat1 and Pat2 are required for import
            of long-chain fatty acids into peroxisomes of Saccharomyces
            cerevisiae.
  JOURNAL   EMBO. J. 15 (1996) 3813-22.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.47
            ExPASy - ENZYME nomenclature database: 3.6.3.47
            ExplorEnz - The Enzyme Database: 3.6.3.47
            ERGO genome analysis and discovery system: 3.6.3.47
            BRENDA, the Enzyme Database: 3.6.3.47
///
ENTRY       EC 3.6.3.48                 Enzyme
NAME        alpha-factor-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (alpha-factor-transporting)
REACTION    ATP + H2O + alpha-factorin = ADP + phosphate + alpha-factorout
            [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            alpha-factor [CPD:C06766]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            alpha-factor [CPD:C06766]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. A yeast enzyme that
            exports the alpha-factor sex pheromone.
REFERENCE   1  [PMID:8095825]
  AUTHORS   Michaelis S.
  TITLE     STE6, the yeast a-factor transporter.
  JOURNAL   Semin. Cell. Biol. 4 (1993) 17-27.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:9889977]
  AUTHORS   Saier MH Jr.
  TITLE     Molecular phylogeny as a basis for the classification of transport
            proteins from bacteria, archaea and eukarya.
  JOURNAL   Adv. Microb. Physiol. 40 (1998) 81-136.
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.48
            ExPASy - ENZYME nomenclature database: 3.6.3.48
            ExplorEnz - The Enzyme Database: 3.6.3.48
            ERGO genome analysis and discovery system: 3.6.3.48
            BRENDA, the Enzyme Database: 3.6.3.48
///
ENTRY       EC 3.6.3.49                 Enzyme
NAME        channel-conductance-controlling ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (channel-conductance-controlling)
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     ABC-type (ATP-binding cassette-type) ATPase, characterised by the
            presence of two similar ATP-binding domains. Does not undergo
            phosphorylation during the transport process. An animal enzyme that
            is active in forming a chloride channel, the absence of which brings
            about cystic fibrosis. It is also involved in the functioning of
            other transmembrane channels.
REFERENCE   1  [PMID:9147660]
  AUTHORS   Chen M, Zhang JT.
  TITLE     Membrane insertion, processing, and topology of cystic fibrosis
            transmembrane conductance regulator (CFTR) in microsomal membranes.
  JOURNAL   Mol. Membr. Biol. 13 (1996) 33-40.
  ORGANISM  human [GN:hsa], rabbit
REFERENCE   2  [PMID:9013845]
  AUTHORS   Tusnady GE, Bakos E, Varadi A, Sarkadi B.
  TITLE     Membrane topology distinguishes a subfamily of the ATP-binding
            cassette (ABC) transporters.
  JOURNAL   FEBS. Lett. 402 (1997) 1-3.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:9922375]
  AUTHORS   Sheppard DN, Welsh MJ.
  TITLE     Structure and function of the CFTR chloride channel.
  JOURNAL   Physiol. Rev. 79 (1999) S23-45.
  ORGANISM  human [GN:hsa]
STRUCTURES  PDB: 1XMI  1XMJ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.49
            ExPASy - ENZYME nomenclature database: 3.6.3.49
            ExplorEnz - The Enzyme Database: 3.6.3.49
            ERGO genome analysis and discovery system: 3.6.3.49
            BRENDA, the Enzyme Database: 3.6.3.49
///
ENTRY       EC 3.6.3.50                 Enzyme
NAME        protein-secreting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (protein-secreting)
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is
            involved in protein transport. There are several families of enzymes
            included here, e.g. ATP-hydrolysing enzymes of the general secretory
            pathway (Sec or Type II), of the virulence-related secretory pathway
            (Type III) and of the conjugal DNA-protein transfer pathway (Type
            IV). Type II enzymes occur in bacteria, archaea and eucarya, whereas
            type III and type IV enzymes occur in bacteria where they form
            components of a multi-subunit complex.
REFERENCE   1  [PMID:8022262]
  AUTHORS   Saier MH Jr, Tam R, Reizer A, Reizer J.
  TITLE     Two novel families of bacterial membrane proteins concerned with
            nodulation, cell division and transport.
  JOURNAL   Mol. Microbiol. 11 (1994) 841-7.
REFERENCE   2  [PMID:8969244]
  AUTHORS   Mecsas JJ, Strauss EJ.
  TITLE     Molecular mechanisms of bacterial virulence: type III secretion and
            pathogenicity islands.
  JOURNAL   Emerg. Infect. Dis. 2 (1996) 270-88.
REFERENCE   3  [PMID:9084158]
  AUTHORS   Thomas JD, Reeves PJ, Salmond GP.
  TITLE     The general secretion pathway of Erwinia carotovora subsp.
            carotovora: analysis of the membrane topology of OutC and OutF.
  JOURNAL   Microbiology. 143 ( Pt 3) (1997) 713-20.
  ORGANISM  Erwinia carotovora [GN:eca]
REFERENCE   4  [PMID:9115193]
  AUTHORS   Baker B, Zambryski P, Staskawicz B, Dinesh-Kumar SP.
  TITLE     Signaling in plant-microbe interactions.
  JOURNAL   Science. 276 (1997) 726-33.
REFERENCE   5  [PMID:9680212]
  AUTHORS   Martinez A, Ostrovsky P, Nunn DN.
  TITLE     Identification of an additional member of the secretin superfamily
            of proteins in Pseudomonas aeruginosa that is able to function in
            type II protein secretion.
  JOURNAL   Mol. Microbiol. 28 (1998) 1235-46.
  ORGANISM  Pseudomonas aeruginosa
REFERENCE   6  [PMID:10085046]
  AUTHORS   Schuch R, Maurelli AT.
  TITLE     The mxi-Spa type III secretory pathway of Shigella flexneri requires
            an outer membrane lipoprotein, MxiM, for invasin translocation.
  JOURNAL   Infect. Immun. 67 (1999) 1982-91.
  ORGANISM  Shigella flexneri
GENES       REH: H16_A0776 H16_A2684(sunT)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.50
            ExPASy - ENZYME nomenclature database: 3.6.3.50
            ExplorEnz - The Enzyme Database: 3.6.3.50
            ERGO genome analysis and discovery system: 3.6.3.50
            BRENDA, the Enzyme Database: 3.6.3.50
///
ENTRY       EC 3.6.3.51                 Enzyme
NAME        mitochondrial protein-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (mitochondrial protein-importing)
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase involved
            in the transport of proteins or preproteins into mitochondria using
            the TIM protein complex. (TIM is the protein transport machinery of
            the inner mitochondrial membrane that contains three essential Tim
            proteins: Tim17 and Tim23 are thought to build a preprotein
            translocation channel while Tim44 interacts transiently with the
            matrix heat-shock protein Hsp70 to form an ATP-driven import motor.)
REFERENCE   1  [PMID:9171336]
  AUTHORS   Bomer U, Meijer M, Maarse AC, Honlinger A, Dekker PJ, Pfanner N,
            Rassow J.
  TITLE     Multiple interactions of components mediating preprotein
            translocation across the inner mitochondrial membrane.
  JOURNAL   EMBO. J. 16 (1997) 2205-16.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:7600576]
  AUTHORS   Berthold J, Bauer MF, Schneider HC, Klaus C, Dietmeier K, Neupert W,
            Brunner M.
  TITLE     The MIM complex mediates preprotein translocation across the
            mitochondrial inner membrane and couples it to the mt-Hsp70/ATP
            driving system.
  JOURNAL   Cell. 81 (1995) 1085-93.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:10548718]
  AUTHORS   Voos W, Martin H, Krimmer T, Pfanner N.
  TITLE     Mechanisms of protein translocation into mitochondria.
  JOURNAL   Biochim. Biophys. Acta. 1422 (1999) 235-54.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], Caenorhabditis elegans [GN:cel]
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.51
            ExPASy - ENZYME nomenclature database: 3.6.3.51
            ExplorEnz - The Enzyme Database: 3.6.3.51
            ERGO genome analysis and discovery system: 3.6.3.51
            BRENDA, the Enzyme Database: 3.6.3.51
///
ENTRY       EC 3.6.3.52                 Enzyme
NAME        chloroplast protein-transporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (chloroplast protein-importing)
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is
            involved in protein transport. Involved in the transport of proteins
            or preproteins into chloroplast stroma (several ATPases may
            participate in this process).
REFERENCE   1  [PMID:1733965]
  AUTHORS   Cline K, Ettinger WF, Theg SM.
  TITLE     Protein-specific energy requirements for protein transport across or
            into thylakoid membranes. Two lumenal proteins are transported in
            the absence of ATP.
  JOURNAL   J. Biol. Chem. 267 (1992) 2688-96.
REFERENCE   2  [PMID:7989297]
  AUTHORS   Nakai M, Goto A, Nohara T, Sugita D, Endo T.
  TITLE     Identification of the SecA protein homolog in pea chloroplasts and
            its possible involvement in thylakoidal protein transport.
  JOURNAL   J. Biol. Chem. 269 (1994) 31338-41.
  ORGANISM  Pisum sativum
REFERENCE   3  [PMID:8567731]
  AUTHORS   Scott SV, Theg SM.
  TITLE     A new chloroplast protein import intermediate reveals distinct
            translocation machineries in the two envelope membranes: energetics
            and mechanistic implications.
  JOURNAL   J. Cell. Biol. 132 (1996) 63-75.
  ORGANISM  Pisum sativum
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.52
            ExPASy - ENZYME nomenclature database: 3.6.3.52
            ExplorEnz - The Enzyme Database: 3.6.3.52
            ERGO genome analysis and discovery system: 3.6.3.52
            BRENDA, the Enzyme Database: 3.6.3.52
///
ENTRY       EC 3.6.3.53                 Enzyme
NAME        Ag+-exporting ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to catalyse transmembrane movement of
            substances
SYSNAME     ATP phosphohydrolase (Ag+-exporting)
REACTION    ATP + H2O + Ag+in = ADP + phosphate + Ag+out [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001];
            Ag+ [CPD:C06710]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            Ag+ [CPD:C06710]
COMMENT     A P-type ATPase that exports Ag+ ions from pathogenic microorganisms
            as well as from some animal tissues.
REFERENCE   1  [PMID:9930866]
  AUTHORS   Gupta A, Matsui K, Lo JF, Silver S.
  TITLE     Molecular basis for resistance to silver cations in Salmonella.
  JOURNAL   Nat. Med. 5 (1999) 183-8.
  ORGANISM  Salmonella sp.
REFERENCE   2  [PMID:10448119]
  AUTHORS   Bury NR, Grosell M, Grover AK, Wood CM.
  TITLE     ATP-dependent silver transport across the basolateral membrane of
            rainbow trout gills.
  JOURNAL   Toxicol. Appl. Pharmacol. 159 (1999) 1-8.
  ORGANISM  Oncorhynchus mykiss
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.3.53
            ExPASy - ENZYME nomenclature database: 3.6.3.53
            ExplorEnz - The Enzyme Database: 3.6.3.53
            ERGO genome analysis and discovery system: 3.6.3.53
            BRENDA, the Enzyme Database: 3.6.3.53
///
ENTRY       EC 3.6.4.1                  Enzyme
NAME        myosin ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to facilitate cellular and subcellular
            movement
SYSNAME     ATP phosphohydrolase (actin-translocating)
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COFACTOR    Calcium [CPD:C00076]
COMMENT     Proteins of the contractile apparatus of muscle and nonmuscle cells;
            myosin molecule consists of two heavy chains (about 200 kDa) and two
            pairs of light chains (15-27 kDa). The head region of the heavy
            chain contains actin- and ATP-binding sites. ATP hydrolysis provides
            energy for actomyosin contraction.
REFERENCE   1  [PMID:8663496]
  AUTHORS   Rayment I.
  TITLE     The structural basis of the myosin ATPase activity.
  JOURNAL   J. Biol. Chem. 271 (1996) 15850-3.
  ORGANISM  Dictyostelium discoideum [GN:ddi]
REFERENCE   2  [PMID:8690736]
  AUTHORS   Hasson T, Mooseker MS.
  TITLE     Vertebrate unconventional myosins.
  JOURNAL   J. Biol. Chem. 271 (1996) 16431-4.
REFERENCE   3  [PMID:10090768]
  AUTHORS   Murphy CT, Spudich JA.
  TITLE     The sequence of the myosin 50-20K loop affects Myosin's affinity for
            actin throughout the actin-myosin ATPase cycle and its maximum
            ATPase activity.
  JOURNAL   Biochemistry. 38 (1999) 3785-92.
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01553  myosin ATPase
GENES       PIC: PICST_30460(SMC5) PICST_31021(RHC18) PICST_53629(RAD50)
                 PICST_75361(MYO2)
            CAL: CaO19_3100(CaO19.3100)
            PFA: MAL13P1.148 PF11_0416 PFL1435c
            HPA: HPAG1_1080
STRUCTURES  PDB: 1W9I  1W9J  1W9K  1W9L  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.4.1
            ExPASy - ENZYME nomenclature database: 3.6.4.1
            ExplorEnz - The Enzyme Database: 3.6.4.1
            ERGO genome analysis and discovery system: 3.6.4.1
            BRENDA, the Enzyme Database: 3.6.4.1
///
ENTRY       EC 3.6.4.2                  Enzyme
NAME        dynein ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to facilitate cellular and subcellular
            movement
SYSNAME     ATP phosphohydrolase (tubulin-translocating); dynein adenosine
            5'-triphosphatase
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     A multisubunit protein complex associated with microtubules.
            Hydrolysis of ATP provides energy for the movement of organelles
            (endosomes, lysosomes, mitochondria) along microtubules to the
            centrosome towards the microtubule's minus end. It also functions in
            the movement of eukaryotic flagella and cilia. It consists of two
            heavy chains (about 500 kDa), three-four intermediate chains (about
            70 kDa) and four light chains (about 50 kDa).
REFERENCE   1  [PMID:5289252]
  AUTHORS   Summers KE, Gibbons IR.
  TITLE     Adenosine triphosphate-induced sliding of tubules in trypsin-treated
            flagella of sea-urchin sperm.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 68 (1971) 3092-6.
  ORGANISM  Tripneustes gratilla
REFERENCE   2  [PMID:2972702]
  AUTHORS   Gibbons IR.
  TITLE     Dynein ATPases as microtubule motors.
  JOURNAL   J. Biol. Chem. 263 (1988) 15837-40.
REFERENCE   3  [PMID:9760728]
  AUTHORS   Gee M, Vallee R.
  TITLE     The role of the dynein stalk in cytoplasmic and flagellar motility.
  JOURNAL   Eur. Biophys. J. 27 (1998) 466-73.
ORTHOLOGY   KO: K06025  
GENES       PFA: PF10_0196 PF10_0224
            EHI: 6.t00103
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.4.2
            ExPASy - ENZYME nomenclature database: 3.6.4.2
            ExplorEnz - The Enzyme Database: 3.6.4.2
            ERGO genome analysis and discovery system: 3.6.4.2
            BRENDA, the Enzyme Database: 3.6.4.2
///
ENTRY       EC 3.6.4.3                  Enzyme
NAME        microtubule-severing ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to facilitate cellular and subcellular
            movement
SYSNAME     ATP phosphohydrolase (tubulin-dimerizing)
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     Another member of the AAA-ATPase family, active in splitting
            microtubules into tubulin dimers in the centrosome.
REFERENCE   1  [PMID:8221885]
  AUTHORS   McNally FJ, Vale RD.
  TITLE     Identification of katanin, an ATPase that severs and disassembles
            stable microtubules.
  JOURNAL   Cell. 75 (1993) 419-29.
REFERENCE   2  [PMID:9568719]
  AUTHORS   Hartman JJ, Mahr J, McNally K, Okawa K, Iwamatsu A, Thomas S,
            Cheesman S, Heuser J, Vale RD, McNally FJ.
  TITLE     Katanin, a microtubule-severing protein, is a novel AAA ATPase that
            targets to the centrosome using a WD40-containing subunit.
  JOURNAL   Cell. 93 (1998) 277-87.
  ORGANISM  Strongylocentrotus purpuratus [GN:spu]
ORTHOLOGY   KO: K07767  microtubule-severing ATPase
GENES       HSA: 11104(KATNA1) 84056(KATNAL1)
            PTR: 452517(KATNAL1)
            MMU: 231912(Katnal1) 23924(Katna1)
            RNO: 288449(Katnal1) 292464(Katna1)
            CFA: 476240(KATNA1)
            GGA: 418920(KATNAL1) 421626(KATNA1)
            SPU: 373368(katn)
            DME: Dmel_CG10229(katanin-60)
            CEL: T01G9.5(mei-1)
            ATH: AT1G80350(ERH3)
            OSA: 4324404
            TET: TTHERM_00036960 TTHERM_00322760 TTHERM_00414230
                 TTHERM_01014660 TTHERM_01128570
            TBR: Tb11.01.0200
            TCR: 506163.80
            LMA: LmjF28.0400
            SPE: Spro_0483
            ASU: Asuc_1459
            PPF: Pput_4584
            PMY: Pmen_3615
            PRW: PsycPRwf_0535
            SBM: Shew185_3288
            SSE: Ssed_3396
            SPL: Spea_3067
            MMW: Mmwyl1_1020
            GUR: Gura_2734 Gura_3252
            AFW: Anae109_2043 Anae109_2338 Anae109_4390
            PLA: Plav_2126
            SMD: Smed_2623
            OAN: Oant_1223 Oant_4465
            XAU: Xaut_3083
            RSQ: Rsph17025_0566
            ACR: Acry_0366 Acry_1428
            BCY: Bcer98_0060
            SAJ: SaurJH9_0533
            SAH: SaurJH1_0546
            LRE: Lreu_0268
            CBE: Cbei_0100 Cbei_3037 Cbei_4783
            AMT: Amet_3170
            CSC: Csac_1210
            KRA: Krad_0538
            STP: Strop_0254 Strop_4308
            RRS: RoseRS_4361
            RCA: Rcas_0717
            TPT: Tpet_0338
            TME: Tmel_0206
            FNO: Fnod_0159
            MMZ: MmarC7_1176
            MAE: Maeo_0920 Maeo_1033
            MVN: Mevan_1180
            IHO: Igni_0587 Igni_1431
            MSE: Msed_0210 Msed_2237 Msed_2275
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.4.3
            ExPASy - ENZYME nomenclature database: 3.6.4.3
            ExplorEnz - The Enzyme Database: 3.6.4.3
            ERGO genome analysis and discovery system: 3.6.4.3
            BRENDA, the Enzyme Database: 3.6.4.3
///
ENTRY       EC 3.6.4.4                  Enzyme
NAME        plus-end-directed kinesin ATPase;
            kinesin
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to facilitate cellular and subcellular
            movement
SYSNAME     kinesin ATP phosphohydrolase (plus-end-directed)
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     Microtubular motor protein, involved in organelle movement, in
            mitosis and meiosis. In contrast to dynein, it moves along
            microtubules towards the plus end. Composed of two heavy (alpha)
            chains (110 kDa) and two or more light (beta) chains (65-75 kDa).
            Also hydrolyses GTP.
REFERENCE   1  [PMID:3926325]
  AUTHORS   Vale RD, Reese TS, Sheetz MP.
  TITLE     Identification of a novel force-generating protein, kinesin,
            involved in microtubule-based motility.
  JOURNAL   Cell. 42 (1985) 39-50.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:9335494]
  AUTHORS   Howard J.
  TITLE     Molecular motors: structural adaptations to cellular functions.
  JOURNAL   Nature. 389 (1997) 561-7.
REFERENCE   3  [PMID:9275178]
  AUTHORS   Nakagawa T, Tanaka Y, Matsuoka E, Kondo S, Okada Y, Noda Y, Kanai Y,
            Hirokawa N.
  TITLE     Identification and classification of 16 new kinesin superfamily
            (KIF) proteins in mouse genome.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 9654-9.
  ORGANISM  mouse [GN:mmu]
ORTHOLOGY   KO: K06026  
GENES       DME: Dmel_CG10718(neb) Dmel_CG6392(cmet) Dmel_CG8590(Klp3A)
            CGR: CAGL0B03641g
            CHU: CHU_2979
STRUCTURES  PDB: 1GOJ  2IEH  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.4.4
            ExPASy - ENZYME nomenclature database: 3.6.4.4
            ExplorEnz - The Enzyme Database: 3.6.4.4
            ERGO genome analysis and discovery system: 3.6.4.4
            BRENDA, the Enzyme Database: 3.6.4.4
///
ENTRY       EC 3.6.4.5                  Enzyme
NAME        minus-end-directed kinesin ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to facilitate cellular and subcellular
            movement
SYSNAME     kinesin ATP phosphohydrolase (minus-end-directed)
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     Structurally almost identical to EC 3.6.4.3 (microtubule-severing
            ATPase) but the movement it catalyses is towards the minus end of
            microtubules.
REFERENCE   1  [PMID:9288974]
  AUTHORS   Henningsen U, Schliwa M.
  TITLE     Reversal in the direction of movement of a molecular motor.
  JOURNAL   Nature. 389 (1997) 93-6.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2  [PMID:9410876]
  AUTHORS   Sharp DJ, Kuriyama R, Essner R, Baas PW.
  TITLE     Expression of a minus-end-directed motor protein induces Sf9 cells
            to form axon-like processes with uniform microtubule polarity
            orientation.
  JOURNAL   J. Cell. Sci. 110 ( Pt 19) (1997) 2373-80.
REFERENCE   3  [PMID:9796817]
  AUTHORS   Sablin EP, Case RB, Dai SC, Hart CL, Ruby A, Vale RD, Fletterick RJ.
  TITLE     Direction determination in the minus-end-directed kinesin motor ncd.
  JOURNAL   Nature. 395 (1998) 813-6.
GENES       DME: Dmel_CG17461(Kif3C)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.4.5
            ExPASy - ENZYME nomenclature database: 3.6.4.5
            ExplorEnz - The Enzyme Database: 3.6.4.5
            ERGO genome analysis and discovery system: 3.6.4.5
            BRENDA, the Enzyme Database: 3.6.4.5
///
ENTRY       EC 3.6.4.6                  Enzyme
NAME        vesicle-fusing ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to facilitate cellular and subcellular
            movement
SYSNAME     ATP phosphohydrolase (vesicle-fusing)
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     A large family of ATP-hydrolysing enzymes involved in the
            heterotypic fusion of membrane vesicles with target membranes and
            the homotypic fusion of various membrane compartments. They belong
            to the AAA-type (ATPase associated with a variety of cell
            activities) ATPase superfamily. They include peroxin, which
            apparently is involved in Zellweger's syndrome.
REFERENCE   1  [PMID:7646486]
  AUTHORS   Confalonieri F, Duguet M.
  TITLE     A 200-amino acid ATPase module in search of a basic function.
  JOURNAL   Bioessays. 17 (1995) 639-50.
REFERENCE   2  [PMID:9817926]
  AUTHORS   Imamura A, Tamura S, Shimozawa N, Suzuki Y, Zhang Z, Tsukamoto T,
            Orii T, Kondo N, Osumi T, Fujiki Y.
  TITLE     Temperature-sensitive mutation in PEX1 moderates the phenotypes of
            peroxisome deficiency disorders.
  JOURNAL   Hum. Mol. Genet. 7 (1998) 2089-94.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:9606181]
  AUTHORS   Babst M, Wendland B, Estepa EJ, Emr SD.
  TITLE     The Vps4p AAA ATPase regulates membrane association of a Vps protein
            complex required for normal endosome function.
  JOURNAL   EMBO. J. 17 (1998) 2982-93.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K06027  
GENES       HSA: 4905(NSF)
            MMU: 18195(Nsf)
            GGA: 419972(NSF)
            SPU: 373397(LOC373397)
            CEL: H15N14.2(nsf-1)
            OSA: 4339340
            PFA: MAL3P1.10
            CPV: cgd2_3010
            CHO: Chro.20314
            TAN: TA11700
            TPV: TP02_0172
            TET: TTHERM_00160720 TTHERM_00365340 TTHERM_00551090
                 TTHERM_00575450
            TBR: Tb927.1.1560
            TCR: 506477.20 508995.40
            LMA: LmjF20.0810
            EHI: 8.t00066
            YPP: YPDSF_3551
            ENT: Ent638_3612
            SFR: Sfri_0983
            SAZ: Sama_0954
            SBL: Sbal_3246
            SLO: Shew_2834
            SPC: Sputcn32_2841
            SHW: Sputw3181_1063
            PIN: Ping_0811 Ping_1247
            MAQ: Maqu_1017 Maqu_3355 Maqu_3391
            FTL: FTL_1468
            NOC: Noc_1903(ftsH)
            HHA: Hhal_1770
            REU: Reut_A2170(ftsH)
            BVI: Bcep1808_1250 Bcep1808_6311 Bcep1808_7277
            BUR: Bcep18194_A4439(ftsH) Bcep18194_B1520(ftsH)
            PNU: Pnuc_1013
            RFR: Rfer_2418
            POL: Bpro_0723
            PNA: Pnap_0392 Pnap_2611
            AAV: Aave_2617
            AJS: Ajs_1495 Ajs_2383
            GUR: Gura_2842
            PCA: Pcar_0681
            PPD: Ppro_2252
            DVL: Dvul_1787
            DDE: Dde_1513(ftsH) Dde_3415(ftsH)
            OTS: OTBS_2168(ftsH)
            RLE: pRL100036
            BRA: BRADO1274 BRADO4385
            RPC: RPC_3574
            RSH: Rsph17029_2318
            PDE: Pden_0690 Pden_4825
            NAR: Saro_0573
            SAL: Sala_1606
            SUS: Acid_7074
            CTH: Cthe_2253
            DRM: Dred_0126 Dred_1923
            SWO: Swol_1258
            MTA: Moth_1077 Moth_1594
            MVA: Mvan_0749 Mvan_3458 Mvan_5372
            MGI: Mflv_0155 Mflv_1416 Mflv_3069
            MMC: Mmcs_0592 Mmcs_3132
            MKM: Mkms_0605 Mkms_3194 Mkms_4856
            MJL: Mjls_0583 Mjls_3144 Mjls_5156
            RHA: RHA1_ro11077
            ART: Arth_0151 Arth_2173
            NCA: Noca_0444 Noca_2639
            TFU: Tfu_1809
            FRA: Francci3_2630 Francci3_4314(ftsH)
            FAL: FRAAL5516
            ACE: Acel_1184
            SEN: SACE_2246
            BAD: BAD_0546
            RXY: Rxyl_0215 Rxyl_1806
            AVA: Ava_0068 Ava_0575 Ava_1248 Ava_2444(ftsH) Ava_3190 Ava_3503
                 Ava_4767 Ava_B0267 Ava_C0030
            PMN: PMN2A_0293(ftsH) PMN2A_0353(ftsH)
            TER: Tery_2337 Tery_4594
            CCH: Cag_0007(ftsH) Cag_0391(ftsH)
            CPH: Cpha266_0426 Cpha266_2678
            PVI: Cvib_0139 Cvib_1504
            PLT: Plut_0078(ftsH) Plut_0697 Plut_1722(ftsH)
            DGE: Dgeo_1832
            MMQ: MmarC5_1499 MmarC5_1761
            MMZ: MmarC7_0920
            MVN: Mevan_0952
            MBU: Mbur_1677 Mbur_2036 Mbur_2113 Mbur_2301
            MTP: Mthe_0077 Mthe_0458 Mthe_0531 Mthe_0613 Mthe_0721 Mthe_1266
            MHU: Mhun_0817 Mhun_1038 Mhun_1040 Mhun_2451
            MLA: Mlab_1189
            MEM: Memar_1305 Memar_1308 Memar_1561 Memar_2157
            MBN: Mboo_1458 Mboo_1461 Mboo_1596 Mboo_2427
            SMR: Smar_0717 Smar_0914 Smar_1123
            IHO: Igni_0693
            MSE: Msed_0470
            PIS: Pisl_0536 Pisl_0683
            PCL: Pcal_1809 Pcal_2115
            PAS: Pars_1658 Pars_2346
            TPE: Tpen_0304 Tpen_0679
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.4.6
            ExPASy - ENZYME nomenclature database: 3.6.4.6
            ExplorEnz - The Enzyme Database: 3.6.4.6
            ERGO genome analysis and discovery system: 3.6.4.6
            BRENDA, the Enzyme Database: 3.6.4.6
///
ENTRY       EC 3.6.4.7                  Enzyme
NAME        peroxisome-assembly ATPase;
            peroxisome assembly factor-2
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to facilitate cellular and subcellular
            movement
SYSNAME     ATP phosphohydrolase (peroxisome-assembling)
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     An extremely diversified group of enzymes that use the energy of ATP
            hydrolysis to import and assemble peroxisome components into the
            organelle. Their molecular masses range from 25 to 600 kDa.
REFERENCE   1  [PMID:1441755]
  AUTHORS   Lee YJ, Wickner RB.
  TITLE     AFG1, a new member of the SEC18-NSF, PAS1, CDC48-VCP, TBP family of
            ATPases.
  JOURNAL   Yeast. 8 (1992) 787-90.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:7493019]
  AUTHORS   Tsukamoto T, Miura S, Nakai T, Yokota S, Shimozawa N, Suzuki Y, Orii
            T, Fujiki Y, Sakai F, Bogaki A, et al.
  TITLE     Peroxisome assembly factor-2, a putative ATPase cloned by functional
            complementation on a peroxisome-deficient mammalian cell mutant.
  JOURNAL   Nat. Genet. 11 (1995) 395-401.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:8670792]
  AUTHORS   Yahraus T, Braverman N, Dodt G, Kalish JE, Morrell JC, Moser HW,
            Valle D, Gould SJ.
  TITLE     The peroxisome biogenesis disorder group 4 gene, PXAAA1, encodes a
            cytoplasmic ATPase required for stability of the PTS1 receptor.
  JOURNAL   EMBO. J. 15 (1996) 2914-23.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.4.7
            ExPASy - ENZYME nomenclature database: 3.6.4.7
            ExplorEnz - The Enzyme Database: 3.6.4.7
            ERGO genome analysis and discovery system: 3.6.4.7
            BRENDA, the Enzyme Database: 3.6.4.7
///
ENTRY       EC 3.6.4.8                  Enzyme
NAME        proteasome ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to facilitate cellular and subcellular
            movement
SYSNAME     ATP phosphohydrolase (polypeptide-degrading)
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     Belongs to the AAA-type superfamily and, like EC 3.6.4.5
            (minus-end-directed kinesin ATPase), is involved in channel gating
            and polypeptide unfolding before proteolysis in the proteasome. Six
            ATPase subunits are present in the regulatory particle (RP) of 26S
            proteasome.
REFERENCE   1  [PMID:9228289]
  AUTHORS   Rivett AJ, Mason GG, Murray RZ, Reidlinger J.
  TITLE     Regulation of proteasome structure and function.
  JOURNAL   Mol. Biol. Rep. 24 (1997) 99-102.
  ORGANISM  Thermoplasma sp.
REFERENCE   2  [PMID:9688553]
  AUTHORS   Mason GG, Murray RZ, Pappin D, Rivett AJ.
  TITLE     Phosphorylation of ATPase subunits of the 26S proteasome.
  JOURNAL   FEBS. Lett. 430 (1998) 269-74.
  ORGANISM  human [GN:hsa]
GENES       DME: Dmel_CG2241
            PFA: PF11_0314 PFD0665c PFL2345c
            TAN: TA17225
            TPV: TP04_0031
            TBR: Tb10.6k15.0580 Tb10.70.3930 Tb11.02.1220 Tb927.6.1090
                 Tb927.7.2500 Tb927.7.2550
            TCR: 510265.20 510311.70
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.4.8
            ExPASy - ENZYME nomenclature database: 3.6.4.8
            ExplorEnz - The Enzyme Database: 3.6.4.8
            ERGO genome analysis and discovery system: 3.6.4.8
            BRENDA, the Enzyme Database: 3.6.4.8
///
ENTRY       EC 3.6.4.9                  Enzyme
NAME        chaperonin ATPase;
            chaperonin
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to facilitate cellular and subcellular
            movement
SYSNAME     ATP phosphohydrolase (polypeptide-unfolding)
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     Multisubunit proteins with 2x7 (Type I, in most cells) or 2x8 (Type
            II, in Archaea) ATP-binding sites involved in maintaining an
            unfolded polypeptide structure before folding or entry into
            mitochondria and chloroplasts. Molecular masses of subunits ranges
            from 10-90 kDa. They are a subclass of molecular chaperones that are
            related to EC 3.6.4.8 (proteasome ATPase).
REFERENCE   1  [PMID:2897629]
  AUTHORS   Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT,
            Georgopoulos CP, Hendrix RW, Ellis RJ.
  TITLE     Homologous plant and bacterial proteins chaperone oligomeric protein
            assembly.
  JOURNAL   Nature. 333 (1988) 330-4.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Lubber, T.H., Donaldson, G.K., Viitanen, P.V. and Gatenby, A.A.
  TITLE     Several proteins imported into chloroplasts form stable complexes
            with the GroEL-related chloroplast molecular chaperone.
  JOURNAL   Plant Cell 1 (1989) 1223-1230.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   In: Ellis, R.J. (Ed.), The Chaperonins, Academic Press, San Diego,
            1996.
  TITLE     4  [PMID:9657960]
  JOURNAL   Ranson NA, White HE, Saibil HR.
REFERENCE   Chaperonins.
  AUTHORS   Biochem. J. 333 ( Pt 2) (1998) 233-42.
ORTHOLOGY   KO: K06028  
GENES       PFA: MAL13P1.283 PF10_0153 PF14_0417 PFB0635w
            ECI: UTI89_C0501(htpG) UTI89_C4741(groEL)
            HPA: HPAG1_0211
            PMB: A9601_05071(groL) A9601_16381(groEL)
            PMC: P9515_05141(groL) P9515_16151(groEL)
            PMF: P9303_05041(groEL) P9303_06501(groL)
            PMG: P9301_04761(groL) P9301_16261(groEL)
            PME: NATL1_05061(groL) NATL1_18361(groEL)
STRUCTURES  PDB: 1Q2V  1Q3Q  1Q3R  1Q3S  2NWC  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.4.9
            ExPASy - ENZYME nomenclature database: 3.6.4.9
            ExplorEnz - The Enzyme Database: 3.6.4.9
            ERGO genome analysis and discovery system: 3.6.4.9
            BRENDA, the Enzyme Database: 3.6.4.9
///
ENTRY       EC 3.6.4.10                 Enzyme
NAME        non-chaperonin molecular chaperone ATPase;
            molecular chaperone Hsc70 ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to facilitate cellular and subcellular
            movement
SYSNAME     ATP phosphohydrolase (polypeptide-polymerizing)
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     This is a highly diverse group of enzymes that perform many
            functions that are similar to those of chaperonins. They comprise a
            number of heat-shock-cognate proteins. They are also active in
            clathrin uncoating and in the oligomerization of actin.
REFERENCE   1  [PMID:1356434]
  AUTHORS   Sadis S, Hightower LE.
  TITLE     Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by
            accelerating ADP/ATP exchange.
  JOURNAL   Biochemistry. 31 (1992) 9406-12.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:8509407]
  AUTHORS   Blond-Elguindi S, Fourie AM, Sambrook JF, Gething MJ.
  TITLE     Peptide-dependent stimulation of the ATPase activity of the
            molecular chaperone BiP is the result of conversion of oligomers to
            active monomers.
  JOURNAL   J. Biol. Chem. 268 (1993) 12730-5.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:7743994]
  AUTHORS   Wawrzynow A, Wojtkowiak D, Marszalek J, Banecki B, Jonsen M, Graves
            B, Georgopoulos C, Zylicz M.
  TITLE     The ClpX heat-shock protein of Escherichia coli, the ATP-dependent
            substrate specificity component of the ClpP-ClpX protease, is a
            novel molecular chaperone.
  JOURNAL   EMBO. J. 14 (1995) 1867-77.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:9083109]
  AUTHORS   Sriram M, Osipiuk J, Freeman B, Morimoto R, Joachimiak A.
  TITLE     Human Hsp70 molecular chaperone binds two calcium ions within the
            ATPase domain.
  JOURNAL   Structure. 5 (1997) 403-14.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:9477575]
  AUTHORS   Li X, Su RT, Hsu HT, Sze H.
  TITLE     The molecular chaperone calnexin associates with the vacuolar
            H(+)-ATPase from oat seedlings.
  JOURNAL   Plant. Cell. 10 (1998) 119-30.
  ORGANISM  Avena sativa
GENES       AZO: azo0974(groEL1) azo1223(groEL2) azo2366(groEL3)
STRUCTURES  PDB: 2GQ0  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.4.10
            ExPASy - ENZYME nomenclature database: 3.6.4.10
            ExplorEnz - The Enzyme Database: 3.6.4.10
            ERGO genome analysis and discovery system: 3.6.4.10
            BRENDA, the Enzyme Database: 3.6.4.10
///
ENTRY       EC 3.6.4.11                 Enzyme
NAME        nucleoplasmin ATPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on acid anhydrides to facilitate cellular and subcellular
            movement
SYSNAME     ATP phosphohydrolase (nucleosome-assembling)
REACTION    ATP + H2O = ADP + phosphate [RN:R00086]
ALL_REAC    R00086
SUBSTRATE   ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     An acidic nuclear protein that is active in the ATP-dependent
            assembly of nucleosome cores, in decondensation of sperm chromatin
            and in other histone-involving processes.
REFERENCE   1  [PMID:8098530]
  AUTHORS   Laskey RA, Mills AD, Philpott A, Leno GH, Dilworth SM, Dingwall C.
  TITLE     The role of nucleoplasmin in chromatin assembly and disassembly.
  JOURNAL   Philos. Trans. R. Soc. Lond. B. Biol. Sci. 339 (1993) 263-9;
            discussion 268-9.
REFERENCE   2  [PMID:8016655]
  AUTHORS   Cote J, Quinn J, Workman JL, Peterson CL.
  TITLE     Stimulation of GAL4 derivative binding to nucleosomal DNA by the
            yeast SWI/SNF complex.
  JOURNAL   Science. 265 (1994) 53-60.
REFERENCE   3  [PMID:8798787]
  AUTHORS   Ito T, Tyler JK, Bulger M, Kobayashi R, Kadonaga JT.
  TITLE     ATP-facilitated chromatin assembly with a nucleoplasmin-like protein
            from Drosophila melanogaster.
  JOURNAL   J. Biol. Chem. 271 (1996) 25041-8.
  ORGANISM  Drosophila melanogaster [GN:dme]
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.4.11
            ExPASy - ENZYME nomenclature database: 3.6.4.11
            ExplorEnz - The Enzyme Database: 3.6.4.11
            ERGO genome analysis and discovery system: 3.6.4.11
            BRENDA, the Enzyme Database: 3.6.4.11
///
ENTRY       EC 3.6.5.1                  Enzyme
NAME        heterotrimeric G-protein GTPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on GTP to facilitate cellular and subcellular movement
SYSNAME     GTP phosphohydrolase (signalling)
REACTION    GTP + H2O = GDP + phosphate [RN:R00335]
ALL_REAC    R00335
SUBSTRATE   GTP [CPD:C00044];
            H2O [CPD:C00001]
PRODUCT     GDP [CPD:C00035];
            phosphate [CPD:C00009]
COMMENT     This group comprises GTP-hydrolysing systems, where GTP and GDP
            alternate in binding. This group includes stimulatory and inhibitory
            G-proteins such as Gs, Gi, Go and Golf, targetting adenylate cyclase
            and/or K+ and Ca2+ channels; Gq stimulating phospholipase C;
            transducin activating cGMP phosphodiesterase; gustducin activating
            cAMP phosphodiesterase. Golf is instrumental in odour perception,
            transducin in vision and gustducin in taste recognition. At least 16
            different alpha subunits (39-52 kDa), 5 beta subunits (36 kDa) and
            12 gamma subunits (6-9 kDa) are known.
REFERENCE   1  [PMID:7834744]
  AUTHORS   Neer EJ.
  TITLE     Heterotrimeric G proteins: organizers of transmembrane signals.
  JOURNAL   Cell. 80 (1995) 249-57.
REFERENCE   2  [PMID:9242920]
  AUTHORS   Sprang SR.
  TITLE     G protein mechanisms: insights from structural analysis.
  JOURNAL   Annu. Rev. Biochem. 66 (1997) 639-78.
REFERENCE   3  [PMID:9188484]
  AUTHORS   Bondarenko VA, Desai M, Dua S, Yamazaki M, Amin RH, Yousif KK,
            Kinumi T, Ohashi M, Komori N, Matsumoto H, Jackson KW, Hayashi F,
            Usukura J, Lipkin VM, Yamazaki A.
  TITLE     Residues within the polycationic region of cGMP phosphodiesterase
            gamma subunit crucial for the interaction with transducin alpha
            subunit. Identification by endogenous ADP-ribosylation and
            site-directed mutagenesis.
  JOURNAL   J. Biol. Chem. 272 (1997) 15856-64.
REFERENCE   4  [PMID:9671782]
  AUTHORS   Ming D, Ruiz-Avila L, Margolskee RF.
  TITLE     Characterization and solubilization of bitter-responsive receptors
            that couple to gustducin.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 8933-8.
  ORGANISM  cow [GN:bta]
GENES       AZO: azo3169
            PMF: P9303_00231
            PME: NATL1_00181
STRUCTURES  PDB: 2BCJ  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.5.1
            ExPASy - ENZYME nomenclature database: 3.6.5.1
            ExplorEnz - The Enzyme Database: 3.6.5.1
            ERGO genome analysis and discovery system: 3.6.5.1
            BRENDA, the Enzyme Database: 3.6.5.1
///
ENTRY       EC 3.6.5.2                  Enzyme
NAME        small monomeric GTPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on GTP to facilitate cellular and subcellular movement
SYSNAME     GTP phosphohydrolase (cell-regulating)
REACTION    GTP + H2O = GDP + phosphate [RN:R00335]
ALL_REAC    R00335
SUBSTRATE   GTP [CPD:C00044];
            H2O [CPD:C00001]
PRODUCT     GDP [CPD:C00035];
            phosphate [CPD:C00009]
COMMENT     A family of about 50 enzymes with a molecular mass of 21 kDa that
            are distantly related to the alpha-subunit of heterotrimeric
            G-protein GTPase (EC 3.6.5.1). They are involved in cell-growth
            regulation (Ras subfamily), membrane vesicle traffic and uncoating
            (Rab and ARF subfamilies), nuclear protein import (Ran subfamily)
            and organization of the cytoskeleton (Rho and Rac subfamilies).
REFERENCE   1  [PMID:1898771]
  AUTHORS   Bourne HR, Sanders DA, McCormick F.
  TITLE     The GTPase superfamily: conserved structure and molecular mechanism.
  JOURNAL   Nature. 349 (1991) 117-27.
REFERENCE   2  [PMID:7888179]
  AUTHORS   Hall A.
  TITLE     Small GTP-binding proteins and the regulation of the actin
            cytoskeleton.
  JOURNAL   Annu. Rev. Cell. Biol. 10 (1994) 31-54.
REFERENCE   3  [PMID:9434896]
  AUTHORS   Geyer M, Wittinghofer A.
  TITLE     GEFs, GAPs, GDIs and effectors: taking a closer (3D) look at the
            regulation of Ras-related GTP-binding proteins.
  JOURNAL   Curr. Opin. Struct. Biol. 7 (1997) 786-92.
  ORGANISM  human [GN:hsa], rat [GN:rno]
REFERENCE   4  [PMID:9446556]
  AUTHORS   Vitale N, Moss J, Vaughan M.
  TITLE     Molecular characterization of the GTPase-activating domain of
            ADP-ribosylation factor domain protein 1 (ARD1).
  JOURNAL   J. Biol. Chem. 273 (1998) 2553-60.
ORTHOLOGY   KO: K03864  small monomeric GTPase
GENES       PFA: MAL13P1.241 MAL13P1.297 MAL1P1.59 PF08_0110 PF13_0090
                 PF13_0119 PF14_0399 PFB0500c PFD0950w PFI0155c PFL1500w
STRUCTURES  PDB: 1RYF  1RYH  2ATX  2BMD  2BME  2C5L  2DPX  2EE4  2EE5  2F9L  
                 2F9M  2GZD  2GZH  2IEY  2IEZ  2IF0  2J1L  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.5.2
            ExPASy - ENZYME nomenclature database: 3.6.5.2
            ExplorEnz - The Enzyme Database: 3.6.5.2
            ERGO genome analysis and discovery system: 3.6.5.2
            BRENDA, the Enzyme Database: 3.6.5.2
///
ENTRY       EC 3.6.5.3                  Enzyme
NAME        protein-synthesizing GTPase;
            elongation factor (EF);
            initiation factor (IF);
            peptide-release or termination factor
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on GTP to facilitate cellular and subcellular movement
SYSNAME     GTP phosphohydrolase (mRNA-translation-assisting)
REACTION    GTP + H2O = GDP + phosphate [RN:R00335]
ALL_REAC    R00335
SUBSTRATE   GTP [CPD:C00044];
            H2O [CPD:C00001]
PRODUCT     GDP [CPD:C00035];
            phosphate [CPD:C00009]
COMMENT     This enzyme comprises a family of proteins involved in prokaryotic
            as well as eukaryotic protein synthesis. In the initiation factor
            complex, it is IF-2b (98 kDa) that binds GTP and subsequently
            hydrolyses it in prokaryotes. In eukaryotes, it is eIF-2 (150 kDa)
            that binds GTP. In the elongation phase, the GTP-hydrolysing
            proteins are the EF-Tu polypeptide of the prokaryotic transfer
            factor (43 kDa), the eukaryotic elongation factor EF-1alpha (53
            kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110
            kDa) and the signal recognition particle that play a role in
            endoplasmic reticulum protein synthesis (325 kDa). EF-Tu and
            EF-1alpha catalyse binding of aminoacyl-tRNA to the ribosomal
            A-site, while EF-G and EF-2 catalyse the translocation of
            peptidyl-tRNA from the A-site to the P-site. GTPase activity is also
            involved in polypeptide release from the ribosome with the aid of
            the pRFs and eRFs.
REFERENCE   1  [PMID:6566615]
  AUTHORS   Kurzchalia TV, Bommer UA, Babkina GT, Karpova GG.
  TITLE     GTP interacts with the gamma-subunit of eukaryotic initiation factor
            eIF-2.
  JOURNAL   FEBS. Lett. 175 (1984) 313-6.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:8722024]
  AUTHORS   Kisselev LL, Frolova LYu.
  TITLE     Termination of translation in eukaryotes.
  JOURNAL   Biochem. Cell. Biol. 73 (1995) 1079-86.
  ORGANISM  Xenopus laevis, human [GN:hsa]
REFERENCE   3  [PMID:8985244]
  AUTHORS   Rodnina MV, Savelsbergh A, Katunin VI, Wintermeyer W.
  TITLE     Hydrolysis of GTP by elongation factor G drives tRNA movement on the
            ribosome.
  JOURNAL   Nature. 385 (1997) 37-41.
  ORGANISM  Thermus thermophilus, Escherichia coli [GN:eco]
REFERENCE   4  [PMID:9233821]
  AUTHORS   Freistroffer DV, Pavlov MY, MacDougall J, Buckingham RH, Ehrenberg
            M.
  TITLE     Release factor RF3 in E.coli accelerates the dissociation of release
            factors RF1 and RF2 from the ribosome in a GTP-dependent manner.
  JOURNAL   EMBO. J. 16 (1997) 4126-33.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:9838020]
  AUTHORS   Krab IM, Parmeggiani A.
  TITLE     EF-Tu, a GTPase odyssey.
  JOURNAL   Biochim. Biophys. Acta. 1443 (1998) 1-22.
  ORGANISM  Thermus thermophilus, Thermus aquaticus, Salmonella typhimurium
ORTHOLOGY   KO: K02355  elongation factor EF-G
            KO: K02358  elongation factor EF-Tu
            KO: K03231  elongation factor EF-1 alpha subunit
            KO: K03234  elongation factor EF-2
            KO: K06029  
GENES       HSA: 1915(EEF1A1) 1917(EEF1A2) 1938(EEF2) 7284(TUFM) 79631(EFTUD1)
                 84340(GFM2) 85476(GFM1)
            PTR: 453590(EFTUD1) 471518(GFM2) 494136(EEF1A1)
            MMU: 101592(Eftud1) 13627(Eef1a1) 13628(Eef1a2) 13629(Eef2)
                 233870(Tufm) 28030(Gfm1) 320806(Gfm2)
            RNO: 114017(Gfm) 171361(Eef1a1) 24799(Eef1a2) 29565(Eef2)
            CFA: 403506(EEF1A1) 476744(EEF2) 477128(GFM1) 477388(LOC477388)
                 478101(GFM2) 478129(LOC478129) 478751(LOC478751)
                 479061(EFTUD1) 479796(TUFM) 480304(LOC480304)
                 487894(LOC487894) 607312(LOC607312) 607980(LOC607980)
                 609640(LOC609640) 609698(LOC609698) 609918(LOC609918)
                 610116(LOC610116) 610824(LOC610824) 612521(LOC612521)
                 612556(LOC612556) 612675(LOC612675)
            BTA: 281556(TUFM) 282220(EEF1A1)
            GGA: 373963(EEF1A1) 396325(EEF2) 415467(RCJMB04_3k21)
                 419244(EEF1A2) 425018(GFM1) 427205(GFM2)
            XLA: 379289(eef1a-o1) 380348(eef2) 380550(eef1a2) 386604(eef1a-s)
                 397890(EF-1aO) 432029(MGC83880) 494720(LOC494720)
            XTR: 394866(eef2) 394920(TGas003i10.1) 496898(eef1a2)
            DRE: 30516(ef1a) 326929(eef2l) 336334(zgc:73138)
            SPU: 548620(LOC548620) 579471(LOC579471) 583958(LOC583958)
                 584381(LOC584381) 592801(LOC592801)
            DME: Dmel_CG12736 Dmel_CG1873(Ef1alpha100E) Dmel_CG31159
                 Dmel_CG33158 Dmel_CG4567 Dmel_CG6050(EfTuM)
                 Dmel_CG8280(Ef1alpha48D)
            CEL: C43E11.4(tufm-2) F25H5.4(eft-2) F29C12.4 F31E3.5(eft-3)
                 R03G5.1(eft-4) Y119D3B.14 Y71H2AM.23(tufm-1)
            ATH: AT1G45332 AT1G56070(LOS1) AT1G62750(ATSCO1/ATSCO1/CPEF-G)
                 AT2G45030 AT3G22980 AT4G02930 AT4G20360(AtRABE1b/AtRab8D)
                 AT5G25230
            OSA: 4324669 4326544 4329493 4329859 4331810 4333268 4333588
                 4334800 4334959 4336525
            CME: CMG196C CMH226C CMI098C CMK150C CMO140C CMS428C CMS502C
            SCE: YBR118W(TEF2) YDR385W(EFT2) YJL102W(MEF2) YKL173W(SNU114)
                 YKR084C(HBS1) YLR069C(MEF1) YNL163C(RIA1) YOR133W(EFT1)
                 YOR187W(TUF1) YPR080W(TEF1)
            AGO: AGOS_AAR143W AGOS_ABR227C AGOS_ADL370C AGOS_ADR221C
                 AGOS_AEL124W AGOS_AFR031C AGOS_AFR085W AGOS_AFR142C
            PIC: PICST_36549(RIA1) PICST_39465 PICST_48738 PICST_65303(TEF1)
                 PICST_65888(TUF1) PICST_66828(EFT2) PICST_67982(MEF2)
            CAL: CaO19.1435 CaO19.4451 CaO19_4932(CaO19.4932)
                 CaO19_6047(CaO19.6047)
            CGR: CAGL0A03234g CAGL0D01188g CAGL0F01529g CAGL0G02255g
                 CAGL0G09581g CAGL0L03652g CAGL0M08294g
            SPO: SPAC23A1.10 SPBC2G5.08 SPBC660.10 SPBC839.15c(ef1-b)
                 SPBC9B6.04c SPCC553.08c SPCC794.09c SPCP31B10.07
            ANI: AN1084.2 AN2223.2 AN3832.2 AN4218.2 AN6330.2 AN6907.2
            AFM: AFUA_1G12170 AFUA_2G13530 AFUA_5G07140 AFUA_5G13520
            AOR: AO090001000151 AO090001000327 AO090011000384 AO090023000758
                 AO090026000260 AO090120000080 AO090120000502 AO090701000264
            CNE: CNA00330 CNC01520 CND06220 CNG03130 CNM01300
            UMA: UM00138.1 UM01261.1
            ECU: ECU04_1100 ECU11_1460
            DDI: DDBDRAFT_0201691 DDBDRAFT_0205988 DDBDRAFT_0219464
                 DDB_0191134(efaAII) DDB_0191363(efbA) DDB_0216236(cinC)
            PFA: PF13_0304 PF13_0305 PF14_0486 PFL1590c
            CPV: cgd8_2930
            CHO: Chro.60459 Chro.80341
            TAN: TA06720 TA16255 TA17805 TA18350 TA20405 TA21450
            TPV: TP01_0278 TP01_0529 TP01_0726 TP01_1088 TP03_0698 TP03_0816
                 TP04_0492 TP05_0019(tufA)
            TET: TTHERM_00151810 TTHERM_00290660 TTHERM_00353350
                 TTHERM_00655820 TTHERM_00938820 TTHERM_01194660
            TBR: Tb10.389.0070 Tb10.70.2190 Tb10.70.2650 Tb10.70.5650
                 Tb11.01.0710 Tb927.3.2170
            TCR: 506357.40 506583.60 507081.30 508169.20 508601.130 509199.10
                 510119.20 510119.9 510963.90 511277.70 511367.360 511367.370
                 511369.10 511369.20 511369.30 511369.5
            LMA: LmjF17.0080 LmjF17.0081 LmjF17.0082 LmjF17.0083 LmjF17.0084
                 LmjF17.0085 LmjF17.0086 LmjF18.0740 LmjF25.2080 LmjF28.1960
                 LmjF36.0180 LmjF36.0190 LmjF36.0570
            EHI: 143.t00006 187.t00004 214.t00016 23.t00018 403.t00006
                 470.t00004 8.t00008
            ECO: b3339(tufA) b3340(fusA) b3980(tufB)
            ECJ: JW3301(tufA) JW3302(fusA) JW3943(tufB)
            ECE: Z4697(tufA) Z4698(fusA) Z5553(tufB)
            ECS: ECs4190 ECs4191 ECs4903
            ECC: c4111(tufA) c4112(fusA) c4935(tufB)
            ECI: UTI89_C2891(lepA) UTI89_C3795(tufB) UTI89_C3841(tufA)
                 UTI89_C3842(fusA) UTI89_C4132(selB) UTI89_C4460(typA)
            ECP: ECP_3429 ECP_3430 ECP_4193
            ECV: APECO1_2492(tufA) APECO1_3113(fusA) APECO1_3114(tufA)
            STY: STY3739(tufB) STY4352(fusA) STY4353(tufA)
            STT: t3481(tufB) t4059(fusA) t4060(tufA)
            SPT: SPA3311(tufA) SPA3312(fusA) SPA3984(tufB)
            SEC: SC3379(tufB) SC3380(fusA) SC4030(tuf)
            STM: STM3445(tufA) STM3446(fusA) STM4146(tufB)
            YPE: YPO0202(fusA) YPO0203(tufA) YPO3754(tufA)
            YPK: y0477(tufB) y3985(fusA) y3986(tufB)
            YPM: YP_0201(fusA) YP_0202(tufA1) YP_3117(tufA)
            YPA: YPA_3269 YPA_3270 YPA_3626
            YPN: YPN_0211 YPN_0212 YPN_3864 YPN_3865
            YPP: YPDSF_0127 YPDSF_3752
            YPS: YPTB0276(tufA) YPTB3702(tufA) YPTB3703(fusA)
            YEN: YE0278(tufA)
            SFL: SF3357(tufA) SF3358(fusA) SF4053(tufA)
            SFX: S3682(tufB) S4404(fusA) S4405(tufA)
            SFV: SFV_3344(tufA) SFV_3345(fusA) SFV_4052(tufB)
            SSN: SSON_3469(tufA) SSON_3470(fusA) SSON_4153(tufB)
            SBO: SBO_3320(tufA) SBO_3321(fusA)
            SDY: SDY_3500(tufA) SDY_3501(fusA)
            ECA: ECA0216(tufA) ECA4035(tufB) ECA4036(fusA)
            PLU: plu0431(fusA) plu0432(tufB) plu4730(tufA)
            BUC: BU526(tufB) BU527(fusA)
            BAS: BUsg507(tufB) BUsg508(fusA)
            BAB: bbp469(tuf) bbp470(fusA)
            BCC: BCc_343(tuf) BCc_344(fusA)
            WBR: WGLp029(fusA) WGLp515(tufA)
            SGL: SG0127 SG2284
            ENT: Ent638_0190
            KPN: KPN_03724(tuf)
            BFL: Bfl564(tuf) Bfl565(fusA)
            BPN: BPEN_584(tuf) BPEN_585(fusA)
            HIN: HI0578(tufA) HI0579(fusA) HI0632(tufB)
            HIT: NTHI0712(tufB) NTHI0747(fusA) NTHI0748(tufB2)
            HDU: HD0054(tufA) HD0657(fusA) HD0658(tufB)
            HSO: HS_0195(tufA) HS_1645(fusA)
            PMU: PM1356(fusA) PM1357(tufA) PM1746(tufB)
            MSU: MS0164(fusA) MS0165(tufB) MS2187(tufB)
            APL: APL_1398(tufB) APL_1399(fusA) APL_1512(tufB)
            XFA: XF2628 XF2629 XF2640
            XFT: PD1996(tuf) PD1997(fusA) PD2009(tuf)
            XCC: XCC0880(tufA) XCC0892(fusA) XCC0893(tufB)
            XCB: XC_3342 XC_3343 XC_3354
            XCV: XCV0984(tuf) XCV0995(fusA) XCV0996(tuf)
            XAC: XAC0957(tufB) XAC0969(fusA) XAC0970(tufA)
            XOO: XOO3587(tufB) XOO3588(fusA) XOO3599(tufB)
            XOM: XOO_3389(XOO3389) XOO_3390(XOO3390) XOO_3401(XOO3401)
            VCH: VC0321 VC0361 VC0362 VC2342
            VVU: VV1_1203 VV1_1204 VV1_1338 VV1_1339 VV1_1737 VV1_1738
                 VV2_0942
            VVY: VV2668 VV3029 VV3030 VV3166 VVA1432
            VPA: VP2428 VP2770 VP2771 VP2930 VPA0328
            VFI: VF0232 VF0233 VF0529 VF2423
            PPR: PBPRA0315 PBPRA0316(tufB) PBPRA1234 PBPRA3439
            PAE: PA2071(fusA2) PA4265(tufA) PA4266(fusA1) PA4277(tufB)
            PAU: PA14_08680(tufB) PA14_08820(fusA1) PA14_37710(fusA2)
            PPU: PP_0440(tuf-1) PP_0451(fusA-1) PP_0452(tuf-2) PP_4111(fusA-2)
            PST: PSPTO_0623(fusA) PSPTO_0624(tuf)
            PSB: Psyr_4550 Psyr_4551
            PSP: PSPPH_4594(tuf) PSPPH_4595(fusA)
            PFL: PFL_5584(tuf) PFL_5585(fusA) PFL_5597(tuf)
            PFO: Pfl_5081 Pfl_5082 Pfl_5093
            PEN: PSEEN0475(tufB) PSEEN0486(fusA-1) PSEEN3478(fusA)
            PAR: Psyc_0383(tufBa) Psyc_1894(tufBb) Psyc_1895(fusA1)
            PCR: Pcryo_0425 Pcryo_2185
            ACI: ACIAD0299(tufB) ACIAD0884(fusA) ACIAD0885(tufA)
            SON: SO_0217(tufB) SO_0228(fusA-1) SO_0229(tufA) SO_0842(fusA-2)
            SDN: Sden_0167 Sden_0168 Sden_2958
            SFR: Sfri_0134 Sfri_0145 Sfri_0146 Sfri_0550
            SAZ: Sama_0199 Sama_0210
            SBL: Sbal_4172 Sbal_4467
            SLO: Shew_0144 Shew_0155
            SPC: Sputcn32_3761
            SHE: Shewmr4_0185 Shewmr4_0196 Shewmr4_0197 Shewmr4_0698
            SHM: Shewmr7_0180 Shewmr7_0191 Shewmr7_0192 Shewmr7_3324
            SHN: Shewana3_0185 Shewana3_0196 Shewana3_0197 Shewana3_3436
            SHW: Sputw3181_0142 Sputw3181_0153
            ILO: IL0338(tufB_1) IL0349(fusA)
            CPS: CPS_0875(fusA1) CPS_4764(tuf1) CPS_4765(fusA2) CPS_4780(tuf2)
            PHA: PSHAa0226(fusA) PSHAa0227(tufA) PSHAa2911(tufB) PSHAa2940
            PAT: Patl_0464 Patl_0602 Patl_0603
            SDE: Sde_0928 Sde_0929 Sde_0930
            PIN: Ping_3438
            MAQ: Maqu_0716 Maqu_0717
            CBU: CBU_0223(tuf-1) CBU_0235(fusA) CBU_0236(tuf-2)
            LPN: lpg0314(tuf2) lpg0326(fusA) lpg0327(tufB)
            LPF: lpl0355(tufA) lpl0366(fusA) lpl0367(tufA)
            LPP: lpp0380(tufA) lpp0391(fusA)
            MCA: MCA0544(fusA-1) MCA1059(tuf-1) MCA2374(tuf-2) MCA2375(fusA-2)
            FTU: FTT0137(tufA) FTT0323(fusA)
            FTF: FTF0137(tufA) FTF0323(fusA)
            FTW: FTW_0227(tufA) FTW_1759(fusA)
            FTL: FTL_0234 FTL_1751
            FTH: FTH_0176(efp) FTH_0220(tsf) FTH_0222(prfH) FTH_0229(fusA)
                 FTH_1213(infA) FTH_1368(infC) FTH_1691(tufA)
            FTN: FTN_0237(fusA) FTN_1576(tufA)
            TCX: Tcr_0281 Tcr_0292 Tcr_0293
            NOC: Noc_2225 Noc_2326 Noc_2327 Noc_2338
            AEH: Mlg_0444 Mlg_0455
            HHA: Hhal_0861
            HCH: HCH_03648 HCH_06219(tuf1) HCH_06220(fusA1)
            CSA: Csal_0418 Csal_0419
            ABO: ABO_0371(tuf-1) ABO_0382(fusA) ABO_0383(tuf)
            AHA: AHA_4018(tuf-1) AHA_4019(fusA)
            DNO: DNO_1277(tufA) DNO_1278(fusA)
            BCI: BCI_0494(fusA) BCI_0495(tuf)
            CRP: CRP_157 CRP_158
            RMA: Rmag_0162
            VOK: COSY_0167(tufA) COSY_0744(tufB)
            NME: NMB0124 NMB0138 NMB0139
            NMA: NMA0134(tufA1) NMA0135(fusA) NMA0149(tufA2)
            NMC: NMC0116
            NGO: NGO1842(tufA1) NGO1843(fusA) NGO1858
            CVI: CV_4188(tufA) CV_4189(fusA) CV_4200(tufB)
            RSO: RSc3021(tuf1) RSc3022(fusA1) RSc3041(tuf2) RSp0804(fusA2)
            REU: Reut_A3182 Reut_A3183 Reut_A3196 Reut_B3749 Reut_B5535
            REH: H16_A3491(tufA) H16_A3492(fusA1) H16_A3505(tufB)
            RME: Rmet_3324 Rmet_3325 Rmet_5930
            BMA: BMA2252(fusA-1) BMA2634(tuf-1) BMA2635(fusA-2) BMA2649(tuf-2)
            BXE: Bxe_A0299 Bxe_A0311 Bxe_A0312 Bxe_A0793
            BUR: Bcep18194_A3444 Bcep18194_A5860
            BCN: Bcen_1916 Bcen_2761 Bcen_2762
            BCH: Bcen2424_0333 Bcen2424_0345 Bcen2424_2528
            BAM: Bamb_0252 Bamb_0264 Bamb_0265 Bamb_2576
            BPS: BPSL0893(fusA) BPSL3215(tufA2) BPSL3216(fusA) BPSL3228(tufA1)
            BPM: BURPS1710b_1105(fusA) BURPS1710b_3778(tuf)
                 BURPS1710b_3779(fusA) BURPS1710b_3794(tuf)
            BTE: BTH_I0756(fusA-1) BTH_I3070(tuf-1) BTH_I3071(fusA-2)
            PNU: Pnuc_0050
            BPE: BP0007(tufA) BP3610(fusA) BP3611(tuf)
            BPA: BPP0007(tufA) BPP0026(fusA) BPP0027(tuf) BPP3814(fusA)
            BBR: BB0007(tuf) BB0026(fusA) BB0027(tuf) BB4259(fusA)
            RFR: Rfer_1382 Rfer_3599 Rfer_3797 Rfer_3798
            POL: Bpro_0253 Bpro_0254 Bpro_4287
            PNA: Pnap_0201
            AAV: Aave_0336
            AJS: Ajs_0276
            VEI: Veis_1262
            MPT: Mpe_A3402 Mpe_A3445 Mpe_A3446 Mpe_A3458
            MMS: mma_3413(tuf1) mma_3414(fusA) mma_3427(tuf2)
            NEU: NE0399(tuf2) NE2052(tuf2) NE2053(fusA1)
            NET: Neut_0555 Neut_0556
            NMU: Nmul_A0752 Nmul_A0764
            EBA: ebA3808(tufB) ebA3824(fusA) ebA3826(tufB) ebA825
            AZO: azo1152(fusA1) azo3419(tufA) azo3420(fusA2) azo3431(tufB)
            DAR: Daro_0222 Daro_0305 Daro_0316 Daro_0317
            TBD: Tbd_0391 Tbd_0402 Tbd_0403
            MFA: Mfla_0265 Mfla_0276 Mfla_0277
            HPY: HP1195(fusA) HP1205(tufB)
            HPJ: jhp1118(fusA) jhp1128(tufA)
            HPA: HPAG1_0350 HPAG1_0399 HPAG1_0457 HPAG1_1134 HPAG1_1145
                 HPAG1_1146 HPAG1_1243
            HHE: HH0101(lepA) HH0358(fusA) HH0369(tufA) HH1772(yihK)
            HAC: Hac_0967(lepA) Hac_1074(typA) Hac_1575(fusA) Hac_1586(tuf)
            WSU: WS0470(efg)
            TDN: Tmden_0345 Tmden_0357
            CJE: Cj0470(tuf) Cj0493(fusA)
            CJR: CJE0520(tuf) CJE0542(fusA)
            CJU: C8J_0443(tuf) C8J_0455(fusA)
            CCO: CCC13826_0687(selB) CCC13826_1307(yihK)
            ABU: Abu_1893(tufA)
            GSU: GSU1933(fusA-1) GSU2529(fusA-2) GSU2859(tuf-1)
                 GSU2860(fusA-3) GSU2871(tuf-2)
            GME: Gmet_0611 Gmet_0623 Gmet_0624 Gmet_1985 Gmet_2521
            PCA: Pcar_0197 Pcar_0686 Pcar_0698 Pcar_0699 Pcar_1969
            PPD: Ppro_0677
            DVU: DVU0881 DVU1300(fusA-1) DVU1799(fusA-2) DVU2920(tuf)
            DDE: Dde_2063 Dde_2261 Dde_2741 Dde_2989
            LIP: LI0935(tufA) LI0944(fusA)
            BBA: Bd0987(fusA-2) Bd2979(fusA) Bd2994(tuf)
            DPS: DP0007 DP1109 DP1121 DP1122 DP2398
            ADE: Adeh_1584 Adeh_1948 Adeh_2292
            MXA: MXAN_2408(fusA) MXAN_3068(tuf) MXAN_3297(fusA) MXAN_3298(tuf)
            SAT: SYN_00983 SYN_01574 SYN_01918 SYN_02930
            SFU: Sfum_0068 Sfum_1044 Sfum_1541 Sfum_1553
            RPR: RP132(fusA) RP661(tuf)
            RTY: RT0121(fusA) RT0653(tuf)
            RCO: RC0174(fusA) RC1008(tuf)
            RFE: RF_0276(tuf) RF_1153(fusA)
            RBE: RBE_1064(tuf) RBE_1160(fusA)
            RAK: A1C_05115
            RBO: A1I_02025
            RCM: A1E_04385
            RRI: A1G_05565
            WOL: WD0016(fusA) WD0017(tuf) WD0683(tuf)
            WBM: Wbm0343 Wbm0344 Wbm0653
            AMA: AM253(fusA) AM254(tuf) AM914(tuf)
            APH: APH_0278(tuf-1) APH_1032(tuf-2) APH_1033(fusA)
            ERU: Erum1650(fusA) Erum1660(tufA) Erum6090(tufB)
            ERW: ERWE_CDS_01620(fusA) ERWE_CDS_06400(tuf)
            ERG: ERGA_CDS_01570(fusA) ERGA_CDS_01580(tufA) ERGA_CDS_06310(tuf)
            ECN: Ecaj_0161 Ecaj_0162 Ecaj_0614
            ECH: ECH_0407(tuf-2) ECH_0961(fusA)
            NSE: NSE_0686(tuf) NSE_0687(fusA)
            PUB: SAR11_1119(fusA) SAR11_1130(tufB)
            MLO: mlr0263 mlr0286 mlr0288 mlr2549
            MES: Meso_1680 Meso_1681 Meso_2110
            SME: SMb20049(fusA2) SMc01311(tufA) SMc01312(fusA1) SMc01326(tufB)
            ATU: Atu1948(tuf) Atu1949(fusA) Atu1966(tuf)
            ATC: AGR_C_3557 AGR_C_3558 AGR_C_3583
            RET: RHE_CH01066(fusA1) RHE_CH01658(tufB) RHE_CH01672(fusA2)
                 RHE_CH01673(tufA)
            RLE: RL1757(tufB1) RL1771(fus)
            BME: BMEI0742 BMEI0754 BMEI0755
            BMF: BAB1_1257(tuf-2) BAB1_1258(fusA) BAB1_1271(tuf-2)
            BMS: BR1235(tuf-1) BR1236(fusA) BR1251(tuf-2)
            BMB: BruAb1_1240(tuf) BruAb1_1241(fusA) BruAb1_1255(tuf)
            BJA: bll5402(tuf) bll5403(fusA) bll7414
            RPA: RPA3252(tufA) RPA3253(fusA) RPA3283(tuf) RPA4328
            RPB: RPB_1300 RPB_2266 RPB_2292 RPB_2293
            RPC: RPC_3450 RPC_3451
            RPD: RPD_3186 RPD_3187 RPD_3204 RPD_3921
            RPE: RPE_3588 RPE_3589 RPE_4173
            NWI: Nwi_1361 Nwi_1362 Nwi_2978
            NHA: Nham_1106 Nham_1542
            BHE: BH06020(tuf1) BH10530(tuf2) BH10540(fusA)
            BQU: BQ07210(tuf2) BQ08250(tuf1) BQ08260(fusA)
            CCR: CC_1240 CC_3199 CC_3200
            SIL: SPO0728(tuf-1) SPO3498(tuf-2) SPO3499(fusA) SPO3533
            SIT: TM1040_0241 TM1040_0242 TM1040_2434
            RSP: RSP_1707(tufA) RSP_1708(fusA1) RSP_1714(tufA) RSP_2247(fusA)
            JAN: Jann_0555 Jann_0577
            RDE: RD1_1396(tufA) RD1_4013(fusA)
            MMR: Mmar10_1797 Mmar10_1798
            HNE: HNE_1734(tuf1) HNE_2853(tuf2) HNE_2854(fusA)
            ZMO: ZMO0515 ZMO0516
            NAR: Saro_1246 Saro_1247 Saro_1277
            SAL: Sala_2820 Sala_2821
            ELI: ELI_08205 ELI_08210
            GOX: GOX0105 GOX0382
            GBE: GbCGDNIH1_0552 GbCGDNIH1_1339
            RRU: Rru_A2690 Rru_A2691 Rru_A2702
            MAG: amb0711 amb3132 amb3133 amb3148
            MGM: Mmc1_0124 Mmc1_0832 Mmc1_0844 Mmc1_0845
            ABA: Acid345_1223 Acid345_1224 Acid345_4753
            SUS: Acid_6322
            BSU: BG11056(tufA) BG11939(fus)
            BHA: BH0131(fus) BH0132(tufA)
            BAN: BA0107(fusA) BA0108(tuf)
            BAR: GBAA0107(fusA) GBAA0108(tuf)
            BAA: BA_0695 BA_0696
            BAT: BAS0107 BAS0108
            BCE: BC0128 BC0129
            BCA: BCE_0107(fusA) BCE_0108(tuf)
            BCZ: BCZK0101(fusA) BCZK0102(tufA) BCZK0127(infA)
            BTK: BT9727_0103(fusA) BT9727_0104(tufA) BT9727_0129(infA)
            BTL: BALH_0105(fusA)
            BLI: BL01055(tufA) BL01057(fusA)
            BLD: BLi00130(fusA) BLi00131(tufA)
            BCL: ABC0147(fus) ABC0148(tufA)
            BPU: BPUM_0098(fusA) BPUM_0099(tufA) BPUM_0126 BPUM_1249
                 BPUM_1549(tsf) BPUM_1551(frr) BPUM_1566 BPUM_2177(efp)
                 BPUM_3177 BPUM_3345
            OIH: OB0116(fus) OB0117(tufA)
            GKA: GK0103(fus) GK0104(tufA)
            GTN: GTNG_0103
            SAU: SA0505(fus) SA0506(tufA)
            SAV: SAV0547(fus) SAV0548(tufA)
            SAM: MW0502(fus) MW0503(tufA)
            SAR: SAR0552(fus) SAR0553(tuf)
            SAS: SAS0505 SAS0506
            SAC: SACOL0593(fusA) SACOL0594(tuf)
            SAB: SAB0498(fus) SAB0499(tuf)
            SAA: SAUSA300_0532(fusA) SAUSA300_0533(tuf)
            SAO: SAOUHSC_00529 SAOUHSC_00530
            SEP: SE0311 SE0312
            SER: SERP0188(fusA) SERP0189(tuf)
            SHA: SH2459(tufA) SH2460(fusA)
            SSP: SSP2207 SSP2208
            LMO: lmo2653(tufA) lmo2654(fus)
            LMF: LMOf2365_2632(tuf) LMOf2365_2633(fusA)
            LIN: lin2802(tufA) lin2803(fus)
            LWE: lwe2602(tufA) lwe2603(fusA)
            LLA: L0368(fusA) L0371(tuf)
            LLC: LACR_2054
            LLM: llmg_2050(tufA) llmg_2556(fusA)
            SPY: SPy_0273(fus) SPy_0611(tufA)
            SPZ: M5005_Spy_0232(fus) M5005_Spy_0508(tuf)
            SPM: spyM18_0260(fusA) spyM18_0678(tufA)
            SPG: SpyM3_0200(fusA) SpyM3_0432(tufA)
            SPS: SPs0206 SPs1423
            SPH: MGAS10270_Spy0232(fus) MGAS10270_Spy0502
            SPI: MGAS10750_Spy0227(fus) MGAS10750_Spy0527
            SPJ: MGAS2096_Spy0251(fus) MGAS2096_Spy0519 MGAS2096_Spy0520
            SPK: MGAS9429_Spy0234(fus) MGAS9429_Spy0498
            SPF: SpyM50211(fus)
            SPA: M6_Spy0264 M6_Spy0529
            SPB: M28_Spy0226(fus) M28_Spy0487(tuf)
            SPN: SP_0273 SP_1489
            SPR: spr0250(fusA) spr1343(tufA)
            SPD: SPD_0253(fusA)
            SAG: SAG0762(tuf) SAG1769(fusA)
            SAN: gbs0782(tufA) gbs1812(fusA)
            SAK: SAK_0887(tuf) SAK_1791(fusA)
            SMU: SMU.359 SMU.714
            STC: str0487(tufA) str1789(fus)
            STL: stu0487(tufA) stu1789(fus)
            STE: STER_1762
            SSA: SSA_1520(tuf) SSA_2109(fusA)
            SSU: SSU05_0152
            SSV: SSU98_0155
            LPL: lp_1027(fusA2) lp_2119(tuf)
            LJO: LJ0337 LJ1009
            LAC: LBA0289 LBA0845
            LSA: LSA1063(tuf) LSA1768(fusA)
            LSL: LSL_0202(efg) LSL_0642(tufB)
            LDB: Ldb0394(fusA) Ldb0776(tuf)
            LBU: LBUL_0348 LBUL_0709
            LBR: LVIS_1389 LVIS_1693
            LCA: LSEI_1332 LSEI_2508
            LGA: LGAS_0289
            PPE: PEPE_1420
            EFA: EF0200(fusA) EF0201(tuf)
            OOE: OEOE_0792 OEOE_1314
            LME: LEUM_0189
            CAC: CAC3136(tufA) CAC3138(fus)
            CPE: CPE0079(fus) CPE2407(tufA) CPE2408(fus) CPE2421(tufA)
            CPF: CPF_0074(fusA) CPF_2716(tuf) CPF_2717(fusA)
            CPR: CPR_0096(fusA) CPR_2402(tuf) CPR_2403(fusA)
            CTC: CTC02602 CTC02604 CTC02616 CTC02640
            CNO: NT01CX_1056(fusA) NT01CX_1100 NT01CX_1112(fusA)
            CTH: Cthe_2729
            CDF: CD0070(fusA)
            CHY: CHY_0961(fusA1) CHY_2312(tuf1) CHY_2313(fusA2) CHY_2327(tuf2)
            DSY: DSY0468 DSY0469 DSY1817
            DRM: Dred_0212
            PTH: PTH_0317(fusA)
            SWO: Swol_1152 Swol_2335 Swol_2336 Swol_2350
            CSC: Csac_0957
            TTE: TTE2295(tufB) TTE2296(fusA) TTE2310(tufB2) TTE2333(fusA2)
            MTA: Moth_1142 Moth_2462 Moth_2463
            MGE: MG_089(fusA) MG_451(tuf)
            MPN: MPN227(fus) MPN665(tuf)
            MPU: MYPU_4050(tufA) MYPU_4280(fus)
            MPE: MYPE310(fusA) MYPE320(tufA)
            MGA: MGA_0260(fusA) MGA_1033(tufB)
            MMY: MSC_0159(fusA) MSC_0160(tufA)
            MMO: MMOB2240(eftU) MMOB3670(tufA)
            MHY: mhp083(fusA) mhp540(tuf)
            MHJ: MHJ_0071(fusA) MHJ_0524(tufA)
            MHP: MHP7448_0075(fusA) MHP7448_0523(tufA)
            MSY: MS53_0047(fusA) MS53_0667(tufA)
            MCP: MCAP_0153(fusA) MCAP_0154(tuf)
            UUR: UU522(tuf) UU523(fusA)
            POY: PAM264(fusA) PAM265(tufB)
            AYW: AYWB_456(tufB) AYWB_457(fusA)
            MFL: Mfl621 Mfl622
            MTU: Rv0120c(fusA2) Rv0684(fusA1) Rv0685(tuf)
            MTC: MT0128(fusA-1) MT0712(fusA-2) MT0713(tufA)
            MBO: Mb0124c(fusA2b) Mb0703(fusA1) Mb0704(tuf)
            MLE: ML1877(tuf) ML1878(fusA)
            MPA: MAP3525c(fusA2) MAP4142(fusA) MAP4143(tuf)
            MSM: MSMEG_1401(tuf) MSMEG_6535
            MMC: Mmcs_0986 Mmcs_0987 Mmcs_5136
            CGL: NCgl0478(cgl0495) NCgl0480(tuf)
            CGB: cg0583(fusA) cg0587(tuf)
            CEF: CE0516 CE0517
            CDI: DIP0469(fusA) DIP0470(tuf)
            CJK: jk1839(tuf) jk1840(fusA)
            NFA: nfa16700(fusA2) nfa50750(tufB) nfa50760(fusA)
            RHA: RHA1_ro00963(infC) RHA1_ro01483(prfA) RHA1_ro01921(tufA)
                 RHA1_ro01922 RHA1_ro05692(prfC) RHA1_ro05886(fusA)
                 RHA1_ro05933 RHA1_ro06157(infA) RHA1_ro06404(prfB)
                 RHA1_ro06579(tsf) RHA1_ro06644(infB) RHA1_ro07145(efp)
            SCO: SCO1321(2SCG61.03c) SCO1528(SCL2.18) SCO4661(fusA)
                 SCO4662(SCD40A.08) SCO6589(fusB)
            SMA: SAV1799(fusA3) SAV4919(fusA1) SAV4920(tuf1) SAV6825(fusA2)
                 SAV7028(tuf2)
            TWH: TWT120(tuf) TWT675(fusA)
            TWS: TW131(tufA) TW694(fusA)
            LXX: Lxx20400(fusA)
            CMI: CMM_2620(tufA) CMM_2621(fusA)
            PAC: PPA1873 PPA1875
            TFU: Tfu_2648 Tfu_2649
            FRA: Francci3_0579 Francci3_0580 Francci3_1361
            FAL: FRAAL1078(fusA) FRAAL1079(tufA) FRAAL2131
            ACE: Acel_0303 Acel_0304
            SEN: SACE_2008(fusA2) SACE_2075(efp) SACE_5926(infB)
                 SACE_6037(tsf) SACE_6808(infA) SACE_6838(tufA) SACE_6839(fusA)
            BLO: BL1097(tuf) BL1098(fusA)
            BAD: BAD_0532(fusA1) BAD_0533(tuf)
            RXY: Rxyl_2157 Rxyl_2158 Rxyl_2318
            FNU: FN1546 FN1555 FN1556
            RBA: RB5434(fusA) RB7821(fusA) RB7894(tufA)
            CTR: CT322(tufA) CT437(fusA)
            CTA: CTA_0345(tufA) CTA_0477(fusA)
            CMU: TC0596 TC0721
            CPN: CPn0074(tufA) CPn0550(fusA)
            CPA: CP0202 CP0701
            CPJ: CPj0074(tufA) CPj0550(fusA)
            CPT: CpB0074 CpB0571
            CCA: CCA00192(fusA) CCA00698(tuf)
            CAB: CAB188 CAB668(tuF)
            CFE: CF0313(tufA) CF0815(fusA)
            PCU: pc0207(fusA) pc0595(tufA)
            BBU: BB0476(tuf) BB0540(fus-1) BB0691(fus-2)
            BGA: BG0487(tuf) BG0550(fus-1) BG0715(fus-2)
            BAF: BAPKO_0504(tuf) BAPKO_0568(fus-1) BAPKO_0736(fus-2)
            TPA: TP0187(tuf) TP0450(fusA-1) TP0767(fusA-2)
            TDE: TDE0285(fusA-1) TDE0765(tuf) TDE0947 TDE1049(fusA-2)
            LIL: LA0313(fusA1) LA0736(fusA2) LA0737
            LIC: LIC10272(fusA) LIC12875(tuf) LIC12876(fus)
            LBJ: LBJ_0381 LBJ_2661(tufB) LBJ_2662
            LBL: LBL_0450 LBL_0451(tufB) LBL_2696
            SYN: sll0830(fus) sll1098(fusB) sll1099(tufA) slr1463(fusA)
            SYW: SYNW2137(fusA) SYNW2138(tufA)
            SYC: syc0655_d(fus) syc0656_d(tufA) syc2011_d(fus)
            SYF: Synpcc7942_0884 Synpcc7942_0885 Synpcc7942_2082
            SYD: Syncc9605_0320(tuf) Syncc9605_0321
            SYE: Syncc9902_2021 Syncc9902_2022(tuf)
            SYG: sync_0381(tuf) sync_0382(fusA)
            SYR: SynRCC307_2169(fusA)
            CYA: CYA_1301(fusA) CYA_1302(tuf)
            CYB: CYB_0920(fusA) CYB_0921(tuf)
            TEL: tll2359(fus) tlr1749(fus) tlr1750(tufA)
            GVI: glr2812(fus) glr3927(fus) glr3928(tufA)
            ANA: all4337(tufA) all4338(fus) alr4383(fus)
            AVA: Ava_1287(tuf) Ava_1288 Ava_3294
            PMA: Pro1664(tufB) Pro1665(fusA)
            PMM: PMM1508(tufA) PMM1509(fusA)
            PMT: PMT1781(fusA) PMT1782(tufA)
            PMN: PMN2A_1074 PMN2A_1075
            PMI: PMT9312_1600 PMT9312_1601
            PMB: A9601_04711(lepA) A9601_08241(typA) A9601_13261(infA)
                 A9601_17111(tufA) A9601_17121(fusA)
            PMC: P9515_04811(lepA) P9515_08211(typA) P9515_13161(infA)
                 P9515_16881(tufA) P9515_16891(fusA)
            PMF: P9303_16761(typA) P9303_20941(lepA) P9303_23631(fusA)
                 P9303_23641(tufA)
            PMG: P9301_04401(lepA) P9301_08221(typA) P9301_13411(infA)
                 P9301_16991(tufA) P9301_17001(fusA)
            PMH: P9215_17761(tufA) P9215_17771(fusA)
            PME: NATL1_04741(lepA) NATL1_07981(typA) NATL1_15991(infA)
                 NATL1_19491(tufA) NATL1_19501(fusA)
            TER: Tery_0475 Tery_0476 Tery_2771 Tery_4509
            BTH: BT_2167 BT_2729 BT_2740
            BFR: BF3867 BF4183 BF4199
            BFS: BF3636 BF4005(fusA) BF4022(tuf)
            PGI: PG0387(tuf) PG0933 PG1940(fusA)
            SRU: SRU_1032(fusA) SRU_1033(tuf) SRU_1150(fus) SRU_1766(tuf)
            CHU: CHU_3164(fusA) CHU_3175(tufB)
            CTE: CT0144(fusA-2) CT2191(tuf) CT2192(fusA-1)
            CCH: Cag_0346 Cag_1853 Cag_1854
            PLT: Plut_0177 Plut_0178 Plut_1973
            DET: DET0472(fusA-1) DET0997(tuf) DET1212(fusA-2)
            DEH: cbdb_A1130(fusA) cbdb_A437(fusA) cbdb_A960(tuf)
            DRA: DR_0307 DR_0309 DR_0393 DR_2050
            DGE: Dgeo_0646 Dgeo_1453 Dgeo_1869 Dgeo_1871
            TTH: TTC1134 TTC1330 TTC1331 TTC1734
            TTJ: TTHA0251 TTHA1498 TTHA1694 TTHA1695
            AAE: aq_001(fusA) aq_005(tufA1) aq_1928(tufA2)
            TMA: TM1502 TM1503 TM1651
            MJA: MJ0324(tuf) MJ0495 MJ1048(fus)
            MMP: MMP1131 MMP1336(selB) MMP1369(aEF-2) MMP1370(aEF-1_alpha)
                 MMP1401(aEF-1_beta)
            MAC: MA1256(ef1A) MA1257(ef2)
            MBA: Mbar_A3685 Mbar_A3686
            MMA: MM_2264(EF-1A) MM_2265(EF-2)
            MBU: Mbur_1170 Mbur_1171
            MHU: Mhun_1592 Mhun_2828
            MTH: MTH1057 MTH1058 MTH1185
            MST: Msp_1366(tuf) Msp_1367(fusA)
            MKA: MK0148 MK0247 MK0679(fusA)
            AFU: AF0744 AF0937(tuf) AF1894(fus)
            HAL: VNG1676G(gbp2) VNG2649G(eef1a) VNG2654Gm(eef2)
            HMA: rrnAC1619(gbp2) rrnAC2406(eef1a) rrnAC2413(fusA)
            HWA: HQ2800A HQ3385A(tef1a) HQ3388A(tef2)
            NPH: NP0130A(tef2) NP0304A(tef1a) NP1740A
            TAC: Ta0444 Ta0446
            TVO: TVN1049 TVN1051
            PTO: PTO0415 PTO0417
            PHO: PH1484 PH1899
            PAB: PAB0187(fus) PAB0465(tuf)
            PFU: PF1375 PF2012
            TKO: TK0308 TK0309
            APE: APE_1432 APE_1844
            SSO: SSO0216(tuf-1) SSO0728(EF-2) SSO2429(tuf-2)
            STO: ST0269 ST0437 ST0557
            SAI: Saci_0603 Saci_0685 Saci_0920
            PAI: PAE0332 PAE1764 PAE3000
            NEQ: NEQ082 NEQ543
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.5.3
            ExPASy - ENZYME nomenclature database: 3.6.5.3
            ExplorEnz - The Enzyme Database: 3.6.5.3
            ERGO genome analysis and discovery system: 3.6.5.3
            BRENDA, the Enzyme Database: 3.6.5.3
///
ENTRY       EC 3.6.5.4                  Enzyme
NAME        signal-recognition-particle GTPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on GTP to facilitate cellular and subcellular movement
SYSNAME     GTP phosphohydrolase (protein-synthesis-assisting)
REACTION    GTP + H2O = GDP + phosphate [RN:R00335]
ALL_REAC    R00335
SUBSTRATE   GTP [CPD:C00044];
            H2O [CPD:C00001]
PRODUCT     GDP [CPD:C00035];
            phosphate [CPD:C00009]
COMMENT     Activity is associated with the signal-recognition particle (a
            protein- and RNA-containing structure involved in
            endoplasmic-reticulum-associated protein synthesis).
REFERENCE   1  [PMID:2541918]
  AUTHORS   Connolly T, Gilmore R.
  TITLE     The signal recognition particle receptor mediates the GTP-dependent
            displacement of SRP from the signal sequence of the nascent
            polypeptide.
  JOURNAL   Cell. 57 (1989) 599-610.
REFERENCE   2  [PMID:1851576]
  AUTHORS   Connolly T, Rapiejko PJ, Gilmore R.
  TITLE     Requirement of GTP hydrolysis for dissociation of the signal
            recognition particle from its receptor.
  JOURNAL   Science. 252 (1991) 1171-3.
REFERENCE   3  [PMID:8247130]
  AUTHORS   Miller JD, Wilhelm H, Gierasch L, Gilmore R, Walter P.
  TITLE     GTP binding and hydrolysis by the signal recognition particle during
            initiation of protein translocation.
  JOURNAL   Nature. 366 (1993) 351-4.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:9002524]
  AUTHORS   Freymann DM, Keenan RJ, Stroud RM, Walter P.
  TITLE     Structure of the conserved GTPase domain of the signal recognition
            particle.
  JOURNAL   Nature. 385 (1997) 361-4.
  ORGANISM  Thermus aquaticus
GENES       HPA: HPAG1_0412 HPAG1_0748 HPAG1_1091
            MMO: MMOB5270(ffh)
            PMB: A9601_14851(ffh)
            PMC: P9515_14471(ffh)
            PMF: P9303_19561(ffh)
            PMG: P9301_14711(ffh)
            PME: NATL1_17061(ffh)
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.5.4
            ExPASy - ENZYME nomenclature database: 3.6.5.4
            ExplorEnz - The Enzyme Database: 3.6.5.4
            ERGO genome analysis and discovery system: 3.6.5.4
            BRENDA, the Enzyme Database: 3.6.5.4
///
ENTRY       EC 3.6.5.5                  Enzyme
NAME        dynamin GTPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on GTP to facilitate cellular and subcellular movement
SYSNAME     GTP phosphohydrolase (vesicle-releasing)
REACTION    GTP + H2O = GDP + phosphate [RN:R00335]
ALL_REAC    R00335
SUBSTRATE   GTP [CPD:C00044];
            H2O [CPD:C00001]
PRODUCT     GDP [CPD:C00035];
            phosphate [CPD:C00009]
COMMENT     An enzyme with a molecular mass of about 100 kDa that is involved in
            endocytosis and is instrumental in pinching off membrane vesicles.
REFERENCE   1  [PMID:8939066]
  AUTHORS   Warnock DE, Schmid SL.
  TITLE     Dynamin GTPase, a force-generating molecular switch.
  JOURNAL   Bioessays. 18 (1996) 885-93.
  ORGANISM  rat [GN:rno], Drosophila sp.
REFERENCE   2  [PMID:9116759]
  AUTHORS   McClure SJ, Robinson PJ.
  TITLE     Dynamin, endocytosis and intracellular signalling (review).
  JOURNAL   Mol. Membr. Biol. 13 (1996) 189-215.
REFERENCE   3  [PMID:9531551]
  AUTHORS   Oh P, McIntosh DP, Schnitzer JE.
  TITLE     Dynamin at the neck of caveolae mediates their budding to form
            transport vesicles by GTP-driven fission from the plasma membrane of
            endothelium.
  JOURNAL   J. Cell. Biol. 141 (1998) 101-14.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K01528  dynamin GTPase
GENES       HSA: 10059(DNM1L) 1759(DNM1) 1785(DNM2) 26052(DNM3)
            PTR: 464766(DNM1) 465266(DNM1L)
            MCC: 713558(DNM2)
            MMU: 103967(Dnm3) 13429(Dnm1) 13430(Dnm2) 74006(Dnm1l)
            RNO: 114114(Dnm1l) 140694(Dnm1) 171574(Dnm3) 25751(Dnm2)
            CFA: 477649(DNM1L) 490341(DNM3)
            GGA: 417217(DNM1) 418132(RCJMB04_2k14)
            XLA: 379244(MGC53884) 379875(dnm1l)
            XTR: 496487(dnm2)
            DRE: 393896(dnm1l) 406525(dnm2l)
            SPU: 577217(LOC577217) 594157(LOC594157)
            DME: Dmel_CG18102(shi) Dmel_CG3210(Drp1)
            CEL: C02C6.1(dyn-1) T12E12.4(drp-1)
            ATH: AT2G14120
            OSA: 4327743
            CME: CME019C
            SCE: YLL001W(DNM1)
            AGO: AGOS_AAL174C
            PIC: PICST_29756
            CAL: CaO19.6987
            CGR: CAGL0D05808g
            SPO: SPBC12C2.08
            ANI: AN8874.2
            AFM: AFUA_1G11970 AFUA_3G13580 AFUA_4G00540 AFUA_4G14300
                 AFUA_6G07630 AFUA_6G11890 AFUA_7G08580 AFUA_8G02840
            AOR: AO090010000776
            CNE: CNA05470 CNC01680
            UMA: UM02907.1 UM05378.1
            DDI: DDB_0216177(dymA)
            PFA: PF10_0368 PF11_0465
            TAN: TA11580
            TPV: TP02_0143
            TET: TTHERM_00160990 TTHERM_00486790 TTHERM_01194750
                 TTHERM_01194760 TTHERM_01194780 TTHERM_01194810
                 TTHERM_02046520
            TBR: Tb927.3.4720 Tb927.3.4760
            TCR: 508153.20
            LMA: LmjF29.2200
            EHI: 14.t00035
STRUCTURES  PDB: 2AKA  
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.5.5
            ExPASy - ENZYME nomenclature database: 3.6.5.5
            ExplorEnz - The Enzyme Database: 3.6.5.5
            ERGO genome analysis and discovery system: 3.6.5.5
            BRENDA, the Enzyme Database: 3.6.5.5
///
ENTRY       EC 3.6.5.6                  Enzyme
NAME        tubulin GTPase
CLASS       Hydrolases;
            Acting on acid anhydrides;
            Acting on GTP to facilitate cellular and subcellular movement
SYSNAME     GTP phosphohydrolase (microtubule-releasing)
REACTION    GTP + H2O = GDP + phosphate [RN:R00335]
ALL_REAC    R00335
SUBSTRATE   GTP [CPD:C00044];
            H2O [CPD:C00001]
PRODUCT     GDP [CPD:C00035];
            phosphate [CPD:C00009]
COMMENT     An intrinsic activity of alpha-tubulin involved in tubulin folding,
            division plane formation in prokaryotic cells and others.
REFERENCE   1  [PMID:9312004]
  AUTHORS   Yu XC, Margolin W.
  TITLE     Ca2+-mediated GTP-dependent dynamic assembly of bacterial cell
            division protein FtsZ into asters and polymer networks in vitro.
  JOURNAL   EMBO. J. 16 (1997) 5455-63.
REFERENCE   2  [PMID:10446175]
  AUTHORS   Tian G, Bhamidipati A, Cowan NJ, Lewis SA.
  TITLE     Tubulin folding cofactors as GTPase-activating proteins. GTP
            hydrolysis and the assembly of the alpha/beta-tubulin heterodimer.
  JOURNAL   J. Biol. Chem. 274 (1999) 24054-8.
  ORGANISM  cow [GN:bta], mouse [GN:mmu]
REFERENCE   3  [PMID:10224115]
  AUTHORS   Roychowdhury S, Panda D, Wilson L, Rasenick MM.
  TITLE     G protein alpha subunits activate tubulin GTPase and modulate
            microtubule polymerization dynamics.
  JOURNAL   J. Biol. Chem. 274 (1999) 13485-90.
  ORGANISM  cow [GN:bta], sheep
DBLINKS     IUBMB Enzyme Nomenclature: 3.6.5.6
            ExPASy - ENZYME nomenclature database: 3.6.5.6
            ExplorEnz - The Enzyme Database: 3.6.5.6
            ERGO genome analysis and discovery system: 3.6.5.6
            BRENDA, the Enzyme Database: 3.6.5.6
///
ENTRY       EC 3.7.1.1                  Enzyme
NAME        oxaloacetase;
            oxalacetic hydrolase
CLASS       Hydrolases;
            Acting on carbon-carbon bonds;
            In ketonic substances
SYSNAME     oxaloacetate acetylhydrolase
REACTION    oxaloacetate + H2O = oxalate + acetate [RN:R00338]
ALL_REAC    R00338
SUBSTRATE   oxaloacetate [CPD:C00036];
            H2O [CPD:C00001]
PRODUCT     oxalate [CPD:C00209];
            acetate [CPD:C00033]
REFERENCE   1
  AUTHORS   Hayaishi, O., Shimazono, H., Katagiri, M. and Saito, Y.
  TITLE     Enzymatic formation of oxalate and acetate from oxaloacetate.
  JOURNAL   J. Am. Chem. Soc. 78 (1956) 5126-5127.
  ORGANISM  Aspergillus niger
DBLINKS     IUBMB Enzyme Nomenclature: 3.7.1.1
            ExPASy - ENZYME nomenclature database: 3.7.1.1
            ExplorEnz - The Enzyme Database: 3.7.1.1
            ERGO genome analysis and discovery system: 3.7.1.1
            BRENDA, the Enzyme Database: 3.7.1.1
            CAS: 9024-89-9
///
ENTRY       EC 3.7.1.2                  Enzyme
NAME        fumarylacetoacetase;
            beta-diketonase;
            fumarylacetoacetate hydrolase
CLASS       Hydrolases;
            Acting on carbon-carbon bonds;
            In ketonic substances
SYSNAME     4-fumarylacetoacetate fumarylhydrolase
REACTION    4-fumarylacetoacetate + H2O = acetoacetate + fumarate [RN:R01364]
ALL_REAC    R01364
SUBSTRATE   4-fumarylacetoacetate [CPD:C01061];
            H2O [CPD:C00001]
PRODUCT     acetoacetate [CPD:C00164];
            fumarate [CPD:C00122]
COMMENT     Also acts on other 3,5- and 2,4-dioxo acids.
REFERENCE   1
  AUTHORS   Connors, W.M. and Stotz, E.
  TITLE     The purification and properties of a triacetic acid-hydrolyzing
            enzyme.
  JOURNAL   J. Biol. Chem. 178 (1949) 881-890.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:13319328]
  AUTHORS   EDWARDS SW, KNOX WE.
  TITLE     Homogentisate metabolism:  the isomerization of maleylacetoacetate
            by an enzyme which requires glutathione.
  JOURNAL   J. Biol. Chem. 220 (1956) 79-91.
  ORGANISM  cow [GN:bta], rat [GN:rno]
REFERENCE   3
  AUTHORS   Meister, A. and Greenstein, J.P.
  TITLE     Enzymatic hydrolysis of 2,4-diketo acids.
  JOURNAL   J. Biol. Chem. 175 (1948) 573-588.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00643  Styrene degradation
ORTHOLOGY   KO: K01555  fumarylacetoacetase
GENES       HSA: 2184(FAH)
            PTR: 467738(FAH)
            MMU: 14085(Fah)
            RNO: 29383(Fah)
            CFA: 610140(FAH)
            GGA: 415482(FAH)
            XLA: 380150(fah)
            DRE: 322372(fah)
            SPU: 582493(LOC582493)
            DME: Dmel_CG14993(Faa)
            CEL: K10C2.4(fumarylacetoacetase)
            ATH: AT1G12050
            OSA: 4328618
            CME: CMQ154C
            ANI: AN1896.2
            AFM: AFUA_2G04230
            AOR: AO090003000211
            UMA: UM01423.1
            TET: TTHERM_00044990
            XCC: XCC0591(uptA)
            XCB: XC_3642
            XCV: XCV3732(uptA)
            XAC: XAC3609(uptA)
            XOO: XOO0771(uptA)
            XOM: XOO_0701(XOO0701)
            PAE: PA2008(fahA)
            PAU: PA14_38530(fahA)
            PAP: PSPA7_3281(fahA)
            PPU: PP_4620
            PPF: Pput_4480
            PST: PSPTO_3550(fahA)
            PSB: Psyr_3325
            PSP: PSPPH_3245(fahA)
            PFL: PFL_0968(fahA)
            PFO: Pfl_0911
            PEN: PSEEN4611(fah)
            PCR: Pcryo_1558
            PRW: PsycPRwf_1038
            ACI: ACIAD3577 ACIAD3578
            PHA: PSHAa2169(fah)
            PAT: Patl_1123
            MMW: Mmwyl1_2735
            RSO: RS01759(RSp0690)
            REU: Reut_A1794 Reut_B3924
            REH: H16_A0361 H16_B0324 H16_B1670(fahA)
            RME: Rmet_4375
            BMA: BMA2055(fahA)
            BMV: BMASAVP1_A0857(fahA)
            BML: BMA10299_A2689(fahA)
            BMN: BMA10247_1920(fahA)
            BXE: Bxe_A2724 Bxe_A3899 Bxe_B2528 Bxe_C0995
            BVI: Bcep1808_0758
            BUR: Bcep18194_A3914 Bcep18194_C7461
            BCN: Bcen_0338 Bcen_5612
            BCH: Bcen2424_0821 Bcen2424_5976
            BAM: Bamb_0702
            BPS: BPSL2738
            BPM: BURPS1710b_3227(fahA)
            BPL: BURPS1106A_3212(fahA)
            BPD: BURPS668_3173(fahA)
            BTE: BTH_I1398(fahA)
            BPE: BP3135(fahA)
            BPA: BPP0806(fahA)
            BBR: BB0891(fahA)
            POL: Bpro_2996
            PNA: Pnap_1118
            AAV: Aave_0256
            RLE: RL1865 pRL90298
            BJA: bll0342(fah)
            BRA: BRADO3702 BRADO6964(fahA)
            BBT: BBta_0567(fahA) BBta_1939 BBta_2632
            RPA: RPA4670(fahA)
            RPB: RPB_0909
            RPC: RPC_0892
            RPD: RPD_1020
            RPE: RPE_0913
            NHA: Nham_0926
            XAU: Xaut_3332
            SIL: SPO0685(hmgB)
            SIT: TM1040_2622
            JAN: Jann_1436
            RDE: RD1_3653(fahA)
            PDE: Pden_3548
            NAR: Saro_2463
            SWI: Swit_1558 Swit_1685 Swit_3863
            ACR: Acry_1081
            ABA: Acid345_2007
            SUS: Acid_6516
            BCE: BC0253
            BCZ: BCZK0216 BCZK1048
            BTL: BALH_0226(hpcE)
            NFA: nfa53050
            RHA: RHA1_ro02309
            SCO: SCO4580(SCD16A.03)
            SMA: SAV4858(fahA)
            NCA: Noca_0655
            SEN: SACE_0136(fahA) SACE_3410 SACE_3942(fahA)
            STP: Strop_4256
            LIL: LA1074
            LIC: LIC12595
            SRU: SRU_2360(fahA)
            GFO: GFO_2263
            FJO: Fjoh_3411
            FPS: FP0680(fahA)
            PTO: PTO1370
STRUCTURES  PDB: 1HYO  1QCN  1QCO  1QQJ  2HZY  
DBLINKS     IUBMB Enzyme Nomenclature: 3.7.1.2
            ExPASy - ENZYME nomenclature database: 3.7.1.2
            ExplorEnz - The Enzyme Database: 3.7.1.2
            ERGO genome analysis and discovery system: 3.7.1.2
            UM-BBD (Biocatalysis/Biodegradation Database): 3.7.1.2
            BRENDA, the Enzyme Database: 3.7.1.2
            CAS: 9032-59-1
///
ENTRY       EC 3.7.1.3                  Enzyme
NAME        kynureninase
CLASS       Hydrolases;
            Acting on carbon-carbon bonds;
            In ketonic substances
SYSNAME     L-kynurenine hydrolase
REACTION    L-kynurenine + H2O = anthranilate + L-alanine [RN:R00987]
ALL_REAC    R00987;
            (other) R02668 R03936
SUBSTRATE   L-kynurenine [CPD:C00328];
            H2O [CPD:C00001]
PRODUCT     anthranilate [CPD:C00108];
            L-alanine [CPD:C00041]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also acts on 3'-hydroxy-L-kynurenine
            and some other (3-arylcarbonyl)-alanines.
REFERENCE   1  [PMID:13129248]
  AUTHORS   JAKOBY WB, BONNER DM.
  TITLE     Kynureninase from Neurospora: purification and properties.
  JOURNAL   J. Biol. Chem. 205 (1953) 699-707.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2  [PMID:13129249]
  AUTHORS   JAKOBY WB, BONNER DM.
  TITLE     Kynureninase from Neurospora: interaction of enzyme with substrates,
            coenzyme, and amines.
  JOURNAL   J. Biol. Chem. 205 (1953) 709-15.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   3  [PMID:13032082]
  AUTHORS   KNOX WE.
  TITLE     The relation of liver kynureninase to tryptophan metabolism in
            pyridoxine deficiency.
  JOURNAL   Biochem. J. 53 (1953) 379-85.
  ORGANISM  rat [GN:rno]
REFERENCE   4
  AUTHORS   Wiss, O. and Weber, F.
  TITLE     Die Reindarstellung der Kynureninase.
  JOURNAL   Hoppe-Seyler's Z. Physiol. Chem. 304 (1956) 232-240.
PATHWAY     PATH: map00380  Tryptophan metabolism
ORTHOLOGY   KO: K01556  kynureninase
GENES       HSA: 8942(KYNU)
            MMU: 70789(Kynu)
            RNO: 116682(Kynu)
            CFA: 483907(KYNU)
            GGA: 424302(KYNU)
            SPU: 580378(LOC580378)
            CEL: C15H9.7(kynureninase)
            CME: CMF128C
            AGO: AGOS_AGL098W
            PIC: PICST_55542(BNA5)
            ANI: AN1857.2 AN5952.2
            AFM: AFUA_2G10360 AFUA_4G09840
            AOR: AO090003001247 AO090011000602
            CNE: CNC03980
            DDI: DDB_0231361(kynU)
            TBR: Tb09.160.0810
            TCR: 503881.10
            LMA: LmjF26.2240
            XCC: XCC1553
            XCB: XC_2681
            XCV: XCV1642
            XAC: XAC1601
            XOO: XOO2428
            XOM: XOO_2305(XOO2305)
            PAU: PA14_37610
            PAP: PSPA7_3208(kynU)
            PFL: PFL_0762(kynU)
            PAT: Patl_2921
            REU: Reut_A0808
            REH: H16_A2815(kynU)
            RME: Rmet_2650 Rmet_5192
            BMA: BMA0352
            BMV: BMASAVP1_A0651(kynU)
            BML: BMA10299_A2486(kynU)
            BMN: BMA10247_0099(kynU)
            BXE: Bxe_A0734
            BUR: Bcep18194_A5909 Bcep18194_C7639
            BCN: Bcen_1967
            BCH: Bcen2424_2578
            BAM: Bamb_2626
            BPS: BPSL0847
            BPM: BURPS1710b_1054(kynU)
            BPL: BURPS1106A_0896(kynU)
            BPD: BURPS668_0893(kynU)
            BTE: BTH_I0710(kynU)
            POL: Bpro_3589
            LIP: LI0415
            MXA: MXAN_0917(kynU)
            MLO: mll0621
            BJA: blr4159
            BRA: BRADO1528
            BBT: BBta_6512
            SIL: SPO2824(kynU)
            SIT: TM1040_2225
            RSP: RSP_0242
            JAN: Jann_2085
            RDE: RD1_3643(kynU)
            MMR: Mmar10_1471
            ABA: Acid345_0680
            BAN: BA2753(kynU)
            BAR: GBAA2753(kynU)
            BAA: BA_3279
            BAT: BAS2567
            BCE: BC2759
            BCA: BCE_2787(kynU)
            BCZ: BCZK2488(kynU)
            BTK: BT9727_2523(kynU)
            BTL: BALH_2478(kynU)
            BCL: ABC0651
            OIH: OB0756
            RHA: RHA1_ro01800
            SEN: SACE_0279 SACE_4057
            CCA: CCA00568(kynU)
            CFE: CF0434(kynU)
            GFO: GFO_2720
            FPS: FP2215(kynU)
            DGE: Dgeo_1534
STRUCTURES  PDB: 1QZ9  2HZP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.7.1.3
            ExPASy - ENZYME nomenclature database: 3.7.1.3
            ExplorEnz - The Enzyme Database: 3.7.1.3
            ERGO genome analysis and discovery system: 3.7.1.3
            BRENDA, the Enzyme Database: 3.7.1.3
            CAS: 9024-78-6
///
ENTRY       EC 3.7.1.4                  Enzyme
NAME        phloretin hydrolase;
            lactase-phlorizin hydrolase
CLASS       Hydrolases;
            Acting on carbon-carbon bonds;
            In ketonic substances
SYSNAME     2',4,4',6'-tetrahydroxydehydrochalcone
            1,3,5-trihydroxybenzenehydrolase
REACTION    phloretin + H2O = phloretate + phloroglucinol [RN:R02901]
ALL_REAC    R02901
SUBSTRATE   phloretin [CPD:C00774];
            H2O [CPD:C00001]
PRODUCT     phloretate [CPD:C01744];
            phloroglucinol [CPD:C02183]
COMMENT     Also hydrolyses other C-acylated phenols related to phloretin.
REFERENCE   1  [PMID:5441377]
  AUTHORS   Minamikawa T, Jayasankar NP, Bohm BA, Taylor IE, Towers GH.
  TITLE     An inducible hydrolase from Aspergillus niger, acting on
            carbon-carbon bonds, for phlorrhizin and other C-acylated phenols.
  JOURNAL   Biochem. J. 116 (1970) 889-97.
  ORGANISM  Aspergillus niger
DBLINKS     IUBMB Enzyme Nomenclature: 3.7.1.4
            ExPASy - ENZYME nomenclature database: 3.7.1.4
            ExplorEnz - The Enzyme Database: 3.7.1.4
            ERGO genome analysis and discovery system: 3.7.1.4
            BRENDA, the Enzyme Database: 3.7.1.4
            CAS: 37289-38-6
///
ENTRY       EC 3.7.1.5                  Enzyme
NAME        acylpyruvate hydrolase
CLASS       Hydrolases;
            Acting on carbon-carbon bonds;
            In ketonic substances
SYSNAME     3-acylpyruvate acylhydrolase
REACTION    a 3-acylpyruvate + H2O = a carboxylate + pyruvate [RN:R00543]
ALL_REAC    R00543 > R01085
SUBSTRATE   3-acylpyruvate [CPD:C02119];
            H2O [CPD:C00001]
PRODUCT     carboxylate [CPD:C00060];
            pyruvate [CPD:C00022]
COMMENT     Acts on formylpyruvate, 2,4-dioxopentanoate, 2,4-dioxohexanoate and
            2,4-dioxoheptanoate.
REFERENCE   1  [PMID:4375963]
  AUTHORS   Watson GK, Houghton C, Cain RB.
  TITLE     Microbial metabolism of the pyridine ring. The metabolism of
            pyridine-3,4-diol (3,4-dihydroxypyridine) by Agrobacterium sp.
  JOURNAL   Biochem. J. 140 (1974) 277-92.
  ORGANISM  Agrobacterium sp.
PATHWAY     PATH: map00350  Tyrosine metabolism
ORTHOLOGY   KO: K01557  acylpyruvate hydrolase
GENES       PIC: PICST_80437(YNQ8)
            CGR: CAGL0J06204g
            PEN: PSEEN2594(mhbB)
            REH: H16_B0428 H16_B0874
            BPM: BURPS1710b_A0012
            RET: RHE_CH02701
            RLE: RL3169
            BME: BMEI1882
            BMF: BAB1_0060
            RDE: RD1_1348
            GBE: GbCGDNIH1_2003
DBLINKS     IUBMB Enzyme Nomenclature: 3.7.1.5
            ExPASy - ENZYME nomenclature database: 3.7.1.5
            ExplorEnz - The Enzyme Database: 3.7.1.5
            ERGO genome analysis and discovery system: 3.7.1.5
            BRENDA, the Enzyme Database: 3.7.1.5
            CAS: 54004-67-0
///
ENTRY       EC 3.7.1.6                  Enzyme
NAME        acetylpyruvate hydrolase
CLASS       Hydrolases;
            Acting on carbon-carbon bonds;
            In ketonic substances
SYSNAME     2,4-dioxopentanoate acetylhydrolase
REACTION    acetylpyruvate + H2O = acetate + pyruvate [RN:R00324]
ALL_REAC    R00324
SUBSTRATE   acetylpyruvate [CPD:C02132];
            H2O [CPD:C00001]
PRODUCT     acetate [CPD:C00033];
            pyruvate [CPD:C00022]
COMMENT     Highly specific; does not act on pyruvate, oxaloacetate,
            maleylpyruvate, fumarylpyruvate or acetylacetone.
REFERENCE   1  [PMID:236305]
  AUTHORS   Davey JF, Ribbons DW.
  TITLE     Metabolism of resorcinylic compounds by bacteria. Purification and
            properties of acetylpyruvate hydrolase from Pseudomonas putida 01.
  JOURNAL   J. Biol. Chem. 250 (1975) 3826-30.
  ORGANISM  Pseudomonas putida [GN:ppu]
DBLINKS     IUBMB Enzyme Nomenclature: 3.7.1.6
            ExPASy - ENZYME nomenclature database: 3.7.1.6
            ExplorEnz - The Enzyme Database: 3.7.1.6
            ERGO genome analysis and discovery system: 3.7.1.6
            UM-BBD (Biocatalysis/Biodegradation Database): 3.7.1.6
            BRENDA, the Enzyme Database: 3.7.1.6
            CAS: 56214-30-3
///
ENTRY       EC 3.7.1.7                  Enzyme
NAME        beta-diketone hydrolase;
            oxidized PVA hydrolase
CLASS       Hydrolases;
            Acting on carbon-carbon bonds;
            In ketonic substances
SYSNAME     nonane-4,6-dione acylhydrolase
REACTION    nonane-4,6-dione + H2O = pentan-2-one + butanoate [RN:R03781]
ALL_REAC    R03781
SUBSTRATE   nonane-4,6-dione [CPD:C02445];
            H2O [CPD:C00001]
PRODUCT     pentan-2-one [CPD:C01949];
            butanoate [CPD:C00246]
COMMENT     Also acts on the product of the action of EC 1.1.3.18
            secondary-alcohol oxidase, on polyvinyl alcohols; involved in the
            bacterial degradation of polyvinyl alcohol.
REFERENCE   1
  AUTHORS   Sakai, K., Hamada, N. and Watanabe, Y.
  TITLE     Separation of secondary alcohol oxidase and oxidized poly(vinyl
            alcohol) hydrolase by hydrophobic and dye-ligand chromatographies.
  JOURNAL   Agric. Biol. Chem. 47 (1983) 153-155.
REFERENCE   2
  AUTHORS   Sakai, K., Hamada, N. and Watanabe, Y.
  TITLE     A new enzyme, beta-diketone hydrolase: a component of a poly(vinyl
            alcohol)-degrading enzyme preparation.
  JOURNAL   Agric. Biol. Chem. 49 (1985) 1901-1902.
  ORGANISM  Pseudomonas. sp
STRUCTURES  PDB: 2J5G  2J5S  
DBLINKS     IUBMB Enzyme Nomenclature: 3.7.1.7
            ExPASy - ENZYME nomenclature database: 3.7.1.7
            ExplorEnz - The Enzyme Database: 3.7.1.7
            ERGO genome analysis and discovery system: 3.7.1.7
            BRENDA, the Enzyme Database: 3.7.1.7
            CAS: 97955-12-9
///
ENTRY       EC 3.7.1.8                  Enzyme
NAME        2,6-dioxo-6-phenylhexa-3-enoate hydrolase;
            HOHPDA hydrolase
CLASS       Hydrolases;
            Acting on carbon-carbon bonds;
            In ketonic substances
SYSNAME     2,6-dioxo-6-phenylhexa-3-enoate benzoylhydrolase
REACTION    2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate +
            2-oxopent-4-enoate [RN:R02606]
ALL_REAC    R02606;
            (other) R05359 R05360 R05361
SUBSTRATE   2,6-dioxo-6-phenylhexa-3-enoate [CPD:C01273];
            H2O [CPD:C00001]
PRODUCT     benzoate [CPD:C00180];
            2-oxopent-4-enoate [CPD:C00596]
COMMENT     Cleaves the products from biphenol, 3-isopropylcatechol and
            3-methylcatechol produced by EC 1.13.11.39 biphenyl-2,3-diol
            1,2-dioxygenase, by ring-fission at a -CO-C bond. Involved in the
            breakdown of biphenyl-related compounds by Pseudomonas sp.
REFERENCE   1
  AUTHORS   Omori, T., Sugimura, K., Ishigooka, H. and Minoda, Y.
  TITLE     Purification and some properties of a
            2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolyzing enzyme
            from Pseudomonas cruciviae S93 B1 involved in the degradation of
            biphenyl.
  JOURNAL   Agric. Biol. Chem. 50 (1986) 931-937.
  ORGANISM  Pseudomonas cruciviae
PATHWAY     PATH: map00621  Biphenyl degradation
            PATH: map00628  Fluorene degradation
ORTHOLOGY   KO: K10222  2,6-dioxo-6-phenylhexa-3-enoate hydrolase
GENES       REH: H16_B0600(bphD)
            BXE: Bxe_C1186(bphD)
            RHA: RHA1_ro10136(bphD1)
STRUCTURES  PDB: 1C4X  1J1I  2OG1  
DBLINKS     IUBMB Enzyme Nomenclature: 3.7.1.8
            ExPASy - ENZYME nomenclature database: 3.7.1.8
            ExplorEnz - The Enzyme Database: 3.7.1.8
            ERGO genome analysis and discovery system: 3.7.1.8
            UM-BBD (Biocatalysis/Biodegradation Database): 3.7.1.8
            BRENDA, the Enzyme Database: 3.7.1.8
            CAS: 102925-38-2
///
ENTRY       EC 3.7.1.9                  Enzyme
NAME        2-hydroxymuconate-semialdehyde hydrolase;
            2-hydroxy-6-oxohepta-2,4-dienoate hydrolase;
            2-hydroxymuconic semialdehyde hydrolase;
            HMSH;
            HOD hydrolase
CLASS       Hydrolases;
            Acting on carbon-carbon bonds;
            In ketonic substances
SYSNAME     2-hydroxymuconate-semialdehyde formylhydrolase
REACTION    2-hydroxymuconate semialdehyde + H2O = formate + 2-oxopent-4-enoate
            [RN:R02604]
ALL_REAC    R02604;
            (other) R05296 R05362 R05865
SUBSTRATE   2-hydroxymuconate semialdehyde [CPD:C00682];
            H2O [CPD:C00001]
PRODUCT     formate [CPD:C00058];
            2-oxopent-4-enoate [CPD:C00596]
REFERENCE   1
  AUTHORS   Harayama, S., Rekik, M., Wasserfallen, A. and Bairoch, A.
  TITLE     Evolutionary relationships between catabolic pathways for aromatics:
            conservtion of gene order and nucleotide sequences of catechol
            oxidation genes of pWW0 and NAH7 plasmids.
  JOURNAL   MGG Mol. Gen. Genet. 210 (1987) 241-247.
REFERENCE   2  [PMID:4325686]
  AUTHORS   Sala-Trepat JM, Evans WC.
  TITLE     The meta cleavage of catechol by Azotobacter species.
            4-Oxalocrotonate pathway.
  JOURNAL   Eur. J. Biochem. 20 (1971) 400-13.
  ORGANISM  Azotobacter sp.
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00622  Toluene and xylene degradation
            PATH: map00627  1,4-Dichlorobenzene degradation
            PATH: map00629  Carbazole degradation
            PATH: map00643  Styrene degradation
ORTHOLOGY   KO: K10216  2-hydroxymuconate-semialdehyde hydrolase
GENES       AZO: azo1968(xylF)
STRUCTURES  PDB: 1IUN  1IUO  1IUP  1UK6  1UK7  1UK8  1UK9  1UKA  1UKB  2D0D  
DBLINKS     IUBMB Enzyme Nomenclature: 3.7.1.9
            ExPASy - ENZYME nomenclature database: 3.7.1.9
            ExplorEnz - The Enzyme Database: 3.7.1.9
            ERGO genome analysis and discovery system: 3.7.1.9
            UM-BBD (Biocatalysis/Biodegradation Database): 3.7.1.9
            BRENDA, the Enzyme Database: 3.7.1.9
            CAS: 54004-61-4
///
ENTRY       EC 3.7.1.10                 Enzyme
NAME        cyclohexane-1,3-dione hydrolase;
            1,3-cyclohexanedione hydrolase
CLASS       Hydrolases;
            Acting on carbon-carbon bonds;
            In ketonic substances
SYSNAME     cyclohexane-1,3-dione acylhydrolase (decyclizing)
REACTION    cyclohexane-1,3-dione + H2O = 5-oxohexanoate [RN:R03211]
ALL_REAC    R03211
SUBSTRATE   cyclohexane-1,3-dione [CPD:C01066];
            H2O [CPD:C00001]
PRODUCT     5-oxohexanoate [CPD:C02129]
COMMENT     Highly specific; does not act on other dione derivatives of
            cyclohexane, cyclopentane or cycloheptane.
REFERENCE   1
  AUTHORS   Dangel, W., Tschech, A. and Fuchs, G.
  TITLE     Enzyme-reactions involved in anaerobic cyclohexanol metabolism by a
            denitrifying Pseudomonas species.
  JOURNAL   Arch. Microbiol. 152 (1989) 273-279.
  ORGANISM  Pseudomonas. sp
DBLINKS     IUBMB Enzyme Nomenclature: 3.7.1.10
            ExPASy - ENZYME nomenclature database: 3.7.1.10
            ExplorEnz - The Enzyme Database: 3.7.1.10
            ERGO genome analysis and discovery system: 3.7.1.10
            BRENDA, the Enzyme Database: 3.7.1.10
            CAS: 123516-46-1
///
ENTRY       EC 3.7.1.-                  Enzyme
CLASS       Hydrolases;
            Acting on carbon-carbon bonds;
            In ketonic substances
REACTION    (1) Glycolate + Pyruvate <=> (4S)-5-Hydroxy-2,4-dioxopentanoate +
            H2O [RN:R01335];
            (2) 2-Hydroxy-2,4-pentadienoate + Succinate <=>
            2-Hydroxy-6-oxonona-2,4-diene-1,9-dioate + H2O [RN:R02603];
            (3) 4-Carboxy-2-hydroxymuconate semialdehyde + H2O <=>
            4-Carboxy-2-oxo-4-pentanoate + Formate [RN:R04488];
            (4) Adipate semialdehyde <=> Cyclohexan-1,2-dione + H2O [RN:R05100];
            (5) 2-Hydroxy-2,4-pentadienoate + Acetate <=>
            2-Hydroxy-6-keto-2,4-heptadienoate + H2O [RN:R05138];
            (6)
            6-Oxo-2-hydroxy-7-(4'-chlorophenyl)-3,8,8-trichloroocta-2E,4E,7E-
            trienoate + H2O <=> 2-(4'-Chlorophenyl)-3,3-dichloropropenoate +
            2-Hydroxy-3-chloropenta-2,4-dienoate [RN:R05363];
            (7) 2-Hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O <=>
            2-Methylpropanoate + 2-Hydroxy-2,4-pentadienoate [RN:R05364];
            (8) 2-Hydroxy-6-oxo-(2'-aminophenyl)-hexa-2,4-dienoate + H2O <=>
            2-Hydroxy-2,4-pentadienoate + Anthranilate [RN:R05365];
            (9) 2-Hydroxy-6-oxo-octa-2,4-dienoate + H2O <=>
            2-Hydroxy-2,4-pentadienoate + Propanoate + H+ [RN:R05366];
            (10) 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA + 2 H2O <=>
            3-Hydroxypimeloyl-CoA [RN:R05594];
            (11) 4-Isopropenyl-2-oxy-cyclohexanecarboxyl-CoA + H2O <=>
            3-Isopropenylpimelyl-CoA [RN:R06371];
            (12) 2-Hydroxy-6-ketononatrienedioate + H2O <=>
            2-Hydroxy-2,4-pentadienoate + Fumarate [RN:R06789];
            (13) 2,6-Dihydroxypseudooxynicotine + H2O <=> 2,6-Dihydroxypyridine
            + 4-Methylaminobutyrate [RN:R07515];
            (14) 2-Hydroxy-6-oxo-6-(2-carboxyphenyl)-hexa-2,4-dienoate + H2O <=>
            Phthalate + 2-Hydroxy-2,4-pentadienoate [RN:R07802];
            (15) Dihydrophloroglucinol + H2O <=> 3-Hydroxy-5-oxohexanoate
            [RN:R07831]
SUBSTRATE   Glycolate [CPD:C00160];
            Pyruvate [CPD:C00022];
            2-Hydroxy-2,4-pentadienoate [CPD:C00596];
            Succinate [CPD:C00042];
            4-Carboxy-2-hydroxymuconate semialdehyde [CPD:C04484];
            H2O [CPD:C00001];
            Adipate semialdehyde [CPD:C06102];
            Acetate [CPD:C00033];
            6-Oxo-2-hydroxy-7-(4'-chlorophenyl)-3,8,8-trichloroocta-2E,4E,7E-
            trienoate [CPD:C06645];
            2-Hydroxy-6-oxo-7-methylocta-2,4-dienoate [CPD:C06582];
            2-Hydroxy-6-oxo-(2'-aminophenyl)-hexa-2,4-dienoate [CPD:C08062];
            2-Hydroxy-6-oxo-octa-2,4-dienoate [CPD:C07123];
            6-Ketoxycyclohex-1-ene-1-carboxyl-CoA [CPD:C09821];
            4-Isopropenyl-2-oxy-cyclohexanecarboxyl-CoA [CPD:C11935];
            2-Hydroxy-6-ketononatrienedioate [CPD:C12624]
PRODUCT     (4S)-5-Hydroxy-2,4-dioxopentanoate [CPD:C05406];
            H2O [CPD:C00001];
            2-Hydroxy-6-oxonona-2,4-diene-1,9-dioate [CPD:C04479];
            4-Carboxy-2-oxo-4-pentanoate [CPD:C05854];
            Formate [CPD:C00058];
            Cyclohexan-1,2-dione [CPD:C06105];
            2-Hydroxy-6-keto-2,4-heptadienoate [CPD:C06210];
            2-(4'-Chlorophenyl)-3,3-dichloropropenoate [CPD:C06646];
            2-Hydroxy-3-chloropenta-2,4-dienoate [CPD:C11353];
            2-Methylpropanoate [CPD:C02632];
            2-Hydroxy-2,4-pentadienoate [CPD:C00596];
            Anthranilate [CPD:C00108];
            Propanoate [CPD:C00163];
            H+ [CPD:C00080];
            3-Hydroxypimeloyl-CoA [CPD:C06714];
            3-Isopropenylpimelyl-CoA [CPD:C11936];
            Fumarate [CPD:C00122]
///
ENTRY       EC 3.8.1.1                  Enzyme
NAME        alkylhalidase;
            halogenase;
            haloalkane halidohydrolase;
            haloalkane dehalogenase
CLASS       Hydrolases;
            Acting on halide bonds;
            In carbon-halide compounds
SYSNAME     alkyl-halide halidohydrolase
REACTION    bromochloromethane + H2O = formaldehyde + bromide + chloride
            [RN:R03523]
ALL_REAC    R03523
SUBSTRATE   bromochloromethane [CPD:C02661];
            H2O [CPD:C00001]
PRODUCT     formaldehyde [CPD:C00067];
            bromide [CPD:C01324];
            chloride [CPD:C00115]
REFERENCE   1
  AUTHORS   Heppel, L.A. and Porterfield, V.T.
  TITLE     Enzymatic dehalogenation of certain brominated and chlorinated
            compounds.
  JOURNAL   J. Biol. Chem. 176 (1948) 763-769.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K06031  
GENES       PFL: PFL_2784 PFL_2787 PFL_3606(prnC)
            BMA: BMAA1201(prnC)
            BPS: BPSS1010
            BPM: BURPS1710b_A0003(prnC) BURPS1710b_A1117(prnC)
            SCO: SCO1275(2SCG18.22)
            RBA: RB1653(prnC) RB390 RB4288
DBLINKS     IUBMB Enzyme Nomenclature: 3.8.1.1
            ExPASy - ENZYME nomenclature database: 3.8.1.1
            ExplorEnz - The Enzyme Database: 3.8.1.1
            ERGO genome analysis and discovery system: 3.8.1.1
            BRENDA, the Enzyme Database: 3.8.1.1
            CAS: 9025-22-3
///
ENTRY       EC 3.8.1.2                  Enzyme
NAME        (S)-2-haloacid dehalogenase;
            2-haloacid dehalogenase[ambiguous];
            2-haloacid halidohydrolase [ambiguous][ambiguous];
            2-haloalkanoic acid dehalogenase;
            2-haloalkanoid acid halidohydrolase;
            2-halocarboxylic acid dehalogenase II;
            DL-2-haloacid dehalogenase[ambiguous];
            L-2-haloacid dehalogenase;
            L-DEX
CLASS       Hydrolases;
            Acting on halide bonds;
            In carbon-halide compounds
SYSNAME     (S)-2-haloacid halidohydrolase
REACTION    (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide [RN:R03830]
ALL_REAC    R03830 > R05287
SUBSTRATE   (S)-2-haloacid [CPD:C02103];
            H2O [CPD:C00001]
PRODUCT     (R)-2-hydroxyacid [CPD:C02489];
            halide [CPD:C00462]
COMMENT     Acts on acids of short chain lengths, C2 to C4, with inversion of
            configuration at C-2. [See also EC 3.8.1.9 (R)-2-haloacid
            dehalogenase, EC 3.8.1.10 2-haloacid dehalogenase
            (configuration-inverting) and EC 3.8.1.11 2-haloacid dehalogenase
            (configuration-retaining)]
REFERENCE   1  [PMID:5635785]
  AUTHORS   Goldman P, Milne GW, Keister DB.
  TITLE     Carbon-halogen bond cleavage. 3. Studies on bacterial
            halidohrolases.
  JOURNAL   J. Biol. Chem. 243 (1968) 428-34.
REFERENCE   2
  AUTHORS   Motosugi, M., Esaki, N. and Soda, K.
  TITLE     Preparation and properties of 2-halo acid dehalogenase from
            Pseudomonas putida.
  JOURNAL   Agric. Biol. Chem. 46 (1982) 837-838.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   3  [PMID:6873881]
  AUTHORS   Klages U, Krauss S, Lingens F.
  TITLE     2-Haloacid dehalogenase from a 4-chlorobenzoate-degrading
            Pseudomonas spec. CBS 3.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 364 (1983) 529-35.
  ORGANISM  Pseudomonas sp.
REFERENCE   4  [PMID:8607850]
  AUTHORS   Diez A, Prieto MI, Alvarez MJ, Bautista JM, Garrido J, Puyet A.
  TITLE     Improved catalytic performance of a 2-haloacid dehalogenase from
            Azotobacter sp. by ion-exchange immobilisation.
  JOURNAL   Biochem. Biophys. Res. Commun. 220 (1996) 828-33.
  ORGANISM  Azotobacter sp.
REFERENCE   5  [PMID:1772590]
  AUTHORS   Morsberger FM, Muller R, Otto MK, Lingens F, Kulbe KD.
  TITLE     Purification and characterization of 2-halocarboxylic acid
            dehalogenase II from Pseudomonas spec. CBS 3.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 372 (1991) 915-22.
  ORGANISM  Pseudomonas sp.
REFERENCE   6  [PMID:9425247]
  AUTHORS   Kohler R, Brokamp A, Schwarze R, Reiting RH, Schmidt FR.
  TITLE     Characteristics and DNA-sequence of a cryptic haloalkanoic acid
            dehalogenase from Agrobacterium tumefaciens RS5.
  JOURNAL   Curr. Microbiol. 36 (1998) 96-101.
  ORGANISM  Agrobacterium tumefaciens
REFERENCE   7  [PMID:7103659]
  AUTHORS   Motosugi K, Esaki N, Soda K.
  TITLE     Bacterial assimilation of D- and L-2-chloropropionates and
            occurrence of a new dehalogenase.
  JOURNAL   Arch. Microbiol. 131 (1982) 179-83.
  ORGANISM  Pseudomonas sp.
REFERENCE   8
  AUTHORS   Kurihara, T., Esaki, N. and Soda, K.
  TITLE     Bacterial 2-haloacid dehalogenases: structures and reaction
            mechanisms.
  JOURNAL   J. Mol. Catal., B Enzym. 10 (2000) 57-65.
REFERENCE   9
  AUTHORS   Soda, K., Kurihara, T., Liu, J.-Q., Nardi-Dei, V., Park, C., Miyagi,
            M., Tsunasawa, S. and Esaki, N.
  TITLE     Bacterial 2-haloacid dehalogenases: Structures and catalytic
            properties.
  JOURNAL   Pure Appl. Chem. 68 (1996) 2097-2103.
  ORGANISM  Pseudomonas putida [GN:ppu], Pseudomonas sp.
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
            PATH: map00631  1,2-Dichloroethane degradation
ORTHOLOGY   KO: K01560  2-haloacid dehalogenase
GENES       ANI: AN5830.2 AN7918.2
            AFM: AFUA_2G07750 AFUA_5G14640 AFUA_8G05870
            AOR: AO090001000019 AO090003001435 AO090011000921
            UMA: UM02622.1
            ECA: ECA3957
            PAE: PA0810
            PAU: PA14_53790
            PAP: PSPA7_4708(dehII)
            PST: PSPTO_0247(dehII)
            PSB: Psyr_0159 Psyr_1791
            PSP: PSPPH_1747(dehII1) PSPPH_5028(dehII2)
            PFO: Pfl_3802
            PAR: Psyc_1396
            PCR: Pcryo_0968
            SFR: Sfri_2142 Sfri_3956
            ILO: IL1575(hadL)
            CPS: CPS_3130(dehII)
            PHA: PSHAa1832
            PAT: Patl_0275
            CSA: Csal_2713
            ABO: ABO_1537(dhlB)
            CVI: CV_0864
            RSO: RSc1362(RS04644)
            REU: Reut_A1952 Reut_B5659 Reut_B5662
            RME: Rmet_1389
            BMA: BMA1589(dheII) BMAA0223(dehII) BMAA0509
            BMV: BMASAVP1_1404(dehII-1) BMASAVP1_A2091(dehII-2)
            BML: BMA10299_1601(dehII-1) BMA10299_A3221(dehII-2)
            BMN: BMA10247_1364(dehII-2) BMA10247_A0260(dehII-1)
            BXE: Bxe_A0441 Bxe_A1648 Bxe_B1493 Bxe_C0774
            BVI: Bcep1808_1957
            BUR: Bcep18194_A3603 Bcep18194_A5360 Bcep18194_B2027
                 Bcep18194_B2556
            BCN: Bcen_2588 Bcen_4315 Bcen_6026 Bcen_6447
            BCH: Bcen2424_0516 Bcen2424_2051 Bcen2424_4051 Bcen2424_6682
            BAM: Bamb_0420 Bamb_2083 Bamb_3446 Bamb_6423
            BPS: BPSL2191 BPSL3068 BPSS1869
            BPM: BURPS1710b_2616(dehII) BURPS1710b_3596
                 BURPS1710b_A0962(dehII)
            BPL: BURPS1106A_2527(dehII) BURPS1106A_A2536(dehII)
            BPD: BURPS668_2474(dehII) BURPS668_A2680(dehII)
            BTE: BTH_I1995(dehII-1) BTH_I2925 BTH_II0507(dehII-2)
            PNU: Pnuc_2046
            BPE: BP2017
            BPA: BPP2397 BPP4207
            BBR: BB1847 BB4677
            RFR: Rfer_3582
            POL: Bpro_0056 Bpro_0530 Bpro_4516
            PNA: Pnap_3684
            MPT: Mpe_A0158
            HAR: HEAR0667(hadL) HEAR2653
            MMS: mma_0898
            EBA: ebA812
            AZO: azo0216(hadL)
            ADE: Adeh_3811
            PUB: SAR11_0137(dhlB)
            MLO: mll7522 mll7634 mlr7041
            MES: Meso_0764 Meso_0860
            SME: SMa1851 SMc00081
            SMD: Smed_0582
            ATU: Atu0797 Atu3405(hadL)
            ATC: AGR_C_1458 AGR_L_2834
            RET: RHE_CH00996 RHE_PF00342
            RLE: RL1077 pRL120620
            BME: BMEI1368 BMEI1443
            BMF: BAB1_0517 BAB1_0590
            BMS: BR0492 BR0565
            BMB: BruAb1_0514 BruAb1_0587
            BOV: BOV_0566(dehII)
            BJA: blr4364 blr7560(dhlB)
            BRA: BRADO1532 BRADO3574
            BBT: BBta_1654 BBta_3998
            RPA: RPA2507 RPA4199
            RPB: RPB_2963
            RPC: RPC_2814
            RPD: RPD_2498
            RPE: RPE_2935
            XAU: Xaut_0978
            SIL: SPO2473 SPOA0437(dehII)
            SIT: TM1040_2669 TM1040_3570
            JAN: Jann_0053 Jann_1658
            RDE: RD1_0322 RD1_3929(deh)
            NAR: Saro_2947
            ACR: Acry_3098
            MAG: amb2538
            ABA: Acid345_4292
            SUS: Acid_5126
            BAN: BA3392 BA5658
            BAR: GBAA3392 GBAA5658
            BAA: BA_0516 BA_3891
            BAT: BAS3145 BAS5260
            BCE: BC3334 BC5408
            BCA: BCE_3362 BCE_5537
            BCZ: BCZK3039 BCZK5105
            BTK: BT9727_3132 BT9727_5088
            BTL: BALH_3014 BALH_4908
            BLI: BL02712
            BLD: BLi00219(yfnB)
            BAY: RBAM_002470(yfnB)
            SSP: SSP0367
            LLC: LACR_0249 LACR_1604
            LLM: llmg_0254(hadL) llmg_2034
            SGO: SGO_2103
            LPL: lp_2835
            LSA: LSA0155 LSA0447
            LSL: LSL_0676
            LBR: LVIS_2192
            CAC: CAC1776
            CTC: CTC01925
            DSY: DSY1360
            MPA: MAP1728c(yfnB)
            MAV: MAV_2690(dehII)
            MSM: MSMEG_0115(dehII) MSMEG_3450(dehII) MSMEG_4059
            MMC: Mmcs_0093
            RHA: RHA1_ro00230
            SCO: SCO0404(SCF51.03) SCO3446(SCE46.03c)
            SMA: SAV737
            SEN: SACE_2965(dhlB) SACE_4364 SACE_4734(hadL)
            RXY: Rxyl_0508 Rxyl_1673
            RBA: RB4567(chd1)
            LIL: LA0080 LA0537 LA0929 LA1476
            LIC: LIC12279 LIC13027
            LBJ: LBJ_0977
            LBL: LBL_2056
            PMF: P9303_21781
            SRU: SRU_1260(dehII)
            GFO: GFO_3460
            HMA: rrnAC0241(hadL)
            HWA: HQ1755A(hadL)
            PHO: PH0459
            PAB: PAB1316
            PFU: PF0463
            TKO: TK0058
            HBU: Hbut_0596
            SSO: SSO0726 SSO1896 SSO2028 SSO2159
            STO: ST0436 ST2145 ST2620
            SAI: Saci_0018 Saci_0239 Saci_0602
STRUCTURES  PDB: 1AQ6  1JUD  1QH9  1QQ5  1QQ6  1QQ7  1ZRM  1ZRN  2NO4  2NO5  
DBLINKS     IUBMB Enzyme Nomenclature: 3.8.1.2
            ExPASy - ENZYME nomenclature database: 3.8.1.2
            ExplorEnz - The Enzyme Database: 3.8.1.2
            ERGO genome analysis and discovery system: 3.8.1.2
            UM-BBD (Biocatalysis/Biodegradation Database): 3.8.1.2
            BRENDA, the Enzyme Database: 3.8.1.2
            CAS: 37289-39-7
///
ENTRY       EC 3.8.1.3                  Enzyme
NAME        haloacetate dehalogenase;
            monohaloacetate dehalogenase
CLASS       Hydrolases;
            Acting on halide bonds;
            In carbon-halide compounds
SYSNAME     haloacetate halidohydrolase
REACTION    haloacetate + H2O = glycolate + halide [RN:R02336]
ALL_REAC    R02336 > R05287
SUBSTRATE   haloacetate [CPD:C01812];
            H2O [CPD:C00001]
PRODUCT     glycolate [CPD:C00160];
            halide [CPD:C00462]
REFERENCE   1  [PMID:14321384]
  AUTHORS   GOLDMAN P.
  TITLE     THE ENZYMATIC CLEAVAGE OF THE CARBON-FLUORINE BOND IN FLUOROACETATE.
  JOURNAL   J. Biol. Chem. 240 (1965) 3434-8.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:5928195]
  AUTHORS   Goldman P, Milne GW.
  TITLE     Carbon-fluorine bond cleavage. II. Studies on the mechanism of the
            defluorination of fluoroacetate.
  JOURNAL   J. Biol. Chem. 241 (1966) 5557-9.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
            PATH: map00631  1,2-Dichloroethane degradation
ORTHOLOGY   KO: K01561  haloacetate dehalogenase
GENES       RSO: RSc0256(dehH)
            BXE: Bxe_A4275
            BUR: Bcep18194_A6314 Bcep18194_B1142
            BAM: Bamb_3012
            BPS: BPSL0329
            BPM: BURPS1710b_0537(dehH)
            BTE: BTH_I0308
            HAR: HEAR0772
            AZO: azo0046(dehH)
            RET: RHE_PF00268
            BJA: bll7497
            RDE: RD1_2829(dehH1)
            MSM: MSMEG_1984
            SEN: SACE_2847
            AVA: Ava_2640 Ava_2685
            SSO: SSO1159
            STO: ST2570
            SAI: Saci_0302
STRUCTURES  PDB: 1Y37  
DBLINKS     IUBMB Enzyme Nomenclature: 3.8.1.3
            ExPASy - ENZYME nomenclature database: 3.8.1.3
            ExplorEnz - The Enzyme Database: 3.8.1.3
            ERGO genome analysis and discovery system: 3.8.1.3
            UM-BBD (Biocatalysis/Biodegradation Database): 3.8.1.3
            BRENDA, the Enzyme Database: 3.8.1.3
            CAS: 37289-40-0
///
ENTRY       EC 3.8.1.4        Obsolete  Enzyme
NAME        Transferred to 1.97.1.10
CLASS       Hydrolases;
            Acting on halide bonds;
            In carbon-halide compounds
COMMENT     Transferred entry: now EC 1.97.1.10 thyroxine 5'-deiodinase (EC
            3.8.1.4 created 1984, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 3.8.1.4
            ExPASy - ENZYME nomenclature database: 3.8.1.4
            ExplorEnz - The Enzyme Database: 3.8.1.4
            ERGO genome analysis and discovery system: 3.8.1.4
            BRENDA, the Enzyme Database: 3.8.1.4
///
ENTRY       EC 3.8.1.5                  Enzyme
NAME        haloalkane dehalogenase;
            1-chlorohexane halidohydrolase;
            1-haloalkane dehalogenase
CLASS       Hydrolases;
            Acting on halide bonds;
            In carbon-halide compounds
SYSNAME     1-haloalkane halidohydrolase
REACTION    1-haloalkane + H2O = a primary alcohol + halide [RN:R02337]
ALL_REAC    R02337 > R05284 R05367 R05368 R07669 R07670;
            (other) R05369 R05370
SUBSTRATE   1-haloalkane [CPD:C01872];
            H2O [CPD:C00001]
PRODUCT     primary alcohol [CPD:C00226];
            halide [CPD:C00462]
COMMENT     Acts on a wide range of 1-haloalkanes, haloalcohols, haloalkenes and
            some haloaromatic compounds.
REFERENCE   1  [PMID:4019411]
  AUTHORS   Keuning S, Janssen DB, Witholt B.
  TITLE     Purification and characterization of hydrolytic haloalkane
            dehalogenase from Xanthobacter autotrophicus GJ10.
  JOURNAL   J. Bacteriol. 163 (1985) 635-9.
  ORGANISM  Xanthobacter autotrophicus
REFERENCE   2  [PMID:3667524]
  AUTHORS   Scholtz R, Leisinger T, Suter F, Cook AM.
  TITLE     Characterization of 1-chlorohexane halidohydrolase, a dehalogenase
            of wide substrate range from an Arthrobacter sp.
  JOURNAL   J. Bacteriol. 169 (1987) 5016-21.
  ORGANISM  Arthrobacter sp.
REFERENCE   3  [PMID:3624201]
  AUTHORS   Yokota T, Omori T, Kodama T.
  TITLE     Purification and properties of haloalkane dehalogenase from
            Corynebacterium sp. strain m15-3.
  JOURNAL   J. Bacteriol. 169 (1987) 4049-54.
  ORGANISM  Corynebacterium sp.
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
            PATH: map00626  Naphthalene and anthracene degradation
            PATH: map00631  1,2-Dichloroethane degradation
            PATH: map00641  3-Chloroacrylic acid degradation
ORTHOLOGY   KO: K01563  haloalkane dehalogenase
GENES       PIC: PICST_39941
            XFA: XF1965
            XFT: PD0836(dhaA)
            XCC: XCC0216(dhaA)
            XCB: XC_0226
            XCV: XCV0241
            XAC: XAC0235(dhaA)
            XOO: XOO4213(dhaA)
            XOM: XOO_3982(XOO3982)
            PPR: PBPRA1463
            SON: SO_1743
            SDN: Sden_1370
            SFR: Sfri_1366
            SHN: Shewana3_2714
            CPS: CPS_2154
            PAT: Patl_1915
            CBU: CBU_1225
            CBD: COXBU7E912_1310
            HCH: HCH_05560
            ABO: ABO_2415(dhmA)
            BUR: Bcep18194_A4031 Bcep18194_A5407 Bcep18194_A6488
                 Bcep18194_B1849
            AZO: azo3045
            AFW: Anae109_0008
            MLO: mlr5354
            ATU: Atu6064(dha)
            ATC: AGR_pTi_130
            RET: RHE_PE00174
            RLE: RL4047 pRL110069 pRL110536
            BJA: blr1087
            BRA: BRADO6133
            BBT: BBta_1660 BBta_3409
            CCR: CC_1175
            HNE: HNE_0985(dhlA)
            ELI: ELI_03475
            MTU: Rv1833c Rv2296 Rv2579(dhaA)
            MTC: MT2353 MT2656(linB)
            MBO: Mb1864c Mb2318 Mb2610(dhaA)
            MBB: BCG_1868c BCG_2312 BCG_2602(dhaA)
            MPA: MAP0345c MAP2057
            MAV: MAV_0357 MAV_2130
            MSM: MSMEG_6314 MSMEG_6837
            MGI: Mflv_4004
            NFA: nfa26230
            RHA: RHA1_ro01411 RHA1_ro02879 RHA1_ro05164
            SMA: SAV4779
            SEN: SACE_1904 SACE_3906 SACE_5821
            RBA: RB10245(dhlA)
            SYF: Synpcc7942_0901
            AVA: Ava_0656 Ava_1799 Ava_2037 Ava_3113 Ava_5038 Ava_C0108
            SRU: SRU_0874
STRUCTURES  PDB: 1B6G  1BE0  1BEE  1BEZ  1BN6  1BN7  1CIJ  1CQW  1CV2  1D07  
                 1EDB  1EDD  1EDE  1HDE  1K5P  1K63  1K6E  1MJ5  2DHC  2DHD  
                 2DHE  2EDA  2EDC  2PKY  2YXP  
DBLINKS     IUBMB Enzyme Nomenclature: 3.8.1.5
            ExPASy - ENZYME nomenclature database: 3.8.1.5
            ExplorEnz - The Enzyme Database: 3.8.1.5
            ERGO genome analysis and discovery system: 3.8.1.5
            UM-BBD (Biocatalysis/Biodegradation Database): 3.8.1.5
            BRENDA, the Enzyme Database: 3.8.1.5
            CAS: 95990-29-7
///
ENTRY       EC 3.8.1.6                  Enzyme
NAME        4-chlorobenzoate dehalogenase;
            halobenzoate dehalogenase
CLASS       Hydrolases;
            Acting on halide bonds;
            In carbon-halide compounds
SYSNAME     4-chlorobenzoate chlorohydrolase
REACTION    4-chlorobenzoate + H2O = 4-hydroxybenzoate + chloride [RN:R01307]
ALL_REAC    R01307
SUBSTRATE   4-chlorobenzoate [CPD:C02370];
            H2O [CPD:C00001]
PRODUCT     4-hydroxybenzoate [CPD:C00156];
            chloride [CPD:C00115]
COMMENT     Catalyses the first step in the degradation of chlorobenzoate in
            Pseudomonas. In many microorganisms, this activity comprises three
            separate enzymes, EC 6.2.1.33 (4-chlorobenzoate---CoA ligase), EC
            3.8.1.7 (4-chlorobenzoyl-CoA dehalogenase) and EC 3.1.2.23
            (4-hydroxybenzoyl-CoA thioesterase).
REFERENCE   1  [PMID:6497878]
  AUTHORS   Muller R, Thiele J, Klages U, Lingens F.
  TITLE     Incorporation of [18O]water into 4-hydroxybenzoic acid in the
            reaction of 4-chlorobenzoate dehalogenase from pseudomonas spec. CBS
            3.
  JOURNAL   Biochem. Biophys. Res. Commun. 124 (1984) 178-82.
  ORGANISM  Pseudomonas sp.
REFERENCE   2
  AUTHORS   Heppel, L.A. and Porterfield, V.T.
  TITLE     Enzymatic dehalogenation of certain brominated and chlorinated
            compounds.
  JOURNAL   J. Biol. Chem. 176 (1948) 763-769.
ORTHOLOGY   KO: K06032  
GENES       GKA: GK1990
STRUCTURES  PDB: 1BVQ  1JXZ  1NZY  
DBLINKS     IUBMB Enzyme Nomenclature: 3.8.1.6
            ExPASy - ENZYME nomenclature database: 3.8.1.6
            ExplorEnz - The Enzyme Database: 3.8.1.6
            ERGO genome analysis and discovery system: 3.8.1.6
            BRENDA, the Enzyme Database: 3.8.1.6
            CAS: 94047-11-7
///
ENTRY       EC 3.8.1.7                  Enzyme
NAME        4-chlorobenzoyl-CoA dehalogenase
CLASS       Hydrolases;
            Acting on halide bonds;
            In carbon-halide compounds
SYSNAME     4-chlorobenzoyl CoA chlorohydrolase
REACTION    4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride
            [RN:R04101]
ALL_REAC    R04101
SUBSTRATE   4-chlorobenzoyl-CoA [CPD:C06387];
            H2O [CPD:C00001]
PRODUCT     4-hydroxybenzoyl CoA;
            chloride [CPD:C00115]
COMMENT     Specific for dehalogenation at the 4-position. Can dehalogenate
            substrates bearing fluorine, chlorine, bromine and iodine in the
            4-position. This enzyme is part of the bacterial
            2,4-dichlorobenzoate degradation pathway.
REFERENCE   1  [PMID:1610806]
  AUTHORS   Chang KH, Liang PH, Beck W, Scholten JD, Dunaway-Mariano D.
  TITLE     Isolation and characterization of the three polypeptide components
            of 4-chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS-3.
  JOURNAL   Biochemistry. 31 (1992) 5605-10.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:7918379]
  AUTHORS   Crooks GP, Copley SD.
  TITLE     Purification and characterization of 4-chlorobenzoyl CoA
            dehalogenase from Arthrobacter sp. strain 4-CB1.
  JOURNAL   Biochemistry. 33 (1994) 11645-9.
  ORGANISM  Arthrobacter sp.
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
DBLINKS     IUBMB Enzyme Nomenclature: 3.8.1.7
            ExPASy - ENZYME nomenclature database: 3.8.1.7
            ExplorEnz - The Enzyme Database: 3.8.1.7
            ERGO genome analysis and discovery system: 3.8.1.7
            UM-BBD (Biocatalysis/Biodegradation Database): 3.8.1.7
            BRENDA, the Enzyme Database: 3.8.1.7
            CAS: 141583-18-8
///
ENTRY       EC 3.8.1.8                  Enzyme
NAME        atrazine chlorohydrolase;
            AtzA
CLASS       Hydrolases;
            Acting on halide bonds;
            In carbon-halide compounds
SYSNAME     atrazine chlorohydrolase
REACTION    atrazine + H2O =
            4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
            [RN:R05558]
ALL_REAC    R05558
SUBSTRATE   atrazine [CPD:C06551];
            H2O [CPD:C00001]
PRODUCT     4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine
            [CPD:C06552];
            HCl [CPD:C01327]
COMMENT     Involved in the degradation of the herbicide atrazine,
            2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, in
            bacteria.
REFERENCE   1  [PMID:7574646]
  AUTHORS   de Souza ML, Wackett LP, Boundy-Mills KL, Mandelbaum RT, Sadowsky
            MJ.
  TITLE     Cloning, characterization, and expression of a gene region from
            Pseudomonas sp. strain ADP involved in the dechlorination of
            atrazine.
  JOURNAL   Appl. Environ. Microbiol. 61 (1995) 3373-8.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:8759853]
  AUTHORS   de Souza ML, Sadowsky MJ, Wackett LP.
  TITLE     Atrazine chlorohydrolase from Pseudomonas sp. strain ADP: gene
            sequence, enzyme purification, and protein characterization.
  JOURNAL   J. Bacteriol. 178 (1996) 4894-900.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00791  Atrazine degradation
ORTHOLOGY   KO: K05394  atrazine chlorohydrolase
GENES       CVI: CV_1032
            BUR: Bcep18194_A5477 Bcep18194_B2475
            EBA: ebA911
            DAR: Daro_1229
            TBD: Tbd_0947
            MFA: Mfla_1577
            DDE: Dde_1812
            BBT: BBta_2101
            RHA: RHA1_ro04512(atzA)
            HWA: HQ2047A(trzA)
DBLINKS     IUBMB Enzyme Nomenclature: 3.8.1.8
            ExPASy - ENZYME nomenclature database: 3.8.1.8
            ExplorEnz - The Enzyme Database: 3.8.1.8
            ERGO genome analysis and discovery system: 3.8.1.8
            UM-BBD (Biocatalysis/Biodegradation Database): 3.8.1.8
            BRENDA, the Enzyme Database: 3.8.1.8
///
ENTRY       EC 3.8.1.9                  Enzyme
NAME        (R)-2-haloacid dehalogenase;
            2-haloalkanoic acid dehalogenase[ambiguous];
            2-haloalkanoid acid halidohydrolase[ambiguous];
            D-2-haloacid dehalogenase;
            D-DEX
CLASS       Hydrolases;
            Acting on halide bonds;
            In carbon-halide compounds
SYSNAME     (R)-2-haloacid halidohydrolase
REACTION    (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide [RN:R07308]
ALL_REAC    R07308
SUBSTRATE   (R)-2-haloacid [CPD:C15564];
            H2O [CPD:C00001]
PRODUCT     (S)-2-hydroxyacid [CPD:C15565];
            halide [CPD:C00462]
COMMENT     Acts on acids of short chain lengths, C2 to C4, with inversion of
            configuration at C-2. [See also EC 3.8.1.2 (S)-2-haloacid
            dehalogenase, EC 3.8.1.10 2-haloacid dehalogenase
            (configuration-inverting) and EC 3.8.1.11 2-haloacid dehalogenase
            (configuration-retaining)]
REFERENCE   1  [PMID:2380688]
  AUTHORS   Smith JM, Harrison K, Colby J.
  TITLE     Purification and characterization of D-2-haloacid dehalogenase from
            Pseudomonas putida strain AJ1/23.
  JOURNAL   J. Gen. Microbiol. 136 (1990) 881-6.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2
  AUTHORS   Leigh, J.A., Skinner, A.J. and Cooper, R.A.
  TITLE     Partial purification, stereospecificity and stoichiometry of three
            dehalogenases from a Rhizobium species.
  JOURNAL   FEMS Microbiol. Lett. 49 (1988) 353-356.
  ORGANISM  Rhizobium sp.
REFERENCE   3
  AUTHORS   Soda, K., Kurihara, T., Liu, J.-Q., Nardi-Dei, V., Park, C., Miyagi,
            M., Tsunasawa, S. and Esaki, N.
  TITLE     Bacterial 2-haloacid dehalogenases: Structures and catalytic
            properties.
  JOURNAL   Pure Appl. Chem. 68 (1996) 2097-2103.
  ORGANISM  Pseudomonas putida [GN:ppu], Rhizobium sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.8.1.9
            ExPASy - ENZYME nomenclature database: 3.8.1.9
            ExplorEnz - The Enzyme Database: 3.8.1.9
            ERGO genome analysis and discovery system: 3.8.1.9
            BRENDA, the Enzyme Database: 3.8.1.9
            CAS: 119345-29-8
///
ENTRY       EC 3.8.1.10                 Enzyme
NAME        2-haloacid dehalogenase (configuration-inverting);
            2-haloalkanoic acid dehalogenase;
            2-haloalkanoid acid halidohydrolase;
            DL-2-haloacid dehalogenase;
            DL-2-haloacid dehalogenase (inversion of configuration);
            DL-2-haloacid halidohydrolase (inversion of configuration);
            DL-DEXi
CLASS       Hydrolases;
            Acting on halide bonds;
            In carbon-halide compounds
SYSNAME     (R,S)-2-haloacid dehalogenase (configuration-inverting)
REACTION    (1) (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide [RN:R03830];
            (2) (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide [RN:R07308]
ALL_REAC    R03830 R07308
SUBSTRATE   (S)-2-haloacid [CPD:C02103];
            H2O [CPD:C00001];
            (R)-2-haloacid [CPD:C15564]
PRODUCT     (R)-2-hydroxyacid [CPD:C02489];
            halide [CPD:C00462];
            (S)-2-hydroxyacid [CPD:C15565]
COMMENT     Dehalogenates both (S)- and (R)-2-haloalkanoic acids to the
            corresponding (R)- and (S)-hydroxyalkanoic acids, respectively, with
            inversion of configuration at C-2. The enzyme from Pseudomonas sp.
            113 acts on 2-haloalkanoic acids whose carbon chain lengths are five
            or less. [See also EC 3.8.1.2 (S)-2-haloacid dehalogenase, EC
            3.8.1.9 (R)-2-haloacid dehalogenase and EC 3.8.1.11 2-haloacid
            dehalogenase (configuration-retaining)]
REFERENCE   1  [PMID:7103659]
  AUTHORS   Motosugi K, Esaki N, Soda K.
  TITLE     Bacterial assimilation of D- and L-2-chloropropionates and
            occurrence of a new dehalogenase.
  JOURNAL   Arch. Microbiol. 131 (1982) 179-83.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:7068529]
  AUTHORS   Motosugi K, Esaki N, Soda K.
  TITLE     Purification and properties of a new enzyme, DL-2-haloacid
            dehalogenase, from Pseudomonas sp.
  JOURNAL   J. Bacteriol. 150 (1982) 522-7.
  ORGANISM  Pseudomonas sp.
REFERENCE   3
  AUTHORS   Motosugi, K., Esahi, N. and Soda, K.
  TITLE     Enzymatic preparation of D- and L-lactic acid from racemic
            2-chloropropionic acid.
  JOURNAL   Biotechnol. Bioeng. 26 (1984) 805-806.
  ORGANISM  Pseudomonas sp., Pseudomonas putida [GN:ppu]
REFERENCE   4
  AUTHORS   Kurihara, T., Esaki, N. and Soda, K.
  TITLE     Bacterial 2-haloacid dehalogenases: structures and reaction
            mechanisms.
  JOURNAL   J. Mol. Catal., B Enzym. 10 (2000) 57-65.
  ORGANISM  Pseudomonas sp.
REFERENCE   5  [PMID:8074519]
  AUTHORS   Liu JQ, Kurihara T, Hasan AK, Nardi-Dei V, Koshikawa H, Esaki N,
            Soda K.
  TITLE     Purification and characterization of thermostable and
            nonthermostable 2-haloacid dehalogenases with different
            stereospecificities from Pseudomonas sp. strain YL.
  JOURNAL   Appl. Environ. Microbiol. 60 (1994) 2389-93.
  ORGANISM  Pseudomonas sp.
REFERENCE   6  [PMID:8654424]
  AUTHORS   Cairns SS, Cornish A, Cooper RA.
  TITLE     Cloning, sequencing and expression in Escherichia coli of two
            Rhizobium sp. genes encoding haloalkanoate dehalogenases of opposite
            stereospecificity.
  JOURNAL   Eur. J. Biochem. 235 (1996) 744-9.
  ORGANISM  Rhizobium sp.
REFERENCE   7
  AUTHORS   Leigh, J.A., Skinner, A.J. and Cooper, R.A.
  TITLE     Partial purification, stereospecificity and stoichiometry of three
            dehalogenases from a Rhizobium species.
  JOURNAL   FEMS Microbiol. Lett. 49 (1988) 353-356.
  ORGANISM  Rhizobium sp.
REFERENCE   8  [PMID:7142958]
  AUTHORS   Weightman AJ, Weightman AL, Slater JH.
  TITLE     Stereospecificity of 2-monochloropropionate dehalogenation by the
            two dehalogenases of Pseudomonas putida PP3: evidence for two
            different dehalogenation mechanisms.
  JOURNAL   J. Gen. Microbiol. 128 (1982) 1755-62.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   9
  AUTHORS   Soda, K., Kurihara, T., Liu, J.-Q., Nardi-Dei, V., Park, C., Miyagi,
            M., Tsunasawa, S. and Esaki, N.
  TITLE     Bacterial 2-haloacid dehalogenases: Structures and catalytic
            properties.
  JOURNAL   Pure Appl. Chem. 68 (1996) 2097-2103.
  ORGANISM  Pseudomonas putida [GN:ppu], Rhizobium sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.8.1.10
            ExPASy - ENZYME nomenclature database: 3.8.1.10
            ExplorEnz - The Enzyme Database: 3.8.1.10
            ERGO genome analysis and discovery system: 3.8.1.10
            BRENDA, the Enzyme Database: 3.8.1.10
///
ENTRY       EC 3.8.1.11                 Enzyme
NAME        2-haloacid dehalogenase (configuration-retaining);
            2-haloalkanoic acid dehalogenase;
            2-haloalkanoid acid halidohydrolase;
            DL-2-haloacid dehalogenase;
            DL-DEXr
CLASS       Hydrolases;
            Acting on halide bonds;
            In carbon-halide compounds
REACTION    (1) (S)-2-haloacid + H2O = (S)-2-hydroxyacid + halide [RN:R07309];
            (2) (R)-2-haloacid + H2O = (R)-2-hydroxyacid + halide [RN:R07310]
ALL_REAC    R07309 R07310
SUBSTRATE   (S)-2-haloacid [CPD:C02103];
            H2O [CPD:C00001];
            (R)-2-haloacid [CPD:C15564]
PRODUCT     (S)-2-hydroxyacid [CPD:C15565];
            halide [CPD:C00462];
            (R)-2-hydroxyacid [CPD:C02489]
COMMENT     Dehalogenates both (S)- and (R)-2-haloalkanoic acids to the
            corresponding (S)- and (R)-hydroxyalkanoic acids, respectively, with
            retention of configuration at C-2. [See also EC 3.8.1.2
            (S)-2-haloacid dehalogenase, EC 3.8.1.9 (R)-2-haloacid dehalogenase
            and EC 3.8.1.10 2-haloacid dehalogenase (configuration-inverting)]
REFERENCE   1  [PMID:7142958]
  AUTHORS   Weightman AJ, Weightman AL, Slater JH.
  TITLE     Stereospecificity of 2-monochloropropionate dehalogenation by the
            two dehalogenases of Pseudomonas putida PP3: evidence for two
            different dehalogenation mechanisms.
  JOURNAL   J. Gen. Microbiol. 128 (1982) 1755-62.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2
  AUTHORS   Soda, K., Kurihara, T., Liu, J.-Q., Nardi-Dei, V., Park, C., Miyagi,
            M., Tsunasawa, S. and Esaki, N.
  TITLE     Bacterial 2-haloacid dehalogenases: Structures and catalytic
            properties.
  JOURNAL   Pure Appl. Chem. 68 (1996) 2097-2103.
  ORGANISM  Pseudotnonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 3.8.1.11
            ExPASy - ENZYME nomenclature database: 3.8.1.11
            ExplorEnz - The Enzyme Database: 3.8.1.11
            ERGO genome analysis and discovery system: 3.8.1.11
            BRENDA, the Enzyme Database: 3.8.1.11
///
ENTRY       EC 3.8.1.-                  Enzyme
CLASS       Hydrolases;
            Acting on halide bonds;
            In C-halide compounds
REACTION    (1) trans-3-Chloroacrylic acid + H2O <=> HCl + 3-Oxopropanoate
            [RN:R05371];
            (2) cis-3-Chloroacrylic acid + H2O <=> HCl + 3-Oxopropanoate
            [RN:R05372];
            (3) Deisopropylatrazine + H2O <=> Deisopropylhydroxyatrazine + HCl
            [RN:R05572]
SUBSTRATE   trans-3-Chloroacrylic acid [CPD:C06614];
            H2O [CPD:C00001];
            cis-3-Chloroacrylic acid [CPD:C06615];
            Deisopropylatrazine [CPD:C06556]
PRODUCT     HCl [CPD:C01327];
            3-Oxopropanoate [CPD:C00222];
            Deisopropylhydroxyatrazine [CPD:C06557]
///
ENTRY       EC 3.8.2.1        Obsolete  Enzyme
NAME        Transferred to 3.1.8.2
CLASS       Hydrolases;
            Acting on halide bonds;
            In phosphorus-halide compounds (deleted sub-subclass)
COMMENT     Transferred entry: now EC 3.1.8.2 diisopropyl-fluorophosphatase (EC
            3.8.2.1 created 1961, modified 1976, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 3.8.2.1
            ExPASy - ENZYME nomenclature database: 3.8.2.1
            ExplorEnz - The Enzyme Database: 3.8.2.1
            ERGO genome analysis and discovery system: 3.8.2.1
            BRENDA, the Enzyme Database: 3.8.2.1
///
ENTRY       EC 3.9.1.1                  Enzyme
NAME        phosphoamidase;
            creatine phosphatase
CLASS       Hydrolases;
            Acting on phosphorus-nitrogen bonds;
            Acting on phosphorus-nitrogen bonds (only sub-subclass identified to
            date)
SYSNAME     phosphamide hydrolase
REACTION    N-phosphocreatine + H2O = creatine + phosphate [RN:R01882]
ALL_REAC    R01882
SUBSTRATE   N-phosphocreatine [CPD:C02305];
            H2O [CPD:C00001]
PRODUCT     creatine [CPD:C00300];
            phosphate [CPD:C00009]
COMMENT     Also acts on N-phospho-arginine and other phosphoamides. Possibly
            identical with EC 3.1.3.9 (glucose-6-phosphatase) or EC 3.1.3.16
            (phosphoprotein phosphatase).
REFERENCE   1  [PMID:4308726]
  AUTHORS   Parvin R, Smith RA.
  TITLE     Phosphoramidates. V. Probable identity of rat liver microsomal
            glucose 6-phosphatase, phosphoramidase, and phosphoramidate-hexose
            phosphotransferase.
  JOURNAL   Biochemistry. 8 (1969) 1748-55.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Singer, M.F. and Fruton, J.S.
  TITLE     Some properties of beef spleen phosphoamidase.
  JOURNAL   J. Biol. Chem. 229 (1957) 111-119.
  ORGANISM  cow [GN:bta]
REFERENCE   3
  AUTHORS   Sundarajan, T.A. and Sarma, P.S.
  TITLE     Substrate specificity of phosphoprotein phosphatase from spleen.
  JOURNAL   Biochem. J. 71 (1959) 537-544.
DBLINKS     IUBMB Enzyme Nomenclature: 3.9.1.1
            ExPASy - ENZYME nomenclature database: 3.9.1.1
            ExplorEnz - The Enzyme Database: 3.9.1.1
            ERGO genome analysis and discovery system: 3.9.1.1
            BRENDA, the Enzyme Database: 3.9.1.1
            CAS: 9001-79-0
///
ENTRY       EC 3.10.1.1                 Enzyme
NAME        N-sulfoglucosamine sulfohydrolase;
            sulfoglucosamine sulfamidase;
            heparin sulfamidase;
            2-desoxy-D-glucoside-2-sulphamate sulphohydrolase (sulphamate
            sulphohydrolase)
CLASS       Hydrolases;
            Acting on sulfur-nitrogen bonds;
            Acting on sulfur-nitrogen bonds (only sub-subclass identified to
            date)
SYSNAME     N-sulfo-D-glucosamine sulfohydrolase
REACTION    N-sulfo-D-glucosamine + H2O = D-glucosamine + sulfate [RN:R01963]
ALL_REAC    R01963;
            (other) R07814(G)
SUBSTRATE   N-sulfo-D-glucosamine [CPD:C01075];
            H2O [CPD:C00001]
PRODUCT     D-glucosamine [CPD:C00329];
            sulfate [CPD:C00059]
REFERENCE   1  [PMID:5775690]
  AUTHORS   Dietrich CP.
  TITLE     Enzymic degradation of heparin. A sulphamidase and a sulphoesterase
            from Flavobacterium heparinum.
  JOURNAL   Biochem. J. 111 (1969) 91-5.
  ORGANISM  Flavobacterium heparinum
REFERENCE   2  [PMID:6849981]
  AUTHORS   Mahuran D, Clements P, Hopwood J.
  TITLE     A rapid four column purification of 2-deoxy-D-glucoside-2-sulphamate
            sulphohydrolase from human liver.
  JOURNAL   Biochim. Biophys. Acta. 757 (1983) 359-65.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00531  Glycosaminoglycan degradation
            PATH: map01032  Glycan structures - degradation
ORTHOLOGY   KO: K01565  N-sulfoglucosamine sulfohydrolase
GENES       CFA: 403707(SGSH)
DBLINKS     IUBMB Enzyme Nomenclature: 3.10.1.1
            ExPASy - ENZYME nomenclature database: 3.10.1.1
            ExplorEnz - The Enzyme Database: 3.10.1.1
            ERGO genome analysis and discovery system: 3.10.1.1
            BRENDA, the Enzyme Database: 3.10.1.1
            CAS: 37289-41-1
///
ENTRY       EC 3.10.1.2                 Enzyme
NAME        cyclamate sulfohydrolase;
            cyclamate sulfamatase;
            cyclamate sulfamidase;
            cyclohexylsulfamate sulfamidase
CLASS       Hydrolases;
            Acting on sulfur-nitrogen bonds;
            Acting on sulfur-nitrogen bonds (only sub-subclass identified to
            date)
SYSNAME     cyclohexylsulfamate sulfohydrolase
REACTION    cyclohexylsulfamate + H2O = cyclohexylamine + sulfate [RN:R02564]
ALL_REAC    R02564
SUBSTRATE   cyclohexylsulfamate [CPD:C02824];
            H2O [CPD:C00001]
PRODUCT     cyclohexylamine [CPD:C00571];
            sulfate [CPD:C00059]
COMMENT     Also readily hydrolyses aliphatic sulfamates with 3 to 8 carbons.
REFERENCE   1  [PMID:4209783]
  AUTHORS   Nimura T, Tokieda T, Yamaha T.
  TITLE     Partial purification and some properties of cyclamate sulfamatase.
  JOURNAL   J. Biochem. (Tokyo). 75 (1974) 407-17.
  ORGANISM  Pseudotnonas sp.
PATHWAY     PATH: map00930  Caprolactam degradation
DBLINKS     IUBMB Enzyme Nomenclature: 3.10.1.2
            ExPASy - ENZYME nomenclature database: 3.10.1.2
            ExplorEnz - The Enzyme Database: 3.10.1.2
            ERGO genome analysis and discovery system: 3.10.1.2
            UM-BBD (Biocatalysis/Biodegradation Database): 3.10.1.2
            BRENDA, the Enzyme Database: 3.10.1.2
            CAS: 52228-00-9
///
ENTRY       EC 3.11.1.1                 Enzyme
NAME        phosphonoacetaldehyde hydrolase;
            phosphonatase;
            2-phosphonoacetylaldehyde phosphonohydrolase
CLASS       Hydrolases;
            Acting on carbon-phosphorus bonds;
            Acting on carbon-phosphorus bonds (only sub-subclass identified to
            date)
SYSNAME     2-oxoethylphosphonate phosphonohydrolase
REACTION    phosphonoacetaldehyde + H2O = acetaldehyde + phosphate [RN:R00747]
ALL_REAC    R00747
SUBSTRATE   phosphonoacetaldehyde [CPD:C03167];
            H2O [CPD:C00001]
PRODUCT     acetaldehyde [CPD:C00084];
            phosphate [CPD:C00009]
COMMENT     This enzyme destabilizes the C-P bond, by forming an imine between
            one of its lysine residues and the carbonyl group of the substrate,
            thus allowing this, normally stable, bond to be broken. The
            mechanism is similar to that used by EC 4.1.2.13,
            fructose-bisphosphate aldolase, to break a C-C bond. Belongs to the
            haloacetate dehalogenase family.
REFERENCE   1  [PMID:4982500]
  AUTHORS   La Nauze JM, Rosenberg H.
  TITLE     The identification of 2-phosphonoacetaldehyde as an intermediate in
            the degradation of 2-aminoethylphosphonate by Bacillus cereus.
  JOURNAL   Biochim. Biophys. Acta. 165 (1968) 438-47.
  ORGANISM  Bacillus cereus
REFERENCE   2  [PMID:4989158]
  AUTHORS   La Nauze JM, Rosenberg H, Shaw DC.
  TITLE     The enzymic cleavage of the carbon-phosphorus bond: purification and
            properties of phosphonatase.
  JOURNAL   Biochim. Biophys. Acta. 212 (1970) 332-50.
REFERENCE   3  [PMID:200222]
  AUTHORS   La Nauze JM, Coggins JR, Dixon HB.
  TITLE     Aldolase-like imine formation in the mechanism of action of
            phosphonoacetaldehyde hydrolase.
  JOURNAL   Biochem. J. 165 (1977) 409-11.
REFERENCE   4  [PMID:3132206]
  AUTHORS   Olsen DB, Hepburn TW, Moos M, Mariano PS, Dunaway-Mariano D.
  TITLE     Investigation of the Bacillus cereus phosphonoacetaldehyde
            hydrolase. Evidence for a Schiff base mechanism and sequence
            analysis of an active-site peptide containing the catalytic lysine
            residue.
  JOURNAL   Biochemistry. 27 (1988) 2229-34.
REFERENCE   5  [PMID:9649311]
  AUTHORS   Baker AS, Ciocci MJ, Metcalf WW, Kim J, Babbitt PC, Wanner BL,
            Martin BM, Dunaway-Mariano D.
  TITLE     Insights into the mechanism of catalysis by the P-C bond-cleaving
            enzyme phosphonoacetaldehyde hydrolase derived from gene sequence
            analysis and mutagenesis.
  JOURNAL   Biochemistry. 37 (1998) 9305-15.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00440  Aminophosphonate metabolism
ORTHOLOGY   KO: K05306  phosphonoacetaldehyde hydrolase
GENES       STY: STY0471(phnX)
            STT: t2431(phnX)
            SPT: SPA2291(phnX)
            VCH: VCA0606
            VVU: VV2_1662
            VVY: VVA0474
            VPA: VPA0233
            PAE: PA1311(phnX)
            PAU: PA14_47280(phnX)
            PAP: PSPA7_4080(phnX)
            PPU: PP_2208(phnX)
            PFL: PFL_3966(phnX)
            PEN: PSEEN3554(phnX)
            PIN: Ping_2749
            HCH: HCH_03084(phnX)
            AHA: AHA_1940(phnX)
            BXE: Bxe_A2117
            BPE: BP2275
            BPA: BPP2453
            BBR: BB1901
            SFU: Sfum_1731 Sfum_2896
            BAN: BA1340(phnX)
            BAR: GBAA1340(phnX)
            BAA: BA_1865
            BAT: BAS1239
            BCE: BC1326
            BCA: BCE_1439(phnX)
            BCZ: BCZK1217(phnX)
            BTK: BT9727_1215(phnX)
            LPL: lp_0711(phnX)
            LSA: LSA1665(phnX)
            BFR: BF3696
            BFS: BF3488
STRUCTURES  PDB: 1SWV  1SWW  
DBLINKS     IUBMB Enzyme Nomenclature: 3.11.1.1
            ExPASy - ENZYME nomenclature database: 3.11.1.1
            ExplorEnz - The Enzyme Database: 3.11.1.1
            ERGO genome analysis and discovery system: 3.11.1.1
            BRENDA, the Enzyme Database: 3.11.1.1
            CAS: 37289-42-2
///
ENTRY       EC 3.11.1.2                 Enzyme
NAME        phosphonoacetate hydrolase
CLASS       Hydrolases;
            Acting on carbon-phosphorus bonds;
            Acting on carbon-phosphorus bonds (only sub-subclass identified to
            date)
SYSNAME     phosphonoacetate phosphonohydrolase
REACTION    phosphonoacetate + H2O = acetate + phosphate [RN:R00318]
ALL_REAC    R00318
SUBSTRATE   phosphonoacetate [CPD:C05682];
            H2O [CPD:C00001]
PRODUCT     acetate [CPD:C00033];
            phosphate [CPD:C00009]
COFACTOR    Zinc [CPD:C00038]
COMMENT     A zinc-dependent enzyme. Belongs to the alkaline phosphatase
            superfamily of zinc-dependent hydrolases.
REFERENCE   1  [PMID:8529644]
  AUTHORS   McGrath JW, Wisdom GB, McMullan G, Larkin MJ, Quinn JP.
  TITLE     The purification and properties of phosphonoacetate hydrolase, a
            novel carbon-phosphorus bond-cleavage enzyme from Pseudomonas
            fluorescens 23F.
  JOURNAL   Eur. J. Biochem. 234 (1995) 225-30.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00440  Aminophosphonate metabolism
GENES       FTU: FTT0544(phnA)
            FTF: FTF0544(phnA)
            FTH: FTH_0976(phnA)
            REH: H16_B0836(phnA)
            AZO: azo1313(phnA)
            HPA: HPAG1_0855
            SGO: SGO_1100(phnA)
            GFO: GFO_0061(phnA)
STRUCTURES  PDB: 1EI6  
DBLINKS     IUBMB Enzyme Nomenclature: 3.11.1.2
            ExPASy - ENZYME nomenclature database: 3.11.1.2
            ExplorEnz - The Enzyme Database: 3.11.1.2
            ERGO genome analysis and discovery system: 3.11.1.2
            BRENDA, the Enzyme Database: 3.11.1.2
            CAS: 153570-68-4
///
ENTRY       EC 3.11.1.3                 Enzyme
NAME        phosphonopyruvate hydrolase;
            PPH
CLASS       Hydrolases;
            Acting on carbon-phosphorus bonds;
            Acting on carbon-phosphorus bonds (only sub-subclass identified to
            date)
REACTION    3-phosphonopyruvate + H2O = pyruvate + phosphate
SUBSTRATE   3-phosphonopyruvate [CPD:C02798];
            H2O [CPD:C00001]
PRODUCT     pyruvate [CPD:C00022];
            phosphate [CPD:C00009]
COMMENT     Highly specific for phosphonopyruvate as substrate [2]. The reaction
            is not inhibited by phosphate but is inhibited by the phosphonates
            phosphonoformic acid, hydroxymethylphosphonic acid and
            3-phosphonopropanoic acid [2]. The enzyme is activated by the
            divalent cations Co2+, Mg2+ and Mn2+. This enzyme is a member of the
            phosphoenolpyruvate mutase/isocitrate lyase superfamily [3].
REFERENCE   1  [PMID:10648102]
  AUTHORS   Ternan NG, Hamilton JT, Quinn JP.
  TITLE     Initial in vitro characterisation of phosphonopyruvate hydrolase, a
            novel phosphate starvation-independent, carbon-phosphorus bond
            cleavage enzyme in Burkholderia cepacia Pal6.
  JOURNAL   Arch. Microbiol. 173 (2000) 35-41.
REFERENCE   2  [PMID:12697754]
  AUTHORS   Kulakova AN, Wisdom GB, Kulakov LA, Quinn JP.
  TITLE     The purification and characterization of phosphonopyruvate
            hydrolase, a novel carbon-phosphorus bond cleavage enzyme from
            Variovorax sp Pal2.
  JOURNAL   J. Biol. Chem. 278 (2003) 23426-31.
REFERENCE   3  [PMID:16981709]
  AUTHORS   Chen CC, Han Y, Niu W, Kulakova AN, Howard A, Quinn JP,
            Dunaway-Mariano D, Herzberg O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily.
  JOURNAL   Biochemistry. 45 (2006) 11491-504.
DBLINKS     IUBMB Enzyme Nomenclature: 3.11.1.3
            ExPASy - ENZYME nomenclature database: 3.11.1.3
            ExplorEnz - The Enzyme Database: 3.11.1.3
            ERGO genome analysis and discovery system: 3.11.1.3
            BRENDA, the Enzyme Database: 3.11.1.3
///
ENTRY       EC 3.12.1.1                 Enzyme
NAME        trithionate hydrolase
CLASS       Hydrolases;
            Acting on sulfur-sulfur bonds;
            Acting on sulfur-sulfur bonds (only sub-subclass identified to date)
SYSNAME     trithionate thiosulfohydrolase
REACTION    trithionate + H2O = thiosulfate + sulfate + 2 H+ [RN:R01930]
ALL_REAC    R01930
SUBSTRATE   trithionate [CPD:C01861];
            H2O [CPD:C00001]
PRODUCT     thiosulfate [CPD:C00320];
            sulfate [CPD:C00059];
            H+ [CPD:C00080]
REFERENCE   1
  AUTHORS   Lu, W.-P. and Kelly, D.P.
  TITLE     Cellular location and partial purification of the
            'thiosulphate-oxidizing enzyme' and 'trithionate hydrolase' from
            Thiobacillus tepidarius.
  JOURNAL   J. Gen. Microbiol. 134 (1988) 877-885.
  ORGANISM  Thiobacillus tepidarius
REFERENCE   2
  AUTHORS   Trudinger, P.A.
  TITLE     The metabolism of trithionate by Thiobacillus X.
  JOURNAL   Aust. J. Biol. Sci. 17 (1964) 459-468.
PATHWAY     PATH: map00920  Sulfur metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 3.12.1.1
            ExPASy - ENZYME nomenclature database: 3.12.1.1
            ExplorEnz - The Enzyme Database: 3.12.1.1
            ERGO genome analysis and discovery system: 3.12.1.1
            BRENDA, the Enzyme Database: 3.12.1.1
            CAS: 115004-90-5
///
ENTRY       EC 3.13.1.1                 Enzyme
NAME        UDP-sulfoquinovose synthase;
            sulfite:UDP-glucose sulfotransferase;
            UDPsulfoquinovose synthase
CLASS       Hydrolases;
            Acting on carbon-sulfur bonds;
            Acting on carbon-sulfur bonds (only sub-subclass identified to date)
SYSNAME     UDP-6-sulfo-6-deoxyglucose sulfohydrolase
REACTION    UDP-glucose + sulfite = UDP-6-sulfoquinovose + H2O [RN:R05775]
ALL_REAC    R05775
SUBSTRATE   UDP-glucose [CPD:C00029];
            sulfite [CPD:C00094]
PRODUCT     UDP-6-sulfoquinovose [CPD:C11521];
            H2O [CPD:C00001]
COMMENT     Requires NAD+, which appears to oxidize the substrate to
            UDP-4-dehydroglucose, which dehydrates to
            UDP-4-dehydro-6-deoxygluc-5-enose, to which sulfite can add; the
            reaction is completed when the substrate is rehydrogenated at C-4.
            The enzyme from Arabidopsis thaliana is specific for UDP-Glc and
            sulfite.
REFERENCE   1  [PMID:9465123]
  AUTHORS   Essigmann B, Guler S, Narang RA, Linke D, Benning C.
  TITLE     Phosphate availability affects the thylakoid lipid composition and
            the expression of SQD1, a gene required for sulfolipid biosynthesis
            in Arabidopsis thaliana.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 1950-5.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   2  [PMID:10462438]
  AUTHORS   Essigmann B, Hespenheide BM, Kuhn LA, Benning C.
  TITLE     Prediction of the active-site structure and NAD(+) binding in SQD1,
            a protein essential for sulfolipid biosynthesis in Arabidopsis.
  JOURNAL   Arch. Biochem. Biophys. 369 (1999) 30-41.
REFERENCE   3  [PMID:10557279]
  AUTHORS   Mulichak AM, Theisen MJ, Essigmann B, Benning C, Garavito RM.
  TITLE     Crystal structure of SQD1, an enzyme involved in the biosynthesis of
            the plant sulfolipid headgroup donor UDP-sulfoquinovose.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 13097-102.
REFERENCE   4  [PMID:11073956]
  AUTHORS   Sanda S, Leustek T, Theisen MJ, Garavito RM, Benning C.
  TITLE     Recombinant Arabidopsis SQD1 converts udp-glucose and sulfite to the
            sulfolipid head group precursor UDP-sulfoquinovose in vitro.
  JOURNAL   J. Biol. Chem. 276 (2001) 3941-6.
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
            PATH: map00561  Glycerolipid metabolism
ORTHOLOGY   KO: K06118  UDP-sulfoquinovose synthase
GENES       ATH: AT4G33030(SQD1)
            OSA: 4338660
            CME: CMR012C
            NOC: Noc_1509
            MMR: Mmar10_2598
            MMC: Mmcs_4564
            MKM: Mkms_4652
            MJL: Mjls_4947
            ACE: Acel_0444
            SEN: SACE_5690
            SYR: SynRCC307_0054 SynRCC307_0204
            CYA: CYA_0577
            CYB: CYB_0060
            AVA: Ava_0293
            PMB: A9601_18741(sqdB)
            PMC: P9515_18551(sqdB)
            PMF: P9303_00511(sqdB)
            PMG: P9301_18551(sqdB)
            PME: NATL1_21351(sqdB)
DBLINKS     IUBMB Enzyme Nomenclature: 3.13.1.1
            ExPASy - ENZYME nomenclature database: 3.13.1.1
            ExplorEnz - The Enzyme Database: 3.13.1.1
            ERGO genome analysis and discovery system: 3.13.1.1
            BRENDA, the Enzyme Database: 3.13.1.1
///
ENTRY       EC 3.13.1.2       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Hydrolases;
            Acting on carbon-sulfur bonds;
            Acting on carbon-sulfur bonds (only sub-subclass identified to date)
COMMENT     Deleted entry: 5-deoxyribos-5-ylhomocysteinase. The activity is most
            probably attributable to EC 4.4.1.21, S-ribosylhomocysteine lyase.
            (EC 3.13.1.2 created 1972 as EC 3.3.1.3, transferred 2001 to EC
            3.2.1.148, transferred 2004 to EC 3.13.1.2, deleted 2005)
DBLINKS     IUBMB Enzyme Nomenclature: 3.13.1.2
            ExPASy - ENZYME nomenclature database: 3.13.1.2
            ExplorEnz - The Enzyme Database: 3.13.1.2
            ERGO genome analysis and discovery system: 3.13.1.2
            BRENDA, the Enzyme Database: 3.13.1.2
///
ENTRY       EC 3.13.1.3                 Enzyme
NAME        2'-hydroxybiphenyl-2-sulfinate desulfinase;
            gene dszB-encoded hydrolase;
            2-(2-hydroxyphenyl) benzenesulfinate:H2O hydrolase;
            DszB;
            HBPSi desulfinase;
            2-(2-hydroxyphenyl) benzenesulfinate sulfohydrolase;
            HPBS desulfinase;
            2-(2-hydroxyphenyl)benzenesulfinate hydrolase;
            2-(2'-hydroxyphenyl)benzenesulfinate desulfinase;
            2-(2-hydroxyphenyl)benzenesulfinate desulfinase
CLASS       Hydrolases;
            Acting on carbon-sulfur bonds;
            Acting on carbon-sulfur bonds (only sub-subclass identified to date)
SYSNAME     2'-hydroxybiphenyl-2-sulfinate sulfohydrolase
REACTION    2'-hydroxybiphenyl-2-sulfinate + H2O = 2-hydroxybiphenyl + sulfite
            [RN:R07311]
ALL_REAC    R07311
SUBSTRATE   2'-hydroxybiphenyl-2-sulfinate [CPD:C06742];
            H2O [CPD:C00001]
PRODUCT     2-hydroxybiphenyl [CPD:C02499];
            sulfite [CPD:C00094]
COMMENT     The enzyme from Rhodococcus sp. strain IGTS8 is encoded by the
            plasmid-encoded dibenzothiophene-desulfurization (dsz) operon. The
            enzyme has a narrow substrate specificity with biphenyl-2-sulfinate
            being the only other substrate known to date [2].
REFERENCE   1  [PMID:9308179]
  AUTHORS   Oldfield C, Pogrebinsky O, Simmonds J, Olson ES, Kulpa CF.
  TITLE     Elucidation of the metabolic pathway for dibenzothiophene
            desulphurization by Rhodococcus sp. strain IGTS8 (ATCC 53968).
  JOURNAL   Microbiology. 143 ( Pt 9) (1997) 2961-73.
REFERENCE   2  [PMID:12147352]
  AUTHORS   Nakayama N, Matsubara T, Ohshiro T, Moroto Y, Kawata Y, Koizumi K,
            Hirakawa Y, Suzuki M, Maruhashi K, Izumi Y, Kurane R.
  TITLE     A novel enzyme, 2'-hydroxybiphenyl-2-sulfinate desulfinase (DszB),
            from a dibenzothiophene-desulfurizing bacterium Rhodococcus
            erythropolis KA2-5-1: gene overexpression and enzyme
            characterization.
  JOURNAL   Biochim. Biophys. Acta. 1598 (2002) 122-30.
  ORGANISM  Rhodococcus erythropolis
REFERENCE   3  [PMID:12801508]
  AUTHORS   Watkins LM, Rodriguez R, Schneider D, Broderick R, Cruz M, Chambers
            R, Ruckman E, Cody M, Mrachko GT.
  TITLE     Purification and characterization of the aromatic desulfinase,
            2-(2'-hydroxyphenyl)benzenesulfinate desulfinase.
  JOURNAL   Arch. Biochem. Biophys. 415 (2003) 14-23.
  ORGANISM  Rhodococcus sp.
ORTHOLOGY   KO: K05977  2'-hydroxybiphenyl-2-sulfinate desulfinase
GENES       PEN: PSEEN3424 PSEEN3429
            ACI: ACIAD1503 ACIAD1512
            MAV: MAV_3808
            RHA: RHA1_ro07049
STRUCTURES  PDB: 2DE2  2DE3  2DE4  
DBLINKS     IUBMB Enzyme Nomenclature: 3.13.1.3
            ExPASy - ENZYME nomenclature database: 3.13.1.3
            ExplorEnz - The Enzyme Database: 3.13.1.3
            ERGO genome analysis and discovery system: 3.13.1.3
            UM-BBD (Biocatalysis/Biodegradation Database): 3.13.1.3
            BRENDA, the Enzyme Database: 3.13.1.3
///
ENTRY       EC 4.1.1.1                  Enzyme
NAME        pyruvate decarboxylase;
            alpha-carboxylase;
            pyruvic decarboxylase;
            alpha-ketoacid carboxylase;
            2-oxo-acid carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     2-oxo-acid carboxy-lyase (aldehyde-forming)
REACTION    a 2-oxo acid = an aldehyde + CO2 [RN:R00636]
ALL_REAC    R00636 > R00224;
            (other) R00014 R00755
SUBSTRATE   2-oxo acid [CPD:C00161]
PRODUCT     aldehyde [CPD:C00071];
            CO2 [CPD:C00011]
COFACTOR    Thiamin diphosphate [CPD:C00068]
COMMENT     A thiamine-diphosphate protein. Also catalyses acyloin formation.
REFERENCE   1  [PMID:12980978]
  AUTHORS   SINGER TP, PENSKY J.
  TITLE     Isolation and properties of the carboxylase of wheat germ.
  JOURNAL   J. Biol. Chem. 196 (1952) 375-88.
  ORGANISM  Triticum aestivum [GN:etae]
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
ORTHOLOGY   KO: K01568  pyruvate decarboxylase
GENES       ATH: AT4G33070 AT5G01320 AT5G01330(PDC3) AT5G54960(PDC2)
            OSA: 4324066 4332519 4339066 4339068
            SCE: YDL080C(THI3) YDR380W(ARO10) YGR087C(PDC6) YLR044C(PDC1)
                 YLR134W(PDC5)
            AGO: AGOS_AAL073W AGOS_ACL134C AGOS_ACR211W AGOS_ADR254W
            PIC: PICST_62095(ARO10) PICST_64926(PDC1) PICST_86443(PDC2)
            CGR: CAGL0A03102g CAGL0L06842g CAGL0M07920g
            SPO: SPAC186.09 SPAC1F8.07c SPAC3G9.11c SPAC3H8.01
            ANI: AN4888.2
            AFM: AFUA_3G11070 AFUA_5G14810 AFUA_6G00750
            AOR: AO090003000661 AO090038000139
            CNE: CNJ00950
            STY: STY2646
            STT: t0452
            SPT: SPA0455
            SEC: SC2408(dciP)
            STM: STM2405
            PEN: PSEEN2115
            PAR: Psyc_0858(pdc)
            PCR: Pcryo_0964
            LPN: lpg1155
            LPF: lpl1162
            LPP: lpp1157
            PCA: Pcar_2858
            RET: RHE_PF00449(ypf00238)
            ZMO: ZMO1360(pdc)
            GOX: GOX1081
            SAU: SA0182
            SAV: SAV0188
            SAM: MW0162
            SAR: SAR0189
            SAS: SAS0163
            SAB: SAB0128c
            SAO: SAOUHSC_00153
            SEP: SE2210
            SHA: SH0376
            SSP: SSP0172
            LLA: L138640(ipd)
            CAC: CA_P0025(pdc)
            MPE: MYPE6890
            MTC: MT0876
            MBO: Mb0876c(pdc)
            MLE: ML2167(pdc)
            MPA: MAP0783c(pdc)
            GVI: gll2057
            MAC: MA0594(ipdC)
            MBA: Mbar_A1429
            RCI: RCIX1497(pdc)
STRUCTURES  PDB: 1PVD  1PYD  1QPB  1VC3  1ZPD  2G1I  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.1
            ExPASy - ENZYME nomenclature database: 4.1.1.1
            ExplorEnz - The Enzyme Database: 4.1.1.1
            ERGO genome analysis and discovery system: 4.1.1.1
            BRENDA, the Enzyme Database: 4.1.1.1
            CAS: 9001-04-1
///
ENTRY       EC 4.1.1.2                  Enzyme
NAME        oxalate decarboxylase;
            oxalate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     oxalate carboxy-lyase (formate-forming)
REACTION    oxalate + H+ = formate + CO2 [RN:R00522]
ALL_REAC    R00522
SUBSTRATE   oxalate [CPD:C00209];
            H+ [CPD:C00080]
PRODUCT     formate [CPD:C00058];
            CO2 [CPD:C00011]
COMMENT     The enzyme from Bacillus subtilis contains manganese and requires O2
            for activity, even though there is no net redox change.
REFERENCE   1  [PMID:13367015]
  AUTHORS   HAYAISHI O, JAKOBY WB, OHMURA E.
  TITLE     Enzymatic decarboxylation of oxalic acid.
  JOURNAL   J. Biol. Chem. 222 (1956) 435-46.
REFERENCE   2  [PMID:10960116]
  AUTHORS   Tanner A, Bornemann S.
  TITLE     Bacillus subtilis YvrK is an acid-induced oxalate decarboxylase.
  JOURNAL   J. Bacteriol. 182 (2000) 5271-3.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   3  [PMID:11546787]
  AUTHORS   Tanner A, Bowater L, Fairhurst SA, Bornemann S.
  TITLE     Oxalate decarboxylase requires manganese and dioxygen for activity.
            Overexpression and characterization of Bacillus subtilis YvrK and
            YoaN.
  JOURNAL   J. Biol. Chem. 276 (2001) 43627-34.
  ORGANISM  Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K01569  oxalate decarboxylase
GENES       OSA: 4333791
            ANI: AN8099.2
            AFM: AFUA_2G14610
            AOR: AO090005000078
            PLU: plu2325
            SPE: Spro_2322
            BMA: BMAA1259
            BMV: BMASAVP1_0231(oxdD)
            BML: BMA10299_0503(oxdD)
            BMN: BMA10247_A1067(oxdD)
            BVI: Bcep1808_5109
            BUR: Bcep18194_B1256
            BCN: Bcen_3780
            BCH: Bcen2424_4588
            BAM: Bamb_4014
            BPS: BPSS0965
            BPM: BURPS1710b_A2575
            BPL: BURPS1106A_A1331(oxdD)
            BPD: BURPS668_A1413(oxdD)
            BTE: BTH_II1426
            ATU: Atu4771
            ATC: AGR_L_224
            BJA: blr0281
            RPB: RPB_0200
            SUS: Acid_0839
            BSU: BG13484(yoaN) BG14148(oxdC)
            BCE: BC1031
            BLI: BL00821(oxdC) BL02520(oxdDA)
            BLD: BLi03275(yoaN1) BLi03580(oxdC)
            BCL: ABC0838
            BAY: RBAM_020670 RBAM_030390
            BPU: BPUM_0805
            SMU: SMU.139
            CBO: CBO0864(oxdD)
            CBA: CLB_0903(oxdD)
            CBH: CLC_0917(oxdD)
            CBF: CLI_0942(oxdD)
            MSM: MSMEG_2254
            SYN: sll1358
            SYC: syc1717_d
            SYF: Synpcc7942_2388
STRUCTURES  PDB: 1UW8  2UY8  2UY9  2UYA  2UYB  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.2
            ExPASy - ENZYME nomenclature database: 4.1.1.2
            ExplorEnz - The Enzyme Database: 4.1.1.2
            ERGO genome analysis and discovery system: 4.1.1.2
            BRENDA, the Enzyme Database: 4.1.1.2
            CAS: 9024-97-9
///
ENTRY       EC 4.1.1.3                  Enzyme
NAME        oxaloacetate decarboxylase;
            oxaloacetate beta-decarboxylase;
            oxalacetic acid decarboxylase;
            oxalate beta-decarboxylase;
            oxaloacetate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     oxaloacetate carboxy-lyase (pyruvate-forming)
REACTION    oxaloacetate = pyruvate + CO2 [RN:R00217]
ALL_REAC    R00217;
            (other) R00214 R00216 R00471
SUBSTRATE   oxaloacetate [CPD:C00036]
PRODUCT     pyruvate [CPD:C00022];
            CO2 [CPD:C00011]
COFACTOR    Manganese [CPD:C00034];
            Biotin [CPD:C00120];
            Sodium [CPD:C01330]
INHIBITOR   Acetyl-CoA [CPD:C00024]
COMMENT     The enzyme from Klebsiella aerogenes is a biotinyl protein and also
            decarboxylates glutaconyl-CoA and methylmalonyl-CoA. The process is
            accompanied by the extrusion of two sodium ions from cells. Some
            animal enzymes require Mn2+.
REFERENCE   1  [PMID:7016536]
  AUTHORS   Dimroth P.
  TITLE     Characterization of a membrane-bound biotin-containing enzyme:
            oxaloacetate decarboxylase from Klebsiella aerogenes.
  JOURNAL   Eur. J. Biochem. 115 (1981) 353-8.
  ORGANISM  Klebsiella aerogenes
REFERENCE   2  [PMID:7037395]
  AUTHORS   Dimroth P.
  TITLE     The role of biotin and sodium in the decarboxylation of oxaloacetate
            by the membrane-bound oxaloacetate decarboxylase from Klebsiella
            aerogenes.
  JOURNAL   Eur. J. Biochem. 121 (1982) 435-41.
  ORGANISM  Klebsiella aerogenes
REFERENCE   3
  AUTHORS   Herbert, D.
  TITLE     Oxalacetic carboxylase of Micrococcus lysodeikticus.
  JOURNAL   Methods Enzymol. 1 (1955) 753-757.
  ORGANISM  Micrococcus lysodeikticus
REFERENCE   4  [PMID:14205502]
  AUTHORS   HORTON AA, KORNBERG HL.
  TITLE     OXALOACETATE 4-CARBOXY-LYASE FROM PSEUDOMONAS OVALIS CHESTER.
  JOURNAL   Biochim. Biophys. Acta. 89 (1964) 381-3.
  ORGANISM  Micrococcus lysodeikticus, Pseudomonas ovalis, Azotobacter
            vinelandii
REFERENCE   5  [PMID:5972993]
  AUTHORS   Schmitt A, Bottke I, Siebert G.
  TITLE     [Properties of oxaloacetate decarboxylase from codfish muscles]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 347 (1966) 18-34.
  ORGANISM  Gadus macrocephalus
PATHWAY     PATH: map00330  Arginine and proline metabolism
            PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K01570  oxaloacetate decarboxylase
            KO: K01571  oxaloacetate decarboxylase, alpha subunit
            KO: K01572  oxaloacetate decarboxylase, beta subunit
            KO: K01573  oxaloacetate decarboxylase, gamma subunit
GENES       STY: STY0063(oadB) STY0064(oadA) STY0065(oadG) STY3531(oadB)
                 STY3532(oadA) STY3533(oadG)
            STT: t0056(oadB) t0057(oadA) t0058(oadG) t3266(oadB) t3267(oadA)
                 t3268(oadG)
            SPT: SPA0055(oadB) SPA0056(oadA) SPA0057(oadG) SPA3218(oadB)
                 SPA3219(oadA) SPA3220(oadG)
            SEC: SC0048(oadB) SC0049(oadA) SC0050(oag3) SC0764(oadG)
                 SC0765(oadA) SC0766(oadB) SC3289(oadB) SC3290(oadA)
                 SC3291(oadG)
            STM: STM0054 STM0055 STM0056 STM0766(dcoC) STM0768(dcoB)
                 STM1884(eda) STM3351(oadB) STM3352(oadA) STM3353(oadG)
            YPI: YpsIP31758_0093(ligK)
            HDU: HD0782(oadB) HD0783(oadA) HD0784(oadG)
            HSO: HS_0201(oadG) HS_0202(oadA) HS_0203(oadB)
            PMU: PM1421 PM1422 PM1423
            MSU: MS0038(oadB) MS0039(oadA) MS0040(oadG)
            APL: APL_1375(oadG) APL_1376(oadA) APL_1377(oadB)
            VCH: VC0549 VC0550 VC0551 VC0792 VC0794
            VCO: VC0395_A0085(oadA-1) VC0395_A0086(oadB-1)
                 VC0395_A0319(oadB-2) VC0395_A0320(oadA-2)
            VVU: VV1_1600 VV1_1601 VV1_1602
            VVY: VV2798 VV2799 VV2800
            VPA: VP2543 VP2544 VP2545
            VFI: VF0539 VF0540
            PPR: PBPRA2298 PBPRA2299 PBPRA3050 PBPRA3051 PBPRA3052
            PAP: PSPA7_6223(oadA)
            PPU: PP_5346(oadA)
            PST: PSPTO_5510(oadA)
            PSB: Psyr_5060
            PSP: PSPPH_5142(oadA)
            PFL: PFL_6157(oadA)
            PFO: Pfl_5639
            PEN: PSEEN5495(oadA)
            PMY: Pmen_2893
            SFR: Sfri_1065 Sfri_1066 Sfri_1067
            SAZ: Sama_1053
            SBL: Sbal_1026
            SBM: Shew185_1092
            SLO: Shew_1221
            SPC: Sputcn32_1031
            SSE: Ssed_1321
            SPL: Spea_1199
            SHE: Shewmr4_2985 Shewmr4_2986 Shewmr4_2987
            SHM: Shewmr7_3067 Shewmr7_3068 Shewmr7_3069
            SHN: Shewana3_3164 Shewana3_3165 Shewana3_3166
            SHW: Sputw3181_3134
            ILO: IL1734(oadB) IL1735(oadA) IL1736(oadG)
            CPS: CPS_1048(oadG) CPS_1049(oadA) CPS_1050(oadB)
            PHA: PSHAa0538(oadG) PSHAa0539(oadA) PSHAa0540(oadB)
            PAT: Patl_3011 Patl_3012
            SDE: Sde_1305 Sde_1306 Sde_1307
            PIN: Ping_3375
            MAQ: Maqu_0972
            LPF: lpl0507(dcoA)
            MCA: MCA2479(oadB) MCA2480(oadA) MCA2481(oadC)
            HCH: HCH_05201 HCH_05202(oadA1) HCH_05203 HCH_06704(oadA2)
            CSA: Csal_0692 Csal_0693 Csal_0694 Csal_1556
            ABO: ABO_0843(oadG) ABO_0844(oadA) ABO_0845(oadB)
            RMA: Rmag_0847
            VOK: COSY_0772(oadB) COSY_0773(oadA)
            TBD: Tbd_1556
            MFA: Mfla_1512
            HHE: HH1686(pycB)
            TDN: Tmden_1258 Tmden_1260
            NIS: NIS_1302 NIS_1303 NIS_1304
            SUN: SUN_1432 SUN_1433 SUN_1434
            DPS: DP0687
            RRU: Rru_A1320
            MGM: Mmc1_3195 Mmc1_3196 Mmc1_3197
            SPY: SPy_1174 SPy_1191(oadA)
            SPZ: M5005_Spy_0894(oadA2) M5005_Spy_0897 M5005_Spy_0902
                 M5005_Spy_0903(oadB) M5005_Spy_0909(oadA1)
            SPM: spyM18_1126 spyM18_1142(oadA)
            SPG: SpyM3_0822 SpyM3_0836(oadA)
            SPS: SPs1023 SPs1036
            SPH: MGAS10270_Spy1008(oadA2) MGAS10270_Spy1010 MGAS10270_Spy1011
                 MGAS10270_Spy1016 MGAS10270_Spy1017(oadB)
                 MGAS10270_Spy1023(oadA1)
            SPI: MGAS10750_Spy1043(oadA2) MGAS10750_Spy1051
                 MGAS10750_Spy1052(oadB) MGAS10750_Spy1053
                 MGAS10750_Spy1059(oadA1)
            SPJ: MGAS2096_Spy0967 MGAS2096_Spy0968(oadA1)
            SPK: MGAS9429_Spy1011(oadA1)
            SPA: M6_Spy0883 M6_Spy0898
            SPB: M28_Spy0867(oadA2) M28_Spy0870 M28_Spy0875 M28_Spy0876(oadB)
                 M28_Spy0882(oadA1)
            SMU: SMU.1017(oadB) SMU.1023(pycB)
            LSA: LSA1222(oadA) LSA1229(oadB) LSA1230(oadG)
            LCA: LSEI_1855 LSEI_1862
            EFA: EF3317
            CHY: CHY_1999(oadA)
            CEF: CE0804
            FNU: FN1376
            TPA: TP0056 TP0057
            BTH: BT_1689 BT_1696
            BFR: BF2936 BF3292
            BFS: BF2819 BF3131(mmdB)
            CTE: CT0834(oadA)
            CCH: Cag_0859
            PVI: Cvib_1017 Cvib_1251
            PLT: Plut_1266 Plut_1267 Plut_1434
            DET: DET0119(oadA)
            DEH: cbdb_A139(oadA)
            AAE: aq_1614(oadA)
            TMA: TM0128 TM0880
            AFU: AF2084(oadB) AF2085
            PHO: PH0834
            TKO: TK0990
STRUCTURES  PDB: 2NX9  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.3
            ExPASy - ENZYME nomenclature database: 4.1.1.3
            ExplorEnz - The Enzyme Database: 4.1.1.3
            ERGO genome analysis and discovery system: 4.1.1.3
            BRENDA, the Enzyme Database: 4.1.1.3
            CAS: 9024-98-0
///
ENTRY       EC 4.1.1.4                  Enzyme
NAME        acetoacetate decarboxylase;
            acetoacetic acid decarboxylase;
            acetoacetate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     acetoacetate carboxy-lyase (acetone-forming)
REACTION    acetoacetate + H+ = acetone + CO2 [RN:R01366]
ALL_REAC    R01366
SUBSTRATE   acetoacetate [CPD:C00164];
            H+ [CPD:C00080]
PRODUCT     acetone [CPD:C00207];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Davies, R.
  TITLE     Studies of the acetone-butanol fermentation. 4. Acetoacetic acid
            decarboxylase of Cl. acetobutylicum (BY).
  JOURNAL   Biochem. J. 37 (1943) 230-238.
  ORGANISM  Clostridium acetobutylicum [GN:cac]
REFERENCE   2  [PMID:5911291]
  AUTHORS   Zerner B, Coutts SM, Lederer F, Waters HH, Westheimer FH.
  TITLE     Acetoacetate decarboxylase. Preparation of the enzyme.
  JOURNAL   Biochemistry. 5 (1966) 813-6.
  ORGANISM  Clostridium acetobutylicum [GN:cac]
PATHWAY     PATH: map00072  Synthesis and degradation of ketone bodies
            PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K01574  acetoacetate decarboxylase
GENES       TET: TTHERM_00035180
            PAP: PSPA7_3628
            LPN: lpg0672
            LPF: lpl0708
            LPP: lpp0728
            FTL: FTL_1279
            FTH: FTH_1252(adc)
            FTA: FTA_1352
            FTN: FTN_0808
            CVI: CV_3520
            RSO: RSp1058(adc)
            BMA: BMAA0018(adc)
            BMV: BMASAVP1_1168(adc)
            BML: BMA10299_1448(adc)
            BMN: BMA10247_A0022(adc)
            BXE: Bxe_A2916
            BVI: Bcep1808_3777 Bcep1808_4583
            BUR: Bcep18194_B1397 Bcep18194_B3166
            BCN: Bcen_5145
            BCH: Bcen2424_5714
            BAM: Bamb_4983
            BPS: BPSS0018(adc)
            BPM: BURPS1710b_A1525
            BPL: BURPS1106A_A0022
            BPD: BURPS668_A0024
            BTE: BTH_II0020
            MLO: mll5917 mlr2399 mlr3634
            RLE: pRL90174(adc)
            BJA: bll7763 blr7028
            BBT: BBta_1411(adc)
            XAU: Xaut_2132
            ACR: Acry_0495
            BAY: RBAM_030030
            LSL: LSL_0135
            LCA: LSEI_0716
            CAC: CA_P0165(adc)
            CBE: Cbei_3835
            MAV: MAV_3542
            RHA: RHA1_ro08625
            SMA: SAV1349(adc)
            SEN: SACE_5407(adc)
            RXY: Rxyl_1034
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.4
            ExPASy - ENZYME nomenclature database: 4.1.1.4
            ExplorEnz - The Enzyme Database: 4.1.1.4
            ERGO genome analysis and discovery system: 4.1.1.4
            BRENDA, the Enzyme Database: 4.1.1.4
            CAS: 9025-03-0
///
ENTRY       EC 4.1.1.5                  Enzyme
NAME        acetolactate decarboxylase;
            alpha-acetolactate decarboxylase;
            (S)-2-hydroxy-2-methyl-3-oxobutanoate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     (S)-2-hydroxy-2-methyl-3-oxobutanoate carboxy-lyase
            [(R)-2-acetoin-forming]
REACTION    (S)-2-hydroxy-2-methyl-3-oxobutanoate = (R)-2-acetoin + CO2
            [RN:R02948]
ALL_REAC    R02948;
            (other) R02947
SUBSTRATE   (S)-2-hydroxy-2-methyl-3-oxobutanoate [CPD:C06010]
PRODUCT     (R)-2-acetoin [CPD:C00810];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Hill, R.K., Sawada, S. and Arfin, S.M.
  TITLE     Stereochemistry of valine and isoleucine biosynthesis. IV.
            Synthesis, configuration, and enzymatic specificity of
            alpha-acetolactate and alpha-aceto-alpha-hydroxybutyrate.
  JOURNAL   Bioorg. Chem. 8 (1979) 175-189.
  ORGANISM  Aerobacter aerogenes
REFERENCE   2  [PMID:6024768]
  AUTHORS   Stormer FC.
  TITLE     Isolation of crystalline pH 6 acetolactate-forming enzyme from
            Aerobacter aerogenes.
  JOURNAL   J. Biol. Chem. 242 (1967) 1756-9.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00650  Butanoate metabolism
            PATH: map00660  C5-Branched dibasic acid metabolism
ORTHOLOGY   KO: K01575  acetolactate decarboxylase
GENES       YEN: YE4016(budA)
            ECA: ECA0740(budA)
            ENT: Ent638_2026
            SPE: Spro_3433
            VCH: VC1589
            VCO: VC0395_A1191(aldC)
            PAT: Patl_3762
            CBU: CBU_1097(aldC)
            MCA: MCA1838(budA)
            AHA: AHA_1125(budA)
            SUN: SUN_0870
            PCA: Pcar_2457
            SFU: Sfum_3912
            BSU: BG10472(alsD)
            BAN: BA0867(alsD)
            BAR: GBAA0867(alsD)
            BAA: BA_1448
            BAT: BAS0824
            BCE: BC0884
            BCA: BCE_0957(alsD)
            BCZ: BCZK0773(alsD)
            BTK: BT9727_0772(alsD)
            BTL: BALH_0785
            BLI: BL02479(alsD)
            BLD: BLi03847(alsD)
            BAY: RBAM_033160
            BPU: BPUM_3272
            SAU: SA2007 SA2394
            SAV: SAV2206 SAV2601
            SAM: MW2131 MW2520
            SAR: SAR2296 SAR2679
            SAS: SAS2105 SAS2486
            SAC: SACOL2198(budA1) SACOL2617(budA2)
            SAB: SAB2086c SAB2474c
            SAA: SAUSA300_2165(budA) SAUSA300_2536(budA)
            SAO: SAOUHSC_02467 SAOUHSC_02921
            SAJ: SaurJH9_2236 SaurJH9_2623
            SAH: SaurJH1_2275 SaurJH1_2677
            SEP: SE2143
            SER: SERP2154(budA)
            SHA: SH0462
            SSP: SSP0083
            LMO: lmo1992
            LMF: LMOf2365_2015(budA)
            LIN: lin2099
            LWE: lwe2011(budA)
            LLA: L0321(aldB) L0322(aldC)
            LLC: LACR_1209 LACR_1307
            LLM: llmg_1275(aldB) llmg_1464(aldC)
            SPN: SP_1392
            SPR: spr1249(aldB)
            SPD: SPD_1224(budA)
            SAG: SAG1191(budA)
            SAN: gbs1264
            SAK: SAK_1278(budA)
            SMU: SMU.1451(aldB)
            STC: str0924(aldB)
            STL: stu0924(aldB)
            SSA: SSA_0901(aldB)
            SGO: SGO_0853(budA)
            LPL: lp_2030(aldB)
            LJO: LJ1125
            LSA: LSA0981(aldB)
            LSL: LSL_0187(alsD)
            LBR: LVIS_0492
            LCA: LSEI_1840
            LRE: Lreu_0133
            EFA: EF1214(budA)
            OOE: OEOE_1704
            CAC: CAC2967
            MPE: MYPE6240(aldB)
            MMO: MMOB2010(alsD)
            CDI: DIP0990
            CJK: jk0157(alsD)
            SYE: Syncc9902_1512
            SYG: sync_0772(budA)
            SYR: SynRCC307_1716(alsD)
            PLT: Plut_1041
            MMP: MMP0613
            MMQ: MmarC5_0992
            MMZ: MmarC7_1636
            MVN: Mevan_1486
            MAC: MA3744(aldC)
            MBA: Mbar_A2915 Mbar_A2916
            MMA: MM_0639
            MBU: Mbur_1014
            MTP: Mthe_0909
            MHU: Mhun_0155
            MEM: Memar_0825
            MBN: Mboo_0212
            RCI: RCIX2494(alsD)
STRUCTURES  PDB: 1XV2  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.5
            ExPASy - ENZYME nomenclature database: 4.1.1.5
            ExplorEnz - The Enzyme Database: 4.1.1.5
            ERGO genome analysis and discovery system: 4.1.1.5
            BRENDA, the Enzyme Database: 4.1.1.5
            CAS: 9025-02-9
///
ENTRY       EC 4.1.1.6                  Enzyme
NAME        aconitate decarboxylase;
            cis-aconitic decarboxylase;
            CAD;
            cis-aconitate carboxy-lyase;
            cis-aconitate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     cis-aconitate carboxy-lyase (itaconate-forming)
REACTION    cis-aconitate = itaconate + CO2 [RN:R02243]
ALL_REAC    R02243
SUBSTRATE   cis-aconitate [CPD:C00417]
PRODUCT     itaconate [CPD:C00490];
            CO2 [CPD:C00011]
REFERENCE   1  [PMID:13438855]
  AUTHORS   BENTLEY R, THIESSEN CP.
  TITLE     Biosynthesis of itaconic acid in Aspergillus terreus.  III.  The
            properties and reaction mechanism of cis-aconitic acid
            decarboxylase.
  JOURNAL   J. Biol. Chem. 226 (1957) 703-20.
  ORGANISM  Aspergillus terreus
PATHWAY     PATH: map00660  C5-Branched dibasic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.6
            ExPASy - ENZYME nomenclature database: 4.1.1.6
            ExplorEnz - The Enzyme Database: 4.1.1.6
            ERGO genome analysis and discovery system: 4.1.1.6
            BRENDA, the Enzyme Database: 4.1.1.6
            CAS: 9025-01-8
///
ENTRY       EC 4.1.1.7                  Enzyme
NAME        benzoylformate decarboxylase;
            phenylglyoxylate decarboxylase;
            benzoylformate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     benzoylformate carboxy-lyase (benzaldehyde-forming)
REACTION    benzoylformate = benzaldehyde + CO2 [RN:R01764]
ALL_REAC    R01764;
            (other) R02672
SUBSTRATE   benzoylformate [CPD:C02137]
PRODUCT     benzaldehyde [CPD:C00261];
            CO2 [CPD:C00011]
COFACTOR    Thiamin diphosphate [CPD:C00068]
COMMENT     A thiamine-diphosphate protein.
REFERENCE   1  [PMID:13108854]
  AUTHORS   GUNSALUS CF, STANIER RY, GUNSALUS IC.
  TITLE     The enzymatic conversion of mandelic acid to benzoic acid. III.
            Fractionation and properties of the soluble enzymes.
  JOURNAL   J. Bacteriol. 66 (1953) 548-53.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00622  Toluene and xylene degradation
ORTHOLOGY   KO: K01576  benzoylformate decarboxylase
GENES       PAE: PA4901(mdlC)
            LPN: lpg0233(mdlC)
            CVI: CV_3101(mdlC)
            BMA: BMA0346(mdlC)
            BMV: BMASAVP1_A0645(mdlC)
            BML: BMA10299_A2480(mdlC)
            BMN: BMA10247_0093(mdlC)
            BXE: Bxe_B0137
            BUR: Bcep18194_A5914
            BCH: Bcen2424_2583
            BAM: Bamb_2631
            BPS: BPSL0842
            BPM: BURPS1710b_1048(mdlC)
            BPL: BURPS1106A_0890(mdlC)
            BPD: BURPS668_0887(mdlC)
            BTE: BTH_I0705
            SFU: Sfum_1851
            BJA: bll7603(mdlC) blr2689(mdlC) blr6416 blr7248
            BRA: BRADO1439(mdlC) BRADO1452 BRADO6150
            BBT: BBta_1644 BBta_6653 BBta_6666(mdlC)
            RPA: RPA1609(mdlC)
            RPB: RPB_3938
            RPD: RPD_3699
            RPE: RPE_1253 RPE_4305
            MSM: MSMEG_1606
            RHA: RHA1_ro02795(mdlC) RHA1_ro02985
            SCO: SCO7437(SC6D11.33c)
            SEN: SACE_0551(mdlC) SACE_3142(mdlC)
            NPH: NP1904A(ilvB_2)
            TAC: Ta0500 Ta0780
            TVO: TVN0784 TVN1197
            SSO: SSO1647(mdlC)
            SAI: Saci_1743
STRUCTURES  PDB: 1BFD  1MCZ  1PI3  1PO7  1Q6Z  1YNO  2FN3  2FWN  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.7
            ExPASy - ENZYME nomenclature database: 4.1.1.7
            ExplorEnz - The Enzyme Database: 4.1.1.7
            ERGO genome analysis and discovery system: 4.1.1.7
            UM-BBD (Biocatalysis/Biodegradation Database): 4.1.1.7
            BRENDA, the Enzyme Database: 4.1.1.7
            CAS: 9025-00-7
///
ENTRY       EC 4.1.1.8                  Enzyme
NAME        oxalyl-CoA decarboxylase;
            oxalyl coenzyme A decarboxylase;
            oxalyl-CoA carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     oxalyl-CoA carboxy-lyase (formyl-CoA-forming)
REACTION    oxalyl-CoA = formyl-CoA + CO2 [RN:R01908]
ALL_REAC    R01908
SUBSTRATE   oxalyl-CoA [CPD:C00313]
PRODUCT     formyl-CoA [CPD:C00798];
            CO2 [CPD:C00011]
COFACTOR    Thiamin diphosphate [CPD:C00068]
COMMENT     A thiamine-diphosphate protein.
REFERENCE   1
  AUTHORS   Quayle, J.R.
  TITLE     Carbon assimilation by Pseudomonas oxalaticus (OX1). 7.
            Decarboxylation of oxalyl-coenzyme A to formyl-coenzyme A.
  JOURNAL   Biochem. J. 89 (1963) 492-503.
  ORGANISM  Pseudomonas oxalaticus
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K01577  oxalyl-CoA decarboxylase
GENES       ECO: b2373(yfdU)
            ECJ: JW2370(oxc)
            ECE: Z3637
            ECS: ECs3253
            ECC: c2909
            ECI: UTI89_C2705
            ECP: ECP_2398
            ECV: APECO1_4163
            SFL: SF2440(yfdU)
            SFX: S2577
            SFV: SFV_2432
            SSN: SSON_2464
            SBO: SBO_2399
            SDY: SDY_2571
            REU: Reut_B4664
            REH: H16_B1712
            BXE: Bxe_B2759
            PNU: Pnuc_0637
            POL: Bpro_2800
            HAR: HEAR0353(oxc)
            MMS: mma_0399
            BJA: bll3157(oxc)
            BPU: BPUM_3103
            LAC: LBA0396
            LGA: LGAS_0248
            MTU: Rv0118c
            MTC: MT0126(oxc)
            MBO: Mb0122c(oxcA)
            MBB: BCG_0152c(oxcA)
            MPA: MAP3523c(oxcA)
            MSM: MSMEG_0157 MSMEG_5297
            MUL: MUL_4804(oxcA)
STRUCTURES  PDB: 2C31  2JI6  2JI7  2JI8  2JI9  2JIB  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.8
            ExPASy - ENZYME nomenclature database: 4.1.1.8
            ExplorEnz - The Enzyme Database: 4.1.1.8
            ERGO genome analysis and discovery system: 4.1.1.8
            BRENDA, the Enzyme Database: 4.1.1.8
            CAS: 9024-96-8
///
ENTRY       EC 4.1.1.9                  Enzyme
NAME        malonyl-CoA decarboxylase;
            malonyl coenzyme A decarboxylase;
            malonyl-CoA carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     malonyl-CoA carboxy-lyase (acetyl-CoA-forming)
REACTION    malonyl-CoA = acetyl-CoA + CO2 [RN:R00233]
ALL_REAC    R00233;
            (other) R05373
SUBSTRATE   malonyl-CoA [CPD:C00083]
PRODUCT     acetyl-CoA [CPD:C00024];
            CO2 [CPD:C00011]
COMMENT     Specific for malonyl-CoA. The enzyme from Pseudomonas ovalis also
            catalyses the reaction of EC 2.8.3.3 malonate CoA-transferase.
REFERENCE   1  [PMID:827976]
  AUTHORS   Buckner JS, Kolattukudy PE, Poulose AJ.
  TITLE     Purification and properties of malonyl-coenzyme A decarboxylase, a
            regulatory enzyme from the uropygial gland of goose.
  JOURNAL   Arch. Biochem. Biophys. 177 (1976) 539-51.
  ORGANISM  goose
REFERENCE   2
  AUTHORS   Takamura, Y. and Kitayama, Y.
  TITLE     Purification and some properties of malonate decarboxylase from
            Pseudomonas ovalis: an oligomeric enzyme with bifunctional
            properties.
  JOURNAL   Biochem. Int. 3 (1981) 483-491.
  ORGANISM  Pseudomonas ovalis
PATHWAY     PATH: map00410  beta-Alanine metabolism
            PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K01578  malonyl-CoA decarboxylase
GENES       HSA: 23417(MLYCD)
            MMU: 56690(Mlycd)
            RNO: 85239(Mlycd)
            CFA: 489688(MLYCD)
            GGA: 415812(MLYCD)
            SPU: 754019(LOC754019)
            TBR: Tb927.8.1060
            TCR: 506401.50 509605.10
            LMA: LmjF07.0730
            AEH: Mlg_2785
            MMW: Mmwyl1_3835
            REU: Reut_A0645
            REH: H16_A2981(mcd)
            RME: Rmet_2797
            PNU: Pnuc_0627
            RFR: Rfer_2049
            POL: Bpro_2091
            PNA: Pnap_2873
            AAV: Aave_1511
            AJS: Ajs_1077
            VEI: Veis_2754
            AZO: azo0623(matA)
            DAR: Daro_1774
            WBM: Wbm0668
            ERU: Erum2840(matA) Erum2880
            ERW: ERWE_CDS_02900
            ECN: Ecaj_0267
            ECH: ECH_0814
            SMD: Smed_5137
            RET: RHE_CH00920(matA)
            RLE: RL0990(matA)
            BRA: BRADO5781
            BBT: BBta_6289
            RPA: RPA0560(MLYCD)
            RPB: RPB_0704
            RPD: RPD_0148
            XAU: Xaut_0519
            RSQ: Rsph17025_3566
            RDE: RD1_1475(mcd)
            PDE: Pden_1720
            ACR: Acry_1683
            RRU: Rru_A1548
            MAG: amb2797
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.9
            ExPASy - ENZYME nomenclature database: 4.1.1.9
            ExplorEnz - The Enzyme Database: 4.1.1.9
            ERGO genome analysis and discovery system: 4.1.1.9
            BRENDA, the Enzyme Database: 4.1.1.9
            CAS: 9024-99-1
///
ENTRY       EC 4.1.1.10       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
COMMENT     Deleted entry: formerly aminomalonate decarboxylase. Now included
            with EC 4.1.1.12 aspartate 4-decarboxylase (EC 4.1.1.10 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.10
            ExPASy - ENZYME nomenclature database: 4.1.1.10
            ExplorEnz - The Enzyme Database: 4.1.1.10
            ERGO genome analysis and discovery system: 4.1.1.10
            BRENDA, the Enzyme Database: 4.1.1.10
///
ENTRY       EC 4.1.1.11                 Enzyme
NAME        aspartate 1-decarboxylase;
            aspartate alpha-decarboxylase;
            L-aspartate alpha-decarboxylase;
            aspartic alpha-decarboxylase;
            L-aspartate 1-carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     L-aspartate 1-carboxy-lyase (beta-alanine-forming)
REACTION    L-aspartate = beta-alanine + CO2 [RN:R00489]
ALL_REAC    R00489
SUBSTRATE   L-aspartate [CPD:C00049]
PRODUCT     beta-alanine [CPD:C00099];
            CO2 [CPD:C00011]
COMMENT     The Escherichia coli enzyme contains a pyruvoyl group.
REFERENCE   1  [PMID:381298]
  AUTHORS   Williamson JM, Brown GM.
  TITLE     Purification and properties of L-Aspartate-alpha-decarboxylase, an
            enzyme that catalyzes the formation of beta-alanine in Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 254 (1979) 8074-82.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
            PATH: map00410  beta-Alanine metabolism
ORTHOLOGY   KO: K01579  aspartate 1-decarboxylase
GENES       ECO: b0131(panD)
            ECJ: JW0127(panD)
            ECE: Z0142(panD)
            ECS: ECs0135
            ECC: c0160(panD)
            ECI: UTI89_C0144(panD)
            ECP: ECP_0139
            ECV: APECO1_1854
            ECW: EcE24377A_0133(panD)
            ECX: EcHS_A0135
            STY: STY0198(panD)
            STT: t0181(panD)
            SPT: SPA0186(panD)
            SEC: SC0180(panD)
            STM: STM0180(panD)
            YPE: YPO3403(panD)
            YPK: y0784(panD)
            YPM: YP_0282(panD)
            YPA: YPA_2904
            YPN: YPN_0686
            YPP: YPDSF_2953
            YPS: YPTB0728(panD)
            YPI: YpsIP31758_3345(panD)
            SFL: SF0128(panD)
            SFX: S0130(panD)
            SFV: SFV_0121(panD)
            SSN: SSON_0139(panD)
            SBO: SBO_0120(panD)
            SDY: SDY_0041(panD)
            ECA: ECA3323(panD)
            PLU: plu0870(panD)
            SGL: SG0486
            ENT: Ent638_0679
            SPE: Spro_3993
            XFA: XF0231
            XFT: PD0189(panD)
            XCC: XCC1770(panD)
            XCB: XC_2466
            XCV: XCV1818(panD)
            XAC: XAC1787(panD)
            XOO: XOO2361(panD)
            XOM: XOO_2243(XOO2243)
            PAE: PA4731
            PAU: PA14_62600(panD)
            PAP: PSPA7_5448(panD)
            PAR: Psyc_0169(panD)
            PCR: Pcryo_0182
            PRW: PsycPRwf_2108
            ACI: ACIAD2911(panD)
            SDE: Sde_1062
            PIN: Ping_0578
            CBU: CBU_0422(panD)
            CBD: COXBU7E912_1651(panD)
            LPN: lpg2929(panD)
            LPF: lpl2856(panD)
            LPP: lpp2996(panD)
            MCA: MCA2316(panD)
            FTU: FTT1391(panD)
            FTF: FTF1391(panD)
            FTW: FTW_0497(panD)
            FTL: FTL_0672
            FTH: FTH_0675(panD)
            FTA: FTA_0707(panD)
            FTN: FTN_1354(panD)
            TCX: Tcr_1522
            NOC: Noc_0887
            AEH: Mlg_0566
            HHA: Hhal_0673
            CSA: Csal_3067
            ABO: ABO_0335(panD)
            MMW: Mmwyl1_1263
            RMA: Rmag_0846
            VOK: COSY_0771(panD)
            NME: NMB1282
            NMA: NMA1492(panD)
            NMC: NMC1216(panD)
            NGO: NGO0620
            CVI: CV_1637(panD)
            RSO: RSc2731(panD)
            REH: H16_A3129(panD)
            BMA: BMA0700(panD)
            BMV: BMASAVP1_A2313(panD)
            BML: BMA10299_A2974(panD)
            BMN: BMA10247_1625(panD)
            BXE: Bxe_A3489
            BVI: Bcep1808_2527
            BUR: Bcep18194_A5774
            BCN: Bcen_1832
            BCH: Bcen2424_2443
            BAM: Bamb_2490
            BPS: BPSL0990(panD)
            BPM: BURPS1710b_1203(panD)
            BPL: BURPS1106A_1048(panD)
            BPD: BURPS668_1042(panD)
            BTE: BTH_I0847(panD)
            PNU: Pnuc_0652
            BPE: BP1816(panD)
            BPA: BPP1899(panD)
            BBR: BB3211(panD)
            RFR: Rfer_3032
            POL: Bpro_0901 Bpro_1578
            PNA: Pnap_0936
            AJS: Ajs_3494
            MPT: Mpe_A3569
            HAR: HEAR0328(panD)
            MMS: mma_0375
            DAR: Daro_3187
            TBD: Tbd_2055
            MFA: Mfla_0594
            HPY: HP0034
            HPA: HPAG1_0032
            HHE: HH0331(panD)
            HAC: Hac_0047(panD)
            WSU: WS1682(panD)
            TDN: Tmden_0334
            CJE: Cj0296c(panD)
            CJR: CJE0341(panD)
            CJJ: CJJ81176_0319(panD)
            CJU: C8J_0273(panD)
            CJD: JJD26997_1668(panD)
            CFF: CFF8240_0064(panD)
            CCV: CCV52592_0074(panD)
            CHA: CHAB381_0199(panD)
            CCO: CCC13826_1739(panD)
            ABU: Abu_0428(panD)
            NIS: NIS_0255(panD)
            SUN: SUN_2279(panD)
            GUR: Gura_2080
            PCA: Pcar_1828
            PPD: Ppro_3533
            BBA: Bd3565(panD)
            DPS: DP1942
            ADE: Adeh_4051
            AFW: Anae109_0377
            MXA: MXAN_6830(panD)
            SAT: SYN_00419
            SFU: Sfum_0368
            MLO: mll5826 mll9093
            ATU: Atu3667(panD)
            ATC: AGR_L_2336
            BJA: blr2096(panD)
            XAU: Xaut_2340
            CCR: CC_2295
            MMR: Mmar10_2123
            HNE: HNE_1379(panD)
            RRU: Rru_A0191
            MAG: amb4022
            BSU: BG11493(panD)
            BHA: BH1689(panD)
            BAN: BA1564(panD)
            BAR: GBAA1564(panD)
            BAA: BA_2083
            BAT: BAS1451
            BCE: BC1542
            BCA: BCE_1670(panD)
            BCZ: BCZK1424(panD)
            BCY: Bcer98_1264
            BTK: BT9727_1423(panD)
            BTL: BALH_1394
            BLI: BL02750(panD)
            BLD: BLi02376(panD)
            BCL: ABC2065(panD)
            BAY: RBAM_020560
            BPU: BPUM_1972
            OIH: OB1763(panD)
            GKA: GK2177(panD)
            SAU: SA2390(panD)
            SAV: SAV2597(panD)
            SAM: MW2516(panD)
            SAR: SAR2675(panD)
            SAS: SAS2482
            SAC: SACOL2613(panD)
            SAB: SAB2470c(panD)
            SAA: SAUSA300_2532(panD)
            SAO: SAOUHSC_02916
            SAJ: SaurJH9_2619
            SAH: SaurJH1_2673
            SEP: SE2139
            SER: SERP2150(panD)
            SHA: SH0183(panD)
            SSP: SSP0933
            LMO: lmo1900(panD)
            LMF: LMOf2365_1929(panD)
            LIN: lin2014(panD)
            LWE: lwe1919(panD)
            LPL: lp_0579(panD)
            EFA: EF1858(panD)
            CAC: CAC2916(panD)
            CNO: NT01CX_1073(panD)
            CTH: Cthe_0900
            CBO: CBO0423(panD)
            CBA: CLB_0456(panD)
            CBH: CLC_0489(panD)
            CBF: CLI_0508(panD)
            CBE: Cbei_2608
            CKL: CKL_1623(panD)
            CHY: CHY_2375(panD)
            DSY: DSY0212
            DRM: Dred_0162 Dred_1790
            SWO: Swol_0103
            CSC: Csac_2708
            MTA: Moth_0142
            MTU: Rv3601c(panD)
            MTC: MT3706.1(panD)
            MBO: Mb3631c(panD)
            MBB: BCG_3665c(panD)
            MLE: ML0231(panD)
            MPA: MAP0457(panD)
            MAV: MAV_0552(panD)
            MSM: MSMEG_0021(panD)
            MVA: Mvan_5363
            MGI: Mflv_1425
            MMC: Mmcs_4761
            MKM: Mkms_4847
            MJL: Mjls_5147
            CGL: NCgl0133(cgl0135)
            CGB: cg0172(panD)
            CEF: CE0135(panD)
            CJK: jk0292(panD)
            NFA: nfa4070(panD)
            RHA: RHA1_ro04416
            SCO: SCO0978(panD)
            SMA: SAV7245(panD)
            ART: Arth_3887
            AAU: AAur_3720(panD) AAur_pTC20125(panD)
            NCA: Noca_0461
            TFU: Tfu_1862
            FRA: Francci3_1112 Francci3_4376
            FAL: FRAAL6671(panD)
            ACE: Acel_0212
            SEN: SACE_0407(panD)
            STP: Strop_4282
            RBA: RB6090(panD)
            LIL: LA1729(panD)
            LIC: LIC12074(panD)
            LBJ: LBJ_1234(panD)
            LBL: LBL_1285(panD)
            SYN: sll0892(panD)
            GVI: glr2845 glr4228
            ANA: all3569
            AVA: Ava_3547
            TER: Tery_0692
            BTH: BT_4309
            BFR: BF1004
            BFS: BF0925(panD)
            PGI: PG1114(panD)
            SRU: SRU_1412(panD)
            CHU: CHU_3834(panD)
            GFO: GFO_3543(panD)
            FJO: Fjoh_0826
            FPS: FP0107(panD)
            CTE: CT0252(panD)
            CCH: Cag_1450
            CPH: Cpha266_0379
            PVI: Cvib_1551
            PLT: Plut_1769
            DET: DET0802(panD)
            DEH: cbdb_A780(panD)
            DEB: DehaBAV1_0726
            DRA: DR_0718
            DGE: Dgeo_1422
            TTH: TTC0241
            TTJ: TTHA0606
            AAE: aq_476(panD)
            TMA: TM0939
            TPT: Tpet_1803
            TME: Tmel_0284
            FNO: Fnod_0880
            HWA: HQ2363A(panD)
STRUCTURES  PDB: 1AW8  1PPY  1PQE  1PQF  1PQH  1PT0  1PT1  1PYQ  1PYU  1UHD  
                 1UHE  2C45  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.11
            ExPASy - ENZYME nomenclature database: 4.1.1.11
            ExplorEnz - The Enzyme Database: 4.1.1.11
            ERGO genome analysis and discovery system: 4.1.1.11
            BRENDA, the Enzyme Database: 4.1.1.11
            CAS: 9024-58-2
///
ENTRY       EC 4.1.1.12                 Enzyme
NAME        aspartate 4-decarboxylase;
            desulfinase;
            aminomalonic decarboxylase;
            aspartate beta-decarboxylase;
            aspartate omega-decarboxylase;
            aspartic omega-decarboxylase;
            aspartic beta-decarboxylase;
            L-aspartate beta-decarboxylase;
            cysteine sulfinic desulfinase;
            L-cysteine sulfinate acid desulfinase;
            L-aspartate 4-carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     L-aspartate 4-carboxy-lyase (L-alanine-forming)
REACTION    L-aspartate = L-alanine + CO2 [RN:R00397]
ALL_REAC    R00397;
            (other) R00863
SUBSTRATE   L-aspartate [CPD:C00049]
PRODUCT     L-alanine [CPD:C00041];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also catalyses the decarboxylation of
            aminomalonate (formerly listed as EC 4.1.1.10), and the
            desulfination of 3-sulfino-L-alanine to sulfite and alanine.
REFERENCE   1  [PMID:5773301]
  AUTHORS   Kakimoto T, Kato J, Shibatani T, Nishimura N, Chibata I.
  TITLE     Crystalline L-aspartate beta-decarboxylase of Pseudomonas dacunhae.
            I. Crystallization and some physiocochemical properties.
  JOURNAL   J. Biol. Chem. 244 (1969) 353-8.
  ORGANISM  Pseudomonas dacunhae
REFERENCE   2
  AUTHORS   Novogrodsky, A. and Meister, A.
  TITLE     Control of aspartate beta-decarboxylase activity by transamination.
  JOURNAL   J. Biol. Chem. 239 (1964) 879-888.
  ORGANISM  Pseudomonas dacunhae
REFERENCE   3  [PMID:5424207]
  AUTHORS   Palekar AG, Tate SS, Meister A.
  TITLE     Inhibition of aspartate beta-decarboxylase by aminomalonate.
            Stereospecific decarboxylation of aminomalonate to glycine.
  JOURNAL   Biochemistry. 9 (1970) 2310-5.
  ORGANISM  Alcaligenes faecalis
REFERENCE   4
  AUTHORS   Wilson, E.M. and Kornberg, H.L.
  TITLE     Properties of crystalline L-aspartate 4-carboxy-lyase from
            Achromobacter sp.
  JOURNAL   Biochem. J. 88 (1963) 578-587.
  ORGANISM  Achromobacter sp.
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
            PATH: map00272  Cysteine metabolism
ORTHOLOGY   KO: K09758  aspartate 4-decarboxylase
GENES       REH: H16_A3009(asdA)
            MMS: mma_1084
            ZMO: ZMO1682(asdA)
            LSA: LSA0306(aspD)
            CBO: CBO1166(asdA)
            CBA: CLB_1197(asdA)
            CBH: CLC_1209(asdA)
            CBF: CLI_1247(asdA)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.12
            ExPASy - ENZYME nomenclature database: 4.1.1.12
            ExplorEnz - The Enzyme Database: 4.1.1.12
            ERGO genome analysis and discovery system: 4.1.1.12
            BRENDA, the Enzyme Database: 4.1.1.12
            CAS: 9024-57-1
///
ENTRY       EC 4.1.1.13       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
COMMENT     Deleted entry: carbamoylaspartate decarboxylase (EC 4.1.1.13 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.13
            ExPASy - ENZYME nomenclature database: 4.1.1.13
            ExplorEnz - The Enzyme Database: 4.1.1.13
            ERGO genome analysis and discovery system: 4.1.1.13
            BRENDA, the Enzyme Database: 4.1.1.13
///
ENTRY       EC 4.1.1.14                 Enzyme
NAME        valine decarboxylase;
            leucine decarboxylase;
            L-valine carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     L-valine carboxy-lyase (2-methylpropanamine-forming)
REACTION    L-valine = 2-methylpropanamine + CO2 [RN:R01437]
ALL_REAC    R01437
SUBSTRATE   L-valine [CPD:C00183]
PRODUCT     2-methylpropanamine [CPD:C02787];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also acts on L-leucine.
REFERENCE   1
  AUTHORS   Sutton, C.R. and King, H.K.
  TITLE     Inhibition of leucine decarboxylase by thiol-binding reagents.
  JOURNAL   Arch. Biochem. Biophys. 96 (1962) 360-370.
  ORGANISM  Proteus vulgaris
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.14
            ExPASy - ENZYME nomenclature database: 4.1.1.14
            ExplorEnz - The Enzyme Database: 4.1.1.14
            ERGO genome analysis and discovery system: 4.1.1.14
            UM-BBD (Biocatalysis/Biodegradation Database): 4.1.1.14
            BRENDA, the Enzyme Database: 4.1.1.14
            CAS: 9031-16-7
///
ENTRY       EC 4.1.1.15                 Enzyme
NAME        glutamate decarboxylase;
            L-glutamic acid decarboxylase;
            L-glutamic decarboxylase;
            cysteic acid decarboxylase;
            L-glutamate alpha-decarboxylase;
            aspartate 1-decarboxylase;
            aspartic alpha-decarboxylase;
            L-aspartate-alpha-decarboxylase;
            gamma-glutamate decarboxylase;
            L-glutamate 1-carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     L-glutamate 1-carboxy-lyase (4-aminobutanoate-forming)
REACTION    L-glutamate = 4-aminobutanoate + CO2 [RN:R00261]
ALL_REAC    R00261;
            (other) R00489 R01682 R02466
SUBSTRATE   L-glutamate [CPD:C00025]
PRODUCT     4-aminobutanoate [CPD:C00334];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. The brain enzyme also acts on
            L-cysteate, 3-sulfino-L-alanine and L-aspartate.
REFERENCE   1  [PMID:14081858]
  AUTHORS   AMBE L, SOHONIE K.
  TITLE     PURIFICATION AND PROPORTIES OF GLUTAMATE DECARBOXYLASE FROM FIELD
            BEAN (DOLICHOS LABLAB).
  JOURNAL   Enzymologia. 26 (1963) 98-107.
  ORGANISM  Dolichos lablab
REFERENCE   2  [PMID:4937550]
  AUTHORS   Nakano Y, Kitaoka S.
  TITLE     L-aspartate  -decarboxylase in a cell-free system from Escherichia
            coli.
  JOURNAL   J. Biochem. (Tokyo). 70 (1971) 327-34.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Roberts, E. and Frankel, S.
  TITLE     Further studies of glutamic acid decarboxylase in brain.
  JOURNAL   J. Biol. Chem. 190 (1951) 505-512.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00252  Alanine and aspartate metabolism
            PATH: map00410  beta-Alanine metabolism
            PATH: map00430  Taurine and hypotaurine metabolism
            PATH: map00650  Butanoate metabolism
            PATH: map04940  Type I diabetes mellitus
ORTHOLOGY   KO: K01580  glutamate decarboxylase
GENES       HSA: 2571(GAD1) 2572(GAD2)
            PTR: 466026(GAD2) 468557(GAD1)
            MCC: 613029(GAD2)
            MMU: 14415(Gad1) 14417(Gad2)
            RNO: 24379(Gad1) 24380(Gad2)
            CFA: 478794(GAD1) 487107(GAD2)
            SSC: 396928(GAD1) 396929(GAD2)
            GGA: 395395(GAD2) 395743(GAD1)
            DRE: 378441(gad1)
            SPU: 579659(LOC579659)
            DME: Dmel_CG14994(Gad1) Dmel_CG7811(b)
            CEL: Y37D8A.23(unc-25)
            ATH: AT2G02000 AT3G17760 AT5G17330(GAD)
            OSA: 4332184 4333932 4335973 4335977 4345787
            CME: CMF072C
            SCE: YMR250W(GAD1)
            PIC: PICST_40180(DCE1) PICST_55334(GAD2) PICST_87778(DPL1)
            ANI: AN5447.2
            AFM: AFUA_3G11120 AFUA_6G13490 AFUA_8G06020
            AOR: AO090003000666 AO090005000539 AO090103000342
            CNE: CNH03700
            UMA: UM02125.1
            DDI: DDB_0231439(gadB) DDB_0231446(gadA)
            TET: TTHERM_00289080
            EHI: 208.t00008 73.t00003
            ECO: b1493(gadB) b3517(gadA)
            ECJ: JW1488(gadB) JW3485(gadA)
            ECE: Z2215(gadB) Z4930(gadA)
            ECS: ECs2098 ECs4397
            ECC: c1922(gadB) c4328(gadA)
            ECI: UTI89_C1707(gadB) UTI89_C4049(gadA)
            ECP: ECP_1489 ECP_3616
            ECV: APECO1_2931(gadB) APECO1_621(gadA)
            ECW: EcE24377A_1682(gadB) EcE24377A_4005(gadA)
            ECX: EcHS_A1578(gadB) EcHS_A3720(gadA)
            YEN: YE3693(gadA)
            SFL: SF1734(gadB) SF3594(gadA)
            SFX: S1867(gadB) S4173(gadA)
            SFV: SFV_1730(gadB) SFV_3989(gadA)
            SSN: SSON_1631(gadB) SSON_3569(gadA)
            SBO: SBO_1563(gadB) SBO_3516(gadA)
            SDY: SDY_1615(gadB)
            VCH: VC1149
            VVU: VV1_2824
            VVY: VV1442
            VPA: VP1237
            VFI: VF0892 VF1064
            PPR: PBPRA1498
            SDN: Sden_2434
            SHN: Shewana3_2686
            ILO: IL2256(gadB)
            CPS: CPS_1007
            PAT: Patl_3931
            FTU: FTT1722c(gad)
            FTF: FTF1722c(gad)
            FTW: FTW_0076
            FTL: FTL_1862 FTL_1863
            FTA: FTA_1969
            FTN: FTN_1701
            HCH: HCH_00996
            AHA: AHA_3494
            REU: Reut_A1624
            RME: Rmet_0460 Rmet_1766
            BXE: Bxe_A3826 Bxe_C0551
            BPA: BPP1580
            BBR: BB2658
            GSU: GSU1707
            GME: Gmet_1644
            LIP: LI0261(gad)
            DPS: DP0385
            SAT: SYN_00664
            BME: BMEII0910 BMEII0911
            BMF: BAB2_0865 BAB2_0866
            BCA: BCE_2691
            LMO: lmo2363 lmo2434
            LMF: LMOf2365_2334(gadB) LMOf2365_2405(gadG)
            LIN: lin2463 lin2528
            LWE: lwe2381(gadB)
            LLA: L123581(gadB)
            LLM: llmg_1179(gadB)
            LPL: lp_3420(gadB)
            LBR: LVIS_0079 LVIS_1847 LVIS_2213
            CPE: CPE2058
            CPF: CPF_2315
            CPR: CPR_2029
            CBO: CBO1917(gadA)
            CBA: CLB_1854
            CBH: CLC_1861
            CBF: CLI_1981
            MTU: Rv3432c(gadB)
            MTC: MT3538(gadB)
            MBO: Mb3462c(gadB)
            MBB: BCG_3498c(gadB)
            MPA: MAP4257(gadB)
            MAV: MAV_4373
            MSM: MSMEG_1574
            MVA: Mvan_1483
            MGI: Mflv_4935
            MMC: Mmcs_1145
            MKM: Mkms_1162
            MJL: Mjls_1172
            NFA: nfa35400
            RHA: RHA1_ro06016(gadA)
            SCO: SCO3416(gad)
            SMA: SAV3601(gadB1) SAV4655(gadB2)
            AAU: AAur_3971
            FRA: Francci3_0181
            FAL: FRAAL0380(gadB)
            SYN: sll1641(gad)
            SYG: sync_0455
            SYR: SynRCC307_1544(gadA)
            PMT: PMT0474(gadA)
            PMF: P9303_18041
            BTH: BT_2570
            BFR: BF0454
            BFS: BF0393(gadB)
            MAC: MA1949
            MBA: Mbar_A2744
            AFU: AF1323 AF2295
            APE: APE_0412 APE_2267.1
STRUCTURES  PDB: 1NWD  1PMM  1PMO  1XEY  2DGK  2DGL  2DGM  2OKJ  2OKK  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.15
            ExPASy - ENZYME nomenclature database: 4.1.1.15
            ExplorEnz - The Enzyme Database: 4.1.1.15
            ERGO genome analysis and discovery system: 4.1.1.15
            BRENDA, the Enzyme Database: 4.1.1.15
            CAS: 9024-58-2
///
ENTRY       EC 4.1.1.16                 Enzyme
NAME        hydroxyglutamate decarboxylase;
            3-hydroxy-L-glutamate 1-carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     3-hydroxy-L-glutamate 1-carboxy-lyase
            (4-amino-3-hydroxybutanoate-forming)
REACTION    3-hydroxy-L-glutamate = 4-amino-3-hydroxybutanoate + CO2 [RN:R04135]
ALL_REAC    R04135
SUBSTRATE   3-hydroxy-L-glutamate [CPD:C03066]
PRODUCT     4-amino-3-hydroxybutanoate [CPD:C03678];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1
  AUTHORS   Umbreit, W.W. and Heneage, P.
  TITLE     beta-Hydroxyglutamic acid decarboxylase.
  JOURNAL   J. Biol. Chem. 201 (1953) 15-20.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.16
            ExPASy - ENZYME nomenclature database: 4.1.1.16
            ExplorEnz - The Enzyme Database: 4.1.1.16
            ERGO genome analysis and discovery system: 4.1.1.16
            BRENDA, the Enzyme Database: 4.1.1.16
            CAS: 9024-59-3
///
ENTRY       EC 4.1.1.17                 Enzyme
NAME        ornithine decarboxylase;
            SpeC;
            L-ornithine carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     L-ornithine carboxy-lyase (putrescine-forming)
REACTION    L-ornithine = putrescine + CO2 [RN:R00670]
ALL_REAC    R00670
SUBSTRATE   L-ornithine [CPD:C00077]
PRODUCT     putrescine [CPD:C00134];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:5073764]
  AUTHORS   Ono M, Inoue H, Suzuki F, Takeda Y.
  TITLE     Studies on ornithine decarboxylase from the liver of
            thioacetamide-treated rats. Purification and some properties.
  JOURNAL   Biochim. Biophys. Acta. 284 (1972) 285-97.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Taylor, E.S. and Gale, E.F.
  TITLE     Studies on bacterial amino-acid decarboxylases. 6. Codecarboxylase
            content and action of inhibitors.
  JOURNAL   Biochem. J. 39 (1945) 52-58.
  ORGANISM  Clostridium septicum
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K01581  ornithine decarboxylase
GENES       HSA: 4953(ODC1)
            MMU: 18263(Odc1)
            RNO: 24609(Odc1)
            CFA: 475666(ODC1)
            BTA: 281365(ODC1)
            GGA: 421937(ODC1)
            XLA: 379379(MGC52527) 379859(odc1)
            XTR: 448028(odc1)
            DRE: 114426(odc1)
            SPU: 589060(LOC589060)
            DME: Dmel_CG8719(Odc2) Dmel_CG8721(Odc1)
            CEL: K11C4.4(odc-1)
            OSA: 4347746
            CME: CMA052C
            SCE: YKL184W(SPE1)
            AGO: AGOS_AER087C
            PIC: PICST_90612(SPE1)
            CGR: CAGL0D00484g
            SPO: SPAC144.04c(spe1)
            ANI: AN3846.2
            AFM: AFUA_4G08010 AFUA_7G08450 AFUA_8G06540
            AOR: AO090023000771
            CNE: CNC04890
            UMA: UM01048.1
            DDI: DDBDRAFT_0204020
            PFA: PF10_0322
            TET: TTHERM_00462900
            TBR: Tb11.01.5300
            LMA: LmjF12.0280
            EHI: 36.t00008
            ECO: b0693(speF) b2965(speC)
            ECJ: JW0680(speF) JW5482(speC)
            ECE: Z0839(speF) Z4310(speC)
            ECS: ECs0721 ECs3841
            ECC: c0777(speF) c3553(speC)
            ECI: UTI89_C0695(speF) UTI89_C3356(speC)
            ECP: ECP_0711 ECP_2959
            ECV: APECO1_1374(speF) APECO1_3536(speC)
            ECW: EcE24377A_0718(speF) EcE24377A_3311(speC)
            ECX: EcHS_A3126(speC)
            STY: STY0739(speF) STY3270(speC)
            SPT: SPA2040(speF) SPA2977(speC)
            SEC: SC0721(speF) SC3055(speC)
            STM: STM0701(speF) STM3114(speC)
            YPE: YPO0960(speC)
            YPK: y3347(speC)
            YPM: YP_3481(speC)
            YPA: YPA_0304
            YPN: YPN_3158
            YPP: YPDSF_0554
            YPS: YPTB3232(speC)
            YPI: YpsIP31758_0811(speC)
            YEN: YE0455(speF) YE3527(speF2)
            SFL: SF2962(speC)
            SFX: S3165(speC)
            SFV: SFV_3024(speC)
            SSN: SSON_0644(speF) SSON_3230(speC)
            SBO: SBO_0554(speF)
            SDY: SDY_3107(speC)
            ECA: ECA0967(speC)
            ENT: Ent638_1205 Ent638_3380
            SPE: Spro_0509 Spro_4047
            HSO: HS_1573(speF)
            PMU: PM0806(speF)
            VCH: VCA1063
            VCO: VC0395_0179(speF)
            VVU: VV2_1030 VV2_1235
            VVY: VVA0063 VVA1524
            VPA: VPA1635
            PAE: PA4519
            PAU: PA14_58630(speC)
            PPU: PP_0864
            PPF: Pput_0894
            PST: PSPTO_4572
            PSB: Psyr_4247
            PSP: PSPPH_4273
            PFL: PFL_0867
            PFO: Pfl_0801
            PEN: PSEEN1035
            PMY: Pmen_0801
            PAR: Psyc_0029
            PCR: Pcryo_0037
            PRW: PsycPRwf_1157
            ACI: ACIAD2768
            SON: SO_0314(speF) SO_4136
            SAZ: Sama_0410 Sama_3334
            SBL: Sbal_4084
            SBM: Shew185_4053
            SLO: Shew_3392
            SPC: Sputcn32_3679
            SHE: Shewmr4_3667
            SHM: Shewmr7_0278
            SHN: Shewana3_3871
            SHW: Sputw3181_3821
            PIN: Ping_1416
            MAQ: Maqu_0077
            CBU: CBU_0722
            TCX: Tcr_0274
            MMW: Mmwyl1_2175
            AHA: AHA_1270
            DNO: DNO_0014
            BXE: Bxe_C0745
            BUR: Bcep18194_B2075
            BCN: Bcen_4358
            BCH: Bcen2424_4008
            NEU: NE0909(speC)
            NET: Neut_1387
            NMU: Nmul_A1964
            PUB: SAR11_0204(speC)
            MLO: mll1584 mll2974
            MES: Meso_2027 Meso_2715
            SME: SMa0680 SMa0682 SMc02983
            SMD: Smed_5195
            ATU: Atu3196(speF)
            ATC: AGR_L_3227
            RET: RHE_CH03629(ypch01283)
            RLE: RL4156
            BME: BMEII1133
            BMF: BAB2_0098
            BMS: BRA0100
            BMB: BruAb2_0099
            BJA: bll3177 blr7759(speF)
            BRA: BRADO4919(speF) BRADO6260
            BBT: BBta_1349 BBta_3132(speF)
            RPA: RPA0870 RPA2051
            RPB: RPB_4547
            RPC: RPC_4837
            RPD: RPD_0856
            RPE: RPE_3166 RPE_4802
            NWI: Nwi_0924
            NHA: Nham_3419
            BHE: BH12730
            BQU: BQ10050(odc)
            XAU: Xaut_0640
            CCR: CC_0360
            SIL: SPO0364
            SIT: TM1040_3110
            RSP: RSP_1991
            JAN: Jann_0801
            MMR: Mmar10_0377
            ZMO: ZMO1020(lysA)
            GOX: GOX0440
            GBE: GbCGDNIH1_0522
            RRU: Rru_A1693
            MAG: amb1108 amb1388
            LJO: LJ1843
            LAC: LBA0996
            LSL: LSL_0138
            LDB: Ldb0547 Ldb1775
            LBU: LBUL_0489 LBUL_1645
            LCA: LSEI_1654
            NFA: nfa37850
            SCO: SCO6035(SC1C3.23)
            SEN: SACE_1266 SACE_4334(odc)
            FNU: FN0501
            RBA: RB8469(odc)
            TDE: TDE1109
            AAE: aq_728(speC)
            TMA: TM1873
            MAC: MA2728
            MBA: Mbar_A2177
            MMA: MM_3185
            HMA: rrnAC0198(odc)
STRUCTURES  PDB: 1C4K  1D7K  1F3T  1NJJ  1ORD  1QU4  1SZR  2ON3  2OO0  2PLJ  
                 2PLK  2TOD  7ODC  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.17
            ExPASy - ENZYME nomenclature database: 4.1.1.17
            ExplorEnz - The Enzyme Database: 4.1.1.17
            ERGO genome analysis and discovery system: 4.1.1.17
            BRENDA, the Enzyme Database: 4.1.1.17
            CAS: 9024-60-6
///
ENTRY       EC 4.1.1.18                 Enzyme
NAME        lysine decarboxylase;
            L-lysine carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     L-lysine carboxy-lyase (cadaverine-forming)
REACTION    L-lysine = cadaverine + CO2 [RN:R00462]
ALL_REAC    R00462
SUBSTRATE   L-lysine [CPD:C00047]
PRODUCT     cadaverine [CPD:C01672];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also acts on 5-hydroxy-L-lysine.
REFERENCE   1
  AUTHORS   Gale, E.F. and Epps, H.M.R.
  TITLE     Studies on bacterial amino-acid decarboxylases. 1. l(+)-lysine
            decarboxylase.
  JOURNAL   Biochem. J. 38 (1944) 232-242.
  ORGANISM  Escherichia coli [GN:eco], Bacterium cardaveris
REFERENCE   2  [PMID:5762458]
  AUTHORS   Soda K, Moriguchi M.
  TITLE     Crystalline lysine decarboxylase.
  JOURNAL   Biochem. Biophys. Res. Commun. 34 (1969) 34-9.
  ORGANISM  Escherichia coli [GN:eco], Bacterium cardaveris
PATHWAY     PATH: map00310  Lysine degradation
            PATH: map00960  Alkaloid biosynthesis II
ORTHOLOGY   KO: K01582  lysine decarboxylase
GENES       PFA: PFD0285c
            ECO: b0186(ldcC) b4131(cadA)
            ECJ: JW0181(ldcC) JW4092(cadA)
            ECE: Z0198(ldcC) Z5734(cadA)
            ECS: ECs0188 ECs5113
            ECC: c0224(ldcC) c5140(cadA)
            ECI: UTI89_C0201(ldcC) UTI89_C4728(cadA)
            ECP: ECP_0194 ECP_0327 ECP_4375
            ECV: APECO1_2322(cadA)
            ECW: EcE24377A_0190(ldcC)
            ECX: EcHS_A0188(ldcC1) EcHS_A4372(ldcC2)
            STY: STY0259(ldcC) STY2806(cadA)
            STT: t0236(ldcC) t0297(cadA)
            SPT: SPA0241(ldcC) SPA0307(cadA)
            SEC: SC0234(ldcC) SC2554(cadA)
            STM: STM0234(ldcC) STM2559(cadA)
            YPN: YPN_2775
            YEN: YE3267(ldcC)
            SFL: SF0176(ldcC)
            SFX: S0179(ldcC)
            SFV: SFV_0169(ldcC)
            SSN: SSON_0199(ldcC)
            ENT: Ent638_0724
            SPE: Spro_3767 Spro_3773 Spro_4822
            HSO: HS_1007(cadA)
            VCH: VC0281
            VCO: VC0395_A2658(cadA)
            VVU: VV1_2060
            VVY: VV2381
            VPA: VP2890
            VFI: VF2057
            PPF: Pput_1725
            PEN: PSEEN3557
            PMY: Pmen_2068
            PHA: PSHAa1094
            SDE: Sde_2967
            FTU: FTT0406(cadA)
            FTF: FTF0406(cadA)
            FTW: FTW_1667(cadA)
            FTL: FTL_0476
            FTH: FTH_0474(cadA)
            FTA: FTA_0502
            FTN: FTN_0504
            AHA: AHA_1192
            CVI: CV_1992
            REU: Reut_A0689
            BVI: Bcep1808_2516 Bcep1808_5440
            BUR: Bcep18194_A5763 Bcep18194_B0779 Bcep18194_B2074
            BCN: Bcen_1821 Bcen_4356
            BCH: Bcen2424_2432 Bcen2424_4010
            BAM: Bamb_2479 Bamb_4345
            PNU: Pnuc_0651
            RFR: Rfer_2126
            POL: Bpro_2415
            PNA: Pnap_2020
            AAV: Aave_3257
            AJS: Ajs_2762
            VEI: Veis_3498
            MFA: Mfla_0915 Mfla_1059
            SMD: Smed_5196
            BHA: BH2640(cad)
            BAN: BA4172(cad-2)
            BAR: GBAA4172(cad-2)
            BAA: BA_4643
            BAT: BAS3874
            BCA: BCE_0027(cad) BCE_4009(cad)
            BCZ: BCZK0025(cad)
            BTK: BT9727_0025(cad) BT9727_3707(cad)
            BTL: BALH_0025(cad)
            BCL: ABC0049 ABC1937
            BAY: RBAM_014490(speA)
            BPU: BPUM_1361(speA)
            OIH: OB0035
            GKA: GK1065(cad)
            SAB: SAB0430
            SAA: SAUSA300_0458
            LWE: lwe2643
            SPN: SP_0916
            SPR: spr0816(cad)
            SPD: SPD_0809(cad)
            CAC: CAC2338
            CPE: CPE0549(dclY)
            CPF: CPF_0528
            CPR: CPR_0514
            CTC: CTC02271
            CBO: CBO0053
            CHY: CHY_0049(cad)
            DSY: DSY0236
            SWO: Swol_1357
            TTE: TTE0093(ldcC) TTE1027(ldcC2)
            MTA: Moth_2265
            MPA: MAP2144
            NFA: nfa6850
            SCO: SCO7311(SC5F8.21c)
            SYN: sll1683(cad)
            SYW: SYNW0944(cad)
            SYC: syc0823_d(cad)
            SYF: Synpcc7942_0707
            SYG: sync_1022(cad)
            TEL: tlr1866
            GVI: gll3487
            ANA: all4887
            PMA: Pro1112(ldcC)
            PMM: PMM1084(cad)
            PMT: PMT1066(cad)
            PMN: PMN2A_0665
            PMB: A9601_11901(cad)
            PMC: P9515_11741(cad)
            PMF: P9303_09861(cad)
            PMG: P9301_11911(cad)
            PME: NATL1_14971(cad)
            MEM: Memar_1269
            MBN: Mboo_0144
STRUCTURES  PDB: 1T35  2PLJ  2PLK  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.18
            ExPASy - ENZYME nomenclature database: 4.1.1.18
            ExplorEnz - The Enzyme Database: 4.1.1.18
            ERGO genome analysis and discovery system: 4.1.1.18
            BRENDA, the Enzyme Database: 4.1.1.18
            CAS: 9024-76-4
///
ENTRY       EC 4.1.1.19                 Enzyme
NAME        arginine decarboxylase;
            SpeA;
            L-arginine carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     L-arginine carboxy-lyase (agmatine-forming)
REACTION    L-arginine = agmatine + CO2 [RN:R00566]
ALL_REAC    R00566;
            (other) R00261
SUBSTRATE   L-arginine [CPD:C00062]
PRODUCT     agmatine [CPD:C00179];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:4870599]
  AUTHORS   Blethen SL, Boeker EA, Snell EE.
  TITLE     Argenine decarboxylase from Escherichia coli. I. Purification and
            specificity for substrates and coenzyme.
  JOURNAL   J. Biol. Chem. 243 (1968) 1671-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:1252]
  AUTHORS   Ramakrishna S, Adiga PR.
  TITLE     Arginine decarboxylase from Lathyrus sativus seedlings. Purification
            and properites.
  JOURNAL   Eur. J. Biochem. 59 (1975) 377-86.
  ORGANISM  Lathyrus sativus
REFERENCE   3
  AUTHORS   Taylor, E.S. and Gale, E.F.
  TITLE     Studies on bacterial amino-acid decarboxylases. 6. Codecarboxylase
            content and action of inhibitors.
  JOURNAL   Biochem. J. 39 (1945) 52-58.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00251  Glutamate metabolism
ORTHOLOGY   KO: K01583  arginine decarboxylase
            KO: K01584  arginine decarboxylase
            KO: K01585  arginine decarboxylase
            KO: K02626  arginine decarboxylase
GENES       HSA: 113451(ADC)
            MMU: 242669(Adc)
            ATH: AT2G16500(ADC1)
            OSA: 4334917 4340008
            TET: TTHERM_00267950
            EHI: 400.t00004
            ECO: b2938(speA) b4117(adiA)
            ECJ: JW2905(speA) JW5731(adiA)
            ECE: Z4283(speA) Z5719(adiA)
            ECS: ECs3814 ECs5099
            ECC: c3524(speA) c4501 c5122(adiA)
            ECI: UTI89_C3327(speA) UTI89_C4711(adiA)
            ECP: ECP_2933 ECP_4360
            ECV: APECO1_2334(adiA) APECO1_3590(speA)
            ECW: EcE24377A_3281(speA) EcE24377A_4671(adiA)
            ECX: EcHS_A3096(speA) EcHS_A4358
            STY: STY3240(speA) STY4495(adi)
            STT: t2999(speA) t4203(adi)
            SPT: SPA2950(speA) SPA4114(adi)
            SEC: SC3026(speA) SC4175(adi)
            STM: STM3086(speA) STM4296(adi)
            YPE: YPO0929(speA) YPO1201
            YPK: y2987(adiA) y3313(speA)
            YPM: YP_0936(adiA) YP_3513(speA)
            YPA: YPA_0336 YPA_0913
            YPN: YPN_3126
            YPP: YPDSF_2494
            YPS: YPTB1241 YPTB3202(speA)
            YPI: YpsIP31758_0843(speA) YpsIP31758_2781(adiA)
            SFL: SF2931(speA) SF4106(adiA)
            SFX: S3133(speA) S3624(adiA)
            SFV: SFV_2993(speA) SFV_4113(adiA)
            SSN: SSON_3092(speA) SSON_4292(adiA)
            SBO: SBO_3051(speA) SBO_4144(adiA)
            SDY: SDY_3134(speA) SDY_4094(adiA)
            ECA: ECA3918(speA)
            PLU: plu3319(adiA) plu3681(speA)
            SGL: SG2018
            PMU: PM1382(speA)
            XFA: XF0144
            XFT: PD0113(speA)
            XCC: XCC3868(speA)
            XCB: XC_3953
            XCV: XCV4038(speA)
            XAC: XAC3923(speA)
            XOO: XOO0220(speA)
            XOM: XOO_0195(XOO0195)
            VCH: VCA0815
            VCO: VC0395_0419(speA)
            VVU: VV1_2356 VV1_2357
            VVY: VV1986
            VPA: VPA0170
            VFI: VFA0840
            PAE: PA1818 PA4839(speA)
            PAU: PA14_41020(adi) PA14_63990(speA)
            PAP: PSPA7_5559(speA)
            PPU: PP_0567(speA)
            PST: PSPTO_4842(speA)
            PSB: Psyr_4381
            PSP: PSPPH_4424(speA)
            PFL: PFL_0679(speA) PFL_3293
            PFO: Pfl_0627 Pfl_2188
            PEN: PSEEN4847(speA)
            ACI: ACIAD3341
            SON: SO_1870(speA)
            SDN: Sden_2280
            SFR: Sfri_1698
            SAZ: Sama_1963
            SBL: Sbal_1768
            SLO: Shew_1619
            SHE: Shewmr4_1557
            SHM: Shewmr7_1632
            SHN: Shewana3_1624
            SHW: Sputw3181_2379
            ILO: IL1213(speA)
            PHA: PSHAa1075(speA) PSHAa2846(speA)
            PAT: Patl_3873
            SDE: Sde_1598
            PIN: Ping_0861
            MAQ: Maqu_0520
            LPN: lpg0006(speA)
            LPF: lpl0006(speA)
            LPP: lpp0006(speA)
            MCA: MCA2047(speA)
            FTU: FTT0432(speA)
            FTF: FTF0432(speA)
            FTL: FTL_0501
            NOC: Noc_0557
            AEH: Mlg_0072
            HHA: Hhal_2412
            HCH: HCH_06406(speA)
            CSA: Csal_0544
            ABO: ABO_2398(speA)
            AHA: AHA_1613(speA)
            NME: NMB0468
            NMA: NMA2017(speA)
            NMC: NMC1682(speA)
            NGO: NGO1487(speA)
            CVI: CV_2876(speA) CV_4040(adi)
            RSO: RSc2365(adi)
            REH: H16_A2930(ldcC)
            BMA: BMA0715
            BXE: Bxe_A3477
            BPS: BPSL1003
            BPM: BURPS1710b_1216(adi)
            BTE: BTH_I0861
            BPE: BP0190
            BPA: BPP0765
            BBR: BB0850
            MPT: Mpe_A1925
            MMS: mma_1191
            NET: Neut_2188
            NMU: Nmul_A1040
            EBA: ebA4413
            DAR: Daro_0578
            TBD: Tbd_2106
            HPY: HP0422(speA)
            HPJ: jhp0962(speA)
            HPA: HPAG1_0972
            HHE: HH1233(speA)
            HAC: Hac_0610(speA)
            WSU: WS0554(speA)
            TDN: Tmden_1132
            CJE: Cj0764c(speA)
            CJR: CJE0855(speA)
            CJJ: CJJ81176_0785(speA)
            CJU: C8J_0715(speA)
            CJD: JJD26997_1248(speA)
            CFF: CFF8240_0895(speA)
            CHA: CHAB381_0926(speA)
            CCO: CCC13826_1273(speA)
            ABU: Abu_0964(speA)
            NIS: NIS_0817(speA)
            SUN: SUN_1360(speA)
            GSU: GSU2537(speA)
            GME: Gmet_0904
            PCA: Pcar_2097
            DVU: DVU0417(speA)
            DDE: Dde_0571
            BBA: Bd0364(speA)
            ADE: Adeh_1896
            MXA: MXAN_2742(speA)
            SAT: SYN_01577
            SFU: Sfum_1025
            SME: SMa0680 SMa0682
            BJA: bll3177 blr3474
            RPA: RPA2051
            SIL: SPO0602(speA)
            GBE: GbCGDNIH1_0522
            MGM: Mmc1_0721
            ABA: Acid345_1944
            SUS: Acid_7696
            BSU: BG10212(speA)
            BCE: BC3962
            BCZ: BCZK3722(cad)
            BLI: BL01634(speA)
            BLD: BLi01681(speA)
            BCL: ABC2407(speA)
            CDF: CD0888(speA) CD3551(speA)
            CBO: CBO3116(speA)
            CKL: CKL_3181(speA1) CKL_3796(speA2)
            CHY: CHY_1622
            DRM: Dred_0487
            SWO: Swol_0667
            MTU: Rv2531c
            MTC: MT2607
            MBO: Mb2560c
            MLE: ML0524(adi)
            MPA: MAP1100(adi)
            MSM: MSMEG_0266
            RBA: RB3708(speA)
            SYN: slr0662(speA) slr1312(speA)
            SYW: SYNW2359
            SYC: syc0510_c
            SYF: Synpcc7942_1037
            SYD: Syncc9605_1621 Syncc9605_2513
            SYE: Syncc9902_1380 Syncc9902_2172
            SYG: sync_2742(speA)
            SYR: SynRCC307_2378(speA)
            SYX: SynWH7803_2389(speA)
            CYA: CYA_0128(speA)
            CYB: CYB_2779(speA)
            TEL: tll1807(speA)
            GVI: gll4070(speA)
            ANA: all3401(speA)
            AVA: Ava_2157 Ava_3423
            PMA: Pro0049(speA)
            PMM: PMM0045
            PMT: PMT2150
            PMN: PMN2A_1378
            PMI: PMT9312_0046 PMT9312_1095
            PMB: A9601_00461(speA)
            PMC: P9515_00521(speA)
            PMF: P9303_28311(speA)
            PMG: P9301_00481(speA)
            PMH: P9215_00551(speA)
            PME: NATL1_00591(speA)
            TER: Tery_1142
            BTH: BT_3394
            BFR: BF0239
            BFS: BF0196
            CHU: CHU_1576(speA)
            GFO: GFO_3625(speA)
            FPS: FP1708(speA)
            CTE: CT0562
            CCH: Cag_0433 Cag_1160
            CPH: Cpha266_0813 Cpha266_1029
            PVI: Cvib_1209
            PLT: Plut_0567
            DRA: DR_0243
            DGE: Dgeo_1771
            TTH: TTC1277
            TTJ: TTHA1640
            MJA: MJ0316
            MMP: MMP1582(pdaD)
            MMQ: MmarC5_1827
            MMZ: MmarC7_0829
            MAE: Maeo_0604
            MVN: Mevan_0894
            MAC: MA3012 MA3496
            MBA: Mbar_A2039 Mbar_A2492
            MMA: MM_0286 MM_2595
            MBU: Mbur_1870
            MHU: Mhun_0113
            MEM: Memar_2150
            MBN: Mboo_1176
            MTH: MTH870
            MST: Msp_1327(pdaD)
            MSI: Msm_0878
            MKA: MK0740
            AFU: AF2301 AF2431
            HAL: VNG1999H
            HMA: rrnAC3199(argDC)
            HWA: HQ3114A(pdaD)
            NPH: NP4484A
            TAC: Ta0778
            TVO: TVN0762
            PTO: PTO1192
            PHO: PH1609
            PAB: PAB0382
            PFU: PF1623
            TKO: TK0149
            RCI: RRC25(speA)
STRUCTURES  PDB: 1MT1  1N13  1N2M  2NV9  2NVA  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.19
            ExPASy - ENZYME nomenclature database: 4.1.1.19
            ExplorEnz - The Enzyme Database: 4.1.1.19
            ERGO genome analysis and discovery system: 4.1.1.19
            BRENDA, the Enzyme Database: 4.1.1.19
            CAS: 9024-77-5
///
ENTRY       EC 4.1.1.20                 Enzyme
NAME        diaminopimelate decarboxylase;
            diaminopimelic acid decarboxylase;
            meso-diaminopimelate decarboxylase;
            DAP-decarboxylase;
            meso-2,6-diaminoheptanedioate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     meso-2,6-diaminoheptanedioate carboxy-lyase (L-lysine-forming)
REACTION    meso-2,6-diaminoheptanedioate = L-lysine + CO2 [RN:R00451]
ALL_REAC    R00451
SUBSTRATE   meso-2,6-diaminoheptanedioate [CPD:C00680]
PRODUCT     L-lysine [CPD:C00047];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:14378182]
  AUTHORS   DENMAN RF, HOARE DS, WORK E.
  TITLE     Diaminopimelic acid decarboxylase in pyridoxin-deficient Escherichia
            coli.
  JOURNAL   Biochim. Biophys. Acta. 16 (1955) 442-3.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K01586  diaminopimelate decarboxylase
GENES       ATH: AT3G14390 AT5G11880
            OSA: 4329234
            CME: CMI221C
            TET: TTHERM_01079150
            ECO: b2838(lysA)
            ECJ: JW2806(lysA)
            ECE: Z4156(lysA)
            ECS: ECs3695
            ECC: c3435(lysA)
            ECI: UTI89_C3242(lysA)
            ECP: ECP_2851
            ECV: APECO1_3668(lysA)
            ECW: EcE24377A_3158(lysA)
            ECX: EcHS_A2985(lysA)
            STY: STY2590 STY3157(lysA)
            STT: t0504 t2923(lysA)
            SPT: SPA0504 SPA2880(lysA)
            SEC: SC2362(dcdA) SC2952(lysA)
            STM: STM2360 STM3013(lysA)
            YPE: YPO0796(lysA)
            YPK: y3184(lysA)
            YPM: YP_2861(lysA)
            YPA: YPA_0473
            YPN: YPN_3000
            YPP: YPDSF_1713
            YPS: YPTB1889(lysA) YPTB3045(lysA)
            YPI: YpsIP31758_0973(lysA)
            SFL: SF2848(lysA)
            SFX: S3046(lysA)
            SFV: SFV_2916(lysA)
            SSN: SSON_2998(lysA)
            SBO: SBO_2730(lysA)
            SDY: SDY_3055(lysA)
            ECA: ECA3652(lysA)
            PLU: plu1191(lysA)
            BUC: BU438(lysA)
            BAS: BUsg423(lysA)
            BAB: bbp388(lysA)
            BCC: BCc_271(lysA)
            SGL: SG1988 SGP1_0043
            ENT: Ent638_3284
            BFL: Bfl263(lysA)
            BPN: BPEN_271(lysA)
            HIN: HI0727(lysA)
            HIT: NTHI0884(lysA)
            HDU: HD0036(lysA)
            HSO: HS_1713(lysA)
            PMU: PM1424(lysA)
            MSU: MS2084(lysA)
            APL: APL_1525(lysA)
            XFA: XF1116
            XFT: PD0408(lysC)
            XCC: XCC2741(lysA) XCC3055(lysA)
            XCB: XC_1103 XC_1372
            XCV: XCV3056(lysA) XCV3311
            XAC: XAC2911(lysA) XAC3181(lysA)
            XOO: XOO1354(lysA) XOO1433(lysA)
            XOM: XOO_1244(XOO1244) XOO_1317(XOO1317)
            VCH: VC0125
            VCO: VC0395_A2394(lysA)
            VVU: VV1_1126
            VVY: VV0086
            VPA: VP2984 VPA1662
            VFI: VF2485
            PPR: PBPRA3523
            PAE: PA5277(lysA)
            PAU: PA14_69670(lysA)
            PAP: PSPA7_6020(lysA)
            PPU: PP_2077(lysA-1) PP_5227(lysA-2)
            PST: PSPTO_0209(lsyA-1) PSPTO_0225(lsyA-2)
            PSB: Psyr_0182 Psyr_2585
            PSP: PSPPH_2752 PSPPH_5008(lysA)
            PFL: PFL_2318(lysA) PFL_6012(lysA)
            PFO: Pfl_5498
            PEN: PSEEN3604(lysA-1) PSEEN5365(lysA-2)
            PAR: Psyc_0199(lysA)
            PCR: Pcryo_0219 Pcryo_1275
            ACI: ACIAD2660(lysA)
            ACB: A1S_2632
            SON: SO_4309(lysA)
            SDN: Sden_0390 Sden_0584 Sden_3075
            SFR: Sfri_0444 Sfri_3405
            SAZ: Sama_3250
            SBL: Sbal_3854 Sbal_3996
            SBM: Shew185_0465
            SLO: Shew_0322
            SPC: Sputcn32_0541
            SHE: Shewmr4_0391 Shewmr4_3507
            SHM: Shewmr7_0445 Shewmr7_3634
            SHN: Shewana3_0390 Shewana3_3682
            SHW: Sputw3181_3631 Sputw3181_3722
            ILO: IL2556(lysA)
            CPS: CPS_1240(lysA) CPS_2875 CPS_4492
            PHA: PSHAa0093(lysA) PSHAa0178(dcdA)
            PAT: Patl_4073
            SDE: Sde_0238
            PIN: Ping_0041
            MAQ: Maqu_0494
            LPN: lpg1811(lysC)
            LPF: lpl1775(lysAC)
            LPP: lpp1774(lysAC)
            MCA: MCA0858(lysA)
            FTU: FTT0027c(lysA)
            FTF: FTF0027c(lysA1)
            FTW: FTW_0770(lysA)
            FTL: FTL_0272 FTL_1834
            FTH: FTH_0271(lysA1) FTH_1770(lysA2)
            FTA: FTA_0289(lysA)
            FTN: FTN_1530(lysA) FTN_1684 FTN_1726
            TCX: Tcr_1847
            NOC: Noc_0314 Noc_1957
            AEH: Mlg_0126 Mlg_0209
            HHA: Hhal_1199
            HCH: HCH_00297(lysA)
            CSA: Csal_3112
            ABO: ABO_2328(lysA)
            AHA: AHA_0473(lysA)
            CRP: CRP_177
            RMA: Rmag_0103
            VOK: COSY_0106(lysA)
            NME: NMB1976
            NMA: NMA0468(lysA)
            NMC: NMC1952(lysA)
            NGO: NGO2098
            CVI: CV_3757(lysA)
            RSO: RS00881(RSp0424) RSc2979(lysA)
            REU: Reut_A3139
            REH: H16_A3443(lysA2)
            RME: Rmet_1110 Rmet_3276
            BMA: BMA2756(lysA) BMA3159 BMAA1455
            BMV: BMASAVP1_A3197(lysA)
            BML: BMA10299_A1897(lysA)
            BMN: BMA10247_3451(lysA)
            BXE: Bxe_A0351 Bxe_C0421
            BUR: Bcep18194_B0837 Bcep18194_C7422
            BCN: Bcen_3483
            BCH: Bcen2424_4883
            BAM: Bamb_4246
            BPS: BPSL0486 BPSL3176(lysA) BPSS0303
            BPM: BURPS1710b_0709(lysA) BURPS1710b_3737(lysA) BURPS1710b_A1853
            BPL: BURPS1106A_3766(lysA)
            BPD: BURPS668_3708(lysA)
            BTE: BTH_I3031(lysA)
            PNU: Pnuc_0086
            BPE: BP3653(lysA)
            BPA: BPP0068(lysA)
            BBR: BB0068(lysA)
            RFR: Rfer_2916
            POL: Bpro_0777 Bpro_4782
            PNA: Pnap_0669
            AAV: Aave_0992
            AJS: Ajs_0716
            VEI: Veis_4766
            MPT: Mpe_A3116
            HAR: HEAR3129(lysA)
            MMS: mma_3371(lysA)
            NEU: NE1126 NE1957
            NET: Neut_0404 Neut_1742
            NMU: Nmul_A0541 Nmul_A2669
            EBA: ebA2271(lysA)
            AZO: azo3248(lysA1) azo3654(lysA2)
            DAR: Daro_0207 Daro_1645
            TBD: Tbd_0226 Tbd_0717
            MFA: Mfla_2443
            HPY: HP0290(lysA)
            HPJ: jhp0275(lysA)
            HPA: HPAG1_0292
            HHE: HH1507(lysA)
            HAC: Hac_0550(lysA)
            WSU: WS0333(lysA)
            TDN: Tmden_0468
            CJE: Cj0314(lysA)
            CJR: CJE0359(lysA)
            CJJ: CJJ81176_0336(lysA)
            CJU: C8J_0291(lysA)
            CJD: JJD26997_1651(lysA)
            CFF: CFF8240_0271(lysA)
            CCV: CCV52592_1665(lysA)
            CHA: CHAB381_1301(lysA)
            CCO: CCC13826_0508(lysA) CCC13826_1588(lysA)
            ABU: Abu_2136(lysA)
            NIS: NIS_0387 NIS_0498
            SUN: SUN_2058(lysA)
            GSU: GSU0158(lysA)
            GME: Gmet_0219
            PCA: Pcar_2420
            PPD: Ppro_1995
            DVU: DVU1647(lysA-1) DVU2566(lysA-2)
            DVL: Dvul_1439
            DDE: Dde_1978 Dde_2664
            LIP: LI0553(lysA)
            BBA: Bd1777(lysA)
            DPS: DP2960
            ADE: Adeh_4070
            MXA: MXAN_2358 MXAN_5929(lysA)
            SAT: SYN_02160
            SFU: Sfum_0058
            ERU: Erum5340(lysA)
            ERW: ERWE_CDS_05600(lysA)
            ERG: ERGA_CDS_05490(lysA)
            ECN: Ecaj_0541
            ECH: ECH_0485(lysA)
            PUB: SAR11_0413(lysA)
            MLO: mlr3508
            MES: Meso_3040
            SME: SMc00723(lysA)
            ATU: Atu3601(lysA)
            ATC: AGR_L_2454
            RET: RHE_CH03797(lysA)
            RLE: RL4325(lysA)
            BME: BMEI0084
            BMF: BAB1_1984(lysA)
            BMS: BR1983(lysA)
            BMB: BruAb1_1959(lysA)
            BOV: BOV_1908(lysA)
            BJA: blr1383(lysA)
            BRA: BRADO6485(lysA)
            BBT: BBta_0632 BBta_1147(lysA)
            RPA: RPA4741(lysA)
            RPB: RPB_0829
            RPC: RPC_4873
            RPD: RPD_0938
            RPE: RPE_4840
            NWI: Nwi_0713
            NHA: Nham_3475
            BHE: BH16170(lysA)
            BQU: BQ13070(lysA)
            BBK: BARBAKC583_0056(lysA)
            CCR: CC_2213
            SIL: SPO0334(lysA)
            SIT: TM1040_3495
            RSP: RSP_0729(lysA)
            JAN: Jann_0481
            RDE: RD1_1595(lysA)
            PDE: Pden_2020
            MMR: Mmar10_0407
            HNE: HNE_3463(lysA)
            ZMO: ZMO1768(lysA)
            GOX: GOX1944
            GBE: GbCGDNIH1_0129
            RRU: Rru_A0396 Rru_A3135
            MAG: amb4491
            MGM: Mmc1_3740
            ABA: Acid345_3440
            SUS: Acid_2187
            BSU: BG10510(lysA)
            BHA: BH1544
            BAN: BA1438(lysA)
            BAR: GBAA1438(lysA)
            BAA: BA_1959
            BAT: BAS1329
            BCE: BC1419
            BCA: BCE_1542(lysA)
            BCZ: BCZK1303(lysA)
            BTK: BT9727_1302(lysA)
            BLI: BL03275(lysA)
            BLD: BLi02486(lysA)
            BCL: ABC1801(lysA)
            BAY: RBAM_021480(lysA)
            BPU: BPUM_2068(lysA)
            OIH: OB1833(lysA)
            GKA: GK2300
            SAU: SA0119 SA1232(lysA)
            SAV: SAV0123 SAV1400(lysA)
            SAM: MW0096 MW1288(lysA)
            SAR: SAR0126 SAR1412(lysA)
            SAS: SAS0097 SAS1341
            SAC: SACOL0107 SACOL1435(lysA)
            SAB: SAB0062 SAB1255(lysA)
            SAA: SAUSA300_0125 SAUSA300_1293(lysA)
            SAO: SAOUHSC_00082 SAOUHSC_01401
            SEP: SE1080
            SER: SERP0970(lysA)
            SHA: SH1511(lysA)
            SSP: SSP1350
            LMO: lmo1952(lysA)
            LMF: LMOf2365_1982(lysA)
            LIN: lin2066(lysA)
            LWE: lwe1978(lysA)
            LLA: L0121(lysA)
            LLC: LACR_1405
            LLM: llmg_1185(lysA)
            SPN: SP_1978
            SPR: spr1792(lysA)
            SPD: SPD_1775(lysA)
            SMU: SMU.1721c
            STC: str0252(lysA)
            STL: stu0252(lysA)
            SSA: SSA_1787(lysA)
            SGO: SGO_1678(lysA)
            LPL: lp_1713(lysA)
            LAC: LBA0851(lysA)
            LSL: LSL_1004(lysA)
            LBU: LBUL_1181
            LCA: LSEI_0098
            EFA: EF1504(lysA)
            OOE: OEOE_0771
            STH: STH1810
            CAC: CAC0608(lisA)
            CPE: CPE0595(lysA)
            CPF: CPF_0576(lysA)
            CPR: CPR_0562(lysA)
            CTC: CTC02456
            CNO: NT01CX_1352(lysA) NT01CX_2116(lysA)
            CDF: CD2053(lysA)
            CBO: CBO3336(lysA)
            CBA: CLB_3394(lysA)
            CBH: CLC_3281(lysA)
            CBF: CLI_3509(lysA)
            CKL: CKL_0608(lysA)
            CHY: CHY_1951(lysA)
            DSY: DSY4977
            SWO: Swol_1422
            TTE: TTE0210(lysA) TTE1981(lysA2)
            MTA: Moth_1364
            MTU: Rv1293(lysA)
            MTC: MT1332(lysA)
            MBO: Mb1325(lysA)
            MBB: BCG_1353(lysA)
            MLE: ML1128(lysA)
            MPA: MAP0986c(lysA_1) MAP2469c(lysA_2)
            MAV: MAV_1160(lysA) MAV_1508(lysA)
            MSM: MSMEG_4958(lysA) MSMEG_6197
            MMC: Mmcs_3897
            CGL: NCgl1133(cgl1180) NCgl2054(cgl2135)
            CGB: cg1334(lysA)
            CEF: CE1277 CE1419
            CDI: DIP1035(lysA)
            CJK: jk1353(lysA)
            NFA: nfa10480(lysA)
            RHA: RHA1_ro01489
            SCO: SCO5353(lysA) SCO6438(SC9B5.05)
            SMA: SAV2919(lysA1) SAV7323 SAV916(lysA2)
            LXX: Lxx06860(lysA)
            AAU: AAur_2613(lysA)
            PAC: PPA1259
            TFU: Tfu_2425
            FRA: Francci3_3726 Francci3_4053
            FAL: FRAAL5952(lysA) FRAAL6420
            ACE: Acel_0629
            SEN: SACE_2107 SACE_6299(lysA)
            BLO: BL1273(lysA)
            BAD: BAD_1417(lysA)
            RXY: Rxyl_0075
            RBA: RB1538(lysA) RB4382 RB9188(lysA)
            LIL: LA1047(lysA)
            LIC: LIC12618(lysA)
            LBJ: LBJ_0281(lysA)
            LBL: LBL_2795(lysA)
            SYN: sll0504(lysA)
            SYW: SYNW0936(lysA)
            SYC: syc1251_c(lysA)
            SYF: Synpcc7942_0262
            SYD: Syncc9605_1629
            SYE: Syncc9902_1391
            SYG: sync_1029(lysA)
            SYR: SynRCC307_0790(lysA)
            SYX: SynWH7803_1533(lysA)
            CYA: CYA_2895(lysA)
            CYB: CYB_1644(lysA)
            TEL: tlr1761(lysA)
            GVI: gll0110(lysA)
            ANA: all2997
            AVA: Ava_0912
            PMA: Pro1105(lysA)
            PMM: PMM1090(lysA)
            PMT: PMT1059(lysA)
            PMN: PMN2A_0658
            PMI: PMT9312_1101
            PMB: A9601_11961(lysA)
            PMC: P9515_11811(lysA)
            PMF: P9303_09931(lysA)
            PMG: P9301_11971(lysA)
            PMH: P9215_12261(lysA)
            PME: NATL1_14901(lysA)
            TER: Tery_2435
            BTH: BT_1374
            BFR: BF3049
            BFS: BF2885
            PGI: PG2188(lysA)
            SRU: SRU_0301
            CHU: CHU_3289(lysA)
            GFO: GFO_0749(lysA)
            CTE: CT1371(lysA)
            CCH: Cag_1109
            PLT: Plut_1348
            DET: DET0534(lysA)
            DEH: cbdb_A508(lysA)
            DRA: DR_1758
            DGE: Dgeo_0790
            AAE: aq_1208(lysA)
            TMA: TM1517
            MMP: MMP1200(lysA)
            MAC: MA0726(lysA)
            MBA: Mbar_A1641
            MMA: MM_1885
            MBU: Mbur_0628
            MHU: Mhun_2942
            MST: Msp_1578(lysA)
            MSI: Msm_1371
            MKA: MK0483(lysA)
            HMA: rrnAC0198(odc)
            HWA: HQ1510A(lysA)
            NPH: NP1646A(lysA)
            TAC: Ta0788m
            TVO: TVN0806
            PTO: PTO0016
            RCI: RCIX1963(lysA)
STRUCTURES  PDB: 1HKV  1HKW  1KNW  1KO0  1TUF  1TWI  2O0T  2P3E  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.20
            ExPASy - ENZYME nomenclature database: 4.1.1.20
            ExplorEnz - The Enzyme Database: 4.1.1.20
            ERGO genome analysis and discovery system: 4.1.1.20
            BRENDA, the Enzyme Database: 4.1.1.20
            CAS: 9024-75-3
///
ENTRY       EC 4.1.1.21                 Enzyme
NAME        phosphoribosylaminoimidazole carboxylase;
            5-phosphoribosyl-5-aminoimidazole carboxylase;
            5-amino-1-ribosylimidazole 5-phosphate carboxylase;
            AIR carboxylase;
            1-(5-phosphoribosyl)-5-amino-4-imidazolecarboxylate carboxy-lyase;
            ADE2;
            class II PurE;
            5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase
            [5-amino-1-(5-phospho-D-ribosyl)imidazole-forming]
REACTION    5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate =
            5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2 [RN:R04209]
ALL_REAC    R04209
SUBSTRATE   5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate [CPD:C04751]
PRODUCT     5-amino-1-(5-phospho-D-ribosyl)imidazole [CPD:C03373];
            CO2 [CPD:C00011]
COMMENT     While this is the reaction that occurs in vertebrates during purine
            biosynthesis, two enzymes are required to carry out the same
            reaction in Escherichia coli, namely EC 6.3.4.18,
            5-(carboxyamino)imidazole ribonucleotide synthase and EC 5.4.99.18,
            5-(carboxyamino)imidazole ribonucleotide mutase [3].
            5-Carboxyamino-1-(5-phospho-D-ribosyl)imidazole is not a substrate.
REFERENCE   1  [PMID:13672967]
  AUTHORS   LUKENS LN, BUCHANAN JM.
  TITLE     Biosynthesis of the purines. XXIV. The enzymatic synthesis of
            5-amino-1-ribosyl-4-imidazolecarboxylic acid 5'-phosphate from
            5-amino-1-ribosylimidazole 5'-phosphate and carbon dioxide.
  JOURNAL   J. Biol. Chem. 234 (1959) 1799-805.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:7918411]
  AUTHORS   Firestine SM, Poon SW, Mueller EJ, Stubbe J, Davisson VJ.
  TITLE     Reactions catalyzed by 5-aminoimidazole ribonucleotide carboxylases
            from Escherichia coli and Gallus gallus: a case for divergent
            catalytic mechanisms.
  JOURNAL   Biochemistry. 33 (1994) 11927-34.
  ORGANISM  Escherichia coli [GN:eco], chicken [GN:gga]
REFERENCE   3  [PMID:9500840]
  AUTHORS   Firestine SM, Misialek S, Toffaletti DL, Klem TJ, Perfect JR,
            Davisson VJ.
  TITLE     Biochemical role of the Cryptococcus neoformans ADE2 protein in
            fungal de novo purine biosynthesis.
  JOURNAL   Arch. Biochem. Biophys. 351 (1998) 123-34.
  ORGANISM  Escherichia coli [GN:eco], chicken [GN:gga], Cryptococcus neoformans
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01587  phosphoribosylaminoimidazole carboxylase
            KO: K01588  phosphoribosylaminoimidazole carboxylase catalytic
                        subunit
            KO: K01589  phosphoribosylaminoimidazole carboxylase ATPase subunit
GENES       HSA: 10606(PAICS)
            MMU: 67054(Paics)
            RNO: 140946(Paics)
            BTA: 404170(PAICS)
            GGA: 396534(PAICS)
            XLA: 379855(paics) 444677(MGC84289)
            DRE: 321193(paics)
            SPU: 575874(LOC575874)
            DME: Dmel_CG3989
            CEL: B0286.3
            ATH: AT2G05140 AT2G37690
            OSA: 4327345
            SCE: YOR128C(ADE2)
            AGO: AGOS_ACR210C
            PIC: PICST_81265(ADE2)
            CAL: CaO19_5906(CaO19.5906)
            CGR: CAGL0K10340g(PUR6_CANGA)
            SPO: SPCC1322.13(ade6)
            ANI: AN3626.2
            AFM: AFUA_4G12600
            AOR: AO090009000333
            CNE: CNE02500
            UMA: UM00993.1
            DDI: DDB_0230088(purC)
            ECO: b0522(purK) b0523(purE)
            ECJ: JW0511(purK) JW0512(purE)
            ECE: Z0677(purK) Z0678(purE)
            ECS: ECs0584 ECs0585
            ECC: c0636(purK) c0637(purE)
            ECI: UTI89_C0550(purK) UTI89_C0551(purE)
            ECP: ECP_0582 ECP_0583
            ECV: APECO1_1492(purE) APECO1_1493(purK)
            ECW: EcE24377A_0560(purK) EcE24377A_0562(purE)
            ECX: EcHS_A0597 EcHS_A0598
            STY: STY0581(purK) STY0582(purE)
            STT: t2327(purE) t2328(purK)
            SPT: SPA2189(purE) SPA2190(purK)
            SEC: SC0572(purK) SC0573(purE)
            STM: STM0533(purK) STM0534(purE)
            YPE: YPO3076(purE) YPO3077(purK)
            YPK: y1102(purK) y1103(purE)
            YPM: YP_0847(purK) YP_0848(purE)
            YPA: YPA_2571 YPA_2572
            YPN: YPN_1013 YPN_1014
            YPP: YPDSF_1348 YPDSF_2714 YPDSF_2715
            YPS: YPTB1031(purK) YPTB1032(purE)
            YPI: YpsIP31758_3017(purE) YpsIP31758_3018(purK)
            SFL: SF0453(purK) SF0454(purE)
            SFX: S0461(purK) S0462(purE)
            SFV: SFV_0480(purK) SFV_0481(purE)
            SSN: SSON_0495(purE) SSON_0496(purK)
            SBO: SBO_0420(purE) SBO_0421(purK)
            SDY: SDY_0274(purK) SDY_0275(purE)
            ECA: ECA3156(purE) ECA3157(purK)
            PLU: plu3807(purE) plu3808(purK)
            WBR: WGLp245(purE) WGLp246(purK)
            SGL: SG0701 SG0702
            ENT: Ent638_0976 Ent638_0977 Ent638_2418
            SPE: Spro_1163 Spro_2805
            HIN: HI1615(purE) HI1616(purK)
            HIT: NTHI1424(purK) NTHI1425(purE)
            HIP: CGSHiEE_05745
            HIQ: CGSHiGG_10050
            HDU: HD1421 HD1423 HD1424(purE)
            HSO: HS_0672(purE) HS_0839(purK)
            PMU: PM0619(purE) PM0620(purK)
            MSU: MS1032(purK) MS1033(purE)
            APL: APL_0659(purE) APL_0661(purK)
            ASU: Asuc_0686 Asuc_1572
            XFA: XF2671 XF2672
            XFT: PD2035(purK) PD2036(purE)
            XCC: XCC2502 XCC2503(purE)
            XCB: XC_1613 XC_1614
            XCV: XCV2828(purK) XCV2829(purE)
            XAC: XAC2678(purK) XAC2679(purE)
            XOO: XOO3209(purK) XOO3210(purE)
            XOM: XOO_3042(XOO3042) XOO_3043(XOO3043)
            VCH: VC0051 VC0052
            VCO: VC0395_A2467(purE) VC0395_A2468(purK)
            VVU: VV1_1053 VV1_1054
            VVY: VV3218 VV3219
            VPA: VP3036 VP3037
            VFI: VF1342 VF2537 VF2538
            PPR: PBPRA3574(purK)
            PAE: PA5425(purK) PA5426(purE)
            PAU: PA14_71600(purK) PA14_71620(purE)
            PPU: PP_5335(purK) PP_5336(purE)
            PPF: Pput_5243 Pput_5244
            PST: PSPTO_5493(purK) PSPTO_5494(purE)
            PSB: Psyr_5047 Psyr_5048
            PSP: PSPPH_5129(purK) PSPPH_5130(purE)
            PFL: PFL_6125(purK) PFL_6126(purE)
            PFO: Pfl_1014 Pfl_3841 Pfl_5621 Pfl_5622
            PEN: PSEEN5479(purK) PSEEN5480(purE)
            PMY: Pmen_0118 Pmen_0119
            PAR: Psyc_0275(purK) Psyc_0276(purE)
            PCR: Pcryo_0302 Pcryo_0303
            PRW: PsycPRwf_2204 PsycPRwf_2205
            ACI: ACIAD3658(purK) ACIAD3659(purE)
            SON: SO_3554(purE) SO_3555(purK)
            SDN: Sden_1223 Sden_1224
            SFR: Sfri_1075 Sfri_1076
            SAZ: Sama_1063 Sama_1064 Sama_2807
            SBL: Sbal_0989 Sbal_1035 Sbal_1036
            SBM: Shew185_1059 Shew185_1103
            SLO: Shew_1230 Shew_1248 Shew_1249
            SPC: Sputcn32_1001 Sputcn32_1040 Sputcn32_1041
            SSE: Ssed_0973 Ssed_1333
            SPL: Spea_0871 Spea_1211
            SHE: Shewmr4_2975 Shewmr4_2976
            SHM: Shewmr7_3057 Shewmr7_3058
            SHN: Shewana3_3155 Shewana3_3156
            SHW: Sputw3181_3124 Sputw3181_3125 Sputw3181_3164
            ILO: IL0035(purE) IL0036(purK)
            CPS: CPS_0025(purK) CPS_0026(purE)
            PHA: PSHAa1572(purK) PSHAa1573(purE)
            PAT: Patl_4224 Patl_4225
            SDE: Sde_2802 Sde_2803
            PIN: Ping_0073 Ping_2048 Ping_2049
            MAQ: Maqu_2021 Maqu_2478
            CBU: CBU_2002(purE)
            CBD: COXBU7E912_2102(purE)
            LPN: lpg0217(purK) lpg0218(purE)
            LPF: lpl0271(purK) lpl0272(purE)
            LPP: lpp0276(purK) lpp0277(purE)
            MCA: MCA2529(purK) MCA2530(purE)
            FTU: FTT0896(purE) FTT0897(purK)
            FTF: FTF0896(purE) FTF0897(purK)
            FTW: FTW_1282(purK) FTW_1283(purE)
            FTL: FTL_0398 FTL_0399
            FTH: FTH_0390(purE) FTH_0391(purK)
            FTA: FTA_0421(purE) FTA_0422(purK)
            FTN: FTN_0422(purE) FTN_0423(purK)
            TCX: Tcr_1818 Tcr_1819
            NOC: Noc_3009
            AEH: Mlg_2236 Mlg_2237
            HHA: Hhal_2070 Hhal_2071
            HCH: HCH_04603(purE) HCH_04604(purK)
            CSA: Csal_2897 Csal_2898
            ABO: ABO_0171(purE) ABO_0172(purK)
            MMW: Mmwyl1_1076
            AHA: AHA_0069(purK) AHA_0070(purE-1) AHA_0263(purE-2)
            DNO: DNO_0077(purE) DNO_0078(purK)
            BCI: BCI_0119(purK) BCI_0120(purE)
            RMA: Rmag_0837 Rmag_0838
            VOK: COSY_0762(purE) COSY_0763(purK)
            NME: NMB1019 NMB1439
            NMA: NMA1245(purK) NMA1651(purE)
            NMC: NMC1011(purK) NMC1374(purE)
            NGO: NGO0748 NGO0875(purK)
            CVI: CV_0161(purE) CV_0162(purK)
            RSO: RSc0575(purE) RSc0576(purK)
            REU: Reut_A0554 Reut_A0555
            REH: H16_A0570(purE) H16_A0571(purK)
            RME: Rmet_0505 Rmet_0506
            BMA: BMA0301(purE) BMA0302(purK)
            BMV: BMASAVP1_A0596(purE) BMASAVP1_A0597(purK)
            BML: BMA10299_A2430(purE) BMA10299_A2431(purK)
            BMN: BMA10247_0042(purE) BMA10247_0043(purK)
            BXE: Bxe_A0693 Bxe_A0694
            BVI: Bcep1808_2738 Bcep1808_2739
            BUR: Bcep18194_A5661 Bcep18194_A5954 Bcep18194_A5955
            BCN: Bcen_2012 Bcen_2013
            BCH: Bcen2424_2623 Bcen2424_2624
            BAM: Bamb_2670 Bamb_2671
            BPS: BPSL0800(purE) BPSL0801(purK)
            BPM: BURPS1710b_1000(purE) BURPS1710b_1001(purK)
            BPL: BURPS1106A_0843(purE) BURPS1106A_0844(purK)
            BPD: BURPS668_0838(purE) BURPS668_0839(purK)
            BTE: BTH_I0667 BTH_I0668(purK)
            PNU: Pnuc_1812 Pnuc_1813
            BPE: BP1526(purE) BP1527(purK)
            BPA: BPP1198(purE) BPP1199(purK)
            BBR: BB1415(purE) BB1416(purK)
            RFR: Rfer_0196 Rfer_0197
            POL: Bpro_4626 Bpro_4627
            PNA: Pnap_3571 Pnap_3862 Pnap_3863
            AAV: Aave_4258 Aave_4562 Aave_4563
            AJS: Ajs_3934 Ajs_3935
            VEI: Veis_1545 Veis_1546
            MPT: Mpe_A0295 Mpe_A0296
            HAR: HEAR1388(purT) HEAR2606(purK) HEAR2607(purE)
            MMS: mma_2843 mma_2844
            NEU: NE0867(purK) NE0868(purE)
            NET: Neut_1201 Neut_1202
            NMU: Nmul_A0610 Nmul_A0611
            EBA: ebA114(purK) ebA116(purE)
            AZO: azo1378(purE) azo1379(purK)
            DAR: Daro_0449 Daro_0451
            TBD: Tbd_2661 Tbd_2662
            MFA: Mfla_2214 Mfla_2215
            HHE: HH0528(purE)
            WSU: WS2121(purE)
            TDN: Tmden_1863
            CJE: Cj0702(purE)
            CJR: CJE0802(purE)
            CJJ: CJJ81176_0725(purE)
            CJU: C8J_0669(purE)
            CJD: JJD26997_1304(purE)
            CFF: CFF8240_1049(purE)
            CCV: CCV52592_0281(purE)
            CHA: CHAB381_1500(purE)
            CCO: CCC13826_1228
            ABU: Abu_1981(purE) Abu_2168
            NIS: NIS_1514(purE)
            SUN: SUN_0356(purE)
            GSU: GSU0611(purE-1)
            GME: Gmet_2903
            GUR: Gura_3844
            PCA: Pcar_1033 Pcar_2230
            PPD: Ppro_2589
            DVU: DVU0487(purE)
            DVL: Dvul_2454
            DDE: Dde_3459
            LIP: LI0922(purK)
            BBA: Bd3008(purE)
            ADE: Adeh_2466
            AFW: Anae109_1401
            MXA: MXAN_2534(purK) MXAN_2535(purE)
            SAT: SYN_00474 SYN_01067 SYN_02442
            SFU: Sfum_2758
            WOL: WD1142(purK) WD1305(purE)
            WBM: Wbm0041 Wbm0397(purE)
            AMA: AM001(purE) AM1036(purK)
            APH: APH_1119(purK) APH_1279(purE)
            ERU: Erum1060(purE) Erum7940(purK)
            ERW: ERWE_CDS_01030(purE) ERWE_CDS_08400(purK)
            ERG: ERGA_CDS_00990(purE) ERGA_CDS_08290(purK)
            ECN: Ecaj_0105 Ecaj_0830
            ECH: ECH_0160(purE) ECH_1034(purK)
            NSE: NSE_0235(purE) NSE_0965(purK)
            PUB: SAR11_1271 SAR11_1272(purE)
            MLO: mlr3809 mlr3811
            MES: Meso_3411 Meso_3412
            PLA: Plav_2071 Plav_2072 Plav_2474
            SME: SMc04001(purE) SMc04002(purK)
            SMD: Smed_2672 Smed_2673
            ATU: Atu3754(purE) Atu3755(purK)
            ATC: AGR_L_2157(airC) AGR_L_2159(airC)
            RET: RHE_CH03531(purE) RHE_CH03532(purK)
            RLE: RL4044(purE) RL4045(purK)
            BME: BMEI0295 BMEI0296
            BMF: BAB1_1757 BAB1_1758(purK)
            BMS: BR1744(purE) BR1745(purK)
            BMB: BruAb1_1729(purE) BruAb1_1730(purK)
            BOV: BOV_1684(purE) BOV_1685(purK)
            OAN: Oant_1168 Oant_1169
            BJA: blr7114(purE) blr7115(purK)
            BRA: BRADO1205(purK) BRADO1206(purE)
            BBT: BBta_6848(purE) BBta_6849(purK)
            RPA: RPA4174(purE) RPA4175(purK)
            RPB: RPB_1446 RPB_1447
            RPC: RPC_3960 RPC_3961
            RPD: RPD_1423 RPD_1424
            RPE: RPE_4089 RPE_4090
            NWI: Nwi_1001 Nwi_1002
            NHA: Nham_1235 Nham_1236
            BHE: BH14290(purE) BH14300(purK)
            BQU: BQ11280(purE) BQ11290(purK)
            BBK: BARBAKC583_0208(purK) BARBAKC583_0209(purE)
            XAU: Xaut_1255 Xaut_1256
            CCR: CC_3283 CC_3284
            SIL: SPO0892(purK) SPO0893(purE)
            SIT: TM1040_0603 TM1040_0604
            RSP: RSP_1570(purK) RSP_1571(purE)
            RSH: Rsph17029_0221 Rsph17029_0222
            RSQ: Rsph17025_3051 Rsph17025_3052
            JAN: Jann_3352 Jann_3353
            RDE: RD1_3510(purE) RD1_3511(purK)
            PDE: Pden_2201 Pden_2202
            MMR: Mmar10_2566 Mmar10_2567
            HNE: HNE_3506(purE) HNE_3507(purK)
            ZMO: ZMO1420(purE) ZMO1421(purK)
            NAR: Saro_3263 Saro_3264
            SAL: Sala_2361 Sala_2362
            SWI: Swit_3131 Swit_3132
            ELI: ELI_13575 ELI_13580(purE)
            GOX: GOX2393 GOX2394
            GBE: GbCGDNIH1_1364 GbCGDNIH1_1365
            ACR: Acry_1609 Acry_1610
            RRU: Rru_A1050 Rru_A1051
            MAG: amb2201 amb2202
            MGM: Mmc1_3464
            ABA: Acid345_4553
            SUS: Acid_5042 Acid_5043
            BSU: BG10700(purE) BG10701(purK)
            BHA: BH0623(purE) BH0624(purK)
            BAN: BA0288(purE) BA0289(purK)
            BAR: GBAA0288(purE) GBAA0289(purK)
            BAA: BA_0860 BA_0861
            BAT: BAS0275 BAS0276
            BCE: BC0323 BC0324
            BCA: BCE_0317(purE) BCE_0318(purK)
            BCZ: BCZK0263(purE) BCZK0264(purK)
            BCY: Bcer98_0267 Bcer98_0268
            BTK: BT9727_0260(purE) BT9727_0261(purK)
            BTL: BALH_0282(purE) BALH_0283(purK)
            BLI: BL01476(purE) BL01477(purK)
            BLD: BLi00693(purE) BLi00694(purK)
            BCL: ABC1024(purE) ABC1025(purK)
            BAY: RBAM_006840 RBAM_006850
            BPU: BPUM_0596 BPUM_0597
            OIH: OB0739 OB0740
            GKA: GK0257 GK0258
            SAU: SA0916(purE) SA0917(purK)
            SAV: SAV1064 SAV1065(purK)
            SAM: MW0947 MW0948(purK)
            SAR: SAR1038(purE) SAR1039(purK)
            SAS: SAS1000 SAS1001
            SAC: SACOL1073(purE) SACOL1074(purK)
            SAB: SAB0931(purE) SAB0932(purK)
            SAA: SAUSA300_0966(purE) SAUSA300_0967(purK)
            SAO: SAOUHSC_01008 SAOUHSC_01009
            SAJ: SaurJH9_1124
            SAH: SaurJH1_1146
            SEP: SE0762 SE0763
            SER: SERP0649(purE) SERP0650(purK)
            SHA: SH1892(purK) SH1893(purE)
            SSP: SSP1725 SSP1726
            LMO: lmo1774(purK) lmo1775(purE)
            LMF: LMOf2365_1799(purK) LMOf2365_1800(purE)
            LIN: lin1886(purK) lin1887(purE)
            LWE: lwe1792(purK) lwe1793(purE)
            LLA: L151330(purK) L152487(purE)
            LLC: LACR_1598 LACR_1599
            LLM: llmg_0999(purE) llmg_1000(purK)
            SPY: SPy_0033(purE) SPy_0034(purK)
            SPZ: M5005_Spy_0030(purE) M5005_Spy_0031(purK)
            SPM: spyM18_0033(purE) spyM18_0034(purK)
            SPG: SpyM3_0027(purE) SpyM3_0028(purK)
            SPS: SPs0028 SPs0029
            SPH: MGAS10270_Spy0031(purE) MGAS10270_Spy0032(purK)
            SPI: MGAS10750_Spy0031(purE) MGAS10750_Spy0032(purK)
            SPJ: MGAS2096_Spy0031(purE) MGAS2096_Spy0032(purK)
            SPK: MGAS9429_Spy0030(purE) MGAS9429_Spy0031(purK)
            SPF: SpyM50030(purE) SpyM50031(purK)
            SPA: M6_Spy0079 M6_Spy0080
            SPB: M28_Spy0030(purE) M28_Spy0031(purK)
            SPN: SP_0053 SP_0054
            SPR: spr0053(purE) spr0054(purK)
            SPD: SPD_0059(purE) SPD_0060(purK)
            SAG: SAG0044(purE) SAG0045(purK)
            SAN: gbs0043 gbs0044
            SAK: SAK_0077(purE) SAK_0078(purK)
            SMU: SMU.50(purE) SMU.51(purK)
            STC: str0041(purE) str0042(purK)
            STL: stu0041(purE) stu0042(purK)
            SSA: SSA_0039(purE) SSA_0040(purK)
            SGO: SGO_2089(purK) SGO_2090(purE)
            LPL: lp_1141(purK2) lp_2728(purK1) lp_2729(purE)
            LAC: LBA1560(purK) LBA1561(purE)
            LSA: LSA0652(purE) LSA0653(purK1) LSA1556(purK2)
            LSL: LSL_0515(purE) LSL_0516(purK) LSL_1350(purK)
            LDB: Ldb1445(purK) Ldb1446(purE)
            LBU: LBUL_1340 LBUL_1341
            LBR: LVIS_1635
            LCA: LSEI_1119 LSEI_1755 LSEI_1756
            LRE: Lreu_0134 Lreu_1446
            EFA: EF1786(purK-1) EF1787(purE) EF2362(purK-2)
            OOE: OEOE_1137 OEOE_1138
            STH: STH1806 STH1807
            CAC: CAC1390(purE)
            CPE: CPE0681(purE)
            CPF: CPF_0672(purE)
            CPR: CPR_0670(purE)
            CTC: CTC01966
            CNO: NT01CX_2424(purE)
            CTH: Cthe_1250
            CDF: CD0218(purE)
            CBO: CBO2878(purE)
            CBA: CLB_2843(purE)
            CBH: CLC_2776(purE)
            CBF: CLI_2936(purE)
            CBE: Cbei_1054
            CKL: CKL_2689(purE)
            AMT: Amet_0916 Amet_0917
            CHY: CHY_1069(purE)
            DSY: DSY3933
            DRM: Dred_2371
            SWO: Swol_1780
            CSC: Csac_1630
            TTE: TTE0585(purE)
            MTA: Moth_2053
            MTU: Rv3275c(purE) Rv3276c(purK)
            MTC: MT3375(purE) MT3376(purK)
            MBO: Mb3303c(purE) Mb3304c(purK)
            MBB: BCG_3304c(purE) BCG_3305c(purK)
            MLE: ML0735(purK) ML0736(purE)
            MPA: MAP3393c(purE) MAP3394c(purK)
            MAV: MAV_4244(purE) MAV_4245(purK)
            MSM: MSMEG_1819(purK) MSMEG_1820(purE)
            MVA: Mvan_1713 Mvan_1714
            MGI: Mflv_4746
            MMC: Mmcs_1298 Mmcs_1299
            MKM: Mkms_1315 Mkms_1316
            MJL: Mjls_1334 Mjls_1335
            CGL: NCgl0681(cgl0711) NCgl0684(cgl0714)
            CGB: cg0816(purK) cg0820(purE)
            CEF: CE0742(purK) CE0744(purE)
            CDI: DIP0663(purK) DIP0664(purE)
            CJK: jk1658(purE) jk1659(purK)
            NFA: nfa10000(purK) nfa10010(purE)
            RHA: RHA1_ro06299(purK) RHA1_ro06300(purE)
            SCO: SCO3059(purE) SCO3060(purK)
            SMA: SAV5021(purK) SAV5022(purE)
            TWH: TWT026(purK) TWT027(purE)
            TWS: TW028(purK) TW029(purE)
            LXX: Lxx04830(purK) Lxx04850(purE)
            CMI: CMM_1003(purK) CMM_1004(purE)
            ART: Arth_1188 Arth_1189
            AAU: AAur_1306(purE) AAur_1307(purK)
            PAC: PPA1701 PPA1702
            NCA: Noca_3489 Noca_3490
            TFU: Tfu_2546 Tfu_2547
            FRA: Francci3_4371
            FAL: FRAAL6664(purE)
            ACE: Acel_0406 Acel_0407
            KRA: Krad_3904 Krad_3905
            SEN: SACE_6485(purE) SACE_6486(purK)
            STP: Strop_0931
            BLO: BL1129(purK) BL1130(purE)
            BAD: BAD_0515(purE) BAD_0516(purK)
            RXY: Rxyl_0253 Rxyl_0254
            FNU: FN0989
            RBA: RB6133(purK) RB6135(purE) RB8291(purE)
            TDE: TDE0687
            LIL: LA1462(purK) LA1463(purE)
            LIC: LIC12292(purE) LIC12293(purK)
            LBJ: LBJ_0961(purK) LBJ_0962(purE)
            LBL: LBL_2071(purE) LBL_2072(purK)
            SYN: sll0578(purK) sll0901(purE)
            SYW: SYNW1308(purK) SYNW2285(purE)
            SYC: syc0128_c(purK) syc1077_c(purE)
            SYF: Synpcc7942_0441 Synpcc7942_1428
            SYD: Syncc9605_1448 Syncc9605_2423
            SYE: Syncc9902_1052 Syncc9902_2103
            SYG: sync_1428(purK) sync_2638(purE)
            SYR: SynRCC307_1417(purK) SynRCC307_2265(purE)
            SYX: SynWH7803_1206(purK) SynWH7803_2304(purE)
            CYA: CYA_1667(purE) CYA_1770(purK)
            CYB: CYB_1031(purE) CYB_1214(purK)
            TEL: tll0586(purE) tlr1258(purK)
            GVI: gll1251(purE) gll1252(purK)
            ANA: alr0989(purK) alr2742
            AVA: Ava_2953 Ava_3022 Ava_4308
            PMA: Pro0191(purE) Pro1008(purK)
            PMM: PMM0167(purE) PMM0683(purK)
            PMT: PMT0669(purK) PMT2038(purE)
            PMN: PMN2A_0117 PMN2A_1534
            PMI: PMT9312_0169 PMT9312_0683
            PMB: A9601_01851(purE) A9601_07381(purK) A9601_14771
            PMC: P9515_01961(purE) P9515_07561(purK) P9515_14391
            PMF: P9303_15551(purK) P9303_19441 P9303_27131(purE)
            PMG: P9301_01871(purE) P9301_07361(purK) P9301_14631
            PMH: P9215_01851 P9215_07681
            PME: NATL1_02411(purE) NATL1_07431(purK) NATL1_16981
            TER: Tery_1473 Tery_4476
            BTH: BT_2518
            BFR: BF4364
            BFS: BF4163(purE)
            PGI: PG0951(purE)
            SRU: SRU_1620(purK) SRU_1621(purE) SRU_1645
            CHU: CHU_3733(purK) CHU_3734(purE)
            GFO: GFO_2869(purK) GFO_2870(purE)
            FJO: Fjoh_0425 Fjoh_0426
            FPS: FP1362(purK) FP1363(purE)
            CTE: CT0371(purE)
            CCH: Cag_0286
            CPH: Cpha266_0613
            PVI: Cvib_1371
            PLT: Plut_1580
            DET: DET0839(purE)
            DEH: cbdb_A820(purE)
            DEB: DehaBAV1_0758
            RRS: RoseRS_1820 RoseRS_1821
            RCA: Rcas_2524 Rcas_2525
            DRA: DR_0023 DR_0024
            DGE: Dgeo_0081 Dgeo_0082
            TTH: TTC0137 TTC0138
            TTJ: TTHA0513 TTHA0514
            AAE: aq_1178(purE) aq_245(purK)
            TMA: TM0446 TM0447
            TPT: Tpet_0474
            TME: Tmel_1232
            FNO: Fnod_1092 Fnod_1093
            MJA: MJ0616(purE)
            MMP: MMP0282(purE)
            MMQ: MmarC5_1391
            MMZ: MmarC7_1122 MmarC7_1285
            MAE: Maeo_0103 Maeo_0558
            MVN: Mevan_1293
            MAC: MA1376
            MBA: Mbar_A3125
            MMA: MM_1616 MM_2149 MM_2360
            MBU: Mbur_0877
            MTP: Mthe_0014
            MHU: Mhun_2474
            MEM: Memar_0055
            MBN: Mboo_0052
            MTH: MTH1393(purE)
            MST: Msp_1480(purE)
            MSI: Msm_1287
            MKA: MK1195(purE)
            AFU: AF1271(purE)
            HAL: VNG0632G(purK) VNG0633G(purE)
            HMA: rrnAC1431(purK) rrnAC1446(purE)
            HWA: HQ1635A(purK) HQ1636A(purE)
            NPH: NP2286A(purK) NP2290A(purE)
            TAC: Ta0303m Ta1107
            TVO: TVN0455 TVN1297
            PTO: PTO1474 PTO1475
            PHO: PH0320
            PAB: PAB1077(purE)
            PFU: PF0426 PF0427
            TKO: TK0835 TK0836
            IHO: Igni_0334
            SSO: SSO1064(purE) SSO1065(purK)
            STO: ST0806 ST0807
            SAI: Saci_1190(purE) Saci_1191
            MSE: Msed_1448 Msed_1449
            PAI: PAE0232(purK) PAE0250(purE)
            PIS: Pisl_0099 Pisl_0100
            PCL: Pcal_1891 Pcal_1892
            PAS: Pars_2174 Pars_2175
STRUCTURES  PDB: 1B6R  1B6S  1D7A  1O4V  1QCZ  1XMP  2ATE  2H31  2NSH  2NSJ  
                 2NSL  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.21
            ExPASy - ENZYME nomenclature database: 4.1.1.21
            ExplorEnz - The Enzyme Database: 4.1.1.21
            ERGO genome analysis and discovery system: 4.1.1.21
            BRENDA, the Enzyme Database: 4.1.1.21
            CAS: 9032-04-6
///
ENTRY       EC 4.1.1.22                 Enzyme
NAME        histidine decarboxylase;
            L-histidine decarboxylase;
            L-histidine carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     L-histidine carboxy-lyase (histamine-forming)
REACTION    L-histidine = histamine + CO2 [RN:R01167]
ALL_REAC    R01167
SUBSTRATE   L-histidine [CPD:C00135]
PRODUCT     histamine [CPD:C00388];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018];
            Pyruvate [CPD:C00022]
COMMENT     A pyridoxal-phosphate protein (in animal tissues). The bacterial
            enzyme has a pyruvoyl residue as prosthetic group.
REFERENCE   1
  AUTHORS   Epps, H.M.R.
  TITLE     Studies on bacterial amino-acid decarboxylases. 4. l(-)-Histidine
            decarboxylase from Cl. welchii type A.
  JOURNAL   Biochem. J. 39 (1945) 42-46.
  ORGANISM  Clostridium welchii
REFERENCE   2  [PMID:5681461]
  AUTHORS   Riley WD, Snell EE.
  TITLE     Histidine decarboxylase of Lactobacillus 30a. IV. The presence of
            covalently bound pyruvate as the prosthetic group.
  JOURNAL   Biochemistry. 7 (1968) 3520-8.
  ORGANISM  Lactobacillus sp.
REFERENCE   3  [PMID:5216347]
  AUTHORS   Rosenthaler J, Guirard BM, Chang GW, Snell EE.
  TITLE     Purification and properties of histidine decarboxylase from
            Lactobacillus 30a.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 54 (1965) 152-8.
  ORGANISM  Lactobacillus sp.
PATHWAY     PATH: map00340  Histidine metabolism
ORTHOLOGY   KO: K01590  histidine decarboxylase
GENES       HSA: 3067(HDC)
            MMU: 15186(Hdc)
            RNO: 24443(Hdc)
            CFA: 487551(HDC)
            GGA: 415454(HDC)
            SPU: 548615(HDC)
            DME: Dmel_CG3454(Hdc)
            PEN: PSEEN2506(pmsA)
            MCA: MCA2307
            FTU: FTT0664c(hdc)
            FTF: FTF0664c(hdc)
            FTL: FTL_0938
            FTH: FTH_0917(hdc)
            SUN: SUN_0880
            MLO: mlr6209
            LRE: Lreu_1832
            CPE: CPE0390(dchS)
            CPF: CPF_0378
            CPR: CPR_0373
            CTC: CTC01478
            GVI: gll2219
STRUCTURES  PDB: 1HQ6  1IBT  1IBU  1IBV  1IBW  1PYA  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.22
            ExPASy - ENZYME nomenclature database: 4.1.1.22
            ExplorEnz - The Enzyme Database: 4.1.1.22
            ERGO genome analysis and discovery system: 4.1.1.22
            BRENDA, the Enzyme Database: 4.1.1.22
            CAS: 9024-61-7
///
ENTRY       EC 4.1.1.23                 Enzyme
NAME        orotidine-5'-phosphate decarboxylase;
            orotidine-5'-monophosphate decarboxylase;
            orotodylate decarboxylase;
            orotidine phosphate decarboxylase;
            OMP decarboxylase;
            orotate monophosphate decarboxylase;
            orotidine monophosphate decarboxylase;
            orotidine phosphate decarboxylase;
            OMP-DC;
            orotate decarboxylase;
            orotidine 5'-phosphate decarboxylase;
            orotidylic decarboxylase;
            orotidylic acid decarboxylase;
            orotodylate decarboxylase;
            ODCase;
            orotic decarboxylase;
            orotidine-5'-phosphate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     orotidine-5'-phosphate carboxy-lyase (UMP-forming)
REACTION    orotidine 5'-phosphate = UMP + CO2 [RN:R00965]
ALL_REAC    R00965
SUBSTRATE   orotidine 5'-phosphate [CPD:C01103]
PRODUCT     UMP [CPD:C00105];
            CO2 [CPD:C00011]
COMMENT     The enzyme from higher eukaryotes is identical with EC 2.4.2.10
            orotate phosphoribosyltransferase .
REFERENCE   1  [PMID:692383]
  AUTHORS   Jones ME, Kavipurapu PR, Traut TW.
  TITLE     Orotate phosphoribosyltransferase: orotidylate decarboxylase
            (Ehrlich ascites cell).
  JOURNAL   Methods. Enzymol. 51 (1978) 155-67.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:14392174]
  AUTHORS   LIEBERMAN I, KORNBERG A, SIMMS ES.
  TITLE     Enzymatic synthesis of pyrimidine nucleotides;
            orotidine-5'-phosphate and uridine-5'-phosphate.
  JOURNAL   J. Biol. Chem. 215 (1955) 403-51.
REFERENCE   3  [PMID:6893554]
  AUTHORS   McClard RW, Black MJ, Livingstone LR, Jones ME.
  TITLE     Isolation and initial characterization of the single polypeptide
            that synthesizes uridine 5'-monophosphate from orotate in Ehrlich
            ascites carcinoma. Purification by tandem affinity chromatography of
            uridine-5'-monophosphate synthase.
  JOURNAL   Biochemistry. 19 (1980) 4699-706.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K01591  orotidine-5'-phosphate decarboxylase
GENES       HSA: 7372(UMPS)
            MMU: 22247(Umps)
            RNO: 288051(Umps)
            CFA: 478593(UMPS)
            BTA: 281568(UMPS)
            GGA: 424256(RCJMB04_1g10)
            XLA: 494728(LOC494728)
            DME: Dmel_CG3593(r-l)
            CEL: T07C4.1
            ATH: AT3G54470
            OSA: 4325739 4325740
            CME: CMK046C
            SCE: YEL021W(URA3)
            AGO: AGOS_AEL059W
            PIC: PICST_50417(URA3)
            CGR: CAGL0I03080g
            SPO: SPCC330.05c(ura4)
            ANI: AN6157.2
            AFM: AFUA_2G08360
            AOR: AO090011000868
            ANG: An12g03570(pyrA)
            UMA: UM04214.1
            DDI: DDB_0214958(pyr56)
            PFA: PF10_0225
            TAN: TA16510
            TPV: TP01_1133
            TBR: Tb927.5.3810
            TCR: 507059.60 508373.29 509899.110
            LMA: LmjF16.0550
            ECO: b1281(pyrF)
            ECJ: JW1273(pyrF)
            ECE: Z2525(pyrF)
            ECS: ECs1854
            ECC: c1750(pyrF)
            ECI: UTI89_C1552(pyrF)
            ECP: ECP_1334
            ECV: APECO1_441(pyrF)
            ECW: EcE24377A_1484(pyrF)
            ECX: EcHS_A1393 EcHS_A4440
            STY: STY1344(pyrF)
            STT: t1620(pyrF)
            SPT: SPA1169(pyrF)
            SEC: SC1702(pyrF)
            STM: STM1707(pyrF)
            YPE: YPO2227(pyrF)
            YPK: y2069(pyrF)
            YPM: YP_2026(pyrF)
            YPA: YPA_1587
            YPN: YPN_1696
            YPP: YPDSF_0907
            YPS: YPTB2149(pyrF)
            YPI: YpsIP31758_1913(pyrF)
            SFL: SF1285(pyrF)
            SFX: S1368(pyrF)
            SFV: SFV_1294(pyrF)
            SSN: SSON_1859(pyrF)
            SBO: SBO_1783(pyrF)
            SDY: SDY_1357(pyrF)
            ECA: ECA1957(pyrF)
            PLU: plu2427(pyrF)
            BUC: BU270(pyrF)
            BAS: BUsg260(pyrF)
            BAB: bbp251(pyrF)
            WBR: WGLp363(pyrF)
            SGL: SG1414
            ENT: Ent638_2187
            SPE: Spro_2647
            HIN: HI1224(pyrF)
            HIT: NTHI1944(pyrF)
            HIP: CGSHiEE_03855
            HIQ: CGSHiGG_01885
            HDU: HD1356(pyrF)
            PMU: PM0797(pyrF)
            MSU: MS1472(pyrF)
            APL: APL_0736(pyrF)
            ASU: Asuc_1548
            XFA: XF0034
            XFT: PD0025(pyrF)
            XCC: XCC4134(pyrF)
            XCB: XC_4226
            XCV: XCV4378(pyrF)
            XAC: XAC4276(pyrF)
            XOO: XOO0247(pyrF)
            XOM: XOO_0226(XOO0226)
            VCH: VC1911
            VCO: VC0395_A1501(pyrF)
            VVU: VV1_2977
            VVY: VV1304
            VPA: VP2026
            VFI: VF1755
            PPR: PBPRA2446
            PAE: PA2876(pyrF)
            PAU: PA14_26890(pyrF)
            PPU: PP_1815(pyrF)
            PPF: Pput_3896
            PST: PSPTO_2028(pyrF)
            PSB: Psyr_1836
            PSP: PSPPH_1796(pyrF)
            PFL: PFL_1754(pyrF)
            PFO: Pfl_4196
            PEN: PSEEN1510(pyrF)
            PMY: Pmen_2681
            PAR: Psyc_1491(pyrF)
            PCR: Pcryo_1670
            PRW: PsycPRwf_0944
            ACI: ACIAD2341(pyrF)
            SON: SO_2398(pyrF)
            SDN: Sden_1757
            SFR: Sfri_2119
            SAZ: Sama_1740
            SBL: Sbal_2074
            SBM: Shew185_2275
            SLO: Shew_1958
            SPC: Sputcn32_2038
            SSE: Ssed_2294
            SPL: Spea_2077
            SHE: Shewmr4_1928
            SHM: Shewmr7_2050
            SHN: Shewana3_1981
            SHW: Sputw3181_1975
            ILO: IL1351(pyrF)
            CPS: CPS_2339(pyrF)
            PHA: PSHAa1429(pyrF)
            PAT: Patl_2463
            SDE: Sde_2141
            PIN: Ping_3009
            MAQ: Maqu_1031
            CBU: CBU_0531(pyrF)
            CBD: COXBU7E912_1532(pyrF)
            LPN: lpg1425(pyrF)
            LPF: lpl1376(pyrF)
            LPP: lpp1380(pyrF)
            MCA: MCA1094(pyrF)
            FTU: FTT1648c(pyrF)
            FTF: FTF1648c(pyrF)
            FTW: FTW_1973(pyrF)
            FTL: FTL_0045
            FTH: FTH_0045(pyrF)
            FTA: FTA_0053(pyrF)
            FTN: FTN_0035(pyrF)
            TCX: Tcr_1201
            NOC: Noc_2353
            AEH: Mlg_0935
            HHA: Hhal_0559
            HCH: HCH_04974
            CSA: Csal_2155
            ABO: ABO_1741(pyrF)
            MMW: Mmwyl1_3220
            AHA: AHA_1813(pyrF)
            DNO: DNO_0564(pyrF)
            BCI: BCI_0298(pyrF)
            RMA: Rmag_0432
            VOK: COSY_0401(pyrF)
            NME: NMB0824
            NMA: NMA1033(pyrF)
            NMC: NMC0768(pyrF)
            NGO: NGO0401
            CVI: CV_3042(pyrF)
            RSO: RSc2773(pyrF)
            REU: Reut_A2851
            REH: H16_A3157(pyrF)
            RME: Rmet_3050
            BMA: BMA2481(pyrF)
            BMV: BMASAVP1_A0401(pyrF)
            BML: BMA10299_A1261(pyrF)
            BMN: BMA10247_3304(pyrF)
            BXE: Bxe_A0552
            BUR: Bcep18194_A3708(pyrF)
            BCN: Bcen_0143
            BCH: Bcen2424_0626
            BAM: Bamb_0527
            BPS: BPSL2963
            BPM: BURPS1710b_3478(pyrF)
            BPL: BURPS1106A_3481(pyrF)
            BPD: BURPS668_3443(pyrF)
            BTE: BTH_I1184(pyrF)
            PNU: Pnuc_0219
            BPE: BP3490(pyrF)
            BPA: BPP0863(pyrF)
            BBR: BB0957(pyrF)
            RFR: Rfer_3776
            POL: Bpro_4616
            PNA: Pnap_3843
            AAV: Aave_4696
            AJS: Ajs_4058
            VEI: Veis_1075
            MPT: Mpe_A3625
            HAR: HEAR0639
            MMS: mma_0606
            NEU: NE1959(pyrF)
            NET: Neut_0402
            NMU: Nmul_A2066
            EBA: ebA2293(pyrF)
            AZO: azo3659(pyrF)
            DAR: Daro_3450
            TBD: Tbd_0960
            MFA: Mfla_0923 Mfla_1067
            HPY: HP0005
            HPJ: jhp0005(pyrF)
            HPA: HPAG1_0005
            HHE: HH0036(pyrF)
            HAC: Hac_0258(pyrF)
            WSU: WS0297(pyrF)
            TDN: Tmden_1447
            CJE: Cj0381c(pyrF)
            CJR: CJE0430(pyrF)
            CJJ: CJJ81176_0404(pyrF)
            CJD: JJD26997_1577(pyrF)
            CFF: CFF8240_1332(pyrF)
            CCV: CCV52592_1179(pyrF)
            CHA: CHAB381_0031(pyrF)
            CCO: CCC13826_0659
            ABU: Abu_1848(pyrF)
            NIS: NIS_0516(pyrF)
            SUN: SUN_0676(pyrF)
            GSU: GSU1461(pyrF)
            GME: Gmet_1355
            GUR: Gura_2797
            PCA: Pcar_0684
            PPD: Ppro_1676
            DVU: DVU0901(pyrF)
            DVL: Dvul_2083
            DDE: Dde_2718
            LIP: LI0311(pyrF)
            BBA: Bd2996(pyrF)
            DPS: DP0722
            ADE: Adeh_3945
            AFW: Anae109_0480
            MXA: MXAN_5910(pyrF)
            SAT: SYN_01281
            SFU: Sfum_1728
            WOL: WD0461(pyrF)
            WBM: Wbm0787
            AMA: AM448(pyrF)
            APH: APH_0527(pyrF)
            ERU: Erum3040(pyrF)
            ERW: ERWE_CDS_03090(pyrF)
            ERG: ERGA_CDS_03040(pyrF)
            ECN: Ecaj_0284
            ECH: ECH_0792(pyrF)
            NSE: NSE_0793(pyrF)
            PUB: SAR11_0490(pyrF)
            MLO: mll4751
            MES: Meso_0683
            PLA: Plav_0145
            SME: SMc00412(pyrF)
            SMD: Smed_3540
            ATU: Atu0298(pyrF)
            ATC: AGR_C_515
            RET: RHE_CH00314(pyrF)
            RLE: RL0331(pyrF)
            BME: BMEI1999
            BMF: BAB1_2132
            BMS: BR2128(pyrF)
            BMB: BruAb1_2103(pyrF)
            BOV: BOV_2044(pyrF)
            OAN: Oant_0786
            BJA: blr0683(pyrF)
            BRA: BRADO0160(pyrF)
            BBT: BBta_0195(pyrF)
            RPA: RPA0337(pyrF)
            RPB: RPB_0433
            RPC: RPC_0333
            RPD: RPD_0387
            RPE: RPE_0345
            NWI: Nwi_1862
            NHA: Nham_1688
            BHE: BH13640(pyrF)
            BQU: BQ10840(pyrF)
            BBK: BARBAKC583_1044(pyrF)
            XAU: Xaut_0357
            CCR: CC_0105
            SIL: SPO3278(pyrF)
            SIT: TM1040_0129
            RSP: RSP_1404
            RSH: Rsph17029_0072
            RSQ: Rsph17025_2812
            JAN: Jann_3989
            RDE: RD1_0720(pyrF)
            PDE: Pden_0060
            MMR: Mmar10_2920
            HNE: HNE_0128(pyrF)
            ZMO: ZMO0587(pyrF)
            NAR: Saro_1307
            SAL: Sala_1066
            SWI: Swit_4089
            ELI: ELI_07575
            GOX: GOX2235
            GBE: GbCGDNIH1_2018
            ACR: Acry_1721
            RRU: Rru_A3424
            MAG: amb4002
            MGM: Mmc1_0514
            ABA: Acid345_2594
            SUS: Acid_4724
            BSU: BG10719(pyrF)
            BHA: BH2533(pyrF)
            BAN: BA4022(pyrF)
            BAR: GBAA4022(pyrF)
            BAA: BA_4493
            BAT: BAS3734
            BCE: BC3883
            BCA: BCE_3928(pyrF)
            BCZ: BCZK3642(pyrF)
            BCY: Bcer98_2532
            BTK: BT9727_3625(pyrF)
            BLI: BL02279(pyrF)
            BLD: BLi01775(pyrF)
            BCL: ABC2330(pyrF)
            BAY: RBAM_015380
            BPU: BPUM_1454
            OIH: OB1494(pyrF)
            GKA: GK1155
            SAU: SA1047(pyrF)
            SAV: SAV1204(pyrF)
            SAM: MW1087(pyrF)
            SAR: SAR1180(pyrF)
            SAS: SAS1138
            SAC: SACOL1216(pyrF)
            SAB: SAB1068(pyrF)
            SAA: SAUSA300_1097(pyrF)
            SAO: SAOUHSC_01171
            SAJ: SaurJH9_1263
            SAH: SaurJH1_1288
            SEP: SE0880
            SER: SERP0770(pyrF)
            SHA: SH1710(pyrF)
            SSP: SSP1568
            LMO: lmo1832(pyrF)
            LMF: LMOf2365_1860(pyrF)
            LIN: lin1946(pyrF)
            LWE: lwe1851(pyrF)
            LLA: L181692(pyrF)
            LLC: LACR_1468
            LLM: llmg_1107(pyrF)
            SPY: SPy_0900(pyrF)
            SPZ: M5005_Spy_0703(pyrF)
            SPM: spyM18_0959(pyrF)
            SPG: SpyM3_0616(pyrF)
            SPS: SPs1237(pyrF)
            SPH: MGAS10270_Spy0761(pyrF)
            SPI: MGAS10750_Spy0795(pyrF)
            SPJ: MGAS2096_Spy0775(pyrF)
            SPK: MGAS9429_Spy0759(pyrF)
            SPF: SpyM51105(pyrF)
            SPA: M6_Spy0720
            SPB: M28_Spy0683(pyrF)
            SPN: SP_0701
            SPR: spr0613(pyrF)
            SPD: SPD_0608(pyrF)
            SAG: SAG1047(pyrF)
            SAN: gbs1082(pyrF)
            SAK: SAK_1137(pyrF)
            SMU: SMU.1222(pyrF)
            STC: str0967(pyrF)
            STL: stu0967(pyrF)
            SSA: SSA_1241(pyrF)
            SGO: SGO_1254(pyrF)
            LPL: lp_2698(pyrF)
            LJO: LJ1282
            LAC: LBA1386(pyrF)
            LSA: LSA0958(pyrF)
            LSL: LSL_0830(pyrF)
            LDB: Ldb1531(pyrF)
            LBU: LBUL_1422
            LBR: LVIS_2229
            LCA: LSEI_1450
            LRE: Lreu_0126
            EFA: EF1713(pyrF)
            OOE: OEOE_0262
            STH: STH1244
            CAC: CAC2652(pyrF)
            CPE: CPE1180(pyrF)
            CPF: CPF_1384(pyrF)
            CPR: CPR_1199(pyrF)
            CTC: CTC02381(pyrF)
            CNO: NT01CX_0393(pyrF)
            CTH: Cthe_0951
            CDF: CD3592(pyrF)
            CBO: CBO3238(pyrF)
            CBA: CLB_3275(pyrF)
            CBH: CLC_3149(pyrF)
            CBF: CLI_3377(pyrF)
            CKL: CKL_3358(pyrF)
            CHY: CHY_1496(pyrF)
            DSY: DSY2856
            DRM: Dred_1687
            SWO: Swol_1278
            TTE: TTE1532(pyrF)
            MTA: Moth_0883
            MPE: MYPE7850(pyrF)
            MTU: Rv1385(pyrF)
            MTC: MT1429(pyrF)
            MBO: Mb1420(pyrF)
            MBB: BCG_1446(pyrF)
            MLE: ML0537(pyrF)
            MPA: MAP1120(pyrF)
            MAV: MAV_3388(pyrF)
            MSM: MSMEG_3048(pyrF)
            MUL: MUL_1785(pyrF)
            MVA: Mvan_2665
            MMC: Mmcs_2368
            MKM: Mkms_2415
            MJL: Mjls_2409
            CGL: NCgl1546(pyrF)
            CGB: cg1812(pyrF)
            CEF: CE1728
            CDI: DIP1330(pyrF)
            CJK: jk1021(pyrF)
            NFA: nfa36180(pyrF) pnf11210
            RHA: RHA1_ro07153(pyrF)
            SCO: SCO1481(pyrF)
            SMA: SAV6869(pyrF)
            TWH: TWT364(pyrF)
            TWS: TW405(pyrF)
            LXX: Lxx11110(pyrF)
            CMI: CMM_1781(pyrF)
            AAU: AAur_2264(pyrF)
            PAC: PPA1003
            TFU: Tfu_1060
            FRA: Francci3_3197
            FAL: FRAAL5233(pyrF)
            ACE: Acel_1295
            SEN: SACE_2084(pyrF)
            BLO: BL0069 BL0791(pyrF)
            BAD: BAD_0537 BAD_0762(pyrF)
            RXY: Rxyl_2300
            FNU: FN0426
            RBA: RB12661(pyrF)
            TDE: TDE2110(pyrF)
            LIL: LB310(pyrF)
            LBJ: LBJ_4227(pyrF)
            LBL: LBL_4241(pyrF)
            SYN: sll0838(pyrF)
            SYW: SYNW0571(pyrF)
            SYC: syc1541_d(pyrF)
            SYF: Synpcc7942_2569
            SYD: Syncc9605_2100
            SYE: Syncc9902_0570
            SYG: sync_0364 sync_2200(pyrF)
            SYR: SynRCC307_1803(pyrF)
            SYX: SynWH7803_1942(pyrF)
            CYA: CYA_1712(pyrF)
            CYB: CYB_0343(pyrF)
            TEL: tll0395(pyrF)
            GVI: gll1658(pyrF) glr1079
            ANA: alr2945 alr2983
            AVA: Ava_0924 Ava_0957
            PMA: Pro1409(pyrF)
            PMM: PMM1328(pyrF)
            PMT: PMT1402(pyrF)
            PMN: PMN2A_0899
            PMI: PMT9312_1426
            PMB: A9601_15281(pyrF)
            PMC: P9515_14891(pyrF)
            PMF: P9303_05621(pyrF)
            PMG: P9301_15141(pyrF)
            PMH: P9215_15571
            PME: NATL1_17551(pyrF)
            TER: Tery_0446
            BTH: BT_4209
            BFR: BF0909
            BFS: BF0831
            PGI: PG0073
            SRU: SRU_1735(pyrF)
            CHU: CHU_2698
            GFO: GFO_0478(pyrF)
            FPS: FP0537(pyrF)
            CTE: CT0129(pyrF)
            CCH: Cag_0006
            CPH: Cpha266_2677
            PLT: Plut_0079
            DET: DET0013(pyrF)
            DEH: cbdb_A14(pyrF)
            DRA: DR_2200
            DGE: Dgeo_1404
            TTH: TTC1381
            TTJ: TTHA1743
            AAE: aq_1580(pyrF)
            TMA: TM0332
            MJA: MJ0252
            MMP: MMP0602(pyrF)
            MMQ: MmarC5_1004
            MMZ: MmarC7_1624
            MAE: Maeo_0073
            MVN: Mevan_1474
            MAC: MA0969
            MBA: Mbar_A0060
            MMA: MM_2083
            MBU: Mbur_1000
            MTP: Mthe_0629
            MHU: Mhun_2545
            MEM: Memar_2350
            MBN: Mboo_0183
            MST: Msp_0397(pyrF)
            MSI: Msm_1617
            MKA: MK0735(pyrF)
            AFU: AF0929
            HAL: VNG1673G(pyrF)
            HMA: rrnAC1515(pyrF)
            HWA: HQ3219A(pyrF)
            NPH: NP1734A(pyrF)
            TAC: Ta0073
            TVO: TVN0028
            PTO: PTO0210
            PHO: PH0731
            PAB: PAB1505
            PFU: PF1114
            TKO: TK2276
            RCI: RRC356(pyrF)
            APE: APE_2348
            HBU: Hbut_0112
            SSO: SSO0616(pyrF)
            STO: ST1482
            SAI: Saci_1598(pyrF)
            PAI: PAE0768(pyrF)
STRUCTURES  PDB: 1DBT  1DQW  1DQX  1DV7  1DVJ  1EIX  1JJK  1KLY  1KLZ  1KM0  
                 1KM1  1KM2  1KM3  1KM4  1KM5  1KM6  1L2U  1LOL  1LOQ  1LOR  
                 1LOS  1LP6  1VQT  1X1Z  2CZ5  2CZD  2CZE  2CZF  2E6Y  2EAW  
                 2F84  2JGY  2V30  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.23
            ExPASy - ENZYME nomenclature database: 4.1.1.23
            ExplorEnz - The Enzyme Database: 4.1.1.23
            ERGO genome analysis and discovery system: 4.1.1.23
            BRENDA, the Enzyme Database: 4.1.1.23
            CAS: 9024-62-8
///
ENTRY       EC 4.1.1.24                 Enzyme
NAME        aminobenzoate decarboxylase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     aminobenzoate carboxy-lyase (aniline-forming)
REACTION    4(or 2)-aminobenzoate = aniline + CO2 [RN:R00990 R01860]
ALL_REAC    R00990 R01860
SUBSTRATE   4-aminobenzoate [CPD:C00568];
            2-aminobenzoate [CPD:C00108]
PRODUCT     aniline [CPD:C00292];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1
  AUTHORS   McCullough, W.G., Piligian, J.T. and Daniel, I.J.
  TITLE     Enzymatic decarboxylation of three aminobenzoates.
  JOURNAL   J. Am. Chem. Soc. 79 (1957) 628-630.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.24
            ExPASy - ENZYME nomenclature database: 4.1.1.24
            ExplorEnz - The Enzyme Database: 4.1.1.24
            ERGO genome analysis and discovery system: 4.1.1.24
            BRENDA, the Enzyme Database: 4.1.1.24
            CAS: 9024-73-1
///
ENTRY       EC 4.1.1.25                 Enzyme
NAME        tyrosine decarboxylase;
            L-tyrosine decarboxylase;
            L-(-)-tyrosine apodecarboxylase;
            L-tyrosine carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     L-tyrosine carboxy-lyase (tyramine-forming)
REACTION    L-tyrosine = tyramine + CO2 [RN:R00736]
ALL_REAC    R00736;
            (other) R02080
SUBSTRATE   L-tyrosine [CPD:C00082]
PRODUCT     tyramine [CPD:C00483];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. The bacterial enzyme also acts on
            3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine.
REFERENCE   1
  AUTHORS   McGilvery, R.W. and Cohen, P.P.
  TITLE     The decarboxylation of L-phenylalanine by Streptococcus faecalis R.
  JOURNAL   J. Biol. Chem. 174 (1948) 813-816.
  ORGANISM  Streptococcus faecalis
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00950  Alkaloid biosynthesis I
ORTHOLOGY   KO: K01592  tyrosine decarboxylase
GENES       DME: Dmel_CG30445(Tdc1) Dmel_CG30446(Tdc2)
            ATH: AT2G20340 AT4G28680
            OSA: 4343080
            REH: H16_A1025
            GBE: GbCGDNIH1_0718
            MJA: MJ0050
            MMP: MMP0131
            MAC: MA0006
            MBA: Mbar_A0977
            MMA: MM_1317
            MBU: Mbur_1732
            MHU: Mhun_2611
            MTH: MTH1116
            MST: Msp_0329(mfnA)
            MSI: Msm_0987
            MKA: MK1500
            AFU: AF2004
            HAL: VNG0327G(gadD)
            HMA: rrnAC1798(gadD)
            NPH: NP1194A(gadD)
            PTO: PTO0150
            PHO: PH0937
            PAB: PAB1578
            PFU: PF1159
            TKO: TK1814
            RCI: RCIX1543(mfnA)
            APE: APE_0020.1
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.25
            ExPASy - ENZYME nomenclature database: 4.1.1.25
            ExplorEnz - The Enzyme Database: 4.1.1.25
            ERGO genome analysis and discovery system: 4.1.1.25
            BRENDA, the Enzyme Database: 4.1.1.25
            CAS: 9002-09-9
///
ENTRY       EC 4.1.1.26       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
COMMENT     Deleted entry: DOPA decarboxylase. Now included with EC 4.1.1.28
            aromatic-L-amino-acid decarboxylase (EC 4.1.1.26 created 1961,
            deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.26
            ExPASy - ENZYME nomenclature database: 4.1.1.26
            ExplorEnz - The Enzyme Database: 4.1.1.26
            ERGO genome analysis and discovery system: 4.1.1.26
            BRENDA, the Enzyme Database: 4.1.1.26
///
ENTRY       EC 4.1.1.27       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
COMMENT     Deleted entry: tryptophan decarboxylase. Now included with EC
            4.1.1.28 aromatic-L-amino-acid decarboxylase (EC 4.1.1.27 created
            1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.27
            ExPASy - ENZYME nomenclature database: 4.1.1.27
            ExplorEnz - The Enzyme Database: 4.1.1.27
            ERGO genome analysis and discovery system: 4.1.1.27
            BRENDA, the Enzyme Database: 4.1.1.27
///
ENTRY       EC 4.1.1.28                 Enzyme
NAME        aromatic-L-amino-acid decarboxylase;
            DOPA decarboxylase;
            tryptophan decarboxylase;
            hydroxytryptophan decarboxylase;
            L-DOPA decarboxylase;
            aromatic amino acid decarboxylase;
            5-hydroxytryptophan decarboxylase;
            aromatic-L-amino-acid carboxy-lyase;
            aromatic-L-amino-acid carboxy-lyase (tryptamine-forming)
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     aromatic-L-amino-acid carboxy-lyase
REACTION    (1) 3,4-dihydroxy-L-phenylalanine = dopamine + CO2 [RN:R02080];
            (2) 5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2 [RN:R02701]
ALL_REAC    R02080 R02701;
            (other) R00685 R00699 R00736 R01167 R04909
SUBSTRATE   3,4-dihydroxy-L-phenylalanine [CPD:C00355];
            5-hydroxy-L-tryptophan [CPD:C00643]
PRODUCT     dopamine [CPD:C03758];
            CO2 [CPD:C00011];
            5-hydroxytryptamine [CPD:C00780]
COFACTOR    Pyridoxal phosphate [CPD:C00018];
            PQQ [CPD:C00113]
COMMENT     A pyridoxal-phosphate protein. The enzyme also acts on some other
            aromatic L-amino acids, including L-tryptophan.
REFERENCE   1  [PMID:4536745]
  AUTHORS   Christenson JG, Dairman W, Udenfriend S.
  TITLE     On the identity of DOPA decarboxylase and 5-hydroxytryptophan
            decarboxylase (immunological titration-aromatic L-amino acid
            decarboxylase-serotonin-dopamine-norepinephrine).
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 69 (1972) 343-7.
  ORGANISM  guinea pig
REFERENCE   2  [PMID:14466899]
  AUTHORS   LOVENBERG W, WEISSBACH H, UDENFRIEND S.
  TITLE     Aromatic L-amino acid decarboxylase.
  JOURNAL   J. Biol. Chem. 237 (1962) 89-93.
  ORGANISM  guinea pig
REFERENCE   3
  AUTHORS   McGilvery, R.W. and Cohen, P.P.
  TITLE     The decarboxylation of L-phenylalanine by Streptococcus faecalis R.
  JOURNAL   J. Biol. Chem. 174 (1948) 813-816.
  ORGANISM  Streptococcus faecalis
REFERENCE   4
  AUTHORS   Sekeris, C.E.
  TITLE     Zur Tyrosinstoffwechsel der Insekten. XII. Reinigung, Eigenschaften
            und Substratspezifitat der DOPA-Decarboxylase.
  JOURNAL   Hoppe-Seyler's Z. Physiol. Chem. 332 (1963) 70-78.
REFERENCE   5  [PMID:13462983]
  AUTHORS   WEISSBACH H, BOGDANSKI DF, REDFIELD BG, UDENFRIEND S.
  TITLE     Studies on the effect of vitamin B6 on 5-hydroxytryptamine
            (serotonin) formation.
  JOURNAL   J. Biol. Chem. 227 (1957) 617-24.
  ORGANISM  guinea pig
PATHWAY     PATH: map00340  Histidine metabolism
            PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
            PATH: map00380  Tryptophan metabolism
            PATH: map00901  Indole and ipecac alkaloid biosynthesis
            PATH: map00950  Alkaloid biosynthesis I
ORTHOLOGY   KO: K01593  aromatic-L-amino-acid decarboxylase
GENES       HSA: 1644(DDC)
            PTR: 463409(DDC)
            MMU: 13195(Ddc)
            RNO: 24311(Ddc)
            CFA: 606852(DDC)
            BTA: 280762(DDC)
            SSC: 396857(DDC)
            GGA: 420947(DDC)
            XTR: 496742(LOC496742)
            SPU: 577767(LOC577767) 593847(LOC593847) 759472(LOC759472)
                 764126(LOC764126)
            DME: Dmel_CG10697(Ddc)
            CEL: C05D2.3 ZK829.2(hdl-1)
            ANI: AN2357.2
            AFM: AFUA_3G02240
            AOR: AO090038000057
            CNE: CND00950
            UMA: UM06083.1
            TET: TTHERM_00929550
            YPE: YPO1193
            YPK: y2996(dcd)
            YPM: YP_0943(dcd1)
            YPA: YPA_0905
            YPN: YPN_2783
            YPP: YPDSF_2502
            YPS: YPTB1234
            YPI: YpsIP31758_2788
            PPU: PP_2552
            PPF: Pput_3163
            PEN: PSEEN2370
            NOC: Noc_2983
            BUR: Bcep18194_B2911
            DVU: DVU0867
            DVL: Dvul_2115
            DDE: Dde_1124
            AFW: Anae109_1428
            MLO: mll0712
            NWI: Nwi_1102
            XAU: Xaut_0071
            SIL: SPO3687
            SIT: TM1040_3466
            MMR: Mmar10_1409
            ABA: Acid345_2160
            SUS: Acid_1182
            FRA: Francci3_2867
            SEN: SACE_2888
            RXY: Rxyl_1038
STRUCTURES  PDB: 1JS3  1JS6  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.28
            ExPASy - ENZYME nomenclature database: 4.1.1.28
            ExplorEnz - The Enzyme Database: 4.1.1.28
            ERGO genome analysis and discovery system: 4.1.1.28
            BRENDA, the Enzyme Database: 4.1.1.28
            CAS: 9042-64-2
///
ENTRY       EC 4.1.1.29                 Enzyme
NAME        sulfinoalanine decarboxylase;
            cysteine-sulfinate decarboxylase;
            L-cysteinesulfinic acid decarboxylase;
            cysteine-sulfinate decarboxylase;
            CADCase/CSADCase;
            CSAD;
            cysteic decarboxylase;
            cysteinesulfinic acid decarboxylase;
            cysteinesulfinate decarboxylase;
            sulfoalanine decarboxylase;
            3-sulfino-L-alanine carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     3-sulfino-L-alanine carboxy-lyase (hypotaurine-forming)
REACTION    3-sulfino-L-alanine = hypotaurine + CO2 [RN:R02466]
ALL_REAC    R02466;
            (other) R01682
SUBSTRATE   3-sulfino-L-alanine [CPD:C00606]
PRODUCT     hypotaurine [CPD:C00519];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also acts on L-cysteate. The 1992
            edition of the Enzyme List erroneously gave the name sulfoalanine
            decarboxylase to this enzyme.
REFERENCE   1  [PMID:236774]
  AUTHORS   Guion-Rain M-C, Portemer C, Chatagner F.
  TITLE     Rat liver cysteine sulfinate decarboxylase: purification, new
            appraisal of the molecular weight and determination of catalytic
            properties.
  JOURNAL   Biochim. Biophys. Acta. 384 (1975) 265-76.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:14159288]
  AUTHORS   JACOBSEN JG, THOMAS LL, SMITH LH Jr.
  TITLE     PROPERTIES AND DISTRIBUTION OF MAMMALIAN L-CYSTEINE SULFINATE
            CARBOXY-LYASES.
  JOURNAL   Biochim. Biophys. Acta. 85 (1964) 103-16.
  ORGANISM  rat [GN:rno], cat, dog [GN:cfa], chicken [GN:gga]
PATHWAY     PATH: map00430  Taurine and hypotaurine metabolism
ORTHOLOGY   KO: K01594  sulfinoalanine decarboxylase
GENES       HSA: 51380(CSAD)
            MMU: 246277(Csad)
            RNO: 60356(Csad)
            SPU: 575490(LOC575490)
            DME: Dmel_CG5618
            SYG: sync_1564
            AVA: Ava_2838
STRUCTURES  PDB: 2JIS  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.29
            ExPASy - ENZYME nomenclature database: 4.1.1.29
            ExplorEnz - The Enzyme Database: 4.1.1.29
            ERGO genome analysis and discovery system: 4.1.1.29
            BRENDA, the Enzyme Database: 4.1.1.29
            CAS: 62213-10-9
///
ENTRY       EC 4.1.1.30                 Enzyme
NAME        pantothenoylcysteine decarboxylase;
            pantothenylcysteine decarboxylase;
            N-[(R)-pantothenoyl]-L-cysteine carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     N-[(R)-pantothenoyl]-L-cysteine carboxy-lyase (pantetheine-forming)
REACTION    N-[(R)-pantothenoyl]-L-cysteine = pantetheine + CO2 [RN:R02972]
ALL_REAC    R02972
SUBSTRATE   N-((R)-pantothenoyl)-L-cysteine [CPD:C04079]
PRODUCT     pantetheine [CPD:C00831];
            CO2 [CPD:C00011]
REFERENCE   1  [PMID:13438850]
  AUTHORS   BROWN GM.
  TITLE     Pantothenylcysteine, a precursor of pantetheine in Lactobacillus
            helveticus.
  JOURNAL   J. Biol. Chem. 226 (1957) 651-61.
  ORGANISM  Lactobacillus helveticus
PATHWAY     PATH: map00770  Pantothenate and CoA biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.30
            ExPASy - ENZYME nomenclature database: 4.1.1.30
            ExplorEnz - The Enzyme Database: 4.1.1.30
            ERGO genome analysis and discovery system: 4.1.1.30
            BRENDA, the Enzyme Database: 4.1.1.30
            CAS: 9024-65-1
///
ENTRY       EC 4.1.1.31                 Enzyme
NAME        phosphoenolpyruvate carboxylase;
            phosphopyruvate (phosphate) carboxylase;
            PEP carboxylase;
            phosphoenolpyruvic carboxylase;
            PEPC;
            PEPCase;
            phosphate:oxaloacetate carboxy-lyase (phosphorylating)
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     phosphate:oxaloacetate carboxy-lyase (adding phosphate;
            phosphoenolpyruvate-forming)
REACTION    phosphate + oxaloacetate = H2O + phosphoenolpyruvate + CO2
            [RN:R00345]
ALL_REAC    R00345
SUBSTRATE   phosphate [CPD:C00009];
            oxaloacetate [CPD:C00036]
PRODUCT     H2O [CPD:C00001];
            phosphoenolpyruvate [CPD:C00074];
            CO2 [CPD:C00011]
REFERENCE   1  [PMID:5501374]
  AUTHORS   Chen JH, Jones RF.
  TITLE     Multiple forms of phosphoenolpyruvate carboxylase from Chlamydomonas
            reeinhardtii.
  JOURNAL   Biochim. Biophys. Acta. 214 (1970) 318-25.
  ORGANISM  Chlamydomonas reeinhardtii
REFERENCE   2  [PMID:16655053]
  AUTHORS   Mazelis M, Vennesland B.
  TITLE     Carbon Dioxide Fixation into Oxalacetate in Higher Plants.
  JOURNAL   Plant. Physiol. 32 (1957) 591-600.
PATHWAY     PATH: map00620  Pyruvate metabolism
            PATH: map00710  Carbon fixation
            PATH: map00720  Reductive carboxylate cycle (CO2 fixation)
ORTHOLOGY   KO: K01595  phosphoenolpyruvate carboxylase
GENES       ATH: AT1G53310(ATPPC1) AT3G14940(ATPPC3)
            OSA: 4325309 4325531 4326138 4328859 4345387
            CME: CME095C
            PFA: PF14_0246
            CPV: cgd5_70
            CHO: Chro.50389
            TET: TTHERM_01207690
            ECO: b3956(ppc)
            ECJ: JW3928(ppc)
            ECE: Z5514(ppc)
            ECS: ECs4885
            ECC: c4915(ppc)
            ECI: UTI89_C4547(ppc)
            ECP: ECP_4169
            ECV: APECO1_2511(ppc)
            ECW: EcE24377A_4495(ppc)
            ECX: EcHS_A4190
            STY: STY3754(ppc)
            STT: t3505(ppc)
            SPT: SPA3957(ppc)
            SEC: SC4009(ppc)
            STM: STM4119(ppc)
            YPE: YPO3929(ppc)
            YPK: y0308(ppc)
            YPM: YP_3121(ppc)
            YPA: YPA_0095
            YPN: YPN_0040
            YPP: YPDSF_3539
            YPS: YPTB0108(ppc)
            YPI: YpsIP31758_0125(ppc)
            YEN: YE0116(glu)
            SFL: SF4033(ppc)
            SFX: S3713(ppc)
            SFV: SFV_4025(ppc)
            SSN: SSON_4129(ppc)
            SBO: SBO_3975(ppc)
            SDY: SDY_3791(ppc)
            ECA: ECA0187(ppc)
            PLU: plu4746(ppc)
            ENT: Ent638_4030
            SPE: Spro_4783
            HIT: NTHI1403(ppc)
            HIP: CGSHiEE_05910
            HIQ: CGSHiGG_09905
            HSO: HS_0994(ppc)
            PMU: PM0546(ppc)
            MSU: MS1017(ppc)
            APL: APL_0339(pepC)
            XCC: XCC0754(ppc)
            XCB: XC_3479
            XCV: XCV0858
            XAC: XAC0806(ppc)
            XOO: XOO3796(ppc)
            XOM: XOO_3578(XOO3578)
            VCH: VC2646
            VCO: VC0395_A2222(ppc)
            VVU: VV1_1369
            VVY: VV3004
            VPA: VP2761
            VFI: VF2308
            PPR: PBPRA0265
            PAE: PA3687(ppc)
            PAU: PA14_16690(ppc)
            PPU: PP_1505(ppc)
            PPF: Pput_4217
            PST: PSPTO_1508(ppc)
            PSB: Psyr_1318
            PSP: PSPPH_3865(ppc)
            PFL: PFL_1147(ppc)
            PFO: Pfl_1069
            PEN: PSEEN1264(ppc)
            PMY: Pmen_3360
            PAR: Psyc_1138(ppc)
            PCR: Pcryo_1822
            PRW: PsycPRwf_0561
            ACI: ACIAD3627(ppc)
            SON: SO_0274(ppc)
            SDN: Sden_0248
            SFR: Sfri_0189
            SAZ: Sama_0254
            SBL: Sbal_4125
            SBM: Shew185_4096
            SLO: Shew_0200
            SPC: Sputcn32_3718
            SSE: Ssed_4278
            SPL: Spea_0225
            SHE: Shewmr4_3710
            SHM: Shewmr7_0235
            SHN: Shewana3_3906
            SHW: Sputw3181_3861
            PHA: PSHAb0314(ppc)
            PAT: Patl_0606
            SDE: Sde_3380
            PIN: Ping_0226
            MAQ: Maqu_2234
            LPN: lpg1607(capP)
            LPF: lpl1418
            LPP: lpp1572
            TCX: Tcr_1521
            NOC: Noc_0770
            AEH: Mlg_0261
            HHA: Hhal_2291
            HCH: HCH_01811(ppc)
            CSA: Csal_1640
            ABO: ABO_0680(ppc)
            MMW: Mmwyl1_1255
            AHA: AHA_0591(ppc)
            NME: NMB2061
            NMA: NMA0374(ppc)
            NMC: NMC2042(ppc)
            NGO: NGO2020
            CVI: CV_0055(ppc)
            RSO: RSc2358(ppc)
            REU: Reut_A0699
            REH: H16_A2921(ppc)
            RME: Rmet_2750
            BMA: BMA0729(ppc)
            BMV: BMASAVP1_A2286(ppc)
            BML: BMA10299_A2999(ppc)
            BMN: BMA10247_1599(ppc)
            BXE: Bxe_A3412
            BVI: Bcep1808_2510
            BUR: Bcep18194_A5753
            BCN: Bcen_1814
            BCH: Bcen2424_2426
            BAM: Bamb_2469
            BPS: BPSL1013
            BPM: BURPS1710b_1228(ppc)
            BPL: BURPS1106A_1075(ppc)
            BPD: BURPS668_1069(ppc)
            BTE: BTH_I0871(ppc)
            BPE: BP0215(ppc)
            BPA: BPP0418(ppc)
            BBR: BB0420(ppc)
            RFR: Rfer_1714
            POL: Bpro_3665
            PNA: Pnap_3091
            AAV: Aave_2000
            AJS: Ajs_2889
            VEI: Veis_1041
            MPT: Mpe_A3003 Mpe_A3255
            HAR: HEAR1006(ppc)
            MMS: mma_1141
            NEU: NE0589(ppc)
            NET: Neut_1036
            NMU: Nmul_A2691
            EBA: ebA1167(ppc)
            AZO: azo0992(ppc)
            DAR: Daro_1759
            TBD: Tbd_0630
            HHE: HH1203(ppc)
            WSU: WS1877(clpA)
            GME: Gmet_0304
            PPD: Ppro_2974
            BBA: Bd0608(ppc)
            MXA: MXAN_4571(ppc)
            PUB: SAR11_0780(ppc)
            BJA: blr2955(ppc)
            BRA: BRADO2580(ppc)
            BBT: BBta_2928(ppc)
            RPA: RPA1772(ppc)
            RPB: RPB_3592
            RPC: RPC_1684
            RPD: RPD_1876
            RPE: RPE_1791
            NWI: Nwi_2278
            NHA: Nham_2691
            XAU: Xaut_0318
            CCR: CC_1493
            SIL: SPO1571(ppc)
            RDE: RD1_4248(ppc)
            HNE: HNE_1122
            ZMO: ZMO1496(ppc)
            NAR: Saro_2567
            SAL: Sala_3081
            SWI: Swit_3135
            ELI: ELI_00525
            GBE: GbCGDNIH1_0054 GbCGDNIH1_1334
            ABA: Acid345_3689
            SPY: SPy_0608(ppc)
            SPZ: M5005_Spy_0505(ppc)
            SPM: spyM18_0675(pepC)
            SPG: SpyM3_0430(ppc)
            SPS: SPs1425
            SPH: MGAS10270_Spy0499(ppc)
            SPI: MGAS10750_Spy0524(ppc)
            SPJ: MGAS2096_Spy0516(ppc)
            SPK: MGAS9429_Spy0495(ppc)
            SPF: SpyM51358(ppc)
            SPA: M6_Spy0526
            SPB: M28_Spy0484(ppc)
            SPN: SP_1068
            SPR: spr0974(ppc)
            SPD: SPD_0953(ppc)
            SAG: SAG0759(ppc)
            SAN: gbs0780
            SAK: SAK_0885(ppc)
            SMU: SMU.712(capP)
            STC: str0718(ppc)
            STL: stu0718(ppc)
            SSA: SSA_1521(ppc)
            SGO: SGO_0760(ppc)
            LJO: LJ1272 LJ1273
            LAC: LBA1092
            LDB: Ldb0501(ppc)
            LBU: LBUL_0443
            CPF: CPF_1350(ppcA)
            MPE: MYPE9390
            MLE: ML0578(ppc)
            MPA: MAP1169(ppc)
            MAV: MAV_3336(ppc)
            MSM: MSMEG_3097(ppc)
            MVA: Mvan_2707
            MGI: Mflv_3706
            MMC: Mmcs_2408
            MKM: Mkms_2454
            MJL: Mjls_2448
            CGL: NCgl1523(cgl1585)
            CGB: cg1787(ppc)
            CEF: CE1703
            CDI: DIP1122(ppc)
            CJK: jk0998(ppc)
            NFA: nfa19280(ppc)
            RHA: RHA1_ro07181(ppc)
            SCO: SCO3127(ppc)
            SMA: SAV3566(ppc)
            ART: Arth_0614
            AAU: AAur_0764(ppc)
            TFU: Tfu_2554
            FAL: FRAAL0594(argE)
            ACE: Acel_0397
            KRA: Krad_3372
            STP: Strop_0883
            BLO: BL0604(ppc)
            BAD: BAD_0024
            RBA: RB4944(ppc)
            SYN: sll0920(ppc)
            SYW: SYNW2047(ppc)
            SYC: syc1846_d(ppc)
            SYF: Synpcc7942_2252
            SYD: Syncc9605_0396
            SYE: Syncc9902_1933
            SYG: sync_0460(ppc)
            SYR: SynRCC307_2090(ppc)
            SYX: SynWH7803_0454(ppc)
            CYA: CYA_0838(ppc)
            CYB: CYB_1842(ppc)
            TEL: tll1912(ppc)
            GVI: gll0414(ppc)
            ANA: all4861(ppc)
            AVA: Ava_2134
            PMA: Pro1730(ppc)
            PMM: PMM1575(ppc)
            PMT: PMT1713(ppc)
            PMN: PMN2A_1147
            PMI: PMT9312_1667
            PMB: A9601_17821(ppc)
            PMC: P9515_17621(ppc)
            PMF: P9303_22741(ppc)
            PMG: P9301_17661(ppc)
            PMH: P9215_18471
            PME: NATL1_20211(ppc)
            TER: Tery_0836
            SRU: SRU_0093(ppc)
            CHU: CHU_2855(ppc)
            GFO: GFO_1487(ppc)
            FJO: Fjoh_2806
            CTE: CT1640(ppc)
            CPH: Cpha266_0559
            PLT: Plut_1629
            RRS: RoseRS_2753 RoseRS_3110
            RCA: Rcas_2377 Rcas_2967
            DRA: DR_1283
            DGE: Dgeo_0661
            TTH: TTC0260
            TTJ: TTHA0626
            HMA: rrnAC0562(pepC)
            HWA: HQ3197A(pepC)
STRUCTURES  PDB: 1FIY  1JQN  1JQO  1QB4  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.31
            ExPASy - ENZYME nomenclature database: 4.1.1.31
            ExplorEnz - The Enzyme Database: 4.1.1.31
            ERGO genome analysis and discovery system: 4.1.1.31
            BRENDA, the Enzyme Database: 4.1.1.31
            CAS: 9067-77-0
///
ENTRY       EC 4.1.1.32                 Enzyme
NAME        phosphoenolpyruvate carboxykinase (GTP);
            phosphoenolpyruvate carboxylase;
            phosphopyruvate carboxylase;
            phosphopyruvate (guanosine triphosphate) carboxykinase;
            phosphoenolpyruvic carboxykinase (GTP);
            phosphopyruvate carboxylase (GTP);
            phosphoenolpyruvic carboxylase (GTP);
            phosphoenolpyruvic carboxykinase;
            phosphoenolpyruvate carboxykinase;
            PEP carboxylase;
            GTP:oxaloacetate carboxy-lyase (transphosphorylating)
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     GTP:oxaloacetate carboxy-lyase (adding GTP;
            phosphoenolpyruvate-forming)
REACTION    GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2 [RN:R00431]
ALL_REAC    R00431;
            (other) R00726
SUBSTRATE   GTP [CPD:C00044];
            oxaloacetate [CPD:C00036]
PRODUCT     GDP [CPD:C00035];
            phosphoenolpyruvate [CPD:C00074];
            CO2 [CPD:C00011]
COMMENT     ITP can act as phosphate donor.
REFERENCE   1  [PMID:5911620]
  AUTHORS   Chang HC, Lane MD.
  TITLE     The enzymatic carboxylation of phosphoenolpyruvate. II. Purification
            and properties of liver mitochondrial phosphoenolpyruvate
            carboxykinase.
  JOURNAL   J. Biol. Chem. 241 (1966) 2413-20.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:13438893]
  AUTHORS   KURAHASHI K, PENNINGTON RJ, UTTER MF.
  TITLE     Nucleotide specificity of oxalacetic carboxylase.
  JOURNAL   J. Biol. Chem. 226 (1957) 1059-75.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00620  Pyruvate metabolism
            PATH: map03320  PPAR signaling pathway
            PATH: map04910  Insulin signaling pathway
            PATH: map04920  Adipocytokine signaling pathway
ORTHOLOGY   KO: K01596  phosphoenolpyruvate carboxykinase (GTP)
GENES       HSA: 5105(PCK1) 5106(PCK2)
            PTR: 452807(PCK2)
            MMU: 18534(Pck1) 74551(Pck2)
            RNO: 361042(Pck2_predicted) 362282(Pck1)
            CFA: 403560(PCK1) 480255(PCK2)
            BTA: 282855(PCK1) 282856(PCK2)
            GGA: 396457(PEPCK-M) 396458(PCK1)
            XLA: 379637(MGC68864) 379844(pck1) 399424(PCK2)
            XTR: 394790(pck1)
            DRE: 378727(pck1)
            SPU: 584898(LOC584898) 752532(LOC752532)
            DME: Dmel_CG10924 Dmel_CG17725(Pepck)
            DDI: DDB_0230145
            ACI: ACIAD2842(pckG)
            HHA: Hhal_1673
            RSO: RSc0017(pckA)
            REU: Reut_A3420
            REH: H16_A3711(pepck)
            RME: Rmet_3577
            BMA: BMA3042(pckA)
            BMV: BMASAVP1_A1250(pckG)
            BML: BMA10299_A0620(pckG)
            BMN: BMA10247_0533(pckG)
            BXE: Bxe_A4422
            BVI: Bcep1808_4996
            BUR: Bcep18194_B1511
            BCN: Bcen_3922
            BCH: Bcen2424_4445
            BAM: Bamb_3877
            BPS: BPSL1324(pckG)
            BPM: BURPS1710b_1574
            BPL: BURPS1106A_1475(pckG)
            BPD: BURPS668_1446(pckG)
            BTE: BTH_I2808
            PNU: Pnuc_2083
            BPA: BPP1368(pckG)
            BBR: BB2434(pckG)
            POL: Bpro_0160
            PNA: Pnap_0102
            AAV: Aave_0138
            AJS: Ajs_0078
            MPT: Mpe_A3705
            EBA: ebA4040(ppcK)
            AZO: azo0820(pckG)
            DAR: Daro_0665
            GSU: GSU3385(pckA)
            GME: Gmet_2638
            GUR: Gura_0870
            PCA: Pcar_1766
            DPS: DP1093
            ADE: Adeh_3676
            AFW: Anae109_3803
            MXA: MXAN_1264(pckG)
            SFU: Sfum_0901
            SWI: Swit_5171
            RRU: Rru_A3419
            MAG: amb0785
            ABA: Acid345_0537
            CTH: Cthe_2874
            CSC: Csac_0274
            MTU: Rv0211(pckA)
            MTC: MT0221(pckA)
            MBO: Mb0217(pckA)
            MBB: BCG_0248(pckA)
            MLE: ML2624(pckA)
            MPA: MAP3646(pckA)
            MAV: MAV_4963 MAV_5106
            MSM: MSMEG_0255
            MVA: Mvan_0201
            MGI: Mflv_0451
            MMC: Mmcs_0176
            MKM: Mkms_0185
            MJL: Mjls_0165
            CGL: NCgl2765(cgl2863)
            CGB: cg3169(pck)
            CEF: CE2691(pck)
            CDI: DIP2180(pckG)
            CJK: jk0151(pck)
            NFA: nfa54790(pckA)
            RHA: RHA1_ro05180
            SCO: SCO4979(2SCK36.02)
            SMA: SAV3287(pck)
            LXX: Lxx04240(pckG)
            CMI: CMM_1473(pckA)
            ART: Arth_0667
            AAU: AAur_0832
            NCA: Noca_0190 Noca_4168 Noca_4472
            TFU: Tfu_0083
            FRA: Francci3_3897
            FAL: FRAAL6204(pckG)
            KRA: Krad_3537
            SEN: SACE_7274(pckA)
            STP: Strop_0861
            CTR: CT710(pckA)
            CTA: CTA_0772(pckA)
            CMU: TC0083
            CPN: CPn0851(pckA)
            CPA: CP1018
            CPJ: CPj0851(pckA)
            CPT: CpB0880
            CCA: CCA00916(pckA)
            CAB: CAB884
            CFE: CF0098(pckA)
            PCU: pc1371(pckG)
            TPA: TP0122
            CTE: CT2232(pckA)
            CCH: Cag_2012
            CPH: Cpha266_0051
            PVI: Cvib_0027
            PLT: Plut_0023
            RRS: RoseRS_2496
            RCA: Rcas_2846
            TAC: Ta0123
            TVO: TVN0200
            PHO: PH0312
            PAB: PAB1253
            PFU: PF0289
            TKO: TK1405
            SSO: SSO2537
            STO: ST1058
            SAI: Saci_1100
            MSE: Msed_1452
            TPE: Tpen_1532
STRUCTURES  PDB: 1II2  1KHB  1KHE  1KHF  1KHG  1M51  1NHX  2FAF  2FAH  2GMV  
                 2QEW  2QEY  2QF1  2QF2  2QZY  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.32
            ExPASy - ENZYME nomenclature database: 4.1.1.32
            ExplorEnz - The Enzyme Database: 4.1.1.32
            ERGO genome analysis and discovery system: 4.1.1.32
            BRENDA, the Enzyme Database: 4.1.1.32
            CAS: 9013-08-5
///
ENTRY       EC 4.1.1.33                 Enzyme
NAME        diphosphomevalonate decarboxylase;
            pyrophosphomevalonate decarboxylase;
            mevalonate-5-pyrophosphate decarboxylase;
            pyrophosphomevalonic acid decarboxylase;
            5-pyrophosphomevalonate decarboxylase;
            mevalonate 5-diphosphate decarboxylase;
            ATP:(R)-5-diphosphomevalonate carboxy-lyase (dehydrating)
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     ATP:(R)-5-diphosphomevalonate carboxy-lyase (adding ATP;
            isopentenyl-diphosphate-forming)
REACTION    ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl
            diphosphate + CO2 [RN:R01121]
ALL_REAC    R01121
SUBSTRATE   ATP [CPD:C00002];
            (R)-5-diphosphomevalonate [CPD:C01143]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            isopentenyl diphosphate [CPD:C00129];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Bloch, K., Chaykin, S., Phillips, A.H. and de Waard, A.
  TITLE     Mevalonic acid pyrophosphate and isopentenyl pyrophosphate.
  JOURNAL   J. Biol. Chem. 234 (1959) 2595-2604.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K01597  diphosphomevalonate decarboxylase
GENES       HSA: 4597(MVD)
            PTR: 468069(MVD)
            MMU: 192156(Mvd)
            RNO: 81726(Mvd)
            CFA: 489663(MVD)
            GGA: 425359(MVD)
            DME: Dmel_CG8239
            SCE: YNR043W(MVD1)
            AGO: AGOS_AGL232C
            PIC: PICST_90752
            CGR: CAGL0C03630g
            SPO: SPAC24C9.03
            ANI: AN4414.2
            AFM: AFUA_4G07130
            AOR: AO090023000862
            CNE: CNL04950
            UMA: UM05179.1
            DDI: DDBDRAFT_0218058
            TET: TTHERM_00849200
            TBR: Tb10.05.0010 Tb10.61.2745
            TCR: 507993.330 511281.40
            LMA: LmjF18.0020
            CBU: CBU_0607(mvaD)
            CBD: COXBU7E912_0619(mvaD)
            LPN: lpg2040
            LPF: lpl2018
            LPP: lpp2023
            TCX: Tcr_1734
            DNO: DNO_0504(mvaD)
            BBA: Bd1629
            MXA: MXAN_5018(mvaD)
            OIH: OB0226
            SAU: SA0548(mvaD)
            SAV: SAV0591(mvaD)
            SAM: MW0546(mvaD)
            SAR: SAR0597(mvaD)
            SAS: SAS0550
            SAC: SACOL0637(mvaD)
            SAB: SAB0541(mvaD)
            SAA: SAUSA300_0573(mvaD)
            SAO: SAOUHSC_00578
            SAJ: SaurJH9_0614
            SAH: SaurJH1_0629
            SEP: SE0362
            SER: SERP0239(mvaD)
            SHA: SH2401(mvaD)
            SSP: SSP2121
            LMO: lmo0011
            LMF: LMOf2365_0012(mvaD)
            LIN: lin0011
            LWE: lwe0012(mvaD)
            LLA: L9089(yeaH)
            LLC: LACR_0455
            LLM: llmg_0426(mvaD)
            SPY: SPy_0877(mvaD)
            SPZ: M5005_Spy_0683(mvaD)
            SPM: spyM18_0938(mvd)
            SPG: SpyM3_0596(mvaD)
            SPS: SPs1257
            SPH: MGAS10270_Spy0741(mvaD)
            SPI: MGAS10750_Spy0775(mvaD)
            SPJ: MGAS2096_Spy0754(mvaD)
            SPK: MGAS9429_Spy0738(mvaD)
            SPF: SpyM51125(mvaD)
            SPA: M6_Spy0700
            SPB: M28_Spy0663(mvaD)
            SPN: SP_0382
            SPR: spr0339(mvd1)
            SPD: SPD_0347(mvaD)
            SAG: SAG1325(mvaD)
            SAN: gbs1395
            SAK: SAK_1356(mvaD)
            SMU: SMU.937
            STC: str0560(mvaD)
            STL: stu0560(mvaD)
            SSA: SSA_0334(mvaD)
            SGO: SGO_0240(mvaD)
            LPL: lp_1734(mvaD)
            LJO: LJ1206
            LAC: LBA1168(mvaD)
            LSA: LSA0907(mvaD)
            LSL: LSL_0684
            LDB: Ldb0998(mvaD)
            LBU: LBUL_0905
            LBR: LVIS_0859
            LCA: LSEI_1492
            LRE: Lreu_0914
            EFA: EF0903(mvaD)
            NFA: nfa22080
            BBU: BB0686
            BGA: BG0709
            BAF: BAPKO_0730
            GFO: GFO_3632
            FPS: FP0310(mvaD)
            HAL: VNG0593G(dmd)
            HMA: rrnAC1489(dmd)
            HWA: HQ1525A(mvaD)
            NPH: NP1580A(mvaD)
            PTO: PTO0478 PTO1356
            SSO: SSO2989
            STO: ST0977
            SAI: Saci_1245(mvd)
            MSE: Msed_1576
STRUCTURES  PDB: 1FI4  2HK2  2HK3  2HKE  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.33
            ExPASy - ENZYME nomenclature database: 4.1.1.33
            ExplorEnz - The Enzyme Database: 4.1.1.33
            ERGO genome analysis and discovery system: 4.1.1.33
            BRENDA, the Enzyme Database: 4.1.1.33
            CAS: 9024-66-2
///
ENTRY       EC 4.1.1.34                 Enzyme
NAME        dehydro-L-gulonate decarboxylase;
            keto-L-gulonate decarboxylase;
            3-keto-L-gulonate decarboxylase;
            3-dehydro-L-gulonate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     3-dehydro-L-gulonate carboxy-lyase (L-xylulose-forming)
REACTION    3-dehydro-L-gulonate = L-xylulose + CO2 [RN:R01905]
ALL_REAC    R01905
SUBSTRATE   3-dehydro-L-gulonate [CPD:C00618]
PRODUCT     L-xylulose [CPD:C00312];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Smiley, J.D. and Ashwell, G.
  TITLE     Purification and properties of beta-L-hydroxy acid dehydrogenase.
            II. Isolation of beta-keto-L-gluconic acid, an intermediate in
            L-xylulose biosynthesis.
  JOURNAL   J. Biol. Chem. 236 (1961) 357-364.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.34
            ExPASy - ENZYME nomenclature database: 4.1.1.34
            ExplorEnz - The Enzyme Database: 4.1.1.34
            ERGO genome analysis and discovery system: 4.1.1.34
            BRENDA, the Enzyme Database: 4.1.1.34
            CAS: 9024-67-3
///
ENTRY       EC 4.1.1.35                 Enzyme
NAME        UDP-glucuronate decarboxylase;
            uridine-diphosphoglucuronate decarboxylase;
            UDP-D-glucuronate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     UDP-D-glucuronate carboxy-lyase (UDP-D-xylose-forming)
REACTION    UDP-D-glucuronate = UDP-D-xylose + CO2 [RN:R01384]
ALL_REAC    R01384
SUBSTRATE   UDP-D-glucuronate [CPD:C00167]
PRODUCT     UDP-D-xylose [CPD:C00190];
            CO2 [CPD:C00011]
COFACTOR    NAD+ [CPD:C00003]
COMMENT     Requires NAD+.
REFERENCE   1
  AUTHORS   Ankel, H. and Feingold, D.S.
  TITLE     Biosynthesis of uridine diphosphate D-xylose. 1. Uridine diphosphate
            glucuronate carboxy-lyase of wheat germ.
  JOURNAL   Biochemistry 4 (1965) 2468-2475.
  ORGANISM  Triticum aestivum [GN:etae]
PATHWAY     PATH: map00500  Starch and sucrose metabolism
            PATH: map00520  Nucleotide sugars metabolism
ORTHOLOGY   KO: K08678  UDP-glucuronate decarboxylase
GENES       HSA: 80146(UXS1)
            PTR: 470464(UXS1)
            MMU: 67883(Uxs1)
            RNO: 246232(Uxs1)
            CFA: 481318(UXS1)
            BTA: 534788(LOC534788)
            GGA: 418728(UXS1)
            XTR: 448599(uxs1)
            DRE: 192315(uxs1)
            REH: H16_A1425
            SAT: SYN_00531
            MAV: MAV_4084
STRUCTURES  PDB: 2B69  2BLL  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.35
            ExPASy - ENZYME nomenclature database: 4.1.1.35
            ExplorEnz - The Enzyme Database: 4.1.1.35
            ERGO genome analysis and discovery system: 4.1.1.35
            BRENDA, the Enzyme Database: 4.1.1.35
            CAS: 9024-68-4
///
ENTRY       EC 4.1.1.36                 Enzyme
NAME        phosphopantothenoylcysteine decarboxylase;
            4-phosphopantotheoylcysteine decarboxylase;
            4-phosphopantothenoyl-L-cysteine decarboxylase;
            PPC-decarboxylase;
            N-[(R)-4'-phosphopantothenoyl]-L-cysteine carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     N-[(R)-4'-phosphopantothenoyl]-L-cysteine carboxy-lyase
            (pantotheine-4'-phosphate-forming)
REACTION    N-[(R)-4'-phosphopantothenoyl]-L-cysteine = pantotheine 4'-phosphate
            + CO2 [RN:R03269]
ALL_REAC    R03269
SUBSTRATE   N-[(R)-4'-phosphopantothenoyl]-L-cysteine [CPD:C04352]
PRODUCT     pantotheine 4'-phosphate;
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Brown, G.M.
  TITLE     Requirement of cytidine triphosphate for the biosynthesis of
            phosphopantetheine.
  JOURNAL   J. Am. Chem. Soc. 80 (1958) 3161.
  ORGANISM  Proteais morgnnii
REFERENCE   2  [PMID:13630913]
  AUTHORS   BROWN GM.
  TITLE     The metabolism of pantothenic acid.
  JOURNAL   J. Biol. Chem. 234 (1959) 370-8.
  ORGANISM  Acetobacter suboxydans, Lactobacillus helveticus, Lactobacillus
            bulgaricus
PATHWAY     PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K01598  phosphopantothenoylcysteine decarboxylase
GENES       HSA: 60490(PPCDC)
            MMU: 66812(Ppcdc)
            CFA: 487653(PPCDC)
            GGA: 427477(PPCDC)
            XLA: 496003(LOC496003)
            DRE: 393753(ppcdc)
            SPU: 584017(LOC584017)
            DME: Dmel_CG30290
            ATH: AT3G18030(ATHAL3A)
            OSA: 4340408
            ANI: AN4305.2
            AOR: AO090003001332
            TET: TTHERM_00266620
            TBR: Tb927.6.2940
            TCR: 507021.110 511751.210
            LMA: LmjF30.1540
            EHI: 50.t00036
            ECO: b3639(dfp)
            ECE: Z5063(dfp)
            ECS: ECs4514
            ECC: c4463(dfp)
            ECI: UTI89_C4183(dfp)
            ECP: ECP_3737
            ECV: APECO1_2822(dfp)
            ECW: EcE24377A_4140(coaBC)
            ECX: EcHS_A3848(coaBC)
            STY: STY4064(dfp)
            STT: t3788(dfp)
            SPT: SPA3582(dfp)
            SEC: SC3653(dfp)
            STM: STM3730(dfp)
            YPE: YPO0048(dfp)
            YPK: y0093(dfp)
            YPM: YP_0049(dfp)
            YPA: YPA_3494
            YPN: YPN_3802
            YPP: YPDSF_3857
            YPS: YPTB0045(dfp)
            YPI: YpsIP31758_0060(coaBC)
            SFL: SF3678(dfp)
            SFX: S4090(dfp)
            SFV: SFV_3891(dfp)
            SSN: SSON_3767(dfp)
            SBO: SBO_3641(dfp)
            SDY: SDY_4069(dfp)
            ECA: ECA0144(dfp)
            PLU: plu4866(dfp)
            WBR: WGLp402(dfp)
            SGL: SG2209
            ENT: Ent638_0100
            KPN: KPN_03979(dfp)
            SPE: Spro_4843
            BPN: BPEN_637(dfp)
            HIN: HI0953(dfp)
            HIT: NTHI1126(dfp)
            HDU: HD0733(dfp)
            HSO: HS_0143(coaBC)
            PMU: PM1153(dfp)
            MSU: MS1938(dfp)
            APL: APL_1969(dfp)
            ASU: Asuc_0012
            XFA: XF0149
            XFT: PD0118(dfp)
            XCC: XCC3859(dfp)
            XCB: XC_3943
            XCV: XCV4027(dfp)
            XAC: XAC3914(dfp)
            XOO: XOO0496(dfp)
            XOM: XOO_0463(XOO0463)
            VCH: VC0215
            VVU: VV1_0828
            VVY: VV0283
            VPA: VP0181
            VFI: VF0125
            PPR: PBPRA0201
            PAE: PA5320(dfp)
            PAU: PA14_70240(coaC)
            PAP: PSPA7_6096(coaBC)
            PPU: PP_5285(coaBC)
            PPF: Pput_5195
            PST: PSPTO_0085(coaBC)
            PSB: Psyr_0221
            PSP: PSPPH_0209(coaBC)
            PFL: PFL_6052(coaBC)
            PFO: Pfl_5540
            PEN: PSEEN5432(dfp)
            PMY: Pmen_4377
            PAR: Psyc_1833(dfp)
            PCR: Pcryo_2118
            PRW: PsycPRwf_0492
            ACI: ACIAD3125(dfp)
            SON: SO_4249(dfp)
            SDN: Sden_0325
            SFR: Sfri_3829
            SAZ: Sama_0326
            SBL: Sbal_0376
            SBM: Shew185_0375
            SLO: Shew_3482
            SPC: Sputcn32_0461
            SSE: Ssed_0384
            SPL: Spea_3838
            SHE: Shewmr4_3598
            SHM: Shewmr7_0358
            SHN: Shewana3_3771
            SHW: Sputw3181_0337
            ILO: IL0239(dfp)
            CPS: CPS_0182(coaBC)
            PHA: PSHAa2644(dfp)
            PAT: Patl_0045
            PIN: Ping_0057
            MAQ: Maqu_3563
            CBU: CBU_0886(coaBC)
            CBD: COXBU7E912_0950(coaBC)
            LPN: lpg2488
            LPF: lpl2408(dfp)
            LPP: lpp2552(dfp)
            MCA: MCA2784(coaBC)
            FTU: FTT1147c(dfp)
            FTF: FTF1147c(dfp)
            FTW: FTW_1186(coaBC)
            FTL: FTL_0808
            FTH: FTH_0802(dfp)
            FTA: FTA_0854(coaBC)
            FTN: FTN_1128(dfp)
            TCX: Tcr_1915
            NOC: Noc_2992
            AEH: Mlg_2847
            HHA: Hhal_2299
            HCH: HCH_01021(coaBC)
            CSA: Csal_2981
            MMW: Mmwyl1_0623
            AHA: AHA_0159(coaBC)
            BCI: BCI_0183(dfp)
            RMA: Rmag_0801
            VOK: COSY_0727(dfp)
            NME: NMB1658
            NMA: NMA1916
            NGO: NGO1307
            CVI: CV_3080(dfp)
            RSO: RSc2461(dfp)
            REU: Reut_A2747
            REH: H16_A3048(dfp)
            RME: Rmet_2887
            BMA: BMA2244(coaBC)
            BMV: BMASAVP1_A2660(coaBC)
            BML: BMA10299_A1035(coaBC)
            BMN: BMA10247_2114(coaBC)
            BXE: Bxe_A0805
            BUR: Bcep18194_A5846
            BAM: Bamb_2561
            BPS: BPSL0904(dfp)
            BPM: BURPS1710b_1120(coaBC)
            BPL: BURPS1106A_0969(coaBC)
            BPD: BURPS668_0965(coaBC)
            BTE: BTH_I0768(coaBC)
            BPE: BP1751(dfp)
            BPA: BPP1982(dfp)
            BBR: BB2170(dfp)
            RFR: Rfer_2647
            POL: Bpro_3180
            MPT: Mpe_A2571
            HAR: HEAR0843(dfp)
            MMS: mma_0826
            NEU: NE1463(dfp)
            NET: Neut_0783
            NMU: Nmul_A2137
            EBA: ebA838(dfp)
            AZO: azo1138(dfp)
            DAR: Daro_3141
            TBD: Tbd_2587
            MFA: Mfla_0314
            HPA: HPAG1_0826
            CFF: CFF8240_0752(coaBC)
            CCV: CCV52592_1267(coaBC)
            CHA: CHAB381_0969(coaBC)
            ABU: Abu_2203(dfp)
            NIS: NIS_1104(dfp)
            SUN: SUN_1837(dfp)
            GSU: GSU1124(coaBC)
            GME: Gmet_2673
            GUR: Gura_2927
            PCA: Pcar_2011
            PPD: Ppro_0088
            DVU: DVU3353(coaBC)
            DDE: Dde_0039
            LIP: LI0582
            DPS: DP1673
            ADE: Adeh_2372
            AFW: Anae109_1495
            MXA: MXAN_4395(coaBC)
            SAT: SYN_02177
            SFU: Sfum_0467
            AMA: AM1335(dfp)
            APH: APH_1297
            ERU: Erum0410(dfp) Erum6340
            ERW: ERWE_CDS_00300(dfp) ERWE_CDS_06650(dfp)
            ERG: ERGA_CDS_00300(dfp)
            ECN: Ecaj_0033
            ECH: ECH_0061
            PUB: SAR11_0405(dfp)
            MLO: mlr3167
            MES: Meso_4055
            PLA: Plav_3656
            SME: SMc01161(dfp)
            ATU: Atu0316(dfp)
            ATC: AGR_C_552
            RET: RHE_CH00342(dfp)
            RLE: RL0357(coaBC)
            BME: BMEII0235
            BMF: BAB2_1024(coaBC)
            BMS: BRA1064(coaBC)
            BMB: BruAb2_1004(coaBC)
            BOV: BOV_A1001(coaBC)
            OAN: Oant_1319
            BJA: bll0759(dfp)
            BRA: BRADO0077(coaBC)
            BBT: BBta_0083(coaBC)
            RPA: RPA0081(coaBC)
            RPB: RPB_0622
            RPC: RPC_0380
            RPD: RPD_0209
            RPE: RPE_0467
            NWI: Nwi_0043
            NHA: Nham_0051
            BHE: BH00380(dfp)
            BQU: BQ00340(dfp)
            BBK: BARBAKC583_1349(coaBC)
            XAU: Xaut_0078
            CCR: CC_3712
            SIL: SPO0408(coaBC)
            SIT: TM1040_0458
            RSP: RSP_0599
            RSQ: Rsph17025_0484
            JAN: Jann_0907
            RDE: RD1_1200(coaBC)
            HNE: HNE_3268(coaBC)
            ZMO: ZMO1190(dfp)
            SWI: Swit_4880
            GOX: GOX2498
            GBE: GbCGDNIH1_0157
            RRU: Rru_A3796
            MAG: amb0202
            MGM: Mmc1_3420
            ABA: Acid345_3776
            BSU: BG13388(yloI)
            BHA: BH2510(dfp)
            BAN: BA4007(coaBC)
            BAR: GBAA4007(coaBC)
            BAA: BA_4478
            BAT: BAS3720
            BCE: BC3867
            BCA: BCE_3912(coaBC)
            BCZ: BCZK3628(dfp)
            BCY: Bcer98_2521
            BTK: BT9727_3610(dfp)
            BLI: BL02295
            BLD: BLi01791(yloI)
            BCL: ABC2320
            BPU: BPUM_1469(coaBC)
            OIH: OB1504
            GKA: GK1169
            SAU: SA1054
            SAV: SAV1211
            SAM: MW1094
            SAR: SAR1187
            SAS: SAS1145
            SAC: SACOL1223(coaBC)
            SAB: SAB1075
            SAA: SAUSA300_1104(coaBC) SAUSA300_1764(epiD)
            SAO: SAOUHSC_01178
            SEP: SE0887
            SER: SERP0778(coaBC)
            SHA: SH1703
            SSP: SSP1560
            LMO: lmo1825
            LMF: LMOf2365_1853(coaBC)
            LIN: lin1939
            LLM: llmg_0543(dfpA)
            SPZ: M5005_Spy_0936(dfp)
            SPH: MGAS10270_Spy1050(dfp)
            SPI: MGAS10750_Spy1085(dfp)
            SPJ: MGAS2096_Spy0995(dfp)
            SPK: MGAS9429_Spy1039(dfp)
            SPF: SpyM50862(coaC)
            SPA: M6_Spy0925
            SPB: M28_Spy0908(dfp)
            SPD: SPD_1089(coaC)
            SAK: SAK_1153(coaC)
            SSA: SSA_1202(dfp)
            SGO: SGO_1213(coaC)
            LPL: lp_1614(dfp)
            LJO: LJ0902
            LAC: LBA0939
            LSA: LSA0687(dfp)
            LSL: LSL_0613
            LDB: Ldb0811(dfp)
            LBU: LBUL_0739
            LBR: LVIS_0967
            LCA: LSEI_1627
            LRE: Lreu_1174
            PPE: PEPE_0827
            OOE: OEOE_0935
            STH: STH1341
            CAC: CAC1720
            CPE: CPE1746
            CPF: CPF_1999(coaBC)
            CPR: CPR_1717(coaBC)
            CTC: CTC01217
            CNO: NT01CX_2247
            CTH: Cthe_1313
            CDF: CD2587(coaBC)
            CBO: CBO2512(coaBC)
            CBA: CLB_2385(coaBC)
            CBH: CLC_2367(coaBC)
            CBF: CLI_2573(coaBC)
            CKL: CKL_1367(coaBC)
            AMT: Amet_2788
            CHY: CHY_1486(coaBC)
            DSY: DSY2727
            DRM: Dred_1702
            SWO: Swol_1235
            CSC: Csac_2084
            TTE: TTE1509(dfp)
            MTA: Moth_0893
            MMO: MMOB5920(dfp)
            MSY: MS53_0007
            MTU: Rv1391(dfp)
            MTC: MT1436(dfp)
            MBO: Mb1426(dfp)
            MPA: MAP1125(dfp)
            MAV: MAV_3383(coaBC)
            MSM: MSMEG_3054(coaBC)
            MVA: Mvan_2669
            MGI: Mflv_3738
            MMC: Mmcs_2372
            MKM: Mkms_2419
            MJL: Mjls_2413
            CJK: jk1017(dfp)
            NFA: nfa36140(dfp)
            RHA: RHA1_ro07157
            SCO: SCO1477(SC9C5.01c)
            SMA: SAV6873(dfp)
            CMI: CMM_1778(dfpA)
            ART: Arth_2257
            NCA: Noca_2438
            TFU: Tfu_1064
            FRA: Francci3_3193
            FAL: FRAAL5228
            ACE: Acel_1291
            KRA: Krad_2990
            SEN: SACE_2102(dfp)
            STP: Strop_1863
            BAD: BAD_0478
            RXY: Rxyl_0014
            FNU: FN0711
            RBA: RB7087
            BBU: BB0812(dfp)
            BGA: BG0838(dfp)
            BAF: BAPKO_0865(dfp)
            SYG: sync_0352(coaBC)
            SYX: SynWH7803_0351(dfp)
            CYA: CYA_0161(coaBC)
            CYB: CYB_0983(coaBC)
            AVA: Ava_3811
            PMB: A9601_02501(dfp)
            PMC: P9515_02611(dfp)
            PMF: P9303_23871(dfp)
            PMG: P9301_02511(dfp)
            PMH: P9215_02511
            PME: NATL1_03101(dfp)
            BTH: BT_1362
            BFR: BF2979
            BFS: BF2855(dfp)
            PGI: PG1851(coaBC)
            SRU: SRU_0028(coaBC)
            CHU: CHU_3015(coaBC)
            GFO: GFO_0650(coaBC)
            FPS: FP1839
            CTE: CT0207(dfp)
            CCH: Cag_1614
            DET: DET0429(coaBC)
            DEH: cbdb_A383(coaBC)
            DEB: DehaBAV1_0406
            RRS: RoseRS_1561
            RCA: Rcas_3412
            DRA: DR_0579
            DGE: Dgeo_2315
            TTH: TTC1195
            TTJ: TTHA1560
            AAE: aq_815(dfp)
            TMA: TM1687
            FNO: Fnod_1467
            MSI: Msm_1048
            HWA: HQ1683A(dfp)
            NPH: NP1374A(dfp)
STRUCTURES  PDB: 1MVL  1MVN  1QZU  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.36
            ExPASy - ENZYME nomenclature database: 4.1.1.36
            ExplorEnz - The Enzyme Database: 4.1.1.36
            ERGO genome analysis and discovery system: 4.1.1.36
            BRENDA, the Enzyme Database: 4.1.1.36
            CAS: 9024-69-5
///
ENTRY       EC 4.1.1.37                 Enzyme
NAME        uroporphyrinogen decarboxylase;
            uroporphyrinogen III decarboxylase;
            porphyrinogen carboxy-lyase;
            porphyrinogen decarboxylase;
            uroporphyrinogen-III carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     uroporphyrinogen-III carboxy-lyase (coproporphyrinogen-III-forming)
REACTION    uroporphyrinogen III = coproporphyrinogen III + 4 CO2 [RN:R03197]
ALL_REAC    R03197;
            (other) R04972
SUBSTRATE   uroporphyrinogen III [CPD:C01051]
PRODUCT     coproporphyrinogen III [CPD:C03263];
            CO2 [CPD:C00011]
COMMENT     Acts on a number of porphyrinogens.
REFERENCE   1  [PMID:13549492]
  AUTHORS   MAUZERALL D, GRANICK S.
  TITLE     Porphyrin biosynthesis in erythrocytes. III. Uroporphyrinogen and
            its decarboxylase.
  JOURNAL   J. Biol. Chem. 232 (1958) 1141-62.
  ORGANISM  rabbit
REFERENCE   2  [PMID:4984554]
  AUTHORS   Tomio JM, Garcia RC, San Martin de Viale LC, Grinstein M.
  TITLE     Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian
            erythrocytes. Purification and properties.
  JOURNAL   Biochim. Biophys. Acta. 198 (1970) 353-63.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K01599  uroporphyrinogen decarboxylase
GENES       HSA: 7389(UROD)
            MMU: 22275(Urod)
            CFA: 475378(UROD)
            GGA: 424590(UROD)
            XLA: 414506(MGC83088) 444410(MGC82980)
            XTR: 496978(urod)
            DRE: 30617(urod)
            SPU: 579081(LOC579081)
            DME: Dmel_CG1818
            OSA: 4326635 4332771
            CME: CME194C CMP083C
            SCE: YDR047W(HEM12)
            AGO: AGOS_AGL210C
            PIC: PICST_46716(HEM12)
            CGR: CAGL0H08371g
            SPO: SPCC4B3.05c
            ANI: AN2733.2
            AFM: AFUA_1G05060
            AOR: AO090003000803
            CNE: CNB00030
            UMA: UM06159.1
            DDI: DDB_0231418(hemE)
            PFA: PFF0360w
            TET: TTHERM_00047580
            ECO: b3997(hemE)
            ECJ: JW3961(hemE)
            ECE: Z5572(hemE)
            ECS: ECs4920
            ECC: c4954(hemE)
            ECI: UTI89_C3822(hemE)
            ECP: ECP_4210
            ECV: APECO1_2478(hemE)
            ECW: EcE24377A_4540(hemE)
            ECX: EcHS_A4231(hemE)
            STY: STY3718(hemE)
            STT: t3464(hemE)
            SPT: SPA4004(hemE)
            SEC: SC4048(hemE)
            STM: STM4167(hemE)
            YPE: YPO3734(hemE)
            YPK: y0496(hemE)
            YPM: YP_3097(hemE)
            YPA: YPA_3607
            YPN: YPN_0231
            YPP: YPDSF_3732
            YPS: YPTB0294(hemE)
            YPI: YpsIP31758_3849(hemE)
            YEN: YE0297(hemE)
            SFL: SF4069(hemE)
            SFX: S3666(hemE)
            SFV: SFV_4069(hemE)
            SSN: SSON_4170(hemE)
            SBO: SBO_4018(hemE)
            SDY: SDY_3729(hemE)
            ECA: ECA0235(hemE)
            PLU: plu0489(hemE)
            WBR: WGLp508(hemE)
            SGL: SG0138
            ENT: Ent638_0210
            SPE: Spro_0287
            HSO: HS_1540(uroD)
            PMU: PM1734(uroD)
            MSU: MS0183(hemE)
            APL: APL_0112(hemE)
            ASU: Asuc_1982
            XFA: XF1332
            XFT: PD0580(hemE)
            XCC: XCC2844(hemE)
            XCB: XC_1265
            XCV: XCV3163(hemE)
            XAC: XAC3013(hemE)
            XOO: XOO1242(hemE)
            XOM: XOO_1141(XOO1141)
            VCH: VC0332
            VCO: VC0395_A2734(hemE)
            VVU: VV1_1218
            VVY: VV3150
            VPA: VP2916
            VFI: VF2402
            PPR: PBPRA3428
            PAE: PA5034(hemE)
            PAU: PA14_66550(hemE)
            PAP: PSPA7_5771(hemE)
            PPU: PP_5074(hemE)
            PPF: Pput_4947
            PST: PSPTO_5118(hemE)
            PSB: Psyr_0414(hemE)
            PSP: PSPPH_0404(hemE)
            PFL: PFL_0455(hemE)
            PFO: Pfl_0415(hemE)
            PEN: PSEEN0339(hemE)
            PMY: Pmen_0552
            PAR: Psyc_1502(hemE)
            PCR: Pcryo_1681
            PRW: PsycPRwf_1599
            ACI: ACIAD2474(hemE)
            SON: SO_0435(hemE)
            SDN: Sden_0468
            SFR: Sfri_0482
            SAZ: Sama_0387
            SBL: Sbal_0413
            SBM: Shew185_3920
            SLO: Shew_3422
            SPC: Sputcn32_3406
            SSE: Ssed_0440
            SPL: Spea_0427
            SHE: Shewmr4_0439
            SHM: Shewmr7_3590
            SHN: Shewana3_0435 Shewana3_3722
            SHW: Sputw3181_0537
            ILO: IL2306(hemE)
            CPS: CPS_0448(hemE)
            PHA: PSHAa2899(hemE)
            PAT: Patl_0245
            SDE: Sde_2681
            PIN: Ping_3222
            MAQ: Maqu_0836
            CBU: CBU_0275(hemE)
            CBD: COXBU7E912_1818(hemE)
            LPN: lpg2028(hemE)
            LPF: lpl2005(hemE)
            LPP: lpp2010(hemE)
            MCA: MCA0332(hemE)
            FTU: FTT0047(hemE)
            FTF: FTF0047(hemE)
            FTW: FTW_0123(hemE)
            FTL: FTL_1812
            FTH: FTH_1749(hemE)
            FTA: FTA_1919(hemE)
            FTN: FTN_1664(hemE)
            TCX: Tcr_0123
            NOC: Noc_3008
            AEH: Mlg_2765
            HHA: Hhal_1058
            HCH: HCH_05963(hemE)
            CSA: Csal_0116
            ABO: ABO_2227(hemE)
            MMW: Mmwyl1_1118
            AHA: AHA_0778(hemE)
            DNO: DNO_1332(hemE)
            RMA: Rmag_1026
            VOK: COSY_0928(hemE)
            NME: NMB0781
            NMA: NMA0991(hemE)
            NMC: NMC0733(hemE)
            NGO: NGO0362
            CVI: CV_1122(hemE)
            RSO: RSc3303(hemE)
            REU: Reut_A3342
            REH: H16_A3633(hemE)
            RME: Rmet_3491
            BMA: BMA2962(hemE)
            BMV: BMASAVP1_A3349(hemE)
            BML: BMA10299_A1580(hemE)
            BMN: BMA10247_3022(hemE)
            BXE: Bxe_A0044
            BVI: Bcep1808_0120
            BUR: Bcep18194_A3292
            BCN: Bcen_2944
            BCH: Bcen2424_0111
            BAM: Bamb_0101
            BPS: BPSL3391(hemE)
            BPM: BURPS1710b_0170(hemE)
            BPL: BURPS1106A_4036(hemE)
            BPD: BURPS668_3963(hemE)
            BTE: BTH_I3304(hemE)
            PNU: Pnuc_0028
            BPE: BP3291(hemE)
            BPA: BPP4132(hemE)
            BBR: BB4602(hemE)
            RFR: Rfer_0821
            POL: Bpro_4264
            PNA: Pnap_0363
            AAV: Aave_4469
            AJS: Ajs_3861
            VEI: Veis_0010
            MPT: Mpe_A0134
            HAR: HEAR3386(hemE)
            MMS: mma_3607(hemE)
            NEU: NE0445
            NET: Neut_0603
            NMU: Nmul_A0705
            EBA: ebA2822(hemE)
            AZO: azo3979(hemE)
            DAR: Daro_0032(hemE)
            TBD: Tbd_2779
            MFA: Mfla_2666
            HPY: HP0604
            HPJ: jhp0551(hemE)
            HPA: HPAG1_0585
            HHE: HH1873(hemE)
            HAC: Hac_1398(hemE)
            WSU: WS0370(hemE)
            TDN: Tmden_0634
            CJE: Cj1243(hemE)
            CJR: CJE1379(hemE)
            CJJ: CJJ81176_1258(hemE)
            CJU: C8J_1186(hemE)
            CJD: JJD26997_0483(hemE)
            CFF: CFF8240_1456(hemE)
            CCV: CCV52592_1470(hemE)
            CHA: CHAB381_1268(hemE)
            CCO: CCC13826_1013(hemE)
            ABU: Abu_1786(hemE)
            NIS: NIS_0486(hemE)
            SUN: SUN_1613(hemE)
            GSU: GSU3453(hemE)
            GME: Gmet_0016
            GUR: Gura_0015
            PCA: Pcar_0769
            PPD: Ppro_0619
            BBA: Bd3452(hemE)
            DPS: DP1280
            ADE: Adeh_1088
            AFW: Anae109_1128
            MXA: MXAN_5373(hemE)
            RPR: RP885(hemE)
            RTY: RT0877(hemE)
            RCO: RC1374(hemE)
            RFE: RF_1400(hemE)
            RBE: RBE_1429(hemE)
            RAK: A1C_06880(hemE)
            RBO: A1I_07950(hemE)
            RCM: A1E_05675(hemE)
            RRI: A1G_07520(hemE)
            OTS: OTBS_1010(hemE)
            WOL: WD1028(hemE)
            WBM: Wbm0001
            AMA: AM1301(hemE)
            APH: APH_0020(hemE)
            ERU: Erum0180(hemE)
            ERW: ERWE_CDS_00050(hemE)
            ERG: ERGA_CDS_00050(hemE)
            ECN: Ecaj_0010
            ECH: ECH_0030(hemE)
            NSE: NSE_0968(hemE)
            PUB: SAR11_0344(hemE)
            MLO: mll4487
            MES: Meso_3476
            PLA: Plav_1257
            SME: SMc02794(hemE)
            SMD: Smed_3208
            ATU: Atu2835(hemE)
            ATC: AGR_C_5140
            RET: RHE_CH04126(hemE)
            RLE: RL4742(hemE)
            BME: BMEI0001
            BMF: BAB1_2067(hemE)
            BMS: BR2066(hemE)
            BMB: BruAb1_2041(hemE)
            BOV: BOV_1986(hemE)
            OAN: Oant_0854
            BJA: bll2399(hemE)
            BRA: BRADO1875(hemE)
            BBT: BBta_2192(hemE)
            RPA: RPA1509(hemE)
            RPB: RPB_4014
            RPC: RPC_1258
            RPD: RPD_3769
            RPE: RPE_1312
            NWI: Nwi_0977
            NHA: Nham_2936
            XAU: Xaut_1826
            CCR: CC_3763
            SIL: SPO3648(hemE)
            SIT: TM1040_2528
            RSP: RSP_0680(hemE)
            RSH: Rsph17029_2335
            RSQ: Rsph17025_0550
            JAN: Jann_3846
            RDE: RD1_1284(hemE)
            PDE: Pden_3629
            MMR: Mmar10_2973
            HNE: HNE_3568(hemE)
            ZMO: ZMO1998(hemE)
            NAR: Saro_0118
            SAL: Sala_2843
            SWI: Swit_2833
            ELI: ELI_13005
            GOX: GOX1037
            GBE: GbCGDNIH1_0002
            ACR: Acry_2475
            RRU: Rru_A3616
            MAG: amb4550
            MGM: Mmc1_0025
            ABA: Acid345_0693
            SUS: Acid_5202
            BSU: BG10429(hemE)
            BHA: BH1202(hemE)
            BAN: BA1070(hemE)
            BAR: GBAA1070(hemE)
            BAA: BA_1622
            BAT: BAS0999
            BCE: BC1068
            BCA: BCE_1167(hemE)
            BCZ: BCZK0986(hemE)
            BCY: Bcer98_0824
            BTK: BT9727_0984(hemE)
            BLI: BL01072(hemE)
            BLD: BLi01092(hemE)
            BCL: ABC1538(hemE)
            BAY: RBAM_010350(hemE)
            BPU: BPUM_0958(hemE)
            OIH: OB1167(hemE)
            GKA: GK0661
            SAU: SA1652(hemE)
            SAV: SAV1834(hemE)
            SAM: MW1774(hemE)
            SAR: SAR1925(hemE)
            SAS: SAS1755
            SAC: SACOL1889(hemE)
            SAB: SAB1765c(hemE)
            SAA: SAUSA300_1783(hemE)
            SAO: SAOUHSC_01962
            SAJ: SaurJH9_1887
            SAH: SaurJH1_1921
            SEP: SE1513
            SER: SERP1368(hemE)
            SHA: SH1128(hemE)
            SSP: SSP0965
            LMO: lmo2212(hemE)
            LMF: LMOf2365_2245(hemE)
            LIN: lin2315(hemE)
            LWE: lwe2229(hemE)
            CHY: CHY_0483(hemE)
            DSY: DSY0250
            SWO: Swol_0417
            MTU: Rv2678c(hemE)
            MTC: MT2752(hemE)
            MBO: Mb2697c(hemE)
            MBB: BCG_2691c(hemE)
            MLE: ML1043(hemE)
            MPA: MAP2799c(hemE)
            MAV: MAV_3573(hemE)
            MSM: MSMEG_2780(hemE)
            MVA: Mvan_2481
            MGI: Mflv_3919
            MMC: Mmcs_2212
            MKM: Mkms_2258
            MJL: Mjls_2201
            CGL: NCgl0420(hemE)
            CGB: cg0516(hemE)
            CEF: CE0458
            CDI: DIP0407(hemE)
            CJK: jk1075(hemE)
            NFA: nfa37380(hemE)
            RHA: RHA1_ro06858
            SCO: SCO6031(hemE)
            SMA: SAV2228(hemE)
            TWH: TWT735(hemE)
            TWS: TW749(hemE)
            LXX: Lxx01040(hemE)
            CMI: CMM_0587(hemE)
            ART: Arth_2772
            AAU: AAur_2755(hemE)
            PAC: PPA0306
            NCA: Noca_3674
            TFU: Tfu_1899
            FRA: Francci3_1334
            FAL: FRAAL2101(hemE)
            ACE: Acel_1382
            KRA: Krad_1585
            SEN: SACE_1836(hemE)
            STP: Strop_1532
            RBA: RB7803(uroD)
            CTR: CT747(hemE)
            CTA: CTA_0813(hemE)
            CMU: TC0123
            CPN: CPn0890(hemE)
            CPA: CP0976
            CPJ: CPj0890(hemE)
            CPT: CpB0921
            CCA: CCA00878(hemE)
            CAB: CAB844
            CFE: CF0138(hemE)
            PCU: pc1513(hemE)
            LIL: LB016(hemE)
            LIC: LIC20014(hemE)
            LBJ: LBJ_4014(hemE)
            LBL: LBL_4014(hemE)
            SYN: slr0536(hemE)
            SYW: SYNW1495(hemE)
            SYC: syc0463_c(hemE)
            SYF: Synpcc7942_1086
            SYD: Syncc9605_1017
            SYE: Syncc9902_0918
            SYG: sync_1887(hemE)
            SYR: SynRCC307_0919(hemE)
            SYX: SynWH7803_0755(hemE)
            CYA: CYA_0376(hemE)
            CYB: CYB_1861(hemE)
            TEL: tlr0741(hemE)
            GVI: gll3877(hemE)
            ANA: all3909(hemE)
            AVA: Ava_1788
            PMA: Pro1079(hemE)
            PMM: PMM0583(hemE)
            PMT: PMT0445(hemE)
            PMN: PMN2A_0019
            PMI: PMT9312_0583
            PMB: A9601_06391(hemE)
            PMC: P9515_06481(hemE)
            PMF: P9303_18361(hemE)
            PMG: P9301_06091(hemE)
            PMH: P9215_06651(hemE)
            PME: NATL1_06391(hemE)
            TER: Tery_1714
            SRU: SRU_1702(hemE)
            CHU: CHU_0774(hemE)
            GFO: GFO_3226(hemE)
            FJO: Fjoh_0946
            FPS: FP0041(hemE)
            CTE: CT2039(hemE)
            CCH: Cag_0130
            CPH: Cpha266_0174
            PVI: Cvib_1635
            PLT: Plut_1992(hemE)
            RRS: RoseRS_1748
            RCA: Rcas_2028
            DRA: DR_1133
            TTH: TTC0232
            TTJ: TTHA0601
            AAE: aq_334(dcuP)
            MMQ: MmarC5_0839
            TAC: Ta0310
            TVO: TVN1292
            PTO: PTO1413
STRUCTURES  PDB: 1J93  1JPH  1JPI  1JPK  1R3Q  1R3R  1R3S  1R3T  1R3V  1R3W  
                 1R3Y  1URO  2INF  2Q6Z  2Q71  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.37
            ExPASy - ENZYME nomenclature database: 4.1.1.37
            ExplorEnz - The Enzyme Database: 4.1.1.37
            ERGO genome analysis and discovery system: 4.1.1.37
            BRENDA, the Enzyme Database: 4.1.1.37
            CAS: 9024-70-8
///
ENTRY       EC 4.1.1.38                 Enzyme
NAME        phosphoenolpyruvate carboxykinase (diphosphate);
            phosphopyruvate carboxylase;
            phosphoenolpyruvate carboxylase;
            PEP carboxyphosphotransferase;
            PEP carboxykinase;
            phosphopyruvate carboxykinase (pyrophosphate);
            PEP carboxylase;
            phosphopyruvate carboxykinase;
            phosphoenolpyruvic carboxykinase;
            phosphoenolpyruvic carboxylase;
            phosphoenolpyruvate carboxykinase;
            phosphoenolpyruvate carboxytransphosphorylase;
            phosphoenolpyruvate carboxykinase;
            phosphopyruvate carboxykinase;
            phosphoenolpyruvic carboxykinase;
            phosphoenolpyruvic carboxylase;
            PEPCTrP;
            phosphoenolpyruvic carboxykinase (pyrophosphate);
            phosphoenolpyruvic carboxylase (pyrophosphate);
            phosphoenolpyruvate carboxylase;
            phosphoenolpyruvate carboxyphosphotransferase;
            phosphoenolpyruvic carboxytransphosphorylase;
            phosphoenolpyruvate carboxylase (pyrophosphate);
            phosphopyruvate carboxylase (pyrophosphate);
            diphosphate:oxaloacetate carboxy-lyase (transphosphorylating)
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     diphosphate:oxaloacetate carboxy-lyase (transphosphorylating;
            phosphoenolpyruvate-forming)
REACTION    diphosphate + oxaloacetate = phosphate + phosphoenolpyruvate + CO2
            [RN:R00346]
ALL_REAC    R00346
SUBSTRATE   diphosphate [CPD:C00013];
            oxaloacetate [CPD:C00036]
PRODUCT     phosphate [CPD:C00009];
            phosphoenolpyruvate [CPD:C00074];
            CO2 [CPD:C00011]
COMMENT     Also catalyses the reaction: phosphoenolpyruvate + phosphate =
            pyruvate + diphosphate.
REFERENCE   1  [PMID:4288896]
  AUTHORS   Lochmuller H, Wood HG, Davis JJ.
  TITLE     Phosphoenolpyruvate carboxytransphosphorylase. II. Crystallization
            and properties.
  JOURNAL   J. Biol. Chem. 241 (1966) 5678-91.
  ORGANISM  Propionibacterium shermanii
PATHWAY     PATH: map00620  Pyruvate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.38
            ExPASy - ENZYME nomenclature database: 4.1.1.38
            ExplorEnz - The Enzyme Database: 4.1.1.38
            ERGO genome analysis and discovery system: 4.1.1.38
            BRENDA, the Enzyme Database: 4.1.1.38
            CAS: 9013-12-1
///
ENTRY       EC 4.1.1.39                 Enzyme
NAME        ribulose-bisphosphate carboxylase;
            D-ribulose 1,5-diphosphate carboxylase;
            D-ribulose-1,5-bisphosphate carboxylase;
            RuBP carboxylase;
            carboxydismutase;
            diphosphoribulose carboxylase;
            ribulose 1,5-bisphosphate carboxylase;
            ribulose 1,5-bisphosphate carboxylase/oxygenase;
            ribulose 1,5-diphosphate carboxylase;
            ribulose 1,5-diphosphate carboxylase/oxygenase;
            ribulose bisphosphate carboxylase/oxygenase;
            ribulose diphosphate carboxylase;
            ribulose diphosphate carboxylase/oxygenase;
            rubisco;
            3-phospho-D-glycerate carboxy-lyase (dimerizing)
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     3-phospho-D-glycerate carboxy-lyase (dimerizing;
            D-ribulose-1,5-bisphosphate-forming)
REACTION    2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 +
            H2O [RN:R00024]
ALL_REAC    R00024;
            (other) R03140
SUBSTRATE   3-phospho-D-glycerate [CPD:C00197];
            H+ [CPD:C00080]
PRODUCT     D-ribulose 1,5-bisphosphate [CPD:C01182];
            CO2 [CPD:C00011];
            H2O [CPD:C00001]
COFACTOR    Copper [CPD:C00070]
COMMENT     Will utilize O2 instead of CO2, forming 3-phospho-D-glycerate and
            2-phosphoglycolate.
REFERENCE   1  [PMID:4331471]
  AUTHORS   Bowes G, Ogren WL, Hageman RH.
  TITLE     Phosphoglycolate production catalyzed by ribulose diphosphate
            carboxylase.
  JOURNAL   Biochem. Biophys. Res. Commun. 45 (1971) 716-22.
  ORGANISM  Glycine max  [GN:egma], Zea mays [GN:ezma]
REFERENCE   2  [PMID:4310607]
  AUTHORS   Wishnick M, Lane MD, Scrutton MC, Mildvan AS.
  TITLE     The presence of tightly bound copper in ribulose diphosphate
            carboxylase from spinach.
  JOURNAL   J. Biol. Chem. 244 (1969) 5761-3.
  ORGANISM  spinach
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
            PATH: map00710  Carbon fixation
ORTHOLOGY   KO: K01600  ribulose-bisphosphate carboxylase
            KO: K01601  ribulose-bisphosphate carboxylase large chain
            KO: K01602  ribulose-bisphosphate carboxylase small chain
GENES       DME: Dmel_CG3757(y)
            ATH: AT1G67090 AT5G38420 AT5G38430 ArthCp030(rbcL)
            OSA: 3131463(OrsajCp033) 4324237 4328326 4338862 4341443 4352016
            PPF: Pput_1846
            MCA: MCA2743(cbbL) MCA2744(cbbS)
            TCX: Tcr_0424 Tcr_0427 Tcr_0428 Tcr_0838 Tcr_0839
            NOC: Noc_0332 Noc_0333
            AEH: Mlg_1168 Mlg_2836 Mlg_2837
            HHA: Hhal_0467 Hhal_1045 Hhal_1046
            MMW: Mmwyl1_3120
            RMA: Rmag_0701
            VOK: COSY_0653(cbbM)
            REH: H16_B1394(cbbS2) H16_B1395(cbbL2)
            RME: Rmet_1500 Rmet_1501
            BXE: Bxe_B2452 Bxe_B2453
            RFR: Rfer_1391
            POL: Bpro_0093
            PNA: Pnap_1978
            MPT: Mpe_A1478(cbbL) Mpe_A1479(cbbS) Mpe_A2782(cbbL)
                 Mpe_A2783(cbbS)
            NEU: NE1920(cbbS) NE1921(cbbL)
            NET: Neut_0804 Neut_0805
            NMU: Nmul_A0685 Nmul_A0686
            DAR: Daro_3637
            TBD: Tbd_2623(cbbS) Tbd_2624(cbbL) Tbd_2638(cbbM)
            SME: SMb20197(cbbS) SMb20198(cbbL)
            SMD: Smed_3724 Smed_3924 Smed_3925
            RLE: pRL120396(cbbl1)
            OAN: Oant_3067
            BJA: blr2585(cbbL) blr2586(cbbS)
            BRA: BRADO1659(cbbL) BRADO1660(cbbS) BRADO2274(cbbL)
                 BRADO2275(cbbS)
            BBT: BBta_0451(cbbL) BBta_0452(cbbS) BBta_2641(cbbL)
                 BBta_2642(cbbS) BBta_6396(cbbS) BBta_6397(cbbL)
            RPA: RPA1559(cbbL) RPA1560(cbbS) RPA4641(cbbM)
            RPB: RPB_0951 RPB_3963(cbbS) RPB_3964(cbbL)
            RPC: RPC_1327 RPC_1328 RPC_2895
            RPD: RPD_1054 RPD_1548 RPD_1549 RPD_3721 RPD_3722
            RPE: RPE_0422 RPE_1361 RPE_1362 RPE_2686
            NWI: Nwi_1986 Nwi_1987 Nwi_2928 Nwi_2929
            NHA: Nham_3750 Nham_3751 Nham_4049 Nham_4332 Nham_4333
            XAU: Xaut_1917 Xaut_1918 Xaut_2924
            RSP: RSP_1281(cbbS) RSP_1282(cbbL) RSP_3271(rbpL)
            RSH: Rsph17029_2940 Rsph17029_2941 Rsph17029_4004
            RSQ: Rsph17025_2711 Rsph17025_2712
            PDE: Pden_1699 Pden_1700
            ACR: Acry_0824 Acry_0825 Acry_1067
            RRU: Rru_A2400
            MAG: amb2696
            BCY: Bcer98_2735
            SYN: slr0009(rbcL) slr0012(rbcS)
            SYW: SYNW1717(rbcS) SYNW1718(rbcL)
            SYC: syc0129_c(rbcS) syc0130_c(rbcL)
            SYF: Synpcc7942_1426 Synpcc7942_1427
            SYD: Syncc9605_0752 Syncc9605_0753
            SYE: Syncc9902_1613 Syncc9902_1614
            SYG: sync_1966(cbbS) sync_1967(cbbL)
            SYR: SynRCC307_0819(rbcL) SynRCC307_0820(rbcS)
            SYX: SynWH7803_0678(rbcL) SynWH7803_0679(rbcS)
            CYA: CYA_1194(cbbL) CYA_1196(cbbS)
            CYB: CYB_2577(cbbS) CYB_2579(cbbL)
            TEL: tll1504(rbcS) tll1506(rbcL)
            GVI: glr2156(rbcL) glr2158(rbcS)
            ANA: alr1524(rbcL) alr1526(rbcS)
            AVA: Ava_3905 Ava_3907
            PMA: Pro0551(rbcL) Pro0552(rbcS)
            PMM: PMM0550(rbcL) PMM0551(rbcS)
            PMT: PMT1204(rbcS) PMT1205(rbcL)
            PMN: PMN2A_1879 PMN2A_1880
            PMI: PMT9312_0550 PMT9312_0551
            PMB: A9601_06061(rbcL) A9601_06071(rbcS)
            PMC: P9515_06141(rbcL) P9515_06151(rbcS)
            PMF: P9303_08081(rbcL) P9303_08091(rbcS)
            PMG: P9301_05761(rbcL) P9301_05771(rbcS)
            PME: NATL1_06041(rbcL) NATL1_06051(rbcS)
            TER: Tery_4408 Tery_4410
            CPH: Cpha266_2001
            PVI: Cvib_0464
            MJA: MJ1235(rbcL)
            MAC: MA4555(rbcL)
            MBA: Mbar_A0902
            MMA: MM_1249
            MBU: Mbur_2322
            MTP: Mthe_1616
            MHU: Mhun_2315
            MEM: Memar_1325
            MBN: Mboo_1105
            AFU: AF1638(rbcL-2)
            NPH: NP2770A(rbcL)
            PHO: PH0939
            PAB: PAB1580(rbcL)
            PFU: PF1156
            TKO: TK2290
            RCI: RCIX222(rbcL)
            SMR: Smar_1051
            HBU: Hbut_0503
            TPE: Tpen_1227
STRUCTURES  PDB: 1AA1  1AUS  1BWV  1BXN  1EJ7  1GEH  1GK8  1IR1  1IR2  1IWA  
                 1RBA  1RBL  1RBO  1RCO  1RCX  1RLC  1RLD  1RSC  1RUS  1RXO  
                 1SVD  1UPM  1UPP  1UW9  1UWA  1UZD  1UZH  1WDD  2CWX  2CXE  
                 2D69  2RUS  2V63  2V67  2V68  2V69  2V6A  3RUB  4RUB  5RUB  
                 8RUC  9RUB  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.39
            ExPASy - ENZYME nomenclature database: 4.1.1.39
            ExplorEnz - The Enzyme Database: 4.1.1.39
            ERGO genome analysis and discovery system: 4.1.1.39
            BRENDA, the Enzyme Database: 4.1.1.39
            CAS: 9027-23-0
///
ENTRY       EC 4.1.1.40                 Enzyme
NAME        hydroxypyruvate decarboxylase;
            hydroxypyruvate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     hydroxypyruvate carboxy-lyase (glycolaldehyde-forming)
REACTION    hydroxypyruvate = glycolaldehyde + CO2 [RN:R01393]
ALL_REAC    R01393
SUBSTRATE   hydroxypyruvate [CPD:C00168]
PRODUCT     glycolaldehyde [CPD:C00266];
            CO2 [CPD:C00011]
REFERENCE   1  [PMID:14186730]
  AUTHORS   HEDRICK JL, SALLACH HJ.
  TITLE     THE NONOXIDATIVE DECARBOXYLATION OF HYDROXYPYRUVATE IN MAMMALIAN
            SYSTEMS.
  JOURNAL   Arch. Biochem. Biophys. 105 (1964) 261-9.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.40
            ExPASy - ENZYME nomenclature database: 4.1.1.40
            ExplorEnz - The Enzyme Database: 4.1.1.40
            ERGO genome analysis and discovery system: 4.1.1.40
            BRENDA, the Enzyme Database: 4.1.1.40
            CAS: 37289-43-3
///
ENTRY       EC 4.1.1.41                 Enzyme
NAME        methylmalonyl-CoA decarboxylase;
            propionyl-CoA carboxylase;
            propionyl coenzyme A carboxylase;
            methylmalonyl-coenzyme A decarboxylase;
            (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase [incorrect];
            (S)-methylmalonyl-CoA carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     (S)-methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming)
REACTION    (S)-methylmalonyl-CoA = propanoyl-CoA + CO2 [RN:R00923]
ALL_REAC    R00923
SUBSTRATE   (S)-methylmalonyl-CoA [CPD:C00683]
PRODUCT     propanoyl-CoA [CPD:C00100];
            CO2 [CPD:C00011]
COMMENT     The enzyme from Veillonella alcalescens is a biotinyl-protein,
            requires Na+ and acts as a sodium pump.
REFERENCE   1  [PMID:5646172]
  AUTHORS   Galivan JH, Allen SH.
  TITLE     Methylmalonyl coenzyme A decarboxylase. Its role in succinate
            decarboxylation by Micrococcus lactilyticus.
  JOURNAL   J. Biol. Chem. 243 (1968) 1253-61.
  ORGANISM  Micrococcus lactilyticus
REFERENCE   2  [PMID:7070502]
  AUTHORS   Hilpert W, Dimroth P.
  TITLE     Conversion of the chemical energy of methylmalonyl-CoA
            decarboxylation into a Na+ gradient.
  JOURNAL   Nature. 296 (1982) 584-5.
REFERENCE   3  [PMID:2920730]
  AUTHORS   Hoffmann A, Hilpert W, Dimroth P.
  TITLE     The carboxyltransferase activity of the sodium-ion-translocating
            methylmalonyl-CoA decarboxylase of Veillonella alcalescens.
  JOURNAL   Eur. J. Biochem. 179 (1989) 645-50.
  ORGANISM  Veillonella alcalescens
PATHWAY     PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K01603  methylmalonyl-CoA decarboxylase
            KO: K01604  methylmalonyl-CoA decarboxylase alpha chain
            KO: K01605  methylmalonyl-CoA decarboxylase beta chain
            KO: K01606  methylmalonyl-CoA decarboxylase gamma chain
GENES       AFM: AFUA_5G07580
            ECO: b2919(ygfG)
            ECJ: JW2886(ygfG)
            ECE: Z4256(ygfG)
            ECS: ECs3789
            ECX: EcHS_A3077
            SFL: SF2904(ygfG)
            SFX: S3104(ygfG)
            SFV: SFV_2965(ygfG)
            SSN: SSON_3070(ygfG)
            SBO: SBO_3075(ygfG)
            CVI: CV_1805(mmdA)
            SAT: SYN_01398
            RPC: RPC_1055
            GKA: GK2135
            SPY: SPy_1176 SPy_1177 SPy_1183 SPy_1184
            SPZ: M5005_Spy_0896
            SPM: spyM18_1128 spyM18_1129 spyM18_1134 spyM18_1135
            SPG: SpyM3_0824 SpyM3_0825 SpyM3_0830 SpyM3_0831
            SPS: SPs1025 SPs1030 SPs1031
            SPI: MGAS10750_Spy1045 MGAS10750_Spy1046
            SPA: M6_Spy0885 M6_Spy0886 M6_Spy0891 M6_Spy0892
            SPB: M28_Spy0869
            SMU: SMU.1016(bcc)
            LCA: LSEI_1863
            EFA: EF3324 EF3325
            TTE: TTE0252(oadB) TTE1215(oadB2) TTE1798(oadB3)
            CEF: CE0807
            CDI: DIP0740(mmdA) DIP0742
            SCO: SCO5535(SC1C2.16) SCO6284(SC1G7.10)
            PAC: PPA2005
            BTH: BT_1688(bccP)
            BFR: BF1137 BF3291
            BFS: BF1050(mmdB) BF3128(mmdA) BF3130(bcc)
            PGI: PG1608(mmdB) PG1609(mmdC)
            TMA: TM0717
            AFU: AF2216(mmdC) AF2217(mmdA)
            HAL: VNG1529G(mmdA)
            PHO: PH1283 PH1284 PH1287
            PAB: PAB1769(mmdA) PAB1771 PAB1772
            PFU: PF0671 PF0673 PF0674
            TKO: TK1622 TK1624 TK1625
            SSO: SSO2463(ppcB)
            STO: ST0591
            SAI: Saci_0262(pccB)
STRUCTURES  PDB: 1EF8  1EF9  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.41
            ExPASy - ENZYME nomenclature database: 4.1.1.41
            ExplorEnz - The Enzyme Database: 4.1.1.41
            ERGO genome analysis and discovery system: 4.1.1.41
            BRENDA, the Enzyme Database: 4.1.1.41
            CAS: 37289-44-4
///
ENTRY       EC 4.1.1.42                 Enzyme
NAME        carnitine decarboxylase;
            carnitine carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     carnitine carboxy-lyase (2-methylcholine-forming)
REACTION    carnitine = 2-methylcholine + CO2 [RN:R02398]
ALL_REAC    R02398
SUBSTRATE   carnitine [CPD:C00487]
PRODUCT     2-methylcholine [CPD:C02224];
            CO2 [CPD:C00011]
COFACTOR    ATP [CPD:C00002]
COMMENT     Requires ATP.
REFERENCE   1  [PMID:6016331]
  AUTHORS   Khairallah EA, Wolf G.
  TITLE     Carnitine decarboxylase. The conversion of carnitine to
            beta-methylcholine.
  JOURNAL   J. Biol. Chem. 242 (1967) 32-9.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.42
            ExPASy - ENZYME nomenclature database: 4.1.1.42
            ExplorEnz - The Enzyme Database: 4.1.1.42
            ERGO genome analysis and discovery system: 4.1.1.42
            BRENDA, the Enzyme Database: 4.1.1.42
            CAS: 37237-38-0
///
ENTRY       EC 4.1.1.43                 Enzyme
NAME        phenylpyruvate decarboxylase;
            phenylpyruvate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     phenylpyruvate carboxy-lyase (phenylacetaldehyde-forming)
REACTION    phenylpyruvate = phenylacetaldehyde + CO2 [RN:R01377]
ALL_REAC    R01377;
            (other) R01974
SUBSTRATE   phenylpyruvate [CPD:C00166]
PRODUCT     phenylacetaldehyde [CPD:C00601];
            CO2 [CPD:C00011]
COMMENT     Also acts on (indol-3-yl)pyruvate.
REFERENCE   1  [PMID:4303395]
  AUTHORS   Asakawa T, Wada H, Yamano T.
  TITLE     Enzymatic conversion of phenylpyruvate to phenylacetate.
  JOURNAL   Biochim. Biophys. Acta. 170 (1968) 375-91.
  ORGANISM  Acromobacter eurydice
PATHWAY     PATH: map00360  Phenylalanine metabolism
            PATH: map00380  Tryptophan metabolism
STRUCTURES  PDB: 2NXW  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.43
            ExPASy - ENZYME nomenclature database: 4.1.1.43
            ExplorEnz - The Enzyme Database: 4.1.1.43
            ERGO genome analysis and discovery system: 4.1.1.43
            BRENDA, the Enzyme Database: 4.1.1.43
            CAS: 37289-45-5
///
ENTRY       EC 4.1.1.44                 Enzyme
NAME        4-carboxymuconolactone decarboxylase;
            gamma-4-carboxymuconolactone decarboxylase;
            4-carboxymuconolactone carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     2-carboxy-2,5-dihydro-5-oxofuran-2-acetate carboxy-lyase
            (4,5-dihydro-5-oxofuran-2-acetate-forming)
REACTION    2-carboxy-2,5-dihydro-5-oxofuran-2-acetate =
            4,5-dihydro-5-oxofuran-2-acetate + CO2 [RN:R03470]
ALL_REAC    R03470
SUBSTRATE   2-carboxy-2,5-dihydro-5-oxofuran-2-acetate [CPD:C01278]
PRODUCT     4,5-dihydro-5-oxofuran-2-acetate [CPD:C03586];
            CO2 [CPD:C00011]
REFERENCE   1  [PMID:5330966]
  AUTHORS   Ornston LN.
  TITLE     The conversion of catechol and protocatechuate to beta-ketoadipate
            by Pseudomonas putida. 3. Enzymes of the catechol pathway.
  JOURNAL   J. Biol. Chem. 241 (1966) 3795-9.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2
  AUTHORS   Ornston, L.N.
  TITLE     Conversion of catechol and protocatechuate to beta-ketoadipate
            (Pseudomonas putida).
  JOURNAL   Methods Enzymol. 17A (1970) 529-549.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
ORTHOLOGY   KO: K01607  4-carboxymuconolactone decarboxylase
GENES       YPE: YPO1999 YPO3649
            YPK: y0218 y2310
            YPM: YP_1846 YP_3898
            YPA: YPA_1381 YPA_3662
            YPN: YPN_1479 YPN_3522
            YPS: YPTB1991 YPTB3581
            SPE: Spro_2504
            MSU: MS0180
            XCC: XCC0371(pcaC)
            XCB: XC_0383
            XCV: XCV0385(pcaC) XCV2352
            XAC: XAC0371(pcaC)
            XOO: XOO0486(pcaC)
            XOM: XOO_0453(XOO0453)
            VPA: VPA1141
            PPR: PBPRA1967
            PAE: PA0232(pcaC) PA4486
            PAU: PA14_02850(pcaC) PA14_58220
            PAP: PSPA7_0318(pcaC)
            PPU: PP_1381(pcaC) PP_3648
            PPF: Pput_4342
            PST: PSPTO_2342(pcaC-1) PSPTO_4478(pcaC-2)
            PSB: Psyr_2126 Psyr_4169
            PSP: PSPPH_2100(pcaC1) PSPPH_4178(pcaC2)
            PFL: PFL_0890(pcaC) PFL_1325(pcaC)
            PFO: Pfl_0832 Pfl_1275 Pfl_3235
            PEN: PSEEN1068 PSEEN1169(pcaC) PSEEN2030
            PAR: Psyc_0750
            PCR: Pcryo_0745
            ACI: ACIAD1710(pcaC) ACIAD2278 ACIAD2538
            SON: SO_0083
            SFR: Sfri_3646 Sfri_3873
            SHE: Shewmr4_0089 Shewmr4_3382
            SHM: Shewmr7_0571
            SHN: Shewana3_3552
            CPS: CPS_1326(pcaC) CPS_3139
            AHA: AHA_1548(pcaC)
            CVI: CV_3288(pcaC)
            RSO: RS03072(RSp1472) RSc2249(pcaC)
            REU: Reut_A0521 Reut_B5022 Reut_B5696
            REH: H16_A0535 H16_B2288(pcaCD)
            RME: Rmet_4016
            BMA: BMA1373 BMAA1291(pcaC) BMAA2093
            BMV: BMASAVP1_0268(pcaC)
            BML: BMA10299_0538(pcaC)
            BMN: BMA10247_A0060(pcaC-2) BMA10247_A1029(pcaC-1)
                 BMA10247_A2386(pcaC-3)
            BXE: Bxe_A2370 Bxe_B0647(pcaC) Bxe_B0976 Bxe_B1965 Bxe_C0504
            BUR: Bcep18194_A5144 Bcep18194_B1956 Bcep18194_B2446
                 Bcep18194_B3125
            BCN: Bcen_4279 Bcen_4700 Bcen_5109 Bcen_6236
            BCH: Bcen2424_1843 Bcen2424_3662 Bcen2424_4087 Bcen2424_5750
            BAM: Bamb_1781 Bamb_4316 Bamb_5021
            BPS: BPSL1488 BPSS0047(pcaC) BPSS0939 BPSS2332
            BPM: BURPS1710b_2385 BURPS1710b_A1482(pcaC) BURPS1710b_A1557(pcaC)
                 BURPS1710b_A2542(pcaC)
            BPL: BURPS1106A_2398(pcaC) BURPS1106A_A0058(pcaC)
                 BURPS1106A_A3153(pcaC)
            BPD: BURPS668_2355(pcaC) BURPS668_A0071(pcaC) BURPS668_A3267(pcaC)
            BTE: BTH_I2127 BTH_I2209 BTH_II0050(pcaC) BTH_II1458 BTH_II2352
            BPE: BP0231(pcaC)
            BPA: BPP0880 BPP3636(pcaC)
            BBR: BB0973 BB1075 BB4071(pcaC)
            POL: Bpro_1856 Bpro_1901
            AZO: azo2506(cmd) azo2959 azo3958(pcaC)
            DAR: Daro_2931
            HHE: HH1468
            GSU: GSU1313
            SAT: SYN_02871
            MLO: mlr7207
            MES: Meso_2049 Meso_2527 Meso_2960
            SME: SMb20578(pcaC)
            SMD: Smed_4207
            ATU: Atu4541(pcaC) Atu5225
            ATC: AGR_L_653 AGR_pAT_316
            RET: RHE_PD00084(pcaCd2) RHE_PD00115(pcaCd1) RHE_PE00058(pcaCe)
                 RHE_PF00193(pcaCf)
            RLE: RL2355 pRL110088(pcaC) pRL90120
            BME: BMEII0637
            BMF: BAB2_0597(pcaC)
            BMS: BRA0644(pcaC)
            BMB: BruAb2_0582(pcaC)
            BOV: BOV_A0606(pcaC)
            BJA: bll1385(pcaC) blr5669(pcaC) bsl4577
            BRA: BRADO5848(pcaC)
            BBT: BBta_0837 BBta_1984(pcaC)
            RPA: RPA4740(pcaC)
            RPB: RPB_0830 RPB_1568
            RPD: RPD_0939
            RPE: RPE_4839
            CCR: CC_2411
            SIL: SPO1589 SPO2768 SPOA0045(pcaC) SPOA0346
            SIT: TM1040_0559 TM1040_0755
            RSP: RSP_2524
            JAN: Jann_1592 Jann_4162
            RDE: RD1_2437 RD1_3274 RD1_3773(pcaC)
            HNE: HNE_0019
            GBE: GbCGDNIH1_0525 GbCGDNIH1_0956
            MAG: amb3965
            BCA: BCE_2858
            BCZ: BCZK1757(pcaC) BCZK2554
            BTL: BALH_1719(pcaC)
            BCL: ABC2008
            BPU: BPUM_0541
            LWE: lwe0628
            LLA: L35675(pcaC)
            LLC: LACR_1625 LACR_2239
            LLM: llmg_2230(pcaC)
            LPL: lp_2852
            LSA: LSA1190 LSA1776
            LCA: LSEI_1214
            CBA: CLB_1759(pcaC-1) CLB_1921(pcaC-2)
            CBH: CLC_1766(pcaC-1) CLC_1927(pcaC-2)
            CBF: CLI_1819(pcaC-1) CLI_2047(pcaC-2)
            MTU: Rv0771
            MBO: Mb0794
            MBB: BCG_0823
            MPA: MAP0745c
            MAV: MAV_0716(pcaC) MAV_0906(pcaC) MAV_1392(pcaC) MAV_2020(pcaC)
                 MAV_2164(pcaC) MAV_2165(pcaC) MAV_2831(pcaC) MAV_3238(pcaC)
                 MAV_3552(pcaC) MAV_3958(pcaC) MAV_4685(pcaC)
            MSM: MSMEG_0905(pcaC) MSMEG_2530(pcaC) MSMEG_2604(pcaC)
                 MSMEG_3562(pcaC) MSMEG_5814(pcaC) MSMEG_5856(pcaC)
                 MSMEG_6370(pcaC)
            MMC: Mmcs_1701 Mmcs_4575
            CGL: NCgl2310(cgl2393) NCgl2312(cgl2395)
            CGB: cg2626(pcaL)
            CEF: CE2296 CE2298
            RHA: RHA1_ro01338(pcaL) RHA1_ro02550(pcaC) RHA1_ro04660
            SCO: SCO6697(pcaL)
            SMA: SAV1706(pcaL1) SAV6757
            AAU: AAur_4040(pcaC)
            SEN: SACE_3510(pcaC)
            RXY: Rxyl_1577
            SYD: Syncc9605_0521
            SRU: SRU_2774(pcaC)
            DRA: DR_0973 DR_1204
            DGE: Dgeo_0717
            TTH: TTC1144
            TTJ: TTHA1508
            MMA: MM_0143 MM_0918
            MTH: MTH234
            RCI: LRC178(cmd-1) RCIX2594(cmd-2) RRC209(cmd-3)
            SSO: SSO2884(pcaC)
            SAI: Saci_1814
STRUCTURES  PDB: 2AF7  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.44
            ExPASy - ENZYME nomenclature database: 4.1.1.44
            ExplorEnz - The Enzyme Database: 4.1.1.44
            ERGO genome analysis and discovery system: 4.1.1.44
            BRENDA, the Enzyme Database: 4.1.1.44
            CAS: 37289-46-6
///
ENTRY       EC 4.1.1.45                 Enzyme
NAME        aminocarboxymuconate-semialdehyde decarboxylase;
            picolinic acid carboxylase;
            picolinic acid decarboxylase;
            alpha-amino-beta-carboxymuconate-epsilon-semialdehade decarboxylase;
            alpha-amino-beta-carboxymuconate-epsilon-semialdehyde
            beta-decarboxylase;
            2-amino-3-(3-oxoprop-2-enyl)but-2-enedioate carboxy-lyase;
            2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate carboxy-lyase
            (2-aminomuconate-semialdehyde-forming)
REACTION    2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate = 2-aminomuconate
            semialdehyde + CO2 [RN:R04323]
ALL_REAC    R04323
SUBSTRATE   2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate [CPD:C04409]
PRODUCT     2-aminomuconate semialdehyde [CPD:C03824];
            CO2 [CPD:C00011]
COMMENT     Product rearranges non-enzymically to picolinate.
REFERENCE   1  [PMID:14275130]
  AUTHORS   ICHIYAMA A, NAKAMURA S, KAWAI H, HONJO T, NISHIZUKA Y, HAYAISHI O,
            SENOH S.
  TITLE     STUDIES ON THE METABOLISM OF THE BENZENE RING OF TRYPTOPHAN IN
            MAMMALIAN TISSUES. II. ENZYMIC FORMATION OF ALPHA-AMINOMUCONIC ACID
            FROM 3-HYDROXYANTHRANILIC ACID.
  JOURNAL   J. Biol. Chem. 240 (1965) 740-9.
  ORGANISM  cat
PATHWAY     PATH: map00380  Tryptophan metabolism
ORTHOLOGY   KO: K03392  aminocarboxymuconate-semialdehyde decarboxylase
GENES       HSA: 130013(ACMSD)
            RNO: 171385(Acmsd)
            GGA: 424288(ACMSD)
            AFM: AFUA_2G17440
            DDI: DDBDRAFT_0218836
            PAT: Patl_0847
            REU: Reut_B5503
            REH: H16_B0330(acmD)
            RME: Rmet_5212
            BXE: Bxe_C0621 Bxe_C0650
            BVI: Bcep1808_6383
            BUR: Bcep18194_B2954 Bcep18194_C7640
            BCH: Bcen2424_0158
            BAM: Bamb_4307
            AZO: azo2542(fldW)
            MXA: MXAN_0918
            SWI: Swit_3524
            MJL: Mjls_4213
            RXY: Rxyl_2240
STRUCTURES  PDB: 2F6K  2HBV  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.45
            ExPASy - ENZYME nomenclature database: 4.1.1.45
            ExplorEnz - The Enzyme Database: 4.1.1.45
            ERGO genome analysis and discovery system: 4.1.1.45
            BRENDA, the Enzyme Database: 4.1.1.45
            CAS: 37289-47-7
///
ENTRY       EC 4.1.1.46                 Enzyme
NAME        o-pyrocatechuate decarboxylase;
            2,3-dihydroxybenzoate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     2,3-dihydroxybenzoate carboxy-lyase (catechol-forming)
REACTION    2,3-dihydroxybenzoate = catechol + CO2 [RN:R00821]
ALL_REAC    R00821
SUBSTRATE   2,3-dihydroxybenzoate [CPD:C00196]
PRODUCT     catechol [CPD:C00090];
            CO2 [CPD:C00011]
REFERENCE   1  [PMID:6066253]
  AUTHORS   Rao PV, Moore K, Towers GH.
  TITLE     O-pyrocatechiuc acid carboxy-lyase from Aspergillus niger.
  JOURNAL   Arch. Biochem. Biophys. 122 (1967) 466-73.
  ORGANISM  Aspergillus niger
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00629  Carbazole degradation
GENES       ANG: An07g02050(dhbD)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.46
            ExPASy - ENZYME nomenclature database: 4.1.1.46
            ExplorEnz - The Enzyme Database: 4.1.1.46
            ERGO genome analysis and discovery system: 4.1.1.46
            BRENDA, the Enzyme Database: 4.1.1.46
            CAS: 37289-48-8
///
ENTRY       EC 4.1.1.47                 Enzyme
NAME        tartronate-semialdehyde synthase;
            tartronate semialdehyde carboxylase;
            glyoxylate carbo-ligase;
            glyoxylic carbo-ligase;
            hydroxymalonic semialdehyde carboxylase;
            tartronic semialdehyde carboxylase;
            glyoxalate carboligase;
            glyoxylate carboxy-lyase (dimerizing)
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     glyoxylate carboxy-lyase (dimerizing;
            tartronate-semialdehyde-forming)
REACTION    2 glyoxylate = tartronate semialdehyde + CO2 [RN:R00013]
ALL_REAC    R00013
SUBSTRATE   glyoxylate [CPD:C00048]
PRODUCT     tartronate semialdehyde [CPD:C01146];
            CO2 [CPD:C00011]
COFACTOR    FAD [CPD:C00016];
            Thiamin diphosphate [CPD:C00068]
COMMENT     A flavoprotein.
REFERENCE   1  [PMID:14257608]
  AUTHORS   GUPTA NK, VENNESLAND B.
  TITLE     GLYOXYLATE CARBOLIGASE OF ESCHERICHIA COLI: A FLAVOPROTEIN.
  JOURNAL   J. Biol. Chem. 239 (1964) 3787-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:13363977]
  AUTHORS   BARKULIS SS, KRAKOW G.
  TITLE     Conversion of glyoxylate to hydroxypyruvate by extracts of
            Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 21 (1956) 593-4.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K01608  tartronate-semialdehyde synthase
GENES       ECO: b0507(gcl)
            ECJ: JW0495(gcl)
            ECE: Z0661(gcl)
            ECS: ECs0568
            ECC: c0622(gcl)
            ECI: UTI89_C0536(gcl)
            ECP: ECP_0568
            ECV: APECO1_1507(gcl)
            ECW: EcE24377A_0544(gcl)
            ECX: EcHS_A0488(thiL) EcHS_A0581(gcl)
            STY: STY0565(gcl)
            STT: t2343(gcl)
            SPT: SPA2205(gcl)
            STM: STM0517(gcl)
            SFL: SF0446(gcl)
            SFX: S0453(gcl)
            SFV: SFV_0474(gcl)
            SBO: SBO_0411(gcl)
            SDY: SDY_0395(gcl)
            PPR: PBPRA2275
            PAE: PA1502(gcl)
            PAU: PA14_45000(gcl)
            PAP: PSPA7_3829(gcl)
            PPU: PP_4297(gcl)
            PFL: PFL_1701(gcl)
            PFO: Pfl_1598
            PEN: PSEEN1672(gcl)
            RSO: RSc3281(gcl)
            REU: Reut_A3291
            REH: H16_A3598
            RME: Rmet_3448
            BXE: Bxe_A2460
            BUR: Bcep18194_A5178
            BCN: Bcen_6201
            BCH: Bcen2424_1878
            BAM: Bamb_1815
            BPS: BPSL1452(gcl)
            BPM: BURPS1710b_2424(gcl)
            BPL: BURPS1106A_2299(gcl)
            BPD: BURPS668_2259(gcl)
            BTE: BTH_I2173(gcl)
            POL: Bpro_4561
            HAR: HEAR0332(gcl)
            MMS: mma_0379(gcl)
            MLO: mlr0251
            SME: SMb20681(gcl)
            BJA: blr3166(gcl)
            BRA: BRADO4946(gcl)
            DSY: DSY4166
            MSM: MSMEG_5476(gcl)
            RHA: RHA1_ro02574 RHA1_ro03223
            SCO: SCO6201(SC2G5.22)
            SMA: SAV2028(gcl)
            AAU: AAur_3508(gcl)
            SEN: SACE_1935(gcl) SACE_6729(gcl)
            RXY: Rxyl_2853
            DGE: Dgeo_2612
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.47
            ExPASy - ENZYME nomenclature database: 4.1.1.47
            ExplorEnz - The Enzyme Database: 4.1.1.47
            ERGO genome analysis and discovery system: 4.1.1.47
            BRENDA, the Enzyme Database: 4.1.1.47
            CAS: 9027-24-1
///
ENTRY       EC 4.1.1.48                 Enzyme
NAME        indole-3-glycerol-phosphate synthase;
            indoleglycerol phosphate synthetase;
            indoleglycerol phosphate synthase;
            indole-3-glycerophosphate synthase;
            1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
            carboxy-lyase (cyclizing)
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
            carboxy-lyase [cyclizing;
            1-C-(indol-3-yl)glycerol-3-phosphate-forming]
REACTION    1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate =
            1-C-(indol-3-yl)-glycerol 3-phosphate + CO2 + H2O [RN:R03508]
ALL_REAC    R03508
SUBSTRATE   1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
PRODUCT     1-C-(indol-3-yl)-glycerol 3-phosphate;
            CO2 [CPD:C00011];
            H2O [CPD:C00001]
COFACTOR    Pyruvate [CPD:C00022]
COMMENT     In some organisms, this enzyme is part of a multifunctional protein,
            together with one or more other components of the system for the
            biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate
            phosphoribosyltransferase), EC 4.1.3.27 (anthranilate synthase), EC
            4.2.1.20 (tryptophan synthase) and EC 5.3.1.24
            (phosphoribosylanthranilate isomerase)].
REFERENCE   1  [PMID:5332729]
  AUTHORS   Creighton TE, Yanofsky C.
  TITLE     Indole-3-glycerol phosphate synthetase of Escherichia coli, an
            enzyme of the tryptophan operon.
  JOURNAL   J. Biol. Chem. 241 (1966) 4616-24.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Creighton, T.E. and Yanofsky, C.
  TITLE     Chorismate to tryptophan (Escherichia coli) - Anthranilate
            synthetase, PR transferase, PRA isomerase, InGP synthetase,
            tryptophan synthetase.
  JOURNAL   Methods Enzymol. 17A (1970) 365-380.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:16526091]
  AUTHORS   Kung CC, Huang WN, Huang YC, Yeh KC.
  TITLE     Proteomic survey of copper-binding proteins in Arabidopsis roots by
            immobilized metal affinity chromatography and mass spectrometry.
  JOURNAL   Proteomics. 6 (2006) 2746-58.
  ORGANISM  Arabidopsis thaliana [GN:ath]
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
            PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K01609  indole-3-glycerol phosphate synthase
GENES       ATH: AT2G04400 AT5G48220
            OSA: 4336102 4345257 4346529
            CME: CMJ081C CMT240C
            SCE: YKL211C(TRP3)
            AGO: AGOS_AER446W
            PIC: PICST_91065(TRP6)
            CGR: CAGL0F00253g
            SPO: SPBC1539.09c(trp1)
            AFM: AFUA_1G13090
            AOR: AO090012000581
            ANG: An08g06080(trpC)
            CNE: CNI00560
            UMA: UM02376.1
            ECO: b1262(trpC)
            ECJ: JW1254(trpC)
            ECE: Z2549(trpC)
            ECS: ECs1834
            ECI: UTI89_C1531(trpC)
            ECP: ECP_1310
            ECV: APECO1_423(trpC)
            ECW: EcE24377A_1461(trpC)
            ECX: EcHS_A1371(trpC)
            STY: STY1326(trpC)
            STT: t1637(trpC)
            SPT: SPA1152(trpC)
            SEC: SC1721(trpC)
            STM: STM1725(trpC)
            YPE: YPO2205(trpC)
            YPK: y2049(trpC)
            YPM: YP_2003(trpC)
            YPA: YPA_1565
            YPN: YPN_1674
            YPP: YPDSF_0928
            YPS: YPTB2127(trpC)
            YPI: YpsIP31758_1935(trpC)
            SFL: SF1265(trpC)
            SFX: S1351(trpC)
            SFV: SFV_1276(trpC)
            SSN: SSON_1881(trpC)
            SBO: SBO_1804(trpC)
            SDY: SDY_1330(trpC)
            ECA: ECA2299(trpC)
            PLU: plu2465(trpC)
            BUC: BU279(trpC)
            BAS: BUsg268(trpC)
            BAB: bbp259(trpC)
            SGL: SG1399
            ENT: Ent638_2206
            KPN: KPN_01255(trpC)
            SPE: Spro_2670
            BFL: Bfl429(trpC)
            BPN: BPEN_441(trpC)
            HIN: HI1389.1(trpC)
            HIT: NTHI1763(trpC)
            PMU: PM0580(trpC)
            MSU: MS1152(trpC)
            APL: APL_0859(trpCF)
            ASU: Asuc_1269
            XFA: XF0213
            XFT: PD0173(trpC)
            XCC: XCC0470(trpC)
            XCB: XC_0484
            XCV: XCV0517(trpC)
            XAC: XAC0481(trpC)
            XOO: XOO4160(trpC)
            XOM: XOO_3935(XOO3935)
            VCH: VC1171
            VCO: VC0395_A0793(trpC)
            VVU: VV1_3067
            VVY: VV1218
            VPA: VP1959(trpF)
            VFI: VF1029(trpC)
            PPR: PBPRA2489(trpC)
            PAE: PA0651(trpC)
            PAU: PA14_08360(trpC)
            PPU: PP_0422(trpC)
            PPF: Pput_0455
            PST: PSPTO_0594(trpC)
            PSB: Psyr_0756 Psyr_4579(trpC)
            PSP: PSPPH_0674(trpC)
            PFL: PFL_5621(trpC)
            PFO: Pfl_5113(trpC)
            PEN: PSEEN0449(trpC)
            PMY: Pmen_3944
            PAR: Psyc_0972(trpC)
            PCR: Pcryo_1443
            PRW: PsycPRwf_1648
            ACI: ACIAD2463(trpC)
            SON: SO_3022(trpC)
            SDN: Sden_2453
            SFR: Sfri_1426
            SAZ: Sama_2132
            SBL: Sbal_2704
            SBM: Shew185_2725
            SLO: Shew_2254
            SPC: Sputcn32_2406
            SSE: Ssed_1683
            SPL: Spea_1587
            SHE: Shewmr4_1459
            SHM: Shewmr7_1525
            SHN: Shewana3_1517
            SHW: Sputw3181_1602
            ILO: IL1754(trpC)
            CPS: CPS_3525(trpC)
            PHA: PSHAa1290(trpCF)
            PAT: Patl_2832
            SDE: Sde_0754
            PIN: Ping_1057
            MAQ: Maqu_3520
            CBU: CBU_1154(trpC)
            CBD: COXBU7E912_1252(trpC)
            LPN: lpg0833(trpC)
            LPF: lpl0864(trpC)
            LPP: lpp0895(trpC)
            MCA: MCA2587
            FTU: FTT1795c(trpC)
            FTF: FTF1795c(trpC)
            FTW: FTW_2017(trpCF)
            FTL: FTL_1958
            FTH: FTH_1875(trpC)
            FTA: FTA_2071
            FTN: FTN_1770
            TCX: Tcr_0269
            NOC: Noc_2497
            AEH: Mlg_2247
            HHA: Hhal_2079
            HCH: HCH_06128
            CSA: Csal_2319
            ABO: ABO_2024(trpC)
            MMW: Mmwyl1_1063
            AHA: AHA_2926(trpCF)
            DNO: DNO_0585(trpC)
            RMA: Rmag_0832
            VOK: COSY_0756
            NME: NMB0275
            NMA: NMA2212(trpC)
            NMC: NMC0270(trpC)
            NGO: NGO1721
            CVI: CV_2712(trpC) CV_2763(trpF)
            RSO: RSc2885(trpC1) RSp0680(trpC2)
            REU: Reut_A3026
            REH: H16_A3322(trpC)
            RME: Rmet_3181
            BMA: BMAA0530(trpC)
            BMV: BMASAVP1_0647(trpC)
            BML: BMA10299_0943(trpC)
            BMN: BMA10247_A1913(trpC)
            BXE: Bxe_A0458
            BVI: Bcep1808_0508
            BUR: Bcep18194_A3618
            BCN: Bcen_2574
            BCH: Bcen2424_0531
            BAM: Bamb_0436
            BPS: BPSL3053(trpC)
            BPM: BURPS1710b_3578(trpC)
            BPL: BURPS1106A_3586(trpC)
            BPD: BURPS668_3559(trpC)
            BTE: BTH_I2912(trpC)
            PNU: Pnuc_0145
            BPE: BP3261(trpC)
            BPA: BPP4159(trpC)
            BBR: BB4629(trpC)
            RFR: Rfer_3601
            POL: Bpro_4451
            PNA: Pnap_3649
            AAV: Aave_0586
            AJS: Ajs_0370
            VEI: Veis_1209
            MPT: Mpe_A3460
            HAR: HEAR0197(trpC)
            MMS: mma_0232(trpC)
            NEU: NE0012(trpC)
            NET: Neut_0133
            NMU: Nmul_A2562
            EBA: ebA4201(trpC)
            AZO: azo3322(trpC)
            DAR: Daro_3475
            TBD: Tbd_2222
            MFA: Mfla_2465
            HPY: HP1279(trpC)
            HPJ: jhp1200(trpC)
            HPA: HPAG1_0278 HPAG1_1233
            HAC: Hac_0015(trpC) Hac_0534(trpC)
            WSU: WS1912(trpC)
            TDN: Tmden_0731
            CJE: Cj0498(trpC)
            CJR: CJE0606(trpC)
            CJJ: CJJ81176_0519(trpC)
            CJU: C8J_0460(trpC)
            CJD: JJD26997_1436(trpC)
            CFF: CFF8240_0640(trpC)
            CCV: CCV52592_1952(trpC)
            CHA: CHAB381_1323(trpC)
            ABU: Abu_0850(trpC)
            NIS: NIS_0989
            SUN: SUN_1695
            GSU: GSU2380(trpC)
            GME: Gmet_2494
            GUR: Gura_1734
            PCA: Pcar_0733
            PPD: Ppro_0711
            DVU: DVU0468(trpC)
            DVL: Dvul_2469
            DDE: Dde_3481
            LIP: LI0413(trpC_2)
            DPS: DP1622
            ADE: Adeh_4055
            AFW: Anae109_0373
            MXA: MXAN_6063(trpC)
            SAT: SYN_01944 SYN_02591
            SFU: Sfum_1773
            PUB: SAR11_0922(trpC)
            MLO: mlr0615
            MES: Meso_1639
            PLA: Plav_3173
            SME: SMc00236(trpC)
            SMD: Smed_1409
            ATU: Atu1688(trpC)
            ATC: AGR_C_3101(igpS)
            RET: RHE_CH02175(trpC)
            RLE: RL2494(trpC)
            BME: BMEI0843
            BMF: BAB1_1164(trpC)
            BMS: BR1141(trpC)
            BMB: BruAb1_1147(trpC)
            BOV: BOV_1100(trpC)
            OAN: Oant_2048
            BJA: blr4810(trpC)
            BRA: BRADO4110(trpC)
            BBT: BBta_4483(trpC)
            RPA: RPA2891(trpC)
            RPB: RPB_2798
            RPC: RPC_2466
            RPD: RPD_2829
            RPE: RPE_2590
            NWI: Nwi_1838
            NHA: Nham_1733
            XAU: Xaut_4302 Xaut_4375
            CCR: CC_1899
            SIL: SPO2151(trpC)
            SIT: TM1040_1138
            RSP: RSP_6214(trpC)
            RSH: Rsph17029_0710
            RSQ: Rsph17025_3097
            JAN: Jann_1877
            RDE: RD1_3213(trpC)
            PDE: Pden_2139
            MMR: Mmar10_1399
            HNE: HNE_1787(trpC)
            ZMO: ZMO0545(trpC)
            NAR: Saro_2024
            SAL: Sala_0835
            SWI: Swit_3219
            ELI: ELI_06515
            GOX: GOX2288
            GBE: GbCGDNIH1_0819
            ACR: Acry_1232
            RRU: Rru_A1897
            MAG: amb2863
            MGM: Mmc1_2332
            ABA: Acid345_1156
            SUS: Acid_7890
            BSU: BG11038(trpC)
            BHA: BH1661(trpC)
            BAN: BA1251
            BAR: GBAA1251
            BAA: BA_1784
            BAT: BAS1159
            BCE: BC1235
            BCA: BCE_1359
            BCZ: BCZK1133(trpC)
            BTK: BT9727_1139(trpC)
            BLI: BL02773(trpC)
            BLD: BLi02401(trpC)
            BCL: ABC1897(trpC)
            BAY: RBAM_020820(trpC)
            BPU: BPUM_1997(trpC)
            OIH: OB0524
            GKA: GK2202(trpC)
            SAU: SA1202(trpC)
            SAV: SAV1370(trpC)
            SAM: MW1257(trpC)
            SAR: SAR1383(trpC)
            SAS: SAS1310
            SAC: SACOL1406(trpC)
            SAB: SAB1225(trpC)
            SAA: SAUSA300_1265(trpC)
            SAO: SAOUHSC_01369
            SAJ: SaurJH9_1431
            SAH: SaurJH1_1460
            SEP: SE1051
            SER: SERP0940(trpC)
            SHA: SH1539(trpC)
            SSP: SSP1376
            LMO: lmo1630(trpC)
            LMF: LMOf2365_1652
            LIN: lin1671(trpC)
            LWE: lwe1646(trpC)
            LLA: L0051(trpC)
            LLC: LACR_1552
            LLM: llmg_1038(trpC)
            SPN: SP_1814
            SPR: spr1634(trpC)
            SPD: SPD_1599(trpC)
            SMU: SMU.535(trpC)
            STC: str1590(trpC)
            STL: stu1590(trpC)
            SSA: SSA_0635(trpC)
            SGO: SGO_0660(trpC)
            LPL: lp_1655(trpC)
            LCA: LSEI_0077
            STH: STH1412
            CAC: CAC3160(trpC)
            CTH: Cthe_0872
            CBE: Cbei_1752
            CKL: CKL_1277(trpC)
            AMT: Amet_1080
            CHY: CHY_1584(trpC)
            DSY: DSY3197
            DRM: Dred_0251
            SWO: Swol_0359
            CSC: Csac_2233
            TTE: TTE1580(trpC)
            MTA: Moth_1339
            MTU: Rv1611(trpC)
            MTC: MT1646(trpC)
            MBO: Mb1637(trpC)
            MBB: BCG_1649(trpC)
            MLE: ML1271(trpC)
            MPA: MAP1305(trpC)
            MAV: MAV_3175(trpC)
            MSM: MSMEG_3219(trpC)
            MVA: Mvan_2816
            MGI: Mflv_3600
            MMC: Mmcs_3051
            MKM: Mkms_3110
            MJL: Mjls_3067
            CGL: NCgl2010(cgl2091) NCgl2930(trpC)
            CGB: cg2293 cg3362(trpCF)
            CEF: CE1991 CE2871(trpC)
            CDI: DIP1555(trpC2) DIP2355(trpC1)
            CJK: jk0797(trpC)
            NFA: nfa18600(trpC)
            RHA: RHA1_ro01014(trpC)
            SCO: SCO2039(SC4G6.08c) SCO3211(SCE8.04c)
            SMA: SAV6175(trpC)
            LXX: Lxx11280(trpC)
            ART: Arth_1687
            AAU: AAur_1838(trpC)
            PAC: PPA1130
            NCA: Noca_3027
            TFU: Tfu_1164
            FRA: Francci3_3017
            FAL: FRAAL4969(trpC)
            ACE: Acel_1073
            KRA: Krad_2966
            SEN: SACE_5750(trpC)
            STP: Strop_3172
            RXY: Rxyl_2094
            RBA: RB10114(trpC)
            CCA: CCA00564(trpC)
            CFE: CF0438(trpC)
            LIL: LA0840(trpC)
            LIC: LIC12786(trpC)
            LBJ: LBJ_0791(trpC)
            LBL: LBL_2288(trpC)
            SYN: slr0546(trpC)
            SYW: SYNW1629(trpC)
            SYC: syc0353_d(trpC)
            SYF: Synpcc7942_1197
            SYD: Syncc9605_0870
            SYE: Syncc9902_1529
            SYG: sync_0751(trpC)
            SYR: SynRCC307_0616(trpC)
            SYX: SynWH7803_1743(trpC)
            CYA: CYA_2369(trpC)
            CYB: CYB_2343(trpC)
            TEL: tll0698(trpC)
            GVI: gll2556(trpC)
            ANA: all0413(trpC) alr3235(trpC) alr4746(trpC)
            AVA: Ava_1926 Ava_4892
            PMA: Pro1371(trpC)
            PMM: PMM1297(trpC)
            PMT: PMT0336(trpC)
            PMN: PMN2A_0863
            PMI: PMT9312_1393
            PMB: A9601_14961(trpC)
            PMC: P9515_14581(trpC)
            PMF: P9303_19771(trpC)
            PMG: P9301_14821(trpC)
            PME: NATL1_17161(trpC)
            TER: Tery_3169
            BTH: BT_0529
            BFR: BF2654
            BFS: BF2676(trpC)
            SRU: SRU_1667(trpC)
            CHU: CHU_3293(trpC)
            GFO: GFO_2671(trpC)
            FJO: Fjoh_4894
            FPS: FP0510(trpC)
            CTE: CT1671(trpC)
            CCH: Cag_0174
            CPH: Cpha266_0531
            PVI: Cvib_1439
            PLT: Plut_1650
            DET: DET1484(trpC)
            DEH: cbdb_A1445(trpC)
            DEB: DehaBAV1_1274
            RRS: RoseRS_1252
            RCA: Rcas_2858
            DRA: DR_1426
            DGE: Dgeo_1587
            TTH: TTC0800
            TTJ: TTHA1164
            AAE: aq_1787(trpC)
            TMA: TM0140
            TPT: Tpet_0785
            MMP: MMP1008(trpC)
            MMQ: MmarC5_0586
            MMZ: MmarC7_0250
            MAE: Maeo_1115
            MVN: Mevan_0333
            MAC: MA2992(trpC)
            MBA: Mbar_A3621
            MMA: MM_2823
            MBU: Mbur_0107
            MTP: Mthe_1543
            MHU: Mhun_1788
            MEM: Memar_0074
            MBN: Mboo_0225
            MST: Msp_1072(trpC)
            MSI: Msm_1143
            MKA: MK1391(trpC)
            AFU: AF1604(trpD)
            HAL: VNG0305G(trpC)
            HMA: rrnAC1886(trpC)
            HWA: HQ1159A(trpC)
            NPH: NP3166A(trpC)
            TAC: Ta0808
            TVO: TVN1022
            PTO: PTO0340
            PAB: PAB2043
            PFU: PF1711
            TKO: TK0252
            RCI: RCIX799(trpC)
            APE: APE_2546
            IHO: Igni_1329
            SSO: SSO0895(trpC)
            STO: ST1226
            SAI: Saci_1427(trpC)
            MSE: Msed_1685
            PAI: PAE0570
            PIS: Pisl_0124
            PCL: Pcal_1213
            PAS: Pars_2240
STRUCTURES  PDB: 1A53  1I4N  1J5T  1JCM  1JUK  1JUL  1LBF  1LBL  1PII  1VC4  
                 2C3Z  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.48
            ExPASy - ENZYME nomenclature database: 4.1.1.48
            ExplorEnz - The Enzyme Database: 4.1.1.48
            ERGO genome analysis and discovery system: 4.1.1.48
            BRENDA, the Enzyme Database: 4.1.1.48
            CAS: 9031-60-1
///
ENTRY       EC 4.1.1.49                 Enzyme
NAME        phosphoenolpyruvate carboxykinase (ATP);
            phosphopyruvate carboxylase (ATP);
            phosphoenolpyruvate carboxylase;
            phosphoenolpyruvate carboxykinase;
            phosphoenolpyruvate carboxykinase;
            phosphopyruvate carboxykinase (adenosine triphosphate);
            PEP carboxylase;
            PEP carboxykinase;
            PEPCK (ATP);
            PEPK;
            PEPCK;
            phosphoenolpyruvic carboxylase;
            phosphoenolpyruvic carboxykinase;
            phosphoenolpyruvate carboxylase (ATP);
            phosphopyruvate carboxykinase;
            ATP:oxaloacetate carboxy-lyase (transphosphorylating)
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     ATP:oxaloacetate carboxy-lyase (transphosphorylating;
            phosphoenolpyruvate-forming)
REACTION    ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO2 [RN:R00341]
ALL_REAC    R00341
SUBSTRATE   ATP [CPD:C00002];
            oxaloacetate [CPD:C00036]
PRODUCT     ADP [CPD:C00008];
            phosphoenolpyruvate [CPD:C00074];
            CO2 [CPD:C00011]
REFERENCE   1  [PMID:5416663]
  AUTHORS   Cannata JJ.
  TITLE     Phosphoenolpyruvate carboxykinase from bakers' yeast. Isolation of
            the enzyme and study of its physical properties.
  JOURNAL   J. Biol. Chem. 245 (1970) 792-8.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2
  AUTHORS   Cannata, J.J.B. and Stoppani, A.O.M.
  TITLE     Phosphopyruvate carboxylase from baker's yeast. I. Isolation,
            purification, and characterization.
  JOURNAL   J. Biol. Chem. 238 (1963) 1196-1207.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Cannata, J.J.B. and Stoppani, A.O.M.
  TITLE     Phosphopyruvate carboxylase from baker's yeast. II. Properties of
            enzyme.
  JOURNAL   J. Biol. Chem. 238 (1963) 1208-1212.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00620  Pyruvate metabolism
            PATH: map00710  Carbon fixation
ORTHOLOGY   KO: K01610  phosphoenolpyruvate carboxykinase (ATP)
GENES       OSA: 4332293
            CME: CMN285C
            SCE: YKR097W(PCK1)
            AGO: AGOS_AFR292W
            PIC: PICST_71471(PCK1)
            CGR: CAGL0H06633g
            ANI: AN1918.2
            AFM: AFUA_6G07720
            AOR: AO090003000174
            CNE: CNI03590
            UMA: UM05130.1
            DDI: DDB_0231108
            PFA: PF13_0234
            TAN: TA20590
            TPV: TP01_0495
            TET: TTHERM_00420030
            TBR: Tb927.2.4210
            TCR: 507547.90 508441.20
            LMA: LmjF27.1805 LmjF27.1810
            ECO: b3403(pck)
            ECJ: JW3366(pck)
            ECE: Z4758(pckA)
            ECS: ECs4245
            ECC: c4176(pckA)
            ECI: UTI89_C3903(pckA)
            ECP: ECP_3489
            ECV: APECO1_3061(pckA)
            ECW: EcE24377A_3877(pckA)
            ECX: EcHS_A3600
            STY: STY4296(pckA)
            STT: t4006(pckA)
            SPT: SPA3365(pckA)
            SEC: SC3432(pckA)
            STM: STM3500(pckA)
            YPE: YPO0138(pckA)
            YPK: y3918(pckA)
            YPM: YP_0139(pckA)
            YPA: YPA_3331
            YPN: YPN_3927
            YPP: YPDSF_0065
            YPS: YPTB3762(pckA)
            YPI: YpsIP31758_3978(pckA)
            SFL: SF3422(pckA)
            SFX: S4341(pckA)
            SFV: SFV_3408(pckA)
            SSN: SSON_3534(pckA)
            SBO: SBO_3390(pckA)
            SDY: SDY_3673(pckA)
            ECA: ECA4106(pckA)
            PLU: plu0100(pckA)
            WBR: WGLp577(pckA)
            SGL: SG2317
            ENT: Ent638_3816
            SPE: Spro_2098 Spro_4617
            HIT: NTHI0973(pckA)
            HIP: CGSHiEE_08015
            HIQ: CGSHiGG_07540
            HDU: HD1331(pckA)
            HSO: HS_1628(pckA)
            PMU: PM1542(pckA)
            MSU: MS2293(pckA)
            APL: APL_0800(pckA)
            ASU: Asuc_0221
            VCH: VC2738
            VCO: VC0395_A2310(pckA)
            VVU: VV1_0881
            VVY: VV0207
            VPA: VP0129
            VFI: VF2478
            PPR: PBPRA3485
            PAE: PA5192(pckA)
            PAU: PA14_68580(pckA)
            PAP: PSPA7_5935(pckA)
            PPF: Pput_0268
            PST: PSPTO_0239(pckA)
            PSB: Psyr_0168
            PSP: PSPPH_5022(pckA)
            PFL: PFL_0284(pckA)
            PFO: Pfl_0268
            PEN: PSEEN0234(pck)
            PMY: Pmen_0368
            SON: SO_0162(pckA)
            SDN: Sden_0117
            SFR: Sfri_0101
            SAZ: Sama_0165
            SBL: Sbal_4210
            SBM: Shew185_0145
            SLO: Shew_3623
            SPC: Sputcn32_3571
            SSE: Ssed_4362
            SPL: Spea_0140
            SHE: Shewmr4_0152
            SHM: Shewmr7_0147
            SHN: Shewana3_0147
            SHW: Sputw3181_3708
            ILO: IL0273(pckA)
            CPS: CPS_4595(pckA)
            PHA: PSHAa0228(pck)
            PAT: Patl_2282
            SDE: Sde_0992
            PIN: Ping_0093
            MAQ: Maqu_3754
            CBU: CBU_2092(pckA)
            CBD: COXBU7E912_2191(pckA)
            FTU: FTT0449(pckA)
            FTF: FTF0449(pckA)
            FTW: FTW_1621(pckA)
            FTL: FTL_1616
            FTH: FTH_1563(pckA)
            FTA: FTA_1704(pckA)
            FTN: FTN_0540(pckA)
            AEH: Mlg_2591
            HCH: HCH_00561(pckA)
            CSA: Csal_2657
            ABO: ABO_0275(pckA)
            MMW: Mmwyl1_3504
            AHA: AHA_0565(pckA)
            BCI: BCI_0013(pckA)
            TDN: Tmden_1696
            CJE: Cj0932c(pckA)
            CJR: CJE1010(pckA)
            CJJ: CJJ81176_0939(pckA)
            CJU: C8J_0869(pckA)
            CJD: JJD26997_0882(pckA)
            CFF: CFF8240_1294(pckA)
            CCV: CCV52592_0965(pckA)
            CHA: CHAB381_1486(pckA)
            CCO: CCC13826_0428 CCC13826_1509(pckA)
            ABU: Abu_1227(pckA)
            NIS: NIS_0043(pckA)
            SUN: SUN_1431(pckA)
            GME: Gmet_3169
            GUR: Gura_0871
            PPD: Ppro_3603
            SAT: SYN_02086
            MLO: mlr5096
            MES: Meso_3502
            PLA: Plav_0109
            SME: SMc02562(pckA)
            SMD: Smed_3253
            ATU: Atu0035(pckA)
            ATC: AGR_C_56
            RET: RHE_CH00037(pckA)
            RLE: RL0037(pckA)
            BME: BMEI2037
            BMS: BR2089(pckA)
            OAN: Oant_0829
            BJA: bll8141(pckA)
            BRA: BRADO0741(pckA)
            BBT: BBta_7365(pckA)
            RPA: RPA0360(pckA)
            RPB: RPB_0461
            RPC: RPC_0599
            RPD: RPD_0365
            RPE: RPE_0819
            NWI: Nwi_0350
            NHA: Nham_0445
            XAU: Xaut_2843
            SIL: SPO0709(pckA)
            SIT: TM1040_2442
            RSP: RSP_1680(pckA)
            RSH: Rsph17029_0313
            RSQ: Rsph17025_2566
            JAN: Jann_0535
            RDE: RD1_1376(pckA)
            PDE: Pden_2852
            MMR: Mmar10_1100
            HNE: HNE_2705(pckA)
            NAR: Saro_2908
            SAL: Sala_2046
            SWI: Swit_0403 Swit_5391
            ELI: ELI_02140
            ACR: Acry_1886
            MGM: Mmc1_0369
            SUS: Acid_1079 Acid_3468
            BSU: BG11841(pckA)
            BHA: BH3302(pckA)
            BAN: BA5019(pckA)
            BAR: GBAA5019(pckA)
            BAA: BA_5438
            BAT: BAS4661
            BCE: BC4762
            BCA: BCE_4916(pckA)
            BCZ: BCZK4518(pckA)
            BCY: Bcer98_3438
            BTK: BT9727_4501(pckA)
            BTL: BALH_4341(pckA)
            BLI: BL00839(pckA)
            BLD: BLi03197(pckA)
            BCL: ABC2879(pckA)
            BAY: RBAM_027580
            BPU: BPUM_2687
            OIH: OB2315(pckA)
            GKA: GK2850
            SAU: SA1609(pckA)
            SAV: SAV1791(pckA)
            SAM: MW1729(pckA)
            SAR: SAR1871(pckA)
            SAS: SAS1712
            SAC: SACOL1838(pckA)
            SAB: SAB1646(pckA)
            SAA: SAUSA300_1731(pckA)
            SAO: SAOUHSC_01910
            SAJ: SaurJH9_1842
            SAH: SaurJH1_1878
            SEP: SE1459
            SER: SERP1353(pckA)
            SHA: SH1137(pckA)
            SSP: SSP0975
            SMU: SMU.1389(pckA)
            LPL: lp_3418(pck)
            LJO: LJ0149
            LAC: LBA0466
            LSL: LSL_0395(pckA)
            LCA: LSEI_1820
            LGA: LGAS_0152
            CKL: CKL_2699(pck)
            DSY: DSY4203(pck)
            PTH: PTH_1008(pckA)
            TTE: TTE1783(pckA)
            MTA: Moth_0633 Moth_1893
            RXY: Rxyl_0680
            FNU: FN1120
            LIL: LA0251(pckA)
            LIC: LIC10216(pckA)
            LBJ: LBJ_2789(pckA)
            LBL: LBL_0282(pckA)
            BTH: BT_2790
            BFR: BF4446
            BFS: BF4244(pckA)
            PGI: PG1676(pckA)
            SRU: SRU_1835(pckA) SRU_2373(pckA)
            GFO: GFO_0105(pckA)
            FJO: Fjoh_1366
            FPS: FP2375(pckA)
            DRA: DR_0977
            DGE: Dgeo_1196
            TTH: TTC1709
            TTJ: TTHA0278
            APE: APE_0033.1
STRUCTURES  PDB: 1AQ2  1AYL  1K3C  1K3D  1OEN  1OS1  1XKV  1YGG  1YLH  1YTM  
                 1YVY  2OLQ  2OLR  2PC9  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.49
            ExPASy - ENZYME nomenclature database: 4.1.1.49
            ExplorEnz - The Enzyme Database: 4.1.1.49
            ERGO genome analysis and discovery system: 4.1.1.49
            BRENDA, the Enzyme Database: 4.1.1.49
            CAS: 9073-94-3
///
ENTRY       EC 4.1.1.50                 Enzyme
NAME        adenosylmethionine decarboxylase;
            S-adenosylmethionine decarboxylase;
            S-adenosyl-L-methionine decarboxylase;
            S-adenosyl-L-methionine carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     S-adenosyl-L-methionine carboxy-lyase
            [(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium-salt-forming]
REACTION    S-adenosyl-L-methionine =
            (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
            [RN:R00178]
ALL_REAC    R00178
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019]
PRODUCT     (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt
            [CPD:C01137];
            CO2 [CPD:C00011]
COFACTOR    Pyruvate [CPD:C00022]
COMMENT     The Escherichia coli enzyme contains a pyruvoyl group.
REFERENCE   1  [PMID:3546296]
  AUTHORS   Anton DL, Kutny R.
  TITLE     Escherichia coli S-adenosylmethionine decarboxylase. Subunit
            structure, reductive amination, and NH2-terminal sequences.
  JOURNAL   J. Biol. Chem. 262 (1987) 2817-22.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Tabor, C.W.
  TITLE     Adenosylmethionine decarboxylase.
  JOURNAL   Methods Enzymol. 5 (1962) 756-760.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K01611  S-adenosylmethionine decarboxylase
GENES       HSA: 262(AMD1)
            MMU: 11702(Amd1) 11703(Amd2)
            RNO: 81640(Amd1)
            CFA: 481960(AMD1)
            BTA: 280997(AMD1)
            GGA: 421755(AMD1)
            XLA: 380052(amd1)
            DRE: 394055(amd1)
            SPU: 580895(LOC580895)
            DME: Dmel_CG5029(SamDC)
            CEL: F47G4.7(smd-1)
            ATH: AT3G02470(SAMDC) AT3G25570 AT5G15950 AT5G18930(BUD2/SAMDC4)
            OSA: 4329955 4336294
            CME: CMO012C
            SCE: YOL052C(SPE2)
            AGO: AGOS_ABL061C
            PIC: PICST_85160(SPE2)
            CAL: CaO19.568
            CGR: CAGL0H02607g
            SPO: SPBP4H10.05c
            ANI: AN8231.2
            AFM: AFUA_5G03670
            AOR: AO090102000577
            CNE: CNA00140
            UMA: UM00999.1
            DDI: DDBDRAFT_0167292
            PFA: PF10_0322
            TBR: Tb927.6.4410 Tb927.6.4460 Tb927.6.4470
            TCR: 504257.30 509167.120
            LMA: LmjF30.3110 LmjF30.3120
            ECO: b0120(speD)
            ECJ: JW0116(speD)
            ECE: Z0130(speD)
            ECS: ECs0124
            ECC: c0149(speD)
            ECI: UTI89_C0133(speD)
            ECP: ECP_0127
            ECV: APECO1_1865(speD)
            ECW: EcE24377A_0122(speD)
            ECX: EcHS_A0124(speD)
            STY: STY0187(speD)
            STT: t0170(speD)
            SPT: SPA0168(speD)
            SEC: SC0165(speD)
            STM: STM0165(speD)
            YPE: YPO3412(speD)
            YPK: y0774(speD)
            YPM: YP_0273(speD)
            YPA: YPA_2914
            YPN: YPN_0676
            YPP: YPDSF_2943
            YPS: YPTB0719(speD)
            YPI: YpsIP31758_3355(speD)
            SFL: SF0117(speD)
            SFX: S0119(speD)
            SFV: SFV_0111(speD)
            SSN: SSON_0128(speD)
            SBO: SBO_0109(speD)
            SDY: SDY_0027(speD)
            ECA: ECA3334(speD)
            PLU: plu0842(speD)
            BUC: BU208(speD)
            BAS: BUsg202(speD)
            SGL: SG0478
            ENT: Ent638_0668
            SPE: Spro_4002
            XFA: XF1539
            XFT: PD0754(speD)
            XCC: XCC0473(speD)
            XCB: XC_0487
            XCV: XCV0520(speD)
            XAC: XAC0484(speD)
            XOO: XOO4157(speD)
            XOM: XOO_3932(XOO3932)
            PAE: PA0654(speD) PA4773
            PAU: PA14_08390(speD)
            PAP: PSPA7_0795(speD) PSPA7_5494
            PST: PSPTO_0598(speD)
            PSB: Psyr_4575
            PSP: PSPPH_0678(speD)
            PFO: Pfl_5109
            SDN: Sden_2279
            SFR: Sfri_1699
            SAZ: Sama_1962
            SBL: Sbal_1769
            SBM: Shew185_1762
            SLO: Shew_1620
            SPC: Sputcn32_1648
            SSE: Ssed_2608
            SPL: Spea_2479
            SHE: Shewmr4_1558
            SHM: Shewmr7_1633
            SHN: Shewana3_1625
            SHW: Sputw3181_2378
            CPS: CPS_0630(speD)
            PHA: PSHAa0199(speD)
            MAQ: Maqu_3552
            MCA: MCA1749(speD)
            FTU: FTT0430(speH)
            FTF: FTF0430(speH)
            FTW: FTW_1644
            FTL: FTL_0499
            FTH: FTH_0497(speH)
            TCX: Tcr_0272
            NOC: Noc_0951
            AEH: Mlg_2244
            HHA: Hhal_2078
            HCH: HCH_06136
            CSA: Csal_0913
            ABO: ABO_2021(speD)
            RSO: RS05338(RSp1293)
            REU: Reut_A3300
            RME: Rmet_3457
            BUR: Bcep18194_B0820
            BCN: Bcen_3477
            BCH: Bcen2424_4889
            MPT: Mpe_A0258
            NEU: NE0348
            NIS: NIS_1526
            SFU: Sfum_0720
            PUB: SAR11_1211(speE)
            RPB: RPB_2045
            RPD: RPD_3345
            SIT: TM1040_1388
            JAN: Jann_2428
            GOX: GOX1090
            GBE: GbCGDNIH1_1385
            RRU: Rru_A1692
            MGM: Mmc1_3177
            ABA: Acid345_0106
            BSU: BG13832(speD)
            BHA: BH1097 BH3148
            BAN: BA4825(speD-1) BA5446(speD-2)
            BAR: GBAA4825(speD-1) GBAA5446(speD-2)
            BAA: BA_0299
            BAT: BAS4477 BAS5061
            BCE: BC4582 BC5214
            BCA: BCE_4712(speD)
            BCZ: BCZK4323(speD) BCZK4906(speD)
            BTK: BT9727_4312(speD) BT9727_4891(speD)
            BTL: BALH_4165(speD) BALH_4706(speD)
            BLD: BLi03051(speD)
            BCL: ABC2704(speD)
            BAY: RBAM_026050(speD)
            BPU: BPUM_2546(speD)
            OIH: OB0938
            GKA: GK1400 GK2725
            STH: STH421
            CAC: CAC2601
            CPE: CPE0548(speD)
            CPF: CPF_0527(speD)
            CPR: CPR_0513(speD)
            CTC: CTC01312
            CTH: Cthe_0715
            CDF: CD0889(speD)
            CBO: CBO3363(speD)
            CBA: CLB_3421(speD)
            CBH: CLC_3308(speD)
            CBF: CLI_3539(speD)
            CKL: CKL_1568(speH)
            CHY: CHY_1811(speD)
            DSY: DSY2236 DSY4124
            DRM: Dred_1479 Dred_2200
            SWO: Swol_0674
            CSC: Csac_1308
            TTE: TTE1354(speD)
            MTA: Moth_1282
            SEN: SACE_1267 SACE_4335(speD)
            RBA: RB3217(speD)
            LIC: LIC20239(speD)
            LBJ: LBJ_4230(speD)
            LBL: LBL_4244(speD)
            SYW: SYNW2050
            SYC: syc1849_d syc2050_d
            SYF: Synpcc7942_2043 Synpcc7942_2249
            SYD: Syncc9605_0393
            SYE: Syncc9902_1936
            SYR: SynRCC307_2094(speH)
            SYX: SynWH7803_0451(speH)
            CYA: CYA_0574
            CYB: CYB_0057
            PMA: Pro1727(speD)
            PMM: PMM1572
            PMT: PMT1716
            PMN: PMN2A_1144
            PMI: PMT9312_1664
            PMB: A9601_17791
            PMC: P9515_17591(speD)
            PMF: P9303_22791(speD)
            PMG: P9301_17631(speD)
            PME: NATL1_20181(speD)
            TTH: TTC0473 TTC1093
            TTJ: TTHA0825 TTHA1457
            AAE: aq_254
            TMA: TM0655
            TPT: Tpet_0276
            TME: Tmel_0571
            MJA: MJ0315
            MMP: MMP1583
            AFU: AF1610
            TAC: Ta1196
            TVO: TVN0405
            PTO: PTO1286
            PHO: PH1992
            PAB: PAB1162
            PFU: PF1930
            TKO: TK1592
            APE: APE_0079 APE_0639.1
            SMR: Smar_0500
            SSO: SSO0536 SSO0585
            STO: ST1348 ST1452
            SAI: Saci_1363(sph1) Saci_1568
            PAI: PAE1490 PAE1749
            PIS: Pisl_1580 Pisl_1714
            PCL: Pcal_0636 Pcal_0807
            PAS: Pars_0617 Pars_0747
STRUCTURES  PDB: 1I72  1I79  1I7B  1I7C  1I7M  1JEN  1JL0  1MHM  1MSV  1TLU  
                 1TMI  1VR7  2III  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.50
            ExPASy - ENZYME nomenclature database: 4.1.1.50
            ExplorEnz - The Enzyme Database: 4.1.1.50
            ERGO genome analysis and discovery system: 4.1.1.50
            BRENDA, the Enzyme Database: 4.1.1.50
            CAS: 9036-20-8
///
ENTRY       EC 4.1.1.51                 Enzyme
NAME        3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase;
            3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-carboxy-lyase
            (3-hydroxy-2-methylpyridine-5-carboxylate-forming)
REACTION    3-hydroxy-2-methylpyridine-4,5-dicarboxylate =
            3-hydroxy-2-methylpyridine-5-carboxylate + CO2 [RN:R03461]
ALL_REAC    R03461
SUBSTRATE   3-hydroxy-2-methylpyridine-4,5-dicarboxylate [CPD:C04604]
PRODUCT     3-hydroxy-2-methylpyridine-5-carboxylate [CPD:C01270];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Snell, E.E., Smucker, A.A., Ringelmann, E. and Lynen, F.
  TITLE     Die bakterielle Oxydation des Vitamin B6. IV. Die enzymatische
            Decarboxylierung von 2-Methyl-3-hydroxypyridine-4,5-dicarbonsaure.
  JOURNAL   Biochem. Z. 341 (1964) 109-119.
PATHWAY     PATH: map00750  Vitamin B6 metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.51
            ExPASy - ENZYME nomenclature database: 4.1.1.51
            ExplorEnz - The Enzyme Database: 4.1.1.51
            ERGO genome analysis and discovery system: 4.1.1.51
            BRENDA, the Enzyme Database: 4.1.1.51
            CAS: 37289-49-9
///
ENTRY       EC 4.1.1.52                 Enzyme
NAME        6-methylsalicylate decarboxylase;
            6-methylsalicylic acid (2,6-cresotic acid) decarboxylase;
            6-MSA decarboxylase;
            6-methylsalicylate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     6-methylsalicylate carboxy-lyase (3-cresol-forming)
REACTION    6-methylsalicylate = 3-cresol + CO2 [RN:R03567]
ALL_REAC    R03567
SUBSTRATE   6-methylsalicylate [CPD:C02657]
PRODUCT     3-cresol [CPD:C01467];
            CO2 [CPD:C00011]
REFERENCE   1  [PMID:5354271]
  AUTHORS   Light RJ.
  TITLE     6-methylsalicylic acid decarboxylase from Penicillium patulum.
  JOURNAL   Biochim. Biophys. Acta. 191 (1969) 430-8.
  ORGANISM  Penicillium patulum
REFERENCE   2
  AUTHORS   Vogel, G. and Lynen, F.
  TITLE     6-Methylsalicylsaure-Decarboxylase.
  JOURNAL   Naturwissenschaften 57 (1970) 664.
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.52
            ExPASy - ENZYME nomenclature database: 4.1.1.52
            ExplorEnz - The Enzyme Database: 4.1.1.52
            ERGO genome analysis and discovery system: 4.1.1.52
            BRENDA, the Enzyme Database: 4.1.1.52
            CAS: 37289-50-2
///
ENTRY       EC 4.1.1.53                 Enzyme
NAME        phenylalanine decarboxylase;
            L-phenylalanine decarboxylase;
            aromatic L-amino acid decarboxylase;
            L-phenylalanine carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     L-phenylalanine carboxy-lyase (phenylethylamine-forming)
REACTION    L-phenylalanine = phenylethylamine + CO2 [RN:R00699]
ALL_REAC    R00699
SUBSTRATE   L-phenylalanine [CPD:C00079]
PRODUCT     phenylethylamine [CPD:C05332];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also acts on tyrosine and other
            aromatic amino acids.
REFERENCE   1  [PMID:14466899]
  AUTHORS   LOVENBERG W, WEISSBACH H, UDENFRIEND S.
  TITLE     Aromatic L-amino acid decarboxylase.
  JOURNAL   J. Biol. Chem. 237 (1962) 89-93.
  ORGANISM  guinea pig, dog [GN:cfa], rat [GN:rno]
REFERENCE   2  [PMID:6034195]
  AUTHORS   Schulz AR, Oliner L.
  TITLE     The possible role of thyroid aromatic amino acid decarboxylase in
            thyroxine biosynthesis.
  JOURNAL   Life. Sci. 6 (1967) 873-80.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00360  Phenylalanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.53
            ExPASy - ENZYME nomenclature database: 4.1.1.53
            ExplorEnz - The Enzyme Database: 4.1.1.53
            ERGO genome analysis and discovery system: 4.1.1.53
            BRENDA, the Enzyme Database: 4.1.1.53
            CAS: 9075-72-3
///
ENTRY       EC 4.1.1.54                 Enzyme
NAME        dihydroxyfumarate decarboxylase;
            dihydroxyfumarate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     dihydroxyfumarate carboxy-lyase (tartronate-semialdehyde-forming)
REACTION    dihydroxyfumarate = tartronate semialdehyde + CO2 [RN:R03127]
ALL_REAC    R03127
SUBSTRATE   dihydroxyfumarate [CPD:C00975]
PRODUCT     tartronate semialdehyde [CPD:C01146];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Fukumaga, K.
  TITLE     Metabolism of dihydroxyfumarate, hydroxypyruvate, and their related
            compounds. I. Enzymic formation of xylulose in liver.
  JOURNAL   J. Biochem. (Tokyo) 47 (1960) 741-754.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.54
            ExPASy - ENZYME nomenclature database: 4.1.1.54
            ExplorEnz - The Enzyme Database: 4.1.1.54
            ERGO genome analysis and discovery system: 4.1.1.54
            BRENDA, the Enzyme Database: 4.1.1.54
            CAS: 37289-51-3
///
ENTRY       EC 4.1.1.55                 Enzyme
NAME        4,5-dihydroxyphthalate decarboxylase;
            4,5-dihydroxyphthalate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     4,5-dihydroxyphthalate carboxy-lyase (3,4-dihydroxybenzoate-forming)
REACTION    4,5-dihydroxyphthalate = 3,4-dihydroxybenzoate + CO2 [RN:R01635]
ALL_REAC    R01635;
            (other) R05375
SUBSTRATE   4,5-dihydroxyphthalate [CPD:C03233]
PRODUCT     3,4-dihydroxybenzoate [CPD:C00230];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Ribbons, D.W. and Evans, W.C.
  TITLE     Oxidative metabolism of phthalic acid by soil pseudomonads.
  JOURNAL   Biochem. J. 76 (1966) 310-318.
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
ORTHOLOGY   KO: K04102  4,5-dihydroxyphthalate decarboxylase
GENES       BXE: Bxe_A2046 Bxe_B2513
            BVI: Bcep1808_4268 Bcep1808_4307
            BPE: BP0683
            BPA: BPP0387
            BBR: BB0389
            POL: Bpro_1912
            PNA: Pnap_4626
            VEI: Veis_2927
            HAR: HEAR2118
            MES: Meso_0812
            MJL: Mjls_4214
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.55
            ExPASy - ENZYME nomenclature database: 4.1.1.55
            ExplorEnz - The Enzyme Database: 4.1.1.55
            ERGO genome analysis and discovery system: 4.1.1.55
            UM-BBD (Biocatalysis/Biodegradation Database): 4.1.1.55
            BRENDA, the Enzyme Database: 4.1.1.55
            CAS: 37290-48-5
///
ENTRY       EC 4.1.1.56                 Enzyme
NAME        3-oxolaurate decarboxylase;
            beta-ketolaurate decarboxylase;
            beta-ketoacyl decarboxylase;
            3-oxododecanoate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     3-oxododecanoate carboxy-lyase (2-undecanone-forming)
REACTION    3-oxododecanoate = 2-undecanone + CO2 [RN:R03747]
ALL_REAC    R03747
SUBSTRATE   3-oxododecanoate [CPD:C02367]
PRODUCT     2-undecanone [CPD:C01875];
            CO2 [CPD:C00011]
COMMENT     Also decarboxylates other C14 to C16 oxo acids.
REFERENCE   1  [PMID:13701396]
  AUTHORS   FRANKE W, PLATZECK A, EICHHORN G.
  TITLE     [On the knowledge of fatty acid catabolism by mold fungi. III. On a
            decarboxylase for average beta-ketomonocarbonic acids
            (beta-ketolaurate decarboxylase)]
  JOURNAL   Arch. Mikrobiol. 40 (1961) 73-93.
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.56
            ExPASy - ENZYME nomenclature database: 4.1.1.56
            ExplorEnz - The Enzyme Database: 4.1.1.56
            ERGO genome analysis and discovery system: 4.1.1.56
            BRENDA, the Enzyme Database: 4.1.1.56
            CAS: 37290-49-6
///
ENTRY       EC 4.1.1.57                 Enzyme
NAME        methionine decarboxylase;
            L-methionine decarboxylase;
            L-methionine carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     L-methionine carboxy-lyase (3-methylthiopropanamine-forming)
REACTION    L-methionine = 3-methylthiopropanamine + CO2 [RN:R00656]
ALL_REAC    R00656
SUBSTRATE   L-methionine [CPD:C00073]
PRODUCT     3-methylthiopropanamine [CPD:C03354];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Hagion, H. and Nakayama, K.
  TITLE     Amino acid metabolism in microorganisms. Part IV. L-Methionine
            decarboxylase produced by Streptomyces strain.
  JOURNAL   Agric. Biol. Chem. 32 (1968) 727-733.
  ORGANISM  Streptomyces sp.
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.57
            ExPASy - ENZYME nomenclature database: 4.1.1.57
            ExplorEnz - The Enzyme Database: 4.1.1.57
            ERGO genome analysis and discovery system: 4.1.1.57
            BRENDA, the Enzyme Database: 4.1.1.57
            CAS: 37290-50-9
///
ENTRY       EC 4.1.1.58                 Enzyme
NAME        orsellinate decarboxylase;
            orsellinate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     2,4-dihydroxy-6-methylbenzoate carboxy-lyase (orcinol-forming)
REACTION    2,4-dihydroxy-6-methylbenzoate = orcinol + CO2 [RN:R02831]
ALL_REAC    R02831
SUBSTRATE   2,4-dihydroxy-6-methylbenzoate [CPD:C01839]
PRODUCT     orcinol [CPD:C00727];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Pettersson, G.
  TITLE     An orsellinic acid decarboxylase isolated from Gliocladium roseum.
  JOURNAL   Acta Chem. Scand. 19 (1965) 2013-2021.
  ORGANISM  Gliocladium roseum
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.58
            ExPASy - ENZYME nomenclature database: 4.1.1.58
            ExplorEnz - The Enzyme Database: 4.1.1.58
            ERGO genome analysis and discovery system: 4.1.1.58
            BRENDA, the Enzyme Database: 4.1.1.58
            CAS: 9076-58-8
///
ENTRY       EC 4.1.1.59                 Enzyme
NAME        gallate decarboxylase;
            gallic acid decarboxylase;
            gallate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     3,4,5-trihydroxybenzoate carboxy-lyase (pyrogallol-forming)
REACTION    3,4,5-trihydroxybenzoate = pyrogallol + CO2 [RN:R03247]
ALL_REAC    R03247
SUBSTRATE   3,4,5-trihydroxybenzoate [CPD:C01424]
PRODUCT     pyrogallol [CPD:C01108];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Grant, D.J.W. and Patel, J.C.
  TITLE     Non-oxidative decarboxylation of p-hydroxybenzoic acid, gentisic
            acid, protocatechuic acid, and gallic acid by Klebsiella aerogenes
            (Aerobacter aerogenes).
  JOURNAL   J. Microbiol. Serol. 35 (1969) 325-343.
  ORGANISM  Klebsiella aerogenes
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.59
            ExPASy - ENZYME nomenclature database: 4.1.1.59
            ExplorEnz - The Enzyme Database: 4.1.1.59
            ERGO genome analysis and discovery system: 4.1.1.59
            UM-BBD (Biocatalysis/Biodegradation Database): 4.1.1.59
            BRENDA, the Enzyme Database: 4.1.1.59
            CAS: 37290-51-0
///
ENTRY       EC 4.1.1.60                 Enzyme
NAME        stipitatonate decarboxylase;
            stipitatonate carboxy-lyase (decyclizing)
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     stipitatonate carboxy-lyase (decyclizing, stipitatate-forming)
REACTION    stipitatonate = stipitatate + CO2 [RN:R03739]
ALL_REAC    R03739
SUBSTRATE   stipitatonate [CPD:C02080]
PRODUCT     stipitatate [CPD:C01853];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Bentley, R. and Thiessen, C.P.
  TITLE     Biosynthesis of tropolones in Penicillium stipitatum. V. Preparation
            and properties of stipitatonic acid decarboxylase.
  JOURNAL   J. Biol. Chem. 238 (1963) 3811-3816.
  ORGANISM  Penicillium stipitatum
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.60
            ExPASy - ENZYME nomenclature database: 4.1.1.60
            ExplorEnz - The Enzyme Database: 4.1.1.60
            ERGO genome analysis and discovery system: 4.1.1.60
            BRENDA, the Enzyme Database: 4.1.1.60
            CAS: 37290-52-1
///
ENTRY       EC 4.1.1.61                 Enzyme
NAME        4-hydroxybenzoate decarboxylase;
            p-hydroxybenzoate decarboxylase;
            4-hydroxybenzoate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     4-hydroxybenzoate carboxy-lyase (phenol-forming)
REACTION    4-hydroxybenzoate = phenol + CO2 [RN:R01238]
ALL_REAC    R01238
SUBSTRATE   4-hydroxybenzoate [CPD:C00156]
PRODUCT     phenol [CPD:C00146];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Grant, D.J.W. and Patel, J.C.
  TITLE     Non-oxidative decarboxylation of p-hydroxybenzoic acid, gentisic
            acid, protocatechuic acid, and gallic acid by Klebsiella aerogenes
            (Aerobacter aerogenes).
  JOURNAL   J. Microbiol. Serol. 35 (1969) 325-343.
  ORGANISM  Klebsiella aerogenes
REFERENCE   2
  AUTHORS   Tschech, A. and Fuchs, G.
  TITLE     Anaerobic degradation of phenol via carboxylation to
            4-hydroxybenzoate - in vitro study of isotope exchange between
            (CO2)-C-14 and 4-hydroxybenzoate.
  JOURNAL   Arch. Microbiol. 152 (1989) 594-599.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
ORTHOLOGY   KO: K01612  4-hydroxybenzoate decarboxylase
GENES       ECW: EcE24377A_3038(kpdD) EcE24377A_3039(kpdC)
                 EcE24377A_3040(kpdB)
            REH: H16_B2446
            MMA: MM_1526
            RCI: RRC445
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.61
            ExPASy - ENZYME nomenclature database: 4.1.1.61
            ExplorEnz - The Enzyme Database: 4.1.1.61
            ERGO genome analysis and discovery system: 4.1.1.61
            UM-BBD (Biocatalysis/Biodegradation Database): 4.1.1.61
            BRENDA, the Enzyme Database: 4.1.1.61
            CAS: 37290-53-2
///
ENTRY       EC 4.1.1.62                 Enzyme
NAME        gentisate decarboxylase;
            2,5-dihydroxybenzoate decarboxylase;
            gentisate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     2,5-dihydroxybenzoate carboxy-lyase (hydroquinone-forming)
REACTION    2,5-dihydroxybenzoate = hydroquinone + CO2 [RN:R02489]
ALL_REAC    R02489
SUBSTRATE   2,5-dihydroxybenzoate [CPD:C00628]
PRODUCT     hydroquinone [CPD:C00530];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Grant, D.J.W. and Patel, J.C.
  TITLE     Non-oxidative decarboxylation of p-hydroxybenzoic acid, gentisic
            acid, protocatechuic acid, and gallic acid by Klebsiella aerogenes
            (Aerobacter aerogenes).
  JOURNAL   J. Microbiol. Serol. 35 (1969) 325-343.
  ORGANISM  Klebsiella aerogenes
PATHWAY     PATH: map00350  Tyrosine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.62
            ExPASy - ENZYME nomenclature database: 4.1.1.62
            ExplorEnz - The Enzyme Database: 4.1.1.62
            ERGO genome analysis and discovery system: 4.1.1.62
            BRENDA, the Enzyme Database: 4.1.1.62
            CAS: 37290-54-3
///
ENTRY       EC 4.1.1.63                 Enzyme
NAME        protocatechuate decarboxylase;
            3,4-dihydrobenzoate decarboxylase;
            protocatechuate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     3,4-dihydroxybenzoate carboxy-lyase (catechol-forming)
REACTION    3,4-dihydroxybenzoate = catechol + CO2 [RN:R00822]
ALL_REAC    R00822
SUBSTRATE   3,4-dihydroxybenzoate [CPD:C00230]
PRODUCT     catechol [CPD:C00090];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Grant, D.J.W. and Patel, J.C.
  TITLE     Non-oxidative decarboxylation of p-hydroxybenzoic acid, gentisic
            acid, protocatechuic acid, and gallic acid by Klebsiella aerogenes
            (Aerobacter aerogenes).
  JOURNAL   J. Microbiol. Serol. 35 (1969) 325-343.
  ORGANISM  Klebsiella aerogenes
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.63
            ExPASy - ENZYME nomenclature database: 4.1.1.63
            ExplorEnz - The Enzyme Database: 4.1.1.63
            ERGO genome analysis and discovery system: 4.1.1.63
            BRENDA, the Enzyme Database: 4.1.1.63
            CAS: 37290-55-4
///
ENTRY       EC 4.1.1.64                 Enzyme
NAME        2,2-dialkylglycine decarboxylase (pyruvate);
            dialkyl amino acid (pyruvate) decarboxylase;
            alpha-dialkyl amino acid transaminase;
            2,2-dialkyl-2-amino acid-pyruvate aminotransferase;
            L-alanine-alpha-ketobutyrate aminotransferase;
            dialkylamino-acid decarboxylase (pyruvate);
            2,2-dialkylglycine carboxy-lyase (amino-transferring)
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     2,2-dialkylglycine carboxy-lyase (amino-transferring;
            L-alanine-forming)
REACTION    2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
            [RN:R03854]
ALL_REAC    R03854
SUBSTRATE   2,2-dialkylglycine [CPD:C02623];
            pyruvate [CPD:C00022]
PRODUCT     dialkyl ketone [CPD:C02146];
            CO2 [CPD:C00011];
            L-alanine [CPD:C00041]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Acts on 2-amino-2-methylpropanoate
            (i.e. 2-methylalanine), 2-amino-2-methylbutanoate and
            1-aminocyclopentanecarboxylate.
REFERENCE   1
  AUTHORS   Bailey, G.B. and Dempsey, W.B.
  TITLE     Purification and properties of an alpha-dialkyl amino acid
            transaminase.
  JOURNAL   Biochemistry 6 (1967) 1526-1533.
  ORGANISM  Pseudomonas sp.
ORTHOLOGY   KO: K00596  2,2-dialkylglycine decarboxylase (pyruvate)
GENES       BUR: Bcep18194_B0665
            MSM: MSMEG_6842
            SEN: SACE_2647
STRUCTURES  PDB: 1D7R  1D7S  1D7U  1D7V  1DGD  1DGE  1DKA  1M0N  1M0O  1M0P  
                 1M0Q  1Z3Z  1ZC9  1ZOB  1ZOD  2DKB  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.64
            ExPASy - ENZYME nomenclature database: 4.1.1.64
            ExplorEnz - The Enzyme Database: 4.1.1.64
            ERGO genome analysis and discovery system: 4.1.1.64
            BRENDA, the Enzyme Database: 4.1.1.64
            CAS: 9032-17-1
///
ENTRY       EC 4.1.1.65                 Enzyme
NAME        phosphatidylserine decarboxylase;
            PS decarboxylase;
            phosphatidyl-L-serine carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     phosphatidyl-L-serine carboxy-lyase
            (phosphatidylethanolamine-forming)
REACTION    phosphatidyl-L-serine = phosphatidylethanolamine + CO2 [RN:R02055]
ALL_REAC    R02055
SUBSTRATE   phosphatidyl-L-serine [CPD:C02737]
PRODUCT     phosphatidylethanolamine [CPD:C00350];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018];
            Pyruvate [CPD:C00022]
COMMENT     A pyridoxal-phosphate protein. In Escherichia coli, the prosthetic
            group is a pyruvoyl group.
REFERENCE   1  [PMID:14213340]
  AUTHORS   KANFER J, KENNEDY EP.
  TITLE     METABOLISM AND FUNCTION OF BACTERIAL LIPIDS. II. BIOSYNTHESIS OF
            PHOSPHOLIPIDS IN ESCHERICHIA COLI.
  JOURNAL   J. Biol. Chem. 239 (1964) 1720-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:338609]
  AUTHORS   Satre M, Kennedy EP.
  TITLE     Identification of bound pyruvate essential for the activity of
            phosphatidylserine decarboxylase of Escherichia coli.
  JOURNAL   J. Biol. Chem. 253 (1978) 479-83.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K01613  phosphatidylserine decarboxylase
GENES       HSA: 23761(PISD)
            MMU: 320951(Pisd)
            CFA: 477544(PISD)
            GGA: 416960(PISD)
            XLA: 379065(MGC52759) 447773(MGC84353)
            XTR: 448069(pisd)
            SPU: 593856(LOC593856)
            DME: Dmel_CG5991
            ATH: AT4G16700
            OSA: 4325237 4331292
            CME: CMK243C
            SCE: YGR170W(PSD2) YNL169C(PSD1)
            AGO: AGOS_AAL131C AGOS_AFR022C
            PIC: PICST_32693(PSD1) PICST_40695(PSD2)
            CAL: CaO19_3954(CaO19.3954)
            CGR: CAGL0I08745g CAGL0J06226g
            SPO: SPAC25B8.03 SPAC31G5.15 SPBC16E9.18 SPBC1E8.01
            ANI: AN0910.2 AN3188.2 AN9039.2
            AFM: AFUA_1G15760 AFUA_1G16930 AFUA_3G13970 AFUA_7G01730
            AOR: AO090005001124 AO090012000733 AO090103000445
            CNE: CNG02480
            UMA: UM02098.1 UM02799.1
            DDI: DDBDRAFT_0184541 DDBDRAFT_0203860
            PFA: PFI1370c
            CHO: Chro.30247
            TAN: TA09760
            TPV: TP01_1219
            TET: TTHERM_00859320 TTHERM_00859340
            LMA: LmjF35.4590
            ECO: b4160(psd)
            ECJ: JW4121(psd)
            ECE: Z5766
            ECS: ECs5139
            ECC: c5247(psd)
            ECI: UTI89_C4760(psd)
            ECP: ECP_4404
            ECW: EcE24377A_4717(psd)
            ECX: EcHS_A4402
            STY: STY4708(psd)
            STT: t4400(psd)
            SPT: SPA4165(psd)
            SEC: SC4227(psd)
            STM: STM4348(psd)
            YPE: YPO0364(psd)
            YPK: y0620(psd)
            YPM: YP_0519(psd)
            YPA: YPA_3920
            YPN: YPN_3307
            YPP: YPDSF_3611
            YPS: YPTB0416(psd)
            YPI: YpsIP31758_3663(psd)
            YEN: YE0367(psd)
            SFL: SF4318(psd)
            SFX: S4582(psd)
            SFV: SFV_4317(psd)
            SSN: SSON_4345(psd)
            SBO: SBO_4297(psd)
            SDY: SDY_4432(psd)
            ECA: ECA3966(psd)
            PLU: plu4597(psd)
            WBR: WGLp428(psd)
            SGL: SG0312
            ENT: Ent638_0346
            SPE: Spro_0422 Spro_2939
            BFL: Bfl074(psd)
            BPN: BPEN_076(psd)
            HIN: HI0160(psd)
            HIT: NTHI0250(psd)
            HIP: CGSHiEE_02480
            HDU: HD0649(psd)
            HSO: HS_1300(psd)
            PMU: PM1899(psd)
            MSU: MS1864(psd)
            APL: APL_1407(psd)
            ASU: Asuc_0719
            XFA: XF1365
            XFT: PD0604(psd)
            XCC: XCC2555(dpsD)
            XCB: XC_1563
            XCV: XCV2880(psd) XCV3402 XCV3403
            XAC: XAC2728(dpsD)
            XOO: XOO3264(dpsD)
            XOM: XOO_3092(XOO3092)
            VCH: VC0339
            VCO: VC0395_A2741(psd)
            VVU: VV1_1284
            VVY: VV3079
            VPA: VP2825
            VFI: VF2331
            PPR: PBPRA3372
            PAE: PA4957(psd)
            PAU: PA14_65500(psd)
            PAP: PSPA7_5686(psd)
            PPU: PP_4908(psd)
            PPF: Pput_1526 Pput_4784
            PST: PSPTO_4955
            PSB: Psyr_0559
            PSP: PSPPH_0552
            PFL: PFL_0552(psd)
            PFO: Pfl_0509(psd)
            PEN: PSEEN4961(psd)
            PMY: Pmen_0621 Pmen_2805
            PAR: Psyc_1925(psd)
            PCR: Pcryo_2218
            PRW: PsycPRwf_2095
            ACI: ACIAD3560(psd)
            ACB: A1S_3378
            SDN: Sden_3214
            SFR: Sfri_3319
            SAZ: Sama_3034
            SBL: Sbal_0549
            SBM: Shew185_2919 Shew185_3776
            SLO: Shew_0557
            SPC: Sputcn32_3289
            SSE: Ssed_0788 Ssed_3049
            SPL: Spea_1378 Spea_3549
            SHE: Shewmr4_0589
            SHM: Shewmr7_3441
            SHN: Shewana3_0588
            SHW: Sputw3181_0652
            ILO: IL2302(psd)
            CPS: CPS_4381(psd)
            PHA: PSHAa0486(psd)
            PAT: Patl_3483
            SDE: Sde_2679
            PIN: Ping_3337
            MAQ: Maqu_2780
            CBU: CBU_1826(psd)
            CBD: COXBU7E912_0055(psd)
            LPN: lpg2974(psd)
            LPF: lpl2903(psd)
            LPP: lpp3046(psd)
            MCA: MCA1409(psd)
            FTU: FTT0384c(psd)
            FTF: FTF0384c(psd)
            FTW: FTW_1690(psd)
            FTL: FTL_0450
            FTH: FTH_0447(psd)
            FTA: FTA_0476(psd)
            FTN: FTN_0481(psd)
            TCX: Tcr_0913
            NOC: Noc_2896
            AEH: Mlg_0862
            HHA: Hhal_0824
            HCH: HCH_05397(psd)
            CSA: Csal_2529
            ABO: ABO_2213(psd)
            MMW: Mmwyl1_2643 Mmwyl1_3428
            AHA: AHA_3461(psd) AHA_4084
            DNO: DNO_1101(psd)
            BCI: BCI_0587(psd)
            RMA: Rmag_0349
            VOK: COSY_0330(psd)
            NME: NMB0963
            NMA: NMA1160
            NGO: NGO1206(psd)
            CVI: CV_0591(psd)
            RSO: RSc2074(RS03639)
            REU: Reut_A0950
            REH: H16_A1038(psd)
            RME: Rmet_0915 Rmet_4116
            BMA: BMA1845 BMAA1997
            BMV: BMASAVP1_A1116(psd)
            BML: BMA10299_A0750(psd)
            BMN: BMA10247_0399(psd)
            BXE: Bxe_A3228
            BVI: Bcep1808_2346
            BUR: Bcep18194_A5589
            BCN: Bcen_1338 Bcen_1651
            BCH: Bcen2424_2262 Bcen2424_6491
            BAM: Bamb_2300
            BPS: BPSL1199 BPSS2261
            BPM: BURPS1710b_1422 BURPS1710b_A1394
            BPL: BURPS1106A_1284(psd)
            BPD: BURPS668_1277(psd)
            BTE: BTH_I1048
            PNU: Pnuc_1060
            BPE: BP1294(psd)
            BPA: BPP2924(psd)
            BBR: BB2894(psd)
            RFR: Rfer_0607
            POL: Bpro_4870
            PNA: Pnap_4088
            AAV: Aave_2955
            AJS: Ajs_1668
            VEI: Veis_1650
            MPT: Mpe_A2796
            HAR: HEAR1445(psd)
            MMS: mma_1900
            NEU: NE1322(psd)
            NET: Neut_1259
            NMU: Nmul_A0681
            EBA: ebA7135(psd)
            AZO: azo3549(psd)
            DAR: Daro_2876
            TBD: Tbd_1988
            MFA: Mfla_2122
            HPY: HP1357
            HPA: HPAG1_0925 HPAG1_1304
            HHE: HH1838(psd)
            HAC: Hac_0198(psd)
            WSU: WS1275
            TDN: Tmden_1033 Tmden_1669
            CJE: Cj0847(psd) Cj1115c
            CJR: CJE0934(psd) CJE1258
            CJJ: CJJ81176_0863(psd)
            CJU: C8J_0794(psd) C8J_1056
            CJD: JJD26997_0997(psd)
            CFF: CFF8240_1154(psd) CFF8240_1346(psd)
            CCV: CCV52592_1195(psd) CCV52592_1320(psd)
            CHA: CHAB381_1384(psd)
            CCO: CCC13826_0440(psd) CCC13826_0474 CCC13826_0525
                 CCC13826_1554(psd)
            ABU: Abu_2192(psd)
            NIS: NIS_0802
            SUN: SUN_1079
            GSU: GSU1908
            GME: Gmet_1263 Gmet_1483
            GUR: Gura_3717 Gura_4108
            PCA: Pcar_1908 Pcar_2301
            PPD: Ppro_2554
            DVU: DVU2979
            DVL: Dvul_0393
            DDE: Dde_3216
            LIP: LI0776(psd)
            BBA: Bd1861(psd)
            DPS: DP0234 DP2771
            ADE: Adeh_1509
            AFW: Anae109_2314
            MXA: MXAN_3724(psd)
            SAT: SYN_00913
            SFU: Sfum_2902 Sfum_2985 Sfum_3027
            RPR: RP241
            RTY: RT0233(psd)
            RCO: RC0325(psd)
            RFE: RF_1046(psd)
            RBE: RBE_0969(psd)
            RAK: A1C_01765
            RBO: A1I_03810
            RCM: A1E_01415
            RRI: A1G_01860
            OTS: OTBS_0145(psd)
            WOL: WD1049
            WBM: Wbm0426
            AMA: AM463(psd)
            APH: APH_0544
            ERU: Erum3170(psd)
            ERW: ERWE_CDS_03220(psd)
            ERG: ERGA_CDS_03170(psd)
            ECN: Ecaj_0296
            ECH: ECH_0779(psd)
            NSE: NSE_0248
            PUB: SAR11_0645(psd2)
            MLO: mlr7821
            MES: Meso_0978
            PLA: Plav_1114
            SME: SMc00551
            SMD: Smed_0723 Smed_1251 Smed_1252
            ATU: Atu1063(psd)
            ATC: AGR_C_1963
            RET: RHE_CH01411(psd)
            RLE: RL1533(psd)
            BME: BMEI1491
            BMF: BAB1_0469
            BMS: BR0443
            BMB: BruAb1_0465
            OAN: Oant_0556
            BJA: bll6631 blr3796
            BRA: BRADO4692(psd) BRADO5693
            BBT: BBta_3505(psd) BBta_6208
            RPA: RPA2006(psd)
            RPB: RPB_3367
            RPC: RPC_2095
            RPD: RPD_2075
            RPE: RPE_2008
            NWI: Nwi_0699 Nwi_1234
            NHA: Nham_1493
            BHE: BH05210(psdA)
            BQU: BQ04400(psdA)
            BBK: BARBAKC583_0483(psd)
            XAU: Xaut_4662
            SIL: SPOA0292(psd)
            SIT: TM1040_3084
            RSP: RSP_0719
            RSH: Rsph17029_2374
            RSQ: Rsph17025_2438
            PDE: Pden_4692
            ZMO: ZMO1160(psd)
            NAR: Saro_1366
            SAL: Sala_1963
            SWI: Swit_0458
            ELI: ELI_03750 ELI_11985
            GOX: GOX0282
            GBE: GbCGDNIH1_0341
            ACR: Acry_0264 Acry_2687
            RRU: Rru_A3585
            MAG: amb0604
            MGM: Mmc1_0901
            ABA: Acid345_2360
            SUS: Acid_1717
            BSU: BG11013(psd)
            BHA: BH1311(psd)
            BAN: BA4565(psd)
            BAR: GBAA4565(psd)
            BAA: BA_5008
            BAT: BAS4235
            BCE: BC4335
            BCA: BCE_4419(psd)
            BCZ: BCZK4083(psd)
            BCY: Bcer98_3064
            BTK: BT9727_4073(psd)
            BTL: BALH_3925(psd)
            BLI: BL02542(psd)
            BLD: BLi03339(psd)
            BAY: RBAM_002720
            GKA: GK2528
            SSA: SSA_1014
            SGO: SGO_0938
            STH: STH1715
            CAC: CAC0031(psdD) CAC0799(psd)
            CPE: CPE0028(psdD)
            CPF: CPF_0033(psd)
            CPR: CPR_0033(psd)
            CTC: CTC00080
            CNO: NT01CX_0831
            CBO: CBO0025(psd2)
            CBA: CLB_0034(psd)
            CBH: CLC_0042(psd-2)
            CBF: CLI_0038(psd)
            CBE: Cbei_0018 Cbei_4249
            CKL: CKL_0049(psd)
            AMT: Amet_2694 Amet_4198
            CHY: CHY_0921(psd)
            DSY: DSY2396
            DRM: Dred_0445
            CSC: Csac_1285
            MTA: Moth_0455
            POY: PAM612(psd)
            AYW: AYWB_121(psd)
            MTU: Rv0437c(psd)
            MTC: MT0453
            MBO: Mb0445c(psd)
            MBB: BCG_0476c(psd)
            MLE: ML0311
            MPA: MAP3930c(psd)
            MAV: MAV_4713(psd)
            MSM: MSMEG_0861(psd)
            MVA: Mvan_0751
            MGI: Mflv_0153
            MMC: Mmcs_0594
            MKM: Mkms_0607
            MJL: Mjls_0585
            NFA: nfa52810(psd)
            RHA: RHA1_ro02159(psd)
            SCO: SCO6468(SC9C7.04c)
            SMA: SAV1916(psd)
            TFU: Tfu_1894
            KRA: Krad_1411
            SEN: SACE_0521(psd)
            STP: Strop_3828
            RXY: Rxyl_0288
            FNU: FN0347
            RBA: RB3822(psd) RB8482(psd)
            CTR: CT699(psdD)
            CTA: CTA_0760(psdD)
            CMU: TC0072
            CPN: CPn0839(psdD)
            CPA: CP1030
            CPJ: CPj0839(psdD)
            CPT: CpB0868
            CCA: CCA00927(psd)
            CAB: CAB896
            CFE: CF0087(psdD)
            PCU: pc0023(psdD)
            LIL: LA2616
            BTH: BT_2231
            BFR: BF0711
            BFS: BF0640
            PGI: PG0965
            SRU: SRU_0961
            CHU: CHU_0357(psd)
            GFO: GFO_2697(psd)
            FJO: Fjoh_2597
            FPS: FP0606(psd)
            CTE: CT1615
            CCH: Cag_1747
            CPH: Cpha266_0578
            PVI: Cvib_1400
            PLT: Plut_1610
            DRA: DR_1574
            TTH: TTC0815
            MJA: MJ0817
            MAE: Maeo_0348
            MAC: MA0115(psd)
            MBA: Mbar_A0875
            MMA: MM_1402
            MBU: Mbur_2197
            MKA: MK0162(psd)
            HAL: VNG2255C
            HWA: HQ3406A(psd)
            NPH: NP4176A(psd)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.65
            ExPASy - ENZYME nomenclature database: 4.1.1.65
            ExplorEnz - The Enzyme Database: 4.1.1.65
            ERGO genome analysis and discovery system: 4.1.1.65
            BRENDA, the Enzyme Database: 4.1.1.65
            CAS: 9054-78-8
///
ENTRY       EC 4.1.1.66                 Enzyme
NAME        uracil-5-carboxylate decarboxylase;
            uracil-5-carboxylic acid decarboxylase;
            uracil-5-carboxylate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     uracil-5-carboxylate carboxy-lyase (uracil-forming)
REACTION    uracil 5-carboxylate = uracil + CO2 [RN:R00973]
ALL_REAC    R00973
SUBSTRATE   uracil 5-carboxylate [CPD:C03030]
PRODUCT     uracil [CPD:C00106];
            CO2 [CPD:C00011]
REFERENCE   1  [PMID:5482775]
  AUTHORS   Palmatier RD, McCroskey RP, Abbott MT.
  TITLE     The enzymatic conversion of uracil 5-carboxylic acid to uracil and
            carbon dioxide.
  JOURNAL   J. Biol. Chem. 245 (1970) 6706-10.
  ORGANISM  Neurospora crassa [GN:dncr]
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.66
            ExPASy - ENZYME nomenclature database: 4.1.1.66
            ExplorEnz - The Enzyme Database: 4.1.1.66
            ERGO genome analysis and discovery system: 4.1.1.66
            BRENDA, the Enzyme Database: 4.1.1.66
            CAS: 59299-01-3
///
ENTRY       EC 4.1.1.67                 Enzyme
NAME        UDP-galacturonate decarboxylase;
            UDP-galacturonic acid decarboxylase;
            UDPGalUA carboxy lyase;
            UDP-D-galacturonate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     UDP-D-galacturonate carboxy-lyase (UDP-L-arabinose-forming)
REACTION    UDP-D-galacturonate = UDP-L-arabinose + CO2 [RN:R02636]
ALL_REAC    R02636
SUBSTRATE   UDP-D-galacturonate [CPD:C00617]
PRODUCT     UDP-L-arabinose [CPD:C00935];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Fan, D.-F. and Feingold, D.S.
  TITLE     UDPgalacturonic acid decarboxylase from Ampullariella digitata.
  JOURNAL   Methods Enzymol. 28B (1972) 438-439.
  ORGANISM  Ampullariella digitata
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.67
            ExPASy - ENZYME nomenclature database: 4.1.1.67
            ExplorEnz - The Enzyme Database: 4.1.1.67
            ERGO genome analysis and discovery system: 4.1.1.67
            BRENDA, the Enzyme Database: 4.1.1.67
            CAS: 9054-79-9
///
ENTRY       EC 4.1.1.68                 Enzyme
NAME        5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase;
            5-carboxymethyl-2-oxo-hex-3-ene-1,6-dioate decarboxylase;
            5-oxopent-3-ene-1,2,5-tricarboxylate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     5-oxopent-3-ene-1,2,5-tricarboxylate carboxy-lyase
            (2-oxohept-3-enedioate-forming)
REACTION    5-oxopent-3-ene-1,2,5-tricarboxylate = 2-oxohept-3-enedioate + CO2
            [RN:R04133]
ALL_REAC    R04133;
            (other) R04380
SUBSTRATE   5-oxopent-3-ene-1,2,5-tricarboxylate [CPD:C04052]
PRODUCT     2-oxohept-3-enedioate [CPD:C03063];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Garrido-Pertierra, A. and Cooper, R.A.
  TITLE     Identification and purification of distinct isomerase and
            decarboxylase enzymes involved in the 4-hydroxyphenylacetate pathway
            of Escherichia coli.
  JOURNAL   Eur. J. Biochem. 117 (1981) 581-584.
PATHWAY     PATH: map00350  Tyrosine metabolism
ORTHOLOGY   KO: K01614  5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase
            KO: K05921  5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase /
                        2-hydroxyhepta-2,4-diene-1,7-dioate isomerase
GENES       ECX: EcHS_A4584(hpaG)
            STY: STY1134(hpaG)
            STT: t1818(hpaG)
            SEC: SC1051(hpaG)
            STM: STM1101(hpaG)
            YPS: YPTB1637(hpaG) YPTB1638
            YPI: YpsIP31758_2364(hpaG2) YpsIP31758_2365(hpaG1)
            SFL: SF4384(hpaG)
            SFX: S4654(hpaG)
            SFV: SFV_4384(hpaG)
            SSN: SSON_4499(hpaG)
            SBO: SBO_4412(hpaG)
            PLU: plu0989(hpaG2)
            ENT: Ent638_3376
            SPE: Spro_4625
            PMU: PM1528(hpaG_1) PM1529(hpaG_2)
            VVY: VV1584
            PAE: PA4121 PA4122
            PFL: PFL_3370
            PEN: PSEEN3092(hpaG-1) PSEEN3093(hpaG-2)
            SDE: Sde_2486
            MMW: Mmwyl1_0866 Mmwyl1_3176 Mmwyl1_3177
            REU: Reut_B4678 Reut_C6233
            BMA: BMAA1139
            BML: BMA10299_0100 BMA10299_0101
            BMN: BMA10247_A1512 BMA10247_A1513
            BXE: Bxe_B2028 Bxe_B2029
            BVI: Bcep1808_3385 Bcep1808_3682
            BUR: Bcep18194_B0137 Bcep18194_B1336 Bcep18194_B1888
                 Bcep18194_C7653
            BCN: Bcen_4893
            BCH: Bcen2424_0160 Bcen2424_3270
            BAM: Bamb_3654 Bamb_4305
            BPS: BPSS0693
            BPM: BURPS1710b_A2263(hpaG) BURPS1710b_A2264(hpaG)
            BPL: BURPS1106A_A0938 BURPS1106A_A0939
            BPD: BURPS668_A1023 BURPS668_A1024
            BTE: BTH_II1734(hpaG-1) BTH_II1735(hpaG-2)
            PNU: Pnuc_1328
            RFR: Rfer_3133
            POL: Bpro_1710
            VEI: Veis_1085
            HAR: HEAR0345
            DDE: Dde_1138
            ADE: Adeh_4067
            AFW: Anae109_0356
            PLA: Plav_0169 Plav_1540
            SMD: Smed_4970
            RLE: pRL120236
            BRA: BRADO2592 BRADO5118 BRADO6046
            BBT: BBta_2938 BBta_5587
            RPB: RPB_4234
            RPD: RPD_3593
            RPE: RPE_4326
            SAL: Sala_1386
            SWI: Swit_3084 Swit_4227 Swit_4308 Swit_4309
            RRU: Rru_A2126
            ABA: Acid345_0177
            SUS: Acid_4970
            BCY: Bcer98_0971 Bcer98_0972
            BCL: ABC2173
            OIH: OB2865 OB2866
            GKA: GK3030 GK3031
            MSM: MSMEG_2382
            MVA: Mvan_2132
            MMC: Mmcs_1918
            MKM: Mkms_1964
            MJL: Mjls_1898
            ART: Arth_3520
            NCA: Noca_0211
            SEN: SACE_6150
            STP: Strop_1256
            RXY: Rxyl_1029
            FJO: Fjoh_4120
            DRA: DR_A0226
            TTH: TTC0592
            TTJ: TTHA0958
            MMP: MMP0144(hpcE)
            MMQ: MmarC5_1531
            MAE: Maeo_1498
            MVN: Mevan_1149
            MBU: Mbur_2333
            HWA: HQ1722A(hcpE) HQ3367A(hcpE)
            NPH: NP2134A(hcpE_1) NP2562A(hcpE_3) NP4386A(hcpE_2)
            PIS: Pisl_0039
            PAS: Pars_0535 Pars_1390
STRUCTURES  PDB: 1I7O  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.68
            ExPASy - ENZYME nomenclature database: 4.1.1.68
            ExplorEnz - The Enzyme Database: 4.1.1.68
            ERGO genome analysis and discovery system: 4.1.1.68
            UM-BBD (Biocatalysis/Biodegradation Database): 4.1.1.68
            BRENDA, the Enzyme Database: 4.1.1.68
///
ENTRY       EC 4.1.1.69                 Enzyme
NAME        3,4-dihydroxyphthalate decarboxylase;
            3,4-dihydroxyphthalate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     3,4-dihydroxyphthalate carboxy-lyase (3,4-dihydroxybenzoate-forming)
REACTION    3,4-dihydroxyphthalate = 3,4-dihydroxybenzoate + CO2 [RN:R01634]
ALL_REAC    R01634
SUBSTRATE   3,4-dihydroxyphthalate [CPD:C03223]
PRODUCT     3,4-dihydroxybenzoate [CPD:C00230];
            CO2 [CPD:C00011]
REFERENCE   1  [PMID:7085570]
  AUTHORS   Eaton RW, Ribbons DW.
  TITLE     Metabolism of dibutylphthalate and phthalate by Micrococcus sp.
            strain 12B.
  JOURNAL   J. Bacteriol. 151 (1982) 48-57.
  ORGANISM  Micrococcus sp.
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.69
            ExPASy - ENZYME nomenclature database: 4.1.1.69
            ExplorEnz - The Enzyme Database: 4.1.1.69
            ERGO genome analysis and discovery system: 4.1.1.69
            BRENDA, the Enzyme Database: 4.1.1.69
            CAS: 83137-76-2
///
ENTRY       EC 4.1.1.70                 Enzyme
NAME        glutaconyl-CoA decarboxylase;
            glutaconyl coenzyme A decarboxylase;
            pent-2-enoyl-CoA carboxy-lyase;
            4-carboxybut-2-enoyl-CoA carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     4-carboxybut-2-enoyl-CoA carboxy-lyase (but-2-enoyl-CoA-forming)
REACTION    4-carboxybut-2-enoyl-CoA = but-2-enoyl-CoA + CO2 [RN:R03028]
ALL_REAC    R03028
SUBSTRATE   4-carboxybut-2-enoyl-CoA [CPD:C02411]
PRODUCT     but-2-enoyl-CoA [CPD:C00877];
            CO2 [CPD:C00011]
COMMENT     The enzyme from Acidaminococcus fermentans is a biotinyl-protein,
            requires Na+, and acts as a sodium pump. Prior to the Na+-dependent
            decarboxylation, the carboxylate is transferred to biotin in a
            Na+-independent manner. The conserved lysine, to which biotin forms
            an amide bond, is located 34 amino acids before the C-terminus,
            flanked on both sides by two methionine residues, which are
            conserved in every biotin-dependent enzyme.
REFERENCE   1  [PMID:6628393]
  AUTHORS   Buckel W, Semmler R.
  TITLE     Purification, characterisation and reconstitution of glutaconyl-CoA
            decarboxylase, a biotin-dependent sodium pump from anaerobic
            bacteria.
  JOURNAL   Eur. J. Biochem. 136 (1983) 427-34.
  ORGANISM  Acidaminococcus fermentans, Peptococcus aerogenes, Clostridium
            symbiosum, Clostridium tetanomorphum
REFERENCE   2  [PMID:11248185]
  AUTHORS   Buckel W.
  TITLE     Sodium ion-translocating decarboxylases.
  JOURNAL   Biochim. Biophys. Acta. 1505 (2001) 15-27.
  ORGANISM  Acidaminococcus fermentans
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
            PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K01615  glutaconyl-CoA decarboxylase
GENES       ASU: Asuc_0301
            PMY: Pmen_2892
            SBM: Shew185_1093
            SSE: Ssed_1322
            SPL: Spea_1200
            MMW: Mmwyl1_3622
            SAT: SYN_00479 SYN_00481 SYN_01431
            RRU: Rru_A3673
            SPF: SpyM50900 SpyM50901
            CTH: Cthe_0509
            AMT: Amet_3216 Amet_4535
            CSC: Csac_2482
            FNU: FN0200 FN0201 FN0204
            RRS: RoseRS_3692
            RCA: Rcas_0953
            TPT: Tpet_0047
            TME: Tmel_1898
            FNO: Fnod_1275 Fnod_1310
            SMR: Smar_1504
STRUCTURES  PDB: 1PIX  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.70
            ExPASy - ENZYME nomenclature database: 4.1.1.70
            ExplorEnz - The Enzyme Database: 4.1.1.70
            ERGO genome analysis and discovery system: 4.1.1.70
            UM-BBD (Biocatalysis/Biodegradation Database): 4.1.1.70
            BRENDA, the Enzyme Database: 4.1.1.70
            CAS: 84399-93-9
///
ENTRY       EC 4.1.1.71                 Enzyme
NAME        2-oxoglutarate decarboxylase;
            oxoglutarate decarboxylase;
            alpha-ketoglutarate decarboxylase;
            alpha-ketoglutaric decarboxylase;
            oxoglutarate decarboxylase;
            pre-2-oxoglutarate decarboxylase;
            2-oxoglutarate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     2-oxoglutarate carboxy-lyase (succinate-semialdehyde-forming)
REACTION    2-oxoglutarate = succinate semialdehyde + CO2 [RN:R00272]
ALL_REAC    R00272;
            (other) R00622
SUBSTRATE   2-oxoglutarate [CPD:C00026]
PRODUCT     succinate semialdehyde [CPD:C00232];
            CO2 [CPD:C00011]
COFACTOR    Thiamin diphosphate [CPD:C00068]
COMMENT     Requires thiamine diphosphate. Highly specific.
REFERENCE   1
  AUTHORS   Shigeoka, S., Onishi, T., Maeda, K., Nakano, Y. and Kitaoka, S.
  TITLE     Occurrence of thiamin pyrophosphate-dependent 2-oxoglutarate
            decarboxylase in mitochondria of Euglena gracilis.
  JOURNAL   FEBS Lett. 195 (1986) 43-47.
  ORGANISM  Euglena gracilis
ORTHOLOGY   KO: K01616  
GENES       ECW: EcE24377A_2560(menD)
            ECX: EcHS_A2410
            YPI: YpsIP31758_1482(menD)
            ENT: Ent638_2814
            SPE: Spro_3283
            VCO: VC0395_A1561(menD)
            SAZ: Sama_3460
            SBL: Sbal_0178
            SLO: Shew_3599
            SPC: Sputcn32_0310
            SHW: Sputw3181_3898
            PIN: Ping_0352
            AHA: AHA_0531(menD)
            MXA: MXAN_3528(menD)
            BAY: RBAM_027800
            BPU: BPUM_2718
            GKA: GK2875
            SAC: SACOL1052(menD)
            SAA: SAUSA300_0946(menD)
            SAO: SAOUHSC_00983
            SER: SERP0630(menD)
            LWE: lwe1693(menD)
            LLM: llmg_1829(menD)
            MBB: BCG_0600(menD) BCG_1308c(kgd)
            MVA: Mvan_0975
            MMC: Mmcs_0751
            MKM: Mkms_0765
            MJL: Mjls_0745
            CGB: cg0552(menD)
            CJK: jk1868(menD)
            RHA: RHA1_ro01997(menD)
            AAU: AAur_3107(menD)
            NCA: Noca_0510
            TFU: Tfu_1411
            SEN: SACE_6913(menD)
            SYR: SynRCC307_1140(menD)
            SYX: SynWH7803_1021(menD)
            CYA: CYA_0082(menD)
            CYB: CYB_2045(menD)
            AVA: Ava_4706
            PMN: PMN2A_0043
            PMB: A9601_06631(menD)
            PMC: P9515_06721(menD)
            PMF: P9303_18801(menD)
            PMG: P9301_06331(menD)
            PMH: P9215_06891
            PME: NATL1_06631(menD)
            TER: Tery_4077
            SRU: SRU_1351(menD)
            FJO: Fjoh_2781
            FPS: FP1676(menD)
            CCH: Cag_1700
            HWA: HQ1873A(menD)
            NPH: NP2726A(menD)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.71
            ExPASy - ENZYME nomenclature database: 4.1.1.71
            ExplorEnz - The Enzyme Database: 4.1.1.71
            ERGO genome analysis and discovery system: 4.1.1.71
            BRENDA, the Enzyme Database: 4.1.1.71
            CAS: 37205-42-8
///
ENTRY       EC 4.1.1.72                 Enzyme
NAME        branched-chain-2-oxoacid decarboxylase;
            branched-chain oxo acid decarboxylase;
            branched-chain alpha-keto acid decarboxylase;
            branched-chain keto acid decarboxylase;
            BCKA;
            (3S)-3-methyl-2-oxopentanoate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     (3S)-3-methyl-2-oxopentanoate carboxy-lyase
            (2-methylbutanal-forming)
REACTION    (3S)-3-methyl-2-oxopentanoate = 2-methylbutanal + CO2 [RN:R03894]
ALL_REAC    R03894
SUBSTRATE   (3S)-3-methyl-2-oxopentanoate [CPD:C00671]
PRODUCT     2-methylbutanal [CPD:C02223];
            CO2 [CPD:C00011]
COMMENT     Acts on a number of 2-oxo acids, with a high affinity towards
            branched-chain substrates. The aldehyde formed may be enzyme-bound,
            and may be an intermediate in the bacterial system for the
            biosynthesis of branched-chain fatty acids.
REFERENCE   1  [PMID:3142877]
  AUTHORS   Oku H, Kaneda T.
  TITLE     Biosynthesis of branched-chain fatty acids in Bacillus subtilis. A
            decarboxylase is essential for branched-chain fatty acid synthetase.
  JOURNAL   J. Biol. Chem. 263 (1988) 18386-96.
  ORGANISM  Bacillus subtilis [GN:bsu]
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.72
            ExPASy - ENZYME nomenclature database: 4.1.1.72
            ExplorEnz - The Enzyme Database: 4.1.1.72
            ERGO genome analysis and discovery system: 4.1.1.72
            BRENDA, the Enzyme Database: 4.1.1.72
            CAS: 63653-19-0
///
ENTRY       EC 4.1.1.73                 Enzyme
NAME        tartrate decarboxylase;
            (R,R)-tartrate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     (R,R)-tartrate carboxy-lyase (D-glycerate-forming)
REACTION    (R,R)-tartrate = D-glycerate + CO2 [RN:R01751]
ALL_REAC    R01751
SUBSTRATE   (R,R)-tartrate [CPD:C00898]
PRODUCT     D-glycerate [CPD:C00258];
            CO2 [CPD:C00011]
REFERENCE   1
  AUTHORS   Furuyoshi, S., Kawabata, N., Tanaka, H. and Soda, K.
  TITLE     Enzymatic production of D-glycerate from L-tartrate.
  JOURNAL   Agric. Biol. Chem. 53 (1989) 2101-2105.
  ORGANISM  Pseudomonas sp.
ORTHOLOGY   KO: K07247  tartrate decarboxylase
GENES       ECO: b1800(yeaU)
            ECJ: JW1789(yeaU)
            ECE: Z2843(yeaU)
            ECS: ECs2509
            ECW: EcE24377A_2026(ttuC)
            ECX: EcHS_A1888(ttuC)
            YPE: YPO2496
            YPM: YP_2311(leuB1)
            YPA: YPA_1991
            YPN: YPN_2090
            YPS: YPTB2532
            SSN: SSON_1361(yeaU)
            SBO: SBO_1288(yeaU)
            SDY: SDY_1701(yeaU)
            MSU: MS1105(leuB)
            PST: PSPTO_2662
            PSB: Psyr_2396
            PSP: PSPPH_2554
            PEN: PSEEN2132
            ABO: ABO_0510(tdh)
            RSO: RSp1612(ttuC)
            REU: Reut_B4115
            RME: Rmet_0404
            BMA: BMAA0011(ttuC)
            BPS: BPSS0011
            BPM: BURPS1710b_A1518
            BPE: BP2291
            BPA: BPP4066
            BBR: BB4539
            RFR: Rfer_2247
            POL: Bpro_3066
            MLO: mll7044
            PLA: Plav_0534
            SME: SMa1846
            ATU: Atu3402
            ATC: AGR_L_2841
            BJA: blr2916
            BRA: BRADO2534(yeaU) BRADO5094(ttuC)
            BBT: BBta_2879(yeaU) BBta_5565(ttuC)
            RPA: RPA1742(yeaU)
            RSP: RSP_3389 RSP_4031
            ACR: Acry_0647
            BSU: BG11222(ycsA)
            BHA: BH1070
            BCY: Bcer98_0765
            BLI: BL03389(ycsA)
            BLD: BLi03766(ycsA)
            OIH: OB0661
            STH: STH2344
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.73
            ExPASy - ENZYME nomenclature database: 4.1.1.73
            ExplorEnz - The Enzyme Database: 4.1.1.73
            ERGO genome analysis and discovery system: 4.1.1.73
            BRENDA, the Enzyme Database: 4.1.1.73
            CAS: 124248-30-2
///
ENTRY       EC 4.1.1.74                 Enzyme
NAME        indolepyruvate decarboxylase;
            indol-3-yl-pyruvate carboxy-lyase;
            3-(indol-3-yl)pyruvate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     3-(indol-3-yl)pyruvate carboxy-lyase
            [(2-indol-3-yl)acetaldehyde-forming]
REACTION    3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO2
            [RN:R01974]
ALL_REAC    R01974
SUBSTRATE   3-(indol-3-yl)pyruvate [CPD:C00331]
PRODUCT     2-(indol-3-yl)acetaldehyde [CPD:C00637];
            CO2 [CPD:C00011]
COMMENT     Thiamine diphosphate- and Mg2+-dependent. More specific than EC
            4.1.1.1 pyruvate decarboxylase
REFERENCE   1  [PMID:7766676]
  AUTHORS   Koga J.
  TITLE     Structure and function of indolepyruvate decarboxylase, a key enzyme
            in indole-3-acetic acid biosynthesis.
  JOURNAL   Biochim. Biophys. Acta. 1249 (1995) 1-13.
  ORGANISM  Enterobacter cloacae
PATHWAY     PATH: map00380  Tryptophan metabolism
ORTHOLOGY   KO: K04103  indolepyruvate decarboxylase
GENES       LMA: LmjF34.3250
            YEN: YE1222(ipdC)
            ECA: ECA3605(ipdC)
            FTU: FTT1744c(ipdC)
            FTF: FTF1744c(ipdC)
            FTL: FTL_0006
            FTN: FTN_0116(ipdC)
            REH: H16_B1399(ipdC)
            BXE: Bxe_B0109
            RFR: Rfer_0518
            DDE: Dde_2331
            BRA: BRADO7016(ipdC)
            BBT: BBta_0512(ipdC)
            RPA: RPA3116(ipdC)
            RPB: RPB_2425
            RPD: RPD_3027
            RRU: Rru_A2719
            BAN: BA2486
            BAR: GBAA2486
            BAA: BA_2981
            BAT: BAS2311
            BCE: BC2433
            BCA: BCE_2517
            BCZ: BCZK2232
            BTK: BT9727_2279
            BTL: BALH_2224 BALH_2225 BALH_2238
            SAC: SACOL0173(ipdC)
            SAA: SAUSA300_0190(ipdC)
            SER: SERP2242(ipdC)
            MAV: MAV_0973
            MSM: MSMEG_5735
            SYG: sync_1491
            SYX: SynWH7803_0869(pdc)
            AVA: Ava_4114
STRUCTURES  PDB: 1OVM  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.74
            ExPASy - ENZYME nomenclature database: 4.1.1.74
            ExplorEnz - The Enzyme Database: 4.1.1.74
            ERGO genome analysis and discovery system: 4.1.1.74
            BRENDA, the Enzyme Database: 4.1.1.74
            CAS: 9074-92-4
///
ENTRY       EC 4.1.1.75                 Enzyme
NAME        5-guanidino-2-oxopentanoate decarboxylase;
            alpha-ketoarginine decarboxylase;
            2-oxo-5-guanidinopentanoate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     5-guanidino-2-oxo-pentanoate carboxy-lyase
            (4-guanidinobutanal-forming)
REACTION    5-guanidino-2-oxo-pentanoate = 4-guanidinobutanal + CO2 [RN:R03178]
ALL_REAC    R03178
SUBSTRATE   5-guanidino-2-oxo-pentanoate [CPD:C03771]
PRODUCT     4-guanidinobutanal [CPD:C02647];
            CO2 [CPD:C00011]
COFACTOR    Thiamin diphosphate [CPD:C00068];
            Divalent cation [CPD:C00572]
COMMENT     Enzyme activity is dependent on the presence of thiamine diphosphate
            and a divalent cation.
REFERENCE   1  [PMID:237915]
  AUTHORS   Vanderbilt AS, Gaby NS, Rodwell VW.
  TITLE     Intermediates and enzymes between alpha-ketoarginine and
            gamma-guanidinobutyrate in the L-arginine catabolic pathway of
            Pseudomonas putida.
  JOURNAL   J. Biol. Chem. 250 (1975) 5322-9.
  ORGANISM  Pseudomonas putida [GN:ppu]
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.75
            ExPASy - ENZYME nomenclature database: 4.1.1.75
            ExplorEnz - The Enzyme Database: 4.1.1.75
            ERGO genome analysis and discovery system: 4.1.1.75
            BRENDA, the Enzyme Database: 4.1.1.75
            CAS: 56831-67-5
///
ENTRY       EC 4.1.1.76                 Enzyme
NAME        arylmalonate decarboxylase;
            AMDASE;
            2-aryl-2-methylmalonate carboxy-lyase;
            2-aryl-2-methylmalonate carboxy-lyase (2-arylpropionate-forming)
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     2-aryl-2-methylmalonate carboxy-lyase (2-arylpropanoate-forming)
REACTION    2-aryl-2-methylmalonate = 2-arylpropanoate + CO2 [RN:R05173]
ALL_REAC    R05173
SUBSTRATE   2-aryl-2-methylmalonate [CPD:C06388]
PRODUCT     2-arylpropanoate;
            CO2 [CPD:C00011]
REFERENCE   1  [PMID:1369144]
  AUTHORS   Miyamoto K, Ohta H.
  TITLE     Cloning and heterologous expression of a novel arylmalonate
            decarboxylase gene from Alcaligenes bronchisepticus KU 1201.
  JOURNAL   Appl. Microbiol. Biotechnol. 38 (1992) 234-8.
  ORGANISM  Alcaligenes bronchisepticus
ORTHOLOGY   KO: K06033  
GENES       BUR: Bcep18194_B0631
            BPE: BP3498
            BPA: BPP0871
            BBR: BB0965
            RLE: pRL120051
            AVA: Ava_4999
STRUCTURES  PDB: 2DGD  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.76
            ExPASy - ENZYME nomenclature database: 4.1.1.76
            ExplorEnz - The Enzyme Database: 4.1.1.76
            ERGO genome analysis and discovery system: 4.1.1.76
            BRENDA, the Enzyme Database: 4.1.1.76
            CAS: 144713-36-0
///
ENTRY       EC 4.1.1.77                 Enzyme
NAME        4-oxalocrotonate decarboxylase;
            4-oxalocrotonate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     4-oxalocrotonate carboxy-lyase (2-oxopent-4-enoate-forming)
REACTION    4-oxalocrotonate = 2-oxopent-4-enoate + CO2 [RN:R02602]
ALL_REAC    R02602;
            (other) R05374
SUBSTRATE   4-oxalocrotonate [CPD:C03453]
PRODUCT     2-oxopent-4-enoate [CPD:C00596];
            CO2 [CPD:C00011]
COMMENT     Involved in the meta-cleavage pathway for the degradation of
            phenols, cresols and catechols
REFERENCE   1  [PMID:1732207]
  AUTHORS   Shingler V, Powlowski J, Marklund U.
  TITLE     Nucleotide sequence and functional analysis of the complete
            phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp.
            strain CF600.
  JOURNAL   J. Bacteriol. 174 (1992) 711-24.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00622  Toluene and xylene degradation
            PATH: map00628  Fluorene degradation
ORTHOLOGY   KO: K01617  4-oxalocrotonate decarboxylase
GENES       YPP: YPDSF_1357
            SPE: Spro_0630
            PPF: Pput_2875 Pput_2890
            SPL: Spea_2118
            PHA: PSHAa2141(xylJ)
            AEH: Mlg_2460
            MMW: Mmwyl1_3178
            RSO: RS01663(RSp0892)
            REU: Reut_A0272 Reut_A1510 Reut_B5220 Reut_B5499 Reut_B5500
                 Reut_B5691 Reut_B5692 Reut_C5928
            REH: H16_B0549
            RME: Rmet_5210
            BXE: Bxe_A1150(amnE)
            BVI: Bcep1808_4806 Bcep1808_5386 Bcep1808_7603 Bcep1808_7606
            BUR: Bcep18194_B1186 Bcep18194_B1459 Bcep18194_B1778
                 Bcep18194_B2958 Bcep18194_B2961 Bcep18194_C7643
                 Bcep18194_C7646
            POL: Bpro_0971 Bpro_1476 Bpro_5137
            PNA: Pnap_4144
            AAV: Aave_4269
            AJS: Ajs_0222 Ajs_0225
            VEI: Veis_2410 Veis_2784 Veis_2785
            MPT: Mpe_A3324
            AZO: azo1854(lapH) azo2430(nahK)
            MXA: MXAN_0925
            PLA: Plav_1790
            RET: RHE_CH02299
            RLE: pRL120704
            BRA: BRADO5041
            BBT: BBta_5513
            XAU: Xaut_0936
            SWI: Swit_0911 Swit_0912 Swit_1639 Swit_2111 Swit_3088 Swit_3520
                 Swit_3521 Swit_4271 Swit_4313 Swit_4925 Swit_5040
            BCA: BCE_2158
            BTL: BALH_1845
            MTA: Moth_1777
            MVA: Mvan_0595 Mvan_5236
            MGI: Mflv_1520
            MMC: Mmcs_4661 Mmcs_5436
            MKM: Mkms_4749 Mkms_5833
            MJL: Mjls_4066 Mjls_4208 Mjls_4209 Mjls_5044
            RHA: RHA1_ro03880
            ART: Arth_3524
            NCA: Noca_1651 Noca_2055 Noca_2151
            STP: Strop_3524 Strop_3527
            RRS: RoseRS_2578
            RCA: Rcas_2405
            DGE: Dgeo_2420
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.77
            ExPASy - ENZYME nomenclature database: 4.1.1.77
            ExplorEnz - The Enzyme Database: 4.1.1.77
            ERGO genome analysis and discovery system: 4.1.1.77
            BRENDA, the Enzyme Database: 4.1.1.77
            CAS: 37325-55-6
///
ENTRY       EC 4.1.1.78                 Enzyme
NAME        acetylenedicarboxylate decarboxylase;
            acetylenedicarboxylate hydratase;
            acetylenedicarboxylate hydrase;
            acetylenedicarboxylate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     acetylenedicarboxylate carboxy-lyase (pyruvate-forming)
REACTION    acetylenedicarboxylate + H2O = pyruvate + CO2 [RN:R00218]
ALL_REAC    R00218;
            (other) R04177
SUBSTRATE   acetylenedicarboxylate [CPD:C03248];
            H2O [CPD:C00001]
PRODUCT     pyruvate [CPD:C00022];
            CO2 [CPD:C00011]
COMMENT     The mechanism appears to involve hydration of the acetylene and
            decarboxylation of the oxaloacetic acid formed, although free
            oxaloacetate is not an intermediate. It is thus analogous to EC
            4.2.1.27 (acetylenecarboxylate hydratase) in its mechanism.
REFERENCE   1
  AUTHORS   Yamada, E.W. and Jakoby, W.B.
  TITLE     Enzymatic utilization of acetylenic compounds. I. An enzyme
            converting acetylenedicarboxylic acid to pyruvate.
  JOURNAL   J. Biol. Chem. 233 (1958) 706-711.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00620  Pyruvate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.78
            ExPASy - ENZYME nomenclature database: 4.1.1.78
            ExplorEnz - The Enzyme Database: 4.1.1.78
            ERGO genome analysis and discovery system: 4.1.1.78
            BRENDA, the Enzyme Database: 4.1.1.78
            CAS: 72561-10-5
///
ENTRY       EC 4.1.1.79                 Enzyme
NAME        sulfopyruvate decarboxylase;
            sulfopyruvate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     3-sulfopyruvate carboxy-lyase (2-sulfoacetaldehyde-forming)
REACTION    3-sulfopyruvate = 2-sulfoacetaldehyde + CO2 [RN:R05774]
ALL_REAC    R05774
SUBSTRATE   3-sulfopyruvate [CPD:C05528]
PRODUCT     2-sulfoacetaldehyde [CPD:C00593];
            CO2 [CPD:C00011]
COMMENT     Requires thiamine diphosphate. Does not decarboxylate pyruvate or
            phosphonopyruvate. The enzyme appears to be oxygen-sensitive.
REFERENCE   1  [PMID:10940029]
  AUTHORS   Graupner M, Xu H, White RH.
  TITLE     Identification of the gene encoding sulfopyruvate decarboxylase, an
            enzyme involved in biosynthesis of coenzyme M.
  JOURNAL   J. Bacteriol. 182 (2000) 4862-7.
  ORGANISM  Methanococcus jannaschii [GN:mja]
ORTHOLOGY   KO: K06034  
GENES       BUR: Bcep18194_B1915
            BRA: BRADO1443 BRADO1444 BRADO4924 BRADO4925
            BBT: BBta_3127 BBta_3128 BBta_6661 BBta_6662
            RDE: RD1_3812 RD1_3813(bcpC)
            RHA: RHA1_ro03356
            SEN: SACE_4585
            MJA: MJ0255a(comD) MJ0256
            MMP: MMP0411(comD) MMP1689(comE)
            MMQ: MmarC5_1227
            MBU: Mbur_1458 Mbur_1459
            MTP: Mthe_1623
            MTH: MTH1206
            MST: Msp_0277(comE) Msp_0278(comD)
            MKA: MK0395
            RCI: LRC441(comD)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.79
            ExPASy - ENZYME nomenclature database: 4.1.1.79
            ExplorEnz - The Enzyme Database: 4.1.1.79
            ERGO genome analysis and discovery system: 4.1.1.79
            BRENDA, the Enzyme Database: 4.1.1.79
///
ENTRY       EC 4.1.1.80                 Enzyme
NAME        4-hydroxyphenylpyruvate decarboxylase;
            4-hydroxyphenylpyruvate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     4-hydroxyphenylpyruvate carboxy-lyase
            (4-hydroxyphenylacetaldehyde-forming)
REACTION    4-hydroxyphenylpyruvate = 4-hydroxyphenylacetaldehyde + CO2
            [RN:R03341]
ALL_REAC    R03341
SUBSTRATE   4-hydroxyphenylpyruvate [CPD:C01179]
PRODUCT     4-hydroxyphenylacetaldehyde [CPD:C03765];
            CO2 [CPD:C00011]
COMMENT     Reacts with dopamine to give the benzylisoquinoline alkaloid
            skeleton.
REFERENCE   1
  AUTHORS   Rueffer, M. and Zenk, M.H.
  TITLE     Distant precursors of benzylisoquinoline alkaloids and their
            enzymatic formation.
  JOURNAL   Z. Naturforsch. C: Biosci. 42 (1987) 319-332.
  ORGANISM  Berberis aristata, Berberis julianae, Berberis stolonifera, Berberis
            regeliana, Tinospora caffra, Tinospora cordifolia, Eschscholzia
            californica, Thalictrum dipterocarpum, Thalictrum minus
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.80
            ExPASy - ENZYME nomenclature database: 4.1.1.80
            ExplorEnz - The Enzyme Database: 4.1.1.80
            ERGO genome analysis and discovery system: 4.1.1.80
            BRENDA, the Enzyme Database: 4.1.1.80
            CAS: 109300-96-1
///
ENTRY       EC 4.1.1.81                 Enzyme
NAME        threonine-phosphate decarboxylase;
            L-threonine-O-3-phosphate decarboxylase;
            CobD;
            L-threonine-O-3-phosphate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     L-threonine-O-3-phosphate carboxy-lyase
            [(R)-1-aminopropan-2-yl-phosphate-forming]
REACTION    L-threonine O-3-phosphate = (R)-1-aminopropan-2-yl phosphate + CO2
            [RN:R06530]
ALL_REAC    R06530
SUBSTRATE   L-threonine O-3-phosphate [CPD:C12147]
PRODUCT     (R)-1-aminopropan-2-yl phosphate [CPD:C04122];
            CO2 [CPD:C00011]
COMMENT     A pyridoxal-phosphate protein. This enzyme is unable to
            decarboxylate the D-isomer of threonine O-3-phosphate. The product
            of this reaction, (R)-1-aminopropan-2-yl phosphate, is the substrate
            of EC 6.3.1.10, adenosylcobinamide-phosphate synthase, which
            converts adenosylcobyric acid into adenosylcobinamide phosphate in
            the anaerobic cobalamin biosynthesis pathway.
REFERENCE   1  [PMID:11939774]
  AUTHORS   Cheong CG, Bauer CB, Brushaber KR, Escalante-Semerena JC, Rayment I.
  TITLE     Three-dimensional structure of the L-threonine-O-3-phosphate
            decarboxylase (CobD) enzyme from Salmonella enterica.
  JOURNAL   Biochemistry. 41 (2002) 4798-808.
  ORGANISM  Salmonella enterica
REFERENCE   2  [PMID:7559521]
  AUTHORS   O'Toole GA, Escalante-Semerena JC.
  TITLE     Purification and characterization of the bifunctional CobU enzyme of
            Salmonella typhimurium LT2. Evidence for a CobU-GMP intermediate.
  JOURNAL   J. Biol. Chem. 270 (1995) 23560-9.
  ORGANISM  Salmonella typhimurium
REFERENCE   3  [PMID:12195810]
  AUTHORS   Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
  TITLE     The biosynthesis of adenosylcobalamin (vitamin B12).
  JOURNAL   Nat. Prod. Rep. 19 (2002) 390-412.
  ORGANISM  Salmonella enterica, Pseudomonas denitrificans
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K04720  threonine-phosphate decarboxylase
GENES       STY: STY0695(cobD)
            STT: t2223(cobD)
            SPT: SPA2090(cobD)
            SEC: SC0674(cobD)
            STM: STM0644(cobD)
            PLU: plu2967(cobD)
            PAP: PSPA7_4114
            PEN: PSEEN1382
            BUR: Bcep18194_A5780
            BPL: BURPS1106A_1042(cobD)
            BPD: BURPS668_1036(cobD)
            HAR: HEAR0968
            GSU: GSU2989
            GME: Gmet_0487
            DDE: Dde_1401
            SFU: Sfum_1737
            BOV: BOV_1258(cobD-2)
            BRA: BRADO4915
            BBT: BBta_3136
            RDE: RD1_1331(cobC)
            GBE: GbCGDNIH1_0652
            RRU: Rru_A2651
            MGM: Mmc1_3126
            BHA: BH1589(cobC)
            GKA: GK2262
            LMO: lmo1169(cobD)
            LIN: lin1133(cobD)
            SSA: SSA_0510
            STH: STH1925
            CNO: NT01CX_2083
            CDF: CD3432(cobD)
            CKL: CKL_0714(cobD1)
            MTA: Moth_1104
            SYN: sll1713(hisC)
            SYC: syc0440_c(hisC)
            SYF: Synpcc7942_1109
            SYE: Syncc9902_2148
            SYG: sync_2715(cobD-2)
            CYA: CYA_0941(cobD-2)
            CYB: CYB_0897(cobD-1)
            TEL: tll2266
            GVI: gll3423(hisC)
            ANA: alr3936(hisC)
            AVA: Ava_1766
            PMB: A9601_02161
            PMC: P9515_02271
            PMF: P9303_27901
            PMG: P9301_02181
            PME: NATL1_02741
            CCH: Cag_1011
            HWA: HQ1407A(cobD)
            RCI: RCIX2655(cobD)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.81
            ExPASy - ENZYME nomenclature database: 4.1.1.81
            ExplorEnz - The Enzyme Database: 4.1.1.81
            ERGO genome analysis and discovery system: 4.1.1.81
            BRENDA, the Enzyme Database: 4.1.1.81
///
ENTRY       EC 4.1.1.82                 Enzyme
NAME        phosphonopyruvate decarboxylase;
            3-phosphonopyruvate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     3-phosphonopyruvate carboxy-lyase (2-phosphonoacetaldehyde-forming)
REACTION    3-phosphonopyruvate = 2-phosphonoacetaldehyde + CO2 [RN:R04053]
ALL_REAC    R04053
SUBSTRATE   3-phosphonopyruvate [CPD:C02798]
PRODUCT     2-phosphonoacetaldehyde [CPD:C03167];
            CO2 [CPD:C00011]
COMMENT     The enzyme catalyses a step in the biosynthetic pathway of
            2-aminoethylphosphonate, a component of the capsular polysaccharide
            complex of Bacteroides fragilis. Requires thiamine diphosphate and
            Mg2+ as cofactors. The enzyme is activated by the divalent cations
            Mg2+, Ca2+ and Mn2+. Pyruvate and sulfopyruvate can also act as
            substrates, but more slowly. This enzyme drives the reaction
            catalysed by EC 5.4.2.9, phosphoenolpyruvate mutase, in the
            thermodynamically unfavourable direction of 3-phosphonopyruvate
            formation [2]. It is the initial step in all of the major
            biosynthetic pathways of phosphonate natural products [3].
REFERENCE   1  [PMID:12904299]
  AUTHORS   Zhang G, Dai J, Lu Z, Dunaway-Mariano D.
  TITLE     The phosphonopyruvate decarboxylase from Bacteroides fragilis.
  JOURNAL   J. Biol. Chem. 278 (2003) 41302-8.
  ORGANISM  Bacteroides fragilis
REFERENCE   2  [PMID:8180189]
  AUTHORS   Seidel HM, Knowles JR.
  TITLE     Interaction of inhibitors with phosphoenolpyruvate mutase:
            implications for the reaction mechanism and the nature of the active
            site.
  JOURNAL   Biochemistry. 33 (1994) 5641-6.
REFERENCE   3  [PMID:9127192]
  AUTHORS   Nakashita H, Watanabe K, Hara O, Hidaka T, Seto H.
  TITLE     Studies on the biosynthesis of bialaphos. Biochemical mechanism of
            C-P bond formation: discovery of phosphonopyruvate decarboxylase
            which catalyzes the formation of phosphonoacetaldehyde from
            phosphonopyruvate.
  JOURNAL   J. Antibiot. (Tokyo). 50 (1997) 212-9.
PATHWAY     PATH: map00440  Aminophosphonate metabolism
ORTHOLOGY   KO: K09459  phosphonopyruvate decarboxylase
GENES       BPL: BURPS1106A_A0817(ppd)
            BPD: BURPS668_A0909(ppd)
            BTH: BT_1719
            BFR: BF1833
            BFS: BF1898(aepY)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.82
            ExPASy - ENZYME nomenclature database: 4.1.1.82
            ExplorEnz - The Enzyme Database: 4.1.1.82
            ERGO genome analysis and discovery system: 4.1.1.82
            BRENDA, the Enzyme Database: 4.1.1.82
///
ENTRY       EC 4.1.1.83                 Enzyme
NAME        4-hydroxyphenylacetate decarboxylase;
            p-hydroxyphenylacetate decarboxylase;
            p-Hpd;
            4-Hpd;
            4-hydroxyphenylacetate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     4-(hydroxyphenyl)acetate carboxy-lyase (4-methylphenol-forming)
REACTION    (4-hydroxyphenyl)acetate + H+ = 4-methylphenol + CO2 [RN:R07312]
ALL_REAC    R07312
SUBSTRATE   4-hydroxyphenylacetate [CPD:C00642];
            H+ [CPD:C00080]
PRODUCT     4-methylphenol [CPD:C01468];
            CO2 [CPD:C00011]
COMMENT     The enzyme, from the strict anaerobe Clostridium difficile, can also
            use (3,4-dihydroxyphenyl)acetate as a substrate, yielding
            4-methylcatechol as a product. The enzyme is a glycyl radical
            enzyme.
REFERENCE   1  [PMID:3938267]
  AUTHORS   D'Ari L, Barker HA.
  TITLE     p-Cresol formation by cell-free extracts of Clostridium difficile.
  JOURNAL   Arch. Microbiol. 143 (1985) 311-2.
  ORGANISM  Clostridium difficile [GN:cdf]
REFERENCE   2  [PMID:11231288]
  AUTHORS   Selmer T, Andrei PI.
  TITLE     p-Hydroxyphenylacetate decarboxylase from Clostridium difficile. A
            novel glycyl radical enzyme catalysing the formation of p-cresol.
  JOURNAL   Eur. J. Biochem. 268 (2001) 1363-72.
  ORGANISM  Clostridium difficile [GN:cdf]
REFERENCE   3  [PMID:15153112]
  AUTHORS   Andrei PI, Pierik AJ, Zauner S, Andrei-Selmer LC, Selmer T.
  TITLE     Subunit composition of the glycyl radical enzyme
            p-hydroxyphenylacetate decarboxylase. A small subunit, HpdC, is
            essential for catalytic activity.
  JOURNAL   Eur. J. Biochem. 271 (2004) 2225-30.
  ORGANISM  Clostridium difficile [GN:cdf]
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.83
            ExPASy - ENZYME nomenclature database: 4.1.1.83
            ExplorEnz - The Enzyme Database: 4.1.1.83
            ERGO genome analysis and discovery system: 4.1.1.83
            BRENDA, the Enzyme Database: 4.1.1.83
///
ENTRY       EC 4.1.1.84                 Enzyme
NAME        D-dopachrome decarboxylase;
            phenylpyruvate tautomerase II;
            D-tautomerase;
            D-dopachrome tautomerase;
            D-dopachrome carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     D-dopachrome carboxy-lyase (5,6-dihydroxyindole-forming)
REACTION    D-dopachrome = 5,6-dihydroxyindole + CO2 [RN:R07313]
ALL_REAC    R07313
SUBSTRATE   D-dopachrome [CPD:C15566]
PRODUCT     5,6-dihydroxyindole [CPD:C05578];
            CO2 [CPD:C00011]
COMMENT     This enzyme is specific for D-dopachrome as substrate and belongs to
            the MIF (macrophage migration inhibitory factor) family of proteins.
            L-Dopachrome, L- or D-alpha-methyldopachrome and dopaminochrome do
            not act as substrates (see also EC 5.3.3.12, L-dopachrome isomerase)
REFERENCE   1  [PMID:8267597]
  AUTHORS   Odh G, Hindemith A, Rosengren AM, Rosengren E, Rorsman H.
  TITLE     Isolation of a new tautomerase monitored by the conversion of
            D-dopachrome to 5,6-dihydroxyindole.
  JOURNAL   Biochem. Biophys. Res. Commun. 197 (1993) 619-24.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:9285056]
  AUTHORS   Yoshida H, Nishihira J, Suzuki M, Hikichi K.
  TITLE     NMR characterization of physicochemical properties of rat
            D-dopachrome tautomerase.
  JOURNAL   Biochem. Mol. Biol. Int. 42 (1997) 891-9.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:10079069]
  AUTHORS   Sugimoto H, Taniguchi M, Nakagawa A, Tanaka I, Suzuki M, Nishihira
            J.
  TITLE     Crystal structure of human D-dopachrome tautomerase, a homologue of
            macrophage migration inhibitory factor, at 1.54 A resolution.
  JOURNAL   Biochemistry. 38 (1999) 3268-79.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:9480844]
  AUTHORS   Nishihira J, Fujinaga M, Kuriyama T, Suzuki M, Sugimoto H, Nakagawa
            A, Tanaka I, Sakai M.
  TITLE     Molecular cloning of human D-dopachrome tautomerase cDNA: N-terminal
            proline is essential for enzyme activation.
  JOURNAL   Biochem. Biophys. Res. Commun. 243 (1998) 538-44.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K10028  D-dopachrome decarboxylase
GENES       HSA: 1652(DDT)
            MCC: 699933(DDT)
            MMU: 13202(Ddt)
            RNO: 29318(Ddt)
            GGA: 416937(RCJMB04_2c16)
            XLA: 447275(MGC86410)
            XTR: 550015(ddt)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.84
            ExPASy - ENZYME nomenclature database: 4.1.1.84
            ExplorEnz - The Enzyme Database: 4.1.1.84
            ERGO genome analysis and discovery system: 4.1.1.84
            BRENDA, the Enzyme Database: 4.1.1.84
            CAS: 184111-06-6
///
ENTRY       EC 4.1.1.85                 Enzyme
NAME        3-dehydro-L-gulonate-6-phosphate decarboxylase;
            3-keto-L-gulonate 6-phosphate decarboxylase;
            UlaD;
            SgaH;
            SgbH;
            KGPDC;
            3-dehydro-L-gulonate-6-phosphate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     3-dehydro-L-gulonate-6-phosphate carboxy-lyase
            (L-xylulose-5-phosphate-forming)
REACTION    3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2
            [RN:R07125]
ALL_REAC    R07125
SUBSTRATE   3-dehydro-L-gulonate 6-phosphate [CPD:C14899];
            H+ [CPD:C00080]
PRODUCT     L-xylulose 5-phosphate [CPD:C03291];
            CO2 [CPD:C00011]
COMMENT     Requires Mg2+. Along with EC 5.1.3.22, L-ribulose-5-phosphate
            3-epimerase, this enzyme is involved in a pathway for the
            utilization of L-ascorbate by Escherichia coli.
REFERENCE   1  [PMID:11741871]
  AUTHORS   Yew WS, Gerlt JA.
  TITLE     Utilization of L-ascorbate by Escherichia coli K-12: assignments of
            functions to products of the yjf-sga and yia-sgb operons.
  JOURNAL   J. Bacteriol. 184 (2002) 302-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:11900527]
  AUTHORS   Wise E, Yew WS, Babbitt PC, Gerlt JA, Rayment I.
  TITLE     Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated
            reactions: orotidine 5'-monophosphate decarboxylase and
            3-keto-L-gulonate 6-phosphate decarboxylase.
  JOURNAL   Biochemistry. 41 (2002) 3861-9.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K03078  3-dehydro-L-gulonate-6-phosphate decarboxylase
            KO: K03081  3-dehydro-L-gulonate-6-phosphate decarboxylase
GENES       ECO: b3581(sgbH) b4196(sgaH)
            ECJ: JW3553(sgbH) JW4154(ulaD)
            ECE: Z5805(sgaH)
            ECS: ECs5172
            ECC: c4404(sgbH) c5285(sgaH)
            ECI: UTI89_C4125(sgbH) UTI89_C4796(sgaH)
            ECP: ECP_3686 ECP_4441
            ECV: APECO1_2196(sgaH) APECO1_2869(sgbH)
            ECW: EcE24377A_4078(sgbH)
            ECX: EcHS_A3785(sgbH)
            STY: STY4121(yiaQ) STY4742(sgaH)
            STT: t3844(yiaQ) t4437(sgaH)
            SPT: SPA3526(yiaQ) SPA4203(sgaH)
            SEC: SC3601(sgbH) SC4260(sgaH)
            STM: STM3675(sgbH) STM4386(sgaH)
            SFL: SF4351(sgaH)
            SFX: S4621(sgaH)
            SFV: SFV_3958(sgbH) SFV_4352(sgaH)
            SSN: SSON_4378(sgaH)
            SBO: SBO_4259(sgaH)
            SDY: SDY_4365(sgaH)
            SPE: Spro_3937
            HIN: HI1024(sgbh)
            HDU: HD1857(sgaH)
            HSO: HS_0771(sgbH)
            PMU: PM0766 PM1246
            MSU: MS0020(sgbH) MS0056(sgbH)
            APL: APL_1698(ulaD)
            ASU: Asuc_0240
            VCH: VCA0242
            VVU: VV2_1084
            VVY: VVA1608
            PPR: PBPRB0276(sgbH)
            MCA: MCA3043 MCA3049
            BCL: ABC3351(hxlA)
            SSP: SSP1619 SSP1626
            SPY: SPy_0177
            SPZ: M5005_Spy_0151
            SPM: spyM18_0176
            SPG: SpyM3_0138
            SPS: SPs0141
            SPH: MGAS10270_Spy0153
            SPA: M6_Spy0197
            SPB: M28_Spy0149
            SPN: SP_2035
            SPR: spr1846(sgh)
            SAG: SAG1812
            SAN: gbs1853
            SAK: SAK_1832
            SMU: SMU.273
            LCA: LSEI_2735
            EFA: EF1129
            CAC: CAC0396
            MPN: MPN493(yjfV)
            MPU: MYPU_5970(sgaH)
            MPE: MYPE7180(sgaH)
            MHY: mhp441(sgaH)
            MHJ: MHJ_0436(sgaH)
            MHP: MHP7448_0438(sgaH)
            MSY: MS53_0029(sgaH)
            TWH: TWT649
            TWS: TW671(sgaH)
            PAC: PPA0880
            SAI: Saci_0802
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.85
            ExPASy - ENZYME nomenclature database: 4.1.1.85
            ExplorEnz - The Enzyme Database: 4.1.1.85
            ERGO genome analysis and discovery system: 4.1.1.85
            BRENDA, the Enzyme Database: 4.1.1.85
///
ENTRY       EC 4.1.1.86                 Enzyme
NAME        diaminobutyrate decarboxylase;
            DABA DC;
            L-2,4-diaminobutyrate decarboxylase;
            L-2,4-diaminobutanoate carboxy-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
SYSNAME     L-2,4-diaminobutanoate carboxy-lyase (propane-1,3-diamine-forming)
REACTION    L-2,4-diaminobutanoate = propane-1,3-diamine + CO2 [RN:R07650]
ALL_REAC    R07650
SUBSTRATE   L-2,4-diaminobutanoate [CPD:C03283]
PRODUCT     propane-1,3-diamine [CPD:C00986];
            CO2 [CPD:C00011]
COMMENT     A pyridoxal-phosphate protein that requires a divalent cation for
            activity [1]. N4-Acetyl-L-2,4-diaminobutanoate,
            2,3-diaminopropanoate, ornithine and lysine are not substrates.
            Found in the proteobacteria Haemophilus influenzae and Acinetobacter
            baumannii. In the latter, this enzyme is cotranscribed with the dat
            gene that encodes EC 2.6.1.76, diaminobutyrate---2-oxoglutarate
            transaminase, which can supply the substrate for this enzyme.
REFERENCE   1  [PMID:1512577]
  AUTHORS   Yamamoto S, Tsuzaki Y, Tougou K, Shinoda S.
  TITLE     Purification and characterization of L-2,4-diaminobutyrate
            decarboxylase from Acinetobacter calcoaceticus.
  JOURNAL   J. Gen. Microbiol. 138 (1992) 1461-5.
  ORGANISM  Acinetobacter calcoaceticus
REFERENCE   2  [PMID:7813892]
  AUTHORS   Ikai H, Yamamoto S.
  TITLE     Cloning and expression in Escherichia coli of the gene encoding a
            novel L-2,4-diaminobutyrate decarboxylase of Acinetobacter
            baumannii.
  JOURNAL   FEMS. Microbiol. Lett. 124 (1994) 225-8.
  ORGANISM  Acinetobacter baumannii [GN:acb]
REFERENCE   3  [PMID:9260954]
  AUTHORS   Ikai H, Yamamoto S.
  TITLE     Identification and analysis of a gene encoding
            L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase involved in
            the 1,3-diaminopropane production pathway in Acinetobacter
            baumannii.
  JOURNAL   J. Bacteriol. 179 (1997) 5118-25.
  ORGANISM  Acinetobacter baumannii [GN:acb]
GENES       BPU: BPUM_0725 BPUM_1020
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.1.86
            ExPASy - ENZYME nomenclature database: 4.1.1.86
            ExplorEnz - The Enzyme Database: 4.1.1.86
            ERGO genome analysis and discovery system: 4.1.1.86
            BRENDA, the Enzyme Database: 4.1.1.86
///
ENTRY       EC 4.1.1.-                  Enzyme
CLASS       Lyases;
            Carbon-carbon lyases;
            Carboxy-lyases
REACTION    (1) Pyruvate + CO2 <=> 2-Hydroxyethylenedicarboxylate [RN:R00219];
            (2) Homogentisate + Oxygen + NADPH <=> Gentisate aldehyde + CO2 +
            NADP+ + H+ + H2O [RN:R02518];
            (3) 4-Coumarate <=> 4-Hydroxystyrene + CO2 [RN:R02952];
            (4) 3-(4-Hydroxyphenyl)pyruvate <=> 4-Hydroxyphenylacetaldehyde +
            CO2 [RN:R03341];
            (5) 3,4-Dihydroxy-trans-cinnamate <=> 3,4-Dihydroxystyrene + CO2
            [RN:R03367];
            (6) L-Dopachrome <=> 5,6-Dihydroxyindole + CO2 [RN:R03674];
            (7) 4-Guanidinobutanal + CO2 <=> 2-Oxoarginine [RN:R04008];
            (8) 3-Hydroxy-L-kynurenine <=> 3-Hydroxykynurenamine + CO2
            [RN:R04172];
            (9) (Z)-5-Oxohex-2-enedioate + H2O <=> 4-Hydroxy-2-oxopentanoate +
            CO2 [RN:R04223];
            (10) (4R,5S)-4,5,6-Trihydroxy-2,3-dioxohexanoate + H2O <=>
            L-Xylonate + CO2 [RN:R04515];
            (11) 3-Hexaprenyl-4,5-dihydroxybenzoate <=> 2-Hexaprenylphenol + CO2
            [RN:R04712];
            (12) 5-Aminoimidazole + CO2 <=> 5-Amino-4-imidazole carboxylate
            [RN:R04732];
            (13) (4R,5S)-4,5,6-Trihydroxy-2,3-dioxohexanoate + H2O <=>
            L-Lyxonate + CO2 [RN:R04784];
            (14) 5,6-Dihydroxyindole + CO2 <=>
            2-Carboxy-2,3-dihydro-5,6-dihydroxyindole [RN:R04885];
            (15) 3-Octaprenyl-4-hydroxybenzoate <=> 2-Octaprenylphenol + CO2
            [RN:R04986];
            (16) 4-Hydroxy-L-threonine <=> 3-Aminopropane-1,2-diol + CO2
            [RN:R05087];
            (17) Bis(4'-chlorophenyl)methane + CO2 <=>
            Bis(4'-chlorophenyl)acetate [RN:R05376];
            (18) 2-Hydroxy-3-carboxy-6-oxo-7-methylocta-2,4-dienoate <=>
            2-Hydroxy-6-oxo-7-methylocta-2,4-dienoate + CO2 [RN:R05377];
            (19) 2-Hydroxyisophthalic acid <=> Salicylate + CO2 [RN:R06925];
            (20) 3-Oxopropanoate <=> Acetaldehyde + CO2 [RN:R06973]
SUBSTRATE   Pyruvate [CPD:C00022];
            CO2 [CPD:C00011];
            Homogentisate [CPD:C00544];
            Oxygen [CPD:C00007];
            NADPH [CPD:C00005];
            4-Coumarate [CPD:C00811];
            3-(4-Hydroxyphenyl)pyruvate [CPD:C01179];
            3,4-Dihydroxy-trans-cinnamate [CPD:C01197];
            L-Dopachrome [CPD:C01693];
            4-Guanidinobutanal [CPD:C02647];
            3-Hydroxy-L-kynurenine [CPD:C03227];
            (Z)-5-Oxohex-2-enedioate [CPD:C03453];
            H2O [CPD:C00001];
            (4R,5S)-4,5,6-Trihydroxy-2,3-dioxohexanoate [CPD:C04575];
            3-Hexaprenyl-4,5-dihydroxybenzoate [CPD:C05200];
            5-Aminoimidazole [CPD:C05239];
            5,6-Dihydroxyindole [CPD:C05578];
            3-Octaprenyl-4-hydroxybenzoate [CPD:C05809];
            4-Hydroxy-L-threonine [CPD:C06056];
            Bis(4'-chlorophenyl)methane [CPD:C06641];
            2-Hydroxy-3-carboxy-6-oxo-7-methylocta-2,4-dienoate [CPD:C06581];
            2-Hydroxyisophthalic acid [CPD:C14097];
            3-Oxopropanoate [CPD:C00222]
PRODUCT     2-Hydroxyethylenedicarboxylate [CPD:C03981];
            Gentisate aldehyde [CPD:C05585];
            CO2 [CPD:C00011];
            NADP+ [CPD:C00006];
            H+ [CPD:C00080];
            H2O [CPD:C00001];
            4-Hydroxystyrene [CPD:C05627];
            4-Hydroxyphenylacetaldehyde [CPD:C03765];
            3,4-Dihydroxystyrene [CPD:C06224];
            5,6-Dihydroxyindole [CPD:C05578];
            2-Oxoarginine [CPD:C05935];
            3-Hydroxykynurenamine [CPD:C05636];
            4-Hydroxy-2-oxopentanoate [CPD:C03589];
            L-Xylonate [CPD:C05411];
            2-Hexaprenylphenol [CPD:C05800];
            5-Amino-4-imidazole carboxylate [CPD:C05516];
            L-Lyxonate [CPD:C05412];
            2-Carboxy-2,3-dihydro-5,6-dihydroxyindole [CPD:C05604];
            2-Octaprenylphenol [CPD:C05810];
            3-Aminopropane-1,2-diol [CPD:C06057];
            Bis(4'-chlorophenyl)acetate [CPD:C06640];
            2-Hydroxy-6-oxo-7-methylocta-2,4-dienoate [CPD:C06582];
            Salicylate [CPD:C00805];
            Acetaldehyde [CPD:C00084]
///
ENTRY       EC 4.1.2.1        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
COMMENT     Deleted entry: hydroxyoxobutyrate aldolase. Now included with EC
            4.1.3.16 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.2.1 created 1961,
            deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.1
            ExPASy - ENZYME nomenclature database: 4.1.2.1
            ExplorEnz - The Enzyme Database: 4.1.2.1
            ERGO genome analysis and discovery system: 4.1.2.1
            BRENDA, the Enzyme Database: 4.1.2.1
///
ENTRY       EC 4.1.2.2                  Enzyme
NAME        ketotetrose-phosphate aldolase;
            phosphoketotetrose aldolase;
            erythrulose-1-phosphate synthetase;
            erythrose-1-phosphate synthase;
            erythrulose-1-phosphate formaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     erythrulose-1-phosphate formaldehyde-lyase
            (glycerone-phosphate-forming)
REACTION    erythrulose 1-phosphate = glycerone phosphate + formaldehyde
            [RN:R01014]
ALL_REAC    R01014
SUBSTRATE   erythrulose 1-phosphate [CPD:C03394]
PRODUCT     glycerone phosphate [CPD:C00111];
            formaldehyde [CPD:C00067]
REFERENCE   1  [PMID:13044785]
  AUTHORS   CHARALAMPOUS FC, MUELLER GC.
  TITLE     Synthesis of erythrulose phosphate by a soluble enzyme from rat
            liver.
  JOURNAL   J. Biol. Chem. 201 (1953) 161-73.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.2
            ExPASy - ENZYME nomenclature database: 4.1.2.2
            ExplorEnz - The Enzyme Database: 4.1.2.2
            ERGO genome analysis and discovery system: 4.1.2.2
            BRENDA, the Enzyme Database: 4.1.2.2
            CAS: 9024-45-7
///
ENTRY       EC 4.1.2.3        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
COMMENT     Deleted entry: pentosealdolase (EC 4.1.2.3 created 1961, deleted
            1972)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.3
            ExPASy - ENZYME nomenclature database: 4.1.2.3
            ExplorEnz - The Enzyme Database: 4.1.2.3
            ERGO genome analysis and discovery system: 4.1.2.3
            BRENDA, the Enzyme Database: 4.1.2.3
///
ENTRY       EC 4.1.2.4                  Enzyme
NAME        deoxyribose-phosphate aldolase;
            phosphodeoxyriboaldolase;
            deoxyriboaldolase;
            deoxyribose-5-phosphate aldolase;
            2-deoxyribose-5-phosphate aldolase;
            2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase
            (D-glyceraldehyde-3-phosphate-forming)
REACTION    2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate +
            acetaldehyde [RN:R01066]
ALL_REAC    R01066
SUBSTRATE   2-deoxy-D-ribose 5-phosphate [CPD:C00673]
PRODUCT     D-glyceraldehyde 3-phosphate [CPD:C00118];
            acetaldehyde [CPD:C00084]
REFERENCE   1  [PMID:4879701]
  AUTHORS   Hoffee PA.
  TITLE     2-deoxyribose-5-phosphate aldolase of Salmonella typhimurium:
            purification and properties.
  JOURNAL   Arch. Biochem. Biophys. 126 (1968) 795-802.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:4989681]
  AUTHORS   Jedziniak JA, Lionetti FJ.
  TITLE     Purification and properties of deoxyriboaldolase from human
            erythrocytes.
  JOURNAL   Biochim. Biophys. Acta. 212 (1970) 478-87.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:12980976]
  AUTHORS   RACKER E.
  TITLE     Enzymatic synthesis and breakdown of desoxyribose phosphate.
  JOURNAL   J. Biol. Chem. 196 (1952) 347-65.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4
  AUTHORS   Hoffee, P. Rosen, O.M. and Horecker, B.L.
  TITLE     The mechanism of action of aldolases. VI. Crystallization of
            deoxyribose 5-phosphate aldolase and the number of active sites.
  JOURNAL   J. Biol. Chem. 240 (1965) 1512-1516.
  ORGANISM  Escherichia coli [GN:eco], Corynebacterium diphtheriae [GN:cdi],
            Lactobacillus plantarum [GN:lpl]
PATHWAY     PATH: map00030  Pentose phosphate pathway
ORTHOLOGY   KO: K01619  deoxyribose-phosphate aldolase
GENES       HSA: 51071(DERA)
            PTR: 465316(DERA)
            MMU: 232449(Dera)
            CFA: 477684(DERA)
            GGA: 418176(DERA)
            XLA: 496174(LOC496174)
            XTR: 448233(MGC88940)
            SPU: 591843(LOC591843)
            DME: Dmel_CG8525
            CEL: F09E5.3
            AFM: AFUA_3G06590 AFUA_7G06490
            AOR: AO090138000062
            PFA: PF10_0210
            TET: TTHERM_00191620
            TBR: Tb927.7.5680
            TCR: 507559.80 510303.50
            LMA: LmjF06.1070
            EHI: 147.t00009
            ECO: b4381(deoC)
            ECJ: JW4344(deoC)
            ECE: Z5983(deoC)
            ECS: ECs5340
            ECC: c5465(deoC)
            ECI: UTI89_C5152(deoC)
            ECP: ECP_4765
            ECV: APECO1_2000(deoC)
            ECW: EcE24377A_4980(deoC)
            ECX: EcHS_A4616
            STY: STY4918(deoC)
            STT: t4610(deoC)
            SPT: SPA4381(deoC)
            STM: STM4567(deoC)
            YPE: YPO0436(deoC) YPO1323(deoC) YPO3622
            YPK: y0247 y2860(deoC) y3743(deoC)
            YPM: YP_1269(deoC1) YP_3745(deoC2) YP_3925(deoC3)
            YPA: YPA_0614 YPA_3635 YPA_3848
            YPN: YPN_0307 YPN_2656 YPN_3548
            YPP: YPDSF_0229 YPDSF_2373 YPDSF_3197
            YPS: YPTB0581(deoC) YPTB1354(deoC) YPTB3607
            YPI: YpsIP31758_2652(deoC2) YpsIP31758_3498(deoC1)
            SFL: SF4413(deoC)
            SFX: S4684(deoC)
            SFV: SFV_4415(deoC)
            SSN: SSON_4532(deoC)
            SBO: SBO_4443(deoC)
            SDY: SDY_4641(deoC)
            ECA: ECA0727(deoC) ECA2684
            PLU: plu0520(deoC)
            SGL: SG0394
            ENT: Ent638_0541
            SPE: Spro_0660 Spro_1632
            HIT: NTHI1280(deoC)
            HIP: CGSHiEE_06475
            HIQ: CGSHiGG_09245
            HDU: HD0888(deoC)
            HSO: HS_0748(deoC)
            PMU: PM1343(deoC)
            MSU: MS0152(deoC)
            APL: APL_1015(deoC)
            ASU: Asuc_2015
            VCH: VC2350
            VCO: VC0395_A1929(deoC)
            VVU: VV1_1725
            VVY: VV0527 VV2679
            VPA: VP2436
            VFI: VF0504
            PPR: PBPRA0630
            PST: PSPTO_0973(deoC)
            PSB: Psyr_0839 Psyr_4491
            PSP: PSPPH_0865(deoC)
            SON: SO_1217(deoC)
            SDN: Sden_1025
            SFR: Sfri_1002
            SAZ: Sama_0973
            SBL: Sbal_3227
            SBM: Shew185_3230
            SLO: Shew_2815
            SPC: Sputcn32_2822
            SSE: Ssed_3378
            SPL: Spea_3048
            SHE: Shewmr4_1037
            SHM: Shewmr7_1102
            SHN: Shewana3_1041
            SHW: Sputw3181_1189
            ILO: IL1883(deoC)
            CPS: CPS_1972(deoC)
            PHA: PSHAa0214
            PIN: Ping_2862
            CBU: CBU_0017(deoC)
            CBD: COXBU7E912_0140(deoC)
            LPN: lpg1433(deoC)
            LPF: lpl1608(deoC)
            LPP: lpp1388(deoC)
            FTU: FTT0114(deoC)
            FTF: FTF0114(deoC)
            FTW: FTW_0199(deoC)
            FTL: FTL_1663
            FTH: FTH_1604(deoC)
            FTA: FTA_1760(deoC)
            FTN: FTN_1601(deoC)
            HCH: HCH_03074(deoC)
            CSA: Csal_0831
            AHA: AHA_0960(deoC-1) AHA_3690(deoC-2)
            CVI: CV_3701(deoC)
            BMA: BMAA0110(deoC)
            BMV: BMASAVP1_1271(deoC)
            BMN: BMA10247_A0130(deoC)
            BXE: Bxe_B1399 Bxe_C1275
            BUR: Bcep18194_C6902
            BCN: Bcen_1543
            BCH: Bcen2424_6286
            BPS: BPSS1962(deoC)
            BPM: BURPS1710b_A1068(deoC)
            BPL: BURPS1106A_A2666(deoC)
            BPD: BURPS668_A2811(deoC)
            BTE: BTH_II0410(deoC)
            VEI: Veis_2688
            PCA: Pcar_2321
            BBA: Bd3854(dra)
            DPS: DP1973
            ADE: Adeh_0904
            AFW: Anae109_0950
            MXA: MXAN_5719(deoC)
            MLO: mll4784
            MES: Meso_0314
            SME: SMb21300(deoC) SMc02333
            SMD: Smed_2469 Smed_4631
            ATU: Atu0132(deoC) Atu4848(deoC)
            ATC: AGR_C_211 AGR_L_76
            RET: RHE_CH00193(deoC)
            RLE: RL0202(deoC) RL2744(deoC)
            OAN: Oant_2837
            BBT: BBta_7828
            SIL: SPO3367(deoC)
            SIT: TM1040_0097
            RSP: RSP_3739
            RSH: Rsph17029_3471
            JAN: Jann_0789
            RDE: RD1_0661(deoC)
            PDE: Pden_3897
            RRU: Rru_A2303
            ABA: Acid345_3057
            SUS: Acid_0515 Acid_2205
            BSU: BG10983(dra)
            BHA: BH1352(dra)
            BAN: BA1892(dra)
            BAR: GBAA1892(dra)
            BAA: BA_2394(deoC)
            BAT: BAS1754
            BCE: BC1820
            BCA: BCE_1975(dra)
            BCZ: BCZK1703(deoC)
            BCY: Bcer98_1469
            BTK: BT9727_1732(deoC)
            BLI: BL00229(deoC) BL02102
            BLD: BLi02734 BLi04229(dra)
            BCL: ABC1666(dra)
            BAY: RBAM_036480
            BPU: BPUM_3587
            OIH: OB1963(dra) OB2751
            GKA: GK2499
            SAU: SA0133(dra) SA1939
            SAV: SAV0138(dra) SAV2137
            SAM: MW0112(dra) MW2061
            SAR: SAR0140(deoC1) SAR2225(deoC2)
            SAS: SAS0112 SAS2040
            SAC: SACOL0123(deoC1) SACOL2129(deoC2)
            SAB: SAB0077(deoC1) SAB2021c(deoC2)
            SAA: SAUSA300_0140(deoC) SAUSA300_2090(deoC)
            SAO: SAOUHSC_00100 SAOUHSC_02379
            SAJ: SaurJH9_0124 SaurJH9_2173
            SAH: SaurJH1_0129 SaurJH1_2211
            SEP: SE1736
            SER: SERP1745(deoC)
            SHA: SH0897(dra)
            SSP: SSP0747
            LMO: lmo1995(dra)
            LMF: LMOf2365_2018(deoC)
            LIN: lin2103(dra)
            LWE: lwe2015(deoC)
            LLA: L63310(deoC)
            LLC: LACR_1529
            LLM: llmg_1062(deoC)
            SPY: SPy_1867(deoC)
            SPZ: M5005_Spy_1585(deoC)
            SPM: spyM18_1931(deoC)
            SPG: SpyM3_1611(deoC)
            SPS: SPs0256
            SPH: MGAS10270_Spy1656(deoC)
            SPI: MGAS10750_Spy1643(deoC)
            SPJ: MGAS2096_Spy1610(deoC)
            SPK: MGAS9429_Spy1590(deoC)
            SPF: SpyM50265(deoC)
            SPA: M6_Spy1597
            SPB: M28_Spy1578(deoC)
            SPN: SP_0843
            SPR: spr0745(deoC)
            SPD: SPD_0737(deoC)
            SAG: SAG2070(deoC)
            SAN: gbs2024
            SAK: SAK_2009(deoC)
            SMU: SMU.1123(deoC)
            STC: str0806
            STL: stu0806
            SSA: SSA_1036(deoC)
            SGO: SGO_1080(deoC)
            LPL: lp_0497(deoC)
            LJO: LJ1661
            LAC: LBA0391
            LSA: LSA0795(deoC)
            LBR: LVIS_1595
            LCA: LSEI_0007 LSEI_0278
            LRE: Lreu_0111
            EFA: EF0174(deoC)
            OOE: OEOE_1206
            STH: STH565
            CAC: CAC1545(deoC)
            CPE: CPE2052(deoC)
            CPF: CPF_2309(deoC)
            CPR: CPR_2024(deoC)
            CTC: CTC01994
            CNO: NT01CX_1496(deoC)
            CTH: Cthe_1583 Cthe_1943
            CDF: CD1502(deoC)
            CBO: CBO1563(deoC)
            CBA: CLB_1583(deoC)
            CBH: CLC_1594(deoC)
            CBF: CLI_1645(deoC)
            CBE: Cbei_0748 Cbei_3120 Cbei_4143
            CKL: CKL_2777(deoC)
            AMT: Amet_2897
            CHY: CHY_1552(deoC)
            DSY: DSY3104
            DRM: Dred_1129
            SWO: Swol_1560
            CSC: Csac_2317
            TTE: TTE0975(deoC)
            MGE: MG_050
            MPN: MPN063(deoC)
            MPU: MYPU_3140(deoC)
            MPE: MYPE1170(deoC)
            MGA: MGA_0363(deoC) MGA_1328(deoC)
            MMY: MSC_0828(deoC)
            MMO: MMOB5370(deoC)
            MHY: mhp544(deoC)
            MHJ: MHJ_0528(deoC)
            MHP: MHP7448_0527(deoC)
            MSY: MS53_0445(deoC)
            MCP: MCAP_0755(deoC)
            UUR: UU585(deoC)
            MFL: Mfl121 Mfl639
            MTU: Rv0478(deoC)
            MTC: MT0496(deoC)
            MBO: Mb0488(deoC)
            MBB: BCG_0519(deoC)
            MLE: ML2451(deoC)
            MPA: MAP3971(deoC)
            MAV: MAV_4672(deoC)
            MSM: MSMEG_0922(deoC) MSMEG_3089(deoC)
            MVA: Mvan_0811
            MGI: Mflv_0097
            MMC: Mmcs_0646
            MKM: Mkms_0659
            MJL: Mjls_0639
            CGL: NCgl0372(cgl0383)
            CGB: cg0458(deoC)
            CEF: CE0401
            CDI: DIP0273(deoC)
            CJK: jk1923(deoC)
            NFA: nfa52030(deoC)
            RHA: RHA1_ro02094
            SCO: SCO4914(SCK13.06c)
            SMA: SAV3346(deoC)
            CMI: CMM_2919(deoC)
            ART: Arth_1248
            AAU: AAur_1359(deoC)
            PAC: PPA1214 PPA2045
            NCA: Noca_0544 Noca_3528
            FRA: Francci3_0688
            FAL: FRAAL1197(deoC)
            ACE: Acel_0572
            KRA: Krad_4162
            SEN: SACE_6564(deoC)
            STP: Strop_0828
            RXY: Rxyl_1505
            RBA: RB6729(deoC)
            TPA: TP0264
            TDE: TDE0448(deoC)
            SYN: sll1776(deoC)
            SYW: SYNW0666
            SYC: syc0561_c(deoC)
            SYF: Synpcc7942_0983
            SYD: Syncc9605_2014
            SYE: Syncc9902_0657
            SYG: sync_0605(deoC)
            SYR: SynRCC307_1799(deoC)
            SYX: SynWH7803_0577(deoC)
            CYA: CYA_1395(deoC)
            CYB: CYB_2558(deoC)
            TEL: tlr1079
            GVI: gll3538
            ANA: alr4174
            AVA: Ava_0730
            PMA: Pro0396(deoC)
            PMM: PMM0399
            PMT: PMT0212(deoC)
            PMN: PMN2A_1734
            PMI: PMT9312_0395
            PMB: A9601_04501(deoC)
            PMC: P9515_04611(deoC)
            PMF: P9303_21421(deoC)
            PMG: P9301_04191(deoC)
            PME: NATL1_04511(deoC)
            TER: Tery_4603
            BTH: BT_3263 BT_4425
            BFR: BF0095
            BFS: BF0108
            PGI: PG1996(deoC)
            SRU: SRU_1227
            GFO: GFO_1415(deoC) GFO_3000(deoC)
            FJO: Fjoh_1656
            FPS: FP2118(deoC)
            RRS: RoseRS_1083 RoseRS_3216
            RCA: Rcas_2706 Rcas_2790
            DRA: DR_1205
            DGE: Dgeo_1266
            TTH: TTC0823
            TTJ: TTHA1186
            AAE: aq_148(deoC)
            TMA: TM1559
            TPT: Tpet_1233
            TME: Tmel_0243
            FNO: Fnod_1507
            MSI: Msm_0843
            HAL: VNG1859G(deoC)
            HMA: rrnAC3429(deoC1)
            HWA: HQ3205A(deoC)
            NPH: NP3200A(deoC)
            TAC: Ta0684
            TVO: TVN0175
            TKO: TK2104
            RCI: RCIX563(deoC)
            APE: APE_2437.1
            SMR: Smar_0331
            HBU: Hbut_0962
            PAI: PAE1231
            PIS: Pisl_1295
            PCL: Pcal_0786
            PAS: Pars_0301
            TPE: Tpen_0763
STRUCTURES  PDB: 1JCJ  1JCL  1KTN  1MZH  1N7K  1O0Y  1P1X  1UB3  1VCV  2A4A  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.4
            ExPASy - ENZYME nomenclature database: 4.1.2.4
            ExplorEnz - The Enzyme Database: 4.1.2.4
            ERGO genome analysis and discovery system: 4.1.2.4
            BRENDA, the Enzyme Database: 4.1.2.4
            CAS: 9026-97-5
///
ENTRY       EC 4.1.2.5                  Enzyme
NAME        threonine aldolase;
            L-threonine acetaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     L-threonine acetaldehyde-lyase (glycine-forming)
REACTION    L-threonine = glycine + acetaldehyde [RN:R00751]
ALL_REAC    R00751;
            (other) R06171
SUBSTRATE   L-threonine [CPD:C00188]
PRODUCT     glycine [CPD:C00037];
            acetaldehyde [CPD:C00084]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1
  AUTHORS   Bell, S.C. and Turner, J.M.
  TITLE     Bacterial threonine aldolase and serine hydroxymethyltransferase
            enzyme.
  JOURNAL   Biochem. Soc. Trans. 1 (1973) 678-681.
REFERENCE   2  [PMID:13449064]
  AUTHORS   KARASEK MA, GREENBERG DM.
  TITLE     Studies on the properties of threonine aldolases.
  JOURNAL   J. Biol. Chem. 227 (1957) 191-205.
  ORGANISM  sheep , rat [GN:rno]
REFERENCE   3  [PMID:5017702]
  AUTHORS   Kumagai H, Nagate T, Yoshida H, Yamada H.
  TITLE     Threonine aldolase from Candida humicola. II. Purification,
            crystallization and properties.
  JOURNAL   Biochim. Biophys. Acta. 258 (1972) 779-90.
  ORGANISM  Candida humicola
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K01620  threonine aldolase
GENES       SCE: YEL046C(GLY1)
            AGO: AGOS_AFR366W
            PIC: PICST_71203(GLY2) PICST_74130(GLY1)
            CGR: CAGL0I01342g
            SPO: SPAC23H3.09c
            ANI: AN7564.2
            AFM: AFUA_2G14930 AFUA_7G06540
            AOR: AO090005000497 AO090012000408
            CNE: CNC04680
            TET: TTHERM_00989450 TTHERM_01001240
            LMA: LmjF01.0480
            ECO: b0870(ltaE)
            ECJ: JW0854(ltaE)
            ECE: Z1104(ybjU)
            ECS: ECs0956
            ECC: c1003(ybjU)
            ECI: UTI89_C0873(ybjU)
            ECP: ECP_0885
            ECV: APECO1_1224(ybjU)
            ECW: EcE24377A_0943(ltaE)
            ECX: EcHS_A0974(ltaE)
            STY: STY0930(ybjU)
            STT: t1999(ybjU)
            SPT: SPA1865(ybjU)
            SEC: SC0889(ltaA)
            STM: STM0934(ltaA)
            YPE: YPO1357(ltaA)
            YPK: y2823
            YPM: YP_1239(ltaA)
            YPA: YPA_0645
            YPN: YPN_2625
            YPP: YPDSF_2340
            YPI: YpsIP31758_2620(ltaE)
            SFL: SF0825(ybjU)
            SFX: S0866(ybjU)
            SFV: SFV_0858(ybjU)
            SSN: SSON_0856(ybjU)
            SBO: SBO_0803(ybjU)
            SDY: SDY_2393(ybjU)
            SGL: SG1098
            ENT: Ent638_1386
            SPE: Spro_1663
            XCC: XCC0460
            XCB: XC_0474
            XCV: XCV0506
            XAC: XAC0477
            XOO: XOO4048
            XOM: XOO_3823(XOO3823)
            VCH: VCA0765
            VCO: VC0395_0706(ybjU)
            VVU: VV2_0053
            VVY: VVA0561
            VPA: VPA1011
            VFI: VFA0497
            PPR: PBPRB0795(ltaA)
            PAE: PA0902 PA5413(ltaA)
            PAU: PA14_52610 PA14_71440(ltaA)
            PPU: PP_0321
            PPF: Pput_0343
            PST: PSPTO_0410 PSPTO_1841
            PSB: Psyr_3557 Psyr_4766
            PSP: PSPPH_3513
            PFL: PFL_4507 PFL_5731(ltaE)
            PFO: Pfl_4276 Pfl_5210
            PEN: PSEEN5163(ltaE)
            PMY: Pmen_2904 Pmen_4134
            PRW: PsycPRwf_0904
            SON: SO_3338(ybjU)
            SDN: Sden_1361
            SFR: Sfri_2801
            SAZ: Sama_2462
            SBL: Sbal_3011
            SBM: Shew185_3026
            SLO: Shew_1155
            SPC: Sputcn32_2673
            SSE: Ssed_1247
            SPL: Spea_1142 Spea_2205
            SHE: Shewmr4_1207
            SHM: Shewmr7_1278
            SHN: Shewana3_1208
            SHW: Sputw3181_1338
            ILO: IL0217
            PHA: PSHAb0295(ltaE)
            PIN: Ping_2292
            NOC: Noc_2606
            HCH: HCH_00857
            CSA: Csal_0880
            MMW: Mmwyl1_1844
            AHA: AHA_1795
            CVI: CV_4309
            RSO: RS05504(RSp1116) RSc0808(ltaA)
            REU: Reut_A0859
            REH: H16_A2762(ltaA)
            RME: Rmet_0809
            BMA: BMAA1834(ltaE)
            BMV: BMASAVP1_0834(ltaE)
            BML: BMA10299_1125(ltaE)
            BMN: BMA10247_A2098(ltaE)
            BXE: Bxe_A1314 Bxe_B2204
            BVI: Bcep1808_3651
            BUR: Bcep18194_B0178
            BCN: Bcen_5386
            BCH: Bcen2424_5475
            BAM: Bamb_4817
            BPS: BPSL1714 BPSS0236(ltaE)
            BPM: BURPS1710b_2159 BURPS1710b_A1771(ltaE)
            BPL: BURPS1106A_A0337(ltaE)
            BPD: BURPS668_A0430(ltaE)
            BTE: BTH_II2147
            BPE: BP2407(ltaE)
            BPA: BPP3272(ltaE)
            BBR: BB3723(ltaE)
            RFR: Rfer_3604
            POL: Bpro_2069 Bpro_4454
            PNA: Pnap_3651
            AAV: Aave_0639
            VEI: Veis_1686
            MPT: Mpe_A1430
            GSU: GSU3162 GSU3408
            GME: Gmet_0270 Gmet_3503
            GUR: Gura_1870
            DVU: DVU1878(ltaE)
            DVL: Dvul_1286
            DDE: Dde_1657
            BBA: Bd1811(lta)
            DPS: DP1003
            ADE: Adeh_0942
            AFW: Anae109_0983 Anae109_3740
            MXA: MXAN_1432
            SFU: Sfum_0699
            PUB: SAR11_0689
            MLO: mlr3032 mlr6130
            MES: Meso_2745
            PLA: Plav_1966
            SME: SMc04029
            SMD: Smed_2712
            ATU: Atu3785
            ATC: AGR_L_2098
            RET: RHE_CH03568(ypch01258)
            RLE: RL4086(ltaE) pRL110498
            BME: BMEII0041
            BMF: BAB2_0051
            BMS: BRA0052
            BMB: BruAb2_0052
            OAN: Oant_4278
            BJA: bll4016
            BRA: BRADO2796
            BBT: BBta_5390
            RPB: RPB_4433
            RPC: RPC_1602
            RPD: RPD_1764
            RPE: RPE_1630
            SIL: SPO3156
            SIT: TM1040_0162
            RSP: RSP_1448 RSP_2302
            RSH: Rsph17029_0097 Rsph17029_0977
            RSQ: Rsph17025_2198
            JAN: Jann_2851
            RDE: RD1_2890 RD1_3525(ltaE)
            PDE: Pden_3664
            MMR: Mmar10_2153
            HNE: HNE_0475(ltaE)
            ZMO: ZMO1347(ltaE)
            NAR: Saro_3267
            SAL: Sala_0496
            SWI: Swit_1176
            ELI: ELI_13610
            GOX: GOX0793
            RRU: Rru_A2249
            ABA: Acid345_2367
            SUS: Acid_5925
            BHA: BH3283
            SAU: SA1154
            SAV: SAV1315
            SAM: MW1203
            SAR: SAR1326
            SAS: SAS1256
            SAC: SACOL1349
            SAB: SAB1178c SAB1181c
            SAA: SAUSA300_1214
            SAO: SAOUHSC_01307
            SEP: SE0995
            SHA: SH1592
            SAG: SAG1756
            SAN: gbs1799
            SAK: SAK_1778(ltaE)
            STH: STH2403
            CAC: CAC3420
            CDF: CD2591(ltaE)
            CBE: Cbei_4155
            AMT: Amet_2445 Amet_3510
            CHY: CHY_0904(ltaE)
            DSY: DSY4242
            DRM: Dred_0105
            TTE: TTE0267(gly1)
            MSM: MSMEG_4454(ltaE)
            MVA: Mvan_1179
            MGI: Mflv_5153
            MMC: Mmcs_5263
            MKM: Mkms_5352
            MJL: Mjls_5642
            SCO: SCO1087(2SCG4.03c)
            SMA: SAV1488(ltaA)
            CMI: CMM_0385(ltaE)
            ART: Arth_1658
            AAU: AAur_1799
            NCA: Noca_3094
            FAL: FRAAL0384(itaE)
            ACE: Acel_0686
            KRA: Krad_1277
            SEN: SACE_7162(ltaE)
            STP: Strop_3255
            BLO: BL1103
            BAD: BAD_0527(tal)
            RXY: Rxyl_0796
            FNU: FN0810
            RBA: RB10307(gly1)
            TDE: TDE0005(ltaE)
            CYB: CYB_0540
            GVI: glr2478
            ANA: alr3296
            AVA: Ava_4955
            TER: Tery_1646
            BTH: BT_1815
            BFR: BF3384
            BFS: BF3212
            PGI: PG0474
            FJO: Fjoh_2554
            FPS: FP0874(ltaE)
            DEH: cbdb_A181(gly1)
            DEB: DehaBAV1_0218
            RCA: Rcas_0734
            DRA: DR_1313
            DGE: Dgeo_1451
            TTH: TTC0397
            TTJ: TTHA0753
            TMA: TM1744
            TPT: Tpet_1039
STRUCTURES  PDB: 1JG8  1LW4  1LW5  1M6S  1SVV  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.5
            ExPASy - ENZYME nomenclature database: 4.1.2.5
            ExplorEnz - The Enzyme Database: 4.1.2.5
            ERGO genome analysis and discovery system: 4.1.2.5
            BRENDA, the Enzyme Database: 4.1.2.5
            CAS: 62213-23-4
///
ENTRY       EC 4.1.2.6        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
COMMENT     Deleted entry: allothreonine aldolase. Reaction is due to EC
            2.1.2.1, glycine hydroxymethyltransferase (EC 4.1.2.6 created 1961,
            deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.6
            ExPASy - ENZYME nomenclature database: 4.1.2.6
            ExplorEnz - The Enzyme Database: 4.1.2.6
            ERGO genome analysis and discovery system: 4.1.2.6
            BRENDA, the Enzyme Database: 4.1.2.6
///
ENTRY       EC 4.1.2.7        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
COMMENT     Deleted entry: ketose-1-phosphate aldolase. Now included with EC
            4.1.2.13 fructose-bisphosphate aldolase (EC 4.1.2.7 created 1961,
            deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.7
            ExPASy - ENZYME nomenclature database: 4.1.2.7
            ExplorEnz - The Enzyme Database: 4.1.2.7
            ERGO genome analysis and discovery system: 4.1.2.7
            BRENDA, the Enzyme Database: 4.1.2.7
///
ENTRY       EC 4.1.2.8                  Enzyme
NAME        indole-3-glycerol-phosphate lyase;
            tryptophan synthase alpha;
            TSA;
            indoleglycerolphosphate aldolase;
            indole glycerol phosphate hydrolase;
            indole synthase;
            indole-3-glycerolphosphate D-glyceraldehyde-3-phosphate-lyase;
            indole-3-glycerol phosphate lyase;
            IGL;
            BX1;
            (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
            D-glyceraldehyde-3-phosphate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     (1S,2R)-1-C-(indol-3-yl)glycerol-3-phosphate
            D-glyceraldehyde-3-phosphate-lyase (indole-forming)
REACTION    (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole +
            D-glyceraldehyde 3-phosphate
ALL_REAC    (other) R02340
SUBSTRATE   (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate [CPD:C03506]
PRODUCT     indole [CPD:C00463];
            D-glyceraldehyde 3-phosphate [CPD:C00118]
COMMENT     Forms part of the defence mechanism against insects and microbial
            pathogens in the grass family, Gramineae, where it catalyses the
            first committed step in the formation of the cyclic hydroxamic acids
            2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one (DIBOA) and
            2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one (DIMBOA) [1].
            This enzyme resembles the alpha-subunit of EC 4.2.1.20, tryptophan
            synthase [3], for which, (1S,2R)-1-C-(indol-3-yl)glycerol
            3-phosphate is also a substrate, but, unlike tryptophan synthase,
            its activity is independent of the beta-subunit and free indole is
            released [2].
REFERENCE   1  [PMID:13376586]
  AUTHORS   YANOFSKY C.
  TITLE     The enzymatic conversion of anthranilic acid to indole.
  JOURNAL   J. Biol. Chem. 223 (1956) 171-84.
REFERENCE   2
  AUTHORS   Frey, M., Chomet, P., Glawischnig, E., Stettner, C., Grun, S.,
            Winklmair, A., Eisenreich, W., Bacher, A., Meeley, R.B., Briggs,
            S.P., Simcox, K. and Gierl, A.
  TITLE     Analysis of a chemical plant defense mechanism in grasses.
  JOURNAL   Science 277 (1997) 696-699.
REFERENCE   3  [PMID:11106389]
  AUTHORS   Frey M, Stettner C, Pare PW, Schmelz EA, Tumlinson JH, Gierl A.
  TITLE     An herbivore elicitor activates the gene for indole emission in
            maize.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 14801-6.
REFERENCE   4  [PMID:9371848]
  AUTHORS   Melanson D, Chilton MD, Masters-Moore D, Chilton WS.
  TITLE     A deletion in an indole synthase gene is responsible for the
            DIMBOA-deficient phenotype of bxbx maize.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 13345-50.
PATHWAY     PATH: map00402  Benzoxazinone biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.8
            ExPASy - ENZYME nomenclature database: 4.1.2.8
            ExplorEnz - The Enzyme Database: 4.1.2.8
            ERGO genome analysis and discovery system: 4.1.2.8
            BRENDA, the Enzyme Database: 4.1.2.8
///
ENTRY       EC 4.1.2.9                  Enzyme
NAME        phosphoketolase;
            D-xylulose-5-phosphate D-glyceraldehyde-3-phosphate-lyase
            (phosphate-acetylating)
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     D-xylulose-5-phosphate D-glyceraldehyde-3-phosphate-lyase (adding
            phosphate; acetyl-phosphate-forming)
REACTION    D-xylulose 5-phosphate + phosphate = acetyl phosphate +
            D-glyceraldehyde 3-phosphate + H2O [RN:R01621]
ALL_REAC    R01621;
            (other) R00761
SUBSTRATE   D-xylulose 5-phosphate [CPD:C00231];
            phosphate [CPD:C00009]
PRODUCT     acetyl phosphate [CPD:C00227];
            D-glyceraldehyde 3-phosphate [CPD:C00118];
            H2O [CPD:C00001]
COFACTOR    Thiamin diphosphate [CPD:C00068]
COMMENT     A thiamine-diphosphate protein.
REFERENCE   1  [PMID:13539033]
  AUTHORS   HEATH EC, HURWITZ J, HORECKER BL, GINSBURG A.
  TITLE     Pentose fermentation by Lactobacillus plantarum. I. The cleavage of
            xylulose 5-phosphate by phosphoketolase.
  JOURNAL   J. Biol. Chem. 231 (1958) 1009-29.
  ORGANISM  Lactobacillus plantarum [GN:lpl]
REFERENCE   2
  AUTHORS   Schramm, M., Klybas, V. and Racker, E.
  TITLE     Phospholytic cleavage of fructose-6-phosphate by
            fructose-6-phosphate phosphoketolase from Acetobacter xylinum.
  JOURNAL   J. Biol. Chem. 233 (1958) 1283-1288.
  ORGANISM  Acetobacter xylinum
PATHWAY     PATH: map00030  Pentose phosphate pathway
            PATH: map00680  Methane metabolism
            PATH: map00710  Carbon fixation
ORTHOLOGY   KO: K01621  phosphoketolase
GENES       PPF: Pput_2459
            SDN: Sden_2731
            SFR: Sfri_2898
            SAZ: Sama_0915
            SBL: Sbal_1046
            SBM: Shew185_1113
            SLO: Shew_1091
            SPC: Sputcn32_1051
            SSE: Ssed_1186
            SPL: Spea_1076
            SHE: Shewmr4_2965
            SHM: Shewmr7_3047
            SHN: Shewana3_3145
            SHW: Sputw3181_3114
            MCA: MCA1587
            MMW: Mmwyl1_1950
            BXE: Bxe_B1345
            SMD: Smed_2995
            RLE: RL0066
            BOV: BOV_A0333(xfp)
            OAN: Oant_4654
            ACR: Acry_3376
            SAK: SAK_1819(xpkA)
            LPL: lp_2659(xpk1) lp_3551(xpk2)
            LJO: LJ0803
            LAC: LBA0600
            LSA: LSA0289(xpk)
            LSL: LSL_1509 LSL_1956
            LDB: Ldb0534
            LBU: LBUL_0475
            LCA: LSEI_0174
            LGA: LGAS_0562
            LRE: Lreu_1686
            OOE: OEOE_1183
            RHA: RHA1_ro01493
            AAU: AAur_1848(xfp)
            STP: Strop_1582
            ANA: all1483
            AVA: Ava_4264
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.9
            ExPASy - ENZYME nomenclature database: 4.1.2.9
            ExplorEnz - The Enzyme Database: 4.1.2.9
            ERGO genome analysis and discovery system: 4.1.2.9
            BRENDA, the Enzyme Database: 4.1.2.9
            CAS: 9031-75-8
///
ENTRY       EC 4.1.2.10                 Enzyme
NAME        mandelonitrile lyase;
            hydroxynitrile lyase;
            (R)-oxynitrilase;
            oxynitrilase;
            D-oxynitrilase;
            D-alpha-hydroxynitrile lyase;
            mandelonitrile benzaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     mandelonitrile benzaldehyde-lyase (cyanide-forming)
REACTION    mandelonitrile = cyanide + benzaldehyde [RN:R01767]
ALL_REAC    R01767;
            (other) R01409 R02811
SUBSTRATE   mandelonitrile [CPD:C00561]
PRODUCT     cyanide [CPD:C00177];
            benzaldehyde [CPD:C00261]
COFACTOR    Flavin [CPD:C00176];
            Flavoprotein [CPD:C06411]
COMMENT     A variety of enzymes from different sources and with different
            properties. Some are flavoproteins, others are not. Active towards a
            number of aromatic and aliphatic hydroxynitriles (cyanohydrins).
REFERENCE   1  [PMID:13970146]
  AUTHORS   BECKER W, BENTHIN U, ESCHENHOF E, PFEIL E.
  TITLE     [On the knowledge of cyanhydrin synthesis. II. Purification and
            properties of hydroxynitrilase from bitter almonds (Prunus communis
            Stokes)]
  JOURNAL   Biochem. Z. 337 (1963) 156-66.
REFERENCE   2
  AUTHORS   Becker, W. and Pfeil, E.
  TITLE     Die Darstellung kristallisierter Oxynitrilase aus bitteren Mandeln
            (Prunus comm. Stks).
  JOURNAL   Naturwissenschaften 51 (1964) 193.
REFERENCE   3  [PMID:6803611]
  AUTHORS   Gross M, Jacobs GH, Poulton JE.
  TITLE     A rapid and sensitive spectrophotometric assay for prunasin
            hydrolase activity employing purified mandelonitrile lyase.
  JOURNAL   Anal. Biochem. 119 (1982) 25-30.
REFERENCE   4  [PMID:3777939]
  AUTHORS   Xu LL, Singh BK, Conn EE.
  TITLE     Purification and characterization of mandelonitrile lyase from
            Prunus lyonii.
  JOURNAL   Arch. Biochem. Biophys. 250 (1986) 322-8.
  ORGANISM  Prunus lyonii
REFERENCE   5  [PMID:3717954]
  AUTHORS   Yemm RS, Poulton JE.
  TITLE     Isolation and characterization of multiple forms of mandelonitrile
            lyase from mature black cherry (Prunus serotina Ehrh.) seeds.
  JOURNAL   Arch. Biochem. Biophys. 247 (1986) 440-5.
  ORGANISM  Prunus serotina
PATHWAY     PATH: map00460  Cyanoamino acid metabolism
ORTHOLOGY   KO: K08248  mandelonitrile lyase
GENES       ATH: AT1G73050
STRUCTURES  PDB: 1JU2  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.10
            ExPASy - ENZYME nomenclature database: 4.1.2.10
            ExplorEnz - The Enzyme Database: 4.1.2.10
            ERGO genome analysis and discovery system: 4.1.2.10
            BRENDA, the Enzyme Database: 4.1.2.10
            CAS: 9024-43-5
///
ENTRY       EC 4.1.2.11                 Enzyme
NAME        hydroxymandelonitrile lyase;
            hydroxynitrile lyase;
            oxynitrilase;
            Sorghum hydroxynitrile lyase;
            (S)-4-hydroxymandelonitrile hydroxybenzaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     (S)-4-hydroxymandelonitrile 4-hydroxybenzaldehyde-lyase
            (cyanide-forming)
REACTION    (S)-4-hydroxymandelonitrile = cyanide + 4-hydroxybenzaldehyde
            [RN:R02676]
ALL_REAC    R02676;
            (other) R01409 R02811
SUBSTRATE   (S)-4-hydroxymandelonitrile [CPD:C03742]
PRODUCT     cyanide [CPD:C00177];
            4-hydroxybenzaldehyde [CPD:C00633]
COMMENT     Does not accept aliphatic hydroxynitriles, unlike EC 4.1.2.10
            (mandelonitrile lyase) and EC 4.1.2.37 (hydroxynitrilase).
REFERENCE   1  [PMID:16495254]
  AUTHORS   Hong Y, Shaw PJ, Nath CE, Yadav SP, Stephen KR, Earl JW, McLachlan
            AJ.
  TITLE     Population pharmacokinetics of liposomal amphotericin B in pediatric
            patients with malignant diseases.
  JOURNAL   Antimicrob. Agents. Chemother. 50 (2006) 935-42.
REFERENCE   2  [PMID:5922969]
  AUTHORS   Seely MK, Criddle RS, Conn EE.
  TITLE     The metabolism of aromatic compounds in higher plants. 8. On the
            requirement of hydroxynitrile lyase for flavin.
  JOURNAL   J. Biol. Chem. 241 (1966) 4457-62.
  ORGANISM  Sorghum vulgare
PATHWAY     PATH: map00460  Cyanoamino acid metabolism
ORTHOLOGY   KO: K08249  hydroxymandelonitrile lyase
GENES       ATH: AT3G07990(SCPL27)
            OSA: 4327407
STRUCTURES  PDB: 1GXS  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.11
            ExPASy - ENZYME nomenclature database: 4.1.2.11
            ExplorEnz - The Enzyme Database: 4.1.2.11
            ERGO genome analysis and discovery system: 4.1.2.11
            BRENDA, the Enzyme Database: 4.1.2.11
            CAS: 9075-38-1
///
ENTRY       EC 4.1.2.12                 Enzyme
NAME        2-dehydropantoate aldolase;
            ketopantoaldolase;
            2-dehydropantoate formaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     2-dehydropantoate formaldehyde-lyase
            (3-methyl-2-oxobutanoate-forming)
REACTION    2-dehydropantoate = 3-methyl-2-oxobutanoate + formaldehyde
            [RN:R01216]
ALL_REAC    R01216
SUBSTRATE   2-dehydropantoate [CPD:C00966]
PRODUCT     3-methyl-2-oxobutanoate [CPD:C00141];
            formaldehyde [CPD:C00067]
REFERENCE   1
  AUTHORS   McIntosh, E.N., Purko, M. and Wood, W.A.
  TITLE     Ketopantoate formation by a hydroxymethylation enzyme from
            Escherichia coli.
  JOURNAL   J. Biol. Chem. 228 (1957) 499-510.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.12
            ExPASy - ENZYME nomenclature database: 4.1.2.12
            ExplorEnz - The Enzyme Database: 4.1.2.12
            ERGO genome analysis and discovery system: 4.1.2.12
            BRENDA, the Enzyme Database: 4.1.2.12
            CAS: 9024-51-5
///
ENTRY       EC 4.1.2.13                 Enzyme
NAME        fructose-bisphosphate aldolase;
            aldolase;
            fructose-1,6-bisphosphate triosephosphate-lyase;
            fructose diphosphate aldolase;
            diphosphofructose aldolase;
            fructose 1,6-diphosphate aldolase;
            ketose 1-phosphate aldolase;
            phosphofructoaldolase;
            zymohexase;
            fructoaldolase;
            fructose 1-phosphate aldolase;
            fructose 1-monophosphate aldolase;
            1,6-Diphosphofructose aldolase;
            SMALDO;
            D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase
            (glycerone-phosphate-forming)
REACTION    D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde
            3-phosphate [RN:R01068]
ALL_REAC    R01068 > R01070;
            (other) R01829 R02568 R05378
SUBSTRATE   D-fructose 1,6-bisphosphate [CPD:C00354]
PRODUCT     glycerone phosphate [CPD:C00111];
            D-glyceraldehyde 3-phosphate [CPD:C00118]
COFACTOR    Zinc [CPD:C00038]
COMMENT     Also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial
            enzymes are zinc proteins. The enzymes increase electron-attraction
            by the carbonyl group, some (Class I) forming a protonated imine
            with it, others (Class II), mainly of microbial origin, polarizing
            it with a metal ion, e.g. zinc.
REFERENCE   1
  AUTHORS   Horecker, B.L., Tsolas, O. and Lai, C.Y.
  TITLE     Aldolases.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 7, Academic Press,
            New York, 1972, p. 213-258.
REFERENCE   2  [PMID:2649077]
  AUTHORS   Alefounder PR, Baldwin SA, Perham RN, Short NJ.
  TITLE     Cloning, sequence analysis and over-expression of the gene for the
            class II fructose 1,6-bisphosphate aldolase of Escherichia coli.
  JOURNAL   Biochem. J. 257 (1989) 529-34.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00030  Pentose phosphate pathway
            PATH: map00031  Inositol metabolism
            PATH: map00051  Fructose and mannose metabolism
            PATH: map00710  Carbon fixation
ORTHOLOGY   KO: K01622  fructose-bisphosphate aldolase
            KO: K01623  fructose-bisphosphate aldolase, class I
            KO: K01624  fructose-bisphosphate aldolase, class II
            KO: K03339  myo-inositol catabolism protein IolJ
GENES       HSA: 226(ALDOA) 229(ALDOB) 230(ALDOC)
            PTR: 464623(ALDOB) 493951(ALDOC)
            MMU: 11674(Aldoa) 11676(Aldoc) 230163(Aldob)
            RNO: 24189(Aldoa) 24190(Aldob) 24191(Aldoc)
            CFA: 474787(ALDOB) 476719(LOC476719)
            GGA: 427308(ALDOB) 771702(LOC771702)
            XLA: 379254(xaldb) 379336(MGC53030) 379489(MGC64482) 380079(aldoc)
                 398623(LOC398623)
            XTR: 394736(MGC76327) 407969(MGC69434) 448112(aldoa)
            DRE: 321664(aldob) 369193(aldoc)
            SPU: 548623(LOC548623) 592868(LOC592868)
            DME: Dmel_CG6058(Ald)
            CEL: F01F1.12 T05D4.1
            ATH: AT2G01140 AT2G36460 AT3G52930 AT4G26520 AT4G26530 AT4G38970
            OSA: 4326074 4341496 4344545 4349897
            CME: CME145C CMI049C
            SCE: YKL060C(FBA1)
            AGO: AGOS_ABR068C
            PIC: PICST_85951(FBA1)
            CAL: CaO19_4618(CaO19.4618)
            CGR: CAGL0L02497g
            SPO: SPBC19C2.07(fba1)
            ANI: AN2875.2
            AFM: AFUA_3G11690
            AOR: AO090003000725
            CNE: CNB00300
            ECU: ECU01_0240
            DDI: DDB_0231387(fba)
            PFA: PF14_0425
            CPV: cgd1_3020
            CHO: Chro.10335
            TAN: TA20060
            TPV: TP01_0101
            TET: TTHERM_00487090
            TBR: Tb10.70.1370
            TCR: 504163.40 504163.50 510301.10 510301.20
            LMA: LmjF36.1260
            EHI: 19.t00021 223.t00001
            ECO: b2097(fbaB) b2925(fbaA)
            ECJ: JW2892(fbaA) JW5344(fbaB)
            ECE: Z3260 Z4263(fba) Z5687
            ECS: ECs2900 ECs3796 ECs5069
            ECC: c2623 c3503(fba) c4483
            ECI: UTI89_C2371 UTI89_C3308(fba) UTI89_C4203
            ECP: ECP_2135 ECP_2914 ECP_3756
            ECV: APECO1_2803 APECO1_3608(fba) APECO1_4448
            ECW: EcE24377A_2385(fbaB) EcE24377A_3253(fbaA)
            ECX: EcHS_A2233(fbaB) EcHS_A3083(fbaA)
            STY: STY2370(fbaB) STY3226(fba)
            STT: t0715(fbaB) t2987(fba)
            SPT: SPA0711(fbaB) SPA2939(fba)
            SEC: SC2156(fbaB) SC3010(fba)
            STM: STM2141(fbaB) STM3068(fba)
            YPE: YPO0920(fbaA) YPO3960
            YPK: y3307(fba) y3869
            YPM: YP_3323(fba) YP_3520(fbaA)
            YPA: YPA_0344 YPA_3788
            YPN: YPN_3046 YPN_3119 YPN_3609
            YPP: YPDSF_0593 YPDSF_0670 YPDSF_3324
            YPS: YPTB3195(fbaA) YPTB3803
            YPI: YpsIP31758_0850(fbaA)
            SFL: SF2159 SF2910(fba)
            SFX: S2285 S3110(fba)
            SFV: SFV_2152 SFV_2971(fba)
            SSN: SSON_2145 SSON_3077(fba)
            SBO: SBO_0918 SBO_3068(fba)
            SDY: SDY_2270 SDY_3157(fba) SDY_4132
            ECA: ECA0338 ECA3911(fbaA)
            PLU: plu0957(fba) plu2781(fbaB)
            BUC: BU451(fba)
            BAS: BUsg436(fba)
            BAB: bbp401(fba)
            BCC: BCc_279(fba)
            WBR: WGLp306(fba)
            SGL: SG2014
            ENT: Ent638_0285 Ent638_2708 Ent638_3338 Ent638_3578
            SPE: Spro_1033 Spro_2255 Spro_2579 Spro_3568 Spro_3944
            BFL: Bfl255(fba)
            BPN: BPEN_262(fbaA)
            HIN: HI0524(fba)
            HIT: NTHI0650(fba)
            HIQ: CGSHiGG_05870
            HDU: HD0864(fbaA)
            HSO: HS_0206(fba)
            PMU: PM1373(fbaA) PM1861(fba)
            MSU: MS0244(fba)
            APL: APL_1250(fba)
            ASU: Asuc_0536
            XFA: XF0826
            XFT: PD1845(fbaB)
            XCC: XCC3185
            XCB: XC_0979
            XCV: XCV3462(fbaB)
            XAC: XAC3344
            XOO: XOO3412
            XOM: XOO_3212(XOO3212)
            VCH: VC0478
            VCO: VC0395_A0031(fbaA)
            VVU: VV1_1541
            VVY: VV2857
            VPA: VP2599
            VFI: VF0443
            PPR: PBPRA3130
            PAE: PA0555(fda)
            PAU: PA14_07230(fda)
            PAP: PSPA7_0658(fba)
            PPU: PP_4960(fda)
            PPF: Pput_4833
            PST: PSPTO_0390(fba)
            PSB: Psyr_4787
            PSP: PSPPH_4816(fba)
            PFL: PFL_5781(fba)
            PFO: Pfl_5262
            PEN: PSEEN5019(fda)
            PMY: Pmen_0462 Pmen_3131
            PAR: Psyc_0085 Psyc_0708(fba)
            PCR: Pcryo_0092 Pcryo_0683
            PRW: PsycPRwf_2273
            ACI: ACIAD1925(fda)
            ACB: A1S_1544
            SON: SO_0933(fba)
            SDN: Sden_1086
            SFR: Sfri_0650
            SAZ: Sama_2756
            SBL: Sbal_0830
            SBM: Shew185_3537
            SLO: Shew_0755
            SPC: Sputcn32_0875
            SSE: Ssed_0877
            SPL: Spea_0791
            SHE: Shewmr4_0776
            SHM: Shewmr7_3247
            SHN: Shewana3_3350
            SHW: Sputw3181_3298
            ILO: IL2211(gatY)
            CPS: CPS_3876(fba)
            PHA: PSHAa0596(fbaA) PSHAa1093(fbaA) PSHAa1743(fbaA) PSHAb0548
            PAT: Patl_3327
            SDE: Sde_1277 Sde_3279
            PIN: Ping_0372 Ping_2682
            MAQ: Maqu_1058 Maqu_3037
            CBU: CBU_1778(fbaA)
            CBD: COXBU7E912_0229(fba)
            LPN: lpg0470
            LPF: lpl0511
            LPP: lpp0535
            MCA: MCA3041(fbaA-1) MCA3047(fbaA-2)
            FTU: FTT1365c(fbaB)
            FTF: FTF1365c(fbaB)
            FTW: FTW_0526(fba)
            FTL: FTL_1149
            FTH: FTH_1124(fba)
            FTA: FTA_1212(fba)
            FTN: FTN_1329(fbaA)
            TCX: Tcr_0248
            NOC: Noc_2804
            AEH: Mlg_2089 Mlg_2844
            HHA: Hhal_1039
            HCH: HCH_01538(fba)
            CSA: Csal_0370 Csal_0375
            ABO: ABO_2612(fda)
            MMW: Mmwyl1_1951 Mmwyl1_4316
            AHA: AHA_0782(fbaA)
            DNO: DNO_0166(fba)
            BCI: BCI_0646(fbaA)
            RMA: Rmag_0067
            VOK: COSY_0074(fbaA)
            NME: NMB1869
            NMA: NMA0587(fba)
            NMC: NMC0350(fba)
            NGO: NGO0034
            CVI: CV_0187(agaY)
            RSO: RSc0573(fbaA)
            REU: Reut_A0557 Reut_B4512
            REH: H16_A0568(fba) H16_B0278(fbaB) H16_B1384(cbbA2)
            RME: Rmet_0503 Rmet_1492 Rmet_1518
            BMA: BMA0299(cbbA)
            BMV: BMASAVP1_A0594(cbbA)
            BML: BMA10299_A2428(cbbA)
            BMN: BMA10247_0040(cbbA)
            BXE: Bxe_A0691 Bxe_B1334 Bxe_B2447
            BVI: Bcep1808_2741
            BUR: Bcep18194_A5957 Bcep18194_B0565 Bcep18194_C6861
            BCN: Bcen_2015
            BCH: Bcen2424_2626
            BAM: Bamb_2673
            BPS: BPSL0798(cbbA)
            BPM: BURPS1710b_0997(fba)
            BPL: BURPS1106A_0841(fba)
            BPD: BURPS668_0836(fba)
            BTE: BTH_I0665(fba)
            PNU: Pnuc_1815
            BPE: BP1519(fba)
            BPA: BPP1192(fba)
            BBR: BB1408(fba)
            RFR: Rfer_0204
            POL: Bpro_1287 Bpro_4630 Bpro_4741
            PNA: Pnap_1988 Pnap_3869
            AAV: Aave_4576
            AJS: Ajs_3955
            VEI: Veis_4747
            MPT: Mpe_A0291(cbbA) Mpe_A2793(cbbA)
            HAR: HEAR2609(fda)
            MMS: mma_2846(fba)
            NEU: NE0324(cbbA)
            NET: Neut_1581 Neut_1996
            NMU: Nmul_A0384 Nmul_A1561
            EBA: ebA1107(fbaA)
            AZO: azo2843(fba)
            DAR: Daro_3596 Daro_3624
            TBD: Tbd_0163(cbbA) Tbd_1513
            MFA: Mfla_2243
            HPY: HP0176(tsr)
            HPJ: jhp0162(fba)
            HPA: HPAG1_0172
            HHE: HH0106(fba)
            HAC: Hac_0357(fba)
            WSU: WS1280
            TDN: Tmden_0509
            CJE: Cj0597(fba)
            CJR: CJE0700(fbaA)
            CJJ: CJJ81176_0625(fbaA)
            CJU: C8J_0559(fba)
            CJD: JJD26997_1072(fbaA)
            CFF: CFF8240_0515(fbaA)
            CCV: CCV52592_0113(fbaA) CCV52592_0739
            CHA: CHAB381_1220(fbaA)
            CCO: CCC13826_0901 CCC13826_2070(fbaA)
            ABU: Abu_0377(fba)
            NIS: NIS_0562(fbaA) NIS_0927
            SUN: SUN_1211(fbaB) SUN_1802(fbaA)
            PCA: Pcar_2253 Pcar_2804
            PPD: Ppro_1853
            DVU: DVU2143(fba)
            DVL: Dvul_1089 Dvul_2477
            DDE: Dde_2341 Dde_3490 Dde_3502
            LIP: LI0763(fba)
            BBA: Bd2339(fba)
            DPS: DP2457
            ADE: Adeh_2510
            AFW: Anae109_1359
            MXA: MXAN_3743
            SAT: SYN_02954
            SFU: Sfum_1469
            WOL: WD1238
            WBM: Wbm0097
            AMA: AM1194(fbaB)
            APH: APH_1258(fba)
            ERU: Erum0650(fbaB)
            ERW: ERWE_CDS_00590(fbaB)
            ERG: ERGA_CDS_00560(fbaB)
            ECN: Ecaj_0059
            ECH: ECH_0097(fba)
            NSE: NSE_0142
            PUB: SAR11_0584(fbaB)
            MLO: mll7273 mlr3754
            MES: Meso_3436
            PLA: Plav_2105
            SME: SMb20199(cbbA) SMb21192(cbbA2) SMc03983(fbaB)
            SMD: Smed_2654 Smed_3923 Smed_4683
            ATU: Atu3740
            ATC: AGR_L_2190
            RET: RHE_CH03500(fbaB)
            RLE: RL0646 RL4012 pRL120027 pRL120196 pRL120762
            BME: BMEII0423
            BMF: BAB2_0365(fbaA)
            BMS: BRA0871(fbaA)
            BMB: BruAb2_0361(fbaA)
            BOV: BOV_A0818(fba)
            OAN: Oant_1185 Oant_2904
            BJA: bll1520 bll1521 blr2584(cbbA)
            BRA: BRADO1120(cbbA) BRADO1658(cbbA)
            BBT: BBta_0450(cbbA) BBta_0455 BBta_6398(cbbA) BBta_6928(cbbA)
                 BBta_6929
            RPA: RPA0940 RPA4642(cbbA)
            RPB: RPB_0950 RPB_4471
            RPC: RPC_2896 RPC_4773
            RPD: RPD_1053 RPD_4317
            RPE: RPE_2685 RPE_4722
            NWI: Nwi_2692 Nwi_2737
            NHA: Nham_3534 Nham_3752
            BHE: BH15060(fbaB)
            BQU: BQ11980(fbaB)
            BBK: BARBAKC583_0141(fbaB)
            XAU: Xaut_1912 Xaut_3077
            CCR: CC_3250
            SIL: SPO1899(fda)
            SIT: TM1040_1976 TM1040_3351
            RSP: RSP_1283(cfxA) RSP_3270(cfxB) RSP_4045(fbaB)
            RSH: Rsph17029_1151 Rsph17029_2942 Rsph17029_4003
            RSQ: Rsph17025_1096 Rsph17025_2713
            JAN: Jann_1417 Jann_1693
            RDE: RD1_0218(fba) RD1_2270(fda)
            PDE: Pden_1698 Pden_1920
            MMR: Mmar10_2595
            HNE: HNE_3181(fda)
            ZMO: ZMO0179(fbaB)
            NAR: Saro_1964
            SAL: Sala_1317
            SWI: Swit_2606
            ELI: ELI_05235
            GOX: GOX0780 GOX1540
            GBE: GbCGDNIH1_1090
            ACR: Acry_0380 Acry_0823
            RRU: Rru_A0596 Rru_A1345 Rru_A2509
            MAG: amb1380
            MGM: Mmc1_3218
            ABA: Acid345_1613
            SUS: Acid_3936
            BSU: BG10412(fbaA) BG11125(iolJ)
            BHA: BH2314 BH3786(fbaA)
            BAN: BA2516(fba-1) BA5580(fba-2)
            BAR: GBAA2516(fba-1) GBAA5580(fba-2)
            BAA: BA_0436 BA_3008
            BAT: BAS2337 BAS5184
            BCE: BC5335
            BCA: BCE_5465(fba)
            BCZ: BCZK2256(fba) BCZK5035 pE33L466_0305(fba)
            BCY: Bcer98_3856
            BTK: BT9727_2300(fbaA) BT9727_5019
            BTL: BALH_2262(fbaA) BALH_4833
            BLI: BL00237(fbaB) BL03969(fbaA)
            BLD: BLi03960(fbaA) BLi04242(fbaB)
            BCL: ABC0428(iolJ) ABC0445 ABC0858 ABC3195 ABC3505 ABC3568
                 ABC3883(fbaA)
            BAY: RBAM_034280(fbaA) RBAM_036690(fbaB)
            BPU: BPUM_1767 BPUM_3357(fbaA)
            OIH: OB3005 OB3245
            GKA: GK1886(fbaA) GK3386
            SAU: SA1927(fbaA) SA2399
            SAV: SAV2125(fbaA) SAV2606
            SAM: MW2049(fbaA) MW2525
            SAR: SAR2213 SAR2684(fda)
            SAS: SAS2028 SAS2491
            SAC: SACOL2117(fbaA) SACOL2622(fdaB)
            SAB: SAB2009c SAB2479(fda)
            SAA: SAUSA300_2079(fba) SAUSA300_2540
            SAO: SAOUHSC_02366 SAOUHSC_02926
            SAJ: SaurJH9_2161 SaurJH9_2628
            SAH: SaurJH1_2199 SaurJH1_2682
            SEP: SE1723 SE2156
            SER: SERP1732(fbaA) SERP2166(fdaB)
            SHA: SH0450 SH0910(fbaA)
            SSP: SSP0191 SSP0759
            LMO: lmo0359 lmo2133 lmo2556(fbaA)
            LMF: LMOf2365_0379 LMOf2365_2167 LMOf2365_2528
            LIN: lin0378 lin2238 lin2701(fbaA)
            LWE: lwe0316 lwe2152 lwe2153 lwe2506(fbaA)
            LLA: L0009(fbaA)
            LLC: LACR_2168
            LLM: llmg_2167(fbaA)
            SPY: SPy_1889(fba)
            SPZ: M5005_Spy_1607(fba)
            SPM: spyM18_1954
            SPG: SpyM3_1630(fba)
            SPS: SPs0237
            SPH: MGAS10270_Spy1676(fba)
            SPI: MGAS10750_Spy1663(fba)
            SPJ: MGAS2096_Spy1631(fba)
            SPK: MGAS9429_Spy1610(fba)
            SPF: SpyM50246(fba)
            SPA: M6_Spy1616
            SPB: M28_Spy1597(fba)
            SPN: SP_0605
            SPR: spr0530(fba)
            SPD: SPD_0526(fba)
            SAG: SAG0127(fba)
            SAN: gbs0125
            SAK: SAK_0178(fba)
            SMU: SMU.99(fbaA)
            STC: str1899(fba)
            STL: stu1899(fba)
            STE: STER_1876
            SSA: SSA_1992(fba)
            SSV: SSU98_0330
            SGO: SGO_1745(fba)
            LPL: lp_0330(fba)
            LJO: LJ0687
            LAC: LBA1599(fbaA)
            LSA: LSA1527(fba)
            LSL: LSL_0406(fba)
            LDB: Ldb1544(fba)
            LBU: LBUL_1433
            LCA: LSEI_0328 LSEI_0432 LSEI_2704
            LGA: LGAS_0467
            LRE: Lreu_0238
            PPE: PEPE_1352
            EFA: EF1167(fba)
            STH: STH2683
            CAC: CAC0827 CA_P0064(alf)
            CPE: CPE0086(alf1) CPE1350(alf2)
            CPF: CPF_0081 CPF_1557(fba)
            CPR: CPR_1350(fba)
            CTC: CTC00341 CTC00507
            CNO: NT01CX_1380
            CTH: Cthe_0349
            CDF: CD0403(fba)
            CBO: CBO0193
            CBA: CLB_0234(fba)
            CBH: CLC_0249(fba)
            CBF: CLI_0258(fba)
            CBE: Cbei_1903 Cbei_3039 Cbei_4551
            CKL: CKL_3599(fba)
            AMT: Amet_3675
            CHY: CHY_0128(fba)
            DSY: DSY4939
            DRM: Dred_3176
            SWO: Swol_2411
            CSC: Csac_0349 Csac_1189
            TTE: TTE0137(fba)
            MTA: Moth_0474 Moth_2404
            MGE: MG_023(fba)
            MPN: MPN025(tsr)
            MPU: MYPU_1100(fba) MYPU_3600(fba)
            MPE: MYPE10340
            MGA: MGA_0498(fba)
            MMY: MSC_0139(fbaA2) MSC_0644(fbaA1)
            MMO: MMOB1260(fba)
            MHY: mhp014(fba) mhp589
            MHJ: MHJ_0014(fba) MHJ_0574(fba-1)
            MHP: MHP7448_0014(fba) MHP7448_0573(fba-1)
            MSY: MS53_0354(fba)
            MCP: MCAP_0136(fba)
            UUR: UU596(tsr)
            POY: PAM172(fba)
            AYW: AYWB_547(fba)
            MFL: Mfl644
            MTU: Rv0363c(fba)
            MTC: MT0379(fba)
            MBO: Mb0370c(fba)
            MBB: BCG_0401c(fba)
            MLE: ML0286(fba)
            MPA: MAP4308c
            MAV: MAV_5271
            MSM: MSMEG_0752(fbaA) MSMEG_3507
            MVA: Mvan_0670 Mvan_3341
            MGI: Mflv_0234 Mflv_3550
            MMC: Mmcs_0503 Mmcs_2704
            MKM: Mkms_0514 Mkms_2748
            MJL: Mjls_0492 Mjls_2734
            CGL: NCgl2673(cgl2770)
            CGB: cg3068(fda)
            CEF: CE2601(fda)
            CDI: DIP2094(fba)
            CJK: jk0216(fda)
            NFA: nfa53820(fba)
            RHA: RHA1_ro05536(fba)
            SCO: SCO3649(fba)
            SMA: SAV4523(fbaA)
            LXX: Lxx16680(fba)
            CMI: CMM_2226(fbaA)
            ART: Arth_0518 Arth_1712
            AAU: AAur_0555(fbaA)
            PAC: PPA2011 PPA2024
            NCA: Noca_1003 Noca_4350
            TFU: Tfu_3010
            FRA: Francci3_2070 Francci3_4205 Francci3_4364
            FAL: FRAAL6655(fbaA)
            ACE: Acel_2125
            KRA: Krad_2157 Krad_4124
            SEN: SACE_7180(fba)
            STP: Strop_0130 Strop_4157
            BLO: BL0550(fba)
            BAD: BAD_0066(fba)
            RXY: Rxyl_2541
            FNU: FN0322
            RBA: RB4737(fbaB) RB6690(fba)
            CTR: CT215(dhnA)
            CTA: CTA_0235(dhnA)
            CMU: TC0487
            CPN: CPn0281(dhnA)
            CPA: CP0477
            CPJ: CPj0281(dhnA)
            CPT: CpB0289
            CCA: CCA00499(fbaB)
            CAB: CAB486(fbaB)
            CFE: CF0509(dhnA)
            PCU: pc0933(dhnA)
            BBU: BB0445(fba)
            BGA: BG0453(fba)
            BAF: BAPKO_0467(fba)
            TPA: TP0662
            TDE: TDE0340
            LIL: LA1532(fbaB)
            LIC: LIC12233
            LBJ: LBJ_1098
            LBL: LBL_1147
            SYN: sll0018(cbbA) slr0943(fda)
            SYW: SYNW0791(cbbA)
            SYC: syc0113_c
            SYF: Synpcc7942_1443
            SYD: Syncc9605_1857
            SYE: Syncc9902_0796 Syncc9902_0797
            SYG: sync_1703(fba) sync_1704
            SYR: SynRCC307_1493(cbbA) SynRCC307_2020(fbaB)
            SYX: SynWH7803_1145(cbbA) SynWH7803_2152(fbaB)
            CYA: CYA_1500(fba)
            CYB: CYB_0357(fba)
            TEL: tlr0376(fbaA)
            GVI: gll0752(fda) gll1025(fda)
            ANA: all3735 all4563(fda)
            AVA: Ava_1590 Ava_2492
            PMA: Pro0855(cbbA) Pro0856(fda)
            PMM: PMM0781(cbbA)
            PMT: PMT0537(cbbA)
            PMN: PMN2A_0188
            PMI: PMT9312_0789
            PMB: A9601_08441(cbbA) A9601_08451
            PMC: P9515_08001 P9515_08011(cbbA)
            PMG: P9301_08421(cbbA)
            PME: NATL1_08201
            TER: Tery_1687 Tery_4099
            BTH: BT_1106 BT_1659 BT_1691
            BFR: BF3251 BF3299
            BFS: BF3090(fbaB) BF3138(fba)
            PGI: PG1755(fbaB)
            SRU: SRU_1906
            CHU: CHU_1341(alf) CHU_3060(fbaA)
            GFO: GFO_0384(fbaA)
            FJO: Fjoh_0953 Fjoh_1463
            FPS: FP0323(fbaA)
            CTE: CT1053(fbaA)
            CCH: Cag_0728
            CPH: Cpha266_0194 Cpha266_1329 Cpha266_2002
            PVI: Cvib_0463 Cvib_0892
            PLT: Plut_0519 Plut_1021
            DRA: DR_1589
            DGE: Dgeo_2083
            TTH: TTC1414
            TTJ: TTHA1773
            AAE: aq_1390(fba)
            TMA: TM0273
            TPT: Tpet_0651
            TME: Tmel_1272
            FNO: Fnod_0761
            MMQ: MmarC5_0890 MmarC5_1380
            MMZ: MmarC7_1296 MmarC7_1710
            MAE: Maeo_0316 Maeo_0690
            MVN: Mevan_1304 Mevan_1506
            MAC: MA0439 MA2666
            MBA: Mbar_A0176 Mbar_A0753
            MMA: MM_0714 MM_1627
            MBU: Mbur_0917 Mbur_2001
            MTP: Mthe_0380 Mthe_0532 Mthe_0617 Mthe_1312
            MHU: Mhun_1035 Mhun_1036 Mhun_1466
            MEM: Memar_1302 Memar_1303 Memar_1367
            MBN: Mboo_1557 Mboo_1558
            HMA: rrnAC0345(fba)
            HWA: HQ1156A(fba)
            NPH: NP1594A(fba_1) NP3160A(fba_2)
            PHO: PH0082
            PAB: PAB0049
            PFU: PF1956
            TKO: TK0989
            RCI: RCIX1359(fbaA) RCIX768(fbaB-1) RRC80(fbaB-2)
            APE: APE_0011.1
            SMR: Smar_1596
            MSE: Msed_0237
            TPE: Tpen_0837 Tpen_1648
STRUCTURES  PDB: 1A5C  1ADO  1ALD  1B57  1DOS  1EPX  1EWD  1EWE  1EWG  1EX5  
                 1F2J  1FBA  1FDJ  1GYN  1J4E  1OJX  1OK4  1OK6  1QO5  1RV8  
                 1RVG  1W8R  1W8S  1XDL  1XDM  1XFB  1ZAH  1ZAI  1ZAJ  1ZAL  
                 1ZEN  2ALD  2EPH  2FJK  2IQT  2ISV  2ISW  2OT0  2OT1  2PC4  
                 2QAP  2QDG  2QDH  2QUT  2QUU  2QUV  4ALD  6ALD  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.13
            ExPASy - ENZYME nomenclature database: 4.1.2.13
            ExplorEnz - The Enzyme Database: 4.1.2.13
            ERGO genome analysis and discovery system: 4.1.2.13
            BRENDA, the Enzyme Database: 4.1.2.13
            CAS: 9024-52-6
///
ENTRY       EC 4.1.2.14                 Enzyme
NAME        2-dehydro-3-deoxy-phosphogluconate aldolase;
            phospho-2-keto-3-deoxygluconate aldolase;
            KDPG aldolase;
            phospho-2-keto-3-deoxygluconic aldolase;
            2-keto-3-deoxy-6-phosphogluconic aldolase;
            2-keto-3-deoxy-6-phosphogluconate aldolase;
            6-phospho-2-keto-3-deoxygluconate aldolase;
            ODPG aldolase;
            2-oxo-3-deoxy-6-phosphogluconate aldolase;
            2-keto-3-deoxygluconate-6-P-aldolase;
            2-keto-3-deoxygluconate-6-phosphate aldolase;
            2-dehydro-3-deoxy-D-gluconate-6-phosphate
            D-glyceraldehyde-3-phosphate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     2-dehydro-3-deoxy-D-gluconate-6-phosphate
            D-glyceraldehyde-3-phosphate-lyase (pyruvate-forming)
REACTION    2-dehydro-3-deoxy-D-gluconate 6-phosphate = pyruvate +
            D-glyceraldehyde 3-phosphate [RN:R05605]
ALL_REAC    R05605;
            (other) R00471
SUBSTRATE   2-dehydro-3-deoxy-D-gluconate 6-phosphate [CPD:C04442]
PRODUCT     pyruvate [CPD:C00022];
            D-glyceraldehyde 3-phosphate [CPD:C00118]
COMMENT     Also acts on 2-oxobutanoate.
REFERENCE   1
  AUTHORS   Meloche, H.P. and Wood, W.A.
  TITLE     Crystallization and characteristics of
            2-keto-3-deoxy-6-phosphogluconic aldolase.
  JOURNAL   J. Biol. Chem. 239 (1964) 3515-3518.
  ORGANISM  Pseudomonas fluorescens, Pseudomonas saccharophila
PATHWAY     PATH: map00030  Pentose phosphate pathway
            PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K01625  2-dehydro-3-deoxyphosphogluconate aldolase
GENES       CME: CMP292C
            ECO: b1850(eda)
            ECJ: JW1839(eda)
            ECE: Z2902(eda)
            ECS: ECs2560
            ECC: c2263(eda) c4777
            ECI: UTI89_C2053(eda) UTI89_C4415
            ECP: ECP_1794
            ECW: EcE24377A_2080(eda)
            ECX: EcHS_A1942(eda)
            STY: STY2091(kdgA)
            STT: t0993
            SPT: SPA0985(eda)
            SEC: SC1889(eda)
            STM: STM1884(eda)
            YPE: YPO2067(eda)
            YPK: y2243(eda)
            YPM: YP_1910(eda)
            YPA: YPA_1450
            YPN: YPN_1544
            YPP: YPDSF_1055
            YPS: YPTB2050(eda)
            YPI: YpsIP31758_2021(eda)
            SFL: SF1860(eda)
            SFX: S1926(eda)
            SFV: SFV_1852(eda)
            SSN: SSON_1298(eda)
            SBO: SBO_1158(eda)
            SDY: SDY_1136(eda)
            ECA: ECA2478(eda)
            PLU: plu0178(eda)
            ENT: Ent638_2419
            SPE: Spro_2767
            HIN: HI0047(eda)
            HIT: NTHI0055(eda)
            HSO: HS_1603(eda)
            PMU: PM0947(eda)
            MSU: MS0546(eda) MS0566(eda)
            APL: APL_1018(eda)
            ASU: Asuc_1471
            XFA: XF1061
            XFT: PD0342(eda)
            XCC: XCC2140(eda)
            XCB: XC_1973
            XCV: XCV2233(alkH)
            XAC: XAC2067(eda)
            XOO: XOO2318(eda)
            XOM: XOO_2195(XOO2195)
            VCH: VC0285
            VVU: VV1_1102 VV2_0904 VV2_1072
            VVY: VV0062 VV0555 VVA1387 VVA1596
            VPA: VP0065 VPA0083 VPA1708
            VFI: VF0090 VFA0987
            PPR: PBPRA1276 PBPRB0159(eda) PBPRB1732 PBPRB1883
            PAE: PA3131 PA3181
            PPU: PP_1024(eda)
            PPF: Pput_1062
            PST: PSPTO_1302(eda-1) PSPTO_2178(eda-2)
            PSB: Psyr_1122 Psyr_1988
            PSP: PSPPH_1190(eda1) PSPPH_1957(eda2)
            PFL: PFL_4608(eda)
            PFO: Pfl_4124 Pfl_4361
            PEN: PSEEN4403(eda)
            PMY: Pmen_3141
            ACI: ACIAD0543(eda)
            SON: SO_2486(eda)
            SDN: Sden_2076
            SAZ: Sama_1809
            SBL: Sbal_2238
            SBM: Shew185_2133
            SLO: Shew_2045
            SPC: Sputcn32_1869
            SPL: Spea_2332
            SHE: Shewmr4_2043
            SHM: Shewmr7_1932
            SHN: Shewana3_2148
            SHW: Sputw3181_2139
            CPS: CPS_2284(eda)
            PHA: PSHAa1367(eda) PSHAa1744
            PAT: Patl_0974
            SDE: Sde_1382
            PIN: Ping_0129 Ping_2930
            MAQ: Maqu_1832
            CBU: CBU_1277(eda)
            CBD: COXBU7E912_1366(eda)
            LPN: lpg0420(eda)
            LPF: lpl0463(eda)
            LPP: lpp0487(eda)
            MCA: MCA0038(eda)
            HCH: HCH_00349(eda)
            CSA: Csal_2739
            MMW: Mmwyl1_1039
            AHA: AHA_0289(eda)
            NME: NMB1394
            NMA: NMA1611(eda)
            NGO: NGO0713
            CVI: CV_0143(eda)
            RSO: RSp1190(eda)
            REU: Reut_B4024
            REH: H16_B1213(eda)
            RME: Rmet_4768
            BMA: BMA2445(eda) BMA2488
            BXE: Bxe_A0544
            BVI: Bcep1808_0629
            BUR: Bcep18194_A3701 Bcep18194_A3747
            BCN: Bcen_0178
            BCH: Bcen2424_0661
            BPS: BPSL2931(eda) BPSL2970
            BPM: BURPS1710b_3441 BURPS1710b_3487(eda-2)
            BPL: BURPS1106A_3441(eda)
            BPD: BURPS668_3406(eda)
            BTE: BTH_I1177 BTH_I1218
            RFR: Rfer_0938 Rfer_0950 Rfer_0961 Rfer_2061
            POL: Bpro_3535 Bpro_3550
            PNA: Pnap_2985
            AAV: Aave_2792
            HAR: HEAR1087(eda)
            MMS: mma_2310(eda)
            MFA: Mfla_0760
            HPY: HP1099(eda)
            HPJ: jhp1025(eda)
            HPA: HPAG1_1037
            HAC: Hac_0443(eda)
            CJD: JJD26997_1272
            MLO: mlr2994
            MES: Meso_2733
            SME: SMc00882 SMc02043(eda1) SMc03153(eda2)
            SMD: Smed_2464 Smed_2779
            ATU: Atu0703(kdgA) Atu4494(kdgA)
            ATC: AGR_C_1269 AGR_L_750
            RET: RHE_CH00853(kdgA) RHE_CH03635(eda)
            RLE: RL4162(eda)
            BME: BMEII0009
            BMF: BAB2_0083
            BMB: BruAb2_0084
            OAN: Oant_4257
            BJA: bll7287(dgoA) blr3923(kdgA)
            BRA: BRADO1806(eda)
            BBT: BBta_2126(eda)
            BHE: BH12770(eda)
            XAU: Xaut_1019
            CCR: CC_0784 CC_1495
            SIL: SPO3031(eda-1) SPOA0330(eda-2)
            SIT: TM1040_0375
            RSP: RSP_2645(eda) RSP_3301(eda)
            RSH: Rsph17029_1302
            RSQ: Rsph17025_1180
            JAN: Jann_1954
            RDE: RD1_2868(dgoA) RD1_2878(eda)
            PDE: Pden_1245
            MMR: Mmar10_2671
            HNE: HNE_1187(eda)
            ZMO: ZMO0997(eda)
            NAR: Saro_2568
            SAL: Sala_0192
            ELI: ELI_00530
            GOX: GOX0430
            GBE: GbCGDNIH1_2044
            ACR: Acry_0467
            BSU: BG11396(kdgA)
            BHA: BH3723(kdgA)
            BCZ: pE33L466_0341(kdgA)
            BLI: BL02470(kdgA) BL03850
            BLD: BLi03826(kdgA) BLi04071
            BCL: ABC0523 ABC3136
            BAY: RBAM_017970(kdgA)
            BPU: BPUM_3243(kdgA)
            OIH: OB2214 OB2703
            GKA: GK1956
            SHA: SH2651
            SSP: SSP2183
            LMO: lmo1969
            LLA: L0022(kdgA)
            LLC: LACR_1740
            SPY: SPy_0639(kgdA)
            SPZ: M5005_Spy_0527(kgdA)
            SPM: spyM18_0702(alkH)
            SPG: SpyM3_0451(kgdA)
            SPS: SPs1405
            SPH: MGAS10270_Spy0522(kgdA) MGAS10270_Spy1172
            SPI: MGAS10750_Spy0546(kgdA)
            SPJ: MGAS2096_Spy0539(kgdA)
            SPK: MGAS9429_Spy0518(kgdA)
            SPF: SpyM51336(kgdA)
            SPA: M6_Spy0548
            SPB: M28_Spy0506(kgdA)
            SPN: SP_0317
            SPR: spr0287(kdgA)
            SPD: SPD_0289(eda)
            SAG: SAG0700(eda-1) SAG1907(eda-2)
            SAN: gbs0673 gbs1894
            SAK: SAK_0826(eda)
            LBR: LVIS_0324
            LCA: LSEI_0051
            EFA: EF0423(eda-1) EF2266 EF3134(eda-2)
            CAC: CAC0394(kdgA) CAC2973(kdgA)
            CPE: CPE0150
            CPF: CPF_0397
            CNO: NT01CX_1477
            CDF: CD3626(kdgA)
            CBA: CLB_0336(eda)
            CBH: CLC_0351(eda)
            CBF: CLI_0365(eda)
            CBE: Cbei_2201
            MTA: Moth_0420
            MSM: MSMEG_0312(eda) MSMEG_3788(eda)
            RHA: RHA1_ro02367 RHA1_ro02464 RHA1_ro02786
            SCO: SCO0852(SCM2.05c) SCO2298(kdgA) SCO3473(SCE65.09c)
                 SCO3495(SCE65.31c)
            SMA: SAV5878(kdgA)
            PAC: PPA0371 PPA2133
            TFU: Tfu_0188
            SEN: SACE_1739(kdgA) SACE_2637 SACE_4936 SACE_5973
            TPA: TP0568
            SYN: sll0107(eda)
            SYW: SYNW0306
            SYC: syc1480_d(eda)
            SYF: Synpcc7942_0017
            SYD: Syncc9605_0302
            SYG: sync_0356(eda)
            SYR: SynRCC307_2192(kdgA)
            SYX: SynWH7803_0356(kdgA)
            CYA: CYA_1625(eda)
            CYB: CYB_1899(eda)
            TEL: tlr1928
            GVI: gll4271
            ANA: all4771
            AVA: Ava_2448
            PMA: Pro0254(eda)
            PMM: PMM0225
            PMT: PMT1797
            PMN: PMN2A_1594
            PMI: PMT9312_0227
            PMB: A9601_02461(eda)
            PMC: P9515_02571(eda)
            PMG: P9301_02471(eda)
            PME: NATL1_03051(eda)
            TER: Tery_4949
            BTH: BT_0489
            BFR: BF2699
            BFS: BF2718
            GFO: GFO_1707(eda)
            DGE: Dgeo_2816
            TTH: TT_P0030
            TTJ: TTHB072
            TMA: TM0066
            HMA: rrnAC3121(eda)
            HWA: HQ1495A(eda)
STRUCTURES  PDB: 1EUA  1EUN  1FQ0  1FWR  1KGA  1MXS  1WA3  1WAU  1WBH  2C0A  
                 2NUW  2NUX  2NUY  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.14
            ExPASy - ENZYME nomenclature database: 4.1.2.14
            ExplorEnz - The Enzyme Database: 4.1.2.14
            ERGO genome analysis and discovery system: 4.1.2.14
            BRENDA, the Enzyme Database: 4.1.2.14
            CAS: 9024-53-7
///
ENTRY       EC 4.1.2.15       Obsolete  Enzyme
NAME        Transferred to 2.5.1.54
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
COMMENT     Transferred entry: now EC 2.5.1.54 3-deoxy-7-phosphoheptulonate
            synthase (EC 4.1.2.15 created 1965, modified 1976, deleted 2002)
STRUCTURES  PDB: 1GG1  1HFB  1KFL  1N8F  1OAB  1OF6  1OF8  1OFA  1OFB  1OFO  
                 1OFP  1OFQ  1OFR  1OG0  1QR7  1ZCO  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.15
            ExPASy - ENZYME nomenclature database: 4.1.2.15
            ExplorEnz - The Enzyme Database: 4.1.2.15
            ERGO genome analysis and discovery system: 4.1.2.15
            BRENDA, the Enzyme Database: 4.1.2.15
///
ENTRY       EC 4.1.2.16       Obsolete  Enzyme
NAME        Transferred to 2.5.1.55
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
COMMENT     Transferred entry: now EC 2.5.1.55 3-deoxy-8-phosphooctulonate
            synthase (EC 4.1.2.16 created 1965, deleted 2002)
STRUCTURES  PDB: 1D9E  1FWN  1FWS  1FWT  1FWW  1FX6  1FXP  1FXQ  1FY6  1G7U  
                 1G7V  1GG0  1JCX  1JCY  1LRN  1LRO  1LRQ  1PCK  1PCW  1PE1  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.16
            ExPASy - ENZYME nomenclature database: 4.1.2.16
            ExplorEnz - The Enzyme Database: 4.1.2.16
            ERGO genome analysis and discovery system: 4.1.2.16
            BRENDA, the Enzyme Database: 4.1.2.16
///
ENTRY       EC 4.1.2.17                 Enzyme
NAME        L-fuculose-phosphate aldolase;
            L-fuculose 1-phosphate aldolase;
            fuculose aldolase;
            L-fuculose-1-phosphate lactaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     L-fuculose-1-phosphate (S)-lactaldehyde-lyase
            (glycerone-phosphate-forming)
REACTION    L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
            [RN:R02262]
ALL_REAC    R02262
SUBSTRATE   L-fuculose 1-phosphate [CPD:C01099]
PRODUCT     glycerone phosphate [CPD:C00111];
            (S)-lactaldehyde [CPD:C00424]
REFERENCE   1  [PMID:5330266]
  AUTHORS   Ghalambor MA, Heath EC.
  TITLE     The biosynthesis of cell wall lipopolysaccharide in Escherichia
            coli. IV. Purification and properties of cytidine monophosphate
            3-deoxy-d-manno-octulosonate synthetase.
  JOURNAL   J. Biol. Chem. 241 (1966) 3216-21.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:8515438]
  AUTHORS   Dreyer MK, Schulz GE.
  TITLE     The spatial structure of the class II L-fuculose-1-phosphate
            aldolase from Escherichia coli.
  JOURNAL   J. Mol. Biol. 231 (1993) 549-53.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:8676381]
  AUTHORS   Dreyer MK, Schulz GE.
  TITLE     Catalytic mechanism of the metal-dependent fuculose aldolase from
            Escherichia coli as derived from the structure.
  JOURNAL   J. Mol. Biol. 259 (1996) 458-66.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K01628  L-fuculose-phosphate aldolase
GENES       PIC: PICST_32146(ALD1)
            ECO: b2800(fucA)
            ECJ: JW2771(fucA)
            ECE: Z4117(fucA)
            ECS: ECs3660
            ECC: c3368(fucA)
            ECI: UTI89_C3104(ygbL) UTI89_C3171(fucA)
            ECP: ECP_2783
            ECV: APECO1_3731(fucA) APECO1_3786(ygbL)
            ECW: EcE24377A_3105(fucA)
            ECX: EcHS_A2944(fucA)
            STY: STY3113(fucA)
            STT: t2882(fucA)
            SPT: SPA2838(fucA)
            SEC: SC2913(fucA)
            STM: STM2974(fucA)
            SFL: SF2814(fucA)
            SFX: S3009(fucA)
            SFV: SFV_2879(fucA)
            SSN: SSON_2957(fucA)
            SBO: SBO_2681(fucA)
            SDY: SDY_3017(fucA)
            SGL: SG0183
            HIT: NTHI0866(fucA)
            HIP: CGSHiEE_02040
            HIQ: CGSHiGG_07005
            HSO: HS_0014(fucA) HS_1451(fucA)
            APL: APL_1687(fucA)
            XFA: XF2209
            XFT: PD1258(fucA2)
            XCC: XCC1820
            XCB: XC_2369
            XCV: XCV1886 XCV4349
            XAC: XAC1840 XAC4243(fucA)
            XOO: XOO2139
            XOM: XOO_2008(XOO2008)
            PAE: PA1683
            PSB: Psyr_0464
            PSP: PSPPH_0455(fucA) PSPPH_2737
            PFL: PFL_3344
            PFO: Pfl_1308 Pfl_1724
            PEN: PSEEN2381
            AEH: Mlg_2778
            ABO: ABO_1445
            MMW: Mmwyl1_4174
            REU: Reut_A1425
            RME: Rmet_1837 Rmet_4108
            BMA: BMAA0575
            BXE: Bxe_A4303 Bxe_B2170
            BUR: Bcep18194_B0077 Bcep18194_B0476
            BCH: Bcen2424_5157
            BPM: BURPS1710b_1161 BURPS1710b_A0440
            BTE: BTH_I0804 BTH_II0975
            RFR: Rfer_3750
            POL: Bpro_0283
            VEI: Veis_2019
            EBA: ebA3888(fucA)
            AZO: azo3361(fucA)
            DAR: Daro_3336
            HPA: HPAG1_0112
            HAC: Hac_1471
            PCA: Pcar_3030
            DVU: DVU0158
            DDE: Dde_3569
            MXA: MXAN_6384(fucA)
            SME: SMb20490(fucA2) SMc01621(fucA1)
            SMD: Smed_3633
            RET: RHE_PF00343(ypf00174)
            RLE: pRL110150 pRL120619
            BME: BMEII0189
            BMF: BAB2_1068
            BMS: BRA1110
            BMB: BruAb2_1049
            BJA: bll6170 blr3542
            BRA: BRADO2550 BRADO4793(fucA)
            BBT: BBta_2510 BBta_2896 BBta_3232(fucA)
            RPA: RPA4655(fucA)
            NWI: Nwi_0882
            RSP: RSP_0476 RSP_2364(fucA)
            RSH: Rsph17029_1025 Rsph17029_2128
            RSQ: Rsph17025_2398
            RDE: RD1_3632(fucA) RD1_3784
            GBE: GbCGDNIH1_2157
            ACR: Acry_2573
            RRU: Rru_A0359 Rru_A3143
            BAN: BA0348(fucA)
            BAR: GBAA0348(fucA)
            BAA: BA_0919
            BCE: BC0380
            BCA: BCE_0444(fucA)
            BCL: ABC4076
            OIH: OB3254
            SPN: SP_2166
            SPR: spr1972(fucA)
            SPD: SPD_1994(fucA)
            CPE: CPE0319(fucA)
            CPF: CPF_1051(fucA)
            CTC: CTC00944
            CNO: NT01CX_0230
            CHY: CHY_1439(fucA1) CHY_1555(fucA2)
            DSY: DSY2602
            SWO: Swol_0780
            TTE: TTE1592(araD)
            MTU: Rv0727c(fucA)
            MTC: MT0752
            MBO: Mb0748c(fucA)
            MBB: BCG_0777c(fucA)
            MPA: MAP4193c(fucA)
            SCO: SCO1844(SCI8.29c)
            SMA: SAV6421(fucA2)
            SEN: SACE_5215(fucA)
            FNU: FN1417
            RBA: RB2568 RB681(fucA)
            SYG: sync_2475(fucA)
            SYR: SynRCC307_2010(fucA)
            SYX: SynWH7803_2143(fucA)
            DET: DET1641
            DEH: cbdb_A1741
            TTH: TTC1459
            TTJ: TTHA1811
            AAE: aq_1658(fucA1) aq_1979(fucA2)
            MJA: MJ1418(fucA)
            MMP: MMP1187(fucA)
            MAC: MA0263
            MBA: Mbar_A1249
            MMA: MM_1535
            MST: Msp_1585
            MSI: Msm_1270
            MKA: MK1585
            HAL: VNG1201G(fucA)
            HMA: pNG7027(fucA)
            TVO: TVN1450
            PTO: PTO1347
            PAB: PAB0117(fucA)
            PFU: PF0108
            TKO: TK2132
            RCI: RCIX919
            APE: APE_1657.1
            HBU: Hbut_0791
            PAI: PAE2158(fucA)
STRUCTURES  PDB: 1DZU  1DZV  1DZW  1DZX  1DZY  1DZZ  1E46  1E47  1E48  1E49  
                 1E4A  1E4B  1E4C  1FUA  2FK5  2FLF  2FUA  2OPI  3FUA  4FUA  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.17
            ExPASy - ENZYME nomenclature database: 4.1.2.17
            ExplorEnz - The Enzyme Database: 4.1.2.17
            ERGO genome analysis and discovery system: 4.1.2.17
            BRENDA, the Enzyme Database: 4.1.2.17
            CAS: 9024-54-8
///
ENTRY       EC 4.1.2.18                 Enzyme
NAME        2-dehydro-3-deoxy-L-pentonate aldolase;
            2-keto-3-deoxy-L-pentonate aldolase;
            2-keto-3-deoxy-L-arabonate aldolase;
            2-keto-3-deoxy-D-xylonate aldolase;
            3-deoxy-D-pentulosonic acid aldolase;
            2-dehydro-3-deoxy-L-pentonate glycolaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     2-dehydro-3-deoxy-L-pentonate glycolaldehyde-lyase
            (pyruvate-forming)
REACTION    2-dehydro-3-deoxy-L-pentonate = pyruvate + glycolaldehyde
            [RN:R01784]
ALL_REAC    R01784;
            (other) R03081
SUBSTRATE   2-dehydro-3-deoxy-L-pentonate [CPD:C00684]
PRODUCT     pyruvate [CPD:C00022];
            glycolaldehyde [CPD:C00266]
REFERENCE   1  [PMID:5808295]
  AUTHORS   Dahms AS, Anderson RL.
  TITLE     2-keto-3-deoxyl-L-arabonate aldolase and its role in a new pathway
            of L-arabinose degradation.
  JOURNAL   Biochem. Biophys. Res. Commun. 36 (1969) 809-14.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00051  Fructose and mannose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.18
            ExPASy - ENZYME nomenclature database: 4.1.2.18
            ExplorEnz - The Enzyme Database: 4.1.2.18
            ERGO genome analysis and discovery system: 4.1.2.18
            BRENDA, the Enzyme Database: 4.1.2.18
            CAS: 9076-49-7
///
ENTRY       EC 4.1.2.19                 Enzyme
NAME        rhamnulose-1-phosphate aldolase;
            rhamnulose phosphate aldolase;
            L-rhamnulose 1-phosphate aldolase;
            L-rhamnulose-phosphate aldolase;
            L-rhamnulose-1-phosphate lactaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     L-rhamnulose-1-phosphate (S)-lactaldehyde-lyase
            (glycerone-phosphate-forming)
REACTION    L-rhamnulose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
            [RN:R02263]
ALL_REAC    R02263;
            (other) R01785
SUBSTRATE   L-rhamnulose 1-phosphate [CPD:C01131]
PRODUCT     glycerone phosphate [CPD:C00111];
            (S)-lactaldehyde [CPD:C00424]
REFERENCE   1  [PMID:4975916]
  AUTHORS   Chiu TH, Feingold DS.
  TITLE     L-rhamnulose 1-phosphate aldolase from Escherichia coli.
            Crystallization and properties.
  JOURNAL   Biochemistry. 8 (1969) 98-108.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Sawada, H. and Takagi, Y.
  TITLE     The metabolism of L-rhamnose in Escherichia coli. 3.
            L-Rhamulose-phosphate aldolase.
  JOURNAL   Biochim. Biophys. Acta 92 (1964) 26-32.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K01629  rhamnulose-1-phosphate aldolase
GENES       ECO: b3902(rhaD)
            ECJ: JW3873(rhaD)
            ECE: Z5446(rhaD)
            ECS: ECs4829
            ECC: c4851(rhaD)
            ECI: UTI89_C4485(rhaD)
            ECP: ECP_4112
            ECV: APECO1_2566(rhaD)
            ECW: EcE24377A_4433(rhaD)
            ECX: EcHS_A4130(rhaD)
            STY: STY3828(rhaD)
            STT: t3574(rhaD)
            SPT: SPA3888(rhaD)
            SEC: SC3935(rhaD)
            STM: STM4045(rhaD)
            YPE: YPO0328(rhaD)
            YPK: y0585(rhaD)
            YPM: YP_0483(rhaD)
            YPA: YPA_3954
            YPN: YPN_3342
            YPP: YPDSF_3644
            YPS: YPTB0383(rhaD)
            YPI: YpsIP31758_3757(rhaD)
            SFL: SF3979(rhaD)
            SFX: S3769(rhaD)
            SFV: SFV_3593(rhaD)
            SSN: SSON_4072(rhaD)
            SBO: SBO_3920(rhaD)
            SDY: SDY_3844(rhaD)
            ECA: ECA0438(rhaD)
            SGL: SG2025
            ENT: Ent638_4069
            MSU: MS2327(araD)
            OIH: OB0497
            LMO: lmo2847
            LMF: LMOf2365_2837(rhaD)
            LIN: lin2979
            LWE: lwe0347(rhaD)
            SAK: SAK_0527(rhaD)
            LPL: lp_3592(rhaD)
            LSL: LSL_1755(araD)
            EFA: EF0435(rhaD)
            CBE: Cbei_0454
            MSM: MSMEG_0590(rhaD)
            AAU: AAur_3716(rhaD)
            BTH: BT_3766
            RRS: RoseRS_1581
            RCA: Rcas_2638
            TMA: TM1072
            TPT: Tpet_1672
STRUCTURES  PDB: 1GT7  1OJR  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.19
            ExPASy - ENZYME nomenclature database: 4.1.2.19
            ExplorEnz - The Enzyme Database: 4.1.2.19
            ERGO genome analysis and discovery system: 4.1.2.19
            BRENDA, the Enzyme Database: 4.1.2.19
            CAS: 9054-58-4
///
ENTRY       EC 4.1.2.20                 Enzyme
NAME        2-dehydro-3-deoxyglucarate aldolase;
            2-keto-3-deoxyglucarate aldolase;
            alpha-keto-beta-deoxy-D-glucarate aldolase;
            2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase
            (pyruvate-forming)
REACTION    2-dehydro-3-deoxy-D-glucarate = pyruvate + tartronate semialdehyde
            [RN:R03277]
ALL_REAC    R03277;
            (other) R02754
SUBSTRATE   2-dehydro-3-deoxy-D-glucarate [CPD:C03921]
PRODUCT     pyruvate [CPD:C00022];
            tartronate semialdehyde [CPD:C01146]
REFERENCE   1
  AUTHORS   Fish, D.C. and Blumenthal, H.J.
  TITLE     2-Keto-3-deoxy-D-glucarate aldolase.
  JOURNAL   Methods Enzymol. 9 (1966) 529-534.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K01630  2-dehydro-3-deoxyglucarate aldolase
GENES       ECO: b3126(garL)
            ECJ: JW3095(garL)
            ECE: Z4478(yhaF)
            ECS: ECs4004
            ECC: c3881(yhaF)
            ECP: ECP_3216
            ECV: APECO1_3301(garL)
            ECW: EcE24377A_3604(garL)
            ECX: EcHS_A3315(garL)
            STY: STY3431(garL)
            STT: t3169(garL)
            SPT: SPA3118(garL)
            SEC: SC3196(garL)
            STM: STM3249(garL)
            YPP: YPDSF_1356
            SFV: SFV_3166(yhaF)
            SSN: SSON_3281(yhaF)
            SBO: SBO_2991(yhaF)
            SDY: SDY_3320(yhaF)
            ECA: ECA3574(garL)
            ENT: Ent638_3568
            SPE: Spro_0631
            MSU: MS0691(pykF)
            ASU: Asuc_1651 Asuc_1859
            CSA: Csal_2517
            MMW: Mmwyl1_0497 Mmwyl1_0519 Mmwyl1_3179
            REU: Reut_A1499 Reut_B4276 Reut_C5927
            RME: Rmet_1633
            BMA: BMA0156
            BVI: Bcep1808_3200 Bcep1808_4807
            BUR: Bcep18194_A6467 Bcep18194_B1777
            BCN: Bcen_2502
            BCH: Bcen2424_3116
            BAM: Bamb_3171
            BPS: BPSL0180
            BPM: BURPS1710b_0359(hpcH)
            BTE: BTH_I0140
            BPE: BP2774
            BPA: BPP2555
            BBR: BB2000
            RFR: Rfer_0941 Rfer_1241
            POL: Bpro_0970 Bpro_1475 Bpro_3103 Bpro_3577 Bpro_4781
            PNA: Pnap_1599
            AAV: Aave_2080 Aave_4270
            AJS: Ajs_3719
            VEI: Veis_0796 Veis_1189
            MPT: Mpe_A0189
            NET: Neut_0434
            NMU: Nmul_A0429
            DVU: DVU0343
            DVL: Dvul_2640
            DDE: Dde_3685
            SMD: Smed_3223
            RET: RHE_CH02300(hpaI)
            RSQ: Rsph17025_1540
            JAN: Jann_2166 Jann_4135
            SWI: Swit_3087 Swit_4270 Swit_4314
            SUS: Acid_3980
            AMT: Amet_0505
            DSY: DSY0990
            MJL: Mjls_4065
            RHA: RHA1_ro10284
            ART: Arth_3525
            FAL: FRAAL3410(garL)
            SEN: SACE_0699
            LIL: LA1624
            PMG: P9301_14021
            MBU: Mbur_1595
            HMA: rrnB0257(citE2)
            PCL: Pcal_1422
            TPE: Tpen_1624
STRUCTURES  PDB: 1DXE  1DXF  1W37  1W3I  1W3N  1W3T  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.20
            ExPASy - ENZYME nomenclature database: 4.1.2.20
            ExplorEnz - The Enzyme Database: 4.1.2.20
            ERGO genome analysis and discovery system: 4.1.2.20
            BRENDA, the Enzyme Database: 4.1.2.20
            CAS: 37290-56-5
///
ENTRY       EC 4.1.2.21                 Enzyme
NAME        2-dehydro-3-deoxy-6-phosphogalactonate aldolase;
            6-phospho-2-keto-3-deoxygalactonate aldolase;
            phospho-2-keto-3-deoxygalactonate aldolase;
            2-keto-3-deoxy-6-phosphogalactonic aldolase;
            phospho-2-keto-3-deoxygalactonic aldolase;
            2-keto-3-deoxy-6-phosphogalactonic acid aldolase;
            (KDPGal)aldolase;
            2-dehydro-3-deoxy-D-galactonate-6-phosphate
            D-glyceraldehyde-3-phosphate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     2-dehydro-3-deoxy-D-galactonate-6-phosphate
            D-glyceraldehyde-3-phosphate-lyase (pyruvate-forming)
REACTION    2-dehydro-3-deoxy-D-galactonate 6-phosphate = pyruvate +
            D-glyceraldehyde 3-phosphate [RN:R01064]
ALL_REAC    R01064
SUBSTRATE   2-dehydro-3-deoxy-D-galactonate 6-phosphate [CPD:C01286]
PRODUCT     pyruvate [CPD:C00022];
            D-glyceraldehyde 3-phosphate [CPD:C00118]
REFERENCE   1
  AUTHORS   Shuster, C.W.
  TITLE     2-Keto-3-deoxy-6-phosphogalactonic acid aldolase.
  JOURNAL   Methods Enzymol. 9 (1966) 524-528.
  ORGANISM  Pseudomonas saccharophila
PATHWAY     PATH: map00052  Galactose metabolism
ORTHOLOGY   KO: K01631  2-dehydro-3-deoxyphosphogalactonate aldolase
GENES       ECO: b4477(dgoA)
            ECI: UTI89_C4244
            ECP: ECP_3893
            ECV: APECO1_2764(dgoA)
            SEC: SC3746(dgoA)
            STM: STM3828(dgoA)
            ECA: ECA4416(dgoA1) ECA4417(dgoA2)
            XCC: XCC1747(dgoA)
            XCB: XC_2487
            XCV: XCV1797(dgoA)
            XAC: XAC1766(dgoA)
            XOO: XOO2917(dgoA)
            XOM: XOO_2768(XOO2768)
            RSO: RSc2752(dgoAa)
            BUR: Bcep18194_B2837 Bcep18194_B3056 Bcep18194_C6937
            MLO: mlr4743
            RLE: RL0915(dgoA)
            BME: BMEII0358
            BMF: BAB2_0296
            BMS: BRA0938
            BMB: BruAb2_0295
            BRA: BRADO1754(dgoA)
            BBT: BBta_2069(dgoA)
            RDE: RD1_3939
            MSM: MSMEG_6176
            SEN: SACE_4102
STRUCTURES  PDB: 2V81  2V82  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.21
            ExPASy - ENZYME nomenclature database: 4.1.2.21
            ExplorEnz - The Enzyme Database: 4.1.2.21
            ERGO genome analysis and discovery system: 4.1.2.21
            BRENDA, the Enzyme Database: 4.1.2.21
            CAS: 9030-99-3
///
ENTRY       EC 4.1.2.22                 Enzyme
NAME        fructose-6-phosphate phosphoketolase;
            D-fructose-6-phosphate D-erythrose-4-phosphate-lyase
            (phosphate-acetylating)
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     D-fructose-6-phosphate D-erythrose-4-phosphate-lyase (adding
            phosphate; acetyl-phosphate-forming)
REACTION    D-fructose 6-phosphate + phosphate = acetyl phosphate + D-erythrose
            4-phosphate + H2O [RN:R00761]
ALL_REAC    R00761
SUBSTRATE   D-fructose 6-phosphate [CPD:C00085];
            phosphate [CPD:C00009]
PRODUCT     acetyl phosphate [CPD:C00227];
            D-erythrose 4-phosphate [CPD:C00279];
            H2O [CPD:C00001]
COMMENT     Also acts on D-xylulose 5-phosphate.
REFERENCE   1
  AUTHORS   Schramm, M., Klybas, V. and Racker, E.
  TITLE     Phospholytic cleavage of fructose-6-phosphate by
            fructose-6-phosphate phosphoketolase from Acetobacter xylinum.
  JOURNAL   J. Biol. Chem. 233 (1958) 1283-1288.
  ORGANISM  Acetobacter xylinum
PATHWAY     PATH: map00030  Pentose phosphate pathway
ORTHOLOGY   KO: K01632  fructose-6-phosphate phosphoketolase
GENES       NOC: Noc_2717
            PNA: Pnap_4497
            NET: Neut_2087
            NMU: Nmul_A0993
            MFA: Mfla_0893 Mfla_1037
            RLE: RL3902(xfp)
            BRA: BRADO2015(xfp)
            BBT: BBta_2340(xfp)
            RPB: RPB_3858
            RPC: RPC_3807
            RPD: RPD_1492
            NWI: Nwi_1947
            NHA: Nham_1896 Nham_4367
            SUS: Acid_4925
            LSL: LSL_1509
            MVA: Mvan_3069
            MGI: Mflv_3341
            MMC: Mmcs_2793
            MKM: Mkms_2837
            MJL: Mjls_2820
            ART: Arth_0143
            AAU: AAur_1848(xfp)
            NCA: Noca_3620
            TFU: Tfu_2970
            FRA: Francci3_3546
            ACE: Acel_0521
            SEN: SACE_1921
            BAD: BAD_0687
            SYF: Synpcc7942_2080
            ANA: all1483
            AVA: Ava_0496
            PLT: Plut_1522
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.22
            ExPASy - ENZYME nomenclature database: 4.1.2.22
            ExplorEnz - The Enzyme Database: 4.1.2.22
            ERGO genome analysis and discovery system: 4.1.2.22
            BRENDA, the Enzyme Database: 4.1.2.22
            CAS: 37290-57-6
///
ENTRY       EC 4.1.2.23                 Enzyme
NAME        3-deoxy-D-manno-octulosonate aldolase;
            2-keto-3-deoxyoctonate aldolase;
            KDOaldolase;
            3-deoxyoctulosonic aldolase;
            2-keto-3-deoxyoctonic aldolase;
            3-deoxy-D-manno-octulosonic aldolase;
            3-deoxy-D-manno-octulosonate D-arabinose-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     3-deoxy-D-manno-octulosonate D-arabinose-lyase (pyruvate-forming)
REACTION    3-deoxy-D-manno-octulosonate = pyruvate + D-arabinose [RN:R01576]
ALL_REAC    R01576
SUBSTRATE   3-deoxy-D-manno-octulosonate [CPD:C01187]
PRODUCT     pyruvate [CPD:C00022];
            D-arabinose [CPD:C00216]
REFERENCE   1  [PMID:5912115]
  AUTHORS   Ghalambor MA, Heath EC.
  TITLE     The biosynthesis of cell wall lipopolysaccharide in Escherichia
            coli. V. Purification and properties of 3-deoxy-D-manno-octulosonate
            aldolase.
  JOURNAL   J. Biol. Chem. 241 (1966) 3222-7.
  ORGANISM  Aerobacter cloacae, Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.23
            ExPASy - ENZYME nomenclature database: 4.1.2.23
            ExplorEnz - The Enzyme Database: 4.1.2.23
            ERGO genome analysis and discovery system: 4.1.2.23
            BRENDA, the Enzyme Database: 4.1.2.23
            CAS: 9026-95-3
///
ENTRY       EC 4.1.2.24                 Enzyme
NAME        dimethylaniline-N-oxide aldolase;
            microsomal oxidase II;
            microsomal N-oxide dealkylase;
            N,N-dimethylaniline-N-oxide formaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     N,N-dimethylaniline-N-oxide formaldehyde-lyase
            (N-methylaniline-forming)
REACTION    N,N-dimethylaniline N-oxide = N-methylaniline + formaldehyde
            [RN:R03345]
ALL_REAC    R03345
SUBSTRATE   N,N-dimethylaniline N-oxide [CPD:C01183]
PRODUCT     N-methylaniline [CPD:C02299];
            formaldehyde [CPD:C00067]
COMMENT     Acts on various N,N-dialkylarylamides.
REFERENCE   1  [PMID:5961882]
  AUTHORS   Machinist JM, Orme-Johnson WH, Ziegler DM.
  TITLE     Microsomal oxidases. II. Properties of a pork liver microsomal
            N-oxide dealkylase.
  JOURNAL   Biochemistry. 5 (1966) 2939-43.
  ORGANISM  pig [GN:ssc]
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.24
            ExPASy - ENZYME nomenclature database: 4.1.2.24
            ExplorEnz - The Enzyme Database: 4.1.2.24
            ERGO genome analysis and discovery system: 4.1.2.24
            BRENDA, the Enzyme Database: 4.1.2.24
            CAS: 37290-58-7
///
ENTRY       EC 4.1.2.25                 Enzyme
NAME        dihydroneopterin aldolase;
            2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-
            dihydropteridine glycolaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropt
            eridine glycolaldehyde-lyase
            (2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-forming)
REACTION    2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-
            dihydropteridine =
            2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine +
            glycolaldehyde [RN:R03504]
ALL_REAC    R03504
SUBSTRATE   2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-
            dihydropteridine [CPD:C04874]
PRODUCT     2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine [CPD:C01300];
            glycolaldehyde [CPD:C00266]
REFERENCE   1  [PMID:4912541]
  AUTHORS   Mathis JB, Brown GM.
  TITLE     The biosynthesis of folic acid. XI. Purification and properties of
            dihydroneopterin aldolase.
  JOURNAL   J. Biol. Chem. 245 (1970) 3015-25.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K01633  dihydroneopterin aldolase
GENES       ATH: AT3G11750
            CME: CMF158C
            SCE: YNL256W(FOL1)
            AGO: AGOS_AFR647C
            PIC: PICST_66087
            CGR: CAGL0J07920g
            SPO: SPBC1734.03
            AFM: AFUA_3G10090
            CNE: CNC04040
            DDI: DDB_0230139
            ECO: b3058(folB)
            ECJ: JW3030(folB)
            ECE: Z4411(ygiG)
            ECS: ECs3941
            ECC: c3808(ygiG)
            ECI: UTI89_C3494(ygiG)
            ECP: ECP_3148
            ECV: APECO1_3356(folB)
            ECW: EcE24377A_3521(folB)
            ECX: EcHS_A3236(folB)
            STY: STY3385(folB)
            STT: t3126(folB)
            SPT: SPA3074(folB)
            SEC: SC3153(folB)
            STM: STM3206(folB)
            YPE: YPO0648(folB)
            YPK: y3531
            YPM: YP_2963(folB)
            YPA: YPA_3142
            YPN: YPN_0508
            YPP: YPDSF_0432
            YPS: YPTB3413(folB)
            YPI: YpsIP31758_0558(folB)
            SFL: SF3099(folB)
            SFX: S3304(ygiG)
            SFV: SFV_3098(ygiG)
            SSN: SSON_3195(ygiG)
            SBO: SBO_2914(ygiG)
            SDY: SDY_3241(ygiG)
            ECA: ECA3590(folB)
            PLU: plu3974(folB)
            WBR: WGLp472(ygiG)
            SGL: SG0256
            BFL: Bfl061(folB)
            BPN: BPEN_062(folB)
            HIN: HI0265
            HIT: NTHI0372(folB)
            HDU: HD0978(folB)
            HSO: HS_1298(folB)
            PMU: PM1697(folB)
            MSU: MS1824(folB)
            APL: APL_1342(folB)
            XFA: XF0436
            XFT: PD1642(folB)
            XCC: XCC3815(folB)
            XCB: XC_3887
            XCV: XCV3989(folB)
            XAC: XAC3870(folB)
            XOO: XOO4124(folB)
            XOM: XOO_3900(XOO3900)
            VCH: VC0524
            VVU: VV1_0625
            VVY: VV0568
            VPA: VP0411(folB)
            VFI: VF2247
            PPR: PBPRA0436
            PAE: PA0582(folB)
            PAU: PA14_07590(folB)
            PAP: PSPA7_0725(folB)
            PPU: PP_0392(folB)
            PST: PSPTO_0542(folB-1)
            PSB: Psyr_4636
            PSP: PSPPH_0624(folB1) PSPPH_1070(folB2)
            PFL: PFL_0948(folB) PFL_5658(folB)
            PFO: Pfl_5144
            PEN: PSEEN0419(folB)
            PMY: Pmen_4023
            PAR: Psyc_1182(folB)
            PCR: Pcryo_1208
            ACI: ACIAD2408(folB)
            SON: SO_1291(folB)
            SDN: Sden_2828
            SFR: Sfri_2990
            SHE: Shewmr4_2902
            SHM: Shewmr7_2984
            SHN: Shewana3_3081
            ILO: IL1968(folB)
            CPS: CPS_4340(folB)
            PHA: PSHAa2302(folB)
            PAT: Patl_1044
            SDE: Sde_0723
            PIN: Ping_0172
            CBU: CBU_1968(folB)
            CBD: COXBU7E912_2066(folB)
            LPN: lpg2029
            LPF: lpl2006(folB)
            LPP: lpp2011(folB)
            MCA: MCA2988(folB)
            FTU: FTT0943c(folB)
            FTF: FTF0943c(folB)
            FTW: FTW_0837
            FTL: FTL_1264
            FTH: FTH_1239(folB)
            FTA: FTA_1337(folB)
            FTN: FTN_0820(folB)
            TCX: Tcr_1812
            NOC: Noc_0039
            AEH: Mlg_2522
            HCH: HCH_06268(folB)
            CSA: Csal_0971
            ABO: ABO_2057(folB)
            AHA: AHA_3847(folB)
            DNO: DNO_1076(folB)
            BCI: BCI_0620(folB)
            RMA: Rmag_0957
            VOK: COSY_0857(folB)
            NME: NMB1063
            NMA: NMA1262(folB)
            NMC: NMC1027(folB)
            NGO: NGO0857
            CVI: CV_3689(folB)
            RSO: RSc0157(RS01027) RSc1105(folB2) RSp0050(folB1)
            REU: Reut_A0226 Reut_B4826
            REH: H16_A0259(folB)
            RME: Rmet_0183
            BMA: BMA3382(folB) BMAA0894
            BMV: BMASAVP1_A3055(folB)
            BML: BMA10299_A2038(folB)
            BMN: BMA10247_2246(folB)
            BXE: Bxe_A0205 Bxe_B2438
            BUR: Bcep18194_A6328 Bcep18194_B0490
            BCN: Bcen_2365 Bcen_3220
            BCH: Bcen2424_2979 Bcen2424_5147
            BAM: Bamb_3026
            BPS: BPSL0315 BPSS1365(folB)
            BPM: BURPS1710b_0520(folB) BURPS1710b_A0391
            BPL: BURPS1106A_0341(folB) BURPS1106A_A1858(folB)
            BPD: BURPS668_0328(folB) BURPS668_A1950(folB)
            BTE: BTH_I0291 BTH_II1000
            BPE: BP3274(folB)
            BPA: BPP4147(folB)
            BBR: BB4617(folB)
            RFR: Rfer_0814
            POL: Bpro_4088
            MPT: Mpe_A2613
            MMS: mma_3437(folB)
            NEU: NE0223
            NET: Neut_0294
            NMU: Nmul_A2063
            EBA: ebA4374(folB)
            AZO: azo3222(folB)
            DAR: Daro_0534
            TBD: Tbd_2381
            MFA: Mfla_2328
            HPY: HP1510
            HPJ: jhp1403(folB)
            HPA: HPAG1_1402
            HHE: HH0924
            HAC: Hac_0074(folB)
            WSU: WS0005
            CCV: CCV52592_1694(folB)
            CHA: CHAB381_1503(folB)
            CCO: CCC13826_0981(folB)
            MXA: MXAN_4112
            AMA: AM563(folB)
            APH: APH_0628(folB)
            ERU: Erum4080(folB)
            ERW: ERWE_CDS_04230
            ERG: ERGA_CDS_04170
            ECN: Ecaj_0397
            ECH: ECH_0642(folB)
            PUB: SAR11_0083(folB)
            MLO: mll0787
            MES: Meso_1413
            SME: SMc00463(folB)
            ATU: Atu1353(folB)
            ATC: AGR_C_2498(dhnA)
            RET: RHE_CH02335(folB)
            RLE: RL2649(folB)
            BME: BMEI0955
            BMF: BAB1_1050
            BMS: BR1030(folB)
            BMB: BruAb1_1035(folB)
            BOV: BOV_0996(folB)
            BJA: bll3058
            BRA: BRADO2684(folB)
            BBT: BBta_3025(folB)
            RPA: RPA1839(folB)
            RPB: RPB_3534
            RPC: RPC_1764
            RPD: RPD_1931
            RPE: RPE_1856
            NWI: Nwi_2234
            NHA: Nham_2634
            CCR: CC_0416
            SIL: SPO1362
            SIT: TM1040_2307
            RSP: RSP_1861
            JAN: Jann_2728
            RDE: RD1_1950(folB)
            MMR: Mmar10_0774
            HNE: HNE_2365(folB)
            NAR: Saro_0923
            SAL: Sala_2114
            ELI: ELI_02770
            GBE: GbCGDNIH1_0762
            MAG: amb2297
            MGM: Mmc1_0329
            BSU: BG10141(folA)
            BHA: BH0094(folA)
            BAN: BA0072(folB)
            BAR: GBAA0072(folB)
            BAA: BA_0662(folB)
            BAT: BAS0072
            BCE: BC0080
            BCA: BCE_0071(folB)
            BCZ: BCZK0068(folB)
            BCY: Bcer98_0068
            BTK: BT9727_0068(folB)
            BTL: BALH_0071(folB)
            BLI: BL00862(folB)
            BLD: BLi00094(folB)
            BCL: ABC0114(folA)
            BAY: RBAM_000890(folA)
            BPU: BPUM_0062(folB)
            OIH: OB0086
            GKA: GK0070
            SAU: SA0473(folB)
            SAV: SAV0515(folB)
            SAM: MW0470(folB)
            SAR: SAR0516(folB)
            SAS: SAS0472
            SAC: SACOL0559(folB)
            SAB: SAB0464(folB)
            SAA: SAUSA300_0493(folB)
            SAO: SAOUHSC_00490
            SAJ: SaurJH9_0537
            SAH: SaurJH1_0550
            SEP: SE2268
            SER: SERP0154(folB)
            SHA: SH2495(folB)
            SSP: SSP2241
            LMO: lmo0225(folA)
            LMF: LMOf2365_0237(folB)
            LIN: lin0257(folA)
            LWE: lwe0189(folB)
            LLA: L165490(folB)
            LLC: LACR_1274
            LLM: llmg_1338(folB)
            SPY: SPy_1099(folQ)
            SPZ: M5005_Spy_0823(folQ)
            SPM: spyM18_1061(folQ)
            SPG: SpyM3_0761(folQ)
            SPS: SPs0961
            SPH: MGAS10270_Spy0939(folQ)
            SPI: MGAS10750_Spy0974(folQ)
            SPJ: MGAS2096_Spy0897(folQ)
            SPK: MGAS9429_Spy0942(folQ)
            SPF: SpyM50965(folB)
            SPA: M6_Spy0821
            SPB: M28_Spy0800(folQ)
            SPN: SP_0292
            SPR: spr0269(sulD)
            SPD: SPD_0272(sulD)
            SAG: SAG1114(folB)
            SAN: gbs1181
            SAK: SAK_1199(folB)
            SMU: SMU.970(folA)
            STC: str1541(folQ)
            STL: stu1541(folQ)
            STE: STER_1499
            SSA: SSA_0200(folK)
            SGO: SGO_1912
            LPL: lp_3299(folB)
            LSA: LSA1102(folB)
            LDB: Ldb0246(folB)
            LBU: LBUL_0208
            EFA: EF3269(folB)
            STH: STH3187
            CAC: CAC2927(folA)
            CPE: CPE1022(folA)
            CPF: CPF_1277(folBK)
            CPR: CPR_1099(folBK)
            CNO: NT01CX_0374
            CDF: CD1451(folB)
            CKL: CKL_0960
            CHY: CHY_2382(folB)
            DSY: DSY0208
            DRM: Dred_0155
            SWO: Swol_0098
            MTA: Moth_0407
            MTU: Rv3607c(folB)
            MTC: MT3712.1(folB)
            MBO: Mb3637c(folB)
            MBB: BCG_3671c(folB)
            MLE: ML0225(folB)
            MPA: MAP0451(folX)
            MAV: MAV_0545(folB)
            MSM: MSMEG_6102(folB)
            MMC: Mmcs_4767
            CGL: NCgl2600(cgl2693)
            CGB: cg2981(folX)
            CEF: CE2539
            CDI: DIP1998
            CJK: jk0281(folX)
            NFA: nfa4010
            RHA: RHA1_ro04410
            SCO: SCO3400(folB)
            SMA: SAV4670(folX)
            TWH: TWT586(folPXK)
            TWS: TW175(folP)
            LXX: Lxx21470(folB)
            ART: Arth_0154
            AAU: AAur_0141(folB)
            PAC: PPA0272
            TFU: Tfu_2891
            FRA: Francci3_4406
            FAL: FRAAL6709(folB)
            SEN: SACE_0399(folX)
            BLO: BL1685(sulD)
            RXY: Rxyl_2579
            FNU: FN0072
            CTR: CT614(folX)
            CTA: CTA_0667(folX)
            CMU: TC0904
            CPN: CPn0757(folX)
            CPA: CP1115
            CPJ: CPj0757(folX)
            CPT: CpB0785
            CCA: CCA01000(folB)
            CAB: CAB970(folB)
            CFE: CF0013(folB)
            LIL: LA3959(folK)
            SYN: slr1626(folB)
            SYW: SYNW1485(folB)
            SYC: syc1459_c(folB)
            SYF: Synpcc7942_0040
            SYD: Syncc9605_1027
            SYE: Syncc9902_0928
            SYG: sync_1877(folB)
            SYR: SynRCC307_0927(folB)
            SYX: SynWH7803_0765(folB)
            CYA: CYA_0021(folB)
            CYB: CYB_1408(folB-1) CYB_2921(folB-2)
            TEL: tll0747
            GVI: glr1487
            ANA: alr3512
            AVA: Ava_3225
            PMA: Pro1070(folB)
            PMM: PMM0591(folB)
            PMT: PMT0435(folB)
            PMN: PMN2A_0027
            PMI: PMT9312_0591
            PMB: A9601_06471(folB)
            PMC: P9515_06561(folB)
            PMF: P9303_18461(folB)
            PMG: P9301_06171(folB)
            PME: NATL1_06471(folB)
            TER: Tery_0687
            BTH: BT_2149
            BFR: BF3830
            BFS: BF3622
            PGI: PG2091(folB)
            SRU: SRU_0761(folB)
            CHU: CHU_0761(folQ)
            GFO: GFO_3309(folB)
            FPS: FP2493(folB)
            CTE: CT1937(folB)
            CCH: Cag_0233
            PLT: Plut_0269
            DRA: DR_0169
            DGE: Dgeo_0397
            TTH: TTC1796
            TTJ: TTHA0190
            SAI: Saci_1101
STRUCTURES  PDB: 1NBU  1RRI  1RRW  1RRY  1RS2  1RS4  1RSD  1RSI  1U68  1Z9W  
                 2CG8  2NM2  2NM3  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.25
            ExPASy - ENZYME nomenclature database: 4.1.2.25
            ExplorEnz - The Enzyme Database: 4.1.2.25
            ERGO genome analysis and discovery system: 4.1.2.25
            BRENDA, the Enzyme Database: 4.1.2.25
            CAS: 37290-59-8
///
ENTRY       EC 4.1.2.26                 Enzyme
NAME        phenylserine aldolase;
            L-threo-3-phenylserine benzaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     L-threo-3-phenylserine benzaldehyde-lyase (glycine-forming)
REACTION    L-threo-3-phenylserine = glycine + benzaldehyde [RN:R01766]
ALL_REAC    R01766
SUBSTRATE   L-threo-3-phenylserine [CPD:C03290]
PRODUCT     glycine [CPD:C00037];
            benzaldehyde [CPD:C00261]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:13566053]
  AUTHORS   BRUNS FH, FIEDLER L.
  TITLE     Enzymatic cleavage and synthesis of L-threo-beta-phenylserine and
            L-erythro-beta-Phenyldrine.
  JOURNAL   Nature. 181 (1958) 1533-4.
STRUCTURES  PDB: 1V72  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.26
            ExPASy - ENZYME nomenclature database: 4.1.2.26
            ExplorEnz - The Enzyme Database: 4.1.2.26
            ERGO genome analysis and discovery system: 4.1.2.26
            BRENDA, the Enzyme Database: 4.1.2.26
            CAS: 37290-60-1
///
ENTRY       EC 4.1.2.27                 Enzyme
NAME        sphinganine-1-phosphate aldolase;
            dihydrosphingosine 1-phosphate aldolase;
            sphinganine-1-phosphate alkanal-lyase;
            sphinganine-1-phosphate lyase;
            sphinganine-1-phosphate palmitaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     sphinganine-1-phosphate palmitaldehyde-lyase
            (phosphoethanolamine-forming)
REACTION    sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde
            [RN:R02464]
ALL_REAC    R02464;
            (other) R06516
SUBSTRATE   sphinganine 1-phosphate [CPD:C01120]
PRODUCT     phosphoethanolamine [CPD:C00346];
            palmitaldehyde [CPD:C00517]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:5389296]
  AUTHORS   Stoffel W, LeKim D, Sticht G.
  TITLE     Distribution and properties of dihydrosphingosine-1-phosphate
            aldolase (sphinganine-1-phosphate alkanal-lyase).
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 350 (1969) 1233-41.
  ORGANISM  rat [GN:rno], pig [GN:ssc], cow [GN:bta], Hansenula ciferrii
PATHWAY     PATH: map00600  Sphingolipid metabolism
ORTHOLOGY   KO: K01634  sphinganine-1-phosphate aldolase
GENES       PTR: 466102(SGPL1)
            RNO: 286896(Sgpl1)
            CFA: 489032(SGPL1)
            GGA: 423714(SGPL1)
            SPU: 585643(LOC585643)
            DME: Dmel_CG8946(Sply)
            CEL: Y66H1B.4(spl-1)
            ATH: AT1G27980
            OSA: 4326459
            CME: CMT631C
            SCE: YDR294C(DPL1)
            CAL: CaO19.6951
            CGR: CAGL0H01309g
            ANI: AN1989.2
            AFM: AFUA_4G10470
            AOR: AO090003001164 AO090010000721
            CNE: CNH00560
            DDI: DDB_0214888(sglA)
            TET: TTHERM_00138450 TTHERM_00259410
            TBR: Tb927.6.3630
            TCR: 506941.150 511511.150
            LMA: LmjF30.2350
            EHI: 73.t00006
            LPN: lpg2176
            LPF: lpl2102
            LPP: lpp2128
            BPS: BPSS2021 BPSS2025
            BPM: BURPS1710b_A1139 BURPS1710b_A1143
            BTE: BTH_II0309 BTH_II0311
            STH: STH1274
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.27
            ExPASy - ENZYME nomenclature database: 4.1.2.27
            ExplorEnz - The Enzyme Database: 4.1.2.27
            ERGO genome analysis and discovery system: 4.1.2.27
            BRENDA, the Enzyme Database: 4.1.2.27
            CAS: 39391-27-0
///
ENTRY       EC 4.1.2.28                 Enzyme
NAME        2-dehydro-3-deoxy-D-pentonate aldolase;
            2-keto-3-deoxy-D-pentonate aldolase;
            3-deoxy-D-pentulosonic acid aldolase;
            2-dehydro-3-deoxy-D-pentonate glycolaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     2-dehydro-3-deoxy-D-pentonate glycolaldehyde-lyase
            (pyruvate-forming)
REACTION    2-dehydro-3-deoxy-D-pentonate = pyruvate + glycolaldehyde
            [RN:R01782]
ALL_REAC    R01782
SUBSTRATE   2-dehydro-3-deoxy-D-pentonate [CPD:C03826]
PRODUCT     pyruvate [CPD:C00022];
            glycolaldehyde [CPD:C00266]
REFERENCE   1  [PMID:4423285]
  AUTHORS   Dahms AS.
  TITLE     3-Deoxy-D-pentulosonic acid aldolase and its role in a new pathway
            of D-xylose degradation.
  JOURNAL   Biochem. Biophys. Res. Commun. 60 (1974) 1433-9.
  ORGANISM  Aerobacter aerogenes, Escherichia coli [GN:eco], Salmonella typhosa,
            Pasteurella pestis, Pseudomonas hydrophila, Pseudomonas fragi
REFERENCE   2  [PMID:7154955]
  AUTHORS   Dahms AS, Donald A.
  TITLE     2-Keto-3-deoxy-d-xylonate aldolase (3-deoxy-d-pentulosonic acid
            aldolase).
  JOURNAL   Methods. Enzymol. 90 Pt E (1982) 269-72.
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.28
            ExPASy - ENZYME nomenclature database: 4.1.2.28
            ExplorEnz - The Enzyme Database: 4.1.2.28
            ERGO genome analysis and discovery system: 4.1.2.28
            BRENDA, the Enzyme Database: 4.1.2.28
            CAS: 55326-36-8
///
ENTRY       EC 4.1.2.29                 Enzyme
NAME        5-dehydro-2-deoxyphosphogluconate aldolase;
            phospho-5-keto-2-deoxygluconate aldolase;
            5-dehydro-2-deoxy-D-gluconate-6-phosphate
            malonate-semialdehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     5-dehydro-2-deoxy-D-gluconate-6-phosphate
            malonate-semialdehyde-lyase (glycerone-phosphate-forming)
REACTION    5-dehydro-2-deoxy-D-gluconate 6-phosphate = glycerone phosphate +
            malonate semialdehyde [RN:R01610]
ALL_REAC    R01610
SUBSTRATE   5-dehydro-2-deoxy-D-gluconate 6-phosphate [CPD:C04456]
PRODUCT     glycerone phosphate [CPD:C00111];
            malonate semialdehyde [CPD:C00222]
REFERENCE   1  [PMID:4328832]
  AUTHORS   Anderson WA, Magasanik B.
  TITLE     The pathway of myo-inositol degradation in Aerobacter aerogenes.
            Conversion of 2-deoxy-5-keto-D-gluconic acid to glycolytic
            intermediates.
  JOURNAL   J. Biol. Chem. 246 (1971) 5662-75.
  ORGANISM  Aerobacter aerogenes
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.29
            ExPASy - ENZYME nomenclature database: 4.1.2.29
            ExplorEnz - The Enzyme Database: 4.1.2.29
            ERGO genome analysis and discovery system: 4.1.2.29
            BRENDA, the Enzyme Database: 4.1.2.29
            CAS: 62213-25-6
///
ENTRY       EC 4.1.2.30                 Enzyme
NAME        17alpha-hydroxyprogesterone aldolase;
            C-17/C-20 lyase;
            17alpha-hydroxyprogesterone acetaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     17alpha-hydroxyprogesterone acetaldehyde-lyase
            (4-androstene-3,17-dione-forming)
REACTION    17alpha-hydroxyprogesterone = 4-androstene-3,17-dione + acetaldehyde
            [RN:R01841]
ALL_REAC    R01841;
            (other) R03403
SUBSTRATE   17alpha-hydroxyprogesterone [CPD:C01176]
PRODUCT     4-androstene-3,17-dione [CPD:C00280];
            acetaldehyde [CPD:C00084]
REFERENCE   1  [PMID:4435747]
  AUTHORS   Nowotny E, Sananez RD, Nattero G, Yantorno C, Faillaci MG.
  TITLE     Bioconversion of steroids in vitro by testes from autoimmunized
            rabbits.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 355 (1974) 716-20.
  ORGANISM  rabbit
PATHWAY     PATH: map00150  Androgen and estrogen metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.30
            ExPASy - ENZYME nomenclature database: 4.1.2.30
            ExplorEnz - The Enzyme Database: 4.1.2.30
            ERGO genome analysis and discovery system: 4.1.2.30
            BRENDA, the Enzyme Database: 4.1.2.30
            CAS: 62213-24-5
///
ENTRY       EC 4.1.2.31       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
COMMENT     Deleted entry: 2-oxo-4-hydroxyglutarate aldolase. Now included with
            EC 4.1.3.16 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.2.31 created
            1978, deleted 1982)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.31
            ExPASy - ENZYME nomenclature database: 4.1.2.31
            ExplorEnz - The Enzyme Database: 4.1.2.31
            ERGO genome analysis and discovery system: 4.1.2.31
            BRENDA, the Enzyme Database: 4.1.2.31
///
ENTRY       EC 4.1.2.32                 Enzyme
NAME        trimethylamine-oxide aldolase;
            trimethylamine N-oxide formaldehyde-lyase;
            trimethylamine N-oxide aldolase;
            trimethylamine N-oxide demethylase;
            trimethylamine-N-oxide formaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     trimethylamine-N-oxide formaldehyde-lyase (dimethylamine-forming)
REACTION    trimethylamine N-oxide = dimethylamine + formaldehyde [RN:R02512]
ALL_REAC    R02512
SUBSTRATE   trimethylamine N-oxide [CPD:C01104]
PRODUCT     dimethylamine [CPD:C00543];
            formaldehyde [CPD:C00067]
REFERENCE   1  [PMID:11946146]
  AUTHORS   Large PJ.
  TITLE     Non-oxidative demethylation of trimethylamine N-oxide by Pseudomonas
            aminovorans.
  JOURNAL   FEBS. Lett. 18 (1971) 297-300.
  ORGANISM  Pseudomonas aminovorans
REFERENCE   2  [PMID:5116524]
  AUTHORS   Myers PA, Zatman LJ.
  TITLE     The metabolism of trimethylamine N-oxide by Bacillus PM6.
  JOURNAL   Biochem. J. 121 (1971) 10P.
  ORGANISM  Bacillus sp.
PATHWAY     PATH: map00680  Methane metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.32
            ExPASy - ENZYME nomenclature database: 4.1.2.32
            ExplorEnz - The Enzyme Database: 4.1.2.32
            ERGO genome analysis and discovery system: 4.1.2.32
            UM-BBD (Biocatalysis/Biodegradation Database): 4.1.2.32
            BRENDA, the Enzyme Database: 4.1.2.32
            CAS: 72561-08-1
///
ENTRY       EC 4.1.2.33                 Enzyme
NAME        fucosterol-epoxide lyase;
            (24R,24'R)-fucosterol-epoxide acetaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     (24R,24'R)-fucosterol-epoxide acetaldehyde-lyase
            (desmosterol-forming)
REACTION    (24R,24'R)-fucosterol epoxide = desmosterol + acetaldehyde
            [RN:R03723]
ALL_REAC    R03723
SUBSTRATE   (24R,24'R)-fucosterol epoxide [CPD:C03910]
PRODUCT     desmosterol [CPD:C01802];
            acetaldehyde [CPD:C00084]
COMMENT     The insect enzyme is involved in the conversion of sitosterol into
            cholesterol.
REFERENCE   1  [PMID:3913328]
  AUTHORS   Prestwich GD, Angelastro M, De Palma A, Perino MA.
  TITLE     Fucosterol epoxide lyase of insects: synthesis of labeled substrates
            and development of a partition assay.
  JOURNAL   Anal. Biochem. 151 (1985) 315-26.
  ORGANISM  Manduca sexta
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.33
            ExPASy - ENZYME nomenclature database: 4.1.2.33
            ExplorEnz - The Enzyme Database: 4.1.2.33
            ERGO genome analysis and discovery system: 4.1.2.33
            BRENDA, the Enzyme Database: 4.1.2.33
            CAS: 99676-42-3
///
ENTRY       EC 4.1.2.34                 Enzyme
NAME        4-(2-carboxyphenyl)-2-oxobut-3-enoate aldolase;
            2'-carboxybenzalpyruvate aldolase;
            (3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
            2-carboxybenzaldehyde-lyase;
            (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate 2-formylbenzoate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate 2-formylbenzoate-lyase
            (pyruvate-forming)
REACTION    (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate + H2O = 2-formylbenzoate
            + pyruvate [RN:R07713]
ALL_REAC    R07713;
            (other) R03465
SUBSTRATE   (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate [CPD:C16149];
            H2O [CPD:C00001]
PRODUCT     2-formylbenzoate;
            pyruvate [CPD:C00022]
COMMENT     Involved, with EC 1.13.11.38 (1-hydroxy-2-naphthoate
            1,2-dioxygenase), in the metabolism of phenanthrene in bacteria.
REFERENCE   1  [PMID:6833175]
  AUTHORS   Barnsley EA.
  TITLE     Phthalate pathway of phenanthrene metabolism: formation of
            2'-carboxybenzalpyruvate.
  JOURNAL   J. Bacteriol. 154 (1983) 113-7.
PATHWAY     PATH: map00626  Naphthalene and anthracene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.34
            ExPASy - ENZYME nomenclature database: 4.1.2.34
            ExplorEnz - The Enzyme Database: 4.1.2.34
            ERGO genome analysis and discovery system: 4.1.2.34
            UM-BBD (Biocatalysis/Biodegradation Database): 4.1.2.34
            BRENDA, the Enzyme Database: 4.1.2.34
            CAS: 86611-90-7
///
ENTRY       EC 4.1.2.35                 Enzyme
NAME        propioin synthase;
            4-hydroxy-3-hexanone aldolase;
            4-hydroxy-3-hexanone propanal-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     4-hydroxy-3-hexanone propanal-lyase (propanal-forming)
REACTION    4-hydroxy-3-hexanone = 2 propanal [RN:R00038]
ALL_REAC    R00038
SUBSTRATE   4-hydroxy-3-hexanone [CPD:C02948]
PRODUCT     propanal [CPD:C00479]
REFERENCE   1
  AUTHORS   Morimoto, S., Azuma, K., Oshima, T. and Sakamoto, M.
  TITLE     Purification and properties of a new enzyme, propioin synthase in
            bakers' yeast which forms propioin from propionaldehyde.
  JOURNAL   J. Ferment. Technol. 66 (1988) 7-12.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.35
            ExPASy - ENZYME nomenclature database: 4.1.2.35
            ExplorEnz - The Enzyme Database: 4.1.2.35
            ERGO genome analysis and discovery system: 4.1.2.35
            BRENDA, the Enzyme Database: 4.1.2.35
            CAS: 114189-86-5
///
ENTRY       EC 4.1.2.36                 Enzyme
NAME        lactate aldolase;
            lactate synthase;
            (S)-lactate acetaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     (S)-lactate acetaldehyde-lyase (formate-forming)
REACTION    (S)-lactate = formate + acetaldehyde [RN:R00753]
ALL_REAC    R00753
SUBSTRATE   (S)-lactate [CPD:C00186]
PRODUCT     formate [CPD:C00058];
            acetaldehyde [CPD:C00084]
REFERENCE   1  [PMID:3629727]
  AUTHORS   Gulyi MF, Silonova NV.
  TITLE     [Various metabolic reactions of formate in animal tissues]
  JOURNAL   Ukr. Biokhim. Zh. 59 (1987) 29-35.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00620  Pyruvate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.36
            ExPASy - ENZYME nomenclature database: 4.1.2.36
            ExplorEnz - The Enzyme Database: 4.1.2.36
            ERGO genome analysis and discovery system: 4.1.2.36
            BRENDA, the Enzyme Database: 4.1.2.36
            CAS: 110777-33-8
///
ENTRY       EC 4.1.2.37                 Enzyme
NAME        hydroxynitrilase;
            alpha-hydroxynitrile lyase;
            hydroxynitrile lyase;
            acetone-cyanhydrin lyase [mis-spelt];
            acetone-cyanohydrin acetone-lyase;
            oxynitrilase;
            2-hydroxyisobutyronitrile acetone-lyase;
            2-hydroxyisobutyronitrile acetone-lyase (cyanide-forming);
            acetone-cyanohydrin lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     acetone-cyanohydrin acetone-lyase (cyanide-forming)
REACTION    acetone cyanohydrin = cyanide + acetone [RN:R01553]
ALL_REAC    R01553
SUBSTRATE   acetone cyanohydrin [CPD:C02659]
PRODUCT     cyanide [CPD:C00177];
            acetone [CPD:C00207]
COMMENT     This enzyme accepts aliphatic and aromatic hydroxynitriles, unlike
            EC 4.1.2.11 (hydroxymandelonitrile lyase) which does not act on
            aliphatic hydroxynitriles. 2-Hydroxyisobutyronitrile (acetone
            cyanohydrin) is liberated by glycosidase action on linamarin.
REFERENCE   1  [PMID:3377504]
  AUTHORS   Xu LL, Singh BK, Conn EE.
  TITLE     Purification and characterization of acetone cyanohydrin lyase from
            Linum usitatissimum.
  JOURNAL   Arch. Biochem. Biophys. 263 (1988) 256-63.
  ORGANISM  Linum usitatissimum
REFERENCE   2
  AUTHORS   Selmar, D., Lieberei, R., Biehl, B., Conn, E.E.
  TITLE     alpha-Hydroxynitrile lyase in Hevea brasiliensis and its
            significance for rapid cyanogenesis.
  JOURNAL   Physiol. Plant 75 (1989) 97-101.
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.37
            ExPASy - ENZYME nomenclature database: 4.1.2.37
            ExplorEnz - The Enzyme Database: 4.1.2.37
            ERGO genome analysis and discovery system: 4.1.2.37
            BRENDA, the Enzyme Database: 4.1.2.37
            CAS: 112567-89-2
///
ENTRY       EC 4.1.2.38                 Enzyme
NAME        benzoin aldolase;
            benzaldehyde lyase;
            2-hydroxy-1,2-diphenylethanone benzaldehyde-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     2-hydroxy-1,2-diphenylethanone benzaldehyde-lyase
            (benzaldehyde-forming)
REACTION    2-hydroxy-1,2-diphenylethanone = 2 benzaldehyde [RN:R00027]
ALL_REAC    R00027
SUBSTRATE   2-hydroxy-1,2-diphenylethanone [CPD:C01408]
PRODUCT     benzaldehyde [CPD:C00261]
COFACTOR    Thiamin diphosphate [CPD:C00068]
COMMENT     A thiamine-diphosphate protein.
REFERENCE   1  [PMID:2496105]
  AUTHORS   Gonzalez B, Vicuna R.
  TITLE     Benzaldehyde lyase, a novel thiamine PPi-requiring enzyme, from
            Pseudomonas fluorescens biovar I.
  JOURNAL   J. Bacteriol. 171 (1989) 2401-5.
  ORGANISM  Pseudomonas fluorescens
STRUCTURES  PDB: 2AG0  2AG1  2UZ1  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.38
            ExPASy - ENZYME nomenclature database: 4.1.2.38
            ExplorEnz - The Enzyme Database: 4.1.2.38
            ERGO genome analysis and discovery system: 4.1.2.38
            BRENDA, the Enzyme Database: 4.1.2.38
            CAS: 122097-01-2
///
ENTRY       EC 4.1.2.39       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
COMMENT     Deleted entry: hydroxynitrilase. The enzyme is identical to EC
            4.1.2.37, hydroxynitrilase. (EC 4.1.2.39 created 1999, deleted 2007)
STRUCTURES  PDB: 1SC9  1SCI  1SCK  1SCQ  1YAS  1YB6  1YB7  2G4L  2YAS  3YAS  
                 4YAS  5YAS  6YAS  7YAS  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.39
            ExPASy - ENZYME nomenclature database: 4.1.2.39
            ExplorEnz - The Enzyme Database: 4.1.2.39
            ERGO genome analysis and discovery system: 4.1.2.39
            BRENDA, the Enzyme Database: 4.1.2.39
///
ENTRY       EC 4.1.2.40                 Enzyme
NAME        tagatose-bisphosphate aldolase;
            D-tagatose-1,6-bisphosphate triosephosphate lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     D-tagatose 1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase
            (glycerone-phosphate-forming)
REACTION    D-tagatose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde
            3-phosphate [RN:R01069]
ALL_REAC    R01069
SUBSTRATE   D-tagatose 1,6-bisphosphate [CPD:C03785]
PRODUCT     glycerone phosphate [CPD:C00111];
            D-glyceraldehyde 3-phosphate [CPD:C00118]
COMMENT     Enzyme activity is stimulated by certain divalent cations. It is
            involved in the tagatose 6-phosphate pathway of lactose catabolism
            in bacteria.
REFERENCE   1
  AUTHORS   Anderson, R.L., Markwell, J.P.
  TITLE     D-Tagatose-1,6-bisphosphate aldolase (Class II) from Klebsiella
            pneumoniae.
  JOURNAL   Methods Enzymol. 90 (1982) 323-324.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   2  [PMID:1901863]
  AUTHORS   van Rooijen RJ, van Schalkwijk S, de Vos WM.
  TITLE     Molecular cloning, characterization, and nucleotide sequence of the
            tagatose 6-phosphate pathway gene cluster of the lactose operon of
            Lactococcus lactis.
  JOURNAL   J. Biol. Chem. 266 (1991) 7176-81.
  ORGANISM  Lactococcus lactis
PATHWAY     PATH: map00052  Galactose metabolism
ORTHOLOGY   KO: K01635  tagatose 1,6-diphosphate aldolase
            KO: K08302  tagatose 1,6-diphosphate aldolase
GENES       AOR: AO090010000514
            ECO: b2096(gatY) b3137(agaY)
            ECJ: JW3106(kbaY) JW5343(gatY)
            ECE: Z3259(gatY) Z4491(agaY)
            ECS: ECs2899 ECs4017
            ECC: c2621(gatY) c3894(agaY) c4018
            ECI: UTI89_C2369(gatY) UTI89_C3568(agaY) UTI89_C3695
            ECP: ECP_2134 ECP_3347
            ECV: APECO1_3184 APECO1_3290(kbaY) APECO1_4449(gatY)
            ECW: EcE24377A_2383
            STY: STY3435(gatY)
            STT: t3173(gatY)
            SPT: SPA3122(gatY)
            SEC: SC3197(gatY)
            STM: STM3253
            YPE: YPO0844(agaY)
            YPK: y3229(agaY)
            YPM: YP_3540(agaY)
            YPA: YPA_0426
            YPS: YPTB3088(agaY)
            YPI: YpsIP31758_0942(agaZ)
            SFL: SF2158(gatY)
            SFX: S2284(gatY)
            SFV: SFV_2151(gatY)
            SSN: SSON_2144(gatY)
            SBO: SBO_0917(gatY) SBO_3248
            SDY: SDY_2269(gatY)
            PLU: plu0839(gatY)
            HSO: HS_1146(lacD)
            VVU: VV2_1017
            VVY: VVA1509
            VFI: VFA0989
            PPR: PBPRB0157 PBPRB1043
            VEI: Veis_0798 Veis_2597
            MLO: mlr3411
            BJA: bll6350
            RSP: RSP_4030(yihT)
            ABA: Acid345_1612
            SUS: Acid_1436
            BCA: BCE_1906(gatY)
            BCZ: BCZK1641(lacD)
            BLI: BL01900
            BLD: BLi03552
            SAU: SA1994(lacD)
            SAV: SAV2192(lacD)
            SAM: MW2118(lacD)
            SAR: SAR2283(lacD)
            SAS: SAS2093
            SAC: SACOL2183(lacD)
            SAB: SAB2073c(lacD)
            SAA: SAUSA300_2152(lacD)
            SAO: SAOUHSC_02452
            SAJ: SaurJH9_2223
            SAH: SaurJH1_2262
            SEP: SE1784
            SER: SERP1792(lacD)
            SHA: SH0845(lacD)
            LMO: lmo0539
            LMF: LMOf2365_0568
            LIN: lin0543
            LWE: lwe0500(lacD) lwe0801(lacD)
            LLC: LACR_D03
            SPY: SPy_1704(lacD.1) SPy_1919(lacD.2)
            SPZ: M5005_Spy_1395(lacD.1) M5005_Spy_1635(lacD.2)
            SPM: spyM18_1714 spyM18_1987
            SPG: SpyM3_1482(lacD.1) SpyM3_1656(lacD.2)
            SPS: SPs0385 SPs1654
            SPH: MGAS10270_Spy1516(lacD1) MGAS10270_Spy1704(lacD2)
            SPI: MGAS10750_Spy1508(lacD1) MGAS10750_Spy1732(lacD2)
            SPJ: MGAS2096_Spy1420(lacD1) MGAS2096_Spy1660(lacD2)
            SPK: MGAS9429_Spy1397(lacD1) MGAS9429_Spy1638(lacD2)
            SPF: SpyM50395(lacD1) SpyM51610(lacD2)
            SPA: M6_Spy1444 M6_Spy1644
            SPB: M28_Spy1438(lacD.1) M28_Spy1625(lacD.2)
            SPN: SP_1190
            SPR: spr1073(lacD)
            SPD: SPD_1050(lacD)
            SAG: SAG1928(lacD)
            SAN: gbs1333 gbs1915
            SAK: SAK_1887(lacD)
            SMU: SMU.116(lacD2) SMU.1493(lacD)
            SSA: SSA_0061 SSA_1696(lacD)
            SSU: SSU05_1258
            SSV: SSU98_1273
            SGO: SGO_1516(lacD-2) SGO_1523(lacD-1)
            LJO: LJ0142
            LCA: LSEI_0678 LSEI_2597
            LGA: LGAS_0145
            PPE: PEPE_0143
            EFA: EF0696(lacD-1) EF1807(lacD-2)
            CAC: CAC2952(gatY)
            CPE: CPE2626(gatY)
            CPF: CPF_2962
            MTA: Moth_0609
            MSM: MSMEG_0898
            GVI: glr2533
            PMB: A9601_08441(cbbA)
            PMC: P9515_08011(cbbA)
            PMG: P9301_08421(cbbA)
            SRU: SRU_2019(lacD)
            DET: DET1345
            DEH: cbdb_A1295
            DEB: DehaBAV1_1156
            RRS: RoseRS_1830
            RCA: Rcas_2514
STRUCTURES  PDB: 1GVF  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.40
            ExPASy - ENZYME nomenclature database: 4.1.2.40
            ExplorEnz - The Enzyme Database: 4.1.2.40
            ERGO genome analysis and discovery system: 4.1.2.40
            BRENDA, the Enzyme Database: 4.1.2.40
            CAS: 39433-95-9
///
ENTRY       EC 4.1.2.41                 Enzyme
NAME        vanillin synthase;
            3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA:vanillin lyase
            (acetyl-CoA-forming)
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
SYSNAME     3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA vanillin-lyase
            (acetyl-CoA-forming)
REACTION    3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA = vanillin +
            acetyl-CoA [RN:R05773]
ALL_REAC    R05773
SUBSTRATE   3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA
PRODUCT     vanillin [CPD:C00755];
            acetyl-CoA [CPD:C00024]
COMMENT     Involved, together with EC 4.2.1.101 trans-feruloyl-CoA hydratase,
            in the production of vanillin from trans-ferulic acid. Vanillin is
            converted to vanillate by EC 1.2.1.67 vanillin dehydrogenase.
REFERENCE   1  [PMID:9611814]
  AUTHORS   Narbad A, Gasson MJ.
  TITLE     Metabolism of ferulic acid via vanillin using a novel CoA-dependent
            pathway in a newly-isolated strain of Pseudomonas fluorescens.
  JOURNAL   Microbiology. 144 ( Pt 5) (1998) 1397-405.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   2  [PMID:6870241]
  AUTHORS   Pometto AL 3rd, Crawford DL.
  TITLE     Whole-cell bioconversion of vanillin to vanillic acid by
            Streptomyces viridosporus.
  JOURNAL   Appl. Environ. Microbiol. 45 (1983) 1582-5.
  ORGANISM  Streptomyces viridosporus
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.2.41
            ExPASy - ENZYME nomenclature database: 4.1.2.41
            ExplorEnz - The Enzyme Database: 4.1.2.41
            ERGO genome analysis and discovery system: 4.1.2.41
            BRENDA, the Enzyme Database: 4.1.2.41
            CAS: 449168-60-9
///
ENTRY       EC 4.1.2.-                  Enzyme
CLASS       Lyases;
            Carbon-carbon lyases;
            Aldehyde-lyases
REACTION    (1) Acetaldehyde + Pyruvate <=> 4-Hydroxy-2-oxopentanoate
            [RN:R00750];
            (2) 4-Hydroxy-2-oxo-heptanedioate <=> Succinate semialdehyde +
            Pyruvate [RN:R01645];
            (3) Succinate semialdehyde + Pyruvate <=>
            2,4-Dihydroxyhept-2-enedioate [RN:R01647];
            (4) 2-Dehydro-3-deoxy-L-rhamnonate <=> (S)-Lactaldehyde + Pyruvate
            [RN:R02261];
            (5) 4-Trimethylammoniobutanal + Glycine <=>
            3-Hydroxy-N6,N6,N6-trimethyl-L-lysine [RN:R03284];
            (6) Hexadecenal + Ethanolamine phosphate <=> Sphingosine 1-phosphate
            [RN:R05104];
            (7) D-Ribulose 5-phosphate + Formaldehyde <=> D-arabino-3-Hexulose
            6-phosphate [RN:R05338];
            (8) cis-4-(1'-Hydroxynaphth-2'-yl)-2-oxobut-3-enoate + H2O <=>
            1-Hydroxy-2-naphthaldehyde + Pyruvate [RN:R05648]
SUBSTRATE   Acetaldehyde [CPD:C00084];
            Pyruvate [CPD:C00022];
            4-Hydroxy-2-oxo-heptanedioate [CPD:C05601];
            Succinate semialdehyde [CPD:C00232];
            2-Dehydro-3-deoxy-L-rhamnonate [CPD:C03979];
            4-Trimethylammoniobutanal [CPD:C01149];
            Glycine [CPD:C00037];
            Hexadecenal [CPD:C06123];
            Ethanolamine phosphate [CPD:C00346];
            D-Ribulose 5-phosphate [CPD:C00199];
            Formaldehyde [CPD:C00067];
            cis-4-(1'-Hydroxynaphth-2'-yl)-2-oxobut-3-enoate [CPD:C11426];
            H2O [CPD:C00001]
PRODUCT     4-Hydroxy-2-oxopentanoate [CPD:C03589];
            Succinate semialdehyde [CPD:C00232];
            Pyruvate [CPD:C00022];
            2,4-Dihydroxyhept-2-enedioate [CPD:C06201];
            (S)-Lactaldehyde [CPD:C00424];
            3-Hydroxy-N6,N6,N6-trimethyl-L-lysine [CPD:C01259];
            Sphingosine 1-phosphate [CPD:C06124];
            D-arabino-3-Hexulose 6-phosphate [CPD:C06019];
            1-Hydroxy-2-naphthaldehyde [CPD:C11427]
///
ENTRY       EC 4.1.3.1                  Enzyme
NAME        isocitrate lyase;
            isocitrase;
            isocitritase;
            isocitratase;
            threo-Ds-isocitrate glyoxylate-lyase;
            isocitrate glyoxylate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     isocitrate glyoxylate-lyase (succinate-forming)
REACTION    isocitrate = succinate + glyoxylate [RN:R00479]
ALL_REAC    R00479
SUBSTRATE   isocitrate [CPD:C00311]
PRODUCT     succinate [CPD:C00042];
            glyoxylate [CPD:C00048]
COMMENT     The isomer of isocitrate involved is
            (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate [3].
REFERENCE   1
  AUTHORS   McFadden, B.A. and Howes, W.V.
  TITLE     Crystallisation and some properties of isocitrate lyase from
            Pseudomonas indigofera.
  JOURNAL   J. Biol. Chem. 238 (1963) 1737-1742.
  ORGANISM  Pseudomonas indigofera
REFERENCE   2
  AUTHORS   Shiio, I., Shiio, T. and McFadden, B.A.
  TITLE     Isocitrate lyase from Pseudomonas indigofera. I. Preparation, amino
            acid composition and molecular weight.
  JOURNAL   Biochim. Biophys. Acta 96 (1965) 114-122.
  ORGANISM  Pseudomonas indigofera
REFERENCE   3  [PMID:13925783]
  AUTHORS   VICKERY HB.
  TITLE     A suggested new nomenclature for the isomers of isocitric acid.
  JOURNAL   J. Biol. Chem. 237 (1962) 1739-41.
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K01637  isocitrate lyase
GENES       ATH: AT3G21720
            OSA: 4343441
            SCE: YER065C(ICL1) YPR006C(ICL2)
            AGO: AGOS_ADL066C AGOS_AGL057W
            PIC: PICST_62080(ICL1)
            CGR: CAGL0J03058g CAGL0L09273g
            SPO: SPBC1683.11c
            ANI: AN5634.2 AN8755.2
            AFM: AFUA_4G13510 AFUA_6G02860
            AOR: AO090009000219 AO090120000179
            CNE: CNH03280
            UMA: UM01892.1
            DDI: DDB_0230179
            TET: TTHERM_01141570
            ECO: b4015(aceA)
            ECJ: JW3975(aceA)
            ECE: Z5601(aceA)
            ECS: ECs4933
            ECC: c4972(aceA)
            ECI: UTI89_C4574(aceA)
            ECP: ECP_4225
            ECV: APECO1_2461(aceA)
            ECW: EcE24377A_4557(aceA)
            ECX: EcHS_A4249
            STY: STY4402(aceA)
            STT: t4112(aceA)
            SPT: SPA4022(aceA)
            SEC: SC4063(aceA)
            STM: STM4184(aceA)
            YPE: YPO3725(aceA)
            YPK: y0016(aceA)
            YPM: YP_3087(aceA)
            YPA: YPA_0018
            YPN: YPN_0015
            YPS: YPTB3656(aceA)
            YPI: YpsIP31758_0295(aceA)
            SFL: SF4081(aceA)
            SFX: S3649(aceA)
            SFV: SFV_4086(aceA)
            SSN: SSON_4187(aceA)
            SDY: SDY_4328(aceA)
            ECA: ECA3990(aceA)
            PLU: plu4395(aceA)
            XCC: XCC0238(aceA)
            XCB: XC_0248
            XCV: XCV0265(aceA)
            XAC: XAC0257(aceA)
            VCH: VC0736
            VCO: VC0395_A0267(aceA)
            VVU: VV1_0449
            VVY: VV0742
            VPA: VP0584
            VFI: VF1972
            PPR: PBPRA0738
            PAE: PA2634
            PAU: PA14_30050(aceA)
            PPU: PP_4116(aceA)
            PST: PSPTO_3364(aceA)
            PSB: Psyr_3196
            PSP: PSPPH_3108(aceA)
            PFL: PFL_3897(aceA)
            PFO: Pfl_3602
            PEN: PSEEN3481(aceA)
            PAR: Psyc_1627(aceA)
            PCR: Pcryo_1860
            ACI: ACIAD1084(aceA)
            SON: SO_1484(aceA)
            SDN: Sden_1246
            SFR: Sfri_1102 Sfri_3139
            SAZ: Sama_2380
            SBL: Sbal_1317
            SLO: Shew_1276
            SHE: Shewmr4_2766
            SHM: Shewmr7_2844
            SHN: Shewana3_2942
            SHW: Sputw3181_2865
            ILO: IL0608(aceA)
            CPS: CPS_1232(icl)
            PHA: PSHAb0062(aceA)
            PAT: Patl_1215
            AEH: Mlg_2682
            HCH: HCH_02323(aceA)
            CSA: Csal_2449
            ABO: ABO_2741(aceA)
            AHA: AHA_2817(aceA)
            CVI: CV_1641(aceA)
            RSO: RSc1358(aceA)
            REU: Reut_A0384 Reut_A1961
            REH: H16_A2211(iclA) H16_A2227(iclB)
            RME: Rmet_1385 Rmet_4737
            BMA: BMA1586(aceA)
            BMV: BMASAVP1_A2088(aceA)
            BML: BMA10299_A3224(aceA)
            BMN: BMA10247_1361(aceA)
            BXE: Bxe_A1651
            BUR: Bcep18194_A5357 Bcep18194_B0610
            BCN: Bcen_3921 Bcen_6029
            BCH: Bcen2424_2048 Bcen2424_4447
            BAM: Bamb_2080
            BPS: BPSL2188(aceA)
            BPM: BURPS1710b_2613(aceA)
            BPL: BURPS1106A_2524(aceA)
            BPD: BURPS668_2470(aceA)
            BTE: BTH_I1998(aceA)
            BPE: BP2085(aceA)
            BPA: BPP1769(aceA)
            BBR: BB3339(aceA)
            RFR: Rfer_1335
            POL: Bpro_2101
            AAV: Aave_2860
            MPT: Mpe_A1889
            HAR: HEAR1689(aceA)
            MMS: mma_1943
            EBA: ebA4473(aceA)
            AZO: azo1117(aceA)
            DAR: Daro_3098
            ADE: Adeh_2998
            MXA: MXAN_6442(aceA)
            PUB: SAR11_1240(aceA)
            MLO: mll6527
            MES: Meso_0311
            SME: SMc00768(aceA)
            ATU: Atu0607(aceA)
            ATC: AGR_C_1079
            RET: RHE_CH00712(aceA)
            RLE: RL0761
            BME: BMEI0409
            BMF: BAB1_1631
            BMS: BR1614(aceA)
            BMB: BruAb1_1601(aceA)
            BOV: BOV_1558(aceA)
            BJA: blr2455
            BRA: BRADO3748(aceA)
            BBT: BBta_4188(aceA)
            RPA: RPA4394(aceA)
            RPB: RPB_4199
            RPC: RPC_1379
            RPD: RPD_4053
            RPE: RPE_1395
            NWI: Nwi_2985
            NHA: Nham_1097
            CCR: CC_1764
            MMR: Mmar10_1625
            HNE: HNE_1239(aceA)
            GBE: GbCGDNIH1_0486
            ABA: Acid345_4706
            BHA: BH2677
            BAN: BA1132(aceA)
            BAR: GBAA1132(aceA)
            BAT: BAS1052
            BCE: BC1128
            BCA: BCE_1229(aceA)
            BCZ: BCZK1030(aceA)
            BTK: BT9727_1027(aceA)
            BLI: BL02646
            BLD: BLi04207
            BCL: ABC2973
            OIH: OB2404
            GKA: GK0676
            STH: STH590
            MTU: Rv0467(icl) Rv1915(aceAa) Rv1916(aceAb)
            MTC: MT0483(aceA-1) MT1966(aceA-2)
            MBO: Mb0476(icl) Mb1950(aceA)
            MBB: BCG_0507(icl) BCG_1954(aceA)
            MLE: ML1985(aceA)
            MPA: MAP1643(aceAb) MAP3961(aceA)
            MAV: MAV_2781(aceA) MAV_4682(aceA)
            MSM: MSMEG_0911(aceA) MSMEG_3706(aceA)
            MMC: Mmcs_0187 Mmcs_0636
            CGL: NCgl0096(cgl0097) NCgl2248(cgl2331)
            CGB: cg2560(aceA)
            CEF: CE2232(aceA)
            CJK: jk1933(aceA)
            NFA: nfa52300(aceA)
            RHA: RHA1_ro02122
            SCO: SCO0982(aceA)
            SMA: SAV2043(aceA)
            AAU: AAur_0722(aceA)
            TFU: Tfu_1377
            FAL: FRAAL2355(aceA)
            SEN: SACE_1449(aceA)
            RXY: Rxyl_2063
            DRA: DR_0828
            DGE: Dgeo_1287
            TTH: TTC1485
            TTJ: TTHA1836
            HWA: HQ3094A(aceA)
            SSO: SSO1333(aceA)
            SAI: Saci_2191(aceA)
            PAI: PAE1872
STRUCTURES  PDB: 1DQU  1F61  1F8I  1F8M  1IGW  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.1
            ExPASy - ENZYME nomenclature database: 4.1.3.1
            ExplorEnz - The Enzyme Database: 4.1.3.1
            ERGO genome analysis and discovery system: 4.1.3.1
            BRENDA, the Enzyme Database: 4.1.3.1
            CAS: 9045-78-7
///
ENTRY       EC 4.1.3.2        Obsolete  Enzyme
NAME        Transferred to 2.3.3.9
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.3.3.9 malate synthase (EC 4.1.3.2
            created 1961, deleted 2002)
STRUCTURES  PDB: 1D8C  1N8I  1N8W  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.2
            ExPASy - ENZYME nomenclature database: 4.1.3.2
            ExplorEnz - The Enzyme Database: 4.1.3.2
            ERGO genome analysis and discovery system: 4.1.3.2
            BRENDA, the Enzyme Database: 4.1.3.2
///
ENTRY       EC 4.1.3.3                  Enzyme
NAME        N-acetylneuraminate lyase;
            N-acetylneuraminic acid aldolase;
            acetylneuraminate lyase;
            sialic aldolase;
            sialic acid aldolase;
            sialate lyase;
            N-acetylneuraminic aldolase;
            neuraminic aldolase;
            N-acetylneuraminate aldolase;
            neuraminic acid aldolase;
            N-acetylneuraminic acid aldolase;
            neuraminate aldolase;
            N-acetylneuraminic lyase;
            N-acetylneuraminic acid lyase;
            NPL;
            NALase;
            NANA lyase;
            acetylneuraminate pyruvate-lyase;
            N-acetylneuraminate pyruvate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     N-acetylneuraminate pyruvate-lyase (N-acetyl-D-mannosamine-forming)
REACTION    N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate [RN:R01811]
ALL_REAC    R01811
SUBSTRATE   N-acetylneuraminate [CPD:C00270]
PRODUCT     N-acetyl-D-mannosamine [CPD:C00645];
            pyruvate [CPD:C00022]
COMMENT     Also acts on N-glycoloylneuraminate, and on O-acetylated sialic
            acids, other than 4-O-acetylated derivatives.
REFERENCE   1  [PMID:13811398]
  AUTHORS   COMB DG, ROSEMAN S.
  TITLE     The sialic acids. I. The structure and enzymatic synthesis of
            N-acetylneuraminic acid.
  JOURNAL   J. Biol. Chem. 235 (1960) 2529-37.
  ORGANISM  Clostridium perfringens, Escherichia coli [GN:eco], cow [GN:bta],
            horse, sheep, pig [GN:ssc]
REFERENCE   2  [PMID:6762816]
  AUTHORS   Schauer R.
  TITLE     Chemistry, metabolism, and biological functions of sialic acids.
  JOURNAL   Adv. Carbohydr. Chem. Biochem. 40 (1982) 131-234.
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K01639  N-acetylneuraminate lyase
GENES       DRE: 322207(npl)
            ECO: b3225(nanA)
            ECJ: JW3194(nanA)
            ECE: Z4583(nanA)
            ECS: ECs4098
            ECC: c3639 c3979(nanA)
            ECI: UTI89_C3655(nanA)
            ECP: ECP_3308
            ECV: APECO1_3218(nanA)
            ECW: EcE24377A_3707(nanA)
            ECX: EcHS_A3413
            STY: STY3520(nanA)
            STT: t3256(nanA)
            SPT: SPA3207(nanA)
            SEC: SC3277(nanA)
            STM: STM3339(nanA)
            YPE: YPO3024(nanA)
            YPK: y1458
            YPM: YP_2647(dapA1)
            YPA: YPA_2212
            YPN: YPN_1361
            YPS: YPTB2742(nanA)
            SFL: SF3261(nanA)
            SFX: S3478(nanA)
            SFV: SFV_3250(nanA)
            SSN: SSON_3366(nanA)
            SBO: SBO_3164(nanA)
            SDY: SDY_3400(nanA)
            HIT: NTHI0228(nanA)
            HIP: CGSHiEE_02575
            HDU: HD1850(nanA)
            HSO: HS_0695(nanA)
            PMU: PM1715(nanA)
            APL: APL_1754(nanA)
            VCH: VC1776
            VCO: VC0395_A1374
            VVU: VV2_0730
            VVY: VVA1199
            VFI: VF0663
            PPR: PBPRA2287(nanA)
            PHA: PSHAb0156(nanA)
            SME: SMb20299(nanA)
            SAU: SA0304(nanA)
            SAV: SAV0315(nanA)
            SAM: MW0292(nanA)
            SAR: SAR0312
            SAS: SAS0292
            SAC: SACOL0312(nanA)
            SAB: SAB0252c
            SAA: SAUSA300_0315(nanA)
            SAO: SAOUHSC_00295
            SAJ: SaurJH9_0298
            SAH: SaurJH1_0305
            SHA: SH0282(nanA)
            SSP: SSP0375
            SPY: SPy_0257(nanH)
            SPZ: M5005_Spy_0217(nanH)
            SPM: spyM18_0240
            SPG: SpyM3_0185(nanH)
            SPS: SPs0190
            SPH: MGAS10270_Spy0217(nanH)
            SPI: MGAS10750_Spy0212(nanH)
            SPJ: MGAS2096_Spy0235(nanH)
            SPK: MGAS9429_Spy0218(nanH)
            SPF: SpyM50196(nanH)
            SPA: M6_Spy0249
            SPB: M28_Spy0211(nanH)
            SPN: SP_1329 SP_1676
            SPR: spr1186 spr1520
            SPD: SPD_1163
            SAG: SAG0039
            SAN: gbs0038
            SAK: SAK_0072
            SSA: SSA_0078
            SGO: SGO_0124
            LPL: lp_3568(nanA)
            LSA: LSA1640(nanA)
            LSL: LSL_1938(nanA)
            CPE: CPE0185(nanA)
            CPF: CPF_0178(nanA)
            CPR: CPR_0175(nanA)
            CDF: CD2240(nanA)
            MMY: MSC_0559(nal)
            MSY: MS53_0198(nanA)
            MCP: MCAP_0415(nanA)
            CGB: cg2931(nanA)
            RHA: RHA1_ro05285
            FNU: FN1475
            RBA: RB3352(nanA)
            BFR: BF1706 BF3940
            BFS: BF1712
STRUCTURES  PDB: 1F5Z  1F6K  1F6P  1F73  1F74  1F7B  1FDY  1FDZ  1HL2  1NAL  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.3
            ExPASy - ENZYME nomenclature database: 4.1.3.3
            ExplorEnz - The Enzyme Database: 4.1.3.3
            ERGO genome analysis and discovery system: 4.1.3.3
            BRENDA, the Enzyme Database: 4.1.3.3
            CAS: 9027-60-5
///
ENTRY       EC 4.1.3.4                  Enzyme
NAME        hydroxymethylglutaryl-CoA lyase;
            hydroxymethylglutaryl coenzyme A-cleaving enzyme;
            hydroxymethylglutaryl coenzyme A lyase;
            3-hydroxy-3-methylglutaryl coenzyme A lyase;
            3-hydroxy-3-methylglutaryl CoA cleaving enzyme;
            3-hydroxy-3-methylglutaryl-CoA lyase;
            (S)-3-hydroxy-3-methylglutaryl-CoA acetoacetate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     (S)-3-hydroxy-3-methylglutaryl-CoA acetoacetate-lyase
            (acetyl-CoA-forming)
REACTION    (S)-3-hydroxy-3-methylglutaryl-CoA = acetyl-CoA + acetoacetate
            [RN:R01360]
ALL_REAC    R01360
SUBSTRATE   (S)-3-hydroxy-3-methylglutaryl-CoA [CPD:C00356]
PRODUCT     acetyl-CoA [CPD:C00024];
            acetoacetate [CPD:C00164]
REFERENCE   1  [PMID:13271348]
  AUTHORS   BACHHAWAT BK, ROBINSON WG, COON MJ.
  TITLE     The enzymatic cleavage of beta-hydroxy-beta-methylglutaryl coenzyme
            A to acetoacetate and acetyl coenzyme A.
  JOURNAL   J. Biol. Chem. 216 (1955) 727-36.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00072  Synthesis and degradation of ketone bodies
            PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K01640  hydroxymethylglutaryl-CoA lyase
GENES       HSA: 3155(HMGCL)
            MMU: 15356(Hmgcl)
            RNO: 79238(Hmgcl)
            BTA: 317658(HMGCL)
            GGA: 396316(HMGCL)
            XLA: 432233(MGC82338)
            DRE: 394190(zgc:56248)
            SPU: 756856(LOC756856)
            DME: Dmel_CG10399
            CEL: Y71G12B.10
            ATH: AT2G26800
            OSA: 4326266
            CME: CMA068C
            ANI: AN5273.2
            AFM: AFUA_2G12450 AFUA_7G01720
            AOR: AO090038000541
            UMA: UM02001.1
            DDI: DDB_0230167(hmgL)
            TET: TTHERM_00686100
            TBR: Tb927.4.2700
            TCR: 506635.80 508027.129 508029.10
            XCC: XCC1832(mvaB)
            XCB: XC_2357
            XCV: XCV1897(mvaB)
            XAC: XAC1851(mvaB)
            XOO: XOO2903(mvaB)
            XOM: XOO_2753(XOO2753)
            VVU: VV2_0499 VV2_0500
            VVY: VVA1049
            VPA: VPA0615 VPA1129
            PPR: PBPRB1119
            PAE: PA2011
            PAU: PA14_38490(gnyL)
            PPU: PP_3540(mvaB)
            PST: PSPTO_2742(mvaB)
            PSB: Psyr_2471
            PSP: PSPPH_2629(mvaB)
            PFL: PFL_3934(mvaB)
            PFO: Pfl_1315 Pfl_3654
            PEN: PSEEN2983(mvaB)
            PAR: Psyc_0312(mvaB)
            ACI: ACIAD2820
            SON: SO_1893(mvaB)
            SDN: Sden_2250
            SFR: Sfri_2731
            SHN: Shewana3_1668
            ILO: IL0878
            CPS: CPS_1599(mvaB)
            PHA: PSHAa1448(hmgcL)
            PAT: Patl_2762 Patl_2929
            CBU: CBU_0520(leuA)
            CBD: COXBU7E912_1542(leuA)
            LPN: lpg1830(mvaB)
            LPF: lpl1794
            LPP: lpp1793
            NOC: Noc_1888
            HCH: HCH_03947
            ABO: ABO_2665(mvaB)
            AHA: AHA_2074
            CVI: CV_1759(mvaB)
            RSO: RSc0261(RS00696)
            REU: Reut_A0153 Reut_A1462 Reut_A2107 Reut_B4194
            REH: H16_A0186 H16_A1235(mvaB) H16_A1547 H16_A2385(hmgL1)
                 H16_B2494(hmgL2)
            RME: Rmet_0607 Rmet_2124
            BXE: Bxe_A2729 Bxe_A4270
            BUR: Bcep18194_A4853 Bcep18194_A6309 Bcep18194_C6961
            BCN: Bcen_1213
            BAM: Bamb_1600 Bamb_3007
            BPS: BPSL0333
            BPM: BURPS1710b_0543
            BTE: BTH_I0313
            BPE: BP0556(hmgcL) BP3695
            BPA: BPP0239(hmgcL) BPP0508 BPP2803(hmgL)
            BBR: BB0243(hmgcL) BB0714(hmgL) BB3124(hmgL)
            RFR: Rfer_3824
            POL: Bpro_2353 Bpro_4037 Bpro_4155
            MPT: Mpe_A3354
            HAR: HEAR0103
            MMS: mma_0124(hmgL)
            EBA: ebA4662(hmgL)
            AZO: azo3065(mvaB)
            DAR: Daro_0086
            GME: Gmet_3293
            BBA: Bd3576(mvaB)
            ADE: Adeh_1644
            MXA: MXAN_3753
            SME: SMb21125(hmgL)
            SMD: Smed_4536
            ATU: Atu3480(hmgL)
            ATC: AGR_L_2702
            BME: BMEI1926
            BMF: BAB1_0017
            BMB: BruAb1_0017(mvaB)
            BOV: BOV_0014(mvaB)
            OAN: Oant_0040
            BJA: bll6364 blr0698 blr4422(hmgL)
            BRA: BRADO3681(hmgL)
            BBT: BBta_4049(hmgL)
            RPA: RPA2540(hmgL)
            RPB: RPB_2932
            RPC: RPC_2780
            RPD: RPD_2536
            RPE: RPE_2910
            CCR: CC_0467
            SIL: SPO2788(mvaB)
            SIT: TM1040_0739
            RSP: RSP_2510(hmgL)
            RSH: Rsph17029_1172
            JAN: Jann_1149
            RDE: RD1_3295(mvaB)
            PDE: Pden_3641
            HNE: HNE_1080 HNE_3374
            RRU: Rru_A1940
            MAG: amb0673
            ABA: Acid345_1427
            BSU: BG13458(yngG)
            BHA: BH1134
            BAN: BA2550(mvaB)
            BAR: GBAA2550(mvaB)
            BAA: BA_3052
            BAT: BAS2372
            BCE: BC2486
            BCA: BCE_2551(mvaB)
            BCZ: BCZK2288(mvaB)
            BTK: BT9727_2330(mvaB)
            BLI: BL01990(yngG)
            BLD: BLi02141(yngG)
            BCL: ABC0547
            BPU: BPUM_1782(yngG)
            OIH: OB1343 OB3230
            GKA: GK1601
            MPA: MAP3194
            MSM: MSMEG_2024
            MMC: Mmcs_1588
            NFA: nfa46700
            RHA: RHA1_ro04924 RHA1_ro05078
            SCO: SCO2778(hmgL)
            SMA: SAV5276(hmgL)
            SEN: SACE_4360 SACE_6499(hmgL)
            LIL: LA0845
            LIC: LIC12782
            LBL: LBL_2733(leuA-4)
            CHU: CHU_1436(leuA)
            GFO: GFO_2517(mvaB)
            FPS: FP1821(mvaB)
            TTH: TTC1162
            TTJ: TTHA1526
STRUCTURES  PDB: 1YDN  2CW6  2FTP  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.4
            ExPASy - ENZYME nomenclature database: 4.1.3.4
            ExplorEnz - The Enzyme Database: 4.1.3.4
            ERGO genome analysis and discovery system: 4.1.3.4
            BRENDA, the Enzyme Database: 4.1.3.4
            CAS: 9030-83-5
///
ENTRY       EC 4.1.3.5        Obsolete  Enzyme
NAME        Transferred to 2.3.3.10
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.3.3.10 hydroxymethylglutaryl-CoA
            synthase (EC 4.1.3.5 created 1961, deleted 2002)
STRUCTURES  PDB: 1TVZ  1TXT  1X9E  1YSL  2HDB  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.5
            ExPASy - ENZYME nomenclature database: 4.1.3.5
            ExplorEnz - The Enzyme Database: 4.1.3.5
            ERGO genome analysis and discovery system: 4.1.3.5
            BRENDA, the Enzyme Database: 4.1.3.5
///
ENTRY       EC 4.1.3.6                  Enzyme
NAME        citrate (pro-3S)-lyase;
            citrase;
            citratase;
            citritase;
            citridesmolase;
            citrate aldolase;
            citric aldolase;
            citrate lyase;
            citrate oxaloacetate-lyase;
            citrate oxaloacetate-lyase [(pro-3S)-CH2COO-->acetate]
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     citrate oxaloacetate-lyase (forming acetate from the pro-S
            carboxymethyl group of citrate)
REACTION    citrate = acetate + oxaloacetate [RN:R00362]
ALL_REAC    R00362
SUBSTRATE   citrate [CPD:C00158]
PRODUCT     acetate [CPD:C00033];
            oxaloacetate [CPD:C00036]
COMMENT     The enzyme can be dissociated into components, two of which are
            identical with EC 2.8.3.10 (citrate CoA-transferase) and EC 4.1.3.34
            (citryl-CoA lyase). EC 3.1.2.16, citrate lyase deacetylase,
            deacetylates and inactivates the enzyme.
REFERENCE   1  [PMID:13239657]
  AUTHORS   DAGLEY S, DAWES EA.
  TITLE     Citridesmolase: its properties and mode of action.
  JOURNAL   Biochim. Biophys. Acta. 17 (1955) 177-84.
  ORGANISM  Escherichia coli [GN:eco], Aerobacter aerogenes
REFERENCE   2  [PMID:336371]
  AUTHORS   Dimroth P, Loyal R, Eggerer H.
  TITLE     Characterization of the isolated transferase subunit of citrate
            lyase as a CoA-Transferase. Evidence against a covalent
            enzyme-substrate intermediate.
  JOURNAL   Eur. J. Biochem. 80 (1977) 479-88.
  ORGANISM  Klebsiella aerogenes
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K01642  citrate lyase
            KO: K01643  citrate lyase alpha chain
            KO: K01644  citrate lyase beta chain
            KO: K01646  citrate lyase gamma chain
GENES       HSA: 171425(CLYBL)
            PTR: 452639(CLYBL)
            MMU: 69634(Clybl)
            CFA: 476974(CLYBL)
            GGA: 418775(CLYBL)
            XLA: 447169(MGC85519)
            SPU: 580730(LOC580730)
            CEL: C01G10.7
            ANI: AN3577.2
            AFM: AFUA_4G13030
            AOR: AO090009000285
            UMA: UM05677.1
            DDI: DDBDRAFT_0185816
            ECO: b0615(citF) b0616(citE) b0617(citD)
            ECJ: JW0608(citE) JW0609(citD) JW5087(citF)
            ECE: Z0759(citF) Z0760(citE) Z0761(citD)
            ECS: ECs0654 ECs0655 ECs0656
            ECC: c0704(citF) c0706(citE)
            ECI: UTI89_C0618(citF) UTI89_C0620(citE) UTI89_C0621(citD)
            ECP: ECP_0646 ECP_0647 ECP_0648
            ECV: APECO1_1435(citE) APECO1_1436(citF)
            ECW: EcE24377A_0637(citF) EcE24377A_0638(citE)
                 EcE24377A_0639(citD)
            ECX: EcHS_A0666(citF) EcHS_A0667(citE) EcHS_A0668(citD)
            STY: STY0068(citD2) STY0069(citE2) STY0070(citF2) STY0670(citF)
                 STY0671(citE) STY0672(citD)
            STT: t0061(citD) t0062(citE) t0063(citF) t2244(citD) t2245(citE)
                 t2246(citF)
            SPT: SPA0060(citD) SPA0061(citE) SPA0062(citF) SPA2111(citD)
                 SPA2112(citE) SPA2113(citF)
            SEC: SC0053(citD2) SC0054(citE2) SC0055(citF2) SC0650(citF)
                 SC0651(citE) SC0652(citD) SC3060(cilB)
            STM: STM0059(citD2) STM0060(citE2) STM0061(citF2) STM0621(citF)
                 STM0622(citE) STM0623(citD) STM3120
            YPE: YPO1928
            YPK: y2383
            YPM: YP_1670(citE2)
            YPA: YPA_1306
            YPS: YPTB1926
            YEN: YE2650(citF)
            SFL: SF0532(citF) SF0533(citE) SF0534(citD)
            SFX: S0539(citF) S0540(citE) S0541(citD)
            SFV: SFV_0568(citF) SFV_0569(citE) SFV_0570(citD)
            SSN: SSON_0567(citF) SSON_0568(citE) SSON_0569(citD)
            SBO: SBO_0480(citF) SBO_0481(citE) SBO_0482(citD)
            ECA: ECA2571(citF) ECA2572(citE) ECA2573(citD) ECA4117
            ENT: Ent638_3372 Ent638_3373
            HIN: HI0022(citF) HI0023(citE) HI0024(citD)
            HIT: NTHI0029(citF) NTHI0030(citE) NTHI0031(citD)
            HDU: HD1241(citD) HD1242(citE) HD1243(citF)
            ASU: Asuc_1195
            VCH: VC0797 VC0798 VC0799
            VCO: VC0395_A0325(citE) VC0395_A0326(citF)
            PPR: PBPRA2292(citF) PBPRA2293
            PAE: PA0883
            PSB: Psyr_2171
            PFL: PFL_2651(citE)
            PCR: Pcryo_0865
            PAT: Patl_2717
            MCA: MCA1739
            HCH: HCH_03524
            RSO: RSc1999(RS03567)
            REU: Reut_A2328 Reut_B3539 Reut_B4148 Reut_B5821
            REH: H16_A2635(citE1) H16_B0353(citE2) H16_B0680(citE3)
                 H16_B2113(citE4)
            RME: Rmet_2490 Rmet_4429
            BMA: BMAA1653 BMAA1752 BMAA1951
            BXE: Bxe_A2758 Bxe_B0989 Bxe_B2581 Bxe_B2899 Bxe_C0268 Bxe_C0669
                 Bxe_C0830
            BUR: Bcep18194_B2155 Bcep18194_C7288 Bcep18194_C7302
            BCN: Bcen_5807
            BCH: Bcen2424_3931 Bcen2424_6171
            BAM: Bamb_3308
            BPS: BPSS1639 BPSS1723 BPSS2150 BPSS2159
            BPM: BURPS1710b_A0703 BURPS1710b_A0797 BURPS1710b_A1261
                 BURPS1710b_A1273
            BPD: BURPS668_A2305(cilB)
            BTE: BTH_II0657 BTH_II2226 BTH_II2235
            BPE: BP1348(citE) BP1861(citE)
            BPA: BPP0350 BPP1572(citE) BPP2682(citE) BPP3513(citE) BPP3643
            BBR: BB2650(citE) BB2826(citE) BB3948(citE) BB4078
            RFR: Rfer_1804 Rfer_2407 Rfer_2408 Rfer_2409 Rfer_3486 Rfer_4179
            POL: Bpro_0580 Bpro_3597
            MPT: Mpe_A2173 Mpe_A3254
            MMS: mma_1503(citE)
            NEU: NE1809
            NET: Neut_0607
            NMU: Nmul_A1078
            EBA: ebA6697(citE)
            AZO: azo1546(citE)
            DAR: Daro_2868
            TDN: Tmden_1111
            NIS: NIS_0713(citE)
            SUN: SUN_0980(citE)
            AFW: Anae109_0199
            SFU: Sfum_2561
            MLO: mll6008 mlr0906 mlr1323 mlr4422(citE)
            MES: Meso_1012
            PLA: Plav_2682
            SME: SMc03793(citE)
            SMD: Smed_3026
            ATU: Atu2788(citE)
            ATC: AGR_C_5061
            RET: RHE_CH04088(citEch) RHE_PC00060(citEc)
            RLE: RL4702(citE) pRL100292
            BME: BMEII0413 BMEII1074
            BMF: BAB2_0164 BAB2_0355
            BMS: BRA0168
            BMB: BruAb2_0163 BruAb2_0351
            OAN: Oant_3299
            BJA: bll0499(citE) blr6797
            RPA: RPA0233(citE) RPA4559
            RPB: RPB_0341
            RPD: RPD_0496
            RPE: RPE_0340 RPE_3428 RPE_3429 RPE_3430
            NWI: Nwi_2289
            NHA: Nham_2705
            CCR: CC_2999 CC_3659
            SIL: SPO0352(citE) SPO1565
            RSP: RSP_0970 RSP_1771
            RSH: Rsph17029_2630
            RSQ: Rsph17025_0082 Rsph17025_2481
            JAN: Jann_0471
            RDE: RD1_1001(citE) RD1_1620(citE) RD1_4242(mclA)
            PDE: Pden_0799
            MMR: Mmar10_2882
            HNE: HNE_3534(citE)
            ZMO: ZMO0487
            NAR: Saro_0092 Saro_0233
            ELI: ELI_03140
            RRU: Rru_A0217 Rru_A1200
            MAG: amb3948 amb3977
            MGM: Mmc1_3153
            ABA: Acid345_2962
            LLA: L0039(citD) L0040(citE) L0041(citF)
            SPY: SPy_1186(citD) SPy_1188(citE) SPy_1189(citF)
            SPZ: M5005_Spy_0905(citD) M5005_Spy_0906(citE)
                 M5005_Spy_0907(citF)
            SPM: spyM18_1137(citD) spyM18_1139(citE) spyM18_1140(citF)
            SPG: SpyM3_0832(citD) SpyM3_0833(citE) SpyM3_0834(citF)
            SPS: SPs1032 SPs1033 SPs1034
            SPH: MGAS10270_Spy1019(citD) MGAS10270_Spy1020(citE)
                 MGAS10270_Spy1021(citF)
            SPI: MGAS10750_Spy1055(citD) MGAS10750_Spy1056(citE)
                 MGAS10750_Spy1057(citF)
            SPF: SpyM50890(citF) SpyM50891(citE)
            SPA: M6_Spy0894 M6_Spy0895 M6_Spy0896
            SPB: M28_Spy0878(citD) M28_Spy0879(citE) M28_Spy0880(citF)
            SMU: SMU.1019(cilG) SMU.1020(cilB) SMU.1021(cilA)
            LPL: lp_1107(citD) lp_1108(citE) lp_1109(citF)
            LAC: LBA0915(citD) LBA0916(citE) LBA0917(citF)
            LSA: LSA1224(citF) LSA1225(citE) LSA1226(citD)
            LCA: LSEI_1857 LSEI_1858 LSEI_1859
            EFA: EF3319(citF) EF3320(citE) EF3321(citD)
            OOE: OEOE_0421 OEOE_0422 OEOE_0423
            CPE: CPE1147(cilG) CPE1148(cilB) CPE1149(cilA)
            CPR: CPR_1163(citD) CPR_1164(citE) CPR_1165(citF)
            CTC: CTC02466 CTC02467 CTC02559 CTC02560
            AMT: Amet_3224
            DSY: DSY1924 DSY3038 DSY3039 DSY3040
            MTA: Moth_0400
            MSY: MS53_0535
            MTU: Rv2498c(citE) Rv3075c
            MTC: MT2573(citE) MT3160
            MBO: Mb2526c(citE)
            MBB: BCG_2518c(citE)
            MPA: MAP0293 MAP1688 MAP2310c(citE) MAP3152c
            MAV: MAV_2730
            MSM: MSMEG_4713 MSMEG_5064
            MVA: Mvan_4487
            MMC: Mmcs_3627 Mmcs_5204
            MKM: Mkms_4060
            MJL: Mjls_4000
            CGL: NCgl0828(cgl0862)
            CEF: CE0938(citE)
            CDI: DIP0845
            CJK: jk1547(citE)
            NFA: nfa47160 nfa50410
            RHA: RHA1_ro00185 RHA1_ro00306 RHA1_ro00662 RHA1_ro00775
                 RHA1_ro02872 RHA1_ro02943 RHA1_ro05986 RHA1_ro06099
                 RHA1_ro06584
            SCO: SCO2033(SC4G6.02) SCO6471(SC9C7.07c) SCP1.302
            SMA: SAV1913(citE2) SAV6181(citE1)
            PAC: PPA1919
            TFU: Tfu_1313
            FRA: Francci3_2166 Francci3_2804 Francci3_2805 Francci3_2925
            FAL: FRAAL3117(citE) FRAAL3432(citF) FRAAL5522(citE) FRAAL6071
            SEN: SACE_1042 SACE_2331(citE3) SACE_4581(citE3)
            FNU: FN1378 FN1379 FN1380
            TDE: TDE1631(citF) TDE1632(citE) TDE1633(citD)
            LIL: LA2841(citE)
            LIC: LIC11194
            LBJ: LBJ_2023(citE)
            LBL: LBL_1027(citE)
            DRA: DR_1240 DR_2206
            HAL: VNG0627G(citE)
            HMA: rrnAC0690(citE1) rrnB0257(citE2)
            NPH: NP4244A(citE)
            APE: APE_0311
            SSO: SSO1254(citE)
            STO: ST1786
            SAI: Saci_0312(citE)
STRUCTURES  PDB: 1U5H  1U5V  1Z6K  2HJ0  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.6
            ExPASy - ENZYME nomenclature database: 4.1.3.6
            ExplorEnz - The Enzyme Database: 4.1.3.6
            ERGO genome analysis and discovery system: 4.1.3.6
            BRENDA, the Enzyme Database: 4.1.3.6
            CAS: 9012-83-3
///
ENTRY       EC 4.1.3.7        Obsolete  Enzyme
NAME        Transferred to 2.3.3.1
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.3.3.1, citrate (Si)-synthase (EC 4.1.3.7
            created 1961, deleted 2002)
STRUCTURES  PDB: 1AJ8  1AL6  1AMZ  1CSC  1CSH  1CSI  1CSR  1CSS  1CTS  1IOM  
                 1IXE  1K3P  1NXE  1NXG  1O7X  1OWB  1OWC  1VGM  1VGP  2CSC  
                 2CTS  3CSC  3CTS  4CSC  4CTS  5CSC  5CTS  6CSC  6CTS  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.7
            ExPASy - ENZYME nomenclature database: 4.1.3.7
            ExplorEnz - The Enzyme Database: 4.1.3.7
            ERGO genome analysis and discovery system: 4.1.3.7
            BRENDA, the Enzyme Database: 4.1.3.7
///
ENTRY       EC 4.1.3.8        Obsolete  Enzyme
NAME        Transferred to 2.3.3.8
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.3.3.8 ATP citrate synthase (EC 4.1.3.8
            created 1965, modified 1986, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.8
            ExPASy - ENZYME nomenclature database: 4.1.3.8
            ExplorEnz - The Enzyme Database: 4.1.3.8
            ERGO genome analysis and discovery system: 4.1.3.8
            BRENDA, the Enzyme Database: 4.1.3.8
///
ENTRY       EC 4.1.3.9        Obsolete  Enzyme
NAME        Transferred to 2.3.3.11
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.3.3.11 2-hydroxyglutarate synthase (EC
            4.1.3.9 created 1965, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.9
            ExPASy - ENZYME nomenclature database: 4.1.3.9
            ExplorEnz - The Enzyme Database: 4.1.3.9
            ERGO genome analysis and discovery system: 4.1.3.9
            BRENDA, the Enzyme Database: 4.1.3.9
///
ENTRY       EC 4.1.3.10       Obsolete  Enzyme
NAME        Transferred to 2.3.3.7
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.3.3.7 3-ethylmalate synthase (EC
            4.1.3.10 created 1965, modified 1983, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.10
            ExPASy - ENZYME nomenclature database: 4.1.3.10
            ExplorEnz - The Enzyme Database: 4.1.3.10
            ERGO genome analysis and discovery system: 4.1.3.10
            BRENDA, the Enzyme Database: 4.1.3.10
///
ENTRY       EC 4.1.3.11       Obsolete  Enzyme
NAME        Transferred to 2.3.3.12
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.3.3.12 3-propylmalate synthase (EC
            4.1.3.11 created 1972, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.11
            ExPASy - ENZYME nomenclature database: 4.1.3.11
            ExplorEnz - The Enzyme Database: 4.1.3.11
            ERGO genome analysis and discovery system: 4.1.3.11
            BRENDA, the Enzyme Database: 4.1.3.11
///
ENTRY       EC 4.1.3.12       Obsolete  Enzyme
NAME        Transferred to 2.3.3.13
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.3.3.13 2-isopropylmalate synthase (EC
            4.1.3.12 created 1972, deleted 2002)
GENES       SPO: SPBC3E7.16c SPBC4F6.03c
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.12
            ExPASy - ENZYME nomenclature database: 4.1.3.12
            ExplorEnz - The Enzyme Database: 4.1.3.12
            ERGO genome analysis and discovery system: 4.1.3.12
            BRENDA, the Enzyme Database: 4.1.3.12
///
ENTRY       EC 4.1.3.13                 Enzyme
NAME        oxalomalate lyase;
            3-oxalomalate glyoxylate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     3-oxalomalate glyoxylate-lyase (oxaloacetate-forming)
REACTION    3-oxalomalate = oxaloacetate + glyoxylate [RN:R00477]
ALL_REAC    R00477
SUBSTRATE   3-oxalomalate [CPD:C01990]
PRODUCT     oxaloacetate [CPD:C00036];
            glyoxylate [CPD:C00048]
REFERENCE   1  [PMID:6005666]
  AUTHORS   Sekizawa Y, Maragoudakis ME, King TE, Cheldelin VH.
  TITLE     Glutamate biosynthesis in an organism lacking a Krebs tricarboxylic
            acid cycle. V. Isolation of alpha-hydroxy-gamma-ketoglutarate (HKG)
            in Acetobacter suboxydans.
  JOURNAL   Biochemistry. 5 (1966) 2392-8.
  ORGANISM  Acetobacter suboxydans
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.13
            ExPASy - ENZYME nomenclature database: 4.1.3.13
            ExplorEnz - The Enzyme Database: 4.1.3.13
            ERGO genome analysis and discovery system: 4.1.3.13
            BRENDA, the Enzyme Database: 4.1.3.13
            CAS: 37290-63-4
///
ENTRY       EC 4.1.3.14                 Enzyme
NAME        3-hydroxyaspartate aldolase;
            erythro-beta-hydroxyaspartate aldolase;
            erythro-beta-hydroxyaspartate glycine-lyase;
            erythro-3-hydroxy-Ls-aspartate glyoxylate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     erythro-3-hydroxy-Ls-aspartate glyoxylate-lyase (glycine-forming)
REACTION    erythro-3-hydroxy-Ls-aspartate = glycine + glyoxylate [RN:R00478]
ALL_REAC    R00478
SUBSTRATE   erythro-3-hydroxy-Ls-aspartate
PRODUCT     glycine [CPD:C00037];
            glyoxylate [CPD:C00048]
REFERENCE   1  [PMID:14194868]
  AUTHORS   GIBBS RG, MORRIS JG.
  TITLE     ASSAY AND PROPERTIES OF BETA-HYDROXYASPARTATE ALDOLASE FROM
            MICROCOCCUS DENITRIFICANS.
  JOURNAL   Biochim. Biophys. Acta. 85 (1964) 501-3.
  ORGANISM  Micrococcus denitrificans
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.14
            ExPASy - ENZYME nomenclature database: 4.1.3.14
            ExplorEnz - The Enzyme Database: 4.1.3.14
            ERGO genome analysis and discovery system: 4.1.3.14
            BRENDA, the Enzyme Database: 4.1.3.14
            CAS: 37290-64-5
///
ENTRY       EC 4.1.3.15       Obsolete  Enzyme
NAME        Transferred to 2.2.1.5
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.2.1.5 2-hydroxy-3-oxoadipate synthase
            (EC 4.1.3.15 created 1972, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.15
            ExPASy - ENZYME nomenclature database: 4.1.3.15
            ExplorEnz - The Enzyme Database: 4.1.3.15
            ERGO genome analysis and discovery system: 4.1.3.15
            BRENDA, the Enzyme Database: 4.1.3.15
///
ENTRY       EC 4.1.3.16                 Enzyme
NAME        4-hydroxy-2-oxoglutarate aldolase;
            2-oxo-4-hydroxyglutarate aldolase;
            hydroxyketoglutaric aldolase;
            4-hydroxy-2-ketoglutaric aldolase;
            2-keto-4-hydroxyglutaric aldolase;
            4-hydroxy-2-ketoglutarate aldolase;
            2-keto-4-hydroxyglutarate aldolase;
            2-oxo-4-hydroxyglutaric aldolase;
            DL-4-hydroxy-2-ketoglutarate aldolase;
            hydroxyketoglutarate aldolase;
            2-keto-4-hydroxybutyrate aldolase;
            4-hydroxy-2-oxoglutarate glyoxylate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     4-hydroxy-2-oxoglutarate glyoxylate-lyase (pyruvate-forming)
REACTION    4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate [RN:R00470]
ALL_REAC    R00470 > R00471
SUBSTRATE   4-hydroxy-2-oxoglutarate [CPD:C01127]
PRODUCT     pyruvate [CPD:C00022];
            glyoxylate [CPD:C00048]
COMMENT     Acts on both stereoisomers. Previously listed also as EC 4.1.2.31.
REFERENCE   1  [PMID:14089442]
  AUTHORS   KURATOMI K, FUKUNAGA K.
  TITLE     THE METABOLISM OF GAMMA-HYDROXYGLUTAMATE IN RAT LIVER. I. ENZYMIC
            SYNTHESIS OF GAMMA-HYDROXY-ALPHA-KETOGLUTARATE FROM PYRUVATE AND
            GLYOXYLATE.
  JOURNAL   Biochim. Biophys. Acta. 78 (1963) 617-28.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:5580656]
  AUTHORS   Lane RS, Shapley A, Dekker EE.
  TITLE     2-keto-4-hydroxybutyrate aldolase. Identification as
            2-keto-4-hydroxyglutarate aldolase, catalytic properties, and role
            in the mammalian metabolism of L-homoserine.
  JOURNAL   Biochemistry. 10 (1971) 1353-64.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:4560498]
  AUTHORS   Nishihara H, Dekker EE.
  TITLE     Purification, substrate specificity and binding,  -decarboxylase
            activity, and other properties of Escherichia coli
            2-keto-4-hydroxyglutarate aldolase.
  JOURNAL   J. Biol. Chem. 247 (1972) 5079-87.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4
  AUTHORS   Wood, W.A.
  TITLE     2-Keto-3-deoxy-6-phosphogluconic and related aldolases.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 7, Academic Press,
            New York, 1972, p. 281-302.
PATHWAY     PATH: map00330  Arginine and proline metabolism
            PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K01650  4-hydroxy-2-oxoglutarate aldolase
GENES       CME: CMP292C
            ECO: b1850(eda)
            ECJ: JW1839(eda)
            ECE: Z2902(eda)
            ECS: ECs2560
            ECC: c2263(eda) c4777
            ECI: UTI89_C2053(eda) UTI89_C4415
            ECP: ECP_1794
            ECW: EcE24377A_2080(eda)
            ECX: EcHS_A1942(eda)
            STY: STY2091(kdgA)
            STT: t0993
            SPT: SPA0985(eda)
            SEC: SC1889(eda)
            STM: STM1884(eda)
            YPE: YPO2067(eda)
            YPK: y2243(eda)
            YPM: YP_1910(eda)
            YPA: YPA_1450
            YPN: YPN_1544
            YPS: YPTB2050(eda)
            SFL: SF1860(eda)
            SFX: S1926(eda)
            SFV: SFV_1852(eda)
            SSN: SSON_1298(eda)
            SBO: SBO_1158(eda)
            SDY: SDY_1136(eda)
            ECA: ECA2478(eda)
            PLU: plu0178(eda)
            SPE: Spro_4500
            HIN: HI0047(eda)
            HIT: NTHI0055(eda)
            HIP: CGSHiEE_03080
            PMU: PM0947(eda)
            MSU: MS0546(eda) MS0566(eda)
            ASU: Asuc_0152 Asuc_0374
            XFA: XF1061
            XFT: PD0342(eda)
            XCC: XCC2140(eda)
            XCB: XC_1973
            XCV: XCV2233(alkH)
            XAC: XAC2067(eda)
            XOO: XOO2318(eda)
            XOM: XOO_2195(XOO2195)
            VCH: VC0285
            VVU: VV1_1102 VV2_0904 VV2_1072
            VVY: VV0062 VV0555 VVA1387 VVA1596
            VPA: VP0065 VPA0083 VPA1708
            VFI: VF0090 VFA0987
            PPR: PBPRA1276 PBPRB0159(eda) PBPRB1732 PBPRB1883
            PAE: PA3131 PA3181
            PPU: PP_1024(eda)
            PST: PSPTO_1302(eda-1) PSPTO_2178(eda-2)
            PSB: Psyr_1122 Psyr_1988
            PSP: PSPPH_1190(eda1) PSPPH_1957(eda2)
            PFL: PFL_4608(eda)
            PFO: Pfl_4124 Pfl_4361
            PEN: PSEEN4403(eda)
            ACI: ACIAD0543(eda)
            SON: SO_2486(eda)
            SDN: Sden_2076
            SFR: Sfri_1895
            SHE: Shewmr4_2043
            SHM: Shewmr7_1932
            SHN: Shewana3_2148
            CPS: CPS_2284(eda)
            PHA: PSHAa1367(eda) PSHAa1744
            PAT: Patl_0974
            CBU: CBU_1277(eda)
            CBD: COXBU7E912_1366(eda)
            LPN: lpg0420(eda)
            LPF: lpl0463(eda)
            LPP: lpp0487(eda)
            MCA: MCA0038(eda)
            HCH: HCH_00349(eda)
            CSA: Csal_2739
            AHA: AHA_0289(eda)
            NME: NMB1394
            NMA: NMA1611(eda)
            NMC: NMC1333(eda)
            NGO: NGO0713
            CVI: CV_0143(eda)
            RSO: RSp1190(eda)
            REU: Reut_B4024
            RME: Rmet_4768
            BMA: BMA2445(eda) BMA2488
            BXE: Bxe_A0590
            BUR: Bcep18194_A3701 Bcep18194_A3747
            BAM: Bamb_0556
            BPS: BPSL2931(eda) BPSL2970
            BPM: BURPS1710b_3441 BURPS1710b_3487(eda-2)
            BPL: BURPS1106A_3441(eda)
            BPD: BURPS668_3406(eda)
            BTE: BTH_I1177 BTH_I1218
            RFR: Rfer_0938 Rfer_0950 Rfer_0961 Rfer_2061
            POL: Bpro_3535 Bpro_3550
            AJS: Ajs_2048
            VEI: Veis_2569
            HAR: HEAR1087(eda)
            HPY: HP1099(eda)
            HPJ: jhp1025(eda)
            HPA: HPAG1_1037
            HAC: Hac_0443(eda)
            CJD: JJD26997_1272
            MLO: mlr2994
            MES: Meso_2733
            SME: SMc00882 SMc02043(eda1) SMc03153(eda2)
            ATU: Atu0703(kdgA) Atu4494(kdgA)
            ATC: AGR_C_1269 AGR_L_750
            RET: RHE_CH00853(kdgA) RHE_CH03635(eda)
            RLE: RL4162(eda)
            BME: BMEII0009
            BMF: BAB2_0083
            BMB: BruAb2_0084
            BOV: BOV_A0079(eda)
            BJA: bll7287(dgoA) blr3923(kdgA)
            BRA: BRADO1806(eda)
            BBT: BBta_2126(eda)
            BHE: BH12770(eda)
            CCR: CC_0784 CC_1495
            SIL: SPO3031(eda-1) SPOA0330(eda-2)
            SIT: TM1040_0375
            RSP: RSP_2645(eda) RSP_3301(eda)
            JAN: Jann_1954
            RDE: RD1_2868(dgoA) RD1_2878(eda)
            MMR: Mmar10_2671
            HNE: HNE_1187(eda)
            ZMO: ZMO0997(eda)
            NAR: Saro_2568
            SAL: Sala_0192
            SWI: Swit_1626 Swit_1883
            ELI: ELI_00530
            GOX: GOX0430
            GBE: GbCGDNIH1_2044
            BSU: BG11396(kdgA)
            BHA: BH3723(kdgA)
            BLI: BL02470(kdgA) BL03850
            BLD: BLi03826(kdgA) BLi04071
            BCL: ABC0523 ABC3136
            OIH: OB2214 OB2703
            GKA: GK1956
            SHA: SH2651
            SSP: SSP2183
            LMO: lmo1969
            LLA: L0022(kdgA)
            LLC: LACR_1740
            LLM: llmg_0864(kdgA)
            SPY: SPy_0639(kgdA)
            SPZ: M5005_Spy_0527(kgdA)
            SPM: spyM18_0702(alkH)
            SPG: SpyM3_0451(kgdA)
            SPS: SPs1405
            SPH: MGAS10270_Spy0522(kgdA) MGAS10270_Spy1172
            SPI: MGAS10750_Spy0546(kgdA)
            SPJ: MGAS2096_Spy0539(kgdA)
            SPK: MGAS9429_Spy0518(kgdA)
            SPF: SpyM51336(kgdA)
            SPA: M6_Spy0548
            SPB: M28_Spy0506(kgdA)
            SPN: SP_0317
            SPR: spr0287(kdgA)
            SPD: SPD_0289(eda)
            SAG: SAG0700(eda-1) SAG1907(eda-2)
            SAN: gbs0673 gbs1894
            SAK: SAK_0826(eda)
            LBR: LVIS_0324
            LCA: LSEI_0051
            EFA: EF0423(eda-1) EF2266 EF3134(eda-2)
            CAC: CAC0394(kdgA) CAC2973(kdgA)
            CPE: CPE0150
            CPF: CPF_0397
            CDF: CD3626(kdgA)
            CBA: CLB_0336(eda)
            CBH: CLC_0351(eda)
            CBF: CLI_0365(eda)
            MTA: Moth_0420
            MSM: MSMEG_0312(eda) MSMEG_3788(eda)
            RHA: RHA1_ro02367
            SCO: SCO0852(SCM2.05c) SCO2298(kdgA) SCO3473(SCE65.09c)
                 SCO3495(SCE65.31c)
            SMA: SAV5878(kdgA)
            ART: Arth_1807
            PAC: PPA0371 PPA2133
            TFU: Tfu_0188
            SEN: SACE_1739(kdgA) SACE_2637 SACE_5973
            RXY: Rxyl_0079
            TPA: TP0568
            SYN: sll0107(eda)
            SYW: SYNW0306
            SYC: syc1480_d(eda)
            SYF: Synpcc7942_0017
            SYD: Syncc9605_0302
            SYG: sync_0356(eda)
            SYR: SynRCC307_2192(kdgA)
            SYX: SynWH7803_0356(kdgA)
            CYA: CYA_1625(eda)
            CYB: CYB_1899(eda)
            TEL: tlr1928
            GVI: gll4271
            ANA: all4771
            PMA: Pro0254(eda)
            PMM: PMM0225
            PMT: PMT1797
            PMN: PMN2A_1594
            PMI: PMT9312_0227
            PMB: A9601_02461(eda)
            PMC: P9515_02571(eda)
            PMG: P9301_02471(eda)
            PME: NATL1_03051(eda)
            TER: Tery_4949
            BTH: BT_0489
            BFR: BF2699
            BFS: BF2718
            DGE: Dgeo_2816
            TTH: TT_P0030
            TTJ: TTHB072
            TMA: TM0066
            HWA: HQ1495A(eda)
STRUCTURES  PDB: 1WAU  2C0A  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.16
            ExPASy - ENZYME nomenclature database: 4.1.3.16
            ExplorEnz - The Enzyme Database: 4.1.3.16
            ERGO genome analysis and discovery system: 4.1.3.16
            BRENDA, the Enzyme Database: 4.1.3.16
            CAS: 9030-81-3
///
ENTRY       EC 4.1.3.17                 Enzyme
NAME        4-hydroxy-4-methyl-2-oxoglutarate aldolase;
            pyruvate aldolase;
            gamma-methyl-gamma-hydroxy-alpha-ketoglutaric aldolase;
            4-hydroxy-4-methyl-2-ketoglutarate aldolase;
            4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase (pyruvate-forming)
REACTION    4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate [RN:R00008]
ALL_REAC    R00008;
            (other) R00350
SUBSTRATE   4-hydroxy-4-methyl-2-oxoglutarate [CPD:C06033]
PRODUCT     pyruvate [CPD:C00022]
COMMENT     Also acts on 4-hydroxy-4-methyl-2-oxoadipate and
            4-carboxy-4-hydroxy-2-oxohexadioate.
REFERENCE   1  [PMID:6841353]
  AUTHORS   Maruyama K.
  TITLE     Purification and properties of 2-pyrone-4,6-dicarboxylate hydrolase.
  JOURNAL   J. Biochem. (Tokyo). 93 (1983) 557-65.
  ORGANISM  Pseudomonas ochraceae
REFERENCE   2
  AUTHORS   Sharma, M.L., Kaul, S.M. and Shukla, O.P.
  TITLE     Metabolism of 2-hydroxypyridine by Bacillus brevis (INA).
  JOURNAL   Biol. Membr. 9 (1984) 43-52.
  ORGANISM  Bacillus brevis
REFERENCE   3  [PMID:5076765]
  AUTHORS   Tack BF, Chapman PJ, Dagley S.
  TITLE     Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate
            aldolase.
  JOURNAL   J. Biol. Chem. 247 (1972) 6444-9.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   4
  AUTHORS   Wood, W.A.
  TITLE     2-Keto-3-deoxy-6-phosphogluconic and related aldolases.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 7, Academic Press,
            New York, 1972, p. 281-302.
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00660  C5-Branched dibasic acid metabolism
ORTHOLOGY   KO: K10218  4-hydroxy-4-methyl-2-oxoglutarate aldolase
GENES       ECX: EcHS_A3300(sdaA1)
            RLE: RL2851
            BRA: BRADO2338(ligK)
            BBT: BBta_2698(ligK)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.17
            ExPASy - ENZYME nomenclature database: 4.1.3.17
            ExplorEnz - The Enzyme Database: 4.1.3.17
            ERGO genome analysis and discovery system: 4.1.3.17
            BRENDA, the Enzyme Database: 4.1.3.17
            CAS: 37290-65-6
///
ENTRY       EC 4.1.3.18       Obsolete  Enzyme
NAME        Transferred to 2.2.1.6
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.2.1.6 acetolactate synthase (EC 4.1.3.18
            created 1972, deleted 2002)
GENES       BTE: BTH_II1989
STRUCTURES  PDB: 1JSC  1N0H  1OZF  1OZG  1OZH  2PC6  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.18
            ExPASy - ENZYME nomenclature database: 4.1.3.18
            ExplorEnz - The Enzyme Database: 4.1.3.18
            ERGO genome analysis and discovery system: 4.1.3.18
            BRENDA, the Enzyme Database: 4.1.3.18
///
ENTRY       EC 4.1.3.19       Obsolete  Enzyme
NAME        Transferred to 2.5.1.56
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.5.1.56 N-acetylneuraminate synthase (EC
            4.1.3.19 created 1972, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.19
            ExPASy - ENZYME nomenclature database: 4.1.3.19
            ExplorEnz - The Enzyme Database: 4.1.3.19
            ERGO genome analysis and discovery system: 4.1.3.19
            BRENDA, the Enzyme Database: 4.1.3.19
///
ENTRY       EC 4.1.3.20       Obsolete  Enzyme
NAME        Transferred to 2.5.1.57
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.5.1.57 N-acylneuraminate-9-phosphate
            synthase (EC 4.1.3.20 created 1972, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.20
            ExPASy - ENZYME nomenclature database: 4.1.3.20
            ExplorEnz - The Enzyme Database: 4.1.3.20
            ERGO genome analysis and discovery system: 4.1.3.20
            BRENDA, the Enzyme Database: 4.1.3.20
///
ENTRY       EC 4.1.3.21       Obsolete  Enzyme
NAME        Transferred to 2.3.3.14
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.3.3.14 homocitrate synthase (EC 4.1.3.21
            created 1972, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.21
            ExPASy - ENZYME nomenclature database: 4.1.3.21
            ExplorEnz - The Enzyme Database: 4.1.3.21
            ERGO genome analysis and discovery system: 4.1.3.21
            BRENDA, the Enzyme Database: 4.1.3.21
///
ENTRY       EC 4.1.3.22                 Enzyme
NAME        citramalate lyase;
            citramalate pyruvate-lyase;
            citramalate synthase;
            citramalic-condensing enzyme;
            citramalate synthetase;
            citramalic synthase;
            (S)-citramalate lyase;
            (+)-citramalate pyruvate-lyase;
            citramalate pyruvate lyase;
            (3S)-citramalate pyruvate-lyase;
            (2S)-2-hydroxy-2-methylbutanedioate pyruvate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     (2S)-2-hydroxy-2-methylbutanedioate pyruvate-lyase (acetate-forming)
REACTION    (2S)-2-hydroxy-2-methylbutanedioate = acetate + pyruvate [RN:R00325]
ALL_REAC    R00325;
            (other) R00237 R03153
SUBSTRATE   (2S)-2-hydroxy-2-methylbutanedioate [CPD:C02614]
PRODUCT     acetate [CPD:C00033];
            pyruvate [CPD:C00022]
COMMENT     The enzyme can be dissociated into components, two of which are
            identical with EC 2.8.3.11 (citramalate CoA-transferase) and EC
            4.1.3.25 (citramalyl-CoA lyase).
REFERENCE   1  [PMID:4301387]
  AUTHORS   Barker HA.
  TITLE     Citramalate lyase of Clostridium tetanomorphum.
  JOURNAL   Arch. Mikrobiol. 59 (1967) 4-12.
  ORGANISM  Clostridium tetanomorphum
REFERENCE   2  [PMID:923590]
  AUTHORS   Dimroth P, Buckel W, Loyal R, Eggerer H.
  TITLE     Isolation and function of the subunits of citramalate lyase and
            formation of hybrids with the subunits of citrate lyase.
  JOURNAL   Eur. J. Biochem. 80 (1977) 469-77.
  ORGANISM  Clostridium tetanomorphum
PATHWAY     PATH: map00660  C5-Branched dibasic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.22
            ExPASy - ENZYME nomenclature database: 4.1.3.22
            ExplorEnz - The Enzyme Database: 4.1.3.22
            ERGO genome analysis and discovery system: 4.1.3.22
            BRENDA, the Enzyme Database: 4.1.3.22
            CAS: 9027-93-4
///
ENTRY       EC 4.1.3.23       Obsolete  Enzyme
NAME        Transferred to 2.3.3.2
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.3.3.2 decylcitrate synthase (EC 4.1.3.23
            created 1972, deleted 2002)
STRUCTURES  PDB: 2FFC  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.23
            ExPASy - ENZYME nomenclature database: 4.1.3.23
            ExplorEnz - The Enzyme Database: 4.1.3.23
            ERGO genome analysis and discovery system: 4.1.3.23
            BRENDA, the Enzyme Database: 4.1.3.23
///
ENTRY       EC 4.1.3.24                 Enzyme
NAME        malyl-CoA lyase;
            malyl-coenzyme A lyase;
            (3S)-3-carboxy-3-hydroxypropanoyl-CoA glyoxylate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     (3S)-3-carboxy-3-hydroxypropanoyl-CoA glyoxylate-lyase
            (acetyl-CoA-forming)
REACTION    (3S)-3-carboxy-3-hydroxypropanoyl-CoA = acetyl-CoA + glyoxylate
            [RN:R00473]
ALL_REAC    R00473
SUBSTRATE   (3S)-3-carboxy-3-hydroxypropanoyl-CoA [CPD:C04348]
PRODUCT     acetyl-CoA [CPD:C00024];
            glyoxylate [CPD:C00048]
REFERENCE   1
  AUTHORS   Tuboi, S. and Kikuchi, G.
  TITLE     Enzymic cleavage of malyl-Coenzyme A into acetyl-Coenzyme A and
            glyoxylic acid.
  JOURNAL   Biochim. Biophys. Acta 96 (1965) 148-153.
  ORGANISM  Rhodopseudomonas sphaeroides
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K08691  malyl-CoA lyase
GENES       SIL: SPO3608(mclA)
            RDE: RD1_1160(mclA)
            HNE: HNE_0078(mclA)
            GBE: GbCGDNIH1_0055
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.24
            ExPASy - ENZYME nomenclature database: 4.1.3.24
            ExplorEnz - The Enzyme Database: 4.1.3.24
            ERGO genome analysis and discovery system: 4.1.3.24
            BRENDA, the Enzyme Database: 4.1.3.24
            CAS: 37290-67-8
///
ENTRY       EC 4.1.3.25                 Enzyme
NAME        citramalyl-CoA lyase;
            citramalyl coenzyme A lyase;
            (+)-CMA-CoA lyase;
            (3S)-citramalyl-CoA pyruvate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     (3S)-citramalyl-CoA pyruvate-lyase (acetyl-CoA-forming)
REACTION    (3S)-citramalyl-CoA = acetyl-CoA + pyruvate [RN:R00237]
ALL_REAC    R00237
SUBSTRATE   (3S)-citramalyl-CoA [CPD:C01011]
PRODUCT     acetyl-CoA [CPD:C00024];
            pyruvate [CPD:C00022]
COMMENT     The enzyme is a component of EC 4.1.3.22 citramalate lyase. Also
            acts on (3S)-citramalyl thioacyl-carrier protein.
REFERENCE   1  [PMID:4284209]
  AUTHORS   Cooper RA, Kornberg HL.
  TITLE     The utilization of itaconate by Pseudomonas sp.
  JOURNAL   Biochem. J. 91 (1964) 82-91.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:923590]
  AUTHORS   Dimroth P, Buckel W, Loyal R, Eggerer H.
  TITLE     Isolation and function of the subunits of citramalate lyase and
            formation of hybrids with the subunits of citrate lyase.
  JOURNAL   Eur. J. Biochem. 80 (1977) 469-77.
  ORGANISM  Clostridium tetanomorphum
PATHWAY     PATH: map00620  Pyruvate metabolism
            PATH: map00660  C5-Branched dibasic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.25
            ExPASy - ENZYME nomenclature database: 4.1.3.25
            ExplorEnz - The Enzyme Database: 4.1.3.25
            ERGO genome analysis and discovery system: 4.1.3.25
            BRENDA, the Enzyme Database: 4.1.3.25
            CAS: 37290-68-9
///
ENTRY       EC 4.1.3.26                 Enzyme
NAME        3-hydroxy-3-isohexenylglutaryl-CoA lyase;
            beta-hydroxy-beta-isohexenylglutaryl CoA-lyase;
            hydroxyisohexenylglutaryl-CoA:acetatelyase;
            3-hydroxy-3-isohexenylglutaryl coenzyme A lyase;
            3-hydroxy-3-isohexenylglutaryl-CoA isopentenylacetoacetyl-CoA-lyase;
            3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA acetate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA acetate-lyase
            (7-methyl-3-oxooct-6-enoyl-CoA-forming)
REACTION    3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA =
            7-methyl-3-oxooct-6-enoyl-CoA + acetate [RN:R04287]
ALL_REAC    R04287
SUBSTRATE   3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA [CPD:C04675]
PRODUCT     7-methyl-3-oxooct-6-enoyl-CoA;
            acetate [CPD:C00033]
COMMENT     Also acts on the hydroxy derivative of farnesoyl-CoA.
REFERENCE   1  [PMID:14339651]
  AUTHORS   SEUBERT W, FASS E.
  TITLE     [STUDIES ON THE BACTERIAL DEGRADATION OF ISOPRENOIDS. IV. THE
            PURIFICATION AND PROPERTIES OF
            BETA-ISOHEXENYLGLUTACONYL-COA-HYDRATASE AND
            BETA-HYDROXY-BETA-ISOHEXENYLGLUTARYL-COA-LYASE.]
  JOURNAL   Biochem. Z. 341 (1964) 23-34.
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.26
            ExPASy - ENZYME nomenclature database: 4.1.3.26
            ExplorEnz - The Enzyme Database: 4.1.3.26
            ERGO genome analysis and discovery system: 4.1.3.26
            BRENDA, the Enzyme Database: 4.1.3.26
            CAS: 37290-69-0
///
ENTRY       EC 4.1.3.27                 Enzyme
NAME        anthranilate synthase;
            anthranilate synthetase;
            chorismate lyase;
            chorismate pyruvate-lyase (amino-accepting)
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     chorismate pyruvate-lyase (amino-accepting; anthranilate-forming)
REACTION    chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
            [RN:R00986]
ALL_REAC    R00986;
            (other) R00985
SUBSTRATE   chorismate [CPD:C00251];
            L-glutamine [CPD:C00064]
PRODUCT     anthranilate [CPD:C00108];
            pyruvate [CPD:C00022];
            L-glutamate [CPD:C00025]
COMMENT     In some organisms, this enzyme is part of a multifunctional protein,
            together with one or more other components of the system for the
            biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate
            phosphoribosyltransferase ), EC 4.1.1.48
            (indole-3-glycerol-phosphate synthase), EC 4.2.1.20 (tryptophan
            synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)].
            The native enzyme in the complex uses either glutamine or, less
            efficiently, NH3. The enzyme separated from the complex uses NH3
            only.
REFERENCE   1  [PMID:5333199]
  AUTHORS   Baker TI, Crawford IP.
  TITLE     Anthranilate synthetase. Partial purification and some kinetic
            studies on the enzyme from Escherichia coli.
  JOURNAL   J. Biol. Chem. 241 (1966) 5577-84.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Creighton, T.E. and Yanofsky, C.
  TITLE     Chorismate to tryptophan (Escherichia coli) - Anthranilate
            synthetase, PR transferase, PRA isomerase, InGP synthetase,
            tryptophan synthetase.
  JOURNAL   Methods Enzymol. 17A (1970) 365-380.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:16526091]
  AUTHORS   Kung CC, Huang WN, Huang YC, Yeh KC.
  TITLE     Proteomic survey of copper-binding proteins in Arabidopsis roots by
            immobilized metal affinity chromatography and mass spectrometry.
  JOURNAL   Proteomics. 6 (2006) 2746-58.
REFERENCE   4  [PMID:4886290]
  AUTHORS   Ito J, Yanofsky C.
  TITLE     Anthranilate synthetase, an enzyme specified by the tryptophan
            operon of Escherichia coli: Comparative studies on the complex and
            the subunits.
  JOURNAL   J. Bacteriol. 97 (1969) 734-42.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:4878701]
  AUTHORS   Zalkin H, Kling D.
  TITLE     Anthranilate synthetase. Purification and properties of component I
            from Salmonella typhimurium.
  JOURNAL   Biochemistry. 7 (1968) 3566-73.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
            PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K01656  anthranilate synthase
            KO: K01657  anthranilate synthase component I
            KO: K01658  anthranilate synthase component II
GENES       ATH: AT3G55870 AT5G05730(ASA1)
            OSA: 4332341 4333918 4334640 4336076
            CME: CMN228C
            SCE: YER090W(TRP2) YKL211C(TRP3)
            AGO: AGOS_ABR209W AGOS_AER446W
            PIC: PICST_74393(ABZ1) PICST_85710(TRP2) PICST_91065(TRP6)
            CAL: CaO19_2546(CaO19.2546)
            CGR: CAGL0F00253g CAGL0I05016g
            SPO: SPBC1539.09c(trp1) SPCC1442.09
            ANI: AN3695.2
            AFM: AFUA_1G13090 AFUA_6G12580
            AOR: AO090003000371 AO090012000581
            ANG: An08g06080(trpC)
            CNE: CNF03410 CNI00560
            UMA: UM00304.1 UM02376.1
            TAN: TA12230
            ECO: b1263(trpD) b1264(trpE)
            ECJ: JW1255(trpD) JW1256(trpE)
            ECE: Z2546m Z2548(trpD)
            ECS: ECs1835 ECs1836
            ECC: c1729(trpD) c1730(trpE)
            ECI: UTI89_C1532(trpD) UTI89_C1533(trpE) UTI89_C2178(ybtS)
            ECP: ECP_1311 ECP_1312
            ECV: APECO1_424(trpD) APECO1_425(trpE)
            ECW: EcE24377A_1462(trpD) EcE24377A_1463(trpE)
            ECX: EcHS_A1372(trpD) EcHS_A1373(trpE)
            STY: STY1327(trpD) STY1328(trpE)
            STT: t1635(trpE) t1636(trpD)
            SPT: SPA1153(trpD) SPA1154(trpE)
            SEC: SC1719(trpE) SC1720(trpD)
            STM: STM1723(trpE) STM1724(trpD)
            YPE: YPO2207(trpG) YPO2208(trpE)
            YPK: y2051(trpE)
            YPM: YP_2005(trpG) YP_2006(trpE2)
            YPA: YPA_1567 YPA_1568
            YPN: YPN_1676 YPN_1677
            YPP: YPDSF_0925
            YPS: YPTB1601(ybtS) YPTB2129(trpG) YPTB2130(trpE)
            YPI: YpsIP31758_1932(trpE) YpsIP31758_1933(trpG)
            SFL: SF1266(trpD) SF1267(trpE)
            SFX: S1352(trpD) S1353(trpE)
            SFV: SFV_1277(trpD) SFV_1278(trpE)
            SSN: SSON_1879(trpE) SSON_1880(trpD)
            SBO: SBO_1802(trpE) SBO_1803(trpD)
            SDY: SDY_1331(trpD) SDY_1332(trpE)
            ECA: ECA2296(trpE) ECA2297(trpG)
            PLU: plu2462(trpE) plu2463(trpG)
            BUC: BUpT01(trpE) BUpT02(trpG) BUpT03(trpE2) BUpT04(trpG2)
            BAB: bbp525(trpG) bbp526(trpE)
            SGL: SG1401 SG1402
            ENT: Ent638_2204
            KPN: KPN_01257(trpE)
            BFL: Bfl426(trpE) Bfl427(trpG)
            BPN: BPEN_438(trpE) BPEN_439(trpG)
            HIN: HI1171(trpG) HI1387(trpE) HI1388(trpG)
            HIT: NTHI1339(trpG2) NTHI1767(trpG) NTHI1768(trpE)
            HIQ: CGSHiGG_00705
            HDU: HD0406(trpG)
            HSO: HS_0130(trpG)
            PMU: PM0583(trpG_1) PM0584(trpE) PM1463(trpG_2)
            MSU: MS1149(trpE) MS1150(pabA) MS2194(pabA)
            APL: APL_1147(trpG) APL_1163(trpE) APL_1164(trpG)
            XFA: XF0210 XF0211 XF0674 XF1914 XF1915
            XFT: PD0170(trpE) PD0171(trpD) PD0876(trpD) PD1500(trpE)
            XCC: XCC0459(trpE) XCC0467(trpG) XCC1021(trpE)
            XCB: XC_0473 XC_0481 XC_3224
            XCV: XCV0505(trpE) XCV0514(trpG) XCV1149(trpE)
            XAC: XAC0476(trpE) XAC0478(trpG) XAC1130(trpE)
            XOO: XOO0884(trpE) XOO4049(trpE) XOO4163(trpG)
            XOM: XOO_0809(XOO0809) XOO_3824(XOO3824) XOO_3938(XOO3938)
            VCH: VC1173 VC1174
            VCO: VC0395_A0795(trpG) VC0395_A0796(trpE)
            VVU: VV1_3064 VV1_3065
            VVY: VV1220 VV1221
            VPA: VP1956 VP1957
            VFI: VF1032 VF1033 VF2285
            PPR: PBPRA2486 PBPRA2487
            PAE: PA0609(trpE) PA0649(trpG) PA1001(phnA) PA1002(phnB)
            PAU: PA14_07940(trpE) PA14_08340(trpG) PA14_51350(phnB)
                 PA14_51360(phnA)
            PAP: PSPA7_0753(trpE2) PSPA7_4397(trpE1)
            PPU: PP_0417(trpE) PP_0420(trpG)
            PPF: Pput_0451
            PST: PSPTO_0568(trpE) PSPTO_0592(trpG)
            PSB: Psyr_4581 Psyr_4609
            PSP: PSPPH_0649(trpE) PSPPH_0672(trpG) PSPPH_2477
            PFL: PFL_5623(trpG) PFL_5629(trpE)
            PFO: Pfl_5115 Pfl_5118
            PEN: PSEEN0444(trpE) PSEEN0447(trpG) PSEEN4392(guaA)
            PMY: Pmen_3997
            PAR: Psyc_0974(trpG) Psyc_1667(trpE) Psyc_1668
            PCR: Pcryo_1441 Pcryo_1923
            PRW: PsycPRwf_1154
            ACI: ACIAD0297(trpE) ACIAD2461(trpG)
            SON: SO_3019(trpE) SO_3020(trpG)
            SDN: Sden_2450 Sden_2451
            SFR: Sfri_1428 Sfri_1429
            SAZ: Sama_2129
            SBL: Sbal_2701
            SLO: Shew_2251
            SPC: Sputcn32_2403
            SSE: Ssed_1686
            SHE: Shewmr4_1461 Shewmr4_1462
            SHM: Shewmr7_1527 Shewmr7_1528
            SHN: Shewana3_1519 Shewana3_1520
            SHW: Sputw3181_1605
            ILO: IL1751(trpE) IL1752
            CPS: CPS_0638(pabA) CPS_3522(trpE) CPS_3523(trpG)
            PHA: PSHAa0192(pabA) PSHAa1292(trpG) PSHAa1293(trpE)
            PAT: Patl_2829
            SDE: Sde_0747 Sde_0752
            PIN: Ping_1060
            MAQ: Maqu_3517
            CBU: CBU_1152(trpE)
            CBD: COXBU7E912_1249(trpE)
            LPN: lpg0835(pabA) lpg1734
            LPF: lpl0866(trpG) lpl1698(trpE)
            LPP: lpp0897(trpG) lpp1699(trpE)
            MCA: MCA2584(trpE) MCA2585(trpG)
            FTU: FTT0946(trpG) FTT1802c(trpE)
            FTF: FTF0946(trpG1) FTF1802c(trpE)
            FTW: FTW_0840 FTW_2024(trpG) FTW_2025(trpE)
            FTL: FTL_1261 FTL_1966
            FTH: FTH_1236(trpG1) FTH_1237(trpE1) FTH_1882(trpG2)
                 FTH_1883(trpE2)
            FTA: FTA_2079 FTA_2080(trpE)
            FTN: FTN_0823(pabA) FTN_1777(trpG) FTN_1778(trpE)
            TCX: Tcr_0266 Tcr_0267 Tcr_0715
            NOC: Noc_2494 Noc_2495
            AEH: Mlg_2250
            HHA: Hhal_2082
            HCH: HCH_06125(trpE) HCH_06126
            CSA: Csal_2323
            ABO: ABO_2026(trpG) ABO_2027(trpE)
            MMW: Mmwyl1_0660
            AHA: AHA_2923(trpE) AHA_2924
            RMA: Rmag_0518 Rmag_0809
            NME: NMB0966 NMB1021
            NMA: NMA1163(trpG) NMA1247(trpE)
            NMC: NMC0947(trpG) NMC1013(trpE)
            NGO: NGO0872(trpE) NGO1204
            CVI: CV_0568 CV_2175(pabA) CV_2179(trpE) CV_3411(pabB)
            RSO: RSc2881(trpE) RSc2882(trpG)
            REU: Reut_A3023 Reut_A3024
            REH: H16_A3319(trpE) H16_A3320(trpG)
            RME: Rmet_3178 Rmet_3179
            BMA: BMAA0532(trpG) BMAA0533(trpE)
            BXE: Bxe_A0460 Bxe_A0461 Bxe_A0954
            BVI: Bcep1808_0511
            BUR: Bcep18194_A3620 Bcep18194_A3621 Bcep18194_B1570
            BCN: Bcen_2571 Bcen_2572
            BCH: Bcen2424_0533 Bcen2424_0534
            BAM: Bamb_0438 Bamb_0439
            BPS: BPSL3050(trpE) BPSL3051(trpG)
            BPM: BURPS1710b_2789 BURPS1710b_3575(trpE) BURPS1710b_3576(trpG)
                 BURPS1710b_A2023
            BPL: BURPS1106A_A0637
            BPD: BURPS668_A0729
            BTE: BTH_I2909(trpE) BTH_I2910
            PNU: Pnuc_0148
            BPE: BP3263(trpG) BP3264(trpE)
            BPA: BPP4156(trpE) BPP4157(trpG)
            BBR: BB4626(trpE) BB4627(trpG)
            RFR: Rfer_3605 Rfer_3607
            POL: Bpro_4455 Bpro_4457
            PNA: Pnap_3654
            AAV: Aave_0442
            AJS: Ajs_0366
            VEI: Veis_1212
            MPT: Mpe_A3462 Mpe_A3463
            HAR: HEAR0199(trpG) HEAR0200(trpE)
            MMS: mma_0234(trpG) mma_0235(trpE)
            NEU: NE0014(trpG) NE2150(trpE)
            NET: Neut_0135 Neut_2098
            NMU: Nmul_A2369 Nmul_A2564
            EBA: ebA4177(trpE) ebA4199(pabA)
            AZO: azo2275 azo3324(trpG) azo3325(trpE)
            DAR: Daro_3477 Daro_3481
            TBD: Tbd_1546 Tbd_2224 Tbd_2228
            MFA: Mfla_2468 Mfla_2471
            HPY: HP1281(trpD) HP1282(trpE)
            HPJ: jhp1202(trpG) jhp1203(trpE)
            HPA: HPAG1_1230 HPAG1_1231
            HHE: HH0303(trpG) HH0314(trpD) HH0315(trpE_2)
            HAC: Hac_0017(trpG) Hac_0018(trpE)
            WSU: WS0088 WS2172
            TDN: Tmden_0568 Tmden_1277
            CJE: Cj0345(trpE) Cj0346(trpD)
            CJR: CJE0394(trpE) CJE0395(trpD)
            CJJ: CJJ81176_0369(trpE) CJJ81176_0370(trpD)
            CJU: C8J_0322(trpE) C8J_0323(trpD)
            CJD: JJD26997_1613(trpD) JJD26997_1614(trpE)
            CFF: CFF8240_0350 CFF8240_0351
            CCV: CCV52592_1683 CCV52592_1684 CCV52592_1709
            CCO: CCC13826_0023 CCC13826_0523(trpE) CCC13826_1602
            ABU: Abu_0651(trpE) Abu_2004(trpG)
            NIS: NIS_1180(trpE)
            SUN: SUN_0471
            GSU: GSU2382(trpG) GSU2383(trpE)
            GME: Gmet_2496 Gmet_2497
            GUR: Gura_1731
            PCA: Pcar_0730 Pcar_0731
            PPD: Ppro_1582
            DVU: DVU0364(pabA) DVU0465 DVU0466(trpG)
            DVL: Dvul_2472
            DDE: Dde_3483 Dde_3484 Dde_3617 Dde_3618
            BBA: Bd0234
            DPS: DP1619 DP1620
            ADE: Adeh_3888 Adeh_4052 Adeh_4053
            AFW: Anae109_0376
            SAT: SYN_01946 SYN_01947
            SFU: Sfum_1775 Sfum_1776
            PUB: SAR11_0832(trpG) SAR11_0924(trpGD) SAR11_0925(trpE)
            MLO: mlr2774
            MES: Meso_2199
            PLA: Plav_3169
            SME: SMc02725(trpE)
            ATU: Atu2289(trpE(G))
            ATC: AGR_C_4162
            RET: RHE_CH03075(trpE) RHE_CH03620
            BME: BMEI0449 BMEII0314
            BMF: BAB1_1586
            BMS: BR1570(trpE)
            BMB: BruAb1_1558(trpE)
            BOV: BOV_1516
            BJA: blr2489(trpE)
            BRA: BRADO1991(trpE(G))
            BBT: BBta_2309(trpE(G))
            RPA: RPA4498(trpG)
            RPB: RPB_4318
            RPC: RPC_4388
            RPD: RPD_2897 RPD_4213
            RPE: RPE_4447
            NWI: Nwi_0951 Nwi_2614
            NHA: Nham_1044
            XAU: Xaut_3582 Xaut_4378
            CCR: CC_1895 CC_1897
            SIL: SPO2146(trpE) SPO2149(trpG)
            SIT: TM1040_1141 TM1040_1143
            RSP: RSP_0244 RSP_2002(trpG) RSP_2004(trpE)
            RSH: Rsph17029_0714
            RSQ: Rsph17025_3101
            JAN: Jann_1882
            RDE: RD1_3205(trpE) RD1_3209(trpG) RD1_3323
            PDE: Pden_2132
            MMR: Mmar10_1401 Mmar10_1403
            HNE: HNE_1789(trpG) HNE_1790(trpE)
            ZMO: ZMO0114(trpGD) ZMO0201(trpG) ZMO0468(trpE)
            NAR: Saro_2021 Saro_2022
            SAL: Sala_0837 Sala_1174
            SWI: Swit_2352
            ELI: ELI_06485 ELI_06505
            GOX: GOX2286
            GBE: GbCGDNIH1_0821 GbCGDNIH1_0824
            ACR: Acry_1234
            RRU: Rru_A1132 Rru_A1891 Rru_A1895 Rru_A3546
            MAG: amb1813 amb2861
            MGM: Mmc1_1121 Mmc1_1122
            ABA: Acid345_4120
            BSU: BG10138(pabA) BG10287(trpE)
            BHA: BH0091(pabA) BH1659(trpE)
            BAN: BA0069(pabA-1) BA1248(trpE) BA1249(pabA-2)
            BAR: GBAA0069(pabA-1) GBAA1248(trpE) GBAA1249(pabA-2)
            BAA: BA_0659 BA_1781 BA_1782
            BAT: BAS0069 BAS1156 BAS1157
            BCE: BC0077 BC1232 BC1233
            BCA: BCE_0068(pabA) BCE_1356(trpE) BCE_1357(pabA)
            BCZ: BCZK0065(pabA) BCZK1130(trpE) BCZK1131(pabA)
            BCY: Bcer98_0064
            BTK: BT9727_0065(pabA) BT9727_1136(trpE) BT9727_1137(pabA)
            BTL: BALH_0068(pabA) BALH_1095
            BLI: BL00859(pabA) BL02775(trpE)
            BLD: BLi00091(pabA) BLi02403(trpE)
            BCL: ABC0111(pabA) ABC1895(trpE)
            BAY: RBAM_020840(trpE)
            BPU: BPUM_0058 BPUM_0059 BPUM_1999(trpE)
            OIH: OB0526 OB0527
            GKA: GK0067 GK2204(trpE)
            SAU: SA0668 SA1199 SA1200(trpG)
            SAV: SAV0713 SAV1367 SAV1368(trpG)
            SAM: MW0675 MW1254 MW1255(trpG)
            SAR: SAR0766 SAR1380(trpE) SAR1381(trpG)
            SAS: SAS0678 SAS1307 SAS1308
            SAC: SACOL0773(pabA) SACOL1403(trpE) SACOL1404(trpG)
            SAB: SAB0662 SAB0663 SAB0664 SAB1222(trpE) SAB1223(trpG)
            SAA: SAUSA300_0698(pabA) SAUSA300_1262(trpE) SAUSA300_1263(trpG)
            SAO: SAOUHSC_00722 SAOUHSC_01366 SAOUHSC_01367
            SAJ: SaurJH9_1428
            SAH: SaurJH1_1457
            SEP: SE0488 SE1048 SE1049
            SER: SERP0374(pabA) SERP0937(trpE) SERP0938(trpG)
            SHA: SH1541(trpG) SH1542 SH2185
            SSP: SSP1378 SSP1379 SSP2007
            LMO: lmo1632(trpG) lmo1633(trpE)
            LMF: LMOf2365_1654(trpG) LMOf2365_1655(trpE)
            LIN: lin1673(trpG) lin1674(trpE)
            LWE: lwe1648(trpG) lwe1649(trpE) lwe1814
            LLA: L0053(trpG) L0054(trpE)
            LLC: LACR_1559 LACR_1560 LACR_C06
            LLM: llmg_1030(trpE) llmg_1031(trpG)
            SPY: SPy_1991(trpG)
            SPZ: M5005_Spy_1698(trpG)
            SPM: spyM18_2057
            SPG: SpyM3_1713(trpG)
            SPS: SPs1713
            SPH: MGAS10270_Spy1766(trpG)
            SPI: MGAS10750_Spy1790(trpG)
            SPJ: MGAS2096_Spy1725(trpG)
            SPK: MGAS9429_Spy1703(trpG)
            SPF: SpyM51668(trpG)
            SPA: M6_Spy1704
            SPB: M28_Spy1683(trpG)
            SPN: SP_1816 SP_1817
            SPR: spr1636(trpG) spr1637(trpE)
            SPD: SPD_1601(trpG) SPD_1602(trpE)
            SAG: SAG0462(trpG)
            SAN: gbs0509
            SAK: SAK_0563
            SMU: SMU.532(trpE) SMU.533(trpG)
            STC: str1592(trpG) str1593(trpE)
            STL: stu1592(trpG) stu1593(trpE)
            SSA: SSA_0632(trpE) SSA_0633(trpG)
            SGO: SGO_0167 SGO_0657(trpE) SGO_0658
            LPL: lp_1652(trpE) lp_1653(trpG)
            STH: STH1407 STH1408 STH580
            CAC: CAC3162(pabA) CAC3163(parB)
            CPE: CPE1016(pabA)
            CPF: CPF_1271(pabA)
            CPR: CPR_1093(pabA)
            CNO: NT01CX_0379 NT01CX_0380
            CTH: Cthe_0875
            CBE: Cbei_1749 Cbei_4119
            CKL: CKL_1274(trpE) CKL_1275(trpG)
            AMT: Amet_1077 Amet_2158
            CHY: CHY_1586(trpG) CHY_1587(trpE) CHY_1931(pabA)
            DSY: DSY3202
            DRM: Dred_0248
            SWO: Swol_0364
            CSC: Csac_0729 Csac_2236
            TTE: TTE1582(pabA) TTE1583(trpE)
            MTA: Moth_1341 Moth_1342 Moth_2108
            MTU: Rv1609(trpE)
            MTC: MT1644(trpE)
            MBO: Mb1635(trpE)
            MBB: BCG_0013(trpG_1) BCG_0043(trpG_2) BCG_1647(trpE)
            MLE: ML1269(trpE)
            MPA: MAP1303(trpE)
            MAV: MAV_0018 MAV_3177(trpE)
            MSM: MSMEG_0029 MSMEG_3217(trpE)
            MVA: Mvan_2814
            MGI: Mflv_3602
            MMC: Mmcs_3053
            MKM: Mkms_3112
            MJL: Mjls_3069
            CGL: NCgl0955(cgl0997) NCgl2927(cgl3029) NCgl2928(cgl3031)
            CGB: cg1134(pabAB) cg3359(trpE) cg3360(trpG)
            CEF: CE1059 CE2868(trpE) CE2869(trpG)
            CDI: DIP2352(trpE) DIP2353(trpG)
            CJK: jk0795(trpE)
            NFA: nfa16010(pabB) nfa18580(trpE)
            RHA: RHA1_ro01016(trpE) RHA1_ro03695(trpG) RHA1_ro06106
                 RHA1_ro06665
            SCO: SCO2043(SC4G6.12c) SCO3213(SCE8.06c) SCO3214(SCE8.07c)
            SMA: SAV1178(pabAB) SAV6171(trpE)
            TWH: TWT386(trpE)
            TWS: TW384(trpE)
            LXX: Lxx11250(trpE) Lxx12360(trpE)
            CMI: CMM_1546(trpE2) CMM_1767(trpE1)
            ART: Arth_1684
            AAU: AAur_0027 AAur_1835(trpE)
            TFU: Tfu_1386 Tfu_1666
            FRA: Francci3_3020
            FAL: FRAAL2126(trpE) FRAAL3440 FRAAL4650(trpE) FRAAL4972(trpE)
            ACE: Acel_1071
            SEN: SACE_2689(trpE) SACE_4036(pabAB) SACE_5354 SACE_5753(trpE)
            STP: Strop_3175
            BAD: BAD_0789(trpE)
            RXY: Rxyl_2096 Rxyl_2115
            FNU: FN0218 FN0505 FN1731
            RBA: RB3936(trpG) RB6300(trpG) RB7967(trpE)
            LIL: LA3628(trpE) LA3629(trpG)
            LIC: LIC10581(trpG) LIC10582(trpE)
            LBJ: LBJ_2858(trpG) LBJ_2859(trpE)
            LBL: LBL_0212(trpE) LBL_0213(trpG)
            SYN: slr0055(trpG) slr0738(trpE) slr1979(trpE)
            SYW: SYNW2045(trpE)
            SYC: syc0542_c(trpE) syc1115_d(trpG)
            SYF: Synpcc7942_0400 Synpcc7942_1003
            SYD: Syncc9605_0398
            SYE: Syncc9902_1931
            SYG: sync_0462
            SYR: SynRCC307_2088(trpE)
            SYX: SynWH7803_0456(trpE) SynWH7803_2470(trpE)
            CYA: CYA_2136(trpE) CYA_2654(trpG)
            CYB: CYB_0535(trpE) CYB_2417(trpG)
            TEL: tll1672(trpE) tlr0285(trpE) tlr1471(trpG)
            GVI: gll0757(trpE) glr0883(trpG) glr1717(trpE)
            ANA: all0269(trpG) all0328 all0414(trpE) alr3233(trpE) alr3443
            AVA: Ava_2780 Ava_3468 Ava_4721 Ava_4890
            PMA: Pro1732(trpE)
            PMM: PMM1577(trpE)
            PMT: PMT1711(trpE)
            PMN: PMN2A_1149
            PMI: PMT9312_1669 PMT9312_1785
            PMB: A9601_02021(pabA) A9601_17841
            PMC: P9515_02131(pabA) P9515_17641
            PMF: P9303_22721 P9303_27421(pabA)
            PMG: P9301_02041(pabA) P9301_17681
            PMH: P9215_18491(trpE)
            PME: NATL1_02601(pabA) NATL1_20231
            TER: Tery_3792
            BTH: BT_0531 BT_0532
            BFR: BF2651 BF2652
            BFS: BF2673(trpE) BF2674(trpG) BF2675(trpD)
            PGI: PG0713(trpG)
            SRU: SRU_1662(trpE) SRU_1665
            CHU: CHU_3290(trpE) CHU_3291(trpG)
            GFO: GFO_2154(trpE) GFO_2668(trpE) GFO_2669(trpG)
            FJO: Fjoh_4890
            FPS: FP0512(pabA) FP0513(trpE)
            CTE: CT1448(trpE) CT1565(pabA)
            CCH: Cag_0298 Cag_0422 Cag_0493
            CPH: Cpha266_1856
            PLT: Plut_0356 Plut_1468
            DET: DET1481(trpE) DET1482(trpG)
            DEH: cbdb_A1441(trpE) cbdb_A1442(trpG)
            DEB: DehaBAV1_1271
            RRS: RoseRS_1455
            RCA: Rcas_2156
            DRA: DR_0196 DR_1766 DR_1791
            DGE: Dgeo_0498 Dgeo_0983 Dgeo_0985
            TTH: TTC0255 TTC1492 TTC1493
            TTJ: TTHA0620 TTHA1843 TTHA1844
            AAE: aq_549(trpG) aq_582(trpE)
            TMA: TM0141 TM0142
            TPT: Tpet_0783
            MJA: MJ0238(trpG) MJ1075(trpE)
            MMP: MMP1005(trpG) MMP1006(trpE)
            MMQ: MmarC5_0588
            MMZ: MmarC7_0248
            MAE: Maeo_1117
            MVN: Mevan_0331
            MAC: MA2986(trpG) MA2987(trpE)
            MBA: Mbar_A3626 Mbar_A3627
            MMA: MM_2817 MM_2818
            MBU: Mbur_2365 Mbur_2366
            MTP: Mthe_1541
            MHU: Mhun_1785 Mhun_1786
            MEM: Memar_0071
            MBN: Mboo_0228
            MTH: MTH1655(trpE) MTH1656(trpG)
            MST: Msp_1070(trpE) Msp_1071(trpG)
            MSI: Msm_1145 Msm_1146
            MKA: MK0436(pabA) MK0437(trpE)
            AFU: AF1602(trpG) AF1603(trpE)
            HAL: VNG0384G(trpE2) VNG0386Gm(trpG2) VNG1646G(trpG1)
                 VNG1647G(trpE1)
            HMA: pNG7325(trpG2) pNG7327(trpE3) rrnAC0709(trpE1)
                 rrnAC0710(trpD2) rrnAC1517(trpG1) rrnAC1518(trpE2)
            HWA: HQ1783A(trpG) HQ1784A(trpE) HQ3166A(trpG) HQ3167A(trpE)
            NPH: NP0800A(trpG_2) NP0802A(trpE_2) NP3342A(trpE_1)
                 NP3344A(trpG_1)
            TAC: Ta0806m Ta0807
            TVO: TVN1023 TVN1024
            PTO: PTO0341 PTO0342
            PAB: PAB2045(trpE) PAB2046(trpG)
            PFU: PF1708 PF1709
            TKO: TK0254 TK0255
            RCI: RCIX796(trpGD) RCIX797(trpE)
            APE: APE_2553.1 APE_2555
            IHO: Igni_0925
            SSO: SSO0893(trpE) SSO0894(trpGD)
            STO: ST1228 ST1229
            SAI: Saci_1425(trpE) Saci_1426(trpGD)
            MSE: Msed_1687
            PAI: PAE2459 PAE2460
            PIS: Pisl_0268 Pisl_1914
            PCL: Pcal_0912 Pcal_1209
            PAS: Pars_0846 Pars_1420
STRUCTURES  PDB: 1I1Q  1I7Q  1I7S  1QDL  2I6Y  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.27
            ExPASy - ENZYME nomenclature database: 4.1.3.27
            ExplorEnz - The Enzyme Database: 4.1.3.27
            ERGO genome analysis and discovery system: 4.1.3.27
            BRENDA, the Enzyme Database: 4.1.3.27
            CAS: 9031-59-8
///
ENTRY       EC 4.1.3.28       Obsolete  Enzyme
NAME        Transferred to 2.3.3.3
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.3.3.3, citrate (Re)-synthase (EC
            4.1.3.28 created 1972, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.28
            ExPASy - ENZYME nomenclature database: 4.1.3.28
            ExplorEnz - The Enzyme Database: 4.1.3.28
            ERGO genome analysis and discovery system: 4.1.3.28
            BRENDA, the Enzyme Database: 4.1.3.28
///
ENTRY       EC 4.1.3.29       Obsolete  Enzyme
NAME        Transferred to 2.3.3.4
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.3.3.4 decylhomocitrate synthase (EC
            4.1.3.29 created 1976, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.29
            ExPASy - ENZYME nomenclature database: 4.1.3.29
            ExplorEnz - The Enzyme Database: 4.1.3.29
            ERGO genome analysis and discovery system: 4.1.3.29
            BRENDA, the Enzyme Database: 4.1.3.29
///
ENTRY       EC 4.1.3.30                 Enzyme
NAME        methylisocitrate lyase;
            2-methylisocitrate lyase;
            MICL;
            (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase
            (succinate-forming)
REACTION    (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = succinate + pyruvate
            [RN:R00409]
ALL_REAC    R00409
SUBSTRATE   (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate [CPD:C04593]
PRODUCT     succinate [CPD:C00042];
            pyruvate [CPD:C00022]
COMMENT     The enzyme acts on threo-Ds-2-methylisocitrate, but not on
            threo-Ds-isocitrate, threo-DL-isocitrate or erythro-Ls-isocitrate.
REFERENCE   1
  AUTHORS   Tabuchi, T. and Satoh, T.
  TITLE     Distinction between isocitrate lyase and methylisocitrate lyase in
            Candida lipolytica.
  JOURNAL   Agric. Biol. Chem. 40 (1976) 1863-1869.
  ORGANISM  Candida lipolytica
REFERENCE   2
  AUTHORS   Tabuchi, T. and Satoh, T.
  TITLE     Purification and properties of methylisocitrate lyase, a key enzyme
            in propionate metabolism, from Candida lipolytica.
  JOURNAL   Agric. Biol. Chem. 41 (1977) 169-174.
  ORGANISM  Candida lipolytica
PATHWAY     PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K03417  methylisocitrate lyase
GENES       AFM: AFUA_2G00120 AFUA_2G00540 AFUA_2G03820 AFUA_4G02820
            UMA: UM01112.1
            ECO: b0331(prpB)
            ECJ: JW0323(prpB)
            ECE: Z0427(prpB)
            ECS: ECs0385
            ECC: c0451(prpB)
            ECI: UTI89_C0363(prpB)
            ECP: ECP_0407
            ECV: APECO1_1657(prpB)
            ECW: EcE24377A_0356(prpB)
            ECX: EcHS_A0397
            STY: STY0400(prpB)
            STT: t2496(prpB)
            SPT: SPA2355(prpB)
            SEC: SC0409(prpB)
            STM: STM0368(prpB)
            PLU: plu3542(prpB)
            XFA: XF1234
            XFT: PD0509(prpB)
            XCC: XCC1031(prpB)
            XCB: XC_3215
            XCV: XCV1156(prpB)
            XAC: XAC1137(prpB)
            XOO: XOO0892(prpB)
            XOM: XOO_0816(XOO0816)
            VCH: VC1336
            VCO: VC0395_A0952(prpB)
            VVU: VV1_2732
            VVY: VV1529
            VPA: VP1648
            PPR: PBPRB0235
            PAE: PA0796(prpB)
            PAU: PA14_53940(prpB)
            PAP: PSPA7_4722(prpB)
            PPU: PP_2334
            PST: PSPTO_2287(prpB)
            PSB: Psyr_2085
            PSP: PSPPH_2056(prpB)
            PFL: PFL_1861(prpB)
            PFO: Pfl_1764
            PEN: PSEEN1902(prpB)
            PAR: Psyc_1110(prpB)
            PCR: Pcryo_1311
            ACI: ACIAD2758
            ACB: A1S_0073
            SON: SO_0345(prpB)
            SDN: Sden_1664
            SFR: Sfri_1857
            SHE: Shewmr4_3629
            SHM: Shewmr7_0315
            SHN: Shewana3_3825
            ILO: IL1427(prpB)
            CPS: CPS_2822
            PHA: PSHAa1775(prpB)
            PAT: Patl_1419
            CBU: CBU_0771(prpB)
            CBD: COXBU7E912_0819(prpB)
            LPN: lpg0052
            LPF: lpl0052
            LPP: lpp0054
            NOC: Noc_2209
            AEH: Mlg_2605
            HCH: HCH_02710
            CSA: Csal_2421
            ABO: ABO_1433(prpB)
            AHA: AHA_2265(prpB)
            NME: NMB0430
            NMA: NMA2055(prpB)
            NGO: NGO1526
            RSO: RSp0122(prpB2)
            REU: Reut_A1808
            REH: H16_A1905(prpB)
            RME: Rmet_1587
            BMA: BMAA1870(prpB)
            BMV: BMASAVP1_0879(prpB)
            BML: BMA10299_1166(prpB)
            BMN: BMA10247_A2143(prpB)
            BUR: Bcep18194_B0141 Bcep18194_B0773 Bcep18194_B2560
            BCN: Bcen_5344
            BCH: Bcen2424_5517
            BPS: BPSS0206(prpB)
            BPM: BURPS1710b_A1735(prpB)
            BPL: BURPS1106A_A0288(prpB)
            BPD: BURPS668_A0382(prpB)
            BTE: BTH_II2189(prpB)
            BPE: BP2366(prpB)
            BPA: BPP3233(prpB)
            BBR: BB3685(prpB)
            POL: Bpro_1029
            NMU: Nmul_A0865
            ABU: Abu_0276(prpB)
            GME: Gmet_1122
            BBA: Bd2502
            PUB: SAR11_1155(prpB)
            RLE: RL0443
            BRA: BRADO4322
            BBT: BBta_5017
            BCZ: BCZK2113(prpB)
            MPA: MAP0296c
            MAV: MAV_0345(prpB)
            MSM: MSMEG_6646(prpB)
            CGL: NCgl0629(cgl0658) NCgl0665(cgl0695)
            CGB: cg0760(prpB2) cg0797(prpB1)
            CEF: CE0717
            CMI: CMM_2379(prpB)
            AAU: AAur_1661(prpB) AAur_pTC20151(prpB)
            FRA: Francci3_2655
            FAL: FRAAL5022(prpB)
            RXY: Rxyl_2400
            ANA: all1863
            AVA: Ava_4757
            TER: Tery_4268
            PTO: PTO0170
STRUCTURES  PDB: 1MUM  1O5Q  1OQF  1UJQ  1XG3  1XG4  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.30
            ExPASy - ENZYME nomenclature database: 4.1.3.30
            ExplorEnz - The Enzyme Database: 4.1.3.30
            ERGO genome analysis and discovery system: 4.1.3.30
            BRENDA, the Enzyme Database: 4.1.3.30
            CAS: 57827-77-7
///
ENTRY       EC 4.1.3.31       Obsolete  Enzyme
NAME        Transferred to 2.3.3.5
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.3.3.5 2-methylcitrate synthase (EC
            4.1.3.31 created 1978, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.31
            ExPASy - ENZYME nomenclature database: 4.1.3.31
            ExplorEnz - The Enzyme Database: 4.1.3.31
            ERGO genome analysis and discovery system: 4.1.3.31
            BRENDA, the Enzyme Database: 4.1.3.31
///
ENTRY       EC 4.1.3.32                 Enzyme
NAME        2,3-dimethylmalate lyase;
            2,3-dimethylmalate pyruvate-lyase;
            (2R,3S)-2,3-dimethylmalate pyruvate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     (2R,3S)-2,3-dimethylmalate pyruvate-lyase (propanoate-forming)
REACTION    (2R,3S)-2,3-dimethylmalate = propanoate + pyruvate [RN:R01355]
ALL_REAC    R01355
SUBSTRATE   (2R,3S)-2,3-dimethylmalate [CPD:C03652]
PRODUCT     propanoate [CPD:C00163];
            pyruvate [CPD:C00022]
REFERENCE   1  [PMID:527937]
  AUTHORS   Pirzer P, Lill U, Eggerer H.
  TITLE     Nicotinic acid metabolism. 2,3-Dimethylmalate lyase.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 360 (1979) 1693-702.
  ORGANISM  Clostridium barkeri
REFERENCE   2  [PMID:16894175]
  AUTHORS   Alhapel A, Darley DJ, Wagener N, Eckel E, Elsner N, Pierik AJ.
  TITLE     Molecular and functional analysis of nicotinate catabolism in
            Eubacterium barkeri.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 12341-6.
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.32
            ExPASy - ENZYME nomenclature database: 4.1.3.32
            ExplorEnz - The Enzyme Database: 4.1.3.32
            ERGO genome analysis and discovery system: 4.1.3.32
            BRENDA, the Enzyme Database: 4.1.3.32
            CAS: 73562-28-4
///
ENTRY       EC 4.1.3.33       Obsolete  Enzyme
NAME        Transferred to 2.3.3.6
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.3.3.6 2-ethylmalate synthase (EC
            4.1.3.33 created 1983, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.33
            ExPASy - ENZYME nomenclature database: 4.1.3.33
            ExplorEnz - The Enzyme Database: 4.1.3.33
            ERGO genome analysis and discovery system: 4.1.3.33
            BRENDA, the Enzyme Database: 4.1.3.33
///
ENTRY       EC 4.1.3.34                 Enzyme
NAME        citryl-CoA lyase;
            (3S)-citryl-CoA oxaloacetate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     (3S)-citryl-CoA oxaloacetate-lyase (acetyl-CoA-forming)
REACTION    (3S)-citryl-CoA = acetyl-CoA + oxaloacetate [RN:R00354]
ALL_REAC    R00354
SUBSTRATE   (3S)-citryl-CoA [CPD:C00566]
PRODUCT     acetyl-CoA [CPD:C00024];
            oxaloacetate [CPD:C00036]
COMMENT     The enzyme is a component of EC 4.1.3.6 {[citrate
            (pro-3S)-lyase]}and EC 2.3.3.8 [ATP citrate synthase]. Also acts on
            (3S)-citryl thioacyl-carrier protein.
REFERENCE   1  [PMID:336371]
  AUTHORS   Dimroth P, Loyal R, Eggerer H.
  TITLE     Characterization of the isolated transferase subunit of citrate
            lyase as a CoA-Transferase. Evidence against a covalent
            enzyme-substrate intermediate.
  JOURNAL   Eur. J. Biochem. 80 (1977) 479-88.
  ORGANISM  Klebsiellu aerogenes
REFERENCE   2  [PMID:6749502]
  AUTHORS   Lill U, Schreil A, Eggerer H.
  TITLE     Isolation of enzymically active fragments formed by limited
            proteolysis of ATP citrate lyase.
  JOURNAL   Eur. J. Biochem. 125 (1982) 645-50.
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
ORTHOLOGY   KO: K01660  citryl-CoA lyase
GENES       ECO: b0616(citE)
            ECJ: JW0608(citE)
            ECE: Z0760(citE)
            ECS: ECs0655
            ECC: c0706(citE)
            ECI: UTI89_C0620(citE)
            ECP: ECP_0647
            ECV: APECO1_1435(citE)
            STY: STY0671(citE)
            STT: t2245(citE)
            SPT: SPA2112(citE)
            SEC: SC0651(citE)
            STM: STM0622(citE)
            SFL: SF0533(citE)
            SFX: S0540(citE)
            SFV: SFV_0569(citE)
            SSN: SSON_0568(citE)
            SBO: SBO_0481(citE)
            SPE: Spro_3169
            HIN: HI0023(citE)
            HIT: NTHI0030(citE)
            HDU: HD1242(citE)
            VCH: VC0798
            PPR: PBPRA2293
            PFL: PFL_2651(citE)
            BUR: Bcep18194_B1721 Bcep18194_B2641 Bcep18194_C7154
            PNU: Pnuc_0539
            RFR: Rfer_4171
            VEI: Veis_1580 Veis_3048
            PPD: Ppro_1085
            ADE: Adeh_0181
            PLA: Plav_1428
            SME: SMc03793(citE)
            ATU: Atu2788(citE)
            ATC: AGR_C_5061
            RET: RHE_CH04088(citEch)
            RLE: RL4702(citE)
            BME: BMEII0413
            BMB: BruAb2_0351
            BRA: BRADO0361
            BBT: BBta_0347
            RPC: RPC_0233
            RPD: RPD_0606
            RPE: RPE_0340
            XAU: Xaut_1974
            SIL: SPO0352(citE)
            SIT: TM1040_3165 TM1040_3520
            RSP: RSP_0970
            RSH: Rsph17029_0417
            RSQ: Rsph17025_3162
            JAN: Jann_0816
            RDE: RD1_1001(citE) RD1_1620(citE)
            PDE: Pden_0563
            MMR: Mmar10_2882
            SAL: Sala_1535
            SWI: Swit_2975
            ABA: Acid345_2963
            SPZ: M5005_Spy_0906(citE)
            SPH: MGAS10270_Spy1020(citE)
            SPI: MGAS10750_Spy1056(citE)
            SPF: SpyM50891(citE)
            SPA: M6_Spy0895
            SPB: M28_Spy0879(citE)
            LPL: lp_1108(citE)
            CTC: CTC02467
            AMT: Amet_3410
            DSY: DSY1924
            MAV: MAV_2730
            MGI: Mflv_2209
            MMC: Mmcs_3986
            CGB: cg0985(citE)
            RHA: RHA1_ro00778
            NCA: Noca_4394
            TFU: Tfu_0341 Tfu_1285
            SEN: SACE_4398
            STP: Strop_0723
            RXY: Rxyl_0366 Rxyl_2830
            FNU: FN1379
            DGE: Dgeo_0359 Dgeo_1253
            HWA: HQ1720A(citE)
            NPH: NP4244A(citE)
            MSE: Msed_0381
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.34
            ExPASy - ENZYME nomenclature database: 4.1.3.34
            ExplorEnz - The Enzyme Database: 4.1.3.34
            ERGO genome analysis and discovery system: 4.1.3.34
            BRENDA, the Enzyme Database: 4.1.3.34
            CAS: 131095-35-7
///
ENTRY       EC 4.1.3.35                 Enzyme
NAME        (1-hydroxycyclohexan-1-yl)acetyl-CoA lyase;
            (1-hydroxycyclohexan-1-yl)acetyl-CoA cyclohexanone-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     (1-hydroxycyclohexan-1-yl)acetyl-CoA cyclohexanone-lyase
            (acetyl-CoA-forming)
REACTION    (1-hydroxycyclohexan-1-yl)acetyl-CoA = acetyl-CoA + cyclohexanone
            [RN:R02232]
ALL_REAC    R02232
SUBSTRATE   (1-hydroxycyclohexan-1-yl)acetyl-CoA [CPD:C04316]
PRODUCT     acetyl-CoA [CPD:C00024];
            cyclohexanone [CPD:C00414]
REFERENCE   1  [PMID:7076617]
  AUTHORS   Ougham HJ, Trudgill PW.
  TITLE     Metabolism of cyclohexaneacetic acid and cyclohexanebutyric acid by
            Arthrobacter sp. strain CA1.
  JOURNAL   J. Bacteriol. 150 (1982) 1172-82.
  ORGANISM  Arthrobacter sp.
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.35
            ExPASy - ENZYME nomenclature database: 4.1.3.35
            ExplorEnz - The Enzyme Database: 4.1.3.35
            ERGO genome analysis and discovery system: 4.1.3.35
            BRENDA, the Enzyme Database: 4.1.3.35
            CAS: 71343-09-4
///
ENTRY       EC 4.1.3.36                 Enzyme
NAME        naphthoate synthase;
            1,4-dihydroxy-2-naphthoate synthase;
            dihydroxynaphthoate synthase;
            o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing)
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing;
            CoA-forming)
REACTION    o-succinylbenzoyl-CoA = CoA + 1,4-dihydroxy-2-naphthoate [RN:R04150]
ALL_REAC    R04150;
            (other) R07263
SUBSTRATE   o-succinylbenzoyl-CoA [CPD:C03160]
PRODUCT     CoA [CPD:C00010];
            1,4-dihydroxy-2-naphthoate [CPD:C03657]
COMMENT     Highly specific.
REFERENCE   1  [PMID:2966501]
  AUTHORS   Kolkmann R, Leistner E.
  TITLE     4-(2'-Carboxyphenyl)-4-oxobutyryl coenzyme A ester, an intermediate
            in vitamin K2 (menaquinone) biosynthesis.
  JOURNAL   Z. Naturforsch. [C]. 42 (1987) 1207-14.
  ORGANISM  Mycobacterium phlei, Escherichia coli [GN:eco], Galium mollugo
REFERENCE   2  [PMID:500558]
  AUTHORS   Meganathan R, Bentley R.
  TITLE     Menaquinone (vitamin K2) biosynthesis: conversion of
            o-succinylbenzoic acid to 1,4-dihydroxy-2-naphthoic acid by
            Mycobacterium phlei enzymes.
  JOURNAL   J. Bacteriol. 140 (1979) 92-8.
  ORGANISM  Mycobacterium phlei
PATHWAY     PATH: map00130  Ubiquinone biosynthesis
ORTHOLOGY   KO: K01661  naphthoate synthase
GENES       ATH: AT1G60550
            OSA: 4327859
            ECO: b2262(menB)
            ECJ: JW2257(menB)
            ECE: Z3522(menB)
            ECS: ECs3150
            ECC: c2805(menB)
            ECI: UTI89_C2545(menB)
            ECP: ECP_2306
            ECV: APECO1_4299(menB)
            ECW: EcE24377A_2558(menB)
            ECX: EcHS_A2408
            STY: STY2537(menB)
            STT: t0556(menB)
            SPT: SPA0556(menB)
            SEC: SC2307(menB)
            STM: STM2307(menB)
            YPE: YPO2525(menB)
            YPK: y1662(menB)
            YPM: YP_2336(menB)
            YPA: YPA_2017
            YPN: YPN_2120
            YPS: YPTB2558(menB)
            YPI: YpsIP31758_1484(menB)
            SFL: SF2341(menB)
            SFX: S2475(menB)
            SFV: SFV_2333(menB)
            SSN: SSON_2323(menB)
            SBO: SBO_2299(menB)
            SDY: SDY_2458(menB)
            ECA: ECA1213(menB)
            PLU: plu3071(menB)
            HIN: HI0968(menB)
            HIT: NTHI1141(menB)
            HIP: CGSHiEE_07125
            HIQ: CGSHiGG_08420
            HDU: HD1925(menB)
            HSO: HS_0562(menB)
            PMU: PM1096(menB)
            MSU: MS1792(menB)
            APL: APL_1824(menB)
            VCH: VC1973
            VCO: VC0395_A1559(menB)
            VVU: VV1_3170
            VVY: VV1118
            VPA: VP0931
            VFI: VF1668 VF1669
            PPR: PBPRB1048 PBPRB1049
            SON: SO_4739(menB)
            SFR: Sfri_4030
            SHE: Shewmr4_3918
            SHM: Shewmr7_4010
            SHN: Shewana3_4123
            AHA: AHA_0529(menB)
            CVI: CV_1330
            REU: Reut_B3916 Reut_C6107
            REH: H16_B1695(menB)
            BXE: Bxe_C1035
            DAR: Daro_1616
            LIP: LI0807(menB)
            BBA: Bd3492(menB)
            DPS: DP0252(menB)
            MXA: MXAN_3154(menB)
            SAT: SYN_02400
            MES: Meso_2953
            RPC: RPC_1033
            RPE: RPE_0612
            BSU: BG10686(menB)
            BAN: BA5109(menB)
            BAR: GBAA5109(menB)
            BAA: BA_5527
            BAT: BAS4748
            BCE: BC4853
            BCA: BCE_5013(menB)
            BCZ: BCZK4608(menB)
            BTK: BT9727_4586(menB)
            BTL: BALH_4419(menB)
            BLI: BL02406(menB)
            BLD: BLi03220(menB)
            BAY: RBAM_027780
            BPU: BPUM_2716
            OIH: OB2323
            GKA: GK2873
            SAU: SA0898(menB)
            SAV: SAV1045(menB)
            SAM: MW0929(menB)
            SAR: SAR1019(menB)
            SAS: SAS0981
            SAC: SACOL1054(menB)
            SAB: SAB0912(menB)
            SAA: SAUSA300_0948(menB)
            SAO: SAOUHSC_00985
            SEP: SE0746
            SER: SERP0632(menB)
            SHA: SH1917(menB)
            SSP: SSP1746
            LMO: lmo1673(menB)
            LMF: LMOf2365_1697(menB)
            LIN: lin1781(menB)
            LWE: lwe1691(menB)
            LLA: L0171(menB)
            LLC: LACR_0771
            LLM: llmg_1831(menB)
            LSL: LSL_0174(menB)
            LBR: LVIS_0066
            EFA: EF0445(menB)
            OOE: OEOE_0279
            DSY: DSY0520(menB)
            MTU: Rv0548c(menB)
            MTC: MT0573(menB)
            MBO: Mb0562c(menB)
            MBB: BCG_0592c(menB)
            MLE: ML2263(menB)
            MPA: MAP4044c(menB)
            MAV: MAV_4596(menB)
            MSM: MSMEG_1075(menB) MSMEG_4114(menB)
            MMC: Mmcs_0735
            CGL: NCgl0446(cgl0463)
            CGB: cg0548(menB)
            CEF: CE0475 CE2780
            CDI: DIP0421(menB)
            CJK: jk1870(menB)
            NFA: nfa51380(menB)
            RHA: RHA1_ro02003 RHA1_ro02630 RHA1_ro11181(menB)
            TWH: TWT110(menB)
            TWS: TW120(menB)
            LXX: Lxx01440(menB)
            CMI: CMM_0576(menB)
            AAU: AAur_3275(menB)
            PAC: PPA0907
            TFU: Tfu_1409
            SEN: SACE_6914(menB)
            RXY: Rxyl_2893
            PCU: pc1064(menB)
            SYN: sll1127(menB)
            SYW: SYNW0998(menB)
            SYC: syc0926_d(menB)
            SYF: Synpcc7942_0597
            SYD: Syncc9605_1123
            SYE: Syncc9902_1333
            SYG: sync_1527(menB)
            SYR: SynRCC307_1141(menB)
            SYX: SynWH7803_1022(menB)
            CYA: CYA_0530(menB)
            CYB: CYB_0565(menB)
            TEL: tll2458(menB)
            ANA: all2347
            AVA: Ava_0166
            PMA: Pro1053(menB)
            PMM: PMM0608(menB)
            PMT: PMT0405(menB)
            PMN: PMN2A_0044
            PMI: PMT9312_0608
            PMB: A9601_06641(menB)
            PMC: P9515_06731(menB)
            PMF: P9303_18811(menB)
            PMG: P9301_06341(menB)
            PMH: P9215_06901
            PME: NATL1_06641(menB)
            TER: Tery_4088
            BTH: BT_4702
            BFR: BF1318
            BFS: BF1303(menB)
            PGI: PG1523(menB)
            SRU: SRU_2766(menB)
            CHU: CHU_1897(menB)
            GFO: GFO_2070(menB)
            FPS: FP0478(menB)
            CTE: CT1846(menB)
            CCH: Cag_1719
            PLT: Plut_0328
            HAL: VNG1079G(menB)
            HWA: HQ1874A(menB)
            NPH: NP2730A(menB)
STRUCTURES  PDB: 1Q51  1Q52  1RJM  1RJN  2IEX  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.36
            ExPASy - ENZYME nomenclature database: 4.1.3.36
            ExplorEnz - The Enzyme Database: 4.1.3.36
            ERGO genome analysis and discovery system: 4.1.3.36
            BRENDA, the Enzyme Database: 4.1.3.36
            CAS: 72506-71-9
///
ENTRY       EC 4.1.3.37       Obsolete  Enzyme
NAME        Transferred to 2.2.1.7
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
COMMENT     Transferred entry: now EC 2.2.1.7 1-deoxy-D-xylulose 5-phosphate
            synthase (EC 4.1.3.37 created 2001, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.37
            ExPASy - ENZYME nomenclature database: 4.1.3.37
            ExplorEnz - The Enzyme Database: 4.1.3.37
            ERGO genome analysis and discovery system: 4.1.3.37
            BRENDA, the Enzyme Database: 4.1.3.37
///
ENTRY       EC 4.1.3.38                 Enzyme
NAME        aminodeoxychorismate lyase;
            enzyme X;
            4-amino-4-deoxychorismate lyase;
            4-amino-4-deoxychorismate pyruvate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     4-amino-4-deoxychorismate pyruvate-lyase (4-aminobenzoate-forming)
REACTION    4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate [RN:R05553]
ALL_REAC    R05553
SUBSTRATE   4-amino-4-deoxychorismate [CPD:C11355]
PRODUCT     4-aminobenzoate [CPD:C00568];
            pyruvate [CPD:C00022]
COMMENT     A pyridoxal-phosphate protein. Forms part of the folate biosynthesis
            pathway. Acts on 4-amino-4-deoxychorismate, the product of EC
            6.3.5.8, aminodeoxychorismate synthase, to form p-aminobenzoate.
REFERENCE   1  [PMID:2251281]
  AUTHORS   Ye QZ, Liu J, Walsh CT.
  TITLE     p-Aminobenzoate synthesis in Escherichia coli: purification and
            characterization of PabB as aminodeoxychorismate synthase and enzyme
            X as aminodeoxychorismate lyase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 9391-5.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:1644759]
  AUTHORS   Green JM, Merkel WK, Nichols BP.
  TITLE     Characterization and sequence of Escherichia coli pabC, the gene
            encoding aminodeoxychorismate lyase, a pyridoxal
            phosphate-containing enzyme.
  JOURNAL   J. Bacteriol. 174 (1992) 5317-23.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:10876155]
  AUTHORS   Nakai T, Mizutani H, Miyahara I, Hirotsu K, Takeda S, Jhee KH,
            Yoshimura T, Esaki N.
  TITLE     Three-dimensional structure of 4-amino-4-deoxychorismate lyase from
            Escherichia coli.
  JOURNAL   J. Biochem. (Tokyo). 128 (2000) 29-38.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K02619  4-amino-4-deoxychorismate lyase
GENES       ECO: b1096(pabC)
            ECJ: JW1082(pabC)
            ECE: Z1735(pabC)
            ECS: ECs1474
            ECC: c1366(pabC)
            ECI: UTI89_C1222(pabC)
            ECP: ECP_1088
            ECV: APECO1_177(pabC)
            ECW: EcE24377A_1217(pabC)
            ECX: EcHS_A1218
            STY: STY1237(pabC)
            STT: t1722(pabC)
            SPT: SPA1653(pabC)
            SEC: SC1148(pabC)
            STM: STM1198(pabC)
            YPE: YPO1603(pabC)
            YPK: y1762(pabC)
            YPM: YP_2251(pabC)
            YPA: YPA_1922
            YPN: YPN_2026
            YPS: YPTB2468(pabC)
            YPI: YpsIP31758_1581(pabC)
            SFL: SF1100(pabC)
            SFX: S1180(pabC)
            SFV: SFV_1116(pabC)
            SSN: SSON_1116(pabC)
            SBO: SBO_1967(pabC)
            SDY: SDY_2054(pabC)
            ECA: ECA1800(pabC)
            PLU: plu2830(pabC)
            SGL: SG1063
            BFL: Bfl402(pabC)
            BPN: BPEN_414(pabC)
            HIN: HI1169
            HIT: NTHI1337
            HDU: HD0409
            PMU: PM1465
            MSU: MS2192(ilvE)
            VCH: VC2018
            VVU: VV1_3005
            VVY: VV1278
            VPA: VP2051
            VFI: VF1737
            PPR: PBPRA1198
            PAE: PA2964
            PAU: PA14_25710(pabC)
            PPU: PP_1917(pabC)
            PST: PSPTO_3829(pabC)
            PSB: Psyr_1650
            PSP: PSPPH_1644
            PFL: PFL_1799
            PFO: Pfl_4154
            PEN: PSEEN1622
            PAR: Psyc_0141
            PCR: Pcryo_0152
            ACI: ACIAD2590(pabC)
            SON: SO_2615(pabC)
            SDN: Sden_2053
            SFR: Sfri_2242
            SAZ: Sama_2045
            SLO: Shew_1577
            SPL: Spea_1921
            SHM: Shewmr7_1734
            SHN: Shewana3_1764
            ILO: IL1338(pabC)
            CPS: CPS_2300(pabC)
            PHA: PSHAa1805(pabC)
            MAQ: Maqu_1864
            LPN: lpg0595
            LPF: lpl0629(pabC)
            LPP: lpp0645(pabC)
            MCA: MCA1998(pabC)
            FTU: FTT0945
            FTF: FTF0945
            TCX: Tcr_0716
            NOC: Noc_1662
            AEH: Mlg_1418
            HHA: Hhal_0004
            HCH: HCH_02146(pabC)
            CSA: Csal_1604
            ABO: ABO_1072(pabC)
            AHA: AHA_2254
            BCI: BCI_0432(pabC)
            VOK: COSY_0213(pabC)
            NME: NMB1970
            NMA: NMA0477
            NGO: NGO2112
            CVI: CV_3410(pabC)
            RSO: RSc2633(pabB)
            REU: Reut_A2783
            REH: H16_A1568
            RME: Rmet_2920
            BMA: BMA2324
            BXE: Bxe_A3959
            BPS: BPSL2825
            BPM: BURPS1710b_3318(pabB)
            BTE: BTH_I1310
            BPE: BP3242
            BPA: BPP3599
            BBR: BB4034
            RFR: Rfer_3314
            POL: Bpro_0904
            HAR: HEAR2983
            EBA: ebA6309(pabB)
            DAR: Daro_3087
            TBD: Tbd_1545
            MFA: Mfla_1502
            HPY: HP0293(pabB)
            HPJ: jhp0278(pabB)
            HPA: HPAG1_0295 HPAG1_0566
            HHE: HH0304(trpE_1)
            HAC: Hac_0553(pabB)
            TDN: Tmden_0434
            CJE: Cj0862c(pabB)
            GSU: GSU0523(pabB)
            GME: Gmet_3010
            DVU: DVU0362
            DDE: Dde_3619
            DPS: DP0875
            MLO: mlr3007
            SME: SMc04014
            ATU: Atu3766
            ATC: AGR_L_2139
            RET: RHE_CH03551
            BME: BMEI1471 BMEII0014
            BMS: BRA0079
            BMB: BruAb2_0079
            CCR: CC_2952
            SIL: SPO0925
            SIT: TM1040_0634
            RSP: RSP_0816
            GBE: GbCGDNIH1_0761
            RRU: Rru_A1131
            MGM: Mmc1_0427
            BSU: BG10139(pabC)
            BHA: BH0092(pabC)
            BAN: BA0070(pabC)
            BAR: GBAA0070(pabC)
            BAA: BA_0660
            BAT: BAS0070
            BCE: BC0078
            BCA: BCE_0069(pabC)
            BCZ: BCZK0066(pabC)
            BTK: BT9727_0066(pabC)
            BTL: BALH_0069(pabC)
            BLI: BL00860(pabC)
            BLD: BLi00092(pabC)
            BCL: ABC0112(pabC)
            BPU: BPUM_0060 BPUM_2373(yrrL)
            OIH: OB0702
            GKA: GK0068
            SAU: SA0670
            SAV: SAV0715
            SAM: MW0677
            SAR: SAR0768
            SAS: SAS0680
            SAA: SAUSA300_0700
            SAO: SAOUHSC_00724
            SEP: SE0490
            SHA: SH2183
            SSP: SSP2005
            LMO: lmo2750
            LMF: LMOf2365_2737(pabB)
            LIN: lin2893
            LWE: lwe2698(pabB)
            SPY: SPy_1990(pabB)
            SPM: spyM18_2056
            SPG: SpyM3_1712(pabP)
            SPS: SPs1712
            SPH: MGAS10270_Spy1765
            SPI: MGAS10750_Spy1789
            SPJ: MGAS2096_Spy1724
            SPK: MGAS9429_Spy1702
            SPA: M6_Spy1703
            SPB: M28_Spy1682
            SPN: SP_0665
            SPR: spr0582(pabB)
            SAG: SAG1528
            SAN: gbs1584
            SAK: SAK_1551(pabB)
            STC: str0771(pabB)
            STL: stu0771(pabB)
            CPE: CPE1018
            CNO: NT01CX_0378
            CHY: CHY_2669(pabC)
            DSY: DSY3274
            MTU: Rv0812(pabC)
            MTC: MT0833(dat)
            MBO: Mb0118 Mb0835 Mb3709
            MPA: MAP0642(pabC)
            MSM: MSMEG_5795
            MMC: Mmcs_4535
            CGL: NCgl2491(cgl2580)
            CGB: cg2851
            CEF: CE2472
            CDI: DIP1916
            CJK: jk0373
            NFA: nfa5840
            RHA: RHA1_ro01826 RHA1_ro04846
            TWH: TWT533
            TWS: TW227
            LXX: Lxx17640(pabC)
            PAC: PPA2261
            SEN: SACE_7111(pabC)
            BAD: BAD_0076(pabC)
            RXY: Rxyl_0760
            FNU: FN1729 FN1976
            PCU: pc1325(pabC)
            LIL: LA0110
            LIC: LIC10098(pabB)
            LBJ: LBJ_0090
            LBL: LBL_0046
            SYN: slr0887
            ANA: alr1260
            AVA: Ava_0576
            PMF: P9303_29691(pabC)
            PME: NATL1_21671(pabC)
            BTH: BT_0768
            BFR: BF2240
            BFS: BF2336
            CHU: CHU_1302(pabC)
            CTE: CT1712
            AAE: aq_1606(pabC)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.38
            ExPASy - ENZYME nomenclature database: 4.1.3.38
            ExplorEnz - The Enzyme Database: 4.1.3.38
            ERGO genome analysis and discovery system: 4.1.3.38
            BRENDA, the Enzyme Database: 4.1.3.38
///
ENTRY       EC 4.1.3.39                 Enzyme
NAME        4-hydroxy-2-oxovalerate aldolase;
            4-hydroxy-2-ketovalerate aldolase;
            HOA;
            DmpG;
            4-hydroxy-2-oxovalerate pyruvate-lyase;
            4-hydroxy-2-oxopentanoate pyruvate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming)
REACTION    4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate [RN:R00750]
ALL_REAC    R00750
SUBSTRATE   4-hydroxy-2-oxopentanoate [CPD:C03589]
PRODUCT     acetaldehyde [CPD:C00084];
            pyruvate [CPD:C00022]
COMMENT     Requires Mn2+ for maximal activity [1]. The enzyme from Pseudomonas
            putida is also stimulated by the presence of NADH [1]. In
            Pseudomonas species, this enzyme forms part of a bifunctional enzyme
            with EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). It
            catalyses the penultimate step in the meta-cleavage pathway for the
            degradation of phenols, cresols and catechol [1].
REFERENCE   1  [PMID:12764229]
  AUTHORS   Manjasetty BA, Powlowski J, Vrielink A.
  TITLE     Crystal structure of a bifunctional aldolase-dehydrogenase:
            sequestering a reactive and volatile intermediate.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 6992-7.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:8419288]
  AUTHORS   Powlowski J, Sahlman L, Shingler V.
  TITLE     Purification and properties of the physically associated
            meta-cleavage pathway enzymes 4-hydroxy-2-ketovalerate aldolase and
            aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain
            CF600.
  JOURNAL   J. Bacteriol. 175 (1993) 377-85.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:11264589]
  AUTHORS   Manjasetty BA, Croteau N, Powlowski J, Vrielink A.
  TITLE     Crystallization and preliminary X-ray analysis of dmpFG-encoded
            4-hydroxy-2-ketovalerate aldolase--aldehyde dehydrogenase
            (acylating) from Pseudomonas sp. strain CF600.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 57 (2001) 582-5.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00360  Phenylalanine metabolism
            PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00621  Biphenyl degradation
            PATH: map00622  Toluene and xylene degradation
            PATH: map00627  1,4-Dichlorobenzene degradation
            PATH: map00628  Fluorene degradation
            PATH: map00629  Carbazole degradation
            PATH: map00643  Styrene degradation
ORTHOLOGY   KO: K01666  4-hydroxy 2-oxovalerate aldolase
GENES       ECO: b0352(mhpE)
            ECJ: JW0343(mhpE)
            ECE: Z0452(mhpE)
            ECS: ECs0407
            SSN: SSON_0331(mhpE)
            ECA: ECA1429(nahM)
            PLU: plu4081
            PPU: PP_1791
            PSB: Psyr_3072
            PSP: PSPPH_2158
            PEN: PSEEN0975
            SDN: Sden_2668
            PHA: PSHAa2143(mhpE)
            LPN: lpg2681
            LPF: lpl2608
            LPP: lpp2735
            AEH: Mlg_2462
            RSO: RS01666(RSp0895)
            REU: Reut_B5823
            REH: H16_A1807(mhpE2) H16_B0552(mhpE1) H16_B0595(bpHI)
            RME: Rmet_1319 Rmet_5209
            BXE: Bxe_A1152(amnG) Bxe_A3546 Bxe_B2325 Bxe_C1187(bphI)
            BUR: Bcep18194_B1188 Bcep18194_B1457 Bcep18194_B2959
                 Bcep18194_C7644
            BPS: BPSS1807(mhpE)
            BPM: BURPS1710b_A0890(mhpE)
            BPL: BURPS1106A_A2454
            BPD: BURPS668_A2590(mhpE)
            BTE: BTH_II0570(mhpE)
            RFR: Rfer_0454
            POL: Bpro_5136
            PNA: Pnap_4142
            AJS: Ajs_0224
            VEI: Veis_2781
            MPT: Mpe_A2266 Mpe_A3321
            AZO: azo1857(lapG) azo1972(mhpE) azo2431(nahM)
            DAR: Daro_0907 Daro_1356 Daro_3238 Daro_3782 Daro_3808
            NAR: Saro_3852
            BCA: BCE_2157
            BTL: BALH_1844
            CHY: CHY_1280(mhpE)
            DSY: DSY3306
            MTA: Moth_1775
            MTU: Rv3469c(mhpE) Rv3534c
            MTC: MT3575(bphI-1) MT3638(bphI-2)
            MBO: Mb3498c(mhpE) Mb3564c
            MBB: BCG_3534c(mhpE) BCG_3598c
            MPA: MAP0533
            MAV: MAV_0627
            MSM: MSMEG_4150 MSMEG_5937
            MUL: MUL_2435 MUL_4095
            MVA: Mvan_0597 Mvan_4391 Mvan_5234
            MMC: Mmcs_4659 Mmcs_5438
            MKM: Mkms_4747 Mkms_5835
            MJL: Mjls_4224 Mjls_5042
            NFA: nfa30510 nfa33200 nfa4670
            RHA: RHA1_ro00515 RHA1_ro03867 RHA1_ro04535(hsaF) RHA1_ro05801
                 RHA1_ro08083(bphF3) RHA1_ro10112(bphF4)
            SCO: SCP1.301
            FAL: FRAAL4663
            STP: Strop_3525
            SYW: SYNW0424
            TTJ: TTHB246
            MLA: Mlab_0987
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.39
            ExPASy - ENZYME nomenclature database: 4.1.3.39
            ExplorEnz - The Enzyme Database: 4.1.3.39
            ERGO genome analysis and discovery system: 4.1.3.39
            BRENDA, the Enzyme Database: 4.1.3.39
///
ENTRY       EC 4.1.3.40                 Enzyme
NAME        chorismate lyase;
            CL;
            CPL;
            UbiC
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
SYSNAME     chorismate pyruvate-lyase (4-hydroxybenzoate-forming)
REACTION    chorismate = 4-hydroxybenzoate + pyruvate [RN:R01302]
ALL_REAC    R01302
SUBSTRATE   chorismate [CPD:C00251]
PRODUCT     4-hydroxybenzoate [CPD:C00156];
            pyruvate [CPD:C00022]
COMMENT     This enzyme catalyses the first step in the biosynthesis of
            ubiquinone in Escherichia coli and other Gram-negative bacteria [1].
            The yeast Saccharomyces cerevisiae can synthesize ubiquinone from
            either chorismate or tyrosine [3].
REFERENCE   1  [PMID:1644758]
  AUTHORS   Nichols BP, Green JM.
  TITLE     Cloning and sequencing of Escherichia coli ubiC and purification of
            chorismate lyase.
  JOURNAL   J. Bacteriol. 174 (1992) 5309-16.
REFERENCE   2  [PMID:8012607]
  AUTHORS   Siebert M, Severin K, Heide L.
  TITLE     Formation of 4-hydroxybenzoate in Escherichia coli: characterization
            of the ubiC gene and its encoded enzyme chorismate pyruvate-lyase.
  JOURNAL   Microbiology. 140 ( Pt 4) (1994) 897-904.
REFERENCE   3  [PMID:11583838]
  AUTHORS   Meganathan R.
  TITLE     Ubiquinone biosynthesis in microorganisms.
  JOURNAL   FEMS. Microbiol. Lett. 203 (2001) 131-9.
PATHWAY     PATH: map00130  Ubiquinone biosynthesis
ORTHOLOGY   KO: K03181  chorismate--pyruvate lyase
GENES       ECO: b4039(ubiC)
            ECJ: JW5713(ubiC)
            ECE: Z5638(ubiC)
            ECS: ECs5022
            ECC: c5009(ubiC)
            ECI: UTI89_C4609(ubiC)
            ECP: ECP_4256
            ECV: APECO1_2430(ubiC)
            STY: STY4429(ubiC)
            STT: t4139(ubiC)
            SPT: SPA4050(ubiC)
            SEC: SC4112(ubiC)
            STM: STM4233(ubiC)
            YPE: YPO0310(ubiC)
            YPK: y0568(ubiC)
            YPM: YP_0466(ubiC)
            YPA: YPA_3974
            YPN: YPN_3359
            YPS: YPTB0366(ubiC)
            SFL: SF4166(ubiC)
            SFX: S3565(ubiC)
            SFV: SFV_4174(ubiC)
            SSN: SSON_4219(ubiC)
            SBO: SBO_4078(ubiC)
            SDY: SDY_4535(ubiC)
            ECA: ECA0626(ubiC)
            PLU: plu4378(ubiC)
            SGL: SG2144
            HSO: HS_0150(ubiC)
            PMU: PM0918
            APL: APL_1840(ubiC)
            VCH: VC0095
            VVU: VV1_1163
            VVY: VV0120
            VPA: VP2949
            VFI: VF2445
            PPR: PBPRA0162(ubiC)
            PAE: PA5357
            PAU: PA14_70720(ubiC)
            PPU: PP_5317
            PST: PSPTO_5475
            PSB: Psyr_5030
            PSP: PSPPH_5112
            PFL: PFL_6105
            PFO: Pfl_5603
            PEN: PSEEN4753 PSEEN5461
            PAR: Psyc_0289(ubiC)
            PCR: Pcryo_0317
            ACI: ACIAD2456(ubiC)
            ACB: A1S_2350
            SON: SO_0131
            SDN: Sden_0095
            SFR: Sfri_0048
            SAZ: Sama_3623
            SBL: Sbal_4229
            SLO: Shew_3743
            SHE: Shewmr4_0126
            SHM: Shewmr7_0120
            SHN: Shewana3_0125
            SHW: Sputw3181_3946
            ILO: IL0265(ubiC)
            CPS: CPS_0125
            PHA: PSHAa2311(ubiC)
            PAT: Patl_0066
            PIN: Ping_3468
            MAQ: Maqu_3594
            CBU: CBU_0054
            MCA: MCA1335
            FTU: FTT0857c
            FTF: FTF0857c
            FTL: FTL_0356
            FTH: FTH_0351
            FTN: FTN_0386(ubiC)
            TCX: Tcr_2154
            AEH: Mlg_2439
            HHA: Hhal_0966
            CSA: Csal_3251
            ABO: ABO_0164(pabA)
            AHA: AHA_0180
            RMA: Rmag_0929
            NME: NMB0734
            NMA: NMA0944
            NGO: NGO0310
            RSO: RSc2780(RS00067)
            REU: Reut_A2859
            REH: H16_A3165
            RME: Rmet_3058
            BMA: BMA1946
            BMV: BMASAVP1_A1006
            BML: BMA10299_A0858
            BXE: Bxe_A3325
            BUR: Bcep18194_A5685
            BCN: Bcen_1734
            BCH: Bcen2424_2346
            BAM: Bamb_2382
            BPS: BPSL1088
            BPM: BURPS1710b_1319(albXX)
            BPL: BURPS1106A_1168(ubiC)
            BPD: BURPS668_1159(ubiC)
            BTE: BTH_I0956
            BPE: BP0981
            BPA: BPP1450
            BBR: BB2524
            RFR: Rfer_3015
            HAR: HEAR2756
            NEU: NE1837
            NET: Neut_1129
            NMU: Nmul_A2612
            EBA: ebA2295(ubiC)
            AZO: azo0478(ubiC)
            DAR: Daro_3252
            TBD: Tbd_0464
            MFA: Mfla_0053
            BHE: BH11580(ubiC)
            BQU: BQ09210(ubiC)
            BBK: BARBAKC583_0971(ubiC)
            MGM: Mmc1_0239
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.3.40
            ExPASy - ENZYME nomenclature database: 4.1.3.40
            ExplorEnz - The Enzyme Database: 4.1.3.40
            ERGO genome analysis and discovery system: 4.1.3.40
            BRENDA, the Enzyme Database: 4.1.3.40
            CAS: 157482-18-3
///
ENTRY       EC 4.1.3.-                  Enzyme
CLASS       Lyases;
            Carbon-carbon lyases;
            Oxo-acid-lyases
REACTION    (1) Succinate semialdehyde-thiamin diphosphate anion + Isochorismate
            <=> 2-Succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate + Thiamin
            diphosphate + Pyruvate [RN:R04992];
            (2) 2-Propylmalate + CoA <=> 2-Oxopentanoic acid + Acetyl-CoA
            [RN:R05063];
            (3) Propanal + Pyruvate <=> 4-Hydroxy-2-oxohexanoic acid [RN:R05298]
SUBSTRATE   Acetaldehyde [CPD:C00084];
            Pyruvate [CPD:C00022];
            4-Hydroxybenzoate [CPD:C00156];
            Succinate semialdehyde-thiamin diphosphate anion [CPD:C05816];
            Isochorismate [CPD:C00885];
            2-Propylmalate [CPD:C05994];
            CoA [CPD:C00010];
            Propanal [CPD:C00479]
PRODUCT     4-Hydroxy-2-oxopentanoate [CPD:C03589];
            Chorismate [CPD:C00251];
            2-Succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate [CPD:C05817];
            Thiamin diphosphate [CPD:C00068];
            Pyruvate [CPD:C00022];
            2-Oxopentanoic acid [CPD:C06255];
            Acetyl-CoA [CPD:C00024];
            4-Hydroxy-2-oxohexanoic acid [CPD:C06762]
///
ENTRY       EC 4.1.99.1                 Enzyme
NAME        tryptophanase;
            L-tryptophanase;
            L-tryptophan indole-lyase (deaminating)
CLASS       Lyases;
            Carbon-carbon lyases;
            Other carbon-carbon lyases
SYSNAME     L-tryptophan indole-lyase (deaminating; pyruvate-forming)
REACTION    L-tryptophan + H2O = indole + pyruvate + NH3 [RN:R00673]
ALL_REAC    R00673
SUBSTRATE   L-tryptophan [CPD:C00078];
            H2O [CPD:C00001]
PRODUCT     indole [CPD:C00463];
            pyruvate [CPD:C00022];
            NH3 [CPD:C00014]
COFACTOR    Pyridoxal phosphate [CPD:C00018];
            Potassium [CPD:C00238]
COMMENT     A pyridoxal-phosphate protein, requiring K+. Also catalyses
            2,3-elimination and beta-replacement reactions of some
            indole-substituted tryptophan analogues of L-cysteine, L-serine and
            other 3-substituted amino acids.
REFERENCE   1  [PMID:14017164]
  AUTHORS   BURNS RO, DEMOSS RD.
  TITLE     Properties of tryptophanase from Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 65 (1962) 233-44.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Cowell, J.L., Maser, K. and DeMoss, R.D.
  TITLE     Tryptophanase from Aeromonas liquifaciens. Purification, molecular
            weight and some chemical, catalytic and immunological properties.
  JOURNAL   Biochim. Biophys. Acta 315 (1973) 449-463.
  ORGANISM  Aeromonas liquifaciens
REFERENCE   3  [PMID:14284727]
  AUTHORS   NEWTON WA, MORINO Y, SNELL EE.
  TITLE     PROPERTIES OF CRYSTALLINE TRYPTOPHANASE.
  JOURNAL   J. Biol. Chem. 240 (1965) 1211-8.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00380  Tryptophan metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K01667  tryptophanase
GENES       EHI: 347.t00005
            ECO: b3708(tnaA)
            ECJ: JW3686(tnaA)
            ECE: Z5203(tnaA)
            ECS: ECs4645
            ECC: c4631(tnaA)
            ECI: UTI89_C4261(tnaA)
            ECP: ECP_3908
            ECV: APECO1_2752(tnaA)
            ECW: EcE24377A_4217(tnaA)
            ECX: EcHS_A3922(tnaA)
            YEN: YE0650(tnaA)
            SFL: SF3754(tnaA)
            SFX: S4017(tnaA)
            SFV: SFV_3805(tnaA)
            PLU: plu0799(tnaA)
            HIT: NTHI0831(tnaA)
            HSO: HS_0801(tnaA)
            PMU: PM1420(tnaA)
            VCH: VCA0161
            VCO: VC0395_1117(tnaA)
            VVU: VV2_0854
            VVY: VVA1325
            VPA: VPA0192
            PPR: PBPRA1344 PBPRA2532 PBPRB0382
            SSE: Ssed_3916
            DNO: DNO_0442
            CVI: CV_1163(tnaA)
            RFR: Rfer_2475
            EBA: ebA605(tnaA)
            DVU: DVU2204(tnaA)
            DVL: Dvul_1032
            AFW: Anae109_1760
            RPA: RPA3564
            RPB: RPB_1966
            RPC: RPC_2787
            RPD: RPD_3423
            RPE: RPE_2915
            ABA: Acid345_3931
            SUS: Acid_6369
            STH: STH439(tna-2) STH441(tna-1)
            CTC: CTC01509
            CNO: NT01CX_2071
            AMT: Amet_3003
            DSY: DSY1332 DSY4042
            DRM: Dred_2018
            TTE: TTE1602(tnaA)
            PAC: PPA1068
            NCA: Noca_1624
            SEN: SACE_1957
            FNU: FN1943
            TDE: TDE0251(tnaA)
            HAL: VNG2373G(tnaA)
            HMA: rrnAC2439(tnaA)
            APE: APE_1275
STRUCTURES  PDB: 1AX4  2C44  2OQX  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.99.1
            ExPASy - ENZYME nomenclature database: 4.1.99.1
            ExplorEnz - The Enzyme Database: 4.1.99.1
            ERGO genome analysis and discovery system: 4.1.99.1
            BRENDA, the Enzyme Database: 4.1.99.1
            CAS: 9024-00-4
///
ENTRY       EC 4.1.99.2                 Enzyme
NAME        tyrosine phenol-lyase;
            beta-tyrosinase;
            L-tyrosine phenol-lyase (deaminating)
CLASS       Lyases;
            Carbon-carbon lyases;
            Other carbon-carbon lyases
SYSNAME     L-tyrosine phenol-lyase (deaminating; pyruvate-forming)
REACTION    L-tyrosine + H2O = phenol + pyruvate + NH3 [RN:R00728]
ALL_REAC    R00728
SUBSTRATE   L-tyrosine [CPD:C00082];
            H2O [CPD:C00001]
PRODUCT     phenol [CPD:C00146];
            pyruvate [CPD:C00022];
            NH3 [CPD:C00014]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. The enzyme also slowly catalyses
            pyruvate formation from D-tyrosine, S-methyl-L-cysteine, L-cysteine,
            L-serine and D-serine.
REFERENCE   1  [PMID:4908868]
  AUTHORS   Kumagai H, Yamada H, Matsui H, Ohkishi H, Ogata K.
  TITLE     Tyrosine phenol lyase. I. Purification, crystallization, and
            properties.
  JOURNAL   J. Biol. Chem. 245 (1970) 1767-72.
  ORGANISM  Escherichia infermedia
REFERENCE   2  [PMID:4908869]
  AUTHORS   Kumagai H, Yamada H, Matsui H, Ohkishi H, Ogata K.
  TITLE     Tyrosine phenol lyase. II. Cofactor requrements.
  JOURNAL   J. Biol. Chem. 245 (1970) 1773-7.
  ORGANISM  Escherichia infermedia
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K01668  tyrosine phenol-lyase
GENES       PMU: PM0811
            AHA: AHA_1963
            SAT: SYN_01455
            STH: STH2842
            CTC: CTC00818
            DSY: DSY3653
            FNU: FN1988
            TDE: TDE1118(tpl)
            BTH: BT_1492
            PGI: PG1401
            RRS: RoseRS_0320
            RCA: Rcas_0866
STRUCTURES  PDB: 1C7G  1TPL  2EZ1  2EZ2  2TPL  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.99.2
            ExPASy - ENZYME nomenclature database: 4.1.99.2
            ExplorEnz - The Enzyme Database: 4.1.99.2
            ERGO genome analysis and discovery system: 4.1.99.2
            BRENDA, the Enzyme Database: 4.1.99.2
            CAS: 9059-31-8
///
ENTRY       EC 4.1.99.3                 Enzyme
NAME        deoxyribodipyrimidine photo-lyase;
            photoreactivating enzyme;
            DNA photolyase;
            DNA-photoreactivating enzyme;
            DNA cyclobutane dipyrimidine photolyase;
            DNA photolyase;
            deoxyribonucleic photolyase;
            deoxyribodipyrimidine photolyase;
            photolyase;
            PRE;
            PhrB photolyase;
            deoxyribonucleic cyclobutane dipyrimidine photolyase;
            phr A photolyase;
            dipyrimidine photolyase (photosensitive);
            deoxyribonucleate pyrimidine dimer lyase (photosensitive)
CLASS       Lyases;
            Carbon-carbon lyases;
            Other carbon-carbon lyases
SYSNAME     deoxyribocyclobutadipyrimidine pyrimidine-lyase
REACTION    cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
ALL_REAC    (other) R00034
SUBSTRATE   cyclobutadipyrimidine (in DNA) [CPD:C03103]
PRODUCT     pyrimidine residues (in DNA)
COFACTOR    FAD [CPD:C00016];
            5,10-Methenyltetrahydrofolate [CPD:C00445]
COMMENT     A flavoprotein (FAD), containing a second chromophore group. The
            enzyme catalyses the reactivation by light of irradiated DNA. A
            similar reactivation of irradiated RNA is probably due to a separate
            enzyme.
REFERENCE   1  [PMID:804322]
  AUTHORS   Eker AP, Fichtinger-Schepman AM.
  TITLE     Studies on a DNA photoreactivating enzyme from Streptomyces griseus.
            II. Purification of the enzyme.
  JOURNAL   Biochim. Biophys. Acta. 378 (1975) 54-63.
  ORGANISM  Streptomyces griseus
REFERENCE   2  [PMID:3539939]
  AUTHORS   Sancar GB, Smith FW, Reid R, Payne G, Levy M, Sancar A.
  TITLE     Action mechanism of Escherichia coli DNA photolyase. I. Formation of
            the enzyme-substrate complex.
  JOURNAL   J. Biol. Chem. 262 (1987) 478-85.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:5649902]
  AUTHORS   Setlow JK, Bollum FJ.
  TITLE     The minimum size of the substrate for yeast photoreactivating
            enzyme.
  JOURNAL   Biochim. Biophys. Acta. 157 (1968) 233-7.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
ORTHOLOGY   KO: K01669  deoxyribodipyrimidine photo-lyase
GENES       MDO: 554181(pOPC1)
            GGA: 424919(LOC424919)
            DME: Dmel_CG11205(phr)
            ATH: AT1G12370(PHR1)
            CME: CMA044C
            SCE: YOR386W(PHR1)
            ANI: AN0387.2
            AFM: AFUA_1G01600
            AOR: AO090102000015
            UMA: UM06079.1
            PFA: PFE0675c
            TET: TTHERM_00046730 TTHERM_00640040
            TBR: Tb10.26.0940 Tb11.01.4170
            TCR: 509027.10 511127.260
            LMA: LmjF09.0360 LmjF33.0470
            ECO: b0708(phr)
            ECJ: JW0698(phr)
            ECE: Z0859(phrB)
            ECS: ECs0733
            ECC: c0787(phrB)
            ECI: UTI89_C0706(phrB)
            ECP: ECP_0721
            ECW: EcE24377A_0733(phrB)
            ECX: EcHS_A0755
            STY: STY0749(phrB)
            STT: t2167(phrB)
            SPT: SPA2032(phrB)
            SEC: SC0728(phrB)
            STM: STM0709(phrB)
            YPE: YPO2695(phrB)
            YPK: y1270(phrB)
            YPM: YP_2499(phrB)
            YPA: YPA_2426
            YPN: YPN_1183
            YPP: YPDSF_1576
            YPS: YPTB2913(phrB)
            YPI: YpsIP31758_1112(phrB)
            SFL: SF0589(phrB)
            SFX: S0602(phrB)
            SFV: SFV_0627(phrB)
            SSN: SSON_0657(phrB)
            SBO: SBO_0567(phrB)
            SDY: SDY_0643(phrB)
            ECA: ECA1349(phrB)
            BUC: BU300(phrB)
            BAB: bbp278(phrB)
            WBR: WGLp182(phrB)
            SGL: SG0868
            ENT: Ent638_1212
            SPE: Spro_1252
            XCC: XCC1435(phr)
            XCB: XC_2803
            XCV: XCV1536
            XAC: XAC1478(phr)
            XOO: XOO1526(phr)
            XOM: XOO_1415(XOO1415)
            VCH: VC1392 VCA0057
            VCO: VC0395_0080(phrB-2)
            VVU: VV2_1543
            VVY: VVA0357
            VPA: VPA1471
            VFI: VFA0753
            PAE: PA4660(phr)
            PAU: PA14_61640(phr)
            PAP: PSPA7_5309(phrB)
            PPU: PP_0739(phrB)
            PPF: Pput_0767
            PST: PSPTO_1121(phrB)
            PSB: Psyr_0961
            PSP: PSPPH_1010(phrB)
            PFL: PFL_5147(phrB)
            PFO: Pfl_4736
            PEN: PSEEN0881(phrB)
            PMY: Pmen_1071
            PAR: Psyc_0430(phrB)
            PCR: Pcryo_0465
            PRW: PsycPRwf_0753
            ACI: ACIAD1182(phrB)
            SON: SO_3384(phrB)
            SDN: Sden_2838
            SFR: Sfri_0779 Sfri_3038
            SAZ: Sama_0811
            SBL: Sbal_3054
            SBM: Shew185_3068
            SLO: Shew_1479
            SPC: Sputcn32_2714
            SHE: Shewmr4_1165
            SHM: Shewmr7_1236
            SHN: Shewana3_1166
            SHW: Sputw3181_1298
            ILO: IL1388(phrB_1)
            CPS: CPS_1380(phrB)
            PHA: PSHAa2200 PSHAb0453(phr)
            PAT: Patl_0151 Patl_0152 Patl_2179
            SDE: Sde_0729
            PIN: Ping_0998 Ping_1548 Ping_1549
            MAQ: Maqu_0320 Maqu_2357 Maqu_3105
            CBU: CBU_1176(phrB)
            LPN: lpg0212(phrB)
            LPF: lpl0266
            LPP: lpp0271
            FTU: FTT0846
            FTF: FTF0846
            FTW: FTW_1173(phrB1) FTW_1339(phrB2)
            FTL: FTL_0341 FTL_0342
            FTN: FTN_0361 FTN_1121(phrB)
            TCX: Tcr_2125
            AEH: Mlg_2256
            HHA: Hhal_0915
            HCH: HCH_00062(phrB1) HCH_01735(phrB2)
            CSA: Csal_0465
            ABO: ABO_0766(phrB)
            MMW: Mmwyl1_0336 Mmwyl1_1152
            AHA: AHA_1101(phrB)
            NMA: NMA2198(phr)
            NMC: NMC1892(phr)
            NGO: NGO1707
            CVI: CV_3481(phrB)
            REU: Reut_A0703
            REH: H16_A1679
            RME: Rmet_2745
            BMA: BMA0636(phrB)
            BMV: BMASAVP1_A2376(phrB)
            BML: BMA10299_A2911(phrB)
            BMN: BMA10247_1691(phrB)
            BXE: Bxe_B2844
            BVI: Bcep1808_5895
            BUR: Bcep18194_A5488
            BCN: Bcen_5899
            BCH: Bcen2424_2178
            BAM: Bamb_2217
            BPS: BPSL2349
            BPM: BURPS1710b_2800(phrB)
            BPL: BURPS1106A_2734(phrB)
            BPD: BURPS668_2677(phrB)
            BTE: BTH_I1815
            PNU: Pnuc_0241
            RFR: Rfer_1376
            PNA: Pnap_3349
            AAV: Aave_0906
            AJS: Ajs_1801
            MPT: Mpe_A0704
            HAR: HEAR2742(phr)
            AZO: azo3458(phrB)
            DAR: Daro_3894
            MFA: Mfla_0591
            WSU: WS1544
            TDN: Tmden_1611
            ABU: Abu_0834(phrB)
            GSU: GSU2829
            PCA: Pcar_2716
            PPD: Ppro_2012
            DVU: DVU0112
            DVL: Dvul_2851
            DDE: Dde_0179
            BBA: Bd2206(phr)
            DPS: DP2576
            ADE: Adeh_3028
            MXA: MXAN_4136(phrB)
            SAT: SYN_00402
            SFU: Sfum_3129
            RBE: RBE_0106(phrB)
            PUB: SAR11_1318(phrB)
            MLO: mll8094
            PLA: Plav_0513
            ATU: Atu1218
            ATC: AGR_C_2249
            RLE: RL1985(phr)
            OAN: Oant_0339
            BJA: blr5310
            BRA: BRADO0442 BRADO3224
            BBT: BBta_4932
            RPA: RPA3179
            RPB: RPB_2364
            RPC: RPC_3356
            RPD: RPD_3098
            RPE: RPE_3442
            XAU: Xaut_4676
            CCR: CC_1428
            SIL: SPO1917(phrB)
            SIT: TM1040_1441
            RSP: RSP_1981 RSP_2143
            RSH: Rsph17029_0817
            RSQ: Rsph17025_0815 Rsph17025_3080
            JAN: Jann_1873 Jann_1989
            RDE: RD1_2295(phrB) RD1_2859
            MMR: Mmar10_1491
            HNE: HNE_1798 HNE_3082
            ZMO: ZMO1450(phrB)
            NAR: Saro_1759
            SAL: Sala_0998
            ELI: ELI_07045
            GOX: GOX0976
            ACR: Acry_1615 Acry_2343
            RRU: Rru_A2903
            MGM: Mmc1_1145
            ABA: Acid345_4497
            SUS: Acid_6673
            BAN: BA3180
            BAR: GBAA3180
            BAA: BA_3689
            BAT: BAS2956
            BCE: BC3137
            BCA: BCE_3184
            BTK: BT9727_2935(phrB)
            BAY: RBAM_025550(uvrC) RBAM_025560(trxA)
            BPU: BPUM_1378
            SAU: SA0646
            SAV: SAV0691
            SAM: MW0653
            SAR: SAR0744
            SAS: SAS0656
            SAC: SACOL0751
            SAB: SAB0640
            SAA: SAUSA300_0677
            SAO: SAOUHSC_00699
            SAJ: SaurJH9_0715
            SAH: SaurJH1_0731
            SEP: SE0463
            SER: SERP0349
            SHA: SH2203
            LMO: lmo0588
            LMF: LMOf2365_0617(phrB)
            LIN: lin0597
            LWE: lwe0555(phrB)
            SPY: SPy_1505(phr)
            SPZ: M5005_Spy_1236(phr)
            SPM: spyM18_1523
            SPG: SpyM3_1159(phr)
            SPS: SPs0703
            SPH: MGAS10270_Spy1252(phr)
            SPI: MGAS10750_Spy1343(phr)
            SPJ: MGAS2096_Spy1254(phr)
            SPK: MGAS9429_Spy1231(phr)
            SPF: SpyM50616(phr)
            SPA: M6_Spy1256 M6_Spy1257
            SPB: M28_Spy1175(phr)
            EFA: EF1598(phrB)
            MPA: MAP3081(phr)
            MSM: MSMEG_2576
            MVA: Mvan_2257
            MGI: Mflv_4086
            MMC: Mmcs_2038
            MKM: Mkms_2084
            MJL: Mjls_2021
            CGL: NCgl0604(cgl0630)
            CGB: cg0728(phr)
            CEF: CE0647
            CDI: DIP0113
            NFA: nfa30660(phr)
            RHA: RHA1_ro05003(phr)
            SCO: SCO0842(phr)
            SMA: SAV1212(phrB)
            LXX: Lxx09540(phrB)
            CMI: CMM_0534(phrB)
            ART: Arth_2747
            NCA: Noca_0778
            TFU: Tfu_0534
            FAL: FRAAL0101
            ACE: Acel_0151
            KRA: Krad_3554
            SEN: SACE_4097(phrB)
            RXY: Rxyl_0663
            RBA: RB12007(phr) RB8498(phr)
            PCU: pc0672(phrB)
            LIL: LA2649
            LIC: LIC11339(phr)
            SYN: sll1629(phr) slr0854(phrA)
            SYW: SYNW0219 SYNW0224 SYNW1757
            SYC: syc1392_c(phrA) syc2227_c
            SYF: Synpcc7942_0112 Synpcc7942_1867
            SYD: Syncc9605_0213 Syncc9605_0218 Syncc9605_0708
            SYE: Syncc9902_0239 Syncc9902_0245 Syncc9902_1651
            SYG: sync_0252(phrB) sync_0257 sync_2007
            SYR: SynRCC307_0225(phr) SynRCC307_1185(phr)
            SYX: SynWH7803_0262(phr) SynWH7803_0636(phr)
            CYA: CYA_0303(phrB-1) CYA_0780(phrB-2)
            CYB: CYB_0202(phrB-1) CYB_0803(phrB-2)
            TEL: tll0425(phrA) tll0552
            GVI: glr0784(phrA) glr0835(phrA) glr1749
            ANA: alr2725 alr2966
            AVA: Ava_0940 Ava_4292
            PMM: PMM0285(phr)
            PMN: PMN2A_1651
            PMI: PMT9312_0287
            PMB: A9601_03081(phrB) A9601_03931
            PMC: P9515_03181(phrB) P9515_03991
            PMG: P9301_03091(phrB) P9301_03921
            PMH: P9215_03101
            PME: NATL1_03651(phrB)
            TER: Tery_1113 Tery_4538
            SRU: SRU_1083(phrB) SRU_1179(phrB) SRU_1754(phrB) SRU_2330
            CHU: CHU_1053(phrB) CHU_1055 CHU_1958(phrB)
            GFO: GFO_1822(phr)
            FJO: Fjoh_0061
            FPS: FP1014(phrB1) FP2041(phrB2) FP2043(phrB3)
            CTE: CT0511(phr)
            CCH: Cag_0876
            CPH: Cpha266_1961
            PVI: Cvib_0575
            PLT: Plut_0522
            RRS: RoseRS_3446
            RCA: Rcas_4411
            TTH: TT_P0058
            TTJ: TTHB102
            FNO: Fnod_1383
            MAC: MA4066(phr)
            MBA: Mbar_A0527
            MMA: MM_0852
            MBU: Mbur_2305
            MHU: Mhun_3221
            HAL: VNG1335G(phr2)
            HMA: rrnAC0832(phrB1) rrnAC1943(phrB2)
            HWA: HQ1298A(phr) HQ1445A(phr) HQ2463A(phr)
            NPH: NP3456A(phr_2) NP4042A(phr_1) NP6210A(phr_3)
            PTO: PTO1062
            SSO: SSO2472(phrB)
            STO: ST0889
            SAI: Saci_1227(phr)
            MSE: Msed_0439
STRUCTURES  PDB: 1DNP  1IQR  1IQU  1OWL  1OWM  1OWN  1OWO  1OWP  1QNF  1TEZ  
                 2E0I  2J07  2J08  2J09  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.99.3
            ExPASy - ENZYME nomenclature database: 4.1.99.3
            ExplorEnz - The Enzyme Database: 4.1.99.3
            ERGO genome analysis and discovery system: 4.1.99.3
            BRENDA, the Enzyme Database: 4.1.99.3
            CAS: 37290-70-3
///
ENTRY       EC 4.1.99.4       Obsolete  Enzyme
NAME        Transferred to 3.5.99.7
CLASS       Lyases;
            Carbon-carbon lyases;
            Other carbon-carbon lyases
COMMENT     Transferred entry: now EC 3.5.99.7 1-aminocyclopropane-1-carboxylate
            deaminase (EC 4.1.99.4 created 1981, deleted 2002)
STRUCTURES  PDB: 1F2D  1J0A  1J0B  1J0C  1J0D  1J0E  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.99.4
            ExPASy - ENZYME nomenclature database: 4.1.99.4
            ExplorEnz - The Enzyme Database: 4.1.99.4
            ERGO genome analysis and discovery system: 4.1.99.4
            BRENDA, the Enzyme Database: 4.1.99.4
///
ENTRY       EC 4.1.99.5                 Enzyme
NAME        octadecanal decarbonylase;
            decarbonylase;
            aldehyde decarbonylase
CLASS       Lyases;
            Carbon-carbon lyases;
            Other carbon-carbon lyases
SYSNAME     octadecanal alkane-lyase
REACTION    octadecanal = heptadecane + CO [RN:R03728]
ALL_REAC    R03728
SUBSTRATE   octadecanal [CPD:C01838]
PRODUCT     heptadecane [CPD:C01816];
            CO [CPD:C00237]
INHIBITOR   EDTA [CPD:C00284]
COMMENT     Involved in the biosynthesis of alkanes in the pea Pisum sativum
            from fatty acids of chain length C18 to C32. Inhibited by
            metal-chelating agents.
REFERENCE   1  [PMID:6593720]
  AUTHORS   Cheesbrough TM, Kolattukudy PE.
  TITLE     Alkane biosynthesis by decarbonylation of aldehydes catalyzed by a
            particulate preparation from Pisum sativum.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 6613-7.
  ORGANISM  Pisum sativum
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.99.5
            ExPASy - ENZYME nomenclature database: 4.1.99.5
            ExplorEnz - The Enzyme Database: 4.1.99.5
            ERGO genome analysis and discovery system: 4.1.99.5
            BRENDA, the Enzyme Database: 4.1.99.5
            CAS: 94185-90-7
///
ENTRY       EC 4.1.99.6       Obsolete  Enzyme
NAME        Transferred to 4.2.3.6
CLASS       Lyases;
            Carbon-carbon lyases;
            Other carbon-carbon lyases
COMMENT     Transferred entry: now EC 4.2.3.6 trichodiene synthase (EC 4.1.99.6
            created 1989, deleted 2000)
STRUCTURES  PDB: 1JFA  1JFG  1KIY  1KIZ  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.99.6
            ExPASy - ENZYME nomenclature database: 4.1.99.6
            ExplorEnz - The Enzyme Database: 4.1.99.6
            ERGO genome analysis and discovery system: 4.1.99.6
            BRENDA, the Enzyme Database: 4.1.99.6
///
ENTRY       EC 4.1.99.7       Obsolete  Enzyme
NAME        Transferred to 4.2.3.9
CLASS       Lyases;
            Carbon-carbon lyases;
            Other carbon-carbon lyases
COMMENT     Transferred entry: now EC 4.2.3.9 aristolochene synthase (EC
            4.1.99.7 created 1992 as EC 2.5.1.40, transferred 1999 to EC
            4.1.99.7, deleted 2000)
STRUCTURES  PDB: 1DGP  1DI1  1HX9  1HXA  1HXC  1HXG  
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.99.7
            ExPASy - ENZYME nomenclature database: 4.1.99.7
            ExplorEnz - The Enzyme Database: 4.1.99.7
            ERGO genome analysis and discovery system: 4.1.99.7
            BRENDA, the Enzyme Database: 4.1.99.7
///
ENTRY       EC 4.1.99.8       Obsolete  Enzyme
NAME        Transferred to 4.2.3.14
CLASS       Lyases;
            Carbon-carbon lyases;
            Other carbon-carbon lyases
COMMENT     Transferred entry: now EC 4.2.3.14 pinene synthase (EC 4.1.99.8
            created 2000, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.99.8
            ExPASy - ENZYME nomenclature database: 4.1.99.8
            ExplorEnz - The Enzyme Database: 4.1.99.8
            ERGO genome analysis and discovery system: 4.1.99.8
            BRENDA, the Enzyme Database: 4.1.99.8
///
ENTRY       EC 4.1.99.9       Obsolete  Enzyme
NAME        Transferred to 4.2.3.15
CLASS       Lyases;
            Carbon-carbon lyases;
            Other carbon-carbon lyases
COMMENT     Transferred entry: now EC 4.2.3.15 myrcene synthase (EC 4.1.99.9
            created 2000, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.99.9
            ExPASy - ENZYME nomenclature database: 4.1.99.9
            ExplorEnz - The Enzyme Database: 4.1.99.9
            ERGO genome analysis and discovery system: 4.1.99.9
            BRENDA, the Enzyme Database: 4.1.99.9
///
ENTRY       EC 4.1.99.10      Obsolete  Enzyme
NAME        Transferred to 4.2.3.16
CLASS       Lyases;
            Carbon-carbon lyases;
            Other carbon-carbon lyases
COMMENT     Transferred entry: now EC 4.2.3.16, (4S)-limonene synthase (EC
            4.1.99.10 created 2000, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.99.10
            ExPASy - ENZYME nomenclature database: 4.1.99.10
            ExplorEnz - The Enzyme Database: 4.1.99.10
            ERGO genome analysis and discovery system: 4.1.99.10
            BRENDA, the Enzyme Database: 4.1.99.10
///
ENTRY       EC 4.1.99.11                Enzyme
NAME        benzylsuccinate synthase;
            benzylsuccinate fumarate-lyase
CLASS       Lyases;
            Carbon-carbon lyases;
            Other carbon-carbon lyases
SYSNAME     benzylsuccinate fumarate-lyase (toluene-forming)
REACTION    benzylsuccinate = toluene + fumarate [RN:R05598]
ALL_REAC    R05598
SUBSTRATE   benzylsuccinate [CPD:C09816]
PRODUCT     toluene [CPD:C01455];
            fumarate [CPD:C00122]
COMMENT     A glycyl radical enzyme that is inhibited by benzyl alcohol,
            benzaldehyde, phenylhydrazine and is inactivated by oxygen.
REFERENCE   1  [PMID:9765580]
  AUTHORS   Beller HR, Spormann AM.
  TITLE     Analysis of the novel benzylsuccinate synthase reaction for
            anaerobic toluene activation based on structural studies of the
            product.
  JOURNAL   J. Bacteriol. 180 (1998) 5454-7.
  ORGANISM  Thauera aromatica
REFERENCE   2  [PMID:9632263]
  AUTHORS   Leuthner B, Leutwein C, Schulz H, Horth P, Haehnel W, Schiltz E,
            Schagger H, Heider J.
  TITLE     Biochemical and genetic characterization of benzylsuccinate synthase
            from Thauera aromatica: a new glycyl radical enzyme catalysing the
            first step in anaerobic toluene metabolism.
  JOURNAL   Mol. Microbiol. 28 (1998) 615-28.
  ORGANISM  Thauera aromatica
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
ORTHOLOGY   KO: K07540  benzylsuccinate synthase
GENES       EBA: c2A303(bssC) c2A304(bssA) c2A305(bssB)
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.99.11
            ExPASy - ENZYME nomenclature database: 4.1.99.11
            ExplorEnz - The Enzyme Database: 4.1.99.11
            ERGO genome analysis and discovery system: 4.1.99.11
            UM-BBD (Biocatalysis/Biodegradation Database): 4.1.99.11
            BRENDA, the Enzyme Database: 4.1.99.11
///
ENTRY       EC 4.1.99.12                Enzyme
NAME        3,4-dihydroxy-2-butanone-4-phosphate synthase;
            DHBP synthase;
            L-3,4-dihydroxybutan-2-one-4-phosphate synthase
CLASS       Lyases;
            Carbon-carbon lyases;
            Other carbon-carbon lyases
SYSNAME     D-ribulose 5-phosphate formate-lyase (L-3,4-dihydroxybutan-2-one
            4-phosphate-forming)
REACTION    D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one
            4-phosphate
SUBSTRATE   D-ribulose 5-phosphate [CPD:C00199]
PRODUCT     formate [CPD:C00058];
            L-3,4-dihydroxybutan-2-one 4-phosphate
COMMENT     Requires a divalent cation, preferably Mg2+, for activity [1]. The
            reaction involves an intramolecular skeletal rearrangement, with the
            bonds in D-ribulose 5-phosphate that connect C-3 and C-5 to C-4
            being broken, C-4 being removed as formate and reconnection of C-3
            and C-5 [1]. The phosphorylated four-carbon product
            (L-3,4-dihydroxybutan-2-one 4-phosphate) is an intermediate in the
            biosynthesis of riboflavin [1].
REFERENCE   1  [PMID:2246238]
  AUTHORS   Volk R, Bacher A.
  TITLE     Studies on the 4-carbon precursor in the biosynthesis of riboflavin.
            Purification and properties of
            L-3,4-dihydroxy-2-butanone-4-phosphate synthase.
  JOURNAL   J. Biol. Chem. 265 (1990) 19479-85.
REFERENCE   2  [PMID:11342130]
  AUTHORS   Liao DI, Calabrese JC, Wawrzak Z, Viitanen PV, Jordan DB.
  TITLE     Crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase
            of riboflavin biosynthesis.
  JOURNAL   Structure. 9 (2001) 11-8.
REFERENCE   3  [PMID:11687623]
  AUTHORS   Kelly MJ, Ball LJ, Krieger C, Yu Y, Fischer M, Schiffmann S,
            Schmieder P, Kuhne R, Bermel W, Bacher A, Richter G, Oschkinat H.
  TITLE     The NMR structure of the 47-kDa dimeric enzyme
            3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding
            studies reveal the location of the active site.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 13025-30.
REFERENCE   4  [PMID:11827524]
  AUTHORS   Liao DI, Zheng YJ, Viitanen PV, Jordan DB.
  TITLE     Structural definition of the active site and catalytic mechanism of
            3,4-dihydroxy-2-butanone-4-phosphate synthase.
  JOURNAL   Biochemistry. 41 (2002) 1795-806.
REFERENCE   5  [PMID:12200440]
  AUTHORS   Fischer M, Romisch W, Schiffmann S, Kelly M, Oschkinat H,
            Steinbacher S, Huber R, Eisenreich W, Richter G, Bacher A.
  TITLE     Biosynthesis of riboflavin in archaea studies on the mechanism of
            3,4-dihydroxy-2-butanone-4-phosphate synthase of Methanococcus
            jannaschii.
  JOURNAL   J. Biol. Chem. 277 (2002) 41410-6.
REFERENCE   6  [PMID:12904291]
  AUTHORS   Steinbacher S, Schiffmann S, Richter G, Huber R, Bacher A, Fischer
            M.
  TITLE     Structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase from
            Methanococcus jannaschii in complex with divalent metal ions and the
            substrate ribulose 5-phosphate: implications for the catalytic
            mechanism.
  JOURNAL   J. Biol. Chem. 278 (2003) 42256-65.
REFERENCE   7  [PMID:15213409]
  AUTHORS   Steinbacher S, Schiffmann S, Bacher A, Fischer M.
  TITLE     Metal sites in 3,4-dihydroxy-2-butanone 4-phosphate synthase from
            Methanococcus jannaschii in complex with the substrate ribulose
            5-phosphate.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 60 (2004) 1338-40.
REFERENCE   8  [PMID:15328619]
  AUTHORS   Echt S, Bauer S, Steinbacher S, Huber R, Bacher A, Fischer M.
  TITLE     Potential anti-infective targets in pathogenic yeasts: structure and
            properties of 3,4-dihydroxy-2-butanone 4-phosphate synthase of
            Candida albicans.
  JOURNAL   J. Mol. Biol. 341 (2004) 1085-96.
DBLINKS     IUBMB Enzyme Nomenclature: 4.1.99.12
            ExPASy - ENZYME nomenclature database: 4.1.99.12
            ExplorEnz - The Enzyme Database: 4.1.99.12
            ERGO genome analysis and discovery system: 4.1.99.12
            BRENDA, the Enzyme Database: 4.1.99.12
///
ENTRY       EC 4.1.99.-                 Enzyme
CLASS       Lyases;
            Carbon-carbon lyases;
            Other carbon-carbon lyases
REACTION    (1) 3-Oxo-4-methylpentanoic acid <=> (R)-3-Methyl-2-oxobutanoate +
            Acetate [RN:R05067];
            (2) Isochorismate <=> Salicylate + Pyruvate [RN:R06602];
            (3) 2-Methylnaphthalene + Fumarate <=> Naphthyl-2-methyl-succinic
            acid [RN:R06903]
SUBSTRATE   3-Oxo-4-methylpentanoic acid [CPD:C03467];
            Isochorismate [CPD:C00885];
            2-Methylnaphthalene [CPD:C14098];
            Fumarate [CPD:C00122]
PRODUCT     (R)-3-Methyl-2-oxobutanoate [CPD:C06004];
            Acetate [CPD:C00033];
            Salicylate [CPD:C00805];
            Pyruvate [CPD:C00022];
            Naphthyl-2-methyl-succinic acid [CPD:C14115]
///
ENTRY       EC 4.2.1.1                  Enzyme
NAME        carbonate dehydratase;
            carbonic anhydrase;
            anhydrase;
            carbonate anhydrase;
            carbonic acid anhydrase;
            carboxyanhydrase;
            carbonic anhydrase A;
            carbonate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     carbonate hydro-lyase (carbon-dioxide-forming)
REACTION    H2CO3 = CO2 + H2O [RN:R00132]
ALL_REAC    R00132
SUBSTRATE   H2CO3 [CPD:C01353]
PRODUCT     CO2 [CPD:C00011];
            H2O [CPD:C00001]
COFACTOR    Zinc [CPD:C00038]
COMMENT     A zinc protein.
REFERENCE   1
  AUTHORS   Keilin, D. and Mann, T.
  TITLE     Carbonic anhydrase.
  JOURNAL   Nature 144 (1939) 442-443.
REFERENCE   2  [PMID:2433278]
  AUTHORS   Murakami H, Sly WS.
  TITLE     Purification and characterization of human salivary carbonic
            anhydrase.
  JOURNAL   J. Biol. Chem. 262 (1987) 1382-8.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K01672  carbonic anhydrase
            KO: K01673  carbonic anhydrase
            KO: K01674  carbonic anhydrase
GENES       HSA: 11238(CA5B) 23632(CA14) 377677(CA13) 759(CA1) 760(CA2)
                 761(CA3) 762(CA4) 763(CA5A) 765(CA6) 766(CA7) 767(CA8)
                 768(CA9) 771(CA12)
            PTR: 450162(CA2) 454807(CA4) 464264(CA1) 469479(CA14)
            MCC: 709540(LOC709540)
            MMU: 12346(Car1) 12349(Car2) 12350(Car3) 12351(Car4) 12352(Car5a)
                 12353(Car6) 12354(Car7) 230099(Car9) 23831(Car14) 56078(Car5b)
                 76459(Car12)
            RNO: 29242(Ca4) 54231(Ca2) 54232(Ca3) 54233(Ca5a)
            CFA: 403503(CA6) 477928(CA2) 478333(CA12) 480591(CA4) 483180(CA14)
                 486453(CA5B) 486965(CA8) 487030(CA13) 487031(CA1) 487032(CA3)
                 608422(LOC608422) 609174(CA5A) 611933(CA9)
            BTA: 280740(CA2) 280741(CA4) 280742(CA6)
            SSC: 494016(CA3)
            GGA: 396257(CA2) 415370(CA12) 415791(CA7) 415833(CA5B) 417647(CA4)
                 420208(CA3) 428187(CA6)
            XLA: 379058(MGC52685) 379478(MGC64443) 379772(ca2)
                 414619(MGC81428) 446816(car13)
            XTR: 496646(ca8)
            DRE: 30331(cahz) 393786(ca7)
            SPU: 576041(LOC576041) 577690(LOC577690) 590675(LOC590675)
                 591885(LOC591885)
            DME: Dmel_CG11284 Dmel_CG12309 Dmel_CG5379 Dmel_CG6074
                 Dmel_CG6906(CAH2) Dmel_CG7820(CAH1) Dmel_CG9235
            CEL: K05G3.3(cah-3) R173.1(cah-5) T28F2.3(cah-6)
            OSA: 4326583 4329556
            CGR: CAGL0G01540g
            SPO: SPBP8B7.05c
            ANI: AN1805.2 AN5611.2
            AFM: AFUA_4G11250 AFUA_8G06550
            AOR: AO090003001096
            CNE: CNC04230 CNL04780
            UMA: UM00201.1
            DDI: DDBDRAFT_0203193 DDB_0191201(cahA)
            TET: TTHERM_00151140 TTHERM_00263620 TTHERM_00263670
                 TTHERM_00373840 TTHERM_00654260 TTHERM_00770610
                 TTHERM_01000160
            TBR: Tb11.01.0290
            LMA: LmjF06.0610
            EHI: 9.t00062
            ECO: b0126(yadF) b0339(cynT)
            ECJ: JW0122(can) JW0330(cynT)
            ECE: Z0137(yadF) Z0435(cynT)
            ECS: ECs0130 ECs0392
            ECC: c0155(yadF)
            ECI: UTI89_C0041(caiE) UTI89_C0139(yadF) UTI89_C1400(ychM)
            ECP: ECP_0134
            ECV: APECO1_1859(yadF)
            ECX: EcHS_A0130(can) EcHS_A0404(cynT)
            STY: STY0193(yadF)
            STT: t0176(yadF)
            SPT: SPA0174(yadF)
            SEC: SC0171(yadF) SCV48(mig5)
            STM: PSLT046 STM0171(yadF)
            YPE: YPO0819 YPO3407(yadF)
            YPK: y0779 y3207
            YPM: YP_0278(cynT1) YP_2837(cynT2)
            YPA: YPA_0450 YPA_2909
            YPN: YPN_0681 YPN_3023
            YPP: YPDSF_2948
            YPS: YPTB0724(yadF) YPTB3068
            YEN: YE0714(yadF)
            SFL: SF0123(yadF)
            SFX: S0125(yadF)
            SFV: SFV_0117(yadF)
            SSN: SSON_0134(yadF)
            SBO: SBO_0115(yadF)
            SDY: SDY_0035(yadF)
            ECA: ECA0257(cah) ECA3327
            PLU: plu0111(cynT) plu0867
            SGL: SG0483
            ENT: Ent638_0674 Ent638_1781 Ent638_3698 Ent638_4225
            SPE: Spro_0526 Spro_0566 Spro_1179 Spro_1380 Spro_1399 Spro_1417
                 Spro_1534 Spro_2274 Spro_2455 Spro_3099 Spro_3131 Spro_3137
                 Spro_3160 Spro_3178 Spro_3997 Spro_4422 Spro_4684 Spro_4864
            HIN: HI1301
            HIT: NTHI1614
            HDU: HD1365
            HSO: HS_0840(cah)
            PMU: PM0575 PM1905
            MSU: MS1065(cynT) MS1805(cah)
            APL: APL_0726
            ASU: Asuc_0215 Asuc_1199 Asuc_1311 Asuc_1536 Asuc_2095
            XFA: XF0880
            XFT: PD1800(yadF)
            XCC: XCC1419(cynT) XCC1530(cynT) XCC1556(yadF) XCC3991(ecaA)
            XCB: XC_2678 XC_2704 XC_2819 XC_4080
            XCV: XCV1519(cynT1) XCV1621(cynT2) XCV1646 XCV4165(ecaA)
            XAC: XAC1462(cynT) XAC1580(cynT) XAC1604(yadF) XAC4079(ecaA)
            XOO: XOO2423(yadF) XOO2457(cynT)
            XOM: XOO_2301(XOO2301) XOO_2327(XOO2327)
            VCH: VC0586 VCA0274
            VCO: VC0395_0957(cah)
            VVU: VV1_1637 VV2_1520
            VVY: VV2768 VVA0337
            VPA: VP2514 VPA0221 VPA1502
            VFI: VF1651 VF2174 VF2369
            PPR: PBPRA3179(yadF) PBPRA3376
            PAE: PA0102 PA2053(cynT) PA4676
            PAU: PA14_01240 PA14_37950(cynT) PA14_61860(yadF)
            PPU: PP_0100(cynT)
            PPF: Pput_0115 Pput_1198 Pput_2545 Pput_3304 Pput_4162 Pput_4522
            PST: PSPTO_0994 PSPTO_1340 PSPTO_5255(cynT)
            PSB: Psyr_0288 Psyr_0859
            PSP: PSPPH_0275(cynT) PSPPH_0890
            PFL: PFL_0058 PFL_1491 PFL_5235
            PFO: Pfl_0082 Pfl_2731 Pfl_3371 Pfl_4773
            PEN: PSEEN0053(cynT-2) PSEEN0054 PSEEN3120 PSEEN3600(cynT-1)
            PMY: Pmen_1528 Pmen_2006 Pmen_2017 Pmen_2204 Pmen_2205 Pmen_3029
                 Pmen_3753 Pmen_4475
            PAR: Psyc_0217
            PCR: Pcryo_0240
            PRW: PsycPRwf_1033
            ACI: ACIAD1056 ACIAD3384
            SON: SO_2474
            SDN: Sden_1811
            SFR: Sfri_1762
            SAZ: Sama_1642
            SBL: Sbal_2372
            SBM: Shew185_0361 Shew185_0642 Shew185_2360 Shew185_2409
                 Shew185_3048
            SLO: Shew_1859
            SPC: Sputcn32_2126
            SSE: Ssed_0631 Ssed_1224 Ssed_2421 Ssed_2586 Ssed_3576 Ssed_4232
            SPL: Spea_0266 Spea_0904 Spea_1113 Spea_1988 Spea_3212 Spea_3694
                 Spea_4209
            SHE: Shewmr4_1854
            SHM: Shewmr7_2124
            SHN: Shewana3_1909
            SHW: Sputw3181_1885
            ILO: IL1769
            CPS: CPS_3483
            PHA: PSHAa2765
            PAT: Patl_4260
            SDE: Sde_2395
            PIN: Ping_0390 Ping_1480
            MAQ: Maqu_1943
            CBU: CBU_0139
            CBD: COXBU7E912_1969
            LPN: lpg0697(sul1) lpg2194 lpg2500
            LPF: lpl0734 lpl1895 lpl2118 lpl2423
            LPP: lpp0752 lpp2143 lpp2569
            MCA: MCA1080(cah) MCA1442 MCA1665
            FTU: FTT0592(cynT)
            FTF: FTF0592(cynT)
            FTW: FTW_1137(cynT)
            FTL: FTL_0856
            FTH: FTH_0142 FTH_0845
            FTN: FTN_0144(paaY) FTN_1087(cynT)
            TCX: Tcr_0421 Tcr_1545
            NOC: Noc_1132
            AEH: Mlg_2421
            HCH: HCH_00805 HCH_04117 HCH_04901
            CSA: Csal_1874
            ABO: ABO_2361(yadF)
            MMW: Mmwyl1_0900 Mmwyl1_1754 Mmwyl1_2286 Mmwyl1_3712
            AHA: AHA_0375 AHA_0748 AHA_3404
            DNO: DNO_1085
            VOK: COSY_0883(cynT)
            NGO: NGO0574(cah)
            CVI: CV_0520 CV_1881(cynT)
            RSO: RS03010(RSp0112) RSc0277(RS03244)
            REU: Reut_A0030 Reut_A0137 Reut_B5007
            REH: H16_A0169(can) H16_B2270(can2) H16_B2403(caa)
            RME: Rmet_0105 Rmet_2078 Rmet_5185 Rmet_5605
            BMA: BMA0095 BMA1839 BMA2465(cynT)
            BMV: BMASAVP1_A0384(cynT) BMASAVP1_A1120 BMASAVP1_A3086
            BML: BMA10299_A0746 BMA10299_A1244(cynT) BMA10299_A2009
            BMN: BMA10247_2278 BMA10247_3322(cynT)
            BXE: Bxe_A3223 Bxe_A4254 Bxe_B1256 Bxe_B1257
            BVI: Bcep1808_2342 Bcep1808_3022 Bcep1808_5914 Bcep1808_6047
            BUR: Bcep18194_A5585 Bcep18194_A6270 Bcep18194_B0319
                 Bcep18194_B2816 Bcep18194_C6589 Bcep18194_C7283
            BCN: Bcen_1646 Bcen_2313 Bcen_4779 Bcen_4960
            BCH: Bcen2424_2257 Bcen2424_2927 Bcen2424_3200 Bcen2424_3388
            BAM: Bamb_2296 Bamb_2976 Bamb_5945
            BPS: BPSL0372 BPSL1203 BPSL2949(cynT)
            BPM: BURPS1710b_0580 BURPS1710b_1425(sul1) BURPS1710b_1426
            BPL: BURPS1106A_0418 BURPS1106A_3463(cynT)
            BPD: BURPS668_0397 BURPS668_3426(cynT)
            BTE: BTH_I0345 BTH_I1052 BTH_I1199
            PNU: Pnuc_0412 Pnuc_2030
            BPE: BP3425
            BPA: BPP0404 BPP2082
            BBR: BB0406 BB1478
            RFR: Rfer_3841
            POL: Bpro_4189 Bpro_4590
            PNA: Pnap_0456 Pnap_3756
            AAV: Aave_0666 Aave_2100 Aave_4370
            AJS: Ajs_0441 Ajs_3778
            VEI: Veis_1332
            MPT: Mpe_A1703 Mpe_A3369
            HAR: HEAR1076 HEAR2507 HEAR2644(yadF)
            MMS: mma_2596(cynT1) mma_2880(cynT2)
            NEU: NE0606(cah) NE1926
            NET: Neut_1628
            NMU: Nmul_A0461 Nmul_A0465
            EBA: ebA2817(can) ebA3637
            AZO: azo0842(ecaA) azo3977
            DAR: Daro_0099 Daro_2091
            TBD: Tbd_2167(ecaA)
            HPY: HP0004(icfA) HP1186
            HPJ: jhp0004(icfA) jhp1112
            HPA: HPAG1_0004 HPAG1_1126
            HHE: HH0040(icfA) HH0921
            HAC: Hac_0257(cynT) Hac_0392(cah)
            WSU: WS0293(cynT)
            TDN: Tmden_0162 Tmden_1236
            CJE: Cj0237(cynT)
            CJR: CJE0288(cynT)
            CJJ: CJJ81176_0262(cynT)
            CJU: C8J_0215(cynT)
            CJD: JJD26997_0235(cynT)
            CCO: CCC13826_0771(cynT)
            ABU: Abu_0103(cynT1) Abu_0253(cynT2)
            NIS: NIS_0309 NIS_0329 NIS_0368
            SUN: SUN_0389 SUN_1170
            GSU: GSU0067 GSU1442 GSU2307
            GME: Gmet_1242 Gmet_3517
            GUR: Gura_2001
            PCA: Pcar_1988 Pcar_2939
            PPD: Ppro_2975
            DVU: DVU1777(cynT)
            DVL: Dvul_1380
            DDE: Dde_2979
            LIP: LI0467(cynT)
            BBA: Bd1735 Bd2259(cah)
            DPS: DP0850 DP0937
            AFW: Anae109_2841 Anae109_3210 Anae109_3640 Anae109_3657
            MXA: MXAN_0617 MXAN_4783(cynT)
            SAT: SYN_02875
            PUB: SAR11_0815(cynT)
            MLO: mll6384 mlr4135
            MES: Meso_3223
            PLA: Plav_2223 Plav_3061
            SME: SMa0045(cah) SMc04083(cynT)
            SMD: Smed_0366 Smed_0393 Smed_0600 Smed_0839 Smed_1261 Smed_2350
                 Smed_3185 Smed_3490 Smed_4450 Smed_5272 Smed_5722 Smed_5891
                 Smed_6140 Smed_6327
            ATU: Atu2488(cah)
            ATC: AGR_C_4521
            RET: RHE_CH01064 RHE_CH04103(cynT) RHE_PD00192(ypd00041)
            RLE: RL0273 RL3777 RL4718(cynT) pRL100447
            BME: BMEI0222 BMEII0502
            BMF: BAB1_1837 BAB2_0449
            BMS: BR1829 BRA0788
            BMB: BruAb2_0444
            BOV: BOV_A0739
            OAN: Oant_0793 Oant_1074 Oant_1277 Oant_2858 Oant_2880 Oant_3009
                 Oant_4247
            BJA: bll1137(cah) bll2065(icfA) bll4863 bll4865 blr0500(cah)
            BRA: BRADO0360 BRADO6744(acaP)
            BBT: BBta_0346 BBta_0791(acaP) BBta_6172
            RPA: RPA0232 RPA0794(acaP) RPA0799
            RPB: RPB_0340 RPB_4620 RPB_4625
            RPC: RPC_0234 RPC_0758
            RPD: RPD_0495 RPD_0785 RPD_0790
            RPE: RPE_0341 RPE_0718
            NWI: Nwi_2792
            NHA: Nham_0361 Nham_3592
            BHE: BH16050(cynT)
            BBK: BARBAKC583_0067
            XAU: Xaut_0322 Xaut_0972 Xaut_2228 Xaut_2936 Xaut_3293 Xaut_3337
                 Xaut_4148
            CCR: CC_3569 CC_3572
            SIL: SPO3715
            SIT: TM1040_3457
            RSP: RSP_1377
            RSH: Rsph17029_0045
            RSQ: Rsph17025_0036
            JAN: Jann_0108
            RDE: RD1_0312(cynT)
            PDE: Pden_2705
            MMR: Mmar10_1165 Mmar10_2700
            HNE: HNE_0015 HNE_1567
            ZMO: ZMO1133
            NAR: Saro_1920 Saro_2617
            SAL: Sala_1282
            SWI: Swit_0240 Swit_2233 Swit_2812 Swit_3085 Swit_4265
            ELI: ELI_06325
            GOX: GOX1785
            GBE: GbCGDNIH1_0056 GbCGDNIH1_1902
            ACR: Acry_0666 Acry_1284 Acry_2777 Acry_3428
            RRU: Rru_A1725 Rru_A2056
            MAG: amb0581 amb4241
            MGM: Mmc1_2491
            ABA: Acid345_1911 Acid345_3139 Acid345_3958
            SUS: Acid_1160
            BHA: BH0360(cah)
            BAN: BA5049
            BAR: GBAA5049
            BAA: BA_5466
            BAT: BAS4689
            BCE: BC4791
            BCA: BCE_4948
            BCZ: BCZK4546(can)
            BTK: BT9727_4527(can)
            BTL: BALH_4362(can)
            BLD: BLi00271 BLi03211(ytiB)
            BCL: ABC2875 ABC3182
            BAY: RBAM_027700(ytiB) RBAM_031920(yvdA)
            BPU: BPUM_2707(ytiB) BPUM_3106
            LMO: lmo0811
            LMF: LMOf2365_0827(cah)
            LIN: lin0807
            LWE: lwe0806(cah)
            SPZ: M5005_Spy_0201
            SPH: MGAS10270_Spy0200
            SPI: MGAS10750_Spy0196
            SPJ: MGAS2096_Spy0214 MGAS2096_Spy0215
            SPK: MGAS9429_Spy0202
            SPF: SpyM50180
            SPA: M6_Spy0232
            SPB: M28_Spy0195
            SAK: SAK_0162
            SMU: SMU.1595(cah)
            STC: str1658(cah)
            STL: stu1658(cah)
            SSA: SSA_2154
            LPL: lp_2736(cah)
            LDB: Ldb0475
            LBU: LBUL_0423
            LBR: LVIS_2247
            LCA: LSEI_0650
            EFA: EF1711
            OOE: OEOE_0238
            CAC: CAC2482
            CPF: CPF_0414
            CPR: CPR_0410
            CKL: CKL_0534
            DSY: DSY1528
            MTU: Rv3273 Rv3588c
            MTC: MT3373 MT3694(cynT)
            MBO: Mb3301 Mb3619c
            MBB: BCG_1343(canA) BCG_3302 BCG_3653c(canB)
            MLE: ML1919 ML2279
            MPA: MAP0470 MAP4060c
            MAV: MAV_0565
            MSM: MSMEG_4985 MSMEG_6082
            MMC: Mmcs_4745
            CGL: NCgl0119(cgl0120) NCgl2579(cgl2670)
            CGB: cg2954(cynT)
            CEF: CE2527
            CDI: DIP1979
            CJK: jk0303(bca)
            NFA: nfa4300 pnf1540
            RHA: RHA1_ro04449 RHA1_ro06403 RHA1_ro08296
            SCO: SCO3721(SCH35.03) SCO6055(SC9B1.02c)
            SMA: SAV2210(cynT1) SAV5657(cynT2)
            LXX: Lxx16790(cynT)
            CMI: CMM_2232(cynT)
            ART: Arth_3333
            NCA: Noca_0359
            FRA: Francci3_3245
            FAL: FRAAL4724
            SEN: SACE_2046(cynT)
            BLO: BL0616(icfA)
            BAD: BAD_0012(icfA)
            RBA: RB11063(sul1) RB4267
            PCU: pc0930(cynT) pc1058(cynT)
            LIL: LA0579(icfA)
            SYN: slr0051(ecaB) slr1347(icfA)
            SYW: SYNW2467
            SYC: syc0110_c(icfA) syc0167_c
            SYF: Synpcc7942_1388 Synpcc7942_1447
            SYE: Syncc9902_2275
            SYG: sync_0948
            SYR: SynRCC307_2433
            GVI: glr0945 glr2088(ecaB)
            ANA: all2910 all2929(ecaA)
            AVA: Ava_0973 Ava_0990 Ava_0991 Ava_2165
            CHU: CHU_0303(yadF) CHU_1041(cab)
            GFO: GFO_3420
            FJO: Fjoh_4763
            FPS: FP2029(cynT)
            CCH: Cag_1171
            DRA: DR_2238
            DGE: Dgeo_2193
            MMP: MMP1299
            MAC: MA1098(camH)
            MMA: MM_2151 MM_3088
            MTP: Mthe_0684
            MHU: Mhun_1281 Mhun_1824
            MEM: Memar_0986
            MBN: Mboo_0316
            MTH: MTH1582
            HAL: VNG0841G(icfA)
            HMA: rrnAC0751(icfA1)
            RCI: RCIX2375(cah-1) RCIX2393(cah-2)
            PAI: PAE3678
STRUCTURES  PDB: 12CA  1A42  1AM6  1AVN  1AZM  1BCD  1BIC  1BN1  1BN3  1BN4  
                 1BNM  1BNN  1BNQ  1BNT  1BNU  1BNV  1BNW  1BV3  1BZM  1CA2  
                 1CA3  1CAH  1CAI  1CAJ  1CAK  1CAL  1CAM  1CAN  1CAO  1CAY  
                 1CAZ  1CCS  1CCT  1CCU  1CIL  1CIM  1CIN  1CNB  1CNC  1CNG  
                 1CNH  1CNI  1CNJ  1CNK  1CNW  1CNX  1CNY  1CRA  1CRM  1CVA  
                 1CVB  1CVC  1CVD  1CVE  1CVF  1CVH  1CZM  1DCA  1DCB  1DDZ  
                 1DMX  1DMY  1EKJ  1EOU  1F2W  1FLJ  1FQL  1FQM  1FQN  1FQR  
                 1FR4  1FR7  1FSN  1FSQ  1FSR  1G0E  1G0F  1G1D  1G3Z  1G45  
                 1G46  1G48  1G4J  1G4O  1G52  1G53  1G54  1G5C  1G6V  1H4N  
                 1H9N  1H9Q  1HCA  1HCB  1HEA  1HEB  1HEC  1HED  1HUG  1HUH  
                 1HVA  1I6O  1I6P  1I8Z  1I90  1I91  1I9L  1I9M  1I9N  1I9O  
                 1I9P  1I9Q  1IF4  1IF5  1IF6  1IF7  1IF8  1IF9  1J9W  1JCZ  
                 1JD0  1JV0  1KEQ  1KOP  1KOQ  1KWQ  1KWR  1LG5  1LG6  1LGD  
                 1LUG  1LZV  1MOO  1MUA  1OKL  1OKM  1OKN  1OQ5  1RAY  1RAZ  
                 1RJ5  1RJ6  1RZA  1RZB  1RZC  1RZD  1RZE  1T75  1T9N  1TB0  
                 1TBT  1TE3  1TEQ  1TEU  1TG3  1TG9  1TH9  1THJ  1THK  1TTM  
                 1UGA  1UGB  1UGC  1UGD  1UGE  1UGF  1UGG  1URT  1V3W  1V67  
                 1V9E  1V9I  1XEG  1XEV  1XPZ  1XQ0  1Y7W  1YDA  1YDB  1YDC  
                 1YDD  1YM3  1YO0  1YO1  1YO2  1Z93  1Z97  1Z9Y  1ZE8  1ZFK  
                 1ZFQ  1ZGE  1ZGF  1ZH9  1ZNC  1ZSA  1ZSB  1ZSC  2A5V  2A8C  
                 2A8D  2ABE  2AW1  2AX2  2CA2  2CAB  2CBA  2CBB  2CBC  2CBD  
                 2CBE  2ESF  2EU2  2EU3  2EZ7  2F14  2FGY  2FKO  2FMG  2FMZ  
                 2FNK  2FNM  2FNN  2FOQ  2FOS  2FOU  2FOV  2FOY  2FW4  2GD8  
                 2GEH  2H15  2H4N  2HD6  2HFW  2HFX  2HFY  2HKK  2HL4  2HNC  
                 2HOC  2ILI  2IT4  2NMX  2NN1  2NN7  2NNG  2NNO  2NNS  2NNV  
                 2NWO  2NWP  2NWY  2NWZ  2NXR  2NXS  2NXT  2O4Z  2POU  2POV  
                 2POW  2Q1B  2Q1Q  2Q38  2ZNC  3CA2  3ZNC  4CA2  4CAC  5CA2  
                 5CAC  6CA2  7CA2  8CA2  9CA2  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.1
            ExPASy - ENZYME nomenclature database: 4.2.1.1
            ExplorEnz - The Enzyme Database: 4.2.1.1
            ERGO genome analysis and discovery system: 4.2.1.1
            BRENDA, the Enzyme Database: 4.2.1.1
            CAS: 9001-03-0
///
ENTRY       EC 4.2.1.2                  Enzyme
NAME        fumarate hydratase;
            fumarase;
            L-malate hydro-lyase;
            (S)-malate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (S)-malate hydro-lyase (fumarate-forming)
REACTION    (S)-malate = fumarate + H2O [RN:R01082]
ALL_REAC    R01082
SUBSTRATE   (S)-malate [CPD:C00149]
PRODUCT     fumarate [CPD:C00122];
            H2O [CPD:C00001]
REFERENCE   1
  AUTHORS   Alberty, R.A.
  TITLE     Fumarase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 5, Academic Press, New York, 1961, p. 531-544.
REFERENCE   2  [PMID:14247669]
  AUTHORS   KANAREK L, HILL RL.
  TITLE     THE PREPARATION AND CHARACTERIZATION OF FUMARASE FROM SWINE HEART
            MUSCLE.
  JOURNAL   J. Biol. Chem. 239 (1964) 4202-6.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00720  Reductive carboxylate cycle (CO2 fixation)
            PATH: map05211  Renal cell carcinoma
ORTHOLOGY   KO: K01675  fumarate hydratase
            KO: K01676  fumarate hydratase, class I
            KO: K01677  fumarate hydratase alpha subunit
            KO: K01678  fumarate hydratase beta subunit
            KO: K01679  fumarate hydratase
GENES       HSA: 2271(FH)
            MMU: 14194(Fh1)
            RNO: 24368(Fh1)
            CFA: 480092(FH)
            BTA: 520260(MGC140701)
            GGA: 420969(FH)
            DRE: 393938(zgc:66253)
            SPU: 577019(LOC577019) 580992(LOC580992)
            DME: Dmel_CG4094(l(1)G0255)
            CEL: H14A12.2(fum-1)
            ATH: AT2G47510(FUM1) AT5G50950
            OSA: 4332774
            CME: CMD058C
            SCE: YPL262W(FUM1)
            AGO: AGOS_ACR013C
            PIC: PICST_74587(FUM2) PICST_85745(FUM1)
            CAL: CaO19_6724(CaO19.6724)
            CGR: CAGL0A01045g
            SPO: SPCC18.18c
            ANI: AN8707.2
            AFM: AFUA_6G02470
            AOR: AO090120000133
            CNE: CNC01700
            UMA: UM00787.1
            PFA: PFI1340w
            TAN: TA03430
            TPV: TP03_0078
            TET: TTHERM_01308050
            TBR: Tb11.02.2700 Tb927.3.4500
            TCR: 507257.60 507669.10 509879.40 510329.270
            LMA: LmjF24.0320 LmjF29.1960
            EHI: 200.t00005
            ECO: b1611(fumC) b1612(fumA) b4122(fumB)
            ECJ: JW1603(fumC) JW1604(fumA) JW4083(fumB)
            ECE: Z0887 Z2614(fumC) Z2615(fumA) Z5724(fumB)
            ECS: ECs0757 ECs2317 ECs2318 ECs5104
            ECC: c2003(fumC) c2004(fumA) c5127(fumB)
            ECI: UTI89_C1799(fumC) UTI89_C1800(fumA) UTI89_C4715(fumB)
            ECP: ECP_1555 ECP_1556 ECP_4364
            ECV: APECO1_2330(fumB) APECO1_694(fumC) APECO1_695(fumA)
            ECW: EcE24377A_1818(fumC) EcE24377A_1820(fumA)
                 EcE24377A_4676(fumB)
            ECX: EcHS_A1686(fumC) EcHS_A1687(fumA) EcHS_A4363(fumB)
            STY: STY1653(fumC) STY1654(fumA) STY4499(fumB)
            STT: t1336(fumA) t1337(fumC) t4207(fumB)
            SPT: SPA1386(fumC) SPA1387(fumA) SPA4118(fumB)
            SEC: SC0760(fumB) SC0761(fumA) SC1485(fumA) SC1486(fumC)
                 SC4179(fumB)
            STM: STM0761 STM0762 STM1468(fumA) STM1469(fumC) STM4300(fumB)
            YPE: YPO2264(fumC) YPO3335(fumA)
            YPK: y0854(fumA) y2106(fumC)
            YPM: YP_0352(fumA) YP_2061(fumC)
            YPA: YPA_1624 YPA_2809
            YPN: YPN_0758 YPN_1736
            YPS: YPTB0796(fumA) YPTB2186(fumC)
            YPI: YpsIP31758_1873(fumC) YpsIP31758_3271
            YEN: YE4036(fumB)
            SFL: SF1634(fumC) SF1635(fumA) SF4101(fumB)
            SFX: S1765(fumC) S1766(fumA) S3629(fumB)
            SFV: SFV_1627(fumC) SFV_1628(fumA) SFV_4108(fumB)
            SSN: SSON_1548(fumA) SSON_1549(fumC) SSON_4299(fumB)
            SBO: SBO_1524(fumA) SBO_1525(fumC) SBO_4326(fumB)
            SDY: SDY_1827(fumC) SDY_1828(fumA) SDY_4231(fumB)
            ECA: ECA0904(fumA) ECA2262(fumC)
            PLU: plu2359(fumC)
            WBR: WGLp341(fumC)
            SGL: SG1462
            BFL: Bfl373(fumC)
            BPN: BPEN_384(fumC)
            HIN: HI1398(fumC)
            HIT: NTHI1749(fumC)
            HIP: CGSHiEE_04580(fumC)
            HIQ: CGSHiGG_00765(fumC)
            HDU: HD1986(fumC)
            HSO: HS_1102(fumC)
            PMU: PM0823(fumC)
            MSU: MS0760(fumC)
            APL: APL_1757(fumC)
            XFA: XF1554 XF1855
            XFT: PD0763(fumC) PD0947(fumB)
            XCC: XCC1416(fumB) XCC1494(fumC)
            XCB: XC_2742 XC_2822
            XCV: XCV1517 XCV1585(fumC)
            XAC: XAC1460(fumB) XAC1542(fumC)
            XOO: XOO2057(fumC) XOO2336(fumB)
            XOM: XOO_1937(XOO1937) XOO_2216(XOO2216)
            VCH: VC1304 VC1573
            VCO: VC0395_A1177(fumC)
            VVU: VV1_2266
            VVY: VV2079
            VPA: VP1873 VP2873
            VFI: VF1180
            PPR: PBPRA2409 PBPRB0402
            PAE: PA0854(fumC2) PA4333 PA4470(fumC1)
            PAU: PA14_53220(fumC2) PA14_56300(fumA) PA14_58030(fumC1)
            PAP: PSPA7_4665(fumC)
            PPU: PP_0897 PP_0944(fumC-1) PP_1755(fumC-2)
            PST: PSPTO_1731(fumC-1) PSPTO_4339 PSPTO_4461(fumC-2)
            PSB: Psyr_3661 Psyr_4031
            PSP: PSPPH_3681(fumC1) PSPPH_4041 PSPPH_4160(fumC2)
            PFL: PFL_0907(fumC) PFL_2140(fumC) PFL_4328(fumC) PFL_4801
            PFO: Pfl_0849 Pfl_4093 Pfl_4452
            PEN: PSEEN1085(fumC-1) PSEEN1145 PSEEN1474(fumC)
            PAR: Psyc_1657(fumC)
            PCR: Pcryo_1894
            ACI: ACIAD0538(fumA) ACIAD1890(fumC)
            SON: SO_2222
            SDN: Sden_1650 Sden_1912
            SFR: Sfri_0229 Sfri_2156
            SAZ: Sama_1688
            SBL: Sbal_1918
            SLO: Shew_1904
            SHE: Shewmr4_2124
            SHM: Shewmr7_2200
            SHN: Shewana3_2302
            SHW: Sputw3181_2218
            ILO: IL0937(fumC) IL1705(fumB)
            CPS: CPS_3613
            PHA: PSHAa0048(fumC) PSHAa1166(fumB)
            PAT: Patl_1628
            SDE: Sde_1992
            PIN: Ping_1977
            MAQ: Maqu_2035
            CBU: CBU_1096(fumC)
            CBD: COXBU7E912_1197(fumC)
            LPN: lpg2937(fum)
            LPF: lpl2866(fumC)
            LPP: lpp3005(fumC)
            MCA: MCA1543
            FTU: FTT0306(fumC) FTT1600c(fumA)
            FTF: FTF0306(fumC) FTF1600c(fumA)
            FTW: FTW_0335(fumA) FTW_1779(fumC)
            FTL: FTL_0217 FTL_0525
            FTH: FTH_0212(fumC) FTH_0524(fumA)
            FTA: FTA_0233(fumC)
            FTN: FTN_0220(fumC) FTN_0337(fumA)
            TCX: Tcr_1384
            NOC: Noc_1627
            AEH: Mlg_1359 Mlg_2412
            HCH: HCH_00016(fumC) HCH_04987
            CSA: Csal_1834 Csal_2108
            ABO: ABO_1540(fumA) ABO_2749
            AHA: AHA_2434 AHA_3294(fumC)
            DNO: DNO_0506(fumC)
            BCI: BCI_0420(fumC)
            RMA: Rmag_0793
            VOK: COSY_0719(fumB)
            NME: NMB1458 NMB1613
            NMA: NMA1670(fumC) NMA1812(fumA)
            NMC: NMC1396(fumC) NMC1534(fumA)
            NGO: NGO1029(fumC)
            CVI: CV_1120(fumC) CV_3476(fumA)
            RSO: RSc1955(fumA) RSp1279(fumC)
            REU: Reut_A2232 Reut_B5517
            REH: H16_A2528(fumA) H16_B0103(fumC)
            RME: Rmet_2273 Rmet_5471 Rmet_5472 Rmet_5754 Rmet_5756
            BMA: BMA0493(fumC) BMAA1797
            BMV: BMASAVP1_0793 BMASAVP1_A2515(fumC)
            BML: BMA10299_1085 BMA10299_A0889(fumC)
            BMN: BMA10247_0259(fumC) BMA10247_A2058
            BXE: Bxe_A1038 Bxe_A3136
            BUR: Bcep18194_A4203
            BCN: Bcen_5883
            BCH: Bcen2424_1090 Bcen2424_2194
            BAM: Bamb_0966 Bamb_2233
            BPS: BPSL2469(fumC) BPSS0372
            BPM: BURPS1710b_2940(fumC) BURPS1710b_A1936(fumA)
            BPL: BURPS1106A_2886(fumC) BURPS1106A_A0527
            BPD: BURPS668_2826(fumC) BURPS668_A0624
            BTE: BTH_I1685 BTH_II2020
            PNU: Pnuc_1139
            BPE: BP0248(fumC)
            BPA: BPP0352 BPP0353 BPP3619(fumC) BPP3646
            BBR: BB0355 BB0356 BB4054(fumC) BB4081
            RFR: Rfer_2365 Rfer_2583
            POL: Bpro_2046 Bpro_2047
            PNA: Pnap_2882 Pnap_2883
            AAV: Aave_1489
            AJS: Ajs_1056 Ajs_1057
            VEI: Veis_3214
            MPT: Mpe_A1382 Mpe_A3332
            HAR: HEAR2526(fumC)
            MMS: mma_0880(fumB) mma_2613(fumC)
            NEU: NE2286(fumC)
            NET: Neut_2124
            NMU: Nmul_A2471
            EBA: ebA173(fumA) ebA3735(fumC)
            AZO: azo0698(fumC) azo2415(fumB)
            DAR: Daro_1627 Daro_2935
            MFA: Mfla_1918
            HPY: HP1325(fumC)
            HPJ: jhp1245(fumC)
            HPA: HPAG1_1270
            HHE: HH0722(fumC) HH1792(ttdA) HH1793(ttdB)
            HAC: Hac_0131(fumC)
            WSU: WS1766(fumB_alpha) WS1767(fumB_beta)
            TDN: Tmden_1049
            CJE: Cj1364c(fumC)
            CJR: CJE1556(fumC)
            CJJ: CJJ81176_1366(fumC)
            CJU: C8J_1282(fumC)
            CJD: JJD26997_0285(fumC)
            CFF: CFF8240_0965(fumC)
            CCV: CCV52592_0433 CCV52592_1795(fumC)
            CHA: CHAB381_0024(fumB)
            CCO: CCC13826_0208(ttdA)
            ABU: Abu_0719(fumC) Abu_1928(fumA)
            SUN: SUN_0575(fumC)
            GSU: GSU0994(fumB)
            GME: Gmet_2570
            PCA: Pcar_0324
            DVU: DVU0080(fumC) DVU3264 DVU3265
            DDE: Dde_0240 Dde_1254 Dde_1255 Dde_3638 Dde_3639
            LIP: LI0293(fumB) LI0294(fumA)
            BBA: Bd1318 Bd2151(fumB)
            DPS: DP2387 DP2952
            ADE: Adeh_0264 Adeh_2068
            MXA: MXAN_3162(fumB) MXAN_6439(fumC)
            SAT: SYN_00158 SYN_00159
            SFU: Sfum_2102 Sfum_2336
            RPR: RP665(fumC)
            RTY: RT0657(fumC)
            RCO: RC1012(fumC)
            RFE: RF_0273(fumC)
            RBE: RBE_1067(fumC)
            RAK: A1C_05130(fumC)
            RBO: A1I_02010(fumC)
            RCM: A1E_04395(fumC)
            RRI: A1G_05585(fumC)
            OTS: OTBS_0663(fumC)
            WOL: WD0492(fumC)
            WBM: Wbm0504
            AMA: AM937(fumC)
            APH: APH_0247(fumC)
            ERU: Erum6330(fumC)
            ERW: ERWE_CDS_06640(fumC)
            ERG: ERGA_CDS_06550(fumC)
            ECN: Ecaj_0637
            ECH: ECH_0376(fumC)
            NSE: NSE_0056(fumC)
            PUB: SAR11_0012(fumC)
            MLO: mll8172 mlr6099
            MES: Meso_0056 Meso_0355
            SME: SMc00149(fumC)
            ATU: Atu1616(fumC)
            ATC: AGR_C_2979
            RET: RHE_CH02383(fumC) RHE_CH02385(fumB)
            RLE: RL2701(fumC) RL2703(fumA)
            BME: BMEI1016 BMEII1051
            BMF: BAB1_0977 BAB2_0186(fumC)
            BMS: BR0961(fumB) BRA0192(fumC)
            BMB: BruAb1_0967(fumB) BruAb2_0187(fumC)
            BOV: BOV_0951(fumB) BOV_A0174(fumC)
            BJA: bll0286(fumC) bll5796 blr6519(fumC)
            BRA: BRADO5016(fumA) BRADO5584(fumC)
            BBT: BBta_5483(fumA) BBta_6106(fumC)
            RPA: RPA1329(fumC1) RPA3500(fumC2) RPA3876(fumA)
            RPB: RPB_2030 RPB_3762
            RPC: RPC_1533 RPC_3271
            RPD: RPD_1708 RPD_3360
            RPE: RPE_1571 RPE_2144
            NWI: Nwi_2353
            NHA: Nham_2732
            BHE: BH13550(fumC)
            BQU: BQ10770(fumC)
            BBK: BARBAKC583_1174(fumC)
            CCR: CC_2109
            SIL: SPO1498 SPO1905(fumC)
            SIT: TM1040_1452
            RSP: RSP_2138(fumC)
            RSH: Rsph17029_0812
            JAN: Jann_2394
            RDE: RD1_2273(fumC)
            PDE: Pden_1908 Pden_4119
            MMR: Mmar10_2046
            HNE: HNE_2950(fumC)
            ZMO: ZMO1307(fumA)
            NAR: Saro_0188 Saro_1696
            SAL: Sala_0374 Sala_3152
            ELI: ELI_12905
            GOX: GOX1643
            GBE: GbCGDNIH1_1041 GbCGDNIH1_1807
            RRU: Rru_A2129
            MAG: amb1331 amb3650
            ABA: Acid345_2742
            SUS: Acid_4293
            BSU: BG10384(citG)
            BHA: BH0894 BH1445(citB)
            BAN: BA0423(fumA) BA1767(fumC)
            BAR: GBAA0423(fumA) GBAA1767(fumC)
            BAA: BA_1000 BA_2277
            BAT: BAS0410 BAS1637
            BCE: BC0466 BC1712
            BCA: BCE_0539(fumA) BCE_1841(fumC)
            BCZ: BCZK0397(fumA) BCZK1587(fumC)
            BTK: BT9727_0401(fumA) BT9727_1617(fumC)
            BTL: BALH_0422(fumA)
            BLI: BL00732(citG)
            BLD: BLi03486(citG)
            BCL: ABC1746(citG)
            BAY: RBAM_030160(citG)
            BPU: BPUM_2957(fumC)
            OIH: OB1132
            GKA: GK0250 GK0426
            SAU: SA1669(citG)
            SAV: SAV1851(citG)
            SAM: MW1792(citG)
            SAR: SAR1942(citG)
            SAS: SAS1772
            SAC: SACOL1908(fumC)
            SAB: SAB1784c(citG)
            SAA: SAUSA300_1801(fumC)
            SAO: SAOUHSC_01983
            SEP: SE1532
            SER: SERP1387(fumC)
            SHA: SH1111(citG)
            SSP: SSP0944
            LMO: lmo2225(citG)
            LMF: LMOf2365_2258(fumC)
            LIN: lin2328(citG)
            LWE: lwe2242(fumC)
            LPL: lp_1112(fum)
            LJO: LJ1405
            LAC: LBA0907
            LSL: LSL_1327(fumC)
            LDB: Ldb2086(fumC)
            LBU: LBUL_1930
            LBR: LVIS_0714
            LCA: LSEI_2410
            OOE: OEOE_0029
            STH: STH2535 STH2536 STH2641 STH2642
            CAC: CAC3090 CAC3091
            CTC: CTC02561 CTC02562
            CNO: NT01CX_2053
            CDF: CD1003(fumA) CD1004(fumB)
            CBO: CBO3441(fumA') CBO3442(fumA)
            CBE: Cbei_0189
            CKL: CKL_0303(fumA) CKL_0304(fumB)
            AMT: Amet_3413
            CHY: CHY_0061 CHY_0062 CHY_1374
            DSY: DSY3229 DSY3230
            CSC: Csac_2759
            TTE: TTE0075(ttdA) TTE0076(fumA)
            MTA: Moth_2282 Moth_2283
            MTU: Rv1098c(fum)
            MTC: MT1130(fum)
            MBO: Mb1128c(fum)
            MBB: BCG_1158c(fum)
            MLE: ML1947(fum)
            MPA: MAP2693(fum)
            MSM: MSMEG_2985 MSMEG_5240
            MMC: Mmcs_4122
            CGL: NCgl0967(fumC)
            CGB: cg1145(fum)
            CEF: CE1071
            CDI: DIP0938(fumC)
            CJK: jk1454(fum)
            NFA: nfa32060(fumA) nfa48010(fumC)
            RHA: RHA1_ro05864(fumC) RHA1_ro05899 RHA1_ro08824
            SCO: SCO5042(fumC) SCO5044(fumB)
            SMA: SAV3218(fumB) SAV3221(fumC)
            LXX: Lxx16800
            CMI: CMM_2233(fumC)
            AAU: AAur_1299(fumC)
            PAC: PPA2292
            TFU: Tfu_0459
            FRA: Francci3_3882
            FAL: FRAAL6152(fumC)
            SEN: SACE_0930(fumC) SACE_1784(fumB)
            RXY: Rxyl_2748 Rxyl_2749 Rxyl_2866
            RBA: RB7623(fumC)
            CTR: CT855(fumC)
            CTA: CTA_0932(fumC)
            CMU: TC0244
            CPN: CPn1013(fumC)
            CPA: CP0840
            CPJ: CPj1013(fumC)
            CPT: CpB1051
            CCA: CCA00748(fumC)
            CAB: CAB715(fumR)
            CFE: CF0267(fumC)
            PCU: pc1660(fumC)
            TDE: TDE1520 TDE1521
            LIL: LA0185(fum)
            LIC: LIC10162(fumC)
            LBJ: LBJ_0153(fumC)
            LBL: LBL_2930(fumC)
            SYN: slr0018(fumC)
            SYW: SYNW0637(fumC)
            SYC: syc0538_d
            SYF: Synpcc7942_1007
            SYD: Syncc9605_2041
            SYE: Syncc9902_0628
            SYG: sync_2336(fumC)
            SYR: SynRCC307_1940(fumC)
            SYX: SynWH7803_2039(fumC)
            TEL: tll1534
            ANA: alr3724
            AVA: Ava_3556
            PMA: Pro1620(fumC)
            PMM: PMM1466(fumC)
            PMT: PMT1485(fumC)
            PMN: PMN2A_0997
            PMI: PMT9312_1559
            PMB: A9601_16681(fumC)
            PMC: P9515_16461(fumC)
            PMF: P9303_04621(fumC)
            PMG: P9301_16561(fumC)
            PMH: P9215_17341(fumC)
            PME: NATL1_18661(fumC)
            TER: Tery_1328
            BTH: BT_2256
            BFR: BF0676
            BFS: BF0601(fumB)
            PGI: PG1417(fumB)
            SRU: SRU_1611
            CHU: CHU_3285(fumB) CHU_3664(fumC)
            GFO: GFO_1808(fumC)
            FPS: FP1606(fumC)
            CTE: CT0833(fumA)
            CCH: Cag_0860
            PLT: Plut_1269
            DET: DET0453 DET0454
            DEH: cbdb_A411 cbdb_A413
            DEB: DehaBAV1_0430
            DRA: DR_2627
            DGE: Dgeo_2328
            TTH: TTC0190
            TTJ: TTHA0558
            AAE: aq_1679(fumX) aq_1780(fumB)
            TMA: TM0540 TM0541
            TPT: Tpet_0381
            MJA: MJ0617 MJ1294
            MMP: MMP0130(fumA) MMP1548
            MMZ: MmarC7_1129
            MAE: Maeo_0629
            MVN: Mevan_1135
            MAC: MA1001 MA2497(fumA) MA2498(fumB)
            MBA: Mbar_A0425 Mbar_A2417 Mbar_A2418
            MMA: MM_3066 MM_3067
            MBU: Mbur_0250 Mbur_0251
            MHU: Mhun_0089 Mhun_0090
            MTH: MTH1115 MTH1735 MTH1910 MTH963
            MST: Msp_0338 Msp_0791
            MSI: Msm_0563 Msm_0769
            MKA: MK0085(ttdA) MK0086(fumA)
            AFU: AF1098(fum-1) AF1099(fum-2)
            HAL: VNG1356G(fumC)
            HMA: rrnAC0028(fumC)
            HWA: HQ2471A(fumC)
            NPH: NP3778A(fumC)
            TAC: Ta0258
            TVO: TVN1336
            PTO: PTO0427
            PHO: PH1683 PH1684
            PAB: PAB2030(fum-1) PAB2031(fum-2)
            PFU: PF1754 PF1755
            TKO: TK1964 TK1965
            RCI: RCIX2056(fumB) RCIX2057(fumA)
            APE: APE_1816.1
            IHO: Igni_0678
            SSO: SSO1077(fumC)
            STO: ST2023
            SAI: Saci_0122(fumC)
            MSE: Msed_1116
            PAI: PAE2131 PAE2132 PAE2743
STRUCTURES  PDB: 1FUO  1FUP  1FUQ  1FUR  1KQ7  1VDK  1YFE  1YFM  2FUS  2ISB  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.2
            ExPASy - ENZYME nomenclature database: 4.2.1.2
            ExplorEnz - The Enzyme Database: 4.2.1.2
            ERGO genome analysis and discovery system: 4.2.1.2
            BRENDA, the Enzyme Database: 4.2.1.2
            CAS: 9032-88-6
///
ENTRY       EC 4.2.1.3                  Enzyme
NAME        aconitate hydratase;
            cis-aconitase;
            aconitase;
            AcnB;
            2-methylaconitate hydratase;
            citrate(isocitrate) hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     citrate(isocitrate) hydro-lyase (cis-aconitate-forming)
REACTION    (1) citrate = isocitrate [RN:R01324];
            (2) (1a) citrate = cis-aconitate + H2O [RN:R01325];
            (3) (1b) cis-aconitate + H2O = isocitrate [RN:R01900]
ALL_REAC    R01324 R01325 R01900
SUBSTRATE   citrate [CPD:C00158];
            cis-aconitate [CPD:C00417];
            H2O [CPD:C00001]
PRODUCT     isocitrate [CPD:C00311];
            cis-aconitate [CPD:C00417];
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023];
            Sulfur [CPD:C00087];
            Iron-sulfur [CPD:C00824]
COMMENT     Besides interconverting citrate and cis-aconitate, it also
            interconverts cis-aconitate with isocitrate and, hence,
            interconverts citrate and isocitrate. The equilibrium mixture is 91%
            citrate, 6% isocitrate and 3% aconitate. cis-Aconitate is used to
            designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. An
            iron-sulfur protein, containing a [4Fe-4S] cluster to which the
            substrate binds.
REFERENCE   1
  AUTHORS   Dickman, S.R.
  TITLE     Aconitase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K (Eds.), The Enzymes, 2nd
            ed., vol. 5, Academic Press, New York, 1961, p. 495-510.
REFERENCE   2  [PMID:13126098]
  AUTHORS   MORRISON JF.
  TITLE     The purification of aconitase.
  JOURNAL   Biochem. J. 56 (1954) 99-105.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:8151704]
  AUTHORS   Lauble H, Kennedy MC, Beinert H, Stout CD.
  TITLE     Crystal structures of aconitase with trans-aconitate and
            nitrocitrate bound.
  JOURNAL   J. Mol. Biol. 237 (1994) 437-51.
  ORGANISM  cow [GN:bta], pig [GN:ssc]
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00630  Glyoxylate and dicarboxylate metabolism
            PATH: map00720  Reductive carboxylate cycle (CO2 fixation)
ORTHOLOGY   KO: K01680  aconitate hydratase
            KO: K01681  aconitate hydratase 1
            KO: K01682  aconitate hydratase 2
GENES       HSA: 48(ACO1) 50(ACO2)
            MMU: 11428(Aco1) 11429(Aco2)
            RNO: 50655(Aco1) 79250(Aco2)
            CFA: 474487(ACO2) 481576(ACO1)
            BTA: 280976(ACO2)
            SSC: 396999(ACO2)
            GGA: 374009(ACO2)
            XLA: 380269(ratireb) 398139(LOC398139)
            XTR: 496933(aco2)
            DRE: 322670(aco2)
            SPU: 577783(LOC577783) 586198(LOC586198)
            DME: Dmel_CG4706 Dmel_CG4900(Irp-1A) Dmel_CG6342(Irp-1B)
                 Dmel_CG9244(Acon)
            CEL: F54H12.1(aco-2) ZK455.1(aco-1)
            ATH: AT4G26970 AT4G35830
            OSA: 4331547 4340833
            CME: CMT561C
            SCE: YJL200C(ACO2) YLR304C(ACO1)
            AGO: AGOS_ADL032W AGOS_AFR629W
            PIC: PICST_85181(ACO1) PICST_90724(ACO2)
            CAL: CaO19.13953(aco2) CaO19_6385(CaO19.6385)
            CGR: CAGL0D06424g CAGL0F02431g
            SPO: SPAC24C9.06c SPBP4H10.15
            ANI: AN3894.2 AN5300.2 AN5525.2
            AFM: AFUA_1G06810 AFUA_6G12930
            AOR: AO090001000484 AO090001000642 AO090003000415 AO090005000045
            CNE: CND02620 CNG01590 CNM01770
            UMA: UM02691.1 UM02899.1
            DDI: DDB_0229908(acnA) DDB_0230168(acnB)
            PFA: PF13_0229
            TAN: TA17020
            TPV: TP01_1050
            TET: TTHERM_00037470 TTHERM_00191800
            TBR: Tb10.61.2880
            TCR: 511277.290
            LMA: LmjF18.0510
            ECO: b0118(acnB) b1276(acnA)
            ECJ: JW0114(acnB) JW1268(acnA)
            ECE: Z0128(acnB) Z2532(acnA)
            ECS: ECs0122 ECs1849
            ECC: c0147(acnB) c1745(acnA)
            ECI: UTI89_C0131(acnB) UTI89_C1547(acnA)
            ECP: ECP_0125 ECP_0784 ECP_1329
            ECV: APECO1_1867(acnB) APECO1_436(acnA)
            ECW: EcE24377A_0120(acnB) EcE24377A_1478(acnA)
            ECX: EcHS_A0122 EcHS_A1387
            STY: STY0181(acnB) STY1339(acnA)
            STT: t0164(acnB) t1625(acnA)
            SPT: SPA0162(acnB) SPA1164(acnA)
            SEC: SC0157(acnB) SC1707(acnA)
            STM: STM0158(acnB) STM1712(acnA)
            YPE: YPO2221(acnA) YPO3415(acnB)
            YPK: y0771(acnB) y2063(acnA)
            YPM: YP_0270(acnB) YP_2019(acnA)
            YPA: YPA_1580 YPA_2917
            YPN: YPN_0673 YPN_1689
            YPP: YPDSF_2940
            YPS: YPTB0716(acnB) YPTB2143(acnA)
            YPI: YpsIP31758_1920(acnA) YpsIP31758_3359(acnB)
            SFL: SF0115(acnB) SF1280(acnA)
            SFX: S0117(acnB) S1363(acnA)
            SFV: SFV_0109(acnB) SFV_1289(acnA)
            SSN: SSON_0126(acnB) SSON_1864(acnA)
            SBO: SBO_0107(acnB)
            SDY: SDY_0025(acnB)
            ECA: ECA1941(acnA) ECA3778(acnB)
            PLU: plu2432(acnA) plu3619(acnB)
            SGL: SG0477
            ENT: Ent638_0665 Ent638_2192
            KPN: KPN_01272(acnA)
            HSO: HS_1270(acnB)
            PMU: PM0204(acnB)
            MSU: MS2369(acnB)
            XFA: XF0290 XF0292
            XFT: PD0234(rpfA)
            XCC: XCC1033(acnA) XCC1860(rpfA) XCC1863(acnB)
            XCB: XC_2326 XC_2329 XC_3213
            XCV: XCV1158(acnA) XCV1924(acnA) XCV1927(acnB)
            XAC: XAC1139(acnA) XAC1882(rpfA) XAC1885(acnB)
            XOO: XOO0894(acnA) XOO2862(acnB) XOO2865(rpfA)
            XOM: XOO_0819(XOO0819) XOO_2717(XOO2717) XOO_2720(XOO2720)
            VCH: VC0604 VC1338
            VCO: VC0395_A0133(acnB) VC0395_A0954(acnA)
            VVU: VV1_1653 VV1_2730
            VVY: VV1531 VV2753
            VPA: VP1646 VP2495
            VFI: VF2158
            PPR: PBPRA3191
            PAE: PA0794 PA1562(acnA) PA1787(acnB)
            PAU: PA14_41470(acnB) PA14_44290(acnA)
            PAP: PSPA7_3517(acnB) PSPA7_3768(acnA)
            PPU: PP_2112(acnA) PP_2336 PP_2339(acnB)
            PPF: Pput_3434
            PST: PSPTO_2016(acnA) PSPTO_2289 PSPTO_3752(acnB)
            PSB: Psyr_1726 Psyr_2087 Psyr_3404
            PSP: PSPPH_2058(acnD) PSPPH_3326(acnA) PSPPH_3558(acnB)
            PFL: PFL_1929(acnA) PFL_2633(acnB)
            PFO: Pfl_1766 Pfl_3395 Pfl_3890
            PEN: PSEEN1905 PSEEN1908(acnB) PSEEN3756(acnA)
            PMY: Pmen_1903
            PAR: Psyc_0751(acnB) Psyc_1112 Psyc_2061(acnA)
            PCR: Pcryo_0746 Pcryo_1309 Pcryo_2384
            ACI: ACIAD2395(acnB) ACIAD2755(acnA) ACIAD3090(acnA)
            SON: SO_0343(acnA) SO_0432(acnB)
            SDN: Sden_1666 Sden_3377
            SFR: Sfri_0230 Sfri_1859 Sfri_3771
            SAZ: Sama_0382
            SBL: Sbal_3905
            SLO: Shew_3424
            SPC: Sputcn32_3409
            SHE: Shewmr4_0437 Shewmr4_3631
            SHM: Shewmr7_0313 Shewmr7_3592
            SHN: Shewana3_0338 Shewana3_0433 Shewana3_3827
            SHW: Sputw3181_0534
            ILO: IL0468(acnB) IL1425 IL1533(acnA)
            CPS: CPS_2820 CPS_4800(acnB) CPS_4802
            PHA: PSHAa0159(acnA) PSHAa0184(acnB) PSHAa1773(acnA)
            PAT: Patl_1284 Patl_1421 Patl_3428
            SDE: Sde_1893
            PIN: Ping_2899
            MAQ: Maqu_1859 Maqu_3674
            CBU: CBU_1720(acnA)
            CBD: COXBU7E912_0285(acnA)
            LPN: lpg1690(acnA)
            LPF: lpl1653(acnA)
            LPP: lpp1659(acnA)
            MCA: MCA2485
            FTU: FTT0087(acnA)
            FTF: FTF0087(acnA)
            FTW: FTW_0164(acnA)
            FTL: FTL_1772
            FTH: FTH_1708(acnA)
            FTA: FTA_1878(acnA)
            FTN: FTN_1623(acnA)
            TCX: Tcr_1142
            NOC: Noc_1788 Noc_2103 Noc_2707
            AEH: Mlg_1453 Mlg_1454 Mlg_2603
            HHA: Hhal_1406
            HCH: HCH_02149(acnB) HCH_06874(acnA)
            CSA: Csal_2058 Csal_2962
            ABO: ABO_0694(acnA) ABO_1201(acnB) ABO_1431(acnA)
            AHA: AHA_3856(acnB)
            RMA: Rmag_0992
            VOK: COSY_0887(acnB)
            NME: NMB0433 NMB1572
            NMA: NMA1761(acnB) NMA2052(acnA)
            NMC: NMC1492(acnB) NMC1729(acnA)
            NGO: NGO1231
            CVI: CV_1121(acnA1) CV_2054(acnA2) CV_2470(acnB)
            RSO: RSc2003(acnA1) RSp0120(acnA2) RSp0330(acnA3) RSp0332(acnB)
            REU: Reut_A1810 Reut_A2331 Reut_B3464
            REH: H16_A1907(acnM) H16_A2638(acnA) H16_B0568(acnB)
            RME: Rmet_1585 Rmet_2492 Rmet_5296
            BMA: BMAA1755(acnA) BMAA1868(acnM)
            BMV: BMASAVP1_0877(acnM) BMASAVP1_1615(acnA)
            BML: BMA10299_1164(acnM) BMA10299_1823(acnA)
            BMN: BMA10247_A0493(acnA) BMA10247_A2141(acnM)
            BXE: Bxe_B1533 Bxe_B2301 Bxe_B2903
            BVI: Bcep1808_5672
            BUR: Bcep18194_B0143 Bcep18194_B1125 Bcep18194_B2158
            BCN: Bcen_3672 Bcen_4439
            BCH: Bcen2424_3928 Bcen2424_4695
            BAM: Bamb_3305 Bamb_5692
            BPS: BPSS0208(acnA) BPSS1726(citB)
            BPM: BURPS1710b_A0800(acnA)
            BPL: BURPS1106A_A2340(acnA)
            BPD: BURPS668_A2478(acnA)
            BTE: BTH_II0654(acnA)
            PNU: Pnuc_0942
            BPE: BP2014(acnA) BP2021(acnB) BP2369(acnA)
            BPA: BPP1126(acnA) BPP2394(acnA) BPP2400(acnB) BPP3235(acnA)
            BBR: BB1342(acnA) BB1844(acnA) BB1850(acnB) BB3687(acnA)
            RFR: Rfer_1806 Rfer_2366
            POL: Bpro_3592 Bpro_3595 Bpro_3871
            PNA: Pnap_3027
            AAV: Aave_2210
            AJS: Ajs_2787
            VEI: Veis_4358
            MPT: Mpe_A1358 Mpe_A1363
            HAR: HEAR1783(acnA)
            MMS: mma_1501
            NEU: NE1002(acnA1)
            NET: Neut_2457
            NMU: Nmul_A0875
            EBA: ebA5264(acnA) ebA5265(acnB) ebA6773(acnA2)
            AZO: azo1533(acnA) azo1534(acnB)
            DAR: Daro_2882
            TBD: Tbd_0891
            MFA: Mfla_1817
            HPY: HP0779(acnB)
            HPJ: jhp0716(acnB)
            HPA: HPAG1_0764
            HHE: HH1737(acnB)
            HAC: Hac_0644(acnB)
            WSU: WS1187(acnB)
            TDN: Tmden_1040
            CJE: Cj0835c(acnB)
            CJR: CJE0922(acnB)
            CJJ: CJJ81176_0852(acnB)
            CJU: C8J_0782(acnB)
            CJD: JJD26997_0985(acnB) JJD26997_1179(acnB)
            CFF: CFF8240_0997(acnB)
            CCV: CCV52592_1414
            CHA: CHAB381_1421(acnB)
            CCO: CCC13826_1408(acnB)
            ABU: Abu_0278(acnA) Abu_1439(acnB)
            NIS: NIS_0828(acnB)
            SUN: SUN_1350(acnB)
            GSU: GSU0846(acnA) GSU1660(acnB) GSU2445
            GME: Gmet_1016 Gmet_1912 Gmet_2763
            GUR: Gura_1265
            PCA: Pcar_2165 Pcar_2450
            PPD: Ppro_1692
            DVU: DVU1064
            DDE: Dde_1406
            BBA: Bd2784(leuC) Bd3178(acnA)
            DPS: DP0128
            ADE: Adeh_1179 Adeh_3665
            MXA: MXAN_1363(acnA)
            SAT: SYN_01409
            SFU: Sfum_2106
            RPR: RP799(acnA)
            RTY: RT0786(acnA)
            RCO: RC1233(acnA)
            RFE: RF_1264(acnA)
            RBE: RBE_0098(acnA)
            RAK: A1C_06180
            RBO: A1I_07445
            RCM: A1E_05095
            RRI: A1G_06750
            WOL: WD0105(acnA)
            WBM: Wbm0540
            AMA: AM1032(acnA)
            APH: APH_1117(acnA)
            ERU: Erum7920(acnA)
            ERW: ERWE_CDS_08380(acnA)
            ERG: ERGA_CDS_08270(acnA)
            ECN: Ecaj_0828
            ECH: ECH_1031(acnA)
            NSE: NSE_0600(acnA)
            PUB: SAR11_1324(acnA)
            MLO: mlr4335
            MES: Meso_3357
            SME: SMc03846(acnA)
            ATU: Atu2685(acnA) Atu4734(acnB)
            ATC: AGR_C_4866 AGR_L_294
            RET: RHE_CH03944(acnA)
            RLE: RL4536(acnA)
            BME: BMEI1855
            BMF: BAB1_0090
            BMS: BR0093(acnA)
            BMB: BruAb1_0090(acnA)
            BOV: BOV_0091(acnA)
            BJA: bll0466(acnA)
            BRA: BRADO0393(acnA)
            BBT: BBta_0382(acnA)
            RPA: RPA0202(acnA)
            RPB: RPB_0291
            RPC: RPC_0204
            RPD: RPD_0525
            RPE: RPE_0310
            NWI: Nwi_0323
            NHA: Nham_0408 Nham_0914
            BHE: BH01160(acnA)
            BQU: BQ01090(acnA)
            BBK: BARBAKC583_1282(acnA)
            CCR: CC_3667
            SIL: SPO2312(acnA)
            SIT: TM1040_1006 TM1040_1026
            RSP: RSP_1806
            JAN: Jann_2646
            RDE: RD1_2555(acnA)
            MMR: Mmar10_2861
            HNE: HNE_3514(acnA)
            ZMO: ZMO0543(acnA)
            NAR: Saro_0425
            SAL: Sala_2096
            ELI: ELI_10400
            GOX: GOX1335
            GBE: GbCGDNIH1_0404
            RRU: Rru_A3511
            MAG: amb3651 amb4400
            MGM: Mmc1_1566
            ABA: Acid345_0224
            BSU: BG10478(citB)
            BHA: BH2299(citB)
            BAN: BA3677(acnA)
            BAR: GBAA3677(acnA)
            BAA: BA_4163
            BAT: BAS3408
            BCE: BC3616
            BCA: BCE_3635(acnA)
            BCZ: BCZK3320(citB)
            BTK: BT9727_3370(citB)
            BTL: BALH_3253
            BLI: BL02940(citB)
            BLD: BLi02047(citB)
            BCL: ABC2157(citB)
            BAY: RBAM_017800(citB)
            BPU: BPUM_1699(citB)
            OIH: OB1681(citB)
            GKA: GK1347(citB)
            GTN: GTNG_1206
            SAU: SA1184(citB)
            SAV: SAV1350(citB)
            SAM: MW1237(citB)
            SAR: SAR1362(citB)
            SAS: SAS1289
            SAC: SACOL1385(acnA)
            SAB: SAB1207(citB)
            SAA: SAUSA300_1246(acnA)
            SAO: SAOUHSC_01347
            SEP: SE1032
            SER: SERP0921(acnA)
            SHA: SH1558(citB)
            SSP: SSP1408
            LMO: lmo1641(citB)
            LMF: LMOf2365_1662(acnA)
            LIN: lin1682(citB)
            LWE: lwe1657(acnA)
            LLA: L68478(citB)
            LLM: llmg_0636(citB)
            SMU: SMU.670(citB)
            STC: str1268(citB)
            STL: stu1268(citB)
            SSA: SSA_0702(citB)
            SGO: SGO_1613(acnA)
            STH: STH3164
            CAC: CAC0971(citB)
            CNO: NT01CX_0140
            CKL: CKL_0974
            DSY: DSY4204(acnA)
            TTE: TTE0473(acnA)
            MTA: Moth_1882
            MTU: Rv1475c(acn)
            MTC: MT1522(acnA)
            MBO: Mb1511c(acn)
            MBB: BCG_1537c(acn)
            MLE: ML1814(acn)
            MPA: MAP1201c(acn)
            MAV: MAV_3303(acnA)
            MSM: MSMEG_1112 MSMEG_3143(acnA)
            MMC: Mmcs_2449
            MKM: Mkms_2494
            MJL: Mjls_2486
            CGL: NCgl1482(cgl1540)
            CGB: cg1737(acn)
            CEF: CE1661(acn)
            CDI: DIP1283(acnA)
            CJK: jk0969(acn)
            NFA: nfa34830(acn)
            RHA: RHA1_ro02399(acnA1) RHA1_ro07207(acnA2) RHA1_ro08266(acnA3)
            SCO: SCO5999(sacA)
            SMA: SAV2258(acnA)
            LXX: Lxx10440
            CMI: CMM_1659(acnA)
            ART: Arth_1644
            AAU: AAur_1789(acnA)
            PAC: PPA1061
            NCA: Noca_2876
            TFU: Tfu_1925
            FRA: Francci3_1312
            FAL: FRAAL2064(acnA) FRAAL3285
            SEN: SACE_3754(acnA1) SACE_3811(acn) SACE_4339(acnA)
            BLO: BL1397(acn)
            BAD: BAD_1052(acn)
            RXY: Rxyl_0618 Rxyl_2824
            RBA: RB2114(citB)
            PCU: pc0865(acnB)
            LIL: LB327(acn)
            LIC: LIC20249(acnA)
            LBJ: LBJ_4240(acnA)
            LBL: LBL_4254(acnA)
            SYN: slr0665(acnB)
            SYW: SYNW2500(acnB)
            SYC: syc0637_d(acnB)
            SYF: Synpcc7942_0903
            SYD: Syncc9605_2667
            SYE: Syncc9902_2296
            SYG: sync_2910(acnB)
            SYR: SynRCC307_2508(acnB)
            SYX: SynWH7803_2505(acnB)
            CYA: CYA_1444(acnB)
            CYB: CYB_1587(acnB)
            TEL: tlr0693
            GVI: glr4087
            ANA: all1267
            AVA: Ava_0569
            PMA: Pro1866(acnB)
            PMM: PMM1700(acnB)
            PMT: PMT2249(acnB)
            PMN: PMN2A_1308
            PMI: PMT9312_1793
            PMB: A9601_19101(acnB)
            PMC: P9515_18911(acnB)
            PMF: P9303_29981(acnB)
            PMG: P9301_18911(acnB)
            PMH: P9215_19731
            PME: NATL1_21811(acnB)
            TER: Tery_0664
            BTH: BT_2072
            BFR: BF3755
            BFS: BF3543(acn)
            SRU: SRU_1477 SRU_1866(acnA)
            CHU: CHU_2223(acnA)
            GFO: GFO_1390(acnA) GFO_1602 GFO_2504(acnA)
            FJO: Fjoh_1952
            FPS: FP1164(acnA)
            CTE: CT0543(acn)
            CCH: Cag_1286
            CPH: Cpha266_0803
            PVI: Cvib_0598
            PLT: Plut_0556
            DRA: DR_1720
            DGE: Dgeo_1682
            TTH: TTC0374
            TTJ: TTHA0726
            AAE: aq_1784(aco)
            MAC: MA0250
            MBA: Mbar_A0714
            MMA: MM_1528
            MBU: Mbur_0316
            HAL: VNG2574G(can)
            HMA: pNG6049(acnA) rrnAC2158(acnB)
            HWA: HQ3117A(citB)
            NPH: NP0404A(citB_1) NP1994A(citB_2)
            TAC: Ta0112
            TVO: TVN0189
            PTO: PTO0935
            PFU: PF0201
            APE: APE_1618.1
            SSO: SSO1095
            STO: ST0833
            SAI: Saci_1214(acnA)
            PAI: PAE1499
STRUCTURES  PDB: 1ACO  1AMI  1AMJ  1B0J  1B0K  1B0M  1C96  1C97  1FGH  1L5J  
                 1NIS  1NIT  2B3X  2B3Y  2IPY  5ACN  6ACN  7ACN  8ACN  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.3
            ExPASy - ENZYME nomenclature database: 4.2.1.3
            ExplorEnz - The Enzyme Database: 4.2.1.3
            ERGO genome analysis and discovery system: 4.2.1.3
            BRENDA, the Enzyme Database: 4.2.1.3
            CAS: 9024-25-3
///
ENTRY       EC 4.2.1.4                  Enzyme
NAME        citrate dehydratase;
            citrate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     citrate hydro-lyase (cis-aconitate-forming)
REACTION    citrate = cis-aconitate + H2O [RN:R01325]
ALL_REAC    R01325
SUBSTRATE   citrate [CPD:C00158]
PRODUCT     cis-aconitate [CPD:C00417];
            H2O [CPD:C00001]
COMMENT     cis-Aconitate is used to designate the isomer
            (Z)-prop-1-ene-1,2,3-tricarboxylate. Does not act on isocitrate.
REFERENCE   1  [PMID:13239639]
  AUTHORS   NEILSON NE.
  TITLE     The aconitase of Aspergillus niger.
  JOURNAL   Biochim. Biophys. Acta. 17 (1955) 139-40.
  ORGANISM  Aspergillus niger
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.4
            ExPASy - ENZYME nomenclature database: 4.2.1.4
            ExplorEnz - The Enzyme Database: 4.2.1.4
            ERGO genome analysis and discovery system: 4.2.1.4
            BRENDA, the Enzyme Database: 4.2.1.4
            CAS: 9024-39-9
///
ENTRY       EC 4.2.1.5                  Enzyme
NAME        arabinonate dehydratase;
            D-arabinonate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     D-arabinonate hydro-lyase (2-dehydro-3-deoxy-D-arabinonate-forming)
REACTION    D-arabinonate = 2-dehydro-3-deoxy-D-arabinonate + H2O [RN:R03032]
ALL_REAC    R03032
SUBSTRATE   D-arabinonate [CPD:C00878]
PRODUCT     2-dehydro-3-deoxy-D-arabinonate [CPD:C03826];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:13376619]
  AUTHORS   DOUDOROFF M, PALLERONI NJ.
  TITLE     Characterization and properties of 2-keto-3-deoxy-D-arabonic acid.
  JOURNAL   J. Biol. Chem. 223 (1956) 499-508.
  ORGANISM  Pseudomonas saccharophila
ORTHOLOGY   KO: K01683  
GENES       CCR: CC_3093
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.5
            ExPASy - ENZYME nomenclature database: 4.2.1.5
            ExplorEnz - The Enzyme Database: 4.2.1.5
            ERGO genome analysis and discovery system: 4.2.1.5
            BRENDA, the Enzyme Database: 4.2.1.5
            CAS: 9024-36-6
///
ENTRY       EC 4.2.1.6                  Enzyme
NAME        galactonate dehydratase;
            D-galactonate dehydrase;
            D-galactonate dehydratase;
            D-galactonate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     D-galactonate hydro-lyase (2-dehydro-3-deoxy-D-galactonate-forming)
REACTION    D-galactonate = 2-dehydro-3-deoxy-D-galactonate + H2O [RN:R03033]
ALL_REAC    R03033
SUBSTRATE   D-galactonate [CPD:C00880]
PRODUCT     2-dehydro-3-deoxy-D-galactonate [CPD:C01216];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:13462997]
  AUTHORS   DE LEY J, DOUDOROFF M.
  TITLE     The metabolism of D-galactose in Pseudomonas saccharophila.
  JOURNAL   J. Biol. Chem. 227 (1957) 745-57.
  ORGANISM  Pseudomonas saccarophila
PATHWAY     PATH: map00052  Galactose metabolism
ORTHOLOGY   KO: K01684  galactonate dehydratase
GENES       AFM: AFUA_1G05520
            CNE: CNI02060
            ECO: b4478(dgoD)
            ECJ: JW5629(dgoD)
            ECI: UTI89_C4243(dgoA)
            SEC: SC3745(dgoA)
            STM: STM3828(dgoA)
            ECA: ECA4416(dgoA1) ECA4417(dgoA2)
            XCC: XCC1746(dgoA)
            XCB: XC_2488
            XCV: XCV1796(dgoD)
            XAC: XAC1765(dgoA)
            XOO: XOO2919(dgoA)
            XOM: XOO_2769(XOO2769)
            VVY: VVA1580
            PST: PSPTO_2179
            PSB: Psyr_1989
            PSP: PSPPH_1958(dgoD)
            PFO: Pfl_4123
            RSO: RSc2751(dgoAb)
            BMA: BMA0254(dgoA)
            BXE: Bxe_A0656
            BUR: Bcep18194_A5994
            BAM: Bamb_2719
            BPS: BPSL0699
            BPM: BURPS1710b_0918(dgoA)
            BTE: BTH_I0611
            RFR: Rfer_0951
            SME: SMb20510(dgoA)
            RET: RHE_CH03697(dgoA)
            RLE: RL3850(dgoD) RL4233
            BME: BMEII0356
            BMF: BAB2_0294
            BMB: BruAb2_0293
            RDE: RD1_0679 RD1_0686
            BLI: BL03851
            BLD: BLi04070
            BCL: ABC0524
            OIH: OB2215
            GKA: GK1955
            MSM: MSMEG_6177
            SCO: SCO3475(SCE65.11c)
            TFU: Tfu_1786
            SEN: SACE_2636
            DGE: Dgeo_2811
            HMA: rrnAC3069(dgoA3)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.6
            ExPASy - ENZYME nomenclature database: 4.2.1.6
            ExplorEnz - The Enzyme Database: 4.2.1.6
            ERGO genome analysis and discovery system: 4.2.1.6
            BRENDA, the Enzyme Database: 4.2.1.6
            CAS: 9024-38-8
///
ENTRY       EC 4.2.1.7                  Enzyme
NAME        altronate dehydratase;
            D-altronate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     D-altronate hydro-lyase (2-dehydro-3-deoxy-D-gluconate-forming)
REACTION    D-altronate = 2-dehydro-3-deoxy-D-gluconate + H2O [RN:R01540]
ALL_REAC    R01540
SUBSTRATE   D-altronate [CPD:C00817]
PRODUCT     2-dehydro-3-deoxy-D-gluconate [CPD:C00204];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:13831814]
  AUTHORS   SMILEY JD, ASHWELL G.
  TITLE     Uronic acid metabolism in bacteria. III. Purification and properties
            of D-altronic acid and D-mannonic acid dehydrases in Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 235 (1960) 1571-5.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K01685  altronate hydrolase
GENES       ECO: b3091(uxaA)
            ECJ: JW3062(uxaA)
            ECE: Z4444(uxaA)
            ECS: ECs3973
            ECC: c3849(uxaA)
            ECI: UTI89_C3529(uxaA)
            ECP: ECP_3182
            ECW: EcE24377A_3559(uxaA)
            ECX: EcHS_A3274(uxaA)
            STY: STY0700 STY0701
            STT: t2217 t2218
            SPT: SPA2084 SPA2085
            SEC: SC0679(uxaA)
            STM: STM0649.S STM0650
            YPE: YPO0581(uxaA)
            YPK: y3598(uxaA)
            YPM: YP_2901(uxaA)
            YPA: YPA_3207
            YPN: YPN_0450
            YPP: YPDSF_0368
            YPS: YPTB3476(uxaA)
            YPI: YpsIP31758_0493(uxaA)
            SFL: SF3131(uxaA)
            SFX: S3338(uxaA)
            SFV: SFV_3132(uxaA)
            SSN: SSON_3244(uxaA)
            SDY: SDY_3276(uxaA)
            ECA: ECA0647(uxaA)
            ENT: Ent638_3545
            SPE: Spro_4320
            MSU: MS0530(uxaA)
            ASU: Asuc_0154
            PPR: PBPRB1517(uxaA)
            PPU: PP_2834
            PPF: Pput_2855
            PAT: Patl_0800
            SDE: Sde_0955
            CSA: Csal_1735 Csal_1749 Csal_1766
            MMW: Mmwyl1_0495
            RSO: RSp1615(uxaA)
            REU: Reut_B3529 Reut_B4278 Reut_B5298 Reut_C6087 Reut_C6356
                 Reut_C6357
            REH: H16_A2758 H16_B0321
            BXE: Bxe_A4448 Bxe_B2960 Bxe_B2961
            BCN: Bcen_6467
            BCH: Bcen2424_6702
            BAM: Bamb_1221
            BPS: BPSS0789 BPSS0790
            BPM: BURPS1710b_A2372 BURPS1710b_A2373(uxaA)
            BTE: BTH_II1606
            PNU: Pnuc_0724
            POL: Bpro_3576 Bpro_3967
            PNA: Pnap_2068
            VEI: Veis_0892 Veis_1537 Veis_3804
            HAR: HEAR3337
            CJE: Cj0483(uxaA')
            CJD: JJD26997_1451(uxaA)
            CFF: CFF8240_1064
            MLO: mlr3330
            SME: SMc02776
            SMD: Smed_3225
            RET: RHE_CH00495(ypch00183)
            RLE: RL0521
            BJA: blr2974
            CCR: CC_1488
            RSP: RSP_1610
            RSH: Rsph17029_0264
            RSQ: Rsph17025_0287
            PDE: Pden_4671
            MMR: Mmar10_0228
            NAR: Saro_2430
            SAL: Sala_3043
            SUS: Acid_1453
            BSU: BG13213(uxaA)
            BHA: BH0490
            BLI: BL00712(uxaA)
            BLD: BLi03512(uxaA)
            BCL: ABC0442 ABC1127 ABC1128 ABC1153(uxaA)
            GKA: GK1958 GK1959
            CAC: CAC0696
            CBE: Cbei_1839
            AMT: Amet_0556
            CHY: CHY_1256 CHY_1290
            DSY: DSY0965 DSY0966 DSY2104 DSY2105 DSY3251
            RHA: RHA1_ro06852
            KRA: Krad_0582
            SEN: SACE_1823
            RBA: RB10616
            BTH: BT_0486
            GFO: GFO_1706(uxaA)
            FJO: Fjoh_4258
            TAC: Ta1392 Ta1393
            PTO: PTO0043 PTO0044
            SSO: SSO1259(garD) SSO1260
            STO: ST2559 ST2560
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.7
            ExPASy - ENZYME nomenclature database: 4.2.1.7
            ExplorEnz - The Enzyme Database: 4.2.1.7
            ERGO genome analysis and discovery system: 4.2.1.7
            BRENDA, the Enzyme Database: 4.2.1.7
            CAS: 62213-26-7
///
ENTRY       EC 4.2.1.8                  Enzyme
NAME        mannonate dehydratase;
            mannonic hydrolase;
            mannonate hydrolyase;
            altronic hydro-lyase;
            altronate hydrolase;
            D-mannonate hydrolyase;
            D-mannonate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     D-mannonate hydro-lyase (2-dehydro-3-deoxy-D-gluconate-forming)
REACTION    D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O [RN:R05606]
ALL_REAC    R05606
SUBSTRATE   D-mannonate [CPD:C00514]
PRODUCT     2-dehydro-3-deoxy-D-gluconate [CPD:C00204];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:13584413]
  AUTHORS   ASHWELL A, WAHBA AJ, HICKMAN J.
  TITLE     A new pathway of uronic acid metabolism.
  JOURNAL   Biochim. Biophys. Acta. 30 (1958) 186-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4581499]
  AUTHORS   Robert-Baudouy JM, Stoeber FR.
  TITLE     [Purification and properties of D-mannonate hydrolyase from
            Escherichia coli K12]
  JOURNAL   Biochim. Biophys. Acta. 309 (1973) 473-85.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K01686  mannonate dehydratase
GENES       ECO: b4322(uxuA)
            ECJ: JW4285(uxuA)
            ECE: Z5920(uxuA)
            ECS: ECs5281
            ECC: c5402(uxuA)
            ECI: UTI89_C5018(uxuA)
            ECP: ECP_4658
            ECV: APECO1_2109(uxuA)
            ECW: EcE24377A_4920(uxuA)
            ECX: EcHS_A4548(uxuA)
            STY: STY3306(uxuA)
            STT: t3056(uxuA)
            SPT: SPA3003(uxuA)
            SEC: SC3076(uxuA)
            STM: STM3135
            YPE: YPO1283(uxuA)
            YPK: y2902(uxuA)
            YPM: YP_1308(uxuA)
            YPA: YPA_0999
            YPN: YPN_2695
            YPP: YPDSF_2413
            YPS: YPTB1315(uxuA)
            YPI: YpsIP31758_2699(uxuA)
            SFL: SF4198(uxuA)
            SFX: S4454(uxuA)
            SFV: SFV_4204(uxuA)
            SSN: SSON_4477(uxuA)
            SBO: SBO_4373(uxuA)
            ECA: ECA1093(uxuA)
            PLU: plu0170(uxuA)
            SGL: SG1838
            ENT: Ent638_2767
            SPE: Spro_3238
            HIT: NTHI0065(uxuA)
            HIP: CGSHiEE_03055
            HIQ: CGSHiGG_02780
            HSO: HS_1596(uxuA)
            MSU: MS0537(uxuA)
            ASU: Asuc_0151 Asuc_0370
            VVU: VV2_1064
            VVY: VVA1588
            VPA: VPA1700
            PPR: PBPRB1874(uxuA)
            PAT: Patl_3648
            SDE: Sde_1273 Sde_1891
            PIN: Ping_0136
            CSA: Csal_2980
            MMW: Mmwyl1_2778
            BUR: Bcep18194_B1358
            BCN: Bcen_3876
            BCH: Bcen2424_4493
            RFR: Rfer_0947
            AZO: azo0149(uxuA)
            MLO: mlr6866
            MES: Meso_4498 Meso_4519
            SME: SMb20446(uxuA)
            SMD: Smed_3684
            ATU: Atu3257(uxuA) Atu3529(uxuA)
            ATC: AGR_L_2605 AGR_L_3119
            RET: RHE_CH02058(uxuAch) RHE_PB00006(uxuAb)
            RLE: RL2336(uxuA) pRL90057(uxuA)
            BME: BMEII0474
            BMF: BAB2_0422(uxuA)
            BMS: BRA0814(uxuA)
            BMB: BruAb2_0418(uxuA)
            BOV: BOV_A0764(uxuA)
            OAN: Oant_4095
            BJA: bll6830(uxuA)
            BRA: BRADO1803(uxuA)
            BBT: BBta_2123(uxuA)
            SIL: SPO1723(uxuA)
            SIT: TM1040_3873
            RSP: RSP_0773
            RSH: Rsph17029_2429
            RSQ: Rsph17025_0406
            RDE: RD1_0665(uxuA)
            PDE: Pden_5061
            ACR: Acry_1858
            SUS: Acid_5062
            BSU: BG13208(uxuA)
            BHA: BH0706 BH1063
            BLI: BL00281(uxuAA) BL03802(uxuA)
            BLD: BLi01356(uxuA) BLi02116
            BCL: ABC0631(uxuA)
            BPU: BPUM_2984(uxaA)
            OIH: OB3411
            GTN: GTNG_1764(uxuA)
            SHA: SH2647(uxuA)
            LLA: L0020(uxuA)
            LLC: LACR_1745
            LLM: llmg_0859(uxuA)
            SPH: MGAS10270_Spy1170
            SAG: SAG0702(uxuA)
            SAN: gbs0675
            SAK: SAK_0828(uxuA)
            LBR: LVIS_0146
            EFA: EF3135
            CAC: CAC1332(uxuA)
            CPE: CPE0151(uxuA)
            CBE: Cbei_2200 Cbei_4084 Cbei_4659
            AMT: Amet_1292 Amet_3784
            CSC: Csac_2687
            MTA: Moth_0430
            PAC: PPA2327
            BTH: BT_0129 BT_1432
            BFR: BF0177
            BFS: BF0142(uxuA)
            FJO: Fjoh_1995 Fjoh_4191
            TMA: TM0069
            TPT: Tpet_0855
            TAC: Ta0753
            TVO: TVN0074
            PTO: PTO0148
STRUCTURES  PDB: 1TZ9  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.8
            ExPASy - ENZYME nomenclature database: 4.2.1.8
            ExplorEnz - The Enzyme Database: 4.2.1.8
            ERGO genome analysis and discovery system: 4.2.1.8
            BRENDA, the Enzyme Database: 4.2.1.8
            CAS: 9024-31-1
///
ENTRY       EC 4.2.1.9                  Enzyme
NAME        dihydroxy-acid dehydratase;
            acetohydroxyacid dehydratase;
            alpha,beta-dihydroxyacid dehydratase;
            2,3-dihydroxyisovalerate dehydratase;
            alpha,beta-dihydroxyisovalerate dehydratase;
            dihydroxy acid dehydrase;
            DHAD;
            2,3-dihydroxy-acid hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     2,3-dihydroxy-3-methylbutanoate hydro-lyase
            (3-methyl-2-oxobutanoate-forming)
REACTION    2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
            [RN:R01209]
ALL_REAC    R01209 > R04441;
            (other) R05070
SUBSTRATE   2,3-dihydroxy-3-methylbutanoate [CPD:C04039]
PRODUCT     3-methyl-2-oxobutanoate [CPD:C00141];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:14030545]
  AUTHORS   KANAMORI M, WIXOM RL.
  TITLE     Studies in valine biosynthesis. V. Characteristics of the purified
            dihydroxyacid dehydratase from spinach leaves.
  JOURNAL   J. Biol. Chem. 238 (1963) 998-1005.
  ORGANISM  spinach
REFERENCE   2  [PMID:13727223]
  AUTHORS   MYERS JW.
  TITLE     Dihydroxy acid dehydrase: an enzyme involved in the biosynthesis of
            isoleucine and valine.
  JOURNAL   J. Biol. Chem. 236 (1961) 1414-8.
  ORGANISM  Escherichia coli [GN:eco], Neurospora crassa [GN:dncr]
PATHWAY     PATH: map00290  Valine, leucine and isoleucine biosynthesis
            PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K01687  dihydroxy-acid dehydratase
GENES       ATH: AT3G23940
            OSA: 4346318
            CME: CMI142C
            SCE: YJR016C(ILV3)
            AGO: AGOS_ACL117W
            PIC: PICST_75802(ILV3)
            CGR: CAGL0B03993g
            SPO: SPAC17G8.06c
            ANI: AN5138.2 AN6346.2 AN7358.2
            AFM: AFUA_1G03550 AFUA_1G07330 AFUA_2G16300
            AOR: AO090009000414 AO090010000053 AO090012000890 AO090023000127
                 AO090102000231
            CNE: CNH01530
            UMA: UM05740.1
            ECO: b3771(ilvD)
            ECJ: JW5605(ilvD)
            ECE: Z5282(ilvD)
            ECS: ECs4705
            ECC: c4693(ilvD)
            ECI: UTI89_C4327(ilvD)
            ECP: ECP_3964
            ECW: EcE24377A_4282(ilvD)
            ECX: EcHS_A3988
            STY: STY3653(ilvD)
            STT: t3394(ilvD)
            SPT: SPA3743(ilvD)
            SEC: SC3809(ilvD)
            STM: STM3531 STM3904(ilvD)
            YPE: YPO3897(ilvD)
            YPK: y0338(ilvD)
            YPM: YP_3150(ilvD)
            YPA: YPA_0124
            YPN: YPN_0069
            YPP: YPDSF_3510
            YPS: YPTB0137(ilvD)
            YPI: YpsIP31758_0157(ilvD)
            SFL: SF3846(ilvD)
            SFX: S3913(ilvD)
            SFV: SFV_3731(ilvD)
            SSN: SSON_3942(ilvD)
            SBO: SBO_3782(ilvD)
            SDY: SDY_3977(ilvD)
            ECA: ECA4226(ilvD)
            PLU: plu4682(ilvD)
            BUC: BU600(ilvD)
            BAS: BUsg576(ilvD)
            BAB: bbp542(ilvD)
            BCC: BCc_389(ilvD)
            SGL: SG2394
            ENT: Ent638_0455 Ent638_4012
            SPE: Spro_0708 Spro_4757
            BFL: Bfl590(ilvD)
            BPN: BPEN_611(ilvD)
            HIT: NTHI0895(ilvD)
            HIP: CGSHiEE_08435
            HIQ: CGSHiGG_07165
            HSO: HS_0342(ilvD)
            PMU: PM1625(ilvD)
            MSU: MS2219(ilvD)
            APL: APL_0097(ilvD)
            ASU: Asuc_0415
            XFA: XF0099
            XFT: PD0074(ilvD)
            XCC: XCC0345(ilvD)
            XCB: XC_0356
            XCV: XCV0357(ilvD)
            XAC: XAC0345(ilvD)
            XOO: XOO4231(ilvD)
            XOM: XOO_3996(XOO3996)
            VCH: VC0028
            VCO: VC0395_A2491(ilvD)
            VVU: VV1_1029
            VVY: VV3243 VVA1581
            VPA: VP3061
            VFI: VF2559
            PPR: PBPRA3595
            PAE: PA0353(ilvD)
            PAU: PA14_04630(ilvD)
            PAP: PSPA7_0446(ilvD)
            PPU: PP_5128(ilvD)
            PPF: Pput_5002
            PST: PSPTO_3772 PSPTO_5057(ilvD)
            PSB: Psyr_0469 Psyr_1708
            PSP: PSPPH_0460(ilvD) PSPPH_3576
            PFL: PFL_5877(ilvD)
            PFO: Pfl_3227 Pfl_5358
            PEN: PSEEN0282(ilvD)
            PMY: Pmen_4205
            PAR: Psyc_1304(ilvD)
            PCR: Pcryo_1074
            PRW: PsycPRwf_1382
            ACI: ACIAD1266(ilvD) ACIAD3636
            SON: SO_4345(ilvD)
            SDN: Sden_3412
            SFR: Sfri_0424
            SAZ: Sama_3279
            SBL: Sbal_4029
            SBM: Shew185_4007
            SLO: Shew_0292
            SPC: Sputcn32_2062 Sputcn32_3612
            SSE: Ssed_4162
            SPL: Spea_0348
            SHE: Shewmr4_0364 Shewmr4_1983
            SHM: Shewmr7_1991 Shewmr7_3662
            SHN: Shewana3_0358 Shewana3_2070
            SHW: Sputw3181_1950 Sputw3181_3752
            CPS: CPS_2080 CPS_4846(ilvD)
            PHA: PSHAa2769(ilvD) PSHAb0129
            PAT: Patl_4250
            SDE: Sde_0358
            PIN: Ping_0346 Ping_2151
            MAQ: Maqu_2116 Maqu_2423
            MCA: MCA2082(ilvD)
            FTU: FTT0640(ilvD)
            FTF: FTF0640(ilvD)
            FTW: FTW_1090(ilvD)
            FTA: FTA_0961 FTA_0962
            FTN: FTN_1043(ilvD)
            TCX: Tcr_0599
            NOC: Noc_2001
            AEH: Mlg_0418 Mlg_1553
            HHA: Hhal_0179
            HCH: HCH_05854(ilvD)
            CSA: Csal_1142 Csal_1145 Csal_2664
            ABO: ABO_0180(ilvD-1) ABO_2312(ilvD2)
            MMW: Mmwyl1_0518 Mmwyl1_0861 Mmwyl1_3737 Mmwyl1_3803 Mmwyl1_4105
            AHA: AHA_4202(ilvD)
            CRP: CRP_029
            RMA: Rmag_0529
            VOK: COSY_0485(ilvD)
            NME: NMB1150 NMB1188
            NMA: NMA1361(ilvD)
            NMC: NMC1090(ilvD)
            NGO: NGO0809
            CVI: CV_1277(ilvD)
            RSO: RSc2412(ilvD)
            REU: Reut_A0639 Reut_A2432 Reut_B3950 Reut_C5894
            REH: H16_A2987 H16_B0280
            RME: Rmet_2804 Rmet_4585 Rmet_5271
            BMA: BMA0677(ilvD)
            BMV: BMASAVP1_A2334(ilvD)
            BML: BMA10299_A2952(ilvD)
            BMN: BMA10247_1647(ilvD)
            BXE: Bxe_A3634 Bxe_A4479 Bxe_B1524 Bxe_B2661 Bxe_C0901 Bxe_C1359
            BVI: Bcep1808_3832 Bcep1808_4698 Bcep1808_5602
            BUR: Bcep18194_A5793 Bcep18194_B0041 Bcep18194_B1899
            BCN: Bcen_1851 Bcen_4231 Bcen_5215 Bcen_6396 Bcen_6461
            BCH: Bcen2424_2462 Bcen2424_4135 Bcen2424_5644 Bcen2424_6629
                 Bcen2424_6696
            BAM: Bamb_2511 Bamb_3546 Bamb_4925
            BPS: BPSL0969(ilvD)
            BPM: BURPS1710b_1180(ilvD)
            BPL: BURPS1106A_1027(ilvD)
            BPD: BURPS668_1020(ilvD)
            BTE: BTH_I0827(ilvD) BTH_II1632
            PNU: Pnuc_0680 Pnuc_0884
            BPE: BP0289(ilvD) BP2779 BP3043(ilvD)
            BPA: BPP0429(ilvD) BPP1380(ilvD) BPP1383(ilvD) BPP2553
                 BPP3770(ilvD)
            BBR: BB0431(ilvD) BB1998 BB2446(ilvD) BB2452(ilvD) BB4216(ilvD)
            RFR: Rfer_0456 Rfer_1921
            POL: Bpro_2052 Bpro_2297 Bpro_3532 Bpro_3810 Bpro_5111
            PNA: Pnap_1698 Pnap_2666 Pnap_2877
            AAV: Aave_0754 Aave_1506 Aave_2248 Aave_3759
            AJS: Ajs_1071 Ajs_1072
            VEI: Veis_0037 Veis_0740 Veis_0940 Veis_3222 Veis_3404 Veis_3540
                 Veis_4523
            MPT: Mpe_A1387 Mpe_A3651
            HAR: HEAR0734(ilvD)
            MMS: mma_0652
            NEU: NE0104
            NET: Neut_2238
            NMU: Nmul_A0346
            EBA: ebA1822(ilvD) ebA478 ebA6761(ilvD)
            AZO: azo0632(ilvD)
            DAR: Daro_0302
            TBD: Tbd_2730
            MFA: Mfla_0340
            HHE: HH0850
            WSU: WS0130(ilvD)
            TDN: Tmden_0065
            CJE: Cj0013(ilvD)
            CJR: CJE0012(ilvD)
            CJJ: CJJ81176_0039(ilvD)
            CJU: C8J_0012(ilvD)
            CJD: JJD26997_0013(ilvD)
            CFF: CFF8240_1752(ilvD)
            CCV: CCV52592_2036(ilvD)
            CHA: CHAB381_1769(ilvD)
            CCO: CCC13826_0012(ilvD)
            ABU: Abu_2100(ilvD)
            NIS: NIS_0126(ilvD)
            SUN: SUN_2427(ilvD)
            GSU: GSU1912(ilvD)
            GME: Gmet_1259
            GUR: Gura_3721
            PCA: Pcar_1911
            PPD: Ppro_2559
            DVU: DVU3373(ilvD)
            DVL: Dvul_0024
            DDE: Dde_0116
            DPS: DP0894 DP0895
            ADE: Adeh_4111
            AFW: Anae109_4269
            SAT: SYN_01708
            SFU: Sfum_0356
            PUB: SAR11_0961(ilvD)
            MLO: mll1102 mll7192 mlr5361 mlr5404
            MES: Meso_0842 Meso_1688 Meso_2666 Meso_3757 Meso_4465
            PLA: Plav_3010
            SME: SMa0235 SMb20115(ilvD4) SMb20890(ilvD5) SMc00884(ilvD1)
                 SMc04045(ilvD2) SMc04144(ilvD3)
            SMD: Smed_0434 Smed_2488 Smed_2723 Smed_3320 Smed_4022 Smed_4478
            ATU: Atu1918(ilvD) Atu2736(ilvD) Atu3219(ilvD) Atu3971(ilvD)
            ATC: AGR_C_3510 AGR_C_4959 AGR_L_1769 AGR_L_3190
            RET: RHE_CH01704(ilvDch1) RHE_CH03160(ilvDch2)
                 RHE_CH03347(ypch01167) RHE_PC00044(ilvDc)
            RLE: RL1803(ilvD) RL3612(ilvD) RL3772(ilvD) RL4421(ilvD)
                 pRL120238(ilvD)
            BME: BMEI1848
            BMF: BAB1_0096(ilvD)
            BMS: BR0099(ilvD)
            BMB: BruAb1_0096(ilvD)
            BOV: BOV_0097(ilvD)
            OAN: Oant_0112 Oant_1421 Oant_3343 Oant_4589
            BJA: bll0378(ilvD) bll3915 bll4536(ilvD) bll4763(ilvD) bll6092
                 blr2826(ilvD)
            BRA: BRADO1812 BRADO2308(ilvD) BRADO2489 BRADO2754(ilvD)
                 BRADO3103(ilvD1) BRADO4080(ilvD) BRADO6988
            BBT: BBta_0539 BBta_2132 BBta_2674(ilvD) BBta_2834
                 BBta_3551(ilvD1) BBta_4456(ilvD) BBta_5433(ilvD)
            RPA: RPA1463(ilvD2) RPA2155(ilvD3) RPA2341(ilvD) RPA3472(ilvD1)
            RPB: RPB_2095 RPB_3247 RPB_4066
            RPC: RPC_2494 RPC_3191 RPC_3648 RPC_4321 RPC_4380
            RPD: RPD_2216 RPD_2806 RPD_3324 RPD_3804
            RPE: RPE_2261 RPE_3688 RPE_4363
            NWI: Nwi_0213
            NHA: Nham_0169
            BHE: BH00980(ilvD)
            XAU: Xaut_0070 Xaut_1022 Xaut_1998
            CCR: CC_0819 CC_3044
            SIL: SPO2410 SPO3314(ilvD) SPOA0332
            SIT: TM1040_2486 TM1040_3487
            RSP: RSP_0176 RSP_3074(ilvD)
            RSH: Rsph17029_1810 Rsph17029_3617 Rsph17029_3801
            RSQ: Rsph17025_1467
            JAN: Jann_0062 Jann_0987
            RDE: RD1_0332(ilvD) RD1_3693(ilvD)
            PDE: Pden_1984 Pden_2933 Pden_4246
            MMR: Mmar10_0291
            HNE: HNE_1411(ilvD)
            ZMO: ZMO1792(ilvD)
            NAR: Saro_1784
            SAL: Sala_1189
            SWI: Swit_1660 Swit_3037 Swit_3271 Swit_4656
            ELI: ELI_06910
            GOX: GOX2491
            GBE: GbCGDNIH1_1938
            ACR: Acry_0087 Acry_1046 Acry_2210 Acry_2470
            RRU: Rru_A1786
            MAG: amb2536
            MGM: Mmc1_1838
            ABA: Acid345_3109
            SUS: Acid_0606 Acid_5357 Acid_5866
            BSU: BG11532(ilvD)
            BHA: BH3062(ilvD)
            BAN: BA1853(ilvD)
            BAR: GBAA1853(ilvD)
            BAA: BA_2356
            BAT: BAS1717
            BCE: BC1780
            BCA: BCE_1937(ilvD)
            BCZ: BCZK1669(ilvD)
            BCY: Bcer98_1446
            BTK: BT9727_1694(ilvD)
            BLI: BL05225(ilvD)
            BLD: BLi02324(ilvD)
            BCL: ABC1110 ABC2646(ilvD)
            BAY: RBAM_020010
            BPU: BPUM_1922
            OIH: OB2624(ilvD)
            GKA: GK2046(ilvD)
            SAU: SA1858(ilvD)
            SAV: SAV2053(ilvD)
            SAM: MW1977(ilvD)
            SAR: SAR2140(ilvD)
            SAS: SAS1958
            SAC: SACOL2042(ilvD)
            SAB: SAB1938
            SAA: SAUSA300_2006(ilvD)
            SAO: SAOUHSC_02281
            SAJ: SaurJH9_2090
            SAH: SaurJH1_2127
            SEP: SE1654
            SER: SERP1665(ilvD)
            SHA: SH0980(ilvD)
            SSP: SSP0825 SSP2293
            LMO: lmo1983(ilvD)
            LMF: LMOf2365_2006(ilvD)
            LIN: lin2090(ilvD)
            LWE: lwe2002(ilvD)
            LLA: L0077(ilvD)
            LLC: LACR_1312
            LLM: llmg_1280(ilvD)
            SPN: SP_2126
            SPR: spr1935(ilvD)
            SPD: SPD_1956(ilvD)
            SMU: SMU.2128
            STC: str1604(ilvD1) str1874
            STL: stu1604(ilvD1) stu1874
            SSA: SSA_2286(ilvD)
            SGO: SGO_2064(ilvD)
            STH: STH2685
            CAC: CAC3170(ilvD) CAC3604(ilvD)
            CNO: NT01CX_1480 NT01CX_2027(ilvD)
            CTH: Cthe_2713
            CDF: CD2014(ilvD)
            CBA: CLB_0335(ilvD)
            CBH: CLC_0350(ilvD)
            CBF: CLI_0364(ilvD)
            CBE: Cbei_1510 Cbei_4095 Cbei_4127
            CKL: CKL_1693(ilvD)
            AMT: Amet_0502 Amet_1268 Amet_3401 Amet_3534
            CHY: CHY_0516(ilvD)
            DSY: DSY1365 DSY3452
            DRM: Dred_0280
            SWO: Swol_2147
            CSC: Csac_0836
            TTE: TTE0020(ilvD)
            MTA: Moth_2259
            MTU: Rv0189c(ilvD)
            MTC: MT0199(ilvD)
            MBO: Mb0195c(ilvD)
            MBB: BCG_0226c(ilvD)
            MLE: ML2608(ilvD)
            MPA: MAP3631c(ilvD)
            MAV: MAV_4989(ilvD)
            MSM: MSMEG_0229(ilvD) MSMEG_0482 MSMEG_1290(ilvD)
            MVA: Mvan_0173 Mvan_1161
            MGI: Mflv_0486 Mflv_5171
            MMC: Mmcs_0146
            MKM: Mkms_0155
            MJL: Mjls_0136
            CGL: NCgl1219(cgl1268)
            CGB: cg1432(ilvD)
            CEF: CE1362 CE2439
            CDI: DIP1096(ilvD)
            CJK: jk1303(ilvD)
            NFA: nfa11740 nfa23830(ilvD2) nfa42340(ilvD)
            RHA: RHA1_ro05087(ilvD1) RHA1_ro06484(ilvD2)
            SCO: SCO1176(SCG11A.07c) SCO1888(SCI7.06c) SCO3345(SCE7.12c)
            SMA: SAV4716(ilvD1) SAV6367(ilvD2)
            TWH: TWT204(ilvD)
            TWS: TW568(ilvD)
            LXX: Lxx13210(ilvD)
            CMI: CMM_1093(ilvD)
            ART: Arth_2540
            AAU: AAur_0356(ilvD) AAur_2510(ilvD)
            NCA: Noca_3419
            TFU: Tfu_2209
            FRA: Francci3_4515
            FAL: FRAAL6844(ilvD)
            ACE: Acel_0433 Acel_0705
            KRA: Krad_1334 Krad_1909
            SEN: SACE_1280(ilvD) SACE_5858(ilvD5) SACE_6161(ilvD)
            STP: Strop_1017 Strop_1231
            BLO: BL1788(ilvD)
            BAD: BAD_0539(ilvD)
            RXY: Rxyl_1326
            RBA: RB11919(ilvD) RB12087(ilvD) RB1480(ilvD)
            LIL: LA2959(ilvD)
            LIC: LIC11101(ilvD)
            LBJ: LBJ_2063(ilvD)
            LBL: LBL_0987(ilvD)
            SYN: slr0452(ilvD)
            SYW: SYNW1123(ilvD)
            SYC: syc0898_c(ilvD)
            SYF: Synpcc7942_0626
            SYD: Syncc9605_1260
            SYE: Syncc9902_1222
            SYG: sync_1692(ilvD)
            SYR: SynRCC307_1248(ilvD)
            SYX: SynWH7803_1131(ilvD)
            CYA: CYA_1697(ilvD)
            CYB: CYB_1987(ilvD)
            TEL: tll1057(ilvD)
            GVI: gll3168(ilvD)
            ANA: alr2771
            AVA: Ava_0023 Ava_B0062
            PMA: Pro0847(ilvD)
            PMM: PMM0774(ilvD)
            PMT: PMT0560
            PMN: PMN2A_0180
            PMI: PMT9312_0782
            PMB: A9601_08361(ilvD)
            PMC: P9515_08091(ilvD)
            PMF: P9303_16921(ilvD)
            PMG: P9301_08341(ilvD)
            PMH: P9215_08681
            PME: NATL1_08121(ilvD)
            TER: Tery_0019
            BTH: BT_2078
            BFR: BF3763
            BFS: BF3551(ilvD)
            SRU: SRU_2153(ilvD)
            CHU: CHU_3745(ilvD)
            GFO: GFO_2113(ilvD)
            FJO: Fjoh_2863 Fjoh_3218
            FPS: FP0449(ilvD)
            CTE: CT0619(ilvD)
            CCH: Cag_1906
            CPH: Cpha266_0854
            PVI: Cvib_1169
            PLT: Plut_0609
            DET: DET0834(ilvD)
            DEH: cbdb_A815(ilvD)
            DEB: DehaBAV1_0753
            RRS: RoseRS_3155
            RCA: Rcas_2979
            DRA: DR_1132
            DGE: Dgeo_1240
            TTH: TTC0871
            TTJ: TTHA1234
            AAE: aq_837(ilvD)
            TMA: TM0551
            TPT: Tpet_0369
            MMP: MMP0318(ilvD)
            MMQ: MmarC5_1356
            MMZ: MmarC7_1320
            MAE: Maeo_0680
            MVN: Mevan_1329
            MAC: MA1802(ilvD) MA3373(ilvD)
            MBA: Mbar_A2069
            MMA: MM_0259
            MBU: Mbur_2246
            MTP: Mthe_0673
            MHU: Mhun_0139
            MEM: Memar_0985
            MBN: Mboo_1203
            MST: Msp_1576(ilvD)
            MSI: Msm_1237
            MKA: MK1197(ilvD)
            HMA: rrnAC0302(ilvD)
            HWA: HQ3021A(ilvD)
            NPH: NP4926A(ilvD)
            PTO: PTO1437
            PAB: PAB0895(ilvD)
            PFU: PF0942
            RCI: RCIX1841(ilvD-2) RCIX238(ilvD-1)
            APE: APE_0013.1
            IHO: Igni_0961
            SSO: SSO3107(ilvD)
            STO: ST2172
            SAI: Saci_1715
            MSE: Msed_0711
            PAI: PAE0615(ilvD)
            PIS: Pisl_0740
            PCL: Pcal_0900
            PAS: Pars_2269
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.9
            ExPASy - ENZYME nomenclature database: 4.2.1.9
            ExplorEnz - The Enzyme Database: 4.2.1.9
            ERGO genome analysis and discovery system: 4.2.1.9
            BRENDA, the Enzyme Database: 4.2.1.9
            CAS: 9024-32-2
///
ENTRY       EC 4.2.1.10                 Enzyme
NAME        3-dehydroquinate dehydratase;
            3-dehydroquinate hydrolase;
            DHQase;
            dehydroquinate dehydratase;
            3-dehydroquinase;
            5-dehydroquinase;
            dehydroquinase;
            5-dehydroquinate dehydratase;
            5-dehydroquinate hydro-lyase;
            3-dehydroquinate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     3-dehydroquinate hydro-lyase (3-dehydroshikimate-forming)
REACTION    3-dehydroquinate = 3-dehydroshikimate + H2O [RN:R03084]
ALL_REAC    R03084
SUBSTRATE   3-dehydroquinate [CPD:C00944]
PRODUCT     3-dehydroshikimate [CPD:C02637];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:13198937]
  AUTHORS   MITSUHASHI S, DAVIS BD.
  TITLE     Aromatic biosynthesis. XII. Conversion of 5-dehydroquinic acid to
            5-dehydroshikimic acid dy 5-dehydroquinase.
  JOURNAL   Biochim. Biophys. Acta. 15 (1954) 54-61.
  ORGANISM  Aerobacter aerogenes, Escherichia coli [GN:eco], Saccharomyces
            cerevisiae [GN:sce], Euglena gracilis, spinach, Pisum sativum
REFERENCE   2  [PMID:13208693]
  AUTHORS   MITSUHASHI S, DAVIS BD.
  TITLE     Aromatic biosynthesis. XIII. Conversion of quinic acid to
            5-dehydroquinic acid by quinic dehydrogenase.
  JOURNAL   Biochim. Biophys. Acta. 15 (1954) 268-80.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K01688  3-dehydroquinate dehydratase
            KO: K03785  3-dehydroquinate dehydratase I
            KO: K03786  3-dehydroquinate dehydratase II
GENES       OSA: 4325444
            CME: CMK269C
            SCE: YDR127W(ARO1)
            AGO: AGOS_AGR066W
            PIC: PICST_62322(DQD1)
            CAL: CaO19.2283 CaO19_4704(CaO19.4704)
            CGR: CAGL0M11484g
            SPO: SPAC1834.02(aro1)
            ANI: AN1135.2
            AFM: AFUA_1G11610 AFUA_1G13740 AFUA_3G14850 AFUA_4G06460
            AOR: AO090012000502 AO090038000261
            CNE: CNB01990
            UMA: UM00053.1 UM03607.1
            ECO: b1693(aroD)
            ECJ: JW1683(aroD)
            ECE: Z2721(aroD)
            ECS: ECs2400
            ECC: c2088(aroD)
            ECI: UTI89_C1885(aroD)
            ECP: ECP_1640
            ECV: APECO1_769(aroD)
            ECW: EcE24377A_1909(aroD)
            ECX: EcHS_A1774
            STY: STY1760(aroD)
            STT: t1231(aroD)
            SPT: SPA1493(aroD)
            SEC: SC1377(aroD)
            STM: STM1358(aroD)
            YPE: YPO3660(aroQ)
            YPK: y0207
            YPM: YP_3886(aroQ)
            YPA: YPA_3673
            YPN: YPN_3511
            YPP: YPDSF_0267
            YPS: YPTB3570(aroQ)
            YPI: YpsIP31758_0393(aroQ)
            SFL: SF1723(aroD)
            SFX: S1855(aroD)
            SFV: SFV_1719(aroD)
            SSN: SSON_1461(aroD)
            SBO: SBO_1438(aroD)
            SDY: SDY_1474(aroD)
            ECA: ECA0262(aroQ)
            PLU: plu4073(aroQ)
            BUC: BU399(aroD)
            BAS: BUsg386(aroD)
            BAB: bbp362(aroQ)
            BCC: BCc_251(aroQ)
            SGL: SG0154
            ENT: Ent638_3692
            SPE: Spro_2094 Spro_4416
            BFL: Bfl293(aroQ)
            BPN: BPEN_301(aroQ)
            HIN: HI0970(aroQ)
            HIT: NTHI1143(aroQ)
            HIP: CGSHiEE_07110
            HIQ: CGSHiGG_08430
            HDU: HD0632(aroQ)
            HSO: HS_0570(aroQ)
            PMU: PM1093(aroD)
            MSU: MS1790(aroQ)
            APL: APL_1862(aroQ)
            ASU: Asuc_0641
            XFA: XF0047
            XFT: PD0034(aroQ)
            XCC: XCC0518(aroQ) XCC4082(aroD)
            XCB: XC_0530 XC_4173
            XCV: XCV0566(aroQ) XCV4302
            XAC: XAC0533(aroQ) XAC4201(aroD)
            XOO: XOO0328(aroD) XOO0559(aroQ)
            XOM: XOO_0299(XOO0299) XOO_0523(XOO0523)
            VCH: VC0297
            VCO: VC0395_A2690(aroQ)
            VVU: VV1_1236
            VVY: VV3134
            VPA: VP2879
            VFI: VF2385
            PPR: PBPRA3404
            PAE: PA0245(aroQ2) PA4846(aroQ1)
            PAU: PA14_03030(aroQ2) PA14_64090(aroQ1)
            PAP: PSPA7_0330(aroQ2) PSPA7_5566(aroQ1)
            PPU: PP_0560(aroQ-1) PP_2407(aroQ-2) PP_3003(aroQ-3)
            PPF: Pput_0599 Pput_2690 Pput_3288
            PST: PSPTO_4859(aroQ)
            PSB: Psyr_4399
            PSP: PSPPH_4442(aroQ)
            PFL: PFL_0673 PFL_5381(aroQ)
            PFO: Pfl_0620 Pfl_4902
            PEN: PSEEN2021(aroQ-2) PSEEN4855(aroQ-1)
            PMY: Pmen_0715
            PAR: Psyc_0941(aroQ)
            PCR: Pcryo_1476
            PRW: PsycPRwf_0768
            ACI: ACIAD1713(quiB) ACIAD1738(aroQ)
            SON: SO_0512(aroQ)
            SDN: Sden_3285
            SFR: Sfri_3593
            SAZ: Sama_3194
            SBL: Sbal_0470
            SBM: Shew185_3854
            SLO: Shew_3363
            SPC: Sputcn32_3348
            SSE: Ssed_4088
            SPL: Spea_0534
            SHE: Shewmr4_0511
            SHM: Shewmr7_3520
            SHN: Shewana3_0511
            SHW: Sputw3181_0593
            ILO: IL2284
            CPS: CPS_0948(aroQ)
            PHA: PSHAa0264(aroQ)
            PAT: Patl_0088
            SDE: Sde_0813
            PIN: Ping_3121
            MAQ: Maqu_3443
            CBU: CBU_2075(aroD)
            CBD: COXBU7E912_2171(aroD)
            LPN: lpg0464(aroQ)
            LPF: lpl0506(aroQ)
            LPP: lpp0530(aroQ)
            MCA: MCA1044(aroQ)
            FTU: FTT0471(aroD)
            FTF: FTF0471(aroD)
            FTW: FTW_1599(aroQ)
            FTL: FTL_1593
            FTH: FTH_1539(aroD)
            FTA: FTA_1679(aroQ)
            FTN: FTN_0562(aroD)
            TCX: Tcr_0445
            NOC: Noc_1053
            AEH: Mlg_0024
            HHA: Hhal_2337
            CSA: Csal_0294 Csal_2283
            ABO: ABO_2008(aroQ)
            MMW: Mmwyl1_3916
            AHA: AHA_3345(aroQ)
            DNO: DNO_0419(aroQ)
            BCI: BCI_0050(aroQ)
            CRP: CRP_012
            RMA: Rmag_1058
            VOK: COSY_0957(aroQ)
            NME: NMB1446
            NMA: NMA1659(aroD)
            NMC: NMC1383(aroD)
            NGO: NGO0740(aroD)
            CVI: CV_0987(aroQ)
            RSO: RSc2785(aroQ1) RSp1397(aroQ2)
            REU: Reut_A2864 Reut_B5032
            REH: H16_A3170(aroQ1) H16_B0465(aroQ2)
            RME: Rmet_3063
            BMA: BMA2500(aroQ-1) BMAA0849(aroQ-2)
            BMV: BMASAVP1_1753(aroQ-2) BMASAVP1_A0421(aroQ-1)
            BML: BMA10299_2207(aroQ-2) BMA10299_A1280(aroQ-1)
            BMN: BMA10247_3284(aroQ-1) BMA10247_A0892(aroQ-2)
            BXE: Bxe_A0533 Bxe_B0883
            BVI: Bcep1808_0581 Bcep1808_3552
            BUR: Bcep18194_A3689 Bcep18194_B0344
            BCN: Bcen_0123 Bcen_3063
            BCH: Bcen2424_0606 Bcen2424_5304
            BAM: Bamb_0508 Bamb_4665
            BPS: BPSL2982(aroQ1) BPSS0340(aroQ2)
            BPM: BURPS1710b_3499(aroQ1) BURPS1710b_A1896(aroQ2)
            BPL: BURPS1106A_3502(aroQ) BURPS1106A_A0482(aroQ)
            BPD: BURPS668_3464 BURPS668_A0579
            BTE: BTH_I1164 BTH_II2058
            PNU: Pnuc_0211
            BPE: BP2998(aroQ)
            BPA: BPP3918(aroQ)
            BBR: BB4391(aroQ)
            RFR: Rfer_2381
            POL: Bpro_4497
            PNA: Pnap_1559 Pnap_3996
            AAV: Aave_2302
            AJS: Ajs_1610
            VEI: Veis_2299
            MPT: Mpe_A3205
            HAR: HEAR2761(aroQ)
            MMS: mma_2970
            NEU: NE0651(aroQ1)
            NET: Neut_1901
            NMU: Nmul_A2754
            EBA: ebA1471(aroQ) ebA234(aroC)
            AZO: azo0865(aroQ)
            DAR: Daro_3940
            TBD: Tbd_0183
            MFA: Mfla_0026
            HPY: HP1038(aroQ)
            HPJ: jhp0386(aroD)
            HPA: HPAG1_0409
            HHE: HH0945
            HAC: Hac_1142(aroQ)
            WSU: WS1645(aroQ)
            TDN: Tmden_0687
            CJE: Cj0066c(aroQ)
            CJR: CJE0063(aroQ)
            CJJ: CJJ81176_0104(aroQ)
            CJU: C8J_0059(aroQ)
            CJD: JJD26997_0076(aroQ)
            CFF: CFF8240_1505(aroQ)
            CCV: CCV52592_0364(aroQ)
            CHA: CHAB381_1211(aroQ)
            CCO: CCC13826_0370(aroQ) CCC13826_0805
            ABU: Abu_0488(aroQ)
            NIS: NIS_0430(aroQ)
            SUN: SUN_1038
            GSU: GSU2022(aroQ)
            GME: Gmet_0981
            GUR: Gura_1823
            PCA: Pcar_2178 Pcar_2188(aroD)
            PPD: Ppro_2360
            DVU: DVU1665(aroQ)
            DVL: Dvul_1422
            DDE: Dde_1952
            DPS: DP3013
            ADE: Adeh_0189
            AFW: Anae109_0209
            SAT: SYN_01938
            SFU: Sfum_2722
            PUB: SAR11_0728(aroQ)
            MLO: mll0207
            MES: Meso_1714
            PLA: Plav_3290
            SME: SMc01343(aroQ)
            SMD: Smed_0954 Smed_5704
            ATU: Atu1332(aroQ) Atu4531(aroQ)
            ATC: AGR_C_2456 AGR_L_675
            RET: RHE_CH01871(aroQ1) RHE_CH02289(aroQ2)
            RLE: RL2090 pRL110076
            BME: BMEI1061
            BMF: BAB1_0926(aroQ)
            BMS: BR0908(aroQ)
            BMB: BruAb1_0919(aroQ)
            BOV: BOV_0904(aroQ)
            OAN: Oant_2272
            BJA: bll4292(aroQ) bll6386(aroQ) blr1201
            BRA: BRADO1385(aroQ2)
            BBT: BBta_4214(aroQ)
            RPA: RPA2437(aroQ2)
            RPB: RPB_3018
            RPC: RPC_2867
            RPD: RPD_2433
            RPE: RPE_2986
            NWI: Nwi_1751
            NHA: Nham_2187
            BHE: BH01210(aroQ)
            BQU: BQ01140(aroQ)
            BBK: BARBAKC583_1276(aroQ)
            XAU: Xaut_2570 Xaut_3500
            CCR: CC_1882
            SIL: SPO1973(aroQ)
            SIT: TM1040_0337
            RSP: RSP_3376(aroQ)
            RSH: Rsph17029_3022
            JAN: Jann_2300
            RDE: RD1_2651(aroQ)
            PDE: Pden_0045
            MMR: Mmar10_1267
            HNE: HNE_2248(aroQ)
            ZMO: ZMO0737(aroD)
            NAR: Saro_2077
            SAL: Sala_1437
            SWI: Swit_4700
            ELI: ELI_03110
            GOX: GOX0437
            GBE: GbCGDNIH1_1959
            ACR: Acry_2377
            RRU: Rru_A2433
            MAG: amb2706
            MGM: Mmc1_0668
            SUS: Acid_7159
            BSU: BG10538(aroC) BG11707(yqhS)
            BHA: BH2801
            BAN: BA4423(aroQ)
            BAR: GBAA4423(aroQ)
            BAA: BA_4876
            BAT: BAS4103
            BCE: BC4199
            BCA: BCE_4272(aroQ)
            BCZ: BCZK3952(aroQ)
            BCY: Bcer98_2893
            BTK: BT9727_3941(aroQ)
            BTL: BALH_3805(aroQ)
            BLI: BL00001(aroC) BL01544(yqhS)
            BLD: BLi00939(aroC) BLi02618(yqhS)
            BCL: ABC0536(aroC)
            BAY: RBAM_008080 RBAM_020790(trpA)
            BPU: BPUM_2179
            OIH: OB0430 OB3242(aroD)
            GKA: GK2057
            SAU: SA0756
            SAV: SAV0829
            SAM: MW0782
            SAR: SAR0860
            SAS: SAS0769
            SAC: SACOL0873(aroD)
            SAB: SAB0760
            SAA: SAUSA300_0787(aroD)
            SAO: SAOUHSC_00832
            SAJ: SaurJH9_0828
            SAH: SaurJH1_0845
            SEP: SE0592
            SER: SERP0481(aroD)
            SHA: SH2055
            SSP: SSP1873
            LMO: lmo0491
            LMF: LMOf2365_0521(aroD)
            LIN: lin0494
            LWE: lwe0462(aroD)
            LLA: L0062(aroD)
            LLC: LACR_1805
            LLM: llmg_0782(aroD)
            SPY: SPy_0809(aroD)
            SPZ: M5005_Spy_0624(aroD)
            SPM: spyM18_0871(aroD)
            SPG: SpyM3_0543(aroD)
            SPS: SPs1311
            SPH: MGAS10270_Spy0679(aroD)
            SPI: MGAS10750_Spy0711(aroD)
            SPJ: MGAS2096_Spy0689(aroD)
            SPK: MGAS9429_Spy0679(aroD)
            SPF: SpyM51183(aroD)
            SPA: M6_Spy0641
            SPB: M28_Spy0603(aroD)
            SPN: SP_1377
            SPR: spr1235(aroD)
            SPD: SPD_1211(aroD)
            SAG: SAG1379(aroD)
            SAN: gbs1449(aroD)
            SAK: SAK_1412(aroD)
            SMU: SMU.777(aroD)
            STC: str0638(aroD)
            STL: stu0638(aroD)
            STE: STER_0688
            SSA: SSA_1470(aroD)
            SGO: SGO_1375(aroD)
            LPL: lp_2798(aroC1) lp_3493(aroC2)
            LSA: LSA0889(aroD)
            LSL: LSL_1796(aroD)
            EFA: EF1731(aroD)
            LME: LEUM_1160
            STH: STH1866
            CAC: CAC0899
            CPE: CPE0702(aroQ)
            CPF: CPF_0695(aroQ)
            CPR: CPR_0695(aroQ)
            CTC: CTC01593
            CNO: NT01CX_1316(aroD)
            CTH: Cthe_0849
            CDF: CD2217(aroD)
            CBO: CBO1898(aroQ)
            CBA: CLB_1835(aroQ)
            CBH: CLC_1842(aroQ)
            CBF: CLI_1962(aroQ)
            CBE: Cbei_4570
            CKL: CKL_1007(aroD)
            AMT: Amet_1074
            CHY: CHY_1874(aroQ)
            DSY: DSY2378
            DRM: Dred_1050
            SWO: Swol_0544
            CSC: Csac_2238
            TTE: TTE1279(aroQ)
            MTA: Moth_1540
            MTU: Rv2537c(aroD)
            MTC: MT2612(aroQ)
            MBO: Mb2566c(aroD)
            MBB: BCG_2559c(aroD)
            MLE: ML0519(aroD)
            MPA: MAP1094(aroD)
            MAV: MAV_3413(aroQ)
            MSM: MSMEG_1922(aroQ) MSMEG_2532(aroQ)
            MVA: Mvan_1784
            MGI: Mflv_4683
            MMC: Mmcs_2355
            MKM: Mkms_2402
            MJL: Mjls_2396
            CGL: NCgl0408(cgl0423)
            CGB: cg0503(aroD)
            CEF: CE0442(aroQ) CE1739(aroQ)
            CDI: DIP1342(aroQ)
            CJK: jk1030(aroD)
            NFA: nfa54990
            RHA: RHA1_ro01368 RHA1_ro03051
            SCO: SCO1961(aroQ)
            SMA: SAV6280(aroD)
            TWH: TWT369(aroD)
            TWS: TW400(aroQ)
            LXX: Lxx10990(aroD)
            CMI: CMM_1794(aroQ)
            ART: Arth_3392
            AAU: AAur_3363(aroQ)
            PAC: PPA1686
            NCA: Noca_2415
            TFU: Tfu_1635
            FRA: Francci3_0428
            FAL: FRAAL0912(aroD)
            ACE: Acel_1306
            KRA: Krad_1000
            SEN: SACE_2068(aroQ-2) SACE_2865(aroD)
            STP: Strop_1848
            BLO: BL0876(aroQ)
            BAD: BAD_0706(aroQ)
            RXY: Rxyl_1588
            FNU: FN0046
            RBA: RB6488
            CTR: CT370(aroE)
            CTA: CTA_0402(aroE)
            CMU: TC0649
            CPN: CPn1035(aroE)
            CPA: CP0817
            CPJ: CPj1035(aroE)
            CPT: CpB1075
            CCA: CCA00727(aroE)
            CAB: CAB694(aroE)
            CFE: CF0289(aroE)
            LIL: LA0045(aroD)
            LIC: LIC10039(aroD)
            LBJ: LBJ_0033(aroD)
            LBL: LBL_2987(aroD)
            SYN: sll1112(aroQ)
            SYW: SYNW1938(aroD)
            SYC: syc0627_d(aroQ)
            SYF: Synpcc7942_0915
            SYD: Syncc9605_0502
            SYE: Syncc9902_1833
            SYG: sync_0578(aroQ)
            SYR: SynRCC307_0456(aroQ)
            SYX: SynWH7803_0549(aroQ)
            CYA: CYA_0718(aroQ)
            CYB: CYB_2912(aroQ)
            TEL: tlr0494(aroQ)
            GVI: glr2442(aroQ)
            ANA: alr2782
            AVA: Ava_0032
            PMA: Pro0384(aroQ)
            PMM: PMM0387(aroD)
            PMT: PMT0195(aroD)
            PMN: PMN2A_1721
            PMI: PMT9312_0383
            PMB: A9601_04381(aroQ)
            PMC: P9515_04491(aroQ)
            PMF: P9303_21621(aroQ)
            PMG: P9301_04071(aroQ)
            PME: NATL1_04381(aroQ)
            TER: Tery_2664
            BTH: BT_2842
            BFR: BF4483
            BFS: BF4278(aroQ)
            PGI: PG1731(aroQ)
            SRU: SRU_0492(aroQ)
            CHU: CHU_2703(aroQ)
            GFO: GFO_1867(aroQ)
            FJO: Fjoh_0128
            FPS: FP2018(aroQ)
            CTE: CT1190(aroQ)
            CCH: Cag_0784
            CPH: Cpha266_1544
            PVI: Cvib_0958
            PLT: Plut_0932
            DET: DET0466(aroD)
            DEH: cbdb_A430(aroD)
            DEB: DehaBAV1_0443
            RRS: RoseRS_3243
            RCA: Rcas_3731
            DRA: DR_0778
            DGE: Dgeo_1733
            TTH: TTC0989
            TTJ: TTHA1354
            AAE: aq_021(aroD)
            TMA: TM0349
            TPT: Tpet_0571
            MJA: MJ1454(aroD)
            MMP: MMP1394(aroD)
            MMQ: MmarC5_0184
            MMZ: MmarC7_0639
            MAE: Maeo_0132
            MVN: Mevan_0705
            MAC: MA4593(aroD)
            MBA: Mbar_A0922
            MMA: MM_1273
            MBU: Mbur_1999
            MTP: Mthe_0540
            MTH: MTH566
            MST: Msp_0577(aroD)
            MSI: Msm_0231
            MKA: MK0429(aroD)
            AFU: AF0228(aroD)
            HAL: VNG0314G(aroD)
            HMA: rrnAC1877(aroD)
            HWA: HQ1154A(aroD)
            NPH: NP2240A(aroD)
            TAC: Ta0116
            TVO: TVN0194
            PTO: PTO0596
            PAB: PAB0299(aroD)
            PFU: PF1692
            TKO: TK0266
            RCI: RCIX1512(aroD)
            APE: APE_0577
            SSO: SSO0311(aroD)
            STO: ST2278
            SAI: Saci_0189(aroD)
            PAI: PAE1960
            PIS: Pisl_1789
            PCL: Pcal_0911
            PAS: Pars_2038
STRUCTURES  PDB: 1D0I  1GQN  1GQO  1GTZ  1GU0  1GU1  1H05  1H0R  1H0S  1J2Y  
                 1L9W  1QFE  1SFJ  1SFL  1UQR  1V1J  2BT4  2C4V  2C4W  2C57  
                 2CJF  2DHQ  2EGZ  2GPT  2OCZ  2YR1  2YSW  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.10
            ExPASy - ENZYME nomenclature database: 4.2.1.10
            ExplorEnz - The Enzyme Database: 4.2.1.10
            ERGO genome analysis and discovery system: 4.2.1.10
            BRENDA, the Enzyme Database: 4.2.1.10
            CAS: 9012-66-2
///
ENTRY       EC 4.2.1.11                 Enzyme
NAME        phosphopyruvate hydratase;
            enolase;
            2-phosphoglycerate dehydratase;
            14-3-2-protein;
            nervous-system specific enolase;
            phosphoenolpyruvate hydratase;
            2-phosphoglycerate dehydratase;
            2-phosphoglyceric dehydratase;
            2-phosphoglycerate enolase;
            gamma-enolase;
            2-phospho-D-glycerate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     2-phospho-D-glycerate hydro-lyase (phosphoenolpyruvate-forming)
REACTION    2-phospho-D-glycerate = phosphoenolpyruvate + H2O [RN:R00658]
ALL_REAC    R00658;
            (other) R04206
SUBSTRATE   2-phospho-D-glycerate [CPD:C00631]
PRODUCT     phosphoenolpyruvate [CPD:C00074];
            H2O [CPD:C00001]
INHIBITOR   Phosphonoacetohydroxamate [CPD:C05347]
COMMENT     Also acts on 3-phospho-D-erythronate.
REFERENCE   1  [PMID:13908561]
  AUTHORS   HOLT A, WOLD F.
  TITLE     The isolation and characterization of rabbit muscle enolase.
  JOURNAL   J. Biol. Chem. 236 (1961) 3227-31.
  ORGANISM  rabbit
REFERENCE   2
  AUTHORS   Malmstrom, B.G.
  TITLE     Enolase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 5, Academic Press, New York, 1961, p. 471-494.
REFERENCE   3  [PMID:14235523]
  AUTHORS   WESTHEAD EW, MCLAIN G.
  TITLE     A PURIFICATION OF BREWERS' AND BAKERS' YEAST ENOLASE YIELDING A
            SINGLE ACTIVE COMPONENT.
  JOURNAL   J. Biol. Chem. 239 (1964) 2464-8.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
ORTHOLOGY   KO: K01689  enolase
GENES       HSA: 2023(ENO1) 2026(ENO2) 2027(ENO3)
            PTR: 454457(ENO3)
            MCC: 709378(ENO1)
            MMU: 13806(Eno1) 13807(Eno2) 13808(Eno3) 433182(EG433182)
            RNO: 24333(Eno1) 24334(Eno2) 25438(Eno3)
            CFA: 476315(LOC476315) 477709(ENO2) 479469(ENO3)
            BTA: 281141(ENO1)
            GGA: 395689(ENO2) 396016(LOC396016) 396017(RCJMB04_24e12)
            XLA: 379079(MGC53543) 380038(eno3) 380298(eno1)
            XTR: 394749(eno1)
            DRE: 334116(eno1) 378963(eno3) 393668(zgc:73056)
            SPU: 583138(LOC583138)
            DME: Dmel_CG17654(Eno)
            CEL: T21B10.2(enolase)
            ATH: AT1G74030 AT2G36530(LOS2)
            OSA: 4332253 4340042 4346906 4348176
            CME: CMK131C
            SCE: YGR254W(ENO1) YHR174W(ENO2) YMR323W(ERR3) YOR393W(ERR1)
            AGO: AGOS_AER294C
            PIC: PICST_70720(ENO1)
            CGR: CAGL0F08261g CAGL0I02486g
            SPO: SPBC1815.01(eno1)
            ANI: AN5746.2
            AFM: AFUA_6G06770
            AOR: AO090003000055
            CNE: CNC00160 CNE00040
            UMA: UM03356.1
            ECU: ECU10_1690
            DDI: DDB_0231355(enoA) DDB_0231356(enoB)
            PFA: PF10_0155
            CPV: cgd5_1960
            CHO: Chro.50184
            TAN: TA10425
            TPV: TP04_0700
            TET: TTHERM_00046480
            TBR: Tb10.70.4740 Tb11.01.8100
            TCR: 504105.140
            LMA: LmjF14.1160
            EHI: 337.t00001
            ECO: b2779(eno)
            ECJ: JW2750(eno)
            ECE: Z4094(eno)
            ECS: ECs3639
            ECC: c3344(eno)
            ECI: UTI89_C3148(eno)
            ECP: ECP_2760
            ECV: APECO1_3751(eno)
            ECW: EcE24377A_3083(eno)
            ECX: EcHS_A2923(eno)
            STY: STY3081(eno)
            STT: t2853(eno)
            SPT: SPA2809(eno)
            SEC: SC2886(eno)
            STM: STM2952(eno)
            YPE: YPO3376(eno)
            YPK: y0814(eno)
            YPM: YP_0310(eno)
            YPA: YPA_2874
            YPN: YPN_0716
            YPP: YPDSF_2983
            YPS: YPTB0755(eno)
            YPI: YpsIP31758_3316(eno)
            YEN: YE0747(eno)
            SFL: SF2794(eno)
            SFX: S2988(eno)
            SFV: SFV_2676(eno)
            SSN: SSON_2936(eno)
            SBO: SBO_2660(eno)
            SDY: SDY_2996(eno)
            ECA: ECA3566(eno)
            PLU: plu0913(eno)
            BUC: BU417(eno)
            BAS: BUsg400(eno)
            BAB: bbp377(eno)
            BCC: BCc_264(eno)
            WBR: WGLp353(eno)
            SGL: SG0513
            ENT: Ent638_3233
            SPE: Spro_0795
            BFL: Bfl157(eno)
            BPN: BPEN_162(eno)
            HIN: HI0932(eno)
            HIT: NTHI1103(eno)
            HIP: CGSHiEE_07335(eno)
            HDU: HD0477(eno)
            HSO: HS_0561(eno)
            PMU: PM1871(eno)
            MSU: MS0256(eno)
            APL: APL_1113(eno)
            ASU: Asuc_2051
            XFA: XF1291
            XFT: PD0543(eno)
            XCC: XCC1700(eno)
            XCB: XC_2531
            XCV: XCV1752(eno)
            XAC: XAC1719(eno)
            XOO: XOO2963(eno)
            XOM: XOO_2814(XOO2814)
            VCH: VC2447
            VCO: VC0395_A2025(eno)
            VVU: VV1_1579
            VVY: VV2818
            VPA: VP2561
            VFI: VF2075(eno)
            PPR: PBPRA3079(eno)
            PAE: PA3635(eno)
            PAU: PA14_17320(eno)
            PAP: PSPA7_1504(eno)
            PPU: PP_1612(eno)
            PPF: Pput_1850 Pput_4165
            PST: PSPTO_1554(eno-1) PSPTO_4616(eno-2)
            PSB: Psyr_1363(eno) Psyr_1482
            PSP: PSPPH_3820(eno)
            PFL: PFL_1196(eno)
            PFO: Pfl_1121(eno)
            PEN: PSEEN4200(eno)
            PMY: Pmen_3033
            PAR: Psyc_1636(eno)
            PCR: Pcryo_1870
            PRW: PsycPRwf_1664
            ACI: ACIAD2001(eno)
            SON: SO_3440(eno)
            SDN: Sden_1196
            SFR: Sfri_1052
            SAZ: Sama_1036
            SBL: Sbal_3127
            SBM: Shew185_3136
            SLO: Shew_1205
            SPC: Sputcn32_2757
            SSE: Ssed_1290
            SPL: Spea_1185
            SHE: Shewmr4_1115
            SHM: Shewmr7_1186
            SHN: Shewana3_1116
            SHW: Sputw3181_1255
            ILO: IL0772
            CPS: CPS_4106(eno)
            PHA: PSHAa0742(eno)
            PAT: Patl_3266
            SDE: Sde_1245
            PIN: Ping_0669
            MAQ: Maqu_0921
            CBU: CBU_1674(eno)
            CBD: COXBU7E912_0327(eno)
            LPN: lpg2037(eno)
            LPF: lpl2015(eno)
            LPP: lpp2020(eno)
            MCA: MCA1933(eno-1) MCA2515(eno-2)
            FTU: FTT0709(eno)
            FTF: FTF0709(eno)
            FTW: FTW_1532(eno)
            FTL: FTL_1527
            FTH: FTH_1477(eno)
            FTA: FTA_1611(eno)
            FTN: FTN_0621(eno)
            TCX: Tcr_1260
            NOC: Noc_0852
            AEH: Mlg_1839
            HHA: Hhal_1437
            HCH: HCH_01867(eno)
            CSA: Csal_0619
            ABO: ABO_1164(eno)
            MMW: Mmwyl1_1299
            AHA: AHA_0821(eno)
            DNO: DNO_0362(eno)
            BCI: BCI_0221(eno)
            RMA: Rmag_0351
            VOK: COSY_0332(eno)
            NME: NMB1285
            NMA: NMA1495(eno)
            NMC: NMC1220(eno)
            NGO: NGO0617
            CVI: CV_3459(eno)
            RSO: RSc1129(eno)
            REU: Reut_A1091(eno)
            REH: H16_A1188(eno)
            RME: Rmet_1055 Rmet_1176
            BMA: BMA1689
            BMV: BMASAVP1_A2193(eno)
            BML: BMA10299_A3125(eno)
            BMN: BMA10247_1466(eno)
            BXE: Bxe_A1573
            BVI: Bcep1808_2186
            BUR: Bcep18194_A5413(eno)
            BCN: Bcen_5970
            BCH: Bcen2424_2107
            BAM: Bamb_2144
            BPS: BPSL2270(eno)
            BPM: BURPS1710b_2711(eno)
            BPL: BURPS1106A_2631(eno)
            BPD: BURPS668_2577(eno)
            BTE: BTH_I1894(eno)
            PNU: Pnuc_0947
            BPE: BP2386(eno)
            BPA: BPP3252(eno)
            BBR: BB3703(eno)
            RFR: Rfer_2650
            POL: Bpro_3184
            PNA: Pnap_1183
            AAV: Aave_1322
            AJS: Ajs_0997
            VEI: Veis_2650 Veis_2870
            MPT: Mpe_A2847
            HAR: HEAR2188(eno)
            MMS: mma_1270(eno)
            NEU: NE1044(eno)
            NET: Neut_2482
            NMU: Nmul_A1228
            EBA: ebA6162(eno)
            AZO: azo2144(eno)
            DAR: Daro_2364
            TBD: Tbd_0621(eno)
            MFA: Mfla_1909
            HPY: HP0154(eno)
            HPJ: jhp0142(eno)
            HPA: HPAG1_0152
            HHE: HH0631(eno)
            HAC: Hac_0337(eno)
            WSU: WS1494(eno)
            TDN: Tmden_2001
            CJE: Cj1672c(eno)
            CJR: CJE1844(eno)
            CJJ: CJJ81176_1668(eno)
            CJU: C8J_1573(eno)
            CJD: JJD26997_2046(eno)
            CFF: CFF8240_0200(eno)
            CCV: CCV52592_0615(eno)
            CHA: CHAB381_1786(eno)
            CCO: CCC13826_1910 CCC13826_2093(eno)
            ABU: Abu_2240(eno)
            NIS: NIS_1657(eno)
            SUN: SUN_0083 SUN_1213
            GSU: GSU2286(eno)
            GME: Gmet_2372
            GUR: Gura_1780
            PCA: Pcar_1230
            PPD: Ppro_1654
            DVU: DVU0322(eno)
            DVL: Dvul_2659
            DDE: Dde_0295
            LIP: LI0091(eno)
            BBA: Bd0796(eno)
            DPS: DP1799
            ADE: Adeh_1642
            AFW: Anae109_2168
            MXA: MXAN_4451(eno)
            SAT: SYN_01733
            SFU: Sfum_0078
            WOL: WD0494(eno)
            WBM: Wbm0119
            AMA: AM600(eno)
            APH: APH_0695(eno)
            ERU: Erum4840(eno)
            ERW: ERWE_CDS_05060(eno)
            ERG: ERGA_CDS_04960(eno)
            ECN: Ecaj_0489
            ECH: ECH_0544(eno)
            NSE: NSE_0733(eno)
            PUB: SAR11_0939(eno)
            MLO: mlr0378
            MES: Meso_1632
            PLA: Plav_3143
            SME: SMc01028(eno)
            SMD: Smed_1072
            ATU: Atu1426(eno)
            ATC: AGR_C_2631
            RET: RHE_CH01931(eno)
            RLE: RL2239(eno)
            BME: BMEI0851
            BMF: BAB1_1155(eno)
            BMS: BR1132(eno)
            BMB: BruAb1_1138(eno)
            BOV: BOV_1092(eno)
            OAN: Oant_2056 Oant_4592
            BJA: bll4794(eno)
            BRA: BRADO4094(eno)
            BBT: BBta_4471(eno)
            RPA: RPA2874(eno)
            RPB: RPB_2778
            RPC: RPC_2483
            RPD: RPD_2816
            RPE: RPE_2607
            NWI: Nwi_1827
            NHA: Nham_1743
            BHE: BH05720(eno)
            BQU: BQ04880(eno)
            BBK: BARBAKC583_0532(eno)
            XAU: Xaut_4289
            CCR: CC_1724
            SIL: SPO2474(eno)
            SIT: TM1040_0931
            RSP: RSP_2491(eno)
            RSH: Rsph17029_1159
            RSQ: Rsph17025_0930
            JAN: Jann_1797
            RDE: RD1_3142(eno)
            PDE: Pden_4060
            MMR: Mmar10_1413
            HNE: HNE_1980(eno)
            ZMO: ZMO1608(eno)
            NAR: Saro_2223
            SAL: Sala_0523
            SWI: Swit_0446
            ELI: ELI_05740
            GOX: GOX2279
            GBE: GbCGDNIH1_1181
            ACR: Acry_0167
            RRU: Rru_A1885
            MAG: amb1823
            MGM: Mmc1_1562
            ABA: Acid345_1070
            SUS: Acid_4373
            BSU: BG10899(eno)
            BHA: BH3556(eno)
            BAN: BA5364(eno)
            BAR: GBAA5364(eno)
            BAA: BA_0223
            BAT: BAS4985
            BCE: BC5135
            BCA: BCE_5238(eno)
            BCZ: BCZK4824(eno)
            BCY: Bcer98_3678
            BTK: BT9727_4814(eno)
            BTL: BALH_4627(eno)
            BLI: BL03468(eno)
            BLD: BLi03661(eno)
            BCL: ABC3017(eno)
            BAY: RBAM_031260(eno)
            BPU: BPUM_3053(eno)
            OIH: OB2434(eno)
            GKA: GK3054(eno)
            SAU: SA0731(eno)
            SAV: SAV0776(eno)
            SAM: MW0738(eno)
            SAR: SAR0832(eno)
            SAS: SAS0742
            SAC: SACOL0842(eno)
            SAB: SAB0732(eno)
            SAA: SAUSA300_0760(eno)
            SAO: SAOUHSC_00799
            SAJ: SaurJH9_0801
            SAH: SaurJH1_0817
            SEP: SE0561
            SER: SERP0446(eno)
            SHA: SH2109(eno)
            SSP: SSP1912
            LMO: lmo2455(eno)
            LMF: LMOf2365_2428(eno)
            LIN: lin2549(eno)
            LWE: lwe2403(eno)
            LLA: L0007(enoA) L0008(enoB)
            LLC: LACR_0283 LACR_0668
            LLM: llmg_0617(enoA)
            SPY: SPy_0731(eno)
            SPZ: M5005_Spy_0556(eno)
            SPM: spyM18_0798(eno)
            SPG: SpyM3_0479(eno)
            SPS: SPs1375
            SPH: MGAS10270_Spy0615(eno)
            SPI: MGAS10750_Spy0639(eno)
            SPJ: MGAS2096_Spy0618(eno)
            SPK: MGAS9429_Spy0609(eno)
            SPF: SpyM51248(eno)
            SPA: M6_Spy0576 M6_Spy0577
            SPB: M28_Spy0535(eno)
            SPN: SP_1128
            SPR: spr1036(eno)
            SPD: SPD_1012(eno)
            SAG: SAG0628(eno)
            SAN: gbs0608(eno)
            SAK: SAK_0713(eno)
            SMU: SMU.1247(eno)
            STC: str0635(eno)
            STL: stu0635(eno)
            SSA: SSA_0886(eno)
            SGO: SGO_1426(eno)
            LPL: lp_0792(enoA1) lp_1920(eno)
            LJO: LJ0875 LJ1246 LJ1416
            LAC: LBA0889(eno)
            LSA: LSA0607(eno)
            LSL: LSL_1163(eno)
            LDB: Ldb1294(eno)
            LBU: LBUL_1209
            LBR: LVIS_0664
            LCA: LSEI_0970
            EFA: EF1961(eno)
            OOE: OEOE_1650
            STH: STH249
            CAC: CAC0713(eno)
            CPE: CPE1299(eno)
            CPF: CPF_1505(eno)
            CPR: CPR_1295(eno)
            CTC: CTC00382(eno)
            CNO: NT01CX_1414
            CTH: Cthe_0143
            CDF: CD3170(eno)
            CBO: CBO0230(eno)
            CBA: CLB_0271(eno)
            CBH: CLC_0286(eno)
            CBF: CLI_0295(eno)
            CBE: Cbei_0602
            AMT: Amet_3576
            CHY: CHY_0284(eno)
            DSY: DSY4838
            DRM: Dred_0136 Dred_2987
            SWO: Swol_0276
            CSC: Csac_1950
            TTE: TTE1759(eno)
            MTA: Moth_0266
            MGE: MG_407(eno)
            MPN: MPN606(eno)
            MPU: MYPU_5180(eno)
            MPE: MYPE3750(eno)
            MGA: MGA_0209(eno)
            MMY: MSC_0253(eno)
            MMO: MMOB1800(eno)
            MHY: mhp129(eno)
            MHJ: MHJ_0242(eno)
            MHP: MHP7448_0250(eno)
            MSY: MS53_0009(eno)
            MCP: MCAP_0213(eno)
            UUR: UU184(eno)
            POY: PAM284(eno)
            AYW: AYWB_437(eno)
            MFL: Mfl468
            MTU: Rv1023(eno)
            MTC: MT1051(eno)
            MBO: Mb1051(eno)
            MBB: BCG_1080(eno)
            MLE: ML0255(eno)
            MPA: MAP0990(eno)
            MAV: MAV_1164(eno) MAV_3957
            MSM: MSMEG_5415(eno)
            MVA: Mvan_4771
            MGI: Mflv_1954
            MMC: Mmcs_4240
            MKM: Mkms_4326
            MJL: Mjls_4619
            CGL: NCgl0935(eno)
            CGB: cg1111(eno)
            CEF: CE1042
            CDI: DIP0917(eno)
            CJK: jk1483(eno)
            NFA: nfa48590(eno)
            RHA: RHA1_ro05777(eno)
            SCO: SCO3096(eno) SCO7638(eno2)
            SMA: SAV3533(eno)
            TWH: TWT783(eno)
            TWS: TW793(eno)
            LXX: Lxx17200(eno)
            CMI: CMM_2263(enoA)
            ART: Arth_1147
            AAU: AAur_1263(eno)
            PAC: PPA0545(eno)
            NCA: Noca_0928
            TFU: Tfu_0428(eno)
            FRA: Francci3_3923
            FAL: FRAAL6233(eno)
            ACE: Acel_1909
            KRA: Krad_1073
            SEN: SACE_0838(eno)
            STP: Strop_0890
            BLO: BL1022(eno)
            BAD: BAD_0645(eno)
            RXY: Rxyl_0912
            FNU: FN1764
            RBA: RB12381(eno)
            CTR: CT587(eno)
            CTA: CTA_0637(eno)
            CMU: TC0876
            CPN: CPn0800(eno)
            CPA: CP1071
            CPJ: CPj0800(eno)
            CPT: CpB0829
            CCA: CCA00963(eno)
            CAB: CAB932(eno)
            CFE: CF0051(eno)
            PCU: pc0143(eno)
            BGA: BG0338(eno)
            BAF: BAPKO_0346(eno)
            TPA: TP0817
            TDE: TDE0949(eno)
            LIL: LA1951(eno)
            LIC: LIC11954(eno)
            LBJ: LBJ_1561(eno)
            LBL: LBL_1785(eno)
            SYN: slr0752(eno)
            SYW: SYNW2348(eno)
            SYC: syc0886_c(eno)
            SYF: Synpcc7942_0639
            SYD: Syncc9605_2476
            SYE: Syncc9902_2161
            SYG: sync_2732(eno)
            SYR: SynRCC307_2363(eno)
            SYX: SynWH7803_2379(eno)
            CYA: CYA_2554(eno)
            CYB: CYB_2531(eno)
            TEL: tlr0658
            GVI: gll2121
            ANA: all3538
            AVA: Ava_3517(eno)
            PMA: Pro0235(eno)
            PMM: PMM0208(eno)
            PMT: PMT2083(eno)
            PMN: PMN2A_1575
            PMI: PMT9312_0210
            PMB: A9601_02261(eno)
            PMC: P9515_02371(eno)
            PMF: P9303_27721(eno)
            PMG: P9301_02281(eno)
            PMH: P9215_02271(eno)
            PME: NATL1_02841(eno)
            TER: Tery_2793
            BTH: BT_4572
            BFR: BF1188
            BFS: BF1155(eno)
            PGI: PG1824(eno)
            SRU: SRU_0787(eno)
            CHU: CHU_3133(eno)
            GFO: GFO_2809(eno)
            FJO: Fjoh_0368
            FPS: FP1309(eno)
            CTE: CT0145(eno-2) CT1962(eno-1)
            CCH: Cag_0347
            CPH: Cpha266_0223
            PVI: Cvib_1615
            PLT: Plut_1972
            DET: DET0593(eno)
            DEH: cbdb_A573(eno)
            DEB: DehaBAV1_0568
            RRS: RoseRS_4532
            RCA: Rcas_0074
            DRA: DR_2637
            DGE: Dgeo_0004
            TTH: TTC1610
            TTJ: TTHA0002
            AAE: aq_484(eno)
            TMA: TM0877
            TPT: Tpet_0050
            TME: Tmel_0174
            FNO: Fnod_1726
            MJA: MJ0232(eno)
            MMP: MMP0396(eno)
            MMQ: MmarC5_1242
            MMZ: MmarC7_1394
            MAE: Maeo_0609
            MVN: Mevan_1383
            MAC: MA1672(eno)
            MBA: Mbar_A2850
            MMA: MM_2836
            MBU: Mbur_1687
            MTP: Mthe_0833
            MHU: Mhun_1018 Mhun_1101 Mhun_2893
            MEM: Memar_0763 Memar_1809
            MBN: Mboo_2216
            MST: Msp_0862(eno)
            MSI: Msm_1435
            MKA: MK1647(eno)
            HAL: VNG1142G(eno)
            HMA: rrnAC0069(eno)
            HWA: HQ2935A(eno)
            NPH: NP2846A(eno)
            TAC: Ta0882
            TVO: TVN0981
            PTO: PTO1234(eno)
            PHO: PH1942
            PAB: PAB1126(eno)
            PFU: PF0215
            TKO: TK2106
            RCI: LRC402(eno)
            APE: APE_2458
            SMR: Smar_1274
            IHO: Igni_1007
            HBU: Hbut_0911
            SSO: SSO0913
            STO: ST1212
            SAI: Saci_1377(eno)
            MSE: Msed_1668
            PAI: PAE0812
            PIS: Pisl_1098
            PCL: Pcal_0022
            PAS: Pars_0056
            TPE: Tpen_0112
STRUCTURES  PDB: 1E9I  1EBG  1EBH  1ELS  1IYX  1L8P  1NEL  1OEP  1ONE  1P43  
                 1P48  1PDY  1PDZ  1TE6  1W6T  2AKM  2AKZ  2AL1  2AL2  2FYM  
                 2ONE  2PA6  3ENL  4ENL  5ENL  6ENL  7ENL  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.11
            ExPASy - ENZYME nomenclature database: 4.2.1.11
            ExplorEnz - The Enzyme Database: 4.2.1.11
            ERGO genome analysis and discovery system: 4.2.1.11
            BRENDA, the Enzyme Database: 4.2.1.11
            CAS: 9014-08-8
///
ENTRY       EC 4.2.1.12                 Enzyme
NAME        phosphogluconate dehydratase;
            6-phosphogluconate dehydratase;
            6-phosphogluconic dehydrase;
            gluconate-6-phosphate dehydratase;
            gluconate 6-phosphate dehydratase;
            6-phosphogluconate dehydrase;
            6-phospho-D-gluconate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     6-phospho-D-gluconate hydro-lyase
            (2-dehydro-3-deoxy-6-phospho-D-gluconate-forming)
REACTION    6-phospho-D-gluconate = 2-dehydro-3-deoxy-6-phospho-D-gluconate +
            H2O [RN:R02036]
ALL_REAC    R02036
SUBSTRATE   6-phospho-D-gluconate [CPD:C00345]
PRODUCT     2-dehydro-3-deoxy-6-phospho-D-gluconate [CPD:C04442];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:14245409]
  AUTHORS   MELOCHE HP, WOOD WA.
  TITLE     THE MECHANISM OF 6-PHOSPHOGLUCONIC DEHYDRASE.
  JOURNAL   J. Biol. Chem. 239 (1964) 3505-10.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00030  Pentose phosphate pathway
ORTHOLOGY   KO: K01690  phosphogluconate dehydratase
GENES       ECO: b1851(edd)
            ECJ: JW1840(edd)
            ECE: Z2903(edd)
            ECS: ECs2561
            ECC: c2264(edd)
            ECI: UTI89_C2054(edd)
            ECP: ECP_1795
            ECV: APECO1_901(edd)
            ECW: EcE24377A_2081(edd)
            ECX: EcHS_A1943(edd)
            STY: STY2093(edd)
            STT: t0992(edd)
            SPT: SPA0984(edd)
            SEC: SC1890(edd)
            STM: STM1885(edd)
            YPE: YPO2533(edd)
            YPK: y1654(edd)
            YPM: YP_2344(edd)
            YPA: YPA_2025
            YPN: YPN_2128
            YPP: YPDSF_1943
            YPS: YPTB2565(edd)
            YPI: YpsIP31758_1476(edd)
            SFL: SF1861(edd)
            SFX: S1927(edd)
            SFV: SFV_1853(edd)
            SSN: SSON_1297(edd)
            SBO: SBO_1159(edd)
            SDY: SDY_1137(edd)
            ECA: ECA1836(edd)
            ENT: Ent638_2420
            SPE: Spro_3330 Spro_4499
            XFA: XF1062
            XFT: PD0343(edd)
            XCC: XCC2139(edd)
            XCB: XC_1974
            XCV: XCV2234(edd)
            XAC: XAC2068(edd)
            XOO: XOO2317(edd)
            XOM: XOO_2194(XOO2194)
            VCH: VC0288
            VCO: VC0395_A2666(edd)
            VVU: VV1_1099
            VVY: VV0059
            VPA: VP0062
            PAE: PA3194(edd)
            PAU: PA14_22910(edd)
            PAP: PSPA7_1934(edd)
            PPU: PP_1010(edd)
            PPF: Pput_1048
            PST: PSPTO_1288(edd)
            PSB: Psyr_1109
            PSP: PSPPH_1177(edd)
            PFL: PFL_4622(edd)
            PFO: Pfl_4375
            PEN: PSEEN4417(edd)
            PMY: Pmen_1312
            ACI: ACIAD0542(edd)
            SON: SO_2487(edd)
            SDN: Sden_2077
            SFR: Sfri_1894
            SAZ: Sama_1810
            SBL: Sbal_2239
            SBM: Shew185_2132
            SLO: Shew_2046
            SPC: Sputcn32_1868
            SSE: Ssed_2072
            SPL: Spea_2333
            SHE: Shewmr4_2044
            SHM: Shewmr7_1931
            SHN: Shewana3_2149
            SHW: Sputw3181_2140
            CPS: CPS_2283(edd)
            PHA: PSHAa1366(edd)
            PAT: Patl_0972
            SDE: Sde_1381
            MAQ: Maqu_1830
            LPN: lpg0418(edd)
            LPF: lpl0461(edd)
            LPP: lpp0485(edd)
            MCA: MCA0037(edd)
            HCH: HCH_00433(edd)
            CSA: Csal_0936
            MMW: Mmwyl1_1080
            AHA: AHA_0288(edd)
            NME: NMB1393
            NMA: NMA1610(edd)
            NMC: NMC1332(edd)
            NGO: NGO0714
            CVI: CV_0144(edd)
            RSO: RSp1560(edd)
            REU: Reut_A1081 Reut_B5330
            REH: H16_A1178(edd1) H16_B2567(edd2)
            RME: Rmet_1045 Rmet_5802
            BMA: BMA2446(edd)
            BMV: BMASAVP1_A0363(edd)
            BML: BMA10299_A1221(edd)
            BMN: BMA10247_2632(edd)
            BXE: Bxe_A0589
            BVI: Bcep1808_0628
            BUR: Bcep18194_A3746
            BCN: Bcen_0177
            BCH: Bcen2424_0660
            BAM: Bamb_0555
            BPS: BPSL2932(edd)
            BPM: BURPS1710b_3442(edd)
            BPL: BURPS1106A_3442(edd)
            BPD: BURPS668_3407(edd)
            BTE: BTH_I1217(edd)
            RFR: Rfer_2060
            POL: Bpro_3551
            PNA: Pnap_2986
            AAV: Aave_2793
            AJS: Ajs_2049
            VEI: Veis_2570
            HAR: HEAR1086(edd)
            MMS: mma_2311(edd)
            MFA: Mfla_0759
            HPY: HP1100
            HPJ: jhp1026(edd)
            HPA: HPAG1_1038
            HAC: Hac_0442(edd)
            CJD: JJD26997_1271(edd)
            PUB: SAR11_0774(edd)
            MLO: mll6512
            MES: Meso_0157
            SME: SMc03068(edd)
            SMD: Smed_0298
            ATU: Atu0598(edd)
            ATC: AGR_C_1060
            RET: RHE_CH00702(edd)
            RLE: RL0751(edd)
            BME: BMEII0511
            BMF: BAB2_0458
            BMB: BruAb2_0452
            BOV: BOV_A0730(edd)
            OAN: Oant_3958
            BHE: BH03930(edd)
            XAU: Xaut_1018 Xaut_1698
            CCR: CC_2055
            SIL: SPO3032(edd)
            SIT: TM1040_0376
            RSH: Rsph17029_1303
            RSQ: Rsph17025_1181
            JAN: Jann_1953
            RDE: RD1_2879(edd)
            PDE: Pden_1955
            MMR: Mmar10_2640
            HNE: HNE_1740(edd)
            ZMO: ZMO0368(edd)
            NAR: Saro_1895
            SAL: Sala_0191
            SWI: Swit_1624 Swit_1727
            ELI: ELI_00540
            GOX: GOX0431
            GBE: GbCGDNIH1_2043
            ACR: Acry_0466
            MSM: MSMEG_0313(edd)
            RHA: RHA1_ro02368(edd)
            SEN: SACE_1740(edd)
            HMA: rrnAC0302(ilvD)
STRUCTURES  PDB: 2GP4  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.12
            ExPASy - ENZYME nomenclature database: 4.2.1.12
            ExplorEnz - The Enzyme Database: 4.2.1.12
            ERGO genome analysis and discovery system: 4.2.1.12
            BRENDA, the Enzyme Database: 4.2.1.12
            CAS: 9024-33-3
///
ENTRY       EC 4.2.1.13       Obsolete  Enzyme
NAME        Transferred to 4.3.1.17
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
COMMENT     Transferred entry: now EC 4.3.1.17 L-serine ammonia-lyase (EC
            4.2.1.13 created 1961, deleted 2001)
GENES       CHY: CHY_0700(sdhB1)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.13
            ExPASy - ENZYME nomenclature database: 4.2.1.13
            ExplorEnz - The Enzyme Database: 4.2.1.13
            ERGO genome analysis and discovery system: 4.2.1.13
            BRENDA, the Enzyme Database: 4.2.1.13
///
ENTRY       EC 4.2.1.14       Obsolete  Enzyme
NAME        Transferred to 4.3.1.18
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
COMMENT     Transferred entry: now EC 4.3.1.18 D-serine ammonia-lyase (EC
            4.2.1.14 created 1961, deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.14
            ExPASy - ENZYME nomenclature database: 4.2.1.14
            ExplorEnz - The Enzyme Database: 4.2.1.14
            ERGO genome analysis and discovery system: 4.2.1.14
            BRENDA, the Enzyme Database: 4.2.1.14
///
ENTRY       EC 4.2.1.15       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
COMMENT     Deleted entry: homoserine dehydratase. Identical with EC 4.4.1.1
            cystathionine gamma-lyase (EC 4.2.1.15 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.15
            ExPASy - ENZYME nomenclature database: 4.2.1.15
            ExplorEnz - The Enzyme Database: 4.2.1.15
            ERGO genome analysis and discovery system: 4.2.1.15
            BRENDA, the Enzyme Database: 4.2.1.15
///
ENTRY       EC 4.2.1.16       Obsolete  Enzyme
NAME        Transferred to 4.3.1.19
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
COMMENT     Transferred entry: now EC 4.3.1.19 threonine ammonia-lyase (EC
            4.2.1.16 created 1961, deleted 2001)
STRUCTURES  PDB: 1TDJ  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.16
            ExPASy - ENZYME nomenclature database: 4.2.1.16
            ExplorEnz - The Enzyme Database: 4.2.1.16
            ERGO genome analysis and discovery system: 4.2.1.16
            BRENDA, the Enzyme Database: 4.2.1.16
///
ENTRY       EC 4.2.1.17                 Enzyme
NAME        enoyl-CoA hydratase;
            enoyl hydrase;
            unsaturated acyl-CoA hydratase;
            beta-hydroxyacyl-CoA dehydrase;
            beta-hydroxyacid dehydrase;
            hydratase, enoyl coenzyme A;
            acyl coenzyme A hydrase;
            crotonase;
            crotonyl hydrase;
            2-octenoyl coenzyme A hydrase;
            enoyl coenzyme A hydratase;
            2-enoyl-CoA hydratase;
            short-chain enoyl-CoA hydratase;
            ECH;
            trans-2-enoyl-CoA hydratase;
            short-chain enoyl-CoA hydratase;
            enoyl coenzyme A hydrase (D);
            enoyl coenzyme A hydrase (L);
            short chain enoyl coenzyme A hydratase;
            D-3-hydroxyacyl-CoA dehydratase;
            enol-CoA hydratase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (3S)-3-hydroxyacyl-CoA hydro-lyase
REACTION    (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O [RN:R02685
            R07314]
ALL_REAC    R02685 > R03026 R03045 R04170 R04204 R04224 R04738 R04740 R04744
            R04746 R04749 R07889 R07893 R07897;
            R07314;
            (other) R03224 R04137 R05595 R06411 R06412 R06942
SUBSTRATE   (3S)-3-hydroxyacyl-CoA [CPD:C00640]
PRODUCT     trans-2-enoyl-CoA [CPD:C00658];
            trans-3-enoyl-CoA [CPD:C05067];
            H2O [CPD:C00001]
COMMENT     Acts in the reverse direction. With cis-compounds, yields
            (3R)-3-hydroxyacyl-CoA. cf. EC 4.2.1.74 long-chain-enoyl-CoA
            hydratase.
REFERENCE   1  [PMID:5808333]
  AUTHORS   Moskowitz GJ, Merrick JM.
  TITLE     Metabolism of poly-beta-hydroxybutyrate. II. Enzymatic synthesis of
            D-(-)-beta hydroxybutyryl coenzyme A by an enoyl hydrase from
            Rhodospirillum rubrum.
  JOURNAL   Biochemistry. 8 (1969) 2748-55.
  ORGANISM  Rhodospirillum rubrum [GN:rru]
REFERENCE   2
  AUTHORS   Stern, J.R.
  TITLE     Thioltranscrotylase and beta-hydroxybutyryl CoA racemase activities
            of crystalline crotonase.
  JOURNAL   Biochim. Biophys. Acta 26 (1957) 641-643.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00062  Fatty acid elongation in mitochondria
            PATH: map00071  Fatty acid metabolism
            PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00310  Lysine degradation
            PATH: map00380  Tryptophan metabolism
            PATH: map00410  beta-Alanine metabolism
            PATH: map00592  alpha-Linolenic acid metabolism
            PATH: map00632  Benzoate degradation via CoA ligation
            PATH: map00640  Propanoate metabolism
            PATH: map00650  Butanoate metabolism
            PATH: map00903  Limonene and pinene degradation
            PATH: map00930  Caprolactam degradation
            PATH: map01040  Polyunsaturated fatty acid biosynthesis
            PATH: map03320  PPAR signaling pathway
ORTHOLOGY   KO: K01692  enoyl-CoA hydratase
            KO: K07511  enoyl-CoA hydratase
            KO: K07514  enoyl-CoA hydratase
            KO: K07515  enoyl-CoA hydratase
            KO: K10527  enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase
GENES       HSA: 1892(ECHS1) 1962(EHHADH) 3030(HADHA)
            PTR: 460996(EHHADH)
            MMU: 74147(Ehhadh) 93747(Echs1) 97212(Hadha)
            RNO: 140547(Echs1) 170670(Hadha) 171142(Ehhadh)
            CFA: 475687(HADHA) 488110(EHHADH)
            BTA: 281748(ECHS1) 281810(HADHA)
            SSC: 397012(HADHA)
            GGA: 395929(HADHA) 424877(EHHADH)
            XLA: 444044(MGC82638)
            XTR: 394832(hadha) 448019(echs1)
            DRE: 368912(echs1)
            SPU: 575690(LOC575690) 585357(LOC585357)
            DME: Dmel_CG6543 Dmel_CG6984 Dmel_CG8778
            CEL: C29F3.1(ech-1) F38H4.8(ech-2) F43H9.1(ech-3) F56B3.5(ech-5)
                 T05G5.6(ech-6) Y105E8A.4(ech-7)
            ATH: AT3G06860(MFP2) AT4G16210 AT4G16800 AT4G29010(AIM1)
            OSA: 4326503 4328997 4330184 4332628 4341424
            CME: CMK139C
            PIC: PICST_30193(ECH1) PICST_32846(EHO3)
            CGR: CAGL0F05071g CAGL0K11968g
            ANI: AN0180.2 AN0370.2 AN5916.2 AN9128.2
            AFM: AFUA_1G01890 AFUA_2G10920 AFUA_3G07560 AFUA_6G04040
                 AFUA_8G01210
            AOR: AO090005000903 AO090011000536 AO090011000537 AO090020000138
            CNE: CND02600 CNI00240
            UMA: UM03158.1 UM04973.1
            DDI: DDB_0231502
            TET: TTHERM_00034980 TTHERM_00052130 TTHERM_00055990
                 TTHERM_00263230 TTHERM_00433850 TTHERM_00693060
            TBR: Tb11.01.8200 Tb927.3.4850
            TCR: 506727.100 507547.40 508153.130 508185.10 509701.10
                 511277.210 511529.160
            LMA: LmjF18.0580 LmjF26.1550 LmjF29.2310 LmjF32.3680 LmjF33.2600
            ECO: b1393(paaF) b1394(paaG) b2341(yfcX) b3846(fadB)
            ECJ: JW1388(paaF) JW1389(paaG) JW2338(yfcX) JW3822(fadB)
            ECE: Z3604 Z5367(fadB)
            ECS: ECs3224 ECs4774
            ECC: c2886 c4793(fadB) c5023
            ECI: UTI89_C2625 UTI89_C4431(fadB) UTI89_C4622
            ECP: ECP_2379 ECP_4059
            ECV: APECO1_2418 APECO1_2611(fadB) APECO1_4225
            ECW: EcE24377A_1579(paaB) EcE24377A_2637(fadJ)
                 EcE24377A_4365(fadB)
            ECX: EcHS_A1481 EcHS_A2492(fadJ) EcHS_A4069(fadB)
            STY: STY2620 STY3577(fadB)
            STT: t0476 t3315(fadB)
            SPT: SPA0476(yfcX) SPA3823(fadB)
            SEC: SC2390(yfcX) SC3880(fadB)
            STM: STM2388(yfcX) STM3983(fadB)
            YPE: YPO2747(faoA) YPO3766(fadB)
            YPK: y0464(fadB) y1580
            YPM: YP_2417(faoA) YP_3282(fadB)
            YPA: YPA_2097 YPA_3436
            YPN: YPN_0198 YPN_2200
            YPS: YPTB0267(fadB) YPTB2636(faoA)
            YPI: YpsIP31758_0283(fadB) YpsIP31758_1400(fadJ)
            SFL: SF2419 SF3922(fadB)
            SFX: S2554 S3830(fadB)
            SFV: SFV_2409 SFV_3654(fadB)
            SSN: SSON_2397 SSON_4019(fadB)
            SBO: SBO_2379
            SDY: SDY_2542 SDY_3899(fadB)
            ECA: ECA0208(fadB) ECA3078
            PLU: plu2614 plu3200 plu4402(fadB)
            APL: APL_0888(fadJ)
            XFA: XF1115
            XFT: PD0407(rpfF)
            XCC: XCC0810(fadB) XCC1262(paaF) XCC1263 XCC1266(fadB) XCC1833
                 XCC1857(rpfF) XCC1979(fadB)
            XCB: XC_2205 XC_2332 XC_2356 XC_2975 XC_2978 XC_2979 XC_3420
            XCV: XCV0918(paaF) XCV1365 XCV1366 XCV1369(fadB) XCV1899
                 XCV1920(rpfF) XCV2064(fadB)
            XAC: XAC0883(fadB) XAC1314(paaF) XAC1315 XAC1318(fadB) XAC1853
                 XAC1879(rpfF) XAC2013(fadB)
            XOO: XOO1844(paaF) XOO1845 XOO1848(fadB) XOO2537(fadB)
                 XOO2869(rpfF) XOO2901 XOO3728(fadB)
            XOM: XOO_1740(XOO1740) XOO_1741(XOO1741) XOO_1744(XOO1744)
                 XOO_2395(XOO2395) XOO_2723(XOO2723) XOO_2751(XOO2751)
                 XOO_3520(XOO3520)
            VCH: VC1047 VC2758
            VVU: VV1_0981 VV1_1976 VV2_0490 VV2_0491 VV2_0498
            VVY: VV0029 VV2440 VVA1039 VVA1040 VVA1048
            VPA: VP0030 VP2208 VPA0616 VPA0623 VPA0624 VPA1119 VPA1120 VPA1127
            VFI: VF0025 VF1810 VFA0023
            PPR: PBPRA0064 PBPRA0962 PBPRA2339 PBPRB1108(paaG) PBPRB1109
                 PBPRB1117 PBPRB1118
            PAE: PA0744 PA0745 PA1021 PA1240 PA1629 PA1737 PA1748 PA1821
                 PA2013 PA2767 PA2841 PA2890 PA3014(faoA) PA3426 PA3591 PA4330
                 PA4980
            PAU: PA14_19740 PA14_26690 PA14_27360 PA14_28310 PA14_38470(gnyH)
                 PA14_40980 PA14_41950 PA14_43440 PA14_51110 PA14_54640
                 PA14_54660 PA14_56250 PA14_65840
            PAP: PSPA7_2145(fadB)
            PPU: PP_1412 PP_1845 PP_2136(fadB) PP_2217(fadB1x) PP_3283(phaB)
                 PP_3284 PP_3358(ech) PP_3491 PP_3726 PP_3732 PP_4030 PP_4066
            PST: PSPTO_2065 PSPTO_2719 PSPTO_2737 PSPTO_2944 PSPTO_3163
                 PSPTO_3517(fadB) PSPTO_3705
            PSB: Psyr_1770 Psyr_1875 Psyr_2452 Psyr_2468 Psyr_2728 Psyr_3030
                 Psyr_3290
            PSP: PSPPH_1721 PSPPH_1834 PSPPH_2210 PSPPH_2433 PSPPH_2626
                 PSPPH_3210(fadB)
            PFL: PFL_1434(echA9) PFL_1840(echA17) PFL_1940(fadB)
                 PFL_2711(fad-1) PFL_3018(fad-2) PFL_3062(echA9)
                 PFL_3064(fad-3) PFL_3130(paaB) PFL_3267(fad-1) PFL_3938(echA7)
                 PFL_4198(echA7) PFL_4798
            PFO: Pfl_1348 Pfl_1744 Pfl_2864 Pfl_2866 Pfl_2882 Pfl_3658
                 Pfl_3879 Pfl_3949 Pfl_4449
            PEN: PSEEN1547 PSEEN2183 PSEEN2560 PSEEN2791(phaA) PSEEN2792(paaB)
                 PSEEN2888 PSEEN3388 PSEEN3545(fadB1x) PSEEN3728(fadB)
                 PSEEN4313
            PAR: Psyc_0310 Psyc_0753 Psyc_0902 Psyc_0903 Psyc_1171 Psyc_1399
                 Psyc_1934(fadB)
            PCR: Pcryo_0010 Pcryo_0341 Pcryo_0382 Pcryo_0750 Pcryo_1021
                 Pcryo_1234 Pcryo_1514 Pcryo_1515
            ACI: ACIAD0335(fadB) ACIAD1568 ACIAD1608 ACIAD1609 ACIAD1692(dcaE)
                 ACIAD1701 ACIAD1726(hcaA) ACIAD1820 ACIAD1829 ACIAD2351
                 ACIAD2607 ACIAD3073
            ACB: A1S_1342
            SON: SO_0021(fadB) SO_1680 SO_1681 SO_1895 SO_3088 SO_3908
            SDN: Sden_0015 Sden_0534 Sden_1530 Sden_1939 Sden_1940 Sden_2247
                 Sden_3229
            SFR: Sfri_0013 Sfri_1341 Sfri_1342 Sfri_2045 Sfri_2046 Sfri_2729
                 Sfri_3336 Sfri_3510
            SAZ: Sama_1360 Sama_1379
            SBL: Sbal_2830
            SLO: Shew_1671 Shew_2572
            SHE: Shewmr4_0018 Shewmr4_0573 Shewmr4_1408 Shewmr4_2324
                 Shewmr4_2593 Shewmr4_2594 Shewmr4_3240
            SHM: Shewmr7_0016 Shewmr7_0749 Shewmr7_1473 Shewmr7_2396
                 Shewmr7_2660 Shewmr7_2661 Shewmr7_3457
            SHN: Shewana3_0024 Shewana3_0572 Shewana3_0721 Shewana3_1461
                 Shewana3_1670 Shewana3_2767 Shewana3_2768
            SHW: Sputw3181_2308 Sputw3181_2700
            ILO: IL0011(fadB) IL0868 IL0876 IL0993 IL1863
            CPS: CPS_0393(fadB) CPS_0656 CPS_0657 CPS_1430 CPS_1601 CPS_1607
                 CPS_1947 CPS_3156(fadJ) CPS_4754
            PHA: PSHAa0011(fadB) PSHAa0717 PSHAa0882(paaF) PSHAa0903 PSHAa0905
                 PSHAa0967(fadJ) PSHAa1450 PSHAa1458 PSHAa2481
            PAT: Patl_0201 Patl_0318 Patl_0587 Patl_0950 Patl_1370 Patl_1462
                 Patl_1664 Patl_2927 Patl_3812
            PIN: Ping_0655 Ping_0656
            CBU: CBU_0976 CBU_1856
            LPN: lpg0870 lpg1352(fadB) lpg1596(yfcX) lpg1828
            LPF: lpl0902 lpl1305 lpl1429 lpl1792
            LPP: lpp0933 lpp1306 lpp1554 lpp1791
            FTU: FTT1530(fadB)
            FTF: FTF1530(fadB)
            NOC: Noc_1733 Noc_1889
            AEH: Mlg_1594 Mlg_2111
            HCH: HCH_00639 HCH_00640 HCH_01573 HCH_01668 HCH_03945 HCH_04756
                 HCH_05751
            CSA: Csal_0278 Csal_2064
            ABO: ABO_0148(ech1) ABO_0526(phaB) ABO_0987(ech2) ABO_1238
                 ABO_1566(fadB) ABO_1645(fadC) ABO_1652(fadB2) ABO_2440
                 ABO_2556(eno)
            AHA: AHA_0139(fadB) AHA_2060 AHA_2076 AHA_2082 AHA_2154(fadJ)
                 AHA_3654
            CVI: CV_1330 CV_1553 CV_1763 CV_2082(paaG) CV_2083 CV_2485
                 CV_2720(fadB) CV_3062
            RSO: RS01778(RSp0671) RS02010(RSp0035) RS05574(RSp0648)
                 RS05575(RSp0647) RSc0267(RS03234) RSc0304(RS03271)
                 RSc0474(RS04421) RSc0476(RS04419) RSc1298(RS02820)
                 RSc1759(RS02946) RSc2014(paaG2) RSc2872(paaF) RSc2873(paaG1)
                 RSp0225(fca)
            REU: Reut_A0110 Reut_A0450 Reut_A1009 Reut_A1464 Reut_A1562
                 Reut_A1671 Reut_A1822 Reut_A1904 Reut_A2019 Reut_A2182
                 Reut_A2554 Reut_A3010 Reut_A3015(paaB) Reut_A3088 Reut_A3282
                 Reut_A3284 Reut_B3608 Reut_B4260 Reut_B4261 Reut_B4461
                 Reut_B4526 Reut_B4549 Reut_B4553 Reut_B4560 Reut_B4597
                 Reut_B4780 Reut_B4870 Reut_B5245 Reut_C6106
            REH: H16_A0100 H16_A0142 H16_A0179 H16_A0461 H16_A0464 H16_A0810
                 H16_A0865 H16_A0873 H16_A1101 H16_A1410 H16_A1699 H16_A1716
                 H16_A1719 H16_A1832 H16_A1885 H16_A1889 H16_A2138 H16_A2258
                 H16_A2979 H16_A3201 H16_A3311 H16_A3593 H16_A3594 H16_B0365
                 H16_B0382 H16_B0389 H16_B0402 H16_B0419 H16_B0420 H16_B0657
                 H16_B0659 H16_B0698 H16_B0724 H16_B0756 H16_B0848 H16_B0915
                 H16_B1188 H16_B1346 H16_B1439 H16_B1738 H16_B1741 H16_B1742
                 H16_B1773 H16_B1905 H16_B1914 H16_B2156 H16_B2478
            RME: Rmet_0080 Rmet_0113 Rmet_0386 Rmet_0389 Rmet_0841 Rmet_0973
                 Rmet_1723 Rmet_2022 Rmet_2200 Rmet_2603 Rmet_3162 Rmet_3163
                 Rmet_3413 Rmet_3470 Rmet_3800 Rmet_4100 Rmet_5094 Rmet_5107
                 Rmet_5145 Rmet_5150 Rmet_5361 Rmet_5431 Rmet_5512 Rmet_5521
                 Rmet_5557 Rmet_5771
            BMA: BMA0076 BMA0198 BMA0200 BMA1244 BMA1438 BMA1803 BMAA0541
                 BMAA0544 BMAA0629 BMAA0804
            BMV: BMASAVP1_0632(fadB1) BMASAVP1_0636
            BML: BMA10299_0933 BMA10299_A1822
            BMN: BMA10247_A1899 BMA10247_A1903
            BXE: Bxe_A0468 Bxe_A0471 Bxe_A0993 Bxe_A2274 Bxe_A2495 Bxe_A2749
                 Bxe_A2765 Bxe_A3185 Bxe_A3571 Bxe_A3572 Bxe_A3896 Bxe_A4035
                 Bxe_A4233 Bxe_B0279 Bxe_B0962 Bxe_B1007 Bxe_B1088 Bxe_B1089
                 Bxe_B2534 Bxe_B2735 Bxe_B2809 Bxe_C0248 Bxe_C0249 Bxe_C0269
                 Bxe_C0278 Bxe_C0280 Bxe_C0330 Bxe_C0566 Bxe_C0567 Bxe_C0603
                 Bxe_C0700 Bxe_C0712 Bxe_C0835 Bxe_C0868 Bxe_C0889 Bxe_C1034
            BUR: Bcep18194_A3628 Bcep18194_A3631 Bcep18194_A4040
                 Bcep18194_A4702 Bcep18194_A5555 Bcep18194_A6045
                 Bcep18194_A6047 Bcep18194_A6254 Bcep18194_B0050
                 Bcep18194_B0149 Bcep18194_B0151 Bcep18194_B0425
                 Bcep18194_B0718 Bcep18194_B0719 Bcep18194_B1319
                 Bcep18194_B1434 Bcep18194_B1436 Bcep18194_B1966
                 Bcep18194_C6738 Bcep18194_C6741 Bcep18194_C7116
                 Bcep18194_C7128 Bcep18194_C7280
            BCN: Bcen_0459 Bcen_1080 Bcen_1615 Bcen_2106 Bcen_2297 Bcen_2561
                 Bcen_2564 Bcen_3129 Bcen_3408 Bcen_3409 Bcen_3840 Bcen_4289
                 Bcen_5223 Bcen_5352 Bcen_5354
            BCH: Bcen2424_0176 Bcen2424_0541 Bcen2424_0544 Bcen2424_0938
                 Bcen2424_1560 Bcen2424_2227 Bcen2424_2718 Bcen2424_2911
                 Bcen2424_3255 Bcen2424_3555 Bcen2424_4077 Bcen2424_4528
                 Bcen2424_4958 Bcen2424_4959 Bcen2424_5238 Bcen2424_5507
                 Bcen2424_5636
            BAM: Bamb_0446 Bamb_0449 Bamb_1461 Bamb_2265 Bamb_2770 Bamb_2960
            BPS: BPSL0063 BPSL0391 BPSL0649 BPSL0651 BPSL1237 BPSL1424
                 BPSL1860 BPSL3040(paaF) BPSL3043(paaG) BPSS0621 BPSS0622
                 BPSS0710 BPSS0779 BPSS1001 BPSS1446 BPSS2033
            BPM: BURPS1710b_0287(fadB) BURPS1710b_0603 BURPS1710b_0633(pimF)
                 BURPS1710b_0858(fadB) BURPS1710b_0860 BURPS1710b_1463(paaG2)
                 BURPS1710b_1985(paaG) BURPS1710b_2455 BURPS1710b_3563(paaF)
                 BURPS1710b_3566(paaB) BURPS1710b_A0469 BURPS1710b_A1151
                 BURPS1710b_A2182 BURPS1710b_A2183 BURPS1710b_A2283
                 BURPS1710b_A2361(ech) BURPS1710b_A2612(pksH)
            BPL: BURPS1106A_3571 BURPS1106A_3575(paaB)
            BPD: BURPS668_3544 BURPS668_3548(paaB)
            BTE: BTH_I0062 BTH_I0363 BTH_I0565 BTH_I0567 BTH_I1086 BTH_I2142
                 BTH_I2504 BTH_I2899 BTH_I2902(paaB) BTH_II0287 BTH_II0949
                 BTH_II1717 BTH_II1798 BTH_II1799
            BPE: BP0201 BP0309 BP0417 BP0635 BP0669 BP1446 BP1702 BP1782
                 BP1808(paaG) BP2093 BP2677(paaG) BP3277 BP3304 BP3305
            BPA: BPP0631 BPP0653 BPP0775 BPP1553 BPP1679(paaG) BPP2013
                 BPP2036(paaG) BPP2343 BPP2725 BPP2727(paaG) BPP2825 BPP3072
                 BPP3514 BPP3810 BPP4118 BPP4119 BPP4144 BPP4217
            BBR: BB0661 BB0750 BB1038 BB1087 BB1794 BB2261 BB2284 BB2631
                 BB2771(paaG) BB2773 BB3035 BB3146 BB3429(paaG) BB3949 BB4255
                 BB4415 BB4588 BB4589 BB4614 BB4711 BB4755 BB4757 BB4805
            RFR: Rfer_0223 Rfer_0608 Rfer_0995 Rfer_1007 Rfer_1009 Rfer_1010
                 Rfer_1573 Rfer_1890 Rfer_2139 Rfer_2282 Rfer_2591 Rfer_2816
                 Rfer_3498 Rfer_3512 Rfer_3517 Rfer_3831 Rfer_4068
            POL: Bpro_0591 Bpro_0649 Bpro_1122 Bpro_1631 Bpro_1633 Bpro_2431
                 Bpro_2472 Bpro_2473 Bpro_2958 Bpro_3834 Bpro_3932 Bpro_3956
                 Bpro_4159 Bpro_4708 Bpro_5267 Bpro_5283
            MPT: Mpe_A0414 Mpe_A0597 Mpe_A0881 Mpe_A0893 Mpe_A0984 Mpe_A1436
                 Mpe_A3358
            HAR: HEAR0207(ECHS1) HEAR1954 HEAR2837(yusL) HEAR3118
            MMS: mma_0240 mma_1382 mma_3090 mma_3361
            NEU: NE1528
            NMU: Nmul_A0097
            EBA: c1A208(fadB) c2A174 ebA1321(ech) ebA2191(crt) ebA2313
                 ebA3542(paaG) ebA3642 ebA5732(paaF) ebA6516 ebA722 p2A341
            AZO: azo0066 azo0300(paaG1) azo0468(fadB2) azo0470(paaG2)
                 azo0790(paaF1) azo1696(paaF2) azo1927 azo1932(abmC)
                 azo2498(paaG3) azo3043(paaG4) azo3056 azo3069(paaG5)
                 azo3857(paaG6)
            DAR: Daro_0090 Daro_0176 Daro_0371(paaB) Daro_0382 Daro_0383
                 Daro_0558 Daro_1547 Daro_2350 Daro_2354 Daro_3320
            TBD: Tbd_2672
            MFA: Mfla_2657
            GME: Gmet_1572 Gmet_2057 Gmet_2071 Gmet_2224 Gmet_3284 Gmet_3291
            BBA: Bd1836 Bd1852 Bd2691 Bd3579
            ADE: Adeh_0408 Adeh_1854
            MXA: MXAN_2034 MXAN_2698 MXAN_3940 MXAN_5136 MXAN_5371(fadJ)
                 MXAN_5841 MXAN_6608 MXAN_7157
            SAT: SYN_03076
            RPR: RP560(fadB)
            RTY: RT0547(fadB)
            RCO: RC0836 RC0837 RC0838 RC0839 RC0840 RC0841 RC0842
            RFE: RF_0890(fadB)
            PUB: SAR11_1260(ydbS)
            MLO: mll1009 mll4199 mll5431 mll5584 mlr1841 mlr5044 mlr5629
                 mlr7453 mlr8461
            MES: Meso_0021 Meso_1130 Meso_1524 Meso_2951 Meso_3285 Meso_4101
            SME: SMb20752 SMb21126(eccH2) SMb21633(paaG) SMc00976 SMc01153
                 SMc01641 SMc01806 SMc02227(fadB) SMc04398
            ATU: Atu0322(fadB) Atu0503(fadB) Atu0733
            ATC: AGR_C_1329 AGR_C_562 AGR_C_888 AGR_L_2647
            RET: RHE_CH00356(fadB1) RHE_CH00559(fadB2) RHE_CH00571(ypch00209)
                 RHE_CH00906(ypch00296) RHE_CH01573(ypch00545)
                 RHE_CH01721(ypch00578) RHE_PC00129 RHE_PF00542(ypf00266)
            RLE: RL0373 RL0606 RL0966 RL1675 RL1852 pRL100293 pRL100378
                 pRL120069 pRL120176 pRL120505(ech)
            BME: BMEI1196 BMEI1522 BMEI1927 BMEI1928 BMEI1945 BMEII0497
                 BMEII1021
            BMF: BAB1_0016 BAB1_0439 BAB1_0781 BAB1_2046 BAB1_2185 BAB2_0444
            BMS: BR0016 BR0411 BR0758 BR2046 BR2184 BRA0222 BRA0793(fadB)
            BMB: BruAb1_0016 BruAb1_0434 BruAb1_0775 BruAb1_2021 BruAb1_2157
                 BruAb2_0439(fadB)
            BOV: BOV_A0744(fadB)
            BJA: bll0116 bll0143 bll0552 bll2655 bll2783 bll2830 bll3036(fadB)
                 bll3950 bll6036 bll6081 bll6263 bll6365(fadB) bll7803 bll7821
                 bll7955 blr0140 blr1160(fadB) blr2230 blr2428 blr2943 blr2950
                 blr2952 blr3445 blr3956 blr4965(fadB) blr5604 blr7901
            BRA: BRADO0646 BRADO0651 BRADO0932 BRADO0943 BRADO0962
                 BRADO0981(pimF) BRADO2169 BRADO2321 BRADO2462 BRADO2490
                 BRADO2571 BRADO2574 BRADO2578 BRADO2663 BRADO2915 BRADO3135
                 BRADO3139 BRADO3707 BRADO4219 BRADO5988 BRADO6723
            BBT: BBta_0817 BBta_1789 BBta_2485 BBta_2630 BBta_2637 BBta_2682
                 BBta_2805 BBta_2835 BBta_2918 BBta_2921 BBta_2926 BBta_3005
                 BBta_3576 BBta_3580 BBta_4594 BBta_5262 BBta_7074(pimF)
                 BBta_7093 BBta_7111 BBta_7120 BBta_7536 BBta_7538
            RPA: RPA0383 RPA0416 RPA0484(paaG1) RPA0818 RPA0957 RPA1411
                 RPA1706 RPA1712 RPA1758 RPA1765 RPA1811 RPA2145 RPA2316
                 RPA2765 RPA3305(paaG2) RPA3447 RPA3717(pimF) RPA3795
                 RPA4321(paaG3) RPA4339
            RPB: RPB_0111 RPB_0555 RPB_0701 RPB_1304 RPB_1746 RPB_2669
                 RPB_3258 RPB_3557 RPB_3605 RPB_4073 RPB_4455 RPB_4604
            RPC: RPC_0344 RPC_0681 RPC_0735 RPC_1036 RPC_1155 RPC_1674
                 RPC_1738 RPC_2226 RPC_2694 RPC_3199
            RPD: RPD_0274 RPD_0691 RPD_0807 RPD_1132 RPD_1545 RPD_1831
                 RPD_1862 RPD_1908 RPD_3553 RPD_3809 RPD_3917
            RPE: RPE_0121 RPE_0615 RPE_0674 RPE_0998 RPE_1073 RPE_1703
                 RPE_1782 RPE_1836 RPE_2256 RPE_2305 RPE_2386 RPE_2855 RPE_3780
                 RPE_3803 RPE_3820
            NWI: Nwi_0636 Nwi_2157 Nwi_2252
            NHA: Nham_0357 Nham_0781 Nham_0938 Nham_2557 Nham_2662
            BHE: BH08520
            CCR: CC_0006 CC_0076 CC_0353 CC_0397 CC_0947 CC_1723 CC_1814
                 CC_1851 CC_2169 CC_2401 CC_2575 CC_3189
            SIL: SPO0147 SPO0666 SPO0739 SPO0740(paaB) SPO0777 SPO1687 SPO1971
                 SPO2212 SPO2787 SPO2920(fabJ-1) SPO3025 SPOA0285(caiD-2)
                 SPOA0404 SPOA0424(fabJ-2)
            SIT: TM1040_0438 TM1040_0740 TM1040_1102 TM1040_1171 TM1040_1436
                 TM1040_1980 TM1040_2240 TM1040_2636 TM1040_2793 TM1040_3030
            RSP: RSP_0155 RSP_1340 RSP_2196 RSP_2511 RSP_3535 RSP_3833(fadB)
            JAN: Jann_0406 Jann_0665 Jann_1150 Jann_1326 Jann_1908 Jann_2430
                 Jann_3824 Jann_4211
            RDE: RD1_0205 RD1_0287 RD1_0476 RD1_0509 RD1_0613(caiD) RD1_1753
                 RD1_3221(paaB) RD1_3294 RD1_3973(fadJ)
            MMR: Mmar10_0312 Mmar10_0543 Mmar10_0752 Mmar10_1543 Mmar10_1674
                 Mmar10_1729 Mmar10_2248 Mmar10_2653 Mmar10_2692 Mmar10_3078
            HNE: HNE_0065 HNE_0566 HNE_0672 HNE_0907 HNE_0981 HNE_1282
                 HNE_1824 HNE_1827 HNE_2016 HNE_2166 HNE_2443 HNE_2777 HNE_2804
                 HNE_3375
            NAR: Saro_0860 Saro_2094
            SAL: Sala_0852 Sala_3055
            ELI: ELI_04665 ELI_10035
            RRU: Rru_A1834 Rru_A1942 Rru_A2156 Rru_A2240 Rru_A2506 Rru_A3801
            MAG: amb0178 amb0634 amb0675 amb0852 amb2589 amb2597 amb3583
                 amb4133
            ABA: Acid345_2469 Acid345_3945 Acid345_4027
            BSU: BG12331(ysiB) BG13457(yngF) BG14024(yusL)
            BHA: BH0201(phaA) BH0202(phaB) BH0207 BH1849 BH1996 BH2582 BH3101
                 BH3488 BH3824
            BAN: BA2356 BA4761 BA5249
            BAR: GBAA2356 GBAA4761 GBAA5249
            BAA: BA_0114 BA_2850 BA_5191
            BAT: BAS0333 BAS2195 BAS4420 BAS4877
            BCE: BC2292 BC5004
            BCA: BCE_2384 BCE_5144
            BCZ: BCZK0320(fucA) BCZK2118(phaB) BCZK2687(fadB) BCZK3237
                 BCZK4271(phaB) BCZK4734(fadB)
            BTK: BT9727_0317(fucA) BT9727_2132(phaB) BT9727_3285(caiD)
                 BT9727_4259(phaB) BT9727_4719(fadB)
            BTL: BALH_0339(fucA) BALH_2100(phaB) BALH_3171(caiD)
                 BALH_4108(phaB) BALH_4547(fadB)
            BLI: BL00294 BL00295 BL00329(ysiB) BL01991(yngF) BL02180(yusL)
            BLD: BLi02102 BLi02103 BLi02140(yngF) BLi03001(ysiB)
                 BLi03466(yusL)
            BCL: ABC1509 ABC1810 ABC2671 ABC2990 ABC3911
            BAY: RBAM_021940 RBAM_025600(ysiB)
            BPU: BPUM_0932 BPUM_1781(yngF) BPUM_2511(ysiB)
            OIH: OB0682 OB0817 OB1698 OB2120 OB2395 OB2668
            GKA: GK1685 GK1992 GK2038 GK2039 GK2688 GK3008
            SAU: SA0224
            SAV: SAV0232
            SAM: MW0208
            SAR: SAR0224(fadB)
            SAS: SAS0208
            SAC: SACOL0212
            SAB: SAB0171c
            SAA: SAUSA300_0226
            SAO: SAOUHSC_00196
            SSP: SSP2424
            SPY: SPy_1758(phaB)
            SPZ: M5005_Spy_1496(phaB)
            SPM: spyM18_1829
            SPG: SpyM3_1529(phaB)
            SPS: SPs0337
            SPH: MGAS10270_Spy1564(phaB)
            SPI: MGAS10750_Spy1556(phaB)
            SPJ: MGAS2096_Spy1524(phaB)
            SPK: MGAS9429_Spy1498(phaB)
            SPA: M6_Spy1490
            SPB: M28_Spy1485(phaB)
            SPN: SP_0415
            SPR: spr0375(phaB)
            SAG: SAG0342
            SAN: gbs0329
            SAK: SAK_0416
            SMU: SMU.1746c
            STC: str0380(phaB)
            STL: stu0380(phaB)
            SSA: SSA_1942(phaB)
            SGO: SGO_1700
            STH: STH212 STH213
            CBO: CBO3202(crt)
            CHY: CHY_1609 CHY_1736 CHY_2254
            DSY: DSY3369 DSY3374 DSY4307
            MTU: Rv0632c(echA3) Rv0675(echA5) Rv0860(fadB) Rv0905(echA6)
                 Rv0971c(echA7) Rv1070c(echA8) Rv1071c Rv1141c Rv1142c Rv1472
                 Rv2486(echA14) Rv2679(echA15) Rv2831(echA16) Rv3039c(echA17)
                 Rv3374(echA18.1) Rv3516(echA19) Rv3550(echA20) Rv3774(echA21)
            MTC: MT0660 MT0704 MT0883 MT0928 MT0999.1 MT1100 MT1101 MT1174
                 MT1175 MT1518 MT2560 MT2753 MT2897 MT3124 MT3617 MT3654 MT3883
            MBO: Mb0464c(echA2) Mb0649c(echA3) Mb0692(echA4) Mb0694(echA5)
                 Mb0883(fadB) Mb0929(echA6) Mb0996c(echA7) Mb1099c(echA8)
                 Mb1100c(echA9) Mb1173c(echA11) Mb1174c(echA10) Mb1507(echA12)
                 Mb1970c(echA13) Mb2511(echA14) Mb2698(echA15) Mb2855(echA16)
                 Mb3065c(echA17) Mb3408(echA18) Mb3545(echA19) Mb3580(echA20)
                 Mb3803(echA21)
            MBB: BCG_0495c(echA2) BCG_0679c(echA3) BCG_0722(echA4)
                 BCG_0724(echA5) BCG_0957(echA6) BCG_1025c(echA7)
                 BCG_1128c(echA8) BCG_1129c(echA9) BCG_1203c(echA11)
                 BCG_1204c(echA10) BCG_1533(echA12) BCG_1974c(echA13)
                 BCG_2504(echA14) BCG_2692 BCG_2851(echA16) BCG_3063c(echA17)
                 BCG_3445(echA18) BCG_3579(echA19) BCG_3614(echA20)
                 BCG_3836(echA21)
            MLE: ML0120(echA1) ML1241 ML1724 ML2118(echA6) ML2161(fadB) ML2401
                 ML2402
            MPA: MAP0249c(echA21) MAP0516c(echA20) MAP0549c(echA19)
                 MAP0790(fadB_1) MAP0840(echA6) MAP0909c(echA7)
                 MAP1017c(echA8_1) MAP1018c(echA9) MAP1197(echA12_2) MAP1593
                 MAP1715(fadB_2) MAP2306(echA14) MAP2390c MAP2639(echA11)
                 MAP2800(echA15) MAP2904(echA16_2) MAP3087c(echA17) MAP3121
                 MAP3949c(echA2) MAP4136(echA5)
            MAV: MAV_0247 MAV_1195 MAV_3307 MAV_5086
            MSM: MSMEG_1048 MSMEG_1331 MSMEG_1594 MSMEG_2047 MSMEG_2229
                 MSMEG_2328 MSMEG_2641 MSMEG_2880 MSMEG_3139 MSMEG_3362
                 MSMEG_3390 MSMEG_3567 MSMEG_4299 MSMEG_4709 MSMEG_4846
                 MSMEG_5185 MSMEG_5276 MSMEG_5277 MSMEG_5495 MSMEG_5620
                 MSMEG_5639 MSMEG_5886 MSMEG_5915 MSMEG_6001 MSMEG_6353
                 MSMEG_6777
            MMC: Mmcs_0178 Mmcs_0306 Mmcs_0615 Mmcs_0911 Mmcs_0976 Mmcs_0978
                 Mmcs_1254 Mmcs_1500 Mmcs_1563 Mmcs_1858 Mmcs_2088 Mmcs_2445
                 Mmcs_2760 Mmcs_3333 Mmcs_3623 Mmcs_3753 Mmcs_4070 Mmcs_4155
                 Mmcs_4156 Mmcs_4309 Mmcs_4399 Mmcs_4431 Mmcs_4607 Mmcs_4628
                 Mmcs_4683 Mmcs_4986
            CGL: NCgl0882(cgl0919)
            CGB: cg1049
            CEF: CE0672 CE0722 CE0981
            CDI: DIP0789 DIP0885
            CJK: jk0159(fadB1) jk0395(echA1) jk0431(echA2) jk1463(echA3)
                 jk1503(echA5) jk2017(echA4)
            NFA: nfa10410(echA8) nfa11770(echA9) nfa21600(echA11)
                 nfa2860(fadB) nfa29860(echA14) nfa33800(echA17) nfa3830(echA1)
                 nfa42890(echA18) nfa50130(echA20) nfa5100(echA4)
                 nfa5280(echA5) nfa53270(echA21) nfa6740(echA6) nfa7230(echA7)
            RHA: RHA1_ro00085 RHA1_ro01538 RHA1_ro01540 RHA1_ro01928
                 RHA1_ro01936 RHA1_ro02289 RHA1_ro02308 RHA1_ro02669
                 RHA1_ro02697 RHA1_ro02860(paaB) RHA1_ro02862(paaA)
                 RHA1_ro03070 RHA1_ro03243 RHA1_ro03948 RHA1_ro03957
                 RHA1_ro04094 RHA1_ro04205(fadB1) RHA1_ro04252 RHA1_ro04398
                 RHA1_ro04594 RHA1_ro04652 RHA1_ro04688(echA19) RHA1_ro05033
                 RHA1_ro05401 RHA1_ro06116(fadB2) RHA1_ro06118 RHA1_ro06453
                 RHA1_ro06513 RHA1_ro06681 RHA1_ro07067 RHA1_ro07071
                 RHA1_ro07072 RHA1_ro08049 RHA1_ro08144 RHA1_ro08870
                 RHA1_ro08944 RHA1_ro09031 RHA1_ro10312 RHA1_ro10316
                 RHA1_ro10427 RHA1_ro11182
            SCO: SCO0364(SCF41.23) SCO4384(SCD10.16) SCO4930(SCK13.22)
                 SCO5144(SCP8.07c) SCO5979(StBAC16H6.14) SCO6732(SC5F2A.15)
                 SCO6789(SC6A5.38)
            SMA: SAV1245(echA4) SAV1350(echA5) SAV1680(fadB1) SAV2316(echA7)
                 SAV3120 SAV3327(echA9) SAV3829(echA11) SAV3863(echA12)
                 SAV6203(echA13) SAV635(echA2) SAV7216(echA15)
            CMI: CMM_1133(echA) CMM_1661(fadB)
            PAC: PPA1899
            NCA: Noca_4295
            TFU: Tfu_0067 Tfu_0501 Tfu_1259
            FRA: Francci3_2457 Francci3_2861 Francci3_3662
            FAL: FRAAL0183 FRAAL0396 FRAAL0884 FRAAL1641 FRAAL1656 FRAAL1669
                 FRAAL2442 FRAAL2628 FRAAL2641 FRAAL2805 FRAAL3109 FRAAL3136
                 FRAAL3424 FRAAL3484 FRAAL3491 FRAAL3544 FRAAL3799 FRAAL3968
                 FRAAL4129 FRAAL4379 FRAAL4399 FRAAL4765 FRAAL4766 FRAAL4771
                 FRAAL4772 FRAAL4854 FRAAL5131 FRAAL5276 FRAAL5547
                 FRAAL5882(echA)
            SEN: SACE_1028(echA11) SACE_1458(echA9) SACE_1464(echA21)
                 SACE_2748 SACE_2794 SACE_3018(phaB) SACE_3084(echA5) SACE_3450
                 SACE_3745 SACE_3868 SACE_3989 SACE_4015(echA6)
                 SACE_4571(echA7) SACE_4787 SACE_5406 SACE_6207(echA)
                 SACE_6362(fadB)
            RXY: Rxyl_1748 Rxyl_1762 Rxyl_2054 Rxyl_2277 Rxyl_2341
            FNU: FN0271
            RBA: RB1092(faoA) RB7812
            LIL: LA0073(ech1) LA0918(ech2) LA1032(ech3) LA1198(ech4)
                 LA2265(ech5) LA3366(ech6) LA3644(ech7)
            AVA: Ava_3339
            SRU: SRU_1210 SRU_1459(yfcX)
            CHU: CHU_0017(paaG) CHU_3179(phaB) CHU_3591(fadB)
            DRA: DR_0114 DR_0184 DR_1487 DR_2477 DR_2510
            DGE: Dgeo_0145 Dgeo_1797 Dgeo_2162
            TTH: TTC0534 TTC1697 TTC1768
            TTJ: TTHA0218 TTHA0290 TTHA0890
            AFU: AF0017(hbd-1) AF0285(hbd-2) AF0435(fad-1) AF1122(hbd-5)
                 AF2273(hbd-10)
            HAL: VNG0428G(fad2) VNG1313G(hbd2) VNG2032Gm(fad1)
            HMA: rrnAC0833(ech2) rrnAC0841(ech1) rrnAC1083(hbd1)
                 rrnAC1979(ech5) rrnAC1982(hbd2) rrnAC2484(ech3) rrnB0237(ech4)
                 rrnB0254(ech6)
            HWA: HQ2394A(fadA)
            NPH: NP0032A(fadA_6) NP1462A(fadA_5) NP2632A(fadA_1)
                 NP2754A(hbd_2) NP2758A(fadB_2) NP2936A(fadA_7) NP3434A(fadA_4)
                 NP3830A(fadA_8) NP4248A(fadB_1) NP4322A(hbd_3)
            TAC: Ta0061 Ta0121 Ta0291 Ta0440
            TVO: TVN0017 TVN0198 TVN0915 TVN1310
            PTO: PTO0954
            APE: APE_0056.1 APE_0591.1 APE_1484.1
            SSO: SSO0050(paaF-1) SSO0654(paaF-2) SSO1311(paaF-3)
                 SSO2017(paaF-4) SSO2514 SSO2535(paaF-5) SSO2623(paaF-6)
                 SSO2624(paaF-7)
            STO: ST0069 ST0095 ST2416 ST2417
            SAI: Saci_1109 Saci_1134 Saci_1772(crt) Saci_2208 Saci_2218
                 Saci_2285(paaF) Saci_2286(paaF)
            PAI: PAE1383
STRUCTURES  PDB: 1DCI  1DUB  1EY3  1HZD  1IQ6  1MJ3  1UIY  1WDK  1WDL  1WDM  
                 1WZ8  2C2I  2D3T  2DUB  2HW5  2PBP  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.17
            ExPASy - ENZYME nomenclature database: 4.2.1.17
            ExplorEnz - The Enzyme Database: 4.2.1.17
            ERGO genome analysis and discovery system: 4.2.1.17
            UM-BBD (Biocatalysis/Biodegradation Database): 4.2.1.17
            BRENDA, the Enzyme Database: 4.2.1.17
            CAS: 9027-13-8
///
ENTRY       EC 4.2.1.18                 Enzyme
NAME        methylglutaconyl-CoA hydratase;
            methylglutaconyl coenzyme A hydratase;
            3-methylglutaconyl CoA hydratase;
            methylglutaconase;
            (S)-3-hydroxy-3-methylglutaryl-CoA hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (S)-3-hydroxy-3-methylglutaryl-CoA hydro-lyase
            (trans-3-methylglutaconyl-CoA-forming)
REACTION    (S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-methylglutaconyl-CoA +
            H2O [RN:R02085]
ALL_REAC    R02085
SUBSTRATE   (S)-3-hydroxy-3-methylglutaryl-CoA [CPD:C00356]
PRODUCT     trans-3-methylglutaconyl-CoA [CPD:C03231];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:13535602]
  AUTHORS   HILZ H, KNAPPE J, RINGELMANN E, LYNEN F.
  TITLE     [Methylglutaconase, a new hydrase participating in the metabolism of
            various carboxylic acids.]
  JOURNAL   Biochem. Z. 329 (1958) 476-89.
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
ORTHOLOGY   KO: K05607  methylglutaconyl-CoA hydratase
GENES       HSA: 549(AUH)
            PTR: 464587(AUH)
            MMU: 11992(Auh)
            CFA: 476348(AUH)
            SPU: 577505(LOC577505)
            AFM: AFUA_3G11480
            UMA: UM01935.1
            TTH: TTC0182
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.18
            ExPASy - ENZYME nomenclature database: 4.2.1.18
            ExplorEnz - The Enzyme Database: 4.2.1.18
            ERGO genome analysis and discovery system: 4.2.1.18
            BRENDA, the Enzyme Database: 4.2.1.18
            CAS: 9024-24-2
///
ENTRY       EC 4.2.1.19                 Enzyme
NAME        imidazoleglycerol-phosphate dehydratase;
            IGP dehydratase;
            D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     D-erythro-1-(imidazol-4-yl)glycerol-3-phosphate hydro-lyase
            [3-(imidazol-4-yl)-2-oxopropyl-phosphate-forming]
REACTION    D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate =
            3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O [RN:R03457]
ALL_REAC    R03457
SUBSTRATE   D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate [CPD:C04666]
PRODUCT     3-(imidazol-4-yl)-2-oxopropyl phosphate [CPD:C01267];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:13475302]
  AUTHORS   AMES BN.
  TITLE     The biosynthesis of histidine; D-erythro-imidazoleglycerol phosphate
            dehydrase.
  JOURNAL   J. Biol. Chem. 228 (1957) 131-43.
  ORGANISM  Neurospora crassa [GN:dncr], Escherichia coli [GN:eco]
PATHWAY     PATH: map00340  Histidine metabolism
ORTHOLOGY   KO: K01693  imidazoleglycerol-phosphate dehydratase
GENES       ATH: AT4G14910(IGPD)
            OSA: 4337007
            CME: CMP234C
            SCE: YOR202W(HIS3)
            AGO: AGOS_ADL270C
            CGR: CAGL0L02937g
            SPO: SPBC21H7.07c(his5)
            ANI: AN6536.2
            AFM: AFUA_6G04700
            AOR: AO090701000070
            CNE: CNH01620
            ECO: b2022(hisB)
            ECJ: JW2004(hisB)
            ECE: Z3184(hisB)
            ECS: ECs2823
            ECC: c2549(hisB)
            ECI: UTI89_C2295(hisB)
            ECP: ECP_2065
            ECW: EcE24377A_2313(hisB)
            ECX: EcHS_A2161(hisB)
            STY: STY2283(hisB)
            STT: t0799(hisB)
            SPT: SPA0797(hisB)
            SEC: SC2084(hisB)
            STM: STM2074(hisB)
            YPE: YPO1546(hisB)
            YPK: y2623(hisB)
            YPM: YP_1435(hisB1)
            YPA: YPA_0842
            YPN: YPN_2433
            YPS: YPTB1559(hisB)
            YPI: YpsIP31758_2431(hisB)
            SFL: SF2084(hisB)
            SFX: S2205(hisB)
            SFV: SFV_2082(hisB)
            SSN: SSON_2093(hisB)
            SBO: SBO_0848(hisB)
            SDY: SDY_2219(hisB)
            ECA: ECA2585(hisB)
            PLU: plu1568(hisB)
            BUC: BU102(hisB)
            BAS: BUsg095(hisB)
            BAB: bbp096(hisB)
            BCC: BCc_066(hisB)
            SGL: SG1127
            BFL: Bfl465(hisB)
            BPN: BPEN_480(hisB)
            HIN: HI0471(hisB)
            HIT: NTHI0602(hisB)
            HIP: CGSHiEE_00635
            HIQ: CGSHiGG_05605
            PMU: PM1200(hisB)
            MSU: MS1890(hisB)
            APL: APL_2023(hisB)
            XFA: XF2217
            XFT: PD1265(hisB)
            XCC: XCC1811(hisB)
            XCB: XC_2378
            XCV: XCV1877(hisB)
            XAC: XAC1831(hisB)
            XOO: XOO2258(hisB)
            XOM: XOO_2121(XOO2121)
            VCH: VC1135
            VCO: VC0395_A0705(hisB)
            VVU: VV1_2917
            VVY: VV1353
            VPA: VP1140
            VFI: VF1015
            PPR: PBPRA1089
            PAE: PA5143(hisB)
            PAU: PA14_67930(hisB)
            PPU: PP_0289(hisB)
            PPF: Pput_0309
            PST: PSPTO_5338(hisB)
            PSB: Psyr_4897
            PSP: PSPPH_4926(hisB)
            PFL: PFL_0361
            PFO: Pfl_0323
            PEN: PSEEN5195(hisB)
            PMY: Pmen_4256
            PAR: Psyc_2121(hisB)
            PCR: Pcryo_2443
            PRW: PsycPRwf_0060
            ACI: ACIAD3395(hisB)
            SON: SO_2071(hisB)
            SHN: Shewana3_1851
            ILO: IL1837(hisB)
            CPS: CPS_3892(hisB)
            PHA: PSHAb0491(hisB)
            SDE: Sde_0487
            MAQ: Maqu_3173
            LPN: lpg1197
            LPF: lpl1205(hisB)
            LPP: lpp1199(hisB)
            MCA: MCA2805(hisB)
            TCX: Tcr_1966
            NOC: Noc_3051
            AEH: Mlg_2617
            HHA: Hhal_1094
            HCH: HCH_01342(hisB)
            CSA: Csal_0519
            ABO: ABO_2281(hisB)
            MMW: Mmwyl1_0753
            AHA: AHA_2193
            BCI: BCI_0402(hisB)
            RMA: Rmag_0950
            VOK: COSY_0849
            NME: NMB1583
            NMA: NMA1772(hisB)
            NMC: NMC1503(hisB)
            NGO: NGO1242
            CVI: CV_0614(hisB)
            RSO: RSc2950(hisB)
            REU: Reut_A3109
            REH: H16_A3414(hisB)
            RME: Rmet_3246
            BMA: BMA2712(hisB)
            BMV: BMASAVP1_A3241(hisB)
            BML: BMA10299_A1790(hisB)
            BMN: BMA10247_2763(hisB)
            BXE: Bxe_A0400
            BVI: Bcep1808_0406
            BUR: Bcep18194_A3525
            BCN: Bcen_2680
            BCH: Bcen2424_0427
            BAM: Bamb_0345
            BPS: BPSL3137(hisB)
            BPM: BURPS1710b_3691(hisB)
            BPL: BURPS1106A_3722(hisB)
            BPD: BURPS668_3664(hisB)
            BTE: BTH_I2991
            PNU: Pnuc_0109
            BPE: BP3770(hisB)
            BPA: BPP4269(hisB)
            BBR: BB4856(hisB)
            RFR: Rfer_2948
            POL: Bpro_0806
            PNA: Pnap_0698
            AAV: Aave_1032
            AJS: Ajs_0763
            VEI: Veis_4375
            MPT: Mpe_A0833
            HAR: HEAR3067(hisB)
            MMS: mma_3286(hisB)
            NEU: NE0646(hisB)
            NET: Neut_1906
            NMU: Nmul_A0817
            EBA: ebA1296(hisB)
            AZO: azo3347(hisB)
            DAR: Daro_3382
            TBD: Tbd_1711
            MFA: Mfla_0251
            HHE: HH1325(hisB)
            WSU: WS2070(hisB)
            TDN: Tmden_1080
            CJE: Cj1599(hisB)
            CJR: CJE1771(hisB)
            CJU: C8J_1501(hisB)
            CFF: CFF8240_1189(hisB)
            CCV: CCV52592_0457(hisB)
            CHA: CHAB381_0302(hisB)
            CCO: CCC13826_1989(hisB)
            ABU: Abu_0977(hisB)
            NIS: NIS_0777
            SUN: SUN_1227
            GSU: GSU3098(hisB)
            GME: Gmet_0386
            GUR: Gura_4056
            PCA: Pcar_2687
            PPD: Ppro_3040
            DVU: DVU1040(hisB)
            DVL: Dvul_1953
            DDE: Dde_1467
            DPS: DP1328
            ADE: Adeh_0713
            AFW: Anae109_0754
            MXA: MXAN_4225(hisB)
            SAT: SYN_03108
            SFU: Sfum_4004
            PUB: SAR11_0332(hisB)
            MLO: mlr5008
            MES: Meso_3493
            PLA: Plav_1237
            SME: SMc02574(hisB)
            SMD: Smed_3263
            ATU: Atu0043(hisB)
            ATC: AGR_C_69(igpD)
            RET: RHE_CH00047(hisB)
            RLE: RL0048(hisB)
            BME: BMEI2045
            BMF: BAB1_2082(hisB)
            BMS: BR2081(hisB)
            BMB: BruAb1_2056(hisB)
            BOV: BOV_2001(hisB)
            OAN: Oant_0838
            BJA: blr0650(hisB)
            BRA: BRADO0212(hisB)
            BBT: BBta_0148(hisB)
            RPA: RPA0309(hisB)
            RPB: RPB_0405
            RPC: RPC_0304
            RPD: RPD_0415
            RPE: RPE_0370
            NWI: Nwi_0126
            NHA: Nham_0122
            XAU: Xaut_2293
            CCR: CC_3734
            SIL: SPO1163(hisB)
            SIT: TM1040_2033
            RSP: RSP_2246(hisB)
            RSH: Rsph17029_0921
            RSQ: Rsph17025_2249
            JAN: Jann_2788
            RDE: RD1_3556(hisB)
            PDE: Pden_1883
            HNE: HNE_0073(hisB)
            ZMO: ZMO1503(hisB)
            NAR: Saro_1006
            SAL: Sala_3149
            SWI: Swit_2717
            ELI: ELI_09570
            GOX: GOX0479
            GBE: GbCGDNIH1_2235
            ACR: Acry_1413
            RRU: Rru_A3597
            MAG: amb4534
            MGM: Mmc1_2938
            ABA: Acid345_3685
            SUS: Acid_3852
            BSU: BG12598(hisB)
            BHA: BH3581(hisB)
            BAN: BA1427(hisB)
            BAR: GBAA1427(hisB)
            BAA: BA_1947
            BAT: BAS1318
            BCE: BC1407
            BCA: BCE_1527(hisB)
            BCZ: BCZK1292(hisB)
            BCY: Bcer98_1130
            BTK: BT9727_1291(hisB)
            BLI: BL03409(hisB)
            BLD: BLi03735(hisB)
            BCL: ABC3047(hisB)
            BAY: RBAM_032110(hisB)
            BPU: BPUM_3125(hisB)
            OIH: OB0550
            GKA: GK3074
            SAU: SA2468(hisB)
            SAV: SAV2676(hisB)
            SAM: MW2595(hisB)
            SAR: SAR2758(hisB)
            SAS: SAS2561
            SAC: SACOL2700(hisB)
            SAB: SAB2552c(hisB)
            SAA: SAUSA300_2609(hisB)
            SAO: SAOUHSC_03011
            SAJ: SaurJH9_2700
            SAH: SaurJH1_2757
            SEP: SE0273
            SER: SERP2304(hisB)
            SSP: SSP0427
            LMO: lmo0566(hisB)
            LMF: LMOf2365_0595(hisB)
            LIN: lin0575(hisB)
            LWE: lwe0532(hisB)
            LLA: L0068(hisB)
            LLC: LACR_1331
            LLM: llmg_1294(hisB)
            SMU: SMU.1268(hisB)
            SSA: SSA_1445(hisB)
            SGO: SGO_1407(igpD)
            LPL: lp_2558(hisB)
            LCA: LSEI_1432
            STH: STH2836(hisB)
            CAC: CAC0938(hisB)
            CNO: NT01CX_1064
            CTH: Cthe_2884
            CDF: CD1550(hisB)
            CBO: CBO1568(hisB)
            CBA: CLB_1588(hisB)
            CBH: CLC_1599(hisB)
            CBF: CLI_1650(hisB)
            CBE: Cbei_1319
            CKL: CKL_1297(hisB)
            AMT: Amet_0574
            CHY: CHY_1087(hisB)
            DSY: DSY3911
            DRM: Dred_2353
            SWO: Swol_1767
            CSC: Csac_2023
            TTE: TTE2136(hisB)
            MTA: Moth_2034
            MTU: Rv1601(hisB)
            MTC: MT1637(hisB)
            MBO: Mb1627(hisB)
            MBB: BCG_1639(hisB)
            MLE: ML1259(hisB)
            MPA: MAP1295(hisB)
            MAV: MAV_3185(hisB)
            MSM: MSMEG_3207(hisB)
            MVA: Mvan_2806
            MGI: Mflv_3611
            MMC: Mmcs_3061
            MKM: Mkms_3120
            MJL: Mjls_3077
            CGL: NCgl2019(cgl2100)
            CGB: cg2303(hisB)
            CEF: CE2001(hisB)
            CDI: DIP1564(hisB)
            CJK: jk0788(hisB)
            NFA: nfa18470(hisB)
            RHA: RHA1_ro01029(hisB)
            SCO: SCO2052(hisB)
            SMA: SAV6155(hisB)
            LXX: Lxx15850(hisB)
            ART: Arth_1471
            AAU: AAur_1605(hisB)
            PAC: PPA1154
            NCA: Noca_3043
            TFU: Tfu_1152
            FRA: Francci3_3025
            FAL: FRAAL2729 FRAAL5002(hisB)
            ACE: Acel_1060
            KRA: Krad_3175
            SEN: SACE_5776(hisB)
            STP: Strop_3194
            BLO: BL1297(hisB)
            BAD: BAD_1127(hisB)
            RXY: Rxyl_1103
            RBA: RB7662(hisBD)
            LIL: LA0124(hisB)
            LIC: LIC10112(hisB)
            LBJ: LBJ_0101(hisB)
            LBL: LBL_0034(hisB)
            SYN: slr0500(hisB)
            SYW: SYNW0226(hisB) SYNW0509(hisB)
            SYC: syc1379_d(hisB) syc1757_c(hisB)
            SYF: Synpcc7942_0125 Synpcc7942_2346
            SYD: Syncc9605_0220 Syncc9605_2174
            SYE: Syncc9902_0247 Syncc9902_0501
            SYG: sync_0260(hisB) sync_2288
            SYR: SynRCC307_2290(hisB)
            SYX: SynWH7803_0269(hisB)
            CYA: CYA_2626(hisB)
            CYB: CYB_0671(hisB)
            TEL: tll0133(hisB) tll0300
            GVI: gll0769(hisB)
            ANA: all4390(hisB) alr0073(hisB)
            AVA: Ava_1448 Ava_3285
            PMA: Pro0313(hisB) Pro1594(gph)
            PMM: PMM0281(hisB) PMM1526(hisB)
            PMT: PMT1455(hisB) PMT1880(hisB)
            PMN: PMN2A_0531 PMN2A_1647
            PMI: PMT9312_0283 PMT9312_1618
            PMB: A9601_03041 A9601_17301
            PMC: P9515_03141 P9515_17051
            PMF: P9303_04971 P9303_25121
            PMG: P9301_03051 P9301_17181
            PME: NATL1_03611 NATL1_12741
            TER: Tery_2028
            BTH: BT_0203(hisB)
            BFR: BF3187(hisB)
            BFS: BF3027(hisB)
            SRU: SRU_1559(hisB)
            FPS: FP0957(hisB)
            CTE: CT0735(hisB)
            CCH: Cag_1533(hisF)
            CPH: Cpha266_0929
            PVI: Cvib_1111
            PLT: Plut_0718(hisF)
            DET: DET0842(hisB)
            DEH: cbdb_A824(hisB)
            DEB: DehaBAV1_0761
            RRS: RoseRS_1120
            RCA: Rcas_3958
            DRA: DR_0424
            DGE: Dgeo_0979
            TTH: TTC0061
            TTJ: TTHA0429
            AAE: aq_039(hisB)
            TMA: TM1039
            TPT: Tpet_1711
            MMP: MMP0548(hisB)
            MMQ: MmarC5_1059
            MMZ: MmarC7_1567
            MAE: Maeo_0141
            MVN: Mevan_0002
            MAC: MA0219(hisB)
            MBA: Mbar_A1310
            MMA: MM_1505
            MTP: Mthe_1585
            MHU: Mhun_0920
            MEM: Memar_0835
            MBN: Mboo_1067
            MST: Msp_0164(hisB)
            MSI: Msm_1206
            MKA: MK0855(hisB)
            AFU: AF0985(hisB)
            HAL: VNG2295G(hisB)
            HMA: rrnAC2555(hisB)
            HWA: HQ1026A(hisB)
            NPH: NP2258A(hisB)
            PTO: PTO1335
            PFU: PF1660
            TKO: TK0245
            RCI: RRC390(hisB)
            IHO: Igni_0805
            SSO: SSO0596(hisB)
            STO: ST1461
            SAI: Saci_1577(hisB)
            MSE: Msed_1945
            PAI: PAE0990
            PIS: Pisl_1217
            PCL: Pcal_0139
            PAS: Pars_0170
STRUCTURES  PDB: 1RHY  2AE8  2F1D  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.19
            ExPASy - ENZYME nomenclature database: 4.2.1.19
            ExplorEnz - The Enzyme Database: 4.2.1.19
            ERGO genome analysis and discovery system: 4.2.1.19
            BRENDA, the Enzyme Database: 4.2.1.19
            CAS: 9024-35-5
///
ENTRY       EC 4.2.1.20                 Enzyme
NAME        tryptophan synthase;
            L-tryptophan synthetase;
            indoleglycerol phosphate aldolase;
            tryptophan desmolase;
            tryptophan synthetase;
            L-serine hydro-lyase (adding indoleglycerol-phosphate)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     L-serine hydro-lyase [adding 1-C-(indol-3-yl)glycerol 3-phosphate;
            L-tryptophan and glyceraldehyde-3-phosphate-forming]
REACTION    L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan +
            glyceraldehyde 3-phosphate + H2O [RN:R02722]
ALL_REAC    R02722;
            (other) R00674 R02340
SUBSTRATE   L-serine [CPD:C00065];
            1-C-(indol-3-yl)glycerol 3-phosphate [CPD:C03506]
PRODUCT     L-tryptophan [CPD:C00078];
            glyceraldehyde 3-phosphate;
            H2O [CPD:C00001]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
INHIBITOR   1-(Indol-3-yl)propanol 3-phosphate [CPD:C04229]
COMMENT     A pyridoxal-phosphate protein. The alpha-subunit catalyses the
            conversion of 1-C-(indol-3-yl)glycerol 3-phosphate to indole and
            glyceraldehyde 3-phosphate. The indole then migrates to the
            beta-subunit where, with serine in the presence of pyridoxal
            5'-phosphate, it is converted into tryptophan. Also catalyses the
            conversion of serine and indole into tryptophan and water, and of
            1-C-(indol-3-yl)glycerol 3-phosphate into indole and glyceraldehyde
            phosphate (the latter reaction was listed formerly as EC 4.1.2.8).
            In some organisms, this enzyme is part of a multifunctional protein,
            together with one or more other components of the system for the
            biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate
            phosphoribosyltransferase ), EC 4.1.1.48
            (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate
            synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)].
REFERENCE   1  [PMID:16590328]
  AUTHORS   Crawford IP, Yanofsky C.
  TITLE     ON THE SEPARATION OF THE TRYPTOPHAN SYNTHETASE OF ESCHERICHIA COLI
            INTO TWO PROTEIN COMPONENTS.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 44 (1958) 1161-70.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Creighton, T.E. and Yanofsky, C.
  TITLE     Chorismate to tryptophan (Escherichia coli) - Anthranilate
            synthetase, PR transferase, PRA isomerase, InGP synthetase,
            tryptophan synthetase.
  JOURNAL   Methods Enzymol. 17A (1970) 365-380.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:16526091]
  AUTHORS   Kung CC, Huang WN, Huang YC, Yeh KC.
  TITLE     Proteomic survey of copper-binding proteins in Arabidopsis roots by
            immobilized metal affinity chromatography and mass spectrometry.
  JOURNAL   Proteomics. 6 (2006) 2746-58.
REFERENCE   4  [PMID:3053720]
  AUTHORS   Hyde CC, Ahmed SA, Padlan EA, Miles EW, Davies DR.
  TITLE     Three-dimensional structure of the tryptophan synthase alpha 2 beta
            2 multienzyme complex from Salmonella typhimurium.
  JOURNAL   J. Biol. Chem. 263 (1988) 17857-71.
  ORGANISM  Salmonella typhimurium
REFERENCE   5  [PMID:10353823]
  AUTHORS   Woehl E, Dunn MF.
  TITLE     Mechanisms of monovalent cation action in enzyme catalysis: the
            tryptophan synthase alpha-, beta-, and alpha beta-reactions.
  JOURNAL   Biochemistry. 38 (1999) 7131-41.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
            PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K01694  tryptophan synthase
            KO: K01695  tryptophan synthase alpha chain
            KO: K01696  tryptophan synthase beta chain
            KO: K06001  tryptophan synthase beta chain
GENES       ATH: AT4G02610 AT4G27070(TSB2) AT5G38530 AT5G54810(TSB1)
            OSA: 4334425 4334427 4334428 4342571 4344612
            CME: CMJ191C
            SCE: YGL026C(TRP5)
            AGO: AGOS_AFR485C
            PIC: PICST_69669(TRP5)
            CAL: CaO19.4718(trp5)
            CGR: CAGL0A01430g
            SPO: SPAC19A8.15
            ANI: AN6231.2
            AFM: AFUA_2G13250 AFUA_6G13520
            AOR: AO090005001315 AO090010000231 AO090026000284
            CNE: CNA06290
            CPV: cgd5_4560
            CHO: Chro.50503
            ECO: b1260(trpA) b1261(trpB)
            ECJ: JW1252(trpA) JW1253(trpB)
            ECE: Z2550(trpB) Z2551(trpA)
            ECS: ECs1832 ECs1833
            ECC: c1725(trpA) c1726(trpB)
            ECI: UTI89_C1529(trpA) UTI89_C1530(trpB)
            ECP: ECP_1308 ECP_1309
            ECV: APECO1_421(trpA) APECO1_422(trpB)
            ECW: EcE24377A_1459(trpA) EcE24377A_1460(trpB)
            ECX: EcHS_A1369(trpA) EcHS_A1370(trpB)
            STY: STY1324(trpA) STY1325(trpB)
            STT: t1638(trpB) t1639(trpA)
            SPT: SPA1150(trpA) SPA1151(trpB)
            SEC: SC1722(trpB) SC1723(trpA)
            STM: STM1726(trpB) STM1727(trpA)
            YPE: YPO2203(trpA) YPO2204(trpB)
            YPK: y2047(trpA) y2048(trpB)
            YPM: YP_2001(trpA) YP_2002(trpB)
            YPA: YPA_1563 YPA_1564
            YPN: YPN_1672 YPN_1673
            YPP: YPDSF_0929 YPDSF_0930
            YPS: YPTB2125(trpA) YPTB2126(trpB)
            YPI: YpsIP31758_1936(trpB) YpsIP31758_1937(trpA)
            SFL: SF1263(trpA) SF1264(trpB)
            SFX: S1349(trpA) S1350(trpB)
            SFV: SFV_1274(trpA) SFV_1275(trpB)
            SSN: SSON_1882(trpB) SSON_1883(trpA)
            SBO: SBO_1805(trpB) SBO_1806(trpA)
            SDY: SDY_1328(trpA) SDY_1329(trpB)
            ECA: ECA2300(trpB) ECA2301(trpA)
            PLU: plu2466(trpB) plu2467(trpA)
            BUC: BU277(trpA) BU278(trpB)
            BAS: BUsg266(trpA) BUsg267(trpB)
            BAB: bbp257(trpA) bbp258(trpB)
            SGL: SG1397 SG1398
            ENT: Ent638_2207 Ent638_2208
            KPN: KPN_01254(trpB)
            SPE: Spro_2672
            BFL: Bfl430(trpB) Bfl431(trpA)
            BPN: BPEN_442(trpB) BPEN_443(trpA)
            HIN: HI1431(trpB) HI1432(trpA)
            HIT: NTHI1701(trpA) NTHI1702(trpB)
            HIP: CGSHiEE_04745
            HIQ: CGSHiGG_01030
            PMU: PM0577(trpA) PM0578(trpB)
            MSU: MS1153(trpB) MS1154(trpA)
            APL: APL_0469(trpB) APL_0470(trpA)
            ASU: Asuc_1479
            XFA: XF1375 XF1376
            XFT: PD0612(trpB) PD0613(trpA)
            XCC: XCC2541(trpA) XCC2543(trpB)
            XCB: XC_1575 XC_1577
            XCV: XCV2865(trpA) XCV2869(trpB)
            XAC: XAC2716(trpA) XAC2717(trpB)
            XOO: XOO3251(trpA) XOO3252(trpB)
            XOM: XOO_3079(XOO3079) XOO_3080(XOO3080)
            VCH: VC1169 VC1170
            VCO: VC0395_A0791(trpA) VC0395_A0792(trpB)
            VVU: VV1_3068 VV1_3069
            VVY: VV1216 VV1217
            VPA: VP1960 VP1961 VPA0585
            VFI: VF1027 VF1028
            PPR: PBPRA2490 PBPRA2491
            PAE: PA0035(tr) PA0036(trpB)
            PAU: PA14_00440(trpA) PA14_00450(trpB)
            PAP: PSPA7_0037(trpA) PSPA7_0038(trpB)
            PPU: PP_0082(trpA) PP_0083(trpB)
            PPF: Pput_0097
            PST: PSPTO_0158(trpB) PSPTO_0159(trpA)
            PSB: Psyr_0033 Psyr_0034
            PSP: PSPPH_0035(trpA) PSPPH_0036(trpB)
            PFL: PFL_0036(trpA) PFL_0037(trpB)
            PFO: Pfl_0103 Pfl_0104
            PEN: PSEEN0037(trpA) PSEEN0038(trpB)
            PMY: Pmen_0070
            PAR: Psyc_0432(trpB) Psyc_0433(trpA)
            PCR: Pcryo_0198 Pcryo_0467 Pcryo_0468
            PRW: PsycPRwf_0756 PsycPRwf_1460
            ACI: ACIAD0636(trpB) ACIAD0642(trpA)
            SON: SO_3023(trpB) SO_3024(trpA)
            SDN: Sden_2454 Sden_2455
            SFR: Sfri_1424 Sfri_1425
            SAZ: Sama_2134
            SBL: Sbal_2705 Sbal_2706
            SBM: Shew185_2727
            SLO: Shew_2255 Shew_2256
            SPC: Sputcn32_2408
            SSE: Ssed_1681
            SPL: Spea_1585
            SHE: Shewmr4_1457 Shewmr4_1458
            SHM: Shewmr7_1523 Shewmr7_1524
            SHN: Shewana3_1515 Shewana3_1516 Shewana3_2682
            SHW: Sputw3181_1600
            ILO: IL1755(trpB) IL1756(trpA)
            CPS: CPS_1954(trpB1) CPS_3526(trpB2) CPS_3527(trpA)
            PHA: PSHAa1288(trpA) PSHAa1289(trpB)
            PAT: Patl_2833 Patl_2834
            SDE: Sde_2078 Sde_2079
            PIN: Ping_1055
            MAQ: Maqu_1557 Maqu_1558 Maqu_3063
            CBU: CBU_1156(trpA)
            CBD: COXBU7E912_1253(trpBF) COXBU7E912_1255(trpA)
            LPN: lpg1304 lpg1305(trpA)
            LPF: lpl1267(trpB) lpl1268(trpA)
            LPP: lpp1268(trpB) lpp1269(trpA)
            MCA: MCA2494(trpA) MCA2495(trpB)
            FTU: FTT1772c(trpA) FTT1773c(trpB)
            FTF: FTF1772c(trpA) FTF1773c(trpB)
            FTW: FTW_0012(trpB) FTW_0013(trpA)
            FTL: FTL_0098 FTL_0099
            FTH: FTH_0092(trpA) FTH_0093(trpB)
            FTA: FTA_0106(trpA) FTA_0107(trpB)
            FTN: FTN_1739(trpB) FTN_1740(trpA)
            TCX: Tcr_0803 Tcr_0804 Tcr_1989
            NOC: Noc_1020 Noc_1021
            AEH: Mlg_0327 Mlg_1236 Mlg_1237
            HHA: Hhal_1642 Hhal_1803
            HCH: HCH_02436(trpB1) HCH_02437(trpA1) HCH_06958(trpB2)
                 HCH_06959(trpA2)
            CSA: Csal_1261 Csal_1262
            ABO: ABO_1460(trpA) ABO_1461(trpB)
            MMW: Mmwyl1_1661 Mmwyl1_2043
            AHA: AHA_2927(trpB) AHA_2928(trpA)
            RMA: Rmag_1025
            VOK: COSY_0927(trpA) COSY_0933(trpB)
            NME: NMB0678 NMB0699
            NMA: NMA0879(trpA) NMA0904(trpB)
            NMC: NMC0628(trpA) NMC0650(trpB)
            NGO: NGO0248(trpA) NGO0274(trpB)
            CVI: CV_2761(trpA) CV_2762(trpB)
            RSO: RSc1981(trpA) RSc1983(trpB)
            REU: Reut_A2304 Reut_A2306
            REH: H16_A2612(trpA) H16_A2614(trpB)
            RME: Rmet_2465 Rmet_2467
            BMA: BMAA1719(trpA) BMAA1721(trpB)
            BMV: BMASAVP1_1649(trpB) BMASAVP1_1651(trpA)
            BML: BMA10299_1858(trpB) BMA10299_1860(trpA)
            BMN: BMA10247_A0529(trpB) BMA10247_A0531(trpA)
            BXE: Bxe_B2879 Bxe_B2881
            BVI: Bcep1808_4464
            BUR: Bcep18194_B2123 Bcep18194_B2125
            BCN: Bcen_4407 Bcen_4409
            BCH: Bcen2424_3958 Bcen2424_3960
            BAM: Bamb_3348 Bamb_3350
            BPS: BPSS1697(trpA) BPSS1699(trpB)
            BPM: BURPS1710b_A0767(trpA) BURPS1710b_A0769(trpB)
            BPL: BURPS1106A_A2305(trpA) BURPS1106A_A2307(trpB)
            BPD: BURPS668_A2443(trpA) BURPS668_A2445(trpB)
            BTE: BTH_II0679(trpB) BTH_II0681(trpA)
            PNU: Pnuc_0773
            BPE: BP3589(trpB) BP3590(trpA)
            BPA: BPP3322(trpA) BPP3323(trpB)
            BBR: BB3773(trpA) BB3774(trpB)
            RFR: Rfer_1328 Rfer_1787 Rfer_1788
            POL: Bpro_3616 Bpro_3617
            PNA: Pnap_3047
            AAV: Aave_1214
            AJS: Ajs_2001 Ajs_3240
            VEI: Veis_1286 Veis_4867
            MPT: Mpe_A2156 Mpe_A2157
            HAR: HEAR1223(trpB) HEAR1224(trpA)
            MMS: mma_2163(trpA) mma_2164(trpB)
            NEU: NE0693(trpB) NE0694(trpA)
            NET: Neut_1152 Neut_1153
            NMU: Nmul_A1911 Nmul_A1912
            EBA: ebA4109 ebA4775(trpB) ebA4776(trpA)
            AZO: azo1047(trpB)
            DAR: Daro_0870 Daro_0871 Daro_3711
            TBD: Tbd_1773 Tbd_1913 Tbd_1914
            MFA: Mfla_1697 Mfla_1698
            HPY: HP1277(trpA) HP1278(trpB)
            HPJ: jhp1198(trpA) jhp1199(trpB)
            HPA: HPAG1_1234 HPAG1_1235
            HHE: HH1414(trpA) HH1415(trpB)
            HAC: Hac_0013(trpA) Hac_0014(trpB)
            WSU: WS0719(trpB) WS1351 WS1827(trpA)
            TDN: Tmden_0742 Tmden_1119 Tmden_1681
            CJE: Cj0348(trpB) Cj0349(trpA)
            CJR: CJE0397(trpB) CJE0398(trpA)
            CJJ: CJJ81176_0372(trpB) CJJ81176_0373(trpA)
            CJU: C8J_0325(trpB) C8J_0326(trpA)
            CJD: JJD26997_1610(trpA) JJD26997_1611(trpB)
            CFF: CFF8240_0353(trpB) CFF8240_0354(trpA)
            CCV: CCV52592_1686(trpB) CCV52592_1687(trpA)
            CHA: CHAB381_1274(trpB) CHAB381_1275(trpA)
            CCO: CCC13826_0972(trpB) CCC13826_0973(trpA)
            ABU: Abu_0700(trpB1) Abu_1295(trpB2) Abu_1773(trpA)
            NIS: NIS_0374(trpA) NIS_0706(trpB)
            SUN: SUN_0653 SUN_1813 SUN_2098(trpA)
            GSU: GSU2371(trpA) GSU2379
            GME: Gmet_2477 Gmet_2482 Gmet_2493
            GUR: Gura_3280 Gura_3288
            PCA: Pcar_1244 Pcar_2240 Pcar_2241
            PPD: Ppro_1162
            DVU: DVU0085(trpB-1) DVU0470(trpB-2) DVU0471(trpA)
            DVL: Dvul_2466 Dvul_2876
            DDE: Dde_0079 Dde_3478 Dde_3479
            LIP: LI0410(trpA) LI0411(trpB)
            DPS: DP1630 DP1631 DP2949
            ADE: Adeh_3748 Adeh_4057 Adeh_4058
            AFW: Anae109_0370
            MXA: MXAN_6065(trpB) MXAN_6066(trpA)
            SAT: SYN_01941 SYN_01942 SYN_01988
            SFU: Sfum_1770 Sfum_1771 Sfum_2404
            PUB: SAR11_0487(trpA) SAR11_0488(trpB)
            MLO: mlr5071 mlr5073
            MES: Meso_0664 Meso_0666
            PLA: Plav_0142
            SME: SMc02765(trpA) SMc02766(trpB)
            SMD: Smed_3238
            ATU: Atu0018(trpB) Atu0019(trpA)
            ATC: AGR_C_28 AGR_C_30
            RET: RHE_CH00021(trpB) RHE_CH00022(trpA)
            RLE: RL0021(trpB) RL0022(trpA)
            BME: BMEI2018 BMEI2019
            BMF: BAB1_2110(trpA) BAB1_2112
            BMS: BR2108(trpA) BR2110(trpB)
            BMB: BruAb1_2083(trpA) BruAb1_2085(trpB)
            BOV: BOV_2024(trpA) BOV_2026(trpB)
            OAN: Oant_0812
            BJA: blr0745(trpB) blr0746(trpA)
            BRA: BRADO0090(trpA) BRADO0091(trpB)
            BBT: BBta_0096(trpA) BBta_0097(trpB)
            RPA: RPA0069(trpB) RPA0070(trpA) RPA1594(trpB-1) RPA1596
            RPB: RPB_0634 RPB_0635 RPB_3714
            RPC: RPC_0391 RPC_0392 RPC_0699
            RPD: RPD_0197 RPD_0198 RPD_1751
            RPE: RPE_0454 RPE_0455 RPE_0770
            NWI: Nwi_0054(trpA) Nwi_0055
            NHA: Nham_0062 Nham_0063
            XAU: Xaut_1695
            CCR: CC_3543 CC_3544
            SIL: SPO0808(trpB) SPO0815(trpA)
            SIT: TM1040_0206 TM1040_0222
            RSP: RSP_0831(trpA) RSP_1513(trpB) RSP_3585
            RSH: Rsph17029_0165 Rsph17029_2489
            RSQ: Rsph17025_0349 Rsph17025_2965 Rsph17025_3885
            JAN: Jann_3584 Jann_3589
            RDE: RD1_3895(trpA) RD1_3906(trpB)
            PDE: Pden_0333
            MMR: Mmar10_0090 Mmar10_0093
            HNE: HNE_3474(trpA) HNE_3476(trpB)
            ZMO: ZMO0584(trpA) ZMO0585(trpB)
            NAR: Saro_1301 Saro_1302
            SAL: Sala_1063 Sala_1064
            SWI: Swit_2727
            ELI: ELI_07590 ELI_07595
            GOX: GOX1201 GOX1202
            GBE: GbCGDNIH1_2014 GbCGDNIH1_2015
            ACR: Acry_1329
            RRU: Rru_A1979 Rru_A3427 Rru_A3428
            MAG: amb1787 amb4010 amb4011
            MGM: Mmc1_0337 Mmc1_0338 Mmc1_0346
            ABA: Acid345_1158 Acid345_1160
            SUS: Acid_7887 Acid_7888
            BSU: BG10290(trpB) BG10291(trpA)
            BHA: BH1663(trpB) BH1664(trpA)
            BAN: BA1253(trpB) BA1254(trpA)
            BAR: GBAA1253(trpB) GBAA1254(trpA)
            BAA: BA_1786 BA_1787
            BAT: BAS1161 BAS1162
            BCE: BC1237 BC1238
            BCA: BCE_1361(trpB) BCE_1362(trpA)
            BCZ: BCZK1135(trpB) BCZK1136(trpA)
            BTK: BT9727_1141(trpB) BT9727_1142(trpA)
            BLI: BL02770(trpA) BL02771(trpB)
            BLD: BLi02398(trpA) BLi02399(trpB)
            BCL: ABC1899(trpB) ABC1900(trpA)
            BAY: RBAM_020800(trpB)
            BPU: BPUM_1994(trpA) BPUM_1995(trpB)
            OIH: OB0521 OB0522
            GKA: GK2102 GK2199(trpA) GK2200(trpB)
            SAU: SA1204(trpB) SA1205(trpA)
            SAV: SAV1372(trpB) SAV1373(trpA)
            SAM: MW1259(trpB) MW1260(trpA)
            SAR: SAR1385(trpB) SAR1386(trpA)
            SAS: SAS1312 SAS1313
            SAC: SACOL1408(trpB) SACOL1409(trpA)
            SAB: SAB1227(trpB) SAB1228(trpA)
            SAA: SAUSA300_1267(trpB) SAUSA300_1268(trpA)
            SAO: SAOUHSC_01371 SAOUHSC_01372
            SAJ: SaurJH9_1433 SaurJH9_1434
            SAH: SaurJH1_1462 SaurJH1_1463
            SEP: SE1053 SE1054
            SER: SERP0942(trpB) SERP0943(trpA)
            SHA: SH1536(trpA) SH1537(trpB)
            SSP: SSP1373 SSP1374
            LMO: lmo1627(trpA) lmo1628(trpB)
            LMF: LMOf2365_1649(trpA) LMOf2365_1650(trpB)
            LIN: lin1668(trpA) lin1669(trpB)
            LWE: lwe1643(trpA) lwe1644(trpB)
            LLA: L0048(trpA) L0049(trpB)
            LLC: LACR_1548 LACR_1549
            LLM: llmg_1041(trpB) llmg_1042(trpA)
            SPN: SP_1811 SP_1812
            SPR: spr1631(trpA) spr1632(trpB)
            SPD: SPD_1596(trpA) SPD_1597(trpB)
            SMU: SMU.537(trpB) SMU.538(trpA)
            STC: str1587(trpA) str1588(trpB)
            STL: stu1587(trpA)
            SSA: SSA_0631(trpB2) SSA_0637(trpB) SSA_0638(trpA)
            SGO: SGO_0424(trpA-1) SGO_0656(trpB-2) SGO_0662(trpB-1)
                 SGO_0663(trpA-2)
            LPL: lp_1657(trpA) lp_1658(trpB)
            LCA: LSEI_0074 LSEI_0075
            STH: STH1414 STH1415
            CAC: CAC3157(trpA) CAC3158(trpB)
            CNO: NT01CX_1342(trpB)
            CTH: Cthe_1411
            CBE: Cbei_1755
            CKL: CKL_1279(trpB1) CKL_1280(trpA) CKL_3062(trpB2)
            AMT: Amet_1082 Amet_1083
            CHY: CHY_0751 CHY_1581(trpA) CHY_1582(trpB)
            DSY: DSY3200 DSY3201 DSY4462
            DRM: Dred_0253 Dred_0254
            SWO: Swol_0361 Swol_0362 Swol_0644
            CSC: Csac_2230
            TTE: TTE1577(trpA) TTE1578(trpB)
            MTA: Moth_1336 Moth_1337
            MTU: Rv1612(trpB) Rv1613(trpA)
            MTC: MT1647(trpB) MT1648(trpA)
            MBO: Mb1638(trpB) Mb1639(trpA)
            MBB: BCG_1650(trpB) BCG_1651(trpA)
            MLE: ML1272(trpB) ML1273(trpA)
            MPA: MAP1306(trpB) MAP1307(trpA)
            MAV: MAV_3173(trpA) MAV_3174(trpB)
            MSM: MSMEG_3220(trpB) MSMEG_3221(trpA)
            MVA: Mvan_2818 Mvan_2923
            MGI: Mflv_3175 Mflv_3598
            MMC: Mmcs_2591 Mmcs_3049 Mmcs_3050
            MKM: Mkms_2635 Mkms_3108
            MJL: Mjls_2628 Mjls_3065
            CGL: NCgl2931(cgl3034) NCgl2932(trpA)
            CGB: cg3363(trpB) cg3364(trpA)
            CEF: CE2872(trpB) CE2873(trpA) CE2880
            CDI: DIP2351(trpB1) DIP2360(trpB2) DIP2361(trpA)
            CJK: jk0798(trpB) jk0799(trpA)
            NFA: nfa18610(trpB) nfa18620(trpA)
            RHA: RHA1_ro01012(trpA) RHA1_ro01013(trpB1) RHA1_ro04524(trpB2)
            SCO: SCO2036(SC4G6.05c) SCO2037(SC4G6.06c)
            SMA: SAV6177(trpB) SAV6178(trpA)
            LXX: Lxx11290(trpB) Lxx11300(trpA)
            ART: Arth_1688 Arth_1689
            AAU: AAur_1839(trpB) AAur_1840(trpA)
            PAC: PPA1131 PPA1132
            NCA: Noca_3025 Noca_3949
            TFU: Tfu_1165 Tfu_1166
            FRA: Francci3_3015 Francci3_3016
            FAL: FRAAL4681(trpB) FRAAL4682(trpA) FRAAL4967(trpA)
                 FRAAL4968(trpB)
            ACE: Acel_1075
            KRA: Krad_2964 Krad_2965
            SEN: SACE_5748(trpA) SACE_5749(trpB)
            STP: Strop_0678 Strop_3170 Strop_3171
            BLO: BL0755(trpA)
            BAD: BAD_0791(trpA)
            RXY: Rxyl_0305 Rxyl_2089 Rxyl_2090
            FNU: FN0317
            RBA: RB10650(trpB) RB5560(trpA)
            CTR: CT170(trpB) CT171(trpA)
            CTA: CTA_0184(trpB_2) CTA_0185(trpB_1) CTA_0186(trpA)
            CCA: CCA00559(trpB-1) CCA00566(trpB-2) CCA00567(trpA)
            CFE: CF0435(trpA) CF0436(trpB1)
            LIL: LA3288(trpA) LA3289(trpB)
            LIC: LIC10859(trpB1) LIC10860(trpA)
            LBJ: LBJ_0913(trpB) LBJ_0914(trpA)
            LBL: LBL_0928(trpB) LBL_0929(trpA)
            SYN: slr0543(trpB) slr0966(trpA)
            SYW: SYNW1519(trpA) SYNW2280(trpB)
            SYC: syc1106_d(trpA) syc1948_c(trpB)
            SYF: Synpcc7942_0411 Synpcc7942_2143
            SYD: Syncc9605_0990(trpA) Syncc9605_2418
            SYE: Syncc9902_0896(trpA) Syncc9902_2098
            SYG: sync_1910(trpA) sync_2633(trpB)
            SYR: SynRCC307_1600(trpA) SynRCC307_2271(trpB)
            SYX: SynWH7803_0732(trpA) SynWH7803_2299(trpB)
            CYA: CYA_0223(trpA-1) CYA_0339(trpB) CYA_1290(trpA-2)
            CYB: CYB_0937(trpA) CYB_1508(trpB)
            TEL: tll0439(trpA) tll2475(trpB)
            GVI: gll2612(trpA) glr2758(trpB)
            ANA: all0410(trpB) all0411(trpA) all3794(trpB) alr4811(trpA)
            AVA: Ava_1911 Ava_2082(trpA)
            PMA: Pro0188(trpB) Pro0574(trpA)
            PMM: PMM0164(trpB) PMM0572(trpA)
            PMT: PMT0465(trpA) PMT2027(trpB)
            PMN: PMN2A_0008 PMN2A_1531
            PMI: PMT9312_0166 PMT9312_0572
            PMB: A9601_01821(trpB) A9601_06281(trpA)
            PMC: P9515_01931(trpB) P9515_06371(trpA)
            PMF: P9303_18161(trpA) P9303_27051(trpB)
            PMG: P9301_01841(trpB) P9301_05981(trpA)
            PMH: P9215_01821(trpB) P9215_06541(trpA)
            PME: NATL1_02381(trpB) NATL1_06271(trpA)
            TER: Tery_0581 Tery_4493
            BTH: BT_0527 BT_0533 BT_4664
            BFR: BF1242 BF2650 BF2656
            BFS: BF1192(trpB) BF2672(trpB) BF2678(trpA)
            SRU: SRU_1669(trpB) SRU_1670(trpA)
            CHU: CHU_3296(trpB) CHU_3297(trpA)
            GFO: GFO_2673(trpB) GFO_2674(trpA)
            FJO: Fjoh_4899
            FPS: FP0507(trpA) FP0508(trpB)
            CTE: CT0192(trpB-2) CT0521(trpB-1) CT0535(trpA)
            CCH: Cag_0451 Cag_1297 Cag_1315
            CPH: Cpha266_0335 Cpha266_1933
            PVI: Cvib_0589 Cvib_1577
            PLT: Plut_0535 Plut_0545 Plut_1929
            DET: DET1035 DET1487(trpB) DET1488(trpA)
            DEH: cbdb_A1008 cbdb_A1450(trpB) cbdb_A1451(trpA)
            DEB: DehaBAV1_1278
            RRS: RoseRS_2950
            RCA: Rcas_1948
            DRA: DR_0941 DR_0942
            DGE: Dgeo_1024 Dgeo_1025
            TTH: TTC0729 TTC0730
            TTJ: TTHA1094 TTHA1095
            AAE: aq_1410(trpB2) aq_1548(trpA) aq_706(trpB1)
            TMA: TM0137 TM0138 TM0539
            TPT: Tpet_0788
            MJA: MJ1037(trpB) MJ1038(trpA)
            MMP: MMP1002(trpA) MMP1003(trpB)
            MMQ: MmarC5_0591 MmarC5_0592
            MMZ: MmarC7_0244
            MAE: Maeo_1122
            MVN: Mevan_0327
            MAC: MA2990(trpA) MA2991(trpB) MA3198(trpB)
            MBA: Mbar_A3503 Mbar_A3622 Mbar_A3623
            MMA: MM_0337 MM_2821 MM_2822
            MBU: Mbur_0108 Mbur_0109 Mbur_1100
            MTP: Mthe_0192 Mthe_0193
            MHU: Mhun_0558 Mhun_1790 Mhun_1791
            MLA: Mlab_0933
            MEM: Memar_0070 Memar_0077
            MBN: Mboo_0063 Mboo_0222
            MTH: MTH1476 MTH1659(trpB) MTH1660(trpA)
            MST: Msp_1074(trpB) Msp_1075(trpA)
            MSI: Msm_1141 Msm_1142 Msm_1242
            MKA: MK0403(trpA) MK0784(trpB)
            AFU: AF1240(trpB-1) AF1599(trpA) AF1600(trpB-2)
            HAL: VNG0307G(trpB) VNG0308Gm(trpA)
            HMA: rrnAC1884(trpA) rrnAC1885(trpB)
            HWA: HQ1157A(trpA) HQ1158A(trpB)
            NPH: NP3162A(trpA) NP3164A(trpB_1) NP3502A(trpB_2)
            TAC: Ta0669 Ta0803m
            TVO: TVN0931 TVN1027
            PTO: PTO0141 PTO0345 PTO0346
            PHO: PH1583
            PAB: PAB1970(trpB-2) PAB2048(trpB-1) PAB2049(trpA)
            PFU: PF1592 PF1705 PF1706
            TKO: TK0257 TK0258 TK1442
            RCI: RCIX793(trpA) RCIX794(trpB)
            APE: APE_2316 APE_2548 APE_2550
            SMR: Smar_0098
            IHO: Igni_0431
            SSO: SSO0888(trpB) SSO0889(trpA) SSO1145(trpB-like)
            STO: ST1232 ST1233 ST1567
            SAI: Saci_1421(trpB1) Saci_1422
            MSE: Msed_1690
            PAI: PAE0257 PAE2458 PAE2462
            PCL: Pcal_1211
            PAS: Pars_1422
STRUCTURES  PDB: 1A50  1A5A  1A5B  1A5S  1BEU  1BKS  1C29  1C8V  1C9D  1CW2  
                 1CX9  1FUY  1GEQ  1K3U  1K7E  1K7F  1K7X  1K8X  1K8Y  1K8Z  
                 1KFC  1KFJ  1KFK  1QOP  1QOQ  1RD5  1TJP  1TJR  1TTP  1TTQ  
                 1UBS  1UJP  1V7Y  1V8Z  1WBJ  1WDW  1WQ5  1WXJ  1X1Q  1XC4  
                 1XCF  2CLE  2CLF  2CLH  2CLI  2CLK  2CLL  2CLM  2CLO  2DH5  
                 2DH6  2DZP  2DZS  2DZT  2DZU  2DZV  2DZW  2DZX  2E09  2EKC  
                 2J9X  2TRS  2TSY  2TYS  2WSY  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.20
            ExPASy - ENZYME nomenclature database: 4.2.1.20
            ExplorEnz - The Enzyme Database: 4.2.1.20
            ERGO genome analysis and discovery system: 4.2.1.20
            BRENDA, the Enzyme Database: 4.2.1.20
            CAS: 9014-52-2
///
ENTRY       EC 4.2.1.21       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
COMMENT     Deleted entry: cystathionine beta-synthase. Now EC 4.2.1.22
            cystathionine beta-synthase (EC 4.2.1.21 created 1961, deleted 1964)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.21
            ExPASy - ENZYME nomenclature database: 4.2.1.21
            ExplorEnz - The Enzyme Database: 4.2.1.21
            ERGO genome analysis and discovery system: 4.2.1.21
            BRENDA, the Enzyme Database: 4.2.1.21
///
ENTRY       EC 4.2.1.22                 Enzyme
NAME        cystathionine beta-synthase;
            serine sulfhydrase;
            beta-thionase;
            methylcysteine synthase;
            cysteine synthase;
            serine sulfhydrylase;
            L-serine hydro-lyase (adding homocysteine)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     L-serine hydro-lyase (adding homocysteine; L-cystathionine-forming)
REACTION    L-serine + L-homocysteine = L-cystathionine + H2O [RN:R01290]
ALL_REAC    R01290;
            (other) R00891 R01289 R04942
SUBSTRATE   L-serine [CPD:C00065];
            L-homocysteine [CPD:C00155]
PRODUCT     L-cystathionine [CPD:C02291];
            H2O [CPD:C00001]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. A multifunctional enzyme: catalyses
            beta-replacement reactions between L-serine, L-cysteine, cysteine
            thioethers, or some other beta-substituted alpha-L-amino acids, and
            a variety of mercaptans.
REFERENCE   1  [PMID:5121611]
  AUTHORS   Braunstein AE, Goryachenkova EV, Tolosa EA, Willhardt IH, Yefremova
            LL.
  TITLE     Specificity and some other properties of liver serine sulphhydrase:
            evidence for its identity with cystathionine  -synthase.
  JOURNAL   Biochim. Biophys. Acta. 242 (1971) 247-60.
  ORGANISM  chicken [GN:gga]
REFERENCE   2  [PMID:5672136]
  AUTHORS   Nakagawa H, Kimura H.
  TITLE     Purification and properties of cystathionine synthetase synthetase
            from rat liver: separation of cystathionine synthetase from serine
            dehydratase.
  JOURNAL   Biochem. Biophys. Res. Commun. 32 (1968) 209-14.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:13991884]
  AUTHORS   SCHLOSSMANN K, BRUEGGEMANN J, LYNEN F.
  TITLE     [Biosynthesis of cysteine. I. Detection and isolation of serine
            sulfhydrase from baker's yeast.]
  JOURNAL   Biochem. Z. 336 (1962) 258-73.
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00271  Methionine metabolism
            PATH: map00450  Selenoamino acid metabolism
            PATH: map05040  Huntington's disease
ORTHOLOGY   KO: K01697  cystathionine beta-synthase
GENES       HSA: 875(CBS)
            MMU: 12411(Cbs)
            RNO: 24250(Cbs)
            CFA: 611071(CBS)
            GGA: 418544(LOC418544) 418545(CBS)
            XLA: 380308(cbs-a) 446655(cbs-b)
            XTR: 493533(TTpA004o05.1)
            SPU: 591266(LOC591266)
            DME: Dmel_CG1753
            CEL: F54A3.4 ZC373.1
            CME: CMS037C
            SCE: YGR155W(CYS4)
            AGO: AGOS_AGR012C
            PIC: PICST_77227(CYS4)
            CAL: CaO19.7152(CYS4)
            CGR: CAGL0E03157g
            ANI: AN5820.2
            AFM: AFUA_2G07620
            AOR: AO090011000931
            CNE: CNA06170
            UMA: UM02792.1
            DDI: DDB_0191292(cysB)
            TET: TTHERM_00558300
            TBR: Tb11.02.5400
            TCR: 506905.50 508175.360 508177.110 508177.120 508241.140
                 509149.9 510381.10 511691.10 511691.20
            LMA: LmjF17.0250
            PLU: plu0524
            XFA: XF0603
            XFT: PD1548(cysM)
            XCC: XCC0597(cysB)
            XCB: XC_3636
            XCV: XCV3726
            XAC: XAC3603(cysB)
            XOO: XOO0777(cysB)
            XOM: XOO_0707(XOO0707)
            PAE: PA0399
            PAU: PA14_05220
            ILO: IL0218(cysM)
            FTU: FTT1287(cbs)
            FTF: FTF1287(cbs)
            FTL: FTL_1174
            FTH: FTH_1148(cysK)
            FTN: FTN_1302(cysK)
            CVI: CV_3395(cysB2)
            BMA: BMA1621
            BPS: BPSL2215
            BPM: BURPS1710b_2647
            BTE: BTH_I1970 BTH_II1370
            POL: Bpro_2830
            BBA: Bd3796
            ADE: Adeh_3706
            MXA: MXAN_2041
            MLO: mll4505
            RET: RHE_CH01775(cysK2)
            RPA: RPA2356
            MTU: Rv1077(cbs)
            MTC: MT1108
            MBO: Mb1106(cbs)
            MBB: BCG_1135(cbs)
            MLE: ML2396(cysM2)
            MPA: MAP1024(cysM2)
            MAV: MAV_1201
            MSM: MSMEG_5270
            CJK: jk1981(cysY)
            NFA: nfa48320
            RHA: RHA1_ro05843
            SCO: SCO3077(SCE25.18c)
            SMA: SAV3510(cysM1)
            LXX: Lxx17700(cysM2)
            CMI: CMM_0872(cysB)
            AAU: AAur_3038
            PAC: PPA1290 PPA2278
            TFU: Tfu_0438
            FRA: Francci3_0375
            FAL: FRAAL0784(cysM)
            SEN: SACE_0899(cysM2)
            BAD: BAD_0490(cbsSV)
            AVA: Ava_4156
            SRU: SRU_1123
            CTE: CT1921
            CCH: Cag_1634
            PLT: Plut_0281
            APE: APE_1223.1 APE_1586
STRUCTURES  PDB: 1JBQ  1M54  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.22
            ExPASy - ENZYME nomenclature database: 4.2.1.22
            ExplorEnz - The Enzyme Database: 4.2.1.22
            ERGO genome analysis and discovery system: 4.2.1.22
            BRENDA, the Enzyme Database: 4.2.1.22
            CAS: 9023-99-8
///
ENTRY       EC 4.2.1.23       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
COMMENT     Deleted entry: methylcysteine synthase. The reaction was due to a
            side-reaction of EC 4.2.1.22 cystathionine beta-synthase (EC
            4.2.1.23 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.23
            ExPASy - ENZYME nomenclature database: 4.2.1.23
            ExplorEnz - The Enzyme Database: 4.2.1.23
            ERGO genome analysis and discovery system: 4.2.1.23
            BRENDA, the Enzyme Database: 4.2.1.23
///
ENTRY       EC 4.2.1.24                 Enzyme
NAME        porphobilinogen synthase;
            aminolevulinate dehydratase;
            delta-aminolevulinate dehydratase;
            delta-aminolevulinic acid dehydrase;
            delta-aminolevulinic acid dehydratase;
            aminolevulinic dehydratase;
            delta-aminolevulinic dehydratase;
            5-levulinic acid dehydratase;
            5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and
            cyclizing)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and
            cyclizing; porphobilinogen-forming)
REACTION    2 5-aminolevulinate = porphobilinogen + 2 H2O [RN:R00036]
ALL_REAC    R00036
SUBSTRATE   5-aminolevulinate [CPD:C00430]
PRODUCT     porphobilinogen [CPD:C00931];
            H2O [CPD:C00001]
COFACTOR    Zinc [CPD:C00038];
            Metal [CPD:C00050]
COMMENT     The fungal enzyme is a metalloprotein.
REFERENCE   1  [PMID:13276347]
  AUTHORS   GIBSON KD, NEUBERGER A, SCOTT JJ.
  TITLE     The purification and properties of delta-aminolaevulic acid
            dehydrase.
  JOURNAL   Biochem. J. 61 (1955) 618-29.
REFERENCE   2  [PMID:5773436]
  AUTHORS   Komai H, Neilands JB.
  TITLE     The metalloprotein nature of Ustilago delta-aminolevulinate
            dehydratase.
  JOURNAL   Biochim. Biophys. Acta. 171 (1969) 311-20.
  ORGANISM  Ustilago sphaerogena
REFERENCE   3  [PMID:4998716]
  AUTHORS   Yamasaki H, Moriyama T.
  TITLE     Delta-aminolevulinic acid dehydratase of Mycobacterium phlei.
  JOURNAL   Biochim. Biophys. Acta. 227 (1971) 698-705.
  ORGANISM  Mycobacterium phlei
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K01698  porphobilinogen synthase
GENES       HSA: 210(ALAD)
            PTR: 464675(ALAD)
            MMU: 17025(Alad)
            RNO: 25374(Alad)
            CFA: 474808(ALAD)
            XLA: 444422(MGC83017) 444744(MGC84775)
            SPU: 577020(LOC577020)
            DME: Dmel_CG10335(Pbgs)
            ATH: AT1G44318(HEMB2) AT1G69740(HEMB1)
            OSA: 4341997
            CME: CMD104C
            SCE: YGL040C(HEM2)
            AGO: AGOS_AGR015C
            CGR: CAGL0D06138g
            SPO: SPAC1805.06c(hem2)
            ANI: AN1403.2
            AFM: AFUA_1G08760
            AOR: AO090005001652
            CNE: CNA03580
            UMA: UM02060.1
            PFA: PF14_0381
            TET: TTHERM_00636900
            ECO: b0369(hemB)
            ECJ: JW0361(hemB)
            ECE: Z0468(hemB)
            ECS: ECs0423
            ECC: c0477(hemB)
            ECI: UTI89_C0388(hemB)
            ECP: ECP_0432
            ECV: APECO1_1635(hemB)
            ECW: EcE24377A_0393(hemB)
            ECX: EcHS_A0433(hemB)
            STY: STY0404(hemB)
            STT: t2492(hemB)
            SPT: SPA2351(hemB)
            SEC: SC0413(hemB)
            STM: STM0372(hemB)
            YPE: YPO3771(hemB)
            YPK: y0459(hemB)
            YPM: YP_3277(hemB)
            YPA: YPA_3441
            YPN: YPN_0193
            YPP: YPDSF_3391
            YPS: YPTB0262(hemB)
            YPI: YpsIP31758_0278(hemB)
            YEN: YE0263(hemB)
            SFL: SF0249(hemB)
            SFX: S0270(hemB)
            SFV: SFV_0333(hemB)
            SSN: SSON_0347(hemB)
            SBO: SBO_0263(hemB)
            SDY: SDY_0501(hemB)
            ECA: ECA0203(hemB)
            PLU: plu4407(hemB)
            WBR: WGLp132(hemB)
            SGL: SG1529
            ENT: Ent638_0843
            SPE: Spro_0255
            HSO: HS_0548(hemB)
            PMU: PM1692(hemB)
            MSU: MS0503(hemB)
            APL: APL_1988(hemB)
            ASU: Asuc_0667
            XFA: XF2306
            XFT: PD1331(hemB)
            XCC: XCC3956(hemB)
            XCB: XC_4045
            XCV: XCV4131(hemB)
            XAC: XAC4040(hemB)
            XOO: XOO0402(hemB)
            XOM: XOO_0365(XOO0365)
            VCH: VC0105
            VCO: VC0395_A2413(hemB)
            VVU: VV1_0902
            VVY: VV0185
            VPA: VP0104
            VFI: VF0053
            PPR: PBPRA0123(hemB)
            PAE: PA5243(hemB)
            PAU: PA14_69240(hemB)
            PPU: PP_2913(hemB-1) PP_3322(hemB-2)
            PPF: Pput_2778
            PST: PSPTO_5251(hemB)
            PSB: Psyr_0292
            PSP: PSPPH_0279(hemB)
            PFL: PFL_2290(hemB) PFL_5985(hemB)
            PFO: Pfl_3751 Pfl_5465
            PEN: PSEEN5337(hemB)
            PMY: Pmen_0299
            PAR: Psyc_1578(hemB)
            PCR: Pcryo_1760
            PRW: PsycPRwf_1822
            ACI: ACIAD0923(hemB)
            SON: SO_2587(hemB-1) SO_4208(hemB-2)
            SDN: Sden_0303 Sden_0452
            SFR: Sfri_0466
            SAZ: Sama_3211
            SBL: Sbal_1858 Sbal_3904
            SBM: Shew185_0410 Shew185_1885
            SLO: Shew_3382
            SPC: Sputcn32_0497 Sputcn32_1755
            SSE: Ssed_4105
            SPL: Spea_3801
            SHE: Shewmr4_2183 Shewmr4_3560
            SHM: Shewmr7_0396 Shewmr7_2260
            SHN: Shewana3_2392 Shewana3_3734
            SHW: Sputw3181_2270 Sputw3181_3673
            ILO: IL2365(hemB)
            CPS: CPS_0169(hemB)
            PHA: PSHAa2935(hemB)
            PAT: Patl_4219
            SDE: Sde_0654
            PIN: Ping_0316
            MAQ: Maqu_3578
            CBU: CBU_1424(hemB)
            CBD: COXBU7E912_0573(hemB)
            LPN: lpg1808(hemB)
            LPF: lpl1772(hemB)
            LPP: lpp1771(hemB)
            MCA: MCA2793(hemB)
            FTU: FTT0462(hemB)
            FTF: FTF0462(hemB)
            FTW: FTW_1608(hemB)
            FTL: FTL_1602
            FTH: FTH_1548(hemB)
            FTA: FTA_1688(hemB)
            FTN: FTN_0553(hemB)
            TCX: Tcr_0154
            NOC: Noc_2574
            AEH: Mlg_2828
            HHA: Hhal_1051
            HCH: HCH_00650 HCH_01004
            CSA: Csal_3279
            ABO: ABO_2459(hemB)
            MMW: Mmwyl1_0074 Mmwyl1_3998
            AHA: AHA_0091(hemB)
            DNO: DNO_0510(hemB)
            RMA: Rmag_0409
            VOK: COSY_0378(hemB)
            NME: NMB0801
            NMA: NMA1011(hemB)
            NMC: NMC0753(hemB)
            NGO: NGO0385
            CVI: CV_1648(hemB)
            RSO: RSc2989(hemB)
            REU: Reut_A3149
            REH: H16_A3453(hemB)
            RME: Rmet_3286
            BMA: BMA2601(hemB)
            BMV: BMASAVP1_A3139(hemB)
            BML: BMA10299_A1954(hemB)
            BMN: BMA10247_3508(hemB)
            BXE: Bxe_A0344
            BVI: Bcep1808_0360
            BUR: Bcep18194_A3477
            BCN: Bcen_2729
            BCH: Bcen2424_0378
            BAM: Bamb_0297
            BPS: BPSL3183(hemB)
            BPM: BURPS1710b_3746(hemB)
            BPL: BURPS1106A_3774(hemB)
            BPD: BURPS668_3716(hemB)
            BTE: BTH_I3038(hemB)
            PNU: Pnuc_0083
            BPE: BP3648(hemB)
            BPA: BPP0063(hemB)
            BBR: BB0063(hemB)
            RFR: Rfer_3805
            POL: Bpro_0245
            PNA: Pnap_0192
            AAV: Aave_0327
            AJS: Ajs_0266
            VEI: Veis_0388
            MPT: Mpe_A0306
            HAR: HEAR3136(hemB)
            MMS: mma_3378(hemB)
            NEU: NE2457
            NET: Neut_0235
            NMU: Nmul_A2079
            EBA: ebA1071(hemB)
            AZO: azo2821(hemB)
            DAR: Daro_0626
            TBD: Tbd_0189
            MFA: Mfla_2464
            HPY: HP0163
            HPA: HPAG1_0160
            HHE: HH1606(hemB)
            HAC: Hac_0345(hemB)
            WSU: WS1821(hemB)
            TDN: Tmden_0385
            CJE: Cj0995c(hemB)
            CJR: CJE1075(hemB)
            CJJ: CJJ81176_1013(hemB)
            CJU: C8J_0932(hemB)
            CJD: JJD26997_0794(hemB)
            CFF: CFF8240_1574(hemB)
            CCV: CCV52592_1348(hemB)
            CHA: CHAB381_1698(hemB)
            CCO: CCC13826_0884(hemB)
            ABU: Abu_1238(hemB)
            NIS: NIS_0360(hemB)
            SUN: SUN_2089(hemB)
            GSU: GSU0135(hemB)
            GME: Gmet_0189
            GUR: Gura_0347
            PCA: Pcar_3061
            PPD: Ppro_0442
            DVU: DVU0856(hemB)
            DVL: Dvul_2127
            DDE: Dde_2576
            LIP: LI0205(hemB)
            BBA: Bd3444(hemB)
            DPS: DP2824
            ADE: Adeh_2452
            AFW: Anae109_1415
            MXA: MXAN_4100(hemB)
            SAT: SYN_02267
            SFU: Sfum_3057
            RPR: RP539
            RTY: RT0528(hemB)
            RCO: RC0798(hemB)
            RFE: RF_0856(hemB)
            RBE: RBE_0920(hemB)
            RAK: A1C_03995
            RBO: A1I_04065
            RCM: A1E_02290
            RRI: A1G_04490
            OTS: OTBS_1224(hemB)
            WOL: WD0158(hemB)
            WBM: Wbm0373
            AMA: AM417(hemB)
            APH: APH_0851(hemB)
            ERU: Erum2720(hemB)
            ERW: ERWE_CDS_02770(hemB)
            ERG: ERGA_CDS_02720(hemB)
            ECN: Ecaj_0262
            ECH: ECH_0821(hemB)
            NSE: NSE_0394(hemB)
            PUB: SAR11_1051(hemB)
            MLO: mll8390
            MES: Meso_1129
            PLA: Plav_2897
            SME: SMc01766(hemB)
            SMD: Smed_0812
            ATU: Atu1161(hemB)
            ATC: AGR_C_2149
            RET: RHE_CH01504(hemB)
            RLE: RL1616(hemB)
            BME: BMEI1197
            BMF: BAB1_0780(hemB)
            BMS: BR0757(hemB)
            BMB: BruAb1_0774(hemB)
            BOV: BOV_0752(hemB)
            OAN: Oant_2536
            BJA: blr5037(hemB)
            BRA: BRADO4436(hemB)
            BBT: BBta_4655(hemB)
            RPA: RPA2712(hemB)
            RPB: RPB_2623
            RPC: RPC_0171 RPC_2651
            RPD: RPD_2660
            RPE: RPE_0277 RPE_3009
            NWI: Nwi_1909
            NHA: Nham_2240
            XAU: Xaut_4295
            CCR: CC_1347
            SIL: SPO2076(hemB)
            SIT: TM1040_1351
            RSP: RSP_2848(hemB)
            RSH: Rsph17029_1445
            RSQ: Rsph17025_1498
            JAN: Jann_2324
            RDE: RD1_2749(hemB)
            PDE: Pden_3809
            MMR: Mmar10_1547
            HNE: HNE_0898(hemB)
            ZMO: ZMO1879(hemB)
            NAR: Saro_0073
            SAL: Sala_2737
            SWI: Swit_1089
            ELI: ELI_13145
            GOX: GOX2308
            GBE: GbCGDNIH1_1001
            ACR: Acry_0181
            RRU: Rru_A0141 Rru_A1837
            MAG: amb2563
            MGM: Mmc1_3144
            ABA: Acid345_4300
            SUS: Acid_2458
            BSU: BG10344(hemB)
            BHA: BH3044(hemB)
            BAN: BA4694(hemB)
            BAR: GBAA4694(hemB)
            BAA: BA_5133
            BAT: BAS4359
            BCE: BC4469
            BCA: BCE_4553(hemB)
            BCZ: BCZK4206(hemB)
            BCY: Bcer98_3178
            BTK: BT9727_4195(hemB)
            BTL: BALH_4055(hemB)
            BLI: BL00627(hemB)
            BLD: BLi02943(hemB)
            BCL: ABC2628(hemB)
            BAY: RBAM_025190(hemB)
            BPU: BPUM_2454(hemB)
            OIH: OB2066(hemB)
            GKA: GK2643
            GTN: GTNG_2572(hemB)
            SAU: SA1492(hemB)
            SAV: SAV1668(hemB)
            SAM: MW1612(hemB)
            SAR: SAR1748(hemB)
            SAS: SAS1597
            SAC: SACOL1715(hemB)
            SAB: SAB1528c(hemB)
            SAA: SAUSA300_1615(hemB)
            SAO: SAOUHSC_01772
            SAJ: SaurJH9_1726
            SAH: SaurJH1_1760
            SEP: SE1343
            SER: SERP1232(hemB)
            SHA: SH1259(hemB)
            SSP: SSP1096
            LMO: lmo1554(hemB)
            LMF: LMOf2365_1575(hemB)
            LIN: lin1589(hemB)
            LWE: lwe1567(hemB)
            SSA: SSA_0487
            LRE: Lreu_1701
            CAC: CAC0100(hemB)
            CPE: CPE1433(hemB)
            CPF: CPF_1686(hemB)
            CPR: CPR_1420(hemB)
            CTC: CTC00729
            CNO: NT01CX_0260(hemB)
            CTH: Cthe_2529
            CDF: CD3419(hemB)
            CBO: CBO0923(hemB)
            CBA: CLB_0964(hemB)
            CBH: CLC_0978(hemB)
            CBF: CLI_1010(hemB)
            CBE: Cbei_1287
            CKL: CKL_0713(hemB)
            AMT: Amet_0062
            CHY: CHY_1210(hemB)
            DSY: DSY2222
            DRM: Dred_2160
            SWO: Swol_0690
            CSC: Csac_1653
            MTA: Moth_1246
            MTU: Rv0512(hemB)
            MTC: MT0533(hemB)
            MBO: Mb0525(hemB)
            MBB: BCG_0555(hemB)
            MLE: ML2419(hemB)
            MPA: MAP4005(hemB)
            MAV: MAV_4637(hemB)
            MSM: MSMEG_0956(hemB)
            MVA: Mvan_0847
            MGI: Mflv_0064
            MMC: Mmcs_0679
            MKM: Mkms_0692
            MJL: Mjls_0672
            CGL: NCgl0416(cgl0431)
            CGB: cg0512(hemB)
            CEF: CE0453
            CDI: DIP0403(hemB)
            CJK: jk1899(hemB)
            NFA: nfa51660(hemB)
            RHA: RHA1_ro02050
            SCO: SCO3311(hemB)
            SMA: SAV4742(hemB)
            TWH: TWT730(hemB)
            TWS: TW744(hemB)
            LXX: Lxx01120(hemB)
            CMI: CMM_0598(hemB)
            ART: Arth_2765
            AAU: AAur_2749(hemB)
            PAC: PPA0302
            NCA: Noca_0497
            TFU: Tfu_2730
            FRA: Francci3_0488
            FAL: FRAAL0986(hemB)
            ACE: Acel_0235
            KRA: Krad_0620
            SEN: SACE_6943(hemB)
            STP: Strop_0359
            RXY: Rxyl_1976
            FNU: FN0460
            RBA: RB1856
            CTR: CT633(hemB)
            CTA: CTA_0687(hemB)
            CMU: TC0001
            CPN: CPn0744(hemB)
            CPA: CP0001
            CPJ: CPj0744(hemB)
            CPT: CpB0772
            CCA: CCA00001(hemB)
            CAB: CAB001(hemB)
            CFE: CF1005(hemB)
            PCU: pc0092(hemB)
            LIL: LB012(hemB)
            LIC: LIC20010(hemB)
            LBJ: LBJ_4010(hemB)
            LBL: LBL_4010(hemB)
            SYN: sll1994(hemB)
            SYW: SYNW1933(hemB)
            SYC: syc2301_c(hemB)
            SYF: Synpcc7942_1792
            SYD: Syncc9605_0507
            SYE: Syncc9902_1828
            SYG: sync_2398(hemB)
            SYR: SynRCC307_0315(hemB)
            SYX: SynWH7803_2099(hemB)
            CYA: CYA_2762(hemB)
            CYB: CYB_2456(hemB)
            TEL: tll0422(hemB)
            GVI: glr4358(hemB)
            ANA: all4725 alr4380(hemB)
            AVA: Ava_1946 Ava_3297 Ava_B0225
            PMA: Pro0243(hemB)
            PMM: PMM0215
            PMT: PMT1547(T6C23.6)
            PMN: PMN2A_1583
            PMI: PMT9312_0217
            PMB: A9601_02351(hemB)
            PMC: P9515_02451(hemB)
            PMF: P9303_03881(hemB)
            PMG: P9301_02361(hemB)
            PMH: P9215_02351(hemB)
            PME: NATL1_02931(hemB)
            TER: Tery_4608
            SRU: SRU_1013(hemB)
            CHU: CHU_0646(hemB)
            GFO: GFO_3230(hemB)
            FJO: Fjoh_0957
            FPS: FP0035(hemB)
            CTE: CT1431(hemB)
            CCH: Cag_1520
            CPH: Cpha266_1804
            PVI: Cvib_1252
            PLT: Plut_1435
            RRS: RoseRS_1752
            RCA: Rcas_2032
            DRA: DR_2160
            DGE: Dgeo_0882
            TTH: TTC1234
            TTJ: TTHA1598
            AAE: aq_2109(hemB)
            TME: Tmel_0709
            MJA: MJ0643
            MMP: MMP1258(hemB)
            MMQ: MmarC5_0333
            MMZ: MmarC7_0504
            MAE: Maeo_0916
            MVN: Mevan_0571
            MAC: MA0578(hemB)
            MBA: Mbar_A1463
            MMA: MM_1742
            MBU: Mbur_1228
            MTP: Mthe_0050
            MHU: Mhun_2561
            MLA: Mlab_0051
            MEM: Memar_0981
            MBN: Mboo_1236
            MST: Msp_0416(hemB)
            MSI: Msm_1476
            MKA: MK0198(hemB)
            HAL: VNG2322G(hem2)
            HMA: rrnAC2610(hemB)
            HWA: HQ3443A(hemB)
            NPH: NP0920A(hemB)
            TAC: Ta0955
            TVO: TVN1100
            PTO: PTO1311
            RCI: RCIX912(hemB)
            APE: APE_2300.1
            IHO: Igni_0324
            HBU: Hbut_1386
            SSO: SSO0181
            STO: ST0214
            SAI: Saci_0778(alaD)
            MSE: Msed_0215
            PAI: PAE0583(hemB)
            PIS: Pisl_0042
            PCL: Pcal_1709
            PAS: Pars_2247
STRUCTURES  PDB: 1AW5  1B4E  1B4K  1E51  1EB3  1GJP  1GZG  1H7N  1H7O  1H7P  
                 1H7R  1I8J  1L6S  1L6Y  1OHL  1PV8  1QML  1QNV  1W1Z  1W31  
                 1W54  1W56  1W5M  1W5N  1W5O  1W5P  1W5Q  1YLV  2C13  2C14  
                 2C15  2C16  2C18  2C19  2C1H  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.24
            ExPASy - ENZYME nomenclature database: 4.2.1.24
            ExplorEnz - The Enzyme Database: 4.2.1.24
            ERGO genome analysis and discovery system: 4.2.1.24
            BRENDA, the Enzyme Database: 4.2.1.24
            CAS: 9036-37-7
///
ENTRY       EC 4.2.1.25                 Enzyme
NAME        L-arabinonate dehydratase;
            L-arabonate dehydrase;
            L-arabonate dehydratase;
            L-arabinonate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     L-arabinonate hydro-lyase (2-dehydro-3-deoxy-L-arabinonate-forming)
REACTION    L-arabinonate = 2-dehydro-3-deoxy-L-arabinonate + H2O [RN:R02522]
ALL_REAC    R02522
SUBSTRATE   L-arabinonate [CPD:C00545]
PRODUCT     2-dehydro-3-deoxy-L-arabinonate [CPD:C00684];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:13654251]
  AUTHORS   WEIMBERG R.
  TITLE     L-2-Keto-4,5-dihydroxyvaleric acid: an intermediate in the oxidation
            of L-arabinose by Pseudomonas saccharophila.
  JOURNAL   J. Biol. Chem. 234 (1959) 727-32.
  ORGANISM  Pseudomonas saccharophila
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.25
            ExPASy - ENZYME nomenclature database: 4.2.1.25
            ExplorEnz - The Enzyme Database: 4.2.1.25
            ERGO genome analysis and discovery system: 4.2.1.25
            BRENDA, the Enzyme Database: 4.2.1.25
            CAS: 9024-30-0
///
ENTRY       EC 4.2.1.26       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
COMMENT     Deleted entry: was transferred to EC 4.3.1.21, aminodeoxygluconate
            ammonia-lyase, which has since been deleted. The enzyme is identical
            to EC 4.3.1.9, glucosaminate ammonia-lyase (EC 4.2.1.26 created
            1965, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.26
            ExPASy - ENZYME nomenclature database: 4.2.1.26
            ExplorEnz - The Enzyme Database: 4.2.1.26
            ERGO genome analysis and discovery system: 4.2.1.26
            BRENDA, the Enzyme Database: 4.2.1.26
///
ENTRY       EC 4.2.1.27                 Enzyme
NAME        acetylenecarboxylate hydratase;
            acetylenemonocarboxylate hydratase;
            alkynoate hydratase;
            acetylenemonocarboxylate hydrase;
            acetylenemonocarboxylic acid hydrase;
            malonate-semialdehyde dehydratase;
            3-oxopropanoate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     3-oxopropanoate hydro-lyase (propynoate-forming)
REACTION    3-oxopropanoate = propynoate + H2O [RN:R01611]
ALL_REAC    R01611;
            (other) R01367
SUBSTRATE   3-oxopropanoate [CPD:C00222]
PRODUCT     propynoate [CPD:C00804];
            H2O [CPD:C00001]
COMMENT     The reaction is effectively irreversible, favouring oxopropanoate
            (malonic semialdehyde) and its tautomers. Also acts on but-3-ynoate
            forming acetoacetate. The mechanism appears to involve hydration of
            the acetylene to 3-hydroxypropenoate, which will spontaneously
            tautomerize to 3-oxopropanoate. It is thus analogous to EC 4.1.1.78,
            acetylenedicarboxylate decarboxylase, in its mechanism.
REFERENCE   1  [PMID:16525953]
  AUTHORS   Hildebrand F, van Griensven M, Giannoudis P, Schreiber T, Frink M,
            Probst C, Grotz M, Krettek C, Pape HC.
  TITLE     Impact of hypothermia on the immunologic response after trauma and
            elective surgery.
  JOURNAL   Surg. Technol. Int. 14 (2005) 41-50.
REFERENCE   2  [PMID:13654296]
  AUTHORS   YAMADA EW, JAKOBY WB.
  TITLE     Enzymatic utilization of acetylenic compounds. II.
            Acetylenemonocarboxylic acid hydrase.
  JOURNAL   J. Biol. Chem. 234 (1959) 941-5.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00410  beta-Alanine metabolism
            PATH: map00640  Propanoate metabolism
            PATH: map00650  Butanoate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.27
            ExPASy - ENZYME nomenclature database: 4.2.1.27
            ExplorEnz - The Enzyme Database: 4.2.1.27
            ERGO genome analysis and discovery system: 4.2.1.27
            BRENDA, the Enzyme Database: 4.2.1.27
            CAS: 9024-26-4
///
ENTRY       EC 4.2.1.28                 Enzyme
NAME        propanediol dehydratase;
            meso-2,3-butanediol dehydrase;
            diol dehydratase;
            DL-1,2-propanediol hydro-lyase;
            diol dehydrase;
            adenosylcobalamin-dependent diol dehydratase;
            propanediol dehydrase;
            coenzyme B12-dependent diol dehydrase;
            1,2-propanediol dehydratase;
            dioldehydratase;
            propane-1,2-diol hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     propane-1,2-diol hydro-lyase (propanal-forming)
REACTION    propane-1,2-diol = propanal + H2O [RN:R02376]
ALL_REAC    R02376
SUBSTRATE   propane-1,2-diol [CPD:C00583]
PRODUCT     propanal [CPD:C00479];
            H2O [CPD:C00001]
COFACTOR    Cobamide [CPD:C00210]
COMMENT     Requires a cobamide coenzyme. Also dehydrates ethylene glycol to
            acetaldehyde.
REFERENCE   1  [PMID:13680987]
  AUTHORS   ABELES RH, LEE HA Jr.
  TITLE     An intramolecular oxidation-reduction requiring a cobamide coenzyme.
  JOURNAL   J. Biol. Chem. 236 (1961) 2347-50.
  ORGANISM  Aerobacter aerogenes
REFERENCE   2  [PMID:7035429]
  AUTHORS   Forage RG, Foster MA.
  TITLE     Glycerol fermentation in Klebsiella pneumoniae: functions of the
            coenzyme B12-dependent glycerol and diol dehydratases.
  JOURNAL   J. Bacteriol. 149 (1982) 413-9.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   3  [PMID:13929077]
  AUTHORS   LEE HA Jr, ABELES RH.
  TITLE     Purification and properties of dioldehydrase, and enzyme requiring a
            cobamide coenzyme.
  JOURNAL   J. Biol. Chem. 238 (1963) 2367-73.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00561  Glycerolipid metabolism
ORTHOLOGY   KO: K01699  diol dehydratase
GENES       RET: RHE_CH03790
            RLE: RL4317
            BME: BMEI0092
            RDE: RD1_1389
            GOX: GOX0183
            CGB: cg2830(pduO)
            FAL: FRAAL5927
            SEN: SACE_6271
            FNU: FN1303
STRUCTURES  PDB: 1DIO  1EEX  1EGM  1EGV  1IWB  1UC4  1UC5  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.28
            ExPASy - ENZYME nomenclature database: 4.2.1.28
            ExplorEnz - The Enzyme Database: 4.2.1.28
            ERGO genome analysis and discovery system: 4.2.1.28
            BRENDA, the Enzyme Database: 4.2.1.28
            CAS: 9026-90-8
///
ENTRY       EC 4.2.1.29       Obsolete  Enzyme
NAME        Transferred to 4.99.1.6
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
COMMENT     Transferred entry: now EC 4.99.1.6 indoleacetaldoxime dehydratase.
            The enzyme was classified incorrectly as a C-O lyase when the bond
            broken is a N-O bond. (EC 4.2.1.29 created 1965, deleted 2004)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.29
            ExPASy - ENZYME nomenclature database: 4.2.1.29
            ExplorEnz - The Enzyme Database: 4.2.1.29
            ERGO genome analysis and discovery system: 4.2.1.29
            BRENDA, the Enzyme Database: 4.2.1.29
///
ENTRY       EC 4.2.1.30                 Enzyme
NAME        glycerol dehydratase;
            glycerol dehydrase;
            glycerol hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     glycerol hydro-lyase (3-hydroxypropanal-forming)
REACTION    glycerol = 3-hydroxypropanal + H2O [RN:R01047]
ALL_REAC    R01047;
            (other) R01048
SUBSTRATE   glycerol [CPD:C00116]
PRODUCT     3-hydroxypropanal [CPD:C00969];
            H2O [CPD:C00001]
COFACTOR    Cobamide [CPD:C00210]
COMMENT     Requires a cobamide coenzyme.
REFERENCE   1  [PMID:7035429]
  AUTHORS   Forage RG, Foster MA.
  TITLE     Glycerol fermentation in Klebsiella pneumoniae: functions of the
            coenzyme B12-dependent glycerol and diol dehydratases.
  JOURNAL   J. Bacteriol. 149 (1982) 413-9.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   2  [PMID:4989992]
  AUTHORS   Schneider Z, Larsen EG, Jacobson G, Johnson BC, Pawelkiewicz J.
  TITLE     Purification and properties of glycerol dehydrase.
  JOURNAL   J. Biol. Chem. 245 (1970) 3388-96.
  ORGANISM  Aerobacter aerogenes
REFERENCE   3  [PMID:5962440]
  AUTHORS   Schneider Z, Pawelkiewicz J.
  TITLE     The properties of glycerol dehydratase isolated from Aerobacter
            aerogenes, and the properties of the apoenzyme subunits.
  JOURNAL   Acta. Biochim. Pol. 13 (1966) 311-28.
  ORGANISM  Aerobacter aerogenes
REFERENCE   4  [PMID:14039344]
  AUTHORS   SMILEY KL, SOBOLOV M.
  TITLE     A cobamide-requiring glycerol dehydrase from an acrolein-forming
            Lactobacillus.
  JOURNAL   Arch. Biochem. Biophys. 97 (1962) 538-43.
  ORGANISM  Lactobacillus sp.
PATHWAY     PATH: map00561  Glycerolipid metabolism
ORTHOLOGY   KO: K01700  glycerol dehydratase
            KO: K06120  glycerol dehydratase large subunit
            KO: K06121  glycerol dehydratase medium subunit
            KO: K06122  glycerol dehydratase small subunit
GENES       ECW: EcE24377A_2281(pduC)
            STY: STY2245(pduC) STY2246(pduD) STY2247(pduE)
            STT: t0832(pduE) t0833(pduD) t0834(pduC)
            SPT: SPA0829(pduE) SPA0830(pduD) SPA0831(pduC)
            SEC: SC2048(pduC) SC2049(pduD) SC2050(pduE)
            STM: STM2040(pduC) STM2041(pduD) STM2042(pduE)
            YEN: YE2730(pddA) YE2731(pddB) YE2732(pddC)
            SSN: SSON_2060(pduC) SSON_2061(pduD) SSON_2062(pduE)
            MLO: mll6722
            LMO: lmo1153 lmo1154 lmo1155
            LMF: LMOf2365_1161(pduC) LMOf2365_1162(pduD) LMOf2365_1163(pduE)
            LIN: lin1117 lin1118 lin1119
            LWE: lwe1111(pduC) lwe1112(pduD) lwe1113(pduE)
            SSA: SSA_0533(pduC) SSA_0535 SSA_0536
            LBR: LVIS_1613 LVIS_1614 LVIS_1615
            LRE: Lreu_1747
            CPE: CPE0929 CPE0930 CPE0931
            CPF: CPF_1173 CPF_1174 CPF_1175
            CPR: CPR_1004(dhaB) CPR_1005(dhaC) CPR_1006(dhaE)
            CKL: CKL_0843(dhaA) CKL_0844(dhaC)
            MSM: MSMEG_1546 MSMEG_1547 MSMEG_1548
            MVA: Mvan_5563
            MGI: Mflv_1245
            MMC: Mmcs_4953 Mmcs_4954
            MKM: Mkms_5042
            MJL: Mjls_5335
STRUCTURES  PDB: 1IWP  1MMF  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.30
            ExPASy - ENZYME nomenclature database: 4.2.1.30
            ExplorEnz - The Enzyme Database: 4.2.1.30
            ERGO genome analysis and discovery system: 4.2.1.30
            BRENDA, the Enzyme Database: 4.2.1.30
            CAS: 9077-68-3
///
ENTRY       EC 4.2.1.31                 Enzyme
NAME        maleate hydratase;
            D-malate hydro-lyase;
            malease;
            (R)-malate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (R)-malate hydro-lyase (maleate-forming)
REACTION    (R)-malate = maleate + H2O [RN:R02419]
ALL_REAC    R02419
SUBSTRATE   (R)-malate [CPD:C00497]
PRODUCT     maleate [CPD:C01384];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:5796106]
  AUTHORS   Britten JS, Morell H, Taggart JV.
  TITLE     Anion activation of maleate hydratase.
  JOURNAL   Biochim. Biophys. Acta. 185 (1969) 220-7.
  ORGANISM  rabbit
REFERENCE   2  [PMID:14917669]
  AUTHORS   SACKS W, JENSEN CO.
  TITLE     Malease, a hydrase from corn kernels.
  JOURNAL   J. Biol. Chem. 192 (1951) 231-6.
  ORGANISM  Zea mays [GN:ezma]
PATHWAY     PATH: map00650  Butanoate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.31
            ExPASy - ENZYME nomenclature database: 4.2.1.31
            ExplorEnz - The Enzyme Database: 4.2.1.31
            ERGO genome analysis and discovery system: 4.2.1.31
            BRENDA, the Enzyme Database: 4.2.1.31
            CAS: 37290-71-4
///
ENTRY       EC 4.2.1.32                 Enzyme
NAME        L(+)-tartrate dehydratase;
            tartrate dehydratase;
            tartaric acid dehydrase;
            L-tartrate dehydratase;
            L-(+)-tartaric acid dehydratase;
            (R,R)-tartrate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (R,R)-tartrate hydro-lyase (oxaloacetate-forming)
REACTION    (R,R)-tartrate = oxaloacetate + H2O [RN:R00339]
ALL_REAC    R00339
SUBSTRATE   (R,R)-tartrate [CPD:C00898]
PRODUCT     oxaloacetate [CPD:C00036];
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023];
            Thiol [CPD:C00145]
COMMENT     The enzyme exists in an inactive low-molecular-mass form, which is
            converted into active enzyme in the presence of Fe2+ and thiol. cf.
            EC 4.2.1.81 D(-)-tartrate dehydratase.
REFERENCE   1  [PMID:14342293]
  AUTHORS   HURLBERT RE, JAKOBY WB.
  TITLE     TARTARIC ACID METABOLISM. I. SUBUNITS OF L(+)-TARTARIC ACID
            DEHYDRASE.
  JOURNAL   J. Biol. Chem. 240 (1965) 2772-7.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K01701  L(+)-tartrate dehydratase
            KO: K03779  L(+)-tartrate dehydratase alpha subunit
            KO: K03780  L(+)-tartrate dehydratase beta subunit
GENES       ECO: b3061(ttdA) b3062(ttdB)
            ECJ: JW3033(ttdA) JW3034(ttdB)
            ECE: Z4414(ttdA) Z4415(ttdB)
            ECS: ECs3944 ECs3945
            ECC: c3812(ttdA) c3813(ttdB)
            ECI: UTI89_C3497(ttdA) UTI89_C3498(ttdB)
            ECP: ECP_3151 ECP_3152
            ECV: APECO1_3352(ttdB) APECO1_3353(ttdA)
            ECW: EcE24377A_3526(ttdB)
            ECX: EcHS_A3242(ttdB)
            STY: STY3534(ttdB) STY3535(ttdA)
            STT: t3269(ttdB) t3270(ttdA)
            SPT: SPA3221(ttdB) SPA3222(ttdA)
            SEC: SC3292(ttdB) SC3293(ttdA)
            STM: STM3354 STM3355
            SFL: SF3102(ttdA) SF3103(ttdB)
            SFX: S3307(ttdA) S3308(ttdB)
            SFV: SFV_3101(ttdA) SFV_3102(ttdB)
            SSN: SSON_3198(ttdA) SSON_3199(ttdB)
            SBO: SBO_2919(ttdA) SBO_2920(ttdB)
            REU: Reut_B5650 Reut_B5651
            BUR: Bcep18194_A5523
            HAR: HEAR0919(fumA) HEAR3330 HEAR3332
            WSU: WS1529(accA) WS1530
            CCO: CCC13826_1231
            RSP: RSP_3145(ttdB) RSP_3146(ttdA)
            RRU: Rru_A2206
            MAG: amb3178 amb3179
            SUS: Acid_5423
            LPL: lp_1089(ttdB) lp_1090(ttdA)
            SWO: Swol_1628 Swol_1629
            RHA: RHA1_ro08823(ttdB)
            MMQ: MmarC5_0028
            MMZ: MmarC7_0796
            MAE: Maeo_0918
            MVN: Mevan_0862
            HBU: Hbut_0158 Hbut_0159
            PIS: Pisl_0951
            PCL: Pcal_1059
            PAS: Pars_0828
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.32
            ExPASy - ENZYME nomenclature database: 4.2.1.32
            ExplorEnz - The Enzyme Database: 4.2.1.32
            ERGO genome analysis and discovery system: 4.2.1.32
            BRENDA, the Enzyme Database: 4.2.1.32
            CAS: 9014-40-8
///
ENTRY       EC 4.2.1.33                 Enzyme
NAME        3-isopropylmalate dehydratase;
            (2R,3S)-3-isopropylmalate hydro-lyase;
            beta-isopropylmalate dehydratase;
            isopropylmalate isomerase;
            alpha-isopropylmalate isomerase;
            3-isopropylmalate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (2R,3S)-3-isopropylmalate hydro-lyase (2-isopropylmaleate-forming)
REACTION    (1) (1a) (2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H2O
            [RN:R04001];
            (2) (1b) 2-isopropylmaleate + H2O = (2S)-2-isopropylmalate
ALL_REAC    R04001;
            (other) R03968
SUBSTRATE   (2R,3S)-3-isopropylmalate [CPD:C04411];
            2-isopropylmaleate [CPD:C02631];
            H2O [CPD:C00001]
PRODUCT     2-isopropylmaleate [CPD:C02631];
            H2O [CPD:C00001];
            (2S)-2-isopropylmalate [CPD:C02504]
COMMENT     Forms part of the leucine-biosynthesis pathway. The enzyme brings
            about the interconversion of the two isomers of isopropylmalate.
REFERENCE   1  [PMID:14087357]
  AUTHORS   GROSS SR, BURNS RO, UMBARGER HE.
  TITLE     THE BIOSYNTHESIS OF LEUCINE. II. THE ENZYMIC ISOMERIZATION OF
            BETA-CARBOXY-BETA-HYDROXYISOCAPROATE AND
            ALPHA-HYDROXY-BETA-CARBOXYISOCAPROATE.
  JOURNAL   Biochemistry. 2 (1963) 1046-52.
  ORGANISM  Neurospora crassa [GN:dncr], Salmonella typhimurium
REFERENCE   2  [PMID:14269331]
  AUTHORS   CALVO JM, STEVENS CM, KALYANPUR MG, UMBARGER HE.
  TITLE     THE ABSOLUTE CONFIGURATION OF ALPHA-HYDROXY-BETA-CARBOXYISOCAPROIC
            ACID (3-ISOPROPYLMALIC ACID), AN INTERMEDIATE IN LEUCINE
            BIOSYNTHESIS.
  JOURNAL   Biochemistry. 19 (1964) 2024-7.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   3  [PMID:4270046]
  AUTHORS   Cole FE, Kalyanpur MG, Stevens CM.
  TITLE     Absolute configuration of alpha isopropylmalate and the mechanism of
            its conversion to beta isopropylmalate in the biosynthesis of
            leucine.
  JOURNAL   Biochemistry. 12 (1973) 3346-50.
  ORGANISM  Neurospora crassa [GN:dncr]
PATHWAY     PATH: map00290  Valine, leucine and isoleucine biosynthesis
ORTHOLOGY   KO: K01702  3-isopropylmalate dehydratase
            KO: K01703  3-isopropylmalate/(R)-2-methylmalate dehydratase large
                        subunit
            KO: K01704  3-isopropylmalate/(R)-2-methylmalate dehydratase small
                        subunit
GENES       ATH: AT2G43090
            OSA: 4330192
            CME: CMO094C
            SCE: YGL009C(LEU1)
            AGO: AGOS_AGR169W
            PIC: PICST_68659(LEU1)
            CAL: CaO19_7498(CaO19.7498)
            CGR: CAGL0A00363g
            YLI: YALI0B01364g(LEU1)
            SPO: SPAC9E9.03
            ANI: AN5886.2
            AFM: AFUA_2G11260
            AOR: AO090026000524
            CNE: CNA02270
            UMA: UM06010.1
            ECO: b0071(leuD) b0072(leuC)
            ECJ: JW0070(leuD) JW0071(leuC)
            ECE: Z0080(leuD) Z0081(leuC)
            ECS: ECs0075 ECs0076
            ECC: c0087(leuD) c0089(leuC)
            ECI: UTI89_C0078(leuD) UTI89_C0079(leuC)
            ECP: ECP_0073 ECP_0074
            ECV: APECO1_1911(leuC) APECO1_1912(leuD)
            ECW: EcE24377A_0074(leuD) EcE24377A_0075(leuC)
            ECX: EcHS_A0076(leuD) EcHS_A0077(leuC)
            STY: STY0129(leuD) STY0130(leuC)
            STT: t0114(leuD) t0115(leuC)
            SPT: SPA0112(leuD) SPA0113(leuC)
            SEC: SC0106(leuD) SC0107(leuC) SC0374(ledL) SC0375(ledS)
            STM: STM0110(leuD) STM0111(leuC) STM0329 STM0330
            YPE: YPO0530(leuD) YPO0531(leuC)
            YPK: y3647(leuC) y3648(leuD)
            YPM: YP_3651(leuC) YP_3652(leuD)
            YPA: YPA_3566 YPA_3567
            YPN: YPN_0400 YPN_0401
            YPP: YPDSF_3108 YPDSF_3109
            YPS: YPTB0669(leuD) YPTB0670(leuC)
            YPI: YpsIP31758_3407(leuC) YpsIP31758_3408(leuD)
            YEN: YE0652(leuC)
            SFL: SF0066(leuD) SF0067(leuC)
            SFX: S0068(leuD) S0069(leuC)
            SFV: SFV_0063(leuD) SFV_0064(leuC)
            SSN: SSON_0078(leuD) SSON_0079(leuC)
            SBO: SBO_0058(leuD) SBO_0059(leuC)
            SDY: SDY_0098(leuD) SDY_0099(leuC)
            ECA: ECA3833(leuC) ECA3834(leuD)
            PLU: plu1869 plu1870 plu3675(leuC) plu3676(leuD)
            BUC: BUpL06(leuC) BUpL07(leuD)
            BAB: bbp494(leuD) bbp495(leuC)
            SGL: SG0434 SG0435
            ENT: Ent638_0619 Ent638_0620
            KPN: KPN_00078(leuC)
            SPE: Spro_0742 Spro_0743
            BFL: Bfl130(leuD) Bfl131(leuC)
            BPN: BPEN_134(leuD) BPEN_135(leuC)
            HIN: HI0988(leuC) HI0989(leuD)
            HIT: NTHI1162(leuC) NTHI1163(leuD)
            HIP: CGSHiEE_07020(leuD) CGSHiEE_07025
            HIQ: CGSHiGG_08525
            HSO: HS_0389(leuD) HS_0390(leuC)
            PMU: PM1959(leuD) PM1960(leuC)
            MSU: MS0333(leuC) MS0334(leuD) MS0595(leuD) MS0596(leuC)
            APL: APL_0138(leuD) APL_0139(leuC)
            ASU: Asuc_1909 Asuc_1910
            XFA: XF2374 XF2375
            XFT: PD1398(leuD) PD1399(leuC)
            XCC: XCC3330(leuD) XCC3331(leuC)
            XCB: XC_0833 XC_0834
            XCV: XCV3585(leuD) XCV3586(leuC)
            XAC: XAC3457(leuD) XAC3458(leuC)
            XOO: XOO0936(leuC) XOO0937(leuD)
            XOM: XOO_0857(XOO0857) XOO_0858(XOO0858)
            VCH: VC2492 VC2493
            VCO: VC0395_A2067(leuC) VC0395_A2068(leuD)
            VVU: VV1_0656 VV1_0657
            VVY: VV0484 VV0485
            VPA: VP0342 VP0343
            VFI: VF0292 VF0293
            PPR: PBPRA0416(leuD) PBPRA0417
            PAE: PA3120(leuD) PA3121(leuC)
            PAU: PA14_23750(leuC) PA14_23760(leuD)
            PPU: PP_1985(leuC) PP_1986(leuD)
            PPF: Pput_3773 Pput_3774 Pput_5021 Pput_5022
            PST: PSPTO_2173(leuC) PSPTO_2174(leuD)
            PSB: Psyr_1983 Psyr_1984
            PSP: PSPPH_1952(leuC) PSPPH_1953(leuD)
            PFL: PFL_2063(leuC) PFL_2064(leuD)
            PFO: Pfl_1889 Pfl_1890 Pfl_2359 Pfl_2360
            PEN: PSEEN1650(leuC) PSEEN1651(leuD)
            PMY: Pmen_2722 Pmen_2723
            PAR: Psyc_1412(leuD) Psyc_1413(leuC)
            PCR: Pcryo_1573 Pcryo_1574
            PRW: PsycPRwf_1935 PsycPRwf_1936
            ACI: ACIAD0463(leuC) ACIAD0466(leuD)
            ACB: A1S_0418
            SON: SO_4233(leuD) SO_4234(leuC)
            SDN: Sden_0336 Sden_0337
            SFR: Sfri_3817 Sfri_3818
            SBL: Sbal_0388
            SBM: Shew185_0387
            SLO: Shew_3469
            SPC: Sputcn32_0473
            SSE: Ssed_0395
            SPL: Spea_3825 Spea_3826
            SHE: Shewmr4_3585 Shewmr4_3586
            SHM: Shewmr7_0370 Shewmr7_0371
            SHN: Shewana3_3758 Shewana3_3759
            SHW: Sputw3181_0376
            CPS: CPS_4210(leuC) CPS_4211(leuD)
            PHA: PSHAa2891(leuD) PSHAa2892(leuC)
            PAT: Patl_2765 Patl_3270 Patl_3271
            SDE: Sde_2085 Sde_2086
            PIN: Ping_1669 Ping_1670
            MAQ: Maqu_1564
            MCA: MCA2064(leuD) MCA2065(leuC)
            FTL: FTL_1888 FTL_1889
            FTH: FTH_1813(leuD) FTH_1814
            FTA: FTA_1998(leuD) FTA_1999(leuC)
            FTN: FTN_0060(leuD) FTN_0061(leuC)
            TCX: Tcr_0795 Tcr_0796
            NOC: Noc_1013 Noc_2935
            AEH: Mlg_1228 Mlg_1229
            HHA: Hhal_1811
            HCH: HCH_02428(leuC) HCH_02429(leuD)
            CSA: Csal_2452 Csal_2453
            ABO: ABO_1469(leuD) ABO_1470(leuC)
            MMW: Mmwyl1_2091 Mmwyl1_2092
            AHA: AHA_0879(leuD) AHA_0880(leuC)
            CRP: CRP_080 CRP_081
            RMA: Rmag_0371
            VOK: COSY_0349(leuD) COSY_0350(leuC)
            NME: NMB1034 NMB1036
            NMA: NMA1450(leuC) NMA1452(leuD)
            NMC: NMC1176(leuC) NMC1179(leuD)
            NGO: NGO0677 NGO0679
            CVI: CV_2168(leuD1) CV_2169(leuC2) CV_2782(leuD2) CV_2784(leuC1)
            RSO: RSc1989(leuD) RSc1990(leuC)
            REU: Reut_A2312 Reut_A2314 Reut_B4842 Reut_B4843 Reut_B5386
                 Reut_B5387
            REH: H16_A1236(leuC1) H16_A1237(leuD1) H16_A1549(leuC2)
                 H16_A1550(leuD2) H16_A2620(leuD3) H16_A2621(leuC3)
                 H16_B0051(leuD4) H16_B0052(leuC4) H16_B2275(leuC5)
                 H16_B2276(leuD5)
            RME: Rmet_0200 Rmet_0201 Rmet_2473 Rmet_2475 Rmet_4273 Rmet_4274
                 Rmet_5867 Rmet_5868
            BMA: BMAA1727(leuD) BMAA1729(leuC)
            BMV: BMASAVP1_1641(leuC) BMASAVP1_1642(leuD)
            BML: BMA10299_1849(leuC) BMA10299_1851(leuD)
            BMN: BMA10247_A0520(leuC) BMA10247_A0522(leuD)
            BXE: Bxe_A2731 Bxe_A2732 Bxe_B0459 Bxe_B0460 Bxe_B2521 Bxe_B2522
                 Bxe_B2888 Bxe_B2889
            BVI: Bcep1808_4456
            BUR: Bcep18194_B2132 Bcep18194_B2133 Bcep18194_C6956
                 Bcep18194_C6957
            BCN: Bcen_4416 Bcen_4418
            BCH: Bcen2424_3949 Bcen2424_3951
            BAM: Bamb_3340 Bamb_3342
            BPS: BPSS1706(leuD) BPSS1707(leuC)
            BPM: BURPS1710b_A0776(leuD) BURPS1710b_A0778(leuC)
            BPL: BURPS1106A_A2314(leuD) BURPS1106A_A2316(leuC)
            BPD: BURPS668_A2452(leuD) BURPS668_A2454(leuC)
            BTE: BTH_II0672(leuC) BTH_II0673(leuD)
            PNU: Pnuc_0766
            BPE: BP1356(leuD) BP1357(leuC) BP1481(leuC) BP1482(leuD)
            BPA: BPP1942(leuC) BPP1943(leuD) BPP2684(leuD) BPP2685(leuC)
                 BPP3650 BPP3651
            BBR: BB1015(leuD) BB1016(leuC) BB2130(leuC) BB2131(leuD)
                 BB2817(leuC) BB2818(leuD) BB4085 BB4086
            RFR: Rfer_1794 Rfer_1795
            POL: Bpro_3608 Bpro_3609
            PNA: Pnap_3040
            AAV: Aave_1222
            AJS: Ajs_3232
            VEI: Veis_1048 Veis_1910 Veis_4656
            MPT: Mpe_A2163 Mpe_A2164
            HAR: HEAR0773(leuC2) HEAR0774(leuD2) HEAR1215(leuC) HEAR1216(leuD)
            MMS: mma_2170(leuD1) mma_2172(leuC1) mma_2343(leuC2)
                 mma_2344(leuD2)
            NEU: NE0685(leuC) NE0687(leuD)
            NET: Neut_1144 Neut_1146
            NMU: Nmul_A1919 Nmul_A1921
            EBA: ebA4757(leuC) ebA4758(leuD)
            AZO: azo1039(leuC) azo1040(leuD)
            DAR: Daro_0861 Daro_0863
            TBD: Tbd_1921 Tbd_1922
            MFA: Mfla_1704 Mfla_1705
            HHE: HH1135(leuD) HH1136(leuC)
            WSU: WS0559 WS1812(leuD-1)
            TDN: Tmden_1102 Tmden_2017
            CJE: Cj1716c(leuD) Cj1717c(leuC)
            CJR: CJE1886(leuD) CJE1887(leuC)
            CJJ: CJJ81176_0014(leuD) CJJ81176_0015(leuC)
            CJU: C8J_1622(leuD) C8J_1623(leuC)
            CJD: JJD26997_2092(leuD) JJD26997_2094(leuC)
            CFF: CFF8240_0195(leuC) CFF8240_1021
            CCV: CCV52592_0523 CCV52592_0608(leuC) CCV52592_0685
            CHA: CHAB381_0124(leuC) CHAB381_1265
            CCO: CCC13826_0035 CCC13826_2194(leuC)
            ABU: Abu_0079(leuC) Abu_1012(leuD)
            NIS: NIS_0726(leuD) NIS_1669(leuC)
            SUN: SUN_0147(leuC) SUN_1706(leuD)
            GSU: GSU1902 GSU1903
            GME: Gmet_1268 Gmet_1269
            GUR: Gura_3709
            PCA: Pcar_1905 Pcar_1906
            PPD: Ppro_0624 Ppro_1926
            DVU: DVU2982 DVU2983(leuD)
            DVL: Dvul_0390
            DDE: Dde_3219 Dde_3220
            DPS: DP1957 DP1958
            ADE: Adeh_1979 Adeh_1980
            AFW: Anae109_1875 Anae109_1876
            SAT: SYN_00091
            SFU: Sfum_2987 Sfum_2988 Sfum_3029 Sfum_3030
            PUB: SAR11_0251(leuD) SAR11_0252(leuC)
            MLO: mll4272 mll4408
            MES: Meso_3269 Meso_3448
            PLA: Plav_1423 Plav_1424
            SME: SMc03795(leuD) SMc03823(leuC)
            SMD: Smed_3028 Smed_3059
            ATU: Atu2709(leuC) Atu2790(leuD)
            ATC: AGR_C_4910 AGR_C_5065
            RET: RHE_CH03965(leuC) RHE_CH04091(leuD)
            RLE: RL4555 RL4705(leuD)
            BME: BMEI0157 BMEII0411
            BMF: BAB1_1905(leuC) BAB2_0353(leuD)
            BMS: BR1906(leuC) BRA0883(leuD)
            BMB: BruAb1_1882(leuC) BruAb2_0349(leuD)
            BOV: BOV_1834(leuC) BOV_A0827(leuD)
            OAN: Oant_0947 Oant_3297
            BJA: bll0415(leuD) bll0416(leuC) blr0488(leuC) blr0495(leuD)
            BRA: BRADO0365(leuD) BRADO0374(leuC) BRADO5516(leuC)
                 BRADO5517(leuD)
            BBT: BBta_0351(leuD) BBta_0363(leuC) BBta_5998(leuC)
                 BBta_5999(leuD)
            RPA: RPA0235(leuD) RPA0240(leuC)
            RPB: RPB_0342 RPB_0348
            RPC: RPC_0227 RPC_0230
            RPD: RPD_0498 RPD_0504
            RPE: RPE_0332 RPE_0339
            NWI: Nwi_2785 Nwi_2791(leuD)
            NHA: Nham_3584 Nham_3591
            XAU: Xaut_1180 Xaut_1185
            CCR: CC_0195 CC_0196
            SIL: SPO0215(leuD-1) SPO0216(leuC-1) SPO1476(leuC-2)
                 SPO1477(leuD-2)
            SIT: TM1040_2508 TM1040_2509
            RSP: RSP_0862(leuD) RSP_0863(leuC)
            RSH: Rsph17029_2521
            RSQ: Rsph17025_0158 Rsph17025_0159
            JAN: Jann_0123 Jann_0135
            RDE: RD1_0226(leuD) RD1_0616(leuC)
            PDE: Pden_2522
            MMR: Mmar10_0284 Mmar10_0285
            HNE: HNE_0047(leuC1) HNE_0052(leuD1) HNE_1078(leuD2)
                 HNE_1476(leuD) HNE_1477(leuC2)
            ZMO: ZMO0105(leuC) ZMO0106(leuD)
            NAR: Saro_1170 Saro_1173
            SAL: Sala_2129 Sala_2131
            SWI: Swit_2315 Swit_2316 Swit_4326 Swit_4327 Swit_4707
            ELI: ELI_03300 ELI_03310
            GOX: GOX0192 GOX0193
            GBE: GbCGDNIH1_1679 GbCGDNIH1_1680
            ACR: Acry_2149
            RRU: Rru_A1189 Rru_A1190
            MAG: amb4067 amb4068
            MGM: Mmc1_1779 Mmc1_1780
            ABA: Acid345_2915 Acid345_2916
            SUS: Acid_4069
            BSU: BG11949(leuC) BG11950(leuD)
            BHA: BH3055(leuD) BH3056(leuC)
            BAN: BA1422(leuC) BA1423(leuD)
            BAR: GBAA1422(leuC) GBAA1423(leuD)
            BAA: BA_1942 BA_1943
            BAT: BAS1313 BAS1314
            BCE: BC1402 BC1403
            BCA: BCE_1522(leuC) BCE_1523(leuD)
            BCZ: BCZK1287(leuC) BCZK1288(leuD)
            BCY: Bcer98_1125
            BTK: BT9727_1286(leuC) BT9727_1287(leuD)
            BLI: BL00613(leuC) BL00615(leuD)
            BLD: BLi02955(leuD) BLi02956(leuC)
            BCL: ABC2639(leuD) ABC2640(leuC)
            BAY: RBAM_025310(leuD) RBAM_025320(leuC)
            BPU: BPUM_2466(leuD) BPUM_2467(leuC)
            OIH: OB2617(leuD) OB2618(leuC)
            GKA: GK2655 GK2656
            GTN: GTNG_2585
            SAU: SA1864(leuC) SA1865(leuD)
            SAV: SAV2059(leuC) SAV2060(leuD)
            SAM: MW1983(leuC) MW1984(leuD)
            SAR: SAR2146(leuC) SAR2147(leuD)
            SAS: SAS1964 SAS1965
            SAC: SACOL2048(leuC) SACOL2049(leuD)
            SAB: SAB1944(leuC) SAB1945(leuD)
            SAA: SAUSA300_2012(leuC) SAUSA300_2013(leuD)
            SAO: SAOUHSC_02287 SAOUHSC_02288
            SAJ: SaurJH9_2096 SaurJH9_2097
            SAH: SaurJH1_2133 SaurJH1_2134
            SEP: SE1660 SE1661
            SER: SERP1671(leuC) SERP1672(leuD)
            SHA: SH0973(leuD) SH0974(leuC)
            SSP: SSP0818 SSP0819
            LMO: lmo1989(leuC) lmo1990(leuD)
            LMF: LMOf2365_2012(leuC) LMOf2365_2013(leuD)
            LIN: lin2096(leuC) lin2097(leuD)
            LWE: lwe2008(leuC) lwe2009(leuD)
            LLA: L0075(leuC) L0076(leuD)
            LLC: LACR_1317
            LLM: llmg_1282(leuD) llmg_1284(leuC)
            SPN: SP_1255
            SPR: spr1133
            SPD: SPD_1113
            SMU: SMU.1381(leuD) SMU.1382(leuC)
            STC: str1200(leuD) str1201(leuC)
            STL: stu1200(leuD) stu1201(leuC)
            SSA: SSA_0980(leuC) SSA_0981(leuD)
            SGO: SGO_0909(leuC) SGO_0910(leuD)
            OOE: OEOE_1725 OEOE_1726
            STH: STH2115 STH2116
            CAC: CAC3172(leuD) CAC3173(leuC)
            CTH: Cthe_2211
            CDF: CD0990(leuC) CD0991(leuD)
            CBE: Cbei_0214
            CKL: CKL_2158(leuD) CKL_2159(leuC)
            AMT: Amet_2963 Amet_3457
            CHY: CHY_0522(leuC) CHY_0523(leuD) CHY_1105
            DSY: DSY1369 DSY1370
            DRM: Dred_0286 Dred_2338
            SWO: Swol_0376 Swol_2141 Swol_2142
            CSC: Csac_1331
            TTE: TTE0017(leuC) TTE0018(leuD)
            MTA: Moth_2253 Moth_2254
            MTU: Rv2987c(leuD) Rv2988c(leuC)
            MTC: MT3065(leuD) MT3066(leuC)
            MBO: Mb3011c(leuD) Mb3012c(leuC)
            MBB: BCG_3008c(leuD) BCG_3009c(leuC)
            MLE: ML1684(leuD) ML1685(leuC)
            MPA: MAP2255 MAP2256 MAP3025c(leuD) MAP3026c(leuC)
            MAV: MAV_1739 MAV_1740 MAV_3837(leuD) MAV_3838(leuC)
            MSM: MSMEG_2387(leuC) MSMEG_2388(leuD) MSMEG_2504 MSMEG_2505
                 MSMEG_6853 MSMEG_6854
            MVA: Mvan_2136
            MGI: Mflv_4226
            MMC: Mmcs_1921 Mmcs_1922
            MKM: Mkms_1967 Mkms_1968
            MJL: Mjls_1901 Mjls_1902
            CGL: NCgl1262(cgl1315) NCgl1263(leuD)
            CGB: cg1487(leuC) cg1488(leuD)
            CEF: CE1427 CE1428
            CDI: DIP1127(leuC) DIP1128(leuD)
            CJK: jk1220(leuD) jk1221(leuC)
            NFA: nfa42110(leuD) nfa42120(leuC)
            RHA: RHA1_ro00726(leuD1) RHA1_ro00727(leuC1) RHA1_ro06499(leuC2)
                 RHA1_ro06500(leuD2)
            SCO: SCO5553(leuC) SCO5554(leuD)
            SMA: SAV2685(leuD) SAV2686(leuC)
            LXX: Lxx09660(leuC) Lxx09680(leuD)
            ART: Arth_2518 Arth_2519
            AAU: AAur_2485(leuD) AAur_2486(leuC)
            PAC: PPA1361 PPA1362 PPA1363
            NCA: Noca_3297
            TFU: Tfu_0626 Tfu_0627
            FRA: Francci3_3620 Francci3_3621
            FAL: FRAAL5828(leuD) FRAAL5829(leuC)
            ACE: Acel_1590 Acel_1591
            KRA: Krad_1358 Krad_1359
            SEN: SACE_6143(leuD) SACE_6144(leuC)
            STP: Strop_1258 Strop_1259
            BLO: BL1262(leuC) BL1263(leuD)
            BAD: BAD_0179(leuC) BAD_0180(leuD)
            RXY: Rxyl_0279 Rxyl_1693
            RBA: RB12656(leuA) RB12658(leuD)
            LIL: LA2095(leuC) LA2096(leuD)
            LIC: LIC11821(leuD) LIC11822(leuC)
            LBJ: LBJ_1912(leuD) LBJ_1913(leuC)
            LBL: LBL_1371(leuC) LBL_1372(leuD)
            SYN: sll1444(leuD) sll1470(leuC)
            SYW: SYNW0262(leuC) SYNW0263(leuD)
            SYC: syc1562_c(leuD) syc2197_d(leuC)
            SYF: Synpcc7942_1898 Synpcc7942_2548
            SYD: Syncc9605_0256 Syncc9605_0257
            SYE: Syncc9902_2087 Syncc9902_2088
            SYG: sync_0303(leuC) sync_0304(leuD)
            SYR: SynRCC307_2331(leuC) SynRCC307_2332(leuD)
            SYX: SynWH7803_0306(leuC) SynWH7803_0307(leuD)
            CYA: CYA_0286(leuC) CYA_2201(leuD)
            CYB: CYB_0327(leuC) CYB_2021(leuD)
            TEL: tlr0909(leuC) tlr1234
            GVI: glr3417(leuC) glr3418
            ANA: all1416(leuD) all1417(leuC)
            AVA: Ava_3966(leuD) Ava_3967
            PMA: Pro0287(leuD) Pro0288(leuC)
            PMM: PMM0255(leuD) PMM0256(leuC)
            PMT: PMT1843(leuD) PMT1844(leuC)
            PMN: PMN2A_1621 PMN2A_1622
            PMI: PMT9312_0257 PMT9312_0258
            PMB: A9601_02771(leuD) A9601_02781(leuC)
            PMC: P9515_02881(leuD) P9515_02891(leuC)
            PMF: P9303_24681(leuD) P9303_24691(leuC)
            PMG: P9301_02781(leuD) P9301_02791(leuC)
            PMH: P9215_02791(leuD) P9215_02801(leuC)
            PME: NATL1_03331(leuD) NATL1_03341(leuC)
            TER: Tery_2728
            BTH: BT_1859 BT_1860
            BFR: BF3446(leuD) BF3447(leuC)
            BFS: BF3265(leuD) BF3266(leuC)
            SRU: SRU_2150(leuC) SRU_2152(leuD)
            CHU: CHU_3742(leuC) CHU_3743(leuD)
            GFO: GFO_2096(leuC) GFO_2097(leuD)
            FJO: Fjoh_1306 Fjoh_1307
            CTE: CT0613 CT0614
            CCH: Cag_1899 Cag_1900
            CPH: Cpha266_0848
            PVI: Cvib_1175
            PLT: Plut_0600 Plut_0601
            DET: DET0448 DET0449 DET0827(leuD) DET0828(leuC)
            DEH: cbdb_A405 cbdb_A407 cbdb_A805(leuD) cbdb_A806(leuC)
            DEB: DehaBAV1_0425 DehaBAV1_0747
            RRS: RoseRS_1053 RoseRS_1960 RoseRS_1961
            RCA: Rcas_1549 Rcas_3474 Rcas_3516
            DRA: DR_1610 DR_1614 DR_1778 DR_1784
            DGE: Dgeo_1030 Dgeo_1032 Dgeo_1154 Dgeo_1156
            TTH: TTC0865 TTC0866 TTC1546 TTC1547
            TTJ: TTHA1228 TTHA1229 TTHA1910 TTHA1911
            AAE: aq_1398(leuD) aq_940(leuC)
            TMA: TM0291 TM0292 TM0554 TM0555
            TPT: Tpet_0366 Tpet_0621
            MJA: MJ0499(leuC) MJ1003(leuC) MJ1271(leuD) MJ1277(leuD)
            MMP: MMP0136(leuD) MMP0381 MMP1149(leuC) MMP1480
            MMQ: MmarC5_0436
            MMZ: MmarC7_0399 MmarC7_0724
            MAE: Maeo_0289 Maeo_0311
            MVN: Mevan_0471 Mevan_0789
            MAC: MA0202(leuD) MA1223(leuC) MA1393 MA3085(leuC) MA3751(leuD)
            MBA: Mbar_A0244 Mbar_A1338 Mbar_A1961 Mbar_A2167 Mbar_A2270
            MMA: MM_0409 MM_0645 MM_1490 MM_2373
            MBU: Mbur_1578 Mbur_1631 Mbur_1883 Mbur_2263
            MTP: Mthe_0788 Mthe_0990
            MHU: Mhun_1800 Mhun_2361 Mhun_2362
            MEM: Memar_0634 Memar_1949
            MBN: Mboo_0599 Mboo_2075
            MTH: MTH1386 MTH1387 MTH1631 MTH829
            MST: Msp_0374(leuD2) Msp_1100(leuC2) Msp_1485(leuD1)
                 Msp_1486(leuC1)
            MSI: Msm_0723 Msm_0847 Msm_1299 Msm_1300
            MKA: MK0781(leuD_1) MK1206(leuD_2) MK1208(leuC_2) MK1440(leuC_1)
            AFU: AF0629(leuD-1) AF1761(leuD-2) AF1963 AF2199(leuC)
            HMA: rrnAC0334(leuC) rrnAC0336(leuD)
            HWA: HQ2705A(leuC) HQ2706A(leuD)
            NPH: NP2192A(leuD) NP2194A(leuC)
            PTO: PTO0911 PTO0912 PTO1464 PTO1465
            PHO: PH1724 PH1726
            PAB: PAB0287(leuC-2) PAB0288(leuD-2) PAB0891(leuC-1)
                 PAB0892(leuD-1)
            PFU: PF0938 PF0939 PF1679 PF1680
            TKO: TK0281 TK0282
            RCI: RCIX2645(leuD-2) RCIX2646(leuC-2) RCIX990(leuC-1)
                 RCIX991(leuD-1) RRC265(leuC-3) RRC266(leuD-3)
            IHO: Igni_0931 Igni_1087
            SSO: SSO2470(leuD) SSO2471(leuC)
            STO: ST0599 ST0600
            SAI: Saci_0252(leuD) Saci_0253(leu2)
            PAI: PAE1984(leuC) PAE1991(leuD)
STRUCTURES  PDB: 1V7L  2HCU  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.33
            ExPASy - ENZYME nomenclature database: 4.2.1.33
            ExplorEnz - The Enzyme Database: 4.2.1.33
            ERGO genome analysis and discovery system: 4.2.1.33
            BRENDA, the Enzyme Database: 4.2.1.33
            CAS: 37290-72-5
///
ENTRY       EC 4.2.1.34                 Enzyme
NAME        (S)-2-methylmalate dehydratase;
            mesaconate hydratase;
            (+)-citramalate hydro-lyase;
            L-citramalate hydrolase;
            citramalate dehydratase;
            (+)-citramalic hydro-lyase;
            mesaconate mesaconase;
            mesaconase;
            (S)-2-methylmalate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (S)-2-methylmalate hydro-lyase (2-methylfumarate-forming)
REACTION    (S)-2-methylmalate = 2-methylfumarate + H2O [RN:R03693]
ALL_REAC    R03693
SUBSTRATE   (S)-2-methylmalate [CPD:C02614]
PRODUCT     2-methylfumarate [CPD:C01732];
            H2O [CPD:C00001]
COMMENT     Also hydrates fumarate to (S)-malate.
REFERENCE   1  [PMID:5903732]
  AUTHORS   Blair AH, Barker HA.
  TITLE     Assay and purification of (+)-citramalate hydro-lyase components
            from Clostridium tetanomorphum.
  JOURNAL   J. Biol. Chem. 241 (1966) 400-8.
  ORGANISM  Clostridium tetanomorphum
REFERENCE   2  [PMID:5769987]
  AUTHORS   Wang CC, Barker HA.
  TITLE     Purification and properties of L-citramalate hydrolyase.
  JOURNAL   J. Biol. Chem. 244 (1969) 2516-26.
  ORGANISM  Clostridium tetanomorphum
PATHWAY     PATH: map00660  C5-Branched dibasic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.34
            ExPASy - ENZYME nomenclature database: 4.2.1.34
            ExplorEnz - The Enzyme Database: 4.2.1.34
            ERGO genome analysis and discovery system: 4.2.1.34
            BRENDA, the Enzyme Database: 4.2.1.34
            CAS: 9027-94-5
///
ENTRY       EC 4.2.1.35                 Enzyme
NAME        (R)-2-methylmalate dehydratase;
            citraconate hydratase;
            citraconase;
            citramalate hydro-lyase;
            (-)-citramalate hydro-lyase;
            (R)-2-methylmalate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (R)-2-methylmalate hydro-lyase (2-methylmaleate-forming)
REACTION    (R)-2-methylmalate = 2-methylmaleate + H2O [RN:R03896]
ALL_REAC    R03896
SUBSTRATE   (R)-2-methylmalate [CPD:C02612]
PRODUCT     2-methylmaleate [CPD:C02226];
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+.
REFERENCE   1  [PMID:4296839]
  AUTHORS   Subramanian SS, Rao MR.
  TITLE     Purification and properties of citraconase.
  JOURNAL   J. Biol. Chem. 243 (1968) 2367-72.
  ORGANISM  Clostridium tetanomorphum, Pseudomonas fluorescens
PATHWAY     PATH: map00290  Valine, leucine and isoleucine biosynthesis
            PATH: map00660  C5-Branched dibasic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.35
            ExPASy - ENZYME nomenclature database: 4.2.1.35
            ExplorEnz - The Enzyme Database: 4.2.1.35
            ERGO genome analysis and discovery system: 4.2.1.35
            BRENDA, the Enzyme Database: 4.2.1.35
            CAS: 9027-92-3
///
ENTRY       EC 4.2.1.36                 Enzyme
NAME        homoaconitate hydratase;
            homoaconitase;
            cis-homoaconitase;
            HACN;
            Lys4;
            LysF;
            2-hydroxybutane-1,2,4-tricarboxylate hydro-lyase (incorrect)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate hydro-lyase
            [(Z)-but-1-ene-1,2,4-tricarboxylate-forming]
REACTION    (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate =
            (Z)-but-1-ene-1,2,4-tricarboxylate + H2O [RN:R03444]
ALL_REAC    R03444;
            (other) R04371
SUBSTRATE   (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate [CPD:C05662]
PRODUCT     (Z)-but-1-ene-1,2,4-tricarboxylate;
            H2O [CPD:C00001]
COMMENT     Requires a [4Fe-4S] cluster for activity. The enzyme from the
            hyperthermophilic eubacterium Thermus thermophilus can catalyse the
            reaction shown above but cannot catalyse the previously described
            reaction, i.e. formation of homocitrate by hydration of
            cis-homoaconitate. The enzyme responsible for the conversion of
            cis-homoaconitate into homocitrate in T. thermophilus is unknown at
            present but the reaction can be catalysed in vitro using aconitate
            hydratase from pig (EC 4.2.1.3) [2].
REFERENCE   1  [PMID:5954805]
  AUTHORS   Strassman M, Ceci LN.
  TITLE     Enzymatic formation of cis-homoaconitic acid, an intermediate in
            lysine biosynthesis in yeast.
  JOURNAL   J. Biol. Chem. 241 (1966) 5401-7.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:16524361]
  AUTHORS   Jia Y, Tomita T, Yamauchi K, Nishiyama M, Palmer DR.
  TITLE     Kinetics and product analysis of the reaction catalysed by
            recombinant homoaconitase from Thermus thermophilus.
  JOURNAL   Biochem. J. 396 (2006) 479-85.
REFERENCE   3  [PMID:10714900]
  AUTHORS   Zabriskie TM, Jackson MD.
  TITLE     Lysine biosynthesis and metabolism in fungi.
  JOURNAL   Nat. Prod. Rep. 17 (2000) 85-97.
PATHWAY     PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K01705  homoaconitate hydratase
GENES       SCE: YDR234W(LYS4)
            AGO: AGOS_ABL106C
            PIC: PICST_88705(LYS4)
            CGR: CAGL0K10978g
            SPO: SPAC343.16
            ANI: AN6521.2
            AFM: AFUA_5G08890
            AOR: AO090701000041
            CNE: CNK00580
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.36
            ExPASy - ENZYME nomenclature database: 4.2.1.36
            ExplorEnz - The Enzyme Database: 4.2.1.36
            ERGO genome analysis and discovery system: 4.2.1.36
            BRENDA, the Enzyme Database: 4.2.1.36
            CAS: 9030-68-6
///
ENTRY       EC 4.2.1.37       Obsolete  Enzyme
NAME        Transferred to 3.3.2.4
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
COMMENT     Transferred entry: now EC 3.3.2.4 trans-epoxysuccinate hydrolase (EC
            4.2.1.37 created 1972, deleted 1992)
STRUCTURES  PDB: 1DWO  1DWP  1DWQ  1E89  1E8D  1EB8  1EB9  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.37
            ExPASy - ENZYME nomenclature database: 4.2.1.37
            ExplorEnz - The Enzyme Database: 4.2.1.37
            ERGO genome analysis and discovery system: 4.2.1.37
            BRENDA, the Enzyme Database: 4.2.1.37
///
ENTRY       EC 4.2.1.38       Obsolete  Enzyme
NAME        Transferred to 4.3.1.20
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
COMMENT     Transferred entry: now EC 4.3.1.20 erythro-3-hydroxyaspartate
            ammonia-lyase (EC 4.2.1.38 created 1972, deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.38
            ExPASy - ENZYME nomenclature database: 4.2.1.38
            ExplorEnz - The Enzyme Database: 4.2.1.38
            ERGO genome analysis and discovery system: 4.2.1.38
            BRENDA, the Enzyme Database: 4.2.1.38
///
ENTRY       EC 4.2.1.39                 Enzyme
NAME        gluconate dehydratase;
            D-gluconate dehydratase;
            D-gluconate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     D-gluconate hydro-lyase (2-dehydro-3-deoxy-D-gluconate-forming)
REACTION    D-gluconate = 2-dehydro-3-deoxy-D-gluconate + H2O [RN:R01538]
ALL_REAC    R01538
SUBSTRATE   D-gluconate [CPD:C00257]
PRODUCT     2-dehydro-3-deoxy-D-gluconate [CPD:C00204];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:5383859]
  AUTHORS   Andreesen JR, Gottschalk G.
  TITLE     The occurrence of a modified Entner-doudoroff pathway in Clostridium
            aceticum.
  JOURNAL   Arch. Mikrobiol. 69 (1969) 160-70.
  ORGANISM  Clostridium aceticum
PATHWAY     PATH: map00030  Pentose phosphate pathway
ORTHOLOGY   KO: K05308  gluconate dehydratase
GENES       PTO: PTO0485
STRUCTURES  PDB: 1QJ4  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.39
            ExPASy - ENZYME nomenclature database: 4.2.1.39
            ExplorEnz - The Enzyme Database: 4.2.1.39
            ERGO genome analysis and discovery system: 4.2.1.39
            BRENDA, the Enzyme Database: 4.2.1.39
            CAS: 37290-75-8
///
ENTRY       EC 4.2.1.40                 Enzyme
NAME        glucarate dehydratase;
            D-glucarate dehydratase;
            D-glucarate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     D-glucarate hydro-lyase (5-dehydro-4-deoxy-D-glucarate-forming)
REACTION    D-glucarate = 5-dehydro-4-deoxy-D-glucarate + H2O [RN:R02752]
ALL_REAC    R02752
SUBSTRATE   D-glucarate [CPD:C00818]
PRODUCT     5-dehydro-4-deoxy-D-glucarate [CPD:C00679];
            H2O [CPD:C00001]
REFERENCE   1
  AUTHORS   Blumenthal, H.J.
  TITLE     D-Glucarate dehydrase.
  JOURNAL   Methods Enzymol. 9 (1966) 660-665.
  ORGANISM  Escherichia coli [GN:eco], Erwinia carotovora , Aerobacter aerogene
            , Escherichia freundii
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K01706  glucarate dehydratase
GENES       ANI: AN0613.2
            ECO: b2787(gudD) b2788(gudX)
            ECJ: JW2758(gudD) JW2759(gudX)
            ECE: Z4102(ygcX) Z4103(ygcY) Z4104
            ECS: ECs3647 ECs3648
            ECC: c3350(ygcX) c3352(ygcY)
            ECI: UTI89_C3157(gudD) UTI89_C3158(ygcY)
            ECP: ECP_2768 ECP_2769
            ECV: APECO1_3743(ygcY) APECO1_3744(gudD)
            STY: STY3098(ygcX) STY3099(ygcY)
            STT: t2869(ygcX) t2870(ygcY)
            SPT: SPA2825(ygcX)
            SEC: SC2900(gudD)
            STM: STM2960(gudD) STM2961(ygcY)
            SFL: SF2800(ygcX) SF2801(ygcY)
            SFX: S2994(ygcX) S2995(ygcY)
            SFV: SFV_2669(ygcY) SFV_2670(ygcX)
            SSN: SSON_2944(ygcX) SSON_2945(ygcY)
            SBO: SBO_2668(ygcX) SBO_2669(ygcY)
            ECA: ECA3575(gudD) ECA3576(gudX)
            SGL: SG0506
            ENT: Ent638_3240
            MSU: MS0689(dgoA)
            ASU: Asuc_1847
            XCC: XCC3242(tcbD)
            XCB: XC_0951
            PPU: PP_4757
            PPF: Pput_4631
            PST: PSPTO_2911 PSPTO_3285(gudD)
            PSB: Psyr_2716 Psyr_3120
            PSP: PSPPH_2467
            PFO: Pfl_3283 Pfl_3721
            PEN: PSEEN0731(gudD)
            PMY: Pmen_1214 Pmen_1216
            ACI: ACIAD0128(gudD)
            CSA: Csal_2481 Csal_2486
            RSO: RSc1079(gudD1) RSp0829(gudD2)
            REU: Reut_B3715
            REH: H16_B0127
            RME: Rmet_0834
            BXE: Bxe_B0539
            BVI: Bcep1808_0280
            BUR: Bcep18194_A3396 Bcep18194_A4275
            BCN: Bcen_2811
            BCH: Bcen2424_0295
            BAM: Bamb_0216 Bamb_1041
            BTE: BTH_I0189
            POL: Bpro_3421
            PNA: Pnap_1130
            AAV: Aave_3623
            AJS: Ajs_1990
            MPT: Mpe_A0970
            ATU: Atu3029(gudD)
            ATC: AGR_L_3551
            BJA: blr5872(gudD)
            BRA: BRADO1564(gudD)
            BBT: BBta_6488(gudD)
            ABA: Acid345_0645
            BSU: BG11161(ycbF)
            BLI: BL01649(gudD)
            BLD: BLi00287(ycbF)
            OIH: OB2836
            MSM: MSMEG_6117 MSMEG_6132
            MVA: Mvan_1017
            NFA: nfa35070
            RHA: RHA1_ro03792 RHA1_ro03934
            SCO: SCO2542(SCC77.09c)
            SMA: SAV5581(gudD)
            ART: Arth_0035
            SEN: SACE_0342 SACE_4841
STRUCTURES  PDB: 1BQG  1EC7  1EC8  1EC9  1ECQ  1JCT  1JDF  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.40
            ExPASy - ENZYME nomenclature database: 4.2.1.40
            ExplorEnz - The Enzyme Database: 4.2.1.40
            ERGO genome analysis and discovery system: 4.2.1.40
            BRENDA, the Enzyme Database: 4.2.1.40
            CAS: 9059-02-3
///
ENTRY       EC 4.2.1.41                 Enzyme
NAME        5-dehydro-4-deoxyglucarate dehydratase;
            5-keto-4-deoxy-glucarate dehydratase;
            5-keto-4-deoxy-glucarate dehydratase;
            deoxyketoglucarate dehydratase;
            D-4-deoxy-5-ketoglucarate hydro-lyase;
            5-dehydro-4-deoxy-D-glucarate hydro-lyase (decarboxylating)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     5-dehydro-4-deoxy-D-glucarate hydro-lyase (decarboxylating;
            2,5-dioxopentanoate-forming)
REACTION    5-dehydro-4-deoxy-D-glucarate = 2,5-dioxopentanoate + H2O + CO2
            [RN:R02279]
ALL_REAC    R02279
SUBSTRATE   5-dehydro-4-deoxy-D-glucarate [CPD:C00679]
PRODUCT     2,5-dioxopentanoate [CPD:C00433];
            H2O [CPD:C00001];
            CO2 [CPD:C00011]
REFERENCE   1  [PMID:4982840]
  AUTHORS   Jeffcoat R, Hassall H, Dagley S.
  TITLE     Purification and properties of D-4-deoxy-5-oxoglucarate hydro-lyase
            (decarboxylating).
  JOURNAL   Biochem. J. 115 (1969) 977-83.
  ORGANISM  Pseudomonas acidovorans
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K01707  5-dehydro-4-deoxyglucarate dehydratase
GENES       XCC: XCC3245(dapA)
            XCB: XC_0954
            PPU: PP_3599
            PST: PSPTO_4549
            PSB: Psyr_4227
            PSP: PSPPH_4252
            PFO: Pfl_0827
            PEN: PSEEN2658(kdgD)
            ACI: ACIAD0130(kdgD)
            ACB: A1S_1101
            CSA: Csal_2487
            RSO: RS05369(RSp0826)
            REU: Reut_B3688
            REH: H16_B0131
            RME: Rmet_4736
            BXE: Bxe_B1802
            BUR: Bcep18194_B0332
            BCN: Bcen_3049
            BCH: Bcen2424_5317
            BAM: Bamb_4676
            BTE: BTH_I0185
            POL: Bpro_3419
            PNA: Pnap_1596
            AAV: Aave_2587
            AJS: Ajs_1993
            SME: SMa1440
            ATU: Atu3140
            ATC: AGR_L_3338
            RET: RHE_CH02057(ypch00666)
            RLE: RL2335(kdgD) pRL120233 pRL120234
            BJA: blr5871
            BRA: BRADO1565(kdgD)
            BBT: BBta_6487(kdgD)
            RSP: RSP_3655
            RSH: Rsph17029_3393
            BSU: BG11158(ycbC)
            BLI: BL01645
            BLD: BLi00284(ycbC)
            BCL: ABC0471
            OIH: OB2841
            MSM: MSMEG_6133
            CGL: NCgl0438(cgl0453)
            CGB: cg0536
            NFA: nfa35040
            RHA: RHA1_ro03304 RHA1_ro03791
            SCO: SCO1895(SCI7.13c)
            SMA: SAV6360(dapA6)
            TFU: Tfu_1718
            SEN: SACE_0344(dapA) SACE_1971
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.41
            ExPASy - ENZYME nomenclature database: 4.2.1.41
            ExplorEnz - The Enzyme Database: 4.2.1.41
            ERGO genome analysis and discovery system: 4.2.1.41
            BRENDA, the Enzyme Database: 4.2.1.41
            CAS: 37290-77-0
///
ENTRY       EC 4.2.1.42                 Enzyme
NAME        galactarate dehydratase;
            D-galactarate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     D-galactarate hydro-lyase (5-dehydro-4-deoxy-D-glucarate-forming)
REACTION    D-galactarate = 5-dehydro-4-deoxy-D-glucarate + H2O [RN:R05608]
ALL_REAC    R05608
SUBSTRATE   D-galactarate [CPD:C00879]
PRODUCT     5-dehydro-4-deoxy-D-glucarate [CPD:C00679];
            H2O [CPD:C00001]
REFERENCE   1
  AUTHORS   Blumenthal, H.J. and Jepson, T.
  TITLE     Galactarate dehydrase.
  JOURNAL   Methods Enzymol. 9 (1966) 665-669.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K01708  galactarate dehydratase
GENES       ECO: b3128(garD)
            ECJ: JW3097(garD)
            ECE: Z4480(yhaG)
            ECS: ECs4006
            ECC: c3883(yhaG)
            ECI: UTI89_C3559(garD)
            ECP: ECP_3218
            ECV: APECO1_3299(garD)
            ECW: EcE24377A_3608(garD)
            ECX: EcHS_A3318(garD)
            STY: STY3432(garD)
            STT: t3170(garD)
            STM: STM3250(garD)
            SFL: SF3165(yhaG)
            SFX: S3380(yhaG)
            SSN: SSON_3283(yhaG)
            ECA: ECA3578(garD)
            ENT: Ent638_3570
            MSU: MS0695(uxaA)
            ASU: Asuc_1855
            XCC: XCC3240
            XCB: XC_0949
            PPU: PP_3601
            PPF: Pput_3100
            PST: PSPTO_4547(garD)
            PSB: Psyr_4225
            PSP: PSPPH_4250(garD)
            PFO: Pfl_0830
            PEN: PSEEN2656(garD)
            PMY: Pmen_1218
            ACI: ACIAD0126(garD)
            RSO: RSp0830(garD)
            REU: Reut_B3690
            REH: H16_A1258 H16_A1259 H16_B0965
            RME: Rmet_4734
            BXE: Bxe_B1801
            BVI: Bcep1808_3560
            BUR: Bcep18194_B0333
            BCN: Bcen_3050
            BCH: Bcen2424_5316
            BAM: Bamb_4675
            BTE: BTH_I0190
            RFR: Rfer_1027
            POL: Bpro_3104
            PNA: Pnap_1597
            AAV: Aave_2082 Aave_2595
            AJS: Ajs_1998
            VEI: Veis_1138 Veis_4262
            PUB: SAR11_0842(garD) SAR11_0843
            MES: Meso_3970
            ATU: Atu2822(garD)
            ATC: AGR_C_5115
            BME: BMEII0485
            BMF: BAB2_0431
            BMS: BRA0806
            BMB: BruAb2_0426
            OAN: Oant_3904
            BJA: blr5874(garD)
            BRA: BRADO1562(garD) BRADO2599
            BBT: BBta_2945 BBta_6490(garD)
            XAU: Xaut_0179 Xaut_1602
            RDE: RD1_0675(garD)
            PDE: Pden_4928
            ACR: Acry_1862
            SUS: Acid_1740
            BSU: BG11163(ycbH)
            BLI: BL01651(garD)
            BLD: BLi00289(ycbH)
            BAY: RBAM_012420(uxaA)
            RHA: RHA1_ro08847
            SEN: SACE_5173
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.42
            ExPASy - ENZYME nomenclature database: 4.2.1.42
            ExplorEnz - The Enzyme Database: 4.2.1.42
            ERGO genome analysis and discovery system: 4.2.1.42
            BRENDA, the Enzyme Database: 4.2.1.42
            CAS: 37290-78-1
///
ENTRY       EC 4.2.1.43                 Enzyme
NAME        2-dehydro-3-deoxy-L-arabinonate dehydratase;
            2-keto-3-deoxy-L-arabinonate dehydratase;
            2-dehydro-3-deoxy-L-arabinonate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     2-dehydro-3-deoxy-L-arabinonate hydro-lyase
            (2,5-dioxopentanoate-forming)
REACTION    2-dehydro-3-deoxy-L-arabinonate = 2,5-dioxopentanoate + H2O
            [RN:R02278]
ALL_REAC    R02278
SUBSTRATE   2-dehydro-3-deoxy-L-arabinonate [CPD:C00684]
PRODUCT     2,5-dioxopentanoate [CPD:C00433];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:5954356]
  AUTHORS   Stoolmiller AC, Abeles RH.
  TITLE     Formation of alpha-ketoglutaric semialdehyde from
            L-2-keto-3-deoxyarabonic acid and isolation of
            L-2-keto-3-deoxyarabonate dehydratase from Pseudomonas
            saccharophila.
  JOURNAL   J. Biol. Chem. 241 (1966) 5764-71.
  ORGANISM  Pseudomonas saccharophila
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.43
            ExPASy - ENZYME nomenclature database: 4.2.1.43
            ExplorEnz - The Enzyme Database: 4.2.1.43
            ERGO genome analysis and discovery system: 4.2.1.43
            BRENDA, the Enzyme Database: 4.2.1.43
            CAS: 37263-10-8
///
ENTRY       EC 4.2.1.44                 Enzyme
NAME        myo-inosose-2 dehydratase;
            inosose 2,3-dehydratase;
            ketoinositol dehydratase;
            2,4,6/3,5-pentahydroxycyclohexanone hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     2,4,6/3,5-pentahydroxycyclohexanone hydro-lyase
            (3,5/4-trihydroxycyclohexa-1,2-dione-forming)
REACTION    2,4,6/3,5-pentahydroxycyclohexanone =
            3,5/4-trihydroxycyclohexa-1,2-dione + H2O [RN:R02782]
ALL_REAC    R02782
SUBSTRATE   2,4,6/3,5-pentahydroxycyclohexanone [CPD:C00691]
PRODUCT     3,5/4-trihydroxycyclohexa-1,2-dione [CPD:C04287];
            H2O [CPD:C00001]
COFACTOR    Manganese [CPD:C00034];
            Cobalt [CPD:C00175]
COMMENT     Requires Co2+ or Mn2+.
REFERENCE   1  [PMID:5905122]
  AUTHORS   Berman T, Magasanik B.
  TITLE     The pathway of myo-inositol degradation in Aerobacter aerogenes.
            Dehydrogenation and dehydration.
  JOURNAL   J. Biol. Chem. 241 (1966) 800-6.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00562  Inositol phosphate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.44
            ExPASy - ENZYME nomenclature database: 4.2.1.44
            ExplorEnz - The Enzyme Database: 4.2.1.44
            ERGO genome analysis and discovery system: 4.2.1.44
            BRENDA, the Enzyme Database: 4.2.1.44
            CAS: 37290-79-2
///
ENTRY       EC 4.2.1.45                 Enzyme
NAME        CDP-glucose 4,6-dehydratase;
            cytidine diphosphoglucose oxidoreductase;
            CDP-glucose 4,6-hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     CDP-glucose 4,6-hydro-lyase
            (CDP-4-dehydro-6-deoxy-D-glucose-forming)
REACTION    CDP-glucose = CDP-4-dehydro-6-deoxy-D-glucose + H2O [RN:R02426]
ALL_REAC    R02426
SUBSTRATE   CDP-glucose [CPD:C00501]
PRODUCT     CDP-4-dehydro-6-deoxy-D-glucose [CPD:C01219];
            H2O [CPD:C00001]
COFACTOR    NAD+ [CPD:C00003]
COMMENT     Requires bound NAD+.
REFERENCE   1  [PMID:4380946]
  AUTHORS   Hey AE, Elbein AD.
  TITLE     Biosynthesis of tyvelose. The purification and properties of
            cytidine diphosphate D-glucose oxidoreductase.
  JOURNAL   J. Biol. Chem. 241 (1966) 5473-8.
  ORGANISM  Salmonella typhi
REFERENCE   2  [PMID:4288651]
  AUTHORS   Matsuhashi S, Matsuhashi M, Brown JG, Strominger JL.
  TITLE     Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. 3.
            Cytidine diphosphate D-glucose oxidoreductase.
  JOURNAL   J. Biol. Chem. 241 (1966) 4283-7.
  ORGANISM  Pasteurella pseudotuberculosis
REFERENCE   3  [PMID:4869560]
  AUTHORS   Melo A, Elliott WH, Glaser L.
  TITLE     The mechanism of 6-deoxyhexose synthesis. I. Intramolecular hydrogen
            transfer catalyzed by deoxythymidine diphosphate D-glucose
            oxidoreductase.
  JOURNAL   J. Biol. Chem. 243 (1968) 1467-74.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01709  CDP-glucose 4,6-dehydratase
GENES       STY: STY2301(rfbG)
            STT: t0781(rfbG)
            SPT: SPA0775(rfbG)
            STM: STM2091(rfbG)
            YPE: YPO3114(ddhB)
            YPK: y1069
            YPM: YP_0816(wcaG1)
            YPA: YPA_2606
            YPN: YPN_0975 YPN_0976
            YPS: YPTB1000(ddhB)
            YPI: YpsIP31758_3050(ddhB)
            YEN: YE3086(ddhB)
            ECA: ECA1423(rfbG)
            VFI: VF0183
            PSP: PSPPH_0958
            PFL: PFL_5095(rfbG)
            PFO: Pfl_1511
            SDN: Sden_2656
            PAT: Patl_3062
            TCX: Tcr_1689
            AHA: AHA_4165(rfbG)
            CVI: CV_3892(rfbG)
            BPS: BPSS0420(rfbG)
            BPM: BURPS1710b_A1962(rfbG)
            BPL: BURPS1106A_A0569(rfbG)
            BPD: BURPS668_A0663(rfbG)
            BTE: BTH_II1983(rfbG)
            RFR: Rfer_1251
            POL: Bpro_4010
            HAR: HEAR1134
            DAR: Daro_1257(capD)
            TBD: Tbd_1880
            SUN: SUN_2138
            PCA: Pcar_1131
            DVU: DVU0073
            DDE: Dde_3695
            BBA: Bd1665(rfbG)
            SAT: SYN_02648
            SME: SMb21417(ddhB)
            RLE: RL0245
            BJA: bll5979
            RPA: RPA4049(rfbG)
            RPE: RPE_4254
            BSU: BG12978(yfnG)
            BCE: BC3359 BC3517
            BCA: BCE_3396
            BCZ: BCZK3070(rfbG)
            LIL: LA1632(rfbG)
            LIC: LIC12151(rfbG)
            SYN: slr0984(rfbG)
            SYC: syc1441_d(rfbG)
            SYF: Synpcc7942_0061
            PMM: PMM1203(rfbG)
            PMC: P9515_07611(rfbG)
            PMF: P9303_01401(rfbG)
            BTH: BT_1350
            BFR: BF1536
            BFS: BF2602
STRUCTURES  PDB: 1RKX  1WVG  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.45
            ExPASy - ENZYME nomenclature database: 4.2.1.45
            ExplorEnz - The Enzyme Database: 4.2.1.45
            ERGO genome analysis and discovery system: 4.2.1.45
            BRENDA, the Enzyme Database: 4.2.1.45
            CAS: 37259-55-5
///
ENTRY       EC 4.2.1.46                 Enzyme
NAME        dTDP-glucose 4,6-dehydratase;
            thymidine diphosphoglucose oxidoreductase;
            TDP-glucose oxidoreductase;
            dTDP-glucose 4,6-hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     dTDP-glucose 4,6-hydro-lyase
            (dTDP-4-dehydro-6-deoxy-D-glucose-forming)
REACTION    dTDP-glucose = dTDP-4-dehydro-6-deoxy-D-glucose + H2O [RN:R06513]
ALL_REAC    R06513 > R02771
SUBSTRATE   dTDP-glucose [CPD:C00842]
PRODUCT     dTDP-4-dehydro-6-deoxy-D-glucose [CPD:C11907];
            H2O [CPD:C00001]
COFACTOR    NAD+ [CPD:C00003]
COMMENT     Requires bound NAD+.
REFERENCE   1  [PMID:14284740]
  AUTHORS   GILBERT JM, MATSUHASHI M, STROMINGER JL.
  TITLE     THYMIDINE DIPHOSPHATE 4-ACETAMIDO-4,6-DIDEOXYHEXOSES. II.
            PURIFICATION AND PROPERTIES OF THYMIDINE DIPHOSPHATE D-GLUCOSE
            OXIDOREDUCTASE.
  JOURNAL   J. Biol. Chem. 240 (1965) 1305-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4869560]
  AUTHORS   Melo A, Elliott WH, Glaser L.
  TITLE     The mechanism of 6-deoxyhexose synthesis. I. Intramolecular hydrogen
            transfer catalyzed by deoxythymidine diphosphate D-glucose
            oxidoreductase.
  JOURNAL   J. Biol. Chem. 243 (1968) 1467-74.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4307450]
  AUTHORS   Wang SF, Gabriel O.
  TITLE     Biological mechanisms involved in the formation of deoxy sugars. V.
            Isolation and crystallization of thymidine diphosphate-D-glucose
            oxidoreductase from Escherichia coli B.
  JOURNAL   J. Biol. Chem. 244 (1969) 3430-7.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
            PATH: map00521  Streptomycin biosynthesis
            PATH: map00523  Polyketide sugar unit biosynthesis
            PATH: map01055  Biosynthesis of vancomycin group antibiotics
ORTHOLOGY   KO: K01710  dTDP-glucose 4,6-dehydratase
GENES       HSA: 23483(TGDS)
            PTR: 467299(TGDS)
            MMU: 76355(Tgds)
            CFA: 485521(TGDS)
            GGA: 418793(TGDS)
            XLA: 495137(LOC495137)
            DME: Dmel_CG7979
            CEL: D2096.4(sqv-1) F53B1.4
            ATH: AT3G46440(UXS5) AT3G53520(UXS1)
            OSA: 4332424 4332425
            CME: CME136C CMJ313C CML007C CMM017C CMN006C CMQ006C
            PIC: PICST_43810(GAL102)
            SPO: SPBPB2B2.11
            AOR: AO090011000701
            DDI: DDB_0231748
            TCR: 503881.20 508119.120 509051.30 509965.380
            LMA: LmjF26.2230
            EHI: 11.t00065 116.t00006
            ECO: b2041(rfbB) b3788(rffG)
            ECJ: JW2026(rfbB) JW5598(rffG)
            ECE: Z5299(rffG)
            ECS: ECs4721
            ECC: c4708(rffG)
            ECI: UTI89_C2312(rfbB) UTI89_C4344(rffG)
            ECP: ECP_3979
            ECV: APECO1_1131(rfbB) APECO1_2687(rffG)
            ECW: EcE24377A_2332(rfbB2) EcE24377A_4299(rfbB1)
            ECX: EcHS_A2182(rfbB1) EcHS_A4005(rfbB2)
            STY: STY2307(rfbB) STY3633(rffG)
            STT: t0775(rfbB) t3375(rffG)
            SPT: SPA0767(wcaM) SPA0769(rfbB) SPA3762(rffG)
            SEC: SC3827(rffG)
            STM: STM2097(rfbB) STM3922(rffG)
            YPE: YPO3862(rffG)
            YPK: y0366(rffG)
            YPM: YP_3183(rffG)
            YPA: YPA_0156
            YPN: YPN_0101
            YPS: YPTB0172(rffG)
            YPI: YpsIP31758_0186(rfbB)
            SFL: SF2104(rfbB) SF3862(rffG)
            SFX: S2227(rfbB) S3898(rffG)
            SFV: SFV_2098(rfbB) SFV_3716(rffG)
            SSN: SSON_3960(rffG)
            SBO: SBO_0868(rfbB) SBO_3799(rffG)
            SDY: SDY_2204(rfbB)
            ECA: ECA4206(rffG)
            PLU: plu4658(rffG)
            SGL: SG2381
            HIN: HI0873(rffG)
            HIT: NTHI1037(rmlB)
            HDU: HD0687(rmlB)
            HSO: HS_0707(rmlB)
            PMU: PM1030(rffG)
            MSU: MS1593(rfbB)
            APL: APL_1472(rfbB1)
            XFA: XF0255 XF0611
            XFT: PD0208(rfbB) PD1543(rfbB)
            XCC: XCC0621(rmlB)
            XCB: XC_3613
            XCV: XCV3709(rmlB)
            XAC: XAC3585(rmlB)
            XOO: XOO0792(rmlB)
            XOM: XOO_0720(XOO0720)
            VVY: VV0300
            VPA: VP0222
            VFI: VF0166 VF0186
            PAE: PA5161(rmlB)
            PAU: PA14_68170(rmlB)
            PAP: PSPA7_5900(rfbB)
            PPU: PP_1785(rmlB)
            PST: PSPTO_1081(rfbB-1) PSPTO_5396(rfbB-2)
            PSB: Psyr_0926 Psyr_4935
            PSP: PSPPH_0150(rfbB1) PSPPH_0969(rfbB2)
            PFL: PFL_0305(rfbB)
            PFO: Pfl_0701 Pfl_4058
            PEN: PSEEN0253(rmlB) PSEEN4745(rmlB-2)
            PAR: Psyc_1212(rffG)
            PCR: Pcryo_0624
            ACI: ACIAD0076(rmlB)
            SON: SO_3167 SO_3188(rfbB)
            SDN: Sden_2663
            SFR: Sfri_2760 Sfri_2830
            SHE: Shewmr4_1318
            SHM: Shewmr7_1399
            SHN: Shewana3_1379
            SHW: Sputw3181_1473
            ILO: IL0541(rffG)
            PAT: Patl_2132
            SDE: Sde_2131
            LPN: lpg0758(rfbB)
            LPF: lpl0795(rmlB)
            LPP: lpp0824(rmlB)
            MCA: MCA1165 MCA1282(rfbB)
            FTU: FTT1450c(wbtM) FTT1464c(wbtA)
            FTF: FTF1450c(wbtM) FTF1464c(wbtA)
            FTW: FTW_0426(wbtM)
            FTL: FTL_0592 FTL_0606
            FTH: FTH_0592
            FTA: FTA_0640(rfbB)
            FTN: FTN_1431(wbtA)
            TCX: Tcr_1462
            NOC: Noc_0773
            AEH: Mlg_2317
            HCH: HCH_02406(rfbB)
            ABO: ABO_0910(rmlB)
            AHA: AHA_2908(rfbB)
            NME: NMB0063 NMB0079
            NMA: NMA0189(rfbB2) NMA0204(rfbB)
            NMC: NMC0047(rfbB) NMC0063(rfbB2)
            NGO: NGO1897
            CVI: CV_4010(rmlB)
            RSO: RSc0682(rfbB)
            REU: Reut_A0712 Reut_B4391
            REH: H16_A0369(rfbB1) H16_A1851(rfbB2) H16_A2909 H16_B1642
            RME: Rmet_2735
            BMA: BMA1990(rfbB) BMAA1978
            BMV: BMASAVP1_A0923(rfbB)
            BML: BMA10299_A2753(rfbB)
            BMN: BMA10247_1852(rfbB)
            BXE: Bxe_A3727 Bxe_A3803 Bxe_B1714
            BUR: Bcep18194_A3969 Bcep18194_B0868
            BCN: Bcen_0389
            BCH: Bcen2424_0871
            BAM: Bamb_0751 Bamb_3383
            BPS: BPSL2686(rmlB) BPSS2245
            BPM: BURPS1710b_3163(rfbB) BURPS1710b_A1378(rfbB)
            BPL: BURPS1106A_3141(rfbB)
            BPD: BURPS668_3105(rfbB)
            BTE: BTH_I1469(rfbB)
            BPE: BP0109(rfbB)
            BPA: BPP0173(rfbB)
            BBR: BB0175(rfbB)
            RFR: Rfer_0715
            POL: Bpro_4022
            MPT: Mpe_A0628
            HAR: HEAR1152(rfbB)
            MMS: mma_2253(rfbB)
            NEU: NE0469(rmlB)
            NET: Neut_2400
            NMU: Nmul_A0264
            EBA: ebA1518(rffG) ebA2278(rmlB)
            AZO: azo0026(acbB) azo1802 azo1877(rmlB)
            DAR: Daro_1237
            TBD: Tbd_1780
            MFA: Mfla_2008
            HHE: HH0099 HH0647
            TDN: Tmden_0179
            CCV: CCV52592_0304(rfbB)
            ABU: Abu_0660 Abu_0696(pglF) Abu_1816
            SUN: SUN_1552
            GSU: GSU1815 GSU2366(rfbB)
            GME: Gmet_1431 Gmet_2473
            PCA: Pcar_2251 Pcar_2593
            DVU: DVU1364(rfbB) DVU2455
            DDE: Dde_2182 Dde_3060
            LIP: LI1066(rfbB)
            BBA: Bd1869(rmlB)
            DPS: DP0045 DP2220
            ADE: Adeh_4288
            MXA: MXAN_4613(rfbB)
            SAT: SYN_01130 SYN_02866
            SFU: Sfum_2264
            PUB: SAR11_0541(rfbB)
            MLO: mll7879 mlr7552
            MES: Meso_2762 Meso_2774
            SME: SMb20239(rmlB) SMb20458 SMb21326(expA9)
            ATU: Atu3316 Atu4617(rffB)
            ATC: AGR_L_3008 AGR_L_530
            RET: RHE_CH00068 RHE_CH01360(ypch00464) RHE_CH01514(rffB)
                 RHE_PB00058(rmlB)
            RLE: RL0077 RL0560 RL1625(rfbB) pRL90147
            BME: BMEII0440 BMEII0731
            BMF: BAB2_0384 BAB2_0695
            BMS: BRA0542 BRA0852
            BMB: BruAb2_0379 BruAb2_0680
            BJA: blr5423 blr6004
            BRA: BRADO2062 BRADO5168 BRADO7029(rfbB)
            BBT: BBta_1071(rfbB) BBta_5635
            RPA: RPA0117 RPA0173 RPA3925 RPA4053
            RPB: RPB_0262 RPB_1562 RPB_3810
            RPC: RPC_4166 RPC_4187
            RPD: RPD_0562 RPD_1571
            RPE: RPE_0275 RPE_1098 RPE_1516 RPE_2674 RPE_3495
            NWI: Nwi_0544 Nwi_2406
            NHA: Nham_1058 Nham_3054
            CCR: CC_1146 CC_3629
            SIT: TM1040_3861
            RSP: RSP_0160 RSP_0514 RSP_3844(rffG)
            JAN: Jann_3843
            RDE: RD1_B0019(rfbB)
            MMR: Mmar10_2456
            HNE: HNE_0790(rfbB)
            GOX: GOX1053
            GBE: GbCGDNIH1_0102
            RRU: Rru_A0935 Rru_A3252 Rru_B0050
            MAG: amb0058 amb0139
            MGM: Mmc1_1405 Mmc1_1535
            BSU: BG10618(spsJ)
            BHA: BH3364(spsJ)
            BAN: BA1230(rfbB)
            BAR: GBAA1230(rfbB)
            BAA: BA_1765
            BAT: BAS1137
            BCE: BC1214
            BCA: BCE_1337(rfbB)
            BCZ: BCZK1111(rfbB)
            BTK: BT9727_1117(rfbB)
            BTL: BALH_1077(rfbB)
            BCL: ABC3689(spsJ)
            BPU: BPUM_3226(rfbB) BPUM_3428(spsJ)
            OIH: OB2420
            GKA: GK3128
            LMO: lmo1083
            LLA: L199221(rmlB)
            LLC: LACR_0204
            LLM: llmg_0209(rmlB)
            SPY: SPy_0936(cpsFQ)
            SPZ: M5005_Spy_0736(cpsFQ)
            SPM: spyM18_0993(cpsFQ)
            SPG: SpyM3_0648(rmlB)
            SPS: SPs1204
            SPH: MGAS10270_Spy0795(cpsFQ)
            SPI: MGAS10750_Spy0830(cpsFQ)
            SPJ: MGAS2096_Spy0811(cpsFQ)
            SPK: MGAS9429_Spy0794(cpsFQ)
            SPF: SpyM51071(rmlB)
            SPA: M6_Spy0762
            SPB: M28_Spy0716(cpsFQ)
            SPR: spr0322(cpsN)
            SPD: SPD_0330(rfbB)
            SAG: SAG1198(rfbB)
            SAN: gbs1271
            SAK: SAK_1285(rfbB)
            SMU: SMU.1457(rmlB)
            STC: str1242(rmlB)
            STL: stu1242(rmlB)
            SSA: SSA_1409(rmlB)
            SGO: SGO_1011(rfbB-1) SGO_2016 SGO_2024
            LPL: lp_1189(rfbB)
            LJO: LJ1049
            LSA: LSA1495(rfbB)
            LSL: LSL_1570(rfbB)
            LBU: LBUL_1838
            LCA: LSEI_2013 LSEI_2054
            EFA: EF2192(rfbB)
            OOE: OEOE_1447
            CAC: CAC2332(spsJ)
            CPE: CPE0619(rfbB)
            CPF: CPF_0482(rfbB) CPF_0600(rfbB)
            CTH: Cthe_1086
            CBA: CLB_1995(rfbB)
            CBH: CLC_2000(rfbB)
            CBF: CLI_2116(rfbB)
            CKL: CKL_2474(rfbB)
            CHY: CHY_0979(rfbB)
            DSY: DSY3316 DSY4440
            MTA: Moth_0751
            MTU: Rv3464(rmlB) Rv3468c Rv3784
            MTC: MT3570(rfbB)
            MBO: Mb3493(rmlB1) Mb3497c(rmlB2) Mb3813(rfbB)
            MBB: BCG_3529(rmlB1) BCG_3533c(rmlB2) BCG_3846(rfbB)
            MLE: ML1964(rmlB)
            MPA: MAP3248 MAP4225c(rmlB)
            MAV: MAV_4406(rfbB)
            MSM: MSMEG_1512(rfbB)
            MMC: Mmcs_1066
            CGL: NCgl0327(cgl0334)
            CGB: cg0391(rmlB2) cg0403(rmlB1) cg0417(capD)
            CEF: CE0344
            CDI: DIP0362(rmlB)
            CJK: jk1888(rmlB)
            NFA: nfa2100(rfbB)
            RHA: RHA1_ro04098
            SCO: SCO0749(SCF81.08c) SCO6179(SC6C5.15)
            SMA: SAV946(aveBII)
            TWH: TWT030(rmlB)
            TWS: TW033
            LXX: Lxx04910
            CMI: CMM_1010(rmlB)
            AAU: AAur_2165(rfbB) AAur_3160(rfbB)
            FRA: Francci3_1294 Francci3_1669 Francci3_3551
            FAL: FRAAL4549(strE) FRAAL5661(capD) FRAAL5662 FRAAL5747(rfbB)
            ACE: Acel_0415
            SEN: SACE_5581 SACE_6480(aveBII)
            BLO: BL0229(rmlB1) BL1244(rmlB2)
            BAD: BAD_1495(rmlB1) BAD_1507(rmlB1)
            RXY: Rxyl_3122
            FNU: FN1299 FN1667
            RBA: RB2507(rfbB) RB3733
            PCU: pc0126(rfbB)
            TDE: TDE1441(rfbB)
            LIL: LA0051 LA0235(rfbB1) LA1606(rfbB3) LA1661(rfbB4)
            LIC: LIC12124(rfbB)
            LBJ: LBJ_1183(rmlB)
            LBL: LBL_1237(rmlB)
            SYN: slr0809(rfbB) slr0836(rfbB)
            SYW: SYNW0198 SYNW0646(rfbB)
            SYC: syc0401_d(rfbB) syc1993_c(rfbB)
            SYF: Synpcc7942_1149 Synpcc7942_2100
            SYD: Syncc9605_0189 Syncc9605_2035
            SYE: Syncc9902_0634
            SYG: sync_0159(rfbB) sync_1724
            SYR: SynRCC307_0084(rfbB)
            SYX: SynWH7803_0107(rfbB) SynWH7803_0192(rfbB)
            CYA: CYA_0484
            CYB: CYB_1929
            TEL: tll0458(rfbB) tll0665(rfbB)
            GVI: gll2179(rfbB) gll3773(rfbB) glr0468(rfbB) glr3235(rfbB)
            ANA: alr0038(rfbB) alr0657(rfbB)
            AVA: Ava_2639 Ava_4588
            PMA: Pro1313(wcaG)
            PMM: PMM1257 PMM1260
            PMT: PMT0115(rfbB) PMT1958(rfbB)
            PMN: PMN2A_1236 PMN2A_1680
            PMB: A9601_13971 A9601_13991(gmd) A9601_14531(rfbB)
            PMC: P9515_01521(rfbB) P9515_07621 P9515_13681(gmd) P9515_13711
                 P9515_13721 P9515_14221
            PMF: P9303_01011 P9303_01131 P9303_01181(rfbB) P9303_25381
                 P9303_26091
            PMG: P9301_13991 P9301_14001 P9301_14111(rfbB) P9301_14441(gmd)
            PMH: P9215_14531(rfbB)
            PME: NATL1_03941 NATL1_03951 NATL1_08571(rfbB) NATL1_20961(gmd)
            TER: Tery_0957
            BTH: BT_0466 BT_1059 BT_2016
            BFR: BF0807 BF2132 BF3711
            BFS: BF2189 BF3504(rffG)
            PGI: PG1560(rfbB)
            SRU: SRU_0588(rfbB)
            CHU: CHU_0850(rfbB) CHU_0900 CHU_3391(rfbB) CHU_3393(rfbB)
            GFO: GFO_2037(rfbB)
            FPS: FP1294(rmlB)
            CTE: CT0308(rfbB)
            CCH: Cag_0516 Cag_0671
            PLT: Plut_0419
            DRA: DR_A0041
            DGE: Dgeo_2650
            MJA: MJ1055
            MAC: MA2186 MA3779(rfbB)
            MBA: Mbar_A0231
            MMA: MM_1167 MM_1191 MM_1193
            MHU: Mhun_2118 Mhun_3072 Mhun_3100
            MTH: MTH373
            MST: Msp_1114
            MSI: Msm_1309
            HMA: rrnAC1010(rfbB1) rrnAC1011(rffG) rrnAC1572(rfbB2)
                 rrnAC2178(rfbB3)
            TVO: TVN0902
            PTO: PTO0310 PTO0312
            PAB: PAB0785(rfbB)
            PFU: PF1357
            RCI: LRC285(rfbB-3) LRC553(rfbB-2) RCIX200(rfbB-1)
            APE: APE_1180
            SSO: SSO0830(rfbB-1) SSO1734(rfbB-2) SSO1781(rfbB-3)
            STO: ST1972
            SAI: Saci_1704
STRUCTURES  PDB: 1BXK  1G1A  1KEP  1KER  1KET  1KEU  1KEW  1OC2  1R66  1R6D  
                 2HUN  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.46
            ExPASy - ENZYME nomenclature database: 4.2.1.46
            ExplorEnz - The Enzyme Database: 4.2.1.46
            ERGO genome analysis and discovery system: 4.2.1.46
            BRENDA, the Enzyme Database: 4.2.1.46
            CAS: 37259-54-4
///
ENTRY       EC 4.2.1.47                 Enzyme
NAME        GDP-mannose 4,6-dehydratase;
            guanosine 5'-diphosphate-D-mannose oxidoreductase;
            guanosine diphosphomannose oxidoreductase;
            guanosine diphosphomannose 4,6-dehydratase;
            GDP-D-mannose dehydratase;
            GDP-D-mannose 4,6-dehydratase;
            Gmd;
            GDP-mannose 4,6-hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     GDP-mannose 4,6-hydro-lyase
            (GDP-4-dehydro-6-deoxy-D-mannose-forming)
REACTION    GDP-mannose = GDP-4-dehydro-6-deoxy-D-mannose + H2O [RN:R00888]
ALL_REAC    R00888
SUBSTRATE   GDP-mannose [CPD:C00096]
PRODUCT     GDP-4-dehydro-6-deoxy-D-mannose [CPD:C01222];
            H2O [CPD:C00001]
COFACTOR    NAD+ [CPD:C00003]
COMMENT     The bacterial enzyme requires bound NAD+. This enzyme forms the
            first step in the biosynthesis of GDP-D-rhamnose and GDP-L-fucose.
            In Aneurinibacillus thermoaerophilus L420-91T, this enzyme acts as a
            bifunctional enzyme, catalysing the above reaction as well as the
            reaction catalysed by EC 1.1.1.281, GDP-4-dehydro-6-deoxy-D-mannose
            reductase [5]. Belongs to the short-chain dehydrogenase/reductase
            enzyme family, having homologous structures and a conserved
            catalytic triad of Lys, Tyr and Ser/Thr residues [6].
REFERENCE   1  [PMID:14299611]
  AUTHORS   ELBEIN AD, HEATH EC.
  TITLE     THE BIOSYNTHESIS OF CELL WALL LIPOPOLYSACCHARIDE IN ESCHERICHIA
            COLI. II. GUANOSINE DIPHOSPHATE 4-KETO-6-DEOXY-D-MANNOSE, AN
            INTERMEDIATE IN THE BIOSYNTHESIS OF GUANOSINE DIPHOSPHATE COLITOSE.
  JOURNAL   J. Biol. Chem. 240 (1965) 1926-31.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:5047712]
  AUTHORS   Liao TH, Barber GA.
  TITLE     Purification of guanosine 5'-diphosphate D-mannose oxidoreductase
            from Phaseolus vulgaris.
  JOURNAL   Biochim. Biophys. Acta. 276 (1972) 85-93.
  ORGANISM  Phaseolus vulgaris
REFERENCE   3  [PMID:4869560]
  AUTHORS   Melo A, Elliott WH, Glaser L.
  TITLE     The mechanism of 6-deoxyhexose synthesis. I. Intramolecular hydrogen
            transfer catalyzed by deoxythymidine diphosphate D-glucose
            oxidoreductase.
  JOURNAL   J. Biol. Chem. 243 (1968) 1467-74.
REFERENCE   4  [PMID:9525924]
  AUTHORS   Sullivan FX, Kumar R, Kriz R, Stahl M, Xu GY, Rouse J, Chang XJ,
            Boodhoo A, Potvin B, Cumming DA.
  TITLE     Molecular cloning of human GDP-mannose 4,6-dehydratase and
            reconstitution of GDP-fucose biosynthesis in vitro.
  JOURNAL   J. Biol. Chem. 273 (1998) 8193-202.
  ORGANISM  human [GN:hsa]
REFERENCE   5  [PMID:11096116]
  AUTHORS   Kneidinger B, Graninger M, Adam G, Puchberger M, Kosma P, Zayni S,
            Messner P.
  TITLE     Identification of two GDP-6-deoxy-D-lyxo-4-hexulose reductases
            synthesizing GDP-D-rhamnose in Aneurinibacillus thermoaerophilus
            L420-91T.
  JOURNAL   J. Biol. Chem. 276 (2001) 5577-83.
  ORGANISM  Aneurinibacillus thermoaerophilus
REFERENCE   6  [PMID:12501186]
  AUTHORS   Mulichak AM, Bonin CP, Reiter WD, Garavito RM.
  TITLE     Structure of the MUR1 GDP-mannose 4,6-dehydratase from Arabidopsis
            thaliana: implications for ligand binding and specificity.
  JOURNAL   Biochemistry. 41 (2002) 15578-89.
  ORGANISM  Arabidopsis thaliana [GN:ath]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K01711  GDPmannose 4,6-dehydratase
GENES       HSA: 2762(GMDS)
            PTR: 462390(GMDS)
            MMU: 218138(Gmds)
            CFA: 488189(GMDS)
            GGA: 420890(GMDS)
            XLA: 380044(gmds) 444039(MGC82624)
            SPU: 588885(LOC588885)
            DME: Dmel_CG8890(Gmd)
            CEL: C53B4.7(bre-1) F56H6.5(gmd-2)
            ATH: AT3G51160(MUR1) AT5G66280(GMD1)
            OSA: 4340050
            AFM: AFUA_7G06990
            PFA: PF08_0077
            TBR: Tb10.61.0880
            TCR: 510027.10
            ECO: b2053(gmd)
            ECJ: JW2038(gmd)
            ECE: Z3198 Z3217(gmd)
            ECS: ECs2839 ECs2858
            ECC: c2579(gmd)
            ECI: UTI89_C2327(gmd)
            ECP: ECP_2093
            ECV: APECO1_1143(gmd)
            ECW: EcE24377A_2346(gmd)
            STY: STY2321(gmd)
            STT: t0763(gmd)
            SPT: SPA0757(gmd)
            SEC: SC2110(gmd)
            STM: STM2109(gmd)
            YPA: YPA_2596
            YPN: YPN_0986
            YPP: YPDSF_2740
            YPS: YPTB1009(gmd)
            YPI: YpsIP31758_3041(gmd)
            YEN: YE3075(gmd)
            SFL: SF2116(gmd)
            SFX: S2239(gmd)
            SFV: SFV_2110(gmd)
            SSN: SSON_2106(gmd)
            SBO: SBO_0880(gmd)
            SGL: SG0331
            XFA: XF0609
            XFT: PD1545(gmd)
            XCC: XCC0606
            XCB: XC_3627
            XCV: XCV3718(gmd)
            VCH: VC0243
            VCO: VC0395_A2623(gmd)
            VVY: VV0349
            PAE: PA5453(gmd)
            PAU: PA14_71990(gmd)
            PAP: PSPA7_6243(gmd)
            PPU: PP_1799(gmd)
            PST: PSPTO_1005(gmd)
            PSB: Psyr_0916
            PSP: PSPPH_0953(gmd)
            PFL: PFL_5491(gmd)
            PFO: Pfl_5682
            CPS: CPS_4199(gmd)
            SDE: Sde_2117
            CBU: CBU_0689(gmd)
            CBD: COXBU7E912_0703(gmd)
            MCA: MCA1146(gmd)
            TCX: Tcr_1680
            NOC: Noc_1523
            AHA: AHA_2902(gmd)
            REU: Reut_A0719
            REH: H16_A2900
            RME: Rmet_5860
            BMA: BMA2297 BMAA1709(gmd)
            BMV: BMASAVP1_1660(gmd)
            BML: BMA10299_1868(gmd)
            BMN: BMA10247_A0540(gmd)
            BXE: Bxe_A2234 Bxe_A3863 Bxe_C1085
            BUR: Bcep18194_B2115 Bcep18194_B2116
            BCN: Bcen_0400 Bcen_4397
            BCH: Bcen2424_0880 Bcen2424_3970
            BAM: Bamb_0759 Bamb_3358
            BPS: BPSL2797(wcbK) BPSS1688(gca)
            BPM: BURPS1710b_3293(wcbK) BURPS1710b_A0758(gmd)
            BPL: BURPS1106A_A2295(gmd)
            BPD: BURPS668_A2434(gmd)
            BTE: BTH_I1331(gmd-1) BTH_II0690(gmd-2)
            RFR: Rfer_1237
            POL: Bpro_4012
            MPT: Mpe_A2731
            NET: Neut_0156
            AZO: azo3587(gmd)
            TBD: Tbd_1776
            MFA: Mfla_1271
            HPY: HP0044(rfbD)
            HPA: HPAG1_0041
            HHE: HH0172(gmd)
            HAC: Hac_0056(gmd)
            TDN: Tmden_1704
            CJR: CJE1611(wcbK)
            CJJ: CJJ81176_1426(wcbK)
            NIS: NIS_1386(gmd)
            SUN: SUN_0342(gmd)
            GSU: GSU0626(gmd)
            GME: Gmet_1311 Gmet_1488
            DVU: DVU0448(gmd)
            DDE: Dde_0432 Dde_2901
            LIP: LIC082(gmd)
            DPS: DP0025
            ADE: Adeh_4287
            MXA: MXAN_5327(gmd)
            SAT: SYN_00584
            SFU: Sfum_3362
            PUB: SAR11_0176(gmdA) SAR11_0570(gmd)
            MLO: mll5922 mlr5849
            ATU: Atu4789(gmd)
            ATC: AGR_L_187
            RET: RHE_CH00762(noeL1) RHE_CH01350(noeL2)
            RLE: RL0825(gmd) pRL90133
            BME: BMEI1413 BMEI1418 BMEII0848
            BMF: BAB1_0540 BAB1_0545(gmd)
            BMS: BR0522(gmd) BRA0419
            BMB: BruAb1_0545(gmd)
            BOV: BOV_0526(gmd-2) BOV_A0362(gmd-1)
            BJA: bll1631(noeL) bll5465(gmd)
            BRA: BRADO2185(gmd) BRADO5260(gmd)
            BBT: BBta_5712(gmd)
            RPA: RPA3951(gmd)
            RPB: RPB_1525
            RPD: RPD_1647
            RPE: RPE_4261
            NWI: Nwi_2385
            NHA: Nham_2780
            CCR: CC_1010
            SIT: TM1040_1482
            RSP: RSP_4109(gmd)
            JAN: Jann_4280
            HNE: HNE_0793(gmd)
            ELI: ELI_13420
            GOX: GOX1612
            GBE: GbCGDNIH1_2354
            RRU: Rru_A0253
            MAG: amb1077
            MGM: Mmc1_1429
            ABA: Acid345_3814
            CAC: CAC2180
            MTU: Rv0112(gca) Rv1511(gmdA)
            MTC: MT0121 MT1561(gmd)
            MBO: Mb0116(gca)
            MBB: BCG_0145(gca)
            MPA: MAP1231(gmdA)
            MMC: Mmcs_0945
            RHA: RHA1_ro05444
            CMI: CMM_1600(gmdA)
            AAU: AAur_4113(gmd)
            FRA: Francci3_1053 Francci3_1307
            FAL: FRAAL1776(gmd)
            ACE: Acel_0449
            RXY: Rxyl_0567
            RBA: RB2512 RB2518
            LIL: LA3964
            LIC: LIC13168(gmd)
            LBJ: LBJ_0410(gmd)
            LBL: LBL_2667(gmd)
            SYN: sll1212(gmd) slr1072(yefA)
            SYW: SYNW0422(gmd)
            SYC: syc0211_c
            SYF: Synpcc7942_1342
            SYE: Syncc9902_0174
            SYG: sync_0146(gmd)
            SYR: SynRCC307_0217(gmd)
            SYX: SynWH7803_0114(gmd)
            CYA: CYA_1520(gmd)
            CYB: CYB_1095(gmd)
            TEL: tll0634
            GVI: gll0763 gll0764
            ANA: all4828 alr3424 asl4827
            AVA: Ava_2097 Ava_3444
            PMA: Pro0063(gmd)
            PMM: PMM1208(gmd)
            PMN: PMN2A_1221
            PMI: PMT9312_1316
            PMB: A9601_13991(gmd) A9601_14531(rfbB)
            PMC: P9515_01521(rfbB) P9515_07621 P9515_13001 P9515_13681(gmd)
                 P9515_14221
            PMF: P9303_01011 P9303_01131 P9303_01181(rfbB) P9303_26091
            PMG: P9301_14001 P9301_14111(rfbB) P9301_14441(gmd)
            PMH: P9215_14141(gmd)
            PME: NATL1_03941 NATL1_08571(rfbB) NATL1_20961(gmd) NATL1_21061
            TER: Tery_0490
            BTH: BT_1224
            BFR: BF1823
            BFS: BF1888
            PGI: PG1288(gmd)
            CHU: CHU_0059(gmd)
            GFO: GFO_0553(gmd)
            FPS: FP1640(gmd)
            CCH: Cag_0652
            PLT: Plut_1863
            AAE: aq_1082(rfbD)
            MAC: MA1173(gmd) MA1174(gmd)
            MBA: Mbar_A0034
            MMA: MM_0659
            MHU: Mhun_2132 Mhun_2858
            MTH: MTH333
            MST: Msp_0990
            AFU: AF0044m(gmd-1)
            RCI: RCIX204(gmd)
STRUCTURES  PDB: 1DB3  1N7G  1N7H  1RPN  1T2A  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.47
            ExPASy - ENZYME nomenclature database: 4.2.1.47
            ExplorEnz - The Enzyme Database: 4.2.1.47
            ERGO genome analysis and discovery system: 4.2.1.47
            BRENDA, the Enzyme Database: 4.2.1.47
            CAS: 37211-59-9
///
ENTRY       EC 4.2.1.48                 Enzyme
NAME        D-glutamate cyclase;
            D-glutamate hydro-lyase (cyclizing)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     D-glutamate hydro-lyase (cyclizing; 5-oxo-D-proline-forming)
REACTION    D-glutamate = 5-oxo-D-proline + H2O [RN:R01583]
ALL_REAC    R01583
SUBSTRATE   D-glutamate [CPD:C00217]
PRODUCT     5-oxo-D-proline [CPD:C02237];
            H2O [CPD:C00001]
COMMENT     Also acts on various derivatives of D-glutamate.
REFERENCE   1  [PMID:14087295]
  AUTHORS   MEISTER A, BUKENBERGER MW, STRASSBURGER M.
  TITLE     THE OPTICALLY-SPECIFIC  ENZYMATIC CYCLIZATION OF D-GLUTAMATE.
  JOURNAL   Biochem. Z. 338 (1963) 217-29.
PATHWAY     PATH: map00471  D-Glutamine and D-glutamate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.48
            ExPASy - ENZYME nomenclature database: 4.2.1.48
            ExplorEnz - The Enzyme Database: 4.2.1.48
            ERGO genome analysis and discovery system: 4.2.1.48
            BRENDA, the Enzyme Database: 4.2.1.48
            CAS: 37290-80-5
///
ENTRY       EC 4.2.1.49                 Enzyme
NAME        urocanate hydratase;
            urocanase;
            3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate hydro-lyase
            (urocanate-forming)
REACTION    3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate = urocanate + H2O
            [RN:R02914]
ALL_REAC    R02914
SUBSTRATE   3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate
PRODUCT     urocanate [CPD:C00785];
            H2O [CPD:C00001]
COFACTOR    NAD+ [CPD:C00003];
            2-Oxobutanoate [CPD:C00109]
COMMENT     Contains tightly bound NAD+.
REFERENCE   1  [PMID:7944380]
  AUTHORS   Retey J.
  TITLE     The urocanase story: a novel role of NAD+ as electrophile.
  JOURNAL   Arch. Biochem. Biophys. 314 (1994) 1-16.
  ORGANISM  Bacillus subtilis [GN:bsu], guinea pig, Clostridium tetanomorphum,
            Pseudomonas sp., Aerobacter aerogenes
REFERENCE   2
  AUTHORS   Hassall, H. and Greenberg, D.M.
  TITLE     Urocanase (beef liver).
  JOURNAL   Methods Enzymol. 17B (1971) 84-88.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:4990470]
  AUTHORS   Kaminskas E, Kimhi Y, Magasanik B.
  TITLE     Urocanase and N-formimino-L-glutamate formiminohydrolase of Bacillus
            subtilis, two enzymes of the histidine degradation pathway.
  JOURNAL   J. Biol. Chem. 245 (1970) 3536-44.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   4  [PMID:5784906]
  AUTHORS   Swaine D.
  TITLE     The effect of substrate analogues on the activity of cat liver
            urocanase.
  JOURNAL   Biochim. Biophys. Acta. 178 (1969) 609-18.
  ORGANISM  cat
PATHWAY     PATH: map00340  Histidine metabolism
ORTHOLOGY   KO: K01712  urocanate hydratase
GENES       HSA: 131669(UROC1)
            MMU: 243537(Uroc1)
            CFA: 476507(UROC1)
            GGA: 416035(UROC1)
            SPU: 582394(LOC582394)
            CEL: Y51H4A.7
            DDI: DDBDRAFT_0169359
            TCR: 504045.110
            STY: STY0823(hutU)
            STT: t2097(hutU)
            SEC: SC0788(hutC)
            YPE: YPO4017(hutU)
            YPK: y4038
            YPM: YP_3380(hutU)
            YPA: YPA_4105
            YPN: YPN_3665
            YPP: YPDSF_3760
            YPS: YPTB3852(hutU)
            YPI: YpsIP31758_4086(hutU)
            PLU: plu3193(hutU)
            ENT: Ent638_1263
            SPE: Spro_0805
            XCC: XCC1577(hutU)
            XCB: XC_2657
            XCV: XCV1676(hutU)
            XAC: XAC1635(hutU)
            XOO: XOO2400(hutU)
            XOM: XOO_2280(XOO2280)
            VCH: VC1203
            VCO: VC0395_A0823(hutU)
            VVU: VV1_2390
            VVY: VV1951
            VPA: VP1274
            VFI: VFA0451
            PPR: PBPRA2172
            PAE: PA5100(hutU)
            PAU: PA14_67350(hutU)
            PAP: PSPA7_5833(hutU)
            PPU: PP_5033(hutU)
            PPF: Pput_4907
            PST: PSPTO_5270(hutU)
            PSB: Psyr_4828
            PSP: PSPPH_4860(hutU)
            PFL: PFL_0401(hutU)
            PFO: Pfl_0360
            PEN: PSEEN5097(hutU)
            PMY: Pmen_4070
            PCR: Pcryo_1930
            PRW: PsycPRwf_0852
            SON: SO_0097(hutU)
            SDN: Sden_0083
            SFR: Sfri_3953
            SAZ: Sama_1632
            SBL: Sbal_4252
            SBM: Shew185_0097
            SLO: Shew_3757
            SPC: Sputcn32_0079
            SSE: Ssed_4447
            SPL: Spea_4169
            SHE: Shewmr4_0099
            SHM: Shewmr7_0094
            SHN: Shewana3_0100
            SHW: Sputw3181_3998
            ILO: IL2451(hutU)
            CPS: CPS_0909(hutU)
            PHA: PSHAa2739(hutU)
            PAT: Patl_1021
            PIN: Ping_1030
            LPN: lpg1379
            LPF: lpl1330(hutU)
            LPP: lpp1334(hutU)
            HCH: HCH_04171(hutU)
            MMW: Mmwyl1_3902
            AHA: AHA_0379(hutU)
            CVI: CV_0323(hutU)
            RSO: RSc2647(hutU)
            REU: Reut_A0896 Reut_A2715 Reut_B5636
            REH: H16_A0695(hutU2) H16_A3017(hutU1)
            RME: Rmet_2854 Rmet_5048
            BMA: BMA0647(hutU)
            BMV: BMASAVP1_A2364(hutU)
            BML: BMA10299_A2921(hutU)
            BMN: BMA10247_1679(hutU)
            BXE: Bxe_A2945
            BVI: Bcep1808_2245
            BUR: Bcep18194_A5480 Bcep18194_B3016
            BCN: Bcen_5907
            BCH: Bcen2424_2170
            BAM: Bamb_2209
            BPS: BPSL1678 BPSL2342(hutU)
            BPM: BURPS1710b_2185(hutU) BURPS1710b_2794(hutU)
            BPL: BURPS1106A_2721(hutU)
            BPD: BURPS668_2665(hutU)
            BTE: BTH_I1822(hutU)
            POL: Bpro_1042 Bpro_1164
            AAV: Aave_2964
            VEI: Veis_3646
            EBA: ebA5741(hutU)
            BBA: Bd2751(hutU)
            DPS: DP2352
            ADE: Adeh_1508
            AFW: Anae109_2315
            MXA: MXAN_4343(hutU)
            SFU: Sfum_2376
            MLO: mlr8323
            MES: Meso_2638 Meso_2983
            SME: SMb21163(hutU)
            SMD: Smed_4656
            ATU: Atu3931(hutU)
            ATC: AGR_L_1830(hutU)
            RET: RHE_CH00347(hutUch) RHE_PE00070(hutUe)
            RLE: RL0364(hutU) pRL110203
            BME: BMEII0365
            BMF: BAB2_0303
            BMS: BRA0932(hutU)
            BMB: BruAb2_0301(hutU)
            BOV: BOV_A0874(hutU)
            OAN: Oant_1433
            BJA: bll6241(hutU)
            BRA: BRADO1605(hutU)
            BBT: BBta_6450(hutU)
            CCR: CC_0957
            SIL: SPO2193(hutU)
            SIT: TM1040_3007
            RSP: RSP_2936(hutU)
            RSH: Rsph17029_1580
            RDE: RD1_3682(hutU)
            PDE: Pden_0715 Pden_3517
            MMR: Mmar10_1601
            HNE: HNE_2398(hutU)
            SAL: Sala_1691
            SWI: Swit_4630
            GOX: GOX1166
            ACR: Acry_1749
            RRU: Rru_A1304
            ABA: Acid345_1048
            SUS: Acid_5209
            BSU: BG10668(hutU)
            BHA: BH1983(hutU)
            BAN: BA3711(hutU)
            BAR: GBAA3711(hutU)
            BAA: BA_4194
            BAT: BAS3441
            BCE: BC3651
            BCA: BCE_3679(hutU)
            BCZ: BCZK3353(hutU)
            BCY: Bcer98_2311
            BTK: BT9727_3404(hutU)
            BCL: ABC3330(hutU)
            BAY: RBAM_036420(hutU)
            GKA: GK1367
            SAU: SA2122(hutU)
            SAV: SAV2331(hutU)
            SAM: MW2252(hutU)
            SAR: SAR2417(hutU)
            SAS: SAS2224
            SAC: SACOL2324(hutU)
            SAB: SAB2208c(hutU)
            SAA: SAUSA300_2278(hutU)
            SAO: SAOUHSC_02607
            SAJ: SaurJH9_2356
            SAH: SaurJH1_2399
            SSP: SSP0572
            SPY: SPy_2082(hutU)
            SPZ: M5005_Spy_1771(hutU)
            SPM: spyM18_2141(hutU)
            SPG: SpyM3_1773(hutU)
            SPS: SPs1770
            SPH: MGAS10270_Spy1837(hutU)
            SPI: MGAS10750_Spy1863(hutU)
            SPJ: MGAS2096_Spy1804(hutU)
            SPK: MGAS9429_Spy1782(hutU)
            SPF: SpyM51729(hutU)
            SPA: M6_Spy1768
            SPB: M28_Spy1755(hutU)
            STC: str1315(hutU)
            STL: stu1315(hutU)
            SSA: SSA_0435(hutU)
            SGO: SGO_1805(hutU)
            STH: STH3193
            CTC: CTC02321
            AMT: Amet_4074
            TTE: TTE0449(hutU)
            MSM: MSMEG_1179(hutU)
            NFA: nfa12270(hutU)
            RHA: RHA1_ro04642(hutU)
            SCO: SCO3073(hutU)
            SMA: SAV3496(hutU)
            ART: Arth_0374
            AAU: AAur_0398(hutU)
            PAC: PPA2165 PPA2166
            NCA: Noca_4397
            KRA: Krad_4452
            SEN: SACE_6406(hutU)
            STP: Strop_1110
            RXY: Rxyl_0583
            FNU: FN0792 FN1401
            TDE: TDE2606(hutU)
            BTH: BT_2694
            BFR: BF4148
            BFS: BF3970(hutU)
            PGI: PG1872(hutU)
            GFO: GFO_0235(hutU)
            FJO: Fjoh_1908
            FPS: FP1957(hutU)
            DRA: DR_A0151
            DGE: Dgeo_2735
            TME: Tmel_1893
            FNO: Fnod_1461
            HAL: VNG1208G(hutU)
            HMA: rrnAC1787(hutU)
            TAC: Ta0239m
            TVO: TVN1356
            PTO: PTO0103
            PAS: Pars_1484
STRUCTURES  PDB: 1UWK  1UWL  1W1U  1X87  2FKN  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.49
            ExPASy - ENZYME nomenclature database: 4.2.1.49
            ExplorEnz - The Enzyme Database: 4.2.1.49
            ERGO genome analysis and discovery system: 4.2.1.49
            BRENDA, the Enzyme Database: 4.2.1.49
            CAS: 9014-58-8
///
ENTRY       EC 4.2.1.50                 Enzyme
NAME        pyrazolylalanine synthase;
            beta-pyrazolylalaninase;
            beta-(1-pyrazolyl)alanine synthase;
            L-serine hydro-lyase (adding pyrazole)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     L-serine hydro-lyase [adding pyrazole;
            3-(pyrazol-1-yl)-L-alanine-forming]
REACTION    L-serine + pyrazole = 3-(pyrazol-1-yl)-L-alanine + H2O [RN:R02378]
ALL_REAC    R02378
SUBSTRATE   L-serine [CPD:C00065];
            pyrazole [CPD:C00481]
PRODUCT     3-(pyrazol-1-yl)-L-alanine [CPD:C01162];
            H2O [CPD:C00001]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1
  AUTHORS   Dunnill, P.M. and Fowden, L.
  TITLE     The biosynthesis of beta-pyrazol-1-ylalanine.
  JOURNAL   J. Exp. Bot. 14 (1963) 237-248.
  ORGANISM  Cucumis sativus, Cucumis melo, Cucurbita pepo, Citrullus vulgaris
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.50
            ExPASy - ENZYME nomenclature database: 4.2.1.50
            ExplorEnz - The Enzyme Database: 4.2.1.50
            ERGO genome analysis and discovery system: 4.2.1.50
            BRENDA, the Enzyme Database: 4.2.1.50
            CAS: 37290-81-6
///
ENTRY       EC 4.2.1.51                 Enzyme
NAME        prephenate dehydratase;
            prephenate hydro-lyase (decarboxylating)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     prephenate hydro-lyase (decarboxylating; phenylpyruvate-forming)
REACTION    prephenate = phenylpyruvate + H2O + CO2 [RN:R01373]
ALL_REAC    R01373;
            (other) R00691
SUBSTRATE   prephenate [CPD:C00254]
PRODUCT     phenylpyruvate [CPD:C00166];
            H2O [CPD:C00001];
            CO2 [CPD:C00011]
COMMENT     This enzyme in the enteric bacteria also possesses chorismate mutase
            (EC 5.4.99.5) activity, and converts chorismate into prephenate.
REFERENCE   1  [PMID:14342329]
  AUTHORS   CERUTTI P, GUROFF G.
  TITLE     ENZYMATIC FORMATION OF PHENYLPYRUVIC ACID IN PSEUDOMONAS SP. (ATCC
            11299A) AND ITS REGULATION.
  JOURNAL   J. Biol. Chem. 240 (1965) 3034-8.
REFERENCE   2  [PMID:14323651]
  AUTHORS   COTTON RG, GIBSON F.
  TITLE     THE BIOSYNTHESIS OF PHENYLALANINE AND TYROSINE; ENZYMES CONVERTING
            CHORISMIC ACID INTO PREPHENIC ACID AND THEIR RELATIONSHIPS TO
            PREPHENATE DEHYDRATASE AND PREPHENATE DEHYDROGENASE.
  JOURNAL   Biochim. Biophys. Acta. 100 (1965) 76-88.
  ORGANISM  Escherichia coli [GN:eco], Aerobacter aerogenes
REFERENCE   3
  AUTHORS   Schmidt, J.C. and Zalkin, H.
  TITLE     Chorismate mutase-prephenate dehydratase. Partial purification and
            properties of the enzyme from Salmonella typhimurium.
  JOURNAL   Biochemistry 8 (1969) 174-181.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K01713  prephenate dehydratase
            KO: K04518  prephenate dehydratase
GENES       OSA: 4332477
            CME: CML204C
            SCE: YNL316C(PHA2)
            AGO: AGOS_ADL180C
            CGR: CAGL0M04059g
            SPO: SPBC30D10.16
            AFM: AFUA_5G05690
            AOR: AO090009000693
            CNE: CNA07970
            ECO: b2599(pheA)
            ECJ: JW2580(pheA)
            ECE: Z3891(pheA)
            ECS: ECs3462
            ECC: c3120(pheA)
            ECI: UTI89_C2932(pheA)
            ECP: ECP_2600
            ECV: APECO1_3934
            ECW: EcE24377A_2883(pheA)
            ECX: EcHS_A2756
            STY: STY2854(pheA)
            STT: t2622(pheA)
            SPT: SPA2526(pheA)
            SEC: SC2669(pheA)
            STM: STM2667(pheA)
            YPE: YPO3281(pheA)
            YPM: YP_0400(pheA1)
            YPA: YPA_2773 YPA_2861
            YPN: YPN_0750 YPN_0815
            YPP: YPDSF_3017
            YPS: YPTB0843(pheA)
            YPI: YpsIP31758_3218(pheA)
            SFL: SF2659(pheA)
            SFX: S2836(pheA)
            SFV: SFV_2872(pheA)
            SSN: SSON_2750(pheA)
            SBO: SBO_2637(pheA)
            SDY: SDY_2767(pheA)
            ECA: ECA3350(pheA)
            PLU: plu1265(pheA)
            BUC: BU392(pheA)
            BAS: BUsg379(pheA)
            BAB: bbp355(pheA)
            BCC: BCc_244(pheA)
            SGL: SG0580
            BFL: Bfl179(pheA)
            BPN: BPEN_185(pheA)
            HIN: HI1145(pheA)
            HIT: NTHI1313(pheA)
            HDU: HD0873(pheA)
            HSO: HS_0365(pheA)
            PMU: PM0150(pheA)
            MSU: MS1657(pheA)
            APL: APL_1033(pheA)
            XFA: XF2325
            XFT: PD1357(pheA)
            XCC: XCC1590(pheA)
            XCB: XC_2644
            XCV: XCV1690(pheA)
            XAC: XAC1649(pheA)
            XOO: XOO2387(pheA)
            XOM: XOO_2267(XOO2267)
            VCH: VC0705
            VVU: VV1_0487
            VPA: VP0555
            VFI: VF0561 VF1270
            PPR: PBPRA3024
            PAE: PA3166(pheA) PA3475(pheC)
            PPU: PP_1769(pheA)
            PST: PSPTO_1747(pheA)
            PSB: Psyr_3645
            PSP: PSPPH_3665(pheA)
            PFL: PFL_4312(pheA)
            PFO: Pfl_4076
            PEN: PSEEN1489(pheA)
            PAR: Psyc_1186(pheA)
            ACI: ACIAD2223(pheA)
            SON: SO_1367(pheA)
            SDN: Sden_2747
            SBL: Sbal_3744
            SHN: Shewana3_3007
            ILO: IL0038(pheA)
            CPS: CPS_1221(pheA)
            PHA: PSHAa0950(pheA)
            PAT: Patl_1590
            PIN: Ping_0627
            CBD: COXBU7E912_1064
            MCA: MCA1418(pheA)
            FTU: FTT0575(pheA)
            FTF: FTF0575(pheA)
            FTW: FTW_1436(pheA)
            FTL: FTL_1336
            FTH: FTH_1301(pheA)
            FTN: FTN_0748(pheA)
            TCX: Tcr_1193
            NOC: Noc_0174
            AEH: Mlg_0926
            HCH: HCH_04981 HCH_06095
            MMW: Mmwyl1_3003
            AHA: AHA_1092(pheA)
            VOK: COSY_0579(pheA)
            NME: NMB0446
            NMA: NMA2039(pheA)
            NGO: NGO1510
            CVI: CV_0224 CV_2355(pheA)
            RSO: RSc0904(pheA)
            REU: Reut_A2575
            RME: Rmet_0716
            BMA: BMA0432 BMA2961(pheC)
            BMV: BMASAVP1_A2575(pheA) BMASAVP1_A3350(pheC)
            BML: BMA10299_A0950(pheA) BMA10299_A1581(pheC)
            BMN: BMA10247_0198(pheA) BMA10247_3021(pheC)
            BXE: Bxe_A0977
            BVI: Bcep1808_0119
            BUR: Bcep18194_A3291 Bcep18194_A3548 Bcep18194_A4156
                 Bcep18194_A4695 Bcep18194_A4762 Bcep18194_A6491
                 Bcep18194_B0836
            BCN: Bcen_2945
            BCH: Bcen2424_0110
            BAM: Bamb_0100 Bamb_0919
            BPS: BPSL2518(pheA) BPSL3392(pheC)
            BPM: BURPS1710b_0172(pheC) BURPS1710b_2997(pheA)
            BPL: BURPS1106A_2948(pheA) BURPS1106A_4037(pheC)
            BPD: BURPS668_2885(pheA) BURPS668_3964(pheC)
            BTE: BTH_I1635 BTH_I3305
            BPE: BP0946(pheA)
            BPA: BPP3132(pheA)
            BBR: BB3471(pheA)
            RFR: Rfer_1569
            POL: Bpro_0969 Bpro_1792 Bpro_4214
            AAV: Aave_2470
            MPT: Mpe_A2241
            HAR: HEAR2579(pheA)
            MMS: mma_2673
            NEU: NE0335(pheA)
            NET: Neut_1570
            NMU: Nmul_A2192
            EBA: ebA906(pheA)
            DAR: Daro_1232
            TBD: Tbd_0951
            MFA: Mfla_1686
            HPA: HPAG1_0293
            HHE: HH1508(pheA)
            WSU: WS0332(pheA)
            TDN: Tmden_0470
            CJE: Cj0316(pheA)
            CJR: CJE0361(pheA)
            CJU: C8J_0293(pheA)
            CCV: CCV52592_1666
            CCO: CCC13826_0509
            ABU: Abu_2137(pheA)
            NIS: NIS_0389(pheA)
            SUN: SUN_2057(pheA)
            GSU: GSU2608(pheA)
            GME: Gmet_0862
            PCA: Pcar_1887
            DVU: DVU0462
            DDE: Dde_3487
            DPS: DP2171
            ADE: Adeh_1779
            AFW: Anae109_2039
            MXA: MXAN_3220
            SAT: SYN_01299
            SFU: Sfum_2723 Sfum_2763
            PUB: SAR11_0506(pheA)
            MLO: mlr5498
            MES: Meso_4087
            PLA: Plav_0252 Plav_0286
            SME: SMc02899(pheA)
            SMD: Smed_3428
            ATU: Atu0099(pheA)
            ATC: AGR_C_151
            RET: RHE_CH00131(pheA)
            RLE: RL0139
            BME: BMEI1905
            BMF: BAB1_0034(pheA)
            BMS: BR0037(pheA)
            BMB: BruAb1_0037(pheA)
            BOV: BOV_0037(pheA)
            OAN: Oant_0018
            BJA: bll1421(pheA)
            BRA: BRADO0999(pheA) BRADO3810
            BBT: BBta_4123 BBta_7058(pheA)
            RPA: RPA3695
            RPB: RPB_1767
            RPC: RPC_3732
            RPD: RPD_3538
            RPE: RPE_3770
            NWI: Nwi_0285
            NHA: Nham_0365
            BHE: BH02350(pheA)
            XAU: Xaut_2629
            CCR: CC_2933
            SIL: SPO3539
            SIT: TM1040_2554
            RSP: RSP_0706(pheA)
            RSH: Rsph17029_2361
            RSQ: Rsph17025_0524
            JAN: Jann_3865
            RDE: RD1_1261(pheA)
            PDE: Pden_1809
            MMR: Mmar10_1341
            HNE: HNE_0659
            ZMO: ZMO1678(pheA)
            NAR: Saro_0467
            SAL: Sala_0622
            SWI: Swit_4688
            ELI: ELI_10290
            GOX: GOX0062
            GBE: GbCGDNIH1_1994
            ACR: Acry_0642
            RRU: Rru_A3162
            MAG: amb4167
            MGM: Mmc1_0176 Mmc1_1881
            ABA: Acid345_2043
            SUS: Acid_7054
            BSU: BG10914(pheA)
            BHA: BH1215(pheA)
            BAN: BA4666(pheA)
            BAR: GBAA4666(pheA)
            BAA: BA_5105
            BAT: BAS4331
            BCE: BC4427
            BCA: BCE_4525(pheA)
            BCZ: BCZK4179(pheA)
            BCY: Bcer98_3149
            BTK: BT9727_4168(pheA)
            BTL: BALH_4015(pheA)
            BLI: BL01156(pheA)
            BLD: BLi02917(pheA)
            BCL: ABC1544(pheA)
            BAY: RBAM_024950
            BPU: BPUM_2430
            OIH: OB2041(pheA)
            GKA: GK2604
            SAU: SA1731
            SAV: SAV1915
            SAM: MW1856
            SAR: SAR2008
            SAS: SAS1839
            SAC: SACOL1977(pheA)
            SAB: SAB1852
            SAA: SAUSA300_1896(pheA)
            SAO: SAOUHSC_02135
            SAJ: SaurJH9_1971
            SAH: SaurJH1_2005
            SEP: SE1599
            SER: SERP1452(pheA)
            SHA: SH1037(pheA)
            SSP: SSP0876
            LMO: lmo1536(pheA)
            LMF: LMOf2365_1555(pheA)
            LIN: lin1571
            LWE: lwe1549(pheA)
            LLA: L0055(pheA)
            LLC: LACR_1905
            LLM: llmg_1924(pheA)
            SPN: SP_1369
            SPR: spr1227(pheA)
            SPD: SPD_1203
            SMU: SMU.786(pheA)
            STC: str0647(pheA)
            STL: stu0647(pheA)
            SSA: SSA_1462(pheA)
            SGO: SGO_1366(pheA)
            EFA: EF1568
            STH: STH2692
            CAC: CAC0217(pheA)
            CTH: Cthe_2260
            CDF: CD1836(pheA)
            CBE: Cbei_4573
            CKL: CKL_0789(pheA)
            AMT: Amet_0648
            DSY: DSY1892
            DRM: Dred_0783
            SWO: Swol_0810
            CSC: Csac_1462
            TTE: TTE1012(pheA)
            MTA: Moth_1334
            MTU: Rv3838c(pheA)
            MTC: MT3946(pheA)
            MBO: Mb3868c(pheA)
            MBB: BCG_3901c(pheA)
            MLE: ML0078(pheA)
            MPA: MAP0193(pheA)
            MAV: MAV_0188
            MSM: MSMEG_3442 MSMEG_6418
            MVA: Mvan_5662
            MGI: Mflv_1145
            MMC: Mmcs_5034
            MKM: Mkms_5122
            MJL: Mjls_5415
            CGL: NCgl2799(cgl2899)
            CGB: cg3207(pheA)
            CEF: CE2732(pheA)
            CDI: DIP2246(pheA)
            CJK: jk0119(pheA)
            NFA: nfa1330
            RHA: RHA1_ro04033(pheA)
            SCO: SCO3962(pheA)
            SMA: SAV4243(pheA)
            LXX: Lxx02400(pheA)
            ART: Arth_0138 Arth_3518
            AAU: AAur_0101(pheA)
            NCA: Noca_0170
            TFU: Tfu_3053
            FRA: Francci3_2485 Francci3_2951
            FAL: FRAAL3225(pheA) FRAAL4901(pheA)
            ACE: Acel_2105
            KRA: Krad_0245
            SEN: SACE_0152(pheA) SACE_1605(pheC)
            STP: Strop_4522
            BLO: BL1381(pheA)
            BAD: BAD_1067(pheA)
            RBA: RB9107(pheA)
            LIL: LA1256(aroQ)
            LIC: LIC12451(pheA)
            LBJ: LBJ_0932(pheA)
            LBL: LBL_2101(pheA)
            SYN: sll1662(pheA)
            SYW: SYNW2142(pheA)
            SYC: syc0659_c(pheA)
            SYF: Synpcc7942_0881
            SYD: Syncc9605_0316
            SYE: Syncc9902_2026
            SYG: sync_0377
            SYR: SynRCC307_2174(pheA)
            SYX: SynWH7803_0375(pheA)
            CYA: CYA_1460
            CYB: CYB_0653
            TEL: tlr2106
            GVI: gll0524
            ANA: alr4334
            AVA: Ava_1284
            PMA: Pro1660(pheA)
            PMM: PMM1504(pheA)
            PMT: PMT1786(pheA)
            PMN: PMN2A_1070
            PMI: PMT9312_1596
            PMB: A9601_17071(pheA)
            PMC: P9515_16841(pheA)
            PMF: P9303_23691(pheA)
            PMG: P9301_16951(pheA)
            PME: NATL1_19451(pheA)
            TER: Tery_0480
            BTH: BT_3936
            BFR: BF3942
            BFS: BF3715
            SRU: SRU_1955(pheA)
            CHU: CHU_0764(pheA)
            GFO: GFO_0340(pheA)
            FJO: Fjoh_0517
            FPS: FP0251(pheA)
            CTE: CT1666(pheA)
            CCH: Cag_0180
            CPH: Cpha266_0537
            PVI: Cvib_1433
            PLT: Plut_1644
            DET: DET0461(tyrA) DET1547(pheA)
            DEH: cbdb_A1639(pheA) cbdb_A424(pheA)
            DEB: DehaBAV1_1303
            RRS: RoseRS_1964
            RCA: Rcas_1552
            DRA: DR_1147
            DGE: Dgeo_1334
            TTJ: TTHA1104
            AAE: aq_951(pheA)
            TMA: TM0155
            TPT: Tpet_0771
            MJA: MJ0637(pheA)
            MMP: MMP1528(pheA)
            MMQ: MmarC5_0047
            MMZ: MmarC7_0776
            MAE: Maeo_0499
            MVN: Mevan_0841
            MAC: MA3150(pheA)
            MBA: Mbar_A1930
            MMA: MM_0370
            MBU: Mbur_0806
            MTP: Mthe_0937
            MHU: Mhun_1032
            MEM: Memar_1299
            MBN: Mboo_1561
            MTH: MTH1220
            MST: Msp_1427(pheA)
            MSI: Msm_1052
            MKA: MK0079(tyrA_1)
            AFU: AF0227(pheA)
            HAL: VNG2222G(pheA)
            HMA: rrnAC2950(pheA)
            HWA: HQ1385A(pheA)
            NPH: NP0106A(pheA2)
            TAC: Ta0915
            TVO: TVN0861
            PTO: PTO1013
            PFU: PF0291
            RCI: RRC474(pheA)
            IHO: Igni_0307
            SSO: SSO0246(pheA)
            STO: ST0294
            SAI: Saci_0712
            MSE: Msed_0012
            PAI: PAE0893
            PIS: Pisl_1150
            PCL: Pcal_0075
            PAS: Pars_0111
            NEQ: NEQ192
STRUCTURES  PDB: 2QMX  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.51
            ExPASy - ENZYME nomenclature database: 4.2.1.51
            ExplorEnz - The Enzyme Database: 4.2.1.51
            ERGO genome analysis and discovery system: 4.2.1.51
            BRENDA, the Enzyme Database: 4.2.1.51
            CAS: 9044-88-6
///
ENTRY       EC 4.2.1.52                 Enzyme
NAME        dihydrodipicolinate synthase;
            dihydropicolinate synthetase;
            dihydrodipicolinic acid synthase;
            L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and
            cyclizing)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     L-aspartate-4-semialdehyde hydro-lyase [adding pyruvate and
            cyclizing; (S)-2,3-dihydropyridine-2,6-dicarboxylate-forming]
REACTION    L-aspartate 4-semialdehyde + pyruvate =
            (S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O [RN:R02292]
ALL_REAC    R02292
SUBSTRATE   L-aspartate 4-semialdehyde [CPD:C00441];
            pyruvate [CPD:C00022]
PRODUCT     (S)-2,3-dihydropyridine-2,6-dicarboxylate;
            H2O [CPD:C00001]
REFERENCE   1  [PMID:4910051]
  AUTHORS   Shedlarski JG, Gilvarg C.
  TITLE     The pyruvate-aspartic semialdehyde condensing enzyme of Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 245 (1970) 1362-73.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:5321309]
  AUTHORS   Yugari Y, Gilvarg C.
  TITLE     The condensation step in diaminopimelate synthesis.
  JOURNAL   J. Biol. Chem. 240 (1965) 4710-6.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K01714  dihydrodipicolinate synthase
GENES       ATH: AT2G45440(DHDPS2)
            OSA: 4335317 4336734
            CME: CME179C
            PIC: PICST_64442
            ANI: AN2728.2
            AFM: AFUA_6G00110
            AOR: AO090003001442
            ECO: b2478(dapA)
            ECJ: JW2463(dapA)
            ECE: Z3737(dapA)
            ECS: ECs3340
            ECC: c0761 c3006(dapA)
            ECI: UTI89_C0679 UTI89_C2805(dapA) UTI89_C3975
            ECP: ECP_0695 ECP_2492
            ECV: APECO1_1389 APECO1_2993 APECO1_4079(dapA)
            ECW: EcE24377A_2760(dapA)
            ECX: EcHS_A2610
            STY: STY2727(dapA)
            STT: t0370(dapA)
            SPT: SPA0380(dapA)
            SEC: SC2484(dapA)
            STM: STM2489(dapA)
            YPE: YPO3062(dapA)
            YPK: y1418(dapA)
            YPM: YP_2684(dapA2)
            YPA: YPA_2253
            YPN: YPN_1323
            YPS: YPTB2783(dapA)
            YPI: YpsIP31758_1247(dapA)
            SFL: SF2521(dapA)
            SFX: S2671(dapA)
            SFV: SFV_2523(dapA)
            SSN: SSON_2559(dapA)
            SBO: SBO_2495(dapA)
            SDY: SDY_2667(dapA)
            ECA: ECA1002 ECA1262(dapA) ECA3763 ECA4425
            PLU: plu1530 plu2245 plu2746(dapA)
            BUC: BU096(dapA)
            BAS: BUsg088(dapA)
            BAB: bbp090(dapA)
            BCC: BCc_060(dapA)
            WBR: WGLp331(dapA)
            SGL: SG1726
            BFL: Bfl518(dapA)
            BPN: BPEN_536(dapA)
            HIT: NTHI0362(dapA)
            HIP: CGSHiEE_01790
            HDU: HD1107(dapA)
            HSO: HS_0492(dapA)
            PMU: PM1051(dapA)
            MSU: MS0067(dapA) MS0265(dapA)
            APL: APL_0899(dapA)
            ASU: Asuc_1954
            XFA: XF0963
            XFT: PD1737(dapA)
            XCC: XCC1741(dapA) XCC2411(dapA)
            XCB: XC_1701 XC_2493
            XCV: XCV1791(dapA) XCV2744(dapA2)
            XAC: XAC1760(dapA) XAC2547(dapA)
            XOO: XOO2923(dapA) XOO3137(dapA)
            XOM: XOO_2774(XOO2774) XOO_2979(XOO2979)
            VCH: VC2157
            VCO: VC0395_A1738(dapA)
            VVU: VV1_1912
            VVY: VV2504 VVA1582
            VPA: VP1335 VP2273
            VFI: VF1918(dapA)
            PPR: PBPRA2898(dapA)
            PAE: PA0223 PA1010(da) PA1254 PA4188
            PAU: PA14_02730 PA14_09730(dapA) PA14_48000 PA14_51270(dapA)
            PAP: PSPA7_4387(dapA)
            PPU: PP_1237(dapA) PP_1257 PP_2036
            PST: PSPTO_3063 PSPTO_3953(dapA)
            PSB: Psyr_1548
            PSP: PSPPH_1537(dapA) PSPPH_1611
            PFL: PFL_1395 PFL_1413 PFL_1457(dapA) PFL_3321(dapA)
            PFO: Pfl_1307 Pfl_1371 Pfl_2307
            PEN: PSEEN0973 PSEEN2380 PSEEN4051 PSEEN4064(dapA)
            PAR: Psyc_0148(dapA)
            PCR: Pcryo_0158 Pcryo_1217
            ACI: ACIAD3585(dapA)
            SON: SO_1879(dapA)
            SDN: Sden_1735
            SFR: Sfri_1864
            SLO: Shew_2362
            SSE: Ssed_2430
            SHE: Shewmr4_2340
            SHM: Shewmr7_2412
            SHN: Shewana3_1656
            ILO: IL1460(dapA)
            CPS: CPS_1449 CPS_3680(dapA)
            PHA: PSHAa0180(dapA) PSHAb0390
            PAT: Patl_2478
            SDE: Sde_2622
            MAQ: Maqu_1691
            CBU: CBU_1222(dapA)
            CBD: COXBU7E912_1306(dapA)
            LPN: lpg2314
            LPF: lpl2234(dapA)
            LPP: lpp2262(dapA) lpp2860
            MCA: MCA0671(dapA)
            FTN: FTN_1728(dapA)
            TCX: Tcr_1552
            NOC: Noc_2524
            AEH: Mlg_2476
            HCH: HCH_03163(dapA1) HCH_04906(dapA2) HCH_06020(dapA3)
            CSA: Csal_2706 Csal_2816
            ABO: ABO_0776(dapA)
            MMW: Mmwyl1_0053
            AHA: AHA_0896(dapA-1) AHA_3801(dapA-2)
            DNO: DNO_1114(dapA)
            CRP: CRP_105
            VOK: COSY_0264(dapA)
            NME: NMB0929
            NMA: NMA1124(dapA)
            NMC: NMC0907(dapA)
            NGO: NGO0947
            CVI: CV_2048 CV_2825 CV_3578(dapA)
            RSO: RSc1145(dapA) RSc2111(RS01493)
            REU: Reut_A1104(dapA)
            REH: H16_A1204(dapA1) H16_B0213(dapA2) H16_B0891(dapA3)
                 H16_B1831(dapA4)
            RME: Rmet_0666 Rmet_1068 Rmet_2960 Rmet_5097 Rmet_5202
            BMA: BMA1678(dapA) BMA1958 BMAA1420
            BMV: BMASAVP1_A2180(dapA)
            BML: BMA10299_A3137(dapA)
            BMN: BMA10247_1453(dapA)
            BXE: Bxe_A1585 Bxe_A4304 Bxe_B0873 Bxe_B1417
            BVI: Bcep1808_2174
            BUR: Bcep18194_A5401(dapA) Bcep18194_A6298 Bcep18194_B0042
                 Bcep18194_B0078 Bcep18194_B1372 Bcep18194_B1895
                 Bcep18194_B3057 Bcep18194_C7621 Bcep18194_C7655
            BCN: Bcen_1537 Bcen_2332 Bcen_4227 Bcen_5216 Bcen_5246 Bcen_5759
                 Bcen_5982
            BCH: Bcen2424_2095 Bcen2424_2946 Bcen2424_3227 Bcen2424_4139
                 Bcen2424_5613 Bcen2424_5643 Bcen2424_5804 Bcen2424_6124
                 Bcen2424_6264 Bcen2424_6292
            BAM: Bamb_1345 Bamb_2132 Bamb_2993 Bamb_4892 Bamb_6107
            BPS: BPSL0936 BPSL2258(dapA) BPSS0331
            BPM: BURPS1710b_0557(dapA) BURPS1710b_1160 BURPS1710b_2699(dapA)
                 BURPS1710b_A1886
            BPL: BURPS1106A_0382(dapA) BURPS1106A_2619(dapA) BURPS1106A_A0471
            BPD: BURPS668_0367(dapA) BURPS668_2565(dapA) BURPS668_A0568
            BTE: BTH_I0323(dapA-1) BTH_I0803 BTH_I1906(dapA-2) BTH_II2068
            PNU: Pnuc_0847
            BPE: BP0644 BP1570(dapA)
            BPA: BPP0679(dapA) BPP2260(dapA)
            BBR: BB0686(dapA) BB1108(dapA) BB1656(dapA) BB4720
            RFR: Rfer_1636 Rfer_2097
            POL: Bpro_2195 Bpro_3170 Bpro_3814
            VEI: Veis_1200
            MPT: Mpe_A2563
            HAR: HEAR2175(dapA)
            MMS: mma_1282 mma_1802
            NEU: NE2403(dapA)
            NET: Neut_0733
            NMU: Nmul_A1540
            EBA: ebA774(dapA)
            AZO: azo1096(dapA)
            DAR: Daro_0846
            TBD: Tbd_1098(dapA)
            MFA: Mfla_0843 Mfla_0987
            HPY: HP1013(dapA)
            HPA: HPAG1_0433
            HHE: HH1626(dapA)
            HAC: Hac_1117(dapA)
            WSU: WS2221(dapA)
            TDN: Tmden_1226
            CJE: Cj0481 Cj0806(dapA)
            CJR: CJE0532 CJE0897(dapA)
            CJJ: CJJ81176_0827(dapA)
            CJU: C8J_0757(dapA)
            CJD: JJD26997_1204(dapA)
            CFF: CFF8240_0784(dapA) CFF8240_1063
            CCV: CCV52592_1138(dapA) CCV52592_1967
            CHA: CHAB381_0583(dapA)
            CCO: CCC13826_0120(dapA) CCC13826_1145
            ABU: Abu_0874(dapA)
            NIS: NIS_0699(dapA)
            SUN: SUN_0809(dapA)
            GSU: GSU0159(dapA)
            GME: Gmet_0211
            GUR: Gura_0234
            PCA: Pcar_2421
            PPD: Ppro_3063
            DVU: DVU1868(dapA)
            DVL: Dvul_1296
            DDE: Dde_1797
            LIP: LI0896(dapA)
            BBA: Bd0046(dapA)
            DPS: DP0432
            ADE: Adeh_4069
            MXA: MXAN_5928(dapA) MXAN_6203 MXAN_6731
            SAT: SYN_02161
            SFU: Sfum_0056
            RPR: RP429(dapA)
            RTY: RT0415(dapA)
            RCO: RC0595(dapA)
            RFE: RF_0660(dapA)
            RBE: RBE_0740(dapA)
            RAK: A1C_03200
            RBO: A1I_04805
            RRI: A1G_03345
            OTS: OTBS_0393(dapA)
            WOL: WD0775(dapA)
            WBM: Wbm0210(dapA)
            AMA: AM407(dapA)
            ERU: Erum2670(dapA)
            ERW: ERWE_CDS_02710(dapA)
            ERG: ERGA_CDS_02670(dapA)
            ECN: Ecaj_0257
            ECH: ECH_0828(dapA)
            NSE: NSE_0929(dapA)
            PUB: SAR11_0175 SAR11_1062(dapA)
            MLO: mll3981 mll6376 mll6811 mlr6292 mlr7746
            MES: Meso_0941 Meso_2568 Meso_3139
            PLA: Plav_2862
            SME: SMa0707 SMb20140(dapA2) SMb20259 SMb21508(dapA3)
                 SMc02404(dapA1) SMc03259
            SMD: Smed_0673
            ATU: Atu0899(dapA) Atu1024(dapA) Atu3960(dapA) Atu4675(dapA)
                 Atu5067(dapA) Atu5457(dapA)
            ATC: AGR_C_1641 AGR_C_1883 AGR_L_1788 AGR_L_411 AGR_pAT_671
                 AGR_pAT_90(dapA)
            RET: RHE_CH00606(dapAch1) RHE_CH01381(dapAch2)
                 RHE_CH02792(dapAch3) RHE_CH03149(dapAch4) RHE_CH03876
                 RHE_PB00031(dapAb) RHE_PC00042(ypc00025) RHE_PF00094(dapAf1)
                 RHE_PF00398(dapAf3)
            RLE: RL1502(mosA) RL1811(dapA) RL3247(dapA) RL3594(dapA)
                 RL4423(dapA) RL4484(dapA) pRL100268 pRL120004 pRL120328
                 pRL120528 pRL120776 pRL90100
            BME: BMEI1301 BMEII0862 BMEII1006
            BMF: BAB1_0666 BAB2_0816 BAB2_0961
            BMS: BR0646(dapA) BRA0239 BRA0406
            BMB: BruAb1_0663(dapA) BruAb2_0795 BruAb2_0940
            BOV: BOV_0640(dapA)
            OAN: Oant_2201 Oant_2641
            BJA: bll4423 bll5072(dapA) bll5331 bll7272 bll7969 blr3302 blr3307
                 blr3884 blr6784(dapA) blr7382(dapA)
            BRA: BRADO1318 BRADO1404 BRADO1813 BRADO4310 BRADO4475(dapA)
            BBT: BBta_1167 BBta_2133 BBta_4694(dapA) BBta_5002 BBta_6344(dapA)
                 BBta_6698 BBta_6805
            RPA: RPA0898(dapA) RPA1571(dapA1) RPA2686(dapA) RPA2998(dapA1)
                 RPA3190
            RPB: RPB_2353 RPB_2602 RPB_3958 RPB_4525
            RPC: RPC_1160 RPC_2147 RPC_2629 RPC_3385 RPC_4382
            RPD: RPD_0658 RPD_2640 RPD_3716
            RPE: RPE_3032 RPE_3527
            NWI: Nwi_0883 Nwi_1929(dapA)
            NHA: Nham_2262
            BHE: BH05000(dapA)
            BQU: BQ04190(dapA)
            BBK: BARBAKC583_0464(dapA)
            XAU: Xaut_3829
            CCR: CC_1195
            SIL: SPO2882 SPO3556(dapA) SPOA0267
            SIT: TM1040_0150 TM1040_1594 TM1040_3198
            RSP: RSP_0882(dapA) RSP_3408(dapA) RSP_3456 RSP_4002
            RSH: Rsph17029_2542
            RSQ: Rsph17025_0124
            JAN: Jann_0033 Jann_1453 Jann_1485 Jann_4114
            RDE: RD1_0744(dapA) RD1_0972(dapA)
            PDE: Pden_0704 Pden_4867
            MMR: Mmar10_0297 Mmar10_1583
            HNE: HNE_2800(dapA)
            ZMO: ZMO0720(dapA) ZMO1853(dapA)
            NAR: Saro_1443
            SAL: Sala_1731
            ELI: ELI_07760
            GOX: GOX0061
            GBE: GbCGDNIH1_1195
            ACR: Acry_1908
            RRU: Rru_A1865 Rru_A2066 Rru_A3342
            MAG: amb2543
            MGM: Mmc1_3473
            ABA: Acid345_2493
            SUS: Acid_2446 Acid_6980
            BSU: BG10785(dapA)
            BHA: BH1742 BH2399(dapA)
            BAN: BA2832(dapA-1) BA3935(dapA-2)
            BAR: GBAA2832(dapA-1) GBAA3935(dapA-2)
            BAA: BA_3353 BA_4407
            BAT: BAS2641 BAS3650
            BCE: BC2833 BC3797
            BCA: BCE_2861(dapA) BCE_3836
            BCZ: BCZK2557(dapA) BCZK3558(dapA) BCZK3561(dapB) BCZK3562(dapA)
            BCY: Bcer98_0964 Bcer98_2451
            BTK: BT9727_2592(dapA) BT9727_3540(dapA) BT9727_3544(dapA)
            BTL: BALH_3431(dapA)
            BLI: BL01208(dapA) BL03431
            BLD: BLi01902(dapA) BLi03702
            BCL: ABC0222 ABC1113 ABC2030 ABC2214(dapA) ABC3015 ABC3607
            BAY: RBAM_016610
            BPU: BPUM_0291 BPUM_1577(spoVFA) BPUM_1578(spoVFB) BPUM_1581
                 BPUM_2978
            OIH: OB1708(dapA) OB2845 OB2867
            GKA: GK1277(dapA) GK1961 GK3032
            SAU: SA1227(dapA)
            SAV: SAV1395(dapA)
            SAM: MW1283(dapA)
            SAR: SAR1407(dapA)
            SAS: SAS1336(dapA)
            SAC: SACOL1430(dapA)
            SAB: SAB1250(dapA)
            SAA: SAUSA300_1288(dapA)
            SAO: SAOUHSC_01396
            SEP: SE1075
            SER: SERP0965(dapA)
            SHA: SH1516(dapA)
            SSP: SSP1355
            LMO: lmo1435
            LMF: LMOf2365_1454(dapA)
            LIN: lin1474
            LWE: lwe1452(dapA)
            LLA: L0093(dapA)
            LLC: LACR_1729
            LLM: llmg_0874(dapA)
            SPN: SP_1014
            SPR: spr0919(dapA)
            SPD: SPD_0901(dapA)
            SMU: SMU.990(dapA)
            STC: str1297(dapA)
            STL: stu1297(dapA)
            SSA: SSA_1193(dapA)
            SGO: SGO_1205(dapA)
            LPL: lp_2123(dapA1) lp_2685(dapA2)
            LAC: LBA0854
            LSL: LSL_0639(dapA)
            LCA: LSEI_0095
            EFA: EF1184(dapA)
            OOE: OEOE_0774
            STH: STH1549
            CAC: CAC2378(dapA) CAC3600(dapA)
            CPE: CPE1905(dapA)
            CPF: CPF_2161(dapA)
            CPR: CPR_1872(dapA)
            CTC: CTC02294(dapA)
            CNO: NT01CX_1746(dapA)
            CTH: Cthe_0962
            CDF: CD3000 CD3223(dapA1) CD3225(dapA2)
            CBO: CBO3152(dapA)
            CBA: CLB_3187(dapA)
            CBH: CLC_3062(dapA)
            CBF: CLI_3217(dapA)
            CBE: Cbei_1796
            CKL: CKL_3206(dapA4)
            AMT: Amet_0229 Amet_3197
            CHY: CHY_1156(dapA1) CHY_1320(dapA2)
            DSY: DSY2498 DSY3444
            DRM: Dred_1939
            SWO: Swol_1269
            CSC: Csac_1583
            TTE: TTE0832(dapA)
            MTA: Moth_1068
            MTU: Rv2753c(dapA)
            MTC: MT2823(dapA)
            MBO: Mb2774c(dapA)
            MBB: BCG_2769c(dapA)
            MLE: ML1513(dapA)
            MPA: MAP1059(dapA_1) MAP2864c(dapA_2)
            MAV: MAV_3644(dapA)
            MSM: MSMEG_0877 MSMEG_1156 MSMEG_2684(dapA)
            MMC: Mmcs_1632 Mmcs_1696 Mmcs_2116 Mmcs_2614
            CGL: NCgl1896(dapA) NCgl2557(cgl2646)
            CGB: cg2161(dapA)
            CEF: CE1864(dapA)
            CDI: DIP0511 DIP1464(dapA)
            CJK: jk1129(dapA)
            NFA: nfa26720(dapA2) nfa38690(dapA)
            RHA: RHA1_ro00613(dapA1) RHA1_ro02876(dapA2) RHA1_ro02890
                 RHA1_ro05285 RHA1_ro06747(dapA3) RHA1_ro07087(dapA4)
                 RHA1_ro08969(dapA5)
            SCO: SCO1912(SCI7.30) SCO5744(dapA) SCO6292(SCBAC8D1.05)
            SMA: SAV1731(dapA1) SAV2516(dapA2) SAV5607(dapA4) SAV6343(dapA5)
            LXX: Lxx10270(dapA)
            CMI: CMM_0810(dapX) CMM_2035(dapA)
            AAU: AAur_1077 AAur_1586(dapA) AAur_3966
            PAC: PPA0642 PPA1998
            TFU: Tfu_0791
            FRA: Francci3_3544
            FAL: FRAAL5738(dapA)
            ACE: Acel_1503
            SEN: SACE_1253(dapA4) SACE_1629(dapA) SACE_2548(dapA2)
                 SACE_3251(dapA1) SACE_4604(dapA) SACE_5158(dapAch1)
                 SACE_5899(dapA)
            BLO: BL1193(dapA)
            BAD: BAD_1297(dapA)
            RXY: Rxyl_0097 Rxyl_0325 Rxyl_2258
            RBA: RB1411 RB2746(dapA) RB4605(dapA) RB5277(dapA) RB8798(dapA)
            CTR: CT361(dapA)
            CTA: CTA_0393(dapA)
            CMU: TC0640
            CPN: CPn1050(dapA)
            CPA: CP0802
            CPJ: CPj1050(dapA)
            CPT: CpB1091
            CCA: CCA00712(dapA)
            CAB: CAB677(dapA)
            CFE: CF0306(dapA)
            PCU: pc0686(dapA)
            LIL: LA3306(dapA)
            LIC: LIC10842(dapA)
            LBJ: LBJ_0896(dapA)
            LBL: LBL_0911(dapA)
            SYN: slr0550(dapA)
            SYW: SYNW0067(dapA)
            SYC: syc2247_d(dapA)
            SYF: Synpcc7942_1847
            SYD: Syncc9605_0068(dapA)
            SYE: Syncc9902_0065(dapA)
            SYG: sync_0068(dapA)
            SYR: SynRCC307_0069(dapA)
            SYX: SynWH7803_0073(dapA)
            CYA: CYA_0627(dapA)
            CYB: CYB_0048(dapA)
            TEL: tlr1219(dapA)
            GVI: glr1018(dapA)
            ANA: all3679
            AVA: Ava_3607(dapA)
            PMA: Pro1813(dapA)
            PMM: PMM1653(dapA)
            PMT: PMT0065(dapA)
            PMN: PMN2A_1251
            PMI: PMT9312_1745
            PMB: A9601_18621(dapA)
            PMC: P9515_18431(dapA)
            PMF: P9303_00721(dapA)
            PMG: P9301_18431(dapA)
            PMH: P9215_19261
            PME: NATL1_21211(dapA)
            TER: Tery_0588
            BTH: BT_0895 BT_2814
            BFR: BF2404
            BFS: BF2486(dapA2) BF3862(dapA1)
            PGI: PG2052(dapA)
            SRU: SRU_1080(dapA)
            CHU: CHU_1312(dapA)
            GFO: GFO_0647(dapA)
            FPS: FP1836(dapA)
            CTE: CT1624(dapA)
            CCH: Cag_1734(dapA)
            PLT: Plut_1613(dapA)
            DET: DET0973(dapA)
            DEH: cbdb_A935(dapA)
            TTH: TTC0591
            TTJ: TTHA0957
            AAE: aq_1143(dapA)
            TMA: TM1521
            TPT: Tpet_1271
            FNO: Fnod_0072
            MMP: MMP0576(dapA)
            MMQ: MmarC5_1031
            MAE: Maeo_0908
            MVN: Mevan_1449
            MAC: MA4473(dapA)
            MBA: Mbar_A1150
            MMA: MM_1201
            MBU: Mbur_0147
            MTP: Mthe_0826
            MHU: Mhun_1492
            MLA: Mlab_0042
            MEM: Memar_1458
            MBN: Mboo_1396
            MST: Msp_0108(dapA)
            MSI: Msm_0831
            MKA: MK1607(dapA)
            HAL: VNG0444G(dapA)
            HMA: rrnAC0207(dapA) rrnAC0960(dapA2)
            HWA: HQ1507A(dapA) HQ2365A(dapA)
            NPH: NP1490A(dapA)
            TAC: Ta1157
            TVO: TVN1228
            PTO: PTO1279
            PAB: PAB0832(dapA)
            PFU: PF0657
            TKO: TK1237
            RCI: RCIX2091(dapA-2) RCIX736(dapA-1)
            APE: APE_1023.1
            SSO: SSO2274(dapA-1) SSO3035(dapA-2) SSO3072(dapA-3)
            STO: ST2235
            SAI: Saci_0162
            PAI: PAE2915
STRUCTURES  PDB: 1DHP  1O5K  1S5T  1S5V  1S5W  1XKY  1XL9  1XXX  1YXC  1YXD  
                 2A6L  2A6N  2ATS  2D5K  2EHH  2PCQ  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.52
            ExPASy - ENZYME nomenclature database: 4.2.1.52
            ExplorEnz - The Enzyme Database: 4.2.1.52
            ERGO genome analysis and discovery system: 4.2.1.52
            BRENDA, the Enzyme Database: 4.2.1.52
            CAS: 9055-59-8
///
ENTRY       EC 4.2.1.53                 Enzyme
NAME        oleate hydratase;
            (R)-10-hydroxystearate 10-hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (R)-10-hydroxystearate 10-hydro-lyase (oleate-forming)
REACTION    (R)-10-hydroxystearate = oleate + H2O [RN:R02813]
ALL_REAC    R02813
SUBSTRATE   (R)-10-hydroxystearate [CPD:C03195]
PRODUCT     oleate [CPD:C00712];
            H2O [CPD:C00001]
COMMENT     Acts on a number of 10-hydroxy acids.
REFERENCE   1  [PMID:5823715]
  AUTHORS   Davis EN, Wallen LL, Goodwin JC, Rohwedder WK, Rhodes RA.
  TITLE     Microbial hydration of cis-9-alkenoic acids.
  JOURNAL   Lipids. 4 (1969) 356-62.
REFERENCE   2  [PMID:3410394]
  AUTHORS   Gotouda H, Takatori T, Terazawa K, Nagao M, Tarao H.
  TITLE     The mechanism of experimental adipocere formation: hydration and
            dehydrogenation in microbial synthesis of hydroxy and oxo fatty
            acids.
  JOURNAL   Forensic. Sci. Int. 37 (1988) 249-57.
  ORGANISM  Flavobacterium meningosepticum
REFERENCE   3  [PMID:5492948]
  AUTHORS   Niehaus WG Jr, Torkelson A, Kisic A, Bednarczyk DJ, Schroepfer GJ
            Jr.
  TITLE     Stereospecific hydration of the delta-9 double bond of oleic acid.
  JOURNAL   J. Biol. Chem. 245 (1970) 3790-7.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.53
            ExPASy - ENZYME nomenclature database: 4.2.1.53
            ExplorEnz - The Enzyme Database: 4.2.1.53
            ERGO genome analysis and discovery system: 4.2.1.53
            BRENDA, the Enzyme Database: 4.2.1.53
            CAS: 9073-51-2
///
ENTRY       EC 4.2.1.54                 Enzyme
NAME        lactoyl-CoA dehydratase;
            lactoyl coenzyme A dehydratase;
            lactyl-coenzyme A dehydrase;
            lactyl CoA dehydratase;
            acrylyl coenzyme A hydratase;
            lactoyl-CoA hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     lactoyl-CoA hydro-lyase (acryloyl-CoA-forming)
REACTION    lactoyl-CoA = acryloyl-CoA + H2O [RN:R02963]
ALL_REAC    R02963
SUBSTRATE   lactoyl-CoA [CPD:C00827]
PRODUCT     acryloyl-CoA [CPD:C00894];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:14292829]
  AUTHORS   BALDWIN RL, WOOD WA, EMERY RS.
  TITLE     LACTATE METABOLISM BY PEPTOSTREPTOCOCCUS ELSDENII: EVIDENCE FOR
            LACTYL COENZYME A DEHYDRASE.
  JOURNAL   Biochim. Biophys. Acta. 97 (1965) 202-13.
  ORGANISM  Peptostreptococcus elsdenii
PATHWAY     PATH: map00640  Propanoate metabolism
            PATH: map00643  Styrene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.54
            ExPASy - ENZYME nomenclature database: 4.2.1.54
            ExplorEnz - The Enzyme Database: 4.2.1.54
            ERGO genome analysis and discovery system: 4.2.1.54
            UM-BBD (Biocatalysis/Biodegradation Database): 4.2.1.54
            BRENDA, the Enzyme Database: 4.2.1.54
            CAS: 9031-12-3
///
ENTRY       EC 4.2.1.55                 Enzyme
NAME        3-hydroxybutyryl-CoA dehydratase;
            D-3-hydroxybutyryl coenzyme A dehydratase;
            D-3-hydroxybutyryl-CoA dehydratase;
            enoyl coenzyme A hydrase (D);
            (3R)-3-hydroxybutanoyl-CoA hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (3R)-3-hydroxybutanoyl-CoA hydro-lyase (crotonoyl-CoA-forming)
REACTION    (3R)-3-hydroxybutanoyl-CoA = crotonoyl-CoA + H2O [RN:R03027]
ALL_REAC    R03027
SUBSTRATE   (3R)-3-hydroxybutanoyl-CoA [CPD:C03561]
PRODUCT     crotonoyl-CoA [CPD:C00877];
            H2O [CPD:C00001]
COMMENT     Also acts on crotonoyl thioesters of pantetheine and acyl-carrier
            protein.
REFERENCE   1  [PMID:5808333]
  AUTHORS   Moskowitz GJ, Merrick JM.
  TITLE     Metabolism of poly-beta-hydroxybutyrate. II. Enzymatic synthesis of
            D-(-)-beta hydroxybutyryl coenzyme A by an enoyl hydrase from
            Rhodospirillum rubrum.
  JOURNAL   Biochemistry. 8 (1969) 2748-55.
  ORGANISM  Rhodospirillum rubrum [GN:rru]
PATHWAY     PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K01715  3-hydroxybutyryl-CoA dehydratase
GENES       ECP: ECP_4456
            XCC: XCC1534(crt)
            XCB: XC_2700
            XCV: XCV1625
            XAC: XAC1584(crt)
            XOO: XOO2452(crt)
            XOM: XOO_2323(XOO2323)
            PHA: PSHAa1457
            LPN: lpg0869
            LPF: lpl0901
            LPP: lpp0932
            HCH: HCH_05047
            AHA: AHA_2081
            REH: H16_B1189(crt) H16_B1843 H16_B2534
            BXE: Bxe_C0643 Bxe_C0855
            BPE: BP3706
            BBR: BB4306
            MPT: Mpe_A2659
            HAR: HEAR2723(croA)
            GSU: GSU1377
            GME: Gmet_1716 Gmet_2212
            ADE: Adeh_1645 Adeh_1666
            MXA: MXAN_3757(crt) MXAN_3799(crt)
            RLE: RL1822
            BME: BMEI0022 BMEI0023 BMEII0214
            BJA: blr7857
            RPC: RPC_0858
            BAN: BA0894
            BAR: GBAA0894 GBAA2551
            BAA: BA_1476 BA_3053
            BAT: BAS0848 BAS2374
            BCE: BC0898 BC2487 BC4524
            BCA: BCE_0979 BCE_2552
            BCZ: BCZK0796(crt) BCZK1205(crt) BCZK2290(crt)
            BTK: BT9727_0791(crt) BT9727_2331(crt) BT9727_2708(crt)
            BTL: BALH_0805(crt) BALH_2292(crt) BALH_2655(crt)
            GKA: GK1914
            CAC: CAC2712(crt)
            CPE: CPE0095 CPE2301(crt)
            CPF: CPF_0090 CPF_2585(crt)
            CPR: CPR_2287(crt)
            CTC: CTC00479 CTC02427
            CNO: NT01CX_0474
            CDF: CD0800(crt1) CD1057(crt2)
            CBO: CBO3202(crt)
            CBA: CLB_3238(crt)
            CBH: CLC_3112(crt)
            CBF: CLI_3341
            CKL: CKL_0454(crt1) CKL_2527(crt2)
            CHY: CHY_1293(crt1) CHY_1601(crt2)
            DSY: DSY1709
            SWO: Swol_1936
            TTE: TTE0544(caiD)
            MSM: MSMEG_4119
            CEF: CE0322
            RHA: RHA1_ro04749 RHA1_ro11035
            AAU: AAur_3259(crt)
            FNU: FN1020
            PGI: PG1079
            GFO: GFO_3215
            FPS: FP0049(crt)
            DRA: DR_1151
            DGE: Dgeo_1595
            TTJ: TTHA1434
            PTO: PTO1021
            STO: ST1516
            SAI: Saci_1633(paaF)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.55
            ExPASy - ENZYME nomenclature database: 4.2.1.55
            ExplorEnz - The Enzyme Database: 4.2.1.55
            ERGO genome analysis and discovery system: 4.2.1.55
            BRENDA, the Enzyme Database: 4.2.1.55
            CAS: 37290-82-7
///
ENTRY       EC 4.2.1.56                 Enzyme
NAME        itaconyl-CoA hydratase;
            itaconyl coenzyme A hydratase;
            citramalyl-CoA hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     citramalyl-CoA hydro-lyase (itaconyl-CoA-forming)
REACTION    citramalyl-CoA = itaconyl-CoA + H2O [RN:R02490]
ALL_REAC    R02490 > R02491
SUBSTRATE   citramalyl-CoA [CPD:C00904]
PRODUCT     itaconyl-CoA [CPD:C00531];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:4284209]
  AUTHORS   Cooper RA, Kornberg HL.
  TITLE     The utilization of itaconate by Pseudomonas sp.
  JOURNAL   Biochem. J. 91 (1964) 82-91.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00660  C5-Branched dibasic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.56
            ExPASy - ENZYME nomenclature database: 4.2.1.56
            ExplorEnz - The Enzyme Database: 4.2.1.56
            ERGO genome analysis and discovery system: 4.2.1.56
            BRENDA, the Enzyme Database: 4.2.1.56
            CAS: 37290-83-8
///
ENTRY       EC 4.2.1.57                 Enzyme
NAME        isohexenylglutaconyl-CoA hydratase;
            3-hydroxy-3-isohexenylglutaryl-CoA-hydrolase;
            isohexenylglutaconyl coenzyme A hydratase;
            beta-isohexenylglutaconyl-CoA-hydratase;
            3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA hydro-lyase
            [3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA-forming]
REACTION    3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA =
            3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA + H2O [RN:R03493]
ALL_REAC    R03493
SUBSTRATE   3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA [CPD:C04675]
PRODUCT     3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA;
            H2O [CPD:C00001]
COMMENT     Also acts on dimethylacryloyl-CoA and farnesoyl-CoA.
REFERENCE   1  [PMID:14339651]
  AUTHORS   SEUBERT W, FASS E.
  TITLE     [STUDIES ON THE BACTERIAL DEGRADATION OF ISOPRENOIDS. IV. THE
            PURIFICATION AND PROPERTIES OF
            BETA-ISOHEXENYLGLUTACONYL-COA-HYDRATASE AND
            BETA-HYDROXY-BETA-ISOHEXENYLGLUTARYL-COA-LYASE.]
  JOURNAL   Biochem. Z. 341 (1964) 23-34.
  ORGANISM  Pseudomonas citronellolis
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.57
            ExPASy - ENZYME nomenclature database: 4.2.1.57
            ExplorEnz - The Enzyme Database: 4.2.1.57
            ERGO genome analysis and discovery system: 4.2.1.57
            UM-BBD (Biocatalysis/Biodegradation Database): 4.2.1.57
            BRENDA, the Enzyme Database: 4.2.1.57
            CAS: 37290-84-9
///
ENTRY       EC 4.2.1.58                 Enzyme
NAME        crotonoyl-[acyl-carrier-protein] hydratase;
            (3R)-3-hydroxybutanoyl-[acyl-carrier-protein] hydro-lyase;
            beta-hydroxybutyryl acyl carrier protein dehydrase;
            beta-hydroxybutyryl acyl carrier protein (ACP) dehydrase;
            beta-hydroxybutyryl acyl carrier protein dehydrase;
            enoyl acyl carrier protein hydrase;
            crotonyl acyl carrier protein hydratase;
            3-hydroxybutyryl acyl carrier protein dehydratase;
            beta-hydroxybutyryl acyl carrier;
            protein dehydrase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (3R)-3-hydroxybutanoyl-[acyl-carrier-protein] hydro-lyase
            (but-2-enoyl-[acyl-carrier protein]-forming)
REACTION    (3R)-3-hydroxybutanoyl-[acyl-carrier-protein] =
            but-2-enoyl-[acyl-carrier-protein] + H2O [RN:R04428]
ALL_REAC    R04428;
            (other) R04535 R04537 R04954 R04965
SUBSTRATE   (3R)-3-hydroxybutanoyl-[acyl-carrier-protein]
PRODUCT     but-2-enoyl-[acyl-carrier-protein];
            H2O [CPD:C00001]
COMMENT     Is specific for short chain-length
            3-hydroxyacyl-[acyl-carrier-protein] derivatives (C4 to C8).
REFERENCE   1  [PMID:14275113]
  AUTHORS   MAJERUS PW, ALBERTS AW, VAGELOS PR.
  TITLE     ACYL CARRIER PROTEIN. 3. AN ENOYL HYDRASE SPECIFIC FOR ACYL CARRIER
            PROTEIN THIOESTERS.
  JOURNAL   J. Biol. Chem. 240 (1965) 618-21.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:5658542]
  AUTHORS   Mizugaki M, Weeks G, Toomey RE, Wakil SJ.
  TITLE     Studies on the mechanism of fatty acid synthesis. XX. Preparation
            and general properties of beta-hydroxybutyryl acyl carrier protein
            dehydrase.
  JOURNAL   J. Biol. Chem. 243 (1968) 3661-70.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00061  Fatty acid biosynthesis
GENES       CVI: CV_2207(fabZ)
            AMA: AM1098(fabZ)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.58
            ExPASy - ENZYME nomenclature database: 4.2.1.58
            ExplorEnz - The Enzyme Database: 4.2.1.58
            ERGO genome analysis and discovery system: 4.2.1.58
            BRENDA, the Enzyme Database: 4.2.1.58
            CAS: 9030-78-8
///
ENTRY       EC 4.2.1.59                 Enzyme
NAME        3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase;
            D-3-hydroxyoctanoyl-[acyl carrier protein] dehydratase;
            D-3-hydroxyoctanoyl-acyl carrier protein dehydratase;
            beta-hydroxyoctanoyl-acyl carrier protein dehydrase;
            beta-hydroxyoctanoyl thioester dehydratase;
            beta-hydroxyoctanoyl-ACP-dehydrase;
            (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase
            (oct-2-enoyl-[acyl-carrier protein]-forming)
REACTION    (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] =
            oct-2-enoyl-[acyl-carrier-protein] + H2O [RN:R04537]
ALL_REAC    R04537
SUBSTRATE   (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein]
PRODUCT     oct-2-enoyl-[acyl-carrier-protein];
            H2O [CPD:C00001]
COMMENT     The enzyme is specific for 3-hydroxyacyl-[acyl-carrier-protein]
            derivatives (C6 to C12).
REFERENCE   1  [PMID:4881058]
  AUTHORS   Mizugaki M, Swindell AC, Wakil SJ.
  TITLE     Intermediate- and long-chain beta-hydroxyacyl-ACP dehydrases from E.
            coli fatty acid synthetase.
  JOURNAL   Biochem. Biophys. Res. Commun. 33 (1968) 520-7.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.59
            ExPASy - ENZYME nomenclature database: 4.2.1.59
            ExplorEnz - The Enzyme Database: 4.2.1.59
            ERGO genome analysis and discovery system: 4.2.1.59
            BRENDA, the Enzyme Database: 4.2.1.59
            CAS: 9030-85-7
///
ENTRY       EC 4.2.1.60                 Enzyme
NAME        3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase;
            D-3-hydroxydecanoyl-[acyl-carrier protein] dehydratase;
            3-hydroxydecanoyl-acyl carrier protein dehydrase;
            3-hydroxydecanoyl-acyl carrier protein dehydratase;
            beta-hydroxydecanoyl thioester dehydrase;
            beta-hydroxydecanoate dehydrase;
            beta-hydroxydecanoyl thiol ester dehydrase;
            FabA;
            beta-hydroxyacyl-acyl carrier protein dehydratase;
            HDDase;
            beta-hydroxyacyl-ACP dehydrase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] hydro-lyase
REACTION    (1) (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] =
            trans-dec-2-enoyl-[acyl-carrier-protein] + H2O [RN:R04414];
            (2) (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] =
            cis-dec-3-enoyl-[acyl-carrier-protein] + H2O [RN:R04416]
ALL_REAC    R04414 > R04535;
            R04416;
            (other) R04965
SUBSTRATE   (3R)-3-hydroxydecanoyl-[acyl-carrier-protein]
PRODUCT     trans-dec-2-enoyl-[acyl-carrier-protein];
            H2O [CPD:C00001];
            cis-dec-3-enoyl-[acyl-carrier-protein]
COMMENT     Specific for C10 chain length.
REFERENCE   1  [PMID:4863739]
  AUTHORS   Kass LR, Brock DJ, Bloch K.
  TITLE     Beta-hydroxydecanoyl thioester dehydrase. I. Purification and
            properties.
  JOURNAL   J. Biol. Chem. 242 (1967) 4418-31.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4863740]
  AUTHORS   Brock DJ, Kass LR, Bloch K.
  TITLE     Beta-hydroxydecanoyl thioester dehydrase. II. Mode of action.
  JOURNAL   J. Biol. Chem. 242 (1967) 4432-40.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:2180957]
  AUTHORS   Sharma A, Henderson BS, Schwab JM, Smith JL.
  TITLE     Crystallization and preliminary X-ray analysis of
            beta-hydroxydecanoyl thiol ester dehydrase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 265 (1990) 5110-2.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:8246839]
  AUTHORS   Magnuson K, Jackowski S, Rock CO, Cronan JE Jr.
  TITLE     Regulation of fatty acid biosynthesis in Escherichia coli.
  JOURNAL   Microbiol. Rev. 57 (1993) 522-42.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5
  AUTHORS   Bloch, K.
  TITLE     Enzymatic synthesis of monounsaturated fatty acids.
  JOURNAL   Acc. Chem. Res. 2 (1969) 193-202.
REFERENCE   6  [PMID:15194690]
  AUTHORS   Wang H, Cronan JE.
  TITLE     Functional replacement of the FabA and FabB proteins of Escherichia
            coli fatty acid synthesis by Enterococcus faecalis FabZ and FabF
            homologues.
  JOURNAL   J. Biol. Chem. 279 (2004) 34489-95.
  ORGANISM  Escherichia coli [GN:eco], Enterococcus faecalis [GN:efa]
REFERENCE   7
  AUTHORS   Cronan, J.E., Jr. and Rock, C.O.
  TITLE     Biosynthesis of membrane lipids.
  JOURNAL   In: Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular
            and Molecular Biology, 2nd ed., vol. 1, ASM Press, Washington, DC,
            1996, p. 612-636.
PATHWAY     PATH: map00061  Fatty acid biosynthesis
ORTHOLOGY   KO: K01716  3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
GENES       ECO: b0954(fabA)
            ECJ: JW0937(fabA)
            ECE: Z1304(fabA)
            ECS: ECs1038
            ECC: c1090(fabA)
            ECI: UTI89_C1019(fabA)
            ECP: ECP_0959
            ECV: APECO1_59(fabA)
            STY: STY1088(fabA)
            STT: t1853(fabA)
            SPT: SPA1783(fabA)
            SEC: SC1019(fabA)
            STM: STM1067(fabA)
            YPE: YPO1430(fabA)
            YPK: y2740(fabA)
            YPM: YP_0875(fabA)
            YPA: YPA_0723
            YPN: YPN_2548
            YPP: YPDSF_1543
            YPS: YPTB1450(fabA)
            SFL: SF0954(fabA)
            SFX: S1020(fabA)
            SFV: SFV_0962(fabA)
            SSN: SSON_0958(fabA)
            SBO: SBO_2277(fabA)
            SDY: SDY_0927(fabA)
            ECA: ECA1748(fabA)
            PLU: plu1772(fabA)
            WBR: WGLp300(fabA)
            SGL: SG1026
            ENT: Ent638_1466
            SPE: Spro_1751
            BFL: Bfl420(fabA)
            BPN: BPEN_432(fabA)
            HIT: NTHI1649(fabA)
            HIP: CGSHiEE_04990
            HIQ: CGSHiGG_01270
            HDU: HD0181(fabA)
            HSO: HS_0907(fabA)
            PMU: PM0484(fabA)
            MSU: MS1194(fabA)
            APL: APL_1889(fabA)
            ASU: Asuc_1443
            XFA: XF0572
            XFT: PD1572(fabA)
            XCC: XCC0582(fabA)
            XCB: XC_3651
            XCV: XCV3741(fabA)
            XAC: XAC3623(fabA)
            XOO: XOO0762(fabA)
            XOM: XOO_0692(XOO0692)
            VCH: VC1483
            VCO: VC0395_A1091(fabA)
            VVU: VV1_2629
            VVY: VV1662
            VPA: VP1591
            VFI: VF1292
            PPR: PBPRA1773
            PAE: PA1610(fabA)
            PAU: PA14_43680(fabA)
            PPU: PP_4174(fabA)
            PPF: Pput_1694
            PST: PSPTO_2211(fabA)
            PSB: Psyr_2020
            PSP: PSPPH_1990(fabA)
            PFL: PFL_1737(fabA)
            PFO: Pfl_4212(fabA)
            PEN: PSEEN3622(fabA)
            PMY: Pmen_2469
            SON: SO_1856(fabA)
            SDN: Sden_2465
            SFR: Sfri_2656
            SAZ: Sama_1605
            SBL: Sbal_2565
            SBM: Shew185_2605
            SLO: Shew_1817
            SPC: Sputcn32_1637
            SSE: Ssed_2468
            SPL: Spea_1951
            SHE: Shewmr4_1545
            SHM: Shewmr7_1612
            SHN: Shewana3_1606
            SHW: Sputw3181_2388
            ILO: IL1287(fabA)
            CPS: CPS_3274(fabA)
            PHA: PSHAa1491(fabA)
            PAT: Patl_2009
            SDE: Sde_0999
            PIN: Ping_1982
            MAQ: Maqu_3147
            CBU: CBU_0037(fabA)
            MCA: MCA2878(fabA)
            TCX: Tcr_1946
            NOC: Noc_2113
            AEH: Mlg_1374
            HHA: Hhal_0017
            CSA: Csal_0457
            ABO: ABO_0835(fabA)
            MMW: Mmwyl1_4241
            AHA: AHA_2280(fabA)
            DNO: DNO_0314(fabA)
            BCI: BCI_0410(fabA)
            RMA: Rmag_1003
            VOK: COSY_0899(fabA)
            REH: H16_A2044
            AAV: Aave_4181
            AJS: Ajs_0525
            VEI: Veis_2159
            MFA: Mfla_1894
            SAT: SYN_01697
            PUB: SAR11_0397(fabA)
            MLO: mll5569
            MES: Meso_3939
            PLA: Plav_3636
            SME: SMc00328(fabA)
            SMD: Smed_3450
            ATU: Atu0151(fabA)
            ATC: AGR_C_246
            RET: RHE_CH00107(fabA)
            RLE: RL0116(fabA)
            BME: BMEI1956
            BMF: BAB1_2174(fabA)
            BMS: BR2173(fabA)
            BMB: BruAb1_2146(fabA)
            OAN: Oant_0739
            BJA: bll4346(fabA) blr0769(fabA)
            BRA: BRADO0063(fabA) BRADO2366(fabA)
            BBT: BBta_0069(fabA) BBta_2720(fabA)
            RPA: RPA0425(fabA)
            RPB: RPB_0613
            RPC: RPC_0349
            RPD: RPD_0220
            RPE: RPE_0257
            NWI: Nwi_0034 Nwi_1578
            NHA: Nham_0042 Nham_2101
            BHE: BH01290(fabA)
            BQU: BQ01220(fabA)
            XAU: Xaut_0054
            CCR: CC_3720
            SIL: SPOA0444(fabA)
            SIT: TM1040_0182
            RSP: RSP_3178(fabA)
            RSH: Rsph17029_3915
            JAN: Jann_1653
            RDE: RD1_3923(fabA)
            PDE: Pden_1649
            MMR: Mmar10_3060
            HNE: HNE_3435(fabZ)
            ELI: ELI_06745(fabA)
            BPU: BPUM_3286(fabZ)
            SPA: M6_Spy1481
            LSL: LSL_0457(fabA)
            CGB: cg0957(fas-IB) cg2743(fas-IA)
            FAL: FRAAL3194
            SEN: SACE_0023
            AVA: Ava_4750
            PMB: A9601_15361(fabZ)
            PMC: P9515_14971(fabZ)
            PMF: P9303_05511(fabZ)
            PMG: P9301_15221(fabZ)
            PME: NATL1_17631(fabZ)
            CHU: CHU_0969(fabA)
STRUCTURES  PDB: 1MKA  1MKB  2OKI  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.60
            ExPASy - ENZYME nomenclature database: 4.2.1.60
            ExplorEnz - The Enzyme Database: 4.2.1.60
            ERGO genome analysis and discovery system: 4.2.1.60
            BRENDA, the Enzyme Database: 4.2.1.60
            CAS: 9030-79-9
///
ENTRY       EC 4.2.1.61                 Enzyme
NAME        3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase;
            D-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase;
            beta-hydroxypalmitoyl-acyl carrier protein dehydrase;
            beta-hydroxypalmitoyl thioester dehydratase;
            beta-hydroxypalmityl-ACP dehydrase;
            (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] hydro-lyase
            (hexadec-2-enoyl-[acyl-carrier protein]-forming)
REACTION    (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] =
            hexadec-2-enoyl-[acyl-carrier-protein] + H2O [RN:R04462]
ALL_REAC    R04462 > R04544;
            (other) R04535 R04537 R04568 R04965
SUBSTRATE   (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein]
PRODUCT     hexadec-2-enoyl-[acyl-carrier-protein];
            H2O [CPD:C00001]
COMMENT     The enzyme is specific for 3-hydroxyacyl-[acyl-carrier-protein]
            derivatives (C12 to C16), and has the highest activity on the C16
            derivative.
REFERENCE   1  [PMID:4881058]
  AUTHORS   Mizugaki M, Swindell AC, Wakil SJ.
  TITLE     Intermediate- and long-chain beta-hydroxyacyl-ACP dehydrases from E.
            coli fatty acid synthetase.
  JOURNAL   Biochem. Biophys. Res. Commun. 33 (1968) 520-7.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00061  Fatty acid biosynthesis
ORTHOLOGY   KO: K01717  3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
GENES       HSA: 2194(FASN)
            MMU: 14104(Fasn)
            RNO: 50671(Fasn)
            BTA: 281152(FASN)
            GGA: 396061(FASN)
            CEL: F32H2.5(fasn-1)
            SCE: YKL182W(FAS1)
            AGO: AGOS_AER085C
            CGR: CAGL0D00528g
            SPO: SPAC926.09c(fas1)
            CNE: CNE04370
            CVI: CV_3950
            CGB: cg0957(fas-IB) cg2743(fas-IA)
STRUCTURES  PDB: 2PFF  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.61
            ExPASy - ENZYME nomenclature database: 4.2.1.61
            ExplorEnz - The Enzyme Database: 4.2.1.61
            ERGO genome analysis and discovery system: 4.2.1.61
            BRENDA, the Enzyme Database: 4.2.1.61
            CAS: 9030-86-8
///
ENTRY       EC 4.2.1.62                 Enzyme
NAME        5alpha-hydroxysteroid dehydratase;
            5alpha-ergosta-7,22-diene-3beta,5-diol 5,6-hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     5alpha-ergosta-7,22-diene-3beta,5-diol 5,6-hydro-lyase
            (ergosterol-forming)
REACTION    5alpha-ergosta-7,22-diene-3beta,5-diol = ergosterol + H2O
            [RN:R03675]
ALL_REAC    R03675
SUBSTRATE   5alpha-ergosta-7,22-diene-3beta,5-diol [CPD:C04416]
PRODUCT     ergosterol [CPD:C01694];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:5442273]
  AUTHORS   Topham RW, Gaylor JL.
  TITLE     Isolation and purification of a 5 alpha-hydroxysterol dehydrase of
            yeast.
  JOURNAL   J. Biol. Chem. 245 (1970) 2319-27.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.62
            ExPASy - ENZYME nomenclature database: 4.2.1.62
            ExplorEnz - The Enzyme Database: 4.2.1.62
            ERGO genome analysis and discovery system: 4.2.1.62
            BRENDA, the Enzyme Database: 4.2.1.62
            CAS: 9075-27-8
///
ENTRY       EC 4.2.1.63       Obsolete  Enzyme
NAME        Transferred to 3.3.2.9 and 3.3.2.10
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
COMMENT     Transferred entry: Now known to comprise two enzymes, microsomal
            epoxide hydrolase (EC 3.3.2.9) and soluble epoxide hydrolase (EC
            3.3.2.10) (EC 4.2.1.63 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.63
            ExPASy - ENZYME nomenclature database: 4.2.1.63
            ExplorEnz - The Enzyme Database: 4.2.1.63
            ERGO genome analysis and discovery system: 4.2.1.63
            BRENDA, the Enzyme Database: 4.2.1.63
///
ENTRY       EC 4.2.1.64       Obsolete  Enzyme
NAME        Transferred to 3.3.2.9 and 3.3.2.10
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
COMMENT     Transferred entry: Now known to comprise two enzymes, microsomal
            epoxide hydrolase (EC 3.3.2.9) and soluble epoxide hydrolase (EC
            3.3.2.10). (EC 4.2.1.64 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.64
            ExPASy - ENZYME nomenclature database: 4.2.1.64
            ExplorEnz - The Enzyme Database: 4.2.1.64
            ERGO genome analysis and discovery system: 4.2.1.64
            BRENDA, the Enzyme Database: 4.2.1.64
///
ENTRY       EC 4.2.1.65                 Enzyme
NAME        3-cyanoalanine hydratase;
            beta-cyanoalanine hydrolase;
            beta-cyanoalanine hydratase;
            beta-CNAla hydrolase;
            beta-CNA nitrilase;
            L-asparagine hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     L-asparagine hydro-lyase (3-cyanoalanine-forming)
REACTION    L-asparagine = 3-cyanoalanine + H2O [RN:R01267]
ALL_REAC    R01267
SUBSTRATE   L-asparagine [CPD:C00152]
PRODUCT     3-cyanoalanine;
            H2O [CPD:C00001]
REFERENCE   1  [PMID:4627358]
  AUTHORS   Castric PA, Farnden KJ, Conn EE.
  TITLE     Cyanide metabolism in higher plants. V. The formation of asparagine
            from  -cyanoalanine.
  JOURNAL   Arch. Biochem. Biophys. 152 (1972) 62-9.
  ORGANISM  Sorghum vulgare, Lupinus angustifolius
PATHWAY     PATH: map00460  Cyanoamino acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.65
            ExPASy - ENZYME nomenclature database: 4.2.1.65
            ExplorEnz - The Enzyme Database: 4.2.1.65
            ERGO genome analysis and discovery system: 4.2.1.65
            BRENDA, the Enzyme Database: 4.2.1.65
            CAS: 37259-64-6
///
ENTRY       EC 4.2.1.66                 Enzyme
NAME        cyanide hydratase;
            formamide dehydratase;
            formamide hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     formamide hydro-lyase (cyanide-forming)
REACTION    formamide = cyanide + H2O [RN:R01408]
ALL_REAC    R01408
SUBSTRATE   formamide [CPD:C00488]
PRODUCT     cyanide [CPD:C00177];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:5065258]
  AUTHORS   Fry WE, Millar RL.
  TITLE     Cyanide degradion by an enzyme from Stemphylium loti.
  JOURNAL   Arch. Biochem. Biophys. 151 (1972) 468-74.
  ORGANISM  Stemphylium loti
PATHWAY     PATH: map00460  Cyanoamino acid metabolism
GENES       AFM: AFUA_2G17500
            BPU: BPUM_0296(ykrU)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.66
            ExPASy - ENZYME nomenclature database: 4.2.1.66
            ExplorEnz - The Enzyme Database: 4.2.1.66
            ERGO genome analysis and discovery system: 4.2.1.66
            BRENDA, the Enzyme Database: 4.2.1.66
            CAS: 37292-83-4
///
ENTRY       EC 4.2.1.67                 Enzyme
NAME        D-fuconate dehydratase;
            D-fuconate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     D-fuconate hydro-lyase (2-dehydro-3-deoxy-D-fuconate-forming)
REACTION    D-fuconate = 2-dehydro-3-deoxy-D-fuconate + H2O [RN:R03671]
ALL_REAC    R03671
SUBSTRATE   D-fuconate [CPD:C01680]
PRODUCT     2-dehydro-3-deoxy-D-fuconate [CPD:C06159];
            H2O [CPD:C00001]
COMMENT     Also acts on L-arabinonate.
REFERENCE   1  [PMID:4335868]
  AUTHORS   Dahms AS, Anderson RL.
  TITLE     D-Fucose metabolism in a pseudomonad. 3. Conversion of D-fuconate to
            2-keto-3-deoxy-D-fuconate by a dehydratase.
  JOURNAL   J. Biol. Chem. 247 (1972) 2233-7.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00051  Fructose and mannose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.67
            ExPASy - ENZYME nomenclature database: 4.2.1.67
            ExplorEnz - The Enzyme Database: 4.2.1.67
            ERGO genome analysis and discovery system: 4.2.1.67
            BRENDA, the Enzyme Database: 4.2.1.67
            CAS: 9076-59-9
///
ENTRY       EC 4.2.1.68                 Enzyme
NAME        L-fuconate dehydratase;
            L-fuconate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     L-fuconate hydro-lyase (2-dehydro-3-deoxy-L-fuconate-forming)
REACTION    L-fuconate = 2-dehydro-3-deoxy-L-fuconate + H2O [RN:R03688]
ALL_REAC    R03688
SUBSTRATE   L-fuconate [CPD:C01720]
PRODUCT     2-dehydro-3-deoxy-L-fuconate [CPD:C03827];
            H2O [CPD:C00001]
COMMENT     Also acts, slowly, on D-arabinonate.
REFERENCE   1  [PMID:5050937]
  AUTHORS   Yuen R, Schachter H.
  TITLE     L-Fucose metabolism in mammals. I. Port liver L-fuconate
            hydro-lyase.
  JOURNAL   Can. J. Biochem. 50 (1972) 798-806.
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.68
            ExPASy - ENZYME nomenclature database: 4.2.1.68
            ExplorEnz - The Enzyme Database: 4.2.1.68
            ERGO genome analysis and discovery system: 4.2.1.68
            BRENDA, the Enzyme Database: 4.2.1.68
            CAS: 37292-84-5
///
ENTRY       EC 4.2.1.69                 Enzyme
NAME        cyanamide hydratase;
            urea hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     urea hydro-lyase (cyanamide-forming)
REACTION    urea = cyanamide + H2O [RN:R00778]
ALL_REAC    R00778
SUBSTRATE   urea [CPD:C00086]
PRODUCT     cyanamide [CPD:C01566];
            H2O [CPD:C00001]
REFERENCE   1
  AUTHORS   Stransky, H. and Amberger, A.
  TITLE     Isolation and properties of a cyanamide hydratase (EC 4.2.1) from
            Myrothecium verrucaria.
  JOURNAL   Z. Pflanzenphysiol. 70 (1973) 74-87.
  ORGANISM  Myrothecium verrucaria
PATHWAY     PATH: map00791  Atrazine degradation
ORTHOLOGY   KO: K06035  cyanamide hydratase
GENES       AFM: AFUA_7G06270
            RHA: RHA1_ro07109
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.69
            ExPASy - ENZYME nomenclature database: 4.2.1.69
            ExplorEnz - The Enzyme Database: 4.2.1.69
            ERGO genome analysis and discovery system: 4.2.1.69
            UM-BBD (Biocatalysis/Biodegradation Database): 4.2.1.69
            BRENDA, the Enzyme Database: 4.2.1.69
            CAS: 50812-20-9
///
ENTRY       EC 4.2.1.70                 Enzyme
NAME        pseudouridylate synthase;
            pseudouridylic acid synthetase;
            pseudouridine monophosphate synthetase;
            5-ribosyluracil 5-phosphate synthetase;
            pseudouridylate synthetase;
            upsilonUMP synthetase;
            uracil hydro-lyase (adding D-ribose 5-phosphate)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     uracil hydro-lyase (adding D-ribose 5-phosphate;
            pseudouridine-5'-phosphate-forming)
REACTION    uracil + D-ribose 5-phosphate = pseudouridine 5'-phosphate + H2O
            [RN:R01055]
ALL_REAC    R01055
SUBSTRATE   uracil [CPD:C00106];
            D-ribose 5-phosphate [CPD:C00117]
PRODUCT     pseudouridine 5'-phosphate [CPD:C01168];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:14165924]
  AUTHORS   HEINRIKSON RL, GOLDWASSER E.
  TITLE     STUDIES ON THE BIOSYNTHESIS OF 5-RIBOSYLURACIL  5'-MONOPHOSPHATE IN
            TETRAHYMENA PYRIFORMIS.
  JOURNAL   J. Biol. Chem. 239 (1964) 1177-87.
  ORGANISM  Tetrahymena pyriformis
REFERENCE   2  [PMID:4936431]
  AUTHORS   Matsushita T, Davis FF.
  TITLE     Studies on pseudouridylic acid synthetase from various sources.
  JOURNAL   Biochim. Biophys. Acta. 238 (1971) 165-73.
  ORGANISM  Agrobacterium tumefaciens
REFERENCE   3  [PMID:4569284]
  AUTHORS   Remsen JF, Matsushita T, Chirikjian JG, Davis FF.
  TITLE     Enzymatic synthesis of deoxypseudouridylic acid and a study of
            certain of its properties.
  JOURNAL   Biochim. Biophys. Acta. 281 (1972) 481-7.
  ORGANISM  Tetrahymena pyriformis, Escherichia coli [GN:eco]
REFERENCE   4  [PMID:5942965]
  AUTHORS   Suzuki T, Hochster RM.
  TITLE     On the biosynthesis of pseudouridine and of pseudouridylic acid in
            Agrobacterium tumefaciens.
  JOURNAL   Can. J. Biochem. 44 (1966) 259-72.
  ORGANISM  Agrobacterium tumefaciens
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K01718  pseudouridylate synthase
GENES       GGA: 428833(RPUSD2)
            DME: Dmel_CG3045 Dmel_CG31719(RluA-1) Dmel_CG6187(RluA-2)
            CEL: E02H1.3(tag-124)
            CME: CMD024C CMK183C
            SCE: YGL063W(PUS2) YNL292W(PUS4)
            AGO: AGOS_AEL198W
            PIC: PICST_33477(RIB2) PICST_50850(PUS5) PICST_61490(RIB6)
                 PICST_63360 PICST_64832(CBF5) PICST_84338(DEG1)
            CGR: CAGL0C05291g CAGL0H03685g CAGL0M03619g
            SPO: SPAC25B8.05 SPBC11C11.10 SPCC16C4.06c
            AFM: AFUA_2G16360 AFUA_5G05710 AFUA_5G12310
            AOR: AO090120000348
            CNE: CNC01370 CNI00670
            UMA: UM03057.1
            DDI: DDBDRAFT_0217957 DDB_0231223(pus3)
            PFA: PF10_0175 PFB0890c PFE1080w PFI0420c PFI0685w PFL1350w
            TAN: TA11550 TA16810
            TBR: Tb09.160.5220 Tb10.70.0780 Tb11.01.1080 Tb11.01.8410
                 Tb927.6.2970 Tb927.7.1510
            TCR: 503579.110 507517.100
            LMA: LmjF26.0420 LmjF30.1550 LmjF36.1660
            EHI: 8.t00006
            YPP: YPDSF_2913 YPDSF_3137 YPDSF_3543
            YEN: YE2636(rluA)
            ENT: Ent638_0605 Ent638_1096 Ent638_3074 Ent638_3216 Ent638_3244
                 Ent638_3603
            HIT: NTHI0050(rluA2)
            VFI: VF1020
            PAU: PA14_38090
            PEN: PSEEN3759
            ACI: ACIAD2377
            SDN: Sden_0111 Sden_2524
            SFR: Sfri_0092 Sfri_0515 Sfri_0992 Sfri_2706
            SAZ: Sama_0963 Sama_1131 Sama_2197
            SBL: Sbal_0733 Sbal_1442 Sbal_2791
            SLO: Shew_0783 Shew_2643
            SPC: Sputcn32_0834 Sputcn32_1022 Sputcn32_1339 Sputcn32_2231
                 Sputcn32_2488 Sputcn32_2753
            SHE: Shewmr4_0283 Shewmr4_1377 Shewmr4_2650 Shewmr4_3139
            SHM: Shewmr7_0827 Shewmr7_1442 Shewmr7_2717 Shewmr7_3738
            SHN: Shewana3_0284 Shewana3_1430 Shewana3_2719
            SHW: Sputw3181_1520 Sputw3181_2764 Sputw3181_3339
            PHA: PSHAa1657
            PAT: Patl_1363 Patl_1630
            MAQ: Maqu_1560
            TCX: Tcr_1328
            HCH: HCH_02061(rluA1) HCH_02226(rluA2)
            AHA: AHA_2665
            DNO: DNO_0027(truB) DNO_0294(rluA) DNO_0479(rluB) DNO_0584(rluE)
                 DNO_1134 DNO_1311(rluD)
            VOK: COSY_0061(truB) COSY_0078(rluC) COSY_0312(rluD) COSY_0321
                 COSY_0881(truA)
            NMC: NMC0190(rluC)
            CVI: CV_1157 CV_4146(rluB)
            REH: H16_A1434(rluA1) H16_A2917(rsuA2) H16_A3057(truA2)
            BVI: Bcep1808_1720
            BCH: Bcen2424_1793
            BAM: Bamb_1731
            AAV: Aave_3381
            AJS: Ajs_2559
            VEI: Veis_2747
            MPT: Mpe_A0657 Mpe_A1919 Mpe_A2003 Mpe_A2159 Mpe_A2195 Mpe_A3042
            HAR: HEAR1697(rsuA) HEAR1926(rluD) HEAR2254(rluA) HEAR2449
                 HEAR3283
            MMS: mma_1169 mma_1393(rluD) mma_1950(rsuA) mma_2061
                 mma_2493(truB) mma_2517
            AZO: azo0013(rluA1) azo0084(rsuA)
            HPA: HPAG1_0342 HPAG1_0940
            HAC: Hac_0975 Hac_1032(rluA)
            WSU: WS0417
            TDN: Tmden_1340 Tmden_2094
            CJE: Cj0022c Cj0708
            CJR: CJE0022
            CJU: C8J_0021
            ABU: Abu_0018 Abu_0050(rluB) Abu_1003(rluD) Abu_1096(rsuA)
                 Abu_1975 Abu_2084(truB) Abu_2117 Abu_2199(truA)
            NIS: NIS_0055 NIS_0064 NIS_0692 NIS_0752 NIS_1108(truA) NIS_1230
                 NIS_1474 NIS_1506
            SUN: SUN_0365 SUN_0383 SUN_0745 SUN_1193 SUN_1263 SUN_1753(rluD)
                 SUN_1841(truA) SUN_2363 SUN_2370
            PPD: Ppro_0966 Ppro_1701 Ppro_3382
            DVL: Dvul_1969 Dvul_2073 Dvul_2436
            BBA: Bd1424(rluA) Bd2358 Bd2820(rluA)
            SAT: SYN_00730
            RCM: A1E_01485
            OTS: OTBS_0164(truB) OTBS_1643(truA) OTBS_2144(rluC)
            BRA: BRADO0055(truB) BRADO1372(rluD)
            BBT: BBta_0059(truB) BBta_1701 BBta_6759(rluD)
            RPE: RPE_0319
            NWI: Nwi_0315
            NHA: Nham_0401
            RSH: Rsph17029_1072 Rsph17029_2770
            PDE: Pden_2801 Pden_2804
            ZMO: ZMO0576
            NAR: Saro_0447
            GOX: GOX0804
            GBE: GbCGDNIH1_0100
            MGM: Mmc1_1777 Mmc1_2132
            SUS: Acid_4994 Acid_6299 Acid_7265
            BAY: RBAM_001730(truA) RBAM_021300(rluB)
            BPU: BPUM_0872(rluA1) BPUM_1091(rluA2) BPUM_1445(ylyB)
                 BPUM_2049(rluB) BPUM_2648(rsuA)
            LLM: llmg_0384(rluE) llmg_1524(rluD)
            SPF: SpyM50719 SpyM50768 SpyM51548(rluB)
            SSA: SSA_0649
            CPF: CPF_1248(truA)
            CTH: Cthe_0908
            CDF: CD0103(truA1) CD1060 CD2596
            CBO: CBO1433(rluC) CBO1476(rluD1) CBO1813(rluB) CBO1914(truA1)
                 CBO2980(rluD2) CBO3273(rluB) CBO3447(truA2)
            CKL: CKL_3486(rsuA)
            DRM: Dred_1673 Dred_1954
            MTA: Moth_1745
            MPE: MYPE130
            MGA: MGA_0186(rluA)
            UUR: UU113(sfhB)
            MBB: BCG_2811c(truB) BCG_3520c(truA)
            MVA: Mvan_1438 Mvan_2329 Mvan_2774
            MGI: Mflv_4028 Mflv_4968
            MKM: Mkms_1132 Mkms_2141 Mkms_3152
            MJL: Mjls_1144 Mjls_2078 Mjls_3112
            RHA: RHA1_ro01072 RHA1_ro04895 RHA1_ro06164 RHA1_ro06651
            CMI: CMM_1851 CMM_1977(rluA) CMM_2144(truB) CMM_2581(truA)
            ART: Arth_1424 Arth_1580 Arth_2938
            AAU: AAur_1565(truB)
            NCA: Noca_3188 Noca_3871
            FNU: FN1026
            CMU: TC0382
            TDE: TDE2576
            LIL: LA2896(rluC2)
            SYW: SYNW2288
            SYD: Syncc9605_2426
            SYE: Syncc9902_2106
            SYG: sync_2641
            SYR: SynRCC307_0777(rsuA) SynRCC307_1686 SynRCC307_2232(rluA)
                 SynRCC307_2262
            SYX: SynWH7803_1547(rsuA) SynWH7803_1572(rluA) SynWH7803_1637
                 SynWH7803_1971(truB) SynWH7803_2308 SynWH7803_2348
            GVI: gll0183
            PMT: PMT2042
            PMB: A9601_02111(rluD) A9601_15481(truB) A9601_17411(truA)
            PMC: P9515_02221(rluD) P9515_15081(truB) P9515_17151(truA)
            PMF: P9303_05391(truB) P9303_08541 P9303_09301(rluA)
                 P9303_23281(truA) P9303_27171 P9303_28001(rluD)
            PMG: P9301_02131(rluD) P9301_15331(truB) P9301_17251(truA)
            PMH: P9215_02111(rluD) P9215_13041(rsuA) P9215_18051(truA)
            PME: NATL1_02691(rluD) NATL1_17741(truB) NATL1_19791(truA)
            CHU: CHU_0734(rluD) CHU_3040(rluA) CHU_3480(rluD) CHU_3766(rluC)
            GFO: GFO_0095(rluD) GFO_0425(truA) GFO_1748(truA) GFO_1954(rluE)
                 GFO_2091(rluD) GFO_2682(rluD) GFO_3038(truB)
            FPS: FP0315 FP0651 FP0887 FP1222 FP1993 FP2357(truB)
            CPH: Cpha266_0371 Cpha266_1086 Cpha266_1633
            PVI: Cvib_0781 Cvib_1061 Cvib_1559
            DRA: DR_0961
            MMQ: MmarC5_0990 MmarC5_1670 MmarC5_1720
            MTP: Mthe_0398 Mthe_0989 Mthe_1702
            MEM: Memar_0538 Memar_1399 Memar_2301
            MBN: Mboo_0217 Mboo_0513 Mboo_0906
            RCI: RCIX2575(truB) RCIX2712(truD)
            PIS: Pisl_0511 Pisl_1128 Pisl_1280
            PCL: Pcal_0054 Pcal_0700 Pcal_1782
            PAS: Pars_0089 Pars_0233 Pars_1684
            TPE: Tpen_0461 Tpen_0685
STRUCTURES  PDB: 1DJ0  1K8W  1KSK  1KSL  1KSV  1PRZ  1QYU  1R3E  1R3F  1SB7  
                 1SGV  1SI7  1SZW  1V9F  1V9K  1VIO  1XPI  1Z2Z  1ZE1  1ZE2  
                 1ZL3  2I82  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.70
            ExPASy - ENZYME nomenclature database: 4.2.1.70
            ExplorEnz - The Enzyme Database: 4.2.1.70
            ERGO genome analysis and discovery system: 4.2.1.70
            BRENDA, the Enzyme Database: 4.2.1.70
            CAS: 9023-35-2
///
ENTRY       EC 4.2.1.71       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
COMMENT     Deleted entry: acetylenecarboxylate hydratase. This enzyme is
            identical to EC 4.2.1.27, acetylenecarboxylate hydratase (EC
            4.2.1.71 created 1978, modified 1989, modified 2000, deleted 2004)
STRUCTURES  PDB: 2E7Z  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.71
            ExPASy - ENZYME nomenclature database: 4.2.1.71
            ExplorEnz - The Enzyme Database: 4.2.1.71
            ERGO genome analysis and discovery system: 4.2.1.71
            BRENDA, the Enzyme Database: 4.2.1.71
///
ENTRY       EC 4.2.1.72       Obsolete  Enzyme
NAME        Transferred to 4.1.1.78
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
COMMENT     Transferred entry: now EC 4.1.1.78 acetylenedicarboxylate
            decarboxylase (EC 4.2.1.72 created 1978, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.72
            ExPASy - ENZYME nomenclature database: 4.2.1.72
            ExplorEnz - The Enzyme Database: 4.2.1.72
            ERGO genome analysis and discovery system: 4.2.1.72
            BRENDA, the Enzyme Database: 4.2.1.72
///
ENTRY       EC 4.2.1.73                 Enzyme
NAME        protoaphin-aglucone dehydratase (cyclizing);
            protoaphin dehydratase;
            protoaphin dehydratase (cyclizing);
            protoaphin-aglucone hydro-lyase (cyclizing)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     protoaphin-aglucone hydro-lyase (cyclizing; xanthoaphin-forming)
REACTION    protoaphin aglucone = xanthoaphin + H2O [RN:R03742]
ALL_REAC    R03742
SUBSTRATE   protoaphin aglucone [CPD:C02879]
PRODUCT     xanthoaphin [CPD:C01863];
            H2O [CPD:C00001]
COMMENT     The product is converted non-enzymically to erythroaphin, an aphid
            pigment.
REFERENCE   1
  AUTHORS   Cameron, D.W., Sawyer, W.H. and Trikojus, V.M.
  TITLE     Colouring matters of the Aphidoidea. XLII. Purification and
            properties of the cyclising enzyme [Protoaphin dehydratase
            (cyclising)] concerned with pigment transformation in the wooly
            aphid Eriosoma lanigerum Hausmann (Hemiptera: Insecta).
  JOURNAL   Aust. J. Biol. Sci. 30 (1977) 173-181.
  ORGANISM  Eriosoma lanigerum
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.73
            ExPASy - ENZYME nomenclature database: 4.2.1.73
            ExplorEnz - The Enzyme Database: 4.2.1.73
            ERGO genome analysis and discovery system: 4.2.1.73
            BRENDA, the Enzyme Database: 4.2.1.73
            CAS: 64177-87-3
///
ENTRY       EC 4.2.1.74                 Enzyme
NAME        long-chain-enoyl-CoA hydratase;
            long-chain enoyl coenzyme A hydratase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     long-chain-(3S)-3-hydroxyacyl-CoA hydro-lyase
REACTION    (3S)-3-hydroxyacyl-CoA = trans-2-enoyl-CoA + H2O [RN:R02685]
ALL_REAC    R02685 > R04170 R04738 R04740 R04744 R04746 R04749 R07889 R07893
            R07897
SUBSTRATE   (3S)-3-hydroxyacyl-CoA [CPD:C00640]
PRODUCT     trans-2-enoyl-CoA [CPD:C00658];
            H2O [CPD:C00001]
COMMENT     Acts in the reverse direction. The best substrate is
            oct-3-enoyl-CoA. Unlike EC 4.2.1.17 enoyl-CoA hydratase, it does not
            act on crotonoyl-CoA.
REFERENCE   1  [PMID:833142]
  AUTHORS   Fong JC, Schulz H.
  TITLE     Purification and properties of pig heart crotonase and the presence
            of short chain and long chain enoyl coenzyme A hydratases in pig and
            guinea pig tissues.
  JOURNAL   J. Biol. Chem. 252 (1977) 542-7.
  ORGANISM  pig [GN:ssc], guinea pig
REFERENCE   2  [PMID:4828315]
  AUTHORS   Schulz H.
  TITLE     Long chain enoyl coenzyme A hydratase from pig heart.
  JOURNAL   J. Biol. Chem. 249 (1974) 2704-9.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00062  Fatty acid elongation in mitochondria
            PATH: map00071  Fatty acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.74
            ExPASy - ENZYME nomenclature database: 4.2.1.74
            ExplorEnz - The Enzyme Database: 4.2.1.74
            ERGO genome analysis and discovery system: 4.2.1.74
            BRENDA, the Enzyme Database: 4.2.1.74
            CAS: 62009-81-8
///
ENTRY       EC 4.2.1.75                 Enzyme
NAME        uroporphyrinogen-III synthase;
            porphobilinogenase;
            uroporphyrinogen isomerase;
            uroporphyrinogen III cosynthase;
            URO-synthase;
            hydroxymethylbilane hydro-lyase (cyclizing)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     hydroxymethylbilane hydro-lyase (cyclizing;
            uroporphyrinogen-III-forming)
REACTION    hydroxymethylbilane = uroporphyrinogen III + H2O [RN:R03165]
ALL_REAC    R03165
SUBSTRATE   hydroxymethylbilane [CPD:C01024]
PRODUCT     uroporphyrinogen III [CPD:C01051];
            H2O [CPD:C00001]
COMMENT     In the presence of EC 2.5.1.61, hydroxymethylbilane synthase, the
            enzyme forms uroporphyrinogen III from porphobilinogen.
REFERENCE   1  [PMID:6769048]
  AUTHORS   Battersby AR, Fookes CJ, Matcham GW, McDonald E.
  TITLE     Biosynthesis of the pigments of life: formation of the macrocycle.
  JOURNAL   Nature. 285 (1980) 17-21.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:3805019]
  AUTHORS   Tsai SF, Bishop DF, Desnick RJ.
  TITLE     Purification and properties of uroporphyrinogen III synthase from
            human erythrocytes.
  JOURNAL   J. Biol. Chem. 262 (1987) 1268-73.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K01719  uroporphyrinogen-III synthase
GENES       HSA: 7390(UROS)
            PTR: 450813(UROS)
            MMU: 22276(Uros)
            CFA: 492116(UROS)
            GGA: 426223(UROS)
            XLA: 447178(MGC85561)
            DRE: 404731(uros)
            SPU: 586365(LOC586365)
            DME: Dmel_CG1885
            OSA: 4331869
            CME: CML040C
            SCE: YOR278W(HEM4)
            AGO: AGOS_AER351W
            PIC: PICST_59732(HEM4)
            CGR: CAGL0L11000g
            SPO: SPAC31G5.08(ups)
            AFM: AFUA_6G12800
            AOR: AO090003000401
            CNE: CNK02510
            ECO: b3804(hemD)
            ECJ: JW3776(hemD)
            ECE: Z5318(hemD)
            ECS: ECs4734
            ECC: c4723(hemD)
            ECI: UTI89_C4363(hemD)
            ECP: ECP_3996
            ECV: APECO1_2674(hemD)
            ECW: EcE24377A_4319(hemD)
            ECX: EcHS_A4024(hemD)
            STY: STY3622(hemD)
            STT: t3360(hemD)
            SPT: SPA3778(hemD)
            SEC: SC3838(hemD)
            STM: STM3937(hemD)
            YPE: YPO3850(hemD)
            YPK: y0380(hemD)
            YPM: YP_3196(hemD)
            YPA: YPA_0171
            YPN: YPN_0113
            YPP: YPDSF_3468
            YPS: YPTB0183(hemD)
            YPI: YpsIP31758_0197(hemD)
            SFL: SF3876(hemD)
            SFX: S3880(hemD)
            SFV: SFV_3698(hemD)
            SSN: SSON_3976(hemD)
            SBO: SBO_3815(hemD)
            SDY: SDY_3942(hemD)
            ECA: ECA4189(hemD)
            PLU: plu4645(hemD)
            WBR: WGLp241(hemD)
            SGL: SG2367
            ENT: Ent638_3988
            SPE: Spro_0177
            BFL: Bfl581(hemD)
            BPN: BPEN_602(hemD)
            HDU: HD1742(hemD)
            HSO: HS_0045(hemD)
            PMU: PM1813(hemX)
            MSU: MS0275(hemD)
            APL: APL_1009(hemD)
            XFA: XF1799
            XFT: PD1068(hemD)
            XCC: XCC0198(hemD)
            XCB: XC_0208
            XCV: XCV0201(hemD)
            XAC: XAC0216(hemD)
            XOO: XOO4088(hemD)
            XOM: XOO_3862(XOO3862)
            VCH: VC0119
            VCO: VC0395_A2399(hemD)
            VVU: VV1_1121
            VVY: VV0080
            VPA: VP2989
            VFI: VF0065
            PPR: PBPRA3529
            PAE: PA5259(hemD)
            PAU: PA14_69440(hemD)
            PPU: PP_0187(hemD)
            PPF: Pput_0209
            PST: PSPTO_0129(hemD)
            PSB: Psyr_0061
            PSP: PSPPH_0066(hemD)
            PFL: PFL_6001(hemD)
            PFO: Pfl_5486
            PEN: PSEEN5352(hemD)
            PAR: Psyc_0090(hemD)
            PCR: Pcryo_0099
            ACI: ACIAD0287(hemD)
            SON: SO_4314(hemD)
            SDN: Sden_0387
            SFR: Sfri_0439
            SHE: Shewmr4_0387
            SHM: Shewmr7_3639
            SHN: Shewana3_0385
            SHW: Sputw3181_3727
            ILO: IL2559(hemD)
            CPS: CPS_0073(hemD)
            PHA: PSHAa0099(hemDX)
            PAT: Patl_0341
            MAQ: Maqu_0486
            CBU: CBU_2077(hemD)
            CBD: COXBU7E912_2173(hemD)
            LPN: lpg2736
            LPF: lpl2661(hemD)
            LPP: lpp2792(hemD)
            MCA: MCA3061(hemDX)
            FTU: FTT1408c(hemD)
            FTF: FTF1408c(hemD)
            FTL: FTL_0654
            FTH: FTH_0657(hemD)
            FTN: FTN_1373(hemD)
            TCX: Tcr_0113
            NOC: Noc_0503
            AEH: Mlg_2669
            HCH: HCH_00290
            CSA: Csal_3108
            ABO: ABO_2321(hemD)
            AHA: AHA_0468(hemD)
            DNO: DNO_0298(hemD)
            BCI: BCI_0062(hemD)
            RMA: Rmag_0853
            VOK: COSY_0778(hemD)
            NME: NMB0777
            NMA: NMA0988
            NGO: NGO0359
            CVI: CV_0052(hemD)
            RSO: RSc2356(RS01190)
            REU: Reut_A0701(hemX)
            RME: Rmet_2748
            BMA: BMA0731
            BUR: Bcep18194_A5751
            BPS: BPSL1016
            BPM: BURPS1710b_1231(hemX)
            BTE: BTH_I0873
            BPE: BP2536
            BPA: BPP2643
            BBR: BB2086
            MPT: Mpe_A3001
            HAR: HEAR1008(hemD)
            MMS: mma_1143(hemD)
            NEU: NE0591(hemD)
            NET: Neut_1038
            NMU: Nmul_A2689
            EBA: ebA1165(hemD)
            AZO: azo0994(hemD)
            DAR: Daro_3673
            TBD: Tbd_2567
            MFA: Mfla_0034
            HPY: HP1224(hemD)
            HPJ: jhp1145(hemD)
            HPA: HPAG1_1166
            HHE: HH0104(hemD)
            HAC: Hac_1600(hemD)
            WSU: WS1602(hemD)
            TDN: Tmden_1228
            CJR: CJE1223(hemD)
            CJJ: CJJ81176_1098(hemD)
            CJD: JJD26997_0644(hemD)
            CFF: CFF8240_1262(hemD)
            CCV: CCV52592_0948(hemD)
            CHA: CHAB381_1483(hemD)
            CCO: CCC13826_0493(hemD)
            ABU: Abu_1177(hemD)
            NIS: NIS_1338
            SUN: SUN_1892
            GSU: GSU3286
            GME: Gmet_3235
            PCA: Pcar_3062
            DVU: DVU0734
            DDE: Dde_2837
            LIP: LI0117(cysG)
            DPS: DP1734(hemD)
            MXA: MXAN_2657(hemD)
            SAT: SYN_02272
            SFU: Sfum_3201
            WOL: WD1000
            WBM: Wbm0728
            AMA: AM830
            APH: APH_0354
            ERU: Erum5380(hemD)
            ERW: ERWE_CDS_05640
            ERG: ERGA_CDS_05530
            ECN: Ecaj_0546
            ECH: ECH_0480(hemD)
            PUB: SAR11_0309(hemD)
            MLO: mll4221
            MES: Meso_3201
            SME: SMc03232(hemD)
            ATU: Atu2653
            ATC: AGR_C_4810
            RET: RHE_CH03905(hemD)
            RLE: RL4496
            BME: BMEI0177
            BMF: BAB1_1886(hemD)
            BMS: BR1886(hemD)
            BMB: BruAb1_1863(hemD)
            BOV: BOV_1814(hemD)
            BJA: bll0566
            BRA: BRADO0301 BRADO5258
            BBT: BBta_0288 BBta_5710
            RPA: RPA0256
            RPB: RPB_0314
            RPC: RPC_0047
            RPD: RPD_0469
            RPE: RPE_0064 RPE_4220
            NWI: Nwi_0472
            NHA: Nham_0563
            SIL: SPO3853
            SIT: TM1040_2828
            RSP: RSP_6208
            JAN: Jann_4081
            RDE: RD1_0471(hemD)
            MMR: Mmar10_0041
            HNE: HNE_3228(hemD)
            ZMO: ZMO1902(hemD)
            GOX: GOX1884
            GBE: GbCGDNIH1_2423
            RRU: Rru_A3567
            MAG: amb4421
            ABA: Acid345_2562
            BSU: BG10343(hemD)
            BHA: BH1495 BH3045(hemD)
            BAN: BA2144 BA4695(hemD)
            BAR: GBAA2144 GBAA4695(hemD)
            BAA: BA_2640 BA_5134
            BAT: BAS1995 BAS4360
            BCE: BC2134 BC4470
            BCA: BCE_4554(hemD)
            BCZ: BCZK1947 BCZK4207(hemD)
            BTK: BT9727_1968 BT9727_4196(hemD)
            BTL: BALH_4056(hemD)
            BLI: BL00626(hemD)
            BLD: BLi02944(hemD)
            BCL: ABC2629(hemD) ABC3411
            BAY: RBAM_025200(hemD)
            BPU: BPUM_1801(yjjA) BPUM_2455(hemD)
            OIH: OB1658(hemD) OB2067
            GKA: GK2644
            SAU: SA1493(hemD)
            SAV: SAV1669(hemD)
            SAM: MW1613(hemD)
            SAR: SAR1749(hemD)
            SAS: SAS1598
            SAC: SACOL1716(hemD)
            SAB: SAB1529c(hemD)
            SAA: SAUSA300_1616(hemD)
            SAO: SAOUHSC_01773
            SEP: SE1344
            SER: SERP1233(hemD)
            SHA: SH1258(hemD)
            SSP: SSP1095
            LMO: lmo1201
            LMF: LMOf2365_1210 LMOf2365_1576(hemD)
            LIN: lin1164
            LWE: lwe1158(hemD) lwe1568(hemD)
            SSA: SSA_0486
            CAC: CAC0098(hemD)
            CPE: CPE1434(hemX)
            CPF: CPF_1687(hemD)
            CPR: CPR_1421(hemD)
            CTC: CTC00728
            CDF: CD3420(hemD)
            CBO: CBO0921(hemD)
            CBA: CLB_0962(cobA)
            CBH: CLC_0976(cobA)
            CBF: CLI_1008(cobA)
            CHY: CHY_1209(hemD) CHY_2407
            DSY: DSY2224
            MTA: Moth_1248
            MTU: Rv0511(hemD)
            MTC: MT0532
            MBO: Mb0524(hemD)
            MLE: ML2420(hemD)
            MPA: MAP4004(cysG)
            MAV: MAV_4638(hemD)
            MSM: MSMEG_0954(hemD)
            CGL: NCgl0414(cgl0429)
            CGB: cg0510(hemD) cg2189(cobA)
            CEF: CE0450
            CDI: DIP0402
            CJK: jk1900(hemD)
            NFA: nfa51680(hemDX)
            SCO: SCO3317(SCE68.15c)
            SMA: SAV4741(hemD)
            TWH: TWT731
            TWS: TW745
            LXX: Lxx01110(hemD)
            PAC: PPA0303 PPA0323
            TFU: Tfu_2731
            FRA: Francci3_0487 Francci3_0528
            FAL: FRAAL0985(hemD) FRAAL1020(corA) FRAAL1354
            ACE: Acel_0236
            SEN: SACE_6944(hemD)
            FNU: FN0644
            RBA: RB7020(hemD) RB7803(uroD)
            CTR: CT433
            CTA: CTA_0473
            CMU: TC0717
            CPN: CPn0522
            CPA: CP0231
            CPJ: CPj0522
            CPT: CpB0543
            CCA: CCA00223
            CAB: CAB219
            CFE: CF0783
            SYN: sll0166(cobA/hemD)
            SYW: SYNW2210(hemD)
            SYC: syc1241_c(hemD)
            SYF: Synpcc7942_0272
            SYD: Syncc9605_2353
            SYE: Syncc9902_0338
            SYG: sync_2565(hemD)
            SYR: SynRCC307_0278(hemD)
            SYX: SynWH7803_2221(hemD)
            CYA: CYA_0529(cobA)
            CYB: CYB_0566(cobA)
            TEL: tlr2155(cobA/hemD)
            GVI: glr1234(cobA/hemD)
            ANA: alr3450(cobA/hemD)
            AVA: Ava_3075 Ava_3474
            PMA: Pro0134(hemD)
            PMM: PMM0113(hemD)
            PMT: PMT1966(hemD)
            PMN: PMN2A_1482
            PMI: PMT9312_0116
            PMB: A9601_01311(hemD)
            PMC: P9515_01271(hemD)
            PMF: P9303_26181(hemD)
            PMG: P9301_01301(hemD)
            PME: NATL1_01871(hemD)
            TER: Tery_3325
            SRU: SRU_1553(hemD)
            CHU: CHU_0169(hemD)
            GFO: GFO_0106(hemD) GFO_3225(hemD)
            FPS: FP0042(hemD)
            CTE: CT1428(hemD)
            CCH: Cag_1514
            CPH: Cpha266_1797
            PVI: Cvib_1246
            PLT: Plut_1428
            DRA: DR_0786 DR_A0011
            DGE: Dgeo_2131
            TTH: TTC0312 TTC1143(hemD)
            TTJ: TTHA1507
            AAE: aq_1771
            MMP: MMP0394(hemD)
            MAC: MA3034(hemD)
            MBA: Mbar_A1792
            MMA: MM_0308
            MBU: Mbur_1106
            MST: Msp_1191(hemD)
            MSI: Msm_1504
            MKA: MK1550(hemD)
            HAL: VNG2332G(cysG)
            HMA: rrnAC3088(cysG1)
            HWA: HQ3452A(hemD)
            NPH: NP1330A(hemD)
            PTO: PTO0250
            RCI: RCIX916(hemD)
            APE: APE_1493(hemD)
            SSO: SSO0184
            STO: ST0218
            SAI: Saci_0781
            PAI: PAE0589
STRUCTURES  PDB: 1JR2  1WCW  1WCX  1WD7  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.75
            ExPASy - ENZYME nomenclature database: 4.2.1.75
            ExplorEnz - The Enzyme Database: 4.2.1.75
            ERGO genome analysis and discovery system: 4.2.1.75
            BRENDA, the Enzyme Database: 4.2.1.75
            CAS: 37340-55-9
///
ENTRY       EC 4.2.1.76                 Enzyme
NAME        UDP-glucose 4,6-dehydratase;
            UDP-D-glucose-4,6-hydrolyase;
            UDP-D-glucose oxidoreductase;
            UDP-glucose 4,6-hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     UDP-glucose 4,6-hydro-lyase
            (UDP-4-dehydro-6-deoxy-D-glucose-forming)
REACTION    UDP-glucose = UDP-4-dehydro-6-deoxy-D-glucose + H2O [RN:R00293]
ALL_REAC    R00293
SUBSTRATE   UDP-glucose [CPD:C00029]
PRODUCT     UDP-4-dehydro-6-deoxy-D-glucose [CPD:C04089];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:680134]
  AUTHORS   Kamsteeg J, Van Brederode J, Van Nigtevecht G.
  TITLE     The formation of UDP-L-rhamnose from UDP-D-glucose by an enzyme
            preparation of red campion (Silene dioica (L) Clairv) leaves.
  JOURNAL   FEBS. Lett. 91 (1978) 281-4.
  ORGANISM  Silene dioica
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
GENES       CHU: CHU_2766
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.76
            ExPASy - ENZYME nomenclature database: 4.2.1.76
            ExplorEnz - The Enzyme Database: 4.2.1.76
            ERGO genome analysis and discovery system: 4.2.1.76
            BRENDA, the Enzyme Database: 4.2.1.76
            CAS: 68189-53-7
///
ENTRY       EC 4.2.1.77                 Enzyme
NAME        trans-L-3-hydroxyproline dehydratase;
            trans-L-3-hydroxyproline hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     trans-L-3-hydroxyproline hydro-lyase
            (Delta1-pyrroline-2-carboxylate-forming)
REACTION    trans-L-3-hydroxyproline = Delta1-pyrroline 2-carboxylate + H2O
            [RN:R04374]
ALL_REAC    R04374
SUBSTRATE   trans-L-3-hydroxyproline [CPD:C05147]
PRODUCT     Delta1-pyrroline 2-carboxylate [CPD:C04027];
            H2O [CPD:C00001]
COMMENT     Highly specific. 2,3-Dehydroproline is an intermediate.
REFERENCE   1
  AUTHORS   Ramaswamy, S.G.
  TITLE     Conversion of 3-hydroxyproline to proline in the rat requires
            reduced pyridine-nucleotides.
  JOURNAL   Fed. Proc. 42 (1983) 2232.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.77
            ExPASy - ENZYME nomenclature database: 4.2.1.77
            ExplorEnz - The Enzyme Database: 4.2.1.77
            ERGO genome analysis and discovery system: 4.2.1.77
            BRENDA, the Enzyme Database: 4.2.1.77
///
ENTRY       EC 4.2.1.78                 Enzyme
NAME        (S)-norcoclaurine synthase;
            (S)-norlaudanosoline synthase;
            4-hydroxyphenylacetaldehyde hydro-lyase (adding dopamine)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     4-hydroxyphenylacetaldehyde hydro-lyase [adding dopamine;
            (S)-norcoclaurine-forming]
REACTION    4-hydroxyphenylacetaldehyde + 4-(2-aminoethyl)benzene-1,2-diol =
            (S)-norcoclaurine + H2O [RN:R04305]
ALL_REAC    R04305;
            (other) R04084
SUBSTRATE   4-hydroxyphenylacetaldehyde [CPD:C03765];
            4-(2-aminoethyl)benzene-1,2-diol [CPD:C03758]
PRODUCT     (S)-norcoclaurine [CPD:C06160];
            H2O [CPD:C00001]
COMMENT     The reaction makes a six-membered ring by forming a bond between C-6
            of the 3,4-dihydroxyphenyl group of the dopamine and C-1 of the
            aldehyde in the imine formed between the substrates. The product is
            the precursor of the benzylisoquinoline alkaloids in plants. The
            enzyme, formerly known as (S)-norlaudanosoline synthase, will also
            catalyse the reaction of 4-(2-aminoethyl)benzene-1,2-diol +
            (3,4-dihydroxyphenyl)acetaldehyde to form (S)-norlaudanosoline, but
            this alkaloid has not been found to occur in plants.
REFERENCE   1
  AUTHORS   Stadler, R., Zenk, M.H.
  TITLE     A revision of the generally accepted pathway for the biosynthesis of
            the benzyltetrahydroisoquinoline reticuline.
  JOURNAL   Liebigs Ann. Chem. (1990) 555-562.
REFERENCE   2
  AUTHORS   Stadler, R., Kutchan, T.M., Zenk, M.H.
  TITLE     (S)-Norcoclaurine is the central intermediate in benzylisoquinoline
            alkaloid biosynthesis.
  JOURNAL   Phytochemistry 28 (1989) 1083-1086.
  ORGANISM  Papaver somniferum
REFERENCE   3  [PMID:12107162]
  AUTHORS   Samanani N, Facchini PJ.
  TITLE     Purification and characterization of norcoclaurine synthase. The
            first committed enzyme in benzylisoquinoline alkaloid biosynthesis
            in plants.
  JOURNAL   J. Biol. Chem. 277 (2002) 33878-83.
  ORGANISM  Thalictrum flavum ssp. glaucum
PATHWAY     PATH: map00950  Alkaloid biosynthesis I
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.78
            ExPASy - ENZYME nomenclature database: 4.2.1.78
            ExplorEnz - The Enzyme Database: 4.2.1.78
            ERGO genome analysis and discovery system: 4.2.1.78
            BRENDA, the Enzyme Database: 4.2.1.78
            CAS: 79122-01-3
///
ENTRY       EC 4.2.1.79                 Enzyme
NAME        2-methylcitrate dehydratase;
            2-methylcitrate hydro-lyase;
            PrpD;
            2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase
            [(Z)-but-2-ene-1,2,3-tricarboxylate-forming]
REACTION    (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate =
            (Z)-but-2-ene-1,2,3-tricarboxylate + H2O [RN:R04424]
ALL_REAC    R04424
SUBSTRATE   (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate
PRODUCT     (Z)-but-2-ene-1,2,3-tricarboxylate [CPD:C04225];
            H2O [CPD:C00001]
COMMENT     Not identical with EC 4.2.1.4, citrate dehydratase. The enzyme is
            specific for (2S,3S)-methylcitrate, showing no activity with
            (2R,3S)-methylcitrate [2]. The enzyme can also use cis-aconitate as
            a substrate but more slowly [2]. Both this enzyme and EC 4.2.1.3,
            aconitate hydratase, are required to complete the isomerization of
            (2S,3S)-methylcitrate to (2R,3S)-2-methylisocitrate [2]
REFERENCE   1
  AUTHORS   Aoki, H. and Tabuchi, T.
  TITLE     Purification and properties of 2-methylcitrate dehydratase from
            Yarrowia lipolytica.
  JOURNAL   Agric. Biol. Chem. 45 (1981) 2831-2837.
  ORGANISM  Yarrowia lipolytica [GN:dyli]
REFERENCE   2  [PMID:12473114]
  AUTHORS   Brock M, Maerker C, Schutz A, Volker U, Buckel W.
  TITLE     Oxidation of propionate to pyruvate in Escherichia coli. Involvement
            of methylcitrate dehydratase and aconitase.
  JOURNAL   Eur. J. Biochem. 269 (2002) 6184-94.
PATHWAY     PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K01720  2-methylcitrate dehydratase
GENES       SCE: YPR002W(PDH1)
            AGO: AGOS_AGR003W
            PIC: PICST_43263(YXE1)
            CGR: CAGL0L09108g
            ANI: AN6639.2
            AFM: AFUA_2G13610 AFUA_6G03730
            AOR: AO090701000175
            UMA: UM06344.1
            DDI: DDB_0191366(prpD)
            ECO: b0334(prpD)
            ECJ: JW0325(prpD)
            ECE: Z0429(prpD)
            ECS: ECs0387
            ECC: c0453(prpD)
            ECI: UTI89_C0365(prpD)
            ECP: ECP_0409
            ECV: APECO1_1655(prpD)
            ECW: EcE24377A_0358(prpD)
            ECX: EcHS_A0399
            STY: STY0402(prpD)
            STT: t2494(prpD)
            SPT: SPA2353(prpD)
            SEC: SC0411(prpD)
            STM: STM0370(prpD)
            PLU: plu3540(prpD)
            PPR: PBPRB0237
            PAE: PA0792(prpD)
            PAU: PA14_54000(prpD)
            PAP: PSPA7_4727(prpD)
            PPU: PP_2338(prpD)
            PPF: Pput_3432
            PFL: PFL_1865(prpD)
            PFO: Pfl_1768
            PEN: PSEEN1907(prpD)
            PAR: Psyc_1117(prpD)
            PCR: Pcryo_1302
            ILO: IL1332(prpD)
            PHA: PSHAa1765(prpD)
            PIN: Ping_1572
            MAQ: Maqu_1662
            CBU: CBU_0912(prpD)
            CBD: COXBU7E912_1162(prpD)
            LPN: lpg1529(prpD)
            LPF: lpl1497(prpD)
            LPP: lpp1486(prpD)
            NOC: Noc_2207(prpD)
            AEH: Mlg_2601
            HHA: Hhal_1070
            HCH: HCH_02712
            CSA: Csal_2419
            ABO: ABO_1429(prpD)
            MMW: Mmwyl1_0923
            AHA: AHA_2267(prpD)
            RSO: RSc2002(prpD)
            REH: H16_A1909(prpD1) H16_B0681(prpD2) H16_B1436(prpD3)
                 H16_B1444(prpD4)
            BMA: BMAA1754(prpD)
            BMV: BMASAVP1_1616(prpD)
            BML: BMA10299_1824(prpD)
            BMN: BMA10247_A0494(prpD)
            BXE: Bxe_B2902
            BVI: Bcep1808_4405
            BUR: Bcep18194_B1723 Bcep18194_B2157(prpD)
            BCN: Bcen_4438
            BCH: Bcen2424_3929
            BAM: Bamb_3306
            BPS: BPSS1725(prpD)
            BPM: BURPS1710b_A0799(prpD)
            BPL: BURPS1106A_A2339(prpD)
            BPD: BURPS668_A2477(prpD)
            BTE: BTH_II0655(prpD) BTH_II2237
            BPE: BP2371(prpD)
            BPA: BPP3237(prpD)
            BBR: BB3689(prpD)
            VEI: Veis_0651
            HAR: HEAR3268(prpD)
            MMS: mma_3489
            NMU: Nmul_A0871
            HHE: HH0399(prpD)
            GME: Gmet_1123(prpD)
            GUR: Gura_0073
            BBA: Bd2500
            PUB: SAR11_1154(prpD)
            MES: Meso_2512
            RET: RHE_CH01981(ypch00640)
            RLE: pRL110483
            RPC: RPC_3512
            PDE: Pden_1348
            ACR: Acry_0620
            RRU: Rru_A2318
            BSU: BG11323(mmgE)
            BHA: BH3923
            BCY: Bcer98_1725
            BCL: ABC1806(prpD)
            BPU: BPUM_1847
            OIH: OB2268
            MTU: Rv1130
            MTC: MT1162
            MBO: Mb1161
            MPA: MAP0297c
            MAV: MAV_0346
            MSM: MSMEG_6645
            CGL: NCgl0664(cgl0694)
            CGB: cg0759(prpD2) cg0796(prpD1)
            CEF: CE0716
            CJK: jk1666(prpD)
            CMI: CMM_2380(prpD)
            ART: Arth_1525
            FRA: Francci3_2656
            FAL: FRAAL5023(prpD)
            ACE: Acel_1656
            KRA: Krad_0107
            SEN: SACE_5045(prpD2)
            RXY: Rxyl_2402 Rxyl_2564
            MSI: Msm_0449
            TAC: Ta1226
            TVO: TVN0369
            PTO: PTO0171
            APE: APE_2147.1
            SSO: SSO2586
            STO: ST1810
            SAI: Saci_0245
            MSE: Msed_0278
            PAI: PAE1717(prpD)
            PIS: Pisl_1703
            PCL: Pcal_0625
            PAS: Pars_0780
STRUCTURES  PDB: 1SZQ  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.79
            ExPASy - ENZYME nomenclature database: 4.2.1.79
            ExplorEnz - The Enzyme Database: 4.2.1.79
            ERGO genome analysis and discovery system: 4.2.1.79
            BRENDA, the Enzyme Database: 4.2.1.79
            CAS: 80891-26-5
///
ENTRY       EC 4.2.1.80                 Enzyme
NAME        2-oxopent-4-enoate hydratase;
            2-keto-4-pentenoate hydratase;
            OEH;
            2-keto-4-pentenoate (vinylpyruvate)hydratase;
            4-hydroxy-2-oxopentanoate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     4-hydroxy-2-oxopentanoate hydro-lyase (2-oxopent-4-enoate-forming)
REACTION    4-hydroxy-2-oxopentanoate = 2-oxopent-4-enoate + H2O [RN:R02601]
ALL_REAC    R02601;
            (other) R04781 R05297 R05864
SUBSTRATE   4-hydroxy-2-oxopentanoate [CPD:C03589]
PRODUCT     2-oxopent-4-enoate [CPD:C00596];
            H2O [CPD:C00001]
COMMENT     Also acts, more slowly, on cis-2-oxohex-4-enoate, but not on the
            trans-isomer.
REFERENCE   1  [PMID:7287632]
  AUTHORS   Kunz DA, Ribbons DW, Chapman PJ.
  TITLE     Metabolism of allylglycine and cis-crotylglycine by Pseudomonas
            putida (arvilla) mt-2 harboring a TOL plasmid.
  JOURNAL   J. Bacteriol. 148 (1981) 72-82.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00360  Phenylalanine metabolism
            PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00621  Biphenyl degradation
            PATH: map00622  Toluene and xylene degradation
            PATH: map00627  1,4-Dichlorobenzene degradation
            PATH: map00628  Fluorene degradation
            PATH: map00629  Carbazole degradation
            PATH: map00642  Ethylbenzene degradation
            PATH: map00643  Styrene degradation
ORTHOLOGY   KO: K02554  2-keto-4-pentenoate hydratase
GENES       ECO: b0350(mhpD)
            ECJ: JW0341(mhpD)
            ECE: Z0448(mhpD)
            ECS: ECs0405
            SSN: SSON_0329(mhpD)
            PLU: plu2201
            XCC: XCC0145(mhpD)
            XCB: XC_0154
            XCV: XCV0146
            XAC: XAC0161(mhpD)
            RSO: RS01662(RSp0891)
            REH: H16_A0143(mhpD2) H16_B0548(mhpD1) H16_B0597(bphH)
                 H16_B0884(mhpD3)
            BXE: Bxe_C1189(bphH)
            MPT: Mpe_A2273 Mpe_A3325
            AZO: azo1853(lapE) azo1974(mhpD) azo2434(nahL)
            DAR: Daro_0905 Daro_1354 Daro_2774
            CCR: CC_1509
            MMR: Mmar10_0237
            BCA: BCE_2155
            MTU: Rv3536c
            MTC: MT3640(mhpD)
            MBO: Mb3566c
            MPA: MAP0531
            NFA: nfa30420 nfa33180 nfa4650
            RHA: RHA1_ro00517 RHA1_ro03881 RHA1_ro08085(bphE3)
                 RHA1_ro10117(bphE4) RHA1_ro10137(bphE2)
            SCO: SCP1.55c
            TTJ: TTHB239
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.80
            ExPASy - ENZYME nomenclature database: 4.2.1.80
            ExplorEnz - The Enzyme Database: 4.2.1.80
            ERGO genome analysis and discovery system: 4.2.1.80
            UM-BBD (Biocatalysis/Biodegradation Database): 4.2.1.80
            BRENDA, the Enzyme Database: 4.2.1.80
            CAS: 64427-80-1
///
ENTRY       EC 4.2.1.81                 Enzyme
NAME        D(-)-tartrate dehydratase;
            D-tartrate dehydratase;
            (S,S)-tartrate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (S,S)-tartrate hydro-lyase (oxaloacetate-forming)
REACTION    (S,S)-tartrate = oxaloacetate + H2O [RN:R00340]
ALL_REAC    R00340
SUBSTRATE   (S,S)-tartrate [CPD:C02107]
PRODUCT     oxaloacetate [CPD:C00036];
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023];
            Manganese [CPD:C00034]
COMMENT     Requires Fe2+ or Mn2+. cf. EC 4.2.1.32 L(+)-tartrate dehydratase.
REFERENCE   1  [PMID:6978882]
  AUTHORS   Rode H, Giffhorn F.
  TITLE     D-(--)-tartrate dehydratase of Rhodopseudomonas sphaeroides:
            purification, characterization, and application to enzymatic
            determination of D-(--)-tartrate.
  JOURNAL   J. Bacteriol. 150 (1982) 1061-8.
  ORGANISM  Rhodopseudomonas sphaeroides
REFERENCE   2  [PMID:7107563]
  AUTHORS   Rode H, Giffhorn F.
  TITLE     Ferrous- or cobalt ion-dependent D-(-)-tartrate dehydratase of
            pseudomonads: purification and properties.
  JOURNAL   J. Bacteriol. 151 (1982) 1602-4.
  ORGANISM  Rhodopseudomonas sphaeroides, Pseudomonas putida [GN:ppu],
            Pseudomonas sp.
STRUCTURES  PDB: 2DW6  2DW7  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.81
            ExPASy - ENZYME nomenclature database: 4.2.1.81
            ExplorEnz - The Enzyme Database: 4.2.1.81
            ERGO genome analysis and discovery system: 4.2.1.81
            BRENDA, the Enzyme Database: 4.2.1.81
            CAS: 82532-88-5
///
ENTRY       EC 4.2.1.82                 Enzyme
NAME        xylonate dehydratase;
            D-xylo-aldonate dehydratase;
            D-xylonate dehydratase;
            D-xylonate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     D-xylonate hydro-lyase (2-dehydro-3-deoxy-D-xylonate-forming)
REACTION    D-xylonate = 2-dehydro-3-deoxy-D-xylonate + H2O [RN:R02429]
ALL_REAC    R02429
SUBSTRATE   D-xylonate [CPD:C00502]
PRODUCT     2-dehydro-3-deoxy-D-xylonate [CPD:C03826];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:7154961]
  AUTHORS   Dahms AS, Donald A.
  TITLE     D-xylo-Aldonate dehydratase.
  JOURNAL   Methods. Enzymol. 90 Pt E (1982) 302-5.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:422572]
  AUTHORS   Donald A, Sibley D, Lyons DE, Dahms AS.
  TITLE     D-Galactonate dehydrase. Purification and properties.
  JOURNAL   J. Biol. Chem. 254 (1979) 2132-7.
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.82
            ExPASy - ENZYME nomenclature database: 4.2.1.82
            ExplorEnz - The Enzyme Database: 4.2.1.82
            ERGO genome analysis and discovery system: 4.2.1.82
            BRENDA, the Enzyme Database: 4.2.1.82
            CAS: 84788-77-2
///
ENTRY       EC 4.2.1.83                 Enzyme
NAME        4-oxalmesaconate hydratase;
            4-carboxy-2-oxohexenedioate hydratase;
            4-carboxy-2-oxobutane-1,2,4-tricarboxylate 2,3-hydro-lyase;
            oxalmesaconate hydratase;
            gamma-oxalmesaconate hydratase;
            4-carboxy-2-oxohexenedioate hydratase;
            2-hydroxy-4-oxobutane-1,2,4-tricarboxylate 2,3-hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     2-hydroxy-4-oxobutane-1,2,4-tricarboxylate 2,3-hydro-lyase
            [(E)-4-oxobut-1-ene-1,2,4-tricarboxylate-forming]
REACTION    2-hydroxy-4-oxobutane-1,2,4-tricarboxylate =
            (E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H2O [RN:R04478]
ALL_REAC    R04478
SUBSTRATE   2-hydroxy-4-oxobutane-1,2,4-tricarboxylate [CPD:C04115]
PRODUCT     (E)-4-oxobut-1-ene-1,2,4-tricarboxylate [CPD:C04434];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:6841353]
  AUTHORS   Maruyama K.
  TITLE     Purification and properties of 2-pyrone-4,6-dicarboxylate hydrolase.
  JOURNAL   J. Biochem. (Tokyo). 93 (1983) 557-65.
  ORGANISM  Pseudomonas ochraceae
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
ORTHOLOGY   KO: K10220  4-oxalmesaconate hydratase
GENES       XCC: XCC4032(fldW)
            XCB: XC_4121
            XCV: XCV4255
            XAC: XAC4157(fldW)
            PAT: Patl_3888
            RME: Rmet_3705
            BXE: Bxe_B2314
            BUR: Bcep18194_C7570
            RFR: Rfer_0338
            POL: Bpro_4320
            PNA: Pnap_2032
            VEI: Veis_0168
            RLE: pRL120276(ligJ)
            BRA: BRADO2337(ligJ)
            BBT: BBta_2697(ligJ)
            RPA: RPA4697(ligJ)
            RPB: RPB_0877
            RPD: RPD_0987
            RPE: RPE_0746
            PDE: Pden_3274
            NAR: Saro_2814
            MAG: amb0251
            ART: Arth_4376
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.83
            ExPASy - ENZYME nomenclature database: 4.2.1.83
            ExplorEnz - The Enzyme Database: 4.2.1.83
            ERGO genome analysis and discovery system: 4.2.1.83
            BRENDA, the Enzyme Database: 4.2.1.83
            CAS: 85204-95-1
///
ENTRY       EC 4.2.1.84                 Enzyme
NAME        nitrile hydratase;
            nitrilase (ambiguous);
            3-cyanopyridine hydratase;
            NHase;
            L-NHase;
            H-NHase;
            acrylonitrile hydratase;
            aliphatic nitrile hydratase;
            nitrile hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     aliphatic-amide hydro-lyase (nitrile-forming)
REACTION    an aliphatic amide = a nitrile + H2O [RN:R02826]
ALL_REAC    R02826 > R02828 R04020 R05379 R05596 R07780 R07854
SUBSTRATE   aliphatic amide [CPD:C02244]
PRODUCT     nitrile [CPD:C00726];
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023];
            PQQ [CPD:C00113];
            Cobalt [CPD:C00175]
INHIBITOR   Semicarbazide [CPD:C02077];
            Phenylhydrazine [CPD:C02304];
            Isobutyronitrile [CPD:C02420]
COMMENT     Acts on short-chain aliphatic nitriles, converting them into the
            corresponding amides. Does not act on these amides or on aromatic
            nitriles. cf. EC 3.5.5.1 nitrilase.
REFERENCE   1
  AUTHORS   Asano, Y., Fujishiro, K., Tani, Y. and Yamada, H.
  TITLE     Microbial degradation of nitrile compounds. 5. Aliphatic nitrile
            hydratase from Arthrobacter sp J-1. Purification and
            characterization.
  JOURNAL   Agric. Biol. Chem. 46 (1982) 1165-1174.
  ORGANISM  Arthrobacter sp.
PATHWAY     PATH: map00380  Tryptophan metabolism
            PATH: map00460  Cyanoamino acid metabolism
            PATH: map00627  1,4-Dichlorobenzene degradation
            PATH: map00632  Benzoate degradation via CoA ligation
            PATH: map00643  Styrene degradation
ORTHOLOGY   KO: K01721  nitrile hydratase
GENES       PPF: Pput_2728 Pput_2729
            ACI: ACIAD1615(nthB) ACIAD1616(nthA)
            BCN: Bcen_4082 Bcen_4083
            BCH: Bcen2424_4283 Bcen2424_4284
            BAM: Bamb_6543 Bamb_6544
            SME: SMc01423(nthB) SMc01424(nthA)
            SMD: Smed_2000 Smed_2001
            RET: RHE_CH02782(nthB) RHE_CH02783(nthA)
            RLE: RL3238(nhb2) RL3239(nha1) pRL110124 pRL110125
            BRA: BRADO3845(nthA) BRADO3846(nthB)
            BBT: BBta_4084(nthB) BBta_4085(nthA)
            RPA: RPA2805(nthA)
            RPB: RPB_2704 RPB_2705
            RPC: RPC_2748 RPC_2749
            RPD: RPD_2746 RPD_2747
            SIL: SPO1314(nthA) SPO1315(nthB)
            SIT: TM1040_1971 TM1040_1972
            RDE: RD1_1908(nthA) RD1_1909(nthB)
            ACR: Acry_1077
            MSM: MSMEG_0377 MSMEG_0378(nthA)
            MVA: Mvan_0647 Mvan_0648
            RHA: RHA1_ro00360(nthA) RHA1_ro00361(nthB)
            AAU: AAur_pTC20145(nthB) AAur_pTC20146(nthA) AAur_pTC20147(nthB)
            RXY: Rxyl_2315
STRUCTURES  PDB: 1AHJ  1IRE  1UGP  1UGQ  1UGR  1UGS  1V29  2AHJ  2CYZ  2CZ0  
                 2CZ1  2CZ6  2CZ7  2D0Q  2DPP  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.84
            ExPASy - ENZYME nomenclature database: 4.2.1.84
            ExplorEnz - The Enzyme Database: 4.2.1.84
            ERGO genome analysis and discovery system: 4.2.1.84
            UM-BBD (Biocatalysis/Biodegradation Database): 4.2.1.84
            BRENDA, the Enzyme Database: 4.2.1.84
            CAS: 82391-37-5
///
ENTRY       EC 4.2.1.85                 Enzyme
NAME        dimethylmaleate hydratase;
            (2R,3S)-2,3-dimethylmalate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (2R,3S)-2,3-dimethylmalate hydro-lyase (dimethylmaleate-forming)
REACTION    (2R,3S)-2,3-dimethylmalate = dimethylmaleate + H2O [RN:R03069]
ALL_REAC    R03069
SUBSTRATE   (2R,3S)-2,3-dimethylmalate [CPD:C03652]
PRODUCT     dimethylmaleate;
            H2O [CPD:C00001]
COFACTOR    Iron [CPD:C00023]
COMMENT     Requires Fe2+. Inhibited by oxygen.
REFERENCE   1  [PMID:6489933]
  AUTHORS   Kollmann-Koch A, Eggerer H.
  TITLE     Nicotinic acid metabolism. Dimethylmaleate hydratase.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 365 (1984) 847-57.
  ORGANISM  Clostridium barkeri
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.85
            ExPASy - ENZYME nomenclature database: 4.2.1.85
            ExplorEnz - The Enzyme Database: 4.2.1.85
            ERGO genome analysis and discovery system: 4.2.1.85
            BRENDA, the Enzyme Database: 4.2.1.85
            CAS: 93229-56-2
///
ENTRY       EC 4.2.1.86       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
COMMENT     Deleted entry: 16-dehydroprogesterone hydratase (reaction is
            identical to that of EC 4.2.1.98, 16alpha-hydroxyprogesterone
            dehydratase) (EC 4.2.1.86 created 1989, deleted 2004)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.86
            ExPASy - ENZYME nomenclature database: 4.2.1.86
            ExplorEnz - The Enzyme Database: 4.2.1.86
            ERGO genome analysis and discovery system: 4.2.1.86
            BRENDA, the Enzyme Database: 4.2.1.86
///
ENTRY       EC 4.2.1.87                 Enzyme
NAME        octopamine dehydratase;
            octopamine hydrolyase;
            octopamine hydro-lyase (deaminating)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     1-(4-hydroxyphenyl)-2-aminoethanol hydro-lyase [deaminating;
            (4-hydroxyphenyl)acetaldehyde-forming]
REACTION    1-(4-hydroxyphenyl)-2-aminoethanol = (4-hydroxyphenyl)acetaldehyde +
            NH3 [RN:R03358]
ALL_REAC    R03358
SUBSTRATE   1-(4-hydroxyphenyl)-2-aminoethanol [CPD:C04227]
PRODUCT     4-hydroxyphenylacetaldehyde [CPD:C03765];
            NH3 [CPD:C00014]
COMMENT     The enzyme-catalysed reaction is believed to be dehydration to an
            enamine, which is spontaneously hydrolysed to an aldehyde and
            ammonia.
REFERENCE   1  [PMID:3034855]
  AUTHORS   Cuskey SM, Peccoraro V, Olsen RH.
  TITLE     Initial catabolism of aromatic biogenic amines by Pseudomonas
            aeruginosa PAO: pathway description, mapping of mutations, and
            cloning of essential genes.
  JOURNAL   J. Bacteriol. 169 (1987) 2398-404.
  ORGANISM  Pseudomonas aeruginosa
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.87
            ExPASy - ENZYME nomenclature database: 4.2.1.87
            ExplorEnz - The Enzyme Database: 4.2.1.87
            ERGO genome analysis and discovery system: 4.2.1.87
            BRENDA, the Enzyme Database: 4.2.1.87
            CAS: 109456-55-5
///
ENTRY       EC 4.2.1.88                 Enzyme
NAME        synephrine dehydratase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     1-(4-hydroxyphenyl)-2-(methylamino)ethanol hydro-lyase
            (methylamine-forming)
REACTION    1-(4-hydroxyphenyl)-2-(methylamino)ethanol =
            (4-hydroxyphenyl)acetaldehyde + methylamine [RN:R03359]
ALL_REAC    R03359
SUBSTRATE   1-(4-hydroxyphenyl)-2-(methylamino)ethanol [CPD:C04548]
PRODUCT     4-hydroxyphenylacetaldehyde [CPD:C03765];
            methylamine [CPD:C00218]
COMMENT     Removal of H2O from (+/-)-synephrine produces a 2,3-enamine, which
            hydrolyses to the products shown in the reaction above. The enzyme
            from Arthrobacter synephrinum is highly specific.
REFERENCE   1  [PMID:1008837]
  AUTHORS   Veeraswamy M, Devi NA, Kutty RK, Rao PV.
  TITLE     Conversion of (+/-)-synephrine into p-hydroxyphenylacetaldehyde by
            Arthrobacter synephrinum. A novel enzymic reaction.
  JOURNAL   Biochem. J. 159 (1976) 807-9.
  ORGANISM  Arthrobacter synephrinum
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.88
            ExPASy - ENZYME nomenclature database: 4.2.1.88
            ExplorEnz - The Enzyme Database: 4.2.1.88
            ERGO genome analysis and discovery system: 4.2.1.88
            BRENDA, the Enzyme Database: 4.2.1.88
            CAS: 104118-54-9
///
ENTRY       EC 4.2.1.89                 Enzyme
NAME        carnitine dehydratase;
            L-carnitine hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     L-carnitine hydro-lyase [4-(trimethylammonio)but-2-enoate-forming]
REACTION    L-carnitine = 4-(trimethylammonio)but-2-enoate + H2O [RN:R01925]
ALL_REAC    R01925
SUBSTRATE   L-carnitine [CPD:C00318]
PRODUCT     4-(trimethylammonio)but-2-enoate [CPD:C04114];
            H2O [CPD:C00001]
REFERENCE   1
  AUTHORS   Fukui, S., Kawamura, M., Akutsu, S., Fukuda, H., Morishita, T.,
            Kano, K., Imai, K. and Nishimori, H.
  TITLE     Production of L-carnitine.
  JOURNAL   Chem. Abstr. 105 (1986) 13214.
ORTHOLOGY   KO: K01722  
GENES       CVI: CV_3013(caiB)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.89
            ExPASy - ENZYME nomenclature database: 4.2.1.89
            ExplorEnz - The Enzyme Database: 4.2.1.89
            ERGO genome analysis and discovery system: 4.2.1.89
            BRENDA, the Enzyme Database: 4.2.1.89
            CAS: 104382-17-4
///
ENTRY       EC 4.2.1.90                 Enzyme
NAME        L-rhamnonate dehydratase;
            L-rhamnonate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     L-rhamnonate hydro-lyase (2-dehydro-3-deoxy-L-rhamnonate-forming)
REACTION    L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H2O [RN:R03774]
ALL_REAC    R03774
SUBSTRATE   L-rhamnonate [CPD:C01934]
PRODUCT     2-dehydro-3-deoxy-L-rhamnonate [CPD:C03979];
            H2O [CPD:C00001]
REFERENCE   1
  AUTHORS   Rigo, L.U., Marechal, L.R., Vieira, M.M. and Veiga, L.A.
  TITLE     Oxidative pathway for L-rhamnose degradation in Pallularia
            pullulans.
  JOURNAL   Can. J. Microbiol. 31 (1985) 817-822.
  ORGANISM  Pullularia pullulans
PATHWAY     PATH: map00051  Fructose and mannose metabolism
STRUCTURES  PDB: 2GSH  2OZ3  2P0I  2P3Z  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.90
            ExPASy - ENZYME nomenclature database: 4.2.1.90
            ExplorEnz - The Enzyme Database: 4.2.1.90
            ERGO genome analysis and discovery system: 4.2.1.90
            BRENDA, the Enzyme Database: 4.2.1.90
///
ENTRY       EC 4.2.1.91                 Enzyme
NAME        arogenate dehydratase;
            carboxycyclohexadienyl dehydratase;
            L-arogenate hydro-lyase (decarboxylating)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     L-arogenate hydro-lyase (decarboxylating; L-phenylalanine-forming)
REACTION    L-arogenate = L-phenylalanine + H2O + CO2 [RN:R00691]
ALL_REAC    R00691;
            (other) R01373
SUBSTRATE   L-arogenate [CPD:C00826]
PRODUCT     L-phenylalanine [CPD:C00079];
            H2O [CPD:C00001];
            CO2 [CPD:C00011]
COMMENT     Also acts on prephenate and D-prephenyllactate. cf. EC 4.2.1.51,
            prephenate dehydratase.
REFERENCE   1  [PMID:3600377]
  AUTHORS   Fischer R, Jensen R.
  TITLE     Arogenate dehydratase.
  JOURNAL   Methods. Enzymol. 142 (1987) 495-502.
REFERENCE   2  [PMID:2972718]
  AUTHORS   Zamir LO, Tiberio R, Devor KA, Sauriol F, Ahmad S, Jensen RA.
  TITLE     Structure of D-prephenyllactate. A carboxycyclohexadienyl metabolite
            from Neurospora crassa.
  JOURNAL   J. Biol. Chem. 263 (1988) 17284-90.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   3  [PMID:3124763]
  AUTHORS   Siehl DL, Conn EE.
  TITLE     Kinetic and regulatory properties of arogenate dehydratase in
            seedlings of Sorghum bicolor (L.) Moench.
  JOURNAL   Arch. Biochem. Biophys. 260 (1988) 822-9.
  ORGANISM  Sorghum bicolor [GN:esbi]
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K05359  carboxycyclohexadienyl dehydratase
GENES       SPE: Spro_4447
            ASU: Asuc_1338
            XCV: XCV0653(pheC)
            CVI: CV_0224
            AZO: azo0499(pheC)
            HPA: HPAG1_1111
            BBT: BBta_4123
            MSM: MSMEG_3442
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.91
            ExPASy - ENZYME nomenclature database: 4.2.1.91
            ExplorEnz - The Enzyme Database: 4.2.1.91
            ERGO genome analysis and discovery system: 4.2.1.91
            BRENDA, the Enzyme Database: 4.2.1.91
///
ENTRY       EC 4.2.1.92                 Enzyme
NAME        hydroperoxide dehydratase;
            hydroperoxide isomerase;
            linoleate hydroperoxide isomerase;
            linoleic acid hydroperoxide isomerase;
            HPI;
            (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate
            12,13-hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate
            12,13-hydro-lyase
            [(9Z)-(13S)-12,13-epoxyoctadeca-9,11-dienoate-forming]
REACTION    (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate =
            (9Z)-(13S)-12,13-epoxyoctadeca-9,11-dienoate + H2O [RN:R04521]
ALL_REAC    R04521;
            (other) R07863 R07865
SUBSTRATE   (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate
PRODUCT     (9Z)-(13S)-12,13-epoxyoctadeca-9,11-dienoate [CPD:C04594];
            H2O [CPD:C00001]
COMMENT     Acts on a number of unsaturated fatty-acid hydroperoxides, forming
            the corresponding allene oxides.
REFERENCE   1  [PMID:4208994]
  AUTHORS   Esselman WJ, Clagett CO.
  TITLE     Products of linoleic hydroperoxide-decomposing enzyme of alfalfa
            seed.
  JOURNAL   J. Lipid. Res. 15 (1974) 173-8.
  ORGANISM  alfalfa
REFERENCE   2
  AUTHORS   Hamberg, M.
  TITLE     Mechanism of corn hydroperoxide isomerase - detection of
            12,13(S)-oxido-9(Z),11-octadecadienoic acid.
  JOURNAL   Biochim. Biophys. Acta 920 (1987) 76-84.
  ORGANISM  Zea mays [GN:ezma]
REFERENCE   3  [PMID:3178850]
  AUTHORS   Hamberg M.
  TITLE     Biosynthesis of 12-oxo-10,15(Z)-phytodienoic acid: identification of
            an allene oxide cyclase.
  JOURNAL   Biochem. Biophys. Res. Commun. 156 (1988) 543-50.
  ORGANISM  Zea mays [GN:ezma]
PATHWAY     PATH: map00592  alpha-Linolenic acid metabolism
ORTHOLOGY   KO: K01723  hydroperoxide dehydratase
GENES       ATH: AT5G42650(AOS)
            OSA: 4334233
STRUCTURES  PDB: 1U5U  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.92
            ExPASy - ENZYME nomenclature database: 4.2.1.92
            ExplorEnz - The Enzyme Database: 4.2.1.92
            ERGO genome analysis and discovery system: 4.2.1.92
            BRENDA, the Enzyme Database: 4.2.1.92
///
ENTRY       EC 4.2.1.93                 Enzyme
NAME        ATP-dependent NAD(P)H-hydrate dehydratase;
            reduced nicotinamide adenine dinucleotide hydrate dehydratase;
            ATP-dependent H4NAD(P)+OH dehydratase;
            (6S)-beta-6-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-
            dinucleotide hydro-lyase(ATP-hydrolysing)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleot
            ide hydro-lyase (ATP-hydrolysing; NADH-forming)
REACTION    ATP + (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine
            dinucleotide = ADP + phosphate + NADH [RN:R00129]
ALL_REAC    R00129
SUBSTRATE   ATP [CPD:C00002];
            (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine
            dinucleotide [CPD:C04856]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            NADH [CPD:C00004]
COMMENT     Also acts on hydrated NADPH. NADH spontaneously hydrates to both
            (6S)- and (6R)- compounds, and these spontaneously interconvert.
            Hence EC 4.2.1.93 can convert the whole mixture into NADH [1].
REFERENCE   1  [PMID:3061454]
  AUTHORS   Acheson SA, Kirkman HN, Wolfenden R.
  TITLE     Equilibrium of 5,6-hydration of NADH and mechanism of ATP-dependent
            dehydration.
  JOURNAL   Biochemistry. 27 (1988) 7371-5.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:13331940]
  AUTHORS   MEINHART JO, CHAYKIN S, KREBS EG.
  TITLE     Enzymatic conversion of a reduced diphosphopyridine nucleotide
            derivative to reduced diphosphopyridine nucleotide.
  JOURNAL   J. Biol. Chem. 220 (1956) 821-9.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:16436443]
  AUTHORS   Regueiro V, Campos MA, Pons J, Alberti S, Bengoechea JA.
  TITLE     The uptake of a Klebsiella pneumoniae capsule polysaccharide mutant
            triggers an inflammatory response by human airway epithelial cells.
  JOURNAL   Microbiology. 152 (2006) 555-66.
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.93
            ExPASy - ENZYME nomenclature database: 4.2.1.93
            ExplorEnz - The Enzyme Database: 4.2.1.93
            ERGO genome analysis and discovery system: 4.2.1.93
            BRENDA, the Enzyme Database: 4.2.1.93
///
ENTRY       EC 4.2.1.94                 Enzyme
NAME        scytalone dehydratase;
            scytalone 7,8-hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     scytalone 7,8-hydro-lyase (1,3,8-trihydroxynaphthalene-forming)
REACTION    scytalone = 1,3,8-trihydroxynaphthalene + H2O [RN:R02907]
ALL_REAC    R02907
SUBSTRATE   scytalone [CPD:C00779]
PRODUCT     1,3,8-trihydroxynaphthalene [CPD:C01173];
            H2O [CPD:C00001]
COMMENT     Involved, with EC 1.1.1.252 tetrahydroxynaphthalene reductase, in
            the biosynthesis of melanin in pathogenic fungi.
REFERENCE   1
  AUTHORS   Butler, M.J., Lazarovits, G., Higgins, V.J. and Lachance, M.-A.
  TITLE     Partial-purification and characterization of a dehydratase
            associated with the pentaketide melanogenesis pathway of
            Phaeococcomyces sp and other fungi.
  JOURNAL   Exp. Mycol. 12 (1988) 367-376.
  ORGANISM  Phaeococcomyces sp.
REFERENCE   2
  AUTHORS   Tajima, S., Kubo, Y., Furusawa, I. and Shishiyama, J.
  TITLE     Purification of a melanin biosynthetic enzyme converting scytalone
            to 1,3,8-trihydroxynaphthalene from Cochliobolus miyabeanus.
  JOURNAL   Exp. Mycol. 13 (1989) 69.
  ORGANISM  Cochliobolus miyabeanus
REFERENCE   3
  AUTHORS   Wheeler, M.H. and Greenblatt, G.A.
  TITLE     The inhibition of melanin biosynthetic reactions in Pyricularia
            oryzae by compounds that prevent rice blast disease.
  JOURNAL   Exp. Mycol. 12 (1988) 151-160.
  ORGANISM  Pyricularia oryzae
STRUCTURES  PDB: 1IDP  1STD  2STD  3STD  4STD  5STD  6STD  7STD  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.94
            ExPASy - ENZYME nomenclature database: 4.2.1.94
            ExplorEnz - The Enzyme Database: 4.2.1.94
            ERGO genome analysis and discovery system: 4.2.1.94
            BRENDA, the Enzyme Database: 4.2.1.94
///
ENTRY       EC 4.2.1.95                 Enzyme
NAME        kievitone hydratase;
            KHase;
            kievitone-hydrate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     kievitone-hydrate hydro-lyase (kievitone-forming)
REACTION    kievitone hydrate = kievitone + H2O [RN:R03622]
ALL_REAC    R03622
SUBSTRATE   kievitone hydrate [CPD:C02549]
PRODUCT     kievitone [CPD:C01590];
            H2O [CPD:C00001]
COMMENT     The enzyme from Fusarium sp. hydrates the methylbutenyl sidechain of
            the isoflavonoid phytoalexins, thus reducing their toxicity.
REFERENCE   1  [PMID:1366757]
  AUTHORS   Turbek CS, Li DX, Choi GH, Schardl CL, Smith DA.
  TITLE     Induction and purification of kievitone hydratase from Fusarium
            solani f. sp. phaseoli.
  JOURNAL   Phytochemistry. 29 (1990) 2841-6.
  ORGANISM  Fusarium solani
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.95
            ExPASy - ENZYME nomenclature database: 4.2.1.95
            ExplorEnz - The Enzyme Database: 4.2.1.95
            ERGO genome analysis and discovery system: 4.2.1.95
            BRENDA, the Enzyme Database: 4.2.1.95
///
ENTRY       EC 4.2.1.96                 Enzyme
NAME        4a-hydroxytetrahydrobiopterin dehydratase;
            4alpha-hydroxy-tetrahydropterin dehydratase;
            pterin-4alpha-carbinolamine dehydratase;
            4a-hydroxytetrahydrobiopterin hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxy
            pterin hydro-lyase
            [(6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin-formin
            g]
REACTION    (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-
            hydroxypterin =
            (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H2O
            [RN:R04734]
ALL_REAC    R04734
SUBSTRATE   (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-
            hydroxypterin [CPD:C06486]
PRODUCT     (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin
            [CPD:C06487];
            H2O [CPD:C00001]
COMMENT     Catalyses the dehydration of 4a-hydroxytetrahydrobiopterins
REFERENCE   1  [PMID:8444860]
  AUTHORS   Hauer CR, Rebrin I, Thony B, Neuheiser F, Curtius HC, Hunziker P,
            Blau N, Ghisla S, Heizmann CW.
  TITLE     Phenylalanine hydroxylase-stimulating protein/pterin-4
            alpha-carbinolamine dehydratase from rat and human liver.
            Purification, characterization, and complete amino acid sequence.
  JOURNAL   J. Biol. Chem. 268 (1993) 4828-31.
  ORGANISM  human [GN:hsa], rat [GN:rno]
ORTHOLOGY   KO: K01724  
GENES       HSA: 5092(PCBD1) 84105(PCBD2)
            MCC: 709875(LOC709875)
            MMU: 13180(Pcbd1)
            RNO: 29700(Pcbd1)
            CFA: 609680(PCBD1) 609970(PCBD2)
            GGA: 395729(PCBD1)
            XLA: 397951(LOC397951) 496367(LOC496367)
            XTR: 496425(pcbd1)
            DRE: 393787(pcbd1)
            DME: Dmel_CG1963(Pcd)
            CEL: T10B11.1(pcbd-1)
            CME: CMM157C
            AGO: AGOS_ABR046C
            SPO: SPAC27D7.04
            AOR: AO090003000574
            DDI: DDBDRAFT_0215286
            TET: TTHERM_01084290
            TCR: 511165.54
            LMA: LmjF11.0220
            XFA: XF2604
            XFT: PD1980(phhB)
            XCC: XCC2080(phhB)
            XCB: XC_2102
            XCV: XCV2428(phhB)
            XAC: XAC2116(phhb)
            XOO: XOO3067(phhB)
            XOM: XOO_2920(XOO2920)
            VCH: VCA0827
            VCO: VC0395_0408(phhB)
            VVU: VV2_0454
            VVY: VVA1004
            VPA: VPA0577
            PPR: PBPRB1163
            PAE: PA0871(phhB)
            PAU: PA14_53000(phhB)
            PPU: PP_4491(phhB)
            PST: PSPTO_1821(phhB)
            PSB: Psyr_3576
            PSP: PSPPH_3532(phhB)
            PFL: PFL_1610
            PFO: Pfl_1498
            PEN: PSEEN3893(phhB)
            PAR: Psyc_0131(phhB)
            PCR: Pcryo_1553
            SON: SO_1667
            SDN: Sden_2594
            SFR: Sfri_1329
            SAZ: Sama_2221
            SBL: Sbal_1485
            SBM: Shew185_1480
            SLO: Shew_1436
            SPC: Sputcn32_1387
            SHE: Shewmr4_2606
            SHM: Shewmr7_2673
            SHN: Shewana3_1422 Shewana3_2780
            SHW: Sputw3181_2714
            ILO: IL0724
            CPS: CPS_3765(phhB)
            PHA: PSHAa2042(phhB)
            PAT: Patl_1692
            MAQ: Maqu_0976
            LPN: lpg1999
            LPF: lpl1975
            LPP: lpp1980
            MCA: MCA0497(phhB)
            TCX: Tcr_0631
            NOC: Noc_2226
            HCH: HCH_04986
            CSA: Csal_1321
            ABO: ABO_2225(phhB)
            AHA: AHA_1884 AHA_1885
            CVI: CV_2366
            RSO: RSc3356(phhB)
            REU: Reut_A0417 Reut_A3388
            REH: H16_A0431 H16_A3679(phhB)
            RME: Rmet_3534
            BMA: BMA2926
            BXE: Bxe_A0010 Bxe_B2429(pcbD)
            BUR: Bcep18194_A3258
            BPS: BPSL3425
            BPM: BURPS1710b_0207
            BTE: BTH_I3338
            BPE: BP3325
            BPA: BPP3671
            BBR: BB4106
            RFR: Rfer_1410
            POL: Bpro_0169 Bpro_1698
            HAR: HEAR0874
            MMS: mma_0850
            NEU: NE0077
            NMU: Nmul_A0712
            EBA: ebB5
            AZO: azo2296(phhB)
            DAR: Daro_0453
            TBD: Tbd_1841
            HPA: HPAG1_0784
            PCA: Pcar_2286
            BBA: Bd0889(pcd)
            ADE: Adeh_4024
            MXA: MXAN_6773
            RFE: RF_0997
            RBE: RBE_1407
            PUB: SAR11_0321(phhB)
            MLO: mlr4350
            MES: Meso_3347
            SME: SMc03834(pcbD)
            ATU: Atu2676
            RET: RHE_CH03934(pcbD)
            RLE: RL4526
            BME: BMEI1864
            BMF: BAB1_0077(phhB)
            BMS: BR0082(phhB)
            BMB: BruAb1_0080(phhB)
            BOV: BOV_0080(phhB)
            BJA: bll0532
            BRA: BRADO0254(phhB)
            BBT: BBta_0248(phhB)
            RPA: RPA0404(phhB)
            RPB: RPB_0099
            RPC: RPC_2524
            RPD: RPD_0703
            RPE: RPE_2708
            NWI: Nwi_2809
            NHA: Nham_3629
            CCR: CC_0245
            SIL: SPO3733(phhB)
            SIT: TM1040_2474
            RSP: RSP_0898(DCOHM)
            RDE: RD1_0944(pcd)
            HNE: HNE_3096
            NAR: Saro_1118
            ELI: ELI_01705
            GBE: GbCGDNIH1_0777
            RRU: Rru_A3581
            MGM: Mmc1_2161
            SUS: Acid_5239
            BAN: BA4587
            BAR: GBAA4587
            BAA: BA_5026
            BAT: BAS4254
            BCE: BC4353
            BCA: BCE_4440
            BCZ: BCZK4103(dcoH)
            BTK: BT9727_4092(dcoH)
            BTL: BALH_3944(dcoH)
            BCL: ABC4006
            GKA: GK1984
            MTU: Rv0984(moaB2) Rv1159A Rv3110(moaB1)
            MTC: MT1196
            MBO: Mb1010(moaB2) Mb1191c Mb3137(moaB1) Mb3354c(moaB3)
            MBB: BCG_1039(moaB2) BCG_3135(moaB1) BCG_3391c(moaB3)
            MLE: ML1503A
            MPA: MAP2623
            MSM: MSMEG_5150
            CGL: NCgl0447(cgl0465)
            CGB: cg0549
            CEF: CE0476
            CJK: jk1529(moaB)
            NFA: nfa27510 nfa47610
            RHA: RHA1_ro05930
            SCO: SCO6540(SC5C7.25)
            SMA: SAV1858(dcoH)
            TFU: Tfu_1547
            FRA: Francci3_1815 Francci3_1826 Francci3_1828 Francci3_3867
            FAL: FRAAL6136
            SEN: SACE_0980
            RBA: RB4517
            LIL: LB335(phhB)
            LIC: LIC20256(phs)
            LBJ: LBJ_4246(phhB)
            LBL: LBL_4260(phhB)
            SYN: ssl2296(dcoH)
            SYW: SYNW1794
            SYC: syc2449_d(dcoH)
            SYF: Synpcc7942_1636
            SYD: Syncc9605_0673
            SYG: sync_1946
            SYR: SynRCC307_0900
            SYX: SynWH7803_1805
            CYA: CYA_1048
            CYB: CYB_2873
            TEL: tsl1825
            GVI: gll0926 gsl1645
            ANA: asr4549
            AVA: Ava_2511
            PMA: Pro0490
            PMM: PMM0491
            PMT: PMT1283
            PMN: PMN2A_1824
            PMI: PMT9312_0492
            PMB: A9601_05471
            PMC: P9515_05551
            PMF: P9303_07131
            PMG: P9301_05181
            PME: NATL1_05481
            SRU: SRU_1447
            CHU: CHU_3388(phhB)
            GFO: GFO_1496(pcbD)
            CTE: CT0342
            PLT: Plut_0106
            TTH: TTC1451
            TTJ: TTHA1803
            AAE: aq_049(phhB)
            HAL: VNG1773G(cad)
            HMA: rrnAC1707(cad)
            HWA: HQ2029A(cad) HQ3342A(cad)
            NPH: NP1766A
            SSO: SSO2187
            STO: STS230
            SAI: Saci_2299(phs)
STRUCTURES  PDB: 1DCO  1DCP  1RU0  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.96
            ExPASy - ENZYME nomenclature database: 4.2.1.96
            ExplorEnz - The Enzyme Database: 4.2.1.96
            ERGO genome analysis and discovery system: 4.2.1.96
            BRENDA, the Enzyme Database: 4.2.1.96
///
ENTRY       EC 4.2.1.97                 Enzyme
NAME        phaseollidin hydratase;
            phaseollidin-hydrate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     phaseollidin-hydrate hydro-lyase (phaseollidin-forming)
REACTION    phaseollidin hydrate = phaseollidin + H2O [RN:R04728]
ALL_REAC    R04728
SUBSTRATE   phaseollidin hydrate [CPD:C05229]
PRODUCT     phaseollidin [CPD:C05230];
            H2O [CPD:C00001]
COMMENT     The enzyme from Fusarium solani, which is distinct from kievitone
            hydratase (EC 4.2.1.95), hydrates the methylbutenyl side-chain of
            the isoflavonoid phytoalexin, phaseollidin.
REFERENCE   1  [PMID:1521768]
  AUTHORS   Turbek CS, Smith DA, Schardl CL.
  TITLE     An extracellular enzyme from Fusarium solani f. sp. phaseoli which
            catalyses hydration of the isoflavonoid phytoalexin, phaseollidin.
  JOURNAL   FEMS. Microbiol. Lett. 73 (1992) 187-90.
  ORGANISM  Fusarium solani
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.97
            ExPASy - ENZYME nomenclature database: 4.2.1.97
            ExplorEnz - The Enzyme Database: 4.2.1.97
            ERGO genome analysis and discovery system: 4.2.1.97
            BRENDA, the Enzyme Database: 4.2.1.97
///
ENTRY       EC 4.2.1.98                 Enzyme
NAME        16alpha-hydroxyprogesterone dehydratase;
            hydroxyprogesterone dehydroxylase;
            16alpha-hydroxyprogesterone dehydroxylase;
            16alpha-dehydroxylase;
            16alpha-hydroxyprogesterone hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     16alpha-hydroxyprogesterone hydro-lyase
            (16,17-didehydroprogesterone-forming)
REACTION    16alpha-hydroxyprogesterone = 16,17-didehydroprogesterone + H2O
            [RN:R04166]
ALL_REAC    R04166;
            (other) R05174
SUBSTRATE   16alpha-hydroxyprogesterone [CPD:C03748]
PRODUCT     16,17-didehydroprogesterone [CPD:C03207];
            H2O [CPD:C00001]
COMMENT     16alpha-Hydroxypregnenolone is also a substrate.
REFERENCE   1  [PMID:4052439]
  AUTHORS   Glass TL, Lamppa RS.
  TITLE     Purification and properties of 16 alpha-hydroxyprogesterone
            dehydroxylase from Eubacterium sp. strain 144.
  JOURNAL   Biochim. Biophys. Acta. 837 (1985) 103-10.
  ORGANISM  Eubacterium sp.
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.98
            ExPASy - ENZYME nomenclature database: 4.2.1.98
            ExplorEnz - The Enzyme Database: 4.2.1.98
            ERGO genome analysis and discovery system: 4.2.1.98
            BRENDA, the Enzyme Database: 4.2.1.98
///
ENTRY       EC 4.2.1.99                 Enzyme
NAME        2-methylisocitrate dehydratase;
            (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase
            [(Z)-but-2-ene-1,2,3-tricarboxylate-forming]
REACTION    (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate =
            (Z)-but-2-ene-1,2,3-tricarboxylate + H2O [RN:R04425]
ALL_REAC    R04425
SUBSTRATE   (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate [CPD:C04593]
PRODUCT     (Z)-but-2-ene-1,2,3-tricarboxylate [CPD:C04225];
            H2O [CPD:C00001]
COMMENT     The enzyme from the fungus Yarrowia lipolytica (Saccharomycopsis)
            does not act on isocitrate.
REFERENCE   1
  AUTHORS   Aoki, H., Uchiyama, H., Umetsu, H., Tabuchi, T.
  TITLE     Isolation of 2-methylisocitrate dehydratase, a new enzyme serving in
            the methylcitric acid cycle for propionate metabolism, from Yarrowia
            lipolytica.
  JOURNAL   Biosci. Biotechnol. Biochem. 59 (1995) 1825-1828.
  ORGANISM  Yarrowia lipolytica [GN:dyli]
REFERENCE   2
  AUTHORS   Tabuchi, T., Umetsu, H., Aoki, H., Uchiyama, H.
  TITLE     Characteristics of 2-methylisocitrate dehydratase, isolated from
            Yarrowia lipolytica, in comparison to aconitase.
  JOURNAL   Biosci. Biotechnol. Biochem. 59 (1995) 2013-2017.
  ORGANISM  Yarrowia lipolytica [GN:dyli]
PATHWAY     PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K05608  2-methylisocitrate dehydratase
GENES       PAP: PSPA7_4724(acnD)
            PFL: PFL_1863(acnD)
            BPM: BURPS1710b_A1738(acnD)
            BPL: BURPS1106A_A0290(acnD)
            BPD: BURPS668_A0384(acnD)
            BTE: BTH_II2187(acnD)
            BAN: BA2349(mmgE)
            BAR: GBAA2349(mmgE)
            BAA: BA_2845
            BAT: BAS2189
            BCE: BC2286
            BCA: BCE_2377(mmgE)
            BCZ: BCZK2112(prpD)
            BTK: BT9727_2126(prpD)
            BLI: BL00562(mmgE)
            BLD: BLi04095(mmgE)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.99
            ExPASy - ENZYME nomenclature database: 4.2.1.99
            ExplorEnz - The Enzyme Database: 4.2.1.99
            ERGO genome analysis and discovery system: 4.2.1.99
            BRENDA, the Enzyme Database: 4.2.1.99
            CAS: 170780-51-5
///
ENTRY       EC 4.2.1.100                Enzyme
NAME        cyclohexa-1,5-dienecarbonyl-CoA hydratase;
            cyclohexa-1,5-diene-1-carbonyl-CoA hydratase;
            dienoyl-CoA hydratase;
            cyclohexa-1,5-dienecarbonyl-CoA hydro-lyase (incorrect)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     6-hydroxycyclohex-1-enecarbonyl-CoA
            (cyclohexa-1,5-dienecarbonyl-CoA-forming)
REACTION    6-hydroxycyclohex-1-enecarbonyl-CoA =
            cyclohexa-1,5-dienecarbonyl-CoA + H2O [RN:R05597]
ALL_REAC    R05597
SUBSTRATE   6-hydroxycyclohex-1-enecarbonyl-CoA [CPD:C06749]
PRODUCT     cyclohexa-1,5-dienecarbonyl-CoA [CPD:C06322];
            H2O [CPD:C00001]
COMMENT     Forms part of the anaerobic benzoate degradation pathway, which also
            includes EC 1.3.99.7 (glutaryl-CoA dehydrogenase), EC 1.3.99.15
            (benzoyl-CoA reductase) and EC 4.2.1.55 (3-hydroyxbutyryl-CoA
            dehydratase).
REFERENCE   1  [PMID:9738901]
  AUTHORS   Laempe D, Eisenreich W, Bacher A, Fuchs G.
  TITLE     Cyclohexa-1,5-diene-1-carbonyl-CoA hydratase [corrected], an enzyme
            involved in anaerobic metabolism of benzoyl-CoA in the denitrifying
            bacterium Thauera aromatica.
  JOURNAL   Eur. J. Biochem. 255 (1998) 618-27.
  ORGANISM  Thauera aromatica
REFERENCE   2  [PMID:8990279]
  AUTHORS   Harwood CS, Gibson J.
  TITLE     Shedding light on anaerobic benzene ring degradation: a process
            unique to prokaryotes?
  JOURNAL   J. Bacteriol. 179 (1997) 301-9.
  ORGANISM  Thauera aromatica, Rhodopseudomonas palustris, Azoarcus evansii,
            Pseudomonas sp.
REFERENCE   3  [PMID:8436125]
  AUTHORS   Koch J, Eisenreich W, Bacher A, Fuchs G.
  TITLE     Products of enzymatic reduction of benzoyl-CoA, a key reaction in
            anaerobic aromatic metabolism.
  JOURNAL   Eur. J. Biochem. 211 (1993) 649-61.
  ORGANISM  Rhodopseudomonas palustris, Pseudomonas sp.
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
ORTHOLOGY   KO: K07537  cyclohexa-1,5-dienecarbonyl-CoA hydratase
GENES       EBA: ebA5296(dch)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.100
            ExPASy - ENZYME nomenclature database: 4.2.1.100
            ExplorEnz - The Enzyme Database: 4.2.1.100
            ERGO genome analysis and discovery system: 4.2.1.100
            UM-BBD (Biocatalysis/Biodegradation Database): 4.2.1.100
            BRENDA, the Enzyme Database: 4.2.1.100
///
ENTRY       EC 4.2.1.101                Enzyme
NAME        trans-feruloyl-CoA hydratase;
            trans-feruloyl-CoA hydro-lyase (incorrect)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     4-hydroxy-3-methoxyphenyl-beta-hydroxypropanoyl-CoA hydro-lyase
            (trans-feruloyl-CoA-forming)
REACTION    4-hydroxy-3-methoxyphenyl-beta-hydroxypropanoyl-CoA =
            trans-feruloyl-CoA + H2O [RN:R05772]
ALL_REAC    R05772
SUBSTRATE   4-hydroxy-3-methoxyphenyl-beta-hydroxypropanoyl-CoA
PRODUCT     trans-feruloyl-CoA [CPD:C00406];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:9611814]
  AUTHORS   Narbad A, Gasson MJ.
  TITLE     Metabolism of ferulic acid via vanillin using a novel CoA-dependent
            pathway in a newly-isolated strain of Pseudomonas fluorescens.
  JOURNAL   Microbiology. 144 ( Pt 5) (1998) 1397-405.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   2  [PMID:6870241]
  AUTHORS   Pometto AL 3rd, Crawford DL.
  TITLE     Whole-cell bioconversion of vanillin to vanillic acid by
            Streptomyces viridosporus.
  JOURNAL   Appl. Environ. Microbiol. 45 (1983) 1582-5.
  ORGANISM  Streptomyces viridosporus
STRUCTURES  PDB: 2J5I  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.101
            ExPASy - ENZYME nomenclature database: 4.2.1.101
            ExplorEnz - The Enzyme Database: 4.2.1.101
            ERGO genome analysis and discovery system: 4.2.1.101
            BRENDA, the Enzyme Database: 4.2.1.101
            CAS: 197462-62-7
///
ENTRY       EC 4.2.1.102      Obsolete  Enzyme
NAME        Transferred to 4.2.1.100
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
COMMENT     Transferred entry: now EC 4.2.1.100, cyclohexa-1,5-dienecarbonyl-CoA
            hydratase (EC 4.2.1.102 created 2001, deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.102
            ExPASy - ENZYME nomenclature database: 4.2.1.102
            ExplorEnz - The Enzyme Database: 4.2.1.102
            ERGO genome analysis and discovery system: 4.2.1.102
            BRENDA, the Enzyme Database: 4.2.1.102
///
ENTRY       EC 4.2.1.103                Enzyme
NAME        cyclohexyl-isocyanide hydratase;
            isonitrile hydratase;
            N-cyclohexylformamide hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     N-cyclohexylformamide hydro-lyase (cyclohexyl-isocyanide-forming)
REACTION    N-cyclohexylformamide = cyclohexyl isocyanide + H2O [RN:R05771]
ALL_REAC    R05771
SUBSTRATE   N-cyclohexylformamide [CPD:C11519]
PRODUCT     cyclohexyl isocyanide [CPD:C11520];
            H2O [CPD:C00001]
COMMENT     The enzyme from Pseudomonas putida strain N19-2 can also catalyse
            the hydration of other isonitriles to the corresponding
            N-substituted formamides. The enzyme has no metal requirements.
REFERENCE   1  [PMID:11306561]
  AUTHORS   Goda M, Hashimoto Y, Shimizu S, Kobayashi M.
  TITLE     Discovery of a novel enzyme, isonitrile hydratase, involved in
            nitrogen-carbon triple bond cleavage.
  JOURNAL   J. Biol. Chem. 276 (2001) 23480-5.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00930  Caprolactam degradation
GENES       BPM: BURPS1710b_A0954
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.103
            ExPASy - ENZYME nomenclature database: 4.2.1.103
            ExplorEnz - The Enzyme Database: 4.2.1.103
            ERGO genome analysis and discovery system: 4.2.1.103
            UM-BBD (Biocatalysis/Biodegradation Database): 4.2.1.103
            BRENDA, the Enzyme Database: 4.2.1.103
///
ENTRY       EC 4.2.1.104                Enzyme
NAME        cyanase;
            cyanate lyase;
            cyanate hydrolase;
            cyanate aminohydrolase;
            cyanate C-N-lyase;
            cyanate hydratase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     carbamate hydro-lyase
REACTION    (1) cyanate + HCO3- + 2 H+ = NH3 + 2 CO2 (overall reaction)
            [RN:R07315];
            (2) (1a) cyanate + HCO3- + H+ = carbamate + CO2 [RN:R07316];
            (3) (1b) carbamate + H+ = NH3 + CO2 (spontaneous)
ALL_REAC    R07315 R07316;
            (other) R03546
SUBSTRATE   cyanate [CPD:C01417];
            HCO3- [CPD:C00288];
            H+ [CPD:C00080];
            carbamate [CPD:C01563]
PRODUCT     NH3 [CPD:C00014];
            CO2 [CPD:C00011];
            carbamate [CPD:C01563]
COMMENT     This enzyme, which is found in bacteria and plants, is used to
            decompose cyanate, which can be used as the sole source of nitrogen
            [6,7]. Reaction (1) can be considered as the reverse of 'carbamate =
            cyanate + H2O', where this is assisted by reaction with bicarbonate
            and carbon dioxide (see mechanism above) [2], and hence is
            classified in sub-subclass 4.2.1. Bicarbonate functions as a
            recycling substrate [2].
REFERENCE   1  [PMID:6994799]
  AUTHORS   Anderson PM.
  TITLE     Purification and properties of the inducible enzyme cyanase.
  JOURNAL   Biochemistry. 19 (1980) 2882-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:3110153]
  AUTHORS   Johnson WV, Anderson PM.
  TITLE     Bicarbonate is a recycling substrate for cyanase.
  JOURNAL   J. Biol. Chem. 262 (1987) 9021-5.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:13775509]
  AUTHORS   TAUSSIG A.
  TITLE     The synthesis of the induced enzyme, ''cyanase'', in E. coli.
  JOURNAL   Biochim. Biophys. Acta. 44 (1960) 510-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:5322950]
  AUTHORS   Taussig A.
  TITLE     Some properties of the induced enzyme cyanase.
  JOURNAL   Can. J. Biochem. 43 (1965) 1063-9.
REFERENCE   5  [PMID:7947823]
  AUTHORS   Anderson PM, Korte JJ, Holcomb TA.
  TITLE     Reaction of the N-terminal methionine residues in cyanase with
            diethylpyrocarbonate.
  JOURNAL   Biochemistry. 33 (1994) 14121-5.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:7768821]
  AUTHORS   Kozliak EI, Fuchs JA, Guilloton MB, Anderson PM.
  TITLE     Role of bicarbonate/CO2 in the inhibition of Escherichia coli growth
            by cyanate.
  JOURNAL   J. Bacteriol. 177 (1995) 3213-9.
REFERENCE   7  [PMID:10801492]
  AUTHORS   Walsh MA, Otwinowski Z, Perrakis A, Anderson PM, Joachimiak A.
  TITLE     Structure of cyanase reveals that a novel dimeric and decameric
            arrangement of subunits is required for formation of the enzyme
            active site.
  JOURNAL   Structure. 8 (2000) 505-14.
PATHWAY     PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K01725  cyanate lyase
GENES       ATH: AT3G23490(CYN)
            OSA: 4348870
            ANI: AN7331.2
            AFM: AFUA_2G16530
            AOR: AO090102000190
            CNE: CND04630
            UMA: UM01973.1
            ECO: b0340(cynS)
            ECJ: JW0331(cynS)
            ECE: Z0436(cynS)
            ECS: ECs0393
            ECW: EcE24377A_0365(cynS)
            ECX: EcHS_A0405(cynS)
            PLU: plu0112(cynS)
            SPE: Spro_1533
            PAE: PA2052(cynS)
            PAU: PA14_37965(cynS)
            PAP: PSPA7_3236(cynS)
            PPF: Pput_3239
            PST: PSPTO_1930(cynS)
            PSB: Psyr_3483
            PSP: PSPPH_3410(cynS)
            PFL: PFL_1490(cynS)
            PFO: Pfl_3369
            PEN: PSEEN3599(cynS)
            PAT: Patl_3478
            SDE: Sde_2824
            PIN: Ping_0702
            TCX: Tcr_0040
            AEH: Mlg_2586
            MMW: Mmwyl1_3729
            CVI: CV_1880(cynS)
            RSO: RS02188(RSp1630)
            REH: H16_B0046(cynS)
            RME: Rmet_5864
            BMA: BMA2466(cynS)
            BMV: BMASAVP1_A0385(cynS)
            BML: BMA10299_A1245(cynS)
            BMN: BMA10247_3321(cynS)
            BXE: Bxe_B0547 Bxe_C0467
            BVI: Bcep1808_6046
            BUR: Bcep18194_B2815
            BCN: Bcen_4778
            BCH: Bcen2424_3389
            BAM: Bamb_5946
            BPS: BPSL2950(cynS)
            BPM: BURPS1710b_3463(cynS)
            BPL: BURPS1106A_3464(cynS)
            BPD: BURPS668_3427(cynS)
            BTE: BTH_I1198(cynS)
            PNU: Pnuc_0994
            RFR: Rfer_3739
            POL: Bpro_0289
            VEI: Veis_3975
            MPT: Mpe_A3484
            DAR: Daro_1442
            TBD: Tbd_1941
            MFA: Mfla_2169
            BJA: bll5731
            BRA: BRADO2774(cynS)
            BBT: BBta_5412(cynS)
            RPA: RPA2115(cynS)
            RPB: RPB_2057
            RPE: RPE_4635
            NWI: Nwi_1302
            NHA: Nham_1631
            XAU: Xaut_2620
            STH: STH22
            MTA: Moth_2054
            MPA: MAP4098
            MAV: MAV_4538(cynS)
            MSM: MSMEG_5359(cynS)
            MVA: Mvan_2755
            MGI: Mflv_1997
            MMC: Mmcs_0717
            MKM: Mkms_0731
            MJL: Mjls_0711
            SYN: slr0899(cynS)
            SYW: SYNW2490(cynS)
            SYC: syc1989_d(cynS)
            SYF: Synpcc7942_2104
            SYD: Syncc9605_2659
            SYE: Syncc9902_2287
            SYG: sync_2901(cynS)
            SYR: SynRCC307_2485(cynS)
            SYX: SynWH7803_2495(cynS)
            ANA: all1291(cynS)
            AVA: Ava_3015
            PMM: PMM0373(cynS)
            PMN: PMN2A_1390
            PME: NATL1_00701(cynS)
            AAE: aq_212(cynS)
            STO: ST1023
STRUCTURES  PDB: 2IU7  2IUO  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.104
            ExPASy - ENZYME nomenclature database: 4.2.1.104
            ExplorEnz - The Enzyme Database: 4.2.1.104
            ERGO genome analysis and discovery system: 4.2.1.104
            UM-BBD (Biocatalysis/Biodegradation Database): 4.2.1.104
            BRENDA, the Enzyme Database: 4.2.1.104
            CAS: 37289-24-0
///
ENTRY       EC 4.2.1.105                Enzyme
NAME        2-hydroxyisoflavanone dehydratase;
            2,7,4'-trihydroxyisoflavanone hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     2,7,4'-trihydroxyisoflavanone hydro-lyase (daidzein-forming)
REACTION    2,7,4'-trihydroxyisoflavanone = daidzein + H2O [RN:R07317]
ALL_REAC    R07317;
            (other) R06793 R07723
SUBSTRATE   2,7,4'-trihydroxyisoflavanone [CPD:C15567]
PRODUCT     daidzein [CPD:C10208];
            H2O [CPD:C00001]
COMMENT     Catalyses the final step in the formation of the isoflavonoid
            skeleton. The reaction also occurs spontaneously.
REFERENCE   1
  AUTHORS   Hakamatsuka, T., Mori, K., Ishida, S., Ebizuka, Y and Sankawa, U.
  TITLE     Purification of 2-hydroxyisoflavanone dehydratase from the cell
            cultures of Pueraria lobata.
  JOURNAL   Phytochemistry 49 (1998) 497-505.
  ORGANISM  Pueraria lobata
PATHWAY     PATH: map00943  Isoflavonoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.105
            ExPASy - ENZYME nomenclature database: 4.2.1.105
            ExplorEnz - The Enzyme Database: 4.2.1.105
            ERGO genome analysis and discovery system: 4.2.1.105
            BRENDA, the Enzyme Database: 4.2.1.105
            CAS: 56022-25-4
///
ENTRY       EC 4.2.1.106                Enzyme
NAME        bile-acid 7alpha-dehydratase;
            7alpha,12alpha-dihydroxy-3-oxochol-4-enoate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     7alpha,12alpha-dihydroxy-3-oxochol-4-enoate hydro-lyase
            (12alpha-hydroxy-3-oxochola-4,6-dienoate-forming)
REACTION    7alpha,12alpha-dihydroxy-3-oxochol-4-enoate =
            12alpha-hydroxy-3-oxochola-4,6-dienoate + H2O [RN:R07318]
ALL_REAC    R07318
SUBSTRATE   7alpha,12alpha-dihydroxy-3-oxochol-4-enoate [CPD:C15568]
PRODUCT     12alpha-hydroxy-3-oxochola-4,6-dienoate [CPD:C15569];
            H2O [CPD:C00001]
COMMENT     The enzyme from Eubacterium sp. strain VPI 12708 can also use
            7alpha-hydroxy-3-oxochol-4-enoate as a substrate but not
            7alpha,12alpha-dihydroxy-3-oxochol-5beta-anoate,
            3alpha,7alpha,12alpha-trihydroxychol-5beta-anoate or
            7beta-hydroxy-3-oxochol-4-enoate.
REFERENCE   1  [PMID:8808760]
  AUTHORS   Dawson JA, Mallonee DH, Bjorkhem I, Hylemon PB.
  TITLE     Expression and characterization of a C24 bile acid 7
            alpha-dehydratase from Eubacterium sp. strain VPI 12708 in
            Escherichia coli.
  JOURNAL   J. Lipid. Res. 37 (1996) 1258-67.
  ORGANISM  Eubacterium sp.
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.106
            ExPASy - ENZYME nomenclature database: 4.2.1.106
            ExplorEnz - The Enzyme Database: 4.2.1.106
            ERGO genome analysis and discovery system: 4.2.1.106
            BRENDA, the Enzyme Database: 4.2.1.106
///
ENTRY       EC 4.2.1.107                Enzyme
NAME        3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA
            hydratase;
            46 kDa hydratase 2;
            (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-
            CoA hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-C
            oA hydro-lyase
            [(24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA-f
            orming]
REACTION    (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-
            CoA =
            (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA +
            H2O [RN:R04813]
ALL_REAC    R04813
SUBSTRATE   (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-
            CoA
PRODUCT     (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA;
            H2O [CPD:C00001]
COMMENT     This enzyme forms part of the rat peroxisomal multifunctional enzyme
            perMFE-2, which also exhibits a dehydrogenase activity. The enzyme
            is involved in the beta-oxidation of the cholesterol side chain in
            the cholic-acid-biosynthesis pathway.
REFERENCE   1  [PMID:9371691]
  AUTHORS   Qin YM, Haapalainen AM, Conry D, Cuebas DA, Hiltunen JK, Novikov DK.
  TITLE     Recombinant 2-enoyl-CoA hydratase derived from rat peroxisomal
            multifunctional enzyme 2: role of the hydratase reaction in bile
            acid synthesis.
  JOURNAL   Biochem. J. 328 ( Pt 2) (1997) 377-82.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:8619845]
  AUTHORS   Xu R, Cuebas DA.
  TITLE     The reactions catalyzed by the inducible bifunctional enzyme of rat
            liver peroxisomes cannot lead to the formation of bile acids.
  JOURNAL   Biochem. Biophys. Res. Commun. 221 (1996) 271-8.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Kinoshita, T., Miyata, M., Ismail, S.M., Fujimoto, Y., Kakinuma, K.,
            Kokawa, N.I. and Morisaki, M.
  TITLE     Synthesis and determination of stereochemistry of four
            diastereoisomers at the C-24 and C-25 positions of
            3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oic acid
            and cholic acid.
  JOURNAL   Chem. Pharm. Bull. 36 (1988) 134-141.
REFERENCE   4
  AUTHORS   Fujimoto, Y., Kinoshita, T., Oya, I., Kakinuma, K., Ismail, S.M.,
            Sonoda, Y., Sato, Y. and Morisaki, M.
  TITLE     Non-stereoselective conversion of the four diastereoisomers at the
            C-24 and C-25 positions of
            3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oic acid
            and cholic acid.
  JOURNAL   Chem. Pharm. Bull. 36 (1988) 142-145.
REFERENCE   5  [PMID:11146090]
  AUTHORS   Kurosawa T, Sato M, Nakano H, Fujiwara M, Murai T, Yoshimura T,
            Hashimoto T.
  TITLE     Conjugation reactions catalyzed by bifunctional proteins related to
            beta-oxidation in bile acid biosynthesis.
  JOURNAL   Steroids. 66 (2001) 107-14.
REFERENCE   6  [PMID:12543708]
  AUTHORS   Russell DW.
  TITLE     The enzymes, regulation, and genetics of bile acid synthesis.
  JOURNAL   Annu. Rev. Biochem. 72 (2003) 137-74.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K08078  3a,7a,12a-trihydroxy-5b-cholest-24-enoyl-CoA hydratase
GENES       HSA: 3295(HSD17B4)
            PTR: 462019(HSD17B4)
            MMU: 15488(Hsd17b4)
            RNO: 79244(Hsd17b4)
            CFA: 474630(HSD17B4)
            BTA: 493643(HSD17B4)
            SSC: 397574(HSD17B4)
            XLA: 444492(MGC81885)
            DRE: 393105(hsd17b4)
            SPU: 581580(LOC581580)
            DME: Dmel_CG3415
            TET: TTHERM_00317440
            SSE: Ssed_3224
            SPL: Spea_4033
            PLA: Plav_0490 Plav_1800
            RLE: pRL120747
            SWI: Swit_3404
            ACR: Acry_2580
            MAV: MAV_5146
            MSM: MSMEG_5943
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.107
            ExPASy - ENZYME nomenclature database: 4.2.1.107
            ExplorEnz - The Enzyme Database: 4.2.1.107
            ERGO genome analysis and discovery system: 4.2.1.107
            BRENDA, the Enzyme Database: 4.2.1.107
///
ENTRY       EC 4.2.1.108                Enzyme
NAME        ectoine synthase;
            N-acetyldiaminobutyrate dehydratase;
            N-acetyldiaminobutanoate dehydratase;
            L-ectoine synthase;
            EctC;
            4-N-acetyl-L-2,4-diaminobutanoate hydro-lyase (L-ectoine-forming)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     N4-acetyl-L-2,4-diaminobutanoate hydro-lyase (L-ectoine-forming)
REACTION    N4-acetyl-L-2,4-diaminobutanoate = L-ectoine + H2O [RN:R06979]
ALL_REAC    R06979
SUBSTRATE   N4-acetyl-L-2,4-diaminobutanoate
PRODUCT     L-ectoine [CPD:C06231];
            H2O [CPD:C00001]
COMMENT     Ectoine is an osmoprotectant that is found in halophilic eubacteria.
            This is the third enzyme in the ectoine-biosynthesis pathway, the
            other enzymes involved being EC 2.6.1.76,
            diaminobutyrate---2-oxoglutarate transaminase and EC 2.3.1.178,
            diaminobutyrate acetyltransferase [1,2].
REFERENCE   1
  AUTHORS   Peters, P., Galinski, E.A. and Truper, H.G.
  TITLE     The biosynthesis of ectoine.
  JOURNAL   FEMS Microbiol. Lett. 71 (1990) 157-162.
  ORGANISM  Ectothiorhodospira halochloris, Halomonas elongata
REFERENCE   2  [PMID:9864317]
  AUTHORS   Ono H, Sawada K, Khunajakr N, Tao T, Yamamoto M, Hiramoto M, Shinmyo
            A, Takano M, Murooka Y.
  TITLE     Characterization of biosynthetic enzymes for ectoine as a compatible
            solute in a moderately halophilic eubacterium, Halomonas elongata.
  JOURNAL   J. Bacteriol. 181 (1999) 91-9.
  ORGANISM  Halomonas elongata
REFERENCE   3  [PMID:11823218]
  AUTHORS   Kuhlmann AU, Bremer E.
  TITLE     Osmotically regulated synthesis of the compatible solute ectoine in
            Bacillus pasteurii and related Bacillus spp.
  JOURNAL   Appl. Environ. Microbiol. 68 (2002) 772-83.
  ORGANISM  Bacillus pasteurii, Bacillus spp.
REFERENCE   4  [PMID:9141677]
  AUTHORS   Louis P, Galinski EA.
  TITLE     Characterization of genes for the biosynthesis of the compatible
            solute ectoine from Marinococcus halophilus and osmoregulated
            expression in Escherichia coli.
  JOURNAL   Microbiology. 143 ( Pt 4) (1997) 1141-9.
  ORGANISM  Marinococcus halophilus
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K06720  L-ectoine synthase
GENES       VCH: VCA0823
            VPA: VP1720
            VFI: VFA1124
            PSB: Psyr_0334
            SDE: Sde_1191
            TCX: Tcr_0520
            NOC: Noc_1028
            AEH: Mlg_1190
            HCH: HCH_01508
            CSA: Csal_1878
            ABO: ABO_2152(ectC)
            BAM: Bamb_3987 Bamb_5030
            BPA: BPP1890(ectC)
            BBR: BB3218(ectC)
            WSU: WS0856
            RET: RHE_CH00924(ectC)
            RLE: RL3086
            BJA: blr2106(ectC)
            SIT: TM1040_0553
            RDE: RD1_3431(ectC)
            HNE: HNE_1641(estC)
            SAL: Sala_2951
            BHA: BH0918(ectC)
            BCL: ABC0336(ectC)
            OIH: OB0519
            MSM: MSMEG_3899(ectC)
            MMC: Mmcs_4192
            NFA: nfa27180(ectC)
            RHA: RHA1_ro01307(ectC)
            SCO: SCO1866(SCI39.13)
            SMA: SAV6396(ectC)
            TFU: Tfu_0302
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.108
            ExPASy - ENZYME nomenclature database: 4.2.1.108
            ExplorEnz - The Enzyme Database: 4.2.1.108
            ERGO genome analysis and discovery system: 4.2.1.108
            BRENDA, the Enzyme Database: 4.2.1.108
///
ENTRY       EC 4.2.1.109                Enzyme
NAME        methylthioribulose 1-phosphate dehydratase;
            1-PMT-ribulose dehydratase;
            S-methyl-5-thio-D-ribulose-1-phosphate hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     S-methyl-5-thio-D-ribulose-1-phosphate 4-hydro-lyase
            [5-(methylthio)-2,3-dioxopentyl-phosphate-forming]
REACTION    S-methyl-5-thio-D-ribulose 1-phosphate =
            5-(methylthio)-2,3-dioxopentyl phosphate + H2O [RN:R07392]
ALL_REAC    R07392
SUBSTRATE   S-methyl-5-thio-D-ribulose 1-phosphate [CPD:C04582]
PRODUCT     5-(methylthio)-2,3-dioxopentyl phosphate [CPD:C15650];
            H2O [CPD:C00001]
COMMENT     This enzyme forms part of the methionine-salvage pathway.
REFERENCE   1  [PMID:2838472]
  AUTHORS   Furfine ES, Abeles RH.
  TITLE     Intermediates in the conversion of 5'-S-methylthioadenosine to
            methionine in Klebsiella pneumoniae.
  JOURNAL   J. Biol. Chem. 263 (1988) 9598-606.
  ORGANISM  Klebsiella pneumoniae
REFERENCE   2  [PMID:7852397]
  AUTHORS   Wray JW, Abeles RH.
  TITLE     The methionine salvage pathway in Klebsiella pneumoniae and rat
            liver. Identification and characterization of two novel
            dioxygenases.
  JOURNAL   J. Biol. Chem. 270 (1995) 3147-53.
  ORGANISM  Klebsiella pneumoniae
PATHWAY     PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K08964  methylthioribulose-1-phosphate dehydratase
GENES       BSU: BG13284(mtnY)
            BAN: BA4257
            BAR: GBAA4257
            BAA: BA_4716
            BAT: BAS3948
            BCE: BC4038
            BCA: BCE_4105
            BCZ: BCZK3795
            BTK: BT9727_3780
            BLI: BL03541
            BLD: BLi01516(ykrY)
            GKA: GK0955
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.109
            ExPASy - ENZYME nomenclature database: 4.2.1.109
            ExplorEnz - The Enzyme Database: 4.2.1.109
            ERGO genome analysis and discovery system: 4.2.1.109
            BRENDA, the Enzyme Database: 4.2.1.109
///
ENTRY       EC 4.2.1.110                Enzyme
NAME        aldos-2-ulose dehydratase;
            pyranosone dehydratase;
            AUDH;
            1,5-anhydro-D-fructose dehydratase (microthecin-forming)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     1,5-anhydro-D-fructose hydro-lyase (microthecin-forming)
REACTION    (1) 1,5-anhydro-D-fructose =
            2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-on + H2O (overall
            reaction);
            (2) (1a) 1,5-anhydro-D-fructose =
            1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O;
            (3) (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose =
            2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one
SUBSTRATE   1,5-anhydro-D-fructose [CPD:C06485];
            1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose
PRODUCT     2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-on;
            H2O [CPD:C00001];
            1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose;
            2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one
COMMENT     This enzyme catalyses two of the steps in the anhydrofructose
            pathway, which leads to the degradation of glycogen and starch via
            1,5-anhydro-D-fructose [1,2]. The other enzymes involved in this
            pathway are EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase), EC
            4.2.2.13 [exo-(1->4)-alpha-D-glucan lyase] and EC 5.3.3.15
            (ascopyrone tautomerase). Aldose-2-uloses such as 2-dehydroglucose
            can also act as substrates, but more slowly [1,2,4]. This is a
            bifunctional enzyme that acts as both a lyase and as an isomerase
            [2]. Differs from EC 4.2.1.111, which can carry out only reaction
            (1a), is inhibited by its product and requires metal ions for
            activity [1].
REFERENCE   1  [PMID:16822618]
  AUTHORS   Yu S, Fiskesund R.
  TITLE     The anhydrofructose pathway and its possible role in stress response
            and signaling.
  JOURNAL   Biochim. Biophys. Acta. 1760 (2006) 1314-22.
REFERENCE   2  [PMID:15716041]
  AUTHORS   Yu S.
  TITLE     Enzymatic description of the anhydrofructose pathway of glycogen
            degradation II. Gene identification and characterization of the
            reactions catalyzed by aldos-2-ulose dehydratase that converts
            1,5-anhydro-D-fructose to microthecin with ascopyrone M as the
            intermediate.
  JOURNAL   Biochim. Biophys. Acta. 1723 (2005) 63-73.
REFERENCE   3
  AUTHORS   Broberg, A., Kenne, L. and Pedersen, M.
  TITLE     Presence of microthecin in the red alga Gracilariopsis lemaneiformis
            and its formation from 1,5-anhydro-D-fructose.
  JOURNAL   Phytochemistry 41 (1996) 151-154.
REFERENCE   4  [PMID:8352649]
  AUTHORS   Gabriel J, Volc J, Sedmera P, Daniel G, Kubatova E.
  TITLE     Pyranosone dehydratase from the basidiomycete Phanerochaete
            chrysosporium: improved purification, and identification of
            6-deoxy-D-glucosone and D-xylosone reaction products.
  JOURNAL   Arch. Microbiol. 160 (1993) 27-34.
REFERENCE   5  [PMID:15110094]
  AUTHORS   Yu S, Refdahl C, Lundt I.
  TITLE     Enzymatic description of the anhydrofructose pathway of glycogen
            degradation; I. Identification and purification of anhydrofructose
            dehydratase, ascopyrone tautomerase and alpha-1,4-glucan lyase in
            the fungus Anthracobia melaloma.
  JOURNAL   Biochim. Biophys. Acta. 1672 (2004) 120-9.
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.110
            ExPASy - ENZYME nomenclature database: 4.2.1.110
            ExplorEnz - The Enzyme Database: 4.2.1.110
            ERGO genome analysis and discovery system: 4.2.1.110
            BRENDA, the Enzyme Database: 4.2.1.110
///
ENTRY       EC 4.2.1.111                Enzyme
NAME        1,5-anhydro-D-fructose dehydratase;
            1,5-anhydro-D-fructose 4-dehydratase;
            1,5-anhydro-D-fructose hydrolyase;
            1,5-anhydro-D-arabino-hex-2-ulose dehydratase;
            AFDH;
            AF dehydratase;
            1,5-anhydro-D-fructose hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     1,5-anhydro-D-fructose hydro-lyase (ascopyrone-M-forming)
REACTION    1,5-anhydro-D-fructose =
            1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O
SUBSTRATE   1,5-anhydro-D-fructose [CPD:C06485]
PRODUCT     1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose;
            H2O [CPD:C00001]
COMMENT     This enzyme catalyses one of the steps in the anhydrofructose
            pathway, which leads to the degradation of glycogen and starch via
            1,5-anhydro-D-fructose [1,2]. The other enzymes involved in this
            pathway are EC 4.2.1.110 (aldos-2-ulose dehydratase), EC 4.2.2.13
            [exo-(1->4)-alpha-D-glucan lyase] and EC 5.3.3.15 (ascopyrone
            tautomerase). Requires divalent (Ca2+ or Mg2+) or monovalent cations
            (Na+) for optimal activity. Unlike EC 4.2.1.110, the enzyme is
            specific for 1,5-anhydro-D-fructose as substrate and shows no
            activity towards aldose-2-uloses such as 2-dehydroglucose [1,2,3].
            In addition, it is inhibited by its end-product ascopyrone M [2] and
            it cannot convert ascopyrone M into microthecin, as can EC
            4.2.1.110.
REFERENCE   1  [PMID:15110094]
  AUTHORS   Yu S, Refdahl C, Lundt I.
  TITLE     Enzymatic description of the anhydrofructose pathway of glycogen
            degradation; I. Identification and purification of anhydrofructose
            dehydratase, ascopyrone tautomerase and alpha-1,4-glucan lyase in
            the fungus Anthracobia melaloma.
  JOURNAL   Biochim. Biophys. Acta. 1672 (2004) 120-9.
REFERENCE   2  [PMID:16822618]
  AUTHORS   Yu S, Fiskesund R.
  TITLE     The anhydrofructose pathway and its possible role in stress response
            and signaling.
  JOURNAL   Biochim. Biophys. Acta. 1760 (2006) 1314-22.
REFERENCE   3  [PMID:15716041]
  AUTHORS   Yu S.
  TITLE     Enzymatic description of the anhydrofructose pathway of glycogen
            degradation II. Gene identification and characterization of the
            reactions catalyzed by aldos-2-ulose dehydratase that converts
            1,5-anhydro-D-fructose to microthecin with ascopyrone M as the
            intermediate.
  JOURNAL   Biochim. Biophys. Acta. 1723 (2005) 63-73.
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.111
            ExPASy - ENZYME nomenclature database: 4.2.1.111
            ExplorEnz - The Enzyme Database: 4.2.1.111
            ERGO genome analysis and discovery system: 4.2.1.111
            BRENDA, the Enzyme Database: 4.2.1.111
///
ENTRY       EC 4.2.1.112                Enzyme
NAME        acetylene hydratase;
            AH;
            acetaldehyde hydro-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
SYSNAME     acetaldehyde hydro-lyase (acetylene-forming)
REACTION    acetaldehyde = acetylene + H2O [RN:R05380]
ALL_REAC    R05380
SUBSTRATE   acetaldehyde [CPD:C00084]
PRODUCT     acetylene [CPD:C01548];
            H2O [CPD:C00001]
COMMENT     This is a non-redox-active enzyme that contains two molybdopterin
            guanine dinucleotide (MGD) cofactors, a tungsten centre and a cubane
            type [4Fe-4S] cluster [2].The tungsten centre binds a water molecule
            that is activated by an adjacent aspartate residue, enabling it to
            attack acetylene bound in a distinct hydrophobic pocket [2].
            Ethylene cannot act as a substrate [1].
REFERENCE   1  [PMID:7592321]
  AUTHORS   Rosner BM, Schink B.
  TITLE     Purification and characterization of acetylene hydratase of
            Pelobacter acetylenicus, a tungsten iron-sulfur protein.
  JOURNAL   J. Bacteriol. 177 (1995) 5767-72.
REFERENCE   2  [PMID:17360611]
  AUTHORS   Seiffert GB, Ullmann GM, Messerschmidt A, Schink B, Kroneck PM,
            Einsle O.
  TITLE     Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene
            hydratase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 3073-7.
PATHWAY     PATH: map00625  Tetrachloroethene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.1.112
            ExPASy - ENZYME nomenclature database: 4.2.1.112
            ExplorEnz - The Enzyme Database: 4.2.1.112
            ERGO genome analysis and discovery system: 4.2.1.112
            BRENDA, the Enzyme Database: 4.2.1.112
///
ENTRY       EC 4.2.1.-                  Enzyme
CLASS       Lyases;
            Carbon-oxygen lyases;
            Hydro-lyases
REACTION    (1) 3-Dehydroshikimate <=> 3,4-Dihydroxybenzoate + H2O [RN:R01627];
            (2) Homocystine + 2 Cyanide <=> alpha-Amino-gamma-cyanobutanoate +
            Homocysteine + Thiocyanate [RN:R03730];
            (3) 2-Aminomuconate + H2O <=> (Z)-5-Oxohex-2-enedioate + NH3
            [RN:R03887];
            (4) Glutaconyl-1-CoA + H2O <=> 2-Hydroxyglutaryl-CoA [RN:R03937];
            (5) 2-Succinylbenzoate + H2O <=>
            2-Succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate [RN:R04031];
            (6) 2-Oxohept-3-enedioate + H2O <=> 4-Hydroxy-2-oxo-heptanedioate
            [RN:R04131];
            (7) 2-Oxohept-3-enedioate + H2O <=> 2,4-Dihydroxyhept-2-enedioate
            [RN:R04132];
            (8) 4-Carboxy-4-hydroxy-2-oxoadipate <=>
            4-Carboxy-2-hydroxy-cis,cis-muconate + H2O [RN:R04399];
            (9) Parapyruvate <=> 4-Carboxy-2-oxo-4-pentanoate + H2O [RN:R04417];
            (10) 3alpha,7alpha-Dihydroxy-5beta-cholest-24-enoyl-CoA + H2O <=>
            3alpha,7alpha,24-Trihydroxy-5beta-cholestanoyl-CoA [RN:R04809];
            (11) 3alpha,7alpha,12alpha,24-Tetrahydroxy-5beta-cholestanoyl-CoA
            <=> 3alpha,7alpha,12alpha-Trihydroxy-5beta-cholest-24-enoyl-CoA +
            H2O [RN:R04813];
            (12) 2-Hydroxyhepta-2,4-dienedioate + H2O <=>
            4-Hydroxy-2-oxo-heptanedioate [RN:R04895];
            (13) Salicylaldehyde + Pyruvate <=>
            trans-O-Hydroxybenzylidenepyruvate [RN:R05136];
            (14) E-Phenylitaconyl-CoA + H2O <=>
            (Hydroxymethylphenyl)succinyl-CoA [RN:R05599];
            (15) Cyclohex-1-ene-1-carboxyl-CoA + H2O <=>
            2-Hydroxycyclohexane-1-carboxyl-CoA [RN:R05600];
            (16) 6-Carboxyhex-2-enoyl-CoA + H2O <=> 3-Hydroxypimeloyl-CoA
            [RN:R05601];
            (17) 6-Hydroxycyclohex-1-enecarbonyl-CoA + H2O <=>
            2,6-Dihydroxycyclohexane-1-carboxyl-CoA [RN:R05602];
            (18) Perillyl-CoA + H2O <=>
            2-Hydroxy-4-isopropenylcyclohexane-1-carboxyl-CoA [RN:R06369];
            (19) 2-Hydroxyhepta-2,4-dienedioate + H2O <=>
            2,4-Dihydroxyhept-2-enedioate [RN:R06897];
            (20) Naphthyl-2-methylene-succinyl-CoA + H2O <=>
            Naphthyl-2-hydroxymethyl-succinyl CoA [RN:R06906];
            (21) 2-Hydroxy-3-methylbenzalpyruvate + H2O <=>
            3-Methylsalicylaldehyde + Pyruvate [RN:R06913];
            (22) 2-Hydroxy-3-carboxybenzalpyruvate + H2O <=> 3-Formylsalicylic
            acid + Pyruvate [RN:R06923];
            (23) 2-Hydroxy-4-hydroxymethylbenzalpyruvate + H2O <=>
            4-Hydroxymethylsalicylaldehyde + Pyruvate [RN:R06934];
            (24) 3-Hydroxyoctadecanoyl-CoA <=> (2E)-Octadecenoyl-CoA + H2O
            [RN:R07760];
            (25) 3-Hydroxyoctadecanoyl-[acp] <=> (2E)-Octadecenoyl-[acp] + H2O
            [RN:R07764];
            (26)
            (6Z,9Z,12Z,15Z,18Z,21Z)-3-Hydroxytetracosahexa-6,9,12,15,18,21-
            enoyl-CoA <=>
            (2E,6Z,9Z,12Z,15Z,18Z,21Z)-Tetracosahepta-2,6,9,12,15,18,21-enoyl-
            CoA + H2O [RN:R07935];
            (27)
            (6Z,9Z,12Z,15Z,18Z)-3-Hydroxytetracosapenta-6,9,12,15,18-enoyl-CoA
            <=> (2E,6Z,9Z,12Z,15Z,18Z)-Tetracosahexa-2,6,9,12,15,18-enoyl-CoA +
            H2O [RN:R07951]
SUBSTRATE   Homocystine [CPD:C01817];
            Cyanide [CPD:C00177];
            2-Aminomuconate [CPD:C02220];
            H2O [CPD:C00001];
            Glutaconyl-1-CoA [CPD:C02411];
            2-Succinylbenzoate [CPD:C02730];
            2-Oxohept-3-enedioate [CPD:C03063];
            4-Carboxy-4-hydroxy-2-oxoadipate [CPD:C04115];
            Parapyruvate [CPD:C06033];
            3alpha,7alpha-Dihydroxy-5beta-cholest-24-enoyl-CoA [CPD:C05447];
            3alpha,7alpha,12alpha,24-Tetrahydroxy-5beta-cholestanoyl-CoA
            [CPD:C05450];
            2-Hydroxyhepta-2,4-dienedioate [CPD:C05600];
            Salicylaldehyde [CPD:C06202];
            Pyruvate [CPD:C00022];
            Acetaldehyde [CPD:C00084];
            E-Phenylitaconyl-CoA [CPD:C09818];
            Cyclohex-1-ene-1-carboxyl-CoA [CPD:C09811];
            6-Carboxyhex-2-enoyl-CoA [CPD:C06723];
            6-Hydroxycyclohex-1-enecarbonyl-CoA [CPD:C06749];
            Perillyl-CoA [CPD:C11929];
            Naphthyl-2-methylene-succinyl-CoA [CPD:C14117];
            2-Hydroxy-3-methylbenzalpyruvate [CPD:C14086];
            2-Hydroxy-3-carboxybenzalpyruvate [CPD:C14095];
            2-Hydroxy-4-hydroxymethylbenzalpyruvate [CPD:C14107]
PRODUCT     alpha-Amino-gamma-cyanobutanoate [CPD:C05717];
            Homocysteine [CPD:C05330];
            Thiocyanate [CPD:C01755];
            (Z)-5-Oxohex-2-enedioate [CPD:C03453];
            NH3 [CPD:C00014];
            2-Hydroxyglutaryl-CoA [CPD:C03058];
            2-Succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate [CPD:C05817];
            4-Hydroxy-2-oxo-heptanedioate [CPD:C05601];
            2,4-Dihydroxyhept-2-enedioate [CPD:C06201];
            4-Carboxy-2-hydroxy-cis,cis-muconate [CPD:C04324];
            H2O [CPD:C00001];
            4-Carboxy-2-oxo-4-pentanoate [CPD:C05854];
            3alpha,7alpha,24-Trihydroxy-5beta-cholestanoyl-CoA [CPD:C05448];
            3alpha,7alpha,12alpha-Trihydroxy-5beta-cholest-24-enoyl-CoA
            [CPD:C05460];
            trans-O-Hydroxybenzylidenepyruvate [CPD:C06203];
            Acetylene [CPD:C01548];
            (Hydroxymethylphenyl)succinyl-CoA [CPD:C09819];
            2-Hydroxycyclohexane-1-carboxyl-CoA [CPD:C09812];
            3-Hydroxypimeloyl-CoA [CPD:C06714];
            2,6-Dihydroxycyclohexane-1-carboxyl-CoA [CPD:C09824];
            2-Hydroxy-4-isopropenylcyclohexane-1-carboxyl-CoA [CPD:C11934];
            Naphthyl-2-hydroxymethyl-succinyl CoA [CPD:C14118];
            3-Methylsalicylaldehyde [CPD:C14087];
            Pyruvate [CPD:C00022];
            3-Formylsalicylic acid [CPD:C14096];
            4-Hydroxymethylsalicylaldehyde [CPD:C14108]
///
ENTRY       EC 4.2.2.1                  Enzyme
NAME        hyaluronate lyase;
            hyaluronidase [but cf. internal_xref(ec_num(3,2,1,35))
            (hyalurononglucosaminidase) and internal_xref(ec_num(3,2,1,36))
            (hyaluronoglucuronidase)];
            glucuronoglycosaminoglycan lyase;
            spreading factor;
            mucinase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     hyaluronate lyase
REACTION    Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA
            bond, ultimately breaking the polysaccharide down to
            3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
            [RN:R02465 R06242]
ALL_REAC    R02465 R06242(G)
COMMENT     Also acts on chondroitin. The product is more systematically known
            as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic
            acid)-2-acetamido-2-deoxy-D-glucose
REFERENCE   1
  AUTHORS   Linker, A., Hoffman, P., Meyer, K., Sampson, P. and Korn, E.D.
  TITLE     The formation of unsaturated disacharides from mucopoly-saccharides
            and their cleavage to alpha-keto acid by bacterial enzymes.
  JOURNAL   J. Biol. Chem. 235 (1960) 3061.
REFERENCE   2  [PMID:14943668]
  AUTHORS   MEYER K, RAPPORT MM.
  TITLE     Hyaluronidases.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 13 (1952) 199-236.
REFERENCE   3  [PMID:5642600]
  AUTHORS   Moran F, Nasuno S, Starr MP.
  TITLE     Extracellular and intracellular polygllacturonic acid
            trans-eliminases of Erwinia carotovora.
  JOURNAL   Arch. Biochem. Biophys. 123 (1968) 298-306.
  ORGANISM  Erwinia carotovora [GN:eca]
ORTHOLOGY   KO: K01727  
GENES       VFI: VFA0994
            SAU: SA2003(hysA)
            SAV: SAV2202(hysA)
            SAM: MW2129(hysA)
            SAR: SAR1892(hysA1) SAR2292(hysA2)
            SAS: SAS2103
            SAC: SACOL2194(hysA)
            SAB: SAB1663(hysA1) SAB2082(hysA2)
            SAA: SAUSA300_2161(hysA)
            SAO: SAOUHSC_02463
            SPY: SPy_1032(hylA)
            SPZ: M5005_Spy_0757(hylA)
            SPH: MGAS10270_Spy0874(hylA)
            SPI: MGAS10750_Spy0909(hylA)
            SPJ: MGAS2096_Spy0830(hylA) MGAS2096_Spy0831
            SPK: MGAS9429_Spy0871(hylA)
            SPA: M6_Spy0782
            SPB: M28_Spy0736(hylA)
            SPN: SP_0314
            SPR: spr0286(hysA)
            SPD: SPD_0287
            SAG: SAG1197
            SAN: gbs1270
            SAK: SAK_1284(hylB)
            ART: Arth_1698
            PAC: PPA0380
STRUCTURES  PDB: 1C82  1EGU  1F1S  1F9G  1I8Q  1LOH  1LXK  1LXM  1N7N  1N7O  
                 1N7P  1N7Q  1N7R  1OJM  1OJN  1OJO  1OJP  1W3Y  2BRP  2BRV  
                 2BRW  2C3F  2DP5  2PK1  2YVV  2YW0  2YX2  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.1
            ExPASy - ENZYME nomenclature database: 4.2.2.1
            ExplorEnz - The Enzyme Database: 4.2.2.1
            ERGO genome analysis and discovery system: 4.2.2.1
            BRENDA, the Enzyme Database: 4.2.2.1
            CAS: 37259-53-3
///
ENTRY       EC 4.2.2.2                  Enzyme
NAME        pectate lyase;
            polygalacturonic transeliminase;
            pectic acid transeliminase;
            polygalacturonate lyase;
            endopectin methyltranseliminase;
            pectate transeliminase;
            endogalacturonate transeliminase;
            pectic acid lyase;
            pectic lyase;
            alpha-1,4-D-endopolygalacturonic acid lyase;
            PGA lyase;
            PPase-N;
            endo-alpha-1,4-polygalacturonic acid lyase;
            polygalacturonic acid lyase;
            pectin trans-eliminase;
            Polygalacturonic acid trans-eliminase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     (1->4)-alpha-D-galacturonan lyase
REACTION    Eliminative cleavage of (1->4)-alpha-D-galacturonan to give
            oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at
            their non-reducing ends [RN:R02361 R06240]
ALL_REAC    R02361 R06240(G)
COMMENT     Favours pectate, the anion, over pectin, the methyl ester (which is
            the preferred substrate of EC 4.2.2.10, pectin lyase).
REFERENCE   1  [PMID:13860094]
  AUTHORS   ALBERSHEIM P, KILLIAS U.
  TITLE     Studies relating to the purification and properties of pectin
            transeliminase.
  JOURNAL   Arch. Biochem. Biophys. 97 (1962) 107-15.
REFERENCE   2  [PMID:14235514]
  AUTHORS   EDSTROM RD, PHAFF HJ.
  TITLE     PURIFICATION AND CERTAIN PROPERTIES OF PECTIN TRANS-ELIMINASE FROM
            ASPERGILLUS FONSECAEUS.
  JOURNAL   J. Biol. Chem. 239 (1964) 2403-8.
  ORGANISM  Aspergillus fonsecaeus
REFERENCE   3  [PMID:14235515]
  AUTHORS   EDSTROM RD, PHAFF HJ.
  TITLE     ELIMINATIVE CLEAVAGE OF PECTIN AND OF OLIGOGALACTURONIDE METHYL
            ESTERS BY PECTIN TRANS-ELIMINASE.
  JOURNAL   J. Biol. Chem. 239 (1964) 2409-15.
  ORGANISM  Aspergillus fonsecaeus
REFERENCE   4
  AUTHORS   Nagel, C.W. and Vaughn, R.H.
  TITLE     The degradation of oligogalacturonides by the polygalacturonase of
            Bacillus polymyxa.
  JOURNAL   Arch. Biochem. Biophys. 94 (1961) 328.
  ORGANISM  Bacillus polymyxa
REFERENCE   5  [PMID:6035509]
  AUTHORS   Nasuno S, Starr MP.
  TITLE     Polygalacturonic acid trans-eliminase of Xanthomonas campestris.
  JOURNAL   Biochem. J. 104 (1967) 178-85.
  ORGANISM  Xanthomonas campestris
REFERENCE   6  [PMID:9195887]
  AUTHORS   Mayans O, Scott M, Connerton I, Gravesen T, Benen J, Visser J,
            Pickersgill R, Jenkins J.
  TITLE     Two crystal structures of pectin lyase A from Aspergillus reveal a
            pH driven conformational change and striking divergence in the
            substrate-binding clefts of pectin and pectate lyases.
  JOURNAL   Structure. 5 (1997) 677-89.
  ORGANISM  Aspergillus niger
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K01728  pectate lyase
GENES       ATH: AT2G02720 AT4G13210 AT4G13710 AT4G22090 AT5G55720
            OSA: 4326883 4335013
            AFM: AFUA_1G01120 AFUA_2G00760 AFUA_7G06400 AFUA_8G05910
            ANG: An10g00870(plyA)
            YPE: YPO3994(pelY)
            YPK: y3834
            YPM: YP_3357(pelY)
            YPA: YPA_3822
            YPN: YPN_3644
            YPS: YPTB3834(pelY)
            ECA: ECA2135 ECA4067(pelA) ECA4068(pelB) ECA4069(pelC)
                 ECA4070(pelZ)
            ENT: Ent638_0482
            XCC: XCC0644(pel) XCC0645(pel) XCC2815(pelB)
            XCB: XC_1298 XC_3590 XC_3591
            XCV: XCV2278 XCV2569 XCV3132(pel1) XCV3687(pel2)
            XAC: XAC2373(pel) XAC2986(pelB) XAC3562(pel)
            XOO: XOO0821(pel) XOO2265
            XOM: XOO_0747(XOO0747)
            MMW: Mmwyl1_2362
            SME: SMb21239
            SMD: Smed_6139
            BSU: BG10840(pel)
            BHA: BH0698
            BLI: BL03760(pelI)
            BLD: BLi01404(pel)
            BCL: ABC0063(pelB) ABC1141
            BAY: RBAM_007720
            BPU: BPUM_3515
            SCO: SCO1880(SCI39.27c)
            TFU: Tfu_0153
            RBA: RB3417 RB5312(pel) RB5316
            TMA: TM0433
STRUCTURES  PDB: 1AIR  1BN8  1EE6  1GXM  1GXN  1GXO  1JRG  1JTA  1O88  1O8D  
                 1O8E  1O8F  1O8G  1O8H  1O8I  1O8J  1O8K  1O8L  1O8M  1OOC  
                 1PCL  1PE9  1PLU  1R76  1RU4  1VBL  2BSP  2EWE  2PEC  2V8I  
                 2V8J  2V8K  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.2
            ExPASy - ENZYME nomenclature database: 4.2.2.2
            ExplorEnz - The Enzyme Database: 4.2.2.2
            ERGO genome analysis and discovery system: 4.2.2.2
            BRENDA, the Enzyme Database: 4.2.2.2
            CAS: 9015-75-2
///
ENTRY       EC 4.2.2.3                  Enzyme
NAME        poly(beta-D-mannuronate) lyase;
            alginate lyase I;
            alginate lyase;
            alginase I;
            alginase II;
            alginase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     poly(beta-D-1,4-mannuronide) lyase
REACTION    Eliminative cleavage of polysaccharides containing
            beta-D-mannuronate residues to give oligosaccharides with
            4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their ends
ALL_REAC    (other) R03706
REFERENCE   1  [PMID:13144]
  AUTHORS   Davidson IW, Lawson CJ, Sutherland IW.
  TITLE     An alginate lysate from Azotobacter vinelandii phage.
  JOURNAL   J. Gen. Microbiol. 98 (1977) 223-9.
  ORGANISM  Azotobacter vinelandii
REFERENCE   2  [PMID:6020438]
  AUTHORS   Nakada HI, Sweeny PC.
  TITLE     Alginic acid degradation by eliminases from abalone hepatopancreas.
  JOURNAL   J. Biol. Chem. 242 (1967) 845-51.
  ORGANISM  Pseudomonas sp.
REFERENCE   3
  AUTHORS   Preiss, J. and Ashwell, G.
  TITLE     Alginic acid metabolism in bacteria. I. Enzymatic formation of
            unsaturated oligosaccharides and 4-deoxy-L-erythro-5-hexoseulose
            uronic acid.
  JOURNAL   J. Biol. Chem. 237 (1962) 309-316.
  ORGANISM  Macrocystis pyrifera
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K01729  poly(beta-D-mannuronate) lyase
GENES       ENT: Ent638_2038
            PAE: PA3547(algL)
            PAU: PA14_18470(algL)
            PPU: PP_1281(algL)
            PPF: Pput_4444
            PST: PSPTO_1236(algL)
            PSB: Psyr_1056(algL)
            PSP: PSPPH_1111(algL)
            PFL: PFL_1017(algL)
            PFO: Pfl_0953(algL)
            PEN: PSEEN3462 PSEEN4542(algL)
            PMY: Pmen_1024
            SFR: Sfri_3103
            PHA: PSHAa0571 PSHAa1749
            PAT: Patl_3639 Patl_3640 Patl_3659
            SDE: Sde_2478 Sde_2547 Sde_2839 Sde_2873 Sde_3274 Sde_3275
                 Sde_3285 Sde_3286
            ABO: ABO_0393(algL)
            BUR: Bcep18194_C7175
            MMR: Mmar10_0255
            RBA: RB3601
STRUCTURES  PDB: 1HV6  1J1T  2CWS  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.3
            ExPASy - ENZYME nomenclature database: 4.2.2.3
            ExplorEnz - The Enzyme Database: 4.2.2.3
            ERGO genome analysis and discovery system: 4.2.2.3
            BRENDA, the Enzyme Database: 4.2.2.3
            CAS: 9024-15-1
///
ENTRY       EC 4.2.2.4        Obsolete  Enzyme
NAME        Transferred to 4.2.2.20 and 4.2.2.21
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
COMMENT     Transferred entry: chondroitin ABC lyase. Now known to comprise two
            enzymes: EC 4.2.2.20, chondroitin-sulfate-ABC endolyase and EC
            4.2.2.21, chondroitin-sulfate-ABC exolyase. (EC 4.2.2.4 created 1972
            (EC 4.2.99.6 created 1965, part incorporated 1976), deleted 2006)
STRUCTURES  PDB: 1HN0  1OFL  1OFM  1RW9  1RWA  1RWC  1RWF  1RWG  1RWH  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.4
            ExPASy - ENZYME nomenclature database: 4.2.2.4
            ExplorEnz - The Enzyme Database: 4.2.2.4
            ERGO genome analysis and discovery system: 4.2.2.4
            BRENDA, the Enzyme Database: 4.2.2.4
///
ENTRY       EC 4.2.2.5                  Enzyme
NAME        chondroitin AC lyase;
            chondroitinase (ambiguous);
            chondroitin sulfate lyase;
            chondroitin AC eliminase;
            chondroitin AC lyase;
            chondroitinase AC;
            ChnAC
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     chondroitin AC lyase
REACTION    Eliminative degradation of polysaccharides containing
            1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to
            disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups
COMMENT     Acts on chondroitin 4-sulfate and chondroitin 6-sulfate, but less
            well on hyaluronate. In general, chondroitin sulfate (CS) and
            dermatan sulfate (DS) chains comprise a linkage region, a chain cap
            and a repeat region. The repeat region of CS is a repeating
            disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine
            (GalNAc) [-4)GlcA(beta1-3)GalNAc(beta1-]n, which may be O-sulfated
            on the C-4 and/or C-6 of GalNAc and C-2 of GlcA. GlcA residues of CS
            may be epimerized to iduronic acid (IdoA) forming the repeating
            disaccharide [-4)IdoA(alpha1-3)GalNAc(beta1-]n of DS. Both the
            concentrations and locations of sulfate-ester substituents vary with
            glucosaminoglycan source [4].
REFERENCE   1  [PMID:13727579]
  AUTHORS   NAKADA HI, WOLFE JB.
  TITLE     Studies on the enzyme chondroitinase: product structure and ion
            effects.
  JOURNAL   Arch. Biochem. Biophys. 94 (1961) 244-51.
  ORGANISM  Proteus vulgaris
REFERENCE   2  [PMID:11500043]
  AUTHORS   Pojasek K, Shriver Z, Kiley P, Venkataraman G, Sasisekharan R.
  TITLE     Recombinant expression, purification, and kinetic characterization
            of chondroitinase AC and chondroitinase B from Flavobacterium
            heparinum.
  JOURNAL   Biochem. Biophys. Res. Commun. 286 (2001) 343-51.
  ORGANISM  Flavobacterium heparinum
REFERENCE   3  [PMID:9761894]
  AUTHORS   Fethiere J, Shilton BH, Li Y, Allaire M, Laliberte M, Eggimann B,
            Cygler M.
  TITLE     Crystallization and preliminary analysis of chondroitinase AC from
            Flavobacterium heparinum.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 54 ( Pt 2) (1998) 279-80.
  ORGANISM  Flavobacterium heparinum
REFERENCE   4  [PMID:16336265]
  AUTHORS   Huckerby TN, Nieduszynski IA, Giannopoulos M, Weeks SD, Sadler IH,
            Lauder RM.
  TITLE     Characterization of oligosaccharides from the chondroitin/dermatan
            sulfates. 1H-NMR and 13C-NMR studies of reduced trisaccharides and
            hexasaccharides.
  JOURNAL   FEBS. J. 272 (2005) 6276-86.
GENES       BTH: BT_2964
STRUCTURES  PDB: 1CB8  1HM2  1HM3  1HMU  1HMW  1RW9  1RWA  1RWC  1RWF  1RWG  
                 1RWH  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.5
            ExPASy - ENZYME nomenclature database: 4.2.2.5
            ExplorEnz - The Enzyme Database: 4.2.2.5
            ERGO genome analysis and discovery system: 4.2.2.5
            BRENDA, the Enzyme Database: 4.2.2.5
            CAS: 9047-57-8
///
ENTRY       EC 4.2.2.6                  Enzyme
NAME        oligogalacturonide lyase;
            oligogalacturonate lyase;
            unsaturated oligogalacturonate transeliminase;
            OGTE
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     oligogalacturonide lyase
REACTION    4-(4-deoxy-beta-D-gluc-4-enuronosyl)-D-galacturonate = 2
            5-dehydro-4-deoxy-D-glucuronate [RN:R00064 R06252]
ALL_REAC    R00064 R06252(G);
            (other) R04382 R06249(G)
SUBSTRATE   4-(4-deoxy-beta-D-gluc-4-enuronosyl)-D-galacturonate [CPD:C04733]
PRODUCT     5-dehydro-4-deoxy-D-glucuronate [CPD:C04053]
COMMENT     Also catalyses eliminative removal of unsaturated terminal residues
            from oligosaccharides of D-galacturonate.
REFERENCE   1  [PMID:5671040]
  AUTHORS   Moran F, Nasuno S, Starr MP.
  TITLE     Oligogalacturonide trans-eliminase of Erwinia carotovora.
  JOURNAL   Arch. Biochem. Biophys. 125 (1968) 734-41.
  ORGANISM  Erwinia carotovora [GN:eca]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K01730  oligogalacturonide lyase
GENES       YPE: YPO1713(ogl)
            YPK: y1875(ogl)
            YPM: YP_1738(ogl)
            YPA: YPA_1808
            YPN: YPN_1917
            YPP: YPDSF_1735
            YPS: YPTB2368(ogl)
            YPI: YpsIP31758_1682(ogl)
            ECA: ECA2426(ogl)
            ENT: Ent638_3293 Ent638_3297
            ASU: Asuc_1467
            MMW: Mmwyl1_0773
            RCA: Rcas_2370
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.6
            ExPASy - ENZYME nomenclature database: 4.2.2.6
            ExplorEnz - The Enzyme Database: 4.2.2.6
            ERGO genome analysis and discovery system: 4.2.2.6
            BRENDA, the Enzyme Database: 4.2.2.6
            CAS: 9031-33-8
///
ENTRY       EC 4.2.2.7                  Enzyme
NAME        heparin lyase;
            heparin eliminase;
            heparinase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     heparin lyase
REACTION    Eliminative cleavage of polysaccharides containing 1,4-linked
            D-glucuronate or L-iduronate residues and 1,4-alpha-linked
            2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give
            oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl
            groups at their non-reducing ends
REFERENCE   1  [PMID:5484472]
  AUTHORS   Hovingh P, Linker A.
  TITLE     The enzymatic degradation of heparin and heparitin sulfate. 3.
            Purification of a heparitinase and a heparinase from flavobacteria.
  JOURNAL   J. Biol. Chem. 245 (1970) 6170-5.
  ORGANISM  Flavobacterium heparinum
GENES       BTH: BT_4675
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.7
            ExPASy - ENZYME nomenclature database: 4.2.2.7
            ExplorEnz - The Enzyme Database: 4.2.2.7
            ERGO genome analysis and discovery system: 4.2.2.7
            BRENDA, the Enzyme Database: 4.2.2.7
            CAS: 9025-39-2
///
ENTRY       EC 4.2.2.8                  Enzyme
NAME        heparin-sulfate lyase;
            heparin-sulfate eliminase;
            heparitin-sulfate lyase;
            heparitinase I;
            heparitinase II
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     heparin-sulfate lyase
REACTION    Elimination of sulfate; appears to act on linkages between
            N-acetyl-D-glucosamine and uronate. Product is an unsaturated sugar.
COMMENT     Does not act on N,O-desulfated glucosamine or N-acetyl-O-sulfated
            glucosamine linkages.
REFERENCE   1  [PMID:5484472]
  AUTHORS   Hovingh P, Linker A.
  TITLE     The enzymatic degradation of heparin and heparitin sulfate. 3.
            Purification of a heparitinase and a heparinase from flavobacteria.
  JOURNAL   J. Biol. Chem. 245 (1970) 6170-5.
  ORGANISM  Flavobacterium heparinum
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.8
            ExPASy - ENZYME nomenclature database: 4.2.2.8
            ExplorEnz - The Enzyme Database: 4.2.2.8
            ERGO genome analysis and discovery system: 4.2.2.8
            BRENDA, the Enzyme Database: 4.2.2.8
            CAS: 37290-86-1
///
ENTRY       EC 4.2.2.9                  Enzyme
NAME        pectate disaccharide-lyase;
            pectate exo-lyase;
            exopectic acid transeliminase;
            exopectate lyase;
            exopolygalacturonic acid-trans-eliminase;
            PATE;
            exo-PATE;
            exo-PGL
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     (1->4)-alpha-D-galacturonan reducing-end-disaccharide-lyase
REACTION    Eliminative cleavage of
            4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate from the
            reducing end of pectate, i.e. de-esterified pectin
REFERENCE   1
  AUTHORS   Macmillan, J.D. and Vaughn, R.H.
  TITLE     Purification and properties of a polygalacturonic
            acid-trans-eliminase produced by Clostridium multifermentans.
  JOURNAL   Biochemistry 3 (1964) 564-572.
  ORGANISM  Clostridium multifermentans
ORTHOLOGY   KO: K01731  
GENES       YPE: YPO1723(pelW)
            YPM: YP_1748(pelW)
            YPA: YPA_1798
            YPN: YPN_1907
            YPP: YPDSF_1725
            YPS: YPTB2358(pelW)
            ECA: ECA2402(pelW) ECA4510(pelX)
            ENT: Ent638_4134
            BHA: BH0494(pelX)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.9
            ExPASy - ENZYME nomenclature database: 4.2.2.9
            ExplorEnz - The Enzyme Database: 4.2.2.9
            ERGO genome analysis and discovery system: 4.2.2.9
            BRENDA, the Enzyme Database: 4.2.2.9
            CAS: 37290-87-2
///
ENTRY       EC 4.2.2.10                 Enzyme
NAME        pectin lyase;
            pectin trans-eliminase;
            endo-pectin lyase;
            polymethylgalacturonic transeliminase;
            pectin methyltranseliminase;
            pectolyase;
            PL;
            PNL;
            PMGL
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     (1->4)-6-O-methyl-alpha-D-galacturonan lyase
REACTION    Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl ester to
            give oligosaccharides with
            4-deoxy-6-O-methyl-alpha-D-galact-4-enuronosyl groups at their
            non-reducing ends
COMMENT     Favours pectin, the methyl ester, over pectate, the anion (which is
            the preferred substrate of EC 4.2.2.2, pectate lyase). Demethylation
            progressively slows its action; it can nevertheless cleave on either
            side of a demethylated residue if the residue at the other end of
            the scissile bond is methylated.
REFERENCE   1
  AUTHORS   Albersheim, P., Neukom, H. and Deuel, H.
  TITLE     Uber die Bildung von ungesattigten Abbauprodukten durch ein
            pekinabbauendes Enzym.
  JOURNAL   Helv. Chim. Acta 43 (1960) 1422-1426.
REFERENCE   2  [PMID:9195887]
  AUTHORS   Mayans O, Scott M, Connerton I, Gravesen T, Benen J, Visser J,
            Pickersgill R, Jenkins J.
  TITLE     Two crystal structures of pectin lyase A from Aspergillus reveal a
            pH driven conformational change and striking divergence in the
            substrate-binding clefts of pectin and pectate lyases.
  JOURNAL   Structure. 5 (1997) 677-89.
  ORGANISM  Aspergillus niger
REFERENCE   3
  AUTHORS   Kester, H.C.M and Visser, J.
  TITLE     Purification and characterization of pectin lyase B, a novel
            pectinolytic enzyme from Aspergillus niger.
  JOURNAL   FEMS Microbiol. Lett. 120 (1994) 63-68.
  ORGANISM  Aspergillus niger
REFERENCE   4  [PMID:12110197]
  AUTHORS   Mutenda KE, Korner R, Christensen TM, Mikkelsen J, Roepstorff P.
  TITLE     Application of mass spectrometry to determine the activity and
            specificity of pectin lyase A.
  JOURNAL   Carbohydr. Res. 337 (2002) 1217-27.
  ORGANISM  Aspergillus niger
ORTHOLOGY   KO: K01732  
GENES       AFM: AFUA_2G00800 AFUA_5G10380 AFUA_7G05030
            ANG: An03g00190(pelB) An14g04370(pelA) An19g00270(pelD)
            ECA: ECA1499(pnl)
            PSP: PSPPH_1424(hopAK1) PSPPH_3992(pnlA)
            BSU: BG12643(pelB)
            BAY: RBAM_036320
STRUCTURES  PDB: 1IDJ  1IDK  1QCX  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.10
            ExPASy - ENZYME nomenclature database: 4.2.2.10
            ExplorEnz - The Enzyme Database: 4.2.2.10
            ERGO genome analysis and discovery system: 4.2.2.10
            BRENDA, the Enzyme Database: 4.2.2.10
            CAS: 9033-35-6
///
ENTRY       EC 4.2.2.11                 Enzyme
NAME        poly(alpha-L-guluronate) lyase;
            alginase II;
            guluronate lyase;
            L-guluronan lyase;
            L-guluronate lyase;
            poly-alpha-L-guluronate lyase;
            polyguluronate-specific alginate lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     poly(alpha-L-1,4-guluronide) exo-lyase
REACTION    Eliminative cleavage of polysaccharides containing a terminal
            alpha-L-guluronate group, to give oligosaccharides with
            4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their
            non-reducing ends
REFERENCE   1  [PMID:332364]
  AUTHORS   Boyd J, Turvey JR.
  TITLE     Isolation of poly-alpha-L-guluronate lyase from Klebsiella
            aerogenes.
  JOURNAL   Carbohydr. Res. 57 (1977) 163-71.
  ORGANISM  Klebsiella aerogenes
REFERENCE   2  [PMID:1008828]
  AUTHORS   Davidson IW, Sutherland IW, Lawson CJ.
  TITLE     Purification and properties of an alginate lyase from a marine
            bacterium.
  JOURNAL   Biochem. J. 159 (1976) 707-13.
STRUCTURES  PDB: 1UAI  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.11
            ExPASy - ENZYME nomenclature database: 4.2.2.11
            ExplorEnz - The Enzyme Database: 4.2.2.11
            ERGO genome analysis and discovery system: 4.2.2.11
            BRENDA, the Enzyme Database: 4.2.2.11
            CAS: 64177-88-4
///
ENTRY       EC 4.2.2.12                 Enzyme
NAME        xanthan lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     xanthan lyase
REACTION    Eliminative cleavage of the terminal
            beta-D-mannosyl-beta-D-1,4-glucuronosyl linkage of the side-chain of
            the polysaccharide xanthan, leaving a
            4-deoxy-alpha-L-threo-hex-4-enuronosyl group at the terminus of the
            side-chain
REFERENCE   1  [PMID:3446747]
  AUTHORS   Sutherland IW.
  TITLE     Xanthan lyases--novel enzymes found in various bacterial species.
  JOURNAL   J. Gen. Microbiol. 133 (1987) 3129-34.
  ORGANISM  Xanthomonas campestris, Bacillus sp., Corynebacterium sp.
GENES       BCZ: pE33L466_0352(xalA)
STRUCTURES  PDB: 1J0M  1J0N  1X1H  1X1I  1X1J  2E22  2E24  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.12
            ExPASy - ENZYME nomenclature database: 4.2.2.12
            ExplorEnz - The Enzyme Database: 4.2.2.12
            ERGO genome analysis and discovery system: 4.2.2.12
            BRENDA, the Enzyme Database: 4.2.2.12
            CAS: 113573-69-6
///
ENTRY       EC 4.2.2.13                 Enzyme
NAME        exo-(1->4)-alpha-D-glucan lyase;
            alpha-(1->4)-glucan 1,5-anhydro-D-fructose eliminase;
            alpha-1,4-glucan exo-lyase;
            alpha-1,4-glucan lyase;
            GLase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     (1->4)-alpha-D-glucan exo-4-lyase (1,5-anhydro-D-fructose-forming)
REACTION    linear alpha-glucan = (n-1) 1,5-anhydro-D-fructose + D-glucose
SUBSTRATE   linear alpha-glucan
PRODUCT     (n-1) 1,5-anhydro-D-fructose;
            D-glucose [CPD:C00031]
COMMENT     The enzyme catalyses the sequential degradation of
            (1->4)-alpha-D-glucans from the non-reducing end with the release of
            1,5-anhydro-D-fructose. Thus, for an alpha-glucan containing n
            (1->4)-linked glucose units, the final products are 1 glucose plus
            (n-1) 1,5-anhydro-D-fructose. Maltose, maltosaccharides and amylose
            are all completely degraded. It does not degrade
            (1->6)-alpha-glucosidic bonds and thus the degradation of a branched
            glucan, such as amylopectin or glycogen, will result in the
            formation of 1,5-anhydro-D-fructose plus a limit dextrin. Other
            enzymes involved in the anhydrofructose pathway are EC 4.2.1.110
            (aldos-2-ulose dehydratase), EC 4.2.1.111 (1,5-anhydro-D-fructose
            dehydratase) and EC 5.3.3.15 (ascopyrone tautomerase).
REFERENCE   1  [PMID:8461323]
  AUTHORS   Yu S, Kenne L, Pedersen M.
  TITLE     Alpha-1,4-glucan lyase, a new class of starch/glycogen degrading
            enzyme. I. Efficient purification and characterization from red
            seaweeds.
  JOURNAL   Biochim. Biophys. Acta. 1156 (1993) 313-20.
  ORGANISM  Gracilariopsis lemaneiformis , Gracilaria verrucosa
REFERENCE   2  [PMID:7763826]
  AUTHORS   Yu S, Pedersen M.
  TITLE     Alpha-1,4-glucan lyase, a new class of starch/glycogen-degrading
            enzyme. II. Subcellular localization and partial amino-acid
            sequence.
  JOURNAL   Planta. 191 (1993) 137-42.
  ORGANISM  Gracilariopsis lemaneiformis
REFERENCE   3  [PMID:7766642]
  AUTHORS   Yu S, Ahmad T, Kenne L, Pedersen M.
  TITLE     alpha-1,4-Glucan lyase, a new class of starch/glycogen degrading
            enzyme. III. Substrate specificity, mode of action, and cleavage
            mechanism.
  JOURNAL   Biochim. Biophys. Acta. 1244 (1995) 1-9.
  ORGANISM  Gracilariopsis lemaneiformis
REFERENCE   4  [PMID:9187252]
  AUTHORS   Yu S, Christensen TM, Kragh KM, Bojsen K, Marcussen J.
  TITLE     Efficient purification, characterization and partial amino acid
            sequencing of two alpha-1,4-glucan lyases from fungi.
  JOURNAL   Biochim. Biophys. Acta. 1339 (1997) 311-20.
  ORGANISM  Morchella costata, Morchella vulgaris
REFERENCE   5  [PMID:10446355]
  AUTHORS   Yu S, Bojsen K, Svensson B, Marcussen J.
  TITLE     alpha-1,4-glucan lyases producing 1,5-anhydro-D-fructose from starch
            and glycogen have sequence similarity to alpha-glucosidases.
  JOURNAL   Biochim. Biophys. Acta. 1433 (1999) 1-15.
  ORGANISM  Gracilariopsis lemaneiformis , Gracilaria verrucosa
REFERENCE   6  [PMID:11982345]
  AUTHORS   Lee SS, Yu S, Withers SG.
  TITLE     alpha-1,4-Glucan lyase performs a trans-elimination via a
            nucleophilic displacement followed by a syn-elimination.
  JOURNAL   J. Am. Chem. Soc. 124 (2002) 4948-9.
  ORGANISM  Gracilariopsis sp.
REFERENCE   7  [PMID:14596624]
  AUTHORS   Lee SS, Yu S, Withers SG.
  TITLE     Detailed dissection of a new mechanism for glycoside cleavage:
            alpha-1,4-glucan lyase.
  JOURNAL   Biochemistry. 42 (2003) 13081-90.
  ORGANISM  Gracilariopsis sp.
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.13
            ExPASy - ENZYME nomenclature database: 4.2.2.13
            ExplorEnz - The Enzyme Database: 4.2.2.13
            ERGO genome analysis and discovery system: 4.2.2.13
            BRENDA, the Enzyme Database: 4.2.2.13
            CAS: 148710-18-3
///
ENTRY       EC 4.2.2.14                 Enzyme
NAME        glucuronan lyase;
            (1,4)-beta-D-glucuronan lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     (1->4)-beta-D-glucuronan lyase
REACTION    Eliminative cleavage of (1->4)-beta-D-glucuronans to give
            oligosaccharides with 4-deoxy-beta-D-gluc-4-enuronosyl groups at
            their non-reducing ends. Complete degradation of glucuronans results
            in the formation of tetrasaccharides.
REFERENCE   1  [PMID:9283009]
  AUTHORS   Michaud P, Pheulpin P, Petit E, Seguin JP, Barbotin JN, Heyraud A,
            Courtois B, Courtois J.
  TITLE     Identification of glucuronan lyase from a mutant strain of Rhizobium
            meliloti.
  JOURNAL   Int. J. Biol. Macromol. 21 (1997) 3-9.
  ORGANISM  Rhizobium meliloti
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.14
            ExPASy - ENZYME nomenclature database: 4.2.2.14
            ExplorEnz - The Enzyme Database: 4.2.2.14
            ERGO genome analysis and discovery system: 4.2.2.14
            BRENDA, the Enzyme Database: 4.2.2.14
///
ENTRY       EC 4.2.2.15                 Enzyme
NAME        anhydrosialidase;
            anhydroneuraminidase;
            sialglycoconjugate N-acylneuraminylhydrolase (2,7-cyclizing);
            sialidase L
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     glycoconjugate sialyl-lyase (2,7-cyclizing)
REACTION    Elimination of alpha-sialyl groups in N-acetylneuraminic acid
            glycosides, releasing 2,7-anhydro-alpha-N-acetylneuraminate
COMMENT     Also acts on N-glycolylneuraminate glycosides. cf. EC 3.2.1.18
            (exo-alpha-sialidase) and EC 3.2.1.129 (endo-alpha-sialidase).
REFERENCE   1  [PMID:2254319]
  AUTHORS   Li YT, Nakagawa H, Ross SA, Hansson GC, Li SC.
  TITLE     A novel sialidase which releases
            2,7-anhydro-alpha-N-acetylneuraminic acid from sialoglycoconjugates.
  JOURNAL   J. Biol. Chem. 265 (1990) 21629-33.
  ORGANISM  Macrobdella decora
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.15
            ExPASy - ENZYME nomenclature database: 4.2.2.15
            ExplorEnz - The Enzyme Database: 4.2.2.15
            ERGO genome analysis and discovery system: 4.2.2.15
            BRENDA, the Enzyme Database: 4.2.2.15
            CAS: 157857-11-9
///
ENTRY       EC 4.2.2.16                 Enzyme
NAME        levan fructotransferase (DFA-IV-forming);
            2,6-beta-D-fructan D-fructosyl-D-fructosyltransferase (forming
            di-beta-D-fructofuranose 2,6':2',6-dianhydride);
            levan fructotransferase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     2,6-beta-D-fructan lyase
            (di-beta-D-fructofuranose-2,6':2',6-dianhydride-forming)
REACTION    Produces di-beta-D-fructofuranose 2,6':2',6-dianhydride (DFA IV) by
            successively eliminating the diminishing (2->6)-beta-D-fructan
            (levan) chain from the terminal D-fructosyl-D-fructosyl disaccharide
COMMENT     This enzyme, like EC 4.2.2.17 [inulin fructotransferase
            (DFA-I-forming)] and EC 4.2.2.18 [inulin fructotransferase
            (DFA-III-forming)] eliminates the fructan chain from the terminal
            disaccharide leaving a difructose dianhydride. These enzymes have
            long been known as fructotransferases, so this is retained in the
            accepted name. Since the transfer is intramolecular, the reaction is
            an elimination and, hence, the enzyme is a lyase, belonging in EC 4.
REFERENCE   1
  AUTHORS   Song, K.B., Bae, K.S., Lee, Y.B., Lee, K.Y. and Rhee, S.K.
  TITLE     Characteristics of levan fructotransferase from Arthrobacter
            ureafaciens K2032 and difructose anhydride IV formation from levan.
  JOURNAL   Enzyme Microb. Technol. 27 (2000) 212-218.
  ORGANISM  Arthrobacter ureafaciens
REFERENCE   2  [PMID:12696949]
  AUTHORS   Jang KH, Ryu EJ, Park BS, Song KB, Kang SA, Kim CH, Uhm TB, Park YI,
            Rhee SK.
  TITLE     Levan fructotransferase from Arthrobacter oxydans J17-21 catalyzes
            the formation of the di-D-fructose dianhydride IV from levan.
  JOURNAL   J. Agric. Food. Chem. 51 (2003) 2632-6.
  ORGANISM  Arthrobacter oxydans
REFERENCE   3  [PMID:10945246]
  AUTHORS   Saito K, Tomita F.
  TITLE     Difructose anhydrides: their mass-production and physiological
            functions.
  JOURNAL   Biosci. Biotechnol. Biochem. 64 (2000) 1321-7.
  ORGANISM  Arthrobacter nicotinovorans, Arthrobacter sp.
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.16
            ExPASy - ENZYME nomenclature database: 4.2.2.16
            ExplorEnz - The Enzyme Database: 4.2.2.16
            ERGO genome analysis and discovery system: 4.2.2.16
            BRENDA, the Enzyme Database: 4.2.2.16
///
ENTRY       EC 4.2.2.17                 Enzyme
NAME        inulin fructotransferase (DFA-I-forming);
            inulin fructotransferase (DFA-I-producing);
            inulin fructotransferase (depolymerizing,
            difructofuranose-1,2':2',1-dianhydride-forming);
            inulin D-fructosyl-D-fructosyltransferase
            (1,2':1',2-dianhydride-forming);
            inulin D-fructosyl-D-fructosyltransferase (forming
            alpha-D-fructofuranose beta-D-fructofuranose 1,2':1',2-dianhydride)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     2,1-beta-D-fructan lyase
            (alpha-D-fructofuranose-beta-D-fructofuranose-1,2':2,1'-dianhydride-
            forming)
REACTION    Produces alpha-D-fructofuranose beta-D-fructofuranose
            1,2':2,1'-dianhydride (DFA I) by successively eliminating the
            diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal
            D-fructosyl-D-fructosyl disaccharide.
COMMENT     This enzyme, like EC 4.2.2.16 [levan fructotransferase
            (DFA-IV-forming)] and EC 4.2.2.18 [inulin fructotransferase
            (DFA-III-forming)] eliminates the fructan chain from the terminal
            disaccharide leaving a difructose dianhydride. These enzymes have
            long been known as fructotransferases, so this is retained in the
            accepted name. Since the transfer is intramolecular, the reaction is
            an elimination and, hence, the enzyme is a lyase, belonging in EC 4.
REFERENCE   1
  AUTHORS   Seki, K., Haraguchi, K., Kishimoto, M., Kobayashi, S. and Kainuma,
            K.
  TITLE     Purification and properties of a novel inulin fructotransferase (DFA
            I-producing) from Arthrobacter globiformis S14-3.
  JOURNAL   Agric. Biol. Chem. 53 (1989) 2089-2094.
  ORGANISM  Arthrobacter globiformis
GENES       ART: Arth_0051
            NCA: Noca_0068
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.17
            ExPASy - ENZYME nomenclature database: 4.2.2.17
            ExplorEnz - The Enzyme Database: 4.2.2.17
            ERGO genome analysis and discovery system: 4.2.2.17
            BRENDA, the Enzyme Database: 4.2.2.17
            CAS: 125008-19-7
///
ENTRY       EC 4.2.2.18                 Enzyme
NAME        inulin fructotransferase (DFA-III-forming);
            inulin fructotransferase (DFA-III-producing);
            inulin fructotransferase (depolymerizing);
            inulase II;
            inulinase II;
            inulin fructotransferase (depolymerizing,
            difructofuranose-1,2':2,3'-dianhydride-forming);
            inulin D-fructosyl-D-fructosyltransferase
            (1,2':2,3'-dianhydride-forming);
            inulin D-fructosyl-D-fructosyltransferase (forming
            alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     2,1-beta-D-fructan lyase
            (alpha-D-fructofuranose-beta-D-fructofuranose-1,2':2,3'-dianhydride-
            forming)
REACTION    Produces alpha-D-fructofuranose beta-D-fructofuranose
            1,2':2,3'-dianhydride (DFA III) by successively eliminating the
            diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal
            D-fructosyl-D-fructosyl disaccharide.
COMMENT     This enzyme, like EC 4.2.2.16 [levan fructotransferase
            (DFA-IV-forming)] and EC 4.2.2.17 [inulin fructotransferase
            (DFA-I-forming)] eliminates the fructan chain from the terminal
            disaccharide leaving a difructose dianhydride. These enzymes have
            long been known as fructotransferases, so this is retained in the
            accepted name. Since the transfer is intramolecular, the reaction is
            an elimination and, hence, the enzyme is a lyase, belonging in EC 4.
REFERENCE   1  [PMID:1148257]
  AUTHORS   Uchiyama T.
  TITLE     Action of Arthrobacter ureafaciens inulinase II on several
            oligofructans and bacterial levans.
  JOURNAL   Biochim. Biophys. Acta. 397 (1975) 153-63.
  ORGANISM  Arthrobacter ureafaciens
REFERENCE   2
  AUTHORS   Uchiyama, T., Niwa, S. and Tanaka, K.
  TITLE     Purification and properties of Arthrobacter ureafaciens inulase II.
  JOURNAL   Biochim. Biophys. Acta 315 (1973) 412-420.
  ORGANISM  Arthrobacter ureafaciens
STRUCTURES  PDB: 2INU  2INV  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.18
            ExPASy - ENZYME nomenclature database: 4.2.2.18
            ExplorEnz - The Enzyme Database: 4.2.2.18
            ERGO genome analysis and discovery system: 4.2.2.18
            BRENDA, the Enzyme Database: 4.2.2.18
            CAS: 50936-42-0
///
ENTRY       EC 4.2.2.19                 Enzyme
NAME        chondroitin B lyase;
            chondroitinase B;
            ChonB;
            ChnB
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     chondroitin B lyase
REACTION    Eliminative cleavage of dermatan sulfate containing
            1,4-beta-D-hexosaminyl and 1,3-beta-D-glucurosonyl or
            1,3-alpha-L-iduronosyl linkages to disaccharides containing
            4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated
            dermatan-sulfate disaccharide (deltaUA-GalNAc-4S).
COMMENT     This is the only lyase that is known to be specific for dermatan
            sulfate as substrate. The minimum substrate length required for
            catalysis is a tetrasaccharide [2]. In general, chondroitin sulfate
            (CS) and dermatan sulfate (DS) chains comprise a linkage region, a
            chain cap and a repeat region. The repeat region of CS is a
            repeating disaccharide of glucuronic acid (GlcA) and
            N-acetylgalactosamine (GalNAc) [-4)GlcA(beta1-3)GalNAc(beta1-]n,
            which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of
            GlcA. GlcA residues of CS may be epimerized to iduronic acid (IdoA)
            forming the repeating disaccharide [-4)IdoA(alpha1-3)GalNAc(beta1-]n
            of DS. Both the concentrations and locations of sulfate-ester
            substituents vary with glucosaminoglycan source [5].
REFERENCE   1  [PMID:8526872]
  AUTHORS   Gu K, Linhardt RJ, Laliberte M, Gu K, Zimmermann J.
  TITLE     Purification, characterization and specificity of chondroitin lyases
            and glycuronidase from Flavobacterium heparinum.
  JOURNAL   Biochem. J. 312 ( Pt 2) (1995) 569-77.
  ORGANISM  Flavobacterium heparinum
REFERENCE   2  [PMID:12063249]
  AUTHORS   Pojasek K, Raman R, Kiley P, Venkataraman G, Sasisekharan R.
  TITLE     Biochemical characterization of the chondroitinase B active site.
  JOURNAL   J. Biol. Chem. 277 (2002) 31179-86.
  ORGANISM  Flavobacterium heparinum
REFERENCE   3  [PMID:11500043]
  AUTHORS   Pojasek K, Shriver Z, Kiley P, Venkataraman G, Sasisekharan R.
  TITLE     Recombinant expression, purification, and kinetic characterization
            of chondroitinase AC and chondroitinase B from Flavobacterium
            heparinum.
  JOURNAL   Biochem. Biophys. Res. Commun. 286 (2001) 343-51.
  ORGANISM  Flavobacterium heparinum
REFERENCE   4  [PMID:12443044]
  AUTHORS   Suzuki K, Terasaki Y, Uyeda M.
  TITLE     Inhibition of hyaluronidases and chondroitinases by fatty acids.
  JOURNAL   J. Enzyme. Inhib. Med. Chem. 17 (2002) 183-6.
  ORGANISM  Flavobacterium heparinum
REFERENCE   5  [PMID:427837]
  AUTHORS   Ototani N, Yosizawa Z.
  TITLE     Purification of chondroitinase B and chondroitinase C using
            glycosaminoglycan-bound AH-Sepharose 4B.
  JOURNAL   Carbohydr. Res. 70 (1979) 295-306.
  ORGANISM  Flavobacterium heparinum
REFERENCE   6  [PMID:10618199]
  AUTHORS   Tkalec AL, Fink D, Blain F, Zhang-Sun G, Laliberte M, Bennett DC, Gu
            K, Zimmermann JJ, Su H.
  TITLE     Isolation and expression in Escherichia coli of cslA and cslB, genes
            coding for the chondroitin sulfate-degrading enzymes chondroitinase
            AC and chondroitinase B, respectively, from Flavobacterium
            heparinum.
  JOURNAL   Appl. Environ. Microbiol. 66 (2000) 29-35.
  ORGANISM  Flavobacterium heparinum
REFERENCE   7  [PMID:15155751]
  AUTHORS   Michel G, Pojasek K, Li Y, Sulea T, Linhardt RJ, Raman R, Prabhakar
            V, Sasisekharan R, Cygler M.
  TITLE     The structure of chondroitin B lyase complexed with
            glycosaminoglycan oligosaccharides unravels a calcium-dependent
            catalytic machinery.
  JOURNAL   J. Biol. Chem. 279 (2004) 32882-96.
  ORGANISM  Pedobacter heparinus
REFERENCE   8  [PMID:10216304]
  AUTHORS   Li Y, Matte A, Su H, Cygler M.
  TITLE     Crystallization and preliminary X-ray analysis of chondroitinase B
            from Flavobacterium heparinum.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 55 (1999) 1055-7.
  ORGANISM  Flavobacterium heparinum
REFERENCE   9  [PMID:10600383]
  AUTHORS   Huang W, Matte A, Li Y, Kim YS, Linhardt RJ, Su H, Cygler M.
  TITLE     Crystal structure of chondroitinase B from Flavobacterium heparinum
            and its complex with a disaccharide product at 1.7 A resolution.
  JOURNAL   J. Mol. Biol. 294 (1999) 1257-69.
  ORGANISM  Flavobacterium heparinum
REFERENCE   10 [PMID:16336265]
  AUTHORS   Huckerby TN, Nieduszynski IA, Giannopoulos M, Weeks SD, Sadler IH,
            Lauder RM.
  TITLE     Characterization of oligosaccharides from the chondroitin/dermatan
            sulfates. 1H-NMR and 13C-NMR studies of reduced trisaccharides and
            hexasaccharides.
  JOURNAL   FEBS. J. 272 (2005) 6276-86.
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.19
            ExPASy - ENZYME nomenclature database: 4.2.2.19
            ExplorEnz - The Enzyme Database: 4.2.2.19
            ERGO genome analysis and discovery system: 4.2.2.19
            BRENDA, the Enzyme Database: 4.2.2.19
            CAS: 52227-83-5
///
ENTRY       EC 4.2.2.20                 Enzyme
NAME        chondroitin-sulfate-ABC endolyase;
            chondroitinase (ambiguous);
            chondroitin ABC eliminase (ambiguous);
            chondroitinase ABC (ambiguous);
            chondroitin ABC lyase (ambiguous);
            chondroitin sulfate ABC lyase (ambiguous);
            ChS ABC lyase (ambiguous);
            chondroitin sulfate ABC endoeliminase;
            chondroitin sulfate ABC endolyase;
            ChS ABC lyase I
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     chondroitin-sulfate-ABC endolyase
REACTION    Endolytic cleavage of beta-1,4-galactosaminic bonds between
            N-acetylgalactosamine and either D-glucuronic acid or L-iduronic
            acid to produce a mixture of Delta4-unsaturated oligosaccharides of
            different sizes that are ultimately degraded to Delta4-unsaturated
            tetra- and disaccharides
COMMENT     This enzyme degrades a variety of glycosaminoglycans of the
            chondroitin-sulfate- and dermatan-sulfate type. Chondroitin sulfate,
            chondroitin-sulfate proteoglycan and dermatan sulfate are the best
            substrates but the enzyme can also act on hyaluronan at a much lower
            rate. Keratan sulfate, heparan sulfate and heparin are not
            substrates. In general, chondroitin sulfate (CS) and dermatan
            sulfate (DS) chains comprise a linkage region, a chain cap and a
            repeat region. The repeat region of CS is a repeating disaccharide
            of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc)
            [-4)GlcA(beta1-3)GalNAc(beta1-]n, which may be O-sulfated on the C-4
            and/or C-6 of GalNAc and C-2 of GlcA. GlcA residues of CS may be
            epimerized to iduronic acid (IdoA) forming the repeating
            disaccharide [-4)IdoA(alpha1-3)GalNAc(beta1-]n of DS. Both the
            concentrations and locations of sulfate-ester substituents vary with
            glucosaminoglycan source [5]. The related enzyme EC 4.2.2.21,
            chondroitin-sulfate-ABC exolyase, has the same substrate specificity
            but removes disaccharide residues from the non-reducing ends of both
            polymeric chondroitin sulfates and their oligosaccharide fragments
            produced by EC 4.2.2.20 [4].
REFERENCE   1  [PMID:5647268]
  AUTHORS   Yamagata T, Saito H, Habuchi O, Suzuki S.
  TITLE     Purification and properties of bacterial chondroitinases and
            chondrosulfatases.
  JOURNAL   J. Biol. Chem. 243 (1968) 1523-35.
  ORGANISM  Proteus vulgaris, Flavobacterium heparinum
REFERENCE   2  [PMID:4231029]
  AUTHORS   Saito H, Yamagata T, Suzuki S.
  TITLE     Enzymatic methods for the determination of small quantities of
            isomeric chondroitin sulfates.
  JOURNAL   J. Biol. Chem. 243 (1968) 1536-42.
  ORGANISM  Proteus vulgaris, Flavobacterium heparinum
REFERENCE   3  [PMID:5647269]
  AUTHORS   Suzuki S, Saito H, Yamagata T, Anno K, Seno N, Kawai Y, Furuhashi T.
  TITLE     Formation of three types of disulfated disaccharides from
            chondroitin sulfates by chondroitinase digestion.
  JOURNAL   J. Biol. Chem. 243 (1968) 1543-50.
  ORGANISM  Proteus vulgaris, Flavobacterium heparinum
REFERENCE   4  [PMID:9083041]
  AUTHORS   Hamai A, Hashimoto N, Mochizuki H, Kato F, Makiguchi Y, Horie K,
            Suzuki S.
  TITLE     Two distinct chondroitin sulfate ABC lyases. An endoeliminase
            yielding tetrasaccharides and an exoeliminase preferentially acting
            on oligosaccharides.
  JOURNAL   J. Biol. Chem. 272 (1997) 9123-30.
  ORGANISM  Proteus vulgaris
REFERENCE   5  [PMID:16336265]
  AUTHORS   Huckerby TN, Nieduszynski IA, Giannopoulos M, Weeks SD, Sadler IH,
            Lauder RM.
  TITLE     Characterization of oligosaccharides from the chondroitin/dermatan
            sulfates. 1H-NMR and 13C-NMR studies of reduced trisaccharides and
            hexasaccharides.
  JOURNAL   FEBS. J. 272 (2005) 6276-86.
  ORGANISM  Proteus vulgaris
ORTHOLOGY   KO: K08961  chondroitin-sulfate-ABC endolyase
GENES       YPE: YPO0824
            YPK: y3211
            YPA: YPA_0445
            YPN: YPN_3027
            YPS: YPTB3073
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.20
            ExPASy - ENZYME nomenclature database: 4.2.2.20
            ExplorEnz - The Enzyme Database: 4.2.2.20
            ERGO genome analysis and discovery system: 4.2.2.20
            BRENDA, the Enzyme Database: 4.2.2.20
///
ENTRY       EC 4.2.2.21                 Enzyme
NAME        chondroitin-sulfate-ABC exolyase;
            chondroitinase (ambiguous);
            chondroitin ABC eliminase (ambiguous);
            chondroitinase ABC (ambiguous);
            chondroitin ABC lyase (ambiguous);
            chondroitin sulfate ABC lyase (ambiguous);
            ChS ABC lyase (ambiguous);
            chondroitin sulfate ABC exoeliminase;
            chondroitin sulfate ABC exolyase;
            ChS ABC lyase II
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on polysaccharides
SYSNAME     chondroitin-sulfate-ABC exolyase
REACTION    Exolytic cleavage of disaccharide residues from the non-reducing
            ends of both polymeric chondroitin sulfates and their
            oligosaccharide fragments
COMMENT     This enzyme degrades a variety of glycosaminoglycans of the
            chondroitin-sulfate- and dermatan-sulfate type. Chondroitin sulfate,
            chondroitin-sulfate proteoglycan and dermatan sulfate are the best
            substrates but the enzyme can also act on hyaluronan at a much lower
            rate. Keratan sulfate, heparan sulfate and heparin are not
            substrates. In general, chondroitin sulfate (CS) and dermatan
            sulfate (DS) chains comprise a linkage region, a chain cap and a
            repeat region. The repeat region of CS is a repeating disaccharide
            of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc)
            [-4)GlcA(beta1-3)GalNAc(beta1-]n, which may be O-sulfated on the C-4
            and/or C-6 of GalNAc and C-2 of GlcA. GlcA residues of CS may be
            epimerized to iduronic acid (IdoA) forming the repeating
            disaccharide [-4)IdoA(alpha1-3)GalNAc(beta1-]n of DS. Both the
            concentrations and locations of sulfate-ester substituents vary with
            glucosaminoglycan source [5]. The related enzyme EC 4.2.2.20,
            chondroitin-sulfate-ABC endolyase, has the same substrate
            specificity but produces a mixture of Delta4-unsaturated
            oligosaccharides of different sizes that are ultimately degraded to
            Delta4-unsaturated tetra- and disaccharides [4].
REFERENCE   1  [PMID:5647268]
  AUTHORS   Yamagata T, Saito H, Habuchi O, Suzuki S.
  TITLE     Purification and properties of bacterial chondroitinases and
            chondrosulfatases.
  JOURNAL   J. Biol. Chem. 243 (1968) 1523-35.
  ORGANISM  Proteus vulgaris
REFERENCE   2  [PMID:4231029]
  AUTHORS   Saito H, Yamagata T, Suzuki S.
  TITLE     Enzymatic methods for the determination of small quantities of
            isomeric chondroitin sulfates.
  JOURNAL   J. Biol. Chem. 243 (1968) 1536-42.
  ORGANISM  Proteus vulgaris
REFERENCE   3  [PMID:5647269]
  AUTHORS   Suzuki S, Saito H, Yamagata T, Anno K, Seno N, Kawai Y, Furuhashi T.
  TITLE     Formation of three types of disulfated disaccharides from
            chondroitin sulfates by chondroitinase digestion.
  JOURNAL   J. Biol. Chem. 243 (1968) 1543-50.
  ORGANISM  Proteus vulgaris
REFERENCE   4  [PMID:9083041]
  AUTHORS   Hamai A, Hashimoto N, Mochizuki H, Kato F, Makiguchi Y, Horie K,
            Suzuki S.
  TITLE     Two distinct chondroitin sulfate ABC lyases. An endoeliminase
            yielding tetrasaccharides and an exoeliminase preferentially acting
            on oligosaccharides.
  JOURNAL   J. Biol. Chem. 272 (1997) 9123-30.
  ORGANISM  Proteus vulgaris
REFERENCE   5  [PMID:16336265]
  AUTHORS   Huckerby TN, Nieduszynski IA, Giannopoulos M, Weeks SD, Sadler IH,
            Lauder RM.
  TITLE     Characterization of oligosaccharides from the chondroitin/dermatan
            sulfates. 1H-NMR and 13C-NMR studies of reduced trisaccharides and
            hexasaccharides.
  JOURNAL   FEBS. J. 272 (2005) 6276-86.
  ORGANISM  Proteus vulgaris
ORTHOLOGY   KO: K08962  chondroitin-sulfate-ABC exolyase
GENES       YPE: YPO0824
            YPK: y3211
            YPA: YPA_0445
            YPN: YPN_3027
            YPS: YPTB3073
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.2.21
            ExPASy - ENZYME nomenclature database: 4.2.2.21
            ExplorEnz - The Enzyme Database: 4.2.2.21
            ERGO genome analysis and discovery system: 4.2.2.21
            BRENDA, the Enzyme Database: 4.2.2.21
///
ENTRY       EC 4.2.3.1                  Enzyme
NAME        threonine synthase;
            threonine synthetase;
            O-phospho-L-homoserine phospho-lyase (adding water)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     O-phospho-L-homoserine phosphate-lyase (adding water;
            L-threonine-forming)
REACTION    O-phospho-L-homoserine + H2O = L-threonine + phosphate [RN:R01466]
ALL_REAC    R01466;
            (other) R05086
SUBSTRATE   O-phospho-L-homoserine [CPD:C01102];
            H2O [CPD:C00001]
PRODUCT     L-threonine [CPD:C00188];
            phosphate [CPD:C00009]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:13823379]
  AUTHORS   FLAVIN M, SLAUGHTER C.
  TITLE     Purification and properties of threonine synthetase of Neurospora.
  JOURNAL   J. Biol. Chem. 235 (1960) 1103-8.
  ORGANISM  Neurospora crassa [GN:dncr]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00750  Vitamin B6 metabolism
ORTHOLOGY   KO: K01733  threonine synthase
GENES       SPU: 586640(LOC586640)
            ATH: AT1G72810
            OSA: 4325651 4339521
            CME: CMR339C
            SCE: YCR053W(THR4)
            AGO: AGOS_AAR059C
            PIC: PICST_65754(THR4)
            CAL: CaO19_4233(CaO19.4233)
            CGR: CAGL0K09328g
            SPO: SPAC9E9.06c
            ANI: AN3031.2
            AFM: AFUA_3G08980
            AOR: AO090038000224
            CNE: CNB01150
            UMA: UM04341.1
            TBR: Tb927.7.4390
            TCR: 504213.80 508857.160
            LMA: LmjF14.0350
            ECO: b0004(thrC)
            ECJ: JW0003(thrC)
            ECE: Z0004(thrC)
            ECS: ECs0004
            ECC: c0005(thrC)
            ECI: UTI89_C0004(thrC)
            ECP: ECP_0004
            ECV: APECO1_1974(thrC)
            ECW: EcE24377A_0003(thrC)
            ECX: EcHS_A0005(thrC)
            STY: STY0004(thrC)
            STT: t0004(thrC)
            SPT: SPA0004(thrC)
            SEC: SC0004(thrC)
            STM: STM0004(thrC)
            YPE: YPO0461(thrC)
            YPK: y3715(thrC)
            YPM: YP_3721(thrC)
            YPA: YPA_4053
            YPN: YPN_0333
            YPP: YPDSF_3172
            YPS: YPTB0604(thrC)
            YPI: YpsIP31758_3474(thrC)
            YEN: YE0602(thrC)
            SFL: SF0004(thrC)
            SFX: S0004(thrC)
            SFV: SFV_0003(thrC)
            SSN: SSON_0004(thrC)
            SBO: SBO_0003(thrC)
            SDY: SDY_0004(thrC)
            ECA: ECA3889(thrC)
            PLU: plu0565(thrC)
            BUC: BU192(thrC)
            BAS: BUsg186(thrC)
            BAB: bbp181(thrC)
            BCC: BCc_125(thrC)
            SGL: SG0406
            ENT: Ent638_0566
            SPE: Spro_0685
            BFL: Bfl113(thrC)
            BPN: BPEN_117(thrC)
            HIN: HI0087(thrC)
            HIT: NTHI0165(thrC)
            HIP: CGSHiEE_02850
            HIQ: CGSHiGG_02985
            HSO: HS_1212(thrC)
            PMU: PM0115(thrC)
            MSU: MS1701(thrC)
            APL: APL_0269(thrCA) APL_1499(thrC)
            ASU: Asuc_0803
            XFA: XF2223
            XFT: PD1271(thrC)
            XCC: XCC1803(thrC)
            XCB: XC_2386
            XCV: XCV1869(thrC)
            XAC: XAC1823(thrC)
            XOO: XOO2247(thrC)
            XOM: XOO_2111(XOO2111)
            VCH: VC2362
            VCO: VC0395_A1941(thrC)
            VVU: VV1_0543
            VVY: VV0652
            VPA: VP0496
            VFI: VF1458 VF2116
            PPR: PBPRA0554
            PAE: PA3735(thrC)
            PAU: PA14_16090(thrC)
            PAP: PSPA7_1384(thrC)
            PPU: PP_0662 PP_1471(thrC)
            PPF: Pput_0696 Pput_4250
            PST: PSPTO_1481(thrC)
            PSB: Psyr_1291
            PSP: PSPPH_1361(thrC)
            PFL: PFL_1104(thrC) PFL_3811
            PFO: Pfl_1028 Pfl_2313
            PEN: PSEEN3862 PSEEN4251(thrC)
            PMY: Pmen_3393
            PAR: Psyc_2137(thrC)
            PCR: Pcryo_2465
            PRW: PsycPRwf_2379
            ACI: ACIAD0263(thrC)
            SON: SO_3413(thrC)
            SDN: Sden_2738
            SFR: Sfri_2904
            SAZ: Sama_0907
            SBL: Sbal_1229
            SBM: Shew185_1273
            SLO: Shew_1081
            SPC: Sputcn32_2733
            SSE: Ssed_1177
            SPL: Spea_1068
            SHE: Shewmr4_1140
            SHM: Shewmr7_1211
            SHN: Shewana3_1141 Shewana3_3018
            SHW: Sputw3181_1279
            CPS: CPS_4289(thrC)
            PHA: PSHAa2377(thrC)
            PAT: Patl_3578
            SDE: Sde_1210
            PIN: Ping_1277
            MAQ: Maqu_2273
            LPN: lpg1643(thrC)
            LPF: lpl1383(thrC)
            LPP: lpp1613(thrC)
            MCA: MCA0596(thrC)
            FTU: FTT0428(thrC)
            FTF: FTF0428(thrC1)
            FTW: FTW_1646(thrC)
            FTL: FTL_0498
            FTH: FTH_0495(thrC)
            FTA: FTA_0523(thrC) FTA_0959
            FTN: FTN_0527(thrC)
            TCX: Tcr_1249
            NOC: Noc_2453
            AEH: Mlg_1821
            HCH: HCH_01780(thrC)
            CSA: Csal_3009
            ABO: ABO_0807(thrC)
            MMW: Mmwyl1_3764
            AHA: AHA_0766 AHA_3016(thrC)
            CRP: CRP_120
            VOK: COSY_0707(thrC)
            NME: NMB1046
            NMA: NMA1440(thrC)
            NMC: NMC1165(thrC)
            NGO: NGO0689
            CVI: CV_0997(thrC)
            RSO: RSc1328(thrC)
            REU: Reut_A1992
            REH: H16_A2265(thrC) H16_B0301
            RME: Rmet_1965
            BMA: BMA1384(thrC)
            BMV: BMASAVP1_A1874(thrC)
            BML: BMA10299_A0023(thrC)
            BMN: BMA10247_1146(thrC)
            BXE: Bxe_A2380
            BVI: Bcep1808_1780
            BUR: Bcep18194_A5154
            BCN: Bcen_6226
            BCH: Bcen2424_1853
            BAM: Bamb_1791
            BPS: BPSL1478(thrC)
            BPM: BURPS1710b_2395(thrC)
            BPL: BURPS1106A_2269(thrC)
            BPD: BURPS668_2231(thrC)
            BTE: BTH_I2199(thrC)
            PNU: Pnuc_0439
            BPE: BP2783(thrC)
            BPA: BPP2480(thrC)
            BBR: BB1927(thrC) BB3742
            RFR: Rfer_1913
            POL: Bpro_2191
            PNA: Pnap_2230
            AAV: Aave_1239
            AJS: Ajs_3205
            VEI: Veis_2664
            MPT: Mpe_A1542
            HAR: HEAR2149
            MMS: mma_1313(thrC)
            NEU: NE2370(thrC)
            NET: Neut_0864
            NMU: Nmul_A1550
            EBA: ebA4955(thrC)
            AZO: azo2080(thrC)
            DAR: Daro_2382
            TBD: Tbd_0844
            MFA: Mfla_0905 Mfla_1049
            HPY: HP0098(thrC)
            HPJ: jhp0090(thrC)
            HPA: HPAG1_0098
            HHE: HH0527(thrC)
            HAC: Hac_1479(thrC)
            WSU: WS2110(thrC)
            TDN: Tmden_0789
            CJE: Cj0812(thrC)
            CJR: CJE0903(thrC)
            CJJ: CJJ81176_0833(thrC)
            CJU: C8J_0763(thrC)
            CJD: JJD26997_1198(thrC)
            CCV: CCV52592_0130(thrC)
            CHA: CHAB381_1020(thrC)
            CCO: CCC13826_2052(thrC)
            ABU: Abu_2067(thrC)
            NIS: NIS_1040(thrC)
            SUN: SUN_1624(thrC)
            GSU: GSU1695(thrC)
            GME: Gmet_1631
            GUR: Gura_1892
            PCA: Pcar_1502
            PPD: Ppro_2395
            DVU: DVU3210(thrC)
            DVL: Dvul_0177
            DDE: Dde_0171
            DPS: DP2619
            ADE: Adeh_1723
            AFW: Anae109_2078
            MXA: MXAN_3409(thrC)
            SAT: SYN_02122
            SFU: Sfum_1930
            PUB: SAR11_0128(thrC)
            MLO: mll7517 mll9542
            MES: Meso_0760
            PLA: Plav_0677
            SME: SMa0485(thrC2) SMc00077(thrC1)
            SMD: Smed_0536
            ATU: Atu0787(thrC)
            ATC: AGR_C_1442
            RET: RHE_CH00979(thrC) RHE_CH04092(ypch01441)
            RLE: RL1062(thrC)
            BME: BMEI1450
            BMF: BAB1_0510
            BMS: BR0484(thrC)
            BMB: BruAb1_0506(thrC)
            BOV: BOV_0489(thrC)
            OAN: Oant_0599 Oant_0665
            BJA: bll4777 bll7236 blr1181(thrC)
            BRA: BRADO4082 BRADO6693(thrC)
            BBT: BBta_0839(thrC) BBta_4458
            RPA: RPA0839(thrC)
            RPB: RPB_4578
            RPC: RPC_4795
            RPD: RPD_0822
            RPE: RPE_4759
            NWI: Nwi_0229
            NHA: Nham_0262
            BHE: BH04480(thrC)
            XAU: Xaut_3524
            CCR: CC_3399
            SIL: SPO3071(thrC)
            SIT: TM1040_2330
            RSP: RSP_1831(thrC)
            RSH: Rsph17029_0480
            RSQ: Rsph17025_0620
            JAN: Jann_3149
            RDE: RD1_2141(thrC)
            PDE: Pden_4315
            MMR: Mmar10_1096
            HNE: HNE_1045(thrC)
            ZMO: ZMO1891(thrC)
            NAR: Saro_0921
            SAL: Sala_1398
            SWI: Swit_1413
            ELI: ELI_02760
            GOX: GOX1868
            GBE: GbCGDNIH1_2253
            ACR: Acry_1787
            RRU: Rru_A3233
            MAG: amb3388
            MGM: Mmc1_0459
            ABA: Acid345_4034
            BSU: BG10461(thrC)
            BHA: BH3421(thrC)
            BAN: BA1969(thrC)
            BAR: GBAA1969(thrC)
            BAA: BA_2469
            BAT: BAS1826
            BCE: BC1965
            BCA: BCE_2052(thrC)
            BCZ: BCZK1783(thrC)
            BTK: BT9727_1800(thrC)
            BTL: BALH_1742(thrC)
            BLI: BL02065(thrCA) BL02136(thrC)
            BLD: BLi02779 BLi03413(thrC)
            BCL: ABC2941(thrC) ABC3183
            BAY: RBAM_029360(thrC)
            BPU: BPUM_1723(thrC2) BPUM_2887(thrC1)
            OIH: OB0465
            GKA: GK1761 GK2963
            SAU: SA1165(thrC)
            SAV: SAV1329(thrC)
            SAM: MW1216(thrC)
            SAR: SAR1339(thrC)
            SAS: SAS1269
            SAC: SACOL1363(thrC)
            SAB: SAB1187(thrC)
            SAA: SAUSA300_1227(thrC)
            SAO: SAOUHSC_01321
            SEP: SE1010
            SER: SERP0898(thrC)
            SHA: SH1578(thrC)
            SSP: SSP1437
            LMO: lmo2546(thrC)
            LMF: LMOf2365_2519(thrC)
            LIN: lin2690(thrC)
            LWE: lwe2495(thrC)
            LLA: L0092(thrC)
            LLC: LACR_2405
            LLM: llmg_2387(thrC)
            SPN: SP_2066
            SPR: spr1878(thrC)
            SPD: SPD_1877(thrC)
            SAG: SAG0055(thrC)
            SAN: gbs0055(thrC)
            SAK: SAK_0088(thrC)
            SMU: SMU.70(thrC)
            STC: str1878(thrC)
            STL: stu1878(thrC)
            SSA: SSA_0095(thrC)
            SGO: SGO_0139(thrC)
            LPL: lp_2758(thrC)
            LAC: LBA1214(thrC)
            LSL: LSL_1521(thrC)
            LDB: Ldb1761(thrC)
            LBU: LBUL_1631
            LCA: LSEI_2150
            EFA: EF2421(thrC)
            OOE: OEOE_1545
            STH: STH2557
            CAC: CAC0999(thrC)
            CTC: CTC00570 CTC02358
            CNO: NT01CX_0897
            CTH: Cthe_1381
            CDF: CD2118(thrC)
            CBO: CBO1638(thrC)
            CBA: CLB_1655(thrC)
            CBH: CLC_1664(thrC)
            CBF: CLI_1715(thrC)
            CBE: Cbei_1293
            CKL: CKL_0704(thrC)
            CHY: CHY_1911(thrC)
            DSY: DSY1894
            DRM: Dred_1379
            SWO: Swol_1302
            CSC: Csac_1221
            TTE: TTE2619(thrC2)
            MTA: Moth_1306 Moth_1998
            MTU: Rv1295(thrC)
            MTC: MT1334(thrC)
            MBO: Mb1327(thrC)
            MBB: BCG_1355(thrC)
            MLE: ML1130(thrC)
            MPA: MAP2467c(thrC)
            MAV: MAV_1510(thrC)
            MSM: MSMEG_4956(thrC)
            MMC: Mmcs_3895
            CGL: NCgl2139(cgl2220)
            CGB: cg2437(thrC)
            CEF: CE2122(thrC)
            CDI: DIP1666(thrC)
            CJK: jk1351(thrC)
            NFA: nfa10500(thrC)
            RHA: RHA1_ro01487(thrC)
            SCO: SCO4293(SCD95A.26) SCO5355(SCBAC5H2.24)
            SMA: SAV2917(thrC1) SAV3191(thrC2) SAV3934(thrC3)
            TWH: TWT438(thrC)
            TWS: TW330(thrC)
            LXX: Lxx06880(thrC) Lxx14980
            AAU: AAur_2611(thrC)
            PAC: PPA1257
            TFU: Tfu_0226 Tfu_2423
            FRA: Francci3_3724 Francci3_4397
            FAL: FRAAL5950(thrC) FRAAL6700(thrC-like)
            ACE: Acel_0100 Acel_0631
            SEN: SACE_1007 SACE_1437(thrC-like) SACE_6297(thrC)
            BLO: BL1036(thrC)
            BAD: BAD_0903(thrC)
            RXY: Rxyl_3123
            RBA: RB10894(thrC)
            TDE: TDE2192 TDE2676
            LIL: LA3747(thrC)
            LIC: LIC10484(thrC)
            LBJ: LBJ_2549(thrC)
            LBL: LBL_0563(thrC)
            SYN: sll1172(thrC) sll1688(thrC)
            SYW: SYNW2526(thrC)
            SYC: syc1498_c(thrC) syc2311_d(thrC)
            SYF: Synpcc7942_1782 Synpcc7942_2612
            SYD: Syncc9605_2695
            SYE: Syncc9902_2321
            SYG: sync_2943(thrC)
            SYR: SynRCC307_1491(thrC) SynRCC307_2535(thrC)
            SYX: SynWH7803_2533(thrC)
            CYA: CYA_0298(thrC-1) CYA_2454(thrC-2)
            CYB: CYB_2298(thrC-1) CYB_2820(thrC-2)
            TEL: tll1227(thrC) tlr0982(thrC)
            GVI: gll1463(thrC) gll2062(thrC) gll2362(thrC)
            ANA: all2072(thrC) alr3293(thrC)
            AVA: Ava_3117 Ava_4952
            PMA: Pro1885(thrC)
            PMM: PMM1716(thrC)
            PMT: PMT2274(thrC)
            PMN: PMN2A_1327
            PMI: PMT9312_1808
            PMB: A9601_19251(thrC)
            PMC: P9515_19071(thrC)
            PMF: P9303_30231(thrC)
            PMG: P9301_19061(thrC)
            PME: NATL1_22001(thrC)
            TER: Tery_0140 Tery_4348
            BTH: BT_2401
            BFR: BF0610
            BFS: BF0560(thrC)
            SRU: SRU_2377(thrC)
            CHU: CHU_0075(thrC)
            GFO: GFO_1968(thrC)
            FJO: Fjoh_2573
            CTE: CT2035(thrC)
            CCH: Cag_0138
            CPH: Cpha266_2546
            PVI: Cvib_1630
            PLT: Plut_1987
            DET: DET1205(thrC)
            DEH: cbdb_A1122(thrC)
            DRA: DR_A0360
            DGE: Dgeo_2252
            TTH: TTC0117
            TTJ: TTHA0491
            AAE: aq_425(thrC2) aq_608(thrC1)
            TMA: TM0546
            MJA: MJ1465(thrC)
            MMP: MMP0135(thrC)
            MAC: MA1610(thrC)
            MBA: Mbar_A2049 Mbar_A3541
            MMA: MM_0133 MM_0282
            MBU: Mbur_0457 Mbur_1454
            MTP: Mthe_1587
            MHU: Mhun_1619
            MTH: MTH253
            MST: Msp_0588(thrC)
            MSI: Msm_0214
            MKA: MK0974(thrC)
            AFU: AF0551(thrC-1) AF1316(thrC-2)
            HAL: VNG0541G(thrC2) VNG2108G(thrC3) VNG2430G(thrC1)
            HMA: pNG7257(thrC2) rrnAC2515(thrC4) rrnAC2667(thrC3)
                 rrnAC3505(thrC1)
            HWA: HQ1042A(thrC) HQ1355A(thrC) HQ1564A(thrC)
            NPH: NP1632A(thrC_3) NP4464A(thrC_2) NP5280A(thrC_1)
            TAC: Ta0026 Ta0495
            TVO: TVN0071 TVN0752
            PTO: PTO0418 PTO0564 PTO1040
            PHO: PH0857 PH1406 PH1627
            PAB: PAB0369(thrC-2) PAB1677(thrC-2) PAB1869(thrC-2)
            PFU: PF0031 PF1055 PF1406 PF1639
            TKO: TK1478 TK2205
            RCI: LRC376(thrC-1) LRC440(thrC-2) LRC583(thrC-3)
            APE: APE_1488.1 APE_2286
            SSO: SSO0493(thrC-1) SSO0878(thrC-2)
            STO: ST0960 ST1240
            SAI: Saci_1023 Saci_1413
            PAI: PAE2878
STRUCTURES  PDB: 1UIM  1UIN  1V7C  1VB3  2C2B  2C2G  2D1F  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.1
            ExPASy - ENZYME nomenclature database: 4.2.3.1
            ExplorEnz - The Enzyme Database: 4.2.3.1
            ERGO genome analysis and discovery system: 4.2.3.1
            BRENDA, the Enzyme Database: 4.2.3.1
            CAS: 9023-97-6
///
ENTRY       EC 4.2.3.2                  Enzyme
NAME        ethanolamine-phosphate phospho-lyase;
            O-phosphoethanolamine-phospholyase;
            amino alcohol O-phosphate phospholyase;
            O-phosphorylethanol-amine phospho-lyase;
            ethanolamine-phosphate phospho-lyase (deaminating)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     ethanolamine-phosphate phosphate-lyase (deaminating;
            acetaldehyde-forming)
REACTION    ethanolamine phosphate + H2O = acetaldehyde + NH3 + phosphate
            [RN:R00748]
ALL_REAC    R00748
SUBSTRATE   ethanolamine phosphate [CPD:C00346];
            H2O [CPD:C00001]
PRODUCT     acetaldehyde [CPD:C00084];
            NH3 [CPD:C00014];
            phosphate [CPD:C00009]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also acts on D(or
            L)-1-aminopropan-2-ol O-phosphate.
REFERENCE   1  [PMID:5498429]
  AUTHORS   Fleshood HL, Pitot HC.
  TITLE     The metabolism of O-phosphorylethanolamine in animal tissues. I.
            O-phosphorylethanolamine phospho-lyase: partial purification and
            characterization.
  JOURNAL   J. Biol. Chem. 245 (1970) 4414-20.
  ORGANISM  rabbit, rat [GN:rno]
REFERENCE   2  [PMID:4357716]
  AUTHORS   Jones A, Faulkner A, Turner JM.
  TITLE     Microbial metabolism of amino alcohols. Metabolism of ethanolamine
            and 1-aminopropan-2-ol in species of Erwinia and the roles of amino
            alcohol kinase and amino alcohol o-phosphate phospho-lyase in
            aldehyde formation.
  JOURNAL   Biochem. J. 134 (1973) 959-68.
  ORGANISM  Erwinia carotovora [GN:eca], Erwinia ananas, Erwinia milletiae
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.2
            ExPASy - ENZYME nomenclature database: 4.2.3.2
            ExplorEnz - The Enzyme Database: 4.2.3.2
            ERGO genome analysis and discovery system: 4.2.3.2
            BRENDA, the Enzyme Database: 4.2.3.2
            CAS: 37290-88-3
///
ENTRY       EC 4.2.3.3                  Enzyme
NAME        methylglyoxal synthase;
            methylglyoxal synthetase;
            glycerone-phosphate phospho-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     glycerone-phosphate phosphate-lyase (methylglyoxal-forming)
REACTION    glycerone phosphate = methylglyoxal + phosphate [RN:R01016]
ALL_REAC    R01016
SUBSTRATE   glycerone phosphate [CPD:C00111]
PRODUCT     methylglyoxal [CPD:C00546];
            phosphate [CPD:C00009]
COMMENT     Does not act on D-glyceraldehyde 3-phosphate.
REFERENCE   1  [PMID:11945504]
  AUTHORS   Cooper RA, Anderson A.
  TITLE     The formation and catabolism of methylglyoxal during glycolysis in
            Escherichia coli.
  JOURNAL   FEBS. Lett. 11 (1970) 273-276.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:11945670]
  AUTHORS   Hopper DJ, Cooper RA.
  TITLE     The regulation of Escherichia coli methylglyoxal synthase; a new
            control site in glycolysis?
  JOURNAL   FEBS. Lett. 13 (1971) 213-216.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:7240200]
  AUTHORS   Ray S, Ray M.
  TITLE     Isolation of methylglyoxal synthase from goat liver.
  JOURNAL   J. Biol. Chem. 256 (1981) 6230-3.
  ORGANISM  goat
PATHWAY     PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K01734  methylglyoxal synthase
GENES       ECO: b0963(mgsA)
            ECJ: JW5129(mgsA)
            ECE: Z1314(mgsA)
            ECS: ECs1047
            ECC: c1100(mgsA)
            ECI: UTI89_C1029(mgsA)
            ECP: ECP_0969
            ECV: APECO1_68(mgsA)
            ECW: EcE24377A_1078(mgsA)
            ECX: EcHS_A1072
            STY: STY1098(mgsA)
            STT: t1844(mgsA)
            SPT: SPA1774(mgsA)
            SEC: SC1028(mgsA)
            STM: STM1076(mgsA)
            YPE: YPO1441(mgsA)
            YPK: y2729(mgsA)
            YPM: YP_1332(mgsA)
            YPA: YPA_0733
            YPN: YPN_2538
            YPP: YPDSF_1533
            YPS: YPTB1459(mgsA)
            YPI: YpsIP31758_2535(mgsA)
            SFL: SF0965(mgsA)
            SFX: S1031(mgsA)
            SFV: SFV_0973(mgsA)
            SSN: SSON_0967(mgsA)
            SBO: SBO_2268(mgsA)
            SDY: SDY_0938(mgsA)
            ECA: ECA1757(mgsA)
            PLU: plu1780(mgsA)
            SGL: SG1032
            ENT: Ent638_1475
            SPE: Spro_1760
            HIN: HI1234(mgsA)
            HIT: NTHI1931(mgsA)
            HIQ: CGSHiGG_01835(mgsA)
            HSO: HS_1350(mgsA)
            PMU: PM0394(mgsA)
            MSU: MS0839(mgsA)
            APL: APL_1498(mgsA)
            VCH: VCA0711
            VCO: VC0395_0650(mgsA)
            VVU: VV2_0123
            VVY: VVA0630
            VPA: VPA0673
            VFI: VF1621
            PPR: PBPRA1230(mgsA)
            PFL: PFL_4624(mgsA)
            PMY: Pmen_1310
            PHA: PSHAa2175(mgsA)
            PAT: Patl_0985
            SDE: Sde_1302
            PIN: Ping_0116
            MAQ: Maqu_1906
            CBU: CBU_0853(mgsA)
            CBD: COXBU7E912_0918(mgsA)
            HCH: HCH_02120(mgsA)
            CSA: Csal_1558
            MMW: Mmwyl1_1077
            AHA: AHA_3831(mgsA)
            RSO: RSc2185(mgsA)
            REU: Reut_A2504(mgsA)
            REH: H16_A0932(mgsA)
            RME: Rmet_0792
            BMA: BMA1881(mgsA)
            BMV: BMASAVP1_A1079(mgsA)
            BML: BMA10299_A0788(mgsA)
            BMN: BMA10247_0362(mgsA)
            BXE: Bxe_A3256
            BVI: Bcep1808_2376
            BUR: Bcep18194_A5618(mgsA)
            BCN: Bcen_1679
            BCH: Bcen2424_2291
            BAM: Bamb_2329
            BPS: BPSL1168(mgsA)
            BPM: BURPS1710b_1390(mgsA)
            BPL: BURPS1106A_1244(mgsA)
            BPD: BURPS668_1235(mgsA)
            BTE: BTH_I1018(mgsA)
            RFR: Rfer_4019
            PNA: Pnap_0042
            DDE: Dde_1979
            BBA: Bd3047(mgsA)
            ADE: Adeh_1240
            AFW: Anae109_2526
            SFU: Sfum_2894
            MES: Meso_3595
            SME: SMc02834(mgsA)
            SMD: Smed_3368
            ATU: Atu0185(mgsA)
            ATC: AGR_C_311
            RET: RHE_CH00173(mgsA)
            RLE: RL0183
            BME: BMEII0252
            BMF: BAB2_1009(mgsA)
            BMS: BRA1048(mgsA)
            BMB: BruAb2_0988(mgsA)
            BOV: BOV_A0986(mgsA)
            OAN: Oant_1333
            SIL: SPOA0329(mgsA)
            JAN: Jann_2072
            RRU: Rru_A2068
            ABA: Acid345_2381
            BSU: BG11211(mgsA)
            BHA: BH1681(mgsA)
            BAN: BA1556(mgsA)
            BAR: GBAA1556(mgsA)
            BAA: BA_2074
            BAT: BAS1443
            BCE: BC1533
            BCA: BCE_1662(mgsA)
            BCZ: BCZK1416(mgsA)
            BCY: Bcer98_1257
            BTK: BT9727_1415(mgsA)
            BTL: BALH_1387
            BLI: BL02757(mgsA)
            BLD: BLi02383(mgsA)
            BCL: ABC1917(mgsA)
            BPU: BPUM_1979
            OIH: OB1767
            GKA: GK2184
            LMO: lmo1906
            LMF: LMOf2365_1935(mgsA)
            LIN: lin2020
            LWE: lwe1925(mgsA)
            LSA: LSA1157(mgsA)
            EFA: EF0939(mgsA)
            STH: STH1646
            CAC: CAC1604
            CPE: CPE1009(mgsA)
            CPF: CPF_1265(mgsA)
            CPR: CPR_1077(mgsA)
            CNO: NT01CX_1696(mgsA)
            CTH: Cthe_0095
            CDF: CD1153(mgsA)
            CBE: Cbei_0026
            AMT: Amet_2297
            CHY: CHY_0470(mgsA)
            DRM: Dred_2527
            CSC: Csac_1874
            TTE: TTE0906(mgsA)
            MTA: Moth_1275
            ACE: Acel_1628
            BBU: BB0364
            BGA: BG0363
            BAF: BAPKO_0372
            LIL: LA0909(mgsA)
            LIC: LIC12733(mgsA)
            LBJ: LBJ_0865(mgsA)
            LBL: LBL_0886(mgsA)
            SYN: sll0036
            SYD: Syncc9605_2517
            GVI: gll3519
            ANA: all1876
            AVA: Ava_4772
            TER: Tery_3603
            BTH: BT_1098 BT_2150
            BFR: BF3853
            BFS: BF3624(mgsA)
            GFO: GFO_1642(mgsA)
            FJO: Fjoh_4588
            PLT: Plut_1001
            DET: DET0137(mgsA)
            DEH: cbdb_A160(mgsA)
            DEB: DehaBAV1_0233 DehaBAV1_1322
            RRS: RoseRS_1706
            RCA: Rcas_3178
            DGE: Dgeo_0241
            TTH: TTC1443
            TTJ: TTHA1794
            TMA: TM1185
            TPT: Tpet_1568
            TME: Tmel_0524
            FNO: Fnod_1481
            HMA: rrnAC2162(mgsA)
            HWA: HQ1527A(mgsA)
STRUCTURES  PDB: 1B93  1EGH  1IK4  1S89  1S8A  1VMD  1WO8  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.3
            ExPASy - ENZYME nomenclature database: 4.2.3.3
            ExplorEnz - The Enzyme Database: 4.2.3.3
            ERGO genome analysis and discovery system: 4.2.3.3
            BRENDA, the Enzyme Database: 4.2.3.3
            CAS: 37279-01-9
///
ENTRY       EC 4.2.3.4                  Enzyme
NAME        3-dehydroquinate synthase;
            5-dehydroquinate synthase;
            5-dehydroquinic acid synthetase;
            dehydroquinate synthase;
            3-dehydroquinate synthetase;
            3-deoxy-arabino-heptulosonate-7-phosphate phosphate-lyase
            (cyclizing);
            3-deoxy-arabino-heptulonate-7-phosphate phosphate-lyase (cyclizing)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     3-deoxy-arabino-heptulonate-7-phosphate phosphate-lyase (cyclizing;
            3-dehydroquinate-forming)
REACTION    3-deoxy-arabino-heptulonate 7-phosphate = 3-dehydroquinate +
            phosphate [RN:R03083]
ALL_REAC    R03083
SUBSTRATE   3-deoxy-arabino-heptulonate 7-phosphate [CPD:C04691]
PRODUCT     3-dehydroquinate [CPD:C00944];
            phosphate [CPD:C00009]
COFACTOR    Cobalt [CPD:C00175]
COMMENT     Requires Co2+ and bound NAD+. The hydrogen atoms on C-7 of the
            substrate are retained on C-2 of the product.
REFERENCE   1  [PMID:5275368]
  AUTHORS   Rotenberg SL, Sprinson DB.
  TITLE     Mechanism and stereochemistry of 5-dehydroquinate synthetase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 67 (1970) 1669-72.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:14085358]
  AUTHORS   SRINIVASAN PR, ROTHSCHILD J, SPRINSON DB.
  TITLE     THE ENZYMIC CONVERSION OF 3-DEOXY-D-ARABINO-HEPTULOSONIC ACID
            7-PHOSPHATE TO 5-DEHYDROQUINATE.
  JOURNAL   J. Biol. Chem. 238 (1963) 3176-82.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:2514789]
  AUTHORS   Bender SL, Mehdi S, Knowles JR.
  TITLE     Dehydroquinate synthase: the role of divalent metal cations and of
            nicotinamide adenine dinucleotide in catalysis.
  JOURNAL   Biochemistry. 28 (1989) 7555-60.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:9685163]
  AUTHORS   Carpenter EP, Hawkins AR, Frost JW, Brown KA.
  TITLE     Structure of dehydroquinate synthase reveals an active site capable
            of multistep catalysis.
  JOURNAL   Nature. 394 (1998) 299-302.
  ORGANISM  Aspergillus nidulans [GN:ani]
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K01735  3-dehydroquinate synthase
GENES       ATH: AT5G66120
            CME: CMK011C
            SCE: YDR127W(ARO1)
            AGO: AGOS_AGR066W
            CAL: CaO19_4704(CaO19.4704)
            SPO: SPAC1834.02(aro1)
            ANI: AN6403.2
            AFM: AFUA_1G13740
            AOR: AO090012000502
            CNE: CNB01990
            UMA: UM01603.1 UM03607.1
            ECO: b3389(aroB)
            ECJ: JW3352(aroB)
            ECE: Z4742(aroB)
            ECS: ECs4231
            ECC: c4159(aroB)
            ECI: UTI89_C3887(aroB)
            ECP: ECP_3475
            ECV: APECO1_3074(aroB)
            ECW: EcE24377A_3859(aroB)
            ECX: EcHS_A3585
            STY: STY4310(aroB)
            STT: t4020(aroB)
            SPT: SPA3351(aroB)
            SEC: SC3418(aroB)
            STM: STM3486(aroB)
            YPE: YPO0152(aroB)
            YPK: y3934(aroB)
            YPM: YP_0154(aroB)
            YPA: YPA_3317
            YPN: YPN_3913
            YPP: YPDSF_0079
            YPS: YPTB3749(aroB)
            YPI: YpsIP31758_3965(aroB)
            SFL: SF3407(aroB)
            SFX: S4355(aroB)
            SFV: SFV_3394(aroB)
            SSN: SSON_3520(aroB)
            SBO: SBO_3376(aroB)
            SDY: SDY_3690(aroB)
            ECA: ECA4092(aroB)
            PLU: plu0089(aroB)
            BUC: BU538(aroB)
            BAS: BUsg519(aroB)
            BAB: bbp480(aroB)
            BCC: BCc_352(aroB)
            SGL: SG2308
            KPN: KPN_03760(aroB)
            BFL: Bfl571(aroB)
            BPN: BPEN_591(aroB)
            HIN: HI0208(aroB)
            HIT: NTHI0306(aroB)
            HDU: HD0422(aroB)
            HSO: HS_1114(aroB)
            PMU: PM1223(aroB)
            MSU: MS1968(aroB)
            APL: APL_0193(aroB)
            XFA: XF1334
            XFT: PD0581(aroB)
            XCC: XCC2842(aroB)
            XCB: XC_1268
            XCV: XCV3161(aroB)
            XAC: XAC3011(aroB)
            XOO: XOO1243(aroB)
            XOM: XOO_1143(XOO1143)
            VCH: VC2628
            VCO: VC0395_A2205(aroB)
            VVU: VV1_1383
            VVY: VV2988
            VPA: VP2744
            VFI: VF2291
            PPR: PBPRA0281
            PAE: PA5038(aroB)
            PAU: PA14_66600(aroB)
            PAP: PSPA7_5775(aroB)
            PPU: PP_5078(aroB)
            PST: PSPTO_5126(aroB)
            PSB: Psyr_0409
            PSP: PSPPH_0396(aroB)
            PFL: PFL_0451(aroB) PFL_5540
            PFO: Pfl_0411
            PEN: PSEEN0335(aroB) PSEEN2474 PSEEN2641
            PAR: Psyc_1877(aroB)
            PCR: Pcryo_2167
            PRW: PsycPRwf_0401
            ACI: ACIAD3353(aroB)
            ACB: A1S_3187
            SON: SO_0287(aroB)
            SDN: Sden_0262
            SFR: Sfri_0376
            SAZ: Sama_3367
            SBL: Sbal_4112
            SLO: Shew_0214
            SHE: Shewmr4_3697
            SHM: Shewmr7_0248
            SHN: Shewana3_3893
            SHW: Sputw3181_3846
            ILO: IL2473(aroB)
            CPS: CPS_0473(aroB)
            PHA: PSHAa2714(aroB)
            PAT: Patl_0665
            SDE: Sde_2685
            PIN: Ping_0164
            MAQ: Maqu_0832
            CBU: CBU_1893(aroB)
            CBD: COXBU7E912_0125(aroB)
            LPN: lpg0933(aroB)
            LPF: lpl0964(aroB)
            LPP: lpp0995(aroB)
            MCA: MCA0331(aroB)
            FTU: FTT1154c(aroB)
            FTF: FTF1154c(aroB)
            FTW: FTW_1193(aroB)
            FTL: FTL_0802
            FTH: FTH_0795(aroB)
            FTA: FTA_0847(aroB)
            FTN: FTN_1135(aroB)
            TCX: Tcr_2136
            NOC: Noc_0253
            AEH: Mlg_2762
            HCH: HCH_05967(aroB)
            CSA: Csal_0614
            ABO: ABO_2231(aroB)
            AHA: AHA_3188(aroB)
            DNO: DNO_1084(aroB)
            BCI: BCI_0023(aroB)
            CRP: CRP_028
            RMA: Rmag_0341
            VOK: COSY_0323(aroB)
            NME: NMB1814
            NMA: NMA0647(aroB)
            NMC: NMC0406(aroB)
            NGO: NGO0092(aroB)
            CVI: CV_0827(aroB) CV_2833
            RSO: RSc2969(aroB)
            REU: Reut_A3129
            REH: H16_A3434(aroB)
            RME: Rmet_3266
            BMA: BMA2746(aroB)
            BMV: BMASAVP1_A3207(aroB)
            BML: BMA10299_A1758(aroB)
            BMN: BMA10247_2796(aroB)
            BXE: Bxe_A0360
            BUR: Bcep18194_A3490
            BCN: Bcen_2714
            BCH: Bcen2424_0393
            BAM: Bamb_0312
            BPS: BPSL3168(aroB)
            BPM: BURPS1710b_3728(aroB)
            BPL: BURPS1106A_3757(aroB)
            BPD: BURPS668_3699(aroB)
            BTE: BTH_I3023(aroB)
            BPE: BP3657(aroB)
            BPA: BPP0072(aroB)
            BBR: BB0072(aroB)
            RFR: Rfer_1247 Rfer_2926
            POL: Bpro_0787
            PNA: Pnap_0679
            AAV: Aave_1003
            AJS: Ajs_0735
            VEI: Veis_0016
            MPT: Mpe_A3107
            HAR: HEAR3120(aroB-aroK)
            MMS: mma_3363
            NEU: NE1981(aroB)
            NET: Neut_0381
            NMU: Nmul_A0703
            EBA: ebA2256(aroB)
            AZO: azo3644(aroB)
            DAR: Daro_0216
            TBD: Tbd_0315 Tbd_1885
            MFA: Mfla_2455
            HPY: HP0283(aroB)
            HPJ: jhp0268(aroB)
            HPA: HPAG1_0285
            HHE: HH0882(aroB)
            HAC: Hac_0543(aroB)
            WSU: WS1517(aroB)
            TDN: Tmden_1020
            CJE: Cj1008c(aroB)
            CJR: CJE1088(aroB)
            CJJ: CJJ81176_1026(aroB)
            CJU: C8J_0945(aroB)
            CJD: JJD26997_0781(aroB)
            CFF: CFF8240_0854(aroB)
            CCV: CCV52592_1438(aroB)
            CHA: CHAB381_1074(aroB)
            CCO: CCC13826_0087(aroB)
            ABU: Abu_1125(aroB) Abu_1154
            NIS: NIS_1083(aroB)
            SUN: SUN_1010(aroB)
            GSU: GSU2025(aroB)
            GME: Gmet_0978
            PCA: Pcar_2132
            DVU: DVU0461
            DDE: Dde_3488
            BBA: Bd3497(aroB)
            DPS: DP1473 DP1474
            ADE: Adeh_0188
            AFW: Anae109_0208
            MXA: MXAN_3521
            SAT: SYN_01939
            SFU: Sfum_2494
            PUB: SAR11_0452(aroB)
            MLO: mll3571
            MES: Meso_3065
            SME: SMc00696(aroB)
            SMD: Smed_2564
            ATU: Atu3625(aroB)
            ATC: AGR_L_2401
            RET: RHE_CH03825(aroB)
            RLE: RL4352(aroB)
            BME: BMEI0043
            BMF: BAB1_2029(aroB)
            BMS: BR2028(aroB)
            BMB: BruAb1_2003(aroB)
            BOV: BOV_1950(aroB)
            OAN: Oant_0910
            BJA: bll0187(aroB)
            BRA: BRADO0609
            BBT: BBta_7572(aroB)
            RPA: RPA0503(aroB) RPA4052
            RPB: RPB_0536
            RPC: RPC_0533 RPC_4194
            RPD: RPD_0293
            RPE: RPE_0144
            NWI: Nwi_0396
            NHA: Nham_0491 Nham_0984
            BHE: BH16370(aroB)
            BQU: BQ13280(aroB)
            BBK: BARBAKC583_0037(aroB)
            XAU: Xaut_1633
            CCR: CC_3009
            SIL: SPO1635(aroB)
            SIT: TM1040_1432
            RSP: RSP_2818(aroB)
            RSH: Rsph17029_1478
            RSQ: Rsph17025_1528
            JAN: Jann_2487
            RDE: RD1_3087(aroB)
            PDE: Pden_1283
            MMR: Mmar10_2274
            HNE: HNE_0082(aroB)
            ZMO: ZMO0593(aroB)
            NAR: Saro_1899
            SAL: Sala_1800
            SWI: Swit_0007
            ELI: ELI_04965
            GOX: GOX1788
            GBE: GbCGDNIH1_0616
            RRU: Rru_A3741
            MAG: amb0135 amb3925
            MGM: Mmc1_2319
            ABA: Acid345_2249
            SUS: Acid_7344
            BSU: BG10285(aroB)
            BHA: BH1657(aroB)
            BAN: BA1538(aroB)
            BAR: GBAA1538(aroB)
            BAA: BA_2058
            BAT: BAS1427
            BCE: BC1517
            BCA: BCE_1644(aroB)
            BCZ: BCZK1399(aroB)
            BTK: BT9727_1399(aroB)
            BLI: BL02777(aroBA)
            BLD: BLi02405(aroB)
            BCL: ABC1893(aroB)
            BPU: BPUM_2001
            OIH: OB1784(aroB)
            GKA: GK2206
            SAU: SA1298(aroB)
            SAV: SAV1465(aroB)
            SAM: MW1355(aroB)
            SAR: SAR1476(aroB)
            SAS: SAS1408
            SAC: SACOL1505(aroB)
            SAB: SAB1329c(aroB)
            SAA: SAUSA300_1356(aroB)
            SAO: SAOUHSC_01482
            SAJ: SaurJH9_1524
            SAH: SaurJH1_1553
            SEP: SE1154
            SER: SERP1035(aroB)
            SHA: SH1447(aroB)
            SSP: SSP1279
            LMO: lmo1927(aroB)
            LMF: LMOf2365_1956(aroB)
            LIN: lin2041(aroB)
            LWE: lwe1953(aroB)
            LLA: L0060(aroB)
            LLC: LACR_1920
            LLM: llmg_1938(aroB)
            SPY: SPy_1577(aroB)
            SPZ: M5005_Spy_1298(aroB)
            SPM: spyM18_1586(aroB)
            SPG: SpyM3_1280(aroB)
            SPS: SPs0582
            SPH: MGAS10270_Spy1413(aroB)
            SPI: MGAS10750_Spy1407(aroB)
            SPJ: MGAS2096_Spy1317(aroB)
            SPK: MGAS9429_Spy1292(aroB)
            SPF: SpyM50557(aroB)
            SPA: M6_Spy1316
            SPB: M28_Spy1339(aroB)
            SPN: SP_1375
            SPR: spr1233(aroB)
            SPD: SPD_1209(aroB)
            SAG: SAG1378(aroB)
            SAN: gbs1448(aroB)
            SAK: SAK_1411(aroB)
            SMU: SMU.779(aroB)
            STC: str0640(aroB)
            STL: stu0640(aroB)
            SSA: SSA_1468(aroB)
            SGO: SGO_1373(aroB)
            LPL: lp_1086(aroB)
            LSA: LSA0894(aroB)
            EFA: EF1563(aroB)
            STH: STH1948
            CAC: CAC0894(aroB)
            CPE: CPE0695(aroB)
            CPF: CPF_0688(aroB)
            CPR: CPR_0689(aroB)
            CTC: CTC01620
            CNO: NT01CX_0625(aroB)
            CDF: CD1833(aroB)
            CBO: CBO1470(aroB) CBO2145(aroB)
            CBA: CLB_1495(aroB)
            CBH: CLC_1507(aroB)
            CBF: CLI_1554(aroB)
            CBE: Cbei_4576
            CKL: CKL_0786(aroB)
            AMT: Amet_0650
            CHY: CHY_0629(aroKB)
            DSY: DSY2390
            CSC: Csac_1913
            TTE: TTE1011(aroB)
            MTA: Moth_1555
            MTU: Rv2538c(aroB)
            MTC: MT2613(aroB)
            MBO: Mb2567c(aroB)
            MBB: BCG_2560c(aroB)
            MLE: ML0518(aroB)
            MPA: MAP1093(aroB)
            MAV: MAV_3415(aroB)
            MSM: MSMEG_3033(aroB)
            MVA: Mvan_2647
            MGI: Mflv_3756
            MMC: Mmcs_2354
            MKM: Mkms_2401
            MJL: Mjls_2395
            CGL: NCgl1559(aroB)
            CGB: cg1827(aroB)
            CEF: CE1740(aroB)
            CDI: DIP1343(aroB)
            CJK: jk1031(aroB)
            NFA: nfa36370(aroB)
            RHA: RHA1_ro07142(aroB)
            SCO: SCO1494(aroB)
            SMA: SAV6856(aroB)
            TWH: TWT370(aroB)
            TWS: TW399(aroB)
            LXX: Lxx10970(aroB)
            CMI: CMM_1796(aroB)
            ART: Arth_2272
            AAU: AAur_2275(aroB)
            PAC: PPA1184
            NCA: Noca_2414
            TFU: Tfu_1092(aroB)
            FRA: Francci3_0434 Francci3_2069 Francci3_3207 Francci3_4206
            FAL: FRAAL0919(aroB) FRAAL5245(aroB)
            ACE: Acel_1307
            SEN: SACE_2067(aroB) SACE_2868(shnQ) SACE_5077
            STP: Strop_1847 Strop_2345
            BLO: BL0877(aroB)
            RXY: Rxyl_1459
            FNU: FN0871
            RBA: RB1898(aroB) RB6147(aroB)
            CTR: CT369(aroB)
            CTA: CTA_0401(aroB)
            CMU: TC0648
            CPN: CPn1036(aroB)
            CPA: CP0816
            CPJ: CPj1036(aroB)
            CPT: CpB1076
            CCA: CCA00726(aroB)
            CAB: CAB693(aroB)
            CFE: CF0290(aroB)
            PCU: pc0073(aroB)
            TDE: TDE0104
            LIL: LB086(aroB)
            LIC: LIC20068(aroB)
            LBJ: LBJ_2109(aroB)
            LBL: LBL_0942(aroB)
            SYN: slr2130(aroB)
            SYW: SYNW1310(aroB)
            SYC: syc0996_d
            SYF: Synpcc7942_0525
            SYD: Syncc9605_1450
            SYE: Syncc9902_1050
            SYG: sync_1430(aroB)
            SYR: SynRCC307_1419(aroB)
            SYX: SynWH7803_1204(aroB)
            CYA: CYA_1866(aroB)
            CYB: CYB_1570(aroB)
            TEL: tlr0784(aroB)
            GVI: glr2513(aroB)
            ANA: all0417(aroB) alr1924(aroB)
            AVA: Ava_3858 Ava_4386
            PMA: Pro1009(aroB)
            PMM: PMM0682(aroB)
            PMT: PMT0667(aroB)
            PMN: PMN2A_0116
            PMI: PMT9312_0682
            PMB: A9601_07371(aroB)
            PMC: P9515_07551(aroB)
            PMF: P9303_01431 P9303_15571(aroB)
            PMG: P9301_07351(aroB)
            PMH: P9215_07671
            PME: NATL1_07421(aroB)
            TER: Tery_2977 Tery_5008
            BTH: BT_3975
            BFR: BF0743
            BFS: BF0672(aroB)
            PGI: PG1247(aroB)
            SRU: SRU_1526(aroB)
            CHU: CHU_0718(aroB)
            GFO: GFO_1492(aroB)
            FJO: Fjoh_2812
            FPS: FP1707(aroB)
            CTE: CT1406(aroB)
            CCH: Cag_1219
            PVI: Cvib_1226
            PLT: Plut_1407
            DET: DET0467(aroB)
            DEH: cbdb_A351(aroB) cbdb_A431(aroB)
            RRS: RoseRS_4545
            RCA: Rcas_0093
            DRA: DR_0777
            DGE: Dgeo_1732 Dgeo_2474
            TTH: TTC1020
            TTJ: TTHA1386
            AAE: aq_1922
            TMA: TM0348
            TPT: Tpet_0572
            MJA: MJ1249
            MMP: MMP0006
            MAC: MA4592
            MBA: Mbar_A0921
            MMA: MM_1272
            MBU: Mbur_2000
            MHU: Mhun_1034
            MTH: MTH580
            MST: Msp_0090
            MSI: Msm_0055
            MKA: MK1408
            AFU: AF0229
            HMA: rrnAC1879(aroB)
            HWA: HQ1155A(aroB)
            NPH: NP2238A
            TAC: Ta0285
            TVO: TVN1316
            PTO: PTO0599
            PAB: PAB0298(aroB)
            PFU: PF1691
            TKO: TK0267
            RCI: RRC152(aroB)
            APE: APE_0579
            IHO: Igni_0018
            SSO: SSO0305(aroB)
            STO: ST2272
            SAI: Saci_0184(aroB)
            MSE: Msed_1875
            PAI: PAE1926
            PIS: Pisl_1774
            PCL: Pcal_0895
            PAS: Pars_2111
STRUCTURES  PDB: 1NR5  1NRX  1NUA  1NVA  1NVB  1NVD  1NVE  1NVF  1SG6  1UJN  
                 1XAG  1XAH  1XAI  1XAJ  1XAL  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.4
            ExPASy - ENZYME nomenclature database: 4.2.3.4
            ExplorEnz - The Enzyme Database: 4.2.3.4
            ERGO genome analysis and discovery system: 4.2.3.4
            BRENDA, the Enzyme Database: 4.2.3.4
            CAS: 37211-77-1
///
ENTRY       EC 4.2.3.5                  Enzyme
NAME        chorismate synthase;
            5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase
            (chorismate-forming)
REACTION    5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
            [RN:R01714]
ALL_REAC    R01714
SUBSTRATE   5-O-(1-carboxyvinyl)-3-phosphoshikimate [CPD:C01269]
PRODUCT     chorismate [CPD:C00251];
            phosphate [CPD:C00009]
COMMENT     Requires FMN. The reaction goes via a radical mechanism that
            involves reduced FMN and its semiquinone (FMNH(.)). Shikimate is
            numbered so that the double-bond is between C-1 and C-2, but some
            earlier papers numbered the ring in the reverse direction.
REFERENCE   1  [PMID:4146266]
  AUTHORS   Gaertner FH, Cole KW.
  TITLE     Properties of chorismate synthase in Neurospora crassa.
  JOURNAL   J. Biol. Chem. 248 (1973) 4602-9.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   2  [PMID:4289188]
  AUTHORS   Morell H, Clark MJ, Knowles PF, Sprinson DB.
  TITLE     The enzymic synthesis of chorismic and prephenic acids from
            3-enolpyruvylshikimic acid 5-phosphate.
  JOURNAL   J. Biol. Chem. 242 (1967) 82-90.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:4155270]
  AUTHORS   Welch GR, Cole KW, Gaertner FH.
  TITLE     Chorismate synthase of Neurospora crassa: a flavoprotein.
  JOURNAL   Arch. Biochem. Biophys. 165 (1974) 505-18.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   4  [PMID:8703965]
  AUTHORS   Bornemann S, Lowe DJ, Thorneley RN.
  TITLE     The transient kinetics of Escherichia coli chorismate synthase:
            substrate consumption, product formation, phosphate dissociation,
            and characterization of a flavin intermediate.
  JOURNAL   Biochemistry. 35 (1996) 9907-16.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:11034781]
  AUTHORS   Bornemann S, Theoclitou ME, Brune M, Webb MR, Thorneley RN, Abell C.
  TITLE     A Secondary beta Deuterium Kinetic Isotope Effect in the Chorismate
            Synthase Reaction.
  JOURNAL   BIO-ORGANIC. CHEMISTRY. 28 (2000) 191-204.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:10956653]
  AUTHORS   Osborne A, Thorneley RN, Abell C, Bornemann S.
  TITLE     Studies with substrate and cofactor analogues provide evidence for a
            radical mechanism in the chorismate synthase reaction.
  JOURNAL   J. Biol. Chem. 275 (2000) 35825-30.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K01736  chorismate synthase
GENES       OSA: 4332286
            CME: CME064C
            SCE: YGL148W(ARO2)
            AGO: AGOS_ADL287C
            PIC: PICST_90939(AROC)
            CGR: CAGL0E05016g
            SPO: SPCC1223.14
            ANI: AN5731.2
            AFM: AFUA_1G06940
            AOR: AO090003000081
            CNE: CNH02650
            UMA: UM01402.1
            PFA: PFF1105c
            TET: TTHERM_00079070
            ECO: b2329(aroC)
            ECJ: JW2326(aroC)
            ECE: Z3592(aroC)
            ECS: ECs3213
            ECC: c2875(aroC)
            ECI: UTI89_C2614(aroC)
            ECP: ECP_2368
            ECV: APECO1_4235(aroC)
            ECW: EcE24377A_2624(aroC)
            ECX: EcHS_A2481
            STY: STY2616(aroC)
            STT: t0480(aroC)
            SPT: SPA0480(aroC)
            SEC: SC2386(aroC)
            STM: STM2384(aroC)
            YPE: YPO2751(aroC)
            YPK: y1585(aroC)
            YPM: YP_2412(aroC)
            YPA: YPA_2092
            YPN: YPN_2195
            YPP: YPDSF_2009
            YPS: YPTB2632(aroC)
            YPI: YpsIP31758_1405(aroC)
            YEN: YE1281(aroC)
            SFL: SF2405(aroC)
            SFX: S2540(aroC)
            SFV: SFV_2398(aroC)
            SSN: SSON_2387(aroC)
            SBO: SBO_2366(aroC)
            SDY: SDY_2528(aroC)
            ECA: ECA3069(aroC)
            PLU: plu3189(aroC)
            BUC: BU097(aroC)
            BAS: BUsg090(aroC)
            BAB: bbp091(aroC)
            BCC: BCc_061(aroC)
            SGL: SG1627
            ENT: Ent638_2877
            SPE: Spro_3374
            BFL: Bfl500(aroC)
            BPN: BPEN_516(aroC)
            HIN: HI0196(aroC)
            HIT: NTHI0292(aroC)
            HDU: HD1274(aroC)
            HSO: HS_1205(aroC)
            PMU: PM0359(aroC)
            MSU: MS0866(aroC)
            APL: APL_0748(aroC)
            ASU: Asuc_0966
            XFA: XF1369
            XFT: PD0607(aroC)
            XCC: XCC2551(aroC)
            XCB: XC_1567
            XCV: XCV2877(aroC)
            XAC: XAC2725(aroC)
            XOO: XOO3261(aroC)
            XOM: XOO_3089(XOO3089)
            VCH: VC2116
            VCO: VC0395_A1699(aroC)
            VVU: VV1_1981
            VVY: VV2434
            VPA: VP2202
            VFI: VF1805
            PPR: PBPRA2714
            PAE: PA1681(aroC)
            PAU: PA14_42760(aroC)
            PAP: PSPA7_3591(aroC)
            PPU: PP_1830(aroC)
            PPF: Pput_3880
            PST: PSPTO_2043(aroC)
            PSB: Psyr_1853
            PSP: PSPPH_1812(aroC)
            PFL: PFL_4348(aroC)
            PFO: Pfl_1722
            PEN: PSEEN1529(aroC)
            PMY: Pmen_1882
            PAR: Psyc_1455(aroC)
            PCR: Pcryo_1635
            PRW: PsycPRwf_0929
            ACI: ACIAD2028(aroC)
            SDN: Sden_1537
            SFR: Sfri_2667
            SAZ: Sama_2159
            SBL: Sbal_2752
            SBM: Shew185_2769
            SLO: Shew_2416
            SPC: Sputcn32_2451
            SSE: Ssed_1638
            SPL: Spea_2588
            SHE: Shewmr4_1416
            SHM: Shewmr7_1481
            SHN: Shewana3_1469
            SHW: Sputw3181_1557
            ILO: IL0892(aroC)
            CPS: CPS_3150(aroC)
            PHA: PSHAa0983(aroC)
            PAT: Patl_1541
            SDE: Sde_2091
            PIN: Ping_1018
            MAQ: Maqu_1568
            CBU: CBU_0874(aroC)
            CBD: COXBU7E912_0938(aroC)
            LPN: lpg2303
            LPF: lpl2222(aroC)
            LPP: lpp2251(aroC)
            MCA: MCA0702(aroC)
            FTU: FTT0876c(aroC)
            FTF: FTF0876c(aroC)
            FTW: FTW_1304(aroC)
            FTL: FTL_0377
            FTH: FTH_0370
            FTA: FTA_0400(aroC)
            FTN: FTN_0402(aroC)
            TCX: Tcr_1538
            NOC: Noc_2938
            AEH: Mlg_1226
            HHA: Hhal_1814
            HCH: HCH_02421(aroC)
            CSA: Csal_2466
            ABO: ABO_1473(aroC)
            MMW: Mmwyl1_2244
            AHA: AHA_2355(aroC)
            DNO: DNO_1072(aroC)
            BCI: BCI_0361(aroC)
            CRP: CRP_079
            RMA: Rmag_0430
            VOK: COSY_0399(aroC)
            NME: NMB1680
            NMA: NMA1939(aroC)
            NMC: NMC1598(aroC)
            NGO: NGO1331(aroC)
            CVI: CV_1187(aroC)
            RSO: RSc1566(aroC)
            REU: Reut_A1257
            REH: H16_A1317(aroC)
            RME: Rmet_1138
            BMA: BMA0946(aroC)
            BMV: BMASAVP1_A1481(aroC)
            BML: BMA10299_A0401(aroC)
            BMN: BMA10247_0762(aroC)
            BXE: Bxe_A1360
            BVI: Bcep1808_1421
            BUR: Bcep18194_A4605
            BCN: Bcen_0978
            BCH: Bcen2424_1460
            BAM: Bamb_1341
            BPS: BPSL1962(aroC)
            BPM: BURPS1710b_1867(aroC)
            BPL: BURPS1106A_1713(aroC)
            BPD: BURPS668_1689(aroC)
            BTE: BTH_I2614(aroC)
            PNU: Pnuc_0977
            BPE: BP1462(aroC)
            BPA: BPP1923(aroC)
            BBR: BB2111(aroC)
            RFR: Rfer_3161
            POL: Bpro_1842
            PNA: Pnap_2745
            AAV: Aave_2995
            AJS: Ajs_1658
            VEI: Veis_2580
            MPT: Mpe_A1425
            HAR: HEAR1213(aroC)
            MMS: mma_2174
            NEU: NE1877(aroC)
            NET: Neut_1957
            NMU: Nmul_A1958
            EBA: ebA4753(aroC)
            AZO: azo1036(aroC)
            DAR: Daro_0858
            TBD: Tbd_0666
            MFA: Mfla_2137
            HPY: HP0663(aroC)
            HPJ: jhp0608(aroC)
            HPA: HPAG1_0648
            HHE: HH0700(aroC)
            HAC: Hac_0848(aroC)
            WSU: WS1897(aroC)
            TDN: Tmden_2023
            CJE: Cj1634c(aroC)
            CJR: CJE1806(aroC)
            CJJ: CJJ81176_1625(aroC)
            CJU: C8J_1536(aroC)
            CJD: JJD26997_1994(aroC)
            CFF: CFF8240_1741(aroC)
            CCV: CCV52592_2064(aroC)
            CHA: CHAB381_0114(aroC)
            ABU: Abu_1614(aroC)
            NIS: NIS_0216(aroC)
            SUN: SUN_2260(aroC)
            GSU: GSU2027(aroC)
            GME: Gmet_0976
            GUR: Gura_1818
            PCA: Pcar_2133
            PPD: Ppro_2028
            DVU: DVU0894(aroC)
            DVL: Dvul_2090
            DDE: Dde_2726
            BBA: Bd3493(aroC)
            DPS: DP3058
            ADE: Adeh_0186
            AFW: Anae109_0206
            MXA: MXAN_3522(aroC)
            SAT: SYN_01934
            SFU: Sfum_0041
            PUB: SAR11_0612(aroC)
            MLO: mlr7461
            MES: Meso_0730
            PLA: Plav_0785
            SME: SMc00007(aroC)
            SMD: Smed_0515
            ATU: Atu0754(aroC)
            ATC: AGR_C_1368
            RET: RHE_CH00935(aroC)
            RLE: RL1007(aroC)
            BME: BMEI1506
            BMF: BAB1_0454(aroC)
            BMS: BR0428(aroC)
            BMB: BruAb1_0450(aroC)
            BOV: BOV_0435(aroC)
            OAN: Oant_0539
            BJA: blr2631(aroC)
            BRA: BRADO2153(aroC)
            BBT: BBta_2470(aroC)
            RPA: RPA1201(aroC)
            RPB: RPB_1212
            RPC: RPC_1142
            RPD: RPD_1314
            RPE: RPE_4589
            NWI: Nwi_0629
            NHA: Nham_0770
            BHE: BH04320(aroC)
            BQU: BQ03510(aroC)
            BBK: BARBAKC583_0397(aroC)
            XAU: Xaut_4138
            CCR: CC_3154
            SIL: SPO0267(aroC)
            SIT: TM1040_2819
            RSP: RSP_1389(aroC)
            RSH: Rsph17029_0057
            RSQ: Rsph17025_2797
            JAN: Jann_0331
            RDE: RD1_0556(aroC)
            PDE: Pden_4332
            MMR: Mmar10_0855
            HNE: HNE_0823(aroC)
            ZMO: ZMO1693(aroC)
            NAR: Saro_0009
            SAL: Sala_0659
            SWI: Swit_4770
            ELI: ELI_10445
            GOX: GOX1991
            GBE: GbCGDNIH1_0224
            ACR: Acry_1320
            RRU: Rru_A2623
            MAG: amb1590
            MGM: Mmc1_3619
            ABA: Acid345_4288
            SUS: Acid_2745
            BSU: BG10284(aroF)
            BHA: BH1656(aroF)
            BAN: BA1537(aroF-1) BA2956(aroF-2)
            BAR: GBAA1537(aroF-1) GBAA2956(aroF-2)
            BAA: BA_2057 BA_3465
            BAT: BAS1426 BAS2747
            BCE: BC1516 BC2941
            BCA: BCE_1643(aroF) BCE_2997(aroF)
            BCZ: BCZK1398(aroC) BCZK2676(aroF)
            BCY: Bcer98_1239
            BTK: BT9727_1398(aroC) BT9727_2697(aroF)
            BLI: BL02779(aroF)
            BLD: BLi02406(aroF)
            BCL: ABC1892(aroF)
            BPU: BPUM_2002
            OIH: OB1785(aroF)
            GKA: GK2207(aroF)
            SAU: SA1299(aroC)
            SAV: SAV1466(aroC)
            SAM: MW1356(aroC)
            SAR: SAR1477(aroC)
            SAS: SAS1409
            SAC: SACOL1506(aroC)
            SAB: SAB1330c(aroC)
            SAA: SAUSA300_1357(aroC)
            SAO: SAOUHSC_01483
            SAJ: SaurJH9_1525
            SAH: SaurJH1_1554
            SEP: SE1155
            SER: SERP1036(aroC)
            SHA: SH1446(aroC)
            SSP: SSP1278
            LMO: lmo1928(aroF)
            LMF: LMOf2365_1957(aroC)
            LIN: lin2042(aroF)
            LWE: lwe1954(aroC)
            LLA: L0059(aroC)
            LLC: LACR_1916
            LLM: llmg_1934(aroC)
            SPY: SPy_0810(aroF)
            SPZ: M5005_Spy_0625(aroF)
            SPM: spyM18_0872(aroC)
            SPG: SpyM3_0544(aroF)
            SPS: SPs1310
            SPH: MGAS10270_Spy0680(aroF)
            SPI: MGAS10750_Spy0712(aroF)
            SPJ: MGAS2096_Spy0690(aroF)
            SPK: MGAS9429_Spy0680(aroF)
            SPF: SpyM51182(aroC)
            SPA: M6_Spy0642
            SPB: M28_Spy0604(aroF)
            SPN: SP_1374
            SPR: spr1232(aroC)
            SPD: SPD_1208(aroC)
            SAG: SAG1377(aroC)
            SAN: gbs1447(aroC)
            SAK: SAK_1410(aroC)
            SMU: SMU.780(aroC)
            STC: str0641(aroF)
            STL: stu0641(aroF)
            SSA: SSA_1467(aroC)
            SGO: SGO_1372(aroC)
            LPL: lp_2037(aroF)
            EFA: EF1564(aroC)
            STH: STH1950
            CAC: CAC0896(aroC)
            CPE: CPE0697(aroC)
            CPF: CPF_0690(aroC)
            CPR: CPR_0691(aroC)
            CTC: CTC02104
            CNO: NT01CX_0623(aroC)
            CTH: Cthe_0732
            CDF: CD1835(aroC)
            CBO: CBO3015
            CBA: CLB_3040(aroC)
            CBH: CLC_2912(aroC)
            CBF: CLI_3069(aroC)
            CBE: Cbei_4574
            CKL: CKL_0788(aroC)
            AMT: Amet_0649
            CHY: CHY_0624(aroC)
            DSY: DSY2392
            DRM: Dred_1019
            SWO: Swol_0527
            CSC: Csac_1844
            TTE: TTE1711(aroC)
            MTA: Moth_1557
            MTU: Rv2540c(aroF)
            MTC: MT2615(aroC)
            MBO: Mb2569c(aroF)
            MBB: BCG_2562c(aroF)
            MLE: ML0516(aroF)
            MPA: MAP1091(aroF)
            MAV: MAV_3417(aroC)
            MSM: MSMEG_3030(aroC)
            MVA: Mvan_2645
            MGI: Mflv_3758
            MMC: Mmcs_2352
            MKM: Mkms_2399
            MJL: Mjls_2393
            CGL: NCgl1561(cgl1623)
            CGB: cg1829(aroC)
            CEF: CE1743(aroC)
            CDI: DIP1345(aroC)
            CJK: jk1033(aroC)
            NFA: nfa36350(aroC)
            RHA: RHA1_ro07140(aroC)
            SCO: SCO1496(aroF)
            SMA: SAV6854(aroC)
            TWH: TWT372(aroF)
            TWS: TW397(aroC)
            LXX: Lxx10950(aroC)
            ART: Arth_2274
            AAU: AAur_2277(aroF)
            PAC: PPA1182
            NCA: Noca_2412
            TFU: Tfu_1090
            FRA: Francci3_3209
            FAL: FRAAL5247(aroF)
            ACE: Acel_1309
            KRA: Krad_4112
            SEN: SACE_2065(aroF)
            STP: Strop_1845
            BLO: BL0878(aroC)
            BAD: BAD_0704(aroC)
            RXY: Rxyl_1461
            FNU: FN0934
            RBA: RB6822(aroC)
            CTR: CT368(aroC)
            CTA: CTA_0400(aroC)
            CMU: TC0647
            CPN: CPn1037(aroC)
            CPA: CP0815
            CPJ: CPj1037(aroC)
            CPT: CpB1077
            CCA: CCA00725(aroC)
            CAB: CAB692(aroC)
            CFE: CF0291(aroC)
            PCU: pc0884(aroC)
            TDE: TDE1132(aroC)
            LIL: LA0157(aroC)
            LIC: LIC10140(aroC)
            LBJ: LBJ_0136(aroC)
            LBL: LBL_2947(aroC)
            SYN: sll1747(aroC)
            SYW: SYNW0308(aroC)
            SYC: syc1300_c(aroC)
            SYF: Synpcc7942_0212
            SYD: Syncc9605_0304
            SYE: Syncc9902_2040
            SYG: sync_0358(aroC)
            SYR: SynRCC307_2190(aroC)
            SYX: SynWH7803_0358(aroC)
            CYA: CYA_0336(aroC)
            CYB: CYB_1511(aroC)
            TEL: tll0463(aroC)
            GVI: glr3393(aroC)
            ANA: all0797
            AVA: Ava_0589
            PMA: Pro0253(aroC)
            PMM: PMM0224(aroC)
            PMT: PMT1795(aroC)
            PMN: PMN2A_1593
            PMI: PMT9312_0226
            PMB: A9601_02451(aroC)
            PMC: P9515_02561(aroC)
            PMF: P9303_23791(aroC)
            PMG: P9301_02461(aroC)
            PMH: P9215_02461
            PME: NATL1_03041(aroC)
            TER: Tery_2866
            BTH: BT_2084
            BFR: BF3792
            BFS: BF3584(aroC)
            PGI: PG1314(aroC)
            SRU: SRU_2063(aroC)
            CHU: CHU_0369(aroC)
            GFO: GFO_1627(aroC)
            FJO: Fjoh_4576
            FPS: FP0765(aroC)
            CTE: CT1432(aroC)
            CCH: Cag_1519
            CPH: Cpha266_1805
            PVI: Cvib_1253
            PLT: Plut_1436
            DET: DET0462(aroC)
            DEH: cbdb_A425(aroC)
            DEB: DehaBAV1_0439
            RRS: RoseRS_1952
            RCA: Rcas_3830
            DRA: DR_0775
            DGE: Dgeo_1730
            TTH: TTC0518 TTC1018
            TTJ: TTHA1384
            AAE: aq_081(aroC)
            TMA: TM0347
            TPT: Tpet_0573
            MJA: MJ1175(aroC)
            MMP: MMP1333(aroC)
            MMQ: MmarC5_0260
            MMZ: MmarC7_0578
            MAE: Maeo_0689
            MVN: Mevan_0644
            MAC: MA0550(aroC)
            MBA: Mbar_A1438
            MMA: MM_1712
            MBU: Mbur_1012
            MTP: Mthe_0161
            MHU: Mhun_1029
            MEM: Memar_1296
            MBN: Mboo_1564
            MTH: MTH748
            MST: Msp_0579(aroC)
            MSI: Msm_1474
            MKA: MK0631(aroC)
            AFU: AF0670(aroC)
            HAL: VNG1230G(aroC)
            HMA: rrnAC0124(aroC)
            HWA: HQ3357A(aroC)
            NPH: NP3082A(aroC)
            TAC: Ta0824
            TVO: TVN0729
            PTO: PTO0272 PTO1520
            PAB: PAB0307(aroC)
            PFU: PF1700
            TKO: TK0262
            RCI: RCIX509(aroC)
            APE: APE_0564
            IHO: Igni_0531
            SSO: SSO0307(aroC)
            STO: ST2274
            SAI: Saci_0186(aroC)
            MSE: Msed_1873
            PAI: PAE1912(aroC)
            PIS: Pisl_1763
            PCL: Pcal_0879
            PAS: Pars_2119
STRUCTURES  PDB: 1Q1L  1QXO  1R52  1R53  1SQ1  1UM0  1UMF  1ZTB  2G85  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.5
            ExPASy - ENZYME nomenclature database: 4.2.3.5
            ExplorEnz - The Enzyme Database: 4.2.3.5
            ERGO genome analysis and discovery system: 4.2.3.5
            BRENDA, the Enzyme Database: 4.2.3.5
            CAS: 9077-07-0
///
ENTRY       EC 4.2.3.6                  Enzyme
NAME        trichodiene synthase;
            trichodiene synthetase;
            sesquiterpene cyclase;
            trans,trans-farnesyl-diphosphate sesquiterpenoid-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing,
            trichodiene-forming)
REACTION    trans,trans-farnesyl diphosphate = trichodiene + diphosphate
            [RN:R02306]
ALL_REAC    R02306;
            (other) R02310
SUBSTRATE   trans,trans-farnesyl diphosphate [CPD:C00448]
PRODUCT     trichodiene [CPD:C01860];
            diphosphate [CPD:C00013]
REFERENCE   1  [PMID:3800398]
  AUTHORS   Hohn TM, Vanmiddlesworth F.
  TITLE     Purification and characterization of the sesquiterpene cyclase
            trichodiene synthetase from Fusarium sporotrichioides.
  JOURNAL   Arch. Biochem. Biophys. 251 (1986) 756-61.
  ORGANISM  Fusarium sporotrichioides
PATHWAY     PATH: map00900  Terpenoid biosynthesis
STRUCTURES  PDB: 1YJ4  1YYQ  1YYR  1YYS  1YYT  1YYU  2AEK  2AEL  2AET  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.6
            ExPASy - ENZYME nomenclature database: 4.2.3.6
            ExplorEnz - The Enzyme Database: 4.2.3.6
            ERGO genome analysis and discovery system: 4.2.3.6
            BRENDA, the Enzyme Database: 4.2.3.6
            CAS: 101915-76-8
///
ENTRY       EC 4.2.3.7                  Enzyme
NAME        pentalenene synthase;
            pentalenene synthetase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (cyclizing,
            pentalenene-forming)
REACTION    2-trans,6-trans-farnesyl diphosphate = pentalenene + diphosphate
            [RN:R02305]
ALL_REAC    R02305
SUBSTRATE   2-trans,6-trans-farnesyl diphosphate [CPD:C00448]
PRODUCT     pentalenene [CPD:C01841];
            diphosphate [CPD:C00013]
COMMENT     The initial step in the reaction is probably a cyclization of
            farnesyl diphosphate to form humulene. The enzyme is involved in the
            biosynthesis of pentalenolactone and related antibiotics.
REFERENCE   1  [PMID:6642060]
  AUTHORS   Cane DE.
  TITLE     Cell-free studies of monoterpene and sesquiterpene biosynthesis.
  JOURNAL   Biochem. Soc. Trans. 11 (1983) 510-5.
REFERENCE   2
  AUTHORS   Cane, D.E. and Tillman, A.M.
  TITLE     Pentalenene biosynthesis and the enzymic cyclization of farnesyl
            pyrophosphate.
  JOURNAL   J. Am. Chem. Soc. 105 (1983) 122-124.
  ORGANISM  Streptomyces sp.
REFERENCE   3  [PMID:8180213]
  AUTHORS   Cane DE, Sohng JK, Lamberson CR, Rudnicki SM, Wu Z, Lloyd MD, Oliver
            JS, Hubbard BR.
  TITLE     Pentalenene synthase. Purification, molecular cloning, sequencing,
            and high-level expression in Escherichia coli of a terpenoid cyclase
            from Streptomyces UC5319.
  JOURNAL   Biochemistry. 33 (1994) 5846-57.
  ORGANISM  Streptomyces sp.
GENES       SMA: SAV2998(ptlA)
            FAL: FRAAL6507
            AVA: Ava_1982
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.7
            ExPASy - ENZYME nomenclature database: 4.2.3.7
            ExplorEnz - The Enzyme Database: 4.2.3.7
            ERGO genome analysis and discovery system: 4.2.3.7
            BRENDA, the Enzyme Database: 4.2.3.7
            CAS: 90597-46-9
///
ENTRY       EC 4.2.3.8                  Enzyme
NAME        casbene synthase;
            casbene synthetase;
            geranylgeranyl-diphosphate diphosphate-lyase (cyclizing)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     geranylgeranyl-diphosphate diphosphate-lyase (cyclizing,
            casbene-forming)
REACTION    geranylgeranyl diphosphate = casbene + diphosphate [RN:R02064]
ALL_REAC    R02064
SUBSTRATE   geranylgeranyl diphosphate [CPD:C00353]
PRODUCT     casbene [CPD:C01414];
            diphosphate [CPD:C00013]
COMMENT     The enzyme from castor bean (Ricinus communis) produces the
            antifungal diterpene casbene.
REFERENCE   1  [PMID:3985625]
  AUTHORS   Moesta P, West CA.
  TITLE     Casbene synthetase: regulation of phytoalexin biosynthesis in
            Ricinus communis L. seedlings. Purification of casbene synthetase
            and regulation of its biosynthesis during elicitation.
  JOURNAL   Arch. Biochem. Biophys. 238 (1985) 325-33.
  ORGANISM  Ricinus communis
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.8
            ExPASy - ENZYME nomenclature database: 4.2.3.8
            ExplorEnz - The Enzyme Database: 4.2.3.8
            ERGO genome analysis and discovery system: 4.2.3.8
            BRENDA, the Enzyme Database: 4.2.3.8
            CAS: 69106-45-2
///
ENTRY       EC 4.2.3.9                  Enzyme
NAME        aristolochene synthase;
            sesquiterpene cyclase;
            trans,trans-farnesyl diphosphate aristolochene-lyase;
            trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing,
            aristolochene-forming)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (cyclizing,
            aristolochene-forming)
REACTION    2-trans,6-trans-farnesyl diphosphate = aristolochene + diphosphate
            [RN:R02307]
ALL_REAC    R02307
SUBSTRATE   2-trans,6-trans-farnesyl diphosphate [CPD:C00448]
PRODUCT     aristolochene [CPD:C02004];
            diphosphate [CPD:C00013]
COMMENT     The initial internal cyclization produces the monocyclic
            intermediate germacrene A; further cyclization and methyl transfer
            converts the intermediate into aristolochene. While in some species
            germacrene A remains as an enzyme-bound intermediate, it has been
            shown to be a minor product of the reaction in Penicillium
            roqueforti [5] (see also EC 4.2.3.23, germacrene-A synthase). The
            enzyme from Penicillium roqueforti requires Mg2+ and Mn2+ for
            activity. Aristolochene is the likely parent compound for a number
            of sesquiterpenes produced by filamentous fungi.
REFERENCE   1
  AUTHORS   Cane, D.E., Prabhakaran, P.C., Oliver, J.S. and McIlwaine, D.B.
  TITLE     Aristolochene biosynthesis. Stereochemistry of the deprotonation
            steps in the enzymatic cyclization of farnesyl pyrophosphate.
  JOURNAL   J. Am. Chem. Soc. 112 (1990) 3209-3210.
  ORGANISM  Penicillium roqueforti, Aspergills terreus
REFERENCE   2
  AUTHORS   Cane, D.E., Prabhakaran, P.C., Salaski, E.J., Harrison, P.M.H.,
            Noguchi, H. and Rawlings, B.J.
  TITLE     Aristolochene biosynthesis and enzymatic cyclization of farnesyl
            pyrophosphate.
  JOURNAL   J. Am. Chem. Soc. 111 (1989) 8914-8916.
  ORGANISM  Penicillium roqueforti, Aspergills terreus
REFERENCE   3  [PMID:2544140]
  AUTHORS   Hohn TM, Plattner RD.
  TITLE     Purification and characterization of the sesquiterpene cyclase
            aristolochene synthase from Penicillium roqueforti.
  JOURNAL   Arch. Biochem. Biophys. 272 (1989) 137-43.
  ORGANISM  Penicillium roqueforti
REFERENCE   4  [PMID:8440737]
  AUTHORS   Proctor RH, Hohn TM.
  TITLE     Aristolochene synthase. Isolation, characterization, and bacterial
            expression of a sesquiterpenoid biosynthetic gene (Ari1) from
            Penicillium roqueforti.
  JOURNAL   J. Biol. Chem. 268 (1993) 4543-8.
  ORGANISM  Penicillium roqueforti
REFERENCE   5  [PMID:12296728]
  AUTHORS   Calvert MJ, Ashton PR, Allemann RK.
  TITLE     Germacrene A is a product of the aristolochene synthase-mediated
            conversion of farnesylpyrophosphate to aristolochene.
  JOURNAL   J. Am. Chem. Soc. 124 (2002) 11636-41.
  ORGANISM  Penicillium roqueforti
PATHWAY     PATH: map00900  Terpenoid biosynthesis
STRUCTURES  PDB: 2E4O  2OA6  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.9
            ExPASy - ENZYME nomenclature database: 4.2.3.9
            ExplorEnz - The Enzyme Database: 4.2.3.9
            ERGO genome analysis and discovery system: 4.2.3.9
            BRENDA, the Enzyme Database: 4.2.3.9
///
ENTRY       EC 4.2.3.10                 Enzyme
NAME        (-)-endo-fenchol synthase;
            (-)-endo-fenchol cyclase;
            geranyl pyrophosphate:(-)-endo-fenchol cyclase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     geranyl-diphosphate diphosphate-lyase [cyclizing,
            (-)-endo-fenchol-forming]
REACTION    geranyl diphosphate + H2O = (-)-endo-fenchol + diphosphate
            [RN:R02004]
ALL_REAC    R02004
SUBSTRATE   geranyl diphosphate [CPD:C00341];
            H2O [CPD:C00001]
PRODUCT     (-)-endo-fenchol [CPD:C02344];
            diphosphate [CPD:C00013]
COMMENT     (3R)-Linalyl diphosphate is an intermediate in the reaction
REFERENCE   1  [PMID:2919880]
  AUTHORS   Croteau R, Miyazaki JH, Wheeler CJ.
  TITLE     Monoterpene biosynthesis: mechanistic evaluation of the geranyl
            pyrophosphate:(-)-endo-fenchol cyclase from fennel (Foeniculum
            vulgare).
  JOURNAL   Arch. Biochem. Biophys. 269 (1989) 507-16.
  ORGANISM  Foeniculum vulgare
REFERENCE   2  [PMID:3170591]
  AUTHORS   Croteau R, Satterwhite DM, Wheeler CJ, Felton NM.
  TITLE     Biosynthesis of monoterpenes. Stereochemistry of the enzymatic
            cyclization of geranyl pyrophosphate to (-)-endo-fenchol.
  JOURNAL   J. Biol. Chem. 263 (1988) 15449-53.
  ORGANISM  Foeniculum vulgare
PATHWAY     PATH: map00902  Monoterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.10
            ExPASy - ENZYME nomenclature database: 4.2.3.10
            ExplorEnz - The Enzyme Database: 4.2.3.10
            ERGO genome analysis and discovery system: 4.2.3.10
            BRENDA, the Enzyme Database: 4.2.3.10
            CAS: 117758-41-5
///
ENTRY       EC 4.2.3.11                 Enzyme
NAME        sabinene-hydrate synthase;
            sabinene hydrate cyclase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     geranyl-diphosphate diphosphate-lyase (cyclizing,
            sabinene-hydrate-forming)
REACTION    geranyl diphosphate + H2O = sabinene hydrate + diphosphate
            [RN:R02006]
ALL_REAC    R02006
SUBSTRATE   geranyl diphosphate [CPD:C00341];
            H2O [CPD:C00001]
PRODUCT     sabinene hydrate [CPD:C02462];
            diphosphate [CPD:C00013]
COMMENT     Both cis- and trans- isomers of sabinene hydrate are formed.
            (3R)-Linalyl diphosphate is an intermediate in the reaction
REFERENCE   1  [PMID:3401015]
  AUTHORS   Hallahan TW, Croteau R.
  TITLE     Monoterpene biosynthesis: demonstration of a geranyl
            pyrophosphate:sabinene hydrate cyclase in soluble enzyme
            preparations from sweet marjoram (Majorana hortensis).
  JOURNAL   Arch. Biochem. Biophys. 264 (1988) 618-31.
  ORGANISM  Majorana hortensis
REFERENCE   2  [PMID:2916845]
  AUTHORS   Hallahan TW, Croteau R.
  TITLE     Monoterpene biosynthesis: mechanism and stereochemistry of the
            enzymatic cyclization of geranyl pyrophosphate to (+)-cis- and
            (+)-trans-sabinene hydrate.
  JOURNAL   Arch. Biochem. Biophys. 269 (1989) 313-26.
  ORGANISM  Majorana hortensis
PATHWAY     PATH: map00902  Monoterpenoid biosynthesis
ORTHOLOGY   KO: K07385  sabinene-hydrate synthase
GENES       ATH: AT3G25830(ATTPS-CIN)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.11
            ExPASy - ENZYME nomenclature database: 4.2.3.11
            ExplorEnz - The Enzyme Database: 4.2.3.11
            ERGO genome analysis and discovery system: 4.2.3.11
            BRENDA, the Enzyme Database: 4.2.3.11
            CAS: 166800-09-5
///
ENTRY       EC 4.2.3.12                 Enzyme
NAME        6-pyruvoyltetrahydropterin synthase;
            2-amino-4-oxo-6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-
            dihydroxypteridine triphosphate lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin
            triphosphate-lyase (6-pyruvoyl-5,6,7,8-tetrahydropterin-forming)
REACTION    6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin =
            6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate [RN:R04286]
ALL_REAC    R04286;
            (other) R04735
SUBSTRATE   6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin
            [CPD:C04895]
PRODUCT     6-pyruvoyl-5,6,7,8-tetrahydropterin [CPD:C03684];
            triphosphate [CPD:C00536]
COMMENT     Catalyses triphosphate elimination and an intramolecular redox
            reaction in the presence of Mg2+. It has been identified in human
            liver. The product is 6-pyruvoyltetrahydrobiopterin.
REFERENCE   1  [PMID:2656673]
  AUTHORS   Milstien S, Kaufman S.
  TITLE     The biosynthesis of tetrahydrobiopterin in rat brain. Purification
            and characterization of 6-pyruvoyl tetrahydropterin
            (2'-oxo)reductase.
  JOURNAL   J. Biol. Chem. 264 (1989) 8066-73.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:1282802]
  AUTHORS   Thony B, Leimbacher W, Burgisser D, Heizmann CW.
  TITLE     Human 6-pyruvoyltetrahydropterin synthase: cDNA cloning and
            heterologous expression of the recombinant enzyme.
  JOURNAL   Biochem. Biophys. Res. Commun. 189 (1992) 1437-43.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K01737  6-pyruvoyl tetrahydrobiopterin synthase
GENES       HSA: 5805(PTS)
            MMU: 19286(Pts)
            RNO: 29498(Pts)
            CFA: 611326(PTS)
            GGA: 374144(PTS)
            SPU: 574852(LOC574852) 590962(LOC590962)
            DME: Dmel_CG16784(pr)
            CEL: B0041.6(ptps-1)
            PFA: PFF1360w
            ECO: b2765(ygcM)
            ECJ: JW2735(ygcM)
            ECE: Z4075(ygcM)
            ECS: ECs3620
            ECC: c3324(ygcM)
            ECI: UTI89_C3129(ygcM)
            ECP: ECP_2739
            ECV: APECO1_3767(ygcM)
            STY: STY3077
            STT: t2850
            SPT: SPA2805(ptpS)
            SEC: SC2880(ptpS)
            STM: STM2949(ptpS)
            YPE: YPO3373(ygcM)
            YPK: y0817
            YPM: YP_0313
            YPA: YPA_2871
            YPN: YPN_0719
            YPS: YPTB0758(ygcM)
            SFL: SF2781(ygcM)
            SFX: S2974(ygcM)
            SFV: SFV_2740(ygcM)
            SSN: SSON_2918(ygcM)
            SBO: SBO_2649(ygcM)
            SDY: SDY_2967(ygcM)
            ECA: ECA3553
            PLU: plu0702 plu2794
            BAS: BUsg402(ygcM)
            SGL: SG0515
            HIN: HI1190
            HIT: NTHI1361
            HDU: HD0557
            PMU: PM0185
            MSU: MS1856
            APL: APL_1098
            XFA: XF0193
            XFT: PD0158(ygcM)
            XCC: XCC0589(ptpS)
            XCB: XC_3644
            XCV: XCV3734(ptpS)
            XAC: XAC3614(ptps)
            XOO: XOO0769(ptpS)
            XOM: XOO_0699(XOO0699)
            VCH: VC1299
            VVU: VV1_2257
            VVY: VV2088
            VPA: VP1883
            VFI: VF1160(queD)
            PAE: PA2666
            PAU: PA14_29600(ptpS)
            PPU: PP_2341
            PST: PSPTO_3430
            PSB: Psyr_3215
            PSP: PSPPH_3130
            PFL: PFL_4019
            PFO: Pfl_3776
            PEN: PSEEN1910 PSEEN2520
            CPS: CPS_2933
            CBU: CBU_1883
            LPN: lpg2865
            LPF: lpl2777
            LPP: lpp2923
            MCA: MCA2527
            TCX: Tcr_1389
            NOC: Noc_2038
            AEH: Mlg_0831
            BCI: BCI_0219
            VOK: COSY_0285(ptpS)
            NME: NMB0527
            NMA: NMA0704
            NMC: NMC0466
            NGO: NGO0131
            CVI: CV_3508
            RSO: RSc1450(RS03857)
            REU: Reut_A1847
            REH: H16_A1924(ptpS)
            RME: Rmet_1572
            BMA: BMA0154
            BMV: BMASAVP1_A2793
            BML: BMA10299_A2286
            BMN: BMA10247_2365
            BXE: Bxe_A4405
            BUR: Bcep18194_A6468
            BCN: Bcen_2503
            BCH: Bcen2424_3117 Bcen2424_5330
            BAM: Bamb_3172
            BPS: BPSL0179
            BPM: BURPS1710b_0358(queD)
            BPL: BURPS1106A_0173
            BPD: BURPS668_0163
            BTE: BTH_I0139
            BPE: BP2660
            BPA: BPP1652
            BBR: BB3076
            RFR: Rfer_2613
            POL: Bpro_1495
            MPT: Mpe_A0527
            HAR: HEAR1380
            MMS: mma_2009
            NEU: NE1517
            NET: Neut_1286
            NMU: Nmul_A1944
            EBA: ebA642
            AZO: azo3118
            DAR: Daro_0854
            TBD: Tbd_2184 Tbd_2314
            MFA: Mfla_1477
            HPA: HPAG1_0913
            HAC: Hac_1077 Hac_1083
            WSU: WS1659
            CFF: CFF8240_0224
            CCV: CCV52592_0824
            CHA: CHAB381_0328
            CCO: CCC13826_1154 CCC13826_1394
            ABU: Abu_2060
            NIS: NIS_1580
            SUN: SUN_0215
            GSU: GSU1720
            GME: Gmet_1657
            PCA: Pcar_1643
            DVU: DVU1352 DVU2657
            DDE: Dde_2197
            LIP: LI0258
            BBA: Bd1863(ygcM) Bd1968(pts)
            DPS: DP0165 DP2265 DP2266
            MXA: MXAN_6868
            RPR: RP178
            RTY: RT0169
            RCO: RC0225
            RFE: RF_1094
            RBE: RBE_1097
            MLO: mll5797 mll8751
            MES: Meso_4052
            SME: SMb20939(exsC)
            ATU: Atu3345
            ATC: AGR_L_2952(exsC)
            RET: RHE_CH03712(exsC)
            RLE: RL4255(exsC)
            BME: BMEI0094
            BMF: BAB1_1974
            BMS: BR1973
            BMB: BruAb1_1949
            BJA: bll2482
            BRA: BRADO1973
            BBT: BBta_2297
            RPA: RPA1658(ptpS)
            RPB: RPB_3873
            RPC: RPC_3820
            RPE: RPE_3943
            NWI: Nwi_2620
            NHA: Nham_3244
            CCR: CC_3158
            SIL: SPO3903
            SIT: TM1040_2046
            ZMO: ZMO0818(ygcM)
            RRU: Rru_A1831
            MAG: amb0248
            MGM: Mmc1_0635
            ABA: Acid345_2209 Acid345_2210 Acid345_4642
            SUS: Acid_1041 Acid_1563 Acid_1564
            BSU: BG13313(ykvK)
            BHA: BH2243
            BAN: BA1360
            BAR: GBAA1360
            BAA: BA_1884
            BAT: BAS1258
            BCE: BC1342
            BCA: BCE_1459
            BCZ: BCZK1233(ygcM)
            BTK: BT9727_1231(ygcM)
            BLI: BL03547(queD)
            BLD: BLi01528(ykvK)
            BCL: ABC2128
            BPU: BPUM_1264(queD)
            OIH: OB2804
            GKA: GK0976 GK1470
            SAU: SA0666
            SAV: SAV0711
            SAM: MW0673
            SAR: SAR0764
            SAS: SAS0676
            SAC: SACOL0771
            SAB: SAB0660c
            SAA: SAUSA300_0696
            SAO: SAOUHSC_00720
            SEP: SE0486
            SER: SERP0372
            SHA: SH0157 SH2187
            SSP: SSP0291 SSP2009
            SMU: SMU.917c
            STC: str0826(ptpS)
            STL: stu0826(ptpS)
            LSL: LSL_0905
            CAC: CAC3624
            CNO: NT01CX_2384
            CBO: CBO0827
            CBA: CLB_0868 CLB_1575
            CBH: CLC_0882 CLC_1586
            CBF: CLI_0909 CLI_1636
            TTE: TTE2368
            FRA: Francci3_1755 Francci3_3381
            FAL: FRAAL2745(ptp)
            RXY: Rxyl_2576
            RBA: RB5135 RB8806
            LIL: LA0332(ptpS)
            LIC: LIC10287(ptpS)
            LBJ: LBJ_2715(ptpS)
            LBL: LBL_0359(ptpS)
            SYN: slr0078
            SYW: SYNW2201
            SYC: syc0366_c syc2141_d
            SYF: Synpcc7942_1184 Synpcc7942_1953
            SYD: Syncc9605_2344
            SYE: Syncc9902_0347
            SYG: sync_2556
            SYR: SynRCC307_0292 SynRCC307_1620
            SYX: SynWH7803_0747 SynWH7803_2212
            CYA: CYA_1099
            CYB: CYB_0675
            TEL: tll1095
            GVI: glr3579
            ANA: alr0080 alr4554
            AVA: Ava_1455 Ava_2504
            PMA: Pro0127
            PMM: PMM0106
            PMT: PMT0164
            PMN: PMN2A_1475
            PMI: PMT9312_0110
            PMB: A9601_01231
            PMC: P9515_01191
            PMF: P9303_02061
            PMG: P9301_01221
            PME: NATL1_01781
            BTH: BT_4453
            BFR: BF3596
            BFS: BF3400
            PGI: PG1056
            CHU: CHU_0956(ygcM) CHU_1390(ygcM)
            GFO: GFO_3363
            FPS: FP1791(ygcM) FP2248
            CTE: CT0782 CT1437
            CCH: Cag_0373 Cag_0421
            CPH: Cpha266_1847
            PLT: Plut_1438
            DET: DET1605
            DEH: cbdb_A1699(ptpS)
            AAE: aq_269 aq_853
            TMA: TM0038
            MAC: MA0956(ptpS) MA4196
            MBA: Mbar_A0134 Mbar_A2626
            MMA: MM_0756
            MBU: Mbur_1269
            MHU: Mhun_2831
            MST: Msp_1432
            AFU: AF0440
            HAL: VNG1024C
            HMA: rrnAC2166(ptpS)
            HWA: HQ2423A(ptpS)
            NPH: NP1342A
            PTO: PTO1064
            PHO: PH0634
            PAB: PAB1445
            PFU: PF1278
            TKO: TK1119
            RCI: RCIX32(ptpS)
STRUCTURES  PDB: 1Y13  2A0S  2DJ6  2G64  2OBA  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.12
            ExPASy - ENZYME nomenclature database: 4.2.3.12
            ExplorEnz - The Enzyme Database: 4.2.3.12
            ERGO genome analysis and discovery system: 4.2.3.12
            BRENDA, the Enzyme Database: 4.2.3.12
            CAS: 97089-82-2
///
ENTRY       EC 4.2.3.13                 Enzyme
NAME        (+)-delta-cadinene synthase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (cyclizing,
            (+)-delta-cadinene-forming)
REACTION    2-trans,6-trans-farnesyl diphosphate = (+)-delta-cadinene +
            diphosphate [RN:R02311]
ALL_REAC    R02311
SUBSTRATE   2-trans,6-trans-farnesyl diphosphate [CPD:C00448]
PRODUCT     (+)-delta-cadinene [CPD:C06394];
            diphosphate [CPD:C00013]
COFACTOR    Magnesium [CPD:C00305]
COMMENT     The sesquiterpenoid (+)-delta-cadinene is an intermediate in
            phytoalexin biosynthesis. Mg2+ is required for activity.
REFERENCE   1  [PMID:8554317]
  AUTHORS   Chen XY, Chen Y, Heinstein P, Davisson VJ.
  TITLE     Cloning, expression, and characterization of (+)-delta-cadinene
            synthase: a catalyst for cotton phytoalexin biosynthesis.
  JOURNAL   Arch. Biochem. Biophys. 324 (1995) 255-66.
  ORGANISM  Gossypium arboreum [GN:egar]
REFERENCE   2  [PMID:8728715]
  AUTHORS   Davis EM, Tsuji J, Davis GD, Pierce ML, Essenberg M.
  TITLE     Purification of (+)-delta-cadinene synthase, a sesquiterpene cyclase
            from bacteria-inoculated cotton foliar tissue.
  JOURNAL   Phytochemistry. 41 (1996) 1047-55.
  ORGANISM  Gossypium hirsutum
REFERENCE   3
  AUTHORS   Davis, G.D., Essenberg, M.
  TITLE     (+)-delta-Cadinene is a product of sesquiterpene cyclase activity in
            cotton.
  JOURNAL   Phytochemistry 39 (1995) 553-567.
  ORGANISM  Gossypium hirsutum
PATHWAY     PATH: map00900  Terpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.13
            ExPASy - ENZYME nomenclature database: 4.2.3.13
            ExplorEnz - The Enzyme Database: 4.2.3.13
            ERGO genome analysis and discovery system: 4.2.3.13
            BRENDA, the Enzyme Database: 4.2.3.13
            CAS: 166800-09-5
///
ENTRY       EC 4.2.3.14                 Enzyme
NAME        pinene synthase;
            beta-geraniolene synthase;
            (-)-(1S,5S)-pinene synthase;
            geranyldiphosphate diphosphate lyase (pinene forming)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     geranyl-diphosphate diphosphate-lyase (cyclizing, pinene-forming)
REACTION    geranyl diphosphate = pinene + diphosphate [RN:R02012]
ALL_REAC    R02012 > R05765 R05766
SUBSTRATE   geranyl diphosphate [CPD:C00341]
PRODUCT     pinene [CPD:C06077];
            diphosphate [CPD:C00013]
COMMENT     A recombinant enzyme (also known as a monoterpene synthase or
            cyclase) from the grand fir (Abies grandis) requires Mn2+ and K+ for
            activity. Mg2+ is essentially ineffective as the divalent metal ion
            cofactor. A mixture of alpha and beta-pinene is produced.
REFERENCE   1  [PMID:9268308]
  AUTHORS   Bohlmann J, Steele CL, Croteau R.
  TITLE     Monoterpene synthases from grand fir (Abies grandis). cDNA
            isolation, characterization, and functional expression of myrcene
            synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene
            synthase.
  JOURNAL   J. Biol. Chem. 272 (1997) 21784-92.
  ORGANISM  Abies grandis
REFERENCE   2  [PMID:1898071]
  AUTHORS   Gijzen M, Lewinsohn E, Croteau R.
  TITLE     Characterization of the constitutive and wound-inducible monoterpene
            cyclases of grand fir (Abies grandis).
  JOURNAL   Arch. Biochem. Biophys. 289 (1991) 267-73.
  ORGANISM  Abies grandis
REFERENCE   3  [PMID:8109978]
  AUTHORS   Wagschal KC, Pyun HJ, Coates RM, Croteau R.
  TITLE     Monoterpene biosynthesis: isotope effects associated with bicyclic
            olefin formation catalyzed by pinene synthases from sage (Salvia
            officinalis).
  JOURNAL   Arch. Biochem. Biophys. 308 (1994) 477-87.
  ORGANISM  Salvia officinalis
PATHWAY     PATH: map00902  Monoterpenoid biosynthesis
ORTHOLOGY   KO: K07384  pinene synthase
GENES       ATH: AT4G16730
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.14
            ExPASy - ENZYME nomenclature database: 4.2.3.14
            ExplorEnz - The Enzyme Database: 4.2.3.14
            ERGO genome analysis and discovery system: 4.2.3.14
            BRENDA, the Enzyme Database: 4.2.3.14
///
ENTRY       EC 4.2.3.15                 Enzyme
NAME        myrcene synthase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     geranyl-diphosphate diphosphate-lyase (myrcene-forming)
REACTION    geranyl diphosphate = myrcene + diphosphate [RN:R02009]
ALL_REAC    R02009
SUBSTRATE   geranyl diphosphate [CPD:C00341]
PRODUCT     myrcene [CPD:C06074];
            diphosphate [CPD:C00013]
COMMENT     A recombinant enzyme (also known as a monoterpene synthase or
            cyclase) from the grand fir (Abies grandis) requires Mn2+ and K+ for
            activity. Mg2+ is essentially ineffective as the divalent metal ion
            cofactor.
REFERENCE   1  [PMID:9268308]
  AUTHORS   Bohlmann J, Steele CL, Croteau R.
  TITLE     Monoterpene synthases from grand fir (Abies grandis). cDNA
            isolation, characterization, and functional expression of myrcene
            synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene
            synthase.
  JOURNAL   J. Biol. Chem. 272 (1997) 21784-92.
  ORGANISM  Abies grandis
PATHWAY     PATH: map00902  Monoterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.15
            ExPASy - ENZYME nomenclature database: 4.2.3.15
            ExplorEnz - The Enzyme Database: 4.2.3.15
            ERGO genome analysis and discovery system: 4.2.3.15
            BRENDA, the Enzyme Database: 4.2.3.15
///
ENTRY       EC 4.2.3.16                 Enzyme
NAME        (4S)-limonene synthase;
            (-)-(4S)-limonene synthase;
            4S-(-)-limonene synthase;
            geranyldiphosphate diphosphate lyase (limonene forming);
            geranyldiphosphate diphosphate lyase [cyclizing,
            (4S)-limonene-forming]
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     geranyl-diphosphate diphosphate-lyase [cyclizing,
            (-)-(4S)-limonene-forming]
REACTION    geranyl diphosphate = (-)-(4S)-limonene + diphosphate [RN:R02013]
ALL_REAC    R02013
SUBSTRATE   geranyl diphosphate [CPD:C00341]
PRODUCT     (-)-(4S)-limonene [CPD:C00521];
            diphosphate [CPD:C00013]
COMMENT     A recombinant enzyme (also known as a monoterpene synthase or
            cyclase) from the grand fir (Abies grandis) requires Mn2+ and K+ for
            activity. Mg2+ is essentially ineffective as the divalent metal ion
            cofactor.
REFERENCE   1  [PMID:9268308]
  AUTHORS   Bohlmann J, Steele CL, Croteau R.
  TITLE     Monoterpene synthases from grand fir (Abies grandis). cDNA
            isolation, characterization, and functional expression of myrcene
            synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene
            synthase.
  JOURNAL   J. Biol. Chem. 272 (1997) 21784-92.
  ORGANISM  Abies grandis
REFERENCE   2  [PMID:8226816]
  AUTHORS   Colby SM, Alonso WR, Katahira EJ, McGarvey DJ, Croteau R.
  TITLE     4S-limonene synthase from the oil glands of spearmint (Mentha
            spicata). cDNA isolation, characterization, and bacterial expression
            of the catalytically active monoterpene cyclase.
  JOURNAL   J. Biol. Chem. 268 (1993) 23016-24.
  ORGANISM  Mentha spicata
REFERENCE   3  [PMID:8806736]
  AUTHORS   Yuba A, Yazaki K, Tabata M, Honda G, Croteau R.
  TITLE     cDNA cloning, characterization, and functional expression of
            4S-(-)-limonene synthase from Perilla frutescens.
  JOURNAL   Arch. Biochem. Biophys. 332 (1996) 280-7.
  ORGANISM  Perilla frutescens
PATHWAY     PATH: map00902  Monoterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.16
            ExPASy - ENZYME nomenclature database: 4.2.3.16
            ExplorEnz - The Enzyme Database: 4.2.3.16
            ERGO genome analysis and discovery system: 4.2.3.16
            BRENDA, the Enzyme Database: 4.2.3.16
///
ENTRY       EC 4.2.3.17                 Enzyme
NAME        taxadiene synthase;
            geranylgeranyl-diphosphate diphosphate-lyase (cyclizing,
            taxadiene-forming)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     geranylgeranyl-diphosphate diphosphate-lyase (cyclizing,
            taxa-4,11-diene-forming)
REACTION    geranylgeranyl diphosphate = taxa-4,11-diene + diphosphate
            [RN:R06305]
ALL_REAC    R06305
SUBSTRATE   geranylgeranyl diphosphate [CPD:C00353]
PRODUCT     taxa-4,11-diene [CPD:C11894];
            diphosphate [CPD:C00013]
COMMENT     The cyclization involves a 1,5-hydride shift.
REFERENCE   1  [PMID:7721772]
  AUTHORS   Koepp AE, Hezari M, Zajicek J, Vogel BS, LaFever RE, Lewis NG,
            Croteau R.
  TITLE     Cyclization of geranylgeranyl diphosphate to taxa-4(5),11(12)-diene
            is the committed step of taxol biosynthesis in Pacific yew.
  JOURNAL   J. Biol. Chem. 270 (1995) 8686-90.
  ORGANISM  Taxus brevifolia
REFERENCE   2  [PMID:7574719]
  AUTHORS   Hezari M, Lewis NG, Croteau R.
  TITLE     Purification and characterization of taxa-4(5),11(12)-diene synthase
            from Pacific yew (Taxus brevifolia) that catalyzes the first
            committed step of taxol biosynthesis.
  JOURNAL   Arch. Biochem. Biophys. 322 (1995) 437-44.
  ORGANISM  Taxus brevifolia
REFERENCE   3  [PMID:8608134]
  AUTHORS   Lin X, Hezari M, Koepp AE, Floss HG, Croteau R.
  TITLE     Mechanism of taxadiene synthase, a diterpene cyclase that catalyzes
            the first step of taxol biosynthesis in Pacific yew.
  JOURNAL   Biochemistry. 35 (1996) 2968-77.
  ORGANISM  Taxus brevifolia
REFERENCE   4  [PMID:9016812]
  AUTHORS   Hezari M, Ketchum RE, Gibson DM, Croteau R.
  TITLE     Taxol production and taxadiene synthase activity in Taxus canadensis
            cell suspension cultures.
  JOURNAL   Arch. Biochem. Biophys. 337 (1997) 185-90.
  ORGANISM  Taxus canadensis
REFERENCE   5  [PMID:11137819]
  AUTHORS   Williams DC, Carroll BJ, Jin Q, Rithner CD, Lenger SR, Floss HG,
            Coates RM, Williams RM, Croteau R.
  TITLE     Intramolecular proton transfer in the cyclization of geranylgeranyl
            diphosphate to the taxadiene precursor of taxol catalyzed by
            recombinant taxadiene synthase.
  JOURNAL   Chem. Biol. 7 (2000) 969-77.
  ORGANISM  Taxus brevifolia
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.17
            ExPASy - ENZYME nomenclature database: 4.2.3.17
            ExplorEnz - The Enzyme Database: 4.2.3.17
            ERGO genome analysis and discovery system: 4.2.3.17
            BRENDA, the Enzyme Database: 4.2.3.17
            CAS: 169277-52-5
///
ENTRY       EC 4.2.3.18                 Enzyme
NAME        abietadiene synthase;
            copalyl-diphosphate diphosphate-lyase (cyclizing)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     (+)-copalyl-diphosphate diphosphate-lyase [cyclizing;
            (-)-abietadiene-forming]
REACTION    (+)-copalyl diphosphate = (-)-abietadiene + diphosphate [RN:R06301]
ALL_REAC    R06301;
            (other) R06299 R06300 R06302 R06303 R06304
SUBSTRATE   (+)-copalyl diphosphate [CPD:C11901]
PRODUCT     (-)-abietadiene [CPD:C11878];
            diphosphate [CPD:C00013]
COMMENT     Part of a bifunctional enzyme involved in the biosynthesis of
            abietadiene. See also EC 5.5.1.12 (copalyl diphosphate synthase).
            Requires Mg2+
REFERENCE   1  [PMID:11112547]
  AUTHORS   Peters RJ, Flory JE, Jetter R, Ravn MM, Lee HJ, Coates RM, Croteau
            RB.
  TITLE     Abietadiene synthase from grand fir (Abies grandis):
            characterization and mechanism of action of the
            &quot;pseudomature&quot; recombinant enzyme.
  JOURNAL   Biochemistry. 39 (2000) 15592-602.
  ORGANISM  Abies grandis
REFERENCE   2  [PMID:11552804]
  AUTHORS   Peters RJ, Ravn MM, Coates RM, Croteau RB.
  TITLE     Bifunctional abietadiene synthase: free diffusive transfer of the
            (+)-copalyl diphosphate intermediate between two distinct active
            sites.
  JOURNAL   J. Am. Chem. Soc. 123 (2001) 8974-8.
  ORGANISM  Abies grandis
REFERENCE   3  [PMID:11805316]
  AUTHORS   Peters RJ, Croteau RB.
  TITLE     Abietadiene synthase catalysis: mutational analysis of a prenyl
            diphosphate ionization-initiated cyclization and rearrangement.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 580-4.
  ORGANISM  Abies grandis
REFERENCE   4  [PMID:11827528]
  AUTHORS   Peters RJ, Croteau RB.
  TITLE     Abietadiene synthase catalysis: conserved residues involved in
            protonation-initiated cyclization of geranylgeranyl diphosphate to
            (+)-copalyl diphosphate.
  JOURNAL   Biochemistry. 41 (2002) 1836-42.
  ORGANISM  Abies grandis
REFERENCE   5  [PMID:12059223]
  AUTHORS   Ravn MM, Peters RJ, Coates RM, Croteau R.
  TITLE     Mechanism of abietadiene synthase catalysis: stereochemistry and
            stabilization of the cryptic pimarenyl carbocation intermediates.
  JOURNAL   J. Am. Chem. Soc. 124 (2002) 6998-7006.
  ORGANISM  Abies grandis
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.18
            ExPASy - ENZYME nomenclature database: 4.2.3.18
            ExplorEnz - The Enzyme Database: 4.2.3.18
            ERGO genome analysis and discovery system: 4.2.3.18
            BRENDA, the Enzyme Database: 4.2.3.18
            CAS: 157972-08-2
///
ENTRY       EC 4.2.3.19                 Enzyme
NAME        ent-kaurene synthase;
            ent-kaurene synthase B;
            ent-kaurene synthetase B, ent-copalyl-diphosphate diphosphate-lyase
            (cyclizing)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     ent-copalyl-diphosphate diphosphate-lyase (cyclizing,
            ent-kaurene-forming)
REACTION    ent-copalyl diphosphate = ent-kaurene + diphosphate [RN:R05092]
ALL_REAC    R05092
SUBSTRATE   ent-copalyl diphosphate [CPD:C06089]
PRODUCT     ent-kaurene [CPD:C06090];
            diphosphate [CPD:C00013]
COMMENT     Part of a bifunctional enzyme involved in the biosynthesis of
            ent-kaurene. See also EC 5.5.1.13 (ent-copalyl diphosphate synthase)
REFERENCE   1  [PMID:4331199]
  AUTHORS   Fall RR, West CA.
  TITLE     Purification and properties of kaurene synthetase from Fusarium
            moniliforme.
  JOURNAL   J. Biol. Chem. 246 (1971) 6913-28.
  ORGANISM  Fusarium moniliforme
REFERENCE   2  [PMID:8771778]
  AUTHORS   Yamaguchi S, Saito T, Abe H, Yamane H, Murofushi N, Kamiya Y.
  TITLE     Molecular cloning and characterization of a cDNA encoding the
            gibberellin biosynthetic enzyme ent-kaurene synthase B from pumpkin
            (Cucurbita maxima L.).
  JOURNAL   Plant. J. 10 (1996) 203-13.
  ORGANISM  Cucurbita maxima
REFERENCE   3  [PMID:9268298]
  AUTHORS   Kawaide H, Imai R, Sassa T, Kamiya Y.
  TITLE     Ent-kaurene synthase from the fungus Phaeosphaeria sp. L487. cDNA
            isolation, characterization, and bacterial expression of a
            bifunctional diterpene cyclase in fungal gibberellin biosynthesis.
  JOURNAL   J. Biol. Chem. 272 (1997) 21706-12.
  ORGANISM  Phaeosphaeria sp.
REFERENCE   4  [PMID:10803977]
  AUTHORS   Toyomasu T, Kawaide H, Ishizaki A, Shinoda S, Otsuka M, Mitsuhashi
            W, Sassa T.
  TITLE     Cloning of a full-length cDNA encoding ent-kaurene synthase from
            Gibberella fujikuroi: functional analysis of a bifunctional
            diterpene cyclase.
  JOURNAL   Biosci. Biotechnol. Biochem. 64 (2000) 660-4.
  ORGANISM  Gibberella fujikuroi
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
ORTHOLOGY   KO: K04121  ent-kaurene synthase
GENES       ATH: AT1G79460(GA2)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.19
            ExPASy - ENZYME nomenclature database: 4.2.3.19
            ExplorEnz - The Enzyme Database: 4.2.3.19
            ERGO genome analysis and discovery system: 4.2.3.19
            BRENDA, the Enzyme Database: 4.2.3.19
            CAS: 9055-64-5
///
ENTRY       EC 4.2.3.20                 Enzyme
NAME        (R)-limonene synthase;
            (+)-limonene synthase;
            geranyldiphosphate diphosphate lyase [(+)-(R)-limonene-forming]
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     geranyl-diphosphate diphosphate-lyase [cyclizing,
            (+)-(4R)-limonene-forming]
REACTION    geranyl diphosphate = (+)-(4R)-limonene + diphosphate [RN:R06120]
ALL_REAC    R06120
SUBSTRATE   geranyl diphosphate [CPD:C00341]
PRODUCT     (+)-(4R)-limonene [CPD:C06099];
            diphosphate [CPD:C00013]
COMMENT     Forms the first step of carvone biosynthesis in caraway. The enzyme
            from Carum carvi (caraway) seeds requires a divalent metal ion
            (preferably Mn2+) for catalysis. This enzyme occurs in Citrus, Carum
            (caraway) and Anethum (dill); (-)-limonene, however, is made in the
            fir, Abies, and mint, Mentha, by EC 4.2.3.16, (4S)-limonene
            synthase.
REFERENCE   1  [PMID:9662532]
  AUTHORS   Bouwmeester HJ, Gershenzon J, Konings MC, Croteau R.
  TITLE     Biosynthesis of the monoterpenes limonene and carvone in the fruit
            of caraway. I. Demonstration Of enzyme activities and their changes
            with development
  JOURNAL   Plant. Physiol. 117 (1998) 901-12.
  ORGANISM  Carum carvi
REFERENCE   2  [PMID:12084056]
  AUTHORS   Lucker J, El Tamer MK, Schwab W, Verstappen FW, van der Plas LH,
            Bouwmeester HJ, Verhoeven HA.
  TITLE     Monoterpene biosynthesis in lemon (Citrus limon). cDNA isolation and
            functional analysis of four monoterpene synthases.
  JOURNAL   Eur. J. Biochem. 269 (2002) 3160-71.
  ORGANISM  Citrus limon
REFERENCE   3  [PMID:11305598]
  AUTHORS   Maruyama T, Ito M, Kiuchi F, Honda G.
  TITLE     Molecular cloning, functional expression and characterization of
            d-limonene synthase from Schizonepeta tenuifolia.
  JOURNAL   Biol. Pharm. Bull. 24 (2001) 373-7.
  ORGANISM  Schizonepeta tenuifolia
PATHWAY     PATH: map00902  Monoterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.20
            ExPASy - ENZYME nomenclature database: 4.2.3.20
            ExplorEnz - The Enzyme Database: 4.2.3.20
            ERGO genome analysis and discovery system: 4.2.3.20
            BRENDA, the Enzyme Database: 4.2.3.20
///
ENTRY       EC 4.2.3.21                 Enzyme
NAME        vetispiradiene synthase;
            vetispiradiene-forming farnesyl pyrophosphate cyclase;
            pemnaspirodiene synthase;
            HVS;
            vetispiradiene cyclase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing,
            vetispiradiene-forming)
REACTION    trans,trans-farnesyl diphosphate = vetispiradiene + diphosphate
            [RN:R06523]
ALL_REAC    R06523
SUBSTRATE   trans,trans-farnesyl diphosphate [CPD:C00448]
PRODUCT     vetispiradiene [CPD:C12142];
            diphosphate [CPD:C00013]
COMMENT     The initial internal cyclization produces the monocyclic
            intermediate germacrene A.
REFERENCE   1  [PMID:7706281]
  AUTHORS   Back K, Chappell J.
  TITLE     Cloning and bacterial expression of a sesquiterpene cyclase from
            Hyoscyamus muticus and its molecular comparison to related terpene
            cyclases.
  JOURNAL   J. Biol. Chem. 270 (1995) 7375-81.
  ORGANISM  Hyoscyamus muticus
REFERENCE   2
  AUTHORS   Keller, H., Czernic, P., Ponchet, M., Ducrot, P.H., Back, K.,
            Chappell, J., Ricci, P. and Marco, Y.
  TITLE     Sesquiterpene cyclase is not a determining factor for elicitor- and
            pathogen-induced capsidiol accumulation in tobacco.
  JOURNAL   Planta 205 (1998) 467-476.
REFERENCE   3  [PMID:9204881]
  AUTHORS   Mathis JR, Back K, Starks C, Noel J, Poulter CD, Chappell J.
  TITLE     Pre-steady-state study of recombinant sesquiterpene cyclases.
  JOURNAL   Biochemistry. 36 (1997) 8340-8.
  ORGANISM  Hyoscyamus muticus
REFERENCE   4  [PMID:10588069]
  AUTHORS   Yoshioka H, Yamada N, Doke N.
  TITLE     cDNA cloning of sesquiterpene cyclase and squalene synthase, and
            expression of the genes in potato tuber infected with Phytophthora
            infestans.
  JOURNAL   Plant. Cell. Physiol. 40 (1999) 993-8.
  ORGANISM  Hyoscyamus muticus, potato
REFERENCE   5  [PMID:11745124]
  AUTHORS   Martin VJ, Yoshikuni Y, Keasling JD.
  TITLE     The in vivo synthesis of plant sesquiterpenes by Escherichia coli.
  JOURNAL   Biotechnol. Bioeng. 75 (2001) 497-503.
  ORGANISM  Hyoscyamus muticus
PATHWAY     PATH: map00900  Terpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.21
            ExPASy - ENZYME nomenclature database: 4.2.3.21
            ExplorEnz - The Enzyme Database: 4.2.3.21
            ERGO genome analysis and discovery system: 4.2.3.21
            BRENDA, the Enzyme Database: 4.2.3.21
///
ENTRY       EC 4.2.3.22                 Enzyme
NAME        germacradienol synthase;
            germacradienol/germacrene-D synthase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase
            [(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol-forming]
REACTION    (1) 2-trans,6-trans-farnesyl diphosphate + H2O =
            (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + diphosphate [RN:R07647];
            (2) 2-trans,6-trans-farnesyl diphosphate = (-)-(7S)-germacrene D +
            diphosphate [RN:R07648]
ALL_REAC    R07647 R07648
SUBSTRATE   2-trans,6-trans-farnesyl diphosphate [CPD:C00448];
            H2O [CPD:C00001]
PRODUCT     (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol [CPD:C16143];
            diphosphate [CPD:C00013];
            (-)-(7S)-germacrene D
COMMENT     Requires Mg2+ for activity. H-1si of farnesyl diphosphate is lost in
            the formation of (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol.
            Formation of (-)-germacrene D involves a stereospecific 1,3-hydride
            shift of H-1si of farnesyl diphosphate. Both products are formed
            from a common intermediate [2]. Other enzymes produce germacrene D
            as the sole product using a different mechanism. The enzyme mediates
            a key step in the biosynthesis of geosmin, a widely occurring
            metabolite of many streptomycetes, bacteria and fungi [2].
REFERENCE   1  [PMID:12556563]
  AUTHORS   Cane DE, Watt RM.
  TITLE     Expression and mechanistic analysis of a germacradienol synthase
            from Streptomyces coelicolor implicated in geosmin biosynthesis.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 1547-51.
  ORGANISM  Streptomyces coelicolor
REFERENCE   2  [PMID:14995166]
  AUTHORS   He X, Cane DE.
  TITLE     Mechanism and stereochemistry of the germacradienol/germacrene D
            synthase of Streptomyces coelicolor A3(2).
  JOURNAL   J. Am. Chem. Soc. 126 (2004) 2678-9.
  ORGANISM  Streptomyces coelicolor
REFERENCE   3  [PMID:12563033]
  AUTHORS   Gust B, Challis GL, Fowler K, Kieser T, Chater KF.
  TITLE     PCR-targeted Streptomyces gene replacement identifies a protein
            domain needed for biosynthesis of the sesquiterpene soil odor
            geosmin.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 1541-6.
  ORGANISM  Streptomyces coelicolor
ORTHOLOGY   KO: K10187  germacradienol/germacrene-D synthase
GENES       SCO: SCO6073(SC9B1.20)
            SMA: SAV2163(geoA)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.22
            ExPASy - ENZYME nomenclature database: 4.2.3.22
            ExplorEnz - The Enzyme Database: 4.2.3.22
            ERGO genome analysis and discovery system: 4.2.3.22
            BRENDA, the Enzyme Database: 4.2.3.22
///
ENTRY       EC 4.2.3.23                 Enzyme
NAME        germacrene-A synthase;
            germacrene A synthase;
            (+)-germacrene A synthase;
            (+)-(10R)-germacrene A synthase;
            GAS;
            2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase
            (germacrene-A-forming)
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase
            [(+)-(R)-germacrene-A-forming]
REACTION    2-trans,6-trans-farnesyl diphosphate = (+)-(R)-gemacrene A +
            diphosphate [RN:R07649]
ALL_REAC    R07649
SUBSTRATE   2-trans,6-trans-farnesyl diphosphate [CPD:C00448]
PRODUCT     (+)-(R)-gemacrene A;
            diphosphate [CPD:C00013]
COMMENT     Requires Mg2+ for activity. While germacrene A is an enzyme-bound
            intermediate in the biosynthesis of a number of phytoalexins, e.g.
            EC 4.2.3.9 (aristolochene synthase) from some species and EC
            4.2.3.21 (vetispiradiene synthase), it is the sole sesquiterpenoid
            product formed in chicory [1].
REFERENCE   1  [PMID:12011345]
  AUTHORS   Bouwmeester HJ, Kodde J, Verstappen FW, Altug IG, de Kraker JW,
            Wallaart TE.
  TITLE     Isolation and characterization of two germacrene A synthase cDNA
            clones from chicory.
  JOURNAL   Plant. Physiol. 129 (2002) 134-44.
  ORGANISM  Cichorium intybus
REFERENCE   2  [PMID:12127586]
  AUTHORS   Prosser I, Phillips AL, Gittings S, Lewis MJ, Hooper AM, Pickett JA,
            Beale MH.
  TITLE     (+)-(10R)-Germacrene A synthase from goldenrod, Solidago canadensis;
            cDNA isolation, bacterial expression and functional analysis.
  JOURNAL   Phytochemistry. 60 (2002) 691-702.
  ORGANISM  Solidago canadensis
REFERENCE   3  [PMID:9701594]
  AUTHORS   de Kraker JW, Franssen MC, de Groot A, Konig WA, Bouwmeester HJ.
  TITLE     (+)-Germacrene A biosynthesis . The committed step in the
            biosynthesis of bitter sesquiterpene lactones in chicory
  JOURNAL   Plant. Physiol. 117 (1998) 1381-92.
  ORGANISM  Cichorium intybus
REFERENCE   4  [PMID:12296728]
  AUTHORS   Calvert MJ, Ashton PR, Allemann RK.
  TITLE     Germacrene A is a product of the aristolochene synthase-mediated
            conversion of farnesylpyrophosphate to aristolochene.
  JOURNAL   J. Am. Chem. Soc. 124 (2002) 11636-41.
REFERENCE   5  [PMID:15834787]
  AUTHORS   Chang YJ, Jin J, Nam HY, Kim SU.
  TITLE     Point mutation of (+)-germacrene A synthase from Ixeris dentata.
  JOURNAL   Biotechnol. Lett. 27 (2005) 285-8.
  ORGANISM  Ixeris dentata
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.23
            ExPASy - ENZYME nomenclature database: 4.2.3.23
            ExplorEnz - The Enzyme Database: 4.2.3.23
            ERGO genome analysis and discovery system: 4.2.3.23
            BRENDA, the Enzyme Database: 4.2.3.23
///
ENTRY       EC 4.2.3.24                 Enzyme
NAME        amorpha-4,11-diene synthase;
            amorphadiene synthase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase
            (amorpha-4,11-diene-forming)
REACTION    2-trans,6-trans-farnesyl diphosphate = amorpha-4,11-diene +
            diphosphate [RN:R07630]
ALL_REAC    R07630
SUBSTRATE   2-trans,6-trans-farnesyl diphosphate [CPD:C00448]
PRODUCT     amorpha-4,11-diene [CPD:C16028];
            diphosphate [CPD:C00013]
COMMENT     Requires Mg2+ and Mn2+ for activity. This is a key enzyme in the
            biosynthesis of the antimalarial endoperoxide artemisinin [3].
            Catalyses the formation of both olefinic [e.g. amorpha-4,11-diene,
            amorpha-4,7(11)-diene, gamma-humulene and beta-sesquiphellandrene]
            and oxygenated (e.g. amorpha-4-en-7-ol) sesquiterpenes, with
            amorpha-4,11-diene being the major product. When geranyl diphosphate
            is used as a substrate, no monoterpenes are produced [2].
REFERENCE   1  [PMID:11289612]
  AUTHORS   Wallaart TE, Bouwmeester HJ, Hille J, Poppinga L, Maijers NC.
  TITLE     Amorpha-4,11-diene synthase: cloning and functional expression of a
            key enzyme in the biosynthetic pathway of the novel antimalarial
            drug artemisinin.
  JOURNAL   Planta. 212 (2001) 460-5.
  ORGANISM  Artemisia annua
REFERENCE   2  [PMID:11032404]
  AUTHORS   Mercke P, Bengtsson M, Bouwmeester HJ, Posthumus MA, Brodelius PE.
  TITLE     Molecular cloning, expression, and characterization of
            amorpha-4,11-diene synthase, a key enzyme of artemisinin
            biosynthesis in Artemisia annua L.
  JOURNAL   Arch. Biochem. Biophys. 381 (2000) 173-80.
  ORGANISM  Artemisia annua
REFERENCE   3  [PMID:10626375]
  AUTHORS   Bouwmeester HJ, Wallaart TE, Janssen MH, van Loo B, Jansen BJ,
            Posthumus MA, Schmidt CO, De Kraker JW, Konig WA, Franssen MC.
  TITLE     Amorpha-4,11-diene synthase catalyses the first probable step in
            artemisinin biosynthesis.
  JOURNAL   Phytochemistry. 52 (1999) 843-54.
  ORGANISM  Artemisia annua
REFERENCE   4  [PMID:11185551]
  AUTHORS   Chang YJ, Song SH, Park SH, Kim SU.
  TITLE     Amorpha-4,11-diene synthase of Artemisia annua: cDNA isolation and
            bacterial expression of a terpene synthase involved in artemisinin
            biosynthesis.
  JOURNAL   Arch. Biochem. Biophys. 383 (2000) 178-84.
  ORGANISM  Artemisia annua
REFERENCE   5  [PMID:12778056]
  AUTHORS   Martin VJ, Pitera DJ, Withers ST, Newman JD, Keasling JD.
  TITLE     Engineering a mevalonate pathway in Escherichia coli for production
            of terpenoids.
  JOURNAL   Nat. Biotechnol. 21 (2003) 796-802.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   6  [PMID:16143293]
  AUTHORS   Picaud S, Mercke P, He X, Sterner O, Brodelius M, Cane DE, Brodelius
            PE.
  TITLE     Amorpha-4,11-diene synthase: mechanism and stereochemistry of the
            enzymatic cyclization of farnesyl diphosphate.
  JOURNAL   Arch. Biochem. Biophys. 448 (2006) 150-5.
  ORGANISM  Artemisia annua
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.24
            ExPASy - ENZYME nomenclature database: 4.2.3.24
            ExplorEnz - The Enzyme Database: 4.2.3.24
            ERGO genome analysis and discovery system: 4.2.3.24
            BRENDA, the Enzyme Database: 4.2.3.24
///
ENTRY       EC 4.2.3.25                 Enzyme
NAME        S-linalool synthase;
            LIS;
            Lis;
            3S-linalool synthase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     geranyl-diphosphate diphosphate-lyase [(3S)-linalool-forming]
REACTION    geranyl diphosphate + H2O = (3S)-linalool + diphosphate [RN:R07631]
ALL_REAC    R07631
SUBSTRATE   geranyl diphosphate [CPD:C00341];
            H2O [CPD:C00001]
PRODUCT     (3S)-linalool [CPD:C11389];
            diphosphate [CPD:C00013]
COMMENT     Requires Mn2+ or Mg2+ for activity. Neither (S)- nor (R)-linalyl
            diphosphate can act as substrate for the enzyme from the flower
            Clarkia breweri [1]. Unlike many other monoterpene synthases, only a
            single product, (3S)-linalool, is formed.
REFERENCE   1  [PMID:7864636]
  AUTHORS   Pichersky E, Lewinsohn E, Croteau R.
  TITLE     Purification and characterization of S-linalool synthase, an enzyme
            involved in the production of floral scent in Clarkia breweri.
  JOURNAL   Arch. Biochem. Biophys. 316 (1995) 803-7.
  ORGANISM  Clarkia breweri
REFERENCE   2  [PMID:11532177]
  AUTHORS   Lucker J, Bouwmeester HJ, Schwab W, Blaas J, van der Plas LH,
            Verhoeven HA.
  TITLE     Expression of Clarkia S-linalool synthase in transgenic petunia
            plants results in the accumulation of
            S-linalyl-beta-D-glucopyranoside.
  JOURNAL   Plant. J. 27 (2001) 315-24.
  ORGANISM  Clarkia breweri
REFERENCE   3  [PMID:8768373]
  AUTHORS   Dudareva N, Cseke L, Blanc VM, Pichersky E.
  TITLE     Evolution of floral scent in Clarkia: novel patterns of S-linalool
            synthase gene expression in the C. breweri flower.
  JOURNAL   Plant. Cell. 8 (1996) 1137-48.
  ORGANISM  Clarkia breweri
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.25
            ExPASy - ENZYME nomenclature database: 4.2.3.25
            ExplorEnz - The Enzyme Database: 4.2.3.25
            ERGO genome analysis and discovery system: 4.2.3.25
            BRENDA, the Enzyme Database: 4.2.3.25
///
ENTRY       EC 4.2.3.26                 Enzyme
NAME        R-linalool synthase;
            (3R)-linalool synthase;
            (-)-3R-linalool synthase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     geranyl-diphosphate diphosphate-lyase [(3R)-linalool-forming]
REACTION    geranyl diphosphate + H2O = (3R)-linalool + diphosphate [RN:R07632]
ALL_REAC    R07632
SUBSTRATE   geranyl diphosphate [CPD:C00341];
            H2O [CPD:C00001]
PRODUCT     (3R)-linalool [CPD:C11388];
            diphosphate [CPD:C00013]
COMMENT     Geranyl diphosphate cannot be replaced by isopentenyl diphosphate,
            dimethylallyl diphosphate, farnesyl diphosphate or geranylgeranyl
            diphosphate as substrate [1]. Requires Mg2+ or Mn2+ for activity.
            Unlike many other monoterpene synthases, only a single product,
            (3R)-linalool, is formed.
REFERENCE   1  [PMID:10562427]
  AUTHORS   Jia JW, Crock J, Lu S, Croteau R, Chen XY.
  TITLE     (3R)-Linalool synthase from Artemisia annua L.: cDNA isolation,
            characterization, and wound induction.
  JOURNAL   Arch. Biochem. Biophys. 372 (1999) 143-9.
  ORGANISM  Artemisia annua
REFERENCE   2  [PMID:12176064]
  AUTHORS   Crowell AL, Williams DC, Davis EM, Wildung MR, Croteau R.
  TITLE     Molecular cloning and characterization of a new linalool synthase.
  JOURNAL   Arch. Biochem. Biophys. 405 (2002) 112-21.
  ORGANISM  Mentha citrata
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.26
            ExPASy - ENZYME nomenclature database: 4.2.3.26
            ExplorEnz - The Enzyme Database: 4.2.3.26
            ERGO genome analysis and discovery system: 4.2.3.26
            BRENDA, the Enzyme Database: 4.2.3.26
///
ENTRY       EC 4.2.3.27                 Enzyme
NAME        isoprene synthase;
            ISPC;
            ISPS
CLASS       Lyases;
            Carbon-oxygen lyases;
            Acting on phosphates
SYSNAME     dimethylallyl-diphosphate diphosphate-lyase (isoprene-forming)
REACTION    dimethylallyl diphosphate = isoprene + diphosphate
SUBSTRATE   dimethylallyl diphosphate [CPD:C00235]
PRODUCT     isoprene;
            diphosphate [CPD:C00013]
COMMENT     Requires Mg2+ or Mn2+ for activity. This enzyme is located in the
            chloroplast of isoprene-emitting plants, such as poplar and aspen,
            and may be activitated by light-dependent changes in chloroplast pH
            and Mg2+ concentration [2,8].
REFERENCE   1  [PMID:16668590]
  AUTHORS   Silver GM, Fall R.
  TITLE     Enzymatic Synthesis of Isoprene from Dimethylallyl Diphosphate in
            Aspen Leaf Extracts.
  JOURNAL   Plant. Physiol. 97 (1991) 1588-1591.
REFERENCE   2  [PMID:7768893]
  AUTHORS   Silver GM, Fall R.
  TITLE     Characterization of aspen isoprene synthase, an enzyme responsible
            for leaf isoprene emission to the atmosphere.
  JOURNAL   J. Biol. Chem. 270 (1995) 13010-6.
REFERENCE   3  [PMID:12226383]
  AUTHORS   Wildermuth MC, Fall R.
  TITLE     Light-Dependent Isoprene Emission (Characterization of a
            Thylakoid-Bound Isoprene Synthase in Salix discolor Chloroplasts).
  JOURNAL   Plant. Physiol. 112 (1996) 171-182.
REFERENCE   4
  AUTHORS   Schnitzler, J.P., Arenz, R., Steinbrecher, R. and Lehming, A.
  TITLE     Characterization of an isoprene synthase from leaves of Quercus
            petraea.
  JOURNAL   Bot. Acta 109 (1996) 216-221.
REFERENCE   5  [PMID:11506373]
  AUTHORS   Miller B, Oschinski C, Zimmer W.
  TITLE     First isolation of an isoprene synthase gene from poplar and
            successful expression of the gene in Escherichia coli.
  JOURNAL   Planta. 213 (2001) 483-7.
REFERENCE   6  [PMID:12054742]
  AUTHORS   Sivy TL, Shirk MC, Fall R.
  TITLE     Isoprene synthase activity parallels fluctuations of isoprene
            release during growth of Bacillus subtilis.
  JOURNAL   Biochem. Biophys. Res. Commun. 294 (2002) 71-5.
REFERENCE   7  [PMID:15848197]
  AUTHORS   Sasaki K, Ohara K, Yazaki K.
  TITLE     Gene expression and characterization of isoprene synthase from
            Populus alba.
  JOURNAL   FEBS. Lett. 579 (2005) 2514-8.
REFERENCE   8  [PMID:16052321]
  AUTHORS   Schnitzler JP, Zimmer I, Bachl A, Arend M, Fromm J, Fischbach RJ.
  TITLE     Biochemical properties of isoprene synthase in poplar (Populus x
            canescens).
  JOURNAL   Planta. 222 (2005) 777-86.
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.3.27
            ExPASy - ENZYME nomenclature database: 4.2.3.27
            ExplorEnz - The Enzyme Database: 4.2.3.27
            ERGO genome analysis and discovery system: 4.2.3.27
            BRENDA, the Enzyme Database: 4.2.3.27
///
ENTRY       EC 4.2.99.1       Obsolete  Enzyme
NAME        Transferred to 4.2.2.1
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Transferred entry: now EC 4.2.2.1 hyaluronate lyase (EC 4.2.99.1
            created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.1
            ExPASy - ENZYME nomenclature database: 4.2.99.1
            ExplorEnz - The Enzyme Database: 4.2.99.1
            ERGO genome analysis and discovery system: 4.2.99.1
            BRENDA, the Enzyme Database: 4.2.99.1
///
ENTRY       EC 4.2.99.2       Obsolete  Enzyme
NAME        Transferred to 4.2.3.1
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Transferred entry: now EC 4.2.3.1 threonine synthase (EC 4.2.99.2
            created 1961, deleted 2000)
STRUCTURES  PDB: 1E5X  1KL7  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.2
            ExPASy - ENZYME nomenclature database: 4.2.99.2
            ExplorEnz - The Enzyme Database: 4.2.99.2
            ERGO genome analysis and discovery system: 4.2.99.2
            BRENDA, the Enzyme Database: 4.2.99.2
///
ENTRY       EC 4.2.99.3       Obsolete  Enzyme
NAME        Transferred to 4.2.2.2
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Transferred entry: now EC 4.2.2.2 pectate lyase (EC 4.2.99.3 created
            1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.3
            ExPASy - ENZYME nomenclature database: 4.2.99.3
            ExplorEnz - The Enzyme Database: 4.2.99.3
            ERGO genome analysis and discovery system: 4.2.99.3
            BRENDA, the Enzyme Database: 4.2.99.3
///
ENTRY       EC 4.2.99.4       Obsolete  Enzyme
NAME        Transferred to 4.2.2.3
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Transferred entry: now EC 4.2.2.3, poly(beta-D-mannuronate) lyase
            (EC 4.2.99.4 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.4
            ExPASy - ENZYME nomenclature database: 4.2.99.4
            ExplorEnz - The Enzyme Database: 4.2.99.4
            ERGO genome analysis and discovery system: 4.2.99.4
            BRENDA, the Enzyme Database: 4.2.99.4
///
ENTRY       EC 4.2.99.5       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Deleted entry: polyglucuronide lyase (EC 4.2.99.5 created 1965,
            deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.5
            ExPASy - ENZYME nomenclature database: 4.2.99.5
            ExplorEnz - The Enzyme Database: 4.2.99.5
            ERGO genome analysis and discovery system: 4.2.99.5
            BRENDA, the Enzyme Database: 4.2.99.5
///
ENTRY       EC 4.2.99.6       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Deleted entry: chondroitin sulfate lyase. Now included with EC
            4.2.2.4 (chondroitin ABC lyase) and EC 4.2.2.5 (chondroitin AC
            lyase) (EC 4.2.99.6 created 1965, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.6
            ExPASy - ENZYME nomenclature database: 4.2.99.6
            ExplorEnz - The Enzyme Database: 4.2.99.6
            ERGO genome analysis and discovery system: 4.2.99.6
            BRENDA, the Enzyme Database: 4.2.99.6
///
ENTRY       EC 4.2.99.7       Obsolete  Enzyme
NAME        Transferred to 4.2.3.2
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Transferred entry: now EC 4.2.3.2 ethanolamine-phosphate
            phospho-lyase (EC 4.2.99.7 created 1972, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.7
            ExPASy - ENZYME nomenclature database: 4.2.99.7
            ExplorEnz - The Enzyme Database: 4.2.99.7
            ERGO genome analysis and discovery system: 4.2.99.7
            BRENDA, the Enzyme Database: 4.2.99.7
///
ENTRY       EC 4.2.99.8       Obsolete  Enzyme
NAME        Transferred to 2.5.1.47
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Transferred entry: now EC 2.5.1.47 cysteine synthase (EC 4.2.99.8
            created 1972, modified 1976, modified 1990, deleted 2002)
GENES       SAT: SYN_01255
STRUCTURES  PDB: 1D6S  1FCJ  1OAS  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.8
            ExPASy - ENZYME nomenclature database: 4.2.99.8
            ExplorEnz - The Enzyme Database: 4.2.99.8
            ERGO genome analysis and discovery system: 4.2.99.8
            BRENDA, the Enzyme Database: 4.2.99.8
///
ENTRY       EC 4.2.99.9       Obsolete  Enzyme
NAME        Transferred to 2.5.1.48
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Transferred entry: now EC 2.5.1.48 cystathionine gamma-synthase (EC
            4.2.99.9 created 1972, deleted 2002)
STRUCTURES  PDB: 1CS1  1I41  1I43  1I48  1QGN  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.9
            ExPASy - ENZYME nomenclature database: 4.2.99.9
            ExplorEnz - The Enzyme Database: 4.2.99.9
            ERGO genome analysis and discovery system: 4.2.99.9
            BRENDA, the Enzyme Database: 4.2.99.9
///
ENTRY       EC 4.2.99.10      Obsolete  Enzyme
NAME        Transferred to 2.5.1.49
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Transferred entry: now EC 2.5.1.49 O-acetylhomoserine
            aminocarboxypropyltransferase (EC 4.2.99.10 created 1972, deleted
            2002)
STRUCTURES  PDB: 2CB1  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.10
            ExPASy - ENZYME nomenclature database: 4.2.99.10
            ExplorEnz - The Enzyme Database: 4.2.99.10
            ERGO genome analysis and discovery system: 4.2.99.10
            BRENDA, the Enzyme Database: 4.2.99.10
///
ENTRY       EC 4.2.99.11      Obsolete  Enzyme
NAME        Transferred to 4.2.3.3
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Transferred entry: now EC 4.2.3.3 methylglyoxal synthase (EC
            4.2.99.11 created 1972, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.11
            ExPASy - ENZYME nomenclature database: 4.2.99.11
            ExplorEnz - The Enzyme Database: 4.2.99.11
            ERGO genome analysis and discovery system: 4.2.99.11
            BRENDA, the Enzyme Database: 4.2.99.11
///
ENTRY       EC 4.2.99.12                Enzyme
NAME        carboxymethyloxysuccinate lyase;
            carbon-oxygen lyase;
            carboxymethyloxysuccinate glycolate-lyase
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
SYSNAME     carboxymethyloxysuccinate glycolate-lyase (fumarate-forming)
REACTION    carboxymethyloxysuccinate = fumarate + glycolate [RN:R01336]
ALL_REAC    R01336
SUBSTRATE   carboxymethyloxysuccinate [CPD:C03600]
PRODUCT     fumarate [CPD:C00122];
            glycolate [CPD:C00160]
REFERENCE   1  [PMID:4831330]
  AUTHORS   Peterson D, Llaneza J.
  TITLE     Identification of a carbon-oxygen lyase activity cleaving the ether
            linkage in carboxymethyloxysuccinic acid.
  JOURNAL   Arch. Biochem. Biophys. 162 (1974) 135-46.
  ORGANISM  Zoogloea sp.
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.12
            ExPASy - ENZYME nomenclature database: 4.2.99.12
            ExplorEnz - The Enzyme Database: 4.2.99.12
            ERGO genome analysis and discovery system: 4.2.99.12
            BRENDA, the Enzyme Database: 4.2.99.12
            CAS: 53167-89-8
///
ENTRY       EC 4.2.99.13      Obsolete  Enzyme
NAME        Transferred to 2.5.1.50
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Transferred entry: now EC 2.5.1.50 zeatin
            9-aminocarboxyethyltransferase (EC 4.2.99.13 created 1984, deleted
            2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.13
            ExPASy - ENZYME nomenclature database: 4.2.99.13
            ExplorEnz - The Enzyme Database: 4.2.99.13
            ERGO genome analysis and discovery system: 4.2.99.13
            BRENDA, the Enzyme Database: 4.2.99.13
///
ENTRY       EC 4.2.99.14      Obsolete  Enzyme
NAME        Transferred to 2.5.1.51
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Transferred entry: now EC 2.5.1.51 beta-pyrazolylalanine synthase
            (EC 4.2.99.14 created 1989 (EC 4.2.99.17 incorporated 1992), deleted
            2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.14
            ExPASy - ENZYME nomenclature database: 4.2.99.14
            ExplorEnz - The Enzyme Database: 4.2.99.14
            ERGO genome analysis and discovery system: 4.2.99.14
            BRENDA, the Enzyme Database: 4.2.99.14
///
ENTRY       EC 4.2.99.15      Obsolete  Enzyme
NAME        Transferred to 2.5.1.52
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Transferred entry: now EC 2.5.1.52 L-mimosine synthase (EC 4.2.99.15
            created 1989, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.15
            ExPASy - ENZYME nomenclature database: 4.2.99.15
            ExplorEnz - The Enzyme Database: 4.2.99.15
            ERGO genome analysis and discovery system: 4.2.99.15
            BRENDA, the Enzyme Database: 4.2.99.15
///
ENTRY       EC 4.2.99.16      Obsolete  Enzyme
NAME        Transferred to 2.5.1.53
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Transferred entry: now EC 2.5.1.53 uracilylalanine synthase (EC
            4.2.99.16 created 1990, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.16
            ExPASy - ENZYME nomenclature database: 4.2.99.16
            ExplorEnz - The Enzyme Database: 4.2.99.16
            ERGO genome analysis and discovery system: 4.2.99.16
            BRENDA, the Enzyme Database: 4.2.99.16
///
ENTRY       EC 4.2.99.17      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Deleted entry: listed as EC 2.5.1.51, beta-pyrazolylalanine synthase
            (EC 4.2.99.17 created 1992, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.17
            ExPASy - ENZYME nomenclature database: 4.2.99.17
            ExplorEnz - The Enzyme Database: 4.2.99.17
            ERGO genome analysis and discovery system: 4.2.99.17
            BRENDA, the Enzyme Database: 4.2.99.17
///
ENTRY       EC 4.2.99.18                Enzyme
NAME        DNA-(apurinic or apyrimidinic site) lyase;
            AP lyase;
            AP endonuclease class I;
            endodeoxyribonuclease (apurinic or apyrimidinic);
            deoxyribonuclease (apurinic or apyrimidinic);
            E. coli endonuclease III;
            phage-T4 UV endonuclease;
            Micrococcus luteus UV endonuclease;
            AP site-DNA 5'-phosphomonoester-lyase;
            X-ray endonuclease III
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
SYSNAME     DNA-(apurinic or apyrimidinic site) 5'-phosphomonoester-lyase
REACTION    The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is
            broken by a beta-elimination reaction, leaving a 3'-terminal
            unsaturated sugar and a product with a terminal 5'-phosphate
COMMENT     'Nicking' of the phosphodiester bond is due to a lyase-type
            reaction, not hydrolysis. This group of enzymes was previously
            listed as endonucleases, under EC 3.1.25.2.
REFERENCE   1  [PMID:2471512]
  AUTHORS   Bailly V, Sente B, Verly WG.
  TITLE     Bacteriophage-T4 and Micrococcus luteus UV endonucleases are not
            endonucleases but beta-elimination and sometimes beta
            delta-elimination catalysts.
  JOURNAL   Biochem. J. 259 (1989) 751-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:2439070]
  AUTHORS   Bailly V, Verly WG.
  TITLE     Escherichia coli endonuclease III is not an endonuclease but a
            beta-elimination catalyst.
  JOURNAL   Biochem. J. 242 (1987) 565-72.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:2471157]
  AUTHORS   Bailly V, Verly WG.
  TITLE     AP endonucleases and AP lyases.
  JOURNAL   Nucleic. Acids. Res. 17 (1989) 3617-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4
  AUTHORS   Manoharan, M., Mazumder, A., Ransom, S.C., Gerlt, J.A. and Bolton,
            P.H.
  TITLE     Mechanism of UV endonuclease-V cleavage of abasic sites in DNA
            determined by C-13 labeling.
  JOURNAL   J. Am. Chem. Soc. 110 (1988) 2690-2691.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01741  DNA-(apurinic or apyrimidinic site) lyase
GENES       HSA: 252969(NEIL2) 328(APEX1) 4913(NTHL1) 4968(OGG1) 79661(NEIL1)
            PTR: 463992(NEIL2) 465200(APEX1)
            MMU: 11792(Apex1) 18207(Nthl1) 18294(Ogg1) 382913(Neil2)
                 72774(Neil1)
            RNO: 79116(Apex1) 81528(Ogg1)
            CFA: 482558(APEX1) 484666(OGG1) 486078(NEIL2) 611615(NEIL1)
            BTA: 281630(APEX1) 444987(NEIL2)
            GGA: 422037(NEIL2) 770068(RCJMB04_9m20) 771001(OGG1)
            DRE: 393253(zgc:56361) 406730(apex1)
            SPU: 584564(LOC584564) 586897(LOC586897)
            DME: Dmel_CG3178(Rrp1)
            CEL: R10E4.5(endonuclease) T05H10.2(apn-1)
            ATH: AT1G21710(OGG1)
            CME: CMG142C CML016C CML249C
            SCE: YBL019W(APN2) YKL114C(APN1) YML060W(OGG1)
            AGO: AGOS_ABL054C AGOS_ACR278W AGOS_AER127C AGOS_AFR016W
            PIC: PICST_28317(APN2) PICST_30161 PICST_35111(OGG1)
            CGR: CAGL0J04356g
            SPO: SPAC30D11.07 SPBC3D6.10 SPCC622.17(apn1)
            ANI: AN3947.2 AN4736.2 AN6682.2
            AFM: AFUA_6G03760 AFUA_6G08110 AFUA_7G05320
            AOR: AO090005000260 AO090020000091
            CNE: CNB02890
            UMA: UM00618.1 UM01304.1
            ECU: ECU08_0880
            DDI: DDB_0206584(apnA) DDB_0232975(apnB) DDB_0233024(ogg1)
            PFA: MAL3P2.19 PF11_0306 PF13_0176 PFF0715c PFI0835c
            CPV: cgd1_310 cgd8_2020
            CHO: Chro.10041 Chro.70202 Chro.80237
            TAN: TA02660 TA05440 TA12590 TA16100
            TPV: TP02_0334 TP03_0162
            TET: TTHERM_01106120
            TBR: Tb11.01.2410 Tb11.01.3910 Tb927.4.2480 Tb927.8.5510
            TCR: 504005.10 507083.30 509901.170 511481.50
            LMA: LmjF09.0050 LmjF16.0680
            EHI: 234.t00010 38.t00008 62.t00015
            ECO: b1633(nth)
            ECJ: JW1625(nth)
            ECE: Z2644(nth)
            ECS: ECs2342
            ECC: c2025(nth)
            ECI: UTI89_C1823(nth)
            ECP: ECP_1578
            ECW: EcE24377A_0740(nei) EcE24377A_1842(nth)
            ECX: EcHS_A0691 EcHS_A0762 EcHS_A1709
            STY: STY1669(nth)
            STT: t1321(nth)
            SPT: SPA1400(nth)
            SEC: SC1471(nth)
            STM: STM1453(nth)
            YPE: YPO2239(nth)
            YPK: y2080(nth)
            YPM: YP_2037(nth)
            YPS: YPTB2160(nth)
            YPI: YpsIP31758_1901(nth)
            SFL: SF1658(nth)
            SFX: S1790(nth)
            ECA: ECA2282(nth)
            PLU: plu2383(nth)
            BUC: BU119(nth)
            BAS: BUsg111(nth)
            BAB: bbp114(nth)
            WBR: WGLp339(nth)
            SPE: Spro_1261 Spro_2234
            BFL: Bfl372(nth)
            HIN: HI1689(nth)
            HIT: NTHI1996(nth)
            HDU: HD1115(nth)
            HSO: HS_1065(nth)
            PMU: PM0381(nth)
            MSU: MS0916(nth)
            APL: APL_0886(nth)
            ASU: Asuc_1741
            XFA: XF0647
            XFT: PD1523(nth)
            XCC: XCC1532(nth)
            XCB: XC_2702
            XCV: XCV1623
            XAC: XAC1582(nth)
            XOO: XOO2454(nth)
            VCH: VC1011
            VCO: VC0395_A0532(nth)
            VVU: VV1_3099
            VVY: VV1186
            VPA: VP2108
            VFI: VF0929
            PPR: PBPRA2566
            PAE: PA3495(nth)
            PAP: PSPA7_1634(nth)
            PPU: PP_1092(nth)
            PPF: Pput_1133
            PST: PSPTO_4149(nth)
            PSB: Psyr_3888
            PSP: PSPPH_1376(nth)
            PFL: PFL_4850(nth)
            PFO: Pfl_4513
            PEN: PSEEN1214(nth)
            PMY: Pmen_1398
            PAR: Psyc_0829(nth)
            PRW: PsycPRwf_0880
            ACI: ACIAD1108(nth)
            SON: SO_2514(nth)
            SBM: Shew185_2059
            SSE: Ssed_2038
            SPL: Spea_2359
            ILO: IL1800(nth)
            CPS: CPS_2193(nth)
            PHA: PSHAa1099(nth)
            CBU: CBU_1697(nth)
            CBD: COXBU7E912_0305(nth)
            LPN: lpg2880(nth)
            LPF: lpl2793(nth)
            LPP: lpp2939(nth)
            MCA: MCA2899
            FTU: FTT0648c(nth)
            FTF: FTF0648c(nth)
            FTW: FTW_1081(nth)
            FTH: FTH_0901(nth)
            FTA: FTA_0971(nth)
            NOC: Noc_1169
            HCH: HCH_01887(nth)
            ABO: ABO_1617(nth)
            MMW: Mmwyl1_1539
            AHA: AHA_2640(nth)
            DNO: DNO_0548(nth)
            RMA: Rmag_0996
            VOK: COSY_0847(nth)
            NME: NMB0533
            NMA: NMA0711(nth)
            NMC: NMC0472(nth)
            NGO: NGO0139
            CVI: CV_3293(nth)
            RSO: RSc1005(nth)
            REU: Reut_A0194 Reut_A1046
            REH: H16_A1147(nth)
            BMA: BMA1931(nth)
            BMV: BMASAVP1_A1022(nth)
            BML: BMA10299_A0843(nth)
            BMN: BMA10247_0305(nth)
            BXE: Bxe_A3311
            BVI: Bcep1808_3189
            BUR: Bcep18194_A6456
            BCN: Bcen_2491
            BCH: Bcen2424_3105
            BAM: Bamb_3160
            BPS: BPSL1103(nth)
            BPM: BURPS1710b_1336(nth)
            BPL: BURPS1106A_1183(nth)
            BPD: BURPS668_1175(nth)
            BTE: BTH_I0970(nth)
            PNU: Pnuc_2008
            BPE: BP3578(nth)
            BPA: BPP3334(nth)
            BBR: BB3785(nth)
            PNA: Pnap_0167
            AAV: Aave_0288
            AJS: Ajs_0233
            VEI: Veis_1619
            MPT: Mpe_A2297
            HAR: HEAR0799(nth)
            MMS: mma_0716
            NEU: NE2223(nth)
            NMU: Nmul_A2704
            EBA: ebA4877(nth)
            AZO: azo1435(nth)
            DAR: Daro_1155
            TBD: Tbd_2021
            HPY: HP0585(nth) HP0602
            HPJ: jhp0549
            HPA: HPAG1_0564 HPAG1_0583
            HHE: HH1575(nth) HH1787(magIII)
            HAC: Hac_1401 Hac_1427(nth)
            WSU: WS1060(NTH) WS1507
            TDN: Tmden_0340 Tmden_0516
            CJE: Cj0595c(nth) Cj1083c
            CJR: CJE0698(nth) CJE1226
            CJJ: CJJ81176_0623(nth)
            CJU: C8J_0557(nth) C8J_1024
            CJD: JJD26997_1074(nth)
            CFF: CFF8240_0512(nth)
            CCV: CCV52592_0115(nth)
            CHA: CHAB381_1222(nth)
            ABU: Abu_0623(nth) Abu_1462
            NIS: NIS_0060 NIS_0559(nth) NIS_1458
            SUN: SUN_1197 SUN_1806(nth)
            GSU: GSU1450 GSU3377
            GME: Gmet_1973
            GUR: Gura_2806
            PCA: Pcar_0009 Pcar_2572
            DVU: DVU0990 DVU2338
            DVL: Dvul_0130
            DDE: Dde_0551 Dde_1491
            BBA: Bd0591
            DPS: DP1908 DP2416(exoA)
            AFW: Anae109_1725 Anae109_3737
            MXA: MXAN_1431(nth) MXAN_3148(nth)
            SAT: SYN_00287
            RPR: RP746(nth)
            RTY: RT0731(nth)
            RCO: RC1149(nth)
            RFE: RF_1191(nth)
            RBE: RBE_1306(nth)
            OTS: OTBS_1708(nth)
            WOL: WD0789(nth)
            WBM: Wbm0365
            AMA: AM373(nth)
            APH: APH_0897(nth)
            ERU: Erum2430(nth)
            ERW: ERWE_CDS_02470(nth)
            ERG: ERGA_CDS_02430(nth)
            ECN: Ecaj_0235
            ECH: ECH_0857(nth)
            NSE: NSE_0246(nth)
            PUB: SAR11_0365(nth)
            MLO: mll3176
            PLA: Plav_3568
            SME: SMc02843(nth)
            SMD: Smed_3375
            ATU: Atu4457
            ATC: AGR_L_820
            RET: RHE_CH03671(nth)
            BME: BMEI1782
            BMF: BAB1_0165
            BMS: BR0166(nth)
            BMB: BruAb1_0162(nth)
            BOV: BOV_0159(nth)
            OAN: Oant_0176
            BJA: blr0689
            BRA: BRADO0074(mutM) BRADO0152(nth)
            BBT: BBta_0080(mutM) BBta_0201(nth)
            RPA: RPA0343(nth)
            NWI: Nwi_0205
            BHE: BH00810(nth)
            BQU: BQ00740(nth)
            BBK: BARBAKC583_1316(nth)
            XAU: Xaut_1632
            CCR: CC_2272 CC_3731
            SIL: SPO3581(nth)
            RSP: RSP_1031
            RSQ: Rsph17025_0197
            RDE: RD1_0963(nth)
            HNE: HNE_2040(nth)
            ZMO: ZMO0706(nth)
            SWI: Swit_0203
            GOX: GOX1274
            GBE: GbCGDNIH1_2428
            ACR: Acry_2500
            BSU: BG10956(nth)
            BHA: BH1698(nth)
            BAN: BA1570(nth)
            BAR: GBAA1570(nth)
            BAA: BA_2089
            BAT: BAS1456
            BCE: BC1548
            BCA: BCE_1676(nth)
            BCZ: BCZK0990 BCZK1429(nth)
            BCY: Bcer98_1270
            BTK: BT9727_1428(nth)
            BLI: BL02743(nth)
            BLD: BLi02369(nth)
            BCL: ABC2057(nth)
            BAY: RBAM_020490
            BPU: BPUM_1966
            OIH: OB1042 OB1757(nth)
            GKA: GK2169(nth)
            SAU: SA0565 SA1285(nth)
            SAV: SAV0608 SAV1452(nth)
            SAM: MW0572 MW1342(nth)
            SAR: SAR0617 SAR1463
            SAS: SAS0576 SAS1395
            SAC: SACOL0664 SACOL1492(nth)
            SAB: SAB0561 SAB1316c
            SAA: SAUSA300_1343(nth)
            SAO: SAOUHSC_00612 SAOUHSC_01469
            SAJ: SaurJH9_1511
            SAH: SaurJH1_1540
            SEP: SE0381 SE1140
            SER: SERP0263 SERP1022(nth)
            SHA: SH1460(nth) SH2292
            SSP: SSP1292 SSP2111
            LMO: lmo0658 lmo1894(nth)
            LMF: LMOf2365_0690 LMOf2365_1923(nth)
            LIN: lin0662 lin2008(nth)
            LWE: lwe0626 lwe1913(nth)
            LLA: L0253(nth)
            LLM: llmg_1501(nth)
            SPY: SPy_0929(nth)
            SPZ: M5005_Spy_0730(nth)
            SPM: spyM18_0986
            SPG: SpyM3_0642(nth)
            SPS: SPs1210
            SPH: MGAS10270_Spy0789(nth)
            SPI: MGAS10750_Spy0824(nth)
            SPJ: MGAS2096_Spy0802(nth)
            SPK: MGAS9429_Spy0788(nth)
            SPF: SpyM51077(nth) SpyM51461(fpg)
            SPA: M6_Spy0756
            SPB: M28_Spy0710(nth)
            SPN: SP_1279
            SPR: spr1157(nth)
            SPD: SPD_1135(nth)
            SAG: SAG0468(nth)
            SAN: gbs0515
            SAK: SAK_0570(nth)
            SMU: SMU.1650(end3)
            STC: str1220(nth)
            STL: stu1220(nth)
            SSA: SSA_1607(mutM) SSA_1711(nth)
            SGO: SGO_1533(nth)
            LPL: lp_2860(nth1) lp_3241(nth2)
            LJO: LJ1198
            LAC: LBA1160
            LSA: LSA0916
            LSL: LSL_0691(nth)
            LDB: Ldb1006(nth)
            LBR: LVIS_0818
            LRE: Lreu_0197 Lreu_1311
            EFA: EF1155(nth)
            STH: STH2666 STH2787
            CAC: CAC0689(ntH)
            CPE: CPE1318
            CPF: CPF_1525(nth)
            CPR: CPR_1318(nth)
            CTC: CTC00355
            CNO: NT01CX_1394
            CTH: Cthe_0458
            CDF: CD0565(nth)
            CBA: CLB_0250(nth)
            CBH: CLC_0265(nth)
            CBF: CLI_0274(nth)
            CBE: Cbei_0580 Cbei_2355
            AMT: Amet_0585 Amet_3628
            CHY: CHY_1121(nth)
            SWO: Swol_1210
            CSC: Csac_2015
            TTE: TTE1769(nth)
            MTU: Rv3674c(nth)
            MTC: MT3775(pdg)
            MBO: Mb3698c(nth)
            MBB: BCG_3732c(nth)
            MLE: ML2301(nth)
            MPA: MAP0400(nth)
            MAV: MAV_0455(nth)
            MSM: MSMEG_6187(nth)
            MVA: Mvan_1556
            MMC: Mmcs_1211
            MKM: Mkms_1228
            MJL: Mjls_1238
            CGL: NCgl0288(cgl0293)
            CGB: cg0353(nth)
            CEF: CE0289
            CDI: DIP0304(nth)
            CJK: jk1971(nth)
            NFA: nfa3480
            RHA: RHA1_ro02178 RHA1_ro04323 RHA1_ro06240
            SCO: SCO3569(SCH17.03c)
            SMA: SAV4593(nth)
            AAU: AAur_3351(nth)
            PAC: PPA0223
            TFU: Tfu_0118 Tfu_1541
            FAL: FRAAL6558(nth)
            KRA: Krad_0151 Krad_0422 Krad_3521
            SEN: SACE_0331(nth) SACE_6601
            STP: Strop_4319 Strop_4491
            BLO: BL0393(nth) BL1081
            BAD: BAD_1448(nth)
            FNU: FN0057 FN0622
            RBA: RB5097
            CTR: CT697(nth)
            CTA: CTA_0758(nth)
            CMU: TC0069
            CPN: CPn0837(nth)
            CPA: CP1032
            CPJ: CPj0837(nth)
            CPT: CpB0866
            CCA: CCA00929(nth)
            CAB: CAB898
            PCU: pc0021(nth)
            BBU: BB0745(nth)
            BGA: BG0768(nth)
            TPA: TP0775(nth)
            TDE: TDE2534(nth)
            LIL: LA2163
            LIC: LIC11759(nth)
            LBJ: LBJ_1856
            LBL: LBL_1428
            SYN: slr1822(nth)
            SYW: SYNW1342
            SYC: syc1071_d(nth)
            SYF: Synpcc7942_0447
            SYG: sync_1850(nth)
            SYR: SynRCC307_1045(nth)
            SYX: SynWH7803_0798(nth)
            CYA: CYA_0912(nth)
            CYB: CYB_0991(nth)
            TEL: tll1641
            GVI: gll0656 gll1821
            ANA: all3970(nth)
            AVA: Ava_1731
            PMA: Pro0880(nth)
            PMM: PMM0802
            PMT: PMT0504
            PMN: PMN2A_0210
            PMB: A9601_08661(nth)
            PMC: P9515_07791(nth)
            PMF: P9303_17641(nth)
            PMG: P9301_08631(nth)
            PMH: P9215_08971
            PME: NATL1_08421(nth)
            BTH: BT_1671
            BFR: BF3268
            BFS: BF3106
            PGI: PG1772(nth)
            SRU: SRU_2356(nth)
            CHU: CHU_3695(nth)
            GFO: GFO_1784(nth)
            FJO: Fjoh_0832 Fjoh_2438 Fjoh_2740
            FPS: FP1101(nth)
            CTE: CT1710(nth)
            CCH: Cag_0416
            CPH: Cpha266_2513
            PLT: Plut_0113 Plut_1681
            DET: DET0935(nth) DET1612
            DEH: cbdb_A1706 cbdb_A889(nth)
            DEB: DehaBAV1_0819
            RRS: RoseRS_2523
            RCA: Rcas_2765
            DRA: DR_0289 DR_0928 DR_2438
            DGE: Dgeo_0248
            TTH: TTC1892
            TTJ: TTHA0112
            AAE: aq_172(mutY2) aq_251 aq_282(mutY1) aq_496(mutY3)
            TMA: TM0366 TM0382 TM1821
            TPT: Tpet_0552 Tpet_1106
            TME: Tmel_0438 Tmel_1811
            FNO: Fnod_0399 Fnod_0807
            MJA: MJ0724 MJ1434(nth2)
            MMP: MMP0537(nth1) MMP0586
            MMQ: MmarC5_0582
            MMZ: MmarC7_0254 MmarC7_1306 MmarC7_1555
            MAE: Maeo_0628 Maeo_0859
            MVN: Mevan_0339 Mevan_1314 Mevan_1691
            MAC: MA2268 MA4014 MA4609
            MBA: Mbar_A0569 Mbar_A0936 Mbar_A3333
            MMA: MM_0793 MM_0895 MM_1280 MM_2888
            MBU: Mbur_1101 Mbur_2145 Mbur_2164
            MHU: Mhun_0441
            MBN: Mboo_0350 Mboo_2415
            MTH: MTH1342 MTH746
            MST: Msp_0497
            MKA: MK0193(NTH_1)
            AFU: AF0371 AF1692(nth)
            HAL: VNG0592G(nthA2) VNG0694G(nthB)
            HMA: pNG7116(nthC) rrnAC0265(apl) rrnAC0739(nthA) rrnAC1908(nthD)
                 rrnAC2648(nthB)
            HWA: HQ1151A(nthA) HQ1545A(nthA)
            NPH: NP2746A NP4064A NP4496A
            TAC: Ta0014m Ta0321 Ta0790m
            TVO: TVN0062 TVN0804 TVN1273
            PTO: PTO0481 PTO0593 PTO0898
            PHO: PH1498
            PAB: PAB0459(nth)
            PFU: PF1229(mutY)
            TKO: TK1141
            APE: APE_0150.1
            IHO: Igni_1373
            HBU: Hbut_0266
            SSO: SSO0116(nth-1) SSO0904(ogg) SSO2484(nth-2)
            STO: ST0964 ST1219 ST1401
            SAI: Saci_1264 Saci_1367(ogg) Saci_1497
            MSE: Msed_1434 Msed_1676 Msed_2110
            PAI: PAE0880
            NEQ: NEQ398
STRUCTURES  PDB: 1BIX  1CQG  1CQH  1DE8  1DE9  1DEW  1E9N  1HD7  1N39  1N3A  
                 1N3C  1VYB  2ABK  2I5W  2ISI  2J63  2NOB  2NOE  2NOF  2NOH  
                 2NOI  2NOL  2NOZ  
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.18
            ExPASy - ENZYME nomenclature database: 4.2.99.18
            ExplorEnz - The Enzyme Database: 4.2.99.18
            ERGO genome analysis and discovery system: 4.2.99.18
            BRENDA, the Enzyme Database: 4.2.99.18
            CAS: 61811-29-8
///
ENTRY       EC 4.2.99.19      Obsolete  Enzyme
NAME        Transferred to 4.4.1.23
CLASS       Lyases;
            Carbon-oxygen lyases;
            Other carbon-oxygen lyases
COMMENT     Transferred entry: now EC 4.4.1.23 2-hydroxypropyl-CoM lyase. The
            enzyme was incorrectly classified as acting on a C-O bond rather
            than a C-S bond (EC 4.2.99.19 created 2001, deleted 2005)
GENES       BUR: Bcep18194_C7369
DBLINKS     IUBMB Enzyme Nomenclature: 4.2.99.19
            ExPASy - ENZYME nomenclature database: 4.2.99.19
            ExplorEnz - The Enzyme Database: 4.2.99.19
            ERGO genome analysis and discovery system: 4.2.99.19
            UM-BBD (Biocatalysis/Biodegradation Database): 4.2.99.19
            BRENDA, the Enzyme Database: 4.2.99.19
///
ENTRY       EC 4.3.1.1                  Enzyme
NAME        aspartate ammonia-lyase;
            aspartase;
            fumaric aminase;
            L-aspartase;
            L-aspartate ammonia-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     L-aspartate ammonia-lyase (fumarate-forming)
REACTION    L-aspartate = fumarate + NH3 [RN:R00490]
ALL_REAC    R00490
SUBSTRATE   L-aspartate [CPD:C00049]
PRODUCT     fumarate [CPD:C00122];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Ellfolk, N.
  TITLE     Studies on aspartase. 1. Quantitative separation of aspartase from
            bacterial cells, and its partial purification.
  JOURNAL   Acta Chem. Scand. 7 (1953) 824-830.
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K01744  aspartate ammonia-lyase
GENES       EHI: 22.t00031
            ECO: b4139(aspA)
            ECJ: JW4099(aspA)
            ECE: Z5744(aspA)
            ECS: ECs5120
            ECC: c5222(aspA)
            ECI: UTI89_C4736(aspA)
            ECP: ECP_4383
            ECV: APECO1_2250(aspA)
            ECW: EcE24377A_4694(aspA)
            ECX: EcHS_A4380
            STY: STY4685(aspA)
            STT: t4377(aspA)
            SPT: SPA4142(aspA)
            SEC: SC4204(aspA)
            STM: STM4326(aspA)
            YPE: YPO0348(aspA)
            YPK: y0606(aspA)
            YPM: YP_0502(aspA)
            YPA: YPA_3934
            YPN: YPN_3322
            YPS: YPTB0402(aspA)
            YPI: YpsIP31758_3678(aspA)
            SFL: SF4293(aspA)
            SFX: S4560(aspA)
            SFV: SFV_4295(aspA)
            SSN: SSON_4322(aspA)
            SBO: SBO_4317(aspA)
            SDY: SDY_4444(aspA)
            ECA: ECA0426(aspA1) ECA0621(aspA2)
            PLU: plu4137(aspA)
            WBR: WGLp395(aspA)
            SGL: SG0303
            HIT: NTHI0660(aspA)
            HIP: CGSHiEE_00325(aspA)
            HIQ: CGSHiGG_05965(aspA)
            HDU: HD0564(aspA)
            HSO: HS_0466(aspA)
            PMU: PM1103(aspA)
            MSU: MS1984(aspA)
            APL: APL_1091(aspA)
            VCH: VC2698
            VCO: VC0395_A2270(aspA)
            VVU: VV1_1249
            VVY: VV3118
            VPA: VP2863
            VFI: VF2353
            PPR: PBPRA3391 PBPRB0046
            PAE: PA5429(as)
            PAU: PA14_71650(aspA)
            PAP: PSPA7_6217(aspA)
            PPU: PP_5338(aspA)
            PST: PSPTO_5499(aspA)
            PSB: Psyr_5051
            PSP: PSPPH_5133(aspA)
            PFL: PFL_6128(aspA)
            PFO: Pfl_5625
            PEN: PSEEN5482(aspA)
            ACI: ACIAD1744(aspA)
            SFR: Sfri_0682
            CPS: CPS_2052(aspA)
            HCH: HCH_01841(aspA)
            AHA: AHA_0856(aspA)
            DNO: DNO_0874(aspA)
            BCI: BCI_0593(aspA)
            NME: NMB1029
            NMA: NMA1459(aspA)
            NMC: NMC1185(aspA)
            NGO: NGO0556
            CVI: CV_4112(aspA)
            REU: Reut_A1791
            BUR: Bcep18194_B1984
            BCN: Bcen_4302
            BCH: Bcen2424_4064
            RFR: Rfer_3846
            HAR: HEAR0768(aspA)
            AZO: azo0437
            DAR: Daro_0481
            TBD: Tbd_2119
            HPY: HP0649(aspA)
            HPA: HPAG1_0634
            HAC: Hac_1065(aspA)
            CJE: Cj0087(aspA)
            CJR: CJE0082(aspA)
            CJJ: CJJ81176_0122(aspA)
            CJU: C8J_0079(aspA)
            CJD: JJD26997_0094(aspA)
            CFF: CFF8240_1643(aspA)
            CHA: CHAB381_1555
            CCO: CCC13826_0826(aspA)
            ABU: Abu_1581(aspA)
            GSU: GSU0479(aspA)
            GME: Gmet_3082
            PCA: Pcar_1630
            DVU: DVU1766 DVU1871(aspA)
            DDE: Dde_1663 Dde_3552
            LIP: LI0913(aspA)
            BBA: Bd2857(aspA)
            DPS: DP0352
            SFU: Sfum_0589 Sfum_1842 Sfum_2438
            ATU: Atu3793(aspA)
            ATC: AGR_L_2078
            RET: RHE_PE00351(ansB)
            BME: BMEI0109
            BMF: BAB1_1959(aspA)
            BMS: BR1958(aspA)
            BMB: BruAb1_1934(aspA)
            BOV: BOV_1884(aspA)
            BJA: blr1326(aspA)
            SIL: SPO2663(aspA)
            PDE: Pden_1095
            ABA: Acid345_2689
            BSU: BG10301(ansB)
            BHA: BH1426(ansB)
            BAN: BA0609(aspA-1) BA1800(aspA-2) BA3136(aspA-3)
            BAR: GBAA0609(aspA-1) GBAA1800(aspA-2)
            BAA: BA_1192 BA_2305 BA_3637
            BAT: BAS0576 BAS1667 BAS2915
            BCE: BC0611 BC1740 BC3093
            BCA: BCE_0677(aspA) BCE_1872(aspA)
            BCZ: BCZK0520(aspA) BCZK1614(aspA) BCZK2845(aspA)
            BTK: BT9727_0520(aspA) BT9727_1649(aspA) BT9727_2883(ansB)
            BTL: BALH_0548(aspA) BALH_1582(aspA) BALH_2796(aspA)
            BLI: BL02922 BL05376(ansB)
            BLD: BLi00528(ansB) BLi04139
            BCL: ABC1732(ansB)
            BAY: RBAM_021700
            BPU: BPUM_3018 BPUM_3547
            LPL: lp_2830(ansB)
            LDB: Ldb1750(aspA)
            LBU: LBUL_1622
            LCA: LSEI_2863
            STH: STH833
            CAC: CAC0274(ansB) CAC1652(aspA)
            CTC: CTC00824
            CKL: CKL_1546(aspA1) CKL_2331(aspA2)
            DSY: DSY3182
            TTE: TTE0813(aspA)
            MTA: Moth_1273
            MSM: MSMEG_1677(aspA)
            CGL: NCgl1446(cgl1503)
            CGB: cg1697(aspA)
            CEF: CE1633(aspA)
            CDI: DIP1254(aspA)
            CJK: jk0951(aspA)
            RHA: RHA1_ro02944(aspA1) RHA1_ro04453(aspA2) RHA1_ro04556(aspA3)
            SMA: SAV1315(aspA)
            LXX: Lxx08930(aspA)
            CMI: CMM_2077(aspA)
            AAU: AAur_0572(aspA) AAur_3794(aspA)
            PAC: PPA0094
            SEN: SACE_2829(aspA) SACE_5071(aspA)
            BLO: BL0338(ansB)
            TDE: TDE1993
            GVI: glr1457
            BTH: BT_2755
            BFR: BF4213
            BFS: BF4037(aspA)
            PGI: PG1741(aspA)
            TMA: TM0444
STRUCTURES  PDB: 1J3U  1JSW  
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.1
            ExPASy - ENZYME nomenclature database: 4.3.1.1
            ExplorEnz - The Enzyme Database: 4.3.1.1
            ERGO genome analysis and discovery system: 4.3.1.1
            BRENDA, the Enzyme Database: 4.3.1.1
            CAS: 9027-30-9
///
ENTRY       EC 4.3.1.2                  Enzyme
NAME        methylaspartate ammonia-lyase;
            beta-methylaspartase;
            3-methylaspartase;
            L-threo-3-methylaspartate ammonia-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     L-threo-3-methylaspartate ammonia-lyase (mesaconate-forming)
REACTION    L-threo-3-methylaspartate = mesaconate + NH3 [RN:R03696]
ALL_REAC    R03696
SUBSTRATE   L-threo-3-methylaspartate [CPD:C03618]
PRODUCT     mesaconate [CPD:C01732];
            NH3 [CPD:C00014]
COFACTOR    Cobamide [CPD:C00210]
COMMENT     A cobalamin protein.
REFERENCE   1  [PMID:13618029]
  AUTHORS   BARKER HA, SMYTH RD, WAWSZKIEWICZ EJ, LEE MN, WILSON RM.
  TITLE     Enzymic preparation and characterization of an
            alpha-L-beta-methylaspartic acid.
  JOURNAL   Arch. Biochem. Biophys. 78 (1958) 468-76.
  ORGANISM  Clostridium tetanomorphum
REFERENCE   2
  AUTHORS   Bright, H.J. and Ingraham, L.L.
  TITLE     The preparation of crystalline beta-methylaspartase.
  JOURNAL   Biochim. Biophys. Acta 44 (1960) 586-588.
  ORGANISM  Clostridium tetanomorphum
PATHWAY     PATH: map00660  C5-Branched dibasic acid metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K04835  methylaspartate ammonia-lyase
GENES       AFM: AFUA_3G00790
            AOR: AO090010000710
            ECE: Z0892
            ECS: ECs0761
            YEN: YE4043
            SDY: SDY_0673
            BPE: BP0806 BP3177
            BPA: BPP3422 BPP3864
            BBR: BB3872 BB4337
            MLO: mlr6095
            CTC: CTC02563
            AMT: Amet_3414
            CHY: CHY_0484 CHY_0582
            DSY: DSY3233
            DRM: Dred_2689
            TDE: TDE2235
            HAL: VNG2289G(mal)
            HMA: rrnAC0687(mal)
STRUCTURES  PDB: 1KCZ  1KD0  1KKO  1KKR  
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.2
            ExPASy - ENZYME nomenclature database: 4.3.1.2
            ExplorEnz - The Enzyme Database: 4.3.1.2
            ERGO genome analysis and discovery system: 4.3.1.2
            BRENDA, the Enzyme Database: 4.3.1.2
            CAS: 9033-26-5
///
ENTRY       EC 4.3.1.3                  Enzyme
NAME        histidine ammonia-lyase;
            histidase;
            histidinase;
            histidine alpha-deaminase;
            L-histidine ammonia-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     L-histidine ammonia-lyase (urocanate-forming)
REACTION    L-histidine = urocanate + NH3 [RN:R01168]
ALL_REAC    R01168;
            (other) R06132
SUBSTRATE   L-histidine [CPD:C00135]
PRODUCT     urocanate [CPD:C00785];
            NH3 [CPD:C00014]
REFERENCE   1  [PMID:13061415]
  AUTHORS   MEHLER AH, TABOR H.
  TITLE     Deamination of histidine to form urocanic acid in liver.
  JOURNAL   J. Biol. Chem. 201 (1953) 775-84.
  ORGANISM  guinea pig, Pseudomonas fluorescens
PATHWAY     PATH: map00340  Histidine metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K01745  histidine ammonia-lyase
GENES       HSA: 3034(HAL)
            PTR: 452144(HAL)
            MMU: 15109(Hal)
            RNO: 29301(Hal)
            CFA: 475433(HAL)
            GGA: 378924(HAL)
            XLA: 444493(MGC81887) 446479(hal)
            XTR: 448568(hal)
            SPU: 583726(LOC583726)
            CEL: F47B10.2
            DDI: DDB_0231727
            TCR: 506247.220
            STY: STY0824(hutH)
            STT: t2096(hutH)
            SPT: SPA1961(hutH)
            SEC: SC0789(hutH)
            STM: STM0791(hutH)
            YPE: YPO4016(hutH)
            YPK: y4037
            YPM: YP_3379(hutH)
            YPA: YPA_4104
            YPN: YPN_3664
            YPP: YPDSF_3759
            YPS: YPTB3851(hutH)
            YPI: YpsIP31758_4085(hutH)
            PLU: plu2234 plu3192(hutH)
            ENT: Ent638_1264
            SPE: Spro_0799 Spro_0804
            XCC: XCC1579(hutH)
            XCB: XC_2655
            XCV: XCV1678(hutH)
            XAC: XAC1637(hutH)
            XOO: XOO2398(hutH)
            XOM: XOO_2278(XOO2278)
            VCH: VC1202
            VCO: VC0395_A0822(hutH)
            VVU: VV1_0053 VV1_2389
            VVY: VV1074 VV1952
            VPA: VP0889 VP1273
            VFI: VF0852 VFA0450(hutH)
            PPR: PBPRA2173 PBPRB0112
            PAE: PA5093 PA5098(hutH)
            PAU: PA14_67260 PA14_67320(hutH)
            PAP: PSPA7_5827(hutH2) PSPA7_5831(hutH1)
            PPU: PP_5032(hutH)
            PPF: Pput_4906
            PST: PSPTO_5099(hutH-1) PSPTO_5274(hutH-2) PSPTO_5275(hutH-3)
            PSB: Psyr_4832 Psyr_4833(hutH)
            PSP: PSPPH_0422 PSPPH_4864(hutH1) PSPPH_4865(hutH2)
            PFL: PFL_0406(hutH) PFL_0407(hutH) PFL_0472
            PFO: Pfl_0365 Pfl_0366
            PEN: PSEEN0356 PSEEN2604(hutH-2) PSEEN5096(hutH)
            PMY: Pmen_4069
            PCR: Pcryo_1932
            PRW: PsycPRwf_0850
            ACI: ACIAD0574(hutH)
            SON: SO_0098(hutH) SO_3057 SO_4374
            SDN: Sden_0084
            SFR: Sfri_0346 Sfri_3952
            SAZ: Sama_1631 Sama_3385
            SBL: Sbal_0336 Sbal_4251
            SBM: Shew185_0098 Shew185_0334
            SLO: Shew_3517 Shew_3756
            SPC: Sputcn32_0080 Sputcn32_0440
            SSE: Ssed_0319 Ssed_4446
            SPL: Spea_3894 Spea_4168
            SHE: Shewmr4_0100 Shewmr4_0344
            SHM: Shewmr7_0095 Shewmr7_3682
            SHN: Shewana3_0101 Shewana3_0335 Shewana3_1490 Shewana3_3829
            SHW: Sputw3181_0294 Sputw3181_3997
            ILO: IL0134(hutH_1) IL2450(hutH_2)
            CPS: CPS_0908(hutH)
            PHA: PSHAa2740(hutH) PSHAb0401
            PAT: Patl_1022
            PIN: Ping_1029
            LPN: lpg1380
            LPF: lpl1331(hutH)
            LPP: lpp1335(hutH)
            HHA: Hhal_1820
            HCH: HCH_04172(hutH)
            MMW: Mmwyl1_3901
            AHA: AHA_0380(hutH) AHA_3390
            CVI: CV_0325(hutH)
            RSO: RSc2646(hutH1) RSp0365(hutH2)
            REU: Reut_A2716 Reut_B5637
            REH: H16_A3018(hutH)
            RME: Rmet_0231 Rmet_2855 Rmet_5047
            BMA: BMA0645(hutH)
            BMV: BMASAVP1_A2366(hutH)
            BML: BMA10299_A2919(hutH)
            BMN: BMA10247_1681(hutH)
            BXE: Bxe_A0933 Bxe_A1482 Bxe_A2947 Bxe_B0058 Bxe_B1825
            BVI: Bcep1808_2247 Bcep1808_5960
            BUR: Bcep18194_A5482 Bcep18194_B3018
            BCN: Bcen_5747 Bcen_5905
            BCH: Bcen2424_2172 Bcen2424_6111
            BAM: Bamb_2211 Bamb_3604
            BPS: BPSL1676 BPSL2344(hutH)
            BPM: BURPS1710b_2187 BURPS1710b_2796(hutH)
            BPL: BURPS1106A_2723(hutH)
            BPD: BURPS668_2667(hutH)
            BTE: BTH_I1820(hutH)
            POL: Bpro_1043 Bpro_1157 Bpro_1160 Bpro_5198
            AAV: Aave_2965
            VEI: Veis_3645
            MMS: mma_0515(hutH)
            EBA: ebA5742(hutH)
            BBA: Bd2753(hutH)
            DPS: DP2353
            ADE: Adeh_1814
            AFW: Anae109_2013
            MXA: MXAN_3465(hutH)
            SFU: Sfum_2378
            MLO: mll0151 mlr1730 mlr8321
            MES: Meso_2985
            PLA: Plav_1493
            SME: SMa0306 SMb21165(hutH1) SMc00669(hutH2)
            SMD: Smed_2586 Smed_4658
            ATU: Atu3803(hutH) Atu3933(hutH)
            ATC: AGR_L_1400GM AGR_L_1825(hutH)
            RET: RHE_CH00352(hutHch) RHE_PE00072(hutHe1) RHE_PE00081(hutHe2)
            RLE: RL0369(hutH) RL4470(hutH) pRL110205(hutH1) pRL110215(hutH2)
                 pRL120749
            BME: BMEII0367 BMEII0368
            BMF: BAB2_0305(hutH)
            BMS: BRA0930(hutH)
            BMB: BruAb2_0303(hutH)
            BOV: BOV_A0872(hutH)
            OAN: Oant_1435
            BJA: bll6242(hutH)
            BRA: BRADO1604(hutH)
            BBT: BBta_6451(hutH)
            BHE: BH06500(hutH)
            BQU: BQ06730(hutH)
            XAU: Xaut_1004
            CCR: CC_0959
            SIL: SPO2192(hutH)
            SIT: TM1040_3005
            RSP: RSP_2935(hutH) RSP_3574(hutH)
            RSH: Rsph17029_1579 Rsph17029_3256
            RDE: RD1_3678(hutH)
            PDE: Pden_0711
            MMR: Mmar10_1603
            HNE: HNE_2396(hutH)
            SAL: Sala_1689
            SWI: Swit_4632
            GOX: GOX1167(hutH)
            ACR: Acry_1747
            RRU: Rru_A1301
            ABA: Acid345_1410
            SUS: Acid_5210
            BSU: BG10667(hutH)
            BHA: BH1982(hutH)
            BAN: BA3712(hutH)
            BAR: GBAA3712(hutH)
            BAA: BA_4195
            BAT: BAS3442
            BCE: BC3652(hutH)
            BCA: BCE_3680(hutH)
            BCZ: BCZK3354(hutH)
            BCY: Bcer98_2312
            BTK: BT9727_3405(hutH)
            BCL: ABC3933(hutH)
            BAY: RBAM_036410(hutH)
            GKA: GK0385(hutH)
            SAU: SA0008(hutH)
            SAV: SAV0008(hutH)
            SAM: MW0008(hutH)
            SAR: SAR0008(hutH)
            SAS: SAS0008(hutH)
            SAC: SACOL0008(hutH)
            SAB: SAB0008(hutH)
            SAA: SAUSA300_0008(hutH)
            SAO: SAOUHSC_00008
            SAJ: SaurJH9_0008
            SAH: SaurJH1_0008
            SSP: SSP0008
            SPY: SPy_2089(hutH)
            SPZ: M5005_Spy_1777(hutH)
            SPM: spyM18_2147
            SPG: SpyM3_1779(hutH)
            SPS: SPs1776
            SPH: MGAS10270_Spy1843(hutH)
            SPI: MGAS10750_Spy1869(hutH)
            SPJ: MGAS2096_Spy1810(hutH)
            SPK: MGAS9429_Spy1788(hutH)
            SPF: SpyM51735(hutH)
            SPA: M6_Spy1774(hutH) M6_Spy1775
            SPB: M28_Spy1761(hutH)
            STC: str1313(hutH)
            STL: stu1313(hutH)
            SSA: SSA_0429(hutH)
            SGO: SGO_1811(hutH)
            STH: STH3194
            CTC: CTC02318
            AMT: Amet_3149
            TTE: TTE0844(hutH)
            MSM: MSMEG_1183(hutH)
            NFA: nfa12280(hutH)
            RHA: RHA1_ro02154(hutH) RHA1_ro02588
            SCO: SCO4932(hutH)
            SMA: SAV3325(hutH1)
            LXX: Lxx22140(hutH)
            ART: Arth_0375
            AAU: AAur_0399(hutH) AAur_3659(hutH)
            PAC: PPA2170(hutH)
            NCA: Noca_4398
            KRA: Krad_4453
            SEN: SACE_6407(hutH)
            STP: Strop_1106
            BLO: BL1249(hutH)
            RXY: Rxyl_0576 Rxyl_0581 Rxyl_1739
            FNU: FN0791 FN1406
            TDE: TDE0588(hutH)
            GVI: glr3066
            AVA: Ava_3988
            BTH: BT_2690
            BFR: BF4144
            BFS: BF3966(hutH)
            PGI: PG0324(hutH)
            SRU: SRU_0722(hutH)
            CHU: CHU_2124(hutH)
            GFO: GFO_1500(hutH) GFO_1668(hutH)
            FJO: Fjoh_1109 Fjoh_2576
            FPS: FP0838(hutH1) FP2287(hutH2)
            DRA: DR_A0147
            DGE: Dgeo_2730
            TME: Tmel_1777
            FNO: Fnod_0129
            HAL: VNG1212Gm(hutH)
            HMA: rrnAC1791(hutH)
            TAC: Ta0242
            TVO: TVN1353
            PTO: PTO0107(hutH)
            PAS: Pars_1482
STRUCTURES  PDB: 1B8F  1EB4  1GK2  1GK3  1GKJ  1GKM  2NYN  
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.3
            ExPASy - ENZYME nomenclature database: 4.3.1.3
            ExplorEnz - The Enzyme Database: 4.3.1.3
            ERGO genome analysis and discovery system: 4.3.1.3
            BRENDA, the Enzyme Database: 4.3.1.3
            CAS: 9013-75-6
///
ENTRY       EC 4.3.1.4                  Enzyme
NAME        formimidoyltetrahydrofolate cyclodeaminase;
            formiminotetrahydrofolate cyclodeaminase;
            5-formimidoyltetrahydrofolate ammonia-lyase (cyclizing)
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     5-formimidoyltetrahydrofolate ammonia-lyase (cyclizing;
            5,10-methenyltetrahydrofolate-forming)
REACTION    5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH3
            [RN:R02302]
ALL_REAC    R02302
SUBSTRATE   5-formimidoyltetrahydrofolate [CPD:C00664]
PRODUCT     5,10-methenyltetrahydrofolate [CPD:C00445];
            NH3 [CPD:C00014]
COMMENT     In eukaroytes, occurs as a bifunctional enzyme that also has
            glutamate formimidoyltransferase (EC 2.1.2.5) activity.
REFERENCE   1
  AUTHORS   Rabinowitz, J.C. and Pricer, W.E.
  TITLE     Formiminotetrahydrofolic acid and methenyltetrahydrofolic acid as
            intermediates in the formation of N10-formyltetrahydrofolic acid.
  JOURNAL   J. Am. Chem. Soc. 78 (1956) 5702-5704.
  ORGANISM  Clostridium cylindrosporum
PATHWAY     PATH: map00670  One carbon pool by folate
ORTHOLOGY   KO: K01746  formiminotetrahydrofolate cyclodeaminase
GENES       HSA: 10841(FTCD)
            PTR: 474057(FTCD)
            MMU: 14317(Ftcd)
            RNO: 89833(Ftcd)
            SSC: 397517(FTCD)
            XLA: 379483(MGC64458)
            XTR: 448617(TGas028n11.1)
            SPU: 584654(LOC584654)
            DDI: DDBDRAFT_0187716
            DPS: DP2350
            SPY: SPy_2083
            SPZ: M5005_Spy_1773
            SPM: spyM18_2142
            SPH: MGAS10270_Spy1839
            SPI: MGAS10750_Spy1865
            SPJ: MGAS2096_Spy1806
            SPK: MGAS9429_Spy1784
            SPF: SpyM51731
            SPA: M6_Spy1770
            SPB: M28_Spy1757
            SSA: SSA_0433 SSA_0434
            CTC: CTC02303
            AMT: Amet_4586
            FNU: FN0739 FN1405
            TMA: TM0843
            TME: Tmel_1173
            HMA: pNG7381(ftc)
            TAC: Ta1476
            TVO: TVN0091
            PTO: PTO1243
STRUCTURES  PDB: 1O5H  1TT9  2PFD  
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.4
            ExPASy - ENZYME nomenclature database: 4.3.1.4
            ExplorEnz - The Enzyme Database: 4.3.1.4
            ERGO genome analysis and discovery system: 4.3.1.4
            BRENDA, the Enzyme Database: 4.3.1.4
            CAS: 9032-05-7
///
ENTRY       EC 4.3.1.5                  Enzyme
NAME        phenylalanine ammonia-lyase;
            tyrase;
            phenylalanine deaminase;
            tyrosine ammonia-lyase;
            L-tyrosine ammonia-lyase;
            phenylalanine ammonium-lyase;
            PAL;
            L-phenylalanine ammonia-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     L-phenylalanine ammonia-lyase (trans-cinnamate-forming)
REACTION    L-phenylalanine = trans-cinnamate + NH3 [RN:R00697]
ALL_REAC    R00697;
            (other) R00737 R06132
SUBSTRATE   L-phenylalanine [CPD:C00079]
PRODUCT     trans-cinnamate [CPD:C00423];
            NH3 [CPD:C00014]
COMMENT     This enzyme may also act on L-tyrosine.
REFERENCE   1  [PMID:14458851]
  AUTHORS   KOUKOL J, CONN EE.
  TITLE     The metabolism of aromatic compounds in higher plans. IV.
            Purification and properties of the phenylalanine deaminase of
            Hordeum vulgare.
  JOURNAL   J. Biol. Chem. 236 (1961) 2692-8.
  ORGANISM  Hordeum vulgare [GN:ehvu]
REFERENCE   2
  AUTHORS   Young, M.R. and Neish, A.C.
  TITLE     Properties of the ammonia-lyases deaminating phenylalanine and
            related compounds in Triticum sestivum and Pteridium aquilinum.
  JOURNAL   Phytochemistry 5 (1966) 1121-1132.
  ORGANISM  Triticum aestivum [GN:etae], Pteridium aquilinum
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
            PATH: map00910  Nitrogen metabolism
            PATH: map00940  Phenylpropanoid biosynthesis
            PATH: map00960  Alkaloid biosynthesis II
ORTHOLOGY   KO: K01747  phenylalanine ammonia-lyase
GENES       ATH: AT3G10340 AT3G53260(PAL2)
            OSA: 4336415 4338861
            ANI: AN6075.2
            AFM: AFUA_2G09110
            AOR: AO090005000532 AO090011000788
            UMA: UM00078.1
            PFO: Pfl_0433
STRUCTURES  PDB: 1T6J  1T6P  1W27  1Y2M  2NYF  
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.5
            ExPASy - ENZYME nomenclature database: 4.3.1.5
            ExplorEnz - The Enzyme Database: 4.3.1.5
            ERGO genome analysis and discovery system: 4.3.1.5
            BRENDA, the Enzyme Database: 4.3.1.5
            CAS: 9024-28-6
///
ENTRY       EC 4.3.1.6                  Enzyme
NAME        beta-alanyl-CoA ammonia-lyase;
            beta-alanyl coenzyme A ammonia-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     beta-alanyl-CoA ammonia-lyase (acryloyl-CoA-forming)
REACTION    beta-alanyl-CoA = acryloyl-CoA + NH3 [RN:R03046]
ALL_REAC    R03046;
            (other) R06132
SUBSTRATE   beta-alanyl-CoA [CPD:C02335]
PRODUCT     acryloyl-CoA [CPD:C00894];
            NH3 [CPD:C00014]
COMMENT     The reaction has only been demonstrated in the direction of addition
            of ammonia.
REFERENCE   1
  AUTHORS   Stadtman, E.R.
  TITLE     The enzymic synthesis of beta-alanyl coenzyme A.
  JOURNAL   J. Am. Chem. Soc. 77 (1955) 5765-5766.
  ORGANISM  Clostridium propionicum
PATHWAY     PATH: map00410  beta-Alanine metabolism
            PATH: map00640  Propanoate metabolism
GENES       MXA: MXAN_4385
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.6
            ExPASy - ENZYME nomenclature database: 4.3.1.6
            ExplorEnz - The Enzyme Database: 4.3.1.6
            ERGO genome analysis and discovery system: 4.3.1.6
            BRENDA, the Enzyme Database: 4.3.1.6
            CAS: 9024-29-7
///
ENTRY       EC 4.3.1.7                  Enzyme
NAME        ethanolamine ammonia-lyase;
            ethanolamine deaminase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     ethanolamine ammonia-lyase (acetaldehyde-forming)
REACTION    ethanolamine = acetaldehyde + NH3 [RN:R00749]
ALL_REAC    R00749;
            (other) R06132
SUBSTRATE   ethanolamine [CPD:C00189]
PRODUCT     acetaldehyde [CPD:C00084];
            NH3 [CPD:C00014]
COFACTOR    Cobamide [CPD:C00210]
COMMENT     A cobalamin protein.
REFERENCE   1  [PMID:5846987]
  AUTHORS   Bradbeer C.
  TITLE     The clostridial fermentations of choline and ethanolamine. 1.
            Preparation and properties of cell-free extracts.
  JOURNAL   J. Biol. Chem. 240 (1965) 4669-74.
  ORGANISM  Clostridium sp.
REFERENCE   2  [PMID:5846988]
  AUTHORS   Bradbeer C.
  TITLE     The clostridial fermentations of choline and ethanolamine. II.
            Requirement for a cobamide coenzyme by an ethanolamine deaminase.
  JOURNAL   J. Biol. Chem. 240 (1965) 4675-81.
  ORGANISM  Clostridium sp.
REFERENCE   3  [PMID:4297225]
  AUTHORS   Kaplan BH, Stadtman ER.
  TITLE     Ethanolamine deaminase, a cobamide coenzyme-dependent enzyme. I.
            Purification, assay, and properties of the enzyme.
  JOURNAL   J. Biol. Chem. 243 (1968) 1787-93.
  ORGANISM  Clostridium sp.
PATHWAY     PATH: map00564  Glycerophospholipid metabolism
ORTHOLOGY   KO: K01748  ethanolamine ammonia-lyase
            KO: K03735  ethanolamine ammonia-lyase large subunit
            KO: K03736  ethanolamine ammonia-lyase small subunit
GENES       ECO: b2440(eutC) b2441(eutB)
            ECJ: JW2433(eutC) JW2434(eutB)
            ECE: Z3705(eutC) Z3706(eutB)
            ECS: ECs3311 ECs3312
            ECC: c2974(eutC) c2975(eutB)
            ECI: UTI89_C2773(eutC) UTI89_C2774(eutB)
            ECP: ECP_2461 ECP_2462
            ECV: APECO1_4107(eutB) APECO1_4108(eutC)
            ECW: EcE24377A_2726(eutC) EcE24377A_2727(eutB)
            ECX: EcHS_A2577(eutC) EcHS_A2578(eutB)
            STY: STY2694(eutC) STY2695(eutB)
            STT: t0400(eutB) t0401(eutC)
            SPT: SPA0410(eutB) SPA0411(eutC)
            SEC: SC2455(eutB)
            STM: STM2457(eutC) STM2458(eutB)
            SSN: SSON_2529(eutC)
            SBO: SBO_2465(eutC) SBO_2468(eutB)
            SDY: SDY_2638(eutC)
            PLU: plu2970(eutB) plu2971(eutC)
            SPE: Spro_3435
            XCC: XCC2260(eutA) XCC2261(eutC)
            XCB: XC_1854 XC_1855
            XCV: XCV2563(eutA) XCV2564(eutC)
            XAC: XAC2365(eutA) XAC2366(eutC)
            XOO: XOO2685(eutC)
            XOM: XOO_2533(XOO2533)
            PAE: PA4024(eutB) PA4025
            PAU: PA14_11760(eutC) PA14_11770(eutB)
            PPU: PP_0542 PP_0543(eutB)
            PPF: Pput_0581
            PST: PSPTO_0726(eutC) PSPTO_0727(eutB)
            PSB: Psyr_0627 Psyr_0628
            PSP: PSPPH_4667(eutB) PSPPH_4668(eutC)
            PFL: PFL_5472(eutBC) PFL_5473(eutB) PFL_5474(eutC)
            PFO: Pfl_4991 Pfl_4992
            PEN: PSEEN0631 PSEEN0632(eutB)
            PMY: Pmen_2683
            SDN: Sden_1072 Sden_1073
            PAT: Patl_1427 Patl_1428
            PIN: Ping_0277
            MAQ: Maqu_1241 Maqu_2942
            MMW: Mmwyl1_0476
            CVI: CV_1184(eutC) CV_1185(eutB)
            RSO: RSc3126(eutC) RSc3127(eutB)
            REU: Reut_B5490 Reut_B5491
            REH: H16_B0096(eutB) H16_B0097(eutC)
            RME: Rmet_5902 Rmet_5903
            BMA: BMA2983(eutB) BMA2984(eutC)
            BMV: BMASAVP1_A3322(eutC) BMASAVP1_A3323(eutB)
            BML: BMA10299_A1554(eutC) BMA10299_A1555(eutB)
            BMN: BMA10247_3047(eutB) BMA10247_3048(eutC)
            BXE: Bxe_A4443 Bxe_A4444
            BVI: Bcep1808_0136
            BUR: Bcep18194_A3309 Bcep18194_A3310
            BCN: Bcen_2925 Bcen_2926
            BCH: Bcen2424_0129 Bcen2424_0130
            BAM: Bamb_0119 Bamb_0120
            BPS: BPSL3371(eutC) BPSL3372(eutB)
            BPM: BURPS1710b_0140(eutC) BURPS1710b_0141(eutB)
            BPL: BURPS1106A_4010(eutC) BURPS1106A_4011(eutB)
            BPD: BURPS668_3938(eutC) BURPS668_3939(eutB)
            BTE: BTH_I3281(eutC) BTH_I3282(eutB)
            RFR: Rfer_0586 Rfer_0587
            PNA: Pnap_2627
            AAV: Aave_4775
            MPT: Mpe_A2417 Mpe_A2418
            AZO: azo3830(eutC)
            PCA: Pcar_0467
            RLE: RL4365(eutB) RL4366(eutC)
            BJA: blr2994 blr2996
            BRA: BRADO4577(eutB) BRADO4578(eutC)
            BBT: BBta_2263(eutC) BBta_2264(eutB) BBta_2600 BBta_3738(eutC)
                 BBta_3739(eutB)
            RPA: RPA3747(eutC) RPA3749(eutB)
            RPB: RPB_1717 RPB_1719
            RPC: RPC_1711 RPC_1713
            RPD: RPD_2981 RPD_2982
            RPE: RPE_1805 RPE_1807
            XAU: Xaut_4033
            JAN: Jann_2576 Jann_2577
            GBE: GbCGDNIH1_1891 GbCGDNIH1_1892
            RRU: Rru_A1031 Rru_A1032
            SUS: Acid_3823
            LMO: lmo1175(eutB) lmo1176(eutC)
            LMF: LMOf2365_1185(eutB) LMOf2365_1186(eutC)
            LIN: lin1139(eutB) lin1140(eutC)
            LWE: lwe1133(eutB) lwe1134(eutC)
            SSA: SSA_0519 SSA_0520
            EFA: EF1627(eutC) EF1629(eutB)
            STH: STH2063
            CAC: CAC2717 CAC2718
            CPE: CPE0898(eutB) CPE0899(eutC)
            CPF: CPF_0891 CPF_0892
            CTC: CTC02175 CTC02176
            CDF: CD1913(eutB) CD1914(eutC)
            AMT: Amet_0256
            DSY: DSY4961 DSY4962
            DRM: Dred_1296
            MSM: MSMEG_1553(eutB) MSMEG_1554(eutC)
            MVA: Mvan_3198
            NFA: nfa21870(eutB) nfa21880(eutC)
            RHA: RHA1_ro06084(eutB) RHA1_ro06085(eutC)
            SMA: SAV4544(eutB) SAV4545(eutC)
            NCA: Noca_4033
            FAL: FRAAL5560(eutB) FRAAL5561(eutC)
            FNU: FN0079 FN0080
            CHU: CHU_3052(eutC) CHU_3053(eutB)
STRUCTURES  PDB: 2QEZ  
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.7
            ExPASy - ENZYME nomenclature database: 4.3.1.7
            ExplorEnz - The Enzyme Database: 4.3.1.7
            ERGO genome analysis and discovery system: 4.3.1.7
            BRENDA, the Enzyme Database: 4.3.1.7
            CAS: 9054-69-7
///
ENTRY       EC 4.3.1.8        Obsolete  Enzyme
NAME        Transferred to 2.5.1.61
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
COMMENT     Transferred entry: now EC 2.5.1.61, hydroxymethylbilane synthase (EC
            4.3.1.8 created 1972, modified 1982, modified 1989, deleted 2003)
STRUCTURES  PDB: 1AH5  1GTK  1PDA  1YPN  2YPN  
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.8
            ExPASy - ENZYME nomenclature database: 4.3.1.8
            ExplorEnz - The Enzyme Database: 4.3.1.8
            ERGO genome analysis and discovery system: 4.3.1.8
            BRENDA, the Enzyme Database: 4.3.1.8
///
ENTRY       EC 4.3.1.9                  Enzyme
NAME        glucosaminate ammonia-lyase;
            glucosaminic dehydrase;
            D-glucosaminate dehydratase;
            D-glucosaminic acid dehydrase;
            aminodeoxygluconate dehydratase;
            2-amino-2-deoxy-D-gluconate hydro-lyase (deaminating);
            aminodeoxygluconate ammonia-lyase;
            2-amino-2-deoxy-D-gluconate ammonia-lyase;
            D-glucosaminate ammonia-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     D-glucosaminate ammonia-lyase (isomerizing;
            2-dehydro-3-deoxy-D-gluconate-forming)
REACTION    D-glucosaminate = 2-dehydro-3-deoxy-D-gluconate + NH3 [RN:R01544]
ALL_REAC    R01544;
            (other) R06132
SUBSTRATE   D-glucosaminate [CPD:C03752]
PRODUCT     2-dehydro-3-deoxy-D-gluconate [CPD:C00204];
            NH3 [CPD:C00014]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     Contains pyridoxal phosphate.
REFERENCE   1
  AUTHORS   Imanaga, Y.
  TITLE     Metabolism of D-glucosamine. III. Enzymic degradation of
            D-glucosaminic acid.
  JOURNAL   J. Biochem. (Tokyo) 45 (1958) 647-650.
  ORGANISM  soil bacterium
REFERENCE   2
  AUTHORS   Merrick, J.M. and Roseman, S.
  TITLE     D-Glucosaminic acid dehydrase.
  JOURNAL   Methods Enzymol. 9 (1966) 657-660.
REFERENCE   3  [PMID:7068563]
  AUTHORS   Iwamoto R, Imanaga Y, Soda K.
  TITLE     D-glucosaminate dehydratase from Agrobacterium radiobacter.
            Physicochemical and enzymological properties.
  JOURNAL   J. Biochem. (Tokyo). 91 (1982) 283-9.
  ORGANISM  Agrobacterium radiobacter
REFERENCE   4  [PMID:7766176]
  AUTHORS   Iwamoto R, Taniki H, Koishi J, Nakura S.
  TITLE     D-glucosaminate aldolase activity of D-glucosaminate dehydratase
            from Pseudomonas fluorescens and its requirement for Mn2+ ion.
  JOURNAL   Biosci. Biotechnol. Biochem. 59 (1995) 408-11.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00030  Pentose phosphate pathway
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.9
            ExPASy - ENZYME nomenclature database: 4.3.1.9
            ExplorEnz - The Enzyme Database: 4.3.1.9
            ERGO genome analysis and discovery system: 4.3.1.9
            BRENDA, the Enzyme Database: 4.3.1.9
            CAS: 37290-91-8
///
ENTRY       EC 4.3.1.10                 Enzyme
NAME        serine-sulfate ammonia-lyase;
            (L-SOS)lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     L-serine-O-sulfate ammonia-lyase (pyruvate-forming)
REACTION    L-serine O-sulfate + H2O = pyruvate + NH3 + sulfate [RN:R00532]
ALL_REAC    R00532;
            (other) R06132
SUBSTRATE   L-serine O-sulfate [CPD:C02703];
            H2O [CPD:C00001]
PRODUCT     pyruvate [CPD:C00022];
            NH3 [CPD:C00014];
            sulfate [CPD:C00059]
REFERENCE   1  [PMID:5583990]
  AUTHORS   Thomas JH, Tudball N.
  TITLE     Studies on the enzymic degradation of L-serine O-sulphate by a rat
            liver preparation.
  JOURNAL   Biochem. J. 105 (1967) 467-72.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.10
            ExPASy - ENZYME nomenclature database: 4.3.1.10
            ExplorEnz - The Enzyme Database: 4.3.1.10
            ERGO genome analysis and discovery system: 4.3.1.10
            BRENDA, the Enzyme Database: 4.3.1.10
            CAS: 9054-70-0
///
ENTRY       EC 4.3.1.11                 Enzyme
NAME        dihydroxyphenylalanine ammonia-lyase;
            beta-(3,4-dihydroxyphenyl)-L-alanine (DOPA) ammonia-lyase;
            3,4-dihydroxy-L-phenylalanine ammonia-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     3,4-dihydroxy-L-phenylalanine ammonia-lyase (trans-caffeate-forming)
REACTION    3,4-dihydroxy-L-phenylalanine = trans-caffeate + NH3 [RN:R02079]
ALL_REAC    R02079;
            (other) R06132
SUBSTRATE   3,4-dihydroxy-L-phenylalanine [CPD:C00355]
PRODUCT     trans-caffeate [CPD:C01197];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   MacLeod, N.J. and Pridham, J.B.
  TITLE     Deamination of beta-(3,4-dihydroxyphenyl)-L-alanine by plants.
  JOURNAL   Biochem. J. 88 (1963) 45.
PATHWAY     PATH: map00350  Tyrosine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.11
            ExPASy - ENZYME nomenclature database: 4.3.1.11
            ExplorEnz - The Enzyme Database: 4.3.1.11
            ERGO genome analysis and discovery system: 4.3.1.11
            BRENDA, the Enzyme Database: 4.3.1.11
            CAS: 37290-92-9
///
ENTRY       EC 4.3.1.12                 Enzyme
NAME        ornithine cyclodeaminase;
            ornithine cyclase;
            ornithine cyclase (deaminating);
            L-ornithine ammonia-lyase (cyclizing)
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     L-ornithine ammonia-lyase (cyclizing; L-proline-forming)
REACTION    L-ornithine = L-proline + NH3 [RN:R00671]
ALL_REAC    R00671
SUBSTRATE   L-ornithine [CPD:C00077]
PRODUCT     L-proline [CPD:C00148];
            NH3 [CPD:C00014]
COFACTOR    NAD+ [CPD:C00003]
COMMENT     Requires NAD+. The enzyme is a member of the mu-crystallin protein
            family [4]. The reaction is stimulated by the presence of ADP or ATP
            and is inhibited by O2 [2].
REFERENCE   1  [PMID:4399881]
  AUTHORS   Costilow RN, Laycock L.
  TITLE     Ornithine cyclase (deaminating). Purification of a protein that
            converts ornithine to proline and definition of the optimal assay
            conditions.
  JOURNAL   J. Biol. Chem. 246 (1971) 6655-60.
  ORGANISM  Clostridium sporogenes
REFERENCE   2  [PMID:4373469]
  AUTHORS   Muth WL, Costilow RN.
  TITLE     Ornithine cyclase (deaminating). II. Properties of the homogeneous
            enzyme.
  JOURNAL   J. Biol. Chem. 249 (1974) 7457-62.
  ORGANISM  Clostridium sporogenes
REFERENCE   3  [PMID:10468639]
  AUTHORS   Espineda CE, Linford AS, Devine D, Brusslan JA.
  TITLE     The AtCAO gene, encoding chlorophyll a oxygenase, is required for
            chlorophyll b synthesis in Arabidopsis thaliana.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 10507-11.
REFERENCE   4  [PMID:15518536]
  AUTHORS   Goodman JL, Wang S, Alam S, Ruzicka FJ, Frey PA, Wedekind JE.
  TITLE     Ornithine cyclodeaminase: structure, mechanism of action, and
            implications for the mu-crystallin family.
  JOURNAL   Biochemistry. 43 (2004) 13883-91.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   5  [PMID:15103146]
  AUTHORS   Alam S, Wang SC, Ruzicka FJ, Frey PA, Wedekind JE.
  TITLE     Crystallization and X-ray diffraction analysis of ornithine
            cyclodeaminase from Pseudomonas putida.
  JOURNAL   Acta. Crystallogr. D. Biol. Crystallogr. 60 (2004) 941-4.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K01750  ornithine cyclodeaminase
GENES       SPO: SPAP11E10.01
            AFM: AFUA_6G08780
            DDI: DDBDRAFT_0191677
            EHI: 149.t00020
            YPE: YPO4090
            YPK: y4106
            YPM: YP_3998
            YPA: YPA_2995
            YPN: YPN_3734
            YPP: YPDSF_0007
            YPS: YPTB3900
            ECA: ECA2039
            SPE: Spro_3024
            VVY: VV1563
            PAE: PA4908
            PAU: PA14_14020 PA14_64850
            PPU: PP_3190 PP_3533 PP_4431
            PPF: Pput_2240 Pput_2526
            PFL: PFL_3641(arcB)
            PEN: PSEEN1859(arcB) PSEEN2151 PSEEN5012
            PAR: Psyc_1391(ocd)
            PCR: Pcryo_0899 Pcryo_0978 Pcryo_1795
            SDN: Sden_0589
            SAZ: Sama_2610
            SLO: Shew_2955
            SSE: Ssed_3503
            SPL: Spea_1610 Spea_3170
            CPS: CPS_2747 CPS_4886
            PHA: PSHAb0543
            PIN: Ping_2540
            CBU: CBU_1727(arcB)
            CBD: COXBU7E912_0275(arcB)
            LPN: lpg2196
            LPF: lpl2120
            LPP: lpp2145
            FTW: FTW_0394
            FTL: FTL_0578
            FTA: FTA_0612
            FTN: FTN_1444
            CSA: Csal_2722
            MMW: Mmwyl1_0204 Mmwyl1_3082
            CVI: CV_3249(ocd)
            RSO: RS00361(RSp0483) RS00875(RSp0418) RSc3352(RS02627)
            REU: Reut_A2671 Reut_A3381 Reut_B5760
            REH: H16_A0689 H16_A1394(arcB) H16_A3673 H16_B1881
            RME: Rmet_0586 Rmet_1116 Rmet_3527 Rmet_3634 Rmet_4824
            BMA: BMAA1290
            BXE: Bxe_A1829 Bxe_B1765 Bxe_C0057
            BVI: Bcep1808_4040 Bcep1808_5463
            BUR: Bcep18194_A3938 Bcep18194_B1663 Bcep18194_B2542
                 Bcep18194_B2555 Bcep18194_B2946 Bcep18194_C6879
            BCN: Bcen_0365 Bcen_4010 Bcen_5804
            BCH: Bcen2424_0848 Bcen2424_3568 Bcen2424_3577 Bcen2424_4357
                 Bcen2424_6168
            BAM: Bamb_0723 Bamb_5302 Bamb_5311 Bamb_6019
            BPS: BPSS0940
            BPM: BURPS1710b_A2543
            BTE: BTH_II1457
            BPE: BP1505
            BPA: BPP1970
            BBR: BB1012
            RFR: Rfer_0976 Rfer_3226 Rfer_3883
            POL: Bpro_1163 Bpro_2024 Bpro_4333 Bpro_4602
            PNA: Pnap_3771
            AAV: Aave_0121 Aave_0151
            AJS: Ajs_0613
            VEI: Veis_2150 Veis_4197
            NET: Neut_2213
            EBA: ebA4164(ocd)
            DAR: Daro_3361
            PCA: Pcar_0765
            MXA: MXAN_7463
            MLO: mll6776 mlr3204 mlr7139
            MES: Meso_3311 Meso_3962
            SME: SMa0486 SMa1871 SMb20433 SMb21494(ocd)
            SMD: Smed_3694
            ATU: Atu4008(arcB*) Atu4758(arcB) Atu6016(ocd)
            ATC: AGR_L_1687 AGR_L_1691 AGR_L_247 AGR_pTi_54(ocd)
            RET: RHE_CH00058(ocdch1) RHE_CH02026(ocdch2) RHE_CH02594
                 RHE_PF00181(ocdF)
            RLE: RL0060 RL3003(arcB) RL3095(arcB) RL4459(ocd) pRL120053(arcB)
                 pRL120751
            BME: BMEII0397
            BMF: BAB2_0338
            BMS: BRA0899(arcB)
            BMB: BruAb2_0334(arcB)
            BOV: BOV_A0842(arcB)
            OAN: Oant_1471 Oant_3468
            SIL: SPO1141 SPO2121(arcB) SPO3821
            SIT: TM1040_1163 TM1040_2670 TM1040_2702
            RSP: RSP_0854
            RSH: Rsph17029_2513
            RSQ: Rsph17025_3121 Rsph17025_3175
            JAN: Jann_0054 Jann_2605
            RDE: RD1_0323 RD1_1415(arcB) RD1_2889
            PDE: Pden_0286 Pden_3918 Pden_4637
            ZMO: ZMO1975
            SWI: Swit_1052 Swit_1566 Swit_2415
            RRU: Rru_A2867
            SUS: Acid_1837 Acid_2302 Acid_5671
            BAN: BA0902
            BAR: GBAA0902
            BAA: BA_1484
            BAT: BAS0854
            BCE: BC0906
            BCA: BCE_0995
            BCZ: BCZK0803(arcB)
            BCY: Bcer98_2042
            BTK: BT9727_0800(arcB)
            BTL: BALH_0814
            BCL: ABC1182
            SAU: SA0113
            SAV: SAV0117
            SAM: MW0090
            SAR: SAR0120
            SAS: SAS0091
            SAC: SACOL0101
            SAB: SAB0056
            SAA: SAUSA300_0119
            SAO: SAOUHSC_00076
            SAJ: SaurJH9_0104
            SAH: SaurJH1_0108
            SEP: SE0315
            SER: SERP0192
            SHA: SH2453
            SSP: SSP2196
            LLM: llmg_1149(ocd)
            LSL: LSL_1273
            LCA: LSEI_0332
            CGL: NCgl1520(cgl1582)
            CGB: cg1784(ocd)
            CEF: CE1700 CE2115(ocd)
            CJK: jk1979(ocd)
            RHA: RHA1_ro04990
            SMA: SAV7163(arcB4)
            ART: Arth_3596
            PAC: PPA1289
            SEN: SACE_3017(arcB4) SACE_4281(arcB4)
            STP: Strop_1041
            RXY: Rxyl_2097 Rxyl_2927
            TDE: TDE2754(arcB)
            DEH: cbdb_A155(arcB)
            DEB: DehaBAV1_0238
            RRS: RoseRS_1351
            RCA: Rcas_3909
            MAC: MA3252(ocd)
            MBA: Mbar_A3192
            MMA: MM_0097
            MBU: Mbur_1274
            MTP: Mthe_0713
            MHU: Mhun_1928
            MEM: Memar_1004
            MBN: Mboo_0844
            MKA: MK1411
            HAL: VNG2224G(ocd1)
            HMA: rrnAC0038(ocd1) rrnAC0227(ocd3) rrnAC2941(ocd2)
            HWA: HQ1386A(ocd) HQ1803A(ocd) HQ2237A(ocd)
            NPH: NP0448A(arcB) NP3802A
            PTO: PTO0381
            RCI: RCIX1588(arcB)
            APE: APE_0916.1(ocd)
            SSO: SSO0378(ocd-like1)
            STO: ST2179
            SAI: Saci_2372
            TPE: Tpen_0208
STRUCTURES  PDB: 1U7H  1X7D  
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.12
            ExPASy - ENZYME nomenclature database: 4.3.1.12
            ExplorEnz - The Enzyme Database: 4.3.1.12
            ERGO genome analysis and discovery system: 4.3.1.12
            BRENDA, the Enzyme Database: 4.3.1.12
            CAS: 9054-76-6
///
ENTRY       EC 4.3.1.13                 Enzyme
NAME        carbamoyl-serine ammonia-lyase;
            O-carbamoyl-L-serine deaminase;
            carbamoylserine deaminase;
            O-carbamoyl-L-serine ammonia-lyase (pyruvate-forming)
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     O-carbamoyl-L-serine ammonia-lyase (decarboxylating;
            pyruvate-forming)
REACTION    O-carbamoyl-L-serine + H2O = pyruvate + 2 NH3 + CO2 [RN:R00213]
ALL_REAC    R00213
SUBSTRATE   O-carbamoyl-L-serine [CPD:C03015];
            H2O [CPD:C00001]
PRODUCT     pyruvate [CPD:C00022];
            NH3 [CPD:C00014];
            CO2 [CPD:C00011]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:4761084]
  AUTHORS   Copper AJ, Meister A.
  TITLE     Enzymatic conversion of O-carbamyl-L-serine to pyruvate and ammonia.
  JOURNAL   Biochem. Biophys. Res. Commun. 55 (1973) 780-7.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.13
            ExPASy - ENZYME nomenclature database: 4.3.1.13
            ExplorEnz - The Enzyme Database: 4.3.1.13
            ERGO genome analysis and discovery system: 4.3.1.13
            BRENDA, the Enzyme Database: 4.3.1.13
            CAS: 52227-64-2
///
ENTRY       EC 4.3.1.14                 Enzyme
NAME        3-aminobutyryl-CoA ammonia-lyase;
            L-3-aminobutyryl-CoA deaminase;
            L-3-aminobutyryl-CoA ammonia-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     L-3-aminobutyryl-CoA ammonia-lyase (crotonoyl-CoA-forming)
REACTION    L-3-aminobutyryl-CoA = crotonoyl-CoA + NH3 [RN:R03030]
ALL_REAC    R03030
SUBSTRATE   L-3-aminobutyryl-CoA [CPD:C05231]
PRODUCT     crotonoyl-CoA [CPD:C00877];
            NH3 [CPD:C00014]
COMMENT     Hydroxylamine can replace ammonia as a substrate.
            Crotonoyl-pantetheine can replace crotonoyl-CoA but it is a poorer
            substrate.
REFERENCE   1  [PMID:4420467]
  AUTHORS   Jeng I, Barker HA.
  TITLE     Purification and properties of l-3-aminobutyryl coenzyme A deaminase
            from a lysine-fermenting Clostridium.
  JOURNAL   J. Biol. Chem. 249 (1974) 6578-84.
  ORGANISM  Clostridium sp.
REFERENCE   2  [PMID:7410315]
  AUTHORS   Barker HA, Kahn JM, Chew S.
  TITLE     Enzymes involved in 3,5-diaminohexanoate degradation by
            Brevibacterium sp.
  JOURNAL   J. Bacteriol. 143 (1980) 1165-70.
  ORGANISM  Brevibacterium sp.
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.14
            ExPASy - ENZYME nomenclature database: 4.3.1.14
            ExplorEnz - The Enzyme Database: 4.3.1.14
            ERGO genome analysis and discovery system: 4.3.1.14
            BRENDA, the Enzyme Database: 4.3.1.14
            CAS: 55467-41-9
///
ENTRY       EC 4.3.1.15                 Enzyme
NAME        diaminopropionate ammonia-lyase;
            diaminopropionatase;
            alpha,beta-diaminopropionate ammonia-lyase;
            2,3-diaminopropionate ammonia-lyase;
            2,3-diaminopropanoate ammonia-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     2,3-diaminopropanoate ammonia-lyase (adding H2O; pyruvate-forming)
REACTION    2,3-diaminopropanoate + H2O = pyruvate + 2 NH3 [RN:R00195]
ALL_REAC    R00195;
            (other) R00223
SUBSTRATE   2,3-diaminopropanoate [CPD:C06393];
            H2O [CPD:C00001]
PRODUCT     pyruvate [CPD:C00022];
            NH3 [CPD:C00014]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal phosphate enzyme. Active towards both D- and
            L-diaminopropanoate. D- and L-serine are poor substrates.
REFERENCE   1  [PMID:3275662]
  AUTHORS   Nagasawa T, Tanizawa K, Satoda T, Yamada H.
  TITLE     Diaminopropionate ammonia-lyase from Salmonella typhimurium.
            Purification and characterization of the crystalline enzyme, and
            sequence determination of the pyridoxal 5'-phosphate binding
            peptide.
  JOURNAL   J. Biol. Chem. 263 (1988) 958-64.
  ORGANISM  Salmonella typhimurium
ORTHOLOGY   KO: K01751  
GENES       AFM: AFUA_2G00340
            ECO: b2871(ygeX)
            ECJ: JW2839(ygeX)
            ECE: Z4210(ygeX)
            ECS: ECs3744
            ECC: c3449(ygeX)
            ECI: UTI89_C3256(ygeX)
            ECP: ECP_2865
            ECV: APECO1_3655(ygeX)
            ECW: EcE24377A_3196
            ECX: EcHS_A3031
            STY: STY1006
            SPT: SPA1796
            SEC: SC0959(dpaL)
            STM: STM1002
            SSN: SSON_3022(ygeX)
            SBO: SBO_3113(ygeX)
            PPR: PBPRA1993
            CPS: CPS_4911(dpaL)
            AHA: AHA_2162
            REU: Reut_B4533
            BUR: Bcep18194_B0057
            BCN: Bcen_5230
            BCH: Bcen2424_5629
            BAM: Bamb_6425
            BPA: BPP2124
            BBR: BB1521
            RFR: Rfer_0159
            POL: Bpro_1499
            DDE: Dde_1266
            SIL: SPO2196
            SIT: TM1040_2709
            RDE: RD1_3473
            EFA: EF2579
            CDF: CD2085(dpaL1) CD3184(dpaL2)
            CBO: CBO2888(dpaL)
            CBA: CLB_2852(dpaL)
            CBH: CLC_2785(dpaL)
            CBF: CLI_2944(dpaL)
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.15
            ExPASy - ENZYME nomenclature database: 4.3.1.15
            ExplorEnz - The Enzyme Database: 4.3.1.15
            ERGO genome analysis and discovery system: 4.3.1.15
            BRENDA, the Enzyme Database: 4.3.1.15
            CAS: 51901-19-0
///
ENTRY       EC 4.3.1.16                 Enzyme
NAME        threo-3-hydroxyaspartate ammonia-lyase;
            threo-3-hydroxyaspartate dehydratase;
            L-threo-3-hydroxyaspartate dehydratase;
            threo-3-hydroxy-L-aspartate ammonia-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     threo-3-hydroxy-L-aspartate ammonia-lyase (oxaloacetate-forming)
REACTION    threo-3-hydroxy-L-aspartate = oxaloacetate + NH3 [RN:R05758]
ALL_REAC    R05758
SUBSTRATE   threo-3-hydroxy-L-aspartate [CPD:C11511]
PRODUCT     oxaloacetate [CPD:C00036];
            NH3 [CPD:C00014]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:10481099]
  AUTHORS   Wada M, Matsumoto T, Nakamori S, Sakamoto M, Kataoka M, Liu JQ, Itoh
            N, Yamada H, Shimizu S.
  TITLE     Purification and characterization of a novel enzyme,
            L-threo-3-hydroxyaspartate dehydratase, from Pseudomonas sp. T62.
  JOURNAL   FEMS. Microbiol. Lett. 179 (1999) 147-51.
  ORGANISM  Pseudomonas sp.
GENES       OTS: OTBS_0854(tdcB)
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.16
            ExPASy - ENZYME nomenclature database: 4.3.1.16
            ExplorEnz - The Enzyme Database: 4.3.1.16
            ERGO genome analysis and discovery system: 4.3.1.16
            BRENDA, the Enzyme Database: 4.3.1.16
///
ENTRY       EC 4.3.1.17                 Enzyme
NAME        L-serine ammonia-lyase;
            serine deaminase;
            L-hydroxyaminoacid dehydratase;
            L-serine deaminase;
            L-serine dehydratase;
            L-serine hydro-lyase (deaminating)
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     L-serine ammonia-lyase (pyruvate-forming)
REACTION    L-serine = pyruvate + NH3 [RN:R00220]
ALL_REAC    R00220;
            (other) R00590 R06131
SUBSTRATE   L-serine [CPD:C00065]
PRODUCT     pyruvate [CPD:C00022];
            NH3 [CPD:C00014]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. This reaction is also carried out by
            EC 4.3.1.19 threonine ammonia-lyase, from a number of sources. The
            reaction catalysed probably involves initial elimination of water
            (hence the enzyme's original classification as EC 4.2.1.13, L-serine
            dehydratase), followed by isomerization and hydrolysis of the
            product with C-N bond breakage.
REFERENCE   1  [PMID:7042346]
  AUTHORS   Ramos F, Wiame JM.
  TITLE     Occurrence of a catabolic L-serine (L-threonine) deaminase in
            Saccharomyces cerevisiae.
  JOURNAL   Eur. J. Biochem. 123 (1982) 571-6.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:4750769]
  AUTHORS   Simon D, Hoshino J, Kroger H.
  TITLE     L-serine dehydratase from rat liver. Purification and some
            properties.
  JOURNAL   Biochim. Biophys. Acta. 321 (1973) 361-8.
  ORGANISM  rat [GN:rno]
REFERENCE   3
  AUTHORS   Suda, M. and Nakagawa, H.
  TITLE     L-Serine dehydratase (rat liver).
  JOURNAL   Methods Enzymol. 17B (1971) 346-351.
  ORGANISM  rat [GN:rno]
REFERENCE   4
  AUTHORS   Sagers, R.D. and Carter, J.
  TITLE     E. L-Serine dehydratase (Clostridium acidiurica).
  JOURNAL   Methods Enzymol. 17B (1971) 351-356.
  ORGANISM  Clostridium acidiurica
REFERENCE   5
  AUTHORS   Robinson, W.G. and Labow, R.
  TITLE     L-Serine dehydratase (Escherichia coli).
  JOURNAL   Methods Enzymol. 17B (1971) 356-360.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00272  Cysteine metabolism
ORTHOLOGY   KO: K01752  L-serine dehydratase
GENES       HSA: 10993(SDS)
            MMU: 231691(Sds)
            RNO: 25044(Sds)
            CFA: 486281(SDS)
            SCE: YCL064C(CHA1)
            ANI: AN4217.2
            DDI: DDB_0230212
            ECO: b1814(sdaA) b2797(sdaB) b4471(tdcG)
            ECJ: JW1803(sdaA) JW2768(sdaB) JW5520(tdcG)
            ECE: Z2857(sdaA) Z4114(sdaB) Z4464
            ECS: ECs2523 ECs3657 ECs3992
            ECC: c2219(sdaA) c3365(sdaB) c3870
            ECI: UTI89_C2010(sdaA) UTI89_C3168(sdaB) UTI89_C3547(tdcG)
            ECP: ECP_1757 ECP_3205
            ECV: APECO1_3312(tdcG) APECO1_3734(sdaB) APECO1_871(sdaA)
            ECW: EcE24377A_2042(sdaA) EcE24377A_3102(sdaB)
                 EcE24377A_3586(tdcG)
            ECX: EcHS_A1904(sdaA2)
            STY: STY1956(sdaA) STY2430(sdaC) STY3110(sdaB) STY3422(tdcG)
            STT: t0659(sdaC) t1051(sdaA) t2879(sdaB) t3160(tdcG)
            SPT: SPA1047(sdaA) SPA2835(sdaB) SPA3109(tdcG)
            SEC: SC1820(sdaA) SC2212(sdhL) SC2910(sdaB) SC3186(tdcG)
            STM: STM1826(sdaA) STM2196 STM2971(sdaB) STM3240(tdcG)
            YPE: YPO1771(sdaA)
            YPK: y2537(sdaA)
            YPM: YP_1622(sdaA)
            YPA: YPA_1143
            YPN: YPN_2352
            YPP: YPDSF_1352
            YPS: YPTB1647(sdaA)
            YPI: YpsIP31758_2355(sdaA)
            YEN: YE1472(sdaB)
            SFL: SF1414(sdaA) SF2811(sdaB) SF3152(sdaA)
            SFX: S1529(sdaA) S3006(sdaB) S3363
            SFV: SFV_1415(sdaA) SFV_2876(sdaB) SFV_3153(yhaP)
            SSN: SSON_1346(sdaA) SSON_2954(sdaB) SSON_3269(yhaP)
            SBO: SBO_1270(sdaA) SBO_2678(sdaB) SBO_2977
            SDY: SDY_1720(sdaA) SDY_3014(sdaB)
            ECA: ECA2380(sdaA) ECA3159(sdaB)
            PLU: plu2696(sdaA)
            SGL: SG1328
            ENT: Ent638_2383 Ent638_3250
            SPE: Spro_1629 Spro_2810
            HIN: HI0288(sdaA)
            HIT: NTHI0397(sdaA)
            HDU: HD1142(sdaA)
            PMU: PM0036(sdaA)
            MSU: MS1311(sdaA)
            APL: APL_0857(sdaA)
            XCC: XCC2853(sdaA)
            XCB: XC_1255
            XCV: XCV3173(tdcG)
            XAC: XAC3036(sdaA)
            XOO: XOO1821(sdaA)
            XOM: XOO_1719(XOO1719)
            VCH: VC1300 VCA0666
            VCO: VC0395_0608(sdaA-2) VC0395_A0918(sdaA-1)
            VVU: VV1_2260 VV2_1677
            VVY: VV2085 VVA0104 VVA0496
            VPA: VP1880 VPA0254
            VFI: VF1176 VFA0966
            PPR: PBPRA2413 PBPRB0319
            PAE: PA2443(sdaA) PA5379(sdaB)
            PAU: PA14_33030(sdaA) PA14_71060(sdaB)
            PAP: PSPA7_2808(sdaA2) PSPA7_6165(sdaA1)
            PPU: PP_0297(sda-1) PP_0987(sda-2) PP_3144(sda-3)
            PPF: Pput_0317 Pput_1024 Pput_2570
            PST: PSPTO_1886(sdaA)
            PSB: Psyr_3522
            PSP: PSPPH_3461(sdaA)
            PFL: PFL_0979(sdaA) PFL_4642(sdaA) PFL_5761(sdaA)
            PFO: Pfl_0920 Pfl_4393 Pfl_5237
            PEN: PSEEN2008 PSEEN2454(sda-3) PSEEN4437(sdaA-2) PSEEN5187(sdaA)
            PMY: Pmen_4547
            PAR: Psyc_1196(sdaA)
            PCR: Pcryo_1195
            PRW: PsycPRwf_1149
            SON: SO_2248(sdaA)
            SDN: Sden_1946
            SFR: Sfri_0687 Sfri_2402
            SAZ: Sama_1325 Sama_2771
            SBL: Sbal_2417
            SBM: Shew185_2406
            SLO: Shew_0740 Shew_1625
            SPC: Sputcn32_2171
            SSE: Ssed_0859 Ssed_2838
            SPL: Spea_0772 Spea_1538
            SHE: Shewmr4_1725
            SHM: Shewmr7_1804
            SHN: Shewana3_2295
            SHW: Sputw3181_1837
            ILO: IL1708(sdaA)
            CPS: CPS_3617(sdaA)
            PHA: PSHAa1163(sdaA)
            PAT: Patl_1625
            PIN: Ping_3256
            CBU: CBU_0194(sda)
            CBD: COXBU7E912_1902(sdaA)
            LPN: lpg0790(sda-2)
            LPF: lpl0828(sdhL)
            LPP: lpp0854(sdhL)
            FTU: FTT0577(sdaA)
            FTF: FTF0577(sdaA)
            FTW: FTW_1434(sdaA)
            FTL: FTL_1334
            FTH: FTH_1299(sdaA)
            FTA: FTA_1409(sdaA)
            FTN: FTN_0750(sdaA)
            HCH: HCH_03859(sdaA)
            CSA: Csal_0982
            MMW: Mmwyl1_3280
            AHA: AHA_2137(sdaA-1) AHA_2138(sdaA-2)
            DNO: DNO_0619(sdaA)
            NME: NMB0211
            NMA: NMA0057(sdaA)
            NGO: NGO1773(sdaA)
            CVI: CV_1408(sdaA2) CV_2874(sdaA1)
            RSO: RSc1099(sda2a) RSc1100(sda2b) RSc3296(sdaA2) RSp0045(sdaA1)
            REU: Reut_A3333 Reut_B4807 Reut_B4831
            REH: H16_A3622(sdaA)
            RME: Rmet_3483
            BMA: BMA2991(sdaA)
            BMV: BMASAVP1_A3314(sdaA)
            BML: BMA10299_A1546(sdaA)
            BMN: BMA10247_3056(sdaA)
            BXE: Bxe_A0052 Bxe_B0082 Bxe_B1601
            BVI: Bcep1808_0147 Bcep1808_3460 Bcep1808_7031
            BUR: Bcep18194_A3321 Bcep18194_A4400 Bcep18194_B0485
            BCN: Bcen_0776 Bcen_2913 Bcen_3215
            BCH: Bcen2424_0142 Bcen2424_1257 Bcen2424_5152
            BAM: Bamb_0129 Bamb_4547
            BPS: BPSL3364(sdaA) BPSS1370(sdaB)
            BPM: BURPS1710b_0131(sdaA) BURPS1710b_A0396(sdaA)
            BPL: BURPS1106A_4002(sdaA) BURPS1106A_A1863(sdaA)
            BPD: BURPS668_3931(sdaA) BURPS668_A1955(sdaA)
            BTE: BTH_I3251(sdaA-1) BTH_II0995(sdaA-2)
            BPE: BP1258(sdaA)
            BPA: BPP1873(sdaA)
            BBR: BB3235(sdaA)
            RFR: Rfer_1084
            POL: Bpro_4369
            AAV: Aave_0302
            AJS: Ajs_0095
            VEI: Veis_3225
            MPT: Mpe_A1429
            MMS: mma_3335(sdaA)
            NEU: NE0380
            NET: Neut_1760
            HPY: HP0132(sdaA)
            HPJ: jhp0120(sdaB)
            HPA: HPAG1_0130
            HAC: Hac_0312(sdaA)
            CJE: Cj1624c(sdaA)
            CJR: CJE1796(sdaA)
            CJJ: CJJ81176_1615(sdaA)
            CJU: C8J_1526(sdaA)
            CJD: JJD26997_1984(sdaA)
            DVU: DVU2147
            DDE: Dde_3034 Dde_3111
            DPS: DP2186
            MXA: MXAN_6186(sdaA)
            MLO: mll0670
            MES: Meso_1367 Meso_4265
            SME: SMc01256(sda)
            SMD: Smed_1037
            ATU: Atu1759(sdaA)
            ATC: AGR_C_3229
            RET: RHE_CH02214(sda) RHE_CH04092(ypch01441)
            RLE: RL2544(sdaA)
            BME: BMEI0811
            BMS: BR1175(sda)
            BOV: BOV_1134(sdaA)
            OAN: Oant_2016
            BBT: BBta_7663
            BHE: BH06140(sdaA)
            BQU: BQ07090(sdaA)
            XAU: Xaut_0871
            CCR: CC_3108
            SIL: SPO1323(sdaA)
            SIT: TM1040_1962
            RSP: RSP_0361(sda)
            RSH: Rsph17029_2005
            RSQ: Rsph17025_0881
            JAN: Jann_0316
            RDE: RD1_1917(sdaA)
            PDE: Pden_4132
            MMR: Mmar10_1473
            HNE: HNE_1878(sdaA)
            ZMO: ZMO0189(sdaA)
            SAL: Sala_0292
            SWI: Swit_3038 Swit_4357
            GOX: GOX0794
            GBE: GbCGDNIH1_0078
            ACR: Acry_0996
            ABA: Acid345_0897
            BSU: BG13397(sdaAB) BG13398(sdaAA)
            BHA: BH2496 BH2497
            BAN: BA3307(sdhA-1) BA3308(sdhB-1) BA4360(sdhA-2) BA4361(sdhB-2)
            BAR: GBAA3307(sdhA-1) GBAA3308(sdhB-1) GBAA4360(sdhA-2)
                 GBAA4361(sdhB-2)
            BAA: BA_3809 BA_3810 BA_4818 BA_4819
            BAT: BAS3067 BAS3068 BAS4046 BAS4047
            BCE: BC4135 BC4136
            BCA: BCE_4208(sdhA) BCE_4209(sdhB)
            BCZ: BCZK3892(sdhA) BCZK3893(sdhB)
            BCY: Bcer98_2834 Bcer98_2835
            BTK: BT9727_3884(sdhA) BT9727_3885(sdhB)
            BTL: BALH_2933(sdhA) BALH_2934(sdhB)
            BLI: BL02309(sdaAB) BL02310(sdaAA)
            BLD: BLi01806(sdaAB) BLi01807(sdaAA)
            BCL: ABC2306(sdaAA) ABC2307(sdaAB)
            BAY: RBAM_015680(sdaAB) RBAM_015690(sdaAA)
            BPU: BPUM_1484(sdaAB) BPUM_1485(sdaAA)
            OIH: OB1518 OB1519
            GKA: GK1184 GK1185
            SAU: SA2318 SA2319
            SAV: SAV2530 SAV2531
            SAM: MW2451 MW2452
            SAR: SAR2610 SAR2611
            SAS: SAS2416 SAS2417
            SAC: SACOL2544(sdaAA) SACOL2545(sdaAB)
            SAB: SAB2404c SAB2405c
            SAA: SAUSA300_2469(sdaAA) SAUSA300_2470(sdaAB)
            SAO: SAOUHSC_02839 SAOUHSC_02840
            SAJ: SaurJH9_2554
            SAH: SaurJH1_2606
            SEP: SE2080 SE2081
            SER: SERP2094(sdhA) SERP2095(sdhB)
            SHA: SH0538 SH0539
            SSP: SSP1544 SSP1545
            LMO: lmo1812 lmo1813
            LMF: LMOf2365_1840(sdhA) LMOf2365_1841(sdhB)
            LIN: lin1926 lin1927
            LWE: lwe1831(sdhA) lwe1832(sdhB)
            LLA: L43452(sdaB) L44083(sdaA)
            LLC: LACR_0887 LACR_0888
            LLM: llmg_1732(sdaA) llmg_1733(sdaB)
            SPY: SPy_2189(sdhB) SPy_2190(sdhA)
            SPZ: M5005_Spy_1841(sdhB) M5005_Spy_1842(sdhA)
            SPM: spyM18_2224 spyM18_2225
            SPG: SpyM3_1841(sdhB) SpyM3_1842(sdhA)
            SPS: SPs1837 SPs1838
            SPH: MGAS10270_Spy1960(sdhB) MGAS10270_Spy1961(sdhA)
            SPI: MGAS10750_Spy1957(sdhB) MGAS10750_Spy1958(sdhA)
            SPJ: MGAS2096_Spy1872(sdhB) MGAS2096_Spy1873(sdhA)
            SPK: MGAS9429_Spy1852(sdhB) MGAS9429_Spy1853(sdhA)
            SPF: SpyM51813(sdhB)
            SPA: M6_Spy1858 M6_Spy1859
            SPB: M28_Spy1873(sdhB) M28_Spy1874(sdhA)
            SPN: SP_0105 SP_0106
            SPR: spr0094(sdaA) spr0095(sdaB)
            SPD: SPD_0102(sdhA) SPD_0103(sdhB)
            SAG: SAG2145(sdhB) SAG2146(sdhA)
            SAN: gbs2104 gbs2105
            SAK: SAK_2103(sdhB) SAK_2104(sdhA)
            STC: str1316(sdaB) str1317(sdaA)
            STL: stu1316(sdaB) stu1317(sdaA)
            SSA: SSA_2361(sdaB) SSA_2362(sdaA)
            SGO: SGO_0019(sdhA) SGO_0020(sdhB)
            LPL: lp_0505(sdhB) lp_0506(sdhA)
            LJO: LJ1328 LJ1329
            LAC: LBA1397(sdhB) LBA1398(sdhA)
            LSA: LSA0316(sdhB) LSA0317(sdhA)
            LSL: LSL_1931(sdaA) LSL_1932(sdaB)
            LCA: LSEI_1199 LSEI_1200
            LRE: Lreu_1073
            EFA: EF0098(sdhB-1) EF0099(sdhA-1) EF2721(sdhB-2) EF2722(sdhA-2)
            CAC: CAC0673 CAC0674
            CPE: CPE0988(sdhB) CPE0989(sdhA) CPE2623(sdhB) CPE2624(sdhA)
            CPF: CPF_1245(sdhB) CPF_1246(sdhA) CPF_2959(sdhB) CPF_2960(sdhA)
            CPR: CPR_1057(sdhB) CPR_1058(sdhA) CPR_2642(sdhB) CPR_2643(sdhA)
            CTC: CTC01981 CTC01982
            CNO: NT01CX_1254(sdaAA) NT01CX_1255(sdaAB)
            CDF: CD3222(sdaB)
            CBO: CBO1214(sdhB) CBO1215(sdhA)
            CBA: CLB_1243(sdhB) CLB_1244(sdhA)
            CBH: CLC_1255(sdhB) CLC_1256(sdhA)
            CBF: CLI_1297(sdhB) CLI_1298(sdhA)
            CBE: Cbei_4498
            CKL: CKL_0700(sdhB) CKL_0701(sdhA)
            AMT: Amet_2318
            CHY: CHY_0701(sdhA1) CHY_2457(sdhA2) CHY_2458(sdhB2)
            DSY: DSY2675 DSY2676
            DRM: Dred_1252
            TTE: TTE1008(sdaA) TTE1009(sdaA2)
            MTA: Moth_1946 Moth_1947
            MTU: Rv0069c(sdaA)
            MTC: MT0075(sdaA)
            MBO: Mb0070c(sdaA)
            MBB: BCG_0100c(sdaA)
            MLE: ML1755(sdaA)
            MSM: MSMEG_3440(sdaA)
            MGI: Mflv_0819
            CGL: NCgl1583(cgl1645)
            CGB: cg1852(sdaA)
            CDI: DIP0490(sdaA) DIP1359(sdaB)
            CJK: jk1506(sdaA)
            RHA: RHA1_ro01828 RHA1_ro02934(sdaA) RHA1_ro05336
            SCO: SCO5469(sdaA)
            SMA: SAV2776(sdaA)
            CMI: CMM_2405(sdaA)
            ART: Arth_0061 Arth_0768 Arth_3700
            AAU: AAur_0990(sdaA) AAur_3830(sdaA) AAur_4003(sdaA)
            PAC: PPA0396
            ACE: Acel_1846
            KRA: Krad_4045
            SEN: SACE_4501(sdaA) SACE_6377(sdaA)
            STP: Strop_0430
            BLO: BL1017(sdaA)
            BAD: BAD_0650(sdaA)
            FNU: FN1106
            RBA: RB8779(sdaA) RB8979
            PCU: pc0878(sdaB)
            TDE: TDE1506(sdhA) TDE1507(sdhB)
            SYR: SynRCC307_1391(ilvA)
            SYX: SynWH7803_1222(ilvA)
            GVI: glr2358
            BTH: BT_4678
            BFR: BF1265
            BFS: BF1216(tdcG)
            PGI: PG0084(sda)
            GFO: GFO_2084
            FJO: Fjoh_4709
            FPS: FP0884(sdaA)
            DRA: DR_0377 DR_0497
            DGE: Dgeo_1331 Dgeo_1332
            TTH: TTC0387 TTC0667
            TTJ: TTHA0739 TTHA1029
            TME: Tmel_0337
            FNO: Fnod_1474
STRUCTURES  PDB: 1P5J  1PWE  1PWH  2IQQ  
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.17
            ExPASy - ENZYME nomenclature database: 4.3.1.17
            ExplorEnz - The Enzyme Database: 4.3.1.17
            ERGO genome analysis and discovery system: 4.3.1.17
            BRENDA, the Enzyme Database: 4.3.1.17
///
ENTRY       EC 4.3.1.18                 Enzyme
NAME        D-serine ammonia-lyase;
            D-hydroxyaminoacid dehydratase;
            D-serine dehydrase;
            D-hydroxy amino acid dehydratase;
            D-serine hydrolase;
            D-serine dehydratase (deaminating);
            D-serine deaminase;
            D-serine hydro-lyase (deaminating)
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     D-serine ammonia-lyase (pyruvate-forming)
REACTION    D-serine = pyruvate + NH3 [RN:R00221]
ALL_REAC    R00221;
            (other) R06131
SUBSTRATE   D-serine [CPD:C00740]
PRODUCT     pyruvate [CPD:C00022];
            NH3 [CPD:C00014]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also acts, slowly, on D-threonine.
            The reaction catalysed probably involves initial elimination of
            water (hence the enzyme's original classification as EC 4.2.1.14,
            D-serine dehydratase), followed by isomerization and hydrolysis of
            the product with C-N bond breakage.
REFERENCE   1  [PMID:5327100]
  AUTHORS   Dupourque D, Newton WA, Snell EE.
  TITLE     Purification and properties of D-serine dehydrase from Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 241 (1966) 1233-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:12999751]
  AUTHORS   METZLER DE, SNELL EE.
  TITLE     Deamination of serine.  II.  D-Serine dehydrase, a vitamin B6 enzyme
            from Escherichia coli.
  JOURNAL   J. Biol. Chem. 198 (1952) 363-73.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
ORTHOLOGY   KO: K01753  D-serine dehydratase
GENES       ECO: b2366(dsdA)
            ECJ: JW2363(dsdA)
            ECE: Z3628(dsdA)
            ECS: ECs3245
            ECC: c2901(dsdA)
            ECI: UTI89_C2697(dsdA)
            ECP: ECP_2391 ECP_4590
            ECV: APECO1_4170(dsdA)
            ECW: EcE24377A_2652(dsdA)
            ECX: EcHS_A2503
            STY: STY3977(dsdA)
            STT: t3715(dsdA)
            SPT: SPA3653(dsdA)
            SEC: SC3724(dsdA)
            STM: STM3802(dsdA)
            YEN: YE0800(dsdA)
            SFL: SF2433(dsdA)
            SFX: S2570(dsdA)
            SFV: SFV_2425(dsdA)
            SSN: SSON_2457(dsdA)
            SBO: SBO_2392(dsdA)
            SDY: SDY_2561(dsdA)
            PLU: plu1970(dsdA)
            SPE: Spro_2515
            HSO: HS_1718(dsdA)
            VCH: VCA0875
            VCO: VC0395_0362(dsdA)
            VPA: VP1248
            PPR: PBPRB1408
            PAE: PA3357(dsdA)
            PAU: PA14_20650(dsdA)
            PAP: PSPA7_1773(dsdA)
            ACI: ACIAD1048(dsdA)
            SPL: Spea_3449
            CPS: CPS_4659(dsdA)
            HCH: HCH_02978(dsdA)
            AHA: AHA_1438(dsdA)
            CVI: CV_2648(dsdA)
            RSO: RSp1185(dsd)
            REU: Reut_A2915 Reut_B4022
            RME: Rmet_4770
            BMA: BMA0176
            BMV: BMASAVP1_1577
            BML: BMA10299_1762
            BMN: BMA10247_A0431
            BXE: Bxe_A4060
            BUR: Bcep18194_A6070 Bcep18194_B1364
            BCN: Bcen_2130
            BAM: Bamb_2792
            BPS: BPSL0628 BPSS2116(dsdA)
            BPM: BURPS1710b_0834(dsd) BURPS1710b_A1220(dsdA)
            BPL: BURPS1106A_A2856(dsdA)
            BPD: BURPS668_A2980(dsdA)
            BTE: BTH_I0544 BTH_II0245(dsdA)
            RFR: Rfer_0929
            POL: Bpro_0661
            PNA: Pnap_4614
            RET: RHE_PC00175
            RLE: pRL100420
            BSU: BG11747(dsdA)
            BHA: BH1762(dsdA)
            BAN: BA1784(dsdA)
            BAR: GBAA1784(dsdA)
            BAA: BA_2290
            BAT: BAS1653
            BCE: BC1725
            BCA: BCE_1855(dsdA)
            BCZ: BCZK1600(dsdA)
            BTK: BT9727_1631(dsdA)
            BCL: ABC1954(dsdA)
            BAY: RBAM_021900
            GKA: GK1922(dsdA)
            SSP: SSP0432
            LPL: lp_2776(dsdA)
            OOE: OEOE_0657
            CHY: CHY_0067(dsdA)
            DSY: DSY1743
            FNU: FN0553
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.18
            ExPASy - ENZYME nomenclature database: 4.3.1.18
            ExplorEnz - The Enzyme Database: 4.3.1.18
            ERGO genome analysis and discovery system: 4.3.1.18
            BRENDA, the Enzyme Database: 4.3.1.18
            CAS: 9015-88-7
///
ENTRY       EC 4.3.1.19                 Enzyme
NAME        threonine ammonia-lyase;
            threonine deaminase;
            L-serine dehydratase;
            serine deaminase;
            L-threonine dehydratase;
            threonine dehydrase;
            L-threonine deaminase;
            threonine dehydratase;
            L-threonine hydro-lyase (deaminating);
            L-threonine ammonia-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     L-threonine ammonia-lyase (2-oxobutanoate-forming)
REACTION    L-threonine = 2-oxobutanoate + NH3 [RN:R00996]
ALL_REAC    R00996;
            (other) R00220 R06131
SUBSTRATE   L-threonine [CPD:C00188]
PRODUCT     2-oxobutanoate [CPD:C00109];
            NH3 [CPD:C00014]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     The enzyme from many sources is a pyridoxal-phosphate protein; that
            from Pseudomonas putida is not. The enzyme from a number of sources
            also acts on L-serine, cf. EC 4.3.1.17, L-serine ammonia-lyase. The
            reaction catalysed probably involves initial elimination of water
            (hence the enzyme's original classification as EC 4.2.1.16,
            threonine dehydratase), followed by isomerization and hydrolysis of
            the product with C-N bond breakage.
REFERENCE   1  [PMID:4814721]
  AUTHORS   Cohn MS, Phillips AT.
  TITLE     Purification and characterization of a B6-independent threonine
            dehydratase from Pseudomonas putida.
  JOURNAL   Biochemistry. 13 (1974) 1208-14.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2  [PMID:14479973]
  AUTHORS   NISHIMURA JS, GREENBERG DM.
  TITLE     Purification and properties of L-threonine dehydrase of sheep liver.
  JOURNAL   J. Biol. Chem. 236 (1961) 2684-91.
  ORGANISM  sheep
REFERENCE   3  [PMID:5321308]
  AUTHORS   Phillips AT, Wood WA.
  TITLE     The mechanism of action of 5'-adenylic acid-activated threonine
            dehydrase.
  JOURNAL   J. Biol. Chem. 240 (1965) 4703-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:4889010]
  AUTHORS   Shizuta Y, Nakazawa A, Tokushige M, Hayaishi O.
  TITLE     Studies on the interaction between regulatory enzymes and effectors.
            3. Crystallization and characterization of adenosine
            5'-monophosphate-dependent threonine deaminase from Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 244 (1969) 1883-9.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00290  Valine, leucine and isoleucine biosynthesis
ORTHOLOGY   KO: K01754  threonine dehydratase
GENES       XLA: 398771(MGC68790)
            XTR: 496756(sdsl)
            CEL: K01C8.1 Y51H7C.9
            ATH: AT3G10050(OMR1)
            OSA: 4333898
            CME: CMR420C
            SCE: YCL064C(CHA1) YER086W(ILV1)
            AGO: AGOS_ACR232C
            PIC: PICST_83915(ILV1)
            CGR: CAGL0I05126g
            SPO: SPBC1677.03c
            ANI: AN3830.2 AN4217.2
            AFM: AFUA_1G06150 AFUA_3G14470 AFUA_4G07810 AFUA_4G08140
            AOR: AO090023000756
            CNE: CNK01420
            UMA: UM05113.1
            DDI: DDB_0230210
            TET: TTHERM_00688520 TTHERM_00923020 TTHERM_01046840
                 TTHERM_01109980
            EHI: 117.t00004 221.t00005 26.t00010 4.t00026
            ECO: b3117(tdcB) b3772(ilvA)
            ECJ: JW3088(tdcB) JW3745(ilvA)
            ECE: Z4469(tdcB) Z5283(ilvA)
            ECS: ECs3997 ECs4706
            ECC: c3875(tdcB) c4694(ilvA)
            ECI: UTI89_C3552(tdcB) UTI89_C4328(ilvA)
            ECP: ECP_3210 ECP_3965
            ECV: APECO1_2699(ilvA) APECO1_3307(tdcB)
            ECW: EcE24377A_3591(tdcB) EcE24377A_4284(ilvA)
            ECX: EcHS_A2941(sdaB) EcHS_A3305(tdcB) EcHS_A3989
            STY: STY3427(tdcB) STY3652(ilvA)
            STT: t3164(tdcB) t3393(ilvA)
            SPT: SPA3113(tdcB) SPA3744(ilvA)
            SEC: SC3190(tdcB) SC3810(ilvA)
            STM: STM3244(tdcB) STM3905(ilvA)
            YPE: YPO3896(ilvA) YPO4089
            YPK: y0339(ilvA) y4105(tdcB)
            YPM: YP_3151(ilvA) YP_3997(tdcB)
            YPA: YPA_0125 YPA_2996
            YPN: YPN_0070 YPN_3733
            YPS: YPTB0138(ilvA)
            YPI: YpsIP31758_0158(ilvA)
            YEN: YE0336(tdcB) YE3209
            SFL: SF3157(tdcB) SF3847(ilvA)
            SFX: S3369(tdcB) S3912(ilvA)
            SFV: SFV_3158(tdcB) SFV_3730(ilvA)
            SSN: SSON_3274(tdcB) SSON_3943(ilvA)
            SBO: SBO_2982(tdcB) SBO_3783(ilvA)
            SDY: SDY_3309(tdcB) SDY_3976(ilvA)
            ECA: ECA1571(tdcB) ECA2040 ECA4225(ilvA)
            PLU: plu0803 plu4681(ilvA)
            SGL: SG2393
            BFL: Bfl589(ilvA)
            BPN: BPEN_610(ilvA)
            HIN: HI0738.1(ilvA)
            HIT: NTHI0896(thd1)
            HIP: CGSHiEE_08420
            HSO: HS_0183(ilvA)
            PMU: PM1624(ilvA)
            MSU: MS2218(ilvA)
            APL: APL_1455(ilvA)
            XFA: XF1819
            XFT: PD1046(tdcB)
            XCC: XCC0379(ilvA) XCC3326(tdcB)
            XCB: XC_0391 XC_0838
            XCV: XCV0394 XCV3582
            XAC: XAC0379(ilvA) XAC3454(tdcB)
            XOO: XOO0228(ilvA) XOO0943(tdcB)
            XOM: XOO_0209(XOO0209) XOO_0862(XOO0862)
            VCH: VC0027
            VCO: VC0395_A2492(ilvA)
            VVU: VV1_1028
            VVY: VV3244
            VPA: VP3062
            VFI: VF2560
            PPR: PBPRA3596
            PAE: PA0331(ilvA1) PA1326(ilvA2) PA2683
            PAU: PA14_04320(ilvA1) PA14_29410 PA14_47100(ilvA2)
            PAP: PSPA7_0423(ilvA2) PSPA7_4064(ilvA1)
            PPU: PP_3191 PP_3446(ilvA-1) PP_4430 PP_5149(ilvA-2)
            PST: PSPTO_3806(ilvA-1) PSPTO_5288(ilvA-2)
            PSB: Psyr_1672 Psyr_4846
            PSP: PSPPH_1669(ilvA1) PSPPH_4878(ilvA2) PSPPH_4879(ilvA3)
            PFL: PFL_3098(ilvA) PFL_5905(ilvA)
            PFO: Pfl_2619 Pfl_5381
            PEN: PSEEN2960(ilvA-1) PSEEN3999 PSEEN4437(sdaA-2) PSEEN5013
                 PSEEN5242(ilvA-2)
            PAR: Psyc_0951(ilvA) Psyc_1389(tdcB)
            PCR: Pcryo_1467
            ACI: ACIAD1357(ilvA)
            SON: SO_4344(ilvA)
            SDN: Sden_0399 Sden_3411
            SFR: Sfri_0425
            SHE: Shewmr4_0365
            SHM: Shewmr7_3661
            SHN: Shewana3_0359
            CPS: CPS_4847(ilvA)
            PHA: PSHAa2768(ilvA)
            PAT: Patl_4249
            SDE: Sde_3386
            MCA: MCA0354(ilvA)
            FTU: FTT0577(sdaA)
            FTF: FTF0577(sdaA)
            FTH: FTH_1299(sdaA)
            TCX: Tcr_1563
            NOC: Noc_2666
            AEH: Mlg_0087
            HCH: HCH_01063(ilvA)
            CSA: Csal_0020
            ABO: ABO_2605(ilvA)
            AHA: AHA_4201(ilvA)
            DNO: DNO_0323(ilvA)
            NME: NMB0878
            NMA: NMA1096(ilvA)
            NMC: NMC0819(ilvA)
            NGO: NGO0444
            CVI: CV_3093(ilvA) CV_3250(tdcB)
            RSO: RS04793(RSp1516) RSc0449(ilvA)
            REU: Reut_A0413 Reut_B4347 Reut_B4909
            REH: H16_A0427 H16_B0554(tdcB)
            RME: Rmet_0354 Rmet_4825
            BMA: BMA0181(ilvA) BMA1494(tdcB) BMA2154
            BMV: BMASAVP1_A1991(tdcB) BMASAVP1_A2766(ilvA)
            BML: BMA10299_0281 BMA10299_A2312(ilvA) BMA10299_A3316(tdcB)
            BMN: BMA10247_1263(tdcB) BMA10247_2392(ilvA)
            BXE: Bxe_A2039 Bxe_A4054 Bxe_C0056
            BUR: Bcep18194_A5257 Bcep18194_A6064 Bcep18194_B1493
            BCN: Bcen_2124 Bcen_3918
            BCH: Bcen2424_1946 Bcen2424_2736 Bcen2424_6169
            BAM: Bamb_1934 Bamb_2787
            BPS: BPSL0633(ilvA) BPSL2102 BPSL2633 BPSS1279
            BPM: BURPS1710b_0840(ilvA) BURPS1710b_2515(tdcB) BURPS1710b_3108
                 BURPS1710b_A0284(ilvA)
            BPL: BURPS1106A_0677(ilvA) BURPS1106A_A1725(ilvA)
            BPD: BURPS668_0662(ilvA) BURPS668_A1809(ilvA)
            BTE: BTH_I0549(ilvA-1) BTH_I1524 BTH_I2085 BTH_II1144(ilvA-2)
            BPE: BP0139(ilvA) BP0798(tdcB) BP3420
            BPA: BPP1052(ilvA) BPP3429(tdcB) BPP3570 BPP4016(ilvA)
            BBR: BB1268(ilvA) BB3879(tdcB) BB4005 BB4489(ilvA)
            RFR: Rfer_0344 Rfer_0733
            POL: Bpro_0165 Bpro_0743 Bpro_3215
            AAV: Aave_4441
            VEI: Veis_4911
            MPT: Mpe_A3125 Mpe_A3770
            HAR: HEAR2861(ilvA)
            MMS: mma_3116
            NEU: NE0701(ilvA)
            NET: Neut_1160
            NMU: Nmul_A0437
            EBA: ebA3389 ebA3463(ilvA)
            AZO: azo0500(ilvA)
            DAR: Daro_4123
            TBD: Tbd_2363
            MFA: Mfla_0128
            HHE: HH0896(cysK)
            WSU: WS0132(ilvA)
            TDN: Tmden_1143
            CJE: Cj0828c(ilvA)
            CJR: CJE0915(ilvA)
            CJJ: CJJ81176_0845(ilvA)
            CJU: C8J_0775(ilvA)
            CJD: JJD26997_1187(ilvA)
            CFF: CFF8240_0743(ilvA)
            CCV: CCV52592_1422(ilvA)
            CHA: CHAB381_0338 CHAB381_1373(ilvA)
            CCO: CCC13826_1403(ilvA)
            ABU: Abu_2029(ilvA)
            NIS: NIS_0808(tdcB)
            SUN: SUN_1827(tdeB)
            GSU: GSU0486(ilvA)
            GME: Gmet_3072
            PCA: Pcar_2979
            BBA: Bd1056(ilvA)
            DPS: DP0889 DP1388
            MXA: MXAN_5874(ilvA)
            SFU: Sfum_0736
            RPR: RP449(tdcB)
            RTY: RT0436(tdcB)
            RCO: RC0628(tdcB)
            RFE: RF_0691(tdcB)
            RBE: RBE_0798(tdcB)
            RAK: A1C_03410
            RBO: A1I_05120
            RCM: A1E_03125
            RRI: A1G_03535
            MLO: mll4597 mll7611 mlr0162 mlr3510 mlr7138
            MES: Meso_0309 Meso_1421
            SME: SMa1872 SMb20432 SMc00936(ilvA)
            ATU: Atu1205(ilvA) Atu2735(ilvA) Atu4759(tdcB)
            ATC: AGR_C_2225 AGR_C_4956 AGR_L_246
            RET: RHE_CH01759(ilvA) RHE_CH02027(ypch00645)
                 RHE_CH03537(ypch01250) RHE_CH04092(ypch01441)
                 RHE_PF00182(ypf00081)
            RLE: RL1953(ilvA) RL4051(tdcB) RL4706(ilvA) pRL120052(tdcB)
            BME: BMEI0935
            BMS: BR1051
            BMB: BruAb1_1056
            BJA: bll1413 bll4731 bll5902(ilvA)
            BRA: BRADO3559 BRADO5091 BRADO5563
            BBT: BBta_3984 BBta_5562 BBta_6086
            RPA: RPA3967
            RPB: RPB_1623
            RPC: RPC_1447
            RPD: RPD_1632
            RPE: RPE_1467 RPE_2188
            NWI: Nwi_2254
            NHA: Nham_2664
            BHE: BH10760(ilvA)
            CCR: CC_3105 CC_3635
            SIL: SPO0020(ilvA) SPO1142 SPO3341 SPOA0435
            SIT: TM1040_2885 TM1040_3568
            RSP: RSP_2252
            JAN: Jann_0069 Jann_1660
            RDE: RD1_0416(ilvA) RD1_2891(srr) RD1_3931
            MMR: Mmar10_1589
            HNE: HNE_0171(ilvA)
            ZMO: ZMO1275(tdcB)
            GOX: GOX0325
            GBE: GbCGDNIH1_2290
            RRU: Rru_A0647 Rru_A2877
            MGM: Mmc1_3647
            ABA: Acid345_0688
            BSU: BG10673(ilvA)
            BHA: BH1711(ilvA)
            BAN: BA1854(ilvA) BA2469(tdcB)
            BAR: GBAA1854(ilvA) GBAA2469(tdcB)
            BAA: BA_2357 BA_2964
            BAT: BAS1718 BAS2297
            BCE: BC1781 BC2400
            BCA: BCE_1938(ilvA) BCE_2502(tdcB)
            BCZ: BCZK1670(ilvA) BCZK2218(tdcB)
            BTK: BT9727_1695(ilvA) BT9727_2260(tdcB)
            BLI: BL03302(ilvA)
            BLD: BLi02315(ilvA)
            BCL: ABC1181 ABC2049(ilvA)
            BPU: BPUM_1911
            OIH: OB2616
            GKA: GK1591 GK1773
            SAU: SA1271 SA1866(ilvA)
            SAV: SAV1438 SAV2061(ilvA)
            SAM: MW1327 MW1985(ilvA)
            SAR: SAR1450(tdcB) SAR2148(ilvA)
            SAS: SAS1381 SAS1966
            SAC: SACOL1477(ilvA1) SACOL2050(ilvA2)
            SAB: SAB1303c(tdcB) SAB1946(ilvA)
            SAA: SAUSA300_1330(ilvA) SAUSA300_2014(ilvA)
            SAO: SAOUHSC_01451 SAOUHSC_02289
            SEP: SE1662
            SER: SERP1673(ilvA)
            SHA: SH0972(ilvA)
            SSP: SSP0817
            LMO: lmo1991(ilvA)
            LMF: LMOf2365_2014(ilvA)
            LIN: lin2098(ilvA)
            LWE: lwe2010(ilvA)
            LLA: L0081(ilvA)
            LLM: llmg_1276(ilvA)
            SPN: SP_0450
            SPR: spr0406(ilvA)
            SPD: SPD_0409(ilvA)
            SMU: SMU.234(ilvA)
            STC: str0150(ilvA)
            STL: stu0150(ilvA)
            SSA: SSA_1967(ilvA)
            SGO: SGO_0529(ilvA)
            LSA: LSA0572(tdcB)
            LCA: LSEI_2183
            CPE: CPE1165(thd)
            CPF: CPF_1368(tdcB)
            CPR: CPR_1181(tdcB)
            CTC: CTC00071 CTC02624
            CNO: NT01CX_2074(ilvA)
            CDF: CD2514(tdcB)
            CBO: CBO3502(tdcB)
            CBA: CLB_3562(ilvA)
            CBH: CLC_3451(ilvA)
            CBF: CLI_3689(ilvA)
            CKL: CKL_0426(ilvE1)
            CHY: CHY_0191(ilvA1) CHY_2459(ilvA2)
            DSY: DSY1809 DSY4244 DSY4319
            MMY: MSC_0114(ilvA)
            MCP: MCAP_0125(ilvA)
            MTU: Rv1559(ilvA)
            MTC: MT1610(ilvA)
            MBO: Mb1585(ilvA)
            MBB: BCG_1611(ilvA)
            MLE: ML1209(ilvA)
            MPA: MAP1264(ilvA)
            MAV: MAV_3217(ilvA)
            MSM: MSMEG_3183(ilvA) MSMEG_3532
            MMC: Mmcs_3083
            CGL: NCgl0939(cgl0978) NCgl2046(cgl2127)
            CGB: cg1116(tdcB) cg2334(ilvA)
            CEF: CE2026(ilvA)
            CDI: DIP1579(ilvA)
            CJK: jk1313(ilvA)
            NFA: nfa18070(ilvA) nfa44640
            RHA: RHA1_ro01065(ilvA) RHA1_ro01945 RHA1_ro05846
            SCO: SCO4962(2SCK31.22)
            SMA: SAV3302(ilvA)
            TWH: TWT681(ilvA)
            TWS: TW700(tdcB)
            LXX: Lxx16900(ilvA)
            CMI: CMM_2245(ilvA)
            AAU: AAur_1283(ilvA)
            TFU: Tfu_1741
            FRA: Francci3_0646
            FAL: FRAAL1151 FRAAL3883
            SEN: SACE_0904(ilvA) SACE_3404 SACE_4356(ilvA)
            BLO: BL1527(tdcB)
            BAD: BAD_1570(tdcB)
            FNU: FN1411
            RBA: RB10894(thrC) RB5151(ilvA)
            SYN: slr2072(ilvA)
            SYW: SYNW1293(ilvA)
            SYD: Syncc9605_1431
            SYE: Syncc9902_1068
            SYG: sync_1411(ilvA)
            CYA: CYA_0143(ilvA)
            ANA: alr4232
            AVA: Ava_0676 Ava_2749
            PMA: Pro0927(ilvA)
            PMM: PMM0908(ilvA)
            PMT: PMT0684(ilvA)
            PMN: PMN2A_0299
            PMI: PMT9312_0892
            PMB: A9601_09531(ilvA)
            PMC: P9515_09911(ilvA)
            PMF: P9303_15381(ilvA)
            PMG: P9301_09511(ilvA)
            PMH: P9215_09841
            PME: NATL1_09711(ilvA)
            SRU: SRU_1270(ilvA) SRU_2287(ilvA)
            CHU: CHU_0207(ilvA)
            GFO: GFO_2109(ilvA)
            FPS: FP0445(ilvA)
            DRA: DR_0567
            DGE: Dgeo_1794
            TTH: TTC1708
            TTJ: TTHA0279
            TMA: TM0356
            MHU: Mhun_1939
            HAL: VNG2100G(iluA)
            HMA: pNG7371(ilvA3) rrnAC1231(ilvA1) rrnAC2508(ilvA2)
            HWA: HQ1348A(ilvA) HQ1762A(ilvA)
            NPH: NP1076A(ilvA)
            TAC: Ta0113
            TVO: TVN0190
            PTO: PTO0238
            APE: APE_1498.1
            HBU: Hbut_0216
            SSO: SSO0248(tdcB)
            STO: ST0295
            SAI: Saci_0713
            PAI: PAE2316(ilvA)
STRUCTURES  PDB: 1VE5  2GN0  2GN1  2GN2  
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.19
            ExPASy - ENZYME nomenclature database: 4.3.1.19
            ExplorEnz - The Enzyme Database: 4.3.1.19
            ERGO genome analysis and discovery system: 4.3.1.19
            UM-BBD (Biocatalysis/Biodegradation Database): 4.3.1.19
            BRENDA, the Enzyme Database: 4.3.1.19
///
ENTRY       EC 4.3.1.20                 Enzyme
NAME        erythro-3-hydroxyaspartate ammonia-lyase;
            3-hydroxyaspartate dehydratase;
            erythro-beta-hydroxyaspartate dehydratase;
            erythro-3-hydroxyaspartate dehydratase;
            erythro-3-hydroxy-Ls-aspartate hydro-lyase (deaminating);
            erythro-3-hydroxy-Ls-aspartate ammonia-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
SYSNAME     erythro-3-hydroxy-Ls-aspartate ammonia-lyase (oxaloacetate-forming)
REACTION    erythro-3-hydroxy-Ls-aspartate = oxaloacetate + NH3 [RN:R00347]
ALL_REAC    R00347;
            (other) R06131
SUBSTRATE   erythro-3-hydroxy-Ls-aspartate
PRODUCT     oxaloacetate [CPD:C00036];
            NH3 [CPD:C00014]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. The reaction catalysed probably
            involves initial elimination of water (hence the enzyme's original
            classification as EC 4.2.1.38, erythro-3-hydroxyaspartate
            dehydratase), followed by isomerization and hydrolysis of the
            product with C-N bond breakage.
REFERENCE   1  [PMID:16749162]
  AUTHORS   Gibbs RG, Morris JG.
  TITLE     Purification and properties of erythro-beta-hydroxyasparate
            dehydratase from Micrococcus denitrificans.
  JOURNAL   Biochem. J. 97 (1965) 547-54.
  ORGANISM  Micrococcus denitrificans
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.20
            ExPASy - ENZYME nomenclature database: 4.3.1.20
            ExplorEnz - The Enzyme Database: 4.3.1.20
            ERGO genome analysis and discovery system: 4.3.1.20
            BRENDA, the Enzyme Database: 4.3.1.20
///
ENTRY       EC 4.3.1.21       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Ammonia-lyases
COMMENT     Deleted entry: aminodeoxygluconate ammonia-lyase. Enzyme is
            identical to EC 4.3.1.9, glucosaminate ammonia-lyase (EC 4.3.1.21
            created 1965 as EC 4.2.1.26, transferred 2002 to EC 4.3.1.21,
            deleted 2004)
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.1.21
            ExPASy - ENZYME nomenclature database: 4.3.1.21
            ExplorEnz - The Enzyme Database: 4.3.1.21
            ERGO genome analysis and discovery system: 4.3.1.21
            BRENDA, the Enzyme Database: 4.3.1.21
///
ENTRY       EC 4.3.2.1                  Enzyme
NAME        argininosuccinate lyase;
            arginosuccinase;
            argininosuccinic acid lyase;
            arginine-succinate lyase;
            N-(L-argininosuccinate) arginine-lyase;
            omega-N-(L-arginino)succinate arginine-lyase;
            2-(omega-N-L-arginino)succinate arginine-lyase (fumarate-forming)
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Amidine-lyases
SYSNAME     2-(Nomega-L-arginino)succinate arginine-lyase (fumarate-forming)
REACTION    2-(Nomega-L-arginino)succinate = fumarate + L-arginine [RN:R01086]
ALL_REAC    R01086
SUBSTRATE   2-(Nomega-L-arginino)succinate
PRODUCT     fumarate [CPD:C00122];
            L-arginine [CPD:C00062]
REFERENCE   1  [PMID:14910762]
  AUTHORS   DAVISON DC, ELLIOTT WH.
  TITLE     Enzymic reaction between arginine and fumarate in plant and animal
            tissues.
  JOURNAL   Nature. 169 (1952) 313-4.
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00252  Alanine and aspartate metabolism
            PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K01755  argininosuccinate lyase
GENES       HSA: 435(ASL)
            PTR: 463444(ASL)
            MMU: 109900(Asl)
            RNO: 59085(Asl)
            CFA: 479704(ASL)
            GGA: 417545(ASL)
            XLA: 447450(MGC81570)
            DRE: 393423(zgc:63532)
            SPU: 574725(LOC574725)
            ATH: AT5G10920
            OSA: 4332596
            CME: CMK232C
            SCE: YHR018C(ARG4)
            AGO: AGOS_AEL019W
            PIC: PICST_62615(ARG4)
            CGR: CAGL0I08987g
            SPO: SPBC1539.03c(argx) SPBC1773.14(arg7)
            ANI: AN2914.2
            AFM: AFUA_3G07790
            AOR: AO090020000418
            UMA: UM04497.1
            ECO: b3960(argH)
            ECJ: JW3932(argH)
            ECE: Z5518(argH)
            ECS: ECs4889
            ECC: c4919(argH)
            ECI: UTI89_C4551(argH)
            ECP: ECP_4173
            ECV: APECO1_2507(argH)
            ECW: EcE24377A_4499(argH)
            ECX: EcHS_A4194 EcHS_A4263(lysC)
            STY: STY3750(argH)
            STT: t3501(argH)
            SPT: SPA3961(argH)
            SEC: SC4013(argH)
            STM: STM4123(argH)
            YPE: YPO3924(argH)
            YPK: y0312(argH)
            YPM: YP_3125(argH)
            YPA: YPA_0099
            YPN: YPN_0044
            YPS: YPTB0112(argH)
            YPI: YpsIP31758_0129(argH)
            SFL: SF4037(argH)
            SFX: S3709(argH)
            SFV: SFV_4029(argH)
            SSN: SSON_4133(argH)
            SBO: SBO_3979(argH)
            SDY: SDY_3795(argH)
            ECA: ECA0194(argH)
            PLU: plu4741(argH)
            BUC: BU051(argH)
            BAS: BUsg048(argH)
            BAB: bbp049(argH)
            BCC: BCc_033(argH)
            SGL: SG2159
            HIT: NTHI0975(argH)
            HIP: CGSHiEE_08005
            HIQ: CGSHiGG_07555
            HDU: HD1033(argH)
            HSO: HS_0692(argH)
            PMU: PM1120(argH)
            MSU: MS0237(argH)
            APL: APL_1179(argH)
            XFA: XF1003
            XFT: PD0295(argH)
            XCC: XCC2242(argH)
            XCB: XC_1876
            XCV: XCV2544(argH)
            XAC: XAC2345(argH)
            XOO: XOO2669(argH)
            XOM: XOO_2515(XOO2515)
            VCH: VC2641
            VCO: VC0395_A2217(argH)
            VVU: VV1_1374
            VVY: VV2999
            VPA: VP2756
            VFI: VF2303
            PPR: PBPRA0269
            PAE: PA5263(argH)
            PAU: PA14_69500(argH)
            PAP: PSPA7_6009(argH)
            PPU: PP_0184(argH)
            PST: PSPTO_0125(argH)
            PSB: Psyr_0065
            PSP: PSPPH_0071(argH)
            PFL: PFL_6004(argH)
            PFO: Pfl_2852 Pfl_5489
            PEN: PSEEN5355(argH)
            PAR: Psyc_0088(argH)
            PCR: Pcryo_0095
            ACI: ACIAD0283(argH)
            SON: SO_0279(argH)
            SDN: Sden_0254
            SFR: Sfri_0195
            SHE: Shewmr4_3705
            SHM: Shewmr7_0240
            SHN: Shewana3_3901
            ILO: IL0616(argH)
            CPS: CPS_0464(argHA)
            PHA: PSHAa2287(argHA)
            PAT: Patl_0978
            SDE: Sde_3670
            LPN: lpg0495(argH)
            LPF: lpl0533(argH)
            LPP: lpp0557(argH)
            MCA: MCA1248(argH)
            TCX: Tcr_0110
            NOC: Noc_0501
            AEH: Mlg_2673
            HCH: HCH_00294(argH)
            CSA: Csal_3110
            ABO: ABO_2325(argH)
            AHA: AHA_0597(argH)
            VOK: COSY_0714(argH)
            NME: NMB0637
            NMA: NMA0847(argH)
            NMC: NMC0580(argH)
            NGO: NGO0219
            CVI: CV_0115(argH)
            RSO: RSc2363(argH)
            REU: Reut_A0695 Reut_A1775
            REH: H16_A2925(argH)
            RME: Rmet_2751 Rmet_4342
            BMA: BMA0718(argH) BMA1620
            BMV: BMASAVP1_A2295(argH)
            BML: BMA10299_A2991(argH)
            BMN: BMA10247_1608(argH)
            BXE: Bxe_A3415
            BVI: Bcep1808_5167
            BUR: Bcep18194_A5760
            BCN: Bcen_1818
            BCH: Bcen2424_2429
            BAM: Bamb_2476
            BPS: BPSL1006(argH) BPSL1715 BPSL1720 BPSL2214
            BPM: BURPS1710b_1219(argH) BURPS1710b_2153(argH) BURPS1710b_2158
                 BURPS1710b_2646
            BPL: BURPS1106A_1067(argH) BURPS1106A_2017(argH) BURPS1106A_2022
            BPD: BURPS668_1061(argH) BURPS668_1997(argH) BURPS668_2002
            BTE: BTH_I0864(argH) BTH_I1971
            BPE: BP0809(argH) BP2702(argH)
            BPA: BPP1433(argH) BPP3419(argH)
            BBR: BB2507(argH) BB3869(argH)
            RFR: Rfer_1710
            POL: Bpro_3672 Bpro_4386
            AAV: Aave_1945
            MPT: Mpe_A1111
            HAR: HEAR1003(argH)
            MMS: mma_1138
            NEU: NE1854(argH)
            NET: Neut_1269
            NMU: Nmul_A2328
            EBA: ebA1170(argH)
            AZO: azo0989(argH)
            DAR: Daro_3681
            TBD: Tbd_0229
            MFA: Mfla_0038
            HHE: HH1718(argH)
            WSU: WS1218(argH)
            TDN: Tmden_0866
            CJE: Cj0931c(argH)
            CJR: CJE1009(argH)
            CJJ: CJJ81176_0938(argH)
            CJU: C8J_0868(argH)
            CJD: JJD26997_0883(argH)
            CFF: CFF8240_1295(argH)
            CCV: CCV52592_0522(argH)
            CHA: CHAB381_0307 CHAB381_1484(argH)
            CCO: CCC13826_0439 CCC13826_1520(argH)
            ABU: Abu_0616(argH)
            NIS: NIS_0657(argH)
            SUN: SUN_0544(argH)
            GSU: GSU0156(argH)
            GME: Gmet_0209
            PCA: Pcar_2418
            DVU: DVU1094(argH)
            DDE: Dde_2530
            LIP: LI0657(argH)
            DPS: DP0435
            ADE: Adeh_4071
            MXA: MXAN_5107(argH)
            SAT: SYN_02158
            SFU: Sfum_0060
            ERU: Erum1830(argH)
            ERW: ERWE_CDS_01820(argH)
            ERG: ERGA_CDS_01770(argH)
            ECN: Ecaj_0180
            ECH: ECH_0937(argH)
            PUB: SAR11_0415(argH)
            MLO: mll9226 mlr3506(asaL)
            MES: Meso_3038
            SME: SMb21094(argH2) SMc00725(argH1)
            ATU: Atu3599(argH) Atu4651(argH)
            ATC: AGR_L_2457(asaL) AGR_L_463(asaL)
            RET: RHE_CH03796(argH)
            RLE: RL4323(argH)
            BME: BMEI0086
            BMF: BAB1_1982
            BMS: BR1981(argH)
            BMB: BruAb1_1957(argH)
            BOV: BOV_1906(argH)
            BJA: blr1381(argH)
            BRA: BRADO6487(argH)
            BBT: BBta_1145(argH)
            RPA: RPA4743(argH)
            RPB: RPB_0827
            RPC: RPC_4875
            RPD: RPD_0936
            RPE: RPE_4842
            NWI: Nwi_0715
            NHA: Nham_3477
            BBK: BARBAKC583_0054(argH)
            XAU: Xaut_4873 Xaut_5068
            CCR: CC_2211
            SIL: SPO0332(argH)
            SIT: TM1040_3732
            RSP: RSP_0726 RSP_3955
            JAN: Jann_0497 Jann_2584
            RDE: RD1_1591(argH)
            MMR: Mmar10_2371
            HNE: HNE_3465(argH)
            ZMO: ZMO1770(argH)
            NAR: Saro_2677
            SAL: Sala_0201
            ELI: ELI_02035
            GOX: GOX1955
            GBE: GbCGDNIH1_0127
            RRU: Rru_A0397
            MAG: amb4489
            MGM: Mmc1_3741
            ABA: Acid345_4157
            SUS: Acid_2504
            BSU: BG12571(argH)
            BHA: BH3186(argH)
            BAN: BA3604(argH-1) BA4879(argH-2)
            BAR: GBAA3604(argH-1) GBAA4879(argH-2)
            BAA: BA_4096 BA_5300
            BAT: BAS3343 BAS4527
            BCE: BC3550 BC4629
            BCA: BCE_3564 BCE_4764(argH)
            BCZ: BCZK3258(argH) BCZK4374(argH)
            BCY: Bcer98_2224
            BTK: BT9727_3308(argH) BT9727_4363(argH)
            BTL: BALH_3189(argH) BALH_4209(argH)
            BLI: BL00416(argH)
            BLD: BLi03083(argH)
            BCL: ABC1487 ABC2736(argH)
            BAY: RBAM_026370
            BPU: BPUM_2576
            OIH: OB3128(argH)
            GKA: GK2756
            SAU: SA0821(argH)
            SAV: SAV0960(argH)
            SAM: MW0842(argH)
            SAR: SAR0922(argH)
            SAS: SAS0830
            SAC: SACOL0963(argH)
            SAB: SAB0828c(argH)
            SAA: SAUSA300_0863(argH)
            SAO: SAOUHSC_00898
            SEP: SE0656
            SER: SERP0548(argH)
            SHA: SH1990(argH)
            SSP: SSP1815
            LMO: lmo2091(argH)
            LMF: LMOf2365_2123(argH)
            LIN: lin2196(argH)
            LWE: lwe2112(argH)
            LLA: L0114(argH)
            LLC: LACR_0126
            LLM: llmg_0139(argH)
            SPR: spr0103(argH)
            SPD: SPD_0111(argH)
            SAG: SAG0126(argH)
            SAN: gbs0124
            SAK: SAK_0177(argH)
            SMU: SMU.335
            STC: str1812(argH)
            STL: stu1812(argH)
            STE: STER_1791
            SSA: SSA_2141(argH)
            SSU: SSU05_2016
            SSV: SSU98_2018
            SGO: SGO_0176(argH)
            LPL: lp_0776(argH)
            LSL: LSL_0305(argH)
            LCA: LSEI_2812
            STH: STH2750 STH486
            CAC: CAC0974(argH)
            CPE: CPE0690(argH)
            CPF: CPF_0682(argH)
            CTC: CTC00562
            CNO: NT01CX_0134(argH)
            CDF: CD2500(argH)
            CBO: CBO2669(argH)
            CBA: CLB_2611(argH)
            CBH: CLC_2543(argH)
            CBF: CLI_2735(argH)
            CKL: CKL_0982(argH)
            CHY: CHY_2259(argH)
            DSY: DSY0786
            TTE: TTE2493(argH)
            MTA: Moth_2284
            MTU: Rv1659(argH)
            MTC: MT1697(argH)
            MBO: Mb1687(argH)
            MBB: BCG_1698(argH)
            MLE: ML1413(argH)
            MPA: MAP1368(argH)
            MAV: MAV_3111(argH)
            MSM: MSMEG_3769(argH)
            MMC: Mmcs_2965
            CGL: NCgl1347(cgl1401)
            CGB: cg1588(argH)
            CEF: CE1533(argH)
            CDI: DIP1174(argH)
            CJK: jk0848(argH)
            NFA: nfa19630(argH)
            RHA: RHA1_ro00949(argH)
            SCO: SCO1570(argH)
            SMA: SAV6779(argH)
            LXX: Lxx06080(argH)
            CMI: CMM_1995(argH)
            AAU: AAur_1638(argH)
            PAC: PPA1346
            NCA: Noca_4820 Noca_4835
            TFU: Tfu_2051
            FRA: Francci3_3168
            FAL: FRAAL5201(argH)
            SEN: SACE_5256(argH) SACE_6330
            BLO: BL1057(argH)
            BAD: BAD_0918(argH)
            RXY: Rxyl_0979
            RBA: RB10834(argH)
            LIL: LA2076(argH)
            LIC: LIC11840(argH)
            LBJ: LBJ_1932(argH)
            LBL: LBL_1352(argH)
            SYN: slr1133(argH)
            SYW: SYNW0013(argH)
            SYC: syc1629_c(argH)
            SYF: Synpcc7942_2475
            SYD: Syncc9605_0013
            SYE: Syncc9902_0013
            SYG: sync_0013(argH)
            SYR: SynRCC307_0013(argH)
            SYX: SynWH7803_0013(argH)
            CYA: CYA_0103(argH)
            CYB: CYB_2070(argH)
            TEL: tll0366(argH)
            GVI: gll1051(argH)
            ANA: alr3887
            AVA: Ava_1807
            PMA: Pro0012(argH)
            PMM: PMM0012(argH)
            PMT: PMT0013(argH)
            PMN: PMN2A_1339
            PMI: PMT9312_0012
            PMB: A9601_00111(argH)
            PMC: P9515_00111(argH)
            PMF: P9303_00121(argH)
            PMG: P9301_00111(argH)
            PMH: P9215_00111
            PME: NATL1_00111(argH)
            BTH: BT_3733
            BFR: BF0512
            BFS: BF0457(argH)
            SRU: SRU_2221(argH)
            CHU: CHU_3088(argH)
            GFO: GFO_2099(argH)
            CTE: CT1055(argH)
            CCH: Cag_0730
            PLT: Plut_1043
            DET: DET1261(argH)
            DEH: cbdb_A1185(argH)
            DRA: DR_0678
            DGE: Dgeo_2065
            TTH: TTC1702
            TTJ: TTHA0283
            AAE: aq_1372(argH)
            TMA: TM1781(argH)
            MMP: MMP0013(argH)
            MAC: MA1318(argH)
            MBA: Mbar_A0004
            MMA: MM_2307
            MBU: Mbur_1025
            MHU: Mhun_0084
            MST: Msp_0618(argH)
            MSI: Msm_0192
            MKA: MK0622(argH)
            HAL: VNG2436G(argH)
            HMA: rrnAC2681(argH)
            HWA: HQ3712A(argH)
            NPH: NP5254A(argH)
            TAC: Ta0649
            TVO: TVN0928
            PTO: PTO0531
            PFU: PF0208
            RCI: RCIX271(argH)
            HBU: Hbut_0304
            SSO: SSO0639(argH)
            STO: ST1502
            SAI: Saci_1618(argH)
            MSE: Msed_1988
            PAI: PAE2887(argH)
            PIS: Pisl_0281
            PCL: Pcal_0368
            PAS: Pars_0971
STRUCTURES  PDB: 1AOS  1AUW  1DCN  1HY0  1HY1  1I0A  1K62  1K7W  1TJ7  1TJU  
                 1TJV  1TJW  1U15  1U16  1XWO  2E9F  
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.2.1
            ExPASy - ENZYME nomenclature database: 4.3.2.1
            ExplorEnz - The Enzyme Database: 4.3.2.1
            ERGO genome analysis and discovery system: 4.3.2.1
            BRENDA, the Enzyme Database: 4.3.2.1
            CAS: 9027-34-3
///
ENTRY       EC 4.3.2.2                  Enzyme
NAME        adenylosuccinate lyase;
            adenylosuccinase;
            succino AMP-lyase;
            6-N-(1,2-dicarboxyethyl)AMP AMP-lyase;
            6-N-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming)
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Amidine-lyases
SYSNAME     N6-(1,2-dicarboxyethyl)AMP AMP-lyase
REACTION    (1) N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP [RN:R01083];
            (2)
            (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-
            carboxamido]succinate = fumarate +
            5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide [RN:R04559]
ALL_REAC    R01083 R04559
SUBSTRATE   N6-(1,2-dicarboxyethyl)AMP;
            (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-
            carboxamido]succinate [CPD:C04823]
PRODUCT     fumarate [CPD:C00122];
            AMP [CPD:C00020];
            5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide [CPD:C04677]
COMMENT     Also acts on
            1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole.
REFERENCE   1  [PMID:13366975]
  AUTHORS   CARTER CE, COHEN LH.
  TITLE     The preparation and properties of adenylosuccinase and
            adenylosuccinic acid.
  JOURNAL   J. Biol. Chem. 222 (1956) 17-30.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00252  Alanine and aspartate metabolism
ORTHOLOGY   KO: K01756  adenylosuccinate lyase
GENES       HSA: 158(ADSL)
            MMU: 11564(Adsl)
            CFA: 474499(ADSL)
            BTA: 510949(ADSL)
            GGA: 396540(ADSL)
            XLA: 380285(adsl)
            XTR: 448055(adsl)
            SPU: 593658(LOC593658)
            ATH: AT1G36280 AT4G18440
            OSA: 4332642
            CME: CMQ211C
            SCE: YLR359W(ADE13)
            AGO: AGOS_ABL006C
            PIC: PICST_84718(ADE13)
            CGR: CAGL0B02794g
            SPO: SPBC14F5.09c(ade8)
            ANI: AN6209.2
            AFM: AFUA_2G11940
            AOR: AO090026000450
            CNE: CNG03070
            DDI: DDB_0230094(purB)
            PFA: PFB0295w
            TAN: TA18170
            TPV: TP03_0773
            TET: TTHERM_00377250
            TBR: Tb09.160.5560
            TCR: 503855.30 510337.30
            LMA: LmjF04.0460
            ECO: b1131(purB)
            ECJ: JW1117(purB)
            ECE: Z1860(purB)
            ECS: ECs1603
            ECC: c1510(purB)
            ECI: UTI89_C1260(purB)
            ECP: ECP_1126
            ECW: EcE24377A_1294(purB)
            ECX: EcHS_A1251
            STY: STY1272(purB)
            STT: t1688(purB)
            SPT: SPA1618(purB)
            SEC: SC1183(purB)
            STM: STM1232(purB)
            YPE: YPO1636(purB)
            YPK: y1797(purB)
            YPM: YP_1766(purB)
            YPA: YPA_1888
            YPN: YPN_1995
            YPP: YPDSF_1812
            YPS: YPTB2432(purB)
            YPI: YpsIP31758_1610(purB)
            SFL: SF1150(purB)
            SFX: S1233(purB)
            SFV: SFV_1166(purB)
            SSN: SSON_1149(purB)
            SBO: SBO_1908(purB)
            SDY: SDY_2021(purB)
            ECA: ECA2444(purB) ECA4197
            PLU: plu2806(purB)
            BUC: BU263(purB)
            BAS: BUsg253(purB)
            BAB: bbp244(purB)
            WBR: WGLp103(purB)
            SGL: SG1083
            ENT: Ent638_1644
            SPE: Spro_2020
            BFL: Bfl393(purB)
            BPN: BPEN_405(purB)
            HIN: HI0639(purB)
            HIT: NTHI0758(purB)
            HIP: CGSHiEE_09025
            HIQ: CGSHiGG_06455
            HDU: HD1649(purB)
            HSO: HS_1593(purB)
            PMU: PM1851(purB)
            MSU: MS0297(purB)
            APL: APL_0824(purB)
            ASU: Asuc_0027
            XFA: XF1553
            XFT: PD0762(purB)
            XCC: XCC1492(purB)
            XCB: XC_2744
            XCV: XCV1582(purB)
            XAC: XAC1539(purB)
            XOO: XOO2048(purB)
            XOM: XOO_1930(XOO1930)
            VCH: VC1126
            VCO: VC0395_A0644(purB)
            VVU: VV1_2928
            VVY: VV1341
            VPA: VP1128
            VFI: VF1786
            PPR: PBPRA1145
            PAE: PA2629(purB) PA3516 PA3517
            PAU: PA14_18830 PA14_18850 PA14_30110(purB)
            PAP: PSPA7_2578(purB)
            PPU: PP_4016(purB)
            PST: PSPTO_3360(purB)
            PSB: Psyr_3192
            PSP: PSPPH_3104(purB)
            PFL: PFL_3893(purB)
            PFO: Pfl_3598
            PEN: PSEEN2198(purB)
            PAR: Psyc_1245(purB)
            PCR: Pcryo_1146
            ACI: ACIAD1219(purB)
            SON: SO_2635(purB)
            SDN: Sden_1826
            SFR: Sfri_2262
            SAZ: Sama_2064
            SBL: Sbal_2480
            SBM: Shew185_2473
            SLO: Shew_1558
            SPC: Sputcn32_2235
            SHE: Shewmr4_1601
            SHM: Shewmr7_1676
            SHN: Shewana3_1745
            SHW: Sputw3181_1774
            ILO: IL1312(purB)
            CPS: CPS_2902(purB)
            PHA: PSHAa1692(purB)
            PAT: Patl_2381
            SDE: Sde_1675
            PIN: Ping_0961
            MAQ: Maqu_1764
            CBU: CBU_0824(purB)
            CBD: COXBU7E912_0889(purB)
            LPN: lpg0801
            LPF: lpl0834(purB)
            LPP: lpp0863(purB)
            MCA: MCA1784(purB)
            FTU: FTT0015(purB)
            FTF: FTF0015(purB)
            FTW: FTW_0089(purB)
            FTL: FTL_1850
            FTH: FTH_1782(purB)
            FTA: FTA_1956(purB)
            FTN: FTN_1694(purB)
            TCX: Tcr_1137
            NOC: Noc_2106
            AEH: Mlg_1358
            HHA: Hhal_0026
            HCH: HCH_02331(purB)
            CSA: Csal_2446
            ABO: ABO_1273(purB)
            AHA: AHA_1413(purB)
            DNO: DNO_0667(purB)
            BCI: BCI_0423(purB)
            RMA: Rmag_0991
            VOK: COSY_0886(purB)
            NME: NMB0284
            NMA: NMA2203(purB)
            NMC: NMC0290(purB)
            NGO: NGO1711
            CVI: CV_3834(purB)
            RSO: RSc2720(purB)
            REU: Reut_A2819 Reut_B5023
            REH: H16_A3124(purB)
            RME: Rmet_2956
            BMA: BMA2442(purB)
            BMV: BMASAVP1_A0358(purB)
            BML: BMA10299_A1216(purB)
            BMN: BMA10247_2627(purB)
            BXE: Bxe_A0593
            BVI: Bcep1808_0632
            BUR: Bcep18194_A3752
            BCN: Bcen_0183
            BCH: Bcen2424_0666
            BAM: Bamb_0561
            BPS: BPSL2928(purB)
            BPM: BURPS1710b_3438(purB)
            BPL: BURPS1106A_3436(purB)
            BPD: BURPS668_3402(purB)
            BTE: BTH_I1221(purB)
            PNU: Pnuc_1794
            BPE: BP2890(purB)
            BPA: BPP2506(purB)
            BBR: BB1953(purB)
            RFR: Rfer_4049
            POL: Bpro_4662
            AAV: Aave_4669
            AJS: Ajs_4026
            VEI: Veis_1158
            MPT: Mpe_A3624
            HAR: HEAR0312(purB)
            MMS: mma_0359
            NEU: NE1951
            NET: Neut_0410
            NMU: Nmul_A2241
            EBA: ebA1420(purB)
            AZO: azo0901(purB)
            DAR: Daro_3288
            TBD: Tbd_0518
            MFA: Mfla_1819
            HPY: HP1112
            HPJ: jhp1039(purB)
            HPA: HPAG1_1051
            HHE: HH1353(purB)
            HAC: Hac_0429(purB)
            WSU: WS0416(purB)
            TDN: Tmden_2095
            CJE: Cj0023(purB) Cj1394
            CJR: CJE0023(purB-1) CJE1582(purB-2)
            CJJ: CJJ81176_0050(purB-1) CJJ81176_1393(purB-2)
            CJU: C8J_0022(purB) C8J_1309(purB-2)
            CJD: JJD26997_0025(purB-1)
            CFF: CFF8240_1819(purB)
            CCV: CCV52592_0005(purB) CCV52592_1121(purB) CCV52592_1984(purB)
            CHA: CHAB381_1740(purB)
            CCO: CCC13826_1894(purB)
            ABU: Abu_0019(purB)
            NIS: NIS_0054
            SUN: SUN_2371
            GSU: GSU1632(purB)
            GME: Gmet_1943
            PCA: Pcar_2646
            PPD: Ppro_1145
            DVU: DVU2942(purB)
            DDE: Dde_3011
            LIP: LI0997(purB)
            BBA: Bd1949(purB)
            DPS: DP1928
            ADE: Adeh_1109
            MXA: MXAN_2079(purB)
            SAT: SYN_00426
            SFU: Sfum_0660
            WOL: WD0786(purB)
            WBM: Wbm0503
            AMA: AM384(purB)
            APH: APH_0867(purB)
            ERU: Erum2460(purB)
            ERW: ERWE_CDS_02500(purB)
            ERG: ERGA_CDS_02460(purB)
            ECN: Ecaj_0238
            ECH: ECH_0852(purB)
            NSE: NSE_0059(purB)
            PUB: SAR11_1137(purB)
            MLO: mll0079
            MES: Meso_1285
            SME: SMc00508(purB)
            ATU: Atu1841(purB)
            ATC: AGR_C_3377
            RET: RHE_CH02273(purB)
            RLE: RL2601(purB)
            BME: BMEI1117
            BMF: BAB1_0868(purB)
            BMS: BR0849(purB)
            BMB: BruAb1_0861(purB)
            BOV: BOV_0841(purB)
            BJA: blr5690(purB)
            BRA: BRADO2830(purB)
            BBT: BBta_5353(purB)
            RPA: RPA3817(purB)
            RPB: RPB_3693
            RPC: RPC_1610
            RPD: RPD_1769
            RPE: RPE_1640
            NWI: Nwi_2167
            NHA: Nham_2569
            BHE: BH09690(purB)
            BQU: BQ07450(purB)
            BBK: BARBAKC583_0857(purB)
            CCR: CC_2487
            SIL: SPO2305(purB)
            SIT: TM1040_1011
            RSP: RSP_2221(purB)
            JAN: Jann_2663
            RDE: RD1_2559(purB)
            PDE: Pden_4463
            MMR: Mmar10_1036
            HNE: HNE_1969(purB)
            ZMO: ZMO0662(purB)
            NAR: Saro_1309
            SAL: Sala_1068
            ELI: ELI_07565
            GOX: GOX2299
            GBE: GbCGDNIH1_1658
            RRU: Rru_A0716 Rru_A1963
            MAG: amb3052
            MGM: Mmc1_1065
            ABA: Acid345_2952
            SUS: Acid_2438
            BSU: BG10702(purB)
            BHA: BH0625(purB)
            BAN: BA0290(purB)
            BAR: GBAA0290(purB)
            BAA: BA_0862
            BAT: BAS0277
            BCE: BC0325
            BCA: BCE_0319(purB)
            BCZ: BCZK0265(purB)
            BTK: BT9727_0262(purB)
            BTL: BALH_0284(purB)
            BLI: BL01478(purB)
            BLD: BLi00695(purB)
            BCL: ABC1026(purB) ABC2086
            BPU: BPUM_0598
            OIH: OB0741
            GKA: GK0259
            GTN: GTNG_0239(purB)
            SAU: SA1724(purB)
            SAV: SAV1908(purB)
            SAM: MW1849(purB)
            SAR: SAR2000(purB)
            SAS: SAS1831
            SAC: SACOL1969(purB)
            SAB: SAB1843c(purB)
            SAA: SAUSA300_1889(purB)
            SAO: SAOUHSC_02126
            SEP: SE1593
            SER: SERP1446(purB)
            SHA: SH1043(purB)
            SSP: SSP0882
            LMO: lmo1773(purB)
            LMF: LMOf2365_1798(purB)
            LIN: lin1885(purB)
            LWE: lwe1791(purB)
            LLA: L88187(purB)
            LLC: LACR_1804
            LLM: llmg_0783(purB)
            SPY: SPy_0036(purB)
            SPZ: M5005_Spy_0033(purB)
            SPM: spyM18_0037(purB)
            SPG: SpyM3_0030(purB)
            SPS: SPs0031
            SPH: MGAS10270_Spy0034(purB)
            SPI: MGAS10750_Spy0035(purB)
            SPJ: MGAS2096_Spy0035(purB)
            SPK: MGAS9429_Spy0034(purB)
            SPF: SpyM50033(purB)
            SPA: M6_Spy0082
            SPB: M28_Spy0033(purB)
            SPN: SP_0056
            SPR: spr0056(purB)
            SPD: SPD_0062(purB)
            SAG: SAG0047(purB)
            SAN: gbs0047
            SAK: SAK_0080(purB)
            SMU: SMU.59(purB)
            STC: str0045(purB1) str1345(purB2)
            STL: stu0045(purB)
            STE: STER_0064
            SSA: SSA_0046(purB)
            SSU: SSU05_0039
            SSV: SSU98_0040
            SGO: SGO_2085(purB)
            LPL: lp_3269(purB)
            LJO: LJ0443
            LAC: LBA1891(purB)
            LSA: LSA0654(purB1) LSA1555(purB2)
            LSL: LSL_0517(purB)
            LDB: Ldb1444(purB)
            LBU: LBUL_1339
            LBR: LVIS_0228
            LCA: LSEI_1120
            LGA: LGAS_0391
            PPE: PEPE_1246
            EFA: EF2361(purB)
            OOE: OEOE_1125
            LME: LEUM_1390
            STH: STH2860
            CAC: CAC1821(purB)
            CPE: CPE1668(purB)
            CPF: CPF_1922(purB)
            CPR: CPR_1640(purB)
            CNO: NT01CX_2118(purB)
            CTH: Cthe_0741
            CDF: CD1334
            CBO: CBO2396
            CBA: CLB_2259(purB)
            CBH: CLC_2242(purB)
            CBF: CLI_2451(purB)
            CKL: CKL_1454(purB)
            CHY: CHY_1070(purB)
            DSY: DSY3932 DSY5028
            DRM: Dred_2370
            PTH: PTH_2547(purB)
            SWO: Swol_1779
            TTE: TTE1367(purB)
            MTA: Moth_2052
            MPE: MYPE5820
            MMY: MSC_0849(purB)
            MCP: MCAP_0766(purB)
            MFL: Mfl075
            MTU: Rv0777(purB)
            MTC: MT0801(purB)
            MBO: Mb0800(purB)
            MBB: BCG_0829(purB)
            MLE: ML2230(purB)
            MPA: MAP0611(purB)
            MAV: MAV_0722(purB)
            MSM: MSMEG_5847(purB)
            MVA: Mvan_5145
            MGI: Mflv_1613
            MMC: Mmcs_4566
            MKM: Mkms_4654
            MJL: Mjls_4949
            CGL: NCgl2509(cgl2598)
            CGB: cg2876(purB)
            CEF: CE2488(purB)
            CDI: DIP1928(purB)
            CJK: jk0349(purB)
            NFA: nfa5590(purB)
            RHA: RHA1_ro00315 RHA1_ro04787(purB)
            SCO: SCO1254(2SCG1.29)
            SMA: SAV7077(purB)
            TWH: TWT791(purB)
            TWS: TW800(purB)
            LXX: Lxx25100(purB)
            CMI: CMM_2950(purB)
            ART: Arth_4033
            AAU: AAur_3897(purB)
            PAC: PPA1992
            NCA: Noca_4341
            TFU: Tfu_3014
            FRA: Francci3_4372
            FAL: FRAAL6665(purB)
            ACE: Acel_2128
            KRA: Krad_4296
            SEN: SACE_7153(purB)
            STP: Strop_0147
            BLO: BL1800(purB)
            BAD: BAD_0554(purB)
            RXY: Rxyl_0992
            FNU: FN0368
            RBA: RB8343(purB)
            TDE: TDE1499
            LIL: LA3080(purB)
            LIC: LIC11016(purB)
            LBJ: LBJ_0845(purB)
            LBL: LBL_2237(purB)
            SYN: sll0421(purB)
            SYW: SYNW0405(purB)
            SYC: syc1198_d(purB)
            SYF: Synpcc7942_0315
            SYD: Syncc9605_2209
            SYE: Syncc9902_0469
            SYG: sync_2334(purB)
            SYR: SynRCC307_1899(purB)
            SYX: SynWH7803_2038(purB)
            CYA: CYA_1729(purB)
            CYB: CYB_1918(purB)
            TEL: tll1829(purB)
            GVI: glr0043(purB)
            ANA: alr3395
            AVA: Ava_3410
            PMA: Pro1619(purB)
            PMM: PMM1465(purB)
            PMT: PMT1484(purB)
            PMN: PMN2A_0996
            PMI: PMT9312_1558
            PMB: A9601_16671(purB)
            PMC: P9515_16451(purB)
            PMF: P9303_04631(purB)
            PMG: P9301_16551(purB)
            PMH: P9215_17331
            PME: NATL1_18651(purB)
            TER: Tery_4169
            BTH: BT_3871
            BFR: BF4018
            BFS: BF3792(purB)
            PGI: PG1123(purB)
            SRU: SRU_0386(purB)
            CHU: CHU_1563(purB)
            GFO: GFO_1092(purB)
            FJO: Fjoh_5015
            FPS: FP1805(purB)
            CTE: CT0989(purB)
            CCH: Cag_1139
            PLT: Plut_1152
            DET: DET0840(purB)
            DEH: cbdb_A821(purB)
            DEB: DehaBAV1_0759
            RRS: RoseRS_0043
            RCA: Rcas_4199
            DRA: DR_2178
            DGE: Dgeo_0688
            TTH: TTC1149
            TTJ: TTHA1513
            AAE: aq_597(purB)
            TMA: TM1095
            MMP: MMP0971(purB)
            MAC: MA3971(purB)
            MBA: Mbar_A0673
            MMA: MM_0941
            MBU: Mbur_1160
            MHU: Mhun_0824
            MST: Msp_1247(purB)
            MSI: Msm_1151
            MKA: MK1085(purB)
            HAL: VNG0415G(purB)
            HMA: rrnAC0192(purB)
            HWA: HQ1662A(purB)
            NPH: NP1658A(purB)
            TAC: Ta0523
            TVO: TVN0999
            PTO: PTO0816
            PAB: PAB0829(purB)
            PFU: PF0667
            TKO: TK0561
            RCI: RCIX2420(purB)
            SSO: SSO0240(purB)
            STO: ST0288
            SAI: Saci_0706(als)
            PAI: PAE0972(purB)
STRUCTURES  PDB: 1C3C  1C3U  1DOF  1F1O  1YIS  2HVG  2J91  2PFM  2PTQ  2PTR  
                 2PTS  2QGA  
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.2.2
            ExPASy - ENZYME nomenclature database: 4.3.2.2
            ExplorEnz - The Enzyme Database: 4.3.2.2
            ERGO genome analysis and discovery system: 4.3.2.2
            BRENDA, the Enzyme Database: 4.3.2.2
            CAS: 9027-81-0
///
ENTRY       EC 4.3.2.3                  Enzyme
NAME        ureidoglycolate lyase;
            ureidoglycolatase;
            ureidoglycolase;
            ureidoglycolate hydrolase;
            (S)-ureidoglycolate urea-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Amidine-lyases
SYSNAME     (S)-ureidoglycolate urea-lyase (glyoxylate-forming)
REACTION    (S)-ureidoglycolate = glyoxylate + urea [RN:R00776]
ALL_REAC    R00776
SUBSTRATE   (S)-ureidoglycolate [CPD:C00603]
PRODUCT     glyoxylate [CPD:C00048];
            urea [CPD:C00086]
REFERENCE   1  [PMID:6030341]
  AUTHORS   Trijbels F, Vogels GD.
  TITLE     Allantoate and ureidoglycolate degradation by Pseudomonas
            aeruginosa.
  JOURNAL   Biochim. Biophys. Acta. 132 (1967) 115-26.
  ORGANISM  Pseudomonas aeruginosa
PATHWAY     PATH: map00230  Purine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.2.3
            ExPASy - ENZYME nomenclature database: 4.3.2.3
            ExplorEnz - The Enzyme Database: 4.3.2.3
            ERGO genome analysis and discovery system: 4.3.2.3
            BRENDA, the Enzyme Database: 4.3.2.3
            CAS: 9014-57-7
///
ENTRY       EC 4.3.2.4                  Enzyme
NAME        purine imidazole-ring cyclase;
            DNA-4,6-diamino-5-formamidopyrimidine 8-C,9-N-lyase (cyclizing);
            DNA-4,6-diamino-5-formamidopyrimidine 8-C,9-N-lyase (cyclizing;
            DNA-adenine-forming)
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Amidine-lyases
SYSNAME     DNA-4,6-diamino-5-formamidopyrimidine C8-N9-lyase (cyclizing;
            DNA-adenine-forming)
REACTION    DNA 4,6-diamino-5-formamidopyrimidine = DNA adenine + H2O
            [RN:R02960]
ALL_REAC    R02960
SUBSTRATE   DNA 4,6-diamino-5-formamidopyrimidine [CPD:C04381]
PRODUCT     DNA adenine [CPD:C00821];
            H2O [CPD:C00001]
COMMENT     Also acts on 2,6-diamino-5-formamido-3,4-dihydro-4-oxopyrimidine
            residues. Brings about the reclosure of the imidazole rings of
            purine residues damaged by gamma-rays.
REFERENCE   1  [PMID:3856219]
  AUTHORS   Chetsanga CJ, Grigorian C.
  TITLE     In situ enzymatic reclosure of opened imidazole rings of purines in
            DNA damaged by gamma-irradiation.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 633-7.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.2.4
            ExPASy - ENZYME nomenclature database: 4.3.2.4
            ExplorEnz - The Enzyme Database: 4.3.2.4
            ERGO genome analysis and discovery system: 4.3.2.4
            BRENDA, the Enzyme Database: 4.3.2.4
            CAS: 95990-28-6
///
ENTRY       EC 4.3.2.5                  Enzyme
NAME        peptidylamidoglycolate lyase;
            alpha-hydroxyglycine amidating dealkylase;
            peptidyl-alpha-hydroxyglycine alpha-amidating lyase;
            HGAD;
            PGL;
            PAL;
            peptidylamidoglycolate peptidylamide-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Amidine-lyases
SYSNAME     peptidylamidoglycolate peptidyl-amide-lyase (glyoxylate-forming)
REACTION    peptidylamidoglycolate = peptidyl amide + glyoxylate [RN:R03874]
ALL_REAC    R03874
SUBSTRATE   peptidylamidoglycolate [CPD:C03303]
PRODUCT     peptidyl amide [CPD:C02179];
            glyoxylate [CPD:C00048]
COMMENT     The enzyme acts on the product of the reaction catalysed by EC
            1.14.17.3 peptidylglycine monooxygenase, thus removing a terminal
            glycine residue and leaving a des-glycine peptide amide.
REFERENCE   1  [PMID:2207061]
  AUTHORS   Katopodis AG, Ping D, May SW.
  TITLE     A novel enzyme from bovine neurointermediate pituitary catalyzes
            dealkylation of alpha-hydroxyglycine derivatives, thereby
            functioning sequentially with peptidylglycine alpha-amidating
            monooxygenase in peptide amidation.
  JOURNAL   Biochemistry. 29 (1990) 6115-20.
  ORGANISM  cow [GN:bta]
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.2.5
            ExPASy - ENZYME nomenclature database: 4.3.2.5
            ExplorEnz - The Enzyme Database: 4.3.2.5
            ERGO genome analysis and discovery system: 4.3.2.5
            BRENDA, the Enzyme Database: 4.3.2.5
            CAS: 131689-50-4
///
ENTRY       EC 4.3.3.1                  Enzyme
NAME        3-ketovalidoxylamine C-N-lyase;
            3-ketovalidoxylamine A C-N-lyase;
            p-nitrophenyl-3-ketovalidamine p-nitroaniline lyase;
            4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Amine-lyases
SYSNAME     4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase
            [5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one-form
            ing]
REACTION    4-nitrophenyl-3-ketovalidamine = 4-nitroaniline +
            5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one
            [RN:R04367]
ALL_REAC    R04367
SUBSTRATE   4-nitrophenyl-3-ketovalidamine [CPD:C03995]
PRODUCT     4-nitroaniline [CPD:C02126];
            5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one
            [CPD:C04815]
COFACTOR    Calcium [CPD:C00076]
COMMENT     Requires Ca2+. Eliminates 4-nitroaniline from
            4-nitrophenyl-3-ketovalidamine, or 4-nitrophenol from
            4-nitrophenyl-alpha-D-3-dehydroglucoside. Involved in the
            degradation of the fungicide validamycin A by Flavobacterium
            saccharophilum.
REFERENCE   1  [PMID:6548220]
  AUTHORS   Asano N, Takeuchi M, Ninomiya K, Kameda Y, Matsui K.
  TITLE     Microbial degradation of validamycin A by Flavobacterium
            saccharophilum. Enzymatic cleavage of C-N linkage in validoxylamine
            A.
  JOURNAL   J. Antibiot. (Tokyo). 37 (1984) 859-67.
  ORGANISM  Flavobacterium saccharophilum
REFERENCE   2  [PMID:4093450]
  AUTHORS   Takeuchi M, Asano N, Kameda Y, Matsui K.
  TITLE     Purification and properties of 3-ketovalidoxylamine A C-N lyase from
            Flavobacterium saccharophilum.
  JOURNAL   J. Biochem. (Tokyo). 98 (1985) 1631-8.
  ORGANISM  Flavobacterium saccharophilum
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.3.1
            ExPASy - ENZYME nomenclature database: 4.3.3.1
            ExplorEnz - The Enzyme Database: 4.3.3.1
            ERGO genome analysis and discovery system: 4.3.3.1
            BRENDA, the Enzyme Database: 4.3.3.1
            CAS: 99889-98-2
///
ENTRY       EC 4.3.3.2                  Enzyme
NAME        strictosidine synthase;
            strictosidine synthetase;
            STR;
            3-alpha(S)-strictosidine tryptamine-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Amine-lyases
SYSNAME     3-alpha(S)-strictosidine tryptamine-lyase (secologanin-forming)
REACTION    3-alpha(S)-strictosidine + H2O = tryptamine + secologanin
            [RN:R03738]
ALL_REAC    R03738
SUBSTRATE   3-alpha(S)-strictosidine [CPD:C03470];
            H2O [CPD:C00001]
PRODUCT     tryptamine [CPD:C00398];
            secologanin [CPD:C01852]
COMMENT     Catalyses a Pictet-Spengler reaction between the aldehyde group of
            secologanin and the amino group of tryptamine [4,5]. Involved in the
            biosynthesis of the monoterpenoid indole alkaloids.
REFERENCE   1  [PMID:510306]
  AUTHORS   Treimer JF, Zenk MH.
  TITLE     Purification and properties of strictosidine synthase, the key
            enzyme in indole alkaloid formation.
  JOURNAL   Eur. J. Biochem. 101 (1979) 225-33.
  ORGANISM  Catharanthus roseus
REFERENCE   2  [PMID:7763429]
  AUTHORS   Kutchan TM.
  TITLE     Strictosidine: from alkaloid to enzyme to gene.
  JOURNAL   Phytochemistry. 32 (1993) 493-506.
  ORGANISM  Catharanthus roseus, Rauvolfia serpentina
REFERENCE   3  [PMID:7887913]
  AUTHORS   de Waal A, Meijer AH, Verpoorte R.
  TITLE     Strictosidine synthase from Catharanthus roseus: purification and
            characterization of multiple forms.
  JOURNAL   Biochem. J. 306 ( Pt 2) (1995) 571-80.
  ORGANISM  Catharanthus roseus
REFERENCE   4  [PMID:16133216]
  AUTHORS   Ruppert M, Woll J, Giritch A, Genady E, Ma X, Stockigt J.
  TITLE     Functional expression of an ajmaline pathway-specific esterase from
            Rauvolfia in a novel plant-virus expression system.
  JOURNAL   Planta. 222 (2005) 888-98.
  ORGANISM  Rauvolfia serpentina
REFERENCE   5  [PMID:16481164]
  AUTHORS   McCoy E, Galan MC, O'Connor SE.
  TITLE     Substrate specificity of strictosidine synthase.
  JOURNAL   Bioorg. Med. Chem. Lett. 16 (2006) 2475-8.
  ORGANISM  Catharanthus roseus
REFERENCE   6  [PMID:16531499]
  AUTHORS   Ma X, Panjikar S, Koepke J, Loris E, Stockigt J.
  TITLE     The structure of Rauvolfia serpentina strictosidine synthase is a
            novel six-bladed beta-propeller fold in plant proteins.
  JOURNAL   Plant. Cell. 18 (2006) 907-20.
  ORGANISM  Rauvolfia serpentina
PATHWAY     PATH: map00900  Terpenoid biosynthesis
            PATH: map00901  Indole and ipecac alkaloid biosynthesis
ORTHOLOGY   KO: K01757  strictosidine synthase
GENES       DME: Dmel_CG11833(Ssl2) Dmel_CG3373(Hmu)
            ATH: AT1G74010 AT1G74020(SS2)
            BBT: BBta_4828
            RHA: RHA1_ro00912
            LIL: LA4215
            LIC: LIC13366
STRUCTURES  PDB: 2FP8  2FP9  2FPB  2FPC  
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.3.2
            ExPASy - ENZYME nomenclature database: 4.3.3.2
            ExplorEnz - The Enzyme Database: 4.3.3.2
            ERGO genome analysis and discovery system: 4.3.3.2
            BRENDA, the Enzyme Database: 4.3.3.2
            CAS: 69669-72-3
///
ENTRY       EC 4.3.3.3                  Enzyme
NAME        deacetylisoipecoside synthase;
            deacetylisoipecoside dopamine-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Amine-lyases
SYSNAME     deacetylisoipecoside dopamine-lyase (secologanin-forming)
REACTION    deacetylisoipecoside + H2O = dopamine + secologanin [RN:R05750]
ALL_REAC    R05750
SUBSTRATE   deacetylisoipecoside [CPD:C07304];
            H2O [CPD:C00001]
PRODUCT     dopamine [CPD:C03758];
            secologanin [CPD:C01852]
COMMENT     The enzyme from the leaves of Alangium lamarckii differs in
            enantiomeric specificity from EC 4.3.3.4 deacetylipecoside synthase.
            The product is rapidly converted to demethylisoalangiside.
REFERENCE   1
  AUTHORS   DeEknamkul, W., Ounaroon, A., Tanahashi, T., Kutchan, T. and Zenk,
            M.H.
  TITLE     Enzymatic condensation of dopamine and secologanin by cell-free
            extracts of Alangium lamarckii.
  JOURNAL   Phytochemistry 45 (1997) 477-484.
  ORGANISM  Alangium lamarckii
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.3.3
            ExPASy - ENZYME nomenclature database: 4.3.3.3
            ExplorEnz - The Enzyme Database: 4.3.3.3
            ERGO genome analysis and discovery system: 4.3.3.3
            BRENDA, the Enzyme Database: 4.3.3.3
///
ENTRY       EC 4.3.3.4                  Enzyme
NAME        deacetylipecoside synthase;
            deacetylipecoside dopamine-lyase
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Amine-lyases
SYSNAME     deacetylipecoside dopamine-lyase (secologanin-forming)
REACTION    deacetylipecoside + H2O = dopamine + secologanin [RN:R05749]
ALL_REAC    R05749
SUBSTRATE   deacetylipecoside [CPD:C07307];
            H2O [CPD:C00001]
PRODUCT     dopamine [CPD:C03758];
            secologanin [CPD:C01852]
COMMENT     The enzyme from the leaves of Alangium lamarckii differs in
            enantiomeric specificity from EC 4.3.3.3 deacetylisoipecoside
            synthase. The product is rapidly converted to demethylalangiside.
REFERENCE   1
  AUTHORS   DeEknamkul, W., Ounaroon, A., Tanahashi, T., Kutchan, T. and Zenk,
            M.H.
  TITLE     Enzymatic condensation of dopamine and secologanin by cell-free
            extracts of Alangium lamarckii.
  JOURNAL   Phytochemistry 45 (1997) 477-484.
  ORGANISM  Alangium lamarckii
PATHWAY     PATH: map00901  Indole and ipecac alkaloid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.3.4
            ExPASy - ENZYME nomenclature database: 4.3.3.4
            ExplorEnz - The Enzyme Database: 4.3.3.4
            ERGO genome analysis and discovery system: 4.3.3.4
            BRENDA, the Enzyme Database: 4.3.3.4
///
ENTRY       EC 4.3.3.-                  Enzyme
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Amine-lyases
REACTION    (1) Ethanolamine + Acetaldehyde <=> Diethanolamine [RN:R05381];
            (2) Triethanolamine <=> Diethanolamine + Acetaldehyde [RN:R05382]
SUBSTRATE   Ethanolamine [CPD:C00189];
            Acetaldehyde [CPD:C00084];
            Triethanolamine [CPD:C06771]
PRODUCT     Diethanolamine [CPD:C06772];
            Acetaldehyde [CPD:C00084]
///
ENTRY       EC 4.3.99.1       Obsolete  Enzyme
NAME        Transferred to 4.2.1.104
CLASS       Lyases;
            Carbon-nitrogen lyases;
            Other carbon-nitrogen lyases (deleted sub-subclass)
COMMENT     Transferred entry: now EC 4.2.1.104 cyanate hydratase (EC 4.3.99.1
            created 1972 as EC 3.5.5.3, transferred 1990 to EC 4.3.99.1, deleted
            2001)
STRUCTURES  PDB: 1DW9  1DWK  
DBLINKS     IUBMB Enzyme Nomenclature: 4.3.99.1
            ExPASy - ENZYME nomenclature database: 4.3.99.1
            ExplorEnz - The Enzyme Database: 4.3.99.1
            ERGO genome analysis and discovery system: 4.3.99.1
            BRENDA, the Enzyme Database: 4.3.99.1
///
ENTRY       EC 4.4.1.1                  Enzyme
NAME        cystathionine gamma-lyase;
            homoserine deaminase;
            homoserine dehydratase;
            cystine desulfhydrase;
            cysteine desulfhydrase;
            gamma-cystathionase;
            cystathionase;
            homoserine deaminase-cystathionase;
            gamma-CTL;
            cystalysin;
            cysteine lyase;
            L-cystathionine cysteine-lyase (deaminating)
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     L-cystathionine cysteine-lyase (deaminating; 2-oxobutanoate-forming)
REACTION    L-cystathionine + H2O = L-cysteine + NH3 + 2-oxobutanoate
            [RN:R01001]
ALL_REAC    R01001;
            (other) R00782 R02408 R04930
SUBSTRATE   L-cystathionine [CPD:C02291];
            H2O [CPD:C00001]
PRODUCT     L-cysteine [CPD:C00097];
            NH3 [CPD:C00014];
            2-oxobutanoate [CPD:C00109]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
EFFECTOR    Cysteine [CPD:C00736]
COMMENT     A multifunctional pyridoxal-phosphate protein. Also catalyses
            elimination reactions of L-homoserine to form H2O, NH3 and
            2-oxobutanoate, of L-cystine, producing thiocysteine, pyruvate and
            NH3, and of L-cysteine producing pyruvate, NH3 and H2S.
REFERENCE   1
  AUTHORS   Braunstein, A.E. and Azarkh, R.M.
  TITLE     [Participation of vitamin B6 in enzymic formation of hydrogen
            sulfide from L-cysteine.].
  JOURNAL   Dokl. Akad. Nauk. S.S.S.R. 71 (1950) 93-96.
REFERENCE   2
  AUTHORS   Braunstein, A.E. and Azarkh, R.M.
  TITLE     [Phosphopyridoxal in aerobic deamination of homoserine and serine.].
  JOURNAL   Dokl. Akad. Nauk. S.S.S.R. 85 (1952) 385-388.
REFERENCE   3  [PMID:14209951]
  AUTHORS   FLAVIN M, SEGAL A.
  TITLE     PURIFICATION AND PROPERTIES OF THE CYSTATHIONINE GAMMA-CLEAVAGE
            ENZYME OF NEUROSPORA.
  JOURNAL   J. Biol. Chem. 239 (1964) 2220-7.
  ORGANISM  Neurospora sp.
REFERENCE   4  [PMID:13641250]
  AUTHORS   MATSUO Y, GREENBERG DM.
  TITLE     A crystalline enzyme that cleaves homoserine and cystathionine. III.
            Coenzyme resolution, activators, and inhibitors.
  JOURNAL   J. Biol. Chem. 234 (1959) 507-15.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:13641251]
  AUTHORS   MATSUO Y, GREENBERG DM.
  TITLE     A crystalline enzyme that cleaves homoserine and cystathionine. IV.
            Mechanism of action, reversibility, and substrate specificity.
  JOURNAL   J. Biol. Chem. 234 (1959) 516-9.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00271  Methionine metabolism
            PATH: map00272  Cysteine metabolism
            PATH: map00450  Selenoamino acid metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K01758  cystathionine gamma-lyase
GENES       HSA: 1491(CTH)
            MMU: 107869(Cth)
            RNO: 24962(Cth)
            DRE: 322055(cth)
            DME: Dmel_CG5345
            CEL: C12C8.2 F22B8.6 ZK1127.10
            CME: CMT389C
            SCE: YAL012W(CYS3)
            AGO: AGOS_AEL341W
            PIC: PICST_77247(CYS3)
            CGR: CAGL0H06369g
            ANI: AN1446.2
            AFM: AFUA_8G04340
            AOR: AO090103000051
            CNE: CNN01730
            DDI: DDB_0191318(cysA)
            TET: TTHERM_00052400
            PLU: plu0523
            XCC: XCC0598(metB)
            XCB: XC_3635
            XAC: XAC3602(metB)
            XOO: XOO0778(metB)
            XOM: XOO_0708(XOO0708)
            PAE: PA0400
            PPU: PP_4594
            PPF: Pput_1294
            MMW: Mmwyl1_2049
            NGO: NGO0386
            CVI: CV_3394 CV_4049(metB)
            BBA: Bd3795(metB)
            AFW: Anae109_3845
            MLO: mll4503 mlr1566
            OAN: Oant_0398
            RPA: RPA0371(metB) RPA2357
            SIL: SPO3344
            RSH: Rsph17029_1561
            SAL: Sala_0483
            SWI: Swit_1198
            ABA: Acid345_0668
            BSU: BG12291(yrhB)
            BHA: BH1736
            BCY: Bcer98_3326
            BTL: BALH_4012(nifS)
            BLI: BL02018(yrhB)
            BLD: BLi02853(yrhB)
            BCL: ABC0866
            GKA: GK2540
            SPZ: M5005_Spy_0724
            SPA: M6_Spy0750
            SPB: M28_Spy0704
            LSL: LSL_0027(metC)
            MPA: MAP3053c
            RHA: RHA1_ro06506
            SCO: SCO3920(cysA)
            SMA: SAV4273(cysA1)
            KRA: Krad_3476
            SEN: SACE_6136
            BLO: BL1559
            RBA: RB6443(metB)
            AVA: Ava_4213
            PMN: PMN2A_1743
            PMI: PMT9312_0404
            FJO: Fjoh_0710 Fjoh_1496
            RCA: Rcas_3672
            TPT: Tpet_1501
            MBN: Mboo_1991
            HAL: VNG0796G(cgs)
            NPH: NP4746A(metB)
            TAC: Ta0080
            TVO: TVN0174
            PFU: PF1266
            APE: APE_1226
            PAS: Pars_1485
STRUCTURES  PDB: 1N8P  
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.1
            ExPASy - ENZYME nomenclature database: 4.4.1.1
            ExplorEnz - The Enzyme Database: 4.4.1.1
            ERGO genome analysis and discovery system: 4.4.1.1
            BRENDA, the Enzyme Database: 4.4.1.1
            CAS: 9012-96-8
///
ENTRY       EC 4.4.1.2                  Enzyme
NAME        homocysteine desulfhydrase;
            homocysteine desulfurase, L-homocysteine hydrogen-sulfide-lyase
            (deaminating)
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     L-homocysteine hydrogen-sulfide-lyase (deaminating;
            2-oxobutanoate-forming)
REACTION    L-homocysteine + H2O = hydrogen sulfide + NH3 + 2-oxobutanoate
            [RN:R01283]
ALL_REAC    R01283
SUBSTRATE   L-homocysteine [CPD:C00155];
            H2O [CPD:C00001]
PRODUCT     hydrogen sulfide [CPD:C00283];
            NH3 [CPD:C00014];
            2-oxobutanoate [CPD:C00109]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:14917685]
  AUTHORS   KALLIO RE.
  TITLE     Function of pyridoxal phosphate in desulfhydrase systems of Proteus
            morganii.
  JOURNAL   J. Biol. Chem. 192 (1951) 371-7.
  ORGANISM  Proteus morganii
PATHWAY     PATH: map00910  Nitrogen metabolism
            PATH: map00920  Sulfur metabolism
GENES       ZMO: ZMO0858(nifS) ZMO1022(nifS)
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.2
            ExPASy - ENZYME nomenclature database: 4.4.1.2
            ExplorEnz - The Enzyme Database: 4.4.1.2
            ERGO genome analysis and discovery system: 4.4.1.2
            BRENDA, the Enzyme Database: 4.4.1.2
            CAS: 9024-41-3
///
ENTRY       EC 4.4.1.3                  Enzyme
NAME        dimethylpropiothetin dethiomethylase;
            desulfhydrase;
            S,S-dimethyl-beta-propiothetin dimethyl-sulfide-lyase
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     S,S-dimethyl-beta-propiothetin dimethyl-sulfide-lyase
            (acrylate-forming)
REACTION    S,S-dimethyl-beta-propiothetin = dimethyl sulfide + acrylate
            [RN:R02574]
ALL_REAC    R02574
SUBSTRATE   S,S-dimethyl-beta-propiothetin [CPD:C04022]
PRODUCT     dimethyl sulfide [CPD:C00580];
            acrylate [CPD:C00511]
REFERENCE   1  [PMID:13366990]
  AUTHORS   ANDERSON DG, CANTONI GL.
  TITLE     Enzymatic cleavage of dimethylpropiothetin by Polysiphonia lanosa.
  JOURNAL   J. Biol. Chem. 222 (1956) 171-7.
  ORGANISM  Polysiphonia lanosa
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.3
            ExPASy - ENZYME nomenclature database: 4.4.1.3
            ExplorEnz - The Enzyme Database: 4.4.1.3
            ERGO genome analysis and discovery system: 4.4.1.3
            BRENDA, the Enzyme Database: 4.4.1.3
            CAS: 9026-85-1
///
ENTRY       EC 4.4.1.4                  Enzyme
NAME        alliin lyase;
            alliinase;
            cysteine sulfoxide lyase;
            alkylcysteine sulfoxide lyase;
            S-alkylcysteine sulfoxide lyase;
            L-cysteine sulfoxide lyase;
            S-alkyl-L-cysteine sulfoxide lyase;
            alliin alkyl-sulfenate-lyase
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     S-alkyl-L-cysteine S-oxide alkyl-sulfenate-lyase
            (2-aminoacrylate-forming)
REACTION    an S-alkyl-L-cysteine S-oxide = an alkyl sulfenate + 2-aminoacrylate
            [RN:R03901]
ALL_REAC    R03901
SUBSTRATE   S-alkyl-L-cysteine S-oxide [CPD:C03726]
PRODUCT     alkyl sulfenate [CPD:C02245];
            2-aminoacrylate [CPD:C02218]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1
  AUTHORS   Durbin, R.D. and Uchytil, T.F.
  TITLE     Purification and properties of alliin lyase from the fungus
            Penicillium corymbiferum.
  JOURNAL   Biochim. Biophys. Acta 235 (1971) 518-520.
  ORGANISM  Penicillium corymbiferum
REFERENCE   2
  AUTHORS   Goryachenkova, E.V.
  TITLE     [Enzyme in garlic which forms allycine (allyinase), a protein with
            phosphopyridoxal.].
  JOURNAL   Dokl. Akad. Nauk. S.S.S.R. 87 (1952) 457-460.
REFERENCE   3
  AUTHORS   Jacobsen, J.V., Yamaguchi, M., Howard, F.D. and Bernhard, R.A.
  TITLE     Product inhibition of the cysteine sulfoxide lyase of Tulbaghia
            violacea.
  JOURNAL   Arch. Biochem. Biophys. 127 (1968) 252-258.
  ORGANISM  Tulbaghia violacea
STRUCTURES  PDB: 1LK9  2HOR  2HOX  
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.4
            ExPASy - ENZYME nomenclature database: 4.4.1.4
            ExplorEnz - The Enzyme Database: 4.4.1.4
            ERGO genome analysis and discovery system: 4.4.1.4
            BRENDA, the Enzyme Database: 4.4.1.4
            CAS: 9031-77-0
///
ENTRY       EC 4.4.1.5                  Enzyme
NAME        lactoylglutathione lyase;
            methylglyoxalase;
            aldoketomutase;
            ketone-aldehyde mutase;
            glyoxylase I;
            (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing)
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing;
            glutathione-forming)
REACTION    (R)-S-lactoylglutathione = glutathione + methylglyoxal [RN:R02530]
ALL_REAC    R02530
SUBSTRATE   (R)-S-lactoylglutathione [CPD:C03451]
PRODUCT     glutathione [CPD:C00051];
            methylglyoxal [CPD:C00546]
INHIBITOR   S-(N-Hydroxy-N-methylcarbamoyl)glutathione [CPD:C04572]
COMMENT     Also acts on 3-phosphoglycerol-glutathione.
REFERENCE   1  [PMID:4574550]
  AUTHORS   Ekwall K, Mannervik B.
  TITLE     The stereochemical configuration of the lactoyl group of
            S-lactoylglutathionine formed by the action of glyoxalase I from
            porcine erythrocytes and yeast.
  JOURNAL   Biochim. Biophys. Acta. 297 (1973) 297-9.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:14841219]
  AUTHORS   RACKER E.
  TITLE     The mechanism of action of glyoxalase.
  JOURNAL   J. Biol. Chem. 190 (1951) 685-96.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K01759  lactoylglutathione lyase
GENES       HSA: 2739(GLO1)
            PTR: 748215(GLO1)
            MMU: 109801(Glo1)
            RNO: 294320(Glo1)
            CFA: 474894(GLO1)
            BTA: 540335(MGC139859)
            GGA: 421428(GLO1)
            XLA: 446359(MGC82317) 447401(MGC84827)
            DRE: 368213(glo1)
            SPU: 577630(LOC577630)
            DME: Dmel_CG1707
            OSA: 4338324
            CME: CMD108C
            SCE: YML004C(GLO1)
            AGO: AGOS_ADR285W AGOS_ADR286C
            PIC: PICST_64811(GLO1)
            CGR: CAGL0L07656g
            SPO: SPBC21D10.03c
            ANI: AN4174.2
            AFM: AFUA_2G13550 AFUA_5G14830 AFUA_6G07940
            AOR: AO090003000140
            CNE: CNI03610
            DDI: DDB_0230987(gloA)
            PFA: PF11_0145 PFF0230c
            TET: TTHERM_00572000
            TCR: 510659.240 510743.70
            LMA: LmjF35.3010
            ECO: b1651(gloA)
            ECJ: JW1643(gloA)
            ECE: Z2669(gloA)
            ECS: ECs2360
            ECC: c2044(gloA)
            ECI: UTI89_C1842(gloA)
            ECP: ECP_1597
            ECV: APECO1_733(gloA)
            ECW: EcE24377A_1862(gloA)
            ECX: EcHS_A1728(gloA)
            STY: STY1687(gloA)
            STT: t1303(gloA)
            SPT: SPA1418(gloA)
            SEC: SC1454(gloA)
            STM: STM1435(gloA)
            YPE: YPO2381(gloA)
            YPK: y1957(gloA)
            YPM: YP_2167(gloA1)
            YPA: YPA_1727
            YPN: YPN_1836
            YPP: YPDSF_0765
            YPS: YPTB2295(gloA)
            YPI: YpsIP31758_1760(gloA)
            SFL: SF1678(gloA)
            SFX: S1810(gloA)
            SFV: SFV_1671(gloA)
            SSN: SSON_1505(gloA)
            SBO: SBO_1484(gloA)
            SDY: SDY_1877(gloA)
            ECA: ECA1929(gloA) ECA2168
            PLU: plu2602(gloA)
            ENT: Ent638_1795
            SPE: Spro_2200
            HIN: HI0323(gloA)
            HIT: NTHI0441(gloA)
            HDU: HD0610(gloA)
            HSO: HS_0502(gloA)
            PMU: PM0987(gloA)
            MSU: MS0597(gloA) MS0703(gloA)
            APL: APL_0181(gloA)
            ASU: Asuc_1808
            XFA: XF1399
            XFT: PD0629(gloA)
            XCC: XCC0575(gloA)
            XCB: XC_3658
            XCV: XCV3749(gloA)
            XAC: XAC3632(gloA)
            XOO: XOO0754(gloA)
            XOM: XOO_0684(XOO0684)
            VCH: VC1010
            VCO: VC0395_A0531(gloA)
            VVU: VV1_2016 VV1_3100
            VVY: VV0155 VV1185 VV2400
            VPA: VP2109 VP2166 VPA0302 VPA0774
            VFI: VF0928 VF1212 VFA0119 VFA0640
            PPR: PBPRA2567 PBPRB0895
            PAE: PA0710(gloA2) PA3524(gloA1) PA5111(gloA3)
            PAU: PA14_18750(gloA1) PA14_67500(gloA3)
            PAP: PSPA7_1623(gloA2) PSPA7_5844(gloA1)
            PPU: PP_3766(gloA)
            PPF: Pput_1997
            PST: PSPTO_3106(gloA)
            PSB: Psyr_2973
            PSP: PSPPH_2267(gloA)
            PFL: PFL_3393(gloA)
            PFO: Pfl_2923
            PEN: PSEEN3212(gloA)
            PMY: Pmen_1395 Pmen_4207
            PAR: Psyc_0218(gloA)
            PCR: Pcryo_0241
            PRW: PsycPRwf_0406
            ACI: ACIAD2213(gloA)
            SON: SO_2044(gloA)
            SDN: Sden_1873
            SFR: Sfri_2098 Sfri_2179
            SAZ: Sama_1837
            SBL: Sbal_2269
            SBM: Shew185_2057
            SLO: Shew_2073
            SPC: Sputcn32_2101
            SSE: Ssed_2037 Ssed_2709
            SPL: Spea_2360
            SHE: Shewmr4_2107
            SHM: Shewmr7_1867
            SHN: Shewana3_2232
            SHW: Sputw3181_1911
            ILO: IL1434(gloA) IL2633
            CPS: CPS_1846 CPS_2191(gloA)
            PHA: PSHAa1091(gloA) PSHAa1601(gloA)
            PAT: Patl_1402 Patl_2635
            SDE: Sde_2413
            PIN: Ping_0169
            MAQ: Maqu_3005
            LPN: lpg1882(gloA)
            LPF: lpl1843
            LPP: lpp1846
            MCA: MCA1648(gloA)
            FTU: FTT1212c(gloA)
            FTF: FTF1212c(gloA)
            FTW: FTW_0734(gloA)
            FTL: FTL_0732
            FTH: FTH_0734(gloA)
            FTA: FTA_0772(gloA)
            FTN: FTN_1231(gloA)
            TCX: Tcr_1536
            NOC: Noc_2681
            HHA: Hhal_0906
            HCH: HCH_01189(gloA1) HCH_04598(gloA2)
            CSA: Csal_0217 Csal_0685
            ABO: ABO_0095(gloA) ABO_0726(gloA)
            AHA: AHA_2563 AHA_2641(gloA) AHA_3972
            DNO: DNO_0735
            NME: NMB0340
            NMA: NMA2147(gloA)
            NMC: NMC1830(gloA)
            CVI: CV_1660(gloA)
            RSO: RSc0520(gloA)
            REU: Reut_A0503
            REH: H16_A0274 H16_A0517(gloA1) H16_A2179 H16_B1143(gloA2)
                 H16_B2255(gloA5)
            RME: Rmet_0442
            BMA: BMA0213(gloA)
            BMV: BMASAVP1_A2732(gloA)
            BML: BMA10299_A2346(gloA)
            BMN: BMA10247_2426(gloA)
            BXE: Bxe_A1399 Bxe_A4018
            BVI: Bcep1808_2807
            BUR: Bcep18194_A6033
            BCN: Bcen_2094
            BCH: Bcen2424_2706
            BAM: Bamb_2758
            BPS: BPSL0663(gloA)
            BPM: BURPS1710b_0876(gloA)
            BPL: BURPS1106A_0712(gloA)
            BPD: BURPS668_0697(gloA)
            BTE: BTH_I0580(gloA)
            PNU: Pnuc_0823
            BPE: BP0038(gloA)
            BPA: BPP3659(gloA)
            BBR: BB4094(gloA)
            RFR: Rfer_2552 Rfer_2801
            POL: Bpro_2168 Bpro_3549
            PNA: Pnap_2984
            AAV: Aave_2791
            AJS: Ajs_2047
            VEI: Veis_2703
            MPT: Mpe_A0933 Mpe_A1018 Mpe_A2925
            HAR: HEAR0370(gloA)
            MMS: mma_0421(gloA1) mma_0489(gloA2)
            NEU: NE1427(gloA)
            NET: Neut_1541
            NMU: Nmul_A2625
            EBA: ebA3749 ebB148(gloA)
            AZO: azo0692(gloA1) azo1226(lguL) azo2616 azo2654 azo3228(gloA2)
                 azo3679 azo3708
            DAR: Daro_0300 Daro_3539
            TBD: Tbd_2343
            MFA: Mfla_0739
            GSU: GSU3303
            GME: Gmet_3253
            PCA: Pcar_0506 Pcar_1477
            BBA: Bd0456 Bd2848(gloA)
            ADE: Adeh_2111
            AFW: Anae109_2364
            MXA: MXAN_0480(gloA)
            SAT: SYN_00718
            PUB: SAR11_0652(gloA)
            MLO: mll0167
            MES: Meso_1734
            SME: SMc00290(gloA)
            ATU: Atu1802(gloA) Atu2456(lguL)
            ATC: AGR_C_3314 AGR_C_4460
            RET: RHE_CH00481(lguL) RHE_CH01621 RHE_CH01884(gloA)
            RLE: RL0403 RL0508 RL0589 RL1210 RL1211 RL1405 RL1717 RL2101
                 RL3060 RL4121 RL4165 RL4642 pRL120456
            BME: BMEI0164 BMEI0730 BMEI1142 BMEI1888 BMEII0064 BMEII0415
            BMF: BAB1_0053 BAB1_0838 BAB1_1286(gloA)
            BMS: BR0056 BR1268(gloA)
            BMB: BruAb1_0056 BruAb1_1270(gloA) BruAb2_0029
            BOV: BOV_1229(gloA)
            BJA: bll4399(gloA) blr7489(lguL)
            BRA: BRADO3665(gloA) BRADO6075
            BBT: BBta_1707 BBta_4033(gloA)
            RPA: RPA1377 RPA2523
            RPB: RPB_2940
            RPC: RPC_2794
            RPE: RPE_2539 RPE_2920
            NWI: Nwi_1611 Nwi_1871
            CCR: CC_1315
            SIL: SPO0917 SPO1270
            SIT: TM1040_1730 TM1040_1863 TM1040_2289 TM1040_3164
            RSP: RSP_0392 RSP_0812 RSP_3237(lguL)
            RDE: RD1_0545 RD1_1872(gloA) RD1_2192(glo)
            HNE: HNE_3387
            ZMO: ZMO0030(gloA) ZMO0760(gloA) ZMO0761(gloA) ZMO1721(gloA)
            SWI: Swit_1990
            GOX: GOX1824
            GBE: GbCGDNIH1_0946 GbCGDNIH1_1231
            ACR: Acry_2450
            RRU: Rru_A1572 Rru_A2466
            MAG: amb2483
            MGM: Mmc1_3401
            BSU: BG10044(yyaH)
            BAN: BA2111 BA3011 BA3208 BA3399
            BAR: GBAA2111 GBAA3011 GBAA3208 GBAA3399
            BAA: BA_2606 BA_3519 BA_3720 BA_3898
            BAT: BAS1963 BAS2799 BAS2983 BAS3152
            BCE: BC2105 BC2954 BC2993 BC3178 BC5220
            BCA: BCE_2192 BCE_3047 BCE_3232
            BCZ: BCZK0704 BCZK1730 BCZK1918 BCZK2730 BCZK2900 BCZK2910(gloA)
                 BCZK2991 BCZK3046 BCZK3242 BCZK3343 BCZK3346 BCZK4912(glxI)
            BTK: BT9727_0717 BT9727_1752 BT9727_1942 BT9727_2750 BT9727_2965
                 BT9727_2976(gloA) BT9727_3080 BT9727_3138 BT9727_3395
                 BT9727_4899(glxI)
            BTL: BALH_1875 BALH_2695 BALH_2864(gloA) BALH_3024 BALH_3175
                 BALH_3945 BALH_4713(glxI)
            BLI: BL01952(yyaH)
            BLD: BLi01307(yyaH)
            BCL: ABC0834 ABC1752
            BAY: RBAM_021880(yqjT)
            BPU: BPUM_1180(gloA) BPUM_3715
            OIH: OB1861
            GKA: GK1362 GK2350
            SAB: SAB0287
            SAA: SAUSA300_1088 SAUSA300_1458
            LMO: lmo0406 lmo2168
            LMF: LMOf2365_0426 LMOf2365_2200
            LIN: lin0429 lin2271
            LWE: lwe0370 lwe2184
            LLC: LACR_0178
            LLM: llmg_0184
            SPY: SPy_0511(gloA)
            SPZ: M5005_Spy_0421(gloA)
            SPM: spyM18_0569
            SPG: SpyM3_0359(gloA)
            SPS: SPs1494
            SPH: MGAS10270_Spy0422(gloA)
            SPI: MGAS10750_Spy0434(gloA)
            SPJ: MGAS2096_Spy0440(gloA)
            SPK: MGAS9429_Spy0420(gloA)
            SPF: SpyM51449(gloA)
            SPA: M6_Spy0448
            SPB: M28_Spy0409(gloA)
            SPN: SP_0962
            SPR: spr0864(lguL)
            SPD: SPD_0850(gloA)
            SAG: SAG1478(gloA)
            SAN: gbs1544
            SAK: SAK_1508(gloA)
            SMU: SMU.1603(lguL)
            STC: str1532(gloA)
            STL: stu1532(gloA)
            SSA: SSA_0962(lguL)
            SGO: SGO_1035(gloA)
            LSA: LSA0608(gloAN) LSA0609(gloAC)
            LBR: LVIS_2160
            EFA: EF1140(gloA)
            STH: STH1188
            CPE: CPE0447(lguL)
            CPF: CPF_0449
            CPR: CPR_0440(gloA)
            CNO: NT01CX_2371
            CDF: CD1134(gloA)
            CKL: CKL_1146(gloA)
            DSY: DSY1378 DSY4986
            TTE: TTE2386(gloA3)
            CGL: NCgl0903(cgl0940)
            SMA: SAV5402(gloA)
            FNU: FN0356 FN1050
            TDE: TDE1367
            LIL: LA1417(gloA)
            LIC: LIC12328
            SYN: slr0381(gloA)
            SYW: SYNW2347(gloA)
            SYC: syc0887_d(gloA)
            SYF: Synpcc7942_0638
            SYD: Syncc9605_2475
            SYE: Syncc9902_2160
            SYG: sync_2731(gloA)
            SYR: SynRCC307_2362(gloA)
            SYX: SynWH7803_2378(gloA)
            CYA: CYA_1244(gloA)
            GVI: gll3561
            ANA: alr2321
            AVA: Ava_0139
            PMA: Pro0234(gloA)
            PMM: PMM0653(gloA)
            PMT: PMT2084(gloA)
            PMI: PMT9312_0652
            PMB: A9601_07081(gloA)
            PMF: P9303_27731(gloA)
            PMG: P9301_06791(gloA)
            PMH: P9215_07351(gloA)
            TER: Tery_3491
            BTH: BT_1580 BT_1685
            BFR: BF1450 BF2387 BF3288
            BFS: BF1382 BF2471 BF3127
            PGI: PG0745 PG1613
            SRU: SRU_2344
            CHU: CHU_2166(gloA)
            GFO: GFO_0937 GFO_3335
            MMA: MM_3029
            MSI: Msm_1366
            HMA: rrnAC1409(gloA1) rrnAC1966(gloA3) rrnAC2504(lgl)
            HWA: HQ1123A(glo) HQ1605A(glo) HQ1721A(glo) HQ2401A(glo)
                 HQ3086A(gloA)
            NPH: NP1228A(glo_2) NP2650A(glo_4) NP3948A(glo_1) NP4460A(glo_3)
            PAB: PAB2438
            PFU: PF1948
            TKO: TK0330
            RCI: RCIX774(gloA)
            SSO: SSO2426
            STO: ST0554
            SAI: Saci_0923
STRUCTURES  PDB: 1BH5  1F9Z  1FA5  1FA6  1FA7  1FA8  1FRO  1QIN  1QIP  2P25  
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.5
            ExPASy - ENZYME nomenclature database: 4.4.1.5
            ExplorEnz - The Enzyme Database: 4.4.1.5
            ERGO genome analysis and discovery system: 4.4.1.5
            BRENDA, the Enzyme Database: 4.4.1.5
            CAS: 9033-12-9
///
ENTRY       EC 4.4.1.6                  Enzyme
NAME        S-alkylcysteine lyase;
            S-alkylcysteinase;
            alkylcysteine lyase;
            S-alkyl-L-cysteine sulfoxide lyase;
            S-alkyl-L-cysteine lyase;
            S-alkyl-L-cysteinase;
            alkyl cysteine lyase;
            S-alkyl-L-cysteine alkylthiol-lyase (deaminating)
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     S-alkyl-L-cysteine alkyl-thiol-lyase (deaminating; pyruvate-forming)
REACTION    an S-alkyl-L-cysteine + H2O = an alkyl thiol + NH3 + pyruvate
            [RN:R02953]
ALL_REAC    R02953
SUBSTRATE   S-alkyl-L-cysteine [CPD:C02749];
            H2O [CPD:C00001]
PRODUCT     alkyl thiol [CPD:C00812];
            NH3 [CPD:C00014];
            pyruvate [CPD:C00022]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Decomposes S-alkyl-L-cysteines by
            alpha,beta-elimination. Possibly identical, in yeast, with EC
            4.4.1.8 cystathionine beta-lyase.
REFERENCE   1
  AUTHORS   Nomura, J., Nishizuka, Y. and Hayaishi, O.
  TITLE     S-Alkylcysteinase: enzymatic cleavage of S-methyl-L-cysteine and its
            sulfoxide.
  JOURNAL   J. Biol. Chem. 238 (1963) 1441-1446.
  ORGANISM  Pseudomonas cruciviae
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.6
            ExPASy - ENZYME nomenclature database: 4.4.1.6
            ExplorEnz - The Enzyme Database: 4.4.1.6
            ERGO genome analysis and discovery system: 4.4.1.6
            BRENDA, the Enzyme Database: 4.4.1.6
            CAS: 62213-27-8
///
ENTRY       EC 4.4.1.7        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
COMMENT     Deleted entry: S-(hydroxyalkyl)glutathione lyase. Now included with
            EC 2.5.1.18 glutathione transferase (EC 4.4.1.7 created 1972,
            deleted 1976)
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.7
            ExPASy - ENZYME nomenclature database: 4.4.1.7
            ExplorEnz - The Enzyme Database: 4.4.1.7
            ERGO genome analysis and discovery system: 4.4.1.7
            BRENDA, the Enzyme Database: 4.4.1.7
///
ENTRY       EC 4.4.1.8                  Enzyme
NAME        cystathionine beta-lyase;
            beta-cystathionase;
            cystine lyase;
            cystathionine L-homocysteine-lyase (deaminating);
            L-cystathionine L-homocysteine-lyase (deaminating)
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     L-cystathionine L-homocysteine-lyase (deaminating; pyruvate-forming)
REACTION    L-cystathionine + H2O = L-homocysteine + NH3 + pyruvate [RN:R01286]
ALL_REAC    R01286;
            (other) R00782 R01285 R02408 R04941
SUBSTRATE   L-cystathionine [CPD:C02291];
            H2O [CPD:C00001]
PRODUCT     L-homocysteine [CPD:C00155];
            NH3 [CPD:C00014];
            pyruvate [CPD:C00022]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. The enzyme from some sources also
            acts on L-cystine, forming pyruvate, ammonia and cysteine
            persulfide, and a number of related compounds. Possibly identical,
            in yeast, with EC 4.4.1.6 S-alkylcysteine lyase.
REFERENCE   1
  AUTHORS   Anderson, N.W. and Thompson, J.F.
  TITLE     Cystine lyase: beta-cystathionase from turnip roots.
  JOURNAL   Phytochemistry 18 (1979) 1953-1958.
  ORGANISM  turnip
REFERENCE   2  [PMID:14209950]
  AUTHORS   FLAVIN M, SLAUGHTER C.
  TITLE     CYSTATHIONINE CLEAVAGE ENZYMES OF NEUROSPORA.
  JOURNAL   J. Biol. Chem. 239 (1964) 2212-9.
  ORGANISM  Neurospora crassa [GN:dncr]
PATHWAY     PATH: map00271  Methionine metabolism
            PATH: map00272  Cysteine metabolism
            PATH: map00450  Selenoamino acid metabolism
            PATH: map00910  Nitrogen metabolism
            PATH: map00920  Sulfur metabolism
ORTHOLOGY   KO: K01760  cystathionine beta-lyase
GENES       OSA: 4340283
            CME: CMH121C
            SCE: YFR055W(IRC7)
            PIC: PICST_54505(STR3)
            SPO: SPCC61.06
            ANI: AN7051.2
            AFM: AFUA_4G03950 AFUA_7G01590
            AOR: AO090011000323
            LMA: LmjF14.0460 LmjF32.2640
            ECO: b1622(malY) b3008(metC)
            ECJ: JW1614(malY) JW2975(metC)
            ECE: Z2627(malY) Z4361(metC)
            ECS: ECs2330 ECs3892
            ECC: c2014(malY) c3407 c3742(metC)
            ECI: UTI89_C1810(malY) UTI89_C3214 UTI89_C3428(metC)
            ECP: ECP_1566 ECP_3091
            ECV: APECO1_3417(metC) APECO1_3691 APECO1_705(malY)
            ECW: EcE24377A_1830(malY) EcE24377A_3476(metC)
            ECX: EcHS_A1697 EcHS_A3186
            STY: STY3333(metC)
            STT: t3081(metC)
            SPT: SPA3029(metC)
            SEC: SC1481(malY) SC3105(metC)
            STM: STM3161(metC)
            YPE: YPO0278(metC) YPO0681(metC)
            YPK: y0538(metC) y3496(metC)
            YPM: YP_0433(metC2) YP_2996(metC3)
            YPA: YPA_3111 YPA_4004
            YPN: YPN_0538 YPN_3389
            YPS: YPTB0335(metC) YPTB3384(metC)
            YPI: YpsIP31758_0590(metC1) YpsIP31758_3806(metC2)
            YEN: YE1470(uptG)
            SFL: SF1647(malY) SF3053(metC)
            SFX: S1779(malY) S3256(metC)
            SFV: SFV_1639(malY) SFV_3058(metC)
            SSN: SSON_1536(malY) SSON_3151(metC)
            SBO: SBO_1512(malY) SBO_2704 SBO_3002(metC)
            SDY: SDY_1845(malY) SDY_3065(metC)
            ECA: ECA0354(metC)
            PLU: plu3942(metC)
            SGL: SG0280
            BFL: Bfl067(metC)
            BPN: BPEN_069(metC)
            HIT: NTHI0211(metC)
            HIP: CGSHiEE_02675
            HIQ: CGSHiGG_03220
            HSO: HS_0475(metC)
            PMU: PM0738(metC_1) PM0794(metC_2)
            MSU: MS1520(metC)
            APL: APL_0320(metC) APL_0701
            VCH: VC1671
            VCO: VC0395_A1276(metC)
            VVU: VV1_2872
            VVY: VV1399
            VPA: VP1182
            VFI: VF1186 VF1253 VF1718
            PPR: PBPRB0454
            PST: PSPTO_0701(metC-1) PSPTO_4265(metC-2)
            PSB: Psyr_0607
            PSP: PSPPH_0602(metC)
            ACI: ACIAD3222
            SON: SO_2191(metC)
            SDN: Sden_2313
            SFR: Sfri_1621
            SPL: Spea_2520
            SHE: Shewmr4_2204
            SHM: Shewmr7_2281
            SHN: Shewana3_2414
            CPS: CPS_2274(metC)
            PHA: PSHAa1925(metC)
            CBU: CBU_2025(metC)
            LPN: lpg0890(metC)
            LPP: lpp0951(metB)
            MMW: Mmwyl1_3936
            AHA: AHA_1428
            BCI: BCI_0540(metC)
            RSO: RSc1639(metC)
            REU: Reut_A1355 Reut_B3581
            REH: H16_A1447(metC)
            RME: Rmet_1364
            BMA: BMA1314(metC)
            BMV: BMASAVP1_A1803(metC)
            BML: BMA10299_A0093(metC)
            BMN: BMA10247_1074(metC)
            BXE: Bxe_A2333 Bxe_C1131
            BUR: Bcep18194_A5078 Bcep18194_B0833
            BCN: Bcen_6300
            BCH: Bcen2424_1779
            BAM: Bamb_1719 Bamb_4251 Bamb_5045
            BPS: BPSL1542
            BPM: BURPS1710b_2323(metC)
            BPL: BURPS1106A_2195(metC)
            BPD: BURPS668_2158(metC)
            BTE: BTH_I2263(metC)
            BPE: BP0112(metC) BP0815(metC)
            BPA: BPP0671(metC) BPP2145(metC) BPP3415(metC) BPP4355(metC)
            BBR: BB0678(metC) BB1542(metC) BB3865(metC) BB4941(metC)
            RFR: Rfer_2294
            POL: Bpro_2039 Bpro_2595
            VEI: Veis_3477 Veis_4134
            MPT: Mpe_A1615
            HAR: HEAR1919
            MMS: mma_1400
            EBA: ebA4598(metC)
            AZO: azo1054(metZ)
            CJE: Cj1393(metC')
            CJR: CJE1581(metC)
            CJJ: CJJ81176_1392(metC)
            CJU: C8J_1308(metC)
            CJD: JJD26997_0259(metC)
            CCV: CCV52592_0807 CCV52592_1206
            GSU: GSU0944(metC-1) GSU0945(metC-2)
            GME: Gmet_0699
            DPS: DP2948
            AFW: Anae109_4085
            WOL: WD0925(metC)
            WBM: Wbm0493
            AMA: AM284(metC)
            PUB: SAR11_0829(metC)
            MLO: mll8145 mll9139
            MES: Meso_1112 Meso_2364
            PLA: Plav_2983
            SME: SMc02117(metC)
            SMD: Smed_1109 Smed_2419
            ATU: Atu1575(metC)
            ATC: AGR_C_2902
            RET: RHE_CH01899(metC)
            RLE: RL2205(metC) pRL120318(metC)
            BME: BMEI1213
            BMF: BAB1_0760
            BMS: BR0739(metC)
            BMB: BruAb1_0756(metC)
            BOV: BOV_0734(metC)
            OAN: Oant_2559
            BJA: bll4445(metC)
            BRA: BRADO3525 BRADO3914(metC)
            BBT: BBta_3922(metC) BBta_3953 BBta_p0051
            RPA: RPA2559(metC)
            RPB: RPB_2913
            RPC: RPC_2548
            RPD: RPD_2557
            RPE: RPE_2728
            NWI: Nwi_1530
            NHA: Nham_2072
            XAU: Xaut_4545
            CCR: CC_1424
            RSH: Rsph17029_3588
            MMR: Mmar10_1495
            HNE: HNE_1418(metC)
            ZMO: ZMO0327(metC)
            NAR: Saro_2554
            SAL: Sala_2413 Sala_3059
            ELI: ELI_01900
            GOX: GOX0067
            GBE: GbCGDNIH1_0970
            RRU: Rru_A1613
            MAG: amb1294
            ABA: Acid345_1980
            BSU: BG13163(yjcJ)
            BHA: BH1628(metC)
            BAN: BA4480(metC-1) BA4481(metC-2) BA4600(metC-3)
            BAR: GBAA4480(metC-1) GBAA4481(metC-2) GBAA4600(metC-3)
            BAA: BA_4927 BA_4928 BA_5041
            BAT: BAS4158 BAS4159 BAS4268
            BCE: BC4254 BC4366
            BCA: BCE_4336(metC) BCE_4337(metC) BCE_4454(metC)
            BCZ: BCZK4007(metC) BCZK4008(metC) BCZK4116(metC)
            BTK: BT9727_3997(metC) BT9727_3998(metC) BT9727_4105(metC)
            BTL: BALH_3852(metC) BALH_3853(metC) BALH_3957(metC)
            BLI: BL02659
            BLD: BLi01290(yjcJ)
            BAY: RBAM_011940(yjcJ)
            BPU: BPUM_1119(yjcI) BPUM_1120(yjcJ) BPUM_2360(yrhB)
            OIH: OB1109(metC)
            GKA: GK0867
            SAU: SA0346
            SAV: SAV0358
            SAM: MW0334
            SAR: SAR0355
            SAS: SAS0334
            SAC: SACOL0430
            SAB: SAB0308c
            SAA: SAUSA300_0359 SAUSA300_0360 SAUSA300_0434(metB)
            SAO: SAOUHSC_00340
            SEP: SE2380
            SER: SERP0036
            SHA: SH2636
            SSP: SSP2414
            LMO: lmo1679
            LMF: LMOf2365_1703 LMOf2365_1704
            LIN: lin1787
            LWE: lwe1697
            LLA: L0181(metB2)
            LLC: LACR_0831
            LLM: llmg_1776(metC)
            SPY: SPy_0172(metB)
            SPM: spyM18_0170
            SPG: SpyM3_0133(metB)
            SPS: SPs0136
            SPH: MGAS10270_Spy0148(metB)
            SPI: MGAS10750_Spy0152(metB)
            SPJ: MGAS2096_Spy0152(metB) MGAS2096_Spy0153
            SPK: MGAS9429_Spy0148(metB)
            SPF: SpyM50140
            SPA: M6_Spy0192 M6_Spy0750
            SPB: M28_Spy0144(metB)
            STC: str0847(metB2)
            STL: stu0847(metB2)
            LPL: lp_0255(metC1) lp_3517(metC2)
            LAC: LBA1089 LBA1090(metC)
            LSL: LSL_0027(metC)
            LDB: Ldb1187(patC) Ldb1326
            LBU: LBUL_1236
            LCA: LSEI_0600
            EFA: EF0029 EF0290(metC)
            CAC: CAC0391
            CPF: CPF_0169(metC)
            CPR: CPR_0165(metC)
            CDF: CD3029(malY)
            CBO: CBO0726(metC)
            CBA: CLB_0767(metC)
            CBH: CLC_0782(metC)
            CBF: CLI_0815(metC)
            MTC: MT3443
            MPA: MAP3457(metC)
            CGB: cg2536(aecD)
            CEF: CE2211(metC)
            CDI: DIP1736(aecD)
            CJK: jk0592(aecD)
            NFA: nfa35960(metC)
            SCO: SCO0435(malY)
            LXX: Lxx18930(cysD)
            BLO: BL0078(metC)
            BAD: BAD_0507(metC)
            FNU: FN1746
            CHU: CHU_2639(metC)
            GFO: GFO_3443(metC)
            NPH: NP4746A(metB)
            PTO: PTO0477
STRUCTURES  PDB: 1CL1  1CL2  1IBJ  2FQ6  2GQN  
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.8
            ExPASy - ENZYME nomenclature database: 4.4.1.8
            ExplorEnz - The Enzyme Database: 4.4.1.8
            ERGO genome analysis and discovery system: 4.4.1.8
            BRENDA, the Enzyme Database: 4.4.1.8
            CAS: 9055-05-4
///
ENTRY       EC 4.4.1.9                  Enzyme
NAME        L-3-cyanoalanine synthase;
            beta-cyanoalanine synthase;
            beta-cyanoalanine synthetase;
            beta-cyano-L-alanine synthase;
            L-cysteine hydrogen-sulfide-lyase (adding HCN)
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     L-cysteine hydrogen-sulfide-lyase (adding hydrogen cyanide;
            L-3-cyanoalanine-forming)
REACTION    L-cysteine + hydrogen cyanide = L-3-cyanoalanine + hydrogen sulfide
            [RN:R03524]
ALL_REAC    R03524;
            (other) R02846
SUBSTRATE   L-cysteine [CPD:C00097];
            hydrogen cyanide [CPD:C01326]
PRODUCT     L-3-cyanoalanine [CPD:C02512];
            hydrogen sulfide [CPD:C00283]
COMMENT     Contains pyridoxal phospate.
REFERENCE   1  [PMID:1055433]
  AUTHORS   Akopyan TN, Braunstein AE, Goryachenkova EV.
  TITLE     Beta-cyanoalanine synthase: purification and characterization.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 72 (1975) 1617-21.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:5001194]
  AUTHORS   Castric PA, Conn EE.
  TITLE     Formation of  -cyanoalanine by O-acetylserine sulfhydrylase.
  JOURNAL   J. Bacteriol. 108 (1971) 132-6.
  ORGANISM  Bacillus megaterium
REFERENCE   3
  AUTHORS   Hendrickson, H.R.
  TITLE     The beta-cyanoalanine synthase of blue lupine.
  JOURNAL   Fed. Proc. 27 (1968) 593.
REFERENCE   4  [PMID:5769995]
  AUTHORS   Hendrickson HR, Conn EE.
  TITLE     Cyanide metabolism in higher plants. IV. Purification and properties
            of the beta-cyanolanine synthase of blue lupine.
  JOURNAL   J. Biol. Chem. 244 (1969) 2632-40.
  ORGANISM  Lupinus angustifolia
PATHWAY     PATH: map00460  Cyanoamino acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.9
            ExPASy - ENZYME nomenclature database: 4.4.1.9
            ExplorEnz - The Enzyme Database: 4.4.1.9
            ERGO genome analysis and discovery system: 4.4.1.9
            BRENDA, the Enzyme Database: 4.4.1.9
            CAS: 9059-53-4
///
ENTRY       EC 4.4.1.10                 Enzyme
NAME        cysteine lyase;
            cysteine (sulfite) lyase;
            L-cysteine hydrogen-sulfide-lyase (adding sulfite)
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     L-cysteine hydrogen-sulfide-lyase (adding sulfite;
            L-cysteate-forming)
REACTION    L-cysteine + sulfite = L-cysteate + hydrogen sulfide [RN:R00901]
ALL_REAC    R00901
SUBSTRATE   L-cysteine [CPD:C00097];
            sulfite [CPD:C00094]
PRODUCT     L-cysteate [CPD:C00506];
            hydrogen sulfide [CPD:C00283]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Can use a second molecule of cysteine
            (producing lanthionine), or other alkyl thiols, as a replacing
            agent.
REFERENCE   1  [PMID:5813025]
  AUTHORS   Tolosa EA, Chepurnova NK, Khomutov RM, Severin ES.
  TITLE     Reactions catalysed by cysteine lyase from the yolk sac of chicken
            embryo.
  JOURNAL   Biochim. Biophys. Acta. 171 (1969) 369-71.
  ORGANISM  chicken [GN:gga]
PATHWAY     PATH: map00272  Cysteine metabolism
            PATH: map00430  Taurine and hypotaurine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.10
            ExPASy - ENZYME nomenclature database: 4.4.1.10
            ExplorEnz - The Enzyme Database: 4.4.1.10
            ERGO genome analysis and discovery system: 4.4.1.10
            BRENDA, the Enzyme Database: 4.4.1.10
            CAS: 9079-86-1
///
ENTRY       EC 4.4.1.11                 Enzyme
NAME        methionine gamma-lyase;
            L-methioninase;
            methionine lyase;
            methioninase;
            methionine dethiomethylase;
            L-methionine gamma-lyase;
            L-methionine methanethiol-lyase (deaminating)
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     L-methionine methanethiol-lyase (deaminating;
            2-oxobutanoate-forming)
REACTION    L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate [RN:R00654]
ALL_REAC    R00654;
            (other) R04770
SUBSTRATE   L-methionine [CPD:C00073];
            H2O [CPD:C00001]
PRODUCT     methanethiol [CPD:C00409];
            NH3 [CPD:C00014];
            2-oxobutanoate [CPD:C00109]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:4720797]
  AUTHORS   Kreis W, Hession C.
  TITLE     Isolation and purification of
            L-methionine-alpha-deamino-gamma-mercaptomethane-lyase
            (L-methioninase) from Clostridium sporogenes.
  JOURNAL   Cancer. Res. 33 (1973) 1862-5.
  ORGANISM  Clostridium sporogenes
PATHWAY     PATH: map00450  Selenoamino acid metabolism
ORTHOLOGY   KO: K01761  methionine-gamma-lyase
GENES       SPE: Spro_0798
            PPU: PP_1308(mdeA)
            PPF: Pput_4416
            PFL: PFL_3514(megL) PFL_3814(mdeA)
            PEN: PSEEN4515(mdeA)
            SON: SO_1812(mdeA)
            SDN: Sden_2521
            SFR: Sfri_1369
            SAZ: Sama_1242
            SBL: Sbal_0312 Sbal_1622
            SBM: Shew185_1611
            SLO: Shew_2491
            SPC: Sputcn32_0729 Sputcn32_1507
            SSE: Ssed_1559
            SHE: Shewmr4_2477
            SHM: Shewmr7_2545
            SHN: Shewana3_1556 Shewana3_2643
            SHW: Sputw3181_2594 Sputw3181_3444
            ILO: IL0726
            CPS: CPS_1705(megL)
            PHA: PSHAa2044(mdeA)
            AHA: AHA_1947
            RFR: Rfer_3649 Rfer_4139
            CCV: CCV52592_1762
            MLO: mll1618
            SME: SMc01666(mdeA)
            ATU: Atu3806(mdeA)
            ATC: AGR_L_2052
            BJA: bll5911(mdeA)
            RPB: RPB_0450
            CCR: CC_3168
            SIL: SPOA0318(megL)
            SIT: TM1040_2737
            JAN: Jann_1854
            RDE: RD1_2640(mdeA)
            HNE: HNE_3448(mdeA)
            ZMO: ZMO0676
            ACR: Acry_3103
            MGM: Mmc1_0771
            BHA: BH0799
            BAN: BA4906(megL)
            BAR: GBAA4906(megL)
            BAA: BA_5327
            BAT: BAS4553
            BCE: BC4654
            BCA: BCE_4791(megL)
            BCZ: BCZK4398(megL)
            BTK: BT9727_4388(megL)
            BTL: BALH_4232(megL)
            BCL: ABC3938
            OIH: OB3046
            STH: STH832
            CTC: CTC02530
            CNO: NT01CX_0149(megL)
            CDF: CD3577(mdeA)
            CBO: CBO0029(mdeA)
            CBA: CLB_0039(megL)
            CBH: CLC_0047(megL)
            CBF: CLI_0043(megL)
            SMA: SAV7062(mgl)
            SEN: SACE_3377(megL)
            FNU: FN1419
            TDE: TDE2200(megL)
            PGI: PG0343(megL)
            GFO: GFO_2175(mdeA)
            DRA: DR_0921
            DGE: Dgeo_0011
            MAC: MA2532(mgl)
            MBA: Mbar_A3023
            MMA: MM_3085
            HBU: Hbut_0818
STRUCTURES  PDB: 1E5E  1E5F  1GC0  1GC2  1PFF  1PG8  1UKJ  1Y4I  
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.11
            ExPASy - ENZYME nomenclature database: 4.4.1.11
            ExplorEnz - The Enzyme Database: 4.4.1.11
            ERGO genome analysis and discovery system: 4.4.1.11
            UM-BBD (Biocatalysis/Biodegradation Database): 4.4.1.11
            BRENDA, the Enzyme Database: 4.4.1.11
            CAS: 42616-25-1
///
ENTRY       EC 4.4.1.12       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
COMMENT     Deleted entry: sulfoacetaldehyde lyase. Activity due to EC 2.3.3.15,
            sulfoacetaldehyde acetyltransferase. (EC 4.4.1.12 created 1976,
            deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.12
            ExPASy - ENZYME nomenclature database: 4.4.1.12
            ExplorEnz - The Enzyme Database: 4.4.1.12
            ERGO genome analysis and discovery system: 4.4.1.12
            BRENDA, the Enzyme Database: 4.4.1.12
///
ENTRY       EC 4.4.1.13                 Enzyme
NAME        cysteine-S-conjugate beta-lyase;
            cysteine conjugate beta-lyase;
            glutamine transaminase K/cysteine conjugate beta-lyase;
            L-cysteine-S-conjugate thiol-lyase (deaminating)
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     L-cysteine-S-conjugate thiol-lyase (deaminating; pyruvate-forming)
REACTION    RS-CH2-CH(NH3+)COO- = RSH + NH3 + pyruvate [RN:R03528]
ALL_REAC    R03528
SUBSTRATE   RS-CH2-CH(NH3+)COO- [CPD:C02882]
PRODUCT     RSH [CPD:C01336];
            NH3 [CPD:C00014];
            pyruvate [CPD:C00022]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. In the reaction, RH may represent
            aromatic compounds such as 4-bromobenzene and 2,4-dinitrobenzene.
REFERENCE   1  [PMID:721818]
  AUTHORS   Tateishi M, Suzuki S, Shimizu H.
  TITLE     Cysteine conjugate beta-lyase in rat liver. A novel enzyme
            catalyzing formation of thiol-containing metabolites of drugs.
  JOURNAL   J. Biol. Chem. 253 (1978) 8854-9.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K08079  cysteine-S-conjugate beta-lyase
GENES       MMU: 70266(Ccbl1)
            RNO: 311844(Ccbl1)
            CFA: 491310(CCBL1)
STRUCTURES  PDB: 1W7L  1W7M  1W7N  
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.13
            ExPASy - ENZYME nomenclature database: 4.4.1.13
            ExplorEnz - The Enzyme Database: 4.4.1.13
            ERGO genome analysis and discovery system: 4.4.1.13
            BRENDA, the Enzyme Database: 4.4.1.13
            CAS: 68652-57-3
///
ENTRY       EC 4.4.1.14                 Enzyme
NAME        1-aminocyclopropane-1-carboxylate synthase;
            1-aminocyclopropanecarboxylate synthase;
            1-aminocyclopropane-1-carboxylic acid synthase;
            1-aminocyclopropane-1-carboxylate synthetase;
            aminocyclopropanecarboxylic acid synthase;
            aminocyclopropanecarboxylate synthase;
            ACC synthase;
            S-adenosyl-L-methionine methylthioadenosine-lyase
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     S-adenosyl-L-methionine methylthioadenosine-lyase
            (1-aminocyclopropane-1-carboxylate-forming)
REACTION    S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate +
            methylthioadenosine [RN:R00179]
ALL_REAC    R00179
SUBSTRATE   S-adenosyl-L-methionine [CPD:C00019]
PRODUCT     1-aminocyclopropane-1-carboxylate [CPD:C01234];
            methylthioadenosine [CPD:C00170]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. The enzyme catalyses an
            alpha,gamma-elimination.
REFERENCE   1
  AUTHORS   Boller, T., Herner, R.C. and Kende, H.
  TITLE     Assay for and enzymatic formation of an ethylene precursor,
            1-aminocyclopropane-1-carboxylic acid.
  JOURNAL   Planta 145 (1979) 293-303.
  ORGANISM  Lycopersicon esculentum [GN:eles]
REFERENCE   2  [PMID:507845]
  AUTHORS   Yu YB, Adams DO, Yang SF.
  TITLE     1-Aminocyclopropanecarboxylate synthase, a key enzyme in ethylene
            biosynthesis.
  JOURNAL   Arch. Biochem. Biophys. 198 (1979) 280-6.
  ORGANISM  Lycopersicon esculentum [GN:eles]
PATHWAY     PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K01762  1-aminocyclopropane-1-carboxylate synthase
GENES       ATH: AT2G22810(ACS4) AT3G49700(ETO3) AT3G61510(ACS1)
                 AT4G37770(ACS8) AT5G65800(ACS5)
            OSA: 4333976 4336750
STRUCTURES  PDB: 1B8G  1IAX  1IAY  1M4N  1M7Y  1YNU  
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.14
            ExPASy - ENZYME nomenclature database: 4.4.1.14
            ExplorEnz - The Enzyme Database: 4.4.1.14
            ERGO genome analysis and discovery system: 4.4.1.14
            BRENDA, the Enzyme Database: 4.4.1.14
            CAS: 72506-68-4
///
ENTRY       EC 4.4.1.15                 Enzyme
NAME        D-cysteine desulfhydrase;
            D-cysteine lyase;
            D-cysteine sulfide-lyase (deaminating)
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     D-cysteine sulfide-lyase (deaminating; pyruvate-forming)
REACTION    D-cysteine + H2O = sulfide + NH3 + pyruvate [RN:R01874]
ALL_REAC    R01874
SUBSTRATE   D-cysteine [CPD:C00793];
            H2O [CPD:C00001]
PRODUCT     sulfide [CPD:C00297];
            NH3 [CPD:C00014];
            pyruvate [CPD:C00022]
REFERENCE   1  [PMID:3908101]
  AUTHORS   Nagasawa T, Ishii T, Kumagai H, Yamada H.
  TITLE     D-Cysteine desulfhydrase of Escherichia coli. Purification and
            characterization.
  JOURNAL   Eur. J. Biochem. 153 (1985) 541-51.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Schmidt, A.
  TITLE     A cysteine desulfhydrase from spinach leaves specific for
            D-cysteine.
  JOURNAL   Z. Pflanzenphysiol. 107 (1982) 301-312.
  ORGANISM  spinach
REFERENCE   3
  AUTHORS   Schmidt, A. and Erdle, I.
  TITLE     A cysteine desulfhydrase specific for D-cysteine from the green-alga
            Chlorella fusca.
  JOURNAL   Z. Naturforsch. C: Biosci. 38 (1983) 428-435.
  ORGANISM  Chlorella fusca
PATHWAY     PATH: map00272  Cysteine metabolism
ORTHOLOGY   KO: K05396  D-cysteine desulfhydrase
GENES       ECO: b1919(yedO)
            ECJ: JW5313(yedO)
            ECE: Z3008(yedO)
            ECC: c2333(yedO)
            ECI: UTI89_C2120
            ECV: APECO1_960(yedO)
            ECX: EcHS_A2018
            STY: STY2161
            STT: t0923
            SPT: SPA0916(yedO)
            SEC: SC1957(yedO)
            STM: STM1953(yedO)
            YPE: YPO1845(yedO)
            YPK: y2462
            YPM: YP_1548(Acd)
            YPA: YPA_1221
            YPN: YPN_2278
            YPP: YPDSF_1281
            YPS: YPTB1717(yedO)
            YPI: YpsIP31758_2275(dcyD)
            SFL: SF1962(yedO)
            SFX: S2058(yedO)
            SFV: SFV_1963(yedO)
            SSN: SSON_1199(yedO)
            SBO: SBO_1087(yedO)
            SDY: SDY_1098(yedO)
            SGL: SG0911
            ENT: Ent638_2506
            PST: PSPTO_5179
            PSB: Psyr_0359
            PSP: PSPPH_0343(dcyD)
            PFL: PFL_0249
            PFO: Pfl_0245
            PMY: Pmen_2010
            ACI: ACIAD0753
            REU: Reut_B3582
            BMA: BMA2137(dcyD)
            BMV: BMASAVP1_A0774(dcyD)
            BML: BMA10299_A2607(dcyD)
            BMN: BMA10247_2006(dcyD)
            BPS: BPSL2618
            BPM: BURPS1710b_3094(dcyD)
            BPL: BURPS1106A_3059(dcyD)
            BPD: BURPS668_3006(dcyD)
            BTE: BTH_II1216
            AZO: azo0369(csdB)
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.15
            ExPASy - ENZYME nomenclature database: 4.4.1.15
            ExplorEnz - The Enzyme Database: 4.4.1.15
            ERGO genome analysis and discovery system: 4.4.1.15
            BRENDA, the Enzyme Database: 4.4.1.15
            CAS: 84012-74-8
///
ENTRY       EC 4.4.1.16                 Enzyme
NAME        selenocysteine lyase;
            selenocysteine reductase;
            selenocysteine beta-lyase
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     L-selenocysteine selenide-lyase (L-alanine-forming)
REACTION    L-selenocysteine + reduced acceptor = selenide + L-alanine +
            acceptor [RN:R03598]
ALL_REAC    R03598;
            (other) R03599
SUBSTRATE   L-selenocysteine [CPD:C02432];
            reduced acceptor [CPD:C00030]
PRODUCT     selenide [CPD:C01528];
            L-alanine [CPD:C00041];
            acceptor [CPD:C00028]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Dithiothreitol or 2-mercaptoethanol
            can act as the reducing agent in the reaction. The enzyme does not
            act on cysteine, serine or chloroalanine.
REFERENCE   1  [PMID:6461656]
  AUTHORS   Esaki N, Nakamura T, Tanaka H, Soda K.
  TITLE     Selenocysteine lyase, a novel enzyme that specifically acts on
            selenocysteine. Mammalian distribution and purification and
            properties of pig liver enzyme.
  JOURNAL   J. Biol. Chem. 257 (1982) 4386-91.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00450  Selenoamino acid metabolism
ORTHOLOGY   KO: K01763  selenocysteine lyase
GENES       HSA: 51540(SCLY)
            MMU: 50880(Scly)
            RNO: 363285(Scly)
            CFA: 477422(SCLY)
            GGA: 424739(SCLY)
            PIC: PICST_61494(CSD1) PICST_64026(CSD2)
            AFM: AFUA_4G08990
            TAN: TA16295
            TPV: TP01_1094
            ECO: b1680(sufS)
            ECJ: JW1670(sufS)
            ECE: Z2708
            ECS: ECs2387
            ECC: c2075
            ECI: UTI89_C1872(sufS)
            ECP: ECP_1627
            ECV: APECO1_757(sufS)
            ECW: EcE24377A_1896(sufS)
            ECX: EcHS_A1761(sufS)
            STY: STY1750
            STT: t1241
            SEC: SC1393(sufS)
            STM: STM1373(sufS)
            YPE: YPO2400
            YPK: y1938
            YPM: YP_2187(csdB1)
            YPA: YPA_1745
            YPN: YPN_1855
            YPS: YPTB0557 YPTB2310
            YPI: YpsIP31758_1745(sufS)
            SFX: S1842
            SFV: SFV_1703
            SSN: SSON_1476
            SBO: SBO_1450
            SDY: SDY_1911
            ECA: ECA1863(sufS)
            PLU: plu2618(sufS)
            WBR: WGLp357
            SGL: SG1435
            BFL: Bfl362(sufS)
            BPN: BPEN_373(sufS)
            HIT: NTHI1829(nifS)
            XFA: XF1473
            XFT: PD0690(csdB)
            XCC: XCC2769(nifS)
            XCB: XC_1344
            XCV: XCV3082
            XAC: XAC2938(nifS)
            XOO: XOO1402(nifS)
            XOM: XOO_1285(XOO1285)
            VFI: VF0590 VFA0768
            PAE: PA3667
            PPU: PP_1529(csdA)
            PST: PSPTO_1527(csdA)
            PSB: Psyr_1335
            PFL: PFL_1169
            PFO: Pfl_1092
            ACI: ACIAD1582
            SON: SO_3789
            SDN: Sden_0753
            SFR: Sfri_3181
            SHE: Shewmr4_3131
            SHN: Shewana3_0808
            ILO: IL0151(csdA) IL0219(metB)
            CPS: CPS_2211
            CBU: CBU_1357(csdB)
            LPN: lpg0604
            LPF: lpl0639
            MCA: MCA0989(csdB)
            FTU: FTT0578(csdB)
            FTF: FTF0578(csdB)
            FTL: FTL_1333
            FTH: FTH_1298(csdB)
            FTA: FTA_1408
            TCX: Tcr_0582
            AHA: AHA_4239
            DNO: DNO_0834(sufS)
            BCI: BCI_0462(sufS)
            REU: Reut_B5541
            BMA: BMAA0933
            BXE: Bxe_B1552 Bxe_C0124
            BPS: BPSS1341
            BPM: BURPS1710b_A0362
            POL: Bpro_4272
            MPT: Mpe_A0023
            MMS: mma_2535(csdB)
            NEU: NE0573 NE1447
            EBA: ebA6367
            DAR: Daro_2137
            MFA: Mfla_0617
            HPA: HPAG1_0987 HPAG1_1121
            GME: Gmet_2006
            PCA: Pcar_1729
            BBA: Bd0189(csdB)
            SAT: SYN_01071 SYN_01251
            PUB: SAR11_0742(csdB)
            MLO: mlr0021
            MES: Meso_1778
            SME: SMc00533
            ATU: Atu1821(nifS)
            ATC: AGR_C_3344
            RET: RHE_CH02249(ypch00729) RHE_PE00221
            RLE: RL2578(sufS)
            BME: BMEI1039
            BMF: BAB1_0951
            BMS: BR0934
            BMB: BruAb1_0943
            BJA: blr4342(nifS)
            RPA: RPA1424 RPA2467(sufS)
            RPB: RPB_2990
            RPC: RPC_2837 RPC_3637
            RPE: RPE_2964 RPE_3186
            NWI: Nwi_1661(sufS)
            NHA: Nham_2325
            BHE: BH08610(nifS1)
            BQU: BQ05980(nifS2)
            CCR: CC_1860
            SIL: SPO2014(sufS)
            SIT: TM1040_1249
            RSP: RSP_0431
            RDE: RD1_2689(sufS)
            MMR: Mmar10_1319
            ZMO: ZMO0427(csdB)
            GOX: GOX0095
            GBE: GbCGDNIH1_1943 GbCGDNIH1_1944
            MAG: amb1849
            BAR: GBAA5215
            BAA: BA_0088
            BAT: BAS4849
            BCE: BC4981
            BCA: BCE_5118
            BCZ: BCZK4705(nifS)
            BTK: BT9727_4690(csd)
            BLI: BL02164(csd)
            BLD: BLi03449(csd)
            BCL: ABC2976(csd)
            BPU: BPUM_2392(yrvO)
            OIH: OB2378
            LMO: lmo2413
            LMF: LMOf2365_2384
            LIN: lin2508
            LLA: L32195(yseI)
            LLC: LACR_1972
            SPY: SPy_0288
            SPZ: M5005_Spy_0244(nifS3)
            SPM: spyM18_0276
            SPG: SpyM3_0210
            SPS: SPs0216
            SPH: MGAS10270_Spy0244(nifS3) MGAS10270_Spy0686(nifS1)
                 MGAS10270_Spy0960(nifS2)
            SPI: MGAS10750_Spy0241(nifS3) MGAS10750_Spy0718(nifS1)
                 MGAS10750_Spy0995(nifS2)
            SPJ: MGAS2096_Spy0263(nifS3) MGAS2096_Spy0695(nifS1)
                 MGAS2096_Spy0919(nifS2)
            SPK: MGAS9429_Spy0246(nifS3) MGAS9429_Spy0685(nifS1)
                 MGAS9429_Spy0963(nifS2)
            SPF: SpyM50222(csdB) SpyM50944
            SPA: M6_Spy0275
            SPB: M28_Spy0239(nifS3) M28_Spy0610(nifS1) M28_Spy0820(nifS2)
            SPN: SP_0869
            SPR: spr0773
            SAG: SAG0143(csdB)
            SAN: gbs0139
            SAK: SAK_0201(sufS)
            SMU: SMU.249(nifS)
            STC: str0166(nifS1)
            STL: stu0166(nifS1)
            SSA: SSA_1954
            LPL: lp_1470(csd1)
            LJO: LJ1140
            LSA: LSA1111
            LSL: LSL_0860(nifS) LSL_1074(nifS) LSL_1879
            LCA: LSEI_1182
            EFA: EF2392
            STH: STH2036
            CAC: CAC3291
            CDF: CD3670
            CBO: CBO3633(csdB)
            CHY: CHY_0011
            TTE: TTE2670(csdB)
            MTA: Moth_2214
            MHP: MHP7448_0164(nifS)
            MSY: MS53_0322(nifS)
            AYW: AYWB_310(csdB)
            MTU: Rv1464(csd)
            MTC: MT1511
            MBO: Mb1499(csd)
            MLE: ML0842
            MPA: MAP2120c
            MAV: MAV_3315
            MSM: MSMEG_3125
            CGL: NCgl1500(cgl1561)
            CGB: cg1761(nifS2)
            CEF: CE1683
            CDI: DIP1292(csd)
            CJK: jk0981(sufS)
            NFA: nfa35570
            RHA: RHA1_ro04390 RHA1_ro07199(sufS)
            SCO: SCO1921(SCC22.03c)
            SMA: SAV6329
            LXX: Lxx09470(csd)
            PAC: PPA1545
            TFU: Tfu_1983(sufS)
            FRA: Francci3_1664
            FAL: FRAAL4559(csdB) FRAAL5124(iscS) FRAAL6800(nifS)
            SEN: SACE_2177(csdB) SACE_4122
            BLO: BL0869
            BAD: BAD_0713
            RBA: RB3597
            CTA: CTA_0748(yfhO_2)
            PCU: pc0192(sufS)
            TDE: TDE2052
            LIL: LA3560
            LIC: LIC10634
            SYN: slr0077(sufS)
            SYW: SYNW0322
            SYC: syc2353_c(nifS)
            SYF: Synpcc7942_1738
            SYD: Syncc9605_2279
            SYE: Syncc9902_0407
            SYG: sync_2480
            SYR: SynRCC307_2015(csdB)
            SYX: SynWH7803_2147(csd)
            CYA: CYA_0391
            CYB: CYB_1997
            TEL: tlr2068(nifS)
            GVI: glr1373
            ANA: alr2495
            PMA: Pro0083(csdB)
            PMM: PMM0070
            PMT: PMT1603
            PMN: PMN2A_1433(sufS)
            PMB: A9601_00821
            PMC: P9515_00791
            PMF: P9303_03051
            PMG: P9301_00811
            PMH: P9215_00821(csdB)
            PME: NATL1_01341
            TER: Tery_4358
            BTH: BT_3409
            BFR: BF0269
            BFS: BF0225
            PGI: PG0735
            CHU: CHU_1815(sufS)
            TTH: TTC1373
            TTJ: TTHA1735
            HMA: rrnAC1497(nifS) rrnAC3104(csd1)
STRUCTURES  PDB: 1I29  1JF9  1KMJ  1KMK  
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.16
            ExPASy - ENZYME nomenclature database: 4.4.1.16
            ExplorEnz - The Enzyme Database: 4.4.1.16
            ERGO genome analysis and discovery system: 4.4.1.16
            BRENDA, the Enzyme Database: 4.4.1.16
            CAS: 82047-76-5
///
ENTRY       EC 4.4.1.17                 Enzyme
NAME        holocytochrome-c synthase;
            cytochrome c heme-lyase;
            holocytochrome c synthetase;
            holocytochrome-c apocytochrome-c-lyase
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     holocytochrome-c apocytochrome-c-lyase (heme-forming)
REACTION    holocytochrome c = apocytochrome c + heme [RN:R03902]
ALL_REAC    R03902;
            (other) R02480
SUBSTRATE   holocytochrome c [CPD:C02416]
PRODUCT     apocytochrome c [CPD:C02248];
            heme [CPD:C00032]
COMMENT     In the reverse direction, the enzyme catalyses the attachment of
            heme to two cysteine residues in the protein, forming thioether
            links.
REFERENCE   1  [PMID:3034577]
  AUTHORS   Dumont ME, Ernst JF, Hampsey DM, Sherman F.
  TITLE     Identification and sequence of the gene encoding cytochrome c heme
            lyase in the yeast Saccharomyces cerevisiae.
  JOURNAL   EMBO. J. 6 (1987) 235-41.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K01764  cytochrome c heme-lyase
GENES       HSA: 3052(HCCS)
            PTR: 465489(LOC465489)
            MMU: 15159(Hccs)
            CFA: 480834(LOC480834)
            GGA: 424482(RCJMB04_37l21)
            XLA: 380272(hccs-a)
            XTR: 448226(hccs)
            DRE: 58016(hccs)
            SPU: 583826(LOC583826)
            DME: Dmel_CG6022
            CEL: T06D8.6(cchl-1)
            SCE: YAL039C(CYC3)
            AGO: AGOS_ADR382W
            PIC: PICST_33494(CYC3) PICST_37815(CYT2)
            CGR: CAGL0L05280g CAGL0M12012g
            SPO: SPAC24C9.02c SPBC26H8.12
            ANI: AN4415.2 AN6990.2
            AFM: AFUA_4G07120
            AOR: AO090023000863 AO090206000030
            CNE: CNF00970
            UMA: UM04702.1
            DDI: DDBDRAFT_0217711
            PFA: PFL0180w PFL1185c
            TAN: TA15105
            TPV: TP02_0784
            HPA: HPAG1_0267
            PUB: SAR11_0781(ccdA)
            RPA: RPA3812
            BCZ: BCZK3367(ccdA)
            BTK: BT9727_3417(ccdA)
            OIH: OB1677(ccdA)
            GKA: GK0900
            SGO: SGO_1173(ccdA2) SGO_1179(ccdA1)
            AAU: AAur_3288(ccdA) AAur_pTC10144(ccdA) AAur_pTC10197(ccdA)
                 AAur_pTC20033(ccdA)
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.17
            ExPASy - ENZYME nomenclature database: 4.4.1.17
            ExplorEnz - The Enzyme Database: 4.4.1.17
            ERGO genome analysis and discovery system: 4.4.1.17
            BRENDA, the Enzyme Database: 4.4.1.17
            CAS: 75139-03-6
///
ENTRY       EC 4.4.1.18       Obsolete  Enzyme
NAME        Transferred to 1.8.3.5
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
COMMENT     Transferred entry: now EC 1.8.3.5, prenylcysteine oxidase (EC
            4.4.1.18 created 2000, deleted 2002)
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.18
            ExPASy - ENZYME nomenclature database: 4.4.1.18
            ExplorEnz - The Enzyme Database: 4.4.1.18
            ERGO genome analysis and discovery system: 4.4.1.18
            BRENDA, the Enzyme Database: 4.4.1.18
///
ENTRY       EC 4.4.1.19                 Enzyme
NAME        phosphosulfolactate synthase;
            (2R)-phospho-3-sulfolactate synthase;
            (2R)-O-phospho-3-sulfolactate sulfo-lyase
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     (2R)-2-O-phospho-3-sulfolactate hydrogen-sulfite-lyase
            (phosphoenolpyruvate-forming)
REACTION    (2R)-2-O-phospho-3-sulfolactate = phosphoenolpyruvate + hydrogen
            sulfite [RN:R07476]
ALL_REAC    R07476
SUBSTRATE   (2R)-2-O-phospho-3-sulfolactate
PRODUCT     phosphoenolpyruvate [CPD:C00074];
            hydrogen sulfite [CPD:C11481]
COMMENT     Requires Mg2+. The enzyme from Methanococcus jannaschii catalyses
            the Michael addition of sulfite to phosphoenolpyruvate. It
            specifically requires phosphoenolpyruvate and its broad alkaline pH
            optimum suggests that it uses sulfite rather than bisulfite.
REFERENCE   1  [PMID:11830598]
  AUTHORS   Graham DE, Xu H, White RH.
  TITLE     Identification of coenzyme M biosynthetic phosphosulfolactate
            synthase: a new family of sulfonate-biosynthesizing enzymes.
  JOURNAL   J. Biol. Chem. 277 (2002) 13421-9.
  ORGANISM  Methanococcus jannaschii [GN:mja]
ORTHOLOGY   KO: K08097  phosphosulfolactate synthase
GENES       XAU: Xaut_4872 Xaut_5052 Xaut_5069
            SUS: Acid_4865
            BSU: BG13109(yitD)
            BLI: BL02005(yitD)
            BLD: BLi02155(yitD)
            OOE: OEOE_0441
            DRM: Dred_1677
            MTA: Moth_0118
            NCA: Noca_4816 Noca_4839
            SYD: Syncc9605_1170
            SRU: SRU_0020
            MJA: MJ0255
            MMP: MMP0273(comA)
            MMQ: MmarC5_1399
            MMZ: MmarC7_1277
            MAE: Maeo_0153
            MVN: Mevan_1285
            MTH: MTH1674
            MST: Msp_1270(comA)
            MKA: MK0394
STRUCTURES  PDB: 1U83  
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.19
            ExPASy - ENZYME nomenclature database: 4.4.1.19
            ExplorEnz - The Enzyme Database: 4.4.1.19
            ERGO genome analysis and discovery system: 4.4.1.19
            BRENDA, the Enzyme Database: 4.4.1.19
///
ENTRY       EC 4.4.1.20                 Enzyme
NAME        leukotriene-C4 synthase;
            leukotriene C4 synthetase;
            LTC4 synthase;
            LTC4 synthetase;
            leukotriene A4:glutathione S-leukotrienyltransferase;
            (7E,9E,11Z,14Z)-(5S,6R)-5,6-epoxyicosa-7,9,11,14-
            tetraenoate:glutathione leukotriene-transferase
            (epoxide-ring-opening);
            (7E,9E,11Z,14Z)-(5S,6R)-6-(glutathion-S-yl)-5-hydroxyicosa-
            7,9,11,14-tetraenoate glutathione-lyase (epoxide-forming)
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     leukotriene-C4 glutathione-lyase (leukotriene-A4-forming)
REACTION    leukotriene C4 = leukotriene A4 + glutathione [RN:R03059]
ALL_REAC    R03059
SUBSTRATE   leukotriene C4 [CPD:C02166]
PRODUCT     leukotriene A4 [CPD:C00909];
            glutathione [CPD:C00051]
COMMENT     The reaction proceeds in the direction of addition. Not identical
            with EC 2.5.1.18, glutathione transferase.
REFERENCE   1  [PMID:6324687]
  AUTHORS   Bach MK, Brashler JR, Morton DR Jr.
  TITLE     Solubilization and characterization of the leukotriene C4 synthetase
            of rat basophil leukemia cells: a novel, particulate glutathione
            S-transferase.
  JOURNAL   Arch. Biochem. Biophys. 230 (1984) 455-65.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:2846379]
  AUTHORS   Shimizu T.
  TITLE     Enzymes functional in the syntheses of leukotrienes and related
            compounds.
  JOURNAL   Int. J. Biochem. 20 (1988) 661-6.
REFERENCE   3  [PMID:12432940]
  AUTHORS   Lam BK, Austen KF.
  TITLE     Leukotriene C4 synthase: a pivotal enzyme in cellular biosynthesis
            of the cysteinyl leukotrienes.
  JOURNAL   Prostaglandins. Other. Lipid. Mediat. 68-69 (2002) 511-20.
  ORGANISM  human [GN:hsa]
REFERENCE   4  [PMID:12023288]
  AUTHORS   Christmas P, Weber BM, McKee M, Brown D, Soberman RJ.
  TITLE     Membrane localization and topology of leukotriene C4 synthase.
  JOURNAL   J. Biol. Chem. 277 (2002) 28902-8.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00590  Arachidonic acid metabolism
ORTHOLOGY   KO: K00807  leukotriene-C4 synthase
GENES       HSA: 4056(LTC4S)
            MMU: 17001(Ltc4s)
            RNO: 114097(Ltc4s)
            CFA: 607316(LTC4S)
            GGA: 416289(LTC4S)
STRUCTURES  PDB: 2PNO  2UUH  2UUI  
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.20
            ExPASy - ENZYME nomenclature database: 4.4.1.20
            ExplorEnz - The Enzyme Database: 4.4.1.20
            ERGO genome analysis and discovery system: 4.4.1.20
            BRENDA, the Enzyme Database: 4.4.1.20
            CAS: 90698-32-1
///
ENTRY       EC 4.4.1.21                 Enzyme
NAME        S-ribosylhomocysteine lyase;
            S-ribosylhomocysteinase;
            LuxS
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     S-(5-deoxy-D-ribos-5-yl)-L-homocysteine L-homocysteine-lyase
            [(4S)-4,5-dihydroxypentan-2,3-dione-forming]
REACTION    S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine +
            (4S)-4,5-dihydroxypentan-2,3-dione [RN:R01291]
ALL_REAC    R01291
SUBSTRATE   S-(5-deoxy-D-ribos-5-yl)-L-homocysteine [CPD:C03539]
PRODUCT     L-homocysteine [CPD:C00155];
            (4S)-4,5-dihydroxypentan-2,3-dione
COMMENT     Contains Fe2+. The 4,5-dihydroxypentan-2,3-dione formed
            spontaneously cyclizes and combines with borate to form an
            autoinducer (AI-2) in the bacterial quorum-sensing mechanism, which
            is used by many bacteria to control gene expression in response to
            cell density [2].
REFERENCE   1  [PMID:12705835]
  AUTHORS   Zhu J, Dizin E, Hu X, Wavreille AS, Park J, Pei D.
  TITLE     S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein.
  JOURNAL   Biochemistry. 42 (2003) 4717-26.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   2  [PMID:11544353]
  AUTHORS   Miller MB, Bassler BL.
  TITLE     Quorum sensing in bacteria.
  JOURNAL   Annu. Rev. Microbiol. 55 (2001) 165-99.
  ORGANISM  Vibrio harveyi
PATHWAY     PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K07173  S-ribosylhomocysteine lyase
GENES       ECO: b2687(ygaG)
            ECJ: JW2662(luxS)
            ECE: Z3988(ygaG)
            ECS: ECs3549
            ECC: c3244(ygaG)
            ECI: UTI89_C3049(luxS)
            ECV: APECO1_3834(luxS)
            ECW: EcE24377A_2970(luxS)
            ECX: EcHS_A2823(luxS)
            STY: STY2943(luxS)
            STT: t2714(luxS)
            SPT: SPA2675(luxS)
            STM: STM2817(luxS)
            YPE: YPO3300(luxS)
            YPK: y0888
            YPM: YP_0386(luxS)
            YPA: YPA_2844
            YPN: YPN_0794
            YPS: YPTB0830(luxS)
            YPI: YpsIP31758_3233(luxS)
            SFL: SF2714(ygaG)
            SFX: S2901(ygaG)
            SFV: SFV_2817(ygaG)
            SSN: SSON_2831(ygaG)
            SBO: SBO_2830(ygaG)
            SDY: SDY_2884(ygaG)
            ECA: ECA3362(luxS)
            PLU: plu1253(luxS)
            SGL: SG0542
            SPE: Spro_0848
            HIN: HI0491(luxS)
            HIT: NTHI0621(luxS)
            HDU: HD0370(luxS)
            HSO: HS_0550(luxS)
            PMU: PM1054
            MSU: MS0419(luxS)
            APL: APL_1216(luxS)
            ASU: Asuc_0685
            VCH: VC0557
            VVU: VV1_1608
            VVY: VV2792(luxS)
            VPA: VP2537(luxS)
            VFI: VF0545(luxS)
            PPR: PBPRA3045(luxS)
            SON: SO_1101(luxS)
            SDN: Sden_0981
            SFR: Sfri_0947
            SBM: Shew185_3440
            SSE: Ssed_3432
            SPL: Spea_3104
            SHE: Shewmr4_0934
            SHM: Shewmr7_0972
            SHN: Shewana3_0936
            TCX: Tcr_2129
            MMW: Mmwyl1_1324
            AHA: AHA_0700(luxS)
            NME: NMB1981
            NMA: NMA0463
            NGO: NGO2102
            HPY: HP0105
            HPJ: jhp0097
            HPA: HPAG1_0105
            HHE: HH0176(ygaG)
            HAC: Hac_1463(luxS)
            WSU: WS2126
            TDN: Tmden_1938
            CJE: Cj1198
            CJR: CJE1332(luxS)
            CJU: C8J_1142(luxS)
            CCO: CCC13826_2098
            NIS: NIS_1601
            SUN: SUN_0202
            DPS: DP0529(luxS)
            BSU: BG13866(ytjB)
            BHA: BH3353
            BAN: BA5047(luxS)
            BAR: GBAA5047(luxS)
            BAA: BA_5464
            BAT: BAS4687(luxS)
            BCE: BC4789
            BCA: BCE_4946(luxS)
            BCY: Bcer98_3461
            BTK: BT9727_4525(luxS)
            BLI: BL05306(luxS)
            BLD: BLi03209(luxS)
            BCL: ABC2915(luxS)
            BAY: RBAM_027680(luxS)
            BPU: BPUM_2705(luxS)
            OIH: OB1107
            GKA: GK2863
            SAU: SA1936(luxS)
            SAV: SAV2134(luxS)
            SAM: MW2058(luxS)
            SAR: SAR2222(luxS)
            SAS: SAS2037
            SAC: SACOL2126(luxS)
            SAO: SAOUHSC_02375
            SAJ: SaurJH9_2170
            SAH: SaurJH1_2208
            SEP: SE1732
            SER: SERP1741(luxS)
            SHA: SH0901
            SSP: SSP0751
            LMO: lmo1288
            LMF: LMOf2365_1306(luxS)
            LIN: lin1327
            LWE: lwe1305(luxS)
            LLA: L65029(ycgE)
            LLC: LACR_0270
            LLM: llmg_0273(luxS)
            SPY: SPy_1642(luxS)
            SPZ: M5005_Spy_1349(luxS)
            SPM: spyM18_1653(luxS)
            SPG: SpyM3_1384(luxS)
            SPS: SPs0478
            SPH: MGAS10270_Spy1466(luxS)
            SPA: M6_Spy1395(luxS)
            SPN: SP_0340
            SPR: spr0308(luxS)
            SPD: SPD_0309(luxS)
            SAG: SAG0305(luxS)
            SAN: gbs0294
            SMU: SMU.474(luxS)
            STC: str0394(luxS)
            STL: stu0394(luxS)
            SSA: SSA_1853(luxS)
            LPL: lp_0774(luxS)
            LJO: LJ0631
            LAC: LBA1081(luxS)
            LSL: LSL_1173(luxS)
            LDB: Ldb0105(luxS)
            LBU: LBUL_0088
            LBR: LVIS_0340
            LCA: LSEI_0765
            LRE: Lreu_1586
            EFA: EF1182(luxS)
            OOE: OEOE_1562
            CAC: CAC2942
            CPE: CPE0178(luxS)
            CBE: Cbei_1237
            PAC: PPA0450
            BLO: BL1152(luxS)
            BAD: BAD_0493
            BBU: BB0377
            BGA: BG0376
            BAF: BAPKO_0386
            PGI: PG0498(luxS)
            DRA: DR_2387
            DGE: Dgeo_2248
            TTH: TTC1186(luxS)
            TTJ: TTHA1551
STRUCTURES  PDB: 1JQW  2FQO  2FQT  
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.21
            ExPASy - ENZYME nomenclature database: 4.4.1.21
            ExplorEnz - The Enzyme Database: 4.4.1.21
            ERGO genome analysis and discovery system: 4.4.1.21
            BRENDA, the Enzyme Database: 4.4.1.21
            CAS: 37288-63-4
///
ENTRY       EC 4.4.1.22                 Enzyme
NAME        S-(hydroxymethyl)glutathione synthase;
            glutathione-dependent formaldehyde-activating enzyme;
            Gfa;
            S-(hydroxymethyl)glutathione formaldehyde-lyase
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     S-(hydroxymethyl)glutathione formaldehyde-lyase
            (glutathione-forming)
REACTION    S-(hydroxymethyl)glutathione = glutathione + formaldehyde
            [RN:R06982]
ALL_REAC    R06982
SUBSTRATE   S-(hydroxymethyl)glutathione [CPD:C14180]
PRODUCT     glutathione [CPD:C00051];
            formaldehyde [CPD:C00067]
COMMENT     The enzyme from Paracoccus denitrificans accelerates the spontaneous
            reaction in which the adduct of formaldehyde and glutathione is
            formed, i.e. the substrate for EC 1.1.1.284,
            S-(hydroxymethyl)glutathione dehydrogenase, in the
            formaldehyde-detoxification pathway.
REFERENCE   1  [PMID:11741920]
  AUTHORS   Goenrich M, Bartoschek S, Hagemeier CH, Griesinger C, Vorholt JA.
  TITLE     A glutathione-dependent formaldehyde-activating enzyme (Gfa) from
            Paracoccus denitrificans detected and purified via two-dimensional
            proton exchange NMR spectroscopy.
  JOURNAL   J. Biol. Chem. 277 (2002) 3069-72.
  ORGANISM  Paracoccus denitrificans [GN:pde]
PATHWAY     PATH: map00680  Methane metabolism
ORTHOLOGY   KO: K03396  S-(hydroxymethyl)glutathione synthase
GENES       SSE: Ssed_4230
            SPL: Spea_0267 Spea_3387
            SMD: Smed_3930
            BRA: BRADO5487(gfa)
            BBT: BBta_5971(gfa)
            RSQ: Rsph17025_1948
            ACR: Acry_2793
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.22
            ExPASy - ENZYME nomenclature database: 4.4.1.22
            ExplorEnz - The Enzyme Database: 4.4.1.22
            ERGO genome analysis and discovery system: 4.4.1.22
            UM-BBD (Biocatalysis/Biodegradation Database): 4.4.1.22
            BRENDA, the Enzyme Database: 4.4.1.22
///
ENTRY       EC 4.4.1.23                 Enzyme
NAME        2-hydroxypropyl-CoM lyase;
            epoxyalkane:coenzyme M transferase;
            epoxyalkane:CoM transferase;
            epoxyalkane:2-mercaptoethanesulfonate transferase;
            coenzyme M-epoxyalkane ligase;
            epoxyalkyl:CoM transferase;
            epoxypropane:coenzyme M transferase;
            epoxypropyl:CoM transferase;
            EaCoMT;
            2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase
            (epoxyalkane-ring-forming);
            (R)-[or (S)-]2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase
            (epoxyalkane-ring-forming)
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     (R)-2-hydroxypropyl-CoM 2-mercaptoethanesulfonate lyase (cyclizing;
            (R)-1,2-epoxypropane-forming)
REACTION    (1) (R)-2-hydroxypropyl-CoM = (R)-1,2-epoxypropane + HS-CoM
            [RN:R05761 R05762];
            (2) (S)-2-hydroxypropyl-CoM = (S)-1,2-epoxypropane + HS-CoM
ALL_REAC    R05761 R05762
SUBSTRATE   (R)-2-hydroxypropyl-CoM [CPD:C11496];
            (S)-2-hydroxypropyl-CoM [CPD:C11498]
PRODUCT     (R)-1,2-epoxypropane [CPD:C11506];
            HS-CoM [CPD:C03576];
            (S)-1,2-epoxypropane [CPD:C11507]
COMMENT     Requires zinc. Acts on both enantiomers of chiral epoxyalkanes to
            form the corresponding (R)- and (S)-2-hydroxyalkyl-CoM adducts. The
            enzyme will function with some other thiols (e.g.,
            2-sulfanylethanol) as the nucleophile. Uses short-chain epoxyalkanes
            from C2 (epoxyethane) to C6 (1,2-epoxyhexane). This enzyme forms
            component I of a four-component enzyme system {comprising EC
            4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5
            [2-oxopropyl-CoM reductase (carboxylating); component II], EC
            1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and
            EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]}
            that is involved in epoxyalkane carboxylation in Xanthobacter sp.
            strain Py2.
REFERENCE   1  [PMID:10411892]
  AUTHORS   Allen JR, Clark DD, Krum JG, Ensign SA.
  TITLE     A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial
            pathway of aliphatic epoxide carboxylation.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 8432-7.
  ORGANISM  Xanthobacter sp.
REFERENCE   2  [PMID:11939797]
  AUTHORS   Krum JG, Ellsworth H, Sargeant RR, Rich G, Ensign SA.
  TITLE     Kinetic and microcalorimetric analysis of substrate and cofactor
            interactions in epoxyalkane:CoM transferase, a zinc-dependent
            epoxidase.
  JOURNAL   Biochemistry. 41 (2002) 5005-14.
  ORGANISM  Xanthobacter autotrophicus
REFERENCE   3  [PMID:12949106]
  AUTHORS   Coleman NV, Spain JC.
  TITLE     Epoxyalkane: coenzyme M transferase in the ethene and vinyl chloride
            biodegradation pathways of mycobacterium strain JS60.
  JOURNAL   J. Bacteriol. 185 (2003) 5536-45.
  ORGANISM  Mycobacterium sp.
GENES       XAU: Xaut_4865 Xaut_5047
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.23
            ExPASy - ENZYME nomenclature database: 4.4.1.23
            ExplorEnz - The Enzyme Database: 4.4.1.23
            ERGO genome analysis and discovery system: 4.4.1.23
            BRENDA, the Enzyme Database: 4.4.1.23
            CAS: 244301-07-3
///
ENTRY       EC 4.4.1.24                 Enzyme
NAME        sulfolactate sulfo-lyase;
            Suy;
            SuyAB;
            3-sulfolactate bisulfite-lyase
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     3-sulfolactate bisulfite-lyase (pyruvate-forming)
REACTION    3-sulfolactate = pyruvate + bisulfite [RN:R07633]
ALL_REAC    R07633
SUBSTRATE   3-sulfolactate [CPD:C16069]
PRODUCT     pyruvate [CPD:C00022];
            bisulfite [CPD:C11481]
COMMENT     Requires iron(II). This inducible enzyme from Paracoccus
            pantotrophus NKNCYSA forms part of the cysteate-degradation pathway.
            L-Cysteate [(2S)-2-amino-3-sulfopropanoate] serves as a sole source
            of carbon and energy for the aerobic growth of Paracoccus
            pantotrophus, as an electron acceptor for several sulfate-reducing
            bacteria, as an electron donor for some nitrate-reducing bacteria
            and as a substrate for a fermentation in a sulfate-reducing
            bacterium.
REFERENCE   1  [PMID:15758220]
  AUTHORS   Rein U, Gueta R, Denger K, Ruff J, Hollemeyer K, Cook AM.
  TITLE     Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a
            sulfate exporter in Paracoccus pantotrophus NKNCYSA.
  JOURNAL   Microbiology. 151 (2005) 737-47.
  ORGANISM  Paracoccus pantotrophus
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.24
            ExPASy - ENZYME nomenclature database: 4.4.1.24
            ExplorEnz - The Enzyme Database: 4.4.1.24
            ERGO genome analysis and discovery system: 4.4.1.24
            BRENDA, the Enzyme Database: 4.4.1.24
///
ENTRY       EC 4.4.1.25                 Enzyme
NAME        L-cysteate sulfo-lyase;
            L-cysteate sulfo-lyase (deaminating);
            CuyA
CLASS       Lyases;
            Carbon-sulfur lyases;
            Carbon-sulfur lyases (only sub-subclass identified to date)
SYSNAME     L-cysteate bisulfite-lyase (deaminating; pyruvate-forming)
REACTION    L-cysteate + H2O = pyruvate + bisulfite + NH3 [RN:R07634]
ALL_REAC    R07634
SUBSTRATE   L-cysteate [CPD:C00506];
            H2O [CPD:C00001]
PRODUCT     pyruvate [CPD:C00022];
            bisulfite [CPD:C11481];
            NH3 [CPD:C00014]
COMMENT     A pyridoxal-phosphate protein. D-Cysteine can also act as a
            substrate, but more slowly. It is converted into pyruvate, sulfide
            and NH3. This inducible enzyme from the marine bacterium
            Silicibacter pomeroyi DSS-3 forms part of the cysteate-degradation
            pathway.
REFERENCE   1  [PMID:16302849]
  AUTHORS   Denger K, Smits TH, Cook AM.
  TITLE     L-cysteate sulpho-lyase, a widespread pyridoxal 5'-phosphate-coupled
            desulphonative enzyme purified from Silicibacter pomeroyi DSS-3(T).
  JOURNAL   Biochem. J. 394 (2006) 657-64.
  ORGANISM  Silicibacter pomeroyi [GN:sil]
DBLINKS     IUBMB Enzyme Nomenclature: 4.4.1.25
            ExPASy - ENZYME nomenclature database: 4.4.1.25
            ExplorEnz - The Enzyme Database: 4.4.1.25
            ERGO genome analysis and discovery system: 4.4.1.25
            BRENDA, the Enzyme Database: 4.4.1.25
///
ENTRY       EC 4.5.1.1                  Enzyme
NAME        DDT-dehydrochlorinase;
            DDT-ase;
            1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane chloride-lyase;
            DDTase
CLASS       Lyases;
            Carbon-halide lyases;
            Carbon-halide lyases (only sub-subclass identified to date)
SYSNAME     1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane chloride-lyase
            [1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene-forming]
REACTION    1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane =
            1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene + chloride [RN:R04522]
ALL_REAC    R04522
SUBSTRATE   1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane [CPD:C04623]
PRODUCT     1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene [CPD:C04596];
            chloride [CPD:C00115]
REFERENCE   1  [PMID:13673024]
  AUTHORS   LIPKE H, KEARNS CW.
  TITLE     DDT dehydrochlorinase. I. Isolation, chemical properties, and
            spectrophotometric assay.
  JOURNAL   J. Biol. Chem. 234 (1959) 2123-8.
  ORGANISM  Musca domestica
REFERENCE   2  [PMID:13673025]
  AUTHORS   LIPKE H, KEARNS CW.
  TITLE     DDT dehydrochlorinase. II. Substrate and cofactor specificity.
  JOURNAL   J. Biol. Chem. 234 (1959) 2129-32.
REFERENCE   3
  AUTHORS   Moorefield, H.H.
  TITLE     Purification of DDT-dehydrochlorinase from resistant houseflies.
  JOURNAL   Contr. Boyce Thompson Inst. 18 (1956) 303-310.
PATHWAY     PATH: map00351  1,1,1-Trichloro-2,2-bis(4-chlorophenyl)ethane (DDT)
                            degradation
DBLINKS     IUBMB Enzyme Nomenclature: 4.5.1.1
            ExPASy - ENZYME nomenclature database: 4.5.1.1
            ExplorEnz - The Enzyme Database: 4.5.1.1
            ERGO genome analysis and discovery system: 4.5.1.1
            UM-BBD (Biocatalysis/Biodegradation Database): 4.5.1.1
            BRENDA, the Enzyme Database: 4.5.1.1
            CAS: 9031-20-3
///
ENTRY       EC 4.5.1.2                  Enzyme
NAME        3-chloro-D-alanine dehydrochlorinase;
            beta-chloro-D-alanine dehydrochlorinase;
            3-chloro-D-alanine chloride-lyase (deaminating)
CLASS       Lyases;
            Carbon-halide lyases;
            Carbon-halide lyases (only sub-subclass identified to date)
SYSNAME     3-chloro-D-alanine chloride-lyase (deaminating; pyruvate-forming)
REACTION    3-chloro-D-alanine + H2O = pyruvate + chloride + NH3 [RN:R01031]
ALL_REAC    R01031
SUBSTRATE   3-chloro-D-alanine [CPD:C02634];
            H2O [CPD:C00001]
PRODUCT     pyruvate [CPD:C00022];
            chloride [CPD:C00115];
            NH3 [CPD:C00014]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein. Also catalyses beta-replacement
            reactions, e.g. converts 3-chloro-D-alanine and H2S into D-cysteine
            and HCl.
REFERENCE   1  [PMID:3132906]
  AUTHORS   Nagasawa T, Ishii T, Yamada H.
  TITLE     Physiological comparison of D-cysteine desulfhydrase of Escherichia
            coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida
            CR 1-1.
  JOURNAL   Arch. Microbiol. 149 (1988) 413-6.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2  [PMID:6791643]
  AUTHORS   Yamada H, Nagasawa T, Ohkishi H, Kawakami B, Tani Y.
  TITLE     Synthesis of D-cysteine from 3-chloro-D-alanine and hydrogen sulfide
            by 3-chloro-D-alanine hydrogen chloride-lyase (deaminating) of
            Pseudomonas putida.
  JOURNAL   Biochem. Biophys. Res. Commun. 100 (1981) 1104-10.
  ORGANISM  Pseudomonas putida [GN:ppu]
DBLINKS     IUBMB Enzyme Nomenclature: 4.5.1.2
            ExPASy - ENZYME nomenclature database: 4.5.1.2
            ExplorEnz - The Enzyme Database: 4.5.1.2
            ERGO genome analysis and discovery system: 4.5.1.2
            BRENDA, the Enzyme Database: 4.5.1.2
            CAS: 78990-65-5
///
ENTRY       EC 4.5.1.3                  Enzyme
NAME        dichloromethane dehalogenase;
            dichloromethane chloride-lyase (chloride-hydrolysing)
CLASS       Lyases;
            Carbon-halide lyases;
            Carbon-halide lyases (only sub-subclass identified to date)
SYSNAME     dichloromethane chloride-lyase (adding H2O; chloride-hydrolysing;
            formaldehyde-forming)
REACTION    dichloromethane + H2O = formaldehyde + 2 chloride [RN:R00603]
ALL_REAC    R00603
SUBSTRATE   dichloromethane [CPD:C02271];
            H2O [CPD:C00001]
PRODUCT     formaldehyde [CPD:C00067];
            chloride [CPD:C00115]
COFACTOR    Glutathione [CPD:C00051]
COMMENT     Requires glutathione.
REFERENCE   1  [PMID:3988708]
  AUTHORS   Kohler-Staub D, Leisinger T.
  TITLE     Dichloromethane dehalogenase of Hyphomicrobium sp. strain DM2.
  JOURNAL   J. Bacteriol. 162 (1985) 676-81.
  ORGANISM  Hyphomicrobium sp.
DBLINKS     IUBMB Enzyme Nomenclature: 4.5.1.3
            ExPASy - ENZYME nomenclature database: 4.5.1.3
            ExplorEnz - The Enzyme Database: 4.5.1.3
            ERGO genome analysis and discovery system: 4.5.1.3
            UM-BBD (Biocatalysis/Biodegradation Database): 4.5.1.3
            BRENDA, the Enzyme Database: 4.5.1.3
            CAS: 97002-70-5
///
ENTRY       EC 4.5.1.4                  Enzyme
NAME        L-2-amino-4-chloropent-4-enoate dehydrochlorinase;
            L-2-amino-4-chloro-4-pentenoate dehalogenase;
            L-2-amino-4-chloropent-4-enoate chloride-lyase (deaminating)
CLASS       Lyases;
            Carbon-halide lyases;
            Carbon-halide lyases (only sub-subclass identified to date)
SYSNAME     L-2-amino-4-chloropent-4-enoate chloride-lyase (adding H2O;
            deaminating; 2-oxopent-4-enoate-forming)
REACTION    L-2-amino-4-chloropent-4-enoate + H2O = 2-oxopent-4-enoate +
            chloride + NH3 [RN:R02605]
ALL_REAC    R02605
SUBSTRATE   L-2-amino-4-chloropent-4-enoate [CPD:C04075];
            H2O [CPD:C00001]
PRODUCT     2-oxopent-4-enoate [CPD:C00596];
            chloride [CPD:C00115];
            NH3 [CPD:C00014]
REFERENCE   1
  AUTHORS   Moriguchi, M., Hoshino, S. and Hatanaka, S.-I.
  TITLE     Dehalogenation and deamination of l-2-amino-4-chloro-4-pentenoic
            acid by Proteus mirabilis.
  JOURNAL   Agric. Biol. Chem. 51 (1987) 3295.
  ORGANISM  Proteus mirabilis
DBLINKS     IUBMB Enzyme Nomenclature: 4.5.1.4
            ExPASy - ENZYME nomenclature database: 4.5.1.4
            ExplorEnz - The Enzyme Database: 4.5.1.4
            ERGO genome analysis and discovery system: 4.5.1.4
            BRENDA, the Enzyme Database: 4.5.1.4
            CAS: 113066-37-8
///
ENTRY       EC 4.5.1.5                  Enzyme
NAME        S-carboxymethylcysteine synthase;
            S-carboxymethyl-L-cysteine synthase
CLASS       Lyases;
            Carbon-halide lyases;
            Carbon-halide lyases (only sub-subclass identified to date)
SYSNAME     3-chloro-L-alanine chloride-lyase (adding thioglycolate;
            S-carboxymethyl-L-cysteine-forming)
REACTION    3-chloro-L-alanine + thioglycolate = S-carboxymethyl-L-cysteine +
            chloride [RN:R04003]
ALL_REAC    R04003
SUBSTRATE   3-chloro-L-alanine [CPD:C02635];
            thioglycolate [CPD:C02086]
PRODUCT     S-carboxymethyl-L-cysteine [CPD:C03727];
            chloride [CPD:C00115]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1
  AUTHORS   Kumagai, H., Suzuki, H., Shigematsu, H. and Tuchikura, T.
  TITLE     S-Carboxymethylcysteine synthase from Escherichia coli.
  JOURNAL   Agric. Biol. Chem. 53 (1989) 2481-2487.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 4.5.1.5
            ExPASy - ENZYME nomenclature database: 4.5.1.5
            ExplorEnz - The Enzyme Database: 4.5.1.5
            ERGO genome analysis and discovery system: 4.5.1.5
            BRENDA, the Enzyme Database: 4.5.1.5
            CAS: 124671-39-2
///
ENTRY       EC 4.5.1.-                  Enzyme
CLASS       Lyases;
            Carbon-halide lyases
REACTION    (1) 1,1-Dichloro-2,2-bis(4'-chlorophenyl)ethane <=>
            1-Chloro-2,2-bis(4'-chlorophenyl)ethylene + HCl [RN:R05384];
            (2) 1-Chloro-2,2-bis(4'-chlorophenyl)ethane <=>
            unsym-Bis(4'-chlorophenyl)ethylene + HCl [RN:R05385];
            (3) gamma-Hexachlorocyclohexane <=> gamma-Pentachlorocyclohexene +
            HCl [RN:R05386];
            (4) gamma-Pentachlorocyclohexene <=>
            1,3,4,6-Tetrachloro-1,4-cyclohexadiene + HCl [RN:R05387];
            (5) 5-Chloro-1,2,4-trihydroxybenzene <=> 2-Hydroxy-1,4-benzoquinone
            + HCl [RN:R05388]
SUBSTRATE   1,1-Dichloro-2,2-bis(4'-chlorophenyl)ethane [CPD:C06636];
            1-Chloro-2,2-bis(4'-chlorophenyl)ethane [CPD:C06638];
            gamma-Hexachlorocyclohexane [CPD:C06595];
            gamma-Pentachlorocyclohexene [CPD:C06596];
            5-Chloro-1,2,4-trihydroxybenzene [CPD:C07102]
PRODUCT     1-Chloro-2,2-bis(4'-chlorophenyl)ethylene [CPD:C06637];
            HCl [CPD:C01327];
            unsym-Bis(4'-chlorophenyl)ethylene [CPD:C06642];
            gamma-Pentachlorocyclohexene [CPD:C06596];
            1,3,4,6-Tetrachloro-1,4-cyclohexadiene [CPD:C06597];
            2-Hydroxy-1,4-benzoquinone [CPD:C07103]
///
ENTRY       EC 4.6.1.1                  Enzyme
NAME        adenylate cyclase;
            adenylylcyclase;
            adenyl cyclase;
            3',5'-cyclic AMP synthetase;
            ATP diphosphate-lyase (cyclizing)
CLASS       Lyases;
            Phosphorus-oxygen lyases;
            Phosphorus-oxygen lyases (only sub-subclass identified to date)
SYSNAME     ATP diphosphate-lyase (cyclizing; 3',5'-cyclic-AMP-forming)
REACTION    ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
ALL_REAC    R00089;
            (other) R00434
SUBSTRATE   ATP [CPD:C00002]
PRODUCT     3',5'-cyclic AMP [CPD:C00575];
            diphosphate [CPD:C00013]
COFACTOR    Pyruvate [CPD:C00022]
EFFECTOR    NAD+ [CPD:C00003]
COMMENT     Also acts on dATP to form 3',5'-cyclic dAMP. Requires pyruvate.
            Activated by NAD+ in the presence of EC 2.4.2.31 NAD(P)+---arginine
            ADP-ribosyltransferase.
REFERENCE   1  [PMID:4295782]
  AUTHORS   Hirata M, Hayaishi O.
  TITLE     Adenyl cyclase of Brevibacterium liquefaciens.
  JOURNAL   Biochim. Biophys. Acta. 149 (1967) 1-11.
  ORGANISM  Brevibacterium liquefaciens
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map04020  Calcium signaling pathway
            PATH: map04540  Gap junction
            PATH: map04720  Long-term potentiation
            PATH: map04740  Olfactory transduction
            PATH: map04742  Taste transduction
            PATH: map04912  GnRH signaling pathway
            PATH: map04914  Progesterone-mediated oocyte maturation
            PATH: map04916  Melanogenesis
ORTHOLOGY   KO: K01768  adenylate cyclase
            KO: K05851  adenylate cyclase, class 1
            KO: K05873  adenylate cyclase, class 2
            KO: K08041  adenylate cyclase 1 (brain)
            KO: K08042  adenylate cyclase 2 (brain)
            KO: K08043  adenylate cyclase 3
            KO: K08044  adenylate cyclase 4
            KO: K08045  adenylate cyclase 5
            KO: K08046  adenylate cyclase 6
            KO: K08047  adenylate cyclase 7
            KO: K08048  adenylate cyclase 8 (brain)
            KO: K08049  adenylate cyclase 9
GENES       HSA: 107(ADCY1) 108(ADCY2) 109(ADCY3) 111(ADCY5) 112(ADCY6)
                 113(ADCY7) 114(ADCY8) 115(ADCY9) 196883(ADCY4) 55811(SAC)
            PTR: 451866(ADCY6) 452819(ADCY4) 453869(ADCY9) 459070(ADCY3)
                 463392(ADCY1) 469570(LOC469570) 473278(ADCY7)
            MCC: 700574(LOC700574)
            MMU: 104110(Adcy4) 104111(Adcy3) 11512(Adcy6) 11513(Adcy7)
                 11514(Adcy8) 11515(Adcy9) 210044(Adcy2) 224129(Adcy5)
                 271639(Sacy) 432530(Adcy1)
            RNO: 25289(Adcy6) 29241(Adcy8) 305509(Adcy1_predicted)
                 54223(Adcy4) 59320(Adcy10) 64508(Adcy3) 64532(Adcy5)
                 81636(Adcy2) 84420(Adcy7)
            CFA: 403859(ADCY5) 477625(Adcy6) 478624(ADCY2) 480087(LOC480087)
                 480271(ADCY4) 482045(ADCY8) 482994(ADCY3) 487289(ADCY7)
                 490031(ADCY9) 607357(LOC607357)
            BTA: 281601(ADCY1) 281603(ADCY7) 535603(LOC535603)
            GGA: 395339(ADCY9) 395340(ADCY5) 415732(ADCY7) 420328(ADCY8)
                 420788(ADCY1) 420935(ADCY2)
            DRE: 564719(si:ch211-153j24.5)
            SPU: 574069(LOC574069) 575180(LOC575180) 593842(LOC593842)
            DME: Dmel_CG10255(Lap1) Dmel_CG10564(Ac78C) Dmel_CG1506(Ac3)
                 Dmel_CG17174 Dmel_CG17176 Dmel_CG17178 Dmel_CG5712
                 Dmel_CG5983(ACXC) Dmel_CG7978(Ac76E) Dmel_CG9210(Ac13E)
                 Dmel_CG9533(rut)
            CEL: F17C8.1(acy-1)
            SCE: YJL005W(CYR1)
            AGO: AGOS_AAL162C
            PIC: PICST_63917(CDC27) PICST_67440(CDC35) PICST_67704(SDS2)
            CAL: CaO19_3231(CaO19.3231)
            CGR: CAGL0D03168g
            SPO: SPBC19C7.03(cyr1)
            ANI: AN3913.2
            AFM: AFUA_6G08520
            AOR: AO090001000512
            CNE: CNG03670
            UMA: UM05232.1
            TET: TTHERM_00046210 TTHERM_00429720 TTHERM_00449540
                 TTHERM_00666450 TTHERM_00977610 TTHERM_01156830
            TBR: Tb09.244.2380 Tb10.389.0430 Tb10.61.0060 Tb10.61.0280
                 Tb10.70.5260 Tb11.01.5310 Tb11.01.8820 Tb11.02.3740
                 Tb11.03.0990 Tb11.27.0001 Tb927.4.3750 Tb927.4.3860
                 Tb927.4.3870 Tb927.4.3880 Tb927.4.4410 Tb927.4.4430
                 Tb927.4.4440 Tb927.4.4450 Tb927.4.4460 Tb927.4.4470
                 Tb927.5.1450 Tb927.5.320 Tb927.5.330 Tb927.5.4540 Tb927.5.4550
                 Tb927.5.650 Tb927.6.170 Tb927.6.180 Tb927.6.190 Tb927.6.200
                 Tb927.6.280 Tb927.6.300 Tb927.6.310 Tb927.6.330 Tb927.6.430
                 Tb927.6.760 Tb927.6.770 Tb927.6.780 Tb927.6.790 Tb927.6.800
                 Tb927.7.6040 Tb927.7.6050 Tb927.7.6060 Tb927.7.6070
                 Tb927.7.6080 Tb927.7.7470 Tb927.7.7520 Tb927.7.7530
                 Tb927.8.7590 Tb927.8.7860 Tb927.8.7870 Tb927.8.7890
                 Tb927.8.7900 Tb927.8.7920 Tb927.8.7930 Tb927.8.7940
                 Tb927.8.8360 Tb927.8.8360f
            TCR: 506355.20
            LMA: LmjF17.0190 LmjF17.0237
            EHI: 224.t00010 68.t00029
            ECO: b3806(cyaA)
            ECJ: JW3778(cyaA)
            ECE: Z5322(cyaA)
            ECS: ECs4736
            ECC: c4725(cyaA)
            ECI: UTI89_C2847(fdx) UTI89_C3094(fhlA) UTI89_C4365(cyaA)
                 UTI89_C4926(hlyA)
            ECP: ECP_3999
            ECV: APECO1_2672(cyaA)
            ECW: EcE24377A_3517 EcE24377A_4321(cyaA)
            ECX: EcHS_A3231 EcHS_A4026(cyaA)
            STY: STY3620(cyaA)
            STT: t3358(cyaA)
            SPT: SPA3780(cyaA)
            SEC: SC3840(cyaA)
            STM: STM3939(cyaA)
            YPE: YPO1178(cyaB) YPO3848(cyaA)
            YPK: y0382(cyaA) y3011
            YPM: YP_0959(cyaB) YP_3199(cyaA)
            YPA: YPA_0174 YPA_0889
            YPN: YPN_0116 YPN_2799
            YPP: YPDSF_3465
            YPS: YPTB0185(cyaA) YPTB1219(cyaB)
            YPI: YpsIP31758_0201(cyaA)
            YEN: YE0189(cya)
            SFL: SF3878(cyaA)
            SFX: S3878(cyaA)
            SFV: SFV_3696(cyaA)
            SSN: SSON_3978(cyaA)
            SBO: SBO_3817(cyaA)
            SDY: SDY_3940(cyaA)
            ECA: ECA2795(cyaB) ECA4187(cyaA)
            PLU: plu4643(cyaA)
            SGL: SG2347
            ENT: Ent638_3986
            SPE: Spro_0179
            HIN: HI0604(cyaA)
            HIT: NTHI0859(cya)
            HIP: CGSHiEE_01995(cyaA)
            HIQ: CGSHiGG_06955(cyaA)
            HDU: HD0613(cyaA)
            HSO: HS_0043(cyaA)
            PMU: PM1811(cyaA)
            MSU: MS0277(cyaA)
            APL: APL_1054(cyaA)
            ASU: Asuc_0361
            XFA: XF2357
            XFT: PD1384
            XCC: XCC1279
            XCB: XC_2962
            XCV: XCV1382
            XAC: XAC1330
            XOO: XOO1860
            XOM: XOO_1756(XOO1756)
            VCH: VC0122
            VCO: VC0395_A2397(cyaA)
            VVU: VV1_1123
            VVY: VV0083
            VPA: VP1760 VP2987
            VFI: VF0067
            PPR: PBPRA3526(cyaA) PBPRB0776(cyaB)
            PAE: PA5272(cyaA)
            PAU: PA14_69610(cyaA)
            PPU: PP_5222(cyaA)
            PPF: Pput_5131
            PST: PSPTO_0230(cyaA)
            PSB: Psyr_0177
            PSP: PSPPH_5013(cyaA)
            PFL: PFL_6008(cyaA)
            PFO: Pfl_5493
            PEN: PSEEN5359(cyaA)
            PMY: Pmen_0273
            SON: SO_3778 SO_4312
            SFR: Sfri_0441 Sfri_1665
            SAZ: Sama_3253
            SBM: Shew185_3977
            SLO: Shew_0319
            SPC: Sputcn32_3586
            SSE: Ssed_4132
            SPL: Spea_0374
            SHE: Shewmr4_0389 Shewmr4_3125
            SHM: Shewmr7_0842 Shewmr7_3637
            SHN: Shewana3_0387 Shewana3_0814 Shewana3_3045
            SHW: Sputw3181_3725
            SDE: Sde_3600
            PIN: Ping_0061
            MAQ: Maqu_0492
            CBD: COXBU7E912_1170(cyaA)
            LPN: lpg0674 lpg1130(cyaA4) lpg1322(cyaA) lpg1490(cyaA)
                 lpg1739(gidA)
            LPF: lpl0710 lpl1135(ladC) lpl1276 lpl1703
            LPP: lpp0730 lpp1131(ladC) lpp1277 lpp1446 lpp1704
            TCX: Tcr_1305
            NOC: Noc_1062
            AEH: Mlg_1325
            HCH: HCH_00295 HCH_02328
            ABO: ABO_0435 ABO_0885
            AHA: AHA_0470(cyaA) AHA_2412 AHA_3770
            REU: Reut_C6414
            REH: H16_A0674 H16_A0827(cycR1) H16_A1791 H16_A1809
                 H16_B0376(cycR2)
            BXE: Bxe_B0811
            BUR: Bcep18194_B2092 Bcep18194_C6723
            BPM: BURPS1710b_0923
            BPE: BP0760(cyaA)
            BPA: BPP0321(cyaA)
            BBR: BB0324(cyaA)
            POL: Bpro_0721
            NEU: NE1299
            AZO: azo1292
            DAR: Daro_3699
            TBD: Tbd_0983
            MFA: Mfla_2129
            WSU: WS1633(gidA)
            TDN: Tmden_0929
            ABU: Abu_0928(cyaA)
            SUN: SUN_1191
            DVU: DVU1600
            DDE: Dde_2101
            LIP: LI1110
            BBA: Bd0081(cyaB) Bd1116(cyaA) Bd2640(cyaK) Bd2671(cyaA10)
                 Bd2833(hik)
            MXA: MXAN_0639 MXAN_0873 MXAN_2723 MXAN_7396
            SAT: SYN_01481 SYN_02853
            SFU: Sfum_4085
            SME: SMa1046 SMa1103 SMa1583(cyaF5) SMb20300(cyaF7)
                 SMb20539(cyaF6) SMb20707(cyaG2) SMb20776(cyaK) SMc00339(cyaA)
                 SMc00621(cyaB) SMc01818(cyaC) SMc02176(cyaD1) SMc02285(cyaE)
                 SMc03099(cyaF1) SMc03937(cyaG1) SMc03985(cyaF2)
                 SMc04307(cyaD2)
            ATU: Atu1149(cya) Atu2580(cyaA) Atu4013(cyaA)
            ATC: AGR_C_2127 AGR_C_4673 AGR_L_1679
            RET: RHE_CH01494(cyaB) RHE_CH02138 RHE_CH02493(ypch00836)
                 RHE_CH02684(ypch00918) RHE_CH02696(cyaK) RHE_CH03586(cyaFch2)
                 RHE_CH03605(cyaD) RHE_CH03606 RHE_CH03700(cyaG1)
                 RHE_CH03714(cyaG2) RHE_PE00043(cyaA) RHE_PE00049(cyaCe)
                 RHE_PE00170 RHE_PE00177
            RLE: RL0458 RL1127 RL1187(cya3) RL1224(cya1) RL1331(cyaA)
                 RL1602(cya) RL2262(cya3) RL2429(cya) RL2441 RL2506(cya)
                 RL2737(ohr) RL2834(cya) RL2873(cya3) RL2951(cya) RL2953
                 RL3062(cya3) RL3166 RL3271(cya3) RL4106(cya) RL4128(cyaA)
                 RL4129(cyaB1) RL4163 RL4164 RL4236(cyaB) RL4257(cyaA)
                 pRL110055 pRL110066 pRL110185
            BJA: bll5046 bll5647 bll7664 bll7923 blr2264 blr2632 blr6052
                 blr7256
            BRA: BRADO0421 BRADO0901 BRADO1430(cyaA) BRADO2154 BRADO2872
                 BRADO2991 BRADO4443 BRADO6087 BRADO6170 BRADO6220 BRADO6221
                 BRADO6971 BRADO7095
            BBT: BBta_0410 BBta_0561 BBta_1383 BBta_1384 BBta_2471 BBta_4661
                 BBta_5176 BBta_5302 BBta_6677(cyaA) BBta_7152
            RPA: RPA1202 RPA1582(cyaA) RPA2291
            RPB: RPB_1213 RPB_3153 RPB_3665 RPB_3943
            RPD: RPD_1795 RPD_3704
            RPE: RPE_0894 RPE_3000 RPE_4376 RPE_4397
            NWI: Nwi_1740 Nwi_3040
            NHA: Nham_2169
            SIL: SPO0688 SPO0901 SPO3450
            SIT: TM1040_0613 TM1040_2619 TM1040_2648
            JAN: Jann_1674
            RDE: RD1_0501 RD1_2687(cyaA)
            GOX: GOX2023
            RRU: Rru_A1071
            MAG: amb1226 amb2235 amb3040 amb3618
            MGM: Mmc1_0642 Mmc1_1112 Mmc1_1205 Mmc1_1858 Mmc1_3697
            ABA: Acid345_1344 Acid345_2026
            SUS: Acid_1195
            CPF: CPF_1559
            CPR: CPR_1352
            CTC: CTC00338
            CNO: NT01CX_1378
            MTU: Rv1264 Rv1318c Rv1319c Rv1320c Rv1625c(cya)
            MTC: MT1359 MT1360 MT1361 MT1362 MT1661
            MBO: Mb1295 Mb1352c Mb1353c Mb1354c Mb1651c(cya)
            MBB: BCG_1323 BCG_1379c BCG_1380c BCG_1381c BCG_1663c(cya)
            MPA: MAP1318c MAP2440
            MAV: MAV_3162
            MSM: MSMEG_0228 MSMEG_3780 MSMEG_4279 MSMEG_4924 MSMEG_5018
            MVA: Mvan_2839
            MMC: Mmcs_3025 Mmcs_3868 Mmcs_3949 Mmcs_4795
            MKM: Mkms_3084
            MJL: Mjls_3041
            CGL: NCgl0306(cgl0311)
            CGB: cg0375(cyaB)
            CJK: jk1952(cya)
            NFA: nfa6840
            RHA: RHA1_ro01460 RHA1_ro01942 RHA1_ro02184 RHA1_ro05084
                 RHA1_ro05168
            SCO: SCO4928(cya)
            SMA: SAV3329(cyaA)
            TFU: Tfu_2552
            FAL: FRAAL0057 FRAAL6555
            SEN: SACE_1989(cya) SACE_3984
            RBA: RB4958 RB5744(cya) RB6328 RB6945(cyaA) RB7781(cyaA)
            TPA: TP0485
            TDE: TDE1986
            LIL: LA0027(cyaA1) LA0288(cyaA2) LA0565(cyaA3) LA0993(cyaA4)
                 LA1070(cyaA5) LA1184(cyaA6) LA1419(cyaA7) LA2536(cyaA8)
                 LA2643(cyaA9) LA2834(cyaA10) LA2968(cyaA11) LA3041(cyaA12)
                 LA3234(cyaA13) LA3286(cyaA14) LA3843(cyaA15) LA4008(cyaA16)
                 LB094(cyaA17) LB118(cyaA18)
            LIC: LIC10862 LIC11095 LIC11198 LIC11343 LIC11437 LIC12506
                 LIC12598 LIC12670(cyaA) LIC13004 LIC13072 LIC13201 LIC20075
                 LIC20094
            SYN: sll1161(cya3) slr1991(cya1)
            SYC: syc0865_c(cya2)
            SYF: Synpcc7942_0663
            SYD: Syncc9605_2515
            SYG: sync_2745
            SYX: SynWH7803_2394(cya1)
            CYA: CYA_2405
            CYB: CYB_0179 CYB_2200
            TEL: tll2280 tll2410
            ANA: all0743(cyaD) all1118(cyaA) alr2266(cyaB1)
            AVA: Ava_0091 Ava_1972 Ava_2239 Ava_3735 Ava_4645 Ava_4698
            PMT: PMT2146
            GFO: GFO_3390
            MJA: MJ0240
            MMP: MMP1064
            MAC: MA4044(cyaB)
            MBA: Mbar_A0548
            MMA: MM_0868
            MBU: Mbur_1935
            MHU: Mhun_1167
            MTH: MTH1629
            MST: Msp_1098
            MSI: Msm_0721
            MKA: MK0871(cyaB)
            AFU: AF1988
            HMA: rrnAC1232(cytH)
            HWA: HQ2585A(cyaB)
            NPH: NP3092A(cyaB)
            PHO: PH1819
            PAB: PAB2098
            PFU: PF1859
            TKO: TK1179
            RCI: LRC431(cyaB)
            SSO: SSO0253(cyaB)
            STO: ST0300
            SAI: Saci_0718
            PAI: PAE0832
STRUCTURES  PDB: 1AB8  1AZS  1CJK  1CJT  1CJU  1CJV  1CS4  1CUL  1FX2  1FX4  
                 1K8T  1K90  1K93  1LVC  1PK0  1S26  1SK6  1TL7  1U0H  1WC0  
                 1WC1  1WC3  1WC4  1WC5  1WC6  1XFU  1XFV  1XFW  1XFX  1XFY  
                 1XFZ  1Y0V  1Y10  1Y11  1YBT  1YBU  1YK9  1YKD  1YRT  1YRU  
                 1ZOT  2BW7  2COL  2EV1  2EV2  2EV3  2EV4  2FJT  2GVD  2GVZ  
DBLINKS     IUBMB Enzyme Nomenclature: 4.6.1.1
            ExPASy - ENZYME nomenclature database: 4.6.1.1
            ExplorEnz - The Enzyme Database: 4.6.1.1
            ERGO genome analysis and discovery system: 4.6.1.1
            BRENDA, the Enzyme Database: 4.6.1.1
            CAS: 9012-42-4
///
ENTRY       EC 4.6.1.2                  Enzyme
NAME        guanylate cyclase;
            guanylyl cyclase;
            guanyl cyclase;
            GTP diphosphate-lyase (cyclizing)
CLASS       Lyases;
            Phosphorus-oxygen lyases;
            Phosphorus-oxygen lyases (only sub-subclass identified to date)
SYSNAME     GTP diphosphate-lyase (cyclizing; 3',5'-cyclic-GMP-forming)
REACTION    GTP = 3',5'-cyclic GMP + diphosphate [RN:R00434]
ALL_REAC    R00434
SUBSTRATE   GTP [CPD:C00044]
PRODUCT     3',5'-cyclic GMP [CPD:C00942];
            diphosphate [CPD:C00013]
COMMENT     Also acts on ITP and dGTP.
REFERENCE   1  [PMID:235291]
  AUTHORS   Garbers DL, Suddath JL, Hardman JG.
  TITLE     Enzymatic formation of inosine 3',5'-monophosphate and of
            2'-deoxyguanosine 3',5'-monophosphate. Inosinate and deoxyguanylate
            cyclase activity.
  JOURNAL   Biochim. Biophys. Acta. 377 (1975) 174-85.
  ORGANISM  rat [GN:rno], sea urchin
REFERENCE   2  [PMID:4982201]
  AUTHORS   Hardman JG, Sutherland EW.
  TITLE     Guanyl cyclase, an enzyme catalyzing the formation of guanosine
            3',5'-monophosphate from guanosine trihosphate.
  JOURNAL   J. Biol. Chem. 244 (1969) 6363-70.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map04540  Gap junction
            PATH: map04730  Long-term depression
ORTHOLOGY   KO: K01769  guanylate cyclase
GENES       HSA: 2977(GUCY1A2) 2982(GUCY1A3) 2983(GUCY1B3) 2984(GUCY2C)
                 2986(GUCY2F) 3000(GUCY2D) 4881(NPR1) 4882(NPR2)
            PTR: 452727(GUCY1B2) 466769(GUCY1A2) 473375(GUCY2C)
            MMU: 14919(Gucy2e) 18160(Npr1) 230103(Npr2) 234889(Gucy1a2)
                 239134(Gucy1b2) 54195(Gucy1b3) 60596(Gucy1a3)
            RNO: 116556(Gucy2f) 116564(Npr2) 24603(Npr1) 25202(Gucy1b3)
                 25206(Gucy1b2) 25711(Gucy2c) 497757(Gucy1a3) 66012(Gucy1a2)
                 79222(Gucy2e)
            CFA: 403863(GUCY2D) 474762(NPR2) 479455(GUCY1A2) 481016(GUCY2F)
                 482663(GUCY1A3) 485435(LOC485435) 486671(GUCY2C) 490455(NPR1)
                 553102(GUCY1B3)
            BTA: 281216(GUCY1A3) 281357(NPR2) 282244(GUCY2C) 282245(GUCY2D)
                 282246(GUCY2F) 282433(GUCY1B3)
            SSC: 397193(GUCY2C) 444999(GUCY1B3)
            GGA: 417968(GUCY2C) 419089(GUCY2F) 422407(GUCY1A3) 422408(GUCY1B3)
                 429128(LOC429128) 771678(GUCY1A2)
            XLA: 432281(MGC82401)
            SPU: 373321(LOC373321) 576434(LOC576434) 579464(LOC579464)
            DME: Dmel_CG1470(Gycbeta100B) Dmel_CG14885(Gyc-89Da)
                 Dmel_CG14886(Gyc-89Db) Dmel_CG1912(Gycalpha99B) Dmel_CG31183
                 Dmel_CG33114(Gyc32E)
            CEL: AH6.1(gcy-1) B0024.6(gcy-6) C06A12.4(gcy-27) C06B3.8(gcy-32)
                 C17F4.6(gcy-19) C30G4.3(gcy-11) C46E1.2(gcy-36) C49H3.1(gcy-8)
                 F08B1.2(gcy-12) F21H7.9(gcy-20) F22E5.3(gcy-21)
                 F23H12.6(gcy-13) M04G12.3(gcy-34) R01E6.1(odr-1) R134.1(gcy-3)
                 R134.2(gcy-2) T01A4.1(gcy-28) T03D8.5(gcy-22) T04D3.4(gcy-35)
                 T26C12.4(gcy-23) W03F11.2(gcy-17) Y105C5B.2(gcy-25)
                 ZC239.7(gcy-15) ZC412.2(gcy-14) ZK455.2(gcy-9) ZK896.8(gcy-18)
                 ZK970.5(gcy-4) ZK970.6(gcy-5)
            PFA: MAL13P1.301 PF11_0395
            TAN: TA15475
            PAT: Patl_2382
            MFA: Mfla_1571
            SMD: Smed_3762
            BRA: BRADO2991
            BBT: BBta_5176
            JAN: Jann_1561
            RDE: RD1_2531
            MGI: Mflv_3576
            SYN: sll0646(cya2)
            TER: Tery_2417 Tery_3993
STRUCTURES  PDB: 1DP4  1JBA  
DBLINKS     IUBMB Enzyme Nomenclature: 4.6.1.2
            ExPASy - ENZYME nomenclature database: 4.6.1.2
            ExplorEnz - The Enzyme Database: 4.6.1.2
            ERGO genome analysis and discovery system: 4.6.1.2
            BRENDA, the Enzyme Database: 4.6.1.2
            CAS: 9054-75-5
///
ENTRY       EC 4.6.1.3        Obsolete  Enzyme
NAME        Transferred to 4.2.3.4
CLASS       Lyases;
            Phosphorus-oxygen lyases;
            Phosphorus-oxygen lyases (only sub-subclass identified to date)
COMMENT     Transferred entry: now EC 4.2.3.4 3-dehydroquinate synthase (EC
            4.6.1.3 created 1978, deleted 2000)
STRUCTURES  PDB: 1DQS  
DBLINKS     IUBMB Enzyme Nomenclature: 4.6.1.3
            ExPASy - ENZYME nomenclature database: 4.6.1.3
            ExplorEnz - The Enzyme Database: 4.6.1.3
            ERGO genome analysis and discovery system: 4.6.1.3
            BRENDA, the Enzyme Database: 4.6.1.3
///
ENTRY       EC 4.6.1.4        Obsolete  Enzyme
NAME        Transferred to 4.2.3.5
CLASS       Lyases;
            Phosphorus-oxygen lyases;
            Phosphorus-oxygen lyases (only sub-subclass identified to date)
COMMENT     Transferred entry: now EC 4.2.3.5 chorismate synthase (EC 4.6.1.4
            created 1978, modified 1983, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 4.6.1.4
            ExPASy - ENZYME nomenclature database: 4.6.1.4
            ExplorEnz - The Enzyme Database: 4.6.1.4
            ERGO genome analysis and discovery system: 4.6.1.4
            BRENDA, the Enzyme Database: 4.6.1.4
///
ENTRY       EC 4.6.1.5        Obsolete  Enzyme
NAME        Transferred to 4.2.3.7
CLASS       Lyases;
            Phosphorus-oxygen lyases;
            Phosphorus-oxygen lyases (only sub-subclass identified to date)
COMMENT     Transferred entry: now EC 4.2.3.7 pentalenene synthase (EC 4.6.1.5
            created 1989, deleted 2000)
STRUCTURES  PDB: 1HM4  1HM7  1PS1  
DBLINKS     IUBMB Enzyme Nomenclature: 4.6.1.5
            ExPASy - ENZYME nomenclature database: 4.6.1.5
            ExplorEnz - The Enzyme Database: 4.6.1.5
            ERGO genome analysis and discovery system: 4.6.1.5
            BRENDA, the Enzyme Database: 4.6.1.5
///
ENTRY       EC 4.6.1.6                  Enzyme
NAME        cytidylate cyclase;
            3',5'-cyclic-CMP synthase;
            cytidylyl cyclase;
            cytidyl cyclase;
            CTP diphosphate-lyase (cyclizing)
CLASS       Lyases;
            Phosphorus-oxygen lyases;
            Phosphorus-oxygen lyases (only sub-subclass identified to date)
SYSNAME     CTP diphosphate-lyase (cyclizing; 3',5'-cyclic-CMP-forming)
REACTION    CTP = 3',5'-cyclic CMP + diphosphate [RN:R00574]
ALL_REAC    R00574
SUBSTRATE   CTP [CPD:C00063]
PRODUCT     3',5'-cyclic CMP [CPD:C00941];
            diphosphate [CPD:C00013]
REFERENCE   1  [PMID:23778]
  AUTHORS   Cech SY, Ignarro LJ.
  TITLE     Cytidine 3',5'-monophosphate (cyclic CMP) formation by homogenates
            of mouse liver.
  JOURNAL   Biochem. Biophys. Res. Commun. 80 (1978) 119-25.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2
  AUTHORS   Newton, R.P., Salih, S.G., Hakeem, N.A., Kingston, E.E. and Beynon,
            J.H.
  TITLE     3',5'-Cyclic UMP, -cyclic IMP, -cyclic TMP and related enzymes in
            mammalian-tissues.
  JOURNAL   Biochem. Soc. Trans. 13 (1985) 1134-1135.
DBLINKS     IUBMB Enzyme Nomenclature: 4.6.1.6
            ExPASy - ENZYME nomenclature database: 4.6.1.6
            ExplorEnz - The Enzyme Database: 4.6.1.6
            ERGO genome analysis and discovery system: 4.6.1.6
            BRENDA, the Enzyme Database: 4.6.1.6
            CAS: 65357-82-6
///
ENTRY       EC 4.6.1.7        Obsolete  Enzyme
NAME        Transferred to 4.2.3.8
CLASS       Lyases;
            Phosphorus-oxygen lyases;
            Phosphorus-oxygen lyases (only sub-subclass identified to date)
COMMENT     Transferred entry: now EC 4.2.3.8, casbene synthase (EC 4.6.1.7
            created 1989, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 4.6.1.7
            ExPASy - ENZYME nomenclature database: 4.6.1.7
            ExplorEnz - The Enzyme Database: 4.6.1.7
            ERGO genome analysis and discovery system: 4.6.1.7
            BRENDA, the Enzyme Database: 4.6.1.7
///
ENTRY       EC 4.6.1.8        Obsolete  Enzyme
NAME        Transferred to 4.2.3.10
CLASS       Lyases;
            Phosphorus-oxygen lyases;
            Phosphorus-oxygen lyases (only sub-subclass identified to date)
COMMENT     Transferred entry: now EC 4.2.3.10, (-)-endo-fenchol synthase (EC
            4.6.1.8 created 1992, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 4.6.1.8
            ExPASy - ENZYME nomenclature database: 4.6.1.8
            ExplorEnz - The Enzyme Database: 4.6.1.8
            ERGO genome analysis and discovery system: 4.6.1.8
            BRENDA, the Enzyme Database: 4.6.1.8
///
ENTRY       EC 4.6.1.9        Obsolete  Enzyme
NAME        Transferred to 4.2.3.11
CLASS       Lyases;
            Phosphorus-oxygen lyases;
            Phosphorus-oxygen lyases (only sub-subclass identified to date)
COMMENT     Transferred entry: now EC 4.2.3.11 sabinene-hydrate synthase (EC
            4.6.1.9 created 1992, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 4.6.1.9
            ExPASy - ENZYME nomenclature database: 4.6.1.9
            ExplorEnz - The Enzyme Database: 4.6.1.9
            ERGO genome analysis and discovery system: 4.6.1.9
            BRENDA, the Enzyme Database: 4.6.1.9
///
ENTRY       EC 4.6.1.10       Obsolete  Enzyme
NAME        Transferred to 4.2.3.12
CLASS       Lyases;
            Phosphorus-oxygen lyases;
            Phosphorus-oxygen lyases (only sub-subclass identified to date)
COMMENT     Transferred entry: now EC 4.2.3.12 6-pyruvoyltetrahydropterin
            synthase (EC 4.6.1.10 created 1999, deleted 2000)
STRUCTURES  PDB: 1B66  1B6Z  1GTQ  
DBLINKS     IUBMB Enzyme Nomenclature: 4.6.1.10
            ExPASy - ENZYME nomenclature database: 4.6.1.10
            ExplorEnz - The Enzyme Database: 4.6.1.10
            ERGO genome analysis and discovery system: 4.6.1.10
            BRENDA, the Enzyme Database: 4.6.1.10
///
ENTRY       EC 4.6.1.11       Obsolete  Enzyme
NAME        Transferred to 4.2.3.13
CLASS       Lyases;
            Phosphorus-oxygen lyases;
            Phosphorus-oxygen lyases (only sub-subclass identified to date)
COMMENT     Transferred entry: now EC 4.2.3.13, (+)-delta-cadinene synthase (EC
            4.6.1.11 created 1999, deleted 2000)
DBLINKS     IUBMB Enzyme Nomenclature: 4.6.1.11
            ExPASy - ENZYME nomenclature database: 4.6.1.11
            ExplorEnz - The Enzyme Database: 4.6.1.11
            ERGO genome analysis and discovery system: 4.6.1.11
            BRENDA, the Enzyme Database: 4.6.1.11
///
ENTRY       EC 4.6.1.12                 Enzyme
NAME        2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase;
            MECDP-synthase;
            2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
            CMP-lyase (cyclizing)
CLASS       Lyases;
            Phosphorus-oxygen lyases;
            Phosphorus-oxygen lyases (only sub-subclass identified to date)
SYSNAME     2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
            CMP-lyase (cyclizing; 2-C-methyl-D-erythritol
            2,4-cyclodiphosphate-forming)
REACTION    2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol =
            2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP [RN:R05637]
ALL_REAC    R05637
SUBSTRATE   2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
            [CPD:C11436]
PRODUCT     2-C-methyl-D-erythritol 2,4-cyclodiphosphate [CPD:C11453];
            CMP [CPD:C00055]
COMMENT     The enzyme from Escherichia coli requires Mg2+ or Mn2+. Forms part
            of an alternative nonmevalonate pathway for terpenoid biosynthesis
            (for diagram, click here).
REFERENCE   1  [PMID:10694574]
  AUTHORS   Herz S, Wungsintaweekul J, Schuhr CA, Hecht S, Luttgen H, Sagner S,
            Fellermeier M, Eisenreich W, Zenk MH, Bacher A, Rohdich F.
  TITLE     Biosynthesis of terpenoids: YgbB protein converts
            4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate to
            2C-methyl-D-erythritol 2,4-cyclodiphosphate.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 2486-90.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Takagi, M., Kuzuyama, T., Kaneda, K., Watanabe, H., Dairi, T. and
            Seto, H.
  TITLE     Studies on the nonmevalonate pathway: Formation of
            2-C-methyl-D-erythritol 2,4-cyclodiphosphate from
            2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol.
  JOURNAL   Tetrahedron Lett. 41 (2000) 3395-3398.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K01770  2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
GENES       OSA: 4330320
            PFA: PFB0420w
            TAN: TA04155
            TPV: TP03_0365
            TET: TTHERM_01003920
            ECO: b2746(ispF)
            ECJ: JW2716(ispF)
            ECE: Z4054(ygbB)
            ECS: ECs3600
            ECC: c3313(ispF)
            ECI: UTI89_C3117(ygbB)
            ECP: ECP_2728
            ECV: APECO1_3777(ispF)
            ECW: EcE24377A_3047(ispF)
            ECX: EcHS_A2884
            STY: STY3054(ygbB)
            STT: t2830(ygbB)
            SPT: SPA2785(ygbB)
            SEC: SC2861(ispF)
            STM: STM2929(ispF)
            YPE: YPO3360(ispF)
            YPK: y0829
            YPM: YP_0327(ispF)
            YPA: YPA_2783
            YPN: YPN_0733
            YPP: YPDSF_3000
            YPS: YPTB0771(ispF)
            YPI: YpsIP31758_3298(ispF)
            YEN: YE0770(b2746)
            SFL: SF2769(ygbB)
            SFX: S2962(ygbB)
            SFV: SFV_2752(ygbB)
            SSN: SSON_2894(ygbB)
            SBO: SBO_2774(ygbB)
            SDY: SDY_2945(ygbB)
            ECA: ECA3534(ispF)
            PLU: plu0714(ispF)
            BUC: BU419(ygbB)
            BAS: BUsg404(ygbB)
            WBR: WGLp531(ygbB)
            SGL: SG0527
            ENT: Ent638_3217
            KPN: KPN_03108(ispF)
            SPE: Spro_0827
            BPN: BPEN_172(ispF)
            HIN: HI0671(ispF)
            HIT: NTHI0793(ispF)
            HIP: CGSHiEE_08820(ispF)
            HIQ: CGSHiGG_06630(ispF)
            HDU: HD1328(ispF)
            HSO: HS_1498(ispF)
            PMU: PM1609
            MSU: MS2274(ispF)
            APL: APL_0803(ispF)
            ASU: Asuc_2031
            XFA: XF1294
            XFT: PD0546(ispF)
            XCC: XCC1703(ispF)
            XCB: XC_2528
            XCV: XCV1755(ispF)
            XAC: XAC1722(ispF)
            XOO: XOO2960(ispF)
            XOM: XOO_2811(XOO2811)
            VCH: VC0529
            VCO: VC0395_A0057(ispF)
            VVU: VV1_1583
            VVY: VV2814
            VPA: VP2558
            VFI: VF2072(ispF)
            PPR: PBPRA3076
            PAE: PA3627
            PAU: PA14_17420(ispF)
            PAP: PSPA7_1512(ispF)
            PPU: PP_1618
            PPF: Pput_4159
            PST: PSPTO_1560(ispF)
            PSB: Psyr_1369(ispF)
            PSP: PSPPH_3814(ispF)
            PFL: PFL_1202(ispF)
            PFO: Pfl_1127
            PEN: PSEEN4194(ispF)
            PMY: Pmen_3026
            PAR: Psyc_1243(ispF)
            PCR: Pcryo_1149
            PRW: PsycPRwf_0962
            ACI: ACIAD1996(ispF)
            SON: SO_3437(ispF)
            SDN: Sden_1199
            SFR: Sfri_1055
            SAZ: Sama_1039
            SBL: Sbal_3124
            SBM: Shew185_3133
            SLO: Shew_1208
            SPC: Sputcn32_2754
            SSE: Ssed_1293
            SPL: Spea_1188
            SHE: Shewmr4_1118
            SHM: Shewmr7_1189
            SHN: Shewana3_1119
            SHW: Sputw3181_1258
            ILO: IL0751(ispF)
            CPS: CPS_1073(ispF)
            PHA: PSHAa0685(ispF)
            PAT: Patl_3858
            SDE: Sde_1248
            PIN: Ping_0673
            MAQ: Maqu_0924
            MCA: MCA2518(ispF)
            FTU: FTT1128(ispF)
            FTF: FTF1128(ispF)
            FTW: FTW_1161(ispF)
            FTL: FTL_0833
            FTH: FTH_0823(ispF)
            FTA: FTA_0882(ispF)
            FTN: FTN_1110(ispF)
            NOC: Noc_0855
            AEH: Mlg_1836
            HHA: Hhal_1434
            HCH: HCH_01870(ispF)
            CSA: Csal_2637
            ABO: ABO_1167(ispF)
            MMW: Mmwyl1_1302
            AHA: AHA_0824(ispF)
            BCI: BCI_0210(ispF)
            RMA: Rmag_0756
            VOK: COSY_0698(ispF)
            NME: NMB1512
            NMA: NMA1712
            NGO: NGO0971
            CVI: CV_1259(ispF)
            RSO: RSc1644(RS04019)
            REU: Reut_A1362
            RME: Rmet_1953
            BMA: BMA1489(ispF)
            BMV: BMASAVP1_A1986(ispF)
            BML: BMA10299_A3320(ispF)
            BMN: BMA10247_1258(ispF)
            BXE: Bxe_A2311
            BVI: Bcep1808_1869
            BUR: Bcep18194_A5253
            BCN: Bcen_6137
            BCH: Bcen2424_1942
            BAM: Bamb_1930
            BPS: BPSL2098(ispF)
            BPM: BURPS1710b_2511(ispF)
            BPL: BURPS1106A_2400(ispF)
            BPD: BURPS668_2357(ispF)
            BTE: BTH_I2090(ispF)
            PNU: Pnuc_0931
            BPE: BP0866(ispF)
            BPA: BPP3365(ispF)
            BBR: BB3816(ispF)
            RFR: Rfer_1332
            POL: Bpro_2715
            PNA: Pnap_2548
            AAV: Aave_1582
            AJS: Ajs_3155
            VEI: Veis_4361
            MPT: Mpe_A1571
            HAR: HEAR1911(ispF)
            MMS: mma_1410
            NEU: NE1402
            NET: Neut_1300
            NMU: Nmul_A2126
            EBA: ebA6542(ispF)
            AZO: azo1683(ispF)
            DAR: Daro_1974
            TBD: Tbd_1004
            MFA: Mfla_1117
            HPY: HP1020
            HPJ: jhp0404
            HPA: HPAG1_0427
            HHE: HH1582
            HAC: Hac_1124(ispD)
            WSU: WS1940
            TDN: Tmden_1487
            CJE: Cj1607
            CJR: CJE1779
            CJU: C8J_1508
            CFF: CFF8240_0409
            CHA: CHAB381_0932
            CCO: CCC13826_0390
            ABU: Abu_0126(ispDF)
            NIS: NIS_0595
            SUN: SUN_0522
            GSU: GSU3367(ispF)
            GME: Gmet_0059
            GUR: Gura_4164
            PCA: Pcar_0102
            PPD: Ppro_0012
            DVU: DVU1454(ispD)
            DDE: Dde_1726
            LIP: LI0446
            DPS: DP0257
            ADE: Adeh_1272
            SAT: SYN_01400
            SFU: Sfum_1636
            WOL: WD1143
            WBM: Wbm0409
            AMA: AM1356(ispF)
            APH: APH_1276(ispF)
            ERU: Erum1020(ispF)
            ERW: ERWE_CDS_00990(ispF)
            ERG: ERGA_CDS_00950(ispF)
            ECN: Ecaj_0102
            ECH: ECH_0156(ispF)
            NSE: NSE_0134(ispF)
            MLO: mll0395
            MES: Meso_1621
            SME: SMc01040
            ATU: Atu1443(ispF)
            ATC: AGR_C_2659
            RET: RHE_CH01945(ispDF)
            RLE: RL2254(ispDF)
            BME: BMEI0863
            BMF: BAB1_1143
            BMS: BR1120
            BMB: BruAb1_1126(ispDF)
            BOV: BOV_1078
            BJA: bll4485
            BRA: BRADO3869(ispDF)
            BBT: BBta_4067(ispDF)
            RPA: RPA2590(ispD)
            RPB: RPB_2885
            RPC: RPC_2575
            RPD: RPD_2587
            RPE: RPE_2755
            NWI: Nwi_1442
            NHA: Nham_1834
            BHE: BH05820
            BQU: BQ04980(ispDF)
            BBK: BARBAKC583_0540(ispDF)
            CCR: CC_1738
            SIL: SPO2090(ispDF)
            RSP: RSP_6071(ispF)
            RSH: Rsph17029_1460
            RSQ: Rsph17025_1484
            RDE: RD1_2767(ispF)
            MMR: Mmar10_1439
            ZMO: ZMO1128
            NAR: Saro_1925
            SAL: Sala_1278
            ELI: ELI_06290
            GOX: GOX1669(ispD)
            GBE: GbCGDNIH1_1019
            ACR: Acry_2031
            RRU: Rru_A1674
            MAG: amb2363
            MGM: Mmc1_2673
            ABA: Acid345_0187
            SUS: Acid_1861
            BSU: BG10153(ispF)
            BHA: BH0108
            BAN: BA0085(ispF)
            BAR: GBAA0085(ispF)
            BAA: BA_0675(ygbB)
            BAT: BAS0086
            BCE: BC0107(ispF)
            BCA: BCE_0086(ispF)
            BCZ: BCZK0082(ispF)
            BCY: Bcer98_0081
            BTK: BT9727_0083(ispF)
            BTL: BALH_0086(ispF)
            BLI: BL03266(ispF)
            BLD: BLi00109(yacN)
            BCL: ABC0126(ispF)
            BPU: BPUM_0076
            GKA: GK0082(ispF)
            LMO: lmo0236
            LMF: LMOf2365_0248(ispF)
            LIN: lin0268
            EFA: EF0042(ispF)
            CAC: CAC0434
            CPE: CPE2316
            CPF: CPF_2616(ispF)
            CPR: CPR_2302(ispF)
            CTC: CTC00232
            CNO: NT01CX_0736(ispF)
            CTH: Cthe_2946
            CDF: CD0048(ispF)
            CBO: CBO0066(ispF)
            CBA: CLB_0102(ispF)
            CBH: CLC_0114(ispF)
            CBF: CLI_0123(ispF)
            CBE: Cbei_0297
            CKL: CKL_3774(ispF)
            AMT: Amet_4505
            CHY: CHY_2341(ispF)
            DSY: DSY0444
            DRM: Dred_0188
            SWO: Swol_2360
            CSC: Csac_1587
            TTE: TTE2320(ispF)
            MTA: Moth_2486
            MPE: MYPE10270
            MGA: MGA_0657
            MTU: Rv3581c(ispF)
            MTC: MT3687
            MBO: Mb3612c(ispF)
            MLE: ML0322
            MPA: MAP0477
            MAV: MAV_0572(ispF)
            MSM: MSMEG_6075(ispF)
            MVA: Mvan_5339
            MGI: Mflv_1445
            MMC: Mmcs_4738
            MKM: Mkms_4824
            MJL: Mjls_5124
            CGL: NCgl2569(ispF)
            CGB: cg2944(ispF)
            CEF: CE2520
            CDI: DIP1972
            CJK: jk0309(ispF)
            NFA: nfa4370(mecS)
            RHA: RHA1_ro04461
            SCO: SCO4234(SCD8A.07)
            SMA: SAV3968(mecS)
            TWH: TWT348(ispDF)
            TWS: TW422
            LXX: Lxx18250(ispF)
            ART: Arth_0728
            AAU: AAur_0899(ispF)
            PAC: PPA0354
            NCA: Noca_4024
            TFU: Tfu_2906
            FRA: Francci3_4253
            FAL: FRAAL6523(ispF)
            ACE: Acel_0081
            KRA: Krad_0900
            SEN: SACE_0440(ispF)
            STP: Strop_4260
            BLO: BL0997(ispF)
            BAD: BAD_0669(ispF)
            RXY: Rxyl_2175
            FNU: FN1788
            RBA: RB3451(ispF)
            CTR: CT434(ygbB)
            CTA: CTA_0474(ispF)
            CMU: TC0718
            CPN: CPn0547(ygbB)
            CPA: CP0205
            CPJ: CPj0547(ygbB)
            CPT: CpB0568
            CCA: CCA00195
            CAB: CAB191
            CFE: CF0812(ispF)
            PCU: pc0227(ipsF)
            TPA: TP0512
            TDE: TDE2292(ispF)
            LIL: LA3591(ygbB)
            LIC: LIC10610(ispF)
            LBJ: LBJ_0323(ispF)
            LBL: LBL_2753(ispF)
            SYN: slr1542
            SYW: SYNW1610
            SYC: syc0380_d
            SYF: Synpcc7942_1170
            SYD: Syncc9605_0890
            SYE: Syncc9902_1508
            SYG: sync_0781(ispF)
            SYR: SynRCC307_1730(ispF)
            SYX: SynWH7803_1723(ispF)
            CYA: CYA_0267(ispF)
            CYB: CYB_0783(ispF)
            TEL: tlr2035
            GVI: glr3547
            ANA: alr3883
            AVA: Ava_1811(ispF)
            PMA: Pro1354(trmD)
            PMM: PMM1280
            PMT: PMT0356
            PMN: PMN2A_0847
            PMI: PMT9312_1374
            PMB: A9601_14791(trmD)
            PMC: P9515_14411(trmD)
            PMF: P9303_19461(trmD)
            PMG: P9301_14651(trmD)
            PMH: P9215_15051
            PME: NATL1_17001(trmD)
            TER: Tery_4716
            BTH: BT_3884
            BFR: BF4006
            BFS: BF3780(ispF)
            PGI: PG0028(ispF)
            SRU: SRU_1651(ispF)
            CHU: CHU_3180(ispF)
            CTE: CT1601(ispF)
            CCH: Cag_1782
            CPH: Cpha266_0591
            PVI: Cvib_1388
            PLT: Plut_1598
            DET: DET0060(ispF)
            DEH: cbdb_A75(ispF)
            DEB: DehaBAV1_0054
            DRA: DR_0230
            DGE: Dgeo_0073
            TTH: TTC1438
            TTJ: TTHA1790
            AAE: aq_957
            TMA: TM0647
            TPT: Tpet_0283
            TME: Tmel_0239
            FNO: Fnod_1503
STRUCTURES  PDB: 1GX1  1H47  1H48  1IV1  1IV2  1IV3  1IV4  1T0A  1U3L  1U3P  
                 1U40  1U43  1VH8  1VHA  1W55  1W57  1YQN  2AMT  2GZL  2PMP  
DBLINKS     IUBMB Enzyme Nomenclature: 4.6.1.12
            ExPASy - ENZYME nomenclature database: 4.6.1.12
            ExplorEnz - The Enzyme Database: 4.6.1.12
            ERGO genome analysis and discovery system: 4.6.1.12
            BRENDA, the Enzyme Database: 4.6.1.12
///
ENTRY       EC 4.6.1.13                 Enzyme
NAME        phosphatidylinositol diacylglycerol-lyase;
            monophosphatidylinositol phosphodiesterase;
            phosphatidylinositol phospholipase C;
            1-phosphatidylinositol phosphodiesterase;
            1-phosphatidyl-D-myo-inositol inositolphosphohydrolase
            (cyclic-phosphate-forming);
            1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase
            (1,2-cyclic-phosphate-forming)
CLASS       Lyases;
            Phosphorus-oxygen lyases;
            Phosphorus-oxygen lyases (only sub-subclass identified to date)
SYSNAME     1-phosphatidyl-1D-myo-inositol 1,2-diacyl-sn-glycerol-lyase
            (1D-myo-inositol-1,2-cyclic-phosphate-forming)
REACTION    1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic
            phosphate + 1,2-diacyl-sn-glycerol [RN:R03364]
ALL_REAC    R03364;
            (other) R03332
SUBSTRATE   1-phosphatidyl-1D-myo-inositol [CPD:C01194]
PRODUCT     1D-myo-inositol 1,2-cyclic phosphate [CPD:C04299];
            1,2-diacyl-sn-glycerol [CPD:C00641]
COMMENT     This enzyme is bacterial. Activity is also found in animals, but
            this activity is due to the presence of EC 3.1.4.11,
            phosphoinositide phospholipase C.
REFERENCE   1  [PMID:4377210]
  AUTHORS   Allan D, Michell RH.
  TITLE     Phosphatidylinositol cleavage catalysed by the soluble fraction from
            lymphocytes. Activity at pH5.5 and pH7.0.
  JOURNAL   Biochem. J. 142 (1974) 591-7.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:4294905]
  AUTHORS   Friedel RO, Brown JD, Durell.
  TITLE     Monophosphatidyl inositol inositolphosphohydrolase in guinea-pig
            brain.
  JOURNAL   Biochim. Biophys. Acta. 144 (1967) 684-6.
  ORGANISM  guinea pig
REFERENCE   3  [PMID:6297738]
  AUTHORS   Irvine RF.
  TITLE     The enzymology of stimulated inositol lipid turnover.
  JOURNAL   Cell. Calcium. 3 (1982) 295-309.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:236918]
  AUTHORS   Michell RH, Allan D.
  TITLE     Inositol cyclis phosphate as a product of phosphatidylinositol
            breakdown by phospholipase C (Bacillus cereus).
  JOURNAL   FEBS. Lett. 53 (1975) 302-4.
  ORGANISM  Bacillus cereus
REFERENCE   5  [PMID:588258]
  AUTHORS   Low MG, Finean JB.
  TITLE     Release of alkaline phosphatase from membranes by a
            phosphatidylinositol-specific phospholipase C.
  JOURNAL   Biochem. J. 167 (1977) 281-4.
  ORGANISM  Staphylococcus aureus
REFERENCE   6  [PMID:3194218]
  AUTHORS   Henner DJ, Yang M, Chen E, Hellmiss R, Rodriguez H, Low MG.
  TITLE     Sequence of the Bacillus thuringiensis phosphatidylinositol specific
            phospholipase C.
  JOURNAL   Nucleic. Acids. Res. 16 (1988) 10383.
  ORGANISM  Bacillus thuringiensis
PATHWAY     PATH: map00562  Inositol phosphate metabolism
ORTHOLOGY   KO: K01771  1-phosphatidylinositol phosphodiesterase
GENES       PIC: PICST_70308
            CAL: CaO19_1586(CaO19.1586)
            ANI: AN3636.2
            AFM: AFUA_4G12000
            AOR: AO090003001009
            TET: TTHERM_00426140
            BUR: Bcep18194_B0943
            BCH: Bcen2424_4771
            BAM: Bamb_4154
            BAN: BA3891
            BAR: GBAA3891
            BAA: BA_4362
            BAT: BAS3604
            BCE: BC3761
            BCA: BCE_3793
            SAU: SA0091(plc)
            SAV: SAV0095(plc)
            SAM: MW0070(plc)
            SAR: SAR0105(plc)
            SAS: SAS0070(plc)
            SAC: SACOL0078(plc)
            SAB: SAB0038(plc)
            SAA: SAUSA300_0099(plc)
            SAO: SAOUHSC_00051
            SAJ: SaurJH9_0083
            SAH: SaurJH1_0086
            LMO: lmo0201(plcA)
            LMF: LMOf2365_0212(plcA)
            FAL: FRAAL3352
STRUCTURES  PDB: 1T6M  2OR2  
DBLINKS     IUBMB Enzyme Nomenclature: 4.6.1.13
            ExPASy - ENZYME nomenclature database: 4.6.1.13
            ExplorEnz - The Enzyme Database: 4.6.1.13
            ERGO genome analysis and discovery system: 4.6.1.13
            BRENDA, the Enzyme Database: 4.6.1.13
            CAS: 37288-19-0
///
ENTRY       EC 4.6.1.14                 Enzyme
NAME        glycosylphosphatidylinositol diacylglycerol-lyase;
            (glycosyl)phosphatidylinositol-specific phospholipase C;
            GPI-PLC;
            GPI-specific phospholipase C;
            VSG-lipase;
            glycosyl inositol phospholipid anchor-hydrolyzing enzyme;
            glycosylphosphatidylinositol-phospholipase C;
            glycosylphosphatidylinositol-specific phospholipase C;
            variant-surface-glycoprotein phospholipase C;
            6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
            diacylglycerol-lyase (1,2-cyclic-phosphate-forming)
CLASS       Lyases;
            Phosphorus-oxygen lyases;
            Phosphorus-oxygen lyases (only sub-subclass identified to date)
SYSNAME     6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
            1,2-diacyl-sn-glycerol-lyase
            [6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic
            phosphate-forming]
REACTION    6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol =
            6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate +
            1,2-diacyl-sn-glycerol [RN:R07635]
ALL_REAC    R07635;
            (other) R04459
SUBSTRATE   6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol [CPD:C04248]
PRODUCT     6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate
            [CPD:C16070];
            1,2-diacyl-sn-glycerol [CPD:C00641]
COMMENT     This enzyme is also active when O-4 of the glucosamine is
            substituted by carrying the oligosaccharide that can link a protein
            to the structure. It therefore cleaves proteins from the lipid part
            of the glycosylphostphatidylinositol (GPI) anchors. In some cases,
            the long-chain acyl group at the sn-1 position of glycerol is
            replaced by an alkyl or alk-1-enyl group. In other cases, the
            diacylglycerol is replaced by ceramide (see Lip-1.4 and Lip-1.5 for
            definition). The only characterized enzyme with this specificity is
            from Trypanosoma brucei, where the acyl groups are myristoyl, but
            the function of the trypanosome enzyme is unknown. Substitution on
            O-2 of the inositol blocks action of this enzyme. It is not
            identical with EC 3.1.4.50, glycosylphosphatidylinositol
            phospholipase D.
REFERENCE   1  [PMID:3759991]
  AUTHORS   Hereld D, Krakow JL, Bangs JD, Hart GW, Englund PT.
  TITLE     A phospholipase C from Trypanosoma brucei which selectively cleaves
            the glycolipid on the variant surface glycoprotein.
  JOURNAL   J. Biol. Chem. 261 (1986) 13813-9.
  ORGANISM  Trypanosoma brucei [GN:tbr]
REFERENCE   2  [PMID:9476790]
  AUTHORS   Carnall N, Webb H, Carrington M.
  TITLE     Mutagenesis study of the glycosylphosphatidylinositol phospholipase
            C of Trypanosoma brucei.
  JOURNAL   Mol. Biochem. Parasitol. 90 (1997) 423-32.
  ORGANISM  Trypanosoma brucei [GN:tbr]
REFERENCE   3  [PMID:10764777]
  AUTHORS   Armah DA, Mensa-Wilmot K.
  TITLE     Tetramerization of glycosylphosphatidylinositol-specific
            phospholipase C from Trypanosoma brucei.
  JOURNAL   J. Biol. Chem. 275 (2000) 19334-42.
  ORGANISM  Trypanosoma brucei [GN:tbr]
ORTHOLOGY   KO: K06038  
GENES       TCR: 507041.120 508233.50
            BCZ: BCZK3513
            BTK: BT9727_3501
DBLINKS     IUBMB Enzyme Nomenclature: 4.6.1.14
            ExPASy - ENZYME nomenclature database: 4.6.1.14
            ExplorEnz - The Enzyme Database: 4.6.1.14
            ERGO genome analysis and discovery system: 4.6.1.14
            BRENDA, the Enzyme Database: 4.6.1.14
            CAS: 129070-68-4
///
ENTRY       EC 4.6.1.15                 Enzyme
NAME        FAD-AMP lyase (cyclizing);
            FMN cyclase;
            FAD AMP-lyase (cyclic-FMN-forming)
CLASS       Lyases;
            Phosphorus-oxygen lyases;
            Phosphorus-oxygen lyases (only sub-subclass identified to date)
SYSNAME     FAD AMP-lyase (riboflavin-cyclic-4',5'-phosphate-forming)
REACTION    FAD = AMP + riboflavin cyclic-4',5'-phosphate [RN:R07636]
ALL_REAC    R07636
SUBSTRATE   FAD [CPD:C00016]
PRODUCT     AMP [CPD:C00020];
            riboflavin cyclic-4',5'-phosphate [CPD:C16071]
COMMENT     Requires Mn2+ or Co2+. While FAD was the best substrate tested [2],
            the enzyme also splits ribonucleoside diphosphate-X compounds in
            which X is an acyclic or cyclic monosaccharide or derivative bearing
            an X-OH group that is able to attack internally the proximal
            phosphorus with the geometry necessary to form a P=X product; either
            a five-atom monocyclic phosphodiester or a cis-bicyclic
            phosphodiester-pyranose fusion. The reaction is strongly inhibited
            by ADP or ATP but is unaffected by the presence of the product,
            cFMN.
REFERENCE   1  [PMID:9480905]
  AUTHORS   Fraiz FJ, Pinto RM, Costas MJ, Aavalos M, Canales J, Cabezas A,
            Cameselle JC.
  TITLE     Enzymic formation of riboflavin 4',5'-cyclic phosphate from FAD:
            evidence for a specific low-Km FMN cyclase in rat liver1.
  JOURNAL   Biochem. J. 330 ( Pt 2) (1998) 881-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:11695920]
  AUTHORS   Cabezas A, Pinto RM, Fraiz F, Canales J, Gonzalez-Santiago S,
            Cameselle JC.
  TITLE     Purification, characterization, and substrate and inhibitor
            structure-activity studies of rat liver FAD-AMP lyase (cyclizing):
            preference for FAD and specificity for splitting ribonucleoside
            diphosphate-X into ribonucleotide and a five-atom cyclic
            phosphodiester of X, either a monocyclic compound or a cis-bicyclic
            phosphodiester-pyranose fusion.
  JOURNAL   Biochemistry. 40 (2001) 13710-22.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 4.6.1.15
            ExPASy - ENZYME nomenclature database: 4.6.1.15
            ExplorEnz - The Enzyme Database: 4.6.1.15
            ERGO genome analysis and discovery system: 4.6.1.15
            BRENDA, the Enzyme Database: 4.6.1.15
            CAS: 208349-48-8
///
ENTRY       EC 4.6.1.-                  Enzyme
CLASS       Lyases;
            Phosphorus-oxygen lyases
REACTION    2,3-Bisphospho-D-glycerate + ATP <=> Cyclic
            2,3-bisphospho-D-glycerate + ADP + Orthophosphate [RN:R03298]
SUBSTRATE   2,3-Bisphospho-D-glycerate [CPD:C01159];
            ATP [CPD:C00002]
PRODUCT     Cyclic 2,3-bisphospho-D-glycerate [CPD:C06189];
            ADP [CPD:C00008];
            Orthophosphate [CPD:C00009]
///
ENTRY       EC 4.99.1.1                 Enzyme
NAME        ferrochelatase;
            ferro-protoporphyrin chelatase;
            iron chelatase;
            heme synthetase;
            heme synthase;
            protoheme ferro-lyase
CLASS       Lyases;
            Other lyases;
            Sole sub-subclass for lyases that do not belong in the other
            subclasses
SYSNAME     protoheme ferro-lyase (protoporphyrin-forming)
REACTION    protoheme + 2 H+ = protoporphyrin + Fe2+ [RN:R00310]
ALL_REAC    R00310
SUBSTRATE   protoheme [CPD:C00032];
            H+ [CPD:C00080]
PRODUCT     protoporphyrin [CPD:C02191];
            Fe2+ [CPD:C14818]
REFERENCE   1  [PMID:3805002]
  AUTHORS   Bloomer JR, Hill HD, Morton KO, Anderson-Burnham LA, Straka JG.
  TITLE     The enzyme defect in bovine protoporphyria. Studies with purified
            ferrochelatase.
  JOURNAL   J. Biol. Chem. 262 (1987) 667-71.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:13972328]
  AUTHORS   PORRA RJ, JONES OT.
  TITLE     Studies on ferrochelatase. 1. Assay and properties of ferrochelatase
            from a pig-liver mitochondrial extract.
  JOURNAL   Biochem. J. 87 (1963) 181-5.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:13972329]
  AUTHORS   PORRA RJ, JONES OT.
  TITLE     Studies on ferrochelatase. 2. An in vestigation of the role
            offerrochelatase in the biosynthesis of various haem prosthetic
            groups.
  JOURNAL   Biochem. J. 87 (1963) 186-92.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K01772  ferrochelatase
GENES       HSA: 2235(FECH)
            PTR: 455437(FECH)
            MMU: 14151(Fech)
            CFA: 610360(FECH)
            BTA: 281158(FECH)
            GGA: 374020(FECH)
            DRE: 58215(fech)
            SPU: 582724(LOC582724)
            DME: Dmel_CG2098(ferrochelatase)
            ATH: AT5G26030
            OSA: 4338537 4346651
            CME: CMS035C
            SCE: YOR176W(HEM15)
            AGO: AGOS_AGR272W
            PIC: PICST_36859(HEM15)
            CGR: CAGL0L04664g
            SPO: SPCC320.09
            ANI: AN7752.2
            AFM: AFUA_5G07750
            AOR: AO090701000682
            CNE: CNF01700
            UMA: UM03444.1
            DDI: DDB_0231413(hemH)
            PFA: MAL13P1.326
            TET: TTHERM_00439000
            LMA: LmjF17.1460
            ECO: b0475(hemH)
            ECJ: JW0464(hemH)
            ECE: Z0592(hemH)
            ECS: ECs0528
            ECC: c0595(hemH)
            ECI: UTI89_C0503(hemH)
            ECP: ECP_0536
            ECV: APECO1_1540(hemH)
            ECW: EcE24377A_0515(hemH)
            ECX: EcHS_A0552(hemH)
            STY: STY0533(hemH)
            STT: t2371(hemH)
            SPT: SPA2233(hemH)
            SEC: SC0531(hemH)
            STM: STM0489(hemH)
            YPE: YPO3117(hemH)
            YPK: y1066(hemH)
            YPM: YP_0813(hemH)
            YPA: YPA_2610
            YPN: YPN_0972
            YPP: YPDSF_2753
            YPS: YPTB0997(hemH)
            YPI: YpsIP31758_3053(hemH)
            SFL: SF0420(hemH)
            SFX: S0427(hemH)
            SFV: SFV_0448(hemH)
            SSN: SSON_0462(hemH)
            SBO: SBO_0375(hemH)
            SDY: SDY_0444(hemH)
            ECA: ECA1181(hemH)
            PLU: plu3835(hemH)
            WBR: WGLp529(hemH)
            SGL: SG0694
            ENT: Ent638_0955
            SPE: Spro_1143
            HIT: NTHI1329(hemH)
            HIP: CGSHiEE_06250(hemH)
            HIQ: CGSHiGG_09520(hemH)
            HSO: HS_1047(hemH)
            PMU: PM0789(hemH)
            MSU: MS1346(hemH)
            APL: APL_1937(hemH)
            ASU: Asuc_1562
            XFA: XF0566
            XFT: PD1576(hemH)
            XCC: XCC4095(hemH)
            XCB: XC_4186
            XCV: XCV4323(hemH)
            XAC: XAC4220(hemH)
            XOO: XOO4410(hemH)
            XOM: XOO_4154(XOO4154)
            VCH: VC0987
            VCO: VC0395_A0508(hemH)
            VVU: VV1_0187
            VVY: VV1003
            VPA: VP0823
            VFI: VF0794
            PPR: PBPRA1025
            PAE: PA4655(hemH)
            PAU: PA14_61580(hemH)
            PAP: PSPA7_5304(hemH)
            PPU: PP_0744(hemH)
            PPF: Pput_0772
            PST: PSPTO_1128(hemH)
            PSB: Psyr_0967(hemH)
            PSP: PSPPH_1016(hemH)
            PFL: PFL_5141(hemH)
            PFO: Pfl_4730
            PEN: PSEEN0886(hemH)
            PMY: Pmen_1077
            PAR: Psyc_0376(hemH)
            PCR: Pcryo_0415
            PRW: PsycPRwf_2057
            ACI: ACIAD3255(hemH)
            SON: SO_2019(hemH-1) SO_3348(hemH-2)
            SDN: Sden_2678
            SFR: Sfri_2852
            SAZ: Sama_1316
            SBL: Sbal_2545 Sbal_3021
            SBM: Shew185_2583 Shew185_3036
            SLO: Shew_1140 Shew_2229
            SPC: Sputcn32_2296 Sputcn32_2683
            SSE: Ssed_1235 Ssed_2846
            SPL: Spea_1130 Spea_1529
            SHE: Shewmr4_1197 Shewmr4_2248
            SHM: Shewmr7_1268 Shewmr7_2320
            SHN: Shewana3_1198 Shewana3_2440
            SHW: Sputw3181_1328 Sputw3181_1712
            ILO: IL2347(hemH)
            CPS: CPS_1039(hemH)
            PHA: PSHAb0112(hemH)
            PAT: Patl_3987
            SDE: Sde_0129
            PIN: Ping_2535
            MAQ: Maqu_1496
            CBU: CBU_0042(hemH)
            CBD: COXBU7E912_2060(hemH)
            LPN: lpg0425(hemH)
            LPF: lpl0468(hemZ)
            LPP: lpp0492(hemZ)
            MCA: MCA1671(hemH)
            FTU: FTT1138(hemH)
            FTF: FTF1138(hemH)
            FTW: FTW_1172(hemH)
            FTL: FTL_0821
            FTH: FTH_0813(hemH)
            FTA: FTA_0870(hemH)
            FTN: FTN_1120(hemH)
            TCX: Tcr_1864
            NOC: Noc_1545
            AEH: Mlg_0737
            HHA: Hhal_0819
            HCH: HCH_00646(hemH)
            CSA: Csal_0897
            ABO: ABO_0294(hemH)
            MMW: Mmwyl1_2215
            AHA: AHA_2488(hemH)
            DNO: DNO_1249(hemH)
            RMA: Rmag_0522
            VOK: COSY_0478(hemH)
            NME: NMB0718
            NMA: NMA0927(hemH)
            NMC: NMC0669(hemH)
            NGO: NGO0293
            CVI: CV_2480(hemH)
            RSO: RSc2643(hemH)
            REU: Reut_A1037
            REH: H16_A1134(hemH)
            RME: Rmet_1001
            BMA: BMA2330(hemH)
            BMV: BMASAVP1_A0495(hemH)
            BML: BMA10299_A1104(hemH)
            BMN: BMA10247_2211(hemH)
            BXE: Bxe_A3965
            BVI: Bcep1808_0707
            BUR: Bcep18194_A3835
            BCN: Bcen_0262
            BCH: Bcen2424_0746
            BAM: Bamb_0640
            BPS: BPSL2831
            BPM: BURPS1710b_3326(hemH)
            BPL: BURPS1106A_3316(hemH)
            BPD: BURPS668_3283(hemH)
            BTE: BTH_I1303(hemH)
            PNU: Pnuc_1771
            BPE: BP2503(hemH)
            BPA: BPP3489(hemH)
            BBR: BB3938(hemH)
            RFR: Rfer_1545
            POL: Bpro_2013
            PNA: Pnap_2973
            AAV: Aave_3000
            AJS: Ajs_1652
            VEI: Veis_1574
            MPT: Mpe_A2495
            HAR: HEAR2650(hemH)
            MMS: mma_2885(hemH)
            NEU: NE1476(hemH)
            NET: Neut_0770
            NMU: Nmul_A2424
            EBA: ebA4802(hemH)
            AZO: azo2582(hemH)
            DAR: Daro_0929
            TBD: Tbd_2033
            MFA: Mfla_0772
            HPY: HP0376
            HPA: HPAG1_1016
            HHE: HH0996(hemH)
            HAC: Hac_0490(hemH)
            WSU: WS2157(hemH)
            TDN: Tmden_0918
            CJE: Cj0503c(hemH)
            CJR: CJE0610(hemH)
            CJJ: CJJ81176_0531(hemH)
            CJU: C8J_0467(hemH)
            CJD: JJD26997_1433(hemH)
            CFF: CFF8240_0703(hemH)
            CCV: CCV52592_0446
            CHA: CHAB381_0988(hemH)
            CCO: CCC13826_0053(hemH)
            ABU: Abu_0550(hemH)
            NIS: NIS_0734(hemH)
            SUN: SUN_1669(hemH)
            GSU: GSU3312(hemH)
            GME: Gmet_0019
            GUR: Gura_0173
            PCA: Pcar_0770
            PPD: Ppro_2715
            BBA: Bd3456(hemH)
            DPS: DP1085
            ADE: Adeh_1090
            AFW: Anae109_1130
            MXA: MXAN_1537(hemH)
            RPR: RP884
            RTY: RT0876(hemH)
            RCO: RC1373(hemH)
            RFE: RF_1399(hemH)
            RBE: RBE_1428(hemH)
            RAK: A1C_06875(hemH)
            RBO: A1I_07945(hemH)
            RCM: A1E_05670(hemH)
            RRI: A1G_07515(hemH)
            OTS: OTBS_1009(hemH)
            WOL: WD1186(hemH)
            WBM: Wbm0719
            AMA: AM922(hemH)
            APH: APH_0263(hemH)
            ERU: Erum6180(hemH)
            ERW: ERWE_CDS_06490(hemH)
            ERG: ERGA_CDS_06400(hemH)
            ECN: Ecaj_0623
            ECH: ECH_0395(hemH)
            NSE: NSE_0790(hemH)
            PUB: SAR11_0346(hemH)
            MLO: mlr3019
            MES: Meso_2724
            PLA: Plav_1258
            SME: SMc04019(hemH)
            SMD: Smed_2691
            ATU: Atu3771(hemH)
            ATC: AGR_L_2129
            RET: RHE_CH03556(hemH)
            RLE: RL4076(hemH)
            BME: BMEII0018
            BMF: BAB2_0075(hemH)
            BMS: BRA0076(hemH)
            BMB: BruAb2_0076(hemH)
            BOV: BOV_A0071(hemH)
            OAN: Oant_4266
            BJA: bll7752(hemH)
            BRA: BRADO6249(hemH)
            BBT: BBta_1357(hemH)
            RPA: RPA0875(hemZ)
            RPB: RPB_4542
            RPC: RPC_4842
            RPD: RPD_0861
            RPE: RPE_4807
            NWI: Nwi_0928
            NHA: Nham_3415
            XAU: Xaut_2814
            CCR: CC_3762
            SIL: SPO0073(hemH)
            SIT: TM1040_2900
            RSP: RSP_1197(hemH)
            RSH: Rsph17029_2858
            RSQ: Rsph17025_2635
            JAN: Jann_0293
            RDE: RD1_0401(hemH)
            PDE: Pden_2583
            MMR: Mmar10_2972
            HNE: HNE_3567(hemH)
            ZMO: ZMO0303(hemH)
            NAR: Saro_3336
            SAL: Sala_2253
            SWI: Swit_4598
            ELI: ELI_11315
            GOX: GOX0874
            GBE: GbCGDNIH1_2434
            ACR: Acry_2474
            RRU: Rru_A3617
            MAG: amb4551
            MGM: Mmc1_1701
            ABA: Acid345_0694
            SUS: Acid_1029 Acid_5203
            BSU: BG10430(hemH)
            BHA: BH1203(hemH)
            BAN: BA1071(hemH-1) BA1158(hemH-2)
            BAR: GBAA1071(hemH-1) GBAA1158(hemH-2)
            BAA: BA_1623 BA_1703
            BAT: BAS1000 BAS1075
            BCE: BC1069 BC1154
            BCA: BCE_1168(hemH) BCE_1260(hemH)
            BCZ: BCZK0987(hemH) BCZK1054
            BCY: Bcer98_0825 Bcer98_0873
            BTK: BT9727_0985(hemH) BT9727_1056(hemH)
            BTL: BALH_1018
            BLI: BL00949 BL01073(hemH)
            BLD: BLi01093(hemH) BLi04115
            BCL: ABC1539(hemH)
            BAY: RBAM_010360(hemH)
            BPU: BPUM_0959(hemH)
            OIH: OB1168(hemH)
            GKA: GK0662
            SAU: SA1651(hemH)
            SAV: SAV1833(hemH)
            SAM: MW1773(hemH)
            SAR: SAR1924(hemH)
            SAS: SAS1754
            SAC: SACOL1888(hemH)
            SAB: SAB1764c(hemH)
            SAA: SAUSA300_1782(hemH)
            SAO: SAOUHSC_01961
            SAJ: SaurJH9_1886
            SAH: SaurJH1_1920
            SEP: SE1512
            SER: SERP1367(hemH)
            SHA: SH1129(hemH)
            SSP: SSP0966
            LMO: lmo2211(hemH)
            LMF: LMOf2365_2244(hemH)
            LIN: lin2314(hemH)
            LWE: lwe2228(hemH)
            LLA: L0194(hemH)
            LLC: LACR_1661
            LLM: llmg_0934(hemH)
            SPN: SP_1009
            SPR: spr0914(hemH)
            SPD: SPD_0895(hemH)
            SMU: SMU.2063(hemZ)
            STC: str0934 str0935
            STL: stu0934 stu0935
            SSA: SSA_1321(hemH)
            SGO: SGO_1311(hemH)
            LPL: lp_1296(hemH)
            LCA: LSEI_1991
            LRE: Lreu_1554
            EFA: EF1989(hemH)
            STH: STH160
            CHY: CHY_0482(hemH)
            MTU: Rv1485(hemZ)
            MTC: MT1532(hemH)
            MBO: Mb1521(hemZ)
            MBB: BCG_1547(hemZ)
            MLE: ML1805(hemZ)
            MPA: MAP1211(hemZ)
            MAV: MAV_3293(hemH)
            MSM: MSMEG_3152(hemH)
            MVA: Mvan_2754
            MGI: Mflv_3656
            MMC: Mmcs_2458
            MKM: Mkms_2503
            MJL: Mjls_2495
            CGL: NCgl1479(cgl1537)
            CGB: cg1734(hemH)
            CEF: CE1658
            CDI: DIP1280
            CJK: jk1996(hemH)
            NFA: nfa34750(hemH)
            RHA: RHA1_ro07215(hemZ)
            SCO: SCO5859(hemH)
            SMA: SAV2407(hemH)
            TWH: TWT733(hemZ)
            TWS: TW747(hemH)
            LXX: Lxx01090(hemZ)
            CMI: CMM_0595(hemH)
            ART: Arth_2768
            PAC: PPA0308
            NCA: Noca_2913
            TFU: Tfu_1945
            FRA: Francci3_1902
            FAL: FRAAL4516(hemH)
            ACE: Acel_1407
            KRA: Krad_1552
            SEN: SACE_3785(hemH)
            STP: Strop_3023
            RBA: RB8233(hemH)
            CTR: CT485(hemZ)
            CTA: CTA_0532(hemZ)
            CMU: TC0772
            CPN: CPn0603(hemZ)
            CPA: CP0144
            CPJ: CPj0603(hemZ)
            CPT: CpB0627
            CCA: CCA00137(hemH)
            CAB: CAB136(hemH)
            CFE: CF0869(hemZ)
            PCU: pc1557(hemH)
            LIL: LB023 LB024
            LIC: LIC20018(hemH)
            LBJ: LBJ_4018(hemH)
            LBL: LBL_4018(hemH)
            SYN: slr0839(hemH)
            SYW: SYNW1747(hemH)
            SYC: syc1368_c(hemH)
            SYF: Synpcc7942_0137
            SYD: Syncc9605_0716
            SYE: Syncc9902_1643
            SYG: sync_1238(hli-1) sync_2000(hemH) sync_2075(hli-2)
                 sync_2227(hli-3) sync_2528(hli-4)
            SYR: SynRCC307_0854(hemH)
            SYX: SynWH7803_0644(hemH)
            CYA: CYA_1034(hemH)
            CYB: CYB_2857(hemH)
            TEL: tlr2216(hemH)
            GVI: gll0839(hemH)
            ANA: alr3751(hemH)
            AVA: Ava_1574 Ava_2754
            PMA: Pro0525(hemH)
            PMM: PMM0525
            PMT: PMT1240(hemH)
            PMN: PMN2A_1857
            PMI: PMT9312_0525
            PMB: A9601_05811(hemH)
            PMC: P9515_05891(hemH)
            PMF: P9303_07661(hemH)
            PMG: P9301_05511(hemH)
            PMH: P9215_06061(hemH)
            PME: NATL1_05821(hemH)
            TER: Tery_0602 Tery_4313
            PGI: PG0127(hemH)
            SRU: SRU_1741(hemH) SRU_2695(hemH)
            CHU: CHU_3490(hemH)
            GFO: GFO_3220(hemH)
            FJO: Fjoh_0939
            FPS: FP0046(hemH)
            CCH: Cag_0631
            RRS: RoseRS_1749 RoseRS_4065
            RCA: Rcas_1204 Rcas_2029
            DRA: DR_1131
            TTH: TTC0231
            TTJ: TTHA0600
            AAE: aq_948(hemH)
            TAC: Ta0311
            TVO: TVN1293
            PTO: PTO0948
STRUCTURES  PDB: 1AK1  1C1H  1C9E  1DOZ  1HRK  1KYQ  1L8X  1LBQ  1LD3  1N0I  
                 2AC2  2AC4  2C8J  2H1V  2H1W  2HK6  2HRC  2HRE  2PNJ  2PO5  
                 2PO7  
DBLINKS     IUBMB Enzyme Nomenclature: 4.99.1.1
            ExPASy - ENZYME nomenclature database: 4.99.1.1
            ExplorEnz - The Enzyme Database: 4.99.1.1
            ERGO genome analysis and discovery system: 4.99.1.1
            BRENDA, the Enzyme Database: 4.99.1.1
            CAS: 9012-93-5
///
ENTRY       EC 4.99.1.2                 Enzyme
NAME        alkylmercury lyase;
            organomercury lyase;
            organomercurial lyase;
            alkylmercury mercuric-lyase
CLASS       Lyases;
            Other lyases;
            Sole sub-subclass for lyases that do not belong in the other
            subclasses
SYSNAME     alkylmercury mercuric-lyase (alkane-forming)
REACTION    an alkylmercury + H+ = an alkane + Hg2+ [RN:R03529]
ALL_REAC    R03529
SUBSTRATE   alkylmercury [CPD:C01886];
            H+ [CPD:C00080]
PRODUCT     alkane [CPD:C01371];
            Hg2+ [CPD:C00703]
COMMENT     Acts on CH3Hg+ and a number of other alkylmercury compounds, in the
            presence of cysteine or other thiols, liberating mercury as a
            mercaptide. Some arylmercury compounds can also act as substrates.
REFERENCE   1  [PMID:9382]
  AUTHORS   Tezuka T, Tonomura K.
  TITLE     Purification and properties of an enzyme catalyzing the splitting of
            carbon-mercury linkages from mercury-resistant Pseudomonas K-62
            strain. I. Splitting enzyme 1.
  JOURNAL   J. Biochem. (Tokyo). 80 (1976) 79-87.
  ORGANISM  Pseudomonas sp.
ORTHOLOGY   KO: K00221  alkylmercury lyase
GENES       MAQ: Maqu_0243
            SEP: SE0086
            MGI: Mflv_3214
STRUCTURES  PDB: 1S6L  
DBLINKS     IUBMB Enzyme Nomenclature: 4.99.1.2
            ExPASy - ENZYME nomenclature database: 4.99.1.2
            ExplorEnz - The Enzyme Database: 4.99.1.2
            ERGO genome analysis and discovery system: 4.99.1.2
            UM-BBD (Biocatalysis/Biodegradation Database): 4.99.1.2
            BRENDA, the Enzyme Database: 4.99.1.2
            CAS: 72560-99-7
///
ENTRY       EC 4.99.1.3                 Enzyme
NAME        sirohydrochlorin cobaltochelatase;
            CbiK;
            CbiX;
            CbiXS;
            anaerobic cobalt chelatase;
            cobaltochelatase [ambiguous];
            sirohydrochlorin cobalt-lyase (incorrect)
CLASS       Lyases;
            Other lyases;
            Sole sub-subclass for lyases that do not belong in the other
            subclasses
SYSNAME     cobalt-sirohydrochlorin cobalt-lyase (sirohydrochlorin-forming)
REACTION    cobalt-sirohydrochlorin + 2 H+ = sirohydrochlorin + Co2+ [RN:R05807]
ALL_REAC    R05807
SUBSTRATE   cobalt-sirohydrochlorin [CPD:C11538];
            H+ [CPD:C00080]
PRODUCT     sirohydrochlorin [CPD:C05778];
            Co2+ [CPD:C00175]
COMMENT     This enzyme is a type II chelatase, being either a monomer (CbiX) or
            a homodimer (CibK) and being ATP-independent. CbiK from Salmonella
            enterica uses precorrin-2 as the substrate to yield
            cobalt-precorrin-2. The enzyme contains two histidines at the active
            site that are thought to be involved in the deprotonation of the
            tetrapyrrole substrate as well as in metal binding. CbiX from
            Bacillus megaterium inserts cobalt at the level of sirohydrochlorin
            (factor-II) rather than precorrin-2.
REFERENCE   1  [PMID:10451360]
  AUTHORS   Schubert HL, Raux E, Wilson KS, Warren MJ.
  TITLE     Common chelatase design in the branched tetrapyrrole pathways of
            heme and anaerobic cobalamin synthesis.
  JOURNAL   Biochemistry. 38 (1999) 10660-9.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:12686546]
  AUTHORS   Brindley AA, Raux E, Leech HK, Schubert HL, Warren MJ.
  TITLE     A story of chelatase evolution: identification and characterization
            of a small 13-15-kDa &quot;ancestral&quot; cobaltochelatase (CbiXS)
            in the archaea.
  JOURNAL   J. Biol. Chem. 278 (2003) 22388-95.
  ORGANISM  Bacillus megaterium, Methanosarcina barkeri [GN:mba], Methanobacter
            thermoautotrophicum
REFERENCE   3  [PMID:12195810]
  AUTHORS   Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
  TITLE     The biosynthesis of adenosylcobalamin (vitamin B12).
  JOURNAL   Nat. Prod. Rep. 19 (2002) 390-412.
  ORGANISM  Bacillus megaterium
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K02190  sirohydrochlorin cobaltochelatase
            KO: K03795  sirohydrochlorin cobaltochelatase
GENES       STY: STY2229(cbiK)
            STT: t0849(cbiK)
            SPT: SPA0846(cbiK)
            SEC: SC2033(cbiK)
            STM: STM2025(cbiK)
            PLU: plu2989(cbiK)
            CSA: Csal_0467
            RSO: RSc2418(RS02695)
            REU: Reut_A2686
            RME: Rmet_2810
            BMA: BMA0669
            BXE: Bxe_A3641
            BUR: Bcep18194_A5800
            BCN: Bcen_1858
            BCH: Bcen2424_2469
            BAM: Bamb_2518
            BPS: BPSL0962
            BPM: BURPS1710b_1172(cbiX)
            BTE: BTH_I0820(cbiX)
            RFR: Rfer_2113
            POL: Bpro_2405
            HAR: HEAR2398
            DAR: Daro_0828
            ABU: Abu_1192
            PCA: Pcar_0478
            DVU: DVU0650 DVU1365
            DDE: Dde_2181 Dde_3103
            LIP: LI1067
            DPS: DP0212
            SFU: Sfum_1101
            BPU: BPUM_1461(cbiX)
            LMO: lmo1202(cbiK)
            LMF: LMOf2365_1211(cbiK)
            LIN: lin1165(cbiK)
            LWE: lwe1159(cbiK)
            SSA: SSA_0475
            CAC: CAC1373(cbiK)
            CPE: CPE1228(cbiK)
            CPF: CPF_1436(cbiK)
            CPR: CPR_1242
            CTC: CTC00743(cbiK)
            CNO: NT01CX_0573(cbiK)
            CDF: CD3422(cbiK)
            CBA: CLB_0994(cbiK)
            CBH: CLC_1008(cbiK)
            CBF: CLI_1042(cbiK)
            CKL: CKL_0720(cbiK)
            MAV: MAV_4901
            FAL: FRAAL1021
            FNU: FN1263
            TDE: TDE2656(cbiK)
            SYN: sll0037(cbiX)
            SYG: sync_1195(cbiX)
            SYR: SynRCC307_0990(cbiX)
            SYX: SynWH7803_1422(cbiX)
            CYA: CYA_2373(cbiX)
            CYB: CYB_2347(cbiX)
            BFR: BF2511(cbiK)
            BFS: BF2540
            PGI: PG0669(fetB)
            CTE: CT0389
            MJA: MJ0970
            MMP: MMP0164(cbiX(s))
            MMQ: MmarC5_1511
            MMZ: MmarC7_1164
            MAE: Maeo_1381
            MVN: Mevan_1169
            MAC: MA3631(cbiX)
            MBA: Mbar_A0344
            MMA: MM_0517
            MBU: Mbur_1035
            MHU: Mhun_0266 Mhun_0668
            MTH: MTH1397
            MST: Msp_1563(cbiX)
            MSI: Msm_1280 Msm_1281
            MKA: MK0428
            AFU: AF0721
            HAL: VNG1093C
            HWA: HQ1656A(cbiX)
            RCI: RCIX2006(cbiX-1) RCIX98(cbiX-2)
            SSO: SSO0410
            STO: ST0383
            SAI: Saci_0830
STRUCTURES  PDB: 1TJN  2DJ5  
DBLINKS     IUBMB Enzyme Nomenclature: 4.99.1.3
            ExPASy - ENZYME nomenclature database: 4.99.1.3
            ExplorEnz - The Enzyme Database: 4.99.1.3
            ERGO genome analysis and discovery system: 4.99.1.3
            BRENDA, the Enzyme Database: 4.99.1.3
///
ENTRY       EC 4.99.1.4                 Enzyme
NAME        sirohydrochlorin ferrochelatase;
            CysG;
            Met8P;
            SirB;
            sirohydrochlorin ferro-lyase (incorrect)
CLASS       Lyases;
            Other lyases;
            Sole sub-subclass for lyases that do not belong in the other
            subclasses
SYSNAME     siroheme ferro-lyase (sirohydrochlorin-forming)
REACTION    siroheme + 2 H+ = sirohydrochlorin + Fe2+ [RN:R02864]
ALL_REAC    R02864
SUBSTRATE   siroheme [CPD:C00748];
            H+ [CPD:C00080]
PRODUCT     sirohydrochlorin [CPD:C05778];
            Fe2+ [CPD:C14818]
COMMENT     This enzyme catalyses the third of three steps leading to the
            formation of siroheme from uroporphyrinogen III. The first step
            involves the donation of two S-adenosyl-L-methionine-derived methyl
            groups to carbons 2 and 7 of uroporphyrinogen III to form
            precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and
            the second step involves an NAD+-dependent dehydrogenation to form
            sirohydrochlorin from precorrin-2 (EC 1.3.1.76, precorrin-2
            dehydrogenase). In Saccharomyces cerevisiae, the last two steps are
            carried out by a single bifunctional enzyme, Met8p. In some
            bacteria, steps 1-3 are catalysed by a single multifunctional
            protein called CysG, whereas in Bacillus megaterium, three separate
            enzymes carry out each of the steps, with SirB being responsible for
            the above reaction.
REFERENCE   1  [PMID:11980703]
  AUTHORS   Schubert HL, Raux E, Brindley AA, Leech HK, Wilson KS, Hill CP,
            Warren MJ.
  TITLE     The structure of Saccharomyces cerevisiae Met8p, a bifunctional
            dehydrogenase and ferrochelatase.
  JOURNAL   EMBO. J. 21 (2002) 2068-75.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:12195810]
  AUTHORS   Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
  TITLE     The biosynthesis of adenosylcobalamin (vitamin B12).
  JOURNAL   Nat. Prod. Rep. 19 (2002) 390-412.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], Salmonella enterica
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K02304  sirohydrochlorin ferrochelatase
            KO: K03794  sirohydrochlorin ferrochelatase
GENES       CME: CMB055C
            SCE: YBR213W(MET8)
            AGO: AGOS_AAR152W
            CAL: CaO19_6780(CaO19.6780)
            CGR: CAGL0K06677g
            SPO: SPAC4D7.06c
            ANI: AN6710.2
            AFM: AFUA_7G05680
            AOR: AO090005000430
            CNE: CNF00750
            UMA: UM00458.1
            ECO: b3368(cysG)
            ECJ: JW3331(cysG)
            ECE: Z4729(cysG)
            ECS: ECs4219
            ECC: c4144(cysG)
            ECI: UTI89_C3872(cysG)
            ECP: ECP_3459
            ECV: APECO1_3088(cysG)
            ECW: EcE24377A_3838(cysG)
            ECX: EcHS_A3564(cysG)
            STY: STY4319(cysG)
            STT: t4028(cysG)
            SPT: SPA3343(cysG)
            SEC: SC3411(cysG)
            STM: STM3477(cysG)
            YPE: YPO0158(cysG) YPO3367(cysG)
            YPK: y3941(cysG)
            YPM: YP_0160(cysG1)
            YPA: YPA_2776 YPA_3311
            YPN: YPN_0726 YPN_3907
            YPS: YPTB0764(cysG) YPTB3743(cysG)
            YPI: YpsIP31758_3305(cysG2) YpsIP31758_3959(cysG1)
            SFL: SF3387(cysG)
            SFX: S4376(cysG)
            SFV: SFV_3374(cysG)
            SSN: SSON_3499(cysG)
            SBO: SBO_3350(cysG)
            SDY: SDY_3530(cysG)
            ECA: ECA3544(cysG1) ECA4081(cysG2)
            PLU: plu0708(cysG)
            BUC: BU425(cysG)
            SGL: SG0520
            BFL: Bfl161(cysG)
            BPN: BPEN_166(cysG)
            MSU: MS1254(cysG)
            XFA: XF0832
            XFT: PD1840(cysG)
            XCC: XCC2003(cysG) XCC3181(cysG)
            XCB: XC_0983 XC_2181
            XCV: XCV2089 XCV3458(cysG)
            XAC: XAC2159(cysG) XAC3340(cysG)
            XOO: XOO3102(cysG) XOO3408(cysG)
            XOM: XOO_2947(XOO2947) XOO_3208(XOO3208)
            VCH: VC1363
            VVU: VV1_2702
            VVY: VV1558
            VPA: VP1619
            VFI: VF1531
            PPR: PBPRA1425 PBPRA2524 PBPRA3312 PBPRB0870(cobA2)
            PAE: PA2611(cysG)
            PPU: PP_3999(cobA-2)
            PST: PSPTO_3344(cysG)
            PSB: Psyr_3174
            PSP: PSPPH_3088(cysG)
            PFL: PFL_3875
            PFO: Pfl_3581
            PEN: PSEEN2217(cysG)
            PAR: Psyc_1065(cysG)
            ACI: ACIAD2934(cysG)
            SON: SO_3108
            SDN: Sden_3717
            SHN: Shewana3_1441
            PHA: PSHAa0213(cysG)
            PAT: Patl_0417
            MCA: MCA2089(cysG)
            TCX: Tcr_1160
            NOC: Noc_0863
            AEH: Mlg_1679
            HCH: HCH_02450(cysG)
            ABO: ABO_1295(cysG)
            AHA: AHA_2578 AHA_3568 AHA_4121
            BCI: BCI_0215(cysG)
            VOK: COSY_0254(cysG)
            NME: NMB1156 NMB1194
            NMA: NMA1367(cysG)
            CVI: CV_0813(cobA2)
            BPE: BP1055(cysG)
            BPA: BPP1151(cysG)
            BBR: BB1367(cysG)
            POL: Bpro_2765
            NEU: NE0532(cysG)
            NET: Neut_1002
            NMU: Nmul_A2313
            TBD: Tbd_2471
            MFA: Mfla_0652
            WSU: WS1003(cysG)
            DVU: DVU1463
            DDE: Dde_2023
            LIP: LI0320(cysG)
            ADE: Adeh_3154
            SAT: SYN_02276
            SFU: Sfum_1588
            MLO: mll3232
            MES: Meso_3989
            SME: SMc01053(cysG)
            ATU: Atu1454(cysG) Atu3899(cysG)
            ATC: AGR_C_2683 AGR_L_1897
            RET: RHE_CH01958(cysG)
            RLE: RL2288(cysG2)
            BME: BMEI1768
            BMF: BAB1_0179(cysG)
            BMS: BR0179(cysG)
            BMB: BruAb1_0175(cysG)
            BJA: blr1477
            BRA: BRADO1065(cysG)
            BBT: BBta_6982(cysG)
            RPA: RPA4215(cysG)
            RPB: RPB_1399
            RPC: RPC_4015
            RPD: RPD_1379
            RPE: RPE_1763
            NWI: Nwi_2762
            CCR: CC_0024
            RDE: RD1_2964(cysG) RD1_4164(cysG)
            MMR: Mmar10_0347
            HNE: HNE_0322(cysG)
            GOX: GOX2065
            GBE: GbCGDNIH1_0735
            BSU: BG13381(ylnE) BG13382(ylnF)
            BHA: BH1497
            BAN: BA1447 BA2142
            BAR: GBAA1447 GBAA2142
            BAA: BA_1968 BA_2638
            BAT: BAS1337 BAS1993
            BCE: BC1428 BC2132
            BCA: BCE_1551
            BCZ: BCZK1311(cysG) BCZK1945
            BTK: BT9727_1310(cysG) BT9727_1966
            BLI: BL02289(sirA)
            BLD: BLi01784(ylnF)
            BAY: RBAM_015450(sirB)
            OIH: OB1657
            GKA: GK0404
            SAU: SA2412
            SAV: SAV2619
            SAM: MW2539
            SAR: SAR2697
            SAS: SAS2505
            SAC: SACOL2638
            SAB: SAB2493c
            SAA: SAUSA300_2553
            SAO: SAOUHSC_02945
            SEP: SE2177
            SER: SERP2188
            SHA: SH0417
            SSP: SSP2404
            LMO: lmo1141
            LMF: LMOf2365_1148
            LIN: lin1105
            LWE: lwe1099
            CAC: CAC0096(hemW)
            CPE: CPE1436
            CPR: CPR_1423
            CTC: CTC00726
            DSY: DSY2227(cysG)
            MTU: Rv2847c(cysG)
            MTC: MT2913(cysG)
            MBO: Mb2872c(cysG)
            MPA: MAP2916c(cysG2)
            MMC: Mmcs_2074
            NFA: nfa40770(cysG)
            SCO: SCO1553(SCL11.09c)
            SMA: SAV6796(cysG)
            TFU: Tfu_2221
            FAL: FRAAL1357(cysG)
            FNU: FN0539
            LIL: LA4217
            LIC: LIC13368(cysG)
            LBJ: LBJ_2838(cysG)
            LBL: LBL_0233(cysG)
            CTE: CT2239
            CCH: Cag_1943
            PLT: Plut_0049
            TTH: TTC0311
            TTJ: TTHA0670
            AAE: aq_1237(cysG)
            MJA: MJ0140
            MMP: MMP0089
            MAC: MA0576(cysG)
            MBA: Mbar_A1461
            MMA: MM_1740
            MBU: Mbur_1230
            MTH: MTH1013
            MKA: MK1495(cysG_1)
            AFU: AF1592
            HAL: VNG1775C
            HMA: rrnAC1709(hemX)
            HWA: HQ3335A(cysG)
            NPH: NP4500A(cysG1)
            TAC: Ta0652
            TVO: TVN0924
            APE: APE_1491.1
            STO: ST0211
            SAI: Saci_0776
            PAI: PAE0585
DBLINKS     IUBMB Enzyme Nomenclature: 4.99.1.4
            ExPASy - ENZYME nomenclature database: 4.99.1.4
            ExplorEnz - The Enzyme Database: 4.99.1.4
            ERGO genome analysis and discovery system: 4.99.1.4
            BRENDA, the Enzyme Database: 4.99.1.4
///
ENTRY       EC 4.99.1.5                 Enzyme
NAME        aliphatic aldoxime dehydratase;
            OxdA;
            aliphatic aldoxime hydro-lyase
CLASS       Lyases;
            Other lyases;
            Sole sub-subclass for lyases that do not belong in the other
            subclasses
SYSNAME     aliphatic aldoxime hydro-lyase (aliphatic-nitrile-forming)
REACTION    an aliphatic aldoxime = an aliphatic nitrile + H2O [RN:R07637]
ALL_REAC    R07637
SUBSTRATE   aliphatic aldoxime [CPD:C16073]
PRODUCT     aliphatic nitrile [CPD:C16072];
            H2O [CPD:C00001]
COMMENT     The enzyme from Pseudomonas chlororaphis contains Ca2+ and protoheme
            IX, the iron of which must be in the form Fe(II) for activity. The
            enzyme exhibits a strong preference for aliphatic aldoximes, such as
            butyraldoxime and acetaldoxime, over aromatic aldoximes, such as
            pyridine-2-aldoxime, which is a poor substrate. No activity was
            found with the aromatic aldoximes benzaldoxime and
            pyridine-4-aldoxime.
REFERENCE   1  [PMID:12773527]
  AUTHORS   Oinuma K, Hashimoto Y, Konishi K, Goda M, Noguchi T, Higashibata H,
            Kobayashi M.
  TITLE     Novel aldoxime dehydratase involved in carbon-nitrogen triple bond
            synthesis of Pseudomonas chlororaphis B23. Sequencing, gene
            expression, purification, and characterization.
  JOURNAL   J. Biol. Chem. 278 (2003) 29600-8.
  ORGANISM  Pseudomonas chlororaphis
REFERENCE   2  [PMID:14556637]
  AUTHORS   Xie SX, Kato Y, Komeda H, Yoshida S, Asano Y.
  TITLE     A gene cluster responsible for alkylaldoxime metabolism coexisting
            with nitrile hydratase and amidase in Rhodococcus globerulus A-4.
  JOURNAL   Biochemistry. 42 (2003) 12056-66.
  ORGANISM  Rhodococcus globerulus
REFERENCE   3  [PMID:16233624]
  AUTHORS   Kato Y, Yoshida S, Xie SX, Asano Y.
  TITLE     Aldoxime dehydratase co-existing with nitrile hydratase and amidase
            in the iron-type nitrile hydratase-producer Rhodococcus sp. N-771.
  JOURNAL   J. Biosci. Bioeng. 97 (2004) 250-9.
  ORGANISM  Rhodococcus sp.
GENES       AAU: AAur_1899(oxdA)
DBLINKS     IUBMB Enzyme Nomenclature: 4.99.1.5
            ExPASy - ENZYME nomenclature database: 4.99.1.5
            ExplorEnz - The Enzyme Database: 4.99.1.5
            ERGO genome analysis and discovery system: 4.99.1.5
            BRENDA, the Enzyme Database: 4.99.1.5
///
ENTRY       EC 4.99.1.6                 Enzyme
NAME        indoleacetaldoxime dehydratase;
            indoleacetaldoxime hydro-lyase;
            3-indoleacetaldoxime hydro-lyase;
            indole-3-acetaldoxime hydro-lyase;
            indole-3-acetaldehyde-oxime hydro-lyase;
            (indol-3-yl)acetaldehyde-oxime hydro-lyase
CLASS       Lyases;
            Other lyases;
            Sole sub-subclass for lyases that do not belong in the other
            subclasses
SYSNAME     (indol-3-yl)acetaldehyde-oxime hydro-lyase
            [(indol-3-yl)acetonitrile-forming]
REACTION    (indol-3-yl)acetaldehyde oxime = (indol-3-yl)acetonitrile + H2O
            [RN:R04093]
ALL_REAC    R04093;
            (other) R02827
SUBSTRATE   (indol-3-yl)acetaldehyde oxime
PRODUCT     (indol-3-yl)acetonitrile [CPD:C02938];
            H2O [CPD:C00001]
REFERENCE   1  [PMID:14099566]
  AUTHORS   KUMAR SA, MAHADEVAN S.
  TITLE     3-INDOLEACETALDOXIME HYDRO-LYASE: A PYRIDOXAL-5'-PHOSPHATE ACTIVATED
            ENZYME.
  JOURNAL   Arch. Biochem. Biophys. 103 (1963) 516-8.
  ORGANISM  Gibberella fujikuroi
REFERENCE   2
  AUTHORS   Mahadevan, S.
  TITLE     Conversion of 3-indoleacetoxime to 3-indoleacetonitrile by plants.
  JOURNAL   Arch. Biochem. Biophys. 100 (1963) 557-558.
  ORGANISM  Aspergillus niger, Penicillium chrysogenum, Fusarium oxysporum,
            Gibberella fujikuroi
PATHWAY     PATH: map00460  Cyanoamino acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 4.99.1.6
            ExPASy - ENZYME nomenclature database: 4.99.1.6
            ExplorEnz - The Enzyme Database: 4.99.1.6
            ERGO genome analysis and discovery system: 4.99.1.6
            BRENDA, the Enzyme Database: 4.99.1.6
            CAS: 9024-27-5
///
ENTRY       EC 4.99.1.7                 Enzyme
NAME        phenylacetaldoxime dehydratase;
            PAOx dehydratase;
            arylacetaldoxime dehydratase;
            OxdB;
            (Z)-phenylacetaldehyde-oxime hydro-lyase
CLASS       Lyases;
            Other lyases;
            Sole sub-subclass for lyases that do not belong in the other
            subclasses
SYSNAME     (Z)-phenylacetaldehyde-oxime hydro-lyase
            (phenylacetonitrile-forming)
REACTION    (Z)-phenylacetaldehyde oxime = phenylacetonitrile + H2O [RN:R07638]
ALL_REAC    R07638
SUBSTRATE   (Z)-phenylacetaldehyde oxime [CPD:C16075]
PRODUCT     phenylacetonitrile [CPD:C16074];
            H2O [CPD:C00001]
COMMENT     The enzyme from Bacillus sp. OxB-1 contains protoheme IX, the iron
            of which must be in the form iron(II) for activity.
            (Z)-Phenylacetaldoxime binds to ferric heme (the iron(III) form) via
            the oxygen atom whereas it binds to the active ferrous form via the
            nitrogen atom. In this way, the oxidation state of the heme controls
            the coordination stucture of the substrate---heme complex, which
            regulates enzyme activity [2]. The enzyme is active towards several
            (Z)-arylacetaldoximes and (E/Z)-alkylaldoximes as well as towards
            arylalkylaldoximes such as 3-phenylpropionaldoxime and
            4-phenylbutyraldoxime. However, it is inactive with
            phenylacetaldoximes that have a substituent group at an alpha-site
            of an oxime group, for example, with (E/Z)-2-phenylpropionaldoxime
            and (E/Z)-mandelaldoxime. The activity of the enzyme is inhibited
            completely by the heavy-metal cations Cu+, Cu2+, Ag+ and Hg+ whereas
            Fe2+ and Sn2+ have an activatory effect.
REFERENCE   1  [PMID:10651646]
  AUTHORS   Kato Y, Nakamura K, Sakiyama H, Mayhew SG, Asano Y.
  TITLE     Novel heme-containing lyase, phenylacetaldoxime dehydratase from
            Bacillus sp. strain OxB-1: purification, characterization, and
            molecular cloning of the gene.
  JOURNAL   Biochemistry. 39 (2000) 800-9.
  ORGANISM  Bacillus sp.
REFERENCE   2  [PMID:15596434]
  AUTHORS   Kobayashi K, Yoshioka S, Kato Y, Asano Y, Aono S.
  TITLE     Regulation of aldoxime dehydratase activity by redox-dependent
            change in the coordination structure of the aldoxime-heme complex.
  JOURNAL   J. Biol. Chem. 280 (2005) 5486-90.
  ORGANISM  Bacillus sp.
PATHWAY     PATH: map00643  Styrene degradation
GENES       PPF: Pput_2724
            BBT: BBta_4765
            XAU: Xaut_1560
            SWI: Swit_0988
DBLINKS     IUBMB Enzyme Nomenclature: 4.99.1.7
            ExPASy - ENZYME nomenclature database: 4.99.1.7
            ExplorEnz - The Enzyme Database: 4.99.1.7
            ERGO genome analysis and discovery system: 4.99.1.7
            BRENDA, the Enzyme Database: 4.99.1.7
///
ENTRY       EC 4.99.1.-                 Enzyme
CLASS       Lyases;
            Other lyases
REACTION    (2-Aminoethyl)phosphonate + H2O2 <=> Ethanolamine + Orthophosphate
            [RN:R04248]
SUBSTRATE   (2-Aminoethyl)phosphonate [CPD:C03557];
            H2O2 [CPD:C00027]
PRODUCT     Ethanolamine [CPD:C00189];
            Orthophosphate [CPD:C00009]
///
ENTRY       EC 5.1.1.1                  Enzyme
NAME        alanine racemase;
            L-alanine racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     alanine racemase
REACTION    L-alanine = D-alanine [RN:R00401]
ALL_REAC    R00401
SUBSTRATE   L-alanine [CPD:C00041]
PRODUCT     D-alanine [CPD:C00133]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
INHIBITOR   3-Fluoro-D-alanine [CPD:C02638]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:13159289]
  AUTHORS   MARR AG, WILSON PW.
  TITLE     The alanine racemase of Brucella abortus.
  JOURNAL   Arch. Biochem. Biophys. 49 (1954) 424-33.
  ORGANISM  Streptococcus faecalis
REFERENCE   2
  AUTHORS   Wood, W.A.
  TITLE     Amino acid racemases.
  JOURNAL   Methods Enzymol. 2 (1955) 212-217.
  ORGANISM  Streptococcus faecalis
REFERENCE   3  [PMID:14841188]
  AUTHORS   WOOD WA, GUNSALUS IC.
  TITLE     D-Alanine formation; a racemase in Streptococcus faecalis.
  JOURNAL   J. Biol. Chem. 190 (1951) 403-16.
  ORGANISM  Streptococcus faecalis
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
            PATH: map00473  D-Alanine metabolism
ORTHOLOGY   KO: K01775  alanine racemase
GENES       SPO: SPBC359.02 SPCC965.08c
            TCR: 508303.10 511179.150
            ECO: b1190(dadX) b4053(alr)
            ECJ: JW1179(dadX) JW4013(alr)
            ECE: Z1953(dadX) Z5651(alr)
            ECS: ECs1685 ECs5035
            ECC: c1639(alr) c5028(alr)
            ECI: UTI89_C1376(dadX) UTI89_C4626(alr)
            ECP: ECP_1233 ECP_4270
            ECV: APECO1_2414(alr) APECO1_302(dadX)
            ECW: EcE24377A_1335(alr1) EcE24377A_4605(alr2)
            ECX: EcHS_A1293 EcHS_A4293
            STY: STY1930(dadX) STY3763 STY4443(alr)
            STT: t1075(dadX) t3513 t4153(alr)
            SPT: SPA1071(dadX) SPA3949 SPA4064(alr)
            SEC: SC1795(dadX) SC4126(alr)
            STM: STM1802(dadX) STM4247(alr)
            YPE: YPO0321(alr) YPO1687
            YPK: y0578(alr) y1849
            YPM: YP_0476(alr)
            YPA: YPA_1835 YPA_3964
            YPN: YPN_1944 YPN_3349
            YPP: YPDSF_1761 YPDSF_3651
            YPS: YPTB0376(alr) YPTB2392(alr)
            YPI: YpsIP31758_1652(alr1) YpsIP31758_3764(alr2)
            YEN: YE2280(dadB)
            SFL: SF1179(dadX) SF4152(alr)
            SFX: S1267(dadX) S3578(alr)
            SFV: SFV_1197(dadX) SFV_4160(alr)
            SSN: SSON_1182(dadX) SSON_4233(alr)
            SBO: SBO_4064(alr)
            SDY: SDY_4521(alr)
            ECA: ECA3665(alr)
            PLU: plu2560(dadX) plu4358(alr)
            WBR: WGLp376(dadX)
            SGL: SG1342
            ENT: Ent638_0257 Ent638_2362
            SPE: Spro_0577 Spro_1562 Spro_2271 Spro_2679 Spro_2745 Spro_3616
                 Spro_3832 Spro_3834 Spro_4207 Spro_4283 Spro_4448 Spro_4466
                 Spro_4573 Spro_4592 Spro_4790
            HIN: HI1575(alr)
            HIT: NTHI1476(alr)
            HIP: CGSHiEE_05465(alr)
            HIQ: CGSHiGG_00040(alr)
            HDU: HD0624(alr)
            HSO: HS_0939(alr)
            PMU: PM0413(alr)
            MSU: MS1182(alr)
            APL: APL_0252(alr)
            ASU: Asuc_0357 Asuc_1426
            XFA: XF0852
            XFT: PD1823(alr)
            XCC: XCC3647(alr)
            XCB: XC_3718
            XCV: XCV3808(alr)
            XAC: XAC3687(alr)
            XOO: XOO0694(alr)
            XOM: XOO_0631(XOO0631)
            VCH: VC0372 VC1312
            VCO: VC0395_A2783(alr)
            VVU: VV1_1393 VV2_0478
            VVY: VV2978 VVA1029
            VPA: VP2734 VP2848 VPA1001
            VFI: VF0302(alr) VF0735(alr)
            PPR: PBPRA3330(alr) PBPRA3385(alr) PBPRB1952(alr)
            PAE: PA4930(alr) PA5302(dadX)
            PAU: PA14_65110(alr) PA14_69990(dadX)
            PAP: PSPA7_5657(alr2) PSPA7_6076(alr1)
            PPU: PP_3722 PP_5269(dadX)
            PPF: Pput_2041 Pput_3233 Pput_5179
            PST: PSPTO_0103(dadX)
            PSB: Psyr_0237(alr)
            PSP: PSPPH_0225(alr)
            PFL: PFL_6036(alr)
            PFO: Pfl_5524
            PEN: PSEEN5415(dadX)
            PMY: Pmen_0247 Pmen_0650 Pmen_0785
            PAR: Psyc_0958(alr)
            PCR: Pcryo_1460
            PRW: PsycPRwf_0782
            ACI: ACIAD0116(dadX) ACIAD2434(alr)
            ACB: A1S_0096
            SON: SO_3916(alr)
            SDN: Sden_0522
            SFR: Sfri_3345
            SAZ: Sama_3057
            SBL: Sbal_3637
            SBM: Shew185_0717 Shew185_1181 Shew185_2345
            SLO: Shew_3277
            SPC: Sputcn32_0759
            SSE: Ssed_0763 Ssed_1207
            SPL: Spea_0519 Spea_1096 Spea_3580
            SHE: Shewmr4_3247
            SHM: Shewmr7_0693
            SHN: Shewana3_0714
            SHW: Sputw3181_3416
            ILO: IL0040(dadX)
            CPS: CPS_2882(alr)
            PHA: PSHAa2434(alr)
            PAT: Patl_4025
            SDE: Sde_0914
            PIN: Ping_0191 Ping_2084
            MAQ: Maqu_2381
            CBU: CBU_0869(alr)
            CBD: COXBU7E912_0932(alr)
            LPN: lpg0739
            LPF: lpl0775
            LPP: lpp0804
            MCA: MCA1734(alr)
            FTU: FTT0573(alr)
            FTF: FTF0573(alr)
            FTW: FTW_1439(alr)
            FTL: FTL_1338
            FTH: FTH_1303(alr)
            FTA: FTA_1414(alr)
            FTN: FTN_0746(alr)
            TCX: Tcr_1359
            NOC: Noc_0224
            AEH: Mlg_0588
            HHA: Hhal_0652
            HCH: HCH_01715(alr)
            CSA: Csal_2629
            ABO: ABO_2186(dadX)
            MMW: Mmwyl1_0185 Mmwyl1_3629
            AHA: AHA_1015(alr-1) AHA_2536(alr-2) AHA_2607(alr-3)
            DNO: DNO_0325(alr)
            RMA: Rmag_0668
            VOK: COSY_0613(alr)
            NME: NMB1651
            NMA: NMA1906(alr)
            NMC: NMC1567(alr)
            NGO: NGO1295
            CVI: CV_1915(alr) CV_3793(dadB)
            RSO: RSc1371(dadX)
            REU: Reut_A1934(alr) Reut_A2530
            REH: H16_A2113(dadX)
            RME: Rmet_1400
            BMA: BMA1575(alr)
            BMV: BMASAVP1_A2078(alr)
            BML: BMA10299_A3234(alr)
            BMN: BMA10247_1350(alr)
            BXE: Bxe_A1660 Bxe_B0373
            BVI: Bcep1808_1945 Bcep1808_4643 Bcep1808_6675
            BUR: Bcep18194_A5348(alr) Bcep18194_B1965(alr)
            BCN: Bcen_4288 Bcen_6038
            BCH: Bcen2424_2039 Bcen2424_4078
            BAM: Bamb_2071 Bamb_3490 Bamb_6514
            BPS: BPSL2179(dadX) BPSS0711(dadX)
            BPM: BURPS1710b_2603(alr) BURPS1710b_A2286(alr)
            BPL: BURPS1106A_1987(arcA) BURPS1106A_2514(alr)
                 BURPS1106A_A0961(alr)
            BPD: BURPS668_1968(arcA) BURPS668_2458(alr) BURPS668_A1047(alr)
            BTE: BTH_I2007(alr-1) BTH_II1715(alr-2)
            PNU: Pnuc_0919
            BPE: BP1221(dadX) BP2228(alr)
            BPA: BPP1835(dadX) BPP2247(alr)
            BBR: BB1644(alr) BB3271(dadX)
            RFR: Rfer_0488
            POL: Bpro_0193
            PNA: Pnap_0131
            AAV: Aave_0253
            AJS: Ajs_0176
            VEI: Veis_4337
            MPT: Mpe_A3562
            HAR: HEAR1759(dadX)
            MMS: mma_1525
            NEU: NE1417(dadX)
            NET: Neut_1531
            NMU: Nmul_A2115
            EBA: ebA3534(dadX)
            AZO: azo3925(alr)
            DAR: Daro_1986
            TBD: Tbd_2100
            MFA: Mfla_1331
            HPY: HP0941(alr)
            HPJ: jhp0876(alr)
            HPA: HPAG1_0924
            HHE: HH0466(alr) HH1516
            HAC: Hac_1313
            WSU: WS0701(alr)
            TDN: Tmden_0379
            CJE: Cj0905c(alr)
            CJR: CJE0984(alr)
            CJJ: CJJ81176_0914(alr)
            CJU: C8J_0842(alr)
            CJD: JJD26997_0907(alr)
            CFF: CFF8240_1580(alr)
            CCV: CCV52592_1338(alr)
            CHA: CHAB381_0420
            CCO: CCC13826_0875(alr)
            ABU: Abu_0786(alr)
            NIS: NIS_0355
            SUN: SUN_2123
            GSU: GSU0606(alr)
            GME: Gmet_2908
            GUR: Gura_3850
            PCA: Pcar_2234
            PPD: Ppro_2594
            DVU: DVU0955(alr)
            DVL: Dvul_2031
            DDE: Dde_1547
            LIP: LI0034(alr)
            BBA: Bd3124(alr)
            DPS: DP2753
            ADE: Adeh_3427
            AFW: Anae109_3487
            MXA: MXAN_7160(alr)
            SAT: SYN_01482
            SFU: Sfum_0562
            RPR: RP095(alr)
            RTY: RT0042(alr)
            RCO: RC0128(alr)
            RFE: RF_0079(alr)
            RBE: RBE_1339(alr)
            RAK: A1C_00720(alr)
            RBO: A1I_00855(alr)
            RCM: A1E_00470(alr)
            RRI: A1G_00750(alr)
            MLO: mll3997 mll6211 mlr9371
            MES: Meso_0396 Meso_0986
            PLA: Plav_3482
            SME: SMc00557(alr)
            SMD: Smed_0291 Smed_0730 Smed_2316 Smed_2764 Smed_3813 Smed_4116
                 Smed_4158 Smed_4247 Smed_4264 Smed_5456
            ATU: Atu1080(alr) Atu3292(alr)
            ATC: AGR_C_1996 AGR_L_3051
            RET: RHE_CH01432(alr) RHE_PF00437(dadX)
            RLE: RL1550 pRL120416(dadX)
            BME: BMEII0374
            BMF: BAB2_0312
            BMS: BRA0923(alr)
            BMB: BruAb2_0310(alr)
            BOV: BOV_A0865(alr)
            OAN: Oant_0274 Oant_0870 Oant_1376 Oant_1445 Oant_2762 Oant_2939
            BJA: bll4070(alr)
            BRA: BRADO3301
            BBT: BBta_3807
            RPA: RPA3085
            RPB: RPB_1502 RPB_2457
            RPC: RPC_2289
            RPD: RPD_2992
            RPE: RPE_3334
            NWI: Nwi_2014
            NHA: Nham_2290
            BHE: BH12810(alr)
            BQU: BQ10100(alr)
            BBK: BARBAKC583_1093(alr)
            XAU: Xaut_2153 Xaut_2403 Xaut_4738
            CCR: CC_1661
            SIL: SPO2670(alr)
            SIT: TM1040_1779
            RSP: RSP_2460(alr)
            RSH: Rsph17029_1123
            RSQ: Rsph17025_0609 Rsph17025_1068 Rsph17025_2582 Rsph17025_2680
            JAN: Jann_1739
            RDE: RD1_3240(alr)
            PDE: Pden_3689
            MMR: Mmar10_1208
            HNE: HNE_0725(alr1) HNE_2417(alr2)
            ZMO: ZMO1592(alr)
            NAR: Saro_1952
            SAL: Sala_1227
            SWI: Swit_0013 Swit_0807
            ELI: ELI_06095
            GOX: GOX1193 GOX1195 GOX2061
            GBE: GbCGDNIH1_2218
            ACR: Acry_0186 Acry_1589 Acry_2432 Acry_2871
            RRU: Rru_A0409
            MAG: amb2095
            MGM: Mmc1_0259
            ABA: Acid345_4221
            SUS: Acid_7398
            BSU: BG10950(alr) BG12267(yncD)
            BHA: BH0520
            BAN: BA0252(dal-1) BA2079(dal-2)
            BAR: GBAA0252(dal-1) GBAA2079(dal-2)
            BAA: BA_0822 BA_2575
            BAT: BAS0238 BAS1932
            BCE: BC0264 BC2063
            BCA: BCE_0272(dal) BCE_2163(alr)
            BCZ: BCZK0226(alr) BCZK1884(dal)
            BCY: Bcer98_0238 Bcer98_0837 Bcer98_1563 Bcer98_2711 Bcer98_3082
            BTK: BT9727_0224(alr) BT9727_1894(dal)
            BTL: BALH_0237(alr)
            BLI: BL02201(dal) BL02566(alr2)
            BLD: BLi00551(alr) BLi03274(yncD)
            BCL: ABC0807(dal)
            BAY: RBAM_004980
            BPU: BPUM_0437 BPUM_0979 BPUM_1146
            OIH: OB3149 OB3226
            GKA: GK0231
            GTN: GTNG_0205
            SAU: SA1231 SA1874(alr)
            SAV: SAV1399 SAV2070(alr)
            SAM: MW1287 MW1994(alr)
            SAR: SAR1411(dal) SAR2158(alr)
            SAS: SAS1340 SAS1975
            SAC: SACOL1434 SACOL2060(alr)
            SAB: SAB1254(alr) SAB1955c(alr)
            SAA: SAUSA300_1292(alr2) SAUSA300_2027(alr)
            SAO: SAOUHSC_01400 SAOUHSC_02305
            SAJ: SaurJH9_1460 SaurJH9_1565 SaurJH9_2107
            SAH: SaurJH1_1489 SaurJH1_1596 SaurJH1_2145
            SEP: SE1079 SE1674
            SER: SERP0969 SERP1683(alr)
            SHA: SH0961(alr1) SH1512(alr2)
            SSP: SSP0807 SSP1351
            LMO: lmo0886(dal)
            LMF: LMOf2365_0905(alr)
            LIN: lin0885
            LWE: lwe0868(dal)
            LLA: L0103(dal)
            LLC: LACR_0910
            LLM: llmg_1704(alr)
            SPY: SPy_1802(alr)
            SPZ: M5005_Spy_1532(alr)
            SPM: spyM18_1871
            SPG: SpyM3_1563(alr)
            SPS: SPs0304
            SPH: MGAS10270_Spy1600(acpS)
            SPI: MGAS10750_Spy1591(acpS)
            SPJ: MGAS2096_Spy1559(acpS)
            SPK: MGAS9429_Spy1536(acpS)
            SPF: SpyM50314(alr)
            SPA: M6_Spy1524(alr)
            SPB: M28_Spy1522(alr)
            SPN: SP_1698
            SPR: spr1540(alr)
            SPD: SPD_1508(alr)
            SAG: SAG1684(alr)
            SAN: gbs1728
            SAK: SAK_1696(alr)
            SMU: SMU.1834(alr)
            STC: str1726(alr)
            STL: stu1726(alr)
            STE: STER_1701
            SSA: SSA_0548(alr)
            SSU: SSU05_1812
            SSV: SSU98_1816
            SGO: SGO_0418(alr)
            LPL: lp_0523(alr)
            LJO: LJ0272
            LAC: LBA0269
            LSA: LSA1613(alr)
            LSL: LSL_0358(alr)
            LDB: Ldb0360(alr)
            LBU: LBUL_0315
            LBR: LVIS_0508
            LCA: LSEI_2560
            LGA: LGAS_0267
            LRE: Lreu_0255 Lreu_0550 Lreu_1286
            PPE: PEPE_1559
            EFA: EF0849(alr)
            OOE: OEOE_0162 OEOE_1641
            LME: LEUM_0422 LEUM_1941
            STH: STH2936
            CAC: CAC0492 CAC3331
            CPE: CPE0868 CPE1061(alr)
            CPF: CPF_0861(alr) CPF_1317
            CPR: CPR_0852(alr) CPR_1133
            CTC: CTC02513(alr)
            CNO: NT01CX_1264
            CTH: Cthe_2697
            CDF: CD3463(alr)
            CBO: CBO0276 CBO1660(alr) CBO3397(alr)
            CBA: CLB_0320(alr-1) CLB_1676(alr-2) CLB_3454(alr-3)
            CBH: CLC_0335(alr-1) CLC_1685(alr-2) CLC_3341(alr-3)
            CBF: CLI_1734(alr-1) CLI_3582(alr-2)
            CBE: Cbei_0047 Cbei_0234 Cbei_0731 Cbei_0863 Cbei_1831 Cbei_2457
                 Cbei_2758 Cbei_4113 Cbei_4148 Cbei_4422
            CKL: CKL_3581(alr)
            AMT: Amet_0455 Amet_0902 Amet_1065 Amet_4145
            CHY: CHY_0667(alr)
            DSY: DSY4022 DSY4942
            DRM: Dred_2865
            PTH: PTH_0660(alr)
            SWO: Swol_1882 Swol_2416
            CSC: Csac_0430 Csac_0443 Csac_0797 Csac_1041 Csac_1171 Csac_1228
                 Csac_1338 Csac_2494
            TTE: TTE1207(alr) TTE2168(alr2)
            MTA: Moth_2167 Moth_2407
            MTU: Rv3423c(alr)
            MTC: MT3532(alr)
            MBO: Mb3457c(alr)
            MBB: BCG_3493c(alr)
            MLE: ML0375(alr)
            MPA: MAP4258(alr)
            MAV: MAV_4372(alr)
            MSM: MSMEG_1575(alr)
            MVA: Mvan_1484
            MGI: Mflv_4934
            MMC: Mmcs_1146
            MKM: Mkms_1163
            MJL: Mjls_1173
            CGL: NCgl0563(alr)
            CGB: cg0681(alr)
            CEF: CE0593(alr)
            CDI: DIP0568
            CJK: jk1734(alr)
            NFA: nfa8790(alr)
            RHA: RHA1_ro06180(alr)
            SCO: SCO4745(alr)
            SMA: SAV4967(alr)
            TWH: TWT495 TWT496(alr)
            TWS: TW266(alr1) TW267(alr2)
            LXX: Lxx10330(alr) Lxx10340(alr) Lxx19950(alr)
            CMI: CMM_2573(alrA2) CMM_2574(alrA1)
            ART: Arth_1108 Arth_2896
            AAU: AAur_1219(alr) AAur_2887(alr)
            PAC: PPA2285
            NCA: Noca_0900 Noca_3485
            TFU: Tfu_2606
            FRA: Francci3_0622
            FAL: FRAAL1122
            ACE: Acel_0355
            KRA: Krad_0032 Krad_0549 Krad_0581 Krad_0727 Krad_0775 Krad_1038
                 Krad_2497 Krad_2584 Krad_3482 Krad_3965 Krad_4014
            SEN: SACE_6764(alr)
            STP: Strop_0802 Strop_3259 Strop_3857
            BLO: BL1149(alr)
            BAD: BAD_0496(alr)
            RXY: Rxyl_0804
            FNU: FN0406 FN0491
            PCU: pc0631(alr)
            BGA: BG0158(alr)
            BAF: BAPKO_0161(alr)
            TPA: TP0681
            TDE: TDE1095(alr)
            LIL: LB317
            LIC: LIC20241(alr)
            LBJ: LBJ_4232(alr)
            LBL: LBL_4246(alr)
            SYN: slr0827(alr)
            SYW: SYNW2098(alr)
            SYC: syc1896_d(alr)
            SYF: Synpcc7942_2201
            SYD: Syncc9605_0345(alr)
            SYE: Syncc9902_1986(alr)
            SYG: sync_0406(alr)
            SYR: SynRCC307_2147(alr)
            CYA: CYA_1462(alr)
            CYB: CYB_0655(alr)
            TEL: tll0460
            GVI: glr3818
            ANA: alr2458
            AVA: Ava_0390(alr)
            PMA: Pro1681(alr)
            PMM: PMM1527(alr)
            PMT: PMT1763(alr)
            PMN: PMN2A_1098(alr)
            PMI: PMT9312_1620
            PMB: A9601_17351(alr)
            PMC: P9515_17091(alr)
            PMF: P9303_23341(alr)
            PMG: P9301_17191(alr)
            PMH: P9215_17991
            PME: NATL1_19731(alr)
            TER: Tery_1583
            BTH: BT_4101
            BFR: BF0892
            BFS: BF0816
            PGI: PG1097
            SRU: SRU_0573(alr)
            CHU: CHU_3724(alr)
            GFO: GFO_3353(alr)
            FJO: Fjoh_1259 Fjoh_1990
            FPS: FP1064(mur)
            CTE: CT1922(alr)
            CCH: Cag_1635
            CPH: Cpha266_2284
            PVI: Cvib_0345
            PLT: Plut_0280
            RRS: RoseRS_0524 RoseRS_2559
            RCA: Rcas_0512 Rcas_0907 Rcas_1277 Rcas_1849
            DRA: DR_1086
            DGE: Dgeo_1380
            TTH: TTC1944
            TTJ: TTHA0062
            AAE: aq_1827(alr)
            TPT: Tpet_0941
            TME: Tmel_1026
            FNO: Fnod_0285 Fnod_0418 Fnod_1025 Fnod_1559 Fnod_1601
            MMP: MMP1512(alr)
            MMQ: MmarC5_0063
            MMZ: MmarC7_0758
            MVN: Mevan_0824
STRUCTURES  PDB: 1BD0  1EPV  1FTX  1L6F  1L6G  1NIU  1RCQ  1SFT  1VFH  1VFS  
                 1VFT  1XFC  1XQK  1XQL  2DY3  2SFP  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.1
            ExPASy - ENZYME nomenclature database: 5.1.1.1
            ExplorEnz - The Enzyme Database: 5.1.1.1
            ERGO genome analysis and discovery system: 5.1.1.1
            BRENDA, the Enzyme Database: 5.1.1.1
            CAS: 9024-06-0
///
ENTRY       EC 5.1.1.2                  Enzyme
NAME        methionine racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     methionine racemase
REACTION    L-methionine = D-methionine [RN:R00655]
ALL_REAC    R00655
SUBSTRATE   L-methionine [CPD:C00073]
PRODUCT     D-methionine [CPD:C00855]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1
  AUTHORS   Kallio, R.E. and Larson, A.D.
  TITLE     Methionine degradation by a species of Pseudomonas.
  JOURNAL   In: McElroy, W.D. and Glass, H.B. (Eds.), A Symposium on Amino Acid
            Metabolism, A Symposium on Amino Acid Metabolism, Baltimore, 1955,
            p. 616-634.
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.2
            ExPASy - ENZYME nomenclature database: 5.1.1.2
            ExplorEnz - The Enzyme Database: 5.1.1.2
            ERGO genome analysis and discovery system: 5.1.1.2
            BRENDA, the Enzyme Database: 5.1.1.2
            CAS: 9024-07-1
///
ENTRY       EC 5.1.1.3                  Enzyme
NAME        glutamate racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     glutamate racemase
REACTION    L-glutamate = D-glutamate [RN:R00260]
ALL_REAC    R00260
SUBSTRATE   L-glutamate [CPD:C00025]
PRODUCT     D-glutamate [CPD:C00217]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:13828348]
  AUTHORS   GLASER L.
  TITLE     Glutamic acid racemase from Lactobacillus arabinosus.
  JOURNAL   J. Biol. Chem. 235 (1960) 2095-8.
  ORGANISM  Lactobacillus arabinosus
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00471  D-Glutamine and D-glutamate metabolism
ORTHOLOGY   KO: K01776  glutamate racemase
GENES       ECO: b3967(murI)
            ECJ: JW5550(murI)
            ECE: Z5528(murI)
            ECS: ECs4898
            ECC: c4930(murI)
            ECI: UTI89_C4562(murI)
            ECP: ECP_4184
            ECV: APECO1_2496(murI)
            ECW: EcE24377A_4508(murI)
            ECX: EcHS_A4201
            STY: STY3743(murI)
            STT: t3494(murI)
            SPT: SPA3969(murI)
            SEC: SC4020(murI)
            STM: STM4131(murI)
            YPE: YPO3909(murI)
            YPK: y0326(murI)
            YPM: YP_3139(murI)
            YPA: YPA_0113
            YPN: YPN_0058
            YPP: YPDSF_3521
            YPS: YPTB0126(murI)
            YPI: YpsIP31758_0143(murI)
            SFL: SF2500 SF4049(murI)
            SFX: S3695(murI)
            SFV: SFV_2500 SFV_4040(murI)
            SSN: SSON_4140(murI)
            SBO: SBO_3986(murI)
            SDY: SDY_3761(murI)
            ECA: ECA4237(murI)
            PLU: plu4734(murI)
            BUC: BU554(murI)
            BAS: BUsg536(murI)
            BAB: bbp502(murI)
            WBR: WGLp133(murI)
            SGL: SG2153
            ENT: Ent638_4019
            SPE: Spro_4769
            BPN: BPEN_618(murI)
            HIT: NTHI2050(murI)
            HIP: CGSHiEE_03340
            HIQ: CGSHiGG_02450
            HDU: HD1906(murI)
            HSO: HS_1453(murI)
            PMU: PM0917(murI)
            MSU: MS1734(murI)
            APL: APL_1841(murI)
            ASU: Asuc_0854
            VCH: VC0158
            VCO: VC0395_A2339(murI)
            VVU: VV1_1175
            VVY: VV0168
            VPA: VP2936
            VFI: VF2433
            PPR: PBPRA3462(murI)
            PAE: PA4662(murI)
            PAU: PA14_61660(murI)
            PAP: PSPA7_5311(murI)
            PPU: PP_0736(murI)
            PPF: Pput_0764
            PST: PSPTO_1112(murI)
            PSB: Psyr_0952
            PSP: PSPPH_1000(murI)
            PFL: PFL_5156(murI)
            PFO: Pfl_4745
            PEN: PSEEN0879(murI)
            PMY: Pmen_1063
            PAR: Psyc_1954
            PCR: Pcryo_2249
            PRW: PsycPRwf_0284
            ACI: ACIAD3257(murI)
            SON: SO_0207(murI)
            SDN: Sden_0232
            SFR: Sfri_0126
            SAZ: Sama_0194
            SBL: Sbal_4177
            SBM: Shew185_0177
            SLO: Shew_0139
            SPC: Sputcn32_3000 Sputcn32_3509
            SSE: Ssed_4337
            SPL: Spea_0165
            SHE: Shewmr4_0179
            SHM: Shewmr7_0174
            SHN: Shewana3_0180
            SHW: Sputw3181_0949 Sputw3181_3676
            ILO: IL0597(murI)
            CPS: CPS_1257(murI)
            PHA: PSHAa0252(murI)
            SDE: Sde_1613
            PIN: Ping_0629
            MAQ: Maqu_2226
            CBU: CBU_0298(murI)
            CBD: COXBU7E912_1783(murI)
            LPN: lpg2310(murI)
            LPF: lpl2229(murI)
            LPP: lpp2258(murI)
            MCA: MCA1276(murI)
            FTU: FTT1197c(murI)
            FTF: FTF1197c(murI)
            FTW: FTW_1244(murI)
            FTL: FTL_0747
            FTH: FTH_0749(murI)
            FTA: FTA_0789(murI)
            FTN: FTN_1174(murI)
            HCH: HCH_05080(murI)
            CSA: Csal_1338
            ABO: ABO_2364(murI)
            MMW: Mmwyl1_2156
            AHA: AHA_0075(murI)
            DNO: DNO_0005
            BCI: BCI_0153(murI)
            NME: NMB0458
            NMA: NMA2026(glr)
            NMC: NMC1692(glr)
            NGO: NGO1500
            CVI: CV_1203(murI)
            RSO: RSc1956(RS03530)
            REU: Reut_A2233
            REH: H16_A2529(murI)
            RME: Rmet_2274
            BMA: BMAA1799(murI)
            BMV: BMASAVP1_0796(murI)
            BML: BMA10299_1088(murI)
            BMN: BMA10247_A2060(murI)
            BXE: Bxe_A3138
            BVI: Bcep1808_2282
            BUR: Bcep18194_A5525 Bcep18194_B0672 Bcep18194_B0673
            BCN: Bcen_5881
            BCH: Bcen2424_2196
            BAM: Bamb_2235
            BPS: BPSS0370
            BPM: BURPS1710b_A1934(murI)
            BPL: BURPS1106A_A0524(murI)
            BPD: BURPS668_A0621(murI)
            BTE: BTH_II2022(murI)
            PNU: Pnuc_1140
            RFR: Rfer_2597
            POL: Bpro_2045
            PNA: Pnap_2884
            AAV: Aave_1488
            AJS: Ajs_2867
            VEI: Veis_3213
            MPT: Mpe_A1295
            HAR: HEAR0918(murI)
            MMS: mma_0879
            NEU: NE0449(murI)
            NET: Neut_1752
            NMU: Nmul_A1214
            EBA: ebA4456(murI)
            AZO: azo2755(murI)
            DAR: Daro_3114
            TBD: Tbd_1522
            MFA: Mfla_0624
            HPY: HP0549
            HPA: HPAG1_0527
            HHE: HH0024(murI)
            HAC: Hac_0876(murI)
            WSU: WS0809(murI)
            TDN: Tmden_1554
            CJE: Cj1652c(murI)
            CJR: CJE1824(murI)
            CJJ: CJJ81176_1643(murI)
            CJU: C8J_1554(murI)
            CJD: JJD26997_2013(murI)
            CFF: CFF8240_0590(murI)
            CCV: CCV52592_1992(murI)
            CCO: CCC13826_0084 CCC13826_1245(murI)
            ABU: Abu_0286(murI)
            NIS: NIS_1456
            SUN: SUN_1926
            GSU: GSU2923(murI)
            GME: Gmet_0547
            GUR: Gura_0487
            PCA: Pcar_2724
            PPD: Ppro_1411
            DVU: DVU0768(murI)
            DVL: Dvul_2202
            DDE: Dde_2743
            LIP: LI0867(murI)
            BBA: Bd1778(murI)
            DPS: DP0692
            ADE: Adeh_0664
            AFW: Anae109_0708
            MXA: MXAN_5751(murI)
            SAT: SYN_00222
            SFU: Sfum_3010 Sfum_3052
            MLO: mlr0039
            MES: Meso_1269
            PLA: Plav_0264
            SME: SMc00483(murI)
            SMD: Smed_1516
            ATU: Atu1867(murI)
            ATC: AGR_C_3425
            RET: RHE_CH02314(murI)
            RLE: RL2627(murI)
            BME: BMEI0795
            BMF: BAB1_1217(murI)
            BMS: BR1195(murI)
            BMB: BruAb1_1200(murI)
            BOV: BOV_1157(murI)
            OAN: Oant_1996
            BJA: blr5702(murI)
            BRA: BRADO2802(murI)
            BBT: BBta_5384(murI)
            RPA: RPA1592(murI)
            RPB: RPB_3694
            RPC: RPC_1606
            RPD: RPD_1768
            RPE: RPE_1635
            NWI: Nwi_1317
            NHA: Nham_1645
            BHE: BH08380(murI)
            BQU: BQ06200(murI)
            BBK: BARBAKC583_0827(murI)
            XAU: Xaut_3847
            CCR: CC_3703
            SIL: SPO1875(murI)
            SIT: TM1040_1122
            RSP: RSP_2947
            RSH: Rsph17029_1593
            RSQ: Rsph17025_0897
            JAN: Jann_2338
            RDE: RD1_3228(murI)
            PDE: Pden_3973
            HNE: HNE_2992(murI)
            ZMO: ZMO1197(murI)
            NAR: Saro_1799
            SAL: Sala_1207
            SWI: Swit_3824
            ELI: ELI_04790
            GOX: GOX1997
            GBE: GbCGDNIH1_0872
            MAG: amb3526 amb3579
            MGM: Mmc1_3231
            ABA: Acid345_2509
            SUS: Acid_7305
            BSU: BG11964(murI) BG12306(yrpC)
            BHA: BH3071
            BAN: BA4717(racE-2)
            BAR: GBAA0847(racE-1) GBAA4717(racE-2)
            BAA: BA_1429 BA_5151
            BAT: BAS0806 BAS4379
            BCE: BC0866 BC4496
            BCA: BCE_0939(racE) BCE_4589(racE)
            BCZ: BCZK4236(murI)
            BCY: Bcer98_3204
            BTK: BT9727_0755(racE) BT9727_4220(murI)
            BTL: BALH_0769(racE) BALH_4075(murI)
            BLI: BL00315(racE)
            BLD: BLi02987(racE)
            BCL: ABC2656(racE)
            BAY: RBAM_025460(racE)
            BPU: BPUM_2493(racE)
            OIH: OB2108
            GKA: GK2668
            SAU: SA0997(murI)
            SAV: SAV1151(murI)
            SAM: MW1033(murI)
            SAR: SAR1123(murI)
            SAS: SAS1084
            SAC: SACOL1161(murI)
            SAB: SAB1014(murI)
            SAA: SAUSA300_1049(murI)
            SAO: SAOUHSC_01106
            SAJ: SaurJH9_1209
            SAH: SaurJH1_1231
            SEP: SE0843
            SER: SERP0733(murI)
            SHA: SH1811(murI)
            SSP: SSP1645
            LMO: lmo1237(racE)
            LMF: LMOf2365_1246(murI)
            LIN: lin1200(racE)
            LWE: lwe1192(racE)
            LLA: L0120(murI)
            LLC: LACR_1403
            LLM: llmg_1187(murI)
            SPY: SPy_0361(glr)
            SPZ: M5005_Spy_0303(glr)
            SPM: spyM18_0411
            SPG: SpyM3_0262(glr)
            SPS: SPs1597
            SPH: MGAS10270_Spy0298(glr)
            SPI: MGAS10750_Spy0297(glr)
            SPJ: MGAS2096_Spy0320(glr)
            SPK: MGAS9429_Spy0302(glr)
            SPF: SpyM51555(glr)
            SPA: M6_Spy0329
            SPB: M28_Spy0292(glr)
            SPN: SP_1881
            SPR: spr1696(murI)
            SPD: SPD_1661(murI)
            SAG: SAG1600(murI)
            SAN: gbs1649
            SAK: SAK_1615(murI)
            SMU: SMU.1718(murI)
            STC: str0255(glr)
            STL: stu0255(glr)
            STE: STER_0302
            SSA: SSA_1784(murI)
            SSU: SSU05_1706
            SSV: SSU98_1718
            SGO: SGO_1676(murI)
            LPL: lp_2268(murI)
            LJO: LJ0482
            LAC: LBA0425(murI)
            LSA: LSA0405(murI)
            LSL: LSL_0836(murI)
            LDB: Ldb0510(murI)
            LBU: LBUL_0451
            LBR: LVIS_1214
            LGA: LGAS_0429
            LRE: Lreu_0541
            PPE: PEPE_1257
            EFA: EF1121(murI)
            OOE: OEOE_0680
            LME: LEUM_0609
            STH: STH342
            CAC: CAC3250
            CPE: CPE2568
            CPF: CPF_2893(murI)
            CPR: CPR_2572
            CTC: CTC00259
            CNO: NT01CX_0654(murI)
            CTH: Cthe_1937
            CDF: CD3562(murI)
            CBO: CBO3562(dga)
            CBA: CLB_3644(murI)
            CBH: CLC_3542(murI)
            CBF: CLI_3784(murI)
            CBE: Cbei_0032 Cbei_3599
            CKL: CKL_0131(murI)
            AMT: Amet_1376
            CHY: CHY_0306(murI)
            DSY: DSY3237
            DRM: Dred_1240
            PTH: PTH_0787(murI)
            SWO: Swol_0449
            CSC: Csac_1373
            TTE: TTE0209(murI) TTE0595(murI2) TTE1225(murI3)
            MTA: Moth_0518
            MTU: Rv1338(murI)
            MTC: MT1379(murI)
            MBO: Mb1373(murI)
            MBB: BCG_1400(murI)
            MLE: ML1172(murI)
            MPA: MAP2424c(murI)
            MAV: MAV_1555(murI)
            MSM: MSMEG_4903(murI)
            MVA: Mvan_4289
            MGI: Mflv_2356
            MMC: Mmcs_3846
            MKM: Mkms_3920
            MJL: Mjls_3832
            CGL: NCgl2423(cgl2509)
            CGB: cg2762(murI)
            CEF: CE2403(murI)
            CDI: DIP1853(murI)
            CJK: jk0496(murI)
            NFA: nfa50700(murI)
            RHA: RHA1_ro00141 RHA1_ro02207 RHA1_ro05452 RHA1_ro06051
            SCO: SCO1018(2SCG2.32c)
            SMA: SAV1425(murI)
            LXX: Lxx13590(murI)
            ART: Arth_2583
            AAU: AAur_2572(murI)
            PAC: PPA1675
            NCA: Noca_1315
            TFU: Tfu_2162
            FRA: Francci3_0872
            FAL: FRAAL1505(murI)
            ACE: Acel_1686
            KRA: Krad_3764
            SEN: SACE_1209(murI)
            BLO: BL0086(murI)
            BAD: BAD_1168(murI)
            RXY: Rxyl_1602
            FNU: FN1161
            PCU: pc1853(murI)
            BGA: BG0101(murI)
            BAF: BAPKO_0101(murI)
            TPA: TP0406
            TDE: TDE1448
            LIL: LA3051(murI)
            LIC: LIC11039(murI)
            LBJ: LBJ_2292(murI)
            LBL: LBL_0815(murI)
            SYN: slr1746(murI)
            SYW: SYNW1010(murI)
            SYC: syc1742_c(murI)
            SYF: Synpcc7942_2361
            SYD: Syncc9605_1136
            SYE: Syncc9902_1321
            SYG: sync_1550(murI)
            SYR: SynRCC307_1158(murI)
            SYX: SynWH7803_1037(murI)
            CYA: CYA_2180(murI)
            CYB: CYB_0359(murI)
            TEL: tlr0461
            GVI: gll1496
            ANA: alr0094
            AVA: Ava_1467
            PMA: Pro1043(murI)
            PMM: PMM0617(murI)
            PMT: PMT0393(murI)
            PMN: PMN2A_0054
            PMI: PMT9312_0617
            PMB: A9601_06731(murI)
            PMC: P9515_06821(murI)
            PMF: P9303_18941(murI)
            PMG: P9301_06431(murI)
            PME: NATL1_06751(murI)
            TER: Tery_0161
            BTH: BT_3722
            BFR: BF0501
            BFS: BF0446(murI)
            PGI: PG0705(murI)
            CHU: CHU_1088(murI) CHU_1670(murI) CHU_2624(murI)
            GFO: GFO_0209(murI)
            FJO: Fjoh_1687
            FPS: FP2099(murI)
            CTE: CT0284(murI)
            CCH: Cag_0573
            CPH: Cpha266_0415
            PVI: Cvib_1517
            PLT: Plut_1735
            RRS: RoseRS_1521
            DRA: DR_1586
            DGE: Dgeo_2085
            TTH: TTC1280
            TTJ: TTHA1643
            AAE: aq_325(murI)
            TME: Tmel_1372
            FNO: Fnod_1160
STRUCTURES  PDB: 1B73  1B74  1ZUW  2DWU  2GZM  2JFN  2JFO  2JFP  2JFQ  2JFU  
                 2JFV  2JFW  2JFX  2JFZ  2OHG  2OHO  2OHV  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.3
            ExPASy - ENZYME nomenclature database: 5.1.1.3
            ExplorEnz - The Enzyme Database: 5.1.1.3
            ERGO genome analysis and discovery system: 5.1.1.3
            BRENDA, the Enzyme Database: 5.1.1.3
            CAS: 9024-08-2
///
ENTRY       EC 5.1.1.4                  Enzyme
NAME        proline racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     proline racemase
REACTION    L-proline = D-proline [RN:R01255]
ALL_REAC    R01255
SUBSTRATE   L-proline [CPD:C00148]
PRODUCT     D-proline [CPD:C00763]
REFERENCE   1
  AUTHORS   Stadtman, T.C. and Elliott, P.
  TITLE     Studies on the enzymic reduction of amino acids. II. Purification
            and properties of a D-proline reductase and a proline racemase from
            Clostridium sticklandii.
  JOURNAL   J. Biol. Chem. 228 (1957) 983-997.
  ORGANISM  Clostridium sticklandii
PATHWAY     PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K01777  proline racemase
GENES       AOR: AO090010000012
            PLU: plu2243
            XCC: XCC2415
            XCB: XC_1697
            XCV: XCV2748
            XAC: XAC2550
            XOO: XOO3141
            XOM: XOO_2983(XOO2983)
            PAE: PA1268
            PAU: PA14_47840 PA14_47970
            PPU: PP_1258
            PFL: PFL_1412
            PFO: Pfl_2308
            PEN: PSEEN4050
            PCR: Pcryo_1219
            ACB: A1S_1325
            CSA: Csal_2705
            CVI: CV_2826
            BMA: BMAA1419
            BML: BMA10299_2195
            BMN: BMA10247_A0881
            BXE: Bxe_B0874 Bxe_B1024
            BUR: Bcep18194_B1660 Bcep18194_B1894
            BCN: Bcen_4007 Bcen_4226
            BCH: Bcen2424_4140
            BAM: Bamb_3550
            BPS: BPSS0332
            BPM: BURPS1710b_A1887
            BPL: BURPS1106A_A0473
            BPD: BURPS668_A0570
            BTE: BTH_II2067
            VEI: Veis_1044
            MXA: MXAN_6199
            RET: RHE_CH00452 RHE_PF00391(ypf00209)
            RLE: RL0479(prdF) pRL120535
            BME: BMEI0257 BMEI1586
            SIT: TM1040_3199
            RSP: RSP_3519
            RRU: Rru_A2065
            BAN: BA2834
            BAR: GBAA2834
            BAA: BA_3355
            BAT: BAS2643
            BCE: BC2834 BC2835
            BCA: BCE_2863
            BCZ: BCZK0802(prdF) BCZK2559(prdF)
            BTK: BT9727_0799(prdF) BT9727_2594
            CBA: CLB_2343
            CBH: CLC_2326
            CBF: CLI_2533
            RHA: RHA1_ro05288
            CMI: CMM_0811
            RXY: Rxyl_2251 Rxyl_2259
            HMA: rrnAC2470(prr)
STRUCTURES  PDB: 1TM0  1W61  1W62  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.4
            ExPASy - ENZYME nomenclature database: 5.1.1.4
            ExplorEnz - The Enzyme Database: 5.1.1.4
            ERGO genome analysis and discovery system: 5.1.1.4
            BRENDA, the Enzyme Database: 5.1.1.4
            CAS: 9024-09-3
///
ENTRY       EC 5.1.1.5                  Enzyme
NAME        lysine racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     lysine racemase
REACTION    L-lysine = D-lysine [RN:R00460]
ALL_REAC    R00460
SUBSTRATE   L-lysine [CPD:C00047]
PRODUCT     D-lysine [CPD:C00739]
REFERENCE   1
  AUTHORS   Huang, H.T.
  TITLE     Pat.
  JOURNAL   Chem. Abstr. 54 (1960) 20073.
PATHWAY     PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.5
            ExPASy - ENZYME nomenclature database: 5.1.1.5
            ExplorEnz - The Enzyme Database: 5.1.1.5
            ERGO genome analysis and discovery system: 5.1.1.5
            BRENDA, the Enzyme Database: 5.1.1.5
            CAS: 9024-10-6
///
ENTRY       EC 5.1.1.6                  Enzyme
NAME        threonine racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     threonine racemase
REACTION    L-threonine = D-threonine [RN:R01467]
ALL_REAC    R01467
SUBSTRATE   L-threonine [CPD:C00188]
PRODUCT     D-threonine [CPD:C00820]
COMMENT     Inverts both chiral centres.
REFERENCE   1
  AUTHORS   Amos, H.
  TITLE     A racemase for threonine in Escherichia coli.
  JOURNAL   J. Am. Chem. Soc. 76 (1954) 3858.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.6
            ExPASy - ENZYME nomenclature database: 5.1.1.6
            ExplorEnz - The Enzyme Database: 5.1.1.6
            ERGO genome analysis and discovery system: 5.1.1.6
            BRENDA, the Enzyme Database: 5.1.1.6
            CAS: 9024-11-7
///
ENTRY       EC 5.1.1.7                  Enzyme
NAME        diaminopimelate epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     LL-2,6-diaminoheptanedioate 2-epimerase
REACTION    LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate [RN:R02735]
ALL_REAC    R02735
SUBSTRATE   LL-2,6-diaminoheptanedioate [CPD:C00666]
PRODUCT     meso-diaminoheptanedioate [CPD:C00680]
REFERENCE   1  [PMID:13412646]
  AUTHORS   ANTIA M, HOARE DS, WORK E.
  TITLE     The stereoisomers of alpha epsilon-diaminopimelic acid.  III.
            Properties and distribution of diaminopimelic acid racemase, an
            enzyme causing interconversion of the LL and meso isomers.
  JOURNAL   Biochem. J. 65 (1957) 448-59.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00300  Lysine biosynthesis
ORTHOLOGY   KO: K01778  diaminopimelate epimerase
GENES       ATH: AT3G53580
            OSA: 4352558
            CME: CMQ230C
            DDI: DDBDRAFT_0188427 DDBDRAFT_0190752 DDBDRAFT_0190753
                 DDB_0220128(dafE)
            TET: TTHERM_00128420
            ECO: b3809(dapF)
            ECJ: JW5592(dapF)
            ECE: Z5326(dapF)
            ECS: ECs4739
            ECC: c4730(dapF)
            ECI: UTI89_C4372(dapF)
            ECP: ECP_4003
            ECV: APECO1_2667(dapF)
            ECW: EcE24377A_4328(dapF)
            ECX: EcHS_A4034
            STY: STY3612(dapF)
            STT: t3350(dapF)
            SPT: SPA3788(dapF)
            SEC: SC3846(dapF)
            STM: STM3947(dapF)
            YPE: YPO3845(dapF)
            YPK: y0385(dapF)
            YPM: YP_3202(dapF)
            YPA: YPA_0177
            YPN: YPN_0119
            YPP: YPDSF_3462
            YPS: YPTB0190(dapF)
            YPI: YpsIP31758_0205(dapF)
            SFL: SF3887(dapF)
            SFX: S3869(dapF)
            SFV: SFV_3690(dapF)
            SSN: SSON_3982(dapF)
            SBO: SBO_3820(dapF)
            SDY: SDY_3936(dapF)
            ECA: ECA4183(dapF)
            PLU: plu4640(dapF)
            BUC: BU589(dapF)
            BAS: BUsg568(dapF)
            BAB: bbp533(dapF)
            BCC: BCc_380(dapF)
            WBR: WGLp270(dapF)
            SGL: SG2346
            ENT: Ent638_3983
            SPE: Spro_0182
            BFL: Bfl579(dapF)
            BPN: BPEN_600(dapF)
            HIT: NTHI0906(dapF)
            HIP: CGSHiEE_08355(dapF)
            HIQ: CGSHiGG_07250(dapF)
            HDU: HD0026(dapF)
            HSO: HS_1610(dapF)
            PMU: PM1703(dapF)
            MSU: MS1784(dapF)
            APL: APL_1531(dapF)
            ASU: Asuc_1968
            XFA: XF1481
            XFT: PD0698(dapF)
            XCC: XCC3499(dapF)
            XCB: XC_0662
            XCV: XCV0689(dapF)
            XAC: XAC0634(dapF)
            XOO: XOO3997
            XOM: XOO_3767(XOO3767)
            VCH: VC0126
            VCO: VC0395_A2393(dapF)
            VVU: VV1_1127
            VVY: VV0087
            VPA: VP2983
            VFI: VF2484(dapF)
            PPR: PBPRA3522(dapF)
            PAE: PA5278(dapF)
            PAU: PA14_69690(dapF)
            PAP: PSPA7_6021(dapF)
            PPU: PP_3790(dapF-1) PP_5228(dapF-2)
            PPF: Pput_2751 Pput_5137
            PST: PSPTO_0224(dapF)
            PSB: Psyr_0183(dapF)
            PSP: PSPPH_5007(dapF)
            PFL: PFL_2539(dapF) PFL_6013(dapF)
            PFO: Pfl_5499
            PEN: PSEEN5366(dapF)
            PMY: Pmen_0266
            PAR: Psyc_0200(dapF)
            PCR: Pcryo_0220
            PRW: PsycPRwf_0349
            ACI: ACIAD2659(dapF)
            SON: SO_4308(dapF)
            SDN: Sden_0391
            SFR: Sfri_0445
            SAZ: Sama_3249
            SBL: Sbal_3995
            SBM: Shew185_3973
            SLO: Shew_0323
            SPC: Sputcn32_3582
            SSE: Ssed_4129
            SPL: Spea_0378
            SHE: Shewmr4_0392
            SHM: Shewmr7_3633
            SHN: Shewana3_0391
            SHW: Sputw3181_3721
            ILO: IL2555(dapF)
            CPS: CPS_0077(dapF)
            PHA: PSHAa0092(dapF)
            PAT: Patl_4074
            SDE: Sde_0237
            PIN: Ping_0040 Ping_3334
            MAQ: Maqu_0495
            CBU: CBU_1970(dapF)
            CBD: COXBU7E912_2069(dapF)
            LPN: lpg0366(dapF)
            LPF: lpl0407(dapF)
            LPP: lpp0431(dapF)
            MCA: MCA0859(dapF)
            TCX: Tcr_0405
            NOC: Noc_0316
            AEH: Mlg_0061
            HHA: Hhal_1200
            HCH: HCH_00298(dapF1) HCH_03641(dapF2)
            CSA: Csal_3113
            ABO: ABO_2332(dapF)
            MMW: Mmwyl1_0680 Mmwyl1_3587
            AHA: AHA_0474(dapF)
            DNO: DNO_0042(dapF)
            BCI: BCI_0125(dapF)
            CRP: CRP_178
            RMA: Rmag_0550
            VOK: COSY_0505(dapF)
            NME: NMB0760
            NMA: NMA0972(dapF)
            NMC: NMC0713(dapF)
            NGO: NGO0338
            CVI: CV_2528(dapF)
            RSO: RSc0137(dapF)
            REU: Reut_A0198(dapF)
            REH: H16_A0227(dapF)
            RME: Rmet_0153
            BMA: BMA3260(dapF)
            BMV: BMASAVP1_A2922(dapF)
            BML: BMA10299_A2167(dapF)
            BMN: BMA10247_3426(dapF)
            BXE: Bxe_A4373
            BVI: Bcep1808_3168
            BUR: Bcep18194_A6435(dapF) Bcep18194_B0095
            BCN: Bcen_2471 Bcen_5260
            BCH: Bcen2424_3085 Bcen2424_5599
            BAM: Bamb_3131
            BPS: BPSL0210(dapF)
            BPL: BURPS1106A_0209(dapF)
            BPD: BURPS668_0197(dapF)
            BTE: BTH_I0172(dapF)
            PNU: Pnuc_2006
            BPE: BP3074(dapF)
            BPA: BPP0189(dapF)
            BBR: BB0192(dapF)
            RFR: Rfer_3444
            POL: Bpro_1058
            PNA: Pnap_3435
            AAV: Aave_0799
            AJS: Ajs_3688
            VEI: Veis_4553
            MPT: Mpe_A3245
            HAR: HEAR2955(dapF)
            MMS: mma_3201
            NEU: NE1612(dapF)
            NET: Neut_0505
            NMU: Nmul_A2542
            EBA: ebA3950(dapF)
            AZO: azo0594(dapF)
            DAR: Daro_0192
            TBD: Tbd_2526
            MFA: Mfla_0196
            HPY: HP0566(dapF)
            HPJ: jhp0513(dapF)
            HPA: HPAG1_0545
            HHE: HH1701(dapF)
            HAC: Hac_0786(dapF)
            WSU: WS2150(dapF)
            TDN: Tmden_2046
            CJE: Cj1531(dapF)
            CJR: CJE1702(dapF)
            CJJ: CJJ81176_1516(dapF)
            CJU: C8J_1430(dapF)
            CJD: JJD26997_1883(dapF)
            CFF: CFF8240_1771(dapF)
            CCV: CCV52592_0348(dapF) CCV52592_1811
            CHA: CHAB381_0107(dapF) CHAB381_0492(dapF)
            CCO: CCC13826_1841(dapF) CCC13826_2114
            ABU: Abu_0144(dapF)
            NIS: NIS_0102(dapF)
            SUN: SUN_2410(dapF)
            GSU: GSU0531(dapF)
            GME: Gmet_2992
            GUR: Gura_3911
            PCA: Pcar_3074
            PPD: Ppro_3414
            DVU: DVU1867(dapF)
            DVL: Dvul_1297
            DDE: Dde_1798
            LIP: LI0895(dapF)
            BBA: Bd0045(dapF)
            DPS: DP0433
            ADE: Adeh_0570
            AFW: Anae109_0613
            MXA: MXAN_5054(dapF)
            SAT: SYN_00169 SYN_00706
            SFU: Sfum_0057
            RPR: RP415(dapF)
            RTY: RT0401(dapF)
            RCO: RC0579(dapF)
            RFE: RF_0645(dapF)
            RBE: RBE_0652(dapF)
            RAK: A1C_03130(dapF)
            RBO: A1I_04280(dapF)
            RRI: A1G_03270(dapF)
            WOL: WD1208(dapF)
            WBM: Wbm0518
            AMA: AM1323(dapF)
            ERU: Erum0340(dapF)
            ERW: ERWE_CDS_00210(dapF)
            ERG: ERGA_CDS_00210(dapF)
            ECN: Ecaj_0026
            ECH: ECH_0050(dapF)
            PUB: SAR11_0257(dapF)
            MLO: mlr4318
            MES: Meso_3391
            PLA: Plav_1415
            SME: SMc03856(dapF)
            SMD: Smed_3093
            ATU: Atu2695(dapF)
            ATC: AGR_C_4886(dapF)
            RET: RHE_CH03955(dapF)
            RLE: RL4545(dapF)
            BME: BMEI0133
            BMF: BAB1_1932(dapF)
            BMS: BR1932(dapF)
            BMB: BruAb1_1908(dapF)
            BOV: BOV_1859(dapF)
            OAN: Oant_0927
            BJA: bll0477(dapF)
            BRA: BRADO0383(dapF)
            BBT: BBta_0372(dapF)
            RPA: RPA0250(dapF)
            RPB: RPB_0359
            RPC: RPC_0215
            RPD: RPD_0514
            RPE: RPE_0321
            NWI: Nwi_2776(dapF)
            NHA: Nham_3575
            BHE: BH16600(dapF)
            BQU: BQ13480(dapF)
            BBK: BARBAKC583_0019(dapF)
            XAU: Xaut_0411
            CCR: CC_3686
            SIL: SPO0278(dapF)
            SIT: TM1040_2809
            RSP: RSP_0936(dapF)
            RSH: Rsph17029_2595
            RSQ: Rsph17025_2979
            JAN: Jann_0318
            RDE: RD1_0813(dapF)
            PDE: Pden_0395
            MMR: Mmar10_0019
            HNE: HNE_3529(dapF)
            ZMO: ZMO1072(dapF)
            NAR: Saro_1402
            SAL: Sala_2730
            SWI: Swit_2928
            ELI: ELI_03915
            GOX: GOX1453
            GBE: GbCGDNIH1_1500
            ACR: Acry_2498
            RRU: Rru_A1183
            MAG: amb0215
            MGM: Mmc1_3739
            ABA: Acid345_2622
            SUS: Acid_4598
            BSU: BG14048(dapF)
            BHA: BH3412
            BAN: BA5170(dapF)
            BAA: BA_0043
            BAT: BAS4806
            BCE: BC4936(dapF)
            BCA: BCE_5074(dapF)
            BCZ: BCZK4667(dapF)
            BCY: Bcer98_3545
            BTK: BT9727_4647(dapF)
            BTL: BALH_4473(dapF)
            BLI: BL03150(dapF)
            BLD: BLi03399(dapF)
            BCL: ABC2934(dapF)
            BAY: RBAM_029280
            BPU: BPUM_2877
            OIH: OB2354(dapF)
            GKA: GK2957
            LMO: lmo2018
            LMF: LMOf2365_2043(dapF)
            LIN: lin2126
            LWE: lwe2038(dapF)
            LPL: lp_2185(dapF)
            LAC: LBA0849(dapF)
            LSL: LSL_0856(dapF)
            LCA: LSEI_0100
            LRE: Lreu_0610
            EFA: EF0464(dapF)
            STH: STH234
            CAC: CAC2624(dapF)
            CPE: CPE1846(dapF)
            CPF: CPF_2100(dapF)
            CPR: CPR_1814(dapF)
            CNO: NT01CX_1955(dapF)
            CTH: Cthe_3100
            CDF: CD2590(dapF)
            CBO: CBO1912(dapF)
            CBA: CLB_1849(dapF)
            CBH: CLC_1856(dapF)
            CBF: CLI_1976(dapF)
            CBE: Cbei_1600
            CKL: CKL_1203(dapF)
            AMT: Amet_2793
            CHY: CHY_1493(dapF)
            DSY: DSY2743
            DRM: Dred_1694
            CSC: Csac_1315
            TTE: TTE1514(dapF)
            MTA: Moth_0888
            MTU: Rv2726c(dapF)
            MTC: MT2798(dapF)
            MBO: Mb2745c(dapF)
            MBB: BCG_2739c(dapF)
            MLE: ML0996(dapF)
            MPA: MAP2840c(dapF)
            MAV: MAV_3619(dapF)
            MSM: MSMEG_2735(dapF)
            MVA: Mvan_2435
            MGI: Mflv_3961
            MMC: Mmcs_2163
            MKM: Mkms_2209
            MJL: Mjls_2150
            CGL: NCgl1868(dapF)
            CGB: cg2129(dapF)
            CEF: CE1837
            CDI: DIP1442(dapF)
            CJK: jk1110(dapF)
            NFA: nfa38290(dapF)
            RHA: RHA1_ro06777(dapF)
            SCO: SCO5793(dapF)
            SMA: SAV2473(dapF1) SAV3161(dapF2)
            LXX: Lxx15970(dapF)
            ART: Arth_1464
            AAU: AAur_1599(dapF)
            PAC: PPA1020(dapF)
            NCA: Noca_3841
            TFU: Tfu_0816
            FRA: Francci3_3514
            FAL: FRAAL5707(dapF)
            ACE: Acel_1483
            KRA: Krad_1501
            SEN: SACE_1753(dapF)
            STP: Strop_1446
            BLO: BL0087(dapF)
            BAD: BAD_1167(dapF)
            RXY: Rxyl_0095
            CTR: CT430(dapF)
            CTA: CTA_0470(dapF)
            CMU: TC0714
            CPN: CPn0519(dapF)
            CPA: CP0234
            CPJ: CPj0519(dapF)
            CPT: CpB0540
            CCA: CCA00226(dapF)
            CAB: CAB223
            CFE: CF0780(dapF)
            PCU: pc0442(dapF)
            LIL: LA0083(dapF)
            LIC: LIC10074(dapF)
            LBJ: LBJ_0071(dapF)
            LBL: LBL_3025(dapF)
            SYN: slr1665(dapF)
            SYW: SYNW1254(dapF)
            SYC: syc2167_c(dapF)
            SYF: Synpcc7942_1927
            SYD: Syncc9605_1371
            SYE: Syncc9902_1107
            SYG: sync_1368(dapF)
            SYR: SynRCC307_1190(dapF)
            SYX: SynWH7803_1262(dapF)
            CYA: CYA_1324(dapF)
            CYB: CYB_1371(dapF)
            TEL: tll2294(dapF)
            GVI: gll0815(dapF)
            ANA: alr2048 alr4841(dapF)
            AVA: Ava_2112(dapF) Ava_3088(dapF)
            PMA: Pro0948(dapF)
            PMM: PMM0888(dapF)
            PMT: PMT0716(dapF)
            PMN: PMN2A_0322
            PMI: PMT9312_0912
            PMB: A9601_09731(dapF)
            PMC: P9515_09701(dapF)
            PMF: P9303_15041(dapF)
            PMG: P9301_09711(dapF)
            PMH: P9215_10041
            PME: NATL1_09951(dapF)
            TER: Tery_1173
            BTH: BT_0548
            BFR: BF2642
            BFS: BF2665(dapF)
            SRU: SRU_1415(dapF)
            CHU: CHU_0127(dapF)
            GFO: GFO_0624(dapF)
            FJO: Fjoh_0018
            FPS: FP1215(dapF)
            CTE: CT2021(dapF)
            CCH: Cag_0342
            CPH: Cpha266_0218
            PVI: Cvib_1620
            PLT: Plut_1977
            DET: DET0740(dapF)
            DEH: cbdb_A715(dapF)
            DEB: DehaBAV1_0670
            AAE: aq_1838(dapF)
            TMA: TM1522
            TPT: Tpet_1270
            TME: Tmel_1874
            FNO: Fnod_0071
            MMP: MMP0917(dapF)
            MMQ: MmarC5_0724
            MMZ: MmarC7_0164
            MAE: Maeo_0204
            MVN: Mevan_0004
            MTP: Mthe_0454
            MHU: Mhun_2316
            MEM: Memar_2160
            MBN: Mboo_2431
            MST: Msp_1579(dapF)
            MSI: Msm_1372
            MKA: MK0434(dapF)
            HMA: rrnAC1794(dapF)
            HWA: HQ1511A(dapF)
            RCI: RCIX1964(dapF)
STRUCTURES  PDB: 1BWZ  1GQZ  2GKE  2GKJ  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.7
            ExPASy - ENZYME nomenclature database: 5.1.1.7
            ExplorEnz - The Enzyme Database: 5.1.1.7
            ERGO genome analysis and discovery system: 5.1.1.7
            BRENDA, the Enzyme Database: 5.1.1.7
            CAS: 9024-22-0
///
ENTRY       EC 5.1.1.8                  Enzyme
NAME        4-hydroxyproline epimerase;
            hydroxyproline epimerase;
            hydroxyproline 2-epimerase;
            L-hydroxyproline epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     4-hydroxyproline 2-epimerase
REACTION    trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline [RN:R03296]
ALL_REAC    R03296
SUBSTRATE   trans-4-hydroxy-L-proline [CPD:C01157]
PRODUCT     cis-4-hydroxy-D-proline [CPD:C03440]
COMMENT     Also interconverts trans-4-hydroxy-D-proline and
            cis-4-hydroxy-L-proline.
REFERENCE   1
  AUTHORS   Adams, E. and Norton, I.L.
  TITLE     Purification and properties of inducible hydroxyproline 2-epimerase
            from Pseudomonas.
  JOURNAL   J. Biol. Chem. 239 (1964) 1525-1535.
  ORGANISM  Pseudomonas striata
PATHWAY     PATH: map00330  Arginine and proline metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.8
            ExPASy - ENZYME nomenclature database: 5.1.1.8
            ExplorEnz - The Enzyme Database: 5.1.1.8
            ERGO genome analysis and discovery system: 5.1.1.8
            BRENDA, the Enzyme Database: 5.1.1.8
            CAS: 9024-23-1
///
ENTRY       EC 5.1.1.9                  Enzyme
NAME        arginine racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     arginine racemase
REACTION    L-arginine = D-arginine [RN:R00567]
ALL_REAC    R00567;
            (other) R00460 R00579 R00672
SUBSTRATE   L-arginine [CPD:C00062]
PRODUCT     D-arginine [CPD:C00792]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:5779761]
  AUTHORS   Yorifuji T, Ogata K, Soda K.
  TITLE     Crystalline arginine racemase.
  JOURNAL   Biochem. Biophys. Res. Commun. 34 (1969) 760-4.
  ORGANISM  Pseudomonas graveolens
PATHWAY     PATH: map00310  Lysine degradation
            PATH: map00471  D-Glutamine and D-glutamate metabolism
            PATH: map00472  D-Arginine and D-ornithine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.9
            ExPASy - ENZYME nomenclature database: 5.1.1.9
            ExplorEnz - The Enzyme Database: 5.1.1.9
            ERGO genome analysis and discovery system: 5.1.1.9
            BRENDA, the Enzyme Database: 5.1.1.9
            CAS: 37290-94-1
///
ENTRY       EC 5.1.1.10                 Enzyme
NAME        amino-acid racemase;
            L-amino acid racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     amino-acid racemase
REACTION    an L-amino acid = a D-amino acid [RN:R01265]
ALL_REAC    R01265 > R00579 R00589 R00672 R00903
SUBSTRATE   L-amino acid [CPD:C00151]
PRODUCT     D-amino acid [CPD:C00405]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     A pyridoxal-phosphate protein.
REFERENCE   1  [PMID:5788493]
  AUTHORS   Soda K, Osumi T.
  TITLE     Crystalline amino acid racemase with low substrate specificity.
  JOURNAL   Biochem. Biophys. Res. Commun. 35 (1969) 363-8.
  ORGANISM  Pseudomonas striata
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00272  Cysteine metabolism
            PATH: map00471  D-Glutamine and D-glutamate metabolism
            PATH: map00472  D-Arginine and D-ornithine metabolism
STRUCTURES  PDB: 2FKP  2GGG  2GGH  2GGI  2GGJ  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.10
            ExPASy - ENZYME nomenclature database: 5.1.1.10
            ExplorEnz - The Enzyme Database: 5.1.1.10
            ERGO genome analysis and discovery system: 5.1.1.10
            BRENDA, the Enzyme Database: 5.1.1.10
            CAS: 9068-61-5
///
ENTRY       EC 5.1.1.11                 Enzyme
NAME        phenylalanine racemase (ATP-hydrolysing);
            phenylalanine racemase;
            phenylalanine racemase (adenosine triphosphate-hydrolysing);
            gramicidin S synthetase I
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     phenylalanine racemase (ATP-hydrolysing)
REACTION    ATP + L-phenylalanine + H2O = AMP + diphosphate + D-phenylalanine
            [RN:R00686]
ALL_REAC    R00686
SUBSTRATE   ATP [CPD:C00002];
            L-phenylalanine [CPD:C00079];
            H2O [CPD:C00001]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            D-phenylalanine [CPD:C02265]
REFERENCE   1  [PMID:5354026]
  AUTHORS   Yamada M, Kurahashi K.
  TITLE     Further purification and properties of adenosine
            triphosphate-dependent phenylalanine racemase of Bacillus brevis
            Nagano.
  JOURNAL   J. Biochem. (Tokyo). 66 (1969) 529-40.
  ORGANISM  Bacillus brevis
PATHWAY     PATH: map00360  Phenylalanine metabolism
GENES       NOC: Noc_1956
            BUR: Bcep18194_A4786 Bcep18194_A4787 Bcep18194_C7423
            BBT: BBta_3701 BBta_3702 BBta_4110
            RHA: RHA1_ro00433
            FAL: FRAAL0189(dhbE) FRAAL2542
            SEN: SACE_2618 SACE_4304
            AVA: Ava_1649 Ava_3855 Ava_3984 Ava_4101 Ava_4745 Ava_4746
                 Ava_4833 Ava_C0002 Ava_C0004 Ava_C0008
STRUCTURES  PDB: 1AMU  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.11
            ExPASy - ENZYME nomenclature database: 5.1.1.11
            ExplorEnz - The Enzyme Database: 5.1.1.11
            ERGO genome analysis and discovery system: 5.1.1.11
            BRENDA, the Enzyme Database: 5.1.1.11
            CAS: 37290-95-2
///
ENTRY       EC 5.1.1.12                 Enzyme
NAME        ornithine racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     ornithine racemase
REACTION    L-ornithine = D-ornithine [RN:R00672]
ALL_REAC    R00672
SUBSTRATE   L-ornithine [CPD:C00077]
PRODUCT     D-ornithine [CPD:C00515]
REFERENCE   1  [PMID:10715017]
  AUTHORS   Chen HP, Lin CF, Lee YJ, Tsay SS, Wu SH.
  TITLE     Purification and properties of ornithine racemase from Clostridium
            sticklandii.
  JOURNAL   J. Bacteriol. 182 (2000) 2052-4.
  ORGANISM  Clostridium sticklandii
PATHWAY     PATH: map00472  D-Arginine and D-ornithine metabolism
GENES       BBT: BBta_1087 BBta_1089
            RHA: RHA1_ro00232 RHA1_ro02397
            AVA: Ava_4109 Ava_4837 Ava_C0009
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.12
            ExPASy - ENZYME nomenclature database: 5.1.1.12
            ExplorEnz - The Enzyme Database: 5.1.1.12
            ERGO genome analysis and discovery system: 5.1.1.12
            BRENDA, the Enzyme Database: 5.1.1.12
            CAS: 62213-28-9
///
ENTRY       EC 5.1.1.13                 Enzyme
NAME        aspartate racemase;
            D-aspartate racemase;
            McyF
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     aspartate racemase
REACTION    L-aspartate = D-aspartate [RN:R00491]
ALL_REAC    R00491
SUBSTRATE   L-aspartate [CPD:C00049]
PRODUCT     D-aspartate [CPD:C00402]
COMMENT     Also acts, at half the rate, on L-alanine.
REFERENCE   1  [PMID:4626916]
  AUTHORS   Lamont HC, Staudenbauer WL, Strominger JL.
  TITLE     Partial purification and characterization of an aspartate racemase
            from Streptococcus faecalis.
  JOURNAL   J. Biol. Chem. 247 (1972) 5103-6.
  ORGANISM  Streptococcus faecalis
REFERENCE   2  [PMID:1526977]
  AUTHORS   Yamauchi T, Choi SY, Okada H, Yohda M, Kumagai H, Esaki N, Soda K.
  TITLE     Properties of aspartate racemase, a pyridoxal
            5'-phosphate-independent amino acid racemase.
  JOURNAL   J. Biol. Chem. 267 (1992) 18361-4.
  ORGANISM  Streptococcus thermophilus
REFERENCE   3  [PMID:12051922]
  AUTHORS   Liu L, Iwata K, Kita A, Kawarabayasi Y, Yohda M, Miki K.
  TITLE     Crystal structure of aspartate racemase from Pyrococcus horikoshii
            OT3 and its implications for molecular mechanism of PLP-independent
            racemization.
  JOURNAL   J. Mol. Biol. 319 (2002) 479-89.
  ORGANISM  Pyrococcus horikoshii [GN:pho]
REFERENCE   4  [PMID:12713441]
  AUTHORS   Sielaff H, Dittmann E, Tandeau De Marsac N, Bouchier C, Von Dohren
            H, Borner T, Schwecke T.
  TITLE     The mcyF gene of the microcystin biosynthetic gene cluster from
            Microcystis aeruginosa encodes an aspartate racemase.
  JOURNAL   Biochem. J. 373 (2003) 909-16.
  ORGANISM  Microcystis aeruginosa
REFERENCE   5  [PMID:15606767]
  AUTHORS   Yamashita T, Ashiuchi M, Ohnishi K, Kato S, Nagata S, Misono H.
  TITLE     Molecular identification of monomeric aspartate racemase from
            Bifidobacterium bifidum.
  JOURNAL   Eur. J. Biochem. 271 (2004) 4798-803.
  ORGANISM  Bifidobacterium bifidum
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
ORTHOLOGY   KO: K01779  aspartate racemase
GENES       ECP: ECP_2853
            YPE: YPO2758
            YPK: y1592
            YPM: YP_2405(racX)
            YPA: YPA_2085
            YPN: YPN_2188
            YPS: YPTB2625
            ECA: ECA1293 ECA1500 ECA1532
            XCC: XCC1785(ygeA)
            XCB: XC_2451
            XCV: XCV1832
            XAC: XAC1802(ygeA)
            VFI: VF1547 VFA0624
            PFL: PFL_2830
            PCR: Pcryo_0021
            ACI: ACIAD0318
            SDN: Sden_1375 Sden_1468
            SFR: Sfri_1897
            ILO: IL1778
            PAT: Patl_0005
            HCH: HCH_00437
            CSA: Csal_0199
            AHA: AHA_3590
            CVI: CV_0113
            RSO: RSc0212(RS00644)
            REU: Reut_A1720
            REH: H16_B2421(racX)
            RME: Rmet_4003
            BXE: Bxe_A1530
            BUR: Bcep18194_A5449
            BCN: Bcen_5934
            BCH: Bcen2424_2143
            BAM: Bamb_2180 Bamb_6429
            BTE: BTH_II1157
            RFR: Rfer_3727
            POL: Bpro_4755
            HHE: HH0075(ygeA)
            CCV: CCV52592_0918
            PUB: SAR11_1277(racX)
            RET: RHE_CH02763(ypch00952)
            RLE: RL3216(asr)
            RDE: RD1_0818
            ZMO: ZMO0371(asr) ZMO1158(asr)
            RRU: Rru_A3109
            ABA: Acid345_4593
            BAN: BA2223 BA2639 BA5005
            BAR: GBAA2223 GBAA2639 GBAA5005
            BAA: BA_2726 BA_3158 BA_5425
            BAT: BAS2067 BAS2459 BAS4650
            BCE: BC2177 BC2623 BC4750
            BCA: BCE_0308 BCE_2253 BCE_2665 BCE_4895
            BCZ: BCZK2006(racD) BCZK2383(asp) BCZK4503
            BTK: BT9727_2007(racD) BT9727_2422(asp) BT9727_4485
            BTL: BALH_1986(racD) BALH_2374(asp) BALH_4328
            BCL: ABC3598(racX)
            BPU: BPUM_1136(racX)
            LLA: L92665(racD)
            LLC: LACR_2531
            LLM: llmg_2504(racD)
            SSA: SSA_0042
            LPL: lp_1523(racD)
            LJO: LJ0566
            LAC: LBA0546 LBA1817
            LSA: LSA0099(racD)
            LSL: LSL_0018(racX)
            LDB: Ldb2043(racD)
            LBR: LVIS_1499
            LCA: LSEI_0224
            LRE: Lreu_0282
            CTC: CTC00823
            CBE: Cbei_0251
            DSY: DSY4104
            RHA: RHA1_ro00144 RHA1_ro02319 RHA1_ro06103 RHA1_ro06664
            FAL: FRAAL2547
            SEN: SACE_2953(racX)
            BAD: BAD_1087(racD)
            AVA: Ava_4838 Ava_C0005 Ava_C0007
            MMP: MMP0739
            PTO: PTO0149
STRUCTURES  PDB: 1IU9  1JFL  2DX7  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.13
            ExPASy - ENZYME nomenclature database: 5.1.1.13
            ExplorEnz - The Enzyme Database: 5.1.1.13
            ERGO genome analysis and discovery system: 5.1.1.13
            BRENDA, the Enzyme Database: 5.1.1.13
            CAS: 37237-56-2
///
ENTRY       EC 5.1.1.14                 Enzyme
NAME        nocardicin-A epimerase;
            isonocardicin A epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     nocardicin-A epimerase
REACTION    isonocardicin A = nocardicin A [RN:R03073]
ALL_REAC    R03073
SUBSTRATE   isonocardicin A [CPD:C00927]
PRODUCT     nocardicin A [CPD:C01941]
COMMENT     The (9'S) configuration of isonocardicin A is converted into the
            (9'R) configuration.
REFERENCE   1
  AUTHORS   Wilson, B.A., Bantia, S., Salituro, G.M., Reeve, A.M. and Townsend,
            C.A.
  TITLE     Cell-free biosynthesis of nocardicin A from nocardicin E and
            S-adenosylmethionine.
  JOURNAL   J. Am. Chem. Soc. 110 (1988) 8238-8239.
  ORGANISM  Nocardia uniformis
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.14
            ExPASy - ENZYME nomenclature database: 5.1.1.14
            ExplorEnz - The Enzyme Database: 5.1.1.14
            ERGO genome analysis and discovery system: 5.1.1.14
            BRENDA, the Enzyme Database: 5.1.1.14
            CAS: 118246-75-6
///
ENTRY       EC 5.1.1.15                 Enzyme
NAME        2-aminohexano-6-lactam racemase;
            alpha-amino-epsilon-caprolactam racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     2-aminohexano-6-lactam racemase
REACTION    L-2-aminohexano-6-lactam = D-2-aminohexano-6-lactam [RN:R04736]
ALL_REAC    R04736
SUBSTRATE   L-2-aminohexano-6-lactam
PRODUCT     D-2-aminohexano-6-lactam
COMMENT     Contains pyridoxal 5'-phosphate. Also racemises
            2-aminopentano-5-lactam (alpha-amino-delta-valerolactam) and
            2-amino-4-thiahexano-6-lactam (where S replaces CH2 of C-4). It does
            not catalyse the racemisation of alpha-amino acids but has some
            transaminase activity with them.
REFERENCE   1
  AUTHORS   Ahmed, S.A., Esaki, N., Tanaka, H., Soda, K.
  TITLE     L-alpha-Amino-beta-thio-epsilon-caprolactam, a new sulfur-containing
            substrate for alpha-amino-epsilon-caprolactam racemase.
  JOURNAL   FEBS Lett. 174 (1984) 76-79.
  ORGANISM  Achromobacter obae
REFERENCE   2  [PMID:3955003]
  AUTHORS   Ahmed SA, Esaki N, Tanaka H, Soda K.
  TITLE     Mechanism of alpha-amino-epsilon-caprolactam racemase reaction.
  JOURNAL   Biochemistry. 25 (1986) 385-8.
  ORGANISM  Achromobacter obae
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.15
            ExPASy - ENZYME nomenclature database: 5.1.1.15
            ExplorEnz - The Enzyme Database: 5.1.1.15
            ERGO genome analysis and discovery system: 5.1.1.15
            BRENDA, the Enzyme Database: 5.1.1.15
            CAS: 52652-64-9
///
ENTRY       EC 5.1.1.16                 Enzyme
NAME        protein-serine epimerase;
            protein-serine racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     [protein]-serine epimerase
REACTION    [protein]-L-serine = [protein]-D-serine [RN:R05175]
ALL_REAC    R05175
SUBSTRATE   [protein]-L-serine [CPD:C06395]
PRODUCT     [protein]-D-serine [CPD:C06396]
COMMENT     The enzyme specifically interconverts the configuration of Ser-46 of
            the peptide omega-agatoxin-KT, found in the venom of the funnel web
            spider, Agelenopsis aperta, but not that of the other serine
            residue, Ser-28.
REFERENCE   1  [PMID:7622482]
  AUTHORS   Shikata Y, Watanabe T, Teramoto T, Inoue A, Kawakami Y, Nishizawa Y,
            Katayama K, Kuwada M.
  TITLE     Isolation and characterization of a peptide isomerase from funnel
            web spider venom.
  JOURNAL   J. Biol. Chem. 270 (1995) 16719-23.
  ORGANISM  Agelenopsis aperta
STRUCTURES  PDB: 1WTC  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.16
            ExPASy - ENZYME nomenclature database: 5.1.1.16
            ExplorEnz - The Enzyme Database: 5.1.1.16
            ERGO genome analysis and discovery system: 5.1.1.16
            BRENDA, the Enzyme Database: 5.1.1.16
            CAS: 169592-52-3
///
ENTRY       EC 5.1.1.17                 Enzyme
NAME        isopenicillin-N epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on amino acids and derivatives
SYSNAME     penicillin-N 5-amino-5-carboxypentanoyl-epimerase
REACTION    isopenicillin N = penicillin N [RN:R04147]
ALL_REAC    R04147
SUBSTRATE   isopenicillin N [CPD:C05557]
PRODUCT     penicillin N [CPD:C06564]
COMMENT     This enzyme contains pyridoxal phosphate. Epimerization at C-5 of
            the 5-amino-5-carboxypentanoyl group to form penicillin N is
            required to make a substrate for EC 1.14.20.1,
            deactoxycephalosporin-C synthase, to produce cephalosporins. Forms
            part of the penicillin biosynthesis pathway (for pathway, click
            here).
REFERENCE   1  [PMID:2804141]
  AUTHORS   Usui S, Yu CA.
  TITLE     Purification and properties of isopenicillin N epimerase from
            Streptomyces clavuligerus.
  JOURNAL   Biochim. Biophys. Acta. 999 (1989) 78-85.
  ORGANISM  Streptomyces clavuligerus
REFERENCE   2
  AUTHORS   Laiz, L., Liras, P., Castro, J.M. and Martin, J.F.
  TITLE     Purification and characterization of the isopenicillin-N epimerase
            from Nocardia lactamdurans.
  JOURNAL   J. Gen. Microbiol. 136 (1990) 663-671.
  ORGANISM  Nocardia lactamdurans
REFERENCE   3  [PMID:1354366]
  AUTHORS   Cantwell C, Beckmann R, Whiteman P, Queener SW, Abraham EP.
  TITLE     Isolation of deacetoxycephalosporin C from fermentation broths of
            Penicillium chrysogenum transformants: construction of a new fungal
            biosynthetic pathway.
  JOURNAL   Proc. R. Soc. Lond. B. Biol. Sci. 248 (1992) 283-9.
  ORGANISM  Streptomyces lipmanii
REFERENCE   4
  AUTHORS   Yeh, W.K., Ghag, S.K. and Queener, S.W.
  TITLE     Enzymes for epimerization of isopenicillin N, ring expansion of
            penicillin N, and 3'-hydroxylation of deacetoxycephalosporin C.
            Function, evolution, refolding, and enzyme engineering.
  JOURNAL   Ann. N.Y. Acad. Sci. 672 (1992) 396-408.
PATHWAY     PATH: map00311  Penicillin and cephalosporin biosynthesis
ORTHOLOGY   KO: K04127  isopenicillin-N epimerase
GENES       XCC: XCC1212(nifS)
            XCB: XC_3030
            RSO: RS01753(RSp0696)
            BMA: BMAA0692
            BPS: BPSS0826
            BPM: BURPS1710b_A2417(cefD)
            BPL: BURPS1106A_A1140(cefD)
            BBA: Bd2034
            MXA: MXAN_5758(cefD)
            RBA: RB7564(cefD)
            CYA: CYA_0818(cefD)
            CYB: CYB_1874(cefD)
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.1.17
            ExPASy - ENZYME nomenclature database: 5.1.1.17
            ExplorEnz - The Enzyme Database: 5.1.1.17
            ERGO genome analysis and discovery system: 5.1.1.17
            BRENDA, the Enzyme Database: 5.1.1.17
            CAS: 88201-43-8
///
ENTRY       EC 5.1.2.1                  Enzyme
NAME        lactate racemase;
            lacticoracemase;
            hydroxyacid racemase;
            lactic acid racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on hydroxy acids and derivatives
SYSNAME     lactate racemase
REACTION    (S)-lactate = (R)-lactate [RN:R01450]
ALL_REAC    R01450
SUBSTRATE   (S)-lactate [CPD:C00186]
PRODUCT     (R)-lactate [CPD:C00256]
REFERENCE   1  [PMID:14800428]
  AUTHORS   HUENNEKENS FM, MAHLER HR, NORDMANN J.
  TITLE     Studies on the cyclophorase system. XVII. The occurrence and
            properties of an alpha-hydroxy acid racemose.
  JOURNAL   Arch. Biochem. 30 (1951) 77-89.
REFERENCE   2
  AUTHORS   Kitahara, K., Obayashi, A. and Fukui, S.
  TITLE     Racemase I cell-free racemase.
  JOURNAL   Enzymologia 15 (1953) 259-266.
PATHWAY     PATH: map00620  Pyruvate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.2.1
            ExPASy - ENZYME nomenclature database: 5.1.2.1
            ExplorEnz - The Enzyme Database: 5.1.2.1
            ERGO genome analysis and discovery system: 5.1.2.1
            BRENDA, the Enzyme Database: 5.1.2.1
            CAS: 9024-05-9
///
ENTRY       EC 5.1.2.2                  Enzyme
NAME        mandelate racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on hydroxy acids and derivatives
SYSNAME     mandelate racemase
REACTION    (S)-mandelate = (R)-mandelate [RN:R03791]
ALL_REAC    R03791;
            (other) R04161
SUBSTRATE   (S)-mandelate [CPD:C01984]
PRODUCT     (R)-mandelate [CPD:C01983]
COFACTOR    Manganese [CPD:C00034];
            Magnesium [CPD:C00305]
REFERENCE   1  [PMID:13108854]
  AUTHORS   GUNSALUS CF, STANIER RY, GUNSALUS IC.
  TITLE     The enzymatic conversion of mandelic acid to benzoic acid. III.
            Fractionation and properties of the soluble enzymes.
  JOURNAL   J. Bacteriol. 66 (1953) 548-53.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00622  Toluene and xylene degradation
ORTHOLOGY   KO: K01781  mandelate racemase
GENES       ANI: AN6035.2
            AFM: AFUA_2G09810
            AOR: AO090011000654
            ECI: UTI89_C4552
            STY: STY4099
            STT: t3822
            SPT: SPA3549
            SEC: SC3621(yin)
            STM: STM3697
            ECA: ECA0998 ECA3116
            PAT: Patl_2550 Patl_2790
            SDE: Sde_2648
            CBU: CBU_1275(rspA)
            FTW: FTW_0641
            NOC: Noc_0470
            REU: Reut_B4441 Reut_B4643
            BXE: Bxe_B0135 Bxe_C1041 Bxe_C1285
            BUR: Bcep18194_B0622
            BPS: BPSL0725
            BPM: BURPS1710b_0947
            BPD: BURPS668_0799
            BPE: BP1161
            BBR: BB2683
            POL: Bpro_0435 Bpro_3962
            MMS: mma_3075
            AZO: azo1246
            DDE: Dde_1177
            MXA: MXAN_3652
            MLO: mll7149 mlr0803
            MES: Meso_1539 Meso_3550
            SME: SMb21107(manR) SMc00459
            ATU: Atu1648 Atu4120
            ATC: AGR_C_3037 AGR_L_1470
            RET: RHE_CH02350 RHE_PE00430
            RLE: pRL110598 pRL120237
            BME: BMEI1707 BMEI1712
            BMF: BAB1_0242 BAB1_1037
            BMS: BR0239 BR1018
            BMB: BruAb1_0234 BruAb1_1023
            BJA: blr5895 blr7625
            BRA: BRADO0023 BRADO4202 BRADO5087 BRADO6325
            BBT: BBta_0028 BBta_4577
            RPB: RPB_1626
            RPC: RPC_1451
            RPD: RPD_1635
            RPE: RPE_1470
            NWI: Nwi_1085
            NHA: Nham_1314 Nham_4191
            CCR: CC_3113
            SIL: SPO3606
            SIT: TM1040_3167 TM1040_3391
            RSP: RSP_1769 RSP_3384
            JAN: Jann_0365
            RDE: RD1_0690 RD1_1003
            HNE: HNE_2922
            ZMO: ZMO1228(ykfB) ZMO1264(rspA)
            BCZ: BCZK2578(ykfB)
            MPA: MAP1382c
            MSM: MSMEG_0126
            RHA: RHA1_ro02789 RHA1_ro08313
            SCO: SCO3480(SCE65.16c)
            AAU: AAur_0037(clcB)
            TFU: Tfu_1717
            FRA: Francci3_1987
            SEN: SACE_1998 SACE_3937 SACE_4598 SACE_4937 SACE_5057
            RXY: Rxyl_2719
STRUCTURES  PDB: 1DTN  1MDL  1MDR  1MNS  1MRA  2MNR  2OG9  2OX4  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.2.2
            ExPASy - ENZYME nomenclature database: 5.1.2.2
            ExplorEnz - The Enzyme Database: 5.1.2.2
            ERGO genome analysis and discovery system: 5.1.2.2
            UM-BBD (Biocatalysis/Biodegradation Database): 5.1.2.2
            BRENDA, the Enzyme Database: 5.1.2.2
            CAS: 9024-04-8
///
ENTRY       EC 5.1.2.3                  Enzyme
NAME        3-hydroxybutyryl-CoA epimerase;
            3-hydroxybutyryl coenzyme A epimerase;
            3-hydroxyacyl-CoA epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on hydroxy acids and derivatives
SYSNAME     3-hydroxybutanoyl-CoA 3-epimerase
REACTION    (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA [RN:R03276]
ALL_REAC    R03276;
            (other) R04755
SUBSTRATE   (S)-3-hydroxybutanoyl-CoA [CPD:C01144]
PRODUCT     (R)-3-hydroxybutanoyl-CoA [CPD:C03561]
REFERENCE   1
  AUTHORS   Stern, J.R., del Campillo, A. and Lehninger, A.L.
  TITLE     Enzymatic racemization of beta-hydroxybutyryl-S-CoA and the
            stereospecificity of enzymes of the fatty acid cycle.
  JOURNAL   J. Am. Chem. Soc. 77 (1955) 1073-1074.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Wakil, S.J.
  TITLE     D(-)beta-Hydroxybutyryl CoA dehydrogenase.
  JOURNAL   Biochim. Biophys. Acta 18 (1955) 314-315.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00071  Fatty acid metabolism
            PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K01782  3-hydroxybutyryl-CoA epimerase
GENES       TCR: 509701.10
            LMA: LmjF26.1550
            ECO: b2341(yfcX) b3846(fadB)
            ECJ: JW2338(yfcX) JW3822(fadB)
            ECE: Z3604 Z5367(fadB)
            ECS: ECs3224 ECs4774
            ECC: c2886 c4793(fadB)
            ECI: UTI89_C2625 UTI89_C4431(fadB)
            ECP: ECP_2379 ECP_4059
            ECV: APECO1_2611(fadB) APECO1_4225
            ECW: EcE24377A_2637(fadJ) EcE24377A_4365(fadB)
            ECX: EcHS_A2492(fadJ) EcHS_A4069(fadB)
            STY: STY2620 STY3577(fadB)
            STT: t0476 t3315(fadB)
            SPT: SPA0476(yfcX) SPA3823(fadB)
            SEC: SC2390(yfcX) SC3880(fadB)
            STM: STM2388(yfcX) STM3983(fadB)
            YPE: YPO2747(faoA) YPO3766(fadB)
            YPK: y0464(fadB) y1580
            YPM: YP_2417(faoA) YP_3282(fadB)
            YPA: YPA_2097 YPA_3436
            YPN: YPN_0198 YPN_2200
            YPS: YPTB0267(fadB) YPTB2636(faoA)
            YPI: YpsIP31758_0283(fadB) YpsIP31758_1400(fadJ)
            SFL: SF2419
            SFX: S2554
            SFV: SFV_2409
            SSN: SSON_2397 SSON_4019(fadB)
            SBO: SBO_2379
            SDY: SDY_2542 SDY_3899(fadB)
            ECA: ECA0208(fadB) ECA3078
            PLU: plu3200 plu4402(fadB)
            APL: APL_0888(fadJ)
            XCC: XCC1266(fadB)
            XCB: XC_2975
            XCV: XCV1369(fadB)
            XAC: XAC1318(fadB)
            XOO: XOO1848(fadB)
            XOM: XOO_1744(XOO1744)
            VCH: VC1047 VC2758
            VVU: VV1_0981 VV1_1976
            VVY: VV0029 VV2440
            VPA: VP0030 VP2208
            VFI: VF0025 VF1810
            PPR: PBPRA0064 PBPRA0962
            PAE: PA3014(faoA)
            PAP: PSPA7_2145(fadB)
            PPU: PP_2136(fadB)
            PPF: Pput_3694
            PST: PSPTO_3517(fadB)
            PSB: Psyr_3290
            PSP: PSPPH_3210(fadB)
            PFL: PFL_1940(fadB)
            PFO: Pfl_3879
            PEN: PSEEN3728(fadB)
            PMY: Pmen_0379
            PAR: Psyc_1399 Psyc_1934(fadB)
            ACI: ACIAD0335(fadB) ACIAD2989
            SON: SO_0021(fadB) SO_3088
            SDN: Sden_0015 Sden_1530
            SFR: Sfri_0013
            SHE: Shewmr4_0018 Shewmr4_1408
            SHM: Shewmr7_0016 Shewmr7_1473
            SHN: Shewana3_0024 Shewana3_1461
            ILO: IL0011(fadB) IL0993
            CPS: CPS_0393(fadB) CPS_3156(fadJ)
            PHA: PSHAa0011(fadB) PSHAa0967(fadJ)
            PAT: Patl_0201 Patl_1664
            FTU: FTT1530(fadB)
            FTF: FTF1530(fadB)
            NOC: Noc_0826 Noc_1733
            AEH: Mlg_2111
            HCH: HCH_04756
            ABO: ABO_1566(fadB)
            AHA: AHA_0139(fadB) AHA_2154(fadJ)
            CVI: CV_2720(fadB)
            REU: Reut_B4799
            BMA: BMA0198
            BML: BMA10299_A1822
            BXE: Bxe_C0280
            BUR: Bcep18194_A5207 Bcep18194_A6221 Bcep18194_C7186
            BPS: BPSL0063 BPSL0649
            BPM: BURPS1710b_0287(fadB) BURPS1710b_0858(fadB)
            BTE: BTH_I0062 BTH_I0565
            NET: Neut_0724
            AZO: azo0465(fadB1)
            DAR: Daro_2350
            ADE: Adeh_0408
            MXA: MXAN_5371(fadJ)
            MLO: mlr5629
            MES: Meso_0021 Meso_1524
            SME: SMc02227(fadB)
            SMD: Smed_4155
            ATU: Atu0503(fadB)
            ATC: AGR_C_888
            RET: RHE_CH00559(fadB2)
            BME: BMEII0497
            BMF: BAB2_0444
            BMS: BRA0793(fadB)
            BMB: BruAb2_0439(fadB)
            BJA: blr1160(fadB) blr2428
            RPA: RPA0818
            RPB: RPB_4604
            RPC: RPC_0735
            RPD: RPD_0807
            RPE: RPE_0674
            NWI: Nwi_2993
            CCR: CC_0076
            SIL: SPO2920(fabJ-1)
            RSP: RSP_2196
            RDE: RD1_3973(fadJ)
            MMR: Mmar10_0543
            HNE: HNE_0672
            NAR: Saro_0869
            MGM: Mmc1_3556
            MTU: Rv0860(fadB)
            MTC: MT0883
            MBO: Mb0883(fadB)
            MLE: ML2161(fadB)
            MPA: MAP0790(fadB_1) MAP1715(fadB_2)
            CJK: jk0159(fadB1)
            NFA: nfa2860(fadB)
            RHA: RHA1_ro00407 RHA1_ro04205(fadB1) RHA1_ro06116(fadB2)
                 RHA1_ro06852
            SCO: SCO6732(SC5F2A.15) SCO6789(SC6A5.38)
            SMA: SAV1680(fadB1)
            FRA: Francci3_1329
            FAL: FRAAL2096
            SEN: SACE_1823 SACE_6362(fadB)
            RBA: RB1092(faoA)
            SRU: SRU_1459(yfcX)
            DRA: DR_1487
            PIS: Pisl_1438
STRUCTURES  PDB: 1WDK  1WDL  1WDM  2D3T  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.2.3
            ExPASy - ENZYME nomenclature database: 5.1.2.3
            ExplorEnz - The Enzyme Database: 5.1.2.3
            ERGO genome analysis and discovery system: 5.1.2.3
            BRENDA, the Enzyme Database: 5.1.2.3
            CAS: 9024-21-9
///
ENTRY       EC 5.1.2.4                  Enzyme
NAME        acetoin racemase;
            acetylmethylcarbinol racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on hydroxy acids and derivatives
SYSNAME     acetoin racemase
REACTION    (S)-acetoin = (R)-acetoin [RN:R02949]
ALL_REAC    R02949
SUBSTRATE   (S)-acetoin [CPD:C01769]
PRODUCT     (R)-acetoin [CPD:C00810]
REFERENCE   1
  AUTHORS   Taylor, M.B. and Juni, E.
  TITLE     Stereoisomeric specificities of 2,3-butanediol dehydrogenase.
  JOURNAL   Biochim. Biophys. Acta 39 (1960) 448-457.
  ORGANISM  guinea pig, rat [GN:rno], human [GN:hsa]
PATHWAY     PATH: map00650  Butanoate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.2.4
            ExPASy - ENZYME nomenclature database: 5.1.2.4
            ExplorEnz - The Enzyme Database: 5.1.2.4
            ERGO genome analysis and discovery system: 5.1.2.4
            BRENDA, the Enzyme Database: 5.1.2.4
            CAS: 37318-32-4
///
ENTRY       EC 5.1.2.5                  Enzyme
NAME        tartrate epimerase;
            tartaric racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on hydroxy acids and derivatives
SYSNAME     tartrate epimerase
REACTION    (R,R)-tartrate = meso-tartrate [RN:R02546]
ALL_REAC    R02546
SUBSTRATE   (R,R)-tartrate [CPD:C00898]
PRODUCT     meso-tartrate [CPD:C00552]
REFERENCE   1
  AUTHORS   Ranjan, S., Patnaik, K.K. and Laloraya, M.M.
  TITLE     Enzymic conversion of meso-tartrate to dextro-tartrate in tamarind.
  JOURNAL   Naturwissenschaften 48 (1961) 406.
  ORGANISM  tamarind
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.2.5
            ExPASy - ENZYME nomenclature database: 5.1.2.5
            ExplorEnz - The Enzyme Database: 5.1.2.5
            ERGO genome analysis and discovery system: 5.1.2.5
            BRENDA, the Enzyme Database: 5.1.2.5
            CAS: 37318-33-5
///
ENTRY       EC 5.1.2.6                  Enzyme
NAME        isocitrate epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on hydroxy acids and derivatives
SYSNAME     (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate 1-epimerase
REACTION    (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate =
            (1S,2S)-1-hydroxypropane-1,2,3-tricarboxylate [RN:R02318]
ALL_REAC    R02318
SUBSTRATE   (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate [CPD:C00451]
PRODUCT     (1S,2S)-1-hydroxypropane-1,2,3-tricarboxylate [CPD:C04617]
COMMENT     (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate is the commonly
            occurring isomer of isocitrate.
REFERENCE   1
  AUTHORS   Hoshiko, S., Kunimoto, Y., Arima, K. and Beppu, T.
  TITLE     Mechanism of L-alloisocitric acid fermentation: isocitrate epimerase
            activity in the cell-free-extract of Penicillium purpurogenum.
  JOURNAL   Agric. Biol. Chem. 46 (1982) 143-151.
  ORGANISM  Penicillium purpurogenum
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.2.6
            ExPASy - ENZYME nomenclature database: 5.1.2.6
            ExplorEnz - The Enzyme Database: 5.1.2.6
            ERGO genome analysis and discovery system: 5.1.2.6
            BRENDA, the Enzyme Database: 5.1.2.6
            CAS: 81210-68-6
///
ENTRY       EC 5.1.2.-                  Enzyme
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on hydroxy acids and derivatives
REACTION    2-Hydroxy-2H-benzo[h]chromene-2-carboxylate <=>
            cis-4-(1'-Hydroxynaphth-2'-yl)-2-oxobut-3-enoate [RN:R05642]
SUBSTRATE   2-Hydroxy-2H-benzo[h]chromene-2-carboxylate [CPD:C11425]
PRODUCT     cis-4-(1'-Hydroxynaphth-2'-yl)-2-oxobut-3-enoate [CPD:C11426]
///
ENTRY       EC 5.1.3.1                  Enzyme
NAME        ribulose-phosphate 3-epimerase;
            phosphoribulose epimerase;
            erythrose-4-phosphate isomerase;
            phosphoketopentose 3-epimerase;
            xylulose phosphate 3-epimerase;
            phosphoketopentose epimerase;
            ribulose 5-phosphate 3-epimerase;
            D-ribulose phosphate-3-epimerase;
            D-ribulose 5-phosphate epimerase;
            D-ribulose-5-P 3-epimerase;
            D-xylulose-5-phosphate 3-epimerase;
            pentose-5-phosphate 3-epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     D-ribulose-5-phosphate 3-epimerase
REACTION    D-ribulose 5-phosphate = D-xylulose 5-phosphate [RN:R01529]
ALL_REAC    R01529
SUBSTRATE   D-ribulose 5-phosphate [CPD:C00199]
PRODUCT     D-xylulose 5-phosphate [CPD:C00231]
COMMENT     The enzyme also converts D-erythrose 4-phosphate into D-erythrulose
            4-phosphate and D-threose 4-phosphate.
REFERENCE   1
  AUTHORS   Ashwell, G. and Hickman, J.
  TITLE     Enzymatic formation of xylulose 5-phosphate from ribose 5-phosphate
            in spleen.
  JOURNAL   J. Biol. Chem. 226 (1957) 65-76.
  ORGANISM  Lactobacillus pentosus
REFERENCE   2  [PMID:13373810]
  AUTHORS   DICKENS F, WILLIAMSON DH.
  TITLE     Pentose phosphate isomerase and epimerase from animal tissues.
  JOURNAL   Biochem. J. 64 (1956) 567-78.
  ORGANISM  Lactobacillus pentosus
REFERENCE   3
  AUTHORS   Hurwitz, J. and Horecker, B.L.
  TITLE     The purification of phosphoketopentoepimerase from Lactobacillus
            pentosus and the preparation of xylulose 5-phosphate.
  JOURNAL   J. Biol. Chem. 223 (1956) 993-1008.
  ORGANISM  Lactobacillus pentosus
REFERENCE   4
  AUTHORS   Stumpf, P.K. and Horecker, B.L.
  TITLE     The roole of xylulose 5-phosphate in xylose metabolism of
            Lactobacillus pentosus.
  JOURNAL   J. Biol. Chem. 218 (1956) 753-768.
  ORGANISM  Lactobacillus pentosus
REFERENCE   5  [PMID:3987693]
  AUTHORS   Terada T, Mukae H, Ohashi K, Hosomi S, Mizoguchi T, Uehara K.
  TITLE     Characterization of an enzyme which catalyzes isomerization and
            epimerization of D-erythrose 4-phosphate.
  JOURNAL   Eur. J. Biochem. 148 (1985) 345-51.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00030  Pentose phosphate pathway
            PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00710  Carbon fixation
ORTHOLOGY   KO: K01783  ribulose-phosphate 3-epimerase
GENES       HSA: 6120(RPE)
            MMU: 66646(Rpe)
            CFA: 478893(RPE)
            GGA: 770045(RPE)
            XLA: 494647(LOC494647)
            DRE: 334897(rpe)
            SPU: 588015(LOC588015)
            DME: Dmel_CG30499
            CEL: F08F8.7
            ATH: AT1G63290
            OSA: 4331761
            CME: CMI084C CMO229C CMT633C
            SCE: YJL121C(RPE1)
            AGO: AGOS_AFL208C
            PIC: PICST_50761(RPE1)
            CAL: CaJ7.0022
            CGR: CAGL0L05478g
            SPO: SPAC31G5.05c
            ANI: AN7588.2
            AFM: AFUA_2G15190
            AOR: AO090012000303
            CNE: CNA06630
            UMA: UM04797.1
            ECU: ECU06_1040
            DDI: DDB_0231226(rpe)
            PFA: PFL0960w
            TET: TTHERM_00086760 TTHERM_00492730
            TBR: Tb10.389.1530
            TCR: 509213.70 510257.30
            LMA: LmjF33.1570
            EHI: 53.t00013
            ECO: b3386(rpe)
            ECJ: JW3349(rpe)
            ECE: Z4739(rpe)
            ECS: ECs4228
            ECC: c4156(rpe)
            ECI: UTI89_C3884(rpe)
            ECP: ECP_3471
            ECV: APECO1_3077(rpe)
            ECW: EcE24377A_3855(rpe)
            ECX: EcHS_A3582(rpe)
            STY: STY4313(rpe)
            STT: t4023(rpe)
            SPT: SPA3348(rpe)
            SEC: SC3415(rpe)
            STM: STM3483(rpe)
            YPE: YPO0155(rpe)
            YPK: y3938(rpe)
            YPM: YP_0157(rpe)
            YPA: YPA_3314
            YPN: YPN_3910
            YPP: YPDSF_0082
            YPS: YPTB3746(rpe)
            YPI: YpsIP31758_3962(rpe)
            SFL: SF3404(rpe)
            SFX: S4358(rpe)
            SFV: SFV_3391(rpe)
            SSN: SSON_3517(rpe)
            SBO: SBO_3373(rpe)
            SDY: SDY_3693(rpe)
            ECA: ECA4089(rpe)
            PLU: plu0086(rpe)
            BUC: BU537(rpe)
            BAS: BUsg518(rpe)
            BAB: bbp479(rpe)
            BCC: BCc_351(rpe)
            WBR: WGLp580(rpe)
            SGL: SG2305
            ENT: Ent638_3799
            KPN: KPN_03757(rpe)
            SPE: Spro_2667 Spro_4601
            BFL: Bfl570(rpe)
            BPN: BPEN_590(rpe)
            HIN: HI0566(dod)
            HIT: NTHI0698(rpe)
            HIP: CGSHiEE_00155 CGSHiEE_08235
            HIQ: CGSHiGG_06105
            HDU: HD1929(rpe)
            HSO: HS_0057(rpe) HS_0175(rpe)
            PMU: PM1619(dod_2)
            MSU: MS2330(rpe)
            APL: APL_1820(rpe)
            ASU: Asuc_0218
            XFA: XF0208
            XFT: PD0168(rpe)
            XCC: XCC0455(rpe)
            XCB: XC_0469
            XCV: XCV0502(rpe)
            XAC: XAC0472(rpe)
            XOO: XOO4052(rpe)
            XOM: XOO_3827(XOO3827)
            VCH: VC2625
            VCO: VC0395_A2202(rpe)
            VVU: VV1_1386
            VVY: VV2985
            VPA: VP2741
            VFI: VF2288
            PPR: PBPRA0284
            PAE: PA0607(rpe)
            PAU: PA14_07910(rpe)
            PAP: PSPA7_0751(rpe)
            PPU: PP_0415(rpe)
            PPF: Pput_0449
            PST: PSPTO_0566(rpe)
            PSB: Psyr_4611
            PSP: PSPPH_0647(rpe)
            PFL: PFL_5631(rpe)
            PFO: Pfl_5120
            PEN: PSEEN0442(rpe)
            PMY: Pmen_3999
            PAR: Psyc_1715(rpe)
            PCR: Pcryo_1994
            PRW: PsycPRwf_0584
            ACI: ACIAD0685(rpe)
            SON: SO_0292(rpe)
            SDN: Sden_0267
            SFR: Sfri_0381
            SAZ: Sama_3362
            SBL: Sbal_4107
            SBM: Shew185_4077
            SLO: Shew_0219
            SPC: Sputcn32_3700
            SSE: Ssed_4259
            SPL: Spea_0244
            SHE: Shewmr4_3692
            SHM: Shewmr7_0253
            SHN: Shewana3_3888
            SHW: Sputw3181_3842
            ILO: IL2324
            CPS: CPS_0479(rpe)
            PHA: PSHAa2710(rpe)
            PAT: Patl_0659
            SDE: Sde_0746
            PIN: Ping_0167
            MAQ: Maqu_3515
            CBU: CBU_1872(rpe)
            CBD: COXBU7E912_0103(rpe)
            LPN: lpg0664(rpe)
            LPF: lpl0701(rpe)
            LPP: lpp0721(rpe)
            MCA: MCA2582(rpe)
            FTU: FTT0789(rpe)
            FTF: FTF0789(rpe)
            FTW: FTW_0586(rpe)
            FTL: FTL_1432
            FTH: FTH_1395(rpe)
            FTA: FTA_1520(rpe)
            FTN: FTN_1221(rpe)
            TCX: Tcr_0264
            NOC: Noc_2492
            AEH: Mlg_2834
            HHA: Hhal_1048
            HCH: HCH_06112(rpe)
            CSA: Csal_2328
            ABO: ABO_2042(rpe)
            MMW: Mmwyl1_1057
            AHA: AHA_3185(rpe)
            DNO: DNO_0540(rpe)
            BCI: BCI_0022(rpe)
            CRP: CRP_076
            RMA: Rmag_1071
            VOK: COSY_0970(rpe)
            NME: NMB1244
            NMA: NMA1413(rpe)
            NMC: NMC1145(rpe)
            NGO: NGO0758
            CVI: CV_2182(rpe)
            RSO: RSc2879(rpe)
            REU: Reut_A3021
            REH: H16_A3317(rpe) H16_B1391(cbbE2)
            RME: Rmet_1510 Rmet_3176
            BMA: BMAA0535(rpe)
            BMV: BMASAVP1_0642(rpe)
            BML: BMA10299_0938(rpe)
            BMN: BMA10247_A1908(rpe)
            BXE: Bxe_A0463 Bxe_B2446
            BVI: Bcep1808_0513
            BUR: Bcep18194_A3623
            BCN: Bcen_2569
            BCH: Bcen2424_0536
            BAM: Bamb_0441
            BPS: BPSL3048
            BPM: BURPS1710b_3573(rpe)
            BPL: BURPS1106A_3581(rpe)
            BPD: BURPS668_3554(rpe)
            BTE: BTH_I2907(rpe)
            PNU: Pnuc_0149
            BPE: BP3266(rpe)
            BPA: BPP4154(rpe)
            BBR: BB4624(rpe)
            RFR: Rfer_0532
            POL: Bpro_4466
            PNA: Pnap_1981 Pnap_3660
            AAV: Aave_0438
            AJS: Ajs_0361
            VEI: Veis_0587
            MPT: Mpe_A2786(cbbE) Mpe_A3466(cbbE)
            HAR: HEAR0202(rpe) HEAR2648(grpE)
            MMS: mma_0237(rpe)
            NEU: NE2148(cbbE)
            NET: Neut_2096
            NMU: Nmul_A2371
            EBA: ebA4173(rpe)
            AZO: azo3327(rpe)
            DAR: Daro_3483
            TBD: Tbd_2230(cbbE)
            MFA: Mfla_2472
            HPY: HP1386
            HPA: HPAG1_1482
            HHE: HH1346(rpe)
            HAC: Hac_1779(rpe)
            WSU: WS0219(REP)
            TDN: Tmden_1605
            CJE: Cj0451(rep)
            CJR: CJE0501(rpe)
            CJJ: CJJ81176_0476(rpe)
            CJU: C8J_0424(rpe)
            CJD: JJD26997_1488(rpe)
            CFF: CFF8240_0861(rpe)
            CHA: CHAB381_0769(rpe)
            ABU: Abu_0860(rpe)
            NIS: NIS_0320(rpe)
            SUN: SUN_2156(rpe)
            GSU: GSU3374(rpe)
            GME: Gmet_0067
            GUR: Gura_0194
            PCA: Pcar_0240
            PPD: Ppro_3241
            DVU: DVU2531(rpe)
            DVL: Dvul_0714
            DDE: Dde_2632
            LIP: LI0218(rpe)
            BBA: Bd2756
            DPS: DP0795
            ADE: Adeh_3971
            AFW: Anae109_0447
            MXA: MXAN_6297(rpe)
            SAT: SYN_01763
            SFU: Sfum_1951
            WOL: WD0712(rpe)
            WBM: Wbm0236
            AMA: AM1213(rpe)
            APH: APH_0002(rpe)
            ERU: Erum0560(rpe)
            ERW: ERWE_CDS_00470(rpe)
            ERG: ERGA_CDS_00460(rpe)
            ECN: Ecaj_0049
            ECH: ECH_0082(rpe)
            NSE: NSE_0336(rpe)
            PUB: SAR11_0317(rpe)
            MLO: mlr4760
            MES: Meso_0005
            PLA: Plav_1322
            SME: SMb20195(ppe) SMc00511(rpe)
            SMD: Smed_0012 Smed_1489 Smed_3927
            ATU: Atu1839(rpe)
            ATC: AGR_C_3374
            RET: RHE_CH02270(rpe)
            RLE: RL2598(rpe) pRL120033
            BME: BMEI1116
            BMF: BAB1_0869(rpe)
            BMS: BR0850(rpe)
            BMB: BruAb1_0862(rpe)
            BOV: BOV_0842(rpe)
            OAN: Oant_0180 Oant_2376
            BJA: blr2588 blr5680(rpe)
            BRA: BRADO2842(rpe)
            BBT: BBta_0454(rpe) BBta_5332(rpe)
            RPA: RPA3815(cbbE)
            RPB: RPB_3689
            RPC: RPC_1614
            RPD: RPD_1771
            RPE: RPE_0573 RPE_1642
            NWI: Nwi_2218
            NHA: Nham_2620
            BHE: BH09680(rpe)
            BQU: BQ07440(rpe)
            BBK: BARBAKC583_0856(rpe)
            XAU: Xaut_1911 Xaut_2533
            CCR: CC_0101
            SIL: SPO0779(rpe)
            SIT: TM1040_3710
            RSP: RSP_2864(cbbE)
            RSH: Rsph17029_1430
            RSQ: Rsph17025_1512
            JAN: Jann_0790
            RDE: RD1_1105(rpe)
            PDE: Pden_2572
            MMR: Mmar10_2925
            HNE: HNE_3370(rpe)
            ZMO: ZMO0018(rpe)
            NAR: Saro_0104
            SAL: Sala_3128
            SWI: Swit_1941
            ELI: ELI_12550
            GOX: GOX1352
            GBE: GbCGDNIH1_2141
            ACR: Acry_0022 Acry_0827
            RRU: Rru_A2402
            MAG: amb1379
            MGM: Mmc1_3649
            ABA: Acid345_0074
            SUS: Acid_3191
            BSU: BG13393(rpe)
            BHA: BH2502
            BAN: BA3998(rpe)
            BAR: GBAA3998(rpe)
            BAT: BAS3711
            BCE: BC3858
            BCA: BCE_3902(rpe)
            BCZ: BCZK3619(rpe)
            BCY: Bcer98_2512
            BTK: BT9727_3601(rpe)
            BTL: BALH_3491
            BLI: BL02305(rpe)
            BLD: BLi01800(rpe)
            BCL: ABC2313(rpe)
            BAY: RBAM_015620(rpe)
            BPU: BPUM_1478(rpe) BPUM_1755
            OIH: OB1511
            GKA: GK1178
            GTN: GTNG_1031(rpe)
            SAU: SA1065(cfxE)
            SAV: SAV1222(cfxE)
            SAM: MW1105(cfxE)
            SAR: SAR1198
            SAS: SAS1156
            SAC: SACOL1235(rpe)
            SAB: SAB1086
            SAA: SAUSA300_1115(rpe)
            SAO: SAOUHSC_01189
            SAJ: SaurJH9_1281 SaurJH9_2430
            SAH: SaurJH1_1306 SaurJH1_2478
            SEP: SE0897
            SER: SERP0788(rpe)
            SHA: SH1693(cfxE)
            SSP: SSP1550
            LMO: lmo0499 lmo0505 lmo0735 lmo1818 lmo2659 lmo2661
            LMF: LMOf2365_0528 LMOf2365_0534(rpe-1) LMOf2365_1846(rpe-2)
                 LMOf2365_2639(rpe-3) LMOf2365_2641
            LIN: lin0499 lin0505 lin1932 lin2808 lin2810
            LWE: lwe0704 lwe1837(rpe) lwe2608(rpe) lwe2610
            LLA: L0047(rpe)
            LLC: LACR_1639 LACR_2195
            LLM: llmg_0957(rpe2) llmg_2190(rpe)
            SPY: SPy_0264(rpe)
            SPZ: M5005_Spy_0224(rpe)
            SPM: spyM18_0248
            SPG: SpyM3_0192(rpe)
            SPS: SPs0197
            SPH: MGAS10270_Spy0224(rpe)
            SPI: MGAS10750_Spy0219(rpe)
            SPJ: MGAS2096_Spy0242(rpe)
            SPK: MGAS9429_Spy0226(rpe)
            SPF: SpyM50203(rpe)
            SPA: M6_Spy0256
            SPB: M28_Spy0218(rpe)
            SPN: SP_1983
            SPR: spr1797(rpe)
            SPD: SPD_1780(rpe)
            SAG: SAG1776(rpe)
            SAN: gbs1819
            SAK: SAK_1798(rpe)
            SMU: SMU.352
            STC: str1797(rpe)
            STL: stu1797(rpe)
            SSA: SSA_2119(rpe)
            SSU: SSU05_1993
            SSV: SSU98_1998
            SGO: SGO_0198(rpe)
            LPL: lp_1621(rpe)
            LJO: LJ1535
            LAC: LBA1315
            LSA: LSA0694(rpe)
            LSL: LSL_1807(rpe) LSL_1948(rpe)
            LDB: Ldb0530(rpe)
            LBU: LBUL_0471
            LBR: LVIS_0960
            LCA: LSEI_1620
            LGA: LGAS_0766
            LRE: Lreu_1167
            EFA: EF3118(rpe)
            OOE: OEOE_0790
            LME: LEUM_1509
            STH: STH1355 STH2338
            CAC: CAC1730
            CPE: CPE1736
            CPF: CPF_1989(rpe)
            CPR: CPR_1707(rpe)
            CTC: CTC01227
            CNO: NT01CX_2237
            CTH: Cthe_0576
            CDF: CD2319(rpe) CD2575
            CBO: CBO2502
            CBA: CLB_2375(rpe)
            CBH: CLC_2357(rpe)
            CBF: CLI_2563(rpe)
            CBE: Cbei_0226 Cbei_0529 Cbei_0547 Cbei_1153
            CKL: CKL_1377
            AMT: Amet_2777
            CHY: CHY_1476(rpe)
            DSY: DSY2683 DSY3012
            DRM: Dred_1716
            SWO: Swol_1223
            CSC: Csac_2074
            TTE: TTE1498(rpe2)
            MTA: Moth_0914
            MGE: MG_112
            MPN: MPN251(cfxE)
            MPU: MYPU_6830(rpe)
            MPE: MYPE3050(rpe)
            MGA: MGA_0455(tpe)
            MMY: MSC_0305(rpe) MSC_0396(rpe)
            MMO: MMOB5610(rpe)
            MHY: mhp231(rpe) mhp577(rpe)
            MHJ: MHJ_0147(rpe) MHJ_0560
            MHP: MHP7448_0151(rpe) MHP7448_0557
            MSY: MS53_0119(rpe)
            MCP: MCAP_0260(rpe) MCAP_0589
            UUR: UU456(rpe)
            MFL: Mfl223 Mfl640
            MTU: Rv1408(rpe)
            MTC: MT1452(rpe)
            MBO: Mb1443(rpe)
            MBB: BCG_1469(rpe)
            MLE: ML0554(rpe)
            MPA: MAP1135(rpe)
            MAV: MAV_3370(rpe)
            MSM: MSMEG_3066(rpe)
            MVA: Mvan_2689
            MGI: Mflv_3728
            MMC: Mmcs_2385
            MKM: Mkms_2432
            MJL: Mjls_2426
            CGL: NCgl1536(cgl1598)
            CGB: cg1801(rpe)
            CEF: CE1717
            CDI: DIP1320(rpe)
            CJK: jk1011(rpe)
            NFA: nfa36030(rpe)
            RHA: RHA1_ro07167(rpe)
            SCO: SCO1464(rpe)
            SMA: SAV6880(rpe)
            TWH: TWT357(rpe)
            TWS: TW413(rpe)
            LXX: Lxx11200
            CMI: CMM_1773(rpeA)
            ART: Arth_1673
            AAU: AAur_1824(rpe)
            PAC: PPA1199
            NCA: Noca_2446
            TFU: Tfu_1077
            FRA: Francci3_1797 Francci3_3188
            FAL: FRAAL5223(rpe)
            ACE: Acel_1276
            KRA: Krad_2980
            SEN: SACE_2120(rpe)
            STP: Strop_1872
            BLO: BL0753(rpe)
            BAD: BAD_0793(rpe)
            RXY: Rxyl_1363
            FNU: FN0680
            RBA: RB1561(rpe)
            CTR: CT121(araD)
            CTA: CTA_0128(araD)
            CMU: TC0397
            CPN: CPn0185(rpe)
            CPA: CP0583
            CPJ: CPj0185(rpe)
            CPT: CpB0188
            CCA: CCA00551(rpe)
            CAB: CAB537
            CFE: CF0457(rpe)
            PCU: pc0768(rpe)
            TPA: TP0945
            TDE: TDE2597(rpe)
            LIL: LA2394
            LIC: LIC11554(rpe)
            LBJ: LBJ_1437(rpe)
            LBL: LBL_1661(rpe)
            SYN: sll0807(rpe)
            SYW: SYNW1115(rpe)
            SYC: syc0920_c(rpe)
            SYF: Synpcc7942_0604
            SYD: Syncc9605_1252
            SYE: Syncc9902_1230
            SYG: sync_1683(rpe-1) sync_1684(rpe-2)
            SYR: SynRCC307_1256(rpe)
            SYX: SynWH7803_1301(rpe)
            CYA: CYA_0084(rpe)
            CYB: CYB_2047(rpe)
            TEL: tll2369(rpe)
            GVI: gll3548
            ANA: alr0782
            AVA: Ava_4675
            PMA: Pro0839(rpe)
            PMM: PMM0766(rpe)
            PMT: PMT0569(rpe)
            PMN: PMN2A_0172
            PMI: PMT9312_0774
            PMB: A9601_08281(rpe)
            PMC: P9515_08171(rpe)
            PMF: P9303_16821(rpe)
            PMG: P9301_08261(rpe)
            PMH: P9215_08601(rpe)
            PME: NATL1_08041(rpe)
            TER: Tery_2606
            BTH: BT_3946
            BFR: BF3902
            BFS: BF3672
            PGI: PG1595(rpe)
            CHU: CHU_1605(rpe)
            GFO: GFO_0377(cbbE)
            FJO: Fjoh_1432
            FPS: FP2049(rpe)
            CTE: CT1670(rpe)
            CCH: Cag_0175
            CPH: Cpha266_0532
            PVI: Cvib_1438
            PLT: Plut_1649
            DET: DET0642 DET0676
            DEH: cbdb_A627
            DEB: DehaBAV1_0614
            RRS: RoseRS_1777
            RCA: Rcas_2057
            DRA: DR_1401
            DGE: Dgeo_1319
            TTH: TTC1898
            TTJ: TTHA0106
            AAE: aq_968(cbbE2)
            TMA: TM1718
            TPT: Tpet_1014
            TME: Tmel_1525
            FNO: Fnod_0985
            MMP: MMP1114(rpe)
            MMQ: MmarC5_0470
            MMZ: MmarC7_0366
            MAE: Maeo_1504
            MVN: Mevan_0439
            TAC: Ta1315
            TVO: TVN0264
            PTO: PTO0845
STRUCTURES  PDB: 1H1Y  1H1Z  1RPX  1TQJ  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.1
            ExPASy - ENZYME nomenclature database: 5.1.3.1
            ExplorEnz - The Enzyme Database: 5.1.3.1
            ERGO genome analysis and discovery system: 5.1.3.1
            BRENDA, the Enzyme Database: 5.1.3.1
            CAS: 9024-20-8
///
ENTRY       EC 5.1.3.2                  Enzyme
NAME        UDP-glucose 4-epimerase;
            UDP-galactose 4-epimerase;
            uridine diphosphoglucose epimerase;
            galactowaldenase;
            UDPG-4-epimerase;
            uridine diphosphate galactose 4-epimerase;
            uridine diphospho-galactose-4-epimerase;
            UDP-glucose epimerase;
            UDP-galactose 4-epimerase;
            4-epimerase;
            UDPG-4-epimerase;
            uridine diphosphoglucose 4-epimerase;
            uridine diphosphate glucose 4-epimerase;
            UDP-D-galactose 4-epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     UDP-glucose 4-epimerase
REACTION    UDP-glucose = UDP-galactose [RN:R00291]
ALL_REAC    R00291;
            (other) R02984
SUBSTRATE   UDP-glucose [CPD:C00029]
PRODUCT     UDP-galactose [CPD:C00052]
COFACTOR    NAD+ [CPD:C00003]
COMMENT     Requires NAD+. Also acts on UDP-2-deoxyglucose.
REFERENCE   1  [PMID:13057717]
  AUTHORS   LELOIR LF.
  TITLE     Enzymic isomerization and related processes.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 14 (1953) 193-218.
REFERENCE   2
  AUTHORS   Maxwell, E.S. and de Robichon-Szulmajster, H.
  TITLE     Purification of uridine diphosphate galactose-4-epimerase from yeast
            and the identification of protein-bound diphosphopyridine
            nucleotide.
  JOURNAL   J. Biol. Chem. 235 (1960) 308-312.
  ORGANISM  cow [GN:bta], Saccharomyces fragilis
REFERENCE   3
  AUTHORS   Wilson, D.B. and Hogness, D.S.
  TITLE     The enzymes of the galactose operon in Escherichia coli. I.
            Purification and characterization of uridine diphosphogalactose
            4-epimerase.
  JOURNAL   J. Biol. Chem. 239 (1964) 2469-2481.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00052  Galactose metabolism
            PATH: map00520  Nucleotide sugars metabolism
ORTHOLOGY   KO: K01784  UDP-glucose 4-epimerase
GENES       HSA: 2582(GALE)
            MMU: 74246(Gale)
            RNO: 114860(Gale)
            CFA: 487373(GALE)
            GGA: 419686(GALE)
            XLA: 380596(1n569) 432137(MGC80057)
            XTR: 448443(gale)
            DME: Dmel_CG12030
            CEL: C47B2.6
            ATH: AT1G12780(UGE1) AT1G30620(MUR4) AT1G63180(UGE3)
                 AT1G64440(RHD1) AT2G34850(MEE25) AT4G23920(UGE2)
            OSA: 4339812 4342364 4347638
            CME: CMA041C
            SCE: YBR019C(GAL10)
            PIC: PICST_76750(GAL10)
            SPO: SPBC365.14c SPBPB2B2.12c
            ANI: AN4727.2
            AFM: AFUA_3G07910 AFUA_4G14090 AFUA_5G10780
            AOR: AO090010000463
            CNE: CNA06760 CNM00600
            DDI: DDB_0231575(galE)
            CHO: Chro.40292
            TET: TTHERM_00136080
            TBR: Tb11.02.0330
            TCR: 506303.50 506811.190
            LMA: LmjF33.2300
            EHI: 226.t00013
            ECO: b0759(galE)
            ECJ: JW0742(galE)
            ECE: Z0929(galE)
            ECS: ECs0787
            ECC: c0835(galE) c2560
            ECI: UTI89_C0756
            ECP: ECP_0770 ECP_2076
            ECV: APECO1_1329(galE)
            ECW: EcE24377A_0786(galE)
            ECX: EcHS_A0813(galE)
            STY: STY0809(galE)
            STT: t2111(galE)
            SPT: SPA1976(galE)
            SEC: SC0774(galE)
            STM: STM0776(galE)
            YPE: YPO1139(galE)
            YPK: y3043(galE)
            YPM: YP_1020(galE)
            YPA: YPA_1047
            YPN: YPN_2861
            YPS: YPTB1171(galE)
            YPI: YpsIP31758_2855(galE)
            YEN: YE3071(galE)
            SFL: SF0545(galE)
            SFX: S0553(galE)
            SFV: SFV_0581(galE)
            SSN: SSON_0711(galE)
            SBO: SBO_0614(galE)
            SDY: SDY_0706(galE)
            ECA: ECA1389(galE)
            PLU: plu4831(galE)
            SGL: SG0897
            KPN: KPN_00773(galE)
            HIN: HI0351(galE)
            HIT: NTHI0471(galE)
            HDU: HD0829(galE)
            HSO: HS_0789(galE)
            PMU: PM0286(galE)
            MSU: MS0798(galE)
            APL: APL_1301(galE)
            XCC: XCC3696
            XCB: XC_3767
            XCV: XCV3859(galE)
            XAC: XAC3740
            VCH: VCA0774
            VCO: VC0395_0714(galE-2) VC0395_A2639(galE-1)
            VVU: VV1_1342 VV1_1770 VV2_1095
            VVY: VV2639 VV3026 VVA1618
            VPA: VP2400 VPA0879
            VFI: VF0201 VFA0352
            PPR: PBPRA2082(galE) PBPRB0983(galE) PBPRB1065
            PAE: PA1384(galE) PA4068
            PAP: PSPA7_1984
            PPU: PP_0501 PP_3129(galE)
            PST: PSPTO_0678 PSPTO_2900(galE)
            PSB: Psyr_2704 Psyr_4475
            PSP: PSPPH_2479(galE) PSPPH_4519
            PFL: PFL_2971 PFL_5405(galE) PFL_5533
            PFO: Pfl_2824 Pfl_3834 Pfl_5030
            PEN: PSEEN0575 PSEEN1504(wbpV) PSEEN2439(galE)
            PAR: Psyc_0107(galE) Psyc_0651
            PCR: Pcryo_0116
            ACI: ACIAD0096 ACIAD0102(galE) ACIAD1891
            SON: SO_1664(galE)
            SDN: Sden_2597 Sden_2644
            SFR: Sfri_1327
            SAZ: Sama_2224
            SBL: Sbal_1482
            SLO: Shew_1433
            SPC: Sputcn32_1384
            SHE: Shewmr4_2609
            SHM: Shewmr7_2676
            SHN: Shewana3_2783
            SHW: Sputw3181_2717
            ILO: IL0559(galE)
            CPS: CPS_2147(galE)
            PHA: PSHAa0469(galE)
            PAT: Patl_3246
            SDE: Sde_0734
            PIN: Ping_3477
            CBU: CBU_0677 CBU_0829
            MCA: MCA0612(galE-1) MCA2451(galE-2)
            FTU: FTT0791(galE) FTT1459c(wbtF) FTT1462c(wbtC)
            FTF: FTF0791(galE) FTF1459c(wbtF) FTF1462c(wbtC)
            FTW: FTW_0588(galE)
            FTL: FTL_0594 FTL_0597 FTL_1430
            FTH: FTH_0594 FTH_0597 FTH_1393(galE)
            FTA: FTA_1518(galE)
            FTN: FTN_1219(galE) FTN_1425(wbtF)
            NOC: Noc_1516 Noc_2339
            AEH: Mlg_0163
            HCH: HCH_02234 HCH_04939(galE)
            CSA: Csal_1722
            ABO: ABO_0909(galE) ABO_0938(galE)
            AHA: AHA_1113(galE-1) AHA_2893 AHA_4103(galE-2)
            DNO: DNO_0941(galE)
            NME: NMB0064
            NMA: NMA0190(galE2') NMA0203(galE)
            NMC: NMC0048(galE)
            NGO: NGO1896
            CVI: CV_3884(galE)
            RSO: RSp1101(galE)
            REU: Reut_B5374 Reut_B5595
            REH: H16_B0226(galE) H16_B0283
            RME: Rmet_3676
            BMA: BMA1978 BMA1983 BMA2195(galE)
            BMV: BMASAVP1_A0712(galE)
            BML: BMA10299_A2546(galE)
            BMN: BMA10247_2068(galE)
            BXE: Bxe_A3705 Bxe_A3721 Bxe_A3782
            BVI: Bcep1808_0822
            BUR: Bcep18194_A3982 Bcep18194_A3984 Bcep18194_A3986
                 Bcep18194_A5163 Bcep18194_B0473 Bcep18194_B0867
                 Bcep18194_B2716
            BCN: Bcen_0410
            BCH: Bcen2424_0885 Bcen2424_0889
            BAM: Bamb_0763 Bamb_0768
            BPS: BPSL2670 BPSL2674(wbiG) BPSL2679(wbiB)
            BPM: BURPS1710b_3147(galE) BURPS1710b_3152(wbiG)
                 BURPS1710b_3157(wbiB)
            BPL: BURPS1106A_3124(galE)
            BPD: BURPS668_3087(galE)
            BTE: BTH_I1476 BTH_I1481 BTH_I1485(galE)
            BPA: BPP0121
            RFR: Rfer_0713 Rfer_1260
            POL: Bpro_1892
            MPT: Mpe_A1914
            HAR: HEAR0726(galE) HEAR1132 HEAR1137 HEAR1147 HEAR1149
            MMS: mma_0644(galE) mma_2275 mma_2277
            NEU: NE0679 NE1689
            NET: Neut_1879
            NMU: Nmul_A0260 Nmul_A0271 Nmul_A0427 Nmul_A2404
            EBA: ebA3856(galE)
            AZO: azo3173(galE1) azo3389(galE2) azo3583(wbpV)
            DAR: Daro_1236 Daro_1255 Daro_1259
            TBD: Tbd_0099 Tbd_1774 Tbd_2064
            MFA: Mfla_2007
            HPY: HP0360
            HPA: HPAG1_1033
            HHE: HH0380(galE)
            HAC: Hac_0415(galE)
            CJE: Cj1131c(galE)
            CJR: CJE1273(galE)
            CJJ: CJJ81176_1148(galE)
            CJU: C8J_1071(galE)
            CJD: JJD26997_0590(galE)
            CFF: CFF8240_1392(galE)
            CCV: CCV52592_1224(galE)
            CHA: CHAB381_0783(galE)
            CCO: CCC13826_0464(galE)
            ABU: Abu_0666 Abu_2243(pseB)
            SUN: SUN_1933(galE)
            GSU: GSU2240(galE)
            GME: Gmet_1486 Gmet_2329
            PCA: Pcar_1804 Pcar_1807
            PPD: Ppro_2440
            DVU: DVU0319 DVU0342 DVU0554 DVU1360(galE) DVU2996
            DVL: Dvul_2662
            DDE: Dde_0358 Dde_0427 Dde_2187 Dde_2888 Dde_3686 Dde_3691
            LIP: LI0379(galE) LI0466(galE) LIA023(galE) LIC023(galE)
            DPS: DP0026 DP1007 DPPB64
            ADE: Adeh_1060 Adeh_1954
            MXA: MXAN_3507(galE)
            SAT: SYN_01125 SYN_02668
            SFU: Sfum_1718 Sfum_3358
            PUB: SAR11_0538 SAR11_0569(galE)
            MLO: mll1234 mll7878 mlr5697 mlr6767 mlr8551
            MES: Meso_0777 Meso_2780
            SME: SMb20245 SMb20459 SMb20942(exoB) SMc00430 SMc02252(galE)
            ATU: Atu0530(galE) Atu1626 Atu3315(galE) Atu4166(galE)
            ATC: AGR_C_3001 AGR_C_938 AGR_L_1374 AGR_L_3011
            RET: RHE_CH00069(galE1) RHE_CH00569(galE2) RHE_CH00760(ypch00258)
                 RHE_CH01367(ypch00469) RHE_CH02844 RHE_CH03195(ypch01111)
                 RHE_CH03492(ypch01236) RHE_CH03985(galE3)
                 RHE_PB00052(ypb00028) RHE_PB00053(ypb00029) RHE_PF00088
            RLE: RL0078(exoB) RL0559 RL0604(exoB) RL0810 RL0813 RL1758
                 RL3304(galE) RL3628 RL4002 RL4658(exoB) pRL120105 pRL120124
                 pRL120227 pRL120778 pRL90154
            BME: BMEI0921 BMEI1237 BMEII0730
            BMF: BAB1_0734 BAB1_1088(galE-1) BAB2_0694(galE-2)
            BMS: BR1066(galE-1) BRA0543(galE-2)
            BMB: BruAb1_1071(galE-1) BruAb2_0679(galE-2)
            BOV: BOV_1030(galE-2) BOV_A0474(galE-1)
            BJA: bll0593 bll5923 bll6007(galE) bll6421 blr5421 blr5931(galE)
                 blr5989 blr6312(galE) blr7578(exoB)
            BRA: BRADO1793 BRADO2069 BRADO2488 BRADO4824 BRADO4832 BRADO5166
                 BRADO5190 BRADO5207(galE) BRADO6165(exoB) BRADO6182
            BBT: BBta_1046 BBta_1610 BBta_1626(exoB) BBta_2109 BBta_2833
                 BBta_5633 BBta_5674(galE)
            RPA: RPA3990(galE1) RPA4582(galE2)
            RPB: RPB_1012 RPB_1597
            RPC: RPC_1427 RPC_4198 RPC_4439
            RPD: RPD_1115 RPD_1609
            RPE: RPE_1081 RPE_1448 RPE_1509 RPE_1510 RPE_3197 RPE_3508
                 RPE_4271
            NWI: Nwi_0898 Nwi_1065 Nwi_2387
            NHA: Nham_1293 Nham_3022
            CCR: CC_0092 CC_2383
            SIT: TM1040_0016
            RSP: RSP_0159(galE-2) RSP_0520 RSP_0652 RSP_3989
            JAN: Jann_4249
            RDE: RD1_0683 RD1_4203(galE) RD1_B0005 RD1_B0040(galE)
            MMR: Mmar10_2760
            HNE: HNE_1200(galE)
            NAR: Saro_1618 Saro_3275
            SAL: Sala_1559
            ELI: ELI_10930
            GOX: GOX1487
            GBE: GbCGDNIH1_1626
            RRU: Rru_A1486 Rru_A3108 Rru_B0006
            MAG: amb0061 amb0108 amb0122 amb1437
            MGM: Mmc1_0160 Mmc1_0768 Mmc1_1063
            ABA: Acid345_1702 Acid345_3097
            SUS: Acid_5906
            BSU: BG11837(galE)
            BHA: BH1108(galE) BH2891 BH3379 BH3649 BH3715
            BAN: BA0507 BA5505(galE-1) BA5700(galE-2)
            BAR: GBAA0507 GBAA5505(galE-1) GBAA5700(galE-2)
            BAA: BA_0353 BA_0558 BA_1078
            BAT: BAS0263 BAS0479 BAS5114 BAS5304
            BCE: BC0312 BC0488 BC5263 BC5448
            BCA: BCE_0303 BCE_0561 BCE_5380(galE) BCE_5381(galE)
                 BCE_5588(galE)
            BCZ: BCZK0251 BCZK0252 BCZK0418(galE) BCZK0531(galE)
                 BCZK3072(galE) BCZK4960(galE) BCZK5146(galE)
            BTK: BT9727_0248(galE) BT9727_0249(galE) BT9727_0422(galE)
                 BT9727_4945(galE) BT9727_5131(galE)
            BTL: BALH_0271(galE) BALH_0444(galE) BALH_4766(galE)
                 BALH_4958(galE)
            BLI: BL00192(galE) BL01937 BL02665 BL03353 BL03870
            BLD: BLi01280 BLi03803 BLi04041(galE) BLi04190 BLi04283
            BCL: ABC0508 ABC3822(galE)
            BAY: RBAM_012140(galE1) RBAM_036080(galE)
            BPU: BPUM_3207(galE2) BPUM_3467(galE1)
            OIH: OB2082
            GKA: GK2149 GK3296
            SAU: SA0123 SA0157(capN)
            SAV: SAV0128 SAV0162(capN)
            SAM: MW0102 MW0137(cap8N)
            SAR: SAR0130 SAR0164(capN)
            SAS: SAS0102 SAS0137
            SAC: SACOL0113 SACOL0149(cap5N)
            SAB: SAB0067 SAB0103(capN)
            SAA: SAUSA300_0130 SAUSA300_0165(cap5N) SAUSA300_0538
            SAO: SAOUHSC_00088 SAOUHSC_00127
            SSP: SSP0630
            LMO: lmo2477(galE)
            LMF: LMOf2365_2450(galE)
            LIN: lin2620(galE)
            LWE: lwe2425(galE)
            LLA: L0024(galE) L12335(ycbD)
            LLC: LACR_2242
            LLM: llmg_0247 llmg_2003 llmg_2233(galE)
            SPN: SP_1607 SP_1828 SP_1867
            SPR: spr1460(galE) spr1647(galE) spr1683
            SPD: SPD_1432(galE-1) SPD_1612(galE-2)
            SAG: SAG1923(galE)
            SAN: gbs1910
            SAK: SAK_0538(galE) SAK_1882(galE)
            SMU: SMU.2065 SMU.888(galE)
            STC: str1169(galE2) str1400(galE1)
            STL: stu1169(galE2) stu1400(galE1)
            STE: STER_1125
            SSA: SSA_1010(galE) SSA_2219
            SSV: SSU98_1444
            SGO: SGO_0934(galE-2) SGO_1012(galE-1) SGO_2022
            LPL: lp_0709(galE1) lp_1200(galE2) lp_2105(galE3) lp_3481(galE4)
            LJO: LJ0853 LJ1759
            LAC: LBA1469(galE)
            LSA: LSA0765(galE1) LSA1280(galE2)
            LSL: LSL_0382(galE) LSL_0965(gAlE) LSL_1507(galE)
            LDB: Ldb1792(galE)
            LBU: LBUL_1664
            LBR: LVIS_1903
            LCA: LSEI_0665 LSEI_2018
            EFA: EF0646 EF1070(galE-1) EF2165 EF2783(galE-2)
            OOE: OEOE_1402
            STH: STH1370 STH2711 STH2715
            CAC: CAC0794 CAC1429(galE) CAC2334 CAC2960(galE)
            CPE: CPE0286(galE) CPE0509(galE)
            CPF: CPF_0282(galE) CPF_0486(galE)
            CPR: CPR_0273(galE) CPR_0468(galE)
            CTC: CTC00866(galE)
            CNO: NT01CX_1536(galE)
            CDF: CD2714(galE)
            CBO: CBO2679 CBO2777(galE)
            CBA: CLB_2720(galE)
            CBH: CLC_2653(galE)
            CBF: CLI_2829(galE)
            CKL: CKL_1547(galE)
            CHY: CHY_0545(galE) CHY_1057
            DSY: DSY3287
            DRM: Dred_3002
            SWO: Swol_1942
            TTE: TTE1927(galE)
            MTA: Moth_0673
            MGE: MG_118(galE)
            MPN: MPN257(galE)
            MMY: MSC_0971(galE) MSC_0978(galE) MSC_0985(galE)
            MMO: MMOB1930(galE)
            MTU: Rv0501(galE2) Rv0536(galE3) Rv0806c(cpsY) Rv3634c(galE1)
            MTC: MT0522 MT0560 MT3574 MT3736
            MBO: Mb0513(galE2) Mb0550(galE3) Mb0829c(cpsY) Mb3658c(galE1)
            MBB: BCG_0544(galE2) BCG_0580(galE3) BCG_0858c(cpsY)
                 BCG_3692c(galE1)
            MLE: ML0204(rmlB2) ML2428
            MPA: MAP0430(rmlB2) MAP3993(galE1) MAP4031 MAP4032
            MSM: MSMEG_6142
            MUL: MUL_4210(galE1)
            MMC: Mmcs_0671 Mmcs_4789
            CGL: NCgl0317(cgl0323) NCgl1846(cgl1921)
            CGB: cg2104(galE)
            CEF: CE0333 CE0380 CE1813(galE)
            CDI: DIP1415(galE)
            CJK: jk1098(galE)
            NFA: nfa37800(galE) nfa51750
            RHA: RHA1_ro02058 RHA1_ro03648 RHA1_ro04260(galE) RHA1_ro06809
            SCO: SCO2988(galE2) SCO3137(galE1) SCO3326(SCE68.24c)
                 SCO3739(SCH22A.17)
            SMA: SAV1011(galE5) SAV1662(galE6) SAV2239(galE7) SAV357(galE4)
                 SAV3575(galE1) SAV4574(galE2) SAV4732 SAV5086(galE3)
            LXX: Lxx04960(galE) Lxx05210(exoB)
            CMI: CMM_0858(galE2) CMM_1909(cpsY)
            AAU: AAur_2794(galE) AAur_pTC20231(galE)
            PAC: PPA0069
            TFU: Tfu_0169 Tfu_2591 Tfu_2723
            FRA: Francci3_0479 Francci3_0976 Francci3_3475 Francci3_3550
            FAL: FRAAL0508 FRAAL0977(galE) FRAAL1490 FRAAL1626 FRAAL5746(galE)
                 FRAAL6256
            SEN: SACE_1537(galE) SACE_1774(galE) SACE_3345(galE)
                 SACE_3730(galE1) SACE_5693 SACE_6956(galE)
            BLO: BL1644(galE1) BL1671(galE2)
            BAD: BAD_0391(galE2) BAD_0393
            RXY: Rxyl_3113
            FNU: FN0378 FN2109
            RBA: RB1819(galE) RB2500 RB2884(galE) RB3751 RB6269(galE)
            PCU: pc1302(galE)
            TDE: TDE1753(galE)
            LIL: LA1580(galE1) LA1583(galE2) LA1634(galE3) LA3948(galE4)
                 LA4261
            LIC: LIC12149(galE) LIC12199 LIC12202 LIC13153
            LBJ: LBJ_0407(galE)
            LBL: LBL_2670(galE)
            SYN: sll0244(galE) slr1067(galE) slr1078(galE)
            SYW: SYNW0191(galE) SYNW0421 SYNW0445
            SYC: syc1193_c(galE)
            SYF: Synpcc7942_0320
            SYD: Syncc9605_0187
            SYE: Syncc9902_0215
            SYG: sync_0231(galE)
            SYR: SynRCC307_0159(galE)
            SYX: SynWH7803_0092(galE) SynWH7803_0242(galE)
            CYA: CYA_2679(galE)
            CYB: CYB_2194(galE)
            TEL: tlr2206
            GVI: glr2820
            ANA: all2853 all4713
            AVA: Ava_1047 Ava_1957 Ava_2101 Ava_3228 Ava_3352 Ava_3353
            PMA: Pro1314(galE)
            PMM: PMM1209(galE)
            PMT: PMT0086 PMT1907(galE)
            PMN: PMN2A_0221
            PMI: PMT9312_1317 PMT9312_1334
            PMB: A9601_13991(gmd) A9601_14271(galE) A9601_14431
                 A9601_14531(rfbB)
            PMC: P9515_01521(rfbB) P9515_07621 P9515_13681(gmd) P9515_13721
                 P9515_14221 P9515_18321(galE)
            PMF: P9303_01011 P9303_01131 P9303_01181(rfbB) P9303_25441(galE)
                 P9303_26091
            PMG: P9301_14001 P9301_14111(rfbB) P9301_14151(galE)
                 P9301_14241(galE) P9301_14441(gmd)
            PMH: P9215_14131(galE)
            PME: NATL1_03941 NATL1_08531(galE) NATL1_08571(rfbB)
                 NATL1_20961(gmd)
            TER: Tery_2514 Tery_4279
            BTH: BT_0623
            BFR: BF2592
            BFS: BF2613(galE) BF4355
            PGI: PG0347(galE)
            SRU: SRU_1772(galE)
            CHU: CHU_0833(galE) CHU_2411(galE)
            GFO: GFO_1521(galE)
            FPS: FP0406(galE)
            CTE: CT0024(galE)
            CCH: Cag_0517
            PLT: Plut_0420
            DET: DET0204
            DRA: DR_0711 DR_2202
            DGE: Dgeo_2242
            TTH: TTC0222
            TTJ: TTHA0591
            AAE: aq_1069(galE)
            TMA: TM0509
            MMP: MMP1090
            MMQ: MmarC5_0494
            MAC: MA1185 MA4460 MA4464
            MBA: Mbar_A0021 Mbar_A0036 Mbar_A1122
            MMA: MM_1134 MM_1162
            MBU: Mbur_2024 Mbur_2037
            MHU: Mhun_0448 Mhun_2136
            MTH: MTH380
            MST: Msp_0067 Msp_1088(exoB)
            MSI: Msm_0327 Msm_1702
            MKA: MK0724
            HAL: VNG0063G(galE2) VNG0065G(gmd) VNG0752G(galE1)
            HMA: pNG7014(galE3) rrnAC0452(galE) rrnAC0855(galE4)
                 rrnAC2897(galE2) rrnAC3259(galE1)
            HWA: HQ2494A(galE) HQ2650A(galE) HQ2683A(galE) HQ2985A(galE)
                 HQ2986A(galE) HQ3509A(galE) HQ3510A(galE)
            NPH: NP3504A(galE_3) NP4112A(galE_2) NP4662A(galE_1)
            TAC: Ta0011
            TVO: TVN0059
            PTO: PTO0541
            PHO: PH1742
            PAB: PAB1299(galE-2) PAB2145(galE-1)
            PFU: PF0402 PF1788
            TKO: TK1004 TK1708
            RCI: RCIX1448(galE-2) RCIX205(galE-1)
            SSO: SSO0166(galE-2) SSO0809(galE-2)
            STO: ST0187
            SAI: Saci_0761
            PAI: PAE1922(galE-1)
STRUCTURES  PDB: 1A9Y  1A9Z  1EK5  1EK6  1GY8  1HZJ  1I3K  1I3L  1I3M  1I3N  
                 1KVQ  1KVR  1KVS  1KVT  1KVU  1LRJ  1LRK  1LRL  1NAH  1NAI  
                 1UDA  1UDB  1UDC  1XEL  1Z45  2C20  2CNB  2P5U  2P5Y  2UDP  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.2
            ExPASy - ENZYME nomenclature database: 5.1.3.2
            ExplorEnz - The Enzyme Database: 5.1.3.2
            ERGO genome analysis and discovery system: 5.1.3.2
            BRENDA, the Enzyme Database: 5.1.3.2
            CAS: 9032-89-7
///
ENTRY       EC 5.1.3.3                  Enzyme
NAME        aldose 1-epimerase;
            mutarotase;
            aldose mutarotase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     aldose 1-epimerase
REACTION    alpha-D-glucose = beta-D-glucose [RN:R01602]
ALL_REAC    R01602
SUBSTRATE   alpha-D-glucose [CPD:C00267]
PRODUCT     beta-D-glucose [CPD:C00221]
COMMENT     Also acts on L-arabinose, D-xylose, D-galactose, maltose and
            lactose.
REFERENCE   1
  AUTHORS   Bentley, R. and Bhate, D.S.
  TITLE     Mutarotase from Penicillium notatum. I. Purification, assay, and
            general properties of the enzyme.
  JOURNAL   J. Biol. Chem. 235 (1960) 1219-1224.
  ORGANISM  Penicillium notatum
REFERENCE   2
  AUTHORS   Bentley, R. and Bhate, D.S.
  TITLE     Mutarotase from Penicillium notatum. II. The mechanism of the
            mutarotation reaction.
  JOURNAL   J. Biol. Chem. 235 (1960) 1225-1233.
  ORGANISM  Penicillium notatum
REFERENCE   3  [PMID:14915955]
  AUTHORS   KEILIN D, HARTREE EF.
  TITLE     Biological catalysis of mutarotation of glucose.
  JOURNAL   Biochem. J. 50 (1952) 341-8.
  ORGANISM  Penicillium notatum
REFERENCE   4  [PMID:13159947]
  AUTHORS   LEVY GB, COOK ES.
  TITLE     A rotographic study of mutarotase.
  JOURNAL   Biochem. J. 57 (1954) 50-5.
  ORGANISM  Penicillium notatum
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
ORTHOLOGY   KO: K01785  aldose 1-epimerase
GENES       HSA: 130589(GALM)
            PTR: 459166(LOC459166)
            MCC: 713322(LOC713322)
            MMU: 319625(Galm)
            RNO: 313843(Galm)
            CFA: 483039(GALM)
            SSC: 399536(GALM)
            GGA: 426268(GALM)
            DRE: 436646(zgc:92501)
            DME: Dmel_CG10467 Dmel_CG10996 Dmel_CG4988
            CEL: C01B4.6
            ATH: AT3G17940 AT3G47800 AT5G15140
            OSA: 4329753 4332976 4336037
            SCE: YBR019C(GAL10)
            PIC: PICST_76750(GAL10)
            SPO: SPBPB2B2.12c
            ANI: AN3184.2 AN3432.2 AN4727.2
            AFM: AFUA_3G05740 AFUA_3G13240 AFUA_5G10780
            AOR: AO090010000463 AO090012000809 AO090020000042
            UMA: UM01772.1
            TET: TTHERM_00566660
            TCR: 504425.90 509331.180
            LMA: LmjF23.0430 LmjF35.0970
            EHI: 349.t00005
            ECO: b0756(galM)
            ECJ: JW0739(galM)
            ECE: Z0926(galM)
            ECS: ECs0784
            ECC: c0832(galM)
            ECI: UTI89_C0753(galM)
            ECP: ECP_0767 ECP_4093
            ECV: APECO1_1332(galM)
            STY: STY0806(galM)
            STT: t2114(galM)
            SPT: SPA1979(galM)
            SEC: SC0771(galM)
            STM: STM0773(galM)
            YPA: YPA_1043
            YPN: YPN_2865
            YPP: YPDSF_2562
            YPS: YPTB1168(galM)
            YEN: YE2920(galM)
            SFL: SF0548(galM)
            SFX: S0556(galM)
            SFV: SFV_0584(galM)
            SSN: SSON_0708(galM)
            SBO: SBO_0611(galM)
            SDY: SDY_0703(galM)
            ECA: ECA1388(galM)
            PLU: plu0577(galM)
            ENT: Ent638_1247
            SPE: Spro_1290
            HIT: NTHI0982(galM)
            HIP: CGSHiEE_07970(galM)
            HIQ: CGSHiGG_07590(galM)
            HSO: HS_0236(galM)
            PMU: PM1034(galM)
            MSU: MS0649(galM)
            ASU: Asuc_1901
            XCC: XCC1192(galM)
            XCB: XC_3050
            XCV: XCV1336
            XAC: XAC1287(galM)
            XOO: XOO1318(galM)
            XOM: XOO_1212(XOO1212)
            VCH: VC1594
            VCO: VC0395_A1196(galM)
            VVU: VV1_1773
            VVY: VV2636
            VPA: VP2397
            VFI: VFA0356
            PPR: PBPRA2079(galM)
            PST: PSPTO_2636(galM)
            PSB: Psyr_2369
            PSP: PSPPH_2504(galM)
            PFO: Pfl_3731
            SON: SO_0693(galM)
            SDN: Sden_0413
            SFR: Sfri_3669
            SAZ: Sama_0535
            SBL: Sbal_3729
            SBM: Shew185_0633
            SLO: Shew_3272
            SPC: Sputcn32_2060 Sputcn32_3250
            SSE: Ssed_4021
            SPL: Spea_0576
            SHE: Shewmr4_1985 Shewmr4_3409
            SHM: Shewmr7_0543 Shewmr7_1989
            SHN: Shewana3_2072 Shewana3_3579
            SHW: Sputw3181_0691 Sputw3181_1952
            PHA: PSHAa1767(galM)
            PAT: Patl_2682 Patl_3534
            SDE: Sde_0788 Sde_1187
            PIN: Ping_2018 Ping_2506
            FTW: FTW_0086
            FTN: FTN_1127(galM)
            CSA: Csal_0799
            MMW: Mmwyl1_2717
            AHA: AHA_4106(galM)
            NME: NMB0389
            NMA: NMA2099(galM)
            NMC: NMC1778(galM)
            CVI: CV_1395(galM)
            REH: H16_A2863(galM)
            BXE: Bxe_B1758 Bxe_B2624
            BVI: Bcep1808_5646 Bcep1808_6453
            BCN: Bcen_1457 Bcen_6508
            BCH: Bcen2424_6371 Bcen2424_6742
            BAM: Bamb_5727 Bamb_6330
            BTE: BTH_I2336
            POL: Bpro_3100
            DDE: Dde_3655
            MLO: mll1167
            MES: Meso_0451
            SME: SMc03798(galM)
            SMD: Smed_3031
            ATU: Atu2719(galM)
            ATC: AGR_C_4929
            RET: RHE_CH04034(galM)
            RLE: RL4605(galM)
            BME: BMEI1109
            BMF: BAB1_0876(galM)
            BMS: BR0857(galM)
            BMB: BruAb1_0869(galM)
            BOV: BOV_0850(galM)
            OAN: Oant_2369
            BJA: blr3206
            BRA: BRADO1815
            BBT: BBta_2135
            XAU: Xaut_1020
            CCR: CC_1418
            SIL: SPO0857(galM)
            SIT: TM1040_0030
            RSP: RSP_3572(galM)
            RSH: Rsph17029_3254
            RSQ: Rsph17025_3149
            RDE: RD1_3109(galM)
            PDE: Pden_2751
            ZMO: ZMO0889(mro)
            NAR: Saro_0819
            SAL: Sala_0738
            GOX: GOX0748
            GBE: GbCGDNIH1_0796
            ACR: Acry_1033
            ABA: Acid345_0321 Acid345_1147
            SUS: Acid_1458
            BHA: BH2755
            BCA: BCE_2212(galM)
            BCZ: pE33L466_0354(galM)
            BCL: ABC0574
            BPU: BPUM_3589
            OIH: OB2208
            GKA: GK1877
            SAU: SA2129
            SAV: SAV2338
            SAM: MW2258
            SAR: SAR2424
            SAS: SAS2230
            SAC: SACOL2332(galM)
            SAB: SAB2215c
            SAA: SAUSA300_2285(galM)
            SAO: SAOUHSC_02614
            SAJ: SaurJH9_2363
            SAH: SaurJH1_2407
            SEP: SE1913
            SER: SERP1926(galM)
            SHA: SH0718
            SSP: SSP0566
            LMO: lmo2476
            LMF: LMOf2365_2449(mro)
            LIN: lin2619
            LWE: lwe2424(mro)
            LLA: L0029(galM) L0232(xylM)
            LLC: LACR_1593 LACR_2245
            LLM: llmg_2236(galM)
            SPN: SP_0066
            SPR: spr0065(galM)
            SPD: SPD_0071(galM)
            SAK: SAK_0539
            STC: str1399(galM)
            STL: stu1399(galM)
            SSA: SSA_0062(galM)
            SGO: SGO_0049(galM)
            LPL: lp_0826(galM1) lp_1731(galM2) lp_3487(galM3)
            LJO: LJ0861
            LAC: LBA1457(galM)
            LSA: LSA0767(galM)
            LSL: LSL_1281(galM) LSL_1503(galM)
            LDB: Ldb1268
            LBR: LVIS_1908
            LCA: LSEI_0668
            LRE: Lreu_1538
            EFA: EF0955 EF1068(galM)
            OOE: OEOE_0301
            CAC: CAC1349(galM)
            CPE: CPE1344
            CPF: CPF_1551
            CPR: CPR_1344
            CBE: Cbei_4465
            AMT: Amet_3800
            CJK: jk0287
            RHA: RHA1_ro04996
            SCO: SCO2393(SC4A7.21) SCO2407(SC4A7.35)
            SMA: SAV5766(galM1) SAV5782(galM2)
            PAC: PPA1015
            FAL: FRAAL2426
            ACE: Acel_1611
            KRA: Krad_0282 Krad_0621 Krad_3640
            SEN: SACE_0644(yihR) SACE_3904(yihR)
            FNU: FN1707
            RBA: RB1220(galM) RB6537(galM)
            TDE: TDE1357(galM)
            BTH: BT_0356 BT_0372 BT_2849 BT_3529 BT_3532
            BFR: BF0352 BF1655 BF4385
            BFS: BF0300 BF1663 BF4183
            PGI: PG1632(galM)
            GFO: GFO_0700(mro) GFO_2150(mro)
            FJO: Fjoh_1115 Fjoh_1122 Fjoh_2026
            RRS: RoseRS_2311
            RCA: Rcas_3154
            DGE: Dgeo_2798
            TMA: TM0282
            TPT: Tpet_0630
            FNO: Fnod_1210
            PTO: PTO0756
STRUCTURES  PDB: 1L7J  1L7K  1LUR  1MMU  1MMX  1MMY  1MMZ  1MN0  1NS0  1NS2  
                 1NS4  1NS7  1NS8  1NSM  1NSR  1NSS  1NSU  1NSV  1NSX  1NSZ  
                 1SNZ  1SO0  1YGA  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.3
            ExPASy - ENZYME nomenclature database: 5.1.3.3
            ExplorEnz - The Enzyme Database: 5.1.3.3
            ERGO genome analysis and discovery system: 5.1.3.3
            BRENDA, the Enzyme Database: 5.1.3.3
            CAS: 9031-76-9
///
ENTRY       EC 5.1.3.4                  Enzyme
NAME        L-ribulose-5-phosphate 4-epimerase;
            phosphoribulose isomerase;
            ribulose phosphate 4-epimerase;
            L-ribulose-phosphate 4-epimerase;
            L-ribulose 5-phosphate 4-epimerase;
            AraD;
            L-Ru5P
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     L-ribulose-5-phosphate 4-epimerase
REACTION    L-ribulose 5-phosphate = D-xylulose 5-phosphate [RN:R05850]
ALL_REAC    R05850
SUBSTRATE   L-ribulose 5-phosphate [CPD:C01101]
PRODUCT     D-xylulose 5-phosphate [CPD:C00231]
COMMENT     Requires a divalent cation for activity.
REFERENCE   1  [PMID:13539036]
  AUTHORS   BURMA DP, HORECKER BL.
  TITLE     Not Available
  JOURNAL   J. Biol. Chem. 231 (1958) 1053-64.
  ORGANISM  Lactobucillus plantarum
REFERENCE   2  [PMID:4395381]
  AUTHORS   Deupree JD.
  TITLE     Wood WA: L-ribulose 5-phosphate 4-epimerase of Aerobacter aerogenes.
            Evidence for nicotinamide adenine dinucleotide-independent
            4-epimerization by the crystalline enzyme.
  JOURNAL   J. Biol. Chem. 245 (1970) 3988-95.
  ORGANISM  Aerobacter aerogenes
REFERENCE   3  [PMID:4879898]
  AUTHORS   Lee N, Patrick JW, Masson M.
  TITLE     Crystalline L-ribulose 5-phosphate 4-epimerase from Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 243 (1968) 4700-5.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:13549442]
  AUTHORS   WOLIN MJ, SIMPSON FJ, WOOD WA.
  TITLE     Degradation of L-arabinose by Aerobacter aerogenes. III.
            Identification and properties of L-ribulose-5-phosphate 4-epimerase.
  JOURNAL   J. Biol. Chem. 232 (1958) 559-75.
  ORGANISM  Aerobacter aerogenes
REFERENCE   5  [PMID:8520491]
  AUTHORS   Andersson A, Schneider G, Lindqvist Y.
  TITLE     Purification and preliminary X-ray crystallographic studies of
            recombinant L-ribulose-5-phosphate 4-epimerase from Escherichia
            coli.
  JOURNAL   Protein. Sci. 4 (1995) 1648-50.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:10769139]
  AUTHORS   Lee LV, Poyner RR, Vu MV, Cleland WW.
  TITLE     Role of metal ions in the reaction catalyzed by
            L-ribulose-5-phosphate 4-epimerase.
  JOURNAL   Biochemistry. 39 (2000) 4821-30.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   7  [PMID:11732896]
  AUTHORS   Samuel J, Luo Y, Morgan PM, Strynadka NC, Tanner ME.
  TITLE     Catalysis and binding in L-ribulose-5-phosphate 4-epimerase: a
            comparison with L-fuculose-1-phosphate aldolase.
  JOURNAL   Biochemistry. 40 (2001) 14772-80.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K01786  L-ribulose-5-phosphate 4-epimerase
            KO: K03077  L-ribulose-5-phosphate 4-epimerase
            KO: K03080  L-ribulose-5-phosphate 4-epimerase
GENES       ECO: b0061(araD) b3583(sgbE) b4198(sgaE)
            ECJ: JW0060(araD) JW3555(sgbE) JW4156(ulaF)
            ECE: Z0069(araD) Z5807(sgaE)
            ECS: ECs0065 ECs5174
            ECC: c0073(araD) c4406(sgbE) c5288(sgaE)
            ECI: UTI89_C0066(araD) UTI89_C4127(sgbE) UTI89_C4798(sgaE)
            ECP: ECP_0062 ECP_3688 ECP_4443
            ECV: APECO1_1923(araC) APECO1_2194(sgaE)
            ECW: EcE24377A_0063(araD) EcE24377A_4080(sgbE)
                 EcE24377A_4759(ulaF)
            ECX: EcHS_A0065 EcHS_A3787(sgbE) EcHS_A4442(ulaF)
            STY: STY0118(araD) STY4119(yiaS) STY4744(sgaE)
            STT: t0105(araD) t3842(yiaS) t4439(sgaE)
            SPT: SPA0103(araD) SPA3528(yiaS) SPA4205(sgaE)
            SEC: SC0095(araD) SC4262(sgaE)
            STM: STM0101(araD) STM3677(sgbE) STM4388(sgaE)
            YPE: YPO2230(araD) YPO3326(araD)
            YPK: y0863(araD) y2072(araD)
            YPM: YP_0360(araD1) YP_2029(araD3)
            YPA: YPA_1590 YPA_2818
            YPN: YPN_0767 YPN_1699
            YPP: YPDSF_0904 YPDSF_3034
            YPS: YPTB0804(araD) YPTB2152(araD)
            YPI: YpsIP31758_1910(araD1) YpsIP31758_3262(araD2)
            SFL: SF0056(araD) SF4353(sgaE)
            SFX: S0058(araD) S4623(sgaE)
            SFV: SFV_0053(araD) SFV_3956(sgbE) SFV_4354(sgaE)
            SSN: SSON_0067(araD) SSON_4380(sgaE)
            SBO: SBO_0048(araD)
            SDY: SDY_0088(araD) SDY_4367(sgaE)
            ECA: ECA1960(araD)
            SGL: SG1415
            ENT: Ent638_0608
            SPE: Spro_2644 Spro_3939
            HIN: HI1025(araD)
            HIQ: CGSHiGG_08780(araD)
            HDU: HD1866(sgbE)
            HSO: HS_0773(araD)
            PMU: PM1244(araD)
            MSU: MS0046(araD)
            APL: APL_1704
            ASU: Asuc_0234
            VCH: VCA0244
            VVU: VV2_1082
            VVY: VVA1606
            PPR: PBPRB0275(sgbE)
            SPC: Sputcn32_2067
            SHE: Shewmr4_1978
            SHM: Shewmr7_1996
            SHN: Shewana3_2065
            SHW: Sputw3181_1945
            SDE: Sde_0773
            HCH: HCH_01844
            AHA: AHA_1901
            BSU: BG11906(araD)
            BHA: BH1871(araD)
            BLI: BL00350(araD) BL01183(araDA)
            BLD: BLi02063 BLi03026(araD)
            BCL: ABC0406(araD)
            BAY: RBAM_025840
            BPU: BPUM_2328
            OIH: OB2798
            GKA: GK1906(araD)
            SPY: SPy_0179(araD)
            SPZ: M5005_Spy_0153(araD)
            SPM: spyM18_0178
            SPG: SpyM3_0140(araD)
            SPS: SPs0143
            SPH: MGAS10270_Spy0155(araD)
            SPI: MGAS10750_Spy0159(araD)
            SPJ: MGAS2096_Spy0161(araD)
            SPK: MGAS9429_Spy0155(araD)
            SPF: SpyM50147
            SPA: M6_Spy0199
            SPB: M28_Spy0151(araD)
            SPN: SP_2033
            SPR: spr1844(araD)
            SPD: SPD_1842(araD)
            SAG: SAG1810
            SAN: gbs1851
            SAK: SAK_1830(araD)
            SMU: SMU.275
            SSA: SSA_2088(araD)
            LPL: lp_3555(araD)
            LSA: LSA1857(araD)
            LBR: LVIS_1741
            LCA: LSEI_2731
            EFA: EF1131(araD)
            CAC: CAC1341(araD)
            CPF: CPF_0648
            CDF: CD2278(araD)
            CBE: Cbei_0549
            MPN: MPN498(araD)
            MPU: MYPU_5990(sgaE)
            MPE: MYPE7160(sgaE)
            MHY: mhp439(araD)
            MSY: MS53_0031(sgaE)
            MSM: MSMEG_1714
            TWH: TWT647(araD)
            TWS: TW669(sgaE)
            CMI: CMM_0877(araD)
            AAU: AAur_3710(araD)
            PAC: PPA0882 PPA2325
            ACE: Acel_0872
            BLO: BL0273(araD)
            PMF: P9303_21771
            BTH: BT_0353
            GFO: GFO_0698(araD)
            TMA: TM0283
STRUCTURES  PDB: 1JDI  1K0W  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.4
            ExPASy - ENZYME nomenclature database: 5.1.3.4
            ExplorEnz - The Enzyme Database: 5.1.3.4
            ERGO genome analysis and discovery system: 5.1.3.4
            BRENDA, the Enzyme Database: 5.1.3.4
            CAS: 9024-19-5
///
ENTRY       EC 5.1.3.5                  Enzyme
NAME        UDP-arabinose 4-epimerase;
            uridine diphosphoarabinose epimerase;
            UDP arabinose epimerase;
            uridine 5'-diphosphate-D-xylose 4-epimerase;
            UDP-D-xylose 4-epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     UDP-L-arabinose 4-epimerase
REACTION    UDP-L-arabinose = UDP-D-xylose [RN:R01473]
ALL_REAC    R01473
SUBSTRATE   UDP-L-arabinose [CPD:C00935]
PRODUCT     UDP-D-xylose [CPD:C00190]
REFERENCE   1  [PMID:13821949]
  AUTHORS   FEINGOLD DS, NEUFELD EF, HASSID WZ.
  TITLE     The 4-epimerization and decarboxylation of uridine diphosphate
            D-glucuronic acid by extracts from Phaseolus aureus seedlings.
  JOURNAL   J. Biol. Chem. 235 (1960) 910-3.
  ORGANISM  Phaseolus aureus
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.5
            ExPASy - ENZYME nomenclature database: 5.1.3.5
            ExplorEnz - The Enzyme Database: 5.1.3.5
            ERGO genome analysis and discovery system: 5.1.3.5
            BRENDA, the Enzyme Database: 5.1.3.5
            CAS: 9024-18-4
///
ENTRY       EC 5.1.3.6                  Enzyme
NAME        UDP-glucuronate 4-epimerase;
            uridine diphospho-D-galacturonic acid;
            UDP glucuronic epimerase;
            uridine diphosphoglucuronic epimerase;
            UDP-galacturonate 4-epimerase;
            uridine diphosphoglucuronate epimerase;
            UDP-D-galacturonic acid 4-epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     UDP-glucuronate 4-epimerase
REACTION    UDP-glucuronate = UDP-D-galacturonate [RN:R01385]
ALL_REAC    R01385
SUBSTRATE   UDP-glucuronate [CPD:C00167]
PRODUCT     UDP-D-galacturonate [CPD:C00617]
REFERENCE   1  [PMID:13821949]
  AUTHORS   FEINGOLD DS, NEUFELD EF, HASSID WZ.
  TITLE     The 4-epimerization and decarboxylation of uridine diphosphate
            D-glucuronic acid by extracts from Phaseolus aureus seedlings.
  JOURNAL   J. Biol. Chem. 235 (1960) 910-3.
  ORGANISM  Phaseolus aureus
PATHWAY     PATH: map00500  Starch and sucrose metabolism
            PATH: map00520  Nucleotide sugars metabolism
ORTHOLOGY   KO: K08679  UDP-glucuronate 4-epimerase
GENES       LSL: LSL_0980
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.6
            ExPASy - ENZYME nomenclature database: 5.1.3.6
            ExplorEnz - The Enzyme Database: 5.1.3.6
            ERGO genome analysis and discovery system: 5.1.3.6
            BRENDA, the Enzyme Database: 5.1.3.6
            CAS: 9024-17-3
///
ENTRY       EC 5.1.3.7                  Enzyme
NAME        UDP-N-acetylglucosamine 4-epimerase;
            UDP acetylglucosamine epimerase;
            uridine diphosphoacetylglucosamine epimerase;
            uridine diphosphate N-acetylglucosamine-4-epimerase;
            uridine 5'-diphospho-N-acetylglucosamine-4-epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     UDP-N-acetyl-D-glucosamine 4-epimerase
REACTION    UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-galactosamine
            [RN:R00418]
ALL_REAC    R00418
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043]
PRODUCT     UDP-N-acetyl-D-galactosamine [CPD:C00203]
REFERENCE   1  [PMID:13828347]
  AUTHORS   GLASER L.
  TITLE     The biosynthesis of N-acetylgalactosamine.
  JOURNAL   J. Biol. Chem. 234 (1959) 2801-5.
  ORGANISM  Bacillus subtilis [GN:bsu], rat [GN:rno]
REFERENCE   2
  AUTHORS   Kornfeld, S. and Glaser, L.
  TITLE     The synthesis of thymidine-linked sugars. V. Thymidine
            diphosphate-amino sugars.
  JOURNAL   J. Biol. Chem. 237 (1962) 3052-3059.
  ORGANISM  Pseudomonas aeruginosa
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K02473  UDP-N-acetylglucosamine 4-epimerase
GENES       SSN: SSO_P225(wbgU)
            ACI: ACIAD0088
            SON: SO_3189
            CPS: CPS_3643
            BPE: BP1630(wbpP)
            BPA: BPP0792
            BBR: BB2924(wbpP)
            POL: Bpro_3996
            EBA: ebA5873(wbpP)
            DPS: DP0046(wbpP)
            SAT: SYN_01112
            GBE: GbCGDNIH1_0736
            PMB: A9601_13991(gmd) A9601_14271(galE) A9601_14431
                 A9601_14531(rfbB)
            PMC: P9515_01521(rfbB) P9515_07621 P9515_13681(gmd) P9515_13721
                 P9515_14221 P9515_18321(galE)
            PMF: P9303_01011 P9303_01131 P9303_01181(rfbB) P9303_25441(galE)
                 P9303_26091
            PMG: P9301_14001 P9301_14111(rfbB) P9301_14151(galE)
                 P9301_14241(galE) P9301_14441(gmd)
            PME: NATL1_03941 NATL1_08531(galE) NATL1_08571(rfbB)
                 NATL1_20961(gmd)
STRUCTURES  PDB: 1SB8  1SB9  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.7
            ExPASy - ENZYME nomenclature database: 5.1.3.7
            ExplorEnz - The Enzyme Database: 5.1.3.7
            ERGO genome analysis and discovery system: 5.1.3.7
            BRENDA, the Enzyme Database: 5.1.3.7
            CAS: 9024-16-2
///
ENTRY       EC 5.1.3.8                  Enzyme
NAME        N-acylglucosamine 2-epimerase;
            acylglucosamine 2-epimerase;
            N-acetylglucosamine 2-epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     N-acyl-D-glucosamine 2-epimerase
REACTION    N-acyl-D-glucosamine = N-acyl-D-mannosamine [RN:R02652]
ALL_REAC    R02652 > R01207
SUBSTRATE   N-acyl-D-glucosamine [CPD:C03000]
PRODUCT     N-acyl-D-mannosamine [CPD:C00625]
COFACTOR    ATP [CPD:C00002]
COMMENT     Requires catalytic amounts of ATP.
REFERENCE   1
  AUTHORS   Ghosh, S. and Roseman, S.
  TITLE     The sialic acids. V. N-Acyl-D-glucosamine 2-epimerase.
  JOURNAL   J. Biol. Chem. 240 (1965) 1531-1536.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K01787  N-acylglucosamine 2-epimerase
GENES       HSA: 5973(RENBP)
            MMU: 19703(Renbp)
            RNO: 81759(Renbp)
            CFA: 612532(RENBP)
            SSC: 396934(RENBP)
            SPU: 579325(LOC579325)
            ECW: EcE24377A_4403
            BPM: BURPS1710b_0527
            RLE: RL3363
            HNE: HNE_0032 HNE_0782
            RBA: RB3348
            SYN: slr1975
            ANA: all3695
            AVA: Ava_3567
            BTH: BT_0453
            RRS: RoseRS_1977
            RCA: Rcas_3784
STRUCTURES  PDB: 1FP3  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.8
            ExPASy - ENZYME nomenclature database: 5.1.3.8
            ExplorEnz - The Enzyme Database: 5.1.3.8
            ERGO genome analysis and discovery system: 5.1.3.8
            BRENDA, the Enzyme Database: 5.1.3.8
            CAS: 37318-34-6
///
ENTRY       EC 5.1.3.9                  Enzyme
NAME        N-acylglucosamine-6-phosphate 2-epimerase;
            acylglucosamine-6-phosphate 2-epimerase;
            acylglucosamine phosphate 2-epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     N-acyl-D-glucosamine-6-phosphate 2-epimerase
REACTION    N-acyl-D-glucosamine 6-phosphate = N-acyl-D-mannosamine 6-phosphate
            [RN:R02770]
ALL_REAC    R02770 > R02087
SUBSTRATE   N-acyl-D-glucosamine 6-phosphate [CPD:C04136]
PRODUCT     N-acyl-D-mannosamine 6-phosphate [CPD:C00686]
REFERENCE   1
  AUTHORS   Ghosh, S. and Roseman, S.
  TITLE     The sialic acids. IV. N-Acyl-D-glucosamine 6-phosphate 2-epimerase.
  JOURNAL   J. Biol. Chem. 240 (1965) 1525-1530.
  ORGANISM  Aerobacter cloacae
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K01788  N-acylglucosamine-6-phosphate 2-epimerase
GENES       ECO: b3223(nanE)
            ECJ: JW3192(nanE)
            ECE: Z4581(yhcJ)
            ECS: ECs4096
            ECC: c3977(yhcJ)
            ECP: ECP_3306
            ECV: APECO1_3220(nanE)
            STY: STY1166
            STT: t1791
            SPT: SPA1722 SPA3205(nanE)
            SEC: SC1079 SC3275(nanE)
            STM: STM1129 STM3337(nanE)
            YPE: YPO3023
            YPK: y1459
            YPM: YP_2646(nanE)
            YPS: YPTB2741
            SFL: SF3259(nanE)
            SFX: S3476(yhcJ)
            SFV: SFV_3248(yhcJ)
            SSN: SSON_3364(yhcJ)
            SBO: SBO_3166(yhcJ)
            SDY: SDY_3398(yhcJ)
            SGL: SG1912
            ENT: Ent638_3230
            HIN: HI0145
            HIT: NTHI0231(nanE)
            HIP: CGSHiEE_02560
            HDU: HD1852(nanE)
            HSO: HS_0699(nanE)
            PMU: PM1711
            APL: APL_1752(nanE)
            VCH: VC1781
            VVU: VV2_0734
            VVY: VVA1204
            VFI: VF0666
            PPR: PBPRA2285
            SPL: Spea_1519
            PHA: PSHAb0150(nanE)
            BME: BMEII0857
            BMF: BAB2_0810
            BMS: BRA0411
            BMB: BruAb2_0790
            BCL: ABC0712
            OIH: OB2795
            SAU: SA0307
            SAV: SAV0318
            SAM: MW0295
            SAR: SAR0315
            SAS: SAS0295
            SAC: SACOL0315
            SAB: SAB0255
            SAA: SAUSA300_0318
            SAO: SAOUHSC_00298
            SAJ: SaurJH9_0301
            SAH: SaurJH1_0308
            SHA: SH0279
            SSP: SSP0372
            LMO: lmo2801
            LMF: LMOf2365_2789
            LIN: lin2933
            LWE: lwe2738(nanE)
            LLA: L191486(yljB)
            LLC: LACR_1356
            LLM: llmg_1317
            SPY: SPy_0251
            SPZ: M5005_Spy_0212
            SPM: spyM18_0233
            SPG: SpyM3_0179
            SPS: SPs0184
            SPH: MGAS10270_Spy0211
            SPI: MGAS10750_Spy0206
            SPJ: MGAS2096_Spy0229
            SPK: MGAS9429_Spy0213
            SPF: SpyM50191
            SPA: M6_Spy0243
            SPB: M28_Spy0206
            SPN: SP_1330 SP_1685
            SPR: spr1196(nanE) spr1529(nanE)
            SPD: SPD_1172(nanE-2) SPD_1497(nanE-1)
            SAG: SAG0033
            SAN: gbs0032
            SAK: SAK_0066
            SSA: SSA_0071(nanE)
            SGO: SGO_0118
            LPL: lp_3571
            LJO: LJ0611
            LSA: LSA1641(nanE)
            LSL: LSL_1939(nanE)
            EFA: EF0069 EF0540
            CPE: CPE0184(nanP)
            CPF: CPF_0177(nanE)
            CPR: CPR_0174
            CDF: CD2241(nanE)
            TTE: TTE2420(nanE)
            MPU: MYPU_3630
            MPE: MYPE1740
            MMY: MSC_0555
            MSY: MS53_0197
            MCP: MCAP_0419
            CGL: NCgl2559(cgl2648)
            CGB: cg2933(nanE)
            CDI: DIP0519
            ART: Arth_0182
            PAC: PPA1997
            FNU: FN1476
            BBU: BB0644
            BGA: BG0667
            SYW: SYNW1855
            SYC: syc1640_d
            SYF: Synpcc7942_2464
            SYD: Syncc9605_0614
            SYE: Syncc9902_1748
            SYG: sync_2133
            SYR: SynRCC307_0678(nanE)
            SYX: SynWH7803_1865(nanE)
            TEL: tlr2260
            GVI: glr2614
            PMT: PMT1335
            PMF: P9303_06491
            TER: Tery_1417
            DGE: Dgeo_2395
STRUCTURES  PDB: 1Y0E  1YXY  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.9
            ExPASy - ENZYME nomenclature database: 5.1.3.9
            ExplorEnz - The Enzyme Database: 5.1.3.9
            ERGO genome analysis and discovery system: 5.1.3.9
            BRENDA, the Enzyme Database: 5.1.3.9
            CAS: 37318-35-7
///
ENTRY       EC 5.1.3.10                 Enzyme
NAME        CDP-paratose 2-epimerase;
            CDP-paratose epimerase;
            cytidine diphosphoabequose epimerase;
            cytidine diphosphodideoxyglucose epimerase;
            cytidine diphosphoparatose epimerase;
            cytidine diphosphate paratose-2-epimerase;
            CDP-abequose epimerase (incorrect);
            CDP-D-abequose 2-epimerase (incorrect)
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     CDP-3,6-dideoxy-D-glucose 2-epimerase
REACTION    CDP-3,6-dideoxy-D-glucose = CDP-3,6-dideoxy-D-mannose [RN:R04266]
ALL_REAC    R04266
SUBSTRATE   CDP-3,6-dideoxy-D-glucose [CPD:C03598]
PRODUCT     CDP-3,6-dideoxy-D-mannose [CPD:C03599]
COFACTOR    NAD+ [CPD:C00003]
COMMENT     Requires NAD+. CDP-paratose (CDP-3,6-dideoxy-D-glucose), is more
            systematically called CDP-alpha-3,6-dideoxy-D-ribo-hexose.
            CDP-tyvelose (CDP-3,6-dideoxy-D-mannose) is systematically called
            CDP-3,6-dideoxy-D-arabino-hexose.
REFERENCE   1  [PMID:5924649]
  AUTHORS   Matsuhashi S.
  TITLE     Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. II.
            Reversible 2-epimerization of cytidine diphosphate paratose.
  JOURNAL   J. Biol. Chem. 241 (1966) 4275-82.
  ORGANISM  Salmonella enteritidis, Pasteurella pseudotuberculosis
REFERENCE   2  [PMID:7826006]
  AUTHORS   Liu HW, Thorson JS.
  TITLE     Pathways and mechanisms in the biogenesis of novel deoxysugars by
            bacteria.
  JOURNAL   Annu. Rev. Microbiol. 48 (1994) 223-56.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.10
            ExPASy - ENZYME nomenclature database: 5.1.3.10
            ExplorEnz - The Enzyme Database: 5.1.3.10
            ERGO genome analysis and discovery system: 5.1.3.10
            BRENDA, the Enzyme Database: 5.1.3.10
            CAS: 37318-36-8
///
ENTRY       EC 5.1.3.11                 Enzyme
NAME        cellobiose epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     cellobiose 2-epimerase
REACTION    cellobiose = D-glucosyl-D-mannose [RN:R01445 R06245]
ALL_REAC    R01445 R06245(G)
SUBSTRATE   cellobiose [CPD:C00185]
PRODUCT     D-glucosyl-D-mannose [CPD:C02964]
REFERENCE   1  [PMID:6069974]
  AUTHORS   Tyler TR, Leatherwood JM.
  TITLE     Epimerization of disaccharides by enzyme preparations from
            Ruminococcus albus.
  JOURNAL   Arch. Biochem. Biophys. 119 (1967) 363-7.
  ORGANISM  Ruminococcus albus
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.11
            ExPASy - ENZYME nomenclature database: 5.1.3.11
            ExplorEnz - The Enzyme Database: 5.1.3.11
            ERGO genome analysis and discovery system: 5.1.3.11
            BRENDA, the Enzyme Database: 5.1.3.11
            CAS: 37318-37-9
///
ENTRY       EC 5.1.3.12                 Enzyme
NAME        UDP-glucuronate 5'-epimerase;
            uridine diphosphoglucuronate 5'-epimerase;
            UDP-glucuronic acid 5'-epimerase;
            C-5-uronosyl epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     UDP-glucuronate 5'-epimerase
REACTION    UDP-glucuronate = UDP-L-iduronate [RN:R01387]
ALL_REAC    R01387
SUBSTRATE   UDP-glucuronate [CPD:C00167]
PRODUCT     UDP-L-iduronate [CPD:C02330]
COFACTOR    NAD+ [CPD:C00003]
COMMENT     Requires NAD+.
REFERENCE   1
  AUTHORS   Jacobson, B. and Davidson, E.A.
  TITLE     Biosynthesis of uronic acids by skin enzymes. I. Uridine
            diphosphate-D-glucuronic acid-5-epimerase.
  JOURNAL   J. Biol. Chem. 237 (1962) 638-642.
  ORGANISM  rabbit
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
ORTHOLOGY   KO: K01789  UDP-glucuronate 5'-epimerase
GENES       PEN: PSEEN3360
            SBL: Sbal_0070
            SHE: Shewmr4_3886
            SHM: Shewmr7_3979
            NOC: Noc_2638
            SME: SMc02640(lpsL)
            ATU: Atu4148(lspL)
            ATC: AGR_L_1415
            RET: RHE_CH03247(lpsL)
            RLE: RL3677(lspL)
            SIT: TM1040_3776
            RSP: RSP_3926
            RDE: RD1_B0043
            HNE: HNE_2639
            ZMO: ZMO0941
            RRU: Rru_A3576
            SRU: SRU_0619
            GFO: GFO_0148
            CCH: Cag_1182
            MMQ: MmarC5_0496
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.12
            ExPASy - ENZYME nomenclature database: 5.1.3.12
            ExplorEnz - The Enzyme Database: 5.1.3.12
            ERGO genome analysis and discovery system: 5.1.3.12
            BRENDA, the Enzyme Database: 5.1.3.12
            CAS: 37318-38-0
///
ENTRY       EC 5.1.3.13                 Enzyme
NAME        dTDP-4-dehydrorhamnose 3,5-epimerase;
            dTDP-L-rhamnose synthetase;
            dTDP-L-rhamnose synthetase;
            thymidine diphospho-4-ketorhamnose 3,5-epimerase;
            TDP-4-ketorhamnose 3,5-epimerase;
            dTDP-4-dehydro-6-deoxy-D-glucose 3,5-epimerase;
            TDP-4-keto-L-rhamnose-3,5-epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     dTDP-4-dehydro-6-deoxy-D-glucose 3,5-epimerase
REACTION    dTDP-4-dehydro-6-deoxy-D-glucose = dTDP-4-dehydro-6-deoxy-L-mannose
            [RN:R06514]
ALL_REAC    R06514 > R02774;
            (other) R02775
SUBSTRATE   dTDP-4-dehydro-6-deoxy-D-glucose [CPD:C11907]
PRODUCT     dTDP-4-dehydro-6-deoxy-L-mannose [CPD:C00688]
COMMENT     The enzyme occurs in a complex with EC 1.1.1.133
            dTDP-4-dehydrorhamnose reductase.
REFERENCE   1  [PMID:4199258]
  AUTHORS   Gaugler RW, Gabriel O.
  TITLE     Biological mechanisms involved in the formation of deoxy sugars.
            VII. Biosynthesis of 6-deoxy-L-talose.
  JOURNAL   J. Biol. Chem. 248 (1973) 6041-9.
  ORGANISM  Escherichia coli [GN:eco], Pseudomonas aeruginosa
REFERENCE   2  [PMID:4384782]
  AUTHORS   Melo A, Glaser L.
  TITLE     The mechanism of 6-deoxyhexose synthesis. II. Conversion of
            deoxythymidine diphosphate 4-keto-6-deoxy-D-glucose to
            deoxythymidine diphosphate L-rhamnose.
  JOURNAL   J. Biol. Chem. 243 (1968) 1475-8.
  ORGANISM  Pseudomonas aeruginosa
PATHWAY     PATH: map00520  Nucleotide sugars metabolism
            PATH: map00521  Streptomycin biosynthesis
            PATH: map00523  Polyketide sugar unit biosynthesis
ORTHOLOGY   KO: K01790  dTDP-4-dehydrorhamnose 3,5-epimerase
GENES       CEL: C14F11.6
            ECO: b2038(rfbC)
            ECJ: JW2023(rfbC)
            ECI: UTI89_C2309(rfbC) UTI89_C2317(wcaK)
            ECV: APECO1_1128(rmlC)
            ECW: EcE24377A_2329(rfbC)
            ECX: EcHS_A2179(rfbC)
            STY: STY2304(rfbC)
            STT: t0778(rfbC)
            SPT: SPA0772(rfbC)
            STM: STM2094(rfbC)
            SFL: SF2101(rfbC)
            SFX: S2223(rfbC)
            SFV: SFV_2095(rfbC)
            SBO: SBO_0865(rfbC)
            SDY: SDY_2207(rfbC)
            ECA: ECA1441(rfbC)
            ENT: Ent638_2651
            ASU: Asuc_0832
            XFA: XF0257
            XFT: PD0210(rfbD)
            XCC: XCC0623(rmlC) XCC2013(rfbD)
            XCB: XC_2171 XC_3611
            XCV: XCV3707(rmlC)
            XAC: XAC3583(rmlC)
            XOO: XOO0794(rmlC)
            XOM: XOO_0722(XOO0722)
            VVY: VV0303
            VPA: VP0229
            VFI: VF0168
            PAE: PA5164(rmlC)
            PAU: PA14_68210(rmlC)
            PAP: PSPA7_5903(rfbC)
            PPU: PP_0265 PP_1782(rmlC)
            PPF: Pput_0280 Pput_3923
            PST: PSPTO_1077(rfbC-1) PSPTO_5397(rfbC-2)
            PSB: Psyr_4936
            PSP: PSPPH_0149(rfbC)
            PFL: PFL_0303(rfbC)
            PFO: Pfl_0289 Pfl_1512
            PEN: PSEEN0251(rmlC)
            PMY: Pmen_4291
            PAR: Psyc_1215(rfbC)
            PCR: Pcryo_0626
            ACI: ACIAD0080(rmlC)
            SON: SO_3160(rfbC)
            SDN: Sden_2548 Sden_2655 Sden_2660
            SFR: Sfri_2759 Sfri_2827
            SAZ: Sama_2237
            SBL: Sbal_2865 Sbal_2887
            SBM: Shew185_2882 Shew185_2898
            SLO: Shew_1404 Shew_3703
            SPC: Sputcn32_2537 Sputcn32_3890
            SSE: Ssed_0108 Ssed_3012
            SPL: Spea_1420
            SHE: Shewmr4_1339
            SHM: Shewmr7_1404
            SHN: Shewana3_1382 Shewana3_1392 Shewana3_2825
            SHW: Sputw3181_1466 Sputw3181_1476
            PAT: Patl_2130 Patl_3061
            PIN: Ping_3462
            MAQ: Maqu_2628
            CBU: CBU_1838(rfbC)
            CBD: COXBU7E912_0068(rfbC)
            LPN: lpg0756
            LPF: lpl0793(rmlC)
            LPP: lpp0822(rmlC)
            MCA: MCA1284(rfbC)
            TCX: Tcr_1686
            NOC: Noc_0775
            AEH: Mlg_2320
            HCH: HCH_02409(rfbC)
            ABO: ABO_0914(rmlC)
            MMW: Mmwyl1_0839
            AHA: AHA_2905(rfbC-1) AHA_4164(rfbC-2)
            NME: NMB0081
            NMA: NMA0187(rfbC2) NMA0206(rfbC)
            NMC: NMC0045(rfbC) NMC0065(rfbC2)
            CVI: CV_4013(rfbC)
            RSO: RSc0685(rfbC)
            REU: Reut_A0715
            REH: H16_A1848(rfbC) H16_A2906
            RME: Rmet_2732
            BMA: BMA1988(rfbC)
            BMV: BMASAVP1_A0925(rfbC)
            BML: BMA10299_A2755(rfbC)
            BMN: BMA10247_1850(rfbC)
            BXE: Bxe_A2982 Bxe_A3800 Bxe_B1735 Bxe_C1092
            BVI: Bcep1808_0807 Bcep1808_3214
            BUR: Bcep18194_A3971
            BCN: Bcen_0391
            BCH: Bcen2424_0873 Bcen2424_6650
            BAM: Bamb_0753 Bamb_3385
            BPS: BPSL2684(rmlC)
            BPL: BURPS1106A_3139(rfbC)
            BPD: BURPS668_3102(rfbC)
            BTE: BTH_I1471
            PNU: Pnuc_0256
            BPE: BP0107(rfbC)
            BPA: BPP0171(rfbC)
            BBR: BB0173(rfbC)
            RFR: Rfer_1252 Rfer_2678
            POL: Bpro_4017
            PNA: Pnap_3488
            AAV: Aave_4163
            AJS: Ajs_0540
            VEI: Veis_0695 Veis_4418
            MPT: Mpe_A0625
            HAR: HEAR1154(rfbC)
            MMS: mma_2251(rfbC)
            NEU: NE0678(rmlC)
            NET: Neut_2244
            NMU: Nmul_A0267
            EBA: ebA2275(rmlC)
            AZO: azo1874(rmlC)
            DAR: Daro_1239 Daro_1258
            TBD: Tbd_1778
            MFA: Mfla_2010
            CJE: Cj1430c
            CJD: JJD26997_0704
            ABU: Abu_0695
            SUN: SUN_1716(rfbC)
            PCA: Pcar_1129 Pcar_2596
            PPD: Ppro_2118 Ppro_3347
            DVU: DVU0074 DVU0698(rfbC)
            DVL: Dvul_2266
            DDE: Dde_2930 Dde_3696
            LIP: LIC004(rfbC)
            DPS: DP2223
            ADE: Adeh_4289
            MXA: MXAN_4610(rfbC)
            SAT: SYN_00576
            SFU: Sfum_2265
            MLO: mlr7551
            MES: Meso_2761
            PLA: Plav_3305 Plav_3351
            SME: SMb21325(expA8) SMb21428(rmlC)
            SMD: Smed_4722 Smed_4813
            ATU: Atu4618(rfbC) Atu4799(rfbC)
            ATC: AGR_L_166 AGR_L_529
            RET: RHE_CH01515(ypch00522)
            RLE: RL0243 RL1626(rfbC)
            BME: BMEII0830 BMEII0836
            BMS: BRA0437(rfbC)
            BOV: BOV_A0379(rfbC)
            OAN: Oant_2720 Oant_3389
            BRA: BRADO4830 BRADO7027(rfbC)
            BBT: BBta_1049 BBta_1070(rfbC)
            RPA: RPA0118(rmlC)
            RPB: RPB_1563
            RPC: RPC_4207 RPC_4220
            RPD: RPD_1572
            RPE: RPE_4256
            NWI: Nwi_0546
            NHA: Nham_1060 Nham_2769 Nham_3055
            XAU: Xaut_3548 Xaut_3553
            CCR: CC_3633
            SIT: TM1040_3863
            RSP: RSP_0024(rfbC) RSP_3843(rfbC)
            RSH: Rsph17029_1653 Rsph17029_4079
            RSQ: Rsph17025_2178
            JAN: Jann_3844
            RDE: RD1_B0020(rfbC)
            PDE: Pden_2122
            MMR: Mmar10_2457
            HNE: HNE_0779(rfbC)
            NAR: Saro_3237
            SWI: Swit_4018 Swit_4542
            GOX: GOX1051
            GBE: GbCGDNIH1_0104
            ACR: Acry_0593 Acry_0612 Acry_1216
            RRU: Rru_B0038
            MAG: amb0049 amb0124
            MGM: Mmc1_2443 Mmc1_3490
            SUS: Acid_6227
            BSU: BG14195(spsL)
            BHA: BH3366(rfbC)
            BAN: BA1229(rfbC)
            BAR: GBAA1229(rfbC)
            BAA: BA_1764
            BAT: BAS1136
            BCE: BC1213
            BCA: BCE_1336(rfbC)
            BCZ: BCZK1110(rfbC)
            BCY: Bcer98_0938
            BTK: BT9727_1116(rfbC)
            BCL: ABC3690(spsL)
            BPU: BPUM_3426(spsL)
            OIH: OB1127
            LMO: lmo1082
            LLA: L198323(cpsM)
            LLC: LACR_0202
            LLM: llmg_0207(rmlC)
            SPY: SPy_0935(cpsFP)
            SPZ: M5005_Spy_0735(cpsFP)
            SPM: spyM18_0992(cpsFP)
            SPG: SpyM3_0647(rmlC)
            SPS: SPs1205
            SPH: MGAS10270_Spy0794(cpsFP)
            SPI: MGAS10750_Spy0829(cpsFP)
            SPJ: MGAS2096_Spy0809 MGAS2096_Spy0810(cpsFP)
            SPK: MGAS9429_Spy0793(cpsFP)
            SPF: SpyM51072(rmlC)
            SPA: M6_Spy0761
            SPB: M28_Spy0715(cpsFP)
            SPR: spr0321(cps2M)
            SPD: SPD_0329(rfbC)
            SAG: SAG1199
            SAN: gbs1272(rmlC)
            SAK: SAK_1286(rmlC)
            SMU: SMU.1460(rmlC)
            STC: str1243(rmlC)
            STL: stu1243(rmlC)
            SSA: SSA_2349(galE1)
            SGO: SGO_1010(rmlC)
            LPL: lp_1188(rfbC)
            LJO: LJ1051
            LSL: LSL_1571(rfbC)
            LBU: LBUL_1836
            LCA: LSEI_2014
            EFA: EF2193(rfbC)
            OOE: OEOE_1448
            CAC: CAC2331
            CPE: CPE0617(rfbC)
            CPF: CPF_0480(rfbC) CPF_0598(rfbC)
            CTH: Cthe_1366 Cthe_2560
            CBO: CBO2715
            CBA: CLB_2656(rfbC)
            CBH: CLC_2589(rfbC)
            CBE: Cbei_2601 Cbei_4755
            CHY: CHY_0977(rfbC)
            DRM: Dred_3037
            MTA: Moth_0165
            MTU: Rv3465(rmlC)
            MTC: MT3571(strM)
            MBO: Mb3494(rmlC)
            MBB: BCG_3530(rmlC)
            MLE: ML1965(rmlC)
            MPA: MAP0965c MAP4224c(rmlC)
            MAV: MAV_4407(rfbC)
            MSM: MSMEG_1510 MSMEG_5977(rfbC)
            MVA: Mvan_0213 Mvan_1364
            MMC: Mmcs_1065
            MKM: Mkms_1081
            MJL: Mjls_1092
            CGL: NCgl0326(cgl0333)
            CGB: cg0402(rmlCD)
            CEF: CE0343
            CDI: DIP0361
            CJK: jk1883(rmlC)
            NFA: nfa2060(rfbC)
            RHA: RHA1_ro04096 RHA1_ro05744
            SCO: SCO0400(SCF62.26)
            SMA: SAV949(aveBV)
            TWH: TWT031(rmlC)
            TWS: TW035
            LXX: Lxx04920(rmlC)
            CMI: CMM_1012(rmlC)
            AAU: AAur_2164(rfbC) AAur_3161(rfbC)
            FRA: Francci3_3752 Francci3_3940
            FAL: FRAAL5989(rfbC) FRAAL6255
            ACE: Acel_0568
            KRA: Krad_0571
            SEN: SACE_0714(eryBVII) SACE_6416(rmlC)
            STP: Strop_2217
            BLO: BL0228
            BAD: BAD_1508(rmlCD)
            RXY: Rxyl_3120
            FNU: FN1699 FN1847
            PCU: pc0124(rfbC)
            LIL: LA1633 LA1659(rfbC)
            LIC: LIC12126(rfbC) LIC12150
            LBJ: LBJ_1181(rmlC)
            LBL: LBL_1235(rmlC)
            SYN: slr0985(rfbC) slr1933(rfbC)
            SYW: SYNW0648(rfbC)
            SYC: syc1442_d(rfbC) syc1995_c(rfbC)
            SYF: Synpcc7942_0058 Synpcc7942_2098
            SYD: Syncc9605_2033
            SYE: Syncc9902_0636
            SYR: SynRCC307_0082(rfbC)
            SYX: SynWH7803_0103(rfbC)
            TEL: tll0456(rfbC)
            GVI: gll2205(rfbC) gll3702(rfbC) glr0470(rfbC)
            ANA: alr2830(rfbC) alr4489(rfbC)
            AVA: Ava_1113 Ava_3354
            PMT: PMT0113(rfbC)
            PMN: PMN2A_1240
            PMB: A9601_14061(rfbC)
            PMC: P9515_14111(rfbC)
            PMF: P9303_00941(rfbC)
            PMH: P9215_14511(rfbC)
            PME: NATL1_08551(rfbC)
            TER: Tery_1346
            BTH: BT_0828 BT_1338
            BFR: BF0806 BF2296
            BFS: BF2385(rfbC2) BF3452(rfbC1)
            PGI: PG1562(rfbC)
            SRU: SRU_0590(rfbC)
            CHU: CHU_3843(rmlC)
            GFO: GFO_3287(rfbC)
            FJO: Fjoh_0333
            FPS: FP2479(rmlC)
            CTE: CT0306(rfbC)
            CCH: Cag_0514
            CPH: Cpha266_1997
            PVI: Cvib_0469
            PLT: Plut_0417
            RRS: RoseRS_4097
            RCA: Rcas_3652
            DRA: DR_A0043
            TME: Tmel_1070
            MMQ: MmarC5_1316
            MAE: Maeo_0383
            MAC: MA1909 MA3780(rfbC)
            MBA: Mbar_A0230 Mbar_A1887
            MMA: MM_1166
            MBU: Mbur_2233
            MTP: Mthe_0955
            MHU: Mhun_3074
            MBN: Mboo_1751
            MTH: MTH1790
            MST: Msp_0539
            MSI: Msm_1308
            AFU: AF0323b
            TVO: TVN0901
            PTO: PTO0308 PTO0311
            PHO: PH0416
            PAB: PAB0787(rfbC)
            RCI: RCIX202(rfbC)
            APE: APE_1178
            SSO: SSO0833(rfbC-1) SSO1923(rfbC-2)
            STO: ST1969
            SAI: Saci_1706
            MSE: Msed_1851
            PAS: Pars_0353
            TPE: Tpen_1712
STRUCTURES  PDB: 1DZR  1DZT  1EP0  1EPZ  1NXM  1NYW  1NZC  1PM7  1RTV  1UPI  
                 1WLT  2B9U  2IXC  2IXL  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.13
            ExPASy - ENZYME nomenclature database: 5.1.3.13
            ExplorEnz - The Enzyme Database: 5.1.3.13
            ERGO genome analysis and discovery system: 5.1.3.13
            BRENDA, the Enzyme Database: 5.1.3.13
            CAS: 37318-39-1
///
ENTRY       EC 5.1.3.14                 Enzyme
NAME        UDP-N-acetylglucosamine 2-epimerase;
            UDP-N-acetylglucosamine 2'-epimerase;
            uridine diphosphoacetylglucosamine 2'-epimerase;
            uridine diphospho-N-acetylglucosamine 2'-epimerase;
            uridine diphosphate-N-acetylglucosamine-2'-epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     UDP-N-acetyl-D-glucosamine 2-epimerase
REACTION    UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-mannosamine [RN:R00420]
ALL_REAC    R00420;
            (other) R00414
SUBSTRATE   UDP-N-acetyl-D-glucosamine [CPD:C00043]
PRODUCT     UDP-N-acetyl-D-mannosamine [CPD:C01170]
COMMENT     The enzyme hydrolyses the product to UDP and N-acetyl-D-mannosamine.
REFERENCE   1  [PMID:4770741]
  AUTHORS   Kikuchi K, Tsuiki S.
  TITLE     Purification and properties of UDP-N-acetylglucosamine 2'-epimerase
            from rat liver.
  JOURNAL   Biochim. Biophys. Acta. 327 (1973) 193-206.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K01791  UDP-N-acetylglucosamine 2-epimerase
GENES       HSA: 10020(GNE)
            RNO: 114711(Gne)
            CFA: 481607(GNE)
            SPU: 590539(LOC590539)
            ECO: b3786(rffE)
            ECJ: JW5600(rffE)
            ECE: Z5297(wecB)
            ECS: ECs4719
            ECC: c4706(wecB)
            ECI: UTI89_C3370(neuC) UTI89_C4342(rffE)
            ECP: ECP_3977
            ECV: APECO1_26882(rffE) APECO1_3473(neuC)
            ECW: EcE24377A_4297
            ECX: EcHS_A4003
            STY: STY3635(rffE)
            STT: t3377(wecB)
            SPT: SPA3760(wecB)
            SEC: SC3825(wecB)
            STM: STM3920(wecB)
            YPE: YPO3864(rffE)
            YPK: y0364(wecB)
            YPM: YP_3181(rffE)
            YPA: YPA_0154
            YPN: YPN_0099
            YPP: YPDSF_3482
            YPS: YPTB0170(rffE)
            YPI: YpsIP31758_0184
            YEN: YE0171(nfrC)
            SFL: SF3860(wecB)
            SFX: S3900(wecB)
            SFV: SFV_3718(wecB)
            SSN: SSON_3958(wecB)
            SBO: SBO_3797(wecB)
            SDY: SDY_3962(wecB)
            ECA: ECA4208(wecB)
            PLU: plu4660(wecB) plu4804(wblH)
            SGL: SG2383
            ENT: Ent638_4000
            SPE: Spro_0163
            HDU: HD1843(wecB)
            PMU: PM1009(wbjD)
            APL: APL_1552(wecB)
            XAC: XAC0044(bplD)
            VCH: VC0917
            VCO: VC0395_A0441(wecB)
            VVU: VV1_0780
            VVY: VV0341
            VFI: VF0193
            PAE: PA3148(wbpI)
            PAU: PA14_23370(orfK)
            PAP: PSPA7_1971 PSPA7_1982
            PPU: PP_1811(wecB)
            PST: PSPTO_1196
            PSB: Psyr_1032
            PSP: PSPPH_1083
            PFL: PFL_3595 PFL_5107
            PEN: PSEEN1502 PSEEN2475 PSEEN2963(wecB)
            PMY: Pmen_1709 Pmen_1873
            ACI: ACIAD1175(wecB)
            SAZ: Sama_2261
            SBL: Sbal_0067
            SSE: Ssed_2966 Ssed_2967
            PHA: PSHAa0466(rffE)
            PIN: Ping_0431 Ping_0791
            CBU: CBU_0842(wecB)
            CBD: COXBU7E912_0907
            TCX: Tcr_1457
            NOC: Noc_1976
            AEH: Mlg_0109
            MMW: Mmwyl1_0801 Mmwyl1_0835
            NMA: NMA0199(sacA)
            NMC: NMC0054(sacA)
            CVI: CV_4020(wecB) CV_4033(neuC)
            RSO: RSp0510(epsC2) RSp1017(epsC)
            REU: Reut_B4950
            BXE: Bxe_A3733 Bxe_B0648
            BVI: Bcep1808_0810 Bcep1808_3862 Bcep1808_4142
            BUR: Bcep18194_A3974 Bcep18194_A4466
            BCN: Bcen_0854
            BCH: Bcen2424_1335
            BAM: Bamb_5473
            BPS: BPSS2016(wecB)
            BPM: BURPS1710b_A1131
            BPL: BURPS1106A_A2748
            BPD: BURPS668_A2901
            BTE: BTH_II0340(wecB)
            BPE: BP0090(bplD)
            BPA: BPP0152(bplD)
            BBR: BB0152(bplD)
            RFR: Rfer_0663
            AAV: Aave_0953
            AJS: Ajs_3032
            HAR: HEAR1148
            MMS: mma_2257(wecB1) mma_2283(wecB2) mma_2625(wecB3)
            NEU: NE0486(rffE) NE2249(wbpI)
            NET: Neut_0619
            NMU: Nmul_A0259
            EBA: ebA4257(wbpI) ebA5890
            AZO: azo3278(mnaA)
            DAR: Daro_1265 Daro_2402
            TBD: Tbd_0286
            HHE: HH0082
            WSU: WS2189(wbpI)
            TDN: Tmden_0597 Tmden_1418
            CJE: Cj1328(neuC2)
            CJR: CJE1517(neuC)
            CJJ: CJJ81176_1159
            CJD: JJD26997_0381 JJD26997_0384
            CHA: CHAB381_1479
            CCO: CCC13826_0521 CCC13826_2302
            ABU: Abu_0692
            NIS: NIS_1259(wecB)
            GSU: GSU2243 GSU2245
            GME: Gmet_1489 Gmet_1504
            GUR: Gura_1696
            PPD: Ppro_2450
            BBA: Bd1695(capG)
            ADE: Adeh_2771 Adeh_4176 Adeh_4279 Adeh_4302
            AFW: Anae109_1410
            MXA: MXAN_1101
            SAT: SYN_02683
            SFU: Sfum_3330
            RPR: RP334
            RTY: RT0324(rffE)
            RCO: RC0458(rffE)
            RFE: RF_0540(rffE)
            RBE: RBE_0708(rffE)
            MES: Meso_3697
            RPB: RPB_1535
            RPC: RPC_4203
            RPD: RPD_0749 RPD_2723
            NWI: Nwi_2398
            NHA: Nham_3043
            XAU: Xaut_1736
            NAR: Saro_3149
            SAL: Sala_1590
            SWI: Swit_4666
            ELI: ELI_13265
            RRU: Rru_A1493 Rru_A2740
            MAG: amb0102
            MGM: Mmc1_0561 Mmc1_0587
            ABA: Acid345_1025 Acid345_3306
            SUS: Acid_7476
            BSU: BG10403(yvyH)
            BAN: BA5433 BA5509
            BAR: GBAA5433 GBAA5509
            BAA: BA_0286
            BAT: BAS5048 BAS5117
            BCE: BC5201
            BCA: BCE_5307
            BCZ: BCZK4893(mnaA) BCZK4964(mnaA)
            BCY: Bcer98_3744
            BTK: BT9727_4878
            BTL: BALH_4693
            BLI: BL02459(mnaA)
            BLD: BLi03812(yvyH)
            BAY: RBAM_032810
            BPU: BPUM_3218
            GKA: GK3162
            GTN: GTNG_3104
            SAU: SA0159(capP) SA1913(mnaA)
            SAV: SAV0164(capP) SAV2111(mnaA)
            SAM: MW0139(cap8P) MW2035(mnaA)
            SAR: SAR0166(capP) SAR2199(mnaA)
            SAS: SAS0139 SAS2014
            SAC: SACOL0142(cap5G) SACOL0151(cap5P) SACOL2103
            SAB: SAB0105(capP) SAB1995c(mnaA)
            SAA: SAUSA300_0158(cap5G) SAUSA300_0167(cap5P) SAUSA300_2065
            SAO: SAOUHSC_00120 SAOUHSC_00129 SAOUHSC_02352
            SAJ: SaurJH9_0141 SaurJH9_0150 SaurJH9_2147
            SAH: SaurJH1_0146 SaurJH1_0155 SaurJH1_2185
            SEP: SE1708
            SER: SERP1717
            SHA: SH0394(capG) SH0924(mnaA)
            SSP: SSP0773
            LMO: lmo2537
            LMF: LMOf2365_2510
            LIN: lin2681
            LWE: lwe2486
            LLA: L98310(ymjF)
            SPN: SP_0357 SP_0360
            SAG: SAG1160(neuC)
            SAN: gbs1235(neuC)
            SAK: SAK_1249(neuC)
            SMU: SMU.1437(epsC)
            SSA: SSA_0178(epsC)
            LPL: lp_1173
            LJO: LJ1598
            LAC: LBA0620 LBA1720
            LSA: LSA1520(mnaA)
            LSL: LSL_1276(wecB)
            LDB: Ldb0553
            LBU: LBUL_0493
            LBR: LVIS_1574
            LGA: LGAS_0697
            LRE: Lreu_0312 Lreu_1389
            PPE: PEPE_0597
            EFA: EF2917
            STH: STH82
            CAC: CAC2874 CAC3064
            CPE: CPE2196
            CPF: CPF_2461(mnaA)
            CPR: CPR_2171
            CTC: CTC00311
            CNO: NT01CX_0539 NT01CX_1526 NT01CX_1785
            CTH: Cthe_2601 Cthe_2640
            CDF: CD1033(mnaA)
            CBO: CBO0148(mnaA)
            CBA: CLB_0184(mnaA) CLB_3129
            CBH: CLC_0196(mnaA) CLC_3002
            CBF: CLI_0203(mnaA) CLI_2777 CLI_3159
            CBE: Cbei_0410 Cbei_4627
            CKL: CKL_3166 CKL_3699(epsC)
            AMT: Amet_0207 Amet_0343
            CHY: CHY_2554
            DSY: DSY4924
            DRM: Dred_3031 Dred_3159
            PTH: PTH_2821(wecB)
            SWO: Swol_0184 Swol_0728
            CSC: Csac_1006
            TTE: TTE0155(wecB) TTE0661(wecB2)
            MTA: Moth_2387
            MMC: Mmcs_1315
            MKM: Mkms_1332
            MJL: Mjls_1351
            LXX: Lxx21100(wecB)
            PAC: PPA0148
            FRA: Francci3_1308
            FAL: FRAAL2057(rffE) FRAAL2071
            ACE: Acel_0638
            KRA: Krad_2936
            RXY: Rxyl_2626
            RBA: RB9169(wecB)
            LIL: LA1645
            LIC: LIC12139(rffE)
            LBJ: LBJ_1165
            LBL: LBL_1219
            SYN: slr0624
            SYW: SYNW1830(nfrC)
            SYC: syc0969_c(nfrC)
            SYF: Synpcc7942_0552
            SYD: Syncc9605_0638
            SYE: Syncc9902_1723
            SYG: sync_0169 sync_2159
            SYR: SynRCC307_0714(nfrC)
            SYX: SynWH7803_1840(nfrC)
            CYA: CYA_0107 CYA_0674
            CYB: CYB_2112
            TEL: tll2040
            GVI: glr0701
            ANA: all2497
            AVA: Ava_0429
            PMT: PMT1312(nfrC)
            PMF: P9303_01091 P9303_06751(wecB)
            PMG: P9301_14071
            PME: NATL1_08581(wecB) NATL1_08731
            TER: Tery_2401
            BTH: BT_0383 BT_0601 BT_1202 BT_1203 BT_2944
            BFR: BF1100 BF1844.1 BF2569.1 BF3656 BF4509
            BFS: BF0744 BF1910(wcgT) BF4303
            PGI: PG0120(epsC)
            SRU: SRU_0602
            CHU: CHU_2775(wecB)
            GFO: GFO_0571
            FJO: Fjoh_0304 Fjoh_1039
            FPS: FP1255(neuC)
            CTE: CT2095
            CPH: Cpha266_2553
            PVI: Cvib_1677
            RRS: RoseRS_1131 RoseRS_4430
            RCA: Rcas_0784 Rcas_3971
            DRA: DR_1561
            DGE: Dgeo_1294
            TTH: TTC0285 TTC0948
            TTJ: TTHA1314
            TMA: TM0610 TM1034
            TPT: Tpet_0300 Tpet_0308 Tpet_1716
            TME: Tmel_0366 Tmel_0815
            FNO: Fnod_0229 Fnod_0568
            MJA: MJ1504(wbpI)
            MMP: MMP0357 MMP0705(wbpI)
            MMQ: MmarC5_0871
            MMZ: MmarC7_1732
            MAE: Maeo_0423 Maeo_0485
            MVN: Mevan_0198 Mevan_1583
            MBA: Mbar_A0052 Mbar_A2140
            MMA: MM_1170
            MBU: Mbur_1587 Mbur_2022
            MTP: Mthe_1235
            MHU: Mhun_0382 Mhun_0396
            MEM: Memar_1595 Memar_1605 Memar_2303 Memar_2395
            MTH: MTH837
            MST: Msp_0217
            MSI: Msm_0853
            HMA: pNG7011(wecB)
            PHO: PH1617
            PAB: PAB0379(wlbD)
            PFU: PF0794 PF1630
            TKO: TK1230
            RCI: RCIX1930(wecB)
            IHO: Igni_0623
            TPE: Tpen_1715
STRUCTURES  PDB: 1F6D  1O6C  1V4V  1VGV  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.14
            ExPASy - ENZYME nomenclature database: 5.1.3.14
            ExplorEnz - The Enzyme Database: 5.1.3.14
            ERGO genome analysis and discovery system: 5.1.3.14
            BRENDA, the Enzyme Database: 5.1.3.14
            CAS: 9037-71-2
///
ENTRY       EC 5.1.3.15                 Enzyme
NAME        glucose-6-phosphate 1-epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     D-glucose-6-phosphate 1-epimerase
REACTION    alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate [RN:R02739]
ALL_REAC    R02739
SUBSTRATE   alpha-D-glucose 6-phosphate [CPD:C00668]
PRODUCT     beta-D-glucose 6-phosphate [CPD:C01172]
REFERENCE   1  [PMID:11946648]
  AUTHORS   Wurster B, Hess B.
  TITLE     Glucose-6-phosphate-1-epimerase from baker's yeast. A new enzyme.
  JOURNAL   FEBS. Lett. 23 (1972) 341-344.
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
ORTHOLOGY   KO: K01792  glucose-6-phosphate 1-epimerase
GENES       SAT: SYN_02950
            BME: BMEI1636
            CTA: CTA_0412(pgi)
STRUCTURES  PDB: 2CIQ  2CIR  2CIS  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.15
            ExPASy - ENZYME nomenclature database: 5.1.3.15
            ExplorEnz - The Enzyme Database: 5.1.3.15
            ERGO genome analysis and discovery system: 5.1.3.15
            BRENDA, the Enzyme Database: 5.1.3.15
            CAS: 37259-65-7
///
ENTRY       EC 5.1.3.16                 Enzyme
NAME        UDP-glucosamine 4-epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     UDP-glucosamine 4-epimerase
REACTION    UDP-glucosamine = UDP-galactosamine [RN:R03881]
ALL_REAC    R03881
SUBSTRATE   UDP-glucosamine [CPD:C02200]
PRODUCT     UDP-galactosamine [CPD:C02467]
REFERENCE   1  [PMID:13628700]
  AUTHORS   MALEY F, MALEY GF.
  TITLE     The enzymic conversion of glucosamine to galactosamine.
  JOURNAL   Biochim. Biophys. Acta. 31 (1959) 577-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Silbert, J.E. and Brown, D.H.
  TITLE     Enzymic synthesis of uridine diphosphate glucosamine and heparin
            from [14C]glucosamine by a mouse mast-cell tumor.
  JOURNAL   Biochim. Biophys. Acta 54 (1961) 590-592.
  ORGANISM  mouse [GN:mmu]
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.16
            ExPASy - ENZYME nomenclature database: 5.1.3.16
            ExplorEnz - The Enzyme Database: 5.1.3.16
            ERGO genome analysis and discovery system: 5.1.3.16
            BRENDA, the Enzyme Database: 5.1.3.16
///
ENTRY       EC 5.1.3.17                 Enzyme
NAME        heparosan-N-sulfate-glucuronate 5-epimerase;
            heparosan epimerase;
            heparosan-N-sulfate-D-glucuronosyl 5-epimerase;
            C-5 uronosyl epimerase;
            polyglucuronate epimerase;
            D-glucuronyl C-5 epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     poly[(1,4)-beta-D-glucuronosyl-(1,4)-N-sulfo-alpha-D-glucosaminyl]
            glucurono-5-epimerase
REACTION    heparosan-N-sulfate D-glucuronate = heparosan-N-sulfate L-iduronate
            [RN:R04389]
ALL_REAC    R04389
SUBSTRATE   heparosan-N-sulfate D-glucuronate [CPD:C04196]
PRODUCT     heparosan-N-sulfate L-iduronate [CPD:C04073]
COMMENT     Acts on D-glucuronosyl residues adjacent to sulfated D-glucosamine
            units in the heparin precursor. Not identical with EC 5.1.3.19
            chondroitin-glucuronate 5-epimerase.
REFERENCE   1  [PMID:107165]
  AUTHORS   Backstrom G, Hook M, Lindahl U, Feingold DS, Malmstrom A, Roden L,
            Jacobsson I.
  TITLE     Biosynthesis of heparin. Assay and properties of the microsomal
            uronosyl C-5 epimerase.
  JOURNAL   J. Biol. Chem. 254 (1979) 2975-82.
  ORGANISM  mouse [GN:mmu]
PATHWAY     PATH: map00534  Heparan sulfate biosynthesis
ORTHOLOGY   KO: K01793  heparosan-N-sulfate-glucuronate 5-epimerase
GENES       HSA: 26035(GLCE)
            PTR: 453542(GLCE)
            MMU: 93683(Glce)
            RNO: 363073(RGD1565253_predicted)
            CFA: 487622(GLCE)
            BTA: 281195(GLCE)
            XLA: 432242(MGC79110)
            DRE: 405775(glceb) 405776(glcea)
            SPU: 575562(LOC575562)
            DME: Dmel_CG3194
            CEL: B0285.5(hse-5)
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.17
            ExPASy - ENZYME nomenclature database: 5.1.3.17
            ExplorEnz - The Enzyme Database: 5.1.3.17
            ERGO genome analysis and discovery system: 5.1.3.17
            BRENDA, the Enzyme Database: 5.1.3.17
            CAS: 112567-86-9
///
ENTRY       EC 5.1.3.18                 Enzyme
NAME        GDP-mannose 3,5-epimerase;
            GDP-D-mannose:GDP-L-galactose epimerase;
            guanosine 5'-diphosphate D-mannose:guanosine 5'-diphosphate
            L-galactose epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     GDP-mannose 3,5-epimerase
REACTION    GDP-mannose = GDP-L-galactose [RN:R00889]
ALL_REAC    R00889;
            (other) R07672
SUBSTRATE   GDP-mannose [CPD:C00096]
PRODUCT     GDP-L-galactose [CPD:C02280]
REFERENCE   1  [PMID:7098948]
  AUTHORS   Barber GA, Hebda PA.
  TITLE     GDP-D-mannose: GDP-L-galactose epimerase from Chlorella pyrenoidosa.
  JOURNAL   Methods. Enzymol. 83 (1982) 522-5.
  ORGANISM  Chlorella pyrenoidosa
REFERENCE   2  [PMID:443816]
  AUTHORS   Hebda PA, Behrman EJ, Barber GA.
  TITLE     The guanosine 5'-diphosphate D-mannose: guanosine 5'-diphosphate
            L-galactose epimerase of Chlorella pyrenoidosa. Chemical synthesis
            of guanosine 5'-diphosphate L-galactose and further studies of the
            enzyme and the reaction it catalyzes.
  JOURNAL   Arch. Biochem. Biophys. 194 (1979) 496-502.
  ORGANISM  Chlorella pyrenoidosa
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K10046  GDP-D-mannose 3', 5'-epimerase
GENES       ATH: AT5G28840(GME)
            OSA: 4348636
STRUCTURES  PDB: 2C54  2C59  2C5A  2C5E  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.18
            ExPASy - ENZYME nomenclature database: 5.1.3.18
            ExplorEnz - The Enzyme Database: 5.1.3.18
            ERGO genome analysis and discovery system: 5.1.3.18
            BRENDA, the Enzyme Database: 5.1.3.18
            CAS: 72162-82-4
///
ENTRY       EC 5.1.3.19                 Enzyme
NAME        chondroitin-glucuronate 5-epimerase;
            polyglucuronate 5-epimerase;
            dermatan-sulfate 5-epimerase;
            urunosyl C-5 epimerase;
            chondroitin D-glucuronosyl 5-epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     chondroitin-D-glucuronate 5-epimerase
REACTION    chondroitin D-glucuronate = dermatan L-iduronate [RN:R04104]
ALL_REAC    R04104
SUBSTRATE   chondroitin D-glucuronate
PRODUCT     dermatan L-iduronate [CPD:C00426]
COMMENT     Not identical with EC 5.1.3.17 heparosan-N-sulfate-glucuronate
            5-epimerase.
REFERENCE   1  [PMID:7092807]
  AUTHORS   Malmstrom A, Aberg L.
  TITLE     Biosynthesis of dermatan sulphate. Assay and properties of the
            uronosyl C-5 epimerase.
  JOURNAL   Biochem. J. 201 (1982) 489-93.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00532  Chondroitin sulfate biosynthesis
ORTHOLOGY   KO: K01794  chondroitin-glucuronate 5-epimerase
GENES       HSA: 29940(DSE)
            GGA: 421745(DSE)
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.19
            ExPASy - ENZYME nomenclature database: 5.1.3.19
            ExplorEnz - The Enzyme Database: 5.1.3.19
            ERGO genome analysis and discovery system: 5.1.3.19
            BRENDA, the Enzyme Database: 5.1.3.19
            CAS: 86417-91-6
///
ENTRY       EC 5.1.3.20                 Enzyme
NAME        ADP-glyceromanno-heptose 6-epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     ADP-L-glycero-D-manno-heptose 6-epimerase
REACTION    ADP-D-glycero-D-manno-heptose = ADP-L-glycero-D-manno-heptose
            [RN:R05176]
ALL_REAC    R05176
SUBSTRATE   ADP-D-glycero-D-manno-heptose [CPD:C06397]
PRODUCT     ADP-L-glycero-D-manno-heptose [CPD:C06398]
COFACTOR    NAD+ [CPD:C00003]
COMMENT     Requires NAD+.
REFERENCE   1  [PMID:7929099]
  AUTHORS   Ding L, Seto BL, Ahmed SA, Coleman WG Jr.
  TITLE     Purification and properties of the Escherichia coli K-12
            NAD-dependent nucleotide diphosphosugar epimerase,
            ADP-L-glycero-D-mannoheptose 6-epimerase.
  JOURNAL   J. Biol. Chem. 269 (1994) 24384-90.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:1695830]
  AUTHORS   Raetz CR.
  TITLE     Biochemistry of endotoxins.
  JOURNAL   Annu. Rev. Biochem. 59 (1990) 129-70.
PATHWAY     PATH: map00540  Lipopolysaccharide biosynthesis
ORTHOLOGY   KO: K03274  ADP-L-glycero-D-manno-heptose 6-epimerase
            KO: K06039  
GENES       ECO: b3619(rfaD)
            ECJ: JW3594(rfaD)
            ECE: Z5046(rfaD)
            ECS: ECs4497
            ECC: c4445(rfaD)
            ECI: UTI89_C4164(rfaD)
            ECP: ECP_3719
            ECV: APECO1_2837(rfaD)
            ECW: EcE24377A_4122(rfaD)
            ECX: EcHS_A3830(rfaD)
            STY: STY4085(rfaD)
            STT: t3809(rfaD)
            SPT: SPA3562(rfaD)
            SEC: SC3633(rfaD)
            STM: STM3710(rfaD)
            YPE: YPO0058(rfaD)
            YPK: y0083(rfaD)
            YPM: YP_0059(rfaD)
            YPA: YPA_3484
            YPN: YPN_3792
            YPS: YPTB0055(rfaD)
            YPI: YpsIP31758_0070(rfaD)
            SFL: SF3659(rfaD)
            SFX: S4109(rfaD)
            SFV: SFV_3909(rfaD)
            SSN: SSON_3786(waaD)
            SBO: SBO_3624(rfaD)
            SDY: SDY_4051(rfaD)
            ECA: ECA0165(rfaD)
            PLU: plu4847(rfaD)
            SGL: SG2193
            BFL: Bfl607(rfaD)
            BPN: BPEN_630(hldD)
            HIN: HI1114(rfaD)
            HIT: NTHI1278(rfaD)
            HIP: CGSHiEE_06485(rfaD)
            HIQ: CGSHiGG_09230(rfaD)
            HDU: HD1890(gmhD)
            HSO: HS_1613(rfaD)
            PMU: PM1342(rfaD)
            MSU: MS0146(wcaG)
            APL: APL_1710(hldD)
            VCH: VC0240
            VCO: VC0395_A2620(rfaD)
            VVU: VV1_0796
            VVY: VV0327
            VPA: VP0214(gmhD)
            VFI: VF0152
            PPR: PBPRA0220(gmhD)
            PAE: PA3337(rfaD)
            PAU: PA14_20890(rfaD)
            PAP: PSPA7_1793(rfaD)
            SFR: Sfri_3929
            TCX: Tcr_1517
            NOC: Noc_2614
            AEH: Mlg_2809
            CSA: Csal_0008
            AHA: AHA_4232(rfaD)
            NME: NMB0828
            NMA: NMA1037(rfaD)
            NMC: NMC0773(rfaD)
            NGO: NGO0403
            CVI: CV_3038(rfaD)
            RSO: RSc0915(rfaD)
            REU: Reut_A2563
            RME: Rmet_0728
            BMA: BMA0421(rfaD)
            BMV: BMASAVP1_A2565(rfaD)
            BML: BMA10299_A0940(rfaD)
            BMN: BMA10247_0208(rfaD)
            BXE: Bxe_A0988
            BUR: Bcep18194_A4166
            BCN: Bcen_0574
            BCH: Bcen2424_1053
            BAM: Bamb_0929
            BPS: BPSL2509(gmhD)
            BPM: BURPS1710b_2986(rfaD)
            BPL: BURPS1106A_2939(rfaD)
            BPD: BURPS668_2876(rfaD)
            BTE: BTH_I1644(rfaD)
            BPE: BP0955(rfaD)
            BPA: BPP3123(rfaD)
            BBR: BB3462(rfaD)
            RFR: Rfer_1561
            POL: Bpro_1784
            EBA: ebA3999(wcaG)
            AZO: azo3564(rfaD)
            DAR: Daro_1286
            TBD: Tbd_0963
            MFA: Mfla_0771
            HPY: HP0859(rfaD)
            HPJ: jhp0793(gmhD)
            HPA: HPAG1_0842
            HHE: HH1533
            HAC: Hac_1222(waaD)
            WSU: WS0679(gmhD)
            TDN: Tmden_0579
            CJE: Cj1151c(waaD)
            CJR: CJE1287(waaD)
            CJJ: CJJ81176_1168(waaD)
            CJU: C8J_1097(waaD)
            CJD: JJD26997_0577(waaD)
            CFF: CFF8240_1414(rfaD)
            CCV: CCV52592_0243(rfaD)
            CCO: CCC13826_0576(rfaD)
            ABU: Abu_1796(waaD)
            NIS: NIS_1449
            PCA: Pcar_0024
            DVU: DVU0481(rfaD)
            DDE: Dde_3466
            LIP: LI0621
            BBA: Bd3536(rfaD)
            PUB: SAR11_0572(rfaD)
            MLO: mlr2565
            BJA: bll5928(rfaD)
            BRA: BRADO5202(rfaD)
            BBT: BBta_5669(rfaD)
            RPA: RPA3985
            RPB: RPB_1602
            RPC: RPC_1431
            RPD: RPD_1614
            RPE: RPE_1452
            NWI: Nwi_1070
            NHA: Nham_1298
            CCR: CC_1430
            GOX: GOX1134
            GBE: GbCGDNIH1_1533
            RRU: Rru_A3278
            MAG: amb0596
            MGM: Mmc1_1553
            ABA: Acid345_3812
            FNU: FN1703
            PCU: pc1588(hldD)
            LIL: LA2326(rfaD)
            LIC: LIC11616(rfaD)
            LBJ: LBJ_1298
            LBL: LBL_1523
            CHU: CHU_0958(rfaD) CHU_1387(rfaD)
            CTE: CT1258(rfaD)
            CCH: Cag_1084
            PLT: Plut_1208
            AAE: aq_344(rfaD)
STRUCTURES  PDB: 1EQ2  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.20
            ExPASy - ENZYME nomenclature database: 5.1.3.20
            ExplorEnz - The Enzyme Database: 5.1.3.20
            ERGO genome analysis and discovery system: 5.1.3.20
            BRENDA, the Enzyme Database: 5.1.3.20
            CAS: 85030-75-7
///
ENTRY       EC 5.1.3.21                 Enzyme
NAME        maltose epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     maltose 1-epimerase
REACTION    alpha-maltose = beta-maltose [RN:R07319]
ALL_REAC    R07319
SUBSTRATE   alpha-maltose [CPD:C00897]
PRODUCT     beta-maltose [CPD:C01971]
COMMENT     The enzyme catalyses the interconversion of alpha and beta anomers
            of maltose more effectively than those of disaccharides such as
            lactose and cellobiose.
REFERENCE   1  [PMID:7796915]
  AUTHORS   Shirokane Y, Suzuki M.
  TITLE     A novel enzyme, maltose 1-epimerase from Lactobacillus brevis IFO
            3345.
  JOURNAL   FEBS. Lett. 367 (1995) 177-9.
  ORGANISM  Lactobacillus brevis [GN:lbr]
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.21
            ExPASy - ENZYME nomenclature database: 5.1.3.21
            ExplorEnz - The Enzyme Database: 5.1.3.21
            ERGO genome analysis and discovery system: 5.1.3.21
            BRENDA, the Enzyme Database: 5.1.3.21
            CAS: 166799-98-0
///
ENTRY       EC 5.1.3.22                 Enzyme
NAME        L-ribulose-5-phosphate 3-epimerase;
            L-xylulose 5-phosphate 3-epimerase;
            UlaE;
            SgaU
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on carbohydrates and derivatives
SYSNAME     L-ribulose-5-phosphate 3-epimerase
REACTION    L-ribulose 5-phosphate = L-xylulose 5-phosphate [RN:R03244]
ALL_REAC    R03244
SUBSTRATE   L-ribulose 5-phosphate [CPD:C01101]
PRODUCT     L-xylulose 5-phosphate [CPD:C03291]
COMMENT     Along with EC 4.1.1.85, 3-dehydro-L-gulonate-6-phosphate
            decarboxylase, this enzyme is involved in a pathway for the
            utilization of L-ascorbate by Escherichia coli.
REFERENCE   1  [PMID:11741871]
  AUTHORS   Yew WS, Gerlt JA.
  TITLE     Utilization of L-ascorbate by Escherichia coli K-12: assignments of
            functions to products of the yjf-sga and yia-sgb operons.
  JOURNAL   J. Bacteriol. 184 (2002) 302-6.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00053  Ascorbate and aldarate metabolism
ORTHOLOGY   KO: K03079  L-ribulose-5-phosphate 3-epimerase
GENES       ECO: b4197(sgaU)
            ECJ: JW4155(ulaE)
            ECE: Z5806(sgaU)
            ECS: ECs5173
            ECC: c5287(sgaU)
            ECI: UTI89_C4797(sgaU)
            ECP: ECP_4442
            ECV: APECO1_2195(ulaE)
            ECW: EcE24377A_4758(ulaE)
            ECX: EcHS_A4441(ulaE)
            STY: STY4743(sgaU)
            STT: t4438(sgaU)
            SPT: SPA4204(sgaU)
            SEC: SC4261(sgaU)
            STM: STM4387(sgaU)
            SFL: SF4352(sgaU)
            SFX: S4622(sgaU)
            SFV: SFV_4353(sgaU)
            SSN: SSON_4379(sgaU)
            SBO: SBO_4258(sgaU)
            SPE: Spro_3938
            ASU: Asuc_0235
            VCH: VCA0241
            VVU: VV2_1085
            VVY: VVA1609
            PPR: PBPRB0269(sgbU)
            MPN: MPN492(yjfW)
            MPU: MYPU_5980(sgaU)
            MPE: MYPE7170(sgaU)
            MHY: mhp440(sgaU)
            MHJ: MHJ_0435(sgaU)
            MHP: MHP7448_0437(sgaU)
            MSY: MS53_0030(sgaU)
            TWH: TWT648(sgaU)
            TWS: TW670(sgaU)
            PAC: PPA0881
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.3.22
            ExPASy - ENZYME nomenclature database: 5.1.3.22
            ExplorEnz - The Enzyme Database: 5.1.3.22
            ERGO genome analysis and discovery system: 5.1.3.22
            BRENDA, the Enzyme Database: 5.1.3.22
///
ENTRY       EC 5.1.99.1                 Enzyme
NAME        methylmalonyl-CoA epimerase;
            methylmalonyl-CoA racemase;
            methylmalonyl coenzyme A racemase;
            DL-methylmalonyl-CoA racemase;
            2-methyl-3-oxopropanoyl-CoA 2-epimerase [incorrect]
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on other compounds
SYSNAME     methylmalonyl-CoA 2-epimerase
REACTION    (R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA [RN:R02765]
ALL_REAC    R02765
SUBSTRATE   (R)-methylmalonyl-CoA [CPD:C01213]
PRODUCT     (S)-methylmalonyl-CoA [CPD:C00683]
REFERENCE   1  [PMID:13934211]
  AUTHORS   MAZUMDER R, SASAKAWA T, KAZIRO Y, OCHOA S.
  TITLE     Metabolism of propionic acid in animal tissues. IX. Methylmalonyl
            coenzyme A racemase.
  JOURNAL   J. Biol. Chem. 237 (1962) 3065-8.
  ORGANISM  Propionibacterium shermanii
REFERENCE   2  [PMID:14482843]
  AUTHORS   OVERATH P, KELLERMAN GM, LYNEN F, FRITZ HP, KELLER HJ.
  TITLE     [On the mechanism of the rearrangement of methylmalonyl-Co A into
            succinyl-Co A. II. Experiments on the mechanism of action of
            methylmalonyl-Co A isomerase and methylmalonyl-Co A racemase.]
  JOURNAL   Biochem. Z. 335 (1962) 500-18.
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K05606  methylmalonyl-CoA epimerase
GENES       HSA: 84693(MCEE)
            MMU: 73724(Mcee)
            RNO: 293829(Mcee_predicted)
            CFA: 479018(MCEE)
            GGA: 415385(MCEE)
            REH: H16_A3551
            SAT: SYN_00683 SYN_01971
            PLA: Plav_3210
            SMD: Smed_0906
            BOV: BOV_0813(mce)
            OAN: Oant_2407
            BRA: BRADO4168
            BBT: BBta_4545
            XAU: Xaut_4617
            SIL: SPO0932
            RSQ: Rsph17025_0368
            RDE: RD1_1179
            HNE: HNE_1762
            SWI: Swit_2892
            BCE: BC1837
            MAV: MAV_1543(mce)
            MSM: MSMEG_4921(mce)
            PAC: PPA1104
STRUCTURES  PDB: 1JC4  1JC5  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.99.1
            ExPASy - ENZYME nomenclature database: 5.1.99.1
            ExplorEnz - The Enzyme Database: 5.1.99.1
            ERGO genome analysis and discovery system: 5.1.99.1
            BRENDA, the Enzyme Database: 5.1.99.1
            CAS: 9024-03-7
///
ENTRY       EC 5.1.99.2                 Enzyme
NAME        16-hydroxysteroid epimerase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on other compounds
SYSNAME     16-hydroxysteroid 16-epimerase
REACTION    16alpha-hydroxysteroid = 16beta-hydroxysteroid [RN:R03228]
ALL_REAC    R03228
SUBSTRATE   16alpha-hydroxysteroid [CPD:C01090]
PRODUCT     16beta-hydroxysteroid [CPD:C03050]
REFERENCE   1  [PMID:5657462]
  AUTHORS   Dahm K, Lindlau M, Breuer H.
  TITLE     [Steroid epimerase--a new enzyme of estrogen metabolism]
  JOURNAL   Biochim. Biophys. Acta. 159 (1968) 377-89.
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.99.2
            ExPASy - ENZYME nomenclature database: 5.1.99.2
            ExplorEnz - The Enzyme Database: 5.1.99.2
            ERGO genome analysis and discovery system: 5.1.99.2
            BRENDA, the Enzyme Database: 5.1.99.2
            CAS: 37318-40-4
///
ENTRY       EC 5.1.99.3                 Enzyme
NAME        allantoin racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on other compounds
SYSNAME     allantoin racemase
REACTION    (S)(+)-allantoin = (R)(-)-allantoin [RN:R03925]
ALL_REAC    R03925
SUBSTRATE   (S)(+)-allantoin [CPD:C02350]
PRODUCT     (R)(-)-allantoin [CPD:C02348]
REFERENCE   1  [PMID:237557]
  AUTHORS   Van der Drift L, Vogels GD, Van der Drift C.
  TITLE     Allantoin racemase: a new enzyme from Pseudomonas species.
  JOURNAL   Biochim. Biophys. Acta. 391 (1975) 240-8.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00230  Purine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.99.3
            ExPASy - ENZYME nomenclature database: 5.1.99.3
            ExplorEnz - The Enzyme Database: 5.1.99.3
            ERGO genome analysis and discovery system: 5.1.99.3
            BRENDA, the Enzyme Database: 5.1.99.3
            CAS: 56214-40-5
///
ENTRY       EC 5.1.99.4                 Enzyme
NAME        alpha-methylacyl-CoA racemase
CLASS       Isomerases;
            Racemases and epimerases;
            Acting on other compounds
SYSNAME     2-methylacyl-CoA 2-epimerase
REACTION    (2S)-2-methylacyl-CoA = (2R)-2-methylacyl-CoA [RN:R04729]
ALL_REAC    R04729
SUBSTRATE   (2S)-2-methylacyl-CoA [CPD:C05232]
PRODUCT     (2R)-2-methylacyl-CoA [CPD:C05329]
COMMENT     alpha-methyl-branched acyl-CoA derivatives with chain lengths of
            more than C10 are substrates. Also active towards some aromatic
            compounds (e.g. ibuprofen) and bile acid intermediates, such as
            trihydroxycoprostanoyl-CoA. Not active towards free acids
REFERENCE   1  [PMID:8020470]
  AUTHORS   Schmitz W, Fingerhut R, Conzelmann E.
  TITLE     Purification and properties of an alpha-methylacyl-CoA racemase from
            rat liver.
  JOURNAL   Eur. J. Biochem. 222 (1994) 313-23.
  ORGANISM  rat [GN:rno]
ORTHOLOGY   KO: K01796  
GENES       HSA: 23600(AMACR)
            MMU: 17117(Amacr)
            RNO: 25284(Amacr)
            CFA: 612603(AMACR)
            GGA: 427429(RCJMB04_7i6)
            XTR: 493271(amacr)
            SPU: 589843(LOC589843)
            DME: Dmel_CG9319
            UMA: UM05961.1
            PFO: Pfl_4235
            ACI: ACIAD1683(caiB) ACIAD1687(caiB)
            PAT: Patl_2713
            MAQ: Maqu_2037
            REU: Reut_B5306
            REH: H16_A2145
            RME: Rmet_5435
            BXE: Bxe_A3539
            BUR: Bcep18194_A5865 Bcep18194_B0153 Bcep18194_B2483
                 Bcep18194_B2645 Bcep18194_C7120 Bcep18194_C7158
                 Bcep18194_C7187 Bcep18194_C7292 Bcep18194_C7493
            BCH: Bcen2424_5504
            BPS: BPSL0064
            BPM: BURPS1710b_0288
            BTE: BTH_I0064
            RFR: Rfer_0993 Rfer_4167
            ADE: Adeh_2342
            SFU: Sfum_1527
            BME: BMEII1019 BMEII1076
            BMF: BAB2_0217
            BJA: blr0338(AMACR)
            BRA: BRADO3032 BRADO6960
            BBT: BBta_0571 BBta_5109
            RPE: RPE_0934
            CCR: CC_1841
            RRU: Rru_A2103
            DSY: DSY0939 DSY3794
            MTU: Rv1143(mcr)
            MTC: MT1176
            MBO: Mb1175(mcr)
            MBB: BCG_1205(mcr)
            MPA: MAP2638c(mcr)
            MAV: MAV_0976
            MSM: MSMEG_5184 MSMEG_5734
            RHA: RHA1_ro05557
            TFU: Tfu_0399
            FRA: Francci3_0340
            FAL: FRAAL2612 FRAAL2613(frc) FRAAL2828 FRAAL3129 FRAAL3385
                 FRAAL3468
            SEN: SACE_4225 SACE_6370
            LIL: LA3144
            HWA: HQ1940A HQ1988A
            NPH: NP4210A NP6182A
STRUCTURES  PDB: 1X74  2G04  2GCE  2GCI  2GD0  2GD2  2GD6  
DBLINKS     IUBMB Enzyme Nomenclature: 5.1.99.4
            ExPASy - ENZYME nomenclature database: 5.1.99.4
            ExplorEnz - The Enzyme Database: 5.1.99.4
            ERGO genome analysis and discovery system: 5.1.99.4
            BRENDA, the Enzyme Database: 5.1.99.4
            CAS: 156681-44-6
///
ENTRY       EC 5.1.-.-                  Enzyme
CLASS       Isomerases;
            Racemases and epimerases
REACTION    Ecgonine <=> Pseudoecgonine [RN:R06730]
SUBSTRATE   Ecgonine [CPD:C10858]
PRODUCT     Pseudoecgonine [CPD:C12449]
///
ENTRY       EC 5.2.1.1                  Enzyme
NAME        maleate isomerase
CLASS       Isomerases;
            cis-trans-Isomerases;
            cis-trans Isomerases (only sub-subclass identified to date)
SYSNAME     maleate cis-trans-isomerase
REACTION    maleate = fumarate [RN:R01087]
ALL_REAC    R01087
SUBSTRATE   maleate [CPD:C01384]
PRODUCT     fumarate [CPD:C00122]
REFERENCE   1  [PMID:13475371]
  AUTHORS   BEHRMAN EJ, STANIER RY.
  TITLE     The bacterial oxidation of nicotinic acid.
  JOURNAL   J. Biol. Chem. 228 (1957) 923-45.
  ORGANISM  Pseudomonas fluorescens
PATHWAY     PATH: map00650  Butanoate metabolism
            PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K01799  maleate isomerase
GENES       RSO: RSc1822(RS04251)
            REH: H16_A0069 H16_A0923 H16_B0811
            HAR: HEAR1463(maiA)
            RLE: pRL100067
            SEN: SACE_1839 SACE_4875
            PFU: PF1344
            APE: APE_2520.1(maiA)
            SSO: SSO2939(maiA)
DBLINKS     IUBMB Enzyme Nomenclature: 5.2.1.1
            ExPASy - ENZYME nomenclature database: 5.2.1.1
            ExplorEnz - The Enzyme Database: 5.2.1.1
            ERGO genome analysis and discovery system: 5.2.1.1
            BRENDA, the Enzyme Database: 5.2.1.1
            CAS: 9023-74-9
///
ENTRY       EC 5.2.1.2                  Enzyme
NAME        maleylacetoacetate isomerase;
            maleylacetoacetic isomerase;
            maleylacetone isomerase;
            maleylacetone cis-trans-isomerase
CLASS       Isomerases;
            cis-trans-Isomerases;
            cis-trans Isomerases (only sub-subclass identified to date)
SYSNAME     4-maleylacetoacetate cis-trans-isomerase
REACTION    4-maleylacetoacetate = 4-fumarylacetoacetate [RN:R03181]
ALL_REAC    R03181
SUBSTRATE   4-maleylacetoacetate [CPD:C01036]
PRODUCT     4-fumarylacetoacetate [CPD:C01061]
COMMENT     Also acts on maleylpyruvate.
REFERENCE   1  [PMID:13319328]
  AUTHORS   EDWARDS SW, KNOX WE.
  TITLE     Homogentisate metabolism:  the isomerization of maleylacetoacetate
            by an enzyme which requires glutathione.
  JOURNAL   J. Biol. Chem. 220 (1956) 79-91.
  ORGANISM  cow [GN:bta], rat [GN:rno]
REFERENCE   2
  AUTHORS   Lack, L.
  TITLE     Enzymic cis-trans isomerization of maleylpyruvic acid.
  JOURNAL   J. Biol. Chem. 236 (1961) 2835-2840.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:4692831]
  AUTHORS   Seltzer S.
  TITLE     Purification and properties of maleylacetone cis-trans isomerase
            from vibrio 01.
  JOURNAL   J. Biol. Chem. 248 (1973) 215-22.
  ORGANISM  Vibrio sp.
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00643  Styrene degradation
ORTHOLOGY   KO: K01800  maleylacetoacetate isomerase
GENES       HSA: 2954(GSTZ1)
            MMU: 14874(Gstz1)
            GGA: 423374(GSTZ1)
            XLA: 496168(LOC496168)
            SPU: 580863(LOC580863)
            DME: Dmel_CG9362
            CEL: D1053.1(gst-42)
            AFM: AFUA_2G04240
            DDI: DDB_0231608(mai)
            ECW: EcE24377A_2431(maiA)
            XCC: XCC0592(uptB)
            XCB: XC_3641
            XCV: XCV3731
            XAC: XAC3608(uptB)
            XOO: XOO0772(uptB)
            XOM: XOO_0702(XOO0702)
            VCH: VC1347
            VCO: VC0395_A0964(maiA)
            VVU: VV1_2765
            VVY: VV1498
            VPA: VP1352
            PPR: PBPRB1167
            PAE: PA2007(maiA)
            PAU: PA14_38550(maiA)
            PAP: PSPA7_2765(maiA2) PSPA7_3282(maiA1)
            PPU: PP_4619
            PST: PSPTO_3554(maiA)
            PSP: PSPPH_3251(maiA)
            PFL: PFL_0969(maiA)
            PFO: Pfl_0912
            PEN: PSEEN2595(mhbI) PSEEN4610(maiA)
            PCR: Pcryo_1561
            SON: SO_1671
            SDN: Sden_2591
            SFR: Sfri_1332
            SHE: Shewmr4_2603
            SHM: Shewmr7_2670
            SHN: Shewana3_2777
            ILO: IL0719
            CPS: CPS_3762(maiA)
            PHA: PSHAa2527(sspA) PSHAb0337(maiA)
            PAT: Patl_1448
            LPN: lpg2280
            LPF: lpl2206
            LPP: lpp2234
            NOC: Noc_1440
            HCH: HCH_00952(maiA)
            AHA: AHA_2660(maiA)
            CVI: CV_0972
            RSO: RSc0384(RS03352)
            REU: Reut_A0333 Reut_B5804
            REH: H16_A0362
            RME: Rmet_0280
            BMA: BMA3128(maiA)
            BMV: BMASAVP1_A0097(maiA)
            BML: BMA10299_A1492(maiA)
            BMN: BMA10247_2921(maiA)
            BXE: Bxe_A2723 Bxe_A4141
            BUR: Bcep18194_A3542 Bcep18194_A6140 Bcep18194_B1887
                 Bcep18194_B2364
            BCN: Bcen_2196 Bcen_4219
            BCH: Bcen2424_2810 Bcen2424_4147
            BAM: Bamb_2870
            BPS: BPSL0513
            BPM: BURPS1710b_0744(maiA)
            BPL: BURPS1106A_0575(maiA)
            BPD: BURPS668_0560(maiA)
            BTE: BTH_I0465(maiA)
            BPE: BP1238
            BPA: BPP1853
            BBR: BB3255
            POL: Bpro_0991 Bpro_2136
            MPT: Mpe_A1872
            EBA: ebA1379(nagL)
            BBA: Bd0291(maiA)
            ADE: Adeh_3421
            MXA: MXAN_6348(maiA)
            MLO: mlr1135
            MES: Meso_3563
            SME: SMc03206(maiA)
            RET: RHE_CH01748(maiA)
            RLE: RL1866 RL2736(maiA)
            BJA: bll0109
            BRA: BRADO0684(maiA) BRADO5768 BRADO5975
            BBT: BBta_1799 BBta_6278 BBta_6524 BBta_7500(maiA)
            RPA: RPA4671(maiA)
            RPB: RPB_0908
            RPD: RPD_1019
            NHA: Nham_0920
            SIL: SPO0679(hmgC)
            SIT: TM1040_2626
            JAN: Jann_1437
            RDE: RD1_3652(maiA)
            MMR: Mmar10_1997
            HNE: HNE_1992(maiA)
            RRU: Rru_A3193
            SYD: Syncc9605_0553
STRUCTURES  PDB: 1FW1  2CZ2  2CZ3  
DBLINKS     IUBMB Enzyme Nomenclature: 5.2.1.2
            ExPASy - ENZYME nomenclature database: 5.2.1.2
            ExplorEnz - The Enzyme Database: 5.2.1.2
            ERGO genome analysis and discovery system: 5.2.1.2
            UM-BBD (Biocatalysis/Biodegradation Database): 5.2.1.2
            BRENDA, the Enzyme Database: 5.2.1.2
            CAS: 9023-75-0
///
ENTRY       EC 5.2.1.3                  Enzyme
NAME        retinal isomerase;
            retinene isomerase;
            retinoid isomerase
CLASS       Isomerases;
            cis-trans-Isomerases;
            cis-trans Isomerases (only sub-subclass identified to date)
SYSNAME     all-trans-retinal 11-cis-trans-isomerase
REACTION    all-trans-retinal = 11-cis-retinal [RN:R02126]
ALL_REAC    R02126
SUBSTRATE   all-trans-retinal [CPD:C00376]
PRODUCT     11-cis-retinal [CPD:C02110]
COMMENT     Light shifts the reaction towards the cis-isomer.
REFERENCE   1  [PMID:13346046]
  AUTHORS   HUBBARD R.
  TITLE     Retinene isomerase.
  JOURNAL   J. Gen. Physiol. 39 (1956) 935-62.
REFERENCE   2  [PMID:4472816]
  AUTHORS   Shichi H, Somers RL.
  TITLE     Possible involvement of retinylidene phospholipid in
            photoisomerization of all-trans-retinal to 11-cis-retinal.
  JOURNAL   J. Biol. Chem. 249 (1974) 6570-7.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00830  Retinol metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 5.2.1.3
            ExPASy - ENZYME nomenclature database: 5.2.1.3
            ExplorEnz - The Enzyme Database: 5.2.1.3
            ERGO genome analysis and discovery system: 5.2.1.3
            BRENDA, the Enzyme Database: 5.2.1.3
            CAS: 9023-76-1
///
ENTRY       EC 5.2.1.4                  Enzyme
NAME        maleylpyruvate isomerase
CLASS       Isomerases;
            cis-trans-Isomerases;
            cis-trans Isomerases (only sub-subclass identified to date)
SYSNAME     3-maleylpyruvate cis-trans-isomerase
REACTION    3-maleylpyruvate = 3-fumarylpyruvate [RN:R03868]
ALL_REAC    R03868
SUBSTRATE   3-maleylpyruvate [CPD:C02167]
PRODUCT     3-fumarylpyruvate [CPD:C02514]
REFERENCE   1
  AUTHORS   Lack, L.
  TITLE     Enzymic cis-trans isomerization of maleylpyruvic acid.
  JOURNAL   J. Biol. Chem. 236 (1961) 2835-2840.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00350  Tyrosine metabolism
ORTHOLOGY   KO: K01801  maleylpyruvate isomerase
GENES       REH: H16_B0875
            BXE: Bxe_A2629 Bxe_A4524
            AZO: azo2423(nagL1) azo3676(nagL2)
            RET: RHE_CH02410(ypch00797)
            BME: BMEI1125
            RHA: RHA1_ro01865
STRUCTURES  PDB: 2NSF  2NSG  
DBLINKS     IUBMB Enzyme Nomenclature: 5.2.1.4
            ExPASy - ENZYME nomenclature database: 5.2.1.4
            ExplorEnz - The Enzyme Database: 5.2.1.4
            ERGO genome analysis and discovery system: 5.2.1.4
            BRENDA, the Enzyme Database: 5.2.1.4
            CAS: 9023-77-2
///
ENTRY       EC 5.2.1.5                  Enzyme
NAME        linoleate isomerase;
            linoleic acid isomerase
CLASS       Isomerases;
            cis-trans-Isomerases;
            cis-trans Isomerases (only sub-subclass identified to date)
SYSNAME     linoleate Delta12-cis-Delta11-trans-isomerase
REACTION    9-cis,12-cis-octadecadienoate = 9-cis,11-trans-octadecadienoate
            [RN:R03627]
ALL_REAC    R03627
SUBSTRATE   9-cis,12-cis-octadecadienoate [CPD:C01595]
PRODUCT     9-cis,11-trans-octadecadienoate [CPD:C04056]
REFERENCE   1  [PMID:5633396]
  AUTHORS   Kepler CR, Tove SB.
  TITLE     Biohydrogenation of unsaturated fatty acids. 3. Purification and
            properties of a linoleate delta-12-cis, delta-11-trans-isomerase
            from Butyrivibrio fibrisolvens.
  JOURNAL   J. Biol. Chem. 242 (1967) 5686-92.
  ORGANISM  Butyrivibrio fibrosolvens
PATHWAY     PATH: map00591  Linoleic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 5.2.1.5
            ExPASy - ENZYME nomenclature database: 5.2.1.5
            ExplorEnz - The Enzyme Database: 5.2.1.5
            ERGO genome analysis and discovery system: 5.2.1.5
            BRENDA, the Enzyme Database: 5.2.1.5
            CAS: 37318-41-5
///
ENTRY       EC 5.2.1.6                  Enzyme
NAME        furylfuramide isomerase
CLASS       Isomerases;
            cis-trans-Isomerases;
            cis-trans Isomerases (only sub-subclass identified to date)
SYSNAME     2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide cis-trans-isomerase
REACTION    (E)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide =
            (Z)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide [RN:R04538]
ALL_REAC    R04538
SUBSTRATE   (E)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide [CPD:C04621]
PRODUCT     (Z)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide [CPD:C04622]
COFACTOR    NAD+ [CPD:C00003];
            NADH [CPD:C00004]
COMMENT     Requires NADH.
REFERENCE   1  [PMID:12827]
  AUTHORS   Tomoeda M, Kitamura R.
  TITLE     A cis-trans isomerising activity of Escherichia coli. Isomerization
            from 2-(2-furyl)-3-cis-(5-nitro-2-furyl) acrylamide (furylfuramide)
            to its trans isomer.
  JOURNAL   Biochim. Biophys. Acta. 480 (1977) 315-25.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 5.2.1.6
            ExPASy - ENZYME nomenclature database: 5.2.1.6
            ExplorEnz - The Enzyme Database: 5.2.1.6
            ERGO genome analysis and discovery system: 5.2.1.6
            BRENDA, the Enzyme Database: 5.2.1.6
            CAS: 72561-07-0
///
ENTRY       EC 5.2.1.7                  Enzyme
NAME        retinol isomerase;
            all-trans-retinol isomerase
CLASS       Isomerases;
            cis-trans-Isomerases;
            cis-trans Isomerases (only sub-subclass identified to date)
SYSNAME     all-trans-retinol 11-cis-trans-isomerase
REACTION    all-trans-retinol = 11-cis-retinol [RN:R02369]
ALL_REAC    R02369
SUBSTRATE   all-trans-retinol [CPD:C00473]
PRODUCT     11-cis-retinol [CPD:C00899]
COMMENT     Converts all-trans-retinol to 11-cis-retinol in the dark, thus
            reversing the effect of EC 5.2.1.3 retinal isomerase.
REFERENCE   1  [PMID:3494246]
  AUTHORS   Bernstein PS, Law WC, Rando RR.
  TITLE     Isomerization of all-trans-retinoids to 11-cis-retinoids in vitro.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 1849-53.
  ORGANISM  frog
REFERENCE   2  [PMID:3603006]
  AUTHORS   Bridges CD, Alvarez RA.
  TITLE     The visual cycle operates via an isomerase acting on all-trans
            retinol in the pigment epithelium.
  JOURNAL   Science. 236 (1987) 1678-80.
PATHWAY     PATH: map00830  Retinol metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 5.2.1.7
            ExPASy - ENZYME nomenclature database: 5.2.1.7
            ExplorEnz - The Enzyme Database: 5.2.1.7
            ERGO genome analysis and discovery system: 5.2.1.7
            BRENDA, the Enzyme Database: 5.2.1.7
            CAS: 109740-80-9
///
ENTRY       EC 5.2.1.8                  Enzyme
NAME        peptidylprolyl isomerase;
            PPIase;
            cyclophilin [misleading, see comments];
            peptide bond isomerase;
            peptidyl-prolyl cis-trans isomerase
CLASS       Isomerases;
            cis-trans-Isomerases;
            cis-trans Isomerases (only sub-subclass identified to date)
SYSNAME     peptidylproline cis-trans-isomerase
REACTION    peptidylproline (omega=180) = peptidylproline (omega=0) [RN:R04273]
ALL_REAC    R04273
SUBSTRATE   peptidylproline (omega=180) [CPD:C03798]
PRODUCT     peptidylproline (omega=0) [CPD:C03633]
INHIBITOR   Tacrolimus [CPD:C01375]
COMMENT     The first type of this enzyme found [1] proved to be the protein
            cyclophilin, which binds the immunosuppressant cyclosporin A. Other
            distinct families of the enzyme exist, one being FK-506 binding
            proteins (FKBP) and another that includes parvulin from Escherichia
            coli. The three families are structurally unrelated and can be
            distinguished by being inhibited by cyclosporin A, FK-506 and
            5-hydroxy-1,4-naphthoquinone, respectively.
REFERENCE   1  [PMID:3882150]
  AUTHORS   Fischer G, Bang H.
  TITLE     The refolding of urea-denatured ribonuclease A is catalyzed by
            peptidyl-prolyl cis-trans isomerase.
  JOURNAL   Biochim. Biophys. Acta. 828 (1985) 39-42.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:6395866]
  AUTHORS   Fischer G, Bang H, Mech C.
  TITLE     [Determination of enzymatic catalysis for the
            cis-trans-isomerization of peptide binding in proline-containing
            peptides]
  JOURNAL   Biomed. Biochim. Acta. 43 (1984) 1101-11.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:2492638]
  AUTHORS   Fischer G, Wittmann-Liebold B, Lang K, Kiefhaber T, Schmid FX.
  TITLE     Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably
            identical proteins.
  JOURNAL   Nature. 337 (1989) 476-8.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:2644542]
  AUTHORS   Takahashi N, Hayano T, Suzuki M.
  TITLE     Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding
            protein cyclophilin.
  JOURNAL   Nature. 337 (1989) 473-5.
  ORGANISM  pig [GN:ssc]
REFERENCE   5  [PMID:9558330]
  AUTHORS   Hennig L, Christner C, Kipping M, Schelbert B, Rucknagel KP, Grabley
            S, Kullertz G, Fischer G.
  TITLE     Selective inactivation of parvulin-like peptidyl-prolyl cis/trans
            isomerases by juglone.
  JOURNAL   Biochemistry. 37 (1998) 5953-60.
REFERENCE   6
  AUTHORS   Fischer, G.
  TITLE     Peptidyl-prolyl cis/trans isomerases and their effectors.
  JOURNAL   Angew. Chem. Int. Ed. Engl. 33 (1994) 1415-1436.
REFERENCE   7  [PMID:1693856]
  AUTHORS   Harrison RK, Stein RL.
  TITLE     Substrate specificities of the peptidyl prolyl cis-trans isomerase
            activities of cyclophilin and FK-506 binding protein: evidence for
            the existence of a family of distinct enzymes.
  JOURNAL   Biochemistry. 29 (1990) 3813-6.
REFERENCE   8  [PMID:11859194]
  AUTHORS   Eisenmesser EZ, Bosco DA, Akke M, Kern D.
  TITLE     Enzyme dynamics during catalysis.
  JOURNAL   Science. 295 (2002) 1520-3.
PATHWAY     PATH: map04020  Calcium signaling pathway
ORTHOLOGY   KO: K01802  peptidylprolyl isomerase
            KO: K03767  peptidyl-prolyl cis-trans isomerase A (cyclophilin A)
            KO: K03768  peptidyl-prolyl cis-trans isomerase B (cyclophilin B)
            KO: K03769  peptidyl-prolyl cis-trans isomerase C
            KO: K03770  peptidyl-prolyl cis-trans isomerase D
            KO: K03771  peptidyl-prolyl cis-trans isomerase SurA
            KO: K03772  FKBP-type peptidyl-prolyl cis-trans isomerase FkpA
            KO: K03773  FKBP-type peptidyl-prolyl cis-trans isomerase FklB
            KO: K03774  FKBP-type peptidyl-prolyl cis-trans isomerase SlpA
            KO: K03775  FKBP-type peptidyl-prolyl cis-trans isomerase SlyD
            KO: K05864  peptidyl-prolyl isomerase D (cyclophilin D)
            KO: K07533  foldase protein PrsA
            KO: K09563  peptidyl-prolyl isomerase C (cyclophilin C)
            KO: K09564  peptidyl-prolyl isomerase E (cyclophilin E)
            KO: K09565  peptidyl-prolyl isomerase F (cyclophilin F)
            KO: K09566  peptidyl-prolyl isomerase G (cyclophilin G)
            KO: K09567  peptidyl-prolyl isomerase H (cyclophilin H)
            KO: K09568  FK506-binding protein 1
            KO: K09569  FK506-binding protein 2
            KO: K09570  FK506-binding protein 3
            KO: K09571  FK506-binding protein 4/5
            KO: K09572  FK506-binding protein 6
            KO: K09573  FK506-binding protein 7
            KO: K09574  FK506-binding protein 8
            KO: K09575  FK506-binding protein 9/10
            KO: K09576  FK506-binding protein 11
            KO: K09577  FK506-binding protein 14
            KO: K09578  peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
            KO: K09579  peptidyl-prolyl cis-trans isomerase NIMA-interacting 4
GENES       HSA: 10105(PPIF) 10450(PPIE) 10465(PPIH) 11328(FKBP9) 2280(FKBP1A)
                 2281(FKBP1B) 2286(FKBP2) 2287(FKBP3) 2288(FKBP4) 2289(FKBP5)
                 23759(PPIL2) 390956(LOC390956) 51303(FKBP11) 51645(PPIL1)
                 51661(FKBP7) 5300(PIN1) 5303(PIN4) 53938(PPIL3) 5478(PPIA)
                 5479(PPIB) 5480(PPIC) 5481(PPID) 55033(FKBP14) 60681(FKBP10)
                 8468(FKBP6) 85313(PPIL4) 9360(PPIG)
            PTR: 450545(PPIF) 451748(FKBP4) 452883(FKBP3) 456784(PPIE)
                 459718(PPIG) 459778(FKBP7) 462639(FKBP5) 462652(PPIL1)
                 462800(LOC462800) 463324(FKBP14) 463339(FKBP9) 463386(PPIA)
                 466649(LOC466649) 469303(PPIH) 472150(PPIL4) 472404(FKBP6)
                 741603(FKBP10)
            MMU: 105675(Ppif) 106369(Ypel1) 14225(Fkbp1a) 14226(Fkbp1b)
                 14227(Fkbp2) 14228(Fkbp4) 14229(Fkbp5) 14230(Fkbp10)
                 14231(Fkbp7) 19035(Ppib) 19038(Ppic) 228005(Ppig)
                 231997(Fkbp14) 23988(Pin1) 268373(Ppia) 27055(Fkbp9)
                 30795(Fkbp3) 56031(Ppie) 628161(EG628161) 66053(Ppil2)
                 66101(Ppih) 66120(Fkbp11) 67418(Ppil4) 67738(Ppid)
                 68816(Ppil1) 70225(Ppil3) 94244(Fkbp6)
            RNO: 25518(Ppia) 25639(Fkbp1a) 260321(Fkbp4) 282819(Ppif)
                 288597(Fkbp6_predicted) 291463(Ppic) 293702(Fkbp2_predicted)
                 295672(Fkbp7_predicted) 297123(Fkbp9) 298508(Ppie)
                 298696(Pin1_predicted) 299104(Fkbp3_predicted) 300211(Fkbp11)
                 301432(Ppil3) 360627(LOC360627) 361810(Fkbp5) 361967(Ppid)
                 362366(Fkbp14) 366461(RGD1564921_predicted) 58950(Fkbp1b)
                 64367(Ppib) 684441(LOC684441) 83624(Ppig)
            CFA: 403581(PPIA) 474891(PPIL1) 475276(FKBP9) 475481(PPID)
                 477573(PPIL2) 477726(FKBP4) 480306(FKBP3) 481480(PPIC)
                 481759(FKBP5) 483764(FKBP2) 484030(PPIL4) 484963(PIN1)
                 488424(FKBP7) 489810(FKBP6) 490762(LOC490762) 490975(FKBP10)
                 492022(ARMCX3) 606861(LOC606861) 606899(PPIH)
                 607090(LOC607090) 607232(PPIE) 607430(PPIL3) 607519(PPIG)
                 608951(FKBP11) 609903(LOC609903) 609977(LOC609977)
                 610502(PPIF) 611108(LOC611108) 611546(FKBP14) 612965(FKBP1B)
            BTA: 281419(PPIB) 281420(PPID) 414346(LOC414346) 506043(FKBP11)
                 508535(FKBP4) 509422(LOC509422) 513428(MGC142309)
                 515069(FKBP3) 530827(LOC530827) 534182(FKBP9) 535310(FKBP10)
                 535470(PIN1) 535494(MGC140018) 535704(LOC535704)
                 537921(MGC152367) 538998(MGC133593) 539221(LOC539221)
                 614506(LOC614506) 615718(FKBP14)
            SSC: 397637(PPIA)
            GGA: 374233(FKBP1A) 395254(FKBP1B) 395353(FKBP3) 395652(FKBP9)
                 396447(PPIB) 416775(RCJMB04_18c10) 417460(FKBP6) 418261(FKBP4)
                 419507(PPIH) 420636(FKBP14) 421186(FKBP5) 421625(PPIL4)
                 421764(PPIL6) 422134(PIN4) 423723(RCJMB04_1o7) 424075(PPIL3)
                 424129(FKBP7) 424162(PPIG) 426061(PPIE) 428725(PPID)
            XLA: 379069(MGC52785) 379180(MGC53657) 379271(MGC53046)
                 379640(MGC68882) 379952(cyp-7) 380130(fkbp9) 380197(ppib)
                 399004(MGC68829) 414546(MGC81078) 431811(MGC83096)
                 431968(MGC83716) 432298(MGC80316) 443985(MGC80429)
                 444769(MGC81908) 447040(fkbp10) 447086(MGC85245)
                 447715(MGC81732) 495270(LOC495270)
            XTR: 394470(MGC75715) 394581(ppid) 394649(fkbp6) 394809(pin4)
                 394997(ppih) 407915(ppig) 448435(TEgg140k03.1)
                 448493(MGC79515) 448687(MGC89927) 493472(pin1)
                 496501(LOC496501) 549377(LOC549377) 549537(LOC549537)
                 549817(ppib)
            DRE: 321795(fkbp4) 324381(fkbp10) 334319(ppil4) 335335(zgc:73373)
                 335519(ppial) 368498(fkbp7) 368823(fkbp11) 368863(fkbp3)
                 368924(fkbp5) 393721(pin1) 393785(fkbp1b) 394180(zgc:55766)
                 402839(si:dkey-189h5.5) 406292(ppib) 406773(ppig) 415155(ppid)
                 445077(zgc:91851) 445126(fkbp9) 447939(zgc:101826)
                 550373(ppie) 553574(zgc:110008) 553623(zgc:110463)
                 641328(zgc:123307)
            SPU: 575422(LOC575422) 575746(LOC575746) 575816(LOC575816)
                 575873(LOC575873) 576707(LOC576707) 577298(LOC577298)
                 577318(LOC577318) 577919(LOC577919) 580876(LOC580876)
                 581334(LOC581334) 585122(LOC585122) 587884(LOC587884)
                 588808(LOC588808) 592298(LOC592298) 593388(LOC593388)
                 594575(LOC594575) 762048(LOC762048) 763313(LOC763313)
            DME: Dmel_CG11001(FK506-bp2) Dmel_CG11777 Dmel_CG11858
                 Dmel_CG13892(Cypl) Dmel_CG14715 Dmel_CG17051(dod) Dmel_CG17266
                 Dmel_CG1866 Dmel_CG2852 Dmel_CG31478(mRpL9) Dmel_CG3511
                 Dmel_CG3966(ninaA) Dmel_CG4535(FKBP59) Dmel_CG4735(shu)
                 Dmel_CG4886(cyp33) Dmel_CG5808 Dmel_CG6226(FK506-bp1)
                 Dmel_CG7747 Dmel_CG7768 Dmel_CG8336 Dmel_CG9847
                 Dmel_CG9916(Cyp1)
            CEL: B0252.4(Cyclophilin) C05C8.3(fkb-3) C34D4.12(cyn-12)
                 D1009.2(cyn-8) F31C3.1(cyclophillin) F31D4.3(fkb-6)
                 F36H1.1(fkb-1) F42G9.2(cyn-6) F59E10.2(cyclophilin)
                 T01B7.4(cyn-11) T27D1.1(cyn-9) Y110A2AL.13 Y116A8C.34(cyn-13)
                 Y17G7B.9(cyn-16) Y17G9B.4(isomerase) Y48C3A.16 Y49A3A.5(cyn-1)
                 Y75B12B.2(cyn-7) Y75B12B.5(cyn-3) Y87G2A.6(cyclophilin)
                 ZK520.5(cyn-2)
            ATH: AT1G01940 AT1G20810 AT2G21130 AT2G36130 AT2G38730 AT2G43560
                 AT3G22920 AT3G25220(FKBP15-1) AT3G25230(ROF1) AT3G55920
                 AT3G56070(ROC2) AT3G62030(ROC4) AT4G32420 AT5G05420 AT5G13120
                 AT5G45680 AT5G48570 AT5G48580(FKBP15-2) AT5G58710(ROC7)
                 AT5G64350(FKBP12) AT5G67530
            OSA: 4324328 4327912 4328090 4328121 4329388 4330800 4331972
                 4334542 4334960 4335968 4337307 4337539 4340003 4340493
                 4341766 4341804 4342021 4342022 4346090 4346316 4347035
                 4347707 4347920
            CME: CMD070C CMH076C CMH207C CMH263C CMO300C CMR402C
            SCE: YCR069W(CPR4) YDR155C(CPR1) YDR304C(CPR5) YDR519W(FPR2)
                 YHR057C(CPR2) YJR017C(ESS1) YJR032W(CPR7) YLR216C(CPR6)
                 YLR449W(FPR4) YML074C(FPR3) YML078W(CPR3) YNL135C(FPR1)
                 YNR028W(CPR8) YPL152W(RRD2)
            AGO: AGOS_AAL056C AGOS_AAR045C AGOS_ACL120W AGOS_ACR139C
                 AGOS_ADR087C AGOS_AEL062C AGOS_AER150W AGOS_AER156C
                 AGOS_AFR064C AGOS_AGL177C
            KLA: KLLA0F11187g
            DHA: DEHA0C13541g
            PIC: PICST_23499 PICST_32751(ESS1.2) PICST_54718(FPR1) PICST_55226
                 PICST_55838 PICST_75268(CPR6) PICST_78835 PICST_79040(ESS1.1)
                 PICST_87511
            CAL: CaO19.14195
            CGR: CAGL0B04037g CAGL0E01177g CAGL0H01529g CAGL0H01705g
                 CAGL0H04301g CAGL0J03520g CAGL0J08954g CAGL0K09724g
                 CAGL0L11484g CAGL0M00638g CAGL0M02255g CAGL0M08030g
            SPO: SPAC1782.05 SPAC1B3.03c(wis2) SPAC21E11.05c SPAC27F1.06c
                 SPAC57A10.03(cyp1) SPBC1347.02(fkbp39) SPBC16H5.05c
                 SPBC1709.04c SPBC28F2.03(ppi1) SPBC839.17c SPBP8B7.25
                 SPCC16C4.03
            ANI: AN0679.2 AN3598.2 AN4069.2 AN4467.2 AN4583.2 AN6145.2
                 AN6894.2 AN8061.2 AN8343.2 AN8680.2 AN9095.2
            AFM: AFUA_1G01750 AFUA_1G05450 AFUA_1G13420 AFUA_2G02050
                 AFUA_2G03720 AFUA_2G03870 AFUA_2G07650 AFUA_2G08550
                 AFUA_2G12990 AFUA_3G07430 AFUA_4G04020 AFUA_4G07650
                 AFUA_5G01890 AFUA_5G13350 AFUA_6G02140 AFUA_6G08580
                 AFUA_6G10480 AFUA_6G12170 AFUA_7G02170 AFUA_8G03890
            AOR: AO090001000519 AO090003001047 AO090003001330 AO090005001515
                 AO090011000475 AO090011000848 AO090012000537 AO090023000811
                 AO090038000594 AO090103000002 AO090103000136 AO090120000099
                 AO090120000480 AO090120000486
            ANG: An07g08300(cypA)
            CNE: CNB01230 CNB01290 CNB01800 CNC01490 CNC03250 CND02730
                 CNE00680 CNE00760 CNE02370 CNF00430 CNG01060 CNH01590 CNJ00200
                 CNJ02490 CNK00020
            UMA: UM01018.1 UM02103.1 UM02185.1 UM03726.1 UM03941.1 UM04310.1
                 UM04455.1 UM06003.1 UM06259.1
            ECU: ECU06_0330 ECU08_0470
            DDI: DDBDRAFT_0167834 DDBDRAFT_0184037 DDBDRAFT_0185614
                 DDBDRAFT_0186469 DDBDRAFT_0203130 DDBDRAFT_0205305
                 DDBDRAFT_0205799 DDBDRAFT_0216615 DDB_0191208(cypE)
                 DDB_0191497(cypB) DDB_0216173(ppiA) DDB_0232264(impA)
            PFA: PF08_0121 PF11_0164 PF11_0170 PF13_0122 PF14_0223 PFCPR3
                 PFE0505w PFE1430ca PFL0120c PFL0735w PFL2275c
            CPV: cgd1_870 cgd8_1560
            CHO: Chro.10107 Chro.20180 Chro.20441 Chro.50038 Chro.80184
                 Chro.80276
            TAN: TA04070 TA05805 TA13185 TA13975 TA14055 TA15740 TA16315
                 TA16335 TA18945 TA19340 TA19600 TA21175
            TPV: TP01_0114 TP01_0244 TP01_0815 TP01_1099 TP01_1103 TP02_0580
                 TP03_0222 TP03_0350
            TET: TTHERM_00051740 TTHERM_00075590 TTHERM_00118710
                 TTHERM_00227040 TTHERM_00227050 TTHERM_00227060
                 TTHERM_00243800 TTHERM_00532620 TTHERM_00538480
                 TTHERM_00757550 TTHERM_00772040 TTHERM_00865250
                 TTHERM_00865350 TTHERM_00877050 TTHERM_00890120
                 TTHERM_00997720
            TBR: Tb09.160.2070 Tb09.211.1350 Tb09.211.2850 Tb09.211.4880
                 Tb10.389.0240 Tb10.61.0180 Tb10.61.0760 Tb10.70.2600
                 Tb11.01.1215 Tb11.03.0250 Tb927.2.1560 Tb927.2.1680
                 Tb927.3.3100 Tb927.5.1370 Tb927.6.1320 Tb927.6.1340
                 Tb927.6.1360 Tb927.6.1380 Tb927.6.1400 Tb927.7.280
                 Tb927.7.3420 Tb927.7.3430 Tb927.7.4770 Tb927.8.2000
                 Tb927.8.2090 Tb927.8.5230 Tb927.8.690 Tb927.8.6910
            TCR: 503581.20 503687.40 504797.100 505807.10 506581.14 506697.50
                 506885.400 506925.300 507009.100 507521.70 508153.490
                 508169.69 508323.84 508567.70 508577.140 508897.110 509033.30
                 509215.40 509499.10 509611.20 510259.50 510667.60 510947.50
                 511217.120 511353.10 511577.40 511825.63
            LMA: LmjF01.0220 LmjF06.0120 LmjF07.1030 LmjF10.0890 LmjF16.1200
                 LmjF19.1530 LmjF22.1430 LmjF23.0050 LmjF23.0125 LmjF25.0910
                 LmjF31.0050 LmjF33.1630 LmjF35.3610 LmjF35.4770 LmjF36.0230
            EHI: 11.t00051 3.t00108 3.t00121 43.t00038 49.t00033 490.t00003
                 54.t00038 75.t00037 84.t00010 84.t00012
            ECO: b0028(fkpB) b0053(surA) b0441(ppiD) b0525(ppiB) b3347(fkpA)
                 b3349(slyD) b3363(ppiA) b3775(ppiC) b4207(fklB)
            ECJ: JW0026(fkpB) JW0052(surA) JW0431(ppiD) JW0514(ppiB)
                 JW3309(fkpA) JW3311(slyD) JW3326(ppiA) JW3748(ppiC)
                 JW5746(fklB)
            ECE: Z0033(slpA) Z0062(surA) Z0548(ybaU) Z0680(ppiB) Z4705(fkpA)
                 Z4707(slyD) Z4724(ppiA) Z5286(ppiC) Z5818(fklB)
            ECS: ECs0031 ECs0058 ECs0495 ECs0587 ECs4198 ECs4200 ECs4214
                 ECs4709 ECs5185
            ECC: c0032(slpA) c0066(surA) c0557(ybaU) c0641(ppiB) c4121(fkpA)
                 c4123(slyD) c4138(ppiA) c4697(ppiC) c5306(fklB)
            ECI: UTI89_C0030(slpA) UTI89_C0060(surA) UTI89_C0463(tig)
                 UTI89_C0469(ybaU) UTI89_C0554(ppiB) UTI89_C3849(fkpA)
                 UTI89_C3851(slyD) UTI89_C3866(ppiA) UTI89_C4331(ppiC)
                 UTI89_C4816(fklB)
            ECP: ECP_0026 ECP_0502 ECP_0586 ECP_3437 ECP_3438 ECP_3454
                 ECP_3968 ECP_4461
            ECV: APECO1_1570(ppiD) APECO1_1929(surA) APECO1_1955(slpA)
                 APECO1_2179(fklB) APECO1_2696(ppiC) APECO1_3093(ppiA)
                 APECO1_3105(slyD) APECO1_3106(fkpA)
            ECW: EcE24377A_0028(fkpB) EcE24377A_0057(surA) EcE24377A_0472(tig)
                 EcE24377A_0477(ppiD) EcE24377A_0564(ppiB) EcE24377A_3816(fkpA)
                 EcE24377A_3818(slyD) EcE24377A_3832(ppiA) EcE24377A_4286(ppiC)
                 EcE24377A_4775(fklB)
            ECX: EcHS_A0030(fkpB) EcHS_A0059(surA) EcHS_A0513(tig) EcHS_A0518
                 EcHS_A0600 EcHS_A3543(fkpA) EcHS_A3545(slyD) EcHS_A3559
                 EcHS_A3992 EcHS_A4457(fklB)
            STY: STY0057(fkpB) STY0107(surA) STY0494(ppiD) STY0584(ppiB)
                 STY3647(ppiC) STY4324(ppiA) STY4343(slyD) STY4345(fkpA)
                 STY4753(fklB)
            STT: t0050(fkpB) t0095(surA) t2325(ppiB) t2408(ppiD) t3388(ppiC)
                 t4033(ppiA) t4050(slyD) t4052(fkpA) t4448(fklB)
            SPT: SPA0049(fkpB) SPA0093(surA) SPA2187(ppiB) SPA2270(ppiD)
                 SPA3319(fkpA) SPA3321(slyD) SPA3338(ppiA) SPA3749(ppiC)
                 SPA4214(fklB)
            SEC: SC0042(slpA) SC0087(surA) SC0494(cypD) SC0575(ppiB)
                 SC3387(fkpA) SC3389(slyD) SC3405(ppiA) SC3815(ppiC)
                 SC4271(fklB)
            STM: STM0048(slpA) STM0092(surA) STM0452(cypD) STM0536(ppiB)
                 STM3453(fkpA) STM3455(slyD) STM3472(ppiA) STM3910(ppiC)
                 STM4397(fklB)
            YPE: YPO0167(ppiA) YPO0193(slyD) YPO0195(fkpA) YPO0476a(fkpB)
                 YPO0494(surA) YPO3074(ppiB) YPO3153(ppiD) YPO3532(fklB)
                 YPO3873(ppiC)
            YPK: y0355(ppiC) y0651(fklB) y1031 y1106(ppiB) y3681(surA)
                 y3698(slpA) y3951(ppiA) y3975(slyD) y3977(fkpA)
            YPM: YP_0169(ppiA) YP_0191(slyD) YP_0194(fkpA) YP_0551(fklB)
                 YP_0778(ppiD) YP_0851(ppiB) YP_3172(ppiC) YP_3685(surA)
                 YP_3703(slpA2)
            YPA: YPA_0082 YPA_0145 YPA_2569 YPA_2648 YPA_3277 YPA_3279
                 YPA_3302 YPA_4070 YPA_4088
            YPN: YPN_0090 YPN_0349 YPN_0368 YPN_0937 YPN_1016 YPN_3276
                 YPN_3872 YPN_3874 YPN_3897
            YPP: YPDSF_0095 YPDSF_0120 YPDSF_2712 YPDSF_3140 YPDSF_3155
                 YPDSF_3490
            YPS: YPTB0162(ppiC) YPTB0444(fklB) YPTB0619(fkpB) YPTB0635(surA)
                 YPTB0963(ppiD) YPTB1034(ppiB) YPTB3710(fkpA) YPTB3712(slyD)
                 YPTB3734(ppiA)
            YPI: YpsIP31758_0173(ppiC) YpsIP31758_3015(ppiB) YpsIP31758_3088
                 YpsIP31758_3093(tig) YpsIP31758_3442(surA) YpsIP31758_3926
                 YpsIP31758_3928(slyD) YpsIP31758_3950(ppiA)
            YEN: YE0162(ppiC) YE0618(b0028) YE0632(b0053)
            SFL: SF0024(slpA) SF0025(slpA) SF0050(surA) SF0386(ybaU)
                 SF0456(ppiB) SF3365(fkpA) SF3367(slyD) SF3382(ppiA)
                 SF3850(ppiC) SF4279(fklB)
            SFX: S0027(slpA) S0052(surA) S0392(ybaU) S0464(ppiB) S3909(ppiC)
                 S4381(ppiA) S4395(slyD) S4397(fkpA)
            SFV: SFV_0022(slpA) SFV_0047(surA) SFV_0415(ybaU) SFV_0483(ppiB)
                 SFV_3352(fkpA) SFV_3354(slyD) SFV_3369(ppiA) SFV_3727(ppiC)
                 SFV_4280(fklB)
            SSN: SSON_0033(slpA) SSON_0061(surA) SSON_0424(ybaU)
                 SSON_0493(ppiB) SSON_3477(fkpA) SSON_3479(slyD)
                 SSON_3494(ppiA) SSON_3946(ppiC)
            SBO: SBO_0027(slpA) SBO_0042(surA) SBO_0335(ybaU) SBO_0418(ppiB)
                 SBO_3327(fkpA) SBO_3329(slyD) SBO_3345(ppiA) SBO_3786(ppiC)
            SDY: SDY_0050(slpA) SDY_0078(surA) SDY_0277(ppiB) SDY_0291(ybaU)
                 SDY_3508(fkpA) SDY_3510(slyD) SDY_3525(ppiA) SDY_3973(ppiC)
                 SDY_4377(fklB)
            ECA: ECA1152(ppiD) ECA3154(ppiB) ECA3607(fklB) ECA3857(surA)
                 ECA3874(fkpB) ECA4049(fkpA) ECA4054(slyD) ECA4071(ppiA)
                 ECA4216(ppiC)
            PLU: plu0391(ppiA) plu0422(slyD) plu0424(fkpA) plu0593(fkpB)
                 plu0611(surA) plu3805(ppiB) plu3865(ppiD) plu4561(fklB)
            BUC: BU140(surA) BU478(ppiD) BU533(fkpA)
            BAS: BUsg133(surA) BUsg462(ppiD) BUsg514(fkpA)
            BAB: bbp422(ppiD) bbp476(fkpA)
            WBR: WGLp018(surA) WGLp152(ppiD)
            SGL: SG0349 SG0416 SG0426 SG0675 SG0704 SG2291 SG2293 SG2303
            ENT: Ent638_0979 Ent638_3790 Ent638_4008
            KPN: KPN_00403(ppiD) KPN_04274(ppiC) KPN_04600(fklB)
            BFL: Bfl128(surA)
            BPN: BPEN_132(surA)
            HIN: HI0079(ppiB) HI0458(surA) HI0574(fkpA) HI0699(slyD) HI1004
            HIT: NTHI0092(ppiB) NTHI0588(surA) NTHI0707(fkbY) NTHI0822(slyD)
                 NTHI1179(ppiD)
            HDU: HD0202(slyD) HD1092(ppiB) HD1180(surA) HD1737(ppiD)
                 HD1900(fkpA)
            HSO: HS_0241(ppiB) HS_1087(ppiD) HS_1301(fklB) HS_1560(surA)
                 HS_1631(slyD) HS_1637(slyD)
            PMU: PM0943 PM0944(ppiB) PM1208(surA) PM1349(slyD) PM1567(fkpA)
                 PM1898 PM1979
            MSU: MS0157(fkpA) MS0623(ppiB) MS0624(ppiB) MS0629(surA)
                 MS1843(surA) MS1863(fkpA) MS2199(slpA)
            APL: APL_0400(surA) APL_0914(ppiB) APL_1003(ppiD) APL_1456(slyD)
                 APL_1640(fkpA) APL_1705
            XFA: XF0644 XF0652 XF0838 XF1191 XF1212 XF1605
            XFT: PD0478(ppiD) PD0493(ppiB) PD1168 PD1519(slyD) PD1525
                 PD1835(surA)
            XCC: XCC0793(surA) XCC0927(ppiB) XCC0982(ppiD) XCC1310(slyD)
                 XCC1502(fkpA) XCC1535 XCC2088(fkpA) XCC2582(slyD) XCC2625
            XCB: XC_1492 XC_1536 XC_2093 XC_2699 XC_2734 XC_2929 XC_3261
                 XC_3308 XC_3438
            XCV: XCV0902(surA) XCV1033 XCV1085(ppiD) XCV1412 XCV1413
                 XCV1593(fkpA) XCV1626 XCV2419(fkpA) XCV2906(slyD) XCV2946
            XAC: XAC0865(surA) XAC1005(ppiB) XAC1085(ppiD) XAC1358(slyD)
                 XAC1550(fkpA) XAC1585 XAC2107(fkpA) XAC2754(slyD) XAC2789
            XOO: XOO0972(ppiB) XOO1037(ppiD) XOO1893(slyD) XOO2065(fkpA)
                 XOO2450 XOO2451 XOO3080(fkpA) XOO3290(slyD) XOO3340
                 XOO3746(surA)
            XOM: XOO_0887(XOO0887) XOO_0936(XOO0936) XOO_1790(XOO1790)
                 XOO_1945(XOO1945) XOO_2322(XOO2322) XOO_2933(XOO2933)
                 XOO_3113(XOO3113) XOO_3152(XOO3152) XOO_3536(XOO3536)
            VCH: VC0354 VC0445(surA) VC0684 VC1849 VC1918 VC2299 VC2568 VC2604
                 VCA0661 VCA0953
            VCO: VC0395_0286(ppiC) VC0395_A0216(fkpB) VC0395_A1440(ppiB)
                 VC0395_A1508(ppiD) VC0395_A1513(tig) VC0395_A1888(ppiA)
                 VC0395_A2145(fklB) VC0395_A2182(slyD) VC0395_A2766(fkpA)
                 VC0395_A2863(surA)
            VVU: VV1_0018 VV1_0505 VV1_0661 VV1_0733 VV1_1327 VV1_1331
                 VV1_1817 VV1_2909 VV2_0526 VV2_1620
            VVY: VV0402 VV0480 VV0689 VV1108 VV1361 VV2595 VV3037 VV3041
                 VVA0430 VVA1075
            VPA: VP0285 VP0338(surA) VP0536 VP0921 VP1149 VP2355 VP2778 VP2783
                 VPA0023 VPA0432 VPA0545
            VFI: VF0223 VF0226 VF0288 VF0314 VF0469 VF0721 VF0795 VF0800
                 VF1098 VF1601 VFA0456 VFA0697
            PPR: PBPRA0305 PBPRA0308 PBPRA0404(surA) PBPRA0593(fkpB) PBPRA0817
                 PBPRA1097 PBPRA1266 PBPRA2395 PBPRA2633 PBPRA3317(fklB)
                 PBPRB0852
            PAE: PA0594(surA) PA0699 PA0837(slyD) PA1793(ppiB) PA1805(ppiD)
                 PA1996(ppiC1) PA3227(ppiA) PA3262 PA3717 PA3871 PA4176(ppiC2)
                 PA4558 PA4572(fklB) PA5254
            PAU: PA14_07760(surA) PA14_09890(ppiC2) PA14_13840
                 PA14_16320(fkbP-1) PA14_21820 PA14_22450(ppiA)
                 PA14_38700(ppiC1) PA14_41190(ppiD) PA14_41390(ppiB)
                 PA14_53430(slyD) PA14_55280 PA14_60350 PA14_60500(fklB)
                 PA14_69380(fkl)
            PAP: PSPA7_3497(tig)
            PPU: PP_0192(fkl) PP_0403(surA) PP_0605(fkpB) PP_0684(fklB-1)
                 PP_0776(slyD) PP_1714(fklB-2) PP_2304 PP_2903(ppiB)
                 PP_3070(ppiC-1) PP_3079(ppiC-2) PP_4313 PP_4541(ppiA)
            PST: PSPTO_0135 PSPTO_0553(surA) PSPTO_0808 PSPTO_1171 PSPTO_2529
                 PSPTO_3028(ppiC-1) PSPTO_3034(ppiC-2) PSPTO_3722
                 PSPTO_3744(ppiB) PSPTO_3890 PSPTO_4090(ppiA) PSPTO_4581
            PSB: Psyr_0055 Psyr_0712 Psyr_1009 Psyr_1594 Psyr_1733 Psyr_1751
                 Psyr_2340 Psyr_2901 Psyr_2907 Psyr_3826 Psyr_4255 Psyr_4625
            PSP: PSPPH_0060 PSPPH_0635(surA) PSPPH_0723 PSPPH_1058
                 PSPPH_1433(ppiA) PSPPH_1582 PSPPH_1677(ppiB) PSPPH_1697(tig)
                 PSPPH_1702 PSPPH_2318(ppiC1) PSPPH_2324(ppiC2) PSPPH_2826
                 PSPPH_4282
            PFL: PFL_0940 PFL_1542 PFL_2505 PFL_3569(ppiC) PFL_3579 PFL_3914
                 PFL_3983 PFL_3988(tig) PFL_4399 PFL_5319 PFL_5333 PFL_5647
                 PFL_5996
            PFO: Pfl_0882 Pfl_1428 Pfl_1671 Pfl_1980 Pfl_3072 Pfl_3084
                 Pfl_3507 Pfl_3640 Pfl_3693 Pfl_4850 Pfl_4864 Pfl_5133 Pfl_5481
            PEN: PSEEN0160 PSEEN0430 PSEEN0821(fklB) PSEEN0918 PSEEN1426
                 PSEEN1656 PSEEN1872 PSEEN2085(ppiB) PSEEN2827 PSEEN2850
                 PSEEN3151(ppiC-2) PSEEN3160(ppiC-1) PSEEN3963(ppiA) PSEEN4690
            PMY: Pmen_3171 Pmen_4011
            PAR: Psyc_0283(slyD) Psyc_0358 Psyc_0609 Psyc_0693(ppiB) Psyc_0857
                 Psyc_1473 Psyc_1520 Psyc_2090
            PCR: Pcryo_0310 Pcryo_0399 Pcryo_0664 Pcryo_1652 Pcryo_1699
                 Pcryo_1818 Pcryo_2406
            PRW: PsycPRwf_0813
            ACI: ACIAD0020(fkpB) ACIAD0065(fklB) ACIAD0066(fkpA)
                 ACIAD0706(ppiC) ACIAD1028(fbp) ACIAD1183(slyD) ACIAD1409(ppiD)
                 ACIAD1921(ppiB) ACIAD2372(surA) ACIAD3647(ppiA)
            ACB: A1S_0018 A1S_2481 A1S_2832
            SON: SO_0453(fkbP-1) SO_0481 SO_0635(ppiC-1) SO_1065(fkpA)
                 SO_1139(fklB) SO_1390 SO_1492 SO_1790(ppiB-1) SO_1798(ppiD)
                 SO_1832(ppiC-2) SO_1995 SO_2572(ppiB-2) SO_3417(slyD)
                 SO_3530(fkbP-2) SO_3637(surA) SO_3812(ppiA)
            SDN: Sden_0773 Sden_0889 Sden_0993 Sden_2140 Sden_2207 Sden_2417
                 Sden_2491 Sden_2499 Sden_2721 Sden_2741 Sden_2886 Sden_2909
                 Sden_3302 Sden_3308
            SFR: Sfri_0245 Sfri_0973 Sfri_2312 Sfri_2592 Sfri_2600 Sfri_2619
                 Sfri_2888 Sfri_2907 Sfri_3045 Sfri_3077 Sfri_3112 Sfri_3238
                 Sfri_3604 Sfri_3636
            SAZ: Sama_0821 Sama_0904 Sama_0926 Sama_1228 Sama_1262 Sama_1666
                 Sama_2817
            SBL: Sbal_0429 Sbal_0979 Sbal_1226 Sbal_1608 Sbal_1648
            SLO: Shew_0881 Shew_1078 Shew_1101 Shew_2470 Shew_2504 Shew_2512
            SPC: Sputcn32_0991 Sputcn32_1525
            SHE: Shewmr4_0457 Shewmr4_0490 Shewmr4_0625 Shewmr4_0907
                 Shewmr4_0963 Shewmr4_1137 Shewmr4_2268 Shewmr4_2456
                 Shewmr4_2491 Shewmr4_2499 Shewmr4_2804 Shewmr4_2955
                 Shewmr4_3034 Shewmr4_3153
            SHM: Shewmr7_0814 Shewmr7_0940 Shewmr7_1001 Shewmr7_1208
                 Shewmr7_2246 Shewmr7_2340 Shewmr7_2526 Shewmr7_2559
                 Shewmr7_2567 Shewmr7_2887 Shewmr7_3037 Shewmr7_3113
                 Shewmr7_3405 Shewmr7_3540 Shewmr7_3572
            SHN: Shewana3_0453 Shewana3_0491 Shewana3_0624 Shewana3_0785
                 Shewana3_0903 Shewana3_0965 Shewana3_1138 Shewana3_2377
                 Shewana3_2458 Shewana3_2618 Shewana3_2657 Shewana3_2665
                 Shewana3_2936 Shewana3_2983 Shewana3_3134 Shewana3_3207
            SHW: Sputw3181_0552 Sputw3181_1276 Sputw3181_2575 Sputw3181_2607
                 Sputw3181_3104 Sputw3181_3176
            ILO: IL0821(slyD) IL1001 IL1032(ppiB) IL1126(slpA) IL1866(ppiA)
                 IL2230(surA) IL2309(fkpA) IL2411(ppiC)
            CPS: CPS_0437(fkpA) CPS_0643(ppiA1) CPS_0709(ppiA2)
                 CPS_0749(ppiC1) CPS_1184(fkbP) CPS_1329 CPS_2846(slyD1)
                 CPS_3462(fklB) CPS_3482(ppiC2) CPS_3636(ppiC3) CPS_3780(ppiD)
                 CPS_3786(tig) CPS_3793(ppiB) CPS_3848 CPS_4133(slyD2)
                 CPS_4524(surA) CPS_4968
            PHA: PSHAa0292(slyDB) PSHAa0721(slyDA) PSHAa0920(fkpB) PSHAa1034
                 PSHAa1414(fklB) PSHAa1981 PSHAa2058(ppiD) PSHAa2066(ppiB)
                 PSHAa2247 PSHAa2488(ppiC) PSHAa2633(surA) PSHAa2901(fkpA)
                 PSHAb0308(ppiCB)
            PAT: Patl_0108 Patl_0502 Patl_0607 Patl_1552 Patl_1568 Patl_1684
                 Patl_1887 Patl_3132 Patl_3161 Patl_3176 Patl_3419
            SDE: Sde_0739 Sde_1555 Sde_1612 Sde_1714 Sde_1901 Sde_2564
                 Sde_2637
            PIN: Ping_1917 Ping_2185 Ping_3199 Ping_3269
            MAQ: Maqu_0470 Maqu_0864 Maqu_1836 Maqu_2883 Maqu_2962 Maqu_3509
            CBU: CBU_0630(mip) CBU_1451 CBU_1980
            CBD: COXBU7E912_0642(mip) COXBU7E912_0751(tig)
            LPN: lpg0298(surA) lpg0791(mip) lpg1855(ppiD) lpg1962
                 lpg2726(ppiB)
            LPF: lpl0351(surA) lpl0829(mip) lpl1821 lpl1936 lpl2652(ppiB)
            LPP: lpp0376(surA) lpp0855(mip) lpp1825 lpp1946 lpp2783(ppiB)
            MCA: MCA0081(slyD) MCA0516(ppiB) MCA0523 MCA0528(tig)
                 MCA0533(ppiD) MCA0602(surA)
            FTU: FTT0468(surA) FTT0623(tig) FTT0628 FTT0832(fkpB) FTT1043
                 FTT1472c(ppiC)
            FTF: FTF0468(surA) FTF0623(tig) FTF0628 FTF0832(fkpB) FTF1043
                 FTF1472c(ppiC)
            FTW: FTW_0626(ppiC) FTW_0952 FTW_1106(tig) FTW_1354 FTW_1602
            FTL: FTL_0326 FTL_0896 FTL_1042 FTL_1393 FTL_1596
            FTH: FTH_0324 FTH_0876 FTH_0881 FTH_1021 FTH_1355 FTH_1542(surA)
            FTA: FTA_0942(tig)
            FTN: FTN_0347(fkpB) FTN_0559 FTN_0689(ppiC) FTN_0921
            TCX: Tcr_0762 Tcr_0920 Tcr_0921 Tcr_0931 Tcr_1026 Tcr_1096
                 Tcr_1326 Tcr_1376 Tcr_1598 Tcr_1655 Tcr_1716
            NOC: Noc_0767 Noc_1086 Noc_1219 Noc_1723 Noc_1771 Noc_2251
            AEH: Mlg_0200 Mlg_0922 Mlg_0999 Mlg_2284 Mlg_2415
            HHA: Hhal_0168 Hhal_0599 Hhal_1021
            HCH: HCH_00278(fkpA) HCH_01421(slpA) HCH_02152(ppiB)
                 HCH_02157(tig) HCH_02164 HCH_04007 HCH_04404 HCH_04725
                 HCH_05931 HCH_06105 HCH_06609
            CSA: Csal_0483 Csal_0918 Csal_1297 Csal_1334 Csal_2042 Csal_2053
                 Csal_3141
            ABO: ABO_0098 ABO_0258(fklB-1) ABO_0461(fkpB) ABO_0542
                 ABO_1205(ppiA) ABO_1206(ppiB) ABO_1214(ppiD) ABO_2046(surA)
                 ABO_2363(slyD)
            AHA: AHA_0684(fkpB) AHA_0944(surA) AHA_1000(slyD) AHA_1003(fkpA)
                 AHA_1132 AHA_1261(fklB) AHA_1551 AHA_2010(tig) AHA_2015(ppiD)
                 AHA_2757(ppiB) AHA_3007
            DNO: DNO_0012 DNO_0209 DNO_0210 DNO_0230(tig) DNO_0921
            BCI: BCI_0266(tig) BCI_0565(surA)
            RMA: Rmag_0310 Rmag_0656
            VOK: COSY_0020(fkpA) COSY_0094 COSY_0601 COSY_0826(ppiB) COSY_0925
            NME: NMB0027 NMB0281 NMB0791 NMB1238 NMB1262 NMB1522 NMB1567
            NMA: NMA0273(fbp) NMA1002(ppiB) NMA1407 NMA1469(ppiA) NMA1722
                 NMA1756 NMA2206
            NMC: NMC0004(fbp) NMC0744(ppiB) NMC1138 NMC1195(ppiA) NMC1487
            NGO: NGO0376 NGO0544 NGO0766 NGO0981 NGO1225 NGO1714
            CVI: CV_0705 CV_2362(fkpA) CV_2553 CV_2829 CV_2932 CV_2933 CV_2934
                 CV_3184 CV_3185 CV_3582(slyD) CV_3791 CV_4230(surA)
            RSO: RSc0516(surA) RSc0784(fkpA) RSc1149(slyD) RSc1164(ppiB)
                 RSc1165(ppiA) RSc1715(ppiD) RSc2443(fkpB)
            REU: Reut_A0498 Reut_A0827 Reut_A1109 Reut_A1119 Reut_A1120
                 Reut_A1383 Reut_A1392 Reut_A2731 Reut_B4907 Reut_B5006
            REH: H16_A0512 H16_A1208(slpA) H16_A1218(ppiB) H16_A1219(ppiA)
                 H16_A1482(tig) H16_A1499 H16_A1514 H16_A2685 H16_A2790
                 H16_A3032 H16_B2178 H16_B2269(ppiC2)
            RME: Rmet_0437 Rmet_0812 Rmet_1073 Rmet_1082 Rmet_1083 Rmet_1868
                 Rmet_1882 Rmet_2869 Rmet_5623
            BMA: BMA0209 BMA1444 BMA1453 BMA1466(tig) BMA1658(ppiA)
                 BMA1659(ppiB) BMA2229(fkpB)
            BMV: BMASAVP1_A1945 BMASAVP1_A1958(tig) BMASAVP1_A2161(ppiA)
                 BMASAVP1_A2162(ppiB) BMASAVP1_A2645(fkpB) BMASAVP1_A2736
            BML: BMA10299_A1019(fkpB) BMA10299_A2342 BMA10299_A3153(ppiB)
                 BMA10299_A3154(ppiA) BMA10299_A3347(tig) BMA10299_A3359
            BMN: BMA10247_1220 BMA10247_1233(tig) BMA10247_1434(ppiA)
                 BMA10247_1435(ppiB) BMA10247_2098(fkpB) BMA10247_2422
            BXE: Bxe_A0819 Bxe_A1615 Bxe_A1623 Bxe_A1624 Bxe_A2280 Bxe_A2291
                 Bxe_A4023 Bxe_B0780 Bxe_B2871
            BVI: Bcep1808_1982 Bcep1808_2811 Bcep1808_4215
            BUR: Bcep18194_A5213 Bcep18194_A5221 Bcep18194_A5386
                 Bcep18194_A5387 Bcep18194_A5396 Bcep18194_A5832
                 Bcep18194_A6037 Bcep18194_B1094 Bcep18194_B2261
            BCN: Bcen_1889 Bcen_2098 Bcen_4527 Bcen_5996 Bcen_5997 Bcen_6159
                 Bcen_6167
            BCH: Bcen2424_1912 Bcen2424_1920 Bcen2424_2080 Bcen2424_2081
                 Bcen2424_2090 Bcen2424_2500 Bcen2424_2710 Bcen2424_3836
            BAM: Bamb_1900 Bamb_1908 Bamb_2115 Bamb_2116 Bamb_2126 Bamb_2547
                 Bamb_2762 Bamb_5559
            BPS: BPSL0659 BPSL0918 BPSL1410 BPSL1418 BPSL2245(ppiA)
                 BPSL2246(ppiB) BPSL2254 BPSS1155 BPSS1823(fbp)
            BPM: BURPS1710b_0872(surA) BURPS1710b_1140(fkpB) BURPS1710b_2460
                 BURPS1710b_2470 BURPS1710b_2482(tig) BURPS1710b_2683(ppiA)
                 BURPS1710b_2684 BURPS1710b_2693(slyD) BURPS1710b_A0118
                 BURPS1710b_A0410 BURPS1710b_A0907
            BPL: BURPS1106A_0707 BURPS1106A_0985(fkpB) BURPS1106A_2350
                 BURPS1106A_2366(tig) BURPS1106A_2599(ppiB) BURPS1106A_2613
                 BURPS1106A_A1541 BURPS1106A_A2474
            BPD: BURPS668_0693 BURPS668_0980(fkpB) BURPS668_2312
                 BURPS668_2324(tig) BURPS668_2548(ppiB) BURPS668_2560
                 BURPS668_A1626 BURPS668_A2612
            BTE: BTH_I0576 BTH_I0782 BTH_I1911 BTH_I1938 BTH_I1939
                 BTH_I2118(tig) BTH_I2129 BTH_I2136 BTH_II0554(fbp) BTH_II1253
            PNU: Pnuc_0856
            BPE: BP1236(fkpB) BP1732(ppiD) BP1906(ppiB) BP3330 BP3561
            BPA: BPP1851(fkpB) BPP2281(ppiB) BPP3044(ppiD) BPP3352 BPP3666
            BBR: BB1733(ppiB) BB3007(ppiD) BB3257(fkpB) BB3803 BB4101
            RFR: Rfer_0097 Rfer_1277 Rfer_1345 Rfer_1346 Rfer_1971 Rfer_2249
                 Rfer_2399 Rfer_2796 Rfer_3249
            POL: Bpro_0950 Bpro_2585 Bpro_2868 Bpro_3064 Bpro_3081 Bpro_4591
                 Bpro_4719 Bpro_4862
            AAV: Aave_1387 Aave_2316 Aave_2317
            AJS: Ajs_1621 Ajs_3146
            VEI: Veis_4230
            MPT: Mpe_A0203 Mpe_A1704 Mpe_A1955 Mpe_A2212 Mpe_A2457 Mpe_A2458
                 Mpe_A2569 Mpe_A2694
            HAR: HEAR0367(surA) HEAR0807(fklB) HEAR1283(ppiB) HEAR1284(ppiA)
                 HEAR1658 HEAR1739 HEAR1748 HEAR2169(slyD)
            MMS: mma_0418(surA) mma_0724(fkpA) mma_1287(slyD) mma_1535
                 mma_2109 mma_2110 mma_2374 mma_2550(fkpB)
            NEU: NE0041(ppiB) NE0042(ppiA) NE0079(fkpA) NE0882(surA) NE1418
                 NE1706(slyD) NE2206(ppiD)
            NET: Neut_0192 Neut_0193 Neut_0662 Neut_1217 Neut_1532
            NMU: Nmul_A0520 Nmul_A0669 Nmul_A0751 Nmul_A1884 Nmul_A1885
                 Nmul_A2114 Nmul_A2336
            EBA: ebA1140(surA) ebA4137 ebA4212(fkpA) ebA4788(ppiB)
                 ebA4790(ppiA) ebA6468(slyD) ebA6504 ebA6665(ppiD) ebB150(fkpB)
            AZO: azo0546(nifM) azo1056(ppiB) azo1057(ppiA) azo1203(slpA)
                 azo1568(ppiD) azo2062 azo2886(surA) azo3319(fkbP)
            DAR: Daro_0915 Daro_0916 Daro_0990 Daro_1933 Daro_2349 Daro_2906
                 Daro_3044 Daro_3469 Daro_3658
            TBD: Tbd_0587 Tbd_1673 Tbd_1859 Tbd_1904 Tbd_2047 Tbd_2152
                 Tbd_2338
            MFA: Mfla_0379 Mfla_0496 Mfla_0497 Mfla_0836 Mfla_1413 Mfla_1881
                 Mfla_1891 Mfla_2150
            HPY: HP1123(slyD) HP1441(ppi)
            HPJ: jhp1052(slyD) jhp1334(ppiA)
            HPA: HPAG1_0171 HPAG1_0780 HPAG1_0958 HPAG1_1062 HPAG1_1367
            HHE: HH0437(slyD) HH1615(ppiA)
            HAC: Hac_0177(ppi) Hac_0590(slyD)
            WSU: WS0363(ppiA) WS0380 WS0525(slyD)
            TDN: Tmden_0504 Tmden_1292 Tmden_1395 Tmden_1460
            CJE: Cj0115(slyD) Cj1171c(ppi)
            CJR: CJE0110(slyD) CJE0186(tig) CJE1305(ppiB)
            CJJ: CJJ81176_0150(slyD) CJJ81176_0224(tig) CJJ81176_1186(ppiB)
            CJU: C8J_1115(ppi)
            CJD: JJD26997_0122(slyD) JJD26997_0558(ppiB)
            CFF: CFF8240_0425 CFF8240_0514 CFF8240_1517 CFF8240_1693(tig)
            CCV: CCV52592_1036 CCV52592_1078(ppi) CCV52592_1498(tig)
                 CCV52592_1746
            CHA: CHAB381_0016(tig) CHAB381_0696 CHAB381_1076 CHAB381_1221
                 CHAB381_1427 CHAB381_1752
            CCO: CCC13826_0094(slyD) CCC13826_0432 CCC13826_0902 CCC13826_1513
                 CCC13826_1780(tig)
            ABU: Abu_0376(ppiC) Abu_0427 Abu_1381 Abu_1587(slyD) Abu_1912(ppi)
            NIS: NIS_0537 NIS_0561 NIS_1212(slyD)
            SUN: SUN_0602 SUN_0675 SUN_1759(slyD) SUN_2255(ppiC)
            GSU: GSU0228 GSU0383 GSU0823(ppiC) GSU0894 GSU1793(tig)
                 GSU2274(fbP-2) GSU2429 GSU3319(ppiA)
            GME: Gmet_0137 Gmet_0259 Gmet_0815 Gmet_1817 Gmet_2362 Gmet_2722
                 Gmet_3146
            PCA: Pcar_0089 Pcar_0293 Pcar_0572 Pcar_0774 Pcar_1050 Pcar_1069
                 Pcar_2076 Pcar_2077 Pcar_2604 Pcar_2669 Pcar_2880
            PPD: Ppro_0570 Ppro_2730 Ppro_3065
            DVU: DVU0284(ppiB-1) DVU1065 DVU1334(tig) DVU1470(ppiC)
                 DVU1873(ppiB-2) DVU1901 DVU2569
            DVL: Dvul_1609 Dvul_2696
            DDE: Dde_0209 Dde_1407 Dde_1662 Dde_2010 Dde_2037 Dde_2668
            LIP: LI0166(ppiB) LI0167 LI0303(ppi) LI1114
            BBA: Bd0017(surA) Bd0018(ppiC) Bd0019(ppiD) Bd0177(ppiA)
                 Bd0258(prsA) Bd0336(slyD) Bd0722(slyD) Bd1903(fkpA)
                 Bd2569(fkpA) Bd3764(tig)
            DPS: DP0996 DP1167 DP2641 DP3115
            ADE: Adeh_1220 Adeh_1651 Adeh_1652 Adeh_2074 Adeh_2501 Adeh_3398
                 Adeh_3603 Adeh_4335
            AFW: Anae109_2157
            MXA: MXAN_0468 MXAN_0469 MXAN_1176 MXAN_2013(tig) MXAN_2404(slyD)
                 MXAN_2644 MXAN_3763 MXAN_3764 MXAN_3831(slyD) MXAN_4085
                 MXAN_4676 MXAN_6849 MXAN_7110
            SAT: SYN_00555 SYN_02039 SYN_02487 SYN_02784 SYN_03141
            SFU: Sfum_0160 Sfum_0568 Sfum_1338 Sfum_2710 Sfum_2744 Sfum_2853
                 Sfum_3231 Sfum_3480 Sfum_4039
            RPR: RP576(prsA)
            RTY: RT0565(prsA)
            RCO: RC0880(prsA)
            RFE: RF_0942(prsA)
            RBE: RBE_0898(prsA)
            WOL: WD0797
            WBM: Wbm0530
            AMA: AM516
            ERU: Erum3500(ppiD)
            ERW: ERWE_CDS_03570(ppiD)
            ERG: ERGA_CDS_03530(ppiD)
            ECN: Ecaj_0201 Ecaj_0334
            ECH: ECH_0731 ECH_0902(tig)
            PUB: SAR11_0712 SAR11_0859(fbp) SAR11_0879(tig) SAR11_0987(ppiB)
                 SAR11_1331(ppiA)
            MLO: mll0727 mll0728 mll7863 mlr0613
            MES: Meso_1403 Meso_1404 Meso_1471 Meso_1637 Meso_1760
            SME: SMc00234(ppiD) SMc00581 SMc01208(ppiB) SMc01700(ppiA)
                 SMc02451
            ATU: Atu1105 Atu1679(ppiB) Atu1680(ppiB) Atu1686(ppiD)
            ATC: AGR_C_2045 AGR_C_3088 AGR_C_3090 AGR_C_3099
            RET: RHE_CH01451 RHE_CH02114(ppiA) RHE_CH02115(ppiB)
                 RHE_CH02173(ppiD1) RHE_CH03769(ppiD2)
            RLE: RL1566 RL2404 RL2405 RL2492(ppiD) RL4297
            BME: BMEI0845 BMEI0887 BMEI0888 BMEI1265 BMEII0954
            BMF: BAB1_0706 BAB1_1117 BAB1_1118 BAB1_1162 BAB2_0908
            BMS: BR0684 BR1093 BR1094 BR1139 BRA0295
            BMB: BruAb1_0703 BruAb1_1099 BruAb1_1100 BruAb1_1145 BruAb2_0886
            BOV: BOV_0895(tig)
            BJA: bll4104 bll4690(ppiB) bll4692 blr2405(fbp) blr4808
            BRA: BRADO0589 BRADO1884(fbp) BRADO2210 BRADO2231 BRADO3995(ppiB)
                 BRADO3996(ppiA) BRADO4108
            BBT: BBta_2200(fbp) BBta_4367(ppiB) BBta_4368(ppiA) BBta_4481
                 BBta_7589
            RPA: RPA0511 RPA2546 RPA2602 RPA2604 RPA2889 RPA3064
            RPB: RPB_0529 RPB_2796 RPB_2871 RPB_2873 RPB_2929
            RPC: RPC_0525 RPC_2468 RPC_2532 RPC_2589 RPC_2590
            RPD: RPD_0300 RPD_2540 RPD_2599 RPD_2601 RPD_2827 RPD_2969
            RPE: RPE_0147 RPE_2592 RPE_2711 RPE_2767 RPE_2769 RPE_3295
                 RPE_3460
            NWI: Nwi_0389 Nwi_1680 Nwi_1797 Nwi_1798 Nwi_1836 Nwi_2171
            NHA: Nham_0484 Nham_1767 Nham_1769 Nham_2343 Nham_2573
            BHE: BH05420 BH05670(ppiD) BH10090(ppiB1) BH10100(ppiB2)
            BQU: BQ01880 BQ04600 BQ04830(ppiD) BQ07820(ppiB1) BQ07830(ppiB2)
            BBK: BARBAKC583_0553(tig)
            CCR: CC_0979 CC_1584 CC_1688 CC_1894
            SIL: SPO0058 SPO2145 SPO2233 SPO2234 SPO2456 SPOA0438
            SIT: TM1040_0946 TM1040_1085 TM1040_1086 TM1040_1144 TM1040_2916
                 TM1040_3571
            RSP: RSP_1168(surA) RSP_2005(ybaU) RSP_2903 RSP_4042 RSP_4043
            JAN: Jann_0290 Jann_1811 Jann_1883 Jann_1917 Jann_1918
            RDE: RD1_0383 RD1_2446 RD1_3006(ppiB) RD1_3007 RD1_3049(tig)
                 RD1_3122(surA) RD1_3203 RD1_3928(slyD)
            MMR: Mmar10_1223 Mmar10_1826 Mmar10_1870 Mmar10_2604 Mmar10_2702
            HNE: HNE_0170 HNE_0375 HNE_0897 HNE_1791 HNE_2069(tig) HNE_2150
                 HNE_2758
            ZMO: ZMO0467 ZMO0773 ZMO0853 ZMO1312 ZMO1712
            NAR: Saro_0837 Saro_0888 Saro_0966 Saro_2251
            SAL: Sala_0544 Sala_1148 Sala_1476 Sala_2192
            ELI: ELI_03005 ELI_05585 ELI_07135 ELI_08530 ELI_08890
            GOX: GOX0256 GOX0301 GOX0889 GOX1677 GOX2285
            GBE: GbCGDNIH1_0623 GbCGDNIH1_0825 GbCGDNIH1_1217 GbCGDNIH1_1309
                 GbCGDNIH1_2196
            RRU: Rru_A0395 Rru_A0433 Rru_A1742
            MAG: amb1814 amb2383 amb2384 amb3716 amb3872
            MGM: Mmc1_0349 Mmc1_2126 Mmc1_2149 Mmc1_2327
            ABA: Acid345_2561 Acid345_2580 Acid345_4533
            SUS: Acid_1293 Acid_4828
            BSU: BG10464(prsA) BG10512(ppiB)
            BHA: BH1177(prsA) BH1545
            BAN: BA1041(prsA-1) BA1169(prsA-2) BA2336(prsA-3) BA4283
            BAR: GBAA1041(prsA-1) GBAA1169(prsA-2) GBAA2336(prsA-3) GBAA4283
            BAA: BA_1599 BA_1711 BA_2835 BA_4741
            BAT: BAS0974(prsA) BAS1084(prsA) BAS2178(prsA) BAS3972
            BCE: BC1043(prsA) BC1161 BC2272(prsA) BC2862(prsA) BC4061
            BCA: BCE_1145(prsA) BCE_1280(prsA) BCE_2359(prsA) BCE_4131
                 BCE_4564(tiG)
            BCZ: BCZK0952(prsA) BCZK1061(prsA) BCZK2101(prsA) BCZK3817(ppiB)
            BTK: BT9727_0962(prsA) BT9727_1066(prsA) BT9727_2115(prsA)
                 BT9727_2619(prsA) BT9727_3802(ppiB)
            BTL: BALH_0931(prsA) BALH_1026(prsA) BALH_2079(prsA)
                 BALH_4066(tig)
            BLI: BL02827(prsA) BL05245(ppiB)
            BLD: BLi01072(prsA) BLi02481(ppiB)
            BCL: ABC0749 ABC1527(prsA) ABC1802(ppiB)
            BAY: RBAM_021460
            BPU: BPUM_0184 BPUM_2066 BPUM_2464(tig)
            OIH: OB1148(prsA) OB1360 OB1832(ppiB)
            GKA: GK0656 GK2298
            SAU: SA0815 SA1659(prsA)
            SAV: SAV0954 SAV1841(prsA)
            SAM: MW0836 MW1782(prsA)
            SAR: SAR0916 SAR1932
            SAS: SAS0824 SAS1762
            SAC: SACOL0957 SACOL1722(tig) SACOL1897
            SAB: SAB0821 SAB1535c(tig) SAB1774
            SAA: SAUSA300_0857 SAUSA300_1622(tig) SAUSA300_1790(prsA)
            SAO: SAOUHSC_00891 SAOUHSC_01779 SAOUHSC_01972
            SAJ: SaurJH9_0954
            SAH: SaurJH1_0973
            SEP: SE0648 SE1521
            SER: SERP0540 SERP1239(tig) SERP1376
            SHA: SH1121(prsA) SH1997
            SSP: SSP0958 SSP1821
            LMO: lmo1444 lmo2219 lmo2376
            LMF: LMOf2365_1284(tig) LMOf2365_1463(prsA-1)
                 LMOf2365_2252(prsA-2) LMOf2365_2349
            LIN: lin1482 lin2322 lin2475
            LWE: lwe1284(tig) lwe1460(prsA-1) lwe2236(prsA) lwe2324
            LLA: L113864(ppiB) L164604(pmpA) L168484(ppiA)
            LLC: LACR_0411 LACR_0969 LACR_1888 LACR_C43
            LLM: llmg_0385(ppiA) llmg_0519(tig) llmg_1646(ppiB)
                 llmg_1907(pmpA)
            SPY: SPy_0457 SPy_1390 SPy_2037
            SPZ: M5005_Spy_0371 M5005_Spy_1133(prsA) M5005_Spy_1331
                 M5005_Spy_1612(tig) M5005_Spy_1732(prsA)
            SPM: spyM18_0499(cypB) spyM18_1400 spyM18_2097
            SPG: SpyM3_0321(cypB) SpyM3_1059(prtM.1) SpyM3_1740(prtM.2)
            SPS: SPs0804 SPs1536 SPs1736
            SPH: MGAS10270_Spy0375 MGAS10270_Spy1203(surA) MGAS10270_Spy1447
                 MGAS10270_Spy1680(ropA) MGAS10270_Spy1800
            SPI: MGAS10750_Spy0373 MGAS10750_Spy1240(surA) MGAS10750_Spy1440
                 MGAS10750_Spy1667(ropA) MGAS10750_Spy1825
            SPJ: MGAS2096_Spy0391 MGAS2096_Spy1199(surA) MGAS2096_Spy1352
                 MGAS2096_Spy1635 MGAS2096_Spy1636(ropA) MGAS2096_Spy1764
            SPK: MGAS9429_Spy0374 MGAS9429_Spy1180(surA) MGAS9429_Spy1326
                 MGAS9429_Spy1615(ropA) MGAS9429_Spy1740
            SPF: SpyM50242(tig) SpyM50725(prsA1) SpyM51695(prsA2)
            SPA: M6_Spy0395 M6_Spy1108(prsA) M6_Spy1377 M6_Spy1620
                 M6_Spy1732(prsA)
            SPB: M28_Spy0360 M28_Spy1127(prsA) M28_Spy1372 M28_Spy1601(tig)
                 M28_Spy1718(prsA)
            SPN: SP_0771 SP_0981
            SPR: spr0679(ppiA) spr0884(ppmA)
            SPD: SPD_0365(tig)
            SAG: SAG0808 SAG1530
            SAN: gbs0827 gbs1586
            SAK: SAK_0155(tig) SAK_0393 SAK_0932(prsA) SAK_1553
            SMU: SMU.1631 SMU.648(prtM)
            STC: str0515(ppiA)
            STL: stu0515(ppiA)
            SSA: SSA_0753(prtM) SSA_1629(ppiA) SSA_1841(pplB) SSA_1998(ropA)
            SGO: SGO_0412(tig) SGO_1463 SGO_1572
            LPL: lp_1452(prtM1) lp_2231c(ppiB) lp_3193(prtM2)
            LJO: LJ1175 LJ1673
            LAC: LBA1126 LBA1588(prtM)
            LSA: LSA0436 LSA0626(prtM)
            LSL: LSL_0055(ppiB) LSL_0475(surA) LSL_0643(tig)
            LDB: Ldb1104(ppiB) Ldb1533(prsA)
            LBU: LBUL_1004 LBUL_1424
            LBR: LVIS_1174 LVIS_1484
            LCA: LSEI_0827 LSEI_1722 LSEI_2271
            LRE: Lreu_1534
            EFA: EF0685 EF1534 EF2898
            OOE: OEOE_1277
            STH: STH2625 STH2667 STH2943
            CAC: CAC0279 CAC2769(ppiB)
            CPE: CPE1567(ppiB) CPE2483(prsA) CPE2566
            CPF: CPF_0262 CPF_1648(tig) CPF_2806 CPF_2891
            CPR: CPR_0253 CPR_1386(tig) CPR_2492 CPR_2570
            CTC: CTC00195 CTC00215 CTC00678
            CNO: NT01CX_0372 NT01CX_0777 NT01CX_1021
            CTH: Cthe_0068
            CDF: CD0331(ppiB) CD1357 CD3500(prsA)
            CBO: CBO3561(ppiB)
            CBA: CLB_3269(tig) CLB_3619(prsA-1)
            CBH: CLC_3143(tig) CLC_3516(prsA-1)
            CBF: CLI_3371(tig) CLI_3758(prsA-1)
            CBE: Cbei_0033 Cbei_0553
            CKL: CKL_0153(prsA) CKL_2308(rotA)
            AMT: Amet_1282
            CHY: CHY_0201 CHY_0324(tig)
            DSY: DSY0190 DSY1841 DSY3510
            DRM: Dred_1741
            SWO: Swol_2433
            TTE: TTE2564(surA2)
            MMO: MMOB0850(tig) MMOB1120(grpE)
            AYW: AYWB_334(tig) AYWB_548
            MTU: Rv0009(ppiA) Rv2582(ppiB)
            MTC: MT0011(ppi-1) MT2659(ppi-2)
            MBO: Mb0009(ppiA) Mb2613(ppiB)
            MBB: BCG_0009(ppiA_1) BCG_0039(ppiA_2) BCG_2605(ppiB)
            MLE: ML0011(ppiA) ML0492(ppiB)
            MPA: MAP0011(ppiA) MAP1050c(ppiB)
            MAV: MAV_0013 MAV_1712(tig)
            MSM: MSMEG_0024 MSMEG_3434 MSMEG_4674(tig) MSMEG_5664
            MVA: Mvan_0017
            MGI: Mflv_0817
            MMC: Mmcs_0010 Mmcs_4450
            MKM: Mkms_0018
            MJL: Mjls_0010
            CGL: NCgl0033(cgl0034) NCgl0796(cgl0830) NCgl1587(cgl1649)
            CGB: cg0048(ppiA) cg0950(fkpA) cg1857(ppiB) cg2647(tig)
            CEF: CE0029 CE0906 CE1765
            CDI: DIP0025(ppiA) DIP0786 DIP1363
            CJK: jk0033(ppiA) jk0427(fkb) jk1047(ppiB)
            NFA: nfa13310 nfa1910 nfa36650 nfa38520 nfa6570
            RHA: RHA1_ro03690 RHA1_ro04999 RHA1_ro06901 RHA1_ro06902(ppiB)
            SCO: SCO1510(SC9C5.34) SCO1638(fkbP) SCO3856(SCH69.26c)
                 SCO5939(SC7H1.09) SCO7510(cypH)
            SMA: SAV4329(ppiA) SAV6687(fkbP) SAV6842(ppiB)
            LXX: Lxx00160(ppiB) Lxx08960(fkb) Lxx10860(ppiB)
            CMI: CMM_0010(ppiA) CMM_1772 CMM_2161
            ART: Arth_0012
            AAU: AAur_2180 AAur_2181 AAur_2383(tig)
            PAC: PPA0718 PPA1100 PPA1384 PPA2163
            NCA: Noca_0017
            TFU: Tfu_2820 Tfu_3069
            FRA: Francci3_1381 Francci3_4444
            FAL: FRAAL2152 FRAAL2879(ppiC) FRAAL3370(fklB) FRAAL6765(fkpA)
            ACE: Acel_0012
            KRA: Krad_0022
            SEN: SACE_0034 SACE_0709 SACE_2030 SACE_7072
            STP: Strop_4482
            BLO: BL1016(fkbP) BL1442
            BAD: BAD_0651(fkbP) BAD_1001
            RXY: Rxyl_0911
            FNU: FN0263 FN0342 FN1320 FN1800 FN1875
            RBA: RB10129(mip) RB1279 RB3240(fkpA) RB342(fkpA) RB3446
                 RB7244(ppiB) RB8476(ppiC) RB8649(cypH)
            CTR: CT541(mip)
            CTA: CTA_0591(mip) CTA_0768(tig)
            CMU: TC0828
            CPN: CPn0661(mip)
            CPA: CP0086
            CPJ: CPj0661(mip)
            CPT: CpB0687
            CCA: CCA00078(mip)
            CAB: CAB080(mip)
            CFE: CF0926(mip)
            PCU: pc0383(mip)
            TPA: TP0349 TP0862(fklB) TP0947
            TDE: TDE1671(tig) TDE1925 TDE2287
            LIL: LA2194 LA2535(ppiA) LA2550
            LIC: LIC11424(fkp) LIC11438(ppi) LIC11731(slyD)
            LBJ: LBJ_1357(slpA) LBJ_1690
            LBL: LBL_1582(slpA) LBL_1898
            SYN: sll0227(ppiB) slr1251(cyp) slr1761(ytfC)
            SYW: SYNW0679 SYNW0759 SYNW1264 SYNW1625
            SYC: syc0125_c(rot) syc0875_d(ppiB) syc1544_c(ppiB)
                 syc1749_d(ytfC)
            SYF: Synpcc7942_0653 Synpcc7942_1431 Synpcc7942_2354
                 Synpcc7942_2566
            SYD: Syncc9605_0874 Syncc9605_1391 Syncc9605_1990
            SYE: Syncc9902_0670 Syncc9902_1097 Syncc9902_1524
            SYG: sync_0031 sync_0066(tig) sync_0756 sync_0899 sync_1384(ppi)
            SYR: SynRCC307_0030 SynRCC307_1355(ppiB) SynRCC307_1790(fkpA)
            SYX: SynWH7803_0031 SynWH7803_1251(ppiB)
            CYA: CYA_0114 CYA_1482 CYA_1589 CYA_2088
            CYB: CYB_0395 CYB_1473 CYB_2104 CYB_2506
            TEL: tlr0137 tlr1102
            GVI: gll2610 glr0841 glr0973
            ANA: all4287 alr0577
            AVA: Ava_0331 Ava_1240 Ava_2316
            PMA: Pro0942(ppiB) Pro1252(ppiB) Pro1367(fkpA)
            PMM: PMM0894 PMM1155(ppiA) PMM1293
            PMT: PMT0341 PMT0707 PMT1177(ppiB)
            PMN: PMN2A_0765 PMN2A_0860
            PMI: PMT9312_0906 PMT9312_1254 PMT9312_1389
            PMB: A9601_09671 A9601_13321 A9601_14921 A9601_18641(tig)
            PMC: P9515_09761 P9515_13221 P9515_14541 P9515_18451(tig)
            PMF: P9303_00701(tig) P9303_08461 P9303_15141 P9303_19721(fkpA)
            PMG: P9301_09651 P9301_13471 P9301_14781(fkpA) P9301_18451(tig)
            PMH: P9215_19281(tig)
            PME: NATL1_09891 NATL1_16051 NATL1_17131 NATL1_21241(tig)
            TER: Tery_0301 Tery_0511 Tery_1467
            BTH: BT_2079 BT_2976 BT_2977 BT_3802 BT_3848
            BFR: BF2021 BF3770 BF4072 BF4113 BF4514
            BFS: BF2075 BF3558 BF3888 BF3928 BF4308(fklB)
            PGI: PG0415 PG0709(fkpA) PG0710 PG1226 PG1315(slyD)
            SRU: SRU_0478 SRU_1416 SRU_1797 SRU_1799 SRU_2208 SRU_2431
                 SRU_2673(tig) SRU_2676
            CHU: CHU_0191(surA) CHU_0192 CHU_0493(ppiC) CHU_1613(ppiA)
                 CHU_1687(fklB) CHU_1705(tig) CHU_3084(ppiC) CHU_3268
                 CHU_3430(slyD) CHU_3652 CHU_3663(fklB) CHU_3665(fkpA)
            GFO: GFO_0786 GFO_1007 GFO_1544(fkpB) GFO_2506(surA) GFO_2538
                 GFO_2975
            FPS: FP1167(surA) FP1168 FP1890(ppiB) FP1891(ppiA) FP1908(ppiC)
            CTE: CT1813(ppiA) CT1896 CT2264(surA)
            CCH: Cag_0028(surA) Cag_0246 Cag_1209 Cag_1349
            PLT: Plut_0009(surA) Plut_0293 Plut_0479
            DET: DET0709(tig) DET1240
            DEH: cbdb_A1159(ppiB) cbdb_A664(tig)
            DEB: DehaBAV1_1053
            RRS: RoseRS_2438 RoseRS_3720
            RCA: Rcas_2216 Rcas_3544
            DRA: DR_0071 DR_0237 DR_1063 DR_1839 DR_1893 DR_2464 DR_2542
            DGE: Dgeo_0070 Dgeo_0740 Dgeo_0773 Dgeo_1601 Dgeo_1650 Dgeo_1945
                 Dgeo_2219
            TTH: TTC0233 TTC0249 TTC1637
            TTJ: TTHA0346 TTHA0602
            AAE: aq_1694
            MJA: MJ0278(slyD) MJ0825(slyD)
            MMP: MMP0572(slyD) MMP1128(ppiB) MMP1129(ppiB) MMP1190
            MMQ: MmarC5_0456
            MAC: MA1661 MA2813(slyD) MA3136 MA3137 MA3138
            MBA: Mbar_A1939 Mbar_A1940 Mbar_A1941 Mbar_A2249 Mbar_A3616
            MMA: MM_0380 MM_0381 MM_0382 MM_2656 MM_2829
            MBU: Mbur_0313 Mbur_1485 Mbur_2255
            MTP: Mthe_0045
            MHU: Mhun_1165 Mhun_1166
            MEM: Memar_0036
            MBN: Mboo_0460 Mboo_0461
            MTH: MTH1338
            MST: Msp_0035 Msp_0325
            MSI: Msm_0930 Msm_1367
            MKA: MK1231(slpA)
            AFU: AF1989(slyD)
            HAL: VNG1294G(slyD) VNG1914G(ppiA)
            HMA: rrnAC0638(ppiB2) rrnAC1230(slyD) rrnAC3303(ppiB1)
            HWA: HQ1886A(mtfK1) HQ2586A(mtfK2) HQ3123A(ppiA) HQ3692A(mtfK1)
            NPH: NP2228A(mtfK_1) NP3056A(ppiA) NP3090A(mtfK_2)
            TAC: Ta1011
            TVO: TVN0578
            PTO: PTO0328 PTO0637
            PAB: PAB1864(slyD)
            PFU: PF1401
            TKO: TK0441 TK1850
            RCI: LRC433(ppi-1) LRC434(ppi-2) RCIX757(ppiB) RRC200(ppi-3)
                 RRC331(ppi-4)
            APE: APE_0517
            SSO: SSO0758
            STO: ST0345
            SAI: Saci_0641
            PAI: PAE0805
            NEQ: NEQ002
STRUCTURES  PDB: 1A33  1A7X  1AK4  1AWQ  1AWR  1AWS  1AWT  1AWU  1AWV  1B6C  
                 1BCK  1BKF  1BL4  1C5F  1CWF  1CWH  1CWI  1CWJ  1CWK  1CWL  
                 1CWM  1CWO  1D6O  1D7H  1D7I  1D7J  1DYW  1EYM  1F8A  1FAP  
                 1FD9  1FGL  1FKJ  1FKK  1FKL  1H0P  1I6C  1I8G  1I8H  1IHG  
                 1IIP  1IST  1IX5  1J2A  1J4H  1J4I  1J4R  1JNS  1JNT  1JVW  
                 1KT0  1KT1  1L1P  1LOP  1M5Y  1M63  1M9C  1M9D  1M9E  1M9F  
                 1M9X  1M9Y  1MF8  1N1A  1NMK  1NMV  1NMW  1NSG  1OCA  1OMS  
                 1P5Q  1P9Y  1PBK  1PIN  1Q1C  1Q6H  1Q6I  1Q6U  1QNG  1QNH  
                 1QZ2  1TCO  1U79  1V9T  1VAI  1VDN  1W74  1W8L  1W8M  1W8V  
                 1XWN  1XYH  1Y0O  1YND  1YW5  1Z81  1ZCN  1ZK6  1ZKC  1ZKF  
                 1ZMF  2A2N  2ALF  2BIT  2BIU  2CK1  2CMT  2CQB  2DG3  2DG4  
                 2DG9  2ESL  2F21  2FAP  2FU0  2GW2  2HAQ  2HE9  2HQJ  2IGV  
                 2IGW  2ITK  2NUL  2PBC  2PV1  2PV2  2PV3  2Q5A  2R99  2RMA  
                 2RMB  2UZ5  3FAP  4FAP  
DBLINKS     IUBMB Enzyme Nomenclature: 5.2.1.8
            ExPASy - ENZYME nomenclature database: 5.2.1.8
            ExplorEnz - The Enzyme Database: 5.2.1.8
            ERGO genome analysis and discovery system: 5.2.1.8
            BRENDA, the Enzyme Database: 5.2.1.8
            CAS: 95076-93-0
///
ENTRY       EC 5.2.1.9                  Enzyme
NAME        farnesol 2-isomerase;
            farnesol isomerase
CLASS       Isomerases;
            cis-trans-Isomerases;
            cis-trans Isomerases (only sub-subclass identified to date)
SYSNAME     2-trans,6-trans-farnesol 2-cis-trans-isomerase
REACTION    2-trans,6-trans-farnesol = 2-cis,6-trans-farnesol [RN:R03265]
ALL_REAC    R03265
SUBSTRATE   2-trans,6-trans-farnesol [CPD:C01126]
PRODUCT     2-cis,6-trans-farnesol [CPD:C03220]
REFERENCE   1
  AUTHORS   Anastasis, P., Freer, I., Gilmore, C., Mackie, H., Overton, K.,
            Picken, D. and Swanson, S.
  TITLE     Biosynthesis of gamma-bisabolene in tissue-cultures of Andrographis
            paniculata.
  JOURNAL   Can. J. Chem. 62 (1984) 2079-2088.
  ORGANISM  Andrographis paniculata
DBLINKS     IUBMB Enzyme Nomenclature: 5.2.1.9
            ExPASy - ENZYME nomenclature database: 5.2.1.9
            ExplorEnz - The Enzyme Database: 5.2.1.9
            ERGO genome analysis and discovery system: 5.2.1.9
            BRENDA, the Enzyme Database: 5.2.1.9
            CAS: 94047-16-2
///
ENTRY       EC 5.2.1.10                 Enzyme
NAME        2-chloro-4-carboxymethylenebut-2-en-1,4-olide isomerase;
            2-chlorocarboxymethylenebutenolide isomerase;
            chlorodienelactone isomerase
CLASS       Isomerases;
            cis-trans-Isomerases;
            cis-trans Isomerases (only sub-subclass identified to date)
SYSNAME     2-chloro-4-carboxymethylenebut-2-en-1,4-olide cis-trans-isomerase
REACTION    cis-2-chloro-4-carboxymethylenebut-2-en-1,4-olide =
            trans-2-chloro-4-carboxymethylenebut-2-en-1,4-olide [RN:R04576]
ALL_REAC    R04576
SUBSTRATE   cis-2-chloro-4-carboxymethylenebut-2-en-1,4-olide [CPD:C04706]
PRODUCT     trans-2-chloro-4-carboxymethylenebut-2-en-1,4-olide [CPD:C04729]
REFERENCE   1
  AUTHORS   Schwien, U., Schmidt, E., Knackmuss, H.-J. and Reinecke, W.
  TITLE     Degradation of chlorosubstituted aromatic-compounds by Pseudomonas
            sp. strain-B13 - fate of 3,5-dichlorocatechol.
  JOURNAL   Arch. Microbiol. 150 (1988) 78-84.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00627  1,4-Dichlorobenzene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 5.2.1.10
            ExPASy - ENZYME nomenclature database: 5.2.1.10
            ExplorEnz - The Enzyme Database: 5.2.1.10
            ERGO genome analysis and discovery system: 5.2.1.10
            BRENDA, the Enzyme Database: 5.2.1.10
            CAS: 115629-29-3
///
ENTRY       EC 5.2.1.11       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Isomerases;
            cis-trans-Isomerases;
            cis-trans Isomerases (only sub-subclass identified to date)
COMMENT     Deleted entry: 4-hydroxyphenylacetaldehyde-oxime isomerase. The
            existence of this enzyme has been called into question by one of the
            authors of the reference cited. (EC 5.2.1.11 created 1992, deleted
            2005)
DBLINKS     IUBMB Enzyme Nomenclature: 5.2.1.11
            ExPASy - ENZYME nomenclature database: 5.2.1.11
            ExplorEnz - The Enzyme Database: 5.2.1.11
            ERGO genome analysis and discovery system: 5.2.1.11
            BRENDA, the Enzyme Database: 5.2.1.11
///
ENTRY       EC 5.2.1.-                  Enzyme
CLASS       Isomerases;
            cis-trans-Isomerases
REACTION    trans-beta-D-Glucosyl-2-hydroxycinnamate <=>
            cis-beta-D-Glucosyl-2-hydroxycinnamate [RN:R04686]
SUBSTRATE   trans-beta-D-Glucosyl-2-hydroxycinnamate [CPD:C05158]
PRODUCT     cis-beta-D-Glucosyl-2-hydroxycinnamate [CPD:C05839]
///
ENTRY       EC 5.3.1.1                  Enzyme
NAME        triose-phosphate isomerase;
            phosphotriose isomerase;
            triose phosphoisomerase;
            triose phosphate mutase;
            D-glyceraldehyde-3-phosphate ketol-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     D-glyceraldehyde-3-phosphate aldose-ketose-isomerase
REACTION    D-glyceraldehyde 3-phosphate = glycerone phosphate [RN:R01015]
ALL_REAC    R01015
SUBSTRATE   D-glyceraldehyde 3-phosphate [CPD:C00118]
PRODUCT     glycerone phosphate [CPD:C00111]
INHIBITOR   2-Phosphoglycolate [CPD:C00988];
            Phosphoglycolohydroxamate [CPD:C05348]
REFERENCE   1
  AUTHORS   Meyer-Arendt, E., Beisenherz, G. and Bucher, T.
  TITLE     Triosephosphate isomerase.
  JOURNAL   Naturwissenschaften 40 (1953) 59.
REFERENCE   2
  AUTHORS   Meyerhof, O. and Beck, L.V.
  TITLE     Triosephosphate isomerase.
  JOURNAL   J. Biol. Chem. 156 (1944) 109-120.
  ORGANISM  rabbit
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00031  Inositol metabolism
            PATH: map00051  Fructose and mannose metabolism
            PATH: map00710  Carbon fixation
ORTHOLOGY   KO: K01803  triosephosphate isomerase (TIM)
GENES       HSA: 7167(TPI1)
            PTR: 451799(TPI1)
            MMU: 21991(Tpi1)
            RNO: 246267(LOC246267) 24849(Tpi1)
            CFA: 477711(TPI1)
            BTA: 281543(TPI1)
            GGA: 396435(TPI1)
            XLA: 380168(tpi)
            DRE: 192309(tpi1a) 192310(tpi1b)
            SPU: 548616(LOC548616)
            DME: Dmel_CG2171(Tpi)
            CEL: Y17G7B.7(tpi-1)
            ATH: AT2G21170(TIM) AT3G55440(ATCTIMC)
            OSA: 4325211 4327400 4334145 4347691
            CME: CMQ172C
            SCE: YDR050C(TPI1)
            AGO: AGOS_AGL201C
            PIC: PICST_91105(TPI1)
            CGR: CAGL0H08327g
            SPO: SPCC24B10.21(tpi1)
            ANI: AN5908.2 AN6900.2
            AFM: AFUA_2G11020 AFUA_5G13450
            AOR: AO090026000543 AO090120000493
            ANG: An14g04920(tpiA)
            CNE: CNE05000
            UMA: UM03299.1
            ECU: ECU11_0230
            DDI: DDB_0231425(tpiA)
            PFA: MAL3P6.25 PF14_0378
            CPV: cgd1_3040
            CHO: Chro.10337
            TAN: TA08590 TA10540
            TPV: TP04_0464 TP04_0676
            TET: TTHERM_00185230
            TBR: Tb09.211.1370 Tb11.02.3210
            TCR: 508647.200
            LMA: LmjF24.0850
            EHI: 202.t00008
            ECO: b3919(tpiA)
            ECJ: JW3890(tpiA)
            ECE: Z5464(tpiA)
            ECS: ECs4844
            ECC: c4871(tpiA)
            ECI: UTI89_C4503(tpiA)
            ECP: ECP_4128
            ECV: APECO1_2550(tpiA)
            ECW: EcE24377A_4453(tpiA)
            ECX: EcHS_A4150(tpiA)
            STY: STY3789(tpiA)
            STT: t3537(tpiA)
            SPT: SPA3924(tpiA)
            SEC: SC3970(tpiA)
            STM: STM4081(tpiA)
            YPE: YPO0085(tpiA)
            YPK: y0052(tpiA)
            YPM: YP_0089(tpiA)
            YPA: YPA_3456
            YPN: YPN_3763
            YPP: YPDSF_3818
            YPS: YPTB0081(tpiA)
            YPI: YpsIP31758_0096(tpiA)
            YEN: YE0093(tpi)
            SFL: SF3997(tpiA)
            SFX: S3750(tpiA)
            SFV: SFV_3575(tpiA)
            SSN: SSON_4088(tpiA)
            SBO: SBO_3936(tpiA)
            SDY: SDY_3826(tpiA)
            ECA: ECA0867(tpiA) ECA4272(tpiA)
            PLU: plu4772(tpiA)
            BUC: BU307(tpiA)
            BAS: BUsg297(tpiA)
            BAB: bbp285(tpiA)
            BCC: BCc_188(tpiA)
            WBR: WGLp274(tpiA)
            SGL: SG2176
            ENT: Ent638_4052
            SPE: Spro_4805
            BFL: Bfl601(tpiA)
            BPN: BPEN_623(tpiA)
            HIN: HI0678(tpiA)
            HIT: NTHI0800(tpiA)
            HIP: CGSHiEE_08710(tpiA)
            HDU: HD0762(tpiA)
            HSO: HS_1591(tpiA)
            PMU: PM1311(tpiA_1) PM1640(tpiA_2)
            MSU: MS0324(tpiA) MS0379(tpiA)
            APL: APL_1925(tpiA)
            ASU: Asuc_0677 Asuc_1601
            XFA: XF0303
            XFT: PD0245(tpiA)
            XCC: XCC2531(tpiA)
            XCB: XC_1587
            XCV: XCV2855(tpiA)
            XAC: XAC2707(tpiA)
            XOO: XOO3238(tpiA)
            XOM: XOO_3069(XOO3069)
            VCH: VC2670
            VCO: VC0395_A2243(tpiA)
            VVU: VV1_1343
            VVY: VV3025
            VPA: VP0239
            VFI: VF0206
            PPR: PBPRA0235
            PAE: PA4748(tpiA)
            PAU: PA14_62830(tpiA)
            PAP: PSPA7_5468(tpiA)
            PPU: PP_4715(tpiA)
            PPF: Pput_4581
            PST: PSPTO_4494(tpiA)
            PSB: Psyr_4184(tpiA)
            PSP: PSPPH_4195(tpiA)
            PFL: PFL_0839(tpiA)
            PFO: Pfl_0775
            PEN: PSEEN0790(tpiA)
            PMY: Pmen_3612
            PAR: Psyc_0065(tpiA)
            PCR: Pcryo_0070
            PRW: PsycPRwf_0152
            ACI: ACIAD0363(tpiA)
            SON: SO_1200(tpiA)
            SDN: Sden_1003
            SFR: Sfri_0986
            SAZ: Sama_0957
            SBL: Sbal_3243
            SBM: Shew185_3284
            SLO: Shew_2831
            SPC: Sputcn32_2838
            SSE: Ssed_3393
            SPL: Spea_3064
            SHE: Shewmr4_1022
            SHM: Shewmr7_1087
            SHN: Shewana3_1026
            SHW: Sputw3181_1066
            ILO: IL0972(tpiA)
            CPS: CPS_3448(tpiA)
            PHA: PSHAa0873(tpiA)
            PAT: Patl_1574
            SDE: Sde_0693 Sde_2717 Sde_3277
            PIN: Ping_2199
            MAQ: Maqu_3352
            CBU: CBU_1450(tpiA)
            CBD: COXBU7E912_0542(tpiA)
            LPN: lpg2792(tpiA)
            LPF: lpl2707(tpi)
            LPP: lpp2838(tpi)
            MCA: MCA0674(tpiA)
            FTU: FTT0080(tpiA)
            FTF: FTF0080(tpiA)
            FTW: FTW_0156(tpiA)
            FTL: FTL_1780
            FTH: FTH_1716(tpiA)
            FTA: FTA_1886(tpiA)
            FTN: FTN_1631(tpiA)
            TCX: Tcr_0815
            NOC: Noc_2566
            AEH: Mlg_1972
            HHA: Hhal_1767
            HCH: HCH_01235(tpiA)
            CSA: Csal_3078
            ABO: ABO_0325(tpiA)
            MMW: Mmwyl1_1023 Mmwyl1_3113
            AHA: AHA_2382(tpiA-1) AHA_3309(tpiA-2)
            DNO: DNO_0814(tpiA)
            BCI: BCI_0169(tpiA)
            RMA: Rmag_1076
            VOK: COSY_0977(tpiA)
            NME: NMB1887
            NMA: NMA0570(tpi)
            NMC: NMC0334(tpi)
            NGO: NGO0017
            CVI: CV_0939(tpiA)
            RSO: RSc2064(tpiA)
            REU: Reut_A0959
            REH: H16_A1047(tim)
            RME: Rmet_0925 Rmet_1520
            BMA: BMA1832(tpiA)
            BMV: BMASAVP1_A1127(tpiA)
            BML: BMA10299_A0740(tpiA)
            BMN: BMA10247_0410(tpiA)
            BXE: Bxe_A3216
            BVI: Bcep1808_2336
            BUR: Bcep18194_A5579
            BCN: Bcen_1639
            BCH: Bcen2424_2251
            BAM: Bamb_2289
            BPS: BPSL1209(tpiA)
            BPM: BURPS1710b_1432(tpiA)
            BPL: BURPS1106A_1296(tpiA)
            BPD: BURPS668_1287(tpiA)
            BTE: BTH_I1058(tpiA)
            PNU: Pnuc_1053
            BPE: BP0801(tpiA)
            BPA: BPP3426(tpiA)
            BBR: BB3876(tpiA)
            RFR: Rfer_1491
            POL: Bpro_3258
            PNA: Pnap_1422
            AAV: Aave_1261
            AJS: Ajs_0955
            VEI: Veis_2815
            MPT: Mpe_A1401(tpiA)
            HAR: HEAR1828(tpiA)
            MMS: mma_1460(tpiA)
            NEU: NE1779(cbbJ)
            NET: Neut_0920
            NMU: Nmul_A1089
            EBA: ebA4831(tpiA)
            AZO: azo1394(tim)
            DAR: Daro_0947
            TBD: Tbd_1140(cbbJ)
            MFA: Mfla_2064
            HPY: HP0194
            HPJ: jhp0180(tpi)
            HPA: HPAG1_0188
            HHE: HH1315(tpi)
            HAC: Hac_0379(tim)
            WSU: WS0424(tpiA)
            TDN: Tmden_1752
            CJE: Cj1401c(tpiA)
            CJR: CJE1588(tpiA)
            CJJ: CJJ81176_1400(tpiA)
            CJU: C8J_1315(tpiA)
            CJD: JJD26997_1735(tpiA)
            CFF: CFF8240_1427(tpiA)
            CCV: CCV52592_1247(tpiA)
            CHA: CHAB381_0779(tpiA)
            CCO: CCC13826_0514(tpiA) CCC13826_1506
            ABU: Abu_2134(tpiA)
            NIS: NIS_1490(tpiA)
            SUN: SUN_2202(tpiA)
            GSU: GSU1628
            GME: Gmet_1948
            GUR: Gura_2059
            PCA: Pcar_1333
            PPD: Ppro_1695
            DVU: DVU1677(tpiA)
            DVL: Dvul_1410
            DDE: Dde_1989
            LIP: LI1132(tpiA)
            BBA: Bd1051(tpiA)
            DPS: DP0100
            ADE: Adeh_1532
            AFW: Anae109_2280
            MXA: MXAN_2817(tpiA)
            SAT: SYN_03790
            SFU: Sfum_2059
            OTS: OTBS_0140(tpiA)
            WOL: WD0091(tpiA)
            WBM: Wbm0408
            AMA: AM559(tpiA)
            APH: APH_0624(tpiA)
            ERU: Erum4040(tpiA)
            ERW: ERWE_CDS_04170(tpiA)
            ERG: ERGA_CDS_04120(tpiA)
            ECN: Ecaj_0393
            ECH: ECH_0646(tpiA)
            NSE: NSE_0254(tpiA)
            PUB: SAR11_0927(tpiA)
            MLO: mll0610 mlr7275
            MES: Meso_1636
            PLA: Plav_3166
            SME: SMc01023(tpiA1) SMc01614(tpiA2)
            SMD: Smed_1067 Smed_2150
            ATU: Atu1620(tpiA)
            ATC: AGR_C_2987
            RET: RHE_CH02186(tpiAch) RHE_PF00040(tpiAf)
            RLE: RL2513(tpiA) pRL120209
            BME: BMEI0846 BMEII0425
            BMF: BAB1_1161(tpiA-1) BAB2_0367(tpiA-2)
            BMS: BR1138(tpiA-1) BRA0869(tpiA-2)
            BMB: BruAb1_1144(tpiA-1) BruAb2_0363(tpiA-2)
            BOV: BOV_1097(tpiA-2) BOV_A0816(tpiA-1)
            OAN: Oant_2051 Oant_2906
            BJA: bll4807(tpiA)
            BRA: BRADO4107(tpiA)
            BBT: BBta_4480(tpiA)
            RPA: RPA2888(cbbJ)
            RPB: RPB_2795
            RPC: RPC_2471
            RPD: RPD_2826
            RPE: RPE_2593
            NWI: Nwi_1835
            NHA: Nham_1736
            BHE: BH05680(tpiA)
            BQU: BQ04840(tpiA)
            BBK: BARBAKC583_0528(tpiA)
            XAU: Xaut_4380
            CCR: CC_1893
            SIL: SPO2621(tpiA)
            SIT: TM1040_0764
            RSP: RSP_1947(cbbJ)
            RSH: Rsph17029_0598
            RSQ: Rsph17025_0343
            JAN: Jann_1733
            RDE: RD1_2961(tpiA) RD1_3625(tpiA)
            PDE: Pden_4305
            MMR: Mmar10_1405
            HNE: HNE_1792(tpiA)
            ZMO: ZMO0465(tpi)
            NAR: Saro_2019
            SAL: Sala_1172
            SWI: Swit_2350
            ELI: ELI_06470
            GOX: GOX2217 GOX2284
            GBE: GbCGDNIH1_0826
            ACR: Acry_1236
            RRU: Rru_A1358 Rru_A1889
            MAG: amb1819
            MGM: Mmc1_1885
            ABA: Acid345_2544
            SUS: Acid_6502
            BSU: BG10897(tpi)
            BHA: BH3558(tpi)
            BAN: BA5366(tpi)
            BAR: GBAA5366(tpi)
            BAA: BA_0225
            BAT: BAS4987
            BCA: BCE_5240(tpiA)
            BCZ: BCZK4826(tpiA)
            BCY: Bcer98_3680
            BTK: BT9727_4816(tpiA)
            BTL: BALH_4629(tpiA)
            BLI: BL03466(tpiA)
            BLD: BLi03663(tpiA)
            BCL: ABC3019(tpi)
            BAY: RBAM_031280(tpiA)
            BPU: BPUM_3055(tpiA)
            OIH: OB2436(tpi)
            GKA: GK3056(tpi)
            SAU: SA0729(tpi)
            SAV: SAV0774(tpi)
            SAM: MW0736(tpi)
            SAR: SAR0830(tpiA)
            SAS: SAS0740
            SAC: SACOL0840(tpiA)
            SAB: SAB0730(tpiA)
            SAA: SAUSA300_0758(tpiA)
            SAO: SAOUHSC_00797
            SAJ: SaurJH9_0799
            SAH: SaurJH1_0815
            SEP: SE0559
            SER: SERP0444(tpiA)
            SHA: SH2111(tpiA)
            SSP: SSP1914
            LMO: lmo0346 lmo2457(tpi)
            LMF: LMOf2365_0366(tpiA-1) LMOf2365_2430(tpiA-2)
            LIN: lin0364 lin2551(tpi)
            LWE: lwe0302 lwe2405(tpi)
            LLA: L0006(tpiA)
            LLC: LACR_1244
            LLM: llmg_1424(tpiA)
            SPY: SPy_0613(tpiA)
            SPZ: M5005_Spy_0509(tpiA)
            SPM: spyM18_0680(tpiA)
            SPG: SpyM3_0433(tpi)
            SPS: SPs1422
            SPH: MGAS10270_Spy0503(tpi)
            SPI: MGAS10750_Spy0528(tpi)
            SPJ: MGAS2096_Spy0521(tpi)
            SPK: MGAS9429_Spy0499(tpi)
            SPF: SpyM51354(tpi)
            SPA: M6_Spy0530(tpiA)
            SPB: M28_Spy0488(tpiA)
            SPN: SP_1574
            SPR: spr1432(tpi)
            SPD: SPD_1404(tpiA)
            SAG: SAG0763(tpiA)
            SAN: gbs0783
            SAK: SAK_0888(tpiA)
            SMU: SMU.715
            STC: str0488(tpi)
            STL: stu0488(tpi)
            SSA: SSA_0859(tpi)
            SGO: SGO_0762(tpiA)
            LPL: lp_0791(tpiA)
            LJO: LJ0874
            LAC: LBA0700
            LSA: LSA0606(tpi)
            LSL: LSL_1164(tpiA)
            LDB: Ldb0637(tpi)
            LBU: LBUL_0569
            LBR: LVIS_0663
            LCA: LSEI_0969
            LRE: Lreu_0171 Lreu_0237
            EFA: EF1962(tpiA)
            OOE: OEOE_1652
            STH: STH244
            CAC: CAC0711(tpi)
            CPE: CPE1302(tpiA)
            CPF: CPF_1509(tpiA)
            CPR: CPR_1299(tpiA)
            CTC: CTC00380
            CNO: NT01CX_1412(tpiA)
            CTH: Cthe_0139
            CDF: CD3172(tpi)
            CBO: CBO0228(tpi)
            CBA: CLB_0269(tpiA)
            CBH: CLC_0284(tpiA)
            CBF: CLI_0293(tpiA)
            CBE: Cbei_0599
            AMT: Amet_3578
            CHY: CHY_0282(tpiA)
            DSY: DSY4840
            DRM: Dred_0134 Dred_2989
            SWO: Swol_0274
            CSC: Csac_1952
            TTE: TTE1760(tpiA)
            MTA: Moth_0264
            MGE: MG_431(tpiA)
            MPN: MPN629(tim)
            MPU: MYPU_4580(tim)
            MPE: MYPE3730(tpiA)
            MGA: MGA_0357(tpiA)
            MMY: MSC_0823(tpi)
            MMO: MMOB4190(tpiA)
            MHY: mhp277(tpiA)
            MHJ: MHJ_0099(tpiA)
            MHP: MHP7448_0102(tpiA)
            MSY: MS53_0486(tpiA)
            MCP: MCAP_0750(tpiA)
            UUR: UU181(tpiA)
            POY: PAM170(tpiA)
            AYW: AYWB_549(tpiA)
            MFL: Mfl504
            MTU: Rv1438(tpi)
            MTC: MT1482(tpi)
            MBO: Mb1473(tpi)
            MBB: BCG_1499(tpi)
            MLE: ML0572(tpi)
            MPA: MAP1166(tpi)
            MAV: MAV_3339(tpiA)
            MSM: MSMEG_3086(tpiA) MSMEG_6785(tpiA)
            MVA: Mvan_2705
            MGI: Mflv_3708
            MMC: Mmcs_2406
            MKM: Mkms_2452
            MJL: Mjls_2446
            CGL: NCgl1524(cgl1586)
            CGB: cg1789(tpi)
            CEF: CE1704
            CDI: DIP1308(tpiA)
            CJK: jk0999(tpi)
            NFA: nfa35870(tpi)
            RHA: RHA1_ro07179(tpiA)
            SCO: SCO1945(SCC54.05c)
            SMA: SAV6298(tpiA)
            TWH: TWT302(tpi)
            TWS: TW470(tpiA)
            LXX: Lxx11540(tpiA)
            CMI: CMM_0786(tpiB)
            ART: Arth_0889 Arth_2089
            AAU: AAur_2090(tpiA)
            PAC: PPA0818
            NCA: Noca_2532
            TFU: Tfu_2015
            FRA: Francci3_1639
            FAL: FRAAL4586(tpiA)
            ACE: Acel_1115
            KRA: Krad_1917 Krad_2929
            SEN: SACE_2145(tpiA)
            STP: Strop_3096
            BLO: BL0708(tpi)
            BAD: BAD_0834(tpi)
            RXY: Rxyl_2003
            FNU: FN1366
            RBA: RB7095(tpiA)
            CTR: CT328(tpiS)
            CTA: CTA_0355(tpiS)
            CMU: TC0604
            CPN: CPn1063(tpiS)
            CPA: CP0786
            CPJ: CPj1063(tpiS)
            CPT: CpB1106
            CCA: CCA00308(tpiA)
            CAB: CAB305(tpiA)
            CFE: CF0695(tpiS)
            PCU: pc0801(tpiA)
            BBU: BB0055(tpiA)
            BGA: BG0054
            BAF: BAPKO_0055
            TPA: TP0537
            TDE: TDE1236(tpiA)
            LIL: LA1696(tpiA)
            LIC: LIC12094(tpiA)
            LBJ: LBJ_1218(tpiA)
            LBL: LBL_1269(tpiA)
            SYN: slr0783(tpiA)
            SYW: SYNW0823(tpiA)
            SYC: syc0290_d(tpi)
            SYF: Synpcc7942_1261
            SYD: Syncc9605_1825
            SYE: Syncc9902_0830
            SYG: sync_1210(tpiA)
            SYR: SynRCC307_0974(tpiA)
            SYX: SynWH7803_1435(tpiA)
            CYA: CYA_0398(tpiA)
            CYB: CYB_2157(tpiA)
            TEL: tlr0966(tpi)
            GVI: gll1040(tpi)
            ANA: alr4385
            AVA: Ava_3290
            PMA: Pro0901(tpi)
            PMM: PMM0829(tpi)
            PMT: PMT0817(tpi)
            PMN: PMN2A_0382
            PMI: PMT9312_0971
            PMB: A9601_10411(tpi)
            PMC: P9515_09041(tpi)
            PMF: P9303_13911(tpi)
            PMG: P9301_10411(tpi)
            PMH: P9215_10731(tpi)
            PME: NATL1_10641(tpi)
            TER: Tery_1380
            BTH: BT_3929
            BFR: BF3956
            BFS: BF3729(tpiA)
            PGI: PG0623(tpiA)
            SRU: SRU_1905(tpiA)
            CHU: CHU_3277(tpiA)
            GFO: GFO_0432(tpiA)
            FJO: Fjoh_3504
            FPS: FP1429(tpiA)
            CTE: CT1444(tpiA)
            CCH: Cag_0497
            CPH: Cpha266_1852
            PVI: Cvib_1275
            PLT: Plut_1464
            DET: DET0742(tpiA)
            DEH: cbdb_A717(tpiA)
            DEB: DehaBAV1_0672
            RRS: RoseRS_3813
            RCA: Rcas_0991
            DRA: DR_1339
            DGE: Dgeo_1135
            TTH: TTC0581
            TTJ: TTHA0947
            AAE: aq_360(timA)
            TMA: TM0689
            TPT: Tpet_0241
            TME: Tmel_1264
            FNO: Fnod_0738
            MMP: MMP0687(tpiA)
            MMQ: MmarC5_0889
            MMZ: MmarC7_1711
            MAE: Maeo_0315
            MVN: Mevan_1505
            MAC: MA4607(tpi)
            MBA: Mbar_A0934
            MMA: MM_1278
            MBU: Mbur_1995
            MTP: Mthe_0041
            MHU: Mhun_1027
            MEM: Memar_1292
            MST: Msp_1382(tpiA)
            MSI: Msm_0919
            MKA: MK1664(tpiA)
            HAL: VNG1027G(tpiA)
            HMA: rrnAC0537(tpiA)
            HWA: HQ3360A(tpiA)
            NPH: NP2182A(tpiA_1) NP3716A(tpiA_2)
            TAC: Ta0313
            TVO: TVN1287
            PTO: PTO0348
            PAB: PAB1208(tpiA)
            PFU: PF1920
            TKO: TK2129
            RCI: RCIX770(tpi)
            APE: APE_1538.1
            SMR: Smar_0901
            HBU: Hbut_0946
            SSO: SSO2592(tpiA)
            STO: ST2030
            SAI: Saci_0117(tpiA)
            MSE: Msed_1451
            PAI: PAE1501(tpiA)
            TPE: Tpen_0880
STRUCTURES  PDB: 1AG1  1AMK  1AW1  1AW2  1B9B  1BTM  1CI1  1DKW  1HG3  1HTI  
                 1I45  1IF2  1IIG  1IIH  1KV5  1LYX  1LZO  1M6J  1M7O  1M7P  
                 1ML1  1MO0  1MSS  1N55  1NEY  1NF0  1O5X  1QDS  1R2R  1R2S  
                 1R2T  1SPQ  1SQ7  1SSD  1SSG  1SU5  1SUX  1SW0  1SW3  1SW7  
                 1TCD  1TIM  1TMH  1TPB  1TPC  1TPD  1TPE  1TPF  1TPH  1TPU  
                 1TPV  1TPW  1TRD  1TRE  1TRI  1TSI  1TTI  1TTJ  1VGA  1W0M  
                 1WOA  1WOB  1WYI  1YDV  1YPI  1YYA  2BTM  2DP3  2H6R  2I9E  
                 2IAM  2IAN  2J24  2J27  2V5L  2YPI  3TIM  3YPI  4TIM  5TIM  
                 6TIM  7TIM  8TIM  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.1
            ExPASy - ENZYME nomenclature database: 5.3.1.1
            ExplorEnz - The Enzyme Database: 5.3.1.1
            ERGO genome analysis and discovery system: 5.3.1.1
            BRENDA, the Enzyme Database: 5.3.1.1
            CAS: 9023-78-3
///
ENTRY       EC 5.3.1.2        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
COMMENT     Deleted entry: erythrose isomerase (EC 5.3.1.2 created 1961, deleted
            1976)
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.2
            ExPASy - ENZYME nomenclature database: 5.3.1.2
            ExplorEnz - The Enzyme Database: 5.3.1.2
            ERGO genome analysis and discovery system: 5.3.1.2
            BRENDA, the Enzyme Database: 5.3.1.2
///
ENTRY       EC 5.3.1.3                  Enzyme
NAME        arabinose isomerase;
            D-arabinose(L-fucose) isomerase;
            D-arabinose isomerase;
            L-fucose isomerase;
            D-arabinose ketol-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     D-arabinose aldose-ketose-isomerase
REACTION    D-arabinose = D-ribulose [RN:R01577]
ALL_REAC    R01577
SUBSTRATE   D-arabinose [CPD:C00216]
PRODUCT     D-ribulose [CPD:C00309]
COMMENT     Also acts on L-fucose and, more slowly, on L-galactose and
            D-altrose.
REFERENCE   1
  AUTHORS   Cohen, S.S.
  TITLE     Studies on D-ribulose and its enzymatic conversion to D-arabinose.
  JOURNAL   J. Biol. Chem. 201 (1953) 71-84.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Green, M. and Cohen, S.S.
  TITLE     Enzymatic conversion of L-fucose to L-fuculose.
  JOURNAL   J. Biol. Chem. 219 (1956) 557-568.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K06040  arabinose isomerase
STRUCTURES  PDB: 1FUI  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.3
            ExPASy - ENZYME nomenclature database: 5.3.1.3
            ExplorEnz - The Enzyme Database: 5.3.1.3
            ERGO genome analysis and discovery system: 5.3.1.3
            BRENDA, the Enzyme Database: 5.3.1.3
            CAS: 9023-81-8
///
ENTRY       EC 5.3.1.4                  Enzyme
NAME        L-arabinose isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     L-arabinose aldose-ketose-isomerase
REACTION    L-arabinose = L-ribulose [RN:R01761]
ALL_REAC    R01761
SUBSTRATE   L-arabinose [CPD:C00259]
PRODUCT     L-ribulose [CPD:C00508]
REFERENCE   1  [PMID:13539034]
  AUTHORS   HEATH EC, HORECKER BL, SMYRNIOTIS PZ, TAKAGI Y.
  TITLE     Pentose fermentation by Lactobacillus plantarum. II. L-arabinose
            isomerase.
  JOURNAL   J. Biol. Chem. 231 (1958) 1031-7.
  ORGANISM  Lactobacillus plantarum [GN:lpl]
REFERENCE   2  [PMID:5773448]
  AUTHORS   Nakamatu T, Yamanaka K.
  TITLE     Crystallization and properties of L-arabinose isomerase from
            Lactobacillus gayonii.
  JOURNAL   Biochim. Biophys. Acta. 178 (1969) 156-65.
  ORGANISM  Lactobacillus gayonii
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K01804  L-arabinose isomerase
GENES       CAL: CaO19.3526
            ECO: b0062(araA)
            ECJ: JW0061(araA)
            ECE: Z0070(araA)
            ECS: ECs0066
            ECC: c0074(araA)
            ECI: UTI89_C0067(araA)
            ECP: ECP_0063
            ECV: APECO1_1922(araA)
            ECW: EcE24377A_0064(araA)
            ECX: EcHS_A0066
            STY: STY0119(araA)
            STT: t0106(araA)
            SPT: SPA0104(araA)
            SEC: SC0096(araA)
            STM: STM0102(araA)
            YPE: YPO2253(araA)
            YPK: y2094(araA)
            YPM: YP_2049(araA)
            YPA: YPA_1613
            YPN: YPN_1722
            YPP: YPDSF_0881
            YPS: YPTB2172(araA)
            YPI: YpsIP31758_1887(araA)
            SFX: S0059(araA)
            SFV: SFV_0054(araA)
            SSN: SSON_0068(araA)
            SBO: SBO_0049(araA)
            SDY: SDY_0089(araA)
            ECA: ECA2275(araA)
            ENT: Ent638_0609
            SPE: Spro_2243
            MSU: MS0058(araA)
            ASU: Asuc_0494
            VPA: VPA1676
            SPC: Sputcn32_2066
            SHE: Shewmr4_1979
            SHM: Shewmr7_1995
            SHN: Shewana3_2066
            SHW: Sputw3181_1946
            SDE: Sde_0774
            AHA: AHA_1900(araA)
            RLE: RL0632(araA)
            JAN: Jann_3096
            ABA: Acid345_0326
            BSU: BG11904(araA)
            BHA: BH1873(araA)
            BLI: BL00352(araA) BL01182(araAA)
            BLD: BLi02064 BLi03028(araA)
            BCL: ABC0408(araA)
            BAY: RBAM_025860
            BPU: BPUM_2327
            OIH: OB2797
            GKA: GK1904(araA)
            LPL: lp_3554(araA)
            LSA: LSA1856(araA)
            LBR: LVIS_1740
            LRE: Lreu_0482
            CAC: CAC1342(araA) CAC1346(araA)
            CBE: Cbei_4457
            MSM: MSMEG_1715(araA)
            RHA: RHA1_ro04091
            CMI: CMM_0878(araA)
            ART: Arth_0224
            AAU: AAur_3711(araA)
            NCA: Noca_0382
            ACE: Acel_0873
            BLO: BL0272(araA)
            BAD: BAD_1410(araA)
            BTH: BT_0351
            GFO: GFO_0699(araA)
            FJO: Fjoh_1121
            TMA: TM0276
            TPT: Tpet_0648
STRUCTURES  PDB: 2AJT  2HXG  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.4
            ExPASy - ENZYME nomenclature database: 5.3.1.4
            ExplorEnz - The Enzyme Database: 5.3.1.4
            ERGO genome analysis and discovery system: 5.3.1.4
            BRENDA, the Enzyme Database: 5.3.1.4
            CAS: 9023-80-7
///
ENTRY       EC 5.3.1.5                  Enzyme
NAME        xylose isomerase;
            D-xylose isomerase;
            D-xylose ketoisomerase;
            D-xylose ketol-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     D-xylose aldose-ketose-isomerase
REACTION    D-xylose = D-xylulose [RN:R01432]
ALL_REAC    R01432;
            (other) R00307 R00878
SUBSTRATE   D-xylose [CPD:C00181]
PRODUCT     D-xylulose [CPD:C00310]
COMMENT     Some enzymes also convert D-glucose to D-fructose.
REFERENCE   1  [PMID:13125579]
  AUTHORS   HOCHSTER RM, WATSON RW.
  TITLE     Enzymatic isomerization of D-xylose to D-xylulose.
  JOURNAL   Arch. Biochem. Biophys. 48 (1954) 120-9.
  ORGANISM  Pseudomonas hydrophila
REFERENCE   2
  AUTHORS   Slein, M.W.
  TITLE     Xylose isomerase from Pasteurella pestis, strain A-1122.
  JOURNAL   J. Am. Chem. Soc. 77 (1955) 1663-1667.
  ORGANISM  Pasteurella pestis
REFERENCE   3  [PMID:5646045]
  AUTHORS   Yamanaka K.
  TITLE     Purification, crystallization and properties of the D-xylose
            isomerase from Lactobacillus brevis.
  JOURNAL   Biochim. Biophys. Acta. 151 (1968) 670-80.
  ORGANISM  Lactobacillus brevis [GN:lbr]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
            PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K01805  xylose isomerase
GENES       SPU: 590215(LOC590215)
            DME: Dmel_CG8536(beta4GalNAcTA)
            ECO: b3565(xylA)
            ECJ: JW3537(xylA)
            ECE: Z4990(xylA)
            ECS: ECs4448
            ECC: c4385(xylA)
            ECI: UTI89_C4106(xylA)
            ECP: ECP_3668
            ECV: APECO1_2884(xylA)
            ECW: EcE24377A_4061(xylA)
            ECX: EcHS_A3768(xylA)
            STY: STY4137(xylA)
            STT: t3858(xylA)
            SPT: SPA3512(xylA)
            SEC: SC3596(xylA)
            STM: STM3661(xylA)
            YPE: YPO4038(xylA)
            YPK: y4057(xylA)
            YPM: YP_3400(xylA)
            YPA: YPA_4128
            YPN: YPN_3685
            YPP: YPDSF_3780
            YPS: YPTB3891(xylA)
            YPI: YpsIP31758_4102(xylA)
            SSN: SSON_3820(xylA)
            SBO: SBO_3573(xylA)
            ECA: ECA0097(xylA) ECA1953
            PLU: plu2275(xylA)
            ENT: Ent638_0156
            SPE: Spro_0098
            HIT: NTHI1276(xylA)
            HIP: CGSHiEE_06495
            HIQ: CGSHiGG_09220
            HSO: HS_0587(xylA)
            MSU: MS2373(xylA)
            APL: APL_1908(xylA)
            ASU: Asuc_0500
            XCC: XCC1758(xylA) XCC4100(xylA)
            XCB: XC_2477 XC_4191
            XCV: XCV1808 XCV4330(xylA)
            XAC: XAC1776(xylA) XAC4225(xylA)
            XOO: XOO2910(xylA) XOO4417(xylA)
            XOM: XOO_2761(XOO2761) XOO_4160(XOO4160)
            PPR: PBPRA0457
            PST: PSPTO_3002(xylA)
            PSB: Psyr_2883
            PSP: PSPPH_2356(xylA)
            PFO: Pfl_2303
            PAT: Patl_3726
            SDE: Sde_2504
            CBD: COXBU7E912_1733(xylA)
            MMW: Mmwyl1_1876
            BXE: Bxe_B2622
            BVI: Bcep1808_6451
            BCN: Bcen_6506
            BCH: Bcen2424_6740
            BAM: Bamb_6332
            BTE: BTH_I2338(xylA)
            MLO: mll4975 mlr5036 mlr5709
            MES: Meso_2820
            SME: SMc03163(xylA)
            SMD: Smed_2789
            ATU: Atu4483(xylA)
            ATC: AGR_L_774
            RET: RHE_CH03648(xylA)
            RLE: RL3588 RL4176(xylA)
            BME: BMEI1387
            BMF: BAB1_0570
            BMS: BR0547(xylA)
            BMB: BruAb1_0569(xylA)
            BOV: BOV_0549(xylA)
            OAN: Oant_3411
            BJA: blr1120(xylA)
            BRA: BRADO2360(xylA)
            BBT: BBta_2714(xylA)
            SIL: SPO0856(xylA)
            SIT: TM1040_0029
            RSP: RSP_1176(xylA)
            RSH: Rsph17029_2838
            RSQ: Rsph17025_2615
            JAN: Jann_2108
            RDE: RD1_3705(xylA) RD1_3765(xylA)
            NAR: Saro_0757
            ABA: Acid345_0903
            SUS: Acid_3042
            BSU: BG10806(xylA)
            BHA: BH2757(xylA)
            BCA: BCE_2210(xylA)
            BLI: BL03867(xylA)
            BLD: BLi04048
            BCL: ABC0572(xylA)
            BAY: RBAM_017350(xylA)
            BPU: BPUM_1829(xylA)
            OIH: OB3119
            GKA: GK1875
            GTN: GTNG_1757(xylA)
            LWE: lwe0243(xylA) lwe0277
            LLA: L0230(xylA)
            LLC: LACR_1596
            LLM: llmg_1002(xylA)
            LBR: LVIS_0183
            EFA: EF0556(xylA)
            CDF: CD3064(xylA)
            CBE: Cbei_2383
            AMT: Amet_3796
            MSM: MSMEG_6021(xylA)
            MVA: Mvan_5294
            RHA: RHA1_ro04090
            SCO: SCO1169(2SCG11.03c)
            SMA: SAV7182(xylA)
            LXX: Lxx03370(xylA)
            CMI: CMM_0882(xylA)
            ART: Arth_2430
            AAU: AAur_3706(xylA)
            NCA: Noca_2375
            TFU: Tfu_1603
            ACE: Acel_2064
            STP: Strop_3592
            BLO: BL1704(xylA)
            BAD: BAD_0422(xylA)
            RXY: Rxyl_0401
            RBA: RB2658(xylA)
            BTH: BT_0793
            BFR: BF2262
            BFS: BF2356
            SRU: SRU_0980
            FJO: Fjoh_2001
            RRS: RoseRS_2884
            RCA: Rcas_2618
            DGE: Dgeo_2692
            TMA: TM1071 TM1667
            TPT: Tpet_1124
STRUCTURES  PDB: 1A0C  1A0D  1A0E  1BHW  1BXB  1BXC  1CLK  1DID  1DIE  1DXI  
                 1GW9  1MNZ  1MUW  1O1H  1OAD  1QT1  1S5M  1S5N  1XIA  1XIB  
                 1XIC  1XID  1XIE  1XIF  1XIG  1XIH  1XII  1XIJ  1XIM  1XIN  
                 1XIS  1XLA  1XLB  1XLC  1XLD  1XLE  1XLF  1XLG  1XLH  1XLI  
                 1XLJ  1XLK  1XLL  1XLM  1XYA  1XYB  1XYC  1XYL  1XYM  2G4J  
                 2GLK  2GUB  2GVE  2GYI  2XIM  2XIN  2XIS  3XIM  3XIN  3XIS  
                 4XIA  4XIM  4XIS  5XIA  5XIM  5XIN  6XIA  6XIM  7XIM  8XIA  
                 8XIM  9XIA  9XIM  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.5
            ExPASy - ENZYME nomenclature database: 5.3.1.5
            ExplorEnz - The Enzyme Database: 5.3.1.5
            ERGO genome analysis and discovery system: 5.3.1.5
            BRENDA, the Enzyme Database: 5.3.1.5
            CAS: 9023-82-9
///
ENTRY       EC 5.3.1.6                  Enzyme
NAME        ribose-5-phosphate isomerase;
            phosphopentosisomerase;
            phosphoriboisomerase;
            ribose phosphate isomerase;
            5-phosphoribose isomerase;
            D-ribose 5-phosphate isomerase;
            D-ribose-5-phosphate ketol-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     D-ribose-5-phosphate aldose-ketose-isomerase
REACTION    D-ribose 5-phosphate = D-ribulose 5-phosphate [RN:R01056]
ALL_REAC    R01056
SUBSTRATE   D-ribose 5-phosphate [CPD:C00117]
PRODUCT     D-ribulose 5-phosphate [CPD:C00199]
COMMENT     Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate.
REFERENCE   1  [PMID:13373810]
  AUTHORS   DICKENS F, WILLIAMSON DH.
  TITLE     Pentose phosphate isomerase and epimerase from animal tissues.
  JOURNAL   Biochem. J. 64 (1956) 567-78.
  ORGANISM  horse, rabbit, mouse [GN:mmu]
REFERENCE   2  [PMID:14907726]
  AUTHORS   HORECKER BL, SMYRNIOTIS PZ, SEEGMILLER JE.
  TITLE     The enzymatic conversion of 6-phosphogluconate to
            ribulose-5-phosphate and ribose-5-phosphate.
  JOURNAL   J. Biol. Chem. 193 (1951) 383-96.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:13295229]
  AUTHORS   HURWITZ J, WEISSBACH A, HORECKER BL, SMYRNIOTIS PZ.
  TITLE     Spinach phosphoribulokinase.
  JOURNAL   J. Biol. Chem. 218 (1956) 769-83.
  ORGANISM  spinach
PATHWAY     PATH: map00030  Pentose phosphate pathway
            PATH: map00710  Carbon fixation
ORTHOLOGY   KO: K01806  ribose 5-phosphate isomerase
            KO: K01807  ribose 5-phosphate isomerase A
            KO: K01808  ribose 5-phosphate isomerase B
GENES       HSA: 22934(RPIA)
            MMU: 19895(Rpia)
            CFA: 475755(RPIA)
            GGA: 422931(RCJMB04_30l19)
            XLA: 414499(MGC83218)
            SPU: 575803(LOC575803)
            CEL: B0280.3
            ATH: AT1G71100(RSW10) AT2G01290 AT3G04790
            OSA: 4335430 4342543
            CME: CMO291C
            OLU: OSTLU_12567
            SCE: YOR095C(RKI1)
            AGO: AGOS_ACL077C
            PIC: PICST_57049(RPI1) PICST_76151(RKI1)
            CGR: CAGL0L03740g
            SPO: SPAC144.12
            ANI: AN2440.2 AN5907.2
            AFM: AFUA_6G10610
            AOR: AO090023000209 AO090026000544
            CNE: CNA08060 CND05060
            UMA: UM03103.1 UM04159.1
            ECU: ECU10_0180
            DDI: DDB_0231225(rpiA)
            PFA: PFE0730c
            TAN: TA18725
            TPV: TP03_0628
            TET: TTHERM_00411870
            TBR: Tb11.01.0700
            TCR: 508601.119 509199.24
            LMA: LmjF28.1970
            EHI: 156.t00004
            ECO: b2914(rpiA) b4090(rpiB)
            ECJ: JW4051(rpiB) JW5475(rpiA)
            ECE: Z4252(rpiA)
            ECS: ECs3785
            ECC: c3495(rpiA) c5096(rpiB)
            ECI: UTI89_C3300(rpiA) UTI89_C4685(rpiB)
            ECP: ECP_2906 ECP_4333
            ECV: APECO1_2360(rpiB) APECO1_3615(rpiA)
            ECW: EcE24377A_3241(rpiA)
            ECX: EcHS_A3072(rpiA)
            STY: STY3219(rpiA)
            STT: t2981(rpiA)
            SPT: SPA2934(rpiA)
            SEC: SC3004(rpiA)
            STM: STM3063(rpiA)
            YPE: YPO0915(rpiA) YPO1292(rpiA) YPO3353(rpiB)
            YPK: y0837(rpiB) y2892 y3302(rpiA)
            YPM: YP_0334(rpiB1) YP_1299(rpiA1) YP_3612(rpiA2)
            YPA: YPA_0352 YPA_1010 YPA_2791
            YPN: YPN_0741 YPN_2686 YPN_3114
            YPP: YPDSF_0598 YPDSF_2404
            YPS: YPTB0779(rpiB) YPTB1324(rpiA) YPTB3190(rpiA)
            YPI: YpsIP31758_0855(rpiA2) YpsIP31758_2690(rpiA1)
                 YpsIP31758_3289(rpiB)
            SFL: SF2899(rpiA)
            SFX: S3099(rpiA)
            SFV: SFV_2961(rpiA)
            SSN: SSON_3066(rpiA) SSON_4266(rpiB)
            SBO: SBO_3079(rpiA) SBO_4116(rpiB)
            SDY: SDY_3168(rpiA)
            ECA: ECA0863(rpiB) ECA3906(rpiA)
            PLU: plu3606(rpiA)
            BUC: BU411(rpiA)
            BAS: BUsg397(rpiA)
            BAB: bbp371(rpiA)
            BCC: BCc_259(rpiA)
            WBR: WGLp502(rpiA)
            SGL: SG2010
            ENT: Ent638_3333
            KPN: KPN_03349(rpiA)
            SPE: Spro_3924
            BFL: Bfl256(rpiA)
            BPN: BPEN_263(rpiA)
            HIN: HI0464(rpiA)
            HIT: NTHI0595(rpiA)
            HIP: CGSHiEE_00670
            HIQ: CGSHiGG_05560
            HDU: HD0199(rpiA)
            HSO: HS_0123(rpiA)
            PMU: PM1645(rpiA_1) PM1670(rpiA_2)
            MSU: MS0383(rpiB) MS1744(rpiA)
            APL: APL_1453(rpiA)
            ASU: Asuc_1870
            XFA: XF2015
            XFT: PD0797(rpiA)
            XCC: XCC0153 XCC3265(rpiA)
            XCB: XC_0162 XC_0899
            XCV: XCV0154(rpiB) XCV3528(rpiA)
            XAC: XAC0170 XAC3411(rpiA)
            XOO: XOO0264 XOO1127(rpiA)
            XOM: XOO_0240(XOO0240) XOO_1023(XOO1023)
            VCH: VC2480
            VCO: VC0395_A2056(rpiA)
            VVU: VV1_1547
            VVY: VV2850
            VPA: VP2592
            VFI: VF2105
            PPR: PBPRA3122
            PAE: PA0330(rpiA)
            PAU: PA14_04310(rpiA)
            PAP: PSPA7_0422(rpiA)
            PPU: PP_5150(rpiA)
            PPF: Pput_5057
            PST: PSPTO_5289(rpiA)
            PSB: Psyr_2572 Psyr_4847
            PSP: PSPPH_4880(rpiA)
            PFL: PFL_5906(rpiA)
            PFO: Pfl_5382
            PEN: PSEEN5243(rpiA)
            PMY: Pmen_4223
            PAR: Psyc_0956(rpiA)
            PCR: Pcryo_1462
            PRW: PsycPRwf_0779
            ACI: ACIAD1358(rpiA)
            SON: SO_1150(rpiA)
            SDN: Sden_1092
            SFR: Sfri_0848
            SAZ: Sama_2736
            SBL: Sbal_3293
            SBM: Shew185_3389
            SLO: Shew_0825
            SPC: Sputcn32_2931
            SSE: Ssed_0898
            SPL: Spea_0816
            SHE: Shewmr4_0974
            SHM: Shewmr7_1012
            SHN: Shewana3_0978
            SHW: Sputw3181_1013
            ILO: IL2103(rpiA)
            CPS: CPS_1545(rpiA)
            PHA: PSHAa0667(rpiA)
            PAT: Patl_3508
            SDE: Sde_0612 Sde_3387
            PIN: Ping_0601
            MAQ: Maqu_3437
            CBU: CBU_0026(rpiA)
            CBD: COXBU7E912_0147(rpiA)
            LPN: lpg0094(rpiA)
            LPF: lpl0093
            LPP: lpp0108
            MCA: MCA0043(rpiB) MCA0355(rpiA)
            FTU: FTT1208(rpiA)
            FTF: FTF1208(rpiA)
            FTW: FTW_1255(rpiA)
            FTL: FTL_0736
            FTH: FTH_0738(rpiA)
            FTA: FTA_0777(rpiA)
            FTN: FTN_1185(rpiA)
            TCX: Tcr_1568
            NOC: Noc_2667
            AEH: Mlg_0086
            HHA: Hhal_1176
            HCH: HCH_01062(rpiA)
            CSA: Csal_0019 Csal_0757
            ABO: ABO_2606(rpiA)
            MMW: Mmwyl1_4136
            AHA: AHA_2728(rpiA)
            ASA: ASA_1642(rpiA)
            DNO: DNO_0522(rpiA)
            BCI: BCI_0647(rpiA)
            RMA: Rmag_0227
            VOK: COSY_0220(rpiA)
            NME: NMB1511
            NMA: NMA1711(rpiA)
            NMC: NMC1440(rpiA)
            NGO: NGO0970
            CVI: CV_1260(rpiA)
            RSO: RSc1232(rpiA)
            REU: Reut_A2068
            REH: H16_A2345(rpiA)
            RME: Rmet_1521 Rmet_2088
            BMA: BMA1260(rpiA) BMAA1815(rpiB)
            BMV: BMASAVP1_0813(rpiB) BMASAVP1_A1743(rpiA)
            BML: BMA10299_1104(rpiB) BMA10299_A0149(rpiA)
            BMN: BMA10247_1017(rpiA) BMA10247_A2077(rpiB)
            BXE: Bxe_A2538
            BVI: Bcep1808_1513
            BUR: Bcep18194_A4691
            BCN: Bcen_1069
            BCH: Bcen2424_1549
            BAM: Bamb_1450
            BPS: BPSL1871(rpiA) BPSS0254
            BPM: BURPS1710b_1973(rpiA) BURPS1710b_A1791(rpiB)
            BPL: BURPS1106A_1820(rpiA) BURPS1106A_A0359(rpiB)
            BPD: BURPS668_1803(rpiA) BURPS668_A0454(rpiB)
            BTE: BTH_I2516(rpiA)
            PNU: Pnuc_1264
            BPE: BP2339(rpiA)
            BPA: BPP1700(rpiA)
            BBR: BB3408(rpiA)
            RFR: Rfer_2206
            POL: Bpro_1460 Bpro_2857
            PNA: Pnap_2616
            AAV: Aave_2456
            AJS: Ajs_2131
            VEI: Veis_1934
            MPT: Mpe_A2134(cbbI)
            HAR: HEAR1091(rpiA)
            MMS: mma_2308(rpiA)
            NEU: NE1743(cbbI)
            NET: Neut_1829
            NMU: Nmul_A0436
            EBA: ebA1080(rpiA)
            AZO: azo2826(rpiA)
            DAR: Daro_3560
            TBD: Tbd_2364(cbbI)
            MFA: Mfla_0129 Mfla_0962 Mfla_1106
            HPY: HP0574(lacA)
            HPJ: jhp0521(rpi)
            HPA: HPAG1_0553
            HHE: HH1368(rpiB)
            HAC: Hac_1438(rpiB)
            WSU: WS1348(lacA)
            TDN: Tmden_1116
            CJE: Cj0925(rpiB)
            CJR: CJE1003(rpiB)
            CJJ: CJJ81176_0932(rpiB)
            CJU: C8J_0862(rpiB)
            CJD: JJD26997_0889(rpiB)
            CFF: CFF8240_1171(rpiB)
            CCV: CCV52592_1313(rpiB)
            CHA: CHAB381_1042(rpiB)
            CCO: CCC13826_2228(rpiB)
            ABU: Abu_0635(rpiB)
            NIS: NIS_0708(rpiB)
            SUN: SUN_0662(rpiB)
            GSU: GSU1606
            GME: Gmet_1604 Gmet_2621
            PCA: Pcar_1441
            DVU: DVU1580
            DDE: Dde_2120
            LIP: LI0609(rpiB)
            BBA: Bd2009(rpiB)
            DPS: DP2787
            ADE: Adeh_2745
            MXA: MXAN_4767(rpiB) MXAN_5489(rpiA)
            SAT: SYN_02366
            SFU: Sfum_0934 Sfum_1376
            RPR: RP299(lacA)
            RTY: RT0290(rpiB)
            RCO: RC0402(lacA)
            RFE: RF_0486(lacA)
            RBE: RBE_0278(lacA)
            RAK: A1C_02230
            RBO: A1I_06400
            RRI: A1G_02295
            OTS: OTBS_0684(lacA)
            AMA: AM570(rpiB)
            APH: APH_0642(rpiB)
            ERU: Erum4100(rpiB)
            ERW: ERWE_CDS_04260(rpiB)
            ERG: ERGA_CDS_04200(rpiB)
            ECN: Ecaj_0401
            ECH: ECH_0638(rpiB)
            NSE: NSE_0217(rpiB)
            PUB: SAR11_1049(rpiB)
            MLO: mll0526
            MES: Meso_1459
            PLA: Plav_1094
            SME: SMb20371 SMc00152(rpiA) SMc01613(rpiB)
            SMD: Smed_1573
            ATU: Atu1613(rpiA)
            ATC: AGR_C_2972(rpi)
            RET: RHE_CH02380(rpiA) RHE_PF00039(rpiB)
            RLE: RL2547(rpiB) RL2698(rpiA) pRL120210
            BME: BMEI0974 BMEII0424
            BMF: BAB2_0366
            BMS: BR1010(rpiA) BRA0870
            BMB: BruAb1_1015(rpiA) BruAb2_0362
            BOV: BOV_0976(rpiA)
            OAN: Oant_2092
            BJA: blr3755(rpiA)
            BRA: BRADO4714(rpiA)
            BBT: BBta_3483(rpiA)
            RPA: RPA1981(cbbI)
            RPB: RPB_3386
            RPC: RPC_2076
            RPD: RPD_2055
            RPE: RPE_0572 RPE_1987
            NWI: Nwi_1221
            NHA: Nham_1480
            BHE: BH06410(rpiA)
            BQU: BQ06820(rpiA)
            BBK: BARBAKC583_0602(rpiA)
            XAU: Xaut_3221
            CCR: CC_2303
            SIL: SPO1327(rpiA) SPO3180(rpiB)
            SIT: TM1040_1960 TM1040_2314
            RSP: RSP_0359(cbbI)
            RSH: Rsph17029_2003
            RSQ: Rsph17025_0883
            JAN: Jann_3175
            RDE: RD1_1918(rpiA) RD1_3624(rpiB)
            PDE: Pden_3668
            MMR: Mmar10_0972
            HNE: HNE_0706(rpiA)
            ZMO: ZMO1200(rpiA)
            NAR: Saro_2239
            SAL: Sala_0089 Sala_0792
            ELI: ELI_05655
            GOX: GOX1708 GOX2218
            GBE: GbCGDNIH1_0858
            ACR: Acry_1272
            MAG: amb2338
            MGM: Mmc1_0170
            ABA: Acid345_2809
            BSU: BG10942(ywlF)
            BHA: BH3767
            BAN: BA2791(rpiA) BA5560
            BAR: GBAA2791(rpiA) GBAA5560
            BAA: BA_3313
            BAT: BAS2602 BAS5167
            BCE: BC2796 BC5318
            BCA: BCE_2822(rpiA) BCE_5443
            BCZ: BCZK2521(rpiA) BCZK5017(rpi)
            BTK: BT9727_2554(rpiA) BT9727_5000(rpi)
            BTL: BALH_2508 BALH_4818(rpiB)
            BLI: BL03989(ywlF)
            BLD: BLi03937(ywlF)
            BCL: ABC3353 ABC3611 ABC3865
            BPU: BPUM_3337(ywlF)
            OIH: OB2609 OB2699
            GKA: GK3371
            SAU: SA2127(rpi)
            SAV: SAV2336
            SAM: MW2256
            SAR: SAR2422
            SAS: SAS2228
            SAC: SACOL2329(rpiA)
            SAB: SAB2213c
            SAA: SAUSA300_2283(rpiA)
            SAO: SAOUHSC_02612
            SAJ: SaurJH9_2361
            SAH: SaurJH1_2404
            SEP: SE1911
            SER: SERP1924(rpiA)
            SHA: SH0720(rpi) SH0843(lacB)
            SSP: SSP0527 SSP0568
            LMO: lmo0345 lmo0498 lmo0736 lmo0975 lmo2662 lmo2674
            LMF: LMOf2365_0365(rpiB-1) LMOf2365_0527(rpiB-2)
                 LMOf2365_0996(rpiA) LMOf2365_2642(rpiB-3)
                 LMOf2365_2654(rpiB-4)
            LIN: lin0363 lin0498 lin0974 lin2811 lin2821
            LWE: lwe0301(rpiB) lwe0705(rpiB) lwe0958(rpiA) lwe2611(rpiB)
                 lwe2623(rpiB)
            LLA: L0045(rpiA)
            LLC: LACR_1638 LACR_2538
            LLM: llmg_0958(rpiB) llmg_2511(rpiA)
            SPY: SPy_0889(rpiA)
            SPZ: M5005_Spy_0695(rpiA)
            SPM: spyM18_0950(rpiA)
            SPG: SpyM3_0608(rpiA)
            SPS: SPs1245
            SPH: MGAS10270_Spy0753(rpiA)
            SPI: MGAS10750_Spy0787(rpiA)
            SPJ: MGAS2096_Spy0767(rpiA)
            SPK: MGAS9429_Spy0751(rpiA)
            SPF: SpyM51113(rpiA)
            SPA: M6_Spy0712
            SPB: M28_Spy0675(rpiA)
            SPN: SP_0828
            SPR: spr0731(rpiA)
            SPD: SPD_0723(rpiA)
            SAG: SAG1183(rpiA)
            SAN: gbs1256
            SAK: SAK_1270(rpiA)
            SMU: SMU.1234(rpiA)
            STC: str1121(rpiA)
            STL: stu1121(rpiA)
            STE: STER_1078
            SSA: SSA_1261(rpiA)
            SSU: SSU05_1449
            SSV: SSU98_1458
            SGO: SGO_1265(rpiA)
            LPL: lp_0354(rpiA2) lp_0602(rpiA1)
            LJO: LJ0798
            LAC: LBA0588(rpiA) LBA1174
            LSA: LSA1685(rpiA)
            LSL: LSL_1439(rpiA) LSL_1806(rpiA)
            LDB: Ldb0531(rpiA)
            LBU: LBUL_0472
            LBR: LVIS_0574
            LCA: LSEI_2315 LSEI_2675
            LGA: LGAS_0557
            LRE: Lreu_0298
            PPE: PEPE_1506
            EFA: EF0197(rpiA)
            OOE: OEOE_0159 OEOE_1611
            LME: LEUM_0154
            STH: STH2337 STH77
            CAC: CAC0726 CAC1431(rpiA) CAC2880
            CPE: CPE2198
            CPF: CPF_2463(rpiB)
            CPR: CPR_2173
            CTC: CTC00307
            CNO: NT01CX_0543(rpiB)
            CDF: CD2320(rpiB1) CD3480(rpiB2)
            CBO: CBO0144(rpiB)
            CBA: CLB_0180(rpiB)
            CBH: CLC_0192(rpiB)
            CBF: CLI_0199(rpiB)
            CBE: Cbei_0761 Cbei_2367
            CHY: CHY_2558(rpiB)
            DSY: DSY4929
            TTE: TTE0146(rpiB)
            MTA: Moth_2392
            MGE: MG_396(rpiB)
            MPN: MPN595(lacA)
            MPU: MYPU_6120
            MPE: MYPE680
            MGA: MGA_0866(rpiB)
            MMY: MSC_0895(rpiB)
            MMO: MMOB3700(rpiB)
            MHY: mhp594
            MHJ: MHJ_0578(rpiB)
            MHP: MHP7448_0577(rpiB)
            MSY: MS53_0392(rpiB)
            MCP: MCAP_0074
            UUR: UU006(lacA)
            MFL: Mfl105
            MTU: Rv2465c(rpi)
            MTC: MT2540
            MBO: Mb2492c
            MBB: BCG_2485c(rpiB)
            MLE: ML1484
            MPA: MAP2285c(rpi)
            MAV: MAV_1707
            MSM: MSMEG_3272 MSMEG_4684 MSMEG_6787
            MMC: Mmcs_2561 Mmcs_3599
            CGL: NCgl2337(cgl2423)
            CGB: cg2658(rpi)
            CEF: CE2318
            CDI: DIP1796
            CJK: jk0541(rpi)
            NFA: nfa13270
            RHA: RHA1_ro01378 RHA1_ro02899
            SCO: SCO0579(SCF55.03c) SCO1224(2SCG58.24c) SCO2627(SC8E4.02c)
            SMA: SAV1547(rpiB1) SAV5426(rpiB2)
            TWH: TWT397(rpi)
            TWS: TW373(rpiB)
            LXX: Lxx08770(rpiB)
            CMI: CMM_0787(rpiB) CMM_1459(rpiA)
            AAU: AAur_1103(rpiB) AAur_2387(rpiB) AAur_4136(rpiB)
            PAC: PPA1624 PPA2324
            TFU: Tfu_2202
            FRA: Francci3_1162
            FAL: FRAAL1862
            SEN: SACE_1349(rpi) SACE_4764 SACE_5216
            BLO: BL1623
            BAD: BAD_0361
            RXY: Rxyl_0733
            FNU: FN1874
            RBA: RB10817(rpiB) RB5998(rpiB)
            CTR: CT213(rpiA)
            CTA: CTA_0233(rpiA)
            CMU: TC0485
            CPN: CPn0141(rpiA)
            CPA: CP0631
            CPJ: CPj0141(rpiA)
            CPT: CpB0142
            CCA: CCA00632(rpiA)
            CAB: CAB606
            CFE: CF0371(rpiA)
            PCU: pc1175(rpiA)
            BBU: BB0657(rpi)
            BGA: BG0680(rpi)
            BAF: BAPKO_0701(rpi)
            TPA: TP0616
            TDE: TDE0352(rpiB) TDE1641(rpiA)
            LIL: LA0369(rpiB)
            LIC: LIC10317(rpiB)
            LBJ: LBJ_2755(rpiB)
            LBL: LBL_0316(rpiB)
            SYN: slr0194(rpiA) ssl2153(rpiB)
            SYW: SYNW0609(rpiA)
            SYC: syc0939_d(rpiA)
            SYF: Synpcc7942_0584
            SYD: Syncc9605_2071
            SYE: Syncc9902_0601
            SYG: sync_2363(rpiA)
            SYR: SynRCC307_1964(rpiA)
            SYX: SynWH7803_2066(rpiA)
            CYA: CYA_2325(rpiA)
            CYB: CYB_2038(rpiA)
            TEL: tll1273(rpiA)
            GVI: gll0030(rpiA) gll1688
            ANA: all0888
            AVA: Ava_4491
            PMA: Pro1644(rpi)
            PMM: PMM1489(rpiA)
            PMT: PMT1511(rpiA)
            PMN: PMN2A_1020
            PMI: PMT9312_1582
            PMB: A9601_16931(rpiA)
            PMC: P9515_16691(rpiA)
            PMF: P9303_04321(rpiA)
            PMG: P9301_16801(rpiA)
            PMH: P9215_17581(rpiA)
            PME: NATL1_18901(rpiA)
            TER: Tery_2528
            BTH: BT_0346 BT_1986
            BFR: BF1651 BF3677
            BFS: BF1659(rpiB) BF3474
            PGI: PG1747
            SRU: SRU_0511(rpiA)
            CHU: CHU_3631(rpiB)
            FPS: FP2488(rpiB)
            CTE: CT1050(rpiB)
            CCH: Cag_0901
            PLT: Plut_1017
            DET: DET0643 DET0677
            DEH: cbdb_A628(rpiB)
            RRS: RoseRS_2910
            RCA: Rcas_2980
            DRA: DR_0845
            DGE: Dgeo_1265
            TTH: TTC0932
            TTJ: TTHA1299
            AAE: aq_1138(rpiB)
            TMA: TM1080
            MJA: MJ1603
            MMP: MMP1189
            MMQ: MmarC5_0401
            MMZ: MmarC7_0436
            MAE: Maeo_0737
            MVN: Mevan_0505
            MAC: MA1683(rpiA)
            MBA: Mbar_A3172
            MMA: MM_0073
            MBU: Mbur_0773
            MTP: Mthe_0364
            MHU: Mhun_0569
            MEM: Memar_1386
            MBN: Mboo_0918
            MTH: MTH608
            MST: Msp_0995(rpiA)
            MSI: Msm_0284
            MKA: MK1665(rpiA)
            AFU: AF0943(rpi)
            HAL: VNG2272G(rpi)
            HMA: rrnAC2572(rpiA)
            HWA: HQ3679A(rpiA)
            NPH: NP0786A(rpiA)
            TAC: Ta0878
            TVO: TVN0717
            PTO: PTO0565
            PHO: PH1375
            PAB: PAB0522(rpi)
            PFU: PF1258
            TKO: TK1426
            RCI: RCIX1835(rpi)
            APE: APE_0665
            SMR: Smar_0990
            IHO: Igni_0428
            SSO: SSO0978(rpiA)
            STO: ST1302
            SAI: Saci_1301(rpiA)
            MSE: Msed_2287
            PAI: PAE1027
            PIS: Pisl_1200
            PCL: Pcal_0662
            PAS: Pars_0187
            TPE: Tpen_0327
STRUCTURES  PDB: 1LK5  1LK7  1LKZ  1M0S  1NN4  1O1X  1O8B  1UJ4  1UJ5  1UJ6  
                 1USL  1XTZ  2BES  2BET  2F8M  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.6
            ExPASy - ENZYME nomenclature database: 5.3.1.6
            ExplorEnz - The Enzyme Database: 5.3.1.6
            ERGO genome analysis and discovery system: 5.3.1.6
            BRENDA, the Enzyme Database: 5.3.1.6
            CAS: 9023-83-0
///
ENTRY       EC 5.3.1.7                  Enzyme
NAME        mannose isomerase;
            D-mannose isomerase;
            D-mannose ketol-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     D-mannose aldose-ketose-isomerase
REACTION    D-mannose = D-fructose [RN:R00877]
ALL_REAC    R00877
SUBSTRATE   D-mannose [CPD:C00159]
PRODUCT     D-fructose [CPD:C00095]
COMMENT     Also acts on D-lyxose and D-rhamnose.
REFERENCE   1
  AUTHORS   Palleroni, N.J. and Doudoroff, M.
  TITLE     Mannose isomerase of Pseudomonas saccharophila.
  JOURNAL   J. Biol. Chem. 218 (1956) 535-548.
  ORGANISM  Pseudomonas saccharophila
PATHWAY     PATH: map00051  Fructose and mannose metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.7
            ExPASy - ENZYME nomenclature database: 5.3.1.7
            ExplorEnz - The Enzyme Database: 5.3.1.7
            ERGO genome analysis and discovery system: 5.3.1.7
            BRENDA, the Enzyme Database: 5.3.1.7
            CAS: 9031-25-8
///
ENTRY       EC 5.3.1.8                  Enzyme
NAME        mannose-6-phosphate isomerase;
            phosphomannose isomerase;
            phosphohexomutase;
            phosphohexoisomerase;
            mannose phosphate isomerase;
            phosphomannoisomerase;
            D-mannose-6-phosphate ketol-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     D-mannose-6-phosphate aldose-ketose-isomerase
REACTION    D-mannose 6-phosphate = D-fructose 6-phosphate [RN:R00772]
ALL_REAC    R00772 > R01819
SUBSTRATE   D-mannose 6-phosphate [CPD:C00275]
PRODUCT     D-fructose 6-phosphate [CPD:C00085]
COFACTOR    Zinc [CPD:C00038]
COMMENT     A zinc protein.
REFERENCE   1  [PMID:13596383]
  AUTHORS   BRUNS FH, NOLTMANN E, WILLEMSEN A.
  TITLE     [Phosphomannose isomerase. I. Activity measurement and dependence of
            enzyme action on sulfhydryl groups and metals in some animal
            tissues.]
  JOURNAL   Biochem. Z. 330 (1958) 411-20.
REFERENCE   2  [PMID:4969968]
  AUTHORS   Gracy RW, Noltmann EA.
  TITLE     Studies on phosphomannose isomerase. II. Characterization as a zinc
            metalloenzyme.
  JOURNAL   J. Biol. Chem. 243 (1968) 4109-16.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3  [PMID:14794671]
  AUTHORS   SLEIN MW.
  TITLE     Phosphomannose isomerase.
  JOURNAL   J. Biol. Chem. 186 (1950) 753-61.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K01809  mannose-6-phosphate isomerase
GENES       HSA: 4351(MPI)
            PTR: 453748(MPI)
            MMU: 110119(Mpi)
            RNO: 300741(Mpi)
            CFA: 478369(MPI)
            GGA: 769765(MPI)
            SPU: 574815(LOC574815)
            DME: Dmel_CG8417
            CEL: C05C8.7 ZK632.4
            ATH: AT1G67070(DIN9) AT3G02570(MEE31)
            CME: CMQ359C
            SCE: YER003C(PMI40)
            AGO: AGOS_ADR003C
            PIC: PICST_72090(PMI1)
            CGR: CAGL0J02244g
            SPO: SPBC2G2.16
            ANI: AN0667.2 AN1715.2
            AFM: AFUA_1G13280 AFUA_4G08410
            AOR: AO090011000454 AO090012000554 AO090023000719
            CNE: CNI02370
            UMA: UM06167.1
            DDI: DDB_0231659(mpi)
            CPV: cgd8_1920
            TAN: TA11125
            TPV: TP04_0879
            TET: TTHERM_00684730
            TBR: Tb11.01.6410
            TCR: 503677.10 511717.90
            LMA: LmjF32.1580
            EHI: 90.t00031
            ECO: b1613(manA)
            ECJ: JW1605(manA)
            ECE: Z2616(manA)
            ECS: ECs2319
            ECC: c2005(manA)
            ECI: UTI89_C1801(manA)
            ECP: ECP_1557
            ECV: APECO1_696(manA)
            ECW: EcE24377A_1821(manA)
            ECX: EcHS_A1688
            STY: STY1655(manA)
            STT: t1335(manA)
            SPT: SPA1388(manA)
            SEC: SC1484(manA)
            STM: STM1467(manA)
            YPE: YPO2263(manA)
            YPK: y2105(manA)
            YPM: YP_2060(manA)
            YPA: YPA_1623
            YPN: YPN_1735
            YPS: YPTB2185(manA)
            YPI: YpsIP31758_1874(manA)
            YEN: YE4098(manA)
            SFL: SF1636(manA)
            SFX: S1767(manA)
            SFV: SFV_1629(manA)
            SSN: SSON_1547(manA)
            SBO: SBO_1523(manA)
            SDY: SDY_1829(manA)
            ECA: ECA2263(manA)
            PLU: plu2360(manA)
            SGL: SG1461
            ENT: Ent638_1830
            HDU: HD0765(manA)
            HSO: HS_0605(pmi)
            PMU: PM0829(pmi)
            MSU: MS0614(manA)
            APL: APL_1395(manA)
            XFA: XF0259
            XFT: PD0212(xanB)
            XCC: XCC0625(xanB)
            XCB: XC_3609
            XCV: XCV3704(xanB)
            XAC: XAC3580(xanB)
            XOO: XOO0796(xanB)
            XOM: XOO_0724(XOO0724)
            VCH: VC0269 VC1827
            VCO: VC0395_A1422(manA-2) VC0395_A2647(manA-1)
            VVU: VV2_0514 VV2_0515 VV2_1348
            VVY: VVA0187 VVA1064 VVA1390
            VPA: VPA0967 VPA1425
            VFI: VFA0710
            PPR: PBPRA2716
            PPU: PP_4860
            PPF: Pput_4448
            PST: PSPTO_4913
            PSB: Psyr_0603
            PSP: PSPPH_0598 PSPPH_0984
            PFL: PFL_0605
            PFO: Pfl_0559
            PEN: PSEEN3742 PSEEN4546(algA) PSEEN4909
            PMY: Pmen_1020
            ACI: ACIAD0086(epsM)
            SDE: Sde_0505
            FTW: FTW_0453 FTW_1298
            FTA: FTA_0406
            AEH: Mlg_0100
            HCH: HCH_02412
            CSA: Csal_1774
            ABO: ABO_0395(algA)
            AHA: AHA_1434(manA) AHA_2338
            CVI: CV_2312(manA)
            RSO: RSc3058(manA)
            REU: Reut_B4304
            REH: H16_B1152
            RME: Rmet_4175 Rmet_5843
            BMA: BMA0029 BMA2310 BMAA1857
            BML: BMA10299_1649
            BMN: BMA10247_A0304
            BXE: Bxe_A3713 Bxe_B1730 Bxe_B2949
            BUR: Bcep18194_A3856 Bcep18194_B0158 Bcep18194_B2277
            BAM: Bamb_5545
            BPS: BPSL2810(manC) BPSS0218 BPSS1835
            BPM: BURPS1710b_3304 BURPS1710b_A0919 BURPS1710b_A1747
            BTE: BTH_I1324 BTH_II0542 BTH_II2177
            BPE: BP0894(pmi)
            BPA: BPP1621(pmi)
            BBR: BB3107(pmi)
            RFR: Rfer_0711
            HAR: HEAR0728(cpsB)
            NET: Neut_0618
            NMU: Nmul_A0261
            EBA: ebA1533(xanB)
            AZO: azo0951
            DAR: Daro_2389
            TBD: Tbd_1239
            MFA: Mfla_2012
            GSU: GSU2364
            GUR: Gura_3271
            PPD: Ppro_2096
            LIP: LI0984(xanB)
            BBA: Bd2919(manA)
            DPS: DP2458
            SAT: SYN_01359 SYN_03119
            PUB: SAR11_0962(manC)
            SME: SMc03111(pmi)
            SMD: Smed_2871
            ATU: Atu3311
            ATC: AGR_L_3017
            BME: BMEI1394
            BMS: BR0539(manA)
            BMB: BruAb1_0562(manA)
            BJA: bll5968
            BRA: BRADO5152(manC)
            BBT: BBta_5620(manC)
            RPC: RPC_4240
            RPE: RPE_4272 RPE_4279
            XAU: Xaut_3549
            CCR: CC_3617
            RSP: RSP_0834(xanB) RSP_4053(xanB)
            JAN: Jann_4214
            RDE: RD1_B0036(xanB)
            MMR: Mmar10_2432
            ZMO: ZMO1233(pmi)
            SAL: Sala_1593
            GOX: GOX0455 GOX1040
            GBE: GbCGDNIH1_0356
            RRU: Rru_A0924 Rru_B0046
            MAG: amb0037
            MGM: Mmc1_0913
            ABA: Acid345_0569
            BSU: BG10454(pmi) BG12196(ydhS) BG13177(manA)
            BHA: BH3916
            BCY: Bcer98_1171
            BTL: BALH_4763(manA) BALH_4769(manA) BALH_4770(manA)
            BLI: BL00290(manA) BL02466(pmi)
            BLD: BLi02107(manA) BLi03822(pmi)
            BCL: ABC3253(manA)
            BAY: RBAM_024190 RBAM_032910
            BPU: BPUM_3235
            OIH: OB2765
            GKA: GK3304 GK3464
            SAU: SA1945 SA2435(pmi)
            SAV: SAV2143 SAV2642(pmi)
            SAM: MW2067 MW2563(pmi)
            SAR: SAR2231 SAR2721(pmi)
            SAS: SAS2046 SAS2528
            SAC: SACOL2135(manA1) SACOL2664(manA2)
            SAB: SAB2027c SAB2517(pmi)
            SAA: SAUSA300_2096(manA) SAUSA300_2577(manA)
            SAO: SAOUHSC_02385 SAOUHSC_02976
            SAJ: SaurJH9_2179 SaurJH9_2666
            SAH: SaurJH1_2217 SaurJH1_2722
            SEP: SE1743 SE2229
            SER: SERP1752(manA-1) SERP2261(manA-2)
            SHA: SH0891
            SSP: SSP0739
            LMO: lmo2110
            LMF: LMOf2365_2143(manA)
            LIN: lin2215
            LWE: lwe2129(manA)
            LLA: L179409(pmi)
            LLC: LACR_0819
            LLM: llmg_1789(pmi)
            SPY: SPy_1810(pmi)
            SPZ: M5005_Spy_1538(pmi)
            SPM: spyM18_1876(manA)
            SPG: SpyM3_1566(pmi)
            SPS: SPs0301
            SPH: MGAS10270_Spy1605(pmi)
            SPI: MGAS10750_Spy1597(pmi)
            SPJ: MGAS2096_Spy1563(pmi)
            SPK: MGAS9429_Spy1541(pmi)
            SPF: SpyM50311(manA)
            SPA: M6_Spy1528
            SPB: M28_Spy1525(pmi)
            SPN: SP_0736
            SPR: spr0647(pmi)
            SPD: SPD_0641(manA)
            SAG: SAG1688(manA)
            SAN: gbs1732
            SAK: SAK_1700(manA)
            SMU: SMU.1839(manA)
            STC: str1358 str1359 str1732(pmi1)
            STL: stu1358 stu1359 stu1732(pmi1)
            SSA: SSA_0781(pmi)
            SGO: SGO_1749(manA)
            LPL: lp_2384(pmi)
            LJO: LJ0916
            LAC: LBA0745
            LSA: LSA1146(manA)
            LSL: LSL_1613(manA)
            LDB: Ldb0059(pmi)
            LBU: LBUL_0050
            LBR: LVIS_1656
            LCA: LSEI_0292
            LRE: Lreu_1575
            EFA: EF2589(manA)
            OOE: OEOE_0249
            STH: STH1983
            CAC: CAC2918(pmi)
            CPE: CPE1187(manA)
            CPF: CPF_1391(manA)
            CPR: CPR_1205(manA)
            CTC: CTC00339
            CNO: NT01CX_1588(manA)
            CTH: Cthe_3116
            CDF: CD2491(pmi)
            CBO: CBO0412
            CBA: CLB_0437(manA)
            CBH: CLC_0468(manA)
            CBF: CLI_0487(manA)
            CBE: Cbei_0996
            CSC: Csac_1187
            TTE: TTE1751(manA)
            MPU: MYPU_7250(pmi)
            MPE: MYPE7700(pmi)
            MGA: MGA_0514(manA)
            MMY: MSC_0495(pmi)
            MMO: MMOB5280(manA)
            MHY: mhp492(pmi)
            MHJ: MHJ_0491
            MHP: MHP7448_0494
            MCP: MCAP_0475(pmi)
            MTU: Rv3255c(manA)
            MTC: MT3353(manA)
            MBO: Mb3283c(manA)
            MBB: BCG_3284c(manA)
            MLE: ML0765(manA)
            MPA: MAP3367c(manA)
            MAV: MAV_4217(manA)
            MSM: MSMEG_1371 MSMEG_1836(manA)
            MMC: Mmcs_1330
            CGL: NCgl0716(cgl0748)
            CGB: cg0856(manA)
            CEF: CE0764
            CDI: DIP0689
            CJK: jk1640(manA)
            NFA: nfa46270(manA)
            RHA: RHA1_ro05436(manA1) RHA1_ro06318(manA2)
            SCO: SCO3025(manA)
            SMA: SAV5051(manA)
            TWH: TWT122(manA)
            TWS: TW133(manA)
            LXX: Lxx05180(manA)
            CMI: CMM_1027(manA)
            AAU: AAur_1304(manA)
            PAC: PPA0008 PPA0451
            TFU: Tfu_0016
            FRA: Francci3_0748
            FAL: FRAAL1268(manA)
            SEN: SACE_6227(manA) SACE_6457(manA)
            RBA: RB9983(pmi)
            BGA: BG0409(manA)
            BAF: BAPKO_0424(manA)
            LIL: LA0656(manA)
            LIC: LIC12934(manA)
            LBJ: LBJ_0650(manA)
            LBL: LBL_2429(manA)
            SYF: Synpcc7942_1608
            SYG: sync_1052
            CYB: CYB_2283
            ANA: all4538
            AVA: Ava_1405
            TER: Tery_0471
            BTH: BT_0373
            BFR: BF1656
            BFS: BF1664
            PGI: PG0468(manA)
            CHU: CHU_0467(manA)
            GFO: GFO_1692 GFO_2205
            FJO: Fjoh_0266
            FPS: FP1789(manA)
            DEB: DehaBAV1_0485
            RRS: RoseRS_3802
            RCA: Rcas_1081
            DRA: DR_A0032 DR_A0048
            DGE: Dgeo_0321
            TTH: TTC0980 TTC1388
            TTJ: TTHA1345 TTHA1750
            TMA: TM0736
            AFU: AF0035
            MSE: Msed_2078
STRUCTURES  PDB: 1PMI  1QWR  1TZB  1TZC  1X9H  1X9I  2GZ6  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.8
            ExPASy - ENZYME nomenclature database: 5.3.1.8
            ExplorEnz - The Enzyme Database: 5.3.1.8
            ERGO genome analysis and discovery system: 5.3.1.8
            BRENDA, the Enzyme Database: 5.3.1.8
            CAS: 9023-88-5
///
ENTRY       EC 5.3.1.9                  Enzyme
NAME        glucose-6-phosphate isomerase;
            phosphohexose isomerase;
            phosphohexomutase;
            oxoisomerase;
            hexosephosphate isomerase;
            phosphosaccharomutase;
            phosphoglucoisomerase;
            phosphohexoisomerase;
            phosphoglucose isomerase;
            glucose phosphate isomerase;
            hexose phosphate isomerase;
            D-glucose-6-phosphate ketol-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     D-glucose-6-phosphate aldose-ketose-isomerase
REACTION    D-glucose 6-phosphate = D-fructose 6-phosphate [RN:R00771]
ALL_REAC    R00771 > R02740 R03321;
            (other) R02739
SUBSTRATE   D-glucose 6-phosphate [CPD:C00092]
PRODUCT     D-fructose 6-phosphate [CPD:C00085]
COMMENT     Also catalyses the anomerization of D-glucose 6-phosphate.
REFERENCE   1  [PMID:13685918]
  AUTHORS   BAICH A, WOLFE RG, REITHEL FJ.
  TITLE     The enzymes of mammary gland. I. Isolation of phosphoglucose
            isomerase.
  JOURNAL   J. Biol. Chem. 235 (1960) 3130-3.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:14299604]
  AUTHORS   NAKAGAWA Y, NOLTMANN EA.
  TITLE     ISOLATION OF CRYSTALLINE PHOSPHOGLUCOSE ISOMERASE FROM BREWERS'
            YEAST.
  JOURNAL   J. Biol. Chem. 240 (1965) 1877-81.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Noltmann, E. and Bruns, F.H.
  TITLE     Reindarstellung und Eigenschaften von Phosphoglucose-isomerase aus
            Hefe.
  JOURNAL   Biochem. Z. 331 (1959) 436-445.
REFERENCE   4
  AUTHORS   Noltmann, E.A.
  TITLE     Isolation of crystalline phosphoglucose isomerase from rabbit
            muscle.
  JOURNAL   J. Biol. Chem. 239 (1964) 1545-1550.
  ORGANISM  rabbit
REFERENCE   5  [PMID:13314642]
  AUTHORS   RAMASARMA T, GIRI KV.
  TITLE     Phosphoglucose isomerase of green gram (Phaseolus radiatus).
  JOURNAL   Arch. Biochem. Biophys. 62 (1956) 91-6.
  ORGANISM  Phaseolus radiatus
REFERENCE   6
  AUTHORS   Tsuboi, K.K., Estrada, J. and Hudson, P.B.
  TITLE     Enzymes of the human erythrocytes. IV. Phosphoglucose isomerase,
            purification and properties.
  JOURNAL   J. Biol. Chem. 231 (1958) 19-29.
  ORGANISM  human [GN:hsa]
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00030  Pentose phosphate pathway
            PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01810  glucose-6-phosphate isomerase
            KO: K06859  glucose-6-phosphate isomerase
GENES       HSA: 2821(GPI)
            MMU: 14751(Gpi1)
            CFA: 479379(LOC479379) 611942(GPI)
            SSC: 397602(GPI)
            GGA: 415783(GPI)
            XLA: 444192(MGC80718)
            XTR: 496419(gpi)
            DRE: 246094(gpia) 246095(gpib)
            SPU: 759609(LOC759609)
            DME: Dmel_CG8251(Pgi)
            ATH: AT4G24620(PGI1) AT5G42740
            OSA: 4334290 4340677 4347311
            CME: CMO124C CMT497C
            SCE: YBR196C(PGI1)
            AGO: AGOS_AEL249C
            PIC: PICST_84923(PGI1)
            CGR: CAGL0H05445g
            SPO: SPBC1604.05(pgi1)
            ANI: AN6037.2
            AFM: AFUA_2G09790
            AOR: AO090011000659
            CNE: CNB04050
            ECU: ECU05_0650
            DDI: DDB_0231026(G6PI)
            PFA: PF14_0341
            CPV: cgd2_3200
            CHO: Chro.20336
            TAN: TA04045
            TPV: TP03_0346
            TET: TTHERM_01108660 TTHERM_01108680 TTHERM_01108700
            TBR: Tb927.1.3830(PGI)
            TCR: 506529.508 510889.221
            LMA: LmjF12.0530
            EHI: 209.t00010 209.t00016
            ECO: b4025(pgi)
            ECJ: JW3985(pgi)
            ECE: Z5623(pgi)
            ECS: ECs5008
            ECC: c4991(pgi)
            ECI: UTI89_C4593(pgi)
            ECP: ECP_4243
            ECV: APECO1_2443(pgi)
            ECW: EcE24377A_4573(pgi)
            ECX: EcHS_A4264
            STY: STY4417(pgi)
            STT: t4127(pgi)
            SPT: SPA4038(pgi)
            SEC: SC4100(pgi)
            STM: STM2757 STM4221(pgi)
            YPE: YPO3718(pgi)
            YPK: y0024(pgi)
            YPM: YP_3080(pgi)
            YPA: YPA_0026
            YPN: YPN_0023
            YPP: YPDSF_0182
            YPS: YPTB3649(pgi)
            YPI: YpsIP31758_0302(pgi)
            SFL: SF4180(pgi)
            SFX: S3551(pgi)
            SFV: SFV_4188(pgi)
            SSN: SSON_4203(pgi)
            SBO: SBO_4053(pgi)
            SDY: SDY_4226(pgi)
            ECA: ECA3979(pgi)
            PLU: plu4379(pgi)
            BUC: BU573(pgi)
            BAS: BUsg553(pgi)
            BAB: bbp518(pgi)
            BCC: BCc_372(pgi)
            WBR: WGLp598(pgi)
            SGL: SG2146
            ENT: Ent638_0230
            SPE: Spro_4276 Spro_4477
            BFL: Bfl629(pgi)
            BPN: BPEN_656(pgi)
            HIN: HI1576(pgi)
            HIT: NTHI1475(pgi)
            HIP: CGSHiEE_05500(pgi)
            HIQ: CGSHiGG_00035(pgi)
            HDU: HD0418(pgi)
            HSO: HS_0938(pgi)
            PMU: PM0416(pgi)
            MSU: MS1181(pgi)
            APL: APL_1137(pgi)
            ASU: Asuc_1425
            XFA: XF0232
            XFT: PD0190(pgi)
            XCC: XCC1771(pgi)
            XCB: XC_2465
            XCV: XCV1819(pgi)
            XAC: XAC1788(pgi)
            XOO: XOO2360(pgi)
            XOM: XOO_2242(XOO2242)
            VCH: VC0374
            VCO: VC0395_A2785(pgi)
            VVU: VV1_1396
            VVY: VV2975
            VPA: VP2731
            VFI: VF0304
            PPR: PBPRA3328(pgi)
            PAE: PA4732(pgi)
            PAU: PA14_62620(pgi)
            PPU: PP_1808(pgi-1) PP_4701(pgi-2)
            PPF: Pput_4566
            PST: PSPTO_0959(pgi)
            PSB: Psyr_0826
            PSP: PSPPH_0852(pgi)
            PFL: PFL_5280(pgi)
            PFO: Pfl_4813
            PEN: PSEEN4737(pgi)
            PMY: Pmen_3594
            PAR: Psyc_0109(pgi)
            PCR: Pcryo_0118
            PRW: PsycPRwf_0272
            ACI: ACIAD0101(pgi)
            SON: SO_3547(pgi)
            SDN: Sden_2735
            SFR: Sfri_2901
            SAZ: Sama_0912
            SBL: Sbal_1043
            SBM: Shew185_1110
            SLO: Shew_1088
            SPC: Sputcn32_1048
            SSE: Ssed_1184
            SPL: Spea_1073
            SHE: Shewmr4_2968
            SHM: Shewmr7_3050
            SHN: Shewana3_3148
            SHW: Sputw3181_3117
            ILO: IL0570(pgi)
            CPS: CPS_1020(pgi1) CPS_2108(pgi2)
            PHA: PSHAa1139(pgi)
            PAT: Patl_3623
            SDE: Sde_1006
            PIN: Ping_0324
            MAQ: Maqu_0665
            CBU: CBU_0848(pgi)
            CBD: COXBU7E912_0913(pgi)
            LPN: lpg0759(pgi)
            LPF: lpl0796(gpi)
            LPP: lpp0825(gpi)
            MCA: MCA1247(pgi)
            FTU: FTT1315c(pgi)
            FTF: FTF1315c(pgi)
            FTW: FTW_1481(pgi)
            FTL: FTL_1476
            FTH: FTH_1430(pgi)
            FTA: FTA_1561(pgi)
            FTN: FTN_0663(pgi)
            TCX: Tcr_0608
            NOC: Noc_0903
            AEH: Mlg_0290
            HHA: Hhal_2177
            HCH: HCH_06266(pgi)
            CSA: Csal_0932 Csal_2546
            ABO: ABO_0936(pgi)
            MMW: Mmwyl1_4018
            AHA: AHA_0154(pgi) AHA_2345
            DNO: DNO_0163(pgi)
            BCI: BCI_0012(pgi)
            RMA: Rmag_0884
            VOK: COSY_0810(pgi)
            NME: NMB0334 NMB1388
            NMA: NMA1604(pgi1) NMA2154(pgi2)
            NMC: NMC1326(pgi1) NMC1837(pgi2)
            NGO: NGO0719 NGO1668
            CVI: CV_0149(pgi2) CV_2369(pgi1)
            RSO: RSc1719(pgi)
            REU: Reut_A1386 Reut_A1649
            REH: H16_A1502(pgi1) H16_B1502(pgi2)
            RME: Rmet_1879
            BMA: BMA1449(pgi)
            BMV: BMASAVP1_A1942(pgi)
            BML: BMA10299_A3363(pgi)
            BMN: BMA10247_1215(pgi)
            BXE: Bxe_A2287
            BVI: Bcep1808_1849 Bcep1808_3217
            BUR: Bcep18194_A5218
            BCN: Bcen_6162
            BCH: Bcen2424_1917
            BAM: Bamb_1905
            BPS: BPSL1413(pgi)
            BPM: BURPS1710b_2466(pgi)
            BPL: BURPS1106A_2347(pgi)
            BPD: BURPS668_2308(pgi)
            BTE: BTH_I2132
            PNU: Pnuc_1091
            BPE: BP1971(pgi) BP3142(pgi)
            BPA: BPP0799(pgi) BPP2350(pgi)
            BBR: BB0884(pgi) BB1801(pgi)
            RFR: Rfer_1127
            POL: Bpro_0753
            PNA: Pnap_0655
            AAV: Aave_0944
            AJS: Ajs_0697
            VEI: Veis_2081 Veis_4222
            MPT: Mpe_A3094
            HAR: HEAR1085(pgi)
            MMS: mma_2312
            NEU: NE2263(pgi)
            NET: Neut_0609
            NMU: Nmul_A0469
            EBA: ebA5208(pgi)
            AZO: azo1519(pgi)
            DAR: Daro_0581
            TBD: Tbd_0974 Tbd_2063
            MFA: Mfla_1325
            HPY: HP1166(pgi)
            HPA: HPAG1_1105
            HHE: HH0491(pgi)
            HAC: Hac_1346(pgi)
            WSU: WS1027
            TDN: Tmden_1472
            CJE: Cj1535c(pgi)
            CJR: CJE1706(pgi)
            CJJ: CJJ81176_1520(pgi)
            CJU: C8J_1434(pgi)
            CJD: JJD26997_1267(pgi) JJD26997_1887(pgi)
            CFF: CFF8240_0079(pgi)
            CCV: CCV52592_2200(pgi)
            CHA: CHAB381_0522(pgi)
            CCO: CCC13826_0430(pgi)
            ABU: Abu_0838(pgi)
            NIS: NIS_0945
            SUN: SUN_1276 SUN_1935
            GSU: GSU1311(glk)
            GME: Gmet_2458
            GUR: Gura_3752
            PCA: Pcar_2367
            PPD: Ppro_1372
            DVU: DVU3222(pgi)
            DVL: Dvul_0166
            DDE: Dde_3597
            LIP: LI0879(pgi)
            BBA: Bd0741(pgi)
            DPS: DP0796
            ADE: Adeh_3080
            AFW: Anae109_2086
            MXA: MXAN_6908(pgi)
            SAT: SYN_02950
            SFU: Sfum_3591
            PUB: SAR11_0155(pgi) SAR11_0523
            MLO: mlr5411
            MES: Meso_0070
            PLA: Plav_0292
            SME: SMb20857 SMc02042 SMc02163(pgi)
            SMD: Smed_0109 Smed_2463
            ATU: Atu0404(pgi)
            ATC: AGR_C_711
            RET: RHE_CH00477(pgi)
            RLE: RL0504(pgi)
            BME: BMEI1636
            BMF: BAB1_0316
            BMS: BR0285(pgi)
            BMB: BruAb1_0311(pgi)
            BOV: BOV_0299(pgi)
            OAN: Oant_0369
            BJA: blr6758
            BRA: BRADO5809
            BBT: BBta_6315
            RPA: RPA3634(tal)
            RPB: RPB_1892
            RPC: RPC_3670
            RPD: RPD_3474
            RPE: RPE_3708
            NWI: Nwi_2641
            BHE: BH01370(gpi)
            BQU: BQ01300(gpi)
            BBK: BARBAKC583_0307(pgi)
            XAU: Xaut_1250
            CCR: CC_0222
            SIL: SPO2046(pgi)
            SIT: TM1040_0378
            RSP: RSP_2736(pgi)
            RSH: Rsph17029_1394
            RSQ: Rsph17025_1776
            JAN: Jann_1971
            RDE: RD1_2720(pgi)
            PDE: Pden_1950
            MMR: Mmar10_2431
            HNE: HNE_1733(pgi)
            ZMO: ZMO1212(pgi)
            NAR: Saro_1809
            SAL: Sala_1215
            SWI: Swit_2723
            ELI: ELI_04850
            GOX: GOX1704
            GBE: GbCGDNIH1_0855
            RRU: Rru_A2947
            MAG: amb4414
            MGM: Mmc1_1935
            ABA: Acid345_2810
            SUS: Acid_1923
            BSU: BG12366(pgi)
            BHA: BH3343(pgi)
            BAN: BA5130(pgi)
            BAR: GBAA5130(pgi)
            BAA: BA_0004
            BAT: BAS4767
            BCE: BC4898
            BCA: BCE_5037(pgi)
            BCZ: BCZK4630(pgi)
            BCY: Bcer98_3509
            BTK: BT9727_4607(pgi)
            BTL: BALH_4440(pgi)
            BLI: BL02591(pgi)
            BLD: BLi03314(pgi)
            BCL: ABC2906(pgi)
            BAY: RBAM_028430
            BPU: BPUM_2802
            OIH: OB2336(pgi)
            GKA: GK2924
            SAU: SA0823(pgi)
            SAV: SAV0962(pgi)
            SAM: MW0844(pgi)
            SAR: SAR0924
            SAS: SAS0832
            SAC: SACOL0966(pgi)
            SAB: SAB0830
            SAA: SAUSA300_0865(pgi)
            SAO: SAOUHSC_00900
            SAJ: SaurJH9_0962 SaurJH9_2766
            SAH: SaurJH1_0981 SaurJH1_2811
            SEP: SE0658
            SER: SERP0550(pgi)
            SHA: SH1988(pgi)
            SSP: SSP1813
            LMO: lmo2367(pgi)
            LMF: LMOf2365_2338(pgi)
            LIN: lin2466(pgi)
            LWE: lwe2316(pgi)
            LLA: L0012(pgiA)
            LLC: LACR_2470
            LLM: llmg_2448(pgiA)
            SPY: SPy_0215(pgi)
            SPZ: M5005_Spy_0185(pgi)
            SPM: spyM18_0204(pgi)
            SPG: SpyM3_0156(pgi)
            SPS: SPs0162
            SPH: MGAS10270_Spy0187(pgi)
            SPI: MGAS10750_Spy0179(pgi)
            SPJ: MGAS2096_Spy0198(pgi)
            SPK: MGAS9429_Spy0187(pgi)
            SPF: SpyM50167(pgi)
            SPA: M6_Spy0219
            SPB: M28_Spy0183(pgi)
            SPN: SP_2070
            SPR: spr1882(gpi)
            SPD: SPD_1897(pgi)
            SAG: SAG0402(pgi)
            SAN: gbs0437(pgi)
            SAK: SAK_0475(pgi)
            SMU: SMU.307(pgi)
            STC: str0194(pgi)
            STL: stu0194(pgi)
            SSA: SSA_2183(pgi)
            SGO: SGO_0154(pgi)
            LPL: lp_2502(pgi)
            LJO: LJ0924
            LAC: LBA0752
            LSA: LSA1179(pgi)
            LSL: LSL_0464(pgi)
            LDB: Ldb0692(pgi)
            LBU: LBUL_0625
            LBR: LVIS_1312
            LCA: LSEI_1126
            LRE: Lreu_0420
            EFA: EF1416(pgi)
            OOE: OEOE_0636
            STH: STH1008
            CAC: CAC2680(pgi)
            CPE: CPE2267
            CPF: CPF_2549(pgi)
            CPR: CPR_2252(pgi)
            CTC: CTC02404
            CNO: NT01CX_0441
            CTH: Cthe_0217
            CDF: CD3285(pgi)
            CBO: CBO3278(pgi)
            CBA: CLB_3335(pgi)
            CBH: CLC_3221(pgi)
            CBF: CLI_3449(pgi)
            CBE: Cbei_0341
            CKL: CKL_3491(pgi)
            AMT: Amet_1375
            CHY: CHY_0239(pgi)
            DSY: DSY2034
            DRM: Dred_2902
            TTE: TTE1806(pgi)
            MGE: MG_111(pgi)
            MPN: MPN250(pgiB)
            MPU: MYPU_1310(pgiB)
            MPE: MYPE4690(pgi)
            MGA: MGA_0457(pgi)
            MMY: MSC_0505(pgi)
            MMO: MMOB5540(pgi)
            MHY: mhp548(pgiB)
            MHJ: MHJ_0532(pgiB)
            MHP: MHP7448_0531(pgiB)
            MSY: MS53_0483(pgiB)
            MCP: MCAP_0465(pgi)
            POY: PAM283(pgi)
            AYW: AYWB_438(pgi)
            MFL: Mfl254
            MTU: Rv0946c(pgi)
            MTC: MT0972(pgi)
            MBO: Mb0971c(pgi)
            MBB: BCG_1000c(pgi)
            MLE: ML0150(pgi)
            MPA: MAP0891c(pgi)
            MAV: MAV_1068(pgi)
            MSM: MSMEG_2114 MSMEG_5541(pgi)
            MVA: Mvan_4877
            MGI: Mflv_1857
            MMC: Mmcs_4334
            MKM: Mkms_4420
            MJL: Mjls_4714
            CGL: NCgl0817(pgi)
            CGB: cg0973(pgi)
            CEF: CE0927
            CDI: DIP0832(pgi)
            CJK: jk0449(pgi)
            NFA: nfa49980(pgi)
            RHA: RHA1_ro05567 RHA1_ro11063(pgi1) RHA1_ro11167(pgi2)
                 RHA1_ro11327(pgi3)
            SCO: SCO1942(pgi2) SCO6659(pgi)
            SMA: SAV1770(pgi1) SAV6302(pgi2)
            TWH: TWT342(gpi)
            TWS: TW429(pgi)
            LXX: Lxx11600(pgiA)
            ART: Arth_1801
            AAU: AAur_2095(pgi)
            PAC: PPA2131
            TFU: Tfu_2004
            FRA: Francci3_0045
            FAL: FRAAL0052(pgi)
            KRA: Krad_1463
            SEN: SACE_2158(pgiA)
            BLO: BL0279(gpi)
            BAD: BAD_0231(pgi)
            RXY: Rxyl_2677
            FNU: FN2054
            RBA: RB399(pgi)
            CTR: CT378(pgi)
            CTA: CTA_0412(pgi)
            CMU: TC0657
            CPN: CPn1025(pgi)
            CPA: CP0827
            CPJ: CPj1025(pgi)
            CPT: CpB1064
            CCA: CCA00736(pgi)
            CAB: CAB703(pgi)
            CFE: CF0280(pgi)
            PCU: pc0781(pgi)
            BGA: BG0752(pgi)
            BAF: BAPKO_0774(pgi)
            TPA: TP0475
            TDE: TDE2573(pgi)
            LIL: LA3888(pgi)
            LIC: LIC13105(pgi)
            LBJ: LBJ_0600(pgi)
            LBL: LBL_2480(pgi)
            SYN: slr1349(pgi)
            SYW: SYNW1256(pgi)
            SYC: syc2066_c(pgi)
            SYF: Synpcc7942_2029
            SYD: Syncc9605_1381
            SYE: Syncc9902_1105
            SYG: sync_1376(pgi)
            SYR: SynRCC307_1347(pgi)
            SYX: SynWH7803_1259(pgi)
            CYA: CYA_0387(pgi)
            CYB: CYB_2919(pgi)
            TEL: tll0717
            GVI: gll1692
            ANA: alr1050
            AVA: Ava_3708
            PMA: Pro0946(pgi)
            PMM: PMM0890(pgi)
            PMT: PMT0714(pgi)
            PMN: PMN2A_0320
            PMI: PMT9312_0910
            PMB: A9601_09711(pgi)
            PMC: P9515_09721(pgi)
            PMF: P9303_15071(pgi)
            PMG: P9301_09691(pgi)
            PMH: P9215_10021
            PME: NATL1_09931(pgi)
            TER: Tery_4024
            BTH: BT_2124
            BFR: BF3812
            BFS: BF3604(pgiA)
            PGI: PG1368(pgi)
            CHU: CHU_0472(pgi)
            GFO: GFO_3166(pgi)
            FJO: Fjoh_0735
            FPS: FP0145(pgi)
            CTE: CT0988(pgi)
            CCH: Cag_0612
            CPH: Cpha266_1095
            PVI: Cvib_0791
            PLT: Plut_1161
            RRS: RoseRS_4356
            RCA: Rcas_0710
            DRA: DR_1742
            DGE: Dgeo_1304
            TTH: TTC1710
            TTJ: TTHA0277
            AAE: aq_750(pgi)
            TMA: TM1385
            TPT: Tpet_1398
            TME: Tmel_1843
            FNO: Fnod_0874
            MJA: MJ1605
            MMP: MMP1295
            MMQ: MmarC5_0298
            MMZ: MmarC7_0540
            MAE: Maeo_0006
            MVN: Mevan_0605
            MAC: MA0821
            MBA: Mbar_A1750
            MMA: MM_1968
            MBU: Mbur_1503
            MHU: Mhun_2600
            AFU: AF1494
            HAL: VNG1992G(pgi)
            HMA: rrnAC3210(pgi)
            HWA: HQ3101A(pgi)
            NPH: NP4992A(pgi)
            PTO: PTO1226
            PHO: PH1956
            PAB: PAB1199
            PFU: PF0196
            TKO: TK1111
            RCI: RCIX333(gpi)
            APE: APE_0768.1
STRUCTURES  PDB: 1B0Z  1C7Q  1C7R  1DQR  1G98  1GZD  1GZV  1HM5  1HOX  1IAT  
                 1IRI  1J3P  1J3Q  1J3R  1JIQ  1JLH  1KOJ  1N8T  1NUH  1PGI  
                 1Q50  1QXJ  1QXR  1QY4  1T10  1TZB  1TZC  1U0E  1U0F  1U0G  
                 1X7N  1X82  1X8E  1X9H  1X9I  1XTB  1ZZG  2CVP  2CXN  2CXO  
                 2CXP  2CXQ  2CXR  2CXS  2CXT  2CXU  2GC0  2GC1  2GC2  2GC3  
                 2PGI  2Q8N  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.9
            ExPASy - ENZYME nomenclature database: 5.3.1.9
            ExplorEnz - The Enzyme Database: 5.3.1.9
            ERGO genome analysis and discovery system: 5.3.1.9
            BRENDA, the Enzyme Database: 5.3.1.9
            CAS: 9001-41-6
///
ENTRY       EC 5.3.1.10       Obsolete  Enzyme
NAME        Transferred to 3.5.99.6
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
COMMENT     Transferred entry: now EC 3.5.99.6, glucosamine-6-phosphate
            deaminase (EC 5.3.1.10 created 1961, deleted 2000)
STRUCTURES  PDB: 1CD5  1DEA  1FQO  1FRZ  1FS5  1FS6  1FSF  1HOR  1HOT  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.10
            ExPASy - ENZYME nomenclature database: 5.3.1.10
            ExplorEnz - The Enzyme Database: 5.3.1.10
            ERGO genome analysis and discovery system: 5.3.1.10
            BRENDA, the Enzyme Database: 5.3.1.10
///
ENTRY       EC 5.3.1.11       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
COMMENT     Deleted entry: acetylglucosaminephosphate isomerase (EC 5.3.1.11
            created 1961, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.11
            ExPASy - ENZYME nomenclature database: 5.3.1.11
            ExplorEnz - The Enzyme Database: 5.3.1.11
            ERGO genome analysis and discovery system: 5.3.1.11
            BRENDA, the Enzyme Database: 5.3.1.11
///
ENTRY       EC 5.3.1.12                 Enzyme
NAME        glucuronate isomerase;
            uronic isomerase;
            uronate isomerase;
            D-glucuronate isomerase;
            uronic acid isomerase;
            D-glucuronate ketol-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     D-glucuronate aldose-ketose-isomerase
REACTION    D-glucuronate = D-fructuronate [RN:R01482]
ALL_REAC    R01482;
            (other) R01983
SUBSTRATE   D-glucuronate [CPD:C00191]
PRODUCT     D-fructuronate [CPD:C00905]
COMMENT     Also converts D-galacturonate to D-tagaturonate.
REFERENCE   1
  AUTHORS   Ashwell, G., Wahba, A.J. and Hickman, J.
  TITLE     Uronic acid metabolism in bacteria. I. Purification and properties
            of uronic acid isomerase in Escherichia coli.
  JOURNAL   J. Biol. Chem. 235 (1960) 1559-1565.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:14409051]
  AUTHORS   KILGORE WW, STARR MP.
  TITLE     Catabolism of galacturonic and glucuronic acids by Erwinia
            carotovora.
  JOURNAL   J. Biol. Chem. 234 (1959) 2227-35.
  ORGANISM  Erwinia carotovora [GN:eca]
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K01812  glucuronate isomerase
GENES       ECO: b3092(uxaC)
            ECJ: JW3063(uxaC)
            ECE: Z4445(uxaC)
            ECS: ECs3974
            ECC: c3850(uxaC)
            ECI: UTI89_C3530(uxaC)
            ECP: ECP_3183
            ECV: APECO1_3327(uxaC)
            ECW: EcE24377A_3560(uxaC)
            ECX: EcHS_A3275(uxaC)
            STY: STY3308(uxaC)
            STT: t3058(uxaC)
            SPT: SPA3005(uxaC)
            SEC: SC3078(uxaC)
            STM: STM3137
            YPE: YPO0579(uxaC)
            YPK: y3600(uxaC)
            YPM: YP_2899(uxaC)
            YPA: YPA_3210
            YPN: YPN_0447 YPN_0448
            YPP: YPDSF_0366
            YPS: YPTB3478(uxaC)
            YPI: YpsIP31758_0491(uxaC)
            SFL: SF3132(uxaC)
            SFX: S3339(uxaC)
            SFV: SFV_3133(uxaC)
            SSN: SSON_3245(uxaC)
            SBO: SBO_2953(uxaC)
            ECA: ECA0645(uxaC)
            PLU: plu0176(uxaC)
            ENT: Ent638_3546
            SPE: Spro_4321
            HIT: NTHI0056(uxuC)
            HIQ: CGSHiGG_02755
            HSO: HS_1602(uxaC)
            MSU: MS0544(uxaC)
            APL: APL_1020(uxaC)
            ASU: Asuc_0145
            XCC: XCC4117(hrmI)
            XCB: XC_4209
            XCV: XCV4357(uxaC)
            XAC: XAC4251(hrmI)
            XOO: XOO4427(hrmI)
            XOM: XOO_4170(XOO4170)
            VVU: VV2_1070
            VVY: VVA1594
            VPA: VPA1706
            PPR: PBPRB1515(uxaC)
            SDE: Sde_0940 Sde_1272
            PIN: Ping_0131
            MMW: Mmwyl1_2780
            GME: Gmet_0451
            MLO: mll4056
            MES: Meso_4496
            SME: SMb21354(uxaC)
            SMD: Smed_4749
            RET: RHE_CH00090(uxaC)
            RLE: RL0099
            BME: BMEII0476 BMEII0477
            BMF: BAB2_0424 BAB2_0425
            BMS: BRA0812
            CCR: CC_1490
            SIT: TM1040_3865
            RSP: RSP_0488(uxaC)
            RSH: Rsph17029_2139
            RSQ: Rsph17025_2412
            RDE: RD1_2934(uxaC)
            MMR: Mmar10_0230
            SAL: Sala_3046
            SWI: Swit_1887
            ABA: Acid345_4306
            SUS: Acid_5330
            BSU: BG13204(uxaC)
            BHA: BH0705
            BLI: BL00708(uxaC)
            BLD: BLi03516(uxaC)
            BCL: ABC0995(uxaC)
            BAY: RBAM_012380(uxaC)
            BPU: BPUM_2987(uxaC)
            OIH: OB0367
            SHA: SH2648
            LLA: L0019(uxaC)
            LLC: LACR_1742
            LLM: llmg_0862(uxaC)
            SPH: MGAS10270_Spy1171
            SAG: SAG0701(uxaC)
            SAN: gbs0674
            SAK: SAK_0827(uxaC)
            LSA: LSA0129(uxaC)
            LBR: LVIS_0135 LVIS_0150
            CAC: CAC0692(uxaC)
            CPE: CPE0152(uxaC)
            CBE: Cbei_1832 Cbei_4082 Cbei_4657
            AMT: Amet_1291
            CSC: Csac_1949
            TTE: TTE1939(uxaC)
            CGL: NCgl2398(cgl2484)
            CGB: cg2731(uxaC)
            CEF: CE2377
            LXX: Lxx17350(uxaC)
            ART: Arth_0502
            AAU: AAur_0527(uxaC)
            PAC: PPA2329
            KRA: Krad_0587
            SEN: SACE_5055(hrmI)
            BTH: BT_0823
            BFR: BF2293
            BFS: BF2382(uxaC)
            FJO: Fjoh_4262
            TMA: TM0064
            TPT: Tpet_0860
STRUCTURES  PDB: 1J5S  2Q01  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.12
            ExPASy - ENZYME nomenclature database: 5.3.1.12
            ExplorEnz - The Enzyme Database: 5.3.1.12
            ERGO genome analysis and discovery system: 5.3.1.12
            BRENDA, the Enzyme Database: 5.3.1.12
            CAS: 9023-87-4
///
ENTRY       EC 5.3.1.13                 Enzyme
NAME        arabinose-5-phosphate isomerase;
            arabinose phosphate isomerase;
            phosphoarabinoisomerase;
            D-arabinose-5-phosphate ketol-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     D-arabinose-5-phosphate aldose-ketose-isomerase
REACTION    D-arabinose 5-phosphate = D-ribulose 5-phosphate [RN:R01530]
ALL_REAC    R01530
SUBSTRATE   D-arabinose 5-phosphate [CPD:C01112]
PRODUCT     D-ribulose 5-phosphate [CPD:C00199]
REFERENCE   1
  AUTHORS   Volk, W.A.
  TITLE     Purification and properties of phosphoarabinoisomerase from
            Propionibacterium pentosaceum.
  JOURNAL   J. Biol. Chem. 235 (1960) 1550-1553.
  ORGANISM  Propionibacterium pentosaceum
ORTHOLOGY   KO: K06041  arabinose-5-phosphate isomerase
GENES       OSA: 4328364
            ECO: b3197(yrbH)
            ECJ: JW3164(kdsD)
            ECE: Z4560(yrbH)
            ECS: ECs4076
            ECC: c3957(yrbH)
            ECI: UTI89_C3362(kpsF) UTI89_C3633(yrbH)
            ECP: ECP_3285
            ECV: APECO1_3238(kdsD) APECO1_3482(kpsF)
            ECW: EcE24377A_3685(kdsD)
            ECX: EcHS_A3390(kdsD)
            STY: STY3494
            STT: t3232
            SPT: SPA3182(yrbH)
            SEC: SC3253(yrbH)
            STM: STM3315(yrbH)
            YPE: YPO3577
            YPK: y0149
            YPM: YP_3832(gutQ1)
            YPA: YPA_3726
            YPN: YPN_3459
            YPP: YPDSF_0320
            YPS: YPTB3521
            YPI: YpsIP31758_0446(kdsD)
            SFL: SF3237(yrbH)
            SFX: S3455(yrbH)
            SFV: SFV_3227(yrbH)
            SSN: SSON_3345(yrbH)
            SBO: SBO_3185(yrbH)
            SDY: SDY_3378(yrbH)
            ECA: ECA0293
            PLU: plu4036
            SGL: SG0204
            ENT: Ent638_3180 Ent638_3633
            KPN: KPN_03607(yrbH)
            SPE: Spro_3575 Spro_4362
            BPN: BPEN_474(gutQ)
            HIN: HI1678(kpsF)
            HIT: NTHI1981
            PMU: PM0525(kpsF)
            MSU: MS0996(gutQ)
            ASU: Asuc_1671
            XFA: XF1413
            XFT: PD0642(kpsF)
            XCC: XCC2797(kpsF)
            XCB: XC_1316
            XCV: XCV3113
            XAC: XAC2967(kpsF)
            XOO: XOO1289(kpsF)
            XOM: XOO_1188(XOO1188)
            VCH: VC2523
            VVU: VV1_0687
            VVY: VV0453
            VPA: VP2666
            VFI: VF0179 VF0392
            PPR: PBPRA3250
            PAE: PA4457
            PAU: PA14_57890(yrbH)
            PPU: PP_0957
            PPF: Pput_0996 Pput_3910
            PST: PSPTO_4448
            PSB: Psyr_4142
            PSP: PSPPH_4146(kdsD)
            PFL: PFL_0920(kdsD)
            PFO: Pfl_0862
            PEN: PSEEN1098
            PMY: Pmen_0875
            PAR: Psyc_0922(kpsF)
            PCR: Pcryo_1492
            PRW: PsycPRwf_0822
            ACI: ACIAD1482(kdsD)
            ACB: A1S_1236
            SON: SO_3956
            SDN: Sden_0494
            SFR: Sfri_3372
            SAZ: Sama_3083
            SBL: Sbal_3663
            SBM: Shew185_0691
            SLO: Shew_3306
            SPC: Sputcn32_0720
            SSE: Ssed_0731
            SPL: Spea_3611
            SHE: Shewmr4_0678
            SHM: Shewmr7_3344
            SHN: Shewana3_0677
            SHW: Sputw3181_3453
            ILO: IL0401
            CPS: CPS_4538
            PHA: PSHAa2546(ksdD)
            PAT: Patl_0563
            SDE: Sde_3174
            PIN: Ping_0617
            MAQ: Maqu_2710
            CBU: CBU_0750
            CBD: COXBU7E912_0763(kdsD)
            LPN: lpg0840
            LPF: lpl0871(kdsD)
            LPP: lpp0902(kdsD)
            MCA: MCA0746
            FTU: FTT0788c(kdsD)
            FTF: FTF0788c(kdsD)
            FTL: FTL_1433
            FTH: FTH_1396(kdsD)
            FTA: FTA_1521
            FTN: FTN_1222(kpsF)
            TCX: Tcr_0503
            NOC: Noc_2788
            AEH: Mlg_2225
            HHA: Hhal_2121
            HCH: HCH_05315
            CSA: Csal_2221
            ABO: ABO_0557(kpsF)
            MMW: Mmwyl1_1123
            AHA: AHA_3928(kdsD)
            DNO: DNO_0536
            RMA: Rmag_0158
            VOK: COSY_0163
            NME: NMB0352
            NMA: NMA2135
            NMC: NMC1816
            NGO: NGO1609(kpsF)
            CVI: CV_3327
            RSO: RSc0413(RS03381)
            REU: Reut_A0359
            RME: Rmet_0307 Rmet_5735
            BMA: BMA3102
            BXE: Bxe_A4117
            BVI: Bcep1808_2891
            BUR: Bcep18194_A6116 Bcep18194_C7389
            BCN: Bcen_2172
            BCH: Bcen2424_2786
            BAM: Bamb_2846 Bamb_6185
            BPS: BPSL2770
            BPM: BURPS1710b_0770 BURPS1710b_3262(kpsF)
            BTE: BTH_I0491 BTH_I1362
            PNU: Pnuc_1907
            RFR: Rfer_4237
            POL: Bpro_4898
            PNA: Pnap_4108
            AAV: Aave_4785
            AJS: Ajs_4132
            VEI: Veis_0154
            HAR: HEAR3104(kdsD)
            DAR: Daro_3418
            TBD: Tbd_0538(kpsF)
            MFA: Mfla_0137
            HPA: HPAG1_1354
            HAC: Hac_0115
            TDN: Tmden_0213
            CJE: Cj1443c(kpsF)
            CCV: CCV52592_1114
            CCO: CCC13826_1886
            NIS: NIS_0063
            SUN: SUN_2364
            GSU: GSU1893
            GME: Gmet_1278
            GUR: Gura_2977
            PCA: Pcar_1943
            PPD: Ppro_0969
            DVL: Dvul_2580 Dvul_2808
            DDE: Dde_0335
            LIP: LI0083(kpsF)
            ADE: Adeh_4064
            AFW: Anae109_0363
            MXA: MXAN_5923(gutQ)
            SAT: SYN_00471
            SFU: Sfum_0006
            RFE: RF_0720(kpsF)
            RBE: RBE_0774(kpsF)
            PUB: SAR11_0497(gutQ)
            PLA: Plav_1901
            SMD: Smed_0192 Smed_4997 Smed_5015
            RET: RHE_CH03559(kpsF)
            RLE: RL4079(kdsD)
            OAN: Oant_4269
            BRA: BRADO6245(kpsF)
            BBT: BBta_1362(kpsF)
            RPB: RPB_4539
            RPC: RPC_0769
            RPD: RPD_0864
            RPE: RPE_0696
            NWI: Nwi_0931
            NHA: Nham_3413
            XAU: Xaut_1895
            SIL: SPO0082(kdsD)
            SIT: TM1040_3854
            RSP: RSP_1153(gutQ)
            RSH: Rsph17029_2814
            RSQ: Rsph17025_2774
            JAN: Jann_0073
            RDE: RD1_0368(kdsD)
            PDE: Pden_2608
            MMR: Mmar10_2497
            NAR: Saro_0727
            SWI: Swit_3965 Swit_4477
            GBE: GbCGDNIH1_0700
            ACR: Acry_1670
            RRU: Rru_A0014
            MAG: amb3933
            MGM: Mmc1_3339
            ABA: Acid345_1058
            SUS: Acid_2500
            CTR: CT399(yrbH)
            CTA: CTA_0434(yrbH)
            CMU: TC0679
            CPN: CPn0526(kpsF)
            CPA: CP0226
            CPJ: CPj0526(kpsF)
            CPT: CpB0547(kpsF)
            CCA: CCA00219
            CAB: CAB215
            CFE: CF0788(kpsF)
            PCU: pc1782(gutQ)
            SYF: Synpcc7942_2291
            SYD: Syncc9605_0183
            SYE: Syncc9902_0211
            PMF: P9303_25501
            TER: Tery_3105
            BFR: BF0172
            CHU: CHU_0298
            FJO: Fjoh_0282
            FPS: FP1234(kdsD)
            CTE: CT0270
            CCH: Cag_0467
            CPH: Cpha266_0401
            PVI: Cvib_1528
            PLT: Plut_1747
            AAE: aq_1546(kpsF)
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.13
            ExPASy - ENZYME nomenclature database: 5.3.1.13
            ExplorEnz - The Enzyme Database: 5.3.1.13
            ERGO genome analysis and discovery system: 5.3.1.13
            BRENDA, the Enzyme Database: 5.3.1.13
            CAS: 9023-86-3
///
ENTRY       EC 5.3.1.14                 Enzyme
NAME        L-rhamnose isomerase;
            rhamnose isomerase;
            L-rhamnose ketol-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     L-rhamnose aldose-ketose-isomerase
REACTION    L-rhamnose = L-rhamnulose [RN:R02437]
ALL_REAC    R02437
SUBSTRATE   L-rhamnose [CPD:C00507]
PRODUCT     L-rhamnulose [CPD:C00861]
REFERENCE   1  [PMID:14095156]
  AUTHORS   DOMAGK GF, ZECH R.
  TITLE     [ON THE DECOMPOSITION OF DESOXY SUGARS BY BACTERIAL ENZYMES. I.
            L-RHAMNOSE ISOMERASE FROM LACTOBACILLUS PLANTARUM.]
  JOURNAL   Biochem. Z. 339 (1963) 145-53.
  ORGANISM  Lactobacillus plantarum [GN:lpl]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K01813  L-rhamnose isomerase
GENES       ECO: b3903(rhaA)
            ECJ: JW5561(rhaA)
            ECE: Z5447(rhaA)
            ECS: ECs4830
            ECC: c4852(rhaA)
            ECI: UTI89_C4486(rhaA)
            ECP: ECP_4113
            ECV: APECO1_2565(rhaA)
            ECW: EcE24377A_4434(rhaA)
            ECX: EcHS_A4132(rhaA)
            STY: STY3827(rhaA)
            STT: t3573(rhaA)
            SPT: SPA3889(rhaA)
            SEC: SC3936(rhaA)
            STM: STM4046(rhaA)
            YPE: YPO0329(rhaA)
            YPK: y0586(rhaA)
            YPM: YP_0484(rhaA)
            YPA: YPA_3953
            YPN: YPN_3341
            YPP: YPDSF_3643
            YPS: YPTB0384(rhaA)
            YPI: YpsIP31758_3756(rhaA)
            SFX: S3768(rhaA)
            SFV: SFV_3592(rhaA)
            SSN: SSON_4073(rhaA)
            SBO: SBO_3921(rhaA)
            ECA: ECA0439(rhaA)
            ENT: Ent638_4068
            MSU: MS2328
            JAN: Jann_2591
            BSU: BG12387(yulE)
            BHA: BH1552
            BCL: ABC0374
            OIH: OB0496
            LMO: lmo2848
            LMF: LMOf2365_2838(rhaA)
            LIN: lin2980
            LPL: lp_3593(rhaA)
            LSL: LSL_1754
            EFA: EF0434(rhaA)
            CBE: Cbei_0446
            CSC: Csac_0876
            MSM: MSMEG_0589(rhaI)
            AAU: AAur_3715(rhaI)
            RBA: RB678(rhaA)
            BTH: BT_3764
            RRS: RoseRS_2730
            RCA: Rcas_3455
STRUCTURES  PDB: 1D8W  1DE5  1DE6  2HCV  2I56  2I57  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.14
            ExPASy - ENZYME nomenclature database: 5.3.1.14
            ExplorEnz - The Enzyme Database: 5.3.1.14
            ERGO genome analysis and discovery system: 5.3.1.14
            BRENDA, the Enzyme Database: 5.3.1.14
            CAS: 9023-84-1
///
ENTRY       EC 5.3.1.15                 Enzyme
NAME        D-lyxose ketol-isomerase;
            D-lyxose isomerase;
            D-lyxose ketol-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     D-lyxose aldose-ketose-isomerase
REACTION    D-lyxose = D-xylulose [RN:R01898]
ALL_REAC    R01898
SUBSTRATE   D-lyxose [CPD:C00476]
PRODUCT     D-xylulose [CPD:C00310]
REFERENCE   1  [PMID:14304839]
  AUTHORS   ANDERSON RL, ALLISON DP.
  TITLE     PURIFICATION AND CHARACTERIZATION OF D-LYXOSE ISOMERASE.
  JOURNAL   J. Biol. Chem. 240 (1965) 2367-72.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
STRUCTURES  PDB: 1QO2  1VZW  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.15
            ExPASy - ENZYME nomenclature database: 5.3.1.15
            ExplorEnz - The Enzyme Database: 5.3.1.15
            ERGO genome analysis and discovery system: 5.3.1.15
            BRENDA, the Enzyme Database: 5.3.1.15
            CAS: 37318-42-6
///
ENTRY       EC 5.3.1.16                 Enzyme
NAME        1-(5-phosphoribosyl)-5-[(5-
            phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
            isomerase;
            N-(5'-phospho-D-ribosylformimino)-5-amino-1-(5"-phosphoribosyl)-4-
            imidazolecarboxamide isomerase;
            phosphoribosylformiminoaminophosphoribosylimidazolecarboxamide
            isomerase;
            N-(phosphoribosylformimino) aminophosphoribosylimidazolecarboxamide
            isomerase;
            1-(5-phosphoribosyl)-5-[(5-
            phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
            ketol-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imid
            azole-4-carboxamide aldose-ketose-isomerase
REACTION    1-(5-phosphoribosyl)-5-[(5-
            phosphoribosylamino)methylideneamino]imidazole-4-carboxamide =
            5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-
            phosphoribosyl)imidazole-4-carboxamide [RN:R04640]
ALL_REAC    R04640
SUBSTRATE   1-(5-phosphoribosyl)-5-[(5-
            phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
            [CPD:C04896]
PRODUCT     5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-
            phosphoribosyl)imidazole-4-carboxamide [CPD:C04916]
REFERENCE   1  [PMID:5330429]
  AUTHORS   Margolies MN, Goldberger RF.
  TITLE     Isolation of the fourth (isomerase) of histidine biosynthesis from
            Salmonella typhimurium.
  JOURNAL   J. Biol. Chem. 241 (1966) 3262-9.
  ORGANISM  Salmonella typhimurium
PATHWAY     PATH: map00340  Histidine metabolism
ORTHOLOGY   KO: K01814  phosphoribosylformimino-5-aminoimidazole carboxamide
                        ribotide isomerase
GENES       ATH: AT2G36230(APG10)
            OSA: 4338727
            CME: CMS245C
            SCE: YIL020C(HIS6)
            AGO: AGOS_ADL121W
            PIC: PICST_65481(HIS7)
            CGR: CAGL0J02398g
            SPO: SPAC3F10.09 SPBC418.01c
            ANI: AN2293.2
            AFM: AFUA_5G06160
            AOR: AO090009000641
            ECO: b2024(hisA)
            ECJ: JW2006(hisA)
            ECE: Z3186(hisA)
            ECS: ECs2825
            ECC: c2551(hisA)
            ECI: UTI89_C2297(hisA)
            ECP: ECP_2067
            ECV: APECO1_1121(hisA)
            ECW: EcE24377A_2315(hisA)
            ECX: EcHS_A2163(hisA)
            STY: STY2285(hisA)
            STT: t0797(hisA)
            SPT: SPA0795(hisA)
            SEC: SC2086(hisA)
            STM: STM2076(hisA)
            YPE: YPO1544(hisA)
            YPK: y2626(hisA)
            YPM: YP_1433(hisA)
            YPA: YPA_0839
            YPN: YPN_2436
            YPS: YPTB1557(hisA)
            YPI: YpsIP31758_2433(hisA)
            SFL: SF2086(hisA)
            SFX: S2207(hisA)
            SFV: SFV_2084(hisA)
            SSN: SSON_2095(hisA)
            SBO: SBO_0850(hisA)
            SDY: SDY_2217(hisA)
            ECA: ECA2587(hisA)
            PLU: plu0797 plu1566(hisA)
            BUC: BU104(hisA)
            BAS: BUsg097(hisA)
            BAB: bbp098(hisA)
            BCC: BCc_068(hisA)
            SGL: SG1125
            BFL: Bfl467(hisA)
            BPN: BPEN_482(hisA)
            HIN: HI0473(hisA)
            HIT: NTHI0604(hisA)
            HIP: CGSHiEE_00630
            HIQ: CGSHiGG_05610
            PMU: PM1203(hisA)
            MSU: MS1883(hisA)
            APL: APL_2026(hisA)
            XFA: XF2215
            XFT: PD1263(hisA)
            XCC: XCC1813(hisA)
            XCB: XC_2376
            XCV: XCV1879(hisA)
            XAC: XAC1833(hisA)
            XOO: XOO2260(hisA)
            VCH: VC1137
            VCO: VC0395_A0707(hisA)
            VVU: VV1_2915
            VVY: VV1355
            VPA: VP1142
            VFI: VF1017
            PPR: PBPRA1087
            PAE: PA5141(hisA)
            PAU: PA14_67890(hisA)
            PAP: PSPA7_5876(hisA)
            PPU: PP_0292(hisA)
            PST: PSPTO_5335(hisA)
            PSB: Psyr_4894
            PSP: PSPPH_0380 PSPPH_4923(hisA)
            PFL: PFL_0364
            PFO: Pfl_0326
            PEN: PSEEN5192(hisA)
            PAR: Psyc_2103(hisA)
            PCR: Pcryo_2423
            ACI: ACIAD3398(hisA)
            ACB: A1S_3238
            SON: SO_2069(hisA)
            SDN: Sden_1613
            SFR: Sfri_1715
            SAZ: Sama_1946
            SBL: Sbal_2430
            SLO: Shew_2202
            SHE: Shewmr4_1795
            SHM: Shewmr7_2182
            SHN: Shewana3_1849 Shewana3_2312
            SHW: Sputw3181_1826
            ILO: IL1839(hisA)
            CPS: CPS_3894(hisA)
            PHA: PSHAb0489(hisA)
            PAT: Patl_2885
            SDE: Sde_0489
            PIN: Ping_1652
            MAQ: Maqu_3171
            LPN: lpg1195(hisA)
            LPF: lpl1203(hisA)
            LPP: lpp1197(hisA)
            MCA: MCA2803(hisA)
            TCX: Tcr_1968
            NOC: Noc_0258 Noc_3053
            AEH: Mlg_2615
            HHA: Hhal_1092
            HCH: HCH_01346(hisA)
            CSA: Csal_0517
            ABO: ABO_2279(hisA)
            AHA: AHA_2191(hisA)
            BCI: BCI_0400(hisA)
            RMA: Rmag_0977
            VOK: COSY_0877(hisA)
            NME: NMB0629
            NMA: NMA0839(hisA)
            NMC: NMC0573(hisA)
            NGO: NGO0212
            CVI: CV_0617(hisA)
            RSO: RSc2947(hisA)
            REU: Reut_A3106
            REH: H16_A3411(hisA)
            RME: Rmet_3243
            BMA: BMA2709(hisA)
            BMV: BMASAVP1_A3244(hisA)
            BML: BMA10299_A1793(hisA)
            BMN: BMA10247_2760(hisA)
            BXE: Bxe_A0403 Bxe_B2460(orf17)
            BUR: Bcep18194_A3528
            BCN: Bcen_2677
            BCH: Bcen2424_0430
            BAM: Bamb_0348
            BPS: BPSL3134(hisA)
            BPM: BURPS1710b_3688(hisA)
            BPL: BURPS1106A_3719(hisA)
            BPD: BURPS668_3661(hisA)
            BTE: BTH_I2988
            BPE: BP3772(hisA)
            BPA: BPP4271(hisA)
            BBR: BB4858(hisA)
            RFR: Rfer_2950
            POL: Bpro_0808
            PNA: Pnap_0700
            AAV: Aave_1034
            AJS: Ajs_0765
            VEI: Veis_4377
            MPT: Mpe_A0835
            HAR: HEAR3065(hisA)
            MMS: mma_3284(hisA)
            NEU: NE0644(hisA)
            NET: Neut_1908
            NMU: Nmul_A0815
            EBA: ebA1293(hisA)
            AZO: azo3345(hisA)
            DAR: Daro_3380
            TBD: Tbd_1709
            MFA: Mfla_0253 Mfla_1651
            HHE: HH0826(hisA)
            WSU: WS0618(hisA)
            TDN: Tmden_1673
            CJE: Cj1601(hisA)
            CJR: CJE1773(hisA)
            CJJ: CJJ81176_1588(hisA)
            CJU: C8J_1503(hisA)
            CJD: JJD26997_1956
            CFF: CFF8240_1351(hisA)
            CCV: CCV52592_1199(hisA)
            CHA: CHAB381_0946(hisA)
            CCO: CCC13826_0444(hisA)
            ABU: Abu_0473(hisA)
            NIS: NIS_1411(hisA)
            SUN: SUN_1951(hisA)
            GSU: GSU3096(hisA)
            GME: Gmet_0388
            GUR: Gura_4054
            PCA: Pcar_2685
            PPD: Ppro_3056
            DVU: DVU1038(hisA)
            DVL: Dvul_1955
            DDE: Dde_1465
            DPS: DP0005
            ADE: Adeh_0715
            MXA: MXAN_4226
            SAT: SYN_00761
            SFU: Sfum_1215
            PUB: SAR11_0330(hisA)
            MLO: mlr5014
            MES: Meso_3496
            SME: SMc02570(hisA)
            ATU: Atu0040(hisA)
            ATC: AGR_C_63
            RET: RHE_CH00043(hisA)
            RLE: RL0043(hisA)
            BME: BMEI2042
            BMF: BAB1_2085
            BMS: BR2084(hisA)
            BMB: BruAb1_2059(hisA)
            BOV: BOV_2004(hisA)
            BJA: blr0653(hisA)
            BRA: BRADO0215(hisA)
            BBT: BBta_0145(hisA)
            RPA: RPA0312(hisA)
            RPB: RPB_0408
            RPC: RPC_0307
            RPD: RPD_0412
            RPE: RPE_0367
            NWI: Nwi_0123
            NHA: Nham_0125
            CCR: CC_3736
            SIL: SPO1158(hisA) SPO2272
            SIT: TM1040_2039
            RSP: RSP_2243(hisA)
            RSH: Rsph17029_0918
            JAN: Jann_2792
            RDE: RD1_3560(hisA)
            PDE: Pden_1886
            MMR: Mmar10_1612
            HNE: HNE_0070(hisA)
            ZMO: ZMO1501(hisA)
            NAR: Saro_1009
            SAL: Sala_3147
            ELI: ELI_09560
            GOX: GOX0482
            GBE: GbCGDNIH1_0769 GbCGDNIH1_2231
            RRU: Rru_A3595
            MAG: amb4532
            MGM: Mmc1_3155
            ABA: Acid345_3688
            BSU: BG12597(hisA)
            BHA: BH3579(hisA)
            BAN: BA1429(hisA)
            BAR: GBAA1429(hisA)
            BAA: BA_1949
            BAT: BAS1320
            BCE: BC1409
            BCA: BCE_1529(hisA)
            BCZ: BCZK1294(hisA)
            BTK: BT9727_1293(hisA)
            BLI: BL03411(hisA)
            BLD: BLi03733(hisA)
            BCL: ABC3045(hisA)
            BAY: RBAM_032090(hisA)
            BPU: BPUM_3123(hisA)
            OIH: OB0548
            GKA: GK3072
            SAU: SA2466
            SAV: SAV2674
            SAM: MW2593
            SAR: SAR2756(hisA)
            SAS: SAS2559
            SAC: SACOL2698(hisA)
            SAB: SAB2550c(hisA)
            SAA: SAUSA300_2607(hisA)
            SAO: SAOUHSC_03009
            SEP: SE0275
            SER: SERP2302(hisA)
            SSP: SSP0425
            LMO: lmo0564(hisA)
            LMF: LMOf2365_0593(hisA)
            LIN: lin0573(hisA)
            LWE: lwe0530(hisA)
            LLA: L0070(hisA)
            LLC: LACR_1328
            LLM: llmg_1291(hisA)
            SMU: SMU.1265(hisA)
            SSA: SSA_1443(hisA)
            SGO: SGO_1405(hisA)
            LPL: lp_2556(hisA)
            LCA: LSEI_1430
            LME: LEUM_1551
            STH: STH2834(hisA)
            CAC: CAC0940(hisA)
            CNO: NT01CX_1065(hisA)
            CTH: Cthe_2887
            CDF: CD1552(hisA)
            CBO: CBO1570(hisA)
            CBA: CLB_1590(hisA)
            CBH: CLC_1601(hisA)
            CBF: CLI_1652(hisA)
            CBE: Cbei_1321
            CKL: CKL_1299(hisA)
            AMT: Amet_0576
            CHY: CHY_1089(hisA)
            DSY: DSY3909
            DRM: Dred_2351
            SWO: Swol_1766
            TTE: TTE2134(hisA)
            MTA: Moth_2032
            MTU: Rv1603(hisA)
            MTC: MT1639(hisA)
            MBO: Mb1629(hisA)
            MBB: BCG_1641(hisA)
            MLE: ML1261(hisA)
            MPA: MAP1297(hisA)
            CGL: NCgl2015(cgl2096)
            CGB: cg2299(hisA)
            CEF: CE1996(hisA)
            CDI: DIP1560(hisA)
            CJK: jk0791(hisA)
            NFA: nfa18500(hisA)
            RHA: RHA1_ro01024(hisA)
            SCO: SCO2050(hisA)
            SMA: SAV6158(hisA)
            LXX: Lxx15830(hisA)
            CMI: CMM_2014(hisA)
            PAC: PPA1156
            TFU: Tfu_1155
            FRA: Francci3_3023
            FAL: FRAAL4977(hisA)
            SEN: SACE_5759(hisA)
            BLO: BL1300(hisA)
            BAD: BAD_1124(hisA)
            RXY: Rxyl_1105
            RBA: RB8080(hisA)
            LIL: LA0126(hisA)
            LIC: LIC10114(hisA)
            LBJ: LBJ_0103(hisA)
            LBL: LBL_0032(hisA)
            SYN: slr0652(hisA)
            SYW: SYNW0773(hisA)
            SYC: syc2265_c(hisA)
            SYF: Synpcc7942_1829
            SYD: Syncc9605_1876
            SYE: Syncc9902_0777
            SYG: sync_1723(hisA)
            SYR: SynRCC307_1010(hisA)
            SYX: SynWH7803_1163(hisA)
            CYA: CYA_2513(hisA)
            CYB: CYB_1964(hisA)
            TEL: tll0216(hisA)
            GVI: glr0706(hisA)
            ANA: all4506(hisA)
            AVA: Ava_3372
            PMA: Pro0872(hisA)
            PMM: PMM0796(hisA)
            PMT: PMT0520(hisA)
            PMN: PMN2A_0204
            PMI: PMT9312_0804
            PMB: A9601_08601(hisA)
            PMC: P9515_07851(hisA)
            PMF: P9303_17461(hisA)
            PMG: P9301_08571(hisA)
            PMH: P9215_08911(hisA)
            PME: NATL1_08361(hisA)
            TER: Tery_3731
            BTH: BT_1379
            BFR: BF3054
            BFS: BF2890(hisA)
            SRU: SRU_1564(hisA)
            CHU: CHU_1272(hisA)
            GFO: GFO_1759(hisA)
            FPS: FP0955(hisA)
            CTE: CT0477(hisA)
            CCH: Cag_0540
            CPH: Cpha266_0492
            PVI: Cvib_1475
            PLT: Plut_1690
            DET: DET1331(hisA)
            DEH: cbdb_A1278(hisA)
            DEB: DehaBAV1_1142
            DRA: DR_2495
            DGE: Dgeo_2158
            TTH: TTC0801
            TTJ: TTHA1165
            AAE: aq_1303(hisA)
            TMA: TM1037
            MJA: MJ0703
            MMP: MMP0417(hisA) MMP1690
            MMZ: MmarC7_0997
            MAE: Maeo_0738
            MVN: Mevan_1024
            MAC: MA0218(hisA) MA4435(hisA)
            MBA: Mbar_A1100 Mbar_A1311
            MMA: MM_1113 MM_1504
            MBU: Mbur_1332 Mbur_1675
            MTP: Mthe_1506
            MHU: Mhun_0921
            MBN: Mboo_0659
            MST: Msp_0389(hisA)
            MSI: Msm_0858 Msm_1636
            MKA: MK0364(hisA)
            AFU: AF0713(hisA-1)
            HAL: VNG2294G(hisA)
            HMA: rrnAC2529(hisA)
            HWA: HQ1025A(hisA)
            NPH: NP1268A(hisA)
            PTO: PTO1333
            PFU: PF1662
            TKO: TK0247
            RCI: RCIX677(hisA-1) RRC389(hisA-2)
            SSO: SSO0594(hisA)
            STO: ST1460
            SAI: Saci_1576(hisA)
            PAI: PAE0991(hisA)
STRUCTURES  PDB: 2AGK  2CFF  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.16
            ExPASy - ENZYME nomenclature database: 5.3.1.16
            ExplorEnz - The Enzyme Database: 5.3.1.16
            ERGO genome analysis and discovery system: 5.3.1.16
            BRENDA, the Enzyme Database: 5.3.1.16
            CAS: 37318-43-7
///
ENTRY       EC 5.3.1.17                 Enzyme
NAME        4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase;
            4-deoxy-L-threo-5-hexulose uronate isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     4-deoxy-L-threo-5-hexosulose-uronate aldose-ketose-isomerase
REACTION    4-deoxy-L-threo-5-hexosulose uronate =
            3-deoxy-D-glycero-2,5-hexodiulosonate [RN:R04383]
ALL_REAC    R04383
SUBSTRATE   4-deoxy-L-threo-5-hexosulose uronate [CPD:C04053]
PRODUCT     3-deoxy-D-glycero-2,5-hexodiulosonate [CPD:C04349]
REFERENCE   1
  AUTHORS   Preiss, J.
  TITLE     4-Deoxy-L-threo-5-hexosulose uronic acid isomerase.
  JOURNAL   Methods Enzymol. 9 (1966) 602-604.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00040  Pentose and glucuronate interconversions
ORTHOLOGY   KO: K01815  4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase
GENES       ECO: b2843(kduI)
            ECJ: JW2811(kduI)
            ECE: Z4163(kduI)
            ECS: ECs3700
            ECC: c3440(kduI)
            ECI: UTI89_C3246(kduI)
            ECP: ECP_2856
            ECV: APECO1_3663(kduI)
            ECX: EcHS_A2990(kduI)
            STY: STY3163(kduI)
            STT: t2928(kduI)
            SPT: SPA2885(kduI)
            SEC: SC2957(kduI)
            STM: STM3018(kduI)
            YPE: YPO1725(kduI)
            YPK: y1887(kduI)
            YPM: YP_1750(kduI)
            YPA: YPA_1793
            YPN: YPN_1905
            YPP: YPDSF_1723
            YPS: YPTB2356(kduI)
            YPI: YpsIP31758_1694(kduI)
            YEN: YE1888(kduI)
            SFL: SF2853(kduI)
            SFX: S3051(kduI)
            SFV: SFV_2921(kduI)
            SSN: SSON_3003(kduI)
            SBO: SBO_2735(kduI)
            ECA: ECA2400(kduI1) ECA4125(kduI2)
            ENT: Ent638_3296
            XCC: XCC0151(kduI)
            XCB: XC_0160
            XCV: XCV0152(kduI)
            XAC: XAC0168(kduI)
            XOO: XOO0189(kduI)
            XOM: XOO_0167(XOO0167) XOO_0168(XOO0168)
            VFI: VFA0998
            PPR: PBPRB0148 PBPRB1731
            SDE: Sde_0950 Sde_1280
            SME: SMa0214(kduI) SMb21349
            SMD: Smed_4744
            ATU: Atu3142(kduI)
            ATC: AGR_L_3335
            RET: RHE_PE00400(ype00208)
            RLE: pRL110530
            CCR: CC_1491
            RSP: RSP_0482(kduI)
            RSH: Rsph17029_2134
            RSQ: Rsph17025_2407
            BSU: BG11401(kduI)
            BHA: BH2166(kduI)
            BCZ: pE33L466_0343(kduI)
            BLD: BLi03829(kduI)
            BCL: ABC0994(kduI)
            BPU: BPUM_3246(kduI)
            OIH: OB2813
            LBR: LVIS_0127
            LCA: LSEI_2671
            EFA: EF0425(kduI-1) EF2264(kduI-2)
            CPF: CPF_0395(kduI) CPF_0399(kduI)
            CPR: CPR_0391(kduI) CPR_0395
            CBE: Cbei_0447 Cbei_2458
            AMT: Amet_0900
            CSC: Csac_0356 Csac_2719
            KRA: Krad_0197
            BTH: BT_3231 BT_4106
            BFR: BF0071
            BFS: BF0082
            FJO: Fjoh_4264
STRUCTURES  PDB: 1X8M  1XRU  1YWK  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.17
            ExPASy - ENZYME nomenclature database: 5.3.1.17
            ExplorEnz - The Enzyme Database: 5.3.1.17
            ERGO genome analysis and discovery system: 5.3.1.17
            BRENDA, the Enzyme Database: 5.3.1.17
            CAS: 37318-44-8
///
ENTRY       EC 5.3.1.18       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
COMMENT     Deleted entry: glucose isomerase. Reaction is due to EC 5.3.1.9
            glucose-6-phosphate isomerase, in the presence of arsenate, or EC
            5.3.1.5 xylose isomerase (EC 5.3.1.18 created 1972, deleted 1978)
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.18
            ExPASy - ENZYME nomenclature database: 5.3.1.18
            ExplorEnz - The Enzyme Database: 5.3.1.18
            ERGO genome analysis and discovery system: 5.3.1.18
            BRENDA, the Enzyme Database: 5.3.1.18
///
ENTRY       EC 5.3.1.19       Obsolete  Enzyme
NAME        Transferred to 2.6.1.16
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
COMMENT     Transferred entry: now EC 2.6.1.16, glutamine-fructose-6-phosphate
            transaminase (isomerizing) (EC 5.3.1.19 created 1972, deleted 1984)
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.19
            ExPASy - ENZYME nomenclature database: 5.3.1.19
            ExplorEnz - The Enzyme Database: 5.3.1.19
            ERGO genome analysis and discovery system: 5.3.1.19
            BRENDA, the Enzyme Database: 5.3.1.19
///
ENTRY       EC 5.3.1.20                 Enzyme
NAME        ribose isomerase;
            D-ribose isomerase;
            D-ribose ketol-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     D-ribose aldose-ketose-isomerase
REACTION    D-ribose = D-ribulose [RN:R01081]
ALL_REAC    R01081
SUBSTRATE   D-ribose [CPD:C00121]
PRODUCT     D-ribulose [CPD:C00309]
COMMENT     Also acts on L-lyxose and L-rhamnose.
REFERENCE   1  [PMID:240851]
  AUTHORS   Izumori K, Rees AW, Elbein AD.
  TITLE     Purification, crystallization, and properties of D-ribose isomerase
            from Mycobacterium smegmatis.
  JOURNAL   J. Biol. Chem. 250 (1975) 8085-7.
  ORGANISM  Mycobacterium smegmatis [GN:msm]
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.20
            ExPASy - ENZYME nomenclature database: 5.3.1.20
            ExplorEnz - The Enzyme Database: 5.3.1.20
            ERGO genome analysis and discovery system: 5.3.1.20
            BRENDA, the Enzyme Database: 5.3.1.20
            CAS: 57534-76-6
///
ENTRY       EC 5.3.1.21                 Enzyme
NAME        corticosteroid side-chain-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     11-deoxycorticosterone aldose-ketose-isomerase
REACTION    11-deoxycorticosterone = 20-hydroxy-3-oxopregn-4-en-21-al
            [RN:R04165]
ALL_REAC    R04165
SUBSTRATE   11-deoxycorticosterone [CPD:C03205]
PRODUCT     20-hydroxy-3-oxopregn-4-en-21-al [CPD:C04108]
COMMENT     An epimerization at C-20 and C-21 is probably catalysed by the same
            enzyme.
REFERENCE   1  [PMID:901753]
  AUTHORS   Martin KO, Oh SW, Lee HJ, Monder C.
  TITLE     Studies on 21-3H-labeled corticosteroids: evidence for isomerization
            of the ketol side chain of 11-deoxycorticosterone by a hamster liver
            enzyme.
  JOURNAL   Biochemistry. 16 (1977) 3803-9.
  ORGANISM  hamster
REFERENCE   2  [PMID:7391077]
  AUTHORS   Monder C, Martin KO, Bogumil J.
  TITLE     Presence of epimerase activity in hamster liver corticosteroid side
            chain isomerase.
  JOURNAL   J. Biol. Chem. 255 (1980) 7192-8.
  ORGANISM  hamster
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.21
            ExPASy - ENZYME nomenclature database: 5.3.1.21
            ExplorEnz - The Enzyme Database: 5.3.1.21
            ERGO genome analysis and discovery system: 5.3.1.21
            BRENDA, the Enzyme Database: 5.3.1.21
            CAS: 75139-73-0
///
ENTRY       EC 5.3.1.22                 Enzyme
NAME        hydroxypyruvate isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     hydroxypyruvate aldose-ketose-isomerase
REACTION    hydroxypyruvate = 2-hydroxy-3-oxopropanoate [RN:R01394]
ALL_REAC    R01394
SUBSTRATE   hydroxypyruvate [CPD:C00168]
PRODUCT     2-hydroxy-3-oxopropanoate [CPD:C01146]
REFERENCE   1  [PMID:7448201]
  AUTHORS   de Windt FE, van der Drift C.
  TITLE     Purification and some properties of hydroxypyruvate isomerase of
            Bacillus fastidiosus.
  JOURNAL   Biochim. Biophys. Acta. 613 (1980) 556-62.
  ORGANISM  Bacillus fastidiosus
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K01816  hydroxypyruvate isomerase
GENES       HSA: 81888(HYI)
            MMU: 68180(Hyi)
            CFA: 482531(HYI)
            XLA: 414666(MGC81041)
            DRE: 393305(zgc:63850)
            ECO: b0508(hyi)
            ECJ: JW0496(hyi)
            ECE: Z0662(gip)
            ECS: ECs0569
            ECC: c0623(gip)
            ECI: UTI89_C0537(hyi) UTI89_C5031(gclR)
            ECP: ECP_0569
            ECV: APECO1_1506(hyi) APECO1_2096(gclR) APECO1_3785(ygbM)
            ECW: EcE24377A_0545(hyi)
            ECX: EcHS_A0582(hyi)
            STY: STY0566(gip) STY3040(hyi)
            STT: t2342(hyi) t2816(hyi)
            SPT: SPA2204(hyi)
            SEC: SC0558(gip)
            STM: STM0518(gip)
            YPM: YP_0903(hfi1)
            SFX: S0454(gip)
            SSN: SSON_0503(gip)
            PLU: plu2510
            SPE: Spro_1489
            HSO: HS_0015
            ASU: Asuc_0120
            PPR: PBPRA2274
            PAE: PA0550 PA1501
            PAU: PA14_07150(hyi) PA14_45010(hyi)
            PAP: PSPA7_3830(hyi)
            PPU: PP_4298(hyi)
            PPF: Pput_1571
            PST: PSPTO_5064
            PSB: Psyr_0462
            PSP: PSPPH_0453
            PFL: PFL_1700 PFL_3342
            PFO: Pfl_1597
            PEN: PSEEN1671(hyi)
            PMY: Pmen_2770 Pmen_3195
            ACI: ACIAD3075(hyi)
            MAQ: Maqu_3741
            HCH: HCH_00577(gip)
            CSA: Csal_3181
            ABO: ABO_1233(hyi)
            MMW: Mmwyl1_2552
            RSO: RSc0020(RS01842) RSc3282(hyi)
            REU: Reut_A1423 Reut_A3292
            REH: H16_A1558(hyi1) H16_A3599(hyi2)
            RME: Rmet_1839 Rmet_3449
            BMA: BMAA0573(hyi)
            BML: BMA10299_0894(hyi)
            BMN: BMA10247_A1861(hyi)
            BXE: Bxe_A2461 Bxe_B2169 Bxe_C0958
            BVI: Bcep1808_1803 Bcep1808_3462
            BUR: Bcep18194_A5179 Bcep18194_B0474
            BCN: Bcen_3208 Bcen_6200
            BCH: Bcen2424_1879 Bcen2424_5159
            BAM: Bamb_1816 Bamb_4554
            BPS: BPSL1451(hyi) BPSS1419(hyi)
            BPM: BURPS1710b_2425(hyi) BURPS1710b_A0442(hyi)
            BPL: BURPS1106A_2300 BURPS1106A_A1924(hyi)
            BPD: BURPS668_2260
            BTE: BTH_I2172(hyi) BTH_II0973
            PNU: Pnuc_1567 Pnuc_1631
            RFR: Rfer_0443
            POL: Bpro_4562 Bpro_4876
            PNA: Pnap_4098
            AJS: Ajs_1815
            VEI: Veis_2462
            MPT: Mpe_A3533
            HAR: HEAR0333(hyi)
            MMS: mma_0380(gip)
            EBA: ebA4617(hfi)
            AZO: azo1163(gip)
            DAR: Daro_3317
            MLO: mlr0252
            SME: SMb20669 SMb20680(hyi)
            SMD: Smed_4309 Smed_4320 Smed_5560
            RET: RHE_CH02358 RHE_CH03366(ypch01180) RHE_PF00346(ypf00177)
            RLE: RL3792 RL3799 pRL110149 pRL120615
            BME: BMEII1092
            BMF: BAB2_0144
            BMS: BRA0147
            BMB: BruAb2_0143
            OAN: Oant_0459
            BJA: blr2929 blr3167(hyi)
            BRA: BRADO4945(hyi)
            RPA: RPA1753
            RPB: RPB_3611
            RPD: RPD_1855
            RPE: RPE_1699
            XAU: Xaut_1026 Xaut_2368
            SIL: SPO2563
            SIT: TM1040_2765
            RDE: RD1_0350 RD1_3783
            PDE: Pden_3899 Pden_5018
            SWI: Swit_3267
            GBE: GbCGDNIH1_0973
            ACR: Acry_1158 Acry_2430
            RRU: Rru_A2503
            GKA: GK1528
            DSY: DSY4167
            MSM: MSMEG_5478
            CGL: NCgl2384(cgl2471)
            CGB: cg2312(gip) cg2716(hyi)
            CEF: CE2368
            CJK: jk1284
            RHA: RHA1_ro02576 RHA1_ro03225 RHA1_ro05268
            SCO: SCO6206(SC2G5.27c)
            SMA: SAV2024(gip)
            KRA: Krad_2140
            RXY: Rxyl_2851
            RBA: RB8188
            DGE: Dgeo_2613
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.22
            ExPASy - ENZYME nomenclature database: 5.3.1.22
            ExplorEnz - The Enzyme Database: 5.3.1.22
            ERGO genome analysis and discovery system: 5.3.1.22
            BRENDA, the Enzyme Database: 5.3.1.22
            CAS: 74812-48-9
///
ENTRY       EC 5.3.1.23                 Enzyme
NAME        S-methyl-5-thioribose-1-phosphate isomerase;
            methylthioribose 1-phosphate isomerase;
            1-PMTR isomerase;
            5-methylthio-5-deoxy-D-ribose-1-phosphate ketol-isomerase;
            S-methyl-5-thio-5-deoxy-D-ribose-1-phosphate ketol-isomerase;
            S-methyl-5-thio-5-deoxy-D-ribose-1-phosphate
            aldose-ketose-isomerase;
            1-phospho-5'-S-methylthioribose isomerase;
            S-methyl-5-thio-D-ribose-1-phosphate aldose-ketose-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     S-methyl-5-thio-alpha-D-ribose-1-phosphate aldose-ketose-isomerase
REACTION    S-methyl-5-thio-alpha-D-ribose 1-phosphate =
            S-methyl-5-thio-D-ribulose 1-phosphate [RN:R04420]
ALL_REAC    R04420
SUBSTRATE   S-methyl-5-thio-alpha-D-ribose 1-phosphate [CPD:C04188]
PRODUCT     S-methyl-5-thio-D-ribulose 1-phosphate [CPD:C04582]
REFERENCE   1  [PMID:6725268]
  AUTHORS   Ghoda LY, Savarese TM, Dexter DL, Parks RE Jr, Trackman PC, Abeles
            RH.
  TITLE     Characterization of a defect in the pathway for converting
            5'-deoxy-5'-methylthioadenosine to methionine in a subline of a
            cultured heterogeneous human colon carcinoma.
  JOURNAL   J. Biol. Chem. 259 (1984) 6715-9.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:6853500]
  AUTHORS   Trackman PC, Abeles RH.
  TITLE     Methionine synthesis from 5'-S-Methylthioadenosine. Resolution of
            enzyme activities and identification of 1-phospho-5-S
            methylthioribulose.
  JOURNAL   J. Biol. Chem. 258 (1983) 6717-20.
  ORGANISM  rat [GN:rno]
REFERENCE   3  [PMID:2838472]
  AUTHORS   Furfine ES, Abeles RH.
  TITLE     Intermediates in the conversion of 5'-S-methylthioadenosine to
            methionine in Klebsiella pneumoniae.
  JOURNAL   J. Biol. Chem. 263 (1988) 9598-606.
  ORGANISM  Klebsiella pneumoniae
PATHWAY     PATH: map00271  Methionine metabolism
ORTHOLOGY   KO: K08963  methylthioribose-1-phosphate isomerase
GENES       SCE: YPR118W(MRI1)
            TET: TTHERM_00787070
            YPP: YPDSF_2879
            YPS: YPTB0877(eif)
            ECA: ECA3477
            ENT: Ent638_1140
            SPE: Spro_0945
            XFA: XF2553
            XFT: PD1936
            XCC: XCC1573
            XCB: XC_2661
            XCV: XCV1671(gcn3)
            XAC: XAC1630
            XOO: XOO2407
            XOM: XOO_2285(XOO2285)
            PAE: PA3169
            PPU: PP_1766
            PPF: Pput_3948
            PST: PSPTO_1744
            PSB: Psyr_3648
            PSP: PSPPH_3668
            PFL: PFL_4315
            PFO: Pfl_4079
            PEN: PSEEN1486
            PMY: Pmen_1847
            MAQ: Maqu_2493
            MCA: MCA1974
            NOC: Noc_2293
            AEH: Mlg_0913
            HHA: Hhal_0573
            HCH: HCH_04355
            ABO: ABO_1444(eif)
            RFR: Rfer_3749
            EBA: ebA3889
            DAR: Daro_3335
            MFA: Mfla_1913
            TDN: Tmden_1971
            GSU: GSU3379
            GME: Gmet_0072
            GUR: Gura_4322
            PCA: Pcar_2170
            PPD: Ppro_0510
            DVU: DVU0084
            DVL: Dvul_2877
            DDE: Dde_0076
            ADE: Adeh_4186
            AFW: Anae109_4334
            MXA: MXAN_6385
            SAT: SYN_00310
            SFU: Sfum_1706
            MLO: mll7284
            PLA: Plav_2247
            SME: SMb20624
            SMD: Smed_5890
            OAN: Oant_4832
            BJA: blr0961
            BRA: BRADO6903(mtnA)
            BBT: BBta_0648(mtnA)
            RPA: RPA4820(eIF-2B)
            RPB: RPB_4697
            RPC: RPC_4936
            RPD: RPD_4407
            RPE: RPE_4906
            RSP: RSP_2386
            RSH: Rsph17029_1050
            RSQ: Rsph17025_1886
            RDE: RD1_2384
            GOX: GOX1605
            ACR: Acry_0161
            RRU: Rru_A0360
            MAG: amb4123
            MGM: Mmc1_1944
            ABA: Acid345_1175
            SUS: Acid_1486
            BSU: BG13278(mtnS)
            BAN: BA0347 BA4251
            BAR: GBAA0347 GBAA4251
            BAA: BA_0918 BA_4710
            BAT: BAS0332 BAS3942
            BCE: BC0379 BC4032
            BCA: BCE_4098
            BCZ: BCZK0319 BCZK3789
            BCY: Bcer98_2731
            BTK: BT9727_0316 BT9727_3774
            BTL: BALH_0338
            BLI: BL03632(mtnS)
            BLD: BLi01511(ykrS)
            BAY: RBAM_013330
            GKA: GK0949
            STH: STH2068 STH816
            CTC: CTC00945
            CTH: Cthe_0621
            CBO: CBO1268(mtnA)
            CBA: CLB_1296(mtnA)
            CBH: CLC_1306(mtnA)
            CBF: CLI_1353(mtnA)
            AMT: Amet_3757
            CHY: CHY_1556
            DSY: DSY2603
            DRM: Dred_1773 Dred_2064
            SWO: Swol_0779
            CSC: Csac_1923
            TTE: TTE1590(gcn3)
            MTA: Moth_0703
            NFA: nfa45440
            SCO: SCO3014(SCE33.16c)
            SMA: SAV5062(eif1) SAV6658(eif2)
            NCA: Noca_0403
            FAL: FRAAL1411(mtnA)
            SEN: SACE_3608(gcn3)
            FNU: FN1413
            RBA: RB10264(eIF-2B)
            TDE: TDE1667
            LIL: LA2868(infB2)
            LIC: LIC11175(eif)
            LBJ: LBJ_2026
            LBL: LBL_1024
            SYN: slr1938
            SYW: SYNW1962(eIF2B)
            SYC: syc2104_d(eIF2BA)
            SYF: Synpcc7942_1992
            SYD: Syncc9605_0491
            SYE: Syncc9902_1844
            SYG: sync_2476
            TEL: tll1061
            GVI: gll0195
            ANA: all3566
            AVA: Ava_3544
            PMT: PMT1901
            TER: Tery_2078
            CTE: CT1816
            CCH: Cag_1355
            CPH: Cpha266_0701
            PVI: Cvib_0532
            PLT: Plut_0476
            DET: DET0518
            DEH: cbdb_A484
            DEB: DehaBAV1_0494
            RRS: RoseRS_0485
            RCA: Rcas_0156
            TTH: TTC0707
            TTJ: TTHA1072
            AAE: aq_2114(eif)
            TMA: TM0911
            TPT: Tpet_0016
            TME: Tmel_0254
            FNO: Fnod_1519
            MMQ: MmarC5_1791
            MMZ: MmarC7_0865
            MAE: Maeo_0027 Maeo_0673
            MVN: Mevan_0927
            MAC: MA0076(eif2B1)
            MBA: Mbar_A1041
            MMA: MM_1371
            MBU: Mbur_1938 Mbur_2118
            MTP: Mthe_0365 Mthe_1262
            MHU: Mhun_0623 Mhun_2314
            MLA: Mlab_0017
            MEM: Memar_1694 Memar_2067
            MBN: Mboo_1840 Mboo_2432
            AFU: AF0370(eif2BD)
            SMR: Smar_0989 Smar_1357
            IHO: Igni_0519
            HBU: Hbut_0956
            MSE: Msed_2269
            PIS: Pisl_0663
            PCL: Pcal_2173
            PAS: Pars_0008
            TPE: Tpen_0246 Tpen_0384
STRUCTURES  PDB: 1T9K  1W2W  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.23
            ExPASy - ENZYME nomenclature database: 5.3.1.23
            ExplorEnz - The Enzyme Database: 5.3.1.23
            ERGO genome analysis and discovery system: 5.3.1.23
            BRENDA, the Enzyme Database: 5.3.1.23
            CAS: 91608-95-6
///
ENTRY       EC 5.3.1.24                 Enzyme
NAME        phosphoribosylanthranilate isomerase;
            PRA isomerase;
            PRAI;
            IGPS:PRAI (indole-3-glycerol-phosphate
            synthetase/N-5'-phosphoribosylanthranilate isomerase complex);
            N-(5-phospho-beta-D-ribosyl)anthranilate ketol-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     N-(5-phospho-beta-D-ribosyl)anthranilate aldose-ketose-isomerase
REACTION    N-(5-phospho-beta-D-ribosyl)anthranilate =
            1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate [RN:R03509]
ALL_REAC    R03509
SUBSTRATE   N-(5-phospho-beta-D-ribosyl)anthranilate [CPD:C04302]
PRODUCT     1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
COMMENT     In some organisms, this enzyme is part of a multifunctional protein,
            together with one or more other components of the system for the
            biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate
            phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate
            synthase), EC 4.1.3.27 (anthranilate synthase) and EC 4.2.1.20
            (tryptophan synthase)].
REFERENCE   1  [PMID:3286643]
  AUTHORS   Braus GH, Luger K, Paravicini G, Schmidheini T, Kirschner K, Hutter
            R.
  TITLE     The role of the TRP1 gene in yeast tryptophan biosynthesis.
  JOURNAL   J. Biol. Chem. 263 (1988) 7868-75.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2
  AUTHORS   Creighton, T.E. and Yanofsky, C.
  TITLE     Chorismate to tryptophan (Escherichia coli) - Anthranilate
            synthetase, PR transferase, PRA isomerase, InGP synthetase,
            tryptophan synthetase.
  JOURNAL   Methods Enzymol. 17A (1970) 365-380.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:16526091]
  AUTHORS   Kung CC, Huang WN, Huang YC, Yeh KC.
  TITLE     Proteomic survey of copper-binding proteins in Arabidopsis roots by
            immobilized metal affinity chromatography and mass spectrometry.
  JOURNAL   Proteomics. 6 (2006) 2746-58.
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K01817  phosphoribosylanthranilate isomerase
GENES       SCE: YDR007W(TRP1)
            AGO: AGOS_AER014W
            PIC: PICST_38245(TRP1)
            CGR: CAGL0C04092g(TRPF_CANGA)
            SPO: SPBC1539.09c(trp1)
            AFM: AFUA_1G13090
            AOR: AO090012000581
            ANG: An08g06080(trpC)
            CNE: CNI00560
            UMA: UM02376.1
            ECO: b1262(trpC)
            ECJ: JW1254(trpC)
            ECE: Z2549(trpC)
            ECS: ECs1834
            ECI: UTI89_C1531(trpC)
            ECP: ECP_1310
            ECV: APECO1_423(trpC)
            ECW: EcE24377A_1461(trpC)
            ECX: EcHS_A1371(trpC)
            STY: STY1326(trpC)
            STT: t1637(trpC)
            SPT: SPA1152(trpC)
            SEC: SC1721(trpC)
            STM: STM1725(trpC)
            YPE: YPO2205(trpC)
            YPK: y2049(trpC)
            YPM: YP_2003(trpC)
            YPA: YPA_1565
            YPN: YPN_1674
            YPP: YPDSF_0928
            YPS: YPTB2127(trpC)
            YPI: YpsIP31758_1935(trpC)
            SFL: SF1265(trpC)
            SFX: S1351(trpC)
            SFV: SFV_1276(trpC)
            SSN: SSON_1881(trpC)
            SBO: SBO_1804(trpC)
            SDY: SDY_1330(trpC)
            ECA: ECA2299(trpC)
            PLU: plu2465(trpC)
            BUC: BU279(trpC)
            BAS: BUsg268(trpC)
            BAB: bbp259(trpC)
            SGL: SG1399
            ENT: Ent638_2206
            KPN: KPN_01255(trpC)
            SPE: Spro_2670
            BFL: Bfl429(trpC)
            BPN: BPEN_441(trpC)
            HIN: HI1389.1(trpC)
            HIT: NTHI1763(trpC)
            HIP: CGSHiEE_04515
            HIQ: CGSHiGG_00715
            PMU: PM0580(trpC)
            MSU: MS1152(trpC)
            APL: APL_0859(trpCF)
            ASU: Asuc_1269
            XFA: XF1374
            XFT: PD0611(trpF)
            XCC: XCC2545(trpF)
            XCB: XC_1573
            XCV: XCV2871(trpF)
            XAC: XAC2719(trpF)
            XOO: XOO3254(trpF)
            XOM: XOO_3082(XOO3082)
            VCH: VC1171
            VVU: VV1_3067
            VVY: VV1218
            VPA: VP1959(trpF)
            VFI: VF1029(trpC)
            PPR: PBPRA2489(trpC)
            PAE: PA3113(trpF)
            PAU: PA14_23850(trpF)
            PPU: PP_1995(trpF)
            PPF: Pput_3766
            PST: PSPTO_3816(trpF)
            PSB: Psyr_1663
            PSP: PSPPH_1657(trpF)
            PFL: PFL_2072(trpF)
            PFO: Pfl_1897
            PEN: PSEEN1690(trpF)
            PMY: Pmen_2716
            PAR: Psyc_0431
            PCR: Pcryo_0466
            PRW: PsycPRwf_0754
            ACI: ACIAD0635(trpF)
            SON: SO_3022(trpC)
            SDN: Sden_2453
            SFR: Sfri_1426
            SAZ: Sama_2132
            SBL: Sbal_2704
            SBM: Shew185_2725
            SLO: Shew_2254
            SPC: Sputcn32_2406
            SSE: Ssed_1683
            SPL: Spea_1587
            SHE: Shewmr4_1459
            SHM: Shewmr7_1525
            SHN: Shewana3_1517
            SHW: Sputw3181_1602
            ILO: IL1754(trpC)
            CPS: CPS_3525(trpC)
            PHA: PSHAa1290(trpCF)
            PAT: Patl_2832
            SDE: Sde_2080
            PIN: Ping_1057
            MAQ: Maqu_1559
            CBD: COXBU7E912_1253(trpBF)
            LPN: lpg1303(trpF)
            LPF: lpl1266(trpF)
            LPP: lpp1267(trpF)
            MCA: MCA2496(trpF)
            FTU: FTT1795c(trpC)
            FTF: FTF1795c(trpC)
            FTW: FTW_2017(trpCF)
            FTL: FTL_1958
            FTH: FTH_1875(trpC)
            FTA: FTA_2071
            FTN: FTN_1770
            TCX: Tcr_0802
            NOC: Noc_1019
            AEH: Mlg_1235
            HHA: Hhal_1805
            HCH: HCH_02435(trpF)
            CSA: Csal_1260
            ABO: ABO_1462(trpF)
            MMW: Mmwyl1_2041
            AHA: AHA_2926(trpCF)
            RMA: Rmag_1032
            VOK: COSY_0934(trpF)
            NME: NMB0688
            NMA: NMA0890(trpF)
            NMC: NMC0639(trpF)
            NGO: NGO0261
            CVI: CV_2763(trpF)
            RSO: RSc1984(trpF)
            REU: Reut_A2307
            REH: H16_A2615(trpF)
            RME: Rmet_2468
            BMA: BMAA1722(trpF)
            BMV: BMASAVP1_1648(trpF)
            BML: BMA10299_1857(trpF)
            BMN: BMA10247_A0528(trpF)
            BXE: Bxe_B2882
            BVI: Bcep1808_4461
            BUR: Bcep18194_B2126
            BCN: Bcen_4410
            BCH: Bcen2424_3957
            BAM: Bamb_3347
            BPS: BPSS1700(trpF)
            BPM: BURPS1710b_A0770(trpF)
            BPL: BURPS1106A_A2308(hscA)
            BPD: BURPS668_A2446(hscA)
            BTE: BTH_II0678
            PNU: Pnuc_0771
            BPE: BP1490(trpF)
            BPA: BPP1951(trpF)
            BBR: BB2139(trpF)
            RFR: Rfer_1789
            POL: Bpro_3615
            PNA: Pnap_3045
            AAV: Aave_1216
            AJS: Ajs_3238
            VEI: Veis_4869
            MPT: Mpe_A2158
            HAR: HEAR1222(trpF)
            MMS: mma_2165(trpF)
            NEU: NE0692(trpF)
            NET: Neut_1151
            NMU: Nmul_A1913
            EBA: ebB163(trpF)
            AZO: azo1046(trpF)
            DAR: Daro_0869
            TBD: Tbd_1915
            MFA: Mfla_1699
            HPY: HP1279(trpC)
            HPJ: jhp1200(trpC)
            HPA: HPAG1_1233
            HHE: HH0002(trpC)
            HAC: Hac_0015(trpC)
            WSU: WS0220(trpF)
            TDN: Tmden_1606
            CJE: Cj0347(trpF)
            CJR: CJE0396(trpF)
            CJJ: CJJ81176_0371(trpF)
            CJU: C8J_0324(trpF)
            CJD: JJD26997_1612(trpF)
            CFF: CFF8240_0352(trpF)
            CCV: CCV52592_1685(trpF)
            CHA: CHAB381_1273(trpF)
            CCO: CCC13826_0970(trpF)
            ABU: Abu_0859(trpF)
            NIS: NIS_0321(trpF)
            SUN: SUN_2155
            GSU: GSU2378(trpF)
            GME: Gmet_2492
            GUR: Gura_1736
            PCA: Pcar_0734
            PPD: Ppro_1292
            DVU: DVU0469(trpF-1) DVU2492(trpF-2)
            DVL: Dvul_0752 Dvul_2468
            DDE: Dde_1054 Dde_3480
            LIP: LI0412(trpF)
            DPS: DP1623
            ADE: Adeh_4056
            AFW: Anae109_0372
            MXA: MXAN_6064(trpF)
            SAT: SYN_01943 SYN_02481 SYN_02592
            SFU: Sfum_1772
            PUB: SAR11_0489(trpF)
            MLO: mlr5070
            MES: Meso_0667
            PLA: Plav_0144
            SME: SMc02767(trpF)
            SMD: Smed_3236
            ATU: Atu0017(trpF)
            ATC: AGR_C_26
            RET: RHE_CH00020(trpF)
            RLE: RL0020
            BME: BMEI2017
            BMF: BAB1_2113(trpF)
            BMS: BR2111(trpF)
            BMB: BruAb1_2086(trpF)
            BOV: BOV_2027(trpF)
            OAN: Oant_0809
            BJA: bll8013 blr0744(trpF)
            BRA: BRADO0092(trpF)
            BBT: BBta_0098(trpF)
            RPA: RPA0068(trpF)
            RPB: RPB_0636
            RPC: RPC_0393
            RPD: RPD_0196
            RPE: RPE_0453
            NWI: Nwi_0056
            NHA: Nham_0064
            XAU: Xaut_1692
            CCR: CC_3545
            SIL: SPO0806(trpF)
            SIT: TM1040_0204
            RSP: RSP_3587
            RSH: Rsph17029_3272
            JAN: Jann_3587
            RDE: RD1_3907(trpF)
            PDE: Pden_3789
            MMR: Mmar10_0094
            HNE: HNE_3477(trpF)
            ZMO: ZMO0586(trpF)
            NAR: Saro_1304
            SAL: Sala_1065
            SWI: Swit_2725
            ELI: ELI_07585
            GOX: GOX2234
            GBE: GbCGDNIH1_2017
            ACR: Acry_1722
            RRU: Rru_A3425
            MAG: amb4001
            MGM: Mmc1_2331
            ABA: Acid345_1157
            SUS: Acid_7889
            BSU: BG10289(trpF)
            BHA: BH1662(trpF)
            BAN: BA1252(trpF)
            BAR: GBAA1252(trpF)
            BAA: BA_1785
            BAT: BAS1160
            BCE: BC1236
            BCA: BCE_1360(trpF)
            BCZ: BCZK1134(trpF)
            BTK: BT9727_1140(trpF)
            BLI: BL02772(trpF)
            BLD: BLi02400(trpF)
            BCL: ABC1898(trpF)
            BAY: RBAM_020810(trpF)
            BPU: BPUM_1996(trpF)
            OIH: OB0523
            GKA: GK2201(trpF)
            SAU: SA1203(trpF)
            SAV: SAV1371(trpF)
            SAM: MW1258(trpF)
            SAR: SAR1384(trpF)
            SAS: SAS1311
            SAC: SACOL1407(trpF)
            SAB: SAB1226(trpF)
            SAA: SAUSA300_1266(trpF)
            SAO: SAOUHSC_01370
            SAJ: SaurJH9_1432
            SAH: SaurJH1_1461
            SEP: SE1052
            SER: SERP0941(trpF)
            SHA: SH1538(trpF)
            SSP: SSP1375
            LMO: lmo1629(trpF)
            LMF: LMOf2365_1651(trpF)
            LIN: lin1670(trpF)
            LWE: lwe1645(trpF)
            LLA: L0050(trpF)
            LLC: LACR_1551
            LLM: llmg_1039(trpF)
            SPN: SP_1813
            SPR: spr1633(trpF)
            SPD: SPD_1598(trpF)
            SMU: SMU.536(trpF)
            STC: str1589(trpF)
            STL: stu1589(trpF)
            SSA: SSA_0636(trpF)
            SGO: SGO_0661(trpF) SGO_1194
            LPL: lp_1656(trpF)
            LSA: LSA0255
            LCA: LSEI_0076
            STH: STH1413
            CAC: CAC3159(trpF)
            CTH: Cthe_0871
            CBE: Cbei_1753
            CKL: CKL_1278(trpF)
            AMT: Amet_1081
            CHY: CHY_1583(trpF)
            DSY: DSY3198
            DRM: Dred_0252
            SWO: Swol_0360
            CSC: Csac_2232
            TTE: TTE1579(trpF)
            MTA: Moth_1338
            MTU: Rv1603(hisA)
            MTC: MT1639(hisA)
            MBO: Mb1629(hisA)
            MLE: ML1261(hisA)
            MPA: MAP1297(hisA)
            MVA: Mvan_2808
            MGI: Mflv_3609
            MMC: Mmcs_3059
            MKM: Mkms_3118
            MJL: Mjls_3075
            CGL: NCgl2930(trpC)
            CGB: cg3362(trpCF)
            CEF: CE2871(trpC)
            CJK: jk0791(hisA)
            NFA: nfa18500(hisA)
            RHA: RHA1_ro05141(trpF)
            SCO: SCO2050(hisA)
            SMA: SAV6158(hisA)
            ART: Arth_1473 Arth_3759
            AAU: AAur_3542(trpF)
            NCA: Noca_3040
            TFU: Tfu_1155
            FRA: Francci3_3023
            FAL: FRAAL4977(hisA)
            ACE: Acel_1062
            KRA: Krad_3173
            SEN: SACE_5759(hisA)
            STP: Strop_3190
            RXY: Rxyl_2091
            RBA: RB8913(trpF)
            CTR: CT327(trpC)
            CTA: CTA_0354(trpC)
            CMU: TC0603
            CCA: CCA00565(trpF)
            CFE: CF0437(trpF)
            LIL: LA2147(trpF)
            LIC: LIC11773(trpF)
            LBJ: LBJ_1866(trpF)
            LBL: LBL_1418(trpF)
            SYN: sll0356(trpF)
            SYW: SYNW1733(trpF)
            SYC: syc1108_c(trpF)
            SYF: Synpcc7942_0408
            SYD: Syncc9605_0733
            SYE: Syncc9902_1630
            SYG: sync_1984(trpF)
            SYR: SynRCC307_1580(trpF)
            SYX: SynWH7803_0660(trpF)
            CYA: CYA_0771(trpF)
            CYB: CYB_0194(trpF)
            TEL: tll2272(trpF)
            GVI: gll0754(trpF)
            ANA: all5288
            AVA: Ava_2538
            PMA: Pro0538(trpF)
            PMM: PMM0537(trpF)
            PMT: PMT1226(trpF)
            PMN: PMN2A_1867
            PMI: PMT9312_0537
            PMB: A9601_05931(trpF)
            PMC: P9515_06011(trpF)
            PMF: P9303_07861(trpF)
            PMG: P9301_05631(trpF)
            PME: NATL1_05921(trpF)
            TER: Tery_3920
            BTH: BT_0528
            BFR: BF2655
            BFS: BF2677(trpF)
            SRU: SRU_1668(trpF)
            CHU: CHU_3294(trpF)
            GFO: GFO_2672(trpF)
            FJO: Fjoh_4895
            FPS: FP0509(trpF)
            CTE: CT0718(trpF)
            CCH: Cag_1549
            CPH: Cpha266_0920
            PVI: Cvib_1123
            PLT: Plut_0670
            DET: DET1485(trpF)
            DEH: cbdb_A1447(trpF)
            DEB: DehaBAV1_1275
            RRS: RoseRS_3444
            RCA: Rcas_4413
            DRA: DR_0123
            DGE: Dgeo_2266
            TTH: TTC1929
            TTJ: TTHA0076
            AAE: aq_2076(trpF)
            TMA: TM0139
            TPT: Tpet_0786
            MMP: MMP1004(trpF)
            MMQ: MmarC5_0590
            MMZ: MmarC7_0246
            MAE: Maeo_1119
            MVN: Mevan_0329
            MAC: MA2988(trpF)
            MBA: Mbar_A3625
            MMA: MM_2819 MM_3314
            MBU: Mbur_2364
            MTP: Mthe_1540
            MLA: Mlab_0932
            MEM: Memar_0075 Memar_2017
            MBN: Mboo_0224
            MST: Msp_1073(trpF)
            MKA: MK0508(trpF)
            AFU: AF1601(trpF)
            HAL: VNG1648G(trpF)
            HMA: rrnAC1519(trpF)
            HWA: HQ3168A(trpF)
            NPH: NP3340A(trpF)
            TAC: Ta0805m
            TVO: TVN1025
            PTO: PTO0343
            PAB: PAB2047(trpF)
            PFU: PF1707
            TKO: TK0256
            RCI: RCIX795(trpF)
            APE: APE_2547
            SSO: SSO0892(trpF)
            STO: ST1230
            SAI: Saci_1424(trpF)
            PAI: PAE2499
            PIS: Pisl_1918
            PAS: Pars_1415
STRUCTURES  PDB: 1DL3  1LBM  1NSJ  1V5X  1VZW  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.24
            ExPASy - ENZYME nomenclature database: 5.3.1.24
            ExplorEnz - The Enzyme Database: 5.3.1.24
            ERGO genome analysis and discovery system: 5.3.1.24
            BRENDA, the Enzyme Database: 5.3.1.24
            CAS: 37259-82-8
///
ENTRY       EC 5.3.1.25                 Enzyme
NAME        L-fucose isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     L-fucose aldose-ketose-isomerase
REACTION    L-fucose = L-fuculose [RN:R03163]
ALL_REAC    R03163
SUBSTRATE   L-fucose [CPD:C01019]
PRODUCT     L-fuculose [CPD:C01721]
REFERENCE   1  [PMID:2664711]
  AUTHORS   Lu Z, Lin EC.
  TITLE     The nucleotide sequence of Escherichia coli genes for L-fucose
            dissimilation.
  JOURNAL   Nucleic. Acids. Res. 17 (1989) 4883-4.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K01818  L-fucose isomerase
GENES       ECO: b2802(fucI)
            ECJ: JW2773(fucI)
            ECE: Z4119(fucI)
            ECS: ECs3662
            ECC: c3371(fucI)
            ECI: UTI89_C3174(fucI)
            ECP: ECP_2785
            ECV: APECO1_3729(fucI)
            ECW: EcE24377A_3107(fucI)
            ECX: EcHS_A2946(fucI)
            STY: STY3116(fucI)
            STT: t2884(fucI)
            SPT: SPA2840(fucI)
            SEC: SC2916(fucI)
            STM: STM2976(fucI)
            SFL: SF2816(fucI)
            SFX: S3011(fucI)
            SFV: SFV_2881(fucI)
            SBO: SBO_2685(fucI)
            SDY: SDY_3020(fucI)
            SGL: SG0181
            HIT: NTHI0871(fucI)
            HIP: CGSHiEE_02055(fucI)
            HIQ: CGSHiGG_07025(fucI)
            HSO: HS_1448(fucI)
            APL: APL_1684(fucI)
            VVY: VV2179
            SPN: SP_2158
            SPR: spr1964(fucI)
            SPD: SPD_1986(fucI)
            CPE: CPE0318(fucI)
            CPF: CPF_1048(fucI)
            CSC: Csac_1339
            PAC: PPA0608 PPA0609
            SEN: SACE_0948
            RXY: Rxyl_0832
            BTH: BT_1273
            BFR: BF0253
            BFS: BF0211(fucI)
            TMA: TM0307
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.25
            ExPASy - ENZYME nomenclature database: 5.3.1.25
            ExplorEnz - The Enzyme Database: 5.3.1.25
            ERGO genome analysis and discovery system: 5.3.1.25
            BRENDA, the Enzyme Database: 5.3.1.25
            CAS: 60063-83-4
///
ENTRY       EC 5.3.1.26                 Enzyme
NAME        galactose-6-phosphate isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
SYSNAME     D-galactose-6-phosphate aldose-ketose-isomerase
REACTION    D-galactose 6-phosphate = D-tagatose 6-phosphate [RN:R03240]
ALL_REAC    R03240
SUBSTRATE   D-galactose 6-phosphate [CPD:C01113]
PRODUCT     D-tagatose 6-phosphate [CPD:C01097]
COMMENT     Involved in the tagatose 6-phosphate pathway of lactose catabolism
            in bacteria.
REFERENCE   1  [PMID:2125052]
  AUTHORS   de Vos WM, Boerrigter I, van Rooyen RJ, Reiche B, Hengstenberg W.
  TITLE     Characterization of the lactose-specific enzymes of the
            phosphotransferase system in Lactococcus lactis.
  JOURNAL   J. Biol. Chem. 265 (1990) 22554-60.
  ORGANISM  Lactococcus lactis
REFERENCE   2  [PMID:1901863]
  AUTHORS   van Rooijen RJ, van Schalkwijk S, de Vos WM.
  TITLE     Molecular cloning, characterization, and nucleotide sequence of the
            tagatose 6-phosphate pathway gene cluster of the lactose operon of
            Lactococcus lactis.
  JOURNAL   J. Biol. Chem. 266 (1991) 7176-81.
  ORGANISM  Lactococcus lactis
PATHWAY     PATH: map00052  Galactose metabolism
ORTHOLOGY   KO: K01819  galactose-6-phosphate isomerase
GENES       SGL: SG1887
            GUR: Gura_1880
            AFW: Anae109_2734
            SMD: Smed_3746
            SWI: Swit_1130
            RRU: Rru_A1334 Rru_A1359 Rru_A1828
            SAU: SA1996(lacB) SA1997(lacA)
            SAV: SAV2194(lacB) SAV2195(lacA)
            SAM: MW2120(lacB) MW2121(lacA)
            SAR: SAR2285(lacB) SAR2286(lacA)
            SAS: SAS2095 SAS2096
            SAC: SACOL2185(lacB) SACOL2186
            SAB: SAB2075c(lacB) SAB2076c(lacA)
            SAA: SAUSA300_2154(lacB) SAUSA300_2155(lacA)
            SAO: SAOUHSC_02454 SAOUHSC_02455
            SAJ: SaurJH9_2225 SaurJH9_2226
            SAH: SaurJH1_2264 SaurJH1_2265
            SEP: SE1786 SE1787
            SER: SERP1794(lacB) SERP1795(lacA)
            SHA: SH0842(lacA)
            LLC: LACR_D05 LACR_D06
            SPY: SPy_1707(lacB.1) SPy_1708(lacA.1) SPy_1922(lacB.2)
                 SPy_1923(lacA.2)
            SPZ: M5005_Spy_0525 M5005_Spy_1397(lacB.1) M5005_Spy_1398(lacA.1)
                 M5005_Spy_1637(lacB.2) M5005_Spy_1638(lacA.2)
            SPM: spyM18_1716 spyM18_1717 spyM18_1990 spyM18_1991
            SPG: SpyM3_1484(lacB.1) SpyM3_1485(lacA.1) SpyM3_1658(lacB.2)
                 SpyM3_1659(lacA.2)
            SPS: SPs0382 SPs0383 SPs1656 SPs1657
            SPH: MGAS10270_Spy0520 MGAS10270_Spy1518(lacB1)
                 MGAS10270_Spy1519(lacA1) MGAS10270_Spy1706(lacB2)
                 MGAS10270_Spy1707(lacA2)
            SPI: MGAS10750_Spy0544 MGAS10750_Spy1510(lacB1)
                 MGAS10750_Spy1511(lacA1) MGAS10750_Spy1734(lacB2)
                 MGAS10750_Spy1735(lacA2)
            SPJ: MGAS2096_Spy0537 MGAS2096_Spy1422(lacB1)
                 MGAS2096_Spy1423(lacA1) MGAS2096_Spy1662(lacB2)
                 MGAS2096_Spy1663(lacA2)
            SPK: MGAS9429_Spy0516 MGAS9429_Spy1399 MGAS9429_Spy1400(lacA1)
                 MGAS9429_Spy1640(lacB2) MGAS9429_Spy1641(lacA2)
            SPF: SpyM50392(lacA1) SpyM50393(lacB1) SpyM51612(lacB2)
                 SpyM51613(lacA2)
            SPA: M6_Spy0546 M6_Spy1446 M6_Spy1447 M6_Spy1646 M6_Spy1647
            SPB: M28_Spy0504 M28_Spy1440(lacB.1) M28_Spy1441(lacA.1)
                 M28_Spy1627(lacB.2) M28_Spy1628(lacA.2)
            SPN: SP_1192 SP_1193
            SPR: spr1075(lacB) spr1076(lacA)
            SPD: SPD_1052(lacB) SPD_1053(lacA)
            SAG: SAG1930(lacB) SAG1931(lacA)
            SAN: gbs1335 gbs1336 gbs1917 gbs1918
            SAK: SAK_1889(lacB) SAK_1890(lacA)
            SMU: SMU.1495(lacB) SMU.1496(lacA)
            SSA: SSA_1698(lacB)
            SGO: SGO_1518(lacB-2) SGO_1519(lacA-1) SGO_1525(lacB-1)
                 SGO_1526(lacA-2)
            LCA: LSEI_0679 LSEI_0680
            LGA: LGAS_0492 LGAS_0493
            EFA: EF1834(lacB) EF1835(lacA)
            CAC: CAC2953(lacB) CAC2954(lacA)
            CPE: CPE0326(lacA) CPE0327(lacB)
            CTH: Cthe_2597
            CBE: Cbei_0227 Cbei_0407
            AMT: Amet_0338
            CSC: Csac_1200
            CPH: Cpha266_1332
            TPT: Tpet_1664
            TME: Tmel_1182
            FNO: Fnod_0790
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.1.26
            ExPASy - ENZYME nomenclature database: 5.3.1.26
            ExplorEnz - The Enzyme Database: 5.3.1.26
            ERGO genome analysis and discovery system: 5.3.1.26
            BRENDA, the Enzyme Database: 5.3.1.26
            CAS: 39433-98-2
///
ENTRY       EC 5.3.1.-                  Enzyme
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting aldoses and ketoses
REACTION    (1) L-Xylulose <=> L-Lyxose [RN:R01906];
            (2) Kanosamine 6-phosphate <=> Aminofructose 6-phosphate [RN:R06589]
SUBSTRATE   L-Xylulose [CPD:C00312];
            Kanosamine 6-phosphate [CPD:C12213]
PRODUCT     L-Lyxose [CPD:C01508];
            Aminofructose 6-phosphate [CPD:C12214]
///
ENTRY       EC 5.3.2.1                  Enzyme
NAME        phenylpyruvate tautomerase;
            phenylpyruvic keto-enol isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting keto- and enol-groups
SYSNAME     phenylpyruvate keto---enol-isomerase
REACTION    keto-phenylpyruvate = enol-phenylpyruvate [RN:R01378]
ALL_REAC    R01378;
            (other) R03342
SUBSTRATE   keto-phenylpyruvate [CPD:C00166]
PRODUCT     enol-phenylpyruvate [CPD:C02763]
COMMENT     Also acts on other arylpyruvates.
REFERENCE   1  [PMID:5824560]
  AUTHORS   Blasi F, Fragomele F, Covelli I.
  TITLE     Thyroidal phenylpyruvate tautomerase. Isolation and
            characterization.
  JOURNAL   J. Biol. Chem. 244 (1969) 4864-70.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   Knox, W.E.
  TITLE     p-Hydroxyphenylpyruvate enol-keto tautomerase.
  JOURNAL   Methods Enzymol. 2 (1955) 289-295.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:13416270]
  AUTHORS   KNOX WE, PITT BM.
  TITLE     Enzymic catalysis of the keto-enol tautomerization of phenylpyruvic
            acids.
  JOURNAL   J. Biol. Chem. 225 (1957) 675-88.
  ORGANISM  cow [GN:bta], rabbit, rat [GN:rno], pig [GN:ssc], guinea pig
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
ORTHOLOGY   KO: K07253  phenylpyruvate tautomerase
GENES       HSA: 4282(MIF)
            MMU: 17319(Mif)
            RNO: 81683(Mif)
            BTA: 280858(MIF)
            SPU: 761184(LOC761184)
STRUCTURES  PDB: 1GYJ  1GYX  1GYY  2GDG  2OOH  2OOW  2OOZ  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.2.1
            ExPASy - ENZYME nomenclature database: 5.3.2.1
            ExplorEnz - The Enzyme Database: 5.3.2.1
            ERGO genome analysis and discovery system: 5.3.2.1
            BRENDA, the Enzyme Database: 5.3.2.1
            CAS: 9023-54-5
///
ENTRY       EC 5.3.2.2                  Enzyme
NAME        oxaloacetate tautomerase;
            oxalacetic keto-enol isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting keto- and enol-groups
SYSNAME     oxaloacetate keto---enol-isomerase
REACTION    keto-oxaloacetate = enol-oxaloacetate [RN:R00363]
ALL_REAC    R00363
SUBSTRATE   keto-oxaloacetate [CPD:C00036]
PRODUCT     enol-oxaloacetate [CPD:C03981]
REFERENCE   1  [PMID:5781999]
  AUTHORS   Annett RG, Kosicki GW.
  TITLE     Oxalacetate keto-enol tautomerase. Purification and
            characterization.
  JOURNAL   J. Biol. Chem. 244 (1969) 2059-67.
  ORGANISM  pig [GN:ssc]
GENES       AZO: azo0131(dmpI) azo1855(lapI) azo2359
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.2.2
            ExPASy - ENZYME nomenclature database: 5.3.2.2
            ExplorEnz - The Enzyme Database: 5.3.2.2
            ERGO genome analysis and discovery system: 5.3.2.2
            BRENDA, the Enzyme Database: 5.3.2.2
            CAS: 37318-45-9
///
ENTRY       EC 5.3.2.-                  Enzyme
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Interconverting keto- and enol-groups
REACTION    (1) 2-Hydroxymuconate <=> (Z)-5-Oxohex-2-enedioate [RN:R03966];
            (2) 2-Hydroxy-5-methyl-cis,cis-muconate <=>
            2-Oxo-5-methyl-cis-muconate [RN:R05389]
SUBSTRATE   2-Hydroxy-5-methyl-cis,cis-muconate [CPD:C07478]
PRODUCT     2-Oxo-5-methyl-cis-muconate [CPD:C07479]
///
ENTRY       EC 5.3.3.1                  Enzyme
NAME        steroid Delta-isomerase;
            hydroxysteroid isomerase;
            steroid isomerase;
            Delta5-ketosteroid isomerase;
            Delta5(or Delta4)-3-keto steroid isomerase;
            Delta5-steroid isomerase;
            3-oxosteroid isomerase;
            Delta5-3-keto steroid isomerase;
            Delta5-3-oxosteroid isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing C=C bonds
SYSNAME     3-oxosteroid Delta5-Delta4-isomerase
REACTION    a 3-oxo-Delta5-steroid = a 3-oxo-Delta4-steroid [RN:R02644]
ALL_REAC    R02644;
            (other) R01837 R01839 R02216 R02217 R02499 R02500 R02840 R02842
            R03327 R03328 R04163 R04164 R04678 R04680 R04849 R04851 R07427
SUBSTRATE   3-oxo-Delta5-steroid [CPD:C01034]
PRODUCT     3-oxo-Delta4-steroid [CPD:C00619]
COMMENT     May be at least three distinct enzymes.
REFERENCE   1  [PMID:5867327]
  AUTHORS   Ewald W, Werbin H, Chaikoff IL.
  TITLE     Evidence for the presence of 17-hydroxypregnenedione isomerase in
            beef adrenal cortex.
  JOURNAL   Biochim. Biophys. Acta. 111 (1965) 306-12.
  ORGANISM  cow [GN:bta]
REFERENCE   2
  AUTHORS   Kawahara, F.S. and Talalay, P.
  TITLE     Crystalline Delta5-3-ketosteroid isomerase.
  JOURNAL   J. Biol. Chem. 235 (1960) PC1-PC2.
  ORGANISM  Pseudomonas testosteroni
REFERENCE   3
  AUTHORS   Talalay, P. and Wang, V.S.
  TITLE     Enzymic isomerization of Delta5-3-ketosteroids.
  JOURNAL   Biochim. Biophys. Acta 18 (1955) 300-301.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00140  C21-Steroid hormone metabolism
            PATH: map00150  Androgen and estrogen metabolism
ORTHOLOGY   KO: K01822  steroid delta-isomerase
GENES       HSA: 3283(HSD3B1) 3284(HSD3B2)
            MMU: 15492(Hsd3b1) 15493(Hsd3b2) 15497(Hsd3b6)
            RNO: 24470(Hsd3b) 29632(Hsd3b6)
            CFA: 483146(HSD3B1)
            BTA: 281824(HSD3B)
            SSC: 445539(3B-HSD)
            GGA: 396015(HSD3B1)
            DRE: 373131(hsd3b1)
            REH: H16_B0602
            OIH: OB0288
            MAV: MAV_1209 MAV_1444
            MSM: MSMEG_5258
            RHA: RHA1_ro03609
            SEN: SACE_4441
STRUCTURES  PDB: 1BUQ  1C7H  1CQS  1DMM  1DMN  1DMQ  1E97  1GS3  1ISK  1K41  
                 1OCV  1OGX  1OGZ  1OH0  1OHO  1OHP  1OHS  1OPY  1VZZ  1W00  
                 1W01  1W02  1W6Y  2PZV  8CHO  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.3.1
            ExPASy - ENZYME nomenclature database: 5.3.3.1
            ExplorEnz - The Enzyme Database: 5.3.3.1
            ERGO genome analysis and discovery system: 5.3.3.1
            BRENDA, the Enzyme Database: 5.3.3.1
            CAS: 9031-36-1
///
ENTRY       EC 5.3.3.2                  Enzyme
NAME        isopentenyl-diphosphate Delta-isomerase;
            isopentenylpyrophosphate Delta-isomerase;
            methylbutenylpyrophosphate isomerase;
            isopentenylpyrophosphate isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing C=C bonds
SYSNAME     isopentenyl-diphosphate Delta3-Delta2-isomerase
REACTION    isopentenyl diphosphate = dimethylallyl diphosphate [RN:R01123]
ALL_REAC    R01123
SUBSTRATE   isopentenyl diphosphate [CPD:C00129]
PRODUCT     dimethylallyl diphosphate [CPD:C00235]
COMMENT     The enzyme from Streptomyces sp. strain CL190 requires FMN and
            NAD(P)H as cofactors. Activity is reduced if FMN is replaced by FAD,
            but the enzyme becomes inactive when NAD(P)H is replaced by NAD+ or
            NADP+. That enzyme also requires Mg2+, Mn2+ or Ca2+ for activity.
REFERENCE   1  [PMID:11158573]
  AUTHORS   Kaneda K, Kuzuyama T, Takagi M, Hayakawa Y, Seto H.
  TITLE     An unusual isopentenyl diphosphate isomerase found in the mevalonate
            pathway gene cluster from Streptomyces sp. strain CL190.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 932-7.
  ORGANISM  Streptomyces sp.
REFERENCE   2  [PMID:6351725]
  AUTHORS   Bishop JM.
  TITLE     Cellular oncogenes and retroviruses.
  JOURNAL   Annu. Rev. Biochem. 52 (1983) 301-54.
REFERENCE   3  [PMID:13792054]
  AUTHORS   AGRANOFF BW, EGGERER H, HENNING U, LYNEN F.
  TITLE     Biosynthesis of terpenes. VII. Isopentenyl pyrophosphate isomerase.
  JOURNAL   J. Biol. Chem. 235 (1960) 326-32.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00100  Biosynthesis of steroids
            PATH: map00900  Terpenoid biosynthesis
ORTHOLOGY   KO: K01823  isopentenyl-diphosphate delta-isomerase
GENES       HSA: 3422(IDI1) 91734(IDI2)
            PTR: 450263(IDI1)
            MMU: 319554(Idi1)
            RNO: 89784(Idi1)
            GGA: 420459(IDI1)
            XLA: 494671(LOC494671)
            XTR: 496783(idi2)
            SPU: 586184(LOC586184)
            CEL: K06H7.9(idi-1)
            ATH: AT3G02780(IPP2)
            OSA: 4338791 4343523
            CME: CMB062C
            SCE: YPL117C(IDI1)
            AGO: AGOS_ADL268C
            PIC: PICST_68990(IDI1)
            CGR: CAGL0J06952g
            SPO: SPBC106.15(idi1)
            ANI: AN0579.2
            AFM: AFUA_6G11160
            AOR: AO090023000500
            CNE: CNA02550
            UMA: UM04838.1
            ECU: ECU02_0230
            DDI: DDB_0191342(ipi)
            TET: TTHERM_00237280 TTHERM_00438860
            TBR: Tb09.211.0700
            TCR: 408799.19 510431.10
            LMA: LmjF35.5330
            EHI: 46.t00025
            ECO: b2889(idi)
            ECJ: JW2857(idi)
            ECE: Z4227
            ECS: ECs3761
            ECC: c3467
            ECI: UTI89_C3274
            ECP: ECP_2882
            ECV: APECO1_3638
            ECW: EcE24377A_3215(idi)
            ECX: EcHS_A3048
            STY: STY3195
            STT: t2957
            SPT: SPA2907(idi)
            SEC: SC2979(idi)
            STM: STM3039(idi)
            SFL: SF2875(idi)
            SFX: S3074
            SFV: SFV_2937
            SSN: SSON_3042 SSON_3489(yhfK)
            SBO: SBO_3103
            SDY: SDY_3193
            ECA: ECA2789
            PLU: plu3987
            ENT: Ent638_3307
            SPE: Spro_2201
            VPA: VPA0278
            VFI: VF0403
            PPR: PBPRA0469(mvaD)
            PEN: PSEEN4850
            CBU: CBU_0607(mvaD)
            CBD: COXBU7E912_0619(mvaD)
            LPN: lpg2051
            LPF: lpl2029
            LPP: lpp2034
            TCX: Tcr_1718
            HHA: Hhal_1623
            DNO: DNO_0798
            EBA: ebA5678 p2A143
            DVU: DVU1679(idi)
            DDE: Dde_1991
            LIP: LI1134
            BBA: Bd1626
            AFW: Anae109_4082
            MXA: MXAN_5021(fni)
            RPR: RP452
            RTY: RT0439(idi)
            RCO: RC0744
            RFE: RF_0785(fni)
            RBE: RBE_0731(fni)
            RAK: A1C_04190
            RBO: A1I_04755
            RCM: A1E_02555
            RRI: A1G_04195
            MLO: mlr6371
            RET: RHE_PD00245(ypd00046)
            XAU: Xaut_4134
            SIL: SPO0131
            SIT: TM1040_3442
            RSP: RSP_0276
            RSH: Rsph17029_1919
            RSQ: Rsph17025_1019
            JAN: Jann_0168
            RDE: RD1_0147(idi)
            BSU: BG11440(ypgA)
            BAN: BA1520
            BAR: GBAA1520
            BAA: BA_2041
            BAT: BAS1409
            BCE: BC1499
            BCA: BCE_1626
            BCZ: BCZK1380(fni)
            BCY: Bcer98_1222
            BTK: BT9727_1381(fni)
            BLI: BL02217(fni)
            BLD: BLi02426
            BAY: RBAM_021020(fni)
            BPU: BPUM_2020(fni)
            OIH: OB0537
            SAU: SA2136(fni)
            SAV: SAV2346(fni)
            SAM: MW2267(fni)
            SAR: SAR2431(fni)
            SAS: SAS2237
            SAC: SACOL2341(fni)
            SAB: SAB2225c(fni)
            SAA: SAUSA300_2292(fni)
            SAO: SAOUHSC_02623
            SEP: SE1925
            SER: SERP1937(fni-2)
            SHA: SH0712(fni)
            SSP: SSP0556
            LMO: lmo1383
            LMF: LMOf2365_1402(fni)
            LIN: lin1420
            LWE: lwe1399(fni)
            LLA: L11083(yebB)
            LLC: LACR_0457
            LLM: llmg_0428(fni)
            SPY: SPy_0879
            SPZ: M5005_Spy_0685
            SPM: spyM18_0940
            SPG: SpyM3_0598
            SPS: SPs1255
            SPH: MGAS10270_Spy0743
            SPI: MGAS10750_Spy0777
            SPJ: MGAS2096_Spy0756
            SPK: MGAS9429_Spy0740
            SPF: SpyM51123(fni)
            SPA: M6_Spy0702
            SPB: M28_Spy0665
            SPN: SP_0384
            SPR: spr0341(fni)
            SPD: SPD_0349(fni)
            SAG: SAG1323
            SAN: gbs1393
            SAK: SAK_1354(fni)
            SMU: SMU.939
            STC: str0562(idi)
            STL: stu0562(idi)
            SSA: SSA_0336
            SGO: SGO_0242
            LPL: lp_1732(idi1)
            LJO: LJ1208
            LAC: LBA1171
            LSA: LSA0905(idi)
            LSL: LSL_0682
            LDB: Ldb0996(fni)
            LBU: LBUL_0903
            LBR: LVIS_0861
            LCA: LSEI_1493
            LRE: Lreu_0912
            EFA: EF0901
            OOE: OEOE_1103
            STH: STH1674
            CBE: Cbei_3081
            DRM: Dred_0474
            SWO: Swol_1341
            MTA: Moth_1328
            MTU: Rv1745c(idi)
            MTC: MT1787(idi)
            MBO: Mb1774c(idi)
            MBB: BCG_1784c(idi)
            MPA: MAP3079c
            MAV: MAV_3894(fni)
            MSM: MSMEG_1057(fni) MSMEG_2337(fni)
            MVA: Mvan_1582 Mvan_2176
            MGI: Mflv_1842 Mflv_4187
            MMC: Mmcs_1954
            MKM: Mkms_2000
            MJL: Mjls_1934
            CGL: NCgl2223(cgl2305)
            CGB: cg2531(idi)
            CEF: CE2207
            CDI: DIP1730(idi)
            NFA: nfa19790 nfa22100
            RHA: RHA1_ro00239
            SCO: SCO6750(SC5F2A.33c)
            SMA: SAV1663(idi)
            LXX: Lxx23810(idi)
            CMI: CMM_2889(idiA)
            AAU: AAur_0321(idi)
            PAC: PPA2115
            FRA: Francci3_4188
            FAL: FRAAL6504(idi)
            KRA: Krad_3991
            SEN: SACE_2627(idiB_2) SACE_5210(idi)
            STP: Strop_4438
            RXY: Rxyl_0400
            BBU: BB0684
            BGA: BG0707
            SYN: sll1556
            SYC: syc2161_c
            SYF: Synpcc7942_1933
            CYA: CYA_2395(fni)
            CYB: CYB_2691(fni)
            TEL: tll1403
            ANA: all4591
            AVA: Ava_2461 Ava_B0346
            TER: Tery_1589
            SRU: SRU_1900(idi)
            CHU: CHU_0674(idi)
            GFO: GFO_2363(idi)
            FJO: Fjoh_0269
            FPS: FP1792(idi)
            CTE: CT0257
            CCH: Cag_1445
            CPH: Cpha266_0385
            PVI: Cvib_1545
            PLT: Plut_1764
            RRS: RoseRS_2437
            RCA: Rcas_2215
            DRA: DR_1087
            DGE: Dgeo_1381
            TTH: TT_P0067
            TTJ: TTHB110
            MJA: MJ0862
            MMP: MMP0043
            MMQ: MmarC5_1637
            MMZ: MmarC7_1040
            MAE: Maeo_1184
            MVN: Mevan_1058
            MAC: MA0604(idi)
            MBA: Mbar_A1419
            MMA: MM_1764
            MBU: Mbur_2397
            MTP: Mthe_0474
            MHU: Mhun_2888
            MLA: Mlab_1665
            MEM: Memar_1814
            MBN: Mboo_2211
            MTH: MTH48
            MST: Msp_0856(fni)
            MSI: Msm_1441
            MKA: MK0776(lldD)
            AFU: AF2287
            HAL: VNG1818G(idi) VNG6081G(crt_1) VNG6445G(crt_2) VNG7060 VNG7149
            HMA: rrnAC3484(idi)
            HWA: HQ2772A(idiA) HQ2847A(idiB)
            NPH: NP0360A(idiB_1) NP4826A(idiA) NP5124A(idiB_2)
            TAC: Ta0102
            TVO: TVN0179
            PTO: PTO0496
            PHO: PH1202
            PAB: PAB1662
            PFU: PF0856
            TKO: TK1470
            RCI: LRC397(fni)
            APE: APE_1765.1
            SMR: Smar_0822
            IHO: Igni_0804
            HBU: Hbut_0539
            SSO: SSO0063
            STO: ST2059
            SAI: Saci_0091
            MSE: Msed_2136
            PAI: PAE0801
            PIS: Pisl_1093
            PCL: Pcal_0017
            PAS: Pars_0051
            TPE: Tpen_0272
STRUCTURES  PDB: 1HX3  1HZT  1I9A  1NFS  1NFZ  1OW2  1P0K  1P0N  1PPV  1PPW  
                 1PVF  1Q54  1R67  1VCF  1VCG  1X83  1X84  2B2K  2DHO  2G73  
                 2G74  2I6K  2ICJ  2ICK  2PNY  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.3.2
            ExPASy - ENZYME nomenclature database: 5.3.3.2
            ExplorEnz - The Enzyme Database: 5.3.3.2
            ERGO genome analysis and discovery system: 5.3.3.2
            BRENDA, the Enzyme Database: 5.3.3.2
            CAS: 9033-27-6
///
ENTRY       EC 5.3.3.3                  Enzyme
NAME        vinylacetyl-CoA Delta-isomerase;
            vinylacetyl coenzyme A Delta-isomerase;
            vinylacetyl coenzyme A isomerase;
            Delta3-cis-Delta2-trans-enoyl-CoA isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing C=C bonds
SYSNAME     vinylacetyl-CoA Delta3-Delta2-isomerase
REACTION    vinylacetyl-CoA = crotonyl-CoA [RN:R03031]
ALL_REAC    R03031
SUBSTRATE   vinylacetyl-CoA [CPD:C02331]
PRODUCT     crotonyl-CoA [CPD:C00877]
COMMENT     Also acts on 3-methyl-vinylacetyl-CoA.
REFERENCE   1
  AUTHORS   Lynen, F., Knappe, J., Lorch, E., Jutting, G. and Ringelmann, E.
  TITLE     Die biochemische Funktion des Biotins.
  JOURNAL   Angew. Chem. 71 (1959) 481-486.
REFERENCE   2
  AUTHORS   Rilling, H.C. and Coon, M.J.
  TITLE     The enzymatic isomerization of alpha-methylvinylacetyl coenzyme A
            and the specificity of a bacterial alpha-methylcrotonyl coenzyme A
            carboxylase.
  JOURNAL   J. Biol. Chem. 235 (1960) 3087-3092.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00650  Butanoate metabolism
GENES       BUR: Bcep18194_B2410
            PNU: Pnuc_0370
            CDF: CD2341(abfD)
            CBE: Cbei_2100
            CHY: CHY_1314(abfD)
            PGI: PG0692(abfD)
            IHO: Igni_0595
            MSE: Msed_1220 Msed_1321
            PIS: Pisl_0248
            PCL: Pcal_1396
STRUCTURES  PDB: 1U8V  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.3.3
            ExPASy - ENZYME nomenclature database: 5.3.3.3
            ExplorEnz - The Enzyme Database: 5.3.3.3
            ERGO genome analysis and discovery system: 5.3.3.3
            BRENDA, the Enzyme Database: 5.3.3.3
            CAS: 9023-73-8
///
ENTRY       EC 5.3.3.4                  Enzyme
NAME        muconolactone Delta-isomerase;
            muconolactone isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing C=C bonds
SYSNAME     5-oxo-4,5-dihydrofuran-2-acetate Delta3-Delta2-isomerase
REACTION    (S)-5-oxo-2,5-dihydrofuran-2-acetate =
            5-oxo-4,5-dihydrofuran-2-acetate [RN:R06990]
ALL_REAC    R06990;
            (other) R04260
SUBSTRATE   (S)-5-oxo-2,5-dihydrofuran-2-acetate [CPD:C14610]
PRODUCT     5-oxo-4,5-dihydrofuran-2-acetate [CPD:C03586]
REFERENCE   1  [PMID:5330966]
  AUTHORS   Ornston LN.
  TITLE     The conversion of catechol and protocatechuate to beta-ketoadipate
            by Pseudomonas putida. 3. Enzymes of the catechol pathway.
  JOURNAL   J. Biol. Chem. 241 (1966) 3795-9.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2
  AUTHORS   Ornston, L.N.
  TITLE     Conversion of catechol and protocatechuate to beta-ketoadipate
            (Pseudomonas putida).
  JOURNAL   Methods Enzymol. 17A (1970) 529-549.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
ORTHOLOGY   KO: K03464  muconolactone D-isomerase
GENES       PAE: PA2508(catC)
            PAU: PA14_32230(catC)
            PAP: PSPA7_2731(catC)
            PPU: PP_3714(catC)
            PPF: Pput_2054
            PFL: PFL_3861(catC)
            PFO: Pfl_2326 Pfl_2962
            PEN: PSEEN3137(catC)
            PCR: Pcryo_1269
            ACI: ACIAD1447(catC)
            MMW: Mmwyl1_3041
            REU: Reut_A1502 Reut_A1690
            REH: H16_A1967(catC3) H16_B1584(catC2)
            RME: Rmet_4677 Rmet_4877
            BMA: BMAA0198(catC)
            BMV: BMASAVP1_1373(catC)
            BML: BMA10299_1570(catC)
            BMN: BMA10247_A0229(catC)
            BXE: Bxe_A2110(catC)
            BVI: Bcep1808_4157
            BUR: Bcep18194_B2330
            BCN: Bcen_4595
            BCH: Bcen2424_3768
            BAM: Bamb_5497 Bamb_6586
            BPS: BPSS1893(catC)
            BPM: BURPS1710b_A0988(catC)
            BPL: BURPS1106A_A2568(catC)
            BPD: BURPS668_A2712(catC)
            BTE: BTH_II0483
            BPE: BP0223(catC2)
            BPA: BPP0410(catC2)
            BBR: BB0412(catC2)
            PNA: Pnap_2118
            AAV: Aave_3938
            AJS: Ajs_0141
            XAU: Xaut_1121
            PDE: Pden_1175
            SWI: Swit_0976
            MSM: MSMEG_1912 MSMEG_4045
            MGI: Mflv_1359
            MMC: Mmcs_1377
            MKM: Mkms_1395
            MJL: Mjls_1411
            CGL: NCgl2317(cgl2400)
            CGB: cg2634(catC)
            CEF: CE2302
            NFA: nfa35230
            RHA: RHA1_ro02371(catC)
            NCA: Noca_0837
            SEN: SACE_4383(catC)
STRUCTURES  PDB: 1MLI  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.3.4
            ExPASy - ENZYME nomenclature database: 5.3.3.4
            ExplorEnz - The Enzyme Database: 5.3.3.4
            ERGO genome analysis and discovery system: 5.3.3.4
            BRENDA, the Enzyme Database: 5.3.3.4
            CAS: 37318-46-0
///
ENTRY       EC 5.3.3.5                  Enzyme
NAME        cholestenol Delta-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing C=C bonds
SYSNAME     Delta7-cholestenol Delta7-Delta8-isomerase
REACTION    5alpha-cholest-7-en-3beta-ol = 5alpha-cholest-8-en-3beta-ol
            [RN:R03353]
ALL_REAC    R03353;
            (other) R04671 R04804 R07484
SUBSTRATE   5alpha-cholest-7-en-3beta-ol [CPD:C01189]
PRODUCT     5alpha-cholest-8-en-3beta-ol [CPD:C03845]
REFERENCE   1  [PMID:5810070]
  AUTHORS   Wilton DC, Rahimtula AD, Akhtar M.
  TITLE     The reversibility of the delta8-cholestenol-delta7-cholestenol
            isomerase reaction in cholesterol biosynthesis.
  JOURNAL   Biochem. J. 114 (1969) 71-3.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K01824  cholestenol delta-isomerase
GENES       HSA: 10682(EBP)
            MMU: 13595(Ebp)
            RNO: 117278(Ebp)
            CFA: 609430(LOC609430)
            XLA: 380161(ebp)
            SPU: 589723(LOC589723)
            ATH: AT1G20050(HYD1)
            OSA: 4326449
            ANI: AN7211.2
            AFM: AFUA_3G00810
            AOR: AO090026000084
            TET: TTHERM_00011840 TTHERM_00533890 TTHERM_00721710
                 TTHERM_00974100 TTHERM_00992980 TTHERM_01013190
                 TTHERM_01165190 TTHERM_01587460
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.3.5
            ExPASy - ENZYME nomenclature database: 5.3.3.5
            ExplorEnz - The Enzyme Database: 5.3.3.5
            ERGO genome analysis and discovery system: 5.3.3.5
            BRENDA, the Enzyme Database: 5.3.3.5
            CAS: 37318-47-1
///
ENTRY       EC 5.3.3.6                  Enzyme
NAME        methylitaconate Delta-isomerase;
            methylitaconate isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing C=C bonds
SYSNAME     methylitaconate Delta2-Delta3-isomerase
REACTION    methylitaconate = 2,3-dimethylmaleate [RN:R03070]
ALL_REAC    R03070
SUBSTRATE   methylitaconate [CPD:C02295]
PRODUCT     2,3-dimethylmaleate [CPD:C00922]
REFERENCE   1  [PMID:5574401]
  AUTHORS   Kung HF, Stadtman TC.
  TITLE     Nicotinic acid metabolism. VI. Purification and properties of
            alpha-methyleneglutarate mutase (B 12-dependent) and methylitaconate
            isomerase.
  JOURNAL   J. Biol. Chem. 246 (1971) 3378-88.
  ORGANISM  Clostridium barkeri
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.3.6
            ExPASy - ENZYME nomenclature database: 5.3.3.6
            ExplorEnz - The Enzyme Database: 5.3.3.6
            ERGO genome analysis and discovery system: 5.3.3.6
            BRENDA, the Enzyme Database: 5.3.3.6
            CAS: 9059-08-9
///
ENTRY       EC 5.3.3.7                  Enzyme
NAME        aconitate Delta-isomerase;
            aconitate isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing C=C bonds
SYSNAME     aconitate Delta2-Delta3-isomerase
REACTION    trans-aconitate = cis-aconitate [RN:R02244]
ALL_REAC    R02244
SUBSTRATE   trans-aconitate [CPD:C02341]
PRODUCT     cis-aconitate [CPD:C00417]
COMMENT     cis-Aconitate is used to designate the isomer
            (Z)-prop-1-ene-1,2,3-tricarboxylate. This isomerization could take
            place either in a direct cis-trans interconversion or by an allelic
            rearrangement; the enzyme has been shown to catalyse the latter
            change.
REFERENCE   1
  AUTHORS   Klinman, J.P. and Rose, I.A.
  TITLE     Purification and kinetic properties of aconitate isomerase from
            Pseudomonas putida.
  JOURNAL   Biochemistry 10 (1971) 2253-2259.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2  [PMID:5114988]
  AUTHORS   Klinman JP, Rose IA.
  TITLE     Mechanism of the aconitate isomerase reaction.
  JOURNAL   Biochemistry. 10 (1971) 2259-66.
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.3.7
            ExPASy - ENZYME nomenclature database: 5.3.3.7
            ExplorEnz - The Enzyme Database: 5.3.3.7
            ERGO genome analysis and discovery system: 5.3.3.7
            BRENDA, the Enzyme Database: 5.3.3.7
            CAS: 37318-48-2
///
ENTRY       EC 5.3.3.8                  Enzyme
NAME        dodecenoyl-CoA isomerase;
            dodecenoyl-CoA Delta-isomerase;
            Delta3-cis-Delta2-trans-enoyl-CoA isomerase;
            acetylene-allene isomerase;
            dodecenoyl-CoA Delta-isomerase;
            dodecenoyl-CoA Delta3-cis-Delta2-trans-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing C=C bonds
SYSNAME     dodecenoyl-CoA (3Z)-(2E)-isomerase
REACTION    (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA [RN:R04100]
ALL_REAC    R04100;
            (other) R04756
SUBSTRATE   (3Z)-dodec-3-enoyl-CoA [CPD:C02944]
PRODUCT     (2E)-dodec-2-enoyl-CoA [CPD:C03221]
COMMENT     Also catalyses the interconversion of 3-acetylenic fatty acyl
            thioesters and (+)-2,3-dienoyl fatty acyl thioesters, with fatty
            acid chain lengths C6 to C12.
REFERENCE   1  [PMID:376522]
  AUTHORS   Miesowicz FM, Bloch K.
  TITLE     Purification of hog liver isomerase. Mechanism of isomerization of
            3-alkenyl and 3-alkynyl thioesters.
  JOURNAL   J. Biol. Chem. 254 (1979) 5868-77.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:5830064]
  AUTHORS   Stoffel W, Ditzer R, Caesar H.
  TITLE     [The metabolism of unsaturated fatty acid. 3. On the beta-oxidation
            of mono- and polyene-fatty acids. The mechanism of the enzymatic
            reaction on delta-3-cis-enoyl-CoA compounds]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 339 (1964) 167-81.
REFERENCE   3
  AUTHORS   Stoffel, W. and Ecker, W.
  TITLE     Delta3-cis,-Delta2-trans-Enoyl-CoA isomerase from rat liver
            mitochondria.
  JOURNAL   Methods Enzymol. 14 (1979) 99-105.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:738702]
  AUTHORS   Stoffel W, Grol M.
  TITLE     Purification and properties of 3-cis-2-trans-enoyl-CoA isomerase
            (dodecenoyl-CoA delta-isomerase) from rat liver mitochondria.
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 359 (1978) 1777-82.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00071  Fatty acid metabolism
ORTHOLOGY   KO: K01825  dodecenoyl-CoA delta-isomerase
            KO: K07517  3,2-trans-enoyl-CoA isomerase
GENES       HSA: 10455(PECI) 1632(DCI) 1962(EHHADH)
            PTR: 460996(EHHADH) 471843(PECI)
            MMU: 13177(Dci) 23986(Peci) 74147(Ehhadh)
            RNO: 171142(Ehhadh) 29740(Dci)
            CFA: 478706(PECI) 488110(EHHADH) 490059(DCI)
            GGA: 416657(DCI) 420878(PECI) 424877(EHHADH)
            XLA: 432103(MGC82167)
            XTR: 496654(dci)
            SPU: 592077(LOC592077)
            DME: Dmel_CG13890 Dmel_CG4594 Dmel_CG4598
            CEL: R06F6.9(ech-4)
            TET: TTHERM_00752190
            TBR: Tb927.3.5630 Tb927.4.4910 Tb927.8.7530
            TCR: 507107.40 509261.30 510645.30
            LMA: LmjF29.0010 LmjF31.2250
            ECO: b3846(fadB)
            ECJ: JW3822(fadB)
            ECE: Z5367(fadB)
            ECS: ECs4774
            ECC: c4793(fadB)
            ECI: UTI89_C4431(fadB)
            ECP: ECP_4059
            ECV: APECO1_2611(fadB)
            ECW: EcE24377A_4365(fadB)
            ECX: EcHS_A4069(fadB)
            STY: STY3577(fadB)
            STT: t3315(fadB)
            SPT: SPA3823(fadB)
            SEC: SC3880(fadB)
            STM: STM3983(fadB)
            YPE: YPO3766(fadB)
            YPK: y0464(fadB)
            YPM: YP_3282(fadB)
            YPA: YPA_3436
            YPN: YPN_0198
            YPS: YPTB0267(fadB)
            YPI: YpsIP31758_0283(fadB)
            SSN: SSON_4019(fadB)
            SDY: SDY_3899(fadB)
            ECA: ECA0208(fadB)
            PLU: plu4402(fadB)
            VCH: VC2758
            VVU: VV1_0981
            VVY: VV0029
            VPA: VP0030
            VFI: VF0025 VF1810
            PPR: PBPRA0064
            PAE: PA3014(faoA)
            PAP: PSPA7_2145(fadB)
            PPU: PP_2136(fadB)
            PST: PSPTO_3517(fadB)
            PSB: Psyr_3290
            PSP: PSPPH_3210(fadB)
            PFL: PFL_1940(fadB)
            PFO: Pfl_3879
            PEN: PSEEN3728(fadB)
            PAR: Psyc_1934(fadB)
            ACI: ACIAD0335(fadB)
            SON: SO_0021(fadB)
            SDN: Sden_0015
            SFR: Sfri_0013
            SHE: Shewmr4_0018
            SHM: Shewmr7_0016
            SHN: Shewana3_0024
            ILO: IL0011(fadB)
            CPS: CPS_0393(fadB)
            PHA: PSHAa0011(fadB) PSHAa0967(fadJ)
            PAT: Patl_0201
            FTU: FTT1530(fadB)
            FTF: FTF1530(fadB)
            HCH: HCH_04756
            AHA: AHA_0139(fadB)
            CVI: CV_1553
            RSO: RSc1759(RS02946)
            DAR: Daro_2350
            BRA: BRADO0651 BRADO6723
            BBT: BBta_0817 BBta_7536
            RHA: RHA1_ro04205(fadB1) RHA1_ro06116(fadB2) RHA1_ro06852
            SEN: SACE_1823
            RBA: RB1092(faoA)
            DRA: DR_2477
            TTH: TTC0534
            TTJ: TTHA0890
STRUCTURES  PDB: 1HNO  1HNU  1K39  1PJH  1SG4  1WDK  1WDL  1WDM  1XX4  2CQU  
                 2D3T  2F6Q  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.3.8
            ExPASy - ENZYME nomenclature database: 5.3.3.8
            ExplorEnz - The Enzyme Database: 5.3.3.8
            ERGO genome analysis and discovery system: 5.3.3.8
            BRENDA, the Enzyme Database: 5.3.3.8
            CAS: 62213-29-0
///
ENTRY       EC 5.3.3.9                  Enzyme
NAME        prostaglandin-A1 Delta-isomerase;
            prostaglandin A isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing C=C bonds
SYSNAME     (13E)-(15S)-15-hydroxy-9-oxoprosta-10,13-dienoate
            Delta10-Delta11-isomerase
REACTION    (13E)-(15S)-15-hydroxy-9-oxoprosta-10,13-dienoate =
            (13E)-(15S)-15-hydroxy-9-oxoprosta-11,13-dienoate [RN:R04565]
ALL_REAC    R04565
SUBSTRATE   (13E)-(15S)-15-hydroxy-9-oxoprosta-10,13-dienoate [CPD:C04685]
PRODUCT     (13E)-(15S)-15-hydroxy-9-oxoprosta-11,13-dienoate [CPD:C04686]
COMMENT     Interconverts prostaglandin A1 and prostaglandin C1.
REFERENCE   1  [PMID:234423]
  AUTHORS   Polet H, Levine L.
  TITLE     Metabolism of prostaglandins E, A, and C in serum.
  JOURNAL   J. Biol. Chem. 250 (1975) 351-7.
  ORGANISM  human [GN:hsa], rabbit
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.3.9
            ExPASy - ENZYME nomenclature database: 5.3.3.9
            ExplorEnz - The Enzyme Database: 5.3.3.9
            ERGO genome analysis and discovery system: 5.3.3.9
            BRENDA, the Enzyme Database: 5.3.3.9
            CAS: 9055-01-0
///
ENTRY       EC 5.3.3.10                 Enzyme
NAME        5-carboxymethyl-2-hydroxymuconate Delta-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing C=C bonds
SYSNAME     5-carboxymethyl-2-hydroxymuconate
            Delta2,Delta4-2-oxo,Delta3-isomerase
REACTION    5-carboxymethyl-2-hydroxymuconate = 5-carboxy-2-oxohept-3-enedioate
            [RN:R04379]
ALL_REAC    R04379;
            (other) R04482 R07839
SUBSTRATE   5-carboxymethyl-2-hydroxymuconate [CPD:C04186]
PRODUCT     5-carboxy-2-oxohept-3-enedioate [CPD:C04052]
REFERENCE   1
  AUTHORS   Garrido-Pertierra, A. and Cooper, R.A.
  TITLE     Identification and purification of distinct isomerase and
            decarboxylase enzymes involved in the 4-hydroxyphenylacetate pathway
            of Escherichia coli.
  JOURNAL   Eur. J. Biochem. 117 (1981) 581-584.
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00362  Benzoate degradation via hydroxylation
ORTHOLOGY   KO: K01826  5-carboxymethyl-2-hydroxymuconate isomerase
GENES       PIC: PICST_30014(FML1)
            ECX: EcHS_A4581(hpcD) EcHS_A4584(hpaG)
            STY: STY1138(hpcD)
            STT: t1815(hpcD)
            SPT: SPA1746(hpcD)
            SEC: SC1054(hpaF)
            STM: STM1104(hpaF)
            YPE: YPO1765(hpaF)
            YPK: y2544(hpaF)
            YPM: YP_1628(hpaF)
            YPA: YPA_1134 YPA_1137
            YPN: YPN_2358 YPN_2361 YPN_2413
            YPP: YPDSF_1361 YPDSF_1409
            YPS: YPTB1641(hpaF)
            YPI: YpsIP31758_2361(hpaF) YpsIP31758_2364(hpaG2)
                 YpsIP31758_2365(hpaG1)
            SFL: SF4381(hpcD)
            SFX: S4651(hpaF)
            SFV: SFV_4381(hpaF)
            SSN: SSON_4496(hpaF)
            SBO: SBO_4409(hpaF)
            PLU: plu0986(hpcD)
            ENT: Ent638_2369
            SPE: Spro_0625 Spro_0626 Spro_0639
            PMU: PM1532(hpaF)
            VCH: VC2669
            VVU: VV1_1345
            VVY: VV1586 VV3024
            VPA: VP0240
            VFI: VF0207
            PPR: PBPRA0236
            PAE: PA1966 PA4125(hpcD)
            PAU: PA14_10610(hpcD) PA14_39100
            PFL: PFL_1486 PFL_3371 PFL_3374(hpaF)
            PFO: Pfl_1384
            PEN: PSEEN3096(hpaF) PSEEN4037
            PAR: Psyc_0136
            PCR: Pcryo_0147
            ACI: ACIAD2013
            SDN: Sden_1896
            CPS: CPS_3921
            PHA: PSHAa0329
            PAT: Patl_2612
            AEH: Mlg_2259
            HHA: Hhal_1445
            HCH: HCH_03011
            CSA: Csal_1737
            CVI: CV_0893
            RSO: RSc2419(hpaF)
            REU: Reut_A0050 Reut_A0332 Reut_A1135 Reut_B4052 Reut_B5809
                 Reut_C5929
            REH: H16_A0624(hpaF) H16_B1250
            RME: Rmet_4733
            BMA: BMAA1136(hpcD)
            BML: BMA10299_0100 BMA10299_0101 BMA10299_0104(hpaF)
            BMN: BMA10247_A1509(hpaF) BMA10247_A1512 BMA10247_A1513
            BXE: Bxe_B2032
            BVI: Bcep1808_4801 Bcep1808_4802
            BUR: Bcep18194_B0621 Bcep18194_B1779 Bcep18194_B1782
                 Bcep18194_B1783
            BCN: Bcen_1231 Bcen_3325 Bcen_4131 Bcen_4134 Bcen_4135 Bcen_5340
            BCH: Bcen2424_4231 Bcen2424_4232 Bcen2424_4235 Bcen2424_5042
                 Bcen2424_5521 Bcen2424_6601 Bcen2424_6914
            BAM: Bamb_3653 Bamb_3657 Bamb_4450 Bamb_4846
            BPS: BPSS0696(hpcD)
            BPM: BURPS1710b_A2263(hpaG) BURPS1710b_A2264(hpaG)
                 BURPS1710b_A2268(hpcD)
            BPL: BURPS1106A_A0938 BURPS1106A_A0939 BURPS1106A_A0942(hpaF)
            BPD: BURPS668_A1023 BURPS668_A1024 BURPS668_A1027(hpaF)
            BTE: BTH_II1731(hpcD) BTH_II1734(hpaG-1) BTH_II1735(hpaG-2)
            PNU: Pnuc_1369
            BBR: BB0738(hpaF)
            POL: Bpro_0199 Bpro_1490 Bpro_2792 Bpro_3959
            PNA: Pnap_0137 Pnap_0618 Pnap_2474
            AAV: Aave_3875 Aave_4268
            AJS: Ajs_2258
            VEI: Veis_2409 Veis_3438 Veis_4213
            HAR: HEAR1199
            DAR: Daro_2149
            GUR: Gura_3666
            DVL: Dvul_2107
            SFU: Sfum_0938
            MES: Meso_2508
            PLA: Plav_1788
            RET: RHE_CH02290(ypch00743)
            RLE: pRL80045
            BME: BMEII0134
            BMF: BAB2_1120
            BMS: BRA1162(hpcD)
            BMB: BruAb2_1098(hpcD)
            BOV: BOV_A1065(hpcD)
            OAN: Oant_0318
            BJA: bll2969(hpcD)
            BRA: BRADO2592 BRADO2594 BRADO5118 BRADO6046
            BBT: BBta_2938 BBta_2940 BBta_3244 BBta_5587
            RPA: RPA2986 RPA3759(hpcD)
            RPB: RPB_1704 RPB_1707 RPB_2522
            RPC: RPC_1347 RPC_1694
            RPD: RPD_2022 RPD_3590 RPD_4085
            RPE: RPE_1953
            XAU: Xaut_0927 Xaut_0940 Xaut_4106
            SIL: SPOA0320(hpcD)
            SIT: TM1040_3392 TM1040_3465 TM1040_3469 TM1040_3675
            RSH: Rsph17029_1807
            RSQ: Rsph17025_1470
            JAN: Jann_0869 Jann_2105 Jann_2909 Jann_3500 Jann_3504 Jann_3923
            PDE: Pden_0245 Pden_2753
            NAR: Saro_2426 Saro_2598
            SWI: Swit_0820 Swit_1650 Swit_1681 Swit_2286 Swit_2295 Swit_2302
                 Swit_3022 Swit_4247 Swit_4261
            ACR: Acry_1963
            RRU: Rru_A3697
            MAG: amb0803
            ABA: Acid345_0647
            BCY: Bcer98_0868
            OIH: OB2864
            GKA: GK3029
            SAJ: SaurJH9_0968
            SAH: SaurJH1_0987
            CBE: Cbei_4954
            AMT: Amet_0677
            CSC: Csac_0967
            MTA: Moth_1492
            MGI: Mflv_4230
            MMC: Mmcs_2615
            MKM: Mkms_2659
            MJL: Mjls_2644
            ART: Arth_2051 Arth_2527 Arth_3441
            NCA: Noca_3337
            TFU: Tfu_0621
            FRA: Francci3_3626
            ACE: Acel_0713 Acel_1102
            KRA: Krad_4192
            SEN: SACE_2626
            BAD: BAD_1465
            RXY: Rxyl_0204 Rxyl_2370
            AVA: Ava_2073
            DEB: DehaBAV1_1032
            RRS: RoseRS_3934
            RCA: Rcas_3608
            DRA: DR_A0227
            DGE: Dgeo_1217 Dgeo_2413
            MMZ: MmarC7_1144
            MTP: Mthe_0452
            MSE: Msed_1358
            PCL: Pcal_1503
STRUCTURES  PDB: 1GTT  1I7O  1WZO  2DFU  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.3.10
            ExPASy - ENZYME nomenclature database: 5.3.3.10
            ExplorEnz - The Enzyme Database: 5.3.3.10
            ERGO genome analysis and discovery system: 5.3.3.10
            UM-BBD (Biocatalysis/Biodegradation Database): 5.3.3.10
            BRENDA, the Enzyme Database: 5.3.3.10
            CAS: 79079-05-3
///
ENTRY       EC 5.3.3.11                 Enzyme
NAME        isopiperitenone Delta-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing C=C bonds
SYSNAME     isopiperitenone Delta8-Delta4-isomerase
REACTION    isopiperitenone = piperitenone [RN:R03782]
ALL_REAC    R03782
SUBSTRATE   isopiperitenone [CPD:C02289]
PRODUCT     piperitenone [CPD:C01951]
COMMENT     Involved in the biosynthesis of menthol and related monoterpenes in
            peppermint (Mentha piperita) leaves.
REFERENCE   1  [PMID:3885858]
  AUTHORS   Kjonaas RB, Venkatachalam KV, Croteau R.
  TITLE     Metabolism of monoterpenes: oxidation of isopiperitenol to
            isopiperitenone, and subsequent isomerization to piperitenone by
            soluble enzyme preparations from peppermint (Mentha piperita)
            leaves.
  JOURNAL   Arch. Biochem. Biophys. 238 (1985) 49-60.
  ORGANISM  Mentha piperita
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.3.11
            ExPASy - ENZYME nomenclature database: 5.3.3.11
            ExplorEnz - The Enzyme Database: 5.3.3.11
            ERGO genome analysis and discovery system: 5.3.3.11
            BRENDA, the Enzyme Database: 5.3.3.11
            CAS: 96595-07-2
///
ENTRY       EC 5.3.3.12                 Enzyme
NAME        L-dopachrome isomerase;
            dopachrome tautomerase;
            tyrosinase-related protein 2;
            TRP-1;
            TRP2;
            TRP-2;
            tyrosinase-related protein-2;
            dopachrome Delta7,Delta2-isomerase;
            dopachrome Delta-isomerase;
            dopachrome conversion factor;
            dopachrome isomerase;
            dopachrome oxidoreductase;
            dopachrome-rearranging enzyme;
            DCF;
            DCT;
            dopachrome keto-enol isomerase;
            L-dopachrome-methyl ester tautomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing C=C bonds
SYSNAME     L-dopachrome keto-enol isomerase
REACTION    L-dopachrome = 5,6-dihydroxyindole-2-carboxylate [RN:R03673]
ALL_REAC    R03673
SUBSTRATE   L-dopachrome [CPD:C01693]
PRODUCT     5,6-dihydroxyindole-2-carboxylate [CPD:C04185]
COMMENT     A zinc enzyme. Stereospecific for L-dopachrome. Dopachrome methyl
            ester is a substrate, but dopaminochrome
            (2,3-dihydroindole-5,6-quinone) is not (see also EC 4.1.1.84,
            D-dopachrome decarboxylase).
REFERENCE   1  [PMID:8573077]
  AUTHORS   Solano F, Jimenez-Cervantes C, Martinez-Liarte JH, Garcia-Borron JC,
            Jara JR, Lozano JA.
  TITLE     Molecular mechanism for catalysis by a new zinc-enzyme, dopachrome
            tautomerase.
  JOURNAL   Biochem. J. 313 ( Pt 2) (1996) 447-53.
  ORGANISM  mouse [GN:mmu]
REFERENCE   2  [PMID:2106316]
  AUTHORS   Pawelek JM.
  TITLE     Dopachrome conversion factor functions as an isomerase.
  JOURNAL   Biochem. Biophys. Res. Commun. 166 (1990) 1328-33.
  ORGANISM  mouse [GN:mmu]
REFERENCE   3  [PMID:9794786]
  AUTHORS   Pennock JL, Behnke JM, Bickle QD, Devaney E, Grencis RK, Isaac RE,
            Joshua GW, Selkirk ME, Zhang Y, Meyer DJ.
  TITLE     Rapid purification and characterization of L-dopachrome-methyl ester
            tautomerase (macrophage-migration-inhibitory factor) from
            Trichinella spiralis, Trichuris muris and Brugia pahangi.
  JOURNAL   Biochem. J. 335 ( Pt 3) (1998) 495-8.
  ORGANISM  Trichinella spiralis, Trichuris muris, Brugia pahangi
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map04916  Melanogenesis
ORTHOLOGY   KO: K01827  dopachrome tautomerase
GENES       HSA: 1638(DCT)
            MMU: 13190(Dct)
            RNO: 290484(RGD1564975_predicted)
            CFA: 485520(DCT)
            BTA: 280761(DCT)
            SSC: 574066(DCT)
            GGA: 395775(DCT)
            DRE: 58074(dct)
            DME: Dmel_CG18550(yellow-f) Dmel_CG8063(yellow-f2)
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.3.12
            ExPASy - ENZYME nomenclature database: 5.3.3.12
            ExplorEnz - The Enzyme Database: 5.3.3.12
            ERGO genome analysis and discovery system: 5.3.3.12
            BRENDA, the Enzyme Database: 5.3.3.12
            CAS: 130122-81-5
///
ENTRY       EC 5.3.3.13                 Enzyme
NAME        polyenoic fatty acid isomerase;
            PFI;
            eicosapentaenoate cis-Delta5,8,11,14,17-eicosapentaenoate
            cis-Delta5-trans-Delta7,9-cis-Delta14,17 isomerase;
            (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate Delta8,11-Delta7,8-isomerase
            (incorrect);
            (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate Delta8,11-Delta7,9-isomerase
            (trans-double-bond-forming)
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing C=C bonds
SYSNAME     (5Z,8Z,11Z,14Z,17Z)-icosapentaenoate Delta8,11-Delta7,9-isomerase
            (trans-double-bond-forming)
REACTION    (5Z,8Z,11Z,14Z,17Z)-icosapentaenoate =
            (5Z,7E,9E,14Z,17Z)-icosapentaenoate [RN:R06502]
ALL_REAC    R06502
SUBSTRATE   (5Z,8Z,11Z,14Z,17Z)-icosapentaenoate
PRODUCT     (5Z,7E,9E,14Z,17Z)-icosapentaenoate
COMMENT     The enzyme from the red alga Ptilota filicina catalyses the
            isomerization of skip dienes (methylene-interrupted double bonds) in
            a broad range of fatty acids and fatty-acid analogues, such as
            arachidonate and gamma-linolenate, to yield a conjugated triene.
REFERENCE   1  [PMID:7803384]
  AUTHORS   Wise ML, Hamberg M, Gerwick WH.
  TITLE     Biosynthesis of conjugated triene-containing fatty acids by a novel
            isomerase from the red marine alga Ptilota filicina.
  JOURNAL   Biochemistry. 33 (1994) 15223-32.
  ORGANISM  Ptilota filicina
REFERENCE   2  [PMID:8575565]
  AUTHORS   Wise ML, Soderstrom K, Murray TF, Gerwick WH.
  TITLE     Synthesis and cannabinoid receptor binding activity of conjugated
            triene anandamide, a novel eicosanoid.
  JOURNAL   Experientia. 52 (1996) 88-92.
REFERENCE   3  [PMID:9062129]
  AUTHORS   Wise ML, Rossi J, Gerwick WH.
  TITLE     Characterization of the substrate binding site of polyenoic fatty
            acid isomerase, a novel enzyme from the marine alga Ptilota
            filicina.
  JOURNAL   Biochemistry. 36 (1997) 2985-92.
  ORGANISM  Ptilota filicina
REFERENCE   4  [PMID:12054482]
  AUTHORS   Zheng W, Wise ML, Wyrick A, Metz JG, Yuan L, Gerwick WH.
  TITLE     Polyenoic fatty acid isomerase from the marine alga Ptilota
            filicina: protein characterization and functional expression of the
            cloned cDNA.
  JOURNAL   Arch. Biochem. Biophys. 401 (2002) 11-20.
  ORGANISM  Ptilota filicina
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.3.13
            ExPASy - ENZYME nomenclature database: 5.3.3.13
            ExplorEnz - The Enzyme Database: 5.3.3.13
            ERGO genome analysis and discovery system: 5.3.3.13
            BRENDA, the Enzyme Database: 5.3.3.13
///
ENTRY       EC 5.3.3.14                 Enzyme
NAME        trans-2-decenoyl-[acyl-carrier protein] isomerase;
            beta-hydroxydecanoyl thioester dehydrase;
            trans-2-cis-3-decenoyl-ACP isomerase;
            trans-2,cis-3-decenoyl-ACP isomerase;
            trans-2-decenoyl-ACP isomerase;
            FabM
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing C=C bonds
SYSNAME     decenoyl-[acyl-carrier-protein] Delta2-trans-Delta3-cis-isomerase
REACTION    trans-dec-2-enoyl-[acyl-carrier-protein] =
            cis-dec-3-enoyl-[acyl-carrier-protein] [RN:R07639]
ALL_REAC    R07639
SUBSTRATE   trans-dec-2-enoyl-[acyl-carrier-protein]
PRODUCT     cis-dec-3-enoyl-[acyl-carrier-protein]
COMMENT     While the enzyme from Escherichia coli is highly specific for the
            10-carbon enoyl-ACP, the enzyme from Streptococcus pneumoniae can
            also use the 12-carbon enoyl-ACP as substrate in vitro but not 14-
            or 16-carbon enoyl-ACPs [3]. ACP can be replaced by either CoA or
            N-acetylcysteamine thioesters. The cis-3-enoyl product is required
            to form unsaturated fatty acids, such as palmitoleic acid and
            cis-vaccenic acid, in dissociated (or type II) fatty-acid
            biosynthesis.
REFERENCE   1  [PMID:4863740]
  AUTHORS   Brock DJ, Kass LR, Bloch K.
  TITLE     Beta-hydroxydecanoyl thioester dehydrase. II. Mode of action.
  JOURNAL   J. Biol. Chem. 242 (1967) 4432-40.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Bloch, K.
  TITLE     Enzymatic synthesis of monounsaturated fatty acids.
  JOURNAL   Acc. Chem. Res. 2 (1969) 193-202.
REFERENCE   3  [PMID:12237320]
  AUTHORS   Marrakchi H, Choi KH, Rock CO.
  TITLE     A new mechanism for anaerobic unsaturated fatty acid formation in
            Streptococcus pneumoniae.
  JOURNAL   J. Biol. Chem. 277 (2002) 44809-16.
  ORGANISM  Streptococcus pneumoniae
REFERENCE   4
  AUTHORS   Cronan, J.E., Jr. and Rock, C.O.
  TITLE     Biosynthesis of membrane lipids.
  JOURNAL   In: Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular
            and Molecular Biology, 2nd ed., vol. 1, ASM Press, Washington, DC,
            1996, p. 612-636.
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.3.14
            ExPASy - ENZYME nomenclature database: 5.3.3.14
            ExplorEnz - The Enzyme Database: 5.3.3.14
            ERGO genome analysis and discovery system: 5.3.3.14
            BRENDA, the Enzyme Database: 5.3.3.14
            CAS: 9030-80-2
///
ENTRY       EC 5.3.3.15                 Enzyme
NAME        ascopyrone tautomerase;
            ascopyrone isomerase;
            ascopyrone intramolecular oxidoreductase;
            1,5-anhydro-D-glycero-hex-3-en-2-ulose tautomerase;
            APM tautomerase;
            ascopyrone P tautomerase;
            APTM
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing C=C bonds
SYSNAME     1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose
            Delta3-Delta1-isomerase
REACTION    1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose =
            1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose
SUBSTRATE   1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose
PRODUCT     1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose
COMMENT     This enzyme catalyses one of the steps in the anhydrofructose
            pathway, which leads to the degradation of glycogen and starch via
            1,5-anhydro-D-fructose [1,2]. The other enzymes involved in this
            pathway are EC 4.2.1.110 (aldos-2-ulose dehydratase), EC 4.2.1.111
            (1,5-anhydro-D-fructose dehydratase) and EC 4.2.2.13
            [exo-(1->4)-alpha-D-glucan lyase]. Ascopyrone P is an anti-oxidant
            [2].
REFERENCE   1  [PMID:15110094]
  AUTHORS   Yu S, Refdahl C, Lundt I.
  TITLE     Enzymatic description of the anhydrofructose pathway of glycogen
            degradation; I. Identification and purification of anhydrofructose
            dehydratase, ascopyrone tautomerase and alpha-1,4-glucan lyase in
            the fungus Anthracobia melaloma.
  JOURNAL   Biochim. Biophys. Acta. 1672 (2004) 120-9.
REFERENCE   2  [PMID:16822618]
  AUTHORS   Yu S, Fiskesund R.
  TITLE     The anhydrofructose pathway and its possible role in stress response
            and signaling.
  JOURNAL   Biochim. Biophys. Acta. 1760 (2006) 1314-22.
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.3.15
            ExPASy - ENZYME nomenclature database: 5.3.3.15
            ExplorEnz - The Enzyme Database: 5.3.3.15
            ERGO genome analysis and discovery system: 5.3.3.15
            BRENDA, the Enzyme Database: 5.3.3.15
///
ENTRY       EC 5.3.3.-                  Enzyme
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing C=C bonds
REACTION    (1) 2-Oxohept-3-enedioate <=> 2-Hydroxyhepta-2,4-dienedioate
            [RN:R04134];
            (2) 12-Oxo-9(Z)-dodecenoic acid <=> Traumatin [RN:R07872]
SUBSTRATE   2-Hydroxymuconate [CPD:C02501];
            2-Oxohept-3-enedioate [CPD:C03063]
PRODUCT     (Z)-5-Oxohex-2-enedioate [CPD:C03453];
            2-Hydroxyhepta-2,4-dienedioate [CPD:C05600]
///
ENTRY       EC 5.3.4.1                  Enzyme
NAME        protein disulfide-isomerase;
            S-S rearrangase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Transposing S-S bonds
SYSNAME     protein disulfide-isomerase
REACTION    Catalyses the rearrangement of -S-S- bonds in proteins
COMMENT     Needs reducing agents or partly reduced enzyme; the reaction depends
            on sulfhydryl-disulfide interchange.
REFERENCE   1  [PMID:5946614]
  AUTHORS   De Lorenzo F, Goldberger RF, Steers E Jr, Givol D, Anfinsen B.
  TITLE     Purification and properties of an enzyme from beef liver which
            catalyzes sulfhydryl-disulfide interchange in proteins.
  JOURNAL   J. Biol. Chem. 241 (1966) 1562-7.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:6022836]
  AUTHORS   Fuchs S, De Lorenzo F, Anfinsen CB.
  TITLE     Studies on the mechanism of the enzymic catalysis of disulfide
            interchange in proteins.
  JOURNAL   J. Biol. Chem. 242 (1967) 398-402.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map04612  Antigen processing and presentation
ORTHOLOGY   KO: K01829  protein disulfide-isomerase
            KO: K03981  thiol:disulfide interchange protein DsbC
            KO: K08056  protein disulfide isomerase family A, member 3
            KO: K09580  prolyl 4-hydroxylase, beta polypeptide
            KO: K09581  protein disulfide isomerase family A, member 2
            KO: K09582  protein disulfide isomerase family A, member 4
            KO: K09583  protein disulfide isomerase family A, member 5
            KO: K09584  protein disulfide isomerase family A, member 6
            KO: K09585  thioredoxin domain-containing protein 10
GENES       HSA: 10130(PDIA6) 10954(PDIA5) 2923(PDIA3) 5034(P4HB)
                 54495(TXNDC10) 64714(PDIA2) 9601(PDIA4)
            PTR: 454970(P4HB)
            MMU: 12304(Pdia4) 14827(Pdia3) 18453(P4hb) 67988(Txndc10)
                 69191(Pdia2) 71853(Pdia6) 72599(Pdia5)
            RNO: 116598(Pdia4) 25506(P4hb) 286906(Pdia6)
                 287164(Pdia2_predicted) 29468(Pdia3) 360722(Pdia5)
                 682967(LOC682967)
            CFA: 475668(PDIA6) 476176(TXNDC10) 478279(PDIA3) 478589(PDIA5)
                 482715(PDIA4) 483369(P4HB)
            BTA: 281373(P4HB) 281803(GRP58) 415110(PDIA4) 504356(MGC157374)
                 511603(PDIA5) 511898(LOC511898)
            GGA: 373899(PDIA3) 396376(GSBP9) 420785(PDIA4) 421027(TXNDC10)
                 421940(PDIA6) 424249(PDIA5)
            XLA: 379505(MGC64309) 379743(grp58) 379997(pdip5) 399248(P4hb)
                 444355(MGC82829) 446435(MGC84594) 446478(MGC79068)
                 495169(LOC495169)
            XTR: 394954(MGC75624) 395048(p4hb) 493341(MGC89831) 496734(pdia2)
                 550094(LOC550094)
            DRE: 322160(pdip5) 405841(zgc:77086) 445123(zgc:100906)
                 553250(zgc:152808) 556162(LOC556162)
            SPU: 373305(ECaSt/PDI) 576717(LOC576717) 577673(LOC577673)
                 585584(LOC585584) 586525(LOC586525)
            DME: Dmel_CG1837 Dmel_CG5027 Dmel_CG5809 Dmel_CG6988(Pdi)
                 Dmel_CG8983 Dmel_CG9302 Dmel_CG9432(l(2)01289)
            CEL: B0403.4(tag-320) C07A12.4(pdi-2) C14B9.2(erp72)
                 H06O01.1(pdi-3) ZK973.11(thioredoxin)
            ATH: AT1G77510(ATPDIL1-2) AT2G32920(ATPDIL2-3)
            OSA: 4326806 4327971 4337858 4347226
            CME: CMC180C CMK015C
            SCE: YCL043C(PDI1) YDR518W(EUG1) YIL005W(EPS1) YOR288C(MPD1)
            AGO: AGOS_AFR559C AGOS_AFR718W
            PIC: PICST_32213 PICST_50192
            CGR: CAGL0B00704g
            SPO: SPAC13F5.05 SPAC17H9.14c SPAC1F5.02
            ANI: AN0075.2 AN0248.2 AN7436.2
            AFM: AFUA_1G05320 AFUA_2G06150 AFUA_2G10590 AFUA_5G12260
            AOR: AO090001000733 AO090003000829 AO090120000344
            ANG: An01g04600(prpA) An02g14800(pdiA) An18g02020(tigA)
            CNE: CNA00620 CNM02410
            UMA: UM01802.1 UM02443.1 UM05352.1
            DDI: DDBDRAFT_0167375 DDBDRAFT_0217531 DDB_0185040(disA)
                 DDB_0231409
            PFA: MAL8P1.17 PF11_0352 PF13_0272 PF14_0694 PFI0950w
            CPV: cgd6_120 cgd7_4080
            CHO: Chro.60023 Chro.70453
            TAN: TA04450 TA06075 TA12705 TA14090 TA19010
            TPV: TP01_0863 TP03_0419
            TET: TTHERM_00549480 TTHERM_01005160 TTHERM_01018410
            TBR: Tb10.6k15.2290 Tb927.4.2450 Tb927.7.1300 Tb927.7.5790
            TCR: 506247.10 507611.370 508173.150 508209.140
            LMA: LmjF06.1050 LmjF26.0660 LmjF36.6940
            EHI: 186.t00012 206.t00013 253.t00005 41.t00018 5.t00007 61.t00017
                 81.t00029
            ECO: b2893(dsbC)
            ECJ: JW2861(dsbC)
            ECE: Z4231(dsbC)
            ECS: ECs3765
            ECC: c3473(dsbC)
            ECI: UTI89_C0607(dsbG) UTI89_C3278(dsbC)
            ECP: ECP_2886
            ECV: APECO1_3634(dsbC)
            STY: STY3199(dsbC)
            STT: t2961(dsbC)
            SPT: SPA2911(dsbC)
            SEC: SC2983(dsbC)
            STM: STM3043(dsbC)
            YPE: YPO0891(dsbC)
            YPK: y3275(dsbC)
            YPM: YP_3587(dsbC)
            YPA: YPA_0378
            YPN: YPN_3090
            YPS: YPTB3166(dsbC)
            SFL: SF2879(dsbC)
            SFX: S3078(dsbC)
            SFV: SFV_2941(dsbC)
            SSN: SSON_3046(dsbC)
            SBO: SBO_3099(dsbC)
            SDY: SDY_3189(dsbC)
            ECA: ECA0771(dsbC)
            PLU: plu3551(dsbC)
            SGL: SG1992
            HIN: HI1213(dsbC)
            HIT: NTHI1384(dsbC)
            HDU: HD1340(dsbC)
            HSO: HS_1475(dsbC)
            PMU: PM0191(dsbC)
            MSU: MS1540(dsbG)
            APL: APL_0458(dsbC)
            XFA: XF1424
            XFT: PD0651(dsbC)
            XCC: XCC0655(dsbC) XCC3823
            XCB: XC_3579 XC_3895
            XCV: XCV3675(dsbC) XCV3996 XCVd0137(dsbC)
            XAC: XAC3550(dsbC) XAC3878
            XOO: XOO0840(dsbC) XOO4131
            XOM: XOO_0765(XOO0765) XOO_3910(XOO3910)
            VCH: VC2418(dsbC)
            VCO: VC0395_A2485(tpcG)
            VVU: VV1_0529
            VVY: VV0666
            VPA: VP0510(dsbC)
            VFI: VF0449(dsbC)
            PPR: PBPRA0567
            PAE: PA3737(dsbC)
            PAU: PA14_16050(dsbC)
            PAP: PSPA7_3138
            PPU: PP_1469(dsbC)
            PST: PSPTO_1479(dsbC)
            PSB: Psyr_1289
            PSP: PSPPH_1359(dsbC)
            PFL: PFL_1102
            PFO: Pfl_1026
            PEN: PSEEN4253(dsbC)
            PAR: Psyc_0254(dsbC)
            PCR: Pcryo_0280
            ACI: ACIAD0045(dsbA) ACIAD0265(dsbC) ACIAD3673
            SON: SO_0951(dsbC)
            SDN: Sden_0748
            SFR: Sfri_0664
            SAZ: Sama_2738
            SLO: Shew_0771
            SHE: Shewmr4_0796
            SHM: Shewmr7_3227
            SHN: Shewana3_3330
            ILO: IL0825(dsbC)
            CPS: CPS_4095(dsbC) CPS_4348(dsbA)
            PHA: PSHAa0248(dsbA) PSHAa0249(porA) PSHAa0515(dsbC)
            PAT: Patl_3713
            SDE: Sde_1208
            MAQ: Maqu_2275
            MCA: MCA0575(dsbC) MCA2602(dsbA)
            TCX: Tcr_0652
            NOC: Noc_2253(dsbC)
            AEH: Mlg_1487
            HCH: HCH_01777(dsbC)
            CSA: Csal_3011
            ABO: ABO_0804(dsbC)
            AHA: AHA_3271(dsbC)
            DNO: DNO_1317(dsbC)
            BCI: BCI_0257(dsbA)
            NME: NMB0550(dsbC)
            NMA: NMA0730
            NGO: NGO1438
            CVI: CV_1325 CV_3119(dsbC)
            RSO: RSc2892(dsbC)
            REU: Reut_A3035
            REH: H16_A3331
            RME: Rmet_3190 Rmet_6169
            BMA: BMAA0525
            BXE: Bxe_A0453
            BUR: Bcep18194_A3613 Bcep18194_A5129
            BCN: Bcen_2579
            BCH: Bcen2424_0526
            BAM: Bamb_0431
            BPS: BPSL3058(dsbC)
            BPM: BURPS1710b_0590(dsbA) BURPS1710b_3584(dsbC)
            BPL: BURPS1106A_0428
            BTE: BTH_I2917
            BPE: BP3270
            BPA: BPP4150(dsbC)
            BBR: BB4620(dsbC)
            RFR: Rfer_1575
            POL: Bpro_1124 Bpro_3505
            MPT: Mpe_A0592
            MMS: mma_0230
            NEU: NE0516 NE1511(dsbC)
            NET: Neut_1688
            NMU: Nmul_A2445
            EBA: ebA4099(dsbC) ebA6610(dsbC)
            AZO: azo0321(cutA2) azo0382(dsbA) azo0724(dsbC) azo3929(ccmG)
            DAR: Daro_2318 Daro_3509
            TBD: Tbd_2331(dsbC)
            MFA: Mfla_2143
            HAC: Hac_0489(dsbC)
            GSU: GSU0850
            GME: Gmet_1150
            PCA: Pcar_2069(dsbC)
            SAT: SYN_03114
            RLE: RL2388
            ELI: ELI_00900(dsbC)
            RRU: Rru_A3433
            BCZ: BCZK0249(frnE)
            BTL: BALH_0269(frnE)
            BPU: BPUM_2331
            RBA: RB13184(dsbD) RB4606 RB5897(trx)
            CTR: CT780 CT783
            CTA: CTA_0850 CTA_0853
            CMU: TC0161 TC0166
            CPN: CPn0926 CPn0933
            CPA: CP0928 CP0940
            CPJ: CPj0926 CPj0933
            CPT: CpB0958 CpB0968
            CCA: CCA00836 CCA00842
            CAB: CAB805 CAB808
            CFE: CF0173(dsbD1) CF0177(dsbD2)
            AVA: Ava_0187 Ava_1747 Ava_3763 Ava_4761
            CHU: CHU_2493(dsb) CHU_3640(dsbC)
            CCH: Cag_1150
            AAE: aq_1740 aq_1811(trxA2) aq_2093(dsbC)
STRUCTURES  PDB: 1BJX  1EEJ  1G0T  1MEK  1T3B  1TJD  1X5C  1X5D  2ALB  2B5E  
                 2BJX  2DJ1  2DJ2  2DJ3  2DJJ  2DJK  2DML  2DMM  2H8L  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.4.1
            ExPASy - ENZYME nomenclature database: 5.3.4.1
            ExplorEnz - The Enzyme Database: 5.3.4.1
            ERGO genome analysis and discovery system: 5.3.4.1
            BRENDA, the Enzyme Database: 5.3.4.1
            CAS: 37318-49-3
///
ENTRY       EC 5.3.99.1       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Other intramolecular oxidoreductases
COMMENT     Deleted entry: hydroperoxide isomerase. Reaction due to combined
            action of EC 4.2.1.92 (hydroperoxide dehydratase) and EC 5.3.99.6
            (allene-oxide cyclase) (EC 5.3.99.1 created 1972, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.99.1
            ExPASy - ENZYME nomenclature database: 5.3.99.1
            ExplorEnz - The Enzyme Database: 5.3.99.1
            ERGO genome analysis and discovery system: 5.3.99.1
            BRENDA, the Enzyme Database: 5.3.99.1
///
ENTRY       EC 5.3.99.2                 Enzyme
NAME        prostaglandin-D synthase;
            prostaglandin-H2 Delta-isomerase;
            prostaglandin-R-prostaglandin D isomerase;
            PGH-PGD isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Other intramolecular oxidoreductases
SYSNAME     (5,13)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
            Delta-isomerase
REACTION    (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-
            dienoate =
            (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
            [RN:R02266]
ALL_REAC    R02266
SUBSTRATE   (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-
            dienoate [CPD:C00427]
PRODUCT     (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
            [CPD:C00696]
COMMENT     Brings about the opening of the epidioxy bridge. Some enzymes
            require glutathione.
REFERENCE   1  [PMID:32914]
  AUTHORS   Christ-Hazelhof E, Nugteren DH.
  TITLE     Purification and characterisation of prostaglandin endoperoxide
            D-isomerase, a cytoplasmic, glutathione-requiring enzyme.
  JOURNAL   Biochim. Biophys. Acta. 572 (1979) 43-51.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:109431]
  AUTHORS   Shimizu T, Yamamoto S, Hayaishi O.
  TITLE     Purification and properties of prostaglandin D synthetase from rat
            brain.
  JOURNAL   J. Biol. Chem. 254 (1979) 5222-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00590  Arachidonic acid metabolism
ORTHOLOGY   KO: K01830  prostaglandin-H2 D-isomerase
GENES       HSA: 27306(PGDS) 5730(PTGDS)
            MMU: 19215(Ptgds)
            RNO: 25526(Ptgds) 58962(Ptgds2)
            CFA: 403740(PTGDS) 478481(LOC478481)
            BTA: 286858(PTGDS)
            SSC: 397456(PTGDS)
            GGA: 374110(PTGDS) 395863(PGDS)
            XLA: 397884(cpl-1)
STRUCTURES  PDB: 1IYH  1IYI  1PD2  1V40  2CZT  2CZU  2E4J  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.99.2
            ExPASy - ENZYME nomenclature database: 5.3.99.2
            ExplorEnz - The Enzyme Database: 5.3.99.2
            ERGO genome analysis and discovery system: 5.3.99.2
            BRENDA, the Enzyme Database: 5.3.99.2
            CAS: 65802-85-9
///
ENTRY       EC 5.3.99.3                 Enzyme
NAME        prostaglandin-E synthase;
            prostaglandin-H2 E-isomerase;
            endoperoxide isomerase;
            endoperoxide isomerase;
            prostaglandin R-prostaglandin E isomerase;
            prostaglandin endoperoxide E isomerase;
            PGE isomerase;
            PGH-PGE isomerase;
            PGE2 isomerase;
            prostaglandin endoperoxide E2 isomerase;
            prostaglandin H-E isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Other intramolecular oxidoreductases
SYSNAME     (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoat
            e E-isomerase
REACTION    (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-
            dienoate =
            (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate
            [RN:R02265]
ALL_REAC    R02265
SUBSTRATE   (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-
            dienoate [CPD:C00427]
PRODUCT     (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate
            [CPD:C00584]
COFACTOR    Glutathione [CPD:C00051]
COMMENT     Brings about the opening of the epidioxy bridge. Requires
            glutathione.
REFERENCE   1  [PMID:838703]
  AUTHORS   Ogino N, Miyamoto T, Yamamoto S, Hayaishi O.
  TITLE     Prostaglandin endoperoxide E isomerase from bovine vesicular gland
            microsomes, a glutathione-requiring enzyme.
  JOURNAL   J. Biol. Chem. 252 (1977) 890-5.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:3100531]
  AUTHORS   Tanaka Y, Ward SL, Smith WL.
  TITLE     Immunochemical and kinetic evidence for two different prostaglandin
            H-prostaglandin E isomerases in sheep vesicular gland microsomes.
  JOURNAL   J. Biol. Chem. 262 (1987) 1374-81.
  ORGANISM  sheep
PATHWAY     PATH: map00590  Arachidonic acid metabolism
ORTHOLOGY   KO: K05309  prostaglandin-E synthase
GENES       HSA: 80142(PTGES2) 9536(PTGES)
            PTR: 473071(PTGES)
            MMU: 64292(Ptges) 96979(Ptges2)
            RNO: 59103(Ptges)
            CFA: 480698(PTGES)
            BTA: 282019(PTGES)
            GGA: 417193(PTGES) 417214(PTGES2)
            DRE: 393250(ptgesl)
STRUCTURES  PDB: 1Z9H  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.99.3
            ExPASy - ENZYME nomenclature database: 5.3.99.3
            ExplorEnz - The Enzyme Database: 5.3.99.3
            ERGO genome analysis and discovery system: 5.3.99.3
            BRENDA, the Enzyme Database: 5.3.99.3
            CAS: 52227-79-9
///
ENTRY       EC 5.3.99.4                 Enzyme
NAME        prostaglandin-I synthase;
            prostacyclin synthase;
            prostacycline synthetase;
            prostagladin I2 synthetase;
            PGI2 synthase;
            PGI2 synthetase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Other intramolecular oxidoreductases
SYSNAME     (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoat
            e 6-isomerase
REACTION    (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-
            dienoate =
            (5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-
            dienoate [RN:R02267]
ALL_REAC    R02267
SUBSTRATE   (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-
            dienoate [CPD:C00427]
PRODUCT     (5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-
            dienoate [CPD:C01312]
COFACTOR    Heme [CPD:C00032]
COMMENT     Converts prostaglandin H2 into prostaglandin I2 (prostacyclin). A
            heme-thiolate protein.
REFERENCE   1  [PMID:6338016]
  AUTHORS   DeWitt DL, Smith WL.
  TITLE     Purification of prostacyclin synthase from bovine aorta by
            immunoaffinity  chromatography. Evidence that the enzyme is a
            hemoprotein.
  JOURNAL   J. Biol. Chem. 258 (1983) 3285-93.
  ORGANISM  cow [GN:bta]
REFERENCE   2  [PMID:7023490]
  AUTHORS   Ullrich V, Castle L, Weber P.
  TITLE     Spectral evidence for the cytochrome P450 nature of prostacyclin
            synthetase.
  JOURNAL   Biochem. Pharmacol. 30 (1981) 2033-6.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00590  Arachidonic acid metabolism
ORTHOLOGY   KO: K01831  cytochrome P450, family 8, subfamily A (Prostacyclin
                        synthase)
GENES       HSA: 5740(PTGIS)
            MMU: 19223(Ptgis)
            RNO: 25527(Ptgis)
            CFA: 485919(PTGIS)
            BTA: 282021(PTGIS)
STRUCTURES  PDB: 2IAG  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.99.4
            ExPASy - ENZYME nomenclature database: 5.3.99.4
            ExplorEnz - The Enzyme Database: 5.3.99.4
            ERGO genome analysis and discovery system: 5.3.99.4
            BRENDA, the Enzyme Database: 5.3.99.4
            CAS: 65802-86-0
///
ENTRY       EC 5.3.99.5                 Enzyme
NAME        thromboxane-A synthase;
            thromboxane synthase;
            (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-
            dienoate thromboxane-A2-isomerase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Other intramolecular oxidoreductases
SYSNAME     (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoat
            e isomerase
REACTION    (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-
            dienoate =
            (5Z,13E)-(15S)-9alpha,11alpha-epoxy-15-hydroxythromboxa-5,13-
            dienoate [RN:R02268]
ALL_REAC    R02268
SUBSTRATE   (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-
            dienoate [CPD:C00427]
PRODUCT     (5Z,13E)-(15S)-9alpha,11alpha-epoxy-15-hydroxythromboxa-5,13-
            dienoate [CPD:C02198]
COFACTOR    Heme [CPD:C00032]
COMMENT     Converts prostaglandin H2 into thromboxane A2. A heme-thiolate
            protein.
REFERENCE   1  [PMID:3745158]
  AUTHORS   Shen RF, Tai HH.
  TITLE     Immunoaffinity purification and characterization of thromboxane
            synthase from porcine lung.
  JOURNAL   J. Biol. Chem. 261 (1986) 11592-9.
  ORGANISM  pig [GN:ssc]
REFERENCE   2
  AUTHORS   Ullrich, V. and Haurand, M.
  TITLE     Thromboxane synthase as a cytochrome P450 enzyme.
  JOURNAL   Adv. Prostaglandin Thromboxane Res. 11 (1983) 105-110.
PATHWAY     PATH: map00590  Arachidonic acid metabolism
ORTHOLOGY   KO: K01832  cytochrome P450, family 5, subfamily A (thromboxane-A
                        synthase)
GENES       HSA: 6916(TBXAS1)
            PTR: 463774(TBXAS1)
            MMU: 21391(Tbxas1)
            RNO: 24886(Tbxas1)
            CFA: 482771(LOC482771)
            SSC: 397112(TBXAS1)
            GGA: 418101(LOC418101)
            XLA: 379702(MGC68990)
            DRE: 402902(zgc:136708)
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.99.5
            ExPASy - ENZYME nomenclature database: 5.3.99.5
            ExplorEnz - The Enzyme Database: 5.3.99.5
            ERGO genome analysis and discovery system: 5.3.99.5
            BRENDA, the Enzyme Database: 5.3.99.5
            CAS: 61276-89-9
///
ENTRY       EC 5.3.99.6                 Enzyme
NAME        allene-oxide cyclase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Other intramolecular oxidoreductases
SYSNAME     (9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate isomerase
            (cyclizing)
REACTION    (9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate =
            (15Z)-12-oxophyto-10,15-dienoate [RN:R03402]
ALL_REAC    R03402
SUBSTRATE   (9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate [CPD:C04672]
PRODUCT     (15Z)-12-oxophyto-10,15-dienoate [CPD:C01226]
COMMENT     Allene oxides formed by the action of EC 4.2.1.92 hydroperoxide
            dehydratase, are converted into cyclopentenone derivatives.
REFERENCE   1  [PMID:3178850]
  AUTHORS   Hamberg M.
  TITLE     Biosynthesis of 12-oxo-10,15(Z)-phytodienoic acid: identification of
            an allene oxide cyclase.
  JOURNAL   Biochem. Biophys. Res. Commun. 156 (1988) 543-50.
  ORGANISM  Zea mays [GN:ezma]
PATHWAY     PATH: map00592  alpha-Linolenic acid metabolism
ORTHOLOGY   KO: K10525  allene oxide cyclase
GENES       ATH: AT1G13280(AOC4) AT3G25760(AOC1) AT3G25770(AOC2)
                 AT3G25780(AOC3)
            OSA: 4333201
STRUCTURES  PDB: 1Z8K  1ZVC  2BRJ  2DIO  2GIN  2Q4I  
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.99.6
            ExPASy - ENZYME nomenclature database: 5.3.99.6
            ExplorEnz - The Enzyme Database: 5.3.99.6
            ERGO genome analysis and discovery system: 5.3.99.6
            BRENDA, the Enzyme Database: 5.3.99.6
            CAS: 118390-59-3
///
ENTRY       EC 5.3.99.7                 Enzyme
NAME        styrene-oxide isomerase;
            SOI
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Other intramolecular oxidoreductases
SYSNAME     styrene-oxide isomerase (epoxide-cleaving)
REACTION    styrene oxide = phenylacetaldehyde [RN:R02615]
ALL_REAC    R02615
SUBSTRATE   styrene oxide [CPD:C02083]
PRODUCT     phenylacetaldehyde [CPD:C00601]
COMMENT     Highly specific.
REFERENCE   1  [PMID:16348047]
  AUTHORS   Hartmans S, Smits JP, van der Werf MJ, Volkering F, de Bont JA.
  TITLE     Metabolism of Styrene Oxide and 2-Phenylethanol in the
            Styrene-Degrading Xanthobacter Strain 124X.
  JOURNAL   Appl. Environ. Microbiol. 55 (1989) 2850-2855.
  ORGANISM  Xanthobacter sp.
PATHWAY     PATH: map00643  Styrene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.99.7
            ExPASy - ENZYME nomenclature database: 5.3.99.7
            ExplorEnz - The Enzyme Database: 5.3.99.7
            ERGO genome analysis and discovery system: 5.3.99.7
            UM-BBD (Biocatalysis/Biodegradation Database): 5.3.99.7
            BRENDA, the Enzyme Database: 5.3.99.7
            CAS: 124541-89-5
///
ENTRY       EC 5.3.99.8                 Enzyme
NAME        capsanthin/capsorubin synthase;
            CCS;
            ketoxanthophyll synthase;
            capsanthin-capsorubin synthase
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Other intramolecular oxidoreductases
SYSNAME     violaxanthin---capsorubin isomerase (ketone-forming)
REACTION    (1) violaxanthin = capsorubin [RN:R07320];
            (2) antheraxanthin = capsanthin [RN:R07321]
ALL_REAC    R07320 R07321
SUBSTRATE   violaxanthin [CPD:C08614];
            antheraxanthin [CPD:C08579]
PRODUCT     capsorubin [CPD:C08585];
            capsanthin [CPD:C08584]
COMMENT     This multifunctional enzyme is induced during chromoplast
            differentiation in plants [1]. Isomerization of the epoxide ring of
            violaxanthin gives the cyclopentyl-ketone of capsorubin or
            capsanthin.
REFERENCE   1  [PMID:7920703]
  AUTHORS   Bouvier F, Hugueney P, d'Harlingue A, Kuntz M, Camara B.
  TITLE     Xanthophyll biosynthesis in chromoplasts: isolation and molecular
            cloning of an enzyme catalyzing the conversion of
            5,6-epoxycarotenoid into ketocarotenoid.
  JOURNAL   Plant. J. 6 (1994) 45-54.
  ORGANISM  Capsicum annuum
REFERENCE   2  [PMID:9526511]
  AUTHORS   Lefebvre V, Kuntz M, Camara B, Palloix A.
  TITLE     The capsanthin-capsorubin synthase gene: a candidate gene for the y
            locus controlling the red fruit colour in pepper.
  JOURNAL   Plant. Mol. Biol. 36 (1998) 785-9.
  ORGANISM  Capsicum annuum
REFERENCE   3  [PMID:12549109]
  AUTHORS   Xu CJ, Chen DM, Zhang SL.
  TITLE     [Molecular cloning of full length capsanthin/capsorubin synthase
            homologous gene from orange (Citrus sinensis)]
  JOURNAL   Shi. Yan. Sheng. Wu. Xue. Bao. 34 (2001) 147-50.
  ORGANISM  Citrus sinensis [GN:ecsi]
PATHWAY     PATH: map00906  Carotenoid biosynthesis - General
GENES       RRS: RoseRS_2643
            RCA: Rcas_2711
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.99.8
            ExPASy - ENZYME nomenclature database: 5.3.99.8
            ExplorEnz - The Enzyme Database: 5.3.99.8
            ERGO genome analysis and discovery system: 5.3.99.8
            BRENDA, the Enzyme Database: 5.3.99.8
///
ENTRY       EC 5.3.99.9                 Enzyme
NAME        neoxanthin synthase;
            NSY
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Other intramolecular oxidoreductases
SYSNAME     violaxanthin---neoxanthin isomerase (epoxide-opening)
REACTION    violaxanthin = neoxanthin [RN:R06948]
ALL_REAC    R06948
SUBSTRATE   violaxanthin [CPD:C08614]
PRODUCT     neoxanthin [CPD:C08606]
COMMENT     The opening of the epoxide ring of violaxanthin generates a chiral
            allene. Neoxanthin is a precursor of the plant hormone abscisic acid
            and the last product of carotenoid synthesis in green plants [2].
REFERENCE   1  [PMID:11094161]
  AUTHORS   Al-Babili S, Hugueney P, Schledz M, Welsch R, Frohnmeyer H, Laule O,
            Beyer P.
  TITLE     Identification of a novel gene coding for neoxanthin synthase from
            Solanum tuberosum.
  JOURNAL   FEBS. Lett. 485 (2000) 168-72.
  ORGANISM  Solanum tuberosum [GN:estu]
REFERENCE   2  [PMID:11029576]
  AUTHORS   Bouvier F, D'harlingue A, Backhaus RA, Kumagai MH, Camara B.
  TITLE     Identification of neoxanthin synthase as a carotenoid cyclase
            paralog.
  JOURNAL   Eur. J. Biochem. 267 (2000) 6346-52.
  ORGANISM  Lycopersicon esculentum [GN:eles]
PATHWAY     PATH: map00906  Carotenoid biosynthesis - General
DBLINKS     IUBMB Enzyme Nomenclature: 5.3.99.9
            ExPASy - ENZYME nomenclature database: 5.3.99.9
            ExplorEnz - The Enzyme Database: 5.3.99.9
            ERGO genome analysis and discovery system: 5.3.99.9
            BRENDA, the Enzyme Database: 5.3.99.9
///
ENTRY       EC 5.3.99.-                 Enzyme
CLASS       Isomerases;
            Intramolecular oxidoreductases;
            Other intramolecular oxidoreductases
REACTION    (1) trans-O-Hydroxybenzylidenepyruvate <=>
            2-Hydroxychromene-2-carboxylate [RN:R05137];
            (2) 2-Hydroxy-8-methylchromene-2-carboxylate <=>
            2-Hydroxy-3-methylbenzalpyruvate [RN:R06912];
            (3) 2-Carboxy-2-hydroxy-8-carboxychromene <=>
            2-Hydroxy-3-carboxybenzalpyruvate [RN:R06922];
            (4) 2-Hydroxy-7-hydroxymethylchromene-2-carboxylate <=>
            2-Hydroxy-4-hydroxymethylbenzalpyruvate [RN:R06933]
SUBSTRATE   trans-O-Hydroxybenzylidenepyruvate [CPD:C06203];
            2-Hydroxy-8-methylchromene-2-carboxylate [CPD:C14085];
            2-Carboxy-2-hydroxy-8-carboxychromene [CPD:C14094];
            2-Hydroxy-7-hydroxymethylchromene-2-carboxylate [CPD:C14106]
PRODUCT     2-Hydroxychromene-2-carboxylate [CPD:C06204];
            2-Hydroxy-3-methylbenzalpyruvate [CPD:C14086];
            2-Hydroxy-3-carboxybenzalpyruvate [CPD:C14095];
            2-Hydroxy-4-hydroxymethylbenzalpyruvate [CPD:C14107]
///
ENTRY       EC 5.4.1.1                  Enzyme
NAME        lysolecithin acylmutase;
            lysolecithin migratase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring acyl groups
SYSNAME     lysolecithin 2,3-acylmutase
REACTION    2-lysolecithin = 3-lysolecithin [RN:R03334]
ALL_REAC    R03334
SUBSTRATE   2-lysolecithin [CPD:C04230]
PRODUCT     3-lysolecithin [CPD:C04233]
REFERENCE   1
  AUTHORS   Uziel, M. and Hanahan, D.J.
  TITLE     An enzyme-catalyzed acyl migration: a lysolecithin migratase.
  JOURNAL   J. Biol. Chem. 226 (1957) 789-798.
  ORGANISM  Penicillium notatum
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.1.1
            ExPASy - ENZYME nomenclature database: 5.4.1.1
            ExplorEnz - The Enzyme Database: 5.4.1.1
            ERGO genome analysis and discovery system: 5.4.1.1
            BRENDA, the Enzyme Database: 5.4.1.1
            CAS: 9031-24-7
///
ENTRY       EC 5.4.1.2                  Enzyme
NAME        precorrin-8X methylmutase;
            precorrin isomerase;
            hydrogenobyrinic acid-binding protein
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring acyl groups
SYSNAME     precorrin-8X 11,12-methylmutase
REACTION    precorrin-8X = hydrogenobyrinate [RN:R05177]
ALL_REAC    R05177;
            (other) R05814
SUBSTRATE   precorrin 8X [CPD:C06408]
PRODUCT     hydrogenobyrinate [CPD:C06399]
REFERENCE   1  [PMID:1732194]
  AUTHORS   Thibaut D, Couder M, Famechon A, Debussche L, Cameron B, Crouzet J,
            Blanche F.
  TITLE     The final step in the biosynthesis of hydrogenobyrinic acid is
            catalyzed by the cobH gene product with precorrin-8x as the
            substrate.
  JOURNAL   J. Bacteriol. 174 (1992) 1043-9.
  ORGANISM  Pseudomonas denitrificans
REFERENCE   2  [PMID:8501034]
  AUTHORS   Roth JR, Lawrence JG, Rubenfield M, Kieffer-Higgins S, Church GM.
  TITLE     Characterization of the cobalamin (vitamin B12) biosynthetic genes
            of Salmonella typhimurium.
  JOURNAL   J. Bacteriol. 175 (1993) 3303-16.
  ORGANISM  Salmonella typhimurium
REFERENCE   3  [PMID:1451790]
  AUTHORS   Roessner CA, Warren MJ, Santander PJ, Atshaves BP, Ozaki S,
            Stolowich NJ, Iida K, Scott AI.
  TITLE     Expression of 9 Salmonella typhimurium enzymes for cobinamide
            synthesis. Identification of the 11-methyl and 20-methyl
            transferases of corrin biosynthesis.
  JOURNAL   FEBS. Lett. 301 (1992) 73-8.
  ORGANISM  Salmonella typhimurium
REFERENCE   4  [PMID:2211521]
  AUTHORS   Crouzet J, Cameron B, Cauchois L, Rigault S, Rouyez MC, Blanche F,
            Thibaut D, Debussche L.
  TITLE     Genetic and sequence analysis of an 8.7-kilobase Pseudomonas
            denitrificans fragment carrying eight genes involved in
            transformation of precorrin-2 to cobyrinic acid.
  JOURNAL   J. Bacteriol. 172 (1990) 5980-90.
  ORGANISM  Pseudomonas denitrificans
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K06042  precorrin-8X methylmutase
GENES       ECI: UTI89_C3737(yhdM)
            STY: STY2238(cbiC)
            STT: t0841(cbiC)
            SPT: SPA0838(cbiC)
            SEC: SC2041(cbiC)
            STM: STM2033(cbiC)
            YEN: YE2723(cbiC)
            PLU: plu2997(cbiC)
            PAE: PA2905(cobH)
            PAU: PA14_26500(cobH)
            PPU: PP_4828(cobH)
            PPF: Pput_4706
            PST: PSPTO_4876(cobH)
            PSB: Psyr_4416
            PSP: PSPPH_4459(cobH)
            PFL: PFL_0658
            PFO: Pfl_0605
            PEN: PSEEN4870(cobH)
            PMY: Pmen_4572
            MCA: MCA2298(cobH)
            MMW: Mmwyl1_3376
            CVI: CV_1567(cbiC)
            RSO: RS03744(RSp0623)
            BMA: BMA1162(cobH)
            BMV: BMASAVP1_A1603(cobH)
            BML: BMA10299_A0265(cobH)
            BMN: BMA10247_0895(cobH)
            BXE: Bxe_B1244
            BVI: Bcep1808_1609
            BUR: Bcep18194_A4823
            BCN: Bcen_1193
            BCH: Bcen2424_1673
            BAM: Bamb_1573
            BPS: BPSL1760(cobH)
            BPM: BURPS1710b_2112(cobH)
            BPL: BURPS1106A_1966(cobH)
            BPD: BURPS668_1949(cobH)
            BTE: BTH_I2399
            POL: Bpro_2777
            MPT: Mpe_B0440(cobH) Mpe_B0475(cobH)
            AZO: azo3531(cbiC)
            DAR: Daro_1691
            GSU: GSU2999(cobH)
            GME: Gmet_0477
            PCA: Pcar_0480
            PPD: Ppro_1269 Ppro_1298
            DVU: DVU3087(cobH)
            DDE: Dde_0342
            DPS: DP0219(cobH)
            SFU: Sfum_2136
            MLO: mlr1379
            SME: SMc03192(cobH)
            SMD: Smed_2817
            ATU: Atu2802(cobH)
            ATC: AGR_C_5081
            RET: RHE_PE00454(cobH)
            RLE: pRL110630(cobH)
            BME: BMEI0714
            BMF: BAB1_1305
            BMS: BR1287(cobH)
            BMB: BruAb1_1288(cobH)
            BOV: BOV_1250(cobH)
            OAN: Oant_1898
            BJA: blr3265(cobH)
            BRA: BRADO4905(cobH)
            BBT: BBta_3146(cobH)
            RPA: RPA2090(cobH)
            RPB: RPB_3178
            RPC: RPC_1888
            RPD: RPD_2320
            RPE: RPE_2225
            XAU: Xaut_3284
            SIL: SPO2865(cobH)
            SIT: TM1040_2212
            RSP: RSP_6217(cobH)
            RSH: Rsph17029_1469
            RSQ: Rsph17025_1519
            JAN: Jann_2929
            RDE: RD1_3825(cobH)
            PDE: Pden_2534
            NAR: Saro_0340
            GBE: GbCGDNIH1_0660
            RRU: Rru_A2991
            MAG: amb0295
            MGM: Mmc1_3134
            GKA: GK1802
            LMO: lmo1193
            LMF: LMOf2365_1202(cobH)
            LIN: lin1156
            LWE: lwe1150(cbiC)
            SSA: SSA_0465 SSA_0466
            CAC: CAC1376(cbiC)
            CPE: CPE1227(cbiC)
            CPF: CPF_1435(cobH)
            CPR: CPR_1241(cobH)
            CTC: CTC00732
            CNO: NT01CX_0582(cobH)
            CDF: CD3430(cbiC)
            CBO: CBO0925(cbiC)
            CBA: CLB_0966(cobH)
            CBH: CLC_0980(cobH)
            CBF: CLI_1014(cobH)
            CKL: CKL_0723(cbiC)
            CHY: CHY_0767(cobH)
            DSY: DSY4063(cobH)
            MTA: Moth_1097
            MTU: Rv2065(cobH)
            MTC: MT2125(cobH)
            MBO: Mb2091(cobH)
            MBB: BCG_2084(cobH)
            MPA: MAP1811(cobH)
            MAV: MAV_2431
            MSM: MSMEG_3872
            MVA: Mvan_3430
            MGI: Mflv_3105
            MMC: Mmcs_2488
            MKM: Mkms_2533
            MJL: Mjls_2525
            CDI: DIP1232(cobH)
            NFA: nfa31510(cobH)
            RHA: RHA1_ro00173
            SCO: SCO3282(SCE39.32)
            SMA: SAV6406(cobH)
            PAC: PPA0429
            NCA: Noca_2893
            TFU: Tfu_0317
            FRA: Francci3_1520
            FAL: FRAAL2332(cobH) FRAAL3733
            SEN: SACE_5952(cobH)
            RXY: Rxyl_0645
            FNU: FN0970
            TDE: TDE2555(cobH)
            LIL: LB161(cbiC)
            LIC: LIC20131(cobH)
            LBJ: LBJ_4181(cobH)
            LBL: LBL_4196(cobH)
            SYN: sll0794(coaR) sll0916(cbiC) slr1467
            SYW: SYNW0074(cobH)
            SYC: syc2242_c
            SYF: Synpcc7942_1852
            SYD: Syncc9605_0073
            SYE: Syncc9902_0073
            SYG: sync_0078(cobH)
            SYR: SynRCC307_0077(cobH)
            SYX: SynWH7803_0083(cobH)
            CYA: CYA_0461(cobH-1) CYA_1574(cobH-2)
            CYB: CYB_0225(cobH-1) CYB_0379(cobH-2)
            TEL: tll0173(cobH) tlr1064
            GVI: gll0384(cobH)
            ANA: all0456 all2544 alr3162
            AVA: Ava_0476 Ava_2866 Ava_3862
            PMA: Pro1806(cobH)
            PMM: PMM1646(cobH)
            PMT: PMT0075(cobH)
            PMN: PMN2A_1244(cobH)
            PMI: PMT9312_1738
            PMB: A9601_18551(cobH)
            PMC: P9515_18361(cobH)
            PMF: P9303_00841(cobH)
            PMG: P9301_18361(cobH)
            PME: NATL1_21141(cobH)
            TER: Tery_1670 Tery_3745
            BFR: BF2518
            BFS: BF2547(cobJ)
            PGI: PG0213
            CTE: CT0387(cbiCH)
            DGE: Dgeo_2360
            TTH: TT_P0009
            TTJ: TTHB052
            MJA: MJ0930(cbiC)
            MMP: MMP0330(cbiC)
            MAC: MA4258(cbiC)
            MBA: Mbar_A0630
            MMA: MM_0994
            MBU: Mbur_2355
            MTH: MTH227
            MST: Msp_1179(cbiC)
            MSI: Msm_1234
            MKA: MK1196(cobH)
            AFU: AF0724(cbiH)
            HAL: VNG1567G(cbiC)
            HMA: rrnAC3020(cbiC)
            HWA: HQ2297A(cbiC)
            NPH: NP1090A(cbiC)
            TAC: Ta0654
            TVO: TVN0922
            PTO: PTO0040 PTO0111
            SSO: SSO2308(cbiC)
            STO: ST1824
            SAI: Saci_0399
            PAI: PAE0343
STRUCTURES  PDB: 1F2V  1I1H  1OU0  1V9C  2AFR  2AFV  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.1.2
            ExPASy - ENZYME nomenclature database: 5.4.1.2
            ExplorEnz - The Enzyme Database: 5.4.1.2
            ERGO genome analysis and discovery system: 5.4.1.2
            BRENDA, the Enzyme Database: 5.4.1.2
///
ENTRY       EC 5.4.2.1                  Enzyme
NAME        phosphoglycerate mutase;
            phosphoglycerate phosphomutase;
            phosphoglyceromutase;
            glycerate phosphomutase (diphosphoglycerate cofactor);
            monophosphoglycerate mutase;
            monophosphoglyceromutase;
            diphosphoglycomutase;
            diphosphoglycerate mutase;
            bisphosphoglyceromutase;
            GriP mutase;
            MPGM;
            PGA mutase;
            PGAM-i;
            PGAM;
            PGAM-d;
            PGM
CLASS       Isomerases;
            Intramolecular transferases;
            Phosphotransferases (phosphomutases)
SYSNAME     D-phosphoglycerate 2,3-phosphomutase
REACTION    2-phospho-D-glycerate = 3-phospho-D-glycerate [RN:R01518]
ALL_REAC    R01518;
            (other) R01662
SUBSTRATE   2-phospho-D-glycerate [CPD:C00631]
PRODUCT     3-phospho-D-glycerate [CPD:C00197]
COMMENT     The enzymes from mammals and from yeast are phosphorylated by
            (2R)-2,3-bis-phosphoglycerate, which is also an intermediate (see
            intro.html">introduction to section EC 5.4.2). With the rabbit
            muscle enzyme, dissociation of bisphosphate from the enzyme is much
            slower than the overall isomerization. These enzymes also catalyse,
            slowly, the reactions of EC 5.4.2.4 bisphosphoglycerate mutase; they
            were formerly listed as EC 2.7.5.3. Enzymes from wheat, rice,
            insects and some fungi, however, have maximum activity in the
            absence of 2,3-bisphosphoglycerate, and were formerly listed under
            the present number as phosphoglycerate phosphomutase.
REFERENCE   1
  AUTHORS   Grisolia, S.
  TITLE     Phosphoglyceric acid mutase.
  JOURNAL   Methods Enzymol. 5 (1962) 236-242.
  ORGANISM  Saccharomyces cerevisiae [GN:sce], rabbit
REFERENCE   2
  AUTHORS   Ray, W.J., Jr. and Peck, E.J., Jr.
  TITLE     Phosphomutases.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p.
            407-477.
REFERENCE   3  [PMID:6255773]
  AUTHORS   Rose ZB.
  TITLE     The enzymology of 2,3-bisphosphoglycerate.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 51 (1980) 211-53.
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
ORTHOLOGY   KO: K01834  phosphoglycerate mutase
GENES       HSA: 441531(PGAM4) 5223(PGAM1) 5224(PGAM2) 669(BPGM)
            PTR: 463746(BPGM) 494122(PGAM4)
            MMU: 12183(Bpgm) 18648(Pgam1) 56012(Pgam2)
            RNO: 24642(Pgam1) 24959(Pgam2)
            CFA: 475495(PGAM2) 477786(PGAM1) 482704(BPGM)
            BTA: 404148(PGAM1)
            GGA: 418172(RCJMB04_32o10) 428969(RCJMB04_5g20)
            XLA: 379778(pgam2) 432058(MGC81450) 444102(MGC80400)
                 446644(MGC82549) 447767(MGC84250)
            XTR: 448157(pgam1)
            DRE: 393999(pgam2) 408255(pgam1l)
            SPU: 591606(LOC591606)
            DME: Dmel_CG1721(Pglym78) Dmel_CG17645
            CEL: F57B10.3
            ATH: AT1G09780 AT3G50520
            OSA: 4327493 4330747 4332728 4339133 4349723
            CME: CMK188C
            SCE: YDL021W(GPM2) YKL152C(GPM1)
            AGO: AGOS_ACR056W AGOS_AER228C
            PIC: PICST_34127(GPM1.3) PICST_48292(GPM1.2) PICST_70394(GPM1.1)
                 PICST_89865(GPM2)
            CGR: CAGL0E06358g CAGL0K01705g CAGL0L03311g CAGL0L11088g
            SPO: SPAC1687.21 SPAC26F1.06(gpm1)
            ANI: AN3059.2 AN8720.2
            AFM: AFUA_3G09290 AFUA_6G02600 AFUA_6G08500
            AOR: AO090005001300 AO090011000152 AO090120000145
            CNE: CNK00280
            UMA: UM05339.1
            ECU: ECU10_1060
            DDI: DDB_0231354(gpmA)
            PFA: PF11_0208 PFD0660w
            CPV: cgd7_4270
            CHO: Chro.70471
            TAN: TA10465
            TPV: TP04_0690
            TET: TTHERM_00185740 TTHERM_00384710 TTHERM_00571980
                 TTHERM_00641240
            TBR: Tb10.6k15.2620 Tb927.5.3580
            TCR: 506247.330 507811.44 511649.150
            LMA: LmjF08.0060 LmjF36.6650
            EHI: 146.t00012 351.t00001 60.t00033
            ECO: b0755(gpmA) b3612(yibO) b4395(ytjC)
            ECJ: JW0738(gpmA) JW3587(gpmI) JW4358(ytjC)
            ECE: Z0925(gpmA) Z5039(yibO) Z5997(gpmB)
            ECS: ECs0783 ECs4490 ECs5353
            ECC: c0831(gpmA) c4438(yibO) c5482(gpmB)
            ECI: UTI89_C0752(gpmA) UTI89_C4157(yibO) UTI89_C5168(gpmB)
            ECP: ECP_0766 ECP_3713 ECP_4781
            ECV: APECO1_1333(gpmA) APECO1_1984(gpmB) APECO1_2843(yibO)
            ECW: EcE24377A_0782(gpmA) EcE24377A_4116(gpmI)
            ECX: EcHS_A0809(gpmA) EcHS_A3824(gpmI)
            STY: STY0804(gpmA) STY4091 STY4932(gpmB)
            STT: t2115(gpmA) t3815 t4624(gpmB)
            SPT: SPA1980(gpmA) SPA3556(pmgI) SPA4395(gpmB)
            SEC: SC0770(gpmA) SC3627(pmgI) SC4430(gpmB)
            STM: STM0772(gpmA) STM3704(pmgI) STM4585(gpmB)
            YPE: YPO0064 YPO0455(gpmB) YPO1133(gpmA)
            YPK: y0077 y3048(gpmA) y3724(gpmB)
            YPM: YP_0064(gpmI) YP_1025(gpmA) YP_3728(gpmB)
            YPA: YPA_1041 YPA_3478 YPA_4046
            YPN: YPN_0326 YPN_2867 YPN_3786
            YPP: YPDSF_3841
            YPS: YPTB0060 YPTB0598(gpmB) YPTB1166(gpmA)
            YPI: YpsIP31758_0075(gpmI) YpsIP31758_2861(gpmA)
            SFL: SF0549(gpmA) SF3651(gpmI) SF4427(gpmB)
            SFX: S0557(gpmA) S4117(yibO) S4698(gpmB)
            SFV: SFV_0585(gpmA) SFV_3917(yibO) SFV_4429(gpmB)
            SSN: SSON_0707(gpmA) SSON_3793(yibO) SSON_4545(gpmB)
            SBO: SBO_0610(gpmA) SBO_3618(yibO) SBO_4458(gpmB)
            SDY: SDY_0702(gpmA) SDY_4045(yibO) SDY_4656(gpmB)
            ECA: ECA1382(gpmA) ECA3897(gpmB)
            PLU: plu0559(gpmB) plu1471(gpmA)
            BUC: BU304(gpmA)
            BAS: BUsg294(gpmA)
            BAB: bbp283(gpmA)
            BCC: BCc_186(gpmA)
            WBR: WGLp218(gpmA)
            SGL: SG0894
            ENT: Ent638_0123
            SPE: Spro_1288 Spro_4819
            BFL: Bfl342(gpmA)
            BPN: BPEN_352(gpmA)
            HIN: HI0757(gpmA)
            HIT: NTHI0916(gpmA)
            HDU: HD1659(gpmA)
            HSO: HS_1445(gpmA) HS_1664(gpm)
            PMU: PM0634(gpmB) PM1506(gpmA)
            MSU: MS1172(gpmB) MS2321(gpmA)
            APL: APL_0230(gpmB) APL_0832(gpmA)
            ASU: Asuc_0572
            XFA: XF1886 XF1893
            XFT: PD0898(gpmA) PD0905(gpmA)
            XCC: XCC0948(pgmA) XCC2712(gpm)
            XCB: XC_1404 XC_3287
            XCV: XCV1057 XCV3029(gpmA)
            XAC: XAC1028(pgmA) XAC2874(gpm)
            XOO: XOO1460(gpm) XOO3680(pgmA)
            XOM: XOO_1362(XOO1362) XOO_3476(XOO3476)
            VCH: VC0336
            VCO: VC0395_A2738(yibO)
            VVU: VV1_1281
            VVY: VV3082
            VPA: VP2829
            VFI: VF0202
            PPR: PBPRA0224(yibO)
            PAE: PA5131(pgm)
            PAU: PA14_67770(pgm)
            PAP: PSPA7_5865(gpmI)
            PPU: PP_5056(pgm)
            PPF: Pput_4929
            PST: PSPTO_5327(gpmA)
            PSB: Psyr_4885
            PSP: PSPPH_4916(gpmI)
            PFL: PFL_0371(gpmA)
            PFO: Pfl_0333
            PEN: PSEEN0380(gpmA) PSEEN4638
            PMY: Pmen_4246
            PAR: Psyc_0701(pgm)
            PCR: Pcryo_0673 Pcryo_1028
            PRW: PsycPRwf_1431
            ACI: ACIAD0256(gpmI)
            SON: SO_0049(gpmA)
            SDN: Sden_3698
            SFR: Sfri_4021
            SAZ: Sama_0060
            SBL: Sbal_4332
            SBM: Shew185_0043
            SLO: Shew_3806
            SPC: Sputcn32_0040
            SSE: Ssed_4470
            SPL: Spea_4217
            SHE: Shewmr4_0045
            SHM: Shewmr7_0043
            SHN: Shewana3_0051 Shewana3_4088
            SHW: Sputw3181_4038
            ILO: IL0233
            CPS: CPS_1144 CPS_4391(gpmA)
            PHA: PSHAa0366(gpmM)
            PAT: Patl_1132 Patl_2593 Patl_3611
            SDE: Sde_0494 Sde_0632 Sde_2062
            PIN: Ping_3211
            MAQ: Maqu_3166
            CBU: CBU_1536(yibO)
            CBD: COXBU7E912_0451(gpmI)
            LPN: lpg0501(pgm)
            LPF: lpl0539(gpmI)
            LPP: lpp0563(gpmI)
            MCA: MCA0753(gpmA)
            FTU: FTT1329(gpmI)
            FTF: FTF1329(gpmI)
            FTW: FTW_1495(gpmI)
            FTL: FTL_1490
            FTH: FTH_1444(gpmI)
            FTA: FTA_1575(gpmI)
            FTN: FTN_0648(gpmI)
            TCX: Tcr_1956
            NOC: Noc_0031 Noc_1395 Noc_1928
            AEH: Mlg_1323
            HHA: Hhal_1264
            HCH: HCH_01352(gpmI) HCH_03079(gpmB)
            CSA: Csal_0046 Csal_3230
            ABO: ABO_0877(gpmA) ABO_0956 ABO_1769(gpm) ABO_2403(gpmA)
            MMW: Mmwyl1_0723
            AHA: AHA_0293(gpmI) AHA_2360
            DNO: DNO_0706
            BCI: BCI_0251(gpmA)
            RMA: Rmag_1070
            VOK: COSY_0969(gpm)
            NME: NMB1604
            NMA: NMA1801(gpm)
            NMC: NMC1524(gpm)
            NGO: NGO1258
            CVI: CV_0492(gpmA) CV_3211(gpmB) CV_3352(pgm)
            RSO: RSc0353(gpmA) RSc0499(gpmB)
            REU: Reut_A0304 Reut_A0479
            REH: H16_A0332(pgam1) H16_A0493(pgam2)
            RME: Rmet_0251 Rmet_0420
            BMA: BMA1804 BMA2350 BMA3208(gpmA)
            BMV: BMASAVP1_A0181(gpmA)
            BML: BMA10299_A1411(gpmA)
            BMN: BMA10247_2838(gpmA)
            BXE: Bxe_A0613 Bxe_A4181 Bxe_B0981 Bxe_B2602
            BVI: Bcep1808_2957
            BUR: Bcep18194_A3771 Bcep18194_A6186
            BCN: Bcen_0202 Bcen_2243
            BCH: Bcen2424_0685 Bcen2424_2857 Bcen2424_5290
            BAM: Bamb_0579 Bamb_2912
            BPS: BPSL0443(gpmA) BPSL1236 BPSL2902
            BPM: BURPS1710b_0662(gpmA) BURPS1710b_1461 BURPS1710b_3410(gpmB)
            BTE: BTH_I0416 BTH_I1085 BTH_I1243
            PNU: Pnuc_1948
            BPE: BP0607(gpmA) BP1455(gpmB)
            BPA: BPP0295(gpmA) BPP2056(gpmB)
            BBR: BB0298(gpmA) BB1449(gpmB)
            RFR: Rfer_0816 Rfer_1309
            POL: Bpro_0886 Bpro_4091
            PNA: Pnap_0927
            AAV: Aave_3858
            AJS: Ajs_3505
            VEI: Veis_0036
            MPT: Mpe_A0330 Mpe_A0713 Mpe_B0562
            HAR: HEAR2975(gpmA) HEAR3261
            MMS: mma_0305(gpm1) mma_1381(gpm4) mma_3222(gpm2) mma_3476(gpm3)
            NEU: NE0178(gpmA) NE1780
            NET: Neut_0265 Neut_0919
            NMU: Nmul_A0422 Nmul_A1121
            EBA: ebA1038(gpmB) ebA1052(gpmA) ebA4004(gpmA)
            AZO: azo2798(gpmB) azo2808(gpmA)
            DAR: Daro_0151 Daro_0233 Daro_0602
            TBD: Tbd_2394
            MFA: Mfla_2188
            HPY: HP0974(pgm)
            HPJ: jhp0908(pgm)
            HPA: HPAG1_0955
            HHE: HH1169(pgm)
            HAC: Hac_1059(pgm)
            WSU: WS2039(PGM)
            TDN: Tmden_1614
            CJE: Cj0434(pgm)
            CJR: CJE0484(pgm)
            CJJ: CJJ81176_0460(pgm)
            CJU: C8J_0409(pgm)
            CJD: JJD26997_1510(pgm)
            CFF: CFF8240_1360(gpmI)
            CCV: CCV52592_1044(gpmI)
            CHA: CHAB381_1593(gpmI)
            CCO: CCC13826_0563(gpmI) CCC13826_1555
            ABU: Abu_1900(pgm)
            NIS: NIS_0920(gpmA)
            SUN: SUN_1290(gpmA) SUN_2191
            GSU: GSU1612(gpm) GSU1818 GSU3207(gpmA)
            GME: Gmet_1428 Gmet_1653 Gmet_3203
            GUR: Gura_2382 Gura_4127
            PCA: Pcar_1514 Pcar_2574 Pcar_2741
            PPD: Ppro_0776 Ppro_3611
            DVU: DVU1619(gpmA) DVU2935(gpm)
            DVL: Dvul_0432 Dvul_1516 Dvul_2095
            DDE: Dde_0736 Dde_1757 Dde_2732 Dde_3004
            LIP: LI1015(gmpA)
            BBA: Bd1653 Bd2727(gpmA)
            DPS: DP1731 DP1750(gpmB) DP2472
            ADE: Adeh_0235 Adeh_2893
            AFW: Anae109_0257
            MXA: MXAN_1236(gpmI)
            SAT: SYN_00621 SYN_00891 SYN_01002
            SFU: Sfum_1217 Sfum_2410
            WOL: WD0868(pgm)
            WBM: Wbm0403
            AMA: AM802(yibO)
            APH: APH_0389(gpmI)
            ERU: Erum5150(gpmI)
            ERW: ERWE_CDS_05400(gmpI)
            ERG: ERGA_CDS_05300(gmpI)
            ECN: Ecaj_0523
            ECH: ECH_0505(gpmI)
            NSE: NSE_0891(gpmI)
            PUB: SAR11_0193(gpmA)
            MLO: mlr0406 mlr4643
            MES: Meso_3591
            PLA: Plav_1474
            SME: SMa0527 SMc02838(gpmA)
            SMD: Smed_3372
            ATU: Atu3469(pgm)
            ATC: AGR_C_1372 AGR_L_2721
            RET: RHE_CH00169(gpmA) RHE_CH00893(ypch00290) RHE_CH00937(gpmB)
                 RHE_CH02353(ypch00772) RHE_CH03439 RHE_PF00323(ypf00165)
            RLE: RL0179(gpmA) RL0954(gpmB) RL1010(gpmB) RL2665 RL2997 RL3898
            BME: BMEII0248
            BMF: BAB2_1013(gpm)
            BMS: BRA1052(gpm)
            BMB: BruAb2_0992(gpm)
            BOV: BOV_A0990(gpm)
            BJA: blr0686
            BRA: BRADO0157(gpmA) BRADO2075 BRADO2152 BRADO3042
            BBT: BBta_0198(gpmA) BBta_1586 BBta_2469 BBta_5099
            RPA: RPA0340(pgm1) RPA3286
            RPB: RPB_0436
            RPC: RPC_0336
            RPD: RPD_0384
            RPE: RPE_0342 RPE_3615 RPE_3847 RPE_4590
            NWI: Nwi_0202 Nwi_0628
            NHA: Nham_0159 Nham_0769
            BHE: BH12450(gpmA)
            BQU: BQ09820(gpmA)
            BBK: BARBAKC583_1052(gpmA)
            CCR: CC_1351 CC_2261
            SIL: SPO1970 SPO3810(gpmI)
            SIT: TM1040_0540 TM1040_0856 TM1040_2757
            RSP: RSP_0934(gpmI)
            RSH: Rsph17029_2593
            RSQ: Rsph17025_2981
            JAN: Jann_0379 Jann_2515
            RDE: RD1_0335(gpmI) RD1_0700 RD1_1092 RD1_1195 RD1_2834
            PDE: Pden_2506
            MMR: Mmar10_2498
            HNE: HNE_0031
            ZMO: ZMO1240(gpm)
            NAR: Saro_3265
            SAL: Sala_2829
            SWI: Swit_3133
            ELI: ELI_13585
            GOX: GOX0330 GOX0965
            GBE: GbCGDNIH1_1712 GbCGDNIH1_2315 GbCGDNIH1_2335
            ACR: Acry_0905
            RRU: Rru_A1234 Rru_A2210
            MAG: amb0305 amb1531
            MGM: Mmc1_0814 Mmc1_3511
            ABA: Acid345_1073
            SUS: Acid_4374
            BSU: BG10898(pgm) BG13062(yhfR)
            BHA: BH3557(pgm)
            BAN: BA1745 BA2044 BA2076 BA2488(gpm) BA3545 BA3876 BA4144 BA5203
                 BA5365(gpmA)
            BAR: GBAA1745 GBAA2044 GBAA2076 GBAA2488(gpm) GBAA3545 GBAA3876
                 GBAA4144 GBAA5203 GBAA5365(gpmA)
            BAA: BA_0076 BA_0224 BA_2257 BA_2544 BA_2572 BA_2983 BA_4037
                 BA_4350 BA_4612
            BAT: BAS1619 BAS1897 BAS1929 BAS2313 BAS3287 BAS3591 BAS3846
                 BAS4837 BAS4986
            BCE: BC1691 BC2029 BC2059 BC2435 BC3478 BC3745 BC3934 BC4971
                 BC5136
            BCA: BCE_1822 BCE_2113 BCE_2160 BCE_2520(gpm) BCE_3497
                 BCE_3765(gpmA) BCE_3778 BCE_3981 BCE_5107 BCE_5239(gpmA)
            BCZ: BCZK1571(gpm) BCZK1849(pgm) BCZK1881 BCZK2234(gpm) BCZK3203
                 BCZK3503(pgm) BCZK3694 BCZK4696(gpmA) BCZK4825(gpmI)
            BCY: Bcer98_1794 Bcer98_3679
            BTK: BT9727_1580(gpm) BT9727_1859(pgm) BT9727_1891
                 BT9727_2281(gpm) BT9727_2951 BT9727_3257 BT9727_3491(pgm)
                 BT9727_3677 BT9727_4680(gpmA) BT9727_4815(gpmI)
            BTL: BALH_1534(gpm) BALH_2422 BALH_3375(pgm) BALH_4502(gpmA)
                 BALH_4628(gpmI)
            BLI: BL01113 BL03467(pgm) BL03733
            BLD: BLi01114(yhfR) BLi01419 BLi03662(pgm)
            BCL: ABC1293 ABC1431 ABC3018(pgm)
            BAY: RBAM_031270
            BPU: BPUM_3054(gpmI)
            OIH: OB0337 OB2435(pgm)
            GKA: GK1466 GK3055
            SAU: SA0361 SA0730(pgm) SA2204
            SAV: SAV0376 SAV0775(pgm) SAV2416
            SAM: MW0351 MW0737(pgm) MW2339
            SAR: SAR0394 SAR0831(pgm) SAR2506
            SAS: SAS0353 SAS0741 SAS2307
            SAC: SACOL0447 SACOL0841(pgm) SACOL2415(gpm)
            SAB: SAB0326 SAB0731(pgm) SAB0756 SAB2296c
            SAA: SAUSA300_0375 SAUSA300_0759(gpmI) SAUSA300_2362(gpmA)
            SAO: SAOUHSC_00359 SAOUHSC_00798 SAOUHSC_02703
            SAJ: SaurJH9_0800 SaurJH9_2442
            SAH: SaurJH1_0816 SaurJH1_2490
            SEP: SE0560 SE1995 SE2364
            SER: SERP0052 SERP0445(pgm) SERP2007(gpm)
            SHA: SH0636(gpmA) SH2110(gpmI) SH2595
            SSP: SSP0483 SSP1913 SSP2337
            LMO: lmo0268 lmo0517 lmo0556 lmo0557 lmo2205 lmo2456(pgm)
            LMF: LMOf2365_0287 LMOf2365_0546 LMOf2365_0585 LMOf2365_0586
                 LMOf2365_2238(gpm) LMOf2365_2429(gpmA)
            LIN: lin0293 lin0517 lin0565 lin0566 lin2308 lin2550(pgm)
            LWE: lwe0238 lwe0473 lwe0522 lwe0523 lwe2222(gpm) lwe2404(pgm)
            LLA: L0011(pmg) L174407(yjhF) L182916(yrjI)
            LLC: LACR_0382 LACR_1022 LACR_1904
            LLM: llmg_0355(pmg) llmg_1579(gpmB) llmg_1923(gpmC)
            SPY: SPy_0598 SPy_1429(gpmA) SPy_1766
            SPZ: M5005_Spy_0497 M5005_Spy_1164(gpmA) M5005_Spy_1503
            SPM: spyM18_0665(pgmA) spyM18_1439 spyM18_1836
            SPG: SpyM3_0422 SpyM3_1090(gpmA) SpyM3_1536
            SPS: SPs0330 SPs0775 SPs1433
            SPH: MGAS10270_Spy0490 MGAS10270_Spy1235(gpmA) MGAS10270_Spy1571
            SPI: MGAS10750_Spy0516 MGAS10750_Spy1272(gpmA) MGAS10750_Spy1563
            SPJ: MGAS2096_Spy0508 MGAS2096_Spy1236(gpmA) MGAS2096_Spy1531
            SPK: MGAS9429_Spy0487 MGAS9429_Spy1212(gpmA) MGAS9429_Spy1505
            SPF: SpyM50696(gpmA)
            SPA: M6_Spy0518 M6_Spy1190 M6_Spy1497
            SPB: M28_Spy0476 M28_Spy1158(gpmA) M28_Spy1492
            SPN: SP_0240 SP_0984 SP_1655
            SPR: spr0219(gpmB) spr0887(gpmB) spr1499(gpmA)
            SPD: SPD_1468
            SAG: SAG0092 SAG0752 SAG0764
            SAN: gbs0091 gbs0773 gbs0784
            SAK: SAK_0142 SAK_0878 SAK_0889(gpmA)
            SMU: SMU.596(pmgY) SMU.700c SMU.74
            STC: str0114(gpmB) str0697(gpmC) str1204(gpmA)
            STL: stu0114 stu0697(gpmC) stu1204(gpmA)
            STE: STER_1172
            SSA: SSA_0421 SSA_0422 SSA_0491 SSA_0688(gpmA) SSA_1528(gpm)
                 SSA_2015 SSA_2016
            SSV: SSU98_1650
            SGO: SGO_0391 SGO_0392 SGO_0704(gpmA)
            LPL: lp_0205(pgm1) lp_0597(pgm2) lp_0900(pgm3) lp_0901(pgm4)
                 lp_1785(pgm5) lp_2170(pgm6) lp_2785(pgm7) lp_2868(pgm8)
                 lp_3170(pmg9)
            LJO: LJ0164 LJ0375 LJ0380 LJ0606 LJ0987
            LAC: LBA0185 LBA0339 LBA0341 LBA0823 LBA1065 LBA1678 LBA1841
            LSA: LSA0100(gpm1) LSA0131(gpm2) LSA0206(gpm3) LSA0803(gpm4)
                 LSA1855(gpm5)
            LSL: LSL_0125(gpmB) LSL_0726(gpmB) LSL_1255(gpmA) LSL_1498(gpmA)
                 LSL_1511(gpmB) LSL_1703(gpmB)
            LDB: Ldb0230(gpmA1) Ldb0756 Ldb1734(gpmA2)
            LBU: LBUL_0203 LBUL_0689 LBUL_1608
            LBR: LVIS_0570 LVIS_1365 LVIS_1433 LVIS_1811 LVIS_2042 LVIS_2169
            LCA: LSEI_1146 LSEI_1201 LSEI_1293 LSEI_1702 LSEI_1992 LSEI_2060
                 LSEI_2134 LSEI_2336 LSEI_2644
            LGA: LGAS_0167 LGAS_0327 LGAS_0332
            LRE: Lreu_0146 Lreu_0291
            PPE: PEPE_1510 PEPE_1710
            EFA: EF0195(gpm) EF0273 EF2433 EF2664
            OOE: OEOE_0122 OEOE_0310
            LME: LEUM_1877
            STH: STH1924 STH248
            CAC: CAC0167 CAC0712(pgm) CAC2741(gpmA) CAC3021
            CPE: CPE0083(gpmA) CPE1301(pgm)
            CPF: CPF_0078 CPF_1508(gpmI)
            CPR: CPR_0100 CPR_1298(gpmI)
            CTC: CTC00381 CTC02637
            CNO: NT01CX_1413(gpmI) NT01CX_2076 NT01CX_2398(apgM)
            CTH: Cthe_0140 Cthe_1292
            CDF: CD3171(gpmI)
            CBO: CBO0229(gpmI)
            CBA: CLB_0270(gpmI)
            CBH: CLC_0285(gpmI)
            CBF: CLI_0294(gpmI)
            CBE: Cbei_0600 Cbei_1759
            AMT: Amet_3577
            CHY: CHY_0283(gpmI)
            DSY: DSY1834 DSY4839
            DRM: Dred_0135 Dred_2988
            SWO: Swol_0275 Swol_1301
            CSC: Csac_1951
            TTE: TTE1346(gpmB) TTE2487(gpmA)
            MTA: Moth_0265
            MGE: MG_430(pgm)
            MPN: MPN628(pgm)
            MPU: MYPU_4590(pgm)
            MPE: MYPE3740(pgm)
            MGA: MGA_0356(gpmI)
            MMY: MSC_0825(gpm)
            MMO: MMOB3310(pgm)
            MHY: mhp615(pgm)
            MHJ: MHJ_0595(pgm)
            MHP: MHP7448_0595(pgm)
            MSY: MS53_0656(pgm)
            MCP: MCAP_0752(gpmI)
            UUR: UU182(pgm)
            POY: PAM285(gpmI)
            AYW: AYWB_436(gpmI)
            MFL: Mfl502
            MTU: Rv0489(gpm1) Rv2419c Rv3214(gpm2)
            MTC: MT0508(gpm) MT2492 MT3310
            MBO: Mb0499(gpm1) Mb2442c Mb3240(gpm2)
            MBB: BCG_0530(gpm1) BCG_2435c BCG_3241(gpm2_1) BCG_3334(gpm2_2)
            MLE: ML1452 ML2441(gpm)
            MPA: MAP2242c MAP3315(entD) MAP3981(gpm)
            MAV: MAV_4662
            MSM: MSMEG_0935 MSMEG_1926 MSMEG_4579 MSMEG_6088 MSMEG_6338
            MVA: Mvan_0829
            MGI: Mflv_0084
            MMC: Mmcs_0659 Mmcs_1388 Mmcs_3528 Mmcs_4753
            MKM: Mkms_0672
            MJL: Mjls_0652
            CGL: NCgl0390(cgl0402) NCgl0423(cgl0438) NCgl1013(cgl1058)
                 NCgl2268(cgl2350)
            CGB: cg0482(gpmA) cg2581
            CEF: CE0423 CE2254
            CDI: DIP0389(gpmA) DIP1773
            CJK: jk0569(gpmB) jk1912(gpmA)
            NFA: nfa13780 nfa51890
            RHA: RHA1_ro01295 RHA1_ro02070(gpmA) RHA1_ro03730 RHA1_ro06349
            SCO: SCO2576(pgm2) SCO4209(2SCD46.23) SCO6818(SC1A2.27c)
            SMA: SAV3979(gpm1) SAV5481(gpm2)
            TWH: TWT655(gpm)
            TWS: TW678(pgm)
            LXX: Lxx11870(gpm) Lxx18320(gpm)
            CMI: CMM_2495(gpmA)
            ART: Arth_0721
            AAU: AAur_0892(gpm)
            PAC: PPA0364 PPA0809 PPA0838
            NCA: Noca_4043
            TFU: Tfu_2169 Tfu_2911
            FRA: Francci3_0468 Francci3_1234
            FAL: FRAAL0174 FRAAL0964(gpmA) FRAAL0998 FRAAL1530 FRAAL1939(gpm)
                 FRAAL5405(pgmB)
            ACE: Acel_0075 Acel_0250
            KRA: Krad_0891
            SEN: SACE_0153(pgmB) SACE_1433 SACE_3448 SACE_6422(entD)
                 SACE_6967(gpmA)
            STP: Strop_0335
            BLO: BL0884 BL0966 BL1447 BL1656(gpm)
            BAD: BAD_0378(gpm) BAD_0698 BAD_0869
            RXY: Rxyl_0651 Rxyl_1248 Rxyl_2948
            FNU: FN0729 FN0730 FN0808
            RBA: RB1559(pgaM) RB4904 RB6467 RB8562(pgm)
            CTR: CT722(pgm)
            CTA: CTA_0784(pgmA)
            CMU: TC0095
            CPN: CPn0863(pgmA)
            CPA: CP1006
            CPJ: CPj0863(pgmA)
            CPT: CpB0892
            CCA: CCA00904(gpmA)
            CAB: CAB872
            CFE: CF0110(pgmA)
            PCU: pc0161(pgmA) pc1869
            BBU: BB0658(gpmA)
            BGA: BG0681(gpmA)
            BAF: BAPKO_0702(gpmA)
            TPA: TP0168
            TDE: TDE1697(gpm)
            LIL: LA0439(pmgI) LA4206(gpmA) LB149(pmgA)
            LIC: LIC10383(yibO) LIC20119(pgmA)
            LBJ: LBJ_2872(gpmI)
            LBL: LBL_0199(gpmI)
            SYN: sll0395 slr1124(gpmB) slr1945(yibO)
            SYW: SYNW0519(pgmI) SYNW1763(cobC)
            SYC: syc1034_c(gpm) syc1049_d(yibO) syc2015_d
            SYF: Synpcc7942_0469 Synpcc7942_0485 Synpcc7942_2078
            SYD: Syncc9605_0701 Syncc9605_2164
            SYE: Syncc9902_0513 Syncc9902_1657
            SYG: sync_2012(cobC) sync_2276(gpmI)
            SYR: SynRCC307_0867(gmpB) SynRCC307_1857(gpmI)
            SYX: SynWH7803_0630(gmpB) SynWH7803_1995(gpmI)
            CYA: CYA_1663 CYA_2123(gpmI)
            CYB: CYB_0464 CYB_1020 CYB_2684(gpmI)
            TEL: tlr0151 tlr1532
            GVI: gll0756 gll0771 gll1596 gll1875 glr0999
            ANA: all4182 all4906 alr1107 alr3338
            AVA: Ava_0723 Ava_2177 Ava_3651
            PMA: Pro0515(gpmB) Pro1587(gpmI)
            PMM: PMM0515(cobC) PMM1434(pgmI)
            PMT: PMT1252(cobC) PMT1446(pgmI)
            PMN: PMN2A_0966 PMN2A_1847
            PMI: PMT9312_0515 PMT9312_1527
            PMB: A9601_05711(gpmB) A9601_16361(gpmI)
            PMC: P9515_05791(gpmB) P9515_16131(gpmI)
            PMF: P9303_05081(gpmI) P9303_07531(gpmB) P9303_09371
            PMG: P9301_05411(gpmB) P9301_16241(gpmI)
            PMH: P9215_17011(gpmI)
            PME: NATL1_05721(gpmB) NATL1_18341(gpmI)
            TER: Tery_1011 Tery_2181
            BTH: BT_1105 BT_1660 BT_2402 BT_3419
            BFR: BF0292 BF0609 BF3252
            BFS: BF0241(gpmI) BF0559 BF3091(gpmA)
            PGI: PG0130(gpm)
            SRU: SRU_2355(gpmI)
            CHU: CHU_2250(gpmA) CHU_3731(apgM)
            GFO: GFO_0414(gpmI)
            FJO: Fjoh_1764
            FPS: FP1458(gpmA) FP2135(gpmI)
            CTE: CT0399(gpm)
            CCH: Cag_0187
            CPH: Cpha266_0627
            PVI: Cvib_0557
            PLT: Plut_0501
            DET: DET0743 DET1635
            DEH: cbdb_A1386 cbdb_A1734 cbdb_A718
            DEB: DehaBAV1_0673 DehaBAV1_1380
            RRS: RoseRS_0822
            RCA: Rcas_0656
            DRA: DR_0278 DR_1097 DR_1393 DR_2227
            DGE: Dgeo_1615 Dgeo_2228 Dgeo_2232
            TTH: TTC1618 TTC1888 TT_P0006
            TTJ: TTHA0116 TTHA0368 TTHB049
            AAE: aq_1744(gpmA) aq_1990(pgmA) aq_542(bcpC)
            TMA: TM1374 TM1774
            TPT: Tpet_1062
            TME: Tmel_1409
            FNO: Fnod_0732
            MJA: MJ0010 MJ1612
            MMP: MMP0112 MMP0598 MMP1439
            MMQ: MmarC5_0139 MmarC5_1008 MmarC5_1566
            MMZ: MmarC7_0684 MmarC7_1111 MmarC7_1620
            MAE: Maeo_0182 Maeo_0339
            MVN: Mevan_0750 Mevan_1117 Mevan_1390 Mevan_1470
            MAC: MA0132 MA2400(gpmA) MA2671(yibO) MA4007(yibO)
            MBA: Mbar_A0860 Mbar_A1223 Mbar_A2222 Mbar_A2961
            MMA: MM_0904 MM_1418 MM_2779 MM_2993
            MBU: Mbur_1914 Mbur_1982
            MTP: Mthe_0167 Mthe_0545 Mthe_0757
            MHU: Mhun_0447 Mhun_2324
            MLA: Mlab_1701
            MEM: Memar_0425 Memar_0702
            MBN: Mboo_0678 Mboo_1450
            MTH: MTH1591 MTH418
            MST: Msp_0485(apgM1) Msp_1299(apgM2)
            MSI: Msm_0153 Msm_0657
            MKA: MK1193
            AFU: AF1425(bcpC-1) AF1751(bcpC-2)
            HAL: VNG1887G(gpm)
            HMA: rrnAC2859(gpmB) rrnAC3403(pgm)
            HWA: HQ2781A(gpmA) HQ3517A(gpmB)
            NPH: NP1332A(gpmB) NP1964A(gpmA)
            TAC: Ta0413
            TVO: TVN1158
            PTO: PTO1271
            PHO: PH0037
            PAB: PAB2318
            PFU: PF1959(bcpC)
            TKO: TK0866
            RCI: RCIX2144(gpmA-2) RCIX838(gpmA-1)
            APE: APE_1616.1
            SMR: Smar_0332
            IHO: Igni_1374
            HBU: Hbut_1197
            SSO: SSO0417
            STO: ST0377
            SAI: Saci_0837
            MSE: Msed_2238
            PAI: PAE2326
            PIS: Pisl_1043
            PCL: Pcal_1668
            PAS: Pars_1540
            TPE: Tpen_1046 Tpen_1567
STRUCTURES  PDB: 1BQ3  1BQ4  1E58  1E59  1EJJ  1EQJ  1FZT  1O98  1O99  1QHF  
                 1RII  1V37  1V7Q  1YFK  1YJX  2A6P  2F90  2H4X  2H4Z  2H52  
                 2HHJ  2IFY  2P9F  4PGM  5PGM  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.2.1
            ExPASy - ENZYME nomenclature database: 5.4.2.1
            ExplorEnz - The Enzyme Database: 5.4.2.1
            ERGO genome analysis and discovery system: 5.4.2.1
            BRENDA, the Enzyme Database: 5.4.2.1
            CAS: 9023-91-0
///
ENTRY       EC 5.4.2.2                  Enzyme
NAME        phosphoglucomutase;
            glucose phosphomutase;
            phosphoglucose mutase
CLASS       Isomerases;
            Intramolecular transferases;
            Phosphotransferases (phosphomutases)
SYSNAME     alpha-D-glucose 1,6-phosphomutase
REACTION    alpha-D-glucose 1-phosphate = D-glucose 6-phosphate [RN:R00959]
ALL_REAC    R00959;
            (other) R01057 R02299 R03319
SUBSTRATE   alpha-D-glucose 1-phosphate [CPD:C00103]
PRODUCT     D-glucose 6-phosphate [CPD:C00092]
COFACTOR    alpha-D-Glucose 1,6-bisphosphate [CPD:C01231]
COMMENT     Maximum activity is only obtained in the presence of alpha-D-glucose
            1,6-bisphosphate. This bisphosphate is an intermediate in the
            reaction, being formed by transfer of a phosphate residue from the
            enzyme to the substrate, but the dissociation of bisphosphate from
            the enzyme complex is much slower than the overall isomerization.
            The enzyme also catalyses (more slowly) the interconversion of
            1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses,
            and the interconversion of alpha-D-ribose 1-phosphate and
            5-phosphate.
REFERENCE   1  [PMID:14216423]
  AUTHORS   JOSHI JG, HANDLER P.
  TITLE     PHOSPHOGLUCOMUTASE. I. PURIFICATION AND PROPERTIES OF
            PHOSPHOGLUCOMUTASE FROM ESCHERICHIA COLI.
  JOURNAL   J. Biol. Chem. 239 (1964) 2741-51.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Najjar, V.A.
  TITLE     Phosphoglucomutase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 6, Academic Press, New York, 1962, p. 161-178.
REFERENCE   3
  AUTHORS   Ray, W.J. and Roscelli, G.A.
  TITLE     A kinetic study of the phosphoglucomutase pathway.
  JOURNAL   J. Biol. Chem. 239 (1964) 1228-1236.
REFERENCE   4
  AUTHORS   Ray, W.J., Jr. and Peck, E.J., Jr.
  TITLE     Phosphomutases.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p.
            407-477.
REFERENCE   5
  AUTHORS   Sutherland, E.W., Cohn, M., Posternak, T. and Cori, C.F.
  TITLE     The mechanism of the phosphoglucomutase reaction.
  JOURNAL   J. Biol. Chem. 180 (1949) 1285-1295.
  ORGANISM  rabbit
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00030  Pentose phosphate pathway
            PATH: map00052  Galactose metabolism
            PATH: map00500  Starch and sucrose metabolism
            PATH: map00521  Streptomycin biosynthesis
ORTHOLOGY   KO: K01835  phosphoglucomutase
GENES       HSA: 5236(PGM1) 5238(PGM3)
            MMU: 72157(Pgm2)
            RNO: 24645(Pgm1)
            CFA: 476332(PGM5)
            GGA: 424691(PGM1)
            XLA: 379864(pgm2) 380578(pgm3)
            XTR: 407960(pgm1)
            DRE: 394000(pgm1)
            SPU: 575075(LOC575075)
            DME: Dmel_CG5165(Pgm)
            CEL: R05F9.6(phosphoglucomutase)
            ATH: AT5G51820(PGM)
            OSA: 4333895 4348230
            CME: CMJ272C CMT285C
            SCE: YKL127W(PGM1) YMR105C(PGM2)
            AGO: AGOS_ABL029W
            PIC: PICST_77218(PGM2)
            CGR: CAGL0K03421g CAGL0K07480g
            SPO: SPBC32F12.10
            ANI: AN2867.2
            AFM: AFUA_3G11830
            AOR: AO090003000746
            CNE: CNN00430
            UMA: UM00486.1
            DDI: DDB_0191348(pgmA)
            PFA: PF10_0122
            CPV: cgd2_3260 cgd2_3270
            CHO: Chro.20343
            TET: TTHERM_00577080
            TCR: 508637.90 511911.130
            LMA: LmjF21.0640
            EHI: 5.t00030
            ECO: b0688(pgm)
            ECJ: JW0675(pgm)
            ECE: Z0837(pgm)
            ECS: ECs0719
            ECC: c0775(pgm)
            ECI: UTI89_C0693(pgm)
            ECP: ECP_0709
            ECV: APECO1_1376(pgm)
            ECW: EcE24377A_0716(pgm)
            ECX: EcHS_A0735
            STY: STY0736(pgm)
            STT: t2177(pgm)
            SPT: SPA2043(pgm)
            SEC: SC0718(pgm)
            STM: STM0698(pgm)
            YPE: YPO2686(pgm)
            YPK: y1258(pgm)
            YPM: YP_2488(pgm)
            YPA: YPA_2414
            YPN: YPN_1171
            YPS: YPTB2923(pgm)
            YPI: YpsIP31758_1099(pgm)
            SFL: SF0605(pgm)
            SFX: S0616(pgm)
            SFV: SFV_0643(pgm)
            SSN: SSON_0642(pgm)
            SBO: SBO_0550(pgm)
            SDY: SDY_0628(pgm)
            ECA: ECA1336(pgm)
            PLU: plu1407(pgm)
            WBR: WGLp425(pgm)
            SGL: SG0866
            BFL: Bfl326(pgm)
            BPN: BPEN_335(pgm)
            HSO: HS_1670(manB)
            XFA: XF0260
            XFT: PD0213(xanA)
            XCC: XCC0626(xanA)
            XCB: XC_3608
            XCV: XCV3703(xanA)
            XAC: XAC3579(xanA)
            XOO: XOO0797(xanA)
            XOM: XOO_0725(XOO0725)
            VCH: VC2095
            VCO: VC0395_A1681(pgm)
            VVU: VV1_0169
            VVY: VV1020
            VPA: VP0839
            VFI: VF0816 VF1056 VF2148
            PPR: PBPRA1040
            PAE: PA5322(algC)
            PPU: PP_1777(xanA) PP_3578 PP_5288
            PST: PSPTO_0083(algC) PSPTO_3035(pgm)
            PSB: Psyr_0219 Psyr_2908
            PSP: PSPPH_0207(algC) PSPPH_2317(pgm)
            PFL: PFL_3231(pgm) PFL_6054
            PFO: Pfl_2670
            PEN: PSEEN2645(pgm) PSEEN5434(algC)
            ACI: ACIAD0104(manB)
            SON: SO_2336(pgm)
            SDN: Sden_1985
            SFR: Sfri_1915
            SHE: Shewmr4_2031
            SHM: Shewmr7_1944
            SHN: Shewana3_2134
            ILO: IL1471(pgm)
            CPS: CPS_1581(pgm)
            PHA: PSHAa1634(pgm)
            PAT: Patl_2198
            PIN: Ping_0879
            MCA: MCA0607(pgm) MCA2782
            FTU: FTT0414(pgm)
            FTF: FTF0414(pgm)
            FTL: FTL_0484
            FTH: FTH_0482(pgm)
            FTA: FTA_0510
            FTN: FTN_0514(pgm)
            TCX: Tcr_1677 Tcr_2017
            NOC: Noc_1719 Noc_2994
            HCH: HCH_01025
            ABO: ABO_0211(pgm)
            AHA: AHA_1537(pgm)
            NME: NMB0790
            NMA: NMA1001(pgm)
            NMC: NMC0743(pgm)
            NGO: NGO0375
            CVI: CV_2172(algC)
            RME: Rmet_2716
            BMA: BMA2191
            BXE: Bxe_B1518 Bxe_C0545
            BPS: BPSL2666(pgm)
            BPM: BURPS1710b_3143
            BTE: BTH_I1489
            RFR: Rfer_1145
            PNA: Pnap_4496
            MMS: mma_2235 mma_2943
            NEU: NE1895
            NET: Neut_2007 Neut_2184
            NMU: Nmul_A0467
            DAR: Daro_1444
            TBD: Tbd_2138
            MFA: Mfla_1921 Mfla_1925
            CJR: CJE1594(algC)
            CJJ: CJJ81176_1406(algC)
            CJU: C8J_1321(algC)
            CJD: JJD26997_1740(algC)
            CFF: CFF8240_0102
            CHA: CHAB381_0418
            NIS: NIS_0946(pgm)
            SUN: SUN_1277(pgm)
            GUR: Gura_4381
            PCA: Pcar_1989
            PPD: Ppro_2017 Ppro_3418
            DVU: DVU1428(pgm)
            DDE: Dde_1695
            LIP: LI0674
            ADE: Adeh_2029
            MXA: MXAN_4888(pgm) MXAN_6499(algC)
            SAT: SYN_01343
            SFU: Sfum_0744
            MLO: mlr7590
            MES: Meso_0831
            SME: SMb21081(manB) SMc03925(pgm)
            ATU: Atu4074(pgm)
            ATC: AGR_L_1564(pgm)
            RET: RHE_CH03597(pgm)
            RLE: RL4118(pgm)
            BME: BMEI1886
            BMF: BAB1_0055(pgm)
            BMS: BR0058(pgm)
            BMB: BruAb1_0058(pgm)
            BOV: BOV_0058(pgm)
            BJA: bll8126 blr2389(celB)
            BRA: BRADO0757 BRADO1937(pgm)
            BBT: BBta_2244(pgm) BBta_7350
            RPA: RPA1484(pgm2)
            RPB: RPB_4039
            RPC: RPC_1233
            RPD: RPD_3793
            RPE: RPE_1281 RPE_3492
            BHE: BH13570(pgm)
            BQU: BQ10790(pgm)
            BBK: BARBAKC583_1175
            CCR: CC_0085 CC_2264
            SIL: SPO0946(algC)
            SIT: TM1040_0652
            RSP: RSP_1863 RSP_2883(pgm)
            RSH: Rsph17029_1529
            JAN: Jann_2725 Jann_3117
            RDE: RD1_2870(pgm)
            PDE: Pden_4423
            MMR: Mmar10_2488
            NAR: Saro_1655
            GOX: GOX0044
            RRU: Rru_A2115
            MAG: amb0574
            MGM: Mmc1_3433
            SUS: Acid_2893 Acid_3937
            BSU: BG10189(yhxB)
            BHA: BH1106
            BAN: BA5153
            BAR: GBAA5153
            BAA: BA_0026
            BAT: BAS4790
            BCE: BC4919
            BCA: BCE_5058
            BCZ: BCZK4651(manB)
            BTK: BT9727_4631(manB)
            BTL: BALH_4459(manB)
            BLI: BL02901
            BCL: ABC1499
            BPU: BPUM_0885
            SAB: SAB2041c SAB2371
            LLM: llmg_0451(femD)
            SPZ: M5005_Spy_1235
            SPH: MGAS10270_Spy1052(pgmA) MGAS10270_Spy1251
            SPI: MGAS10750_Spy1087(pgmA) MGAS10750_Spy1342
            SPJ: MGAS2096_Spy0997(pgmA) MGAS2096_Spy1253
            SPK: MGAS9429_Spy1041(pgmA) MGAS9429_Spy1229
            SPA: M6_Spy0927 M6_Spy1255
            SPB: M28_Spy0910(pgmA) M28_Spy1174
            SSA: SSA_0804(glmM) SSA_1204(pgm)
            LPL: lp_0764(pgm)
            LJO: LJ0862
            LAC: LBA0687
            LSA: LSA0521(pgm)
            LSL: LSL_1176(glmM)
            LDB: Ldb1773(pgm)
            LBU: LBUL_1643
            LBR: LVIS_1907
            LCA: LSEI_0949
            CTC: CTC00454 CTC00779
            CDF: CD1577(pgm1)
            CBO: CBO3114(pgcA)
            CKL: CKL_0798(pgm1) CKL_3180(pgm2)
            DSY: DSY1669
            DRM: Dred_3100
            CSC: Csac_2295
            MTA: Moth_0221
            MMO: MMOB2020(manB)
            MTU: Rv3068c(pgmA)
            MTC: MT3153(pgmA)
            MBO: Mb3095c(pgmA)
            MBB: BCG_3093c(pgmA)
            MPA: MAP3146c(pgmA)
            MSM: MSMEG_1834 MSMEG_2136(pgm)
            MMC: Mmcs_1728
            CGL: NCgl2453(cgl2541)
            CGB: cg0788(pmmB) cg2800(pgm)
            CEF: CE2433
            CDI: DIP1882(pgm)
            CJK: jk0468(pgm)
            NFA: nfa44530
            RHA: RHA1_ro06413
            SCO: SCO7443(pgm)
            SMA: SAV803(pgmA)
            LXX: Lxx02380(pgm)
            AAU: AAur_0094(pgm)
            PAC: PPA1105
            FRA: Francci3_1231
            FAL: FRAAL1271(manB) FRAAL1935(pgm)
            BLO: BL1630(pgm)
            BAD: BAD_0365(pgm)
            FNU: FN0559
            CTA: CTA_0317(mrsA_1)
            BGA: BG0004(femD)
            BAF: BAPKO_0003(femD)
            TPA: TP0413
            TDE: TDE0864
            SYN: sll0726(pgm)
            SYW: SYNW2154(pgm)
            SYC: syc1350_d
            SYF: Synpcc7942_0156 Synpcc7942_1268
            SYD: Syncc9605_2297
            SYE: Syncc9902_0392
            SYG: sync_2500
            SYR: SynRCC307_0402(pmg)
            SYX: SynWH7803_2164(pmg)
            CYA: CYA_1969
            CYB: CYB_2304
            TEL: tlr1976
            GVI: gll3983
            PMA: Pro0090(pgm)
            PMM: PMM0076(pgm)
            PMT: PMT1614(pgm)
            PMN: PMN2A_1440
            PMI: PMT9312_0079 PMT9312_0243
            PMB: A9601_00891(pgm) A9601_02631 A9601_03011
            PMC: P9515_00861(pgm) P9515_02741 P9515_03111
            PMF: P9303_02691(pgm) P9303_24421 P9303_24991
            PMG: P9301_00881(pgm) P9301_02641 P9301_03021
            PMH: P9215_00891
            PME: NATL1_01411(pgm) NATL1_03581
            TER: Tery_0970 Tery_1084
            PVI: Cvib_1521
            DRA: DR_0303(pgm)
            DGE: Dgeo_0352 Dgeo_1875
            TTH: TTC0291 TTC1063 TTC1630
            TTJ: TTHA0353 TTHA0650 TTHA1428
            MBA: Mbar_A2021
            MMA: MM_0301 MM_1521
            MBU: Mbur_2342
            HMA: rrnAC0444(manB2) rrnAC2522(manB3) rrnAC2568(pmm)
                 rrnAC2574(manB1)
            HWA: HQ1024A(pmm) HQ1522A(pmm3) HQ3673A(pmm)
            NPH: NP3514A(pmm_3) NP4660A(pmm_1) NP4676A(pmm_2) NP5158A(pmm_4)
            PTO: PTO1166
            RCI: RCIX1437(pgm-1) RCIX2409(pgm-2)
STRUCTURES  PDB: 1JDY  1KFI  1KFQ  1LXT  1VKL  2F7L  2FKF  2FUV  2H4L  2H5A  
                 3PMG  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.2.2
            ExPASy - ENZYME nomenclature database: 5.4.2.2
            ExplorEnz - The Enzyme Database: 5.4.2.2
            ERGO genome analysis and discovery system: 5.4.2.2
            BRENDA, the Enzyme Database: 5.4.2.2
            CAS: 9001-81-4
///
ENTRY       EC 5.4.2.3                  Enzyme
NAME        phosphoacetylglucosamine mutase;
            acetylglucosamine phosphomutase;
            acetylglucosamine phosphomutase;
            acetylaminodeoxyglucose phosphomutase;
            phospho-N-acetylglucosamine mutase;
            N-acetyl-D-glucosamine 1,6-phosphomutase
CLASS       Isomerases;
            Intramolecular transferases;
            Phosphotransferases (phosphomutases)
SYSNAME     N-acetyl-alpha-D-glucosamine 1,6-phosphomutase
REACTION    N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine
            6-phosphate [RN:R02086]
ALL_REAC    R02086
SUBSTRATE   N-acetyl-alpha-D-glucosamine 1-phosphate [CPD:C04501]
PRODUCT     N-acetyl-D-glucosamine 6-phosphate [CPD:C00357]
EFFECTOR    N-Acetyl-D-glucosamine 1,6-bisphosphate [CPD:C04461]
COMMENT     The enzyme is activated by N-acetyl-alpha-D-glucosamine
            1,6-bisphosphate.
REFERENCE   1
  AUTHORS   Carlson, D.M.
  TITLE     Phosphoacetylglucosamine mutase from pig submaxillary gland.
  JOURNAL   Methods Enzymol. 8 (1966) 179-182.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:13315346]
  AUTHORS   LELOIR LF, CARDINI CE.
  TITLE     Enzymes acting on glucosamine phosphate.
  JOURNAL   Biochim. Biophys. Acta. 20 (1956) 33-42.
  ORGANISM  pig [GN:ssc]
REFERENCE   3
  AUTHORS   Ray, W.J., Jr. and Peck, E.J., Jr.
  TITLE     Phosphomutases.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p.
            407-477.
REFERENCE   4
  AUTHORS   Reissig, J.L. and Leloir, L.F.
  TITLE     Phosphoacetylglucosamine mutase from Neurospora.
  JOURNAL   Methods Enzymol. 8 (1966) 175-178.
  ORGANISM  Neurospora crassa [GN:dncr]
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K01836  phosphoacetylglucosamine mutase
GENES       HSA: 5238(PGM3)
            PTR: 462852(PGM3)
            MMU: 109785(Pgm3)
            CFA: 474981(PGM3)
            GGA: 421841(PGM3)
            XLA: 380578(pgm3)
            DME: Dmel_CG10627
            CEL: F21D5.1
            ATH: AT5G18070(DRT101)
            OSA: 4342646
            CME: CMO272C
            SCE: YEL058W(PCM1)
            AGO: AGOS_ACR015W
            PIC: PICST_81149(PCM1)
            CGR: CAGL0B03597g
            SPO: SPAC1296.01c SPAC13C5.05c SPAC22F3.01
            ANI: AN4234.2
            AFM: AFUA_1G06210
            AOR: AO090001000429
            CNE: CNE01130
            UMA: UM04983.1
            ECU: ECU01_0650
            PFA: PF11_0311
            CPV: cgd4_3310
            CHO: Chro.40374
            TAN: TA15865
            TPV: TP02_0925
            TET: TTHERM_00046870
            TBR: Tb927.8.980
            TCR: 503733.70 508569.80
            LMA: LmjF07.0805
            SYG: sync_0325
            TTH: TTC0691
STRUCTURES  PDB: 1WJW  2DKA  2DKC  2DKD  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.2.3
            ExPASy - ENZYME nomenclature database: 5.4.2.3
            ExplorEnz - The Enzyme Database: 5.4.2.3
            ERGO genome analysis and discovery system: 5.4.2.3
            BRENDA, the Enzyme Database: 5.4.2.3
            CAS: 9027-51-4
///
ENTRY       EC 5.4.2.4                  Enzyme
NAME        bisphosphoglycerate mutase;
            diphosphoglycerate mutase;
            glycerate phosphomutase;
            bisphosphoglycerate synthase;
            bisphosphoglyceromutase;
            biphosphoglycerate synthase;
            diphosphoglyceric mutase;
            2,3-diphosphoglycerate mutase;
            phosphoglyceromutase;
            2,3-diphosphoglycerate synthase;
            DPGM;
            2,3-bisphosphoglycerate mutase;
            BPGM;
            diphosphoglyceromutase;
            2,3-diphosphoglyceromutase
CLASS       Isomerases;
            Intramolecular transferases;
            Phosphotransferases (phosphomutases)
SYSNAME     3-phospho-D-glycerate 1,2-phosphomutase
REACTION    3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
            [RN:R01662]
ALL_REAC    R01662;
            (other) R01516 R01518
SUBSTRATE   3-phospho-D-glyceroyl phosphate [CPD:C00236]
PRODUCT     2,3-bisphospho-D-glycerate [CPD:C01159]
COMMENT     In the direction shown, this enzyme is phosphorylated by
            3-phosphoglyceroyl phosphate, to give phosphoenzyme and
            3-phosphoglycerate. The latter is rephosphorylated by the enzyme to
            yield 2,3-bisphosphoglycerate, but this reaction is slowed by
            dissociation of 3-phosphoglycerate from the enzyme, which is
            therefore more active in the presence of added 3-phosphoglycerate.
            This enzyme also catalyses, slowly, the reactions of EC 3.1.3.13
            (bisphosphoglycerate phosphatase) and EC 5.4.2.1 (phosphoglycerate
            mutase).
REFERENCE   1
  AUTHORS   Ray, W.J., Jr. and Peck, E.J., Jr.
  TITLE     Phosphomutases.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p.
            407-477.
REFERENCE   2  [PMID:5687724]
  AUTHORS   Rose ZB.
  TITLE     The purification and properties of diphosphoglycerate mutase from
            human erythrocytes.
  JOURNAL   J. Biol. Chem. 243 (1968) 4810-20.
  ORGANISM  human [GN:hsa]
REFERENCE   3  [PMID:6255773]
  AUTHORS   Rose ZB.
  TITLE     The enzymology of 2,3-bisphosphoglycerate.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 51 (1980) 211-53.
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
ORTHOLOGY   KO: K01837  bisphosphoglycerate mutase
GENES       HSA: 441531(PGAM4) 5223(PGAM1) 5224(PGAM2) 669(BPGM)
            PTR: 463746(BPGM) 494122(PGAM4)
            MMU: 12183(Bpgm) 18648(Pgam1) 56012(Pgam2)
            RNO: 24642(Pgam1) 24959(Pgam2)
            CFA: 475495(PGAM2) 477786(PGAM1) 482704(BPGM)
            BTA: 404148(PGAM1)
            GGA: 418172(RCJMB04_32o10) 428969(RCJMB04_5g20)
            XLA: 432058(MGC81450) 444102(MGC80400) 447767(MGC84250)
            XTR: 448157(pgam1)
            DRE: 393999(pgam2) 408255(pgam1l)
            DME: Dmel_CG1721(Pglym78)
            HMA: rrnAC2859(gpmB)
STRUCTURES  PDB: 1T8P  1YFK  1YJX  2A9J  2F90  2H4X  2H4Z  2H52  2HHJ  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.2.4
            ExPASy - ENZYME nomenclature database: 5.4.2.4
            ExplorEnz - The Enzyme Database: 5.4.2.4
            ERGO genome analysis and discovery system: 5.4.2.4
            BRENDA, the Enzyme Database: 5.4.2.4
            CAS: 37211-69-1
///
ENTRY       EC 5.4.2.5                  Enzyme
NAME        phosphoglucomutase (glucose-cofactor);
            glucose phosphomutase;
            glucose-1-phosphate phosphotransferase
CLASS       Isomerases;
            Intramolecular transferases;
            Phosphotransferases (phosphomutases)
SYSNAME     alpha-D-glucose 1,6-phosphomutase (glucose-cofactor)
REACTION    alpha-D-glucose 1-phosphate = D-glucose 6-phosphate [RN:R00959]
ALL_REAC    R00959
SUBSTRATE   alpha-D-glucose 1-phosphate [CPD:C00103]
PRODUCT     D-glucose 6-phosphate [CPD:C00092]
EFFECTOR    D-Glucose [CPD:C00031]
COMMENT     The enzyme is activated by D-glucose, which probably acts as an
            acceptor for a phosphate residue from the substrate, thus being
            itself converted into the product.
REFERENCE   1  [PMID:14285271]
  AUTHORS   FUJIMOTO A, INGRAM P, SMITH RA.
  TITLE     D-GLUCOSE-I-PHOSPHATE:D-GLUCOSE-6-PHOSPHOTRANSFERASE.
  JOURNAL   Biochim. Biophys. Acta. 96 (1965) 91-101.
  ORGANISM  Escherichia coli [GN:eco], Escherichia coli [GN:eco], Aerobacter
            aerogene
REFERENCE   2
  AUTHORS   Ray, W.J., Jr. and Peck, E.J., Jr.
  TITLE     Phosphomutases.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p.
            407-477.
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.2.5
            ExPASy - ENZYME nomenclature database: 5.4.2.5
            ExplorEnz - The Enzyme Database: 5.4.2.5
            ERGO genome analysis and discovery system: 5.4.2.5
            BRENDA, the Enzyme Database: 5.4.2.5
            CAS: 37278-22-1
///
ENTRY       EC 5.4.2.6                  Enzyme
NAME        beta-phosphoglucomutase
CLASS       Isomerases;
            Intramolecular transferases;
            Phosphotransferases (phosphomutases)
SYSNAME     beta-D-glucose 1,6-phosphomutase
REACTION    beta-D-glucose 1-phosphate = beta-D-glucose 6-phosphate [RN:R02728]
ALL_REAC    R02728
SUBSTRATE   beta-D-glucose 1-phosphate [CPD:C00663]
PRODUCT     beta-D-glucose 6-phosphate [CPD:C01172]
COMMENT     No cofactor requirement has been demonstrated.
REFERENCE   1
  AUTHORS   Ben-Zvi, R. and Schramm, M.
  TITLE     A phosphoglucomutase specific for beta-glucose 1-phosphate.
  JOURNAL   J. Biol. Chem. 236 (1961) 2186-2189.
  ORGANISM  Neisseria perflava
REFERENCE   2
  AUTHORS   Ray, W.J., Jr. and Peck, E.J., Jr.
  TITLE     Phosphomutases.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p.
            407-477.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K01838  beta-phosphoglucomutase
GENES       ECO: b1317(ycjU)
            ECJ: JW1310(ycjU)
            ECE: Z2465(ycjU)
            ECS: ECs1896
            ECC: c1789(ycjU)
            ECI: UTI89_C1588(ycjU)
            ECP: ECP_1369
            ECV: APECO1_470(ycjU)
            ECW: EcE24377A_1528(pgmB)
            ECX: EcHS_A1432
            SFL: SF1323(ycjU)
            SFX: S1406(ycjU)
            SFV: SFV_1333(ycjU)
            SSN: SSON_1823(ycjU)
            CPS: CPS_0979
            LPN: lpg1092
            LPF: lpl1096
            LPP: lpp1093
            NME: NMB0391
            NMA: NMA2093(pgm2) NMA2097(pgm1)
            NMC: NMC1776(pgm2)
            CVI: CV_1394 CV_1397
            BXE: Bxe_B1761
            GSU: GSU1839
            BSU: BG12422(yvdM)
            BHA: BH3864
            BLI: BL00490(pgcM)
            BLD: BLi00665(pgcM)
            LMO: lmo2831
            LMF: LMOf2365_2822
            LIN: lin2964
            LWE: lwe2761
            LLA: L0001(pgmB)
            LLC: LACR_0484
            LLM: llmg_0456(pgmB)
            SPZ: M5005_Spy_0528
            SPH: MGAS10270_Spy0523
            SPI: MGAS10750_Spy0547
            SPJ: MGAS2096_Spy0540
            SPK: MGAS9429_Spy0519
            SPA: M6_Spy0549
            LPL: lp_0027(pgmB1) lp_0066(pgmB2)
            LJO: LJ0214
            LAC: LBA1869(pgmB)
            LSL: LSL_1279
            LBR: LVIS_1518
            LCA: LSEI_0983
            LGA: LGAS_0217
            LRE: Lreu_0055
            PPE: PEPE_0966
            EFA: EF0956(pgmB) EF3158
            OOE: OEOE_0319
            LME: LEUM_0895
            CAC: CAC2614
            CDF: CD2189(pgmB) CD3128(pgmB)
            TTE: TTE0802
            MPU: MYPU_6350(pgmB)
            MGA: MGA_1263(beta-pgm)
            MMO: MMOB3960(pgmB)
            MSY: MS53_0106(pgmB)
            FAL: FRAAL6634(pgcM)
            SEN: SACE_3173
            SYN: sll1138
            TEL: tll0697
            GVI: glr3176
            ANA: alr3528
            AVA: Ava_3074 Ava_3752 Ava_4630
            PMF: P9303_14541
            GFO: GFO_2135(pgmB)
            CCH: Cag_0071 Cag_0927
            TMA: TM1254
            MAC: MA0451
            MBA: Mbar_A0742
            MMA: MM_0696 MM_1635
            RCI: LRC444(pgmB-1) RCIX511(pgmB-2)
            SAI: Saci_0094(pgmB)
STRUCTURES  PDB: 1LVH  1O03  1O08  1Z4N  1Z4O  1ZOL  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.2.6
            ExPASy - ENZYME nomenclature database: 5.4.2.6
            ExplorEnz - The Enzyme Database: 5.4.2.6
            ERGO genome analysis and discovery system: 5.4.2.6
            BRENDA, the Enzyme Database: 5.4.2.6
            CAS: 68651-99-0
///
ENTRY       EC 5.4.2.7                  Enzyme
NAME        phosphopentomutase;
            phosphodeoxyribomutase;
            deoxyribose phosphomutase;
            deoxyribomutase;
            phosphoribomutase;
            alpha-D-glucose-1,6-bisphosphate:deoxy-D-ribose-1-phosphate
            phosphotransferase;
            D-ribose 1,5-phosphomutase
CLASS       Isomerases;
            Intramolecular transferases;
            Phosphotransferases (phosphomutases)
SYSNAME     alpha-D-ribose 1,5-phosphomutase
REACTION    alpha-D-ribose 1-phosphate = D-ribose 5-phosphate [RN:R01057]
ALL_REAC    R01057;
            (other) R02749
SUBSTRATE   alpha-D-ribose 1-phosphate [CPD:C00620]
PRODUCT     D-ribose 5-phosphate [CPD:C00117]
COFACTOR    D-Ribose 1,5-bisphosphate [CPD:C01151];
            alpha-D-Glucose 1,6-bisphosphate [CPD:C01231];
            2-Deoxy-D-ribose 1,5-bisphosphate [CPD:C04175]
COMMENT     Also converts 2-deoxy-alpha-D-ribose 1-phosphate into
            2-deoxy-D-ribose 5-phosphate. alpha-D-Ribose 1,5-bisphosphate,
            2-deoxy-alpha-D-ribose 1,5-bisphosphate, or alpha-D-glucose
            1,6-bisphosphate can act as cofactor.
REFERENCE   1  [PMID:4992818]
  AUTHORS   Hammer-Jespersen K, Munch-Petersen A.
  TITLE     Phosphodeoxyribomutase from Escherichia coli. Purification and some
            properties.
  JOURNAL   Eur. J. Biochem. 17 (1970) 397-407.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:5824563]
  AUTHORS   Kammen HO, Koo R.
  TITLE     Phosphopentomutases. I. Identification of two activities in rabbit
            tissues.
  JOURNAL   J. Biol. Chem. 244 (1969) 4888-93.
  ORGANISM  rabbit
REFERENCE   3
  AUTHORS   Ray, W.J., Jr. and Peck, E.J., Jr.
  TITLE     Phosphomutases.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p.
            407-477.
PATHWAY     PATH: map00030  Pentose phosphate pathway
            PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01839  phosphopentomutase
GENES       ECO: b4383(deoB)
            ECJ: JW4346(deoB)
            ECE: Z5985(deoB)
            ECS: ECs5342
            ECC: c5467(deoB)
            ECI: UTI89_C5154(deoB)
            ECP: ECP_4767
            ECV: APECO1_1998(deoB)
            ECW: EcE24377A_4982(deoB)
            ECX: EcHS_A4618
            STY: STY4920(deoB)
            STT: t4612(deoB)
            SPT: SPA4383(deoB)
            SEC: SC4417(deoB)
            STM: STM4569(deoB)
            YPE: YPO0439(deoB)
            YPK: y3741(deoB)
            YPM: YP_3743(deoB)
            YPA: YPA_3845
            YPN: YPN_0310
            YPP: YPDSF_3195
            YPS: YPTB0583(deoB)
            YPI: YpsIP31758_3496(deoB)
            YEN: YE0572(b4383)
            SFL: SF4415(deoB)
            SFX: S4686(deoB)
            SFV: SFV_4417(deoB)
            SSN: SSON_4534(deoB)
            SBO: SBO_4445(deoB)
            SDY: SDY_4643(deoB)
            ECA: ECA0729(deoB)
            PLU: plu0521(deoB)
            BUC: BU542(deoB)
            BAS: BUsg522(deoB)
            BAB: bbp484(deoB)
            SGL: SG0396
            ENT: Ent638_0543
            KPN: KPN_04839(deoB)
            SPE: Spro_0662 Spro_4006
            ASU: Asuc_0625
            VCH: VC2348
            VCO: VC0395_A1927(deoB)
            VVU: VV1_1727
            VVY: VV2677
            VPA: VP2434
            VFI: VF0506
            PPR: PBPRA0632
            SON: SO_1219(deoB)
            SDN: Sden_1027
            SFR: Sfri_1004
            SAZ: Sama_0975
            SBL: Sbal_3225
            SBM: Shew185_3228
            SLO: Shew_2813
            SPC: Sputcn32_2820
            SSE: Ssed_3376
            SPL: Spea_3046
            SHE: Shewmr4_1039
            SHM: Shewmr7_1104
            SHN: Shewana3_1043
            SHW: Sputw3181_1191
            ILO: IL1881(deoB)
            CPS: CPS_1976(deoB)
            PHA: PSHAb0081(deoB)
            PIN: Ping_2863
            LPN: lpg0639(deoB)
            LPF: lpl0676(deoB)
            LPP: lpp0693(deoB)
            FTU: FTT0113(deoB)
            FTF: FTF0113(deoB)
            FTW: FTW_0198(deoB)
            FTL: FTL_1664
            FTH: FTH_1605(deoB)
            FTA: FTA_1761(deoB)
            FTN: FTN_1602(deoB)
            HCH: HCH_03075(deoB)
            CSA: Csal_0829
            AHA: AHA_3688(deoB)
            CVI: CV_3699(deoB)
            HPY: HP1179
            HPJ: jhp1105(deoB)
            HPA: HPAG1_1118
            HAC: Hac_0399(deoB)
            PCA: Pcar_2320
            ADE: Adeh_0905
            MLO: mll5587
            MES: Meso_4099
            SME: SMc04119(deoB)
            SMD: Smed_3345
            ATU: Atu0137(drm)
            ATC: AGR_C_219
            RET: RHE_CH00198(deoB)
            RLE: RL0207(deoB)
            BRA: BRADO2070(deoB)
            SIL: SPO2928(deoB)
            SIT: TM1040_1570
            RSP: RSP_1596(deoB)
            RSH: Rsph17029_0249
            RSQ: Rsph17025_0277
            JAN: Jann_2985
            RDE: RD1_3978(deoB)
            PDE: Pden_2221
            MGM: Mmc1_2446
            BSU: BG11331(drm)
            BHA: BH1530
            BAN: BA4309(deoB)
            BAR: GBAA4309(deoB)
            BAA: BA_4767
            BAT: BAS3997
            BCE: BC4087
            BCA: BCE_4156(deoB)
            BCZ: BCZK3844(deoB)
            BCY: Bcer98_2786
            BTK: BT9727_3828(deoB)
            BTL: BALH_3705(deoB)
            BLI: BL00772(drm)
            BLD: BLi02500(drm)
            BCL: ABC1783(drm)
            BAY: RBAM_021610
            BPU: BPUM_2081
            OIH: OB1846(drm)
            GKA: GK2314
            SAU: SA0134(drm)
            SAV: SAV0139(drm)
            SAM: MW0113(drm)
            SAR: SAR0141(drm)
            SAS: SAS0113
            SAC: SACOL0124(deoB)
            SAB: SAB0078(drm)
            SAA: SAUSA300_0141(deoB)
            SAO: SAOUHSC_00101
            SAJ: SaurJH9_0125
            SAH: SaurJH1_0130
            SEP: SE1734
            SER: SERP1743(deoB)
            SHA: SH0899(drm)
            SSP: SSP0749
            LMO: lmo1954(drm)
            LMF: LMOf2365_1984(deoB)
            LIN: lin2068(drm)
            LWE: lwe1980(deoB)
            LLA: L154925(deoB)
            LLC: LACR_1001
            LLM: llmg_1601(deoB)
            SPY: SPy_0890(deoB)
            SPZ: M5005_Spy_0696(deoB)
            SPM: spyM18_0951(deoB)
            SPG: SpyM3_0609(deoB)
            SPS: SPs1244
            SPH: MGAS10270_Spy0754(deoB)
            SPI: MGAS10750_Spy0788(deoB)
            SPJ: MGAS2096_Spy0768(deoB)
            SPK: MGAS9429_Spy0752(deoB)
            SPF: SpyM51112(deoB)
            SPA: M6_Spy0713
            SPB: M28_Spy0676(deoB)
            SPN: SP_0829
            SPR: spr0732(deoB)
            SPD: SPD_0724(deoB)
            SAG: SAG1182(deoB-1) SAG2069(deoB-2)
            SAN: gbs1255 gbs2023
            SAK: SAK_1269(deoB) SAK_2008(deoB)
            SMU: SMU.1233(deoB)
            STC: str1120(deoB)
            STL: stu1120(deoB)
            SSA: SSA_1260(deoB)
            SGO: SGO_1264(deoB)
            LSA: LSA0796(deoB)
            LBR: LVIS_1594
            LCA: LSEI_0279 LSEI_2341
            LRE: Lreu_0112 Lreu_0181
            EFA: EF0185(deoB)
            STH: STH1820
            CAC: CAC2065(deoB)
            CPE: CPE0388(deoB)
            CPF: CPF_0376(deoB)
            CPR: CPR_0371(deoB)
            CTC: CTC01389
            CNO: NT01CX_1497(deoB)
            CTH: Cthe_0677
            CDF: CD1223(deoB)
            CBE: Cbei_3127
            CKL: CKL_1242(deoB)
            CHY: CHY_1963(deoB)
            DSY: DSY2312
            DRM: Dred_1100
            SWO: Swol_0608
            CSC: Csac_2316
            TTE: TTE0463(deoB)
            MTA: Moth_1500
            MPU: MYPU_2770(deoB)
            MMO: MMOB3190(deoB)
            MHY: mhp221(deoB)
            MHJ: MHJ_0157(deoB)
            MHP: MHP7448_0161(deoB)
            MSY: MS53_0083(deoB)
            RXY: Rxyl_0610
            DRA: DR_2135
            DGE: Dgeo_0586
            TTH: TTC1659
            TTJ: TTHA0324
            TMA: TM0167
            TPT: Tpet_0758
STRUCTURES  PDB: 2I09  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.2.7
            ExPASy - ENZYME nomenclature database: 5.4.2.7
            ExplorEnz - The Enzyme Database: 5.4.2.7
            ERGO genome analysis and discovery system: 5.4.2.7
            BRENDA, the Enzyme Database: 5.4.2.7
            CAS: 9026-77-1
///
ENTRY       EC 5.4.2.8                  Enzyme
NAME        phosphomannomutase;
            mannose phosphomutase;
            phosphomannose mutase;
            D-mannose 1,6-phosphomutase
CLASS       Isomerases;
            Intramolecular transferases;
            Phosphotransferases (phosphomutases)
SYSNAME     alpha-D-mannose 1,6-phosphomutase
REACTION    alpha-D-mannose 1-phosphate = D-mannose 6-phosphate [RN:R01818]
ALL_REAC    R01818
SUBSTRATE   alpha-D-mannose 1-phosphate [CPD:C00636]
PRODUCT     D-mannose 6-phosphate [CPD:C00275]
COFACTOR    D-Glucose 1,6-bisphosphate [CPD:C00660];
            D-Mannose 1,6-bisphosphate [CPD:C03693]
COMMENT     alpha-D-Mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate
            can act as cofactor.
REFERENCE   1
  AUTHORS   Small, D.M. and Matheson, N.K.
  TITLE     Phosphomannomutase and phosphoglucomutase in developing Cassia
            corymbosa seeds.
  JOURNAL   Phytochemistry 18 (1979) 1147-1150.
  ORGANISM  Cassia corymbosa
PATHWAY     PATH: map00051  Fructose and mannose metabolism
ORTHOLOGY   KO: K01840  phosphomannomutase
GENES       HSA: 5372(PMM1) 5373(PMM2) 55276(PGM2)
            PTR: 453905(PMM2)
            MMU: 29858(Pmm1) 54128(Pmm2) 66681(Pgm1)
            CFA: 474486(PMM1) 479116(PGM2) 490013(PMM2)
            GGA: 417989(PMM1) 426435(RCJMB04_33e1) 427679(RCJMB04_20k18)
                 776748(PGM2)
            XLA: 446420(pgm2l1) 447608(MGC85250) 495465(LOC495465)
            DRE: 368229(pmm2) 405822(pgm2)
            SPU: 588721(LOC588721)
            DME: Dmel_CG10202 Dmel_CG10688 Dmel_CG8073(Pmm45A)
            CEL: F52B11.2
            ATH: AT2G45790(ATPMM)
            OSA: 4337437 4341038
            CME: CMC121C CMQ067C CMT314C
            SCE: YFL045C(SEC53) YMR278W
            AGO: AGOS_ABL126W AGOS_ABR236W
            PIC: PICST_77262(PMM1) PICST_91072(PGM3)
            CGR: CAGL0K12848g CAGL0M02981g
            SPO: SPAC1556.07(pmm1) SPCC1840.05c
            ANI: AN4591.2 AN5772.2
            AFM: AFUA_2G02120 AFUA_3G03020 AFUA_6G06580
            AOR: AO090001000101 AO090003000030 AO090011000487
            CNE: CNH00170
            UMA: UM04703.1
            ECU: ECU03_0340 ECU05_0260
            DDI: DDBDRAFT_0204675 DDBDRAFT_0215239 DDB_0231660(pmmA)
            PFA: PF10_0169
            CPV: cgd4_960
            CHO: Chro.40115
            TAN: TA07020
            TPV: TP01_0785
            TET: TTHERM_00059380
            TBR: Tb10.70.0370
            TCR: 506405.10 508257.70 510187.480
            LMA: LmjF34.3780 LmjF36.1960
            EHI: 246.t00005 26.t00064 409.t00002
            ECO: b2048(cpsG)
            ECJ: JW2033(cpsG)
            ECE: Z3194(manB) Z3212(cpsG)
            ECS: ECs2835 ECs2853
            ECC: c2557(manB) c2573(cpsG)
            ECI: UTI89_C2321(cpsG)
            ECP: ECP_2073 ECP_2088
            ECV: APECO1_1138(cpsG)
            ECW: EcE24377A_2340
            ECX: EcHS_A2172
            STY: STY2292(rfbK) STY2316(cpsG)
            STT: t0768(manB) t0790(rfbK)
            SPT: SPA0762(manB) SPA0788(rfbK)
            SEC: SC2093(manB) SC2105(cpsG)
            STM: STM2083(rfbK) STM2104(cpsG)
            YPE: YPO2479(manB) YPO3097(manB)
            YPK: y1083(cpsG) y1710(cpsG)
            YPM: YP_0829(manB1) YP_2298(manB2)
            YPA: YPA_1975 YPA_2592
            YPN: YPN_0990 YPN_2073
            YPP: YPDSF_1892 YPDSF_2736
            YPS: YPTB1013(manB) YPTB2520(manB)
            YPI: YpsIP31758_1525(manB2) YpsIP31758_3037(manB1)
            SFL: SF2111(cpsG)
            SFX: S2234(cpsG)
            SSN: SSON_2101(cpsG)
            SBO: SBO_0875(cpsG)
            ECA: ECA1439(rfbK)
            SGL: SG1115
            ENT: Ent638_2643 Ent638_2662
            SPE: Spro_1600
            HIT: NTHI0899(pgmB)
            HDU: HD1507(manB)
            HSO: HS_1118(manB)
            PMU: PM1074(yhxB)
            MSU: MS0346(cpsG) MS0771(cpsG)
            APL: APL_0591(pgm) APL_0652(manB)
            ASU: Asuc_0050
            XFA: XF0151 XF0260
            XFT: PD0213(xanA)
            XCC: XCC0626(xanA) XCC3857(algC)
            XCB: XC_3608 XC_3941
            XCV: XCV3703(xanA) XCV4025(manB)
            XAC: XAC3579(xanA) XAC3912(algC)
            XOO: XOO0498(algC) XOO0797(xanA)
            XOM: XOO_0465(XOO0465) XOO_0725(XOO0725)
            VCH: VC0242 VC0611 VCA1041
            VCO: VC0395_A2622(rfbB)
            VVU: VV1_1664 VV2_0569
            VVY: VV0353 VV2743 VVA1117
            VPA: VP2488 VPA0535
            VFI: VF0816 VF1056 VF2148
            PPR: PBPRA0516 PBPRB0614
            PAE: PA5322(algC)
            PPU: PP_1777(xanA) PP_5288
            PPF: Pput_5197
            PST: PSPTO_0083(algC)
            PSB: Psyr_0219
            PSP: PSPPH_0207(algC)
            PFL: PFL_6054
            PFO: Pfl_5542
            PEN: PSEEN5434(algC)
            PMY: Pmen_4379
            PAR: Psyc_0111(cpsG)
            PCR: Pcryo_0120 Pcryo_0569
            PRW: PsycPRwf_0274
            ACI: ACIAD0104(manB) ACIAD0902(algC)
            SON: SO_1755
            SDN: Sden_1966
            SFR: Sfri_2159
            SHE: Shewmr4_1329 Shewmr4_2541
            SHM: Shewmr7_2608
            SHN: Shewana3_2707
            CPS: CPS_0302(manB)
            PAT: Patl_1793
            SDE: Sde_1001 Sde_3676
            PIN: Ping_0769
            MAQ: Maqu_0458 Maqu_3561
            CBU: CBU_0294
            CBD: COXBU7E912_1786(algC)
            LPN: lpg2486
            LPF: lpl2406(algC)
            LPP: lpp2550(algC)
            MCA: MCA2782
            FTU: FTT1447c(manB)
            FTF: FTF1447c(manB)
            FTL: FTL_0609
            FTH: FTH_0610(manB)
            FTN: FTN_1417(manB)
            TCX: Tcr_1677 Tcr_1905
            NOC: Noc_2994
            AEH: Mlg_2845
            HHA: Hhal_2297
            HCH: HCH_01025 HCH_06439
            CSA: Csal_2983
            ABO: ABO_0937(algC)
            AHA: AHA_2903
            RMA: Rmag_0456
            VOK: COSY_0423
            CVI: CV_2172(algC)
            REU: Reut_A0745
            REH: H16_A1847(manB1) H16_A2445(manB3) H16_A2885(manB2)
            RME: Rmet_2716
            BMA: BMA2191
            BVI: Bcep1808_0826 Bcep1808_6499
            BUR: Bcep18194_A3990
            BCN: Bcen_0414
            BCH: Bcen2424_0893
            BAM: Bamb_0772
            BPS: BPSL2666(pgm)
            BPM: BURPS1710b_3143
            BTE: BTH_I1489
            PNU: Pnuc_1092
            BPE: BP1970(pgm) BP3141(pgm)
            BPA: BPP0800(pgm) BPP2349(pgm)
            BBR: BB0885(pgm) BB1800(pgm)
            RFR: Rfer_2999
            POL: Bpro_1639
            PNA: Pnap_1108
            AAV: Aave_2822
            AJS: Ajs_2021
            VEI: Veis_2559
            HAR: HEAR2721(algC)
            MMS: mma_2943
            NEU: NE1895
            NET: Neut_2007
            NMU: Nmul_A1062
            AZO: azo2778(pgm)
            DAR: Daro_3299
            TBD: Tbd_2138
            HPY: HP1275(algC)
            HPA: HPAG1_1219
            HHE: HH0613(glmM_1)
            HAC: Hac_0209(algC)
            WSU: WS2001
            TDN: Tmden_0623
            CJE: Cj1407c
            CJR: CJE1594(algC)
            CJJ: CJJ81176_1406(algC)
            CJU: C8J_1321(algC)
            CJD: JJD26997_1740(algC)
            CFF: CFF8240_0102
            CHA: CHAB381_0418
            NIS: NIS_1428
            SUN: SUN_1693 SUN_1934(cpsG)
            GSU: GSU2013 GSU3254 GSU3321
            GME: Gmet_0135 Gmet_0990 Gmet_3178
            PCA: Pcar_1311 Pcar_1779 Pcar_1792 Pcar_2958
            DVU: DVU0685
            DVL: Dvul_2278
            DDE: Dde_2945
            LIP: LI0674
            BBA: Bd0014(pmm)
            DPS: DP2231 DP2925
            ADE: Adeh_0160
            AFW: Anae109_0166
            MXA: MXAN_5717 MXAN_6499(algC)
            SAT: SYN_00938
            SFU: Sfum_0481
            RPR: RP509
            RTY: RT0494(exoC)
            RCO: RC0657(exoC)
            RFE: RF_0716(exoC)
            RBE: RBE_0778(exoC)
            WOL: WD0695
            WBM: Wbm0480
            PUB: SAR11_1160(manB)
            MLO: mll7567 mlr5801
            MES: Meso_0831
            ATU: Atu2379(noeK)
            ATC: AGR_C_4315(pmm)
            RET: RHE_CH03243(noeK) RHE_CH03457(ypch01223)
            RLE: RL3674(noeK)
            BME: BMEI1396 BMEII0899
            BMF: BAB1_0560 BAB2_0855
            BMS: BR0537 BRA0348
            BMB: BruAb1_0560 BruAb2_0833
            BRA: BRADO0757 BRADO1937(pgm)
            BBT: BBta_2244(pgm) BBta_7350
            RPA: RPA3321(algC)
            RPB: RPB_1523
            RPC: RPC_4239
            RPD: RPD_1464
            RPE: RPE_3492 RPE_4278
            NWI: Nwi_0361
            NHA: Nham_0458
            SIL: SPO0946(algC)
            SIT: TM1040_0652
            RSP: RSP_0835(manB) RSP_4052(noeK)
            JAN: Jann_4216
            RDE: RD1_B0016(noeK)
            PDE: Pden_4824
            MMR: Mmar10_2488
            ZMO: ZMO0339(exoC)
            NAR: Saro_3316 Saro_3790
            SAL: Sala_3001
            SWI: Swit_2791
            ELI: ELI_13715
            GOX: GOX0044
            GBE: GbCGDNIH1_0590
            ACR: Acry_1021
            RRU: Rru_B0045
            MAG: amb0573
            MGM: Mmc1_0332
            ABA: Acid345_1751
            SUS: Acid_6473
            BSU: BG10189(yhxB)
            BHA: BH1106
            BAN: BA4491 BA5153
            BAR: GBAA4491 GBAA5153
            BAA: BA_0026 BA_4938
            BAT: BAS4169 BAS4790
            BCE: BC4264 BC4919
            BCA: BCE_4347 BCE_5058
            BCZ: BCZK4017 BCZK4651(manB)
            BTK: BT9727_4007 BT9727_4631(manB)
            BTL: BALH_4459(manB)
            BLI: BL02901
            BLD: BLi00997(yhxB)
            BCL: ABC1499
            OIH: OB3037
            GKA: GK0363 GK0570 GK3297
            SAU: SA2279
            SAV: SAV2491
            SAM: MW2411
            SAR: SAR2576
            SAS: SAS2378
            SAC: SACOL2501
            SAA: SAUSA300_2433
            SAO: SAOUHSC_02793
            SEP: SE2042
            SER: SERP2055
            SHA: SH0301
            SSP: SSP1737
            LMO: lmo0865 lmo2475
            LMF: LMOf2365_0882 LMOf2365_1901 LMOf2365_2448
            LIN: lin0858 lin2618
            LWE: lwe0858 lwe2423
            SPY: SPy_1224(pgmA) SPy_1503
            SPZ: M5005_Spy_0938(pgmA) M5005_Spy_1235
            SPM: spyM18_1176 spyM18_1521
            SPG: SpyM3_0864(pgmA) SpyM3_1158
            SPS: SPs0704 SPs1064
            SPH: MGAS10270_Spy1052(pgmA) MGAS10270_Spy1251
            SPI: MGAS10750_Spy1087(pgmA) MGAS10750_Spy1342
            SPJ: MGAS2096_Spy0997(pgmA) MGAS2096_Spy1253
            SPK: MGAS9429_Spy1041(pgmA) MGAS9429_Spy1229
            SPA: M6_Spy0927 M6_Spy1255
            SPB: M28_Spy0910(pgmA) M28_Spy1174
            SPN: SP_1498
            SPR: spr1351(pgm)
            SAG: SAG0493 SAG1066(pgm)
            SAN: gbs0539 gbs1100
            SAK: SAK_0594 SAK_1155
            SMU: SMU.1077(pgm)
            STC: str0787(pgmA)
            STL: stu0787(pgmA)
            SSA: SSA_1204(pgm)
            SGO: SGO_1215(manB)
            EFA: EF0677 EF2425
            STH: STH1118 STH2734
            CAC: CAC2337 CAC2981
            CPE: CPE1873(manB)
            CPF: CPF_2127
            CPR: CPR_1841
            CTC: CTC00454 CTC00779
            CNO: NT01CX_1230 NT01CX_1776
            CBE: Cbei_0228 Cbei_0550
            CHY: CHY_2580
            DSY: DSY1669
            DRM: Dred_1398 Dred_3126
            SWO: Swol_1915 Swol_2154
            CSC: Csac_1371
            TTE: TTE0731(cpsG) TTE2013(gcd1.2) TTE2704(cpsG3)
            MTA: Moth_1925
            MPN: MPN066(cpsG)
            MPE: MYPE1070(manB)
            MGA: MGA_0358(cpsG)
            MMY: MSC_0829(manB)
            MMO: MMOB2020(manB) MMOB2630(manB) MMOB5240(manB)
            MCP: MCAP_0756
            UUR: UU530(cpsG)
            MFL: Mfl120
            MTU: Rv3257c(pmmA) Rv3308(pmmB)
            MTC: MT3355(manB-1) MT3407(manB-2)
            MBO: Mb3285c(manB) Mb3336(pmmB)
            MBB: BCG_3286c(manB) BCG_3373(pmmB)
            MLE: ML0706(pmmB) ML0763(pmmA)
            MPA: MAP3369c(pmmA) MAP3430(pmmB)
            MSM: MSMEG_1695 MSMEG_1834
            MVA: Mvan_1737
            MGI: Mflv_4726
            MMC: Mmcs_1241 Mmcs_1328
            MKM: Mkms_1345
            MJL: Mjls_1364
            CGL: NCgl0656(cgl0687) NCgl0714(cgl0746)
            CGB: cg0788(pmmB) cg0854(pmmA)
            CEF: CE0706 CE0762
            CDI: DIP0274 DIP0687
            CJK: jk1641(pmmA) jk1675(pmmB)
            NFA: nfa46250(cpsG) nfa9600
            RHA: RHA1_ro06256 RHA1_ro06316(manB)
            SCO: SCO1388(SC1A8A.08c) SCO3028(manB) SCO4916(SCK13.08c)
            SMA: SAV3343(pmmB) SAV5048(manB) SAV6977(mpg3)
            TWH: TWT017(pmmB) TWT127(pmmA)
            TWS: TW017 TW137(manB)
            LXX: Lxx04690(cpsG)
            CMI: CMM_0988(manB)
            ART: Arth_0671 Arth_1952
            AAU: AAur_0836(manB) AAur_1400
            PAC: PPA1723 PPA2286
            NCA: Noca_1425
            TFU: Tfu_1394 Tfu_2510
            FRA: Francci3_0690 Francci3_0751 Francci3_1463
            FAL: FRAAL1199 FRAAL1271(manB) FRAAL2265
            ACE: Acel_0465
            KRA: Krad_3841
            SEN: SACE_6460(manB) SACE_6548(pmmB)
            STP: Strop_0961
            RXY: Rxyl_1134
            FNU: FN0559
            RBA: RB6061(pmm) RB9832
            CTR: CT295(mrsA_1)
            CTA: CTA_0317(mrsA_1)
            CMU: TC0568
            CPN: CPn0056(mrsA)
            CPA: CP0719
            CPJ: CPj0056(mrsA)
            CPT: CpB0057
            CCA: CCA00344
            CAB: CAB336
            CFE: CF0662(mrsA2)
            PCU: pc1262(pgm)
            BGA: BG0860(cpsG)
            BAF: BAPKO_0888(cpsG)
            TPA: TP0642
            TDE: TDE1998
            LIL: LA2154(manB) LA3800(pgm)
            LIC: LIC10446 LIC11766(manB)
            LBJ: LBJ_1861(manB-2)
            LBL: LBL_1423(manB-2)
            SYN: sll1496 slr1334
            SYW: SYNW0235
            SYC: syc0283_d syc1022_c
            SYF: Synpcc7942_0498
            SYD: Syncc9605_0228
            SYE: Syncc9902_0257
            SYG: sync_0273(pmm)
            SYR: SynRCC307_2298
            SYX: SynWH7803_0278
            CYA: CYA_0009
            CYB: CYB_0014
            TEL: tlr0436 tlr1520
            GVI: gll3341 glr0388
            ANA: all3964 all5089 alr2361
            AVA: Ava_0182 Ava_1737 Ava_2367
            PMA: Pro0310(manB)
            PMM: PMM0278
            PMT: PMT1871
            PMN: PMN2A_1644
            PMI: PMT9312_0280
            PMB: A9601_03011
            PMC: P9515_03111
            PMF: P9303_24991
            PMG: P9301_03021
            PME: NATL1_03581
            TER: Tery_3188
            BTH: BT_1548 BT_3950
            BFR: BF1478 BF3898
            BFS: BF1409 BF3668
            PGI: PG1094(pgm) PG2010
            SRU: SRU_2202 SRU_2367(pgm)
            CHU: CHU_0998(pgm) CHU_3484(cpsG)
            FJO: Fjoh_4504
            CTE: CT0260 CT0279
            CCH: Cag_0454 Cag_0474
            CPH: Cpha266_0410
            PLT: Plut_1740 Plut_1760
            DET: DET0510 DET0528
            DEH: cbdb_A474 cbdb_A497(pmmB)
            DEB: DehaBAV1_0486
            RRS: RoseRS_2652 RoseRS_4124
            RCA: Rcas_1218 Rcas_2720
            DRA: DR_A0047
            DGE: Dgeo_0352
            TTH: TTC0291 TTC0691 TTC1063
            TTJ: TTHA0650 TTHA1428
            AAE: aq_501(pmu) aq_718(mpg)
            TMA: TM0769
            TME: Tmel_0573
            FNO: Fnod_0486
            MJA: MJ1100
            MMP: MMP1077 MMP1372(manB)
            MMQ: MmarC5_0206
            MMZ: MmarC7_0617
            MAE: Maeo_0032
            MVN: Mevan_0682
            MAC: MA0241 MA2665(pmm) MA3024(pmmB)
            MBA: Mbar_A0721 Mbar_A2021 Mbar_A2225
            MMA: MM_0301 MM_1521
            MBU: Mbur_2342
            MHU: Mhun_2852
            MEM: Memar_2432
            MBN: Mboo_0714
            MST: Msp_0263 Msp_1300
            MSI: Msm_0648 Msm_0656
            MKA: MK0893(cpsG_1) MK0920(cpsG_2)
            HAL: VNG0905G(pmu2) VNG2206G(pmu1) VNG2276G(pmm)
            HMA: rrnAC0444(manB2) rrnAC2522(manB3) rrnAC2568(pmm)
                 rrnAC2574(manB1)
            HWA: HQ1024A(pmm) HQ1522A(pmm3) HQ3673A(pmm)
            NPH: NP3514A(pmm_3) NP4660A(pmm_1) NP4676A(pmm_2) NP5158A(pmm_4)
            TAC: Ta0568
            TVO: TVN0620
            PTO: PTO1166
            PHO: PH0923 PH1210
            PAB: PAB0819(pmm) PAB1666
            PFU: PF0588 PF0861
            TKO: TK1108 TK1777 TK2185
            APE: APE_0317.1 APE_2433.1
            SSO: SSO0207(pmm)
            STO: ST0242
            SAI: Saci_0806
            PAI: PAE0764(pmm)
            PIS: Pisl_1061
            PCL: Pcal_2157
            PAS: Pars_0025
            TPE: Tpen_0810
STRUCTURES  PDB: 1K2Y  1K35  1P5D  1P5G  1PCJ  1PCM  1WQA  2AMY  2F7L  2FKF  
                 2FKM  2FUC  2FUE  2H4L  2H5A  2I54  2I55  2Q4R  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.2.8
            ExPASy - ENZYME nomenclature database: 5.4.2.8
            ExplorEnz - The Enzyme Database: 5.4.2.8
            ERGO genome analysis and discovery system: 5.4.2.8
            BRENDA, the Enzyme Database: 5.4.2.8
            CAS: 59536-73-1
///
ENTRY       EC 5.4.2.9                  Enzyme
NAME        phosphoenolpyruvate mutase;
            phosphoenolpyruvate-phosphonopyruvate phosphomutase;
            PEP phosphomutase;
            phosphoenolpyruvate phosphomutase;
            PEPPM;
            PEP phosphomutase
CLASS       Isomerases;
            Intramolecular transferases;
            Phosphotransferases (phosphomutases)
SYSNAME     phosphoenolpyruvate 2,3-phosphonomutase
REACTION    phosphoenolpyruvate = 3-phosphonopyruvate [RN:R00661]
ALL_REAC    R00661
SUBSTRATE   phosphoenolpyruvate [CPD:C00074]
PRODUCT     3-phosphonopyruvate [CPD:C02798]
COMMENT     Involved in the biosynthesis of the C-P bond, although the
            equilibrium greatly favours phosphoenolpyruvate.
REFERENCE   1
  AUTHORS   Bowman, E., McQueney, M., Barry, R.J. and Dunaway-Mariano, D.
  TITLE     Catalysis and thermodynamics of the phosphoenolpyruvate
            phosphonopyruvate rearrangement - entry into the phosphonate class
            of naturally-occurring organo-phosphorus compounds.
  JOURNAL   J. Am. Chem. Soc. 110 (1988) 5575-5576.
  ORGANISM  Tetrahymena pyriformis
REFERENCE   2  [PMID:2160937]
  AUTHORS   Hidaka T, Imai S, Hara O, Anzai H, Murakami T, Nagaoka K, Seto H.
  TITLE     Carboxyphosphonoenolpyruvate phosphonomutase, a novel enzyme
            catalyzing C-P bond formation.
  JOURNAL   J. Bacteriol. 172 (1990) 3066-72.
  ORGANISM  Streptomyces hygroscopicus
REFERENCE   3  [PMID:3138545]
  AUTHORS   Seidel HM, Freeman S, Seto H, Knowles JR.
  TITLE     Phosphonate biosynthesis: isolation of the enzyme responsible for
            the formation of a carbon-phosphorus bond.
  JOURNAL   Nature. 335 (1988) 457-8.
  ORGANISM  Tetrahymena pyriformis
PATHWAY     PATH: map00440  Aminophosphonate metabolism
ORTHOLOGY   KO: K01841  phosphoenolpyruvate phosphomutase
GENES       TET: TTHERM_00022810
            TCR: 508851.189 511589.140
            VFI: VF1249
            PEN: PSEEN3956
            SDN: Sden_1161
            NOC: Noc_1317
            RME: Rmet_1808
            BMA: BMAA1768(pepM)
            BMV: BMASAVP1_0758(pepM)
            BML: BMA10299_1051(pepM)
            BMN: BMA10247_A2026(pepM)
            BXE: Bxe_B2235
            BUR: Bcep18194_B1914
            BCN: Bcen_4245
            BCH: Bcen2424_4121
            BPS: BPSS0509
            BPM: BURPS1710b_A2065(pepM)
            BPL: BURPS1106A_A0691
            BPD: BURPS668_A0780
            BTE: BTH_II1908
            BBR: BB1046(pepM)
            AZO: azo2698(pepM)
            PCA: Pcar_0628
            MLO: mlr5882 mlr9115
            RPC: RPC_3871
            BAY: RBAM_022400(yqiQ)
            CTC: CTC01698
            FRA: Francci3_1533
            FAL: FRAAL6377
            TDE: TDE1413
            BTH: BT_1720
            BFR: BF1832
            BFS: BF1897(aepX)
STRUCTURES  PDB: 1M1B  1PYM  1S2T  1S2U  1S2V  1S2W  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.2.9
            ExPASy - ENZYME nomenclature database: 5.4.2.9
            ExplorEnz - The Enzyme Database: 5.4.2.9
            ERGO genome analysis and discovery system: 5.4.2.9
            BRENDA, the Enzyme Database: 5.4.2.9
            CAS: 115756-49-5
///
ENTRY       EC 5.4.2.10                 Enzyme
NAME        phosphoglucosamine mutase
CLASS       Isomerases;
            Intramolecular transferases;
            Phosphotransferases (phosphomutases)
SYSNAME     alpha-D-glucosamine 1,6-phosphomutase
REACTION    alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
            [RN:R02060]
ALL_REAC    R02060
SUBSTRATE   alpha-D-glucosamine 1-phosphate [CPD:C06156]
PRODUCT     D-glucosamine 6-phosphate [CPD:C00352]
COMMENT     The enzyme is involved in the pathway for bacterial cell-wall
            peptidoglycan and lipopolysaccharide biosyntheses, being an
            essential step in the pathway for UDP-N-acetylglucosamine
            biosynthesis. The enzyme from Escherichia coli is activated by
            phosphorylation and can be autophosphorylated in vitro by
            alpha-D-glucosamine 1,6-bisphosphate, which is an intermediate in
            the reaction, alpha-D-glucose 1,6-bisphosphate or ATP. It can also
            catalyse the interconversion of alpha-D-glucose 1-phosphate and
            glucose 6-phosphate, although at a much lower rate.
REFERENCE   1  [PMID:8550580]
  AUTHORS   Mengin-Lecreulx D, van Heijenoort J.
  TITLE     Characterization of the essential gene glmM encoding
            phosphoglucosamine mutase in Escherichia coli.
  JOURNAL   J. Biol. Chem. 271 (1996) 32-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:9171391]
  AUTHORS   De Reuse H, Labigne A, Mengin-Lecreulx D.
  TITLE     The Helicobacter pylori ureC gene codes for a phosphoglucosamine
            mutase.
  JOURNAL   J. Bacteriol. 179 (1997) 3488-93.
  ORGANISM  Helicobacter pylori
REFERENCE   3  [PMID:9286983]
  AUTHORS   Jolly L, Wu S, van Heijenoort J, de Lencastre H, Mengin-Lecreulx D,
            Tomasz A.
  TITLE     The femR315 gene from Staphylococcus aureus, the interruption of
            which results in reduced methicillin resistance, encodes a
            phosphoglucosamine mutase.
  JOURNAL   J. Bacteriol. 179 (1997) 5321-5.
  ORGANISM  Staphylococcus aureus
REFERENCE   4  [PMID:10231382]
  AUTHORS   Jolly L, Ferrari P, Blanot D, Van Heijenoort J, Fassy F,
            Mengin-Lecreulx D.
  TITLE     Reaction mechanism of phosphoglucosamine mutase from Escherichia
            coli.
  JOURNAL   Eur. J. Biochem. 262 (1999) 202-10.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:10671448]
  AUTHORS   Jolly L, Pompeo F, van Heijenoort J, Fassy F, Mengin-Lecreulx D.
  TITLE     Autophosphorylation of phosphoglucosamine mutase from Escherichia
            coli.
  JOURNAL   J. Bacteriol. 182 (2000) 1280-5.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00530  Aminosugars metabolism
ORTHOLOGY   KO: K03431  phosphoglucosamine mutase
GENES       ECO: b3176(glmM)
            ECJ: JW3143(glmM)
            ECE: Z4538(mrsA)
            ECS: ECs4055
            ECC: c3932(mrsA)
            ECI: UTI89_C3608(mrsA)
            ECP: ECP_3263
            ECV: APECO1_3256(glmM)
            ECW: EcE24377A_3661(glmM)
            ECX: EcHS_A3368(glmM)
            STY: STY3472
            STT: t3211
            SPT: SPA3161(mrsA)
            SEC: SC3233(mrsA)
            STM: STM3294(mrsA)
            YPE: YPO3500(mrsA)
            YPK: y0684(mrsA)
            YPM: YP_0583(mrsA)
            YPA: YPA_0050
            YPN: YPN_3244
            YPP: YPDSF_3549
            YPS: YPTB0476(mrsA)
            YPI: YpsIP31758_3600(glmM)
            YEN: YE0430(mrsA)
            SFL: SF3216(mrsA)
            SFX: S3434(mrsA)
            SFV: SFV_3206(mrsA)
            SSN: SSON_3324(mrsA)
            SBO: SBO_3206(mrsA)
            SDY: SDY_3357(mrsA)
            ECA: ECA0700(mrsA)
            PLU: plu4533(mrsA)
            BUC: BU381(mrsA)
            BAB: bbp344(mrsA)
            WBR: WGLp229(mrsA)
            SGL: SG0373
            BFL: Bfl100(mrsA)
            BPN: BPEN_103(mrsA)
            HIN: HI1337(mrsA)
            HIT: NTHI1664(mrsA)
            HDU: HD0201(mrsA)
            HSO: HS_0730(mrsA)
            PMU: PM0440(mrsA)
            MSU: MS0967(cpsG)
            APL: APL_1454(mrsA)
            XFA: XF1468
            XFT: PD0686(mrsA)
            XCC: XCC2539(mrsA)
            XCB: XC_1579
            XCV: XCV2863(mrsA)
            XAC: XAC2714(mrsA)
            XOO: XOO3249(mrsA)
            XOM: XOO_3077(XOO3077)
            VCH: VC0639(mrsA)
            VVU: VV1_1692
            VVY: VV2713
            VPA: VP2461(mrsA)
            VFI: VF0481
            PPR: PBPRA0606
            PAE: PA4749(glmM)
            PAU: PA14_62840(glmM)
            PAP: PSPA7_5469(glmM)
            PPU: PP_4716(glmM)
            PPF: Pput_4582
            PST: PSPTO_4495(glmM)
            PSB: Psyr_4185
            PSP: PSPPH_4196(glmM)
            PFL: PFL_0838(glmM)
            PFO: Pfl_0774
            PEN: PSEEN0789(glmM)
            PAR: Psyc_1359
            PCR: Pcryo_1006
            ACI: ACIAD3502(glmM)
            SON: SO_1199(glmM)
            SDN: Sden_1002
            SFR: Sfri_0985
            SAZ: Sama_0956
            SBL: Sbal_3244
            SHE: Shewmr4_1021 Shewmr4_1333
            SHM: Shewmr7_1086 Shewmr7_1398
            SHN: Shewana3_1025
            SHW: Sputw3181_1065
            ILO: IL0973(mrsA)
            CPS: CPS_3449(glmM)
            PHA: PSHAa0872(glmM)
            PAT: Patl_1573
            SDE: Sde_2718
            MAQ: Maqu_3353
            CBU: CBU_1350(glmM)
            CBD: COXBU7E912_1438(glmM)
            LPN: lpg2794(mrsA)
            LPF: lpl2709(msrA)
            LPP: lpp2840(msrA)
            MCA: MCA1847(glmM)
            FTU: FTT0079(mrsA)
            FTF: FTF0079(mrsA)
            FTW: FTW_0155(mrsA)
            FTL: FTL_1781
            FTH: FTH_1717(mrsA)
            FTA: FTA_1887(glmM)
            FTN: FTN_1632(mrsA)
            TCX: Tcr_0814
            NOC: Noc_2567
            AEH: Mlg_1973
            HCH: HCH_01234(glmM)
            CSA: Csal_3079
            ABO: ABO_0324(glmM)
            AHA: AHA_3310(glmM)
            BCI: BCI_0636(glmM)
            VOK: COSY_0140(glmM)
            NME: NMB1690
            NMA: NMA1949
            NMC: NMC1608
            NGO: NGO1341
            CVI: CV_3795(glmM)
            RSO: RSc1528(mrsA)
            REU: Reut_A2168
            RME: Rmet_2186
            BMA: BMA0779(glmM)
            BXE: Bxe_A1264
            BUR: Bcep18194_A4441
            BCN: Bcen_0818
            BCH: Bcen2424_1299
            BAM: Bamb_1176
            BPS: BPSL1358
            BPM: BURPS1710b_1617(glmM)
            BPL: BURPS1106A_1514(glmM)
            BPD: BURPS668_1484(glmM)
            BTE: BTH_I2774(glmM)
            PNU: Pnuc_1011
            BPE: BP1075(mrsA)
            BPA: BPP2069(mrsA)
            BBR: BB1462(mrsA)
            RFR: Rfer_2013
            POL: Bpro_2850
            PNA: Pnap_2609
            AAV: Aave_2619
            AJS: Ajs_2381
            VEI: Veis_0209
            MPT: Mpe_A1270
            HAR: HEAR1172(glmM)
            NEU: NE0530(mrsA)
            NET: Neut_1000
            NMU: Nmul_A0485
            EBA: ebA4825(mrsA)
            AZO: azo1389(glmM)
            DAR: Daro_0946
            TBD: Tbd_1135
            MFA: Mfla_0785
            HPY: HP0075(ureC)
            HPJ: jhp0070(glmM)
            HPA: HPAG1_0076
            HHE: HH1779(glmM_2)
            HAC: Hac_1529(mrsA)
            WSU: WS0818
            TDN: Tmden_2039
            CJE: Cj0360
            CJR: CJE0409(glmM)
            CJU: C8J_0336
            CFF: CFF8240_1717(glmM)
            CCV: CCV52592_0742(glmM)
            CHA: CHAB381_1789(glmM)
            CCO: CCC13826_1807(glmM) CCC13826_2149
            ABU: Abu_0081(glmM)
            GSU: GSU1805(glmM)
            GME: Gmet_1886
            PCA: Pcar_1001
            DVU: DVU1282(glmM)
            DDE: Dde_1517
            LIP: LI0192
            BBA: Bd1931(glmM)
            DPS: DP1641
            ADE: Adeh_1499
            AFW: Anae109_2334
            MXA: MXAN_4352(glmM)
            SAT: SYN_02959
            SFU: Sfum_2913
            AMA: AM940(glmM)
            PUB: SAR11_0603(mrsA)
            MLO: mll3879(mrsA)
            MES: Meso_3166
            SME: SMc00637
            SMD: Smed_2622
            ATU: Atu3709(mrsA)
            ATC: AGR_L_2256(mrsA)
            RLE: RL3964(glmM)
            BME: BMEI0344
            BMF: BAB1_1702(glmM)
            BMS: BR1690(glmM)
            BMB: BruAb1_1675(glmM)
            BOV: BOV_1634(glmM)
            BJA: bll7408
            BRA: BRADO5957(glmM)
            BBT: BBta_1817(glmM)
            RPA: RPA4318(mrsA)
            RPB: RPB_1307
            RPC: RPC_4113
            RPD: RPD_3914
            RPE: RPE_4168
            NWI: Nwi_2973
            NHA: Nham_1114
            BHE: BH14740(mrsA)
            BQU: BQ11740(mrsA)
            BBK: BARBAKC583_0171(glmM)
            XAU: Xaut_2566
            CCR: CC_0117
            SIL: SPO1364(glmM)
            SIT: TM1040_2305
            RSP: RSP_1863
            RSQ: Rsph17025_0649
            RDE: RD1_1952(glmM)
            MMR: Mmar10_2490
            HNE: HNE_0168(glmM)
            ZMO: ZMO1002(mrsA)
            NAR: Saro_0481
            SAL: Sala_0960
            ELI: ELI_10245
            GOX: GOX1692(mrsA)
            GBE: GbCGDNIH1_1112
            ACR: Acry_0817
            RRU: Rru_A1100
            MAG: amb3199
            MGM: Mmc1_0360
            ABA: Acid345_0276 Acid345_0571
            BSU: BG12704(glmM)
            BHA: BH0267
            BAN: BA0157(glmM)
            BAR: GBAA0157(glmM)
            BAA: BA_0738
            BAT: BAS0158
            BCE: BC0188
            BCA: BCE_0157(glmM)
            BCZ: BCZK0150(glmM)
            BTK: BT9727_0152(glmM)
            BTL: BALH_0154(glmM)
            BLI: BL02703(glmM)
            BLD: BLi00203(ybbT)
            BCL: ABC0243(glmM)
            BAY: RBAM_002300(ybbT)
            BPU: BPUM_0164(glmM)
            OIH: OB0232
            GKA: GK0154
            SAU: SA1965(glmM(femD))
            SAV: SAV2161(glmM(femD))
            SAM: MW2088(glmM)
            SAR: SAR2252
            SAS: SAS2063
            SAC: SACOL2151(glmM)
            SAA: SAUSA300_2111(glmM)
            SAO: SAOUHSC_02405
            SEP: SE1752
            SER: SERP1762(glmM)
            SHA: SH0879(femD)
            SSP: SSP0724
            LMO: lmo2118
            LMF: LMOf2365_2151(glmM)
            LIN: lin2223
            LWE: lwe2137(glmM)
            LLA: L35068(femD)
            LLC: LACR_0479
            SPY: SPy_1038
            SPZ: M5005_Spy_0763(femD)
            SPM: spyM18_1020
            SPG: SpyM3_0671
            SPS: SPs1182
            SPH: MGAS10270_Spy0880(femD)
            SPI: MGAS10750_Spy0915(femD)
            SPJ: MGAS2096_Spy0837(femD)
            SPK: MGAS9429_Spy0878(femD)
            SPA: M6_Spy0788
            SPB: M28_Spy0742(femD)
            SPN: SP_1559
            SPR: spr1417(glmM)
            SAG: SAG0887
            SAN: gbs0904
            SAK: SAK_1010(glmM)
            SMU: SMU.1426c
            STC: str1251
            STL: stu1251
            SSA: SSA_0804(glmM)
            LPL: lp_0820(glmM)
            LJO: LJ0894
            LAC: LBA0716
            LSA: LSA1357(glmM)
            LSL: LSL_1144(glmM)
            LDB: Ldb0654(manB)
            LBU: LBUL_0584
            LBR: LVIS_0686
            LCA: LSEI_1018
            LRE: Lreu_0409
            STH: STH194
            CAC: CAC0484
            CPE: CPE2329
            CPF: CPF_2638(glmM)
            CPR: CPR_2324(glmM)
            CTC: CTC02544
            CNO: NT01CX_1165(glmM)
            CDF: CD0119
            CBO: CBO3420(glmM)
            CBA: CLB_3477(glmM)
            CBH: CLC_3365(glmM)
            CBF: CLI_3603(glmM)
            CBE: Cbei_0210
            CKL: CKL_0316(glmM)
            AMT: Amet_4300
            CHY: CHY_2012(glmM)
            DSY: DSY4486
            CSC: Csac_0605
            TTE: TTE2191(cpsG2)
            MTA: Moth_2246
            MTU: Rv3441c(mrsA)
            MTC: MT3546
            MBO: Mb3471c(mrsA)
            MLE: ML0366(mrsA)
            MPA: MAP4247(mrsA)
            MAV: MAV_4384(glmM)
            MSM: MSMEG_1559(glmM)
            MMC: Mmcs_1134
            CGL: NCgl0558(cgl0583)
            CGB: cg0675(mrsA)
            CEF: CE0588
            CDI: DIP0563
            CJK: jk1743(pmmC)
            NFA: nfa8680(glmM)
            RHA: RHA1_ro06173
            SCO: SCO4736(SC6G4.14)
            SMA: SAV4959(mrsA)
            TWH: TWT146(mrsA)
            TWS: TW155
            LXX: Lxx20010(mrsA)
            PAC: PPA1801
            TFU: Tfu_2612
            FRA: Francci3_0616
            FAL: FRAAL1116(glmM)
            ACE: Acel_0343
            SEN: SACE_6779(glmM)
            STP: Strop_3862
            BLO: BL1187(mrsA)
            BAD: BAD_1294(mrsA)
            RXY: Rxyl_2119
            FNU: FN0366
            CTR: CT815(mrsA_2)
            CTA: CTA_0888(mrsA_2)
            CMU: TC0202
            CPN: CPn0967(pgm)
            CPA: CP0893
            CPJ: CPj0967(pgm)
            CPT: CpB1004
            CCA: CCA00789(glmM)
            CAB: CAB757
            CFE: CF0224(mrsA1)
            PCU: pc1307(pgm)
            SYN: sll1758
            SYW: SYNW0282
            SYC: syc1960_c(manB)
            SYF: Synpcc7942_2132
            SYD: Syncc9605_0277
            SYE: Syncc9902_2067
            TEL: tll1772
            ANA: alr1900
            AVA: Ava_3769
            PMA: Pro0271(manB)
            PMM: PMM0241
            PMT: PMT1823
            PMB: A9601_02631
            PMC: P9515_02741
            PMF: P9303_24421
            PMG: P9301_02641
            TER: Tery_1095
            DEB: DehaBAV1_0504
            DRA: DR_2071
            DGE: Dgeo_1664
            TTJ: TTHA1056
            TMA: TM0184
            MMZ: MmarC7_0330
            MAE: Maeo_0433
            MVN: Mevan_0400
            MBU: Mbur_2115
            SMR: Smar_1286
            IHO: Igni_0885
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.2.10
            ExPASy - ENZYME nomenclature database: 5.4.2.10
            ExplorEnz - The Enzyme Database: 5.4.2.10
            ERGO genome analysis and discovery system: 5.4.2.10
            BRENDA, the Enzyme Database: 5.4.2.10
///
ENTRY       EC 5.4.3.1        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring amino groups
COMMENT     Deleted entry: ornithine 4,5-aminomutase. This reaction was due to a
            mixture of EC 5.1.1.12 (ornithine racemase) and EC 5.4.3.5
            (D-ornithine 4,5-aminomutase) (EC 5.4.3.1 created 1972, deleted
            1976)
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.3.1
            ExPASy - ENZYME nomenclature database: 5.4.3.1
            ExplorEnz - The Enzyme Database: 5.4.3.1
            ERGO genome analysis and discovery system: 5.4.3.1
            BRENDA, the Enzyme Database: 5.4.3.1
///
ENTRY       EC 5.4.3.2                  Enzyme
NAME        lysine 2,3-aminomutase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring amino groups
SYSNAME     L-lysine 2,3-aminomutase
REACTION    L-lysine = (3S)-3,6-diaminohexanoate [RN:R00461]
ALL_REAC    R00461
SUBSTRATE   L-lysine [CPD:C00047]
PRODUCT     (3S)-3,6-diaminohexanoate [CPD:C01142]
COFACTOR    Pyridoxal phosphate [CPD:C00018];
            S-Adenosyl-L-methionine [CPD:C00019]
COMMENT     Activity is stimulated by S-adenosyl-L-methionine and pyridoxal
            phosphate.
REFERENCE   1
  AUTHORS   Aberhart, D.J., Lim, H.-J. and Weiller, B.H.
  TITLE     Stereochemistry of lysine 2,3-aminomutase.
  JOURNAL   J. Am. Chem. Soc. 103 (1981) 6750-6752.
  ORGANISM  Clostridium subterminale
REFERENCE   2  [PMID:5452674]
  AUTHORS   Zappia V, Barker HA.
  TITLE     Studies on lysine-2,3-aminomutase. Subunit structure and sulfhydryl
            groups.
  JOURNAL   Biochim. Biophys. Acta. 207 (1970) 505-13.
PATHWAY     PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K01843  lysine 2,3-aminomutase
GENES       ECI: UTI89_C4744(yjeK)
            ECV: APECO1_2243(yjeK)
            BAB: bbp022(yjeK)
            SGL: SG0308
            SPE: Spro_0411
            HIT: NTHI0447
            ASU: Asuc_2106
            VFI: VF2339
            PSP: PSPPH_4554
            PAR: Psyc_1679(kamA)
            PCR: Pcryo_1949
            PRW: PsycPRwf_0487
            SSE: Ssed_1818
            CPS: CPS_0971
            PHA: PSHAa0473(kamA)
            TCX: Tcr_1742
            NOC: Noc_2627
            MMW: Mmwyl1_0898
            DNO: DNO_0590(kamA)
            VOK: COSY_0303(kamA)
            BCN: Bcen_5091
            BCH: Bcen2424_5769
            RFR: Rfer_3891
            GSU: GSU1754(kamA)
            GME: Gmet_1840
            GUR: Gura_2149
            PCA: Pcar_1401 Pcar_2520
            DDE: Dde_0189 Dde_2747 Dde_3041
            BBA: Bd3344(kamA)
            DPS: DP2159
            ADE: Adeh_2548
            AFW: Anae109_1315 Anae109_1316
            MXA: MXAN_4698(kamA)
            SAT: SYN_00182 SYN_02634
            SFU: Sfum_0711
            MLO: mll1971
            SME: SMc00355
            SMD: Smed_3476
            ATU: Atu2555(kamA)
            ATC: AGR_C_4629
            RET: RHE_CH04042(kamA)
            RLE: RL4598
            BJA: blr4388
            RPA: RPA2515(kamA)
            RPB: RPB_2954
            RPC: RPC_2807
            RPD: RPD_2506
            RPE: RPE_2928
            NWI: Nwi_1641
            NHA: Nham_2300
            XAU: Xaut_3908
            CCR: CC_0716
            RSP: RSP_3227
            HNE: HNE_3138
            GOX: GOX0234
            GBE: GbCGDNIH1_1087
            ACR: Acry_2376
            RRU: Rru_A0224
            MAG: amb1284
            BSU: BG13542(kamA)
            BHA: BH2255
            BAN: BA2300(kamA)
            BAR: GBAA2300(kamA)
            BAA: BA_2804
            BAT: BAS2145
            BCE: BC2251
            BCA: BCE_2334(kamA)
            BCZ: BCZK2079(kamA)
            BCY: Bcer98_1688
            BTK: BT9727_2083(kamA)
            BLI: BL01430(kamA)
            BLD: BLi02294(kamA)
            BAY: RBAM_019520(kamA)
            BPU: BPUM_1892(kamA)
            STH: STH35
            CTC: CTC00890
            CDF: CD2252(kamA)
            AMT: Amet_2738 Amet_4552
            CHY: CHY_2479
            DSY: DSY4027
            SWO: Swol_1121
            CSC: Csac_0232
            TTE: TTE0723(kamA) TTE1204(kamA2)
            MTA: Moth_0457
            FNU: FN1866
            RBA: RB1214(kamA)
            LIL: LA2701 LB298
            LIC: LIC11303 LIC20230(kamA)
            LBJ: LBJ_2006(kamA) LBJ_4222(kamA)
            LBL: LBL_1044(kamA) LBL_4236(kamA)
            PGI: PG1070(kamA)
            SRU: SRU_1133
            PLT: Plut_1576
            DET: DET0628
            DEH: cbdb_A615(kamA)
            DEB: DehaBAV1_0133 DehaBAV1_0601
            DRA: DR_A0027
            DGE: Dgeo_0988
            AAE: aq_454
            TPT: Tpet_0803
            TME: Tmel_0192 Tmel_1010
            FNO: Fnod_0207
            MMP: MMP0861(kamA)
            MMZ: MmarC7_0106 MmarC7_1783
            MAE: Maeo_0240
            MVN: Mevan_1195 Mevan_1223
            MAC: MA3979
            MBA: Mbar_A0670
            MMA: MM_0934
            MBU: Mbur_0274
            IHO: Igni_1382
STRUCTURES  PDB: 2A5H  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.3.2
            ExPASy - ENZYME nomenclature database: 5.4.3.2
            ExplorEnz - The Enzyme Database: 5.4.3.2
            ERGO genome analysis and discovery system: 5.4.3.2
            BRENDA, the Enzyme Database: 5.4.3.2
            CAS: 9075-20-1
///
ENTRY       EC 5.4.3.3                  Enzyme
NAME        beta-lysine 5,6-aminomutase;
            beta-lysine mutase;
            L-beta-lysine 5,6-aminomutase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring amino groups
SYSNAME     (3S)-3,6-diaminohexanoate 5,6-aminomutase
REACTION    (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate [RN:R03275]
ALL_REAC    R03275
SUBSTRATE   (3S)-3,6-diaminohexanoate [CPD:C01142]
PRODUCT     (3S,5S)-3,5-diaminohexanoate [CPD:C01186]
COFACTOR    Cobamide coenzyme [CPD:C00194]
COMMENT     Requires a cobamide coenzyme.
REFERENCE   1
  AUTHORS   Retey, J., Kunz, F., Arigoni, D. and Stadtman, T.C.
  TITLE     Zur Kenntnis der beta-Lysin-Mutase-Reaktion: mechanismus und
            sterischer Verlauf.
  JOURNAL   Helv. Chim. Acta 61 (1978) 2989-2998.
  ORGANISM  Clostridium sticklandii
REFERENCE   2  [PMID:5649516]
  AUTHORS   Stadtman TC, Renz P.
  TITLE     Anaerobic degradation of lysine. V. Some properties of the cobamide
            coenzyme-dependent beta-lysine mutase of Clostridium sticklandii.
  JOURNAL   Arch. Biochem. Biophys. 125 (1968) 226-39.
  ORGANISM  Clostridium sticklandii
PATHWAY     PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K01844  beta-lysine 5,6-aminomutase
GENES       RFR: Rfer_3887 Rfer_3888
            STH: STH37 STH38
            TTE: TTE0726 TTE0727
            FNU: FN1862 FN1863
            PGI: PG1073(kamD) PG1074(kamE)
STRUCTURES  PDB: 1XRS  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.3.3
            ExPASy - ENZYME nomenclature database: 5.4.3.3
            ExplorEnz - The Enzyme Database: 5.4.3.3
            ERGO genome analysis and discovery system: 5.4.3.3
            BRENDA, the Enzyme Database: 5.4.3.3
            CAS: 9075-69-8
///
ENTRY       EC 5.4.3.4                  Enzyme
NAME        D-lysine 5,6-aminomutase;
            D-alpha-lysine mutase;
            adenosylcobalamin-dependent D-lysine 5,6-aminomutase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring amino groups
SYSNAME     D-2,6-diaminohexanoate 5,6-aminomutase
REACTION    D-lysine = 2,5-diaminohexanoate [RN:R02852]
ALL_REAC    R02852
SUBSTRATE   D-lysine [CPD:C00739]
PRODUCT     2,5-diaminohexanoate [CPD:C05161]
COFACTOR    Cobamide coenzyme [CPD:C00194]
COMMENT     Requires a cobamide coenzyme.
REFERENCE   1  [PMID:5480154]
  AUTHORS   Morley CG, Stadtman TC.
  TITLE     Studies on the fermentation of D-alpha-lysine. Purification and
            properties of an adenosine triphosphate regulated B
            12-coenzyme-dependent D-alpha-lysine mutase complex from Clostridium
            sticklandii.
  JOURNAL   Biochemistry. 9 (1970) 4890-900.
  ORGANISM  Clostridium sticklandii
REFERENCE   2  [PMID:4229021]
  AUTHORS   Stadtman TC, Tsai L.
  TITLE     A cobamide coenzyme dependent migration of the epsilon-amino group
            of D-lysine.
  JOURNAL   Biochem. Biophys. Res. Commun. 28 (1967) 920-6.
  ORGANISM  Clostridium sticklandii
PATHWAY     PATH: map00310  Lysine degradation
GENES       MXA: MXAN_4386(kamE) MXAN_4388(kamD)
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.3.4
            ExPASy - ENZYME nomenclature database: 5.4.3.4
            ExplorEnz - The Enzyme Database: 5.4.3.4
            ERGO genome analysis and discovery system: 5.4.3.4
            BRENDA, the Enzyme Database: 5.4.3.4
            CAS: 9075-70-1
///
ENTRY       EC 5.4.3.5                  Enzyme
NAME        D-ornithine 4,5-aminomutase;
            D-alpha-ornithine 5,4-aminomutase;
            D-ornithine aminomutase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring amino groups
SYSNAME     D-ornithine 4,5-aminomutase
REACTION    D-ornithine = (2R,4S)-2,4-diaminopentanoate [RN:R02461]
ALL_REAC    R02461
SUBSTRATE   D-ornithine [CPD:C00515]
PRODUCT     (2R,4S)-2,4-diaminopentanoate [CPD:C03943]
COFACTOR    Pyridoxal phosphate [CPD:C00018];
            Cobamide coenzyme [CPD:C00194];
            Dithiothreitol [CPD:C00265]
COMMENT     A pyridoxal-phosphate protein that requires a cobamide coenzyme for
            activity.
REFERENCE   1  [PMID:4711468]
  AUTHORS   Somack R, Costilow RN.
  TITLE     Purification and properties of a pyridoxal phosphate and coenzyme B
            12  dependent D- -ornithine 5,4-aminomutase.
  JOURNAL   Biochemistry. 12 (1973) 2597-604.
  ORGANISM  Clostridium sticklandii
PATHWAY     PATH: map00472  D-Arginine and D-ornithine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.3.5
            ExPASy - ENZYME nomenclature database: 5.4.3.5
            ExplorEnz - The Enzyme Database: 5.4.3.5
            ERGO genome analysis and discovery system: 5.4.3.5
            BRENDA, the Enzyme Database: 5.4.3.5
            CAS: 62213-30-3
///
ENTRY       EC 5.4.3.6                  Enzyme
NAME        tyrosine 2,3-aminomutase;
            tyrosine alpha,beta-mutase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring amino groups
SYSNAME     L-tyrosine 2,3-aminomutase
REACTION    L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate [RN:R00739]
ALL_REAC    R00739
SUBSTRATE   L-tyrosine [CPD:C00082]
PRODUCT     3-amino-3-(4-hydroxyphenyl)propanoate [CPD:C04368]
COFACTOR    ATP [CPD:C00002]
COMMENT     Requires ATP.
REFERENCE   1  [PMID:5021987]
  AUTHORS   Kurylo-Borowska Z, Abramsky T.
  TITLE     Biosynthesis of  -tyrosine.
  JOURNAL   Biochim. Biophys. Acta. 264 (1972) 1-10.
  ORGANISM  Bacillus brevis
PATHWAY     PATH: map00350  Tyrosine metabolism
STRUCTURES  PDB: 2OHY  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.3.6
            ExPASy - ENZYME nomenclature database: 5.4.3.6
            ExplorEnz - The Enzyme Database: 5.4.3.6
            ERGO genome analysis and discovery system: 5.4.3.6
            BRENDA, the Enzyme Database: 5.4.3.6
            CAS: 9073-38-5
///
ENTRY       EC 5.4.3.7                  Enzyme
NAME        leucine 2,3-aminomutase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring amino groups
SYSNAME     (2S)-alpha-leucine 2,3-aminomutase
REACTION    (2S)-alpha-leucine = (3R)-beta-leucine [RN:R01091]
ALL_REAC    R01091
SUBSTRATE   (2S)-alpha-leucine [CPD:C00123]
PRODUCT     (3R)-beta-leucine [CPD:C02486]
COFACTOR    Cobamide coenzyme [CPD:C00194]
COMMENT     Requires a cobamide coenzyme.
REFERENCE   1
  AUTHORS   Freer, I., Pedrocchi-Fantoni, G., Picken, D.J. and Overton, K.H.
  TITLE     Stereochemistry of the leucine 2,3-aminomutase from tissue-cultures
            of Andrographis paniculata.
  JOURNAL   J. Chem. Soc. Chem. Commun. (1981) 80-82.
  ORGANISM  Andrographis paniculata
REFERENCE   2  [PMID:1270414]
  AUTHORS   Poston JM.
  TITLE     Leucine 2,3-aminomutase, an enzyme of leucine catabolism.
  JOURNAL   J. Biol. Chem. 251 (1976) 1859-63.
  ORGANISM  Clostridium sporogenes
REFERENCE   3
  AUTHORS   Poston, J.M.
  TITLE     Coenzyme B12-dependent enzymes in potatoes: leucine 2,3-aminomutase
            and methylmalonyl-CoA mutase.
  JOURNAL   Phytochemistry 17 (1976) 401-402.
  ORGANISM  Solanum tuberosum [GN:estu]
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.3.7
            ExPASy - ENZYME nomenclature database: 5.4.3.7
            ExplorEnz - The Enzyme Database: 5.4.3.7
            ERGO genome analysis and discovery system: 5.4.3.7
            BRENDA, the Enzyme Database: 5.4.3.7
            CAS: 59125-53-0
///
ENTRY       EC 5.4.3.8                  Enzyme
NAME        glutamate-1-semialdehyde 2,1-aminomutase;
            glutamate-1-semialdehyde aminotransferase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring amino groups
SYSNAME     (S)-4-amino-5-oxopentanoate 4,5-aminomutase
REACTION    L-glutamate 1-semialdehyde = 5-aminolevulinate [RN:R02272]
ALL_REAC    R02272
SUBSTRATE   L-glutamate 1-semialdehyde [CPD:C03741]
PRODUCT     5-aminolevulinate [CPD:C00430]
COFACTOR    Pyridoxal phosphate [CPD:C00018]
COMMENT     Requires pyridoxal phosphate.
REFERENCE   1
  AUTHORS   Gough, S.P. and Kannangara, C.G.
  TITLE     Biosynthesis of delta-aminolevulinate in greening barley leaves:
            glutamate 1-semialdehyde aminotransferase.
  JOURNAL   Carlsberg Res. Commun. 43 (1978) 185-194.
  ORGANISM  Hordeum vulgare [GN:ehvu]
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K01845  glutamate-1-semialdehyde 2,1-aminomutase
GENES       ATH: AT3G48730(GSA2) AT5G63570(GSA1)
            OSA: 4346136
            CME: CMP285C
            SPO: SPCC417.11c
            AOR: AO090020000375
            CNE: CNF01050
            ECO: b0154(hemL)
            ECJ: JW0150(hemL)
            ECE: Z0165(hemL)
            ECS: ECs0158
            ECC: c0189(hemL)
            ECI: UTI89_C0170(hemL)
            ECP: ECP_0164
            ECV: APECO1_1831(hemL)
            ECW: EcE24377A_0159(hemL)
            ECX: EcHS_A0158(hemL)
            STY: STY0223(hemL)
            STT: t0203(hemL)
            SPT: SPA0208(hemL)
            SEC: SC0202(hemL)
            STM: STM0202(hemL)
            YPE: YPO3389(hemL)
            YPK: y0799(hemL)
            YPM: YP_0296(hemL)
            YPA: YPA_2889
            YPN: YPN_0701
            YPP: YPDSF_2968
            YPS: YPTB0742(hemL)
            YPI: YpsIP31758_3330(hemL)
            YEN: YE0734(gsa)
            SFL: SF0146(hemL)
            SFX: S0149(hemL)
            SFV: SFV_0139(hemL)
            SSN: SSON_0166(hemL)
            SBO: SBO_0143(hemL)
            SDY: SDY_0170(hemL)
            ECA: ECA3307(hemL)
            PLU: plu0902(hemL)
            WBR: WGLp073(hemL)
            SGL: SG0500
            ENT: Ent638_0694
            KPN: KPN_00169(hemL)
            SPE: Spro_1850
            HSO: HS_1229(hemL)
            PMU: PM0462(hemL)
            MSU: MS0910(hemL)
            APL: APL_1555(hemL)
            XFA: XF2302
            XFT: PD1335(hemL)
            XCC: XCC3272(hemL)
            XCB: XC_0892
            XCV: XCV3535(hemL) XCV4348(hemL)
            XAC: XAC3420(hemL) XAC4241(hemL) XAC4242(hemL)
            XOO: XOO1232(hemL)
            XOM: XOO_1128(XOO1128)
            VCH: VC0626
            VCO: VC0395_A0154(hemL)
            VVU: VV1_1678
            VVY: VV2728
            VPA: VP2475
            VFI: VF2135
            PPR: PBPRA0529(hemL)
            PAE: PA3977(hemL) PA4088 PA5523
            PAU: PA14_12390(hemL) PA14_72870
            PAP: PSPA7_1131(hemL)
            PPU: PP_4784(hemL)
            PST: PSPTO_4800(hemL)
            PSB: Psyr_4342
            PSP: PSPPH_2738 PSPPH_2771 PSPPH_4384(hemL)
            PFL: PFL_3222 PFL_5429(hemL)
            PFO: Pfl_4947
            PEN: PSEEN4804(hemL)
            PMY: Pmen_3774
            PAR: Psyc_0161(hemL)
            PCR: Pcryo_0171
            ACI: ACIAD1201(hemL)
            SON: SO_1300(hemL)
            SDN: Sden_2819
            SFR: Sfri_2980
            SAZ: Sama_0839
            SBL: Sbal_1159
            SLO: Shew_1012
            SPC: Sputcn32_1119
            SSE: Ssed_2453
            SPL: Spea_1955
            SHE: Shewmr4_2893
            SHM: Shewmr7_2975
            SHN: Shewana3_3071
            SHW: Sputw3181_3045
            ILO: IL2245(hemL)
            CPS: CPS_3593 CPS_4629(hemL)
            PHA: PSHAa2255(hemL)
            PAT: Patl_0495
            SDE: Sde_0827
            PIN: Ping_0865
            MAQ: Maqu_0686
            CBU: CBU_1882(hemL)
            CBD: COXBU7E912_0113(hemL)
            LPN: lpg1534(hemL)
            LPF: lpl1492(hemL)
            LPP: lpp1491(hemL)
            MCA: MCA0054(hemL)
            FTU: FTT0927(hemL)
            FTF: FTF0927(hemL)
            FTW: FTW_0820(hemL)
            FTL: FTL_1283
            FTH: FTH_1255(hemL)
            FTA: FTA_1356(hemL)
            FTN: FTN_0805(hemL)
            TCX: Tcr_1570
            NOC: Noc_0600
            AEH: Mlg_0806
            HCH: HCH_06248(hemL)
            CSA: Csal_3304
            ABO: ABO_0354(hemL)
            MMW: Mmwyl1_3240
            AHA: AHA_3520(hemL)
            DNO: DNO_1024(hemL)
            RMA: Rmag_0222
            VOK: COSY_0216(hemL)
            NME: NMB1864
            NMA: NMA0592(hemL)
            NMC: NMC0354(hemL)
            NGO: NGO0040
            CVI: CV_0067(hemL) CV_2819
            RSO: RSc0666(hemL)
            REU: Reut_A2625
            REH: H16_A0734(hemL)
            RME: Rmet_0667
            BMA: BMA2142(hemL) BMAA1966
            BMV: BMASAVP1_A0768(hemL)
            BML: BMA10299_A2601(hemL)
            BMN: BMA10247_2012(hemL)
            BXE: Bxe_A0896
            BUR: Bcep18194_A4065 Bcep18194_B0060 Bcep18194_C6794
            BCN: Bcen_0482 Bcen_5548
            BCH: Bcen2424_0961 Bcen2424_5913
            BAM: Bamb_0822
            BPS: BPSL2623(hemL) BPSS2171
            BPM: BURPS1710b_3099(hemL) BURPS1710b_A1290
            BPL: BURPS1106A_3064(hemL)
            BPD: BURPS668_3011(hemL)
            BTE: BTH_I1543(hemL) BTH_II2249
            BPE: BP0315(hemL)
            BPA: BPP3936(hemL)
            BBR: BB4409(hemL)
            RFR: Rfer_1369
            POL: Bpro_1133
            MPT: Mpe_A3193
            HAR: HEAR1123 HEAR2750(hemL)
            MMS: mma_2959(hemL)
            NEU: NE1423(hemL)
            NET: Neut_1537
            NMU: Nmul_A2629
            EBA: ebA1743(hemL)
            AZO: azo3449(hemL)
            DAR: Daro_3902
            TBD: Tbd_2557
            MFA: Mfla_2664
            HPY: HP0306
            HPJ: jhp0291(hemL)
            HPA: HPAG1_0308
            HHE: HH0964(hemL)
            HAC: Hac_1022(hemL)
            WSU: WS1886(hemL)
            TDN: Tmden_1109
            CJE: Cj0853c(hemL)
            CJR: CJE0940(hemL)
            CJJ: CJJ81176_0869(hemL)
            CJU: C8J_0800(hemL)
            CJD: JJD26997_1002(hemL)
            CFF: CFF8240_1176(hemL)
            CCV: CCV52592_0797(hemL)
            CHA: CHAB381_1034(hemL)
            CCO: CCC13826_0834(hemL) CCC13826_1085
            ABU: Abu_1006(hemL)
            NIS: NIS_0721(hemL)
            SUN: SUN_1254(hemL)
            GSU: GSU0337(hemL)
            GME: Gmet_3356
            PCA: Pcar_0266
            DVU: DVU3168(hemL)
            DDE: Dde_3180
            LIP: LI0906(hemL)
            BBA: Bd3449(hemL)
            DPS: DP0812
            ADE: Adeh_4344
            MXA: MXAN_0395(hemL)
            SAT: SYN_00583
            SFU: Sfum_1608
            MLO: mll5149
            SME: SMa0956(atrB)
            ATU: Atu5124(atrB)
            ATC: AGR_pAT_182(atrB)
            RLE: RL4477(hemL)
            BME: BMEII0192
            BMF: BAB2_1066
            BMS: BRA1108
            BMB: BruAb2_1047
            BJA: blr3552
            BRA: BRADO5694
            BBT: BBta_1045 BBta_6209
            RPD: RPD_2366
            NWI: Nwi_0698 Nwi_2388
            CCR: CC_3139
            SIL: SPO1597(hemL) SPOA0312
            RSP: RSP_1569
            HNE: HNE_2418(hemL)
            NAR: Saro_0248
            MGM: Mmc1_0093
            ABA: Acid345_1537 Acid345_4548
            BSU: BG10345(hemL) BG11943(gsaB)
            BHA: BH0943(gsaB) BH2941 BH3043(hemL)
            BAN: BA0531(hemL-1) BA4693(hemL-2)
            BAR: GBAA0531(hemL-1) GBAA4693(hemL-2)
            BAA: BA_1102 BA_5132
            BAT: BAS0499 BAS4358
            BCE: BC0512 BC4468
            BCA: BCE_0586(hemL) BCE_4552(hemL)
            BCZ: BCZK0438(gsaB) BCZK4205(hemL)
            BTK: BT9727_0442(gsaB) BT9727_4194(hemL)
            BTL: BALH_0464(hemL) BALH_4054(hemL)
            BLI: BL00628(hemL) BL03060(gsaB)
            BLD: BLi00898(gsaB) BLi02942(hemL)
            BCL: ABC1318(gsaB) ABC2627(hemL)
            BAY: RBAM_008800(gsaB) RBAM_025180(hemL)
            BPU: BPUM_0825(gsaB) BPUM_2453(hemL)
            OIH: OB0901 OB2065(hemL)
            GKA: GK0471 GK2642
            SAU: SA1491(hemL) SA1681(gsaB)
            SAV: SAV1667(hemL) SAV1864(gsaB)
            SAM: MW1611(hemL) MW1804(gsaB)
            SAR: SAR1747(hemL) SAR1954
            SAS: SAS1596 SAS1786
            SAC: SACOL1714(hemL1) SACOL1922(hemL2)
            SAB: SAB1527c(hemL) SAB1797
            SAA: SAUSA300_1614(hemL) SAUSA300_1845(hemL)
            SAO: SAOUHSC_01771 SAOUHSC_02000
            SEP: SE1342 SE1548
            SER: SERP1231(hemL-1) SERP1401(hemL-2)
            SHA: SH1097(gsaB) SH1260(hemL)
            SSP: SSP0929 SSP1097
            LMO: lmo1553(hemL) lmo1685(gsaB)
            LMF: LMOf2365_1574(hemL) LMOf2365_1709(gsaB)
            LIN: lin1588(hemL) lin1793(gsaB)
            LWE: lwe1566(hemL) lwe1703(gsaB)
            SSA: SSA_0488
            STH: STH2790
            CAC: CAC0099(hemL)
            CPE: CPE1432(hemL)
            CPF: CPF_1685(hemL)
            CPR: CPR_1419(hemL)
            CTC: CTC00730
            CNO: NT01CX_0259(hemL)
            CKL: CKL_0658(hemL)
            CHY: CHY_1212(hemL)
            DSY: DSY2219
            SWO: Swol_0203 Swol_0694
            CSC: Csac_0948
            MTA: Moth_1244
            MTU: Rv0524(hemL)
            MTC: MT0546(hemL)
            MBO: Mb0537(hemL)
            MBB: BCG_0567(hemL)
            MLE: ML2414(hemL)
            MPA: MAP4020(hemL)
            MAV: MAV_4621(hemL)
            MSM: MSMEG_0661 MSMEG_0969(hemL) MSMEG_5970
            MMC: Mmcs_0690
            CGL: NCgl0422(cgl0437)
            CGB: cg0518(hemL)
            CEF: CE0460
            CDI: DIP0409(hemL)
            CJK: jk1895(hemL)
            NFA: nfa51600(hemL)
            RHA: RHA1_ro02037(hemL) RHA1_ro05728
            SCO: SCO4469(hemL)
            SMA: SAV4795(hemL)
            TWH: TWT729(hemL)
            TWS: TW743(hemL)
            LXX: Lxx01130(hemL)
            CMI: CMM_0599(hemL)
            AAU: AAur_2747(hemL)
            PAC: PPA0301
            TFU: Tfu_2726
            FRA: Francci3_0507 Francci3_3778
            FAL: FRAAL0997(hemL) FRAAL6024
            ACE: Acel_0231
            SEN: SACE_6935(hemL)
            RXY: Rxyl_1975
            FNU: FN0540
            RBA: RB6831(hemL)
            CTR: CT210(hemL)
            CTA: CTA_0230(hemL)
            CMU: TC0482
            CPN: CPn0138(hemL)
            CPA: CP0634
            CPJ: CPj0138(hemL)
            CPT: CpB0139
            CCA: CCA00629(hemL)
            CAB: CAB603(hemL)
            CFE: CF0374(gsa)
            PCU: pc1748(hemL)
            LIL: LB013(hemL)
            LIC: LIC20011(hemL)
            LBJ: LBJ_4011(hemL)
            LBL: LBL_4011(hemL)
            SYN: sll0017(hemL)
            SYW: SYNW1809(hemL)
            SYC: syc0881_c(hemL)
            SYF: Synpcc7942_0645
            SYD: Syncc9605_0659
            SYE: Syncc9902_1701
            SYG: sync_2058(hemL)
            SYR: SynRCC307_1648(hemL)
            SYX: SynWH7803_1821(hemL)
            CYA: CYA_2386(hemL)
            CYB: CYB_1012(hemL)
            TEL: tlr0479(hemL)
            GVI: glr0071(hemL)
            ANA: alr3265(hemL)
            AVA: Ava_4109 Ava_4834 Ava_4920
            PMA: Pro0482(hemL)
            PMM: PMM0483(hemL)
            PMT: PMT1296(hemL)
            PMN: PMN2A_1816
            PMI: PMT9312_0484
            PMB: A9601_05391(hemL)
            PMC: P9515_05471(hemL)
            PMF: P9303_06961(hemL)
            PMG: P9301_05101(hemL)
            PMH: P9215_05651(hemL)
            PME: NATL1_05401(hemL)
            TER: Tery_2741
            SRU: SRU_1740(hemL)
            CHU: CHU_0936(hemL)
            GFO: GFO_0240(hemL)
            FPS: FP1204(hemL)
            CTE: CT2099(hemL)
            CCH: Cag_1968
            PLT: Plut_2038
            DRA: DR_0555
            DGE: Dgeo_1942
            TTH: TTC0564
            TTJ: TTHA0934
            AAE: aq_816(gsa)
            MMP: MMP0224(hemL)
            MAE: Maeo_0518
            MVN: Mevan_1239
            MAC: MA0581(hemL)
            MBA: Mbar_A1464
            MMA: MM_1743
            MBU: Mbur_1227
            MHU: Mhun_2560
            MST: Msp_1180(hemL)
            MSI: Msm_1233
            MKA: MK0280(hemL)
            HAL: VNG2326G(hemL)
            HMA: rrnAC2628(hemL)
            HWA: HQ3447A(hemL)
            NPH: NP1246A(hemL)
            TAC: Ta0571
            TVO: TVN0635
            PTO: PTO0248
            RCI: RCIX913(hemL)
            APE: APE_2130.1 APE_2299.1
            HBU: Hbut_0837 Hbut_1430
            SSO: SSO0182(hemL)
            STO: ST0215
            SAI: Saci_0779(hemL)
            PAI: PAE0594(hemL)
STRUCTURES  PDB: 2CFB  2E7U  2EPJ  2GSA  2HOY  2HOZ  2HP1  2HP2  3GSB  4GSA  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.3.8
            ExPASy - ENZYME nomenclature database: 5.4.3.8
            ExplorEnz - The Enzyme Database: 5.4.3.8
            ERGO genome analysis and discovery system: 5.4.3.8
            BRENDA, the Enzyme Database: 5.4.3.8
            CAS: 68518-07-0
///
ENTRY       EC 5.4.4.1                  Enzyme
NAME        (hydroxyamino)benzene mutase;
            HAB mutase;
            hydroxylaminobenzene hydroxymutase;
            hydroxylaminobenzene mutase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring hydroxy groups
SYSNAME     (hydroxyamino)benzene hydroxymutase
REACTION    (hydroxyamino)benzene = 2-aminophenol [RN:R05383]
ALL_REAC    R05383
SUBSTRATE   (hydroxyamino)benzene [CPD:C02720]
PRODUCT     2-aminophenol [CPD:C01987]
REFERENCE   1  [PMID:10672020]
  AUTHORS   He Z, Nadeau LJ, Spain JC.
  TITLE     Characterization of hydroxylaminobenzene mutase from pNBZ139 cloned
            from Pseudomonas pseudoalcaligenes JS45. A highly associated
            SDS-stable enzyme catalyzing an intramolecular transfer of hydroxy
            groups.
  JOURNAL   Eur. J. Biochem. 267 (2000) 1110-6.
  ORGANISM  Pseudomonas pseudoalcaligenes
REFERENCE   2  [PMID:10877793]
  AUTHORS   Davis JK, Paoli GC, He Z, Nadeau LJ, Somerville CC, Spain JC.
  TITLE     Sequence analysis and initial characterization of two isozymes of
            hydroxylaminobenzene mutase from Pseudomonas pseudoalcaligenes JS45.
  JOURNAL   Appl. Environ. Microbiol. 66 (2000) 2965-71.
  ORGANISM  Pseudomonas pseudoalcaligenes
PATHWAY     PATH: map00626  Naphthalene and anthracene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.4.1
            ExPASy - ENZYME nomenclature database: 5.4.4.1
            ExplorEnz - The Enzyme Database: 5.4.4.1
            ERGO genome analysis and discovery system: 5.4.4.1
            BRENDA, the Enzyme Database: 5.4.4.1
///
ENTRY       EC 5.4.4.2                  Enzyme
NAME        isochorismate synthase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring hydroxy groups
SYSNAME     isochorismate hydroxymutase
REACTION    chorismate = isochorismate [RN:R01717]
ALL_REAC    R01717
SUBSTRATE   chorismate [CPD:C00251]
PRODUCT     isochorismate [CPD:C00885]
COMMENT     Requires Mg2+. The reaction is reversible.
REFERENCE   1  [PMID:4306838]
  AUTHORS   Young IG, Gibson F.
  TITLE     Regulation of the enzymes involved in the biosynthesis of
            2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia
            coli.
  JOURNAL   Biochim. Biophys. Acta. 177 (1969) 401-11.
  ORGANISM  Aerobacter aerogenes, Escherichia coli [GN:eco]
REFERENCE   2  [PMID:9952467]
  AUTHORS   van Tegelen LJ, Moreno PR, Croes AF, Verpoorte R, Wullems GJ.
  TITLE     Purification and cDNA cloning of isochorismate synthase from
            elicited cell cultures of Catharanthus roseus.
  JOURNAL   Plant. Physiol. 119 (1999) 705-12.
  ORGANISM  Catharanthus roseus
REFERENCE   3  [PMID:9795253]
  AUTHORS   Dahm C, Muller R, Schulte G, Schmidt K, Leistner E.
  TITLE     The role of isochorismate hydroxymutase genes entC and menF in
            enterobactin and menaquinone biosynthesis in Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta. 1425 (1998) 377-86.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00130  Ubiquinone biosynthesis
            PATH: map01053  Biosynthesis of siderophore group nonribosomal
                            peptides
ORTHOLOGY   KO: K01851  isochorismate synthase
            KO: K02361  isochorismate synthase
            KO: K02552  menaquinone-specific isochorismate synthase
GENES       OSA: 4346852
            ECO: b0593(entC) b2265(menF)
            ECJ: JW0585(entC) JW2260(menF)
            ECE: Z0735(entC) Z3525(menF)
            ECS: ECs0632 ECs3153
            ECC: c0680(entC) c2809(menF)
            ECI: UTI89_C0595(entC) UTI89_C2549(menF)
            ECP: ECP_0625 ECP_2309
            ECV: APECO1_1456(entC) APECO1_4296(menF)
            ECW: EcE24377A_0613(entC) EcE24377A_2562(menF)
            ECX: EcHS_A0644(entC) EcHS_A2411
            STY: STY0639(entC) STY2541(menF)
            STT: t0553(menF) t2273(entC)
            SPT: SPA0553(menF) SPA2139(entC)
            SEC: SC0626(entC) SC2310(menF)
            STM: STM0595(entC) STM2310(menF)
            YPE: YPO2528(menF)
            YPK: y1659(menF)
            YPM: YP_2339(menF)
            YPA: YPA_2020
            YPN: YPN_2123
            YPS: YPTB2561(menF)
            YPI: YpsIP31758_1481(menF)
            SFL: SF2344(menF)
            SFX: S2478(menF)
            SFV: SFV_2336(menF)
            SSN: SSON_0544(entC) SSON_2326(menF)
            SBO: SBO_0454(entC) SBO_2302(menF)
            SDY: SDY_0524(entC) SDY_2461(menF)
            ECA: ECA0477(entC) ECA1210(menF)
            PLU: plu3074(menF)
            ENT: Ent638_2815
            HIN: HI0285(menF)
            HIT: NTHI0393(menF)
            HDU: HD0621(menF)
            HSO: HS_0618(menF)
            PMU: PM0053(menF)
            MSU: MS1795(menF)
            APL: APL_1042(menF)
            VCH: VC0773 VC1976
            VCO: VC0395_A0302(vibC) VC0395_A1562(menF)
            VVU: VV1_3173 VV2_0835
            VVY: VV1115 VVA1300
            VPA: VP0928
            VFI: VF1672
            PPR: PBPRA2625 PBPRB1824
            PAE: PA4231(pchA)
            PAU: PA14_09210(pchA)
            PST: PSPTO_2595(pchA)
            PSP: PSPPH_2904(pchA)
            PFL: PFL_3488(pchA)
            PEN: PSEEN2504(pmsC)
            ACI: ACIAD2776(entC)
            SON: SO_4713
            SFR: Sfri_3913
            SHE: Shewmr4_3868
            SHM: Shewmr7_3961
            SHN: Shewana3_4071
            SDE: Sde_3400
            HCH: HCH_06563
            AHA: AHA_0532(menF) AHA_2479
            CVI: CV_1485(entC)
            BUR: Bcep18194_B0667
            BCN: Bcen_3364
            BCH: Bcen2424_5003
            BAM: Bamb_1690
            BPS: BPSS0581(pchA)
            BPM: BURPS1710b_A2145(pchA)
            BPL: BURPS1106A_A0781(pchA)
            BPD: BURPS668_A0871(pchA)
            BTE: BTH_II1833
            DAR: Daro_2823
            BBA: Bd3485(menF)
            DPS: DP0254(menF)
            MXA: MXAN_3527 MXAN_3646
            BME: BMEII0077
            BMF: BAB2_0015
            BMS: BRA0016(entC)
            BMB: BruAb2_0016(entC)
            BOV: BOV_A0013(entC)
            BSU: BG10682(menF) BG11242(dhbC)
            BAN: BA2369(dhbC) BA5112(menF)
            BAR: GBAA2369(dhbC) GBAA5112(menF)
            BAA: BA_2863 BA_5530
            BAT: BAS2205 BAS4751
            BCE: BC2303 BC4856
            BCA: BCE_2399(dhbC) BCE_5016(menF)
            BCZ: BCZK2128(entC) BCZK4611(menF)
            BTK: BT9727_2144(entC) BT9727_4589(menF)
            BTL: BALH_2108(entC) BALH_4422(menF)
            BLI: BL02409(menF) BL04021(dhbC)
            BLD: BLi03223(menF) BLi03901(dhbC)
            BPU: BPUM_2719
            OIH: OB0955(dhbC) OB2326(menF)
            GKA: GK2876
            SAU: SA0895
            SAV: SAV1042
            SAM: MW0926
            SAR: SAR1016
            SAS: SAS0978
            SAC: SACOL1051
            SAB: SAB0909
            SAA: SAUSA300_0945
            SAO: SAOUHSC_00982
            SEP: SE0743
            SER: SERP0629
            SHA: SH1920
            SSP: SSP1749
            LMO: lmo1676(menF)
            LMF: LMOf2365_1700
            LIN: lin1784(menF)
            LWE: lwe1694
            LLA: L0168(menF)
            LLC: LACR_0774
            LLM: llmg_1828(menF)
            EFA: EF0447
            DSY: DSY0517(menF)
            MTU: Rv3215(entC)
            MTC: MT3311
            MBO: Mb3241(entC)
            MBB: BCG_3242(entC_1) BCG_3335(entC_2)
            MLE: ML0808(entC)
            MPA: MAP3316(entC)
            MAV: MAV_4163
            MSM: MSMEG_1925
            MMC: Mmcs_1387
            CGL: NCgl1243(cgl1292)
            CGB: cg1462(entC)
            CEF: CE1388
            CDI: DIP1114
            CJK: jk1285(menF)
            NFA: nfa54680
            RHA: RHA1_ro04795(dhbC) RHA1_ro05194
            TWH: TWT052(menF)
            TWS: TW062
            LXX: Lxx01810(menF)
            CMI: CMM_2810(menF)
            PAC: PPA0904 PPA1940
            TFU: Tfu_1413 Tfu_1872
            SEN: SACE_3854(dhbC) SACE_6911(menF)
            RXY: Rxyl_2897
            PCU: pc1069(menF)
            SYN: slr0817(menF)
            SYW: SYNW2308(menF)
            SYC: syc1908_d(menF)
            SYF: Synpcc7942_2188
            SYD: Syncc9605_2439
            SYE: Syncc9902_2120
            SYG: sync_2656
            SYR: SynRCC307_2252(menF)
            SYX: SynWH7803_2319(menF)
            CYA: CYA_2455
            CYB: CYB_2299
            TEL: tll1213
            ANA: all0032
            AVA: Ava_2632
            PMA: Pro0202(menF)
            PMM: PMM0177(menF)
            PMT: PMT2060(menF)
            PMN: PMN2A_1545
            PMI: PMT9312_0179
            PMB: A9601_01951(menF)
            PMC: P9515_02061(menF)
            PMF: P9303_27351(menF)
            PMG: P9301_01971(menF)
            PME: NATL1_02521(menF)
            TER: Tery_4072
            BTH: BT_4700(entC)
            BFR: BF1315(entC)
            BFS: BF1300
            PGI: PG1525
            SRU: SRU_1350
            CHU: CHU_1758(entC)
            GFO: GFO_2076
            FPS: FP0658(menF)
            CTE: CT1838(menF)
            CCH: Cag_1701
            PLT: Plut_0332
            RCA: Rcas_4216
            HAL: VNG1083G(menF)
            HMA: rrnAC0837(menF)
            HWA: HQ1872A(menF)
            NPH: NP2724A(menF)
STRUCTURES  PDB: 2EUA  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.4.2
            ExPASy - ENZYME nomenclature database: 5.4.4.2
            ExplorEnz - The Enzyme Database: 5.4.4.2
            ERGO genome analysis and discovery system: 5.4.4.2
            BRENDA, the Enzyme Database: 5.4.4.2
            CAS: 37318-53-9
///
ENTRY       EC 5.4.4.3                  Enzyme
NAME        3-(hydroxyamino)phenol mutase;
            3-hydroxylaminophenol mutase;
            3HAP mutase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring hydroxy groups
SYSNAME     3-(hydroxyamino)phenol hydroxymutase
REACTION    3-hydroxyaminophenol = aminohydroquinone [RN:R06988]
ALL_REAC    R06988
SUBSTRATE   3-hydroxyaminophenol [CPD:C14602]
PRODUCT     aminohydroquinone [CPD:C14604]
REFERENCE   1  [PMID:10049374]
  AUTHORS   Schenzle A, Lenke H, Spain JC, Knackmuss HJ.
  TITLE     3-Hydroxylaminophenol mutase from Ralstonia eutropha JMP134
            catalyzes a Bamberger rearrangement.
  JOURNAL   J. Bacteriol. 181 (1999) 1444-50.
  ORGANISM  Ralstonia eutropha
ORTHOLOGY   KO: K07815  3-(hydroxyamino)phenol mutase
GENES       RSO: RSc1258(glnA1)
            REU: Reut_A2057
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.4.3
            ExPASy - ENZYME nomenclature database: 5.4.4.3
            ExplorEnz - The Enzyme Database: 5.4.4.3
            ERGO genome analysis and discovery system: 5.4.4.3
            BRENDA, the Enzyme Database: 5.4.4.3
///
ENTRY       EC 5.4.4.-                  Enzyme
CLASS       Isomerases;
            Intramolecular transferases (mutases);
            Transferring hydroxy groups
REACTION    (1) 12(S)-HPETE <=> Hepoxilin A3 [RN:R07039];
            (2) 12(S)-HPETE <=> Hepoxilin B3 [RN:R07040]
SUBSTRATE   12(S)-HPETE [CPD:C05965]
PRODUCT     Hepoxilin A3 [CPD:C14808];
            Hepoxilin B3 [CPD:C14810]
///
ENTRY       EC 5.4.99.1                 Enzyme
NAME        methylaspartate mutase;
            glutamate mutase;
            glutamic mutase;
            glutamic isomerase;
            glutamic acid mutase;
            glutamic acid isomerase;
            methylaspartic acid mutase;
            beta-methylaspartate-glutamate mutase;
            glutamate isomerase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
SYSNAME     L-threo-3-methylaspartate carboxy-aminomethylmutase
REACTION    L-threo-3-methylaspartate = L-glutamate [RN:R00262]
ALL_REAC    R00262
SUBSTRATE   L-threo-3-methylaspartate [CPD:C03618]
PRODUCT     L-glutamate [CPD:C00025]
COFACTOR    Cobamide coenzyme [CPD:C00194]
COMMENT     Requires a cobamide coenzyme.
REFERENCE   1  [PMID:14245371]
  AUTHORS   BARKER HA, ROOZE V, SUZUKI F, IODICE AA.
  TITLE     THE GLUTAMATE MUTASE SYSTEM. ASSAYS AND PROPERTIES.
  JOURNAL   J. Biol. Chem. 239 (1964) 3260-6.
  ORGANISM  Clostridium tetanomorphum
REFERENCE   2
  AUTHORS   Weissbach, H., Toohey, J. and Barker, H.A.
  TITLE     Isolation and properties of B12 coenzymes containing benzimidazole
            or dimethylbenzimidazole.
  JOURNAL   Proc. Natl. Acad. Sci. USA 45 (1959) 521-528.
  ORGANISM  Clostridium tetanomorphum
PATHWAY     PATH: map00660  C5-Branched dibasic acid metabolism
ORTHOLOGY   KO: K01846  methylaspartate mutase
GENES       ECE: Z0895
            ECS: ECs0764
            YEN: YE4042(mutE)
            SDY: SDY_0676
            SUN: SUN_1085 SUN_1086
            CTC: CTC02568(mutS)
            CKL: CKL_0302(mutE)
            AMT: Amet_3416
            CHY: CHY_0307(mamA) CHY_0309(mutE)
            DSY: DSY3234 DSY3235 DSY3236
            DRM: Dred_2692
            TTE: TTE1239
            PAC: PPA2281
            FNU: FN1853 FN1854 FN1855
            TDE: TDE1023(mamA) TDE2236(glmE)
            HAL: VNG2286G(mamA)
            HMA: rrnAC0684(mamA1) rrnAC0984(mamA2)
STRUCTURES  PDB: 1B1A  1BE1  1CB7  1CCW  1FMF  1I9C  1ID8  2PWH  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.1
            ExPASy - ENZYME nomenclature database: 5.4.99.1
            ExplorEnz - The Enzyme Database: 5.4.99.1
            ERGO genome analysis and discovery system: 5.4.99.1
            BRENDA, the Enzyme Database: 5.4.99.1
            CAS: 9032-97-7
///
ENTRY       EC 5.4.99.2                 Enzyme
NAME        methylmalonyl-CoA mutase;
            methylmalonyl-CoA CoA-carbonyl mutase;
            methylmalonyl coenzyme A mutase;
            methylmalonyl coenzyme A carbonylmutase;
            (S)-methylmalonyl-CoA mutase;
            (R)-2-methyl-3-oxopropanoyl-CoA CoA-carbonylmutase [incorrect]
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
SYSNAME     (R)-methylmalonyl-CoA CoA-carbonylmutase
REACTION    (R)-methylmalonyl-CoA = succinyl-CoA [RN:R00833]
ALL_REAC    R00833
SUBSTRATE   (R)-methylmalonyl-CoA [CPD:C01213]
PRODUCT     succinyl-CoA [CPD:C00091]
COFACTOR    Cobamide [CPD:C00210]
COMMENT     Requires a cobamide coenzyme.
REFERENCE   1
  AUTHORS   Barker, H.A.
  TITLE     Coenzyme B12-dependent mutases causing carbon chain rearrangements.
  JOURNAL   In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, Academic Press,
            New York, 1972, p. 509-537.
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K01847  methylmalonyl-CoA mutase
            KO: K01848  methylmalonyl-CoA mutase, N-terminal domain
            KO: K01849  methylmalonyl-CoA mutase, C-terminal domain
GENES       HSA: 4594(MUT)
            MMU: 17850(Mut)
            CFA: 474930(MUT)
            BTA: 280871(MUT)
            SSC: 399535(MUT)
            GGA: 422049(MUT)
            SPU: 576452(LOC576452)
            CEL: ZK1058.1(mmcm-1)
            DDI: DDBDRAFT_0187533
            LMA: LmjF27.0300
            ECO: b2917(sbm)
            ECJ: JW2884(yliK)
            ECE: Z4254(sbm)
            ECS: ECs3787
            ECC: c3498
            ECI: UTI89_C3303
            ECP: ECP_2909
            ECW: EcE24377A_3244(msm)
            YEN: YE1895
            SFL: SF2902(sbm)
            SFX: S3102(sbm)
            SFV: SFV_2963(sbm)
            SSN: SSON_3068(sbm)
            NOC: Noc_1893
            RSO: RSc0237(RS00669)
            REU: Reut_A0253
            REH: H16_A0280(sbm1) H16_A1949(sbm2) H16_B1841 H16_B1842
            RME: Rmet_0210
            BXE: Bxe_A4277
            BVI: Bcep1808_6060
            PNU: Pnuc_0910
            RFR: Rfer_2805 Rfer_3612
            POL: Bpro_2161 Bpro_4054
            PNA: Pnap_2383 Pnap_3524
            AAV: Aave_2510
            AJS: Ajs_2040
            VEI: Veis_3398
            MPT: Mpe_A0903 Mpe_A1014 Mpe_B0541
            EBA: ebA2060(sbmA) ebA3738(sbmB) ebA3766 ebD52(sbmB)
            AZO: azo0685(mutB) azo0696
            DAR: Daro_0243 Daro_4006
            GSU: GSU1578 GSU3302
            GME: Gmet_1574 Gmet_1722 Gmet_3251
            GUR: Gura_0654 Gura_1342 Gura_3481
            PPD: Ppro_0523 Ppro_1284 Ppro_1285
            BBA: Bd1853
            ADE: Adeh_0259 Adeh_1832 Adeh_1834
            AFW: Anae109_0281 Anae109_1988 Anae109_3169
            MXA: MXAN_2261 MXAN_2263(mutB) MXAN_2264(mutA)
            SFU: Sfum_0458
            MLO: mll7619 mll7621
            MES: Meso_0856 Meso_0857
            PLA: Plav_1625 Plav_1702
            SME: SMb20757(bhbA)
            SMD: Smed_4237 Smed_5086
            ATU: Atu3580(mutA)
            ATC: AGR_L_2498
            RET: RHE_PB00157(bhbA)
            BME: BMEI0799
            BMF: BAB1_1212(bhbA)
            BMS: BR1190(bhbA)
            BMB: BruAb1_1195(bhbA)
            OAN: Oant_2001
            BJA: bll3054(mutA) bll3056(mutA)
            BRA: BRADO2679(mutB) BRADO2682(mutA)
            BBT: BBta_3021(mutB) BBta_3023(mutA)
            RPA: RPA1835(mutB) RPA1837
            RPB: RPB_3536 RPB_3538
            RPC: RPC_1760 RPC_1762
            RPD: RPD_1927 RPD_1929
            RPE: RPE_1852 RPE_1854 RPE_3223 RPE_3224
            NWI: Nwi_2236 Nwi_2238
            NHA: Nham_2636 Nham_2638
            XAU: Xaut_1197 Xaut_4729 Xaut_4731 Xaut_5021 Xaut_5043
            CCR: CC_2373 CC_2374 CC_3081
            SIL: SPO0368 SPO1105
            SIT: TM1040_1865 TM1040_3106
            RSP: RSP_0961(meaA) RSP_2192(mcmA)
            RSH: Rsph17029_0867 Rsph17029_2621 Rsph17029_3657
            RSQ: Rsph17025_2300 Rsph17025_3008
            JAN: Jann_0797 Jann_3367
            RDE: RD1_1635(mutB) RD1_2035(mutA)
            PDE: Pden_3681 Pden_3875
            MMR: Mmar10_1119 Mmar10_1120
            HNE: HNE_1326(mutB) HNE_1327(mutA)
            NAR: Saro_0811
            SAL: Sala_1221
            SWI: Swit_2891
            ELI: ELI_04910
            RRU: Rru_A2479 Rru_A2480 Rru_A3062
            MGM: Mmc1_0388
            ABA: Acid345_1023 Acid345_1432 Acid345_1454
            SUS: Acid_6472 Acid_6955 Acid_6956 Acid_7412
            BHA: BH2955(mutA) BH2956(mutB) BH3796
            GKA: GK2370 GK2371 GK3391
            STH: STH1186 STH1187 STH2465 STH2466
            AMT: Amet_4542
            DSY: DSY1563 DSY1564
            DRM: Dred_1768
            TTE: TTE1217(sbm) TTE1218(sbm2) TTE2389(sbm5)
            MTU: Rv1492(mutA) Rv1493(mutB)
            MTC: MT1539(mutA) MT1540(mutB)
            MBO: Mb1529(mutA) Mb1530(mutB)
            MBB: BCG_1555(mutA) BCG_1556(mutB)
            MLE: ML1799(mutB) ML1800(mutA)
            MPA: MAP1225(mutA) MAP1226(mutB)
            MAV: MAV_3277 MAV_3278(mutA)
            MSM: MSMEG_3158(mutA) MSMEG_3159 MSMEG_4880 MSMEG_4881
            MVA: Mvan_2762 Mvan_2763 Mvan_4261
            MGI: Mflv_2387 Mflv_3649 Mflv_3650
            MMC: Mmcs_3122 Mmcs_3123 Mmcs_3825 Mmcs_3826
            MKM: Mkms_3183 Mkms_3184 Mkms_3900
            MJL: Mjls_3133 Mjls_3134 Mjls_3812
            CGL: NCgl1471(cgl1529) NCgl1472(cgl1530)
            CGB: cg1725(mcmB) cg1726(mcmA)
            CEF: CE1650 CE1651
            CDI: DIP1272(sbm) DIP1273
            NFA: nfa10360 nfa34660 nfa34670
            RHA: RHA1_ro07233(mutA) RHA1_ro07234(mutB)
            SCO: SCO4800(icmB) SCO4869(mutA2) SCO5415(icmA) SCO6472(SC9C7.08c)
                 SCO6832(mutA) SCO6833(SC3D9.01)
            SMA: SAV1912(meaA1) SAV2039(mcmB) SAV2040(meaA2) SAV2832(icmA)
                 SAV3382(mcmA2) SAV3460(icmB)
            PAC: PPA0595 PPA0596
            NCA: Noca_0798 Noca_1772 Noca_1802 Noca_2131 Noca_3544 Noca_3545
                 Noca_4143
            TFU: Tfu_2761 Tfu_2762 Tfu_2811
            FRA: Francci3_2169 Francci3_3005 Francci3_3006 Francci3_3652
            FAL: FRAAL4950(mutB) FRAAL4951(mutA) FRAAL5865(mcm)
                 FRAAL5921(meaA)
            ACE: Acel_0377 Acel_0674
            SEN: SACE_5638(mutA) SACE_5639(mutB)
            STP: Strop_0832 Strop_3608 Strop_3621
            RXY: Rxyl_1283 Rxyl_2481
            LIL: LA2956(mcm1) LB074(mcm2) LB273(mcm2) LB274(mcm3)
            LIC: LIC11105(mcm1) LIC20058(mcm2) LIC20208 LIC20209(mcmA)
            LBJ: LBJ_2060 LBJ_4062(meaA) LBJ_4126 LBJ_4127(sbm)
            LBL: LBL_4062(meaA) LBL_4142 LBL_4143(sbm)
            BTH: BT_2090 BT_2091
            BFR: BF3800 BF3801
            BFS: BF3592(mutB) BF3593(mutA)
            PGI: PG1656(mutA) PG1657(mutB)
            SRU: SRU_1689 SRU_1791 SRU_1792(mutA)
            GFO: GFO_0809(mutB) GFO_0810(mutA)
            FJO: Fjoh_0013 Fjoh_0014 Fjoh_2332
            FPS: FP1121(mutA) FP1123(mutB) FP1940
            CCH: Cag_1222 Cag_1223
            CPH: Cpha266_1164 Cpha266_1165
            PVI: Cvib_1038 Cvib_1039
            PLT: Plut_1291 Plut_1292
            RRS: RoseRS_0214 RoseRS_0544 RoseRS_0545
            RCA: Rcas_3871 Rcas_3872 Rcas_4326
            DRA: DR_1084 DR_1189 DR_2032
            DGE: Dgeo_0862 Dgeo_1320 Dgeo_1541
            TTH: TTC0676 TTC0677 TTC0881 TTC0882
            TTJ: TTHA1038 TTHA1039 TTHA1246
            TME: Tmel_1860
            FNO: Fnod_1752
            AFU: AF1288b AF2215(mcmA1) AF2219(mcmA2)
            HAL: VNG0481G(mcmA1) VNG0653G(mcmA1) VNG0673G(mcmA2)
            HMA: rrnAC0637(mcmA1) rrnAC0934(mcmA3) rrnAC1275(mcmA2)
            HWA: HQ2301A(mcmB) HQ2400A(mcmA)
            NPH: NP1226A(mcmA_2) NP2320A(mcmA_1) NP2710A(mcmB)
            TAC: Ta0462 Ta0463
            TVO: TVN0772 TVN0773
            PTO: PTO0269 PTO0270
            PHO: PH0275 PH1306
            PAB: PAB1800(mcmA1) PAB2187(mcmA2)
            PFU: PF1477 PF1946
            TKO: TK0328 TK1149
            APE: APE_1686.1 APE_1687
            SSO: SSO2266(mcmA2) SSO2425(mcmA1)
            STO: ST0552 ST2096
            SAI: Saci_0062 Saci_0924
            MSE: Msed_0638
STRUCTURES  PDB: 1E1C  1REQ  2REQ  3REQ  4REQ  5REQ  6REQ  7REQ  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.2
            ExPASy - ENZYME nomenclature database: 5.4.99.2
            ExplorEnz - The Enzyme Database: 5.4.99.2
            ERGO genome analysis and discovery system: 5.4.99.2
            UM-BBD (Biocatalysis/Biodegradation Database): 5.4.99.2
            BRENDA, the Enzyme Database: 5.4.99.2
            CAS: 9023-90-9
///
ENTRY       EC 5.4.99.3                 Enzyme
NAME        2-acetolactate mutase;
            acetolactate mutase;
            acetohydroxy acid isomerase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
SYSNAME     2-acetolactate methylmutase
REACTION    2-acetolactate = 3-hydroxy-3-methyl-2-oxobutanoate [RN:R03052]
ALL_REAC    R03052 > R05071;
            (other) R05069
SUBSTRATE   2-acetolactate [CPD:C00900]
PRODUCT     3-hydroxy-3-methyl-2-oxobutanoate [CPD:C04181]
COFACTOR    Ascorbate [CPD:C00072]
COMMENT     Requires ascorbic acid; also converts 2-aceto-2-hydroxybutanoate to
            3-hydroxy-3-methyl-2-oxopentanoate.
REFERENCE   1  [PMID:4384955]
  AUTHORS   Allaudeen HS, Ramakrishnan T.
  TITLE     Biosynthesis of isoleucine and valine in Mycobacterium tuberculosis
            H37 Rv.
  JOURNAL   Arch. Biochem. Biophys. 125 (1968) 199-209.
  ORGANISM  Mycobacterium tuberculosis
PATHWAY     PATH: map00290  Valine, leucine and isoleucine biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.3
            ExPASy - ENZYME nomenclature database: 5.4.99.3
            ExplorEnz - The Enzyme Database: 5.4.99.3
            ERGO genome analysis and discovery system: 5.4.99.3
            BRENDA, the Enzyme Database: 5.4.99.3
            CAS: 37318-52-8
///
ENTRY       EC 5.4.99.4                 Enzyme
NAME        2-methyleneglutarate mutase;
            alpha-methyleneglutarate mutase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
SYSNAME     2-methyleneglutarate carboxy-methylenemethylmutase
REACTION    2-methyleneglutarate = 2-methylene-3-methylsuccinate [RN:R03908]
ALL_REAC    R03908
SUBSTRATE   2-methyleneglutarate [CPD:C02930]
PRODUCT     2-methylene-3-methylsuccinate [CPD:C02295]
COFACTOR    Cobamide coenzyme [CPD:C00194]
COMMENT     Requires a cobamide coenzyme.
REFERENCE   1  [PMID:5266166]
  AUTHORS   Kung HF, Cederbaum S, Tsai L, Stadtman TC.
  TITLE     Nicotinic acid metabolism. V. A cobamide coenzyme-dependent
            conversion of alpha-methyleneglutaric acid to dimethylmaleic acid.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 65 (1970) 978-84.
REFERENCE   2  [PMID:5574401]
  AUTHORS   Kung HF, Stadtman TC.
  TITLE     Nicotinic acid metabolism. VI. Purification and properties of
            alpha-methyleneglutarate mutase (B 12-dependent) and methylitaconate
            isomerase.
  JOURNAL   J. Biol. Chem. 246 (1971) 3378-88.
  ORGANISM  Clostridium barkeri
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.4
            ExPASy - ENZYME nomenclature database: 5.4.99.4
            ExplorEnz - The Enzyme Database: 5.4.99.4
            ERGO genome analysis and discovery system: 5.4.99.4
            BRENDA, the Enzyme Database: 5.4.99.4
            CAS: 9059-10-3
///
ENTRY       EC 5.4.99.5                 Enzyme
NAME        chorismate mutase;
            hydroxyphenylpyruvate synthase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
SYSNAME     chorismate pyruvatemutase
REACTION    chorismate = prephenate [RN:R01715]
ALL_REAC    R01715
SUBSTRATE   chorismate [CPD:C00251]
PRODUCT     prephenate [CPD:C00254]
REFERENCE   1  [PMID:14323651]
  AUTHORS   COTTON RG, GIBSON F.
  TITLE     THE BIOSYNTHESIS OF PHENYLALANINE AND TYROSINE; ENZYMES CONVERTING
            CHORISMIC ACID INTO PREPHENIC ACID AND THEIR RELATIONSHIPS TO
            PREPHENATE DEHYDRATASE AND PREPHENATE DEHYDROGENASE.
  JOURNAL   Biochim. Biophys. Acta. 100 (1965) 76-88.
  ORGANISM  Escherichia coli [GN:eco], Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4962500]
  AUTHORS   Lorence JH, Nester EW.
  TITLE     Multiple molecular forms of chorismate mutase in Bacillus subtillis.
  JOURNAL   Biochemistry. 6 (1967) 1541-53.
  ORGANISM  Bacillus subtillis
REFERENCE   3  [PMID:5443801]
  AUTHORS   Sprossler B, Lingens F.
  TITLE     [Chorismate mutase from Claviceps. I. Properties of chorismate
            mutase from different strains of Claviceps]
  JOURNAL   Hoppe. Seylers. Z. Physiol. Chem. 351 (1970) 448-58.
REFERENCE   4  [PMID:4708674]
  AUTHORS   Woodin TS, Nishioka L.
  TITLE     Evidence for three isozymes of chorismate mutase in alfalfa.
  JOURNAL   Biochim. Biophys. Acta. 309 (1973) 211-23.
  ORGANISM  alfalfa
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ORTHOLOGY   KO: K01850  chorismate mutase
            KO: K04092  chorismate mutase
            KO: K04093  chorismate mutase
            KO: K04516  chorismate mutase
            KO: K06208  chorismate mutase
            KO: K06209  chorismate mutase
GENES       ATH: AT1G69370(CM3) AT3G29200(CM1) AT5G10870(ATCM2)
            OSA: 4326889 4328508
            CME: CMQ210C
            SCE: YPR060C(ARO7)
            AGO: AGOS_ADL326W
            PIC: PICST_73224
            CGR: CAGL0K12232g
            SPO: SPAC16E8.04c
            ANI: AN6866.2
            AFM: AFUA_5G05690 AFUA_5G13130
            AOR: AO090009000693 AO090120000438
            CNE: CNA07970 CNM00820
            UMA: UM04220.1
            ECO: b2599(pheA) b2600(tyrA)
            ECJ: JW2580(pheA) JW2581(tyrA)
            ECE: Z3891(pheA) Z3892(tyrA)
            ECS: ECs3462 ECs3463
            ECC: c3120(pheA) c3121(tyrA)
            ECI: UTI89_C2932(pheA) UTI89_C2933(tyrA)
            ECP: ECP_2600 ECP_2601
            ECV: APECO1_3933(pheA) APECO1_3934
            ECW: EcE24377A_2883(pheA) EcE24377A_2884(tyrA)
            ECX: EcHS_A2756 EcHS_A2757(tyrA)
            STY: STY1852(aroQ) STY2854(pheA) STY2856(tyrA)
            STT: t1147(aroQ) t2622(pheA) t2624(tyrA)
            SPT: SPA1577(aroQ) SPA2526(pheA) SPA2528(tyrA)
            SEC: SC1279 SC2669(pheA) SC2671(tyrA)
            STM: STM2667(pheA) STM2669(tyrA)
            YPE: YPO1353 YPO3281(pheA) YPO3285(tyrA)
            YPK: y0904(tyrA) y2828
            YPM: YP_0399(tyrA) YP_0400(pheA1) YP_1243(pheA2)
            YPA: YPA_0640 YPA_2773 YPA_2860
            YPN: YPN_0814 YPN_0815 YPN_2630
            YPS: YPTB0842(tyrA) YPTB0843(pheA) YPTB1379
            YPI: YpsIP31758_3218(pheA) YpsIP31758_3219(tyrA)
            SFL: SF2659(pheA) SF2660(tyrA)
            SFX: S2836(pheA) S2837(tyrA)
            SFV: SFV_2871(tyrA) SFV_2872(pheA)
            SSN: SSON_2750(pheA) SSON_2751(tyrA)
            SBO: SBO_2637(pheA) SBO_2638(tyrA)
            SDY: SDY_2766(tyrA) SDY_2767(pheA)
            ECA: ECA1449 ECA3350(pheA) ECA3351(tyrA)
            PLU: plu1263(tyrA) plu1265(pheA)
            BUC: BU392(pheA)
            BAS: BUsg379(pheA)
            BAB: bbp355(pheA)
            BCC: BCc_244(pheA)
            SGL: SG0579 SG0580
            ENT: Ent638_1896
            BFL: Bfl178(tyrA)
            BPN: BPEN_184(tyrA)
            HIN: HI1145(pheA) HI1290(tyrA)
            HIT: NTHI1313(pheA) NTHI1833(tyrA)
            HDU: HD0873(pheA)
            HSO: HS_0365(pheA) HS_0671(tyrA)
            PMU: PM0150(pheA) PM0664(tyrA)
            MSU: MS1102(tyrA) MS1657(pheA)
            APL: APL_0184(tyrA) APL_1033(pheA)
            XFA: XF1141 XF2325
            XFT: PD0426(pheA) PD1357(pheA)
            XCC: XCC0556(pheA) XCC1590(pheA)
            XCB: XC_2644 XC_3676
            XCV: XCV1690(pheA) XCV3765
            XAC: XAC1649(pheA) XAC3647(pheA)
            XOO: XOO0734(pheA) XOO2387(pheA)
            XOM: XOO_0670(XOO0670) XOO_2267(XOO2267)
            VCH: VC0696 VC0705
            VCO: VC0395_A0227(tyrA) VC0395_A0235(pheA)
            VVU: VV1_0487 VV1_0494
            VVY: VV0702
            VPA: VP0547 VP0555
            VFI: VF0554 VF0561
            PPR: PBPRA3024 PBPRA3025
            PAE: PA3166(pheA) PA5184
            PPU: PP_1769(pheA)
            PST: PSPTO_0357(aroH) PSPTO_1747(pheA)
            PSB: Psyr_3645 Psyr_4818
            PSP: PSPPH_3665(pheA) PSPPH_4849(aroH)
            PFL: PFL_0385 PFL_4312(pheA)
            PFO: Pfl_3544 Pfl_4076
            PEN: PSEEN0389 PSEEN1489(pheA)
            PAR: Psyc_1186(pheA)
            ACI: ACIAD2223(pheA)
            SON: SO_1362(tyrA) SO_1367(pheA)
            SDN: Sden_2747 Sden_2749
            SFR: Sfri_2915
            SHE: Shewmr4_2833
            SHM: Shewmr7_2915
            SHN: Shewana3_3007 Shewana3_3012
            ILO: IL1721(tyrA)
            CPS: CPS_1221(pheA) CPS_3953(tyrA)
            PHA: PSHAa0949(tyrA) PSHAa0950(pheA)
            PAT: Patl_1588 Patl_1590
            CBD: COXBU7E912_1065(pheA)
            MCA: MCA1418(pheA)
            FTU: FTT0834(aroQ) FTT1650c
            FTF: FTF0834(aroQ) FTF1650c
            FTW: FTW_1352(aroH)
            FTL: FTL_0043 FTL_0328
            FTH: FTH_0043 FTH_0326
            FTA: FTA_0055 FTA_0349(aroH) FTA_1470
            FTN: FTN_0033 FTN_0349(aroH)
            TCX: Tcr_1193
            NOC: Noc_0174
            AEH: Mlg_0926
            HCH: HCH_03913(aroQ1) HCH_04981 HCH_06004(aroQ2)
            ABO: ABO_1749(pheA)
            AHA: AHA_1092(pheA) AHA_1655(tyrA)
            DNO: DNO_0926
            VOK: COSY_0579(pheA)
            NME: NMB0446
            NMA: NMA2039(pheA)
            NMC: NMC1705(pheA)
            NGO: NGO1510
            CVI: CV_2355(pheA)
            RSO: RS04710(RSp0197) RSc0904(pheA)
            REU: Reut_A2575
            REH: H16_A0792(pheA)
            RME: Rmet_0716
            BMA: BMA0432 BMA0480
            BMV: BMASAVP1_A2575(pheA) BMASAVP1_A2635(aroQ)
            BML: BMA10299_A0950(pheA)
            BMN: BMA10247_0141(aroQ) BMA10247_0198(pheA)
            BXE: Bxe_A0915 Bxe_A0977
            BUR: Bcep18194_A4115 Bcep18194_A4156
            BAM: Bamb_0867 Bamb_0919
            BPS: BPSL2518(pheA) BPSL2555
            BPM: BURPS1710b_2997(pheA) BURPS1710b_3039(aroH)
            BPL: BURPS1106A_2948(pheA) BURPS1106A_3005
            BPD: BURPS668_2885(pheA) BURPS668_2939
            BTE: BTH_I1596 BTH_I1635
            BPE: BP0946(pheA)
            BPA: BPP3132(pheA)
            BBR: BB3471(pheA)
            RFR: Rfer_1569
            POL: Bpro_1792
            HAR: HEAR2579(pheA)
            MMS: mma_2673
            NEU: NE0335(pheA)
            NET: Neut_1570
            NMU: Nmul_A2192
            EBA: ebA906(pheA)
            AZO: azo1068(pheA)
            DAR: Daro_1232
            TBD: Tbd_0951
            MFA: Mfla_1686
            HHE: HH1508(pheA)
            WSU: WS0332(pheA)
            TDN: Tmden_0470
            CJE: Cj0316(pheA)
            CJR: CJE0361(pheA)
            CJU: C8J_0293(pheA)
            CCV: CCV52592_1666
            CCO: CCC13826_0509
            ABU: Abu_2137(pheA)
            NIS: NIS_0389(pheA) NIS_0982
            SUN: SUN_1870 SUN_2057(pheA)
            GSU: GSU1828 GSU2608(pheA)
            GME: Gmet_0862 Gmet_1955
            PCA: Pcar_1323 Pcar_1887
            DVU: DVU0462
            DDE: Dde_3487
            BBA: Bd0925 Bd3700
            DPS: DP2171
            ADE: Adeh_0182
            MXA: MXAN_3221(pheA)
            SAT: SYN_01299
            SFU: Sfum_2723 Sfum_2763
            PUB: SAR11_1032
            MLO: mlr4380
            MES: Meso_3340
            SME: SMc03858(pheAa)
            ATU: Atu2698(tyrA)
            ATC: AGR_C_4890A
            RET: RHE_CH03958(tyrA)
            RLE: RL4548
            BME: BMEI0226
            BMF: BAB1_1833
            BMS: BR1825
            BMB: BruAb1_1804
            BOV: BOV_1757
            BRA: BRADO6462
            BBT: BBta_1184
            BHE: BH16030(tyrA)
            BQU: BQ12930(tyrA)
            SIL: SPO3252
            SIT: TM1040_2606
            RSP: RSP_1049(pheAa)
            JAN: Jann_0750
            RDE: RD1_1312
            MMR: Mmar10_1341
            HNE: HNE_0037
            ZMO: ZMO0563(aroH)
            NAR: Saro_1352
            SAL: Sala_0513
            ELI: ELI_03660
            GOX: GOX2001
            GBE: GbCGDNIH1_0141
            MGM: Mmc1_0176
            BSU: BG10286(aroH) BG10375(aroA) BG10913(pheB)
            BHA: BH1214(pheB) BH1658(aroH) BH3242(aroA)
            BAN: BA2958
            BAR: GBAA2958
            BAA: BA_3466
            BAT: BAS2748
            BCE: BC2942 BC4674
            BCA: BCE_2998
            BCZ: BCZK2677(aroA)
            BTK: BT9727_2698(aroA)
            BLI: BL00056(aroA) BL01157(pheB) BL02776(aroH)
            BLD: BLi02404(aroH) BLi02918(pheB) BLi03126(aroA)
            BCL: ABC1543(pheB) ABC1894(aroH) ABC2765(aroA)
            BAY: RBAM_020850 RBAM_024960
            BPU: BPUM_2000 BPUM_2431 BPUM_2621
            OIH: OB1783(aroH) OB2227(aroG)
            GKA: GK2205(aroH) GK2605 GK2811
            SAU: SA1469 SA1558
            SAV: SAV1643(pheB) SAV1737
            SAM: MW1593 MW1680
            SAR: SAR1723 SAR1815
            SAS: SAS1579 SAS1663
            SAC: SACOL1698 SACOL1787
            SAB: SAB1512c SAB1597c(aroA)
            SAA: SAUSA300_1599(pheB) SAUSA300_1683
            SAO: SAOUHSC_01752 SAOUHSC_01852
            SEP: SE1326 SE1410
            SER: SERP1207 SERP1297
            SHA: SH1185(aroA) SH1278
            SSP: SSP1026 SSP1116
            LMO: lmo1600(aroA) lmo1926
            LMF: LMOf2365_1621 LMOf2365_1955(aroH)
            LIN: lin1641(aroA) lin2040
            LWE: lwe1614 lwe1952(aroH)
            LLA: L64445(ywiC)
            LLC: LACR_2509
            LLM: llmg_2481
            SPY: SPy_0722
            SPZ: M5005_Spy_0549
            SPM: spyM18_0789(cm)
            SPG: SpyM3_0472
            SPS: SPs1383
            SPH: MGAS10270_Spy0606
            SPI: MGAS10750_Spy0632
            SPJ: MGAS2096_Spy0610
            SPK: MGAS9429_Spy0602
            SPA: M6_Spy0569
            SPB: M28_Spy0527
            SPN: SP_1296
            SPR: spr1174
            SPD: SPD_1151
            SAG: SAG0540
            SAN: gbs0585
            SAK: SAK_0690
            SMU: SMU.1291c SMU.531
            STC: str1181(aroH)
            STL: stu1181(aroH)
            SSA: SSA_1268(aroH)
            SGO: SGO_1386
            LSA: LSA1662
            LDB: Ldb0313 Ldb1351(pheB)
            LBU: LBUL_0271 LBUL_1260
            LCA: LSEI_1046
            CAC: CAC1234(pheB)
            CPE: CPE0698 CPE1414(pheB)
            CPF: CPF_0691 CPF_1668
            CPR: CPR_0692 CPR_1404
            CTC: CTC00116 CTC01316
            CNO: NT01CX_0622 NT01CX_1681
            CTH: Cthe_0711
            CDF: CD1453 CD1832 CD1836(pheA)
            CBO: CBO1809(aroH)
            CBA: CLB_1744(aroH)
            CBH: CLC_1751(aroH)
            CBF: CLI_1804(aroH)
            CKL: CKL_0789(pheA)
            CHY: CHY_0473(aroH1) CHY_1913(pheB) CHY_1932(aroH2)
            DSY: DSY2247 DSY2265
            SWO: Swol_1395
            TTE: TTE1349 TTE2621
            MTA: Moth_1343
            MTU: Rv1885c
            MTC: MT1933
            MBO: Mb1917c
            MPA: MAP1608c
            MAV: MAV_1069
            MSM: MSMEG_5536
            MMC: Mmcs_2737
            RHA: RHA1_ro06105(tryA)
            SCO: SCO1762(SCI51.02c) SCO2019(SC7H2.33c)
            SMA: SAV6210(aroH2) SAV6520(aroH1)
            TWH: TWT793
            TWS: TW802
            LXX: Lxx23250(tyrA)
            AAU: AAur_2705
            PAC: PPA1766
            NCA: Noca_2499
            TFU: Tfu_1207
            FRA: Francci3_2464
            SEN: SACE_7067(aroH)
            BLO: BL0397
            BAD: BAD_1452
            FNU: FN1487
            RBA: RB8741(aroH) RB9107(pheA)
            CTA: CTA_0416(aroG)
            TDE: TDE1502(aroH)
            LIL: LA1256(aroQ)
            LIC: LIC12451(pheA)
            LBJ: LBJ_0932(pheA)
            LBL: LBL_2101(pheA)
            SYN: sll0109(aroH)
            SYW: SYNW1885(tyrA)
            SYC: syc2179_d(aroH)
            SYF: Synpcc7942_1915
            SYD: Syncc9605_0582
            SYE: Syncc9902_1782
            SYG: sync_2100(aroH)
            SYR: SynRCC307_0643(aroH)
            SYX: SynWH7803_1896(aroH)
            CYA: CYA_0836(aroH)
            CYB: CYB_1839(aroH)
            TEL: tll1803(aroH)
            GVI: glr2705
            ANA: all0418 all4012
            AVA: Ava_1690
            PMA: Pro1297(aroH)
            PMM: PMM1181(tyrA)
            PMT: PMT1366(tyrA)
            PMN: PMN2A_0800
            PMI: PMT9312_1282
            PMB: A9601_13741(aroH)
            PMC: P9515_13531(aroH)
            PMF: P9303_06141(aroH)
            PMG: P9301_13821(aroH)
            PME: NATL1_16551(aroH)
            TER: Tery_2493
            BTH: BT_3933(tyrA) BT_3934
            BFR: BF3944 BF3945
            BFS: BF3717 BF3718
            PGI: PG0885
            CHU: CHU_0719(pheB)
            DET: DET0461(tyrA)
            DEH: cbdb_A424(pheA)
            DRA: DR_1001
            DGE: Dgeo_1572
            TTH: TTC0020 TTC0514
            TTJ: TTHA0388 TTHA0868
            AAE: aq_951(pheA)
            TMA: TM0155
            MJA: MJ0246
            MMP: MMP0578(aroQ)
            MAC: MA1377
            MBA: Mbar_A3126
            MMA: MM_2361
            MBU: Mbur_0876
            MTH: MTH804
            MST: Msp_0105
            MSI: Msm_0834
            MKA: MK1609(pheA)
            AFU: AF0227(pheA)
            HAL: VNG1244C
            HMA: rrnAC0752
            HWA: HQ2763A(pheA)
            NPH: NP3980A(pheA1)
            PTO: PTO0837
            PFU: PF1701
            TKO: TK0261
            RCI: RCIX1315(aroQ)
            APE: APE_0562.1 APE_0562a(aroQ)
            STO: ST0294
            PAI: PAE1941
            NEQ: NEQ192
STRUCTURES  PDB: 1COM  1DBF  1FNJ  1FNK  1ODE  1UFY  1UI9  1YBZ  2AO2  2CHS  
                 2CHT  2CSM  2D8D  2D8E  2F6L  2FP1  2FP2  2GBB  2GTV  2PV7  
                 2QBV  3CSM  4CSM  5CSM  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.5
            ExPASy - ENZYME nomenclature database: 5.4.99.5
            ExplorEnz - The Enzyme Database: 5.4.99.5
            ERGO genome analysis and discovery system: 5.4.99.5
            BRENDA, the Enzyme Database: 5.4.99.5
            CAS: 9068-30-8
///
ENTRY       EC 5.4.99.6       Obsolete  Enzyme
NAME        Transferred to 5.4.4.2
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
COMMENT     Transferred entry: Now EC 5.4.4.2, isochorismate synthase (EC
            5.4.99.6 created 1972, deleted 2003)
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.6
            ExPASy - ENZYME nomenclature database: 5.4.99.6
            ExplorEnz - The Enzyme Database: 5.4.99.6
            ERGO genome analysis and discovery system: 5.4.99.6
            BRENDA, the Enzyme Database: 5.4.99.6
///
ENTRY       EC 5.4.99.7                 Enzyme
NAME        lanosterol synthase;
            2,3-epoxysqualene lanosterol cyclase;
            squalene-2,3-oxide-lanosterol cyclase;
            lanosterol 2,3-oxidosqualene cyclase;
            squalene 2,3-epoxide:lanosterol cyclase;
            2,3-oxidosqualene sterol cyclase;
            oxidosqualene cyclase;
            2,3-oxidosqualene cyclase;
            2,3-oxidosqualene-lanosterol cyclase;
            oxidosqualene-lanosterol cyclase;
            squalene epoxidase-cyclase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
SYSNAME     (S)-2,3-epoxysqualene mutase (cyclizing, lanosterol-forming)
REACTION    (S)-2,3-epoxysqualene = lanosterol [RN:R03199]
ALL_REAC    R03199
SUBSTRATE   (S)-2,3-epoxysqualene [CPD:C01054]
PRODUCT     lanosterol [CPD:C01724]
INHIBITOR   29-MOS [CPD:C05373]
REFERENCE   1  [PMID:6027261]
  AUTHORS   Dean PD, Ortiz de Montellano PR, Bloch K, Corey EJ.
  TITLE     A soluble 2,3-oxidosqualene sterol cyclase.
  JOURNAL   J. Biol. Chem. 242 (1967) 3014-5.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K01852  lanosterol synthase
GENES       HSA: 4047(LSS)
            PTR: 474058(LSS)
            MMU: 16987(Lss)
            RNO: 81681(Lss)
            CFA: 491611(LOC491611)
            BTA: 615906(LSS)
            GGA: 424037(LSS)
            CME: CMJ009C
            SCE: YHR072W(ERG7)
            AGO: AGOS_AGR351W
            PIC: PICST_49236(NOP10) PICST_77382(ERG7)
            CAL: CaO19_1570(CaO19.1570)
            CGR: CAGL0J10824g
            SPO: SPAC13G7.01c(erg7)
            AFM: AFUA_4G14770 AFUA_5G04080
            AOR: AO090102000611
            CNE: CND02520 CND02590
            DDI: DDB_0191311(CAS1)
            TBR: Tb927.7.5230
            BBA: Bd1064(osc)
            RPD: RPD_3573
STRUCTURES  PDB: 1W6J  1W6K  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.7
            ExPASy - ENZYME nomenclature database: 5.4.99.7
            ExplorEnz - The Enzyme Database: 5.4.99.7
            ERGO genome analysis and discovery system: 5.4.99.7
            BRENDA, the Enzyme Database: 5.4.99.7
            CAS: 9032-71-7
///
ENTRY       EC 5.4.99.8                 Enzyme
NAME        cycloartenol synthase;
            2,3-epoxysqualene cycloartenol-cyclase;
            squalene-2,3-epoxide-cycloartenol cyclase;
            2,3-epoxysqualene cycloartenol-cyclase;
            2,3-epoxysqualene-cycloartenol cyclase;
            2,3-oxidosqualene-cycloartenol cyclase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
SYSNAME     (S)-2,3-epoxysqualene mutase (cyclizing, cycloartenol-forming)
REACTION    (S)-2,3-epoxysqualene = cycloartenol [RN:R03200]
ALL_REAC    R03200
SUBSTRATE   (S)-2,3-epoxysqualene [CPD:C01054]
PRODUCT     cycloartenol [CPD:C01902]
REFERENCE   1  [PMID:5797101]
  AUTHORS   Rees HH, Goad LJ, Goodwin TW.
  TITLE     2,3-oxidosqualene cycloartenol cyclase from Ochromonas malhamensis.
  JOURNAL   Biochim. Biophys. Acta. 176 (1969) 892-4.
  ORGANISM  Ochromonas malhamensis
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K01853  cycloartenol synthase
GENES       ATH: AT1G78960(ATLUP2) AT2G07050(CAS1) AT3G45130(LAS1)
                 AT4G15340(ATPEN1) AT5G36150(ATPEN3) AT5G42600(MRN)
            OSA: 4328256
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.8
            ExPASy - ENZYME nomenclature database: 5.4.99.8
            ExplorEnz - The Enzyme Database: 5.4.99.8
            ERGO genome analysis and discovery system: 5.4.99.8
            BRENDA, the Enzyme Database: 5.4.99.8
            CAS: 9075-25-6
///
ENTRY       EC 5.4.99.9                 Enzyme
NAME        UDP-galactopyranose mutase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
SYSNAME     UDP-D-galactopyranose furanomutase
REACTION    UDP-D-galactopyranose = UDP-D-galacto-1,4-furanose [RN:R00505]
ALL_REAC    R00505
SUBSTRATE   UDP-D-galactopyranose [CPD:C00052]
PRODUCT     UDP-D-galacto-1,4-furanose [CPD:C03733]
REFERENCE   1  [PMID:5419754]
  AUTHORS   Trejo AG, Chittenden GJ, Buchanan JG, Baddiley J.
  TITLE     Uridine diphosphate alpha-D-galactofuranose, an intermediate in the
            biosynthesis of galactofuranosyl residues.
  JOURNAL   Biochem. J. 117 (1970) 637-9.
ORTHOLOGY   KO: K01854  UDP-galactopyranose mutase
GENES       ECO: b2036(glf)
            ECJ: JW2021(glf)
            STY: STY0759
            STT: t2157
            SPT: SPA2022
            STM: STM0719
            MSU: MS0661(glf)
            APL: APL_1467(rfbD)
            ASU: Asuc_0821
            XCC: XCC3698(rfbD)
            XCB: XC_3769
            XCV: XCV3861(glf)
            XAC: XAC3742(rfbD)
            PST: PSPTO_2898(glf)
            PSB: Psyr_2702
            PSP: PSPPH_2481(glf)
            PMY: Pmen_2341
            SPC: Sputcn32_3894
            SPL: Spea_0608
            PAT: Patl_3069
            PIN: Ping_2040
            DNO: DNO_0338(glf)
            MFA: Mfla_1194
            HHE: HH0203(glf)
            CJE: Cj1439c(glf)
            CJD: JJD26997_0717(glf)
            SMD: Smed_5685
            ATU: Atu3975(glf)
            ATC: AGR_L_1762
            PDE: Pden_5043
            GOX: GOX1488
            GKA: GK3316
            LLC: LACR_0219
            LLM: llmg_0224(glf1)
            SPR: spr0319(cps2P)
            SPD: SPD_0327(cps2P)
            LPL: lp_1176(glf1) lp_1219(glf2)
            LJO: LJ1032
            LAC: LBA1725(epsJ) LBA1726
            LSL: LSL_1548(glf)
            LDB: Ldb1949(glf1) Ldb2002(glf2)
            LBU: LBUL_1810
            LRE: Lreu_1374
            EFA: EF2487(glf)
            OOE: OEOE_1741
            CAC: CAC2169
            CBO: CBO2685
            CBA: CLB_2626(glf)
            CBH: CLC_2558(glf)
            CBF: CLI_2750(glf)
            CKL: CKL_3625(glf)
            DSY: DSY3008
            MGE: MG_137(glf)
            MPN: MPN278(yefE)
            MMY: MSC_0970(glf) MSC_0977(glf) MSC_0984(glf)
            MMO: MMOB4200(glf)
            MTU: Rv3809c(glf)
            MTC: MT3916(glf)
            MBO: Mb3839c(glf)
            MBB: BCG_3871c(glf)
            MLE: ML0092(glf)
            MPA: MAP0211(glf)
            MAV: MAV_0208(glf)
            MSM: MSMEG_6404(glf)
            MVA: Mvan_5650
            MGI: Mflv_1159
            MMC: Mmcs_5020
            MKM: Mkms_5108
            MJL: Mjls_5401
            CGL: NCgl2788(cgl2888)
            CGB: cg3196(glf)
            CEF: CE2719
            CDI: DIP2203(glf)
            CJK: jk0127(glf)
            NFA: nfa1760(glf)
            RHA: RHA1_ro04053
            ART: Arth_2694
            AAU: AAur_2676(glf)
            NCA: Noca_1401
            KRA: Krad_3888
            SEN: SACE_0165(glf)
            STP: Strop_1637
            BLO: BL1245(gif)
            BAD: BAD_0159(gif)
            PMA: Pro1286(glf)
            PMB: A9601_14591(glf)
            BFS: BF1370(wcfM)
            DRA: DR_A0367
            DGE: Dgeo_2530
            TTH: TTC0529
            TTJ: TTHA0886
            FNO: Fnod_1454
            MST: Msp_0065 Msp_0223
STRUCTURES  PDB: 1I8T  1V0J  1WAM  2BI7  2BI8  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.9
            ExPASy - ENZYME nomenclature database: 5.4.99.9
            ExplorEnz - The Enzyme Database: 5.4.99.9
            ERGO genome analysis and discovery system: 5.4.99.9
            BRENDA, the Enzyme Database: 5.4.99.9
            CAS: 174632-18-9
///
ENTRY       EC 5.4.99.10      Obsolete  Enzyme
NAME        Deleted entry
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
COMMENT     Deleted entry: Now included with EC 5.4.99.11 isomaltulose synthase
            (EC 5.4.99.10 created 1984, deleted 1992)
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.10
            ExPASy - ENZYME nomenclature database: 5.4.99.10
            ExplorEnz - The Enzyme Database: 5.4.99.10
            ERGO genome analysis and discovery system: 5.4.99.10
            BRENDA, the Enzyme Database: 5.4.99.10
///
ENTRY       EC 5.4.99.11                Enzyme
NAME        isomaltulose synthase;
            isomaltulose synthetase;
            sucrose alpha-glucosyltransferase;
            trehalulose synthase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
SYSNAME     sucrose glucosylmutase
REACTION    sucrose = 6-O-alpha-D-glucopyranosyl-D-fructofuranose [RN:R00810
            R06217]
ALL_REAC    R00810 R06217(G)
SUBSTRATE   sucrose [CPD:C00089]
PRODUCT     6-O-alpha-D-glucopyranosyl-D-fructofuranose [CPD:C01742]
COMMENT     The enzyme simultaneously produces isomaltulose
            (6-O-alpha-D-glucopyranosyl-D-fructose) and smaller amounts of
            trehalulose (1-O-alpha-D-glucopyranosyl-beta-D-fructose) from
            sucrose.
REFERENCE   1  [PMID:6743261]
  AUTHORS   Cheetham PS.
  TITLE     The extraction and mechanism of a novel isomaltulose-synthesizing
            enzyme from Erwinia rhapontici.
  JOURNAL   Biochem. J. 220 (1984) 213-20.
  ORGANISM  Erwinia rhapontici
REFERENCE   2
  AUTHORS   Cheetham, P.S.J., Imber, C.E. and Isherwood, J.
  TITLE     The formation of isomaltulose by immobilized Erwinia rhapontici.
  JOURNAL   Nature 299 (1982) 628-631.
  ORGANISM  Erwinia rhapontici
STRUCTURES  PDB: 1M53  1ZJA  1ZJB  2PWD  2PWE  2PWF  2PWG  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.11
            ExPASy - ENZYME nomenclature database: 5.4.99.11
            ExplorEnz - The Enzyme Database: 5.4.99.11
            ERGO genome analysis and discovery system: 5.4.99.11
            BRENDA, the Enzyme Database: 5.4.99.11
            CAS: 159940-49-5
///
ENTRY       EC 5.4.99.12                Enzyme
NAME        tRNA-pseudouridine synthase I;
            tRNA-uridine isomerase;
            tRNA pseudouridylate synthase I;
            transfer ribonucleate pseudouridine synthetase;
            pseudouridine synthase;
            transfer RNA pseudouridine synthetase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
SYSNAME     tRNA-uridine uracilmutase
REACTION    tRNA uridine = tRNA pseudouridine [RN:R03020]
ALL_REAC    R03020
SUBSTRATE   tRNA uridine [CPD:C00868]
PRODUCT     tRNA pseudouridine [CPD:C02764]
COMMENT     The uridylate residues at positions 38, 39 and 40 of nearly all
            tRNAs are isomerized to pseudouridine.
REFERENCE   1  [PMID:370771]
  AUTHORS   Arena F, Ciliberto G, Ciampi S, Cortese R.
  TITLE     Purification of pseudouridylate synthetase I from Salmonella
            typhimurium.
  JOURNAL   Nucleic. Acids. Res. 5 (1978) 4523-36.
  ORGANISM  Salmonella typhimurium
REFERENCE   2  [PMID:3276686]
  AUTHORS   Kammen HO, Marvel CC, Hardy L, Penhoet EE.
  TITLE     Purification, structure, and properties of Escherichia coli tRNA
            pseudouridine synthase I.
  JOURNAL   J. Biol. Chem. 263 (1988) 2255-63.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K03177  tRNA pseudouridine synthase B
            KO: K06043  tRNA-pseudouridine synthase I
            KO: K06173  tRNA pseudouridine synthase A
            KO: K06175  tRNA pseudouridine synthase C
            KO: K06176  tRNA pseudouridine synthase D
            KO: K06177  ribosomal large subunit pseudouridine synthase A
            KO: K06178  ribosomal large subunit pseudouridine synthase B
            KO: K06179  ribosomal large subunit pseudouridine synthase C
            KO: K06180  ribosomal large subunit pseudouridine synthase D
            KO: K06181  ribosomal large subunit pseudouridine synthase E
            KO: K06182  ribosomal large subunit pseudouridine synthase F
            KO: K06183  ribosomal small subunit pseudouridine synthase A
GENES       HSA: 80324(PUS1)
            MMU: 56361(Pus1)
            CFA: 609867(PUS1)
            GGA: 416799(PUS1)
            SPU: 591551(LOC591551)
            DME: Dmel_CG4159
            CEL: W06H3.2(pus-1)
            ATH: AT1G76120 AT3G06950
            OSA: 4338284 4342081
            CME: CMC024C CMQ041C
            SCE: YPL212C(PUS1)
            AGO: AGOS_AFL105C
            PIC: PICST_58964
            CGR: CAGL0E05764g CAGL0M05797g
            SPO: SPCC126.03
            ANI: AN6165.2
            AFM: AFUA_2G08460
            AOR: AO090011000855
            CNE: CNN00820
            UMA: UM05416.1
            ECU: ECU04_0890
            DDI: DDBDRAFT_0216904 DDBDRAFT_0218427 DDB_0231224(pus1)
            TAN: TA12870 TA13560 TA16330
            TPV: TP01_1009 TP02_0380 TP02_0508
            TET: TTHERM_00011450 TTHERM_00181100 TTHERM_00218830
                 TTHERM_01107460
            TBR: Tb927.6.2910
            EHI: 15.t00020 359.t00004 45.t00007 76.t00032
            ECO: b0058(rluA) b1086(rluC) b1135(ymfC) b1269(yciL) b2183(rsuA)
                 b2318(truA) b2594(rluD) b2745(ygbO) b2791(yqcB) b3166(truB)
                 b4022(yjbC)
            ECJ: JW0057(rluA) JW1072(rluC) JW1121(ymfC) JW1261(rluB)
                 JW2171(rsuA) JW2315(truA) JW2576(rluD) JW2715(truD)
                 JW2762(yqcB) JW3135(truB) JW3982(yjbC)
            ECE: Z0066(yabO) Z1725(yceC) Z1864(ymfC) Z2541(yciL) Z3442(rsuA)
                 Z3580(truA) Z3888(sfhB) Z4053(ygbO) Z4107 Z4527(truB)
                 Z5620(yjbC)
            ECS: ECs0062 ECs1464 ECs1607 ECs1841 ECs3075 ECs3202 ECs3457
                 ECs3599 ECs3651 ECs4047 ECs5005
            ECC: c0069(yabO) c1355(rluC) c1514 c1734(yciL) c2720(rsuA)
                 c2863(truA) c3116(sfhB) c3312(ygbO) c3357(yqcB) c3922(truB)
                 c4988(yjbC)
            ECI: UTI89_C0063(rluA) UTI89_C1211(yceC) UTI89_C1264(rluE)
                 UTI89_C1537(yciL) UTI89_C2460(rsuA) UTI89_C2603(truA)
                 UTI89_C2927(rluD) UTI89_C3116(truD) UTI89_C3161(truC)
                 UTI89_C3596(truB) UTI89_C4590(yjbC)
            ECP: ECP_0059 ECP_1078 ECP_1130 ECP_1316 ECP_2224 ECP_2357
                 ECP_2597 ECP_2727 ECP_2772 ECP_3254 ECP_4240
            ECV: APECO1_168 APECO1_1926(rluA) APECO1_217(rluE)
                 APECO1_2446(yjbC) APECO1_3264(truB) APECO1_3740(yqcB)
                 APECO1_3778(truD) APECO1_3936(rluD) APECO1_4246(truA)
                 APECO1_429(rluB) APECO1_4372(rsuA)
            ECW: EcE24377A_2612(truA)
            ECX: EcHS_A2469(truA)
            STY: STY0110(rluA) STY1227(rluC) STY1277(rluB) STY1331
                 STY2459(yejD) STY2599(truA) STY2851(sfhB) STY3053
                 STY3103(yqcB) STY3465(truB) STY4410(yjbC)
            STT: t0098(rluA) t0496(truA) t0632(yejD) t1632 t1683(rluB)
                 t1732(rluC) t2618(sfhB) t2829 t2873(yqcB) t3202(truB)
                 t4120(yjbC)
            SPT: SPA0096(rluA) SPA0496(truA) SPA0628(yejD) SPA1157(yciL)
                 SPA1613(rluB) SPA1664(rluC) SPA2523(sfhB) SPA2784(ygbO)
                 SPA2828(yqcB) SPA3152(truB) SPA4031(yjbC)
            SEC: SC0090(rluA) SC1134(rluC) SC1188(ymfC) SC1716(yciL)
                 SC2239(rsuA) SC2370(truA) SC2665(rluD) SC2860(ygbO)
                 SC2904(yqcB) SC3225(truB) SC4072(yjbC)
            STM: STM0095(rluA) STM1187(rluC) STM1237(ymfC) STM1719(yciL)
                 STM2222(rsuA) STM2368(truA) STM2662(rluD) STM2928(ygbO)
                 STM2964(yqcB) STM3284(truB) STM4193(yjbC)
            YPE: YPO0497(rluA) YPO1038 YPO1266(rsuA) YPO1591(rluC)
                 YPO1640(ymfC) YPO2213 YPO2766(truA) YPO3277(rluD) YPO3359
                 YPO3494(truB)
            YPK: y0690(truB) y0830 y0912(sfhB) y1599(truA) y1750 y1801 y2054
                 y2917(rsuA) y3143 y3678
            YPM: YP_0328 YP_0589(truB) YP_0654(rluD) YP_1322(rsuA1)
                 YP_1770(rsuA2) YP_2010(rsuA3) YP_2262(rluA1) YP_2398(truA)
                 YP_2813(rluA2) YP_3682(rluA3)
            YPA: YPA_0044 YPA_0512 YPA_0984 YPA_1571 YPA_1884 YPA_1934
                 YPA_2078 YPA_2768 YPA_2784 YPA_4091
            YPN: YPN_0371 YPN_0734 YPN_0819 YPN_1680 YPN_1991 YPN_2037
                 YPN_2181 YPN_2710 YPN_2964 YPN_3238
            YPP: YPDSF_0922 YPDSF_1855 YPDSF_1995
            YPS: YPTB0482(truB) YPTB0638(rluA) YPTB0772(ygbO) YPTB0846(rluD)
                 YPTB1058 YPTB1301(rsuA) YPTB2135 YPTB2428(ymfC) YPTB2478(rluC)
                 YPTB2618(truA) YPTB3009
            YPI: YpsIP31758_1420(truA)
            YEN: YE0635(rluA) YE0771 YE0891(rluD) YE1309(truA) YE1424(rsuA)
                 YE1628(rluC) YE1724(ymfC)
            SFL: SF0053(rluA) SF1090(rluC) SF1154(ymfC) SF2270(rsuA)
                 SF2394(truA) SF2653(sfhB) SF2768(ygbO) SF2804(yqcB)
                 SF3207(truB) SF4095(yjbC)
            SFX: S0055(yabO) S1170(yceC) S1237(ymfC) S1356(yciL) S2399(rsuA)
                 S2529(truA) S2829(sfhB) S2961(ygbO) S2998(yqcB) S3424(truB)
                 S3635(yjbC)
            SFV: SFV_0050(yabO) SFV_1107(yceC) SFV_1170(ymfC) SFV_1281(yciL)
                 SFV_2261(rsuA) SFV_2387(truA) SFV_2658(sfhB) SFV_2666(yqcB)
                 SFV_2753(ygbO) SFV_3196(truB) SFV_4100(yjbC)
            SSN: SSON_0064(yabO) SSON_1106(yceC) SSON_1153(ymfC)
                 SSON_1874(yciL) SSON_2239(rsuA) SSON_2376(truA)
                 SSON_2720(sfhB) SSON_2893(ygbO) SSON_2948(yqcB)
                 SSON_3312(truB) SSON_4200(yjbC)
            SBO: SBO_0045(yabO) SBO_1797(yciL) SBO_1904(ymfC) SBO_1977(yceC)
                 SBO_2141(rsuA) SBO_2355(truA) SBO_2629(sfhB) SBO_2672(yqcB)
                 SBO_2775(ygbO) SBO_3216(truB) SBO_4050(yjbC)
            SDY: SDY_0082(yabO) SDY_0896(rsuA) SDY_1339(yciL) SDY_2017(ymfC)
                 SDY_2065(yceC) SDY_2517(truA) SDY_2837(sfhB) SDY_2944(ygbO)
                 SDY_3008(yqcB) SDY_3345(truB) SDY_4310(yjbC)
            ECA: ECA0714(truB) ECA1025 ECA1790(rluC) ECA2291 ECA2440
                 ECA2742(rsuA) ECA3058(truA) ECA3347(rluD) ECA3533
                 ECA3854(rluA)
            PLU: plu0614(rluA) plu0665 plu0715 plu1268(rluD) plu2452 plu2802
                 plu2840(rluC) plu2867(rsuA) plu3173(truA) plu4527(truB)
            BUC: BU199(truA) BU282(yciL) BU348(rluC) BU375(truB) BU401(rluD)
            BAS: BUsg193(truA) BUsg271(yciL) BUsg336(rluC) BUsg363(truB)
                 BUsg388(rluD)
            BAB: bbp185(truA) bbp262(yciL) bbp318(rluC) bbp338(truB)
                 bbp363(rluD)
            BCC: BCc_129(truA) BCc_174(yciL) BCc_214(rluC) BCc_229(truB)
                 BCc_253(rluD)
            WBR: WGLp224(truB) WGLp309(truA) WGLp535(rluD)
            SGL: SG0379 SG0429 SG0583 SG1053 SG1405 SG1570 SG1619
            ENT: Ent638_1601 Ent638_2867
            KPN: KPN_01084(rluC) KPN_02708(truA)
            SPE: Spro_3334
            BFL: Bfl106(truB) Bfl181(rluD) Bfl409(rluC) Bfl496(truA)
            BPN: BPEN_110(truB) BPEN_187(rluD) BPEN_421(rluC) BPEN_512(truA)
            HIN: HI0176(sfhB) HI0412(rluC) HI0617(rluA) HI0694 HI0701 HI1199
                 HI1243(rsuA) HI1289(truB) HI1435 HI1644(truA)
            HIT: NTHI0264(rluD) NTHI0536(rluC) NTHI0817(rluE) NTHI0824(truD)
                 NTHI0874(rluA) NTHI1370(rluB) NTHI1395(truA) NTHI1696(truC)
                 NTHI1834(truB) NTHI1922(rsuA)
            HIP: CGSHiEE_08635(truD)
            HIQ: CGSHiGG_09895(truA)
            HDU: HD0337(rluB) HD0469(rluD) HD0645(rluC) HD1052 HD1057(rsuA)
                 HD1104(truA) HD1138 HD1459(truB) HD1762(rluA)
            HSO: HS_0367(sfhB) HS_0438(rusA) HS_0714(rluC) HS_0743(rluB)
                 HS_0823(truB) HS_0854(truC) HS_1258(truA) HS_1499(truD)
                 HS_1515(rluA) HS_1640(rluE)
            PMU: PM0003(rsuA_1) PM0479 PM0637(truA) PM0661 PM0756(truB)
                 PM0992(rluC) PM1605 PM1610 PM1719(sfB) PM1836(rsuA_2)
            MSU: MS0231(rluA) MS0391(rsuA) MS1038(rsuA) MS1072(rluA)
                 MS1175(truA) MS1441(truB) MS1624(rluA) MS1821(rluA) MS2273
                 MS2342(rsuA)
            APL: APL_0088(rluE) APL_0315(rluA) APL_0354(rsuA) APL_0641(truB)
                 APL_0862(truC) APL_0902(truA) APL_1122(rluD) APL_1160(rluB)
                 APL_1877(rluC) APL_1926(truD)
            ASU: Asuc_1711
            XFA: XF0237 XF0939 XF1200 XF1373 XF2453 XF2606
            XFT: PD0196(truB) PD0484(rsuA) PD0610(truA) PD1471(yciL)
                 PD1755(rluD) PD1982(rluC)
            XCC: XCC0225 XCC0273 XCC0937 XCC1704 XCC2083(rluC) XCC2214
                 XCC2509(truB) XCC2546(truA) XCC2640 XCC2951 XCC3088(rluD)
                 XCC3638(rsuA)
            XCB: XC_0235 XC_0283 XC_1070 XC_1158 XC_1477 XC_1572 XC_1607
                 XC_1904 XC_2099 XC_2527 XC_3298 XC_3709
            XCV: XCV0250(truC) XCV0298(rluE) XCV1044(rluB1) XCV1756(truD)
                 XCV2424(rluC) XCV2517(rluB2) XCV2835(truB) XCV2872(truA)
                 XCV2972(rluF) XCV3259(rsuA1) XCV3342(rluD) XCV3799(rsuA2)
            XAC: XAC0244 XAC0290 XAC1014 XAC1723 XAC2112(rluC) XAC2318
                 XAC2685(truB) XAC2720(truA) XAC2811 XAC3129 XAC3217(rluD)
                 XAC3678(rsuA)
            XOO: XOO0348 XOO0703(rsuA) XOO1552 XOO1597(rluD) XOO2161 XOO2959
                 XOO3072(rluC) XOO3216(truB) XOO3255(truA) XOO3693 XOO4531
            XOM: XOO_0320(XOO0320) XOO_0641(XOO0641) XOO_1440(XOO1440)
                 XOO_1481(XOO1481) XOO_1558(XOO1558) XOO_2030(XOO2030)
                 XOO_2810(XOO2810) XOO_2925(XOO2925) XOO_3049(XOO3049)
                 XOO_3083(XOO3083) XOO_3488(XOO3488) XOO_4268(XOO4268)
            VCH: VC0530 VC0645 VC0709 VC0888 VC0999 VC1140 VC1179 VC1635
                 VC2028 VC2223 VC2505 VCA0104
            VVU: VV1_0246 VV1_0484 VV1_1461 VV1_1584 VV1_1698 VV1_1855
                 VV1_1992 VV1_2116 VV1_2843 VV1_3016 VV1_3060 VV2_1318
            VVY: VV0713 VV0938 VV1227 VV1267 VV1426 VV2326 VV2425 VV2561
                 VV2706 VV2813 VV2924 VVA0154
            VPA: VP0559 VP0750 VP1010 VP1215 VP1951 VP2061 VP2190 VP2322
                 VP2454 VP2557 VP2679 VPA0062
            VFI: VF0271 VF0488 VF0564 VF0613 VF0880 VF1038 VF1568 VF1696
                 VF1747 VF1776 VF2071 VFA0484 VFA0485
            PPR: PBPRA0408(rluA) PBPRA0614 PBPRA1148 PBPRA1187(rluC)
                 PBPRA1544(rsuA) PBPRA1949 PBPRA2482 PBPRA2653 PBPRA2720
                 PBPRA2973 PBPRA3021(rluD) PBPRA3075 PBPRB1023(rsuA)
            PAE: PA0733 PA1110 PA2975(rluC) PA3114(truA) PA3179 PA3246(rluA)
                 PA3626 PA3968 PA4544(rluD) PA4742(truB)
            PAU: PA14_12540 PA14_17440 PA14_22000(rluA) PA14_23110(yciL)
                 PA14_23840(truA) PA14_25580(rluC) PA14_50030 PA14_54800(rsuA)
                 PA14_60210(rluD) PA14_62730(truB)
            PAP: PSPA7_2019(truA)
            PPU: PP_1191 PP_1619
            PPF: Pput_3767
            PST: PSPTO_1561 PSPTO_4021
            PSB: Psyr_0726(rluD) Psyr_1370(truD) Psyr_1390 Psyr_1610
                 Psyr_1639(rluD) Psyr_1662 Psyr_3581 Psyr_3981 Psyr_4178
                 Psyr_4336
            PSP: PSPPH_0740(sfhB) PSPPH_1603(rluA) PSPPH_1633(rluC)
                 PSPPH_1656(truA) PSPPH_3538(rluB) PSPPH_3794 PSPPH_3813(truD)
                 PSPPH_3980(rsuA) PSPPH_4187(truB) PSPPH_4378(rluE)
            PFL: PFL_0846(truB) PFL_1203(truD) PFL_1245(rsuA) PFL_1430(rsuA)
                 PFL_1602(rluB) PFL_1788(rluC) PFL_2071(truA) PFL_4382(rluA)
                 PFL_5306(rluD) PFL_5423(rluE)
            PFO: Pfl_0781 Pfl_1128 Pfl_1189 Pfl_1335 Pfl_1492 Pfl_1692
                 Pfl_1896 Pfl_4165(rluD) Pfl_4836(rluD) Pfl_4941
            PEN: PSEEN0797(truB) PSEEN1443(rluA) PSEEN1609(rluC)
                 PSEEN1689(truA) PSEEN3900(rluB) PSEEN4116 PSEEN4193(truD)
                 PSEEN4317(rsuA) PSEEN4680(rluD) PSEEN4798(rluE)
            PMY: Pmen_2717 Pmen_3606
            PAR: Psyc_0024 Psyc_0071(truB) Psyc_0257(rlu) Psyc_0286(rsu)
                 Psyc_0646 Psyc_0855 Psyc_1257(rluD) Psyc_1408(truA) Psyc_1696
                 Psyc_1988(rluA)
            PCR: Pcryo_0031 Pcryo_0076 Pcryo_0283 Pcryo_0313 Pcryo_0608
                 Pcryo_0908 Pcryo_1127 Pcryo_1568 Pcryo_1821 Pcryo_1971
                 Pcryo_2291
            PRW: PsycPRwf_1931
            ACI: ACIAD0442(rluC) ACIAD0474(truA) ACIAD0715(rluA) ACIAD0861
                 ACIAD1189 ACIAD1203 ACIAD2380(rsuA) ACIAD2897(rluD)
                 ACIAD3307(truB)
            ACB: A1S_0841 A1S_3158
            SON: SO_3436
            SDN: Sden_0685 Sden_0688 Sden_0793 Sden_1009 Sden_1014 Sden_1090
                 Sden_1200 Sden_1486 Sden_1546 Sden_1748 Sden_1830 Sden_2301
                 Sden_2436 Sden_2863 Sden_2876 Sden_3048
            SFR: Sfri_0572 Sfri_0603 Sfri_0667 Sfri_0843 Sfri_0886 Sfri_0911
                 Sfri_1056 Sfri_1262 Sfri_1395 Sfri_1437 Sfri_1491 Sfri_2258
                 Sfri_2562
            SAZ: Sama_1040 Sama_1988 Sama_2060 Sama_2124 Sama_2150 Sama_2605
                 Sama_2614 Sama_2785 Sama_2937
            SBL: Sbal_0687 Sbal_0902 Sbal_1013 Sbal_1017 Sbal_1711 Sbal_2476
                 Sbal_2696 Sbal_2742 Sbal_3123 Sbal_3237
            SBM: Shew185_2759
            SLO: Shew_0916 Shew_1209 Shew_1562 Shew_1594 Shew_2246 Shew_2306
                 Shew_2825 Shew_2950 Shew_2975 Shew_3180
            SPC: Sputcn32_1574 Sputcn32_2441 Sputcn32_2832
            SSE: Ssed_1652
            SPL: Spea_1617
            SHE: Shewmr4_0917 Shewmr4_1028 Shewmr4_1119 Shewmr4_1426
                 Shewmr4_1467 Shewmr4_1605 Shewmr4_2404 Shewmr4_2993
                 Shewmr4_2997 Shewmr4_3178
            SHM: Shewmr7_0788 Shewmr7_0952 Shewmr7_1093 Shewmr7_1190
                 Shewmr7_1491 Shewmr7_1533 Shewmr7_1680 Shewmr7_2474
                 Shewmr7_3074 Shewmr7_3078
            SHN: Shewana3_0760 Shewana3_0799 Shewana3_0916 Shewana3_1032
                 Shewana3_1120 Shewana3_1479 Shewana3_1525 Shewana3_1749
                 Shewana3_2566 Shewana3_2824 Shewana3_3171 Shewana3_3175
            SHW: Sputw3181_1072 Sputw3181_1259 Sputw3181_1567 Sputw3181_1610
                 Sputw3181_1778 Sputw3181_2448 Sputw3181_3143 Sputw3181_3146
                 Sputw3181_3254 Sputw3181_3383
            ILO: IL0750 IL0849 IL0966(truB) IL1017(truA) IL1183(sfhB) IL1309
                 IL1348 IL1743 IL2224
            CPS: CPS_0536 CPS_0916 CPS_1074 CPS_1154 CPS_2136(rsuA)
                 CPS_2205(truB) CPS_2290(rluC) CPS_2898(rluE) CPS_3519(rluB)
                 CPS_3649(truC) CPS_3803(truA) CPS_3915(rluD) CPS_4413
                 CPS_4520(rluA)
            PHA: PSHAa0085 PSHAa0467(rsuA) PSHAa0686(truD) PSHAa0933(rluD)
                 PSHAa0999(truB) PSHAa1206 PSHAa1238 PSHAa1342(rluB)
                 PSHAa1688(rluE) PSHAa1815(rluC) PSHAa1970(truC)
                 PSHAa2075(truA) PSHAa2627(rluA) PSHAb0436(rluC)
            PAT: Patl_1335 Patl_1604 Patl_1646 Patl_1697 Patl_2133 Patl_2328
                 Patl_2378 Patl_2824 Patl_3184 Patl_3469 Patl_3831 Patl_3859
            SDE: Sde_0782 Sde_1249 Sde_1620 Sde_1651 Sde_1683 Sde_1722
                 Sde_1919 Sde_2081 Sde_2551 Sde_2706 Sde_3714
            PIN: Ping_0674 Ping_0819 Ping_0982 Ping_1063 Ping_1969 Ping_2207
                 Ping_2242 Ping_3265 Ping_3527
            MAQ: Maqu_0878 Maqu_0925 Maqu_1162 Maqu_1760 Maqu_1875 Maqu_2908
                 Maqu_3346 Maqu_3602 Maqu_3815
            CBU: CBU_0487(rluC) CBU_0757(rluD) CBU_0892(truA) CBU_1059
                 CBU_1430(truB)
            CBD: COXBU7E912_0956(truA)
            LPN: lpg0814 lpg1302 lpg1333(rluD) lpg1447 lpg1623 lpg2295(rluC)
                 lpg2770
            LPF: lpl0847 lpl1265(truA) lpl1286(rluD) lpl1400 lpl1594(rluB)
                 lpl2214(rluC) lpl2687(truB)
            LPP: lpp0876 lpp1266(truA) lpp1287(rluD) lpp1402(rluB) lpp1593
                 lpp2242(rluC) lpp2818(truB)
            LPC: LPC_0727(truA)
            MCA: MCA0548 MCA0972(rluD) MCA1479(rluC) MCA1592(rluA) MCA2205
                 MCA2497(truA) MCA2519
            FTU: FTT0055(rluC) FTT1021c(truA) FTT1056c(rluB) FTT1245(rluD)
                 FTT1554c(truB)
            FTF: FTF0055(rluC) FTF1021c(truA) FTF1056c(rluB) FTF1245(rluD)
                 FTF1554c(truB)
            FTW: FTW_0131(rluC) FTW_0373(truB) FTW_0928(truA) FTW_0966
            FTL: FTL_0555 FTL_0699 FTL_1030 FTL_1068 FTL_1804
            FTH: FTH_0556(truB) FTH_0701(rluD) FTH_1006(rluB) FTH_1044(truA)
                 FTH_1741(rluC)
            FTA: FTA_1127(truA)
            FTN: FTN_0899(truA) FTN_0945(rsuA) FTN_1264(rluD) FTN_1462(truB)
                 FTN_1655(rluC)
            TCX: Tcr_0216 Tcr_0279 Tcr_0655 Tcr_0704 Tcr_0801 Tcr_0944
                 Tcr_1100 Tcr_1125 Tcr_1228 Tcr_1370
            NOC: Noc_0856(glu) Noc_1018 Noc_1041 Noc_2118 Noc_2550(rluD)
                 Noc_2844
            AEH: Mlg_1089 Mlg_1234 Mlg_1835 Mlg_1946 Mlg_1955 Mlg_2552
            HHA: Hhal_0581 Hhal_1433 Hhal_1747 Hhal_1806 Hhal_2235
            HCH: HCH_01241(truB) HCH_01871 HCH_02136(rluC) HCH_02335(rsuA)
                 HCH_02434(truA) HCH_04661 HCH_04736 HCH_05780 HCH_05920
            CSA: Csal_0497 Csal_0851 Csal_1259 Csal_1593 Csal_1950 Csal_2442
                 Csal_2636 Csal_2894 Csal_3072
            ABO: ABO_0331(truB) ABO_0476(rluD) ABO_1061(rluC) ABO_1098(rsuA)
                 ABO_1168 ABO_1194(rluA) ABO_1280 ABO_1387 ABO_1463(truA)
                 ABO_2537(rsuA)
            MMW: Mmwyl1_2040
            AHA: AHA_0825(truD) AHA_0863 AHA_1164 AHA_1417 AHA_1628 AHA_2240
                 AHA_2680(truA) AHA_2851 AHA_2917 AHA_3301 AHA_4073
            ASA: ASA_2531(truA)
            BCI: BCI_0193(rluD) BCI_0364(truA) BCI_0439(rluC) BCI_0629(truB)
            CRP: CRP_128
            RMA: Rmag_0056 Rmag_0329 Rmag_0984
            NME: NMB0198 NMB0704 NMB0806 NMB1298 NMB1361 NMB1374 NMB1496
                 NMB2036
            NMA: NMA0070(rluC) NMA0402(truA) NMA0908(rluD) NMA1016 NMA1508
                 NMA1573 NMA1588(truB)
            NMC: NMC0654(rluD) NMC0757 NMC1296 NMC1309(truB) NMC2017(truA)
            NGO: NGO0278(rluD) NGO0389 NGO0607 NGO0642 NGO0657 NGO1783(rluC)
                 NGO1811(truA)
            CVI: CV_0389(rsuA) CV_1464(truB) CV_1818(rluC) CV_2192(rluD)
                 CV_2346 CV_2406 CV_2764(truA) CV_3386 CV_3663 CV_3751(rluA)
            RSO: RSc0674(rsuA) RSc1041(rluC) RSc1286(RS02799) RSc1291(truB)
                 RSc1401(RS05291) RSc1628(rluD) RSc1985(truA)
            REU: Reut_A0704 Reut_A1344(rluD) Reut_A1884 Reut_A2026 Reut_A2031
                 Reut_A2274(rluD) Reut_A2308 Reut_A2757
            REH: H16_A2058(rsuA1) H16_A2309 H16_A2578(rluA2) H16_A2616(truA1)
            RME: Rmet_1353 Rmet_1432 Rmet_2029 Rmet_2034 Rmet_2439 Rmet_2469
                 Rmet_2744 Rmet_2896
            BMA: BMA0485 BMA0521(rluC) BMA1059(truB) BMA1064 BMA1324(rluD)
                 BMA1558 BMA1964(rsuA) BMAA1723(truA)
            BMV: BMASAVP1_1647(truA) BMASAVP1_A0685 BMASAVP1_A1505(truB)
                 BMASAVP1_A1510 BMASAVP1_A2060
            BML: BMA10299_1856(truA) BMA10299_A0173(truB) BMA10299_A0178
                 BMA10299_A1014 BMA10299_A3251
            BMN: BMA10247_0134 BMA10247_0988 BMA10247_0993(truB) BMA10247_1332
                 BMA10247_A0527(truA)
            BXE: Bxe_A0796 Bxe_A0832 Bxe_A1063 Bxe_A1678 Bxe_A2346 Bxe_A2818
                 Bxe_A2823 Bxe_B2883
            BVI: Bcep1808_1468 Bcep1808_4460
            BUR: Bcep18194_A4224(rluD) Bcep18194_A4638 Bcep18194_A4643
                 Bcep18194_A5094(rluD) Bcep18194_A5332 Bcep18194_A5819
                 Bcep18194_A5857 Bcep18194_B2127
            BCN: Bcen_0632 Bcen_1016 Bcen_1022 Bcen_1876 Bcen_1914 Bcen_4411
                 Bcen_6055 Bcen_6286
            BCH: Bcen2424_1112 Bcen2424_1497 Bcen2424_1502 Bcen2424_2022
                 Bcen2424_2487 Bcen2424_2525 Bcen2424_3956
            BAM: Bamb_0988 Bamb_1379 Bamb_1384 Bamb_2055 Bamb_2534 Bamb_2573
                 Bamb_3346
            BPS: BPSL0895 BPSL0930 BPSL1532 BPSL1916(truB) BPSL1921 BPSL2162
                 BPSL2451(rluC) BPSS1701(truA)
            BPM: BURPS1710b_1107 BURPS1710b_1153(rsuA) BURPS1710b_1912
                 BURPS1710b_1917 BURPS1710b_2333(rluD) BURPS1710b_2586(rsuA)
                 BURPS1710b_2917(rluC) BURPS1710b_A0771(truA)
            BPL: BURPS1106A_0958 BURPS1106A_1759 BURPS1106A_1764(truB)
                 BURPS1106A_2497 BURPS1106A_A2309(truA)
            BPD: BURPS668_0954 BURPS668_1737 BURPS668_1742(truB) BURPS668_2440
                 BURPS668_A2447(truA)
            BTE: BTH_I0758 BTH_I0795 BTH_I1708 BTH_I2024 BTH_I2253 BTH_I2562
                 BTH_I2567 BTH_II0677(truA)
            PNU: Pnuc_0770 Pnuc_1225 Pnuc_1230 Pnuc_2035
            BPE: BP0477(rluC) BP0982 BP1147(rluD) BP1244 BP1249(truB)
                 BP1486(truA)
            BPA: BPP1451 BPP1859 BPP1864(truB) BPP1947(truA) BPP3198(rluD)
                 BPP3317(rluC)
            BBR: BB2135(truA) BB2525 BB3244(truB) BB3249 BB3598(rluD)
                 BB3768(rluC)
            RFR: Rfer_1721 Rfer_1790 Rfer_2136 Rfer_2312 Rfer_2314 Rfer_2765
                 Rfer_2976 Rfer_3457 Rfer_3544
            POL: Bpro_0606 Bpro_1128 Bpro_1800 Bpro_2428 Bpro_2613 Bpro_2615
                 Bpro_3457 Bpro_3614 Bpro_3659
            PNA: Pnap_1335 Pnap_1867 Pnap_2009 Pnap_2786 Pnap_3044 Pnap_3362
                 Pnap_3595
            AAV: Aave_0792 Aave_1174 Aave_1217 Aave_1419 Aave_2287 Aave_4291
            AJS: Ajs_0474 Ajs_1165 Ajs_2497 Ajs_3237 Ajs_3692
            VEI: Veis_0085 Veis_0485 Veis_1889 Veis_4870
            MPT: Mpe_A2001 Mpe_A2033
            HAR: HEAR1067 HEAR1221(truA) HEAR1332 HEAR2087(rluC)
                 HEAR2431(truB) HEAR2438
            NEU: NE0005 NE0435 NE0505(rluD) NE0691 NE0763 NE1456(rluC)
            NET: Neut_0005 Neut_0592 Neut_1150 Neut_1230 Neut_1644 Neut_2203
            NMU: Nmul_A0263 Nmul_A1065(rluD) Nmul_A1855 Nmul_A1862 Nmul_A1914
                 Nmul_A1976(rluD)
            EBA: ebA2976(rsuA) ebA4056(rsuA) ebA4725(rluD) ebA4770(truA)
                 ebA5443(rluC) ebA5843(truB) ebA6135(rsuA) ebA713
            AZO: azo0828 azo1018(rluD) azo1045 azo1101 azo1614(rluC)
                 azo1862(rluA2) azo2105(truB) azo2110
            DAR: Daro_0016 Daro_0868 Daro_1604(rluD) Daro_2006(rluD) Daro_2450
                 Daro_2455 Daro_2869 Daro_3254 Daro_3468 Daro_4154
            TBD: Tbd_0435 Tbd_0658 Tbd_0695 Tbd_0779 Tbd_0810(rluD) Tbd_0853
                 Tbd_1258 Tbd_1563(rluD) Tbd_1916
            MFA: Mfla_0069 Mfla_0955 Mfla_1099 Mfla_1322 Mfla_1612 Mfla_1700
                 Mfla_1872 Mfla_2138 Mfla_2529
            HPY: HP0361(hisT) HP0745 HP0926 HP1459
            HPJ: jhp0682 jhp0860 jhp1019(truA) jhp1352
            HPA: HPAG1_0730 HPAG1_0907 HPAG1_1032 HPAG1_1456
            HHE: HH0124(truB) HH0601(truA) HH0717 HH0783 HH1515(glu)
            HAC: Hac_0125(yciL) Hac_0414(truA) Hac_0673 Hac_1089
            WSU: WS0143 WS0676(truA) WS0878(truB) WS1227 WS1979
            TDN: Tmden_0212 Tmden_0438 Tmden_0611 Tmden_0783 Tmden_0994
                 Tmden_1032 Tmden_2010
            CJE: Cj0827(truA) Cj1102(truB) Cj1280c Cj1457c Cj1709c
            CJR: CJE0914(truA) CJE1245(truB) CJE1416 CJE1631 CJE1878
            CJJ: CJJ81176_1450
            CJU: C8J_0774(truA) C8J_1043(truB) C8J_1224 C8J_1363 C8J_1613
            CFF: CFF8240_0747(truA)
            CCV: CCV52592_1426(truA)
            CHA: CHAB381_0973
            CCO: CCC13826_0699(truA)
            GSU: GSU0082(rluD) GSU0520 GSU0671(rluC) GSU1403(rluB)
                 GSU1591(truB) GSU2877(truA) GSU3160
            GME: Gmet_0267 Gmet_0605 Gmet_1217 Gmet_1589 Gmet_2838 Gmet_3033
                 Gmet_3435
            GUR: Gura_1048
            PCA: Pcar_0760 Pcar_1301 Pcar_1559 Pcar_1901 Pcar_2357 Pcar_2950
            PPD: Ppro_2070
            DVU: DVU0505(truB) DVU0911(truA) DVU1024(rluD) DVU1669(rluB)
                 DVU3191(rluC)
            DVL: Dvul_1418
            DDE: Dde_0120 Dde_0975 Dde_1447(rluD) Dde_1958 Dde_2707 Dde_3165
            LIP: LI0715(rluD) LI0813(rluD) LI0868(rluB) LI1005(truB)
                 LI1062(truA)
            BBA: Bd0491(truA) Bd1519 Bd1549(truB) Bd1793(rluC) Bd1967(rsuA2)
                 Bd3264 Bd3791(rluD)
            DPS: DP0459 DP0819 DP0820 DP1324 DP2356 DP2610 DP2730 DP3109
            ADE: Adeh_0056 Adeh_0265 Adeh_0381 Adeh_1105 Adeh_1544 Adeh_1682
                 Adeh_1901 Adeh_3643
            AFW: Anae109_2269 Anae109_4191
            MXA: MXAN_1586 MXAN_2071(truB) MXAN_3352 MXAN_3839(rluB)
                 MXAN_5115(truA) MXAN_5195(truD) MXAN_6019(rluA)
            SAT: SYN_01395 SYN_01783 SYN_01800 SYN_02701 SYN_02856
            SFU: Sfum_0683 Sfum_1232 Sfum_1666 Sfum_3657
            RPR: RP258 RP501(truB) RP502 RP544 RP846(sfhB) RP857(truA)
            RTY: RT0249(rluC) RT0487(truB) RT0532(rluB) RT0834(rluD)
                 RT0846(truA)
            RCO: RC0344(rluC) RC0665(truB) RC0807(rluB) RC1310(sfhB)
                 RC1328(truA)
            RFE: RF_0723(truB) RF_0863(rluA2) RF_1023(rluA1) RF_1341 RF_1343
                 RF_1356(truA)
            RBE: RBE_0060(truA) RBE_0256(rluA1) RBE_0321(rluA2) RBE_0771(truB)
                 RBE_1246
            RAK: A1C_06640(truA)
            RBO: A1I_00590(truA)
            RCM: A1E_05490(truA)
            RRI: A1G_07265(truA)
            WOL: WD0415 WD1068(truA) WD1162
            WBM: Wbm0206 Wbm0428
            AMA: AM474(rluC) AM524(truB) AM661(truA) AM825(sfhB)
            APH: APH_0362 APH_0502(truA) APH_0549(rluC) APH_0769(truB)
            ERU: Erum3210(rluC) Erum3520(truB) Erum4240(truA) Erum5330(rluD)
            ERW: ERWE_CDS_03270(rluC) ERWE_CDS_03590(truB)
                 ERWE_CDS_04410(truA) ERWE_CDS_05590(sfhB)
            ERG: ERGA_CDS_03220(rluC) ERGA_CDS_03550(truB)
                 ERGA_CDS_04360(truA) ERGA_CDS_05480(sfhB)
            ECN: Ecaj_0303(rluD) Ecaj_0336 Ecaj_0419 Ecaj_0540(rluD)
            ECH: ECH_0486 ECH_0622(truA) ECH_0728(truB) ECH_0774(rluC)
            NSE: NSE_0020(truA) NSE_0101(truB) NSE_0146 NSE_0556(rluC)
            PUB: SAR11_0458(truA) SAR11_0607(sfhB) SAR11_1091(rluC)
            MLO: mll4852 mlr0334 mlr2177 mlr3740 mlr5558 mlr8253
            MES: Meso_0391 Meso_0428 Meso_1648 Meso_3146 Meso_3932
            PLA: Plav_0263
            SME: SMb20024 SMc00321(truB) SMc00647(rluD) SMc00904
                 SMc01099(truA) SMc01275(rluC)
            SMD: Smed_0056
            ATU: Atu0085(truB) Atu0368(truA) Atu0689(rluB) Atu1471(rluC)
                 Atu2443(rluD) Atu4041(rluA)
            ATC: AGR_C_1238 AGR_C_127 AGR_C_2714 AGR_C_4432 AGR_C_644
                 AGR_L_1625
            RET: RHE_CH00114(truB) RHE_CH00415(truA) RHE_CH00835(rluB)
                 RHE_CH02236(rluC) RHE_CH03341(rluD) RHE_CH03406
            RLE: RL0123(truB) RL0434(truA) RL0892 RL2567(rLuC) RL3765(rLuD)
                 RL3869(rLuB)
            BME: BMEI0377 BMEI0983 BMEI1963 BMEII0266 BMEII1039
            BMF: BAB1_1019 BAB1_1666 BAB1_2167 BAB2_0198 BAB2_0995
            BMS: BR1000(rluC) BR1651 BR2167(truB)
            BMB: BruAb1_1005 BruAb1_1639 BruAb1_2140(truB) BruAb2_0201
                 BruAb2_0973(truA)
            BOV: BOV_A0974(truA)
            OAN: Oant_1346
            BJA: bll0781(truB) bll5366 bll7495 bll8107(truA) blr7336
            BRA: BRADO0772(truA) BRADO6081
            BBT: BBta_7335(truA)
            RPA: RPA0368(rluD) RPA0434(truB) RPA0623(truA) RPA1165
                 RPA3208(rluC)
            RPB: RPB_0454(rluD) RPB_0603 RPB_0675 RPB_1171 RPB_2335(rluD)
            RPC: RPC_0482 RPC_0606 RPC_0807 RPC_0907 RPC_3403
            RPD: RPD_0079 RPD_0229 RPD_0359 RPD_1273 RPD_3129
            RPE: RPE_0194 RPE_0654 RPE_0817 RPE_0930 RPE_3547
            NWI: Nwi_0026(truB) Nwi_1394(rluD) Nwi_2431(rluD) Nwi_2550
                 Nwi_3066(truA)
            NHA: Nham_0033 Nham_1575 Nham_2859 Nham_3171 Nham_3695
            BHE: BH00740(truA) BH02130(truB) BH02610 BH03820(rluD)
                 BH10200(rluC)
            BQU: BQ00670(truA) BQ02010(truB) BQ02470 BQ02830(rluD)
                 BQ07920(rluC)
            BBK: BARBAKC583_1210 BARBAKC583_1321(truA)
            XAU: Xaut_3303
            CCR: CC_0036 CC_0230 CC_0278 CC_0453 CC_0855 CC_1284 CC_1838
                 CC_1980
            SIL: SPO0516(rluC) SPO1408(rluD) SPO2124 SPO2984 SPO3143(truA)
                 SPO3392(rluA) SPO3837(truB)
            SIT: TM1040_0072 TM1040_0084 TM1040_0291 TM1040_1161 TM1040_1927
                 TM1040_2118 TM1040_2384
            RSP: RSP_0571 RSP_1108(truB) RSP_1506 RSP_1745 RSP_2266(rluB)
                 RSP_2409(rluD)
            RSH: Rsph17029_0940 Rsph17029_2224
            RSQ: Rsph17025_0502
            JAN: Jann_0624 Jann_1217 Jann_1685 Jann_3401 Jann_3462 Jann_4024
                 Jann_4034
            RDE: RD1_0016(rluA) RD1_0647(truB) RD1_1441(rluC) RD1_1813(rluD)
                 RD1_1992 RD1_2070(truA) RD1_2753
            PDE: Pden_0534 Pden_4142
            MMR: Mmar10_0447 Mmar10_0618 Mmar10_0793 Mmar10_1763 Mmar10_2406
                 Mmar10_3048
            HNE: HNE_0117(truB) HNE_0515(truA) HNE_0755(rsuA) HNE_0940
                 HNE_1002 HNE_1378 HNE_1844
            ZMO: ZMO0439(rluC) ZMO0505(rluC) ZMO0551(rulB) ZMO0750(rluD)
                 ZMO0810(rulA)
            NAR: Saro_1297 Saro_2484 Saro_2837 Saro_2893 Saro_3046 Saro_3113
            SAL: Sala_0248 Sala_0541 Sala_1058 Sala_1742 Sala_2102 Sala_2302
            SWI: Swit_4041
            ELI: ELI_01180 ELI_01345 ELI_02060 ELI_03525 ELI_07615
            GOX: GOX0505 GOX0801 GOX1584 GOX1665 GOX1834
            GBE: GbCGDNIH1_0459 GbCGDNIH1_0582 GbCGDNIH1_0690 GbCGDNIH1_0849
                 GbCGDNIH1_2353
            ACR: Acry_0411
            RRU: Rru_A0652 Rru_A1111 Rru_A1939 Rru_A2659 Rru_A3352 Rru_A3783
            MAG: amb0241 amb2472 amb2477 amb3186 amb4115 amb4126
            MGM: Mmc1_0138 Mmc1_1038 Mmc1_2098 Mmc1_3724
            ABA: Acid345_1444 Acid345_1630 Acid345_2203 Acid345_3345
                 Acid345_3863
            SUS: Acid_6491
            BSU: BG10271(truB) BG10530(rluB) BG11796(ylyB) BG11992(truA)
                 BG13144(yjbO) BG13940(ytzF)
            BHA: BH0167(truA) BH1576(rluB) BH2410(truB) BH2542 BH2847 BH3273
            BAA: BA_0725 BA_1062 BA_1749 BA_1831 BA_2017 BA_2880 BA_4418
                 BA_4502 BA_5219 BA_5376
            BAT: BAS0142 BAS0462 BAS1121 BAS1206 BAS1382 BAS2221 BAS3661
                 BAS3743 BAS4446 BAS4602
            BCE: BC0163 BC0471 BC1200 BC1293 BC1472 BC2321 BC3808 BC3892
                 BC4551 BC4704
            BCA: BCE_0142(truA) BCE_0543(truA) BCE_1322 BCE_1405
                 BCE_1597(rluB) BCE_2417 BCE_3848(truB) BCE_3937 BCE_4674
                 BCE_4848
            BCZ: BCZK0135(truA) BCZK0401(truA) BCZK1097(rluD) BCZK1186(rluD)
                 BCZK1354(rluB) BCZK2144 BCZK3569(truB) BCZK3651(rluD)
                 BCZK4295(truA) BCZK4456
            BCY: Bcer98_0136 Bcer98_0421
            BTK: BT9727_0137(truA) BT9727_0405(truA) BT9727_1103(rluD)
                 BT9727_1184(rluD) BT9727_1355(rluB) BT9727_2160
                 BT9727_3551(truB) BT9727_3634(rluD) BT9727_4284 BT9727_4438
            BTL: BALH_0140(truA) BALH_0426(truA) BALH_1155 BALH_1329(rluB)
                 BALH_2124 BALH_3438 BALH_3523(rluD) BALH_4134 BALH_4280
            BLI: BL00034(ytzF) BL00662(rluB) BL01010(yjbO) BL01020(truA)
                 BL01222(truB) BL02270
            BLD: BLi00166(truA) BLi01256(yjbO) BLi01766(ylyB) BLi01891(truB)
                 BLi02462(rluB) BLi03154
            BCL: ABC0182(truA) ABC1831(rluB) ABC2225(truB) ABC2339 ABC2518
                 ABC2798
            BPU: BPUM_0135(truA)
            OIH: OB0150 OB1222 OB1486 OB1601(truB) OB1823 OB2299
            GKA: GK0138 GK0565 GK0831 GK1146 GK1266 GK2283 GK2833
            GTN: GTNG_0136 GTNG_0508 GTNG_1120
            SAU: SA0866 SA1040 SA1114(truB) SA1324(rluB) SA1574 SA1668
                 SA2018(truA)
            SAV: SAV1008 SAV1197 SAV1271(truB) SAV1493(rluB) SAV1753 SAV1850
                 SAV2219(truA)
            SAM: MW0889 MW1080 MW1154(truB) MW1447(rluB) MW1696 MW1791
                 MW2138(truA)
            SAR: SAR0975 SAR1173 SAR1247 SAR1569(rluB) SAR1838 SAR1941 SAR2302
            SAS: SAS0877 SAS1131 SAS1205 SAS1433 SAS1679 SAS1771 SAS2110
            SAC: SACOL1012 SACOL1209 SACOL1290(truB) SACOL1536(rluB) SACOL1803
                 SACOL1907 SACOL2208(truA)
            SAB: SAB0874 SAB1061 SAB1133(truB) SAB1354c(rluB) SAB1613c SAB1783
                 SAB2092c
            SAA: SAUSA300_0909 SAUSA300_1090 SAUSA300_1164(truB)
                 SAUSA300_1443(rluB) SAUSA300_1699 SAUSA300_1800
                 SAUSA300_2173(truA)
            SAO: SAOUHSC_00944 SAOUHSC_01163 SAOUHSC_01248 SAOUHSC_01587
                 SAOUHSC_01870 SAOUHSC_01982 SAOUHSC_02480
            SAJ: SaurJH9_2246
            SAH: SaurJH1_2287
            SEP: SE0697 SE0872 SE0948 SE1177 SE1426 SE1531 SE1792
            SER: SERP0588 SERP0763 SERP0838(truB) SERP1056(rluB) SERP1312
                 SERP1386 SERP1800(truA)
            SHA: SH0834(truA) SH1112 SH1169(rsuA) SH1423(rluB) SH1642(truB)
                 SH1717 SH1950
            SSP: SSP0694 SSP0945 SSP1010 SSP1259 SSP1494 SSP1575 SSP1777
            LMO: lmo0969 lmo1328(truB) lmo1843 lmo1949 lmo2244 lmo2342
                 lmo2598(truA)
            LMF: LMOf2365_0989 LMOf2365_1345(truB) LMOf2365_1871
                 LMOf2365_1979(rluB) LMOf2365_2277 LMOf2365_2312(rsuA)
                 LMOf2365_2571(truA)
            LIN: lin0968 lin1365(truB) lin1957 lin2063 lin2346 lin2436
                 lin2747(truA)
            LWE: lwe0951 lwe1343(truB) lwe1862(rluD) lwe1975(rluB) lwe2261
                 lwe2294(rsuA) lwe2548(truA)
            LLA: L0328(truB) L0331(truA) L107724(rluB) L109527(rsuA)
                 L164789(rluA) L167555(rluE) L189881(rluC) L25787(rluD)
            LLC: LACR_0410 LACR_0491 LACR_1082 LACR_1237 LACR_1396 LACR_1484
                 LACR_2414 LACR_2545
            LLM: llmg_0462(truA) llmg_1100(rluC) llmg_1194(rluB)
                 llmg_1431(truB) llmg_2396(rluA) llmg_2518
            SPY: SPy_0369 SPy_0827 SPy_1127 SPy_1251(truB) SPy_1337(rsuA)
                 SPy_1398 SPy_1901(truA) SPy_2063
            SPZ: M5005_Spy_0310 M5005_Spy_0638 M5005_Spy_0849
                 M5005_Spy_0961(truB) M5005_Spy_1092(rsuA) M5005_Spy_1138
                 M5005_Spy_1617(truA) M5005_Spy_1756
            SPM: spyM18_0418 spyM18_0889(sfhB) spyM18_1088 spyM18_1200(truB)
                 spyM18_1351 spyM18_1406 spyM18_1966(truA) spyM18_2124
            SPG: SpyM3_0269 SpyM3_0557 SpyM3_0786(rluD) SpyM3_0887(truB)
                 SpyM3_1018(rsuA) SpyM3_1064 SpyM3_1639(truA) SpyM3_1761
            SPS: SPs0227 SPs0799 SPs0842 SPs0987 SPs1087 SPs1297 SPs1590
                 SPs1758
            SPH: MGAS10270_Spy0305 MGAS10270_Spy0694 MGAS10270_Spy0965
                 MGAS10270_Spy1076(truB) MGAS10270_Spy1149(rsuA)
                 MGAS10270_Spy1208 MGAS10270_Spy1685 MGAS10270_Spy1825
            SPI: MGAS10750_Spy0304 MGAS10750_Spy0727 MGAS10750_Spy1000
                 MGAS10750_Spy1112(truB) MGAS10750_Spy1191(rsuA)
                 MGAS10750_Spy1245 MGAS10750_Spy1672 MGAS10750_Spy1850
            SPJ: MGAS2096_Spy0327 MGAS2096_Spy0704 MGAS2096_Spy0705
                 MGAS2096_Spy0925 MGAS2096_Spy1021(truB) MGAS2096_Spy1094(rsuA)
                 MGAS2096_Spy1204 MGAS2096_Spy1641 MGAS2096_Spy1791
            SPK: MGAS9429_Spy0309 MGAS9429_Spy0693 MGAS9429_Spy0968
                 MGAS9429_Spy1065(truB) MGAS9429_Spy1135(rsuA) MGAS9429_Spy1185
                 MGAS9429_Spy1620 MGAS9429_Spy1766
            SPF: SpyM50237(truA) SpyM50837(truB) SpyM51717
            SPA: M6_Spy0336 M6_Spy0656 M6_Spy0847 M6_Spy0951 M6_Spy1064
                 M6_Spy1113 M6_Spy1625 M6_Spy1756
            SPB: M28_Spy0299 M28_Spy0618 M28_Spy0825 M28_Spy0934(truB)
                 M28_Spy1073(rsuA) M28_Spy1132 M28_Spy1606(truA) M28_Spy1742
            SPN: SP_0280 SP_0680 SP_0929 SP_1099 SP_1212 SP_1599 SP_1874
                 SP_2011
            SPR: spr0256(rsuA) spr0597(rsuA) spr0830(rluD) spr1006(rluD)
                 spr1092(truB) spr1451(truA) spr1689(rluB) spr1824(rluD)
            SPD: SPD_0260(rsuA-1) SPD_1070(truB) SPD_1424(truA) SPD_1654(rluB)
                 SPD_1822
            SAG: SAG0100(truA) SAG0801 SAG0998(truB) SAG1093 SAG1365
                 SAG1475(rsuA) SAG1593(rluB) SAG2067
            SAN: gbs0099 gbs0821 gbs1033(truB) gbs1160 gbs1435 gbs1541 gbs1642
                 gbs2021
            SAK: SAK_0150(truA) SAK_0926 SAK_1093(truB) SAK_1178 SAK_1398
                 SAK_1505 SAK_1608(rluB) SAK_2006
            SMU: SMU.1044c SMU.1144(truB) SMU.1711(rluB) SMU.1950 SMU.638
                 SMU.84(truA) SMU.854
            STC: str0122(truA) str0211 str0262(rluB) str0522(rluD)
                 str0553(rsuA1) str0995(truB) str1456 str1505(rsuA2)
            STL: stu0122(truA) stu0211 stu0262(rluB) stu0522(rluD)
                 stu0553(rsuA1) stu0995(truB) stu1456 stu1505(rsuA2)
            STE: STER_0165 STER_0259 STER_0309 STER_1000 STER_1466
            SSA: SSA_0935(truB) SSA_1777(rluB) SSA_2002(truA) SSA_2059
                 SSA_2210
            SSU: SSU05_0311 SSU05_1114 SSU05_1987
            SSV: SSU98_0307 SSU98_1992
            LPL: lp_0963(rluE) lp_1076(truA) lp_1319(rsuA) lp_1781(rluD1)
                 lp_1888(rluB) lp_2032(truB) lp_2221(rluD2) lp_2653(rluA)
            LJO: LJ0366 LJ0825 LJ0955 LJ1086 LJ1186 LJ1485 LJ1679
            LAC: LBA0322 LBA0648(rluD) LBA0791 LBA0964(rluB) LBA1151
                 LBA1253(truB) LBA1594
            LSA: LSA0620(rluA1) LSA0949(rluA2) LSA1024(rsuA1) LSA1242(truB)
                 LSA1316(rluA3) LSA1431(rsuA2) LSA1442(rluA4) LSA1723(truA)
            LSL: LSL_0445(rsuA) LSL_0574(truB) LSL_0826(rluD) LSL_0938(rluB)
                 LSL_1303(rluD) LSL_1404(truA) LSL_1457(rluD) LSL_1482(rluD)
            LDB: Ldb0427(truA) Ldb0586 Ldb0726(rsuA) Ldb0847(rluB) Ldb1022
                 Ldb1330(truB) Ldb1543
            LBU: LBUL_0381 LBUL_0521 LBUL_0658 LBUL_0771 LBUL_0930 LBUL_1239
                 LBUL_1432
            LBR: LVIS_0168 LVIS_0771 LVIS_0832 LVIS_1057 LVIS_1333 LVIS_1471
                 LVIS_1659 LVIS_1736
            LCA: LSEI_0886 LSEI_0903 LSEI_1372 LSEI_1458 LSEI_1570 LSEI_1726
                 LSEI_1849 LSEI_2471 LSEI_2558
            LGA: LGAS_0321 LGAS_0816 LGAS_0888 LGAS_1222 LGAS_1453
            LRE: Lreu_1452
            PPE: PEPE_0354 PEPE_0647 PEPE_0892 PEPE_1084 PEPE_1387
            OOE: OEOE_0176 OEOE_0626 OEOE_1006 OEOE_1079 OEOE_1158 OEOE_1313
            LME: LEUM_0046 LEUM_0228 LEUM_1296 LEUM_1351
            STH: STH1243 STH1525 STH1527 STH1783 STH1891
            CAC: CAC1015 CAC1266 CAC1805(truB) CAC1851 CAC2114 CAC2676
                 CAC3099(truA)
            CPE: CPE0991(truA) CPE1080 CPE1204 CPE1683(truB) CPE1850 CPE2122
                 CPE2264 CPE2313 CPE2371(truA)
            CPF: CPF_1151 CPF_1336(rluB) CPF_1937(truB) CPF_2104 CPF_2377
                 CPF_2546 CPF_2613 CPF_2680(truA)
            CPR: CPR_0987 CPR_1060(truA) CPR_1147(rluB) CPR_1224 CPR_1655
                 CPR_2089 CPR_2249 CPR_2299 CPR_2365(truA)
            CTC: CTC00155 CTC00986 CTC01278 CTC01319 CTC01614 CTC01851
                 CTC02052 CTC02399 CTC02573
            CNO: NT01CX_0072 NT01CX_0437 NT01CX_1149(truA) NT01CX_1440
                 NT01CX_1631 NT01CX_1952 NT01CX_2092 NT01CX_2133
                 NT01CX_2290(truA)
            CTH: Cthe_0693 Cthe_0988 Cthe_2939 Cthe_3161
            CDF: CD0405 CD1784(truA2) CD2050(rluB)
            CBA: CLB_1851(truA-1) CLB_2279(truB) CLB_3503(truA-2)
            CBH: CLC_1858(truA-1) CLC_2262(truB) CLC_3391(truA-2)
            CBF: CLI_1978(truA-1) CLI_2471(truB) CLI_3629(truA-2)
            CBE: Cbei_0185
            CKL: CKL_0257(truA)
            AMT: Amet_2332 Amet_4444 Amet_4634
            CHY: CHY_1505 CHY_1531(rsuA) CHY_1763(truB) CHY_1938(rluB)
                 CHY_2276(truA)
            DSY: DSY0516 DSY1290 DSY2280 DSY2514 DSY2865
            DRM: Dred_0255
            PTH: PTH_0355(truA)
            SWO: Swol_0903 Swol_1286 Swol_1406 Swol_2299
            CSC: Csac_1765
            TTE: TTE0052(rsuA) TTE1332(rsuA2) TTE1390(truB) TTE1538(rluA)
                 TTE2258(truA)
            MTA: Moth_0869(rluD) Moth_1053 Moth_1352 Moth_1744 Moth_2426
            MGE: MG_182(trua) MG_209 MG_370
            MPN: MPN196(hisT) MPN292(yceC)
            MPU: MYPU_1170(rluC) MYPU_2980(rluD) MYPU_3370(rluB)
                 MYPU_5500(truB)
            MPE: MYPE9280(truB) MYPE9740(hisT)
            MGA: MGA_0831(truB) MGA_0996(rluA) MGA_1331d(truA)
            MMY: MSC_0336(truB) MSC_0387(rluB) MSC_0583(rluD) MSC_0715(truA)
                 MSC_0766(rluC)
            MMO: MMOB3260(rluD) MMOB4660(truB) MMOB4750(rluC)
            MHY: mhp015(rluC) mhp104(truB) mhp215 mhp457(rluD)
            MHJ: MHJ_0015(rluC) MHJ_0162(rluB) MHJ_0268(truB) MHJ_0455(rluD)
            MHP: MHP7448_0015(rluC) MHP7448_0166(rluB) MHP7448_0276(truB)
                 MHP7448_0458(rluD)
            MSY: MS53_0094(rluC) MS53_0318(rluB) MS53_0417(rsuA)
                 MS53_0565(truB) MS53_0595(rluD)
            MCP: MCAP_0326 MCAP_0395 MCAP_0600 MCAP_0665 MCAP_0714
            UUR: UU313(rluD) UU354(truB) UU536(hisT)
            POY: PAM131(rluA) PAM229(truA) PAM237(truB) PAM238(rsuA)
            AYW: AYWB_483(rsuA) AYWB_484(truB) AYWB_493(truA) AYWB_590(rluA)
            MFL: Mfl155 Mfl282 Mfl387 Mfl548 Mfl563
            MTU: Rv1540 Rv1711 Rv2793c Rv3455c(truA)
            MTC: MT1592 MT1751.1 MT2862.1(truB) MT3562(truA)
            MBO: Mb1567 Mb1738 Mb2816c(truB) Mb3484c(truA)
            MBB: BCG_1750
            MLE: ML1200 ML1370 ML1546(truB) ML1955(truA)
            MPA: MAP1251 MAP1413 MAP2898c(truB) MAP4235(truA)
            MAV: MAV_3065 MAV_4395(truA)
            MSM: MSMEG_1527(truA) MSMEG_2649(truB) MSMEG_3175 MSMEG_3740(rluB)
            MUL: MUL_3234
            MVA: Mvan_3276
            MMC: Mmcs_1115 Mmcs_2095 Mmcs_2929 Mmcs_3092
            MKM: Mkms_2973
            MJL: Mjls_2944
            CGL: NCgl0310(cgl0316) NCgl0542(truA) NCgl1371(cgl1426)
                 NCgl1904(truB) NCgl2057(cgl2138)
            CGB: cg0384(rluC1) cg0657(truA) cg1615 cg2170(truB) cg2346(rluD)
            CEF: CE0328 CE0574 CE1559 CE1872 CE2032
            CDI: DIP0551(truA) DIP1195 DIP1471(truB) DIP1583(rluC)
            CJK: jk0766(rluD) jk0877 jk1137(truB) jk1755(truA) jk1873(rluC)
            NFA: nfa17870 nfa20110 nfa40530(truB) nfa8390(truA)
            RHA: RHA1_ro00925
            SCO: SCO1768(SCI51.08c) SCO2073(SC4A10.06c) SCO4731(SC6G4.09)
                 SCO5709(SC9F2.07c)
            SMA: SAV2548(truB) SAV4955(truA) SAV6133 SAV6512(rluB)
            TWH: TWT087(truB) TWT511 TWT526(truA)
            TWS: TW097(truB) TW234(truA) TW251
            LXX: Lxx05710(rsuA) Lxx07250(truB) Lxx15170(rlu) Lxx20040(truA)
            ART: Arth_1534
            AAU: AAur_1672
            PAC: PPA0768 PPA1385 PPA1478 PPA1809
            TFU: Tfu_0781 Tfu_1123(rluD) Tfu_1206 Tfu_2616
            FRA: Francci3_0612 Francci3_1426(rluD) Francci3_1454 Francci3_3558
            FAL: FRAAL1112(truA) FRAAL2209(rluD) FRAAL2251(rluB)
                 FRAAL5756(rluA)
            ACE: Acel_0336 Acel_1032 Acel_1236 Acel_1512
            KRA: Krad_0717
            SEN: SACE_5237 SACE_5823(rlu) SACE_6801(truA)
            STP: Strop_1928 Strop_3893
            BLO: BL0123 BL0737(rluB) BL1608(truA) BL1618(truB)
            BAD: BAD_0349(truA) BAD_0356(truB) BAD_1131
            RXY: Rxyl_1415 Rxyl_1442 Rxyl_1482 Rxyl_2123
            FNU: FN0635 FN0651 FN0717 FN0756 FN1372 FN1600
            RBA: RB12885(rluD) RB2141(rluA) RB2676(truA) RB3174 RB3266(rluD)
                 RB6411(truB)
            CTR: CT094(truB) CT106(yceC) CT463(truA) CT658(sfhB) CT723(yjbC)
            CTA: CTA_0099(truB_1) CTA_0100(truB_2) CTA_0113(yceC)
                 CTA_0506(truA) CTA_0715(sfhB) CTA_0785(yjbC)
            CMU: TC0029 TC0096
            CPN: CPn0319(truB) CPn0580(truA) CPn0719(sfhB) CPn0864(yjbC)
            CPA: CP0027 CP0168 CP0438 CP1005
            CPJ: CPj0319(truB) CPj0580(truA) CPj0719(sfhB) CPj0864(yjbC)
            CPT: CpB0329 CpB0605(truA) CpB0747 CpB0893
            CAB: CAB023(rluD) CAB159(truA) CAB379(rluC) CAB449(truB)
                 CAB871(rluB)
            CFE: CF0111(rsuB) CF0544(truB) CF0617(rsuC) CF0846(truA)
                 CF0982(rsuD)
            PCU: pc0160(yjbC) pc0328(truA) pc0355(rluD) pc0682(truA)
                 pc0759(truB)
            BBU: BB0012(hisT) BB0018 BB0129 BB0803(truB)
            BGA: BG0012(hisT) BG0018 BG0131 BG0829(truB)
            BAF: BAPKO_0011(hisT) BAPKO_0017 BAPKO_0131 BAPKO_0856(truB)
                 BAPKO_0868
            TPA: TP0339 TP0459 TP0830 TP0889
            TDE: TDE0860(rsuA) TDE0875(rluB) TDE1082 TDE1104(truB)
                 TDE2275(truA)
            LIL: LA0223(rluD) LA0945(truB) LA1490(rluC1) LA2291(rluB)
                 LA2740(truA)
            LIC: LIC10192 LIC11647 LIC12267(rluC) LIC12703(truB)
            LBJ: LBJ_0159(rluA) LBJ_0948(truB) LBJ_0989 LBJ_1323(rsuA)
                 LBJ_1717(truA)
            LBL: LBL_1548(rsuA) LBL_1936(truA) LBL_2044 LBL_2085(truB)
                 LBL_2924(rluA)
            SYN: sll1820(truA) slr0361 slr0457(truB) slr0612 slr1629
            SYW: SYNW0544(truB) SYNW0685 SYNW0737(rluA) SYNW0949(rsuA)
                 SYNW2092(truA) SYNW2326(rluD)
            SYC: syc0182_d(rluA) syc0328_c(truB) syc0437_d syc0535_d
                 syc1890_d(truA) syc2499_d
            SYF: Synpcc7942_1010 Synpcc7942_1112 Synpcc7942_1222
                 Synpcc7942_1374 Synpcc7942_1514 Synpcc7942_2207
            SYD: Syncc9605_0351 Syncc9605_1616 Syncc9605_1931 Syncc9605_1983
                 Syncc9605_2131 Syncc9605_2457
            SYE: Syncc9902_0543 Syncc9902_0678 Syncc9902_0735 Syncc9902_1377
                 Syncc9902_1980 Syncc9902_2141
            SYG: sync_0412(truA) sync_0907 sync_0988 sync_1017 sync_2233(truB)
                 sync_2706
            SYR: SynRCC307_2141(truA)
            SYX: SynWH7803_0409(truA)
            CYA: CYA_0740 CYA_0773 CYA_1338(truB) CYA_1449(truA) CYA_2627
            CYB: CYB_0078 CYB_0196 CYB_1113 CYB_1582(truA) CYB_2212(truB)
            TEL: tll0646 tll1538 tlr0107 tlr0656 tlr1606
            GVI: gll1379 gll3569 gll3690 glr0073 glr4397
            ANA: all3873 all4080 all4189 alr0522 alr0545 alr1543(truB)
            AVA: Ava_0356 Ava_0717(truA) Ava_1820 Ava_2924 Ava_3138 Ava_4983
            PMA: Pro0219(rluA) Pro1114(rsuA) Pro1428(truB) Pro1687(truA)
            PMM: PMM0193(rluD) PMM0658(rsuA) PMM1347(truB) PMM1533(truA)
            PMT: PMT1069(rsuA) PMT1112(rluA) PMT1170 PMT1422(truB)
                 PMT1757(truA) PMT2109(rluD)
            PMN: PMN2A_0601 PMN2A_0918 PMN2A_1104 PMN2A_1560(rluD)
            PMI: PMT9312_0195 PMT9312_1204 PMT9312_1445 PMT9312_1626
            PMB: A9601_12611(rsuA)
            PMC: P9515_12541(rsuA)
            PMF: P9303_09831(rsuA)
            PMG: P9301_12681(rsuA)
            PME: NATL1_14081(rsuA)
            TER: Tery_1293 Tery_1849 Tery_2319 Tery_2403 Tery_2986
            BTH: BT_3213 BT_3712 BT_3872 BT_4237 BT_4501
            BFR: BF0057 BF0489 BF0925 BF1141 BF4017
            BFS: BF0069 BF0434(rluD) BF0847(truA) BF1056 BF3791
            SRU: SRU_0664(truA) SRU_1189(rluD) SRU_1495(rluB)
            CHU: CHU_0143(rluB) CHU_0483(truA) CHU_0948(truB) CHU_1834
            GFO: GFO_2790(rluF) GFO_3627(rluF)
            FJO: Fjoh_4667
            FPS: FP1423(truA)
            CTE: CT0243(truB) CT0479(rsuA) CT0978(truA) CT1299(rluD)
            CCH: Cag_0542 Cag_1380 Cag_1460 Cag_1622(rluD)
            CPH: Cpha266_0494
            PLT: Plut_0783(rluD) Plut_1175 Plut_1688 Plut_1777
            DET: DET0504(truA) DET0789 DET0981(truB) DET1375
            DEH: cbdb_A1328 cbdb_A468(truA) cbdb_A767 cbdb_A945(truB)
            DEB: DehaBAV1_0481 DehaBAV1_0872
            RRS: RoseRS_1156
            RCA: Rcas_3997
            DRA: DR_0896 DR_1323 DR_1789 DR_1991 DR_2290
            DGE: Dgeo_0037 Dgeo_0594 Dgeo_0604 Dgeo_0761 Dgeo_0763
            TTH: TTC0040 TTC1167 TTC1267 TTC1767 TTC1769 TTC1847
            TTJ: TTHA0148 TTHA0217 TTHA0219 TTHA0408 TTHA1531 TTHA1631
            AAE: aq_1464 aq_1758 aq_554 aq_705(truB) aq_749(truA)
            TMA: TM0264 TM0462 TM0856 TM0940 TM1574
            TPT: Tpet_1218
            TME: Tmel_0937
            FNO: Fnod_0686
            MJA: MJ0148(cbf5) MJ0588 MJ1675(truA)
            MMP: MMP0268(truA) MMP0615 MMP1686(cbf5)
            MAC: MA0208(truA) MA1105 MA3271(glu)
            MBA: Mbar_A0082 Mbar_A1332 Mbar_A3206
            MMA: MM_0114 MM_1495 MM_2154
            MBU: Mbur_0028 Mbur_1281 Mbur_1625
            MHU: Mhun_0808 Mhun_2268 Mhun_2400
            MTH: MTH1529 MTH32 MTH840
            MST: Msp_0221(truD) Msp_0388(truA) Msp_0873(truB)
            MSI: Msm_0732 Msm_0855 Msm_1156
            MKA: MK0133(truB) MK0676 MK0888(truA)
            AFU: AF0238(cbf5) AF1677 AF1730(truA)
            HAL: VNG0243Cm VNG1729G(sus) VNG2003G(truA)
            HMA: rrnAC1758(glu) rrnAC3188(truA) rrnAC3342(truB)
            HWA: HQ1108A(truA) HQ1281A(truD) HQ2764A(truB)
            NPH: NP4916A(truB) NP5042A(truA) NP5228A(glu)
            TAC: Ta0214 Ta0932m Ta1244
            TVO: TVN0352 TVN1070 TVN1380
            PTO: PTO0505 PTO0667 PTO0780
            PHO: PH1242 PH1538 PH1644
            PAB: PAB0356(truB) PAB0430 PAB1701(truA)
            PFU: PF0918 PF1555 PF1785
            TKO: TK0927 TK1509 TK2302
            RCI: RCIX2227(truA)
            APE: APE_0989.1
            SSO: SSO0393(truB) SSO5761(truB)
            STO: ST0402(cbf5) STS055(cbf5)
            SAI: Saci_0811(tru)
            PAI: PAE0865 PAE1142 PAE3134
            NEQ: NEQ333 NEQ454
STRUCTURES  PDB: 1VS3  2NQP  2NR0  2NRE  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.12
            ExPASy - ENZYME nomenclature database: 5.4.99.12
            ExplorEnz - The Enzyme Database: 5.4.99.12
            ERGO genome analysis and discovery system: 5.4.99.12
            BRENDA, the Enzyme Database: 5.4.99.12
///
ENTRY       EC 5.4.99.13                Enzyme
NAME        isobutyryl-CoA mutase;
            isobutyryl coenzyme A mutase;
            butyryl-CoA:isobutyryl-CoA mutase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
SYSNAME     2-methylpropanoyl-CoA CoA-carbonylmutase
REACTION    2-methylpropanoyl-CoA = butanoyl-CoA [RN:R01181]
ALL_REAC    R01181
SUBSTRATE   2-methylpropanoyl-CoA [CPD:C00630]
PRODUCT     butanoyl-CoA [CPD:C00136]
COFACTOR    Cobalt [CPD:C00175];
            Cobamide coenzyme [CPD:C00194]
COMMENT     Requires a cobamide coenzyme.
REFERENCE   1
  AUTHORS   Brendelberger, G., Retey, J., Ashworth, D.M., Reynolds, K.,
            Willenbrock, F. and Robinson, J.A.
  TITLE     The enzymic interconversion of isobutyryl and
            N-butyrylcarba(dethia)-coenzyme-A - a coenzyme-B12-dependent carbon
            skeleton rearrangement.
  JOURNAL   Angew. Chem. Int. Ed. Engl. 27 (1988) 1089-1091.
  ORGANISM  Streptomyces cinnamonensis
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.13
            ExPASy - ENZYME nomenclature database: 5.4.99.13
            ExplorEnz - The Enzyme Database: 5.4.99.13
            ERGO genome analysis and discovery system: 5.4.99.13
            BRENDA, the Enzyme Database: 5.4.99.13
///
ENTRY       EC 5.4.99.14                Enzyme
NAME        4-carboxymethyl-4-methylbutenolide mutase;
            4-methyl-2-enelactone isomerase;
            4-methylmuconolactone methylisomerase;
            4-methyl-3-enelactone methyl isomerase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
SYSNAME     4-carboxymethyl-4-methylbut-2-en-1,4-olide methylmutase
REACTION    4-carboxymethyl-4-methylbut-2-en-1,4-olide =
            4-carboxymethyl-3-methylbut-2-en-1,4-olide [RN:R04510]
ALL_REAC    R04510
SUBSTRATE   4-carboxymethyl-4-methylbut-2-en-1,4-olide [CPD:C04559]
PRODUCT     4-carboxymethyl-3-methylbut-2-en-1,4-olide [CPD:C04558]
REFERENCE   1
  AUTHORS   Bruce, N.C. and Cain, R.B.
  TITLE     beta-Methylmuconolactone, a key intermediate in the dissimilation of
            methylaromatic compounds by a modified 3-oxoadipate pathway evolved
            in nocardioform actinomycetes.
  JOURNAL   FEMS Microbiol. Lett. 50 (1988) 233-239.
  ORGANISM  Rhodococcus ruber, Rhodococcus corallinus, Rhodococcus rhodochrous,
            Rhodococcus sp.
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.14
            ExPASy - ENZYME nomenclature database: 5.4.99.14
            ExplorEnz - The Enzyme Database: 5.4.99.14
            ERGO genome analysis and discovery system: 5.4.99.14
            BRENDA, the Enzyme Database: 5.4.99.14
///
ENTRY       EC 5.4.99.15                Enzyme
NAME        (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase;
            malto-oligosyltrehalose synthase;
            maltodextrin alpha-D-glucosyltransferase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
SYSNAME     (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase
REACTION    4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose =
            1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
            [RN:R01824 R06243]
ALL_REAC    R01824 R06243(G)
SUBSTRATE   4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose
PRODUCT     1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
COMMENT     The enzyme from Arthrobacter sp., Sulfolobus acidocaldarius acts on
            (1->4)-alpha-D-glucans containing three or more (1->4)-alpha-linked
            D-glucose units. Not active towards maltose.
REFERENCE   1  [PMID:8534970]
  AUTHORS   Maruta K, Nakada T, Kubota M, Chaen H, Sugimoto T, Kurimoto M,
            Tsujisaka Y.
  TITLE     Formation of trehalose from maltooligosaccharides by a novel
            enzymatic system.
  JOURNAL   Biosci. Biotechnol. Biochem. 59 (1995) 1829-34.
REFERENCE   2  [PMID:8611744]
  AUTHORS   Nakada T, Maruta K, Tsusaki K, Kubota M, Chaen H, Sugimoto T,
            Kurimoto M, Tsujisaka Y.
  TITLE     Purification and properties of a novel enzyme, maltooligosyl
            trehalose synthase, from Arthrobacter sp. Q36.
  JOURNAL   Biosci. Biotechnol. Biochem. 59 (1995) 2210-4.
  ORGANISM  Arthrobacter sp.
REFERENCE   3  [PMID:9063973]
  AUTHORS   Nakada T, Ikegami S, Chaen H, Kubota M, Fukuda S, Sugimoto T,
            Kurimoto M, Tsujisaka Y.
  TITLE     Purification and characterization of thermostable maltooligosyl
            trehalose synthase from the thermoacidophilic archaebacterium
            Sulfolobus acidocaldarius.
  JOURNAL   Biosci. Biotechnol. Biochem. 60 (1996) 263-6.
  ORGANISM  Sulfolobus acidocaldarius [GN:sai]
ORTHOLOGY   KO: K06044  
GENES       XCC: XCC0412(glgY)
            XCB: XC_0425
            XCV: XCV0455(glgY)
            XAC: XAC0429(glgY)
            XOO: XOO0116(glgY)
            XOM: XOO_0062(XOO0062)
            PAP: PSPA7_3144(treY)
            PPF: Pput_1790
            PSP: PSPPH_2245(treY)
            PFL: PFL_2884(treY)
            PFO: Pfl_2546
            PEN: PSEEN2051
            NOC: Noc_1680
            BMA: BMA0816
            BUR: Bcep18194_C7028
            BPS: BPSL2080
            BPM: BURPS1710b_1733(treY)
            BPL: BURPS1106A_1562(treY)
            AAV: Aave_2985
            NMU: Nmul_A1402
            MFA: Mfla_1416
            MXA: MXAN_1533(treY)
            SMD: Smed_4211
            RET: RHE_PE00008
            RLE: pRL110011
            BRA: BRADO5820
            BBT: BBta_6326
            RPC: RPC_3682
            RPD: RPD_3487
            RPE: RPE_3721
            NWI: Nwi_0946
            RSQ: Rsph17025_1779
            GBE: GbCGDNIH1_0747
            RRU: Rru_A0507
            MTU: Rv1563c(treY)
            MTC: MT1614(treY)
            MPA: MAP1269c(glgY)
            MAV: MAV_3211(treY)
            MMC: Mmcs_3081
            CGL: NCgl2037(cgl2118)
            CGB: cg2323(treY)
            CEF: CE2018
            CJK: jk0778(treY)
            NFA: nfa18140
            RHA: RHA1_ro01057
            LXX: Lxx02190(treY)
            CMI: CMM_1431(treY)
            AAU: AAur_2896(treY)
            FRA: Francci3_1349
            FAL: FRAAL2117(treY)
            KRA: Krad_3074
            CYA: CYA_0399(treY)
            CYB: CYB_2158(treY)
STRUCTURES  PDB: 1IV8  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.15
            ExPASy - ENZYME nomenclature database: 5.4.99.15
            ExplorEnz - The Enzyme Database: 5.4.99.15
            ERGO genome analysis and discovery system: 5.4.99.15
            BRENDA, the Enzyme Database: 5.4.99.15
            CAS: 170780-49-1
///
ENTRY       EC 5.4.99.16                Enzyme
NAME        maltose alpha-D-glucosyltransferase;
            trehalose synthase;
            maltose glucosylmutase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
SYSNAME     maltose alpha-D-glucosylmutase
REACTION    maltose = alpha,alpha-trehalose [RN:R01557 R06218]
ALL_REAC    R01557 R06218(G)
SUBSTRATE   maltose [CPD:C00208]
PRODUCT     alpha,alpha-trehalose [CPD:C01083]
REFERENCE   1
  AUTHORS   Nishimoto, T., Nakano, M., Ikegami, S., Chaen, H., Fukuda, S.,
            Sugimoto, T., Kurimoto, M., Tsujisaka, Y.
  TITLE     Existence of a novel enzyme converting maltose to trehalose.
  JOURNAL   Biosci. Biotechnol. Biochem. 59 (1995) 2189-2190.
REFERENCE   2  [PMID:8829531]
  AUTHORS   Nishimoto T, Nakano M, Nakada T, Chaen H, Fukuda S, Sugimoto T,
            Kurimoto M, Tsujisaka Y.
  TITLE     Purification and properties of a novel enzyme, trehalose synthase,
            from Pimelobacter sp. R48.
  JOURNAL   Biosci. Biotechnol. Biochem. 60 (1996) 640-4.
  ORGANISM  Pimelobacter sp.
PATHWAY     PATH: map00500  Starch and sucrose metabolism
ORTHOLOGY   KO: K05343  maltose alpha-D-glucosyltransferase
GENES       XCC: XCC0134
            XCB: XC_0142
            XCV: XCV0140
            XAC: XAC0155
            XOO: XOO0196
            XOM: XOO_0174(XOO0174)
            PAP: PSPA7_3106
            PSP: PSPPH_2425(treS)
            PFL: PFL_2873
            PEN: PSEEN2045
            NOC: Noc_0218 Noc_0830
            REH: H16_B1558 H16_B1564(treY)
            BXE: Bxe_B2862
            BUR: Bcep18194_C7033
            BCH: Bcen2424_6498
            BPL: BURPS1106A_1567(treS)
            AZO: azo1727(treS)
            MFA: Mfla_1418
            DDE: Dde_2353
            MXA: MXAN_3684(treS)
            RET: RHE_CH02260 RHE_PF00276
            RLE: pRL120709(treS)
            BRA: BRADO0512 BRADO5816
            BBT: BBta_6322
            RPE: RPE_3717
            NWI: Nwi_1208
            GBE: GbCGDNIH1_0751
            RRU: Rru_A1605
            MAV: MAV_5186(treS)
            MSM: MSMEG_6515(treS)
            AAU: AAur_0909(treS) AAur_4069(treS)
            PAC: PPA1113
            FRA: Francci3_3679
            FAL: FRAAL0625 FRAAL5900(treS)
            SYW: SYNW1955
            SYG: sync_0567
            SYR: SynRCC307_1380
            SYX: SynWH7803_0545
            CYA: CYA_1097
            CYB: CYB_0677
            SRU: SRU_0847
            CCH: Cag_1983
            PTO: PTO0069 PTO0071
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.16
            ExPASy - ENZYME nomenclature database: 5.4.99.16
            ExplorEnz - The Enzyme Database: 5.4.99.16
            ERGO genome analysis and discovery system: 5.4.99.16
            BRENDA, the Enzyme Database: 5.4.99.16
///
ENTRY       EC 5.4.99.17                Enzyme
NAME        squalene---hopene cyclase
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
SYSNAME     squalene mutase (cyclizing)
REACTION    (1) squalene = hop-22(29)-ene [RN:R07322];
            (2) squalene + H2O = hopan-22-ol [RN:R07323]
ALL_REAC    R07322 R07323
SUBSTRATE   squalene [CPD:C00751];
            H2O [CPD:C00001]
PRODUCT     hop-22(29)-ene [CPD:C06310];
            hopan-22-ol [CPD:C06309]
REFERENCE   1
  AUTHORS   Seckler, B. and Poralla, K.
  TITLE     Characterization and partial purification of squalene-hopene cyclase
            from Bacillus acidocaldarius.
  JOURNAL   Biochim. Biophys. Acta 881 (1986) 356-363.
  ORGANISM  Bacillus acidocaldarius
REFERENCE   2
  AUTHORS   Hoshino, T. and Sato, T.
  TITLE     Squalene-hopene cyclase: catalytic mechanism and substrate
            recognition.
  JOURNAL   Chem. Commun. (2002) 291-301.
  ORGANISM  Alicyclobacillus acidocaldarius
ORTHOLOGY   KO: K06045  squalene-hopene cyclase
GENES       AFM: AFUA_7G00260
            TET: TTHERM_01008630
            NOC: Noc_1320
            REU: Reut_B4954
            RME: Rmet_4148 Rmet_4403
            BMA: BMAA2100(shc)
            BMV: BMASAVP1_1129(shc)
            BML: BMA10299_1409(shc)
            BMN: BMA10247_A2394(shc)
            BXE: Bxe_B0012
            BVI: Bcep1808_3808
            BUR: Bcep18194_B0019 Bcep18194_C7519
            BCN: Bcen_5180 Bcen_5698
            BCH: Bcen2424_5679 Bcen2424_6062
            BAM: Bamb_4951 Bamb_6104
            BPS: BPSS2339(shc)
            BPM: BURPS1710b_A1490(shc)
            BPL: BURPS1106A_A3161(shc)
            BPD: BURPS668_A3275(shc)
            BTE: BTH_II2359(shc)
            NET: Neut_1507
            GSU: GSU0688(shc-1) GSU3061(shc-2)
            GME: Gmet_0419 Gmet_2820
            GUR: Gura_1020
            PCA: Pcar_0355 Pcar_0441
            PPD: Ppro_1189
            SFU: Sfum_1989 Sfum_2736
            BJA: blr3004(shc)
            BRA: BRADO6252(shc)
            BBT: BBta_1355(shc)
            RPA: RPA3740(sqhC)
            RPB: RPB_1726
            RPC: RPC_1720
            RPE: RPE_4468
            NWI: Nwi_2269
            NHA: Nham_2682
            ZMO: ZMO0872(shc) ZMO1548(shc)
            GOX: GOX2260
            GBE: GbCGDNIH1_2107
            RRU: Rru_A0062
            MAG: amb1367
            ABA: Acid345_1740
            BPU: BPUM_1858(sqhC)
            SCO: SCO6764(SC6A5.13)
            SMA: SAV1650(hopA)
            FRA: Francci3_0823
            FAL: FRAAL1432(shc1) FRAAL2491(shc2)
            SEN: SACE_4327(shc1)
            SYN: slr2089(shc)
            TEL: tlr2309(shc)
            GVI: glr4057(shc)
            ANA: all0775
            AVA: Ava_4671
STRUCTURES  PDB: 1UMP  
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.17
            ExPASy - ENZYME nomenclature database: 5.4.99.17
            ExplorEnz - The Enzyme Database: 5.4.99.17
            ERGO genome analysis and discovery system: 5.4.99.17
            BRENDA, the Enzyme Database: 5.4.99.17
            CAS: 76600-69-6
///
ENTRY       EC 5.4.99.18                Enzyme
NAME        5-(carboxyamino)imidazole ribonucleotide mutase;
            N5-CAIR mutase;
            PurE;
            N5-carboxyaminoimidazole ribonucleotide mutase;
            class I PurE
CLASS       Isomerases;
            Intramolecular transferases;
            Transferring other groups
SYSNAME     5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole carboxymutase
REACTION    5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole =
            5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate [RN:R07405]
ALL_REAC    R07405
SUBSTRATE   5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole [CPD:C15667]
PRODUCT     5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate [CPD:C04751]
COMMENT     In eubacteria, fungi and plants, this enzyme, along with EC
            6.3.4.18, 5-(carboxyamino)imidazole ribonucleotide synthase, is
            required to carry out the single reaction catalysed by EC 4.1.1.21,
            phosphoribosylaminoimidazole carboxylase, in vertebrates [6]. In the
            absence of EC 6.3.2.6,
            phosphoribosylaminoimidazolesuccinocarboxamide synthase, the
            reaction is reversible [3]. The substrate is readily converted into
            5-amino-1-(5-phospho-D-ribosyl)imidazole by non-enzymic
            decarboxylation [3].
REFERENCE   1  [PMID:1534690]
  AUTHORS   Meyer E, Leonard NJ, Bhat B, Stubbe J, Smith JM.
  TITLE     Purification and characterization of the purE, purK, and purC gene
            products: identification of a previously unrecognized energy
            requirement in the purine biosynthetic pathway.
  JOURNAL   Biochemistry. 31 (1992) 5022-32.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:8117684]
  AUTHORS   Mueller EJ, Meyer E, Rudolph J, Davisson VJ, Stubbe J.
  TITLE     N5-carboxyaminoimidazole ribonucleotide: evidence for a new
            intermediate and two new enzymatic activities in the de novo purine
            biosynthetic pathway of Escherichia coli.
  JOURNAL   Biochemistry. 33 (1994) 2269-78.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:10074353]
  AUTHORS   Meyer E, Kappock TJ, Osuji C, Stubbe J.
  TITLE     Evidence for the direct transfer of the carboxylate of
            N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to generate
            4-carboxy-5-aminoimidazole ribonucleotide catalyzed by Escherichia
            coli PurE, an N5-CAIR mutase.
  JOURNAL   Biochemistry. 38 (1999) 3012-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:10574791]
  AUTHORS   Mathews II, Kappock TJ, Stubbe J, Ealick SE.
  TITLE     Crystal structure of Escherichia coli PurE, an unusual mutase in the
            purine biosynthetic pathway.
  JOURNAL   Structure. 7 (1999) 1395-406.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:7918411]
  AUTHORS   Firestine SM, Poon SW, Mueller EJ, Stubbe J, Davisson VJ.
  TITLE     Reactions catalyzed by 5-aminoimidazole ribonucleotide carboxylases
            from Escherichia coli and Gallus gallus: a case for divergent
            catalytic mechanisms.
  JOURNAL   Biochemistry. 33 (1994) 11927-34.
REFERENCE   6  [PMID:9500840]
  AUTHORS   Firestine SM, Misialek S, Toffaletti DL, Klem TJ, Perfect JR,
            Davisson VJ.
  TITLE     Biochemical role of the Cryptococcus neoformans ADE2 protein in
            fungal de novo purine biosynthesis.
  JOURNAL   Arch. Biochem. Biophys. 351 (1998) 123-34.
DBLINKS     IUBMB Enzyme Nomenclature: 5.4.99.18
            ExPASy - ENZYME nomenclature database: 5.4.99.18
            ExplorEnz - The Enzyme Database: 5.4.99.18
            ERGO genome analysis and discovery system: 5.4.99.18
            BRENDA, the Enzyme Database: 5.4.99.18
///
ENTRY       EC 5.5.1.1                  Enzyme
NAME        muconate cycloisomerase;
            muconate cycloisomerase I;
            cis,cis-muconate-lactonizing enzyme;
            cis,cis-muconate cycloisomerase;
            muconate lactonizing enzyme;
            4-carboxymethyl-4-hydroxyisocrotonolactone lyase (decyclizing)
CLASS       Isomerases;
            Intramolecular lyases;
            Intramolecular lyases (only sub-subclass identified to date)
SYSNAME     2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
REACTION    2,5-dihydro-5-oxofuran-2-acetate = cis,cis-hexadienedioate
            [RN:R03959]
ALL_REAC    R03959 > R06989;
            (other) R04489 R05300 R05390
SUBSTRATE   2,5-dihydro-5-oxofuran-2-acetate [CPD:C04105]
PRODUCT     cis,cis-hexadienedioate [CPD:C02480]
COFACTOR    Manganese [CPD:C00034]
COMMENT     Requires Mn2+. Also acts (in the reverse reaction) on
            3-methyl-cis,cis-hexadienedioate and, very slowly, on
            cis,trans-hexadienedioate. Not identical with EC 5.5.1.7
            (chloromuconate cycloisomerase) or EC 5.5.1.11 (dichloromuconate
            cycloisomerase).
REFERENCE   1  [PMID:5330966]
  AUTHORS   Ornston LN.
  TITLE     The conversion of catechol and protocatechuate to beta-ketoadipate
            by Pseudomonas putida. 3. Enzymes of the catechol pathway.
  JOURNAL   J. Biol. Chem. 241 (1966) 3795-9.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2
  AUTHORS   Ornston, L.N.
  TITLE     Conversion of catechol and protocatechuate to beta-ketoadipate
            (Pseudomonas putida).
  JOURNAL   Methods Enzymol. 17A (1970) 529-549.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   3
  AUTHORS   Sistrom, W.R. and Stanier, R.Y.
  TITLE     The mechanism of formation of beta-ketoadipic acid by bacteria.
  JOURNAL   J. Biol. Chem. 210 (1954) 821-836.
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
            PATH: map00622  Toluene and xylene degradation
            PATH: map00627  1,4-Dichlorobenzene degradation
ORTHOLOGY   KO: K01856  muconate cycloisomerase
GENES       AFM: AFUA_6G11580
            ECI: UTI89_C1768(rspA)
            ECA: ECA3116
            PAE: PA2509(catB)
            PAU: PA14_32220(catB)
            PPU: PP_3715(catB)
            PFL: PFL_3862(catB)
            PFO: Pfl_2325 Pfl_2963
            PEN: PSEEN3138(catB)
            PCR: Pcryo_1270
            ACI: ACIAD1446(catB)
            PAT: Patl_2790
            FTW: FTW_0641
            REU: Reut_B4400 Reut_D6465 Reut_D6474
            REH: H16_A1966(catB3) H16_B0536(catB4)
            RME: Rmet_4878
            BMA: BMAA0200(catB)
            BMV: BMASAVP1_1375(catB)
            BML: BMA10299_1572(catB)
            BMN: BMA10247_A0231(catB)
            BXE: Bxe_A2108(catB) Bxe_C1041
            BUR: Bcep18194_A4351 Bcep18194_B2328 Bcep18194_C7044
            BCN: Bcen_4593
            BCH: Bcen2424_3770
            BAM: Bamb_5499
            BPS: BPSS1891(catB)
            BPM: BURPS1710b_A0986(catB)
            BPL: BURPS1106A_A2566(catB)
            BPD: BURPS668_A2710(catB)
            BTE: BTH_II0485
            POL: Bpro_4404
            PNA: Pnap_2119
            AJS: Ajs_0140
            DDE: Dde_1177
            MLO: mlr0803
            MES: Meso_1539
            SME: SMa1461 SMc00459
            ATU: Atu1648
            ATC: AGR_C_3037
            RET: RHE_CH02350
            BME: BMEI0966
            BMF: BAB1_1037
            BMS: BR1018
            BMB: BruAb1_1023
            BJA: blr5895
            BRA: BRADO0023 BRADO4202 BRADO5087 BRADO6325
            BBT: BBta_0028 BBta_4577
            RPA: RPA3964
            RPB: RPB_1626
            RPC: RPC_1451
            RPD: RPD_1635
            RPE: RPE_1470
            NWI: Nwi_1085
            NHA: Nham_1314
            XAU: Xaut_1132 Xaut_4358
            CCR: CC_3113
            SIL: SPO3606 SPO3667(catB)
            RSP: RSP_1769
            JAN: Jann_0365 Jann_1408
            RDE: RD1_1003
            PDE: Pden_1174
            HNE: HNE_2922
            SWI: Swit_0975
            RRU: Rru_A2556
            BCL: ABC3013
            MBB: BCG_0598(menC)
            MSM: MSMEG_1910
            RHA: RHA1_ro02372(catB)
            SEN: SACE_4412 SACE_6327
            RXY: Rxyl_3044
            RBA: RB10855
            AVA: Ava_3512
            TTH: TTC1473
            HBU: Hbut_0684
STRUCTURES  PDB: 1BKH  1F9C  1MUC  2MUC  2PGW  3MUC  
DBLINKS     IUBMB Enzyme Nomenclature: 5.5.1.1
            ExPASy - ENZYME nomenclature database: 5.5.1.1
            ExplorEnz - The Enzyme Database: 5.5.1.1
            ERGO genome analysis and discovery system: 5.5.1.1
            UM-BBD (Biocatalysis/Biodegradation Database): 5.5.1.1
            BRENDA, the Enzyme Database: 5.5.1.1
            CAS: 9023-72-7
///
ENTRY       EC 5.5.1.2                  Enzyme
NAME        3-carboxy-cis,cis-muconate cycloisomerase;
            beta-carboxymuconate lactonizing enzyme;
            3-carboxymuconolactone hydrolase
CLASS       Isomerases;
            Intramolecular lyases;
            Intramolecular lyases (only sub-subclass identified to date)
SYSNAME     2-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
REACTION    2-carboxy-2,5-dihydro-5-oxofuran-2-acetate =
            cis,cis-butadiene-1,2,4-tricarboxylate [RN:R03307]
ALL_REAC    R03307
SUBSTRATE   2-carboxy-2,5-dihydro-5-oxofuran-2-acetate [CPD:C01278]
PRODUCT     cis,cis-butadiene-1,2,4-tricarboxylate [CPD:C01163]
REFERENCE   1  [PMID:5916392]
  AUTHORS   Ornston LN.
  TITLE     The conversion of catechol and protocatechuate to beta-ketoadipate
            by Pseudomonas putida. II. Enzymes of the protocatechuate pathway.
  JOURNAL   J. Biol. Chem. 241 (1966) 3787-94.
  ORGANISM  Pseudomonas putida [GN:ppu]
REFERENCE   2
  AUTHORS   Ornston, L.N.
  TITLE     Conversion of catechol and protocatechuate to beta-ketoadipate
            (Pseudomonas putida).
  JOURNAL   Methods Enzymol. 17A (1970) 529-549.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
ORTHOLOGY   KO: K01857  3-carboxy-cis,cis-muconate cycloisomerase
GENES       SPO: SPBC8E4.05c
            ECA: ECA2842(pcaB)
            XCC: XCC0369(pcaB)
            XCB: XC_0381
            XCV: XCV0383(pcaB)
            XAC: XAC0369(pcaB)
            XOO: XOO0484(pcaB)
            XOM: XOO_0451(XOO0451)
            VVY: VV2243
            PAE: PA0230(pcaB)
            PAU: PA14_02830(pcaB)
            PAP: PSPA7_0316(pcaB)
            PPU: PP_1379(pcaB)
            PST: PSPTO_2341(pcaB)
            PSB: Psyr_2125
            PSP: PSPPH_2099(pcaB)
            PFL: PFL_1323(pcaB)
            PFO: Pfl_1273
            PEN: PSEEN1167(pcaB)
            ACI: ACIAD1707(pcaB)
            CSA: Csal_0298
            RSO: RSc2251(pcaB)
            REH: H16_A2422(pcaB2) H16_B2289(pcaB1)
            RME: Rmet_4015
            BMA: BMAA0048(pcaB)
            BMV: BMASAVP1_1202(pcaB)
            BML: BMA10299_1485(pcaB)
            BMN: BMA10247_A0058(pcaB)
            BXE: Bxe_B0645(pcaB) Bxe_B1906
            BUR: Bcep18194_B3127
            BCN: Bcen_5111
            BCH: Bcen2424_5748
            BAM: Bamb_5019
            BPS: BPSS0045(pcaB)
            BPM: BURPS1710b_A1555(pcaB)
            BPL: BURPS1106A_A0056(pcaB)
            BPD: BURPS668_A0069(pcaB)
            BTE: BTH_II0048
            RFR: Rfer_0014 Rfer_3487
            POL: Bpro_4557
            MLO: mlr7211
            MES: Meso_2052
            SME: SMb20575(pcaB)
            ATU: Atu4538(pcaB)
            ATC: AGR_L_661
            RET: RHE_PE00055(pcaB)
            RLE: pRL110085
            BME: BMEII0634
            BMF: BAB2_0594
            BMS: BRA0647
            BMB: BruAb2_0579
            BJA: bll7942(pcaB) blr5667(pcaB)
            CCR: CC_2410
            SIL: SPOA0432(pcaB)
            SIT: TM1040_0555
            RDE: RD1_3935(pcaB)
            MPA: MAP2729c(pcaB)
            MAV: MAV_3504(pcaB)
            MSM: MSMEG_2603(pcaB)
            MMC: Mmcs_1700
            CGL: NCgl1969(cgl2046) NCgl2313(cgl2396)
            CGB: cg2244(pcaB2) cg2629(pcaB1)
            CEF: CE2299
            RHA: RHA1_ro01337(pcaB)
            SCO: SCO6698(pcaB)
            SMA: SAV1705(pcaB)
            ART: Arth_4076
            FRA: Francci3_0150
            SEN: SACE_3512(pcaB)
            RXY: Rxyl_1579
            DGE: Dgeo_2385
STRUCTURES  PDB: 1Q5N  
DBLINKS     IUBMB Enzyme Nomenclature: 5.5.1.2
            ExPASy - ENZYME nomenclature database: 5.5.1.2
            ExplorEnz - The Enzyme Database: 5.5.1.2
            ERGO genome analysis and discovery system: 5.5.1.2
            BRENDA, the Enzyme Database: 5.5.1.2
            CAS: 9075-77-8
///
ENTRY       EC 5.5.1.3                  Enzyme
NAME        tetrahydroxypteridine cycloisomerase
CLASS       Isomerases;
            Intramolecular lyases;
            Intramolecular lyases (only sub-subclass identified to date)
SYSNAME     tetrahydroxypteridine lyase (isomerizing)
REACTION    tetrahydroxypteridine = xanthine-8-carboxylate [RN:R04154]
ALL_REAC    R04154
SUBSTRATE   tetrahydroxypteridine [CPD:C03178]
PRODUCT     xanthine-8-carboxylate [CPD:C03314]
COFACTOR    NAD+ [CPD:C00003]
REFERENCE   1
  AUTHORS   McNutt, W.S. and Damle, S.P.
  TITLE     Tetraoxypteridine isomerase.
  JOURNAL   J. Biol. Chem. 239 (1964) 4272-4279.
  ORGANISM  Alcaligenes faecalis
DBLINKS     IUBMB Enzyme Nomenclature: 5.5.1.3
            ExPASy - ENZYME nomenclature database: 5.5.1.3
            ExplorEnz - The Enzyme Database: 5.5.1.3
            ERGO genome analysis and discovery system: 5.5.1.3
            BRENDA, the Enzyme Database: 5.5.1.3
            CAS: 37318-54-0
///
ENTRY       EC 5.5.1.4                  Enzyme
NAME        inositol-3-phosphate synthase;
            myo-inositol-1-phosphate synthase;
            D-glucose 6-phosphate cycloaldolase;
            inositol 1-phosphate synthatase;
            glucose 6-phosphate cyclase;
            inositol 1-phosphate synthetase;
            glucose-6-phosphate inositol monophosphate cycloaldolase;
            glucocycloaldolase;
            1L-myo-inositol-1-phosphate lyase (isomerizing)
CLASS       Isomerases;
            Intramolecular lyases;
            Intramolecular lyases (only sub-subclass identified to date)
SYSNAME     1D-myo-inositol-3-phosphate lyase (isomerizing)
REACTION    D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate [RN:R07324]
ALL_REAC    R07324;
            (other) R00840
SUBSTRATE   D-glucose 6-phosphate [CPD:C00092]
PRODUCT     1D-myo-inositol 3-phosphate [CPD:C04006]
COFACTOR    NAD+ [CPD:C00003]
COMMENT     Requires NAD+, which dehydrogenates the -CHOH- group to -CO- at C-5
            of the glucose 6-phosphate, making C-6 into an active methylene,
            able to condense with the -CHO at C-1. Finally, the enzyme-bound
            NADH reconverts C-5 into the -CHOH- form.
REFERENCE   1  [PMID:4290245]
  AUTHORS   Eisenberg F Jr.
  TITLE     D-myoinositol 1-phosphate as product of cyclization of glucose
            6-phosphate and substrate for a specific phosphatase in rat testis.
  JOURNAL   J. Biol. Chem. 242 (1967) 1375-82.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:4310603]
  AUTHORS   Sherman WR, Stewart MA, Zinbo M.
  TITLE     Mass spectrometric study on the mechanism of D-glucose
            6-phosphate-L-myo-inositol 1-phosphate cyclase.
  JOURNAL   J. Biol. Chem. 244 (1969) 5703-8.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:4297937]
  AUTHORS   Barnett JE, Corina DL.
  TITLE     The mechanism of glucose 6-phosphate-D-myo-inositol 1-phosphate
            cyclase of rat testis. The involvement of hydrogen atoms.
  JOURNAL   Biochem. J. 108 (1968) 125-9.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:4352864]
  AUTHORS   Barnett JE, Rasheed A, Corina DL.
  TITLE     Partial reactions of D-glucose 6-phosphate-1L-myoinositiol
            1-phosphate cyclase.
  JOURNAL   Biochem. J. 131 (1973) 21-30.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00521  Streptomycin biosynthesis
            PATH: map00562  Inositol phosphate metabolism
ORTHOLOGY   KO: K01858  myo-inositol-1-phosphate synthase
GENES       HSA: 51477(ISYNA1)
            CFA: 476667(LOC476667)
            XLA: 379227(MGC52653)
            SPU: 575252(LOC575252)
            DME: Dmel_CG11143
            CEL: VF13D12L.1
            ATH: AT2G22240 AT4G39800(MI-1-P_SYNTHASE) AT5G10170
            OSA: 4331917
            CME: CMR036C
            SCE: YJL153C(INO1)
            PIC: PICST_29246(INO1)
            CGR: CAGL0I06050g
            ANI: AN7625.2
            AFM: AFUA_2G01010
            AOR: AO090701000359
            CNE: CNC06440
            DDI: DDB_0231710(ino1)
            PFA: PFE0585c
            TET: TTHERM_00519810
            TBR: Tb10.6k15.3600
            TCR: 507609.60
            LMA: LmjF14.1360
            EHI: 273.t00008 57.t00034
            NOC: Noc_2981
            GUR: Gura_2530
            ADE: Adeh_1535 Adeh_4149
            AFW: Anae109_2277 Anae109_4291
            MXA: MXAN_0452
            SFU: Sfum_1734 Sfum_1982
            SME: SMb20249
            RET: RHE_CH02739(ypch00943)
            NAR: Saro_0101
            GBE: GbCGDNIH1_0236
            ABA: Acid345_2392
            SUS: Acid_1254
            BCE: BC2648
            MTU: Rv0046c(ino1)
            MTC: MT0052
            MBO: Mb0047c(ino1)
            MBB: BCG_0077c(ino1)
            MLE: ML0396
            MPA: MAP0060c
            MAV: MAV_0067
            MMC: Mmcs_5376
            CGL: NCgl2894(cgl2996)
            CGB: cg3323
            CEF: CE2831
            CDI: DIP0115
            CJK: jk2071
            NFA: nfa55520
            RHA: RHA1_ro03447
            SCO: SCO3243(SCE29.12c) SCO3899(SCH24.21c)
            SMA: SAV4296(ino1)
            TFU: Tfu_3099
            FRA: Francci3_4529
            FAL: FRAAL6860
            SEN: SACE_2992 SACE_7359(ino1)
            BAD: BAD_0158
            RXY: Rxyl_0688 Rxyl_1213
            BTH: BT_1526
            DET: DET0979
            DEH: cbdb_A943
            AAE: aq_1763
            TMA: TM1419
            MAC: MA0075 MA2253
            MBA: Mbar_A1040
            MMA: MM_1370
            MBU: Mbur_2381
            MTH: MTH1105
            MST: Msp_1166
            MSI: Msm_0940
            PHO: PH1605
            PAB: PAB1989(ino1)
            PFU: PF1616
            TKO: TK2278
            APE: APE_1517
            SSO: SSO0330 SSO0886
            STO: ST1234 ST2224
            SAI: Saci_1419 Saci_2337(mipS)
            PAI: PAE1761
STRUCTURES  PDB: 1GR0  1JKF  1JKI  1LA2  1P1F  1P1H  1P1I  1P1J  1P1K  1RM0  
                 1VJP  1VKO  
DBLINKS     IUBMB Enzyme Nomenclature: 5.5.1.4
            ExPASy - ENZYME nomenclature database: 5.5.1.4
            ExplorEnz - The Enzyme Database: 5.5.1.4
            ERGO genome analysis and discovery system: 5.5.1.4
            BRENDA, the Enzyme Database: 5.5.1.4
            CAS: 9032-95-5
///
ENTRY       EC 5.5.1.5                  Enzyme
NAME        carboxy-cis,cis-muconate cyclase;
            3-carboxymuconate cyclase
CLASS       Isomerases;
            Intramolecular lyases;
            Intramolecular lyases (only sub-subclass identified to date)
SYSNAME     3-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
REACTION    3-carboxy-2,5-dihydro-5-oxofuran-2-acetate =
            3-carboxy-cis,cis-muconate [RN:R03308]
ALL_REAC    R03308
SUBSTRATE   3-carboxy-2,5-dihydro-5-oxofuran-2-acetate [CPD:C04553]
PRODUCT     3-carboxy-cis,cis-muconate [CPD:C01163]
REFERENCE   1  [PMID:13319299]
  AUTHORS   GROSS SR, GAFFORD RD, TATUM EL.
  TITLE     The metabolism of protocatechuic acid by Neurospora.
  JOURNAL   J. Biol. Chem. 219 (1956) 781-96.
  ORGANISM  Neurospora crassa [GN:dncr]
PATHWAY     PATH: map00362  Benzoate degradation via hydroxylation
GENES       GOX: GOX0039
            LDB: Ldb0588
STRUCTURES  PDB: 1JOF  
DBLINKS     IUBMB Enzyme Nomenclature: 5.5.1.5
            ExPASy - ENZYME nomenclature database: 5.5.1.5
            ExplorEnz - The Enzyme Database: 5.5.1.5
            ERGO genome analysis and discovery system: 5.5.1.5
            BRENDA, the Enzyme Database: 5.5.1.5
            CAS: 37318-55-1
///
ENTRY       EC 5.5.1.6                  Enzyme
NAME        chalcone isomerase;
            chalcone-flavanone isomerase
CLASS       Isomerases;
            Intramolecular lyases;
            Intramolecular lyases (only sub-subclass identified to date)
SYSNAME     flavanone lyase (decyclizing)
REACTION    a chalcone = a flavanone [RN:R07344]
ALL_REAC    R07344 > R02446 R02898 R06556
SUBSTRATE   chalcone [CPD:C01484]
PRODUCT     flavanone [CPD:C00766]
REFERENCE   1
  AUTHORS   Moustafa, E. and Wong, E.
  TITLE     Purification and properties of chalcone-flavanone isomerase from
            soya bean seed.
  JOURNAL   Phytochemistry 6 (1967) 625-632.
  ORGANISM  Soja hispida
PATHWAY     PATH: map00941  Flavonoid biosynthesis
ORTHOLOGY   KO: K01859  chalcone isomerase
GENES       ATH: AT3G55120(TT5) AT5G66220
            OSA: 4334588
STRUCTURES  PDB: 1EYP  1EYQ  1FM7  1FM8  1JEP  1JX0  1JX1  
DBLINKS     IUBMB Enzyme Nomenclature: 5.5.1.6
            ExPASy - ENZYME nomenclature database: 5.5.1.6
            ExplorEnz - The Enzyme Database: 5.5.1.6
            ERGO genome analysis and discovery system: 5.5.1.6
            BRENDA, the Enzyme Database: 5.5.1.6
            CAS: 9073-57-8
///
ENTRY       EC 5.5.1.7                  Enzyme
NAME        chloromuconate cycloisomerase;
            muconate cycloisomerase II
CLASS       Isomerases;
            Intramolecular lyases;
            Intramolecular lyases (only sub-subclass identified to date)
SYSNAME     2-chloro-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
REACTION    2-chloro-2,5-dihydro-5-oxofuran-2-acetate =
            3-chloro-cis,cis-muconate [RN:R04259]
ALL_REAC    R04259;
            (other) R05391 R05392 R06834 R06840
SUBSTRATE   2-chloro-2,5-dihydro-5-oxofuran-2-acetate [CPD:C04522]
PRODUCT     3-chloro-cis,cis-muconate [CPD:C03585]
COFACTOR    Manganese [CPD:C00034]
COMMENT     Requires Mn2+. The product of cycloisomerization of
            3-chloro-cis,cis-muconate spontaneously eliminates chloride to
            produce cis-4-carboxymethylenebut-2-en-4-olide. Also acts (in the
            reverse direction) on 2-chloro-cis,cis-muconate. Not identical with
            EC 5.5.1.1 (muconate cycloisomerase) or EC 5.5.1.11
            (dichloromuconate cycloisomerase).
REFERENCE   1  [PMID:7305906]
  AUTHORS   Schmidt E, Knackmuss HJ.
  TITLE     Chemical structure and biodegradability of halogenated aromatic
            compounds. Conversion of chlorinated muconic acids into
            maleoylacetic acid.
  JOURNAL   Biochem. J. 192 (1980) 339-47.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00361  gamma-Hexachlorocyclohexane degradation
            PATH: map00627  1,4-Dichlorobenzene degradation
ORTHOLOGY   KO: K01860  chloromuconate cycloisomerase
GENES       DDI: DDBDRAFT_0186151
            XCC: XCC3807(tcbD)
            XCB: XC_3879
            XCV: XCV3980(tcbD)
            XAC: XAC3862(tcbD)
            XOO: XOO4102(tcbD)
            XOM: XOO_3878(XOO3878)
            BXE: Bxe_A1129(clcB)
            SUN: SUN_1179
            BOV: BOV_0985
            BTL: BALH_0330
            CGB: cg2635(catB)
            RBA: RB11118 RB8686(ykfB)
            CHU: CHU_2140(tfdD) CHU_2415(clcB)
            SAI: Saci_2196
STRUCTURES  PDB: 1CHR  1NU5  2CHR  
DBLINKS     IUBMB Enzyme Nomenclature: 5.5.1.7
            ExPASy - ENZYME nomenclature database: 5.5.1.7
            ExplorEnz - The Enzyme Database: 5.5.1.7
            ERGO genome analysis and discovery system: 5.5.1.7
            UM-BBD (Biocatalysis/Biodegradation Database): 5.5.1.7
            BRENDA, the Enzyme Database: 5.5.1.7
            CAS: 95990-33-3
///
ENTRY       EC 5.5.1.8                  Enzyme
NAME        bornyl diphosphate synthase;
            bornyl pyrophosphate synthase;
            bornyl pyrophosphate synthetase;
            (+)-bornylpyrophosphate cyclase;
            geranyl-diphosphate cyclase (ambiguous)
CLASS       Isomerases;
            Intramolecular lyases;
            Intramolecular lyases (only sub-subclass identified to date)
SYSNAME     (+)-bornyl-diphosphate lyase (decyclizing)
REACTION    geranyl diphosphate = (+)-bornyl diphosphate [RN:R02007]
ALL_REAC    R02007
SUBSTRATE   geranyl diphosphate [CPD:C00341]
PRODUCT     (+)-bornyl diphosphate
REFERENCE   1  [PMID:42356]
  AUTHORS   Croteau R, Karp F.
  TITLE     Biosynthesis of monoterpenes: preliminary characterization of bornyl
            pyrophosphate synthetase from sage (Salvia officinalis) and
            demonstration that Geranyl pyrophosphate is the preferred substrate
            for cyclization.
  JOURNAL   Arch. Biochem. Biophys. 198 (1979) 512-22.
  ORGANISM  Salvia officinalis
PATHWAY     PATH: map00902  Monoterpenoid biosynthesis
STRUCTURES  PDB: 1N1B  1N1Z  1N20  1N21  1N22  1N23  1N24  
DBLINKS     IUBMB Enzyme Nomenclature: 5.5.1.8
            ExPASy - ENZYME nomenclature database: 5.5.1.8
            ExplorEnz - The Enzyme Database: 5.5.1.8
            ERGO genome analysis and discovery system: 5.5.1.8
            BRENDA, the Enzyme Database: 5.5.1.8
            CAS: 72668-91-8
///
ENTRY       EC 5.5.1.9                  Enzyme
NAME        cycloeucalenol cycloisomerase;
            cycloeucalenol---obtusifoliol isomerase
CLASS       Isomerases;
            Intramolecular lyases;
            Intramolecular lyases (only sub-subclass identified to date)
SYSNAME     cycloeucalenol lyase (cyclopropane-decyclizing)
REACTION    cycloeucalenol = obtusifoliol [RN:R03775]
ALL_REAC    R03775
SUBSTRATE   cycloeucalenol [CPD:C02141]
PRODUCT     obtusifoliol [CPD:C01943]
COMMENT     Opens the cyclopropane ring of a number of related
            4alpha-methyl-9beta-19-cyclosterols, but not those with a
            4beta-methyl group, with formation of an 8(9) double bond. Involved
            in the synthesis of plant sterols.
REFERENCE   1  [PMID:4369016]
  AUTHORS   Heintz R, Benveniste P.
  TITLE     Plant sterol metabolism. Enzymatic cleavage of the 9beta,
            19beta-cyclopropane ring of cyclopropyl sterols in bramble tissue
            cultures.
  JOURNAL   J. Biol. Chem. 249 (1974) 4267-74.
  ORGANISM  Rubus fruticosus
REFERENCE   2
  AUTHORS   Rahier, A., Schmitt, P. and Benveniste, P.
  TITLE     7-oxo-24&xi;(28)-dihydrocycloeucalenol, a potent inhibitor of plant
            sterol biosynthesis.
  JOURNAL   Phytochemistry 21 (1982) 1969-1974.
  ORGANISM  Zea mays [GN:ezma]
PATHWAY     PATH: map00100  Biosynthesis of steroids
ORTHOLOGY   KO: K08246  cycloeucalenol cycloisomerase
GENES       ATH: AT5G50375(CPI1)
DBLINKS     IUBMB Enzyme Nomenclature: 5.5.1.9
            ExPASy - ENZYME nomenclature database: 5.5.1.9
            ExplorEnz - The Enzyme Database: 5.5.1.9
            ERGO genome analysis and discovery system: 5.5.1.9
            BRENDA, the Enzyme Database: 5.5.1.9
            CAS: 60496-19-7
///
ENTRY       EC 5.5.1.10                 Enzyme
NAME        alpha-pinene-oxide decyclase;
            alpha-pinene oxide lyase
CLASS       Isomerases;
            Intramolecular lyases;
            Intramolecular lyases (only sub-subclass identified to date)
SYSNAME     alpha-pinene-oxide lyase (decyclizing)
REACTION    alpha-pinene oxide = (Z)-2-methyl-5-isopropylhexa-2,5-dienal
            [RN:R04040]
ALL_REAC    R04040
SUBSTRATE   alpha-pinene oxide
PRODUCT     (Z)-2-methyl-5-isopropylhexa-2,5-dienal [CPD:C04435]
COMMENT     Both rings of pinene are cleaved in the reaction.
REFERENCE   1  [PMID:3667522]
  AUTHORS   Griffiths ET, Harries PC, Jeffcoat R, Trudgill PW.
  TITLE     Purification and properties of alpha-pinene oxide lyase from
            Nocardia sp. strain P18.3.
  JOURNAL   J. Bacteriol. 169 (1987) 4980-3.
  ORGANISM  Nocardia sp.
PATHWAY     PATH: map00903  Limonene and pinene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 5.5.1.10
            ExPASy - ENZYME nomenclature database: 5.5.1.10
            ExplorEnz - The Enzyme Database: 5.5.1.10
            ERGO genome analysis and discovery system: 5.5.1.10
            UM-BBD (Biocatalysis/Biodegradation Database): 5.5.1.10
            BRENDA, the Enzyme Database: 5.5.1.10
            CAS: 112692-50-9
///
ENTRY       EC 5.5.1.11                 Enzyme
NAME        dichloromuconate cycloisomerase
CLASS       Isomerases;
            Intramolecular lyases;
            Intramolecular lyases (only sub-subclass identified to date)
SYSNAME     2,4-dichloro-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
REACTION    2,4-dichloro-2,5-dihydro-5-oxofuran-2-acetate =
            2,4-dichloro-cis,cis-muconate [RN:R04345]
ALL_REAC    R04345;
            (other) R05393
SUBSTRATE   2,4-dichloro-2,5-dihydro-5-oxofuran-2-acetate [CPD:C04625]
PRODUCT     2,4-dichloro-cis,cis-muconate [CPD:C03918]
COFACTOR    Manganese [CPD:C00034]
COMMENT     Requires Mn2+. The product of cyclisomerization of
            dichloro-cis,cis-muconate spontaneously eliminates chloride to
            produce cis-4-carboxymethylene-3-chlorobut-2-en-4-olide. Also acts,
            in the reverse direction, on cis,cis-muconate and its
            monochloro-derivatives, but with lower affinity. Not identical with
            EC 5.5.1.1 (muconate cycloisomerase) or EC 5.5.1.7 (chloromuconate
            cycloisomerase).
REFERENCE   1  [PMID:2327971]
  AUTHORS   Kuhm AE, Schlomann M, Knackmuss HJ, Pieper DH.
  TITLE     Purification and characterization of dichloromuconate cycloisomerase
            from Alcaligenes eutrophus JMP 134.
  JOURNAL   Biochem. J. 266 (1990) 877-83.
  ORGANISM  Alcaligenes eutrophus
PATHWAY     PATH: map00627  1,4-Dichlorobenzene degradation
DBLINKS     IUBMB Enzyme Nomenclature: 5.5.1.11
            ExPASy - ENZYME nomenclature database: 5.5.1.11
            ExplorEnz - The Enzyme Database: 5.5.1.11
            ERGO genome analysis and discovery system: 5.5.1.11
            UM-BBD (Biocatalysis/Biodegradation Database): 5.5.1.11
            BRENDA, the Enzyme Database: 5.5.1.11
            CAS: 126904-95-8
///
ENTRY       EC 5.5.1.12                 Enzyme
NAME        copalyl diphosphate synthase
CLASS       Isomerases;
            Intramolecular lyases;
            Intramolecular lyases (only sub-subclass identified to date)
SYSNAME     (+)-copalyl-diphosphate lyase (decyclizing)
REACTION    geranylgeranyl diphosphate = (+)-copalyl diphosphate [RN:R06298]
ALL_REAC    R06298
SUBSTRATE   geranylgeranyl diphosphate [CPD:C00353]
PRODUCT     (+)-copalyl diphosphate [CPD:C11901]
COMMENT     Part of a bifunctional enzyme involved in the biosynthesis of
            abietadiene. See also EC 4.2.3.18 (abietadiene synthase)
REFERENCE   1  [PMID:11112547]
  AUTHORS   Peters RJ, Flory JE, Jetter R, Ravn MM, Lee HJ, Coates RM, Croteau
            RB.
  TITLE     Abietadiene synthase from grand fir (Abies grandis):
            characterization and mechanism of action of the
            &quot;pseudomature&quot; recombinant enzyme.
  JOURNAL   Biochemistry. 39 (2000) 15592-602.
  ORGANISM  Abies grandis
REFERENCE   2  [PMID:11552804]
  AUTHORS   Peters RJ, Ravn MM, Coates RM, Croteau RB.
  TITLE     Bifunctional abietadiene synthase: free diffusive transfer of the
            (+)-copalyl diphosphate intermediate between two distinct active
            sites.
  JOURNAL   J. Am. Chem. Soc. 123 (2001) 8974-8.
  ORGANISM  Abies grandis
REFERENCE   3  [PMID:11805316]
  AUTHORS   Peters RJ, Croteau RB.
  TITLE     Abietadiene synthase catalysis: mutational analysis of a prenyl
            diphosphate ionization-initiated cyclization and rearrangement.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 580-4.
  ORGANISM  Abies grandis
REFERENCE   4  [PMID:12059223]
  AUTHORS   Ravn MM, Peters RJ, Coates RM, Croteau R.
  TITLE     Mechanism of abietadiene synthase catalysis: stereochemistry and
            stabilization of the cryptic pimarenyl carbocation intermediates.
  JOURNAL   J. Am. Chem. Soc. 124 (2002) 6998-7006.
  ORGANISM  Abies grandis
REFERENCE   5  [PMID:11827528]
  AUTHORS   Peters RJ, Croteau RB.
  TITLE     Abietadiene synthase catalysis: conserved residues involved in
            protonation-initiated cyclization of geranylgeranyl diphosphate to
            (+)-copalyl diphosphate.
  JOURNAL   Biochemistry. 41 (2002) 1836-42.
  ORGANISM  Abies grandis
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 5.5.1.12
            ExPASy - ENZYME nomenclature database: 5.5.1.12
            ExplorEnz - The Enzyme Database: 5.5.1.12
            ERGO genome analysis and discovery system: 5.5.1.12
            BRENDA, the Enzyme Database: 5.5.1.12
            CAS: 157972-08-2
///
ENTRY       EC 5.5.1.13                 Enzyme
NAME        ent-copalyl diphosphate synthase;
            ent-kaurene synthase A;
            ent-kaurene synthetase A
CLASS       Isomerases;
            Intramolecular lyases;
            Intramolecular lyases (only sub-subclass identified to date)
SYSNAME     ent-copalyl-diphosphate lyase (decyclizing)
REACTION    geranylgeranyl diphosphate = ent-copalyl diphosphate [RN:R02068]
ALL_REAC    R02068
SUBSTRATE   geranylgeranyl diphosphate [CPD:C00353]
PRODUCT     ent-copalyl diphosphate [CPD:C06089]
COMMENT     Part of a bifunctional enzyme involved in the biosynthesis of
            kaurene. See also EC 4.2.3.19 (ent-kaurene synthase)
REFERENCE   1  [PMID:4331199]
  AUTHORS   Fall RR, West CA.
  TITLE     Purification and properties of kaurene synthetase from Fusarium
            moniliforme.
  JOURNAL   J. Biol. Chem. 246 (1971) 6913-28.
  ORGANISM  Fusarium moniliforme
REFERENCE   2  [PMID:7994182]
  AUTHORS   Sun TP, Kamiya Y.
  TITLE     The Arabidopsis GA1 locus encodes the cyclase ent-kaurene synthetase
            A of gibberellin biosynthesis.
  JOURNAL   Plant. Cell. 6 (1994) 1509-18.
  ORGANISM  Pisum sativum
REFERENCE   3  [PMID:9268298]
  AUTHORS   Kawaide H, Imai R, Sassa T, Kamiya Y.
  TITLE     Ent-kaurene synthase from the fungus Phaeosphaeria sp. L487. cDNA
            isolation, characterization, and bacterial expression of a
            bifunctional diterpene cyclase in fungal gibberellin biosynthesis.
  JOURNAL   J. Biol. Chem. 272 (1997) 21706-12.
  ORGANISM  Phaeosphaeria sp.
REFERENCE   4  [PMID:10803977]
  AUTHORS   Toyomasu T, Kawaide H, Ishizaki A, Shinoda S, Otsuka M, Mitsuhashi
            W, Sassa T.
  TITLE     Cloning of a full-length cDNA encoding ent-kaurene synthase from
            Gibberella fujikuroi: functional analysis of a bifunctional
            diterpene cyclase.
  JOURNAL   Biosci. Biotechnol. Biochem. 64 (2000) 660-4.
  ORGANISM  Gibberella fujikuroi
PATHWAY     PATH: map00904  Diterpenoid biosynthesis
ORTHOLOGY   KO: K04120  ent-copalyl diphosphate synthase
GENES       ATH: AT4G02780(GA1)
DBLINKS     IUBMB Enzyme Nomenclature: 5.5.1.13
            ExPASy - ENZYME nomenclature database: 5.5.1.13
            ExplorEnz - The Enzyme Database: 5.5.1.13
            ERGO genome analysis and discovery system: 5.5.1.13
            BRENDA, the Enzyme Database: 5.5.1.13
            CAS: 9055-64-5
///
ENTRY       EC 5.5.1.-                  Enzyme
CLASS       Isomerases;
            Intramolecular lyases
REACTION    (1) 3-Sulfomuconate <=> 4-Sulfolactone [RN:R05394];
            (2) Cyclopropanecarboxyl-CoA <=> Crotonoyl-CoA [RN:R07829]
SUBSTRATE   3-Sulfomuconate [CPD:C06675]
PRODUCT     4-Sulfolactone [CPD:C06676]
///
ENTRY       EC 5.99.1.1                 Enzyme
NAME        thiocyanate isomerase;
            isothiocyanate isomerase
CLASS       Isomerases;
            Other isomerases;
            Sole sub-subclass for isomerases that do not belong in the other
            subclasses
SYSNAME     benzyl-thiocyanate isomerase
REACTION    benzyl isothiocyanate = benzyl thiocyanate [RN:R04010]
ALL_REAC    R04010
SUBSTRATE   benzyl isothiocyanate [CPD:C03098]
PRODUCT     benzyl thiocyanate [CPD:C02660]
REFERENCE   1
  AUTHORS   Virtanen, A.I.
  TITLE     On enzymic and chemical reactions in crushed plants.
  JOURNAL   Arch. Biochem. Biophys. Suppl. 1 (1962) 200-208.
DBLINKS     IUBMB Enzyme Nomenclature: 5.99.1.1
            ExPASy - ENZYME nomenclature database: 5.99.1.1
            ExplorEnz - The Enzyme Database: 5.99.1.1
            ERGO genome analysis and discovery system: 5.99.1.1
            BRENDA, the Enzyme Database: 5.99.1.1
            CAS: 9023-71-6
///
ENTRY       EC 5.99.1.2                 Enzyme
NAME        DNA topoisomerase;
            type I DNA topoisomerase;
            untwisting enzyme;
            relaxing enzyme;
            nicking-closing enzyme;
            swivelase;
            omega-protein;
            deoxyribonucleate topoisomerase;
            topoisomerase;
            type I DNA topoisomerase
CLASS       Isomerases;
            Other isomerases;
            Sole sub-subclass for isomerases that do not belong in the other
            subclasses
SYSNAME     DNA topoisomerase
REACTION    ATP-independent breakage of single-stranded DNA, followed by passage
            and rejoining
INHIBITOR   Camptothecin [CPD:C01897]
COMMENT     These enzymes bring about the conversion of one topological isomer
            of DNA into another, e.g., the relaxation of superhelical turns in
            DNA, the interconversion of simple and knotted rings of
            single-stranded DNA, and the intertwisting of single-stranded rings
            of complementary sequences, cf. EC 5.99.1.3 DNA topoisomerase
            (ATP-hydrolysing).
REFERENCE   1  [PMID:6267993]
  AUTHORS   Gellert M.
  TITLE     DNA topoisomerases.
  JOURNAL   Annu. Rev. Biochem. 50 (1981) 879-910.
ORTHOLOGY   KO: K01862  DNA topoisomerase type I
            KO: K03163  DNA topoisomerase I
            KO: K03165  DNA topoisomerase III
            KO: K03168  DNA topoisomerase I
            KO: K03169  DNA topoisomerase III
GENES       HSA: 116447(TOP1MT) 7150(TOP1) 7156(TOP3A) 8940(TOP3B)
            PTR: 458252(TOP1) 472883(TOP1MT)
            MMU: 21969(Top1) 21975(Top3a) 21976(Top3b) 72960(Top1mt)
            RNO: 300029(Top1mt) 64550(Top1)
            CFA: 477229(TOP1) 477576(TOP3B) 489537(TOP3A)
            BTA: 534799(LOC534799)
            GGA: 396004(TOP1) 408025(TOP1MT) 416517(TOP3A) 416771(TOP3B)
            XLA: 398564(MGC53016) 444125(MGC80537)
            DRE: 553496(top1l)
            SPU: 576420(LOC576420) 576753(LOC576753) 588512(LOC588512)
                 591288(LOC591288)
            DME: Dmel_CG10123(Top3alpha) Dmel_CG3458(Top3beta)
                 Dmel_CG6146(Top1)
            CEL: M01E5.5(top-1) Y48C3A.14 Y56A3A.27(top-3)
            ATH: AT5G55300(TOP1BETA)
            OSA: 4340762 4344685 4347482
            CME: CMG056C CMI252C CMM263C
            SCE: YLR234W(TOP3) YOL006C(TOP1)
            AGO: AGOS_ACL008C AGOS_AGL101C
            PIC: PICST_34564(TOP3) PICST_46944(TOP1)
            CAL: CaO19.96 CaO19_5934(CaO19.5934)
            CGR: CAGL0E02431g CAGL0G08470g CAGL0J11660g
            SPO: SPBC16G5.12c(top3) SPBC1703.14c(top1)
            ANI: AN0253.2 AN4555.2
            AFM: AFUA_1G02020 AFUA_1G03500 AFUA_2G02660
            AOR: AO090005000750 AO090026000611
            CNE: CNI03280 CNJ00400
            UMA: UM05101.1
            ECU: ECU04_1070
            DDI: DDBDRAFT_0185416 DDBDRAFT_0217608
            PFA: PF13_0251 PFE0520c
            CPV: cgd7_3350
            CHO: Chro.50266 Chro.50267 Chro.60278 Chro.70373
            TAN: TA11835 TA17755
            TPV: TP02_0198 TP03_0692
            TET: TTHERM_00464990 TTHERM_01262890 TTHERM_01299650
            TBR: Tb09.160.5070 Tb11.01.0910 Tb11.01.1280 Tb927.4.1330
            TCR: 506625.110 508693.20 508851.170 510121.160 510901.100
                 511589.120
            LMA: LmjF04.0060 LmjF28.1780 LmjF34.3440 LmjF36.3200
            EHI: 111.t00004 7.t00040
            ECO: b1274(topA) b1763(topB)
            ECJ: JW1266(topA) JW1752(topB)
            ECE: Z2536(topA) Z2796(topB)
            ECS: ECs1846 ECs2469
            ECC: c1741(topA) c2166(topB)
            ECI: UTI89_C1543(topA) UTI89_C1958(topB)
            ECP: ECP_1325 ECP_1711
            ECV: APECO1_434(topA) APECO1_832(topB)
            ECW: EcE24377A_1474(topA) EcE24377A_1986(topB)
            ECX: EcHS_A1383(topA) EcHS_A1847(topB)
            STY: STY1336(topA) STY1816(topB) STY4530(topB)
            STT: t1177(topB) t1627(topA) t4234(topB)
            SPT: SPA1162(topA) SPA1546(topB)
            SEC: SC1320(topB) SC1711(topA)
            STM: STM1298(topB) STM1714(topA)
            YPE: YPO2165(topB) YPO2218(topA)
            YPK: y2060(topA) y2156(topB)
            YPM: YP_1965(topB) YP_2016(topA2)
            YPA: YPA_1522 YPA_1577
            YPN: YPN_1631 YPN_1686
            YPP: YPDSF_0917 YPDSF_0969
            YPS: YPTB2091(topB) YPTB2140(topA) pYptb0031(topB)
            YPI: YpsIP31758_1923(topA) YpsIP31758_1979(topB)
            SFL: SF1276(topA) SF1460(topB)
            SFX: S1361(topA) S1575(topB)
            SFV: SFV_1285(topA) SFV_1454(topB)
            SSN: SSON_1392(topB) SSON_1869(topA)
            SBO: SBO_1324(topB) SBO_1792(topA)
            SDY: SDY_1344(topA) SDY_1510(topB)
            ECA: ECA0525(topB) ECA2286(topA) ECA2337(topB)
            PLU: plu1037 plu2435(topA) plu2550(topB)
            BUC: BU284(topA)
            BAS: BUsg273(topA)
            SGL: SG1361 SG1408
            ENT: Ent638_1684 Ent638_2196
            SPE: Spro_0310 Spro_4107
            HIN: HI0444(topB) HI1365(topA)
            HIT: NTHI0112(topB2) NTHI0571(topB) NTHI1799(topA)
            HIP: CGSHiEE_04365
            HIQ: CGSHiGG_00490
            HDU: HD0954(topB1) HD1276(topB2) HD1385(topA)
            HSO: HS_0914(topA) HS_1310(topB) HS_1737(topA)
            PMU: PM0207(topB) PM0615(topA)
            MSU: MS0730(topA) MS1096(topA)
            APL: APL_0696(topA) APL_0744(topB2)
            ASU: Asuc_1399 Asuc_1706
            XFA: XF0920 XF1776 XF2059 XFa0003
            XFT: PD1023(traE) PD1767(topA)
            XCC: XCC3755(topA)
            XCB: XC_2064 XC_3825
            XCV: XCV2287(topB) XCV2406(topB2) XCV3932(topA) XCVd0036
                 XCVd0152(traE)
            XAC: XAC2212(topB) XAC3807(topA)
            XOO: XOO0579(topA)
            XOM: XOO_0540(XOO0540)
            VCH: VC1730 VC2043
            VCO: VC0395_A1332(topA) VC0395_A1630(topB)
            VVU: VV1_2130 VV1_3130
            VVY: VV1155 VV2314
            VPA: VP1022 VP2149
            VFI: VF1051 VF1641 VFB46
            PPR: PBPRA2477(topA) PBPRA2590
            PAE: PA3011(topA)
            PAU: PA14_25110(topA) PA14_59180
            PAP: PSPA7_2148(topA) PSPA7_4465
            PPU: PP_2139(topA) PP_4019(topB)
            PPF: Pput_1814 Pput_1939 Pput_2923 Pput_3603
            PST: PSPTO_2478(topB) PSPTO_3514(topA)
            PSB: Psyr_1473 Psyr_2244 Psyr_3287
            PSP: PSPPH_0752 PSPPH_2943(topB1) PSPPH_3207(topA)
                 PSPPH_B0043(topB2)
            PFL: PFL_1942(topA) PFL_4672(topA)
            PFO: Pfl_3001 Pfl_3364 Pfl_3876
            PEN: PSEEN2193(topB) PSEEN2283 PSEEN3725(topA)
            PMY: Pmen_1583 Pmen_2775
            PAR: Psyc_1660(topA)
            PCR: Pcryo_1901
            PRW: PsycPRwf_0393
            ACI: ACIAD0493(topA)
            SON: SO_2705(topA) SO_3061(topB)
            SDN: Sden_2328 Sden_2400
            SFR: Sfri_1401 Sfri_2478
            SAZ: Sama_1322 Sama_2145
            SBL: Sbal_2496 Sbal_2736 Sbal_4425
            SBM: Shew185_2489 Shew185_2753
            SLO: Shew_2224 Shew_2299
            SPC: Sputcn32_2250 Sputcn32_2435
            SSE: Ssed_1658 Ssed_2841
            SPL: Spea_1535 Spea_1625
            SHE: Shewmr4_1433 Shewmr4_1585
            SHM: Shewmr7_1498 Shewmr7_1660
            SHN: Shewana3_1486 Shewana3_1729
            SHW: Sputw3181_1573 Sputw3181_1758
            ILO: IL1010(topA)
            CPS: CPS_1197(topA) CPS_4792(topB)
            PHA: PSHAa1348(topA) PSHAa2345 PSHAa2356(topB)
            PAT: Patl_0776 Patl_2356
            SDE: Sde_1542 Sde_1783
            PIN: Ping_1971 Ping_2461
            MAQ: Maqu_1146 Maqu_2529 Maqu_4200
            CBU: CBU_2000(topA)
            CBD: COXBU7E912_2100(topA)
            LPN: lpg2599(topA)
            LPF: lpl2522(topA)
            LPP: lpp2652(topA)
            MCA: MCA2839(topA)
            FTU: FTT0906c(topA)
            FTF: FTF0906c(topA)
            FTW: FTW_1273(topA)
            FTL: FTL_0426
            FTH: FTH_0419(topA)
            FTA: FTA_0448(topA)
            FTN: FTN_0432(topA)
            TCX: Tcr_0196
            NOC: Noc_3010
            AEH: Mlg_2632
            HHA: Hhal_2326
            HCH: HCH_04752(topA)
            CSA: Csal_1560 Csal_2146
            ABO: ABO_1012(topA)
            MMW: Mmwyl1_2114 Mmwyl1_3275
            AHA: AHA_3104(topA) AHA_4047(topB)
            DNO: DNO_0152(topA)
            BCI: BCI_0302(topA)
            RMA: Rmag_1034
            VOK: COSY_0936(topA)
            NME: NMB0118
            NMA: NMA0156(topA)
            NMC: NMC0110(topA)
            NGO: NGO1863(topA)
            CVI: CV_4269(topA)
            RSO: RSc0066(topB)
            REU: Reut_A3412 Reut_D6523
            REH: H16_A1489 H16_A3704(topB)
            RME: Rmet_2298 Rmet_3569
            BMA: BMA0139(topB)
            BMV: BMASAVP1_A2810(topB)
            BML: BMA10299_A2271(topB)
            BMN: BMA10247_2348(topB)
            BXE: Bxe_A1223 Bxe_A4419
            BVI: Bcep1808_2123 Bcep1808_3289 Bcep1808_6722 Bcep1808_7313
                 Bcep1808_7656
            BUR: Bcep18194_A6481
            BCN: Bcen_2517
            BCH: Bcen2424_3130
            BAM: Bamb_3185 Bamb_6614
            BPS: BPSL0118
            BPM: BURPS1710b_0343(topB)
            BPL: BURPS1106A_0155(topB)
            BPD: BURPS668_0146(topB)
            BTE: BTH_I0125
            PNU: Pnuc_2081
            BPE: BP0460(topB)
            BPA: BPP4374(topB)
            BBR: BB4960(topB)
            RFR: Rfer_3955
            POL: Bpro_4713
            PNA: Pnap_3963
            AAV: Aave_0558 Aave_4627
            AJS: Ajs_1311 Ajs_1445 Ajs_2233 Ajs_3990 Ajs_4319
            VEI: Veis_3177
            MPT: Mpe_A0265 Mpe_A2342 Mpe_B0401
            HAR: HEAR1978(topB)
            MMS: mma_0139(topB)
            NEU: NE1966(topB)
            NET: Neut_0116 Neut_0396
            NMU: Nmul_A0396
            EBA: ebA2458(topB1) ebA2963(topB2) p1B145(topA) p2B17(traE)
            AZO: azo0095
            DAR: Daro_0018
            TBD: Tbd_0010
            MFA: Mfla_0227
            HPY: HP0116(topA) HP0440(topA)
            HPJ: jhp0108(topA_1) jhp0919(topA_2) jhp0931(topA_3)
            HPA: HPAG1_0116
            HHE: HH1798(topA)
            HAC: Hac_1475(topA)
            WSU: WS1501(topA)
            TDN: Tmden_0171
            CJE: Cj1686c(topA)
            CJR: CJE1854(topA)
            CJJ: CJJ81176_1678(topA) CJJ81176_pTet0045 CJJ81176_pVir0012
            CJU: C8J_1583(topA)
            CJD: JJD26997_2058(topA)
            CFF: CFF8240_0175(topA)
            CCV: CCV52592_0571(topA)
            CHA: CHAB381_0164 CHAB381_1551(topA)
            CCO: CCC13826_2296(topA)
            ABU: Abu_2235(topA)
            NIS: NIS_1651(topA)
            SUN: SUN_0088(topA)
            GSU: GSU2549(topA)
            GME: Gmet_0891
            GUR: Gura_3689
            PCA: Pcar_0406
            PPD: Ppro_0528
            DVU: DVU2316(topB) DVU3389(topA)
            DVL: Dvul_0011 Dvul_0943
            DDE: Dde_0106 Dde_1318
            LIP: LI0654(topA)
            BBA: Bd0964(topA)
            DPS: DP2617
            ADE: Adeh_2699
            AFW: Anae109_2693
            MXA: MXAN_0535(topB)
            SAT: SYN_01883 SYN_02798
            SFU: Sfum_0213
            RPR: RP326(topA)
            RTY: RT0317(topA)
            RCO: RC0449(topA)
            RFE: RF_0530(topA)
            RBE: RBE_0712(topA)
            RAK: A1C_02440
            RBO: A1I_04655
            RRI: A1G_02540
            OTS: OTBS_1844(topA)
            WOL: WD1133(topA)
            WBM: Wbm0037(topA)
            AMA: AM502(topA)
            APH: APH_0597(topA)
            ERU: Erum3400(topA)
            ERW: ERWE_CDS_03470(topA)
            ERG: ERGA_CDS_03430(topA)
            ECN: Ecaj_0323
            ECH: ECH_0750(topA)
            NSE: NSE_0594(topA)
            PUB: SAR11_1083(topA)
            MLO: mlr0839
            MES: Meso_1354
            PLA: Plav_3385
            SME: SMb21445 SMc01364(topA)
            ATU: Atu1304(topA)
            ATC: AGR_C_2398
            RET: RHE_CH01638(topA) RHE_PE00209
            RLE: RL1735(topA) pRL110305
            BME: BMEII0666
            BMF: BAB2_0636
            BMS: BRA0604(topA)
            BMB: BruAb2_0620(topA)
            BOV: BOV_A0569(topA)
            BJA: bll0572 blr5111(topA)
            BRA: BRADO4508(topA)
            BBT: BBta_4733(topA)
            RPA: RPA3124(topA) RPA4136
            RPB: RPB_2419
            RPC: RPC_2239
            RPD: RPD_3033
            RPE: RPE_3379
            NWI: Nwi_1712
            NHA: Nham_2437
            BHE: BH08160(topA)
            BQU: BQ06420(topA)
            BBK: BARBAKC583_0843(topA)
            CCR: CC_2451
            SIL: SPO3079(topA)
            SIT: TM1040_2339
            RSP: RSP_0946 RSP_2178(topA)
            RSH: Rsph17029_0850
            JAN: Jann_0278 Jann_3160
            RDE: RD1_2131(topA)
            PDE: Pden_0659
            MMR: Mmar10_1282
            HNE: HNE_2276(topA)
            ZMO: ZMO1193(topA)
            NAR: Saro_1803
            SAL: Sala_1211
            SWI: Swit_3826
            ELI: ELI_04810
            GOX: GOX1257 GOX1263 GOX1374
            GBE: GbCGDNIH1_0804
            ACR: Acry_0729
            RRU: Rru_A3202
            MAG: amb0682
            MGM: Mmc1_2541 Mmc1_3660
            ABA: Acid345_3340
            SUS: Acid_2399 Acid_7732
            BSU: BG11007(topA) BG11979(topB)
            BHA: BH2467(topA) BH3387(topB)
            BAN: BA0375(topB-1) BA1905(topB-2) BA3971(topA)
            BAR: GBAA0375(topB-1) GBAA1905(topB-2) GBAA3971(topA)
            BAA: BA_2409 BA_4441
            BAT: BAS0361 BAS1767 BAS3684
            BCE: BC0417 BC1832 BC3831
            BCA: BCE_0485(topB) BCE_1984 BCE_3875(topA) BCE_A0140
            BCZ: BCZK0347(topB) BCZK1725(topB) BCZK3592(topA)
            BCY: Bcer98_1472 Bcer98_2485
            BTK: BT9727_0351(topB) BT9727_1589(topB) BT9727_1744(topB)
                 BT9727_3574(topA) pBT9727_0072(topA)
            BTL: BALH_0373(topB) BALH_1686(topB)
            BLI: BL01281(topA) BL02823(topB)
            BLD: BLi00518(topB) BLi01832(topA)
            BCL: ABC2119 ABC2278(topA) ABC3953(topB)
            BAY: RBAM_004480(topB) RBAM_015950(topA)
            BPU: BPUM_0400(topB) BPUM_1510(topA)
            OIH: OB1546(topA) OB2590(topB)
            GKA: GK1211(topA) GK1688 GK1815
            SAU: SA1093 SA2051(topB)
            SAV: SAV1250 SAV2254(topB)
            SAM: MW1133 MW2173(topB)
            SAR: SAR1226(topA) SAR2339
            SAS: SAS1184 SAS2145
            SAC: SACOL1267(topA) SACOL2243(topB)
            SAB: SAB1112(topA) SAB2126c
            SAA: SAUSA300_1143(topA) SAUSA300_2208(topB)
                 SAUSA300_pUSA0318(traI)
            SAO: SAOUHSC_01222 SAOUHSC_02517
            SAJ: SaurJH9_1310 SaurJH9_2281
            SAH: SaurJH1_1335 SaurJH1_2322
            SEP: SE0926 SE1482 SE1828
            SER: SERP0816(topA) SERP1836(topB)
            SHA: SH0798(topB) SH1664(topA)
            SSP: SSP0659 SSP1518
            LMO: lmo1275(topA) lmo2756(topB)
            LMF: LMOf2365_1293(topA) LMOf2365_2744(topB)
            LIN: lin1314(topA)
            LWE: lwe1292(topA) lwe2703(topB)
            LLA: L0298(topA)
            LLC: LACR_1304
            LLM: llmg_1272(topA) llmg_1374(ltrE)
            SPY: SPy_1164(topA)
            SPZ: M5005_Spy_0885
            SPM: spyM18_1124(topA)
            SPG: SpyM3_0820(topA)
            SPS: SPs1021
            SPH: MGAS10270_Spy0999
            SPI: MGAS10750_Spy1034 MGAS10750_Spy1696
            SPJ: MGAS2096_Spy0959
            SPK: MGAS9429_Spy1003
            SPF: SpyM50905(topA)
            SPA: M6_Spy0881
            SPB: M28_Spy0859
            SPN: SP_1263
            SPR: spr1141(topA)
            SPD: SPD_1120(topA)
            SAG: SAG1005(topA)
            SAN: gbs1040
            SAK: SAK_1100(topA)
            SMU: SMU.1002(topA)
            STC: str0897(topA)
            STL: stu0897(topA)
            SSA: SSA_1184(topA)
            SGO: SGO_1197(topA)
            LPL: lp_1850(topA) pWCFS103_22(traI)
            LJO: LJ1108
            LAC: LBA0981
            LSA: LSA0761(topB) LSA0989(topA)
            LSL: LSL_0720(topA) LSL_1306(topB)
            LDB: Ldb1273(topA)
            LBU: LBUL_1190 LBUL_1348
            LBR: LVIS_0798
            LCA: LSEI_1401
            LRE: Lreu_0779
            EFA: EF1650(topA) EF2064(topB-1) EF2312(topB-2)
            OOE: OEOE_0093 OEOE_1021
            STH: STH1481 STH1672
            CAC: CAC1785(topA) CAC2947(topB) CAC3567(topB)
            CPE: CPE1508(topB) CPE1702(topA) CPE1983(topB)
            CPF: CPF_1760(topB) CPF_1956(topA)
            CPR: CPR_1489(topB) CPR_1674(topA)
            CTC: CTC00403 CTC01259 CTC01836
            CNO: NT01CX_0335 NT01CX_2151(topA)
            CTH: Cthe_0460 Cthe_2509
            CDF: CD1274(topA)
            CBA: CLB_1317(topB) CLB_2301(topA)
            CBH: CLC_1327(topB) CLC_2285(topA)
            CBF: CLI_1374(topB) CLI_2493(topA)
            CBE: Cbei_0868 Cbei_1186
            CKL: CKL_0559(topA1) CKL_1068(topA2)
            AMT: Amet_2735
            CHY: CHY_1794(topA)
            DSY: DSY2072 DSY2554 DSY4907
            DRM: Dred_0974 Dred_1853 Dred_1984 Dred_3223
            SWO: Swol_0497 Swol_0840
            CSC: Csac_1249
            TTE: TTE1449(topA)
            MTA: Moth_0349 Moth_1026
            MGE: MG_122(topA)
            MPN: MPN261(topA)
            MPU: MYPU_4710(topA)
            MPE: MYPE4140(topA)
            MGA: MGA_0454(topA)
            MMY: MSC_0931(topA)
            MMO: MMOB0820(topA)
            MHY: mhp097(topA)
            MHJ: MHJ_0275(topA)
            MHP: MHP7448_0283(topA)
            MSY: MS53_0531(topA)
            MCP: MCAP_0792(topA)
            UUR: UU590(topA)
            POY: PAM279(topA)
            AYW: AYWB_442(topA)
            MFL: Mfl654
            MTU: Rv3646c(topA)
            MTC: MT3749(topA)
            MBO: Mb3670c(topA)
            MBB: BCG_3704c(topA)
            MLE: ML0200(topA)
            MPA: MAP0425(topA)
            MAV: MAV_0519(topA)
            MSM: MSMEG_6157(topA)
            MUL: MUL_4222(topA)
            MVA: Mvan_5396
            MGI: Mflv_1394
            MMC: Mmcs_4796
            MKM: Mkms_4882
            MJL: Mjls_5182
            CGL: NCgl0304(cgl0309) NCgl1769(cgl1843)
            CGB: cg0373(topA) cg2064
            CEF: CE0307
            CDI: DIP0327(topA)
            CJK: jk1954(topA)
            NFA: nfa3670(topA)
            RHA: RHA1_ro04353
            SCO: SCO3543(SCH5.06c)
            SMA: SAV4621(topA)
            TWH: TWT696(topA)
            TWS: TW715(topA)
            LXX: Lxx04060(topA)
            CMI: CMM_0927(topA)
            ART: Arth_3355
            AAU: AAur_3334(topA)
            PAC: PPA0241
            NCA: Noca_0378
            TFU: Tfu_2784
            FRA: Francci3_4305
            FAL: FRAAL3903 FRAAL6579(topA)
            ACE: Acel_1972
            SEN: SACE_0377(topA)
            STP: Strop_4027
            BLO: BL0485(topA) BL1469(topB)
            BAD: BAD_0161(topA)
            RXY: Rxyl_0752 Rxyl_1964
            FNU: FN1069
            RBA: RB7957(topA)
            CTR: CT643(topA)
            CTA: CTA_0698(topA)
            CMU: TC0012
            CPN: CPn0769(topA)
            CPA: CP1103
            CPJ: CPj0769(topA)
            CPT: CpB0796
            CCA: CCA00988(topA)
            CAB: CAB958(topA)
            CFE: CF0025(topA)
            PCU: pc0071(topA)
            BBU: BB0828(topA)
            BGA: BG0853(topA)
            BAF: BAPKO_0881(topA)
            TPA: TP0394
            TDE: TDE1208(topA)
            LIL: LA1721(topA)
            LIC: LIC12080(topA)
            LBJ: LBJ_1228(topA)
            LBL: LBL_1279(topA)
            SYN: slr2058(topA)
            SYW: SYNW1872(topA)
            SYC: syc0139_c(topA)
            SYF: Synpcc7942_1416
            SYD: Syncc9605_0597
            SYE: Syncc9902_1765
            SYG: sync_2114(topA)
            SYR: SynRCC307_0660(topA)
            SYX: SynWH7803_1883(topA)
            CYA: CYA_0561(topA)
            CYB: CYB_2358(topA)
            TEL: tll1881(topA)
            GVI: gll1020(topA) glr3198(topA)
            ANA: all2631 alr2780
            AVA: Ava_0030 Ava_3784
            PMA: Pro0432(topA)
            PMM: PMM0436(topA)
            PMT: PMT1353(topA)
            PMN: PMN2A_1768
            PMI: PMT9312_0435
            PMB: A9601_04911(topA)
            PMC: P9515_04981(topA)
            PMF: P9303_06301(topA)
            PMG: P9301_04601(topA)
            PME: NATL1_04911(topA)
            TER: Tery_0027
            BTH: BT_0105 BT_2089 BT_2324 BT_2827
            BFR: BF3798 BF4419
            BFS: BF1254(exc) BF1736(top1) BF3590 BF4217(topA)
            PGI: PG0104(topB-1) PG0754(topA) PG1495(topB-2)
            SRU: SRU_1118(topA)
            CHU: CHU_2343(topA) CHU_3602(topB)
            GFO: GFO_1903 GFO_3017(topA)
            FJO: Fjoh_1851 Fjoh_2289 Fjoh_3021
            FPS: FP1975(topA)
            CTE: CT0055(topA)
            CCH: Cag_0075
            CPH: Cpha266_0109
            PVI: Cvib_1714
            PLT: Plut_2073
            DET: DET0717(topA)
            DEH: cbdb_A674(topA)
            DEB: DehaBAV1_0652
            RRS: RoseRS_1430
            RCA: Rcas_1690
            DRA: DR_1374
            DGE: Dgeo_2001
            TTH: TTC1931
            TTJ: TTHA0074
            AAE: aq_657(topA)
            TMA: TM0258
            TPT: Tpet_0666
            TME: Tmel_1024
            FNO: Fnod_1027
            MJA: MJ1652(topA)
            MMP: MMP0956(topA)
            MMQ: MmarC5_0781
            MAC: MA1789(topA) MA2510(topA)
            MBA: Mbar_A2128 Mbar_A2410
            MMA: MM_0183 MM_3076
            MBU: Mbur_0095 Mbur_0705
            MTP: Mthe_0595
            MHU: Mhun_1011
            MEM: Memar_0770
            MBN: Mboo_0859
            MTH: MTH1624
            MST: Msp_0366(topA)
            MSI: Msm_0717
            MKA: MK1604(topA)
            AFU: AF1806(topA)
            HAL: VNG0349Gm(topA)
            HMA: rrnAC1645(topA)
            HWA: HQ1045A(topA) HQ1267A(topA)
            NPH: NP0446A NP1222A(topA)
            TAC: Ta0063
            TVO: TVN0019
            PTO: PTO0747
            PHO: PH0622
            PAB: PAB1430(topA)
            PFU: PF0494
            TKO: TK1091
            RCI: RCIX2309(topA-1) RCIX2432(topA-2)
            APE: APE_1794
            SMR: Smar_0967 Smar_1121 Smar_1271
            HBU: Hbut_0916
            SSO: SSO0907(topA)
            STO: ST1216
            SAI: Saci_1371(top1)
            PAI: PAE2993(topA)
            PIS: Pisl_0392 Pisl_1245
            PCL: Pcal_0692 Pcal_1115
            PAS: Pars_0259 Pars_1359
            TPE: Tpen_0575 Tpen_0885
            NEQ: NEQ045
STRUCTURES  PDB: 1A31  1A35  1A36  1A41  1CY0  1CY1  1CY2  1CY4  1CY6  1CY7  
                 1CY8  1CY9  1CYY  1D6M  1ECL  1EJ9  1I7D  1K4S  1K4T  1LPQ  
                 1MW8  1MW9  1NH3  1OIS  1R49  1RR8  1RRJ  1SC7  1SEU  1T8I  
                 1TL8  1VCC  1YUA  2B9S  2GAI  2GAJ  2H7F  2H7G  2O19  2O54  
                 2O59  2O5C  2O5E  
DBLINKS     IUBMB Enzyme Nomenclature: 5.99.1.2
            ExPASy - ENZYME nomenclature database: 5.99.1.2
            ExplorEnz - The Enzyme Database: 5.99.1.2
            ERGO genome analysis and discovery system: 5.99.1.2
            BRENDA, the Enzyme Database: 5.99.1.2
            CAS: 80449-01-0
///
ENTRY       EC 5.99.1.3                 Enzyme
NAME        DNA topoisomerase (ATP-hydrolysing);
            type II DNA topoisomerase;
            DNA-gyrase;
            deoxyribonucleate topoisomerase;
            deoxyribonucleic topoisomerase;
            topoisomerase;
            DNA topoisomerase II
CLASS       Isomerases;
            Other isomerases;
            Sole sub-subclass for isomerases that do not belong in the other
            subclasses
SYSNAME     DNA topoisomerase (ATP-hydrolysing)
REACTION    ATP-dependent breakage, passage and rejoining of double-stranded DNA
INHIBITOR   Coumermycin A1 [CPD:C05073];
            GRI22222X [CPD:C05075];
            Nalidixic acid [CPD:C05079];
            Novobiocin [CPD:C05080];
            Ciprofloxacin [CPD:C05349]
COMMENT     The enzyme can introduce negative superhelical turns into
            double-stranded circular DNA. One unit has nicking-closing activity,
            and another catalyses super-twisting and hydrolysis of ATP (cf. EC
            5.99.1.2 DNA topoisomerase).
REFERENCE   1  [PMID:6267993]
  AUTHORS   Gellert M.
  TITLE     DNA topoisomerases.
  JOURNAL   Annu. Rev. Biochem. 50 (1981) 879-910.
ORTHOLOGY   KO: K01863  DNA topoisomerase type II
            KO: K02469  DNA gyrase subunit A
            KO: K02470  DNA gyrase subunit B
            KO: K03164  DNA topoisomerase II
            KO: K03166  DNA topoisomerase VI subunit A
            KO: K03167  DNA topoisomerase VI subunit B
            KO: K03170  reverse gyrase
GENES       HSA: 7153(TOP2A) 7155(TOP2B)
            MMU: 21973(Top2a) 21974(Top2b)
            RNO: 360243(Top2a)
            CFA: 477044(TOP2B) 480525(TOP2A)
            SSC: 396917(TOPOII)
            GGA: 395570(TOP2A) 395966(TOP2B)
            XLA: 398512(LOC398512)
            SPU: 578275(LOC578275)
            DME: Dmel_CG10223(Top2)
            CEL: K12D12.1 R05D3.1 T05E11.4(spo-11) ZK1127.7
            ATH: AT3G10270 AT3G10690 AT3G23890(TOPII) AT5G04130
            OSA: 4326261 4330426 4334546
            CME: CMB013C CMH166C CML330C CMS243C
            SCE: YHL022C(SPO11) YNL088W(TOP2)
            AGO: AGOS_ADR025W AGOS_AER410W
            PIC: PICST_74317(TOP2)
            CAL: CaO19.3589 CaO19_2873(CaO19.2873)
            CGR: CAGL0J05610g(TOP1_CANGA)
            SPO: SPAC17A5.11(rec12) SPBC1A4.03c
            ANI: AN5406.2
            AFM: AFUA_5G04070 AFUA_6G13690
            AOR: AO090103000347
            CNE: CNA03600
            ECU: ECU04_0350 ECU04_1110
            DDI: DDB_0214907(topA) DDB_0231510(topB)
            PFA: PF13_0251 PF14_0316 PFL1120c PFL1915w
            CPV: cgd4_780
            CHO: Chro.40097
            TAN: TA13325 TA14985 TA16475
            TPV: TP01_1125 TP02_0467 TP02_0771
            TET: TTHERM_00052080 TTHERM_00456750 TTHERM_00825440
                 TTHERM_01335310
            TBR: Tb09.160.4090 Tb11.01.3390
            TCR: 506445.60 508277.370 508699.10 509203.70
            LMA: LmjF15.1290 LmjF28.2280
            EHI: 138.t00004 46.t00014 73.t00025
            ECO: b2231(gyrA) b3699(gyrB)
            ECJ: JW2225(gyrA) JW5625(gyrB)
            ECE: Z3484(gyrA) Z5190(gyrB)
            ECS: ECs3114 ECs4634
            ECC: c2773(gyrA) c4621(gyrB)
            ECI: UTI89_C2512(gyrA) UTI89_C4249(gyrB)
            ECP: ECP_2274 ECP_3900
            ECV: APECO1_2758(gyrB) APECO1_4329(gyrA)
            ECW: EcE24377A_2526(gyrA) EcE24377A_4209(gyrB)
            ECX: EcHS_A2371(gyrA) EcHS_A3912(gyrB)
            STY: STY2499(gyrA) STY3943(gyrB)
            STT: t0592(gyrA) t3684(gyrB)
            SPT: SPA0592(gyrA) SPA3679(gyrB)
            SEC: SC2275(gyrA) SC3753(gyrB)
            STM: STM2272(gyrA) STM3835(gyrB)
            YPE: YPO1216(gyrA) YPO4094(gyrB)
            YPK: y2972(gyrA) y4110(gyrB)
            YPM: YP_0921(gyrA) YP_4002(gyrB2)
            YPA: YPA_0930 YPA_4140
            YPN: YPN_2761 YPN_3952
            YPP: YPDSF_0004 YPDSF_0450 YPDSF_2477
            YPS: YPTB1256(gyrA) YPTB3940(gyrB)
            YPI: YpsIP31758_2767(gyrA) YpsIP31758_4150(gyrB)
            YEN: YE1395(gyrA)
            SFL: SF2311(gyrA) SF3765(gyrB)
            SFX: S2444(gyrA) S4006(gyrB)
            SFV: SFV_2302(gyrA) SFV_3813(gyrB)
            SSN: SSON_2289(gyrA) SSON_3649(gyrB)
            SBO: SBO_2065(gyrA) SBO_3678(gyrB)
            SDY: SDY_2423(gyrA) SDY_4181(gyrB)
            ECA: ECA1201(gyrA) ECA4438(gyrB)
            PLU: plu0004(gyrB) plu3050(gyrA)
            BUC: BU010(gyrB) BU180(gyrA)
            BAS: BUsg010(gyrB) BUsg174(gyrA)
            BAB: bbp010(gyrB) bbp169(gyrA)
            BCC: BCc_002(gyrB) BCc_116(gyrA)
            WBR: WGLp016(gyrB) WGLp445(gyrA)
            SGL: SG0004 SG1582
            ENT: Ent638_0004 Ent638_3443
            KPN: KPN_04102(gyrB)
            SPE: Spro_0035 Spro_3269 Spro_4259 Spro_4263
            BFL: Bfl017(gyrB) Bfl476(gyrA)
            BPN: BPEN_016(gyrB) BPEN_492(gyrA)
            HIN: HI0567(gyrB) HI1264(gyrA)
            HIT: NTHI0699(gyrB) NTHI1900(gyrA)
            HDU: HD1643(gyrB) HD1748(gyrA)
            HSO: HS_1163(gyrA) HS_1708(gyrB)
            PMU: PM0841(gyrA) PM1476(gyrB)
            MSU: MS0858(gyrA) MS2249(gyrB)
            APL: APL_0286(gyrA) APL_0821(gyrB)
            ASU: Asuc_0132 Asuc_0977 Asuc_0979 Asuc_1753
            XFA: XF0005 XF2552
            XFT: PD0005(gyrB) PD1935(gyrA)
            XCC: XCC0004(gyrB) XCC1574(gyrA)
            XCB: XC_0004 XC_2660
            XCV: XCV0004(gyrB) XCV1672(gyrA)
            XAC: XAC0004(gyrB) XAC1631(gyrA)
            XOO: XOO0004(gyrB) XOO2406(gyrA)
            XOM: XOO_0004(XOO0004) XOO_2284(XOO2284)
            VCH: VC0015 VC1258
            VCO: VC0395_A0877(gyrA) VC0395_A2007(parC) VC0395_A2504(gyrB)
            VVU: VV1_0996 VV1_3038 VV1_3039
            VVY: VV0014 VV1247
            VPA: VP0014 VP1932
            VFI: VF0012 VF1204
            PPR: PBPRA0011 PBPRA2456(gyrA)
            PAE: PA0004(gyrB) PA3168(gyrA)
            PAU: PA14_00050(gyrB) PA14_23260(gyrA)
            PAP: PSPA7_0004(gyrB) PSPA7_1961(gyrA)
            PPU: PP_0013(gyrB) PP_1767(gyrA)
            PPF: Pput_0004 Pput_3947 Pput_4788 Pput_4791
            PST: PSPTO_0004(gyrB) PSPTO_1745(gyrA)
            PSB: Psyr_0004 Psyr_3647
            PSP: PSPPH_0004(gyrB) PSPPH_3667(gyrA)
            PFL: PFL_0004(gyrB) PFL_4314(gyrA)
            PFO: Pfl_0004 Pfl_0499 Pfl_4078
            PEN: PSEEN0004(gyrB) PSEEN1487(gyrA)
            PMY: Pmen_0004 Pmen_0601 Pmen_0604 Pmen_1848
            PAR: Psyc_0004(gyrB) Psyc_1543(gyrA)
            PCR: Pcryo_0006 Pcryo_1724
            PRW: PsycPRwf_0005 PsycPRwf_0873 PsycPRwf_2194 PsycPRwf_2255
            ACI: ACIAD0004(gyrB) ACIAD2652(gyrA)
            SON: SO_0011(gyrB) SO_2411(gyrA)
            SDN: Sden_0004 Sden_1948
            SFR: Sfri_0004 Sfri_2130
            SAZ: Sama_0016 Sama_1731 Sama_3043
            SBL: Sbal_0004 Sbal_2062 Sbal_3573
            SBM: Shew185_0004 Shew185_0786 Shew185_0788 Shew185_2287
            SLO: Shew_0004 Shew_0549 Shew_1949
            SPC: Sputcn32_0004 Sputcn32_0773
            SSE: Ssed_0009 Ssed_0779 Ssed_0781 Ssed_2303
            SPL: Spea_0004 Spea_2067 Spea_3556 Spea_3558
            SHE: Shewmr4_0004 Shewmr4_1919
            SHM: Shewmr7_0004 Shewmr7_2059
            SHN: Shewana3_0012 Shewana3_1972
            SHW: Sputw3181_0004 Sputw3181_1942 Sputw3181_3402
            ILO: IL0004(gyrB) IL1360(gyrA)
            CPS: CPS_0004(gyrB) CPS_2331(gyrA)
            PHA: PSHAa0004(gyrB) PSHAa1421(gyrA)
            PAT: Patl_0004 Patl_2470
            SDE: Sde_0004 Sde_0374 Sde_2148
            PIN: Ping_1114 Ping_3354 Ping_3717
            MAQ: Maqu_0005 Maqu_1021 Maqu_2794
            CBU: CBU_0004(gyrB) CBU_0524(gyrA)
            CBD: COXBU7E912_0005(gyrB) COXBU7E912_1539(gyrA)
            LPN: lpg0004(gyrB) lpg1417(gyrA)
            LPF: lpl0004(gyrB) lpl1368(gyrA)
            LPP: lpp0004(gyrB) lpp1372(gyrA)
            MCA: MCA1421(gyrA) MCA3030(gyrB)
            FTU: FTT0510(gyrB) FTT1575c(gyrA)
            FTF: FTF0510(gyrB) FTF1575c(gyrA)
            FTW: FTW_0351(gyrA) FTW_1555(gyrB)
            FTL: FTL_0533 FTL_1547
            FTH: FTH_0459(parC) FTH_0535(gyrA) FTH_1497(gyrB) FTH_1665(parE)
            FTA: FTA_0566(gyrA) FTA_1632(gyrB)
            FTN: FTN_0600(gyrB) FTN_1484(gyrA)
            TCX: Tcr_0012 Tcr_0364 Tcr_1191
            NOC: Noc_0019 Noc_0171 Noc_2283
            AEH: Mlg_0004 Mlg_0923
            HHA: Hhal_0571 Hhal_1224 Hhal_1983
            HCH: HCH_00008(gyrB) HCH_04983(gyrA)
            CSA: Csal_0004 Csal_2168
            ABO: ABO_0004(gyrB) ABO_1751(gyrA)
            MMW: Mmwyl1_0004 Mmwyl1_2836 Mmwyl1_2860 Mmwyl1_3554
            AHA: AHA_0004(gyrB) AHA_2330(gyrA)
            DNO: DNO_0321(gyrA) DNO_0612(gyrB)
            BCI: BCI_0131(gyrB) BCI_0387(gyrA)
            RMA: Rmag_0003 Rmag_0563
            VOK: COSY_0003(gyrB)
            NME: NMB0212 NMB1384
            NMA: NMA0056(gyrB) NMA1599(gyrA)
            NMC: NMC0204(gyrB) NMC1320(gyrA)
            NGO: NGO0629 NGO1772(gyrB)
            CVI: CV_0003(gyrB) CV_2298(gyrA)
            RSO: RSc0901(gyrA) RSc3440(gyrB)
            REU: Reut_A0003 Reut_A2358 Reut_A2578
            REH: H16_A0003(gyrB) H16_A0789(gyrA)
            RME: Rmet_0003 Rmet_0713
            BMA: BMA0003(gyrB) BMA0435(gyrA)
            BMV: BMASAVP1_A2578(gyrA) BMASAVP1_A2850(gyrB)
            BML: BMA10299_A0953(gyrA) BMA10299_A2235(gyrB)
            BMN: BMA10247_0003(gyrB) BMA10247_0195(gyrA)
            BXE: Bxe_A0974 Bxe_A4460
            BVI: Bcep1808_0003 Bcep1808_2447 Bcep1808_6768
            BUR: Bcep18194_A3184 Bcep18194_A4153 Bcep18194_A5699
            BCN: Bcen_0561 Bcen_1748 Bcen_2555
            BCH: Bcen2424_0003 Bcen2424_1040 Bcen2424_2360
            BAM: Bamb_0003 Bamb_0916 Bamb_2396
            BPS: BPSL0073 BPSL2521(gyrA)
            BPM: BURPS1710b_0299(gyrB) BURPS1710b_3000(gyrA)
            BPL: BURPS1106A_0101(gyrB) BURPS1106A_2951(gyrA)
            BPD: BURPS668_0087(gyrB) BURPS668_2888(gyrA)
            BTE: BTH_I1632(gyrA) BTH_I3241(gyrB)
            PNU: Pnuc_0003 Pnuc_0900
            BPE: BP0489(gyrB) BP0944(gyrA)
            BPA: BPP3134(gyrA) BPP4399(gyrB)
            BBR: BB3473(gyrA) BB4987(gyrB)
            RFR: Rfer_0003 Rfer_1571 Rfer_2642
            POL: Bpro_0003 Bpro_1795 Bpro_3165
            PNA: Pnap_1199 Pnap_4119
            AAV: Aave_0003 Aave_1340
            AJS: Ajs_1014 Ajs_4146
            VEI: Veis_0003 Veis_1664
            MPT: Mpe_A0003 Mpe_A2238
            HAR: HEAR0005(gyrB) HEAR0790(parE) HEAR2581(gyrA)
            MMS: mma_0003(gyrB) mma_2675(gyrA)
            NEU: NE0003(gyrB) NE0332(gyrA)
            NET: Neut_0003 Neut_1573
            NMU: Nmul_A0003 Nmul_A2189
            EBA: ebA2848(gyrB) ebA909(gyrA)
            AZO: azo0003(gyrB) azo1066(gyrA)
            DAR: Daro_0003 Daro_1230
            TBD: Tbd_0003 Tbd_0948
            MFA: Mfla_0003 Mfla_1688
            HPY: HP0501(gyrB) HP0701(gyrA)
            HPJ: jhp0453(gyrB) jhp0641(gyrA)
            HPA: HPAG1_0477 HPAG1_0686
            HHE: HH1127(gyrB) HH1633(gyrA)
            HAC: Hac_0822(gyrB) Hac_0961(gyrA)
            WSU: WS0002(gyrB) WS0365(gyrA)
            TDN: Tmden_0003 Tmden_0640
            CJE: Cj0003(gyrB) Cj1027c(gyrA)
            CJR: CJE0003(gyrB) CJE1171(gyrA)
            CJJ: CJJ81176_0029(gyrB) CJJ81176_1046(gyrA)
            CJU: C8J_0003(gyrB) C8J_0964(gyrA)
            CJD: JJD26997_0003(gyrB) JJD26997_0761(gyrA)
            CFF: CFF8240_0003(gyrB) CFF8240_1462(gyrA)
            CCV: CCV52592_1459(gyrA) CCV52592_2054(gyrB)
            CHA: CHAB381_0004(gyrB) CHAB381_1244(gyrA)
            CCO: CCC13826_0843 CCC13826_1076 CCC13826_1850(gyrB) CCC13826_2105
            ABU: Abu_0003(gyrB) Abu_1789(gyrA)
            NIS: NIS_0003(gyrB)
            GSU: GSU0003(gyrB) GSU0004(gyrA)
            GME: Gmet_0004 Gmet_0005
            GUR: Gura_0004 Gura_0005
            PCA: Pcar_0004 Pcar_0005
            PPD: Ppro_0004
            DVU: DVU0003(gyrB) DVU0004(gyrA)
            DVL: Dvul_0005
            DDE: Dde_0003 Dde_0004
            LIP: LI0784(gyrA) LI0785(gyrB)
            BBA: Bd0004 Bd0005(gyrA) Bd2864(top6A) Bd2865(top6B)
            DPS: DP0649 DP0650 DP2280
            ADE: Adeh_0004 Adeh_2839 Adeh_2840 Adeh_4346
            AFW: Anae109_0004 Anae109_2770 Anae109_2771 Anae109_4493
            MXA: MXAN_0264(gyrB) MXAN_0766(gyrA) MXAN_2483 MXAN_2485
            SAT: SYN_02048 SYN_02049
            SFU: Sfum_2689 Sfum_2690
            RPR: RP206(gyrA) RP227(gyrB1) RP580(gyrB2)
            RTY: RT0196(gyrA) RT0569(gyrB)
            RCO: RC0273(gyrA) RC0309(gyrB1) RC0884(gyrB2)
            RFE: RF_0947(gyrB) RF_0988(parE) RF_1055(gyrA)
            RBE: RBE_0794(gyrA) RBE_0995(gyrB)
            OTS: OTBS_0252(gyrA) OTBS_1419(gyrB)
            WOL: WD0112(gyrB) WD1202(gyrA)
            WBM: Wbm0405(gyrA) Wbm0764(gyrB)
            AMA: AM372(gyrA) AM644(gyrB2)
            APH: APH_0716(gyrB) APH_0899(gyrA)
            ERU: Erum2420(gyrA) Erum4260(gyrB) Erum4431
            ERW: ERWE_CDS_02460(gyrA) ERWE_CDS_04430(gyrB)
            ERG: ERGA_CDS_02420(gyrA) ERGA_CDS_04380(gyrB)
            ECN: Ecaj_0234 Ecaj_0417
            ECH: ECH_0620(gyrB) ECH_0858(gyrA)
            NSE: NSE_0721(gyrB) NSE_0958(gyrA)
            PUB: SAR11_0446(gyrB) SAR11_0985(gyrA)
            MLO: mll0732 mll5188 mlr0901
            MES: Meso_1015 Meso_1400 Meso_3603
            PLA: Plav_0007 Plav_2877 Plav_3049 Plav_3250
            SME: SMc01018(parE) SMc01231(gyrA) SMc02782(gyrB)
            SMD: Smed_0807 Smed_1062 Smed_1241 Smed_3220
            ATU: Atu0012(gyrB) Atu1507(gyrA) Atu1622(gyrB)
            ATC: AGR_C_19 AGR_C_2778 AGR_C_2992
            RET: RHE_CH00012(gyrB) RHE_CH02110(gyrA)
            RLE: RL0012(gyrB) RL2401(gyrA)
            BME: BMEI0884 BMEI1823 BMEII0676
            BMF: BAB1_0122 BAB1_1121(gyrA) BAB2_0649
            BMS: BR0125(gyrB) BR1097(gyrA) BRA0591(parE)
            BMB: BruAb1_0122(gyrB) BruAb1_1103(gyrA) BruAb2_0633(parE)
            BOV: BOV_0121(gyrB) BOV_1058(gyrA)
            OAN: Oant_0139 Oant_2182 Oant_2539 Oant_3657
            BJA: bll0823(gyrB) bll4355(gyrB) bll4696(gyrA)
            BRA: BRADO0004(gyrB) BRADO3555(parE) BRADO3999(gyrA)
            BBT: BBta_0008(gyrB) BBta_3980(parE) BBta_4371(gyrA)
            RPA: RPA0004(gyrB) RPA2486(parE) RPA2599(gyrA)
            RPB: RPB_0005 RPB_2876 RPB_2978
            RPC: RPC_0005 RPC_2584 RPC_2827
            RPD: RPD_0004 RPD_2596
            RPE: RPE_0005 RPE_2764
            NWI: Nwi_0004 Nwi_1653 Nwi_1801
            NHA: Nham_0004 Nham_1764
            BHE: BH00410(gyrB) BH10120(gyrA)
            BQU: BQ00370(gyrB) BQ06610(parE) BQ07850(gyrA)
            BBK: BARBAKC583_0737(gyrA) BARBAKC583_1346(gyrB)
            XAU: Xaut_3884 Xaut_4317 Xaut_4757
            CCR: CC_0160 CC_1580
            SIL: SPO0155(gyrB) SPO2051(gyrA)
            SIT: TM1040_0007 TM1040_1332
            RSP: RSP_1346 RSP_2630(gyrA)
            RSH: Rsph17029_0015 Rsph17029_2428
            RSQ: Rsph17025_0006 Rsph17025_0407 Rsph17025_1166 Rsph17025_2551
            JAN: Jann_0004
            RDE: RD1_0212(gyrB) RD1_2726(gyrA)
            PDE: Pden_0416 Pden_1836
            MMR: Mmar10_0014 Mmar10_1873
            HNE: HNE_0552(gyrB) HNE_2760(gyrA)
            ZMO: ZMO0411(gyrB) ZMO0692(gyrA) ZMO1583(gyrB)
            NAR: Saro_1918 Saro_3310
            SAL: Sala_2972
            SWI: Swit_0107 Swit_2802 Swit_4563 Swit_4578
            ELI: ELI_06340 ELI_11730
            GOX: GOX0004 GOX0887
            GBE: GbCGDNIH1_0321 GbCGDNIH1_0684 GbCGDNIH1_1219
            ACR: Acry_1179 Acry_1208 Acry_2886
            RRU: Rru_A0004 Rru_A1744
            MAG: amb0639 amb2381
            MGM: Mmc1_0006 Mmc1_0719 Mmc1_1072
            ABA: Acid345_0008 Acid345_4772
            SUS: Acid_0003
            BSU: BG10070(gyrB) BG10071(gyrA)
            BHA: BH0006(gyrB) BH0007(gyrA)
            BAN: BA0005(gyrB) BA0006(gyrA)
            BAR: GBAA0005(gyrB) GBAA0006(gyrA)
            BAA: BA_0600 BA_0601
            BAT: BAS0005 BAS0006
            BCE: BC0005 BC0006
            BCA: BCE_0005(gyrB) BCE_0006(gyrA)
            BCZ: BCZK0005(gyrB) BCZK0006(gyrA)
            BCY: Bcer98_0005 Bcer98_0006 Bcer98_2246 Bcer98_2247
            BTK: BT9727_0005(gyrB) BT9727_0006(gyrA)
            BTL: BALH_0005(gyrB) BALH_0006(gyrA)
            BLI: BL00081(gyrB) BL00082(gyrA)
            BLD: BLi00006(gyrB) BLi00007(gyrA)
            BCL: ABC0006(gyrB) ABC0007(gyrA)
            BAY: RBAM_000060(gyrB) RBAM_000070(gyrA)
            BPU: BPUM_0006(gyrB) BPUM_0007(gyrA) BPUM_1709 BPUM_1710
            OIH: OB0006(gyrB) OB0007(gyrA)
            GKA: GK0005(gyrB) GK0006(gyrA)
            GTN: GTNG_0005 GTNG_0006
            SAU: SA0005(gyrB) SA0006(gyrA)
            SAV: SAV0005(gyrB) SAV0006(gyrA)
            SAM: MW0005(gyrB) MW0006(gyrA)
            SAR: SAR0005(gyrB) SAR0006(gyrA)
            SAS: SAS0005 SAS0006
            SAC: SACOL0005(gyrB) SACOL0006(gyrA)
            SAB: SAB0005(gyrB) SAB0006(gyrA)
            SAA: SAUSA300_0005(gyrB) SAUSA300_0006(gyrA)
            SAO: SAOUHSC_00005 SAOUHSC_00006
            SAJ: SaurJH9_0005 SaurJH9_0006 SaurJH9_1416 SaurJH9_1417
            SAH: SaurJH1_0005 SaurJH1_0006 SaurJH1_1443 SaurJH1_1444
            SEP: SE0004 SE0005
            SER: SERP2548(gyrA) SERP2549(gyrB)
            SHA: SH0005(gyrB) SH0006(gyrA)
            SSP: SSP0005 SSP0006
            LMO: lmo0006(gyrB) lmo0007(gyrA)
            LMF: LMOf2365_0006(gyrB) LMOf2365_0007(gyrA)
            LIN: lin0006(gyrB) lin0007(gyrA)
            LWE: lwe0006(gyrB) lwe0007(gyrA)
            LLA: L0282(gyrA) L0283(gyrB)
            LLC: LACR_0984 LACR_1216
            LLM: llmg_1451(gyrA) llmg_1631(gyrB)
            SPY: SPy_0727(gyrB) SPy_1152(gyrA)
            SPZ: M5005_Spy_0553(gyrB) M5005_Spy_0874(gyrA)
            SPM: spyM18_0795(gryB) spyM18_1112(gyrA)
            SPG: SpyM3_0476(gyrB) SpyM3_0810(gyrA)
            SPS: SPs1009 SPs1378
            SPH: MGAS10270_Spy0611(gyrB) MGAS10270_Spy0612
                 MGAS10270_Spy0988(gyrA)
            SPI: MGAS10750_Spy0635 MGAS10750_Spy0636(gyrB)
                 MGAS10750_Spy1023(gyrA)
            SPJ: MGAS2096_Spy0615(gyrB) MGAS2096_Spy0948(gyrA)
            SPK: MGAS9429_Spy0606(gyrB) MGAS9429_Spy0992(gyrA)
            SPF: SpyM50916(cafB) SpyM51097(parE) SpyM51251(gyrB)
            SPA: M6_Spy0573 M6_Spy0870
            SPB: M28_Spy0532(gyrB) M28_Spy0848(gyrA)
            SPN: SP_0806 SP_1219
            SPR: spr0715(gyrB) spr1099(gyrA)
            SPD: SPD_0709(gyrB) SPD_1077(gyrA)
            SAG: SAG0623(gyrB) SAG0960(gyrA)
            SAN: gbs0603(gyrB) gbs0948(gyrA)
            SAK: SAK_0708(gyrB) SAK_1055(gyrA)
            SMU: SMU.1114(gyrA) SMU.1210(parE) SMU.1277(gyrB)
            STC: str1279(gyrA) str1521(gyrB)
            STL: stu1279(gyrA) stu1521(gyrB)
            STE: STER_1256
            SSA: SSA_0878(gyrB) SSA_1220(gyrA)
            SSU: SSU05_1075 SSU05_1510
            SSV: SSU98_1086
            SGO: SGO_1231(gyrA) SGO_1432(gyrB)
            LPL: lp_0006(gyrB) lp_0007(gyrA)
            LJO: LJ0004 LJ0005
            LAC: LBA0005(gyrB) LBA0006(gyrA) LBA1122 LBA1123
            LSA: LSA0005(gyrB) LSA0006(gyrA) LSA0975(parC)
            LSL: LSL_0005(gyrB) LSL_0006(gyrA)
            LDB: Ldb0005(gyrB) Ldb0006(gyrA)
            LBU: LBUL_0005 LBUL_0006
            LBR: LVIS_0005 LVIS_0006
            LCA: LSEI_0005 LSEI_0006
            LGA: LGAS_0005 LGAS_0006
            LRE: Lreu_0005 Lreu_0006 Lreu_0782 Lreu_0783
            PPE: PEPE_0005 PEPE_0006
            EFA: EF0005(gyrB) EF0006(gyrA)
            OOE: OEOE_0005 OEOE_0006
            LME: LEUM_0005 LEUM_0006
            STH: STH7(gyrA)
            CAC: CAC0006(gyrB) CAC0007(gyrA) CAC1627(gyrB) CAC1628(gyrA)
            CPE: CPE0006(gyrB) CPE0007(gyrA)
            CPF: CPF_0006(gyrB) CPF_0007(gyrA) CPF_2325(gyrA)
            CPR: CPR_0006(gyrB) CPR_0007(gyrA)
            CTC: CTC00090 CTC00091 CTC01766 CTC01767
            CNO: NT01CX_0861(gyrA) NT01CX_0862(gyrB) NT01CX_2325
            CTH: Cthe_0305 Cthe_2361 Cthe_2376
            CDF: CD0005(gyrB) CD0006(gyrA)
            CBO: CBO0006(gyrB) CBO0007(gyrA) CBO2769(gyrA) CBO2770(gyrB)
            CBA: CLB_0006(gyrB) CLB_0007(gyrA)
            CBH: CLC_0006(gyrB) CLC_0007(gyrA)
            CBF: CLI_0006(gyrB) CLI_0007(gyrA)
            CBE: Cbei_0006 Cbei_0007 Cbei_4323 Cbei_4324
            CKL: CKL_0006(gyrB1) CKL_0007(gyrA1) CKL_2143(gyrA2)
                 CKL_2144(gyrB2)
            AMT: Amet_0006 Amet_0007 Amet_3106
            CHY: CHY_2704(gyrA) CHY_2705(gyrB)
            DSY: DSY0005(gyrB) DSY0006(gyrA)
            DRM: Dred_0006 Dred_0007
            SWO: Swol_0005 Swol_0006
            CSC: Csac_0005 Csac_0006 Csac_1580
            TTE: TTE0010(gyrB) TTE0011(gyrA) TTE1745
            MTA: Moth_0007 Moth_0008
            MGE: MG_003(gyrB) MG_004(gyrA)
            MPN: MPN003(gyrB) MPN004(gyrA)
            MPU: MYPU_1470(gyrA) MYPU_7390(gyrB)
            MPE: MYPE30(gyrB) MYPE40(gyrA)
            MGA: MGA_0612(gyrA) MGA_0616(gyrB)
            MMY: MSC_0006(gyrB) MSC_0007(gyrA)
            MMO: MMOB1010(gyrB) MMOB4940(gyrA)
            MHY: mhp270(gyrB) mhp545(gyrA)
            MHJ: MHJ_0106(gyrB) MHJ_0529(gyrA)
            MHP: MHP7448_0109(gyrB) MHP7448_0528(gyrA)
            MSY: MS53_0317(gyrA) MS53_0684(gyrB)
            MCP: MCAP_0040(gyrA) MCAP_0041(gyrB)
            UUR: UU081(gyrB) UU082(gyrA)
            POY: PAM498(gyrB) PAM499(gyrA)
            AYW: AYWB_254(gyrA) AYWB_255(gyrB)
            MFL: Mfl006 Mfl007
            MTU: Rv0005(gyrB) Rv0006(gyrA)
            MTC: MT0005(gyrB) MT0006(gyrA)
            MBO: Mb0005(gyrB) Mb0006(gyrA)
            MBB: BCG_0005(gyrB_1) BCG_0006(gyrA_1) BCG_0035(gyrB_2)
                 BCG_0036(gyrA_2)
            MLE: ML0005(gyrB) ML0006(gyrA)
            MPA: MAP0005(gyrB) MAP0006(gyrA)
            MAV: MAV_0005(gyrB) MAV_0006(gyrA)
            MSM: MSMEG_0005(gyrB) MSMEG_0006(gyrA) MSMEG_0456 MSMEG_1229(gyrB)
            MUL: MUL_0005(gyrB) MUL_0006(gyrA)
            MVA: Mvan_0006 Mvan_0007 Mvan_5897
            MGI: Mflv_0496 Mflv_0821 Mflv_0822
            MMC: Mmcs_0006 Mmcs_0007 Mmcs_5342 Mmcs_5343
            MKM: Mkms_0014 Mkms_0015 Mkms_5431
            MJL: Mjls_0006 Mjls_0007 Mjls_5721
            CGL: NCgl0005(cgl0006) NCgl0012(cgl0013)
            CGB: cg0007(gyrB) cg0015(gyrA)
            CEF: CE0006 CE0015
            CDI: DIP0005(gyrB) DIP0009(gyrA)
            CJK: jk0005(gyrB) jk0011(gyrA)
            NFA: nfa60(gyrB) nfa70(gyrA)
            RHA: RHA1_ro03674(gyrB) RHA1_ro03680(gyrA)
            SCO: SCO3873(gyrA) SCO3874(gyrB) SCO5822 SCO5836(SC9B10.03c)
            SMA: SAV2423(parC) SAV2442(parE) SAV4321(gyrB) SAV4322(gyrA)
            TWH: TWT005(gyrB1) TWT006(gyrA1) TWT491(gyrA2) TWT494(gyrB2)
            TWS: TW005(gyrB1) TW006(gyrA1) TW268(gyrB2) TW273(gyrA1)
            LXX: Lxx00060(gyrB) Lxx00070(gyrA) Lxx10320(gyrB) Lxx10360(gyrA)
            CMI: CMM_0006(gyrB) CMM_0007(gyrA) CMM_1650 CMM_1651
            ART: Arth_0006 Arth_1619
            AAU: AAur_0006(gyrB) AAur_0007(gyrA)
            PAC: PPA0009 PPA0010 PPA1042 PPA1045
            NCA: Noca_0006 Noca_2958
            TFU: Tfu_0006 Tfu_0007 Tfu_2131 Tfu_2134
            FRA: Francci3_0006 Francci3_0007 Francci3_1761
            FAL: FRAAL0008(gyrB) FRAAL0009(gyrA)
            ACE: Acel_0005 Acel_0006 Acel_1427
            KRA: Krad_0006 Krad_0007 Krad_1534 Krad_1546
            SEN: SACE_0008(gyrB) SACE_0009(gyrA)
            STP: Strop_0008 Strop_1681
            BLO: BL0634(gyrA1) BL0635(gyrB1) BL1429(gyrB2) BL1434(gyrA2)
            BAD: BAD_0005(gyrB) BAD_0006(gyrA) BAD_1007(gyrA2) BAD_1010(gyrB2)
            RXY: Rxyl_0005 Rxyl_0006
            FNU: FN2125 FN2126
            RBA: RB3272(gyrB) RB3465(gyrA) RB3466(gyrB) RB8841(gyrA)
                 RB9109(gyrB)
            CTR: CT189(gyrA_1) CT190(gyrB_1) CT660(gyrA_2) CT661(gyrB_2)
            CTA: CTA_0207(gyrA_1) CTA_0208(gyrB_1) CTA_0717(gyrA_2)
                 CTA_0718(gyrB_2)
            CMU: TC0031 TC0032 TC0461 TC0462
            CPN: CPn0274(gyrA_1) CPn0275(gyrB_1) CPn0715(gyrB_2)
                 CPn0716(gyrA_2)
            CPA: CP0030 CP0031 CP0484 CP0485
            CPJ: CPj0274(gyrA_1) CPj0275(gyrB_1) CPj0715(gyrB_2)
                 CPj0716(gyrA_2)
            CPT: CpB0281 CpB0282 CpB0743 CpB0744
            CCA: CCA00026 CCA00027 CCA00506(gyrB) CCA00507(gyrA)
            CAB: CAB026 CAB027(gyrB_2) CAB493(gyrbB) CAB494(gyrA)
            CFE: CF0501(gyrA2) CF0502(gyrB2) CF0978(gyrB1) CF0979(gyrA1)
            PCU: pc0350(gyrB) pc1074(gyrA) pc1075(gyrB)
            BBU: BB0435(gyrA) BB0436(gyrB)
            BGA: BG0442(gyrA) BG0443(gyrB)
            BAF: BAPKO_0457(gyrA) BAPKO_0458(gyrB)
            TPA: TP0005 TP1006
            TDE: TDE0002(gyrB) TDE0295(gyrA)
            LIL: LA0005(gyrB1) LA0006(gyrA1) LA4193(gyrA2) LA4194(gyrB2)
            LIC: LIC10005 LIC10006(gyrA)
            LBJ: LBJ_0008(gyrB) LBJ_0009(gyrA)
            LBL: LBL_0008(gyrB) LBL_0009(gyrA)
            SYN: sll1941(gyrA) sll2005(gyrB) slr0417(gyrA)
            SYW: SYNW0005 SYNW0095(gyrB) SYNW0727(gyrA)
            SYC: syc1259_c(gyrA) syc1615_c(gyrB) syc2396_c(gyrA)
            SYF: Synpcc7942_0254 Synpcc7942_1694 Synpcc7942_2491
            SYD: Syncc9605_0005 Syncc9605_0087 Syncc9605_1942
            SYE: Syncc9902_0005 Syncc9902_0133 Syncc9902_0723
            SYG: sync_0005(gyrA-1) sync_0092(gyrB) sync_0973(gyrA-2)
            SYR: SynRCC307_0005(gyrA) SynRCC307_0092(gyrB)
                 SynRCC307_0742(gyrA)
            SYX: SynWH7803_0147(gyrB) SynWH7803_1589(gyrA)
            CYA: CYA_0008 CYA_1415(gyrA) CYA_1523(gyrB)
            CYB: CYB_0008 CYB_0322(gyrB) CYB_1609(gyrA)
            TEL: tll0647(gyrB) tll1617(gyrA) tlr1369(gyrA)
            GVI: gll2050(gyrA) gll2506(gyrB) gll3082(gyrA)
            ANA: all0441 all0860 all5265
            AVA: Ava_2517 Ava_2854 Ava_4464
            PMA: Pro0005(gyrA) Pro1137(gyrA) Pro1796(gyrB)
            PMM: PMM0005 PMM1063(gyrA) PMM1634(gyrB)
            PMT: PMT0005 PMT0121(gyrB) PMT1124(gyrA)
            PMN: PMN2A_0689 PMN2A_1213 PMN2A_1332
            PMI: PMT9312_0005 PMT9312_1074 PMT9312_1727
            PMB: A9601_00041 A9601_11681 A9601_18441(gyrB)
            PMC: P9515_00041 P9515_11531 P9515_18231(gyrB)
            PMF: P9303_00041 P9303_01571(gyrB) P9303_09151
            PMG: P9301_00041 P9301_11691 P9301_18251(gyrB)
            PMH: P9215_11981(gyrA) P9215_19081(gyrB)
            PME: NATL1_00041 NATL1_15231 NATL1_20881(gyrB)
            TER: Tery_1901 Tery_3961 Tery_4186
            BTH: BT_0899 BT_3429
            BFR: BF0297 BF2411
            BFS: BF0246 BF2493(gyrA)
            PGI: PG1386(gyrA) PG1702(gyrB)
            SRU: SRU_1483 SRU_1484 SRU_2199(gyrA) SRU_2408(gyrB)
            CHU: CHU_1413(gyrB) CHU_1639(gyrA) CHU_1682(gyrA)
            GFO: GFO_1503(gyrA) GFO_2749(gyrB)
            FJO: Fjoh_2254 Fjoh_2475 Fjoh_2584
            FPS: FP0527(gyrB) FP0748(gyrA)
            CTE: CT0141(gyrA) CT2263(gyrB)
            CCH: Cag_0029 Cag_0088
            CPH: Cpha266_0036
            PVI: Cvib_0013
            PLT: Plut_0010 Plut_0098
            DET: DET0004(gyrB) DET1630(gyrA)
            DEH: cbdb_A1728(gyrA) cbdb_A4(gyrB)
            DEB: DehaBAV1_0004 DehaBAV1_1375
            RRS: RoseRS_0047 RoseRS_0729
            RCA: Rcas_0328 Rcas_4195
            DRA: DR_0906 DR_1913
            DGE: Dgeo_0546 Dgeo_1016
            TTH: TTC0990 TTC1222
            TTJ: TTHA1355 TTHA1586 TTHB172
            AAE: aq_1026(gyrB) aq_1159(topG1) aq_886(topG2) aq_980(gyrA)
            TMA: TM0173 TM0833 TM1084
            TPT: Tpet_0094 Tpet_0752 Tpet_1660
            TME: Tmel_0671 Tmel_1186
            FNO: Fnod_0795 Fnod_0966 Fnod_1363
            MJA: MJ0369(top6A) MJ1028(top6B) MJ1512(rgy)
            MMP: MMP0989(top6B) MMP1437(top6A)
            MMZ: MmarC7_0230 MmarC7_0682
            MAE: Maeo_0438 Maeo_1013
            MVN: Mevan_0315 Mevan_0748
            MAC: MA1583(gyrA) MA1584(gyrB) MA1586 MA1587
            MBA: Mbar_A2804 Mbar_A2805 Mbar_A2806 Mbar_A2807
            MMA: MM_2417 MM_2418 MM_2419 MM_2420
            MBU: Mbur_0419 Mbur_0420 Mbur_1202 Mbur_1203
            MTP: Mthe_1393
            MHU: Mhun_1044 Mhun_1045 Mhun_2919 Mhun_2920
            MEM: Memar_1407
            MBN: Mboo_1634
            MTH: MTH1007 MTH1008
            MST: Msp_1339 Msp_1340
            MSI: Msm_0955 Msm_0956
            MKA: MK0049 MK0289 MK0512 MK0921
            AFU: AF0465(gyrA) AF0530(gyrB) AF0652(top6B) AF0940(top6A)
                 AF1024(top-RG)
            HAL: VNG0884G(top6A) VNG0885G(top6B) VNG0887G(gyrB) VNG0889G(gyrA)
            HMA: rrnAC0455(gyrA) rrnAC0456(gyrB) rrnAC0457(top6B)
                 rrnAC0459(top6A)
            HWA: HQ2651A(gyrA) HQ2652A(gyrB) HQ2653A(top6B) HQ2654A(top6A)
            NPH: NP3480A(top6A) NP3482A(top6B) NP3498A(gyrB) NP3500A(gyrA)
            TAC: Ta1054 Ta1055
            TVO: TVN0541 TVN0542
            PTO: PTO1414 PTO1415
            PHO: PH0800 PH1563 PH1564
            PAB: PAB0407(top6B) PAB2411(top6A) PAB2423(top-RG)
            PFU: PF0495 PF1578 PF1579
            TKO: TK0470 TK0798 TK0799
            RCI: LRC137(top6A-1) LRC138(top6B-1) RCIX1075(top6B-2)
                 RCIX1077(top6A-2) RCIX58(gyrA) RCIX59(gyrB)
            APE: APE_0703.1 APE_0706.1 APE_1340.1 APE_1376.1
            IHO: Igni_0418 Igni_0516 Igni_1053 Igni_1090
            HBU: Hbut_0960 Hbut_0961
            SSO: SSO0420(topR-1) SSO0963(topR-2) SSO0968(top6B) SSO0969(top6A)
            STO: ST0374 ST1290 ST1294 ST1295
            SAI: Saci_0839 Saci_1314(top6A) Saci_1315(top6B)
            MSE: Msed_1748 Msed_1754 Msed_1755 Msed_2236
            PAI: PAE1108 PAE2217 PAE2219
            NEQ: NEQ144 NEQ318 NEQ434 NEQ542
STRUCTURES  PDB: 1AB4  1AJ6  1BJT  1D3Y  1EI1  1KIJ  1KZN  1MU5  1MX0  1PVG  
                 1QZR  1SUU  1X75  1Z59  1Z5A  1Z5B  1Z5C  1ZI0  1ZXM  1ZXN  
                 2HKJ  2Q2E  
DBLINKS     IUBMB Enzyme Nomenclature: 5.99.1.3
            ExPASy - ENZYME nomenclature database: 5.99.1.3
            ExplorEnz - The Enzyme Database: 5.99.1.3
            ERGO genome analysis and discovery system: 5.99.1.3
            BRENDA, the Enzyme Database: 5.99.1.3
            CAS: 142805-56-9
///
ENTRY       EC 5.-.-.-                  Enzyme
CLASS       Isomerases
REACTION    (1) L-Ribulose 5-phosphate <=> L-Xylulose 5-phosphate [RN:R03244];
            (2) D-arabino-3-Hexulose 6-phosphate <=> D-Fructose 6-phosphate
            [RN:R05339];
            (3) Sedoheptulose 7-phosphate <=> D-glycero-D-manno-Heptose
            7-phosphate [RN:R05645]
SUBSTRATE   L-Ribulose 5-phosphate [CPD:C01101];
            D-arabino-3-Hexulose 6-phosphate [CPD:C06019];
            Sedoheptulose 7-phosphate [CPD:C00281]
PRODUCT     L-Xylulose 5-phosphate [CPD:C03291];
            D-Fructose 6-phosphate [CPD:C00085];
            D-glycero-D-manno-Heptose 7-phosphate [CPD:C07836]
///
ENTRY       EC 6.1.1.1                  Enzyme
NAME        tyrosine---tRNA ligase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-tyrosine:tRNATyr ligase (AMP-forming)
REACTION    ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
            [RN:R02918]
ALL_REAC    R02918
SUBSTRATE   ATP [CPD:C00002];
            L-tyrosine [CPD:C00082];
            tRNA(Tyr) [CPD:C00787]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-tyrosyl-tRNA(Tyr) [CPD:C02839]
REFERENCE   1  [PMID:13792726]
  AUTHORS   ALLEN EH, GLASSMAN E, SCHWEET RS.
  TITLE     Incorporation of amino acids into ribonucleic acid. I. The role of
            activating enzymes.
  JOURNAL   J. Biol. Chem. 235 (1960) 1061-7.
  ORGANISM  guinea pig
REFERENCE   2  [PMID:4563531]
  AUTHORS   Cowles JR, Key JL.
  TITLE     Demonstration of two tyrosyl-tRNA synthetases of pea roots.
  JOURNAL   Biochim. Biophys. Acta. 281 (1972) 33-44.
  ORGANISM  Pisum sativum
REFERENCE   3  [PMID:13715350]
  AUTHORS   HOLLEY RW, BRUNNGRABER EF, SAAD F, WILLIAMS HH.
  TITLE     Partial purification of the threonine- and tyrosine-activating
            enzymes from rat liver, and the effect of patassium ions on the
            activity of the tyrosine enzyme.
  JOURNAL   J. Biol. Chem. 236 (1961) 197-9.
  ORGANISM  rat [GN:rno]
REFERENCE   4
  AUTHORS   Schweet, R.S. and Allen, E.H.
  TITLE     Purification and properties of tyrosine-activating enzyme of hog
            pancreas.
  JOURNAL   J. Biol. Chem. 233 (1958) 1104-1108.
  ORGANISM  pig [GN:ssc]
REFERENCE   5  [PMID:2504923]
  AUTHORS   Brick P, Bhat TN, Blow DM.
  TITLE     Structure of tyrosyl-tRNA synthetase refined at 2.3 A resolution.
            Interaction of the enzyme with the tyrosyl adenylate intermediate.
  JOURNAL   J. Mol. Biol. 208 (1989) 83-98.
  ORGANISM  Bacillus stearothermophilus
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01866  tyrosyl-tRNA synthetase
GENES       HSA: 51067(YARS2) 8565(YARS)
            PTR: 469266(YARS)
            MCC: 697033(LOC697033)
            MMU: 107271(Yars)
            CFA: 478148(YARS) 486614(YARS2)
            BTA: 281581(YARS)
            GGA: 418131(YARS2) 419666(YARS)
            XLA: 380438(yars)
            XTR: 448444(yars)
            DRE: 368235(yars)
            SPU: 582945(LOC582945)
            DME: Dmel_CG16912 Dmel_CG4561(Aats-tyr)
            CEL: Y105E8A.19
            ATH: AT2G33840 AT3G02660
            OSA: 4324476 4344663
            CME: CMJ139C CMQ275C
            SCE: YGR185C(TYS1) YPL097W(MSY1)
            AGO: AGOS_AAL148W AGOS_ABR192W
            PIC: PICST_31908(MSY1) PICST_74631(TYS1)
            CGR: CAGL0H05775g CAGL0H09372g
            SPO: SPCC1672.05c SPCC576.06c
            ANI: AN0057.2 AN1709.2
            AFM: AFUA_4G08320 AFUA_5G10640
            AOR: AO090023000727 AO090124000024
            CNE: CNJ03200
            UMA: UM05111.1 UM05847.1
            ECU: ECU05_1120i
            DDI: DDB_0231243(tyrS) DDB_0231247(mtyrS)
            PFA: MAL8P1.125 PF11_0181
            CPV: cgd6_2970
            CHO: Chro.60344
            TAN: TA06885 TA08075
            TPV: TP01_0760 TP04_0367
            TET: TTHERM_00149980 TTHERM_00300470
            TBR: Tb927.7.3620
            TCR: 509937.180
            LMA: LmjF14.1370
            EHI: 237.t00005
            ECO: b1637(tyrS)
            ECJ: JW1629(tyrS)
            ECE: Z2650(tyrS)
            ECS: ECs2346
            ECC: c2029(tyrS)
            ECI: UTI89_C1828(tyrS) UTI89_C3513(ygjH)
            ECV: APECO1_720(tyrS)
            ECW: EcE24377A_1847(tyrS)
            ECX: EcHS_A1713(tyrS)
            STY: STY1673(tyrS)
            STT: t1317(tyrS)
            SPT: SPA1404(tyrS)
            SEC: SC1467(tyrS)
            STM: STM1449(tyrS)
            YPE: YPO2369(tyrS)
            YPK: y1966(tyrS)
            YPM: YP_2155(tyrS)
            YPA: YPA_1715
            YPN: YPN_1826
            YPP: YPDSF_0777
            YPS: YPTB2283(tyrS)
            YPI: YpsIP31758_1773(tyrS)
            SFL: SF1662(tyrS)
            SFX: S1794(tyrS)
            SFV: SFV_1654(tyrS)
            SSN: SSON_1519(tyrS)
            SBO: SBO_1497(tyrS)
            SDY: SDY_1860(tyrS)
            ECA: ECA1936(tyrS)
            PLU: plu0201 plu2596(tyrS)
            BUC: BU121(tyrS)
            BAS: BUsg113(tyrS)
            BAB: bbp115(tyrS)
            BCC: BCc_075(tyrS)
            WBR: WGLp338(tyrS)
            SGL: SG1448
            ENT: Ent638_1811
            KPN: KPN_01975(tyrS)
            SPE: Spro_2219
            BFL: Bfl371(tyrS)
            BPN: BPEN_382(tyrS)
            HIN: HI1610(tyrS)
            HIT: NTHI1432(tyrS)
            HIQ: CGSHiGG_10070
            HDU: HD0693(tyrS)
            HSO: HS_1307(tyrS)
            PMU: PM0755(tyrS)
            MSU: MS1232(tyrS)
            APL: APL_1476(tyrS)
            XFA: XF0169
            XFT: PD0132(tyrS)
            XCC: XCC3841(tyrS)
            XCB: XC_3925
            XCV: XCV4010(tyrS)
            XAC: XAC3897(tyrS)
            XOO: XOO0515(tyrS)
            XOM: XOO_0480(XOO0480)
            VCH: VC0465 VC0631
            VCO: VC0395_A0017(tyrS-1) VC0395_A0160(tyrS-2)
            VVU: VV1_1683 VV2_0878
            VVY: VV2723 VVA1349
            VPA: VP2470 VPA0368
            VFI: VF1727
            PPR: PBPRA0533
            PAE: PA0668(tyrZ) PA4138(tyrS)
            PAU: PA14_08560(tyrZ) PA14_10420(tyrS)
            PAP: PSPA7_0809(tyrS2) PSPA7_0952(tyrS1)
            PPU: PP_0436(tyrS)
            PPF: Pput_0469
            PST: PSPTO_0609(tyrS)
            PSB: Psyr_4565
            PSP: PSPPH_0688(tyrS)
            PFL: PFL_5607(tyrS)
            PFO: Pfl_5098
            PEN: PSEEN0464(tyrS)
            PMY: Pmen_3927
            PAR: Psyc_1970(tyrS)
            PCR: Pcryo_2269
            PRW: PsycPRwf_2221
            ACI: ACIAD0013(tyrS)
            SON: SO_1315(tyrS)
            SDN: Sden_2810
            SFR: Sfri_2971
            SAZ: Sama_0850
            SBL: Sbal_1170
            SLO: Shew_1022
            SSE: Ssed_1104
            SPL: Spea_0995
            SHE: Shewmr4_2880
            SHM: Shewmr7_2962
            SHN: Shewana3_3058
            SHW: Sputw3181_3036
            ILO: IL2236(tyrS)
            CPS: CPS_4727(tyrS)
            PHA: PSHAa0545(tyrZ) PSHAa2413(tyrS)
            PAT: Patl_0514
            SDE: Sde_1088
            PIN: Ping_0921
            MAQ: Maqu_0697
            CBU: CBU_0181(tyrS)
            CBD: COXBU7E912_1919(tyrS)
            LPN: lpg0568(tyrS)
            LPF: lpl0611(tyrS)
            LPP: lpp0628(tyrS)
            MCA: MCA0749(tyrS)
            FTU: FTT0691(tyrS)
            FTF: FTF0691(tyrS)
            FTW: FTW_1035(tyrS)
            FTL: FTL_0968
            FTH: FTH_0945(tyrS)
            FTA: FTA_1019(tyrS)
            FTN: FTN_0992(tyrS)
            TCX: Tcr_1949
            NOC: Noc_0911
            AEH: Mlg_0438
            HHA: Hhal_0876
            HCH: HCH_06238(tyrS)
            CSA: Csal_3050
            ABO: ABO_0366(tyrS)
            MMW: Mmwyl1_1071
            AHA: AHA_0581(tyrS-1) AHA_3117(tyrS-2)
            DNO: DNO_1321(tyrS)
            BCI: BCI_0081(tyrS)
            RMA: Rmag_0132
            VOK: COSY_0134(tyrS)
            NME: NMB1835
            NMA: NMA0620(tyrS)
            NMC: NMC0381(tyrS)
            NGO: NGO0066
            CVI: CV_3072(tyrS)
            RSO: RSc0496(tyrS)
            REU: Reut_A0476
            REH: H16_A0490(tyrS)
            RME: Rmet_0417
            BMA: BMA2348(tyrS)
            BMV: BMASAVP1_A0261(tyrS)
            BML: BMA10299_A1123(tyrS)
            BMN: BMA10247_2527(tyrS)
            BXE: Bxe_A0611
            BUR: Bcep18194_A3769
            BCN: Bcen_0200
            BCH: Bcen2424_0683
            BAM: Bamb_0577
            BPS: BPSL2904(tyrZ)
            BPM: BURPS1710b_3412(tyrS)
            BPL: BURPS1106A_3406(tyrS)
            BPD: BURPS668_3371(tyrS)
            BTE: BTH_I1240(tyrS)
            PNU: Pnuc_1881
            BPE: BP2954(tyrS)
            BPA: BPP3877(tyrS)
            BBR: BB4350(tyrS)
            RFR: Rfer_0728
            POL: Bpro_4106
            PNA: Pnap_0506
            AAV: Aave_4045
            AJS: Ajs_0632
            VEI: Veis_2645
            MPT: Mpe_A3150
            HAR: HEAR0248(tyrZ)
            MMS: mma_0302(tyrS)
            NEU: NE1431
            NET: Neut_1545
            NMU: Nmul_A0502
            EBA: ebA931(tyrS)
            AZO: azo2756
            DAR: Daro_3175
            TBD: Tbd_0459
            MFA: Mfla_0064
            HPY: HP0774(tyr)
            HPJ: jhp0711(tyrS)
            HPA: HPAG1_0759
            HHE: HH0830(tyrS)
            HAC: Hac_0639(tyrS)
            WSU: WS0241(tyrS)
            TDN: Tmden_0720
            CJE: Cj1271c(tyrS)
            CJR: CJE1407(tyrS)
            CJJ: CJJ81176_1287(tyrS)
            CJU: C8J_1215(tyrS)
            CJD: JJD26997_0454(tyrS)
            CFF: CFF8240_1211(tyrS)
            CCV: CCV52592_0484(tyrS)
            CHA: CHAB381_1280(tyrS)
            CCO: CCC13826_0499(tyrS) CCC13826_1296(tyrS)
            ABU: Abu_0644(tyrS)
            NIS: NIS_0761(tyrS)
            SUN: SUN_1744(tyrS)
            GSU: GSU1139(tyrS)
            GME: Gmet_1182
            PCA: Pcar_2348
            PPD: Ppro_3310
            DVU: DVU0953(tyrS)
            DDE: Dde_0228
            LIP: LI0022(tyrS)
            BBA: Bd1189(tyrS)
            DPS: DP2869
            ADE: Adeh_1044
            AFW: Anae109_1094
            MXA: MXAN_2976(tyrS)
            SAT: SYN_02977
            SFU: Sfum_2577
            RPR: RP556
            RTY: RT0544(tyrS)
            RCO: RC0823(tyrS)
            RFE: RF_0877(tyrS)
            RBE: RBE_0911(tyrS)
            RAK: A1C_04095
            RCM: A1E_02195
            RRI: A1G_04630
            OTS: OTBS_0179(tyrS)
            WOL: WD1115(tyrS)
            WBM: Wbm0248
            AMA: AM1205(tyrS)
            APH: APH_1244(tyrS)
            ERU: Erum0620(tyrS)
            ERW: ERWE_CDS_00530(tyrS)
            ERG: ERGA_CDS_00520(tyrS)
            ECN: Ecaj_0055
            ECH: ECH_0091(tyrS)
            NSE: NSE_0345(tyrS)
            PUB: SAR11_0735(tyrS)
            MLO: mll0007
            MES: Meso_1785
            PLA: Plav_3267
            SME: SMc00526(tyrS)
            SMD: Smed_1473
            ATU: Atu1828(tyrS)
            ATC: AGR_C_3358
            RET: RHE_CH02258(tyrS)
            RLE: RL2588(tyrS) RL3013(tyrS)
            BME: BMEI1047
            BMF: BAB1_0943
            BMS: BR0926(tyrS)
            BMB: BruAb1_0935(tyrS)
            BOV: BOV_0920(tyrS)
            OAN: Oant_2260
            BJA: bll4330(tyrS)
            BRA: BRADO3532(tyrS)
            BBT: BBta_3960(tyrS)
            RPA: RPA2460(tyrS)
            RPB: RPB_2998
            RPC: RPC_2845
            RPD: RPD_2452
            RPE: RPE_2972
            NWI: Nwi_1668
            NHA: Nham_2332
            BHE: BH08670(tyrS)
            BQU: BQ05920(tyrS)
            BBK: BARBAKC583_0806(tyrS)
            XAU: Xaut_4474
            CCR: CC_1870
            SIL: SPO2484(tyrS)
            SIT: TM1040_0923
            RSP: RSP_4041(tyrS)
            RSH: Rsph17029_1155
            RSQ: Rsph17025_0927
            JAN: Jann_1792
            RDE: RD1_3146(tyrS)
            PDE: Pden_1913
            MMR: Mmar10_1308
            HNE: HNE_2625(tyrS)
            ZMO: ZMO1643(tyrS)
            NAR: Saro_2100
            SAL: Sala_1649
            SWI: Swit_1513
            ELI: ELI_05915
            GOX: GOX1364
            GBE: GbCGDNIH1_1946
            ACR: Acry_0726
            RRU: Rru_A2032
            MAG: amb3035
            MGM: Mmc1_2333
            ABA: Acid345_3069
            BSU: BG10371(tyrS) BG10555(tyrZ)
            BHA: BH3228(tyrZ)
            BAN: BA4911(tyrS-1) BA5314(tyrS-2)
            BAR: GBAA4911(tyrS-1) GBAA5314(tyrS-2)
            BAA: BA_0173 BA_5330
            BAT: BAS4556 BAS4936
            BCE: BC4657 BC5062
            BCA: BCE_4796(tyrS) BCE_5211(tyrS)
            BCZ: BCZK4407(tyrS) BCZK4797(tyrS)
            BCY: Bcer98_3333
            BTK: BT9727_4391(tyrS) BT9727_4777(tyrS)
            BTL: BALH_4238(tyrS) BALH_4603(tyrS)
            BLI: BL00439(tyrS) BL00484(tyrZ)
            BLD: BLi00666(tyrZ) BLi03118(tyrS)
            BCL: ABC2758(tyrZ)
            BAY: RBAM_026790(tyrS)
            BPU: BPUM_2615(tyrS)
            OIH: OB2218(tyrS)
            GKA: GK2803(tyrS)
            GTN: GTNG_2709
            SAU: SA1550(tyrS)
            SAV: SAV1729(tyrS)
            SAM: MW1671(tyrS)
            SAR: SAR1806(tyrS)
            SAS: SAS1655
            SAC: SACOL1778(tyrS)
            SAB: SAB1587c(tyrS)
            SAA: SAUSA300_1675(tyrS)
            SAO: SAOUHSC_01839
            SAJ: SaurJH9_1784
            SAH: SaurJH1_1819
            SEP: SE1406
            SER: SERP1293(tyrS)
            SHA: SH1192(tyrS)
            SSP: SSP1034
            LMO: lmo1598(tyrS)
            LMF: LMOf2365_1619(tyrS)
            LIN: lin1639(tyrS)
            LWE: lwe1612(tyrS)
            LLA: L0359(tyrS)
            LLC: LACR_0431
            LLM: llmg_0401(tyrS)
            SPY: SPy_0096(tyrS)
            SPZ: M5005_Spy_0081(tyrS)
            SPM: spyM18_0096(tyrS)
            SPG: SpyM3_0073(tyrS)
            SPS: SPs0074
            SPH: MGAS10270_Spy0083(tyrS)
            SPI: MGAS10750_Spy0088(tyrS)
            SPJ: MGAS2096_Spy0084(tyrS)
            SPK: MGAS9429_Spy0081(tyrS)
            SPF: SpyM50079(tyrS)
            SPA: M6_Spy0129
            SPB: M28_Spy0079(tyrS)
            SPN: SP_2100
            SPR: spr1910(tyrS)
            SPD: SPD_1926(tyrS)
            SAG: SAG0158(tyrS)
            SAN: gbs0154(tyrS)
            SAK: SAK_0221(tyrS)
            SMU: SMU.1992(tyrS)
            STC: str1870(tyrS)
            STL: stu1870(tyrS)
            STE: STER_1847
            SSA: SSA_0174(tyrS)
            SSV: SSU98_0120
            SGO: SGO_1929(tyrS)
            LPL: lp_2807(tyrS)
            LJO: LJ0175
            LAC: LBA0192
            LSA: LSA0769(tyrS)
            LSL: LSL_1366(tyrS)
            LDB: Ldb0256(tyrS)
            LBU: LBUL_0219
            LBR: LVIS_0424 LVIS_2214
            LCA: LSEI_2031
            LGA: LGAS_0177
            LRE: Lreu_0148
            PPE: PEPE_0235
            EFA: EF0633(tryS-1) EF1739(tryS-2)
            OOE: OEOE_1815
            LME: LEUM_2044
            STH: STH1122(tyrS)
            CAC: CAC0637(tyrS) CAC0780(tyrZ)
            CPE: CPE0652(tyrS)
            CPF: CPF_0633(tyrS)
            CPR: CPR_0619(tyrS)
            CTC: CTC02446
            CNO: NT01CX_1364(tyrS)
            CTH: Cthe_0723
            CDF: CD1521(tyrR)
            CBO: CBO1204(tyrR) CBO3323(tyrS)
            CBA: CLB_1234(tyrS-1) CLB_3381(tyrS-2)
            CBH: CLC_1246(tyrS-1) CLC_3268(tyrS-2)
            CBF: CLI_1287(tyrS-1) CLI_3496(tyrS-2)
            CBE: Cbei_2416 Cbei_4615
            CKL: CKL_0758(tyrS1) CKL_3527(tyrS2)
            AMT: Amet_3606
            CHY: CHY_1561(tyrS)
            DSY: DSY0289 DSY3830
            DRM: Dred_1647
            SWO: Swol_1110
            CSC: Csac_1470
            TTE: TTE2679(tyrS)
            MTA: Moth_1709
            MGE: MG_455(tyrS)
            MPN: MPN669(tyrS)
            MPU: MYPU_4850(tyrS)
            MPE: MYPE7960(tyrS)
            MGA: MGA_1144(tyrS)
            MMY: MSC_0686(tyrS)
            MMO: MMOB5470(tyrS)
            MHY: mhp066(tyrS)
            MHJ: MHJ_0059(tyrS)
            MHP: MHP7448_0063(tyrS)
            MSY: MS53_0622(tyrS)
            MCP: MCAP_0639(tyrS)
            UUR: UU117(tyrS)
            POY: PAM469(tyrS)
            AYW: AYWB_309(tyrS)
            MFL: Mfl587
            MTU: Rv1689(tyrS)
            MTC: MT1728(tyrS)
            MBO: Mb1715(tyrS)
            MBB: BCG_1727(tyrS)
            MLE: ML1352(tyrS)
            MPA: MAP1396(tyrS)
            MAV: MAV_3082(tyrS)
            MSM: MSMEG_3758(tyrS)
            MVA: Mvan_3294
            MGI: Mflv_3513
            MMC: Mmcs_2955
            MKM: Mkms_2999
            MJL: Mjls_2970
            CGL: NCgl1352(cgl1406)
            CGB: cg1594(tyrS)
            CEF: CE1540
            CDI: DIP1176(tyrS)
            CJK: jk0860(tyrS)
            NFA: nfa19910(tyrS)
            RHA: RHA1_ro00942(tyrS)
            SCO: SCO1818(tyrS)
            SMA: SAV6459(tyrS)
            TWH: TWT169(tyrS)
            TWS: TW603(tyrS)
            LXX: Lxx06140(tyrS)
            ART: Arth_1512
            AAU: AAur_1643(tyrS)
            PAC: PPA1404
            NCA: Noca_1979
            TFU: Tfu_2043
            FRA: Francci3_3946
            FAL: FRAAL6261(tyrS)
            ACE: Acel_1254
            KRA: Krad_3153
            SEN: SACE_5254(tyrS)
            STP: Strop_1905
            BLO: BL1051(tyrS)
            BAD: BAD_0914(tyrS)
            FNU: FN0054
            RBA: RB9134(tyrS)
            CTR: CT062(tyrS)
            CTA: CTA_0067(tyrS)
            CMU: TC0332
            CPN: CPn0361(tyrS)
            CPA: CP0397
            CPJ: CPj0361(tyrS)
            CPT: CpB0370
            CCA: CCA00431(tyrS)
            CAB: CAB417(tyrS)
            CFE: CF0577(tyrS)
            PCU: pc1169(tyrS)
            BGA: BG0369(tyrS)
            BAF: BAPKO_0379(tyrS)
            TPA: TP0834
            TDE: TDE0861(tyrS)
            LIL: LA2237(tyrS)
            LIC: LIC11698(tyrS)
            LBJ: LBJ_1381(tyrS)
            LBL: LBL_1606(tyrS)
            SYN: slr1031(tyrS) ssr1720(tyrS)
            SYW: SYNW0568(tyrS)
            SYC: syc1540_d(tyrS)
            SYF: Synpcc7942_2570
            SYD: Syncc9605_2102
            SYE: Syncc9902_0567
            SYG: sync_2203(tyrS)
            SYR: SynRCC307_1805(tyrS)
            SYX: SynWH7803_1946(tyrS)
            CYA: CYA_2096(tyrS)
            CYB: CYB_2511(tyrS)
            TEL: tlr0050(tyrS)
            GVI: gll4415(tyrS)
            ANA: alr2982(tyrS)
            AVA: Ava_0925
            PMA: Pro1410(tyrS)
            PMM: PMM1329(tyrS)
            PMT: PMT1403(tyrS)
            PMN: PMN2A_0900
            PMI: PMT9312_1427
            PMB: A9601_15291(tyrS)
            PMC: P9515_14901(tyrS)
            PMF: P9303_05611(tyrS)
            PMG: P9301_15151(tyrS)
            PMH: P9215_15581(tyrS)
            PME: NATL1_17561(tyrS)
            TER: Tery_0445
            BTH: BT_3230
            BFR: BF0068
            BFS: BF0079(tyrS)
            PGI: PG0263(tyrS)
            SRU: SRU_1623(tyrS)
            CHU: CHU_1536(tyrS)
            GFO: GFO_0112(tyrS)
            FJO: Fjoh_0550 Fjoh_3386
            FPS: FP0161(tyrS)
            CTE: CT0563(tyrS)
            CCH: Cag_1161
            CPH: Cpha266_0814
            PLT: Plut_0568
            DET: DET0601(tyrS)
            DEH: cbdb_A583(tyrS)
            RRS: RoseRS_2069
            RCA: Rcas_1792
            DRA: DR_2634
            DGE: Dgeo_0006
            TTH: TTC1033(tyr)
            TTJ: TTHA1399
            AAE: aq_1751(tyrS)
            TMA: TM0478
            MJA: MJ0389(tyrS)
            MMP: MMP0263(tyrS)
            MAC: MA0815(tyrS)
            MBA: Mbar_A1745
            MMA: MM_1963
            MBU: Mbur_1463
            MHU: Mhun_2463
            MST: Msp_0359(tyrS)
            MSI: Msm_0513
            MKA: MK0516(tyrS)
            HAL: VNG2237G(tyrS)
            HMA: rrnAC0543(tyrS)
            HWA: HQ3400A(tyrS)
            NPH: NP2810A(tyrS)
            TAC: Ta0512
            TVO: TVN0989
            PTO: PTO0226
            PHO: PH1011
            PAB: PAB1728(tyrS)
            PFU: PF0862
            TKO: TK0568
            RCI: RCIX2415(tyrS)
            APE: APE_2074.1
            HBU: Hbut_0889
            SSO: SSO0078(tyrS)
            STO: ST2074
            SAI: Saci_0076(tys1)
            PAI: PAE0630 PAE1931
            NEQ: NEQ389
STRUCTURES  PDB: 1H3E  1J1U  1JH3  1JII  1JIJ  1JIK  1JIL  1N3L  1NTG  1Q11  
                 1TYA  1TYB  1TYC  1TYD  1U7D  1U7X  1VBM  1VBN  1WQ3  1WQ4  
                 1X8X  1Y42  1ZH0  1ZH6  2AG6  2CYA  2CYB  2CYC  2DLC  2HGZ  
                 2J5B  2TS1  3TS1  4TS1  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.1
            ExPASy - ENZYME nomenclature database: 6.1.1.1
            ExplorEnz - The Enzyme Database: 6.1.1.1
            ERGO genome analysis and discovery system: 6.1.1.1
            BRENDA, the Enzyme Database: 6.1.1.1
            CAS: 9023-45-4
///
ENTRY       EC 6.1.1.2                  Enzyme
NAME        tryptophan---tRNA ligase;
            tryptophanyl-tRNA synthetase;
            L-tryptophan-tRNATrp ligase (AMP-forming);
            tryptophanyl-transfer ribonucleate synthetase;
            tryptophanyl-transfer ribonucleic acid synthetase;
            tryptophanyl-transfer RNA synthetase;
            tryptophanyl ribonucleic synthetase;
            tryptophanyl-transfer ribonucleic synthetase;
            tryptophanyl-tRNA synthase;
            tryptophan translase;
            TrpRS
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-tryptophan:tRNATrp ligase (AMP-forming)
REACTION    ATP + L-tryptophan + tRNATrp = AMP + diphosphate +
            L-tryptophyl-tRNATrp [RN:R03664]
ALL_REAC    R03664
SUBSTRATE   ATP [CPD:C00002];
            L-tryptophan [CPD:C00078];
            tRNA(Trp) [CPD:C01652]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-tryptophyl-tRNATrp
REFERENCE   1  [PMID:13373404]
  AUTHORS   DAVIE EW, KONINGSBERGER VV, LIPMANN F.
  TITLE     The isolation of a tryptophan-activating enzyme from pancreas.
  JOURNAL   Arch. Biochem. Biophys. 65 (1956) 21-38.
REFERENCE   2  [PMID:5805407]
  AUTHORS   Preddie EC.
  TITLE     Tryptophanyl transfer ribonucleic acid synthetase from bovine
            pancreas. II. The chemically different subunits.
  JOURNAL   J. Biol. Chem. 244 (1969) 3958-68.
  ORGANISM  cow [GN:bta]
REFERENCE   3
  AUTHORS   Wong, K.K., Meister, A. and Moldave, K.
  TITLE     Enzymic formation of ribonucleic acid-amino acid from synthetic
            aminoacyladenylate and ribonucleic acid.
  JOURNAL   Biochim. Biophys. Acta 36 (1959) 531-533.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00380  Tryptophan metabolism
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01867  tryptophanyl-tRNA synthetase
GENES       HSA: 10352(WARS2) 7453(WARS)
            MMU: 22375(Wars) 70560(Wars2)
            CFA: 480435(WARS) 483145(WARS2)
            BTA: 281576(WARS)
            GGA: 418312(WARS2) 423458(WARS)
            XLA: 380225(wars) 414492(MGC81110)
            DRE: 393745(wars)
            SPU: 574927(LOC574927)
            DME: Dmel_CG7441 Dmel_CG9735(Aats-trp)
            CEL: Y80D3A.1(wrs-1)
            OSA: 4326551
            CME: CMB010C CMG043C
            SCE: YDR268W(MSW1) YOL097C(WRS1)
            AGO: AGOS_ACR089C AGOS_ADR117W
            PIC: PICST_46284(MSW1) PICST_53719(SYWC)
            CGR: CAGL0I07579g CAGL0M08624g
            SPO: SPAC2F7.13c SPAC3G9.13c
            ANI: AN6488.2
            AFM: AFUA_2G01640 AFUA_6G05340
            AOR: AO090012000399 AO090701000003 AO090701000783
            UMA: UM03798.1
            ECU: ECU11_0530
            DDI: DDB_0231245(trpS) DDB_0231246(mtrpS)
            PFA: PF13_0205 PFL2485c
            CPV: cgd7_1490
            CHO: Chro.70176
            TAN: TA10040 TA20460
            TPV: TP01_0518 TP04_0776
            TET: TTHERM_00500890 TTHERM_00997610
            TBR: Tb927.3.5580 Tb927.8.2240
            TCR: 506375.10 506375.60 507589.14 510647.30 510671.20
            LMA: LmjF23.0300 LmjF29.0060
            EHI: 334.t00004 5.t00005
            ECO: b3384(trpS)
            ECJ: JW3347(trpS)
            ECE: Z4737(trpS)
            ECS: ECs4226
            ECC: c4154(trpS)
            ECI: UTI89_C3882(trpS)
            ECP: ECP_3469
            ECV: APECO1_3079(trpS)
            ECW: EcE24377A_3853(trpS)
            ECX: EcHS_A3580(trpS)
            STY: STY4315(trpS) STY4863(trpS2)
            STT: t4024(trpS) t4557(trpS)
            SPT: SPA3346(trpS) SPA4327
            SEC: SC3413(trpS) SC4363(trpS2)
            STM: STM3481(trpS) STM4508(trpS2)
            YPE: YPO0157(trpS)
            YPK: y3940(trpS)
            YPM: YP_0159(trpS)
            YPA: YPA_3312
            YPN: YPN_3908
            YPP: YPDSF_0084
            YPS: YPTB3744(trpS)
            YPI: YpsIP31758_3960(trpS)
            SFL: SF3402(trpS)
            SFX: S4360(trpS)
            SFV: SFV_3389(trpS)
            SSN: SSON_3515(trpS)
            SBO: SBO_3371(trpS)
            SDY: SDY_3695(trpS)
            ECA: ECA4087(trpS)
            PLU: plu0084(trpS)
            BUC: BU536(trpS)
            BAS: BUsg517(trpS)
            BAB: bbp478(trpS)
            BCC: BCc_350(trpS)
            WBR: WGLp581(trpS)
            SGL: SG2304
            ENT: Ent638_0485 Ent638_3797
            KPN: KPN_04752(trpS)
            SPE: Spro_1406 Spro_4599
            BFL: Bfl569(trpS)
            BPN: BPEN_589(trpS)
            HIN: HI0637(trpS)
            HIT: NTHI0755(trpS)
            HIP: CGSHiEE_09040
            HIQ: CGSHiGG_06445
            HDU: HD0177(trpS)
            HSO: HS_0177(trpS)
            PMU: PM1621(trpS)
            MSU: MS2332(trpS)
            APL: APL_1892(trpS)
            ASU: Asuc_0220
            XFA: XF0428
            XFT: PD1650(trpS)
            XCC: XCC3923(trpS)
            XCB: XC_4011
            XCV: XCV4098(trpS)
            XAC: XAC4006(trpS)
            XOO: XOO0437(trpS)
            XOM: XOO_0401(XOO0401)
            VCH: VC2623
            VCO: VC0395_A2200(trpS)
            VVU: VV1_1307
            VVY: VV3058
            VPA: VP1096 VP2804
            VFI: VF2286
            PPR: PBPRA0286 PBPRB0397(trpS)
            PAE: PA4439(trpS)
            PAU: PA14_57670(trpS)
            PAP: PSPA7_5011(trpS)
            PPU: PP_1311
            PPF: Pput_4413
            PST: PSPTO_4429(trpS)
            PSB: Psyr_4123
            PSP: PSPPH_4129(trpS)
            PFL: PFL_5087(trpS)
            PFO: Pfl_4699
            PEN: PSEEN4511(trpS)
            PMY: Pmen_0894 Pmen_1837
            PAR: Psyc_1568(trpS)
            PCR: Pcryo_1750
            PRW: PsycPRwf_1953
            ACI: ACIAD2871(trpS)
            SON: SO_0294(trpS)
            SDN: Sden_0269
            SFR: Sfri_0383
            SAZ: Sama_3360
            SBL: Sbal_4105
            SBM: Shew185_4075
            SLO: Shew_0221
            SPC: Sputcn32_3698
            SSE: Ssed_4257
            SPL: Spea_0246
            SHE: Shewmr4_3690
            SHM: Shewmr7_0255
            SHN: Shewana3_3886
            SHW: Sputw3181_3840
            ILO: IL2323(trpS)
            CPS: CPS_0480(trpS)
            PHA: PSHAa2708(trpS)
            PAT: Patl_0658
            SDE: Sde_2228
            PIN: Ping_0168
            MAQ: Maqu_1159
            CBU: CBU_2049(trpS)
            CBD: COXBU7E912_2145(trpS)
            LPN: lpg1444(trpS)
            LPF: lpl1597(trpS)
            LPP: lpp1399(trpS)
            MCA: MCA2526(trpS)
            FTU: FTT1488(trpS)
            FTF: FTF1488(trpS)
            FTW: FTW_0805(trpS)
            FTL: FTL_0306
            FTH: FTH_0307(trpS)
            FTA: FTA_0325(trpS)
            FTN: FTN_1499(trpS)
            TCX: Tcr_1530
            NOC: Noc_1038
            AEH: Mlg_0720
            HHA: Hhal_0584
            HCH: HCH_02552(trpS) HCH_04739
            CSA: Csal_2965
            ABO: ABO_1390(trpS)
            MMW: Mmwyl1_3230
            AHA: AHA_0049(trpS-1) AHA_3183(trpS-2)
            ASA: ASA_0045(trpS)
            DNO: DNO_0236(trpS)
            BCI: BCI_0021(trpS)
            CRP: CRP_114
            RMA: Rmag_0338
            VOK: COSY_0320(trpS)
            NME: NMB1471
            NMA: NMA1682(trpS)
            NMC: NMC1408(trpS)
            NGO: NGO1045
            CVI: CV_1697(trpS1) CV_3715(trpS2)
            RSO: RSc1143(trpS)
            REU: Reut_A0501
            REH: H16_A0515(trpS)
            RME: Rmet_0440
            BMA: BMA1680(trpS-1) BMAA0230(trpS-2)
            BMV: BMASAVP1_1413(trpS-2) BMASAVP1_A2182(trpS)
            BML: BMA10299_1609(trpS-2) BMA10299_A3135(trpS)
            BMN: BMA10247_1455(trpS) BMA10247_A0267(trpS-2)
            BXE: Bxe_A1583 Bxe_B0406
            BVI: Bcep1808_2176 Bcep1808_5675
            BUR: Bcep18194_A5403 Bcep18194_C6975
            BCN: Bcen_1413 Bcen_5980
            BCH: Bcen2424_2097 Bcen2424_6416
            BAM: Bamb_2134 Bamb_5680
            BPS: BPSL2260 BPSS1865(trpS)
            BPM: BURPS1710b_2701(trpS-1) BURPS1710b_A0956(trpS)
            BPL: BURPS1106A_2621(trpS) BURPS1106A_A2528(trpS)
            BPD: BURPS668_2567(trpS) BURPS668_A2670(trpS)
            BTE: BTH_I1904 BTH_II0512(trpS)
            PNU: Pnuc_0845
            BPE: BP1143(trpS)
            BPA: BPP3202(trpS)
            BBR: BB3602(trpS)
            RFR: Rfer_3240
            POL: Bpro_1001
            PNA: Pnap_3278
            AAV: Aave_3711
            AJS: Ajs_3438
            VEI: Veis_1623
            MPT: Mpe_A2640
            HAR: HEAR2177(trpS)
            MMS: mma_0845(trpS)
            NEU: NE1727(trpS)
            NET: Neut_2042
            NMU: Nmul_A2317
            EBA: ebA6131(trpS)
            AZO: azo3695(trpS)
            DAR: Daro_2459
            TBD: Tbd_1525
            MFA: Mfla_1138
            HPY: HP1253
            HPJ: jhp1174(trpS)
            HPA: HPAG1_1197
            HHE: HH0558(trpS)
            HAC: Hac_0232(trpS)
            WSU: WS0311
            TDN: Tmden_0389
            CJE: Cj0388(trpS)
            CJR: CJE0437(trpS)
            CJJ: CJJ81176_0411(trpS)
            CJU: C8J_0363(trpS)
            CJD: JJD26997_1570(trpS)
            CFF: CFF8240_1341(trpS)
            CCV: CCV52592_1188(trpS)
            CHA: CHAB381_0050(trpS)
            CCO: CCC13826_0669 CCC13826_0775(trpS)
            ABU: Abu_0327(trpS)
            NIS: NIS_1370(trpS)
            SUN: SUN_1925(trpS)
            GSU: GSU1833(trpS)
            GME: Gmet_1960
            GUR: Gura_2250
            PCA: Pcar_0588
            PPD: Ppro_0579 Ppro_1687
            DVU: DVU0142(trpS)
            DVL: Dvul_2825
            DDE: Dde_3607
            LIP: LI0020(trpS)
            BBA: Bd0507(trpS)
            DPS: DP1644
            ADE: Adeh_1685
            AFW: Anae109_2119
            MXA: MXAN_3842(trpS)
            SAT: SYN_02857
            SFU: Sfum_0682
            RPR: RP468
            RTY: RT0455(trpS)
            RCO: RC0710(trpS)
            RFE: RF_0824(trpS)
            RBE: RBE_0790(trpS)
            RAK: A1C_03905
            RBO: A1I_05070
            RCM: A1E_02425
            RRI: A1G_04020
            OTS: OTBS_0762(trpS) OTBS_1824(trpS)
            WOL: WD0801(trpS)
            WBM: Wbm0534
            AMA: AM012(trpS)
            APH: APH_0035(trpS)
            ERU: Erum1120(trpS)
            ERW: ERWE_CDS_01090(trpS)
            ERG: ERGA_CDS_01050(trpS)
            ECN: Ecaj_0110
            ECH: ECH_0167(trpS)
            NSE: NSE_0213(trpS)
            PUB: SAR11_0377(trpS)
            MLO: mll5317
            MES: Meso_4035
            PLA: Plav_2364 Plav_3608
            SME: SMc01121(trpS)
            SMD: Smed_0034
            ATU: Atu0349(trpS)
            ATC: AGR_C_611
            RET: RHE_CH00383(trpS)
            RLE: RL0402(trpS)
            BME: BMEI1806
            BMF: BAB1_0141(trpS)
            BMS: BR0142(trpS)
            BMB: BruAb1_0139(trpS)
            BOV: BOV_0136(trpS)
            OAN: Oant_0155
            BJA: bll0802(trpS)
            BRA: BRADO0033(trpS)
            BBT: BBta_0038(trpS)
            RPA: RPA0455(trpS)
            RPB: RPB_0583
            RPC: RPC_0459
            RPD: RPD_0249
            RPE: RPE_0216
            NWI: Nwi_0216
            NHA: Nham_0012
            BHE: BH13470(trpS)
            BQU: BQ10700(trpS)
            BBK: BARBAKC583_1167(trpS)
            XAU: Xaut_3085
            CCR: CC_0064
            SIL: SPO0392(trpS)
            SIT: TM1040_0443
            RSP: RSP_1808(trpS)
            RSH: Rsph17029_0455
            RSQ: Rsph17025_0466
            JAN: Jann_0894
            RDE: RD1_1185(trpS)
            PDE: Pden_3953
            MMR: Mmar10_3024
            HNE: HNE_0520(trpS)
            ZMO: ZMO1640(trpS)
            NAR: Saro_0588
            SAL: Sala_2013
            SWI: Swit_3827
            ELI: ELI_10510
            GOX: GOX0259
            GBE: GbCGDNIH1_2415
            ACR: Acry_1020
            RRU: Rru_A3535
            MAG: amb4408
            MGM: Mmc1_1037
            ABA: Acid345_3860
            SUS: Acid_5840
            BSU: BG10799(trpS)
            BHA: BH2200 BH2870(trpS)
            BAN: BA1188(trpS) BA3408
            BAR: GBAA1188(trpS) GBAA3408
            BAA: BA_1726 BA_3906
            BAT: BAS1099 BAS3159
            BCE: BC3340
            BCA: BCE_1297(trpS) BCE_3376
            BCZ: BCZK1075(trpS) BCZK3053(trpS)
            BCY: Bcer98_0894 Bcer98_2370
            BTK: BT9727_1081(trpS) BT9727_3143(trpS)
            BLI: BL03339(trpS)
            BLD: BLi01231(trpS)
            BCL: ABC0274 ABC2535(trpS)
            BAY: RBAM_011420(trpS)
            BPU: BPUM_1068(trpS)
            OIH: OB1208(trpS)
            GKA: GK0809(trpS)
            GTN: GTNG_0689
            SAU: SA0855(trpS)
            SAV: SAV0996(trpS)
            SAM: MW0878(trpS)
            SAR: SAR0964(trpS)
            SAS: SAS0866
            SAC: SACOL1001(trpS)
            SAB: SAB0863c(trpS)
            SAA: SAUSA300_0897(trpS)
            SAO: SAOUHSC_00933
            SAJ: SaurJH9_0995
            SAH: SaurJH1_1014
            SEP: SE0685
            SER: SERP0575(trpS)
            SHA: SH1962(trpS)
            SSP: SSP1789
            LMO: lmo2198(trpS)
            LMF: LMOf2365_2231(trpS)
            LIN: lin2301(trpS)
            LWE: lwe2215(trpS)
            LLA: L0358(trpS)
            LLC: LACR_0058
            LLM: llmg_0079(trpS)
            SPY: SPy_2207(trsA)
            SPZ: M5005_Spy_1858(trsA)
            SPM: spyM18_2245(trpS)
            SPG: SpyM3_1858(trsA)
            SPS: SPs1854
            SPH: MGAS10270_Spy1978 MGAS10270_Spy1979(trsA)
            SPI: MGAS10750_Spy1971(trsA)
            SPJ: MGAS2096_Spy1889(trsA)
            SPK: MGAS9429_Spy1869(trsA)
            SPF: SpyM51831(trpS)
            SPA: M6_Spy1876
            SPB: M28_Spy1891(trsA)
            SPN: SP_2229
            SPR: spr2034(trpS)
            SPD: SPD_2056(trpS)
            SAG: SAG2168(trpS)
            SAN: gbs2127(trpS)
            SAK: SAK_2126(trpS)
            SMU: SMU.2158c
            STC: str2018(trpS)
            STL: stu2018(trpS)
            STE: STER_1993
            SSA: SSA_2375(trpS)
            SSU: SSU05_2184
            SSV: SSU98_2182
            SGO: SGO_0007(trpS)
            LPL: lp_0434(trpS)
            LJO: LJ0198
            LAC: LBA0209
            LSA: LSA0327(trpS)
            LSL: LSL_0218(trpS)
            LDB: Ldb0338(trpS)
            LBU: LBUL_0293
            LBR: LVIS_0448
            LCA: LSEI_2624
            LGA: LGAS_0201
            LRE: Lreu_0204
            PPE: PEPE_0256
            EFA: EF2228 EF2679(trpS)
            OOE: OEOE_1800
            LME: LEUM_1856
            STH: STH1411(trpS)
            CAC: CAC0626(trpS)
            CPE: CPE0633(trpS)
            CPF: CPF_0614(trpS)
            CPR: CPR_0600(trpS)
            CTC: CTC02453
            CNO: NT01CX_1355(trpS)
            CTH: Cthe_0686
            CDF: CD2610(trpS)
            CBO: CBO3331(trpS)
            CBA: CLB_3389(trpS)
            CBH: CLC_3276(trpS)
            CBF: CLI_3504(trpS)
            CBE: Cbei_0798
            CKL: CKL_0610(trpS)
            AMT: Amet_1200
            CHY: CHY_1947(trpS)
            DSY: DSY1052 DSY2289
            DRM: Dred_1133
            SWO: Swol_0672
            CSC: Csac_0937
            TTE: TTE1453(trpS)
            MTA: Moth_1919
            MGE: MG_126(trpS)
            MPN: MPN265(trpS)
            MPU: MYPU_7450(trpS)
            MPE: MYPE4580(trpS)
            MGA: MGA_0293(trpS)
            MMY: MSC_0358(trpS)
            MMO: MMOB5010(trpS)
            MHY: mhp609(trpS)
            MHJ: MHJ_0590(trpS)
            MHP: MHP7448_0590(trpS)
            MSY: MS53_0169(trpS)
            MCP: MCAP_0342(trpS)
            UUR: UU175(trpS)
            POY: PAM466(trpS)
            AYW: AYWB_312(trpS)
            MFL: Mfl192
            MTU: Rv3336c(trpS)
            MTC: MT3440(trpS)
            MBO: Mb3369c(trpS)
            MBB: BCG_3407c(trpS)
            MLE: ML0686(trpS)
            MPA: MAP3453c(trpS)
            MAV: MAV_4310(trpS)
            MSM: MSMEG_1657(trpS)
            MVA: Mvan_1560
            MGI: Mflv_4871
            MMC: Mmcs_1212
            MKM: Mkms_1229
            MJL: Mjls_1239
            CGL: NCgl0647(cgl0677)
            CGB: cg0779(trpS)
            CEF: CE0696
            CDI: DIP0635(trpS)
            CJK: jk1689(trpS)
            NFA: nfa9360(trpS)
            RHA: RHA1_ro06241(trpS)
            SCO: SCO3334(SCE68.32) SCO4839(SC5G8.07)
            SMA: SAV3417(trpS1) SAV4725(trpS2)
            TWH: TWT686(trpS)
            TWS: TW705(trpS)
            LXX: Lxx04450(trpS)
            ART: Arth_1122
            AAU: AAur_1237(trpS)
            PAC: PPA1327
            NCA: Noca_0482
            TFU: Tfu_2376
            FRA: Francci3_1867 Francci3_3963
            FAL: FRAAL6284(trpS)
            ACE: Acel_0390
            KRA: Krad_3969
            SEN: SACE_1002(trpS) SACE_6592(trpS)
            STP: Strop_0797
            BLO: BL0600(trpS)
            BAD: BAD_0027(trpS)
            RXY: Rxyl_0275
            FNU: FN0405
            RBA: RB6436(trpS)
            CTR: CT585(trpS)
            CTA: CTA_0635(trpS)
            CMU: TC0874
            CPN: CPn0802(trpS)
            CPA: CP1069
            CPJ: CPj0802(trpS)
            CPT: CpB0831
            CCA: CCA00961(trpS)
            CAB: CAB930(trpS)
            CFE: CF0053(trpS)
            PCU: pc0170(trpS)
            BBU: BB0005
            BGA: BG0005(trsA)
            BAF: BAPKO_0004(trsA)
            TPA: TP0632
            TDE: TDE1588
            LIL: LA0408(trpS)
            LIC: LIC10357(trpS)
            LBJ: LBJ_2435(trpS)
            LBL: LBL_0676(trpS)
            SYN: slr1884(trpS)
            SYW: SYNW1475(trpS)
            SYC: syc0245_c(trpS)
            SYF: Synpcc7942_1308
            SYD: Syncc9605_1037
            SYE: Syncc9902_0938
            SYG: sync_1863(trpS)
            SYR: SynRCC307_1445(trpS)
            SYX: SynWH7803_0780(trpS)
            CYA: CYA_1340(trpS)
            CYB: CYB_2214(trpS)
            TEL: tlr1996(trpS)
            GVI: glr3011(trpS)
            ANA: all1269(trpS)
            AVA: Ava_2993
            PMA: Pro1063(trpS)
            PMM: PMM0598(trpS)
            PMT: PMT0422(trpS)
            PMN: PMN2A_0034
            PMI: PMT9312_0598
            PMB: A9601_06541(trpS)
            PMC: P9515_06631(trpS)
            PMF: P9303_18651(trpS)
            PMG: P9301_06241(trpS)
            PMH: P9215_06801(trpS)
            PME: NATL1_06541(trpS)
            TER: Tery_4693
            BTH: BT_3864
            BFR: BF4036
            BFS: BF3809(trpS)
            PGI: PG2085(trpS)
            SRU: SRU_1664(trpS)
            CHU: CHU_1002(trpS)
            GFO: GFO_3251(trpS)
            FJO: Fjoh_0990
            FPS: FP2247(trpS)
            CTE: CT0013(trpS)
            CCH: Cag_0072
            CPH: Cpha266_2700
            PVI: Cvib_1730
            PLT: Plut_2090
            DET: DET1343(trpS)
            DEH: cbdb_A1293(trpS)
            DEB: DehaBAV1_1154
            DRA: DR_0558 DR_1093
            DGE: Dgeo_0450 Dgeo_1602
            TTH: TTC0864
            TTJ: TTHA1227
            AAE: aq_992(trpS)
            TMA: TM0492
            FNO: Fnod_0887
            MJA: MJ1415(trpS)
            MMP: MMP1592(trpS)
            MMQ: MmarC5_1817
            MMZ: MmarC7_0839
            MAE: Maeo_1485
            MVN: Mevan_0904
            MAC: MA0172(trpS)
            MBA: Mbar_A1374
            MMA: MM_1471
            MBU: Mbur_1426
            MTP: Mthe_0368
            MHU: Mhun_1732
            MEM: Memar_0642
            MBN: Mboo_0656
            MST: Msp_0653(trpS)
            MSI: Msm_0216
            MKA: MK0343(trpS)
            HAL: VNG2208G(trpS1) VNG2232G(trpS2)
            HMA: rrnAC2965(trpS)
            HWA: HQ1048A(trpS)
            NPH: NP0442A(trpS)
            TAC: Ta1211
            TVO: TVN1253
            PTO: PTO0262
            PHO: PH1921
            PAB: PAB1111(trpS)
            PFU: PF0241
            TKO: TK1874
            RCI: RRC219(trpS)
            APE: APE_2461.1
            IHO: Igni_1301
            HBU: Hbut_0947
            SSO: SSO0452(trpS)
            STO: ST0169
            SAI: Saci_0450(trpS)
            MSE: Msed_2178
            PAI: PAE3091
            PIS: Pisl_0454
            PCL: Pcal_1822
            PAS: Pars_1612
            TPE: Tpen_0587
            NEQ: NEQ115
STRUCTURES  PDB: 1D2R  1I6K  1I6L  1I6M  1M83  1MAU  1MAW  1MB2  1O5T  1R6T  
                 1R6U  1ULH  1YIA  1YID  2A4M  2AKE  2AZX  2DR2  2G36  2IP1  
                 2OV4  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.2
            ExPASy - ENZYME nomenclature database: 6.1.1.2
            ExplorEnz - The Enzyme Database: 6.1.1.2
            ERGO genome analysis and discovery system: 6.1.1.2
            BRENDA, the Enzyme Database: 6.1.1.2
            CAS: 9023-44-3
///
ENTRY       EC 6.1.1.3                  Enzyme
NAME        threonine---tRNA ligase;
            threonyl-tRNA synthetase;
            threonyl-transfer ribonucleate synthetase;
            threonyl-transfer RNA synthetase;
            threonyl-transfer ribonucleic acid synthetase;
            threonyl ribonucleic synthetase;
            threonine-transfer ribonucleate synthetase;
            threonine translase;
            threonyl-tRNA synthetase;
            TRS
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-threonine:tRNAThr ligase (AMP-forming)
REACTION    ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr
            [RN:R03663]
ALL_REAC    R03663
SUBSTRATE   ATP [CPD:C00002];
            L-threonine [CPD:C00188];
            tRNA(Thr) [CPD:C01651]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-threonyl-tRNA(Thr) [CPD:C02992]
REFERENCE   1  [PMID:13792726]
  AUTHORS   ALLEN EH, GLASSMAN E, SCHWEET RS.
  TITLE     Incorporation of amino acids into ribonucleic acid. I. The role of
            activating enzymes.
  JOURNAL   J. Biol. Chem. 235 (1960) 1061-7.
REFERENCE   2  [PMID:13715350]
  AUTHORS   HOLLEY RW, BRUNNGRABER EF, SAAD F, WILLIAMS HH.
  TITLE     Partial purification of the threonine- and tyrosine-activating
            enzymes from rat liver, and the effect of patassium ions on the
            activity of the tyrosine enzyme.
  JOURNAL   J. Biol. Chem. 236 (1961) 197-9.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01868  threonyl-tRNA synthetase
GENES       HSA: 6897(TARS) 80222(TARS2)
            PTR: 461951(TARS)
            MMU: 110960(Tars)
            RNO: 294810(Tars)
            CFA: 479370(TARS)
            GGA: 427427(RCJMB04_4k14)
            XLA: 447636(MGC86352)
            XTR: 407892(tarsl2)
            SPU: 583724(LOC583724)
            DME: Dmel_CG17166(mRpL39) Dmel_CG5353(Aats-thr)
            ATH: AT5G26830
            OSA: 4329580 4345200
            CME: CMO098C CMS208C
            SCE: YIL078W(THS1) YKL194C(MST1)
            AGO: AGOS_ACL039W AGOS_AER105W
            PIC: PICST_47981(MST1) PICST_78070(THS1)
            CGR: CAGL0D03542g CAGL0M12991g
            SPO: SPAC24C9.09 SPBC25H2.02(ths1)
            ANI: AN5662.2
            AFM: AFUA_1G16210 AFUA_4G13700
            AOR: AO090005001088 AO090009000201
            CNE: CNB00480
            UMA: UM03815.1 UM04848.1
            ECU: ECU07_1570
            DDI: DDB_0231248(thrS1) DDB_0231249(thrS2)
            PFA: PF11_0270
            CPV: cgd7_1710
            CHO: Chro.70201
            TAN: TA06605
            TPV: TP01_0957
            TET: TTHERM_00194650
            TBR: Tb927.5.1090
            TCR: 508299.80 511181.80
            LMA: LmjF35.1410
            EHI: 85.t00031
            ECO: b1719(thrS)
            ECJ: JW1709(thrS)
            ECE: Z2748(thrS)
            ECS: ECs2426
            ECC: c2116(thrS)
            ECI: UTI89_C1912(thrS)
            ECP: ECP_1666
            ECV: APECO1_791(thrS)
            ECW: EcE24377A_1937(thrS)
            ECX: EcHS_A1800(thrS)
            STY: STY1778(thrS)
            STT: t1213(thrS)
            SPT: SPA1511(thrS)
            SEC: SC1352(thrS)
            STM: STM1333(thrS)
            YPE: YPO2433(thrS)
            YPK: y1903(thrS)
            YPM: YP_2221(thrS)
            YPA: YPA_1778
            YPN: YPN_1888
            YPS: YPTB2342(thrS)
            YPI: YpsIP31758_1712(thrS)
            SFL: SF1512(thrS)
            SFX: S1630(thrS)
            SFV: SFV_1504(thrS)
            SSN: SSON_1439(thrS)
            SBO: SBO_1375(thrS)
            SDY: SDY_1814(thrS)
            ECA: ECA2422(thrS)
            PLU: plu2669(thrS)
            BUC: BU125(thrS)
            BAS: BUsg117(thrS)
            BAB: bbp119(thrS)
            BCC: BCc_078(thrS)
            WBR: WGLp081(thrS)
            SGL: SG1419
            BFL: Bfl351(thrS)
            BPN: BPEN_362(thrS)
            HIN: HI1367(thrS)
            HIT: NTHI1797(thrS)
            HIP: CGSHiEE_04405
            HDU: HD1803(thrS)
            HSO: HS_0844(thrS)
            PMU: PM0593(thrS)
            MSU: MS1053(thrS)
            APL: APL_0219(thrS)
            XFA: XF0736
            XFT: PD1916(thrS)
            XCC: XCC2463(thrS)
            XCB: XC_1650
            XCV: XCV2795(thrS)
            XAC: XAC2594(thrS)
            XOO: XOO3187(thrS)
            XOM: XOO_3027(XOO3027)
            VCH: VCA0287
            VCO: VC0395_0942(thrS)
            VVU: VV1_2397
            VVY: VV1945
            VPA: VP1280
            VFI: VF1214 VF1215
            PPR: PBPRA2159(thrS) PBPRA2160 PBPRA2161
            PAE: PA2744(thrS)
            PAU: PA14_28650(thrS)
            PAP: PSPA7_2504(thrS)
            PPU: PP_2465(thrS)
            PST: PSPTO_2378(thrS)
            PSB: Psyr_2162
            PSP: PSPPH_2135(thrS)
            PFL: PFL_2111(thrS) PFL_6184(thrS)
            PFO: Pfl_1931
            PEN: PSEEN1963(thrS)
            PMY: Pmen_1976
            PAR: Psyc_2098(thrS)
            PCR: Pcryo_2417
            ACI: ACIAD3055(thrS)
            SON: SO_2299(thrS)
            SDN: Sden_1705
            SFR: Sfri_2028
            SAZ: Sama_1765
            SBL: Sbal_2148
            SLO: Shew_2032
            SPC: Sputcn32_2018
            SHE: Shewmr4_1955
            SHM: Shewmr7_2021
            SHN: Shewana3_2043
            SHW: Sputw3181_1994
            ILO: IL1399(thrS)
            CPS: CPS_2909(thrS)
            PHA: PSHAa1396(thrS)
            PAT: Patl_2499
            SDE: Sde_1577
            PIN: Ping_2219
            MAQ: Maqu_2061
            CBU: CBU_1326(thrS)
            CBD: COXBU7E912_1415(thrS)
            LPN: lpg2714(thrS)
            LPF: lpl2643(thrS)
            LPP: lpp2770(thrS)
            MCA: MCA0693(thrS)
            FTU: FTT0817(thrS)
            FTF: FTF0817(thrS)
            FTW: FTW_0612(thrS)
            FTL: FTL_1407
            FTH: FTH_1369(thrS)
            FTA: FTA_1494(thrS)
            FTN: FTN_1191(thrS)
            TCX: Tcr_1667
            NOC: Noc_1140
            AEH: Mlg_0768
            HHA: Hhal_0427
            HCH: HCH_02794(thrS1) HCH_04580(thrS2)
            CSA: Csal_1799
            ABO: ABO_2133(thrS)
            AHA: AHA_2327(thrS)
            DNO: DNO_0527(thrS)
            BCI: BCI_0472(thrS)
            RMA: Rmag_0648
            VOK: COSY_0595(thrS)
            NME: NMB0720
            NMA: NMA0929(thrS)
            NMC: NMC0672(thrS)
            NGO: NGO0295
            CVI: CV_1348(thrS)
            RSO: RSc1577(thrS)
            REU: Reut_A1275
            REH: H16_A1339(thrS)
            RME: Rmet_1160
            BMA: BMA1096(thrS)
            BMV: BMASAVP1_A1539(thrS)
            BML: BMA10299_A0202(thrS)
            BMN: BMA10247_0963(thrS)
            BXE: Bxe_A1371
            BVI: Bcep1808_1439
            BUR: Bcep18194_A4615 Bcep18194_C7257
            BCN: Bcen_0993
            BCH: Bcen2424_1475
            BAM: Bamb_1359 Bamb_5039
            BPS: BPSL1945(thrS)
            BPM: BURPS1710b_1890(thrS)
            BPL: BURPS1106A_1735(thrS)
            BPD: BURPS668_1712(thrS)
            BTE: BTH_I2595(thrS)
            PNU: Pnuc_0829
            BPE: BP1497(thrS)
            BPA: BPP1963(thrS)
            BBR: BB2150(thrS)
            RFR: Rfer_1336
            POL: Bpro_2102
            AAV: Aave_2859
            AJS: Ajs_2400
            VEI: Veis_3089
            MPT: Mpe_A1888
            HAR: HEAR1801(thrS)
            MMS: mma_1487(thrS)
            NEU: NE0958(thrS)
            NET: Neut_2331
            NMU: Nmul_A0487
            EBA: ebA871(thrS)
            AZO: azo1079
            DAR: Daro_2677
            TBD: Tbd_1007
            MFA: Mfla_2003
            HPY: HP0123
            HPJ: jhp0113(thrS)
            HPA: HPAG1_0122
            HHE: HH0442(thrS)
            HAC: Hac_1457(thrS)
            WSU: WS0820(thrS)
            TDN: Tmden_0066
            CJE: Cj0206(thrS)
            CJR: CJE0199(thrS)
            CJJ: CJJ81176_0238(thrS)
            CJU: C8J_0195(thrS)
            CJD: JJD26997_0216(thrS)
            CFF: CFF8240_1702(thrS)
            CCV: CCV52592_0330(thrS)
            CHA: CHAB381_0611(thrS)
            CCO: CCC13826_1819(thrS)
            ABU: Abu_0071(thrS)
            NIS: NIS_0108(thrS)
            SUN: SUN_2425(thrS)
            GSU: GSU1515(thrS)
            GME: Gmet_1411
            PCA: Pcar_1418
            DVU: DVU2538(thrS)
            DDE: Dde_2639
            LIP: LI0212(thrS)
            BBA: Bd1617(thrS) Bd1807(thrS)
            DPS: DP1428
            ADE: Adeh_1982
            MXA: MXAN_2352(thrS) MXAN_3591(thrS)
            SAT: SYN_01717
            SFU: Sfum_0424
            RPR: RP221(thrS)
            RTY: RT0212(thrS)
            RCO: RC0296(thrS)
            RFE: RF_0979(thrS)
            RBE: RBE_0535(thrS)
            RAK: A1C_01640(thrS)
            RBO: A1I_03065(thrS)
            RCM: A1E_01310(thrS)
            RRI: A1G_01690(thrS)
            OTS: OTBS_0583(thrS)
            WOL: WD0978(thrS)
            WBM: Wbm0472
            AMA: AM1273(thrS)
            APH: APH_1264(thrS)
            ERU: Erum8890(thrS)
            ERW: ERWE_CDS_09410(thrS)
            ERG: ERGA_CDS_09320(thrS)
            ECN: Ecaj_0934
            ECH: ECH_0006(thrS)
            NSE: NSE_0294(thrS)
            PUB: SAR11_0438(thrS)
            MLO: mll0914
            MES: Meso_1007
            SME: SMc01010(thrS)
            ATU: Atu1746(thrS)
            ATC: AGR_C_3205
            RET: RHE_CH02196(thrS)
            RLE: RL2528(thrS)
            BME: BMEI0915
            BMF: BAB1_1093
            BMS: BR1071(thrS)
            BMB: BruAb1_1076(thrS)
            BOV: BOV_1035(thrS)
            BJA: blr5537(thrS)
            BRA: BRADO2971(thrS) BRADO3294
            BBT: BBta_5204(thrS)
            RPA: RPA3406(thrS)
            RPB: RPB_2168
            RPC: RPC_3121
            RPD: RPD_3261
            RPE: RPE_2337
            NWI: Nwi_2035
            NHA: Nham_1669
            BHE: BH07660(thrS)
            BQU: BQ05510(thrS)
            BBK: BARBAKC583_0641(thrS)
            CCR: CC_0464
            SIL: SPO1282(thrS)
            SIT: TM1040_1721
            RSP: RSP_0385
            JAN: Jann_1098
            RDE: RD1_1883(thrS)
            MMR: Mmar10_2393
            HNE: HNE_3196(thrS)
            ZMO: ZMO0765(thrS)
            NAR: Saro_0204
            SAL: Sala_0692
            ELI: ELI_12370
            GOX: GOX0823
            GBE: GbCGDNIH1_1614
            RRU: Rru_A3487
            MAG: amb0340
            MGM: Mmc1_0363
            ABA: Acid345_4736
            BSU: BG10362(thrS) BG10421(thrZ)
            BHA: BH3141(thrS)
            BAN: BA2388(thrS-1) BA4820(thrS-2)
            BAR: GBAA2388(thrS-1) GBAA4820(thrS-2)
            BAA: BA_2882 BA_5245
            BAT: BAS2222 BAS4472
            BCE: BC2322 BC4576
            BCA: BCE_2419(thrS) BCE_4707(thrS)
            BCZ: BCZK2145(thrS) BCZK4318(thrS)
            BTK: BT9727_2161(thrS) BT9727_4307(thrS)
            BTL: BALH_2125(thrS) BALH_4160(thrS)
            BLI: BL00382(thrS)
            BLD: BLi00234(thrZ) BLi03043(thrS)
            BCL: ABC2697(thrS) ABC3978(thrZ)
            BAY: RBAM_025990(thrS)
            BPU: BPUM_0761(thrZ) BPUM_2539(thrS)
            OIH: OB2154(thrS)
            GKA: GK2719(thrS)
            SAU: SA1506(thrS)
            SAV: SAV1683(thrS)
            SAM: MW1626(thrS)
            SAR: SAR1762(thrS)
            SAS: SAS1611
            SAC: SACOL1729(thrS)
            SAB: SAB1542c(thrS)
            SAA: SAUSA300_1629(thrS)
            SAO: SAOUHSC_01788
            SEP: SE1357
            SER: SERP1246(thrS)
            SHA: SH0134(thrS) SH1242(thrS)
            SSP: SSP1082
            LMO: lmo1559(thrS)
            LMF: LMOf2365_1580(thrS)
            LIN: lin1594(thrS)
            LWE: lwe1572(thrS)
            LLA: L0357(thrS)
            LLC: LACR_2181
            LLM: llmg_2169(thrS)
            SPY: SPy_0517(thrS)
            SPZ: M5005_Spy_0427(thrS)
            SPM: spyM18_0576
            SPG: SpyM3_0365(thrS)
            SPS: SPs1488
            SPH: MGAS10270_Spy0428(thrS)
            SPI: MGAS10750_Spy0440(thrS)
            SPJ: MGAS2096_Spy0446(thrS)
            SPK: MGAS9429_Spy0426(thrS)
            SPF: SpyM51443(thrS)
            SPA: M6_Spy0454
            SPB: M28_Spy0415(thrS)
            SPN: SP_1631
            SPR: spr1472(thrS)
            SPD: SPD_1444(thrS)
            SAG: SAG0711(thrS)
            SAN: gbs0684(thrS)
            SAK: SAK_0837(thrS)
            SMU: SMU.1586(syt1)
            STC: str0572(thrS)
            STL: stu0572(thrS)
            SSA: SSA_1571(thrS)
            SGO: SGO_0778(thrS)
            LPL: lp_1514(thrS)
            LJO: LJ1645
            LAC: LBA1543(thrS)
            LSA: LSA1400(thrS)
            LSL: LSL_0494(thrS)
            LDB: Ldb1506(thrS)
            LBU: LBUL_1401
            LBR: LVIS_1036
            LCA: LSEI_1703
            EFA: EF2858(thrS)
            OOE: OEOE_0460
            STH: STH2558(thrS)
            CAC: CAC2362(thrS)
            CPE: CPE2322(thrS)
            CPF: CPF_2631(thrS)
            CPR: CPR_2317(thrS)
            CTC: CTC02286(thrS)
            CNO: NT01CX_1760(thrS)
            CDF: CD0574(thrS)
            CBO: CBO3138(thrS)
            CBA: CLB_3168(thrS)
            CBH: CLC_3041(thrS)
            CBF: CLI_3196(thrS)
            CKL: CKL_3196(thrS)
            CHY: CHY_1579(thrS)
            DSY: DSY0240
            SWO: Swol_1089
            TTE: TTE1713(thrS)
            MTA: Moth_1759
            MGE: MG_375(thrs)
            MPN: MPN553(thrSv)
            MPU: MYPU_7460(thrS)
            MPE: MYPE2740(thrS)
            MGA: MGA_0925(thrS)
            MMY: MSC_0262(thrS)
            MMO: MMOB5680(thrS)
            MHY: mhp608(thrS)
            MHJ: MHJ_0589(thrS)
            MHP: MHP7448_0589(thrS)
            MSY: MS53_0170(thrS)
            MCP: MCAP_0222(thrS)
            UUR: UU534(thrS)
            POY: PAM745(thrS)
            AYW: AYWB_663(thrS)
            MFL: Mfl177
            MTU: Rv2614c(thrS)
            MTC: MT2689(thrS)
            MBO: Mb2646c(thrS)
            MBB: BCG_2639c(thrS)
            MLE: ML0456(thrS)
            MPA: MAP2716c(thrS)
            MAV: MAV_3490(thrS)
            MSM: MSMEG_2931(thrS)
            MVA: Mvan_2558
            MMC: Mmcs_2242
            CGL: NCgl1607(cgl1671)
            CGB: cg1880(thrS)
            CEF: CE1785
            CDI: DIP1388(thrS)
            CJK: jk1066(thrS)
            NFA: nfa37120(thrS)
            RHA: RHA1_ro06878(thrS)
            SCO: SCO1531(SCL2.21c)
            SMA: SAV6822(thrS)
            TWH: TWT262(thrS)
            TWS: TW508(thrS)
            LXX: Lxx10690(thrS)
            AAU: AAur_2309(thrS)
            PAC: PPA1076
            TFU: Tfu_2108
            FRA: Francci3_3147
            FAL: FRAAL0293(thrS) FRAAL5168(thrS2)
            SEN: SACE_2004(thrS)
            BLO: BL0724(thrS)
            BAD: BAD_0800(thrS)
            RXY: Rxyl_1300
            FNU: FN0611
            RBA: RB12129
            CTR: CT581(thrS)
            CTA: CTA_0631(thrS)
            CMU: TC0870
            CPN: CPn0806(thrS)
            CPA: CP1065
            CPJ: CPj0806(thrS)
            CPT: CpB0835
            CCA: CCA00957(thrS)
            CAB: CAB926(thrS)
            CFE: CF0057(thrS)
            PCU: pc2015(thrS)
            BGA: BG0742(thrZ)
            BAF: BAPKO_0764(thrZ)
            TPA: TP0837
            TDE: TDE1090(thrS)
            LIL: LA1240(thrS)
            LIC: LIC12465(thrS)
            LBJ: LBJ_2118(thrS)
            LBL: LBL_2115(thrS)
            SYN: sll0078(thrS)
            SYW: SYNW1478(thrS)
            SYC: syc1504_d(thrS)
            SYF: Synpcc7942_2606
            SYD: Syncc9605_1034
            SYE: Syncc9902_0935
            SYG: sync_1866(thrS)
            SYR: SynRCC307_0945(thrS)
            SYX: SynWH7803_0776(thrS)
            CYA: CYA_2433(thrS)
            CYB: CYB_1492(thrS)
            TEL: tll2202(thrS)
            GVI: glr2886(thrS)
            ANA: all4723(thrS) alr0335(thrS)
            AVA: Ava_2787 Ava_B0226
            PMA: Pro1064(thrS)
            PMM: PMM0597(thrS)
            PMT: PMT0424(thrS)
            PMN: PMN2A_0033
            PMI: PMT9312_0597
            PMB: A9601_06531(thrS)
            PMC: P9515_06621(thrS)
            PMF: P9303_18621(thrS)
            PMG: P9301_06231(thrS)
            PMH: P9215_06791(thrS)
            PME: NATL1_06531(thrS)
            TER: Tery_1457
            BTH: BT_0422
            BFR: BF1687
            BFS: BF1694(thrS) BF4152
            PGI: PG0992(thrS)
            SRU: SRU_2802(thrS)
            CHU: CHU_1643(thrS)
            GFO: GFO_0605(thrS)
            FPS: FP0895(thrS)
            CTE: CT2126(thrS)
            CCH: Cag_1715
            PLT: Plut_0123
            DET: DET0753(thrS)
            DEH: cbdb_A726(thrS)
            DRA: DR_2081
            DGE: Dgeo_1507
            TTH: TTC1516
            TTJ: TTHA1875
            AAE: aq_1667(thrS)
            TMA: TM0740
            TME: Tmel_1327
            MJA: MJ1197(thrS)
            MMP: MMP0414(thrS)
            MAC: MA2896(thrS)
            MBA: Mbar_A2945
            MMA: MM_3304
            MBU: Mbur_1324
            MHU: Mhun_1007
            MST: Msp_1573(thrS)
            MSI: Msm_1214
            MKA: MK0544(thrS)
            HAL: VNG1835G(thrS)
            HMA: rrnAC3462(thrS)
            HWA: HQ2579A(thrS)
            NPH: NP2410A(thrS)
            TAC: Ta0330
            TVO: TVN1282
            PTO: PTO0594
            PHO: PH0699
            PAB: PAB1490(thrS)
            PFU: PF1351
            TKO: TK1170
            RCI: RCIX1693(thrS)
            APE: APE_0117.1 APE_0809.1
            HBU: Hbut_0966
            SSO: SSO2486(thrS)
            STO: ST0966
            SAI: Saci_1261
            PAI: PAE1748
            NEQ: NEQ177
STRUCTURES  PDB: 1EVK  1EVL  1FYF  1KOG  1NYQ  1NYR  1QF6  1TJE  1TKE  1TKG  
                 1TKY  1WWT  1Y2Q  2HKZ  2HL0  2HL1  2HL2  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.3
            ExPASy - ENZYME nomenclature database: 6.1.1.3
            ExplorEnz - The Enzyme Database: 6.1.1.3
            ERGO genome analysis and discovery system: 6.1.1.3
            BRENDA, the Enzyme Database: 6.1.1.3
            CAS: 9023-46-5
///
ENTRY       EC 6.1.1.4                  Enzyme
NAME        leucine---tRNA ligase;
            leucyl-tRNA synthetase;
            leucyl-transfer ribonucleate synthetase;
            leucyl-transfer RNA synthetase;
            leucyl-transfer ribonucleic acid synthetase;
            leucine-tRNA synthetase;
            leucine translase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-leucine:tRNALeu ligase (AMP-forming)
REACTION    ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu
            [RN:R03657]
ALL_REAC    R03657
SUBSTRATE   ATP [CPD:C00002];
            L-leucine [CPD:C00123];
            tRNA(Leu) [CPD:C01645]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-leucyl-tRNA(Leu) [CPD:C02047]
REFERENCE   1  [PMID:13792726]
  AUTHORS   ALLEN EH, GLASSMAN E, SCHWEET RS.
  TITLE     Incorporation of amino acids into ribonucleic acid. I. The role of
            activating enzymes.
  JOURNAL   J. Biol. Chem. 235 (1960) 1061-7.
REFERENCE   2
  AUTHORS   Berg, P., Bergmann, F.H., Ofengand, E.J. and Dieckmann, M.
  TITLE     The enzymic synthesis of amino acyl derivatives of ribonucleic acid.
            I. The mechanism of leucyl-, valyl-, isoleucyl- and methionyl
            ribonucleic acid formation.
  JOURNAL   J. Biol. Chem. 236 (1961) 1726-1734.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Bergmann, F.H., Berg, P. and Dieckmann, M.
  TITLE     The enzymic synthesis of amino acyl derivatives of ribonucleic acid.
            II. The preparation of leucyl-, valyl-, isoleucyl- and methionyl
            ribonucleic acid synthetases from Escherichia coli.
  JOURNAL   J. Biol. Chem. 236 (1961) 1735-1740.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00290  Valine, leucine and isoleucine biosynthesis
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01869  leucyl-tRNA synthetase
GENES       HSA: 23395(LARS2) 51520(LARS)
            PTR: 462167(LARS)
            MMU: 102436(Lars2)
            RNO: 363172(Lars2_predicted)
            CFA: 476652(LARS2) 478051(LARS)
            GGA: 416347(LARS) 420702(LARS2)
            XLA: 443989(MGC80460) 447217(MGC82093)
            SPU: 592856(LOC592856)
            DME: Dmel_CG33123 Dmel_CG7479(Aats-leu)
            CEL: R74.1(lrs-1)
            ATH: AT4G04350(EMB2369)
            OSA: 4326033 4338190 4346920
            CME: CMP205C CMQ336C
            SCE: YLR382C(NAM2) YPL160W(CDC60)
            AGO: AGOS_AAL088W AGOS_AER043C
            PIC: PICST_56543(NAM2) PICST_77997(CDC60)
            CGR: CAGL0H05049g CAGL0J03652g
            SPO: SPAC26F1.13c SPAC4G8.09
            ANI: AN3702.2 AN6526.2
            AFM: AFUA_6G04910 AFUA_6G12630
            AOR: AO090003000376 AO090701000047
            CNE: CNM01290
            UMA: UM05108.1
            ECU: ECU06_0280
            DDI: DDB_0231251(mleuS) DDB_0231253(leuS)
            PFA: PF08_0011 PFF1095w
            CHO: Chro.50330 Chro.50331
            TAN: TA04430 TA10995
            TPV: TP03_0416 TP04_0592
            TET: TTHERM_00532220 TTHERM_00670340
            TBR: Tb11.02.1210
            TCR: 511049.40
            LMA: LmjF13.1100
            EHI: 338.t00006
            ECO: b0642(leuS)
            ECJ: JW0637(leuS)
            ECE: Z0789(leuS)
            ECS: ECs0680
            ECC: c0733(leuS)
            ECI: UTI89_C0645(leuS)
            ECP: ECP_0672
            ECV: APECO1_14132(leuS)
            ECW: EcE24377A_0668(leuS)
            ECX: EcHS_A0694(leuS)
            STY: STY0699(leuS)
            STT: t2219(leuS)
            SPT: SPA2086(leuS)
            SEC: SC0678(leuS)
            STM: STM0648(leuS)
            YPE: YPO2610(leuS)
            YPK: y1184(leuS)
            YPM: YP_1103(leuS)
            YPA: YPA_2487
            YPN: YPN_1095
            YPP: YPDSF_2643
            YPS: YPTB1103(leuS)
            YPI: YpsIP31758_2926(leuS)
            SFL: SF0639(leuS)
            SFX: S0661(leuS)
            SFV: SFV_0684(leuS)
            SSN: SSON_0596(leuS)
            SBO: SBO_0506(leuS)
            SDY: SDY_0564(leuS)
            ECA: ECA1309(leuS)
            PLU: plu1303(leuS)
            BUC: BU444(leuS)
            BAS: BUsg429(leuS)
            BAB: bbp395(leuS)
            BCC: BCc_274(leuS)
            WBR: WGLp168(leuS)
            SGL: SG0803
            BFL: Bfl313(leuS)
            BPN: BPEN_321(leuS)
            HIN: HI0921(leuS)
            HIT: NTHI1090(leuS)
            HIP: CGSHiEE_07435(leuS)
            HDU: HD1132(leuS)
            HSO: HS_1557(leuS)
            PMU: PM1214(leuS)
            MSU: MS0338(leuS)
            APL: APL_0872(leuS)
            XFA: XF2176
            XFT: PD1230(leuS)
            XCC: XCC2620(leuS)
            XCB: XC_1497
            XCV: XCV2938(leuS)
            XAC: XAC2781(leuS)
            XOO: XOO3329(leuS)
            XOM: XOO_3142(XOO3142)
            VCH: VC0956
            VCO: VC0395_A0478(leuS)
            VVU: VV1_0272
            VVY: VV0911
            VPA: VP0727
            VFI: VF0753(leuS)
            PPR: PBPRA2885
            PAE: PA3987(leuS)
            PAU: PA14_12230(leuS)
            PAP: PSPA7_1121(leuS)
            PPU: PP_4794(leuS)
            PST: PSPTO_4812(leuS)
            PSB: Psyr_4352
            PSP: PSPPH_4394(leuS)
            PFL: PFL_5439(leuS)
            PFO: Pfl_4957
            PEN: PSEEN4813(leuS)
            PMY: Pmen_3786
            PAR: Psyc_0576(leuS)
            PCR: Pcryo_0566
            ACI: ACIAD3106(leuS)
            SON: SO_1174(leuS)
            SDN: Sden_0797
            SFR: Sfri_0705
            SAZ: Sama_2582
            SHE: Shewmr4_0997
            SHM: Shewmr7_1062
            SHN: Shewana3_1001
            SHW: Sputw3181_1040
            ILO: IL0947(leuS)
            CPS: CPS_1722(leuS)
            PHA: PSHAa1031(leuS)
            PAT: Patl_1566
            SDE: Sde_3308
            PIN: Ping_1191
            MAQ: Maqu_2744
            CBU: CBU_0559(leuS)
            CBD: COXBU7E912_1506(leuS)
            LPN: lpg1348(leuS)
            LPF: lpl1301(leuS)
            LPP: lpp1302(leuS)
            MCA: MCA1453(leuS)
            FTU: FTT0990(leuS)
            FTF: FTF0990(leuS)
            FTW: FTW_0897(leuS)
            FTL: FTL_1212
            FTH: FTH_1186(leuS)
            FTA: FTA_1281(leuS)
            FTN: FTN_0870(leuS)
            TCX: Tcr_0479
            NOC: Noc_2665
            AEH: Mlg_0400
            HHA: Hhal_2145
            HCH: HCH_05355(leuS)
            CSA: Csal_2344
            ABO: ABO_1947(leuS)
            AHA: AHA_3247(leuS)
            DNO: DNO_0246(leuS)
            BCI: BCI_0232(leuS)
            CRP: CRP_098
            RMA: Rmag_0005
            NME: NMB1897
            NMA: NMA0559(leuS)
            NMC: NMC0326(leuS)
            NGO: NGO0006
            CVI: CV_0505(leuS)
            RSO: RSc2744(leuS)
            REU: Reut_A2834
            REH: H16_A3139(leuS)
            RME: Rmet_2973
            BMA: BMA2453(leuS)
            BMV: BMASAVP1_A0370(leuS)
            BML: BMA10299_A1229(leuS)
            BMN: BMA10247_2640(leuS) BMA10247_A1744
            BXE: Bxe_A0576
            BUR: Bcep18194_A3740(leuS)
            BCN: Bcen_0171
            BCH: Bcen2424_0654
            BAM: Bamb_0549
            BPS: BPSL2938(leuS) BPSS0820
            BPM: BURPS1710b_3451(leuS) BURPS1710b_A2411(leuS)
            BPL: BURPS1106A_3450(leuS)
            BPD: BURPS668_3415(leuS)
            BTE: BTH_I1211(leuS)
            BPE: BP2044(leuS)
            BPA: BPP1731(leuS)
            BBR: BB3377(leuS)
            RFR: Rfer_0758
            POL: Bpro_4605
            MPT: Mpe_A0218
            HAR: HEAR2661(leuS)
            MMS: mma_2896(leuS)
            NEU: NE1139(leuS)
            NET: Neut_1429
            NMU: Nmul_A0511
            EBA: ebA4386(leuS)
            DAR: Daro_0544
            TBD: Tbd_2445
            MFA: Mfla_2155
            HPY: HP1547(leuS)
            HPJ: jhp1452(leuS)
            HPA: HPAG1_1496
            HHE: HH0465(leuS)
            HAC: Hac_0293(leuS)
            WSU: WS1245(leuS)
            TDN: Tmden_1572
            CJE: Cj1091c(leuS)
            CJR: CJE1234(leuS)
            CJJ: CJJ81176_1109(leuS)
            CJU: C8J_1032(leuS)
            CJD: JJD26997_0632(leuS)
            CFF: CFF8240_0731(leuS)
            CCV: CCV52592_0710(leuS)
            CHA: CHAB381_0473(leuS)
            CCO: CCC13826_0074(leuS)
            ABU: Abu_0402(leuS)
            NIS: NIS_1464(leuS)
            SUN: SUN_2044(leuS)
            GSU: GSU2209(leuS)
            GME: Gmet_2300
            PCA: Pcar_1413
            DVU: DVU1196(leuS)
            DDE: Dde_2439
            LIP: LI0152(leuS)
            BBA: Bd0365
            DPS: DP2600
            ADE: Adeh_2727
            MXA: MXAN_4051(leuS) MXAN_4745(leuS)
            SAT: SYN_02374
            SFU: Sfum_2084
            RPR: RP421(leuS)
            RTY: RT0407(leuS)
            RCO: RC0585(leuS)
            RFE: RF_0651(leuS)
            RBE: RBE_0311(leuS)
            RAK: A1C_03160(leuS)
            RRI: A1G_03300(leuS)
            OTS: OTBS_0468(leuS)
            WOL: WD0060(leuS)
            WBM: Wbm0605
            AMA: AM446(leuS)
            APH: APH_0534(leuS)
            ERU: Erum3010(leuS)
            ERW: ERWE_CDS_03070(leuS)
            ERG: ERGA_CDS_03010(leuS)
            ECN: Ecaj_0282
            ECH: ECH_0794(leuS)
            NSE: NSE_0506(leuS)
            PUB: SAR11_0357(leuS)
            MLO: mll4077
            MES: Meso_3209
            SME: SMc02804(leuS)
            ATU: Atu2748(leuS)
            ATC: AGR_C_4985
            RET: RHE_CH04116(leuS)
            RLE: RL2798(leuS) RL4732(leuS)
            BME: BMEI0242(leuS)
            BMF: BAB1_1815
            BMS: BR1807(leuS)
            BMB: BruAb1_1787(leuS)
            BOV: BOV_1740(leuS)
            BJA: blr0627(leuS)
            BRA: BRADO0189(leuS)
            BBT: BBta_0171(leuS)
            RPA: RPA0287(leuS)
            RPB: RPB_0385
            RPC: RPC_0284
            RPD: RPD_0436
            RPE: RPE_0390
            NWI: Nwi_0091(leuS)
            NHA: Nham_0098
            BHE: BH15390(leuS)
            BQU: BQ12310(leuS)
            BBK: BARBAKC583_0104(leuS)
            CCR: CC_3749
            SIL: SPO3432(leuS)
            SIT: TM1040_0045
            RSP: RSP_0840(leuS)
            JAN: Jann_0411
            RDE: RD1_0049(leuS)
            MMR: Mmar10_2957
            HNE: HNE_3557(leuS)
            ZMO: ZMO1435(leuS)
            NAR: Saro_3215
            SAL: Sala_3020
            ELI: ELI_09385
            GOX: GOX0410(leuS)
            GBE: GbCGDNIH1_0005
            RRU: Rru_A3631
            MAG: amb0027
            MGM: Mmc1_0432
            ABA: Acid345_1328
            BSU: BG10676(leuS)
            BHA: BH3281(leuS)
            BAN: BA4991(leuS)
            BAR: GBAA4991(leuS)
            BAA: BA_5411
            BAT: BAS4637
            BCE: BC4737(leuS)
            BCA: BCE_4882(leuS)
            BCZ: BCZK4490(leuS)
            BTK: BT9727_4472(leuS)
            BTL: BALH_4313(leuS)
            BLI: BL00016(leuS)
            BLD: BLi03175(leuS)
            BCL: ABC2871(leuS)
            BAY: RBAM_027250(leuS)
            BPU: BPUM_2669(leuS)
            OIH: OB2307(leuS)
            GKA: GK2842(leuS)
            GTN: GTNG_2742
            SAU: SA1579(leuS)
            SAV: SAV1760(leuS)
            SAM: MW1701(leuS)
            SAR: SAR1843(leuS)
            SAS: SAS1684(leuS)
            SAC: SACOL1808(leuS)
            SAB: SAB1618c(leuS)
            SAA: SAUSA300_1704(leuS)
            SAO: SAOUHSC_01875
            SAJ: SaurJH9_1813
            SEP: SE1431
            SER: SERP1318(leuS)
            SHA: SH1163(leuS)
            SSP: SSP1006
            LMO: lmo1660(leuS)
            LMF: LMOf2365_1684(leuS)
            LIN: lin1769(leuS)
            LWE: lwe1679(leuS)
            LLA: L0352(leuS)
            LLC: LACR_0875
            LLM: llmg_1741(leuS)
            SPY: SPy_0173(leuS)
            SPZ: M5005_Spy_0147(leuS)
            SPM: spyM18_0171(leuS)
            SPG: SpyM3_0134(leuS)
            SPS: SPs0137
            SPH: MGAS10270_Spy0149(leuS)
            SPI: MGAS10750_Spy0153(leuS)
            SPJ: MGAS2096_Spy0154(leuS)
            SPK: MGAS9429_Spy0149(leuS)
            SPF: SpyM50141(leuS)
            SPA: M6_Spy0193(leuS)
            SPB: M28_Spy0145(leuS)
            SPN: SP_0254
            SPR: spr0235(leuS)
            SPD: SPD_0238(leuS)
            SAG: SAG2057(leuS)
            SAN: gbs2012(leuS)
            SAK: SAK_1995(leuS)
            SMU: SMU.1943(leuS)
            STC: str0220(leuS)
            STL: stu0220(leuS)
            STE: STER_0268
            SSA: SSA_0289(leuS)
            SSU: SSU05_2081
            SSV: SSU98_2084
            SGO: SGO_1784(leuS)
            LPL: lp_1316(leuS)
            LJO: LJ0680
            LAC: LBA1617(leuS)
            LSA: LSA1436(leuS)
            LSL: LSL_0442(leuS)
            LDB: Ldb1570(leuS)
            LBU: LBUL_1451
            LBR: LVIS_1062
            LCA: LSEI_0883
            LGA: LGAS_0459
            LRE: Lreu_1295
            PPE: PEPE_0645
            EFA: EF0801(leuS)
            OOE: OEOE_0839
            LME: LEUM_0635
            STH: STH444(leuS)
            CAC: CAC0646(leuS)
            CPE: CPE0670(leuS)
            CPF: CPF_0657(leuS)
            CPR: CPR_0645(leuS)
            CTC: CTC00337(leuS)
            CNO: NT01CX_1372(leuS)
            CDF: CD2521(leuS)
            CBO: CBO0186(leuS)
            CBA: CLB_0226(leuS)
            CBH: CLC_0240(leuS)
            CBF: CLI_0249(leuS)
            CKL: CKL_3605(leuS)
            CHY: CHY_0393(leuS)
            DSY: DSY3158
            SWO: Swol_1599
            TTE: TTE0324(leuS)
            MTA: Moth_0568
            MGE: MG_266(leuS)
            MPN: MPN384(leuS)
            MPU: MYPU_0930(leuS)
            MPE: MYPE3890(leuS)
            MGA: MGA_0087(leuS)
            MMY: MSC_0709(leuS)
            MMO: MMOB5390(leuS)
            MHY: mhp667(leuS)
            MHJ: MHJ_0647(leuS)
            MHP: MHP7448_0647(leuS)
            MSY: MS53_0311(leuS)
            MCP: MCAP_0659(leuS)
            UUR: UU371(leuS)
            POY: PAM738(leuS)
            AYW: AYWB_656(leuS)
            MFL: Mfl490
            MTU: Rv0041(leuS)
            MTC: MT0047(leuS)
            MBO: Mb0042(leuS)
            MBB: BCG_0072(leuS)
            MLE: ML0032(leuS)
            MPA: MAP0048(leuS)
            MAV: MAV_0055(leuS)
            MSM: MSMEG_6917(leuS)
            MUL: MUL_0056(leuS)
            MMC: Mmcs_5389
            CGL: NCgl2915(leuS)
            CGB: cg3346(leuS)
            CEF: CE2848
            CDI: DIP2320(leuS)
            CJK: jk2075(leuS)
            NFA: nfa55240(leuS)
            RHA: RHA1_ro03622(leuS)
            SCO: SCO2571(leuS)
            SMA: SAV5488(leuS)
            TWH: TWT385(leuS)
            TWS: TW385(leuS)
            LXX: Lxx12370(leuS)
            AAU: AAur_2246(leuS)
            PAC: PPA0893
            TFU: Tfu_2156
            FRA: Francci3_3901
            FAL: FRAAL6210(leuS)
            ACE: Acel_0771
            SEN: SACE_7373(leuS)
            BLO: BL1450(leuS)
            BAD: BAD_0864(leuS)
            RXY: Rxyl_3202
            FNU: FN1517
            RBA: RB8919(lueS)
            CTR: CT209(leuS)
            CTA: CTA_0229(leuS)
            CMU: TC0481
            CPN: CPn0153(leuS)
            CPA: CP0618
            CPJ: CPj0153(leuS)
            CPT: CpB0154
            CCA: CCA00612(leuS)
            CAB: CAB585(leuS)
            CFE: CF0391(leuS)
            PCU: pc1047(leuS)
            BGA: BG0254(leuS)
            BAF: BAPKO_0261(leuS)
            TPA: TP0586
            TDE: TDE2339(leuS)
            LIL: LA3714(leuS)
            LIC: LIC10517(leuS)
            LBJ: LBJ_2541(leuS)
            LBL: LBL_0571(leuS)
            SYN: sll1074(leuS)
            SYW: SYNW1255(leuS)
            SYC: syc2174_d(leuS)
            SYF: Synpcc7942_1920
            SYD: Syncc9605_1380
            SYE: Syncc9902_1106
            SYG: sync_1375(leuS)
            SYR: SynRCC307_1188(leuS)
            SYX: SynWH7803_1260(leuS)
            CYA: CYA_1256(leuS)
            CYB: CYB_2881(leuS)
            TEL: tll2098(leuS)
            GVI: gll4081(leuS)
            ANA: alr3283(leuS)
            AVA: Ava_4936(leuS)
            PMA: Pro0947(leuS)
            PMM: PMM0889(leuS)
            PMT: PMT0715(leuS)
            PMN: PMN2A_0321
            PMI: PMT9312_0911
            PMB: A9601_09721(leuS)
            PMC: P9515_09711(leuS)
            PMF: P9303_15061(leuS)
            PMG: P9301_09701(leuS)
            PMH: P9215_10031(leuS)
            PME: NATL1_09941(leuS)
            TER: Tery_1704
            BTH: BT_3126
            BFR: BF4586
            BFS: BF4372(leuS)
            PGI: PG0796(leuS)
            SRU: SRU_0933(leuS)
            CHU: CHU_1287(leuS)
            GFO: GFO_3032(leuS)
            FPS: FP2363(leuS)
            CTE: CT1650(leuS)
            CCH: Cag_1688
            PLT: Plut_1636
            DET: DET0194(leuS)
            DEH: cbdb_A202(leuS)
            DRA: DR_2174
            DGE: Dgeo_0567
            TTH: TTC1825
            TTJ: TTHA0161
            AAE: aq_1770(leuS') aq_351(leuS)
            TMA: TM0168
            MJA: MJ0633(leuS)
            MMP: MMP0697(leuS)
            MAC: MA1611(leuS)
            MBA: Mbar_A2048
            MMA: MM_0283(leuS)
            MBU: Mbur_1356
            MHU: Mhun_2923
            MST: Msp_0171(leuS)
            MSI: Msm_1172
            MKA: MK1364(leuS)
            HAL: VNG2223G(leuS)
            HMA: rrnAC2650(leuS1) rrnAC2947(leuS2)
            HWA: HQ2317A(leuS)
            NPH: NP0452A(leuS)
            TAC: Ta0777
            TVO: TVN0761
            PTO: PTO1191(leuS)
            PHO: PH0965
            PAB: PAB1782(leuS)
            PFU: PF0890
            TKO: TK1461
            RCI: RCIX858(leuS)
            APE: APE_1015
            HBU: Hbut_1241
            SSO: SSO0504(leuS) SSO0589(leuS)
            STO: ST0625 ST1455
            SAI: Saci_0373(leuS) Saci_1572(leuS)
            PAI: PAE1107
            NEQ: NEQ239
STRUCTURES  PDB: 1WKB  1WZ2  2AJG  2AJH  2AJI  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.4
            ExPASy - ENZYME nomenclature database: 6.1.1.4
            ExplorEnz - The Enzyme Database: 6.1.1.4
            ERGO genome analysis and discovery system: 6.1.1.4
            BRENDA, the Enzyme Database: 6.1.1.4
            CAS: 9031-15-6
///
ENTRY       EC 6.1.1.5                  Enzyme
NAME        isoleucine---tRNA ligase;
            isoleucyl-tRNA synthetase;
            isoleucyl-transfer ribonucleate synthetase;
            isoleucyl-transfer RNA synthetase;
            isoleucine-transfer RNA ligase;
            isoleucine-tRNA synthetase;
            isoleucine translase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-isoleucine:tRNAIle ligase (AMP-forming)
REACTION    ATP + L-isoleucine + tRNAIle = AMP + diphosphate +
            L-isoleucyl-tRNAIle [RN:R03656]
ALL_REAC    R03656
SUBSTRATE   ATP [CPD:C00002];
            L-isoleucine [CPD:C00407];
            tRNA(Ile) [CPD:C01644]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-isoleucyl-tRNA(Ile) [CPD:C03127]
REFERENCE   1  [PMID:13792726]
  AUTHORS   ALLEN EH, GLASSMAN E, SCHWEET RS.
  TITLE     Incorporation of amino acids into ribonucleic acid. I. The role of
            activating enzymes.
  JOURNAL   J. Biol. Chem. 235 (1960) 1061-7.
REFERENCE   2
  AUTHORS   Berg, P., Bergmann, F.H., Ofengand, E.J. and Dieckmann, M.
  TITLE     The enzymic synthesis of amino acyl derivatives of ribonucleic acid.
            I. The mechanism of leucyl-, valyl-, isoleucyl- and methionyl
            ribonucleic acid formation.
  JOURNAL   J. Biol. Chem. 236 (1961) 1726-1734.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Bergmann, F.H., Berg, P. and Dieckmann, M.
  TITLE     The enzymic synthesis of amino acyl derivatives of ribonucleic acid.
            II. The preparation of leucyl-, valyl-, isoleucyl- and methionyl
            ribonucleic acid synthetases from Escherichia coli.
  JOURNAL   J. Biol. Chem. 236 (1961) 1735-1740.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00290  Valine, leucine and isoleucine biosynthesis
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01870  isoleucyl-tRNA synthetase
GENES       HSA: 3376(IARS) 55699(IARS2)
            PTR: 465229(IARS)
            MMU: 105148(Iars) 381314(Iars2)
            GGA: 415957(IARS) 421346(IARS2)
            XLA: 403361(MGC68929)
            SPU: 577472(LOC577472) 579671(LOC579671)
            DME: Dmel_CG11471(Aats-ile) Dmel_CG5414
            CEL: R11A8.6(irs-1)
            ATH: AT4G10320
            OSA: 4330908 4341652
            CME: CME047C CMT280C
            SCE: YBL076C(ILS1) YPL040C(ISM1)
            AGO: AGOS_AER394W AGOS_AGL247C
            PIC: PICST_63933(ISM1) PICST_83229(ILS1)
            CGR: CAGL0G03311g CAGL0L12606g
            SPO: SPBC8D2.06 SPCC18B5.08c
            ANI: AN0705.2 AN3362.2
            AFM: AFUA_1G13710 AFUA_7G01420
            AOR: AO090010000218 AO090012000505
            CNE: CNA02290 CNN01660
            UMA: UM05160.1 UM06494.1
            ECU: ECU11_1100
            DDI: DDB_0231256(mileS) DDB_0231258(ileS)
            PFA: PF13_0179
            CHO: Chro.30434
            TAN: TA12460 TA13750
            TPV: TP02_0310
            TET: TTHERM_00492850
            TBR: Tb10.389.0630 Tb10.6k15.1220
            TCR: 504137.10 509797.40 509805.130
            LMA: LmjF18.1220 LmjF36.5620
            EHI: 20.t00045
            ECO: b0026(ileS)
            ECJ: JW0024(ileS)
            ECE: Z0030(ileS)
            ECS: ECs0029
            ECC: c0030(ileS)
            ECI: UTI89_C0028(ileS)
            ECP: ECP_0024
            ECV: APECO1_1957(ileS)
            ECW: EcE24377A_0026(ileS)
            ECX: EcHS_A0028
            STY: STY0055(ileS)
            STT: t0048(ileS)
            SPT: SPA0047(ileS)
            SEC: SC0040(ileS)
            STM: STM0046(ileS)
            YPE: YPO0475(ileS)
            YPK: y3700(ileS)
            YPM: YP_3705(ileS)
            YPA: YPA_4068
            YPN: YPN_0347
            YPP: YPDSF_3157
            YPS: YPTB0617(ileS)
            YPI: YpsIP31758_3460(ileS)
            YEN: YE0616(b0026)
            SFL: SF0022(ileS)
            SFX: S0025(ileS)
            SFV: SFV_0020(ileS)
            SSN: SSON_0031(ileS)
            SBO: SBO_0025(ileS)
            SDY: SDY_0048(ileS)
            ECA: ECA3876(ileS)
            PLU: plu0591(ileS)
            BUC: BU149(ileS)
            BAS: BUsg142(ileS)
            BAB: bbp139(ileS)
            BCC: BCc_093(ileS)
            WBR: WGLp294(ileS)
            SGL: SG0414
            BFL: Bfl118(ileS)
            BPN: BPEN_122(ileS)
            HIN: HI0962(ileS)
            HIT: NTHI1135(ileS)
            HIP: CGSHiEE_07160(ileS)
            HIQ: CGSHiGG_08385(ileS)
            HDU: HD0272(ileS)
            HSO: HS_0186(ileS)
            PMU: PM1662(ileS)
            MSU: MS1751(ileS)
            APL: APL_0044(ileS)
            XFA: XF2418
            XFT: PD1437(ileS)
            XCC: XCC1155(ileS)
            XCB: XC_3087
            XCV: XCV1290(ileS)
            XAC: XAC1254(ileS)
            XOO: XOO1626(ileS)
            XOM: XOO_1512(XOO1512)
            VCH: VC0682
            VCO: VC0395_A0214(ileS)
            VVU: VV1_0507
            VVY: VV0687
            VPA: VP0534
            VFI: VF0467(ile)
            PPR: PBPRA0591
            PAE: PA4560(ileS)
            PAU: PA14_60370(ileS)
            PAP: PSPA7_5200(ileS)
            PPU: PP_0603(ileS)
            PST: PSPTO_0806(ileS)
            PSB: Psyr_0710
            PSP: PSPPH_0721(ileS)
            PFL: PFL_5321(ileS)
            PFO: Pfl_4852
            PEN: PSEEN4692(ileS)
            PAR: Psyc_0364(ileS)
            PCR: Pcryo_0402
            ACI: ACIAD0022(ileS)
            SON: SO_3532(ileS)
            SDN: Sden_2723
            SFR: Sfri_2890
            SAZ: Sama_0924
            SBL: Sbal_1054
            SLO: Shew_1099
            SHE: Shewmr4_2957
            SHM: Shewmr7_3039
            SHN: Shewana3_3136
            SHW: Sputw3181_3106
            ILO: IL1128(ileS)
            CPS: CPS_1182(ileS)
            PHA: PSHAa0918(ileS)
            PAT: Patl_3178
            SDE: Sde_2566
            PIN: Ping_3271
            MAQ: Maqu_0862
            CBU: CBU_0396(ileS)
            CBD: COXBU7E912_1672(ileS)
            LPN: lpg0937(ileS)
            LPF: lpl0968(ileS)
            LPP: lpp0999(ileS)
            MCA: MCA2253(ileS)
            FTU: FTT0915c(ileS)
            FTF: FTF0915c(ileS)
            FTW: FTW_1264(ileS)
            FTL: FTL_0436
            FTH: FTH_0428(ileS)
            FTA: FTA_0458(ileS)
            FTN: FTN_0441(ileS)
            TCX: Tcr_0495
            NOC: Noc_2277
            AEH: Mlg_0852
            HHA: Hhal_1836
            HCH: HCH_05933(ileS)
            CSA: Csal_0481
            ABO: ABO_0459(ileS)
            AHA: AHA_0682(ileS)
            DNO: DNO_0083(ileS)
            BCI: BCI_0556(ileS)
            CRP: CRP_129
            RMA: Rmag_0340
            VOK: COSY_0005(leuS) COSY_0322(ileS)
            NME: NMB1833
            NMA: NMA0622(ileS)
            NMC: NMC0383(ileS)
            NGO: NGO0069
            CVI: CV_3569(ileS)
            RSO: RSc2458(ileS)
            REU: Reut_A2745
            REH: H16_A3046(ileS)
            RME: Rmet_2885
            BMA: BMA2242(ileS-1) BMAA0963(ileS-2)
            BMV: BMASAVP1_0415(ileS-2) BMASAVP1_A2658(ileS)
            BML: BMA10299_0227(ileS-2) BMA10299_A1033(ileS)
            BMN: BMA10247_2112(ileS) BMA10247_A1373(ileS-2)
            BXE: Bxe_A0807
            BUR: Bcep18194_A5844
            BCN: Bcen_1901
            BCH: Bcen2424_2512
            BAM: Bamb_2559
            BPS: BPSL0906(ileS1) BPSS1315(ileS2)
            BPM: BURPS1710b_1122(ileS) BURPS1710b_A0334(ileS)
            BPL: BURPS1106A_0971(ileS) BURPS1106A_A1783(ileS)
            BPD: BURPS668_0967(ileS) BURPS668_A1869(ileS)
            BTE: BTH_I0770(ileS)
            BPE: BP1753(ileS)
            BPA: BPP1984(ileS)
            BBR: BB2172(ileS)
            RFR: Rfer_1432
            POL: Bpro_3849
            MPT: Mpe_A3046
            HAR: HEAR0845(ileS)
            MMS: mma_0828
            NEU: NE1149(ileS)
            NET: Neut_1439
            NMU: Nmul_A2654
            EBA: ebA4448(ileS)
            AZO: azo1205
            DAR: Daro_3046
            TBD: Tbd_1857
            MFA: Mfla_2208
            HPY: HP1422(ile)
            HPJ: jhp1317(ileS)
            HPA: HPAG1_1348
            HHE: HH1190(ileS)
            HAC: Hac_0108(ileS)
            WSU: WS0176(ileS)
            TDN: Tmden_0780
            CJE: Cj1061c(ileS)
            CJR: CJE1204(ileS)
            CJJ: CJJ81176_1080(ileS)
            CJU: C8J_1002(ileS)
            CJD: JJD26997_0662(ileS)
            CFF: CFF8240_0610(ileS)
            CCV: CCV52592_0977(ileS)
            CHA: CHAB381_0906(ileS)
            CCO: CCC13826_0717
            ABU: Abu_0519(ileS)
            NIS: NIS_1282(ileS)
            SUN: SUN_1796(ileS)
            GSU: GSU3136(ileS)
            GME: Gmet_0351
            PCA: Pcar_2455
            DVU: DVU1927(ileS)
            DDE: Dde_2142
            LIP: LI1051(ileS)
            BBA: Bd2257(IleRS)
            DPS: DP2552
            ADE: Adeh_0012
            MXA: MXAN_0358(ileS) MXAN_6220
            SAT: SYN_01454
            SFU: Sfum_0122
            RPR: RP617
            RTY: RT0606(ileS)
            RCO: RC0953(ileS)
            RFE: RF_0423(ileS)
            RBE: RBE_0602(ileS)
            RAK: A1C_04840(ileS)
            RBO: A1I_03430(ileS)
            RCM: A1E_01690(ileS)
            RRI: A1G_05235(ileS)
            OTS: OTBS_0154(ileS)
            WOL: WD0423(ileS)
            WBM: Wbm0363
            AMA: AM684(ileS)
            APH: APH_0796(ileS)
            ERU: Erum4870(ileS)
            ERW: ERWE_CDS_05090(ileS)
            ERG: ERGA_CDS_05000(ileS)
            ECN: Ecaj_0495
            ECH: ECH_0538(ileS)
            NSE: NSE_0537(ileS)
            PUB: SAR11_0158(ileS)
            MLO: mlr8250
            MES: Meso_0425
            SME: SMc00908(ileS)
            ATU: Atu0686(ileS)
            ATC: AGR_C_1230
            RET: RHE_CH00832(ileS)
            RLE: RL0889(ileS)
            BME: BMEII1043
            BMF: BAB2_0194(ileS)
            BMS: BRA0202(ileS)
            BMB: BruAb2_0197(ileS)
            BOV: BOV_A0181(ileS)
            BJA: blr7481(ileS)
            BRA: BRADO6067(ileS)
            BBT: BBta_1716(ileS)
            RPA: RPA4377(ileS)
            RPB: RPB_4182
            RPC: RPC_1395
            RPD: RPD_4038
            RPE: RPE_1414
            NWI: Nwi_2542
            NHA: Nham_3162
            BHE: BH02580(ileS)
            BQU: BQ02440(ileS)
            BBK: BARBAKC583_1212(ileS)
            CCR: CC_0701
            SIL: SPO3136(ileS)
            SIT: TM1040_2389
            RSP: RSP_0568(ile)
            JAN: Jann_3467
            RDE: RD1_2074(ileS)
            MMR: Mmar10_0613
            HNE: HNE_0849(ileS)
            ZMO: ZMO0323(ileS)
            NAR: Saro_3259
            SAL: Sala_2357
            ELI: ELI_13550
            GOX: GOX1249(ile)
            GBE: GbCGDNIH1_0466
            RRU: Rru_A2966
            MAG: amb0834
            MGM: Mmc1_2147
            ABA: Acid345_1861
            BSU: BG11792(ileS)
            BHA: BH2545(ileS)
            BAN: BA2181(ileS-1) BA4034(ileS-2)
            BAR: GBAA2181(ileS-1) GBAA4034(ileS-2)
            BAA: BA_2677 BA_4505
            BAT: BAS2027 BAS3746
            BCE: BC2164 BC3895
            BCA: BCE_2241(ileS) BCE_3940(ileS)
            BCZ: BCZK1977(ileS) BCZK3654(ileS)
            BTK: BT9727_1995(ileS) BT9727_3637(ileS)
            BTL: BALH_1940(ileS) BALH_3526(ileS)
            BLI: BL02267(ileS)
            BLD: BLi01762(ileS)
            BCL: ABC2342(ileS)
            BAY: RBAM_015260
            BPU: BPUM_1442
            OIH: OB0362 OB1484(ileS)
            GKA: GK1136(ileS)
            SAU: SA1036(ileS)
            SAV: SAV1193(ileS)
            SAM: MW1076(ileS)
            SAR: SAR1169(ileS)
            SAS: SAS1127
            SAC: SACOL1206(ileS)
            SAB: SAB1057(ileS)
            SAA: SAUSA300_1087(ileS) SAUSA300_pUSA0303(ileS)
            SAO: SAOUHSC_01159
            SEP: SE0868
            SER: SERP0758(ileS)
            SHA: SH1722(ileS)
            SSP: SSP1578
            LMO: lmo2019(ileS)
            LMF: LMOf2365_2044(ileS)
            LIN: lin2127(ileS)
            LWE: lwe2039(ileS)
            LLA: L0350(ileS)
            LLC: LACR_2056
            LLM: llmg_2053(ileS)
            SPY: SPy_1513(ileS)
            SPZ: M5005_Spy_1243(ileS)
            SPM: spyM18_1531(ileS)
            SPG: SpyM3_1166(ileS)
            SPS: SPs0696
            SPH: MGAS10270_Spy1259(ileS)
            SPI: MGAS10750_Spy1350(ileS)
            SPJ: MGAS2096_Spy1261(ileS)
            SPK: MGAS9429_Spy1238(ileS)
            SPF: SpyM50609(ileS)
            SPA: M6_Spy1264
            SPB: M28_Spy1182(ileS)
            SPN: SP_1659
            SPR: spr1502(ileS)
            SPD: SPD_1472(ileS)
            SAG: SAG0485(ileS)
            SAN: gbs0532(ileS)
            SAK: SAK_0587(ileS)
            SMU: SMU.558
            STC: str0741(ileS)
            STL: stu0741(ileS)
            SSA: SSA_0661(ileS)
            SGO: SGO_0681(ileS)
            LPL: lp_2187(ileS)
            LJO: LJ0980
            LAC: LBA0817
            LSA: LSA0756(ileS)
            LSL: LSL_1042(ileS)
            LDB: Ldb0748(ileS)
            LBU: LBUL_0681
            LBR: LVIS_1441
            LCA: LSEI_1280
            EFA: EF1003(ileS)
            OOE: OEOE_1139
            STH: STH1231(ileS)
            CAC: CAC3038(ileS)
            CPE: CPE2541(ileS)
            CPF: CPF_2865(ileS)
            CPR: CPR_2550(ileS)
            CTC: CTC00261
            CNO: NT01CX_0646(ileS)
            CBA: CLB_0135(ileS)
            CBH: CLC_0147(ileS)
            CBF: CLI_0154(ileS)
            CKL: CKL_3752(ileS)
            CHY: CHY_0534(ileS)
            DSY: DSY2882
            SWO: Swol_0962
            TTE: TTE1594(ileS)
            MTA: Moth_0863
            MGE: MG_345(ileS)
            MPN: MPN520(ileS)
            MPU: MYPU_6670(ileS)
            MPE: MYPE8820(ileS)
            MGA: MGA_1196(ileS)
            MMY: MSC_0585(ileS)
            MMO: MMOB4070(ileS)
            MHY: mhp033(ileS)
            MHJ: MHJ_0028(ileS)
            MHP: MHP7448_0032(ileS)
            MSY: MS53_0558(ileS)
            MCP: MCAP_0393(ileS)
            UUR: UU410(ileS)
            POY: PAM184(ileS)
            AYW: AYWB_535(ileS)
            MFL: Mfl389
            MTU: Rv1536(ileS)
            MTC: MT1587(ileS)
            MBO: Mb1563(ileS)
            MBB: BCG_1588(ileS)
            MLE: ML1195(ileS)
            MPA: MAP1246(ileS)
            MAV: MAV_3235(ileS)
            MSM: MSMEG_3169(ileS)
            MMC: Mmcs_3100
            CGL: NCgl2068(cgl2148)
            CGB: cg2359(ileS)
            CEF: CE2043
            CDI: DIP1589(ileS)
            CJK: jk0760(ileS)
            NFA: nfa17760(ileS)
            RHA: RHA1_ro01078(ileS)
            SCO: SCO2076(SC4A10.09)
            SMA: SAV6130(ileS)
            TWH: TWT477(ileS)
            TWS: TW287
            LXX: Lxx07970(ileS)
            AAU: AAur_2374(ileS)
            PAC: PPA0216
            TFU: Tfu_1120
            FRA: Francci3_1424
            FAL: FRAAL2207(ileS)
            SEN: SACE_5828(ileS)
            BLO: BL1777(ileS)
            BAD: BAD_1187(ileS)
            RXY: Rxyl_2428
            FNU: FN0067
            RBA: RB7259(ileS)
            CTR: CT019(ileS)
            CTA: CTA_0021(ileS)
            CMU: TC0288
            CPN: CPn0109(ileS)
            CPA: CP0665
            CPJ: CPj0109(ileS)
            CPT: CpB0110
            CCA: CCA00664(ileS)
            CAB: CAB634(ileS)
            CFE: CF0347(ileS)
            PCU: pc0494(ileS)
            BGA: BG0858(ileS)
            BAF: BAPKO_0886(ileS)
            TPA: TP0452
            TDE: TDE2663(ileS)
            LIL: LA1325(ileS)
            LIC: LIC12400(ileS)
            LBJ: LBJ_2270(ileS)
            LBL: LBL_0837(ileS)
            SYN: sll1362(ileS)
            SYW: SYNW0289(ileS)
            SYC: syc1669_d(ileS)
            SYF: Synpcc7942_2437
            SYD: Syncc9605_0284
            SYE: Syncc9902_2060
            SYG: sync_0333(ileS)
            SYR: SynRCC307_2212(ileS)
            SYX: SynWH7803_0335(ileS)
            CYA: CYA_1703(ileS)
            CYB: CYB_1022(ileS)
            TEL: tlr2330(ileS)
            GVI: gll3651(ileS)
            ANA: alr1073(ileS)
            AVA: Ava_3774
            PMA: Pro0268(ileS)
            PMM: PMM0238(ileS)
            PMT: PMT1817(ileS)
            PMN: PMN2A_1605
            PMI: PMT9312_0240
            PMB: A9601_02591(ileS)
            PMC: P9515_02701(ileS)
            PMF: P9303_24331(ileS)
            PMG: P9301_02601(ileS)
            PMH: P9215_02601
            PME: NATL1_03171(ileS)
            BTH: BT_0806
            BFR: BF2275
            BFS: BF2367(ileS)
            PGI: PG1596
            SRU: SRU_0456(ileS)
            CHU: CHU_3676(ileS)
            GFO: GFO_3183(ileS)
            FPS: FP0217(ileS)
            CTE: CT0311(ileS)
            CCH: Cag_0523
            PLT: Plut_0423
            DET: DET1038(ileS)
            DEH: cbdb_A1012(ileS)
            DRA: DR_1335
            DGE: Dgeo_1101
            TTH: TTC0702
            TTJ: TTHA1067
            AAE: aq_305(ileS)
            TMA: TM1361
            MJA: MJ0947(ileS)
            MMP: MMP1474(ileS)
            MAC: MA2431(ileS)
            MBA: Mbar_A3613
            MMA: MM_0508 MM_2967
            MBU: Mbur_0185
            MHU: Mhun_0606
            MTH: MTH1375(ileS)
            MST: Msp_1468(ileS)
            MSI: Msm_1341
            MKA: MK0899(ileS)
            HAL: VNG2190G(ileS)
            HMA: rrnAC2634(ileS)
            HWA: HQ2671A(ileS)
            NPH: NP0610A(ileS)
            TAC: Ta0879
            TVO: TVN0829
            PTO: PTO0411
            PHO: PH1065
            PAB: PAB0616(ileS)
            PFU: PF1096
            TKO: TK1748
            RCI: RCIX379(ileS)
            APE: APE_0374
            HBU: Hbut_1425
            SSO: SSO0722(ileS)
            STO: ST0431
            SAI: Saci_0599(ileS)
            PAI: PAE1617
            NEQ: NEQ230
STRUCTURES  PDB: 1FFY  1JZQ  1JZS  1QU2  1QU3  1UDZ  1UE0  1WK8  1WNY  1WNZ  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.5
            ExPASy - ENZYME nomenclature database: 6.1.1.5
            ExplorEnz - The Enzyme Database: 6.1.1.5
            ERGO genome analysis and discovery system: 6.1.1.5
            BRENDA, the Enzyme Database: 6.1.1.5
            CAS: 9030-96-0
///
ENTRY       EC 6.1.1.6                  Enzyme
NAME        lysine---tRNA ligase;
            lysyl-tRNA synthetase;
            lysyl-transfer ribonucleate synthetase;
            lysyl-transfer RNA synthetase;
            L-lysine-transfer RNA ligase;
            lysine-tRNA synthetase;
            lysine translase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-lysine:tRNALys ligase (AMP-forming)
REACTION    ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
            [RN:R03658]
ALL_REAC    R03658
SUBSTRATE   ATP [CPD:C00002];
            L-lysine [CPD:C00047];
            tRNA(Lys) [CPD:C01646]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-lysyl-tRNA(Lys) [CPD:C01931]
REFERENCE   1  [PMID:13792726]
  AUTHORS   ALLEN EH, GLASSMAN E, SCHWEET RS.
  TITLE     Incorporation of amino acids into ribonucleic acid. I. The role of
            activating enzymes.
  JOURNAL   J. Biol. Chem. 235 (1960) 1061-7.
REFERENCE   2  [PMID:4310598]
  AUTHORS   Chlumecka V, Von Tigerstrom M, D'Obrenan P, Smith CJ.
  TITLE     Purification and properties of lysyl transfer ribonucleic acid
            synthetase from bakers' yeast.
  JOURNAL   J. Biol. Chem. 244 (1969) 5481-8.
  ORGANISM  pig [GN:ssc]
REFERENCE   3  [PMID:4555953]
  AUTHORS   Lagerkvist U, Rymo L, Lindqvist O, Andersson E.
  TITLE     Some properties of crystals of lysine transfer ribonucleic acid
            ligase from yeast.
  JOURNAL   J. Biol. Chem. 247 (1972) 3897-9.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:4284804]
  AUTHORS   Stern R, Mehler AH.
  TITLE     Lysyl-sRNA synthetase from Escherichia coli.
  JOURNAL   Biochem. Z. 342 (1965) 400-9.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00300  Lysine biosynthesis
            PATH: map00970  Aminoacyl-tRNA biosynthesis
            PATH: map05030  Amyotrophic lateral sclerosis (ALS)
ORTHOLOGY   KO: K01871  lysyl-tRNA synthetase
            KO: K04566  lysyl-tRNA synthetase, class I
            KO: K04567  lysyl-tRNA synthetase, class II
            KO: K04568  lysyl-tRNA synthetase, class II
GENES       HSA: 3735(KARS)
            PTR: 454252(KARS)
            MMU: 85305(Kars)
            RNO: 292028(Kars)
            CFA: 479644(KARS)
            BTA: 509624(MGC127504)
            GGA: 415885(RCJMB04_9m1)
            XLA: 379742(kars) 380325(krs-1)
            XTR: 407964(kars)
            DRE: 280647(kars)
            SPU: 588700(LOC588700)
            DME: Dmel_CG12141(Aats-lys)
            CEL: T02G5.9(krs-1)
            ATH: AT3G11710 AT3G13490(OVA5)
            OSA: 4330025 4333345
            CME: CMM274C CMO044C
            SCE: YDR037W(KRS1) YNL073W(MSK1)
            AGO: AGOS_AER362W AGOS_AGR037C
            PIC: PICST_42797(MSK1) PICST_74513(KRS1)
            CAL: CaO19_14041(CaO19.14041) CaO19_6749(CaO19.6749)
            CGR: CAGL0J10230g CAGL0K12012g
            SPO: SPBC17G9.03c SPCC18.08
            ANI: AN1913.2
            AFM: AFUA_1G04460 AFUA_6G07640
            AOR: AO090003000186 AO090003000867
            CNE: CNI03160
            UMA: UM05121.1
            ECU: ECU04_0580
            DDI: DDB_0231263(lysS) DDB_0231264(mlysS)
            PFA: PF13_0262 PF14_0166
            CPV: cgd4_2370
            CHO: Chro.40267
            TAN: TA04275 TA08620
            TPV: TP03_0387 TP04_0470
            TET: TTHERM_00158250 TTHERM_00621450 TTHERM_00691520
                 TTHERM_00852690 TTHERM_01220420 TTHERM_01220430
                 TTHERM_01227810
            TBR: Tb927.6.1510 Tb927.8.1600
            TCR: 503815.20 505807.120 508971.30
            LMA: LmjF15.0230 LmjF30.0130
            EHI: 209.t00002
            ECO: b2890(lysS) b4129(lysU) b4155(yjeA)
            ECJ: JW2858(lysS) JW4090(lysU) JW4116(poxA)
            ECE: Z4228(lysS) Z5732(lysU) Z5763(yjeA)
            ECS: ECs3762 ECs5111 ECs5136
            ECC: c3469(lysS) c5138(lysU) c5243(yjeA)
            ECI: UTI89_C3275(lysS) UTI89_C4726(lysU) UTI89_C4755(yjeA)
            ECP: ECP_0325 ECP_2883 ECP_4373 ECP_4401
            ECV: APECO1_2234(yjeA) APECO1_2324(lysS) APECO1_3637(lysS)
            ECW: EcE24377A_3216(lysS1) EcE24377A_4684(lysS2)
            ECX: EcHS_A3049(lysS2) EcHS_A4370(lysS1)
            STY: STY3196(lysS) STY4704(yjeA)
            STT: t2958(lysS) t4396(yjeA)
            SPT: SPA2908(lysS) SPA4161(yjeA)
            SEC: SC2980(lysS) SC4223(yjeA)
            STM: STM3040(lysS) STM4344(yjeA)
            YPE: YPO0362(poxA) YPO0888(lysS)
            YPK: y0618 y3272(lysS)
            YPM: YP_0517 YP_3584(lysS)
            YPA: YPA_0381 YPA_3922
            YPN: YPN_3087 YPN_3309
            YPP: YPDSF_0628 YPDSF_3613
            YPS: YPTB0414(poxA) YPTB3163(lysS)
            YPI: YpsIP31758_0883(lysS)
            YEN: YE0365(b4155)
            SFL: SF2876(lysS) SF4313(yjeA)
            SFX: S3075(lysS) S4578(yjeA)
            SFV: SFV_2938(lysS) SFV_4314(yjeA)
            SSN: SSON_3043(lysS) SSON_4306(lysU) SSON_4341(yjeA)
            SBO: SBO_3102(lysS) SBO_4301(yjeA)
            SDY: SDY_3192(lysS) SDY_4399(yjeA)
            ECA: ECA0774(lysS) ECA3968(poxA)
            PLU: plu3548(lysS) plu4121(genX)
            BUC: BU437(lysS) BU582(yjeA)
            BAS: BUsg422(lysS)
            BAB: bbp389(lysS) bbp528(yjeA)
            BCC: BCc_270(lysS)
            WBR: WGLp441(lysS)
            SGL: SG0310 SG1989
            ENT: Ent638_0344
            KPN: KPN_04554(yjeA)
            BFL: Bfl262(lysS)
            BPN: BPEN_270(lysS)
            HIN: HI0836(genX) HI1211(lysU)
            HIT: NTHI1003(genX) NTHI1382(lysS)
            HIP: CGSHiEE_05980(lysS) CGSHiEE_07880
            HIQ: CGSHiGG_07700 CGSHiGG_09805(lysS)
            HDU: HD0029(genX) HD1318(lysS)
            HSO: HS_1008(lysS) HS_1276(lysS) HS_1477(lysS)
            PMU: PM0189(lysU_1) PM0202(lysU_2)
            MSU: MS1543(lysU) MS1633
            APL: APL_0809(lysS) APL_1530(poxA)
            XFA: XF1112 XF2555
            XFT: PD0404(lysU) PD1938(lysS)
            XCC: XCC1571(lysS) XCC1853(lysU)
            XCB: XC_2336 XC_2663
            XCV: XCV1669(lysS) XCV1916(lysS)
            XAC: XAC1628(lysS) XAC1876(lysU)
            XOO: XOO2409(lysS) XOO2872(lysU)
            XOM: XOO_2287(XOO2287) XOO_2726(XOO2726)
            VCH: VC0664 VC2655
            VCO: VC0395_A0195(lysU)
            VVU: VV1_0526 VV1_1270
            VVY: VV0669 VV3096
            VPA: VP0513 VP2838
            VFI: VF0453 VF2333
            PPR: PBPRA0570 PBPRA3377
            PAE: PA3700(lysS)
            PAU: PA14_16530(lysS)
            PAP: PSPA7_1438(lysS)
            PPU: PP_1496(lysS)
            PST: PSPTO_1501(lysS)
            PSB: Psyr_1311
            PSP: PSPPH_3873(lysS)
            PFL: PFL_1138(lysS)
            PFO: Pfl_1060
            PEN: PSEEN1255(lysS)
            PAR: Psyc_0273(lysS) Psyc_1054(lysS)
            PCR: Pcryo_0299 Pcryo_1409
            ACI: ACIAD1069(lysS) ACIAD2666
            ACB: A1S_2636
            SON: SO_0992(lysS)
            SDN: Sden_3127
            SFR: Sfri_0583
            SAZ: Sama_2877
            SBL: Sbal_0873
            SLO: Shew_0812
            SHE: Shewmr4_0827
            SHM: Shewmr7_3196
            SHN: Shewana3_3296
            SHW: Sputw3181_0896
            ILO: IL0822(lysU) IL2275
            CPS: CPS_4082(lysS) CPS_4763
            PHA: PSHAa0475 PSHAa0518(lysS)
            PAT: Patl_0442 Patl_1361
            SDE: Sde_1217
            PIN: Ping_3277 Ping_3428
            MAQ: Maqu_2270 Maqu_2781
            CBU: CBU_0430(lysS) CBU_1817
            CBD: COXBU7E912_1642(lysS)
            LPN: lpg0607 lpg1777(lysU)
            LPF: lpl0642 lpl1741(lysS)
            LPP: lpp0658 lpp1741(lysS)
            MCA: MCA0301(lysS) MCA1319
            FTU: FTT0192(lysU) FTT0476c(poxA)
            FTF: FTF0192(lysU) FTF0476c(poxA)
            FTW: FTW_1899(lysS)
            FTL: FTL_1587 FTL_1903
            FTH: FTH_1533(poxA) FTH_1825(lysU)
            FTA: FTA_2010(lysS)
            FTN: FTN_0168(lysU) FTN_0567
            TCX: Tcr_0726 Tcr_1740
            NOC: Noc_1618 Noc_2625
            AEH: Mlg_0685 Mlg_1804
            HHA: Hhal_0048 Hhal_1978
            HCH: HCH_01783(lysS) HCH_05398
            CSA: Csal_2530 Csal_2997
            ABO: ABO_1648(lysS) ABO_2447(lysRS)
            AHA: AHA_3369(lysS)
            DNO: DNO_0604 DNO_0938(lysS)
            BCI: BCI_0152(lysS) BCI_0588
            CRP: CRP_118
            RMA: Rmag_0148 Rmag_0594
            VOK: COSY_0152(genX) COSY_0549(lysS)
            NME: NMB1425
            NMA: NMA1638(lysS)
            NMC: NMC1361(lysS)
            NGO: NGO1454(lysRS)
            CVI: CV_1060(lysS)
            RSO: RSc1028(lysS)
            REU: Reut_A1070
            REH: H16_A1167(lysU)
            RME: Rmet_1034
            BMA: BMA1700(lysS)
            BMV: BMASAVP1_A2207(lysS)
            BML: BMA10299_A3111(lysS)
            BMN: BMA10247_1480(lysS)
            BXE: Bxe_A1561
            BUR: Bcep18194_A5424
            BCN: Bcen_5959
            BCH: Bcen2424_2118
            BAM: Bamb_2155
            BPS: BPSL2281(lysS)
            BPM: BURPS1710b_2723(lysS)
            BPL: BURPS1106A_2645(lysS)
            BPD: BURPS668_2591(lysS)
            BTE: BTH_I1883(lysS)
            PNU: Pnuc_1472
            BPE: BP1102(lysS)
            BPA: BPP2045(lysS)
            BBR: BB2293(lysS)
            RFR: Rfer_1784
            POL: Bpro_3620
            PNA: Pnap_3050
            AAV: Aave_1204
            AJS: Ajs_3250
            VEI: Veis_3052
            MPT: Mpe_A0600
            HAR: HEAR2230(lysS)
            MMS: mma_1260(lysS)
            NEU: NE2355(lysS) NE2361
            NET: Neut_0872
            NMU: Nmul_A2275
            EBA: ebA6841(lysU)
            AZO: azo1487(lysS)
            DAR: Daro_2848
            TBD: Tbd_0893
            MFA: Mfla_0797
            HPY: HP0182(lysS)
            HPJ: jhp0170(lysS)
            HPA: HPAG1_0179
            HHE: HH1666(lysS)
            HAC: Hac_0368(lysS)
            WSU: WS0084(lysS)
            TDN: Tmden_1273
            CJE: Cj0401(lysS)
            CJR: CJE0450(lysS)
            CJJ: CJJ81176_0424(lysS)
            CJU: C8J_0376(lysS)
            CJD: JJD26997_1556(lysS)
            CFF: CFF8240_1142(lysS)
            CCV: CCV52592_1349(lysS)
            CHA: CHAB381_1646(lysS)
            CCO: CCC13826_0225(lysS) CCC13826_1691
            ABU: Abu_0654(lysS)
            NIS: NIS_1177
            SUN: SUN_0482
            GSU: GSU1753 GSU2271(lysS)
            GME: Gmet_1839 Gmet_2360
            PCA: Pcar_1248 Pcar_2490
            PPD: Ppro_1764
            DVU: DVU2376(lysS)
            DDE: Dde_1365
            LIP: LI1027(lysU)
            BBA: Bd0702 Bd2338(lysS)
            DPS: DP0846 DP1629
            ADE: Adeh_1078 Adeh_3726
            AFW: Anae109_1117
            MXA: MXAN_4731(lysS) MXAN_5579
            SAT: SYN_00184 SYN_00924
            SFU: Sfum_0076 Sfum_3742
            RPR: RP371(lysS)
            RTY: RT0359(lysS)
            RCO: RC0505(lysS)
            RFE: RF_0582(lysS)
            RBE: RBE_0871(lysS)
            RAK: A1C_02755(lysK)
            RBO: A1I_02545(lysK)
            RRI: A1G_02865(lysK)
            OTS: OTBS_0142(lysS)
            WOL: WD0860(lysS)
            WBM: Wbm0799
            AMA: AM658(lysS)
            APH: APH_0607(lysS)
            ERU: Erum4220(lysS)
            ERW: ERWE_CDS_04390(lysS)
            ERG: ERGA_CDS_04330(lysS)
            ECN: Ecaj_0413
            ECH: ECH_0626(lysS)
            NSE: NSE_0773(lysS)
            PUB: SAR11_0210(lysS)
            MLO: mll5634 mlr8260
            MES: Meso_0017
            PLA: Plav_0432
            SME: SMc00356(genX) SMc03173(lysS)
            SMD: Smed_3477
            ATU: Atu2554(poxA) Atu4473(lysS)
            ATC: AGR_C_4627 AGR_L_794(lysS)
            RET: RHE_CH03657(lysS) RHE_CH04041(genX)
            RLE: RL4185(lysS) RL4599
            BME: BMEII0500
            BMF: BAB2_0447
            BMS: BRA0790
            BMB: BruAb2_0442
            BOV: BOV_A0741(lysS)
            OAN: Oant_3971
            BJA: blr1133(lysS) blr4387
            BRA: BRADO3587 BRADO6745(lysS)
            BBT: BBta_0790(lysS) BBta_4013
            RPA: RPA2514 RPA4685(lysS)
            RPB: RPB_0888 RPB_2955
            RPC: RPC_0730 RPC_2808
            RPD: RPD_1000 RPD_2505
            RPE: RPE_0736 RPE_2929
            NWI: Nwi_0151 Nwi_1642
            NHA: Nham_0201 Nham_2301
            BHE: BH00240(lysS)
            BQU: BQ00220(lysS)
            BBK: BARBAKC583_1360(lysS)
            XAU: Xaut_2384 Xaut_2530
            CCR: CC_0084 CC_0720
            SIL: SPO0455(lysS)
            SIT: TM1040_2261
            RSP: RSP_0478 RSP_0584
            RSH: Rsph17029_2130 Rsph17029_2237
            RSQ: Rsph17025_0487 Rsph17025_2403
            JAN: Jann_3617
            RDE: RD1_1246(lysS)
            PDE: Pden_1321 Pden_1576 Pden_1654
            MMR: Mmar10_0509
            HNE: HNE_3072(lysS)
            ZMO: ZMO0890(lysS)
            NAR: Saro_2360
            SAL: Sala_0463
            SWI: Swit_3566
            ELI: ELI_02975
            GOX: GOX0232 GOX0233 GOX1905
            GBE: GbCGDNIH1_1088 GbCGDNIH1_2174
            ACR: Acry_0707 Acry_2375
            RRU: Rru_A0503 Rru_A1078
            MAG: amb1283 amb3611
            MGM: Mmc1_0949 Mmc1_1032
            ABA: Acid345_1286
            BSU: BG10144(lysS)
            BHA: BH0098(lysS)
            BAN: BA0076(lysS)
            BAR: GBAA0076(lysS)
            BAA: BA_0666
            BAT: BAS0076
            BCE: BC0084 BC2535
            BCA: BCE_0075(lysS)
            BCZ: BCZK0072(lysS) BCZK2340(lysS)
            BCY: Bcer98_0072
            BTK: BT9727_0072(lysS) BT9727_2375(lysS)
            BTL: BALH_0075(lysS)
            BLI: BL03312(lysS)
            BLD: BLi00097(lysS)
            BCL: ABC0117(lysS)
            BAY: RBAM_000920(lysS)
            BPU: BPUM_0066(lysS)
            OIH: OB0088
            GKA: GK0074
            GTN: GTNG_0074
            SAU: SA0475(lysS)
            SAV: SAV0517(lysS)
            SAM: MW0472(lysS)
            SAR: SAR0518(lysS)
            SAS: SAS0474
            SAC: SACOL0562(lysS)
            SAB: SAB0466(lysS)
            SAA: SAUSA300_0496(lysS)
            SAO: SAOUHSC_00493
            SAJ: SaurJH9_0539
            SAH: SaurJH1_0553
            SEP: SE2266
            SER: SERP0156(lysS)
            SHA: SH2493(lysS)
            SSP: SSP2239
            LMO: lmo0228(lysS)
            LMF: LMOf2365_0240(lysS)
            LIN: lin0260(lysS)
            LWE: lwe0192(lysS)
            LLA: L0347(lysS)
            LLC: LACR_0417
            LLM: llmg_0389(lysS)
            SPY: SPy_0595(lysS)
            SPZ: M5005_Spy_0495(lysS)
            SPM: spyM18_0663(lysS)
            SPG: SpyM3_0420(lysS)
            SPS: SPs1435
            SPH: MGAS10270_Spy0488(lysS)
            SPI: MGAS10750_Spy0514(lysS)
            SPJ: MGAS2096_Spy0506(lysS)
            SPK: MGAS9429_Spy0485(lysS)
            SPF: SpyM51368(lysS)
            SPA: M6_Spy0516
            SPB: M28_Spy0474(lysS)
            SPN: SP_0713
            SPR: spr0626(lysS)
            SPD: SPD_0620(lysS)
            SAG: SAG0750(lysS)
            SAN: gbs0771(lysS)
            SAK: SAK_0876(lysS)
            SMU: SMU.773c
            STC: str0692(lysS)
            STL: stu0692(lysS)
            STE: STER_0733
            SSA: SSA_1529(lysS)
            SSU: SSU05_0519
            SSV: SSU98_0511
            SGO: SGO_0753(lysS)
            LPL: lp_0550(lysS)
            LJO: LJ0287
            LAC: LBA0281
            LSA: LSA1594(lysS)
            LSL: LSL_1351(lysS)
            LDB: Ldb0373(lysS)
            LBU: LBUL_0328
            LBR: LVIS_0071
            LCA: LSEI_2532
            LGA: LGAS_0280
            PPE: PEPE_1542
            EFA: EF0268(lysS)
            OOE: OEOE_0190
            LME: LEUM_0406
            STH: STH208(lysS2) STH525(lysS1)
            CAC: CAC3197(lysS)
            CPE: CPE2465(lysS)
            CPF: CPF_2781(lysS)
            CPR: CPR_2467(lysS)
            CTC: CTC00211
            CNO: NT01CX_1046(lysS)
            CTH: Cthe_2815
            CDF: CD3552(lysS)
            CBO: CBO3518(lysS)
            CBA: CLB_3593(lysS)
            CBH: CLC_3482(lysS)
            CBF: CLI_3727(lysS)
            CKL: CKL_0178(lysS)
            CHY: CHY_2365(lysS)
            DSY: DSY0219
            DRM: Dred_0175
            PTH: PTH_0263(lysU)
            SWO: Swol_0116
            CSC: Csac_0828
            TTE: TTE2372(lysU)
            MTA: Moth_0152
            MGE: MG_136(lysS)
            MPN: MPN277(lysS)
            MPU: MYPU_3900(lysS) MYPU_4020(lysS)
            MPE: MYPE8420(lysS)
            MGA: MGA_0753(lysU)
            MMY: MSC_0069(lysS)
            MMO: MMOB0440(lysS)
            MHY: mhp174(lysS)
            MHJ: MHJ_0203(lysS)
            MHP: MHP7448_0207(lysS)
            MSY: MS53_0611(lysS)
            MCP: MCAP_0836(lysS)
            UUR: UU062(lysS)
            POY: PAM589(lysU)
            AYW: AYWB_128(lysU)
            MFL: Mfl030
            MTU: Rv1640c(lysS) Rv3598c(lysS)
            MTC: MT1678 MT3705(lysS)
            MBO: Mb1667c(lysS) Mb3629c(lysS)
            MBB: BCG_1679c(lysX) BCG_3663c(lysS)
            MLE: ML0233(lysS) ML1393(lysX)
            MPA: MAP0459(lysS) MAP1351c(lysX)
            MAV: MAV_0554(lysS)
            MSM: MSMEG_3796 MSMEG_6094(lysS)
            MVA: Mvan_3330
            MMC: Mmcs_2983 Mmcs_4758
            MKM: Mkms_3027
            MJL: Mjls_2998
            CGL: NCgl2594(lysS)
            CGB: cg2974(lysS)
            CEF: CE2533
            CDI: DIP1987(lysU) DIP2138
            CJK: jk0294(lysS) jk1200(lysX)
            NFA: nfa1030(lysS2) nfa4110(lysS)
            RHA: RHA1_ro03733(lysX) RHA1_ro04420(lysS)
            SCO: SCO3303(SCE15.20c)
            SMA: SAV4749(lysS1) SAV7296(lysS2)
            TWH: TWT062(lysS)
            TWS: TW072(lysS)
            LXX: Lxx21400(lysS)
            AAU: AAur_0164(lysS)
            PAC: PPA0181 PPA1621(lysS)
            TFU: Tfu_2881
            FRA: Francci3_0418
            FAL: FRAAL1791(lysS)
            ACE: Acel_0216
            SEN: SACE_0409(lysS) SACE_4738(lysS)
            BLO: BL1654(lysS)
            BAD: BAD_0376(lysS)
            RXY: Rxyl_2180
            FNU: FN0466
            RBA: RB10883(lysS) RB4877
            CTR: CT781(lysS)
            CTA: CTA_0851(lysS)
            CMU: TC0163
            CPN: CPn0931(lysS)
            CPA: CP0932
            CPJ: CPj0931(lysS)
            CPT: CpB0965
            CCA: CCA00839(lysS)
            CAB: CAB807
            CFE: CF0174(lysS)
            PCU: pc1228(lysS) pc1530(lysS)
            BBU: BB0659
            BGA: BG0682
            BAF: BAPKO_0703
            TPA: TP0644 TP1040
            TDE: TDE2282 TDE2553(lysS)
            LIL: LA1995(lysS1) LB329(lysS2)
            LIC: LIC11913(lysS) LIC20251
            LBJ: LBJ_1523(lysU) LBJ_4242
            LBL: LBL_1747(lysU) LBL_4256
            SYN: slr1550(lysS)
            SYW: SYNW0127(lysS)
            SYC: syc1691_d(lysS)
            SYF: Synpcc7942_2415
            SYD: Syncc9605_0110(lysS)
            SYE: Syncc9902_0154(lysS)
            SYG: sync_0116(lysS)
            SYR: SynRCC307_0114(lysS)
            SYX: SynWH7803_0177(lysS)
            CYA: CYA_0333(lysS)
            CYB: CYB_1514(lysS)
            TEL: tll0212(lysS)
            GVI: gll3356(lysS)
            ANA: all4071(lysS)
            AVA: Ava_3150(lysS)
            PMA: Pro1779(lysU)
            PMM: PMM1618(lysS)
            PMT: PMT0147(lysS)
            PMN: PMN2A_1195
            PMI: PMT9312_1711
            PMB: A9601_18281(lysS)
            PMC: P9515_18071(lysS)
            PMF: P9303_01841(lysS)
            PMG: P9301_18101(lysS)
            PMH: P9215_18921(lysS)
            PME: NATL1_20701(lysS)
            TER: Tery_2366
            BTH: BT_2122
            BFR: BF3810
            BFS: BF3602(lysU)
            PGI: PG1370(lysS)
            SRU: SRU_0905(lysS)
            CHU: CHU_0741(lysU)
            GFO: GFO_2926(lysS)
            FPS: FP1202(lysS)
            CTE: CT1387(lysS)
            CCH: Cag_1176(lysS)
            PLT: Plut_1357(lysS)
            DET: DET0578(lysS) DET0869
            DEH: cbdb_A555(lysS) cbdb_A853
            DEB: DehaBAV1_0551
            DRA: DR_0372
            DGE: Dgeo_0903
            TTH: TTC0679
            TTJ: TTHA1041
            AAE: aq_1202(lysU) aq_763(genX)
            TMA: TM1705
            TPT: Tpet_1001
            MJA: MJ0539(lysS)
            MMP: MMP1318(lysS)
            MMQ: MmarC5_0275
            MMZ: MmarC7_0563
            MAE: Maeo_0215
            MVN: Mevan_0629
            MAC: MA0534(lysK) MA0760(lysS)
            MBA: Mbar_A1507 Mbar_A1667
            MMA: MM_1696 MM_1916
            MBU: Mbur_1865
            MTP: Mthe_0773
            MHU: Mhun_2496
            MTH: MTH1542
            MST: Msp_0249(lysS)
            MSI: Msm_1387
            MKA: MK0986(lysS)
            AFU: AF1216(lysS)
            HAL: VNG2017G(lysS)
            HMA: rrnAC3173(lysS)
            HWA: HQ1097A(lysS)
            NPH: NP2270A(lysS)
            TAC: Ta1163
            TVO: TVN1219
            PTO: PTO0466
            PHO: PH0224
            PAB: PAB0139(lysS)
            PFU: PF0135
            TKO: TK2240
            RCI: RCIX1106(lysS)
            APE: APE_0161.1
            SMR: Smar_0107
            IHO: Igni_0465
            HBU: Hbut_0055
            SSO: SSO0090(lysS)
            STO: ST2083
            SAI: Saci_0067(lysS)
            PAI: PAE1840
            TPE: Tpen_0786
            NEQ: NEQ087
STRUCTURES  PDB: 1BBU  1BBW  1E1O  1E1T  1E22  1E24  1IRX  1KRS  1KRT  1LYL  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.6
            ExPASy - ENZYME nomenclature database: 6.1.1.6
            ExplorEnz - The Enzyme Database: 6.1.1.6
            ERGO genome analysis and discovery system: 6.1.1.6
            BRENDA, the Enzyme Database: 6.1.1.6
            CAS: 9031-26-9
///
ENTRY       EC 6.1.1.7                  Enzyme
NAME        alanine---tRNA ligase;
            alanyl-tRNA synthetase;
            alanyl-transfer ribonucleate synthetase;
            alanyl-transfer RNA synthetase;
            alanyl-transfer ribonucleic acid synthetase;
            alanine-transfer RNA ligase;
            alanine transfer RNA synthetase;
            alanine tRNA synthetase;
            alanine translase;
            alanyl-transfer ribonucleate synthase;
            AlaRS;
            Ala-tRNA synthetase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-alanine:tRNAAla ligase (AMP-forming)
REACTION    ATP + L-alanine + tRNAAla = AMP + diphosphate + L-alanyl-tRNAAla
            [RN:R03038]
ALL_REAC    R03038
SUBSTRATE   ATP [CPD:C00002];
            L-alanine [CPD:C00041];
            tRNA(Ala) [CPD:C01635]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-alanyl-tRNA(Ala) [CPD:C00886]
REFERENCE   1  [PMID:13672960]
  AUTHORS   HOLLEY RW, GOLDSTEIN J.
  TITLE     An alanine-dependent, ribonuclease-inhibited conversion of adenosine
            5'-phosphate to adenosine triphosphate. II. Reconstruction of the
            system from purified components.
  JOURNAL   J. Biol. Chem. 234 (1959) 1765-8.
  ORGANISM  rat [GN:rno]
REFERENCE   2
  AUTHORS   Webster, G.C.
  TITLE     Isolation of an alanine-activating enzyme from pig liver.
  JOURNAL   Biochim. Biophys. Acta 49 (1961) 141-152.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01872  alanyl-tRNA synthetase
GENES       HSA: 16(AARS) 57505(AARS2)
            MMU: 234734(Aars)
            CFA: 479656(AARS)
            GGA: 415668(AARS) 421436(RCJMB04_28n18)
            SPU: 592771(LOC592771)
            DME: Dmel_CG13391(Aats-ala) Dmel_CG4633(Aats-ala-m)
            CEL: F28H1.3(ars-2) W02B12.6(ars-1)
            ATH: AT1G50200(ALATS)
            OSA: 4348211
            CME: CMG111C CMM314C
            SCE: YOR335C(ALA1)
            AGO: AGOS_ADR363C
            PIC: PICST_53118(SYA1) PICST_88206(ALA1)
            CGR: CAGL0E05390g
            SPO: SPAC23C11.09
            ANI: AN9419.2
            AFM: AFUA_8G03880 AFUA_8G07110
            AOR: AO090103000001
            CNE: CNF02520
            UMA: UM05233.1
            ECU: ECU02_1490
            DDI: DDB_0214894(alaS) DDB_0231265(malaS)
            PFA: PF13_0354
            CPV: cgd6_560
            CHO: Chro.60075
            TAN: TA16780
            TPV: TP01_1004
            TET: TTHERM_00221140
            TBR: Tb927.6.700
            TCR: 506863.10 511825.220
            LMA: LmjF22.1540
            EHI: 39.t00004
            ECO: b2697(alaS)
            ECJ: JW2667(alaS)
            ECE: Z3999(alaS)
            ECS: ECs3554
            ECI: UTI89_C3058(alaS)
            ECP: ECP_2657
            ECV: APECO1_3829(alaS)
            ECX: EcHS_A2833
            STY: STY2948(alaS)
            STT: t2728(alaS)
            SPT: SPA2685(alaS)
            SEC: SC2760(alaS)
            STM: STM2827(alaS)
            YPE: YPO3305(alaS)
            YPK: y0883(alaS)
            YPM: YP_0381(alaS)
            YPA: YPA_2840
            YPN: YPN_0789
            YPP: YPDSF_3056
            YPS: YPTB0825(alaS)
            YPI: YpsIP31758_3238(alaS)
            YEN: YE0834(alaS)
            SFL: SF2720(alaS)
            SFX: S2911(alaS)
            SFV: SFV_2808(alaS)
            SSN: SSON_2841(alaS)
            SBO: SBO_2821(alaS)
            SDY: SDY_2893(alaS)
            ECA: ECA3367(alaS)
            PLU: plu1250(alaS)
            BUC: BU403(alaS)
            BAS: BUsg390(alaS)
            BAB: bbp364(alaS)
            BCC: BCc_254(alaS)
            WBR: WGLp234(alaS)
            SGL: SG0538
            ENT: Ent638_3172
            KPN: KPN_03029(alaS)
            SPE: Spro_0843
            BFL: Bfl168(alaS)
            BPN: BPEN_174(alaS)
            HIN: HI0814(alaS)
            HIT: NTHI0978(alaS)
            HIP: CGSHiEE_07990(alaS)
            HDU: HD1429(alaS)
            HSO: HS_1120(alaS)
            PMU: PM1287(alaS)
            MSU: MS0348(alaS)
            APL: APL_0654(alaS)
            ASU: Asuc_0052
            XFA: XF0124
            XFT: PD0094(alaS)
            XCC: XCC1724(alaS)
            XCB: XC_2507
            XCV: XCV1775(alaS)
            XAC: XAC1742(alaS)
            XOO: XOO2939(alaS)
            XOM: XOO_2791(XOO2791)
            VCH: VC0545
            VCO: VC0395_A0072(alaS)
            VVU: VV1_1593
            VVY: VV2803
            VPA: VP2548
            VFI: VF0536
            PPR: PBPRA3067
            PAE: PA0903(alaS)
            PAU: PA14_52600(alaS)
            PAP: PSPA7_4612(alaS)
            PPU: PP_4474(alaS)
            PPF: Pput_1441
            PST: PSPTO_1842(alaS)
            PSB: Psyr_3556(alaS)
            PSP: PSPPH_3512(alaS)
            PFL: PFL_4506(alaS)
            PFO: Pfl_4275
            PEN: PSEEN3875(alaS)
            PMY: Pmen_2903
            PAR: Psyc_1460(alaS)
            PCR: Pcryo_1638
            PRW: PsycPRwf_1611
            ACI: ACIAD1253(alaS)
            ACB: A1S_1176
            SON: SO_3428(alaS)
            SDN: Sden_1213
            SFR: Sfri_1063
            SAZ: Sama_1048
            SBL: Sbal_3115
            SBM: Shew185_3124
            SLO: Shew_1217
            SPC: Sputcn32_2745
            SSE: Ssed_1318
            SPL: Spea_1196
            SHE: Shewmr4_1127
            SHM: Shewmr7_1198
            SHN: Shewana3_1128 Shewana3_3039
            SHW: Sputw3181_1267
            ILO: IL1738(alaS)
            CPS: CPS_1042(alaS)
            PHA: PSHAa0532(alaS)
            PAT: Patl_3015
            SDE: Sde_1299
            PIN: Ping_3380
            MAQ: Maqu_0965
            CBU: CBU_1052(alaS)
            CBD: COXBU7E912_0990(alaS)
            LPN: lpg1799(alaS)
            LPF: lpl1763(alaS)
            LPP: lpp1763(alaS)
            MCA: MCA0389(alaS)
            FTU: FTT1096c(alaS)
            FTF: FTF1096c(alaS)
            FTW: FTW_1402(alaS)
            FTL: FTL_1106
            FTH: FTH_1079(alaS)
            FTA: FTA_1166(alaS)
            FTN: FTN_0778(alaS)
            TCX: Tcr_1590
            NOC: Noc_0926
            AEH: Mlg_1481
            HHA: Hhal_1653
            HCH: HCH_05209(alaS)
            CSA: Csal_0625
            ABO: ABO_1798(alarS)
            MMW: Mmwyl1_3628
            AHA: AHA_3714(alaS)
            DNO: DNO_0286(alaS)
            BCI: BCI_0205(alaS)
            CRP: CRP_109
            RMA: Rmag_0882
            VOK: COSY_0806(alaS)
            NME: NMB1595
            NMA: NMA1788(alaS)
            NMC: NMC1518(alaS)
            NGO: NGO1254
            CVI: CV_1604(alaS)
            RSO: RSc0797(alaS)
            REU: Reut_A0850
            REH: H16_A2769(alaS)
            RME: Rmet_0831
            BMA: BMA0895(alaS) BMAA0961
            BMV: BMASAVP1_A1423(alaS)
            BML: BMA10299_A0455(alaS)
            BMN: BMA10247_0705(alaS)
            BXE: Bxe_A1311 Bxe_B2318
            BVI: Bcep1808_1373
            BUR: Bcep18194_A4553 Bcep18194_A5605
            BCN: Bcen_0927
            BCH: Bcen2424_1409
            BAM: Bamb_1286
            BPS: BPSL2009(alaS) BPSS1317
            BPM: BURPS1710b_1402 BURPS1710b_1815(alaS) BURPS1710b_A0336
            BPL: BURPS1106A_1660(alaS)
            BPD: BURPS668_1637(alaS) BURPS668_A1871(alaS)
            BTE: BTH_I2661(alaS)
            PNU: Pnuc_1719
            BPE: BP1836(alaS)
            BPA: BPP2870(alaS)
            BBR: BB3191(alaS)
            RFR: Rfer_0590
            POL: Bpro_2910
            PNA: Pnap_2628
            AAV: Aave_3035
            AJS: Ajs_1979
            VEI: Veis_1670
            MPT: Mpe_A2323
            HAR: HEAR0616(alaS)
            MMS: mma_0583
            NEU: NE1930(alaS)
            NET: Neut_0791
            NMU: Nmul_A0022
            EBA: ebA1021(alaS)
            AZO: azo2780(alaS)
            DAR: Daro_3303
            TBD: Tbd_0553
            MFA: Mfla_0568
            HPY: HP1241(alaS)
            HPJ: jhp1162(alaS)
            HPA: HPAG1_1183
            HHE: HH0859(alaS)
            HAC: Hac_0121(alaS)
            WSU: WS0324(alaS)
            TDN: Tmden_1898
            CJE: Cj0506(alaS)
            CJR: CJE0613(alaS)
            CJJ: CJJ81176_0534(alaS)
            CJU: C8J_0470(alaS)
            CJD: JJD26997_1429(alaS)
            CFF: CFF8240_1029(alaS)
            CCV: CCV52592_0686(alaS)
            CHA: CHAB381_0986(alaS)
            CCO: CCC13826_0051(alaS)
            ABU: Abu_2092(alaS)
            NIS: NIS_1528(alaS)
            SUN: SUN_0346(alaS)
            GSU: GSU0148(alaS)
            GME: Gmet_0201
            GUR: Gura_0222
            PCA: Pcar_2408
            PPD: Ppro_3176
            DVU: DVU1089(alaS)
            DVL: Dvul_1906
            DDE: Dde_2374
            LIP: LI1181(alaS)
            BBA: Bd0501(alaS)
            DPS: DP0828
            ADE: Adeh_3784
            AFW: Anae109_3904
            MXA: MXAN_5802(alaS)
            SAT: SYN_02026
            SFU: Sfum_2527
            RPR: RP856(alaS)
            RTY: RT0845(alaS)
            RCO: RC1327(alaS)
            RFE: RF_1353(alaS)
            RBE: RBE_0071(alaS)
            RAK: A1C_06625(alaS)
            RCM: A1E_05485(alaS)
            RRI: A1G_07260(alaS)
            OTS: OTBS_0574(alaS)
            WOL: WD0862(alaS)
            WBM: Wbm0361
            AMA: AM224(alaS)
            APH: APH_1059(alaS)
            ERU: Erum1500(alaS)
            ERW: ERWE_CDS_01460(alaS)
            ERG: ERGA_CDS_01420(alaS)
            ECN: Ecaj_0146
            ECH: ECH_0981(alaS)
            NSE: NSE_0156(alaS)
            PUB: SAR11_0643(alaS)
            MLO: mlr0032
            MES: Meso_1266
            PLA: Plav_2579
            SME: SMc00475(alaS)
            SMD: Smed_1521
            ATU: Atu1873(alaS)
            ATC: AGR_C_3437
            RET: RHE_CH02322(alaS2)
            RLE: RL2636(alaS)
            BME: BMEI0789
            BMF: BAB1_1223(alaS)
            BMS: BR1201(alaS)
            BMB: BruAb1_1206(alaS)
            BOV: BOV_1164(alaS)
            OAN: Oant_1987
            BJA: bll5750(alaS)
            BRA: BRADO4981(alaS) BRADO5229
            BBT: BBta_5448(alaS) BBta_5692
            RPA: RPA3847(alaS)
            RPB: RPB_3737
            RPC: RPC_1571
            RPD: RPD_1734
            RPE: RPE_1598
            NWI: Nwi_1287
            NHA: Nham_1621
            BHE: BH10220(alaS)
            BQU: BQ07940(alaS)
            BBK: BARBAKC583_0728(alaS)
            XAU: Xaut_4081
            CCR: CC_2529
            SIL: SPO2033(alaS)
            SIT: TM1040_1232
            RSP: RSP_0451(alaS)
            RSH: Rsph17029_2104
            RSQ: Rsph17025_2372
            JAN: Jann_1987
            RDE: RD1_2709(alaS)
            PDE: Pden_0598
            MMR: Mmar10_1008
            HNE: HNE_2741(alaS)
            ZMO: ZMO0845(alaS)
            NAR: Saro_1279
            SAL: Sala_1720
            SWI: Swit_0508
            ELI: ELI_07720
            GOX: GOX1786
            GBE: GbCGDNIH1_1370
            ACR: Acry_1038
            RRU: Rru_A2818 Rru_A2969
            MAG: amb3532
            MGM: Mmc1_0013
            ABA: Acid345_3983
            SUS: Acid_4756
            BSU: BG12563(alaS)
            BHA: BH1267(alaS)
            BAN: BA4616(alaS)
            BAR: GBAA4616(alaS)
            BAA: BA_5057
            BAT: BAS4284
            BCE: BC4383
            BCA: BCE_4471(alaS)
            BCZ: BCZK1549 BCZK3326(alaS) BCZK4132(alaS)
            BCY: Bcer98_3101
            BTK: BT9727_4121(alaS)
            BTL: BALH_3259(alaS) BALH_3972(alaS)
            BLI: BL02033(alaSB)
            BLD: BLi02774 BLi02869(alaS)
            BCL: ABC1592(alaS)
            BAY: RBAM_024510
            BPU: BPUM_2380
            OIH: OB2009(alaS)
            GKA: GK2556(alaS)
            GTN: GTNG_2489
            SAU: SA1446(alaS)
            SAV: SAV1618(alaS)
            SAM: MW1568(alaS)
            SAR: SAR1697(alaS)
            SAS: SAS1554
            SAC: SACOL1673(alaS)
            SAB: SAB1489c(alaS)
            SAA: SAUSA300_1575(alaS)
            SAO: SAOUHSC_01722
            SAJ: SaurJH9_1675
            SAH: SaurJH1_1709
            SEP: SE1301
            SER: SERP1182(alaS)
            SHA: SH1301(alaS)
            SSP: SSP1143
            LMO: lmo1504(alaS)
            LMF: LMOf2365_1523(alaS)
            LIN: lin1539(alaS)
            LWE: lwe1517(alaS)
            LLA: L0343(alaS)
            LLC: LACR_1887
            LLM: llmg_1906(alaS)
            SPY: SPy_1389(alaS)
            SPZ: M5005_Spy_1132(alaS)
            SPM: spyM18_1399(alaS)
            SPG: SpyM3_1058(alaS)
            SPS: SPs0805
            SPH: MGAS10270_Spy1202(alaS)
            SPI: MGAS10750_Spy1239(alaS)
            SPJ: MGAS2096_Spy1198(alaS)
            SPK: MGAS9429_Spy1179(alaS)
            SPF: SpyM50726(alaS)
            SPA: M6_Spy1107
            SPB: M28_Spy1126(alaS)
            SPN: SP_1383
            SPR: spr1240(alaS)
            SPD: SPD_1216(alaS)
            SAG: SAG0810(alaS)
            SAN: gbs0829(alaS)
            SAK: SAK_0934(alaS)
            SMU: SMU.650
            STC: str0457(alaS)
            STL: stu0457(alaS)
            STE: STER_0493
            SSA: SSA_0756(alaS)
            SSU: SSU05_1236
            SSV: SSU98_1252
            SGO: SGO_1570(alaS)
            LPL: lp_2277(alaS)
            LJO: LJ0474
            LAC: LBA0417
            LSA: LSA0387(alaS)
            LSL: LSL_1111(alaS)
            LDB: Ldb1607(alaS)
            LBU: LBUL_1486
            LBR: LVIS_1223
            LCA: LSEI_0784
            LGA: LGAS_0421
            LRE: Lreu_0533
            PPE: PEPE_1263
            EFA: EF1379(alaS)
            OOE: OEOE_1167
            LME: LEUM_0556
            STH: STH2000(alaS1)
            CAC: CAC1678(alaS)
            CPE: CPE1780(alaS)
            CPF: CPF_2033(alaS)
            CPR: CPR_1750(alaS)
            CTC: CTC01055
            CNO: NT01CX_2280(alaS)
            CTH: Cthe_3200
            CDF: CD1282(alaS)
            CBO: CBO2564(alaS)
            CBA: CLB_2505(alaS)
            CBH: CLC_2435(alaS)
            CBF: CLI_2627(alaS)
            CBE: Cbei_1104
            CKL: CKL_1324(alaS)
            AMT: Amet_2458
            CHY: CHY_0538(alaS)
            DSY: DSY2421
            DRM: Dred_0769
            SWO: Swol_0468
            CSC: Csac_1894
            TTE: TTE1248(alaS)
            MTA: Moth_1644
            MGE: MG_292(alaS)
            MPN: MPN418(alaS)
            MPU: MYPU_5570(alaS)
            MPE: MYPE8540(alaS)
            MGA: MGA_0834(alaS)
            MMY: MSC_0178(alaS)
            MMO: MMOB4390(alaS)
            MHY: mhp180(alaS)
            MHJ: MHJ_0197(alaS)
            MHP: MHP7448_0201(alaS)
            MSY: MS53_0376(alaS)
            MCP: MCAP_0159(alaS)
            UUR: UU369(alaS)
            POY: PAM305(alaS)
            AYW: AYWB_416(alaS)
            MFL: Mfl613
            MTU: Rv2555c(alaS)
            MTC: MT2632(alaS)
            MBO: Mb2585c(alaS)
            MBB: BCG_2578c(alaS)
            MLE: ML0512(alaS)
            MPA: MAP1077(alaS)
            MAV: MAV_3431(alaS)
            MSM: MSMEG_3025(alaS)
            MVA: Mvan_2640
            MGI: Mflv_3763
            MMC: Mmcs_2346
            MKM: Mkms_2393
            MJL: Mjls_2387
            CGL: NCgl1570(cgl1632)
            CGB: cg1838(alaS)
            CEF: CE1748
            CDI: DIP1350(alaS)
            CJK: jk1038(alaS)
            NFA: nfa36440(alaS)
            RHA: RHA1_ro07135(alaS)
            SCO: SCO1501(alaS)
            SMA: SAV6850(alaS)
            TWH: TWT376(alaS)
            TWS: TW393(alaS)
            LXX: Lxx10910(alaS)
            ART: Arth_2278
            AAU: AAur_2281(alaS)
            PAC: PPA1178
            NCA: Noca_2407
            TFU: Tfu_2070
            FRA: Francci3_3214
            FAL: FRAAL5252(alaS)
            ACE: Acel_1330
            KRA: Krad_3032
            SEN: SACE_2052(alaS)
            STP: Strop_1828
            BLO: BL0882(alaS)
            BAD: BAD_0700(alaS)
            RXY: Rxyl_1359
            FNU: FN0697
            RBA: RB8543(alaS)
            CTR: CT749(alaS)
            CTA: CTA_0815(alaS)
            CMU: TC0125
            CPN: CPn0892(alaS)
            CPA: CP0974
            CPJ: CPj0892(alaS)
            CPT: CpB0923
            CCA: CCA00876(alaS)
            CAB: CAB842
            CFE: CF0140(alaS)
            PCU: pc1519(alaS)
            BGA: BG0223(alaS)
            BAF: BAPKO_0228(alaS)
            TPA: TP1017
            TDE: TDE1659(alaS)
            LIL: LA3407(alaS)
            LIC: LIC10763(alaS)
            LBJ: LBJ_2392(alaS)
            LBL: LBL_0716(alaS)
            SYN: sll0362(alaS)
            SYW: SYNW2360(alaS)
            SYC: syc0664_c(alaS)
            SYF: Synpcc7942_0876
            SYD: Syncc9605_2518
            SYE: Syncc9902_2173
            SYG: sync_2768(alaS)
            SYR: SynRCC307_2380(alaS)
            SYX: SynWH7803_2398(alaS)
            CYA: CYA_1881(alaS)
            CYB: CYB_1521(alaS)
            TEL: tll2103(alaS)
            GVI: gll2348(alaS) gll2349
            ANA: alr2418
            AVA: Ava_0226
            PMA: Pro0048(alaS)
            PMM: PMM0044(alaS)
            PMT: PMT2157(alaS)
            PMN: PMN2A_1377
            PMI: PMT9312_0045
            PMB: A9601_00451(alaS)
            PMC: P9515_00511(alaS)
            PMF: P9303_28371(alaS)
            PMG: P9301_00471(alaS)
            PMH: P9215_00541
            PME: NATL1_00581(alaS)
            TER: Tery_4806
            BTH: BT_3995
            BFR: BF0761
            BFS: BF0689(alaS)
            PGI: PG1246(alaS)
            SRU: SRU_1141 SRU_1544(alaS)
            CHU: CHU_1446(alaS)
            GFO: GFO_0230(alaS)
            FJO: Fjoh_1894
            FPS: FP1941(alaS)
            CTE: CT0166(alaS)
            CCH: Cag_0369
            CPH: Cpha266_0243
            PVI: Cvib_1595
            PLT: Plut_1952
            DET: DET0050(alaS)
            DEH: cbdb_A65(alaS)
            DEB: DehaBAV1_0047
            RRS: RoseRS_3223
            RCA: Rcas_3711
            DRA: DR_2300
            DGE: Dgeo_2201
            TTH: TTC1480
            TTJ: TTHA1831
            AAE: aq_1293(alaS)
            TMA: TM1396
            TPT: Tpet_1387
            TME: Tmel_1281
            FNO: Fnod_1499
            MJA: MJ0564(alaS)
            MMP: MMP0397(alaS)
            MMQ: MmarC5_1241
            MMZ: MmarC7_1395
            MAE: Maeo_0621
            MVN: Mevan_1384
            MAC: MA0194(alaS)
            MBA: Mbar_A1361
            MMA: MM_1486
            MBU: Mbur_2186
            MTP: Mthe_0657
            MHU: Mhun_0039
            MEM: Memar_1513
            MBN: Mboo_1267
            MST: Msp_1262(alaS)
            MSI: Msm_0619
            MKA: MK0900(alaS)
            HAL: VNG2283G(alaS)
            HMA: rrnAC0517(alaS2) rrnAC2561(alaS1)
            HWA: HQ2873A(alaS) HQ3670A(alaS)
            NPH: NP0710A(alaS)
            TAC: Ta0499 Ta0849
            TVO: TVN0819
            PTO: PTO0423 PTO0778
            PHO: PH0297
            PAB: PAB1245(alaS)
            PFU: PF0270
            TKO: TK1567
            RCI: RCIX939(alaS)
            APE: APE_2166
            SMR: Smar_1097
            IHO: Igni_0196
            HBU: Hbut_1607
            SSO: SSO0341(alaS)
            STO: ST1364
            SAI: Saci_1455(alaRS)
            MSE: Msed_1638
            PAI: PAE3565
            PIS: Pisl_0919
            PCL: Pcal_1993
            PAS: Pars_2228
            TPE: Tpen_0221
            NEQ: NEQ211 NEQ547
STRUCTURES  PDB: 1RIQ  1V4P  1YFR  1YFS  1YFT  1YGB  2E1B  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.7
            ExPASy - ENZYME nomenclature database: 6.1.1.7
            ExplorEnz - The Enzyme Database: 6.1.1.7
            ERGO genome analysis and discovery system: 6.1.1.7
            BRENDA, the Enzyme Database: 6.1.1.7
            CAS: 9031-71-4
///
ENTRY       EC 6.1.1.8        Obsolete  Enzyme
NAME        Deleted entry
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
COMMENT     Deleted entry: D-alanine-sRNA synthetase (EC 6.1.1.8 created 1961,
            deleted 1965)
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.8
            ExPASy - ENZYME nomenclature database: 6.1.1.8
            ExplorEnz - The Enzyme Database: 6.1.1.8
            ERGO genome analysis and discovery system: 6.1.1.8
            BRENDA, the Enzyme Database: 6.1.1.8
///
ENTRY       EC 6.1.1.9                  Enzyme
NAME        valine---tRNA ligase;
            valyl-tRNA synthetase;
            valyl-transfer ribonucleate synthetase;
            valyl-transfer RNA synthetase;
            valyl-transfer ribonucleic acid synthetase;
            valine transfer ribonucleate ligase;
            valine translase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-valine:tRNAVal ligase (AMP-forming)
REACTION    ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal
            [RN:R03665]
ALL_REAC    R03665
SUBSTRATE   ATP [CPD:C00002];
            L-valine [CPD:C00183];
            tRNA(Val) [CPD:C01653]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-valyl-tRNA(Val) [CPD:C02554]
REFERENCE   1
  AUTHORS   Berg, P., Bergmann, F.H., Ofengand, E.J. and Dieckmann, M.
  TITLE     The enzymic synthesis of amino acyl derivatives of ribonucleic acid.
            I. The mechanism of leucyl-, valyl-, isoleucyl- and methionyl
            ribonucleic acid formation.
  JOURNAL   J. Biol. Chem. 236 (1961) 1726-1734.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Bergmann, F.H., Berg, P. and Dieckmann, M.
  TITLE     The enzymic synthesis of amino acyl derivatives of ribonucleic acid.
            II. The preparation of leucyl-, valyl-, isoleucyl- and methionyl
            ribonucleic acid synthetases from Escherichia coli.
  JOURNAL   J. Biol. Chem. 236 (1961) 1735-1740.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00290  Valine, leucine and isoleucine biosynthesis
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01873  valyl-tRNA synthetase
GENES       HSA: 57176(VARS2) 7407(VARS)
            PTR: 462568(VARS)
            MMU: 22321(Vars)
            RNO: 25009(Vars2)
            CFA: 481716(VARS)
            XLA: 495303(LOC495303)
            SPU: 576254(LOC576254)
            DME: Dmel_CG4062(Aats-val) Dmel_CG5660
            CEL: Y87G2A.5(vrs-2) ZC513.4(vrs-1)
            ATH: AT1G14610(TWN2) AT5G16710(DHAR3)
            OSA: 4333799
            CME: CMP345C CMT275C
            SCE: YGR094W(VAS1)
            AGO: AGOS_AAR034W
            PIC: PICST_72245(VAS1)
            CGR: CAGL0G03091g
            SPO: SPAC4A8.08c SPBC1709.02c
            ANI: AN1484.2
            AFM: AFUA_8G04800
            AOR: AO090005000667
            CNE: CNB01880
            ECU: ECU04_1140
            DDI: DDB_0231269(valS1) DDB_0231274(valS2)
            PFA: MAL3P4.19 PF14_0589
            CPV: cgd8_3100
            CHO: Chro.80361
            TAN: TA09105 TA10235
            TPV: TP04_0572 TP04_0740
            TET: TTHERM_00471530 TTHERM_00491030 TTHERM_01080450
                 TTHERM_01443820
            TBR: Tb927.6.4480
            TCR: 504257.70 509167.100
            LMA: LmjF30.3130
            EHI: 206.t00014
            ECO: b4258(valS)
            ECJ: JW4215(valS)
            ECE: Z5870(valS)
            ECS: ECs5235
            ECC: c5358(valS)
            ECI: UTI89_C4864(valS)
            ECP: ECP_4507
            ECV: APECO1_2136(valS)
            ECW: EcE24377A_4829(valS)
            ECX: EcHS_A4514(valS)
            STY: STY4814(valS)
            STT: t4510(valS)
            SPT: SPA4276(valS)
            SEC: SC4331(valS)
            STM: STM4475(valS)
            YPE: YPO3443(valS)
            YPK: y0743(valS)
            YPM: YP_0641(valS)
            YPA: YPA_2944
            YPN: YPN_0645
            YPP: YPDSF_3253
            YPS: YPTB0529(valS)
            YPI: YpsIP31758_3545(valS)
            YEN: YE0498(valS)
            SFL: SF4231(valS)
            SFX: S4492(valS)
            SFV: SFV_4235(valS)
            SSN: SSON_4443(valS)
            SBO: SBO_4182(valS)
            SDY: SDY_4282(valS)
            ECA: ECA0402(valS)
            PLU: plu4483(valS)
            BUC: BU366(valS)
            BAS: BUsg354(valS)
            BAB: bbp331(valS)
            BCC: BCc_223(valS)
            WBR: WGLp460(valS)
            SGL: SG2111
            BFL: Bfl033(valS)
            BPN: BPEN_033(valS)
            HIN: HI1391(valS)
            HIT: NTHI1760(valS)
            HIP: CGSHiEE_04530(valS)
            HIQ: CGSHiGG_00745(valS)
            HDU: HD0669(valS)
            HSO: HS_1259(valS)
            PMU: PM0818(valS)
            MSU: MS1556(valS)
            APL: APL_1502(valS)
            XFA: XF0134
            XFT: PD0102(valS)
            XCC: XCC0646(valS)
            XCB: XC_3588
            XCV: XCV3684(valS)
            XAC: XAC3559(valS)
            XOO: XOO0831(valS)
            XOM: XOO_0757(XOO0757)
            VCH: VC2503
            VCO: VC0395_A2085(valS)
            VVU: VV1_1474
            VVY: VV2910
            VPA: VP2646
            VFI: VF0411(val)
            PPR: PBPRA0483
            PAE: PA3834(valS)
            PAU: PA14_14440(valS)
            PAP: PSPA7_1279(valS)
            PPU: PP_0977(valS)
            PST: PSPTO_1268(valS)
            PSB: Psyr_1086
            PSP: PSPPH_1153(valS)
            PFL: PFL_1063(valS)
            PFO: Pfl_0986
            PEN: PSEEN4446(valS)
            PAR: Psyc_1850(valS)
            PCR: Pcryo_2138
            ACI: ACIAD2950(valS)
            ACB: A1S_2742
            SON: SO_3424(valS)
            SDN: Sden_2867
            SFR: Sfri_0916
            SAZ: Sama_0790
            SBL: Sbal_3112
            SLO: Shew_0923
            SHE: Shewmr4_1130
            SHM: Shewmr7_1201
            SHN: Shewana3_1131
            SHW: Sputw3181_1270
            ILO: IL1950(valS)
            CPS: CPS_0738(valS)
            PHA: PSHAa2425(valS)
            PAT: Patl_3564
            SDE: Sde_1369
            PIN: Ping_0393
            MAQ: Maqu_0959
            CBU: CBU_0808(valS)
            CBD: COXBU7E912_0874(valS)
            LPN: lpg0719(valS)
            LPF: lpl0756(valS)
            LPP: lpp0785(valS)
            MCA: MCA2097(valS)
            FTU: FTT0299(valS)
            FTF: FTF0299(valS)
            FTW: FTW_1786(valS)
            FTL: FTL_0210
            FTH: FTH_0205(valS)
            FTA: FTA_0226(valS)
            FTN: FTN_0214(valS)
            TCX: Tcr_1503
            NOC: Noc_1091
            AEH: Mlg_0555
            HHA: Hhal_0684
            HCH: HCH_01928(valS)
            CSA: Csal_2922
            ABO: ABO_0492(valS)
            AHA: AHA_3702(valS)
            DNO: DNO_0351(valS)
            BCI: BCI_0285(valS)
            CRP: CRP_111
            RMA: Rmag_0464
            VOK: COSY_0429(valS)
            NME: NMB0174
            NMA: NMA0094(valS)
            NGO: NGO1809
            CVI: CV_2669(valS)
            RSO: RSc2236(valS)
            REU: Reut_A0863
            REH: H16_A2751(valS)
            RME: Rmet_2630
            BMA: BMA0927(valS)
            BMV: BMASAVP1_A1460(valS)
            BML: BMA10299_A0422(valS)
            BMN: BMA10247_0741(valS)
            BXE: Bxe_A1335
            BUR: Bcep18194_A4585
            BCN: Bcen_0959
            BCH: Bcen2424_1441
            BAM: Bamb_1321
            BPS: BPSL1980(valS)
            BPM: BURPS1710b_1846(valS)
            BPL: BURPS1106A_1691(valS)
            BPD: BURPS668_1669(valS)
            BTE: BTH_I2633(valS)
            BPE: BP2203(valS)
            BPA: BPP2859(valS)
            BBR: BB3180(valS)
            RFR: Rfer_2376
            POL: Bpro_3721
            MPT: Mpe_A1137
            HAR: HEAR0261(valS)
            MMS: mma_0315(valS)
            NEU: NE0444(valS)
            NET: Neut_0602
            NMU: Nmul_A0742
            EBA: ebA7186(valS)
            AZO: azo2907(valS)
            DAR: Daro_3085
            TBD: Tbd_0577
            MFA: Mfla_0091
            HPY: HP1153(val)
            HPJ: jhp1080(valS)
            HPA: HPAG1_1092
            HHE: HH0933(valS)
            HAC: Hac_1320(valS)
            WSU: WS1652
            TDN: Tmden_0737
            CJE: Cj0775c(valS)
            CJR: CJE0866(valS)
            CJJ: CJJ81176_0796(valS)
            CJU: C8J_0726(valS)
            CJD: JJD26997_1237(valS)
            CFF: CFF8240_0966(valS)
            CCV: CCV52592_1076(valS)
            CHA: CHAB381_1227(valS)
            CCO: CCC13826_0077 CCC13826_1252(valS)
            ABU: Abu_0581(valS)
            NIS: NIS_1013(valS)
            SUN: SUN_1375(valS)
            GSU: GSU2045(valS)
            GME: Gmet_0956
            PCA: Pcar_2315
            DVU: DVU0732(valS)
            DDE: Dde_2839
            LIP: LI0648(valS)
            BBA: Bd0458(valS)
            DPS: DP1796
            ADE: Adeh_2390
            MXA: MXAN_4460(valS)
            SAT: SYN_02886
            SFU: Sfum_0192
            RPR: RP687
            RTY: RT0682(valS)
            RCO: RC1053(valS)
            RFE: RF_0229(valS)
            RBE: RBE_0509(valS)
            RAK: A1C_05365(valS)
            RBO: A1I_02925(valS)
            RCM: A1E_04595(valS)
            RRI: A1G_05850(valS)
            OTS: OTBS_0273(valS)
            WOL: WD0464(valS)
            WBM: Wbm0786
            AMA: AM1170(valS)
            APH: APH_1224(valS)
            ERU: Erum0780(valS) Erum0781 Erum0782
            ERW: ERWE_CDS_00710(valS)
            ERG: ERGA_CDS_00680(valS)
            ECN: Ecaj_0088
            ECH: ECH_0136(valS)
            NSE: NSE_0603
            PUB: SAR11_0960(valS)
            MLO: mll1104
            MES: Meso_1571
            SME: SMc02080(valS)
            ATU: Atu1719(valS)
            ATC: AGR_C_3157
            RET: RHE_CH01811(valS)
            RLE: RL2035(valS)
            BME: BMEI1027
            BMF: BAB1_0966(valS)
            BMS: BR0948(valS)
            BMB: BruAb1_0957(valS)
            BOV: BOV_0940(valS)
            BJA: blr4475(valS)
            BRA: BRADO3881(valS)
            BBT: BBta_3947(valS)
            RPA: RPA2583(valS)
            RPB: RPB_2892
            RPC: RPC_2570
            RPD: RPD_2579
            RPE: RPE_2750
            NWI: Nwi_1436
            NHA: Nham_1828
            BHE: BH10630(valS)
            BQU: BQ08350(valS)
            BBK: BARBAKC583_0654(valS1) BARBAKC583_0687(valS2)
            CCR: CC_1320
            SIL: SPO3022
            SIT: TM1040_1706
            RSP: RSP_1989(valS)
            JAN: Jann_3477
            RDE: RD1_1754(valS)
            MMR: Mmar10_1928
            HNE: HNE_1676(valS)
            ZMO: ZMO1878(valS)
            NAR: Saro_2846
            ELI: ELI_01295
            GOX: GOX2489
            GBE: GbCGDNIH1_0933
            RRU: Rru_A1796
            MAG: amb2247
            MGM: Mmc1_1474
            ABA: Acid345_0132
            BSU: BG10321(valS)
            BHA: BH3038(valS)
            BAN: BA4690(valS)
            BAR: GBAA4690(valS)
            BAA: BA_5129
            BAT: BAS4355
            BCE: BC4465
            BCA: BCE_4549(valS)
            BCZ: BCZK4202(valS)
            BTK: BT9727_4191(valS)
            BTL: BALH_4051(valS)
            BLI: BL00631(valS)
            BLD: BLi02938(valS)
            BCL: ABC2621(valS)
            BAY: RBAM_025140(valS)
            BPU: BPUM_2449(valS)
            OIH: OB2061(valS)
            GKA: GK2638(val)
            SAU: SA1488(valS)
            SAV: SAV1663(valS)
            SAM: MW1607(valS)
            SAR: SAR1743(valS)
            SAS: SAS1592
            SAC: SACOL1710(valS)
            SAB: SAB1524c(valS)
            SAA: SAUSA300_1611(valS)
            SAO: SAOUHSC_01767
            SEP: SE1339
            SER: SERP1228(valS)
            SHA: SH1263(valS)
            SSP: SSP1101
            LMO: lmo1552(valS)
            LMF: LMOf2365_1573(valS)
            LIN: lin1587(valS)
            LWE: lwe1565
            LLA: L0351(valS)
            LLC: LACR_2479
            LLM: llmg_2455(valS)
            SPY: SPy_1568(valS)
            SPZ: M5005_Spy_1292(valS)
            SPM: spyM18_1579(valS)
            SPG: SpyM3_1273(valS)
            SPS: SPs0589
            SPH: MGAS10270_Spy1373(valS)
            SPI: MGAS10750_Spy1400(valS)
            SPJ: MGAS2096_Spy1311(valS)
            SPK: MGAS9429_Spy1286(valS)
            SPF: SpyM50564(valS)
            SPA: M6_Spy1310
            SPB: M28_Spy1296(valS)
            SPN: SP_0568
            SPR: spr0492(valS)
            SPD: SPD_0494(valS)
            SAG: SAG0445(valS)
            SAN: gbs0492
            SAK: SAK_0547(valS)
            SMU: SMU.1770(syv)
            STC: str0477(valS)
            STL: stu0477(valS)
            SSA: SSA_1819(valS)
            SGO: SGO_0639(valS)
            LPL: lp_2322(valS)
            LJO: LJ0958
            LAC: LBA0794
            LSA: LSA0849(valS)
            LSL: LSL_1072(valS)
            LDB: Ldb0727(valS)
            LBU: LBUL_0659
            LBR: LVIS_1253
            LCA: LSEI_1251
            EFA: EF2931(valS)
            OOE: OEOE_1392
            STH: STH366(valS)
            CAC: CAC2399(vals)
            CPE: CPE1919(valS)
            CPF: CPF_2175(valS)
            CPR: CPR_1886(valS)
            CTC: CTC02302
            CNO: NT01CX_1727(valS)
            CDF: CD3256(valS)
            CBO: CBO3164(valS)
            CBA: CLB_3199(valS)
            CBH: CLC_3073(valS)
            CBF: CLI_3228(valS)
            CKL: CKL_3219(valS)
            CHY: CHY_0334(valS)
            DSY: DSY3188
            SWO: Swol_1649
            TTE: TTE0781(valS)
            MTA: Moth_0532
            MGE: MG_334(valS)
            MPN: MPN480(valS)
            MPU: MYPU_2570(valS)
            MPE: MYPE420(valS)
            MGA: MGA_0338(valS)
            MMY: MSC_0303(valS)
            MMO: MMOB1580(valS)
            MHY: mhp694(valS)
            MHJ: MHJ_0671(valS)
            MHP: MHP7448_0672(valS)
            MSY: MS53_0298(valS)
            MCP: MCAP_0258(valS)
            UUR: UU267(valS)
            POY: PAM018(valS)
            AYW: AYWB_012(valS)
            MFL: Mfl355
            MTU: Rv2448c(valS)
            MTC: MT2524(valS)
            MBO: Mb2475c(valS)
            MBB: BCG_2468c(valS)
            MLE: ML1472(valS)
            MPA: MAP2271c(valS)
            MAV: MAV_1724(valS)
            MSM: MSMEG_4630(valS)
            MMC: Mmcs_3558
            CGL: NCgl2293(cgl2376)
            CGB: cg2609(valS)
            CEF: CE2282
            CDI: DIP1786(valS)
            CJK: jk0550(valS)
            NFA: nfa13480(valS)
            RHA: RHA1_ro01318
            SCO: SCO2615(SCC88.26c)
            SMA: SAV5451(valS)
            TWH: TWT478(valS)
            TWS: TW286
            LXX: Lxx07930(valS)
            PAC: PPA1568
            TFU: Tfu_1936
            FRA: Francci3_1314
            FAL: FRAAL2075(valS)
            ACE: Acel_0741
            SEN: SACE_1384(valS)
            BLO: BL0395(valS)
            BAD: BAD_1450(valS)
            RXY: Rxyl_1535
            FNU: FN2011
            RBA: RB1319(valS)
            CTR: CT302(valS)
            CTA: CTA_0324(valS)
            CMU: TC0576
            CPN: CPn0094(valS)
            CPA: CP0680
            CPJ: CPj0094(valS)
            CPT: CpB0094
            CCA: CCA00678(valS)
            CAB: CAB648(valS)
            CFE: CF0333(valS)
            PCU: pc1654(valS)
            BGA: BG0759(valS)
            BAF: BAPKO_0781(valS)
            TPA: TP1035(valS)
            TDE: TDE1364(valS)
            LIL: LA3763(valS)
            LIC: LIC10473(valS)
            LBJ: LBJ_0531(valS)
            LBL: LBL_2548(valS)
            SYN: slr0557(valS)
            SYW: SYNW2396(valS)
            SYC: syc0936_c(valS)
            SYF: Synpcc7942_0587
            SYD: Syncc9605_2558
            SYE: Syncc9902_2213
            SYG: sync_2822 sync_2825(valS)
            SYR: SynRCC307_2416(valS)
            SYX: SynWH7803_2440(valS)
            CYA: CYA_0512(valS)
            CYB: CYB_0301(valS)
            TEL: tlr1503(valS)
            GVI: glr2919(valS)
            ANA: all1318(valS)
            AVA: Ava_2982
            PMA: Pro1844(valS)
            PMM: PMM1682(valS)
            PMT: PMT2191(valS)
            PMN: PMN2A_1281
            PMI: PMT9312_1775
            PMB: A9601_18921(valS)
            PMC: P9515_18731(valS)
            PMF: P9303_29141(valS)
            PMG: P9301_18731(valS)
            PMH: P9215_19551(valS)
            PME: NATL1_21531(valS)
            TER: Tery_3441
            BTH: BT_4353
            BFR: BF1050
            BFS: BF0966(valS)
            PGI: PG1132(valS)
            SRU: SRU_2044(valS)
            CHU: CHU_2435(valS)
            GFO: GFO_2933(valS)
            FPS: FP1698(valS)
            CTE: CT1552(valS)
            CCH: Cag_0388
            PLT: Plut_0386
            DET: DET0430(valS)
            DEH: cbdb_A384(valS)
            DRA: DR_0148
            DGE: Dgeo_1951
            TTH: TTC0805
            TTJ: TTHA1169
            AAE: aq_1413(valS)
            TMA: TM1817
            MJA: MJ1007(valS)
            MMP: MMP0584(valS)
            MAC: MA3052(valS)
            MBA: Mbar_A1976
            MMA: MM_0314
            MBU: Mbur_2184
            MHU: Mhun_2626
            MST: Msp_0499(valS)
            MSI: Msm_0275
            MKA: MK1424(valS)
            HAL: VNG2547G(valS)
            HMA: rrnAC1729(valS)
            HWA: HQ1051A(valS)
            NPH: NP0288A(valS)
            TAC: Ta0040
            TVO: TVN0032
            PTO: PTO0532
            PHO: PH0314
            PAB: PAB1255(valS)
            PFU: PF0290
            TKO: TK1274
            RCI: LRC303(valS)
            APE: APE_1805.1
            HBU: Hbut_0879
            SSO: SSO0899(valS)
            STO: ST1224
            SAI: Saci_1430(valS)
            PAI: PAE2297
            NEQ: NEQ252
STRUCTURES  PDB: 1GAX  1IVS  1IYW  1WK9  1WKA  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.9
            ExPASy - ENZYME nomenclature database: 6.1.1.9
            ExplorEnz - The Enzyme Database: 6.1.1.9
            ERGO genome analysis and discovery system: 6.1.1.9
            BRENDA, the Enzyme Database: 6.1.1.9
            CAS: 9023-47-6
///
ENTRY       EC 6.1.1.10                 Enzyme
NAME        methionine---tRNA ligase;
            methionyl-tRNA synthetase;
            methionyl-transfer ribonucleic acid synthetase;
            methionyl-transfer ribonucleate synthetase;
            methionyl-transfer RNA synthetase;
            methionine translase;
            MetRS
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-methionine:tRNAMet ligase (AMP-forming)
REACTION    ATP + L-methionine + tRNAMet = AMP + diphosphate +
            L-methionyl-tRNAMet [RN:R03659]
ALL_REAC    R03659;
            (other) R04773
SUBSTRATE   ATP [CPD:C00002];
            L-methionine [CPD:C00073];
            tRNA(Met) [CPD:C01647]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-methionyl-tRNA(Met) [CPD:C02430]
COMMENT     In those organisms producing N-formylmethionyl-tRNAfMet for
            translation initiation, this enzyme also recognizes the initiator
            tRNAfMet and catalyses the formation of L-methionyl-tRNAfMet, the
            substrate for EC 2.1.2.9, methionyl-tRNA formyltransferase.
REFERENCE   1
  AUTHORS   Bergmann, F.H., Berg, P. and Dieckmann, M.
  TITLE     The enzymic synthesis of amino acyl derivatives of ribonucleic acid.
            II. The preparation of leucyl-, valyl-, isoleucyl- and methionyl
            ribonucleic acid synthetases from Escherichia coli.
  JOURNAL   J. Biol. Chem. 236 (1961) 1735-1740.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:1409632]
  AUTHORS   Lee CP, Dyson MR, Mandal N, Varshney U, Bahramian B, RajBhandary UL.
  TITLE     Striking effects of coupling mutations in the acceptor stem on
            recognition of tRNAs by Escherichia coli Met-tRNA synthetase and
            Met-tRNA transformylase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 9262-6.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00271  Methionine metabolism
            PATH: map00450  Selenoamino acid metabolism
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01874  methionyl-tRNA synthetase
GENES       HSA: 4141(MARS) 92935(MARS2)
            MCC: 714744(LOC714744)
            MMU: 212679(Mars2) 216443(Mars)
            CFA: 474414(MARS) 608449(MARS2)
            XLA: 379675(MGC69150)
            DRE: 338183(mars)
            DME: Dmel_CG15100 Dmel_CG31322(Aats-met)
            CEL: F58B3.5(mrs-1) Y105E8A.20
            ATH: AT3G55400(OVA1) AT4G13780
            OSA: 4332018 4341140
            CME: CME015C CMI094C
            SCE: YGR171C(MSM1) YGR264C(MES1)
            AGO: AGOS_AAL133W AGOS_AGR332C
            PIC: PICST_65359(ARC1) PICST_76328(MES1) PICST_81660(MSM1)
            CAL: CaO19_3950(CaO19.3950) CaO19_3955(CaO19.3955)
            CGR: CAGL0F08459g CAGL0I08723g CAGL0J10406g
            SPO: SPAC27E2.06c SPBC17A3.04c
            ANI: AN1380.2 AN3865.2
            AFM: AFUA_1G09010 AFUA_4G07820 AFUA_5G03600
            AOR: AO090012000394 AO090023000789
            CNE: CNA00060 CND04250
            UMA: UM02044.1 UM02894.1 UM03531.1
            ECU: ECU11_0890
            DDI: DDB_0231296(mmetS) DDB_0231297(metS)
            PFA: PF10_0053 PF10_0340
            CPV: cgd8_3460
            CHO: Chro.80398
            TAN: TA05325 TA09735
            TPV: TP01_1212 TP03_0137
            TET: TTHERM_00691810 TTHERM_01145010
            TBR: Tb10.70.6470
            TCR: 509247.50
            LMA: LmjF21.0810
            EHI: 102.t00015
            ECO: b2114(metG)
            ECJ: JW2101(metG)
            ECE: Z3282(metG)
            ECS: ECs2920
            ECC: c2642(metG)
            ECI: UTI89_C2388(metG)
            ECP: ECP_2152
            ECV: APECO1_4433(metG)
            ECW: EcE24377A_2404(metG)
            ECX: EcHS_A2249
            STY: STY2384(metG)
            STT: t0701(metG)
            SPT: SPA0697(metG)
            SEC: SC2170(metG)
            STM: STM2155(metG)
            YPE: YPO1522(metG)
            YPK: y2648(metG)
            YPM: YP_1411(metG)
            YPA: YPA_0816
            YPN: YPN_2458
            YPP: YPDSF_1454
            YPS: YPTB1534(metG)
            YPI: YpsIP31758_2455(metG)
            SFL: SF2179(metG_1)
            SFX: S2303(metG)
            SFV: SFV_2170(metG)
            SSN: SSON_2163(metG)
            SBO: SBO_0929(metG)
            SDY: SDY_2181(metG)
            ECA: ECA1409(metG)
            PLU: plu1554(metG)
            BUC: BU109(metG)
            BAS: BUsg102(metG)
            BAB: bbp103(metG)
            BCC: BCc_072(metG)
            WBR: WGLp536(metG)
            SGL: SG0970
            BFL: Bfl471(metG)
            BPN: BPEN_486(metG)
            HIN: HI1276(metG)
            HIT: NTHI1894(metG)
            HIQ: CGSHiGG_01600(metG)
            HDU: HD1054(metG)
            HSO: HS_1179(metG)
            PMU: PM0303(metG)
            MSU: MS1631(metG)
            APL: APL_0352(metG)
            XFA: XF0549
            XFT: PD1590(metG)
            XCC: XCC1339(metS)
            XCB: XC_2900
            XCV: XCV1441(metS)
            XAC: XAC1386(metS)
            XOO: XOO1924(metS)
            XOM: XOO_1823(XOO1823)
            VCH: VC1036
            VCO: VC0395_A0554(metG)
            VVU: VV1_3028
            VVY: VV1259
            VPA: VP2069
            VFI: VF1754
            PPR: PBPRA1168(metG)
            PAE: PA3482(metG)
            PAU: PA14_19050(metG)
            PPU: PP_1097(metG)
            PPF: Pput_1137
            PST: PSPTO_4147(metG)
            PSB: Psyr_2749 Psyr_3886
            PSP: PSPPH_1378(metG)
            PFL: PFL_4844
            PFO: Pfl_4507
            PEN: PSEEN0982 PSEEN1220(metG)
            PMY: Pmen_1405
            PAR: Psyc_1432(metG)
            PCR: Pcryo_1596
            PRW: PsycPRwf_1709
            ACI: ACIAD0768(metG)
            SON: SO_2619(metG)
            SDN: Sden_2056
            SFR: Sfri_2246
            SAZ: Sama_2049
            SBL: Sbal_2465
            SBM: Shew185_2458
            SLO: Shew_1573
            SSE: Ssed_2653
            SPL: Spea_1917
            SHE: Shewmr4_1655
            SHM: Shewmr7_1730
            SHN: Shewana3_1760
            SHW: Sputw3181_1789
            ILO: IL0711(metG)
            CPS: CPS_2839(metG)
            PHA: PSHAa1317(metG)
            PAT: Patl_1897
            SDE: Sde_2398
            PIN: Ping_1623
            MAQ: Maqu_0939
            CBU: CBU_1695(metG)
            CBD: COXBU7E912_0308(metG)
            LPN: lpg2882(metG_1)
            LPF: lpl2795(metG)
            LPP: lpp2941(metG)
            MCA: MCA0016(metG)
            FTU: FTT1290(metG)
            FTF: FTF1290(metG)
            FTW: FTW_0758(metG)
            FTL: FTL_0444
            FTH: FTH_0437(metG)
            FTA: FTA_0468(metG)
            FTN: FTN_0468(metG)
            TCX: Tcr_1037
            NOC: Noc_0971
            AEH: Mlg_0817
            HHA: Hhal_0717
            HCH: HCH_01897(metG)
            CSA: Csal_2120
            ABO: ABO_1599(metG)
            MMW: Mmwyl1_1546
            AHA: AHA_0208 AHA_2233(metG)
            DNO: DNO_0934(metG)
            BCI: BCI_0396(metG)
            CRP: CRP_102
            RMA: Rmag_0570
            VOK: COSY_0525(metG)
            NME: NMB0030
            NMA: NMA0275(metG)
            NMC: NMC0007(metG)
            NGO: NGO2044(metG)
            CVI: CV_1206(metG)
            RSO: RSc1818(metG2) RSc2381(metG1)
            REU: Reut_A0674
            REH: H16_A2945(metG)
            RME: Rmet_2769
            BMA: BMA0709(metG)
            BMV: BMASAVP1_A2304(metG)
            BML: BMA10299_A2982(metG)
            BMN: BMA10247_1617(metG)
            BXE: Bxe_A3483
            BUR: Bcep18194_A5768
            BCN: Bcen_1826
            BCH: Bcen2424_2437
            BAM: Bamb_2484
            BPS: BPSL0998(metG)
            BPM: BURPS1710b_1211(metG)
            BPL: BURPS1106A_1057(metG)
            BPD: BURPS668_1052(metG)
            BTE: BTH_I0856
            BPE: BP0180(metG)
            BPA: BPP0755(metG)
            BBR: BB0840(metG)
            RFR: Rfer_3275
            POL: Bpro_0924
            MPT: Mpe_A1161
            HAR: HEAR0980(metG)
            MMS: mma_1112
            NEU: NE0625(metG1)
            NET: Neut_1921
            NMU: Nmul_A1936
            EBA: ebA4404(metG)
            AZO: azo3203
            DAR: Daro_0574
            TBD: Tbd_0860
            MFA: Mfla_0921 Mfla_1065
            HPY: HP0417(metS)
            HPJ: jhp0967(metG)
            HPA: HPAG1_0977
            HHE: HH1342(metG)
            HAC: Hac_0605(metS)
            WSU: WS0217(metS)
            TDN: Tmden_1065
            CJE: Cj0838c(metS)
            CJR: CJE0925(metS)
            CJJ: CJJ81176_0855(metS)
            CJU: C8J_0785(metS)
            CJD: JJD26997_0988(metS)
            CFF: CFF8240_0796(metG)
            CCV: CCV52592_0445(metG)
            CHA: CHAB381_0727(metG)
            ABU: Abu_1221(metS)
            NIS: NIS_0794(metG)
            SUN: SUN_1128(metG)
            GSU: GSU2232(metG)
            GME: Gmet_2321
            PCA: Pcar_1694
            DVU: DVU2055(metG)
            DDE: Dde_1594
            LIP: LI1183(metG)
            BBA: Bd1733(metG)
            DPS: DP0786
            ADE: Adeh_1314
            MXA: MXAN_2804
            SAT: SYN_00558
            SFU: Sfum_0154
            RPR: RP683(metS)
            RTY: RT0678(metS)
            RCO: RC1046(metG)
            RFE: RF_0235(metG)
            RBE: RBE_0238(metG)
            RAK: A1C_05330
            RBO: A1I_06680
            RCM: A1E_04540
            RRI: A1G_05810
            WOL: WD0352(metG)
            WBM: Wbm0196
            AMA: AM1001(metS)
            APH: APH_1079(metG)
            ERU: Erum7710(metG)
            ERW: ERWE_CDS_08150(metG)
            ERG: ERGA_CDS_08050(metG)
            ECN: Ecaj_0807
            ECH: ECH_1000(metG)
            NSE: NSE_0893(metG)
            PUB: SAR11_1001(metS)
            MLO: mll0419
            MES: Meso_1583
            SME: SMc01192(metS)
            ATU: Atu1496(metS)
            ATC: AGR_C_2757
            RET: RHE_CH02157(metS) RHE_CH03014(csaA) RHE_PD00315(ypd00050)
            RLE: RL2473(metG)
            BME: BMEI0987
            BMF: BAB1_1014(metG)
            BMS: BR0995(metG)
            BMB: BruAb1_1001(metG)
            BOV: BOV_0962(metG)
            BJA: bll4516(metG)
            BRA: BRADO3829
            BBT: BBta_4100
            RPA: RPA2777(metG)
            RPB: RPB_2681
            RPC: RPC_2705
            RPD: RPD_2717
            RPE: RPE_2867
            NWI: Nwi_1462(metG)
            NHA: Nham_2008
            BHE: BH08480(metS)
            BQU: BQ06090(metS)
            BBK: BARBAKC583_0820(metG)
            CCR: CC_1480
            SIL: SPO1403(metG)
            SIT: TM1040_2197
            RSP: RSP_0425(metG)
            RSH: Rsph17029_2081
            RSQ: Rsph17025_2349
            JAN: Jann_3145
            RDE: RD1_2516(metG)
            PDE: Pden_2045
            MMR: Mmar10_1827
            HNE: HNE_1831(metG)
            ZMO: ZMO1092(metG)
            NAR: Saro_1939
            SAL: Sala_1259
            ELI: ELI_06225
            GOX: GOX0016
            GBE: GbCGDNIH1_1077
            RRU: Rru_A1701
            MAG: amb2448
            MGM: Mmc1_1856
            ABA: Acid345_2030
            BSU: BG10101(metS)
            BHA: BH0053(metS)
            BAN: BA0036(metS) BA5278
            BAR: GBAA0036(metS) GBAA5278
            BAA: BA_0140 BA_0626
            BAT: BAS0037 BAS4903
            BCE: BC0043 BC5031
            BCA: BCE_0036(metS) BCE_5177
            BCZ: BCZK0034(metS)
            BTK: BT9727_0034(metS) BT9727_4747(metG)
            BTL: BALH_0034(metS) BALH_4573(metG)
            BLI: BL00533(metS)
            BLD: BLi00051(metS)
            BCL: ABC0061(metS)
            BAY: RBAM_000470
            BPU: BPUM_0022
            OIH: OB0046
            GKA: GK0031
            SAU: SA0448(metS)
            SAV: SAV0490(metS)
            SAM: MW0445(metS)
            SAR: SAR0491(metG)
            SAS: SAS0447
            SAC: SACOL0533(metS)
            SAB: SAB0439(metG)
            SAA: SAUSA300_0467(metS)
            SAO: SAOUHSC_00461
            SEP: SE2293
            SER: SERP0128(metS)
            SHA: SH2521(metS)
            SSP: SSP2266
            LMO: lmo0177(metS)
            LMF: LMOf2365_0188(metG)
            LIN: lin0216(metS)
            LWE: lwe0153(metS)
            LLA: L0353(metS)
            LLC: LACR_0842
            LLM: llmg_1764(metS)
            SPY: SPy_0422(metS)
            SPZ: M5005_Spy_0345(metG)
            SPM: spyM18_0468(metS)
            SPG: SpyM3_0300(metS)
            SPS: SPs1557
            SPH: MGAS10270_Spy0343(metS)
            SPI: MGAS10750_Spy0347(metS)
            SPJ: MGAS2096_Spy0364(metS)
            SPK: MGAS9429_Spy0348(metS)
            SPF: SpyM51515(metG)
            SPA: M6_Spy0370
            SPB: M28_Spy0332(metG)
            SPN: SP_0788
            SPR: spr0696(metS)
            SPD: SPD_0689(metG)
            SAG: SAG1557(metG)
            SAN: gbs1611(metS)
            SAK: SAK_1576(metG)
            SMU: SMU.1639(metS)
            STC: str0451(metS)
            STL: stu0451(metS)
            SSA: SSA_1703(metS)
            SGO: SGO_1530
            LPL: lp_0454(metS)
            LJO: LJ0202
            LAC: LBA0213
            LSA: LSA1658(metS)
            LSL: LSL_0226(metG)
            LDB: Ldb0342(metS)
            LBU: LBUL_0297
            LBR: LVIS_0455
            LCA: LSEI_2603
            EFA: EF0930(metG)
            OOE: OEOE_1746
            STH: STH3252(metS1)
            CAC: CAC2991(metS)
            CPE: CPE2523(metS) CPE2524
            CPF: CPF_2846(metG) CPF_2847(metG)
            CPR: CPR_2532(metG) CPR_2533(metG)
            CTC: CTC00243
            CNO: NT01CX_0697(metG)
            CDF: CD3540(metG)
            CBO: CBO0075(metG)
            CBA: CLB_0111(metG)
            CBH: CLC_0123(metG)
            CBF: CLI_0132(metG)
            CBE: Cbei_3185
            CKL: CKL_3766(metS)
            CHY: CHY_2621(metS)
            DSY: DSY0128
            SWO: Swol_0049
            TTE: TTE0110(metG)
            MTA: Moth_0048
            MGE: MG_021(metS)
            MPN: MPN023(metS)
            MPU: MYPU_4900(metS)
            MPE: MYPE9380(metS)
            MGA: MGA_0893(metS)
            MMY: MSC_0012(metS)
            MMO: MMOB3150(metS)
            MHY: mhp410(metG)
            MHJ: MHJ_0409(metS)
            MHP: MHP7448_0396(metS)
            MSY: MS53_0303(metG)
            MCP: MCAP_0035(metG)
            UUR: UU197(metS)
            POY: PAM233(metG)
            AYW: AYWB_489(metG)
            MFL: Mfl036
            MTU: Rv1007c(metS)
            MTC: MT1036(metS)
            MBO: Mb1034c(metS)
            MBB: BCG_1064c(metS)
            MLE: ML0238(metS)
            MPA: MAP0972c(metS)
            MAV: MAV_1145(metG)
            MSM: MSMEG_5441(metG)
            MMC: Mmcs_4266
            CGL: NCgl0857(cgl0893)
            CGB: cg1017(metS)
            CEF: CE0967
            CDI: DIP0872(metG)
            CJK: jk1516(metS)
            NFA: nfa49060(metS)
            RHA: RHA1_ro05663(metS1) RHA1_ro08655(metS2)
            SCO: SCO3792(SCH63.39)
            SMA: SAV4403(metS)
            TWH: TWT763(metS)
            TWS: TW775(metG)
            LXX: Lxx06770(metG) Lxx17520(metG)
            AAU: AAur_2503(metG)
            PAC: PPA1728
            TFU: Tfu_0389
            FRA: Francci3_0491
            FAL: FRAAL0990(metG)
            ACE: Acel_0175
            SEN: SACE_0799(metS)
            BLO: BL0170(metG)
            BAD: BAD_1535
            FNU: FN1268
            RBA: RB5543(metG)
            CTR: CT032(metG)
            CTA: CTA_0034(metG)
            CMU: TC0301
            CPN: CPn0122(metG)
            CPA: CP0651
            CPJ: CPj0122(metG)
            CPT: CpB0123
            CCA: CCA00651(metG)
            CAB: CAB622(metG)
            CFE: CF0360(metG)
            PCU: pc0665(metG)
            BBU: BB0587(metG)
            BGA: BG0600(metG)
            BAF: BAPKO_0618(metG)
            TPA: TP0798
            TDE: TDE1063(metG)
            LIL: LA3918(metG)
            LIC: LIC13129(metG)
            LBJ: LBJ_2519(metG)
            SYN: slr0649(metS)
            SYW: SYNW1222(metG)
            SYC: syc0408_c(metS)
            SYF: Synpcc7942_1142
            SYD: Syncc9605_1334(metG)
            SYE: Syncc9902_1140(metG)
            SYG: sync_1333(metG)
            SYR: SynRCC307_1228(metG)
            SYX: SynWH7803_1128(metG)
            CYA: CYA_1398(metG)
            CYB: CYB_2229(metG)
            TEL: tlr0750(metS)
            GVI: gll3023(metS)
            ANA: all0233
            AVA: Ava_2723(metG)
            PMA: Pro0970(metG)
            PMM: PMM0867(metG)
            PMT: PMT0743(metG)
            PMN: PMN2A_0342
            PMI: PMT9312_0934
            PMB: A9601_09951(metG)
            PMC: P9515_09481(metG)
            PMF: P9303_14741(metG)
            PMG: P9301_09931(metG)
            PMH: P9215_10261
            PME: NATL1_10151(metG)
            TER: Tery_1806
            BTH: BT_2933
            BFR: BF4503
            BFS: BF4297(metG)
            PGI: PG0170(metG)
            SRU: SRU_1557(metG)
            CHU: CHU_2689(metG) CHU_3785(metG)
            GFO: GFO_3100(metG)
            FPS: FP0055(metG)
            CTE: CT0969(metS)
            CCH: Cag_1403
            CPH: Cpha266_1011
            PLT: Plut_1186
            DET: DET0388(metG)
            DEH: cbdb_A334(metG)
            DRA: DR_1433
            DGE: Dgeo_0724
            TTH: TTC0931
            TTJ: TTHA1298
            AAE: aq_1257(metG)
            TMA: TM1085
            MJA: MJ1263(metS)
            MMP: MMP0326(metS)
            MAC: MA4046(metG)
            MBA: Mbar_A0543
            MMA: MM_0867
            MBU: Mbur_1936
            MHU: Mhun_2825
            MTH: MTH587
            MST: Msp_0083(metG)
            MSI: Msm_0071
            MKA: MK0850(metG)
            AFU: AF1453(metS)
            HAL: VNG0326G(metS)
            HMA: rrnAC1800(metS)
            HWA: HQ1572A(metS)
            NPH: NP1192A(metS)
            TAC: Ta1162
            TVO: TVN1220
            PTO: PTO0542
            PHO: PH0993
            PAB: PAB2364(metS)
            PFU: PF1030
            TKO: TK1049
            RCI: RRC417(metS)
            APE: APE_1129
            SSO: SSO0558(metS)
            STO: ST1432
            SAI: Saci_1544
            MSE: Msed_1913
            PAI: PAE2940
            NEQ: NEQ457
STRUCTURES  PDB: 1A8H  1F4L  1MEA  1MED  1MKH  1P7P  1PFU  1PFV  1PFW  1PFY  
                 1PG0  1PG2  1QQT  1RQG  1WOY  2CSX  2CT8  2D54  2D5B  2DJV  
                 2HSN  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.10
            ExPASy - ENZYME nomenclature database: 6.1.1.10
            ExplorEnz - The Enzyme Database: 6.1.1.10
            ERGO genome analysis and discovery system: 6.1.1.10
            BRENDA, the Enzyme Database: 6.1.1.10
            CAS: 9033-22-1
///
ENTRY       EC 6.1.1.11                 Enzyme
NAME        serine---tRNA ligase;
            seryl-tRNA synthetase;
            SerRS;
            seryl-transfer ribonucleate synthetase;
            seryl-transfer RNA synthetase;
            seryl-transfer ribonucleic acid synthetase;
            serine translase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-serine:tRNASer ligase (AMP-forming)
REACTION    ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer
            [RN:R03662]
ALL_REAC    R03662
SUBSTRATE   ATP [CPD:C00002];
            L-serine [CPD:C00065];
            tRNA(Ser) [CPD:C01650]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-seryl-tRNA(Ser) [CPD:C02553]
COMMENT     This enzyme also recognizes tRNASec, the special tRNA for
            selenocysteine, and catalyses the formation of L-seryl-tRNASec, the
            substrate for EC 2.9.1.1, L-seryl-tRNASec selenium transferase.
REFERENCE   1  [PMID:4906848]
  AUTHORS   Katze JR, Konigsberg W.
  TITLE     Purification and properties of seryl transfer ribonucleic acid
            synthetase from Escherichia coli.
  JOURNAL   J. Biol. Chem. 245 (1970) 923-30.
REFERENCE   2
  AUTHORS   Makman, M.H. and Cantoni, G.L.
  TITLE     Isolation of seryl and phenylalanyl ribonucleic acid synthetases
            from baker's yeast.
  JOURNAL   Biochemistry 4 (1965) 1434-1442.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Webster, L.T. and Davie, E.W.
  TITLE     Purification and properties of serine-activating enzyme from beef
            pancreas.
  JOURNAL   J. Biol. Chem. 236 (1961) 479-484.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:7986071]
  AUTHORS   Ohama T, Yang DC, Hatfield DL.
  TITLE     Selenocysteine tRNA and serine tRNA are aminoacylated by the same
            synthetase, but may manifest different identities with respect to
            the long extra arm.
  JOURNAL   Arch. Biochem. Biophys. 315 (1994) 293-301.
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01875  seryl-tRNA synthetase
GENES       HSA: 54938(SARS2) 6301(SARS)
            MCC: 695081(SARS2)
            MMU: 20226(Sars) 71984(Sars2)
            CFA: 484518(SARS2) 490124(SARS)
            BTA: 281476(SARS) 282060(SARS2)
            GGA: 426697(RCJMB04_2o24)
            XLA: 380179(sars)
            XTR: 407933(sars1)
            DRE: 394154(sars2)
            SPU: 579912(LOC579912) 583727(LOC583727) 588782(LOC588782)
            DME: Dmel_CG17259 Dmel_CG4938(Aats-ser)
            CEL: C47E12.1(srs-2) W03B1.4(srs-1)
            ATH: AT5G27470
            OSA: 4324679 4331954 4350906
            CME: CMK097C CMN178C
            SCE: YDR023W(SES1) YHR011W(DIA4)
            AGO: AGOS_ABL088C AGOS_AFR412C
            PIC: PICST_60912(DIA4) PICST_77516(SES1)
            CGR: CAGL0E04400g CAGL0K11726g
            SPO: SPAC25B8.06c SPAC29A4.15
            ANI: AN8867.2
            AFM: AFUA_3G12640 AFUA_5G05490
            AOR: AO090005000706 AO090009000712
            CNE: CNB00380 CND05490
            UMA: UM00865.1
            ECU: ECU04_0750
            DDI: DDB_0231305(serS) DDB_0231306(mserS)
            PFA: PF07_0073 PFL0770w
            CPV: cgd8_4720
            CHO: Chro.80542
            TAN: TA03465 TA19195
            TPV: TP01_0161
            TET: TTHERM_00114360
            TBR: Tb11.02.5020
            TCR: 506777.80
            LMA: LmjF11.0100
            EHI: 204.t00006
            ECO: b0893(serS)
            ECJ: JW0876(serS)
            ECE: Z1239(serS)
            ECS: ECs0978
            ECC: c1030(serS)
            ECI: UTI89_C0908(serS)
            ECP: ECP_0907
            ECV: APECO1_1196(serS)
            ECW: EcE24377A_0968(serS)
            ECX: EcHS_A0998(serS)
            STY: STY0961(serS)
            STT: t1971(serS)
            SPT: SPA1835(serS)
            SEC: SC0917(serS)
            STM: STM0963(serS)
            YPE: YPO1379(serS)
            YPK: y2796(serS)
            YPM: YP_1214(serS)
            YPA: YPA_0669
            YPN: YPN_2601
            YPP: YPDSF_2316
            YPS: YPTB1404(serS)
            YPI: YpsIP31758_2593(serS)
            YEN: YE1528(serS)
            SFL: SF0852(serS)
            SFX: S0893(serS)
            SFV: SFV_0884(serS)
            SSN: SSON_0894(serS)
            SBO: SBO_0826(serS)
            SDY: SDY_2368(serS)
            ECA: ECA2644(serS)
            PLU: plu1604(serS)
            BUC: BU313(serS)
            BAS: BUsg303(serS)
            BAB: bbp290(serS)
            BCC: BCc_193(serS)
            WBR: WGLp489(serS)
            SGL: SG1111
            ENT: Ent638_1417
            KPN: KPN_00925(serS)
            SPE: Spro_1686
            BFL: Bfl384(serS)
            BPN: BPEN_395(serS)
            HIN: HI0110(serS)
            HIT: NTHI0200(serS)
            HIP: CGSHiEE_02770
            HDU: HD1133(serS)
            HSO: HS_1075(serS)
            PMU: PM0258(serS)
            MSU: MS1450(serS)
            APL: APL_0868(serS)
            XFA: XF2286
            XFT: PD1318(serS)
            XCC: XCC1594(serS)
            XCB: XC_2640
            XCV: XCV1694(serS)
            XAC: XAC1653(serS)
            XOO: XOO2116(serS)
            XOM: XOO_1988(XOO1988)
            VCH: VC1110
            VCO: VC0395_A0628(serS)
            VVU: VV1_2946
            VVY: VV1325
            VPA: VP1108
            VFI: VF0908
            PPR: PBPRA1165(serS)
            PAE: PA2612(serS)
            PAU: PA14_30330(serS)
            PAP: PSPA7_2596(serS)
            PPU: PP_4000(serS)
            PPF: Pput_1833
            PST: PSPTO_3345(serS)
            PSB: Psyr_3175
            PSP: PSPPH_3089(serS)
            PFL: PFL_3876(serS)
            PFO: Pfl_3582
            PEN: PSEEN2216(serS)
            PMY: Pmen_2384
            PAR: Psyc_1618(serS)
            PCR: Pcryo_1850
            PRW: PsycPRwf_1539
            ACI: ACIAD2935(serS)
            SON: SO_2310(serS)
            SDN: Sden_1747
            SFR: Sfri_1799
            SAZ: Sama_1776
            SBL: Sbal_2160
            SBM: Shew185_2211
            SLO: Shew_2020
            SPC: Sputcn32_2007
            SSE: Ssed_2131
            SPL: Spea_2229
            SHE: Shewmr4_1967
            SHM: Shewmr7_2009
            SHN: Shewana3_2054
            SHW: Sputw3181_2005
            ILO: IL0663(serS)
            CPS: CPS_2755(serS)
            PHA: PSHAa1712(serS)
            PAT: Patl_2456
            SDE: Sde_1697
            PIN: Ping_1666
            MAQ: Maqu_1547
            CBU: CBU_1188(serS)
            CBD: COXBU7E912_1278(serS)
            LPN: lpg0513(serS)
            LPF: lpl0551(serS)
            LPP: lpp0575(serS)
            MCA: MCA1971(serS)
            FTU: FTT1330(serS)
            FTF: FTF1330(serS)
            FTW: FTW_1496(serS)
            FTL: FTL_1491
            FTH: FTH_1445(serS)
            FTA: FTA_1576(serS)
            FTN: FTN_0647(serS)
            TCX: Tcr_0768
            NOC: Noc_1036
            AEH: Mlg_1699
            HHA: Hhal_1392
            HCH: HCH_02449(serS)
            CSA: Csal_2315
            ABO: ABO_1294(serS)
            AHA: AHA_1868(serS)
            DNO: DNO_1065(serS)
            BCI: BCI_0318(serS)
            CRP: CRP_084
            VOK: COSY_0904(serS)
            NME: NMB1684
            NMA: NMA1943(serS)
            NMC: NMC1602(serS)
            NGO: NGO1335
            CVI: CV_1375(serS)
            RSO: RSc2337(serS)
            REU: Reut_A2594
            REH: H16_A0764(serS1) H16_B0015(serS2)
            RME: Rmet_0695
            BMA: BMA2118(serS)
            BMV: BMASAVP1_A0794(serS)
            BML: BMA10299_A2626(serS)
            BMN: BMA10247_1986(serS)
            BXE: Bxe_A3435
            BVI: Bcep1808_0895
            BUR: Bcep18194_A4082
            BCN: Bcen_0500
            BCH: Bcen2424_0979
            BAM: Bamb_0839
            BPS: BPSL2600(serS)
            BPM: BURPS1710b_3072(serS)
            BPL: BURPS1106A_3038(serS)
            BPD: BURPS668_2986(serS)
            BTE: BTH_I1565(serS)
            PNU: Pnuc_0692
            BPE: BP2470
            BPA: BPP3459
            BBR: BB3908
            RFR: Rfer_3243
            POL: Bpro_0953
            MPT: Mpe_A2692
            HAR: HEAR1022(serS)
            MMS: mma_1157(serS)
            NEU: NE0180(serS)
            NET: Neut_0263
            NMU: Nmul_A0180
            EBA: ebA7034(serS)
            AZO: azo1369
            DAR: Daro_1300
            TBD: Tbd_1229
            MFA: Mfla_1129
            HPY: HP1480
            HPJ: jhp1373(serS)
            HPA: HPAG1_1433
            HHE: HH1490(serS)
            HAC: Hac_1740(serS)
            WSU: WS0872(serS)
            TDN: Tmden_1667
            CJE: Cj0389(serS)
            CJR: CJE0438(serS)
            CJJ: CJJ81176_0412(serS)
            CJU: C8J_0364(serS)
            CJD: JJD26997_1569(serS)
            CFF: CFF8240_1342(serS)
            CCV: CCV52592_0770 CCV52592_1189(serS)
            CHA: CHAB381_0210(serS) CHAB381_0755
            CCO: CCC13826_0671 CCC13826_0773(serS)
            ABU: Abu_0345(serS)
            NIS: NIS_1379(serS)
            SUN: SUN_1957(serS)
            GSU: GSU0037(serS)
            GME: Gmet_3528
            GUR: Gura_0287
            PCA: Pcar_0326
            PPD: Ppro_0616
            DVU: DVU0237(serS)
            DDE: Dde_0196
            LIP: LI0114(serS)
            BBA: Bd0077(serS)
            DPS: DP1764
            ADE: Adeh_3853
            MXA: MXAN_1941(serS)
            SAT: SYN_00102
            SFU: Sfum_1424
            RPR: RP783
            RTY: RT0770(serS)
            RCO: RC1216(serS)
            RFE: RF_1249(serS)
            RBE: RBE_0079(serS)
            RAK: A1C_06075
            RBO: A1I_07550
            RCM: A1E_05030
            RRI: A1G_06665
            OTS: OTBS_1037(serS)
            WOL: WD0028(serS)
            WBM: Wbm0464
            AMA: AM759(serS)
            APH: APH_0427(serS)
            ERU: Erum4540(serS)
            ERW: ERWE_CDS_04760(serS)
            ERG: ERGA_CDS_04660(serS)
            ECN: Ecaj_0454
            ECH: ECH_0584(serS-1)
            NSE: NSE_0569(serS)
            PUB: SAR11_0978(serS)
            MLO: mll1081
            MES: Meso_1803
            PLA: Plav_3030
            SME: SMc02064(serS)
            SMD: Smed_1167
            ATU: Atu1703(serS)
            ATC: AGR_C_3129
            RET: RHE_CH01826(serS) RHE_CH04045(ypch01429)
            RLE: RL2049(serS) RL4595
            BME: BMEI1082
            BMF: BAB1_0904(serS)
            BMS: BR0885(serS)
            BMB: BruAb1_0897(serS)
            BOV: BOV_0876(serS)
            OAN: Oant_2342
            BJA: bll4748(serS)
            BRA: BRADO4044(serS)
            BBT: BBta_4414(serS)
            RPA: RPA2845(serS) RPA4597
            RPB: RPB_0993 RPB_2742
            RPC: RPC_2517
            RPD: RPD_2787
            RPE: RPE_2700
            NWI: Nwi_1776
            NHA: Nham_1791
            BHE: BH05610(serS)
            BQU: BQ04770(serS)
            BBK: BARBAKC583_0519(serS)
            XAU: Xaut_4404
            CCR: CC_1999
            SIL: SPO2325(serS)
            SIT: TM1040_0994
            RSP: RSP_1795(serS)
            RSH: Rsph17029_0441
            RSQ: Rsph17025_0453
            JAN: Jann_1070
            RDE: RD1_2541(serS)
            PDE: Pden_2429
            MMR: Mmar10_1906
            HNE: HNE_1930(serS)
            ZMO: ZMO0986(serS)
            NAR: Saro_0850
            SAL: Sala_0722
            SWI: Swit_0637
            ELI: ELI_00610
            GOX: GOX1759
            GBE: GbCGDNIH1_1252
            ACR: Acry_0957
            RRU: Rru_A1770
            MAG: amb2521
            MGM: Mmc1_1073
            ABA: Acid345_0391
            SUS: Acid_2483
            BSU: BG10077(serS)
            BHA: BH0024(serS)
            BAN: BA0012(serS)
            BAR: GBAA0012(serS)
            BAA: BA_0607
            BAT: BAS0015
            BCE: BC0017
            BCA: BCE_0013(serS)
            BCZ: BCZK0013(serS)
            BTK: BT9727_0013(serS)
            BTL: BALH_0013(serS)
            BLI: BL02355(serS)
            BLD: BLi00018(serS)
            BCL: ABC0013(serS) ABC1428
            BAY: RBAM_000160(serS)
            BPU: BPUM_0509(serS)
            OIH: OB0012
            GKA: GK0013(serS)
            SAU: SA0009(serS)
            SAV: SAV0009(serS)
            SAM: MW0009(serS)
            SAR: SAR0009(serS)
            SAS: SAS0009
            SAC: SACOL0009(serS)
            SAB: SAB0009(serS)
            SAA: SAUSA300_0009(serS)
            SAO: SAOUHSC_00009
            SAJ: SaurJH9_0009
            SAH: SaurJH1_0009
            SEP: SE0007
            SER: SERP2545(serS)
            SHA: SH0008(serS)
            SSP: SSP0009
            LMO: lmo2747(serS)
            LMF: LMOf2365_2734(serS)
            LIN: lin2890(serS)
            LWE: lwe2695(serS)
            LLA: L150515(serS)
            LLC: LACR_1870
            LLM: llmg_0722(serS)
            SPY: SPy_1742(serS)
            SPZ: M5005_Spy_1483(serS)
            SPM: spyM18_1814(serS)
            SPG: SpyM3_1516(serS)
            SPS: SPs0350
            SPH: MGAS10270_Spy1550(serS)
            SPI: MGAS10750_Spy1542(serS)
            SPJ: MGAS2096_Spy1510(serS)
            SPK: MGAS9429_Spy1485(serS)
            SPF: SpyM50362(serS)
            SPA: M6_Spy1477
            SPB: M28_Spy1472(serS)
            SPN: SP_0411
            SPR: spr0372(serS)
            SPD: SPD_0375(serS)
            SAG: SAG0356(serS)
            SAN: gbs0343(serS)
            SAK: SAK_0430(serS)
            SMU: SMU.1886(sys)
            STC: str0329(serS)
            STL: stu0329(serS)
            SSA: SSA_1925(serS)
            SGO: SGO_1683(serS)
            LPL: lp_0501(serS1) lp_1012(serS2)
            LJO: LJ0671 LJ0676
            LAC: LBA1626
            LSA: LSA1803(serS)
            LSL: LSL_0189(serS)
            LDB: Ldb1882(serS)
            LBU: LBUL_1748
            LBR: LVIS_1710
            LCA: LSEI_1836
            LRE: Lreu_0097
            EFA: EF0100(serS-1) EF3292(serS-2)
            OOE: OEOE_0440
            STH: STH10(serS)
            CAC: CAC0017(serS) CAC0021(serS)
            CPE: CPE0014(serS)
            CPF: CPF_0014(serS)
            CPR: CPR_0014(serS)
            CTC: CTC00081
            CNO: NT01CX_0848(serS)
            CTH: Cthe_2381
            CDF: CD0014(serS1) CD2840(serS2)
            CBO: CBO0016(serS) CBO0510(serS)
            CBA: CLB_0022(serS-1) CLB_0551(serS-2)
            CBH: CLC_0024(serS-1) CLC_0584(serS-2)
            CBF: CLI_0026(serS-1) CLI_0591(serS-2)
            CBE: Cbei_1431
            CKL: CKL_0018(serS)
            AMT: Amet_0024
            CHY: CHY_2697(serS)
            DSY: DSY0008(serS)
            DRM: Dred_0015
            SWO: Swol_0010
            CSC: Csac_1456
            TTE: TTE0025(serS)
            MTA: Moth_0021
            MGE: MG_005(serS)
            MPN: MPN005(serS)
            MPU: MYPU_0340(serS)
            MPE: MYPE4060(serS)
            MGA: MGA_0608(serS)
            MMY: MSC_0066(serS)
            MMO: MMOB0920(serS)
            MHY: mhp128(serS)
            MHJ: MHJ_0243(serS)
            MHP: MHP7448_0251(serS)
            MSY: MS53_0591(serS)
            MCP: MCAP_0839(serS)
            UUR: UU106(serS)
            POY: PAM083(serS)
            AYW: AYWB_632(serS)
            MFL: Mfl017
            MTU: Rv3834c(serS)
            MTC: MT3942(serS)
            MBO: Mb3864c(serS)
            MBB: BCG_3897c(serS)
            MLE: ML0082(serS)
            MPA: MAP0197(serS)
            MAV: MAV_0194(serS)
            MSM: MSMEG_6413(serS)
            MVA: Mvan_5659
            MGI: Mflv_1150
            MMC: Mmcs_5029
            MKM: Mkms_5117
            MJL: Mjls_5410
            CGL: NCgl2793(cgl2893)
            CGB: cg3201(serS)
            CEF: CE2724
            CDI: DIP2240(serS)
            CJK: jk0123(serS)
            NFA: nfa1400(serS)
            RHA: RHA1_ro04041(serS)
            SCO: SCO3961(SCD78.28c)
            SMA: SAV2294(serS2) SAV4244(serS1)
            TWH: TWT726(serS)
            TWS: TW740(serS)
            LXX: Lxx02390(serS)
            ART: Arth_0140
            AAU: AAur_0103(serS)
            PAC: PPA2219
            NCA: Noca_0174
            TFU: Tfu_0031
            FRA: Francci3_1382
            FAL: FRAAL2153(serS)
            ACE: Acel_2104
            KRA: Krad_0249
            SEN: SACE_0158(serS)
            STP: Strop_3397
            BLO: BL1635(serS)
            BAD: BAD_0369
            RXY: Rxyl_1086
            FNU: FN0110
            RBA: RB1039(serS)
            CTR: CT729(serS)
            CTA: CTA_0791(serS)
            CMU: TC0102
            CPN: CPn0870(serS)
            CPA: CP0999
            CPJ: CPj0870(serS)
            CPT: CpB0899
            CCA: CCA00897(serS)
            CAB: CAB865(serS)
            CFE: CF0117(serS)
            PCU: pc1488(serS)
            BGA: BG0229(serS)
            BAF: BAPKO_0234(serS)
            TPA: TP0647
            TDE: TDE2307(serS)
            LIL: LA4339(serS)
            LIC: LIC13480(serS)
            LBJ: LBJ_0024(serS)
            LBL: LBL_2978(serS)
            SYN: slr1703(serS)
            SYW: SYNW1894(serRS)
            SYC: syc1069_d(serS)
            SYF: Synpcc7942_0449
            SYD: Syncc9605_0573
            SYE: Syncc9902_1791
            SYG: sync_2091(serS)
            SYR: SynRCC307_0547(serS)
            SYX: SynWH7803_1905(serS)
            CYA: CYA_0247(serS)
            CYB: CYB_1790(serS)
            TEL: tlr1552(serS)
            GVI: glr0716(serS)
            ANA: all3976(serS)
            AVA: Ava_1724
            PMA: Pro1304(serS)
            PMM: PMM1188(serS)
            PMT: PMT1374(serRS)
            PMN: PMN2A_0807
            PMI: PMT9312_1289
            PMB: A9601_13811(serS)
            PMC: P9515_13601(serS)
            PMF: P9303_06061(serS)
            PMG: P9301_13891(serS)
            PMH: P9215_14021(serS)
            PME: NATL1_16621(serS)
            TER: Tery_3523
            BTH: BT_4312
            BFR: BF1007
            BFS: BF0928(serS)
            PGI: PG0316(serS)
            SRU: SRU_1855(serS)
            CHU: CHU_3604(serS)
            GFO: GFO_3506(serS)
            FJO: Fjoh_0847
            FPS: FP0072(serS)
            CTE: CT0606(serS)
            CCH: Cag_0695
            CPH: Cpha266_1765
            PVI: Cvib_1182
            PLT: Plut_0594
            DET: DET0577(serS)
            DEH: cbdb_A554(serS)
            DEB: DehaBAV1_0550
            RRS: RoseRS_3466
            RCA: Rcas_1494
            DRA: DR_1276
            DGE: Dgeo_0934
            TTH: TTC0520
            TTJ: TTHA0875
            AAE: aq_298(serS)
            TMA: TM1379
            TPT: Tpet_1404
            TME: Tmel_0253
            FNO: Fnod_1518
            MMP: MMP0879(serS)
            MAC: MA4048(serS)
            MBA: Mbar_A0541 Mbar_A2126
            MMA: MM_0865
            MBU: Mbur_2337
            MHU: Mhun_2507
            MEM: Memar_0811
            MST: Msp_1277(serS)
            MSI: Msm_1710
            MKA: MK1460(serS)
            HAL: VNG2072G(serS)
            HMA: rrnAC2808(serS)
            HWA: HQ3138A(serS)
            NPH: NP1692A(serS)
            TAC: Ta0468
            TVO: TVN0987
            PTO: PTO1232
            PHO: PH0710
            PAB: PAB0881(serS)
            PFU: PF1204
            TKO: TK1140
            RCI: LRC224(serS)
            APE: APE_1976.1
            SMR: Smar_1354
            IHO: Igni_0990
            HBU: Hbut_1249
            SSO: SSO0602(serS)
            STO: ST1469
            SAI: Saci_1584
            MSE: Msed_1952
            PAI: PAE3158
            PIS: Pisl_0528
            PCL: Pcal_1802
            PAS: Pars_1667
            TPE: Tpen_0408
            NEQ: NEQ308
STRUCTURES  PDB: 1SER  1SES  1SET  1SRY  1WLE  2CIM  2CJ9  2CJA  2CJB  2DQ0  
                 2DQ1  2DQ2  2DQ3  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.11
            ExPASy - ENZYME nomenclature database: 6.1.1.11
            ExplorEnz - The Enzyme Database: 6.1.1.11
            ERGO genome analysis and discovery system: 6.1.1.11
            BRENDA, the Enzyme Database: 6.1.1.11
            CAS: 9023-48-7
///
ENTRY       EC 6.1.1.12                 Enzyme
NAME        aspartate---tRNA ligase;
            aspartyl-tRNA synthetase;
            aspartyl ribonucleic synthetase;
            aspartyl-transfer RNA synthetase;
            aspartic acid translase;
            aspartyl-transfer ribonucleic acid synthetase;
            aspartyl ribonucleate synthetase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-aspartate:tRNAAsp ligase (AMP-forming)
REACTION    ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp
            [RN:R05577]
ALL_REAC    R05577
SUBSTRATE   ATP [CPD:C00002];
            L-aspartate [CPD:C00049];
            tRNA(Asp) [CPD:C01638]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-aspartyl-tRNA(Asp) [CPD:C02984]
REFERENCE   1  [PMID:4575961]
  AUTHORS   Gangloff J, Dirheimer G.
  TITLE     Studies on aspartyl-tRNA synthetase from Baker's yeast. I.
            Purification and properties of the enzyme.
  JOURNAL   Biochim. Biophys. Acta. 294 (1973) 263-72.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   2  [PMID:13939000]
  AUTHORS   NORTON SJ, RAVEL JM, LEE C, SHIVE W.
  TITLE     Purification and properties of the aspartyl ribonucleic acid
            synthetase of Lactobacillus arabinosus.
  JOURNAL   J. Biol. Chem. 238 (1963) 269-74.
  ORGANISM  Lactobacillus arabinosus
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01876  aspartyl-tRNA synthetase
GENES       HSA: 1615(DARS) 55157(DARS2)
            PTR: 469591(DARS2)
            MMU: 226414(Dars) 226539(Dars2)
            RNO: 116483(Dars)
            CFA: 476132(DARS) 490337(DARS2)
            GGA: 424296(DARS) 424408(DARS2)
            XLA: 380028(dars) 443916(MGC80207)
            XTR: 394926(dars)
            SPU: 588558(LOC588558)
            DME: Dmel_CG3821(Aats-asp)
            CEL: B0464.1(drs-1) F10C2.6(drs-2)
            ATH: AT4G26870
            OSA: 4324505 4330354
            CME: CMJ218C CMK087C
            SCE: YLL018C(DPS1) YPL104W(MSD1)
            AGO: AGOS_ADL039C AGOS_AGR206C
            PIC: PICST_61618(MSD1) PICST_77216(DPS1)
            CGR: CAGL0D06556g CAGL0H05907g
            SPO: SPCC1223.07c SPCC736.06
            ANI: AN1710.2 AN4550.2
            AFM: AFUA_1G02570 AFUA_2G02590 AFUA_4G08330 AFUA_8G00100
            AOR: AO090023000726 AO090026000603
            CNE: CND06300
            UMA: UM06411.1
            ECU: ECU06_0790
            DDI: DDB_0231308(aspS1) DDB_0231311(maspS)
            PFA: MAL1P1.20 PFE0715w
            CHO: Chro.70181
            TAN: TA04845
            TPV: TP03_0489
            TET: TTHERM_00592750 TTHERM_00616050
            TBR: Tb927.6.1880
            TCR: 509967.30 510777.20
            LMA: LmjF30.0460
            EHI: 262.t00004
            ECO: b1866(aspS)
            ECJ: JW1855(aspS)
            ECE: Z2919(aspS)
            ECS: ECs2576
            ECC: c2280(aspS)
            ECI: UTI89_C2070(aspS)
            ECP: ECP_1810
            ECV: APECO1_916(aspS)
            ECW: EcE24377A_2096(aspS)
            ECX: EcHS_A1959
            STY: STY2109(aspS)
            STT: t0976(aspS)
            SPT: SPA0968(aspS)
            SEC: SC1909(aspS)
            STM: STM1901(aspS)
            YPE: YPO2053(aspS)
            YPK: y2258(aspS)
            YPM: YP_1896(aspS)
            YPA: YPA_1435
            YPN: YPN_1530
            YPS: YPTB2036(aspS)
            YPI: YpsIP31758_2035(aspS)
            SFL: SF1876(aspS)
            SFX: S1942(aspS)
            SFV: SFV_1868(aspS)
            SSN: SSON_1275(aspS)
            SBO: SBO_1189(aspS)
            SDY: SDY_1153(aspS)
            ECA: ECA2496(aspS)
            PLU: plu2107(aspS)
            BUC: BU316(aspS)
            BAS: BUsg306(aspS)
            BAB: bbp293(aspS)
            BCC: BCc_196(aspS)
            WBR: WGLp113(aspS)
            SGL: SG1257
            BFL: Bfl452(aspS)
            BPN: BPEN_467(aspS)
            HIN: HI0317(aspS)
            HIT: NTHI0435(aspS)
            HIP: CGSHiEE_01470(aspS)
            HDU: HD0599(aspS)
            HSO: HS_1223(aspS)
            PMU: PM0983(aspS)
            MSU: MS0708(aspS)
            APL: APL_1149(aspS)
            XFA: XF1856
            XFT: PD0946(aspS)
            XCC: XCC3030(aspS)
            XCB: XC_1128
            XCV: XCV3286(aspS)
            XAC: XAC3154(aspS)
            XOO: XOO1656(aspS)
            XOM: XOO_1540(XOO1540)
            VCH: VC1166
            VCO: VC0395_A0735(aspS)
            VVU: VV1_2156
            VVY: VV2288
            VPA: VP1047
            VFI: VF0949
            PPR: PBPRA1112
            PAE: PA0963(aspS)
            PAU: PA14_51820(aspS)
            PAP: PSPA7_4545(aspS)
            PPU: PP_1213(aspS)
            PST: PSPTO_3981(aspS)
            PSB: Psyr_1406
            PSP: PSPPH_3776(aspS)
            PFL: PFL_4767(aspS)
            PFO: Pfl_4411
            PEN: PSEEN4096(aspS)
            PAR: Psyc_1203(aspS)
            PCR: Pcryo_1183
            ACI: ACIAD0609(aspS)
            ACB: A1S_2894
            SON: SO_2433(aspS)
            SDN: Sden_1887
            SFR: Sfri_2184
            SAZ: Sama_1843
            SBL: Sbal_2038
            SLO: Shew_2079
            SHE: Shewmr4_1898
            SHM: Shewmr7_2080
            SHN: Shewana3_1953
            SHW: Sputw3181_2073
            ILO: IL1089(aspS)
            CPS: CPS_2114(aspS)
            PHA: PSHAa1938(aspS)
            PAT: Patl_2948
            SDE: Sde_0913
            PIN: Ping_0699
            MAQ: Maqu_1707
            CBU: CBU_1565(aspS)
            CBD: COXBU7E912_0423(aspS)
            LPN: lpg1478
            LPF: lpl1550(aspS)
            LPP: lpp1434(aspS)
            MCA: MCA1776(aspS)
            FTU: FTT0007(aspS)
            FTF: FTF0007(aspS)
            FTW: FTW_1997(aspS)
            FTL: FTL_0020
            FTH: FTH_0020(aspS)
            FTA: FTA_0024(aspS)
            FTN: FTN_0129(aspS)
            TCX: Tcr_0890
            NOC: Noc_0302
            AEH: Mlg_2665
            HHA: Hhal_2226
            HCH: HCH_04927(aspS)
            CSA: Csal_1844
            ABO: ABO_0749(aspS)
            AHA: AHA_1521(aspS)
            DNO: DNO_1118(aspS)
            BCI: BCI_0315(aspS)
            CRP: CRP_075
            VOK: COSY_0367(aspS)
            NME: NMB0466
            NMA: NMA2019(aspS)
            NMC: NMC1684(aspS)
            NGO: NGO1489 NGO1490
            CVI: CV_3740(aspS)
            RSO: RSc0466(aspS)
            REU: Reut_A0439
            REH: H16_A0453(aspS)
            RME: Rmet_0378
            BMA: BMA0193(aspS)
            BMV: BMASAVP1_A2752(aspS)
            BML: BMA10299_A2326(aspS)
            BMN: BMA10247_2406(aspS)
            BXE: Bxe_A4043
            BUR: Bcep18194_A6052
            BCN: Bcen_2113
            BCH: Bcen2424_2725
            BAM: Bamb_2776
            BPS: BPSL0644(aspS)
            BPM: BURPS1710b_0852(aspS)
            BPL: BURPS1106A_0691(aspS)
            BPD: BURPS668_0675(aspS)
            BTE: BTH_I0560(aspS)
            BPE: BP0709(aspS)
            BPA: BPP0115(aspS)
            BBR: BB0115(aspS)
            RFR: Rfer_1297
            POL: Bpro_0866
            PNA: Pnap_0787
            MPT: Mpe_A1070
            HAR: HEAR2844(aspS)
            MMS: mma_3099
            NEU: NE2252
            NET: Neut_0616
            NMU: Nmul_A0603
            EBA: ebA4339(aspS)
            AZO: azo3239(aspS)
            DAR: Daro_0634
            TBD: Tbd_0442
            MFA: Mfla_2384
            HPY: HP0617
            HPJ: jhp0560(aspS)
            HPA: HPAG1_0598
            HHE: HH1801(aspS)
            HAC: Hac_0833(aspS)
            WSU: WS1781(aspS)
            TDN: Tmden_1086
            CJE: Cj0640c(aspS)
            CJR: CJE0743(aspS)
            CJJ: CJJ81176_0668(aspS)
            CJU: C8J_0599(aspS)
            CJD: JJD26997_1359(aspS)
            CFF: CFF8240_1196(aspS)
            CHA: CHAB381_0296(aspS)
            CCO: CCC13826_1981(aspS)
            ABU: Abu_0776(aspS)
            NIS: NIS_0771(aspS)
            SUN: SUN_1506(aspS)
            GSU: GSU1463(aspS)
            GME: Gmet_1357
            PCA: Pcar_1040
            DVU: DVU3367(aspS)
            DDE: Dde_0012
            LIP: LI0987(aspS)
            BBA: Bd3311(aspS)
            DPS: DP0570
            ADE: Adeh_2533
            MXA: MXAN_4684(aspS)
            SAT: SYN_02535 SYN_02602
            SFU: Sfum_3302 Sfum_3365
            RPR: RP145
            RTY: RT0134(aspS)
            RCO: RC0187(aspS)
            RFE: RF_1138(aspS)
            RBE: RBE_0349(aspS)
            RAK: A1C_01040(aspS)
            RBO: A1I_06025(aspS)
            RCM: A1E_00750(aspS)
            RRI: A1G_01065(aspS)
            OTS: OTBS_0206(aspS)
            WOL: WD0413(aspS)
            WBM: Wbm0012
            APH: APH_0190(aspS)
            ERU: Erum6660(aspS)
            ERW: ERWE_CDS_06980(aspS)
            ERG: ERGA_CDS_06890(aspS)
            ECN: Ecaj_0672
            ECH: ECH_0334(aspS)
            NSE: NSE_0477(aspS)
            PUB: SAR11_0722(aspS)
            MLO: mlr8358
            MES: Meso_1122
            SME: SMc01756(aspS)
            ATU: Atu1153
            ATC: AGR_C_2136
            RET: RHE_CH01497(aspS)
            RLE: RL1605(aspS)
            BME: BMEI1202
            BMF: BAB1_0775(aspS)
            BMS: BR0751(aspS)
            BMB: BruAb1_0768(aspS)
            BOV: BOV_0745(aspS)
            BJA: blr4143
            BRA: BRADO3359(aspS)
            BBT: BBta_3864(aspS)
            RPA: RPA3043(aspS)
            RPB: RPB_2496
            RPC: RPC_2336
            RPD: RPD_2947
            RPE: RPE_3276
            NWI: Nwi_1588
            NHA: Nham_2111
            BHE: BH09790(aspS)
            BQU: BQ07550(aspS)
            BBK: BARBAKC583_0868(aspS)
            CCR: CC_1892
            SIL: SPO0926(aspS)
            SIT: TM1040_0635
            RSP: RSP_0815(aspS)
            JAN: Jann_3166
            RDE: RD1_1176(aspS)
            MMR: Mmar10_1258
            HNE: HNE_2257(aspS)
            ZMO: ZMO0715(aspS)
            NAR: Saro_1338
            SAL: Sala_1751
            ELI: ELI_03965
            GOX: GOX1747 GOX2249
            GBE: GbCGDNIH1_0212
            RRU: Rru_A2072
            MAG: amb2837
            MGM: Mmc1_0942
            ABA: Acid345_1204
            BSU: BG12572(aspS)
            BHA: BH1252(aspS)
            BAN: BA4632(aspS-2)
            BAR: GBAA4632(aspS-2)
            BAA: BA_5071
            BAT: BAS4297
            BCE: BC4397(aspS)
            BCA: BCE_4485(aspS)
            BCZ: BCZK4145(aspS)
            BTK: BT9727_4135(aspS)
            BTL: BALH_3984(aspS)
            BLI: BL05288(aspS)
            BLD: BLi02881(aspS)
            BCL: ABC1577(aspS)
            BAY: RBAM_024660
            BPU: BPUM_2396
            OIH: OB2019(aspS)
            GKA: GK2572(aspS)
            SAU: SA1456(aspS)
            SAV: SAV1630(aspS)
            SAM: MW1580(aspS)
            SAR: SAR1710(aspS)
            SAS: SAS1566
            SAC: SACOL1685(aspS)
            SAB: SAB1499c(aspS)
            SAA: SAUSA300_1586(aspS)
            SAO: SAOUHSC_01737
            SEP: SE1311
            SER: SERP1192(aspS)
            SHA: SH1291(aspS)
            SSP: SSP1129
            LMO: lmo1519(aspS)
            LMF: LMOf2365_1538(aspS)
            LIN: lin1554(aspS)
            LWE: lwe1532(aspS)
            LLA: L0346(aspS)
            LLC: LACR_2226
            LLM: llmg_2215(aspS)
            SPY: SPy_2156(aspS)
            SPZ: M5005_Spy_1813(aspS)
            SPM: spyM18_2188(aspS)
            SPG: SpyM3_1814(aspS)
            SPS: SPs1812
            SPH: MGAS10270_Spy1905(aspS)
            SPI: MGAS10750_Spy1930(aspS)
            SPJ: MGAS2096_Spy1845(aspS)
            SPK: MGAS9429_Spy1824(aspS)
            SPF: SpyM51788(aspS)
            SPA: M6_Spy1832
            SPB: M28_Spy1822(aspS)
            SPN: SP_2114
            SPR: spr1924(aspS)
            SPD: SPD_1941(aspS)
            SAG: SAG2107(aspS)
            SAN: gbs2060(aspS)
            SAK: SAK_2046(aspS)
            SMU: SMU.1822(gatA) SMU.2101(aspS)
            STC: str1969(aspS)
            STL: stu1969(aspS)
            SSA: SSA_0568 SSA_2270(aspRS2)
            SGO: SGO_0434(aspS-2) SGO_2060(aspS-1)
            LPL: lp_1980(aspS)
            LJO: LJ1391
            LAC: LBA0936
            LSA: LSA0864(aspS)
            LSL: LSL_0853(aspS)
            LDB: Ldb0889(aspS)
            LBU: LBUL_0813
            LBR: LVIS_0736
            LCA: LSEI_1526
            EFA: EF1970(aspS)
            OOE: OEOE_0590
            STH: STH2421(aspS)
            CAC: CAC2269(aspS) CAC3564(asnS)
            CPE: CPE1933(aspS)
            CPF: CPF_2188(aspS)
            CPR: CPR_1899(aspS)
            CTC: CTC02194(aspS)
            CNO: NT01CX_1849(aspS)
            CDF: CD2739(aspS)
            CBO: CBO1019(aspS) CBO3054(aspS)
            CBA: CLB_1059(aspS-1) CLB_3083(aspS-2)
            CBH: CLC_1072(aspS-1) CLC_2956(aspS-2)
            CBF: CLI_1101(aspS-1) CLI_3113(aspS-2)
            CKL: CKL_3126(aspS)
            CHY: CHY_2204(aspS)
            DSY: DSY2431
            SWO: Swol_0812
            TTE: TTE1231(aspS)
            MTA: Moth_1676
            MGE: MG_036(aspS)
            MPN: MPN046(aspS)
            MPU: MYPU_3320(aspS)
            MPE: MYPE2870(aspS)
            MGA: MGA_0948(aspS)
            MMY: MSC_0333(aspS) MSC_0432(aspS)
            MMO: MMOB2740(aspS)
            MHY: mhp137(aspS)
            MHJ: MHJ_0235(aspS)
            MHP: MHP7448_0243(aspS)
            MSY: MS53_0436(aspS)
            MCP: MCAP_0323(aspS)
            UUR: UU286(aspS)
            POY: PAM128(aspS)
            AYW: AYWB_593(aspS)
            MFL: Mfl365
            MTU: Rv2572c(aspS)
            MTC: MT2648(aspS)
            MBO: Mb2602c(aspS)
            MBB: BCG_2595c(aspS)
            MLE: ML0501(aspS)
            MPA: MAP1063(aspS)
            MAV: MAV_3447(aspS)
            MSM: MSMEG_3003(aspS)
            MMC: Mmcs_2308
            CGL: NCgl1573(cgl1635)
            CGB: cg1841(aspS)
            CEF: CE1752
            CDI: DIP1353(aspS)
            CJK: jk1041(aspS)
            NFA: nfa36490(aspS)
            RHA: RHA1_ro07129(aspS)
            SCO: SCO3795(aspS)
            SMA: SAV4395(aspS)
            TWH: TWT754(aspS)
            TWS: TW766(aspS)
            LXX: Lxx01320(aspS)
            CMI: CMM_0561(aspS)
            AAU: AAur_2288(aspS)
            PAC: PPA1175
            TFU: Tfu_2086
            FRA: Francci3_0692
            FAL: FRAAL1202(aspS)
            SEN: SACE_2041(aspS)
            BLO: BL0018(aspS)
            BAD: BAD_0576(aspS)
            RXY: Rxyl_1351
            FNU: FN0299
            RBA: RB8253(aspS)
            CTR: CT542(aspS)
            CTA: CTA_0592(aspS)
            CMU: TC0829
            CPN: CPn0662(aspS)
            CPA: CP0085
            CPJ: CPj0662(aspS)
            CPT: CpB0688
            CCA: CCA00077(aspS)
            CAB: CAB079(aspS)
            CFE: CF0927(aspS)
            PCU: pc0384(aspS)
            BGA: BG0454(aspS)
            BAF: BAPKO_0468(aspS)
            TPA: TP0985
            TDE: TDE1587(aspS)
            LIL: LA1680(aspS)
            LIC: LIC12108(aspS)
            LBJ: LBJ_1198(aspS)
            LBL: LBL_1250(aspS)
            SYN: slr1720(aspS)
            SYW: SYNW2426(aspS)
            SYC: syc0240_c(aspS)
            SYF: Synpcc7942_1313
            SYD: Syncc9605_2595
            SYE: Syncc9902_2233
            SYG: sync_2854(aspS)
            SYR: SynRCC307_2438(aspS)
            SYX: SynWH7803_2458(aspS)
            CYA: CYA_1681(aspS)
            CYB: CYB_1161(aspS)
            TEL: tll1144(aspS)
            GVI: gll1928(aspS)
            ANA: all2436
            AVA: Ava_0247
            PMA: Pro1852(aspS)
            PMM: PMM1688(aspS)
            PMT: PMT2216(aspS)
            PMN: PMN2A_1290
            PMI: PMT9312_1781
            PMB: A9601_18981(aspS)
            PMC: P9515_18791(aspS)
            PMF: P9303_29551(aspS)
            PMG: P9301_18791(aspS)
            PMH: P9215_19611
            PME: NATL1_21621(aspS)
            TER: Tery_2354
            BTH: BT_0872
            BFR: BF2379
            BFS: BF2463(aspS)
            PGI: PG0153(aspS)
            SRU: SRU_1963(aspS)
            CHU: CHU_0111(aspS)
            GFO: GFO_3090(aspS)
            FPS: FP0275(aspS)
            CTE: CT1323(aspS)
            CCH: Cag_0932
            PLT: Plut_1320
            DET: DET0708(aspS)
            DEH: cbdb_A663(aspS)
            DRA: DR_1347
            DGE: Dgeo_1122
            TTH: TTC0359
            TTJ: TTHA0711
            AAE: aq_1677(aspS)
            TMA: TM1441
            MJA: MJ1555(aspS)
            MMP: MMP1616(aspS)
            MAE: Maeo_0028
            MAC: MA1684(aspS)
            MBA: Mbar_A3173
            MMA: MM_0074
            MBU: Mbur_0772
            MTP: Mthe_0623
            MHU: Mhun_2446
            MBN: Mboo_0105
            MST: Msp_0135(aspS)
            MSI: Msm_1236
            MKA: MK0710(asnS)
            HAL: VNG0461G(aspS)
            HMA: rrnAC1657(aspS)
            HWA: HQ1270A(aspS)
            NPH: NP1168A(aspS)
            TAC: Ta0946
            TVO: TVN1090
            PTO: PTO1214
            PHO: PH1020
            PAB: PAB0646(aspS)
            PFU: PF0869
            TKO: TK0492
            RCI: RCIX42(aspS)
            APE: APE_2192.1
            HBU: Hbut_0034
            SSO: SSO0173(aspS)
            STO: ST0205
            SAI: Saci_0768(aspS)
            MSE: Msed_0205
            PAI: PAE0703
            NEQ: NEQ535
STRUCTURES  PDB: 1ASY  1ASZ  1B8A  1C0A  1EFW  1EOV  1EQR  1G51  1IL2  1L0W  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.12
            ExPASy - ENZYME nomenclature database: 6.1.1.12
            ExplorEnz - The Enzyme Database: 6.1.1.12
            ERGO genome analysis and discovery system: 6.1.1.12
            BRENDA, the Enzyme Database: 6.1.1.12
            CAS: 9027-32-1
///
ENTRY       EC 6.1.1.13                 Enzyme
NAME        D-alanine---poly(phosphoribitol) ligase;
            D-alanyl-poly(phosphoribitol) synthetase;
            D-alanine: membrane acceptor ligase;
            D-alanine-D-alanyl carrier protein ligase;
            D-alanine-membrane acceptor ligase;
            D-alanine-activating enzyme
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     D-alanine:poly(phosphoribitol) ligase (AMP-forming)
REACTION    ATP + D-alanine + poly(ribitol phosphate) = AMP + diphosphate +
            O-D-alanyl-poly(ribitol phosphate) [RN:R02718]
ALL_REAC    R02718
SUBSTRATE   ATP [CPD:C00002];
            D-alanine [CPD:C00133];
            poly(ribitol phosphate) [CPD:C00653]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            O-D-alanyl-poly(ribitol phosphate) [CPD:C04260]
COMMENT     A thioester bond is formed transiently between D-alanine and the
            sulfhydryl group of the 4'-phosphopantetheine prosthetic group of
            D-alanyl carrier protein during the activation of the alanine.
            Involved in the synthesis of teichoic acids.
REFERENCE   1  [PMID:13795638]
  AUTHORS   BADDILEY J, NEUHAUS FC.
  TITLE     The enzymic activation of D-alanine.
  JOURNAL   Biochem. J. 75 (1960) 579-87.
  ORGANISM  Lactobacillus casei [GN:lca], Bacillus subtilis [GN:bsu],
            Lactobacillus arabinosus, Staphylococcus aureus
REFERENCE   2  [PMID:4399593]
  AUTHORS   Reusch VM Jr, Neuhaus FC.
  TITLE     D-Alanine: membrane acceptor ligase from Lactobacillus casei.
  JOURNAL   J. Biol. Chem. 246 (1971) 6136-43.
  ORGANISM  Lactobacillus casei [GN:lca]
REFERENCE   3  [PMID:7797557]
  AUTHORS   Perego M, Glaser P, Minutello A, Strauch MA, Leopold K, Fischer W.
  TITLE     Incorporation of D-alanine into lipoteichoic acid and wall teichoic
            acid in Bacillus subtilis. Identification of genes and regulation.
  JOURNAL   J. Biol. Chem. 270 (1995) 15598-606.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   4  [PMID:8300523]
  AUTHORS   Heaton MP, Neuhaus FC.
  TITLE     Role of the D-alanyl carrier protein in the biosynthesis of
            D-alanyl-lipoteichoic acid.
  JOURNAL   J. Bacteriol. 176 (1994) 681-90.
  ORGANISM  Lactobacillus casei [GN:lca]
REFERENCE   5  [PMID:8682792]
  AUTHORS   Debabov DV, Heaton MP, Zhang Q, Stewart KD, Lambalot RH, Neuhaus FC.
  TITLE     The D-Alanyl carrier protein in Lactobacillus casei: cloning,
            sequencing, and expression of dltC.
  JOURNAL   J. Bacteriol. 178 (1996) 3869-76.
  ORGANISM  Lactobacillus casei [GN:lca]
PATHWAY     PATH: map00473  D-Alanine metabolism
ORTHOLOGY   KO: K03367  D-alanine-poly(phosphoribitol) ligase
GENES       ECI: UTI89_C2210
            ECP: ECP_1976
            ECA: ECA3128(dltA)
            PLU: plu4384(dltA)
            LPF: lpl2156
            LPP: lpp2183
            BUR: Bcep18194_A4786
            BPM: BURPS1710b_0819
            BPE: BP2987(dltA)
            BPA: BPP3907(dltA)
            BBR: BB4380(dltA)
            ABU: Abu_1280(dltA)
            RLE: RL4597
            BSU: BG10549(dltC) BG10551(dltA)
            BAN: BA1387(dltC) BA1389(dltA)
            BAR: GBAA1387(dltC) GBAA1389(dltA)
            BAA: BA_1913 BA_1915
            BAT: BAS1285 BAS1287
            BCE: BC1370 BC1372
            BCA: BCE_1485(dltC) BCE_1487(dltA)
            BCZ: BCZK1259(dltC) BCZK1261(dltA) pE33L466_0443(dltC)
            BTK: BT9727_1257(dltC) BT9727_1259(dltA)
            BTL: BALH_1229 BALH_1231(dltA)
            BLI: BL03932(dltC) BL03934(dltA)
            BLD: BLi04080(dltA) BLi04082(dltC)
            BAY: RBAM_035710
            SAU: SA0793(dltA) SA0795(dltC)
            SAV: SAV0932(dltA) SAV0934(dltC)
            SAM: MW0814(dltA) MW0816(dltC)
            SAR: SAR0894(dltA) SAR0896(dltC)
            SAS: SAS0802 SAS0804
            SAC: SACOL0935(dltA) SACOL0937(dltC)
            SAB: SAB0798(dltA) SAB0800(dltC)
            SAA: SAUSA300_0835(dltA) SAUSA300_0837(dltC)
            SAO: SAOUHSC_00869 SAOUHSC_00871
            SEP: SE0624 SE0626
            SER: SERP0518(dltA) SERP0520(dltC)
            SHA: SH2019(dltC) SH2021(dltA)
            SSP: SSP1841 SSP1843
            LMO: lmo0972(dltC) lmo0974(dltA)
            LMF: LMOf2365_0992(dltC) LMOf2365_0994(dltA)
            LIN: lin0971(dltC) lin0973(dltA)
            LWE: lwe0954(dltC) lwe0956(dltA)
            LLA: L90005(dltC) L91510(dltA)
            LLC: LACR_1372 LACR_1374
            LLM: llmg_1219(dltA) llmg_1221(dltC)
            SPY: SPy_1310(dltC) SPy_1312(dltA)
            SPZ: M5005_Spy_1071 M5005_Spy_1073(dltA)
            SPM: spyM18_1322 spyM18_1324(dltA)
            SPG: SpyM3_0992(dltC) SpyM3_0994(dltA)
            SPS: SPs0864 SPs0866
            SPH: MGAS10270_Spy1127
            SPI: MGAS10750_Spy1164
            SPJ: MGAS2096_Spy1070 MGAS2096_Spy1073(dltA)
            SPK: MGAS9429_Spy1113 MGAS9429_Spy1115(dltA)
            SPA: M6_Spy1041 M6_Spy1043
            SPB: M28_Spy1052
            SPN: SP_2174 SP_2176
            SPR: spr1980(dltC) spr1982(dltA)
            SPD: SPD_2003(dltC) SPD_2005(dltA)
            SAG: SAG1788(dltC) SAG1790(dltA)
            SAN: gbs1831 gbs1833
            SAK: SAK_1810(dltC) SAK_1812(dltA)
            SMU: SMU.1689(dltC) SMU.1691(dltA)
            STC: str0761(dltA) str0763(dltC)
            STL: stu0761(dltA) stu0763(dltC)
            SSA: SSA_2332(dltC) SSA_2334(dltA)
            LPL: lp_1406(dltC2) lp_2017(dltC1) lp_2019(dltA)
            LJO: LJ1782 LJ1784
            LAC: LBA1924(dltC) LBA1926(dltA)
            LSA: LSA0395(dltA) LSA0397(dltC)
            LSL: LSL_0890 LSL_0892
            LDB: Ldb2146(dltC) Ldb2148(dltA)
            LBU: LBUL_1983 LBUL_1985
            LBR: LVIS_1324 LVIS_1326
            LCA: LSEI_0794 LSEI_0796
            PPE: PEPE_1588 PEPE_1590
            EFA: EF2747(dltC) EF2749
            OOE: OEOE_0287
            LME: LEUM_1815 LEUM_1817
            CDF: CD2851(dltC) CD2853(dltA)
            DSY: DSY0221 DSY0223
            RHA: RHA1_ro00144
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.13
            ExPASy - ENZYME nomenclature database: 6.1.1.13
            ExplorEnz - The Enzyme Database: 6.1.1.13
            ERGO genome analysis and discovery system: 6.1.1.13
            BRENDA, the Enzyme Database: 6.1.1.13
            CAS: 9023-65-8
///
ENTRY       EC 6.1.1.14                 Enzyme
NAME        glycine---tRNA ligase;
            glycyl-tRNA synthetase;
            glycyl-transfer ribonucleate synthetase;
            glycyl-transfer RNA synthetase;
            glycyl-transfer ribonucleic acid synthetase;
            glycyl translase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     glycine:tRNAGly ligase (AMP-forming)
REACTION    ATP + glycine + tRNAGly = AMP + diphosphate + glycyl-tRNAGly
            [RN:R03654]
ALL_REAC    R03654
SUBSTRATE   ATP [CPD:C00002];
            glycine [CPD:C00037];
            tRNA(Gly) [CPD:C01642]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            glycyl-tRNA(Gly) [CPD:C02412]
REFERENCE   1  [PMID:13959340]
  AUTHORS   FRASER MJ.
  TITLE     Glycyl-RNA synthetase of rat liver: partial purification and effects
            of some metal ions on its activity.
  JOURNAL   Can. J. Biochem. Physiol. 41 (1963) 1123-33.
REFERENCE   2  [PMID:4295604]
  AUTHORS   Niyomporn B, Dahl JL, Strominger JL.
  TITLE     Biosynthesis of the peptidoglycan of bacterial cell walls. IX.
            Purification and properties of glycyl transfer ribonucleic acid
            synthetase from Staphylococcus aureus.
  JOURNAL   J. Biol. Chem. 243 (1968) 773-8.
  ORGANISM  Staphylococcus aureus
PATHWAY     PATH: map00260  Glycine, serine and threonine metabolism
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01877  glycyl-tRNA synthetase
            KO: K01878  glycyl-tRNA synthetase alpha chain
            KO: K01879  glycyl-tRNA synthetase beta chain
            KO: K01880  glycyl-tRNA synthetase, class II
GENES       HSA: 2617(GARS)
            PTR: 463329(GARS)
            MMU: 353172(Gars)
            RNO: 297113(Gars)
            CFA: 475268(GARS)
            BTA: 408010(GARS)
            GGA: 428403(RCJMB04_34b10)
            XLA: 446482(gars)
            XTR: 493218(gars)
            SPU: 578936(LOC578936)
            DME: Dmel_CG6778(Aats-gly)
            CEL: T10F2.1(grs-1)
            ATH: AT1G29870 AT1G29880
            OSA: 4339847 4346171
            CME: CMC037C CMC054C
            SCE: YBR121C(GRS1) YPR081C(GRS2)
            AGO: AGOS_ADL373W
            PIC: PICST_64855(GRS1)
            CGR: CAGL0G01364g
            SPO: SPAC3F10.03
            AFM: AFUA_5G05920
            AOR: AO090009000672
            CNE: CNF00730
            UMA: UM03162.1
            ECU: ECU10_1790
            DDI: DDB_0231313(glyS)
            PFA: PF14_0198
            CPV: cgd8_1030
            CHO: Chro.80123
            TAN: TA20715
            TPV: TP01_0460
            TET: TTHERM_00106940
            TBR: Tb11.01.1400
            TCR: 504017.79 511229.110
            LMA: LmjF36.3840
            EHI: 9.t00054
            ECO: b3559(glyS) b3560(glyQ)
            ECJ: JW3530(glyS) JW3531(glyQ)
            ECE: Z4983(glyS) Z4984(glyQ)
            ECS: ECs4442 ECs4443
            ECC: c4378(glyS) c4379(glyQ)
            ECI: UTI89_C4099 UTI89_C4100(glyQ)
            ECP: ECP_3661 ECP_3662
            ECV: APECO1_2890(glyQ) APECO1_2891(glyS)
            ECW: EcE24377A_4054(glyS) EcE24377A_4055(glyQ)
            ECX: EcHS_A3761(glyS) EcHS_A3762(glyQ)
            STY: STY4143(glyQ) STY4144(glyS)
            STT: t3863(glyQ) t3864(glyS)
            SPT: SPA3506(glyS) SPA3507(glyQ)
            SEC: SC3590(glyS) SC3591(glyQ)
            STM: STM3655(glyS) STM3656(glyQ)
            YPE: YPO4071(glyS) YPO4072(glyQ)
            YPK: y4089(glyS) y4090(glyQ)
            YPM: YP_3981(glyS) YP_3982(glyQ)
            YPA: YPA_3011 YPA_3012
            YPN: YPN_3717 YPN_3718
            YPP: YPDSF_0022 YPDSF_0023
            YPS: YPTB3915(glyQ) YPTB3916(glyS)
            YPI: YpsIP31758_4130(glyS) YpsIP31758_4131(glyQ)
            SFL: SF3602(glyS) SF3603(glyQ)
            SFX: S4165(glyQ) S4166(glyS)
            SFV: SFV_3981(glyQ) SFV_3982(glyS)
            SSN: SSON_3829(glyQ) SSON_3830(glyS)
            SBO: SBO_3564(glyS) SBO_3565(glyQ)
            SDY: SDY_4344(glyQ) SDY_4345(glyS)
            ECA: ECA0084(glyQ) ECA0085(glyS)
            PLU: plu0293(glyQ) plu0294(glyS)
            BUC: BU135(glyS) BU136(glyQ)
            BAS: BUsg127(glyS) BUsg128(glyQ)
            BAB: bbp126(glyS) bbp127(glyQ)
            BCC: BCc_085(glyS) BCc_086(glyQ)
            WBR: WGLp593(glyQ) WGLp594(glyS)
            SGL: SG0011 SG0012
            ENT: Ent638_0162 Ent638_0163
            KPN: KPN_03922(glyS)
            SPE: Spro_0069 Spro_0070
            BFL: Bfl020(glyQ) Bfl021(glyS)
            BPN: BPEN_019(glyQ) BPEN_020(glyS)
            HIN: HI0924(glyS) HI0927(glyQ)
            HIT: NTHI1093(glyS) NTHI1098(glyQ)
            HIP: CGSHiEE_07350(glyQ) CGSHiEE_07380(glyS)
            HDU: HD1942(glyS) HD1943(glyQ)
            HSO: HS_0479(glyS) HS_1232(glyQ)
            PMU: PM1098(glyQ) PM1102(glyS)
            MSU: MS1953(glyQ) MS1956(glyS)
            APL: APL_1800(sygA) APL_1803(sygB)
            ASU: Asuc_0409 Asuc_0410
            XFA: XF1959 XF1960
            XFT: PD0840(glyQ) PD0841(glyS)
            XCC: XCC4086(glyS) XCC4087(glyQ)
            XCB: XC_4177 XC_4178
            XCV: XCV4310(glyS) XCV4311(glyQ)
            XAC: XAC4210(glyS) XAC4211(glyQ)
            XOO: XOO4398(glyS) XOO4399(glyQ)
            XOM: XOO_4142(XOO4142) XOO_4143(XOO4143)
            VCH: VC0020 VC0021
            VCO: VC0395_A2498(glyQ) VC0395_A2499(glyS)
            VVU: VV1_0989 VV1_0990
            VVY: VV0020 VV0021
            VPA: VP0021 VP0022
            VFI: VF0015 VF0016
            PPR: PBPRA0055(glyS) PBPRA0056(glyQ)
            PAE: PA0008(glyS) PA0009(glyQ)
            PAU: PA14_00090(glyS) PA14_00100(glyQ)
            PPU: PP_0060(glyS) PP_0061(glyQ)
            PPF: Pput_0076 Pput_0077
            PST: PSPTO_0184(glyQ) PSPTO_0185(glyS)
            PSB: Psyr_0011 Psyr_0012
            PSP: PSPPH_0011(glyS) PSPPH_0012(glyQ)
            PFL: PFL_0013(glyS) PFL_0014(glyQ)
            PFO: Pfl_0009 Pfl_0010
            PEN: PSEEN0016(glyS) PSEEN0017(glyQ)
            PMY: Pmen_0013 Pmen_0014
            PAR: Psyc_1773(glyS) Psyc_1774(glyQ)
            PCR: Pcryo_2055 Pcryo_2056
            PRW: PsycPRwf_2210 PsycPRwf_2211
            ACI: ACIAD3268(glyQ) ACIAD3269(glyS)
            SON: SO_0014(glyS) SO_0015(glyQ)
            SDN: Sden_0008 Sden_0009
            SFR: Sfri_0006 Sfri_0007
            SAZ: Sama_0025 Sama_0026
            SBL: Sbal_0012 Sbal_0013
            SBM: Shew185_0008 Shew185_0009
            SLO: Shew_0009 Shew_0010
            SPC: Sputcn32_0006 Sputcn32_0007
            SSE: Ssed_0014 Ssed_0015
            SPL: Spea_0006 Spea_0007
            SHE: Shewmr4_0008 Shewmr4_0009
            SHM: Shewmr7_0008 Shewmr7_0009
            SHN: Shewana3_0016 Shewana3_0017
            SHW: Sputw3181_0006 Sputw3181_0007
            ILO: IL0005(glyS) IL0006(glyQ)
            CPS: CPS_0005(glyQ) CPS_0006(glyS)
            PHA: PSHAa0005(glyQ) PSHAa0006(glyS)
            PAT: Patl_0008 Patl_0009
            SDE: Sde_0012 Sde_0013
            PIN: Ping_3726 Ping_3727
            MAQ: Maqu_0038 Maqu_0039
            CBU: CBU_1913(glyQ) CBU_1914(glyS)
            CBD: COXBU7E912_0207(glyS) COXBU7E912_0208(glyQ)
            LPN: lpg1839(glyS) lpg1840(glyQ)
            LPF: lpl1804(glyS) lpl1805(glyQ)
            LPP: lpp1803(glyS) lpp1804(glyQ)
            MCA: MCA2049(glyQ) MCA2050(glyS)
            FTU: FTT0419(glyQ) FTT0764(glyS)
            FTF: FTF0419(glyQ) FTF0764(glyS)
            FTW: FTW_0675(glyS) FTW_1654(glyQ)
            FTL: FTL_0489 FTL_1350
            FTH: FTH_0487(glyQ) FTH_1313(glyS)
            FTA: FTA_0515(glyQ) FTA_1428(glyS)
            FTN: FTN_0519(glyQ) FTN_0736(glyS)
            TCX: Tcr_0354 Tcr_0355
            NOC: Noc_0372 Noc_0373
            AEH: Mlg_0011 Mlg_0012
            HHA: Hhal_1220 Hhal_1221
            HCH: HCH_00021(glyS) HCH_00022(glyQ)
            CSA: Csal_0006 Csal_0007
            ABO: ABO_0008(glyS) ABO_0009(glyQ)
            AHA: AHA_0127(glyS) AHA_0128(glyQ)
            DNO: DNO_0701(glyQ) DNO_0702(glyS)
            BCI: BCI_0160(glyS) BCI_0161(glyQ)
            CRP: CRP_179
            RMA: Rmag_0721 Rmag_0740
            VOK: COSY_0669(glyS) COSY_0685(glyQ)
            NME: NMB1930 NMB1932
            NMA: NMA0521(glyQ) NMA0523(glyS)
            NMC: NMC1903(glyS) NMC1904(glyQ)
            NGO: NGO2153 NGO2154
            CVI: CV_1654(glyQ) CV_1656(glyS)
            RSO: RSc0524(glyS) RSc0526(glyQ)
            REU: Reut_A0507 Reut_A0509
            REH: H16_A0521(glyS) H16_A0523(glyQ)
            RME: Rmet_0446 Rmet_0448
            BMA: BMA0218(glyS) BMA0219(glyQ)
            BMV: BMASAVP1_A2727(glyQ) BMASAVP1_A2728(glyS)
            BML: BMA10299_A2350(glyS) BMA10299_A2351(glyQ)
            BMN: BMA10247_2430(glyS) BMA10247_2431(glyQ)
            BXE: Bxe_A4012 Bxe_A4013
            BVI: Bcep1808_2802 Bcep1808_2803
            BUR: Bcep18194_A6028 Bcep18194_A6029
            BCN: Bcen_2089 Bcen_2090
            BCH: Bcen2424_2701 Bcen2424_2702
            BAM: Bamb_2753 Bamb_2754
            BPS: BPSL0667(glyS) BPSL0668(glyQ)
            BPM: BURPS1710b_0881(glyS) BURPS1710b_0882(glyQ)
            BPL: BURPS1106A_0716(glyS) BURPS1106A_0717(glyQ)
            BPD: BURPS668_0701(glyS) BURPS668_0702(glyQ)
            BTE: BTH_I0584(glyS) BTH_I0585
            PNU: Pnuc_1863 Pnuc_1864
            BPE: BP0033(glyQ) BP0034(glyS)
            BPA: BPP3654(glyQ) BPP3655(glyS)
            BBR: BB4089(glyQ) BB4090(glyS)
            RFR: Rfer_3695 Rfer_3696
            POL: Bpro_4202 Bpro_4203
            PNA: Pnap_0443 Pnap_0444
            AAV: Aave_4177 Aave_4178
            AJS: Ajs_0527 Ajs_0528
            VEI: Veis_2162 Veis_2163
            MPT: Mpe_A3380 Mpe_A3381
            HAR: HEAR0375(glyS) HEAR0376(glyQ)
            MMS: mma_0425(glyS) mma_0426(glyQ)
            NEU: NE1186(glyS) NE1187(glyQ)
            NET: Neut_1868 Neut_1869
            NMU: Nmul_A0550 Nmul_A0551
            EBA: ebA1330(glyS) ebA1331(glyQ)
            AZO: azo0785 azo0786(glyS)
            DAR: Daro_3534 Daro_3535
            TBD: Tbd_2347 Tbd_2348
            MFA: Mfla_0644 Mfla_0645
            HPY: HP0960(glyQ) HP0972(glyS)
            HPJ: jhp0894(glyQ) jhp0906(glyS)
            HPA: HPAG1_0944 HPAG1_0953
            HHE: HH0531(glyQ) HH1067(glyS)
            HAC: Hac_1036(glyQ) Hac_1057(glyS)
            WSU: WS0209(glyS) WS2118(glyQ)
            TDN: Tmden_0991 Tmden_1857
            CJE: Cj0704(glyQ) Cj1234(glyS)
            CJR: CJE0804(glyQ) CJE1369(glyS)
            CJJ: CJJ81176_0727(glyQ) CJJ81176_1248(glyS)
            CJU: C8J_0671(glyQ) C8J_1177(glyS)
            CJD: JJD26997_0491(glyS) JJD26997_1302(glyQ)
            CFF: CFF8240_0826(glyS) CFF8240_1047(glyQ)
            CCV: CCV52592_0284(glyQ) CCV52592_1374(glyS)
            CHA: CHAB381_0708(glyQ) CHAB381_1246(glyS)
            CCO: CCC13826_0043(glyS) CCC13826_1017 CCC13826_1439(glyQ)
                 CCC13826_1812
            ABU: Abu_1232(glyS) Abu_1979(glyQ)
            NIS: NIS_0732(glyS) NIS_1511(glyQ)
            SUN: SUN_0359(glyQ) SUN_1701(glyS)
            GSU: GSU0578(glyQ) GSU0579(glyS)
            GME: Gmet_2941 Gmet_2942
            GUR: Gura_3672 Gura_3673
            PCA: Pcar_0598 Pcar_0599
            PPD: Ppro_3059 Ppro_3060
            DVU: DVU1897(glyS) DVU1898(glyQ)
            DVL: Dvul_1265 Dvul_1266
            DDE: Dde_2033 Dde_2034
            LIP: LI0299(glyS) LI0300(glyQ)
            BBA: Bd1147(glyS)
            DPS: DP0118
            ADE: Adeh_1305 Adeh_1306
            AFW: Anae109_2459 Anae109_2460
            MXA: MXAN_3100(glyQ) MXAN_3101(glyS)
            SAT: SYN_01536 SYN_01537
            SFU: Sfum_2445 Sfum_2446
            RPR: RP849(glyS) RP850(glyQ)
            RTY: RT0838(glyS) RT0839(glyQ)
            RCO: RC1316(glyS) RC1317(glyQ)
            RFE: RF_1346(glyS) RF_1347(glyQ)
            RBE: RBE_1359(glyS) RBE_1360(glyQ)
            RAK: A1C_06580(glyS) A1C_06585(glyQ)
            RBO: A1I_00750(glyQ) A1I_00755(glyS)
            RCM: A1E_05440(glyS) A1E_05480(glyQ)
            RRI: A1G_07210(glyS) A1G_07215(glyQ)
            OTS: OTBS_0603(glyQ) OTBS_0604(glyS)
            WOL: WD0155(glyS) WD0156(glyQ)
            WBM: Wbm0370 Wbm0371
            AMA: AM1294(glyQ) AM1295(glyS)
            APH: APH_0013(glyQ-1) APH_0014(glyS) APH_0165(glyQ-2)
            ERU: Erum0110(glyQ) Erum0120(glyS)
            ERW: ERWE_CDS_09560(glyQ) ERWE_CDS_09570(glyS)
            ERG: ERGA_CDS_09480(glyQ) ERGA_CDS_09490(glyS)
            ECN: Ecaj_0003 Ecaj_0004
            ECH: ECH_0023(glyQ) ECH_0024(glyS)
            NSE: NSE_0756(glyS) NSE_0757(glyQ)
            PUB: SAR11_0616(glyQ) SAR11_0617(glyRS)
            MLO: mlr7434 mlr7435
            MES: Meso_0713 Meso_0714
            PLA: Plav_0727 Plav_0728
            SME: SMc00851(glyS) SMc00855(glyQ)
            SMD: Smed_0463 Smed_0466
            ATU: Atu0639(glyQ) Atu0644(glyS)
            ATC: AGR_C_1133 AGR_C_1144
            RET: RHE_CH00881(glyQ) RHE_CH00890(glyS)
            RLE: RL0943(glyQ) RL0951(glyS)
            BME: BMEI1529 BMEI1530
            BMF: BAB1_0431 BAB1_0433
            BMS: BR0403(glyQ) BR0404(glyS)
            BMB: BruAb1_0426(glyQ) BruAb1_0427(glyS)
            BOV: BOV_0412(glyQ) BOV_0413(glyS)
            OAN: Oant_0521 Oant_0522
            BJA: blr2535(glyQ) blr2536(glyS)
            BRA: BRADO2029(glyQ) BRADO2031(glyS)
            BBT: BBta_2355(glyQ) BBta_2357(glyS)
            RPA: RPA1045(sygA) RPA1047(sygB)
            RPB: RPB_1093 RPB_1095
            RPC: RPC_4348 RPC_4349
            RPD: RPD_1219 RPD_1221
            RPE: RPE_4409 RPE_4411
            NWI: Nwi_2586(glyS) Nwi_2587(glyQ)
            NHA: Nham_3210 Nham_3211
            BHE: BH04150(glyS) BH04160(glyQ)
            BQU: BQ03170(glyS) BQ03180(glyQ)
            BBK: BARBAKC583_0380(glyS) BARBAKC583_0381(glyQ)
            XAU: Xaut_3329 Xaut_3330
            CCR: CC_1341 CC_1342
            SIL: SPO1355(glyQ) SPO1358(glyS)
            SIT: TM1040_2310 TM1040_2312
            RSP: RSP_1856(glyQ) RSP_1858(glyS)
            RSH: Rsph17029_0505 Rsph17029_0507
            RSQ: Rsph17025_0642 Rsph17025_0644
            JAN: Jann_2731 Jann_2733
            RDE: RD1_1945(glyQ) RD1_1947(glyS)
            PDE: Pden_0538 Pden_0540
            MMR: Mmar10_2178 Mmar10_2181
            HNE: HNE_0683(glyQ) HNE_0685(glyS)
            ZMO: ZMO1444(glyS) ZMO1446(glyQ)
            NAR: Saro_2111 Saro_2112
            SAL: Sala_1611 Sala_1612
            SWI: Swit_4857 Swit_4858
            ELI: ELI_05860 ELI_05865
            GOX: GOX1743 GOX1744
            GBE: GbCGDNIH1_2099 GbCGDNIH1_2102
            ACR: Acry_2185 Acry_2186
            RRU: Rru_A2954 Rru_A2955
            MAG: amb2650 amb2651
            MGM: Mmc1_1440 Mmc1_1441
            ABA: Acid345_1194 Acid345_1195
            SUS: Acid_7205 Acid_7206
            BSU: BG11657(glyQ) BG11658(glyS)
            BHA: BH1370(glyQ) BH1371(glyS)
            BAN: BA5147(glyS)
            BAR: GBAA5147(glyS)
            BAA: BA_0020
            BAT: BAS4784
            BCA: BCE_5053(glyS)
            BCZ: BCZK4646(glyS)
            BTK: BT9727_4624(glyS)
            BTL: BALH_4454(glyS)
            BLI: BL03676(glyQ) BL03677(glyS)
            BLD: BLi02717(glyS) BLi02718(glyQ)
            BCL: ABC1684(glyQ) ABC1685(glyS)
            BAY: RBAM_023570(glyQ)
            BPU: BPUM_2258(glyS) BPUM_2259(glyQ)
            OIH: OB1948(glyS) OB1949(glyQ)
            GKA: GK3430
            SAU: SA1394(glyS)
            SAV: SAV1565(glyS)
            SAM: MW1517(glyS)
            SAR: SAR1642
            SAS: SAS1503
            SAC: SACOL1622(glyS)
            SAB: SAB1437(glyS)
            SAA: SAUSA300_1525(glyS)
            SAO: SAOUHSC_01666
            SEP: SE1252
            SER: SERP1132(glyS)
            SHA: SH1351(glyS)
            SSP: SSP1191
            LMO: lmo1458(glyS) lmo1459(glyQ)
            LMF: LMOf2365_1477(glyS) LMOf2365_1478(glyQ)
            LIN: lin1495(glyS) lin1496(glyQ)
            LWE: lwe1473(glyS) lwe1474(glyQ)
            LLA: L0360(glyT) L101560(glyS)
            LLC: LACR_1196 LACR_1197
            LLM: llmg_1477(glyS) llmg_1478(glyQ)
            SPY: SPy_1688(glyS) SPy_1689(glyQ)
            SPZ: M5005_Spy_1384(glyS) M5005_Spy_1385(glyQ)
            SPM: spyM18_1700(glyS) spyM18_1701(glyQ)
            SPG: SpyM3_1471(glyS) SpyM3_1472(glyQ)
            SPS: SPs0394 SPs0395
            SPH: MGAS10270_Spy1503(glyS) MGAS10270_Spy1504(glyQ)
            SPI: MGAS10750_Spy1495(glyS) MGAS10750_Spy1496(glyQ)
            SPJ: MGAS2096_Spy1407(glyS) MGAS2096_Spy1408(glyQ)
            SPK: MGAS9429_Spy1382(glyS) MGAS9429_Spy1383(glyQ)
            SPF: SpyM50405(glyQ) SpyM50406(glyS)
            SPA: M6_Spy1432 M6_Spy1433
            SPB: M28_Spy1427(glyS) M28_Spy1428(glyQ)
            SPN: SP_1474 SP_1475
            SPR: spr1328(glyS) spr1329(glyQ)
            SPD: SPD_1304(glyS) SPD_1305(glyQ)
            SAG: SAG0268(glyQ) SAG0270(glyS)
            SAN: gbs0258(glyQ) gbs0260(glyS)
            SAK: SAK_0340(glyQ) SAK_0342(glyS)
            SMU: SMU.445(sygA) SMU.446(sygB)
            STC: str0505(glyQ) str0507(glyS)
            STL: stu0505(glyQ) stu0507(glyS)
            SSA: SSA_1879(glyS) SSA_1880(glyQ)
            SGO: SGO_0568(glyQ) SGO_0569(glyS)
            LPL: lp_1964(glyS) lp_1965(glyQ)
            LJO: LJ1319 LJ1320
            LAC: LBA1198 LBA1199
            LSA: LSA0880(glyQ) LSA0881(glyS)
            LSL: LSL_0911(glyS) LSL_0912(glyQ)
            LDB: Ldb1248(glyS) Ldb1249(glyQ)
            LBU: LBUL_1166 LBUL_1167
            LBR: LVIS_0753 LVIS_0754
            LCA: LSEI_1503 LSEI_1504
            LRE: Lreu_0740 Lreu_0741
            EFA: EF2406(glyS) EF2407(glyQ)
            OOE: OEOE_0992 OEOE_0994
            STH: STH574(glySA) STH575(glySB)
            CAC: CAC3195
            CPE: CPE2464(glyS)
            CPF: CPF_2779(glyS)
            CPR: CPR_2465(glyS)
            CTC: CTC00212
            CNO: NT01CX_1048(glyS)
            CTH: Cthe_1312
            CDF: CD2432(glyS) CD2433(glyQ)
            CBO: CBO3517(glyS)
            CBA: CLB_3592(glyS)
            CBH: CLC_3481(glyS)
            CBF: CLI_3726(glyS)
            CKL: CKL_0180(glyS)
            CHY: CHY_0439(glyQ) CHY_0440(glyS)
            DSY: DSY3083 DSY3084
            DRM: Dred_2472 Dred_2473
            SWO: Swol_1515 Swol_1516
            TTE: TTE0978(gRS1)
            MTA: Moth_0603 Moth_0604
            MGE: MG_251(glys)
            MPN: MPN354(grs1)
            MPU: MYPU_4510(glyS)
            MPE: MYPE3390(glyS)
            MGA: MGA_0015(glyS)
            MMY: MSC_0464(glyS)
            MMO: MMOB2920(glyS)
            MHY: mhp061(glyS)
            MHJ: MHJ_0054(glyS)
            MHP: MHP7448_0058(glyS)
            MSY: MS53_0452(glyS)
            MCP: MCAP_0505(glyS)
            UUR: UU493(glyS)
            POY: PAM626(GRS1)
            AYW: AYWB_109(grs1)
            MFL: Mfl268
            MTU: Rv2357c(glyS)
            MTC: MT2426(glyS)
            MBO: Mb2378c(glyS)
            MBB: BCG_2371c(glyS)
            MLE: ML0826(glyS)
            MPA: MAP2137c(glyS)
            MAV: MAV_2038(glyS)
            MSM: MSMEG_4485(glyS)
            MVA: Mvan_3818
            MGI: Mflv_2719
            MMC: Mmcs_3445
            MKM: Mkms_3508
            MJL: Mjls_3456
            CGL: NCgl2198(cgl2278)
            CGB: cg2499(glyS)
            CEF: CE2178
            CDI: DIP1708(glyS)
            CJK: jk0613(glyS)
            NFA: nfa14590(glyS)
            RHA: RHA1_ro01220(glyS)
            SCO: SCO2504(glyS)
            SMA: SAV5635(glyS)
            TWH: TWT500(glyQS)
            TWS: TW262(glyQS)
            LXX: Lxx01030(glyS)
            CMI: CMM_1581(glyS)
            ART: Arth_1330
            AAU: AAur_1482(glyS)
            PAC: PPA0949
            NCA: Noca_1940
            TFU: Tfu_0861
            FRA: Francci3_1275
            FAL: FRAAL2019(glyQS)
            ACE: Acel_0798
            SEN: SACE_1500(glyS)
            BLO: BL0116(glyS)
            BAD: BAD_1138(glyS)
            RXY: Rxyl_0775
            FNU: FN0069 FN0070
            RBA: RB10547(glyS)
            CTR: CT796(glyQ)
            CTA: CTA_0867(glyQ)
            CMU: TC0178
            CPN: CPn0946(glyQ)
            CPA: CP0913
            CPJ: CPj0946(glyQ)
            CPT: CpB0981
            CCA: CCA00823(glyQS)
            CAB: CAB792(glyQ)
            CFE: CF0191(glyQ)
            PCU: pc0693(glyS)
            BBU: BB0371(glyS)
            BGA: BG0370(glyS)
            BAF: BAPKO_0380(glyS)
            TPA: TP0672
            TDE: TDE0020(glyS)
            LIL: LA1388(glyS)
            LIC: LIC12350(glyS)
            LBJ: LBJ_2234(glyRS)
            LBL: LBL_2227(glyRS)
            SYN: slr0220(glyS) slr0638(glyQ)
            SYW: SYNW1096(glyS) SYNW1671(glyQ)
            SYC: syc1479_d(glyS) syc1647_c(glyQ)
            SYF: Synpcc7942_0018 Synpcc7942_2457
            SYD: Syncc9605_0812 Syncc9605_1228
            SYE: Syncc9902_1241 Syncc9902_1561
            SYG: sync_0717(glyQ) sync_1281(glyS)
            SYR: SynRCC307_0585(glyQ) SynRCC307_1268(glyS)
            SYX: SynWH7803_1318(glyS) SynWH7803_1770(glyQ)
            CYA: CYA_0584(glyQ) CYA_2862(glyS)
            CYB: CYB_0066(glyQ) CYB_2517(glyS)
            TEL: tll1034(glyQ) tll2192(glyS)
            GVI: glr1446(glyQ) glr1646(glyS)
            ANA: all1985(glyQ) alr4111
            AVA: Ava_0794(glyS) Ava_4336(glyQ)
            PMA: Pro0831(glyS) Pro1268(glyQ)
            PMM: PMM0759(glyS) PMM1165(glyQ)
            PMT: PMT0283(glyQ) PMT0578(glyS)
            PMN: PMN2A_0163 PMN2A_0778
            PMI: PMT9312_0767 PMT9312_1265
            PMB: A9601_08211(glyS) A9601_13561(glyQ)
            PMC: P9515_08241(glyS) P9515_13351(glyQ)
            PMF: P9303_16721(glyS) P9303_20541(glyQ)
            PMG: P9301_08191(glyS) P9301_13651(glyQ)
            PMH: P9215_08531(glyS) P9215_13771(glyQ)
            PME: NATL1_07951(glyS) NATL1_16221(glyQ)
            TER: Tery_3866 Tery_4481
            BTH: BT_3611
            BFR: BF0412
            BFS: BF0354(glyS)
            PGI: PG2165(glyS)
            SRU: SRU_2334(glyS)
            CHU: CHU_3489
            GFO: GFO_3534(glyS)
            FPS: FP2429(glyS)
            CTE: CT2255(glyS)
            CCH: Cag_0036
            CPH: Cpha266_0045
            PVI: Cvib_0021
            PLT: Plut_0017
            DET: DET0787(glyS)
            DEH: cbdb_A765(glyS)
            DRA: DR_2059
            DGE: Dgeo_1716
            TTH: TTC0175
            TTJ: TTHA0543
            AAE: aq_2141(glyS) aq_945(glyQ)
            TMA: TM0216 TM0217
            TPT: Tpet_0707 Tpet_0708
            TME: Tmel_0632 Tmel_0633
            FNO: Fnod_1053 Fnod_1054
            MJA: MJ0228(glyS)
            MMP: MMP0212
            MMQ: MmarC5_1458
            MMZ: MmarC7_1214
            MAE: Maeo_1294
            MVN: Mevan_1227
            MAC: MA0097(glyS)
            MBA: Mbar_A1209
            MMA: MM_1388
            MBU: Mbur_0919
            MTP: Mthe_0271
            MHU: Mhun_1707
            MLA: Mlab_1162
            MEM: Memar_1419
            MTH: MTH1846
            MST: Msp_1049(glyS)
            MSI: Msm_0403
            MKA: MK0152(GRS1)
            AFU: AF0916(glyS)
            HAL: VNG2352G(glyS)
            HMA: rrnAC2701(glyS)
            HWA: HQ3709A(glyS)
            NPH: NP0328A(glyS)
            TAC: Ta0206
            TVO: TVN1388
            PTO: PTO1114
            PHO: PH1614
            PAB: PAB0380(glyS)
            PFU: PF1627
            TKO: TK0978
            RCI: RCIX1267(glyS)
            APE: APE_1639
            HBU: Hbut_0050
            SSO: SSO0444(glyS)
            STO: ST0353
            SAI: Saci_0862(glyRS)
            PAI: PAE2266
            PIS: Pisl_0895
            PCL: Pcal_1628
            PAS: Pars_1821
            TPE: Tpen_0288
            NEQ: NEQ417
STRUCTURES  PDB: 1ATI  1B76  1GGM  1J5W  2PME  2PMF  2Q5H  2Q5I  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.14
            ExPASy - ENZYME nomenclature database: 6.1.1.14
            ExplorEnz - The Enzyme Database: 6.1.1.14
            ERGO genome analysis and discovery system: 6.1.1.14
            BRENDA, the Enzyme Database: 6.1.1.14
            CAS: 9037-62-1
///
ENTRY       EC 6.1.1.15                 Enzyme
NAME        proline---tRNA ligase;
            prolyl-tRNA synthetase;
            prolyl-transferRNA synthetase;
            prolyl-transfer ribonucleate synthetase;
            proline translase;
            prolyl-transfer ribonucleic acid synthetase;
            prolyl-s-RNA synthetase;
            prolinyl-tRNA ligase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-proline:tRNAPro ligase (AMP-forming)
REACTION    ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
            [RN:R03661]
ALL_REAC    R03661
SUBSTRATE   ATP [CPD:C00002];
            L-proline [CPD:C00148];
            tRNA(Pro) [CPD:C01649]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-prolyl-tRNA(Pro) [CPD:C02702]
REFERENCE   1
  AUTHORS   Norton, S.J.
  TITLE     Purification and properties of the prolyl RNA synthetase of
            Escherichia coli.
  JOURNAL   Arch. Biochem. Biophys. 106 (1964) 147-152.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Peterson, P.J. and Fowden, L.
  TITLE     Purification, properties and comparative specificities of the enzyme
            prolyl-transfer ribonucleic acid synthetase from Phaseolus aureus
            and Polygonatum multiflorum.
  JOURNAL   Biochem. J. 97 (1965) 112-124.
  ORGANISM  Phaseolus aureus, Polygonatum multiflorum
PATHWAY     PATH: map00330  Arginine and proline metabolism
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01881  prolyl-tRNA synthetase
GENES       HSA: 2058(EPRS) 25973(PARS2)
            MMU: 107508(Eprs) 230577(Pars2)
            RNO: 289352(Eprs) 313429(Pars2)
            CFA: 478962(EPRS) 489574(PARS2)
            GGA: 421348(EPRS) 424659(PARS2)
            XLA: 379241(MGC53152)
            DRE: 325494(pars2)
            SPU: 578133(LOC578133) 581596(LOC581596)
            DME: Dmel_CG12186(Aats-pro) Dmel_CG5394(Aats-glupro)
            CEL: T27F6.5(prs-2)
            ATH: AT5G52520(OVA6)
            OSA: 4342480 4352148
            CME: CMJ098C CMS024C
            SCE: YER087W YHR020W
            AGO: AGOS_ACR233W AGOS_AEL021C
            PIC: PICST_50946(PRS3) PICST_84407(YHI0)
            CGR: CAGL0I05104g
            SPO: SPBC19C7.06 SPBC24C6.03
            ANI: AN2150.2
            AFM: AFUA_1G10750 AFUA_2G16010
            AOR: AO090012000200 AO090038000342
            CNE: CNB05640
            UMA: UM00855.1 UM06184.1
            ECU: ECU02_1360
            DDI: DDB_0231314(mproS) DDB_0231317(proS)
            PFA: PFI1240c PFL0670c
            CPV: cgd6_4400
            TAN: TA12695 TA19220
            TPV: TP01_0166 TP02_0040
            TET: TTHERM_00487020
            TCR: 503939.80
            EHI: 144.t00016 419.t00006
            ECO: b0194(proS)
            ECJ: JW0190(proS)
            ECE: Z0206(proS)
            ECS: ECs0196
            ECC: c0235(proS)
            ECI: UTI89_C0210(proS)
            ECP: ECP_0204
            ECV: APECO1_1793(proS)
            ECW: EcE24377A_0201(proS)
            STY: STY0269(proS)
            STT: t0245(proS)
            SPT: SPA0249(proS)
            SEC: SC0241(proS)
            STM: STM0242(proS)
            YPE: YPO1068(proS)
            YPK: y3109(proS)
            YPM: YP_2781(proS)
            YPA: YPA_0545
            YPN: YPN_2931
            YPP: YPDSF_1643
            YPS: YPTB2978(proS)
            YPI: YpsIP31758_1038(proS)
            SFL: SF0185(proS)
            SFX: S0187(proS)
            SFV: SFV_0178(proS)
            SSN: SSON_0208(proS)
            SBO: SBO_0183(proS)
            SDY: SDY_0213(proS)
            ECA: ECA3529(proS)
            PLU: plu0692(proS)
            BUC: BU239(proS)
            BAS: BUsg234(proS)
            BAB: bbp221(proS)
            BCC: BCc_149(proS)
            WBR: WGLp597(proS)
            SGL: SG1920
            KPN: KPN_00208(proS)
            BFL: Bfl289(proS)
            BPN: BPEN_297(proS)
            HIN: HI0729(proS)
            HIT: NTHI0888(proS)
            HIP: CGSHiEE_08475
            HIQ: CGSHiGG_07110
            HDU: HD1919(proS)
            HSO: HS_1305(proS)
            PMU: PM1370(proS)
            MSU: MS2063(proS)
            APL: APL_1830(syp)
            XFA: XF0445
            XFT: PD1635(proS)
            XCC: XCC0639(proS)
            XCB: XC_3596
            XCV: XCV3692(proS)
            XAC: XAC3567(proS)
            XOO: XOO0809(proS)
            XOM: XOO_0737(XOO0737)
            VCH: VC0875
            VCO: VC0395_A0400(proS)
            VVU: VV1_1838
            VVY: VV2572
            VPA: VP2333
            VFI: VF0682(pro)
            PPR: PBPRA2944(proS)
            PAE: PA0956(proS)
            PAU: PA14_51900(proS)
            PAP: PSPA7_4552(proS)
            PPU: PP_1205(proS)
            PST: PSPTO_3988(proS)
            PSB: Psyr_1399
            PSP: PSPPH_3783(proS)
            PFL: PFL_1256(proS)
            PFO: Pfl_1197
            PEN: PSEEN4105(proS)
            PMY: Pmen_1258
            PAR: Psyc_0429(proS)
            PCR: Pcryo_0463
            ACI: ACIAD0782(proS)
            ACB: A1S_2819
            SON: SO_3154(proS)
            SDN: Sden_2544
            SFR: Sfri_2753
            SAZ: Sama_1161
            SBL: Sbal_2856
            SLO: Shew_2596
            SHE: Shewmr4_1345
            SHM: Shewmr7_1410
            SHN: Shewana3_1398
            SHW: Sputw3181_1490
            ILO: IL0886(proS)
            CPS: CPS_3230(proS)
            PHA: PSHAa1623(proS)
            PAT: Patl_1276
            SDE: Sde_0909
            PIN: Ping_3289
            MAQ: Maqu_1735
            CBU: CBU_0081(proS)
            CBD: COXBU7E912_2026(proS)
            LPN: lpg0694(proS)
            LPF: lpl0731(proS)
            LPP: lpp0749(proS)
            MCA: MCA2013(proS)
            FTU: FTT1412(proS)
            FTF: FTF1412(proS)
            FTW: FTW_0472(proS)
            FTL: FTL_0650
            FTH: FTH_0650(proS)
            FTA: FTA_0684(proS)
            FTN: FTN_1377(proS)
            TCX: Tcr_1075
            NOC: Noc_0897
            AEH: Mlg_0539
            HHA: Hhal_0701
            HCH: HCH_04773(proS)
            CSA: Csal_2139
            ABO: ABO_0739(proS)
            AHA: AHA_3650(proS)
            DNO: DNO_1137(proS)
            BCI: BCI_0609(proS)
            VOK: COSY_0329(proS)
            NME: NMB1339
            NMA: NMA1553(proS)
            NMC: NMC1277(proS)
            NGO: NGO0566
            CVI: CV_0574(proS)
            RSO: RSc2816(proS)
            REU: Reut_A2952
            REH: H16_A3246(proS)
            RME: Rmet_3100
            BMA: BMA2517(proS)
            BMV: BMASAVP1_A0439(proS)
            BML: BMA10299_A1298(proS)
            BMN: BMA10247_3265(proS)
            BXE: Bxe_A0513
            BUR: Bcep18194_A3672
            BCN: Bcen_0105
            BCH: Bcen2424_0587
            BAM: Bamb_0490
            BPS: BPSL2998(proS)
            BPM: BURPS1710b_3518(proS)
            BPL: BURPS1106A_3520(proS)
            BPD: BURPS668_3482(proS)
            BTE: BTH_I1146(proS)
            BPE: BP3348(proS)
            BPA: BPP3787(proS)
            BBR: BB4232(proS)
            RFR: Rfer_1274
            POL: Bpro_0833
            MPT: Mpe_A0517
            HAR: HEAR2781(proS)
            MMS: mma_2988
            NEU: NE1317(proS)
            NET: Neut_1247
            NMU: Nmul_A0450
            EBA: ebA950(proS)
            DAR: Daro_0644
            TBD: Tbd_2112
            MFA: Mfla_0420
            HPY: HP0238(proS)
            HPJ: jhp0223(proS)
            HPA: HPAG1_0241
            HHE: HH1726(proS)
            HAC: Hac_1380(proS)
            WSU: WS1580(proS)
            TDN: Tmden_0860
            CJE: Cj0543(proS)
            CJR: CJE0647(proS)
            CJJ: CJJ81176_0568(proS)
            CJU: C8J_0504(proS)
            CJD: JJD26997_1387(proS)
            CFF: CFF8240_0689(proS)
            CCV: CCV52592_0765(proS)
            CHA: CHAB381_0897(proS)
            CCO: CCC13826_1050(proS)
            ABU: Abu_0388(proS)
            NIS: NIS_1023(proS)
            SUN: SUN_0637(proS)
            GSU: GSU1460(proS)
            GME: Gmet_1354
            PCA: Pcar_0682
            DVU: DVU1345(proS)
            DDE: Dde_2206
            LIP: LI0390(proS)
            BBA: Bd3033(proS)
            DPS: DP1164
            ADE: Adeh_0024 Adeh_3947
            MXA: MXAN_6655(proS)
            SAT: SYN_00905
            SFU: Sfum_1267
            RPR: RP384
            RTY: RT0372(proS)
            RCO: RC0528(proS)
            RFE: RF_0600(proS)
            RBE: RBE_0804(proS)
            RAK: A1C_02875
            RBO: A1I_05150
            RRI: A1G_02995
            OTS: OTBS_0949(proS)
            WOL: WD0813(proS)
            WBM: Wbm0077
            AMA: AM507(proS)
            APH: APH_0647(proS)
            ERU: Erum3440(proS)
            ERW: ERWE_CDS_03510(proS)
            ERG: ERGA_CDS_03470(proS)
            ECN: Ecaj_0327
            ECH: ECH_0740(proS)
            NSE: NSE_0367(proS)
            PUB: SAR11_0902(proS)
            MLO: mll1344
            MES: Meso_1040
            SME: SMc01934(proS)
            ATU: Atu1288(proS)
            ATC: AGR_C_2372
            RET: RHE_CH01623(proS)
            RLE: RL1719(proS)
            BME: BMEI1140
            BMF: BAB1_0842
            BMS: BR0822(proS)
            BMB: BruAb1_0836(proS)
            BOV: BOV_0816(proS)
            BJA: bll4877(proS)
            BRA: BRADO4154(proS)
            BBT: BBta_4531(proS)
            RPA: RPA2928(proS)
            RPB: RPB_2597
            RPC: RPC_2427
            RPD: RPD_2865
            RPE: RPE_2544
            NWI: Nwi_1865
            NHA: Nham_2197
            BHE: BH08790(proS)
            BQU: BQ05800(proS)
            BBK: BARBAKC583_0794(proS)
            CCR: CC_1931
            SIL: SPO1121(proS)
            SIT: TM1040_1852
            RSP: RSP_0778(proS)
            RSH: Rsph17029_2434
            RSQ: Rsph17025_0401
            JAN: Jann_1060
            RDE: RD1_2045(proS)
            PDE: Pden_1299
            MMR: Mmar10_1375
            HNE: HNE_1764(proS)
            ZMO: ZMO0460(proS)
            NAR: Saro_1950
            SAL: Sala_1230
            ELI: ELI_06105
            GOX: GOX0079(pro)
            GBE: GbCGDNIH1_1284
            ACR: Acry_0939
            RRU: Rru_A1576
            MAG: amb3636
            MGM: Mmc1_1767
            ABA: Acid345_1063
            SUS: Acid_1843
            BSU: BG12659(proS)
            BHA: BH2419(proS)
            BAN: BA0396(proS-1) BA3957(proS-2)
            BAR: GBAA0396(proS-1) GBAA3957(proS-2)
            BAA: BA_0971 BA_4427
            BAT: BAS0382 BAS3670
            BCE: BC0439 BC3817
            BCA: BCE_0510(proS) BCE_3860(proS)
            BCZ: BCZK0370(proS) BCZK3578(proS)
            BTK: BT9727_0373(proS) BT9727_3560(proS)
            BTL: BALH_0396(proS) BALH_3449(proS)
            BLI: BL01235(proS)
            BLD: BLi01878(proS)
            BCL: ABC2234(proS)
            BAY: RBAM_016410
            BPU: BPUM_0197 BPUM_1556
            OIH: OB0566
            GKA: GK1257(proS)
            SAU: SA1106(proS)
            SAV: SAV1263(proS)
            SAM: MW1146(proS)
            SAR: SAR1239(proS)
            SAS: SAS1197
            SAC: SACOL1282(proS)
            SAB: SAB1125(proS)
            SAA: SAUSA300_1156(proS)
            SAO: SAOUHSC_01240
            SAJ: SaurJH9_1323
            SEP: SE0939
            SER: SERP0830(proS)
            SHA: SH1651(proS)
            SSP: SSP1505
            LMO: lmo1319(proS)
            LMF: LMOf2365_1336(proS)
            LIN: lin1356(proS)
            LWE: lwe1334(proS)
            LLA: L0356(proS)
            LLC: LACR_2432
            LLM: llmg_2412(proS)
            SPY: SPy_1962(proS)
            SPZ: M5005_Spy_1673(proS)
            SPM: spyM18_2030(proS)
            SPG: SpyM3_1688(proS)
            SPS: SPs1690
            SPH: MGAS10270_Spy1741(proS)
            SPI: MGAS10750_Spy1767(proS)
            SPJ: MGAS2096_Spy1696(proS)
            SPK: MGAS9429_Spy1674(proS)
            SPF: SpyM51645(drpA)
            SPA: M6_Spy1681
            SPB: M28_Spy1661(proS)
            SPN: SP_0264
            SPR: spr0243(proS)
            SPD: SPD_0246(proS)
            SAG: SAG1913(proS)
            SAN: gbs1900(proS)
            SAK: SAK_1871(proS)
            SMU: SMU.1783(proS)
            STC: str0200(proS)
            STL: stu0200(proS)
            SSA: SSA_2069(proS)
            SGO: SGO_1851(proS)
            LPL: lp_2048(proS)
            LJO: LJ1493
            LAC: LBA1262
            LSA: LSA1257(proS)
            LSL: LSL_0566(proS)
            LDB: Ldb1338(proS)
            LBU: LBUL_1247
            LBR: LVIS_1342
            LCA: LSEI_1579
            LGA: LGAS_0808
            LRE: Lreu_0693
            PPE: PEPE_0884
            EFA: EF2379(proS)
            OOE: OEOE_0982
            STH: STH1502(proS)
            CAC: CAC3178(proS)
            CPE: CPE2428(proS)
            CPF: CPF_2738(proS)
            CPR: CPR_2425(proS)
            CTC: CTC02625
            CNO: NT01CX_0337(proS)
            CDF: CD0049(proS) CD0050
            CBO: CBO3344(proS1) CBO3503(proS2)
            CBA: CLB_3402(proS)
            CBH: CLC_3289(proS)
            CBF: CLI_3517(proS)
            CKL: CKL_0602(proS)
            CHY: CHY_1775(proS)
            DSY: DSY2536
            SWO: Swol_0892
            TTE: TTE2319(proS)
            MTA: Moth_1044
            MGE: MG_283(proS)
            MPN: MPN402(proS)
            MPU: MYPU_1830(proS)
            MPE: MYPE8010(proS)
            MGA: MGA_1022(proS)
            MMY: MSC_0327(proS)
            MMO: MMOB1440(proRS)
            MHY: mhp397(proS)
            MHJ: MHJ_0381(proS)
            MHP: MHP7448_0385(proS)
            MSY: MS53_0492(proS)
            MCP: MCAP_0318(proS)
            UUR: UU452(proS)
            POY: PAM246(proS)
            AYW: AYWB_475(proS)
            MFL: Mfl476
            MTU: Rv2845c(proS)
            MTC: MT2911(proS)
            MBO: Mb2870c(proS)
            MBB: BCG_2865c(proS)
            MLE: ML1553(proS)
            MPA: MAP2913c(proS)
            MAV: MAV_3700(proS)
            MSM: MSMEG_2621(proS)
            MVA: Mvan_2308
            MGI: Mflv_4045
            MMC: Mmcs_2076
            MKM: Mkms_2122
            MJL: Mjls_2059
            CGL: NCgl1919(cgl1994)
            CGB: cg2185(proS)
            CEF: CE1888
            CDI: DIP1482(proS)
            CJK: jk1147(proS)
            NFA: nfa40730(proS)
            RHA: RHA1_ro03499(proS1) RHA1_ro06628(proS2)
            SCO: SCO5699(proS)
            SMA: SAV2558(proS1) SAV2646(proS2)
            TWH: TWT183(proS)
            TWS: TW588(proS)
            LXX: Lxx12210(proS)
            ART: Arth_1407
            AAU: AAur_1553(proS)
            PAC: PPA1499
            TFU: Tfu_0772
            FRA: Francci3_4267
            FAL: FRAAL6537(proS)
            KRA: Krad_1436
            SEN: SACE_5936(proS)
            BLO: BL1728(proS)
            BAD: BAD_0456(proS)
            RXY: Rxyl_1087
            FNU: FN1658
            RBA: RB5178(proS)
            CTR: CT393(proS)
            CTA: CTA_0428(proS)
            CMU: TC0672
            CPN: CPn0500(proS)
            CPA: CP0254
            CPJ: CPj0500(proS)
            CPT: CpB0520
            CCA: CCA00244(proS)
            CAB: CAB240(proS)
            CFE: CF0762(proS)
            PCU: pc1324(proS)
            BGA: BG0405(proS)
            BAF: BAPKO_0419(proS)
            TPA: TP0160
            TDE: TDE2220(proS)
            LIL: LA3290(proS)
            LIC: LIC10858(proS)
            LBJ: LBJ_0912(proS)
            LBL: LBL_0927(proS)
            SYN: sll1425(proS)
            SYW: SYNW1771(proS)
            SYC: syc2136_c(proS)
            SYF: Synpcc7942_1959
            SYD: Syncc9605_0693
            SYE: Syncc9902_1665
            SYG: sync_2021(proS)
            SYR: SynRCC307_0876(proS)
            SYX: SynWH7803_0622(proS)
            CYA: CYA_2339(proS)
            CYB: CYB_1126(proS)
            TEL: tlr0777(proS)
            GVI: gll2525
            ANA: alr5053
            AVA: Ava_2311
            PMA: Pro0508(proS)
            PMM: PMM0508(proS)
            PMT: PMT1259(proS)
            PMN: PMN2A_1841
            PMI: PMT9312_0509
            PMB: A9601_05651(proS)
            PMC: P9515_05721(proS)
            PMF: P9303_07441(proS)
            PMG: P9301_05351(proS)
            PMH: P9215_05901
            PME: NATL1_05661(proS)
            TER: Tery_1318
            BTH: BT_0929
            BFR: BF2434
            BFS: BF2515(proS)
            PGI: PG0962(proS)
            SRU: SRU_2541(proS)
            CHU: CHU_3228(proS)
            GFO: GFO_2734(proS)
            FPS: FP1400(proS)
            CTE: CT1491(proS)
            CCH: Cag_0711
            CPH: Cpha266_1877
            PVI: Cvib_1317
            PLT: Plut_1492
            DET: DET0368(proS)
            DEH: cbdb_A310(proS)
            RRS: RoseRS_1775 RoseRS_2277
            RCA: Rcas_2053 Rcas_2992
            DRA: DR_1266
            DGE: Dgeo_0570
            TTH: TTC1889
            TTJ: TTHA0115(pro)
            AAE: aq_365(proS)
            TMA: TM0514
            TPT: Tpet_0408
            MJA: MJ1238(proS)
            MMP: MMP0696(proS)
            MAC: MA3886(proS)
            MBA: Mbar_A0179
            MMA: MM_0707
            MST: Msp_1004(proS)
            MSI: Msm_0287
            MKA: MK1229(proS)
            HAL: VNG0403G(proS)
            HMA: rrnAC0166(proS)
            HWA: HQ1715A(proS)
            NPH: NP1796A(proS)
            TAC: Ta0937
            TVO: TVN1081
            PTO: PTO1364
            PAB: PAB1724(proS)
            PFU: PF1293
            TKO: TK0550
            RCI: RRC469(proS)
            APE: APE_2328
            SSO: SSO0569(proS)
            STO: ST1440
            SAI: Saci_1553
            PAI: PAE2165
            NEQ: NEQ210
STRUCTURES  PDB: 1H4Q  1H4S  1H4T  1HC7  1NJ1  1NJ2  1NJ5  1NJ6  1NJ8  2I4L  
                 2I4M  2I4N  2I4O  2J3L  2J3M  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.15
            ExPASy - ENZYME nomenclature database: 6.1.1.15
            ExplorEnz - The Enzyme Database: 6.1.1.15
            ERGO genome analysis and discovery system: 6.1.1.15
            BRENDA, the Enzyme Database: 6.1.1.15
            CAS: 9055-68-9
///
ENTRY       EC 6.1.1.16                 Enzyme
NAME        cysteine---tRNA ligase;
            cysteinyl-tRNA synthetase;
            cysteinyl-transferRNA synthetase;
            cysteinyl-transfer ribonucleate synthetase;
            cysteine translase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-cysteine:tRNACys ligase (AMP-forming)
REACTION    ATP + L-cysteine + tRNACys = AMP + diphosphate + L-cysteinyl-tRNACys
            [RN:R03650]
ALL_REAC    R03650
SUBSTRATE   ATP [CPD:C00002];
            L-cysteine [CPD:C00097];
            tRNA(Cys) [CPD:C01639]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-cysteinyl-tRNA(Cys) [CPD:C03125]
REFERENCE   1
  AUTHORS   McCorquodale, D.J.
  TITLE     The separation and partial purification of aminoacyl-RNA synthetases
            from Escherichia coli.
  JOURNAL   Biochim. Biophys. Acta 91 (1964) 541-548.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00272  Cysteine metabolism
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01882  cysteinyl-tRNA synthetase
            KO: K01883  cysteinyl-tRNA synthetase
            KO: K01884  cysteinyl-tRNA synthetase
GENES       HSA: 79587(CARS2) 833(CARS)
            PTR: 452665(CARS2)
            MMU: 27267(Cars)
            CFA: 475998(CARS) 476983(CARS2)
            GGA: 418757(CARS2) 423086(CARS)
            XLA: 380479(cars) 398889(MGC68641)
            XTR: 448227(alb) 496832(cars)
            SPU: 593155(LOC593155)
            DME: Dmel_CG8257 Dmel_CG8431(Aats-cys)
            CEL: Y23H5A.7(crs-1)
            ATH: AT2G31170 AT3G56300 AT5G38830
            OSA: 4347821
            CME: CME037C CMH090C
            SCE: YNL247W
            AGO: AGOS_AFR640W
            PIC: PICST_81289(CYR1)
            CAL: CaO19_4931(CaO19.4931)
            CGR: CAGL0J07744g
            SPO: SPAC30.10c
            ANI: AN8800.2
            AFM: AFUA_5G09610
            AOR: AO090023000163
            CNE: CNB00900
            UMA: UM02613.1
            ECU: ECU08_0490
            DDI: DDB_0231318(cysS) DDB_0231320(mcysS)
            PFA: PF10_0149
            CPV: cgd6_960
            CHO: Chro.60125
            TAN: TA03175
            TPV: TP03_0065
            TET: TTHERM_00560000
            TBR: Tb927.6.950
            TCR: 507297.20 507537.30
            LMA: LmjF12.0250
            EHI: 223.t00014
            ECO: b0526(cysS)
            ECJ: JW0515(cysS)
            ECE: Z0681(cysS)
            ECS: ECs0588
            ECC: c0642(cysS)
            ECI: UTI89_C0555(cysS)
            ECP: ECP_0587
            ECV: APECO1_1488(cysS)
            ECW: EcE24377A_0566(cysS)
            ECX: EcHS_A0601(cysS)
            STY: STY0585(cysS)
            STT: t2324(cysS)
            SPT: SPA2186(cysS)
            SEC: SC0576(cysS)
            STM: STM0537(cysS)
            YPE: YPO3073(cysS)
            YPK: y1107(cysS)
            YPM: YP_0852(cysS)
            YPA: YPA_2568
            YPN: YPN_1017
            YPP: YPDSF_2711
            YPS: YPTB1035(cysS)
            YPI: YpsIP31758_3014(cysS)
            SFL: SF0457(cysS)
            SFX: S0465(cysS)
            SFV: SFV_0484(cysS)
            SSN: SSON_0492(cysS)
            SBO: SBO_0417(cysS)
            SDY: SDY_0278(cysS)
            ECA: ECA3151(cysS)
            PLU: plu3804(cysS)
            BUC: BU487(cysS)
            BAS: BUsg471(cysS)
            BAB: bbp431(cysS)
            BCC: BCc_306(cysS)
            WBR: WGLp243(cysS)
            SGL: SG0705
            ENT: Ent638_0980
            KPN: KPN_00482(cysS)
            SPE: Spro_1166
            BFL: Bfl304(cysS)
            BPN: BPEN_312(cysS)
            HIN: HI0078(cysS)
            HIT: NTHI0091(cysS)
            HIP: CGSHiEE_02910(cysS)
            HIQ: CGSHiGG_02970(cysS)
            HDU: HD1093(cysS)
            HSO: HS_0242(cysS)
            PMU: PM0945(cysS)
            MSU: MS0622(cysS)
            APL: APL_0913(cysS)
            ASU: Asuc_1774
            XFA: XF0995
            XFT: PD0287(cysS)
            XCC: XCC2251(cysS)
            XCB: XC_1867
            XCV: XCV2553(cysS)
            XAC: XAC2354(cysS)
            XOO: XOO2678(cysS)
            XOM: XOO_2524(XOO2524)
            VCH: VC1848
            VCO: VC0395_A1439(cysS)
            VVU: VV1_2908
            VVY: VV1362
            VPA: VP1150
            VFI: VF1600
            PPR: PBPRA1098 PBPRB1226(cysS)
            PAE: PA1795(cysS)
            PAU: PA14_41360(cysS)
            PAP: PSPA7_3508(cysS)
            PPU: PP_2905(cysS)
            PPF: Pput_2786
            PST: PSPTO_3742(cysS)
            PSB: Psyr_1735
            PSP: PSPPH_1679(cysS)
            PFL: PFL_3912(cysS)
            PFO: Pfl_3638
            PEN: PSEEN2087(cysS)
            PMY: Pmen_2571
            PAR: Psyc_1361(cysS)
            PCR: Pcryo_1003
            PRW: PsycPRwf_1263
            ACI: ACIAD1481(cysS)
            SON: SO_1791(cysS)
            SDN: Sden_2498
            SFR: Sfri_2599
            SAZ: Sama_1221
            SBL: Sbal_1601
            SBM: Shew185_1590
            SLO: Shew_2511
            SPC: Sputcn32_1487
            SSE: Ssed_1538
            SPL: Spea_2684
            SHE: Shewmr4_2498
            SHM: Shewmr7_2566
            SHN: Shewana3_2664
            SHW: Sputw3181_2614
            ILO: IL1033(cysS)
            CPS: CPS_3792(cysS)
            PHA: PSHAa2065(cysS)
            PAT: Patl_1888
            SDE: Sde_1903
            PIN: Ping_2184
            MAQ: Maqu_1844
            CBU: CBU_1487(cysS)
            CBD: COXBU7E912_0530(cysS)
            LPN: lpg1307(cysS)
            LPF: lpl1270(cysS)
            LPP: lpp1271(cysS)
            MCA: MCA0509(cysS)
            FTU: FTT1616(cysS)
            FTF: FTF1616(cysS)
            FTW: FTW_0301(cysS)
            FTL: FTL_1683
            FTH: FTH_1622(cysS)
            FTA: FTA_1781(cysS)
            FTN: FTN_0310(cysS)
            TCX: Tcr_0923
            NOC: Noc_2249
            AEH: Mlg_1810
            HHA: Hhal_0107
            HCH: HCH_02154(cysS)
            CSA: Csal_2051
            ABO: ABO_2135(cysS)
            MMW: Mmwyl1_2110
            AHA: AHA_2756(cysS)
            DNO: DNO_0208(cysS)
            BCI: BCI_0121(cysS)
            RMA: Rmag_0097
            VOK: COSY_0100(cysS)
            NME: NMB2083
            NMA: NMA0347(cysS)
            NMC: NMC2062(cysS)
            NGO: NGO1993(cysS)
            CVI: CV_1746(cysS)
            RSO: RSc1167(cysS)
            REU: Reut_A1122
            REH: H16_A1221(cysS)
            RME: Rmet_1085 Rmet_1100
            BMA: BMA1656(cysS)
            BMV: BMASAVP1_A2159(cysS)
            BML: BMA10299_A3156(cysS)
            BMN: BMA10247_1432(cysS)
            BXE: Bxe_A1626
            BVI: Bcep1808_1980
            BUR: Bcep18194_A3672 Bcep18194_A5384 Bcep18194_B0590
            BCN: Bcen_5999
            BCH: Bcen2424_2078
            BAM: Bamb_2113
            BPS: BPSL2243(cysS)
            BPM: BURPS1710b_2681(cysS)
            BPL: BURPS1106A_2596(cysS)
            BPD: BURPS668_2545(cysS)
            BTE: BTH_I1941(cysS)
            PNU: Pnuc_0858
            BPE: BP1908(cysS)
            BPA: BPP2283(cysS)
            BBR: BB1735(cysS)
            RFR: Rfer_1349
            POL: Bpro_2865
            PNA: Pnap_2893
            AAV: Aave_2320
            AJS: Ajs_1623
            VEI: Veis_4936
            MPT: Mpe_A2456
            HAR: HEAR1286(cysS) HEAR2781(proS)
            MMS: mma_2108(cysS)
            NEU: NE0043(cysS)
            NET: Neut_0191
            NMU: Nmul_A1881
            EBA: ebA4792(cysS)
            AZO: azo1060(cysS)
            DAR: Daro_0919
            TBD: Tbd_1902
            MFA: Mfla_0500
            HPY: HP0886(cysS)
            HPJ: jhp0818(cysS)
            HPA: HPAG1_0866
            HHE: HH0517(cysS)
            HAC: Hac_1251(cysS)
            WSU: WS0443(cysS)
            TDN: Tmden_1212
            CJE: Cj0802(cysS)
            CJR: CJE0893(cysS)
            CJJ: CJJ81176_0823(cysS)
            CJU: C8J_0753(cysS)
            CJD: JJD26997_1208(cysS)
            CFF: CFF8240_0788(cysS)
            CCV: CCV52592_1142(cysS)
            CHA: CHAB381_0579(cysS)
            CCO: CCC13826_0116(cysS)
            ABU: Abu_0245(cysS)
            NIS: NIS_1101(cysS)
            SUN: SUN_0820(cysS)
            GSU: GSU3365(cysS)
            GME: Gmet_0057
            PCA: Pcar_0100
            DVU: DVU1579(cysS)
            DVL: Dvul_1554
            DDE: Dde_2121
            LIP: LI0608(cysS)
            BBA: Bd2317(cysS)
            DPS: DP2928
            ADE: Adeh_1273
            AFW: Anae109_2496
            MXA: MXAN_2630(cysS)
            SAT: SYN_00075 SYN_03026
            SFU: Sfum_0478 Sfum_1634
            RPR: RP085(cysS)
            RTY: RT0051(cysS)
            RCO: RC0111(cysS)
            RFE: RF_0068(cysS)
            RBE: RBE_1281(cysS)
            RAK: A1C_00615(cysS)
            RBO: A1I_00460(cysS)
            RCM: A1E_00410(cysS)
            RRI: A1G_00675(cysS)
            OTS: OTBS_1958(cysS)
            WOL: WD0149(cysS)
            WBM: Wbm0680
            AMA: AM481(cysS)
            APH: APH_0555(cysS)
            ERU: Erum3250(cysS)
            ERW: ERWE_CDS_03320(cysS)
            ERG: ERGA_CDS_03270(cysS)
            ECN: Ecaj_0308
            ECH: ECH_0768(cysS)
            NSE: NSE_0333(cysS)
            PUB: SAR11_1148(cysS)
            MLO: mlr7799
            MES: Meso_0965
            PLA: Plav_2665
            SME: SMc02551(cysS)
            SMD: Smed_0713
            ATU: Atu1073(cysS)
            ATC: AGR_C_1982
            RET: RHE_CH01425(cysS)
            RLE: RL1543(cysS)
            BME: BMEI1272
            BMF: BAB1_0697
            BMS: BR0677(cysS)
            BMB: BruAb1_0694(cysS)
            BOV: BOV_0670(cysS)
            OAN: Oant_2611
            BJA: blr3790(cysS)
            BRA: BRADO4699(cysS)
            BBT: BBta_3498(cysS)
            RPA: RPA1997(cysS)
            RPB: RPB_3374
            RPC: RPC_2086
            RPD: RPD_2065
            RPE: RPE_1998
            NWI: Nwi_1228(cysS)
            NHA: Nham_1488
            BHE: BH05180(cysS)
            BQU: BQ04370(cysS)
            BBK: BARBAKC583_0481(cysS)
            XAU: Xaut_4717
            CCR: CC_0460
            SIL: SPO2131(cysS)
            SIT: TM1040_1153
            RSP: RSP_2722(cysS)
            RSH: Rsph17029_1380
            RSQ: Rsph17025_2071
            JAN: Jann_1958
            RDE: RD1_3183(cysS)
            PDE: Pden_4063
            MMR: Mmar10_2398
            HNE: HNE_3201(cysS)
            ZMO: ZMO0186(cysS)
            NAR: Saro_2381
            SAL: Sala_0349
            SWI: Swit_0229
            ELI: ELI_08685
            GOX: GOX1776
            GBE: GbCGDNIH1_1136
            ACR: Acry_1404
            RRU: Rru_A0689
            MAG: amb1236
            MGM: Mmc1_0415
            ABA: Acid345_3992
            SUS: Acid_3249
            BSU: BG10156(cysS)
            BHA: BH0111(cysS)
            BAN: BA0089(cysS)
            BAR: GBAA0089(cysS)
            BAA: BA_0678
            BAT: BAS0089
            BCE: BC0110
            BCA: BCE_0089(cysS)
            BCZ: BCZK0085(cysS)
            BCY: Bcer98_0084
            BTK: BT9727_0086(cysS)
            BTL: BALH_0089(cysS)
            BLI: BL03269(cysS)
            BLD: BLi00112(cysS)
            BCL: ABC0129(cysS)
            BAY: RBAM_001190(cysS)
            BPU: BPUM_0079(cysS)
            OIH: OB0099(cysS)
            GKA: GK0085
            GTN: GTNG_0085
            SAU: SA0488(cysS)
            SAV: SAV0530(cysS)
            SAM: MW0485(cysS)
            SAR: SAR0533(cysS)
            SAS: SAS0487
            SAC: SACOL0576(cysS)
            SAB: SAB0480(cysS)
            SAA: SAUSA300_0515(cysS)
            SAO: SAOUHSC_00511
            SAJ: SaurJH9_0552
            SAH: SaurJH1_0566
            SEP: SE0292
            SER: SERP0170(cysS)
            SHA: SH2479(cysS)
            SSP: SSP2226
            LMO: lmo0239(cysS)
            LMF: LMOf2365_0251(cysS)
            LIN: lin0271(cysS)
            LWE: lwe0202(cysS)
            LLA: L0348(cysS)
            LLC: LACR_2043
            LLM: llmg_2040(cysS)
            SPY: SPy_1941(cysS)
            SPZ: M5005_Spy_1655(cysS)
            SPM: spyM18_2008
            SPG: SpyM3_1672(cysS)
            SPS: SPs1673
            SPH: MGAS10270_Spy1723(cysS)
            SPI: MGAS10750_Spy1749(cysS)
            SPJ: MGAS2096_Spy1678(cysS)
            SPK: MGAS9429_Spy1656(cysS)
            SPF: SpyM51628(cysS)
            SPA: M6_Spy1663
            SPB: M28_Spy1643(cysS)
            SPN: SP_0591
            SPR: spr0519(cysS)
            SPD: SPD_0515(cysS)
            SAG: SAG0207(cysS)
            SAN: gbs0202(cysS)
            SAK: SAK_0270(cysS)
            SMU: SMU.158(cysS)
            STC: str0084(cysS)
            STL: stu0084(cysS)
            STE: STER_0117
            SSA: SSA_2044(cysS)
            SSU: SSU05_1924
            SSV: SSU98_1929
            SGO: SGO_0349(cysS)
            LPL: lp_0610(cysS)
            LJO: LJ0400
            LAC: LBA0348
            LSA: LSA1681(cysS)
            LSL: LSL_1247(cysS)
            LDB: Ldb1680(cysS)
            LBU: LBUL_1554
            LBR: LVIS_0580
            LCA: LSEI_2308
            LGA: LGAS_0338
            LRE: Lreu_0303
            PPE: PEPE_1500
            EFA: EF0045(cysS)
            OOE: OEOE_1559
            LME: LEUM_0162
            STH: STH3119(cysS)
            CAC: CAC3177(cysS)
            CPE: CPE2427(cysS)
            CPF: CPF_2737(cysS)
            CPR: CPR_2424(cysS)
            CTC: CTC02622
            CNO: NT01CX_1093(cysS)
            CTH: Cthe_2065
            CDF: CD0052(cysS)
            CBO: CBO3501(cysS)
            CBA: CLB_3561(cysS)
            CBH: CLC_3450(cysS)
            CBF: CLI_3688(cysS)
            CBE: Cbei_0131
            CKL: CKL_0201(cysS)
            AMT: Amet_4501
            CHY: CHY_2338(cysS)
            DSY: DSY0447
            DRM: Dred_0193
            PTH: PTH_0295(cysS)
            CSC: Csac_0708
            TTE: TTE2315(cysS)
            MTA: Moth_2484
            MGE: MG_253(cysS)
            MPN: MPN356(cysS)
            MPU: MYPU_1770(cysS)
            MPE: MYPE220(cysS)
            MGA: MGA_0533(cysS)
            MMY: MSC_0959(cysS)
            MMO: MMOB1480(cysS)
            MHY: mhp661(cysS)
            MHJ: MHJ_0641(cysS)
            MHP: MHP7448_0641(cysS)
            MSY: MS53_0357(cysS)
            MCP: MCAP_0110(cysS)
            UUR: UU123(cysS)
            POY: PAM141(cysS)
            AYW: AYWB_579(cysS)
            MFL: Mfl087
            MTU: Rv2130c(cysS2) Rv3580c(cysS1)
            MTC: MT2188(cysS-1) MT3686(cysS-2)
            MBO: Mb2154c(cysS2) Mb3611c(cysS1)
            MBB: BCG_3645c(cysS1)
            MLE: ML0323(cysS) ML1302(cysS2)
            MPA: MAP0478(cysS) MAP1876c(cysS2)
            MAV: MAV_0573(cysS) MAV_2361(cysS)
            MSM: MSMEG_4189(cysS) MSMEG_6074(cysS)
            MVA: Mvan_3478 Mvan_5338
            MGI: Mflv_1446 Mflv_3049
            MMC: Mmcs_3153 Mmcs_4737
            MKM: Mkms_3215 Mkms_4823
            MJL: Mjls_3165 Mjls_5123
            CGL: NCgl1457(cysS) NCgl2552(cysS)
            CGB: cg1709(cysS2) cg2924(cysS)
            CEF: CE1639(cysS) CE2516
            CDI: DIP1261(cysS2) DIP1971(cysS1)
            CJK: jk0313(cysS3) jk0368(cysS2) jk0956(cysS1)
            NFA: nfa29340(cysS2)
            RHA: RHA1_ro00877 RHA1_ro04462(cysS)
            SCO: SCO1663(SCI52.05c) SCO4235(SCD8A.08)
            SMA: SAV3967(cysS) SAV6647(mshC)
            TWH: TWT316(cysS2) TWT347(cysS1)
            TWS: TW423(cysS1) TW456(cysS2)
            LXX: Lxx18240(cysS)
            ART: Arth_0730 Arth_2168
            AAU: AAur_0901(cysS)
            PAC: PPA0384
            NCA: Noca_1016 Noca_2628 Noca_4021
            TFU: Tfu_0212 Tfu_1832
            FRA: Francci3_2642 Francci3_4251
            FAL: FRAAL2858(cysS2) FRAAL6521(cysS1)
            ACE: Acel_0082 Acel_1172 Acel_1446
            KRA: Krad_0911 Krad_1836
            SEN: SACE_0443(cysS) SACE_2226(cysS2) SACE_2667(cysS)
            STP: Strop_2168 Strop_4222
            BLO: BL0301(cysS)
            BAD: BAD_0212(cysS)
            RXY: Rxyl_2173
            FNU: FN1579
            RBA: RB4675(cysS)
            CTR: CT782(cysS)
            CTA: CTA_0852(cysS)
            CMU: TC0164
            CPN: CPn0932(cysS)
            CPA: CP0931
            CPJ: CPj0932(cysS)
            CPT: CpB0966
            CCA: CCA00838(cysS)
            CAB: CAB806
            CFE: CF0175(cysS)
            PCU: pc1235(cysS)
            BBU: BB0599(cysS)
            BGA: BG0612(cysS)
            BAF: BAPKO_0631(cysS)
            TPA: TP0091
            TDE: TDE0092(cysS)
            LIL: LA1863(cysS)
            LIC: LIC12028(cysS)
            LBJ: LBJ_1653(cysS)
            LBL: LBL_1872(cysS)
            SYN: slr0958(cysS)
            SYW: SYNW0701(cysRS)
            SYC: syc2426_d(cysS)
            SYF: Synpcc7942_1662
            SYD: Syncc9605_1967
            SYE: Syncc9902_0692
            SYG: sync_0924(cysS)
            SYR: SynRCC307_1670(cysS)
            SYX: SynWH7803_1618(cysS)
            CYA: CYA_1896(cysS)
            CYB: CYB_1821(cysS)
            TEL: tlr1827(cysS)
            GVI: glr0851(cysS)
            ANA: all1092(cysS)
            AVA: Ava_3718(cysS)
            PMA: Pro1235(cysS)
            PMM: PMM1141(cysS)
            PMT: PMT1159(cysRS)
            PMN: PMN2A_0749
            PMI: PMT9312_1237
            PMB: A9601_13161(cysS)
            PMC: P9515_13051(cysS)
            PMF: P9303_08671(cysS)
            PMG: P9301_13301(cysS)
            PMH: P9215_13451(cysS)
            PME: NATL1_15891(cysS)
            TER: Tery_4002
            BTH: BT_3351
            BFR: BF0196
            BFS: BF0161(cysS)
            PGI: PG1878(cysS)
            SRU: SRU_1014(cysS)
            CHU: CHU_3418(cysS)
            GFO: GFO_2741(cysS)
            FJO: Fjoh_2268
            FPS: FP0598(cysS)
            CTE: CT2158(cysS)
            CCH: Cag_1818(cysS)
            CPH: Cpha266_2392
            PVI: Cvib_0277
            PLT: Plut_0211(cysS)
            DET: DET0061(cysS)
            DEH: cbdb_A76(cysS)
            DEB: DehaBAV1_0055
            RRS: RoseRS_3036 RoseRS_3331
            RCA: Rcas_2138
            DRA: DR_0705 DR_1670
            DGE: Dgeo_1714
            TTH: TTC0094 TTC0537
            TTJ: TTHA0893
            AAE: aq_1068(cysS)
            TMA: TM0719 TM1410
            TPT: Tpet_0210
            TME: Tmel_0064
            FNO: Fnod_0679
            MJA: MJ1238(proS) MJ1477
            MMP: MMP1060
            MMQ: MmarC5_0534 MmarC5_0880
            MMZ: MmarC7_0313 MmarC7_1723
            MVN: Mevan_0170 Mevan_0382
            MAC: MA0749(cysS)
            MBA: Mbar_A1653
            MMA: MM_1911
            MBU: Mbur_0190
            MTP: Mthe_1640
            MHU: Mhun_1139 Mhun_2176
            MEM: Memar_2042
            MBN: Mboo_1963 Mboo_1992
            MST: Msp_0124(cysS)
            MSI: Msm_0268
            AFU: AF0411(cysS)
            HAL: VNG1097G(cysS)
            HMA: rrnAC1292(cysS)
            HWA: HQ1654A(cysS)
            NPH: NP4440A(cysS)
            TAC: Ta1147
            TVO: TVN1244
            PTO: PTO0084
            PHO: PH0636
            PAB: PAB0931(cysS)
            PFU: PF1024
            TKO: TK0444
            RCI: RRC371(cysS)
            APE: APE_1592.1
            SMR: Smar_0517
            IHO: Igni_0991
            HBU: Hbut_1188
            SSO: SSO2280(cysS)
            STO: ST2244
            SAI: Saci_0152(cysRS)
            MSE: Msed_2077
            PAI: PAE0821
            PIS: Pisl_0822 Pisl_1108
            PCL: Pcal_0031 Pcal_1092
            PAS: Pars_0065 Pars_0803
            TPE: Tpen_0817 Tpen_0902
            NEQ: NEQ055
STRUCTURES  PDB: 1LI5  1LI7  1U0B  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.16
            ExPASy - ENZYME nomenclature database: 6.1.1.16
            ExplorEnz - The Enzyme Database: 6.1.1.16
            ERGO genome analysis and discovery system: 6.1.1.16
            BRENDA, the Enzyme Database: 6.1.1.16
            CAS: 37318-56-2
///
ENTRY       EC 6.1.1.17                 Enzyme
NAME        glutamate---tRNA ligase;
            glutamyl-tRNA synthetase;
            glutamyl-transfer ribonucleate synthetase;
            glutamyl-transfer RNA synthetase;
            glutamyl-transfer ribonucleic acid synthetase;
            glutamate-tRNA synthetase;
            glutamic acid translase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-glutamate:tRNAGlu ligase (AMP-forming)
REACTION    ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu
            [RN:R05578]
ALL_REAC    R05578
SUBSTRATE   ATP [CPD:C00002];
            L-glutamate [CPD:C00025];
            tRNA(Glu) [CPD:C01641]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-glutamyl-tRNA(Glu) [CPD:C02987]
REFERENCE   1
  AUTHORS   Ravel, J.M., Wang, S., Heinemeyer, C. and Shive, W.
  TITLE     Glutamyl and glutaminyl ribonucleic acid synthetases of Escherichia
            coli W. Separation, properties, and stimulation of adenosine
            triphosphate-pyrophosphate exchange by acceptor ribonucleic acid.
  JOURNAL   J. Biol. Chem. 240 (1965) 432-438.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00860  Porphyrin and chlorophyll metabolism
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01885  glutamyl-tRNA synthetase
GENES       HSA: 124454(EARS2) 2058(EPRS)
            MMU: 107508(Eprs) 67417(Ears2)
            RNO: 289352(Eprs)
            CFA: 478962(EPRS)
            GGA: 421348(EPRS) 427672(RCJMB04_20f12)
            XTR: 493404(MGC79577)
            DRE: 751732(zgc:153247)
            SPU: 581596(LOC581596) 583633(LOC583633)
            DME: Dmel_CG4573
            CEL: T07A9.2(ers-3) ZC434.5(ers-2)
            ATH: AT5G26710 AT5G64050(ATERS/ERS/OVA3)
            OSA: 4325167 4328118
            CME: CMC083C CMS192C
            SCE: YGL245W(GUS1) YOL033W(MSE1)
            AGO: AGOS_AEL338C AGOS_AFR264W
            PIC: PICST_57984(MSE1) PICST_89978(SYE1)
            CGR: CAGL0C01947g CAGL0F01133g
            SPO: SPAC17A5.15c SPAPB1A10.11c
            ANI: AN7361.2 AN8224.2
            AFM: AFUA_2G16280 AFUA_5G03560
            AOR: AO090011000526 AO090102000234 AO090102000566
            CNE: CNF00070 CNK01030
            UMA: UM02432.1
            DDI: DDB_0231321(gluS) DDB_0231322(mgluS)
            PFA: MAL13P1.281 PF13_0170 PF13_0257 PFL0670c
            CHO: Chro.80098
            TAN: TA06725 TA17035
            TPV: TP01_0727 TP01_1053
            TET: TTHERM_00420680 TTHERM_00471840 TTHERM_00974260
            TBR: Tb927.6.4590
            TCR: 506831.70 511731.60
            LMA: LmjF30.3240
            EHI: 23.t00028
            ECO: b2400(gltX)
            ECJ: JW2395(gltX)
            ECE: Z3665(gltX)
            ECS: ECs3278
            ECC: c2936(gltX)
            ECI: UTI89_C2731(gltX)
            ECP: ECP_0154 ECP_2422
            ECV: APECO1_4141(gltX)
            ECW: EcE24377A_2689(gltX)
            ECX: EcHS_A2537(gltX)
            STY: STY2654(gltX)
            STT: t0442(gltX)
            SPT: SPA0446(gltX)
            SEC: SC2416(gltX)
            STM: STM2415(gltX)
            YPE: YPO2984(gltX)
            YPK: y1498(gltX)
            YPM: YP_2609(gltX)
            YPA: YPA_2173
            YPN: YPN_0691 YPN_1398
            YPP: YPDSF_2092 YPDSF_2958
            YPS: YPTB2707(gltX)
            YPI: YpsIP31758_1325(gltX)
            YEN: YE1215(gltX)
            SFL: SF2462(gltX)
            SFX: S2605(gltX)
            SFV: SFV_2455(gltX)
            SSN: SSON_2491(gltX)
            SBO: SBO_2426(gltX)
            SDY: SDY_2600(gltX)
            ECA: ECA3291(gltX)
            PLU: plu1401(gltX)
            BUC: BU070(gltX)
            BAS: BUsg065(gltX)
            BAB: bbp065(gltX)
            BCC: BCc_042(gltX)
            WBR: WGLp126(gltX)
            SGL: SG1676
            ENT: Ent638_0684
            SPE: Spro_3986
            BFL: Bfl504(gltX)
            BPN: BPEN_521(gltX)
            HIN: HI0274(gltX)
            HIT: NTHI0382(gltX)
            HIP: CGSHiEE_01680(gltX)
            HDU: HD0320(gltX)
            HSO: HS_0456(gltX)
            PMU: PM1115(gltX_2)
            MSU: MS0490(glnS)
            APL: APL_1275(gltX)
            XFA: XF0822
            XFT: PD1848(gltX)
            XCC: XCC2293 XCC2686(gluS)
            XCB: XC_1429 XC_1822
            XCV: XCV2597(yadB) XCV3007(gltX)
            XAC: XAC2400 XAC2847(gluS)
            XOO: XOO1504(gluS) XOO2727
            XOM: XOO_1394(XOO1394) XOO_2572(XOO2572)
            VCH: VC2214
            VCO: VC0395_A1806(gltX)
            VVU: VV1_0236
            VVY: VV0949
            VPA: VP0762
            VFI: VF1887(gltX)
            PPR: PBPRA0874
            PAE: PA3134(gltX) PA4724
            PAU: PA14_23560(gltX) PA14_62510(yadB)
            PAP: PSPA7_1994(gltX)
            PPU: PP_1977(gltX) PP_4694
            PST: PSPTO_0967 PSPTO_2166(gltX)
            PSB: Psyr_0834(glu) Psyr_1977
            PSP: PSPPH_0860 PSPPH_1942(gltX)
            PFL: PFL_2049(gltX) PFL_5271
            PFO: Pfl_1878 Pfl_4805
            PEN: PSEEN1639(gltX) PSEEN4727
            PAR: Psyc_2057(gltX)
            PCR: Pcryo_2341 Pcryo_2381
            PRW: PsycPRwf_0179
            ACI: ACIAD0272 ACIAD3371(gltX)
            ACB: A1S_3210
            SDN: Sden_2533 Sden_3171
            SFR: Sfri_2714 Sfri_3277
            SAZ: Sama_2207
            SBL: Sbal_2802 Sbal_3491
            SBM: Shew185_0848
            SLO: Shew_1449 Shew_3130
            SPC: Sputcn32_3129
            SHE: Shewmr4_1365
            SHM: Shewmr7_1430
            SHN: Shewana3_1418
            SHW: Sputw3181_0814 Sputw3181_1509
            ILO: IL1770(gltX)
            CPS: CPS_3216(gltX)
            PHA: PSHAa0605(queB) PSHAa0635(gltX)
            PAT: Patl_2919 Patl_3936
            SDE: Sde_1496 Sde_3373
            PIN: Ping_0583 Ping_1626
            MAQ: Maqu_0673 Maqu_1891
            CBU: CBU_0205(gltX-1) CBU_1488(gltX-2)
            CBD: COXBU7E912_0531(gltX1) COXBU7E912_1892(gltX2)
            LPN: lpg1911(gltX)
            LPF: lpl1875(gltX)
            LPP: lpp1886(gltX)
            MCA: MCA0510(gltX-1) MCA0518 MCA1234(gltX-2)
            FTU: FTT0307(gltX)
            FTF: FTF0307(gltX)
            FTW: FTW_1778(gltX)
            FTL: FTL_0218
            FTH: FTH_0213(gltX)
            FTA: FTA_0234(gltX)
            FTN: FTN_0221(gltX)
            TCX: Tcr_1216
            NOC: Noc_0264 Noc_2250
            AEH: Mlg_0676 Mlg_1302 Mlg_1811
            HHA: Hhal_1274
            HCH: HCH_02111(gltX) HCH_06257
            CSA: Csal_1211 Csal_3061
            ABO: ABO_0344(gltX) ABO_1509(gltX)
            MMW: Mmwyl1_4012
            AHA: AHA_3447(gltX)
            DNO: DNO_0734(gltX)
            BCI: BCI_0456(gltX)
            CRP: CRP_101
            RMA: Rmag_0474
            VOK: COSY_0437(gltX)
            NME: NMB0003 NMB0349
            NMA: NMA0250(gltX) NMA2138(glu)
            NMC: NMC2141(gltX)
            NGO: NGO1611 NGO1926(gltX)
            CVI: CV_1937(gltX) CV_3433
            RSO: RSc1179(gltX) RSc2210(RS01389)
            REU: Reut_A0900 Reut_A2123
            REH: H16_A2403(gltX1) H16_A2716(gltX2)
            RME: Rmet_2140 Rmet_2581
            BMA: BMA1600(gltX) BMA1915(glu)
            BMV: BMASAVP1_A2103(gltX)
            BML: BMA10299_A3210(gltX)
            BMN: BMA10247_1376(gltX)
            BXE: Bxe_A1642 Bxe_A3294
            BVI: Bcep1808_2404
            BUR: Bcep18194_A5365(gltX) Bcep18194_A5657
            BCN: Bcen_1703 Bcen_6021
            BCH: Bcen2424_2056 Bcen2424_2315
            BAM: Bamb_2088 Bamb_2354
            BPS: BPSL1115 BPSL2197(gltX)
            BPM: BURPS1710b_1353 BURPS1710b_2628(gltX)
            BPL: BURPS1106A_0122 BURPS1106A_2541(gltX)
            BPD: BURPS668_2487(gltX) BURPS668_3642
            BTE: BTH_I0982 BTH_I1984(gltX)
            PNU: Pnuc_0605
            BPE: BP2978(gltX)
            BPA: BPP3898(gltX) BPP4372
            BBR: BB4371(gltX) BB4958
            RFR: Rfer_1905 Rfer_2681
            POL: Bpro_1609 Bpro_2904
            PNA: Pnap_2934
            AAV: Aave_3032
            AJS: Ajs_1982
            VEI: Veis_4720
            MPT: Mpe_A2149
            HAR: HEAR0981(gltX)
            MMS: mma_0529 mma_1113(gltX)
            NEU: NE1624(gltX)
            NET: Neut_0499
            NMU: Nmul_A0797 Nmul_A1604
            EBA: ebA4133 ebA6855(gltX)
            AZO: azo0745 azo1479(gltX2)
            DAR: Daro_1321 Daro_3769
            TBD: Tbd_1734 Tbd_2709
            MFA: Mfla_1109 Mfla_1590
            HPY: HP0476(gltX) HP0643(gltX)
            HPJ: jhp0428(gltX_1) jhp0588(gltX_2)
            HPA: HPAG1_0453 HPAG1_0628
            HHE: HH0582(gltX) HH0926(gltX)
            HAC: Hac_1071(gltX) Hac_1093(gltRS)
            WSU: WS0274(gltX) WS2217(gltX)
            TDN: Tmden_0145 Tmden_1059
            CJE: Cj0845c(gltX) Cj1288c(gltX2)
            CJR: CJE0932(gltX) CJE1480(gltX)
            CJJ: CJJ81176_0861(gltX-1) CJJ81176_1305(gltX-2)
            CJU: C8J_0792(gltX) C8J_1231(gltX2)
            CJD: JJD26997_0434(gltX-2) JJD26997_0994(gltX-1)
            CFF: CFF8240_0105(gltX) CFF8240_1562(gltX)
            CCV: CCV52592_0438(gltX) CCV52592_0548(gltX)
            CHA: CHAB381_0111(gltX) CHAB381_1380(gltX)
            CCO: CCC13826_0242(gltX) CCC13826_0468 CCC13826_0929
                 CCC13826_1548(gltX)
            ABU: Abu_0058(gltX1) Abu_1214(gltX2)
            NIS: NIS_0801 NIS_1641(gltX)
            SUN: SUN_0108 SUN_1138
            GSU: GSU1219(gltX) GSU1329
            GME: Gmet_1736 Gmet_1780
            PCA: Pcar_1650 Pcar_2698
            PPD: Ppro_3371
            DVU: DVU1693(gltX-1) DVU2552(gltX-2)
            DDE: Dde_2004 Dde_2648
            LIP: LI0462(gltX)
            BBA: Bd2319(gltX)
            DPS: DP2737
            ADE: Adeh_0295 Adeh_2597
            AFW: Anae109_0319
            MXA: MXAN_1271 MXAN_2675(gltX)
            SAT: SYN_01399 SYN_02557
            SFU: Sfum_1366
            RPR: RP325(gltX) RP623(gltX)
            RTY: RT0316(gltX) RT0614(gltX)
            RCO: RC0448(gltX) RC0966(gltX)
            RFE: RF_0413(gltX) RF_0529(gltX)
            RBE: RBE_0457(gltX2) RBE_0711(gltX1)
            RAK: A1C_02435(gltX) A1C_04895(gltX)
            RBO: A1I_04650(gltX) A1I_05405(gltX)
            RCM: A1E_01635(gltX)
            RRI: A1G_02535(gltX) A1G_05305(gltX)
            OTS: OTBS_0573(gltX) OTBS_1957(gltX)
            WOL: WD0435(gltX) WD0778(gltX)
            WBM: Wbm0445 Wbm0453
            AMA: AM039(gltX) AM775(gltX2)
            APH: APH_0072(gltX-1) APH_0408(gltX-2)
            ERU: Erum4310(gltX2) Erum7610(gltX)
            ERW: ERWE_CDS_04490(gltX2) ERWE_CDS_08020(gltX1)
            ERG: ERGA_CDS_04420(gltX2) ERGA_CDS_07930(gltX1)
            ECN: Ecaj_0432 Ecaj_0795(gltX)
            ECH: ECH_0208(gltX-1) ECH_0605(gltX-2)
            NSE: NSE_0518(gltX-1) NSE_0737(gltX-2)
            PUB: SAR11_0920(gltX)
            MLO: mll0813 mlr0628
            MES: Meso_1535 Meso_1645
            SME: SMc03172(gltX)
            ATU: Atu4474(gltX)
            ATC: AGR_L_791
            RET: RHE_CH03656(gltX1) RHE_CH03786(gltX2)
            RLE: RL4184(gltX)
            BME: BMEI0837(gltX) BMEI0968(gltX)
            BMF: BAB1_1034(gltX-1) BAB1_1169
            BMS: BR1016(gltX-1) BR1147(gltX-2)
            BMB: BruAb1_1021(gltX) BruAb1_1153(gltX)
            BOV: BOV_0983(gltX-1) BOV_1105(gltX-2)
            BJA: blr4838(gltX)
            BRA: BRADO4125(gltX) BRADO6498
            BBT: BBta_1135 BBta_4501(gltX)
            RPA: RPA2906(gltX)
            RPB: RPB_2812
            RPC: RPC_2451
            RPD: RPD_2842
            RPE: RPE_2568 RPE_4854
            NWI: Nwi_0748 Nwi_1844(gltX)
            NHA: Nham_1709 Nham_3486
            BHE: BH06390(gltX1) BH06460(gltX2)
            BQU: BQ06770(gltX1) BQ06840(gltX2)
            BBK: BARBAKC583_0600(gltX1) BARBAKC583_0607(gltX2)
            CCR: CC_1905
            SIL: SPO0430(gltX) SPO2156(gltX-2)
            SIT: TM1040_1133 TM1040_1393 TM1040_2275
            RSP: RSP_0797(gltX) RSP_1995(gltX)
            RSQ: Rsph17025_1164
            JAN: Jann_1842 Jann_2500 Jann_3636
            RDE: RD1_1219(gltX) RD1_2608 RD1_3218(gltX)
            MMR: Mmar10_0986 Mmar10_1396
            HNE: HNE_1783(gltX1) HNE_2579(gltX2)
            ZMO: ZMO0900(gltX) ZMO1964(gltX)
            NAR: Saro_0967 Saro_2031
            SAL: Sala_0830 Sala_2945
            ELI: ELI_06540 ELI_14480
            GOX: GOX1268 GOX1772(gltX) GOX1954(glu)
            GBE: GbCGDNIH1_0814 GbCGDNIH1_1416
            RRU: Rru_A0688 Rru_A1601 Rru_A3734
            MAG: amb1235 amb2803
            MGM: Mmc1_0944 Mmc1_3652
            ABA: Acid345_0051 Acid345_0184 Acid345_3027
            BHA: BH0109(gltX)
            BCE: BC0108(gltX)
            BCL: ABC0127(gltX) ABC0263
            BAY: RBAM_001170(gltX)
            BPU: BPUM_0077(gltX)
            OIH: OB0096(gltX)
            GKA: GK0083
            SAU: SA0486(gltX)
            SAV: SAV0528(gltX)
            SAM: MW0483(gltX)
            SAR: SAR0531(gltX)
            SAS: SAS0485
            SAC: SACOL0574(gltX)
            SAB: SAB0478(gltX)
            SAA: SAUSA300_0513(gltX)
            SAO: SAOUHSC_00509
            SEP: SE0290
            SER: SERP0168(gltX)
            SHA: SH2481(gltX)
            SSP: SSP2228
            LMO: lmo0237(gltX)
            LMF: LMOf2365_0249(gltX)
            LIN: lin0269(gltX)
            LWE: lwe0200(gltX)
            LLA: L0349(gltX)
            LLC: LACR_2346
            LLM: llmg_2332(gltX)
            SPY: SPy_0239(gltX)
            SPZ: M5005_Spy_0203(gltX)
            SPM: spyM18_0223(gluS)
            SPG: SpyM3_0170(gluS)
            SPS: SPs0177
            SPH: MGAS10270_Spy0202(gltX)
            SPI: MGAS10750_Spy0198(gltX)
            SPJ: MGAS2096_Spy0217 MGAS2096_Spy0218(gltX)
            SPK: MGAS9429_Spy0204(gltX)
            SPF: SpyM50182(gltX)
            SPA: M6_Spy0234(gltX)
            SPB: M28_Spy0197(gltX)
            SPN: SP_2069
            SPR: spr1881(gltX)
            SPD: SPD_1896(gltX)
            SAG: SAG0113(gltX)
            SAN: gbs0112
            SAK: SAK_0165(gltX)
            SMU: SMU.330(gltX)
            STC: str1814(gltX)
            STL: stu1814(gltX)
            STE: STER_1793
            SSA: SSA_2144(gltX)
            SSV: SSU98_2027
            SGO: SGO_0174(gltX)
            LPL: lp_0609(gltX)
            LJO: LJ0399
            LAC: LBA0347(gltX)
            LSA: LSA0290(gltX)
            LSL: LSL_1248(glnS)
            LDB: Ldb1685(gltX)
            LBU: LBUL_1560
            LBR: LVIS_0579
            LCA: LSEI_2313
            LGA: LGAS_0337
            PPE: PEPE_1501
            EFA: EF0043(gltX)
            OOE: OEOE_0321
            STH: STH16(gltX) STH2668(gluS)
            CAC: CAC0990(gltX)
            CPE: CPE0998(gltX)
            CPF: CPF_1255(gltX)
            CPR: CPR_1067(gltX)
            CTC: CTC00977
            CNO: NT01CX_1614(gltX)
            CDF: CD0051(gltX)
            CBO: CBO1094(gltX)
            CBA: CLB_1134(gltX)
            CBH: CLC_1146(gltX)
            CBF: CLI_1183(gltX)
            CKL: CKL_1456(gluS)
            CHY: CHY_2340(gltX)
            DSY: DSY0445
            SWO: Swol_0930 Swol_2357
            TTE: TTE0929(glnS) TTE2317(glnS2)
            MTA: Moth_1132
            MGE: MG_462(gltX)
            MPN: MPN678(gltX)
            MPU: MYPU_6810(gltX) MYPU_6820(gltX)
            MPE: MYPE10370(gltX)
            MGA: MGA_0594(glnS)
            MMY: MSC_0131(gltX)
            MMO: MMOB0050(gltX)
            MHY: mhp241(gltX)
            MHJ: MHJ_0137(gltX)
            MHP: MHP7448_0141(gltX)
            MSY: MS53_0100(gltX)
            MCP: MCAP_0130(gltX)
            UUR: UU599(gltX)
            POY: PAM140(glnS)
            AYW: AYWB_580(glnS)
            MFL: Mfl651
            MTU: Rv2992c(gltX)
            MTC: MT3070(gltX)
            MBO: Mb3016c(gltX)
            MBB: BCG_3013c(gltS)
            MLE: ML1688(gltS)
            MPA: MAP3029c(gltS)
            MSM: MSMEG_2383(gltX) MSMEG_6306(gltX)
            MVA: Mvan_5575
            MGI: Mflv_1233 Mflv_4229
            MMC: Mmcs_1919 Mmcs_4941
            MKM: Mkms_1965 Mkms_5029
            MJL: Mjls_1899 Mjls_5322
            CGL: NCgl0233(cgl0236) NCgl1244(gltX)
            CGB: cg0289(gltX) cg1463(gltX)
            CEF: CE0203 CE1389
            CDI: DIP0252 DIP1115(gltX)
            CJK: jk1281(gltS) jk2018(gltX)
            NFA: nfa2690 nfa42160(gltX) nfa46970 nfa46980
            RHA: RHA1_ro04178(gltX1) RHA1_ro06493(gltX2)
            SCO: SCO5547(gltX)
            SMA: SAV2691(gltS)
            TWH: TWT209(gltX)
            TWS: TW563(gltX)
            LXX: Lxx13080(gltS)
            CMI: CMM_1108(gluS)
            ART: Arth_3985
            AAU: AAur_2494(gltX)
            PAC: PPA1383 PPA1869
            TFU: Tfu_0623
            FRA: Francci3_3219
            FAL: FRAAL5260(gltX)
            ACE: Acel_0714
            SEN: SACE_6148(gltX)
            BLO: BL0469(gltX)
            BAD: BAD_0176(gltX) BAD_1473(gluQ)
            RXY: Rxyl_2856
            FNU: FN1340
            RBA: RB13261 RB7600(gltX)
            CTR: CT445(gltX)
            CTA: CTA_0486(gltX)
            CMU: TC0730
            CPN: CPn0560(gltX)
            CPA: CP0190
            CPJ: CPj0560(gltX)
            CPT: CpB0582
            CCA: CCA00182(gltX)
            CAB: CAB179(gltX)
            CFE: CF0824(gltX)
            PCU: pc0244(gltX)
            BBU: BB0372(gltX)
            BGA: BG0371(gltX)
            BAF: BAPKO_0381(gltX)
            TPA: TP0673
            TDE: TDE0204(gltX)
            LIL: LA4190(gltX)
            LIC: LIC13345(gltX)
            LBJ: LBJ_2815(glnS)
            LBL: LBL_0256(glnS)
            SYN: sll0179(gltX)
            SYW: SYNW1826(gltX)
            SYC: syc1712_c(gltX)
            SYF: Synpcc7942_0922 Synpcc7942_2393
            SYD: Syncc9605_0641(gltX) Syncc9605_2091
            SYE: Syncc9902_0580 Syncc9902_1719(gltX)
            SYG: sync_2163(gltX) sync_2190(glnS)
            SYR: SynRCC307_0482 SynRCC307_1666(gltX)
            SYX: SynWH7803_1836(gltX)
            CYA: CYA_2715(gltX)
            CYB: CYB_1680(gltX)
            TEL: tll0506(gltX)
            GVI: gll2378(gltX)
            ANA: all3205(gltX)
            AVA: Ava_4861(gltX)
            PMA: Pro0471(gltX)
            PMM: PMM0473(gltX)
            PMT: PMT1308(gltX)
            PMN: PMN2A_1806
            PMI: PMT9312_0473
            PMB: A9601_05281(gltX)
            PMC: P9515_05371(gltX)
            PMF: P9303_05721 P9303_06791(gltX)
            PMG: P9301_04981(gltX)
            PME: NATL1_05291(gltX)
            BTH: BT_2748
            BFR: BF4206
            BFS: BF4030(gltX)
            PGI: PG1566(gltX)
            SRU: SRU_1796(gltX)
            CHU: CHU_3373(gltX)
            GFO: GFO_3302(gltX)
            FPS: FP2499(gltX)
            CTE: CT0299(gltX)
            CCH: Cag_0392
            CPH: Cpha266_0427
            PLT: Plut_1721
            DET: DET1365(gltX)
            DEH: cbdb_A1316(gltX)
            DRA: DR_0485 DR_1687
            DGE: Dgeo_1023 Dgeo_1539
            TTH: TTC0070
            TTJ: TTHA0438
            AAE: aq_1221(gltX)
            TMA: TM1351 TM1875
            MJA: MJ1377(gltX)
            MMP: MMP1011(gltX)
            MMQ: MmarC5_0583
            MMZ: MmarC7_0253
            MAE: Maeo_1110
            MVN: Mevan_0338
            MAC: MA0587(gltX)
            MBA: Mbar_A1470
            MMA: MM_1749(gltX)
            MBU: Mbur_2335
            MTP: Mthe_1466
            MHU: Mhun_2885
            MEM: Memar_1817
            MBN: Mboo_2208
            MTH: MTH51(gltX)
            MST: Msp_0923(gltX)
            MSI: Msm_1452
            MKA: MK0757(glnS)
            HAL: VNG1153G(gltS)
            HWA: HQ2888A(gltS)
            NPH: NP3694A(gltX)
            TAC: Ta0942
            TVO: TVN1086
            PTO: PTO0878(gltX)
            PAB: PAB0323(gltX)
            PFU: PF1753
            TKO: TK1408
            RCI: LRC306(gluS)
            APE: APE_2317.1
            SMR: Smar_0824
            IHO: Igni_1110
            HBU: Hbut_0542
            SSO: SSO0093(gltX)
            STO: ST1423
            SAI: Saci_1519
            MSE: Msed_2131
            PAI: PAE2969
            PIS: Pisl_0371
            PCL: Pcal_1137
            PAS: Pars_1338
            TPE: Tpen_0816
            NEQ: NEQ302
STRUCTURES  PDB: 1FYJ  1G59  1J09  1N75  1N77  1N78  2CFO  2CUZ  2CV0  2CV1  
                 2CV2  2DXI  2HRA  2HRK  2HSM  2O5R  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.17
            ExPASy - ENZYME nomenclature database: 6.1.1.17
            ExplorEnz - The Enzyme Database: 6.1.1.17
            ERGO genome analysis and discovery system: 6.1.1.17
            BRENDA, the Enzyme Database: 6.1.1.17
            CAS: 9068-76-2
///
ENTRY       EC 6.1.1.18                 Enzyme
NAME        glutamine---tRNA ligase;
            glutaminyl-tRNA synthetase;
            glutaminyl-transfer RNA synthetase;
            glutaminyl-transfer ribonucleate synthetase;
            glutamine-tRNA synthetase;
            glutamine translase;
            glutamate-tRNA ligase;
            glutaminyl ribonucleic acid;
            GlnRS
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-glutamine:tRNAGln ligase (AMP-forming)
REACTION    ATP + L-glutamine + tRNAGln = AMP + diphosphate +
            L-glutaminyl-tRNAGln [RN:R03652]
ALL_REAC    R03652
SUBSTRATE   ATP [CPD:C00002];
            L-glutamine [CPD:C00064];
            tRNA(Gln) [CPD:C01640]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-glutaminyl-tRNA(Gln) [CPD:C02282]
REFERENCE   1
  AUTHORS   Ravel, J.M., Wang, S., Heinemeyer, C. and Shive, W.
  TITLE     Glutamyl and glutaminyl ribonucleic acid synthetases of Escherichia
            coli W. Separation, properties, and stimulation of adenosine
            triphosphate-pyrophosphate exchange by acceptor ribonucleic acid.
  JOURNAL   J. Biol. Chem. 240 (1965) 432-438.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01886  glutaminyl-tRNA synthetase
GENES       HSA: 5859(QARS)
            PTR: 460363(QRICH1)
            MMU: 97541(Qars)
            RNO: 290868(Qars)
            CFA: 476628(QARS)
            GGA: 416057(RCJMB04_22h1)
            XLA: 379670(MGC69128)
            DRE: 394188(qars)
            DME: Dmel_CG10506(Aats-gln)
            CEL: Y41E3.4(ers-1)
            ATH: AT1G25350(OVA9)
            OSA: 4325653 4337996
            CME: CMS289C
            SCE: YOR168W(GLN4)
            AGO: AGOS_AGR259C
            PIC: PICST_72287(GLN4)
            CGR: CAGL0L04532g
            SPO: SPBC342.02
            ANI: AN9157.2
            AFM: AFUA_2G01920
            AOR: AO090701000597
            CNE: CNA00740
            UMA: UM05125.1
            ECU: ECU10_1460
            DDI: DDB_0201644(glnS)
            PFA: PF13_0170
            CPV: cgd1_2130
            CHO: Chro.10244
            TAN: TA12530
            TPV: TP02_0322
            TET: TTHERM_00056140 TTHERM_00721810
            TBR: Tb09.160.3730
            TCR: 508277.160
            LMA: LmjF15.1440
            EHI: 212.t00006
            ECO: b0680(glnS)
            ECJ: JW0666(glnS)
            ECE: Z0827(glnS)
            ECS: ECs0710
            ECC: c0766(glnS)
            ECI: UTI89_C0684(glnS)
            ECP: ECP_0700
            ECV: APECO1_1384(glnS)
            ECW: EcE24377A_0706(glnS)
            ECX: EcHS_A0725(glnS)
            STY: STY0724(glnS)
            STT: t2189(glnS)
            SPT: SPA2055(glnS)
            SEC: SC0707(glnS)
            STM: STM0686(glnS)
            YPE: YPO2630(glnS)
            YPK: y1205(glnS)
            YPM: YP_1084(glnS2)
            YPA: YPA_2467
            YPN: YPN_1116
            YPP: YPDSF_2624
            YPS: YPTB1121(glnS)
            YPI: YpsIP31758_2907(glnS)
            SFL: SF0613(glnS)
            SFX: S0624(glnS)
            SFV: SFV_0651(glnS)
            SSN: SSON_0634(glnS)
            SBO: SBO_0542(glnS)
            SDY: SDY_0614(glnS)
            ECA: ECA1328(glnS)
            PLU: plu1319(glnS)
            BUC: BU415(glnS)
            BAS: BUsg398(glnS)
            BAB: bbp375(glnS)
            BCC: BCc_263(glnS)
            WBR: WGLp288(glnS)
            SGL: SG0860
            ENT: Ent638_1195
            BFL: Bfl324(glnS)
            BPN: BPEN_332(glnS)
            HIN: HI1354(glnS)
            HIT: NTHI1812(glnS)
            HIP: CGSHiEE_04295
            HIQ: CGSHiGG_00420
            HDU: HD1404(glnS)
            HSO: HS_0895(glnS)
            PMU: PM0528(glnS)
            MSU: MS1127(glnS)
            APL: APL_0679(glnS)
            XFA: XF1338
            XFT: PD0584(glnS)
            XCC: XCC0821(glnS)
            XCB: XC_3409
            XCV: XCV0930(glnS)
            XAC: XAC0893(glnS)
            XOO: XOO3713(glnS)
            XOM: XOO_3505(XOO3505)
            VCH: VC0997
            VCO: VC0395_A0517(glnS)
            VVU: VV1_0176 VV1_0177
            VVY: VV1013
            VPA: VP0832
            VFI: VF0809
            PPR: PBPRA1034
            PAE: PA1794(glnS)
            PAU: PA14_41380(glnS)
            PAP: PSPA7_3509(glnS)
            PPU: PP_2904(glnS)
            PPF: Pput_2787
            PST: PSPTO_3743(glnS)
            PSB: Psyr_1734
            PSP: PSPPH_1678(glnS)
            PFL: PFL_3913(glnS)
            PFO: Pfl_3639
            PEN: PSEEN2086(glnS)
            PAR: Psyc_0694(glnS)
            PCR: Pcryo_0665
            PRW: PsycPRwf_0814
            ACI: ACIAD1920(glnS)
            ACB: A1S_2108
            SON: SO_1786(glnS)
            SDN: Sden_2413
            SFR: Sfri_2615
            SAZ: Sama_1216
            SBL: Sbal_1596
            SLO: Shew_2516
            SPC: Sputcn32_1482
            SHE: Shewmr4_2503
            SHM: Shewmr7_2571
            SHN: Shewana3_2669
            SHW: Sputw3181_2619
            ILO: IL1478(glnS)
            CPS: CPS_3240(glnS)
            PHA: PSHAa1642(glnS)
            PAT: Patl_2184
            SDE: Sde_1902
            PIN: Ping_0492
            MAQ: Maqu_1845
            LPN: lpg1306(glnS)
            LPF: lpl1269(glnS)
            LPP: lpp1270(glnS)
            FTU: FTT0448c(glnS)
            FTF: FTF0448c(glnS)
            FTW: FTW_1622(glnS)
            FTL: FTL_1617
            FTH: FTH_1564(glnS)
            FTA: FTA_1705(glnS)
            FTN: FTN_0539(glnS)
            TCX: Tcr_0922
            HCH: HCH_02153(glnS)
            CSA: Csal_2052
            ABO: ABO_1207(glnS)
            MMW: Mmwyl1_2109
            AHA: AHA_1529(glnS)
            DNO: DNO_1108(glnS)
            BCI: BCI_0094(glnS)
            CRP: CRP_071
            RMA: Rmag_0909
            VOK: COSY_0816(glnS)
            NME: NMB1560
            NMA: NMA1748(glnS)
            NMC: NMC1478(glnS)
            NGO: NGO1218
            CVI: CV_1742(glnS)
            RSO: RSc0791(glnS)
            REU: Reut_A0833
            REH: H16_A2784(glnS)
            RME: Rmet_0818
            BMA: BMA0892(glnS)
            BMV: BMASAVP1_A1419(glnS)
            BML: BMA10299_A0459(glnS)
            BMN: BMA10247_0701(glnS)
            BXE: Bxe_A1307
            BVI: Bcep1808_1369
            BUR: Bcep18194_A4549
            BCN: Bcen_0923
            BCH: Bcen2424_1405
            BAM: Bamb_1282
            BPS: BPSL2012(glnS)
            BPM: BURPS1710b_1812(glnS)
            BPL: BURPS1106A_1655(glnS)
            BPD: BURPS668_1633(glnS)
            BTE: BTH_I2665(glnS)
            PNU: Pnuc_1722
            BPE: BP3226(glnS)
            BPA: BPP3578(glnS)
            BBR: BB4013(glnS)
            RFR: Rfer_1823
            POL: Bpro_3350
            PNA: Pnap_1351
            AAV: Aave_2300
            AJS: Ajs_1608
            VEI: Veis_4234
            MPT: Mpe_A1314
            HAR: HEAR0612(glnS)
            MMS: mma_0579(glnS)
            NEU: NE2356(glnS) NE2363(glnS)
            NET: Neut_0871
            NMU: Nmul_A2083
            EBA: ebA4065(glnS)
            AZO: azo0836(glnS)
            DAR: Daro_3447
            TBD: Tbd_0850
            MFA: Mfla_2082
            SUN: SUN_1139(glnS)
            GSU: GSU3366(glnS)
            GME: Gmet_0058
            GUR: Gura_4167
            PCA: Pcar_0101
            PPD: Ppro_1725
            DVU: DVU2951(glnS)
            DVL: Dvul_0417
            DDE: Dde_0626
            LIP: LI0493(glnS)
            BBA: Bd1371(glnS)
            DPS: DP2738
            ADE: Adeh_2599
            MXA: MXAN_2363(glnS)
            SAT: SYN_02116
            SFU: Sfum_3516
            BJA: bll4837(glnS)
            BRA: BRADO4124(glnS)
            BBT: BBta_4500(glnS)
            RPA: RPA2905(glnS)
            RPB: RPB_2811
            RPC: RPC_2452
            RPD: RPD_2841
            RPE: RPE_2569
            NWI: Nwi_1843
            NHA: Nham_1710
            SUS: Acid_5012
            CPE: CPE0645(gltX)
            CPF: CPF_0626(glnS)
            CPR: CPR_0612(glnS)
            CNO: NT01CX_0275(glnS)
            CTH: Cthe_0917
            CDF: CD2059(glnS)
            CKL: CKL_1022(glnS)
            DSY: DSY4982
            DRM: Dred_0189
            SWO: Swol_2459
            POY: PAM620(glnS)
            AYW: AYWB_116(glnS)
            PAC: PPA1870
            RBA: RB1578(glnS)
            BTH: BT_1325
            BFR: BF2758
            BFS: BF2773(glnS)
            PGI: PG1951(glnS)
            SRU: SRU_1795
            GFO: GFO_3307(glnS)
            FPS: FP2494(glnS)
            DRA: DR_2611
            DGE: Dgeo_2188
            TTH: TTC0181
            TTJ: TTHA0549
            HMA: rrnAC0085(gltX)
STRUCTURES  PDB: 1EUQ  1EUY  1EXD  1GSG  1GTR  1GTS  1NYL  1O0B  1O0C  1QRS  
                 1QRT  1QRU  1QTQ  1ZJW  2HZ7  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.18
            ExPASy - ENZYME nomenclature database: 6.1.1.18
            ExplorEnz - The Enzyme Database: 6.1.1.18
            ERGO genome analysis and discovery system: 6.1.1.18
            BRENDA, the Enzyme Database: 6.1.1.18
            CAS: 9075-59-6
///
ENTRY       EC 6.1.1.19                 Enzyme
NAME        arginine---tRNA ligase;
            arginyl-tRNA synthetase;
            arginyl-transfer ribonucleate synthetase;
            arginyl-transfer RNA synthetase;
            arginyl transfer ribonucleic acid synthetase;
            arginine-tRNA synthetase;
            arginine translase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-arginine:tRNAArg ligase (AMP-forming)
REACTION    ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
            [RN:R03646]
ALL_REAC    R03646
SUBSTRATE   ATP [CPD:C00002];
            L-arginine [CPD:C00062];
            tRNA(Arg) [CPD:C01636]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-arginyl-tRNA(Arg) [CPD:C02163]
REFERENCE   1  [PMID:14165914]
  AUTHORS   ALLENDE CC, ALLENDE JE.
  TITLE     PURIFICATION AND SUBSTRATE SPECIFICITY OF ARGINYL-RIBONUCLEIC ACID
            SYNTHETASE FROM RAT LIVER.
  JOURNAL   J. Biol. Chem. 239 (1964) 1102-6.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:12325365]
  AUTHORS   Mehler AH, Mitra SK.
  TITLE     The activation of arginyl transfer ribonucleic acid synthetase by
            transfer ribonucleic acid.
  JOURNAL   J. Biol. Chem. 242 (1967) 5495-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Mitra, S.K. and Mehler, A.H.
  TITLE     The arginyl transfer ribonucleic acid synthetase of Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 242 (1967) 5491-5494.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00330  Arginine and proline metabolism
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01887  arginyl-tRNA synthetase
GENES       HSA: 57038(RARS2) 5917(RARS)
            PTR: 462249(RARS)
            MMU: 104458(Rars) 109093(Rars2)
            CFA: 609803(RARS)
            BTA: 525894(MGC140742)
            GGA: 416168(RCJMB04_3h11) 421823(RARS2)
            XLA: 443863(MGC79100)
            XTR: 395040(rars)
            DRE: 337070(rars)
            SPU: 575790(LOC575790) 587297(LOC587297)
            DME: Dmel_CG9020(Aats-arg)
            CEL: C29H12.1(rrt-2)
            OSA: 4324056 4337898
            CME: CMN177C
            SCE: YDR341C(RRS1) YHR091C(MSR1)
            AGO: AGOS_AFL206C
            PIC: PICST_38727(SYR1)
            CGR: CAGL0A02189g
            SPO: SPBC25B2.09c
            ANI: AN6368.2
            AFM: AFUA_2G14030
            AOR: AO090026000140
            CNE: CNG01310
            ECU: ECU08_0550
            DDI: DDB_0231324(argS1) DDB_0231325(argS2)
            PFA: PFL0900c
            CHO: Chro.50402
            TAN: TA08180 TA16890
            TPV: TP04_0389
            TET: TTHERM_00657270
            TBR: Tb11.46.0008
            TCR: 508355.320
            LMA: LmjF27.1310
            EHI: 159.t00014
            ECO: b1876(argS)
            ECJ: JW1865(argS)
            ECE: Z2929(argS)
            ECS: ECs2586
            ECC: c2291(argS)
            ECI: UTI89_C2080(argS)
            ECP: ECP_1822
            ECV: APECO1_926(argS)
            ECW: EcE24377A_2108(argS)
            ECX: EcHS_A1971
            STY: STY2117(argS)
            STT: t0968(argS)
            SPT: SPA0960(argS)
            SEC: SC1916(argS)
            STM: STM1909(argS)
            YPE: YPO2046(argS)
            YPK: y2266(argS)
            YPM: YP_1889(argS)
            YPA: YPA_1428
            YPN: YPN_1523
            YPP: YPDSF_1077
            YPS: YPTB2029(argS)
            YPI: YpsIP31758_2043(argS)
            SFL: SF1917(argS)
            SFX: S2007(argS)
            SFV: SFV_1914(argS)
            SSN: SSON_1242(argS)
            SBO: SBO_1124(argS)
            SDY: SDY_1180(argS)
            ECA: ECA2520(argS)
            PLU: plu2092(argS)
            BUC: BU242(argS)
            BAS: BUsg237(argS)
            BAB: bbp224(argS)
            BCC: BCc_152(argS)
            WBR: WGLp129(argS)
            SGL: SG1248
            ENT: Ent638_2442
            KPN: KPN_02388(argS)
            SPE: Spro_2791
            BFL: Bfl453(argS)
            BPN: BPEN_468(argS)
            HIN: HI1583(argS)
            HIT: NTHI1470(argS)
            HIP: CGSHiEE_05515(argS)
            HIQ: CGSHiGG_10215(argS)
            HDU: HD0268(argS)
            HSO: HS_0955(argS)
            PMU: PM0551(argS)
            MSU: MS1329 MS1330(argS)
            APL: APL_0039(argS)
            ASU: Asuc_1094
            XFA: XF0147
            XFT: PD0116(argS)
            XCC: XCC3861(argS)
            XCB: XC_3945
            XCV: XCV4029(argS)
            XAC: XAC3916(argS)
            XOO: XOO0494(argS)
            XOM: XOO_0461(XOO0461)
            VCH: VC2074
            VCO: VC0395_A1661(argS)
            VVU: VV1_0145
            VVY: VV1044
            VPA: VP0861
            VFI: VF0839
            PPR: PBPRA1064
            PAE: PA5051(argS)
            PAU: PA14_66750(argS)
            PAP: PSPA7_5788(argS)
            PPU: PP_5089(argS)
            PPF: Pput_4962
            PST: PSPTO_5138(argS)
            PSB: Psyr_0397
            PSP: PSPPH_0384(argS)
            PFL: PFL_0439(argS)
            PFO: Pfl_0399
            PEN: PSEEN0323(argS)
            PMY: Pmen_0535
            PAR: Psyc_1946(argS)
            PCR: Pcryo_2239
            PRW: PsycPRwf_0294
            ACI: ACIAD0164(argS)
            SON: SO_4123(argS)
            SDN: Sden_3357
            SFR: Sfri_3762
            SAZ: Sama_0443
            SBL: Sbal_3845
            SBM: Shew185_0474
            SLO: Shew_0378
            SPC: Sputcn32_0550
            SSE: Ssed_0533
            SPL: Spea_3779
            SHE: Shewmr4_3496
            SHM: Shewmr7_0456
            SHN: Shewana3_3673
            SHW: Sputw3181_3622
            ILO: IL2460(argS)
            CPS: CPS_1110(argS)
            PHA: PSHAa0656(argS)
            PAT: Patl_1359
            SDE: Sde_2379
            PIN: Ping_0006
            MAQ: Maqu_0820
            CBU: CBU_2008(argS)
            CBD: COXBU7E912_2109(argS)
            LPN: lpg2031(argS)
            LPF: lpl2008(argS)
            LPP: lpp2013(argS)
            MCA: MCA3089(argS)
            FTU: FTT0466c(argS)
            FTF: FTF0466c(argS)
            FTW: FTW_1604(argS)
            FTL: FTL_1598
            FTH: FTH_1544(argS)
            FTA: FTA_1684(argS)
            FTN: FTN_0557(argS)
            TCX: Tcr_0198
            NOC: Noc_0027
            AEH: Mlg_2774
            HHA: Hhal_2416
            HCH: HCH_01116(argS)
            CSA: Csal_0602
            ABO: ABO_2242(argS)
            MMW: Mmwyl1_4134
            AHA: AHA_4112(argS)
            DNO: DNO_1051(argS)
            BCI: BCI_0276(argS)
            RMA: Rmag_0079
            VOK: COSY_0085(argS)
            NME: NMB1506
            NMA: NMA1707(argS)
            NMC: NMC1436(argS)
            NGO: NGO0963
            CVI: CV_1962(argS)
            RSO: RSc0287(argS)
            REU: Reut_A0127
            REH: H16_A0159(argS)
            RME: Rmet_0096
            BMA: BMA0084(argS)
            BMV: BMASAVP1_A3099(argS)
            BML: BMA10299_A1997(argS)
            BMN: BMA10247_2291(argS)
            BXE: Bxe_A4245
            BVI: Bcep1808_3014
            BUR: Bcep18194_A6262
            BCN: Bcen_2305
            BCH: Bcen2424_2919
            BAM: Bamb_2968
            BPS: BPSL0383(argS)
            BPM: BURPS1710b_0592(argS)
            BPL: BURPS1106A_0430(argS)
            BPD: BURPS668_0410(argS)
            BTE: BTH_I0355(argS)
            PNU: Pnuc_1977
            BPE: BP0115(argS)
            BPA: BPP4352(argS)
            BBR: BB4938(argS)
            RFR: Rfer_0773
            POL: Bpro_4490
            PNA: Pnap_3701
            AAV: Aave_0414
            AJS: Ajs_0343
            VEI: Veis_0573
            MPT: Mpe_A0153
            HAR: HEAR0093
            MMS: mma_0113
            NEU: NE0364(argS)
            NET: Neut_1605
            NMU: Nmul_A2456
            EBA: ebA3614(argS)
            AZO: azo0380(argS)
            DAR: Daro_3866
            TBD: Tbd_2782
            MFA: Mfla_2673
            HPY: HP0319
            HPJ: jhp0302(argS)
            HPA: HPAG1_0322
            HHE: HH0709(argS)
            HAC: Hac_1002(argS)
            WSU: WS0186(argS)
            TDN: Tmden_1794
            CJE: Cj1175c(argS)
            CJR: CJE1309(argS)
            CJJ: CJJ81176_1190(argS)
            CJU: C8J_1119(argS)
            CJD: JJD26997_0554(argS)
            CFF: CFF8240_1433(argS)
            CCV: CCV52592_1254(argS)
            CHA: CHAB381_1254(argS)
            CCO: CCC13826_0543(argS) CCC13826_1535
            ABU: Abu_2129(argS)
            NIS: NIS_1495(argS)
            SUN: SUN_2208(argS)
            GSU: GSU1812(argS)
            GME: Gmet_1434
            GUR: Gura_2304
            PCA: Pcar_0742
            PPD: Ppro_1019
            DVU: DVU1248(argS)
            DVL: Dvul_1814
            DDE: Dde_2295
            LIP: LI0229(argS)
            BBA: Bd2027(argS)
            DPS: DP2752
            ADE: Adeh_1524
            AFW: Anae109_2288
            MXA: MXAN_3289(argS)
            SAT: SYN_00994
            SFU: Sfum_0561
            RPR: RP065(argS)
            RTY: RT0067(argS)
            RCO: RC0095(argS)
            RFE: RF_0109(argS)
            RBE: RBE_1302(argS)
            RAK: A1C_00505(argS)
            RBO: A1I_00355(argS)
            RCM: A1E_00315(argS)
            RRI: A1G_00585(argS)
            OTS: OTBS_0571(argS)
            WOL: WD0402(argS)
            WBM: Wbm0205
            AMA: AM678(argS)
            APH: APH_0700(argS)
            ERU: Erum4910(argS)
            ERW: ERWE_CDS_05130(argS)
            ERG: ERGA_CDS_05040(argS)
            ECN: Ecaj_0498
            ECH: ECH_0537(argS)
            NSE: NSE_0049(argS)
            PUB: SAR11_0970(argS)
            MLO: mll1091
            MES: Meso_1813
            PLA: Plav_3022
            SME: SMc02073(argS)
            SMD: Smed_1158
            ATU: Atu1711(argS)
            ATC: AGR_C_3144
            RET: RHE_CH01818(argS)
            RLE: RL1058(argS) RL2041(argS)
            BME: BMEI1089
            BMF: BAB1_0896(argS)
            BMS: BR0877(argS)
            BMB: BruAb1_0889(argS)
            BOV: BOV_0868(argS)
            OAN: Oant_2351
            BJA: bll4757
            BRA: BRADO4052(argS)
            BBT: BBta_4423(argS)
            RPA: RPA2854(argS)
            RPB: RPB_2750
            RPC: RPC_2508
            RPD: RPD_2795
            RPE: RPE_2691
            NWI: Nwi_1807
            NHA: Nham_1758
            BHE: BH09980(argS)
            BQU: BQ07700(argS)
            BBK: BARBAKC583_0749(argS)
            XAU: Xaut_4245
            CCR: CC_3359
            SIL: SPO2504(argS)
            SIT: TM1040_0903
            RSP: RSP_2943(argS)
            RSH: Rsph17029_1588
            RSQ: Rsph17025_0902
            JAN: Jann_1507
            RDE: RD1_3165(argS)
            PDE: Pden_1870
            MMR: Mmar10_2213
            HNE: HNE_2715(argS)
            ZMO: ZMO0843(argS)
            NAR: Saro_1089
            SAL: Sala_0112 Sala_1138
            SWI: Swit_3935
            ELI: ELI_01570
            GOX: GOX1753
            GBE: GbCGDNIH1_1260
            ACR: Acry_0949
            RRU: Rru_A1779
            MAG: amb2529
            MGM: Mmc1_0704
            ABA: Acid345_2032
            SUS: Acid_5890
            BSU: BG11341(argS)
            BHA: BH0834 BH3808(argS)
            BAN: BA2175(argS-1) BA5611(argS-2)
            BAR: GBAA2175(argS-1) GBAA5611(argS-2)
            BAA: BA_0468 BA_2670
            BAT: BAS2021 BAS5213
            BCE: BC5364
            BCA: BCE_2236(argS) BCE_5493(argS)
            BCZ: BCZK1974(argS) BCZK5061(argS)
            BCY: Bcer98_1620 Bcer98_3878
            BTK: BT9727_1992(argS) BT9727_5045(argS)
            BTL: BALH_1936(argS) BALH_4860(argS)
            BLI: BL03923(argS)
            BLD: BLi03971(argS)
            BCL: ABC2288 ABC3895(argS)
            BAY: RBAM_034480
            BPU: BPUM_3383
            OIH: OB3015(argS)
            GKA: GK3401
            SAU: SA0564(argS)
            SAV: SAV0607(argS)
            SAM: MW0571(argS)
            SAR: SAR0615(argS)
            SAS: SAS0575
            SAC: SACOL0663(argS)
            SAB: SAB0559
            SAA: SAUSA300_0596(argS)
            SAO: SAOUHSC_00611
            SAJ: SaurJH9_0630
            SAH: SaurJH1_0645
            SEP: SE0380
            SER: SERP0262(argS)
            SHA: SH2293(argS)
            SSP: SSP2112
            LMO: lmo2561(argS)
            LMF: LMOf2365_2533(argS)
            LIN: lin2706(argS)
            LWE: lwe2511(argS)
            LLA: L0344(argS)
            LLC: LACR_2323
            LLM: llmg_2314(argS)
            SPY: SPy_2151(argS)
            SPZ: M5005_Spy_1808(argS)
            SPM: spyM18_2183(argS)
            SPG: SpyM3_1809(argS)
            SPS: SPs1807
            SPH: MGAS10270_Spy1900(argS)
            SPI: MGAS10750_Spy1925(argS)
            SPJ: MGAS2096_Spy1840(argS)
            SPK: MGAS9429_Spy1819(argS)
            SPF: SpyM51783(argS)
            SPA: M6_Spy1827
            SPB: M28_Spy1817(argS)
            SPN: SP_2078
            SPR: spr1890(argS)
            SPD: SPD_1905(argS)
            SAG: SAG2103(argS)
            SAN: gbs2056(argS)
            SAK: SAK_2042(argS)
            SMU: SMU.2098(argS)
            STC: str0047(argS)
            STL: stu0047(argS)
            STE: STER_0065
            SSA: SSA_2262(argS)
            SSU: SSU05_2126
            SSV: SSU98_2130
            SGO: SGO_2058(argS)
            LPL: lp_1391(argS)
            LJO: LJ0686
            LAC: LBA1600(argS)
            LSA: LSA1421(argS)
            LSL: LSL_0677(argS)
            LDB: Ldb0809(argS)
            LBR: LVIS_1491
            LCA: LSEI_1728
            LGA: LGAS_0466
            LRE: Lreu_1270
            PPE: PEPE_0669
            EFA: EF2471(argS)
            OOE: OEOE_0899
            LME: LEUM_1215
            STH: STH19(argS)
            CAC: CAC1041(argS)
            CPE: CPE1661(argS)
            CPF: CPF_1915(argS)
            CPR: CPR_1633(argS)
            CTC: CTC00966(argS)
            CNO: NT01CX_1587(argS)
            CTH: Cthe_1935
            CDF: CD0711(argS)
            CBO: CBO1072(argS)
            CBA: CLB_1112(argS)
            CBH: CLC_1124(argS)
            CBF: CLI_1163(argS)
            CBE: Cbei_1019
            CKL: CKL_1548(argS)
            AMT: Amet_1714
            CHY: CHY_0124(argS)
            DSY: DSY4946
            DRM: Dred_3183
            SWO: Swol_2421
            CSC: Csac_1375
            TTE: TTE2533(argS)
            MTA: Moth_2410
            MGE: MG_378(argS)
            MPN: MPN556(argS)
            MPU: MYPU_2430(argS)
            MPE: MYPE6120(argS)
            MGA: MGA_0636(argS)
            MMY: MSC_0599(argS)
            MMO: MMOB1240(argS)
            MHY: mhp012(argS)
            MHJ: MHJ_0012(argS)
            MHP: MHP7448_0012(argS)
            MSY: MS53_0356(argS)
            MCP: MCAP_0376(argS)
            UUR: UU278(argS)
            POY: PAM455(argS)
            AYW: AYWB_316(argS)
            MFL: Mfl554
            MTU: Rv1292(argS)
            MTC: MT1331(argS)
            MBO: Mb1324(argS)
            MBB: BCG_1352(argS)
            MLE: ML1127(argS)
            MPA: MAP2470c(argS)
            MSM: MSMEG_4959(argS)
            MVA: Mvan_4350
            MGI: Mflv_2296
            MMC: Mmcs_3898
            MKM: Mkms_3972
            MJL: Mjls_3884
            CGL: NCgl1132(cgl1179)
            CGB: cg1333(argS)
            CEF: CE1276
            CDI: DIP1034(argS)
            CJK: jk1354(argS)
            NFA: nfa10470(argS)
            RHA: RHA1_ro01490(argS)
            SCO: SCO3304(argS)
            SMA: SAV4748(argS2)
            TWH: TWT351(argS)
            TWS: TW419(argS)
            LXX: Lxx06800(argS)
            ART: Arth_2625 Arth_3151
            AAU: AAur_2614(argS)
            PAC: PPA2128
            NCA: Noca_1742
            TFU: Tfu_0269
            FRA: Francci3_2705 Francci3_3727
            FAL: FRAAL5953(argS)
            ACE: Acel_0628
            KRA: Krad_1250
            SEN: SACE_6300(argS)
            STP: Strop_0146 Strop_3653
            BLO: BL1272(argS)
            BAD: BAD_1418(argS)
            RXY: Rxyl_1659
            FNU: FN0506
            RBA: RB5747(argS)
            CTR: CT454(argS)
            CTA: CTA_0496(argS)
            CMU: TC0739
            CPN: CPn0570(argS)
            CPA: CP0179
            CPJ: CPj0570(argS)
            CPT: CpB0593
            CCA: CCA00172(argS)
            CAB: CAB169(argS)
            CFE: CF0835(argS)
            PCU: pc0231(argS)
            BGA: BG0607(argS)
            BAF: BAPKO_0625(argS)
            TPA: TP0831(argS)
            TDE: TDE0971(argS)
            LIL: LA1688(argS)
            LIC: LIC12102(argS)
            LBJ: LBJ_1204(argS)
            LBL: LBL_1256(argS)
            SYN: sll0502(argS)
            SYW: SYNW2319(argS)
            SYC: syc0034_c(argS)
            SYF: Synpcc7942_1577
            SYD: Syncc9605_2451
            SYE: Syncc9902_2134
            SYG: sync_2667(argS)
            SYR: SynRCC307_2241(argS)
            SYX: SynWH7803_2336(argS)
            CYA: CYA_2732(argS)
            CYB: CYB_1944(argS)
            TEL: tll0826(argS)
            GVI: glr4279(argS)
            ANA: all3717(argS)
            AVA: Ava_3561
            PMA: Pro0212(argS)
            PMM: PMM0187(argS)
            PMT: PMT2070(argS)
            PMN: PMN2A_1554
            PMI: PMT9312_0189
            PMB: A9601_02051(argS)
            PMC: P9515_02161(argS)
            PMF: P9303_27471(argS)
            PMG: P9301_02071(argS)
            PMH: P9215_02051
            PME: NATL1_02621(argS)
            TER: Tery_3985
            BTH: BT_2829
            BFR: BF4421
            BFS: BF4219(argS)
            PGI: PG0267(argS)
            SRU: SRU_0986(argS)
            CHU: CHU_1577(argS)
            GFO: GFO_2798(argS)
            FJO: Fjoh_0251
            FPS: FP1498(argS)
            CTE: CT0015(argS)
            CCH: Cag_0070
            CPH: Cpha266_2702
            PVI: Cvib_1732
            PLT: Plut_2092
            DET: DET1270(argS)
            DEH: cbdb_A1196(argS)
            DEB: DehaBAV1_1081
            RRS: RoseRS_1309
            RCA: Rcas_1644
            DRA: DR_2568
            DGE: Dgeo_1036
            TTH: TTC1906
            TTJ: TTHA0098
            AAE: aq_923(argS)
            TMA: TM1093
            TPT: Tpet_1650
            TME: Tmel_1495
            FNO: Fnod_0405
            MJA: MJ0237(argS)
            MMP: MMP1026(argS)
            MMQ: MmarC5_0568
            MMZ: MmarC7_0268
            MAE: Maeo_1102
            MVN: Mevan_0350
            MAC: MA0043(argS)
            MBA: Mbar_A1008
            MMA: MM_1348
            MBU: Mbur_1739
            MTP: Mthe_0216
            MHU: Mhun_2837
            MEM: Memar_2213
            MBN: Mboo_0271
            MST: Msp_1574(argS)
            MSI: Msm_1231
            MKA: MK0758(argS)
            HAL: VNG6312G(argS)
            HMA: rrnAC3169(argS)
            HWA: HQ3239A(argS)
            NPH: NP0066A(argS)
            TAC: Ta0281
            TVO: TVN1320
            PTO: PTO0603
            PHO: PH1478
            PAB: PAB0469(argS)
            PFU: PF1380
            TKO: TK1235
            RCI: RCIX568(argS)
            APE: APE_1756
            SMR: Smar_1588
            IHO: Igni_0928
            HBU: Hbut_1178
            SSO: SSO0857(argS)
            STO: ST1258
            SAI: Saci_1396(argS)
            MSE: Msed_1715
            PAI: PAE3343
            PIS: Pisl_0586
            PCL: Pcal_0441
            PAS: Pars_1756
            TPE: Tpen_0564
            NEQ: NEQ208
STRUCTURES  PDB: 1BS2  1F7U  1F7V  1IQ0  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.19
            ExPASy - ENZYME nomenclature database: 6.1.1.19
            ExplorEnz - The Enzyme Database: 6.1.1.19
            ERGO genome analysis and discovery system: 6.1.1.19
            BRENDA, the Enzyme Database: 6.1.1.19
            CAS: 37205-35-9
///
ENTRY       EC 6.1.1.20                 Enzyme
NAME        phenylalanine---tRNA ligase;
            phenylalanyl-tRNA synthetase;
            phenylalanyl-transfer ribonucleate synthetase;
            phenylalanine-tRNA synthetase;
            phenylalanyl-transfer RNA synthetase;
            phenylalanyl-tRNA ligase;
            phenylalanyl-transfer RNA ligase;
            L-phenylalanyl-tRNA synthetase;
            phenylalanine translase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-phenylalanine:tRNAPhe ligase (AMP-forming)
REACTION    ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate +
            L-phenylalanyl-tRNAPhe [RN:R03660]
ALL_REAC    R03660
SUBSTRATE   ATP [CPD:C00002];
            L-phenylalanine [CPD:C00079];
            tRNA(Phe) [CPD:C01648]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-phenylalanyl-tRNA(Phe) [CPD:C03511]
REFERENCE   1  [PMID:5335910]
  AUTHORS   Stulberg MP.
  TITLE     The isolation and properties of phenylalanyl ribonucleic acid
            synthetase from Escherichia coli B.
  JOURNAL   J. Biol. Chem. 242 (1967) 1060-4.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00400  Phenylalanine, tyrosine and tryptophan biosynthesis
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01888  phenylalanyl-tRNA synthetase
            KO: K01889  phenylalanyl-tRNA synthetase alpha chain
            KO: K01890  phenylalanyl-tRNA synthetase beta chain
            KO: K07587  phenylalanyl-tRNA synthetase alpha chain, archaeal type
GENES       HSA: 10056(FARSB) 10667(FARS2) 2193(FARSA)
            PTR: 462410(FARS2) 470661(FARSB)
            MMU: 23874(Farsb) 69955(Fars2)
            RNO: 301544(Farslb)
            CFA: 476695(FARSA) 478926(FARSB) 488204(FARS2)
            GGA: 424812(FARSB) 428482(FARS2)
            XLA: 380271(frsb) 380545(farsl) 447019(MGC82761)
            DRE: 493608(zgc:92055)
            SPU: 580714(LOC580714) 581363(LOC581363) 592754(LOC592754)
            DME: Dmel_CG13348(Aats-phe) Dmel_CG2263 Dmel_CG5706
            CEL: F22B5.9(frs-2) T08B2.9(frs-1) Y60A3A.13(frs-3)
            ATH: AT1G72550 AT3G58140 AT4G39280
            OSA: 4339585 4348566 4352408
            CME: CMI295C CMJ128C CMQ354C
            SCE: YFL022C(FRS2) YLR060W(FRS1) YPR047W(MSF1)
            AGO: AGOS_ACR219W AGOS_ADL305C AGOS_AFR516W
            PIC: PICST_55301(MSF1) PICST_71487(FRS2) PICST_72398(SYF2)
            CAL: CaO19_2960(CaO19.2960)
            CGR: CAGL0F01705g CAGL0H08602g CAGL0K07656g
            SPO: SPAC23A1.12c SPAC3G9.06 SPCC736.03c
            ANI: AN3824.2 AN4086.2 AN6253.2
            AFM: AFUA_1G05620 AFUA_2G03580 AFUA_2G13030
            AOR: AO090009000378 AO090026000265
            CNE: CNC03850 CNC06600 CNJ02270
            UMA: UM01530.1 UM04176.1
            ECU: ECU04_0900 ECU07_1660
            DDI: DDB_0231328(pheSA) DDB_0231330(mpheS)
            PFA: MAL1P2.25 PF11_0051 PFF0180w PFL1540c
            CPV: cgd3_3320 cgd8_3320
            CHO: Chro.30378 Chro.80385
            TAN: TA10840 TA11150 TA11685
            TPV: TP02_0167 TP04_0622 TP04_0871
            TET: TTHERM_00133690 TTHERM_00218410 TTHERM_00678250
            TBR: Tb11.01.5710 Tb11.22.0005
            TCR: 506127.30 508271.10 511727.140
            LMA: LmjF19.1040 LmjF32.0870
            EHI: 137.t00008 196.t00004 407.t00011
            ECO: b1713(pheT) b1714(pheS)
            ECJ: JW1703(pheT) JW5277(pheS)
            ECE: Z2742(pheT) Z2743(pheS)
            ECS: ECs2420 ECs2421
            ECC: c2112(pheS)
            ECI: UTI89_C1906(pheT) UTI89_C1907(pheS)
            ECP: ECP_1661 ECP_1662
            ECV: APECO1_787(pheT) APECO1_788(pheS)
            ECW: EcE24377A_1932(pheT) EcE24377A_1933(pheS)
            ECX: EcHS_A1793 EcHS_A1794
            STY: STY1772(pheT) STY1773(pheS)
            STT: t1218(pheS) t1219(pheT)
            SPT: SPA1505(pheT) SPA1506(pheS)
            SEC: SC1356(pheS) SC1357(pheT)
            STM: STM1337(pheS) STM1338(pheT)
            YPE: YPO2428(pheT) YPO2429(pheS)
            YPK: y1908(pheS) y1909(pheT)
            YPM: YP_2215(pheT) YP_2216(pheM)
            YPA: YPA_1772 YPA_1773
            YPN: YPN_1882 YPN_1883
            YPP: YPDSF_0721 YPDSF_0722
            YPS: YPTB2336(pheT) YPTB2337(pheS)
            YPI: YpsIP31758_1716(pheS) YpsIP31758_1717(pheT)
            SFL: SF1517(pheS) SF1518(pheT)
            SFX: S1634(pheS) S1635(pheT)
            SFV: SFV_1509(pheS) SFV_1510(pheT)
            SSN: SSON_1444(pheS) SSON_1445(pheT)
            SBO: SBO_1379(pheS) SBO_1380(pheT)
            SDY: SDY_1808(pheT) SDY_1809(pheS)
            ECA: ECA2417(pheT) ECA2418(pheS)
            PLU: plu2664(pheT) plu2665(pheS)
            BUC: BU129(pheS) BU130(pheT)
            BAS: BUsg121(pheS) BUsg122(pheT)
            BAB: bbp123(pheS) bbp124(pheT)
            BCC: BCc_082(pheS) BCc_083(pheT)
            WBR: WGLp085(pheS) WGLp086(pheT)
            SGL: SG1422 SG1423
            ENT: Ent638_1728 Ent638_1729
            KPN: KPN_02175(pheT) KPN_02176(pheS)
            SPE: Spro_2149
            BFL: Bfl355(pheS) Bfl356(pheT)
            BPN: BPEN_366(pheS) BPEN_367(pheT)
            HIN: HI1311(pheS) HI1312(pheT)
            HIT: NTHI1624(pheS) NTHI1625(pheT)
            HIP: CGSHiEE_05115(pheT) CGSHiEE_05130(pheS)
            HIQ: CGSHiGG_01395(pheT) CGSHiGG_01415(pheS)
            HDU: HD1483(pheT) HD1484(pheS)
            HSO: HS_0859(pheS) HS_0861(pheT)
            PMU: PM0629(pheT) PM0631(pheS)
            MSU: MS1090(pheT) MS1091(pheS)
            APL: APL_0608(pheS) APL_0609(pheT)
            ASU: Asuc_1419
            XFA: XF0741 XF0742
            XFT: PD1911(pheT) PD1912(pheS)
            XCC: XCC2458(pheT) XCC2459(pheS)
            XCB: XC_1654 XC_1655
            XCV: XCV2790(pheT) XCV2791(pheS)
            XAC: XAC2589(pheT) XAC2590(pheS)
            XOO: XOO3182(pheT) XOO3183(pheS)
            XOM: XOO_3022(XOO3022) XOO_3023(XOO3023)
            VCH: VC1219 VC1220
            VCO: VC0395_A0843(pheS) VC0395_A0844(pheT)
            VVU: VV1_2370 VV1_2371
            VVY: VV1970 VV1971
            VPA: VP1290 VP1291
            VFI: VF1235 VF1236
            PPR: PBPRA2155 PBPRA2156
            PAE: PA2739(pheT) PA2740(pheS)
            PAU: PA14_28690(pheS) PA14_28710(pheT)
            PAP: PSPA7_2508(pheS) PSPA7_2509(pheT)
            PPU: PP_2469(pheS) PP_2470(pheT)
            PPF: Pput_3220
            PST: PSPTO_2382(pheS) PSPTO_2383(pheT)
            PSB: Psyr_2166 Psyr_2167
            PSP: PSPPH_2139(pheS) PSPPH_2140(pheT)
            PFL: PFL_2115(pheS) PFL_2116(pheT)
            PFO: Pfl_1935 Pfl_1936
            PEN: PSEEN1967(pheS) PSEEN1968(pheT)
            PMY: Pmen_1980 Pmen_1981
            PAR: Psyc_1995(pheT) Psyc_1996(pheS)
            PCR: Pcryo_2298 Pcryo_2299
            PRW: PsycPRwf_2315
            ACI: ACIAD3041(pheT) ACIAD3042(pheS)
            ACB: A1S_0602
            SON: SO_2085(pheS) SO_2086(pheT)
            SDN: Sden_1602 Sden_1603
            SFR: Sfri_1708 Sfri_1709
            SAZ: Sama_1952 Sama_1953
            SBL: Sbal_1873 Sbal_1874
            SBM: Shew185_1901
            SLO: Shew_2215 Shew_2216
            SPC: Sputcn32_1828 Sputcn32_1829
            SSE: Ssed_2597
            SPL: Spea_2469
            SHE: Shewmr4_1808 Shewmr4_1809
            SHM: Shewmr7_2168 Shewmr7_2169
            SHN: Shewana3_1863 Shewana3_1864
            SHW: Sputw3181_2180 Sputw3181_2181
            ILO: IL1394(pheT) IL1395(pheS)
            CPS: CPS_2995(pheT) CPS_2996(pheS)
            PHA: PSHAa1903(pheT) PSHAa1904(pheS)
            PAT: Patl_2494 Patl_2495
            SDE: Sde_1581 Sde_1582
            PIN: Ping_1403 Ping_1404
            MAQ: Maqu_2056 Maqu_2057
            CBU: CBU_1321(pheT) CBU_1322(pheS)
            CBD: COXBU7E912_1410(pheT) COXBU7E912_1411(pheS)
            LPN: lpg2710(pheT) lpg2711(pheS)
            LPF: lpl2638(pheT) lpl2639(pheS)
            LPP: lpp2765(pheT) lpp2766(pheS)
            MCA: MCA0697(pheS) MCA0698(pheT)
            FTU: FTT1002c(pheT) FTT1003c(pheS)
            FTF: FTF1002c(pheT) FTF1003c(pheS)
            FTW: FTW_0910(pheT) FTW_0911(pheS)
            FTL: FTL_1197 FTL_1198
            FTH: FTH_1173(pheS) FTH_1174
            FTA: FTA_1265(pheS) FTA_1266(pheT)
            FTN: FTN_0882(pheT) FTN_0883(pheS)
            TCX: Tcr_1662 Tcr_1663
            NOC: Noc_1144 Noc_1145
            AEH: Mlg_0763 Mlg_0764
            HHA: Hhal_0431 Hhal_0432
            HCH: HCH_04574(pheT) HCH_04575(pheS)
            CSA: Csal_1803 Csal_1804
            ABO: ABO_1837(pheT) ABO_1838(pheS)
            MMW: Mmwyl1_2592
            AHA: AHA_2322(pheT) AHA_2323(pheS)
            DNO: DNO_1055(pheS) DNO_1056(pheT)
            BCI: BCI_0467(pheT) BCI_0468(pheS)
            CRP: CRP_089
            RMA: Rmag_0642 Rmag_0643
            VOK: COSY_0590(pheT) COSY_0591(pheS)
            NME: NMB0724 NMB0728
            NMA: NMA0933(pheS) NMA0937(pheT)
            NMC: NMC0676(pheS)
            NGO: NGO0299 NGO0304
            CVI: CV_1352(pheS) CV_1353(pheT)
            RSO: RSc1581(pheS) RSc1582(pheT)
            REU: Reut_A1279 Reut_A1280
            REH: H16_A1343(pheS) H16_A1344(pheT)
            RME: Rmet_1164 Rmet_1165
            BMA: BMA1091(pheT) BMA1092(pheS)
            BMV: BMASAVP1_A1534(pheT) BMASAVP1_A1535(pheS)
            BML: BMA10299_A0198(pheT) BMA10299_A0199(pheS)
            BMN: BMA10247_0967(pheS) BMA10247_0968(pheT)
            BXE: Bxe_A1375 Bxe_A1376
            BVI: Bcep1808_1443 Bcep1808_1444
            BUR: Bcep18194_A4619(pheS) Bcep18194_A4620
            BCN: Bcen_0997 Bcen_0998
            BCH: Bcen2424_1479 Bcen2424_1480
            BAM: Bamb_1363 Bamb_1364
            BPS: BPSL1940(pheT) BPSL1941(pheS)
            BPM: BURPS1710b_1894(pheS) BURPS1710b_1896(pheT)
            BPL: BURPS1106A_1739(pheS) BURPS1106A_1740(pheT)
            BPD: BURPS668_1716(pheS) BURPS668_1717(pheT)
            BTE: BTH_I2590(pheT) BTH_I2591(pheS)
            PNU: Pnuc_0833 Pnuc_0834
            BPE: BP2573(pheT) BP2574(pheS)
            BPA: BPP2598(pheS) BPP2599(pheT)
            BBR: BB2040(pheS) BB2041(pheT)
            RFR: Rfer_1340 Rfer_1341
            POL: Bpro_2106 Bpro_2107
            PNA: Pnap_2849 Pnap_2850
            AAV: Aave_2854 Aave_2855
            AJS: Ajs_2395 Ajs_2396
            VEI: Veis_3093 Veis_3094
            MPT: Mpe_A1883 Mpe_A1884
            HAR: HEAR1796(pheT) HEAR1797(pheS)
            MMS: mma_1491 mma_1492
            NEU: NE0953(pheT) NE0954(pheS)
            NET: Neut_2326 Neut_2327
            NMU: Nmul_A0491 Nmul_A0492
            EBA: ebA867(pheT) ebA868(pheS)
            AZO: azo1083(pheS) azo1084(pheT)
            DAR: Daro_2672 Daro_2673
            TBD: Tbd_1011 Tbd_1012
            MFA: Mfla_1998 Mfla_1999
            HPY: HP0402(pheT) HP0403(pheS)
            HPJ: jhp0978(pheS) jhp0979(pheT)
            HPA: HPAG1_0989 HPAG1_0990
            HHE: HH0027(pheT) HH0028(pheS)
            HAC: Hac_0460(pheT) Hac_0461(pheS)
            WSU: WS1307(pheS) WS1308(pheT)
            TDN: Tmden_0869 Tmden_0870
            CJE: Cj0896c(pheT) Cj0897c(pheS)
            CJR: CJE0975(pheT) CJE0976(pheS)
            CJJ: CJJ81176_0905(pheT) CJJ81176_0906(pheS)
            CJU: C8J_0833(pheT) C8J_0834(pheS)
            CJD: JJD26997_0916(pheS) JJD26997_0917(pheT)
            CFF: CFF8240_1253(pheT) CFF8240_1254(pheS)
            CCV: CCV52592_0517(pheT) CCV52592_0518(pheS)
            CHA: CHAB381_0485(pheT) CHAB381_0486(pheS)
            CCO: CCC13826_0483 CCC13826_0484 CCC13826_1563(pheS)
            ABU: Abu_2052(pheT) Abu_2053(pheS)
            NIS: NIS_0659(pheS) NIS_0660(pheT)
            SUN: SUN_0546(pheS) SUN_0547(pheT)
            GSU: GSU1519(pheS) GSU1520(pheT)
            GME: Gmet_1415 Gmet_1416
            GUR: Gura_2623
            PCA: Pcar_1422 Pcar_1423
            PPD: Ppro_2303 Ppro_2304
            DVU: DVU2533(pheT) DVU2534(pheS)
            DVL: Dvul_0711
            DDE: Dde_2634 Dde_2635
            LIP: LI0215(pheS) LI0216(pheT)
            BBA: Bd1637(pheS) Bd1638(pheT)
            DPS: DP1423 DP1424
            ADE: Adeh_1971 Adeh_1972
            AFW: Anae109_1884
            MXA: MXAN_3594(pheS) MXAN_3595(pheT)
            SAT: SYN_01721 SYN_01723
            SFU: Sfum_0428 Sfum_0429
            RPR: RP417(pheS) RP418(pheT)
            RTY: RT0403(pheS) RT0404(pheT)
            RCO: RC0581(pheS) RC0582(pheT)
            RFE: RF_0647(pheS) RF_0648(pheT)
            RBE: RBE_0654(pheS) RBE_0655(pheT)
            RAK: A1C_03140(pheS) A1C_03145(pheT)
            RBO: A1I_04265(pheT) A1I_04270(pheS)
            RRI: A1G_03280(pheS) A1G_03285(pheT)
            OTS: OTBS_1140(pheT) OTBS_1141(pheS)
            WOL: WD0132(pheS) WD0425(pheT)
            WBM: Wbm0087 Wbm0461
            AMA: AM055(pheS) AM885(pheT)
            APH: APH_0059(pheS) APH_0305(pheT)
            ERU: Erum1360(pheS) Erum5830(pheT)
            ERW: ERWE_CDS_01320(pheS) ERWE_CDS_06130(pheT)
            ERG: ERGA_CDS_01280(pheS) ERGA_CDS_06040(pheT)
            ECN: Ecaj_0133 Ecaj_0587
            ECH: ECH_0196(pheS) ECH_0434(pheT)
            NSE: NSE_0216(pheS) NSE_0426
            PUB: SAR11_0442(pheS) SAR11_0443(pheT)
            MLO: mll5053 mll5055
            MES: Meso_0676 Meso_0677
            PLA: Plav_0221
            SME: SMc00365(pheS) SMc00366(pheT)
            SMD: Smed_3487
            ATU: Atu0258(pheS) Atu0259(pheT)
            ATC: AGR_C_443 AGR_C_445
            RET: RHE_CH00263(pheS) RHE_CH00264(pheT)
            RLE: RL0269(pheS) RL0270(pheT)
            BME: BMEI2004 BMEI2005
            BMF: BAB1_2126(pheS) BAB1_2127(pheT)
            BMS: BR2122(pheS) BR2123(pheT)
            BMB: BruAb1_2097(pheS) BruAb1_2098(pheT)
            BOV: BOV_2037(pheS) BOV_2039(pheT)
            OAN: Oant_0797
            BJA: bll0705(pheT) bll0706(pheS)
            BRA: BRADO0139(pheS) BRADO0141(pheT)
            BBT: BBta_0212(pheT) BBta_0214(pheS)
            RPA: RPA0035(pheT) RPA0037(pheS)
            RPB: RPB_0045 RPB_0047
            RPC: RPC_0444 RPC_0447
            RPD: RPD_0162 RPD_0164
            RPE: RPE_0493 RPE_0496
            NWI: Nwi_0065(pheT) Nwi_0066
            NHA: Nham_0073 Nham_0074
            BHE: BH00840(pheS) BH00850(pheT)
            BQU: BQ00770(pheS) BQ00780(pheT)
            BBK: BARBAKC583_1312(pheT) BARBAKC583_1313(pheS)
            XAU: Xaut_1930
            CCR: CC_1043 CC_1044
            SIL: SPO3489(pheT) SPO3594(pheS)
            SIT: TM1040_2511 TM1040_3623
            RSP: RSP_1761(pheT) RSP_1763(pheS)
            RSH: Rsph17029_0409
            RSQ: Rsph17025_2491
            JAN: Jann_0452 Jann_0454
            RDE: RD1_1012(pheS) RD1_1013(pheT)
            PDE: Pden_2270
            MMR: Mmar10_0130 Mmar10_0132
            HNE: HNE_0433(pheS) HNE_0435(pheT)
            ZMO: ZMO1513(pheT) ZMO1514(pheS)
            NAR: Saro_0688 Saro_0689
            SAL: Sala_2782 Sala_2783
            SWI: Swit_2428
            ELI: ELI_13840 ELI_13845
            GOX: GOX0261 GOX0262
            GBE: GbCGDNIH1_1505 GbCGDNIH1_1506
            ACR: Acry_0361
            RRU: Rru_A3523 Rru_A3524
            MAG: amb4380 amb4381
            MGM: Mmc1_0367 Mmc1_0368
            ABA: Acid345_0716 Acid345_0718
            SUS: Acid_6396
            BSU: BG10874(pheS) BG10875(pheT)
            BHA: BH3110(pheT) BH3111(pheS)
            BAN: BA4803(pheT) BA4804(pheS)
            BAR: GBAA4803(pheT) GBAA4804(pheS)
            BAA: BA_5228 BA_5229
            BAT: BAS4455 BAS4456
            BCE: BC4560 BC4561
            BCA: BCE_4686(pheT) BCE_4687(pheS)
            BCZ: BCZK4303(pheT) BCZK4304(pheS)
            BCY: Bcer98_3248
            BTK: BT9727_4293(pheT) BT9727_4294(pheS)
            BTL: BALH_4141(pheT) BALH_4142(pheS)
            BLI: BL00339(pheTB) BL00340(pheS)
            BLD: BLi03015(pheT) BLi03016(pheS)
            BCL: ABC2679(pheT) ABC2680(pheS) ABC2770
            BAY: RBAM_025700 RBAM_025710
            BPU: BPUM_2521 BPUM_2522
            OIH: OB2130 OB2131
            GKA: GK2706 GK2707
            SAU: SA0985(pheS) SA0986(pheT)
            SAV: SAV1138(pheS) SAV1139(pheT)
            SAM: MW1021(pheS) MW1022(pheT)
            SAR: SAR1111(pheS) SAR1112(pheT)
            SAS: SAS1072 SAS1073
            SAC: SACOL1148(pheS) SACOL1149(pheT)
            SAB: SAB1002(pheS) SAB1003(pheT) SAB1602c
            SAA: SAUSA300_1037(pheS) SAUSA300_1038(pheT)
            SAO: SAOUHSC_01092 SAOUHSC_01093
            SAJ: SaurJH9_1198
            SAH: SaurJH1_1220
            SEP: SE0831 SE0832
            SER: SERP0721(pheS) SERP0722(pheT)
            SHA: SH1822(pheT) SH1823(pheS)
            SSP: SSP1656 SSP1657
            LMO: lmo1221(pheS) lmo1222(pheT)
            LMF: LMOf2365_1230(pheS) LMOf2365_1231(pheT)
            LIN: lin1184(pheS) lin1185(pheT)
            LWE: lwe1176(pheS) lwe1177(pheT)
            LLA: L0354(pheS) L0355(pheT)
            LLC: LACR_2200 LACR_2201
            LLM: llmg_0407(pheT) llmg_2195(pheT) llmg_2196(pheS)
            SPY: SPy_0768(pheS) SPy_0769(pheT)
            SPZ: M5005_Spy_0587(pheS) M5005_Spy_0588(pheT)
            SPM: spyM18_0827(pheS) spyM18_0828(pheT)
            SPG: SpyM3_0506(pheS) SpyM3_0507(pheT)
            SPS: SPs1347 SPs1348
            SPH: MGAS10270_Spy0642(pheS) MGAS10270_Spy0643(pheT)
            SPI: MGAS10750_Spy0672(pheS) MGAS10750_Spy0673(pheT)
            SPJ: MGAS2096_Spy0649(pheS) MGAS2096_Spy0650(pheT)
            SPK: MGAS9429_Spy0641(pheS) MGAS9429_Spy0642(pheT)
            SPF: SpyM51219(pheT) SpyM51220(pheS)
            SPA: M6_Spy0604 M6_Spy0605
            SPB: M28_Spy0566(pheS) M28_Spy0567(pheT)
            SPN: SP_0579 SP_0581
            SPR: spr0507(pheS) spr0509(pheT)
            SPD: SPD_0504(pheS) SPD_0506(pheT)
            SAG: SAG0869(pheS) SAG0871(pheT)
            SAN: gbs0886(pheS) gbs0888(pheT)
            SAK: SAK_0992(pheS) SAK_0994(pheT)
            SMU: SMU.1510(syfB) SMU.1512(syfA)
            STC: str1292(pheT) str1294(pheS)
            STL: stu1292(pheT) stu1294(pheS)
            SSA: SSA_0912(pheS) SSA_0914(pheT)
            SGO: SGO_0859(pheS) SGO_0861(pheT) SGO_1901
            LPL: lp_1558(pheS) lp_1559(pheT)
            LJO: LJ1624 LJ1625
            LAC: LBA1518(pheS) LBA1519(pheT)
            LSA: LSA1375(pheT) LSA1376(pheS)
            LSL: LSL_0813(pheS) LSL_0814(pheT)
            LDB: Ldb1486(pheT) Ldb1487(pheS)
            LBU: LBUL_1382 LBUL_1383
            LBR: LVIS_1009 LVIS_1010
            LCA: LSEI_1671 LSEI_1672
            LRE: Lreu_1217
            EFA: EF1115(pheS) EF1116(pheT)
            OOE: OEOE_0917
            STH: STH1105(pheSA) STH1106(pheSB)
            CAC: CAC2356(pheT) CAC2357(pheS)
            CPE: CPE1885(pheT) CPE1886(pheS)
            CPF: CPF_2139(pheT) CPF_2140(pheS)
            CPR: CPR_1851(pheT) CPR_1852(pheS)
            CTC: CTC02277 CTC02278
            CNO: NT01CX_1767(pheS) NT01CX_1768(pheT)
            CTH: Cthe_0214
            CDF: CD0699(pheS) CD0700(pheT)
            CBO: CBO3130(pheT) CBO3131(pheS)
            CBA: CLB_3160(pheT) CLB_3161(pheS)
            CBH: CLC_3033(pheT) CLC_3034(pheS)
            CBF: CLI_3188(pheT) CLI_3189(pheS)
            CBE: Cbei_1574
            CKL: CKL_3191(pheT) CKL_3192(pheS)
            AMT: Amet_1640
            CHY: CHY_1570(pheT) CHY_1571(pheS)
            DSY: DSY0271 DSY0272
            DRM: Dred_1619
            SWO: Swol_1094 Swol_1095
            CSC: Csac_1849
            TTE: TTE1688(pheT) TTE1689(pheS)
            MTA: Moth_1750 Moth_1751
            MGE: MG_194(pheS) MG_195(pheT)
            MPN: MPN105(pheS) MPN106(pheT)
            MPU: MYPU_3470(pheT) MYPU_3480(pheS)
            MPE: MYPE9260(pheT) MYPE9270(pheS)
            MGA: MGA_1278(pheS) MGA_1281(pheT)
            MMY: MSC_0595(pheT) MSC_0596(pheS)
            MMO: MMOB3170(pheS) MMOB5160(pheT)
            MHY: mhp105(pheT) mhp106(pheS)
            MHJ: MHJ_0265(pheS) MHJ_0266(pheT)
            MHP: MHP7448_0273(pheS) MHP7448_0274(pheT)
            MSY: MS53_0306(pheT) MS53_0308(pheS)
            MCP: MCAP_0383(pheS) MCAP_0384(pheT)
            UUR: UU457(pheT) UU458(pheS)
            POY: PAM596(pheS) PAM597 PAM598(pheT)
            AYW: AYWB_133(pheS) AYWB_134(pheT)
            MFL: Mfl398 Mfl399
            MTU: Rv1649(pheS) Rv1650(pheT)
            MTC: MT1687(pheS) MT1688(pheT)
            MBO: Mb1676(pheS) Mb1677(pheT)
            MBB: BCG_1688(pheS) BCG_1689(pheT)
            MLE: ML1401(pheS) ML1402(pheT)
            MPA: MAP1359(pheS) MAP1360(pheT)
            MAV: MAV_3119(pheT) MAV_3120(pheS)
            MSM: MSMEG_3777(pheT) MSMEG_3778(pheS)
            MVA: Mvan_3317
            MGI: Mflv_3533
            MMC: Mmcs_2973 Mmcs_2974
            MKM: Mkms_3018
            MJL: Mjls_2989
            CGL: NCgl1335(pheS) NCgl1336(pheT)
            CGB: cg1574(pheS) cg1575(pheT)
            CEF: CE1520 CE1521
            CDI: DIP1165(pheS) DIP1166(pheT)
            CJK: jk0839(pheS) jk0840(pheT)
            NFA: nfa19180(pheS) nfa19190(pheT)
            RHA: RHA1_ro00958(pheT) RHA1_ro00959(pheS)
            SCO: SCO1594(pheT) SCO1595(pheS)
            SMA: SAV6742(pheS) SAV6743(pheT)
            TWH: TWT167(pheS) TWT168(pheT)
            TWS: TW604(pheT) TW605(pheS)
            LXX: Lxx05980(pheS) Lxx05990(pheT)
            ART: Arth_1489
            AAU: AAur_1623(pheS) AAur_1624(pheT)
            PAC: PPA1408 PPA1409
            NCA: Noca_2465
            TFU: Tfu_2060 Tfu_2061
            FRA: Francci3_3176 Francci3_3177
            FAL: FRAAL5210(pheT) FRAAL5211(pheS)
            ACE: Acel_1265
            KRA: Krad_3163
            SEN: SACE_5276(pheT) SACE_5277(pheS)
            STP: Strop_1887
            BLO: BL1066(pheT) BL1067(pheS)
            BAD: BAD_0927(pheT) BAD_0928(pheS)
            RXY: Rxyl_1305 Rxyl_1306
            FNU: FN2122 FN2123
            RBA: RB7112(pheT) RB7114(pheS)
            CTR: CT475(pheT) CT836(pheS)
            CTA: CTA_0521(pheT) CTA_0911(pheS)
            CMU: TC0224 TC0760
            CPN: CPn0594(pheT) CPn0993(pheS)
            CPA: CP0154 CP0862
            CPJ: CPj0594(pheT) CPj0993(pheS)
            CPT: CpB0618 CpB1031
            CCA: CCA00147(pheT) CCA00768(pheS)
            CAB: CAB145(pheT) CAB736(pheS)
            CFE: CF0246(pheS) CF0860(pheT)
            PCU: pc0369(pheT) pc0705(pheS)
            BBU: BB0513(pheS) BB0514(pheT)
            BGA: BG0524(pheS) BG0525(pheT)
            BAF: BAPKO_0540(pheS) BAPKO_0541(pheT)
            TPA: TP0015 TP0973
            TDE: TDE0109(pheS) TDE1927(pheT)
            LIL: LA4035(pheT) LA4150(pheS)
            LIC: LIC13219(pheT) LIC13310(pheS)
            LBJ: LBJ_0234(pheT) LBJ_2895(pheS)
            LBL: LBL_0168(pheS) LBL_2846(pheT)
            SYN: sll0454(pheS) sll1553(pheT)
            SYW: SYNW1227(pheT) SYNW1600(pheS)
            SYC: syc0260_d(pheT) syc2029_c(pheS)
            SYF: Synpcc7942_1293 Synpcc7942_2064
            SYD: Syncc9605_0900 Syncc9605_1339
            SYE: Syncc9902_1135 Syncc9902_1498
            SYG: sync_0796(pheS) sync_1339(pheT)
            SYR: SynRCC307_1223(pheT) SynRCC307_1741(pheS)
            SYX: SynWH7803_1290(pheT) SynWH7803_1712(pheS)
            CYA: CYA_0309(pheT) CYA_2045(pheS)
            CYB: CYB_0735(pheS) CYB_2916(pheT)
            TEL: tll0662(pheT) tlr0690(pheS)
            GVI: gll2926(pheT) glr3128(pheS)
            ANA: all4845 alr4958
            AVA: Ava_2115(pheS) Ava_2221(pheT)
            PMA: Pro0966(pheT) Pro1344(pheS)
            PMM: PMM0871(pheT) PMM1270(pheS)
            PMT: PMT0367(pheS) PMT0738(pheT)
            PMN: PMN2A_0338 PMN2A_0836
            PMI: PMT9312_0930 PMT9312_1364
            PMB: A9601_09911(pheT) A9601_14691(pheS)
            PMC: P9515_09521(pheT) P9515_14311(pheS)
            PMF: P9303_14801(pheT) P9303_19341(pheS)
            PMG: P9301_09891(pheT) P9301_14551(pheS)
            PMH: P9215_10221 P9215_14951
            PME: NATL1_10111(pheT) NATL1_16891(pheS)
            TER: Tery_2063 Tery_3482
            BTH: BT_0626 BT_1669
            BFR: BF2565 BF3266
            BFS: BF2590 BF3104(pheS)
            PGI: PG0099(pheT) PG1771(pheS)
            SRU: SRU_2806(pheS) SRU_2807(pheT)
            CHU: CHU_1130(pheS) CHU_3247(pheS)
            GFO: GFO_2333(pheT) GFO_3424(pheS)
            FJO: Fjoh_2968
            FPS: FP0124(pheS) FP1041(pheT)
            CTE: CT0730(pheT) CT2130(pheS)
            CCH: Cag_1544 Cag_1711
            CPH: Cpha266_2505
            PVI: Cvib_0186
            PLT: Plut_0119 Plut_0711
            DET: DET0365(pheS) DET0366(pheT)
            DEH: cbdb_A307(pheS) cbdb_A308(pheT)
            DEB: DehaBAV1_0348
            RRS: RoseRS_1038
            RCA: Rcas_1440
            DRA: DR_2354 DR_2357
            DGE: Dgeo_0223
            TTH: TTC1594 TTC1595
            TTJ: TTHA1958 TTHA1959
            AAE: aq_1730(pheT) aq_953(pheS)
            TMA: TM0821 TM0822
            TPT: Tpet_0105
            TME: Tmel_0809
            FNO: Fnod_0932
            MJA: MJ0487 MJ1108(pheT) MJ1660
            MMP: MMP0688 MMP1255(pheT) MMP1496
            MMQ: MmarC5_0081
            MMZ: MmarC7_0501
            MAE: Maeo_1377
            MVN: Mevan_0569
            MAC: MA0090(pheRS) MA0171(pheS) MA1956(pheT)
            MBA: Mbar_A1204 Mbar_A1375 Mbar_A2752
            MMA: MM_1383 MM_1470 MM_2812
            MBU: Mbur_0447 Mbur_0923 Mbur_1427
            MTP: Mthe_1496
            MHU: Mhun_1728 Mhun_1729 Mhun_2839
            MEM: Memar_0643
            MBN: Mboo_0657
            MTH: MTH1501 MTH742 MTH770
            MST: Msp_0429(pheS) Msp_0525(pheT)
            MSI: Msm_0277 Msm_1478
            MKA: MK0271(pheS) MK0439 MK0820(pheT)
            AFU: AF0110 AF1424(pheT) AF1955(pheS)
            HAL: VNG2504G(pheS) VNG2505G(pheY)
            HMA: rrnAC2966(pheS) rrnAC2967(pheT)
            HWA: HQ1049A(pheS) HQ1050A(pheY)
            NPH: NP0694A(pheY) NP0696A(pheS)
            TAC: Ta0551 Ta0639
            TVO: TVN0605 TVN1037
            PTO: PTO0125 PTO0782
            PHO: PH0657 PH0658
            PAB: PAB2426(pheS) PAB2427(pheT)
            PFU: PF0989 PF0990
            TKO: TK0921 TK0925
            RCI: RRC220(pheS) RRC225(pheT)
            APE: APE_2302.1 APE_2305
            SMR: Smar_0257
            IHO: Igni_1226
            HBU: Hbut_0887 Hbut_0888
            SSO: SSO0100(pheS) SSO0101(pheT)
            STO: ST1415 ST1416
            SAI: Saci_1510 Saci_1511
            MSE: Msed_2123
            PAI: PAE1441 PAE1669
            PIS: Pisl_1562
            PCL: Pcal_0795
            PAS: Pars_0400
            TPE: Tpen_0950
            NEQ: NEQ479 NEQ505
STRUCTURES  PDB: 1B70  1B7Y  1EIY  1JJC  1PYS  2AKW  2ALY  2AMC  2CXI  2IY5  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.20
            ExPASy - ENZYME nomenclature database: 6.1.1.20
            ExplorEnz - The Enzyme Database: 6.1.1.20
            ERGO genome analysis and discovery system: 6.1.1.20
            BRENDA, the Enzyme Database: 6.1.1.20
            CAS: 9055-66-7
///
ENTRY       EC 6.1.1.21                 Enzyme
NAME        histidine---tRNA ligase;
            histidyl-tRNA synthetase;
            histidyl-transfer ribonucleate synthetase;
            histidine translase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-histidine:tRNAHis ligase (AMP-forming)
REACTION    ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis
            [RN:R03655]
ALL_REAC    R03655
SUBSTRATE   ATP [CPD:C00002];
            L-histidine [CPD:C00135];
            tRNA(His) [CPD:C01643]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-histidyl-tRNA(His) [CPD:C02988]
REFERENCE   1  [PMID:6035970]
  AUTHORS   von Tigerstrom M, Tener GM.
  TITLE     Histidyl transfer ribonucleic acid synthetase from bakers' yeast.
  JOURNAL   Can. J. Biochem. 45 (1967) 1067-74.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00340  Histidine metabolism
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01891  histidyl-tRNA synthetase
            KO: K01892  histidyl-tRNA synthetase
GENES       HSA: 23438(HARS2) 3035(HARS)
            PTR: 462122(HARS) 462123(HARS2)
            MMU: 15115(Hars) 70791(Hars2)
            CFA: 478034(HARS) 478035(HARS2)
            GGA: 416132(HARS) 768802(HARS2)
            SPU: 582431(LOC582431)
            DME: Dmel_CG6335(Aats-his)
            ATH: AT3G02760 AT3G46100(ATHRS1)
            OSA: 4330767 4337830
            CME: CMJ047C
            SCE: YPR033C(HTS1)
            AGO: AGOS_ACR187W
            PIC: PICST_70094(HTS1)
            CGR: CAGL0K05313g
            SPO: SPBC2G2.12
            ANI: AN0046.2
            AFM: AFUA_4G12920
            AOR: AO090009000295
            CNE: CNC06400
            UMA: UM06027.1
            ECU: ECU06_0620
            DDI: DDB_0231331(mhisS) DDB_0231332(hisS)
            PFA: PF14_0428
            CPV: cgd8_4010
            CHO: Chro.80461
            TAN: TA13155 TA19080
            TPV: TP01_0145
            TET: TTHERM_00401980 TTHERM_00721830
            TBR: Tb927.6.2060
            TCR: 507019.40
            LMA: LmjF30.0630
            EHI: 26.t00043
            ECO: b2514(hisS)
            ECJ: JW2498(hisS)
            ECE: Z3777(hisS)
            ECS: ECs3376
            ECC: c3036(hisS)
            ECI: UTI89_C2835(hisS)
            ECP: ECP_2519
            ECV: APECO1_4010(hisS)
            ECW: EcE24377A_2798(hisS)
            STY: STY2767(hisS)
            STT: t0334(hisS)
            SPT: SPA0345(hisS)
            SEC: SC2519(hisS)
            STM: STM2522(hisS)
            YPE: YPO2878(hisS)
            YPK: y1354(hisS)
            YPM: YP_2744(hisS)
            YPA: YPA_2318
            YPN: YPN_1260
            YPP: YPDSF_2223
            YPS: YPTB2840(hisS)
            YPI: YpsIP31758_1187(hisS)
            YEN: YE1074(hisS)
            SFL: SF2560(hisS)
            SFX: S2732(hisS)
            SFV: SFV_2561(hisS)
            SSN: SSON_2596(hisS)
            SBO: SBO_2538(hisS)
            SDY: SDY_2710(hisS)
            ECA: ECA3219(hisS)
            PLU: plu1377(hisS)
            BUC: BU288(hisS)
            BAS: BUsg277(hisS)
            BAB: bbp267(hisS)
            BCC: BCc_177(hisS)
            WBR: WGLp574(hisS)
            SGL: SG1759
            ENT: Ent638_3008
            KPN: KPN_02844(hisS)
            SPE: Spro_3608
            BFL: Bfl531(hisS)
            BPN: BPEN_550(hisS)
            HIN: HI0369(hisS)
            HIT: NTHI0489(hisS)
            HIP: CGSHiEE_01160(hisS)
            HDU: HD1039(hisS)
            HSO: HS_0405(hisS)
            PMU: PM2011(hisS)
            MSU: MS1920(hisS)
            APL: APL_1175(hisS)
            ASU: Asuc_2026
            XFA: XF2222
            XFT: PD1270(hisS)
            XCC: XCC1806(hisS)
            XCB: XC_2383
            XCV: XCV1872(hisS)
            XAC: XAC1826(hisS)
            XOO: XOO2251(hisS)
            XOM: XOO_2114(XOO2114)
            VCH: VC0760
            VCO: VC0395_A0289(hisS)
            VVU: VV1_0426
            VVY: VV0767
            VPA: VP0609
            VFI: VF0630
            PPR: PBPRA0764
            PAE: PA3802(hisS)
            PAU: PA14_14890(hisS)
            PAP: PSPA7_1312(hisS)
            PPU: PP_0854(hisS)
            PPF: Pput_0884
            PST: PSPTO_1435(hisS)
            PSB: Psyr_1249
            PSP: PSPPH_1321(hisS)
            PFL: PFL_4953(hisS)
            PFO: Pfl_4600
            PEN: PSEEN1022(hisS)
            PMY: Pmen_3499
            PSA: PST_3030(hisS)
            PAR: Psyc_0683(hisS)
            PCR: Pcryo_0653
            PRW: PsycPRwf_1901
            ACI: ACIAD0562(hisS)
            ACB: A1S_0503
            SON: SO_3311(hisS)
            SDN: Sden_1257
            SFR: Sfri_1117
            SAZ: Sama_2364
            SBL: Sbal_2989
            SBM: Shew185_3004
            SLO: Shew_1291
            SPC: Sputcn32_2651
            SSE: Ssed_1433
            SPL: Spea_1306
            SHE: Shewmr4_1229
            SHM: Shewmr7_1300
            SHN: Shewana3_1230
            SHW: Sputw3181_1356
            ILO: IL2033(hisS)
            CPS: CPS_4251(hisS)
            PHA: PSHAb0137(hisS)
            PAT: Patl_3125
            SDE: Sde_1435
            PIN: Ping_1169
            MAQ: Maqu_1128
            CBU: CBU_1248(hisS)
            CBD: COXBU7E912_1332(hisS)
            LPN: lpg1544(hisS)
            LPF: lpl1482(hisS)
            LPP: lpp1501(hisS)
            MCA: MCA2889(hisS)
            FTU: FTT0052(hisS)
            FTF: FTF0052(hisS)
            FTW: FTW_0128(hisS)
            FTL: FTL_1807
            FTH: FTH_1744(hisS)
            FTA: FTA_1914(hisS)
            FTN: FTN_1658(hisS)
            TCX: Tcr_0622
            NOC: Noc_0902
            AEH: Mlg_1252
            HHA: Hhal_1788
            HCH: HCH_04455(hisS)
            CSA: Csal_2855
            ABO: ABO_1859(hisS)
            MMW: Mmwyl1_1357
            AHA: AHA_1760(hisS)
            DNO: DNO_0517(hisS)
            BCI: BCI_0009(hisS)
            CRP: CRP_173
            RMA: Rmag_0671
            VOK: COSY_0618(hisS)
            NME: NMB0854(hisS)
            NMA: NMA1065(hisS)
            NMC: NMC0794(hisS)
            NGO: NGO0426
            CVI: CV_3537(hisS)
            RSO: RSc1216(hisS)
            REU: Reut_A2085
            REH: H16_A2355(hisZ) H16_A2363(hisS)
            RME: Rmet_2105
            BMA: BMA1344(hisS)
            BMV: BMASAVP1_A1834(hisS)
            BML: BMA10299_A0063(hisS)
            BMN: BMA10247_1106(hisS)
            BXE: Bxe_A1595
            BVI: Bcep1808_1738
            BUR: Bcep18194_A5103 Bcep18194_A5112(hisS)
            BCN: Bcen_6268
            BCH: Bcen2424_1811
            BAM: Bamb_1749
            BPS: BPSL1514(hisS)
            BPM: BURPS1710b_2353(hisS)
            BPL: BURPS1106A_2227(hisS)
            BPD: BURPS668_2189(hisS)
            BTE: BTH_I2235(hisS)
            PNU: Pnuc_1290
            BPE: BP2198(hisS)
            BPA: BPP2854(hisS)
            BBR: BB3175(hisS)
            RFR: Rfer_2306
            POL: Bpro_2607
            PNA: Pnap_1873
            AAV: Aave_1425
            AJS: Ajs_1171
            VEI: Veis_0079
            MPT: Mpe_A1995
            HAR: HEAR1265(hisS) HEAR1274(hisZ)
            MMS: mma_2126(hisS)
            NEU: NE0150(hisS)
            NET: Neut_2167
            NMU: Nmul_A2376
            EBA: ebA1260(hisS)
            AZO: azo0928(hisS)
            DAR: Daro_2984
            TBD: Tbd_0595
            MFA: Mfla_1619
            HPY: HP1190(hisS)
            HPJ: jhp1115(hisS)
            HPA: HPAG1_1131
            HHE: HH1809(hisS)
            HAC: Hac_1566(hisS)
            WSU: WS1449
            TDN: Tmden_1130
            CJE: Cj0765c(hisS)
            CJR: CJE0856(hisS)
            CJJ: CJJ81176_0786(hisS)
            CJU: C8J_0716(hisS)
            CJD: JJD26997_1247(hisS)
            CFF: CFF8240_0894(hisS)
            CHA: CHAB381_0925(hisS)
            CCO: CCC13826_1272(hisS)
            ABU: Abu_0965(hisS)
            NIS: NIS_0818(hisS)
            SUN: SUN_1355(hisS)
            GSU: GSU1659(hisS)
            GME: Gmet_1913(hisS)
            GUR: Gura_0661 Gura_1887
            PCA: Pcar_1041(hisS)
            PPD: Ppro_0519 Ppro_1381
            DVU: DVU3368(hisS)
            DVL: Dvul_0027
            DDE: Dde_0011
            LIP: LI0986(hisS)
            BBA: Bd1107(hisS)
            DPS: DP0571
            ADE: Adeh_1264 Adeh_1510
            AFW: Anae109_2313 Anae109_2505
            MXA: MXAN_3725(hisS)
            SAT: SYN_02534
            SFU: Sfum_3303
            RPR: RP308(hisS)
            RTY: RT0298(hisS)
            RCO: RC0412(hisS)
            RFE: RF_0498(hisS)
            RBE: RBE_0533(hisS)
            RAK: A1C_02295(hisS)
            RBO: A1I_03055(hisS)
            RRI: A1G_02350(hisS)
            OTS: OTBS_1585(hisS)
            WOL: WD1076(hisS)
            WBM: Wbm0412
            AMA: AM138(hisS)
            APH: APH_0120(hisS)
            ERU: Erum7010(hisS)
            ERW: ERWE_CDS_07360(hisS)
            ERG: ERGA_CDS_07280(hisS)
            ECN: Ecaj_0712
            ECH: ECH_0291(hisS)
            NSE: NSE_0781(hisS)
            PUB: SAR11_0478(hisS) SAR11_0479(hisZ)
            MLO: mlr6928
            MES: Meso_0422
            PLA: Plav_0598 Plav_0599
            SME: SMc00919(hisS)
            SMD: Smed_0403
            ATU: Atu0676(hisS)
            ATC: AGR_C_1210
            RET: RHE_CH00821(hisS)
            RLE: RL0877 RL0878(hisZ)
            BME: BMEII1056
            BMF: BAB2_0181(hisS)
            BMS: BRA0187(hisS)
            BMB: BruAb2_0182(hisS)
            BOV: BOV_A0169(hisS)
            OAN: Oant_3017
            BJA: bll7457(hisS)
            BRA: BRADO6038(hisS) BRADO6106
            BBT: BBta_1681 BBta_1740(hisS)
            RPA: RPA1178
            RPB: RPB_1185
            RPC: RPC_0893
            RPD: RPD_1289
            RPE: RPE_0872 RPE_0914
            NWI: Nwi_2533(hisS)
            NHA: Nham_3154
            BHE: BH13610(hisS)
            BQU: BQ10830(hisS)
            BBK: BARBAKC583_1178(hisS)
            XAU: Xaut_1216
            CCR: CC_3513
            SIL: SPO0667(hisS)
            SIT: TM1040_0503
            RSP: RSP_3551(hisS)
            RSH: Rsph17029_3234
            JAN: Jann_0945
            RDE: RD1_4064(hisZ) RD1_4065(hisS)
            PDE: Pden_1925
            MMR: Mmar10_0599
            HNE: HNE_0577(hisS)
            ZMO: ZMO1508(hisS)
            NAR: Saro_0289
            SAL: Sala_2715
            SWI: Swit_2531
            ELI: ELI_14260
            GOX: GOX0033 GOX1447
            GBE: GbCGDNIH1_0605
            ACR: Acry_1013
            RRU: Rru_A0748 Rru_A1105
            MGM: Mmc1_3590
            ABA: Acid345_1205
            SUS: Acid_1537
            BSU: BG12605(hisS)
            BHA: BH1251(hisS)
            BAN: BA3376(hisS-1) BA4633(hisS-2)
            BAR: GBAA3376(hisS-1) GBAA4633(hisS-2)
            BAA: BA_3876 BA_5072
            BAT: BAS3130 BAS4298
            BCE: BC3317 BC4398
            BCA: BCE_3348(hisS) BCE_4486(hisS)
            BCZ: BCZK1289(hisZ) BCZK3024(hisS) BCZK4146(hisS)
            BCY: Bcer98_3119
            BTK: BT9727_3117(hisS) BT9727_4136(hisS)
            BTL: BALH_3985(hisS)
            BLI: BL01122(hisS)
            BLD: BLi02882(hisS)
            BCL: ABC1576(hisS) ABC3050(hisZ) ABC3310
            BAY: RBAM_024670(hisS) RBAM_032140(hisZ)
            OIH: OB2020(hisS)
            GKA: GK2573 GK3077
            SAU: SA1457(hisS)
            SAV: SAV1631(hisS)
            SAM: MW1581(hisS)
            SAR: SAR1711(hisS)
            SAS: SAS1567
            SAC: SACOL1686(hisS)
            SAB: SAB1500c(hisS)
            SAA: SAUSA300_1587(hisS)
            SAO: SAOUHSC_01738
            SAJ: SaurJH9_1688
            SAH: SaurJH1_1721
            SEP: SE1312
            SER: SERP1193(hisS)
            SHA: SH1290(hisS)
            SSP: SSP1128
            LMO: lmo1520(hisS)
            LMF: LMOf2365_1539(hisS)
            LIN: lin1555(hisS)
            LWE: lwe1533(hisS)
            LLA: L0342(hisS)
            LLC: LACR_2228
            LLM: llmg_1297(hisZ) llmg_2217(hisS)
            SPY: SPy_2157(hisS)
            SPZ: M5005_Spy_1814(hisS)
            SPM: spyM18_2189(hisS)
            SPG: SpyM3_1815(hisS)
            SPS: SPs1813
            SPH: MGAS10270_Spy1906(hisS)
            SPI: MGAS10750_Spy1931(hisS)
            SPJ: MGAS2096_Spy1846(hisS)
            SPK: MGAS9429_Spy1825(hisS)
            SPF: SpyM51789(hisS)
            SPA: M6_Spy1833
            SPB: M28_Spy1823(hisS)
            SPN: SP_2121
            SPR: spr1931(hisS)
            SPD: SPD_1950(hisS)
            SAG: SAG2108(hisS)
            SAN: gbs2061(hisS)
            SAK: SAK_2047(hisS)
            SMU: SMU.2102(hisS)
            STC: str1971(hisS)
            STL: stu1971(hisS)
            SSA: SSA_2284(hisS)
            SGO: SGO_2062(hisS)
            LPL: lp_1981(hisS)
            LJO: LJ1392
            LAC: LBA0935
            LSA: LSA0863(hisS)
            LSL: LSL_0852(hisS)
            LDB: Ldb0888(hisS)
            LBU: LBUL_0812
            LBR: LVIS_0735
            LCA: LSEI_1527
            LRE: Lreu_1830 Lreu_1848
            EFA: EF1971(hisS)
            OOE: OEOE_0589
            STH: STH2422(hisS1)
            CAC: CAC2740(hisS)
            CPE: CPE1934(hisS)
            CPF: CPF_2189(hisS)
            CPR: CPR_1900(hisS)
            CTC: CTC01958
            CNO: NT01CX_1060(hisS) NT01CX_1848(hisS)
            CTH: Cthe_1332 Cthe_2880
            CDF: CD2740(hisS)
            CBO: CBO3055(hisS)
            CBA: CLB_3084(hisS)
            CBH: CLC_2957(hisS)
            CBF: CLI_3114(hisS)
            CBE: Cbei_1315 Cbei_1544 Cbei_3091
            CKL: CKL_3127(hisS)
            AMT: Amet_0570 Amet_2171 Amet_2358
            CHY: CHY_2205(hisS)
            DSY: DSY2432
            DRM: Dred_0756 Dred_2359
            PTH: PTH_1048(hisS)
            SWO: Swol_0811 Swol_1770
            CSC: Csac_0676 Csac_2027
            TTE: TTE1230(hisS)
            MTA: Moth_1677 Moth_2037
            MGE: MG_035(hisS)
            MPN: MPN045(hisS)
            MPU: MYPU_3330(hisS)
            MPE: MYPE2860(hisS)
            MGA: MGA_0947(hisS)
            MMY: MSC_0334(hisS)
            MMO: MMOB2730(hisS)
            MHY: mhp138(hisS)
            MHJ: MHJ_0234(hisS)
            MHP: MHP7448_0242(hisS)
            MSY: MS53_0437(hisS)
            MCP: MCAP_0324(hisS)
            UUR: UU285(hisS)
            POY: PAM127(hisS)
            AYW: AYWB_594(hisS)
            MFL: Mfl366
            MTU: Rv2580c(hisS)
            MTC: MT2657(hisS)
            MBO: Mb2611c(hisS)
            MBB: BCG_2603c(hisS)
            MLE: ML0494(hisS)
            MPA: MAP1052(hisS)
            MAV: MAV_3460(hisS)
            MSM: MSMEG_2976(hisS)
            MUL: MUL_1732(hisS)
            MVA: Mvan_2590
            MGI: Mflv_3809
            MMC: Mmcs_2285
            MKM: Mkms_2332
            MJL: Mjls_2324
            CGL: NCgl1585(hisS)
            CGB: cg1855(hisS)
            CEF: CE1763
            CDI: DIP1360(hisS)
            CJK: jk1045(hisS)
            NFA: nfa36640(hisS)
            RHA: RHA1_ro06904(hisS)
            SCO: SCO1508(hisS)
            SMA: SAV6844(hisS)
            TWH: TWT785(hisS)
            TWS: TW794(hisS)
            LXX: Lxx17220(hisS)
            ART: Arth_2293
            PAC: PPA1169
            NCA: Noca_2397
            TFU: Tfu_0759
            FRA: Francci3_3548
            FAL: FRAAL5744(hisS)
            ACE: Acel_1335
            KRA: Krad_0299
            SEN: SACE_2032(hisS)
            STP: Strop_1819
            BLO: BL0017(hisS)
            BAD: BAD_0575(hisS)
            RXY: Rxyl_1100 Rxyl_1340
            FNU: FN0298
            RBA: RB251(hisS)
            CTR: CT543(hisS)
            CTA: CTA_0593(hisS)
            CMU: TC0830
            CPN: CPn0663(hisS)
            CPA: CP0084
            CPJ: CPj0663(hisS)
            CPT: CpB0689
            CCA: CCA00076(hisS)
            CAB: CAB078(hisS)
            CFE: CF0928(hisS)
            PCU: pc0385(hisS)
            BBU: BB0135(hisS)
            BGA: BG0137(hisS)
            BAF: BAPKO_0137(hisS)
            TPA: TP0641
            TDE: TDE1442(hisS)
            LIL: LA0054(hisS1) LA1111(hisS2)
            LIC: LIC10048(hisS) LIC12564(hisZ)
            LBJ: LBJ_0042(hisS)
            LBL: LBL_2996(hisS)
            SYN: slr0357(hisS)
            SYW: SYNW0197(hisS)
            SYC: syc1835_d(hisS)
            SYF: Synpcc7942_2263
            SYD: Syncc9605_0188
            SYE: Syncc9902_0220
            SYG: sync_0232(hisS)
            SYR: SynRCC307_0158(hisS)
            SYX: SynWH7803_0243(hisS)
            CYA: CYA_2495(hisS)
            CYB: CYB_0694(hisS)
            TEL: tll1898(hisS)
            GVI: gll2557(hisS)
            ANA: all5012(hisS)
            AVA: Ava_2260
            PMA: Pro0779(hisS)
            PMM: PMM0623(hisS)
            PMT: PMT1905(hisS)
            PMN: PMN2A_0061 PMN2A_0307
            PMI: PMT9312_0623
            PMB: A9601_06791(hisS)
            PMC: P9515_06881(hisS)
            PMF: P9303_25401(hisS)
            PMG: P9301_06491(hisS)
            PMH: P9215_07051(hisS)
            PME: NATL1_06821(hisS)
            TER: Tery_0577 Tery_0758
            BTH: BT_1840
            BFR: BF3416
            BFS: BF3238
            PGI: PG2062(hisS)
            SRU: SRU_0839(hisS)
            CHU: CHU_2673(hisS)
            GFO: GFO_1113(hisS)
            FJO: Fjoh_5052
            FPS: FP2021(hisS)
            CTE: CT0236(hisS)
            CCH: Cag_1467
            CPH: Cpha266_0364
            PVI: Cvib_0696
            PLT: Plut_1786
            DET: DET0006(hisS) DET0846
            DEH: cbdb_A7(hisS) cbdb_A829(hisS)
            DEB: DehaBAV1_0006 DehaBAV1_0765
            RRS: RoseRS_3187 RoseRS_4574
            RCA: Rcas_0121 Rcas_2915
            DRA: DR_1349(hisS)
            DGE: Dgeo_0783 Dgeo_1121
            TTH: TTC0360
            TTJ: TTHA0712
            AAE: aq_122(hisS)
            TMA: TM1043 TM1090
            TPT: Tpet_1653
            TME: Tmel_0744
            FNO: Fnod_1453
            MJA: MJ1000(hisS)
            MMP: MMP1614(hisS)
            MMQ: MmarC5_1794
            MMZ: MmarC7_0862
            MAE: Maeo_0030
            MVN: Mevan_0924
            MAC: MA0943(hisS)
            MBA: Mbar_A3452
            MMA: MM_2061
            MBU: Mbur_2348
            MTP: Mthe_0933
            MHU: Mhun_2918
            MEM: Memar_1585
            MBN: Mboo_1734
            MTH: MTH244
            MST: Msp_0648(hisS)
            MSI: Msm_1181
            MKA: MK1538(hisS)
            AFU: AF1642(hisS)
            HAL: VNG2005G(hisS)
            HMA: rrnAC3183(hisS)
            HWA: HQ1107A(hisS)
            NPH: NP5044A(hisS)
            TAC: Ta0099
            TVO: TVN0154
            PTO: PTO0512
            PHO: PH0290
            PAB: PAB1100(hisS)
            PFU: PF0264
            TKO: TK1562
            RCI: LRC67(hisS)
            APE: APE_0662.1
            SMR: Smar_0986
            IHO: Igni_0879
            HBU: Hbut_0954
            SSO: SSO0279(hisS)
            STO: ST0323
            SAI: Saci_0663
            MSE: Msed_2267
            PAI: PAE1553
            PIS: Pisl_1621
            PCL: Pcal_0528
            PAS: Pars_0658
            TPE: Tpen_0659
            NEQ: NEQ102
STRUCTURES  PDB: 1ADJ  1ADY  1H4V  1HTT  1KMM  1KMN  1QE0  1WU7  1X59  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.21
            ExPASy - ENZYME nomenclature database: 6.1.1.21
            ExplorEnz - The Enzyme Database: 6.1.1.21
            ERGO genome analysis and discovery system: 6.1.1.21
            BRENDA, the Enzyme Database: 6.1.1.21
            CAS: 9068-78-4
///
ENTRY       EC 6.1.1.22                 Enzyme
NAME        asparagine---tRNA ligase;
            asparaginyl-tRNA synthetase;
            asparaginyl-transfer ribonucleate synthetase;
            asparaginyl transfer RNA synthetase;
            asparaginyl transfer ribonucleic acid synthetase;
            asparagyl-transfer RNA synthetase;
            asparagine translase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-asparagine:tRNAAsn ligase (AMP-forming)
REACTION    ATP + L-asparagine + tRNAAsn = AMP + diphosphate +
            L-asparaginyl-tRNAAsn [RN:R03648]
ALL_REAC    R03648
SUBSTRATE   ATP [CPD:C00002];
            L-asparagine [CPD:C00152];
            tRNA(Asn) [CPD:C01637]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-asparaginyl-tRNA(Asn) [CPD:C03402]
REFERENCE   1  [PMID:5040239]
  AUTHORS   Davies MR, Marshall RD.
  TITLE     Partial purification of L-asparaginyl-tRNA synthetase from rabbit
            liver.
  JOURNAL   Biochem. Biophys. Res. Commun. 47 (1972) 1386-95.
  ORGANISM  rabbit
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
            PATH: map00970  Aminoacyl-tRNA biosynthesis
ORTHOLOGY   KO: K01893  asparaginyl-tRNA synthetase
GENES       HSA: 4677(NARS) 79731(NARS2)
            MMU: 70223(Nars)
            CFA: 607631(NARS)
            GGA: 419026(NARS2) 426856(RCJMB04_13p14)
            XLA: 446783(nars)
            SPU: 579372(LOC579372)
            DME: Dmel_CG10687(Aats-asn) Dmel_CG6796
            ATH: AT1G70980(SYNC1) AT3G07420(NS2) AT4G17300(NS1)
                 AT5G56680(EMB2755)
            OSA: 4325717 4328255 4343250 4352065
            CME: CMM098C CMR205C
            SCE: YCR024C(SLM5) YHR019C(DED81)
            AGO: AGOS_AEL020W AGOS_AEL054C
            PIC: PICST_33068(SYN3) PICST_84563(SYN4)
            CGR: CAGL0A02112g CAGL0L08030g
            SPO: SPBC1198.10c SPBC1773.10c
            ANI: AN3073.2 AN7479.2
            AFM: AFUA_2G05650 AFUA_3G09630
            AOR: AO090001000680 AO090005001286
            CNE: CND03890 CNE01390
            UMA: UM04442.1
            ECU: ECU09_1680
            DDI: DDB_0231333(asnS1) DDB_0231334(asnS2)
            PFA: PFB0525w PFE0475w
            CPV: cgd8_350
            CHO: Chro.80047
            TAN: TA05825 TA14880
            TPV: TP01_0818 TP02_0746
            TET: TTHERM_00691890
            TBR: Tb927.4.2310
            TCR: 506559.350
            LMA: LmjF34.2340
            EHI: 159.t00005
            ECO: b0930(asnS)
            ECJ: JW0913(asnS)
            ECE: Z1278(asnS)
            ECS: ECs1013
            ECC: c1072(asnS)
            ECI: UTI89_C1002(asnS)
            ECP: ECP_0941
            ECW: EcE24377A_1030(asnS)
            ECX: EcHS_A1038
            STY: STY1004(asnS)
            STT: t1934(asnS)
            SPT: SPA1798(asnS)
            SEC: SC0957(asnS)
            STM: STM1000(asnS)
            YPE: YPO1412(asnS)
            YPK: y2758(asnS)
            YPM: YP_1181(asnS)
            YPA: YPA_0707
            YPN: YPN_2565
            YPS: YPTB1436(asnS)
            YPI: YpsIP31758_2558(asnS)
            SFL: SF0927(asnS)
            SFX: S0991(asnS)
            SFV: SFV_0932(asnS)
            SSN: SSON_0933(asnS)
            SBO: SBO_2221(asnS)
            SDY: SDY_2327(asnS)
            ECA: ECA2541(asnS)
            PLU: plu1753(asnS)
            BUC: BU360(asnS)
            BAS: BUsg348(asnS)
            BAB: bbp329(asnS)
            BCC: BCc_221(asnS)
            WBR: WGLp263(asnS)
            SGL: SG1015
            BFL: Bfl421(asnS)
            BPN: BPEN_433(asnS)
            HIN: HI1302(asnS)
            HIT: NTHI1615(asnS)
            HIQ: CGSHiGG_01455(asnC)
            HDU: HD1411(asnS)
            HSO: HS_0756(asnS)
            PMU: PM0643(asnS)
            MSU: MS1042(asnS)
            APL: APL_0675(asnS)
            ASU: Asuc_1294
            XFA: XF2563
            XFT: PD1947(asnS)
            XCC: XCC1561(asnS)
            XCB: XC_2673
            XCV: XCV1659(asnS)
            XAC: XAC1618(asnS)
            XOO: XOO2418(asnS)
            XOM: XOO_2296(XOO2296)
            VCH: VC1297
            VCO: VC0395_A0915(asnS)
            VVU: VV1_2254
            VVY: VV2090
            VPA: VP1893
            VFI: VF1159
            PPR: PBPRA2335(asnS)
            SON: SO_2218(asnS)
            SDN: Sden_1958
            SFR: Sfri_2169
            SHE: Shewmr4_2128
            SHM: Shewmr7_2204
            SHN: Shewana3_2306
            ILO: IL1327(asnS)
            CPS: CPS_2591(asnS)
            PHA: PSHAa1616(asnS)
            PAT: Patl_1879
            PIN: Ping_1926
            LPN: lpg2282(asnS)
            LPF: lpl2208(asnS)
            LPP: lpp2236(asnS)
            HCH: HCH_02239(asnS)
            AHA: AHA_1486(asnS)
            BCI: BCI_0408(asnS)
            GSU: GSU1156(asnS)
            GME: Gmet_2412
            PCA: Pcar_0586
            DVU: DVU0007(asnS)
            DDE: Dde_0099
            LIP: LI0704(asnS)
            BBA: Bd1054(asnS)
            DPS: DP1331
            ADE: Adeh_2728
            MXA: MXAN_2298(asnS)
            SFU: Sfum_2475
            AMA: AM199(aspS) AM200(aspS)
            BRA: BRADO3359(aspS)
            BBT: BBta_3864(aspS)
            ABA: Acid345_4597
            BSU: BG10958(asnS)
            BHA: BH1696(asnS)
            BAN: BA4802(asnS)
            BAR: GBAA4802(asnS)
            BAA: BA_5227
            BAT: BAS4454
            BCE: BC4559
            BCA: BCE_4685(asnS)
            BCZ: BCZK4302(asnS)
            BTK: BT9727_4292(asnS)
            BTL: BALH_4140(asnS)
            BLI: BL02745(asnS)
            BLD: BLi02371(asnS)
            BCL: ABC2059(asnS)
            BAY: RBAM_020510
            BPU: BPUM_1968
            OIH: OB1759(asnS)
            GKA: GK2171(asnS)
            SAU: SA1287(asnS)
            SAV: SAV1454(asnS)
            SAM: MW1344(asnS)
            SAR: SAR1465(asnS)
            SAS: SAS1397
            SAC: SACOL1494(asnS)
            SAB: SAB1318c(asnS)
            SAA: SAUSA300_1345(asnS)
            SAO: SAOUHSC_01471
            SEP: SE1142
            SER: SERP1024(asnS)
            SHA: SH1458(asnS)
            SSP: SSP1290
            LMO: lmo1896(ansB)
            LMF: LMOf2365_1925(asnS)
            LIN: lin2010(ansB)
            LWE: lwe1915(asnS)
            LLA: L0345(asnS)
            LLC: LACR_2020
            LLM: llmg_2017(asnS)
            SPY: SPy_0651(asnS)
            SPZ: M5005_Spy_0538(asnS)
            SPM: spyM18_0712(asnS)
            SPG: SpyM3_0461(asnS)
            SPS: SPs1394
            SPH: MGAS10270_Spy0532(asnS)
            SPI: MGAS10750_Spy0556(asnS)
            SPJ: MGAS2096_Spy0549(asnS)
            SPK: MGAS9429_Spy0528(asnS)
            SPF: SpyM51326(asnS)
            SPA: M6_Spy0558
            SPB: M28_Spy0516(asnS)
            SPN: SP_1542
            SPR: spr1397(asnS)
            SPD: SPD_1371(asnS)
            SAG: SAG0526(asnS)
            SAN: gbs0572(asnS)
            SAK: SAK_0677(asnS)
            SMU: SMU.1311(asnS)
            STC: str0818(asnS)
            STL: stu0818(asnS)
            SSA: SSA_1377(asnS)
            SGO: SGO_1293(asnS)
            LPL: lp_0956(asnS1) lp_1740(asnS2)
            LJO: LJ1200
            LAC: LBA1162
            LSA: LSA0914(asnS)
            LSL: LSL_0689(asnS)
            LDB: Ldb1004(asnSa) Ldb1195(asnSb)
            LBU: LBUL_0911 LBUL_1111
            LBR: LVIS_2017
            LCA: LSEI_1485
            LRE: Lreu_1886
            EFA: EF2371(asnS)
            OOE: OEOE_1097
            STH: STH1582(asnS)
            CAC: CAC3260(asnS)
            CPE: CPE2500(asnS)
            CPF: CPF_2823(asnS)
            CPR: CPR_2509(asnS)
            CTC: CTC00143
            CNO: NT01CX_1233(asnS)
            CDF: CD2245(asnS)
            CBO: CBO0597(asnS)
            CBA: CLB_0637(asnS)
            CBH: CLC_0651(asnS)
            CBF: CLI_0677(asnS)
            CKL: CKL_0118(asnS)
            DSY: DSY4952
            MGE: MG_113(asnS)
            MPN: MPN252(asnS)
            MPU: MYPU_7710(asnS)
            MPE: MYPE4040(asnS)
            MGA: MGA_1065(asnS)
            MMY: MSC_0080(asnS)
            MMO: MMOB5070(asnS)
            MHY: mhp416(asnS) mhp497(asnS)
            MHJ: MHJ_0414(asnS) MHJ_0497
            MHP: MHP7448_0401(asnS) MHP7448_0500
            MSY: MS53_0422(asnS)
            MCP: MCAP_0824(asnS)
            UUR: UU365(asnS)
            POY: PAM754(asnS)
            AYW: AYWB_671(asnS)
            MFL: Mfl480
            FNU: FN0040
            RBA: RB13263(asnS)
            PCU: pc0346(asnS)
            BGA: BG0102(asnS)
            BAF: BAPKO_0102(asnS)
            TPA: TP0609
            TDE: TDE0980(asnS)
            LIL: LA1866(asnS)
            LIC: LIC12025(asnS)
            LBJ: LBJ_1650(asnS)
            LBL: LBL_1869(asnS)
            SYN: sll0495(asnS)
            SYC: syc0710_c(asnS)
            SYF: Synpcc7942_0830
            TEL: tlr2473(asnS)
            ANA: alr3658
            AVA: Ava_3630
            TER: Tery_2246
            BTH: BT_3873
            BFR: BF4016
            BFS: BF3790(asnS)
            PGI: PG1121(asnS)
            SRU: SRU_1832(asnS)
            CHU: CHU_3176(asnS)
            GFO: GFO_0096(asnS)
            FPS: FP2250(asnS)
            DRA: DR_1270(asnS)
            DGE: Dgeo_1136
            TTH: TTC0356
            TTJ: TTHA0708
            TAC: Ta0519
            TVO: TVN0996
            PTO: PTO0892 PTO1412
            PHO: PH0241
            PAB: PAB2203(ASNRS)
            PFU: PF0155
            TKO: TK0759
            RCI: RCIX1877(asnS)
            PAI: PAE2973
STRUCTURES  PDB: 1X54  1X55  1X56  
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.22
            ExPASy - ENZYME nomenclature database: 6.1.1.22
            ExplorEnz - The Enzyme Database: 6.1.1.22
            ERGO genome analysis and discovery system: 6.1.1.22
            BRENDA, the Enzyme Database: 6.1.1.22
            CAS: 37211-76-0
///
ENTRY       EC 6.1.1.23                 Enzyme
NAME        aspartate---tRNAAsn ligase;
            nondiscriminating aspartyl-tRNA synthetase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-aspartate:tRNAAsx ligase (AMP-forming)
REACTION    ATP + L-aspartate + tRNAAsx = AMP + diphosphate + aspartyl-tRNAAsx
            [RN:R03647 R05577]
ALL_REAC    R03647 R05577
SUBSTRATE   ATP [CPD:C00002];
            L-aspartate [CPD:C00049];
            tRNAAsx
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            aspartyl-tRNAAsx
COMMENT     When this enzyme acts on tRNAAsp, it catalyses the same reaction as
            EC 6.1.1.12, aspartate---tRNA ligase. It has, however, diminished
            discrimination, so that it can also form aspartyl-tRNAAsn. This
            relaxation of specificity has been found to result from the absence
            of a loop in the tRNA that specifically recognizes the third
            position of the anticodon [1]. This accounts for the ability of this
            enzyme in, for example, Thermus thermophilus, to recognize both
            tRNAAsp (GUC anticodon) and tRNAAsn (GUU anticodon). The
            aspartyl-tRNAAsn is not used in protein synthesis until it is
            converted by EC 6.3.5.6, asparaginyl-tRNA synthase
            (glutamine-hydrolysing), into asparaginyl-tRNAAsn.
REFERENCE   1  [PMID:10966471]
  AUTHORS   Ibba M, Soll D.
  TITLE     Aminoacyl-tRNA synthesis.
  JOURNAL   Annu. Rev. Biochem. 69 (2000) 617-50.
REFERENCE   2  [PMID:9724658]
  AUTHORS   Schmitt E, Moulinier L, Fujiwara S, Imanaka T, Thierry JC, Moras D.
  TITLE     Crystal structure of aspartyl-tRNA synthetase from Pyrococcus
            kodakaraensis KOD: archaeon specificity and catalytic mechanism of
            adenylate formation.
  JOURNAL   EMBO. J. 17 (1998) 5227-37.
  ORGANISM  Pyrococcus kodakaraensis
REFERENCE   3  [PMID:9789000]
  AUTHORS   Becker HD, Kern D.
  TITLE     Thermus thermophilus: a link in evolution of the tRNA-dependent
            amino acid amidation pathways.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 12832-7.
  ORGANISM  Thermus thermophilus
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
ORTHOLOGY   KO: K09759  nondiscriminating aspartyl-tRNA synthetase
GENES       BAN: BA2186(aspS-1)
            BAR: GBAA2186(aspS-1)
            BAA: BA_2681
            BAT: BAS2031
            BCE: BC2169
            BCZ: BCZK1981(aspS)
            BTK: BT9727_1999(aspS)
            BTL: BALH_1944(aspS)
            CAC: CAC2979(aspS)
            CPF: CPF_0770(aspS)
            DRA: DR_1055
            DGE: Dgeo_0796
            TTH: TTC1087
            TTJ: TTHA1452
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.23
            ExPASy - ENZYME nomenclature database: 6.1.1.23
            ExplorEnz - The Enzyme Database: 6.1.1.23
            ERGO genome analysis and discovery system: 6.1.1.23
            BRENDA, the Enzyme Database: 6.1.1.23
            CAS: 9027-32-1
///
ENTRY       EC 6.1.1.24                 Enzyme
NAME        glutamate---tRNAGln ligase;
            nondiscriminating glutamyl-tRNA synthetase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-glutamate:tRNAGlx ligase (AMP-forming)
REACTION    ATP + L-glutamate + tRNAGlx = AMP + diphosphate + glutamyl-tRNAGlx
            [RN:R03651 R05578]
ALL_REAC    R03651 R05578
SUBSTRATE   ATP [CPD:C00002];
            L-glutamate [CPD:C00025];
            tRNAGlx
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            glutamyl-tRNAGlx
COMMENT     When this enzyme acts on tRNAGlu, it catalyses the same reaction as
            EC 6.1.1.17, glutamate---tRNA ligase. It has, however, diminished
            discrimination, so that it can also form glutamyl-tRNAGln. This
            relaxation of specificity has been found to result from the absence
            of a loop in the tRNA that specifically recognizes the third
            position of the anticodon [1]. This accounts for the ability of this
            enzyme in, for example, Bacillus subtilis, to recognize both
            tRNA1Gln (UUG anticodon) and tRNAGlu (UUC anticodon) but not
            tRNA2Gln (CUG anticodon). The ability of this enzyme to recognize
            both tRNAGlu and one of the tRNAGln isoacceptors derives from their
            sharing a major identity element, a hypermodified derivative of U34
            (5-methylaminomethyl-2-thiouridine). The glutamyl-tRNAGln is not
            used in protein synthesis until it is converted by EC 6.3.5.7,
            glutaminyl-tRNA synthase (glutamine-hydrolysing), into
            glutaminyl-tRNAGln.
REFERENCE   1  [PMID:10966471]
  AUTHORS   Ibba M, Soll D.
  TITLE     Aminoacyl-tRNA synthesis.
  JOURNAL   Annu. Rev. Biochem. 69 (2000) 617-50.
REFERENCE   2  [PMID:9724658]
  AUTHORS   Schmitt E, Moulinier L, Fujiwara S, Imanaka T, Thierry JC, Moras D.
  TITLE     Crystal structure of aspartyl-tRNA synthetase from Pyrococcus
            kodakaraensis KOD: archaeon specificity and catalytic mechanism of
            adenylate formation.
  JOURNAL   EMBO. J. 17 (1998) 5227-37.
REFERENCE   3  [PMID:9749534]
  AUTHORS   Kim SI, Soll D.
  TITLE     Major identity element of glutamine tRNAs from Bacillus subtilis and
            Escherichia coli in the reaction with B. subtilis glutamyl-tRNA
            synthetase.
  JOURNAL   Mol. Cells. 8 (1998) 459-65.
  ORGANISM  Bacillus subtilis [GN:bsu], Escherichia coli [GN:eco]
PATHWAY     PATH: map00251  Glutamate metabolism
ORTHOLOGY   KO: K09698  nondiscriminating glutamyl-tRNA synthetase
GENES       BSU: BG10154(gltX)
            BAN: BA0086(gltX)
            BAR: GBAA0086(gltX)
            BAA: BA_0676
            BAT: BAS0087
            BCA: BCE_0087(gltX)
            BCZ: BCZK0083(gltX)
            BTK: BT9727_0084(gltX)
            BTL: BALH_0087(gltX)
            BLI: BL03267(gltX)
            BLD: BLi00110(gltX)
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.24
            ExPASy - ENZYME nomenclature database: 6.1.1.24
            ExplorEnz - The Enzyme Database: 6.1.1.24
            ERGO genome analysis and discovery system: 6.1.1.24
            BRENDA, the Enzyme Database: 6.1.1.24
            CAS: 9068-76-2
///
ENTRY       EC 6.1.1.25                 Enzyme
NAME        lysine---tRNAPyl ligase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-lysine:tRNAPyl ligase (AMP-forming)
REACTION    ATP + L-lysine + tRNAPyl = AMP + diphosphate + L-lysyl-tRNAPyl
            [RN:R07646]
ALL_REAC    R07646
SUBSTRATE   ATP [CPD:C00002];
            L-lysine [CPD:C00047];
            tRNA(Pyl) [CPD:C16139]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-lysyl-tRNA(Pyl) [CPD:C16140]
COMMENT     In organisms such as Methanosarcina barkeri that incorporate the
            modified amino acid pyrrolysine (Pyl) into certain methylamine
            methyltransferases, an unusual tRNAPyl, with a CUA anticodon, is
            charged with lysine by this class II aminoacyl---tRNA ligase. The
            tRNA and the ligase are encoded within the same gene cluster, and
            the ligase does not appear to be closely related to EC 6.1.1.6,
            lysine---tRNA ligase.
REFERENCE   1  [PMID:12029131]
  AUTHORS   Srinivasan G, James CM, Krzycki JA.
  TITLE     Pyrrolysine encoded by UAG in Archaea: charging of a UAG-decoding
            specialized tRNA.
  JOURNAL   Science. 296 (2002) 1459-62.
  ORGANISM  Methanosarcina barkeri [GN:mba]
REFERENCE   2  [PMID:12029132]
  AUTHORS   Hao B, Gong W, Ferguson TK, James CM, Krzycki JA, Chan MK.
  TITLE     A new UAG-encoded residue in the structure of a methanogen
            methyltransferase.
  JOURNAL   Science. 296 (2002) 1462-6.
  ORGANISM  Methanosarcina barkeri [GN:mba]
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.25
            ExPASy - ENZYME nomenclature database: 6.1.1.25
            ExplorEnz - The Enzyme Database: 6.1.1.25
            ERGO genome analysis and discovery system: 6.1.1.25
            BRENDA, the Enzyme Database: 6.1.1.25
            CAS: 782472-12-2
///
ENTRY       EC 6.1.1.26                 Enzyme
NAME        pyrrolysine---tRNAPyl ligase;
            PylS;
            pyrrolysyl-tRNA synthetase
CLASS       Ligases;
            Forming carbon-oxygen bonds;
            Ligases forming aminoacyl-tRNA and related compounds
SYSNAME     L-pyrrolysine:tRNAPyl ligase (AMP-forming)
REACTION    ATP + L-pyrrolysine + tRNAPyl = AMP + diphosphate +
            L-pyrrolysyl-tRNAPyl
SUBSTRATE   ATP [CPD:C00002];
            L-pyrrolysine [CPD:C16138];
            tRNA(Pyl) [CPD:C16139]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-pyrrolysyl-tRNAPyl
COMMENT     In organisms such as Methanosarcina barkeri that incorporate the
            modified amino acid pyrrolysine (Pyl) into certain methylamine
            methyltransferases, an unusual tRNAPyl, with a CUA anticodon, can be
            charged directly with pyrrolysine by this class II aminoacyl---tRNA
            ligase. The enzyme is specific for pyrrolysine as substrate as it
            cannot be replaced by lysine or any of the other natural amino acids
            [1].
REFERENCE   1  [PMID:15329732]
  AUTHORS   Blight SK, Larue RC, Mahapatra A, Longstaff DG, Chang E, Zhao G,
            Kang PT, Green-Church KB, Chan MK, Krzycki JA.
  TITLE     Direct charging of tRNA(CUA) with pyrrolysine in vitro and in vivo.
  JOURNAL   Nature. 431 (2004) 333-5.
REFERENCE   2  [PMID:15314242]
  AUTHORS   Polycarpo C, Ambrogelly A, Berube A, Winbush SM, McCloskey JA, Crain
            PF, Wood JL, Soll D.
  TITLE     An aminoacyl-tRNA synthetase that specifically activates
            pyrrolysine.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 12450-4.
REFERENCE   3  [PMID:15372017]
  AUTHORS   Schimmel P, Beebe K.
  TITLE     Molecular biology: genetic code seizes pyrrolysine.
  JOURNAL   Nature. 431 (2004) 257-8.
DBLINKS     IUBMB Enzyme Nomenclature: 6.1.1.26
            ExPASy - ENZYME nomenclature database: 6.1.1.26
            ExplorEnz - The Enzyme Database: 6.1.1.26
            ERGO genome analysis and discovery system: 6.1.1.26
            BRENDA, the Enzyme Database: 6.1.1.26
///
ENTRY       EC 6.2.1.1                  Enzyme
NAME        acetate---CoA ligase;
            acetyl-CoA synthetase;
            acetyl activating enzyme;
            acetate thiokinase;
            acyl-activating enzyme;
            acetyl coenzyme A synthetase;
            acetic thiokinase;
            acetyl CoA ligase;
            acetyl CoA synthase;
            acetyl-coenzyme A synthase;
            short chain fatty acyl-CoA synthetase;
            short-chain acyl-coenzyme A synthetase;
            ACS
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     acetate:CoA ligase (AMP-forming)
REACTION    ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA [RN:R00235]
ALL_REAC    R00235;
            (other) R00236 R00316 R00926 R01354
SUBSTRATE   ATP [CPD:C00002];
            acetate [CPD:C00033];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            acetyl-CoA [CPD:C00024]
COMMENT     Also acts on propanoate and propenoate.
REFERENCE   1  [PMID:12980945]
  AUTHORS   CHOU TC, LIPMANN F.
  TITLE     Separation of acetyl transfer enzymes in pigeon liver extract.
  JOURNAL   J. Biol. Chem. 196 (1952) 89-103.
  ORGANISM  pigeon
REFERENCE   2
  AUTHORS   Eisenberg, M.A.
  TITLE     The acetate-activating enzyme of Rhodospirillum rubrum.
  JOURNAL   Biochim. Biophys. Acta 16 (1955) 58-65.
  ORGANISM  Rhodospirillum rubrum [GN:rru]
REFERENCE   3  [PMID:13143026]
  AUTHORS   HELE P.
  TITLE     The acetate activating enzyme of beef heart.
  JOURNAL   J. Biol. Chem. 206 (1954) 671-6.
  ORGANISM  cow [GN:bta]
REFERENCE   4  [PMID:13159282]
  AUTHORS   MILLERD A, BONNER J.
  TITLE     Acetate activation and acetoacetate formation in plant systems.
  JOURNAL   Arch. Biochem. Biophys. 49 (1954) 343-55.
  ORGANISM  spinach
PATHWAY     PATH: map00010  Glycolysis / Gluconeogenesis
            PATH: map00620  Pyruvate metabolism
            PATH: map00640  Propanoate metabolism
            PATH: map00720  Reductive carboxylate cycle (CO2 fixation)
ORTHOLOGY   KO: K01895  acetyl-CoA synthetase
GENES       HSA: 55902(ACSS2) 84532(ACSS1)
            MMU: 60525(Acss2) 68738(Acss1)
            CFA: 477002(ACSS1) 477205(ACSS2)
            BTA: 282873(ACAS2L)
            GGA: 416714(ACSS1) 419158(ACSS2) 423347(LOC423347)
            XLA: 443879(MGC80104)
            SPU: 585742(LOC585742)
            DME: Dmel_CG8732(l(2)44DEa) Dmel_CG9390(AcCoAS)
            CEL: K03A1.5(sur-5)
            ATH: AT5G36880
            OSA: 4329518 4334496 4335745
            CME: CMK098C
            SCE: YAL054C(ACS1) YLR153C(ACS2)
            AGO: AGOS_ADR408W AGOS_AGL148C
            PIC: PICST_79135(ACS2) PICST_89873(ACS1)
            CGR: CAGL0B02717g CAGL0L00649g
            ANI: AN5626.2
            AFM: AFUA_4G11080 AFUA_8G00500
            AOR: AO090003001112
            CNE: CNA07740
            UMA: UM03069.1
            ECU: ECU05_0310
            DDI: DDBDRAFT_0166991 DDBDRAFT_0217779 DDB_0231684(acsA)
            PFA: PF14_0357 PFF1350c
            CPV: cgd1_3710
            CHO: Chro.10418
            TAN: TA07295
            TPV: TP04_0219
            TET: TTHERM_00052470 TTHERM_00554420 TTHERM_00695650
                 TTHERM_00994060
            TBR: Tb927.8.2520
            TCR: 504427.110 509331.30
            LMA: LmjF23.0540 LmjF23.0710
            ECO: b4069(acs)
            ECJ: JW4030(acs)
            ECE: Z5668(acs)
            ECS: ECs5051
            ECC: c5064(acs)
            ECI: UTI89_C4659(acs)
            ECP: ECP_4301
            ECV: APECO1_2386(acs)
            ECW: EcE24377A_4625(acsA)
            ECX: EcHS_A4314
            STY: STY4473(acs)
            STT: t4181(acs)
            SPT: SPA4092(acs)
            SEC: SC4154(acs)
            STM: STM4275(acs)
            YPE: YPO0253(acs)
            YPK: y0510(acs)
            YPM: YP_0406(acs)
            YPA: YPA_4031
            YPN: YPN_3416
            YPS: YPTB0308(rcs)
            YPI: YpsIP31758_3835(acsA)
            SFV: SFV_4142(acs)
            SSN: SSON_4250(acs)
            ECA: ECA0808(acs)
            PLU: plu0074(acs)
            SGL: SG2122
            PMU: PM0692(acsA)
            XFA: XF2255
            XFT: PD1296(acs)
            XCC: XCC4060(acs)
            XCB: XC_4149
            XCV: XCV4275(acsA)
            XAC: XAC4179(acs)
            XOO: XOO4544(acs)
            XOM: XOO_4280(XOO4280)
            VCH: VC0298 VCA0829
            VCO: VC0395_0406(acs-2) VC0395_A2691(acs-1)
            VVU: VV1_1237 VV2_0456
            VVY: VV3133 VVA1006
            VPA: VP2878 VPA0575
            VFI: VF2383
            PPR: PBPRA3403(acs) PBPRB1168
            PAE: PA0887(acsA) PA1997 PA2555 PA4733(acsB)
            PAU: PA14_31500 PA14_52800(acsA) PA14_62630(acsB)
            PAP: PSPA7_4627(acsA2) PSPA7_5450(acsA1)
            PPU: PP_2213(fadDx) PP_4487(acsA) PP_4702(acsB)
            PST: PSPTO_1825(acs)
            PSB: Psyr_3572
            PSP: PSPPH_3528(acsA)
            PFL: PFL_3068(acs) PFL_4522(acsA) PFL_5281(acsA)
            PFO: Pfl_2870 Pfl_4293 Pfl_4814
            PEN: PSEEN1919 PSEEN3549(fadDx) PSEEN3888(acs-1) PSEEN4738(acs-2)
            PAR: Psyc_0184(acs) Psyc_0821
            PCR: Pcryo_0203 Pcryo_0838
            ACI: ACIAD1606 ACIAD1611 ACIAD3475(acs)
            SON: SO_2743(acs)
            SDN: Sden_2044
            SFR: Sfri_1469 Sfri_2725
            SAZ: Sama_2079
            SBL: Sbal_1752
            SLO: Shew_1533
            SHE: Shewmr4_2319 Shewmr4_2362
            SHM: Shewmr7_2391 Shewmr7_2434
            SHN: Shewana3_1675 Shewana3_2523
            SHW: Sputw3181_1659
            ILO: IL0879 IL2007(acs)
            CPS: CPS_3955(acs)
            PHA: PSHAa0698(acs)
            PAT: Patl_0521
            SDE: Sde_1067
            MAQ: Maqu_2219
            CBU: CBU_0766
            LPN: lpg0127(acsB) lpg1831
            LPF: lpl0126(acsB) lpl1795
            LPP: lpp0141(acsB) lpp1794
            MCA: MCA2043(acs)
            FTA: FTA_1434
            FTN: FTN_0730(acs)
            TCX: Tcr_1116
            NOC: Noc_0873
            AEH: Mlg_0673 Mlg_2597
            HCH: HCH_04804(acsA1) HCH_05074(acsA2)
            CSA: Csal_0865
            ABO: ABO_0334(acsA)
            AHA: AHA_3344(acsA)
            CVI: CV_1758 CV_3282(acsA)
            RSO: RS05310(RSp1265) RS05571(RSp0651) RSc1952(RS03526)
            REU: Reut_A1097 Reut_A1821 Reut_A2229 Reut_B4371
            REH: H16_A1616 H16_A2525(acoE) H16_B0386 H16_B0591 H16_B0696
                 H16_B0834 H16_B1102
            RME: Rmet_1061 Rmet_2270 Rmet_5743
            BMA: BMA0802(acsA) BMAA1794(acs)
            BMV: BMASAVP1_0788(acsA-1) BMASAVP1_A1317(acsA-2)
            BML: BMA10299_1081(acsA-1) BMA10299_A0554(acsA-2)
            BMN: BMA10247_0599(acsA-2) BMA10247_A2054(acsA-1)
            BXE: Bxe_A1395 Bxe_A1862 Bxe_A2769 Bxe_A3113 Bxe_A3573 Bxe_B1085
            BUR: Bcep18194_A4459 Bcep18194_A5520 Bcep18194_B0715
                 Bcep18194_C6650 Bcep18194_C7155 Bcep18194_C7333
            BCN: Bcen_5886
            BCH: Bcen2424_1316 Bcen2424_2191 Bcen2424_4962 Bcen2424_6230
                 Bcen2424_6401
            BAM: Bamb_1201 Bamb_2230
            BPS: BPSL1380 BPSS0375(acoE) BPSS0618
            BPM: BURPS1710b_1709(acsA) BURPS1710b_A1939(acsA)
                 BURPS1710b_A2179(acsA)
            BPL: BURPS1106A_1539 BURPS1106A_A0530(acsA)
            BPD: BURPS668_A0628(acsA)
            BTE: BTH_I2753 BTH_II0927 BTH_II1802 BTH_II2017(acsA)
            BPE: BP2377 BP2409
            BPA: BPP0609 BPP3243 BPP3274
            BBR: BB0615 BB3695 BB3725
            RFR: Rfer_0388 Rfer_2581 Rfer_2698
            POL: Bpro_0761 Bpro_1590 Bpro_2049 Bpro_3358
            MPT: Mpe_A0343 Mpe_A1385
            HAR: HEAR0921(acs)
            MMS: mma_0882
            NEU: NE2341
            NET: Neut_1690
            NMU: Nmul_A1867 Nmul_A1868
            EBA: ebA1206(acsA) ebA172(acsA) ebA4717
            AZO: azo1996(acS1) azo2149(acsA) azo2414(acsB) azo3447(acS2)
            DAR: Daro_1629 Daro_2708
            TBD: Tbd_0504
            MFA: Mfla_1727
            HPY: HP1045
            HPA: HPAG1_0402
            HAC: Hac_1156(acoE)
            WSU: WS0595(ACS)
            TDN: Tmden_1451
            CJE: Cj1537c(acs)
            CJR: CJE1708(acs)
            CJJ: CJJ81176_1522(acs)
            CJU: C8J_1436(acs)
            CJD: JJD26997_1889(acs)
            NIS: NIS_0521(acs)
            SUN: SUN_0967 SUN_1150(acs)
            GME: Gmet_2340
            PCA: Pcar_1242
            DVU: DVU0748(acs) DVU2250 DVU2969
            DDE: Dde_2317 Dde_2823 Dde_3207
            BBA: Bd0504 Bd1306(acs)
            DPS: DP0825(acs) DP0826(acs) DP2097 DPPB37
            MXA: MXAN_2570(acsA) MXAN_5856(acsA)
            SAT: SYN_01223 SYN_02635
            SFU: Sfum_0745 Sfum_3454
            PUB: SAR11_0314(acsA)
            MLO: mll6017 mlr0619 mlr4089
            MES: Meso_3431
            SME: SMc00741 SMc04093(acsA1)
            ATU: Atu2745(acs)
            ATC: AGR_C_4980
            RET: RHE_CH00719(acsA1) RHE_CH03773(ypch01348) RHE_CH04112(acsA2)
                 RHE_PC00128
            RLE: RL4301(acsA) RL4727(acs) pRL100121(acsA) pRL100377
                 pRL80044(acsA)
            BME: BMEI0238 BMEII0815
            BMF: BAB1_1819 BAB2_0787
            BMS: BR1811
            BMB: BruAb1_1791
            BOV: BOV_1744(acsA)
            BJA: bll0975 bll6076 bll7367 blr0107 blr0573 blr1077 blr3958
            BRA: BRADO0344(acsA) BRADO1339
            BBT: BBta_0333(acsA) BBta_6789
            RPA: RPA0211 RPA3445 RPA4504
            RPB: RPB_0319
            RPC: RPC_0042
            RPD: RPD_0474 RPD_3298
            RPE: RPE_0069 RPE_2388 RPE_4586
            NWI: Nwi_0467
            NHA: Nham_0558
            BHE: BH15410(acs)
            BQU: BQ12330(acs)
            BBK: BARBAKC583_0101(acsA)
            CCR: CC_3581
            SIL: SPO1813(acs) SPO2791(acsA)
            SIT: TM1040_0735 TM1040_1489
            RSP: RSP_0579 RSP_1592(acsA)
            JAN: Jann_3285 Jann_3703
            RDE: RD1_0612 RD1_1117(acsA) RD1_2332(acsA)
            MMR: Mmar10_1621
            HNE: HNE_1402(acsA)
            NAR: Saro_2625
            SAL: Sala_1811
            ELI: ELI_04660
            GOX: GOX0413
            GBE: GbCGDNIH1_0265
            RRU: Rru_A3575
            MAG: amb2262 amb3815 amb4177
            MGM: Mmc1_0598
            ABA: Acid345_3520 Acid345_3521
            BSU: BG10370(acsA) BG13834(ytcI)
            BHA: BH1137 BH3201 BH3234(acsA)
            BAN: BA2553 BA4896 BA4915(acsA)
            BAR: GBAA2553 GBAA4896 GBAA4915(acsA)
            BAA: BA_3055 BA_5317 BA_5334
            BAT: BAS2376 BAS4543 BAS4560
            BCE: BC2489 BC4645 BC4659
            BCA: BCE_2554 BCE_4781 BCE_4801(acsA)
            BCZ: BCZK2292(acs) BCZK4389(acsA) BCZK4411(acsA)
            BTK: BT9727_2333(acs) BT9727_4379(acsA) BT9727_4394(acsA)
            BTL: BALH_2294(acs) BALH_4223(acsA) BALH_4242(acsA)
            BLI: BL00440(acsAA) BL00550(ytcI) BL01993(acsAB)
            BLD: BLi02138 BLi03098(ytcI) BLi03119(acsA)
            BCL: ABC2760(acsA) ABC3255
            BAY: RBAM_026800
            BPU: BPUM_1779 BPUM_2616
            OIH: OB0022 OB2643
            GKA: GK1991 GK2759 GK2793 GK2806
            SAU: SA1554(acsA) SA2402
            SAV: SAV1733(acsA) SAV2609
            SAM: MW1676(acsA) MW2528
            SAR: SAR1811(acsA) SAR2687
            SAS: SAS1659 SAS2494
            SAC: SACOL1783(acs) SACOL2624
            SAB: SAB1593c(acsA) SAB2482c
            SAA: SAUSA300_1679(acsA) SAUSA300_2542
            SAO: SAOUHSC_01846 SAOUHSC_02929
            SEP: SE2161
            SER: SERP2172
            SHA: SH0436(acs) SH1189(acsA)
            SSP: SSP1030 SSP2389
            LMO: lmo2720
            LMF: LMOf2365_2700(acsA)
            LIN: lin2868
            LWE: lwe2672(acsA)
            LLM: llmg_0627(fadD)
            STH: STH1025 STH2321 STH881
            CHY: CHY_0249(acsA) CHY_0572 CHY_0659(acoE)
            DSY: DSY0515
            MTA: Moth_2170
            MTU: Rv3667(acs)
            MTC: MT3768(acs)
            MBO: Mb3691(acs)
            MBB: BCG_3725(acs)
            MPA: MAP0407c(acs)
            MAV: MAV_0462(acsA)
            MSM: MSMEG_0718 MSMEG_3986 MSMEG_6179
            MMC: Mmcs_4231 Mmcs_4809
            NFA: nfa12430 nfa17920 nfa24050
            RHA: RHA1_ro01619(acsA1) RHA1_ro04332(acsA2) RHA1_ro05006
                 RHA1_ro08189 RHA1_ro08877(acsA3) RHA1_ro08923 RHA1_ro10183
                 RHA1_ro11190
            SCO: SCO3563(acsA) SCO5983(StBAC16H6.18c) SCO6195(SC2G5.16)
            SMA: SAV2031(acsA4) SAV2307 SAV4599(acsA1)
            CMI: CMM_0922(acsA1) CMM_1788(acsA2)
            ART: Arth_0533
            AAU: AAur_1375(acsA) AAur_3353(acsA) AAur_pTC20189(acsA)
            PAC: PPA0909 PPA0910
            TFU: Tfu_2808 Tfu_2856
            FRA: Francci3_3663 Francci3_4026
            FAL: FRAAL0381(prpE) FRAAL5886(acs)
            SEN: SACE_0337(acsA) SACE_2375(acsA) SACE_2408 SACE_2851 SACE_3131
                 SACE_3902 SACE_4729(acsA)
            RXY: Rxyl_0856
            RBA: RB13264(acs)
            TDE: TDE0040
            LIL: LA1173 LA4254
            LIC: LIC12516 LIC13404(acsA)
            LBJ: LBJ_2938(acsA)
            LBL: LBL_0125(acsA)
            SYN: sll0542(acs)
            SYW: SYNW1013(acs)
            SYC: syc0203_c
            SYF: Synpcc7942_1352
            SYD: Syncc9605_1139
            SYE: Syncc9902_1318
            SYG: sync_1553(acsA)
            SYR: SynRCC307_1345(acsA)
            SYX: SynWH7803_1040(acsA)
            TEL: tll0887
            GVI: gll0159
            ANA: all4256 all4257
            AVA: Ava_1206
            PMA: Pro1041(acs)
            PMM: PMM0619(acs)
            PMT: PMT0389(acs)
            PMN: PMN2A_0057
            PMI: PMT9312_0619
            PMB: A9601_06751(acs)
            PMC: P9515_06841(acs)
            PMF: P9303_18991(acs)
            PMG: P9301_06451(acs)
            PMH: P9215_07011
            PME: NATL1_06781(acs)
            TER: Tery_2371
            BTH: BT_3755
            BFR: BF0528
            BFS: BF0476
            SRU: SRU_1684(acs) SRU_1820(acs)
            CHU: CHU_2429(acsA) CHU_2982(acs)
            GFO: GFO_1907(acsA)
            FPS: FP0942(acsA)
            CTE: CT1652(acs)
            CCH: Cag_1125 Cag_1685
            PLT: Plut_1637
            DET: DET1209(acs)
            DEH: cbdb_A1126(acs)
            DRA: DR_0460 DR_2471
            DGE: Dgeo_1750 Dgeo_1759 Dgeo_2396
            TTH: TTC0884 TTC0885 TTC0886 TTC0919
            TTJ: TTHA1248 TTHA1249 TTHA1250 TTHA1285
            AAE: aq_2103(acs') aq_2104(acs)
            MMP: MMP0148(acsA) MMP1274
            MAC: MA2912
            MBA: Mbar_A2172
            MMA: MM_3180
            MBU: Mbur_0608 Mbur_0999
            MHU: Mhun_0592 Mhun_1721
            MST: Msp_0266
            MSI: Msm_0330
            AFU: AF2389-N
            HAL: VNG0484G(acs1) VNG0997G(acs2)
            HMA: rrnAC0650(acs1) rrnAC1341(acs) rrnAC3228(acs5)
                 rrnAC3230(acs3) rrnB0217(acs2) rrnB0265(acs4)
            HWA: HQ1538A(acs)
            NPH: NP0164A(acs_5) NP4240A(acs_1) NP4242A(acs_2)
            TAC: Ta0229 Ta0421 Ta0769 Ta1508m
            TVO: TVN0122 TVN1150 TVN1266 TVN1268
            PTO: PTO0283 PTO0501 PTO0502 PTO0631
            RCI: RCIX1692(acs-1) RRC211(acs-2)
            APE: APE_1346.1 APE_2604(acs) APE_2604a.1(acsA)
            SSO: SSO1340(acsA-2) SSO1342(acsA-2) SSO1903(acsA-3)
                 SSO2041(acsA-5) SSO2059(acsA-6) SSO2070(acsA-7)
                 SSO2216(acsA-8) SSO2863(acsA-9) SSO3203(acsA-10)
            STO: ST0050 ST0730 ST0783 ST1190 ST1796 ST1803 ST2019 ST2139
                 ST2575
            SAI: Saci_0025 Saci_0306 Saci_1184 Saci_1774 Saci_2062(acs)
                 Saci_2235 Saci_2298(acsA)
            PAI: PAE2474 PAE2481 PAE2865 PAE2867
STRUCTURES  PDB: 1PG3  1PG4  1RY2  2P20  2P2B  2P2F  2P2J  2P2M  2P2Q  
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.1
            ExPASy - ENZYME nomenclature database: 6.2.1.1
            ExplorEnz - The Enzyme Database: 6.2.1.1
            ERGO genome analysis and discovery system: 6.2.1.1
            BRENDA, the Enzyme Database: 6.2.1.1
            CAS: 9012-31-1
///
ENTRY       EC 6.2.1.2                  Enzyme
NAME        butyrate---CoA ligase;
            butyryl-CoA synthetase;
            fatty acid thiokinase (medium chain);
            acyl-activating enzyme;
            fatty acid elongase;
            fatty acid activating enzyme;
            fatty acyl coenzyme A synthetase;
            medium chain acyl-CoA synthetase;
            butyryl-coenzyme A synthetase;
            L-(+)-3-hydroxybutyryl CoA ligase;
            short-chain acyl-CoA synthetase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     butanoate:CoA ligase (AMP-forming)
REACTION    ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
ALL_REAC    R00389 > R01176
SUBSTRATE   ATP [CPD:C00002];
            acid [CPD:C00174];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            acyl-CoA [CPD:C00040]
COMMENT     Acts on acids from C4 to C11 and on the corresponding 3-hydroxy- and
            2,3- or 3,4-unsaturated acids.
REFERENCE   1  [PMID:13084616]
  AUTHORS   MAHLER HR, WAKIL SJ, BOCK RM.
  TITLE     Studies on fatty acid oxidation. I. Enzymatic activation of fatty
            acids.
  JOURNAL   J. Biol. Chem. 204 (1953) 453-68.
  ORGANISM  cow [GN:bta], pig [GN:ssc], rat [GN:rno]
REFERENCE   2
  AUTHORS   Massaro, E.J. and Lennarz, W.J.
  TITLE     The partial purification and characterization of a bacterial fatty
            acyl coenzyme A synthetase.
  JOURNAL   Biochemistry 4 (1965) 85-90.
  ORGANISM  Bacillus megaterium
REFERENCE   3
  AUTHORS   Websterlt, J.R., Gerowin, L.D. and Rakita, L.
  TITLE     Purification and characteristics of a butyryl coenzyme A synthetase
            from bovine heart mitochondria.
  JOURNAL   J. Biol. Chem. 240 (1965) 29-33.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K01896  butyryl-CoA synthetase
GENES       HSA: 116285(ACSM1)
            MMU: 117147(Acsm1)
            BTA: 282576(BUCS1)
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.2
            ExPASy - ENZYME nomenclature database: 6.2.1.2
            ExplorEnz - The Enzyme Database: 6.2.1.2
            ERGO genome analysis and discovery system: 6.2.1.2
            BRENDA, the Enzyme Database: 6.2.1.2
            CAS: 9080-51-7
///
ENTRY       EC 6.2.1.3                  Enzyme
NAME        long-chain-fatty-acid---CoA ligase;
            acyl-CoA synthetase;
            fatty acid thiokinase (long chain);
            acyl-activating enzyme;
            palmitoyl-CoA synthase;
            lignoceroyl-CoA synthase;
            arachidonyl-CoA synthetase;
            acyl coenzyme A synthetase;
            acyl-CoA ligase;
            palmitoyl coenzyme A synthetase;
            thiokinase;
            palmitoyl-CoA ligase;
            acyl-coenzyme A ligase;
            fatty acid CoA ligase;
            long-chain fatty acyl coenzyme A synthetase;
            oleoyl-CoA synthetase;
            stearoyl-CoA synthetase;
            long chain fatty acyl-CoA synthetase;
            long-chain acyl CoA synthetase;
            fatty acid elongase;
            LCFA synthetase;
            pristanoyl-CoA synthetase;
            ACS3;
            long-chain acyl-CoA synthetase I;
            long-chain acyl-CoA synthetase II;
            fatty acyl-coenzyme A synthetase;
            long-chain acyl-coenzyme A synthetase;
            FAA1
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     acid:CoA ligase (AMP-forming)
REACTION    ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an
            acyl-CoA [RN:R00390]
ALL_REAC    R00390 > R01280
SUBSTRATE   ATP [CPD:C00002];
            long-chain carboxylic acid [CPD:C00347];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            acyl-CoA [CPD:C00040]
COFACTOR    Magnesium [CPD:C00305]
COMMENT     Acts on a wide range of long-chain saturated and unsaturated fatty
            acids, but the enzymes from different tissues show some variation in
            specificity. The liver enzyme acts on acids from C6 to C20; that
            from brain shows high activity up to C24.
REFERENCE   1  [PMID:2528345]
  AUTHORS   Bakken AM, Farstad M.
  TITLE     Identical subcellular distribution of palmitoyl-CoA and
            arachidonoyl-CoA synthetase activities in human blood platelets.
  JOURNAL   Biochem. J. 261 (1989) 71-6.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:108099]
  AUTHORS   Hosaka K, Mishina M, Tanaka T, Kamiryo T, Numa S.
  TITLE     Acyl-coenzyme-A synthetase I from Candida lipolytica. Purification,
            properties and immunochemical studies.
  JOURNAL   Eur. J. Biochem. 93 (1979) 197-203.
  ORGANISM  Candida lipolytica
REFERENCE   3  [PMID:3161545]
  AUTHORS   Nagamatsu K, Soeda S, Mori M, Kishimoto Y.
  TITLE     Lignoceroyl-coenzyme A synthetase from developing rat brain: partial
            purification, characterization and comparison with
            palmitoyl-coenzyme A synthetase activity and liver enzyme.
  JOURNAL   Biochim. Biophys. Acta. 836 (1985) 80-8.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:467438]
  AUTHORS   Tanaka T, Hosaka K, Hoshimaru M, Numa S.
  TITLE     Purification and properties of long-chain acyl-coenzyme-A synthetase
            from rat liver.
  JOURNAL   Eur. J. Biochem. 98 (1979) 165-72.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00071  Fatty acid metabolism
            PATH: map03320  PPAR signaling pathway
            PATH: map04920  Adipocytokine signaling pathway
ORTHOLOGY   KO: K01897  long-chain fatty-acid-CoA ligase
            KO: K08746  solute carrier family 27 (fatty acid transporter),
                        member 2
GENES       HSA: 11001(SLC27A2) 2180(ACSL1) 2181(ACSL3) 2182(ACSL4)
                 23305(ACSL6) 51703(ACSL5)
            PTR: 450739(ACSL5) 453423(SLC27A2) 461631(ACSL1)
            MMU: 14081(Acsl1) 216739(Acsl6) 26458(Slc27a2) 433256(Acsl5)
                 50790(Acsl4) 74205(Acsl3)
            RNO: 113976(Acsl4) 114024(Acsl3) 117243(Acsl6) 25288(Acsl1)
                 65192(Slc27a2) 94340(Acsl5)
            CFA: 474670(ACSL6) 475631(ACSL1) 477820(ACSL5) 478298(SLC27A2)
                 481018(ACSL4)
            BTA: 535727(LOC535727) 537161(MGC139933)
            SSC: 448980(ACSL4)
            GGA: 422345(ACSL4) 422547(ACSL1) 423896(RCJMB04_26g6)
                 424810(ACSL3)
            XLA: 379352(MGC53832) 380135(facl2)
            XTR: 448565(acsl6) 496479(LOC496479) 496813(slc27a6)
            DRE: 393622(acsl4)
            SPU: 575511(LOC575511) 581020(LOC581020) 590937(LOC590937)
                 592091(LOC592091)
            DME: Dmel_CG12512 Dmel_CG4500 Dmel_CG4501(bgm)
            CEL: C46F4.2(acs-17) F28F8.2(acs-2) F37C12.7 F47G6.2 R07C3.4
                 R09E10.3 R09E10.4 T08B1.6 Y65B4BL.5 Y76A2B.3
            ATH: AT1G49430(LACS2) AT1G64400 AT1G77590(LACS9) AT3G05970(LACS6)
                 AT4G11030 AT4G14070(AAE15) AT4G23850 AT5G27600(LACS7)
            OSA: 4324180 4324393 4334764 4338395 4340187 4350728 4351483
                 4351610
            CME: CME186C CML197C CMT459C
            SCE: YER015W(FAA2) YIL009W(FAA3) YMR246W(FAA4) YOR317W(FAA1)
            AGO: AGOS_ABL018C AGOS_ADR052W
            PIC: PICST_35069(FAA23) PICST_55002(FAA24) PICST_65071(FAA4)
                 PICST_89450(FAA22)
            CGR: CAGL0H09460g CAGL0I09878g CAGL0K07293g
            SPO: SPBC18H10.02 SPBP4H10.11c
            ANI: AN0609.2 AN6014.2 AN8280.2
            AFM: AFUA_1G17190 AFUA_2G09910 AFUA_4G06850 AFUA_5G04270
                 AFUA_5G07410 AFUA_5G08470
            AOR: AO090011000642 AO090023000529 AO090038000487 AO090102000633
            CNE: CNC00660 CNI00710
            UMA: UM04803.1 UM05450.1
            ECU: ECU10_0890 ECU10_0910
            DDI: DDB_0191105(fcsA)
            PFA: MAL3P8.9 PF07_0129 PF14_0751 PF14_0761 PFB0685c PFB0695c
                 PFD0085c PFE1250w PFF0945c PFL0035c PFL1880w PFL2570w
            CPV: cgd3_640 cgd4_3400 cgd5_3200
            CHO: Chro.30084 Chro.50052
            TAN: TA15995 TA18970 TA20445
            TPV: TP01_0119 TP01_0520 TP02_0107
            TET: TTHERM_00052710 TTHERM_00083310 TTHERM_00083320
                 TTHERM_00113020 TTHERM_00187190 TTHERM_00187210
                 TTHERM_00187230 TTHERM_00187270 TTHERM_00349120
                 TTHERM_00382380 TTHERM_00678360 TTHERM_00790570
                 TTHERM_00822110 TTHERM_01066950 TTHERM_01124100
                 TTHERM_01250050
            TBR: Tb09.160.2770 Tb09.160.2780 Tb09.160.2810 Tb09.160.2840
                 Tb10.70.4200 Tb11.02.2070
            TCR: 504089.40 504177.10 504177.20 506261.10 506829.100 510151.10
                 511581.10
            LMA: LmjF01.0470 LmjF01.0490 LmjF01.0500 LmjF01.0520 LmjF03.0230
                 LmjF13.0420
            EHI: 1.t00121 100.t00014 112.t00006 112.t00020 13.t00014 13.t00069
                 183.t00002 249.t00010 276.t00003 301.t00003 37.t00042
                 505.t00002 66.t00028
            ECO: b1805(fadD)
            ECJ: JW1794(fadD)
            ECE: Z2848(fadD)
            ECS: ECs2514
            ECC: c2209(fadD)
            ECI: UTI89_C1999(fadD) UTI89_C2907(yfiQ)
            ECP: ECP_1748
            ECV: APECO1_863(fadD)
            ECW: EcE24377A_2031(fadD)
            STY: STY1948(fadD)
            STT: t1059(fadD)
            SPT: SPA1055(fadD)
            SEC: SC1811(fadD)
            STM: STM1818(fadD)
            YPE: YPO0537 YPO2074(fadD)
            YPK: y2236(fadD) y3641
            YPM: YP_1917(fadD) YP_3645(fAA1)
            YPA: YPA_1457 YPA_3561
            YPN: YPN_0406 YPN_1551
            YPP: YPDSF_1047
            YPS: YPTB0674 YPTB2057(fadD)
            YPI: YpsIP31758_2014(fadD)
            SFL: SF1423(fadD)
            SFX: S1538(fadD)
            SFV: SFV_1424(fadD)
            SSN: SSON_1356(fadD)
            SBO: SBO_1283(fadD) SBO_1285(yeaX)
            SDY: SDY_1709(fadD)
            ECA: ECA2372(fadD) ECA3830
            PLU: plu2134(fadD) plu3671(fadD)
            HIN: HI0002 HI0390.1(fadD)
            HIT: NTHI0002 NTHI0510(lcfA)
            HIP: CGSHiEE_01075
            HIQ: CGSHiGG_05135
            HSO: HS_0735(fadD)
            PMU: PM0707(fadD_1) PM0925(fadD_2)
            MSU: MS1358(caiC) MS2265(fAA1)
            APL: APL_0397(lcfA) APL_1413
            XFA: XF0287
            XFT: PD0233(rpfB)
            XCC: XCC1858(rpfB)
            XCB: XC_2331
            XCV: XCV1921(rpfB)
            XAC: XAC1880(rpfB)
            XOO: XOO2868(rpfB)
            XOM: XOO_2722(XOO2722)
            VCH: VC1985 VC2484
            VCO: VC0395_A1570(fadD)
            VVU: VV1_0136 VV1_0649
            VVY: VV0494 VV1053
            VPA: VP0351 VP0870 VP1964 VPA1152
            VFI: VF0533 VF1708 VF2256 VF2264
            PPR: PBPRA0424 PBPRA1075(fadD) PBPRA1287
            PAE: PA2557 PA3299(fadD1) PA3300(fadD2) PA3860
            PAU: PA14_14060 PA14_21340(fadD2) PA14_21370(fadD1) PA14_31470
            PPU: PP_3458 PP_4063 PP_4549(fadD) PP_4550(fadD2)
            PST: PSPTO_4097(fadD-1) PSPTO_4098(fadD-2)
            PSB: Psyr_3834 Psyr_3836
            PSP: PSPPH_1426(fadD1) PSPPH_1427(fadD2)
            PFL: PFL_1472(fadD-6) PFL_2943(fadD-2) PFL_3028(fadD-2) PFL_3528
                 PFL_3935(fadD35) PFL_4598(fadD-2) PFL_4599(fadD-2)
            PFO: Pfl_3655 Pfl_4353 Pfl_4354
            PEN: PSEEN2544 PSEEN2973 PSEEN3384 PSEEN3973(fadD)
                 PSEEN3975(fadD2)
            PAR: Psyc_0308 Psyc_1866 Psyc_1867(fadD)
            PCR: Pcryo_0339
            ACI: ACIAD0235(fadD) ACIAD1572 ACIAD1724(hcaC) ACIAD2106
            SON: SO_0075 SO_1971 SO_2581(fadD-1) SO_3664(fadD-2)
            SDN: Sden_0072 Sden_1625 Sden_2934
            SFR: Sfri_1733 Sfri_2503 Sfri_3973
            SAZ: Sama_1934
            SBL: Sbal_1864
            SLO: Shew_2188
            SHE: Shewmr4_0078 Shewmr4_2177 Shewmr4_2285
            SHM: Shewmr7_0076 Shewmr7_2254 Shewmr7_2357
            SHN: Shewana3_0080 Shewana3_2386 Shewana3_2475 Shewana3_3231
            SHW: Sputw3181_2264
            ILO: IL1827(fadD)
            CPS: CPS_1189(fadD1) CPS_3416 CPS_3427(fadD2)
            PHA: PSHAa1394 PSHAa2132 PSHAa2134 PSHAb0502(fadD)
            PAT: Patl_0154 Patl_0322 Patl_1368 Patl_2804
            SDE: Sde_1886
            MAQ: Maqu_1593
            LPN: lpg1127 lpg1554(fadD-1) lpg2230
            LPF: lpl1133 lpl1472(fadD) lpl2155
            LPP: lpp1128 lpp1511(fadD) lpp2182
            MCA: MCA1569
            FTU: FTT1254(fadD1) FTT1528(fadD2)
            FTF: FTF1254(fadD1) FTF1528(fadD2)
            FTL: FTL_0586 FTL_0690
            FTH: FTH_0586(fadD1) FTH_0692(caiC) FTH_1238(fadD2)
            FTA: FTA_0728
            FTN: FTN_1273 FTN_1436(fadD)
            NOC: Noc_0825 Noc_2380
            AEH: Mlg_2127
            HCH: HCH_02646 HCH_04890
            CSA: Csal_1468
            ABO: ABO_0184(fadB)
            AHA: AHA_0722 AHA_2204
            DNO: DNO_1002
            NME: NMB1276 NMB1555
            NMA: NMA1482 NMA1743(fadD)
            NMC: NMC1472(fadD)
            NGO: NGO0530 NGO1213
            CVI: CV_0093(fadD1) CV_1459(fadD2) CV_1780 CV_3676 CV_4051
            RSO: RSc0442(RS04463) RSc0780(fadD2) RSc2857(fadD1)
            REU: Reut_A0260 Reut_A0823 Reut_A1467 Reut_A1547 Reut_A2994
                 Reut_A2996 Reut_A3057 Reut_B3549 Reut_B3565 Reut_B3605
                 Reut_B4042 Reut_B4155 Reut_B4758 Reut_B5576 Reut_C6056
                 Reut_C6065 Reut_C6185 Reut_D6480
            REH: H16_A0285 H16_A2076 H16_A2150 H16_A2748 H16_A2947
                 H16_A3288(fadD3) H16_A3351 H16_A3514 H16_B0753 H16_B1239
                 H16_B1736
            RME: Rmet_0214 Rmet_0610 Rmet_1744 Rmet_2525 Rmet_2635 Rmet_3148
                 Rmet_3215 Rmet_4068 Rmet_4454 Rmet_4502 Rmet_4746 Rmet_5140
                 Rmet_5528 Rmet_5827
            BMA: BMA1134 BMA1276(fadD) BMA2959 BMA2967(fcs)
            BMV: BMASAVP1_A1764(fadD) BMASAVP1_A3343(fcs)
            BML: BMA10299_A0131(fadD) BMA10299_A1574(fcs)
            BMN: BMA10247_1035(fadD) BMA10247_3028(fcs)
            BXE: Bxe_A0042 Bxe_A0474 Bxe_A2746 Bxe_A2778 Bxe_B0702 Bxe_B1513
                 Bxe_B2539 Bxe_C0318 Bxe_C0707 Bxe_C0867
            BUR: Bcep18194_A3633 Bcep18194_A4674 Bcep18194_B0052
                 Bcep18194_C6801 Bcep18194_C6813
            BCH: Bcen2424_1534 Bcen2424_3256 Bcen2424_6272
            BAM: Bamb_0451 Bamb_1416
            BPS: BPSL1734 BPSL1883 BPSL3037(fadD) BPSL3387 BPSL3394
            BPM: BURPS1710b_0163(fcs) BURPS1710b_0176 BURPS1710b_1957
                 BURPS1710b_2138 BURPS1710b_2456(alkK) BURPS1710b_3556
                 BURPS1710b_A1154 BURPS1710b_A2363(fcs)
            BPL: BURPS1106A_1803(fadD)
            BPD: BURPS668_1782(fadD)
            BTE: BTH_I1106 BTH_I2376 BTH_I2529 BTH_I3299 BTH_I3306 BTH_II1795
            BPE: BP0532 BP1099 BP2811(fadD)
            BPA: BPP0229 BPP0915 BPP2042 BPP2338(fadD) BPP3729(fadD2)
            BBR: BB0233 BB1125 BB1789(fadD) BB2290 BB4175(fadD2)
            RFR: Rfer_2283 Rfer_3503 Rfer_3542 Rfer_3752 Rfer_3775 Rfer_3833
                 Rfer_3898 Rfer_4067
            POL: Bpro_0604 Bpro_3469 Bpro_3837 Bpro_4161 Bpro_4543
            MPT: Mpe_A0344 Mpe_A0353 Mpe_A0894 Mpe_A1011 Mpe_A2687 Mpe_A3572
            HAR: HEAR0221(fadD)
            MMS: mma_0275(fadD)
            NEU: NE1549 NE2235
            NET: Neut_0702
            NMU: Nmul_A0095 Nmul_A1417
            EBA: ebA4661 ebA4749 ebA5317 ebA6829(yfiQ)
            AZO: azo1033(fadD1) azo2499(fadD2) azo3066(fadD3) azo3246(fadD4)
            DAR: Daro_0249 Daro_1553 Daro_2355 Daro_2718 Daro_3240
            TBD: Tbd_2597
            WSU: WS0237
            CCV: CCV52592_0160(fadD)
            CCO: CCC13826_0279(fadD)
            ABU: Abu_1925
            NIS: NIS_0535
            GSU: GSU1103
            GME: Gmet_1469 Gmet_2692
            PCA: Pcar_1241 Pcar_1619 Pcar_1963
            DVU: DVU1453(fadD) DVU3065
            DDE: Dde_0193 Dde_0557 Dde_1725
            BBA: Bd0279 Bd1803(fadD) Bd3149
            DPS: DP0555 DP1202 DP1333
            ADE: Adeh_2359 Adeh_2886
            SAT: SYN_02640 SYN_02643 SYN_03128
            SFU: Sfum_0108
            PUB: SAR11_0422(faa1)
            MLO: mll5415 mlr6932
            MES: Meso_0069
            SME: SMc02162(fadD)
            ATU: Atu0405(fadD)
            ATC: AGR_C_713
            RET: RHE_CH00478(fadD) RHE_CH00921(matB) RHE_PF00013(ypf00005)
            RLE: RL0505(fadD) RL0991(matB) pRL120368
            BME: BMEI1632
            BMF: BAB1_0320(fadD)
            BMS: BR0289(fadD)
            BMB: BruAb1_0315(fadD)
            BOV: BOV_0303(fadD)
            BJA: bll0994 bll1319(fadD) bll5697 bll7293 bll7820 bll7864 bll7928
                 blr1046 blr1288 blr2951 blr3329 blr5963 blr7807
            BRA: BRADO0596 BRADO0982 BRADO1099(fadD) BRADO5264 BRADO6564
                 BRADO6584(fadD)
            BBT: BBta_0779 BBta_0952(fadD) BBta_0972 BBta_5153 BBta_5715
                 BBta_6949(fadD) BBta_7073 BBta_7585
            RPA: RPA0458 RPA0464 RPA1234 RPA1242(fadD1) RPA1449 RPA1763
                 RPA1766 RPA3299 RPA3465 RPA3657(fadD2) RPA3716(pimA) RPA4042
                 RPA4267 RPA4823
            RPB: RPB_0229 RPB_0580 RPB_1344 RPB_1560 RPB_1747 RPB_3597
                 RPB_4080 RPB_4700
            RPC: RPC_0861 RPC_1049 RPC_2227 RPC_3202 RPC_4074 RPC_4176
            RPD: RPD_0252 RPD_1323 RPD_1569 RPD_3552
            RPE: RPE_0847 RPE_1707 RPE_1783 RPE_2253 RPE_2373 RPE_3779
                 RPE_4227 RPE_4911
            NWI: Nwi_2684
            NHA: Nham_3734
            CCR: CC_0944 CC_0966 CC_1321
            SIL: SPO1847 SPO2528 SPO3003 SPO3296
            SIT: TM1040_0113 TM1040_1827 TM1040_2789 TM1040_3271
            RSP: RSP_1041 RSP_2255 RSP_2279
            JAN: Jann_3119
            RDE: RD1_0546(fadD) RD1_0702 RD1_1106 RD1_1474 RD1_1974(lcfA)
                 RD1_2849 RD1_2917
            ZMO: ZMO0704
            SAL: Sala_0169
            ELI: ELI_13210
            RRU: Rru_A1312 Rru_A2191 Rru_A3509
            MAG: amb3589
            MGM: Mmc1_3555
            ABA: Acid345_2081 Acid345_2858
            BSU: BG11946(lcfA) BG13057(yhfL) BG13064(yhfT) BG13460(yngI)
            BHA: BH1131 BH2006 BH3103 BH3104
            BAN: BA0876 BA1091 BA3688 BA4763(fadD)
            BAR: GBAA0876 GBAA1091 GBAA3688 GBAA4763(fadD)
            BAA: BA_1642 BA_5193
            BAT: BAS0832 BAS1019 BAS3419 BAS4422
            BCE: BC0890 BC1088 BC3419 BC3628 BC4526
            BCA: BCE_0965 BCE_1193 BCE_3436 BCE_3647 BCE_4653(fadD)
            BCZ: BCZK0779(fadD) BCZK1006(fadD) BCZK2688(fadD) BCZK3330(fadD)
                 BCZK4273(lcfA)
            BTK: BT9727_0778(fadD) BT9727_1003(fadD) BT9727_3380(fadD)
                 BT9727_4261(lcfA)
            BTL: BALH_0790(fadD) BALH_0970(fadD) BALH_1755 BALH_3074
                 BALH_3263(fadD) BALH_4110(lcfA)
            BLI: BL00331(lcfA) BL01080 BL01325(yngIA) BL01987(yngI)
            BLD: BLi01103(yhfL) BLi01148 BLi02144(yngI) BLi03003(lcfA)
            BCL: ABC0344 ABC0589 ABC2673(lcfA) ABC3618
            BAY: RBAM_025620(lcfA)
            BPU: BPUM_0239(ydaB) BPUM_0969(lcfA1) BPUM_1785(yngI)
                 BPUM_2513(lcfA2)
            OIH: OB0669 OB1058 OB1176 OB2122 OB2217
            GKA: GK0668 GK1491 GK1505 GK2690 GK2782
            SAU: SA0226
            SAV: SAV0234
            SAM: MW0210
            SAR: SAR0226(fadE)
            SAS: SAS0210
            SAC: SACOL0214
            SAB: SAB0173c SAB0525
            SAO: SAOUHSC_00198
            SSP: SSP2426
            LWE: lwe0311(fadD)
            LLM: llmg_1965
            SPZ: M5005_Spy_0433
            SPH: MGAS10270_Spy0434
            SPI: MGAS10750_Spy0453
            SPJ: MGAS2096_Spy0452
            SPK: MGAS9429_Spy0432
            SPA: M6_Spy0467
            SPB: M28_Spy0421
            STH: STH619 STH704
            CKL: CKL_3026(fadD)
            CHY: CHY_0437(fadD1) CHY_0845(fadD2) CHY_1731(fadD3)
                 CHY_1735(fadD4) CHY_2411(fadD5)
            DSY: DSY0943 DSY2317 DSY2479 DSY3791 DSY4298
            MTA: Moth_0503
            MTU: Rv1521(fadD25) Rv2187(fadD15)
            MTC: MT0224 MT0417 MT1572 MT2242 MT2580 MT3666
            MBO: Mb0220(fadD4) Mb0411(fadD30) Mb1548(fadD25) Mb2209
                 Mb2210(fadD15) Mb2533c(fadD35) Mb3591(fadD3)
            MBB: BCG_2203(fadD15)
            MLE: ML0887
            MPA: MAP0506c(fadD3_1) MAP1925(fadD15) MAP3601(fadD5)
                 MAP3649(fadD4)
            MSM: MSMEG_4254
            MMC: Mmcs_3282
            CGL: NCgl0279(cgl0284) NCgl0388(cgl0400) NCgl2216(cgl2296)
            CGB: cg0341(fadD1) cg0480(fadD5) cg1353(fadD4) cg2521(fadD15)
                 cg3179(fadD2)
            CEF: CE0421 CE2195
            CDI: DIP0387 DIP1725
            CJK: jk0597(fadD3) jk1915(fadD6) jk2042(fadD7)
            NFA: nfa30980 nfa41500 nfa47040 nfa4830 nfa5250
            RHA: RHA1_ro00141 RHA1_ro00367 RHA1_ro01121 RHA1_ro01496
                 RHA1_ro01533 RHA1_ro01899 RHA1_ro02071 RHA1_ro02284
                 RHA1_ro02306 RHA1_ro02704 RHA1_ro02708 RHA1_ro02781
                 RHA1_ro03009 RHA1_ro03747 RHA1_ro03779 RHA1_ro04492
                 RHA1_ro06034 RHA1_ro06103 RHA1_ro06989 RHA1_ro08945
                 RHA1_ro10229 RHA1_ro10297 RHA1_ro10402 RHA1_ro11168
            SCO: SCO2131(SC6G10.04) SCO2720(SCC46.05c) SCO6196(SC2G5.17)
                 SCO6552(SC4B5.02c) SCO6968(SC6F7.21)
            SMA: SAV1259(fadD6) SAV1603(fadD7) SAV1848(fadD8) SAV2030
                 SAV377(fadD1) SAV3806(fadD16) SAV4818(fadD10) SAV5562(fadD12)
                 SAV605(fadD2) SAV6069(fadD14) SAV6612(fadD15)
            LXX: Lxx15440(fadD)
            CMI: CMM_2418(fadD)
            PAC: PPA1632 PPA1724 PPA2234
            TFU: Tfu_1031 Tfu_1998 Tfu_2158
            FRA: Francci3_2046 Francci3_2245 Francci3_3097
            FAL: FRAAL2616 FRAAL3190 FRAAL3453 FRAAL5098
            SEN: SACE_0578 SACE_1193(fadD) SACE_1694 SACE_2795 SACE_3153
                 SACE_3444 SACE_3447 SACE_3478 SACE_4038(fadD) SACE_5393
            BLO: BL0266(fadD1) BL0858(fadD2) BL1501(fadD3) BL1748(fadD4)
            BAD: BAD_0724(fadD2) BAD_0774(fadD4) BAD_0779(fadD3)
                 BAD_1409(fadD1)
            FNU: FN0867 FN1122
            RBA: RB8524(lcfA)
            BGA: BG0139 BG0606
            BAF: BAPKO_0139 BAPKO_0624
            TPA: TP0145
            TDE: TDE1742
            LIL: LA0106 LA2177 LA2309 LB093(fadD)
            LIC: LIC10094 LIC11630(fadD) LIC11747(ydiD) LIC20074
            LBJ: LBJ_0086 LBJ_1312
            LBL: LBL_0050 LBL_1537
            SYN: slr1609
            SYW: SYNW0669(fadD)
            SYC: syc0624_c(fadD)
            SYF: Synpcc7942_0918
            SYD: Syncc9605_2011
            SYE: Syncc9902_0660
            SYG: sync_0608(fadD-1)
            SYR: SynRCC307_1796(fadD)
            SYX: SynWH7803_0580(fadD)
            CYA: CYA_0133
            CYB: CYB_2181
            TEL: tll1301
            GVI: gll1950 glr0435 glr1146
            ANA: alr3602
            AVA: Ava_3173 Ava_4108
            PMA: Pro0399(fAA1)
            PMM: PMM0402(fadD)
            PMT: PMT0215(fadD)
            PMN: PMN2A_1737
            PMI: PMT9312_0398
            PMB: A9601_04531(fadD)
            PMC: P9515_04641(fadD)
            PMF: P9303_21391(fadD)
            PMG: P9301_04221(fadD)
            PME: NATL1_04541(fadD)
            BTH: BT_2154 BT_2782 BT_3550
            BFR: BF0373 BF3857 BF4466
            BFS: BF0320 BF3628
            PGI: PG1145
            SRU: SRU_1209(fadD) SRU_2380
            CHU: CHU_3595(fadD)
            GFO: GFO_1049(fadD)
            FPS: FP1720(fadD)
            CTE: CT0046(fadD) CT1156
            CCH: Cag_1135
            PLT: Plut_0972 Plut_2064
            DET: DET0946 DET1033
            DEH: cbdb_A1006 cbdb_A901
            DRA: DR_1692 DR_A0264(fadD-3) DR_A0309
            DGE: Dgeo_1070 Dgeo_2519
            TTH: TTC0079 TTC0217 TTC1065 TTC1099
            TTJ: TTHA0448 TTHA0586 TTHA1430 TTHA1463
            AAE: aq_999(fadD)
            MMP: MMP0566
            MAC: MA1422
            MBA: Mbar_A2821
            MMA: MM_0614 MM_2392
            MBU: Mbur_0663
            MHU: Mhun_2450
            MSI: Msm_0025
            HAL: VNG1073G(lfl1) VNG1339C VNG2071G(lfl2)
            HMA: rrnAC1074(fadD3)
            HWA: HQ1699A(alkK)
            NPH: NP2626A(alkK_1) NP3386A(alkK_4) NP3422A(alkK_3)
                 NP4150A(alkK_5) NP4174A(lfl) NP4256A(alkK_2)
            RCI: RRC116(fadD)
            APE: APE_1307 APE_1310 APE_2284.1
            SSO: SSO0369(fadD-1) SSO2523(fadD-2) SSO3064(fadD-3)
            STO: ST1112 ST1388
            SAI: Saci_1966(fadD) Saci_2148(fadD) Saci_2207
            PAI: PAE1379 PAE2466
STRUCTURES  PDB: 1ULT  1V25  1V26  
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.3
            ExPASy - ENZYME nomenclature database: 6.2.1.3
            ExplorEnz - The Enzyme Database: 6.2.1.3
            ERGO genome analysis and discovery system: 6.2.1.3
            UM-BBD (Biocatalysis/Biodegradation Database): 6.2.1.3
            BRENDA, the Enzyme Database: 6.2.1.3
            CAS: 9013-18-7
///
ENTRY       EC 6.2.1.4                  Enzyme
NAME        succinate---CoA ligase (GDP-forming);
            succinyl-CoA synthetase (GDP-forming);
            succinyl coenzyme A synthetase (guanosine diphosphate-forming);
            succinate thiokinase;
            succinic thiokinase;
            succinyl coenzyme A synthetase;
            succinate-phosphorylating enzyme;
            P-enzyme;
            SCS;
            G-STK;
            succinyl coenzyme A synthetase (GDP-forming);
            succinyl CoA synthetase;
            succinyl coenzyme A synthetase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     succinate:CoA ligase (GDP-forming)
REACTION    GTP + succinate + CoA = GDP + phosphate + succinyl-CoA [RN:R00432]
ALL_REAC    R00432;
            (other) R00727 R02405 R02406
SUBSTRATE   GTP [CPD:C00044];
            succinate [CPD:C00042];
            CoA [CPD:C00010]
PRODUCT     GDP [CPD:C00035];
            phosphate [CPD:C00009];
            succinyl-CoA [CPD:C00091]
COMMENT     Itaconate can act instead of succinate, and ITP instead of GTP.
REFERENCE   1
  AUTHORS   Hager, L.P.
  TITLE     Succinyl CoA synthetase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 6, Academic Press, New York, 1962, p. 387-399.
REFERENCE   2
  AUTHORS   Kaufman, S., Gilvarg, C., Cori, O. and Ochoa, S.
  TITLE     Enzymatic oxidation of alpha-ketoglutarate and coupled
            phosphorylation.
  JOURNAL   J. Biol. Chem. 203 (1953) 869-888.
  ORGANISM  pig [GN:ssc]
REFERENCE   3
  AUTHORS   Mazumder, R., Sanadi, D.R. and Rodwell, W.V.
  TITLE     Purification and properties of hog kidney succinic thiokinase.
  JOURNAL   J. Biol. Chem. 235 (1960) 2546-2550.
  ORGANISM  pig [GN:ssc]
REFERENCE   4  [PMID:13181903]
  AUTHORS   SANADI DR, GIBSON M, AYENGAR P.
  TITLE     Guanosine triphosphate, the primary product of phosphorylation
            coupled to the breakdown of succinyl coenzyme A.
  JOURNAL   Biochim. Biophys. Acta. 14 (1954) 434-6.
  ORGANISM  pig [GN:ssc], cow [GN:bta]
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K01898  succinate--CoA ligase (GDP-forming)
            KO: K01899  succinate--CoA ligase (GDP-forming) alpha chain
            KO: K01900  succinate--CoA ligase (GDP-forming) beta chain
GENES       HSA: 283398(LOC283398) 8801(SUCLG2) 8802(SUCLG1)
            MMU: 20917(Suclg2) 56451(Suclg1)
            RNO: 114597(Suclg1)
            CFA: 475775(SUCLG1) 476562(SUCLG2)
            SSC: 399539(SUCLG1)
            GGA: 416087(SUCLG2) 422932(RCJMB04_7e3)
            XLA: 494796(LOC494796)
            SPU: 581456(LOC581456)
            DME: Dmel_CG10622(Sucb) Dmel_CG1065(Scsalpha) Dmel_CG6255
            CEL: C05G5.4 C50F7.4 F23H11.3
            ATH: AT2G20420 AT5G08300 AT5G23250
            OSA: 4330016 4343710
            CME: CMH132C CMT209C
            SCE: YGR244C(LSC2)
            AGO: AGOS_AEL211W AGOS_AFR134C
            PIC: PICST_69303(LSC1)
            SPO: SPAC16E8.17c SPCC1620.08
            ANI: AN2295.2
            AFM: AFUA_1G10830 AFUA_4G00290 AFUA_5G06130
            AOR: AO090009000644
            CNE: CNG02080
            UMA: UM01672.1
            DDI: DDB_0191520(scsA) DDB_0231358(scsB)
            PFA: PF11_0097
            TAN: TA10625
            TPV: TP04_0660
            TET: TTHERM_00068140 TTHERM_00535260
            TBR: Tb927.3.2230
            TCR: 507681.20 507767.10 508479.340
            LMA: LmjF25.2130 LmjF25.2140
            SAI: Saci_1266
STRUCTURES  PDB: 1EUC  1EUD  2FP4  2FPG  2FPI  2FPP  
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.4
            ExPASy - ENZYME nomenclature database: 6.2.1.4
            ExplorEnz - The Enzyme Database: 6.2.1.4
            ERGO genome analysis and discovery system: 6.2.1.4
            BRENDA, the Enzyme Database: 6.2.1.4
            CAS: 9014-36-2
///
ENTRY       EC 6.2.1.5                  Enzyme
NAME        succinate---CoA ligase (ADP-forming);
            succinyl-CoA synthetase (ADP-forming);
            succinic thiokinase;
            succinate thiokinase;
            succinyl-CoA synthetase;
            succinyl coenzyme A synthetase (adenosine diphosphate-forming);
            succinyl coenzyme A synthetase;
            A-STK (adenin nucleotide-linked succinate thiokinase);
            STK;
            A-SCS
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     succinate:CoA ligase (ADP-forming)
REACTION    ATP + succinate + CoA = ADP + phosphate + succinyl-CoA [RN:R00405]
ALL_REAC    R00405;
            (other) R02404
SUBSTRATE   ATP [CPD:C00002];
            succinate [CPD:C00042];
            CoA [CPD:C00010]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            succinyl-CoA [CPD:C00091]
REFERENCE   1
  AUTHORS   Hager, L.P.
  TITLE     Succinyl CoA synthetase.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 6, Academic Press, New York, 1962, p. 387-399.
REFERENCE   2
  AUTHORS   Kaufman, S.
  TITLE     Studies on the mechanism of the reaction catalyzed by the
            phosphorylating enzyme.
  JOURNAL   J. Biol. Chem. 216 (1955) 153-164.
  ORGANISM  spinach
REFERENCE   3
  AUTHORS   Kaufman, S. and Alivasatos, S.G.A.
  TITLE     Purification and properties of the phosphorylating enzyme from
            spinach.
  JOURNAL   J. Biol. Chem. 216 (1955) 141-152.
  ORGANISM  spinach
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00640  Propanoate metabolism
            PATH: map00660  C5-Branched dibasic acid metabolism
            PATH: map00720  Reductive carboxylate cycle (CO2 fixation)
ORTHOLOGY   KO: K01901  succinyl-CoA synthetase
            KO: K01902  succinyl-CoA synthetase alpha chain
            KO: K01903  succinyl-CoA synthetase beta chain
GENES       HSA: 8803(SUCLA2)
            PTR: 452711(SUCLA2)
            MMU: 20916(Sucla2)
            CFA: 485448(SUCLA2)
            XLA: 447333(MGC82958)
            XTR: 394842(sucla2)
            SPU: 581673(LOC581673)
            DME: Dmel_CG11963
            CEL: F47B10.1
            SCE: YOR142W(LSC1)
            PIC: PICST_66961(LSC2)
            CGR: CAGL0F08107g CAGL0I07139g
            ANI: AN7000.2
            AFM: AFUA_4G04520
            AOR: AO090023000354 AO090206000040
            UMA: UM00368.1
            DDI: DDB_0231357(scsC)
            PFA: PF14_0295
            TAN: TA02815
            TPV: TP01_0677
            TET: TTHERM_00079540 TTHERM_00437600
            TBR: Tb10.6k15.3250
            TCR: 507681.20 507767.10
            LMA: LmjF36.2950
            ECO: b0728(sucC) b0729(sucD)
            ECJ: JW0717(sucC) JW0718(sucD)
            ECE: Z0882(sucC) Z0883(sucD)
            ECS: ECs0753 ECs0754
            ECC: c0805(sucC) c0806(sucD) c5036 c5037
            ECI: UTI89_C0723(sucC) UTI89_C0724(sucD) UTI89_C4634 UTI89_C4635
            ECP: ECP_0739 ECP_0740 ECP_4277 ECP_4278
            ECV: APECO1_1350(sucD) APECO1_1351(sucC) APECO1_2406
                 APECO1_2407(sucC)
            ECW: EcE24377A_0754(sucC) EcE24377A_0755(sucD)
            ECX: EcHS_A0775(sucC) EcHS_A0776(sucD)
            STY: STY0781(sucC) STY0782(sucD)
            STT: t2137(sucD) t2138(sucC)
            SPT: SPA2004(sucD) SPA2005(sucC)
            SEC: SC0742(sucC) SC0743(sucD)
            STM: STM0738(sucC) STM0739(sucD)
            YPE: YPO1115(sucC) YPO1116(sucD)
            YPK: y3064(sucD) y3065(sucC)
            YPM: YP_1040(sucD) YP_1041(sucC)
            YPA: YPA_0593 YPA_0594
            YPN: YPN_2882 YPN_2883
            YPP: YPDSF_2581 YPDSF_2582
            YPS: YPTB1149(sucC) YPTB1150(sucD)
            YPI: YpsIP31758_2878(sucD) YpsIP31758_2879(sucC)
            SFL: SF0568(sucD) SF0569(sucC)
            SFX: S0581(sucD) S0582(sucC)
            SFV: SFV_0607(sucD) SFV_0608(sucC)
            SSN: SSON_0679(sucC) SSON_0680(sucD)
            SBO: SBO_0586(sucC) SBO_0587(sucD)
            SDY: SDY_0666(sucC) SDY_0667(sucD)
            ECA: ECA1363(sucC) ECA1364(sucD)
            PLU: plu1432(sucC) plu1433(sucD)
            WBR: WGLp416(sucD) WGLp417(sucC)
            SGL: SG0878 SG0879
            ENT: Ent638_1228 Ent638_1229
            KPN: KPN_00734(sucC) KPN_00735(sucD)
            SPE: Spro_1269
            BFL: Bfl333(sucC) Bfl334(sucD)
            BPN: BPEN_343(sucC) BPEN_344(sucD)
            HIN: HI1196(sucC) HI1197(sucD)
            HIT: NTHI1367(sucC) NTHI1368(sucD)
            HSO: HS_0956(sucD) HS_0957(sucC)
            PMU: PM0280(sucC) PM0281(sucD)
            MSU: MS1351(sucD) MS1352(sucC)
            APL: APL_0451(sucD) APL_0452(sucC)
            ASU: Asuc_1565
            XFA: XF2547 XF2548
            XFT: PD1930(sucC) PD1931(sucD)
            XCC: XCC3093(sucD) XCC3094(sucC)
            XCB: XC_1063 XC_1064
            XCV: XCV3348(sucD) XCV3349(sucC)
            XAC: XAC3235(sucD) XAC3236(sucC)
            XOO: XOO1593(sucC) XOO1594(sucD)
            XOM: XOO_1476(XOO1476) XOO_1477(XOO1477)
            VCH: VC2084 VC2085
            VCO: VC0395_A1670(sucD) VC0395_A1671(sucC)
            VVU: VV1_0154 VV1_0155
            VVY: VV1034 VV1035
            VPA: VP0849 VP0850
            VFI: VF0825 VF0826
            PPR: PBPRA1050 PBPRA1051
            PAE: PA1588(sucC) PA1589(sucD)
            PAU: PA14_43940(sucD) PA14_43950(sucC)
            PPU: PP_4185(sucD) PP_4186(sucC)
            PPF: Pput_1668
            PST: PSPTO_2202(sucC) PSPTO_2203(sucD)
            PSB: Psyr_2012 Psyr_2013
            PSP: PSPPH_1983(sucC) PSPPH_1984(sucD)
            PFL: PFL_1721(sucC) PFL_1722(sucD)
            PFO: Pfl_1617 Pfl_1618
            PEN: PSEEN3635(sucD) PSEEN3636(sucC)
            PMY: Pmen_2499 Pmen_2500
            PAR: Psyc_0105 Psyc_0106
            PCR: Pcryo_0114 Pcryo_0115
            PRW: PsycPRwf_0269
            ACI: ACIAD2872(sucD) ACIAD2873(sucC)
            ACB: A1S_2718
            SON: SO_1932(sucC) SO_1933(sucD)
            SDN: Sden_2180 Sden_2181
            SFR: Sfri_2340 Sfri_2341
            SAZ: Sama_1429 Sama_1430
            SBL: Sbal_2512 Sbal_2513
            SBM: Shew185_2506
            SLO: Shew_1657 Shew_1658
            SPC: Sputcn32_2266 Sputcn32_2267
            SSE: Ssed_2812
            SPL: Spea_1790
            SHE: Shewmr4_1637 Shewmr4_1638
            SHM: Shewmr7_1712 Shewmr7_1713
            SHN: Shewana3_1712 Shewana3_1713
            SHW: Sputw3181_1741 Sputw3181_1742
            ILO: IL1500(sucD) IL1501(sucC)
            CPS: CPS_2221(sucC) CPS_2222(sucD)
            PHA: PSHAa1644(sucD) PSHAa1645(sucC)
            PAT: Patl_1801 Patl_1802
            SDE: Sde_2102 Sde_2103
            PIN: Ping_2249 Ping_2250
            MAQ: Maqu_1157 Maqu_1158
            CBU: CBU_1396(sucD) CBU_1397(sucC)
            CBD: COXBU7E912_0597(sucC) COXBU7E912_0598(sucD)
            LPN: lpg0534(sucC) lpg0535(sucD)
            LPF: lpl0580(sucC) lpl0581(sucD)
            LPP: lpp0599(sucC) lpp0600(sucD)
            MCA: MCA0967(sucC-1) MCA0968(sucD-1) MCA1740(sucC-2)
                 MCA1741(sucD-2)
            FTU: FTT0503c(sucD) FTT0504c(sucC)
            FTF: FTF0503c(sucD) FTF0504c(sucC)
            FTW: FTW_1561(sucC) FTW_1562(sucA2)
            FTL: FTL_1553 FTL_1554
            FTH: FTH_1504(sucC) FTH_1505(sucD)
            FTA: FTA_1639 FTA_1640
            FTN: FTN_0593(sucD) FTN_0594(sucC)
            TCX: Tcr_1373 Tcr_1374
            NOC: Noc_0713 Noc_0714
            AEH: Mlg_2547 Mlg_2548
            HHA: Hhal_2239 Hhal_2240
            HCH: HCH_04740(sucD) HCH_04741(sucC)
            CSA: Csal_1220 Csal_1221
            ABO: ABO_1492(sucD) ABO_1493(sucC)
            MMW: Mmwyl1_2797
            AHA: AHA_1929 AHA_1930
            DNO: DNO_1312(suc) DNO_1313(sucD)
            BCI: BCI_0097(sucC) BCI_0098(sucD)
            CRP: CRP_099 CRP_100
            RMA: Rmag_0146
            VOK: COSY_0149(sucD) COSY_0150(sucC)
            NME: NMB0959 NMB0960
            NMA: NMA1153(sucC) NMA1154(sucD)
            NMC: NMC0935(sucC) NMC0936(sucD)
            NGO: NGO0912 NGO0913
            CVI: CV_1075(sucC) CV_1076(sucD)
            RSO: RSc0554(sucC) RSc0555(sucD)
            REU: Reut_A0530 Reut_A0531
            REH: H16_A0547(sucC) H16_A0548(sucD)
            RME: Rmet_0469 Rmet_0470 Rmet_4358 Rmet_4359
            BMA: BMA0275(sucC) BMA0276(sucD)
            BMV: BMASAVP1_A2675(sucC) BMASAVP1_A2676(sucD)
            BML: BMA10299_A2400(sucD) BMA10299_A2401(sucC)
            BMN: BMA10247_0013(sucD) BMA10247_0014(sucC)
            BXE: Bxe_A0674 Bxe_A0675
            BVI: Bcep1808_2760
            BUR: Bcep18194_A5975 Bcep18194_A5976
            BCN: Bcen_2037 Bcen_2038
            BCH: Bcen2424_2648 Bcen2424_2649
            BAM: Bamb_2695 Bamb_2696
            BPS: BPSL0779(sucC) BPSL0780(sucD)
            BPM: BURPS1710b_0975(sucC) BURPS1710b_0977(sucD)
            BPL: BURPS1106A_0817(sucC) BURPS1106A_0818(sucD) BURPS1106A_A0787
            BPD: BURPS668_0813(sucC) BURPS668_0814(sucD) BURPS668_A0877
            BTE: BTH_I0646 BTH_I0647
            PNU: Pnuc_1831
            BPE: BP2540(sucD) BP2541(sucC)
            BPA: BPP2638(sucC) BPP2639(sucD)
            BBR: BB2081(sucC) BB2082(sucD)
            RFR: Rfer_3944 Rfer_3945
            POL: Bpro_4681 Bpro_4682
            PNA: Pnap_3953
            AAV: Aave_4684
            AJS: Ajs_4047
            VEI: Veis_2730
            MPT: Mpe_A0071 Mpe_A0072 Mpe_A3256
            HAR: HEAR0343(sucC) HEAR0344(sucD)
            MMS: mma_0390(sucC) mma_0391(sucD)
            NEU: NE0050(sucC) NE0051(sucD) NE1810 NE1811
            NET: Neut_0220 Neut_0221 Neut_0605 Neut_0606
            NMU: Nmul_A1079 Nmul_A1080 Nmul_A1995 Nmul_A1996
            EBA: ebA1271(sucD) ebA1272(sucC)
            AZO: azo3332(sucD)
            DAR: Daro_3363 Daro_3364
            TBD: Tbd_0805 Tbd_0806
            MFA: Mfla_1888 Mfla_1889
            WSU: WS1065(sucC) WS1066(sucD)
            TDN: Tmden_1050 Tmden_1051
            CJE: Cj0533(sucC) Cj0534(sucD)
            CJR: CJE0637(sucC) CJE0638(sucD)
            CJJ: CJJ81176_0558(sucC) CJJ81176_0559(sucD)
            CJU: C8J_0494(sucC) C8J_0495(sucD)
            CJD: JJD26997_1396(sucD) JJD26997_1397(sucC)
            CFF: CFF8240_0910(sucD) CFF8240_0911
            CCV: CCV52592_0620 CCV52592_0621 CCV52592_1882
            CHA: CHAB381_1137
            NIS: NIS_0838(sucC) NIS_0839(sucD)
            SUN: SUN_0576(sucC) SUN_0577(sucD)
            GSU: GSU1058(sucC) GSU1059(sucD)
            GME: Gmet_0729 Gmet_0730 Gmet_2068 Gmet_2069 Gmet_2260 Gmet_2261
            GUR: Gura_0155 Gura_3486 Gura_3998 Gura_4349
            PCA: Pcar_0246 Pcar_0247
            PPD: Ppro_1716
            DVU: DVU2137(sucCD)
            DDE: Dde_2334
            BBA: Bd3810(sucC) Bd3811(sucD)
            DPS: DP0284 DP0286
            ADE: Adeh_1627 Adeh_1628
            AFW: Anae109_2184 Anae109_3724
            MXA: MXAN_3541(sucC) MXAN_3542(sucD)
            SAT: SYN_00001 SYN_02501 SYN_02502 SYN_03227
            SFU: Sfum_1702 Sfum_1703
            RPR: RP432(sucD) RP433(sucC)
            RTY: RT0419(sucD) RT0420(sucC)
            RCO: RC0598(sucD) RC0599(sucC)
            RFE: RF_0664(sucD) RF_0665(sucC)
            RBE: RBE_1227(sucD) RBE_1228(sucC)
            RAK: A1C_03215 A1C_03220(sucC)
            RBO: A1I_01105(sucC) A1I_01110
            RRI: A1G_03360 A1G_03365(sucC)
            OTS: OTBS_0150(sucD) OTBS_0151(sucC)
            WOL: WD1209(sucD) WD1210(sucC)
            WBM: Wbm0519 Wbm0520
            AMA: AM230(sucD) AM231(sucC)
            APH: APH_1052(sucC) APH_1053(sucD)
            ERU: Erum1510(sucD) Erum1520(sucC)
            ERW: ERWE_CDS_01470(sucD) ERWE_CDS_01480(sucC)
            ERG: ERGA_CDS_01430(sucD) ERGA_CDS_01440(sucC)
            ECN: Ecaj_0147 Ecaj_0148
            ECH: ECH_0979(sucC) ECH_0980
            NSE: NSE_0250(sucD) NSE_0251(sucC)
            PUB: SAR11_0238(sucD) SAR11_0239(sucC)
            MLO: mll4303 mll4306 mlr1326
            MES: Meso_3396 Meso_3397
            PLA: Plav_1452
            SME: SMc02480(sucC) SMc02481(sucD)
            SMD: Smed_2943
            ATU: Atu2637(sucD) Atu2638(sucC)
            ATC: AGR_C_4779 AGR_C_4780
            RET: RHE_CH03889(sucD) RHE_CH03890(sucC)
            RLE: RL4436(sucD) RL4438(sucC)
            BME: BMEI0138 BMEI0139
            BMF: BAB1_1925 BAB1_1926(sucC)
            BMS: BR1925(sucD) BR1926(sucC)
            BMB: BruAb1_1901(sucD) BruAb1_1902(sucC)
            BOV: BOV_1853(sucD) BOV_1855(sucC)
            OAN: Oant_0931
            BJA: bll0453(sucD) bll0455(sucC)
            BRA: BRADO0404(sucC) BRADO0405(sucD)
            BBT: BBta_0393(sucC) BBta_0394(sucD)
            RPA: RPA0190(sucD) RPA0191(sucC)
            RPB: RPB_0279 RPB_0280
            RPC: RPC_0192 RPC_0193
            RPD: RPD_0536 RPD_0539
            RPE: RPE_0298 RPE_0299 RPE_3202 RPE_3203
            NWI: Nwi_0420 Nwi_0421
            NHA: Nham_0543 Nham_0544
            BHE: BH16550(sucD) BH16560(sucC)
            BQU: BQ13430(sucD) BQ13440(sucC)
            BBK: BARBAKC583_0023(sucC) BARBAKC583_0024(sucD)
            XAU: Xaut_0154 Xaut_0490
            CCR: CC_0337 CC_0338
            SIL: SPO0346(sucD) SPO0347 SPO1569
            SIT: TM1040_3512 TM1040_3514
            RSP: RSP_0966(sucD) RSP_0967(sucC)
            RSH: Rsph17029_2627
            RSQ: Rsph17025_0079
            JAN: Jann_0821 Jann_0827
            RDE: RD1_1611(sucD) RD1_1615(sucC) RD1_4246(mtkB)
            PDE: Pden_0559
            MMR: Mmar10_2818 Mmar10_2819
            HNE: HNE_0310(sucC) HNE_0311(sucD)
            ZMO: ZMO0567(sucD) ZMO1481(sucC)
            NAR: Saro_3170
            SAL: Sala_0176
            SWI: Swit_3197
            ELI: ELI_07990 ELI_13520
            GBE: GbCGDNIH1_0052 GbCGDNIH1_0053 GbCGDNIH1_2069 GbCGDNIH1_2070
            ACR: Acry_1625
            RRU: Rru_A1211 Rru_A1212 Rru_A1804
            MAG: amb3958 amb3959
            MGM: Mmc1_1747 Mmc1_1748
            ABA: Acid345_3874 Acid345_3875
            SUS: Acid_3378
            BSU: BG12680(sucC) BG12681(sucD)
            BHA: BH2469(sucD) BH2470(sucC)
            BAN: BA3973(sucD) BA3974(sucC)
            BAR: GBAA3973(sucD) GBAA3974(sucC)
            BAA: BA_4443 BA_4444
            BAT: BAS3686 BAS3687
            BCE: BC3833 BC3834
            BCA: BCE_3877(sucD) BCE_3878(sucC)
            BCZ: BCZK3594(sucD) BCZK3595(sucC)
            BCY: Bcer98_2488
            BTK: BT9727_3576(sucD) BT9727_3577(sucC)
            BLI: BL01284(sucD) BL01285(sucC)
            BLD: BLi01829(sucC) BLi01830(sucD)
            BCL: ABC2280(sucD) ABC2281(sucC)
            BAY: RBAM_015920(sucC) RBAM_015930(sucD)
            BPU: BPUM_1507(sucC) BPUM_1508(sucD)
            OIH: OB1543(sucC) OB1544(sucD)
            GKA: GK1208(sucC) GK1209(sucD)
            SAU: SA1088(sucC) SA1089(sucD)
            SAV: SAV1245(sucC) SAV1246(sucD)
            SAM: MW1128(sucC) MW1129(sucD)
            SAR: SAR1221 SAR1222
            SAS: SAS1179 SAS1180
            SAC: SACOL1262(sucC) SACOL1263(sucD)
            SAB: SAB1109 SAB1110
            SAA: SAUSA300_1138(sucC) SAUSA300_1139(sucD)
            SAO: SAOUHSC_01216 SAOUHSC_01218
            SAJ: SaurJH9_1304
            SAH: SaurJH1_1329
            SEP: SE0923 SE0924
            SER: SERP0813(sucC) SERP0814(sucD)
            SHA: SH1667(sucD) SH1668(sucC)
            SSP: SSP1520 SSP1521
            STH: STH2532 STH2533
            AMT: Amet_0484
            CHY: CHY_0912(sucC) CHY_0913(sucD)
            DSY: DSY0245 DSY0982 DSY0983 DSY1925 DSY1926
            MTA: Moth_0397 Moth_0399
            MTU: Rv0951(sucC) Rv0952(sucD)
            MTC: MT0978(sucC) MT0979(sucD)
            MBO: Mb0976(sucC) Mb0977(sucD)
            MBB: BCG_1005(sucC) BCG_1006(sucD)
            MLE: ML0155(sucC) ML0156(sucD)
            MPA: MAP0896(sucC) MAP0897(sucD)
            MAV: MAV_1074 MAV_1075
            MSM: MSMEG_5524(sucD) MSMEG_5525(sucC)
            MVA: Mvan_4870
            MGI: Mflv_1865
            MMC: Mmcs_4326 Mmcs_4327
            MKM: Mkms_4413
            MJL: Mjls_4707
            CGL: NCgl2476(cgl2565) NCgl2477(cgl2566)
            CGB: cg2836(sucD) cg2837(sucC)
            CEF: CE2449 CE2451
            NFA: nfa49900(sucD) nfa49910(sucC)
            RHA: RHA1_ro05573(sucC) RHA1_ro05574(sucD)
            SCO: SCO4808(SCD63A.19) SCO4809(SCD63A.20) SCO6585 SCO6586
            SMA: SAV1817(sucD1) SAV1818(sucC1) SAV3451(sucD2) SAV3452(sucC2)
            LXX: Lxx19700(sucD) Lxx19720(sucC)
            CMI: CMM_2547(sucD) CMM_2548(sucC)
            ART: Arth_0815
            AAU: AAur_1044(sucC) AAur_1045(sucD)
            PAC: PPA1754 PPA1755
            NCA: Noca_3590
            TFU: Tfu_2576 Tfu_2577
            FRA: Francci3_0651 Francci3_0652
            FAL: FRAAL1156(sucC) FRAAL1157(sucD)
            ACE: Acel_0380 Acel_0381
            KRA: Krad_3999
            SEN: SACE_6668 SACE_6669(sucC)
            BLO: BL0732(sucC) BL0733(sucD)
            BAD: BAD_0808(sucC) BAD_0809(sucD)
            RXY: Rxyl_1275 Rxyl_1276
            RBA: RB10617(sucC) RB10619(sucD)
            CTR: CT821(sucC) CT822(sucD)
            CTA: CTA_0895(sucC) CTA_0896(sucD)
            CMU: TC0208 TC0209
            CPN: CPn0973(sucC) CPn0974(sucD)
            CPA: CP0885 CP0886
            CPJ: CPj0972(sucC) CPj0973(sucD)
            CPT: CpB1009 CpB1010
            CCA: CCA00783(sucD) CCA00784(sucC)
            CAB: CAB751(sucD) CAB752(sucC)
            CFE: CF0229(sucC) CF0230(sucD)
            PCU: pc1297(sucD) pc1298(sucC)
            LIL: LA1101(sucD) LA1102(sucC)
            LIC: LIC12573(sucC) LIC12574(sucD)
            LBJ: LBJ_2273(sucC) LBJ_2274(sucD)
            LBL: LBL_0833(sucD) LBL_0834(sucC)
            SYN: sll1023(sucC) sll1557(sucD)
            ANA: all3913 all3914
            AVA: Ava_1783 Ava_1784 Ava_4664
            TER: Tery_2750 Tery_2751
            BTH: BT_0787 BT_0788
            BFR: BF2256 BF2257
            BFS: BF2350(sucD) BF2351(sucC)
            SRU: SRU_0670(sucD) SRU_1125
            CHU: CHU_2240(sucC) CHU_2402(sucD)
            GFO: GFO_0752(sucC) GFO_1768(sucD)
            FJO: Fjoh_2162
            FPS: FP0908(sucC) FP0972(sucD)
            CTE: CT0269(sucD) CT0380(sucC)
            CCH: Cag_0338 Cag_0466 Cag_0796
            CPH: Cpha266_0623
            PVI: Cvib_0553
            PLT: Plut_0497 Plut_1748
            RRS: RoseRS_3930
            RCA: Rcas_3203
            DRA: DR_1247 DR_1248
            DGE: Dgeo_1088 Dgeo_1089
            TTH: TTC0169 TTC0170
            TTJ: TTHA0537 TTHA0538
            AAE: aq_1306(sucC1) aq_1620(sucC2) aq_1622(sucD2) aq_1888(sucD1)
            TME: Tmel_1870
            FNO: Fnod_1378
            MJA: MJ0210(sucC) MJ1246(sucD)
            MMP: MMP0955(sucD) MMP1105(sucC)
            MMQ: MmarC5_0479
            MMZ: MmarC7_0357
            MAE: Maeo_0043
            MVN: Mevan_0430
            MHU: Mhun_0095 Mhun_0096
            MEM: Memar_0841
            MBN: Mboo_0727
            MTH: MTH1036 MTH563
            MST: Msp_0583(sucD) Msp_1386(sucC)
            MSI: Msm_0228 Msm_0924
            MKA: MK0731(sucC) MK0732(sucD)
            AFU: AF1539(sucD-1) AF1540(sucC-1) AF2185(sucD-2) AF2186(sucC-2)
            HAL: VNG1541G(sucC) VNG1542G(sucD)
            HMA: rrnAC0472(sucC) rrnAC0474(sucD) rrnAC0888(scs)
            HWA: HQ2857A(sucD) HQ2858A(sucC)
            NPH: NP4354A(sucD) NP4356A(sucC)
            TAC: Ta1331 Ta1332m
            TVO: TVN0273 TVN0274
            PTO: PTO1002 PTO1003
            APE: APE_1065.1 APE_1072.1
            SMR: Smar_0470 Smar_0471
            IHO: Igni_0085 Igni_0086
            HBU: Hbut_0202 Hbut_0203
            SSO: SSO2482(sucD) SSO2483(sucC)
            STO: ST0962 ST0963
            SAI: Saci_1265(sucC)
            MSE: Msed_1582
            PAI: PAE2312(sucC) PAE2313(sucD)
            PIS: Pisl_1026
            PCL: Pcal_1657
            PAS: Pars_1529
            TPE: Tpen_0516 Tpen_0517
STRUCTURES  PDB: 1CQI  1CQJ  1JKJ  1JLL  1OI7  1SCU  2NU6  2NU7  2NU8  2NU9  
                 2NUA  2SCU  2YV1  2YV2  
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.5
            ExPASy - ENZYME nomenclature database: 6.2.1.5
            ExplorEnz - The Enzyme Database: 6.2.1.5
            ERGO genome analysis and discovery system: 6.2.1.5
            BRENDA, the Enzyme Database: 6.2.1.5
            CAS: 9080-33-5
///
ENTRY       EC 6.2.1.6                  Enzyme
NAME        glutarate---CoA ligase;
            glutaryl-CoA synthetase;
            glutaryl coenzyme A synthetase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     glutarate:CoA ligase (ADP-forming)
REACTION    ATP + glutarate + CoA = ADP + phosphate + glutaryl-CoA [RN:R02402]
ALL_REAC    R02402
SUBSTRATE   ATP [CPD:C00002];
            glutarate [CPD:C00489];
            CoA [CPD:C00010]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            glutaryl-CoA [CPD:C00527]
COMMENT     GTP or ITP can act instead of ATP.
REFERENCE   1
  AUTHORS   Menon, G.K.K., Friedman, D.L. and Stern, J.R.
  TITLE     Enzymic synthesis of glutaryl-coenzyme A.
  JOURNAL   Biochim. Biophys. Acta 44 (1960) 375-377.
  ORGANISM  dog [GN:cfa], rat [GN:rno], pigeon
PATHWAY     PATH: map00071  Fatty acid metabolism
            PATH: map00310  Lysine degradation
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.6
            ExPASy - ENZYME nomenclature database: 6.2.1.6
            ExplorEnz - The Enzyme Database: 6.2.1.6
            ERGO genome analysis and discovery system: 6.2.1.6
            BRENDA, the Enzyme Database: 6.2.1.6
            CAS: 9023-68-1
///
ENTRY       EC 6.2.1.7                  Enzyme
NAME        cholate---CoA ligase;
            BAL;
            bile acid CoA ligase;
            bile acid coenzyme A ligase;
            choloyl-CoA synthetase;
            choloyl coenzyme A synthetase;
            cholic thiokinase;
            cholate thiokinase;
            cholic acid:CoA ligase;
            3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl coenzyme A
            synthetase;
            3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate-CoA ligase;
            3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate-CoA synthetase;
            THCA-CoA ligase;
            3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate---CoA ligase;
            3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate:CoA ligase
            (AMP-forming);
            cholyl-CoA synthetase;
            trihydroxycoprostanoyl-CoA synthetase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     cholate:CoA ligase (AMP-forming)
REACTION    (1) ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA
            [RN:R02794];
            (2) ATP + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate
            + CoA = AMP + diphosphate +
            (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA
            [RN:R04580]
ALL_REAC    R02794 R04580;
            (other) R03974 R04507
SUBSTRATE   ATP [CPD:C00002];
            cholate [CPD:C00695];
            CoA [CPD:C00010];
            (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            choloyl-CoA [CPD:C01794];
            (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA
COMMENT     Requires Mg2+ for activity. This membrane-bound enzyme catalyses the
            first step in the conjugation of bile acids with amino acids,
            converting bile acids into their acyl-CoA thioesters. The second
            step involves EC 2.3.1.65, bile acid-CoA:amino acid
            N-acyltransferase and converts the acyl-CoA thioester into the
            corresponding N-acyl amidate by conjugation with glycine or taurine
            [5]. Chenodeoxycholate, deoxycholate, lithocholate and
            trihydroxycoprostanoate can also act as substrates [6].
REFERENCE   1  [PMID:13303991]
  AUTHORS   ELLIOTT WH.
  TITLE     The enzymic activation of cholic acid by guinea-pig-liver
            microsomes.
  JOURNAL   Biochem. J. 62 (1956) 427-33.
  ORGANISM  guinea pig
REFERENCE   2  [PMID:13403911]
  AUTHORS   ELLIOTT WH.
  TITLE     The breakdown of adenosine triphosphate accompanying cholic acid
            activation by guinea-pig liver microsomes.
  JOURNAL   Biochem. J. 65 (1957) 315-21.
  ORGANISM  guinea pig
REFERENCE   3  [PMID:3183523]
  AUTHORS   Prydz K, Kase BF, Bjorkhem I, Pedersen JI.
  TITLE     Subcellular localization of 3 alpha, 7 alpha-dihydroxy- and 3
            alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoyl-coenzyme A
            ligase(s) in rat liver.
  JOURNAL   J. Lipid. Res. 29 (1988) 997-1004.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:2521999]
  AUTHORS   Schepers L, Casteels M, Verheyden K, Parmentier G, Asselberghs S,
            Eyssen HJ, Mannaerts GP.
  TITLE     Subcellular distribution and characteristics of
            trihydroxycoprostanoyl-CoA synthetase in rat liver.
  JOURNAL   Biochem. J. 257 (1989) 221-9.
  ORGANISM  rat [GN:rno]
REFERENCE   5  [PMID:9390170]
  AUTHORS   Wheeler JB, Shaw DR, Barnes S.
  TITLE     Purification and characterization of a rat liver bile acid coenzyme
            A ligase from rat liver microsomes.
  JOURNAL   Arch. Biochem. Biophys. 348 (1997) 15-24.
  ORGANISM  rat [GN:rno]
REFERENCE   6  [PMID:12454267]
  AUTHORS   Falany CN, Xie X, Wheeler JB, Wang J, Smith M, He D, Barnes S.
  TITLE     Molecular cloning and expression of rat liver bile acid CoA ligase.
  JOURNAL   J. Lipid. Res. 43 (2002) 2062-71.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00120  Bile acid biosynthesis
            PATH: map03320  PPAR signaling pathway
ORTHOLOGY   KO: K08748  solute carrier family 27 (fatty acid transporter),
                        member 5
GENES       HSA: 10998(SLC27A5)
            PTR: 456351(SLC27A5)
            MMU: 26459(Slc27a5)
            CFA: 484223(LOC484223) 608675(SLC27A5)
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.7
            ExPASy - ENZYME nomenclature database: 6.2.1.7
            ExplorEnz - The Enzyme Database: 6.2.1.7
            ERGO genome analysis and discovery system: 6.2.1.7
            BRENDA, the Enzyme Database: 6.2.1.7
            CAS: 9027-90-1
///
ENTRY       EC 6.2.1.8                  Enzyme
NAME        oxalate---CoA ligase;
            oxalyl-CoA synthetase;
            oxalyl coenzyme A synthetase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     oxalate:CoA ligase (AMP-forming)
REACTION    ATP + oxalate + CoA = AMP + diphosphate + oxalyl-CoA [RN:R01558]
ALL_REAC    R01558
SUBSTRATE   ATP [CPD:C00002];
            oxalate [CPD:C00209];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            oxalyl-CoA [CPD:C00313]
REFERENCE   1  [PMID:4288975]
  AUTHORS   Giovanelli J.
  TITLE     Oxalyl-coenzyme A synthetase from pea seeds.
  JOURNAL   Biochim. Biophys. Acta. 118 (1966) 124-43.
  ORGANISM  Pisum sativum
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.8
            ExPASy - ENZYME nomenclature database: 6.2.1.8
            ExplorEnz - The Enzyme Database: 6.2.1.8
            ERGO genome analysis and discovery system: 6.2.1.8
            BRENDA, the Enzyme Database: 6.2.1.8
            CAS: 37318-57-3
///
ENTRY       EC 6.2.1.9                  Enzyme
NAME        malate---CoA ligase;
            malyl-CoA synthetase;
            malyl coenzyme A synthetase;
            malate thiokinase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     malate:CoA ligase (ADP-forming)
REACTION    ATP + malate + CoA = ADP + phosphate + malyl-CoA [RN:R07645]
ALL_REAC    R07645 > R01256
SUBSTRATE   ATP [CPD:C00002];
            malate [CPD:C00711];
            CoA [CPD:C00010]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            malyl-CoA [CPD:C04348]
REFERENCE   1
  AUTHORS   Mue, S., Tuboi, S. and Kikuchi, G.
  TITLE     On malyl-coenzyme A synthetase.
  JOURNAL   J. Biochem. (Tokyo) 56 (1964) 545-551.
  ORGANISM  Rhodopseudomonas spheroides
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
ORTHOLOGY   KO: K08692  malate-CoA ligase
GENES       MPT: Mpe_A3257
            MLO: mlr1324
            SIL: SPO1568
            RDE: RD1_1162(mtkA) RD1_1163(mtkB) RD1_4245(mtkA)
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.9
            ExPASy - ENZYME nomenclature database: 6.2.1.9
            ExplorEnz - The Enzyme Database: 6.2.1.9
            ERGO genome analysis and discovery system: 6.2.1.9
            BRENDA, the Enzyme Database: 6.2.1.9
            CAS: 37318-58-4
///
ENTRY       EC 6.2.1.10                 Enzyme
NAME        acid---CoA ligase (GDP-forming);
            acyl-CoA synthetase (GDP-forming);
            acyl coenzyme A synthetase (guanosine diphosphate forming)
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     acid:CoA ligase (GDP-forming)
REACTION    GTP + an acid + CoA = GDP + phosphate + acyl-CoA [RN:R00394]
ALL_REAC    R00394
SUBSTRATE   GTP [CPD:C00044];
            acid [CPD:C00174];
            CoA [CPD:C00010]
PRODUCT     GDP [CPD:C00035];
            phosphate [CPD:C00009];
            acyl-CoA [CPD:C00040]
REFERENCE   1
  AUTHORS   Rossi, C.R. and Gibson, D.M.
  TITLE     Activation of fatty acids by a guanosine triphosphate-specific
            thiokinase from liver mitochondria.
  JOURNAL   J. Biol. Chem. 239 (1964) 1694-1699.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.10
            ExPASy - ENZYME nomenclature database: 6.2.1.10
            ExplorEnz - The Enzyme Database: 6.2.1.10
            ERGO genome analysis and discovery system: 6.2.1.10
            BRENDA, the Enzyme Database: 6.2.1.10
            CAS: 37318-59-5
///
ENTRY       EC 6.2.1.11                 Enzyme
NAME        biotin---CoA ligase;
            biotinyl-CoA synthetase;
            biotin CoA synthetase;
            biotinyl coenzyme A synthetase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     biotin:CoA ligase (AMP-forming)
REACTION    ATP + biotin + CoA = AMP + diphosphate + biotinyl-CoA [RN:R01075]
ALL_REAC    R01075;
            (other) R01074 R03762
SUBSTRATE   ATP [CPD:C00002];
            biotin [CPD:C00120];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            biotinyl-CoA [CPD:C01894]
REFERENCE   1  [PMID:14257635]
  AUTHORS   CHRISTNER JE, SCHLESINGER MJ, COON MJ.
  TITLE     ENZYMATIC ACTIVATION OF BIOTIN. BIOTINYL ADENYLATE FORMATION.
  JOURNAL   J. Biol. Chem. 239 (1964) 3997-4005.
  ORGANISM  pig [GN:ssc]
PATHWAY     PATH: map00780  Biotin metabolism
GENES       REH: H16_B1756
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.11
            ExPASy - ENZYME nomenclature database: 6.2.1.11
            ExplorEnz - The Enzyme Database: 6.2.1.11
            ERGO genome analysis and discovery system: 6.2.1.11
            BRENDA, the Enzyme Database: 6.2.1.11
            CAS: 37318-60-8
///
ENTRY       EC 6.2.1.12                 Enzyme
NAME        4-coumarate---CoA ligase;
            4-coumaroyl-CoA synthetase;
            p-coumaroyl CoA ligase;
            p-coumaryl coenzyme A synthetase;
            p-coumaryl-CoA synthetase;
            p-coumaryl-CoA ligase;
            feruloyl CoA ligase;
            hydroxycinnamoyl CoA synthetase;
            4-coumarate:coenzyme A ligase;
            caffeolyl coenzyme A synthetase;
            p-hydroxycinnamoyl coenzyme A synthetase;
            feruloyl coenzyme A synthetase;
            sinapoyl coenzyme A synthetase;
            4-coumaryl-CoA synthetase;
            hydroxycinnamate:CoA ligase;
            p-coumaryl-CoA ligase;
            p-hydroxycinnamic acid:CoA ligase;
            4CL
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     4-coumarate:CoA ligase (AMP-forming)
REACTION    ATP + 4-coumarate + CoA = AMP + diphosphate + 4-coumaroyl-CoA
            [RN:R01616]
ALL_REAC    R01616;
            (other) R01943 R02194 R02221 R02255 R06583
SUBSTRATE   ATP [CPD:C00002];
            4-coumarate [CPD:C00811];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            4-coumaroyl-CoA [CPD:C00223]
REFERENCE   1  [PMID:4364250]
  AUTHORS   Gross GG, Zenk MH.
  TITLE     Isolation and properties of hydroxycinnamate: CoA ligase from
            lignifying tissue of Forsythia.
  JOURNAL   Eur. J. Biochem. 42 (1974) 453-9.
  ORGANISM  Forsythia suspensa
REFERENCE   2  [PMID:4699252]
  AUTHORS   Lindl T, Kreuzaler F, Hahlbrock K.
  TITLE     Synthesis of p-coumaroyl coenzyme a with a partially purified
            p-coumarate:CoA ligase from cell suspension cultures of soybean
            (Glycine max).
  JOURNAL   Biochim. Biophys. Acta. 302 (1973) 457-64.
  ORGANISM  Glycine max [GN:egma]
PATHWAY     PATH: map00940  Phenylpropanoid biosynthesis
ORTHOLOGY   KO: K01904  4-coumarate--CoA ligase
GENES       SPU: 581911(LOC581911)
            CEL: AH10.1 C01G6.7 F11A3.1 ZK1127.2
            ATH: AT1G51680(4CL1) AT1G62940 AT1G65060(4CL3) AT3G21240(4CL2)
                 AT4G05160
            OSA: 4335451 4341718
            AFM: AFUA_1G13110
            LMA: LmjF19.0985 LmjF19.1005
            HHA: Hhal_1819
            REH: H16_B0714
            HAR: HEAR2864
            RPA: RPA4421
            SIL: SPO0801(fadD)
            RDE: RD1_1868
            RHA: RHA1_ro03026 RHA1_ro08971
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.12
            ExPASy - ENZYME nomenclature database: 6.2.1.12
            ExplorEnz - The Enzyme Database: 6.2.1.12
            ERGO genome analysis and discovery system: 6.2.1.12
            BRENDA, the Enzyme Database: 6.2.1.12
            CAS: 37332-51-7
///
ENTRY       EC 6.2.1.13                 Enzyme
NAME        acetate---CoA ligase (ADP-forming);
            acetyl-CoA synthetase (ADP-forming);
            acetyl coenzyme A synthetase (adenosine diphosphate-forming);
            acetate thiokinase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     acetate:CoA ligase (ADP-forming)
REACTION    ATP + acetate + CoA = ADP + phosphate + acetyl-CoA [RN:R00229]
ALL_REAC    R00229;
            (other) R00920
SUBSTRATE   ATP [CPD:C00002];
            acetate [CPD:C00033];
            CoA [CPD:C00010]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            acetyl-CoA [CPD:C00024]
COMMENT     Also acts on propanoate and, very slowly, on butanoate.
REFERENCE   1  [PMID:13076]
  AUTHORS   Reeves RE, Warren LG, Susskind B, Lo HS.
  TITLE     An energy-conserving pyruvate-to-acetate pathway in Entamoeba
            histolytica. Pyruvate synthase and a new acetate thiokinase.
  JOURNAL   J. Biol. Chem. 252 (1977) 726-31.
  ORGANISM  Entamoeba histolytica [GN:ehi]
PATHWAY     PATH: map00620  Pyruvate metabolism
            PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K01905  acetyl-CoA synthetase (ADP-forming)
GENES       CME: CMN336C
            PFA: PF14_0357
            BMA: BMAA0367
            BPS: BPSS2130
            BPM: BURPS1710b_A1237
            BTE: BTH_II2206
            BPE: BP0661
            BBR: BB4797
            SAT: SYN_00647 SYN_02607 SYN_02878
            BBT: BBta_7760
            CHY: CHY_0264
            MMP: MMP0253(acd)
            NPH: NP2858A(acdA)
            PFU: PF1540 PF1787
            RCI: RCIX1773(acdB) RCIX1774(acdA) RCIX831(acdAB)
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.13
            ExPASy - ENZYME nomenclature database: 6.2.1.13
            ExplorEnz - The Enzyme Database: 6.2.1.13
            ERGO genome analysis and discovery system: 6.2.1.13
            BRENDA, the Enzyme Database: 6.2.1.13
            CAS: 62009-85-2
///
ENTRY       EC 6.2.1.14                 Enzyme
NAME        6-carboxyhexanoate---CoA ligase;
            6-carboxyhexanoyl-CoA synthetase;
            pimelyl-CoA synthetase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     6-carboxyhexanoate:CoA ligase (AMP-forming)
REACTION    ATP + 6-carboxyhexanoate + CoA = AMP + diphosphate +
            6-carboxyhexanoyl-CoA [RN:R03209]
ALL_REAC    R03209
SUBSTRATE   ATP [CPD:C00002];
            6-carboxyhexanoate [CPD:C02656];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            6-carboxyhexanoyl-CoA [CPD:C01063]
REFERENCE   1  [PMID:4623286]
  AUTHORS   Izumi Y, Morita H, Sato K, Tani Y, Ogata K.
  TITLE     Synthesis of biotin-vitamers from pimelic acid and coenzyme A by
            cell-free extracts of various bacteria.
  JOURNAL   Biochim. Biophys. Acta. 264 (1972) 210-3.
  ORGANISM  Bacillus megaterium, Bacillus sphaericus
REFERENCE   2
  AUTHORS   Izumi, Y., Morita, H., Tani, Y. and Ogata, K.
  TITLE     The pimelyl-CoA synthetase responsible for the first step in biotin
            biosynthesis by microorganisms.
  JOURNAL   Agric. Biol. Chem. 38 (1974) 2257-2262.
PATHWAY     PATH: map00780  Biotin metabolism
ORTHOLOGY   KO: K01906  6-carboxyhexanoate--CoA ligase
GENES       REH: H16_B0928 H16_B1438
            BXE: Bxe_C0568
            PCA: Pcar_1666
            RLE: pRL120177(pauA)
            BJA: blr3446
            BBT: BBta_5094
            BSU: BG11529(bioW)
            BLI: BL02411(bioW)
            BLD: BLi00766(bioW)
            BAY: RBAM_018290(bioW)
            SAU: SA2211
            SAV: SAV2423
            SAM: MW2346
            SAR: SAR2513
            SAS: SAS2314
            SAC: SACOL2424(bioW)
            SAB: SAB2304c
            SAA: SAUSA300_2369
            SAO: SAOUHSC_02712
            SAJ: SaurJH9_2449
            SAH: SaurJH1_2497
            SEP: SE0182
            SER: SERP2393(bioW)
            CDI: DIP1381
            SEN: SACE_5038
            TTH: TTC1711
            AAE: aq_1659(bioW)
            MMP: MMP1575(bioW)
            MMQ: MmarC5_0001
            MMZ: MmarC7_0822
            MAE: Maeo_1420
            MVN: Mevan_0887
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.14
            ExPASy - ENZYME nomenclature database: 6.2.1.14
            ExplorEnz - The Enzyme Database: 6.2.1.14
            ERGO genome analysis and discovery system: 6.2.1.14
            BRENDA, the Enzyme Database: 6.2.1.14
            CAS: 55467-50-0
///
ENTRY       EC 6.2.1.15                 Enzyme
NAME        arachidonate---CoA ligase;
            arachidonoyl-CoA synthetase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     arachidonate:CoA ligase (AMP-forming)
REACTION    ATP + arachidonate + CoA = AMP + diphosphate + arachidonoyl-CoA
            [RN:R01598]
ALL_REAC    R01598
SUBSTRATE   ATP [CPD:C00002];
            arachidonate [CPD:C00219];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            arachidonoyl-CoA [CPD:C02249]
COMMENT     Not identical with EC 6.2.1.3 long-chain-fatty-acid---CoA ligase.
            Icosa-8,11,14-trienoate, but not the other long-chain fatty acids,
            can act in place of arachidonate.
REFERENCE   1  [PMID:7061494]
  AUTHORS   Wilson DB, Prescott SM, Majerus PW.
  TITLE     Discovery of an arachidonoyl coenzyme A synthetase in human
            platelets.
  JOURNAL   J. Biol. Chem. 257 (1982) 3510-5.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.15
            ExPASy - ENZYME nomenclature database: 6.2.1.15
            ExplorEnz - The Enzyme Database: 6.2.1.15
            ERGO genome analysis and discovery system: 6.2.1.15
            BRENDA, the Enzyme Database: 6.2.1.15
            CAS: 82047-87-8
///
ENTRY       EC 6.2.1.16                 Enzyme
NAME        acetoacetate---CoA ligase;
            acetoacetyl-CoA synthetase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     acetoacetate:CoA ligase (AMP-forming)
REACTION    ATP + acetoacetate + CoA = AMP + diphosphate + acetoacetyl-CoA
            [RN:R01357]
ALL_REAC    R01357
SUBSTRATE   ATP [CPD:C00002];
            acetoacetate [CPD:C00164];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            acetoacetyl-CoA [CPD:C00332]
COMMENT     Also acts, more slowly, on L-3-hydroxybutanoate.
REFERENCE   1  [PMID:7140777]
  AUTHORS   Fukui T, Ito M, Tomita K.
  TITLE     Purification and characterization of acetoacetyl-CoA synthetase from
            Zoogloea ramigera I-16-M.
  JOURNAL   Eur. J. Biochem. 127 (1982) 423-8.
  ORGANISM  Zoogloea ramigera
PATHWAY     PATH: map00650  Butanoate metabolism
ORTHOLOGY   KO: K01907  acetoacetyl-CoA synthetase
GENES       HSA: 65985(AACS)
            MMU: 78894(Aacs)
            CFA: 486240(AACS)
            DRE: 393984(aacs)
            CME: CMT445C
            ANI: AN1103.2
            AFM: AFUA_1G11880 AFUA_8G04770
            AOR: AO090001000376
            UMA: UM00285.1 UM05131.1
            PAP: PSPA7_3297
            PFL: PFL_3577
            PFO: Pfl_3080
            PEN: PSEEN3159
            CBD: COXBU7E912_0779
            NOC: Noc_2047
            AEH: Mlg_2108
            HCH: HCH_03948
            CSA: Csal_1820
            ABO: ABO_1236(acsA)
            AHA: AHA_0140
            CVI: CV_1758
            REU: Reut_A0764
            REH: H16_A2860
            RME: Rmet_2699
            BUR: Bcep18194_B1209
            RFR: Rfer_3963
            POL: Bpro_0120
            VEI: Veis_3179
            EBA: ebA321(acsA) ebA4666 ebA5760
            DAR: Daro_0177
            MLO: mlr6539
            SME: SMc00774(acsA2)
            ATU: Atu4130(acsA)
            ATC: AGR_L_1446
            RET: RHE_CH00719(acsA1)
            RLE: RL0768(acsA)
            BME: BMEI1921 BMEI1922
            BMS: BR0021
            BOV: BOV_0018
            BJA: blr4674
            SIL: SPO1959
            SIT: TM1040_3294
            RRU: Rru_A3695
            MAG: amb0580
            OIH: OB0504
            GKA: GK1485
            MSM: MSMEG_6024
            MMC: Mmcs_4700
            RHA: RHA1_ro00539 RHA1_ro02673 RHA1_ro06100
            SCO: SCO1393(acsA)
            SMA: SAV6970(acsA2)
            TFU: Tfu_2245
            FRA: Francci3_3504
            FAL: FRAAL5696(acsA)
            SEN: SACE_0219(acsA)
            RXY: Rxyl_2342
            PTO: PTO1175
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.16
            ExPASy - ENZYME nomenclature database: 6.2.1.16
            ExplorEnz - The Enzyme Database: 6.2.1.16
            ERGO genome analysis and discovery system: 6.2.1.16
            BRENDA, the Enzyme Database: 6.2.1.16
            CAS: 39394-62-2
///
ENTRY       EC 6.2.1.17                 Enzyme
NAME        propionate---CoA ligase;
            propionyl-CoA synthetase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     propanoate:CoA ligase (AMP-forming)
REACTION    ATP + propanoate + CoA = AMP + diphosphate + propanoyl-CoA
            [RN:R00925]
ALL_REAC    R00925;
            (other) R00926 R01354
SUBSTRATE   ATP [CPD:C00002];
            propanoate [CPD:C00163];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            propanoyl-CoA [CPD:C00100]
COMMENT     Propenoate can act instead of propanoate. Not identical with EC
            6.2.1.1 (acetate---CoA ligase) or EC 6.2.1.2 (butyrate---CoA
            ligase).
REFERENCE   1  [PMID:7341659]
  AUTHORS   Ricks CA, Cook RM.
  TITLE     Regulation of volatile fatty acid uptake by mitochondrial acyl CoA
            synthetases of bovine liver.
  JOURNAL   J. Dairy. Sci. 64 (1981) 2324-35.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K01908  propionyl-CoA synthetase
GENES       ANI: AN5833.2
            AFM: AFUA_2G07780
            AOR: AO090011000917
            DDI: DDB_0231689(aslB)
            ECO: b0335(prpE)
            ECJ: JW0326(prpE)
            ECE: Z0430(prpE)
            ECS: ECs0388
            ECC: c0454(prpE)
            ECI: UTI89_C0366(prpE)
            ECP: ECP_0410
            ECV: APECO1_1654(prpE)
            ECW: EcE24377A_0359(prpE)
            ECX: EcHS_A0400
            STY: STY0403(prpE)
            STT: t2493(prpE)
            SPT: SPA2352(prpE)
            SEC: SC0412(prpE)
            STM: STM0371(prpE)
            PLU: plu3539(prpE)
            VCH: VC1340
            VVU: VV1_2728
            VVY: VV1533
            VPA: VP1644
            PPR: PBPRB0238
            PAE: PA3568
            PPU: PP_2351
            PAR: Psyc_0899(prpE)
            PCR: Pcryo_1518
            ILO: IL1063(prpE)
            CPS: CPS_0917
            PHA: PSHAa2444(prpE)
            ABO: ABO_1731(acsA)
            RSO: RSc1518(prpE)
            REU: Reut_A2185
            REH: H16_A2462(prpE)
            RME: Rmet_2203
            BXE: Bxe_A1339
            BPE: BP2412(prpE)
            BPA: BPP3277(prpE)
            BBR: BB3728(prpE)
            RFR: Rfer_2322
            POL: Bpro_2633
            MPT: Mpe_A0395 Mpe_A2513
            HAR: HEAR3269(prpE)
            MMS: mma_3490
            EBA: ebA7220(prpE)
            AZO: azo3179(prpE)
            DAR: Daro_1204
            HHE: HH0396(acoE)
            PUB: SAR11_0624(prpE)
            RET: RHE_CH04114(ypch01449)
            RLE: RL4730(prpE)
            BME: BMEI0307
            BMF: BAB1_1744
            BMS: BR1731(prpE)
            BMB: BruAb1_1716(prpE)
            BOV: BOV_1673(prpE)
            BRA: BRADO6593
            BBT: BBta_0943
            RPE: RPE_4455
            SIL: SPO2934(prpE)
            SIT: TM1040_1574
            RDE: RD1_3986(prpE)
            RRU: Rru_A1046
            MGM: Mmc1_0383
            AAU: AAur_pTC20154(prpE)
            SEN: SACE_3848
            PMB: A9601_06751(acs)
            PMC: P9515_06841(acs)
            PMF: P9303_18991(acs)
            PMG: P9301_06451(acs)
            PME: NATL1_06781(acs)
            PLT: Plut_1288
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.17
            ExPASy - ENZYME nomenclature database: 6.2.1.17
            ExplorEnz - The Enzyme Database: 6.2.1.17
            ERGO genome analysis and discovery system: 6.2.1.17
            BRENDA, the Enzyme Database: 6.2.1.17
            CAS: 55326-49-3
///
ENTRY       EC 6.2.1.18                 Enzyme
NAME        citrate---CoA ligase;
            citryl-CoA synthetase;
            citrate:CoA ligase;
            citrate thiokinase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     citrate:CoA ligase (ADP-forming)
REACTION    ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA [RN:R01322]
ALL_REAC    R01322
SUBSTRATE   ATP [CPD:C00002];
            citrate [CPD:C00158];
            CoA [CPD:C00010]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            (3S)-citryl-CoA [CPD:C00566]
COMMENT     The enzyme is a component of EC 2.3.3.8 ATP citrate synthase.
REFERENCE   1  [PMID:6749502]
  AUTHORS   Lill U, Schreil A, Eggerer H.
  TITLE     Isolation of enzymically active fragments formed by limited
            proteolysis of ATP citrate lyase.
  JOURNAL   Eur. J. Biochem. 125 (1982) 645-50.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:15101981]
  AUTHORS   Aoshima M, Ishii M, Igarashi Y.
  TITLE     A novel enzyme, citryl-CoA synthetase, catalysing the first step of
            the citrate cleavage reaction in Hydrogenobacter thermophilus TK-6.
  JOURNAL   Mol. Microbiol. 52 (2004) 751-61.
  ORGANISM  Hydrogenobacter thermophilus
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.18
            ExPASy - ENZYME nomenclature database: 6.2.1.18
            ExplorEnz - The Enzyme Database: 6.2.1.18
            ERGO genome analysis and discovery system: 6.2.1.18
            BRENDA, the Enzyme Database: 6.2.1.18
            CAS: 856428-87-0
///
ENTRY       EC 6.2.1.19                 Enzyme
NAME        long-chain-fatty-acid---luciferin-component ligase;
            acyl-protein synthetase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     long-chain-fatty-acid:protein ligase (AMP-forming)
REACTION    ATP + an acid + protein = AMP + diphosphate + an acyl-protein
            thioester [RN:R01407]
ALL_REAC    R01407
SUBSTRATE   ATP [CPD:C00002];
            acid [CPD:C00174];
            protein [CPD:C00017]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            acyl-protein thioester
COMMENT     Together with EC 1.2.1.50 long-chain-fatty-acyl-CoA reductase,
            enzyme forms a fatty acid reductase system that produces the
            substrate of EC 1.14.14.3 alkanal monooxygenase (FMN-linked), thus
            being a component of the bacterial luciferase system.
REFERENCE   1  [PMID:7085612]
  AUTHORS   Riendeau D, Rodriguez A, Meighen E.
  TITLE     Resolution of the fatty acid reductase from Photobacterium
            phosphoreum into acyl protein synthetase and acyl-CoA reductase
            activities. Evidence for an enzyme complex.
  JOURNAL   J. Biol. Chem. 257 (1982) 6908-15.
  ORGANISM  Photobacterium phosphoreum
REFERENCE   2
  AUTHORS   Wall, L. and Meighen, E.A.
  TITLE     Subunit structure of the fatty-acid reductase complex from
            Photobacterium phosphoreum.
  JOURNAL   Biochemistry 25 (1986) 4315-4321.
  ORGANISM  Photobacterium phosphoreum
ORTHOLOGY   KO: K06046  
GENES       VFI: VFA0919
            PEN: PSEEN0621
            CVI: CV_4318(luxE)
            CKL: CKL_3025
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.19
            ExPASy - ENZYME nomenclature database: 6.2.1.19
            ExplorEnz - The Enzyme Database: 6.2.1.19
            ERGO genome analysis and discovery system: 6.2.1.19
            BRENDA, the Enzyme Database: 6.2.1.19
            CAS: 82657-98-5
///
ENTRY       EC 6.2.1.20                 Enzyme
NAME        long-chain-fatty-acid---[acyl-carrier-protein] ligase;
            acyl-[acyl-carrier-protein] synthetase;
            acyl-[acyl carrier protein] synthetase;
            acyl-ACP synthetase;
            acyl-[acyl-carrier-protein]synthetase;
            stearoyl-ACP synthetase;
            acyl-acyl carrier protein synthetase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     long-chain-fatty-acid:[acyl-carrier-protein] ligase (AMP-forming)
REACTION    ATP + an acid + [acyl-carrier-protein] = AMP + diphosphate +
            acyl-[acyl-carrier-protein] [RN:R07325]
ALL_REAC    R07325 > R01406
SUBSTRATE   ATP [CPD:C00002];
            acid [CPD:C00174];
            [acyl-carrier-protein]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            acyl-[acyl-carrier-protein]
COMMENT     Not identical with EC 6.2.1.3 long-chain-fatty-acid---CoA ligase.
REFERENCE   1  [PMID:794875]
  AUTHORS   Ray TK, Cronan JE Jr.
  TITLE     Activation of long chain fatty acids with acyl carrier protein:
            demonstration of a new enzyme, acyl-acyl carrier protein synthetase,
            in Escherichia coli.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 73 (1976) 4374-8.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00071  Fatty acid metabolism
ORTHOLOGY   KO: K01909  long-chain-fatty-acid--[acyl-carrier-protein] ligase
GENES       ECO: b2836(aas)
            ECJ: JW2804(aas)
            ECE: Z4154(aas)
            ECS: ECs3693
            ECC: c3431(aas)
            ECI: UTI89_C3240(aas)
            ECP: ECP_2849
            ECV: APECO1_3670(aas)
            ECW: EcE24377A_3156(aas)
            ECX: EcHS_A2983
            STY: STY3153(aas)
            STT: t2919(aas)
            SPT: SPA2875(aas)
            SEC: SC2949(aas)
            STM: STM3010(aas)
            YPE: YPO0793(aas)
            YPK: y3181(aas)
            YPM: YP_2864(aas)
            YPA: YPA_0476
            YPN: YPN_2996 YPN_2997
            YPS: YPTB3042(aas)
            YPI: YpsIP31758_0975(aas)
            SFL: SF2846(aas)
            SFX: S3044(aas)
            SFV: SFV_2914(aas)
            SSN: SSON_2996(aas)
            SBO: SBO_2728(aas)
            SDY: SDY_3053(aas)
            ECA: ECA3641(aas)
            PLU: plu1246(aas)
            XCV: XCV0541
            PSP: PSPPH_1569(aas)
            LPN: lpg0597(aas)
            LPF: lpl0631
            LPP: lpp0647
            TCX: Tcr_0070
            NEU: NE2424 NE2425
            AZO: azo0150(aas)
            DAR: Daro_0402
            HHE: HH0306
            CJE: Cj0938c(aas)
            CJR: CJE1016(aas)
            CJU: C8J_0881(aas)
            SUN: SUN_1164
            GSU: GSU3029
            GME: Gmet_0086
            PCA: Pcar_2776
            RPR: RP620(aas)
            RTY: RT0611(aas)
            RCO: RC0962(aas)
            RFE: RF_0417(aas)
            RBE: RBE_0465(aas)
            RAK: A1C_04865
            RBO: A1I_05365
            RCM: A1E_01675
            RRI: A1G_05280
            OTS: OTBS_1706(aas)
            MLO: mlr5451
            RET: RHE_CH01022(aas)
            BJA: bll2324
            BRA: BRADO5289
            BBT: BBta_5738
            CCR: CC_1733
            MMR: Mmar10_1427
            HNE: HNE_2022(aas)
            GBE: GbCGDNIH1_2359
            MAG: amb2972
            RBA: RB6533(aas)
            CTR: CT776(aas)
            CTA: CTA_0846(aas)
            CMU: TC0157
            CPN: CPn0922(aas)
            CPA: CP0944
            CPJ: CPj0922(aas)
            CPT: CpB0954
            CCA: CCA00847
            CAB: CAB812
            CFE: CF0169(aas)
            PCU: pc1236(aas)
            AAE: aq_2058(aas)
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.20
            ExPASy - ENZYME nomenclature database: 6.2.1.20
            ExplorEnz - The Enzyme Database: 6.2.1.20
            ERGO genome analysis and discovery system: 6.2.1.20
            BRENDA, the Enzyme Database: 6.2.1.20
            CAS: 77322-37-3
///
ENTRY       EC 6.2.1.21       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
COMMENT     Deleted entry: phenylacetate-CoA ligase. Activity covered by EC
            6.2.1.30, phenylacetate-CoA ligase (EC 6.2.1.21 created 1986,
            deleted 2001)
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.21
            ExPASy - ENZYME nomenclature database: 6.2.1.21
            ExplorEnz - The Enzyme Database: 6.2.1.21
            ERGO genome analysis and discovery system: 6.2.1.21
            BRENDA, the Enzyme Database: 6.2.1.21
///
ENTRY       EC 6.2.1.22                 Enzyme
NAME        [citrate (pro-3S)-lyase] ligase;
            citrate lyase ligase;
            citrate lyase synthetase;
            acetate: SH-[acyl-carrier-protein] enzyme ligase (AMP);
            acetate:HS-citrate lyase ligase;
            acetate:citrate-(pro-3S)-lyase(thiol-form) ligase (AMP-forming)
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     acetate:[citrate-(pro-3S)-lyase](thiol-form) ligase (AMP-forming)
REACTION    ATP + acetate + [citrate (pro-3S)-lyase](thiol form) = AMP +
            diphosphate + [citrate (pro-3S)-lyase](acetyl form) [RN:R04449]
ALL_REAC    R04449
SUBSTRATE   ATP [CPD:C00002];
            acetate [CPD:C00033];
            [citrate (pro-3S)-lyase](thiol form) [CPD:C04298]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            [citrate (pro-3S)-lyase](acetyl form) [CPD:C04334]
COMMENT     Both this enzyme and EC 2.3.1.49,deacetyl-[citrate-(pro-3S)-lyase]
            S-acetyltransferase, acetylate and activate EC 4.1.3.6, citrate
            (pro-3S)-lyase.
REFERENCE   1  [PMID:7128585]
  AUTHORS   Antranikian G, Gottschalk G.
  TITLE     Copurification of citrate lyase and citrate lyase ligase from
            Rhodopseudomonas gelatinosa and subsequent separation of the two
            enzymes.
  JOURNAL   Eur. J. Biochem. 126 (1982) 43-7.
  ORGANISM  Rhodopseudomonas gelatinosa
REFERENCE   2  [PMID:3935436]
  AUTHORS   Antranikian G, Herzberg C, Gottschalk G.
  TITLE     Covalent modification of citrate lyase ligase from Clostridium
            sphenoides by phosphorylation/dephosphorylation.
  JOURNAL   Eur. J. Biochem. 153 (1985) 413-20.
  ORGANISM  Clostridium sphenoides
REFERENCE   3  [PMID:3994485]
  AUTHORS   Quentmeier A, Antranikian G.
  TITLE     Characterization of citrate lyase from Clostridium sporosphaeroides.
  JOURNAL   Arch. Microbiol. 141 (1985) 85-90.
  ORGANISM  Clostridium sporosphaeroides
REFERENCE   4  [PMID:4365579]
  AUTHORS   Schmellenkamp H, Eggerer H.
  TITLE     Mechanism of enzymic acetylation of des-acetyl citrate lyase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 71 (1974) 1987-91.
  ORGANISM  Klebsiella aerogenes
PATHWAY     PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K01910  [citrate (pro-3S)-lyase] ligase
GENES       ECO: b0618(citC)
            ECJ: JW0610(citC)
            ECE: Z0762(citC)
            ECS: ECs0657
            ECC: c0709(citC)
            ECI: UTI89_C0622(citC)
            ECP: ECP_0649
            ECV: APECO1_1434(citC)
            ECX: EcHS_A0669(citC)
            STY: STY0067(citC2) STY0673(citC)
            STT: t0060(citC) t2243(citC)
            SPT: SPA0059(citC) SPA2110(citC)
            SEC: SC0052(citC2) SC0653(citC)
            STM: STM0058(citC2) STM0624(citC)
            YEN: YE2653(citC)
            SFL: SF0535(citC)
            SFX: S0542(citC)
            SBO: SBO_0483(citC)
            ECA: ECA2574(citC)
            ENT: Ent638_3375
            SPE: Spro_3171
            HIT: NTHI0032(citC)
            HDU: HD1240(citC)
            ASU: Asuc_0305
            VCH: VC0796
            VCO: VC0395_A0323(citC)
            PPR: PBPRA2295
            RFR: Rfer_2410
            PPD: Ppro_1088
            RPE: RPE_3427
            LLA: L0038(citC)
            SPY: SPy_1192(citC)
            SPZ: M5005_Spy_0910(citC)
            SPM: spyM18_1143(citC)
            SPG: SpyM3_0837(citC)
            SPS: SPs1037
            SPH: MGAS10270_Spy1024(citC)
            SPI: MGAS10750_Spy1060(citC)
            SPJ: MGAS2096_Spy0969(citC)
            SPK: MGAS9429_Spy1012(citC)
            SPF: SpyM50887(citC)
            SPA: M6_Spy0899
            SPB: M28_Spy0883(citC)
            SMU: SMU.1010(citC)
            LPL: lp_1106(citC)
            LAC: LBA0914(citC)
            LSA: LSA1227(citC)
            LCA: LSEI_1860
            EFA: EF3322(citC)
            OOE: OEOE_0420
            CPE: CPE1146(citC)
            CPR: CPR_1162(citC)
            CTC: CTC02557(citC)
            AMT: Amet_2958
            FNU: FN0319
            TDE: TDE1522(citC)
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.22
            ExPASy - ENZYME nomenclature database: 6.2.1.22
            ExplorEnz - The Enzyme Database: 6.2.1.22
            ERGO genome analysis and discovery system: 6.2.1.22
            BRENDA, the Enzyme Database: 6.2.1.22
            CAS: 52660-22-7
///
ENTRY       EC 6.2.1.23                 Enzyme
NAME        dicarboxylate---CoA ligase;
            carboxylyl-CoA synthetase;
            dicarboxylyl-CoA synthetase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     omega-dicarboxylate:CoA ligase (AMP-forming)
REACTION    ATP + an alphaomega-dicarboxylic acid + CoA = AMP + diphosphate + an
            omega-carboxyacyl-CoA [RN:R04157]
ALL_REAC    R04157
SUBSTRATE   ATP [CPD:C00002];
            alphaomega-dicarboxylic acid;
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            omega-carboxyacyl-CoA [CPD:C03188]
COMMENT     Acts on dicarboxylic acids of chain length C5 to C16; the best
            substrate is dodecanedioic acid.
REFERENCE   1  [PMID:4062873]
  AUTHORS   Vamecq J, de Hoffmann E, Van Hoof F.
  TITLE     The microsomal dicarboxylyl-CoA synthetase.
  JOURNAL   Biochem. J. 230 (1985) 683-93.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.23
            ExPASy - ENZYME nomenclature database: 6.2.1.23
            ExplorEnz - The Enzyme Database: 6.2.1.23
            ERGO genome analysis and discovery system: 6.2.1.23
            BRENDA, the Enzyme Database: 6.2.1.23
            CAS: 99332-77-1
///
ENTRY       EC 6.2.1.24                 Enzyme
NAME        phytanate---CoA ligase;
            phytanoyl-CoA ligase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     phytanate:CoA ligase (AMP-forming)
REACTION    ATP + phytanate + CoA = AMP + diphosphate + phytanoyl-CoA
            [RN:R03631]
ALL_REAC    R03631
SUBSTRATE   ATP [CPD:C00002];
            phytanate [CPD:C01607];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            phytanoyl-CoA [CPD:C02060]
COMMENT     Not identical with EC 6.2.1.20
            long-chain-fatty-acid---[acyl-carrier-protein] ligase.
REFERENCE   1  [PMID:3753503]
  AUTHORS   Muralidharan FN, Muralidharan VB.
  TITLE     Phytanoyl-CoA ligase activity in rat liver.
  JOURNAL   Biochem. Int. 13 (1986) 123-30.
  ORGANISM  rat [GN:rno]
GENES       AZO: azo3052(bzdA)
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.24
            ExPASy - ENZYME nomenclature database: 6.2.1.24
            ExplorEnz - The Enzyme Database: 6.2.1.24
            ERGO genome analysis and discovery system: 6.2.1.24
            BRENDA, the Enzyme Database: 6.2.1.24
            CAS: 105238-50-4
///
ENTRY       EC 6.2.1.25                 Enzyme
NAME        benzoate---CoA ligase;
            benzoate---coenzyme A ligase;
            benzoyl-coenzyme A synthetase;
            benzoyl CoA synthetase (AMP forming)
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     benzoate:CoA ligase (AMP-forming)
REACTION    ATP + benzoate + CoA = AMP + diphosphate + benzoyl-CoA [RN:R01422]
ALL_REAC    R01422
SUBSTRATE   ATP [CPD:C00002];
            benzoate [CPD:C00180];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            benzoyl-CoA [CPD:C00512]
COMMENT     Also acts on 2-, 3- and 4-fluorobenzoate, but only very slowly on
            the corresponding chlorobenzoates.
REFERENCE   1
  AUTHORS   Hutber, G.N. and Ribbons, D.W.
  TITLE     Involvement of coenzyme-A esters in the metabolism of benzoate and
            cyclohexanecarboxylate by Rhodopseudomonas palustris.
  JOURNAL   J. Gen. Microbiol. 129 (1983) 2413-2420.
  ORGANISM  Rhodopseudomonas palustris
REFERENCE   2  [PMID:2857161]
  AUTHORS   Schennen U, Braun K, Knackmuss HJ.
  TITLE     Anaerobic degradation of 2-fluorobenzoate by benzoate-degrading,
            denitrifying bacteria.
  JOURNAL   J. Bacteriol. 161 (1985) 321-5.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
ORTHOLOGY   KO: K04110  benzoate-CoA ligase
GENES       REU: Reut_A1327
            REH: H16_A1412 H16_B1918
            RME: Rmet_1224
            BXE: Bxe_A1419 Bxe_C0896
            RFR: Rfer_0216
            POL: Bpro_1624 Bpro_2983
            EBA: ebA2757(bclA) ebA5301(bclA)
            GME: Gmet_2143
            SAT: SYN_02896 SYN_02898
            BBT: BBta_6637(badA)
            RPA: RPA0661(badA)
            RPC: RPC_1025
            RPD: RPD_1534
            RPE: RPE_0592 RPE_0604
            SIL: SPO3697(badA-1) SPOA0401(badA-2)
STRUCTURES  PDB: 2V7B  
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.25
            ExPASy - ENZYME nomenclature database: 6.2.1.25
            ExplorEnz - The Enzyme Database: 6.2.1.25
            ERGO genome analysis and discovery system: 6.2.1.25
            UM-BBD (Biocatalysis/Biodegradation Database): 6.2.1.25
            BRENDA, the Enzyme Database: 6.2.1.25
            CAS: 95329-17-2
///
ENTRY       EC 6.2.1.26                 Enzyme
NAME        o-succinylbenzoate---CoA ligase;
            o-succinylbenzoyl-coenzyme A synthetase;
            o-succinylbenzoate:CoA ligase (AMP-forming)
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     2-succinylbenzoate:CoA ligase (AMP-forming)
REACTION    ATP + 2-succinylbenzoate + CoA = AMP + diphosphate +
            2-succinylbenzoyl-CoA [RN:R04030]
ALL_REAC    R04030
SUBSTRATE   ATP [CPD:C00002];
            2-succinylbenzoate [CPD:C02730];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            2-succinylbenzoyl-CoA [CPD:C03160]
REFERENCE   1  [PMID:7045104]
  AUTHORS   Heide L, Arendt S, Leistner E.
  TITLE     Enzymatic synthesis, characterization, and metabolism of the
            coenzyme A ester of o-succinylbenzoic acid, an intermediate in
            menaquinone (vitamin K2) biosynthesis.
  JOURNAL   J. Biol. Chem. 257 (1982) 7396-400.
  ORGANISM  Mycobacterium phlei, Escherichia coli [GN:eco]
REFERENCE   2  [PMID:2966501]
  AUTHORS   Kolkmann R, Leistner E.
  TITLE     4-(2'-Carboxyphenyl)-4-oxobutyryl coenzyme A ester, an intermediate
            in vitamin K2 (menaquinone) biosynthesis.
  JOURNAL   Z. Naturforsch. [C]. 42 (1987) 1207-14.
REFERENCE   3  [PMID:500558]
  AUTHORS   Meganathan R, Bentley R.
  TITLE     Menaquinone (vitamin K2) biosynthesis: conversion of
            o-succinylbenzoic acid to 1,4-dihydroxy-2-naphthoic acid by
            Mycobacterium phlei enzymes.
  JOURNAL   J. Bacteriol. 140 (1979) 92-8.
  ORGANISM  Mycobacterium phlei
PATHWAY     PATH: map00130  Ubiquinone biosynthesis
ORTHOLOGY   KO: K01911  O-succinylbenzoic acid--CoA ligase
GENES       TET: TTHERM_00158450
            ECO: b2260(menE)
            ECJ: JW2255(menE)
            ECE: Z3520(menE)
            ECS: ECs3148
            ECC: c2803(menE)
            ECI: UTI89_C2543(menE)
            ECP: ECP_2304
            ECV: APECO1_4301(menE)
            ECW: EcE24377A_2556(menE)
            ECX: EcHS_A2406
            STY: STY2535(menE)
            STT: t0558(menE)
            SPT: SPA0558(menE)
            SEC: SC2305(menE)
            STM: STM2305(menE)
            YPE: YPO2523(menE)
            YPK: y1664(menE)
            YPM: YP_2334(caiC)
            YPA: YPA_2015
            YPN: YPN_2118
            YPS: YPTB2556(menE)
            YPI: YpsIP31758_1486(menE)
            SFL: SF2339(menE)
            SFX: S2473(menE)
            SFV: SFV_2331(menE)
            SSN: SSON_2321(menE)
            SBO: SBO_2297(menE)
            SDY: SDY_2456(menE)
            ECA: ECA1215(menE)
            PLU: plu3069(menE)
            HIN: HI0194(menE)
            HIT: NTHI0290(menE)
            HDU: HD1271(menE)
            HSO: HS_1207(menE)
            PMU: PM0357(menE)
            MSU: MS0864(caiC)
            APL: APL_0751(menE)
            VCH: VC1971
            VCO: VC0395_A1557(menE)
            VVU: VV1_3168
            VVY: VV1120
            VPA: VP0933
            VFI: VF1666
            PPR: PBPRA2621
            SON: SO_4576
            SFR: Sfri_0279
            SHE: Shewmr4_3770
            SHM: Shewmr7_3843
            SHN: Shewana3_3968
            AHA: AHA_0527(menE)
            BUR: Bcep18194_A3290 Bcep18194_A3296 Bcep18194_A5208
                 Bcep18194_A5890 Bcep18194_A6091 Bcep18194_B1388
                 Bcep18194_B1417 Bcep18194_B1724 Bcep18194_B2485
                 Bcep18194_B3048 Bcep18194_C6698 Bcep18194_C6739
                 Bcep18194_C6849 Bcep18194_C6898 Bcep18194_C7114
                 Bcep18194_C7121 Bcep18194_C7124 Bcep18194_C7294
                 Bcep18194_C7411
            BAM: Bamb_0099 Bamb_1895
            RFR: Rfer_1017
            DAR: Daro_2822
            LIP: LI0806(menE)
            BBA: Bd0548(menE)
            DPS: DP0250(menE)
            MXA: MXAN_3532(menE)
            SAT: SYN_02620
            RLE: pRL120504(fcs)
            BJA: blr4049
            BRA: BRADO0229 BRADO0963 BRADO2317 BRADO3141 BRADO3743 BRADO4017
                 BRADO6291 BRADO6882
            BBT: BBta_0226 BBta_0667 BBta_0674 BBta_3237 BBta_3258 BBta_3582
                 BBta_3772 BBta_4389 BBta_7092
            RPE: RPE_3218
            NWI: Nwi_2300 Nwi_2797
            RDE: RD1_3974
            RRU: Rru_A1316 Rru_A1658 Rru_A2517 Rru_A3134
            BSU: BG10687(menE)
            BAN: BA5108
            BAR: GBAA5108
            BAA: BA_5526
            BAT: BAS4747
            BCE: BC4851
            BCA: BCE_5012
            BCZ: BCZK4607(menE)
            BTK: BT9727_4585(menE)
            BTL: BALH_4418(menE)
            BLI: BL02405(menE)
            BLD: BLi03219(menE)
            BAY: RBAM_022050 RBAM_027770
            BPU: BPUM_2715
            OIH: OB2322(menE)
            GKA: GK2872
            SAU: SA1615(menE)
            SAV: SAV1797(menE)
            SAM: MW1735(menE)
            SAR: SAR1877
            SAS: SAS1717
            SAC: SACOL1844
            SAB: SAB1651c
            SAA: SAUSA300_1737(menE)
            SAO: SAOUHSC_01916
            SEP: SE1464
            SER: SERP1358(menE)
            SHA: SH1132(menE)
            SSP: SSP0970
            LMO: lmo1672(menE)
            LMF: LMOf2365_1696(menE)
            LIN: lin1780(menE)
            LWE: lwe1690(menE)
            LLA: L0172(menE)
            LLC: LACR_0770
            LLM: llmg_1832(menE)
            LSL: LSL_0175(menE)
            LBR: LVIS_0067
            EFA: EF0446
            OOE: OEOE_0280
            DSY: DSY0521(menE)
            MTA: Moth_1261
            MTU: Rv0542c(menE)
            MTC: MT0567(menE)
            MBO: Mb0556c(menE)
            MBB: BCG_0586c(menE)
            MLE: ML2257(menE)
            MPA: MAP4038c(menE)
            MSM: MSMEG_1062
            CGL: NCgl0435(cgl0450)
            CGB: cg0533(menE)
            CEF: CE0471
            CDI: DIP0420
            CJK: jk1876(menE)
            NFA: nfa51420(menE)
            RHA: RHA1_ro00189 RHA1_ro00416 RHA1_ro02397 RHA1_ro02518
                 RHA1_ro03947 RHA1_ro03962 RHA1_ro05260 RHA1_ro06398
            TWH: TWT111(menE)
            TWS: TW121(menE)
            LXX: Lxx01450(menE)
            CMI: CMM_0577(menE)
            AAU: AAur_0966(menE) AAur_3276(menE)
            PAC: PPA0906
            TFU: Tfu_1408
            FAL: FRAAL1950 FRAAL2631 FRAAL3087 FRAAL3399 FRAAL3485 FRAAL4871
                 FRAAL6539
            SEN: SACE_0019 SACE_6916(menE)
            RXY: Rxyl_2891
            PCU: pc1062(menE)
            SYN: slr0492(menE)
            SYW: SYNW2305(menE)
            SYC: syc0525_c(menE)
            SYF: Synpcc7942_1021
            SYD: Syncc9605_2436
            SYE: Syncc9902_2117
            SYG: sync_2653
            SYR: SynRCC307_2255(menE)
            SYX: SynWH7803_2316(menE)
            CYA: CYA_2666(menE)
            CYB: CYB_2428(menE)
            TEL: tll1221(menE)
            ANA: alr0035(menE)
            AVA: Ava_2636 Ava_3987
            PMA: Pro0199(menE)
            PMM: PMM0174(menE)
            PMT: PMT2057(menE)
            PMN: PMN2A_1542
            PMI: PMT9312_0176
            PMB: A9601_01921(menE) A9601_01931(menC)
            PMC: P9515_02031(menE) P9515_02041(menC)
            PMF: P9303_27321(menE) P9303_27331(menC)
            PMG: P9301_01941(menE) P9301_01951(menC)
            PME: NATL1_02491(menE) NATL1_02501(menC)
            TER: Tery_4067
            BTH: BT_4704
            BFR: BF1321
            BFS: BF1305(menE)
            PGI: PG1521
            SRU: SRU_1355(menE)
            CHU: CHU_1877(menE)
            GFO: GFO_2306(menE)
            FPS: FP1601(menE)
            CTE: CT1848(menE)
            CCH: Cag_0982 Cag_1672
            PLT: Plut_0326
            MSI: Msm_0374
            HMA: rrnAC0843(menE)
            HWA: HQ2402A(menE)
            NPH: NP2738A(menE)
STRUCTURES  PDB: 2OKT  2OLA  
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.26
            ExPASy - ENZYME nomenclature database: 6.2.1.26
            ExplorEnz - The Enzyme Database: 6.2.1.26
            ERGO genome analysis and discovery system: 6.2.1.26
            BRENDA, the Enzyme Database: 6.2.1.26
            CAS: 72506-70-8
///
ENTRY       EC 6.2.1.27                 Enzyme
NAME        4-hydroxybenzoate---CoA ligase;
            4-hydroxybenzoate-CoA synthetase;
            4-hydroxybenzoate---coenzyme A ligase (AMP-forming);
            4-hydroxybenzoyl coenzyme A synthetase;
            4-hydroxybenzoyl-CoA ligase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     4-hydroxybenzoate:CoA ligase (AMP-forming)
REACTION    ATP + 4-hydroxybenzoate + CoA = AMP + diphosphate +
            4-hydroxybenzoyl-CoA [RN:R01300]
ALL_REAC    R01300
SUBSTRATE   ATP [CPD:C00002];
            4-hydroxybenzoate [CPD:C00156];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            4-hydroxybenzoyl-CoA [CPD:C02949]
REFERENCE   1  [PMID:2914844]
  AUTHORS   Merkel SM, Eberhard AE, Gibson J, Harwood CS.
  TITLE     Involvement of coenzyme A thioesters in anaerobic metabolism of
            4-hydroxybenzoate by Rhodopseudomonas palustris.
  JOURNAL   J. Bacteriol. 171 (1989) 1-7.
  ORGANISM  Rhodopseudomonas palustris
PATHWAY     PATH: map00632  Benzoate degradation via CoA ligation
ORTHOLOGY   KO: K04105  4-hydroxybenzoate-CoA ligase
GENES       SAT: SYN_02896 SYN_02898
            RPA: RPA0669(hbaA)
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.27
            ExPASy - ENZYME nomenclature database: 6.2.1.27
            ExplorEnz - The Enzyme Database: 6.2.1.27
            ERGO genome analysis and discovery system: 6.2.1.27
            UM-BBD (Biocatalysis/Biodegradation Database): 6.2.1.27
            BRENDA, the Enzyme Database: 6.2.1.27
            CAS: 119699-80-8
///
ENTRY       EC 6.2.1.28                 Enzyme
NAME        3alpha,7alpha-dihydroxy-5beta-cholestanate---CoA ligase;
            3alpha,7alpha-dihydroxy-5beta-cholestanoyl coenzyme A synthetase;
            DHCA-CoA ligase;
            3alpha,7alpha-dihydroxy-5beta-cholestanate:CoA ligase (AMP-forming)
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     (25R)-3alpha,7alpha-dihydroxy-5beta-cholestan-26-oate:CoA ligase
            (AMP-forming)
REACTION    ATP + (25R)-3alpha,7alpha-dihydroxy-5beta-cholestan-26-oate + CoA =
            AMP + diphosphate +
            (25R)-3alpha,7alpha-dihydroxy-5beta-cholestanoyl-CoA [RN:R04507]
ALL_REAC    R04507
SUBSTRATE   ATP [CPD:C00002];
            (25R)-3alpha,7alpha-dihydroxy-5beta-cholestan-26-oate;
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            (25R)-3alpha,7alpha-dihydroxy-5beta-cholestanoyl-CoA
REFERENCE   1  [PMID:3183523]
  AUTHORS   Prydz K, Kase BF, Bjorkhem I, Pedersen JI.
  TITLE     Subcellular localization of 3 alpha, 7 alpha-dihydroxy- and 3
            alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoyl-coenzyme A
            ligase(s) in rat liver.
  JOURNAL   J. Lipid. Res. 29 (1988) 997-1004.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00120  Bile acid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.28
            ExPASy - ENZYME nomenclature database: 6.2.1.28
            ExplorEnz - The Enzyme Database: 6.2.1.28
            ERGO genome analysis and discovery system: 6.2.1.28
            BRENDA, the Enzyme Database: 6.2.1.28
            CAS: 118732-03-9
///
ENTRY       EC 6.2.1.29       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
COMMENT     Deleted entry:
            3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate-CoA ligase. The
            enzyme is identical to EC 6.2.1.7, cholate-CoA ligase (EC 6.2.1.29
            created 1992, deleted 2005)
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.29
            ExPASy - ENZYME nomenclature database: 6.2.1.29
            ExplorEnz - The Enzyme Database: 6.2.1.29
            ERGO genome analysis and discovery system: 6.2.1.29
            BRENDA, the Enzyme Database: 6.2.1.29
///
ENTRY       EC 6.2.1.30                 Enzyme
NAME        phenylacetate---CoA ligase;
            phenacyl coenzyme A synthetase;
            phenylacetyl-CoA ligase;
            PA-CoA ligase;
            phenylacetyl-CoA ligase (AMP-forming)
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     phenylacetate:CoA ligase (AMP-forming)
REACTION    ATP + phenylacetate + CoA = AMP + diphosphate + phenylacetyl-CoA
            [RN:R02539]
ALL_REAC    R02539;
            (other) R02699
SUBSTRATE   ATP [CPD:C00002];
            phenylacetate [CPD:C07086];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            phenylacetyl-CoA [CPD:C00582]
COMMENT     Also acts, more slowly, on acetate, propanoate and butanoate, but
            not on hydroxy derivatives of phenylacetate and related compounds.
REFERENCE   1  [PMID:2324116]
  AUTHORS   Martinez-Blanco H, Reglero A, Rodriguez-Aparicio LB, Luengo JM.
  TITLE     Purification and biochemical characterization of phenylacetyl-CoA
            ligase from Pseudomonas putida. A specific enzyme for the catabolism
            of phenylacetic acid.
  JOURNAL   J. Biol. Chem. 265 (1990) 7084-90.
  ORGANISM  Pseudomonas putida [GN:ppu]
PATHWAY     PATH: map00350  Tyrosine metabolism
            PATH: map00360  Phenylalanine metabolism
ORTHOLOGY   KO: K01912  phenylacetate-CoA ligase
GENES       ECO: b1398(paaK)
            ECJ: JW5218(paaK)
            ECW: EcE24377A_1584(paaF)
            ECX: EcHS_A1485
            SPE: Spro_3082
            VPA: VPA1147
            PPU: PP_3279(phaE)
            PPF: Pput_2480
            PFL: PFL_3132(paaF)
            PEN: PSEEN2796(paaF)
            SFR: Sfri_1837
            CPS: CPS_3411
            PAT: Patl_1512
            PIN: Ping_0660
            MCA: MCA1132
            NOC: Noc_1971
            HHA: Hhal_0070
            MMW: Mmwyl1_3096
            AHA: AHA_1267
            CVI: CV_3598
            RSO: RSc2875(paaK)
            REU: Reut_A3017 Reut_B3741
            REH: H16_A3313(paaL1) H16_B1357(paaL2)
            RME: Rmet_0220 Rmet_3165
            BMA: BMAA0539(paaK)
            BMV: BMASAVP1_0638(paaF)
            BML: BMA10299_0935(paaK)
            BMN: BMA10247_A1905(paaK)
            BXE: Bxe_A0466 Bxe_C0919
            BVI: Bcep1808_0516 Bcep1808_5068
            BUR: Bcep18194_A3626 Bcep18194_B1318
            BCN: Bcen_2566 Bcen_3839
            BCH: Bcen2424_0539 Bcen2424_4529
            BAM: Bamb_0444 Bamb_3959
            BPS: BPSL3045(paaA)
            BPM: BURPS1710b_3568(paaF)
            BPL: BURPS1106A_3577(paaF)
            BPD: BURPS668_3550(paaF)
            BTE: BTH_I2904(paaF-1) BTH_II1392(paaF-2)
            BPE: BP2675(paaK) BP3189
            BPA: BPP0223 BPP1681(paaK)
            BBR: BB0227 BB0753 BB3427(paaK)
            RFR: Rfer_3536
            POL: Bpro_0598
            VEI: Veis_3944
            MPT: Mpe_A0986
            EBA: ebA3545(paaK) ebA5402(padJ) ebA5727(paaK2)
            AZO: azo0303(paaK) azo2395(phaE) azo3441
            DAR: Daro_0255 Daro_3366
            GSU: GSU1737
            GME: Gmet_1825
            GUR: Gura_2124 Gura_2133
            PCA: Pcar_1320 Pcar_1569
            PPD: Ppro_1669 Ppro_1754
            DVU: DVU0489(paaK-1) DVU1615(paaK-2) DVU2735(paaK-3) DVU3253
            DVL: Dvul_0571 Dvul_1519 Dvul_2452
            DDE: Dde_0540 Dde_0836 Dde_0972 Dde_2084 Dde_3457
            LIP: LI0635(paaK)
            DPS: DP1266
            ADE: Adeh_0036 Adeh_0038
            AFW: Anae109_0039 Anae109_0041
            MXA: MXAN_0305
            SAT: SYN_01100 SYN_01195
            SFU: Sfum_0379 Sfum_0382 Sfum_1676 Sfum_1683
            BJA: blr2897(paaK) blr5969
            BRA: BRADO2524(paaK) BRADO5269
            BBT: BBta_2870(paaK) BBta_5720
            RPA: RPA1229 RPA1723(paaK)
            RPB: RPB_1237 RPB_3634
            RPC: RPC_0561 RPC_0683 RPC_0698
            RPD: RPD_1515 RPD_1829 RPD_3222 RPD_4008
            RPE: RPE_0981 RPE_0996 RPE_3181 RPE_3908
            NHA: Nham_0936
            XAU: Xaut_0901 Xaut_5019
            SIL: SPO0742(paaF) SPO3289
            SIT: TM1040_0121 TM1040_0440
            RSP: RSP_2273
            RSH: Rsph17029_3655
            JAN: Jann_0656 Jann_4001
            RDE: RD1_0710(paaK)
            PDE: Pden_4801
            HNE: HNE_1105
            SWI: Swit_1449
            ACR: Acry_0477
            RRU: Rru_A0790 Rru_A1976 Rru_A3504
            MAG: amb1245 amb2755 amb3594
            ABA: Acid345_3795
            BHA: BH0195(phaE)
            GKA: GK2045
            STH: STH702
            CTH: Cthe_0615 Cthe_2792
            CHY: CHY_0120(paaK1) CHY_0728(paaK2)
            DRM: Dred_2884 Dred_3190
            SWO: Swol_0815
            CSC: Csac_2051 Csac_2054 Csac_2114
            MTA: Moth_0513 Moth_0933 Moth_2278
            CEF: CE0663
            NFA: nfa21660
            RHA: RHA1_ro02854(paaF) RHA1_ro10301
            SCO: SCO7469(paaK)
            SMA: SAV1257(paaK)
            ART: Arth_3247
            AAU: AAur_3244(paaF)
            NCA: Noca_2129
            FAL: FRAAL3108
            SEN: SACE_1120(paaK-2) SACE_3542(paaK)
            RXY: Rxyl_1845 Rxyl_1851
            GVI: gll2007
            ANA: all2410
            AVA: Ava_0218
            BTH: BT_0428 BT_0571
            BFR: BF1693 BF2619
            BFS: BF1700(paaK2) BF2641(paaK1)
            CHU: CHU_2125(paaK)
            GFO: GFO_1652(paaK)
            FJO: Fjoh_1075
            CTE: CT0112(paaK)
            CPH: Cpha266_1968
            PLT: Plut_0066
            DET: DET1015(paaK)
            DEH: cbdb_A988
            DEB: DehaBAV1_0824 DehaBAV1_0902
            DRA: DR_A0256
            DGE: Dgeo_2409
            TTH: TTC0602
            TTJ: TTHA0966
            MMQ: MmarC5_0861 MmarC5_1360 MmarC5_1515
            MMZ: MmarC7_1160 MmarC7_1316 MmarC7_1742
            MVN: Mevan_1165 Mevan_1325 Mevan_1590
            MBU: Mbur_0207 Mbur_0339 Mbur_0760
            MTP: Mthe_0013 Mthe_0260 Mthe_0633
            MHU: Mhun_1624 Mhun_1625
            MEM: Memar_0749 Memar_0750
            MBN: Mboo_0169 Mboo_0709
            MSI: Msm_0387 Msm_1714
            HMA: rrnB0231(paaK2) rrnB0243(paaK1)
            RCI: LRC13(paaK-2) LRC14(paaK-3) LRC7(paaK-1)
            MSE: Msed_0388
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.30
            ExPASy - ENZYME nomenclature database: 6.2.1.30
            ExplorEnz - The Enzyme Database: 6.2.1.30
            ERGO genome analysis and discovery system: 6.2.1.30
            BRENDA, the Enzyme Database: 6.2.1.30
            CAS: 57219-71-3
///
ENTRY       EC 6.2.1.31                 Enzyme
NAME        2-furoate---CoA ligase;
            2-furoyl coenzyme A synthetase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     2-furoate:CoA ligase (AMP-forming)
REACTION    ATP + 2-furoate + CoA = AMP + diphosphate + 2-furoyl-CoA [RN:R02986]
ALL_REAC    R02986
SUBSTRATE   ATP [CPD:C00002];
            2-furoate [CPD:C01546];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            2-furoyl-CoA [CPD:C00845]
REFERENCE   1  [PMID:16347977]
  AUTHORS   Koenig K, Andreesen JR.
  TITLE     Molybdenum Involvement in Aerobic Degradation of 2-Furoic Acid by
            Pseudomonas putida Fu1.
  JOURNAL   Appl. Environ. Microbiol. 55 (1989) 1829-1834.
  ORGANISM  Pseudomonas putida [GN:ppu]
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.31
            ExPASy - ENZYME nomenclature database: 6.2.1.31
            ExplorEnz - The Enzyme Database: 6.2.1.31
            ERGO genome analysis and discovery system: 6.2.1.31
            BRENDA, the Enzyme Database: 6.2.1.31
            CAS: 122320-08-5
///
ENTRY       EC 6.2.1.32                 Enzyme
NAME        anthranilate---CoA ligase;
            anthraniloyl coenzyme A synthetase;
            2-aminobenzoate---CoA ligase;
            2-aminobenzoate---coenzyme A ligase;
            2-aminobenzoate coenzyme A ligase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     anthranilate:CoA ligase (AMP-forming)
REACTION    ATP + anthranilate + CoA = AMP + diphosphate + anthranilyl-CoA
            [RN:R00982]
ALL_REAC    R00982;
            (other) R07416
SUBSTRATE   ATP [CPD:C00002];
            anthranilate [CPD:C00108];
            CoA [CPD:C00010]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            anthranilyl-CoA [CPD:C02247]
REFERENCE   1  [PMID:2176602]
  AUTHORS   Altenschmidt U, Eckerskorn C, Fuchs G.
  TITLE     Evidence that enzymes of a novel aerobic 2-amino-benzoate metabolism
            in denitrifying Pseudomonas are coded on a small plasmid.
  JOURNAL   Eur. J. Biochem. 194 (1990) 647-53.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00629  Carbazole degradation
            PATH: map00632  Benzoate degradation via CoA ligation
            PATH: map01058  Acridone alkaloid biosynthesis
ORTHOLOGY   KO: K08295  2-aminobenzoate-CoA ligase
            KO: K09460  anthranilate-CoA ligase
GENES       RSO: RS02012(RSp0037)
            REU: Reut_A2180
            REH: H16_A2457(abmG)
            RME: Rmet_2198
            BXE: Bxe_B0275
            BPS: BPSS0481
            BPM: BURPS1710b_A2033
            BPL: BURPS1106A_A0653
            BPD: BURPS668_A0744
            BTE: BTH_II1935
            BPE: BP0311
            BPA: BPP3940
            BBR: BB4413
            POL: Bpro_0589
            SAT: SYN_02417
            RPE: RPE_3227
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.32
            ExPASy - ENZYME nomenclature database: 6.2.1.32
            ExplorEnz - The Enzyme Database: 6.2.1.32
            ERGO genome analysis and discovery system: 6.2.1.32
            UM-BBD (Biocatalysis/Biodegradation Database): 6.2.1.32
            BRENDA, the Enzyme Database: 6.2.1.32
            CAS: 112692-58-7
///
ENTRY       EC 6.2.1.33                 Enzyme
NAME        4-chlorobenzoate---CoA ligase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     4-chlorobenzoate:CoA ligase
REACTION    4-chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP +
            diphosphate [RN:R03932]
ALL_REAC    R03932
SUBSTRATE   4-chlorobenzoate [CPD:C02370];
            CoA [CPD:C00010];
            ATP [CPD:C00002]
PRODUCT     4-chlorobenzoyl-CoA [CPD:C06387];
            AMP [CPD:C00020];
            diphosphate [CPD:C00013]
COFACTOR    Magnesium [CPD:C00305]
COMMENT     Requires Mg2+. This enzyme is part of the bacterial
            2,4-dichlorobenzoate degradation pathway.
REFERENCE   1  [PMID:7765837]
  AUTHORS   Dunaway-Mariano D, Babbitt PC.
  TITLE     On the origins and functions of the enzymes of the 4-chlorobenzoate
            to 4-hydroxybenzoate converting pathway.
  JOURNAL   Biodegradation. 5 (1994) 259-76.
  ORGANISM  Pseudomonas sp.
REFERENCE   2  [PMID:1418673]
  AUTHORS   Loffler F, Muller R, Lingens F.
  TITLE     Purification and properties of 4-halobenzoate-coenzyme A ligase from
            Pseudomonas sp. CBS3.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 373 (1992) 1001-7.
  ORGANISM  Pseudomonas sp.
REFERENCE   3  [PMID:1610806]
  AUTHORS   Chang KH, Liang PH, Beck W, Scholten JD, Dunaway-Mariano D.
  TITLE     Isolation and characterization of the three polypeptide components
            of 4-chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS-3.
  JOURNAL   Biochemistry. 31 (1992) 5605-10.
  ORGANISM  Pseudomonas sp.
PATHWAY     PATH: map00623  2,4-Dichlorobenzoate degradation
STRUCTURES  PDB: 1T5D  1T5H  
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.33
            ExPASy - ENZYME nomenclature database: 6.2.1.33
            ExplorEnz - The Enzyme Database: 6.2.1.33
            ERGO genome analysis and discovery system: 6.2.1.33
            UM-BBD (Biocatalysis/Biodegradation Database): 6.2.1.33
            BRENDA, the Enzyme Database: 6.2.1.33
            CAS: 141583-20-2
///
ENTRY       EC 6.2.1.34                 Enzyme
NAME        trans-feruloyl-CoA synthase;
            trans-feruloyl-CoA synthetase
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid-thiol ligases
SYSNAME     trans-ferulate:CoASH ligase (ATP-hydrolysing)
REACTION    ferulic acid + CoASH + ATP = trans-feruloyl-CoA + products of ATP
            breakdown [RN:R05744]
ALL_REAC    R05744
SUBSTRATE   ferulic acid [CPD:C01494];
            CoASH;
            ATP [CPD:C00002]
PRODUCT     trans-feruloyl-CoA [CPD:C00406];
            products of ATP breakdown [CPD:C07305]
COMMENT     Requires Mg2+. It has not yet been established whether AMP +
            diphosphate or ADP + phosphate are formed in this reaction.
REFERENCE   1  [PMID:9611814]
  AUTHORS   Narbad A, Gasson MJ.
  TITLE     Metabolism of ferulic acid via vanillin using a novel CoA-dependent
            pathway in a newly-isolated strain of Pseudomonas fluorescens.
  JOURNAL   Microbiology. 144 ( Pt 5) (1998) 1397-405.
  ORGANISM  Pseudomonas fluorescens
REFERENCE   2  [PMID:6870241]
  AUTHORS   Pometto AL 3rd, Crawford DL.
  TITLE     Whole-cell bioconversion of vanillin to vanillic acid by
            Streptomyces viridosporus.
  JOURNAL   Appl. Environ. Microbiol. 45 (1983) 1582-5.
  ORGANISM  Streptomyces viridosporus
GENES       PSP: PSPPH_2435(fcs)
            BPL: BURPS1106A_4030(fcs)
            BPD: BURPS668_3956(fcs)
            HNE: HNE_3427(fcs5)
            SYG: sync_1471(fcs)
DBLINKS     IUBMB Enzyme Nomenclature: 6.2.1.34
            ExPASy - ENZYME nomenclature database: 6.2.1.34
            ExplorEnz - The Enzyme Database: 6.2.1.34
            ERGO genome analysis and discovery system: 6.2.1.34
            BRENDA, the Enzyme Database: 6.2.1.34
///
ENTRY       EC 6.2.1.-                  Enzyme
CLASS       Ligases;
            Forming carbon-sulfur bonds;
            Acid--thiol ligases
REACTION    (1) 3-Hydroxypropionyl-CoA + Orthophosphate + ADP <=>
            3-Hydroxypropanoate + CoA + ATP [RN:R03157];
            (2) CoA + ATP + 2,4-Dichlorobenzoate <=> Pyrophosphate +
            2,4-Dichlorobenzoyl-CoA + AMP [RN:R05451];
            (3) Benzoyl acetate + CoA + ATP <=> Pyrophosphate + Benzoyl
            acetyl-CoA + AMP [RN:R05452];
            (4) Cyclohexane-1-carboxylate + CoA + ATP <=>
            Cyclohexane-1-carboxyl-CoA + AMP + Pyrophosphate [RN:R05620];
            (5) Perillic acid + CoA + ATP <=> Perillyl-CoA + H2O + ADP +
            Orthophosphate [RN:R06367];
            (6) Perillic acid + CoA + ATP <=> Perillyl-CoA + H2O + AMP +
            Pyrophosphate [RN:R06368];
            (7) (3R)-3-Isopropenyl-6-oxoheptanoate + CoA + ATP <=>
            (3R)-3-Isopropenyl-6-oxoheptanoyl-CoA + H2O + ADP + Orthophosphate
            [RN:R06396];
            (8) (3S)-3-Isopropenyl-6-oxoheptanoate <=>
            (3S)-3-Isopropenyl-6-oxoheptanoyl-CoA [RN:R06397];
            (9) cis-2-Methyl-5-isopropylhexa-2,5-dienoic acid + ATP + CoA <=>
            cis-2-Methyl-5-isopropylhexa-2,5-dienoyl-CoA + AMP + Orthophosphate
            [RN:R06409];
            (10) trans-2-Methyl-5-isopropylhexa-2,5-dienoic acid + ATP + CoA <=>
            trans-2-Methyl-5-isopropylhexa-2,5-dienoyl-CoA + AMP +
            Orthophosphate [RN:R06410];
            (11) (3R)-3-Isopropenyl-6-oxoheptanoate + CoA + ATP <=>
            (3R)-3-Isopropenyl-6-oxoheptanoyl-CoA + H2O + AMP + Pyrophosphate
            [RN:R06515];
            (12) Pseudoecgonine + ATP + CoA <=> Pseudoecgonyl-CoA + AMP
            [RN:R06731];
            (13) Adipate + CoA + ATP <=> Adipyl-CoA + AMP + Pyrophosphate
            [RN:R06944];
            (14) Cyclopropanecarboxylate + CoA + ATP <=>
            Cyclopropanecarboxyl-CoA + ADP + Orthophosphate [RN:R07828];
            (15) ATP + 8-[(1R,2R)-3-Oxo-2-{(Z)-pent-2-enyl}cyclopentyl]octanoate
            + CoA <=> AMP + Pyrophosphate + OPC8-CoA [RN:R07887]
SUBSTRATE   3-Hydroxypropionyl-CoA [CPD:C05668];
            Orthophosphate [CPD:C00009];
            ADP [CPD:C00008];
            CoA [CPD:C00010];
            ATP [CPD:C00002];
            2,4-Dichlorobenzoate [CPD:C06670];
            Benzoyl acetate [CPD:C07114];
            Cyclohexane-1-carboxylate [CPD:C09822];
            Perillic acid [CPD:C11924];
            (3R)-3-Isopropenyl-6-oxoheptanoate [CPD:C11405];
            (3S)-3-Isopropenyl-6-oxoheptanoate [CPD:C11419];
            cis-2-Methyl-5-isopropylhexa-2,5-dienoic acid [CPD:C11944];
            trans-2-Methyl-5-isopropylhexa-2,5-dienoic acid [CPD:C11943];
            Pseudoecgonine [CPD:C12449];
            Adipate [CPD:C06104]
PRODUCT     3-Hydroxypropanoate [CPD:C01013];
            CoA [CPD:C00010];
            ATP [CPD:C00002];
            Pyrophosphate [CPD:C00013];
            2,4-Dichlorobenzoyl-CoA [CPD:C06671];
            AMP [CPD:C00020];
            Benzoyl acetyl-CoA [CPD:C07118];
            Cyclohexane-1-carboxyl-CoA [CPD:C09823];
            Perillyl-CoA [CPD:C11929];
            H2O [CPD:C00001];
            ADP [CPD:C00008];
            Orthophosphate [CPD:C00009];
            (3R)-3-Isopropenyl-6-oxoheptanoyl-CoA [CPD:C11407];
            (3S)-3-Isopropenyl-6-oxoheptanoyl-CoA [CPD:C11421];
            cis-2-Methyl-5-isopropylhexa-2,5-dienoyl-CoA [CPD:C11946];
            trans-2-Methyl-5-isopropylhexa-2,5-dienoyl-CoA [CPD:C11945];
            Pseudoecgonyl-CoA [CPD:C12450];
            Adipyl-CoA [CPD:C14143]
///
ENTRY       EC 6.3.1.1                  Enzyme
NAME        aspartate---ammonia ligase;
            asparagine synthetase;
            L-asparagine synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-ammonia (or amine) ligases (amide synthases)
SYSNAME     L-aspartate:ammonia ligase (AMP-forming)
REACTION    ATP + L-aspartate + NH3 = AMP + diphosphate + L-asparagine
            [RN:R00483]
ALL_REAC    R00483
SUBSTRATE   ATP [CPD:C00002];
            L-aspartate [CPD:C00049];
            NH3 [CPD:C00014]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-asparagine [CPD:C00152]
REFERENCE   1  [PMID:14490631]
  AUTHORS   RAVEL JM, NORTON SJ, HUMPHREYS JS, SHIVE W.
  TITLE     Asparagine biosynthesis in Lactobacillus arabinosus and its control
            by asparagine through enzyme inhibition and repression.
  JOURNAL   J. Biol. Chem. 237 (1962) 2845-9.
  ORGANISM  Lactobacillus arabinosus
REFERENCE   2
  AUTHORS   Webster, G.C. and Varner, J.E.
  TITLE     Aspartate metabolism and asparagine synthesis in plant systems.
  JOURNAL   J. Biol. Chem. 215 (1955) 91-99.
  ORGANISM  lupin, Triticum aestivum [GN:etae]
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
            PATH: map00460  Cyanoamino acid metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K01914  aspartate--ammonia ligase
GENES       CPV: cgd5_4540
            CHO: Chro.50501
            TBR: Tb927.7.1110
            TCR: 503625.10 503899.90
            LMA: LmjF26.0830
            EHI: 1.t00107
            ECO: b3744(asnA)
            ECJ: JW3722(asnA)
            ECE: Z5245(asnA)
            ECS: ECs4686
            ECC: c4672(asnA)
            ECI: UTI89_C4299(asnA)
            ECP: ECP_3943
            ECV: APECO1_2719(asnA)
            ECW: EcE24377A_4260(asnA)
            ECX: EcHS_A3960
            STY: STY3901(asnA)
            STT: t3642(asnA)
            SPT: SPA3716(asnA)
            SEC: SC3790(asnA)
            STM: STM3877(asnA)
            YPE: YPO0003(asnA)
            YPK: y0003(asnA)
            YPM: YP_0003(asnA)
            YPA: YPA_0003
            YPN: YPN_0003
            YPP: YPDSF_3902
            YPS: YPTB0003(asnA)
            YPI: YpsIP31758_0003(asnA)
            SFL: SF3824(asnA)
            SFX: S3944(asnA)
            SFV: SFV_3770(asnA)
            SSN: SSON_3875(asnA)
            SBO: SBO_3743(asnA)
            SDY: SDY_4004(asnA)
            ECA: ECA0003(asnA)
            PLU: plu0052(asnA)
            ENT: Ent638_4120
            SPE: Spro_4905
            HIT: NTHI0692(asnA)
            HIP: CGSHiEE_00160
            HIQ: CGSHiGG_06100
            HDU: HD1913(asnA)
            HSO: HS_1440(asnA)
            PMU: PM1574(asnA)
            MSU: MS0036(asnA)
            APL: APL_1837(asnA)
            ASU: Asuc_0503
            ILO: IL0693(asnA)
            PHA: PSHAa2796(asnA)
            AHA: AHA_4068(asnA)
            ABA: Acid345_0576
            SUS: Acid_6566
            BAN: BA1808(asnA)
            BAR: GBAA1808(asnA)
            BAA: BA_2311
            BAT: BAS1673
            BCE: BC1746
            BCA: BCE_1880(asnA)
            BCZ: BCZK1620(asnA)
            BCY: Bcer98_1427
            BTK: BT9727_1655(asnA)
            SPY: SPy_1539(asnA)
            SPZ: M5005_Spy_1269(asnA)
            SPM: spyM18_1556
            SPG: SpyM3_1190(asnA)
            SPS: SPs0672
            SPH: MGAS10270_Spy1284(asnA)
            SPI: MGAS10750_Spy1376(asnA)
            SPJ: MGAS2096_Spy1288(asnA)
            SPK: MGAS9429_Spy1263(asnA)
            SPF: SpyM50584(asnA)
            SPA: M6_Spy1290
            SPB: M28_Spy1207(asnA)
            SPN: SP_1970
            SPR: spr1785(asnA)
            SPD: SPD_1768(asnA)
            SAG: SAG0450(asnA)
            SAN: gbs0497
            SAK: SAK_0552(asnA)
            STC: str0377(asnA)
            STL: stu0377(asnA)
            LPL: lp_0957(asnA)
            LJO: LJ0511
            LAC: LBA1896(asnA)
            LSL: LSL_1033(asnA)
            LDB: Ldb1194(asnA)
            LBU: LBUL_1110
            LBR: LVIS_1649
            LRE: Lreu_1885
            CPE: CPE1978(asnA)
            CPF: CPF_2233(asnA)
            CPR: CPR_1945(asnA)
            CTC: CTC00781
            CNO: NT01CX_1288(asnA)
            CTH: Cthe_0069
            CDF: CD2695(asnA)
            CBO: CBO1504(asnA)
            CBA: CLB_1526(asnA)
            CBH: CLC_1538(asnA)
            CBF: CLI_1585(asnA)
            AMT: Amet_4660
            MPE: MYPE1480(asnA)
            MGA: MGA_0424(asnA)
            MMY: MSC_1015(asnA) MSC_1040(asnA)
            MSY: MS53_0338
            MCP: MCAP_0817(asnA)
            UUR: UU363(asnA)
            FNU: FN0776
            TPA: TP0556
            BTH: BT_2129
            BFR: BF3815
            BFS: BF3607(asnA)
STRUCTURES  PDB: 11AS  12AS  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.1.1
            ExPASy - ENZYME nomenclature database: 6.3.1.1
            ExplorEnz - The Enzyme Database: 6.3.1.1
            ERGO genome analysis and discovery system: 6.3.1.1
            BRENDA, the Enzyme Database: 6.3.1.1
            CAS: 9023-69-2
///
ENTRY       EC 6.3.1.2                  Enzyme
NAME        glutamate---ammonia ligase;
            glutamine synthetase;
            glutamylhydroxamic synthetase;
            L-glutamine synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-ammonia (or amine) ligases (amide synthases)
SYSNAME     L-glutamate:ammonia ligase (ADP-forming)
REACTION    ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine [RN:R00253]
ALL_REAC    R00253;
            (other) R05028 R05030 R05033
SUBSTRATE   ATP [CPD:C00002];
            L-glutamate [CPD:C00025];
            NH3 [CPD:C00014]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            L-glutamine [CPD:C00064]
INHIBITOR   L-Methionine sulfoximine [CPD:C03510];
            2S,5S-Methionine sulfoximine [CPD:C03829];
            3-(Phosphoacetylamido)-L-alanine [CPD:C04111];
            L-2-Amino-4-(hydroxymethylphosphinyl)butanoate [CPD:C04650]
COMMENT     Also acts, more slowly, on 4-methylene-L-glutamate (cf. EC 6.3.1.7
            4-methyleneglutamate---ammonia ligase).
REFERENCE   1  [PMID:13061404]
  AUTHORS   ELLIOTT WH.
  TITLE     Isolation of glutamine synthetase and glutamotransferase from green
            peas.
  JOURNAL   J. Biol. Chem. 201 (1953) 661-72.
  ORGANISM  Pisum sativum
REFERENCE   2  [PMID:14363150]
  AUTHORS   FRY BA.
  TITLE     Glutamine synthesis by Micrococcus pyogenes var. aureus.
  JOURNAL   Biochem. J. 59 (1955) 579-89.
  ORGANISM  Micrococcus pyogenes
REFERENCE   3  [PMID:13129232]
  AUTHORS   LAJTHA A, MELA P, WAELSCH H.
  TITLE     Manganese-dependent glutamotransferase.
  JOURNAL   J. Biol. Chem. 205 (1953) 553-64.
  ORGANISM  pigeon
REFERENCE   4
  AUTHORS   Meister, A.
  TITLE     Glutamine synthesis.
  JOURNAL   In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
            ed., vol. 6, Academic Press, New York, 1962, p. 443-468.
REFERENCE   5  [PMID:5336023]
  AUTHORS   Woolfolk CA, Shapiro B, Stadtman ER.
  TITLE     Regulation of glutamine synthetase. I. Purification and properties
            of glutamine synthetase from Escherichia coli.
  JOURNAL   Arch. Biochem. Biophys. 116 (1966) 177-92.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00550  Peptidoglycan biosynthesis
            PATH: map00910  Nitrogen metabolism
            PATH: map02020  Two-component system - General
ORTHOLOGY   KO: K01915  glutamine synthetase
GENES       HSA: 2752(GLUL)
            MMU: 14645(Glul)
            RNO: 24957(Glul)
            CFA: 403443(GLUL) 492081(LOC492081) 609703(LOC609703)
            BTA: 281199(GLUL)
            SSC: 396944(GLUL)
            GGA: 396489(GLUL)
            XLA: 380593(glul) 398556(xgs) 432308(MGC80056)
            XTR: 394915(MGC75673)
            DRE: 336473(glulb) 403046(GLUL) 494094(zgc:101551)
            SPU: 574926(LOC574926)
            DME: Dmel_CG15441(Gs1l) Dmel_CG1743(Gs2) Dmel_CG2718(Gs1)
            CEL: C28D4.3(gln-6) C45B2.5(gln-1) F26D10.10(gln-5) K03H1.1(gln-2)
                 Y105C5B.28(gln-3)
            ATH: AT1G48470(GLN1;5) AT3G17820(ATGSKB6) AT5G35630(GS2)
                 AT5G37600(ATGSR1)
            OSA: 4330649 4332108 4333896 4337272
            CME: CMI233C
            SCE: YPR035W(GLN1)
            AGO: AGOS_ACR182C
            PIC: PICST_68474(GLN1)
            CGR: CAGL0K05357g
            SPO: SPAC23H4.06
            ANI: AN4159.2 AN4819.2 AN6654.2
            AFM: AFUA_2G15390 AFUA_4G03710 AFUA_4G13120 AFUA_6G03530
            AOR: AO090009000269 AO090009000558 AO090011000136 AO090011000308
            CNE: CNA04370 CNA06870
            UMA: UM03527.1 UM05971.1
            DDI: DDB_0231551(glnB)
            PFA: PFI1110w
            CPV: cgd6_4570
            CHO: Chro.60524
            TET: TTHERM_01084100 TTHERM_01084110
            TBR: Tb927.7.4970
            TCR: 503405.10 508175.370
            LMA: LmjF06.0370
            EHI: 23.t00033 23.t00038 269.t00005 414.t00007 82.t00001
            ECO: b3870(glnA)
            ECJ: JW3841(glnA)
            ECE: Z5406(glnA)
            ECS: ECs4792
            ECC: c4819(glnA)
            ECI: UTI89_C4459(glnA)
            ECP: ECP_4081
            ECV: APECO1_2592(glnA)
            ECW: EcE24377A_4392(glnA)
            ECX: EcHS_A4097(glnA)
            STY: STY3874(glnA)
            STT: t3614(glnA)
            SPT: SPA3848(glnA)
            SEC: SC3899(glnA)
            STM: STM4007(glnA)
            YPE: YPO0024(glnA)
            YPK: y3804(glnA)
            YPM: YP_0025(glnA)
            YPA: YPA_3517
            YPN: YPN_0251
            YPP: YPDSF_3880
            YPS: YPTB0024(glnA)
            YPI: YpsIP31758_0027(glnA)
            YEN: YE0027(glnA)
            SFL: SF3940(glnA)
            SFX: S3806(glnA)
            SFV: SFV_3631(glnA)
            SSN: SSON_4042(glnA)
            SBO: SBO_3882(glnA)
            SDY: SDY_3873(glnA)
            ECA: ECA0029(glnA)
            PLU: plu0237(glnA)
            WBR: WGLp589(glnA)
            SGL: SG1902 SG2230
            ENT: Ent638_4096
            BFL: Bfl618(glnA)
            BPN: BPEN_643(glnA)
            HIT: NTHI1036(glnA)
            HDU: HD0750(glnA)
            HSO: HS_0418(glnA)
            PMU: PM1175(glnA)
            MSU: MS0262(glnA)
            APL: APL_1941(glnA)
            XFA: XF1842
            XFT: PD1026(glnA)
            XCC: XCC0185(glnA) XCC2346(glnA) XCC2348(glnA)
            XCB: XC_0194 XC_1768 XC_1770
            XCV: XCV0188(glnA) XCV2656(glnA2) XCV2658(glnA3)
            XAC: XAC0204(glnA) XAC2478(glnA) XAC2480(glnA)
            XOO: XOO1387 XOO2782(glnA) XOO2785(glnA) XOO4488(glnA)
            XOM: XOO_1273(XOO1273) XOO_2623(XOO2623) XOO_2625(XOO2625)
                 XOO_4228(XOO4228)
            VCH: VC2746
            VCO: VC0395_A2318(glnA)
            VVU: VV1_0889
            VVY: VV0199
            VPA: VP0121 VP1781
            VFI: VF0098(glnA)
            PPR: PBPRA3492
            PAE: PA0296 PA0298 PA1566 PA2040 PA3356 PA5119(glnA) PA5522
            PAU: PA14_03860 PA14_03880(spuB) PA14_20670 PA14_38140 PA14_44240
                 PA14_67600(glnA) PA14_72690 PA14_72850
            PAP: PSPA7_5853(glnA)
            PPU: PP_3148 PP_4399 PP_4547 PP_5046(glnA) PP_5183 PP_5184 PP_5299
            PST: PSPTO_0359(glnA-1) PSPTO_1921 PSPTO_5309 PSPTO_5310
            PSB: Psyr_2273 Psyr_3492 Psyr_4817 Psyr_4867 Psyr_4868
            PSP: PSPPH_2916(glnT) PSPPH_3419 PSPPH_4847(glnA) PSPPH_4897
                 PSPPH_4898
            PFL: PFL_0386(glnA) PFL_2341 PFL_2473 PFL_2952 PFL_4488 PFL_5928
                 PFL_5930
            PFO: Pfl_0344 Pfl_2122 Pfl_2143 Pfl_2828 Pfl_4259 Pfl_5407
                 Pfl_5408
            PEN: PSEEN0390(glnA) PSEEN2186 PSEEN2565 PSEEN2899 PSEEN3851
                 PSEEN3971 PSEEN5297 PSEEN5299 PSEEN5444
            PAR: Psyc_0975(glnA)
            PCR: Pcryo_1440
            ACI: ACIAD2458(glnA) ACIAD2528(glnT)
            SON: SO_1268 SO_4410(glnA)
            SDN: Sden_3032 Sden_3454
            SFR: Sfri_0325 Sfri_3011
            SAZ: Sama_1174 Sama_2644 Sama_3416
            SBL: Sbal_0306 Sbal_1107 Sbal_2233
            SLO: Shew_0972 Shew_3554
            SPC: Sputcn32_0412 Sputcn32_1093
            SHE: Shewmr4_0305 Shewmr4_2919
            SHM: Shewmr7_3001 Shewmr7_3719
            SHN: Shewana3_0300 Shewana3_1069 Shewana3_3098
            SHW: Sputw3181_0266 Sputw3181_3071
            ILO: IL2437(glnA)
            CPS: CPS_0400(glnA) CPS_4677
            PHA: PSHAa0166(glnA)
            PAT: Patl_1025 Patl_4201
            SDE: Sde_0502
            PIN: Ping_3484
            MAQ: Maqu_0769
            CBU: CBU_0503(glnA)
            CBD: COXBU7E912_1573(glnA)
            LPN: lpg1364(glnA) lpg2252
            LPF: lpl1315(glnA) lpl2178
            LPP: lpp1318(glnA) lpp2206
            MCA: MCA1677(glnA)
            FTU: FTT0196c(glnA)
            FTF: FTF0196c(glnA)
            FTW: FTW_1895
            FTL: FTL_1899
            FTH: FTH_1821(glnA)
            FTA: FTA_2006(glnA)
            FTN: FTN_0172(glnA)
            TCX: Tcr_0536 Tcr_1347 Tcr_1798
            NOC: Noc_2652
            AEH: Mlg_0013
            HHA: Hhal_1217 Hhal_1582
            HCH: HCH_01036(glnA) HCH_06321
            CSA: Csal_0243 Csal_0679 Csal_0777 Csal_1181 Csal_1192
            ABO: ABO_2262(glnA)
            AHA: AHA_0277(glnA) AHA_4140
            RMA: Rmag_0498
            VOK: COSY_0458(glnA)
            NME: NMB0359
            NMA: NMA2128(glnA)
            NMC: NMC1809(glnA)
            NGO: NGO1600
            CVI: CV_1448 CV_2024 CV_3589(glnA)
            RSO: RSp0886(glnA2)
            REH: H16_A2335(glnA1) H16_B0618(glnA2) H16_B2191(glnA3)
            RME: Rmet_2062
            BMA: BMA0656 BMA1743(glnA)
            BMV: BMASAVP1_A2253(glnA)
            BML: BMA10299_A3067(glnA)
            BMN: BMA10247_1524(glnA)
            BXE: Bxe_A1522 Bxe_B0942
            BVI: Bcep1808_2228 Bcep1808_2237 Bcep1808_3080 Bcep1808_6787
            BUR: Bcep18194_A5458 Bcep18194_A5473 Bcep18194_A6343
                 Bcep18194_B0804
            BCN: Bcen_2380 Bcen_3465 Bcen_5549 Bcen_5914 Bcen_5928
            BCH: Bcen2424_2149 Bcen2424_2163 Bcen2424_2994 Bcen2424_4901
                 Bcen2424_5914
            BAM: Bamb_2186 Bamb_2201 Bamb_3041
            BPS: BPSL2318(glnA) BPSL2336 BPSS0469
            BPM: BURPS1710b_2770(glnA) BURPS1710b_2788 BURPS1710b_A2022(glnA)
            BPL: BURPS1106A_2690(glnA) BURPS1106A_2711(glnA)
                 BURPS1106A_A0636(glnA)
            BPD: BURPS668_2634(glnA) BURPS668_A0728(glnA)
            BTE: BTH_I1828 BTH_I1844(glnA) BTH_II1946
            PNU: Pnuc_1255
            BPE: BP1596(glnA)
            BPA: BPP2988(glnA)
            BBR: BB2954(glnA)
            RFR: Rfer_0350 Rfer_2979
            POL: Bpro_1807 Bpro_2132 Bpro_4698 Bpro_5153
            PNA: Pnap_2780 Pnap_2864
            AAV: Aave_1442
            AJS: Ajs_1189
            VEI: Veis_0825 Veis_3034 Veis_3154
            MPT: Mpe_A1901 Mpe_A1911 Mpe_A2076
            HAR: HEAR0948(glnA)
            MMS: mma_1078(glnA)
            NEU: NE0504(glnA1)
            NET: Neut_1231
            NMU: Nmul_A2288
            EBA: ebA4121(glnA)
            AZO: azo0738(glnA) azo3010(glnT)
            DAR: Daro_0077 Daro_3763
            TBD: Tbd_2503
            MFA: Mfla_0456 Mfla_1856 Mfla_2447 Mfla_2562
            HPY: HP0512(glnA)
            HPJ: jhp0461(glnA)
            HPA: HPAG1_0486
            HHE: HH0560(glnA)
            HAC: Hac_0878(glnA)
            WSU: WS2124(glnA)
            TDN: Tmden_1889
            CJE: Cj0699c(glnA)
            CJR: CJE0798(glnA)
            CJJ: CJJ81176_0722(glnA)
            CJU: C8J_0666(glnA)
            CJD: JJD26997_1307(glnA)
            CFF: CFF8240_1054(glnA)
            CCV: CCV52592_0276(glnA)
            CHA: CHAB381_1710(glnA)
            CCO: CCC13826_0367 CCC13826_1446(glnA)
            ABU: Abu_1903(glnA)
            NIS: NIS_1519(glnA)
            SUN: SUN_0353(glnA)
            GSU: GSU1835(glnA)
            GME: Gmet_1352
            PCA: Pcar_1501
            PPD: Ppro_1681
            DVU: DVU1258(glnN) DVU3392(glnA)
            DVL: Dvul_0009
            DDE: Dde_0102 Dde_0104
            BBA: Bd0267(glnA)
            DPS: DP0930
            ADE: Adeh_4252
            MXA: MXAN_0912(glnA) MXAN_5630
            SAT: SYN_01613 SYN_01628
            SFU: Sfum_0576
            RPR: RP495
            RTY: RT0482
            RCO: RC0671
            RFE: RF_0728(glnA)
            RBE: RBE_0679(glnA)
            OTS: OTBS_1575(glnA)
            WOL: WD1322(glnA)
            WBM: Wbm0275
            AMA: AM1206(glnA) AM222(glnA)
            APH: APH_1061 APH_1246(glnA)
            ERU: Erum0610(glnA) Erum1480
            ERW: ERWE_CDS_00520(glnA) ERWE_CDS_01440
            ERG: ERGA_CDS_00510(glnA) ERGA_CDS_01400
            ECN: Ecaj_0054 Ecaj_0144
            ECH: ECH_0089(glnA) ECH_0983
            NSE: NSE_0350(glnA) NSE_0696
            PUB: SAR11_0747(glnA) SAR11_1305 SAR11_1316(glnT)
            MLO: mll0343 mll3074 mll4187 mll5148 mll6521 mll7254 mll7307
                 mlr0339 mlr6210
            MES: Meso_0161 Meso_1544 Meso_1870
            PLA: Plav_2794
            SME: SMb20745(glnII) SMc00762 SMc00948(glnA) SMc01594 SMc01973
                 SMc02352 SMc02613(glnT)
            SMD: Smed_4251
            ATU: Atu0193(glnA) Atu0602(glnA) Atu1770(glnA) Atu2142(glnA)
                 Atu2416(glnA) Atu4230(glnA)
            ATC: AGR_C_1068 AGR_C_3253 AGR_C_326 AGR_C_3883(glnA4) AGR_C_4385
                 AGR_L_1262
            RET: RHE_CH00706(glnA1) RHE_CH01315(ypch00448) RHE_CH02102(glnA2)
                 RHE_CH02886(glnA3) RHE_CH03104(glnII) RHE_PE00418(glnT)
            RLE: RL0755(glnA) RL1466(glnA) RL2392(glnA) RL3346(glnA)
                 RL3549(glnII) pRL110554(glnT)
            BME: BMEI0979 BMEII0523 BMEII0554
            BMF: BAB1_1023(glnA) BAB2_0471 BAB2_0507
            BMS: BR1004(glnA) BRA0732 BRA0768
            BMB: BruAb1_1009(glnA) BruAb2_0464 BruAb2_0499
            BOV: BOV_0970(glnA)
            OAN: Oant_3881 Oant_4157
            BJA: bll1069 blr4169(glnII) blr4835(glnA) blr4949(glnA)
            BRA: BRADO3395(glnII) BRADO4205(glnA) BRADO5882(glnA) BRADO6656
            BBT: BBta_0878 BBta_1945(glnA) BBta_3191 BBta_4311(glnII)
                 BBta_4581(glnA)
            RPA: RPA0984(glnA4) RPA1401(glnAIII) RPA2967(glnA) RPA4209(glnA)
            RPB: RPB_1135 RPB_1405 RPB_2269 RPB_2558
            RPC: RPC_1539 RPC_2386
            RPD: RPD_1385 RPD_2901
            RPE: RPE_2505
            NWI: Nwi_1904
            NHA: Nham_2234
            BHE: BH03890(glnA1) BH10160(glnA2)
            BQU: BQ02910(glnA1) BQ07890(glnA2)
            BBK: BARBAKC583_0733(glnA)
            XAU: Xaut_1141
            CCR: CC_1969 CC_3130 CC_3138
            SIL: SPO1300 SPO1302 SPO1573(glnT) SPO2295(glnA) SPO2607
            SIT: TM1040_1022 TM1040_1836 TM1040_1838 TM1040_2783 TM1040_3720
            RSP: RSP_0147(glnA) RSP_0375 RSP_0377 RSP_1568 RSP_2319(glnA)
            RSH: Rsph17029_0219 Rsph17029_0993 Rsph17029_1780 Rsph17029_2019
                 Rsph17029_2031
            RSQ: Rsph17025_1610
            JAN: Jann_1125 Jann_1127 Jann_1446 Jann_1515 Jann_2918
            RDE: RD1_1497 RD1_1892 RD1_1894 RD1_2173(ipuC) RD1_2569(glnA)
                 RD1_4250(glnT)
            PDE: Pden_1397 Pden_3702 Pden_4462 Pden_4547
            MMR: Mmar10_1330
            HNE: HNE_2084(glnA)
            ZMO: ZMO0493(glnA)
            NAR: Saro_1108 Saro_2609
            SAL: Sala_0149 Sala_1118 Sala_1121
            ELI: ELI_01660
            GOX: GOX1101
            GBE: GbCGDNIH1_0782 GbCGDNIH1_0957 GbCGDNIH1_2110
            RRU: Rru_A1252 Rru_A1253 Rru_A2079 Rru_A2086
            MAG: amb0696
            MGM: Mmc1_0988
            ABA: Acid345_0166 Acid345_3142
            SUS: Acid_0067 Acid_1901 Acid_4831
            BSU: BG10425(glnA)
            BHA: BH2360(glnA) BH3867
            BAN: BA3833(glnA)
            BAR: GBAA3833(glnA)
            BAT: BAS3549
            BCA: BCE_3731(glnA)
            BCZ: BCZK3462(glnA)
            BCY: Bcer98_2381
            BTK: BT9727_3449(glnA)
            BLD: BLi01993(glnA)
            BCL: ABC2179(glnA) ABC3940
            BAY: RBAM_017260(glnA)
            BPU: BPUM_1637(glnA)
            OIH: OB1651(glnA)
            GKA: GK1327(glnA) GK1637
            SAU: SA1150(glnA)
            SAV: SAV1310(glnA)
            SAM: MW1192(glnA)
            SAR: SAR1284(glnA)
            SAS: SAS1242
            SAC: SACOL1329(femC)
            SAB: SAB1172(glnA)
            SAA: SAUSA300_1201(glnA)
            SAO: SAOUHSC_01287
            SAJ: SaurJH9_1368
            SAH: SaurJH1_1394
            SEP: SE0987
            SER: SERP0876(femC)
            SHA: SH1600(glnA)
            SSP: SSP1451
            LMO: lmo1299(glnA)
            LMF: LMOf2365_1317(glnA)
            LIN: lin1337(glnA)
            LWE: lwe1314(glnA)
            LLA: L0118(glnA)
            LLC: LACR_2512
            LLM: llmg_2484(glnA)
            SPY: SPy_1877(glnA)
            SPZ: M5005_Spy_1596(glnA)
            SPM: spyM18_1942(glnA)
            SPG: SpyM3_1621(glnA)
            SPS: SPs0246
            SPH: MGAS10270_Spy1667(glnA)
            SPI: MGAS10750_Spy1654(glnA)
            SPJ: MGAS2096_Spy1622(glnA)
            SPK: MGAS9429_Spy1601(glnA)
            SPF: SpyM50255(glnA)
            SPA: M6_Spy1607
            SPB: M28_Spy1588(glnA)
            SPN: SP_0502
            SPR: spr0444(glnA)
            SPD: SPD_0448(glnA)
            SAG: SAG1763(glnA)
            SAN: gbs1806(glnA)
            SAK: SAK_1785(glnA)
            SMU: SMU.364(glnA)
            STC: str1776(gnlA)
            STL: stu1776(gnlA)
            SSA: SSA_0307(glnA)
            SGO: SGO_0215(glnA)
            LPL: lp_1581(glnA)
            LJO: LJ1614
            LAC: LBA1501(glnA)
            LSA: LSA1321(glnA)
            LSL: LSL_0558(glnA)
            LDB: Ldb1472(glnA)
            LBU: LBUL_1368
            LBR: LVIS_0990
            LCA: LSEI_0439 LSEI_1652
            LRE: Lreu_1202
            EFA: EF2159(glnA)
            OOE: OEOE_0952
            STH: STH198
            CAC: CAC2658(glnA)
            CPE: CPE2569
            CPF: CPF_2894
            CPR: CPR_2573
            CTC: CTC00171
            CNO: NT01CX_0655
            CTH: Cthe_0202
            CDF: CD1343(glnA)
            CBO: CBO3563(glnA)
            CBE: Cbei_4206
            CKL: CKL_0130(glnA)
            CHY: CHY_0704(glnA1) CHY_0712(glnA2)
            DSY: DSY4039 DSY4328 DSY4406
            DRM: Dred_2806 Dred_2807 Dred_2810
            SWO: Swol_1007 Swol_1787
            TTE: TTE0821(glnA)
            MTA: Moth_1294 Moth_1297 Moth_1764 Moth_2299
            MTU: Rv2220(glnA1) Rv2222c(glnA2) Rv2860c(glnA4)
            MTC: MT2278(glnA-1) MT2280(glnA-2) MT2928
            MBO: Mb1910(glnA3) Mb2244(glnA1) Mb2246c(glnA2) Mb2885c(glnA4)
            MBB: BCG_1915(glnA3) BCG_2237(glnA1) BCG_2239c(glnA2)
                 BCG_2882c(glnA4)
            MLE: ML0925(glnA) ML1631(glnA2)
            MPA: MAP1962(glnA1) MAP1966c(glnA2) MAP2931c(glnA4)
            MAV: MAV_2244(glnA) MAV_2267(glnA) MAV_2829(glnA) MAV_3718(glnA)
            MSM: MSMEG_2595 MSMEG_3561(glnA) MSMEG_3827 MSMEG_3828
                 MSMEG_4290(glnA) MSMEG_4294(glnA) MSMEG_5374 MSMEG_6260(glnT)
            MVA: Mvan_0611 Mvan_0612 Mvan_1603 Mvan_1850 Mvan_2278 Mvan_3585
                 Mvan_3598 Mvan_5509
            MGI: Mflv_1300 Mflv_2909 Mflv_2928 Mflv_4065
            MMC: Mmcs_0512 Mmcs_0870 Mmcs_2057 Mmcs_2754 Mmcs_3320 Mmcs_3328
                 Mmcs_4892 Mmcs_5344
            MKM: Mkms_0523 Mkms_0887 Mkms_2103 Mkms_3382 Mkms_3390 Mkms_4981
                 Mkms_5433
            MJL: Mjls_0501 Mjls_0876 Mjls_2040 Mjls_3331 Mjls_3339 Mjls_5260
                 Mjls_5723
            CGL: NCgl2133(cgl2214) NCgl2148(cgl2229)
            CGB: cg2429(glnA) cg2447(glnA2)
            CEF: CE2104(glnA) CE2116 CE2127(glnA2)
            CDI: DIP1644(glnA1) DIP1671(glnA2)
            CJK: jk0675(glnA2) jk0702(glnA1)
            NFA: nfa16600(glnA) nfa16670(glnA2) nfa21040(glnA3)
            RHA: RHA1_ro01157(glnA1) RHA1_ro01167(glnA2) RHA1_ro02820(glnA3)
                 RHA1_ro05312(glnA4)
            SCO: SCO1613(SCI35.35c) SCO2198(glnA) SCO2210(glnII)
                 SCO2241(SC1G2.03)
            SMA: SAV5954(glnA1) SAV5997(glnA2) SAV6005(glnA3) SAV6725(glnA4)
            TWH: TWT261(glnA)
            TWS: TW509(glnA)
            LXX: Lxx10010(glnA) Lxx10080(glnA)
            CMI: CMM_1634(glnA2) CMM_1636(glnA1)
            ART: Arth_1592 Arth_1600
            AAU: AAur_1731(glnA) AAur_1744(glnA)
            PAC: PPA0664 PPA0671
            NCA: Noca_0830 Noca_2046 Noca_2295 Noca_2587
            TFU: Tfu_0982 Tfu_0988
            FRA: Francci3_3142 Francci3_3143 Francci3_3145 Francci3_4059
            FAL: FRAAL0678 FRAAL1887(glnIII) FRAAL5161(glnA) FRAAL5163(glnII)
                 FRAAL5165(glnA1) FRAAL6426
            ACE: Acel_0919 Acel_0923 Acel_1096 Acel_1851
            SEN: SACE_1613(glnA2) SACE_1623(glnA-1) SACE_3095 SACE_5355(glnA4)
            BLO: BL1076(glnA1) BL1302(glnA2)
            BAD: BAD_0943(glnA1) BAD_1123(glnA2)
            RXY: Rxyl_1031 Rxyl_1125 Rxyl_2498 Rxyl_3196
            RBA: RB7247(glnII)
            PCU: pc1240(glnA)
            LIL: LA1313(glnA)
            LIC: LIC12407(glnA)
            LBJ: LBJ_1043(glnA)
            LBL: LBL_1991(glnA)
            SYN: slr0288(glnN) slr1756(glnA)
            SYW: SYNW1073(glnA)
            SYC: syc1338_c(glnN) syc1804_d(glnA) syc1938_d(glnA)
            SYF: Synpcc7942_0169 Synpcc7942_2156 Synpcc7942_2296
            SYD: Syncc9605_1205
            SYE: Syncc9902_1265
            SYG: sync_1253 sync_1569(glnA)
            SYR: SynRCC307_1296(glnA)
            SYX: SynWH7803_1347(glnAI)
            CYA: CYA_1363(glnA)
            CYB: CYB_1005(glnA-1) CYB_2804(glnA-2)
            TEL: tll1588(glnA)
            GVI: gll2499(glnT) glr1052(glnA)
            ANA: alr2328(glnA)
            AVA: Ava_0147
            PMA: Pro1038(glnA)
            PMM: PMM0920(glnA)
            PMT: PMT0601(glnA)
            PMN: PMN2A_0141
            PMI: PMT9312_0880
            PMB: A9601_09401(glnA)
            PMC: P9515_10031(glnA)
            PMF: P9303_16421(glnA)
            PMG: P9301_09391(glnA)
            PMH: P9215_09701(glnA)
            PME: NATL1_07731(glnA)
            TER: Tery_3834 Tery_4681
            BTH: BT_0543 BT_0785 BT_4339
            BFR: BF1040 BF2249
            BFS: BF0955(glnA) BF2343
            SRU: SRU_0385(glnA)
            CHU: CHU_1734(glnA) CHU_1735(glnA) CHU_2502(glnA)
            GFO: GFO_0471(glnA)
            FJO: Fjoh_2344
            FPS: FP0545(glnA)
            CTE: CT1411(glnA)
            CCH: Cag_1588
            PLT: Plut_1413
            DET: DET1123(glnA)
            DEH: cbdb_A1050(glnA)
            RCA: Rcas_3479
            DRA: DR_0451 DR_2033
            DGE: Dgeo_1203 Dgeo_1204
            TTH: TTC0965
            TTJ: TTHA1329
            AAE: aq_111(glnA)
            TMA: TM0943
            TPT: Tpet_1799
            TME: Tmel_0990
            FNO: Fnod_0261
            MMP: MMP1206(glnA)
            MMQ: MmarC5_0384
            MAC: MA4216(glnA)
            MBA: Mbar_A0666
            MMA: MM_0964
            MBU: Mbur_1975
            MTP: Mthe_0249 Mthe_0634
            MHU: Mhun_0779
            MEM: Memar_0335 Memar_2135 Memar_2288
            MBN: Mboo_1689 Mboo_1947
            MST: Msp_0234(glnA)
            MSI: Msm_1418
            MKA: MK0338(glnA)
            HAL: VNG2093G(glnA)
            HMA: rrnAC2780(glnA)
            HWA: HQ3643A(glnA)
            NPH: NP0076A(glnA_1) NP4376A(glnA_2)
            TAC: Ta1498
            TVO: TVN1492
            PTO: PTO0533
            PAB: PAB1292(glnA)
            PFU: PF0450
            TKO: TK1796
            RCI: RCIX649(glnA-1) RCIX942(glnA-2)
            APE: APE_2142.1
            SMR: Smar_0183
            HBU: Hbut_1195
            SSO: SSO0366(glnA-1) SSO2440(glnA-2) SSO2554(glnA-3)
            STO: ST0156 ST0568 ST1387
            SAI: Saci_0558(glnA) Saci_1483(glnA) Saci_2141(glnA)
            PAI: PAE2556 PAE3442
            PIS: Pisl_0144
            PCL: Pcal_1609
            PAS: Pars_1098
            TPE: Tpen_1089
STRUCTURES  PDB: 1F1H  1F52  1FPY  1HTO  1HTQ  1LGR  2BVC  2D3A  2D3B  2D3C  
                 2GLS  2LGS  2OJW  2QC8  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.1.2
            ExPASy - ENZYME nomenclature database: 6.3.1.2
            ExplorEnz - The Enzyme Database: 6.3.1.2
            ERGO genome analysis and discovery system: 6.3.1.2
            BRENDA, the Enzyme Database: 6.3.1.2
            CAS: 9023-70-5
///
ENTRY       EC 6.3.1.3        Obsolete  Enzyme
NAME        Transferred to 6.3.4.13
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-ammonia (or amine) ligases (amide synthases)
COMMENT     Transferred entry: now EC 6.3.4.13 phosphoribosylamine-glycine
            ligase (EC 6.3.1.3 created 1961, deleted 1972)
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.1.3
            ExPASy - ENZYME nomenclature database: 6.3.1.3
            ExplorEnz - The Enzyme Database: 6.3.1.3
            ERGO genome analysis and discovery system: 6.3.1.3
            BRENDA, the Enzyme Database: 6.3.1.3
///
ENTRY       EC 6.3.1.4                  Enzyme
NAME        aspartate---ammonia ligase (ADP-forming);
            asparagine synthetase (ADP-forming);
            asparagine synthetase (adenosine diphosphate-forming)
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-ammonia (or amine) ligases (amide synthases)
SYSNAME     L-aspartate:ammonia ligase (ADP-forming)
REACTION    ATP + L-aspartate + NH3 = ADP + phosphate + L-asparagine [RN:R00482]
ALL_REAC    R00482
SUBSTRATE   ATP [CPD:C00002];
            L-aspartate [CPD:C00049];
            NH3 [CPD:C00014]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            L-asparagine [CPD:C00152]
REFERENCE   1  [PMID:5820987]
  AUTHORS   Nair PM.
  TITLE     Asparagine synthetase from gamma-irradiated potatoes.
  JOURNAL   Arch. Biochem. Biophys. 133 (1969) 208-15.
  ORGANISM  Solanum tuberosum [GN:estu]
PATHWAY     PATH: map00910  Nitrogen metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.1.4
            ExPASy - ENZYME nomenclature database: 6.3.1.4
            ExplorEnz - The Enzyme Database: 6.3.1.4
            ERGO genome analysis and discovery system: 6.3.1.4
            BRENDA, the Enzyme Database: 6.3.1.4
            CAS: 37318-61-9
///
ENTRY       EC 6.3.1.5                  Enzyme
NAME        NAD+ synthase;
            NAD+ synthetase;
            NAD+ synthase;
            nicotinamide adenine dinucleotide synthetase;
            diphosphopyridine nucleotide synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-ammonia (or amine) ligases (amide synthases)
SYSNAME     deamido-NAD+:ammonia ligase (AMP-forming)
REACTION    ATP + deamido-NAD+ + NH3 = AMP + diphosphate + NAD+ [RN:R00189]
ALL_REAC    R00189
SUBSTRATE   ATP [CPD:C00002];
            deamido-NAD+ [CPD:C00857];
            NH3 [CPD:C00014]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            NAD+ [CPD:C00003]
COMMENT     L-Glutamine also acts, more slowly, as amido-donor [cf. EC 6.3.5.1].
REFERENCE   1  [PMID:4290215]
  AUTHORS   Spencer RL, Preiss J.
  TITLE     Biosynthesis of diphosphopyridine nucleotide. The purification and
            the properties of diphospyridine nucleotide synthetase from
            Escherichia coli b.
  JOURNAL   J. Biol. Chem. 242 (1967) 385-92.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00760  Nicotinate and nicotinamide metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K01916  NAD+ synthase
GENES       PFA: PFI1310w
            ECW: EcE24377A_1961(nadE)
            ECX: EcHS_A1822
            ENT: Ent638_1704
            PSP: PSPPH_0587(nadE)
            SPL: Spea_1758
            SHE: Shewmr4_2246
            SHM: Shewmr7_2318
            SHN: Shewana3_2438
            CBD: COXBU7E912_0922(nadE)
            FTW: FTW_0685(nadE)
            FTA: FTA_0724(nadE)
            BUR: Bcep18194_B0372(nadE)
            BCN: Bcen_3089
            BPL: BURPS1106A_1089(nadE) BURPS1106A_A2006(nadE)
            BPD: BURPS668_1084(nadE) BURPS668_A2101(nadE)
            BTE: BTH_II0886(nadE)
            TDN: Tmden_0851
            CFF: CFF8240_1078(nadE)
            CCV: CCV52592_0093 CCV52592_0125(nadE)
            CHA: CHAB381_1025(nadE)
            CCO: CCC13826_0300
            ABU: Abu_1250(nadE)
            GUR: Gura_3754
            PPD: Ppro_2868
            ADE: Adeh_2788
            AFW: Anae109_1248
            NSE: NSE_0097(nadE)
            SMD: Smed_4337
            RLE: RL1332(nadE)
            RPE: RPE_0579
            ZMO: ZMO0899
            SAA: SAUSA300_1893(nadE)
            SAO: SAOUHSC_02132
            SPD: SPD_1250(nadE)
            SSA: SSA_1863(nadE)
            CPF: CPF_1314(nadE)
            CPR: CPR_1130(nadE)
            CDF: CD0794(nadE)
            MMO: MMOB1920(nadE)
            RHA: RHA1_ro06432(nadE)
            AAU: AAur_0519(nadE)
            SYG: sync_2294(nadE)
            CYA: CYA_0206(nadE)
            CYB: CYB_1248(nadE)
            PMB: A9601_16481(nadE)
            PMC: P9515_16251(nadE)
            PMF: P9303_04891(nadE)
            PMG: P9301_16361(nadE)
            PME: NATL1_18451(nadE)
            GFO: GFO_2783(nadE)
            CCH: Cag_1279(nadE)
            CPH: Cpha266_0810
            PVI: Cvib_1211
            PLT: Plut_0564(nadE)
            RCA: Rcas_0488
            DGE: Dgeo_1327
            MAE: Maeo_0662
            MBU: Mbur_1809
            MST: Msp_0170(nadE)
            RCI: RCIX358(nadE)
            SMR: Smar_1310
            HBU: Hbut_0932
            PIS: Pisl_1302 Pisl_1454
            TPE: Tpen_1444
STRUCTURES  PDB: 1WXE  1WXF  1WXG  1WXH  1WXI  1XNG  1XNH  2E18  2PZ8  2PZA  
                 2PZB  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.1.5
            ExPASy - ENZYME nomenclature database: 6.3.1.5
            ExplorEnz - The Enzyme Database: 6.3.1.5
            ERGO genome analysis and discovery system: 6.3.1.5
            BRENDA, the Enzyme Database: 6.3.1.5
            CAS: 9032-69-3
///
ENTRY       EC 6.3.1.6                  Enzyme
NAME        glutamate---ethylamine ligase;
            N5-ethyl-L-glutamine synthetase;
            theanine synthetase;
            N5-ethylglutamine synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-ammonia (or amine) ligases (amide synthases)
SYSNAME     L-glutamate:ethylamine ligase (ADP-forming)
REACTION    ATP + L-glutamate + ethylamine = ADP + phosphate +
            N5-ethyl-L-glutamine [RN:R02929]
ALL_REAC    R02929
SUBSTRATE   ATP [CPD:C00002];
            L-glutamate [CPD:C00025];
            ethylamine [CPD:C00797]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            N5-ethyl-L-glutamine [CPD:C01047]
REFERENCE   1
  AUTHORS   Sasaoka, K. and Kito, M.
  TITLE     Synthesis of theanine by tea seedling homogenate.
  JOURNAL   Agric. Biol. Chem. 28 (1964) 313-317.
  ORGANISM  tea
REFERENCE   2
  AUTHORS   Sasaoka, K., Kito, M. and Inagaki, H.
  TITLE     Studies on the biosynthesis of theanine in tea seedlings. Synthesis
            of theanine by the homogenate of tea seedlings.
  JOURNAL   Agric. Biol. Chem. 27 (1963) 467-468.
REFERENCE   3
  AUTHORS   Sasaoka, K., Kito, M. and Onishi, Y.
  TITLE     Some properties of the theanine synthesizing enzyme in tea
            seedlings.
  JOURNAL   Agric. Biol. Chem. 29 (1965) 984-988.
  ORGANISM  tea
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.1.6
            ExPASy - ENZYME nomenclature database: 6.3.1.6
            ExplorEnz - The Enzyme Database: 6.3.1.6
            ERGO genome analysis and discovery system: 6.3.1.6
            BRENDA, the Enzyme Database: 6.3.1.6
            CAS: 62213-31-4
///
ENTRY       EC 6.3.1.7                  Enzyme
NAME        4-methyleneglutamate---ammonia ligase;
            4-methyleneglutamine synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-ammonia (or amine) ligases (amide synthases)
SYSNAME     4-methylene-L-glutamate:ammonia ligase (AMP-forming)
REACTION    ATP + 4-methylene-L-glutamate + NH3 = AMP + diphosphate +
            4-methylene-L-glutamine [RN:R02711]
ALL_REAC    R02711
SUBSTRATE   ATP [CPD:C00002];
            4-methylene-L-glutamate [CPD:C00651];
            NH3 [CPD:C00014]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            4-methylene-L-glutamine [CPD:C01109]
COMMENT     Glutamine can act instead of NH3, but more slowly.
REFERENCE   1  [PMID:6838571]
  AUTHORS   Winter HC, Su TZ, Dekker EE.
  TITLE     4-methyleneglutamine synthetase: a new amide synthetase present in
            germinating peanuts.
  JOURNAL   Biochem. Biophys. Res. Commun. 111 (1983) 484-9.
  ORGANISM  Arachis hypogaea
PATHWAY     PATH: map00660  C5-Branched dibasic acid metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.1.7
            ExPASy - ENZYME nomenclature database: 6.3.1.7
            ExplorEnz - The Enzyme Database: 6.3.1.7
            ERGO genome analysis and discovery system: 6.3.1.7
            BRENDA, the Enzyme Database: 6.3.1.7
            CAS: 85537-85-5
///
ENTRY       EC 6.3.1.8                  Enzyme
NAME        glutathionylspermidine synthase;
            glutathione:spermidine ligase (ADP-forming)
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-ammonia (or amine) ligases (amide synthases)
SYSNAME     gamma-L-glutamyl-L-cysteinyl-glycine:spermidine ligase (ADP-forming)
            [spermidine is numbered so that atom N-1 is in the amino group of
            the aminopropyl part of the molecule]
REACTION    glutathione + spermidine + ATP = glutathionylspermidine + ADP +
            phosphate [RN:R01917]
ALL_REAC    R01917
SUBSTRATE   glutathione [CPD:C00051];
            spermidine [CPD:C00315];
            ATP [CPD:C00002]
PRODUCT     glutathionylspermidine [CPD:C05730];
            ADP [CPD:C00008];
            phosphate [CPD:C00009]
COFACTOR    Magnesium [CPD:C00305]
COMMENT     Requires magnesium ions. Involved in the synthesis of trypanothione
            in trypanosomatids. The enzyme from Escherichia coli is bifunctional
            and also catalyses the glutathionylspermidine amidase (EC 3.5.1.78)
            reaction, resulting in a net hydrolysis of ATP.
REFERENCE   1  [PMID:1304372]
  AUTHORS   Smith K, Nadeau K, Bradley M, Walsh C, Fairlamb AH.
  TITLE     Purification of glutathionylspermidine and trypanothione synthetases
            from Crithidia fasciculata.
  JOURNAL   Protein. Sci. 1 (1992) 874-83.
  ORGANISM  Crithidia fasciculat
REFERENCE   2  [PMID:7775463]
  AUTHORS   Bollinger JM Jr, Kwon DS, Huisman GW, Kolter R, Walsh CT.
  TITLE     Glutathionylspermidine metabolism in Escherichia coli. Purification,
            cloning, overproduction, and characterization of a bifunctional
            glutathionylspermidine synthetase/amidase.
  JOURNAL   J. Biol. Chem. 270 (1995) 14031-41.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00480  Glutathione metabolism
ORTHOLOGY   KO: K01917  glutathionylspermidine synthase
GENES       ECO: b2988(gss)
            ECJ: JW2956(gss)
            ECE: Z4342(gsp)
            ECS: ECs3873
            ECC: c3725(gsp)
            ECI: UTI89_C3410(gsp)
            ECP: ECP_3073
            ECV: APECO1_3433(gsp)
            ECW: EcE24377A_3455(gsp)
            ECX: EcHS_A3168(gsp)
            STY: STY3310(gsp)
            STT: t3060(gsp)
            SPT: SPA3007(gsp)
            SEC: SC3080(gsp)
            STM: STM3139(gsp)
            SFL: SF3035(gsp)
            SFX: S3236(gsp)
            SFV: SFV_3041(gsp)
            SSN: SSON_3133(gsp)
            SBO: SBO_2875(gsp)
            SDY: SDY_3085(gsp)
            ENT: Ent638_3393
            MSU: MS0671(gsp)
            VVY: VV2267
            PHA: PSHAa2455(gssA)
            REH: H16_A0042
            HPA: HPAG1_0236
            TDN: Tmden_1471
            SUN: SUN_0613
            RLE: pRL120092
            BRA: BRADO1482
            BBT: BBta_6550
            RRU: Rru_A3723
            BAN: BA1602 BA2932
            BAR: GBAA1602 GBAA2932
            BAA: BA_2120 BA_3442
            BAT: BAS1486 BAS2724
            BCE: BC1579
            BCA: BCE_2970
            BCZ: BCZK1458 BCZK2652(gspS)
            BTK: BT9727_1459 BT9727_2675(gspS)
            AVA: Ava_B0291
STRUCTURES  PDB: 2IO7  2IO8  2IO9  2IOA  2IOB  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.1.8
            ExPASy - ENZYME nomenclature database: 6.3.1.8
            ExplorEnz - The Enzyme Database: 6.3.1.8
            ERGO genome analysis and discovery system: 6.3.1.8
            BRENDA, the Enzyme Database: 6.3.1.8
            CAS: 9077-09-2
///
ENTRY       EC 6.3.1.9                  Enzyme
NAME        trypanothione synthase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-ammonia (or amine) ligases (amide synthases)
SYSNAME     glutathionylspermidine:glutathione ligase (ADP-forming)
REACTION    glutathione + glutathionylspermidine + ATP =
            N1,N8-bis(glutathionyl)spermidine + ADP + phosphate [RN:R03822]
ALL_REAC    R03822
SUBSTRATE   glutathione [CPD:C00051];
            glutathionylspermidine [CPD:C05730];
            ATP [CPD:C00002]
PRODUCT     N1,N8-bis(glutathionyl)spermidine;
            ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     Involved in the synthesis of trypanothione in trypanosomatids
REFERENCE   1  [PMID:1304372]
  AUTHORS   Smith K, Nadeau K, Bradley M, Walsh C, Fairlamb AH.
  TITLE     Purification of glutathionylspermidine and trypanothione synthetases
            from Crithidia fasciculata.
  JOURNAL   Protein. Sci. 1 (1992) 874-83.
  ORGANISM  Crithidia fasciculata
ORTHOLOGY   KO: K01833  trypanothione synthase
GENES       TBR: Tb927.2.4370 Tb927.8.2410
            TCR: 504427.10 509331.134
            LMA: LmjF27.1870
            PSP: PSPPH_3588
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.1.9
            ExPASy - ENZYME nomenclature database: 6.3.1.9
            ExplorEnz - The Enzyme Database: 6.3.1.9
            ERGO genome analysis and discovery system: 6.3.1.9
            BRENDA, the Enzyme Database: 6.3.1.9
            CAS: 130246-69-4
///
ENTRY       EC 6.3.1.10                 Enzyme
NAME        adenosylcobinamide-phosphate synthase;
            CbiB
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-ammonia (or amine) ligases (amide synthases)
SYSNAME     adenosylcobyric acid:(R)-1-aminopropan-2-yl phosphate ligase
            (ADP-forming)
REACTION    (1) ATP + adenosylcobyric acid + (R)-1-aminopropan-2-yl phosphate =
            ADP + phosphate + adenosylcobinamide phosphate [RN:R06529];
            (2) ATP + adenosylcobyric acid + (R)-1-aminopropan-2-ol = ADP +
            phosphate + adenosylcobinamide [RN:R07302]
ALL_REAC    R06529 R07302
SUBSTRATE   ATP [CPD:C00002];
            adenosylcobyric acid [CPD:C06507];
            (R)-1-aminopropan-2-yl phosphate [CPD:C04122];
            (R)-1-aminopropan-2-ol [CPD:C03194]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            adenosylcobinamide phosphate;
            adenosylcobinamide
COMMENT     One of the substrates for this reaction, (R)-1-aminopropan-2-yl
            phosphate, is produced by CobD (EC 4.1.1.81, threonine-phosphate
            decarboxylase).
REFERENCE   1  [PMID:11939774]
  AUTHORS   Cheong CG, Bauer CB, Brushaber KR, Escalante-Semerena JC, Rayment I.
  TITLE     Three-dimensional structure of the L-threonine-O-3-phosphate
            decarboxylase (CobD) enzyme from Salmonella enterica.
  JOURNAL   Biochemistry. 41 (2002) 4798-808.
  ORGANISM  Salmonella enterica
REFERENCE   2  [PMID:12195810]
  AUTHORS   Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
  TITLE     The biosynthesis of adenosylcobalamin (vitamin B12).
  JOURNAL   Nat. Prod. Rep. 19 (2002) 390-412.
  ORGANISM  Salmonella enterica
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K02227  adenosylcobinamide-phosphate synthase CobD
GENES       STY: STY2239(cbiB)
            STT: t0839(cbiB)
            SEC: SC2042(cibB)
            STM: STM2034(cbiB)
            PLU: plu2998(cbiB)
            XCC: XCC3062(cobD)
            XCB: XC_1096
            XCV: XCV3319(cobD)
            XAC: XAC3190(cobD)
            VCH: VC2380
            VVU: VV1_0559
            VVY: VV0634(cbiB)
            VPA: VP0478(cbiB)
            VFI: VF2129
            PPR: PBPRA0537(cbiB)
            PAE: PA1275(cobD)
            PAU: PA14_47730(cobD)
            PAP: PSPA7_4115
            PPU: PP_1675(cobD)
            PST: PSPTO_1711(cobD)
            PSB: Psyr_3678(cbiB)
            PSP: PSPPH_3699(cobD)
            PFL: PFL_4428(cobD)
            PFO: Pfl_1644(cbiB)
            PEN: PSEEN1381
            SON: SO_1321
            SDN: Sden_2802
            SFR: Sfri_2967
            SHE: Shewmr4_2875
            SHM: Shewmr7_2957
            SHN: Shewana3_3053
            CPS: CPS_1143 CPS_4742
            PHA: PSHAa0546
            PAT: Patl_0517 Patl_1131
            MCA: MCA2287(cobD)
            AEH: Mlg_2818
            HCH: HCH_06462(cobD)
            ABO: ABO_2377(cobD)
            CVI: CV_1002 CV_1575(cobD)
            RSO: RSc0938(cobD) RSc2392(RS02743)
            REU: Reut_A0663(cbiB) Reut_A0903(cbiB)
            REH: H16_A2963(cbiB) H16_A2964(cobD)
            RME: Rmet_2578 Rmet_2780
            BMA: BMA0396 BMA0695(cobD)
            BMV: BMASAVP1_A2318(cobD)
            BML: BMA10299_A2969(cobD)
            BMN: BMA10247_1630(cobD)
            BXE: Bxe_A1011 Bxe_A3494
            BUR: Bcep18194_A4188(cbiB) Bcep18194_A5779(cbiB)
            BCN: Bcen_1837
            BCH: Bcen2424_1074 Bcen2424_2448
            BAM: Bamb_2496
            BPS: BPSL0985 BPSL2485
            BPM: BURPS1710b_1198(cobD) BURPS1710b_2962(cobD)
            BPL: BURPS1106A_1043
            BPD: BURPS668_1037
            BTE: BTH_I0842(cobD) BTH_I1666
            RFR: Rfer_1407 Rfer_2616
            POL: Bpro_1695 Bpro_2762
            MPT: Mpe_A1109 Mpe_B0516(cbiB)
            NMU: Nmul_A1994(cbiB)
            EBA: ebA2136(cobD) ebA5199(cbiB)
            DAR: Daro_0140(cbiB) Daro_3023(cbiB)
            TBD: Tbd_1044 Tbd_2716(cbiB)
            MFA: Mfla_0102 Mfla_2432
            GSU: GSU2990(cobD)
            GME: Gmet_0486
            PCA: Pcar_0483(cbiB)
            DVU: DVU2237
            DDE: Dde_1529(cobD)
            DPS: DP1949(cobD)
            SFU: Sfum_1738
            MLO: mlr1304(cobD)
            SME: SMc04279(cobD)
            ATU: Atu2809(cobD)
            ATC: AGR_C_5095(cobD)
            RET: RHE_CH02481(cobD)
            RLE: RL2821(cobD)
            BME: BMEI0707
            BMF: BAB1_1314(cobD)
            BMS: BR1294(cobD)
            BMB: BruAb1_1295(cobD)
            BOV: BOV_1256(cobD-1)
            BJA: blr3257(cobD)
            RPA: RPA0719(cobD)
            RPB: RPB_0735(cobD)
            RPC: RPC_3744
            RPD: RPD_0633
            RPE: RPE_2239
            SIL: SPO3225(cobD)
            SIT: TM1040_2585
            RSP: RSP_0430(cobD)
            JAN: Jann_0370
            RDE: RD1_1330(cobD)
            HNE: HNE_1519(cobD)
            NAR: Saro_0324
            GBE: GbCGDNIH1_0653
            RRU: Rru_A3382
            MAG: amb0293
            MGM: Mmc1_1424
            BHA: BH1588(cobD)
            GKA: GK2263
            LMO: lmo1192
            LMF: LMOf2365_1201
            LIN: lin1155
            LWE: lwe1149(cbiB)
            SSA: SSA_0464
            STH: STH1927
            CAC: CAC0582
            CPE: CPE1039(cbiB)
            CPF: CPF_1294(cobB)
            CPR: CPR_1113(cobD)
            CTC: CTC00721(cbiB)
            CNO: NT01CX_2082(cobD)
            CBA: CLB_0955(cobD)
            CBH: CLC_0969(cobD)
            CBF: CLI_1001(cobD)
            CHY: CHY_0770(cobD)
            DSY: DSY4061(cobD)
            TTE: TTE0377(cbiB)
            MTA: Moth_1099(cobD)
            MTU: Rv2236c(cobD)
            MTC: MT2295(cobD)
            MBO: Mb2260c(cobD)
            MPA: MAP1987c(cobD)
            MAV: MAV_2205(cobD)
            MSM: MSMEG_4310(cobD)
            MMC: Mmcs_3349
            CEF: CE2140
            CDI: DIP1685
            NFA: nfa16270
            RHA: RHA1_ro01188
            SCO: SCO1847(cobD)
            SMA: SAV6417(cobD)
            PAC: PPA0418
            TFU: Tfu_2224(cbiB)
            FRA: Francci3_2604(cobD)
            FAL: FRAAL2886
            SEN: SACE_1574(cobD)
            RXY: Rxyl_0649
            FNU: FN0975(cbiB)
            TDE: TDE2389(cobD)
            LIL: LB150(cbiB)
            LIC: LIC20120(cobD)
            LBJ: LBJ_4192(cobD)
            LBL: LBL_4207(cobD)
            SYN: slr1925(cbiB)
            SYW: SYNW1651(cobD)
            SYC: syc0115_d
            SYF: Synpcc7942_1441
            SYD: Syncc9605_0838
            SYE: Syncc9902_1551
            SYG: sync_0724(cobD-1)
            SYR: SynRCC307_0593(cobD)
            CYA: CYA_0424(cobD-1)
            CYB: CYB_2498(cobD-2)
            TEL: tlr2377(cobD)
            GVI: glr2448(cobD)
            ANA: alr2082(cobD)
            AVA: Ava_3127(cobD)
            PMA: Pro1390(cbiB)
            PMM: PMM1316(cobD)
            PMT: PMT0312(cobD)
            PMN: PMN2A_0882(cbiB)
            PMI: PMT9312_1413
            PMB: A9601_15151(cbiB)
            PMC: P9515_14771(cbiB)
            PMF: P9303_20061(cbiB)
            PMG: P9301_15021(cbiB)
            PME: NATL1_17371(cbiB)
            TER: Tery_1861
            BFR: BF2489(cobD)
            BFS: BF2522
            PGI: PG1159(cbiB)
            CTE: CT0940(cbiB)
            CCH: Cag_0757(cbiB)
            PLT: Plut_1138(cbiB)
            DET: DET0654(cobD-2) DET0688(cobD-3) DET1138(cobD-4)
            DEH: cbdb_A1067(cobD) cbdb_A638(cbiB)
            DRA: DR_B0010
            DGE: Dgeo_2348
            TTH: TT_P0019(cbiB)
            TTJ: TTHB062
            MJA: MJ1314(cbiB)
            MMP: MMP0951(chiB)
            MAC: MA0941(cobD)
            MBA: Mbar_A3454
            MMA: MM_2059
            MBU: Mbur_2090
            MHU: Mhun_2321
            MTH: MTH1409
            MST: Msp_1588(cobD)
            MSI: Msm_1266
            MKA: MK1516(cbiB)
            AFU: AF1336(cbiB)
            HAL: VNG1578H
            HMA: rrnAC1930
            HWA: HQ1411A(cbiB)
            NPH: NP5308A(cbiB)
            TAC: Ta0076
            TVO: TVN0030
            PTO: PTO0811
            PHO: PH0376
            PAB: PAB0025(cbiB)
            PFU: PF0296
            TKO: TK0863
            RCI: RCIX2654(cbiB)
            APE: APE_2039.1
            SSO: SSO3235(cbiB)
            STO: ST2342(cobD)
            SAI: Saci_0411(cobD)
            PAI: PAE0381(cbiB)
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.1.10
            ExPASy - ENZYME nomenclature database: 6.3.1.10
            ExplorEnz - The Enzyme Database: 6.3.1.10
            ERGO genome analysis and discovery system: 6.3.1.10
            BRENDA, the Enzyme Database: 6.3.1.10
///
ENTRY       EC 6.3.1.11                 Enzyme
NAME        glutamate---putrescine ligase;
            gamma-glutamylputrescine synthetase;
            YcjK
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-ammonia (or amine) ligases (amide synthases)
SYSNAME     L-glutamate:putrescine ligase (ADP-forming)
REACTION    ATP + L-glutamate + putrescine = ADP + phosphate +
            gamma-L-glutamylputrescine [RN:R07414]
ALL_REAC    R07414
SUBSTRATE   ATP [CPD:C00002];
            L-glutamate [CPD:C00025];
            putrescine [CPD:C00134]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            gamma-L-glutamylputrescine [CPD:C15699]
COMMENT     Forms part of a novel bacterial putrescine utilization pathway in
            Escherichia coli.
REFERENCE   1  [PMID:15590624]
  AUTHORS   Kurihara S, Oda S, Kato K, Kim HG, Koyanagi T, Kumagai H, Suzuki H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12.
  JOURNAL   J. Biol. Chem. 280 (2005) 4602-8.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K09470  gamma-glutamylputrescine synthase
GENES       ECO: b1297(ycjK)
            ECJ: JW5201(puuA)
            ECE: Z2491
            ECS: ECs1874
            ECW: EcE24377A_1506(puuA)
            ECX: EcHS_A1412
            SFL: SF1302
            SFX: S1384
            SFV: SFV_1311
            SSN: SSON_1843
            SBO: SBO_1765
            SDY: SDY_1947
            SPE: Spro_2068
            PPF: Pput_1342 Pput_1455 Pput_2566 Pput_5090 Pput_5091 Pput_5208
            PMY: Pmen_0341 Pmen_0342 Pmen_2634 Pmen_2858 Pmen_4525
            SBM: Shew185_1165 Shew185_2138
            SSE: Ssed_1060
            SPL: Spea_0945
            MMW: Mmwyl1_3517 Mmwyl1_3524
            PLA: Plav_1297
            SMD: Smed_0302
            OAN: Oant_3936
            XAU: Xaut_1939
            RSQ: Rsph17025_0864 Rsph17025_0866
            ACR: Acry_0538
            KRA: Krad_1637
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.1.11
            ExPASy - ENZYME nomenclature database: 6.3.1.11
            ExplorEnz - The Enzyme Database: 6.3.1.11
            ERGO genome analysis and discovery system: 6.3.1.11
            BRENDA, the Enzyme Database: 6.3.1.11
            CAS: 914090-78-1
///
ENTRY       EC 6.3.1.12                 Enzyme
NAME        D-aspartate ligase;
            Aslfm;
            UDP-MurNAc-pentapeptide:D-aspartate ligase;
            D-aspartic acid-activating enzyme
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-ammonia (or amine) ligases (amide synthases)
SYSNAME     D-aspartate:[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D
            -Ala-D-Ala)]n ligase (ADP-forming)
REACTION    ATP + D-aspartate +
            [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
            Ala)]n =
            [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-
            Lys-D-Ala-D-Ala)]n + ADP + phosphate
SUBSTRATE   ATP [CPD:C00002];
            D-aspartate [CPD:C00402];
            [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
            Ala)]n
PRODUCT     [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-
            Lys-D-Ala-D-Ala)]n;
            ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     This enzyme forms part of the peptidoglycan assembly pathway of
            Gram-positive bacteria grown in medium containing D-Asp. Normally,
            the side chains the acylate the 6-amino group of the L-lysine
            residue contain L-Ala-L-Ala but these amino acids are replaced by
            D-Asp when D-Asp is included in the medium. Hybrid chains containing
            L-Ala-D-Asp, L-Ala-L-Ala-D-Asp or D-Asp-L-Ala are not formed [4].
            The enzyme belongs in the ATP-grasp protein superfamily [3,4]. The
            enzyme is highly specific for D-aspartate, as L-aspartate,
            D-glutamate, D-alanine, D-iso-asparagine and D-malic acid are not
            substrates [4]. In Enterococcus faecium, the substrate D-aspartate
            is produced by EC 5.1.1.13, aspartate racemase [4]
REFERENCE   1  [PMID:4262567]
  AUTHORS   Staudenbauer W, Strominger JL.
  TITLE     Activation of D-aspartic acid for incorporation into peptidoglycan.
  JOURNAL   J. Biol. Chem. 247 (1972) 5095-102.
REFERENCE   2  [PMID:4626717]
  AUTHORS   Staudenbauer W, Willoughby E, Strominger JL.
  TITLE     Further studies of the D-aspartic acid-activating enzyme of
            Streptococcus faecalis and its attachment to the membrane.
  JOURNAL   J. Biol. Chem. 247 (1972) 5289-96.
REFERENCE   3  [PMID:9416615]
  AUTHORS   Galperin MY, Koonin EV.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity.
  JOURNAL   Protein. Sci. 6 (1997) 2639-43.
REFERENCE   4  [PMID:16510449]
  AUTHORS   Bellais S, Arthur M, Dubost L, Hugonnet JE, Gutmann L, van
            Heijenoort J, Legrand R, Brouard JP, Rice L, Mainardi JL.
  TITLE     Aslfm, the D-aspartate ligase responsible for the addition of
            D-aspartic acid onto the peptidoglycan precursor of Enterococcus
            faecium.
  JOURNAL   J. Biol. Chem. 281 (2006) 11586-94.
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.1.12
            ExPASy - ENZYME nomenclature database: 6.3.1.12
            ExplorEnz - The Enzyme Database: 6.3.1.12
            ERGO genome analysis and discovery system: 6.3.1.12
            BRENDA, the Enzyme Database: 6.3.1.12
///
ENTRY       EC 6.3.1.-                  Enzyme
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid--ammonia (or amine) ligases (amide synthases)
REACTION    Cobyrinate + 2 L-Glutamine + 2 ATP + 2 H2O <=> Cob(II)yrinate a,c
            diamide + 2 L-Glutamate + 2 ADP + 2 Orthophosphate [RN:R05815]
SUBSTRATE   Cobyrinate [CPD:C05773];
            L-Glutamine [CPD:C00064];
            ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     Cob(II)yrinate a,c diamide [CPD:C06504];
            L-Glutamate [CPD:C00025];
            ADP [CPD:C00008];
            Orthophosphate [CPD:C00009]
///
ENTRY       EC 6.3.2.1                  Enzyme
NAME        pantoate---beta-alanine ligase;
            pantothenate synthetase;
            pantoate activating enzyme;
            pantoic-activating enzyme;
            D-pantoate:beta-alanine ligase (AMP-forming)
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     (R)-pantoate:beta-alanine ligase (AMP-forming)
REACTION    ATP + (R)-pantoate + beta-alanine = AMP + diphosphate +
            (R)-pantothenate [RN:R02473]
ALL_REAC    R02473
SUBSTRATE   ATP [CPD:C00002];
            (R)-pantoate [CPD:C00522];
            beta-alanine [CPD:C00099]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            (R)-pantothenate [CPD:C00864]
REFERENCE   1  [PMID:14377603]
  AUTHORS   GINOZA HS, ALTENBERN RA.
  TITLE     The pantothenate-synthesizing enzyme in cell-free extracts of
            Brucella abortus, strain 19.
  JOURNAL   Arch. Biochem. 56 (1955) 537-41.
REFERENCE   2  [PMID:12999714]
  AUTHORS   MAAS WK.
  TITLE     Pantothenate studies.  III.  Description of the extracted
            pantothenate-synthesizing enzyme of Escherichia coli.
  JOURNAL   J. Biol. Chem. 198 (1952) 23-32.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3
  AUTHORS   Maas, W.K.
  TITLE     Mechanism of the enzymatic synthesis of pantothenate from
            beta-alanine and pantoate.
  JOURNAL   Fed. Proc. 15 (1956) 305-306.
PATHWAY     PATH: map00410  beta-Alanine metabolism
            PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K01918  pantoate--beta-alanine ligase
GENES       ATH: AT5G48840(PANC)
            OSA: 4334806
            CME: CMH138C
            SCE: YIL145C(PAN6)
            AGO: AGOS_AFR282W
            PIC: PICST_57860(PAN4)
            CGR: CAGL0H06523g
            SPO: SPAC5H10.08c(pan6)
            ANI: AN0205.2
            AFM: AFUA_5G11040
            AOR: AO090026000745
            CNE: CND05630
            DDI: DDB_0231511
            ECO: b0133(panC)
            ECJ: JW0129(panC)
            ECE: Z0144(panC)
            ECS: ECs0137
            ECC: c0164(panC)
            ECI: UTI89_C0147(panC)
            ECP: ECP_0142
            ECV: APECO1_1852(panC)
            ECW: EcE24377A_0136(panC)
            ECX: EcHS_A0137
            STY: STY0199(panC)
            STT: t0182(panC)
            SPT: SPA0187(panC)
            SEC: SC0181(panC)
            STM: STM0181(panC)
            YPE: YPO3402(panC)
            YPK: y0785(panC)
            YPM: YP_0283(panC)
            YPA: YPA_2903
            YPN: YPN_0687
            YPP: YPDSF_2954
            YPS: YPTB0729(panC)
            YPI: YpsIP31758_3344(panC)
            YEN: YE0719(panC)
            SFL: SF0130(panC)
            SFX: S0132(panC)
            SFV: SFV_0123(panC)
            SSN: SSON_0141(panC)
            SBO: SBO_0122(panC)
            SDY: SDY_0155(panC)
            ECA: ECA3322(panC)
            PLU: plu0871(panC)
            BUC: BU196(panC)
            BAS: BUsg190(panC)
            WBR: WGLp448(panC)
            SGL: SG0487
            ENT: Ent638_0680
            SPE: Spro_3992
            XFA: XF0230
            XFT: PD0188(panC)
            XCC: XCC1769(panC)
            XCB: XC_2467
            XCV: XCV1817(panC)
            XAC: XAC1786(panC)
            XOO: XOO2363(panC)
            XOM: XOO_2244(XOO2244)
            VCH: VC0591
            VCO: VC0395_A0122(panC)
            VVU: VV1_1642
            VVY: VV2764
            VPA: VP2507
            VFI: VF2170
            PPR: PBPRA3176
            PAE: PA4730
            PAU: PA14_62590(panC)
            PAP: PSPA7_5447(panC)
            PPU: PP_4700(panC)
            PPF: Pput_4565
            PST: PSPTO_0960(panC)
            PSB: Psyr_0827(panC)
            PSP: PSPPH_0853(panC)
            PFL: PFL_5278(panC)
            PFO: Pfl_4812
            PEN: PSEEN4736(panC)
            PMY: Pmen_3593
            PAR: Psyc_0117(panC)
            PCR: Pcryo_0126
            PRW: PsycPRwf_2130
            ACI: ACIAD3060(panC)
            SON: SO_0869(panC)
            SDN: Sden_3175
            SFR: Sfri_3281
            SAZ: Sama_0775
            SBL: Sbal_3495
            SBM: Shew185_0844
            SLO: Shew_3134
            SPC: Sputcn32_3133
            SSE: Ssed_3904
            SPL: Spea_0693
            SHE: Shewmr4_0725
            SHM: Shewmr7_3297
            SHN: Shewana3_0771 Shewana3_3409
            SHW: Sputw3181_0810
            ILO: IL2255(panC)
            CPS: CPS_4313(panC)
            PHA: PSHAa0601(panC)
            PAT: Patl_3932
            SDE: Sde_1061
            PIN: Ping_0579
            MAQ: Maqu_0666
            CBU: CBU_0423(panC)
            CBD: COXBU7E912_1650(panC)
            LPN: lpg2662(panC)
            LPF: lpl2589(panC)
            LPP: lpp2716(panC)
            MCA: MCA2315(panC)
            FTU: FTT1390(panC)
            FTF: FTF1390(panC)
            FTW: FTW_0498(panC)
            FTL: FTL_0673
            FTH: FTH_0676(panC)
            FTA: FTA_0708(panC)
            FTN: FTN_1353(panC)
            TCX: Tcr_1525
            NOC: Noc_0886
            AEH: Mlg_0565
            HHA: Hhal_0674
            HCH: HCH_06265(panC)
            CSA: Csal_3066
            ABO: ABO_0336(panC)
            MMW: Mmwyl1_4017
            AHA: AHA_3539(panC)
            BCI: BCI_0231(panC)
            RMA: Rmag_0416
            VOK: COSY_0385(panC)
            NME: NMB0871
            NMA: NMA1089(panC)
            NMC: NMC0812(panC)
            NGO: NGO0437
            CVI: CV_1636(panC)
            RSO: RSc2387(panC)
            REU: Reut_A0668
            REH: H16_A2959
            RME: Rmet_2774
            BMA: BMA0701(panC)
            BMV: BMASAVP1_A2312(panC)
            BML: BMA10299_A2975(panC)
            BMN: BMA10247_1624(panC)
            BXE: Bxe_A3488
            BVI: Bcep1808_2526
            BUR: Bcep18194_A5773
            BCN: Bcen_1831
            BCH: Bcen2424_2442
            BAM: Bamb_2489
            BPS: BPSL0991(panC)
            BPM: BURPS1710b_1204(panC)
            BPL: BURPS1106A_1049(panC)
            BPD: BURPS668_1043(panC)
            BTE: BTH_I0848(panC)
            PNU: Pnuc_0644
            BPE: BP3821(panC)
            BPA: BPP3965(panC)
            BBR: BB4438(panC)
            RFR: Rfer_3034
            POL: Bpro_0895
            PNA: Pnap_0933
            AAV: Aave_3853
            AJS: Ajs_3500
            VEI: Veis_0029
            MPT: Mpe_A1155
            HAR: HEAR0974(panC)
            MMS: mma_1105
            NEU: NE0073(panC)
            NET: Neut_2292
            NMU: Nmul_A0878
            EBA: ebA7120(panC)
            AZO: azo3145(panC)
            DAR: Daro_3186
            TBD: Tbd_2054
            MFA: Mfla_0596
            HPY: HP0006
            HPJ: jhp0006(panC)
            HPA: HPAG1_0006
            HHE: HH0035(panC)
            HAC: Hac_0259(panC)
            WSU: WS0112
            TDN: Tmden_0361
            CJE: Cj0297c(panC)
            CJR: CJE0342(panC)
            CJJ: CJJ81176_0320(panC)
            CJU: C8J_0274(panC)
            CJD: JJD26997_1667(panC)
            CFF: CFF8240_1370(panC)
            CCV: CCV52592_0252(panC) CCV52592_0840
            CHA: CHAB381_0501(panC)
            CCO: CCC13826_0583(panC)
            ABU: Abu_0215(panC)
            NIS: NIS_1533(panC)
            SUN: SUN_0318(panC)
            GSU: GSU1706(panC)
            GME: Gmet_1643
            GUR: Gura_2079
            PCA: Pcar_1829
            PPD: Ppro_3535
            DVU: DVU2448(panC)
            DVL: Dvul_0787
            DDE: Dde_1498
            BBA: Bd3561(panC)
            DPS: DP1943
            ADE: Adeh_3681
            AFW: Anae109_3808
            MXA: MXAN_2056(panC)
            SAT: SYN_00420
            SFU: Sfum_0369
            AMA: AM1089(panC)
            PUB: SAR11_1088(panC)
            MLO: mll0196
            MES: Meso_2560
            PLA: Plav_2791
            SME: SMc01880(panC)
            SMD: Smed_2060
            ATU: Atu3482(panC)
            ATC: AGR_L_2698
            RET: RHE_PF00001(panC)
            RLE: pRL120359(panC)
            BME: BMEI1593
            BMF: BAB1_0359
            BMS: BR0329(panC)
            BMB: BruAb1_0355(panC)
            BOV: BOV_0346(panC)
            OAN: Oant_0426
            BJA: blr2102(panC) blr5162(panC)
            BRA: BRADO4554(panC)
            BBT: BBta_4783(panC)
            RPA: RPA3155(panC)
            RPB: RPB_2388
            RPC: RPC_3332
            RPD: RPD_3063
            RPE: RPE_3413
            NWI: Nwi_1702
            NHA: Nham_2423
            BHE: BH05120(panC)
            BQU: BQ04310(panC)
            BBK: BARBAKC583_0476(panC)
            XAU: Xaut_4542
            CCR: CC_2166
            SIL: SPO0103(panC)
            SIT: TM1040_3439
            RSP: RSP_1757(panC)
            RSH: Rsph17029_0403
            RSQ: Rsph17025_2495
            RDE: RD1_0091(panC)
            PDE: Pden_1658
            MMR: Mmar10_1721
            HNE: HNE_1126(panC)
            ZMO: ZMO1971(panC)
            NAR: Saro_3319
            SAL: Sala_3003
            SWI: Swit_2788
            ELI: ELI_13700
            GOX: GOX1718
            GBE: GbCGDNIH1_0758
            ACR: Acry_0555
            RRU: Rru_A3320
            MAG: amb4371
            MGM: Mmc1_0039
            ABA: Acid345_4743
            BSU: BG11520(panC)
            BHA: BH1688(panC)
            BAN: BA1563(panC)
            BAR: GBAA1563(panC)
            BAA: BA_2082
            BAT: BAS1450
            BCE: BC1541
            BCA: BCE_1669(panC)
            BCZ: BCZK1423(panC)
            BCY: Bcer98_1263
            BTK: BT9727_1422(panC)
            BTL: BALH_1393
            BLI: BL02751(panC)
            BLD: BLi02377(panC)
            BCL: ABC2066(panC)
            BAY: RBAM_020570
            BPU: BPUM_1973
            OIH: OB3275
            GKA: GK2178
            SAU: SA2391(panC)
            SAV: SAV2598(panC)
            SAM: MW2517(panC)
            SAR: SAR2676(panC)
            SAS: SAS2483
            SAC: SACOL2614(panC)
            SAB: SAB2471c(panC)
            SAA: SAUSA300_2533(panC)
            SAO: SAOUHSC_02918
            SAJ: SaurJH9_2620
            SAH: SaurJH1_2674
            SEP: SE2140
            SER: SERP2151(panC)
            SHA: SH0182(panC)
            SSP: SSP0155
            LMO: lmo1901(panC)
            LMF: LMOf2365_1930(panC)
            LIN: lin2015(panC)
            LWE: lwe1920(panC)
            EFA: EF1859(panC)
            CAC: CAC2915(panC)
            CNO: NT01CX_1072(panC)
            CTH: Cthe_0901
            CDF: CD1512(panC)
            CBO: CBO0424(panC)
            CBA: CLB_0457(panC)
            CBH: CLC_0490(panC)
            CBF: CLI_0509(panC)
            CBE: Cbei_2609
            CKL: CKL_0638(panC)
            CHY: CHY_2376(panC)
            DSY: DSY0211
            DRM: Dred_0161 Dred_1789
            SWO: Swol_0102
            CSC: Csac_2709
            MTA: Moth_0141
            MTU: Rv3602c(panC)
            MTC: MT3707(panC)
            MBO: Mb3632c(panC)
            MBB: BCG_3666c(panC)
            MLE: ML0230(panC)
            MPA: MAP0456(panC)
            MAV: MAV_0551(panC)
            MSM: MSMEG_6097(panC)
            MVA: Mvan_5364
            MGI: Mflv_1424
            MMC: Mmcs_4762
            MKM: Mkms_4848
            MJL: Mjls_5148
            CGL: NCgl0112(cgl0113) NCgl2595(cgl2688)
            CGB: cg0148(panC) cg2975(panC2)
            CEF: CE0115(panC) CE2534
            CDI: DIP1993 DIP2357(panC)
            CJK: jk0286(panC)
            NFA: nfa4060(panC)
            RHA: RHA1_ro04415
            SCO: SCO3383(SCE126.01c)
            SMA: SAV4687(panC)
            TWH: TWT063(panC)
            TWS: TW073(panC)
            LXX: Lxx21410(panC)
            CMI: CMM_0853(panC)
            ART: Arth_0160
            AAU: AAur_0147(panC)
            NCA: Noca_0460
            TFU: Tfu_2884
            FRA: Francci3_4375
            FAL: FRAAL3483 FRAAL5463 FRAAL6371(panC) FRAAL6670(panC)
            ACE: Acel_0211
            KRA: Krad_0575
            SEN: SACE_0406(panC)
            STP: Strop_4283
            RXY: Rxyl_2469
            RBA: RB3735(panC)
            LIL: LA2514(panC)
            LIC: LIC11454(panC)
            LBJ: LBJ_1667(panC)
            LBL: LBL_1886(panC)
            SYN: sll1249(panC)
            SYW: SYNW2027(panC)
            SYC: syc0399_d(panC)
            SYF: Synpcc7942_1151
            SYD: Syncc9605_0416
            SYE: Syncc9902_1914
            SYG: sync_0483(panC)
            SYR: SynRCC307_2069
            SYX: SynWH7803_0474
            CYA: CYA_2663(panC)
            CYB: CYB_2425(panC)
            TEL: tll2450(panC)
            GVI: gll1806
            ANA: alr2936(panC)
            AVA: Ava_0964
            PMA: Pro1746(cmk)
            PMM: PMM1590(panC)
            PMT: PMT1689(panC)
            PMN: PMN2A_1165
            PMI: PMT9312_1682
            PMB: A9601_17991(cmk)
            PMC: P9515_17771(cmk)
            PMF: P9303_22471(panC)
            PMG: P9301_17821(cmk)
            PME: NATL1_20401(cmk)
            TER: Tery_2799
            BTH: BT_4308
            BFR: BF1003
            BFS: BF0924(panC)
            PGI: PG0477(panC)
            SRU: SRU_1411(panC)
            CHU: CHU_3835(panC)
            GFO: GFO_3544(panC)
            FJO: Fjoh_0825
            FPS: FP0108(panC)
            CTE: CT1647(panC)
            CCH: Cag_1707
            CPH: Cpha266_0553
            PVI: Cvib_1423
            PLT: Plut_1634
            DET: DET0804(panC)
            DEH: cbdb_A782(panC)
            DEB: DehaBAV1_0728
            RRS: RoseRS_0744
            RCA: Rcas_0333
            DRA: DR_1164
            DGE: Dgeo_0670
            TTH: TTC1416
            TTJ: TTHA1775
            AAE: aq_2132(panC)
            TMA: TM1077
            TPT: Tpet_1667
            TME: Tmel_1610
            FNO: Fnod_1571
STRUCTURES  PDB: 1IHO  1MOP  1N2B  1N2E  1N2G  1N2H  1N2I  1N2J  1N2O  1UFV  
                 1V8F  2A7X  2A84  2A86  2A88  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.1
            ExPASy - ENZYME nomenclature database: 6.3.2.1
            ExplorEnz - The Enzyme Database: 6.3.2.1
            ERGO genome analysis and discovery system: 6.3.2.1
            BRENDA, the Enzyme Database: 6.3.2.1
            CAS: 9023-49-8
///
ENTRY       EC 6.3.2.2                  Enzyme
NAME        glutamate---cysteine ligase;
            gamma-glutamylcysteine synthetase;
            gamma-glutamyl-L-cysteine synthetase;
            gamma-glutamylcysteinyl synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     L-glutamate:L-cysteine gamma-ligase (ADP-forming)
REACTION    ATP + L-glutamate + L-cysteine = ADP + phosphate +
            gamma-L-glutamyl-L-cysteine [RN:R00894]
ALL_REAC    R00894
SUBSTRATE   ATP [CPD:C00002];
            L-glutamate [CPD:C00025];
            L-cysteine [CPD:C00097]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            gamma-L-glutamyl-L-cysteine [CPD:C00669]
INHIBITOR   S-Butyl-DL-homocysteine-[S,R]-sulfoximine [CPD:C04543]
COMMENT     Can use L-aminohexanoate in place of glutamate.
REFERENCE   1  [PMID:3500856]
  AUTHORS   Mackinnon CM, Carter PE, Smyth SJ, Dunbar B, Fothergill JE.
  TITLE     Molecular cloning of cDNA for human complement component C1s. The
            complete amino acid sequence.
  JOURNAL   Eur. J. Biochem. 169 (1987) 547-53.
  ORGANISM  human [GN:hsa]
REFERENCE   2  [PMID:13061393]
  AUTHORS   SNOKE JE, YANARI S, BLOCH K.
  TITLE     Synthesis of glutathione from gamma-glutamylcysteine.
  JOURNAL   J. Biol. Chem. 201 (1953) 573-86.
  ORGANISM  pigeon
REFERENCE   3  [PMID:14381401]
  AUTHORS   MANDELES S, BLOCK K.
  TITLE     Enzymatic synthesis of gamma-glutamylcysteine.
  JOURNAL   J. Biol. Chem. 214 (1955) 639-46.
  ORGANISM  pigeon, pig [GN:ssc]
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00480  Glutathione metabolism
ORTHOLOGY   KO: K01919  glutamate--cysteine ligase
GENES       HSA: 2729(GCLC) 2730(GCLM)
            MMU: 14629(Gclc)
            RNO: 25283(Gclc) 29739(Gclm)
            CFA: 609822(GCLC) 612283(GCLM)
            GGA: 421894(GCLC) 424492(GCLM)
            XLA: 380105(gclm)
            DRE: 326857(gclc) 333974(gclm)
            SPU: 590426(LOC590426)
            DME: Dmel_CG2259(Gclc) Dmel_CG4917(wfs1) Dmel_CG4919(Gclm)
            CEL: E01A2.1 F37B12.2(gcs-1)
            OSA: 4337696
            CME: CMG141C
            SCE: YJL101C(GSH1)
            AGO: AGOS_AFR086C
            PIC: PICST_62151(GSH1)
            CGR: CAGL0L03630g
            SPO: SPAC22F3.10c(gcs1) SPCC737.06c
            ANI: AN3150.2
            AFM: AFUA_3G13900 AFUA_3G14280
            AOR: AO090012000764 AO090020000623
            CNE: CNN00350
            DDI: DDB_0231403(gcsA)
            PFA: PFI0925w
            TAN: TA03765
            TPV: TP03_0084
            TET: TTHERM_00250970 TTHERM_00250980
            TBR: Tb10.389.1360
            TCR: 507625.99 507787.100
            LMA: LmjF18.1660
            ECO: b0581(ybdK) b2688(gshA)
            ECJ: JW2663(gshA)
            ECE: Z3989(gshA)
            ECS: ECs3550
            ECC: c3245(gshA)
            ECI: UTI89_C3050(gshA)
            ECP: ECP_2653
            ECV: APECO1_3833(gshA)
            ECW: EcE24377A_2971(gshA)
            ECX: EcHS_A2824(gshA)
            STY: STY2944(gshA)
            STT: t2715(gshA)
            SPT: SPA2677(gshA)
            SEC: SC2753(gshA)
            STM: STM2818(gshA)
            YPE: YPO3301(gshA)
            YPK: y0887(gshA)
            YPM: YP_0385(gshA)
            YPA: YPA_2843
            YPN: YPN_0793
            YPP: YPDSF_3060
            YPS: YPTB0829(gshA)
            YPI: YpsIP31758_3234(gshA)
            YEN: YE0838(b2688)
            SFL: SF2715(gshA)
            SFX: S2902(gshA)
            SFV: SFV_2816(gshA)
            SSN: SSON_2832(gshA)
            SBO: SBO_2829(gshA)
            SDY: SDY_2885(gshA)
            ECA: ECA3363(gshA)
            PLU: plu1252(gshA)
            BUC: BU407(gshA)
            BAS: BUsg392(gshA)
            BAB: bbp368(gshA)
            WBR: WGLp247(gshA)
            SGL: SG0541
            ENT: Ent638_3168
            KPN: KPN_03019(gshA)
            SPE: Spro_0847
            HSO: HS_0287(gshA)
            PMU: PM1048
            MSU: MS1683(gshA)
            APL: APL_1408(gshA)
            XFA: XF1428
            XFT: PD0655(gshI)
            XCC: XCC3396(gsh1)
            XCB: XC_0768
            XCV: XCV0782(gsh1)
            XAC: XAC0728(gsh1)
            XOO: XOO3873(gsh1) XOO3877(gsh1)
            XOM: XOO_3659(XOO3659)
            VCH: VC0556
            VCO: VC0395_A0090(gshA)
            VVU: VV1_1606
            VVY: VV2794
            VPA: VP2539
            VFI: VF0543 VF0973
            PPR: PBPRA3047
            PAE: PA5203(gshA)
            PAU: PA14_68730(gshA)
            PAP: PSPA7_5948(gshA)
            PPU: PP_0243(gshA)
            PPF: Pput_0258
            PST: PSPTO_0325(gshA)
            PSB: Psyr_0255
            PSP: PSPPH_0243(gshA)
            PFL: PFL_0273(gshA)
            PFO: Pfl_0257
            PEN: PSEEN0224(gshA)
            PMY: Pmen_0356
            PAR: Psyc_0035(gshA)
            PCR: Pcryo_0043
            PRW: PsycPRwf_0046
            ACI: ACIAD3549(gshA)
            SON: SO_3559(gshA)
            SDN: Sden_1219
            SFR: Sfri_1072 Sfri_3430
            SAZ: Sama_1058
            SBL: Sbal_1031
            SBM: Shew185_1098
            SLO: Shew_1227
            SPC: Sputcn32_1036
            SSE: Ssed_1329
            SPL: Spea_1208
            SHE: Shewmr4_2980
            SHM: Shewmr7_3062
            SHN: Shewana3_3160
            SHW: Sputw3181_3129
            ILO: IL1731(gshA)
            CPS: CPS_4078(gshA)
            PHA: PSHAa0937(gshA) PSHAb0107(gshA)
            PAT: Patl_1366
            SDE: Sde_3583
            PIN: Ping_3373
            MAQ: Maqu_0465
            CBU: CBU_1874
            CBD: COXBU7E912_0105(gshA)
            LPN: lpg1847
            LPF: lpl1812
            LPP: lpp1811
            MCA: MCA2467(gshA)
            FTU: FTT0367c(gshA)
            FTF: FTF0367c(gshA)
            FTW: FTW_1701(gshA)
            FTL: FTL_1304
            FTH: FTH_1276(gshA)
            FTA: FTA_1379(gshA)
            FTN: FTN_0277(gshA)
            TCX: Tcr_1824
            NOC: Noc_1606
            AEH: Mlg_1207
            HCH: HCH_06422(gshA)
            CSA: Csal_2654
            ABO: ABO_0263(gshA)
            MMW: Mmwyl1_0750
            AHA: AHA_0720(gshA)
            DNO: DNO_1217(gshA)
            BCI: BCI_0201(gshA)
            RMA: Rmag_1015
            VOK: COSY_0917(gshA)
            NME: NMB1037
            NMA: NMA1449(gshA)
            NMC: NMC1175(gshA)
            NGO: NGO0680
            CVI: CV_4276
            RSO: RSc0344(RS03311)
            REU: Reut_A0293(gshA)
            REH: H16_A0322(gshA)
            RME: Rmet_0242
            BMA: BMA0117(gshA) BMA3215
            BMV: BMASAVP1_A0189(gshA-1) BMASAVP1_A2834(gshA-2)
            BML: BMA10299_A1403(gshA-1) BMA10299_A2251(gshA-2)
            BMN: BMA10247_2302(gshA-3) BMA10247_2325(gshA-1)
                 BMA10247_2830(gshA-2)
            BXE: Bxe_A4188 Bxe_A4484
            BVI: Bcep1808_3298
            BUR: Bcep18194_A6193(gshA) Bcep18194_A6505
            BCN: Bcen_2250 Bcen_2536
            BCH: Bcen2424_2864 Bcen2424_3149
            BAM: Bamb_2919 Bamb_3202
            BPS: BPSL0102 BPSL0436(gshA)
            BPM: BURPS1710b_0324(gshA) BURPS1710b_0654(gshA)
            BPL: BURPS1106A_0134(gshA) BURPS1106A_0489(gshA)
            BPD: BURPS668_0118(gshA) BURPS668_0470(gshA)
            BTE: BTH_I0087(gshA-1) BTH_I0409(gshA-2)
            BPA: BPP4089(gshA)
            BBR: BB4560(gshA)
            RFR: Rfer_0763 Rfer_3571
            POL: Bpro_3399 Bpro_4583
            PNA: Pnap_1308
            AAV: Aave_2262
            VEI: Veis_0551
            MPT: Mpe_A0173
            HAR: HEAR1064(gshA)
            MMS: mma_0171(gshA1) mma_1166(gshA2)
            NEU: NE1294
            NET: Neut_0954
            NMU: Nmul_A0216(gshA)
            EBA: ebA2547
            AZO: azo1744 azo2276(ybdK) azo3756(gshA)
            DAR: Daro_0011(gshA)
            TBD: Tbd_2408(gshA)
            MFA: Mfla_2516
            PCA: Pcar_3126
            BBA: Bd3760(gshA)
            DPS: DP1233
            ADE: Adeh_3793
            AFW: Anae109_3913
            MXA: MXAN_5806
            WOL: WD1188
            WBM: Wbm0721
            AMA: AM1186
            APH: APH_1231(gshA)
            ERU: Erum0770(gshA)
            ERW: ERWE_CDS_00700
            ERG: ERGA_CDS_00670
            ECN: Ecaj_0076
            ECH: ECH_0125(gshA)
            NSE: NSE_0308(gshA)
            PUB: SAR11_0698(gsh1)
            MLO: mll6902
            MES: Meso_0373
            PLA: Plav_0658
            SME: SMc00825(gsh1)
            SMD: Smed_0387
            ATU: Atu0656(gsh1)
            ATC: AGR_C_1167
            RET: RHE_CH00803(gsh)
            RLE: RL0855
            BME: BMEII0528
            BMF: BAB2_0476
            BMS: BRA0763
            BMB: BruAb2_0469
            BOV: BOV_A0711
            OAN: Oant_2998
            BJA: blr1164(gshA)
            BRA: BRADO6718(gshA)
            BBT: BBta_0820(gshA)
            RPA: RPA0822(gshA)
            RPB: RPB_4597
            RPC: RPC_0732
            RPD: RPD_0810
            RPE: RPE_0677
            NWI: Nwi_0182
            NHA: Nham_0250
            BHE: BH03970(gshA)
            BQU: BQ02990(gshA)
            BBK: BARBAKC583_0301
            XAU: Xaut_4204
            CCR: CC_3414
            SIL: SPO3626(gshA)
            SIT: TM1040_3076
            RSP: RSP_1005(gshA)
            RSQ: Rsph17025_0214
            JAN: Jann_3909
            RDE: RD1_4077(gsh)
            MMR: Mmar10_2240
            HNE: HNE_1374
            ZMO: ZMO1556(gsh)
            SWI: Swit_2364
            GOX: GOX1977
            GBE: GbCGDNIH1_2187
            ACR: Acry_1875
            RRU: Rru_A0570
            MAG: amb4023
            MGM: Mmc1_3679
            LMO: lmo2770
            LMF: LMOf2365_2760
            LIN: lin2913
            LWE: lwe2717
            SAG: SAG1821
            SAN: gbs1862
            SAK: SAK_1841
            SMU: SMU.267c
            STC: str1413
            STL: stu1413
            SSA: SSA_2186
            LPL: lp_2324(gshA)
            LSA: LSA0840
            LSL: LSL_0057(gshA)
            LBR: LVIS_1590
            LCA: LSEI_1196
            EFA: EF3089
            CAC: CAC1539
            CPE: CPE1573
            CPF: CPF_1825
            CPR: CPR_1545
            AMT: Amet_4636
            MTU: Rv3704c
            MBO: Mb3730c(gshA)
            MBB: BCG_3763c(gshA)
            MPA: MAP0306c(gshA)
            MAV: MAV_0399
            MSM: MSMEG_6250
            MMC: Mmcs_4882
            RHA: RHA1_ro05700
            FRA: Francci3_4511
            FAL: FRAAL6840(gshA)
            BAD: BAD_1213
            LIL: LA2106(gshA)
            LIC: LIC11812(gshA)
            LBJ: LBJ_1903(gshA)
            LBL: LBL_1381(gshA)
            PMB: A9601_17831
            PMC: P9515_17631
            PMF: P9303_22731
            PME: NATL1_20221
            MST: Msp_0528(gshA)
            HMA: rrnAC0866(gcs2)
STRUCTURES  PDB: 1V4G  1VA6  2D32  2D33  2GWC  2GWD  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.2
            ExPASy - ENZYME nomenclature database: 6.3.2.2
            ExplorEnz - The Enzyme Database: 6.3.2.2
            ERGO genome analysis and discovery system: 6.3.2.2
            BRENDA, the Enzyme Database: 6.3.2.2
            CAS: 9023-64-7
///
ENTRY       EC 6.3.2.3                  Enzyme
NAME        glutathione synthase;
            glutathione synthetase;
            GSH synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     gamma-L-glutamyl-L-cysteine:glycine ligase (ADP-forming)
REACTION    ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate +
            glutathione [RN:R00497]
ALL_REAC    R00497
SUBSTRATE   ATP [CPD:C00002];
            gamma-L-glutamyl-L-cysteine [CPD:C00669];
            glycine [CPD:C00037]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            glutathione [CPD:C00051]
INHIBITOR   Phosphinate [CPD:C05339]
REFERENCE   1
  AUTHORS   Law, M.Y. and Halliwell, B.
  TITLE     Purification and properties of glutathione synthetase from (Spinacia
            oleracea) leaves.
  JOURNAL   Plant Sci. 43 (1986) 185-191.
  ORGANISM  spinach
REFERENCE   2
  AUTHORS   Macnicol, P.K.
  TITLE     Homoglutathione and glutathione synthetases of legume seedlings -
            partial-purification and substrate-specificity.
  JOURNAL   Plant Sci. 53 (1987) 229-235.
  ORGANISM  Vigna radiata, Pisum sativum
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00480  Glutathione metabolism
ORTHOLOGY   KO: K01920  glutathione synthase
GENES       HSA: 2937(GSS)
            MMU: 14854(Gss)
            RNO: 25458(Gss)
            CFA: 442962(GSS)
            GGA: 428135(GSS)
            XLA: 394329(gssls-a)
            XTR: 493407(gss)
            SPU: 591446(LOC591446)
            DME: Dmel_CG6835(GS)
            CEL: M176.2
            ATH: AT5G27380(GSH2)
            OSA: 4351008
            CME: CMF043C
            SCE: YOL049W(GSH2)
            AGO: AGOS_ACR284C
            PIC: PICST_43206(GSH2)
            CGR: CAGL0F00825g
            SPO: SPAC3F10.04(gsa1)
            AFM: AFUA_5G06610
            AOR: AO090138000051 AO090701000193
            CNE: CNJ00850
            UMA: UM05504.1
            DDI: DDB_0231404(gshB)
            PFA: PFE0605c
            TAN: TA19700
            TPV: TP01_0264
            TET: TTHERM_01049360
            TBR: Tb927.7.4000
            TCR: 506659.30 508865.10
            LMA: LmjF14.0910
            ECO: b2947(gshB)
            ECJ: JW2914(gshB)
            ECE: Z4292(gshB)
            ECS: ECs3823
            ECC: c3533(gshB)
            ECI: UTI89_C3336(gshB)
            ECP: ECP_2941
            ECV: APECO1_3574(gshB)
            ECW: EcE24377A_3290(gshB)
            ECX: EcHS_A3105(gshB)
            STY: STY3248(gshB)
            STT: t3007(gshB)
            SPT: SPA2958(gshB)
            SEC: SC3035(gshB)
            STM: STM3095(gshB)
            YPE: YPO0935(gshB)
            YPK: y3321(gshB)
            YPM: YP_3507(gshB)
            YPA: YPA_0330
            YPN: YPN_3132
            YPP: YPDSF_0580
            YPS: YPTB3207(gshB)
            YPI: YpsIP31758_0836(gshB)
            SFL: SF2938(gshB)
            SFX: S3142(gshB)
            SFV: SFV_3001(gshB)
            SSN: SSON_3101(gshB)
            SBO: SBO_3043(gshB)
            SDY: SDY_3125(gshB)
            ECA: ECA3924(gshB)
            PLU: plu1184(gshB)
            BUC: BU547(gshB)
            BAS: BUsg529(gshB)
            BAB: bbp490(gshB)
            WBR: WGLp166(gshB)
            SGL: SG2022
            ENT: Ent638_3351
            KPN: KPN_03380(gshB)
            SPE: Spro_4026
            ASU: Asuc_1947
            XFA: XF1956
            XFT: PD0844(gshB)
            XCC: XCC2926(gshB)
            XCB: XC_1182
            XCV: XCV3234(gshB)
            XAC: XAC3103(gshB)
            XOO: XOO1745(gshB)
            XOM: XOO_1646(XOO1646)
            VCH: VC0468
            VCO: VC0395_A0020(gshB)
            VVU: VV1_1530 VV2_1204
            VVY: VV2868 VVA0031
            VPA: VP2611
            VFI: VF0435 VF0976
            PPR: PBPRA3138 PBPRB1479
            PAE: PA0407(gshB)
            PAU: PA14_05310(gshB)
            PAP: PSPA7_0507(gshB)
            PPU: PP_4993(gshB)
            PPF: Pput_3965 Pput_4867
            PST: PSPTO_5035(gshB)
            PSB: Psyr_0487
            PSP: PSPPH_0478(gshB)
            PFL: PFL_5828(gshB)
            PFO: Pfl_5309
            PEN: PSEEN5056(gshB)
            PMY: Pmen_0402 Pmen_2956
            PAR: Psyc_1752(gshB)
            PCR: Pcryo_2033
            PRW: PsycPRwf_0522
            ACI: ACIAD3518(gshB)
            SON: SO_0831(gshB)
            SDN: Sden_2975
            SFR: Sfri_0542 Sfri_2513
            SAZ: Sama_0574
            SBL: Sbal_3527
            SBM: Shew185_0808
            SLO: Shew_2899 Shew_3225
            SPC: Sputcn32_1216 Sputcn32_3162 Sputcn32_3824
            SSE: Ssed_3597 Ssed_3973
            SPL: Spea_0599 Spea_2295 Spea_3221
            SHE: Shewmr4_0689
            SHM: Shewmr7_3333
            SHN: Shewana3_1824 Shewana3_2339 Shewana3_3445
            SHW: Sputw3181_0781 Sputw3181_2944
            ILO: IL2217(gshB)
            CPS: CPS_1253(gshB)
            PHA: PSHAa2599(gshB)
            PAT: Patl_1152
            SDE: Sde_3635
            PIN: Ping_1287
            MAQ: Maqu_3766
            CBU: CBU_1875(gshB)
            CBD: COXBU7E912_0106(gshB)
            LPN: lpg1846(gshB)
            LPF: lpl1811(gshB)
            LPP: lpp1810(gshB)
            MCA: MCA2338(gshB)
            FTU: FTT0926(gshB)
            FTF: FTF0926(gshB)
            FTW: FTW_0819(gshB)
            FTL: FTL_1284
            FTH: FTH_1256(gshB)
            FTA: FTA_1357(gshB)
            FTN: FTN_0804(gshB)
            TCX: Tcr_1597 Tcr_1825
            AEH: Mlg_0354
            HHA: Hhal_0935
            HCH: HCH_00547(gshB)
            CSA: Csal_0057
            ABO: ABO_0110(gshB)
            MMW: Mmwyl1_4323
            AHA: AHA_3128(gshB)
            BCI: BCI_0482(gshB)
            RMA: Rmag_0051
            VOK: COSY_0055(gshB)
            NME: NMB1559
            NMA: NMA1747(gshB)
            NMC: NMC1477(gshB)
            NGO: NGO1217
            CVI: CV_4275(gshB)
            RSO: RSc0345(gshB)
            REU: Reut_A0294
            REH: H16_A0323(gshB)
            RME: Rmet_0243
            BMA: BMA3214(gshB)
            BMV: BMASAVP1_A0188(gshB)
            BML: BMA10299_A1404(gshB)
            BMN: BMA10247_2831(gshB)
            BXE: Bxe_A4187
            BVI: Bcep1808_2963
            BUR: Bcep18194_A6192
            BCN: Bcen_2249
            BCH: Bcen2424_2863
            BAM: Bamb_2918
            BPS: BPSL0437(gshB)
            BPM: BURPS1710b_0655(gshB)
            BPL: BURPS1106A_0490(gshB)
            BPD: BURPS668_0471(gshB)
            BTE: BTH_I0410(gshB)
            PNU: Pnuc_1954
            BPE: BP1499(gshB)
            BPA: BPP1965(gshB)
            BBR: BB2152(gshB)
            RFR: Rfer_0765
            POL: Bpro_4540
            PNA: Pnap_3736
            AAV: Aave_4539
            AJS: Ajs_3907
            VEI: Veis_0926
            MPT: Mpe_A0180
            HAR: HEAR0146(gshB)
            MMS: mma_0172(gshB)
            NEU: NE1295(gshB)
            NET: Neut_0953
            NMU: Nmul_A0217
            EBA: ebA2546(gshB)
            AZO: azo3755(gshB)
            DAR: Daro_0010
            TBD: Tbd_2409
            MFA: Mfla_2517
            MXA: MXAN_0017(gshB)
            WOL: WD0322(gshB)
            WBM: Wbm0556
            AMA: AM203(gshB)
            APH: APH_0193(gshB)
            ERU: Erum6640(gshB)
            ERW: ERWE_CDS_06960(gshB)
            ERG: ERGA_CDS_06870(gshB)
            ECN: Ecaj_0670
            ECH: ECH_0336(gshB)
            NSE: NSE_0186(gshB)
            PUB: SAR11_0697(gshB)
            MLO: mll4735
            MES: Meso_3585
            PLA: Plav_0815 Plav_3589
            SME: SMb21586(gshB2) SMc00419(gshB1)
            SMD: Smed_3546 Smed_3641 Smed_4907
            ATU: Atu0310(gshB)
            ATC: AGR_C_538 AGR_L_1416
            RET: RHE_CH00322(gshB)
            RLE: RL0338
            BME: BMEI1996
            BMF: BAB1_2135(gshB)
            BMS: BR2131(gshB)
            BMB: BruAb1_2106(gshB)
            BOV: BOV_2047(gshB)
            OAN: Oant_0783 Oant_2963
            BJA: bll0668(gshB)
            BRA: BRADO0180(gshB)
            BBT: BBta_0180(gshB)
            RPA: RPA0322(gshB)
            RPB: RPB_0419
            RPC: RPC_0319
            RPD: RPD_0401
            RPE: RPE_0359
            NWI: Nwi_0117
            NHA: Nham_0145
            BHE: BH02420(gshB)
            BQU: BQ02290(gshB)
            BBK: BARBAKC583_1229(gshB)
            XAU: Xaut_0338
            CCR: CC_0141
            SIL: SPO0401(gshB)
            SIT: TM1040_0450
            RSP: RSP_1815(gshB)
            RSH: Rsph17029_0462
            RSQ: Rsph17025_0473
            JAN: Jann_0901
            RDE: RD1_1192(gshB)
            PDE: Pden_3960
            MMR: Mmar10_3016
            HNE: HNE_0301(gshB)
            ZMO: ZMO1913(gshB)
            NAR: Saro_2081
            SAL: Sala_0261
            SWI: Swit_0573
            ELI: ELI_05990
            GOX: GOX1861
            GBE: GbCGDNIH1_0112
            ACR: Acry_2025
            RRU: Rru_A3690
            MAG: amb4506
            MGM: Mmc1_3083
            LRE: Lreu_0061 Lreu_1395
            STP: Strop_0916
            SYN: slr1238(gshB)
            SYW: SYNW2309(gshB)
            SYC: syc1778_c(gshB)
            SYF: Synpcc7942_2324
            SYD: Syncc9605_2440
            SYE: Syncc9902_2121
            SYG: sync_2657(gshB)
            SYR: SynRCC307_2251(gshB)
            SYX: SynWH7803_2321(gshB)
            CYA: CYA_2216(gshB)
            CYB: CYB_1049(gshB)
            TEL: tlr0908(gshB)
            GVI: gll3682(gshB)
            ANA: all3859
            AVA: Ava_1836
            PMA: Pro0203(rimK)
            PMM: PMM0178(gshB)
            PMT: PMT2061(gshB)
            PMN: PMN2A_1546
            PMI: PMT9312_0180
            PMB: A9601_01961(gshB)
            PMC: P9515_02071(gshB)
            PMF: P9303_27361(gshB)
            PMG: P9301_01981(gshB)
            PMH: P9215_01961(gshB)
            PME: NATL1_02531(gshB)
            TER: Tery_4206
            GFO: GFO_1741(gshB)
STRUCTURES  PDB: 1GLV  1GSA  1GSH  1M0T  1M0W  2GLT  2HGS  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.3
            ExPASy - ENZYME nomenclature database: 6.3.2.3
            ExplorEnz - The Enzyme Database: 6.3.2.3
            ERGO genome analysis and discovery system: 6.3.2.3
            BRENDA, the Enzyme Database: 6.3.2.3
            CAS: 9023-62-5
///
ENTRY       EC 6.3.2.4                  Enzyme
NAME        D-alanine---D-alanine ligase;
            MurE synthetase [ambiguous];
            alanine:alanine ligase (ADP-forming);
            alanylalanine synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     D-alanine:D-alanine ligase (ADP-forming)
REACTION    ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine [RN:R01150]
ALL_REAC    R01150
SUBSTRATE   ATP [CPD:C00002];
            D-alanine [CPD:C00133]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            D-alanyl-D-alanine [CPD:C00993]
INHIBITOR   Phosphinate [CPD:C05339]
COMMENT     Involved with EC 6.3.2.7
            (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase) or EC
            6.3.2.13
            (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate
            ligase), EC 6.3.2.8 (UDP-N-acetylmuramate---L-alanine ligase), EC
            6.3.2.9 (UDP-N-acetylmuramoyl-L-alanine---D-glutamate ligase) and EC
            6.3.2.10 (UDP-N-acetylmuramoyl-tripeptide---D-alanyl-D-alanine
            ligase) in the synthesis of a cell-wall peptide (click here for
            diagram).
REFERENCE   1
  AUTHORS   Ito, E. and Strominger, J.L.
  TITLE     Enzymatic synthesis of the peptide in bacterial uridine nucleotides.
            II. Enzymatic synthesis and addition of D-alanyl-D-alanine.
  JOURNAL   J. Biol. Chem. 237 (1962) 2696-2703.
  ORGANISM  Staphylococcus aureus
REFERENCE   2
  AUTHORS   Neuhaus, F.C.
  TITLE     Kinetic studies on D-Ala-D-Ala synthetase.
  JOURNAL   Fed. Proc. 21 (1962) 229.
REFERENCE   3  [PMID:11699883]
  AUTHORS   van Heijenoort J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit.
  JOURNAL   Nat. Prod. Rep. 18 (2001) 503-19.
  ORGANISM  Staphylococcus aureus
PATHWAY     PATH: map00473  D-Alanine metabolism
            PATH: map00550  Peptidoglycan biosynthesis
ORTHOLOGY   KO: K01921  D-alanine-D-alanine ligase
GENES       ECO: b0092(ddlB) b0381(ddlA)
            ECJ: JW0090(ddlB) JW0372(ddlA)
            ECE: Z0102(ddlB) Z0477
            ECS: ECs0096 ECs0431
            ECC: c0110(ddl) c0487(ddl)
            ECI: UTI89_C0101(ddlB) UTI89_C0398(ddlA)
            ECP: ECP_0094 ECP_0440
            ECV: APECO1_1627(ddlA) APECO1_1894(ddlB)
            ECW: EcE24377A_0094(ddlB) EcE24377A_0406(ddlA)
            ECX: EcHS_A0098 EcHS_A0447
            STY: STY0150(ddlB) STY0412(ddlA)
            STT: t0134(ddlB) t2484(ddlA)
            SPT: SPA0132(ddlB)
            SEC: SC0127(ddlB) SC0421(ddlA)
            STM: STM0130(ddlB) STM0380(ddlA)
            YPE: YPO0557(ddl)
            YPK: y3624(ddlB)
            YPM: YP_3627(ddlB)
            YPA: YPA_3544
            YPN: YPN_0423
            YPP: YPDSF_3085
            YPS: YPTB0690(ddl)
            YPI: YpsIP31758_3385
            YEN: YE0674(ddl) YE3211(ddlA)
            SFL: SF0089(ddlB) SF0232(ddlA)
            SFX: S0091(ddlB) S0254(ddlA)
            SFV: SFV_0085(ddlB) SFV_0344(ddlA)
            SSN: SSON_0100(ddlB) SSON_0356(ddlA)
            SBO: SBO_0080(ddlB) SBO_0276(ddlA)
            SDY: SDY_0122(ddlB) SDY_0365(ddlA)
            ECA: ECA3813(ddl)
            PLU: plu3652(ddl)
            BAS: BUsg208(ddlB)
            BAB: bbp196(ddlB)
            WBR: WGLp217(ddlA)
            SGL: SG0899
            ENT: Ent638_0638 Ent638_0850
            KPN: KPN_00096(ddl)
            SPE: Spro_0763 Spro_1367
            BFL: Bfl474(ddlA)
            BPN: BPEN_490(ddlA)
            HIN: HI1140(ddl)
            HIT: NTHI1308(ddlB)
            HIP: CGSHiEE_06350(ddl)
            HIQ: CGSHiGG_09370(ddl)
            HDU: HD0821(ddlB)
            HSO: HS_0360(ddl)
            PMU: PM0144(ddlB)
            MSU: MS1664(ddlA)
            APL: APL_0020(ddlB)
            ASU: Asuc_1930
            XFA: XF0799
            XFT: PD1864(ddlB)
            XCC: XCC0222(ddlB) XCC0727(ddlB)
            XCB: XC_0232 XC_3508
            XCV: XCV0246(ddl) XCV0832(ddl)
            XAC: XAC0781(ddlB)
            XOO: XOO0352(ddlB) XOO3824(ddlB)
            XOM: XOO_0324(XOO0324) XOO_3602(XOO3602)
            VCH: VCA0572
            VCO: VC0395_0515(ddlA)
            VVU: VV2_0280
            VVY: VVA0785
            VPA: VPA0886
            VFI: VFA0570(ddl)
            PPR: PBPRA1964 PBPRB0927
            PAE: PA4201(ddlA) PA4410(ddlB)
            PAU: PA14_09600(ddlA) PA14_57320(ddlB)
            PPU: PP_1339(ddlB) PP_4346(ddlA)
            PPF: Pput_1516 Pput_1521
            PST: PSPTO_4182 PSPTO_4406
            PSB: Psyr_3919(ddl) Psyr_4100(ddl)
            PSP: PSPPH_3913(ddlA) PSPPH_4106(ddlB)
            PFL: PFL_5059(ddl) PFL_5194(ddl)
            PFO: Pfl_4671
            PEN: PSEEN4483(ddlB)
            PMY: Pmen_0924
            PAR: Psyc_1749(ddlB)
            PCR: Pcryo_2030
            PRW: PsycPRwf_0526
            ACI: ACIAD3515(ddlB)
            SON: SO_2217(ddlA)
            SDN: Sden_2354
            SFR: Sfri_2550
            SAZ: Sama_1903
            SBL: Sbal_2283
            SBM: Shew185_2043
            SLO: Shew_2133
            SPC: Sputcn32_1801
            SSE: Ssed_1920
            SPL: Spea_2422
            SHE: Shewmr4_2129
            SHM: Shewmr7_2205
            SHN: Shewana3_2307
            SHW: Sputw3181_2224
            ILO: IL0438(ddlB)
            CPS: CPS_4463
            PHA: PSHAa2502(ddlB)
            PAT: Patl_3517
            SDE: Sde_0850
            PIN: Ping_0036 Ping_1149
            MAQ: Maqu_2450
            CBU: CBU_1338
            CBD: COXBU7E912_1427
            LPN: lpg2612(ddlA)
            LPF: lpl2535(ddlA)
            LPP: lpp2665(ddlA)
            MCA: MCA2426(ddl)
            FTU: FTT0185(ddlB)
            FTF: FTF0185(ddlB)
            FTW: FTW_1906
            FTL: FTL_1910
            FTH: FTH_1509(ddlA) FTH_1833(ddlB)
            FTA: FTA_2017
            FTN: FTN_0161(ddlB)
            TCX: Tcr_0585
            NOC: Noc_2858
            AEH: Mlg_2190
            HHA: Hhal_2088
            HCH: HCH_05881 HCH_06188
            CSA: Csal_2188
            ABO: ABO_0600(ddlB)
            MMW: Mmwyl1_2612
            AHA: AHA_2404
            DNO: DNO_0979
            BCI: BCI_0388(ddlA)
            RMA: Rmag_0759
            VOK: COSY_0701(ddlB)
            NME: NMB0424
            NMA: NMA2060(ddlB)
            NMC: NMC1740(ddlB)
            NGO: NGO1531(ddl)
            CVI: CV_2472(ddl) CV_4341(ddl)
            RSO: RSc2842(ddl)
            REU: Reut_A2977(ddl)
            REH: H16_A3271(ddlB)
            RME: Rmet_3126
            BMA: BMA2549(ddlB)
            BMV: BMASAVP1_A0470(ddlB)
            BML: BMA10299_A1329(ddlB)
            BMN: BMA10247_3234(ddlB)
            BXE: Bxe_A0488
            BVI: Bcep1808_0537
            BUR: Bcep18194_A3647 Bcep18194_C6870
            BCN: Bcen_0079
            BCH: Bcen2424_0561
            BAM: Bamb_0465
            BPS: BPSL3023(ddlB)
            BPM: BURPS1710b_3542(ddlB)
            BPL: BURPS1106A_3548(ddlB)
            BPD: BURPS668_3523(ddlB)
            BTE: BTH_I1120
            PNU: Pnuc_0169
            BPE: BP3021(ddl)
            BPA: BPP3750(ddl)
            BBR: BB4196(ddl)
            RFR: Rfer_3423
            POL: Bpro_1077
            PNA: Pnap_3415
            AAV: Aave_0823
            AJS: Ajs_3668
            VEI: Veis_4572
            MPT: Mpe_A0464
            HAR: HEAR2809(ddlB)
            MMS: mma_3013
            NEU: NE0994(ddlB)
            NET: Neut_0243
            NMU: Nmul_A2491
            EBA: ebA1442(ddl)
            AZO: azo0886(ddlB)
            DAR: Daro_3496
            TBD: Tbd_0122(ddl)
            MFA: Mfla_2266
            HPY: HP0738(ddl)
            HPJ: jhp0675(ddl)
            HPA: HPAG1_0722
            HHE: HH0131(ddl)
            HAC: Hac_0681(ddlA)
            WSU: WS0438(ddl)
            TDN: Tmden_1208
            CJE: Cj0798c(ddlA)
            CJR: CJE0889(ddl)
            CJJ: CJJ81176_0819(ddlA)
            CJU: C8J_0749(ddlA)
            CJD: JJD26997_1212(ddlA)
            CFF: CFF8240_0808
            CCV: CCV52592_1152
            CHA: CHAB381_0572
            ABU: Abu_0745(ddlA)
            NIS: NIS_1097(ddlA)
            SUN: SUN_0177(ddlA)
            GSU: GSU3066(ddl)
            GME: Gmet_0415
            PCA: Pcar_2199
            PPD: Ppro_3286
            DVU: DVU0334
            DVL: Dvul_2649
            DDE: Dde_0366 Dde_3042 Dde_3043
            LIP: LI0682(ddlA)
            BBA: Bd0585(ddlA)
            DPS: DP0058
            ADE: Adeh_2449 Adeh_3774
            AFW: Anae109_1418 Anae109_3887
            MXA: MXAN_4097 MXAN_5601 MXAN_5741
            SAT: SYN_00412 SYN_01483
            SFU: Sfum_0712 Sfum_0713 Sfum_4102
            RPR: RP249(ddl)
            RTY: RT0241(ddlB)
            RCO: RC0333(ddl)
            RFE: RF_1035(ddl)
            RBE: RBE_0961(ddlB)
            RAK: A1C_01810(ddl)
            RBO: A1I_03850(ddl)
            RCM: A1E_01460(ddl)
            RRI: A1G_01910(ddl)
            OTS: OTBS_0598(ddlB)
            WOL: WD0095
            WBM: Wbm0570
            AMA: AM205(ddlB)
            PUB: SAR11_0021(ddlB)
            MLO: mll1551 mll1812
            MES: Meso_2004
            PLA: Plav_2424
            SME: SMc01871(ddl)
            SMD: Smed_2077
            ATU: Atu2089(ddl)
            ATC: AGR_C_3788
            RET: RHE_CH02464(ddlA) RHE_CH02843(ddlB)
            RLE: RL2801(ddlA) RL3301(ddlB)
            BME: BMEI0582(ddl) BMEI0727
            BMF: BAB1_1291 BAB1_1447
            BMS: BR1271(ddlA) BR1428(ddlB)
            BMB: BruAb1_1273(ddlA) BruAb1_1423(ddl)
            BOV: BOV_1232(ddlA) BOV_1385(ddlB)
            OAN: Oant_1747
            BJA: bll6599 blr3405(ddlA) blr6438(ddlA)
            BRA: BRADO2810(ddlA) BRADO5656(ddlB)
            BBT: BBta_5374(ddlA) BBta_6169(ddlB)
            RPA: RPA3525(ddlA)
            RPB: RPB_2001
            RPC: RPC_3301
            RPD: RPD_3389
            RPE: RPE_2113
            NWI: Nwi_1055
            NHA: Nham_1283
            BHE: BH11210(ddlB)
            BQU: BQ08830(ddlB)
            BBK: BARBAKC583_0944(ddlB)
            XAU: Xaut_0325
            CCR: CC_2543
            SIL: SPO1201(ddlB)
            SIT: TM1040_0686
            RSP: RSP_2111(ddlA)
            RSH: Rsph17029_0787
            RSQ: Rsph17025_0697
            JAN: Jann_2753
            RDE: RD1_3351(ddlB)
            PDE: Pden_1204 Pden_2406 Pden_4490
            MMR: Mmar10_2074
            HNE: HNE_0393
            ZMO: ZMO0834(ddl)
            NAR: Saro_1136
            SAL: Sala_1878
            SWI: Swit_3943
            ELI: ELI_01810
            GOX: GOX0161
            GBE: GbCGDNIH1_0426
            ACR: Acry_0066
            RRU: Rru_A0947
            MAG: amb3851
            MGM: Mmc1_0750
            ABA: Acid345_1551 Acid345_4592
            SUS: Acid_2799
            BSU: BG11932(ddlA)
            BHA: BH1621(ddlA)
            BAN: BA2610(ddlB)
            BAR: GBAA2610(ddlB)
            BAA: BA_0812
            BAT: BAS0230 BAS2435
            BCE: BC0257(ddl) BC2550(ddl)
            BCA: BCE_0265(ddl) BCE_2628(ddl)
            BCZ: BCZK0219(ddl) BCZK2356(ddl)
            BCY: Bcer98_0232
            BTK: BT9727_0217(ddl) BT9727_2390(ddl)
            BTL: BALH_0230(ddl)
            BLI: BL02193(ddl)
            BLD: BLi00543(ddl)
            BCL: ABC2907(ddl)
            BAY: RBAM_004900
            BPU: BPUM_0427
            OIH: OB1306(ddl)
            GKA: GK0223(ddl)
            SAU: SA1887(ddlA)
            SAV: SAV2083(ddlA)
            SAM: MW2006(ddlA)
            SAR: SAR2170
            SAS: SAS1987
            SAC: SACOL2074(ddl)
            SAB: SAB1967c
            SAA: SAUSA300_2039(ddl)
            SAO: SAOUHSC_02318
            SAJ: SaurJH9_2120
            SAH: SaurJH1_2158
            SEP: SE1681
            SER: SERP1690(ddl)
            SHA: SH0954(ddlA)
            SSP: SSP0800
            LMO: lmo0855(ddlA)
            LMF: LMOf2365_0872(ddl)
            LIN: lin0848(ddlA)
            LWE: lwe0848(ddlA)
            LLA: L140690(ddl)
            LLC: LACR_0387
            LLM: llmg_0360
            SPY: SPy_1421(ddlA)
            SPZ: M5005_Spy_1158(ddl)
            SPM: spyM18_1431
            SPG: SpyM3_1084(ddlA)
            SPS: SPs0780
            SPH: MGAS10270_Spy1229(ddlA)
            SPI: MGAS10750_Spy1266(ddlA)
            SPJ: MGAS2096_Spy1229(ddlA)
            SPK: MGAS9429_Spy1205(ddlA)
            SPF: SpyM50702(ddlA)
            SPA: M6_Spy1185(ddl)
            SPB: M28_Spy1152(ddl)
            SPN: SP_1671
            SPR: spr1515(ddl)
            SPD: SPD_1484(ddlA)
            SAG: SAG0767
            SAN: gbs0787
            SAK: SAK_0892(ddl)
            SMU: SMU.599
            STC: str1583(ddlA)
            STL: stu1583(ddlA)
            SSA: SSA_0691(ddlA)
            SGO: SGO_1447(ddlA)
            LPL: lp_2345(ddl)
            LJO: LJ0108
            LAC: LBA0137
            LSA: LSA0049(ddl)
            LSL: LSL_1083(ddlA)
            LDB: Ldb0185(ddl)
            LBU: LBUL_0161
            LBR: LVIS_1268
            LCA: LSEI_0143
            LGA: LGAS_0107
            LRE: Lreu_0477
            EFA: EF0843 EF2294(vanB)
            OOE: OEOE_0672
            STH: STH512
            CAC: CAC2895(ddlA)
            CPE: CPE0819(ddlB) CPE1315(ddlA)
            CPF: CPF_0816(ddl) CPF_1522(ddl)
            CPR: CPR_1312
            CTC: CTC00291 CTC00683(ddl)
            CNO: NT01CX_0559
            CTH: Cthe_1938
            CDF: CD1408(ddl)
            CBO: CBO0452(ddl)
            CBA: CLB_0493(ddlB)
            CBH: CLC_0526(ddlB)
            CBF: CLI_0538(ddlB)
            CBE: Cbei_0581
            CKL: CKL_2914(ddl)
            AMT: Amet_2954 Amet_3710 Amet_4591
            CHY: CHY_1346(ddl)
            DSY: DSY1579 DSY3690
            DRM: Dred_1796
            SWO: Swol_1155
            CSC: Csac_1372
            TTE: TTE2545(ddlA2)
            MTA: Moth_1140
            MTU: Rv2981c(ddl)
            MTC: MT3059(ddlA)
            MBO: Mb3005c(ddl)
            MBB: BCG_3002c(ddlA)
            MLE: ML1678(ddlA)
            MPA: MAP3019c(ddlA)
            MAV: MAV_3830
            MSM: MSMEG_2395
            MVA: Mvan_2143
            MGI: Mflv_4219
            MMC: Mmcs_1929
            MKM: Mkms_1975
            MJL: Mjls_1909
            CGL: NCgl1267(ddl)
            CGB: cg1493(ddl)
            CEF: CE1431
            CDI: DIP1131(ddl)
            CJK: jk0921(ddlA1-N) jk0922(ddlA1-C) jk1217(ddlA2)
            NFA: nfa42050(ddlA)
            RHA: RHA1_ro06507(ddlA)
            SCO: SCO3595(ddlA2) SCO5560(SC7A1.04)
            SMA: SAV2679(ddlA)
            TWH: TWT505(ddlA)
            TWS: TW257(ddlA)
            LXX: Lxx09710(ddlA)
            CMI: CMM_0263(ddlA) CMM_1346(ddlC) CMM_2970(ddlB)
            ART: Arth_2514
            AAU: AAur_2481(ddlA)
            PAC: PPA1359 PPA2338
            NCA: Noca_3486 Noca_4691
            TFU: Tfu_0633(ddl) Tfu_1640
            FRA: Francci3_3609
            FAL: FRAAL3074(ddlA) FRAAL5814(ddlA)
            ACE: Acel_2153
            KRA: Krad_1363
            SEN: SACE_6130(ddl) SACE_7389(ddlA)
            STP: Strop_1272 Strop_4584
            BLO: BL0345(ddlA)
            BAD: BAD_0186(ddlA)
            RXY: Rxyl_2329 Rxyl_2952
            FNU: FN1454
            RBA: RB13271(ddlA)
            CTR: CT762(murC)
            CTA: CTA_0832(murC-ddlA)
            CMU: TC0143
            CPN: CPn0905(murC)
            CPA: CP0961
            CPJ: CPj0905(murC_ddlA)
            CPT: CpB0937
            CCA: CCA00863(murC)
            CAB: CAB829
            CFE: CF0153(mudD)
            BGA: BG0199(ddlA)
            BAF: BAPKO_0203(ddlA)
            TPA: TP0670
            TDE: TDE2385
            LIL: LA2058 LA2699
            LIC: LIC11304(ddl) LIC11855(ddlA)
            LBJ: LBJ_1946(ddlA) LBJ_2005
            LBL: LBL_1045 LBL_1338(ddlA)
            SYN: slr1874(ddlA)
            SYW: SYNW1641(ddlB)
            SYC: syc1730_c
            SYF: Synpcc7942_2375
            SYD: Syncc9605_0849
            SYE: Syncc9902_1541
            SYG: sync_0734
            SYR: SynRCC307_0603(ddl)
            SYX: SynWH7803_1756(ddl)
            CYA: CYA_0110(ddlB)
            CYB: CYB_2109(ddlB)
            TEL: tll0523
            GVI: gll0297
            ANA: all0980
            AVA: Ava_0360(ddl) Ava_1814
            PMA: Pro1380(ddlA)
            PMM: PMM1306(ddlA)
            PMT: PMT0322(ddlA)
            PMN: PMN2A_0872
            PMI: PMT9312_1402
            PMB: A9601_15051(ddlA)
            PMC: P9515_14671(ddlA)
            PMF: P9303_19931(ddlA)
            PMG: P9301_14921(ddlA)
            PMH: P9215_15351
            PME: NATL1_17261(ddlA)
            TER: Tery_2970 Tery_2971 Tery_4217
            BTH: BT_3713
            BFR: BF0490
            BFS: BF0435(ddlA)
            PGI: PG0729(ddlA)
            SRU: SRU_2197
            CHU: CHU_0924(ddlA)
            GFO: GFO_2684(ddl)
            FJO: Fjoh_2618
            FPS: FP0653(ddl)
            CTE: CT1345(ddlA)
            CCH: Cag_0905
            CPH: Cpha266_1662
            PVI: Cvib_0722
            PLT: Plut_1331
            DET: DET0629
            DEH: cbdb_A616(ddl)
            DEB: DehaBAV1_0602
            RRS: RoseRS_3791
            RCA: Rcas_1090
            DRA: DR_0362
            DGE: Dgeo_2121
            TTH: TTC1223
            TTJ: TTHA1587
            AAE: aq_521(ddlA)
            TMA: TM0259
            TPT: Tpet_0665
            TME: Tmel_0081 Tmel_0486
            FNO: Fnod_1588
            MEM: Memar_0655
            MSI: Msm_0361
STRUCTURES  PDB: 1EHI  1IOV  1IOW  2DLN  2FB9  2I80  2I87  2I8C  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.4
            ExPASy - ENZYME nomenclature database: 6.3.2.4
            ExplorEnz - The Enzyme Database: 6.3.2.4
            ERGO genome analysis and discovery system: 6.3.2.4
            BRENDA, the Enzyme Database: 6.3.2.4
            CAS: 9023-63-6
///
ENTRY       EC 6.3.2.5                  Enzyme
NAME        phosphopantothenate---cysteine ligase;
            phosphopantothenoylcysteine synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     (R)-4'-phosphopantothenate:L-cysteine ligase
REACTION    CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate +
            N-[(R)-4'-phosphopantothenoyl]-L-cysteine [RN:R04231]
ALL_REAC    R04231;
            (other) R04230 R04233
SUBSTRATE   CTP [CPD:C00063];
            (R)-4'-phosphopantothenate [CPD:C03492];
            L-cysteine [CPD:C00097]
PRODUCT     CMP [CPD:C00055];
            diphosphate [CPD:C00013];
            N-[(R)-4'-phosphopantothenoyl]-L-cysteine [CPD:C04352]
COMMENT     Cysteine can be replaced by some of its derivatives.
REFERENCE   1  [PMID:13630913]
  AUTHORS   BROWN GM.
  TITLE     The metabolism of pantothenic acid.
  JOURNAL   J. Biol. Chem. 234 (1959) 370-8.
  ORGANISM  Escherichia coli [GN:eco], rat [GN:rno], Proteus morganii
REFERENCE   2  [PMID:11278255]
  AUTHORS   Strauss E, Kinsland C, Ge Y, McLafferty FW, Begley TP.
  TITLE     Phosphopantothenoylcysteine synthetase from Escherichia coli.
            Identification and characterization of the last unidentified
            coenzyme A biosynthetic enzyme in bacteria.
  JOURNAL   J. Biol. Chem. 276 (2001) 13513-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:12140293]
  AUTHORS   Kupke T.
  TITLE     Molecular characterization of the 4'-phosphopantothenoylcysteine
            synthetase domain of bacterial dfp flavoproteins.
  JOURNAL   J. Biol. Chem. 277 (2002) 36137-45.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00770  Pantothenate and CoA biosynthesis
ORTHOLOGY   KO: K01922  phosphopantothenate-cysteine ligase
GENES       HSA: 79717(PPCS)
            MMU: 106564(Ppcs)
            CFA: 475309(PPCS)
            TET: TTHERM_01309090
            ECO: b3639(dfp)
            ECE: Z5063(dfp)
            ECS: ECs4514
            ECC: c4463(dfp)
            ECI: UTI89_C4183(dfp)
            ECP: ECP_3737
            ECV: APECO1_2822(dfp)
            ECW: EcE24377A_4140(coaBC)
            ECX: EcHS_A3848(coaBC)
            STY: STY4064(dfp)
            STT: t3788(dfp)
            SPT: SPA3582(dfp)
            SEC: SC3653(dfp)
            STM: STM3730(dfp)
            YPE: YPO0048(dfp)
            YPK: y0093(dfp)
            YPM: YP_0049(dfp)
            YPA: YPA_3494
            YPN: YPN_3802
            YPP: YPDSF_3857
            YPS: YPTB0045(dfp)
            YPI: YpsIP31758_0060(coaBC)
            SFL: SF3678(dfp)
            SFX: S4090(dfp)
            SFV: SFV_3891(dfp)
            SSN: SSON_3767(dfp)
            SBO: SBO_3641(dfp)
            SDY: SDY_4069(dfp)
            ECA: ECA0144(dfp)
            PLU: plu4866(dfp)
            WBR: WGLp402(dfp)
            SGL: SG2209
            ENT: Ent638_0100
            KPN: KPN_03979(dfp)
            SPE: Spro_4843
            BPN: BPEN_637(dfp)
            HIN: HI0953(dfp)
            HIT: NTHI1126(dfp)
            HIP: CGSHiEE_07195
            HIQ: CGSHiGG_08340
            HDU: HD0733(dfp)
            HSO: HS_0143(coaBC)
            PMU: PM1153(dfp)
            MSU: MS1938(dfp)
            APL: APL_1969(dfp)
            ASU: Asuc_0012
            XFA: XF0149
            XFT: PD0118(dfp)
            XCC: XCC3859(dfp)
            XCB: XC_3943
            XCV: XCV4027(dfp)
            XAC: XAC3914(dfp)
            XOO: XOO0496(dfp)
            XOM: XOO_0463(XOO0463)
            VCH: VC0215
            VVU: VV1_0828
            VVY: VV0283
            VPA: VP0181
            VFI: VF0125
            PPR: PBPRA0201
            PAE: PA5320(dfp)
            PAU: PA14_70240(coaC)
            PAP: PSPA7_6096(coaBC)
            PPU: PP_5285(coaBC)
            PPF: Pput_5195
            PST: PSPTO_0085(coaBC)
            PSB: Psyr_0221
            PSP: PSPPH_0209(coaBC)
            PFL: PFL_6052(coaBC)
            PFO: Pfl_5540
            PEN: PSEEN5432(dfp)
            PMY: Pmen_4377
            PAR: Psyc_1833(dfp)
            PCR: Pcryo_2118
            PRW: PsycPRwf_0492
            ACI: ACIAD3125(dfp)
            SON: SO_4249(dfp)
            SDN: Sden_0325
            SFR: Sfri_3829
            SAZ: Sama_0326
            SBL: Sbal_0376
            SBM: Shew185_0375
            SLO: Shew_3482
            SPC: Sputcn32_0461
            SSE: Ssed_0384
            SPL: Spea_3838
            SHE: Shewmr4_3598
            SHM: Shewmr7_0358
            SHN: Shewana3_3771
            SHW: Sputw3181_0337
            ILO: IL0239(dfp)
            CPS: CPS_0182(coaBC)
            PHA: PSHAa2644(dfp)
            PAT: Patl_0045
            PIN: Ping_0057
            MAQ: Maqu_3563
            CBU: CBU_0886(coaBC)
            CBD: COXBU7E912_0950(coaBC)
            LPN: lpg2488
            LPF: lpl2408(dfp)
            LPP: lpp2552(dfp)
            MCA: MCA2784(coaBC)
            FTU: FTT1147c(dfp)
            FTF: FTF1147c(dfp)
            FTW: FTW_1186(coaBC)
            FTL: FTL_0808
            FTH: FTH_0802(dfp)
            FTA: FTA_0854(coaBC)
            FTN: FTN_1128(dfp)
            TCX: Tcr_1915
            NOC: Noc_2992
            AEH: Mlg_2847
            HHA: Hhal_2299
            HCH: HCH_01021(coaBC)
            CSA: Csal_2981
            ABO: ABO_0213(coaBC)
            MMW: Mmwyl1_0623
            AHA: AHA_0159(coaBC)
            DNO: DNO_0823(coaBC)
            BCI: BCI_0183(dfp)
            RMA: Rmag_0801
            VOK: COSY_0727(dfp)
            NME: NMB1658
            NMA: NMA1916
            NGO: NGO1307
            CVI: CV_3080(dfp)
            RSO: RSc2461(dfp)
            REU: Reut_A2747
            RME: Rmet_2887
            BMA: BMA2244(coaBC)
            BMV: BMASAVP1_A2660(coaBC)
            BML: BMA10299_A1035(coaBC)
            BMN: BMA10247_2114(coaBC)
            BUR: Bcep18194_A5846
            BAM: Bamb_2561
            BPS: BPSL0904(dfp)
            BPM: BURPS1710b_1120(coaBC)
            BPL: BURPS1106A_0969(coaBC)
            BPD: BURPS668_0965(coaBC)
            BTE: BTH_I0768(coaBC)
            BPE: BP1751(dfp)
            BPA: BPP1982(dfp)
            BBR: BB2170(dfp)
            RFR: Rfer_2647
            POL: Bpro_3180
            HAR: HEAR0843(dfp)
            NEU: NE1463(dfp)
            NET: Neut_0783
            NMU: Nmul_A2137
            EBA: ebA838(dfp)
            DAR: Daro_3141
            TBD: Tbd_2587
            MFA: Mfla_0314
            HAC: Hac_1211(dfp)
            CFF: CFF8240_0752(coaBC)
            CCV: CCV52592_1267(coaBC)
            CHA: CHAB381_0969(coaBC)
            ABU: Abu_2203(dfp)
            NIS: NIS_1104(dfp)
            SUN: SUN_1837(dfp)
            GSU: GSU1124(coaBC)
            GME: Gmet_2673
            GUR: Gura_2927
            PCA: Pcar_2011
            PPD: Ppro_0088
            DVU: DVU3353(coaBC)
            DDE: Dde_0039
            LIP: LI0582
            BBA: Bd3562(dfp)
            DPS: DP1673
            ADE: Adeh_2372
            AFW: Anae109_1495
            MXA: MXAN_4395(coaBC)
            SAT: SYN_02177
            SFU: Sfum_0467
            APH: APH_1297
            ERU: Erum0410(dfp)
            ERW: ERWE_CDS_00300(dfp)
            ERG: ERGA_CDS_00300(dfp)
            ECN: Ecaj_0033 Ecaj_0638
            ECH: ECH_0061
            PUB: SAR11_0405(dfp)
            MLO: mlr3167
            MES: Meso_4055
            PLA: Plav_3656
            SME: SMc01161(dfp)
            ATU: Atu0316(dfp)
            ATC: AGR_C_552
            RET: RHE_CH00342(dfp)
            RLE: RL0357(coaBC)
            BME: BMEII0235
            BMF: BAB2_1024(coaBC)
            BMS: BRA1064(coaBC)
            BMB: BruAb2_1004(coaBC)
            BOV: BOV_A1001(coaBC)
            OAN: Oant_1319
            BJA: bll0759(dfp)
            BRA: BRADO0077(coaBC)
            BBT: BBta_0083(coaBC)
            RPA: RPA0081(coaBC)
            RPB: RPB_0622
            RPC: RPC_0380
            RPD: RPD_0209
            RPE: RPE_0467
            NWI: Nwi_0043
            NHA: Nham_0051
            BHE: BH00380(dfp)
            BQU: BQ00340(dfp)
            BBK: BARBAKC583_1349(coaBC)
            CCR: CC_3712
            SIL: SPO0408(coaBC)
            SIT: TM1040_0458
            RSP: RSP_0599
            RSQ: Rsph17025_0484
            JAN: Jann_0907
            RDE: RD1_1200(coaBC)
            HNE: HNE_3268(coaBC)
            ZMO: ZMO1190(dfp)
            SWI: Swit_4880
            GOX: GOX2498
            GBE: GbCGDNIH1_0157
            RRU: Rru_A3796
            MAG: amb0202
            MGM: Mmc1_3420
            ABA: Acid345_3776
            BSU: BG13388(yloI)
            BHA: BH2510(dfp)
            BAN: BA4007(coaBC)
            BAR: GBAA4007(coaBC)
            BAA: BA_4478
            BAT: BAS3720
            BCE: BC3867
            BCA: BCE_3912(coaBC)
            BCZ: BCZK3628(dfp)
            BCY: Bcer98_2521
            BTK: BT9727_3610(dfp)
            BLI: BL02295
            BLD: BLi01791(yloI)
            BCL: ABC2320
            BPU: BPUM_1469(coaBC)
            OIH: OB1504
            GKA: GK1169
            SAU: SA1054
            SAV: SAV1211
            SAM: MW1094
            SAR: SAR1187
            SAS: SAS1145
            SAC: SACOL1223(coaBC)
            SAB: SAB1075
            SAA: SAUSA300_1104(coaBC)
            SAO: SAOUHSC_01178
            SEP: SE0887
            SER: SERP0778(coaBC)
            SHA: SH1703
            SSP: SSP1560
            LMO: lmo1825
            LMF: LMOf2365_1853(coaBC)
            LIN: lin1939
            LWE: lwe1844(coaBC)
            LLC: LACR_0592
            LLM: llmg_0544(dfpB)
            SPZ: M5005_Spy_0935(dpfB)
            SPH: MGAS10270_Spy1049(dpfB)
            SPI: MGAS10750_Spy1084(dpfB)
            SPJ: MGAS2096_Spy0994(dpfB)
            SPK: MGAS9429_Spy1038(dpfB)
            SPA: M6_Spy0924
            SPB: M28_Spy0907(dpfB)
            SPD: SPD_1088(coaB)
            SGO: SGO_1212(coaB)
            LPL: lp_1614(dfp)
            LJO: LJ0902
            LAC: LBA0939
            LSA: LSA0687(dfp)
            LSL: LSL_0613
            LDB: Ldb0811(dfp)
            LBU: LBUL_0739 LBUL_0741
            LBR: LVIS_0967
            LCA: LSEI_1627
            LRE: Lreu_1174
            PPE: PEPE_0827
            OOE: OEOE_0935
            STH: STH1341
            CAC: CAC1720
            CPE: CPE1746
            CPF: CPF_1999(coaBC)
            CPR: CPR_1717(coaBC)
            CTC: CTC01217
            CNO: NT01CX_2247
            CTH: Cthe_1313
            CBA: CLB_2385(coaBC)
            CBH: CLC_2367(coaBC)
            CBF: CLI_2573(coaBC)
            CKL: CKL_1367(coaBC)
            AMT: Amet_2788
            CHY: CHY_1486(coaBC)
            DSY: DSY2727
            DRM: Dred_1702
            SWO: Swol_1235
            CSC: Csac_2084
            TTE: TTE1509(dfp)
            MTA: Moth_0893
            MMO: MMOB5920(dfp)
            MTU: Rv1391(dfp)
            MTC: MT1436(dfp)
            MBO: Mb1426(dfp)
            MPA: MAP1125(dfp)
            MAV: MAV_3383(coaBC)
            MSM: MSMEG_3054(coaBC)
            MVA: Mvan_2669
            MGI: Mflv_3738
            MMC: Mmcs_2372
            MKM: Mkms_2419
            MJL: Mjls_2413
            NFA: nfa36140(dfp)
            RHA: RHA1_ro07157
            SCO: SCO1477(SC9C5.01c)
            SMA: SAV6873(dfp)
            ART: Arth_2257
            NCA: Noca_2438
            TFU: Tfu_1064
            FRA: Francci3_3193
            FAL: FRAAL5228
            ACE: Acel_1291
            KRA: Krad_2990
            SEN: SACE_2102(dfp)
            STP: Strop_1863
            BAD: BAD_0478
            FNU: FN0711
            RBA: RB7087
            BBU: BB0812(dfp)
            BGA: BG0838(dfp)
            BAF: BAPKO_0865(dfp)
            SYG: sync_0352(coaBC)
            SYR: SynRCC307_2197(dfp)
            SYX: SynWH7803_0351(dfp)
            CYA: CYA_0161(coaBC)
            CYB: CYB_0983(coaBC)
            AVA: Ava_3811
            PMB: A9601_02501(dfp)
            PMC: P9515_02611(dfp)
            PMF: P9303_23871(dfp)
            PMG: P9301_02511(dfp)
            PMH: P9215_02511
            PME: NATL1_03101(dfp)
            BTH: BT_1362
            BFR: BF2979
            BFS: BF2855(dfp)
            PGI: PG1851(coaBC)
            SRU: SRU_0028(coaBC)
            CHU: CHU_3015(coaBC)
            FPS: FP1839
            CTE: CT0207(dfp)
            CCH: Cag_1614
            DET: DET0429(coaBC)
            DEH: cbdb_A383(coaBC)
            DEB: DehaBAV1_0406
            RRS: RoseRS_1561
            RCA: Rcas_3412
            DRA: DR_0579
            DGE: Dgeo_2315
            TTH: TTC1195
            TTJ: TTHA1560
            AAE: aq_815(dfp)
            TMA: TM1687
            FNO: Fnod_1467
            HWA: HQ1683A(dfp)
            NPH: NP1374A(dfp)
STRUCTURES  PDB: 1P9O  1U7U  1U7W  1U7Z  1U80  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.5
            ExPASy - ENZYME nomenclature database: 6.3.2.5
            ExplorEnz - The Enzyme Database: 6.3.2.5
            ERGO genome analysis and discovery system: 6.3.2.5
            BRENDA, the Enzyme Database: 6.3.2.5
            CAS: 9023-50-1
///
ENTRY       EC 6.3.2.6                  Enzyme
NAME        phosphoribosylaminoimidazolesuccinocarboxamide synthase;
            phosphoribosylaminoimidazole-succinocarboxamide synthetase;
            PurC;
            SAICAR synthetase;
            4-(N-succinocarboxamide)-5-aminoimidazole synthetase;
            4-[(N-succinylamino)carbonyl]-5-aminoimidazole ribonucleotide
            synthetase;
            SAICARs;
            phosphoribosylaminoimidazolesuccinocarboxamide synthetase;
            5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate:L-aspartate
            ligase (ADP-forming)
REACTION    ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate +
            L-aspartate = ADP + phosphate +
            (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-
            carboxamido]succinate [RN:R04591]
ALL_REAC    R04591
SUBSTRATE   ATP [CPD:C00002];
            5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate [CPD:C04751];
            L-aspartate [CPD:C00049]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-
            carboxamido]succinate [CPD:C04823]
COMMENT     Forms part of the purine biosynthesis pathway.
REFERENCE   1  [PMID:13672967]
  AUTHORS   LUKENS LN, BUCHANAN JM.
  TITLE     Biosynthesis of the purines. XXIV. The enzymatic synthesis of
            5-amino-1-ribosyl-4-imidazolecarboxylic acid 5'-phosphate from
            5-amino-1-ribosylimidazole 5'-phosphate and carbon dioxide.
  JOURNAL   J. Biol. Chem. 234 (1959) 1799-805.
  ORGANISM  pigeon, chicken [GN:gga]
REFERENCE   2  [PMID:6365889]
  AUTHORS   Parker J.
  TITLE     Identification of the purC gene product of Escherichia coli.
  JOURNAL   J. Bacteriol. 157 (1984) 712-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:3036807]
  AUTHORS   Ebbole DJ, Zalkin H.
  TITLE     Cloning and characterization of a 12-gene cluster from Bacillus
            subtilis encoding nine enzymes for de novo purine nucleotide
            synthesis.
  JOURNAL   J. Biol. Chem. 262 (1987) 8274-87.
  ORGANISM  Bacillus subtilis [GN:bsu]
REFERENCE   4  [PMID:1691501]
  AUTHORS   Chen ZD, Dixon JE, Zalkin H.
  TITLE     Cloning of a chicken liver cDNA encoding 5-aminoimidazole
            ribonucleotide carboxylase and
            5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase by
            functional complementation of Escherichia coli pur mutants.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 3097-101.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:10757766]
  AUTHORS   O'Donnell AF, Tiong S, Nash D, Clark DV.
  TITLE     The Drosophila melanogaster ade5 gene encodes a bifunctional enzyme
            for two steps in the de novo purine synthesis pathway.
  JOURNAL   Genetics. 154 (2000) 1239-53.
  ORGANISM  Drosophila melanogaster [GN:dme]
REFERENCE   6  [PMID:15641804]
  AUTHORS   Nelson SW, Binkowski DJ, Honzatko RB, Fromm HJ.
  TITLE     Mechanism of action of Escherichia coli
            phosphoribosylaminoimidazolesuccinocarboxamide synthetase.
  JOURNAL   Biochemistry. 44 (2005) 766-74.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01923  phosphoribosylaminoimidazole-succinocarboxamide synthase
GENES       HSA: 10606(PAICS)
            MMU: 67054(Paics)
            RNO: 140946(Paics)
            BTA: 404170(PAICS)
            GGA: 396534(PAICS)
            XLA: 379855(paics) 444677(MGC84289)
            DRE: 321193(paics)
            SPU: 575874(LOC575874)
            DME: Dmel_CG17024
            CEL: B0286.3
            ATH: AT3G21110(PUR7)
            OSA: 4347318
            CME: CME023C
            SCE: YAR015W(ADE1)
            AGO: AGOS_AER221W
            PIC: PICST_49451(PUR7)
            CGR: CAGL0I04444g
            SPO: SPBC409.10
            ANI: AN4739.2
            AFM: AFUA_3G06210
            AOR: AO090020000395
            CNE: CNA01310
            UMA: UM04726.1
            ECO: b2476(purC)
            ECJ: JW2461(purC)
            ECE: Z3735(purC)
            ECS: ECs3338
            ECC: c3004(purC)
            ECI: UTI89_C2803(purC)
            ECP: ECP_2490
            ECV: APECO1_4081(purC)
            ECW: EcE24377A_2757(purC)
            ECX: EcHS_A2607
            STY: STY2725(purC)
            STT: t0372(purC)
            SPT: SPA0382(purC)
            SEC: SC2482(purC)
            STM: STM2487(purC)
            YPE: YPO3059(purC)
            YPK: y1421(purC)
            YPM: YP_2681(purC)
            YPA: YPA_2250
            YPN: YPN_1326
            YPP: YPDSF_2164
            YPS: YPTB2781(purC)
            YPI: YpsIP31758_1249(purC)
            YEN: YE1140(purC)
            SFL: SF2519(purC)
            SFX: S2669(purC)
            SFV: SFV_2521(purC)
            SSN: SSON_2557(purC)
            SBO: SBO_2493(purC)
            SDY: SDY_2664(purC)
            ECA: ECA1264(purC)
            PLU: plu2744(purC)
            WBR: WGLp330(purC)
            SGL: SG1724
            ENT: Ent638_2972
            SPE: Spro_3507
            HIT: NTHI2033(purC)
            HIP: CGSHiEE_03425
            HIQ: CGSHiGG_02365
            HSO: HS_1364(purC)
            PMU: PM0815(purC)
            MSU: MS1481(purC)
            APL: APL_2018(purC)
            ASU: Asuc_0983
            XFA: XF0205
            XFT: PD0166(purC)
            XCC: XCC0453(purC)
            XCB: XC_0467
            XCV: XCV0500(hemH)
            XAC: XAC0470(purC)
            XOO: XOO4054(purC)
            XOM: XOO_3829(XOO3829)
            VCH: VC1190
            VVU: VV1_2797
            VVY: VV1468
            VPA: VP1263
            VFI: VF1498(hemH)
            PPR: PBPRA1469
            PAE: PA1013(purC)
            PAU: PA14_51240(purC)
            PAP: PSPA7_4384(purC)
            PPU: PP_1240(purC)
            PPF: Pput_1270
            PST: PSPTO_3950(purC)
            PSB: Psyr_1551
            PSP: PSPPH_1540(purC)
            PFL: PFL_1460(purC)
            PFO: Pfl_1374
            PEN: PSEEN4061(purC)
            PMY: Pmen_1665
            PAR: Psyc_0150(purC)
            PCR: Pcryo_0160
            PRW: PsycPRwf_2126
            ACI: ACIAD3587(purC)
            ACB: A1S_3425
            SON: SO_4066
            SDN: Sden_3063
            SFR: Sfri_3716
            SAZ: Sama_0491
            SBL: Sbal_3785
            SBM: Shew185_0527
            SLO: Shew_2211
            SPC: Sputcn32_0608
            SSE: Ssed_2552
            SPL: Spea_2464
            SHE: Shewmr4_3447
            SHM: Shewmr7_0504
            SHN: Shewana3_3622
            SHW: Sputw3181_3563
            ILO: IL1458(purC)
            CPS: CPS_2905(hemH)
            PHA: PSHAa0454(hemH)
            PAT: Patl_2476
            SDE: Sde_0669
            PIN: Ping_1862
            MAQ: Maqu_1689
            CBU: CBU_1220(purC)
            CBD: COXBU7E912_1304(purC)
            LPN: lpg1675
            LPF: lpl1640(purC)
            LPP: lpp1647(purC)
            MCA: MCA0021(purC)
            FTU: FTT0894(purCD)
            FTF: FTF0894(purCD)
            FTW: FTW_1285(purCD)
            FTL: FTL_0396
            FTH: FTH_0388(purC)
            FTN: FTN_0420
            TCX: Tcr_0262
            NOC: Noc_2522
            AEH: Mlg_2257
            HHA: Hhal_0916
            HCH: HCH_04904(purC)
            CSA: Csal_2813
            ABO: ABO_0779(purC)
            MMW: Mmwyl1_2145
            AHA: AHA_0898(purC)
            DNO: DNO_1112(purC)
            BCI: BCI_0071(purC)
            RMA: Rmag_0023
            VOK: COSY_0022(purC)
            NME: NMB0757
            NMA: NMA0968(purC)
            NMC: NMC0709(purC)
            NGO: NGO0333(hemH)
            CVI: CV_0165(hemH)
            RSO: RSc0574(purC)
            REU: Reut_A0556(hemH)
            REH: H16_A0569(purC)
            RME: Rmet_0504
            BMA: BMA0300(purC)
            BMV: BMASAVP1_A0595(purC)
            BML: BMA10299_A2429(purC)
            BMN: BMA10247_0041(purC)
            BXE: Bxe_A0692
            BVI: Bcep1808_2740
            BUR: Bcep18194_A5956(hemH)
            BCN: Bcen_2014
            BCH: Bcen2424_2625
            BAM: Bamb_2672
            BPS: BPSL0799(purC)
            BPM: BURPS1710b_0999(hemH)
            BPL: BURPS1106A_0842(purC)
            BPD: BURPS668_0837(purC)
            BTE: BTH_I0666(purC)
            PNU: Pnuc_1814
            BPE: BP1521(hemH)
            BPA: BPP1194(hemH)
            BBR: BB1410(hemH)
            RFR: Rfer_0203
            POL: Bpro_4629
            PNA: Pnap_3868
            AAV: Aave_4559
            AJS: Ajs_3928
            VEI: Veis_1549
            MPT: Mpe_A0292
            HAR: HEAR2608(purC)
            MMS: mma_2845
            NEU: NE0866(hemH)
            NET: Neut_1200
            NMU: Nmul_A0612
            EBA: ebA1125(hemH)
            AZO: azo2873(purC)
            DAR: Daro_3640
            TBD: Tbd_2668
            MFA: Mfla_2242
            HHE: HH1619(purC)
            WSU: WS0607(purC)
            TDN: Tmden_0491
            CJE: Cj0512(purC)
            CJR: CJE0619(purC)
            CJJ: CJJ81176_0540(purC)
            CJU: C8J_0476(purC)
            CJD: JJD26997_1419(purC)
            CFF: CFF8240_0945(purC)
            CCV: CCV52592_2005(purC)
            CHA: CHAB381_0847(purC)
            CCO: CCC13826_0132(purC) CCC13826_1155
            ABU: Abu_2121(purC)
            NIS: NIS_0874(purC)
            SUN: SUN_1461(purC)
            GSU: GSU2091(purC)
            GME: Gmet_0916
            GUR: Gura_2868
            PCA: Pcar_1051
            PPD: Ppro_3066
            DVU: DVU0795(purC)
            DVL: Dvul_2179
            DDE: Dde_1007
            LIP: LI0349(purC)
            BBA: Bd3007
            DPS: DP2502
            ADE: Adeh_1112
            AFW: Anae109_1151
            SAT: SYN_00107 SYN_02710
            SFU: Sfum_1263
            RPR: RP220
            RTY: RT0211(purC)
            RCO: RC0294(purC)
            RFE: RF_0339(purC)
            RBE: RBE_0534(purC)
            RAK: A1C_01630
            RBO: A1I_03060
            RCM: A1E_01260
            RRI: A1G_01680
            OTS: OTBS_0388(purC)
            WOL: WD1023(purC)
            WBM: Wbm0227
            AMA: AM137(purC)
            APH: APH_0119(purC)
            ERU: Erum7000(purC)
            ERW: ERWE_CDS_07350(purC)
            ERG: ERGA_CDS_07270(purC)
            ECN: Ecaj_0713
            ECH: ECH_0290(purC)
            NSE: NSE_0852(purC)
            PUB: SAR11_1138(purC)
            MLO: mll0069 mll2603
            MES: Meso_1281
            PLA: Plav_2589
            SME: SMc00495(purC)
            SMD: Smed_1498
            ATU: Atu1843(purC) Atu2548(purC)
            ATC: AGR_C_3382 AGR_C_4615
            RET: RHE_CH02278(purC1) RHE_CH03409(purC2)
            RLE: RL1597 RL2606(purC) RL3872(purC)
            BME: BMEI1122
            BMF: BAB1_0862
            BMS: BR0842(purC)
            BMB: BruAb1_0855(purC)
            BOV: BOV_0834(purC)
            OAN: Oant_2382
            BJA: bll0812(purC) bll5729(purC)
            BRA: BRADO0015 BRADO2776(purC)
            BBT: BBta_0020 BBta_5409(purC)
            RPA: RPA0558(purC1) RPA3821(purC2)
            RPB: RPB_0702 RPB_3719
            RPC: RPC_0345 RPC_1584
            RPD: RPD_0150 RPD_1747
            RPE: RPE_0548 RPE_1607
            NWI: Nwi_1304
            NHA: Nham_1633
            BHE: BH09710(purC)
            BQU: BQ07470(purC)
            BBK: BARBAKC583_0859(purC)
            XAU: Xaut_4093
            CCR: CC_2491 CC_3242
            SIL: SPO1887(purC)
            SIT: TM1040_1465
            RSP: RSP_2126(purC) RSP_2258(hemH)
            RSH: Rsph17029_0801 Rsph17029_0932
            RSQ: Rsph17025_0711 Rsph17025_2238
            JAN: Jann_2545
            RDE: RD1_2262(purC)
            PDE: Pden_2861
            MMR: Mmar10_1032
            HNE: HNE_2605(purC)
            ZMO: ZMO1052(purC)
            NAR: Saro_1041
            SAL: Sala_0584
            SWI: Swit_0102
            ELI: ELI_02460
            GBE: GbCGDNIH1_1666
            ACR: Acry_0393
            RRU: Rru_A0711
            MAG: amb1539 amb2031
            MGM: Mmc1_0497
            ABA: Acid345_2258
            SUS: Acid_5250
            BSU: BG10703(purC)
            BHA: BH0626(purC)
            BAN: BA0291(purC)
            BAR: GBAA0291(purC)
            BAA: BA_0863
            BAT: BAS0278
            BCE: BC0326
            BCA: BCE_0320(purC)
            BCZ: BCZK0266(purC)
            BCY: Bcer98_0270
            BTK: BT9727_0263(purC)
            BTL: BALH_0285(purC)
            BLI: BL01479(purC)
            BLD: BLi00696(purC)
            BCL: ABC1027(purC)
            BAY: RBAM_006870
            BPU: BPUM_0599
            OIH: OB0742
            GKA: GK0260
            SAU: SA0918(purC)
            SAV: SAV1066(purC)
            SAM: MW0949(purC)
            SAR: SAR1040(purC)
            SAS: SAS1002
            SAC: SACOL1075(purC)
            SAB: SAB0933(purC)
            SAA: SAUSA300_0968(purC)
            SAO: SAOUHSC_01010
            SAJ: SaurJH9_1126
            SAH: SaurJH1_1148
            SEP: SE0764
            SER: SERP0651(purC)
            SHA: SH1891(purC)
            SSP: SSP1724
            LMO: lmo1772(purC)
            LMF: LMOf2365_1797(purC)
            LIN: lin1884(purC)
            LWE: lwe1790(purC)
            LLA: L177350(purC)
            LLC: LACR_1622
            LLM: llmg_0973(purC)
            SPY: SPy_0024(purC)
            SPZ: M5005_Spy_0022
            SPM: spyM18_0025(purC)
            SPG: SpyM3_0019(purC)
            SPS: SPs0020
            SPH: MGAS10270_Spy0022
            SPI: MGAS10750_Spy0022
            SPJ: MGAS2096_Spy0023
            SPK: MGAS9429_Spy0022
            SPA: M6_Spy0071
            SPB: M28_Spy0022(purC)
            SPN: SP_0044
            SPR: spr0045(purC)
            SPD: SPD_0051(purC)
            SAG: SAG0024(purC)
            SAN: gbs0023
            SAK: SAK_0057(purC)
            SMU: SMU.29
            STC: str0030(purC)
            STL: stu0030(purC)
            SSA: SSA_0028(purC)
            SGO: SGO_0034(purC)
            LPL: lp_2727(purC)
            LAC: LBA1559(purC)
            LSA: LSA0655(purC)
            LSL: LSL_0663(purC)
            LDB: Ldb1443(purC)
            LBU: LBUL_1338
            LCA: LSEI_1754
            LRE: Lreu_0137
            EFA: EF1785(purC)
            OOE: OEOE_1136
            STH: STH2857
            CAC: CAC1391(purC)
            CPE: CPE0682(purC)
            CPF: CPF_0673(purC)
            CPR: CPR_0671(purC)
            CTC: CTC01170
            CNO: NT01CX_2423(purC)
            CTH: Cthe_2885
            CDF: CD0219(purC) CD0489
            CBO: CBO2877(purC)
            CBA: CLB_2842(purC)
            CBH: CLC_2775(purC)
            CBF: CLI_2935(purC)
            CBE: Cbei_1055
            CKL: CKL_2688(purC)
            AMT: Amet_0918
            CHY: CHY_1071(purC)
            DSY: DSY0789 DSY3931
            DRM: Dred_2369
            SWO: Swol_1209
            CSC: Csac_1999
            TTE: TTE0588(purC)
            MTA: Moth_2051
            MTU: Rv0780(hemH)
            MTC: MT0804(purC)
            MBO: Mb0803(hemH)
            MBB: BCG_0832(purC)
            MLE: ML2227(purC)
            MPA: MAP0614(purC)
            MAV: MAV_0725(purC)
            MSM: MSMEG_5841(purC)
            MVA: Mvan_5138
            MGI: Mflv_1616
            MMC: Mmcs_4560
            MKM: Mkms_4648
            MJL: Mjls_4943
            CGL: NCgl2508(hemH)
            CGB: cg2874(hemH)
            CEF: CE2487(hemH)
            CDI: DIP1927(hemH)
            CJK: jk0350(purC) jk0353(purS)
            NFA: nfa13190(purC)
            RHA: RHA1_ro04817(purC)
            SCO: SCO4071(purC)
            SMA: SAV4146(purC)
            TWH: TWT109(hemH)
            TWS: TW119(hemH)
            LXX: Lxx22800(purC)
            CMI: CMM_0753(purC)
            ART: Arth_3405
            AAU: AAur_3383(purC)
            PAC: PPA1988
            NCA: Noca_4337
            TFU: Tfu_3015(hemH)
            FRA: Francci3_4373
            FAL: FRAAL6667(purC)
            ACE: Acel_2129
            KRA: Krad_4099
            SEN: SACE_7150(purC)
            STP: Strop_3726
            BLO: BL1107(purC)
            BAD: BAD_0524(purC)
            RXY: Rxyl_0993
            FNU: FN0988
            RBA: RB12194(hemH)
            TDE: TDE0686(purC)
            LIL: LA3513(hemH)
            LIC: LIC10679(purC)
            LBJ: LBJ_0698(purC)
            LBL: LBL_2381(purC)
            SYN: slr1226(purC)
            SYW: SYNW0554(purC)
            SYC: syc0615_c(purC)
            SYF: Synpcc7942_0927
            SYD: Syncc9605_2120
            SYE: Syncc9902_0553
            SYG: sync_2216(purC)
            SYR: SynRCC307_1820(purC)
            SYX: SynWH7803_1960(purC)
            CYA: CYA_0240(purC)
            CYB: CYB_1784(purC)
            TEL: tll1496(purC)
            GVI: glr1916(purC)
            ANA: alr2268(purC)
            AVA: Ava_0093
            PMA: Pro1420(purC)
            PMM: PMM1339(purC)
            PMT: PMT1414(purC)
            PMN: PMN2A_0910
            PMI: PMT9312_1437
            PMC: P9515_15001(purC)
            PMF: P9303_05481(purC)
            PMG: P9301_15251(purC)
            PMH: P9215_15681
            PME: NATL1_17661(purC)
            TER: Tery_4655
            BTH: BT_4217
            BFR: BF0918
            BFS: BF0840(hemH)
            PGI: PG0976
            SRU: SRU_1514(purC)
            CHU: CHU_1912(purC)
            GFO: GFO_1908(purC)
            FJO: Fjoh_2728
            FPS: FP1079(purC)
            CTE: CT0960(purC)
            CCH: Cag_1435
            CPH: Cpha266_1019
            PVI: Cvib_0763
            PLT: Plut_1194
            DET: DET0841(purC)
            DEH: cbdb_A823(purC)
            DEB: DehaBAV1_0760
            RRS: RoseRS_2552
            RCA: Rcas_1843
            DRA: DR_0226
            DGE: Dgeo_0067
            TTH: TTC1151
            TTJ: TTHA1515
            AAE: aq_2117(purC)
            TMA: TM1243
            TPT: Tpet_1528
            TME: Tmel_1233
            FNO: Fnod_1094
            MMP: MMP0540(purC)
            MMQ: MmarC5_1067
            MMZ: MmarC7_1559
            MAE: Maeo_0468 Maeo_1445
            MVN: Mevan_1694
            MAC: MA4063(purC)
            MBA: Mbar_A0531
            MMA: MM_0855
            MBU: Mbur_2042
            MTP: Mthe_1509
            MHU: Mhun_1253
            MEM: Memar_1839
            MBN: Mboo_2202
            MST: Msp_1195(purC)
            MSI: Msm_1547
            MKA: MK0792(purC)
            HAL: VNG1939G(purC)
            HMA: rrnAC3275(hemH)
            HWA: HQ3128A(purC)
            NPH: NP4996A(hemH)
            TAC: Ta0309
            TVO: TVN1291
            PTO: PTO1353(hemH)
            PAB: PAB2400(purC)
            PFU: PF0153
            TKO: TK0210
            IHO: Igni_0843
            SSO: SSO0626(purC)
            STO: ST1493
            SAI: Saci_1607(purC)
            MSE: Msed_1977
            PAI: PAE0215(purC)
            PIS: Pisl_0105
            PCL: Pcal_1895
            PAS: Pars_2194
STRUCTURES  PDB: 1A48  1KUT  1OBD  1OBG  2CNQ  2CNU  2CNV  2GQR  2GQS  2H31  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.6
            ExPASy - ENZYME nomenclature database: 6.3.2.6
            ExplorEnz - The Enzyme Database: 6.3.2.6
            ERGO genome analysis and discovery system: 6.3.2.6
            BRENDA, the Enzyme Database: 6.3.2.6
            CAS: 9023-67-0
///
ENTRY       EC 6.3.2.7                  Enzyme
NAME        UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase;
            MurE synthetase;
            UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine synthetase;
            uridine diphospho-N-acetylmuramoylalanyl-D-glutamyllysine
            synthetase;
            UPD-MurNAc-L-Ala-D-Glu:L-Lys ligase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:L-lysine gamma-ligase
            (ADP-forming)
REACTION    ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine = ADP +
            phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine
            [RN:R02785]
ALL_REAC    R02785;
            (other) R02786
SUBSTRATE   ATP [CPD:C00002];
            UDP-N-acetylmuramoyl-L-alanyl-D-glutamate [CPD:C00692];
            L-lysine [CPD:C00047]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine [CPD:C04700]
COMMENT     Involved with EC 6.3.2.4 (D-alanine---D-alanine ligase), EC 6.3.2.8
            (UDP-N-acetylmuramate---L-alanine ligase), EC 6.3.2.9
            (UDP-N-acetylmuramoyl-L-alanine---D-glutamate ligase) and EC
            6.3.2.10 (UDP-N-acetylmuramoyl-tripeptide---D-alanyl-D-alanine
            ligase) in the synthesis of a cell-wall peptide (click here for
            diagram). This enzyme adds lysine in some Gram-positive organisms;
            in others and in Gram-negative organisms EC 6.3.2.13
            (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate
            ligase) adds 2,6-diaminopimelate instead.
REFERENCE   1
  AUTHORS   Ito, E. and Strominger, J.L.
  TITLE     Enzymatic synthesis of the peptide in bacterial uridine nucleotides.
            I. Enzymatic addition of L-alanine, D-glutamic acid, and L-lysine.
  JOURNAL   J. Biol. Chem. 237 (1962) 2689-2695.
  ORGANISM  Staphylococcus aureus
REFERENCE   2  [PMID:11699883]
  AUTHORS   van Heijenoort J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit.
  JOURNAL   Nat. Prod. Rep. 18 (2001) 503-19.
  ORGANISM  Staphylococcus aureus
PATHWAY     PATH: map00550  Peptidoglycan biosynthesis
ORTHOLOGY   KO: K05362  UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine
                        ligase
GENES       SPH: MGAS10270_Spy0320(murE)
            SPI: MGAS10750_Spy0321(murE)
            SPJ: MGAS2096_Spy0342 MGAS2096_Spy0343(murE)
            SPK: MGAS9429_Spy0324(murE)
            SPB: M28_Spy0314(murE)
            LSL: LSL_0016(murE)
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.7
            ExPASy - ENZYME nomenclature database: 6.3.2.7
            ExplorEnz - The Enzyme Database: 6.3.2.7
            ERGO genome analysis and discovery system: 6.3.2.7
            BRENDA, the Enzyme Database: 6.3.2.7
            CAS: 9023-51-2
///
ENTRY       EC 6.3.2.8                  Enzyme
NAME        UDP-N-acetylmuramate---L-alanine ligase;
            MurC synthetase;
            UDP-N-acetylmuramoyl-L-alanine synthetase;
            uridine diphospho-N-acetylmuramoylalanine synthetase;
            UDP-N-acetylmuramoylalanine synthetase;
            L-alanine-adding enzyme;
            UDP-acetylmuramyl-L-alanine synthetase;
            UDPMurNAc-L-alanine synthetase;
            L-Ala ligase;
            uridine diphosphate N-acetylmuramate:L-alanine ligase;
            uridine 5'-diphosphate-N-acetylmuramyl-L-alanine synthetase;
            uridine-diphosphate-N-acetylmuramate:L-alanine ligase;
            UDP-MurNAc:L-alanine ligase;
            alanine-adding enzyme;
            UDP-N-acetylmuramyl:L-alanine ligase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     UDP-N-acetylmuramate:L-alanine ligase (ADP-forming)
REACTION    ATP + UDP-N-acetylmuramate + L-alanine = ADP + phosphate +
            UDP-N-acetylmuramoyl-L-alanine [RN:R03193]
ALL_REAC    R03193
SUBSTRATE   ATP [CPD:C00002];
            UDP-N-acetylmuramate [CPD:C01050];
            L-alanine [CPD:C00041]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            UDP-N-acetylmuramoyl-L-alanine [CPD:C01212]
COMMENT     Involved with EC 6.3.2.4 (D-alanine---D-alanine ligase), EC 6.3.2.7
            (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase) or EC
            6.3.2.13
            (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate
            ligase), EC 6.3.2.9 (UDP-N-acetylmuramoyl-L-alanine---D-glutamate
            ligase) and EC 6.3.2.10
            (UDP-N-acetylmuramoyl-tripeptide---D-alanyl-D-alanine ligase) in the
            synthesis of a cell-wall peptide (click here for diagram).
REFERENCE   1
  AUTHORS   Ito, E. and Strominger, J.L.
  TITLE     Enzymatic synthesis of the peptide in bacterial uridine nucleotides.
            I. Enzymatic addition of L-alanine, D-glutamic acid, and L-lysine.
  JOURNAL   J. Biol. Chem. 237 (1962) 2689-2695.
  ORGANISM  Staphylococcus aureus
REFERENCE   2
  AUTHORS   Nathenson, S.G., Strominger, J.L. and Ito, E.
  TITLE     Enzymatic synthesis of the peptide in bacterial uridine nucleotides.
            IV. Purification and properties of D-glutamic acid-adding enzyme.
  JOURNAL   J. Biol. Chem. 239 (1964) 1773-1776.
  ORGANISM  Staphylococcus aureus
REFERENCE   3  [PMID:11699883]
  AUTHORS   van Heijenoort J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit.
  JOURNAL   Nat. Prod. Rep. 18 (2001) 503-19.
  ORGANISM  Staphylococcus aureus
PATHWAY     PATH: map00471  D-Glutamine and D-glutamate metabolism
            PATH: map00550  Peptidoglycan biosynthesis
ORTHOLOGY   KO: K01924  UDP-N-acetylmuramate--alanine ligase
GENES       AOR: AO090009000505
            ECO: b0091(murC)
            ECJ: JW0089(murC)
            ECE: Z0101(murC)
            ECS: ECs0095
            ECC: c0109(murC)
            ECI: UTI89_C0100(murC)
            ECP: ECP_0093
            ECV: APECO1_1895(murC)
            ECW: EcE24377A_0093(murC)
            ECX: EcHS_A0097
            STY: STY0149(murC)
            STT: t0133(murC)
            SPT: SPA0131(murC)
            SEC: SC0126(murC)
            STM: STM0129(murC)
            YPE: YPO0556(murC)
            YPK: y3625(murC)
            YPM: YP_3628(murC)
            YPA: YPA_3545
            YPN: YPN_0422
            YPS: YPTB0689(murC)
            YPI: YpsIP31758_3386(murC)
            SFL: SF0088(murC)
            SFX: S0090(murC)
            SFV: SFV_0084(murC)
            SSN: SSON_0099(murC)
            SBO: SBO_0079(murC)
            SDY: SDY_0121(murC)
            ECA: ECA3814(murC)
            PLU: plu3653(murC)
            BUC: BU215(murC)
            BAB: bbp197(murC)
            WBR: WGLp205(murC)
            SGL: SG0450
            BFL: Bfl143(murC)
            BPN: BPEN_147(murC)
            HIT: NTHI1307(murC)
            HIP: CGSHiEE_06355(murC)
            HIQ: CGSHiGG_09355(murC)
            HDU: HD0823(murC)
            HSO: HS_0359(murC)
            PMU: PM0143(murC)
            MSU: MS1666(murC)
            APL: APL_0019(murC)
            XFA: XF0798
            XFT: PD1865(murC)
            XCC: XCC0726(murC)
            XCB: XC_3509
            XCV: XCV0831(murC)
            XAC: XAC0780(murC)
            XOO: XOO3825(murC)
            XOM: XOO_3603(XOO3603)
            VCH: VC2400
            VCO: VC0395_A1978(murC)
            VVU: VV1_0577
            VVY: VV0615
            VPA: VP0461
            VFI: VF2200
            PPR: PBPRA3214
            PAE: PA4411(murC)
            PAU: PA14_57330(murC)
            PAP: PSPA7_4983(murC)
            PPU: PP_1338(murC)
            PST: PSPTO_4407(murC)
            PSB: Psyr_4101
            PSP: PSPPH_4107(murC)
            PFL: PFL_5060(murC)
            PFO: Pfl_4672
            PEN: PSEEN4484(murC)
            PAR: Psyc_1750(murC)
            PCR: Pcryo_2031
            ACI: ACIAD3516(murC)
            SON: SO_4218(murC)
            SDN: Sden_0356
            SFR: Sfri_3803
            SHE: Shewmr4_3569
            SHM: Shewmr7_0387
            SHN: Shewana3_3742
            ILO: IL0437(murC_1)
            CPS: CPS_4464(murC)
            PHA: PSHAa2503(murC)
            PAT: Patl_3518
            SDE: Sde_0849
            CBU: CBU_0136(murC)
            CBD: COXBU7E912_1971(murC)
            LPN: lpg2614(murC)
            LPF: lpl2537(murC)
            LPP: lpp2667(murC)
            MCA: MCA2428(murC)
            FTU: FTT0239(murC)
            FTF: FTF0239(murC)
            FTW: FTW_1852(murC)
            FTL: FTL_0172
            FTA: FTA_0188(murC)
            FTN: FTN_0079(murC)
            TCX: Tcr_0584
            NOC: Noc_2347 Noc_2860
            AEH: Mlg_2192
            HCH: HCH_05882(murC)
            CSA: Csal_2189
            ABO: ABO_0599(murC)
            AHA: AHA_3883(murC)
            DNO: DNO_0980(murC)
            BCI: BCI_0518(murC)
            VOK: COSY_0699(murC)
            NME: NMB0423
            NMA: NMA2061(murC)
            NMC: NMC1741(murC)
            NGO: NGO0815 NGO1532
            CVI: CV_4342(murC)
            RSO: RSc2843(murC)
            REU: Reut_A2978
            REH: H16_A3167(murC1) H16_A3272(murC2)
            RME: Rmet_3127
            BMA: BMA2550(murC)
            BMV: BMASAVP1_A0471(murC)
            BML: BMA10299_A1330(murC)
            BMN: BMA10247_3233(murC)
            BXE: Bxe_A0487
            BUR: Bcep18194_A3646 Bcep18194_A3692
            BCN: Bcen_0078
            BCH: Bcen2424_0560
            BAM: Bamb_0464
            BPS: BPSL3024(murC)
            BPM: BURPS1710b_3496(mpl) BURPS1710b_3543(murC)
            BPL: BURPS1106A_3549(murC)
            BPD: BURPS668_3524(murC)
            BTE: BTH_I1119(murC)
            BPE: BP3022(murC)
            BPA: BPP3751(murC)
            BBR: BB4197(murC)
            RFR: Rfer_3424
            POL: Bpro_1076
            MPT: Mpe_A0463
            HAR: HEAR2810(murC)
            MMS: mma_3014
            NEU: NE0992(murC)
            NET: Neut_0245
            NMU: Nmul_A2493
            EBA: ebA1443(murC)
            AZO: azo0885(murC)
            DAR: Daro_3497
            TBD: Tbd_0120
            MFA: Mfla_2268
            HPY: HP0623
            HPJ: jhp0567(murC)
            HPA: HPAG1_0606
            HHE: HH0373(murC)
            HAC: Hac_0737(murC)
            WSU: WS1484(murC)
            TDN: Tmden_0757
            CJE: Cj1054c(murC)
            CJR: CJE1198(murC)
            CJJ: CJJ81176_1074(murC)
            CJU: C8J_0996(murC)
            CJD: JJD26997_0680(murC)
            CFF: CFF8240_0616(murC)
            CCV: CCV52592_0395 CCV52592_0985(murC)
            CHA: CHAB381_1690(murC)
            CCO: CCC13826_1930
            ABU: Abu_0234(murC)
            NIS: NIS_1266(murC)
            SUN: SUN_0410(murC)
            GSU: GSU3068(murC)
            GME: Gmet_0413
            PCA: Pcar_2201
            DVU: DVU2503(murC)
            DDE: Dde_1043
            LIP: LI1105(murC)
            BBA: Bd3196(murC)
            DPS: DP2897
            ADE: Adeh_3772
            MXA: MXAN_5603(murC)
            SAT: SYN_01747
            SFU: Sfum_3470
            RPR: RP247(murC)
            RTY: RT0239(murC)
            RCO: RC0331(murC)
            RFE: RF_1037(murC)
            RBE: RBE_0963(murC)
            RAK: A1C_01800(murC)
            RBO: A1I_03840(murC)
            RCM: A1E_01420(murC)
            RRI: A1G_01900(murC)
            OTS: OTBS_0600(murC)
            WOL: WD0495(murC)
            WBM: Wbm0118
            AMA: AM010(murC) AM011(murC)
            PUB: SAR11_0023(murC)
            MLO: mll1553
            MES: Meso_2006
            SME: SMc01867(murC)
            ATU: Atu2093(murC)
            ATC: AGR_C_3796
            RET: RHE_CH02846(murC)
            RLE: RL3306(murC)
            BME: BMEI0580
            BMF: BAB1_1449(murC)
            BMS: BR1430(murC)
            BMB: BruAb1_1425(murC)
            BOV: BOV_1387(murC)
            BJA: bll6601(murC)
            BRA: BRADO5658(murC)
            BBT: BBta_6171(murC)
            RPA: RPA3529(murC)
            RPB: RPB_1996
            RPC: RPC_3305
            RPD: RPD_3393
            RPE: RPE_2108
            NWI: Nwi_1052
            NHA: Nham_1280
            BHE: BH11230(murC)
            BQU: BQ08850(murC)
            BBK: BARBAKC583_0946(murC)
            CCR: CC_2546
            SIL: SPO1196(murC)
            SIT: TM1040_0683
            RSP: RSP_2108(murC)
            JAN: Jann_2759
            RDE: RD1_3355(murC)
            MMR: Mmar10_2077
            HNE: HNE_3022(murC)
            ZMO: ZMO0832(murC)
            NAR: Saro_1134
            SAL: Sala_1880
            ELI: ELI_01800
            GOX: GOX0159
            GBE: GbCGDNIH1_0428
            RRU: Rru_A0949
            MAG: amb3849
            MGM: Mmc1_0752
            ABA: Acid345_3628
            BSU: BG10973(murC)
            BHA: BH3248(murC)
            BAN: BA4938(murC)
            BAR: GBAA4938(murC)
            BAA: BA_5357
            BAT: BAS4583
            BCE: BC4684
            BCA: BCE_4830(murC)
            BCZ: BCZK4438(murC)
            BTK: BT9727_4420(murC)
            BTL: BALH_4262(murC)
            BLI: BL00050(murC)
            BLD: BLi03131(murC)
            BCL: ABC2768(murC)
            BAY: RBAM_026910
            BPU: BPUM_2626
            OIH: OB2231(murC)
            GKA: GK2815
            SAU: SA1561(murC)
            SAV: SAV1740(murC)
            SAM: MW1683(murC)
            SAR: SAR1818(murC)
            SAS: SAS1666
            SAC: SACOL1790(murC)
            SAB: SAB1600c(murC) SAB1824c
            SAA: SAUSA300_1686(murC)
            SAO: SAOUHSC_01856
            SEP: SE1413
            SER: SERP1300(murC)
            SHA: SH1182(murC)
            SSP: SSP1023
            LMO: lmo1605(murC)
            LMF: LMOf2365_1627(murC)
            LIN: lin1646(murC)
            LWE: lwe1621(murC)
            LLA: L101678(murC)
            LLC: LACR_2326
            LLM: llmg_2316(murC)
            SPY: SPy_0345(murC)
            SPZ: M5005_Spy_0290(murC)
            SPM: spyM18_0398
            SPG: SpyM3_0252(murC.1)
            SPS: SPs1607
            SPH: MGAS10270_Spy0287(murC)
            SPI: MGAS10750_Spy0285(murC)
            SPJ: MGAS2096_Spy0308(murC)
            SPK: MGAS9429_Spy0290(murC)
            SPF: SpyM51565(murC)
            SPA: M6_Spy0318
            SPB: M28_Spy0282(murC)
            SPN: SP_1521
            SPR: spr1373(murC)
            SPD: SPD_1349(murC)
            SAG: SAG1615(murC)
            SAN: gbs1664(murC)
            SAK: SAK_1630(murC)
            SMU: SMU.1731(murC)
            STC: str0239(murC)
            STL: stu0239(murC)
            SSA: SSA_1800(murC)
            SGO: SGO_0515(murC)
            LPL: lp_1462(murC)
            LJO: LJ1663
            LAC: LBA1579(murC)
            LSA: LSA0637(murC)
            LSL: LSL_0485(murC)
            LDB: Ldb1522(murC)
            LBU: LBUL_1413
            LBR: LVIS_1047
            LCA: LSEI_1711
            EFA: EF1908(murC)
            OOE: OEOE_1269
            STH: STH2918
            CAC: CAC3225(murC)
            CPE: CPE2493(murC)
            CPF: CPF_2816(murC)
            CPR: CPR_2502(murC)
            CTC: CTC00185(murC)
            CNO: NT01CX_1011(murC)
            CDF: CD3518(murC)
            CBO: CBO3548(murC)
            CBA: CLB_3629(murC)
            CBH: CLC_3526(murC)
            CBF: CLI_3768(murC)
            CKL: CKL_0143(murC)
            CHY: CHY_2068(murC)
            DSY: DSY0792
            SWO: Swol_0827
            TTE: TTE2575(murC)
            MTA: Moth_0844
            MTU: Rv2152c(murC)
            MTC: MT2211(murC)
            MBO: Mb2176c(murC)
            MBB: BCG_2169c(murC)
            MLE: ML0915(murC)
            MPA: MAP1896c(murC)
            MAV: MAV_2337(murC)
            MSM: MSMEG_4226(murC)
            MMC: Mmcs_3255
            CGL: NCgl2077(cgl2157)
            CGB: cg2368(murC)
            CEF: CE2052(murC)
            CDI: DIP1597(murC)
            CJK: jk0751(murC)
            NFA: nfa17670(murC)
            RHA: RHA1_ro01087(murC)
            SCO: SCO6060(murC)
            SMA: SAV2205(murC)
            TWH: TWT229(murC)
            TWS: TW541(murC)
            LXX: Lxx15250(murC)
            CMI: CMM_1858(murC)
            AAU: AAur_1711(murC)
            PAC: PPA0759
            TFU: Tfu_1111
            FRA: Francci3_1417
            FAL: FRAAL2198(murC)
            ACE: Acel_1011
            SEN: SACE_5850(murC)
            BLO: BL1324(murC)
            BAD: BAD_1100(murC)
            RXY: Rxyl_1492
            FNU: FN1456
            CTR: CT762(murC)
            CTA: CTA_0832(murC-ddlA)
            CMU: TC0143
            CPN: CPn0905(murC)
            CPA: CP0961
            CPJ: CPj0905(murC_ddlA)
            CPT: CpB0937
            CCA: CCA00863(murC)
            CAB: CAB829
            CFE: CF0153(mudD)
            PCU: pc1247(murC)
            BGA: BG0842(murC)
            TPA: TP0341
            TDE: TDE1085(murC)
            LIL: LA2051(murC)
            LIC: LIC11863(murC)
            LBJ: LBJ_0475(murC-1)
            LBL: LBL_2604(murC-1)
            SYN: slr1423(murC)
            SYW: SYNW0029(murC)
            SYC: syc2350_d(murC)
            SYF: Synpcc7942_1741
            SYD: Syncc9605_0029
            SYE: Syncc9902_0025
            SYG: sync_0028(murC)
            SYR: SynRCC307_0027(murC)
            SYX: SynWH7803_0028(murC)
            CYA: CYA_1876(murC)
            CYB: CYB_1559(murC)
            TEL: tll0371(murC)
            GVI: glr2316(murC)
            ANA: alr5065
            AVA: Ava_2320
            PMA: Pro0022(murC)
            PMM: PMM0022(murC)
            PMT: PMT0027(murC)
            PMN: PMN2A_1349
            PMI: PMT9312_0022
            PMB: A9601_00211(murC)
            PMC: P9515_00211(murC)
            PMF: P9303_00261(murC)
            PMG: P9301_00211(murC)
            PMH: P9215_00211
            PME: NATL1_00211(murC)
            TER: Tery_4029
            BTH: BT_3447
            BFR: BF0305
            BFS: BF0253(murC)
            PGI: PG0581(murC)
            SRU: SRU_0561(murC)
            CHU: CHU_2738(murC)
            GFO: GFO_2767(murC) GFO_2861(murC)
            FPS: FP2056(murC)
            CTE: CT0033(murC)
            CCH: Cag_0056 Cag_0449
            PLT: Plut_2109
            RRS: RoseRS_3788
            DRA: DR_0627
            DGE: Dgeo_1631
            TTH: TTC0720
            TTJ: TTHA1085
            AAE: aq_1360(murC)
            TMA: TM0231
            MSI: Msm_0359
STRUCTURES  PDB: 1GQQ  1GQY  1J6U  1P31  1P3D  2F00  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.8
            ExPASy - ENZYME nomenclature database: 6.3.2.8
            ExplorEnz - The Enzyme Database: 6.3.2.8
            ERGO genome analysis and discovery system: 6.3.2.8
            BRENDA, the Enzyme Database: 6.3.2.8
            CAS: 9023-52-3
///
ENTRY       EC 6.3.2.9                  Enzyme
NAME        UDP-N-acetylmuramoyl-L-alanine---D-glutamate ligase;
            MurD synthetase;
            UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase;
            uridine diphospho-N-acetylmuramoylalanyl-D-glutamate synthetase;
            D-glutamate-adding enzyme;
            D-glutamate ligase;
            UDP-Mur-NAC-L-Ala:D-Glu ligase;
            UDP-N-acetylmuramoyl-L-alanine:glutamate ligase (ADP-forming);
            UDP-N-acetylmuramoylalanine---D-glutamate ligase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase (ADP-forming)
REACTION    ATP + UDP-N-acetylmuramoyl-L-alanine + D-glutamate = ADP + phosphate
            + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate [RN:R02783]
ALL_REAC    R02783
SUBSTRATE   ATP [CPD:C00002];
            UDP-N-acetylmuramoyl-L-alanine [CPD:C01212];
            D-glutamate [CPD:C00217]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            UDP-N-acetylmuramoyl-L-alanyl-D-glutamate [CPD:C00692]
COMMENT     Involved with EC 6.3.2.4 (D-alanine---D-alanine ligase), EC 6.3.2.7
            (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase) or EC
            6.3.2.13
            (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate
            ligase), EC 6.3.2.8 (UDP-N-acetylmuramate---L-alanine ligase) and EC
            6.3.2.10 (UDP-N-acetylmuramoyl-tripeptide---D-alanyl-D-alanine
            ligase) in the synthesis of a cell-wall peptide (click here for
            diagram).
REFERENCE   1
  AUTHORS   Ito, E. and Strominger, J.L.
  TITLE     Enzymatic synthesis of the peptide in bacterial uridine nucleotides.
            I. Enzymatic addition of L-alanine, D-glutamic acid, and L-lysine.
  JOURNAL   J. Biol. Chem. 237 (1962) 2689-2695.
  ORGANISM  Staphylococcus aureus
REFERENCE   2  [PMID:11699883]
  AUTHORS   van Heijenoort J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit.
  JOURNAL   Nat. Prod. Rep. 18 (2001) 503-19.
  ORGANISM  Staphylococcus aureus
PATHWAY     PATH: map00471  D-Glutamine and D-glutamate metabolism
            PATH: map00550  Peptidoglycan biosynthesis
ORTHOLOGY   KO: K01925  UDP-N-acetylmuramoylalanine--D-glutamate ligase
GENES       ECO: b0088(murD)
            ECJ: JW0086(murD)
            ECE: Z0098(murD)
            ECS: ECs0092
            ECC: c0106(murD)
            ECI: UTI89_C0097(murD)
            ECP: ECP_0090
            ECV: APECO1_1898(murD)
            ECW: EcE24377A_0090(murD)
            ECX: EcHS_A0094
            STY: STY0146(murD)
            STT: t0130(murD)
            SPT: SPA0128(murD)
            SEC: SC0123(murD)
            STM: STM0126(murD)
            YPE: YPO0553(murD)
            YPK: y3628(murD)
            YPM: YP_3631(murD)
            YPA: YPA_3548
            YPN: YPN_0419
            YPP: YPDSF_3089
            YPS: YPTB0686(murD)
            YPI: YpsIP31758_3389(murD)
            YEN: YE0670(murD)
            SFL: SF0085(murD)
            SFX: S0087(murD)
            SFV: SFV_0081(murD)
            SSN: SSON_0096(murD)
            SBO: SBO_0076(murD)
            SDY: SDY_0118(murD)
            ECA: ECA3817(murD)
            PLU: plu3656(murD)
            BUC: BU218(murD)
            BAS: BUsg212(murD)
            BAB: bbp200(murD)
            WBR: WGLp208(murD)
            SGL: SG0447
            ENT: Ent638_0634
            KPN: KPN_00092(murD)
            BFL: Bfl140(murD)
            BPN: BPEN_144(murD)
            HIN: HI1136(murD)
            HIT: NTHI1303(murD)
            HIP: CGSHiEE_06370(murD)
            HIQ: CGSHiGG_09345(murD)
            HDU: HD0245(murD)
            HSO: HS_0356(murD)
            PMU: PM0140(murD)
            MSU: MS1669(murD)
            APL: APL_0016(murD)
            XFA: XF1118
            XFT: PD0410(murD)
            XCC: XCC2738(murD)
            XCB: XC_1375
            XCV: XCV3053(murD)
            XAC: XAC2908(murD)
            XOO: XOO1436(murD)
            XOM: XOO_1320(XOO1320)
            VCH: VC2403
            VCO: VC0395_A1981(murD)
            VVU: VV1_0580
            VVY: VV0612
            VPA: VP0458
            VFI: VF2203(murD)
            PPR: PBPRA3217(murD)
            PAE: PA4414(murD)
            PAU: PA14_57370(murD)
            PAP: PSPA7_4986(murD)
            PPU: PP_1335(murD)
            PST: PSPTO_4410(murD)
            PSB: Psyr_4104
            PSP: PSPPH_4110(murD)
            PFL: PFL_5063(murD)
            PFO: Pfl_4675
            PEN: PSEEN4487(murD)
            PAR: Psyc_2040(murD)
            PCR: Pcryo_2343
            ACI: ACIAD0270(murD)
            ACB: A1S_0245
            SON: SO_4221(murD)
            SDN: Sden_0353
            SFR: Sfri_3806
            SAZ: Sama_0352
            SBL: Sbal_0400
            SLO: Shew_3455
            SPC: Sputcn32_0485
            SHE: Shewmr4_3572
            SHM: Shewmr7_0384
            SHN: Shewana3_3745
            SHW: Sputw3181_0388
            ILO: IL0434(murD)
            CPS: CPS_4467(murD)
            PHA: PSHAa2506(murD)
            PAT: Patl_3521
            SDE: Sde_0846
            PIN: Ping_1145
            MAQ: Maqu_2454
            CBU: CBU_0131(murD)
            CBD: COXBU7E912_1975(murD)
            LPN: lpg2616(murD)
            LPF: lpl2539(murD)
            LPP: lpp2669(murD)
            MCA: MCA2431(murD)
            FTU: FTT0451(murD)
            FTF: FTF0451(murD)
            FTW: FTW_1619(murD)
            FTL: FTL_1614
            FTH: FTH_1561(murD)
            FTA: FTA_1702(murD)
            FTN: FTN_0542(murD)
            TCX: Tcr_0566
            NOC: Noc_2863
            AEH: Mlg_2195
            HHA: Hhal_2093
            HCH: HCH_05885(murD)
            CSA: Csal_2192
            ABO: ABO_0596(murD)
            AHA: AHA_3886(murD)
            DNO: DNO_0983(murD)
            BCI: BCI_0520(murD)
            RMA: Rmag_0766
            VOK: COSY_0704(murD)
            NME: NMB0420
            NMA: NMA2064(murD)
            NMC: NMC1745(murD)
            NGO: NGO1535(murD)
            CVI: CV_4345(murD)
            RSO: RSc2846(murD)
            REU: Reut_A2981
            REH: H16_A3275(murD)
            RME: Rmet_3130
            BMA: BMA2553(murD)
            BMV: BMASAVP1_A0474(murD)
            BML: BMA10299_A1333(murD)
            BMN: BMA10247_3230(murD)
            BXE: Bxe_A0484
            BUR: Bcep18194_A3643(murD)
            BCN: Bcen_0075
            BCH: Bcen2424_0557
            BAM: Bamb_0461
            BPS: BPSL3027(murD)
            BPM: BURPS1710b_3547(murD)
            BPL: BURPS1106A_3552(murD)
            BPD: BURPS668_3527(murD)
            BTE: BTH_I1116(murD)
            PNU: Pnuc_0165
            BPE: BP3025(murD)
            BPA: BPP3754(murD)
            BBR: BB4200(murD)
            RFR: Rfer_3427
            POL: Bpro_1073
            PNA: Pnap_3419
            AAV: Aave_0819
            AJS: Ajs_3672
            VEI: Veis_4568
            MPT: Mpe_A0460
            HAR: HEAR2813(murD)
            MMS: mma_3017
            NEU: NE0989(murD)
            NET: Neut_0248
            NMU: Nmul_A2496
            EBA: ebA1447(murD)
            AZO: azo0882(murD)
            DAR: Daro_3500
            TBD: Tbd_0117
            MFA: Mfla_2271
            HPY: HP0494(murD)
            HPA: HPAG1_0470
            HHE: HH1167(murD)
            HAC: Hac_0813(murD)
            WSU: WS2037(murD)
            TDN: Tmden_1616
            CJE: Cj0432c(murD)
            CJR: CJE0482(murD)
            CJJ: CJJ81176_0458(murD)
            CJU: C8J_0407(murD)
            CJD: JJD26997_1512(murD)
            CFF: CFF8240_1358(murD)
            CCV: CCV52592_1046(murD) CCV52592_1088
            CHA: CHAB381_1595(murD)
            CCO: CCC13826_0566(murD)
            ABU: Abu_1898(murD)
            NIS: NIS_0311(murD)
            SUN: SUN_2193(murD)
            GSU: GSU3071(murD)
            GME: Gmet_0410
            PCA: Pcar_2204
            DVU: DVU2506(murD)
            DDE: Dde_1040
            LIP: LI1102(murD)
            BBA: Bd0052(murD) Bd3200(murD)
            DPS: DP2899
            ADE: Adeh_3769
            MXA: MXAN_5606(murD)
            SAT: SYN_01744
            SFU: Sfum_3468
            RPR: RP410(murD)
            RTY: RT0396(murD)
            RCO: RC0560(murD)
            RFE: RF_0634(murD)
            RBE: RBE_0881(murD)
            RAK: A1C_03050(murD)
            RBO: A1I_02485(murD)
            RRI: A1G_03160(murD)
            OTS: OTBS_1528(murD)
            WOL: WD0849(murD)
            WBM: Wbm0508
            AMA: AM243(murD)
            PUB: SAR11_0026(murD)
            MLO: mll1557
            MES: Meso_2009
            SME: SMc01864(murD)
            ATU: Atu2096(murD)
            ATC: AGR_C_3803
            RET: RHE_CH02849(murD)
            RLE: RL3309(murD)
            BME: BMEI0577(murD)
            BMF: BAB1_1452(murD)
            BMS: BR1433(murD)
            BMB: BruAb1_1428(murD)
            BOV: BOV_1390(murD)
            BJA: bll6604(murD)
            BRA: BRADO5661(murD)
            BBT: BBta_6176(murD)
            RPA: RPA3532(murD)
            RPB: RPB_1992
            RPC: RPC_2192
            RPD: RPD_3396
            RPE: RPE_2105
            NWI: Nwi_1049(murD)
            NHA: Nham_1277
            BHE: BH11260(murD)
            BQU: BQ08880(murD)
            BBK: BARBAKC583_0949(murD)
            CCR: CC_2556
            SIL: SPO1187(murD)
            SIT: TM1040_0679
            RSP: RSP_2103(murD)
            JAN: Jann_2763
            RDE: RD1_3361(murD)
            MMR: Mmar10_2080
            HNE: HNE_3026(murD)
            ZMO: ZMO0829(murD)
            NAR: Saro_1131
            SAL: Sala_1883
            ELI: ELI_01785
            GOX: GOX0156
            GBE: GbCGDNIH1_0431
            RRU: Rru_A0952
            MAG: amb3846
            MGM: Mmc1_0755
            ABA: Acid345_3631
            BSU: BG10225(murD)
            BHA: BH2567(murD)
            BAN: BA4051(murD)
            BAR: GBAA4051(murD)
            BAA: BA_4521
            BAT: BAS3763
            BCE: BC3912(murD)
            BCA: BCE_3958(murD)
            BCZ: BCZK3671(murD)
            BTK: BT9727_3654(murD)
            BLI: BL02241(murD)
            BLD: BLi01737(murD)
            BCL: ABC2357(murD)
            BAY: RBAM_015060
            BPU: BPUM_1413
            OIH: OB1469(murD)
            GKA: GK1118(murD)
            SAU: SA1026(murD)
            SAV: SAV1183(murD)
            SAM: MW1066(murD)
            SAR: SAR1159(murD)
            SAS: SAS1117(murD)
            SAC: SACOL1196(murD)
            SAB: SAB1047(murD)
            SAA: SAUSA300_1077(murD)
            SAO: SAOUHSC_01147
            SEP: SE0858
            SER: SERP0748(murD)
            SHA: SH1732(murD)
            SSP: SSP1588
            LMO: lmo2036(murD)
            LMF: LMOf2365_2068(murD)
            LIN: lin2142(murD)
            LWE: lwe2050(murD)
            LLA: L0237(murD)
            LLC: LACR_1697
            LLM: llmg_0912(murD)
            SPY: SPy_1525(murD)
            SPZ: M5005_Spy_1253(murD)
            SPM: spyM18_1542(murD)
            SPG: SpyM3_1176(murD)
            SPS: SPs0686
            SPH: MGAS10270_Spy1269(murD)
            SPI: MGAS10750_Spy1361(murD)
            SPJ: MGAS2096_Spy1272(murD)
            SPK: MGAS9429_Spy1248(murD)
            SPF: SpyM50599(murD)
            SPA: M6_Spy1274(murD)
            SPB: M28_Spy1192(murD)
            SPN: SP_0688
            SPR: spr0603(murD)
            SPD: SPD_0598(murD)
            SAG: SAG0475(murD)
            SAN: gbs0522
            SAK: SAK_0577(murD)
            SMU: SMU.548(murD)
            STC: str0731(murD)
            STL: stu0731(murD)
            SSA: SSA_0652(murD)
            SGO: SGO_0671(murD)
            LPL: lp_2197(murD)
            LJO: LJ0971
            LAC: LBA0808(murD)
            LSA: LSA0747(murD)
            LSL: LSL_1051(murD)
            LDB: Ldb0740(murD)
            LBU: LBUL_0673
            LBR: LVIS_1450
            LCA: LSEI_1271
            EFA: EF0993(murD)
            OOE: OEOE_1147
            STH: STH1031
            CAC: CAC3194(murD)
            CPE: CPE2459(murD)
            CPF: CPF_2774(murD)
            CPR: CPR_2461(murD)
            CTC: CTC00213(murD)
            CNO: NT01CX_1049(murD)
            CDF: CD2653(murD)
            CBO: CBO3516(murD)
            CBA: CLB_3591(murD)
            CBH: CLC_3480(murD)
            CBF: CLI_3724(murD)
            CKL: CKL_0181(murD)
            CHY: CHY_2071(murD)
            DSY: DSY2909
            DRM: Dred_0673
            SWO: Swol_0824
            CSC: Csac_0923
            TTE: TTE1647(murD)
            MTA: Moth_0841
            MTU: Rv2155c(murD)
            MTC: MT2214(murD)
            MBO: Mb2179c(murD)
            MBB: BCG_2172c
            MLE: ML0912(murD)
            MPA: MAP1899c(murD)
            MAV: MAV_2334(murD)
            MSM: MSMEG_4229(murD)
            MMC: Mmcs_3258
            CGL: NCgl2080(murD)
            CGB: cg2371(murD)
            CEF: CE2055
            CDI: DIP1600
            CJK: jk0748(murD)
            NFA: nfa17640(murD)
            RHA: RHA1_ro01090(murD) RHA1_ro04218
            SCO: SCO2086(murD)
            SMA: SAV6120(murD)
            TWH: TWT226(murD)
            TWS: TW544(murD)
            LXX: Lxx15280(murD)
            CMI: CMM_1861(murD)
            AAU: AAur_1708(murD)
            PAC: PPA0756(murD)
            TFU: Tfu_1108
            FRA: Francci3_1413
            FAL: FRAAL0637(murD) FRAAL2194(murD)
            ACE: Acel_1008
            SEN: SACE_3574 SACE_5853(murD)
            BLO: BL1321(murD)
            BAD: BAD_1103(murD)
            RXY: Rxyl_1495
            FNU: FN1458
            CTR: CT758(murD)
            CTA: CTA_0828(murD)
            CMU: TC0139
            CPN: CPn0901(murD)
            CPA: CP0965
            CPJ: CPj0901(murD)
            CPT: CpB0933
            CCA: CCA00867(murD)
            CAB: CAB833
            CFE: CF0149(murD)
            PCU: pc1251(murD)
            BGA: BG0598(murD)
            BAF: BAPKO_0616(murD)
            TPA: TP0903
            TDE: TDE0370(murD)
            LIL: LA0838(murD)
            LIC: LIC12788(murD)
            LBJ: LBJ_0789(murD)
            LBL: LBL_2290(murD)
            SYN: sll2010(murD)
            SYW: SYNW0530(murD)
            SYC: syc2422_c(murD)
            SYF: Synpcc7942_1667
            SYD: Syncc9605_2153(murD)
            SYE: Syncc9902_0524(murD)
            SYG: sync_2260(murD)
            SYR: SynRCC307_1847(murD)
            SYX: SynWH7803_1984(murD)
            CYA: CYA_0960(murD)
            CYB: CYB_0292(murD)
            TEL: tll0073(murD)
            GVI: gll3732(murD)
            ANA: alr4112
            AVA: Ava_0793(murD) Ava_4285
            PMA: Pro1439(murD)
            PMM: PMM1364(murD)
            PMT: PMT1434(murD)
            PMN: PMN2A_0929
            PMI: PMT9312_1461
            PMB: A9601_15661(murD)
            PMC: P9515_15291(murD)
            PMF: P9303_05211(murD)
            PMG: P9301_15511(murD)
            PMH: P9215_15941
            PME: NATL1_17861(murD)
            TER: Tery_4482
            BTH: BT_3450
            BFR: BF0308
            BFS: BF0256(murD)
            PGI: PG0578(murD)
            SRU: SRU_0558(murD)
            CHU: CHU_2741(murD)
            GFO: GFO_2770(murD)
            FPS: FP2059(murD)
            CTE: CT0036(murD)
            CCH: Cag_0053
            PLT: Plut_2112
            DRA: DR_2496
            DGE: Dgeo_0485
            TTH: TTC0717
            TTJ: TTHA1082
            AAE: aq_2075(murD)
            TMA: TM0234
            MSI: Msm_1191
            MKA: MK0995(murD_1) MK1047(murD_2)
            RCI: RCIX2005(murD)
STRUCTURES  PDB: 1E0D  1EEH  1UAG  2JFF  2JFG  2JFH  2UAG  3UAG  4UAG  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.9
            ExPASy - ENZYME nomenclature database: 6.3.2.9
            ExplorEnz - The Enzyme Database: 6.3.2.9
            ERGO genome analysis and discovery system: 6.3.2.9
            BRENDA, the Enzyme Database: 6.3.2.9
            CAS: 9023-59-0
///
ENTRY       EC 6.3.2.10                 Enzyme
NAME        UDP-N-acetylmuramoyl-tripeptide---D-alanyl-D-alanine ligase;
            MurF synthetase;
            UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine
            synthetase;
            UDP-N-acetylmuramoylalanyl-D-glutamyl-lysine-D-alanyl-D-alanine
            ligase;
            uridine diphosphoacetylmuramoylpentapeptide synthetase;
            UDPacetylmuramoylpentapeptide synthetase;
            UDP-MurNAc-L-Ala-D-Glu-L-Lys:D-Ala-D-Ala ligase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine:D-alanyl-D-alanine
            ligase (ADP-forming)
REACTION    ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine +
            D-alanyl-D-alanine = ADP + phosphate +
            UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-
            alanine [RN:R04573]
ALL_REAC    R04573;
            (other) R04572 R04617
SUBSTRATE   ATP [CPD:C00002];
            UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine
            [CPD:C05892];
            D-alanyl-D-alanine [CPD:C00993]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-
            alanine [CPD:C04702]
COMMENT     Involved with EC 6.3.2.4 (D-alanine---D-alanine ligase), EC 6.3.2.7
            (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase) or EC
            6.3.2.13
            (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate
            ligase), EC 6.3.2.8 (UDP-N-acetylmuramate---L-alanine ligase) and EC
            6.3.2.9 (UDP-N-acetylmuramoyl-L-alanine---D-glutamate ligase) in the
            synthesis of a cell-wall peptide (click here) for diagram. This
            enzyme also catalyses the reaction when the C-terminal residue of
            the tripeptide is meso-2,4-diaminoheptanedioate (acylated at its
            L-centre), linking the D-Ala-D-Ala to the carboxy group of the
            L-centre. This activity was previously attributed to EC 6.3.2.15,
            which has since been deleted.
REFERENCE   1
  AUTHORS   Ito, E. and Strominger, J.L.
  TITLE     Enzymatic synthesis of the peptide in bacterial uridine nucleotides.
            II. Enzymatic synthesis and addition of D-alanyl-D-alanine.
  JOURNAL   J. Biol. Chem. 237 (1962) 2696-2703.
  ORGANISM  Staphylococcus aureus
REFERENCE   2  [PMID:11699883]
  AUTHORS   van Heijenoort J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit.
  JOURNAL   Nat. Prod. Rep. 18 (2001) 503-19.
  ORGANISM  Staphylococcus aureus
PATHWAY     PATH: map00300  Lysine biosynthesis
            PATH: map00550  Peptidoglycan biosynthesis
ORTHOLOGY   KO: K01929  UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-
                        diaminopimelate--D-alanyl-D-alanine ligase
GENES       ECO: b0086(murF)
            ECJ: JW0084(murF)
            ECE: Z0096(murF)
            ECS: ECs0090
            ECC: c0104(murF)
            ECI: UTI89_C0095(murF)
            ECP: ECP_0088
            ECV: APECO1_1900(murF)
            ECW: EcE24377A_0088(murF)
            ECX: EcHS_A0092
            STY: STY0144(murF)
            STT: t0128(murF)
            SPT: SPA0126(murF)
            SEC: SC0121(murF)
            STM: STM0124(murF)
            YPE: YPO0551(murF)
            YPK: y3630(murF)
            YPM: YP_3633(murF)
            YPA: YPA_3550
            YPN: YPN_0417
            YPP: YPDSF_3091
            YPS: YPTB0684(murF)
            YPI: YpsIP31758_3391(murF)
            YEN: YE0668(mra)
            SFL: SF0083(murF)
            SFX: S0085(murF)
            SFV: SFV_0079(murF)
            SSN: SSON_0094(murF)
            SBO: SBO_0074(murF)
            SDY: SDY_0116(murF)
            ECA: ECA3819(murF)
            PLU: plu3658(murF)
            BUC: BU220(murF)
            BAB: bbp202(murF)
            WBR: WGLp210(murF)
            SGL: SG0445
            BFL: Bfl138(murF)
            BPN: BPEN_142(murF)
            HIN: HI1134(murF)
            HIT: NTHI1301(murF)
            HDU: HD0243(murF)
            HSO: HS_0354(murF)
            PMU: PM0138(murF)
            MSU: MS1671(murF)
            APL: APL_0014(murF)
            XFA: XF0794
            XFT: PD1869(murF)
            XCC: XCC0722(murF)
            XCB: XC_3513
            XCV: XCV0827(murF)
            XAC: XAC0776(murF)
            XOO: XOO3829(murF)
            XOM: XOO_3607(XOO3607)
            VCH: VC2405
            VCO: VC0395_A1983(murF)
            VVU: VV1_0582
            VVY: VV0610
            VPA: VP0456
            VFI: VF2205
            PPR: PBPRA3219
            PAE: PA4416(murF)
            PAU: PA14_57390(murF)
            PPU: PP_1333(murF)
            PST: PSPTO_4412(murF)
            PSB: Psyr_4106
            PSP: PSPPH_4112(murF)
            PFL: PFL_5065(murF)
            PFO: Pfl_4677
            PEN: PSEEN4489(murF)
            PAR: Psyc_2052(murF)
            PCR: Pcryo_2376
            ACI: ACIAD3364(murF)
            SON: SO_4223(murF)
            SDN: Sden_0351
            SFR: Sfri_3808
            SAZ: Sama_0350
            SBL: Sbal_0398
            SLO: Shew_3457
            SHE: Shewmr4_3574
            SHM: Shewmr7_0382
            SHN: Shewana3_3747
            SHW: Sputw3181_0386
            ILO: IL0432(murF)
            CPS: CPS_4469(murF)
            PHA: PSHAa2508(murF)
            PAT: Patl_3523
            SDE: Sde_0844
            PIN: Ping_1143
            MAQ: Maqu_2456
            CBU: CBU_0124(murF)
            CBD: COXBU7E912_1982(murF)
            LPN: lpg2618(murF)
            LPF: lpl2541(murF)
            LPP: lpp2671(murF)
            MCA: MCA1294(murF)
            FTU: FTT0422(murF)
            FTF: FTF0422(murF)
            FTW: FTW_1651(murF)
            FTL: FTL_0492
            FTH: FTH_0490(murF)
            FTN: FTN_0522(murF)
            TCX: Tcr_0564
            NOC: Noc_2865
            AEH: Mlg_2197
            HHA: Hhal_2095
            HCH: HCH_05887
            CSA: Csal_2194
            ABO: ABO_0594(murF)
            AHA: AHA_3888(murF)
            DNO: DNO_0985(murF)
            BCI: BCI_0522(murF)
            VOK: COSY_0159(murF)
            NME: NMB0416
            NMA: NMA2068(murF)
            NMC: NMC1749(murF)
            NGO: NGO1539
            CVI: CV_4347(murF)
            RSO: RSc2848(murF)
            REU: Reut_A2983
            REH: H16_A3277(murF)
            RME: Rmet_3132
            BMA: BMA2555(murF)
            BMV: BMASAVP1_A0476(murF)
            BML: BMA10299_A1335(murF)
            BMN: BMA10247_3228(murF)
            BXE: Bxe_A0482
            BUR: Bcep18194_A3641
            BCN: Bcen_0073
            BCH: Bcen2424_0555
            BAM: Bamb_0459
            BPS: BPSL3029(murF)
            BPM: BURPS1710b_3549(murF)
            BPL: BURPS1106A_3554(murF)
            BPD: BURPS668_3529(murF)
            BTE: BTH_I1114
            PNU: Pnuc_0163
            BPE: BP3027(murE)
            BPA: BPP3756(murE)
            BBR: BB4202(murE)
            RFR: Rfer_3429
            POL: Bpro_1071
            PNA: Pnap_3421
            AAV: Aave_0817
            AJS: Ajs_3674
            VEI: Veis_4566
            MPT: Mpe_A0458
            HAR: HEAR2815(murF)
            MMS: mma_3019
            NEU: NE0987(murF)
            NET: Neut_0250
            NMU: Nmul_A2498
            EBA: ebA1449(murF)
            AZO: azo0880(murF)
            DAR: Daro_3502
            TBD: Tbd_0115
            MFA: Mfla_2273
            HPY: HP0740(murF)
            HPJ: jhp0677(murF)
            HPA: HPAG1_0724
            HHE: HH0128
            HAC: Hac_0679(murF)
            WSU: WS0436(murF)
            TDN: Tmden_1206
            CJE: Cj0795c(murF)
            CJR: CJE0886
            CJU: C8J_0746(murF)
            ABU: Abu_0747(murF)
            NIS: NIS_1093
            SUN: SUN_0832
            GME: Gmet_0408
            PCA: Pcar_2206
            PPD: Ppro_3293
            DVU: DVU2508(murF)
            DDE: Dde_1038
            LIP: LI1100(murF)
            BBA: Bd3204(murF)
            DPS: DP2901
            ADE: Adeh_3767
            MXA: MXAN_5608(murF)
            SAT: SYN_01742
            SFU: Sfum_3467
            RPR: RP596(murF)
            RTY: RT0584(murF)
            RCO: RC0911(murF)
            RFE: RF_0369(murF)
            RBE: RBE_0853(murF)
            WOL: WD1128(murF)
            WBM: Wbm0238
            AMA: AM807(murF)
            NSE: NSE_0478
            PUB: SAR11_0028(murEF)
            MLO: mll1559
            MES: Meso_2011
            SME: SMc01862(murF)
            ATU: Atu2098(murF)
            ATC: AGR_C_3808
            RET: RHE_CH02851(murF)
            RLE: RL3311(murF)
            BME: BMEI0575
            BMF: BAB1_1454
            BMS: BR1435(murF)
            BMB: BruAb1_1430(murF)
            BOV: BOV_1392(murF)
            BJA: bll6606
            BRA: BRADO5663(murF)
            BBT: BBta_6178(murF)
            RPA: RPA3534(murF)
            RPB: RPB_1990
            RPC: RPC_2190
            RPD: RPD_3398
            RPE: RPE_2103
            NWI: Nwi_1047
            NHA: Nham_1275
            BHE: BH11280(murF)
            BQU: BQ08900(murF)
            BBK: BARBAKC583_0951(murF)
            CCR: CC_2558
            SIL: SPO1183(murF)
            SIT: TM1040_2019
            RSP: RSP_2100(murF)
            JAN: Jann_2765
            RDE: RD1_3364(murF)
            MMR: Mmar10_2082
            HNE: HNE_3028(murF)
            ZMO: ZMO0827(murF)
            NAR: Saro_1129
            SAL: Sala_1885
            ELI: ELI_01775
            GOX: GOX0154
            GBE: GbCGDNIH1_0433
            RRU: Rru_A0954
            MAG: amb3844
            MGM: Mmc1_0757
            ABA: Acid345_3633
            BSU: BG12084(murF)
            BHA: BH2570(murF)
            BAN: BA0246(murF)
            BAR: GBAA0246(murF)
            BAT: BAS0232
            BCE: BC0258
            BCA: BCE_0266(murF) BCE_2244
            BCZ: BCZK0220(murF) BCZK1980(murF)
            BTK: BT9727_0218(murF) BT9727_1998(murF)
            BTL: BALH_0231(murF) BALH_1943(murF)
            BLI: BL02194(murF)
            BLD: BLi00544(murF)
            BCL: ABC2359(murF)
            BAY: RBAM_004910
            OIH: OB1467(murF)
            GKA: GK0224(murF)
            GTN: GTNG_0199
            SAU: SA1886(murF)
            SAV: SAV2082(murF)
            SAM: MW2005(murF)
            SAR: SAR2169
            SAS: SAS1986
            SAC: SACOL2073(murF)
            SAB: SAB1966c
            SAA: SAUSA300_2038(murF)
            SAO: SAOUHSC_02317
            SEP: SE1680
            SER: SERP1689(murF)
            SHA: SH0955(murF)
            SSP: SSP0801
            LMO: lmo0856(murF)
            LMF: LMOf2365_0873(murF)
            LIN: lin0849(murF)
            LWE: lwe0849(murF)
            LLA: L141766(murF)
            LLC: LACR_0388
            LLM: llmg_0361(murF)
            SPY: SPy_1420(murF)
            SPZ: M5005_Spy_1157(murF)
            SPM: spyM18_1429
            SPG: SpyM3_1083(murF)
            SPS: SPs0781
            SPH: MGAS10270_Spy1228(murF)
            SPI: MGAS10750_Spy1265(murF)
            SPJ: MGAS2096_Spy1228(murF)
            SPK: MGAS9429_Spy1204(murF)
            SPF: SpyM50703(murF)
            SPA: M6_Spy1184
            SPB: M28_Spy1151(murF)
            SPN: SP_1670
            SPR: spr1514(murF)
            SPD: SPD_1483(murF)
            SAG: SAG0768(murF)
            SAN: gbs0788
            SAK: SAK_0893(murF)
            SMU: SMU.603(murF)
            STC: str1576(murF)
            STL: stu1576(murF)
            STE: STER_1534
            SSA: SSA_0692(murF)
            SSU: SSU05_1350
            SSV: SSU98_1365
            SGO: SGO_1446(murF)
            LPL: lp_0518(murF)
            LJO: LJ0269
            LAC: LBA0266
            LSA: LSA1616(murF)
            LSL: LSL_0355(murF)
            LDB: Ldb0357(murF)
            LBU: LBUL_0312
            LBR: LVIS_0503
            LCA: LSEI_2563
            LGA: LGAS_0264
            PPE: PEPE_1562
            EFA: EF0845(murF)
            OOE: OEOE_1644
            LME: LEUM_0452
            STH: STH1207
            CAC: CAC2128(murF)
            CPE: CPE1861(murF)
            CPF: CPF_2115(murF)
            CPR: CPR_1829(murF)
            CTC: CTC01631
            CNO: NT01CX_1938
            CTH: Cthe_0977
            CDF: CD2655(murF)
            CBO: CBO1458(murF)
            CBA: CLB_1483(murF)
            CBH: CLC_1495(murF)
            CBF: CLI_1542(murF)
            CKL: CKL_1185(murF)
            CHY: CHY_2073(murF)
            DSY: DSY2911 DSY3693
            DRM: Dred_0671
            PTH: PTH_1865(murF)
            SWO: Swol_0822
            TTE: TTE2546(murF)
            MTA: Moth_0839
            MTU: Rv2157c(murF)
            MTC: MT2216(murF)
            MBO: Mb2181c(murF)
            MBB: BCG_2174c(murF)
            MLE: ML0910(murF)
            MPA: MAP1901c(murF)
            MAV: MAV_2332
            MSM: MSMEG_4231
            MMC: Mmcs_3260
            CGL: NCgl2082(cgl2162)
            CGB: cg2373(murF)
            CEF: CE2057(murF)
            CDI: DIP1602(murF)
            CJK: jk0746(murF)
            NFA: nfa17620(murF)
            RHA: RHA1_ro01092(murF)
            SCO: SCO2088(murF)
            SMA: SAV6118(murF)
            TWH: TWT223(murF)
            TWS: TW547(murF)
            LXX: Lxx15300(murF)
            CMI: CMM_1863(murF)
            AAU: AAur_1706(murF)
            PAC: PPA0754
            NCA: Noca_3067
            TFU: Tfu_1106
            FRA: Francci3_1411
            FAL: FRAAL2192(murF)
            ACE: Acel_1006
            SEN: SACE_5855(murF)
            BLO: BL1319(murF)
            BAD: BAD_1105(murF)
            RXY: Rxyl_1497
            FNU: FN1461
            CTR: CT756(murF)
            CTA: CTA_0826(murF)
            CMU: TC0137
            CPN: CPn0899(murF)
            CPA: CP0967
            CPJ: CPj0899(murF)
            CPT: CpB0931
            CCA: CCA00869(murF)
            CAB: CAB835
            CFE: CF0147(murF)
            PCU: pc0631(alr) pc1253(murF)
            BBU: BB0304(murF)
            BGA: BG0308(murF)
            BAF: BAPKO_0315(murF)
            TPA: TP0386
            TDE: TDE1200(murF)
            LIL: LA1464(murF)
            LIC: LIC12291(murF)
            LBJ: LBJ_0963(murF)
            LBL: LBL_2070(murF)
            SYN: slr1351(murF)
            SYW: SYNW1002(murF)
            SYC: syc2253_d(murF)
            SYF: Synpcc7942_1841
            SYD: Syncc9605_1128
            SYE: Syncc9902_1329
            SYG: sync_1531
            SYR: SynRCC307_1146(murF)
            SYX: SynWH7803_1028(murF)
            CYA: CYA_0077(murF)
            CYB: CYB_2039(murF)
            TEL: tlr1553(murF)
            GVI: glr2398(murF)
            ANA: all0036(murF)
            AVA: Ava_2637
            PMA: Pro1051(murF)
            PMM: PMM0610(murF)
            PMT: PMT0401(murF)
            PMN: PMN2A_0046
            PMI: PMT9312_0610
            PMB: A9601_06661(murF)
            PMC: P9515_06751(murF)
            PMF: P9303_18861(murF)
            PMG: P9301_06361(murF)
            PMH: P9215_06921
            PME: NATL1_06661(murF)
            TER: Tery_0495
            BTH: BT_3644 BT_4101
            BFR: BF0451 BF0892
            BFS: BF0391(murF) BF0816
            PGI: PG1097 PG1106(murF)
            SRU: SRU_2342
            CHU: CHU_0699(murF)
            GFO: GFO_2893(murF)
            FPS: FP1390(murF)
            CTE: CT0038(murF)
            CCH: Cag_0051
            PLT: Plut_2114
            DRA: DR_0768
            DGE: Dgeo_1723
            TTH: TTC0714
            TTJ: TTHA1079
            AAE: aq_821(murF)
            TMA: TM0236
STRUCTURES  PDB: 2AM1  2AM2  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.10
            ExPASy - ENZYME nomenclature database: 6.3.2.10
            ExplorEnz - The Enzyme Database: 6.3.2.10
            ERGO genome analysis and discovery system: 6.3.2.10
            BRENDA, the Enzyme Database: 6.3.2.10
            CAS: 9023-60-3
///
ENTRY       EC 6.3.2.11                 Enzyme
NAME        carnosine synthase;
            carnosine synthetase;
            carnosine-anserine synthetase;
            homocarnosine-carnosine synthetase;
            carnosine-homocarnosine synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     L-histidine:beta-alanine ligase (AMP-forming)
REACTION    ATP + L-histidine + beta-alanine = AMP + diphosphate + carnosine
            [RN:R01164]
ALL_REAC    R01164;
            (other) R00910 R00912 R01991 R03286
SUBSTRATE   ATP [CPD:C00002];
            L-histidine [CPD:C00135];
            beta-alanine [CPD:C00099]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            carnosine [CPD:C00386]
REFERENCE   1  [PMID:14404206]
  AUTHORS   KALYANKAR GD, MEISTER A.
  TITLE     Enzymatic synthesis of carnosine and related beta-alanyl and
            gamma-aminobutyryl peptides.
  JOURNAL   J. Biol. Chem. 234 (1959) 3210-8.
  ORGANISM  chicken [GN:gga]
REFERENCE   2
  AUTHORS   Stenesh, J.J. and Winnick, T.
  TITLE     Carnosine-anserine synthetase of muscle. 4. Partial purification of
            the enzyme and further studies of beta-alanyl peptide synthesis.
  JOURNAL   Biochem. J. 77 (1960) 575-581.
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00252  Alanine and aspartate metabolism
            PATH: map00340  Histidine metabolism
            PATH: map00410  beta-Alanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.11
            ExPASy - ENZYME nomenclature database: 6.3.2.11
            ExplorEnz - The Enzyme Database: 6.3.2.11
            ERGO genome analysis and discovery system: 6.3.2.11
            BRENDA, the Enzyme Database: 6.3.2.11
            CAS: 9023-61-4
///
ENTRY       EC 6.3.2.12                 Enzyme
NAME        dihydrofolate synthase;
            dihydrofolate synthetase;
            7,8-dihydrofolate synthetase;
            H2-folate synthetase;
            7,8-dihydropteroate:L-glutamate ligase (ADP);
            dihydrofolate synthetase-folylpolyglutamate synthetase;
            folylpoly-(gamma-glutamate) synthetase-dihydrofolate synthase;
            FHFS;
            FHFS/FPGS;
            dihydropteroate:L-glutamate ligase (ADP-forming);
            DHFS
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     7,8-dihydropteroate:L-glutamate ligase (ADP-forming)
REACTION    ATP + 7,8-dihydropteroate + L-glutamate = ADP + phosphate +
            7,8-dihydropteroylglutamate [RN:R02237]
ALL_REAC    R02237;
            (other) R01654
SUBSTRATE   ATP [CPD:C00002];
            7,8-dihydropteroate [CPD:C00921];
            L-glutamate [CPD:C00025]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            7,8-dihydropteroylglutamate [CPD:C00415]
COMMENT     In some bacteria, a single protein catalyses both this activity and
            that of EC 6.3.2.17, tetrahydrofolate synthase [2], the combined
            activity of which leads to the formation of the coenzyme
            polyglutamated tetrahydropteroate (H4PteGlun), i.e. various
            tetrahydrofolates. In contrast, the activities are located on
            separate proteins in most eukaryotes studied to date [3]. This
            enzyme is reponsible for attaching the first glutamate residue to
            dihydropteroate to form dihydrofolate and is present only in those
            organisms that have the ability to synthesize tetrahydrofolate de
            novo, e.g. plants, most bacteria, fungi and protozoa [3].
REFERENCE   1  [PMID:14114858]
  AUTHORS   GRIFFIN MJ, BROWN GM.
  TITLE     THE BIOSYNTHESIS OF FOLIC ACID. III. ENZYMATIC FORMATION OF
            DIHYDROFOLIC ACID FROM DIHYDROPTEROIC ACID AND OF
            TETRAHYDROPTEROYLPOLYGLUTAMIC ACID COMPOUNDS FROM TETRAHYDROFOLIC
            ACID.
  JOURNAL   J. Biol. Chem. 239 (1964) 310-6.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:2985605]
  AUTHORS   Bognar AL, Osborne C, Shane B, Singer SC, Ferone R.
  TITLE     Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase.
            Cloning and high expression of the Escherichia coli folC gene and
            purification and properties of the gene product.
  JOURNAL   J. Biol. Chem. 260 (1985) 5625-30.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:11752472]
  AUTHORS   Ravanel S, Cherest H, Jabrin S, Grunwald D, Surdin-Kerjan Y, Douce
            R, Rebeille F.
  TITLE     Tetrahydrofolate biosynthesis in plants: molecular and functional
            characterization of dihydrofolate synthetase and three isoforms of
            folylpolyglutamate synthetase in Arabidopsis thaliana.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 15360-5.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   4  [PMID:10799479]
  AUTHORS   Cherest H, Thomas D, Surdin-Kerjan Y.
  TITLE     Polyglutamylation of folate coenzymes is necessary for methionine
            biosynthesis and maintenance of intact mitochondrial genome in
            Saccharomyces cerevisiae.
  JOURNAL   J. Biol. Chem. 275 (2000) 14056-63.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   5  [PMID:9190084]
  AUTHORS   Cossins EA, Chen L.
  TITLE     Folates and one-carbon metabolism in plants and fungi.
  JOURNAL   Phytochemistry. 45 (1997) 437-52.
  ORGANISM  Escherichia coli [GN:eco], Neurospora crassa [GN:dncr],
            Corynebacterium sp.
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K01927  dihydrofolate synthase
GENES       CME: CMQ033C
            PFA: PF13_0140
            TAN: TA20775
            ECO: b2315(folC)
            ECJ: JW2312(folC)
            ECE: Z3577(folC)
            ECS: ECs3199
            ECC: c2860(folC)
            ECI: UTI89_C2600(folC)
            ECP: ECP_2354
            ECV: APECO1_4249(folC)
            ECW: EcE24377A_2609(folC)
            ECX: EcHS_A2466(folC)
            STY: STY2596(folC)
            STT: t0499(folC)
            SPT: SPA0499(folC)
            SEC: SC2367(folC)
            STM: STM2365(folC)
            YPE: YPO2769(folC)
            YPK: y1602(folC)
            YPM: YP_2395(folC)
            YPA: YPA_2075
            YPN: YPN_2178
            YPS: YPTB2615(folC)
            YPI: YpsIP31758_1423(folC)
            YEN: YE1312(dedC)
            SFL: SF2391(folC)
            SFX: S2526(folC)
            SFV: SFV_2384(folC)
            SSN: SSON_2373(folC)
            SBO: SBO_2352(folC)
            SDY: SDY_2514(folC)
            ECA: ECA3055(folC)
            PLU: plu3170(folC)
            BUC: BU167(folC)
            BAS: BUsg161(folC)
            BAB: bbp157(folC)
            WBR: WGLp311(folC)
            SGL: SG1616
            ENT: Ent638_2864
            BFL: Bfl494(folC)
            BPN: BPEN_510(folC)
            HIT: NTHI1903(folC)
            HSO: HS_0880(folC)
            PMU: PM0635(folC)
            MSU: MS1173(folC)
            XFA: XF1946
            XFT: PD0854(folC)
            XCC: XCC0950(folC)
            XCB: XC_3285
            XCV: XCV1058(folC)
            XAC: XAC1029(folC)
            XOO: XOO3679(folC)
            XOM: XOO_3475(XOO3475)
            VCH: VC1001
            VVU: VV1_1994
            VVY: VV2422
            VPA: VP2188
            VFI: VF1694
            PPR: PBPRA2651
            PAE: PA3111(folC)
            PAU: PA14_23880(folC)
            PPU: PP_1997(folC)
            PST: PSPTO_3814(folC)
            PSB: Psyr_1665
            PSP: PSPPH_1659(folC)
            PFL: PFL_2074(folC)
            PFO: Pfl_1899
            PEN: PSEEN1692(folC)
            PMY: Pmen_2714
            PAR: Psyc_0435(folC)
            PCR: Pcryo_0470
            ACI: ACIAD0644(folC)
            SON: SO_3067(folC)
            SDN: Sden_1487
            SFR: Sfri_1396
            SAZ: Sama_2149
            SBM: Shew185_2758
            SLO: Shew_2305
            SPC: Sputcn32_2440
            SSE: Ssed_1653
            SHE: Shewmr4_1427
            SHM: Shewmr7_1492
            SHN: Shewana3_1480
            SHW: Sputw3181_1568
            ILO: IL1015(folC)
            CPS: CPS_3801(folC)
            PHA: PSHAa2073(folC)
            PAT: Patl_1606
            SDE: Sde_2076
            PIN: Ping_1968
            MAQ: Maqu_1555
            CBU: CBU_0894(folC)
            LPN: lpg1342(folC)
            LPF: lpl1295(folC)
            LPP: lpp1296(folC)
            MCA: MCA2492(folC)
            FTU: FTT0371c(folC)
            FTF: FTF0371c(folC)
            FTW: FTW_1705(folC)
            FTL: FTL_1308
            FTH: FTH_1280(folC)
            FTN: FTN_0273(folC)
            TCX: Tcr_0806
            NOC: Noc_1023
            AEH: Mlg_1239
            CSA: Csal_1264
            ABO: ABO_1458(folC)
            AHA: AHA_2678(folC)
            BCI: BCI_0366(folC)
            VOK: COSY_0895(folC)
            NME: NMB0693
            NMA: NMA0896(folC)
            NMC: NMC0644(folC)
            NGO: NGO0266
            CVI: CV_2518(folC)
            RSO: RSc1979(folC)
            REU: Reut_A2302
            RME: Rmet_2463
            BMA: BMAA1717(folC)
            BMV: BMASAVP1_1653(folC)
            BML: BMA10299_1862(folC)
            BMN: BMA10247_A0533(folC)
            BVI: Bcep1808_4466
            BCN: Bcen_4405
            BCH: Bcen2424_3962
            BPS: BPSS1695(folC)
            BPM: BURPS1710b_A0765(folC)
            BPL: BURPS1106A_A2303(folC)
            BPD: BURPS668_A2441(folC)
            BTE: BTH_II0683
            PNU: Pnuc_0775
            BPE: BP1412(folC)
            BPA: BPP1519(folC)
            BBR: BB2597(folC)
            RFR: Rfer_2686
            POL: Bpro_1604
            PNA: Pnap_1089
            AAV: Aave_1860
            MPT: Mpe_A2154
            HAR: HEAR1226(folC)
            MMS: mma_2161(folC)
            NEU: NE0696(folC)
            NET: Neut_1155
            NMU: Nmul_A1909
            AZO: azo1050(folC)
            DAR: Daro_0873
            TBD: Tbd_1911
            MFA: Mfla_1695
            HPY: HP1545(folC)
            HPJ: jhp1454(folC)
            HHE: HH0462(folC)
            HAC: Hac_0295(folC)
            WSU: WS1242(folC)
            TDN: Tmden_1569
            CJE: Cj1088c(folC)
            CJR: CJE1231(folC)
            CJU: C8J_1029(folC)
            ABU: Abu_0404(folC)
            NIS: NIS_1462(folC)
            SUN: SUN_2042(folC)
            MXA: MXAN_2705(folC)
            SAT: SYN_01606
            SFU: Sfum_1671
            RPR: RP536(folC)
            RTY: RT0524(folC)
            RCO: RC0779(folC)
            WOL: WD1052(folC)
            AMA: AM699(folC)
            APH: APH_0747(folC)
            ERU: Erum3680(folC)
            ERW: ERWE_CDS_03790(folC)
            ERG: ERGA_CDS_03740(folC)
            ECN: Ecaj_0353
            ECH: ECH_0702(folC)
            NSE: NSE_0715(folC)
            PUB: SAR11_0485(folC)
            MLO: mlr5076(folC)
            MES: Meso_0662
            SME: SMc02763(folC)
            ATU: Atu0021(folC)
            ATC: AGR_C_35(folC)
            RET: RHE_CH00024(folC)
            RLE: RL0024(folC)
            BME: BMEI2021
            BMF: BAB1_2108(folC)
            BMS: BR2106(folC)
            BMB: BruAb1_2081(folC)
            BJA: blr0748(folC)
            BRA: BRADO0088
            BBT: BBta_0094
            RPA: RPA0072(folC)
            RPB: RPB_0632
            RPC: RPC_0389
            RPD: RPD_0200
            RPE: RPE_0457
            NWI: Nwi_0052
            NHA: Nham_0060
            BHE: BH00330(folC)
            BQU: BQ00310(folC)
            CCR: CC_3541(folC)
            SIL: SPO3818(folC)
            SIT: TM1040_2675
            RSP: RSP_0930(folC)
            RDE: RD1_0327(folC)
            MMR: Mmar10_0088
            ZMO: ZMO0582(folC)
            GOX: GOX1205
            GBE: GbCGDNIH1_2012
            MAG: amb4014
            SPY: SPy_0814(folC.2) SPy_1096(folC.1)
            SPZ: M5005_Spy_0628(folC.2) M5005_Spy_0820(folC.1)
            SPH: MGAS10270_Spy0684(folC2) MGAS10270_Spy0936(folC1)
            SPI: MGAS10750_Spy0716(folC2) MGAS10750_Spy0971(folC1)
            SPJ: MGAS2096_Spy0693(folC2) MGAS2096_Spy0894(folC1)
            SPK: MGAS9429_Spy0683(folC2) MGAS9429_Spy0939(folC1)
            SPA: M6_Spy0645 M6_Spy0818
            SPB: M28_Spy0608(folC.2) M28_Spy0797(folC.1)
            SPN: SP_0197 SP_0290
            SPR: spr0178(folC) spr0267(sulB)
            SPD: SPD_0183(folC) SPD_0270
            SSA: SSA_0198 SSA_2237
            SGO: SGO_1913 SGO_2039
            LSL: LSL_1071(folC)
            CPF: CPF_2174(folC)
            CPR: CPR_1885(folC)
            CBA: CLB_3198(folC)
            CBH: CLC_3072(folC)
            CBF: CLI_3227(folC)
            MMY: MSC_0942(folC)
            MTU: Rv2447c(folC)
            MTC: MT2523(folC)
            MBO: Mb2474c(folC)
            MLE: ML1471(folC)
            MPA: MAP2270c(folC)
            CGL: NCgl2292(cgl2375)
            CGB: cg2608(folC)
            CEF: CE2281
            CDI: DIP1785
            CJK: jk0551(folC)
            NFA: nfa13490(folC)
            SCO: SCO2614(fpgS)
            SMA: SAV5452(fpgS)
            TWH: TWT476(folC)
            TWS: TW288(fgs)
            LXX: Lxx07980(folC)
            PAC: PPA0821
            TFU: Tfu_2190
            FRA: Francci3_1208 Francci3_1209
            FAL: FRAAL1913(folC) FRAAL1914
            SEN: SACE_1387(folC)
            BLO: BL1353(folC)
            BAD: BAD_1088(folC)
            FNU: FN1014
            LIL: LA0637(folC)
            LBJ: LBJ_2330(folC)
            LBL: LBL_0778(folC)
            SYN: sll1612(folC)
            SYW: SYNW1635(folC)
            SYC: syc0598_c(folC)
            SYF: Synpcc7942_0944
            SYR: SynRCC307_0610(folC)
            SYX: SynWH7803_1748(folC)
            CYA: CYA_1353(folC)
            CYB: CYB_1382(folC)
            TEL: tlr0190(folC)
            GVI: glr1074(folC)
            ANA: alr1026
            AVA: Ava_3683
            PMA: Pro1376(folC)
            PMM: PMM1302(folC)
            PMT: PMT0330(folC)
            PMB: A9601_15011(folC)
            PMC: P9515_14631(folC)
            PMF: P9303_19851(folC)
            PMG: P9301_14881(folC)
            PMH: P9215_15311(folC)
            PME: NATL1_17221(folC)
            TER: Tery_1603
            FPS: FP0541(folC)
            DRA: DR_0340
            DGE: Dgeo_0083
            TTH: TTC0975
            TTJ: TTHA1340
            AAE: aq_2045(folC)
            TMA: TM0166
            HAL: VNG0412G(folP)
            TAC: Ta0637
            TVO: TVN0757
            PTO: PTO1256
STRUCTURES  PDB: 1W78  1W7K  2BMB  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.12
            ExPASy - ENZYME nomenclature database: 6.3.2.12
            ExplorEnz - The Enzyme Database: 6.3.2.12
            ERGO genome analysis and discovery system: 6.3.2.12
            BRENDA, the Enzyme Database: 6.3.2.12
            CAS: 37318-62-0
///
ENTRY       EC 6.3.2.13                 Enzyme
NAME        UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate
            ligase;
            MurE synthetase [ambiguous];
            UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-2,6-diamino-
            heptanedioate ligase (ADP-forming);
            UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelate
            synthetase;
            UDP-N-acetylmuramoylalanyl-D-glutamate---2,6-diaminopimelate ligase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:(L)-meso-2,6-diaminoheptan
            edioate gamma-ligase (ADP-forming)
REACTION    ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate +
            meso-2,6-diaminoheptanedioate = ADP + phosphate +
            UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-
            heptanedioate [RN:R02788]
ALL_REAC    R02788
SUBSTRATE   ATP [CPD:C00002];
            UDP-N-acetylmuramoyl-L-alanyl-D-glutamate [CPD:C00692];
            meso-2,6-diaminoheptanedioate [CPD:C00680]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-
            heptanedioate [CPD:C04877]
COMMENT     Involved with EC 6.3.2.4 (D-alanine---D-alanine ligase), EC 6.3.2.8
            (UDP-N-acetylmuramate---L-alanine ligase), EC 6.3.2.9
            (UDP-N-acetylmuramoyl-L-alanine---D-glutamate ligase) and EC
            6.3.2.10 (UDP-N-acetylmuramoyl-tripeptide---D-alanyl-D-alanine
            ligase) in the synthesis of a cell-wall peptide (click here for
            diagram). This enzyme adds diaminopimelate in Gram-negative
            organisms and in some Gram-positive organisms; in others EC 6.3.2.7
            (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase) adds
            lysine instead. It is the amino group of the L-centre of the
            diaminopimelate that is acylated.
REFERENCE   1  [PMID:4967958]
  AUTHORS   Mizuno Y, Ito E.
  TITLE     Purification and properties of uridine diphosphate
            N-acetylmuramyl-L-alanyl-D-glutamate:meso-2,6-diaminopimelate
            ligase.
  JOURNAL   J. Biol. Chem. 243 (1968) 2665-72.
  ORGANISM  Bacillus cereus
REFERENCE   2  [PMID:11699883]
  AUTHORS   van Heijenoort J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit.
  JOURNAL   Nat. Prod. Rep. 18 (2001) 503-19.
  ORGANISM  Staphylococcus aureus
PATHWAY     PATH: map00300  Lysine biosynthesis
            PATH: map00550  Peptidoglycan biosynthesis
ORTHOLOGY   KO: K01928  UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-
                        diaminopimelate ligase
GENES       ECO: b0085(murE)
            ECJ: JW0083(murE)
            ECE: Z0095(murE)
            ECS: ECs0089
            ECC: c0103(murE)
            ECI: UTI89_C0094(murE)
            ECP: ECP_0087
            ECV: APECO1_1901(murE)
            ECW: EcE24377A_0087(murE)
            ECX: EcHS_A0091
            STY: STY0143(murE)
            STT: t0127(murE)
            SPT: SPA0125(murE)
            SEC: SC0120(murE)
            STM: STM0123(murE)
            YPE: YPO0550(murE)
            YPK: y3631(murE)
            YPM: YP_3634(murE)
            YPA: YPA_3551
            YPN: YPN_0416
            YPP: YPDSF_3092
            YPS: YPTB0683(murE)
            YPI: YpsIP31758_3392(murE)
            YEN: YE0667(murE)
            SFX: S0084(murE)
            SFV: SFV_0078(murE)
            SSN: SSON_0093(murE)
            SBO: SBO_0073(murE)
            SDY: SDY_0115(murE)
            ECA: ECA3820(murE)
            PLU: plu3659(murE)
            BUC: BU221(murE)
            BAB: bbp203(murE)
            WBR: WGLp211(murE)
            SGL: SG0444
            BFL: Bfl137(murE)
            BPN: BPEN_141(murE)
            HIN: HI1133(murE)
            HIT: NTHI1300(murE)
            HIP: CGSHiEE_06395(murE)
            HIQ: CGSHiGG_09330(murE)
            HDU: HD0242(murE)
            HSO: HS_0353(murE)
            PMU: PM0137(murE)
            MSU: MS1672(murE)
            APL: APL_0013(murE)
            XFA: XF0793
            XFT: PD1870(murE)
            XCC: XCC0721(murE)
            XCB: XC_3514
            XCV: XCV0826(murE)
            XAC: XAC0775(murE)
            XOO: XOO3830(murE)
            XOM: XOO_3608(XOO3608)
            VCH: VC2406
            VCO: VC0395_A1984(murE)
            VVU: VV1_0583
            VVY: VV0609
            VPA: VP0455
            VFI: VF2206
            PPR: PBPRA3220
            PAE: PA4417(murE)
            PAU: PA14_57410(murE)
            PPU: PP_1332(murE)
            PST: PSPTO_4413(murE)
            PSB: Psyr_4107
            PSP: PSPPH_4113(murE)
            PFL: PFL_5066(murE)
            PFO: Pfl_4678
            PEN: PSEEN4490(murE)
            PAR: Psyc_2053(murE)
            PCR: Pcryo_2377
            ACI: ACIAD3365(murE)
            ACB: A1S_3203
            SON: SO_4224(murE)
            SDN: Sden_0350
            SFR: Sfri_3809
            SAZ: Sama_0349
            SBL: Sbal_0397
            SLO: Shew_3458
            SHE: Shewmr4_3575
            SHM: Shewmr7_0381
            SHN: Shewana3_3748
            SHW: Sputw3181_0385
            ILO: IL0431(murE)
            CPS: CPS_4470(murE)
            PHA: PSHAa2509(murE)
            PAT: Patl_3524
            SDE: Sde_0843
            PIN: Ping_1142
            MAQ: Maqu_2457
            CBU: CBU_0123(murE)
            CBD: COXBU7E912_1983(murE)
            LPN: lpg0917(murE)
            LPF: lpl0948(murE)
            LPP: lpp0978(murE)
            MCA: MCA2433(murE)
            FTU: FTT0420(murE)
            FTF: FTF0420(murE)
            FTW: FTW_1653(murE)
            FTL: FTL_0490
            FTH: FTH_0488(murE)
            FTN: FTN_0520(murE)
            TCX: Tcr_0563
            NOC: Noc_2866
            AEH: Mlg_2198
            HCH: HCH_05888
            CSA: Csal_2195
            ABO: ABO_0593(murE)
            AHA: AHA_3889(murE)
            DNO: DNO_0986(murE)
            BCI: BCI_0523(murE)
            VOK: COSY_0160(murE)
            NME: NMB0414
            NMA: NMA2071(murE)
            NMC: NMC1751(murE)
            NGO: NGO1541(murE)
            CVI: CV_4348(murE)
            RSO: RSc2849(murE)
            REU: Reut_A2984
            REH: H16_A3278(murE)
            RME: Rmet_3133
            BMA: BMA2556(murE)
            BMV: BMASAVP1_A0477(murE)
            BML: BMA10299_A1336(murE)
            BMN: BMA10247_3227(murE)
            BXE: Bxe_A0481
            BUR: Bcep18194_A3640(murE)
            BCN: Bcen_0072
            BCH: Bcen2424_0554
            BAM: Bamb_0458
            BPS: BPSL3030(murE)
            BPM: BURPS1710b_3550(murE)
            BPL: BURPS1106A_3555(murE)
            BPD: BURPS668_3530(murE)
            BTE: BTH_I1113
            PNU: Pnuc_0162
            BPE: BP3027(murE)
            BPA: BPP3756(murE)
            BBR: BB4202(murE)
            RFR: Rfer_3430
            POL: Bpro_1070
            MPT: Mpe_A0457
            HAR: HEAR2816(murE) HEAR3323
            MMS: mma_3020
            NEU: NE0986(murE)
            NET: Neut_0251
            NMU: Nmul_A2499
            EBA: ebA1450(murE)
            AZO: azo0879(murE)
            DAR: Daro_3503
            TBD: Tbd_0114
            MFA: Mfla_2274
            HPY: HP1494(murE)
            HPJ: jhp1387(murE)
            HPA: HPAG1_1419
            HHE: HH1865(murE)
            HAC: Hac_1754(murE)
            WSU: WS1688(murE)
            TDN: Tmden_0332
            CJE: Cj1641(murE)
            CJR: CJE1813(murE)
            CJJ: CJJ81176_1632(murE)
            CJU: C8J_1543(murE)
            CJD: JJD26997_2001(murE)
            CFF: CFF8240_0063(murE)
            CCV: CCV52592_1002
            CHA: CHAB381_0197
            ABU: Abu_0522(murE)
            NIS: NIS_0253(murE)
            SUN: SUN_2285(murE)
            GSU: GSU3074(murE)
            GME: Gmet_0407
            PCA: Pcar_2207
            DVU: DVU2509(murE)
            DDE: Dde_1037
            LIP: LI1099(murE)
            BBA: Bd3205(murE)
            DPS: DP2901
            ADE: Adeh_3766
            MXA: MXAN_5609(murE)
            SAT: SYN_01740
            SFU: Sfum_3466
            RPR: RP597(murE)
            RTY: RT0585(murE)
            RCO: RC0912(murE)
            RFE: RF_0368(murE)
            RBE: RBE_0852(murE)
            RAK: A1C_04670(murE)
            RBO: A1I_02660(murE)
            RRI: A1G_05035(murE)
            OTS: OTBS_0699(murE)
            WOL: WD0924(murE)
            WBM: Wbm0492
            AMA: AM282(murE)
            NSE: NSE_0245
            PUB: SAR11_0028(murEF)
            MLO: mll1560
            MES: Meso_2012
            SME: SMc01861(murE)
            ATU: Atu2099(murE)
            ATC: AGR_C_3809
            RET: RHE_CH02852(murE)
            RLE: RL3312(murE)
            BME: BMEI0574
            BMF: BAB1_1455(murE)
            BMS: BR1436(murE)
            BMB: BruAb1_1431(murE)
            BOV: BOV_1393(murE)
            BJA: bll6607(murE)
            BRA: BRADO5664(murE)
            BBT: BBta_6179(murE)
            RPA: RPA3535(murE)
            RPB: RPB_1989
            RPC: RPC_2189
            RPD: RPD_3399
            RPE: RPE_2102
            NWI: Nwi_1046(murE)
            NHA: Nham_1274
            BHE: BH11290(murE)
            BQU: BQ08910(murE)
            BBK: BARBAKC583_0952(murE)
            CCR: CC_2559
            SIL: SPO1182(murE)
            SIT: TM1040_2018
            RSP: RSP_2099(murE)
            JAN: Jann_2766
            RDE: RD1_3365(murE)
            MMR: Mmar10_2083
            HNE: HNE_3029(murE)
            ZMO: ZMO0826(murE)
            NAR: Saro_1128
            SAL: Sala_1886
            ELI: ELI_01770
            GOX: GOX0153
            GBE: GbCGDNIH1_0434
            RRU: Rru_A0955
            MAG: amb3843
            MGM: Mmc1_0758
            ABA: Acid345_3634
            BSU: BG10223(murE)
            BHA: BH2571(murE)
            BAN: BA4053(murE)
            BAR: GBAA4053(murE)
            BAA: BA_3100 BA_4524
            BAT: BAS2414 BAS3765
            BCE: BC3914(murE)
            BCA: BCE_2609(murE) BCE_3960(murE)
            BCZ: BCZK2336(murE) BCZK2337(murE) BCZK3673(murE)
            BTK: BT9727_2371(murE) BT9727_3656(murE)
            BTL: BALH_3544(murE)
            BLI: BL02239(murE)
            BLD: BLi01735(murE)
            BCL: ABC2360(murE) ABC3462
            BAY: RBAM_015040
            BPU: BPUM_1411
            OIH: OB1466(murE) OB1998
            GKA: GK1115(murE)
            SAU: SA0876(murE)
            SAV: SAV1018(murE)
            SAM: MW0899(murE)
            SAR: SAR0988(murE)
            SAS: SAS0887
            SAC: SACOL1023(murE)
            SAB: SAB0884(murE)
            SAA: SAUSA300_0919(murE)
            SAO: SAOUHSC_00954
            SEP: SE0718
            SER: SERP0607(murE)
            SHA: SH1941(murE)
            SSP: SSP1767
            LMO: lmo2038(murE)
            LMF: LMOf2365_2070(murE)
            LIN: lin2144(murE)
            LWE: lwe2052(murE)
            LLA: L53929(murE)
            LLC: LACR_1987
            LLM: llmg_1465(murC2) llmg_1989(murE)
            SPY: SPy_0388(murE)
            SPZ: M5005_Spy_0325(murE) M5005_Spy_0760
            SPM: spyM18_0440(murE)
            SPG: SpyM3_0284(murE)
            SPS: SPs1575
            SPH: MGAS10270_Spy0877
            SPI: MGAS10750_Spy0912
            SPJ: MGAS2096_Spy0834
            SPK: MGAS9429_Spy0874
            SPF: SpyM51533(murE)
            SPA: M6_Spy0351 M6_Spy0785
            SPB: M28_Spy0739
            SPN: SP_1530
            SPR: spr1384(murE)
            SPD: SPD_1359(murE)
            SAG: SAG1391(murE)
            SAN: gbs1461
            SAK: SAK_1424(murE)
            SMU: SMU.1677(murE)
            STC: str0349(murE)
            STL: stu0349(murE)
            SSA: SSA_1739(murE)
            SGO: SGO_1638(murE)
            LPL: lp_0977(murE1)
            LJO: LJ0565
            LAC: LBA1818(murE)
            LSA: LSA0280(murE) LSA1139
            LSL: LSL_0588(murE)
            LDB: Ldb0699(murE2) Ldb2044(murE)
            LBU: LBUL_0631 LBUL_1891
            LBR: LVIS_1292
            LCA: LSEI_0223 LSEI_1153
            EFA: EF0668
            OOE: OEOE_0897
            STH: STH1206 STH2731
            CAC: CAC2129(murE) CAC2819(murE)
            CPE: CPE1862(murE)
            CPF: CPF_1392 CPF_2116(murE)
            CPR: CPR_1830
            CTC: CTC01632(murE)
            CNO: NT01CX_1937
            CTH: Cthe_0978
            CDF: CD2664(murE)
            CBO: CBO1457(murE)
            CBA: CLB_1482(murE)
            CBH: CLC_1494(murE)
            CBF: CLI_1541(murE)
            CKL: CKL_1184(murE)
            CHY: CHY_2074(murE)
            DSY: DSY2912
            SWO: Swol_0821
            TTE: TTE1649(murE2)
            MTA: Moth_0838
            MTU: Rv2158c(murE)
            MTC: MT2217(murE)
            MBO: Mb2182c(murE)
            MBB: BCG_2175c(murE)
            MLE: ML0909(murE)
            MPA: MAP1902c(murE)
            MAV: MAV_2331
            MSM: MSMEG_4232
            MMC: Mmcs_3261
            CGL: NCgl2083(murE)
            CGB: cg2374(murE)
            CEF: CE2058(murE)
            CDI: DIP1603(murE)
            CJK: jk0745(murE)
            NFA: nfa17610(murE)
            RHA: RHA1_ro01093(murE1) RHA1_ro01268(murE2)
            SCO: SCO2089(murE)
            SMA: SAV6117(murE)
            TWH: TWT225(murE)
            TWS: TW545(murE)
            LXX: Lxx15310(murE)
            CMI: CMM_1864(murE)
            PAC: PPA0753
            TFU: Tfu_1105
            FRA: Francci3_1410
            FAL: FRAAL2191(murE)
            ACE: Acel_1005
            SEN: SACE_5856(murE)
            BLO: BL1356(murE)
            BAD: BAD_1085(murE)
            RXY: Rxyl_2305
            FNU: FN1225
            RBA: RB6114(murE)
            CTR: CT269(murE)
            CTA: CTA_0291(murE)
            CMU: TC0540
            CPN: CPn0418(murE)
            CPA: CP0336
            CPJ: CPj0418(murE)
            CPT: CpB0434
            CCA: CCA00376(murE)
            CAB: CAB363(murE)
            CFE: CF0632(murE)
            PCU: pc0314(murE)
            BGA: BG0200(murE)
            BAF: BAPKO_0204(murE)
            TPA: TP0933
            TDE: TDE0825
            LIL: LA2047(murE)
            LIC: LIC11867(murE)
            LBJ: LBJ_0479(murE)
            LBL: LBL_2600(murE)
            SYN: slr0528(murE)
            SYW: SYNW1690(murE)
            SYC: syc2470_c(murE)
            SYF: Synpcc7942_1484
            SYD: Syncc9605_0790(murE)
            SYE: Syncc9902_1587(murE)
            SYG: sync_0632
            SYR: SynRCC307_0624(murE)
            SYX: SynWH7803_0594(murE)
            CYA: CYA_0196(murE)
            CYB: CYB_1235(murE)
            TEL: tlr1239(murE)
            GVI: gll3492(murE)
            ANA: all1663
            AVA: Ava_1147(murE) Ava_1814
            PMA: Pro0412(murE)
            PMM: PMM0413(murE)
            PMT: PMT0230(murE)
            PMN: PMN2A_1747
            PMI: PMT9312_0408
            PMB: A9601_04631(murE)
            PMC: P9515_04741(murE)
            PMF: P9303_21131(murE)
            PMG: P9301_04321(murE)
            PMH: P9215_04891
            PME: NATL1_04641(murE)
            TER: Tery_4151
            BTH: BT_3452
            BFR: BF0310
            BFS: BF0258(murE)
            PGI: PG0576(murE)
            SRU: SRU_0556(murE)
            CHU: CHU_2745(murE)
            GFO: GFO_2772(murE)
            FPS: FP2061(murE)
            CTE: CT0039(murE)
            CCH: Cag_0050
            PLT: Plut_2115
            DRA: DR_0297
            DGE: Dgeo_0099
            TTH: TTC1904
            TTJ: TTHA0100
            AAE: aq_1747(murE)
            TMA: TM0237
            TPT: Tpet_0687
            MSI: Msm_1190
            MKA: MK0755(murC)
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.13
            ExPASy - ENZYME nomenclature database: 6.3.2.13
            ExplorEnz - The Enzyme Database: 6.3.2.13
            ERGO genome analysis and discovery system: 6.3.2.13
            BRENDA, the Enzyme Database: 6.3.2.13
            CAS: 9075-09-6
///
ENTRY       EC 6.3.2.14                 Enzyme
NAME        2,3-dihydroxybenzoate---serine ligase;
            N-(2,3-dihydroxybenzoyl)-serine synthetase;
            2,3-dihydroxybenzoylserine synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     2,3-dihydroxybenzoate:L-serine ligase
REACTION    ATP + 2,3-dihydroxybenzoate + L-serine = products of ATP breakdown +
            N-(2,3-dihydroxybenzoyl)-L-serine [RN:R07644]
ALL_REAC    R07644;
            (other) R01509 R01510
SUBSTRATE   ATP [CPD:C00002];
            2,3-dihydroxybenzoate [CPD:C00196];
            L-serine [CPD:C00065]
PRODUCT     products of ATP breakdown [CPD:C07305];
            N-(2,3-dihydroxybenzoyl)-L-serine [CPD:C04204]
REFERENCE   1  [PMID:4966114]
  AUTHORS   Brot N, Goodwin J.
  TITLE     Regulation of 2,3-dihydroxybenzoylserine synthetase by iron.
  JOURNAL   J. Biol. Chem. 243 (1968) 510-3.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.14
            ExPASy - ENZYME nomenclature database: 6.3.2.14
            ExplorEnz - The Enzyme Database: 6.3.2.14
            ERGO genome analysis and discovery system: 6.3.2.14
            BRENDA, the Enzyme Database: 6.3.2.14
            CAS: 37318-63-1
///
ENTRY       EC 6.3.2.15       Obsolete  Enzyme
NAME        Deleted entry
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
COMMENT     Deleted entry:
            UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D
            -alanine ligase. The activity observed is due to EC 6.3.2.10,
            UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (EC
            6.3.2.15 created 1976, deleted 2002)
STRUCTURES  PDB: 1GG4  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.15
            ExPASy - ENZYME nomenclature database: 6.3.2.15
            ExplorEnz - The Enzyme Database: 6.3.2.15
            ERGO genome analysis and discovery system: 6.3.2.15
            BRENDA, the Enzyme Database: 6.3.2.15
///
ENTRY       EC 6.3.2.16                 Enzyme
NAME        D-alanine---alanyl-poly(glycerolphosphate) ligase;
            D-alanyl-alanyl-poly(glycerolphosphate) synthetase;
            D-alanine:membrane-acceptor ligase;
            D-alanylalanylpoly(phosphoglycerol) synthetase;
            D-alanyl-poly(phosphoglycerol) synthetase;
            D-alanine-membrane acceptor-ligase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     D-alanine:alanyl-poly(glycerolphosphate) ligase (ADP-forming)
REACTION    ATP + D-alanine + alanyl-poly(glycerolphosphate) = ADP + phosphate +
            D-alanyl-alanyl-poly(glycerolphosphate) [RN:R04369]
ALL_REAC    R04369
SUBSTRATE   ATP [CPD:C00002];
            D-alanine [CPD:C00133];
            alanyl-poly(glycerolphosphate) [CPD:C03999]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            D-alanyl-alanyl-poly(glycerolphosphate) [CPD:C04457]
COMMENT     Involved in the synthesis of teichoic acids.
REFERENCE   1  [PMID:4399593]
  AUTHORS   Reusch VM Jr, Neuhaus FC.
  TITLE     D-Alanine: membrane acceptor ligase from Lactobacillus casei.
  JOURNAL   J. Biol. Chem. 246 (1971) 6136-43.
  ORGANISM  Lactobacillus casei [GN:lca]
PATHWAY     PATH: map00473  D-Alanine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.16
            ExPASy - ENZYME nomenclature database: 6.3.2.16
            ExplorEnz - The Enzyme Database: 6.3.2.16
            ERGO genome analysis and discovery system: 6.3.2.16
            BRENDA, the Enzyme Database: 6.3.2.16
            CAS: 9046-58-6
///
ENTRY       EC 6.3.2.17                 Enzyme
NAME        tetrahydrofolate synthase;
            folylpolyglutamate synthase;
            folate polyglutamate synthetase;
            formyltetrahydropteroyldiglutamate synthetase;
            N10-formyltetrahydropteroyldiglutamate synthetase;
            folylpoly-gamma-glutamate synthase;
            folylpolyglutamyl synthetase;
            folylpoly(gamma-glutamate) synthase;
            folylpolyglutamate synthetase;
            folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase;
            FPGS;
            tetrahydrofolylpolyglutamate synthase;
            tetrahydrofolate:L-glutamate gamma-ligase (ADP-forming);
            tetrahydropteroyl-[gamma-Glu]n:L-glutamate gamma-ligase
            (ADP-forming)
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     tetrahydropteroyl-gamma-polyglutamate:L-glutamate gamma-ligase
            (ADP-forming)
REACTION    ATP + tetrahydropteroyl-[gamma-Glu]n + L-glutamate = ADP + phosphate
            + tetrahydropteroyl-[gamma-Glu]n+1 [RN:R04241]
ALL_REAC    R04241 > R00942;
            (other) R01654 R02237 R05197
SUBSTRATE   ATP [CPD:C00002];
            tetrahydropteroyl-[gamma-Glu]n [CPD:C03541];
            L-glutamate [CPD:C00025]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            tetrahydropteroyl-[gamma-Glu]n+1 [CPD:C03541]
COMMENT     In some bacteria, a single protein catalyses both this activity and
            that of EC 6.3.2.12, dihydrofolate synthase [3], the combined
            activity of which leads to the formation of the coenzyme
            polyglutamated tetrahydropteroate (H4PteGlun), i.e. various
            tetrahydrofolates (H4folate). In contrast, the activities are
            located on separate proteins in most eukaryotes studied to date [4].
            In Arabidopsis thaliana, this enzyme is present as distinct isoforms
            in the mitochondria, the cytosol and the chloroplast. Each isoform
            is encoded by a separate gene, a situation that is unique among
            eukaryotes [4]. As the affinity of folate-dependent enzymes
            increases markedly with the number of glutamic residues, the
            tetrahydropteroyl polyglutamates are the preferred coenzymes of C1
            metabolism. (reviewed in [5]). The enzymes from different sources
            (particularly eukaryotes versus prokaryotes) have different
            substrate specificities with regard to one-carbon substituents and
            the number of glutamate residues present on the tetrahydrofolates.
REFERENCE   1  [PMID:6458762]
  AUTHORS   Cichowicz DJ, Foo SK, Shane B.
  TITLE     Folylpoly-gamma-glutamate synthesis by bacteria and mammalian cells.
  JOURNAL   Mol. Cell. Biochem. 39 (1981) 209-28.
  ORGANISM  pig [GN:ssc], Streptococcus faecalis, Lactobacillus casei [GN:lca],
            Corynebacterium sp., Neurospora crassa [GN:dncr]
REFERENCE   2  [PMID:7027025]
  AUTHORS   McGuire JJ, Bertino JR.
  TITLE     Enzymatic synthesis and function of folylpolyglutamates.
  JOURNAL   Mol. Cell. Biochem. 38 Spec No (1981) 19-48.
  ORGANISM  Neurospora crassa [GN:dncr]
REFERENCE   3  [PMID:2985605]
  AUTHORS   Bognar AL, Osborne C, Shane B, Singer SC, Ferone R.
  TITLE     Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase.
            Cloning and high expression of the Escherichia coli folC gene and
            purification and properties of the gene product.
  JOURNAL   J. Biol. Chem. 260 (1985) 5625-30.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   4  [PMID:11752472]
  AUTHORS   Ravanel S, Cherest H, Jabrin S, Grunwald D, Surdin-Kerjan Y, Douce
            R, Rebeille F.
  TITLE     Tetrahydrofolate biosynthesis in plants: molecular and functional
            characterization of dihydrofolate synthetase and three isoforms of
            folylpolyglutamate synthetase in Arabidopsis thaliana.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 15360-5.
  ORGANISM  Arabidopsis thaliana [GN:ath]
REFERENCE   5  [PMID:9190084]
  AUTHORS   Cossins EA, Chen L.
  TITLE     Folates and one-carbon metabolism in plants and fungi.
  JOURNAL   Phytochemistry. 45 (1997) 437-52.
  ORGANISM  Corynebacterium sp., Neurospora crassa [GN:dncr], Escherichia coli
            [GN:eco]
REFERENCE   6  [PMID:10799479]
  AUTHORS   Cherest H, Thomas D, Surdin-Kerjan Y.
  TITLE     Polyglutamylation of folate coenzymes is necessary for methionine
            biosynthesis and maintenance of intact mitochondrial genome in
            Saccharomyces cerevisiae.
  JOURNAL   J. Biol. Chem. 275 (2000) 14056-63.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
PATHWAY     PATH: map00790  Folate biosynthesis
ORTHOLOGY   KO: K01930  folylpolyglutamate synthase
GENES       HSA: 2356(FPGS)
            MMU: 14287(Fpgs)
            CFA: 609176(FPGS)
            DRE: 406746(fpgs)
            SPU: 592205(LOC592205)
            DME: Dmel_CG2543
            CEL: F25B5.6
            ATH: AT5G41480(GLA1)
            OSA: 4331360
            CME: CMQ033C
            SCE: YKL132C(RMA1) YMR113W(FOL3) YOR241W(MET7)
            AGO: AGOS_ACR134W AGOS_AEL310C
            PIC: PICST_47181(FOL3) PICST_71737
            CGR: CAGL0J03762g CAGL0K03553g
            SPO: SPAC227.09 SPBC1709.17
            ANI: AN3840.2 AN4384.2
            AFM: AFUA_4G06740 AFUA_4G08060 AFUA_6G09440 AFUA_8G04160
            AOR: AO090009000308 AO090023000763 AO090023000912
            CNE: CNC04840 CNH02620
            PFA: PF13_0140
            TAN: TA20775
            TPV: TP01_0440
            TET: TTHERM_01332110
            TBR: Tb10.6k15.3140
            TCR: 509715.70 510105.80
            LMA: LmjF36.2610
            ECO: b2315(folC)
            ECJ: JW2312(folC)
            ECE: Z3577(folC)
            ECS: ECs3199
            ECC: c2860(folC)
            ECI: UTI89_C2600(folC)
            ECP: ECP_2354
            ECV: APECO1_4249(folC)
            ECW: EcE24377A_2609(folC)
            ECX: EcHS_A2466(folC)
            STY: STY2596(folC)
            STT: t0499(folC)
            SPT: SPA0499(folC)
            SEC: SC2367(folC)
            STM: STM2365(folC)
            YPE: YPO2769(folC)
            YPK: y1602(folC)
            YPM: YP_2395(folC)
            YPA: YPA_2075
            YPN: YPN_2178
            YPS: YPTB2615(folC)
            YPI: YpsIP31758_1423(folC)
            YEN: YE1312(dedC)
            SFL: SF2391(folC)
            SFX: S2526(folC)
            SFV: SFV_2384(folC)
            SSN: SSON_2373(folC)
            SBO: SBO_2352(folC)
            SDY: SDY_2514(folC)
            ECA: ECA3055(folC)
            PLU: plu3170(folC)
            BUC: BU167(folC)
            BAS: BUsg161(folC)
            BAB: bbp157(folC)
            WBR: WGLp311(folC)
            SGL: SG1616
            ENT: Ent638_2864
            BFL: Bfl494(folC)
            BPN: BPEN_510(folC)
            HIN: HI1261(folC)
            HIT: NTHI1903(folC)
            HDU: HD1465(folC)
            HSO: HS_0880(folC)
            PMU: PM0635(folC)
            MSU: MS1173(folC)
            APL: APL_0632(folC)
            XFA: XF1946
            XFT: PD0854(folC)
            XCC: XCC0950(folC)
            XCB: XC_3285
            XCV: XCV1058(folC)
            XAC: XAC1029(folC)
            XOO: XOO3679(folC)
            XOM: XOO_3475(XOO3475)
            VCH: VC1001
            VVU: VV1_1994
            VVY: VV2422
            VPA: VP2188
            VFI: VF1694
            PPR: PBPRA2651
            PAE: PA3111(folC)
            PAU: PA14_23880(folC)
            PPU: PP_1997(folC)
            PST: PSPTO_3814(folC)
            PSB: Psyr_1665
            PSP: PSPPH_1659(folC)
            PFL: PFL_2074(folC)
            PFO: Pfl_1899
            PEN: PSEEN1692(folC)
            PMY: Pmen_2714
            PAR: Psyc_0435(folC)
            PCR: Pcryo_0470
            ACI: ACIAD0644(folC)
            SON: SO_3067(folC)
            SDN: Sden_1487
            SFR: Sfri_1396
            SAZ: Sama_2149
            SLO: Shew_2305
            SHE: Shewmr4_1427
            SHN: Shewana3_1480
            ILO: IL1015(folC)
            CPS: CPS_3801(folC)
            PHA: PSHAa2073(folC)
            PAT: Patl_1606
            PIN: Ping_1968
            MAQ: Maqu_1555
            CBU: CBU_0894(folC)
            LPN: lpg1342(folC)
            LPF: lpl1295(folC)
            LPP: lpp1296(folC)
            MCA: MCA2492(folC)
            FTU: FTT0371c(folC)
            FTF: FTF0371c(folC)
            FTW: FTW_1705(folC)
            FTL: FTL_1308
            FTH: FTH_1280(folC)
            FTN: FTN_0273(folC)
            TCX: Tcr_0806
            NOC: Noc_1023
            AEH: Mlg_1239
            HCH: HCH_02439(folC)
            ABO: ABO_1458(folC)
            AHA: AHA_2678(folC)
            DNO: DNO_0404(folC)
            BCI: BCI_0366(folC)
            RMA: Rmag_0999
            VOK: COSY_0895(folC)
            NME: NMB0693
            NMA: NMA0896(folC)
            NMC: NMC0644(folC)
            NGO: NGO0266
            CVI: CV_2518(folC)
            RSO: RSc1979(folC)
            REH: H16_A2610(folC)
            RME: Rmet_2463
            BMA: BMAA1717(folC)
            BMV: BMASAVP1_1653(folC)
            BML: BMA10299_1862(folC)
            BMN: BMA10247_A0533(folC)
            BXE: Bxe_B2877
            BVI: Bcep1808_4466
            BUR: Bcep18194_B2121
            BCN: Bcen_4405
            BCH: Bcen2424_3962
            BAM: Bamb_3352
            BPS: BPSS1695(folC)
            BPM: BURPS1710b_A0765(folC)
            BPL: BURPS1106A_A2303(folC)
            BPD: BURPS668_A2441(folC)
            BTE: BTH_II0683
            PNU: Pnuc_0775
            BPE: BP1412(folC)
            BPA: BPP1519(folC)
            BBR: BB2597(folC)
            RFR: Rfer_2686
            POL: Bpro_1604
            PNA: Pnap_1089
            AAV: Aave_1860
            MPT: Mpe_A3265
            MMS: mma_2161(folC)
            NEU: NE0696(folC)
            NET: Neut_1155
            NMU: Nmul_A1909
            EBA: ebA4777(folC)
            DAR: Daro_0873
            TBD: Tbd_1911
            MFA: Mfla_1695
            HPY: HP1545(folC)
            HPJ: jhp1454(folC)
            HPA: HPAG1_1494
            HHE: HH0462(folC)
            HAC: Hac_0295(folC)
            WSU: WS1242(folC)
            TDN: Tmden_1569
            CJE: Cj1088c(folC)
            CJR: CJE1231(folC)
            CJU: C8J_1029(folC)
            CFF: CFF8240_0734(folC)
            ABU: Abu_0404(folC)
            NIS: NIS_1462(folC)
            SUN: SUN_2042(folC)
            GSU: GSU2368(folC)
            GME: Gmet_2475
            PCA: Pcar_0738
            DVU: DVU2882(folC)
            DVL: Dvul_0483
            DDE: Dde_3058
            LIP: LI0131(folC)
            DPS: DP2878
            MXA: MXAN_2705(folC)
            SAT: SYN_01606
            SFU: Sfum_1671
            RPR: RP536(folC)
            RTY: RT0524(folC)
            RCO: RC0779(folC)
            RFE: RF_0740(folC)
            RBE: RBE_1202(folC)
            RCM: A1E_02820
            OTS: OTBS_0584(folC)
            WOL: WD1052(folC)
            AMA: AM699(folC)
            APH: APH_0747(folC)
            ERU: Erum3680(folC)
            ERW: ERWE_CDS_03790(folC)
            ERG: ERGA_CDS_03740(folC)
            ECN: Ecaj_0353
            ECH: ECH_0702(folC)
            NSE: NSE_0715(folC)
            PUB: SAR11_0485(folC)
            MLO: mlr5076(folC)
            MES: Meso_0662
            PLA: Plav_0140
            SME: SMc02763(folC)
            ATU: Atu0021(folC)
            ATC: AGR_C_35(folC)
            RET: RHE_CH00024(folC)
            RLE: RL0024(folC)
            BME: BMEI2021
            BMF: BAB1_2108(folC)
            BMS: BR2106(folC)
            BMB: BruAb1_2081(folC)
            OAN: Oant_0814
            BJA: blr0748(folC)
            BRA: BRADO0088
            BBT: BBta_0094
            RPA: RPA0072(folC)
            RPB: RPB_0564 RPB_0632
            RPC: RPC_0389
            RPD: RPD_0200
            RPE: RPE_0113 RPE_0457
            NWI: Nwi_0052
            NHA: Nham_0060
            BHE: BH00330(folC)
            BQU: BQ00310(folC)
            BBK: BARBAKC583_1352(folC)
            XAU: Xaut_1697
            CCR: CC_3541(folC)
            SIL: SPO3818(folC)
            SIT: TM1040_2675
            RSP: RSP_0930(folC)
            RSQ: Rsph17025_2985
            JAN: Jann_0059
            RDE: RD1_0327(folC)
            PDE: Pden_1988
            MMR: Mmar10_0088
            ZMO: ZMO0582(folC)
            NAR: Saro_1299
            SAL: Sala_1061
            SWI: Swit_2729
            GOX: GOX1205
            GBE: GbCGDNIH1_2012
            ACR: Acry_0844
            RRU: Rru_A3431
            MAG: amb4014
            MGM: Mmc1_2329
            ABA: Acid345_0119
            BSU: BG10322(folC)
            BHA: BH3037(folC)
            BAN: BA4689(folC)
            BAR: GBAA4689(folC)
            BAA: BA_5128
            BAT: BAS4354
            BCE: BC4464
            BCA: BCE_4548(folC)
            BCZ: BCZK4201(folC)
            BTK: BT9727_4190(folC)
            BTL: BALH_4050(folC)
            BLI: BL00632(folC)
            BLD: BLi02937(folC)
            BCL: ABC2620(folC)
            BAY: RBAM_025130(folC)
            BPU: BPUM_2448(folC)
            OIH: OB2058(folC)
            GKA: GK2637
            SAU: SA1487(folC)
            SAV: SAV1662(folC)
            SAM: MW1606(folC)
            SAR: SAR1742(folC)
            SAS: SAS1591
            SAC: SACOL1709(folC)
            SAB: SAB1523c(folC)
            SAA: SAUSA300_1610(folC)
            SAO: SAOUHSC_01766
            SEP: SE1338
            SER: SERP1227(folC)
            SHA: SH1264(folC)
            SSP: SSP1102
            LMO: lmo1551(folC)
            LMF: LMOf2365_1572(folC)
            LIN: lin1586(folC)
            LWE: lwe1564(folC)
            LLA: L0177(folC)
            LLC: LACR_1278
            LLM: llmg_1334(folC)
            SPY: SPy_0814(folC.2) SPy_1096(folC.1)
            SPZ: M5005_Spy_0628(folC.2) M5005_Spy_0820(folC.1)
            SPM: spyM18_0876(folC) spyM18_1058(folC)
            SPG: SpyM3_0547(folC.2) SpyM3_0758(folC.1)
            SPS: SPs0958 SPs1307
            SPH: MGAS10270_Spy0684(folC2) MGAS10270_Spy0936(folC1)
            SPI: MGAS10750_Spy0716(folC2) MGAS10750_Spy0971(folC1)
            SPJ: MGAS2096_Spy0693(folC2) MGAS2096_Spy0894(folC1)
            SPK: MGAS9429_Spy0683(folC2) MGAS9429_Spy0939(folC1)
            SPF: SpyM50968(folC1) SpyM51179(folC2)
            SPA: M6_Spy0645 M6_Spy0818
            SPB: M28_Spy0608(folC.2) M28_Spy0797(folC.1)
            SAG: SAG1117(folC)
            SAN: gbs1184
            SAK: SAK_1202(folC)
            SMU: SMU.839(fol) SMU.967(folC)
            STC: str0409(folC1) str1546(folC2)
            STL: stu0409(folC1) stu1546(folC2)
            SSA: SSA_0198 SSA_2237
            LPL: lp_2321(folC1) lp_3296(folC2)
            LJO: LJ0959
            LAC: LBA0795(folC)
            LSA: LSA0850(folC1) LSA1099(folC2)
            LSL: LSL_1071(folC)
            LDB: Ldb0248(folC2) Ldb0728(folC1)
            LBU: LBUL_0210 LBUL_0660
            LBR: LVIS_1252
            LCA: LSEI_1252
            EFA: EF2928(folC)
            OOE: OEOE_1391
            STH: STH367
            CAC: CAC2398(folC)
            CPE: CPE1918(folC)
            CPF: CPF_2174(folC)
            CPR: CPR_1885(folC)
            CTC: CTC02301
            CNO: NT01CX_1729
            CDF: CD3253(folC)
            CBO: CBO3163(folC)
            CBA: CLB_3198(folC)
            CBH: CLC_3072(folC)
            CBF: CLI_3227(folC)
            CKL: CKL_3218(folC)
            CHY: CHY_0335(folC)
            DSY: DSY3187
            SWO: Swol_1648
            TTE: TTE0783(folC)
            MTA: Moth_0533
            MMY: MSC_0942(folC)
            MCP: MCAP_0775(folC)
            POY: PAM007(folC)
            MFL: Mfl060
            MTU: Rv2447c(folC)
            MTC: MT2523(folC)
            MBO: Mb2474c(folC)
            MBB: BCG_2467c(folC)
            MLE: ML1471(folC)
            MPA: MAP2270c(folC)
            CGL: NCgl2292(cgl2375)
            CGB: cg2608(folC)
            CEF: CE2281
            CDI: DIP1785
            CJK: jk0551(folC)
            NFA: nfa13490(folC)
            RHA: RHA1_ro01317
            SCO: SCO2614(fpgS)
            SMA: SAV5452(fpgS)
            TWH: TWT476(folC)
            TWS: TW288(fgs)
            LXX: Lxx07980(folC)
            PAC: PPA0821
            TFU: Tfu_2190
            FRA: Francci3_1208 Francci3_1209
            FAL: FRAAL1913(folC) FRAAL1914
            ACE: Acel_0742
            SEN: SACE_1387(folC)
            BLO: BL1353(folC)
            BAD: BAD_1088(folC)
            RXY: Rxyl_1534
            FNU: FN1014
            RBA: RB6237(folC)
            PCU: pc1626(folC)
            TPA: TP0340
            TDE: TDE1084
            LIL: LA0637(folC)
            LIC: LIC12950(folC)
            LBJ: LBJ_2330(folC)
            LBL: LBL_0778(folC)
            SYN: sll1612(folC)
            SYW: SYNW1635(folC)
            SYC: syc0598_c(folC)
            SYF: Synpcc7942_0944
            SYD: Syncc9605_0857
            SYE: Syncc9902_1535
            SYR: SynRCC307_0610(folC)
            SYX: SynWH7803_1748(folC)
            CYA: CYA_1353(folC)
            CYB: CYB_1382(folC)
            TEL: tlr0190(folC)
            GVI: glr1074(folC)
            ANA: alr1026
            AVA: Ava_3683
            PMA: Pro1376(folC)
            PMM: PMM1302(folC)
            PMT: PMT0330(folC)
            PMN: PMN2A_0868
            PMI: PMT9312_1398
            PMB: A9601_15011(folC)
            PMC: P9515_14631(folC)
            PMF: P9303_19851(folC)
            PMG: P9301_14881(folC)
            PMH: P9215_15311(folC)
            PME: NATL1_17221(folC)
            TER: Tery_1603
            BTH: BT_1335
            BFR: BF2974
            BFS: BF2850
            PGI: PG0463(folC)
            SRU: SRU_2420
            CHU: CHU_1542(folC)
            GFO: GFO_2899(folC)
            FPS: FP0541(folC)
            CTE: CT0263(folC)
            CCH: Cag_0458
            PVI: Cvib_1538
            PLT: Plut_1757
            DET: DET0016
            DEH: cbdb_A18(folC)
            DRA: DR_0340 DR_2575(folC)
            DGE: Dgeo_0083 Dgeo_0333
            TTH: TTC0975 TTC1640
            TTJ: TTHA0343 TTHA1340
            AAE: aq_2045(folC)
            TMA: TM0166
            TME: Tmel_1568
            FNO: Fnod_0344
            HAL: VNG0412G(folP)
            HWA: HQ1767A(folCP)
            NPH: NP1478A(folCP)
            TAC: Ta0637
            TVO: TVN0757
            PTO: PTO1256
STRUCTURES  PDB: 1FGS  1JBV  1JBW  2GC5  2GC6  2GCA  2GCB  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.17
            ExPASy - ENZYME nomenclature database: 6.3.2.17
            ExplorEnz - The Enzyme Database: 6.3.2.17
            ERGO genome analysis and discovery system: 6.3.2.17
            BRENDA, the Enzyme Database: 6.3.2.17
            CAS: 63363-84-8
///
ENTRY       EC 6.3.2.18                 Enzyme
NAME        gamma-glutamylhistamine synthase;
            gamma-glutaminylhistamine synthetase;
            gamma-GHA synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     L-glutamate:histamine ligase
REACTION    ATP + L-glutamate + histamine = products of ATP breakdown +
            Nalpha-gamma-L-glutamylhistamine [RN:R07643]
ALL_REAC    R07643;
            (other) R02153 R02154
SUBSTRATE   ATP [CPD:C00002];
            L-glutamate [CPD:C00025];
            histamine [CPD:C00388]
PRODUCT     products of ATP breakdown [CPD:C07305];
            Nalpha-gamma-L-glutamylhistamine
REFERENCE   1  [PMID:6125565]
  AUTHORS   Stein C, Weinreich D.
  TITLE     An in vitro characterization of gamma-glutamylhistamine synthetase:
            a novel enzyme catalyzing histamine metabolism in the central
            nervous system of the marine mollusk, Aplysia californica.
  JOURNAL   J. Neurochem. 38 (1982) 204-14.
  ORGANISM  Aplysia californica
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.18
            ExPASy - ENZYME nomenclature database: 6.3.2.18
            ExplorEnz - The Enzyme Database: 6.3.2.18
            ERGO genome analysis and discovery system: 6.3.2.18
            BRENDA, the Enzyme Database: 6.3.2.18
            CAS: 82904-08-3
///
ENTRY       EC 6.3.2.19                 Enzyme
NAME        ubiquitin---protein ligase;
            ubiquitin-activating enzyme
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     ubiquitin:protein-lysine N-ligase (AMP-forming)
REACTION    ATP + ubiquitin + protein lysine = AMP + diphosphate + protein
            N-ubiquityllysine [RN:R03876]
ALL_REAC    R03876
SUBSTRATE   ATP [CPD:C00002];
            ubiquitin [CPD:C00496];
            protein lysine [CPD:C02188]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            protein N-ubiquityllysine [CPD:C03635]
COMMENT     Ubiquitin is coupled to protein by a peptide bond between the
            C-terminal glycine of ubiquitin and epsilon-amino groups of lysine
            residues in the protein. An intermediate in the reaction contains
            one ubiquitin residue bound as a thioester to the enzyme, and a
            residue of ubiquitin adenylate non-covalently bound to the enzyme.
REFERENCE   1  [PMID:6277904]
  AUTHORS   Ciechanover A, Elias S, Heller H, Hershko A.
  TITLE     "Covalent affinity" purification of ubiquitin-activating enzyme.
  JOURNAL   J. Biol. Chem. 257 (1982) 2537-42.
  ORGANISM  rabbit, human [GN:hsa]
REFERENCE   2  [PMID:6286650]
  AUTHORS   Haas AL, Rose IA.
  TITLE     The mechanism of ubiquitin activating enzyme. A kinetic and
            equilibrium analysis.
  JOURNAL   J. Biol. Chem. 257 (1982) 10329-37.
REFERENCE   3  [PMID:6277905]
  AUTHORS   Haas AL, Warms JV, Hershko A, Rose IA.
  TITLE     Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin
            conjugation.
  JOURNAL   J. Biol. Chem. 257 (1982) 2543-8.
  ORGANISM  rabbit
REFERENCE   4  [PMID:3017957]
  AUTHORS   Hershko A, Heller H, Eytan E, Reiss Y.
  TITLE     The protein substrate binding site of the ubiquitin-protein ligase
            system.
  JOURNAL   J. Biol. Chem. 261 (1986) 11992-9.
  ORGANISM  rabbit
PATHWAY     PATH: map04120  Ubiquitin mediated proteolysis
            PATH: map05020  Parkinson's disease
            PATH: map05040  Huntington's disease
ORTHOLOGY   KO: K01931  
            KO: K02207  ubiquitin-conjugating enzyme E2
            KO: K03178  ubiquitin-activating enzyme E1
            KO: K04552  ubiquitin-conjugating enzyme E2L 3
            KO: K04553  ubiquitin-conjugating enzyme E2L 6
            KO: K04554  ubiquitin-conjugating enzyme E2, J2
            KO: K04555  ubiquitin-conjugating enzyme E2G 2
            KO: K04649  ubiquitin-conjugating enzyme (huntingtin interacting
                        protein 2)
            KO: K06688  ubiquitin-conjugating enzyme E2C
            KO: K06689  ubiquitin-conjugating enzyme UBE2D/E
GENES       HSA: 10477(UBE2E3) 11065(UBE2C) 118424(UBE2J2) 148581(UBE2U)
                 27338(UBE2S) 3093(HIP2) 389898(UBE2NL) 4899(NRF1)
                 51465(UBE2J1) 51619(UBE2D4) 54926(UBE2R2) 7317(UBE1)
                 7319(UBE2A) 7320(UBE2B) 7321(UBE2D1) 7322(UBE2D2) 7323(UBE2D3)
                 7324(UBE2E1) 7325(UBE2E2) 7326(UBE2G1) 7327(UBE2G2)
                 7328(UBE2H) 7329(UBE2I) 7332(UBE2L3) 7334(UBE2N) 9040(UBE2M)
                 9246(UBE2L6) 997(CDC34)
            PTR: 452125(UBE2N) 459792(UBE2E3) 462065(UBE2B) 462108(UBE2D2)
                 462883(UBE2J1) 465601(LOC465601) 466588(UBE2L6) 474042(UBE2G2)
            MMU: 109161(Ube2q2) 140499(Ube2j2) 216080(Ube2d1) 216150(Cdc34)
                 218793(Ube2e2) 22192(Ube2m) 22193(Ube2e3) 22194(Ube2e1)
                 22195(Ube2l3) 22196(Ube2i) 22201(Ube1x) 22202(Ube1y1)
                 22209(Ube2a) 22210(Ube2b) 22213(Ube2g2) 22214(Ube2h)
                 23802(Amfr) 381534(Ube2u) 53323(Hip2) 56228(Ube2j1)
                 56550(Ube2d2) 56791(Ube2l6) 66105(Ube2d3) 66799(Ube2w)
                 67128(Ube2g1) 67615(Ube2r2) 68612(Ube2c) 77891(Ube2s)
                 93765(Ube2n)
            RNO: 116725(Ube2n) 25573(Ube2i) 295686(Ube2e3_predicted)
                 295704(Ube2l6) 298689(MGC94113) 314432(LOC314432)
                 361013(Ube2e2) 361831(Ube2d1_predicted)
                 363836(Ube2l3_predicted) 64631(Ube2g1) 79435(RGD69425)
                 81816(Ube2b) 81920(Ube2d3)
            CFA: 403671(UBE2S) 474993(UBE2J1) 475563(LOC475563) 475967(UBE2L6)
                 476560(UBE1C) 477048(UBE2E1) 477572(UBE2L3) 480896(UBE1)
                 481325(LOC481325) 484221(UBE2M) 485477(UBE2E2) 485898(UBE2C)
                 491332(UBE2I) 492095(UBE2A) 606935(UBE2J2) 607753(LOC607753)
                 607816(UBE2H) 607817(LOC607817) 608578(UBE2D1) 609136(UBE2N)
                 609531(HIP2) 609932(UBE2U) 610206(UBE2NL) 611581(UBE2G2)
                 611799(UBE2R2) 611865(LOC611865) 612742(UBE2D2) 612823(UBE2E3)
            BTA: 281225(HIP2) 326583(UBE2D3) 534349(UBE2E3)
            GGA: 374123(UBE2I) 395178(UBE1L) 395528(UBE2J1) 395672(UBE2A)
                 415356(UBE2Q2) 416137(UBE2D2) 416678(RCJMB04_5p24)
                 416769(UBE2L3) 417898(RCJMB04_3o20) 419421(UBE2J2)
                 420653(UBE2E1) 422713(RCJMB04_7i20) 423641(UBE2D1)
                 424122(UBE2E3) 424837(UBE2G2) 425483(CDC34) 426073(UBE1C)
                 427021(RCJMB04_34a5) 427134(LOC427134) 428787(RCJMB04_25e17)
                 776043(UBE2E2)
            XLA: 379298(MGC53533) 379982(hip2) 380226(ube2r2) 380288(ube2h)
                 380450(ube2i) 380500(ube2g1) 380524(ube2n) 398788(MGC68540)
                 403384(Xubc4) 443745(MGC78891) 444775(MGC81948)
                 446231(LOC446231) 446340(ube2d2) 446360(MGC82328)
                 446800(MGC80512) 494590(Ube2e2) 494592(LOC494592)
                 494742(LOC494742) 494805(LOC494805) 495424(LOC495424)
                 496302(LOC496302)
            XTR: 394553(MGC75750) 394629(ube2e1) 394648(ube2g1) 394925(ube2e3)
                 395006(ube2n) 448013(MGC69351) 448153(hip2) 448176(ube2a)
                 448270(ube2h) 448706(ube2b) 496585(ube2j1)
            DRE: 114445(ube2i2) 30622(ube2i) 321689(ube2e3) 324015(ube2d1)
                 334133(ube2g2) 335444(ube2d2) 368425(ube2h) 368430(ube2a)
                 393313(ube2nl) 393934(zgc:55886) 406335(ube1)
                 406794(zgc:63554) 406807(ube2n) 406851(ube2g1)
                 445100(zgc:92467) 553013(si:ch211-193n21.4) 64604(nrf1)
            SPU: 373404(LOC373404) 578542(LOC578542) 585095(LOC585095)
                 585461(LOC585461) 585800(LOC585800) 586388(LOC586388)
                 586593(LOC586593) 589147(LOC589147) 590010(LOC590010)
                 590611(LOC590611) 590901(LOC590901) 590968(LOC590968)
                 591316(LOC591316) 592882(LOC592882) 754943(LOC754943)
            DME: Dmel_CG10536(cbx) Dmel_CG10640(Uev1A) Dmel_CG10682(vih)
                 Dmel_CG10862 Dmel_CG11988(neur) Dmel_CG12227(skpF)
                 Dmel_CG12284(th) Dmel_CG12799(Ubc84D) Dmel_CG14472(poe)
                 Dmel_CG15104(Topors) Dmel_CG15437(morgue) Dmel_CG16894
                 Dmel_CG16988(Roc1b) Dmel_CG1782(Uba1) Dmel_CG18319(ben)
                 Dmel_CG2013(UbcD6) Dmel_CG2257 Dmel_CG3018(lwr)
                 Dmel_CG32592(hiw) Dmel_CG3473 Dmel_CG4005(yki)
                 Dmel_CG4244(Su(dx)) Dmel_CG4443(crl) Dmel_CG4502
                 Dmel_CG4943(lack) Dmel_CG5203 Dmel_CG5440 Dmel_CG5519(Gbp)
                 Dmel_CG5659(ari-1) Dmel_CG5709(ari-2) Dmel_CG5788(UbcD10)
                 Dmel_CG5823 Dmel_CG5841(mib1) Dmel_CG6303(Bruce)
                 Dmel_CG6720(UbcD2) Dmel_CG7375 Dmel_CG7425(eff)
                 Dmel_CG7555(Nedd4) Dmel_CG8284(UbcD4) Dmel_CG8711(cul-4)
                 Dmel_CG8998(Roc2) Dmel_CG9484(hyd) Dmel_CG9602
                 Dmel_CG9712(TSG101)
            CEL: C06E2.3(ubc-21) C06E2.7(ubc-22) C28G1.1(ubc-23)
                 C35B1.1(ubc-1) C47E12.5(uba-1) D1022.1(ubc-6) F25H2.8(ubc-25)
                 F26H9.7(uev-3) F29B9.6(ubc-9) F39B2.2(uev-1) F40G9.3(ubc-20)
                 F49E12.4(ubc-24) F52C6.12 F56D2.4(uev-2) F58A4.10(ubc-7)
                 M7.1(let-70) R01H2.6(ubc-18) R09B3.4(ubc-12)
                 Y110A2AM.3(ubc-26) Y110A2AR.2(ubc-15) Y54E5B.4(ubc-16)
                 Y54G2A.31(ubc-13) Y69H2.6(ubc-19) Y71G12B.15(ubc-3)
                 Y87G2A.9(ubc-14) Y94H6A.6(ubc-8)
            ATH: AT1G16890(UBC36) AT1G36340(UBC31) AT1G45050(ATUBC2-1)
                 AT1G50490(UBC20) AT1G63800(UBC5) AT1G64230(UBC28)
                 AT1G75440(UBC16) AT2G16740(UBC29) AT2G30110(ATUBA1) AT2G32790
                 AT2G46030(UBC6) AT3G08690(UBC11) AT3G08700(UBC12)
                 AT3G20060(UBC19) AT3G46460(UBC13) AT3G55380(UBC14)
                 AT3G57870(AHUS5) AT5G05080(UBC22) AT5G25760(PEX4)
                 AT5G41340(UBC4) AT5G42990(UBC18) AT5G50870(UBC27)
                 AT5G59300(UBC7) AT5G62540(UBC3)
            OSA: 4325169 4325174 4325905 4327162 4327237 4327386 4330074
                 4331446 4332529 4333728 4334386 4337331 4339013 4340379
                 4341740 4342488 4343707 4348755 4349557
            CME: CMB015C CMD152C CMG003C CMG136C CMH227C CMI034C CMK193C
                 CMK253C CMP181C CMR010C CMS304C CMS503C
            SCE: YBR082C(UBC4) YDL064W(UBC9) YDR054C(CDC34) YDR059C(UBC5)
                 YDR092W(UBC13) YDR177W(UBC1) YEL012W(UBC8) YER100W(UBC6)
                 YGL058W(RAD6) YGR133W(PEX4) YKL210W(UBA1) YLR306W(UBC12)
                 YMR022W(UBC7) YOR339C(UBC11)
            AGO: AGOS_AAR156C AGOS_ABR059W AGOS_ADL035C AGOS_ADR169C
                 AGOS_AEL045W AGOS_AER056C AGOS_AER173C AGOS_AFR314W
                 AGOS_AFR433C AGOS_AGL203C AGOS_AGR121C AGOS_AGR372W
            PIC: PICST_30911 PICST_35186 PICST_36882 PICST_40340 PICST_46734
                 PICST_57900 PICST_68363 PICST_69865 PICST_71285 PICST_80064
                 PICST_84844 PICST_85060 PICST_87984(UBA2)
            CAL: CaO19.1085(ubc1) CaO19.3628 CaO19_3237(CaO19.3237)
                 CaO19_7329(CaO19.7329) CaO19_7347(CaO19.7347)
                 CaO19_7438(CaO19.7438)
            CGR: CAGL0D00814g CAGL0D06468g CAGL0E00671g CAGL0E04598g
                 CAGL0E04752g CAGL0G07733g CAGL0G08063g CAGL0H03157g
                 CAGL0I00352g CAGL0I05478g CAGL0I10450g CAGL0K00319g
                 CAGL0M03399g CAGL0M07568g
            SPO: SPAC10F6.05c SPAC11E3.04c SPAC1250.03 SPAC18B11.07c(rhp6)
                 SPAC30D11.13(hus5) SPBC1105.09 SPBC119.02(ubc4)
                 SPBC1198.09(ubc16) SPBC211.07c SPBC2D10.20 SPBP16F5.04(ubcp3)
                 SPCC1259.15c(ubcp4)
            ANI: AN0226.2 AN1761.2 AN2174.2 AN2212.2 AN2761.2 AN4399.2
                 AN5344.2 AN5351.2 AN5495.2 AN7338.2
            AFM: AFUA_1G11410 AFUA_1G15570 AFUA_2G01130 AFUA_2G11100
                 AFUA_2G13690 AFUA_2G15040 AFUA_2G15760 AFUA_2G16470
                 AFUA_3G06030 AFUA_3G12850 AFUA_3G13060 AFUA_3G14430
                 AFUA_4G04612 AFUA_4G06830 AFUA_4G12080 AFUA_4G13940
                 AFUA_5G04060 AFUA_5G07040 AFUA_5G09200 AFUA_6G02420
                 AFUA_6G08880 AFUA_6G09160 AFUA_6G13170 AFUA_6G14130
                 AFUA_6G14210
            AOR: AO090001000592 AO090003000442 AO090012000248 AO090020000073
                 AO090020000516 AO090023000897 AO090102000209 AO090102000609
                 AO090103000399 AO090103000407 AO090120000129 AO090701000280
                 AO090701000381 AO090701000588
            CNE: CNA01230 CNA08010 CNC05160 CND04010 CNE03030 CNE03880
                 CNF02130 CNF02760 CNF04270 CNI02210 CNJ00500 CNJ01020
            UMA: UM00339.1 UM00525.1 UM00982.1 UM01940.1 UM02426.1 UM03686.1
                 UM04542.1 UM04569.1 UM05955.1 UM06101.1 UM06188.1
            ECU: ECU03_0930 ECU04_0630 ECU08_0860 ECU10_0940 ECU10_1310i
                 ECU11_1990
            DDI: DDBDRAFT_0167874 DDBDRAFT_0168503 DDBDRAFT_0169154
                 DDBDRAFT_0187308 DDBDRAFT_0188215 DDBDRAFT_0188947
                 DDBDRAFT_0202520 DDBDRAFT_0204236 DDBDRAFT_0204633
                 DDBDRAFT_0206182 DDBDRAFT_0206370 DDBDRAFT_0206533
                 DDBDRAFT_0218542 DDBDRAFT_0218828 DDB_0191440(ubc9)
                 DDB_0220497(UAE1)
            PFA: MAL3P6.28 MAL3P6.32 MAL8P1.23 PF08_0085 PF10_0330 PF13_0301
                 PFE1350c PFI0740c PFI1030c PFL0190w PFL1245w PFL2175w
            CPV: cgd1_410 cgd3_2670 cgd4_210 cgd4_2300 cgd4_570 cgd6_4180
            CHO: Chro.10052 Chro.30149 Chro.30262 Chro.40035 Chro.40073
                 Chro.40260 Chro.60479 Chro.80032
            TAN: TA03980 TA04605 TA05120 TA05740 TA05945 TA06755 TA10565
                 TA10690 TA11640 TA12340 TA14305 TA14590 TA20510
            TPV: TP01_0508 TP01_0732 TP01_0804 TP02_0161 TP02_0288 TP02_0689
                 TP03_0448 TP03_0540
            TET: TTHERM_00011330 TTHERM_00185350 TTHERM_00285290
                 TTHERM_00419810 TTHERM_00450870 TTHERM_00456960
                 TTHERM_00531900 TTHERM_00532840 TTHERM_00550720
                 TTHERM_00628690 TTHERM_00931940 TTHERM_00997780
                 TTHERM_01027520 TTHERM_01053020 TTHERM_01082920
                 TTHERM_01082930 TTHERM_01082940 TTHERM_01082960
                 TTHERM_01123950 TTHERM_01341620
            TBR: Tb09.211.0050 Tb11.01.5510 Tb11.01.5790 Tb927.2.2460
                 Tb927.2.3720 Tb927.4.2710 Tb927.4.3190 Tb927.4.3460
                 Tb927.5.1000 Tb927.7.2540 Tb927.8.2640 Tb927.8.6090
                 Tb927.8.6510 Tb927.8.920
            TCR: 453445.20 503515.14 504055.81 504427.250 504643.30 506859.10
                 508043.30 508137.30 508303.4 508569.20 509607.10 511071.70
                 511111.50 511179.160 511727.40 511813.20 511903.30 511907.270
            LMA: LmjF02.0390 LmjF04.0680 LmjF07.0850 LmjF22.0610 LmjF23.0550
                 LmjF24.1710 LmjF24.2130 LmjF32.0700 LmjF32.0960 LmjF33.2770
                 LmjF34.0900 LmjF35.1300
            EHI: 107.t00018 108.t00020 142.t00021 142.t00027 22.t00035
                 22.t00037 327.t00012 334.t00009 361.t00007 408.t00002
                 42.t00021 472.t00011 484.t00005 49.t00025 51.t00013 54.t00036
                 54.t00051 7.t00027 98.t00007
            HPA: HPAG1_0740
            PMF: P9303_22891(thiF)
            PME: NATL1_20151(thiF)
STRUCTURES  PDB: 1A3S  1AYZ  1C4Z  1FBV  1FXT  1FZY  1I7K  1IYF  1J7D  1JAS  
                 1JAT  1JBB  1KPS  1PZV  1Q34  1QCQ  1TTE  1U9A  1U9B  1UMH  
                 1UMI  1UR6  1W4U  1WD2  1WZV  1WZW  1X23  1XR9  1Y6L  1Y8X  
                 1YLA  1YRV  1Z2U  1Z3D  1Z5S  1Z6U  1ZDN  1ZUO  2A4D  2A7L  
                 2AAK  2AWF  2AYV  2BEP  2BF8  2C4O  2C4P  2CLW  2CYX  2E2C  
                 2EKE  2ESK  2ESO  2ESP  2ESQ  2F4W  2FO3  2FUH  2GJD  2GMI  
                 2GRN  2GRO  2GRP  2GRQ  2GRR  2H2Y  2O25  2OB4  2OGB  2ONU  
                 2UCZ  2UYZ  2Z5D  2Z6O  2Z6P  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.19
            ExPASy - ENZYME nomenclature database: 6.3.2.19
            ExplorEnz - The Enzyme Database: 6.3.2.19
            ERGO genome analysis and discovery system: 6.3.2.19
            BRENDA, the Enzyme Database: 6.3.2.19
            CAS: 74812-49-0
///
ENTRY       EC 6.3.2.20                 Enzyme
NAME        indoleacetate---lysine synthetase;
            indoleacetate:L-lysine ligase (ADP-forming)
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     (indol-3-yl)acetate:L-lysine ligase (ADP-forming)
REACTION    ATP + (indol-3-yl)acetate + L-lysine = ADP + phosphate +
            N6-[(indol-3-yl)acetyl]-L-lysine [RN:R03095]
ALL_REAC    R03095
SUBSTRATE   ATP [CPD:C00002];
            (indol-3-yl)acetate [CPD:C00954];
            L-lysine [CPD:C00047]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            N6-[(indol-3-yl)acetyl]-L-lysine [CPD:C04211]
REFERENCE   1  [PMID:3084452]
  AUTHORS   Glass NL, Kosuge T.
  TITLE     Cloning of the gene for indoleacetic acid-lysine synthetase from
            Pseudomonas syringae subsp. savastanoi.
  JOURNAL   J. Bacteriol. 166 (1986) 598-603.
  ORGANISM  Pseudomonas syringae subsp. savastanoi
REFERENCE   2  [PMID:5644130]
  AUTHORS   Hutzinger O, Kosuge T.
  TITLE     Microbial synthesis and degradation of indole-3-acetic acid. 3. The
            isolation and characterization of indole-3-acetyl-epsilon-L-lysine.
  JOURNAL   Biochemistry. 7 (1968) 601-5.
  ORGANISM  Pseudomonas sacastanoi
ORTHOLOGY   KO: K03397  indoleacetate---lysine synthetase
GENES       PST: PSPTO_0371(iaaL)
            BUR: Bcep18194_C6699
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.20
            ExPASy - ENZYME nomenclature database: 6.3.2.20
            ExplorEnz - The Enzyme Database: 6.3.2.20
            ERGO genome analysis and discovery system: 6.3.2.20
            BRENDA, the Enzyme Database: 6.3.2.20
            CAS: 103537-15-1
///
ENTRY       EC 6.3.2.21                 Enzyme
NAME        ubiquitin---calmodulin ligase;
            ubiquityl-calmodulin synthase;
            ubiquitin-calmodulin synthetase;
            ubiquityl-calmodulin synthetase;
            uCaM-synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     calmodulin:ubiquitin ligase (AMP-forming)
REACTION    n ATP + calmodulin + n ubiquitin = n AMP + n diphosphate +
            (ubiquitin)n-calmodulin [RN:R05193]
ALL_REAC    R05193
SUBSTRATE   ATP [CPD:C00002];
            calmodulin [CPD:C00391];
            ubiquitin [CPD:C00496]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            (ubiquitin)n-calmodulin [CPD:C03330]
COMMENT     Specific for Ca2+-calmodulin from vertebrates. At least three
            ubiquitin molecules can be coupled to lysine residues in calmodulin.
REFERENCE   1  [PMID:2853950]
  AUTHORS   Jennissen HP, Laub M.
  TITLE     Ubiquitin-calmodulin conjugating activity from cardiac muscle.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 369 (1988) 1325-30.
  ORGANISM  rabbit
REFERENCE   2  [PMID:2853949]
  AUTHORS   Ziegenhagen R, Jennissen HP.
  TITLE     Multiple ubiquitination of vertebrate calmodulin by reticulocyte
            lysate and inhibition of calmodulin conjugation by phosphorylase
            kinase.
  JOURNAL   Biol. Chem. Hoppe. Seyler. 369 (1988) 1317-24.
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.21
            ExPASy - ENZYME nomenclature database: 6.3.2.21
            ExplorEnz - The Enzyme Database: 6.3.2.21
            ERGO genome analysis and discovery system: 6.3.2.21
            BRENDA, the Enzyme Database: 6.3.2.21
            CAS: 119632-60-9
///
ENTRY       EC 6.3.2.22                 Enzyme
NAME        diphthine---ammonia ligase;
            diphthamide synthase;
            diphthamide synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     diphthine:ammonia ligase (ADP-forming)
REACTION    ATP + diphthine + NH3 = ADP + phosphate + diphthamide [RN:R03613]
ALL_REAC    R03613
SUBSTRATE   ATP [CPD:C00002];
            diphthine [CPD:C01573];
            NH3 [CPD:C00014]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            diphthamide [CPD:C01803]
REFERENCE   1  [PMID:3346227]
  AUTHORS   Moehring JM, Moehring TJ.
  TITLE     The post-translational trimethylation of diphthamide studied in
            vitro.
  JOURNAL   J. Biol. Chem. 263 (1988) 3840-4.
  ORGANISM  hamster
REFERENCE   2
  AUTHORS   Moehring, T.J. and Moehring, J.M.
  TITLE     Mutant cultured cells used to study the synthesis of diphthamide.
  JOURNAL   UCLA Symp. Mol. Cell. Biol. New Ser. 45 (1987) 53-63.
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.22
            ExPASy - ENZYME nomenclature database: 6.3.2.22
            ExplorEnz - The Enzyme Database: 6.3.2.22
            ERGO genome analysis and discovery system: 6.3.2.22
            BRENDA, the Enzyme Database: 6.3.2.22
            CAS: 114514-33-9
///
ENTRY       EC 6.3.2.23                 Enzyme
NAME        homoglutathione synthase;
            homoglutathione synthetase;
            beta-alanine specific hGSH synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     gamma-L-glutamyl-L-cysteine:beta-alanine ligase (ADP-forming)
REACTION    ATP + gamma-L-glutamyl-L-cysteine + beta-alanine = ADP + phosphate +
            gamma-L-glutamyl-L-cysteinyl-beta-alanine [RN:R02741]
ALL_REAC    R02741
SUBSTRATE   ATP [CPD:C00002];
            gamma-L-glutamyl-L-cysteine [CPD:C00669];
            beta-alanine [CPD:C00099]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            gamma-L-glutamyl-L-cysteinyl-beta-alanine [CPD:C04544]
COMMENT     Not identical with EC 6.3.2.3 glutathione synthase.
REFERENCE   1
  AUTHORS   Macnicol, P.K.
  TITLE     Homoglutathione and glutathione synthetases of legume seedlings -
            partial-purification and substrate-specificity.
  JOURNAL   Plant Sci. 53 (1987) 229-235.
  ORGANISM  Pisum sativum, Vigna radiata
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.23
            ExPASy - ENZYME nomenclature database: 6.3.2.23
            ExplorEnz - The Enzyme Database: 6.3.2.23
            ERGO genome analysis and discovery system: 6.3.2.23
            BRENDA, the Enzyme Database: 6.3.2.23
            CAS: 113875-72-2
///
ENTRY       EC 6.3.2.24                 Enzyme
NAME        tyrosine---arginine ligase;
            tyrosyl-arginine synthase;
            kyotorphin synthase;
            kyotorphin-synthesizing enzyme;
            kyotorphin synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     L-tyrosine:L-arginine ligase (AMP-forming)
REACTION    ATP + L-tyrosine + L-arginine = AMP + diphosphate +
            L-tyrosyl-L-arginine [RN:R00735]
ALL_REAC    R00735
SUBSTRATE   ATP [CPD:C00002];
            L-tyrosine [CPD:C00082];
            L-arginine [CPD:C00062]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-tyrosyl-L-arginine [CPD:C02993]
REFERENCE   1  [PMID:3597366]
  AUTHORS   Ueda H, Yoshihara Y, Fukushima N, Shiomi H, Nakamura A, Takagi H.
  TITLE     Kyotorphin (tyrosine-arginine) synthetase in rat brain synaptosomes.
  JOURNAL   J. Biol. Chem. 262 (1987) 8165-73.
  ORGANISM  rat [GN:rno]
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.24
            ExPASy - ENZYME nomenclature database: 6.3.2.24
            ExplorEnz - The Enzyme Database: 6.3.2.24
            ERGO genome analysis and discovery system: 6.3.2.24
            BRENDA, the Enzyme Database: 6.3.2.24
            CAS: 116036-78-3
///
ENTRY       EC 6.3.2.25                 Enzyme
NAME        tubulin---tyrosine ligase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     alpha-tubulin:L-tyrosine ligase (ADP-forming)
REACTION    ATP + detyrosinated alpha-tubulin + L-tyrosine = alpha-tubulin + ADP
            + phosphate [RN:R04730]
ALL_REAC    R04730
SUBSTRATE   ATP [CPD:C00002];
            detyrosinated alpha-tubulin [CPD:C05234];
            L-tyrosine [CPD:C00082]
PRODUCT     alpha-tubulin [CPD:C01392];
            ADP [CPD:C00008];
            phosphate [CPD:C00009]
COMMENT     L-Tyrosine is linked via a peptide bond to the C-terminus of
            de-tyrosinated alpha-tubulin (des-Tyromega-alpha-tubulin). The
            enzyme is highly specific for alpha-tubulin and moderately specific
            for ATP and L-tyrosine. L-Phenylalanine and
            3,4-dihydroxy-L-phenylalanine are transferred but with higher Km
            values.
REFERENCE   1  [PMID:3821560]
  AUTHORS   Wehland J, Schroder HC, Weber K.
  TITLE     Isolation and purification of tubulin tyrosine ligase.
  JOURNAL   Methods. Enzymol. 134 (1986) 170-9.
  ORGANISM  pig [GN:ssc]
REFERENCE   2  [PMID:7510228]
  AUTHORS   Rudiger M, Wehland J, Weber K.
  TITLE     The carboxy-terminal peptide of detyrosinated alpha tubulin provides
            a minimal system to study the substrate specificity of
            tubulin-tyrosine ligase.
  JOURNAL   Eur. J. Biochem. 220 (1994) 309-20.
  ORGANISM  pig [GN:ssc]
ORTHOLOGY   KO: K06047  
GENES       HSA: 26140(TTLL3)
            MMU: 69737(Ttl)
            RNO: 171572(Ttl)
            BTA: 514559(LOC514559)
            SSC: 445530(TTL)
            TET: TTHERM_00035680 TTHERM_00077290 TTHERM_00170310
                 TTHERM_00193570 TTHERM_00418200 TTHERM_00624190
                 TTHERM_00666600 TTHERM_00784660 TTHERM_00859290
                 TTHERM_00985000 TTHERM_01084300 TTHERM_01109810
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.25
            ExPASy - ENZYME nomenclature database: 6.3.2.25
            ExplorEnz - The Enzyme Database: 6.3.2.25
            ERGO genome analysis and discovery system: 6.3.2.25
            BRENDA, the Enzyme Database: 6.3.2.25
            CAS: 60321-03-1
///
ENTRY       EC 6.3.2.26                 Enzyme
NAME        N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase;
            L-delta-(alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase;
            ACV synthetase;
            L-alpha-aminoadipyl-cysteinyl-valine synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     L-2-aminohexanedioate:L-cysteine:L-valine ligase (AMP-forming,
            valine-inverting)
REACTION    3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O = 3 AMP
            + 3 diphosphate +
            N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine [RN:R04870]
ALL_REAC    R04870
SUBSTRATE   ATP [CPD:C00002];
            L-2-aminohexanedioate [CPD:C00956];
            L-cysteine [CPD:C00097];
            L-valine [CPD:C00183];
            H2O [CPD:C00001]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine [CPD:C05556]
COMMENT     Requires Mg2+. The enzyme contains 4'-phosphopantetheine, which may
            be involved in the mechanism of the reaction. Forms part of the
            penicillin biosynthesis pathway (for pathway, click here).
REFERENCE   1  [PMID:11851475]
  AUTHORS   Byford MF, Baldwin JE, Shiau CY, Schofield CJ.
  TITLE     The Mechanism of ACV Synthetase.
  JOURNAL   Chem. Rev. 97 (1997) 2631-2650.
  ORGANISM  Cephalosporium acremonium
REFERENCE   2  [PMID:9355751]
  AUTHORS   Theilgaard HB, Kristiansen KN, Henriksen CM, Nielsen J.
  TITLE     Purification and characterization of
            delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase from
            Penicillium chrysogenum.
  JOURNAL   Biochem. J. 327 ( Pt 1) (1997) 185-91.
  ORGANISM  Penicillium chrysogenum
PATHWAY     PATH: map00311  Penicillin and cephalosporin biosynthesis
GENES       AVA: Ava_1613 Ava_4099
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.26
            ExPASy - ENZYME nomenclature database: 6.3.2.26
            ExplorEnz - The Enzyme Database: 6.3.2.26
            ERGO genome analysis and discovery system: 6.3.2.26
            BRENDA, the Enzyme Database: 6.3.2.26
            CAS: 57219-73-5
///
ENTRY       EC 6.3.2.27                 Enzyme
NAME        aerobactin synthase;
            citrate:6-N-acetyl-6-N-hydroxy-L-lysine ligase (ADP-forming)
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     citrate:N6-acetyl-N6-hydroxy-L-lysine ligase (ADP-forming)
REACTION    4 ATP + citrate + 2 N6-acetyl-N6-hydroxy-L-lysine + 2 H2O = 4 ADP +
            4 phosphate + aerobactin [RN:R04357]
ALL_REAC    R04357
SUBSTRATE   ATP [CPD:C00002];
            citrate [CPD:C00158];
            N6-acetyl-N6-hydroxy-L-lysine [CPD:C03955];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            aerobactin [CPD:C05554]
COMMENT     Requires Mg2+. Aerobactin is one of a group of high-affinity iron
            chelators known as siderophores and is produced under conditions of
            iron deprivation [5]. It is a dihydroxamate comprising two molecules
            of N6-acetyl-N6-hydroxylysine and one molecule of citric acid. This
            is the last of the three enzymes involved in its synthesis, the
            others being EC 1.14.13.59, L-lysine 6-monooxygenase (NADPH) and EC
            2.3.1.102, N6-hydroxylysine O-acetyltransferase [3].
REFERENCE   1
  AUTHORS   Appanna, D.L., Grundy, B.J., Szczepan, E.W. and Viswanatha, T.
  TITLE     Aerobactin synthesis in a cell-free system of Aerobacter aerogenes
            62-1.
  JOURNAL   Biochim. Biophys. Acta 801 (1984) 437-443.
  ORGANISM  Aerobacter aerogenes
REFERENCE   2  [PMID:4313071]
  AUTHORS   Gibson F, Magrath DI.
  TITLE     The isolation and characterization of a hydroxamic acid (aerobactin)
            formed by Aerobacter aerogenes 62-I.
  JOURNAL   Biochim. Biophys. Acta. 192 (1969) 175-84.
  ORGANISM  Aerobacter aerogenes
REFERENCE   3
  AUTHORS   Maurer, P.J. and Miller, M.
  TITLE     Microbial iron chelators: total synthesis of aerobactin and its
            constituent amino acid, N6-acetyl-N6-hydroxylysine.
  JOURNAL   J. Am. Chem. Soc. 104 (1982) 3096-3101.
REFERENCE   4  [PMID:2935523]
  AUTHORS   de Lorenzo V, Bindereif A, Paw BH, Neilands JB.
  TITLE     Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in
            Escherichia coli K-12.
  JOURNAL   J. Bacteriol. 165 (1986) 570-8.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:15719346]
  AUTHORS   Challis GL.
  TITLE     A widely distributed bacterial pathway for siderophore biosynthesis
            independent of nonribosomal peptide synthetases.
  JOURNAL   Chembiochem. 6 (2005) 601-11.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00310  Lysine degradation
ORTHOLOGY   KO: K03894  aerobactin synthetase subunit alpha
            KO: K03895  aerobactin synthetase subunit beta
GENES       ECC: c3625(iucC) c3627(iucA)
            YPE: YPO0992(iucC)
            YPK: y3380(iucA1) y3381(iucA2) y3383(iucC)
            YPM: YP_3448(iucC)
            YPA: YPA_0272 YPA_0274 YPA_0275
            YPN: YPN_3187 YPN_3188 YPN_3190
            YPS: YPTB3263(rhbC) YPTB3265(iucC)
            SFL: SF3715(iucA) SF3717(iucC)
            SFX: S4054(iucC) S4056(iucA)
            SFV: SFV_3852(iucC) SFV_3854(iucA)
            SSN: SSON_3601(iucA) SSON_3603(iucC)
            SBO: SBO_4337(iucA) SBO_4339(iucC)
            VFI: VFA0161(iucA) VFA0163
            NOC: Noc_1812 Noc_1814
            BBA: Bd1574(iucC) Bd1576(iucA)
            GBE: GbCGDNIH1_2376 GbCGDNIH1_2378
            SAO: SAOUHSC_00079 SAOUHSC_00080
            FRA: Francci3_4058
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.27
            ExPASy - ENZYME nomenclature database: 6.3.2.27
            ExplorEnz - The Enzyme Database: 6.3.2.27
            ERGO genome analysis and discovery system: 6.3.2.27
            BRENDA, the Enzyme Database: 6.3.2.27
            CAS: 94047-30-0
///
ENTRY       EC 6.3.2.28                 Enzyme
NAME        L-amino-acid alpha-ligase;
            L-amino acid alpha-ligase;
            bacilysin synthetase;
            YwfE;
            L-amino acid ligase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     L-amino acid:L-amino acid ligase (ADP-forming)
REACTION    ATP + an L-amino acid + an L-amino acid = ADP + phosphate +
            L-aminoacyl-L-amino acid [RN:R07642]
ALL_REAC    R07642
SUBSTRATE   ATP [CPD:C00002];
            L-amino acid [CPD:C00151]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            L-aminoacyl-L-amino acid [CPD:C16116]
COMMENT     The enzyme from Bacillus sp. requires Mg2+ or Mn2+ for activity.
            While the enzyme has extremely broad substrate specificity, it does
            not accept highly charged amino acids, such as Lys, Arg, Glu and
            Asp, nor does it react with secondary amines such as Pro. The
            N-terminal residue of the alpha-dipeptide formed seems to be limited
            to Ala, Gly, Ser, Thr and Met (with Ala and Ser being the most
            preferred), whereas the C-terminal residue seems to allow for a
            wider variety of amino acids (but with a preference for Met and
            Phe). However, not all combinations or dipeptides are formed. For
            example, while Ser is acceptable for the N-terminus and Thr for the
            C-terminus, a Ser-Thr dipeptide is not formed. D-Ala, D-Ser and
            D-Phe are not substrates. Belongs in the ATP-dependent
            carboxylate-amine/thiol ligase superfamily.
REFERENCE   1  [PMID:16030213]
  AUTHORS   Tabata K, Ikeda H, Hashimoto S.
  TITLE     ywfE in Bacillus subtilis codes for a novel enzyme, L-amino acid
            ligase.
  JOURNAL   J. Bacteriol. 187 (2005) 5195-202.
  ORGANISM  Bacillus subtilis [GN:bsu]
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.28
            ExPASy - ENZYME nomenclature database: 6.3.2.28
            ExplorEnz - The Enzyme Database: 6.3.2.28
            ERGO genome analysis and discovery system: 6.3.2.28
            BRENDA, the Enzyme Database: 6.3.2.28
///
ENTRY       EC 6.3.2.29                 Enzyme
NAME        cyanophycin synthase (L-aspartate-adding);
            CphA (ambiguous);
            CphA1 (ambiguous);
            CphA2 (ambiguous);
            cyanophycin synthetase (ambiguous);
            multi-L-arginyl-poly-L-aspartate synthase (ambiguous)
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     cyanophycin:L-aspartate ligase (ADP-forming)
REACTION    ATP + [L-Asp(4-L-Arg)]n + L-Asp = ADP + phosphate +
            [L-Asp(4-L-Arg)]n-L-Asp
SUBSTRATE   ATP [CPD:C00002];
            [L-Asp(4-L-Arg)]n;
            L-Asp
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            [L-Asp(4-L-Arg)]n-L-Asp
COMMENT     Requires Mg2+ for activity. Both this enzyme and EC 6.3.2.30,
            cyanophycin synthase (L-arginine-adding), are required for the
            elongation of cyanophycin, which is a protein-like cell inclusion
            that is unique to cyanobacteria and acts as a temporary nitrogen
            store [2]. Both enzymes are found in the same protein but have
            different active sites [2]. Both L-Asp and L-Arg must be present
            before either enzyme will display significant activity [2].
REFERENCE   1  [PMID:11131019]
  AUTHORS   Aboulmagd E, Oppermann-Sanio FB, Steinbuchel A.
  TITLE     Molecular characterization of the cyanophycin synthetase from
            Synechocystis sp. strain PCC6308.
  JOURNAL   Arch. Microbiol. 174 (2000) 297-306.
REFERENCE   2  [PMID:11319097]
  AUTHORS   Aboulmagd E, Oppermann-Sanio FB, Steinbuchel A.
  TITLE     Purification of Synechocystis sp. strain PCC6308 cyanophycin
            synthetase and its characterization with respect to substrate and
            primer specificity.
  JOURNAL   Appl. Environ. Microbiol. 67 (2001) 2176-82.
REFERENCE   3  [PMID:6767688]
  AUTHORS   Allen MM, Hutchison F, Weathers PJ.
  TITLE     Cyanophycin granule polypeptide formation and degradation in the
            cyanobacterium Aphanocapsa 6308.
  JOURNAL   J. Bacteriol. 141 (1980) 687-93.
REFERENCE   4  [PMID:10951215]
  AUTHORS   Berg H, Ziegler K, Piotukh K, Baier K, Lockau W, Volkmer-Engert R.
  TITLE     Biosynthesis of the cyanobacterial reserve polymer
            multi-L-arginyl-poly-L-aspartic acid (cyanophycin): mechanism of the
            cyanophycin synthetase reaction studied with synthetic primers.
  JOURNAL   Eur. J. Biochem. 267 (2000) 5561-70.
REFERENCE   5  [PMID:12132696]
  AUTHORS   Ziegler K, Deutzmann R, Lockau W.
  TITLE     Cyanophycin synthetase-like enzymes of non-cyanobacterial
            eubacteria: characterization of the polymer produced by a
            recombinant synthetase of Desulfitobacterium hafniense.
  JOURNAL   Z. Naturforsch. [C]. 57 (2002) 522-9.
REFERENCE   6  [PMID:9652408]
  AUTHORS   Ziegler K, Diener A, Herpin C, Richter R, Deutzmann R, Lockau W.
  TITLE     Molecular characterization of cyanophycin synthetase, the enzyme
            catalyzing the biosynthesis of the cyanobacterial reserve material
            multi-L-arginyl-poly-L-aspartate (cyanophycin).
  JOURNAL   Eur. J. Biochem. 254 (1998) 154-9.
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.29
            ExPASy - ENZYME nomenclature database: 6.3.2.29
            ExplorEnz - The Enzyme Database: 6.3.2.29
            ERGO genome analysis and discovery system: 6.3.2.29
            BRENDA, the Enzyme Database: 6.3.2.29
            CAS: 131554-17-1
///
ENTRY       EC 6.3.2.30                 Enzyme
NAME        cyanophycin synthase (L-arginine-adding);
            CphA (ambiguous);
            CphA1 (ambiguous);
            CphA2 (ambiguous);
            cyanophycin synthetase (ambiguous);
            multi-L-arginyl-poly-L-aspartate synthase (ambiguous)
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
SYSNAME     cyanophycin:L-arginine ligase (ADP-forming)
REACTION    ATP + [L-Asp(4-L-Arg)]n-L-Asp + L-Arg = ADP + phosphate +
            [L-Asp(4-L-Arg)]n+1
SUBSTRATE   ATP [CPD:C00002];
            [L-Asp(4-L-Arg)]n-L-Asp;
            L-Arg
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            [L-Asp(4-L-Arg)]n+1
COMMENT     Requires Mg2+ for activity. Both this enzyme and EC 6.3.2.29,
            cyanophycin synthase (L-aspartate-adding), are required for the
            elongation of cyanophycin, which is a protein-like cell inclusion
            that is unique to cyanobacteria and acts as a temporary nitrogen
            store [2]. Both enzymes are found in the same protein but have
            different active sites [2]. Both L-Asp and L-Arg must be present
            before either enzyme will display significant activity [2].
            Canavanine and lysine can be incoporated into the polymer instead of
            arginine [2].
REFERENCE   1  [PMID:11131019]
  AUTHORS   Aboulmagd E, Oppermann-Sanio FB, Steinbuchel A.
  TITLE     Molecular characterization of the cyanophycin synthetase from
            Synechocystis sp. strain PCC6308.
  JOURNAL   Arch. Microbiol. 174 (2000) 297-306.
REFERENCE   2  [PMID:11319097]
  AUTHORS   Aboulmagd E, Oppermann-Sanio FB, Steinbuchel A.
  TITLE     Purification of Synechocystis sp. strain PCC6308 cyanophycin
            synthetase and its characterization with respect to substrate and
            primer specificity.
  JOURNAL   Appl. Environ. Microbiol. 67 (2001) 2176-82.
REFERENCE   3  [PMID:6767688]
  AUTHORS   Allen MM, Hutchison F, Weathers PJ.
  TITLE     Cyanophycin granule polypeptide formation and degradation in the
            cyanobacterium Aphanocapsa 6308.
  JOURNAL   J. Bacteriol. 141 (1980) 687-93.
REFERENCE   4  [PMID:10951215]
  AUTHORS   Berg H, Ziegler K, Piotukh K, Baier K, Lockau W, Volkmer-Engert R.
  TITLE     Biosynthesis of the cyanobacterial reserve polymer
            multi-L-arginyl-poly-L-aspartic acid (cyanophycin): mechanism of the
            cyanophycin synthetase reaction studied with synthetic primers.
  JOURNAL   Eur. J. Biochem. 267 (2000) 5561-70.
REFERENCE   5  [PMID:12132696]
  AUTHORS   Ziegler K, Deutzmann R, Lockau W.
  TITLE     Cyanophycin synthetase-like enzymes of non-cyanobacterial
            eubacteria: characterization of the polymer produced by a
            recombinant synthetase of Desulfitobacterium hafniense.
  JOURNAL   Z. Naturforsch. [C]. 57 (2002) 522-9.
REFERENCE   6  [PMID:9652408]
  AUTHORS   Ziegler K, Diener A, Herpin C, Richter R, Deutzmann R, Lockau W.
  TITLE     Molecular characterization of cyanophycin synthetase, the enzyme
            catalyzing the biosynthesis of the cyanobacterial reserve material
            multi-L-arginyl-poly-L-aspartate (cyanophycin).
  JOURNAL   Eur. J. Biochem. 254 (1998) 154-9.
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.2.30
            ExPASy - ENZYME nomenclature database: 6.3.2.30
            ExplorEnz - The Enzyme Database: 6.3.2.30
            ERGO genome analysis and discovery system: 6.3.2.30
            BRENDA, the Enzyme Database: 6.3.2.30
            CAS: 131554-17-1
///
ENTRY       EC 6.3.2.-                  Enzyme
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Acid-D-amino-acid ligases (peptide synthases)
REACTION    (1) ATP + 2,3-Dihydroxybenzoate <=> Pyrophosphate +
            (2,3-Dihydroxybenzoyl)adenylate [RN:R01504];
            (2) 5-Hydroxyindoleacetate <=> 5-Hydroxyindoleacetylglycine
            [RN:R04906]
SUBSTRATE   ATP [CPD:C00002];
            2,3-Dihydroxybenzoate [CPD:C00196];
            5-Hydroxyindoleacetate [CPD:C05635]
PRODUCT     Pyrophosphate [CPD:C00013];
            (2,3-Dihydroxybenzoyl)adenylate [CPD:C04030];
            5-Hydroxyindoleacetylglycine [CPD:C05832]
///
ENTRY       EC 6.3.3.1                  Enzyme
NAME        phosphoribosylformylglycinamidine cyclo-ligase;
            phosphoribosylaminoimidazole synthetase;
            AIR synthetase;
            5'-aminoimidazole ribonucleotide synthetase;
            2-(formamido)-1-N-(5-phosphoribosyl)acetamidine cyclo-ligase
            (ADP-forming)
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Cyclo-ligases
SYSNAME     2-(formamido)-N1-(5-phosphoribosyl)acetamidine cyclo-ligase
            (ADP-forming)
REACTION    ATP + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine = ADP +
            phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole [RN:R04208]
ALL_REAC    R04208
SUBSTRATE   ATP [CPD:C00002];
            2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine [CPD:C04640]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            5-amino-1-(5-phospho-D-ribosyl)imidazole [CPD:C03373]
REFERENCE   1  [PMID:13405929]
  AUTHORS   LEVENBERG B, BUCHANAN JM.
  TITLE     Biosynthesis of the purines.  XII.  Structure, enzymatic synthesis,
            and metabolism of 5-amino-imidazole ribotide.
  JOURNAL   J. Biol. Chem. 224 (1957) 1005-18.
  ORGANISM  pigeon
REFERENCE   2  [PMID:13405930]
  AUTHORS   LEVENBERG B, BUCHANAN JM.
  TITLE     Biosynthesis of the purines.  XIII.  Structure, enzymatic synthesis,
            and metabolism of (alpha-N-formyl)-glycinamidine ribotide.
  JOURNAL   J. Biol. Chem. 224 (1957) 1019-27.
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01933  phosphoribosylformylglycinamidine cyclo-ligase
GENES       HSA: 2618(GART)
            MMU: 14450(Gart)
            CFA: 487740(LOC487740)
            GGA: 395315(GART)
            CEL: F38B6.4(GARS\\/AIRS\\/GART)
            OSA: 4334671
            CME: CMN264C
            SCE: YGL234W(ADE5,7)
            AGO: AGOS_AFR254C
            SPO: SPBC405.01(ade1)
            ANI: AN6541.2
            AFM: AFUA_6G04730
            AOR: AO090701000066
            CNE: CNN00440
            DDI: DDB_0230084(purD)
            ECO: b2499(purM)
            ECJ: JW2484(purM)
            ECE: Z3762(purM)
            ECS: ECs3361
            ECC: c3017(purM)
            ECI: UTI89_C2815(purM)
            ECP: ECP_2501
            ECV: APECO1_4070(purM)
            ECW: EcE24377A_2782(purM)
            ECX: EcHS_A2634
            STY: STY2740(purM)
            STT: t0358(purM)
            SPT: SPA0368(purM)
            SEC: SC2496(purM)
            STM: STM2499.S(purM)
            YPE: YPO2828(purI)
            YPK: y1407(purM)
            YPM: YP_2696(purI)
            YPA: YPA_2265
            YPN: YPN_1310
            YPP: YPDSF_2178
            YPS: YPTB2795(purI)
            YPI: YpsIP31758_1234(purM)
            YEN: YE1127(purI)
            SFL: SF2543(purM)
            SFX: S2692(purM)
            SFV: SFV_2544(purM)
            SSN: SSON_2581(purM)
            SBO: SBO_2520(purM)
            SDY: SDY_2688(purM)
            ECA: ECA1254(purM)
            PLU: plu2760(purM)
            WBR: WGLp332(purM)
            SGL: SG1732
            ENT: Ent638_2988
            SPE: Spro_3524
            HIN: HI1429(purM)
            HIT: NTHI1704(purM)
            HIQ: CGSHiGG_01020
            HDU: HD0561(purM)
            HSO: HS_1551(purM)
            PMU: PM0021(purM)
            MSU: MS0626(purM)
            APL: APL_1095(purM)
            ASU: Asuc_0729
            XFA: XF0587
            XFT: PD1564(purM)
            XCC: XCC2789(purM)
            XCB: XC_1324
            XCV: XCV3104(purM)
            XAC: XAC2959(purM)
            XOO: XOO1297(purM)
            XOM: XOO_1198(XOO1198)
            VCH: VC2226
            VCO: VC0395_A1819(purM)
            VVU: VV1_1900
            VVY: VV2515
            VPA: VP2285
            VFI: VF1928
            PPR: PBPRA2910(purM)
            PAE: PA0945(purM)
            PAU: PA14_52040(purM)
            PPU: PP_1665(purM)
            PPF: Pput_4053
            PST: PSPTO_1700(purM)
            PSB: Psyr_3689
            PSP: PSPPH_3710(purM)
            PFL: PFL_4440(purM)
            PFO: Pfl_1633
            PEN: PSEEN1370(purM)
            PMY: Pmen_2996
            PAR: Psyc_1624(purM)
            PCR: Pcryo_1856
            PRW: PsycPRwf_1440
            ACI: ACIAD2634(purM)
            SON: SO_2760(purM)
            SDN: Sden_2094
            SFR: Sfri_1452
            SAZ: Sama_2097
            SBL: Sbal_1735
            SBM: Shew185_1730
            SLO: Shew_1513
            SPC: Sputcn32_1596
            SSE: Ssed_1845
            SPL: Spea_2577
            SHE: Shewmr4_2380
            SHM: Shewmr7_2452
            SHN: Shewana3_2545
            SHW: Sputw3181_2426
            ILO: IL1661(purM)
            CPS: CPS_3196(purM)
            PHA: PSHAa1947(purM)
            PAT: Patl_2489
            SDE: Sde_0894
            PIN: Ping_1069
            MAQ: Maqu_0946
            CBU: CBU_1736(purM)
            CBD: COXBU7E912_0265(purM)
            LPN: lpg1677(purM)
            LPF: lpl1642(purM)
            LPP: lpp1649(purM)
            MCA: MCA0373(purM)
            FTU: FTT0893(purM)
            FTF: FTF0893(purM)
            FTW: FTW_1286(purM)
            FTL: FTL_0395
            FTH: FTH_0387(purM)
            FTA: FTA_0418(purM)
            FTN: FTN_0419(purM)
            TCX: Tcr_1046
            NOC: Noc_1182
            AEH: Mlg_0516
            HHA: Hhal_0710
            HCH: HCH_01906(purM)
            CSA: Csal_2112
            ABO: ABO_1573(purM)
            MMW: Mmwyl1_2808
            AHA: AHA_2821(purM)
            DNO: DNO_1113(purM)
            BCI: BCI_0072(purM)
            RMA: Rmag_0266
            VOK: COSY_0250(purM)
            NME: NMB1252
            NMA: NMA1421(purM)
            NMC: NMC1152(purM)
            NGO: NGO0526
            CVI: CV_3615(purM)
            RSO: RSc2623(purM)
            REU: Reut_A2773
            REH: H16_A3077(purM)
            RME: Rmet_2911
            BMA: BMA2317(purM)
            BMV: BMASAVP1_A0511(purM)
            BML: BMA10299_A1088(purM)
            BMN: BMA10247_2195(purM)
            BXE: Bxe_A3936
            BVI: Bcep1808_0721
            BUR: Bcep18194_A3848
            BCN: Bcen_0277
            BCH: Bcen2424_0761
            BAM: Bamb_0655
            BPS: BPSL2818(purM)
            BPM: BURPS1710b_3311(purM)
            BPL: BURPS1106A_3300(purM)
            BPD: BURPS668_3267(purM)
            BTE: BTH_I1317(purM)
            PNU: Pnuc_1761
            BPE: BP0242(purM)
            BPA: BPP3625(purM)
            BBR: BB4060(purM)
            RFR: Rfer_2512
            POL: Bpro_3566
            PNA: Pnap_2994
            AAV: Aave_1970
            AJS: Ajs_2994
            HAR: HEAR2634(purM)
            MMS: mma_2871
            NEU: NE0088(purM)
            NET: Neut_2277
            NMU: Nmul_A2617
            EBA: ebA7104(purM)
            AZO: azo3136(purM)
            DAR: Daro_3174
            TBD: Tbd_2667
            MFA: Mfla_0205
            HHE: HH1245(purM)
            WSU: WS2165(purM)
            TDN: Tmden_2050
            CJE: Cj1529c(purM)
            CJR: CJE1700(purM)
            CJJ: CJJ81176_1514(purM)
            CJU: C8J_1428(purM)
            CJD: JJD26997_1881(purM)
            CFF: CFF8240_1774(purM)
            CCV: CCV52592_0351(purM) CCV52592_1808
            CHA: CHAB381_0109(purM)
            CCO: CCC13826_1844(purM) CCC13826_2111
            ABU: Abu_0141(purM)
            NIS: NIS_0099(purM)
            SUN: SUN_2360(purM)
            GSU: GSU1758(purM)
            GME: Gmet_1844
            GUR: Gura_2153
            PCA: Pcar_1293
            PPD: Ppro_1772
            DVU: DVU1406(purM)
            DVL: Dvul_1668
            DDE: Dde_1672
            LIP: LI0296(purM)
            BBA: Bd3001(purM)
            DPS: DP2534
            ADE: Adeh_1255
            AFW: Anae109_2512
            MXA: MXAN_2701(purM)
            SAT: SYN_00889
            SFU: Sfum_3278
            WOL: WD1024(purM)
            WBM: Wbm0226
            AMA: AM983(purM)
            APH: APH_0202(purM-1) APH_0210(purM-2)
            ERU: Erum6580(purM)
            ERW: ERWE_CDS_06900(purM)
            ERG: ERGA_CDS_06810(purM)
            ECN: Ecaj_0665
            ECH: ECH_0342(purM)
            NSE: NSE_0031(purM)
            PUB: SAR11_0719(purM)
            MLO: mll7962
            MES: Meso_1966
            PLA: Plav_3331
            SME: SMc00615(purM)
            SMD: Smed_0792
            ATU: Atu1141(garS)
            ATC: AGR_C_2111
            RET: RHE_CH01488(purM)
            RLE: RL1596(purM)
            BME: BMEI1240
            BMF: BAB1_0731(purM)
            BMS: BR0710(purM)
            BMB: BruAb1_0729(purM)
            BOV: BOV_0701(purM)
            OAN: Oant_2576
            BJA: blr4125(garS)
            BRA: BRADO3344(purM)
            BBT: BBta_3852(purM)
            RPA: RPA3051(purM)
            RPB: RPB_2489
            RPC: RPC_2326
            RPD: RPD_2955
            RPE: RPE_3284
            NWI: Nwi_1597
            NHA: Nham_2118
            BHE: BH09560(purM)
            BQU: BQ07380(purM)
            BBK: BARBAKC583_0765(purM)
            XAU: Xaut_2323
            CCR: CC_1703
            SIL: SPO2169(purM)
            SIT: TM1040_1476
            RSP: RSP_1969(purM)
            RSH: Rsph17029_0677
            RSQ: Rsph17025_3066
            JAN: Jann_1836
            RDE: RD1_2252
            PDE: Pden_3926
            MMR: Mmar10_1247
            HNE: HNE_2263(purM)
            ZMO: ZMO0709(purM)
            NAR: Saro_0899
            SAL: Sala_1757
            SWI: Swit_0034
            ELI: ELI_08850
            GOX: GOX1934
            GBE: GbCGDNIH1_2037
            ACR: Acry_2537
            RRU: Rru_A2167
            MAG: amb2846
            MGM: Mmc1_2316
            ABA: Acid345_3011
            SUS: Acid_6722
            BSU: BG10708(purM)
            BHA: BH0631(purM)
            BAN: BA0296(purM)
            BAR: GBAA0296(purM)
            BAA: BA_0868
            BAT: BAS0283
            BCE: BC0331
            BCA: BCE_0325(purM)
            BCZ: BCZK0271(purM)
            BCY: Bcer98_0275
            BTK: BT9727_0268(purM)
            BTL: BALH_0290(purM)
            BLI: BL01484(purM)
            BLD: BLi00701(purM)
            BCL: ABC1032(purM)
            BAY: RBAM_006920
            BPU: BPUM_0604
            OIH: OB0747
            GKA: GK0265
            SAU: SA0923(purM)
            SAV: SAV1071(purM)
            SAM: MW0954(purM)
            SAR: SAR1045(purM)
            SAS: SAS1007
            SAC: SACOL1080(purM)
            SAB: SAB0938(purM)
            SAA: SAUSA300_0973(purM)
            SAO: SAOUHSC_01015
            SAJ: SaurJH9_1131
            SAH: SaurJH1_1153
            SEP: SE0769
            SER: SERP0656(purM)
            SHA: SH1886(purM)
            SSP: SSP1719
            LMO: lmo1767(purM)
            LMF: LMOf2365_1792(purM)
            LIN: lin1879(purM)
            LWE: lwe1785(purM)
            LLA: L165202(purM)
            LLC: LACR_1611
            LLM: llmg_0987(purM)
            SPY: SPy_0027(purM)
            SPZ: M5005_Spy_0025(purM)
            SPM: spyM18_0028(purM)
            SPG: SpyM3_0022(purM)
            SPS: SPs0023
            SPH: MGAS10270_Spy0026(purM)
            SPI: MGAS10750_Spy0025(purM)
            SPJ: MGAS2096_Spy0026(purM)
            SPK: MGAS9429_Spy0025(purM)
            SPF: SpyM50024(purM)
            SPA: M6_Spy0074
            SPB: M28_Spy0025(purM)
            SPN: SP_0047
            SPR: spr0048(purM)
            SPD: SPD_0054(purM)
            SAG: SAG0027(purM)
            SAN: gbs0026
            SAK: SAK_0060(purM)
            SMU: SMU.34(purM)
            STC: str0033(purM)
            STL: stu0033(purM)
            STE: STER_0052
            SSA: SSA_0032(purM)
            SGO: SGO_0037(purM)
            LPL: lp_2722(purM)
            LAC: LBA1554(purM)
            LSA: LSA0660(purM)
            LSL: LSL_0668(purM)
            LDB: Ldb1438(purM)
            LBU: LBUL_1333
            LCA: LSEI_1749
            LRE: Lreu_0142
            EFA: EF1780(purM)
            OOE: OEOE_1131
            STH: STH2853
            CAC: CAC1393(purM)
            CPE: CPE0684(purM)
            CPF: CPF_0675(purM)
            CPR: CPR_0673(purM)
            CTC: CTC01964
            CNO: NT01CX_2421(purM)
            CTH: Cthe_1248
            CDF: CD0221(purG)
            CBO: CBO2875(purG)
            CBA: CLB_2840(purM)
            CBH: CLC_2773(purM)
            CBF: CLI_2933(purM)
            CKL: CKL_2686(purM)
            AMT: Amet_0923
            CHY: CHY_1076(purM)
            DSY: DSY3929
            DRM: Dred_2364
            SWO: Swol_1777
            CSC: Csac_1994
            TTE: TTE0590(purM)
            MTA: Moth_2046
            MTU: Rv0809(purM)
            MTC: MT0830(purM)
            MBO: Mb0832(purM)
            MBB: BCG_0861(purM)
            MLE: ML2205(purM)
            MPA: MAP0639(purM)
            MAV: MAV_0748(purM)
            MSM: MSMEG_5798(purM)
            MVA: Mvan_5111
            MGI: Mflv_1636
            MMC: Mmcs_4538
            MKM: Mkms_4625
            MJL: Mjls_4921
            CGL: NCgl2494(cgl2583)
            CGB: cg2856(purM)
            CEF: CE2475(purM)
            CDI: DIP1919(purM)
            CJK: jk0359(purM)
            NFA: nfa5800(purM)
            RHA: RHA1_ro04841(purM)
            SCO: SCO4087(purM)
            SMA: SAV4134(purM)
            TWH: TWT724(purM)
            TWS: TW738(purM)
            LXX: Lxx22750(purM)
            CMI: CMM_0758(purM)
            ART: Arth_3736
            AAU: AAur_3526(purM)
            PAC: PPA1969
            NCA: Noca_4315
            TFU: Tfu_2748
            FRA: Francci3_0095
            FAL: FRAAL0129(purM)
            ACE: Acel_2071
            KRA: Krad_4040
            SEN: SACE_7124(purM)
            STP: Strop_0155
            BLO: BL1122(purM)
            BAD: BAD_0520(purM)
            RXY: Rxyl_0998
            FNU: FN0986
            RBA: RB12745(purM)
            TDE: TDE1266(purM)
            LIL: LA2935(purM)
            LIC: LIC11123(purM)
            LBJ: LBJ_2290(purM)
            LBL: LBL_0817(purM)
            SYN: slr0838(purM)
            SYW: SYNW2029(purM)
            SYC: syc0689_c(purM)
            SYF: Synpcc7942_0851
            SYD: Syncc9605_0414
            SYE: Syncc9902_1916
            SYG: sync_0481(purM)
            SYR: SynRCC307_2071(purM)
            SYX: SynWH7803_0472(purM)
            CYA: CYA_2883(purM)
            CYB: CYB_1656(purM)
            TEL: tlr1811(purM)
            GVI: gll0720(purM)
            ANA: alr3525
            AVA: Ava_3213
            PMA: Pro1745(purM)
            PMM: PMM1589(purM)
            PMT: PMT1691(purM)
            PMN: PMN2A_1164
            PMI: PMT9312_1681
            PMB: A9601_17981(purM)
            PMC: P9515_17761(purM)
            PMF: P9303_22491(purM)
            PMG: P9301_17811(purM)
            PMH: P9215_18621
            PME: NATL1_20391(purM)
            TER: Tery_2801
            BTH: BT_4211
            BFR: BF0911
            BFS: BF0833
            PGI: PG0075
            SRU: SRU_1479(purM)
            CHU: CHU_0126(purM)
            GFO: GFO_0472(purM)
            FJO: Fjoh_2353
            FPS: FP0685(purM)
            CTE: CT0094(purM)
            CCH: Cag_2024
            CPH: Cpha266_2582
            PVI: Cvib_1701
            PLT: Plut_2059
            DET: DET1416(purM)
            DEH: cbdb_A1378(purM)
            DEB: DehaBAV1_1223
            RRS: RoseRS_2554
            RCA: Rcas_1844
            DRA: DR_1394
            DGE: Dgeo_1616
            TTH: TTC1619
            TTJ: TTHA0367
            AAE: aq_769(purM)
            TMA: TM1251
            TPT: Tpet_1520
            TME: Tmel_0385
            FNO: Fnod_1671
            MMP: MMP0882(purM) MMP1254(purM)
            MMZ: MmarC7_0500
            MVN: Mevan_0568
            MAC: MA0130(purM)
            MBA: Mbar_A0862
            MMA: MM_1416
            MBU: Mbur_1979
            MHU: Mhun_3055
            MEM: Memar_0223
            MBN: Mboo_0088
            MST: Msp_0280(purM)
            MSI: Msm_1039
            MKA: MK1226(purM)
            HAL: VNG0876G(purM)
            HMA: rrnAC0438(purM)
            HWA: HQ2665A(purM)
            NPH: NP3940A(purM)
            TAC: Ta0090
            TVO: TVN0164
            PTO: PTO0468 PTO1289
            PAB: PAB1083(purM)
            PFU: PF0431
            TKO: TK0208
            RCI: RCIX1823(purM)
            IHO: Igni_0311
            SSO: SSO0636(purM)
            STO: ST1499
            SAI: Saci_1614
            MSE: Msed_1984
            PAI: PAE0221(purM)
            PIS: Pisl_0110
            PCL: Pcal_1899
            PAS: Pars_2191
STRUCTURES  PDB: 1CLI  2BTU  2QK4  2V9Y  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.3.1
            ExPASy - ENZYME nomenclature database: 6.3.3.1
            ExplorEnz - The Enzyme Database: 6.3.3.1
            ERGO genome analysis and discovery system: 6.3.3.1
            BRENDA, the Enzyme Database: 6.3.3.1
            CAS: 9023-53-4
///
ENTRY       EC 6.3.3.2                  Enzyme
NAME        5-formyltetrahydrofolate cyclo-ligase;
            5,10-methenyltetrahydrofolate synthetase;
            formyltetrahydrofolic cyclodehydrase;
            5-formyltetrahydrofolate cyclodehydrase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Cyclo-ligases
SYSNAME     5-formyltetrahydrofolate cyclo-ligase (ADP-forming)
REACTION    ATP + 5-formyltetrahydrofolate = ADP + phosphate +
            5,10-methenyltetrahydrofolate [RN:R02301]
ALL_REAC    R02301
SUBSTRATE   ATP [CPD:C00002];
            5-formyltetrahydrofolate [CPD:C03479]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            5,10-methenyltetrahydrofolate [CPD:C00445]
REFERENCE   1
  AUTHORS   Greenberg, D.M., Wynston, L.K. and Nagabhushanan, A.
  TITLE     Further studies on N5-formyltetrahydrofolic acid cyclodehydrase.
  JOURNAL   Biochemistry 4 (1965) 1872-1878.
  ORGANISM  sheep
PATHWAY     PATH: map00670  One carbon pool by folate
ORTHOLOGY   KO: K01934  5-formyltetrahydrofolate cyclo-ligase
GENES       HSA: 10588(MTHFS)
            PTR: 453578(MTHFS)
            MMU: 107885(Mthfs)
            CFA: 610157(MTHFS)
            GGA: 415484(MTHFS)
            SPU: 753829(LOC753829)
            CEL: Y106G6E.4
            OSA: 4343714
            CME: CMH212C CMM112C
            SCE: YER183C(FAU1)
            AGO: AGOS_ADL385C
            PIC: PICST_36098(FAU1)
            CGR: CAGL0F09185g
            SPO: SPBC1703.08c
            AOR: AO090005000463
            UMA: UM03307.1
            TET: TTHERM_00149990
            ECV: APECO1_3617
            ECW: EcE24377A_3239
            ECX: EcHS_A3070
            YPE: YPO0913
            YPI: YpsIP31758_0857
            ECA: ECA0462
            SGL: SG2008
            BPN: BPEN_264(ygfA)
            HIT: NTHI1027
            XFA: XF2013
            XFT: PD0799
            XCC: XCC3263
            XCB: XC_0901
            XCV: XCV3526
            XAC: XAC3409
            XOO: XOO1129
            XOM: XOO_1025(XOO1025)
            VFI: VF2104
            PAU: PA14_69040
            PAP: PSPA7_5971
            PSP: PSPPH_0302
            PEN: PSEEN5319
            PAR: Psyc_1658
            PCR: Pcryo_1895
            SDN: Sden_0828
            SFR: Sfri_3159
            SHE: Shewmr4_3336
            SHM: Shewmr7_0617
            SHN: Shewana3_3506
            CPS: CPS_3648
            PHA: PSHAa0668
            SDE: Sde_3517
            CBD: COXBU7E912_2040
            FTU: FTT1220
            FTF: FTF1220
            FTW: FTW_0726
            FTL: FTL_0724
            FTH: FTH_0726
            FTA: FTA_0764
            FTN: FTN_1239
            TCX: Tcr_1562
            AEH: Mlg_2538
            CSA: Csal_0021
            AHA: AHA_2727
            DNO: DNO_1201
            BCI: BCI_0648
            VOK: COSY_0871
            CVI: CV_0499
            REH: H16_A0249
            MMS: mma_3192
            TBD: Tbd_2724
            CFF: CFF8240_0501
            CCV: CCV52592_1397
            CHA: CHAB381_1329
            CCO: CCC13826_1310
            PCA: Pcar_2351
            DVU: DVU0366
            LIP: LI0770
            BBA: Bd1186
            DPS: DP0646
            MXA: MXAN_2978
            RTY: RT0448
            RCO: RC0694
            RFE: RF_0808
            RBE: RBE_0893
            AMA: AM606(ygfA)
            NSE: NSE_0133
            PUB: SAR11_0588(yqgN) SAR11_0590
            ATU: Atu3731
            RET: RHE_CH03471(ypch01227)
            RLE: RL3979
            BME: BMEI0315
            BMF: BAB1_1735
            BOV: BOV_1666
            BRA: BRADO1138
            BBT: BBta_6914
            RPC: RPC_4812
            RPE: RPE_4775
            NWI: Nwi_2731
            NHA: Nham_3528
            BBK: BARBAKC583_0203
            CCR: CC_3245
            SIL: SPO2954
            SIT: TM1040_1903
            RSP: RSP_1898
            JAN: Jann_3386
            RDE: RD1_2010
            ZMO: ZMO0215
            GOX: GOX0226
            GBE: GbCGDNIH1_1094
            MAG: amb3224
            MGM: Mmc1_0714
            BSU: BG11681(yqgN)
            BHA: BH1417
            BAN: BA4489
            BAR: GBAA4489
            BAA: BA_4936
            BAT: BAS4167
            BCE: BC4262
            BCA: BCE_4345
            BCZ: BCZK4016
            BTK: BT9727_4006
            BTL: BALH_3859
            BLD: BLi02666(yqgN)
            BCL: ABC1722
            BAY: RBAM_023210(yqgN)
            BPU: BPUM_2219(yqgN)
            OIH: OB1924
            GKA: GK2449
            LMO: lmo1336
            LMF: LMOf2365_1353
            LIN: lin1373
            LWE: lwe1351
            LLM: llmg_0181
            SPN: SP_2095
            SPR: spr1905
            SAG: SAG0403
            SAN: gbs0438
            SAK: SAK_0476
            SMU: SMU.320
            STC: str1837
            STL: stu1837
            SGO: SGO_0160
            LPL: lp_1570(fthC)
            LJO: LJ1619
            LAC: LBA1507
            LSA: LSA1332(fthC)
            LSL: LSL_0549
            LBU: LBUL_1375
            LBR: LVIS_0999
            LCA: LSEI_0736
            EFA: EF2791
            OOE: OEOE_0779
            LME: LEUM_A22
            STH: STH1192
            CAC: CAC1090
            CPE: CPE2324
            CPF: CPF_2633
            CPR: CPR_2319
            CTC: CTC01011
            CNO: NT01CX_1657
            CHY: CHY_0730
            DSY: DSY3972
            SWO: Swol_1864
            MTA: Moth_2140
            MGE: MG_245
            MMY: MSC_0503
            MCP: MCAP_0467
            MFL: Mfl250
            MAV: MAV_1101
            MSM: MSMEG_5472
            CGL: NCgl0845(cgl0881)
            CGB: cg1003
            CMI: CMM_2447
            SEN: SACE_0773
            RXY: Rxyl_1321
            FNU: FN0902
            RBA: RB5405(mthfs)
            CTR: CT649(ygfA)
            CTA: CTA_0704(ygfA)
            CMU: TC0018
            CPN: CPn0763(ygfA)
            CPA: CP1109
            CPJ: CPj0763(ygfA)
            CPT: CpB0791
            CCA: CCA00994
            CAB: CAB964
            CFE: CF0019(ygfA)
            TPA: TP0694
            TDE: TDE0992
            LIL: LA1247
            LIC: LIC12458
            SYN: sll1643
            SYC: syc0253_c
            SYF: Synpcc7942_1300
            CYA: CYA_1588
            CYB: CYB_0394
            TEL: tll0980
            GVI: glr0759
            ANA: all4825
            AVA: Ava_2095
            TER: Tery_1879
            BTH: BT_4258
            BFR: BF0962
            PGI: PG1854
            CHU: CHU_0687(ygfA)
            GFO: GFO_3177
            FPS: FP0220(ygfA)
            CCH: Cag_0899
            PLT: Plut_1015
            TTH: TTC1803
            MHU: Mhun_0818
            HMA: rrnAC3378
            NPH: NP2438A
STRUCTURES  PDB: 1SBQ  1SOU  1U3F  1U3G  2JCB  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.3.2
            ExPASy - ENZYME nomenclature database: 6.3.3.2
            ExplorEnz - The Enzyme Database: 6.3.3.2
            ERGO genome analysis and discovery system: 6.3.3.2
            BRENDA, the Enzyme Database: 6.3.3.2
            CAS: 37318-64-2
///
ENTRY       EC 6.3.3.3                  Enzyme
NAME        dethiobiotin synthase;
            desthiobiotin synthase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Cyclo-ligases
SYSNAME     7,8-diaminononanoate:carbon-dioxide cyclo-ligase (ADP-forming)
REACTION    ATP + 7,8-diaminononanoate + CO2 = ADP + phosphate + dethiobiotin
            [RN:R03182]
ALL_REAC    R03182
SUBSTRATE   ATP [CPD:C00002];
            7,8-diaminononanoate [CPD:C01037];
            CO2 [CPD:C00011]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            dethiobiotin [CPD:C01909]
COMMENT     CTP has half the activity of ATP.
REFERENCE   1  [PMID:4921568]
  AUTHORS   Krell K, Eisenberg MA.
  TITLE     The purification and properties of dethiobiotin synthetase.
  JOURNAL   J. Biol. Chem. 245 (1970) 6558-66.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Yang, H.-C., Tani, Y. and Ogata, K.
  TITLE     Synthesis of biotin vitamers from biotin diaminocarboxylic acid or
            7,8-diaminopelargonic acid by a purified enzyme of Pseudomonas
            graveolens.
  JOURNAL   Agric. Biol. Chem. 34 (1970) 1748-1750.
  ORGANISM  Pseudomonas graveolens
PATHWAY     PATH: map00780  Biotin metabolism
ORTHOLOGY   KO: K01935  dethiobiotin synthetase
GENES       ATH: AT5G57600
            SCE: YNR057C(BIO4)
            PIC: PICST_85593(BIO4)
            ECO: b0778(bioD) b1593(ynfK)
            ECJ: JW0761(bioD) JW5264(ynfK)
            ECE: Z0997(bioD) Z2585
            ECS: ECs0856 ECs2299
            ECC: c0858(bioD) c1984(bioD)
            ECI: UTI89_C0776(bioD) UTI89_C1780(ynfK)
            ECP: ECP_0792 ECP_1537
            ECV: APECO1_1311(bioD) APECO1_676(ynfK)
            ECW: EcE24377A_0841(bioD)
            ECX: EcHS_A0832(bioD1) EcHS_A1667(bioD2)
            STY: STY0830(bioD) STY1575
            STT: t1410 t2090(bioD)
            SPT: SPA1365(ynfK) SPA1955(bioD)
            SEC: SC0795(bioD) SC1507(ynfK)
            STM: STM0797(bioD) STM1489(ynfK)
            YPE: YPO1154(bioD) YPO2269(bioD)
            YPK: y2111 y3028(bioD)
            YPM: YP_1006(bioD1) YP_2065(bioD2)
            YPA: YPA_1061 YPA_1629
            YPN: YPN_1741 YPN_2847
            YPP: YPDSF_0864 YPDSF_2543
            YPS: YPTB1185(bioD) YPTB2191(bioD)
            YPI: YpsIP31758_1868(bioD1) YpsIP31758_2841(bioD2)
            SFL: SF0728(bioD) SF1614(ynfK)
            SFX: S0769(bioD) S1746
            SFV: SFV_0761(bioD) SFV_1608
            SSN: SSON_0757(bioD) SSON_1571
            SBO: SBO_0665(bioD) SBO_1543
            SDY: SDY_0828(bioD) SDY_1563
            ECA: ECA2257(bioD) ECA2822(bioD)
            PLU: plu1488(bioD) plu2227
            BUC: BU290(bioD)
            BAB: bbp269(bioD)
            WBR: WGLp456(bioD)
            SGL: SG0906 SG1466
            ENT: Ent638_1269 Ent638_1920
            KPN: KPN_00803(bioD)
            SPE: Spro_1314 Spro_2284
            HIN: HI1445(bioD-1)
            HIT: NTHI1583(bioD-B) NTHI1685(bioD-A)
            HIP: CGSHiEE_04830(bioD) CGSHiEE_05340(bioD)
            HIQ: CGSHiGG_00210(bioD) CGSHiGG_01115(bioD)
            HDU: HD1480(bioD1) HD1680(bioD2)
            PMU: PM0641(bioD1) PM1904(bioD2)
            MSU: MS1006(bioD)
            APL: APL_0614(bioD1) APL_0938(bioD2)
            ASU: Asuc_1117
            XFA: XF2477
            XFT: PD1494(bioD)
            XCC: XCC0587(bioD)
            XCB: XC_3646
            XCV: XCV3736(bioD)
            XAC: XAC3616(bioD)
            XOO: XOO0767(bioD)
            XOM: XOO_0697(XOO0697)
            VCH: VC1115
            VCO: VC0395_A0633(bioD)
            VVU: VV1_2940
            VVY: VV1330
            VPA: VP1116
            VFI: VFA0745(bioD)
            PPR: PBPRA2326(bioD)
            PAE: PA0504(bioD)
            PAU: PA14_06570(bioD)
            PAP: PSPA7_0604(bioD)
            PPU: PP_0366(bioD)
            PPF: Pput_0392
            PST: PSPTO_0498(bioD)
            PSB: Psyr_4683(bioD)
            PSP: PSPPH_4717
            PFL: PFL_5689(bioD)
            PFO: Pfl_5172(bioD)
            PEN: PSEEN5117(bioD)
            PMY: Pmen_4084
            PAR: Psyc_0329(bioD)
            PCR: Pcryo_0362
            PRW: PsycPRwf_1160 PsycPRwf_1163
            ACI: ACIAD0859(bioD)
            SON: SO_2737(bioD)
            SDN: Sden_1661
            SFR: Sfri_1478
            SAZ: Sama_1441
            SBL: Sbal_1761
            SBM: Shew185_1754
            SLO: Shew_1722
            SPC: Sputcn32_2342
            SSE: Ssed_2773
            SPL: Spea_1804
            SHE: Shewmr4_2356
            SHM: Shewmr7_2428
            SHN: Shewana3_2516
            SHW: Sputw3181_1666
            ILO: IL1321(bioD)
            CPS: CPS_2597(bioD)
            PHA: PSHAa1606(bioD)
            PAT: Patl_2554
            SDE: Sde_3135
            PIN: Ping_1921
            MAQ: Maqu_2753
            CBU: CBU_1003(bioD)
            CBD: COXBU7E912_1045(bioD)
            LPN: lpg1475(bioD)
            LPF: lpl1553(bioD)
            LPP: lpp1431(bioD)
            MCA: MCA1129(bioD)
            FTU: FTT0934c(bioD)
            FTF: FTF0934c(bioD)
            FTW: FTW_2081
            FTL: FTL_1275
            FTH: FTH_1248(bioD)
            FTA: FTA_1348(bioD)
            FTN: FTN_0812(bioD)
            TCX: Tcr_0261
            NOC: Noc_2097
            AEH: Mlg_0292
            HHA: Hhal_0959
            HCH: HCH_05366(bioD)
            CSA: Csal_1163
            ABO: ABO_2216(bioD)
            MMW: Mmwyl1_3453
            AHA: AHA_1492(bioD)
            BCI: BCI_0249(bioD)
            VOK: COSY_0007(bioD)
            NME: NMB0733
            NMA: NMA0943(bioD)
            NMC: NMC0686(bioD)
            NGO: NGO0309(bioD)
            CVI: CV_0598(bioD)
            RSO: RSc1479(bioD)
            REU: Reut_A0149
            REH: H16_A0182(bioD)
            RME: Rmet_0116
            BMA: BMA0102(bioD)
            BMV: BMASAVP1_A3078(bioD)
            BML: BMA10299_A2016(bioD)
            BMN: BMA10247_2270(bioD)
            BXE: Bxe_A4265
            BVI: Bcep1808_3028
            BUR: Bcep18194_A6277(bioD)
            BCN: Bcen_2319
            BCH: Bcen2424_2933
            BAM: Bamb_2982
            BPS: BPSL0365(bioD)
            BPM: BURPS1710b_0572(bioD)
            BPL: BURPS1106A_0410(bioD)
            BPD: BURPS668_0389(bioD)
            BTE: BTH_I0338
            PNU: Pnuc_0153
            POL: Bpro_0899
            PNA: Pnap_4031
            AAV: Aave_3842
            MPT: Mpe_A0529
            HAR: HEAR0101 HEAR0970(cobQ)
            MMS: mma_0122(bioD)
            NEU: NE2296(bioD)
            NET: Neut_2134
            NMU: Nmul_A1133
            EBA: ebA6011(bioD)
            AZO: azo1892(bioD)
            DAR: Daro_2900
            TBD: Tbd_0323
            MFA: Mfla_2160
            HPY: HP0029(bioD)
            HPA: HPAG1_0027
            HHE: HH1211(bioD)
            HAC: Hac_0043(bioD)
            WSU: WS0335(bioD)
            TDN: Tmden_0460
            CJE: Cj0308c(bioD)
            CJR: CJE0353(bioD)
            CJJ: CJJ81176_0330(bioD)
            CJU: C8J_0285(bioD)
            CJD: JJD26997_1658(bioD)
            CFF: CFF8240_0083(bioD)
            ABU: Abu_1922(bioD)
            NIS: NIS_0378
            SUN: SUN_2067
            GSU: GSU1583(bioD)
            GME: Gmet_1581
            GUR: Gura_2243
            PCA: Pcar_1459
            PPD: Ppro_1176
            DVU: DVU2565(bioD)
            DVL: Dvul_0682
            DDE: Dde_2663
            LIP: LI0425(bioD)
            DPS: DP2544(bioD)
            ADE: Adeh_0070
            AFW: Anae109_0071
            MXA: MXAN_1259(bioD)
            SAT: SYN_02569
            SFU: Sfum_3711
            AMA: AM1128(dtbS)
            APH: APH_1228(bioD)
            ERU: Erum8510
            ERW: ERWE_CDS_09020(bioD)
            ERG: ERGA_CDS_08920(bioD)
            ECN: Ecaj_0888
            ECH: ECH_1110(bioD)
            NSE: NSE_0617(bioD)
            MLO: mll5829 mll6005 mll6270 mll9098
            ATU: Atu3999(bioD)
            ATC: AGR_L_1705(bioD)
            BME: BMEII0777(bioD)
            BMF: BAB2_0746
            BMS: BRA0490(bioD)
            BMB: BruAb2_0732(bioD)
            BOV: BOV_A0428(bioD)
            OAN: Oant_2821
            BJA: blr2098(bioD)
            BBT: BBta_2778(bioD)
            RPA: RPA2971(bioD)
            RPB: RPB_4343
            RPC: RPC_2098
            RPD: RPD_4239
            RPE: RPE_3401
            NWI: Nwi_2420(bioD)
            NHA: Nham_2815
            XAU: Xaut_2919
            CCR: CC_1575
            PDE: Pden_2918
            MMR: Mmar10_1345
            HNE: HNE_1249(bioD)
            ZMO: ZMO1915(bioD)
            NAR: Saro_0717
            SAL: Sala_1474
            SWI: Swit_1255
            GOX: GOX0723(bioD)
            GBE: GbCGDNIH1_0496
            ACR: Acry_1867
            MGM: Mmc1_0036
            BSU: BG11526(bioD)
            BHA: BH0783
            BAN: BA4340(bioD)
            BAR: GBAA4340(bioD)
            BAA: BA_4799(cbiA)
            BAT: BAS4027
            BCE: BC4118(bioD)
            BCA: BCE_4188(bioD)
            BCZ: BCZK3874(bioD)
            BCY: Bcer98_2817
            BTK: BT9727_3860(bioD)
            BLI: BL00955(bioD)
            BLD: BLi00769(bioD)
            BAY: RBAM_018260(bioD)
            GKA: GK3017
            SAU: SA2215(bioD)
            SAV: SAV2427(bioD)
            SAM: MW2350(bioD)
            SAR: SAR2517
            SAS: SAS2318
            SAC: SACOL2428(bioD)
            SAB: SAB2308c
            SAA: SAUSA300_2373(bioD)
            SAO: SAOUHSC_02716
            SAJ: SaurJH9_2453
            SAH: SaurJH1_2501
            SEP: SE0179
            SER: SERP2396(bioD)
            CAC: CAC1361(bioD)
            CPE: CPE1543(bioD)
            CPF: CPF_1794(bioD)
            CTC: CTC01860(bioD)
            CNO: NT01CX_1468
            CTH: Cthe_0021
            CBA: CLB_2199(bioD)
            CBH: CLC_2182(bioD)
            CBF: CLI_2308(bioD)
            CKL: CKL_0937(bioB1)
            CSC: Csac_0305
            MTU: Rv1570(bioD)
            MTC: MT1621(bioD)
            MBO: Mb1597(bioD)
            MBB: BCG_1623(bioD)
            MLE: ML1218(bioD)
            MPA: MAP1276(bioD)
            MAV: MAV_3204(bioD)
            MSM: MSMEG_3190(bioD)
            MVA: Mvan_2790
            MGI: Mflv_3627
            MMC: Mmcs_3076
            MKM: Mkms_3136
            MJL: Mjls_3093
            CGL: NCgl2516(bioD)
            CGB: cg2886(bioD)
            CEF: CE1420(bioD)
            CDI: DIP1189(bioD1) DIP1192(bioD)
            NFA: nfa18200(bioD)
            RHA: RHA1_ro01053(bioD)
            SCO: SCO1246(2SCG1.21)
            SMA: SAV7091(bioD)
            AAU: AAur_1087(bioD)
            PAC: PPA0968
            NCA: Noca_3412
            FRA: Francci3_3762
            FAL: FRAAL2887(bioD) FRAAL6002(bioD)
            ACE: Acel_1052
            SEN: SACE_0978(bioD)
            STP: Strop_1571
            FNU: FN1001
            RBA: RB5694(bioD)
            CPN: CPn1042(bioD)
            CPA: CP0810
            CPJ: CPj1042(bioD)
            CPT: CpB1082
            CAB: CAB687(bioD)
            CFE: CF0296(bioD)
            LIL: LA2141(bioD)
            LIC: LIC11779(bioD)
            LBJ: LBJ_1872(bioD)
            LBL: LBL_1412(bioD)
            SYN: slr0523(bioD)
            SYW: SYNW0631(bioD)
            SYC: syc1467_c(bioD)
            SYF: Synpcc7942_0030
            SYD: Syncc9605_2051
            SYE: Syncc9902_0621
            SYG: sync_2341
            SYR: SynRCC307_1927(bioD)
            SYX: SynWH7803_2045(bioD)
            TEL: tlr0206
            GVI: gll3509(bioD)
            ANA: all4667
            AVA: Ava_1996(bioD)
            PMA: Pro1625(cioD)
            PMM: PMM1471(bioD)
            PMT: PMT1491(bioD)
            PMN: PMN2A_1002
            PMI: PMT9312_1564
            PMB: A9601_16731(bioD)
            PMC: P9515_16511(bioD)
            PMF: P9303_04561(bioD)
            PMG: P9301_16611(bioD)
            PMH: P9215_17391(bioD)
            PME: NATL1_18711(bioD)
            TER: Tery_1842
            BTH: BT_1446
            BFR: BF1600
            BFS: BF1614(bioD)
            PGI: PG2053(bioD)
            CHU: CHU_2977(bioD)
            GFO: GFO_3562(bioD)
            FJO: Fjoh_0811
            FPS: FP2329(bioD)
            CTE: CT0048(bioD)
            CCH: Cag_0082(bioD)
            CPH: Cpha266_0116
            PVI: Cvib_1707
            PLT: Plut_2066(bioD)
            AAE: aq_557(bioD)
            MMP: MMP1573(bioD)
            MMQ: MmarC5_0003
            MMZ: MmarC7_0820
            MAE: Maeo_0883
            MVN: Mevan_0885
            NPH: NP4230A(bioD)
STRUCTURES  PDB: 1A82  1BS1  1BYI  1DAD  1DAE  1DAF  1DAG  1DAH  1DAI  1DAK  
                 1DAM  1DBS  1DTS  2QMO  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.3.3
            ExPASy - ENZYME nomenclature database: 6.3.3.3
            ExplorEnz - The Enzyme Database: 6.3.3.3
            ERGO genome analysis and discovery system: 6.3.3.3
            BRENDA, the Enzyme Database: 6.3.3.3
            CAS: 37259-75-9
///
ENTRY       EC 6.3.3.4                  Enzyme
NAME        (carboxyethyl)arginine beta-lactam-synthase;
            L-2-N-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming)
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Cyclo-ligases
SYSNAME     L-N2-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming)
REACTION    ATP + L-N2-(2-carboxyethyl)arginine = AMP + diphosphate +
            deoxyamidinoproclavaminate [RN:R05467]
ALL_REAC    R05467
SUBSTRATE   ATP [CPD:C00002];
            L-N2-(2-carboxyethyl)arginine [CPD:C06655]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            deoxyamidinoproclavaminate [CPD:C06656]
COMMENT     Forms part of the pathway for the biosythesis of the beta-lactamase
            inhibitor clavulanate in Streptomyces clavuligerus. It has been
            proposed [3] that L-N2-(2-carboxyethyl)arginine is first converted
            into an acyl-AMP by reaction with ATP and loss of diphosphate, and
            that the beta-lactam ring is then formed by the intramolecular
            attack of the beta-nitrogen on the activated carboxy group.
REFERENCE   1  [PMID:11472170]
  AUTHORS   Zhou J, Kelly WL, Bachmann BO, Gunsior M, Townsend CA, Solomon EI.
  TITLE     Spectroscopic studies of substrate interactions with clavaminate
            synthase 2, a multifunctional alpha-KG-dependent non-heme iron
            enzyme: correlation with mechanisms and reactivities.
  JOURNAL   J. Am. Chem. Soc. 123 (2001) 7388-98.
  ORGANISM  Streptomyces clavuligerus
REFERENCE   2  [PMID:12413541]
  AUTHORS   Townsend CA.
  TITLE     New reactions in clavulanic acid biosynthesis.
  JOURNAL   Curr. Opin. Chem. Biol. 6 (2002) 583-9.
  ORGANISM  Streptomyces clavuligerus
REFERENCE   3  [PMID:9689037]
  AUTHORS   Bachmann BO, Li R, Townsend CA.
  TITLE     beta-Lactam synthetase: a new biosynthetic enzyme.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 9082-6.
  ORGANISM  Streptomyces clavuligerus
PATHWAY     PATH: map00331  Clavulanic acid biosynthesis
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.3.4
            ExPASy - ENZYME nomenclature database: 6.3.3.4
            ExplorEnz - The Enzyme Database: 6.3.3.4
            ERGO genome analysis and discovery system: 6.3.3.4
            BRENDA, the Enzyme Database: 6.3.3.4
///
ENTRY       EC 6.3.4.1                  Enzyme
NAME        GMP synthase;
            xanthosine-5'-phosphate---ammonia ligase;
            guanylate synthetase;
            XMP aminase;
            xanthosine 5'-monophosphate aminase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     xanthosine-5'-phosphate:ammonia ligase (AMP-forming)
REACTION    ATP + xanthosine 5'-phosphate + NH3 = AMP + diphosphate + GMP
            [RN:R01230]
ALL_REAC    R01230
SUBSTRATE   ATP [CPD:C00002];
            xanthosine 5'-phosphate [CPD:C00655];
            NH3 [CPD:C00014]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            GMP [CPD:C00144]
REFERENCE   1
  AUTHORS   Moyed, H.S. and Magasanik, B.
  TITLE     Enzymes essential for the biosynthesis of nucleic acid guanine;
            xanthosine 5'-phosphate aminase of Aerobacter aerogenes.
  JOURNAL   J. Biol. Chem. 226 (1957) 351-363.
  ORGANISM  Aerobacter aerogenes
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01936  GMP synthase
GENES       PFA: PF10_0123
            ECO: b2507(guaA)
            FTU: FTT1019c(guaA)
            FTF: FTF1019c(guaA)
            FTN: FTN_0897(guaA)
            RHA: RHA1_ro06202(guaA)
            PMB: A9601_00361
            PMC: P9515_00361
            PMF: P9303_00451
            PMG: P9301_00361
            PMH: P9215_00351(guaA)
            PME: NATL1_00351
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.1
            ExPASy - ENZYME nomenclature database: 6.3.4.1
            ExplorEnz - The Enzyme Database: 6.3.4.1
            ERGO genome analysis and discovery system: 6.3.4.1
            BRENDA, the Enzyme Database: 6.3.4.1
            CAS: 9023-55-6
///
ENTRY       EC 6.3.4.2                  Enzyme
NAME        CTP synthase;
            UTP---ammonia ligase;
            cytidine triphosphate synthetase;
            uridine triphosphate aminase;
            cytidine 5'-triphosphate synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     UTP:ammonia ligase (ADP-forming)
REACTION    ATP + UTP + NH3 = ADP + phosphate + CTP [RN:R00571]
ALL_REAC    R00571;
            (other) R00573
SUBSTRATE   ATP [CPD:C00002];
            UTP [CPD:C00075];
            NH3 [CPD:C00014]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            CTP [CPD:C00063]
COMMENT     Glutamine can replace NH3.
REFERENCE   1  [PMID:13367044]
  AUTHORS   LIEBERMAN I.
  TITLE     Enzymatic amination of uridine triphosphate to cytidine
            triphosphate.
  JOURNAL   J. Biol. Chem. 222 (1956) 765-75.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2
  AUTHORS   Long, C.W., Levitzki, A., Houston, L.L and Koshland, D.E., Jr.
  TITLE     Subunit structures and interactions of CTP synthetase.
  JOURNAL   Fed. Proc. 28 (1969) 342.
PATHWAY     PATH: map00240  Pyrimidine metabolism
ORTHOLOGY   KO: K01937  CTP synthase
GENES       HSA: 1503(CTPS) 56474(CTPS2)
            PTR: 469296(CTPS)
            MMU: 51797(Ctps) 55936(Ctps2)
            RNO: 313560(Ctps_predicted)
            CFA: 480851(CTPS2)
            BTA: 506131(CTPS) 767849(CTPS2)
            GGA: 418620(RCJMB04_4c5)
            XLA: 379880(ctps) 444477(MGC81822)
            DRE: 322089(ctps)
            SPU: 575088(LOC575088)
            DME: Dmel_CG6854
            CEL: W06H3.3
            ATH: AT1G30820 AT2G34890 AT3G12670(EMB2742)
            OSA: 4324172 4326656 4339675
            CME: CMP216C
            SCE: YBL039C(URA7) YJR103W(URA8)
            AGO: AGOS_AGL320C
            PIC: PICST_78143(URA7)
            CGR: CAGL0F04433g
            SPO: SPAC10F6.03c
            ANI: AN0490.2
            AFM: AFUA_7G05210
            AOR: AO090026000606
            CNE: CNC00220
            UMA: UM00770.1
            ECU: ECU11_0480 ECU11_0880
            DDI: DDB_0230162
            PFA: PF14_0100
            CPV: cgd5_1710
            CHO: Chro.50211
            TAN: TA15425
            TPV: TP02_0838
            TET: TTHERM_00459390
            TBR: Tb927.1.1240
            TCR: 506479.130 508993.10
            LMA: LmjF20.0560
            ECO: b2780(pyrG)
            ECJ: JW2751(pyrG)
            ECE: Z4095(pyrG)
            ECS: ECs3640
            ECC: c3345(pyrG)
            ECI: UTI89_C3149(pyrG)
            ECP: ECP_2761
            ECV: APECO1_3750(pyrG)
            ECW: EcE24377A_3084(pyrG)
            ECX: EcHS_A2924
            STY: STY3082(pyrG)
            STT: t2854(pyrG)
            SPT: SPA2810(pyrG)
            SEC: SC2887(pyrG)
            STM: STM2953(pyrG)
            YPE: YPO3377(pyrG)
            YPK: y0813(pyrG)
            YPM: YP_0309(pyrG)
            YPA: YPA_2875
            YPN: YPN_0715
            YPP: YPDSF_2982
            YPS: YPTB0754(pyrG)
            YPI: YpsIP31758_3317(pyrG)
            YEN: YE0746(pyrG)
            SFL: SF2795(pyrG)
            SFX: S2989(pyrG)
            SFV: SFV_2675(pyrG)
            SSN: SSON_2937(pyrG)
            SBO: SBO_2661(pyrG)
            SDY: SDY_2997(pyrG)
            ECA: ECA3567(pyrG)
            PLU: plu0912(pyrG)
            BUC: BU416(pyrG)
            BAS: BUsg399(pyrG)
            BAB: bbp376(pyrG)
            WBR: WGLp354(pyrG)
            SGL: SG0512
            ENT: Ent638_1664 Ent638_3234
            SPE: Spro_0794 Spro_4426
            BFL: Bfl156(pyrG)
            BPN: BPEN_161(pyrG)
            HIN: HI1077(pyrG)
            HIT: NTHI1238(pyrG)
            HIP: CGSHiEE_06720
            HIQ: CGSHiGG_09040
            HDU: HD0373(pyrG)
            HSO: HS_0552(pyrG)
            PMU: PM1872(pyrG)
            MSU: MS0255(pyrG)
            APL: APL_0136(pyrG)
            ASU: Asuc_2052
            XFA: XF1288
            XFT: PD0541(pyrG)
            XCC: XCC1697(pyrG)
            XCB: XC_2534
            XCV: XCV1749(pyrG)
            XAC: XAC1716(pyrG)
            XOO: XOO2967(pyrG)
            XOM: XOO_2817(XOO2817)
            VCH: VC2448
            VCO: VC0395_A2026(pyrG)
            VVU: VV1_1578
            VVY: VV2819
            VPA: VP2562
            VFI: VF2076
            PPR: PBPRA3080
            PAE: PA3637(pyrG)
            PAU: PA14_17290(pyrG)
            PAP: PSPA7_1502(pyrG)
            PPU: PP_1610(pyrG)
            PPF: Pput_4167
            PST: PSPTO_1552(pyrG)
            PSB: Psyr_1361
            PSP: PSPPH_3822(pyrG)
            PFL: PFL_1194(pyrG)
            PFO: Pfl_1119
            PEN: PSEEN4202(pyrG)
            PMY: Pmen_3035
            PAR: Psyc_1641(pyrG)
            PCR: Pcryo_1875
            PRW: PsycPRwf_1670
            ACI: ACIAD2003(pyrG)
            SON: SO_3441(pyrG)
            SDN: Sden_1195
            SFR: Sfri_1051
            SAZ: Sama_1035
            SBL: Sbal_3128
            SBM: Shew185_3137
            SLO: Shew_1204
            SPC: Sputcn32_2758
            SSE: Ssed_1289
            SPL: Spea_1184
            SHE: Shewmr4_1114
            SHM: Shewmr7_1185
            SHN: Shewana3_1115
            SHW: Sputw3181_1254
            ILO: IL0773(pyrG)
            CPS: CPS_4108(pyrG)
            PHA: PSHAa0741(pyrG)
            PAT: Patl_3265
            SDE: Sde_1243
            PIN: Ping_0668
            MAQ: Maqu_0919
            CBU: CBU_1682(pyrG)
            CBD: COXBU7E912_0320(pyrG)
            LPN: lpg1181(pyrG)
            LPF: lpl1190(pyrG)
            LPP: lpp1184(pyrG)
            MCA: MCA2513(pyrG)
            FTU: FTT0374c(pyrG)
            FTF: FTF0374c(pyrG)
            FTW: FTW_1708(pyrG)
            FTL: FTL_1311
            FTH: FTH_1283(pyrG)
            FTA: FTA_1386(pyrG)
            FTN: FTN_0270(pyrG)
            TCX: Tcr_1262
            NOC: Noc_0850
            AEH: Mlg_1841
            HHA: Hhal_1439
            HCH: HCH_01865(pyrG)
            CSA: Csal_0617
            ABO: ABO_1162(pyrG)
            MMW: Mmwyl1_1298
            AHA: AHA_0820(pyrG)
            DNO: DNO_0360(pyrG)
            BCI: BCI_0222(pyrG)
            RMA: Rmag_0674
            VOK: COSY_0621(pyrG)
            NME: NMB1554
            NMA: NMA1742(pyrG)
            NMC: NMC1471(pyrG)
            NGO: NGO1212
            CVI: CV_3457(pyrG)
            RSO: RSc1126(pyrG)
            REU: Reut_A1088
            RME: Rmet_1052
            BMA: BMA1691(pyrG)
            BMV: BMASAVP1_A2195(pyrG)
            BML: BMA10299_A3123(pyrG)
            BMN: BMA10247_1468(pyrG)
            BXE: Bxe_A1571
            BVI: Bcep1808_2188
            BUR: Bcep18194_A5415
            BCN: Bcen_5968
            BCH: Bcen2424_2109
            BAM: Bamb_2146
            BPS: BPSL2272(pyrG)
            BPM: BURPS1710b_2713(pyrG)
            BPL: BURPS1106A_2633(pyrG)
            BPD: BURPS668_2579(pyrG)
            BTE: BTH_I1892(pyrG)
            PNU: Pnuc_0945
            BPE: BP2389(pyrG)
            BPA: BPP3255(pyrG)
            BBR: BB3706(pyrG)
            RFR: Rfer_2648
            POL: Bpro_3181
            PNA: Pnap_1185
            AAV: Aave_1327
            AJS: Ajs_1000
            VEI: Veis_2653
            MPT: Mpe_A2845 Mpe_B0218
            HAR: HEAR2189(pyrG)
            MMS: mma_1269
            NEU: NE1045(pyrG)
            NET: Neut_2483
            NMU: Nmul_A1227
            EBA: ebA6159(pyrG)
            AZO: azo2146(pyrG)
            DAR: Daro_2366
            TBD: Tbd_0619
            MFA: Mfla_1911
            HPY: HP0349
            HPA: HPAG1_0344
            HHE: HH1350(pyrG)
            HAC: Hac_0973(pyrG)
            WSU: WS0224(pyrG)
            TDN: Tmden_2080
            CJE: Cj0027(pyrG)
            CJR: CJE0027(pyrG)
            CJJ: CJJ81176_0054(pyrG)
            CJU: C8J_0026(pyrG)
            CJD: JJD26997_0029(pyrG)
            CFF: CFF8240_1754(pyrG)
            CCV: CCV52592_2084(pyrG)
            CHA: CHAB381_0134(pyrG)
            CCO: CCC13826_0908(pyrG)
            ABU: Abu_2257(pyrG)
            NIS: NIS_0156(pyrG)
            SUN: SUN_0003(pyrG)
            GSU: GSU1895(pyrG)
            GME: Gmet_1276
            GUR: Gura_2979
            PCA: Pcar_1945
            PPD: Ppro_1614
            DVU: DVU1623(pyrG)
            DVL: Dvul_1511
            DDE: Dde_1765
            LIP: LI0451(pyrG)
            BBA: Bd0808(pyrG)
            DPS: DP0766
            ADE: Adeh_4174
            AFW: Anae109_4318
            MXA: MXAN_1096(pyrG)
            SAT: SYN_02922
            SFU: Sfum_2075
            RPR: RP378(pyrG)
            RTY: RT0367(pyrG)
            RCO: RC0523(pyrG)
            RFE: RF_0593(pyrG)
            RBE: RBE_0989(pyrG)
            RAK: A1C_02835 A1C_02845
            RBO: A1I_03710
            RRI: A1G_02970
            WOL: WD0468(pyrG)
            WBM: Wbm0169
            AMA: AM018(pyrG)
            APH: APH_0038(pyrG)
            ERU: Erum1160(pyrG)
            ERW: ERWE_CDS_01130(pyrG)
            ERG: ERGA_CDS_01090(pyrG)
            ECN: Ecaj_0114
            ECH: ECH_0171(pyrG)
            NSE: NSE_0877(pyrG)
            PUB: SAR11_0937(pyrG)
            MLO: mll0606
            MES: Meso_1634
            PLA: Plav_3156
            SME: SMc01025(pyrG)
            SMD: Smed_1069
            ATU: Atu1618(pyrG)
            ATC: AGR_C_2984
            RET: RHE_CH02184(pyrG)
            RLE: RL2511(pyrG)
            BME: BMEI0849
            BMF: BAB1_1157(pyrG)
            BMS: BR1134(pyrG)
            BMB: BruAb1_1140(pyrG)
            BOV: BOV_1094(pyrG)
            OAN: Oant_2054
            BJA: bll4805(pyrG)
            BRA: BRADO4103(pyrG)
            BBT: BBta_4476(pyrG)
            RPA: RPA2886(pyrG)
            RPB: RPB_2790
            RPC: RPC_2473
            RPD: RPD_2824
            RPE: RPE_2595
            NWI: Nwi_1833
            NHA: Nham_1738
            BHE: BH05700(pyrG)
            BQU: BQ04860(pyrG)
            BBK: BARBAKC583_0530(pyrG)
            XAU: Xaut_4200
            CCR: CC_1720
            SIL: SPO1312(pyrG)
            SIT: TM1040_1973
            RSP: RSP_0368
            RSH: Rsph17029_2012
            RSQ: Rsph17025_0873
            JAN: Jann_3181
            RDE: RD1_1906(pyrG)
            PDE: Pden_3711
            MMR: Mmar10_1408
            HNE: HNE_1794(pyrG)
            ZMO: ZMO0462(pyrG)
            NAR: Saro_2017
            SAL: Sala_1170
            SWI: Swit_2348
            ELI: ELI_06460
            GOX: GOX2282
            GBE: GbCGDNIH1_0828
            ACR: Acry_1238
            RRU: Rru_A1887
            MAG: amb1821
            MGM: Mmc1_1557
            ABA: Acid345_2856 Acid345_3670
            SUS: Acid_1187 Acid_6215
            BSU: BG10410(pyrG)
            BHA: BH3792(ctrA)
            BAN: BA5583(ctrA)
            BAR: GBAA5583(ctrA)
            BAA: BA_0439
            BAT: BAS5187
            BCE: BC5338
            BCA: BCE_5468(ctrA)
            BCZ: BCZK5038(ctrA)
            BCY: Bcer98_3859
            BTK: BT9727_5022(ctrA)
            BTL: BALH_4836(ctrA)
            BLI: BL03966(pyrG)
            BLD: BLi03963(pyrG)
            BCL: ABC3886(pyrG)
            BAY: RBAM_034310
            BPU: BPUM_3360
            OIH: OB3007
            GKA: GK3389
            GTN: GTNG_3334(ctrA)
            SAU: SA1929(ctrA)
            SAV: SAV2127(pyrG)
            SAM: MW2051(ctrA)
            SAR: SAR2215(pyrG)
            SAS: SAS2030
            SAC: SACOL2119(pyrG)
            SAB: SAB2011c(pyrG)
            SAA: SAUSA300_2081(pyrG)
            SAO: SAOUHSC_02368
            SAJ: SaurJH9_2163
            SAH: SaurJH1_2201
            SEP: SE1725
            SER: SERP1734(pyrG)
            SHA: SH0908(ctrA)
            SSP: SSP0758
            LMO: lmo2559(pyrG)
            LMF: LMOf2365_2531(pyrG)
            LIN: lin2704(pyrG)
            LWE: lwe2509(pyrG)
            LLA: L88252(pyrG)
            LLC: LACR_0497
            LLM: llmg_0467(pyrG)
            SPY: SPy_1894(pyrG)
            SPZ: M5005_Spy_1609 M5005_Spy_1610(pyrG)
            SPM: spyM18_1959(pyrG)
            SPG: SpyM3_1632(pyrG)
            SPS: SPs0234
            SPH: MGAS10270_Spy1678(pyrG)
            SPI: MGAS10750_Spy1665(pyrG)
            SPJ: MGAS2096_Spy1633(pyrG)
            SPK: MGAS9429_Spy1613(pyrG)
            SPF: SpyM50244(pyrG)
            SPA: M6_Spy1618
            SPB: M28_Spy1599(pyrG)
            SPN: SP_0494
            SPR: spr0438(pyrG)
            SPD: SPD_0442(pyrG)
            SAG: SAG0107(pyrG)
            SAN: gbs0106
            SAK: SAK_0157(pyrG)
            SMU: SMU.97(pyrG)
            STC: str0134(pyrG)
            STL: stu0134(pyrG)
            STE: STER_0193
            SSA: SSA_1994(pyrG)
            SSU: SSU05_0335
            SSV: SSU98_0329
            SGO: SGO_1748(pyrG)
            LPL: lp_0481(pyrG)
            LJO: LJ0224
            LAC: LBA0233
            LSA: LSA1629(pyrG)
            LSL: LSL_0342(pyrG)
            LDB: Ldb0354(pyrG)
            LBU: LBUL_0309
            LBR: LVIS_0487
            LCA: LSEI_2571
            LGA: LGAS_0226
            LRE: Lreu_0230
            PPE: PEPE_1571
            EFA: EF1147(pyrG)
            OOE: OEOE_1786
            LME: LEUM_0519
            STH: STH40
            CAC: CAC2892(ctrA)
            CPE: CPE2208(ctrA)
            CPF: CPF_2472(pyrG)
            CPR: CPR_2182(pyrG)
            CNO: NT01CX_0555(pyrG)
            CTH: Cthe_1923
            CBO: CBO0132(pyrG)
            CBA: CLB_0168(pyrG)
            CBH: CLC_0180(pyrG)
            CBF: CLI_0187(pyrG)
            CBE: Cbei_0398
            CKL: CKL_3715(pyrG)
            AMT: Amet_0183
            CHY: CHY_0125(pyrG)
            DSY: DSY4944
            DRM: Dred_3181
            PTH: PTH_2843(pyrG)
            SWO: Swol_2418
            CSC: Csac_2561
            TTE: TTE2609(pyrG)
            MTA: Moth_2409
            MPU: MYPU_6660(pyrG)
            MPE: MYPE520(pyrG)
            MGA: MGA_0953(pyrG)
            MMY: MSC_0134(ctrA) MSC_0902(pyrG)
            MMO: MMOB4080(pyrG)
            MHY: mhp100(pyrG)
            MHJ: MHJ_0272(pyrG)
            MHP: MHP7448_0280(pyrG)
            MCP: MCAP_0133(pyrG)
            UUR: UU284(pyrG)
            POY: PAM611(pyrG)
            AYW: AYWB_122(pyrG)
            MFL: Mfl648
            MTU: Rv1699(pyrG)
            MTC: MT1738(pyrG)
            MBO: Mb1725(pyrG)
            MBB: BCG_1737(pyrG)
            MLE: ML1363(pyrG)
            MPA: MAP1406(pyrG)
            MAV: MAV_3072(pyrG)
            MSM: MSMEG_3746(pyrG)
            MVA: Mvan_3283
            MGI: Mflv_3502
            MMC: Mmcs_2944
            MKM: Mkms_2988
            MJL: Mjls_2959
            CGL: NCgl1362(cgl1417)
            CGB: cg1606(pyrG)
            CEF: CE1551
            CJK: jk0871(pyrG)
            NFA: nfa20050(pyrG)
            RHA: RHA1_ro00931
            SCO: SCO1776(pyrG)
            SMA: SAV6504(pyrG)
            TWH: TWT100(pyrG)
            TWS: TW110(pyrG)
            LXX: Lxx05650(pyrG)
            CMI: CMM_1983(pyrG)
            ART: Arth_1519
            AAU: AAur_1655(pyrG)
            PAC: PPA1390
            NCA: Noca_2485
            TFU: Tfu_1199
            FRA: Francci3_3157
            FAL: FRAAL5179(pyrG) FRAAL6788
            ACE: Acel_1243
            KRA: Krad_3141
            SEN: SACE_5244(pyrG)
            STP: Strop_1920
            BLO: BL0874(pyrG)
            BAD: BAD_0709(pyrG)
            RXY: Rxyl_1448
            RBA: RB12061(pyrG)
            CTR: CT183(pyrG)
            CTA: CTA_0201(pyrG)
            CMU: TC0455
            CPN: CPn0236(pyrG)
            CPA: CP0526
            CPJ: CPj0236(pyrG)
            CPT: CpB0242
            CCA: CCA00597(pyrG)
            CAB: CAB570(ctrA)
            CFE: CF0407(pyrG)
            PCU: pc0824(pyrG)
            BGA: BG0586(pyrG)
            BAF: BAPKO_0606(pyrG)
            TPA: TP0305
            TDE: TDE2692(pyrG)
            LIL: LA2409(pyrG)
            LIC: LIC11540(pyrG)
            LBJ: LBJ_1451(pyrG)
            LBL: LBL_1675(pyrG)
            SYN: sll1443(pyrG)
            SYW: SYNW2428(pyrG)
            SYC: syc2140_d(pyrG)
            SYF: Synpcc7942_1954
            SYD: Syncc9605_2598
            SYE: Syncc9902_2235
            SYG: sync_2858(pyrG)
            SYR: SynRCC307_2442(pyrG)
            SYX: SynWH7803_2461(pyrG)
            CYA: CYA_1479(pyrG)
            CYB: CYB_1478(pyrG)
            TEL: tll0768(pyrG)
            GVI: glr1524(pyrG)
            ANA: alr5000
            AVA: Ava_2267
            PMA: Pro1853(pyrG)
            PMM: PMM1689(pyrG)
            PMT: PMT2219(pyrG)
            PMN: PMN2A_1291
            PMI: PMT9312_1782
            PMB: A9601_18991(pyrG)
            PMC: P9515_18801(pyrG)
            PMF: P9303_29581(pyrG)
            PMG: P9301_18801(pyrG)
            PMH: P9215_19621
            PME: NATL1_21631(pyrG)
            TER: Tery_2872
            BTH: BT_0590
            BFR: BF2602
            BFS: BF2624(pyrG)
            PGI: PG0525(pyrG)
            SRU: SRU_0550(pyrG)
            CHU: CHU_2536(pyrG)
            GFO: GFO_2218(pyrG)
            FJO: Fjoh_2383
            FPS: FP1899(pyrG)
            CTE: CT0142(pyrG)
            CCH: Cag_0090
            CPH: Cpha266_2661
            PVI: Cvib_0173
            PLT: Plut_0100
            DET: DET1410(pyrG)
            DEH: cbdb_A1371(pyrG)
            DEB: DehaBAV1_1217
            RRS: RoseRS_3115
            RCA: Rcas_2963
            DRA: DR_1573
            DGE: Dgeo_0827
            TTH: TTC1102
            TTJ: TTHA1466
            AAE: aq_1334(pyrG)
            TMA: TM0803
            TPT: Tpet_0125
            TME: Tmel_0784
            FNO: Fnod_0197
            MMP: MMP0893(pyrG)
            MMQ: MmarC5_0701
            MMZ: MmarC7_0141
            MAE: Maeo_0174
            MVN: Mevan_0028
            MAC: MA3279(pyrG)
            MBA: Mbar_A3518
            MMA: MM_0118
            MBU: Mbur_1282
            MTP: Mthe_0862
            MHU: Mhun_2528
            MLA: Mlab_1182
            MEM: Memar_1899
            MBN: Mboo_2140
            MTH: MTH419
            MST: Msp_0453(pyrG)
            MSI: Msm_0147
            MKA: MK0205(pyrG)
            AFU: AF0252(pyrG)
            HAL: VNG1830G(pyrG)
            HMA: rrnAC3471(pyrG)
            HWA: HQ3195A(pyrG)
            NPH: NP1968A(pyrG)
            TAC: Ta0044m
            TVO: TVN0033
            PTO: PTO0560
            PHO: PH1792
            PAB: PAB0231(pyrG)
            PFU: PF1839
            TKO: TK1193
            RCI: RCIX1748(pyrG)
            APE: APE_1604
            SMR: Smar_0604
            IHO: Igni_0331
            HBU: Hbut_0114
            SSO: SSO0201(pyrG)
            STO: ST0237
            SAI: Saci_0801(pyrG)
            MSE: Msed_0228
            PAI: PAE3518(pyrG)
            PIS: Pisl_0799
            PCL: Pcal_1984
            PAS: Pars_1955
            TPE: Tpen_1163
STRUCTURES  PDB: 1S1M  1VCM  1VCN  1VCO  2AD5  2C5M  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.2
            ExPASy - ENZYME nomenclature database: 6.3.4.2
            ExplorEnz - The Enzyme Database: 6.3.4.2
            ERGO genome analysis and discovery system: 6.3.4.2
            BRENDA, the Enzyme Database: 6.3.4.2
            CAS: 9023-56-7
///
ENTRY       EC 6.3.4.3                  Enzyme
NAME        formate---tetrahydrofolate ligase;
            formyltetrahydrofolate synthetase;
            10-formyltetrahydrofolate synthetase;
            tetrahydrofolic formylase;
            tetrahydrofolate formylase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     formate:tetrahydrofolate ligase (ADP-forming)
REACTION    ATP + formate + tetrahydrofolate = ADP + phosphate +
            10-formyltetrahydrofolate [RN:R00943]
ALL_REAC    R00943;
            (other) R01655
SUBSTRATE   ATP [CPD:C00002];
            formate [CPD:C00058];
            tetrahydrofolate [CPD:C00101]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            10-formyltetrahydrofolate [CPD:C00234]
COMMENT     In eukaryotes occurs as a trifunctional enzyme also having
            methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5) and
            methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) activity.
REFERENCE   1  [PMID:13789141]
  AUTHORS   JAENICKE L, BRODE E.
  TITLE     [Research on monocarbon compounds. I. The tetrahydrofolate formylase
            from pigeon liver. Purification and mechanism.]
  JOURNAL   Biochem. Z. 334 (1961) 108-32.
REFERENCE   2
  AUTHORS   Long, C.W., Levitzki, A., Houston, L.L and Koshland, D.E., Jr.
  TITLE     Subunit structures and interactions of CTP synthetase.
  JOURNAL   Fed. Proc. 28 (1969) 342.
REFERENCE   3  [PMID:14489619]
  AUTHORS   RABINOWITZ JC, PRICER WE Jr.
  TITLE     Formyltetrahydrofolate synthetase. I. Isolation and crystallization
            of the enzyme.
  JOURNAL   J. Biol. Chem. 237 (1962) 2898-902.
  ORGANISM  Micrococcus aerogenes, pigeon, Clostridium cylindrosporum,
            Clostridium acidi-urici
REFERENCE   4
  AUTHORS   Whiteley, H.R., Osborn, M.J. and Huennekens, F.M.
  TITLE     Purification and properties of the formate-activating enzyme from
            Micrococcus aerogenes.
  JOURNAL   J. Biol. Chem. 234 (1959) 1538-1543.
  ORGANISM  Micrococcus aerogenes
PATHWAY     PATH: map00630  Glyoxylate and dicarboxylate metabolism
            PATH: map00670  One carbon pool by folate
ORTHOLOGY   KO: K01938  formate--tetrahydrofolate ligase
GENES       HSA: 25902(MTHFD1L) 4522(MTHFD1)
            MMU: 108156(Mthfd1) 270685(Mthfd1l)
            RNO: 64300(Mthfd1)
            CFA: 476245(MTHFD1L)
            GGA: 423508(RCJMB04_29j22)
            XLA: 380266(mthfd1)
            XTR: 493369(TNeu036b14.1)
            DRE: 260441(mthfd1)
            SPU: 589933(LOC589933)
            DME: Dmel_CG4067(pug)
            ATH: AT1G50480(THFS)
            OSA: 4347204
            CME: CMJ099C
            SCE: YBR084W(MIS1) YGR204W(ADE3)
            AGO: AGOS_ACL121C AGOS_AER178W
            PIC: PICST_80013(MIS1) PICST_88119(ADE3)
            CAL: CaO19_7534(CaO19.7534)
            CGR: CAGL0K00913g CAGL0M01694g
            SPO: SPBC2G2.08 SPBC839.16
            AFM: AFUA_3G08650
            CNE: CNG00590
            UMA: UM03320.1
            DDI: DDB_0230114(fthS)
            TCR: 508207.240 509509.20 511517.60 511741.50
            LMA: LmjF30.2600
            ECI: UTI89_C2351(yegO)
            YEN: YE1997
            HDU: HD1282(fhs)
            APL: APL_0466(fhs)
            VCH: VCA0614
            VCO: VC0395_0556(fhs)
            VVU: VV2_0216 VV2_0217
            VVY: VVA0722
            VPA: VPA0834
            VFI: VF1793
            PPR: PBPRA2764(fhs)
            PRW: PsycPRwf_2355
            SON: SO_0560(fhs)
            SAZ: Sama_3146
            SBL: Sbal_0520
            SBM: Shew185_3804
            SLO: Shew_0443
            SPC: Sputcn32_3314
            SSE: Ssed_0612
            SPL: Spea_3720
            SHE: Shewmr4_0561
            SHM: Shewmr7_3469
            SHN: Shewana3_0560
            SHW: Sputw3181_0627
            MCA: MCA2219(fhs)
            AHA: AHA_1604(fhs)
            NME: NMB1839
            NMA: NMA0617(fhs)
            NMC: NMC0378(fhs)
            NGO: NGO0062
            MPT: Mpe_A3264
            MFA: Mfla_2254
            CCV: CCV52592_0358(fhs)
            LIP: LI0874
            DPS: DP2227
            MXA: MXAN_0175(fhs)
            SAT: SYN_02008
            SFU: Sfum_2687
            PUB: SAR11_1285(fhs)
            MLO: mlr2763
            MES: Meso_2204
            SME: SMc02728(fhs)
            SMD: Smed_2298
            RET: RHE_CH03078(fhs)
            RLE: RL3525(fhs)
            XAU: Xaut_1383
            SIL: SPO1557(fhs-1) SPO3103(fhs-2)
            SIT: TM1040_2358
            RSP: RSP_0663
            RSH: Rsph17029_2316
            RSQ: Rsph17025_0569
            JAN: Jann_0981
            RDE: RD1_4235(fhs)
            PDE: Pden_1317 Pden_1580
            MMR: Mmar10_1412
            HNE: HNE_3316(fhs)
            ZMO: ZMO0454(fhs)
            GBE: GbCGDNIH1_0047
            ACR: Acry_2767
            BAN: BA2107(fhs)
            BAR: GBAA2107(fhs)
            BAA: BA_2602
            BAT: BAS1959
            BCE: BC2101
            BCA: BCE_2187(fhs)
            BCZ: BCZK1914(fhs)
            BCY: Bcer98_1593
            BTK: BT9727_1938(fhs)
            BTL: BALH_1871
            BLI: BL01370
            BLD: BLi02328
            BPU: BPUM_1926(fhs)
            SAU: SA1553(fhs)
            SAV: SAV1732(fhs)
            SAM: MW1675(fhs)
            SAR: SAR1810(fhs)
            SAS: SAS1658
            SAC: SACOL1782(fhs)
            SAB: SAB1592c(fhs)
            SAA: SAUSA300_1678(fhs)
            SAO: SAOUHSC_01845
            SAJ: SaurJH9_1787
            SAH: SaurJH1_1822
            SEP: SE1408
            SER: SERP1295(fhs)
            SHA: SH1190(fhs)
            SSP: SSP1031 SSP1032
            LMO: lmo1877
            LMF: LMOf2365_1906(fhs)
            LIN: lin1990
            LWE: lwe1896(fhs)
            LLA: L159505(fhs)
            LLC: LACR_1007
            LLM: llmg_1595(fhs)
            SPY: SPy_1213(fhs.1) SPy_2085(fhs.2)
            SPZ: M5005_Spy_0927(fhs.1) M5005_Spy_1774(fhs.2)
            SPM: spyM18_1165(fhs) spyM18_2144
            SPG: SpyM3_0853(fhs.1) SpyM3_1776(fhs.2)
            SPS: SPs1053 SPs1773
            SPH: MGAS10270_Spy1041(fhs1) MGAS10270_Spy1840(fhs2)
            SPI: MGAS10750_Spy1076(fhs1) MGAS10750_Spy1866(fhs2)
            SPJ: MGAS2096_Spy0986(fhs1) MGAS2096_Spy1807(fhs2)
            SPK: MGAS9429_Spy1030(fhs1) MGAS9429_Spy1785(fhs2)
            SPF: SpyM50871(fhs1) SpyM51732(fhs2)
            SPA: M6_Spy0916 M6_Spy1771
            SPB: M28_Spy0899(fhs.1) M28_Spy1758(fhs.2)
            SPN: SP_1229
            SPR: spr1109(fhs)
            SPD: SPD_1087(fhs)
            SAG: SAG1055(fhs)
            SAN: gbs1089
            SAK: SAK_1144(fhs)
            SMU: SMU.1073(fthS)
            STC: str0791(fhs)
            STL: stu0791(fhs)
            SSA: SSA_0432 SSA_1200(fhs)
            SGO: SGO_1210(fhs-1) SGO_1808(fhs-2)
            LPL: lp_1779(fhs)
            LJO: LJ1188
            LAC: LBA1153(purU) LBA1562
            LSA: LSA0947(fhs)
            LSL: LSL_0842(fhs)
            LDB: Ldb1020(fhs)
            LBU: LBUL_0928
            LBR: LVIS_0834 LVIS_0978
            LCA: LSEI_1460
            LRE: Lreu_0131
            EFA: EF1725(fhs)
            OOE: OEOE_0769
            STH: STH3189
            CAC: CAC3201
            CPE: CPE2469
            CPF: CPF_2785(fhs)
            CPR: CPR_2471(fhs)
            CTC: CTC02304
            CNO: NT01CX_1042
            CTH: Cthe_2399
            CDF: CD0718(fhs)
            CBO: CBO3523(fhs)
            CBA: CLB_3598(fhs)
            CBH: CLC_3487(fhs)
            CBF: CLI_3732(fhs)
            CBE: Cbei_0101
            CKL: CKL_0440(fhs)
            AMT: Amet_2018 Amet_4585
            CHY: CHY_2385(fhs)
            DSY: DSY0205 DSY0605
            DRM: Dred_0129
            SWO: Swol_1409
            CSC: Csac_1224
            TTE: TTE2391(mIS1)
            MTA: Moth_0109
            MPE: MYPE8690
            UUR: UU221(fthS)
            CDI: DIP1253(fhs)
            CJK: jk0881(fhs)
            ART: Arth_2901
            AAU: AAur_2892(fhs)
            PAC: PPA0049
            NCA: Noca_4561
            SEN: SACE_5619(fhs)
            BLO: BL0478(fhs)
            BAD: BAD_0169(fhs)
            RXY: Rxyl_0766 Rxyl_1568 Rxyl_2519
            FNU: FN2082
            TDE: TDE0019(fhs)
            BTH: BT_0737
            BFR: BF2202
            BFS: BF2256(fhs)
            PGI: PG1321(fhs)
            DET: DET0671(fhs-1) DET0705(fhs-2)
            DEH: cbdb_A660(fhs)
            DEB: DehaBAV1_0640
            RRS: RoseRS_0219
            RCA: Rcas_0522
            TTH: TTC1707
            TMA: TM1766
            TPT: Tpet_1054
            TME: Tmel_0304
            FNO: Fnod_1079
            HMA: pNG7380(fhs)
            HWA: HQ1768A(fhs)
            TAC: Ta1478
            TVO: TVN0089
            PTO: PTO1244
STRUCTURES  PDB: 1EG7  1FP7  1FPM  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.3
            ExPASy - ENZYME nomenclature database: 6.3.4.3
            ExplorEnz - The Enzyme Database: 6.3.4.3
            ERGO genome analysis and discovery system: 6.3.4.3
            BRENDA, the Enzyme Database: 6.3.4.3
            CAS: 9023-66-9
///
ENTRY       EC 6.3.4.4                  Enzyme
NAME        adenylosuccinate synthase;
            IMP---aspartate ligase;
            adenylosuccinate synthetase;
            succinoadenylic kinosynthetase;
            succino-AMP synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     IMP:L-aspartate ligase (GDP-forming)
REACTION    GTP + IMP + L-aspartate = GDP + phosphate +
            N6-(1,2-dicarboxyethyl)-AMP [RN:R01135]
ALL_REAC    R01135
SUBSTRATE   GTP [CPD:C00044];
            IMP [CPD:C00130];
            L-aspartate [CPD:C00049]
PRODUCT     GDP [CPD:C00035];
            phosphate [CPD:C00009];
            N6-(1,2-dicarboxyethyl)-AMP [CPD:C03794]
REFERENCE   1  [PMID:13644270]
  AUTHORS   DAVEY CL.
  TITLE     Synthesis of adenylosuccinic acid in preparations of mammalian
            skeletal muscle.
  JOURNAL   Nature. 183 (1959) 995-6.
  ORGANISM  rabbit
REFERENCE   2  [PMID:13376602]
  AUTHORS   LIEBERMAN I.
  TITLE     Enzymatic synthesis of adenosine-5'-phosphate from
            inosine-5'-phosphate.
  JOURNAL   J. Biol. Chem. 223 (1956) 327-39.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:13662023]
  AUTHORS   YEFIMOCHKINA EF, BRAUNSTEIN AE.
  TITLE     The amination of inosinic acid to adenylic acid in muscle extracts.
  JOURNAL   Arch. Biochem. Biophys. 83 (1959) 350-2.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00252  Alanine and aspartate metabolism
ORTHOLOGY   KO: K01939  adenylosuccinate synthase
GENES       HSA: 122622(ADSSL1) 159(ADSS)
            PTR: 467568(ADSSL1)
            MMU: 11565(Adssl1) 11566(Adss)
            CFA: 480098(ADSS)
            GGA: 428579(RCJMB04_17e23) 776127(ADSSL1)
            XLA: 379780(adss) 447329(MGC82806)
            XTR: 394644(adss) 448339(MGC89175)
            DRE: 192305(adss) 407989(zgc:85738)
            SPU: 582026(LOC582026)
            DME: Dmel_CG17273
            CEL: C37H5.6
            OSA: 4331792 4333815
            CME: CMM162C
            SCE: YNL220W(ADE12)
            AGO: AGOS_ABL186W
            PIC: PICST_85387
            CGR: CAGL0K05027g
            SPO: SPAC144.03(ade2)
            ANI: AN0893.2
            AFM: AFUA_1G15450
            AOR: AO090005001150
            CNE: CNC04750
            UMA: UM03851.1
            DDI: DDB_0201565(purA)
            PFA: PF13_0287
            TAN: TA17235
            TPV: TP04_0033
            TET: TTHERM_00773690
            TBR: Tb11.02.1120
            TCR: 508731.60 509683.80
            LMA: LmjF13.1190
            ECO: b4177(purA)
            ECJ: JW4135(purA)
            ECE: Z5784(purA)
            ECS: ECs5153
            ECC: c5261(purA)
            ECI: UTI89_C4777(purA)
            ECP: ECP_4422
            ECV: APECO1_2215(purA)
            ECW: EcE24377A_4736(purA)
            ECX: EcHS_A4420
            STY: STY4723(purA)
            STT: t4417(purA)
            SPT: SPA4183(purA)
            SEC: SC4242(purA)
            STM: STM4366(purA)
            YPE: YPO0378(purA)
            YPK: y0635(purA)
            YPM: YP_0534(purA)
            YPA: YPA_3906
            YPN: YPN_3293
            YPP: YPDSF_3596
            YPS: YPTB0430(purA)
            YPI: YpsIP31758_3648(purA)
            YEN: YE0382(adeK)
            SFL: SF4332(purA)
            SFX: S4600(purA)
            SFV: SFV_4335(purA)
            SSN: SSON_4362(purA)
            SBO: SBO_4279(purA)
            SDY: SDY_4412(purA)
            ECA: ECA3929(purA)
            PLU: plu4577(purA)
            BUC: BU566(purA)
            BAS: BUsg546(purA)
            BAB: bbp511(purA)
            WBR: WGLp179(purA)
            SGL: SG0342
            ENT: Ent638_0360
            SPE: Spro_0436
            BFL: Bfl083(purA)
            BPN: BPEN_086(purA)
            HIN: HI1633(purA)
            HIT: NTHI1407(purA)
            HIP: CGSHiEE_05830
            HIQ: CGSHiGG_09930
            HDU: HD1807(purA)
            HSO: HS_1328(purA)
            PMU: PM0938(purA)
            MSU: MS1621(purA)
            APL: APL_1075(purA)
            ASU: Asuc_1830
            XFA: XF0455
            XFT: PD1627(purA)
            XCC: XCC1053(purA)
            XCB: XC_3193
            XCV: XCV1178(purA)
            XAC: XAC1158(purA)
            XOO: XOO0915(purA)
            XOM: XOO_0840(XOO0840)
            VCH: VC2602
            VCO: VC0395_A2180(purA)
            VVU: VV1_1299 VV2_0768
            VVY: VV3066 VVA1235
            VPA: VP2812 VPA0375
            VFI: VF1062 VF2318
            PPR: PBPRA3345 PBPRB1785 PBPRB1786
            PAE: PA4938(purA)
            PAU: PA14_65230(purA)
            PAP: PSPA7_5667(purA)
            PPU: PP_4889(purA)
            PPF: Pput_4765
            PST: PSPTO_4937(purA)
            PSB: Psyr_0577(purA)
            PSP: PSPPH_0570(purA)
            PFL: PFL_0571(purA)
            PFO: Pfl_0528
            PEN: PSEEN4938(purA)
            PMY: Pmen_0641
            PAR: Psyc_0677(purA)
            PCR: Pcryo_0645
            PRW: PsycPRwf_1810
            ACI: ACIAD1258(purA)
            SON: SO_1258 SO_3937(purA)
            SDN: Sden_0509
            SFR: Sfri_3357
            SAZ: Sama_3069
            SBL: Sbal_3193 Sbal_3649
            SBM: Shew185_0705 Shew185_3187
            SLO: Shew_3291
            SPC: Sputcn32_0747 Sputcn32_2797
            SSE: Ssed_0750 Ssed_2259
            SPL: Spea_3592
            SHE: Shewmr4_1068 Shewmr4_3266
            SHM: Shewmr7_0681 Shewmr7_1140
            SHN: Shewana3_0695 Shewana3_1072
            SHW: Sputw3181_1215 Sputw3181_3428
            ILO: IL0337(purA)
            CPS: CPS_0330(purA)
            PHA: PSHAa0275(purA) PSHAa1943
            PAT: Patl_0215
            SDE: Sde_2661
            PIN: Ping_3234
            MAQ: Maqu_2764
            CBU: CBU_0998(purA)
            CBD: COXBU7E912_1049(purA)
            LPN: lpg0486(purA)
            LPF: lpl0526(purA)
            LPP: lpp0550(purA)
            MCA: MCA1978(purA)
            FTU: FTT0204(purA)
            FTF: FTF0204(purA)
            FTW: FTW_1884(purA)
            FTL: FTL_1930
            FTH: FTH_1850(purA)
            FTA: FTA_2039(purA)
            FTN: FTN_0178(purA)
            TCX: Tcr_1094
            NOC: Noc_2585
            AEH: Mlg_0578
            HHA: Hhal_0660
            HCH: HCH_05377(purA)
            CSA: Csal_1282
            ABO: ABO_2197(purA)
            MMW: Mmwyl1_2626
            AHA: AHA_3113(purA)
            DNO: DNO_0600(purA)
            BCI: BCI_0577(purA)
            RMA: Rmag_0531
            VOK: COSY_0487(purA)
            NME: NMB0815
            NMA: NMA1024(purA)
            NMC: NMC0765(purA)
            NGO: NGO0398
            CVI: CV_0697(purA1) CV_3528(purA2)
            RSO: RSc1226(purA)
            REU: Reut_A2076 Reut_B5180
            REH: H16_A2354(purA1) H16_B1994(purA2)
            RME: Rmet_2096
            BMA: BMA1333(purA)
            BMV: BMASAVP1_A1823(purA)
            BML: BMA10299_A0073(purA)
            BMN: BMA10247_1095(purA)
            BXE: Bxe_A1606
            BVI: Bcep1808_1728 Bcep1808_5488
            BUR: Bcep18194_A5102 Bcep18194_C6526
            BCN: Bcen_5832 Bcen_6278
            BCH: Bcen2424_1801 Bcen2424_6199
            BAM: Bamb_1739 Bamb_5997
            BPS: BPSL1524(purA)
            BPM: BURPS1710b_2344(purA)
            BPL: BURPS1106A_2216(purA)
            BPD: BURPS668_2178(purA)
            BTE: BTH_I2245(purA) BTH_II2004
            PNU: Pnuc_1281
            BPE: BP2188(purA)
            BPA: BPP2844(purA)
            BBR: BB3165(purA)
            RFR: Rfer_2296
            POL: Bpro_2597
            PNA: Pnap_1883
            AAV: Aave_1434
            AJS: Ajs_1181
            VEI: Veis_3162
            MPT: Mpe_A1985
            HAR: HEAR1275(purA)
            MMS: mma_2117 mma_2318
            NEU: NE1281(purA)
            NET: Neut_0967
            NMU: Nmul_A0441
            EBA: ebA1249(purA)
            AZO: azo0938(purA)
            DAR: Daro_2974
            TBD: Tbd_0607
            MFA: Mfla_1583
            HPY: HP0255
            HPJ: jhp0239(purA)
            HPA: HPAG1_0257
            HHE: HH0954(purA)
            HAC: Hac_1353(purA)
            WSU: WS2056(purA)
            TDN: Tmden_0075
            CJE: Cj1498c(purA)
            CJR: CJE1671(purA)
            CJJ: CJJ81176_1490(purA)
            CJU: C8J_1403(purA)
            CJD: JJD26997_1846(purA)
            CFF: CFF8240_0370(purA)
            CCV: CCV52592_1784(purA)
            CHA: CHAB381_1370(purA)
            CCO: CCC13826_1872 CCC13826_2131(purA)
            ABU: Abu_0132(purA)
            NIS: NIS_1625(purA)
            SUN: SUN_0174(purA)
            GSU: GSU3308(purA)
            GME: Gmet_3260
            GUR: Gura_0662
            PCA: Pcar_0203
            PPD: Ppro_0518
            DVU: DVU3204(purA)
            DVL: Dvul_0183
            DDE: Dde_0176
            LIP: LI0202(purA)
            BBA: Bd1460(purA)
            DPS: DP1480
            ADE: Adeh_1265
            AFW: Anae109_2504
            MXA: MXAN_2618(purA)
            SAT: SYN_00122
            SFU: Sfum_1271
            WOL: WD0337(purA)
            WBM: Wbm0273
            AMA: AM856(purA)
            APH: APH_0336(purA)
            ERU: Erum5630(purA)
            ERW: ERWE_CDS_05900(purA)
            ERG: ERGA_CDS_05810(purA)
            ECN: Ecaj_0564
            ECH: ECH_0461(purA)
            NSE: NSE_0225(purA)
            PUB: SAR11_0605(adsS)
            MLO: mll3873
            MES: Meso_3159
            PLA: Plav_2144
            SME: SMc00643(purA)
            SMD: Smed_2616
            ATU: Atu2447(purA)
            ATC: AGR_C_4442
            RET: RHE_CH03344(purA)
            RLE: RL3768(purA)
            BME: BMEI0351
            BMF: BAB1_1695(purA)
            BMS: BR1683(purA)
            BMB: BruAb1_1668(purA)
            BOV: BOV_1627(purA)
            OAN: Oant_1231
            BJA: bll7052(purA)
            BRA: BRADO5935(purA)
            BBT: BBta_1850(purA)
            RPA: RPA4295(purA)
            RPB: RPB_1330
            RPC: RPC_4086
            RPD: RPD_3894
            RPE: RPE_4141
            NWI: Nwi_2965
            NHA: Nham_1123
            BHE: BH03790(purA)
            BQU: BQ02800(purA)
            BBK: BARBAKC583_0285(purA)
            XAU: Xaut_0037
            CCR: CC_3103
            SIL: SPO1318(purA)
            SIT: TM1040_1969
            RSP: RSP_0366
            RSH: Rsph17029_2010
            RSQ: Rsph17025_0875
            JAN: Jann_3179
            RDE: RD1_1912(purA)
            PDE: Pden_0603
            MMR: Mmar10_0558
            HNE: HNE_3124(purA)
            ZMO: ZMO1687(purA)
            NAR: Saro_2683
            SAL: Sala_0510
            SWI: Swit_4682
            ELI: ELI_01995
            GOX: GOX1448
            GBE: GbCGDNIH1_0847
            ACR: Acry_2784
            RRU: Rru_A1106 Rru_A1964
            MAG: amb3190
            MGM: Mmc1_1523
            ABA: Acid345_3868
            SUS: Acid_2022 Acid_6275
            BSU: BG10002(purA)
            BHA: BH4028(purA)
            BAN: BA5716(purA)
            BAR: GBAA5716(purA)
            BAA: BA_0574
            BAT: BAS5320
            BCE: BC5468
            BCA: BCE_5617(purA)
            BCZ: BCZK5164(purA)
            BCY: Bcer98_4007
            BTK: BT9727_5148(purA)
            BTL: BALH_4974(purA)
            BLI: BL03156(purA)
            BLD: BLi04341(purA)
            BCL: ABC4100(purA)
            BAY: RBAM_037450
            BPU: BPUM_3693
            OIH: OB3453(purA)
            GKA: GK3475
            GTN: GTNG_3416(purA)
            SAU: SA0016(purA)
            SAV: SAV0017(purA)
            SAM: MW0017(purA)
            SAR: SAR0017(purA)
            SAS: SAS0017
            SAC: SACOL0018(purA)
            SAB: SAB0017(purA)
            SAA: SAUSA300_0017(purA)
            SAO: SAOUHSC_00019
            SAJ: SaurJH9_0017
            SAH: SaurJH1_0017
            SEP: SE0016
            SER: SERP2536(purA)
            SHA: SH0016(purA)
            SSP: SSP0017
            LMO: lmo0055(purA)
            LMF: LMOf2365_0065(purA)
            LIN: lin0048(purA)
            LWE: lwe0046(purA)
            LLA: L12179(purA)
            LLC: LACR_2207
            LLM: llmg_2201(purA)
            SPY: SPy_0160(purA)
            SPZ: M5005_Spy_0136(purA)
            SPM: spyM18_0156
            SPG: SpyM3_0125(purA)
            SPS: SPs0127
            SPH: MGAS10270_Spy0138(purA)
            SPI: MGAS10750_Spy0141(purA)
            SPJ: MGAS2096_Spy0141 MGAS2096_Spy0142(purA)
            SPK: MGAS9429_Spy0138(purA)
            SPF: SpyM50131(purA)
            SPA: M6_Spy0183
            SPB: M28_Spy0134(purA)
            SPN: SP_0019
            SPR: spr0021(purA)
            SPD: SPD_0024(purA)
            SAG: SAG1818(purA)
            SAN: gbs1859(purA)
            SAK: SAK_1838(purA)
            SMU: SMU.268(purA)
            STC: str1940(purA)
            STL: stu1940(purA)
            STE: STER_1913
            SSA: SSA_2185(purA)
            SSU: SSU05_1966
            SSV: SSU98_1971
            SGO: SGO_1989(purA)
            LPL: lp_3270(purA)
            LJO: LJ0442
            LAC: LBA1892(purA)
            LSA: LSA0063(purA)
            LSL: LSL_1724(purA)
            LDB: Ldb0291(purA)
            LBR: LVIS_0227
            LCA: LSEI_0122
            LGA: LGAS_0390
            LRE: Lreu_0069
            PPE: PEPE_1247
            EFA: EF0014(purA)
            OOE: OEOE_1126
            LME: LEUM_1460
            STH: STH3314
            CAC: CAC3593(purA)
            CPE: CPE2622(purA)
            CPF: CPF_2958(purA)
            CPR: CPR_2641(purA)
            CNO: NT01CX_0905(purA)
            CTH: Cthe_3093
            CDF: CD3655(purA)
            CBO: CBO3616(adeK)
            CBA: CLB_3709(purA)
            CBH: CLC_3615(purA)
            CBF: CLI_3861(purA)
            CBE: Cbei_2082 Cbei_5074
            CKL: CKL_0087(purA)
            AMT: Amet_4765
            CHY: CHY_2670(purA)
            DSY: DSY5027
            DRM: Dred_3300
            PTH: PTH_2883(purA)
            SWO: Swol_2533
            CSC: Csac_2578
            TTE: TTE2696(purA)
            MTA: Moth_2309
            MPE: MYPE5830
            MMY: MSC_0850(purA)
            MCP: MCAP_0767(purA)
            MFL: Mfl074
            MTU: Rv0357c(purA)
            MTC: MT0373(purA)
            MBO: Mb0364c(purA)
            MBB: BCG_0395c(purA)
            MLE: ML0280(purA)
            MPA: MAP3869(purA)
            MAV: MAV_4777(purA)
            MSM: MSMEG_0759(purA)
            MVA: Mvan_0677
            MGI: Mflv_0228
            MMC: Mmcs_0515
            MKM: Mkms_0526
            MJL: Mjls_0504
            CGL: NCgl2669(cgl2766)
            CGB: cg3063(purA)
            CEF: CE2597(purA)
            CDI: DIP2063(purA)
            CJK: jk0222(purA)
            NFA: nfa53730(purA)
            RHA: RHA1_ro05551(purA1) RHA1_ro08616(purA2)
            SCO: SCO3629(purA)
            SMA: SAV4547(purA)
            TWH: TWT792(purA)
            TWS: TW801(purA)
            LXX: Lxx23290(purA)
            CMI: CMM_0689(purA)
            ART: Arth_0522
            AAU: AAur_0563(purA)
            PAC: PPA1994
            NCA: Noca_4344
            TFU: Tfu_3012
            FRA: Francci3_4368
            FAL: FRAAL6660(purA)
            ACE: Acel_2126
            KRA: Krad_4119
            SEN: SACE_7173(purA)
            STP: Strop_0133
            BLO: BL0549(purA)
            BAD: BAD_0067(purA)
            RXY: Rxyl_0990
            FNU: FN1605
            RBA: RB12924(purA)
            LIL: LA1110(purA)
            LIC: LIC12565(purA)
            LBJ: LBJ_2686
            LBL: LBL_0387
            SYN: sll1823(purA)
            SYW: SYNW1773(purA)
            SYC: syc1696_d(purA)
            SYF: Synpcc7942_2409
            SYD: Syncc9605_0691
            SYE: Syncc9902_1667
            SYG: sync_2023(purA)
            SYR: SynRCC307_0879(purA)
            SYX: SynWH7803_0620(purA)
            CYA: CYA_2899(purA)
            CYB: CYB_0079(purA)
            TEL: tll0531(purA)
            GVI: glr3280(purA)
            ANA: alr4784
            AVA: Ava_2053
            PMA: Pro0506(purA)
            PMM: PMM0506(purA)
            PMT: PMT1261(purA)
            PMN: PMN2A_1839
            PMI: PMT9312_0507
            PMB: A9601_05631(purA)
            PMC: P9515_05701(purA)
            PMF: P9303_07421(purA)
            PMG: P9301_05331(purA)
            PMH: P9215_05881
            PME: NATL1_05641(purA)
            TER: Tery_3282
            BTH: BT_1843
            BFR: BF3421
            BFS: BF3243(purA)
            PGI: PG0464(purA)
            SRU: SRU_1827(purA)
            CHU: CHU_1701(purA)
            GFO: GFO_0776(purA)
            FJO: Fjoh_0751 Fjoh_2221
            FPS: FP1902(purA)
            CTE: CT2154(purA)
            CCH: Cag_1816
            CPH: Cpha266_2390
            PVI: Cvib_0279
            PLT: Plut_0213
            DET: DET0976(purA)
            DEH: cbdb_A939(purA)
            DEB: DehaBAV1_0867
            RRS: RoseRS_4214
            RCA: Rcas_0444
            DRA: DR_0035
            DGE: Dgeo_0205
            TTH: TTC1764
            TTJ: TTHA0222
            AAE: aq_1290(purA)
            TMA: TM1096
            TPT: Tpet_1647
            TME: Tmel_0313
            FNO: Fnod_1284
            MMP: MMP1432(purA)
            MMQ: MmarC5_0146
            MMZ: MmarC7_0677
            MAE: Maeo_0033
            MVN: Mevan_0743
            MAC: MA1919 MA4118(purA)
            MBA: Mbar_A0403
            MMA: MM_0801
            MBU: Mbur_0119
            MTP: Mthe_1304
            MHU: Mhun_2319
            MEM: Memar_0005
            MBN: Mboo_0004
            MST: Msp_0986(purA)
            MSI: Msm_1468
            MKA: MK0235(purA)
            HAL: VNG1089G(purA)
            HMA: rrnAC1283(purA)
            HWA: HQ1660A(purA)
            NPH: NP1530A(purA)
            TAC: Ta1367m
            TVO: TVN0287
            PTO: PTO0194
            PAB: PAB1303(purA)
            PFU: PF0308
            TKO: TK1002
            RCI: RCIX1751(purA)
            IHO: Igni_0346
            SSO: SSO0242(purA)
            STO: ST0291
            SAI: Saci_0709
            MSE: Msed_0015
            PAI: PAE0974(purA)
            PIS: Pisl_1196
            PCL: Pcal_0128
            PAS: Pars_0162
STRUCTURES  PDB: 1ADE  1ADI  1CG0  1CG1  1CG3  1CG4  1CH8  1CIB  1DJ2  1DJ3  
                 1GIM  1GIN  1HON  1HOO  1HOP  1IWE  1J4B  1JUY  1KJX  1KKB  
                 1KKF  1KSZ  1LNY  1LON  1LOO  1MEZ  1MF0  1MF1  1NHT  1P9B  
                 1QF4  1QF5  1SON  1SOO  2D7U  2DGN  2GCQ  2V40  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.4
            ExPASy - ENZYME nomenclature database: 6.3.4.4
            ExplorEnz - The Enzyme Database: 6.3.4.4
            ERGO genome analysis and discovery system: 6.3.4.4
            BRENDA, the Enzyme Database: 6.3.4.4
            CAS: 9023-57-8
///
ENTRY       EC 6.3.4.5                  Enzyme
NAME        argininosuccinate synthase;
            citrulline---aspartate ligase;
            argininosuccinate synthetase;
            arginine succinate synthetase;
            argininosuccinic acid synthetase;
            arginosuccinate synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     L-citrulline:L-aspartate ligase (AMP-forming)
REACTION    ATP + L-citrulline + L-aspartate = AMP + diphosphate +
            2-(Nomega-L-arginino)succinate [RN:R01954]
ALL_REAC    R01954
SUBSTRATE   ATP [CPD:C00002];
            L-citrulline [CPD:C00327];
            L-aspartate [CPD:C00049]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            2-(Nomega-L-arginino)succinate
REFERENCE   1  [PMID:13158183]
  AUTHORS   RATNER S.
  TITLE     Urea synthesis and metabolism of arginine and citrulline.
  JOURNAL   Adv. Enzymol. Relat. Subj. Biochem. 15 (1954) 319-87.
REFERENCE   2  [PMID:13748745]
  AUTHORS   SCHUEGRAF A, RATNER S, WARNER RC.
  TITLE     Free energy changes of the argininosuccinate synthetase reaction and
            of the hydrolysis of the inner pyrophosphate bond of adenosine
            triphosphate.
  JOURNAL   J. Biol. Chem. 235 (1960) 3597-602.
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00252  Alanine and aspartate metabolism
            PATH: map00330  Arginine and proline metabolism
ORTHOLOGY   KO: K01940  argininosuccinate synthase
GENES       HSA: 445(ASS1)
            MMU: 11898(Ass1)
            RNO: 25698(Ass)
            CFA: 480693(ASS1)
            BTA: 280726(ASS)
            GGA: 417185(RCJMB04_21j5)
            XLA: 380488(ass)
            XTR: 496645(ass)
            DME: Dmel_CG1315
            ATH: AT4G24830
            OSA: 4351847
            CME: CMT305C
            SCE: YOL058W(ARG1)
            AGO: AGOS_AER230C
            PIC: PICST_34492(ARG1)
            CGR: CAGL0C05115g
            SPO: SPBC428.05c
            ANI: AN1883.2
            AFM: AFUA_2G04310
            AOR: AO090023000395
            CNE: CND00700
            UMA: UM04872.1
            LMA: LmjF23.0260
            ECO: b3172(argG)
            ECJ: JW3140(argG)
            ECE: Z4534(argG)
            ECS: ECs4052
            ECC: c3929(argG)
            ECI: UTI89_C3604(argG)
            ECP: ECP_3259
            ECV: APECO1_3259(argG)
            ECW: EcE24377A_3657(argG)
            ECX: EcHS_A3364
            STY: STY3470(argG)
            STT: t3208(argG)
            SPT: SPA3158(argG)
            SEC: SC3231(argG)
            STM: STM3290.S(argG)
            YPE: YPO1570(argG)
            YPK: y2595(argG)
            YPM: YP_1458(argG)
            YPA: YPA_0865 YPA_0866
            YPN: YPN_2410
            YPP: YPDSF_1406
            YPS: YPTB1579(argG)
            YPI: YpsIP31758_2408(argG)
            SFL: SF3213(argG)
            SFX: S3430(argG)
            SFV: SFV_3202(argG)
            SSN: SSON_3320(argG)
            SBO: SBO_3210(argG)
            SDY: SDY_3351(argG)
            ECA: ECA0104(argG)
            PLU: plu4742(argG)
            BUC: BU050(argG)
            BAS: BUsg047(argG)
            BAB: bbp048(argG)
            BCC: BCc_032(argG)
            ENT: Ent638_3608
            SPE: Spro_4779
            HIN: HI1727(argG)
            HIT: NTHI2034(argG)
            HIP: CGSHiEE_03415
            HIQ: CGSHiGG_02375
            HDU: HD1204(argG)
            HSO: HS_1362(argG)
            PMU: PM0813(argG)
            MSU: MS1479(argG)
            APL: APL_0422(argG)
            ASU: Asuc_0985
            XFA: XF0999
            XFT: PD0291(argG)
            XCC: XCC2247(argG)
            XCB: XC_1871
            XCV: XCV2550(argG)
            XAC: XAC2351(argG)
            XOO: XOO2675(argG)
            XOM: XOO_2521(XOO2521)
            VCH: VC2642
            VCO: VC0395_A2218(argG)
            VVU: VV1_1373
            VVY: VV3000
            VPA: VP2757
            VFI: VF2304
            PPR: PBPRA0268
            PAE: PA3525(argG)
            PAU: PA14_18740(argG)
            PAP: PSPA7_1622(argG)
            PPU: PP_1088(argG)
            PPF: Pput_1129
            PST: PSPTO_4155(argG)
            PSB: Psyr_3892
            PSP: PSPPH_3886(argG)
            PFL: PFL_4853(argG)
            PFO: Pfl_1900 Pfl_4517
            PEN: PSEEN1210(argG)
            PMY: Pmen_1394
            PAR: Psyc_1631(argG)
            PCR: Pcryo_1864
            PRW: PsycPRwf_1659
            ACI: ACIAD1151(argG)
            ACB: A1S_1069
            SON: SO_0278(argG)
            SDN: Sden_0253
            SFR: Sfri_0194
            SAZ: Sama_0259
            SBL: Sbal_4121
            SBM: Shew185_4092
            SLO: Shew_0205
            SPC: Sputcn32_3714
            SSE: Ssed_4273
            SPL: Spea_0230
            SHE: Shewmr4_3706
            SHM: Shewmr7_0239
            SHN: Shewana3_3902
            SHW: Sputw3181_3857
            ILO: IL0615(argG)
            CPS: CPS_0463(argG)
            PHA: PSHAa2288(argG)
            PAT: Patl_0979
            SDE: Sde_2423
            PIN: Ping_0231
            MAQ: Maqu_2588
            LPN: lpg0494(argG)
            LPF: lpl0532(argG)
            LPP: lpp0556(argG)
            MCA: MCA1099(argG)
            TCX: Tcr_0914
            NOC: Noc_2108
            AEH: Mlg_0601
            HHA: Hhal_0725
            HCH: HCH_04989(argG)
            CSA: Csal_2127
            ABO: ABO_0725(argG)
            MMW: Mmwyl1_1533
            AHA: AHA_0596(argG)
            CRP: CRP_104
            RMA: Rmag_0151
            VOK: COSY_0154(argG)
            NME: NMB2129
            NMA: NMA0303(argG)
            NMC: NMC2106(argG)
            NGO: NGO1961
            CVI: CV_1994(argG)
            RSO: RSc2553(argG)
            REU: Reut_B5242
            REH: H16_B2531(argG)
            RME: Rmet_5926
            BMA: BMA3363(argG)
            BMV: BMASAVP1_A3032(argG)
            BML: BMA10299_A2061(argG)
            BMN: BMA10247_2224(argG)
            BXE: Bxe_A0756
            BVI: Bcep1808_4112
            BUR: Bcep18194_B2399
            BCN: Bcen_4651
            BCH: Bcen2424_3712
            BAM: Bamb_5452
            BPS: BPSL0298(argG) BPSL1721
            BPM: BURPS1710b_0501(argG) BURPS1710b_2152(argG)
            BPL: BURPS1106A_0319(argG) BURPS1106A_2016(argG)
            BPD: BURPS668_0305(argG) BURPS668_1996(argG)
            BTE: BTH_I0279(argG)
            PNU: Pnuc_1753
            BPE: BP3537(argG)
            BPA: BPP2541(argG)
            BBR: BB1986(argG)
            RFR: Rfer_2689
            POL: Bpro_1599
            PNA: Pnap_1082
            AAV: Aave_1856
            AJS: Ajs_2743
            VEI: Veis_3461
            MPT: Mpe_A3035
            HAR: HEAR0871(argG)
            MMS: mma_0847
            NEU: NE1437(argG)
            NET: Neut_2065
            NMU: Nmul_A1043
            EBA: ebA5097(argG)
            AZO: azo2186(argG)
            DAR: Daro_3031
            TBD: Tbd_1849
            MFA: Mfla_1708
            HHE: HH1221(argG)
            WSU: WS2164(argG)
            TDN: Tmden_1373
            CJE: Cj0665c(argG)
            CJR: CJE0767(argG)
            CJJ: CJJ81176_0692(argG)
            CJU: C8J_0621(argG)
            CJD: JJD26997_1334(argG)
            CFF: CFF8240_0842(argG)
            CCV: CCV52592_1976(argG)
            CHA: CHAB381_1064(argG)
            CCO: CCC13826_0600 CCC13826_1219(argG)
            ABU: Abu_1279(argG)
            NIS: NIS_0998(argG)
            SUN: SUN_1685(argG)
            GSU: GSU0153(argG)
            GME: Gmet_0206
            GUR: Gura_0228
            PCA: Pcar_2417
            PPD: Ppro_3171
            DVU: DVU1095(argG)
            DVL: Dvul_1900
            DDE: Dde_2531
            LIP: LI0656(argG)
            DPS: DP0436
            ADE: Adeh_3085
            AFW: Anae109_2680
            MXA: MXAN_5108(argG)
            SAT: SYN_01390 SYN_02157
            SFU: Sfum_0061
            ERU: Erum3770(argG)
            ERW: ERWE_CDS_03890(argG)
            ERG: ERGA_CDS_03850(argG)
            ECN: Ecaj_0367
            ECH: ECH_0680(argG)
            PUB: SAR11_0294(argG)
            MLO: mlr4366
            MES: Meso_3344
            PLA: Plav_1377
            SME: SMc03826(argG)
            SMD: Smed_3063
            ATU: Atu2667(argG)
            ATC: AGR_C_4836
            RET: RHE_CH03924(argG2)
            RLE: RL2987(argG) RL4515(argG)
            BME: BMEI1870
            BMF: BAB1_0071
            BMS: BR0074(argG)
            BMB: BruAb1_0074(argG)
            BOV: BOV_0073(argG)
            OAN: Oant_0086
            BJA: bll0522(argG)
            BRA: BRADO0243(argG)
            BBT: BBta_0238(argG)
            RPA: RPA0392(argG)
            RPB: RPB_0090
            RPC: RPC_0031
            RPD: RPD_0713
            RPE: RPE_0034
            NWI: Nwi_2803
            NHA: Nham_3623
            BBK: BARBAKC583_1361(argG)
            XAU: Xaut_2013
            CCR: CC_0129
            SIL: SPO0018(argG)
            SIT: TM1040_2883
            RSP: RSP_1212(argG)
            RSH: Rsph17029_2873
            RSQ: Rsph17025_2650
            JAN: Jann_0067
            RDE: RD1_0417(argG)
            PDE: Pden_0499
            MMR: Mmar10_2916
            HNE: HNE_3491(argG)
            ZMO: ZMO1036(argG)
            NAR: Saro_1195
            SAL: Sala_0495
            SWI: Swit_2970
            ELI: ELI_07850
            GOX: GOX0255
            GBE: GbCGDNIH1_0263
            ACR: Acry_0747
            RRU: Rru_A3751
            MAG: amb1125
            MGM: Mmc1_3742
            ABA: Acid345_4158
            SUS: Acid_4448
            BSU: BG12570(argG)
            BHA: BH3187(argG)
            BAN: BA4880(argG)
            BAR: GBAA4880(argG)
            BAA: BA_5301
            BAT: BAS4528
            BCE: BC4630
            BCA: BCE_4765(argG)
            BCZ: BCZK4375(argG)
            BCY: Bcer98_3306
            BTK: BT9727_4364(argG)
            BTL: BALH_4210(argG)
            BLI: BL00417(argG)
            BLD: BLi03084(argG)
            BCL: ABC2737(argG)
            BAY: RBAM_026380
            BPU: BPUM_2577
            OIH: OB3129(argG)
            GKA: GK2757(argG)
            GTN: GTNG_2682
            SAU: SA0822(argG)
            SAV: SAV0961(argG)
            SAM: MW0843(argG)
            SAR: SAR0923(argG)
            SAS: SAS0831
            SAC: SACOL0964(argG)
            SAB: SAB0829c(argG)
            SAA: SAUSA300_0864(argG)
            SAO: SAOUHSC_00899
            SAJ: SaurJH9_0961
            SAH: SaurJH1_0980
            SEP: SE0657
            SER: SERP0549(argG)
            SHA: SH1989(argG)
            SSP: SSP1814
            LMO: lmo2090(argG)
            LMF: LMOf2365_2122(argG)
            LIN: lin2195(argG)
            LWE: lwe2111(argG)
            LLA: L126739(argG)
            LLC: LACR_0125
            LLM: llmg_0138(argG)
            SPR: spr0102(argG)
            SPD: SPD_0110(argG)
            SAG: SAG0125(argG)
            SAN: gbs0123
            SAK: SAK_0176(argG)
            SMU: SMU.334
            STC: str1813(argG)
            STL: stu1813(argG)
            STE: STER_1792
            SSA: SSA_2142(argG)
            SSU: SSU05_2017
            SSV: SSU98_2019
            SGO: SGO_0175(argG)
            LPL: lp_0775(argG)
            LSL: LSL_0306(argG)
            LCA: LSEI_2811
            LRE: Lreu_0731
            OOE: OEOE_0939
            STH: STH2874
            CAC: CAC0973(argG)
            CPE: CPE0691(argG)
            CPF: CPF_0683(argG)
            CTC: CTC00561
            CNO: NT01CX_0135(argG)
            CTH: Cthe_0179
            CDF: CD1785(argG)
            CBO: CBO2670(argG)
            CBA: CLB_2612(argG)
            CBH: CLC_2544(argG)
            CBF: CLI_2736(argG)
            CBE: Cbei_4515
            CKL: CKL_0981(argG)
            AMT: Amet_0653
            CHY: CHY_2260(argG)
            DSY: DSY0785
            DRM: Dred_0277
            CSC: Csac_1814
            TTE: TTE2494(argG)
            MTA: Moth_2285
            MTU: Rv1658(argG)
            MTC: MT1696(argG)
            MBO: Mb1686(argG)
            MBB: BCG_1697(argG)
            MLE: ML1412(argG)
            MPA: MAP1367(argG)
            MAV: MAV_3112(argG)
            MSM: MSMEG_3770(argG)
            MVA: Mvan_3308
            MGI: Mflv_3524
            MMC: Mmcs_2966
            MKM: Mkms_3010
            MJL: Mjls_2981
            CGL: NCgl1346(cgl1400)
            CGB: cg1586(argG)
            CEF: CE1532(argG)
            CDI: DIP1173(argG)
            CJK: jk0847(argG)
            NFA: nfa19620(argG)
            RHA: RHA1_ro00950(argG)
            SCO: SCO7036(argG)
            SMA: SAV6778(argG2) SAV801(argG1)
            LXX: Lxx21970(argG)
            CMI: CMM_1996(argG)
            ART: Arth_1502
            AAU: AAur_1637(argG)
            PAC: PPA2201
            NCA: Noca_2474
            TFU: Tfu_2052
            FRA: Francci3_3169
            FAL: FRAAL5202(argG)
            ACE: Acel_1257
            KRA: Krad_0765
            SEN: SACE_2917(argG)
            STP: Strop_0690 Strop_1894
            BLO: BL1058(argG)
            BAD: BAD_0919(argG)
            RXY: Rxyl_2882
            RBA: RB8293(argG)
            LIL: LA4165
            LIC: LIC13324(argG)
            LBJ: LBJ_2885(argG)
            LBL: LBL_0178(argG)
            SYN: slr0585(argG)
            SYW: SYNW2513(argG)
            SYC: syc1488_c(argG)
            SYF: Synpcc7942_0009
            SYD: Syncc9605_2679
            SYE: Syncc9902_2308
            SYG: sync_2928(argG)
            SYR: SynRCC307_2522(argG)
            SYX: SynWH7803_2519(argG)
            CYA: CYA_0710(argG)
            CYB: CYB_1752(argG)
            TEL: tlr0712(argG)
            GVI: glr2933(argG)
            ANA: alr4798(argG)
            AVA: Ava_2068
            PMA: Pro1875(argG)
            PMM: PMM1707(argG)
            PMT: PMT2261(argG)
            PMN: PMN2A_1317
            PMI: PMT9312_1800
            PMB: A9601_19171(argG)
            PMC: P9515_18981(argG)
            PMF: P9303_30091(argG)
            PMG: P9301_18981(argG)
            PMH: P9215_19801
            PME: NATL1_21901(argG)
            TER: Tery_0882
            BTH: BT_3760
            BFR: BF0533
            BFS: BF0481(argG)
            SRU: SRU_2214(argG)
            CHU: CHU_3080(argG)
            GFO: GFO_2107(argG)
            FJO: Fjoh_3435
            CTE: CT1114(argG)
            CCH: Cag_0777
            CPH: Cpha266_1325
            PVI: Cvib_0882
            PLT: Plut_1044
            DET: DET1260(argG)
            DEH: cbdb_A1183(argG)
            DEB: DehaBAV1_1071
            RRS: RoseRS_4058
            RCA: Rcas_3356
            DRA: DR_0674
            DGE: Dgeo_2067
            TTH: TTC1701
            TTJ: TTHA0284
            AAE: aq_1140(argG)
            TMA: TM1780
            TPT: Tpet_1067
            MMP: MMP0073(argG)
            MMQ: MmarC5_1604
            MMZ: MmarC7_1072
            MAE: Maeo_0622
            MVN: Mevan_1086
            MAC: MA2142(argG)
            MBA: Mbar_A2373
            MMA: MM_0037
            MBU: Mbur_0873
            MTP: Mthe_1445
            MHU: Mhun_0116
            MLA: Mlab_1027
            MEM: Memar_0995
            MBN: Mboo_0836
            MTH: MTH1254
            MST: Msp_1459(argG)
            MSI: Msm_1084
            MKA: MK0942(argG)
            HAL: VNG2437G(argG)
            HMA: rrnAC2683(argG)
            HWA: HQ3711A(argG)
            NPH: NP5252A(argG)
            TAC: Ta0650
            TVO: TVN0927
            PTO: PTO0530
            PFU: PF0207
            RCI: RCIX1377(argG)
            IHO: Igni_0635
            HBU: Hbut_0305
            SSO: SSO0638(argG)
            STO: ST1501
            SAI: Saci_1617(argG)
            MSE: Msed_1987
            PAI: PAE2884(argG)
            PIS: Pisl_0279
            PCL: Pcal_0370
            PAS: Pars_0969
STRUCTURES  PDB: 1J1Z  1J20  1J21  1K92  1K97  1KH1  1KH2  1KH3  1KOR  1KP2  
                 1KP3  1VL2  2NZ2  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.5
            ExPASy - ENZYME nomenclature database: 6.3.4.5
            ExplorEnz - The Enzyme Database: 6.3.4.5
            ERGO genome analysis and discovery system: 6.3.4.5
            BRENDA, the Enzyme Database: 6.3.4.5
            CAS: 9023-58-9
///
ENTRY       EC 6.3.4.6                  Enzyme
NAME        urea carboxylase;
            urease (ATP-hydrolysing);
            urea carboxylase (hydrolysing);
            ATP---urea amidolyase;
            urea amidolyase;
            UALase;
            UCA
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     urea:carbon-dioxide ligase (ADP-forming)
REACTION    ATP + urea + HCO3- = ADP + phosphate + urea-1-carboxylate
            [RN:R00774]
ALL_REAC    R00774
SUBSTRATE   ATP [CPD:C00002];
            urea [CPD:C00086];
            HCO3- [CPD:C00288]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            urea-1-carboxylate [CPD:C01010]
COFACTOR    Biotin [CPD:C00120]
COMMENT     A biotinyl-protein. The yeast enzyme (but not that from green algae)
            also catalyses the reaction of EC 3.5.1.54 allophanate hydrolase,
            thus bringing about the hydrolysis of urea to CO2 and NH3.
            Previously also listed as EC 3.5.1.45. The enzyme from the
            prokaryotic bacterium Oleomonas sagaranensis can also use acetamide
            and formamide as substrates [4].
REFERENCE   1
  AUTHORS   Roon, R.J. and Levenberg, B.
  TITLE     ATP-Urea amidolyase (ADP) (Candida utilis).
  JOURNAL   Methods Enzymol. 17A (1970) 317-324.
  ORGANISM  Candida utilis
REFERENCE   2  [PMID:4556303]
  AUTHORS   Roon RJ, Levenberg B.
  TITLE     Urea amidolyase. I. Properties of the enzyme from Candida utilis.
  JOURNAL   J. Biol. Chem. 247 (1972) 4107-13.
  ORGANISM  Candida utilis
REFERENCE   3  [PMID:6124544]
  AUTHORS   Sumrada RA, Cooper TG.
  TITLE     Urea carboxylase and allophanate hydrolase are components of a
            multifunctional protein in yeast.
  JOURNAL   J. Biol. Chem. 257 (1982) 9119-27.
  ORGANISM  Candida utilis, Saccharomyces cerevisiae [GN:sce]
REFERENCE   4  [PMID:15090492]
  AUTHORS   Kanamori T, Kanou N, Atomi H, Imanaka T.
  TITLE     Enzymatic characterization of a prokaryotic urea carboxylase.
  JOURNAL   J. Bacteriol. 186 (2004) 2532-9.
  ORGANISM  Oleomonas sagaranensis
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
ORTHOLOGY   KO: K01941  urea carboxylase
GENES       SCE: YBR208C(DUR1,2)
            AGO: AGOS_ADR051C
            PIC: PICST_28452(DUR1)
            CGR: CAGL0M05533g
            ECA: ECA2142
            PPF: Pput_2770
            PSP: PSPPH_3975
            SAZ: Sama_0022
            BPL: BURPS1106A_A0271
            BPD: BURPS668_A0363
            VEI: Veis_0373 Veis_4581
            NET: Neut_2475
            RLE: pRL120150 pRL120151 pRL90293
            BBT: BBta_2438
            RPE: RPE_1219 RPE_1220
            SIT: TM1040_3255
            GBE: GbCGDNIH1_1745
            SUS: Acid_3428
            BCY: Bcer98_2061
            AMT: Amet_2973
            MSM: MSMEG_2187
            RHA: RHA1_ro02135
            CMI: CMM_0120(uahA)
            AAU: AAur_0187(uca)
            ACE: Acel_0594
            TTH: TTC0624
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.6
            ExPASy - ENZYME nomenclature database: 6.3.4.6
            ExplorEnz - The Enzyme Database: 6.3.4.6
            ERGO genome analysis and discovery system: 6.3.4.6
            BRENDA, the Enzyme Database: 6.3.4.6
            CAS: 9058-98-4
///
ENTRY       EC 6.3.4.7                  Enzyme
NAME        ribose-5-phosphate---ammonia ligase;
            5-phosphoribosylamine synthetase;
            ribose 5-phosphate aminotransferase;
            ammonia-ribose 5-phosphate aminotransferase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     ribose-5-phosphate:ammonia ligase (ADP-forming)
REACTION    ATP + ribose 5-phosphate + NH3 = ADP + phosphate +
            5-phosphoribosylamine [RN:R01053]
ALL_REAC    R01053
SUBSTRATE   ATP [CPD:C00002];
            ribose 5-phosphate [CPD:C00117];
            NH3 [CPD:C00014]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            5-phosphoribosylamine [CPD:C03090]
REFERENCE   1  [PMID:5699059]
  AUTHORS   Reem GH.
  TITLE     Enzymatic synthesis of 5'-phosphoribosylamine from ribose
            5-phosphate and ammonia, an alternate first step in purine
            biosynthesis.
  JOURNAL   J. Biol. Chem. 243 (1968) 5695-701.
  ORGANISM  duck, chicken [GN:gga], pigeon
PATHWAY     PATH: map00230  Purine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.7
            ExPASy - ENZYME nomenclature database: 6.3.4.7
            ExplorEnz - The Enzyme Database: 6.3.4.7
            ERGO genome analysis and discovery system: 6.3.4.7
            BRENDA, the Enzyme Database: 6.3.4.7
            CAS: 9082-52-4
///
ENTRY       EC 6.3.4.8                  Enzyme
NAME        imidazoleacetate---phosphoribosyldiphosphate ligase;
            5-phosphoribosylimidazoleacetate synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     imidazoleacetate:5-phosphoribosyl-diphosphate ligase (ADP- and
            diphosphate-forming)
REACTION    ATP + imidazole-4-acetate + 5-phosphoribosyl diphosphate = ADP +
            phosphate + 1-(5-phosphoribosyl)imidazole-4-acetate + diphosphate
            [RN:R04068]
ALL_REAC    R04068
SUBSTRATE   ATP [CPD:C00002];
            imidazole-4-acetate [CPD:C02835];
            5-phosphoribosyl diphosphate [CPD:C00119]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            1-(5-phosphoribosyl)imidazole-4-acetate [CPD:C04437];
            diphosphate [CPD:C00013]
REFERENCE   1  [PMID:14235540]
  AUTHORS   CROWLEY GM.
  TITLE     THE ENZYMATIC SYNTHESIS OF 5'-PHOSPHORIBOSYLIMIDAZOLEACETIC ACID.
  JOURNAL   J. Biol. Chem. 239 (1964) 2593-601.
  ORGANISM  rabbit
PATHWAY     PATH: map00340  Histidine metabolism
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.8
            ExPASy - ENZYME nomenclature database: 6.3.4.8
            ExplorEnz - The Enzyme Database: 6.3.4.8
            ERGO genome analysis and discovery system: 6.3.4.8
            BRENDA, the Enzyme Database: 6.3.4.8
            CAS: 37318-65-3
///
ENTRY       EC 6.3.4.9                  Enzyme
NAME        biotin---[methylmalonyl-CoA-carboxytransferase] ligase;
            biotin-[methylmalonyl-CoA-carboxyltransferase] synthetase;
            biotin-methylmalonyl coenzyme A carboxyltransferase synthetase;
            biotin-transcarboxylase synthetase;
            methylmalonyl coenzyme A holotranscarboxylase synthetase;
            biotin---[methylmalonyl-CoA-carboxyltransferase] ligase;
            biotin:apo[methylmalonyl-CoA:pyruvate carboxyltransferase] ligase
            (AMP-forming)
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     biotin:apo[methylmalonyl-CoA:pyruvate carboxytransferase] ligase
            (AMP-forming)
REACTION    ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxytransferase] =
            AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxytransferase]
            [RN:R04563]
ALL_REAC    R04563;
            (other) R01074 R05145
SUBSTRATE   ATP [CPD:C00002];
            biotin [CPD:C00120];
            apo-[methylmalonyl-CoA:pyruvate carboxytransferase] [CPD:C04736]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            [methylmalonyl-CoA:pyruvate carboxytransferase] [CPD:C04682]
REFERENCE   1
  AUTHORS   Lane, M.D., Young, D.L. and Lynen, F.
  TITLE     The enzymatic synthesis of holotranscarboxylase from
            apotranscarboxylase and (+)-biotin. I. Purification of the apoenzyme
            and synthetase; characteristics of the reaction.
  JOURNAL   J. Biol. Chem. 239 (1964) 2858-2864.
  ORGANISM  Propionibacterium shermanii
PATHWAY     PATH: map00780  Biotin metabolism
ORTHOLOGY   KO: K01942  biotin-[methylmalonyl-CoA-carboxyltransferase] ligase
GENES       HSA: 3141(HLCS)
            PTR: 473989(HLCS)
            MMU: 110948(Hlcs)
            RNO: 288240(RGD1565360_predicted)
            CFA: 478412(HLCS)
            BTA: 510590(LOC510590)
            GGA: 418516(HLCS)
            SCE: YDL141W(BPL1)
            AGO: AGOS_ADR085W
            CAL: CaO19_7645(CaO19.7645)
            SPO: SPBC30D10.07c
            ANI: AN6055.2
            AFM: AFUA_2G09550
            AOR: AO090011000708
            CNE: CNC00800
            EHI: 492.t00007
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.9
            ExPASy - ENZYME nomenclature database: 6.3.4.9
            ExplorEnz - The Enzyme Database: 6.3.4.9
            ERGO genome analysis and discovery system: 6.3.4.9
            BRENDA, the Enzyme Database: 6.3.4.9
            CAS: 37318-66-4
///
ENTRY       EC 6.3.4.10                 Enzyme
NAME        biotin---[propionyl-CoA-carboxylase (ATP-hydrolysing)] ligase;
            biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] synthetase;
            biotin-propionyl coenzyme A carboxylase synthetase;
            propionyl coenzyme A holocarboxylase synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     biotin:apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
            ligase (AMP-forming)
REACTION    ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase
            (ADP-forming)] = AMP + diphosphate + [propionyl-CoA:carbon-dioxide
            ligase (ADP-forming)] [RN:R04582]
ALL_REAC    R04582;
            (other) R01074 R05145
SUBSTRATE   ATP [CPD:C00002];
            biotin [CPD:C00120];
            apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] [CPD:C04763]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            [propionyl-CoA:carbon-dioxide ligase (ADP-forming)] [CPD:C04727]
REFERENCE   1
  AUTHORS   Siegel, L., Foote, J.L. and Coon, M.J.
  TITLE     The enzymatic synthesis of propionyl coenzyme A holocarboxylase from
            d-biotinyl 5'-adenylate and the apocarboxylase.
  JOURNAL   J. Biol. Chem. 240 (1965) 1025-1031.
  ORGANISM  rabbit
PATHWAY     PATH: map00780  Biotin metabolism
ORTHOLOGY   KO: K01943  biotin--[propionyl-CoA-carboxylase (ATP-hydrolysing)]
                        ligase
GENES       HSA: 3141(HLCS)
            PTR: 473989(HLCS)
            MMU: 110948(Hlcs)
            RNO: 288240(RGD1565360_predicted)
            CFA: 478412(HLCS)
            BTA: 510590(LOC510590)
            GGA: 418516(HLCS)
            SCE: YDL141W(BPL1)
            AGO: AGOS_ADR085W
            CAL: CaO19_7645(CaO19.7645)
            SPO: SPBC30D10.07c
            ANI: AN6055.2
            AFM: AFUA_2G09550
            AOR: AO090011000708
            CNE: CNC00800
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.10
            ExPASy - ENZYME nomenclature database: 6.3.4.10
            ExplorEnz - The Enzyme Database: 6.3.4.10
            ERGO genome analysis and discovery system: 6.3.4.10
            BRENDA, the Enzyme Database: 6.3.4.10
            CAS: 37318-67-5
///
ENTRY       EC 6.3.4.11                 Enzyme
NAME        biotin---[methylcrotonoyl-CoA-carboxylase] ligase;
            biotin-[methylcrotonoyl-CoA-carboxylase] synthetase;
            biotin-beta-methylcrotonyl coenzyme A carboxylase synthetase;
            beta-methylcrotonyl coenzyme A holocarboxylase synthetase;
            holocarboxylase-synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     biotin:apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase
            (ADP-forming)] ligase (AMP-forming)
REACTION    ATP + biotin + apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase
            (ADP-forming)] = AMP + diphosphate +
            [3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)]
            [RN:R04604]
ALL_REAC    R04604;
            (other) R01074 R05145
SUBSTRATE   ATP [CPD:C00002];
            biotin [CPD:C00120];
            apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)]
            [CPD:C04827]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            [3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)]
            [CPD:C04801]
REFERENCE   1  [PMID:5867144]
  AUTHORS   Hopner T, Knappe J.
  TITLE     [Synthesis of biotin in beta-methylcrotonyl-CoA-carboxylase by
            holocarboxylase synthetase]
  JOURNAL   Biochem. Z. 342 (1965) 190-206.
PATHWAY     PATH: map00780  Biotin metabolism
ORTHOLOGY   KO: K01944  biotin-[methylcrotonoyl-CoA-carboxylase] ligase
GENES       HSA: 3141(HLCS)
            PTR: 473989(HLCS)
            MMU: 110948(Hlcs)
            RNO: 288240(RGD1565360_predicted)
            CFA: 478412(HLCS)
            BTA: 510590(LOC510590)
            GGA: 418516(HLCS)
            SCE: YDL141W(BPL1)
            AGO: AGOS_ADR085W
            CAL: CaO19_7645(CaO19.7645)
            SPO: SPBC30D10.07c
            ANI: AN6055.2
            AFM: AFUA_2G09550
            AOR: AO090011000708
            CNE: CNC00800
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.11
            ExPASy - ENZYME nomenclature database: 6.3.4.11
            ExplorEnz - The Enzyme Database: 6.3.4.11
            ERGO genome analysis and discovery system: 6.3.4.11
            BRENDA, the Enzyme Database: 6.3.4.11
            CAS: 37318-68-6
///
ENTRY       EC 6.3.4.12                 Enzyme
NAME        glutamate---methylamine ligase;
            gamma-glutamylmethylamide synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     L-glutamate:methylamine ligase (ADP-forming)
REACTION    ATP + L-glutamate + methylamine = ADP + phosphate +
            N5-methyl-L-glutamine [RN:R01585]
ALL_REAC    R01585
SUBSTRATE   ATP [CPD:C00002];
            L-glutamate [CPD:C00025];
            methylamine [CPD:C00218]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            N5-methyl-L-glutamine [CPD:C03153]
REFERENCE   1  [PMID:5800436]
  AUTHORS   Kung HF, Wagner C.
  TITLE     Gamma-glutamylmethylamide. A new intermediate in the metabolism of
            methylamine.
  JOURNAL   J. Biol. Chem. 244 (1969) 4136-40.
  ORGANISM  Pseudomonas sp.
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.12
            ExPASy - ENZYME nomenclature database: 6.3.4.12
            ExplorEnz - The Enzyme Database: 6.3.4.12
            ERGO genome analysis and discovery system: 6.3.4.12
            BRENDA, the Enzyme Database: 6.3.4.12
            CAS: 37318-69-7
///
ENTRY       EC 6.3.4.13                 Enzyme
NAME        phosphoribosylamine---glycine ligase;
            phosphoribosylglycinamide synthetase;
            glycinamide ribonucleotide synthetase;
            phosphoribosylglycineamide synthetase;
            glycineamide ribonucleotide synthetase;
            2-amino-N-ribosylacetamide 5'-phosphate kinosynthase;
            5'-phosphoribosylglycinamide synthetase;
            GAR
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     5-phospho-D-ribosylamine:glycine ligase (ADP-forming)
REACTION    ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate +
            N1-(5-phospho-D-ribosyl)glycinamide [RN:R04144]
ALL_REAC    R04144
SUBSTRATE   ATP [CPD:C00002];
            5-phospho-D-ribosylamine [CPD:C03090];
            glycine [CPD:C00037]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            N1-(5-phospho-D-ribosyl)glycinamide [CPD:C03838]
REFERENCE   1  [PMID:13357451]
  AUTHORS   GOLDTHWAIT DA, GREENBERG GR, PEABODY RA.
  TITLE     On the mechanism of synthesis of glycinamide ribotide and its formyl
            derivative.
  JOURNAL   J. Biol. Chem. 221 (1956) 569-77.
  ORGANISM  pigeon
REFERENCE   2  [PMID:13563520]
  AUTHORS   HARTMAN SC, BUCHANAN JM.
  TITLE     Biosynthesis of the purines. XXII.
            2-Amino-N-ribosylacetamide-5'-phosphate kinosynthase.
  JOURNAL   J. Biol. Chem. 233 (1958) 456-61.
  ORGANISM  chicken [GN:gga], pigeon
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01945  phosphoribosylamine--glycine ligase
GENES       HSA: 2618(GART)
            MMU: 14450(Gart)
            CFA: 487740(LOC487740)
            GGA: 395315(GART)
            XTR: 496927(gart)
            CEL: F38B6.4(GARS\\/AIRS\\/GART)
            ATH: AT1G09830
            OSA: 4344854
            CME: CMJ084C
            SCE: YGL234W(ADE5,7)
            AGO: AGOS_AFR254C
            SPO: SPBC405.01(ade1)
            ANI: AN6541.2
            AFM: AFUA_6G04730
            AOR: AO090701000066
            CNE: CNN00440
            DDI: DDB_0230084(purD)
            ECO: b4005(purD)
            ECJ: JW3969(purD)
            ECE: Z5582(purD)
            ECS: ECs4928
            ECC: c4963(purD)
            ECI: UTI89_C3815(purD)
            ECP: ECP_4218
            ECV: APECO1_2470(purD)
            ECW: EcE24377A_4548(purD)
            ECX: EcHS_A4239
            STY: STY3710(purD)
            STT: t3456(purD)
            SPT: SPA4012(purD)
            SEC: SC4056(purD)
            STM: STM4175(purD)
            YPE: YPO3729(purD)
            YPK: y0501(purD)
            YPM: YP_3092(purD)
            YPA: YPA_3602
            YPN: YPN_0236
            YPP: YPDSF_3727
            YPS: YPTB0299(purD)
            YPI: YpsIP31758_3844(purD)
            SFL: SF4077(purD)
            SFX: S3658(purD)
            SFV: SFV_4077(purD)
            SSN: SSON_4178(purD)
            SBO: SBO_4026(purD)
            SDY: SDY_3721(purD)
            ECA: ECA0240(purD)
            PLU: plu0494(purD)
            WBR: WGLp510(purD)
            SGL: SG0142
            ENT: Ent638_0215
            SPE: Spro_0292
            HIN: HI0888(purD)
            HIT: NTHI1052(purD)
            HIP: CGSHiEE_07590
            HSO: HS_1626(purD)
            PMU: PM0224(purD)
            MSU: MS1296(purD)
            APL: APL_1172(purD)
            ASU: Asuc_1148
            XFA: XF1976
            XFT: PD0827(purD)
            XCC: XCC0497(purD)
            XCB: XC_0509
            XCV: XCV0545(purD)
            XAC: XAC0511(purD)
            XOO: XOO0537(purD)
            XOM: XOO_0503(XOO0503)
            VCH: VC0275
            VCO: VC0395_A2652(purD)
            VVU: VV1_1226
            VVY: VV3143
            VPA: VP2898
            VFI: VF2395
            PPR: PBPRA3420
            PAE: PA4855(purD)
            PAU: PA14_64220(purD)
            PPU: PP_4823(purD)
            PPF: Pput_4698
            PST: PSPTO_4867(purD)
            PSB: Psyr_4407
            PSP: PSPPH_4450(purD)
            PFL: PFL_0665(purD)
            PFO: Pfl_0612
            PEN: PSEEN4864(purD)
            PMY: Pmen_0707
            PAR: Psyc_1061(purD)
            PCR: Pcryo_1401
            PRW: PsycPRwf_1419
            ACI: ACIAD2448(purD)
            SON: SO_0441(purD)
            SDN: Sden_3406
            SFR: Sfri_0492
            SAZ: Sama_0394
            SBL: Sbal_0419
            SBM: Shew185_3914
            SLO: Shew_3413
            SPC: Sputcn32_3402
            SSE: Ssed_0443
            SPL: Spea_0431
            SHE: Shewmr4_0444
            SHM: Shewmr7_3585
            SHN: Shewana3_0440
            SHW: Sputw3181_0541
            ILO: IL2292(purD)
            CPS: CPS_0555(purD)
            PHA: PSHAa0343(purD)
            PAT: Patl_0266
            SDE: Sde_0805
            PIN: Ping_3219
            MAQ: Maqu_3451
            CBU: CBU_0326(purD)
            CBD: COXBU7E912_1753(purD)
            LPN: lpg1673
            LPF: lpl1638(purD)
            LPP: lpp1645(purD)
            MCA: MCA0361(purD)
            FTU: FTT0894(purCD)
            FTF: FTF0894(purCD)
            FTW: FTW_1285(purCD)
            FTL: FTL_0396
            FTH: FTH_0388(purC)
            FTN: FTN_0420
            TCX: Tcr_0438
            NOC: Noc_2827
            AEH: Mlg_0612
            HHA: Hhal_1999
            HCH: HCH_06012
            CSA: Csal_0909
            ABO: ABO_2016(purD)
            MMW: Mmwyl1_2988
            AHA: AHA_0840(purD)
            DNO: DNO_0940(purD)
            BCI: BCI_0036(purD)
            RMA: Rmag_0057
            VOK: COSY_0062(purD)
            NME: NMB2151
            NMA: NMA0238(purD)
            NMC: NMC2129(purD)
            NGO: NGO1939
            CVI: CV_0547(purD)
            RSO: RSc2191(purD)
            REU: Reut_A2523
            REH: H16_A0915(purD)
            RME: Rmet_0784
            BMA: BMA1885(purD)
            BMV: BMASAVP1_A1074(purD)
            BML: BMA10299_A0793(purD)
            BMN: BMA10247_0357(purD)
            BXE: Bxe_A3260
            BVI: Bcep1808_2380
            BUR: Bcep18194_A5622
            BCN: Bcen_1683
            BCH: Bcen2424_2295
            BAM: Bamb_2333
            BPS: BPSL1164(purD)
            BPM: BURPS1710b_1384(purD)
            BPL: BURPS1106A_1239(purD)
            BPD: BURPS668_1230(purD)
            BTE: BTH_I1014(purD)
            PNU: Pnuc_0617
            BPE: BP2309(purD)
            BPA: BPP2421(purD)
            BBR: BB1870(purD)
            RFR: Rfer_2076
            POL: Bpro_1969
            PNA: Pnap_1729
            AAV: Aave_3202
            AJS: Ajs_1899
            VEI: Veis_4239
            MPT: Mpe_A1338
            HAR: HEAR0560(purD)
            MMS: mma_0543
            NEU: NE0877(purD)
            NET: Neut_1211
            NMU: Nmul_A0134
            EBA: ebA1155(purD)
            AZO: azo2895(purD)
            DAR: Daro_3668
            TBD: Tbd_2459
            MFA: Mfla_0348
            HPY: HP1218(purD)
            HPJ: jhp1140(purD)
            HPA: HPAG1_1158
            HHE: HH0598(purD)
            HAC: Hac_1595(purD)
            WSU: WS0894(purD)
            TDN: Tmden_0424
            CJE: Cj1250(purD)
            CJR: CJE1387(purD)
            CJJ: CJJ81176_1266(purD)
            CJU: C8J_1194(purD)
            CJD: JJD26997_0475(purD)
            CFF: CFF8240_1261(purD)
            CCV: CCV52592_0949(purD)
            CHA: CHAB381_0233(purD)
            CCO: CCC13826_0492(purD) CCC13826_0937
            ABU: Abu_1179(purD)
            NIS: NIS_1337(purD)
            SUN: SUN_1891(purD)
            GSU: GSU0610(purD)
            GME: Gmet_2904
            GUR: Gura_3845
            PCA: Pcar_2231
            PPD: Ppro_2591
            DVU: DVU0488(purD)
            DVL: Dvul_2453
            DDE: Dde_3458
            LIP: LI0921(purD)
            BBA: Bd3006(purD)
            DPS: DP2188
            ADE: Adeh_2467
            MXA: MXAN_2916(purD)
            SAT: SYN_02439
            SFU: Sfum_2759
            WOL: WD0029(purD)
            WBM: Wbm0465
            AMA: AM1011(purD)
            APH: APH_1088(purD)
            ERU: Erum7770(purD)
            ERW: ERWE_CDS_08210(purD)
            ERG: ERGA_CDS_08110(purD)
            ECN: Ecaj_0813
            ECH: ECH_1006(purD)
            NSE: NSE_0924(purD)
            PUB: SAR11_0153(purD)
            MLO: mlr7447
            MES: Meso_0719
            PLA: Plav_0619
            SME: SMc00993(purD)
            SMD: Smed_0471
            ATU: Atu0647(purD)
            ATC: AGR_C_1152
            RET: RHE_CH00886(purD)
            RLE: RL0947(purD)
            BME: BMEI1519
            BMF: BAB1_0442(purD)
            BMS: BR0414(purD)
            BMB: BruAb1_0437(purD)
            BOV: BOV_0422(purD)
            OAN: Oant_0529
            BJA: bll7498(purD)
            BRA: BRADO6088(purD)
            BBT: BBta_1699(purD)
            RPA: RPA1162(garS)
            RPB: RPB_1863
            RPC: RPC_4619
            RPD: RPD_4104
            RPE: RPE_4612
            NWI: Nwi_2552
            NHA: Nham_3173
            BHE: BH04270(purD)
            BQU: BQ03460(purD)
            BBK: BARBAKC583_0392(purD)
            XAU: Xaut_1412
            CCR: CC_0297
            SIL: SPO1345(purD)
            SIT: TM1040_1946
            RSP: RSP_1847(purD)
            RSH: Rsph17029_0496
            RSQ: Rsph17025_0635
            JAN: Jann_3302
            RDE: RD1_1927(purD)
            PDE: Pden_4029
            MMR: Mmar10_0627
            HNE: HNE_0922(purD)
            ZMO: ZMO0299(purD)
            NAR: Saro_0172
            SAL: Sala_3104
            SWI: Swit_3149
            ELI: ELI_12715
            GOX: GOX1728
            GBE: GbCGDNIH1_2297
            ACR: Acry_1330
            RRU: Rru_A0646
            MGM: Mmc1_3465
            ABA: Acid345_0231
            SUS: Acid_0014
            BSU: BG10711(purD)
            BHA: BH0634(purD)
            BAN: BA0299(purD)
            BAR: GBAA0299(purD)
            BAA: BA_0871
            BAT: BAS0286
            BCE: BC0334
            BCA: BCE_0328(purD)
            BCZ: BCZK0274(purD)
            BTK: BT9727_0271(purD)
            BTL: BALH_0293(purD)
            BLI: BL01487(purD)
            BLD: BLi00704(purD)
            BCL: ABC1035(purD)
            BAY: RBAM_006950
            BPU: BPUM_0607
            OIH: OB0750
            GKA: GK0268
            SAU: SA0926(purD)
            SAV: SAV1074(purD)
            SAM: MW0957(purD)
            SAR: SAR1048(purD)
            SAS: SAS1010
            SAC: SACOL1083(purD)
            SAB: SAB0941(purD)
            SAA: SAUSA300_0976(purD)
            SAO: SAOUHSC_01018
            SAJ: SaurJH9_1134
            SAH: SaurJH1_1156
            SEP: SE0772
            SER: SERP0659(purD)
            SHA: SH1883(purD)
            SSP: SSP1716
            LMO: lmo1764(purD)
            LMF: LMOf2365_1789(purD)
            LIN: lin1876(purD)
            LWE: lwe1782(purD)
            LLA: L153005(purD)
            LLC: LACR_1601
            LLM: llmg_0997(purD)
            SPY: SPy_0032(purD)
            SPZ: M5005_Spy_0029(purD)
            SPM: spyM18_0032(purD)
            SPG: SpyM3_0026(purD)
            SPS: SPs0027
            SPH: MGAS10270_Spy0030(purD)
            SPI: MGAS10750_Spy0030(purD)
            SPJ: MGAS2096_Spy0030(purD)
            SPK: MGAS9429_Spy0029(purD)
            SPF: SpyM50029(purD)
            SPA: M6_Spy0078
            SPB: M28_Spy0029(purD)
            SPN: SP_0051
            SPR: spr0052(purD)
            SPD: SPD_0058(purD)
            SAG: SAG0043(purD)
            SAN: gbs0042
            SAK: SAK_0076(purD)
            SMU: SMU.48(purD)
            STC: str0040(purD)
            STL: stu0040(purD)
            SSA: SSA_0037(purD)
            SGO: SGO_2092(purD)
            LPL: lp_2719(purD)
            LAC: LBA1551(purD)
            LSA: LSA0663(purD)
            LSL: LSL_0671(purD)
            LDB: Ldb1435(purD)
            LBU: LBUL_1330
            LCA: LSEI_1746
            LRE: Lreu_0145
            EFA: EF1777(purD)
            STH: STH2849
            CAC: CAC1396(purD)
            CPE: CPE0687(purD)
            CPF: CPF_0678(purD)
            CPR: CPR_0676(purD)
            CTC: CTC01961
            CTH: Cthe_1245
            CDF: CD0224(purD)
            CBO: CBO2872(purD)
            CBA: CLB_2837(purD)
            CBH: CLC_2770(purD)
            CBF: CLI_2930(purD)
            CBE: Cbei_1060
            CKL: CKL_2683(purD)
            AMT: Amet_0926
            CHY: CHY_1079(purD)
            DSY: DSY3925
            DRM: Dred_2361
            SWO: Swol_1774
            CSC: Csac_1991
            TTE: TTE0593(purD)
            MTA: Moth_2043
            MTU: Rv0772(purD)
            MTC: MT0796(purD)
            MBO: Mb0795(purD)
            MBB: BCG_0824(purD)
            MLE: ML2235(purD)
            MPA: MAP0606(purD)
            MAV: MAV_0718(purD)
            MSM: MSMEG_5852(purD)
            MVA: Mvan_5150
            MGI: Mflv_1608
            MMC: Mmcs_4571
            MKM: Mkms_4659
            MJL: Mjls_4954
            CGL: NCgl2511(cgl2600)
            CGB: cg2878(purD)
            CEF: CE2490(purD)
            CDI: DIP1932(purD)
            CJK: jk0346(purD)
            NFA: nfa5550(purD)
            RHA: RHA1_ro04777(purD)
            SCO: SCO4068(purD)
            SMA: SAV4149(purD)
            TWH: TWT725(purD)
            TWS: TW739(purD)
            LXX: Lxx22780(purD)
            CMI: CMM_0754(purD)
            ART: Arth_3406
            AAU: AAur_3384(purD)
            PAC: PPA1993
            NCA: Noca_4342
            TFU: Tfu_3013
            FRA: Francci3_4370
            FAL: FRAAL6663(purD)
            ACE: Acel_2127
            KRA: Krad_4100
            SEN: SACE_7168(purD)
            STP: Strop_0134
            BLO: BL1123(purD)
            BAD: BAD_0519(purD)
            RXY: Rxyl_0991
            FNU: FN0981
            RBA: RB6616(purD)
            TDE: TDE1267(purD)
            LIL: LA3764(purD)
            LIC: LIC10472(purD)
            LBJ: LBJ_0530(purD)
            LBL: LBL_2549(purD)
            SYN: slr1159(purD)
            SYW: SYNW0552(purD)
            SYC: syc0617_d(purD)
            SYF: Synpcc7942_0925
            SYD: Syncc9605_2122
            SYE: Syncc9902_0551
            SYG: sync_2218(purD)
            SYR: SynRCC307_1822(purD)
            SYX: SynWH7803_1962(purD)
            CYA: CYA_0622(purD)
            CYB: CYB_0043(purD)
            TEL: tlr1839(purD)
            GVI: glr2779(purD)
            ANA: alr3510
            AVA: Ava_3227
            PMA: Pro1421(purD)
            PMM: PMM1340(purD)
            PMT: PMT1416(purD)
            PMN: PMN2A_0911
            PMI: PMT9312_1438
            PMB: A9601_15411(purD)
            PMC: P9515_15011(purD)
            PMF: P9303_05461(purD)
            PMG: P9301_15261(purD)
            PMH: P9215_15691
            PME: NATL1_17671(purD)
            TER: Tery_1471
            BTH: BT_3253
            BFR: BF0084
            BFS: BF0096(purD)
            PGI: PG1360(purD)
            SRU: SRU_1862(purD)
            CHU: CHU_0296(purD)
            GFO: GFO_3282(purD)
            FJO: Fjoh_1041
            FPS: FP2473(purD)
            CTE: CT1674(purD)
            CCH: Cag_0171
            CPH: Cpha266_0528
            PVI: Cvib_1442
            PLT: Plut_1653
            DET: DET0838(purD)
            DEH: cbdb_A819(purD)
            RRS: RoseRS_0351 RoseRS_2692
            RCA: Rcas_0551 Rcas_3175
            DRA: DR_1431
            DGE: Dgeo_1347
            TTH: TTC0460
            TTJ: TTHA0812
            AAE: aq_742(purD)
            TMA: TM1250
            TPT: Tpet_1521
            TME: Tmel_0386
            FNO: Fnod_1672
            MJA: MJ0937(purD)
            MMP: MMP0392(purD)
            MMQ: MmarC5_1246
            MMZ: MmarC7_1390
            MAE: Maeo_1322
            MVN: Mevan_1379
            MAC: MA3309(purD)
            MBA: Mbar_A3513
            MMA: MM_0144
            MBU: Mbur_1056
            MHU: Mhun_1112
            MEM: Memar_1000
            MBN: Mboo_0840
            MST: Msp_0030(purD)
            MSI: Msm_1227
            MKA: MK1071(purD)
            HAL: VNG1305G(purD)
            HMA: rrnAC0307(purD1) rrnAC1109(purD2)
            HWA: HQ2560A(purD)
            NPH: NP3972A(purD)
            TAC: Ta0595m
            TVO: TVN0625
            PTO: PTO0950
            PHO: PH0323
            PAB: PAB1271(purD)
            PFU: PF0422
            TKO: TK0204
            RCI: RCIX513(purD)
            IHO: Igni_0165
            SSO: SSO0635(purD)
            STO: ST1498
            SAI: Saci_1613(purD)
            MSE: Msed_1983
            PAI: PAE0216(purD)
            PIS: Pisl_0106
            PCL: Pcal_1894
            PAS: Pars_2189
STRUCTURES  PDB: 1GSO  1VKZ  2QK4  2YRW  2YRX  2YS6  2YS7  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.13
            ExPASy - ENZYME nomenclature database: 6.3.4.13
            ExplorEnz - The Enzyme Database: 6.3.4.13
            ERGO genome analysis and discovery system: 6.3.4.13
            BRENDA, the Enzyme Database: 6.3.4.13
            CAS: 9032-01-3
///
ENTRY       EC 6.3.4.14                 Enzyme
NAME        biotin carboxylase;
            biotin carboxylase (component of acetyl CoA carboxylase)
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     biotin-carboxyl-carrier-protein:carbon-dioxide ligase (ADP-forming)
REACTION    ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate +
            carboxybiotin-carboxyl-carrier protein [RN:R04385]
ALL_REAC    R04385
SUBSTRATE   ATP [CPD:C00002];
            biotin-carboxyl-carrier protein [CPD:C06250];
            CO2 [CPD:C00011]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            carboxybiotin-carboxyl-carrier protein [CPD:C04419]
REFERENCE   1  [PMID:4922289]
  AUTHORS   Dimroth P, Guchhait RB, Stoll E, Lane MD.
  TITLE     Enzymatic carboxylation of biotin: molecular and catalytic
            properties of a component enzyme of acetyl CoA carboxylase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 67 (1970) 1353-60.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00061  Fatty acid biosynthesis
ORTHOLOGY   KO: K01946  biotin carboxylase
GENES       HSA: 31(ACACA) 32(ACACB)
            MMU: 100705(Acacb) 107476(Acaca)
            RNO: 116719(Acacb) 60581(Acaca)
            BTA: 281590(ACACA)
            GGA: 396504(ACACA)
            CME: CMM188C CMS299C
            SCE: YNR016C(ACC1)
            AGO: AGOS_AAR071W
            PIC: PICST_81158(ACC1)
            CAL: CaO19_7466(CaO19.7466)
            SPO: SPAC56E4.04c(cut6)
            ANI: AN6126.2
            AFM: AFUA_2G08670
            AOR: AO090011000838
            CNE: CNF02180
            DDI: DDB_0230067(accA)
            PFA: PF14_0664
            CPV: cgd8_3680
            CHO: Chro.80425
            TBR: Tb927.8.7100
            LMA: LmjF31.2970
            ECO: b3256(accC)
            ECJ: JW3224(accC)
            ECE: Z4616(accC)
            ECS: ECs4128
            ECC: c4012(accC)
            ECI: UTI89_C3689(accC)
            ECP: ECP_3341
            ECV: APECO1_3190(accC)
            STY: STY3560(accC)
            STT: t3295(accC)
            SPT: SPA3247(accC)
            SEC: SC3318(accC)
            STM: STM3380(accC)
            YPE: YPO3658(accC)
            YPK: y0209(accC)
            YPM: YP_3888(accC2)
            YPA: YPA_3671
            YPN: YPN_3513
            YPS: YPTB3572(accC)
            SFL: SF3294(accC)
            SFX: S3511(accC)
            SFV: SFV_3281(accC)
            SSN: SSON_3397(accC)
            SBO: SBO_3132(accC)
            SDY: SDY_3433(accC)
            ECA: ECA0260(accC)
            PLU: plu4075(accC) plu4306
            WBR: WGLp603(accC)
            SGL: SG0152
            BFL: Bfl291(accC)
            BPN: BPEN_299(accC)
            HIN: HI0972(accC)
            HIT: NTHI1145(accC)
            HDU: HD0635(accC)
            HSO: HS_0568(accC)
            PMU: PM1091(accC)
            MSU: MS1788(accC)
            APL: APL_1865(accC)
            XFA: XF0049
            XFT: PD0036(accC)
            XCC: XCC0515(accC)
            XCB: XC_0527
            XCV: XCV0271(accC) XCV0563(accC)
            XAC: XAC0530(accC)
            XOO: XOO0556(accC)
            XOM: XOO_0520(XOO0520)
            VCH: VC0295
            VCO: VC0395_A2688(accC)
            VVU: VV1_1234
            VVY: VV3136
            VPA: VP2881
            VFI: VF2387
            PPR: PBPRA3406
            PAE: PA0494 PA4848(accC)
            PAU: PA14_06450(accC)
            PPU: PP_0558(accC-1)
            PST: PSPTO_2921(accC-1) PSPTO_4861(accC-2) PSPTO_5381
            PSB: Psyr_0500 Psyr_4401
            PSP: PSPPH_0491 PSPPH_4444(accC2)
            PFL: PFL_0671(accC) PFL_4549
            PFO: Pfl_0618
            PEN: PSEEN4857(accC-1)
            PAR: Psyc_1101 Psyc_1227(accC)
            PCR: Pcryo_1164
            ACI: ACIAD1736(accC) ACIAD2517(bccA)
            SON: SO_0840
            ILO: IL2286(accC)
            CPS: CPS_0946(accC)
            PHA: PSHAa0266(accC)
            PAT: Patl_0090
            CBU: CBU_1726(accC)
            CBD: COXBU7E912_0276(accC) COXBU7E912_1070
            LPN: lpg0462(accC) lpg1829
            LPF: lpl0504(accC) lpl1793
            LPP: lpp0528(accC) lpp1792
            MCA: MCA1046(accC)
            FTU: FTT0473(accC)
            FTF: FTF0473(accC)
            FTW: FTW_1597(accC)
            FTL: FTL_1591
            FTH: FTH_1537(accC)
            FTN: FTN_0564(accC)
            TCX: Tcr_0443
            NOC: Noc_1051
            AEH: Mlg_0026
            ABO: ABO_2010(accC)
            AHA: AHA_3347(accC)
            BCI: BCI_0052(accC)
            VOK: COSY_0959(accC)
            NME: NMB1861
            NMA: NMA0596(accC)
            NMC: NMC0357(accC)
            NGO: NGO0044
            CVI: CV_0018 CV_0985(accC) CV_1762 CV_1807
            RSO: RSc2787(accC1) RSp0940(accC2)
            REU: Reut_A2451 Reut_A2866
            REH: H16_A0184(accC1) H16_A3172(accC2) H16_A3290(accC3) H16_B1757
            RME: Rmet_3065
            BMA: BMA2502(accC) BMAA1882
            BXE: Bxe_A0531
            BCN: Bcen_0121
            BAM: Bamb_0506
            BPS: BPSL2984(accC) BPSS0196(accC) BPSS2034
            BPM: BURPS1710b_3501(accC) BURPS1710b_A1152
            BTE: BTH_II0286
            BPE: BP0889(accC) BP2996(fabG)
            BPA: BPP2175(accC) BPP3916(fabG)
            BBR: BB1572(accC) BB2689(accC) BB4389(fabG) BB4735(accC)
            RFR: Rfer_0868 Rfer_3352
            POL: Bpro_1100
            MPT: Mpe_A3207
            HAR: HEAR2763(accC)
            MMS: mma_2972
            NEU: NE0653(accC1)
            NET: Neut_1899
            NMU: Nmul_A2752
            EBA: ebA1474(accC) ebA316(xccC) ebA5774(xccC)
            AZO: azo0862(accC1) azo3068(accC2)
            DAR: Daro_3938
            TBD: Tbd_0181
            MFA: Mfla_0024
            HPY: HP0370(accC)
            HPJ: jhp1011(accC)
            HPA: HPAG1_1022
            HHE: HH0195(accC)
            HAC: Hac_0497(accC)
            WSU: WS1074(accC)
            TDN: Tmden_0622
            CJE: Cj1290c(accC)
            CFF: CFF8240_0676
            CCV: CCV52592_0748
            CHA: CHAB381_0801 CHAB381_1156
            NIS: NIS_1644(accC)
            GSU: GSU2019(accC)
            GME: Gmet_0984
            PCA: Pcar_2127
            LIP: LI0488(accC)
            BBA: Bd3861
            ADE: Adeh_0650
            PUB: SAR11_0726
            MLO: mll0203
            MES: Meso_1716
            SME: SMc01345(accC)
            ATU: Atu1330(accC) Atu3913 Atu4273(accC)
            ATC: AGR_C_2451 AGR_L_1177 AGR_L_1864
            RET: RHE_CH01869(accCch) RHE_PC00062(mccB) RHE_PC00191(accCc)
            RLE: RL2088(accC) pRL100436(accC) pRL120152
            BME: BMEI1063
            BMF: BAB1_0924(accC)
            BMS: BR0906(accC)
            BMB: BruAb1_0917(accC)
            BJA: bll3638 bll4290(accC)
            BRA: BRADO3500(accC)
            BBT: BBta_2437 BBta_4216(accC)
            RPA: RPA2144 RPA2435(accC) RPA2539
            RPB: RPB_2933 RPB_3020
            RPC: RPC_2869
            RPD: RPD_2431
            RPE: RPE_2988
            NWI: Nwi_1604 Nwi_1736 Nwi_1753 Nwi_2449(carB)
            NHA: Nham_2189
            BHE: BH08050(accC)
            BQU: BQ06530(accC)
            CCR: CC_1884
            SIL: SPO1010(accC)
            RSP: RSP_0191(accC)
            RDE: RD1_2851(accC)
            MMR: Mmar10_1265
            HNE: HNE_2250(accC)
            ZMO: ZMO0735(accC)
            NAR: Saro_2079
            SAL: Sala_1439
            ELI: ELI_03100
            GOX: GOX0213 GOX0435
            GBE: GbCGDNIH1_1957
            RRU: Rru_A0052 Rru_A2435
            MAG: amb2708
            MGM: Mmc1_0666
            ABA: Acid345_3287
            BSU: BG11384(accC) BG13459(yngH)
            BHA: BH1132 BH2787(accC)
            BAN: BA4408(accC)
            BAR: GBAA4408(accC)
            BAA: BA_4860
            BAT: BAS4088
            BCE: BC4183
            BCA: BCE_4257(accC)
            BCZ: BCZK3937(accC)
            BTK: BT9727_3926(accC)
            BTL: BALH_3792(accC)
            BLI: BL01530(accC) BL01988(yngH)
            BLD: BLi02143(yngH) BLi02605(accC)
            BCL: ABC1507 ABC2468(accC)
            OIH: OB1696 OB1885(accC)
            GKA: GK1599 GK2399
            SAU: SA1357(accC) SA1434
            SAV: SAV1526(accC) SAV1606
            SAM: MW1479(accC) MW1556
            SAR: SAR1604(accC) SAR1685
            SAS: SAS1465 SAS1542
            SAC: SACOL1661
            SAB: SAB1399c(accC) SAB1477c(accC)
            SEP: SE1207 SE1288
            SER: SERP1169
            SHA: SH1313 SH1389(accC)
            SSP: SSP1156
            LMO: lmo1357
            LMF: LMOf2365_1374(accC)
            LIN: lin1394
            LWE: lwe1372(accC)
            LLA: L0189(accC)
            LLC: LACR_0828
            LLM: llmg_1779(accC)
            SPY: SPy_1745(accC)
            SPZ: M5005_Spy_1486(accC)
            SPM: spyM18_1817(accC)
            SPG: SpyM3_1519(accC)
            SPS: SPs0347
            SPH: MGAS10270_Spy1553(accC) MGAS10270_Spy1554
            SPI: MGAS10750_Spy1545(accC)
            SPJ: MGAS2096_Spy1513(accC)
            SPK: MGAS9429_Spy1488(accC)
            SPF: SpyM50359(accC)
            SPA: M6_Spy1480
            SPB: M28_Spy1475(accC)
            SPN: SP_0425
            SPR: spr0385(accC)
            SAG: SAG0352(accC)
            SAN: gbs0339
            SAK: SAK_0426(accC)
            SMU: SMU.1736(accC)
            STC: str0391(accC)
            STL: stu0391(accC)
            SSA: SSA_1932(accC)
            LPL: lp_1678(accC2)
            LSA: LSA0820(accC)
            LSL: LSL_0458(accC)
            LDB: Ldb0907(accC)
            LBU: LBUL_0825
            LBR: LVIS_0928
            LCA: LSEI_2111
            EFA: EF2877(accC)
            STH: STH1191
            CAC: CAC3570(accC)
            CPE: CPE1074(accC)
            CPR: CPR_1142(accC)
            CTC: CTC00134
            CDF: CD1938(accC)
            CBO: CBO3596(accC)
            CBA: CLB_3676(accC)
            CBH: CLC_3574(accC)
            CBF: CLI_3821(accC)
            CKL: CKL_0110(accC)
            CHY: CHY_1998(accC2)
            MTU: Rv2501c(accA1) Rv3285(accA3)
            MTC: MT2576(bccA-2) MT3384(bccA-3)
            MBO: Mb0998c(accA2) Mb2529c(accA1) Mb3313(accA3)
            MBB: BCG_1027c(accA2) BCG_2521c(accA1) BCG_3314(accA3)
            MLE: ML0726(bccA)
            MPA: MAP2313c(accA1) MAP3404(accA3)
            MAV: MAV_1671 MAV_4255
            MSM: MSMEG_1807 MSMEG_4716 MSMEG_5493
            MMC: Mmcs_3630
            CGL: NCgl0670(cgl0700)
            CGB: cg0802(accBC)
            CEF: CE0719(accBC)
            CDI: DIP0649(accBC)
            CJK: jk0405(accBC3) jk1550(accBC1) jk1669(accBC2)
            NFA: nfa50380 nfa9890
            RHA: RHA1_ro04222 RHA1_ro06096(accC1) RHA1_ro08921
                 RHA1_ro10399(accC2)
            SCO: SCO2777(accC) SCO4921(accA2) SCO6271(accA1)
            SMA: SAV3337(accA3) SAV5277(accA1)
            TWH: TWT020(bccA)
            TWS: TW020
            LXX: Lxx04730(accC)
            CMI: CMM_0991(accA)
            AAU: AAur_1410(accA) AAur_1529(accA)
            PAC: PPA1719
            TFU: Tfu_0947 Tfu_1228 Tfu_2557
            FRA: Francci3_0698
            FAL: FRAAL1210(accC) FRAAL2344(accC) FRAAL3159(accC)
                 FRAAL3198(accC)
            SEN: SACE_0028 SACE_3154(accC3) SACE_4237 SACE_7038
            BLO: BL1535(jadJ)
            BAD: BAD_0254
            RBA: RB8550(accC)
            CTR: CT124(accC)
            CTA: CTA_0131(accC)
            CMU: TC0400
            CPN: CPn0182(accC)
            CPA: CP0586
            CPJ: CPj0182(accC)
            CPT: CpB0185
            CCA: CCA00554(accC)
            CAB: CAB540(accC)
            CFE: CF0454(accC)
            PCU: pc0772(accC)
            TDE: TDE0591(accC)
            LIL: LA2432(accC1)
            SYN: sll0053(accC)
            SYW: SYNW0336(accC)
            SYC: syc0177_c(accC)
            SYF: Synpcc7942_1379
            SYD: Syncc9605_2259
            SYE: Syncc9902_0421
            SYG: sync_2459(accC)
            SYR: SynRCC307_0341(accC)
            SYX: SynWH7803_2128(accC)
            CYA: CYA_0852(accC)
            CYB: CYB_1391(accC)
            TEL: tlr1808(accC)
            GVI: gll2012(accC)
            ANA: alr0939(accC)
            PMA: Pro0074(accC)
            PMM: PMM0060(accC)
            PMT: PMT1588(accC)
            PMN: PMN2A_1423
            PMI: PMT9312_0062
            PMB: A9601_00721(accC)
            PMC: P9515_00691(accC)
            PMF: P9303_03221(accC)
            PMG: P9301_00711(accC)
            PMH: P9215_00721
            PME: NATL1_01241(accC)
            BTH: BT_1449 BT_1915
            BFR: BF1612 BF3529
            BFS: BF1624(accC1) BF3337(accC2)
            SRU: SRU_0937(accC)
            CHU: CHU_1622(accC)
            GFO: GFO_0975 GFO_3345(accC)
            FPS: FP2377(accC)
            CTE: CT0157(accC)
            CCH: Cag_0359
            PLT: Plut_1960
            DET: DET0120(accC)
            DRA: DR_0117
            DGE: Dgeo_0466
            TTH: TTC0758
            TTJ: TTHA1123
            AAE: aq_1470(accC2) aq_1664(accC1)
            MSI: Msm_0765
            HWA: HQ2906A(accA2)
            NPH: NP4252A(accA_1) NP4368A(accA_2)
            HBU: Hbut_1157
STRUCTURES  PDB: 1BNC  1DV1  1DV2  2GPS  2GPW  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.14
            ExPASy - ENZYME nomenclature database: 6.3.4.14
            ExplorEnz - The Enzyme Database: 6.3.4.14
            ERGO genome analysis and discovery system: 6.3.4.14
            BRENDA, the Enzyme Database: 6.3.4.14
            CAS: 9075-71-2
///
ENTRY       EC 6.3.4.15                 Enzyme
NAME        biotin---[acetyl-CoA-carboxylase] ligase;
            biotin-[acetyl-CoA carboxylase] synthetase;
            biotin-[acetyl coenzyme A carboxylase] synthetase;
            acetyl coenzyme A holocarboxylase synthetase;
            acetyl CoA holocarboxylase synthetase;
            biotin:apocarboxylase ligase;
            Biotin holoenzyme synthetase;
            HCS
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     biotin:apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] ligase
            (AMP-forming)
REACTION    ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
            = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase
            (ADP-forming)] [RN:R04562]
ALL_REAC    R04562;
            (other) R01074 R05145
SUBSTRATE   ATP [CPD:C00002];
            biotin [CPD:C00120];
            apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] [CPD:C04735]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            [acetyl-CoA:carbon-dioxide ligase (ADP-forming)] [CPD:C04681]
REFERENCE   1  [PMID:239688]
  AUTHORS   Landman AD, Darkshinamurti K.
  TITLE     Acetyl-Coenzyme A carboxylase. Role of the prosthetic group in
            enzyme polymerization.
  JOURNAL   Biochem. J. 145 (1975) 545-8.
  ORGANISM  rat [GN:rno]
PATHWAY     PATH: map00780  Biotin metabolism
ORTHOLOGY   KO: K01947  biotin-[acetyl-CoA-carboxylase] ligase
GENES       HSA: 3141(HLCS)
            PTR: 473989(HLCS)
            MMU: 110948(Hlcs)
            RNO: 288240(RGD1565360_predicted)
            CFA: 478412(HLCS)
            BTA: 510590(LOC510590)
            GGA: 418516(HLCS)
            SCE: YDL141W(BPL1)
            AGO: AGOS_ADR085W
            PIC: PICST_69676(BPL1)
            CAL: CaO19_7645(CaO19.7645)
            SPO: SPBC30D10.07c
            ANI: AN6055.2
            AFM: AFUA_2G09550
            AOR: AO090011000708
            CNE: CNC00800
            UMA: UM03839.1
            DDI: DDBDRAFT_0188109 DDBDRAFT_0188228
            TET: TTHERM_01005310 TTHERM_01151480
            TBR: Tb11.01.1820
            TCR: 510719.60
            LMA: LmjF31.1070
            EHI: 26.t00001
            ECO: b3973(birA)
            ECJ: JW3941(birA)
            ECE: Z5544(birA)
            ECS: ECs4900
            ECC: c4932(birA)
            ECI: UTI89_C3803(birA)
            ECP: ECP_4187
            ECV: APECO1_2494(birA)
            ECW: EcE24377A_4512(birA)
            ECX: EcHS_A4207(birA)
            STY: STY3741(birA)
            STT: t3488(birA)
            SPT: SPA3977(birA)
            SEC: SC4026(birA)
            STM: STM4138(birA)
            YPE: YPO3759(birA)
            YPK: y0472(birA)
            YPM: YP_3289(birA)
            YPA: YPA_3428
            YPN: YPN_0206
            YPP: YPDSF_3380
            YPS: YPTB0273(birA)
            YPI: YpsIP31758_3871(birA)
            SFL: SF4051(birA)
            SFX: S3689(birA)
            SFV: SFV_4046(birA)
            SSN: SSON_4146(birA)
            SBO: SBO_3993(birA)
            SDY: SDY_3755(birA)
            ECA: ECA0214(birA)
            PLU: plu4732(birA)
            WBR: WGLp513(birA)
            SGL: SG0125
            ENT: Ent638_3943
            SPE: Spro_0268
            BFL: Bfl184(birA)
            BPN: BPEN_190(birA)
            HIN: HI0220.1(birA)
            HIT: NTHI0323(birA)
            HIP: CGSHiEE_01975
            HDU: HD0082(birA)
            HSO: HS_0419(birA)
            PMU: PM0296(birA)
            MSU: MS0775(birA)
            APL: APL_1850(birA)
            ASU: Asuc_0892
            XFA: XF1796
            XFT: PD1071(birA)
            XCC: XCC3938(birA)
            XCB: XC_4026
            XCV: XCV4110(birA)
            XAC: XAC4018(birA)
            XOO: XOO0428(birA)
            XOM: XOO_0390(XOO0390)
            VCH: VC0319
            VCO: VC0395_A2717(birA)
            VVU: VV1_1198 VV1_1199
            VVY: VV3169
            VPA: VP2931
            VFI: VF2425
            PPR: PBPRA3445
            PAE: PA4280(birA)
            PAU: PA14_08620(birA)
            PAP: PSPA7_0816
            PPU: PP_0437(birA)
            PPF: Pput_0470
            PST: PSPTO_0610(birA)
            PSB: Psyr_4564
            PSP: PSPPH_4612
            PFL: PFL_5601
            PFO: Pfl_5096
            PEN: PSEEN0471
            PMY: Pmen_3926
            PAR: Psyc_0315(birA)
            ACI: ACIAD0841
            SON: SO_0214(birA)
            SDN: Sden_0154
            SFR: Sfri_0132
            SAZ: Sama_0197
            SBL: Sbal_4174
            SBM: Shew185_0180
            SLO: Shew_0142
            SPC: Sputcn32_3775
            SSE: Ssed_4334
            SPL: Spea_0168
            SHE: Shewmr4_0182
            SHM: Shewmr7_0177
            SHN: Shewana3_0183
            SHW: Sputw3181_0140
            ILO: IL2003(birA)
            CPS: CPS_4745(birA)
            PHA: PSHAa2913(birA)
            PAT: Patl_3998
            SDE: Sde_0915
            PIN: Ping_0219
            CBU: CBU_1002(birA)
            CBD: COXBU7E912_1044(birA)
            LPN: lpg0783(birA)
            LPF: lpl0822(birA)
            LPP: lpp0847(birA)
            MCA: MCA1781(birA)
            FTU: FTT0477c(birA)
            FTF: FTF0477c(birA)
            FTW: FTW_0828(birA) FTW_1593
            FTL: FTL_1276 FTL_1586
            FTH: FTH_1249(birA1) FTH_1532(birA2)
            FTA: FTA_1349 FTA_1671
            FTN: FTN_0568 FTN_0811(birA)
            TCX: Tcr_1948
            NOC: Noc_0188
            AEH: Mlg_0440
            HCH: HCH_06234
            CSA: Csal_0406
            ABO: ABO_0368(birA)
            AHA: AHA_4040
            DNO: DNO_0541(birA)
            BCI: BCI_0505(birA)
            VOK: COSY_0880(birA)
            NME: NMB2075
            NMA: NMA0357(birA)
            NMC: NMC2054(birA)
            NGO: NGO2001(birA)
            CVI: CV_0486(birA)
            RSO: RSc0312(birA)
            REU: Reut_A0102
            REH: H16_A0135(birA) H16_A2946
            RME: Rmet_0073
            BMA: BMA0069
            BXE: Bxe_A4226
            BUR: Bcep18194_A6247
            BCN: Bcen_2290
            BCH: Bcen2424_2904
            BAM: Bamb_2953
            BPS: BPSL0398
            BPM: BURPS1710b_0609
            BPL: BURPS1106A_0447
            BPD: BURPS668_0428
            BTE: BTH_I0370
            BPE: BP0098(birA)
            BPA: BPP0160(birA)
            BBR: BB0161(birA)
            RFR: Rfer_3953
            POL: Bpro_4716
            MPT: Mpe_A0263
            HAR: HEAR2991
            MMS: mma_3240(birA)
            NEU: NE2460(birA)
            NET: Neut_0232
            NMU: Nmul_A2082
            EBA: ebA4113(birA)
            AZO: azo0734(birA)
            DAR: Daro_3757
            TBD: Tbd_0460
            MFA: Mfla_2081
            HPY: HP1140
            HPA: HPAG1_1078
            HHE: HH0421(birA)
            HAC: Hac_0574(birA)
            WSU: WS0508(birA)
            TDN: Tmden_1411
            CJE: Cj0099(birA)
            CJR: CJE0094
            CJJ: CJJ81176_0134
            CJU: C8J_0092
            CJD: JJD26997_0106
            CFF: CFF8240_1533
            CCV: CCV52592_1730
            CHA: CHAB381_0679
            CCO: CCC13826_0360
            ABU: Abu_1603(birA)
            NIS: NIS_1228
            SUN: SUN_1779
            GSU: GSU1935
            GME: Gmet_1987
            GUR: Gura_2817
            PCA: Pcar_1971
            PPD: Ppro_0654
            DVU: DVU1835 DVU2557(birA)
            DDE: Dde_2082 Dde_2654
            LIP: LI0026(birA)
            BBA: Bd2763(birA)
            DPS: DP0800
            ADE: Adeh_2388
            AFW: Anae109_1479
            MXA: MXAN_4152(birA)
            SAT: SYN_02884
            SFU: Sfum_2610 Sfum_3720
            RPR: RP533
            RTY: RT0521(birA)
            RCO: RC0773(birA)
            RFE: RF_0744(birA)
            RBE: RBE_0782(birA)
            WBM: Wbm0620
            AMA: AM389(birA)
            APH: APH_0876
            ERU: Erum2520
            ERW: ERWE_CDS_02560(birA)
            ECN: Ecaj_0240
            ECH: ECH_0848
            PUB: SAR11_0898(birA)
            MLO: mll1351(birA)
            MES: Meso_1036
            PLA: Plav_3212
            SME: SMc01928(birA)
            ATU: Atu1284(birA)
            ATC: AGR_C_2366(birA)
            RET: RHE_CH01619(birA)
            RLE: RL1715(birA)
            BME: BMEI1144
            BMF: BAB1_0836
            BMS: BR0816
            BMB: BruAb1_0830
            BJA: bll4903(birA)
            BRA: BRADO4170
            BBT: BBta_4547
            RPA: RPA2936(birA)
            RPB: RPB_2588 RPB_3299
            RPC: RPC_1056 RPC_2418
            RPD: RPD_2871
            RPE: RPE_2537
            NWI: Nwi_1873
            NHA: Nham_2206
            BHE: BH08810(birA)
            BQU: BQ05780(birA)
            BBK: BARBAKC583_0792
            CCR: CC_1936
            SIL: SPO2762
            SIT: TM1040_0761
            RSP: RSP_2532(birA)
            RSH: Rsph17029_1192
            RSQ: Rsph17025_1990
            JAN: Jann_1197
            RDE: RD1_3267
            PDE: Pden_2230
            MMR: Mmar10_1369
            HNE: HNE_1759
            ZMO: ZMO1868(birA)
            NAR: Saro_2286
            SAL: Sala_1295
            ELI: ELI_06595
            GOX: GOX0082
            GBE: GbCGDNIH1_1288
            RRU: Rru_A1321 Rru_A1569
            MAG: amb2773
            MGM: Mmc1_1476
            ABA: Acid345_0135
            BSU: BG11206(birA)
            BHA: BH1685(birA)
            BAN: BA1560(birA)
            BAR: GBAA1560(birA)
            BAA: BA_2078
            BAT: BAS1447
            BCE: BC1537
            BCA: BCE_1666(birA)
            BCZ: BCZK1420(birA)
            BCY: Bcer98_1261
            BTK: BT9727_1419(birA)
            BTL: BALH_1391
            BLI: BL02753(birA)
            BLD: BLi02379(birA)
            BCL: ABC2068(birA)
            BAY: RBAM_020590(birA)
            BPU: BPUM_1975(birA)
            OIH: OB1764(birA)
            GKA: GK2180(birA)
            SAU: SA1289
            SAV: SAV1456
            SAM: MW1346
            SAR: SAR1467(birA)
            SAS: SAS1399
            SAC: SACOL1496(birA)
            SAA: SAUSA300_1347(birA)
            SAO: SAOUHSC_01473
            SEP: SE1144
            SER: SERP1026(birA)
            SHA: SH1456
            SSP: SSP1288
            LMO: lmo1904(birA)
            LMF: LMOf2365_1933(birA)
            LIN: lin2018(birA)
            LWE: lwe1923(birA)
            LLA: L0191(birA1) L0192(birA2)
            LLC: LACR_1952
            LLM: llmg_1963(birA1) llmg_2162(birA2)
            SPY: SPy_1362(birA)
            SPZ: M5005_Spy_1110(birA)
            SPM: spyM18_1374(birA)
            SPG: SpyM3_1036(birA)
            SPS: SPs0824
            SPH: MGAS10270_Spy1180(birA)
            SPI: MGAS10750_Spy1209(birA)
            SPJ: MGAS2096_Spy1172(birA)
            SPK: MGAS9429_Spy1154(birA)
            SPF: SpyM50749(birA)
            SPA: M6_Spy1084
            SPB: M28_Spy1102(birA)
            SPN: SP_1900
            SPR: spr1715(birA)
            SPD: SPD_1680
            SAG: SAG0830
            SAN: gbs0848
            SAK: SAK_0953
            SMU: SMU.1578(birA)
            STC: str1173(birA)
            STL: stu1173(birA)
            SSA: SSA_0999(birA)
            SGO: SGO_0903(birA)
            LPL: lp_0337(birA1) lp_0854(birA2)
            LSA: LSA0824(birA1) LSA1233(birA2)
            LSL: LSL_0325(birA)
            LDB: Ldb0911(birA)
            LBR: LVIS_0924
            LCA: LSEI_0812
            EFA: EF3240(birA)
            OOE: OEOE_1596
            STH: STH1400
            CAC: CAC0212 CAC0589(birA)
            CPE: CPE0673(birA)
            CPF: CPF_0664(birA)
            CPR: CPR_0663(birA)
            CTC: CTC00852(birA)
            CDF: CD3558(birA)
            CBO: CBO1117(birA)
            CBA: CLB_1156(birA)
            CBH: CLC_1168(birA)
            CBF: CLI_1205(birA)
            AMT: Amet_4534
            CHY: CHY_2371(birA)
            DSY: DSY0215
            DRM: Dred_0168
            SWO: Swol_0775
            TTE: TTE1965(birA)
            MTA: Moth_0143
            MTU: Rv3279c(birA)
            MTC: MT3379(birA)
            MBO: Mb3307c(birA)
            MBB: BCG_3308c(birA)
            MLE: ML0732(birA)
            MPA: MAP3397c(birA)
            MAV: MAV_4248
            MSM: MSMEG_1822
            MMC: Mmcs_1304
            CGL: NCgl0679(cgl0709)
            CGB: cg0814(birA)
            CEF: CE0740(birA)
            CDI: DIP0661
            CJK: jk1661(birA)
            NFA: nfa9950(birA)
            RHA: RHA1_ro06293
            SCO: SCO4927(SCK13.19)
            TWH: TWT024(birA)
            TWS: TW026
            LXX: Lxx04800(birA)
            AAU: AAur_1420
            PAC: PPA1705
            TFU: Tfu_2553
            FRA: Francci3_0701
            FAL: FRAAL1213
            ACE: Acel_0398
            SEN: SACE_6501
            STP: Strop_0857
            BLO: BL1533
            BAD: BAD_0251
            FNU: FN1921
            RBA: RB5918(birA)
            CTR: CT725(birA)
            CTA: CTA_0787(birA)
            CMU: TC0098
            CPN: CPn0866(birA)
            CPA: CP1003
            CPJ: CPj0866(birA)
            CPT: CpB0894(birA)
            CCA: CCA00901
            CAB: CAB869(birA)
            CFE: CF0113(birA)
            PCU: pc0165(birA)
            TPA: TP0357
            TDE: TDE0041(birA)
            LIL: LA0832(birA)
            LIC: LIC12793
            LBJ: LBJ_0490(birA)
            LBL: LBL_2589(birA)
            SYN: sll1655(birA)
            SYW: SYNW1876(birA)
            SYC: syc1168_d(birA)
            SYF: Synpcc7942_0345
            SYD: Syncc9605_0591
            SYE: Syncc9902_1773
            SYG: sync_2109
            SYR: SynRCC307_0656(birA)
            SYX: SynWH7803_1888(birA)
            CYA: CYA_2270
            CYB: CYB_0457
            GVI: gll1338
            ANA: alr5256
            AVA: Ava_1418
            PMA: Pro0429(cirA)
            PMM: PMM0433(birA)
            PMT: PMT1359(birA)
            PMN: PMN2A_1765
            PMI: PMT9312_0432
            PMB: A9601_04881(birA)
            PMC: P9515_04951(birA)
            PMF: P9303_06231(birA)
            PMG: P9301_04571(birA)
            PME: NATL1_04871(birA)
            TER: Tery_3352
            BTH: BT_2238
            BFR: BF0704
            BFS: BF0632
            SRU: SRU_0529
            CHU: CHU_0611(birA)
            GFO: GFO_2692
            FPS: FP0601(birA)
            CTE: CT0053(birA)
            CCH: Cag_0077
            CPH: Cpha266_0111
            PLT: Plut_2071
            DET: DET0849
            DEH: cbdb_A832(birA)
            DRA: DR_2341
            DGE: Dgeo_2140
            TTH: TTC1761
            TTJ: TTHA0225
            AAE: aq_566(birA)
            TMA: TM0224
            MMP: MMP0119(birA)
            MAC: MA0676(bpl)
            MBA: Mbar_A1588
            MMA: MM_1829
            MBU: Mbur_2427
            MTP: Mthe_0793
            MHU: Mhun_3184
            MTH: MTH1916
            AFU: AF0074(birA)
            HAL: VNG1534a(birA)
            HMA: rrnAC0001(birA)
            HWA: HQ2905A(birA)
            NPH: NP4378A(birA2)
            PHO: PH0147
            PAB: PAB0096(birA) PAB0104(birA-like)
            PFU: PF0077 PF1676
            TKO: TK0747 TK0987
            RCI: RCIX1760(birA)
            SSO: SSO0662(bioR)
            STO: ST1525
            SAI: Saci_1641(birA)
STRUCTURES  PDB: 1BIA  1BIB  1HXD  1WNL  1WPY  1WQ7  1WQW  1X01  2CGH  2DEQ  
                 2DJZ  2DKG  2DTH  2DTI  2DTO  2DVE  2DXT  2DXU  2DZ9  2DZC  
                 2E10  2E3Y  2E41  2E64  2E65  2EAY  2EWN  2FYK  2HNI  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.15
            ExPASy - ENZYME nomenclature database: 6.3.4.15
            ExplorEnz - The Enzyme Database: 6.3.4.15
            ERGO genome analysis and discovery system: 6.3.4.15
            BRENDA, the Enzyme Database: 6.3.4.15
            CAS: 37340-95-7
///
ENTRY       EC 6.3.4.16                 Enzyme
NAME        carbamoyl-phosphate synthase (ammonia);
            carbon-dioxide---ammonia ligase;
            carbamoylphosphate synthase;
            carbamylphosphate synthetase;
            carbamoylphosphate synthase (ammonia);
            carbamoylphosphate synthetase;
            carbamylphosphate synthetase I
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     carbon-dioxide:ammonia ligase (ADP-forming,
            carbamate-phosphorylating)
REACTION    2 ATP + NH3 + CO2 + H2O = 2 ADP + phosphate + carbamoyl phosphate
            [RN:R00149]
ALL_REAC    R00149
SUBSTRATE   ATP [CPD:C00002];
            NH3 [CPD:C00014];
            CO2 [CPD:C00011];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            carbamoyl phosphate [CPD:C00169]
EFFECTOR    N-Acetyl-L-glutamate [CPD:C00624]
REFERENCE   1
  AUTHORS   Fahien, L.A. and Cohen, P.P.
  TITLE     A kinetic study of carbamyl phosphate synthetase.
  JOURNAL   J. Biol. Chem. 239 (1964) 1925-1934.
  ORGANISM  frog
REFERENCE   2
  AUTHORS   Jones, M.E. and Spector, L.
  TITLE     The pathway of carbonate in the biosynthesis of carbamyl phosphate.
  JOURNAL   J. Biol. Chem. 235 (1960) 2897-2901.
  ORGANISM  frog
REFERENCE   3
  AUTHORS   Marshall, M., Metzenberg, R.L. and Cohen, P.P.
  TITLE     Purification of carbamyl phosphate synthetase from frog liver.
  JOURNAL   J. Biol. Chem. 233 (1958) 102-105.
  ORGANISM  frog
REFERENCE   4
  AUTHORS   Marshall, M., Metzenberg, R.L. and Cohen, P.P.
  TITLE     Physical and kinetic properties of carbamyl phosphate synthetase
            from frog liver.
  JOURNAL   J. Biol. Chem. 236 (1961) 2229-2237.
  ORGANISM  frog
PATHWAY     PATH: map00220  Urea cycle and metabolism of amino groups
            PATH: map00251  Glutamate metabolism
            PATH: map00330  Arginine and proline metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K01948  carbamoyl-phosphate synthase (ammonia)
GENES       HSA: 1373(CPS1)
            MMU: 227231(Cps1)
            RNO: 497840(Cps1)
            GGA: 428994(CPS1)
            CAL: CaO19.2360
            TCR: 507059.80 511647.4
            BUR: Bcep18194_A4434(carB)
            ECN: Ecaj_0635
            HMA: rrnAC0002(accC2)
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.16
            ExPASy - ENZYME nomenclature database: 6.3.4.16
            ExplorEnz - The Enzyme Database: 6.3.4.16
            ERGO genome analysis and discovery system: 6.3.4.16
            BRENDA, the Enzyme Database: 6.3.4.16
            CAS: 9026-23-7
///
ENTRY       EC 6.3.4.17                 Enzyme
NAME        formate---dihydrofolate ligase;
            formyltransferase, dihydrofolate;
            dihydrofolate formyltransferase;
            formyl dihydrofolate synthase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     formate:dihydrofolate ligase (ADP-forming)
REACTION    ATP + formate + dihydrofolate = ADP + phosphate +
            10-formyldihydrofolate [RN:R02238]
ALL_REAC    R02238
SUBSTRATE   ATP [CPD:C00002];
            formate [CPD:C00058];
            dihydrofolate [CPD:C00415]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            10-formyldihydrofolate [CPD:C03204]
COMMENT     Not identical with EC 6.3.4.3 (formate---tetrahydrofolate ligase).
REFERENCE   1  [PMID:2306274]
  AUTHORS   Drake JC, Baram J, Allegra CJ.
  TITLE     Isolation and characterization of a novel dihydrofolate formylating
            enzyme from human MCF-7 breast cancer cells.
  JOURNAL   Biochem. Pharmacol. 39 (1990) 615-8.
  ORGANISM  human [GN:hsa]
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.17
            ExPASy - ENZYME nomenclature database: 6.3.4.17
            ExplorEnz - The Enzyme Database: 6.3.4.17
            ERGO genome analysis and discovery system: 6.3.4.17
            BRENDA, the Enzyme Database: 6.3.4.17
            CAS: 123303-25-3
///
ENTRY       EC 6.3.4.18                 Enzyme
NAME        5-(carboxyamino)imidazole ribonucleotide synthase;
            N5-CAIR synthetase;
            N5-carboxyaminoimidazole ribonucleotide synthetase;
            PurK
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon-nitrogen ligases
SYSNAME     5-amino-1-(5-phospho-D-ribosyl)imidazole:carbon-dioxide ligase
            (ADP-forming)
REACTION    ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole + HCO3- = ADP +
            phosphate + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
            [RN:R07404]
ALL_REAC    R07404
SUBSTRATE   ATP [CPD:C00002];
            5-amino-1-(5-phospho-D-ribosyl)imidazole [CPD:C03373];
            HCO3- [CPD:C00288]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole [CPD:C15667]
COMMENT     In Escherichia coli, this enzyme, along with EC 5.4.99.18,
            5-(carboxyamino)imidazole ribonucleotide mutase, is required to
            carry out the single reaction catalysed by EC 4.1.1.21,
            phosphoribosylaminoimidazole carboxylase, in vertebrates. Belongs to
            the ATP grasp protein superfamily [3]. Carboxyphosphate is the
            putative acyl phosphate intermediate. Involved in the late stages of
            purine biosynthesis.
REFERENCE   1  [PMID:1534690]
  AUTHORS   Meyer E, Leonard NJ, Bhat B, Stubbe J, Smith JM.
  TITLE     Purification and characterization of the purE, purK, and purC gene
            products: identification of a previously unrecognized energy
            requirement in the purine biosynthetic pathway.
  JOURNAL   Biochemistry. 31 (1992) 5022-32.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:8117684]
  AUTHORS   Mueller EJ, Meyer E, Rudolph J, Davisson VJ, Stubbe J.
  TITLE     N5-carboxyaminoimidazole ribonucleotide: evidence for a new
            intermediate and two new enzymatic activities in the de novo purine
            biosynthetic pathway of Escherichia coli.
  JOURNAL   Biochemistry. 33 (1994) 2269-78.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:10569930]
  AUTHORS   Thoden JB, Kappock TJ, Stubbe J, Holden HM.
  TITLE     Three-dimensional structure of N5-carboxyaminoimidazole
            ribonucleotide synthetase: a member of the ATP grasp protein
            superfamily.
  JOURNAL   Biochemistry. 38 (1999) 15480-92.
  ORGANISM  Escherichia coli [GN:eco]
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.4.18
            ExPASy - ENZYME nomenclature database: 6.3.4.18
            ExplorEnz - The Enzyme Database: 6.3.4.18
            ERGO genome analysis and discovery system: 6.3.4.18
            BRENDA, the Enzyme Database: 6.3.4.18
///
ENTRY       EC 6.3.4.-                  Enzyme
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Other carbon--nitrogen ligases
REACTION    Formate + ATP + 1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide
            <=> ADP + Orthophosphate +
            1-(5'-Phosphoribosyl)-5-formamido-4-imidazolecarboxamide [RN:R06975]
SUBSTRATE   Formate [CPD:C00058];
            ATP [CPD:C00002];
            1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide [CPD:C04677]
PRODUCT     ADP [CPD:C00008];
            Orthophosphate [CPD:C00009];
            1-(5'-Phosphoribosyl)-5-formamido-4-imidazolecarboxamide
            [CPD:C04734]
///
ENTRY       EC 6.3.5.1                  Enzyme
NAME        NAD+ synthase (glutamine-hydrolysing);
            NAD+ synthetase (glutamine-hydrolysing);
            nicotinamide adenine dinucleotide synthetase (glutamine);
            desamidonicotinamide adenine dinucleotide amidotransferase;
            DPN synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Carbon-nitrogen ligases with glutamine as amido-N-donor
SYSNAME     deamido-NAD+:L-glutamine amido-ligase (AMP-forming)
REACTION    ATP + deamido-NAD+ + L-glutamine + H2O = AMP + diphosphate + NAD+ +
            L-glutamate [RN:R00257]
ALL_REAC    R00257
SUBSTRATE   ATP [CPD:C00002];
            deamido-NAD+ [CPD:C00857];
            L-glutamine [CPD:C00064];
            H2O [CPD:C00001]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            NAD+ [CPD:C00003];
            L-glutamate [CPD:C00025]
COMMENT     NH3 can act instead of glutamine (cf. EC 6.3.1.5 NAD+ synthase).
REFERENCE   1  [PMID:13717628]
  AUTHORS   IMSANDE J.
  TITLE     Pathway of diphosphopyridine nucleotide biosynthesis in Escherichia
            coli.
  JOURNAL   J. Biol. Chem. 236 (1961) 1494-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:13717627]
  AUTHORS   IMSANDE J, HANDLER P.
  TITLE     Biosynthesis of diphosphopyridine nucleotide. III. Nicotinic acid
            mononucleotide pyrophos-phorylase.
  JOURNAL   J. Biol. Chem. 236 (1961) 525-30.
  ORGANISM  cow [GN:bta]
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00760  Nicotinate and nicotinamide metabolism
ORTHOLOGY   KO: K01950  NAD+ synthase (glutamine-hydrolysing)
GENES       HSA: 55191(NADSYN1)
            PTR: 451395(NADSYN1)
            MMU: 78914(Nadsyn1)
            RNO: 353255(Nadsyn1)
            CFA: 483674(NADSYN1)
            GGA: 422983(NADSYN1)
            DME: Dmel_CG9940
            CEL: C24F3.4
            ATH: AT1G55090
            OSA: 4342490
            CME: CMT488C
            SCE: YHR074W(QNS1)
            AGO: AGOS_AGR358W
            PIC: PICST_40885(QNS1)
            CGR: CAGL0J10758g
            SPO: SPCC553.02
            ANI: AN8203.2
            AFM: AFUA_5G03350
            AOR: AO090102000540
            CNE: CNK02550
            UMA: UM03555.1
            DDI: DDB_0231365
            PFA: PFI1310w
            TET: TTHERM_00474780
            TBR: Tb11.01.6500
            TCR: 427789.30 506221.80
            LMA: LmjF32.1670
            EHI: 131.t00025
            ECO: b1740(nadE)
            ECJ: JW1729(nadE)
            ECE: Z2770(nadE)
            ECS: ECs2446
            ECC: c2139(nadE)
            ECI: UTI89_C1934(nadE)
            ECP: ECP_1686
            ECV: APECO1_809(nadE)
            STY: STY1803(nadE)
            STT: t1189(nadE)
            SPT: SPA1534(nadE)
            SEC: SC1331(nadE)
            STM: STM1310(nadE)
            YPE: YPO2912(nadE)
            YPK: y1316
            YPM: YP_2544(nadE)
            YPA: YPA_2352
            YPN: YPN_1225
            YPP: YPDSF_2257
            YPS: YPTB2873(nadE)
            SFL: SF1486(nadE)
            SFX: S1603(nadE)
            SFV: SFV_1480(nadE)
            SSN: SSON_1418(nadE)
            SBO: SBO_1350(nadE)
            SDY: SDY_1540(nadE)
            ECA: ECA2412(nadE)
            PLU: plu3310(nadE)
            BUC: BU174(nadE)
            BAS: BUsg168(nadE)
            WBR: WGLp342(nadE)
            SGL: SG1866
            SPE: Spro_3650
            MSU: MS1888(nadE)
            XFA: XF1961
            XFT: PD0839(nadE)
            XCC: XCC3091
            XCB: XC_1067
            XCV: XCV3345(nadE)
            XAC: XAC3220
            XOO: XOO1595
            XOM: XOO_1479(XOO1479)
            VCH: VCA0207
            VCO: VC0395_1021(nadE)
            VVU: VV2_1599
            VVY: VVA0410
            VPA: VPA0412
            VFI: VFA0602(nadE)
            PPR: PBPRB0911(nadE)
            PAE: PA4920(nadE)
            PAU: PA14_64980(nadE)
            PPU: PP_4869(nadE)
            PST: PSPTO_4922(nadE)
            PSB: Psyr_0594
            PSP: PSPPH_2956
            PFL: PFL_0593(nadE) PFL_2468(nadE)
            PFO: Pfl_0547
            PEN: PSEEN4920(nadE)
            PAR: Psyc_0270(nadE)
            PCR: Pcryo_0296
            PRW: PsycPRwf_1882
            ACI: ACIAD2888
            SON: SO_2021(nadE)
            SDN: Sden_1432
            SFR: Sfri_1542
            SAZ: Sama_1552
            SBL: Sbal_2543
            SLO: Shew_1464
            SHW: Sputw3181_1714
            ILO: IL1186
            CPS: CPS_3918(nadE)
            PHA: PSHAa0075(nadE)
            PAT: Patl_3163
            SDE: Sde_2553
            PIN: Ping_3205
            MAQ: Maqu_0876
            CBU: CBU_0858(nadE)
            LPN: lpg0734
            LPF: lpl0771
            LPP: lpp0800
            MCA: MCA0969
            FTU: FTT1259(nadE)
            FTF: FTF1259(nadE)
            FTL: FTL_0685
            FTH: FTH_0687(nadE)
            FTN: FTN_1278(nadE)
            TCX: Tcr_1372
            NOC: Noc_2095(nadE)
            AEH: Mlg_2549
            HHA: Hhal_2238
            HCH: HCH_05923
            CSA: Csal_0495
            ABO: ABO_0474
            MMW: Mmwyl1_2961
            AHA: AHA_0697
            DNO: DNO_0197(nadE)
            RMA: Rmag_0520
            VOK: COSY_0477(nadE)
            NME: NMB1364
            NMA: NMA1576(nadE)
            NMC: NMC1299(nadE)
            NGO: NGO0654
            CVI: CV_1616(nadE)
            RSO: RSc2347(nadE)
            REU: Reut_A2610
            REH: H16_A0749(nadE)
            RME: Rmet_0680
            BMA: BMA0741(nadE-1) BMAA0760(nadE-2)
            BMV: BMASAVP1_0588(nadE-2) BMASAVP1_A2272(nadE-1)
            BML: BMA10299_0698(nadE-2) BMA10299_A3012(nadE-1)
            BMN: BMA10247_1585(nadE-1) BMA10247_A1653(nadE-2)
            BXE: Bxe_A3396 Bxe_B1989 Bxe_C0163
            BVI: Bcep1808_2500
            BUR: Bcep18194_A4513 Bcep18194_A5739
            BCN: Bcen_1800
            BCH: Bcen2424_2412 Bcen2424_5278
            BAM: Bamb_2457 Bamb_4638
            BPS: BPSL1026 BPSS1482(nadE)
            BPM: BURPS1710b_1242(nadE-1) BURPS1710b_A0515(nadE)
            BTE: BTH_I0882 BTH_II0919
            PNU: Pnuc_0684
            BPE: BP2700
            BPA: BPP1435
            BBR: BB2509
            RFR: Rfer_1699
            POL: Bpro_2309
            PNA: Pnap_1709 Pnap_3718
            AAV: Aave_0975 Aave_3120
            AJS: Ajs_1761
            VEI: Veis_1737
            MPT: Mpe_A2113
            HAR: HEAR1014(nadE)
            MMS: mma_1150 mma_1655
            NEU: NE1896(nadE)
            NET: Neut_2008
            NMU: Nmul_A2535
            EBA: ebA7049(nadE)
            AZO: azo1360(nadE)
            DAR: Daro_1290
            TBD: Tbd_0807
            MFA: Mfla_1886
            HPY: HP0329
            HPJ: jhp0312(nadE)
            HPA: HPAG1_0333
            HHE: HH1008(nadE)
            HAC: Hac_0991(nadE)
            WSU: WS0206(nadE)
            CJE: Cj0810(nadE)
            CJR: CJE0901(nadE)
            CJU: C8J_0761(nadE)
            NIS: NIS_0538
            SUN: SUN_0674
            GSU: GSU0652(nadE)
            GME: Gmet_2862(nadE)
            PCA: Pcar_2216(nadE)
            DVU: DVU1610(nadE)
            DVL: Dvul_1524
            DDE: Dde_2091
            LIP: LI0244(nadE)
            BBA: Bd3836(nadE)
            DPS: DP2919
            ADE: Adeh_0285
            AFW: Anae109_0311
            MXA: MXAN_6851
            SAT: SYN_01307
            SFU: Sfum_0572
            AMA: AM416(nadE)
            APH: APH_0852
            ERU: Erum2710(nadE)
            ERW: ERWE_CDS_02760(nadE)
            ERG: ERGA_CDS_02710(nadE)
            ECN: Ecaj_0261
            ECH: ECH_0822(nadE)
            PUB: SAR11_1149(nadE)
            MLO: mll0818 mll6744
            MES: Meso_1463 Meso_2881 Meso_4206
            PLA: Plav_1103
            SME: SMb20649(nadE1) SMc00161(nadE2)
            SMD: Smed_1566
            ATU: Atu1657(nadE)
            ATC: AGR_C_3052
            RET: RHE_CH01195(ypch00397) RHE_CH02371(nadE)
            RLE: RL2688(nadE)
            BME: BMEI0969
            BMF: BAB1_1033
            BMS: BR1015(nadE)
            BMB: BruAb1_1020(nadE)
            OAN: Oant_2097
            BJA: bll4547(nadE) blr3780(nadE)
            BRA: BRADO4702 BRADO6555(nadE)
            BBT: BBta_0979(nadE) BBta_3495
            RPA: RPA1986(nadE)
            RPB: RPB_3381
            RPC: RPC_2082
            RPD: RPD_2060
            RPE: RPE_1993
            NWI: Nwi_1225
            NHA: Nham_1485
            BHE: BH06450(nadE)
            BQU: BQ06780(nadE)
            BBK: BARBAKC583_0606(nadE)
            XAU: Xaut_1377
            CCR: CC_3619
            SIL: SPO0426(nadE)
            SIT: TM1040_2278
            RSP: RSP_2333(nadE)
            RSH: Rsph17029_1008
            RSQ: Rsph17025_1593
            JAN: Jann_3346
            RDE: RD1_1215(nadE)
            PDE: Pden_0853
            MMR: Mmar10_0982
            HNE: HNE_2577(nadE)
            NAR: Saro_0970
            SAL: Sala_2943
            SWI: Swit_2595
            ELI: ELI_08405
            GOX: GOX1121(nadE)
            GBE: GbCGDNIH1_0287
            ACR: Acry_1986
            RRU: Rru_A0687
            MAG: amb1233
            MGM: Mmc1_3593
            ABA: Acid345_2524
            SUS: Acid_0621 Acid_7496
            BSU: BG10694(nadE)
            BHA: BH2285(nadE)
            BAN: BA1998(nadE)
            BAR: GBAA1998(nadE)
            BAA: BA_2498
            BAT: BAS1855
            BCE: BC1994(nadE)
            BCA: BCE_2075(nadE)
            BCZ: BCZK1810(nadE)
            BTK: BT9727_1826(nadE)
            BTL: BALH_1767
            BLI: BL01706(nadE)
            BLD: BLi00370(nadE)
            BCL: ABC2151(nadE)
            BAY: RBAM_003360
            BPU: BPUM_0289
            OIH: OB0387(nadE)
            GKA: GK2596
            SAU: SA1728(nadE)
            SAV: SAV1912(nadE)
            SAM: MW1853(nadE)
            SAR: SAR2005
            SAS: SAS1836
            SAC: SACOL1974(nadE)
            SAB: SAB1849c
            SEP: SE1596
            SER: SERP1449(nadE)
            SHA: SH1040(nadE)
            SSP: SSP0879
            LMO: lmo1093
            LMF: LMOf2365_1107(nadE)
            LIN: lin1078
            LWE: lwe1068
            LLA: L0203(nadE)
            LLC: LACR_1204
            LLM: llmg_1470(nadE)
            SPY: SPy_1652(nadE)
            SPZ: M5005_Spy_1357(nadE)
            SPM: spyM18_1663(nadE)
            SPG: SpyM3_1392(nadE)
            SPS: SPs0470
            SPH: MGAS10270_Spy1474
            SPI: MGAS10750_Spy1466
            SPJ: MGAS2096_Spy1379
            SPK: MGAS9429_Spy1353
            SPF: SpyM50434(nadE)
            SPA: M6_Spy1403(nadE)
            SPB: M28_Spy1398(nadE)
            SPN: SP_1420
            SPR: spr1276(nadE)
            SAG: SAG0296(nadE)
            SAN: gbs0286(nadE)
            SAK: SAK_0368(nadE)
            SMU: SMU.465(nadE)
            STC: str0227(nadE)
            STL: stu0227(nadE)
            SSA: SSA_1863(nadE)
            LPL: lp_0566(nadE)
            LJO: LJ1733
            LAC: LBA0522(nadE)
            LSA: LSA1569(nadE)
            LSL: LSL_1260(nadE)
            LDB: Ldb0455(nadE)
            LBU: LBUL_0405
            LBR: LVIS_0544
            LCA: LSEI_1804
            LGA: LGAS_1527
            PPE: PEPE_1524
            EFA: EF2625(nadE)
            OOE: OEOE_0008
            CAC: CAC1050(nadE) CAC1782(nadE)
            CPE: CPE1058
            CTC: CTC00679(nadE)
            CNO: NT01CX_0103(nadE)
            CBO: CBO0537(nadE)
            CBA: CLB_0577(nadE)
            CBH: CLC_0461(nadE)
            CBF: CLI_0616(nadE)
            CKL: CKL_0992(nadE)
            CHY: CHY_1526(nadE)
            DSY: DSY0788(nadE)
            SWO: Swol_1437
            CSC: Csac_0122
            TTE: TTE0640(nadE)
            MTA: Moth_0553
            MPN: MPN562(outB)
            MPU: MYPU_6230(nadE)
            MPE: MYPE1940(nade)
            MMY: MSC_0440(nadE)
            MMO: MMOB1920(nadE)
            MHY: mhp471(nadE)
            MHJ: MHJ_0470(nadE)
            MHP: MHP7448_0473(nadE)
            MCP: MCAP_0531
            UUR: UU460(nadE)
            POY: PAM123 PAM124(nadE)
            AYW: AYWB_598(qns)
            MFL: Mfl521
            MTU: Rv2438c(nadE)
            MTC: MT2513
            MBO: Mb2464c(nadE)
            MBB: BCG_2457c(nadE)
            MLE: ML1463
            MPA: MAP2258c
            MAV: MAV_1737(nadE)
            MSM: MSMEG_4617(nadE)
            MMC: Mmcs_3543
            CGL: NCgl2446(nadE)
            CGB: cg2792(nadE)
            CEF: CE2428
            CDI: DIP1873(nadE)
            CJK: jk0474(nadE)
            NFA: nfa43120(nadE)
            SCO: SCO0506(nadE1) SCO2238(nadE)
            SMA: SAV5948(nadE)
            TWH: TWT405(nadE)
            TWS: TW365(nadE)
            LXX: Lxx12860
            PAC: PPA2266(nadE)
            TFU: Tfu_0983
            FRA: Francci3_3146
            FAL: FRAAL3251(nadE)
            ACE: Acel_0918
            KRA: Krad_3297
            SEN: SACE_1610(nadE)
            BLO: BL0953(nadE)
            BAD: BAD_0994(nadE)
            RXY: Rxyl_2763
            FNU: FN1202
            RBA: RB5671(nadE)
            BBU: BB0522
            BGA: BG0531
            BAF: BAPKO_0547
            TPA: TP0780
            TDE: TDE1400
            LIL: LA2989(nadE)
            LBJ: LBJ_2102(nadE)
            LBL: LBL_0949(nadE)
            SYN: slr1691(nadE)
            SYW: SYNW0502(nadE)
            SYC: syc1399_d(nadE)
            SYF: Synpcc7942_0105
            SYD: Syncc9605_2180
            SYE: Syncc9902_0495
            SYR: SynRCC307_1870(nadE)
            SYX: SynWH7803_2009(nadE)
            TEL: tlr1180
            GVI: glr2587
            ANA: alr2485
            AVA: Ava_0417(nadE)
            PMA: Pro1599(nadE)
            PMM: PMM1446
            PMT: PMT1461
            PMN: PMN2A_0977
            PMI: PMT9312_1539
            PMB: A9601_16481(nadE)
            PMC: P9515_16251(nadE)
            PMF: P9303_04891(nadE)
            PMG: P9301_16361(nadE)
            PME: NATL1_18451(nadE)
            TER: Tery_1984
            BTH: BT_0205
            BFR: BF3182
            BFS: BF3022
            PGI: PG0531(nadE)
            SRU: SRU_0403
            CHU: CHU_2417
            FPS: FP2070(nadE)
            CTE: CT0560(nadE)
            CCH: Cag_1075
            DET: DET1122
            DEH: cbdb_A1049(nadE)
            DEB: DehaBAV1_0951
            DRA: DR_A0201
            TTH: TTC1538
            TTJ: TTHA1900
            AAE: aq_959(nadE)
            TMA: TM0645 TM1253
            TME: Tmel_1404
            FNO: Fnod_0767
            MJA: MJ1352(nadE)
            MMP: MMP1349
            MAC: MA3526 MA3715
            MBA: Mbar_A0269 Mbar_A2320
            MMA: MM_0446 MM_0612(nadE)
            MTP: Mthe_0727
            MHU: Mhun_2601
            MEM: Memar_1435
            MTH: MTH1510
            MSI: Msm_1171
            MKA: MK1418(nadE)
            HAL: VNG2031G(nadE)
            HMA: pNG7227(nadE2) rrnAC2486(nadE1)
            HWA: HQ1091A(nadE) HQ2580A(nadE)
            NPH: NP0054A(nadE_2) NP3828A(nadE_1)
            TAC: Ta0899
            TVO: TVN1017
            PTO: PTO0986
            PAB: PAB2244(nadE)
            PFU: PF0098
            TKO: TK1798
            APE: APE_1958.1
            SSO: SSO2172(nadE)
            STO: ST2159 ST2160
            SAI: Saci_0008 Saci_0009(nadE)
            PAI: PAE1219
STRUCTURES  PDB: 1EE1  1FYD  1IFX  1IH8  1KQP  1NSY  2NSY  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.5.1
            ExPASy - ENZYME nomenclature database: 6.3.5.1
            ExplorEnz - The Enzyme Database: 6.3.5.1
            ERGO genome analysis and discovery system: 6.3.5.1
            BRENDA, the Enzyme Database: 6.3.5.1
            CAS: 37318-70-0
///
ENTRY       EC 6.3.5.2                  Enzyme
NAME        GMP synthase (glutamine-hydrolysing);
            GMP synthetase (glutamine-hydrolysing);
            guanylate synthetase (glutamine-hydrolyzing);
            guanosine monophosphate synthetase (glutamine-hydrolyzing);
            xanthosine 5'-phosphate amidotransferase;
            guanosine 5'-monophosphate synthetase
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Carbon-nitrogen ligases with glutamine as amido-N-donor
SYSNAME     xanthosine-5'-phosphate:L-glutamine amido-ligase (AMP-forming)
REACTION    ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP +
            diphosphate + GMP + L-glutamate [RN:R01231]
ALL_REAC    R01231
SUBSTRATE   ATP [CPD:C00002];
            xanthosine 5'-phosphate [CPD:C00655];
            L-glutamine [CPD:C00064];
            H2O [CPD:C00001]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            GMP [CPD:C00144];
            L-glutamate [CPD:C00025]
INHIBITOR   Psicofuranin [CPD:C05342]
REFERENCE   1
  AUTHORS   Abrams, R. and Bentley, M.
  TITLE     Biosynthesis of nucleic acid purines. III. Guanosine 5'-phosphate
            formation from xanthosine 5'-phosphate and L-glutamine.
  JOURNAL   Arch. Biochem. Biophys. 79 (1959) 91-110.
  ORGANISM  pigeon
REFERENCE   2  [PMID:13563458]
  AUTHORS   LAGERKVIST U.
  TITLE     Biosynthesis of guanosine 5'-phosphate. II. Amination of xanthosine
            5'-phosphate by purified enzyme from pigeon liver.
  JOURNAL   J. Biol. Chem. 233 (1958) 143-9.
  ORGANISM  pigeon
PATHWAY     PATH: map00230  Purine metabolism
            PATH: map00251  Glutamate metabolism
ORTHOLOGY   KO: K01951  GMP synthase (glutamine-hydrolysing)
GENES       HSA: 8833(GMPS)
            MMU: 229363(Gmps)
            RNO: 295088(Gmps)
            CFA: 477123(GMPS)
            BTA: 511200(GMPS)
            GGA: 425028(GMPS)
            DRE: 393559(gmps)
            SPU: 578500(LOC578500)
            DME: Dmel_CG9242(bur)
            ATH: AT1G63660
            OSA: 4345281
            CME: CML167C
            SCE: YMR217W(GUA1)
            AGO: AGOS_AER350W
            PIC: PICST_70121(GUA1)
            CGR: CAGL0F03927g CAGL0M04213g
            SPO: SPAP7G5.02c SPBPB2B2.05
            ANI: AN5566.2
            AFM: AFUA_3G01110 AFUA_4G03700
            AOR: AO090026000141
            CNE: CNK02180
            UMA: UM04050.1
            DDI: DDB_0215334(guaA)
            PFA: PF10_0123
            CPV: cgd5_4520
            CHO: Chro.50499
            TAN: TA06065
            TPV: TP01_0862
            TBR: Tb927.7.2100
            TCR: 511807.110
            LMA: LmjF22.0110
            ECO: b2507(guaA)
            ECJ: JW2491(guaA)
            ECE: Z3771(guaA)
            ECS: ECs3369
            ECC: c3026(guaA)
            ECI: UTI89_C2825(guaA)
            ECP: ECP_2509
            ECV: APECO1_4019(guaA)
            ECW: EcE24377A_2791(guaA)
            ECX: EcHS_A2658(guaA)
            STY: STY2751(guaA)
            STT: t0347(guaA)
            SPT: SPA0357(guaA)
            SEC: SC2508(guaA)
            STM: STM2510(guaA)
            YPE: YPO2870(guaA)
            YPK: y1363(guaA)
            YPM: YP_2736(guaA)
            YPA: YPA_2311
            YPN: YPN_1268
            YPS: YPTB2832(guaA)
            YPI: YpsIP31758_1196(guaA)
            SFL: SF2553(guaA)
            SFX: S2725(guaA)
            SFV: SFV_2554(guaA)
            SSN: SSON_2589(guaA)
            SBO: SBO_2531(guaA)
            SDY: SDY_2703(guaA)
            ECA: ECA3208(guaA)
            PLU: plu2712(guaA)
            WBR: WGLp606(guaA)
            SGL: SG1748
            BFL: Bfl527(guaA)
            BPN: BPEN_546(guaA)
            HIN: HI0222(guaA)
            HIT: NTHI0326(guaA)
            HIP: CGSHiEE_01965(guaA)
            HDU: HD1504(guaA)
            HSO: HS_0421(guaA)
            PMU: PM0293(guaA)
            MSU: MS0772(guaA)
            APL: APL_0592(guaA)
            XFA: XF0560 XF2429(guaA)
            XFT: PD1447(guaA) PD1582(guaA)
            XCC: XCC2183(guaA) XCC4089(guaA)
            XCB: XC_1935 XC_4180
            XCV: XCV2485(guaA) XCV4317(guaA)
            XAC: XAC2287(guaA) XAC4214(guaA)
            XOO: XOO2195(guaA) XOO4404(guaA)
            XOM: XOO_2063(XOO2063) XOO_4148(XOO4148)
            VCH: VC0768
            VCO: VC0395_A0297(guaA)
            VVU: VV1_0418
            VVY: VV0776
            VPA: VP0617
            VFI: VF0638(guaA)
            PPR: PBPRA0781
            PAE: PA3769(guaA)
            PAU: PA14_15340(guaA) PA14_42010
            PPU: PP_1032(guaA)
            PST: PSPTO_1450(guaA)
            PSB: Psyr_1262
            PSP: PSPPH_1334(guaA)
            PFL: PFL_4939(guaA)
            PFO: Pfl_4587
            PEN: PSEEN1544 PSEEN4392(guaA)
            PAR: Psyc_0009(guaA)
            PCR: Pcryo_0016
            PRW: PsycPRwf_0015
            ACI: ACIAD0151(guaA)
            SON: SO_3292(guaA)
            SDN: Sden_1270
            SFR: Sfri_1138
            SLO: Shew_1298
            SHE: Shewmr4_1235
            SHM: Shewmr7_1306
            SHN: Shewana3_1236
            ILO: IL0579(guaA)
            CPS: CPS_4241(guaA)
            PHA: PSHAa0649(guaA)
            PAT: Patl_3119
            SDE: Sde_1460
            CBU: CBU_1341(guaA)
            CBD: COXBU7E912_1430(guaA)
            LPN: lpg1722(guaA)
            LPF: lpl1686(guaA)
            LPP: lpp1687(guaA)
            MCA: MCA0290(guaA)
            FTU: FTT0909 FTT1019c(guaA)
            FTF: FTF0909 FTF1019c(guaA)
            FTW: FTW_0926(guaA)
            FTL: FTL_1071
            FTH: FTH_0422(guaA1) FTH_0782 FTH_1046(guaA2)
            FTA: FTA_1130
            FTN: FTN_0435 FTN_0897(guaA)
            TCX: Tcr_1615
            NOC: Noc_0614 Noc_2237
            AEH: Mlg_1016
            HCH: HCH_04533(guaA) HCH_04942
            CSA: Csal_0731
            ABO: ABO_0051(guaA) ABO_1850(guaA)
            AHA: AHA_1990 AHA_2408
            DNO: DNO_0380(guaA)
            BCI: BCI_0650(guaA)
            VOK: COSY_0820(guaA)
            NME: NMB1920
            NMA: NMA0534(guaA)
            NMC: NMC0303(guaA)
            NGO: NGO2164(guaA)
            CVI: CV_3465(guaA)
            RSO: RSc1431(guaA)
            REU: Reut_A1854(guaA)
            REH: H16_A2028(guaA)
            RME: Rmet_1463
            BMA: BMA1522(guaA)
            BMV: BMASAVP1_A2021(guaA)
            BML: BMA10299_A3290(guaA)
            BMN: BMA10247_1292(guaA)
            BXE: Bxe_A1708
            BVI: Bcep1808_1895
            BUR: Bcep18194_A3252 Bcep18194_A5299(guaA)
            BCN: Bcen_6088
            BCH: Bcen2424_1989
            BAM: Bamb_2022
            BPS: BPSL2127(guaA)
            BPM: BURPS1710b_2546(guaA)
            BPL: BURPS1106A_2454
            BPD: BURPS668_2402(guaA)
            BTE: BTH_I2058
            PNU: Pnuc_1422
            BPE: BP2624(guaA)
            BPA: BPP1259(guaA)
            BBR: BB2327(guaA)
            RFR: Rfer_2287
            POL: Bpro_2441
            PNA: Pnap_2000
            AAV: Aave_3367
            AJS: Ajs_2547
            VEI: Veis_1245
            MPT: Mpe_A1622
            HAR: HEAR1361(guaA)
            MMS: mma_2032(guaA) mma_3646
            NEU: NE0094(guaA)
            NET: Neut_2251
            NMU: Nmul_A1199
            EBA: ebA6645(guaA)
            AZO: azo1581(guaA)
            DAR: Daro_2337
            TBD: Tbd_1751(guaA)
            MFA: Mfla_1139 Mfla_1302
            HPY: HP0409(guaA)
            HPA: HPAG1_0983
            HHE: HH1444(guaA)
            HAC: Hac_0466(guaA)
            WSU: WS1603(guaA)
            TDN: Tmden_0422
            CJE: Cj1248(guaA)
            CJR: CJE1385(guaA)
            CJJ: CJJ81176_1264(guaA)
            CJU: C8J_1191(guaA)
            CJD: JJD26997_0477(guaA)
            CFF: CFF8240_1264
            CCV: CCV52592_0940
            CHA: CHAB381_0625 CHAB381_0638
            CCO: CCC13826_0475
            ABU: Abu_0921(guaA) Abu_1475
            NIS: NIS_1339(guaA)
            SUN: SUN_1897(guaA)
            GSU: GSU2194(guaA)
            GME: Gmet_2292
            PCA: Pcar_1218
            DVU: DVU1043(guaA)
            DDE: Dde_1470
            LIP: LI0590(guaA)
            BBA: Bd2080(guaA)
            DPS: DP0903
            ADE: Adeh_2348
            MXA: MXAN_3775(guaA)
            SAT: SYN_00475 SYN_01626
            SFU: Sfum_2123 Sfum_3619
            WOL: WD0195(guaA)
            WBM: Wbm0443
            AMA: AM1188(guaA)
            APH: APH_1233(guaA)
            ERU: Erum0740(guaA)
            ERW: ERWE_CDS_00680(guaA)
            ERG: ERGA_CDS_00650(guaA)
            ECN: Ecaj_0074(guaA)
            ECH: ECH_0123(guaA)
            NSE: NSE_0887(guaA)
            PUB: SAR11_0651(guaA)
            MLO: mlr6950
            MES: Meso_0495
            SME: SMc00394(guaA)
            ATU: Atu0281(guaA)
            ATC: AGR_C_480
            RET: RHE_CH00297(guaA1)
            RLE: RL0251 RL0315(guaA)
            BME: BMEII0887
            BMF: BAB2_0842(guaA)
            BMS: BRA0361(guaA)
            BMB: BruAb2_0821(guaA)
            BOV: BOV_A0328(guaA)
            BJA: blr3989(guaA)
            BRA: BRADO0854 BRADO0859 BRADO3169(guaA)
            BBT: BBta_3614(guaA) BBta_7207 BBta_7211
            RPA: RPA2203(guaA)
            RPB: RPB_3189
            RPC: RPC_3063
            RPD: RPD_2269
            RPE: RPE_3262
            NWI: Nwi_2143
            NHA: Nham_2542
            BHE: BH01820(guaA)
            BQU: BQ01710(guaA)
            BBK: BARBAKC583_0344(guaA)
            CCR: CC_1620
            SIL: SPO2109(guaA)
            SIT: TM1040_1375 TM1040_1837
            RSP: RSP_0005(guaA)
            RSH: Rsph17029_1635
            RSQ: Rsph17025_1867
            JAN: Jann_1126 Jann_2221
            RDE: RD1_1893 RD1_2778
            MMR: Mmar10_1184
            HNE: HNE_1808(guaA)
            ZMO: ZMO1267(guaA)
            NAR: Saro_0550
            SAL: Sala_0634
            ELI: ELI_11710
            GOX: GOX1950
            GBE: GbCGDNIH1_0068 GbCGDNIH1_1150
            RRU: Rru_A0299 Rru_A0355 Rru_A3512
            MAG: amb0732
            MGM: Mmc1_3014
            ABA: Acid345_1793
            BSU: BG10647(guaA)
            BHA: BH0607(guaA)
            BAN: BA0268(guaA)
            BAR: GBAA0268(guaA)
            BAA: BA_0840
            BAT: BAS0254
            BCE: BC0296(guaA)
            BCA: BCE_0291(guaA)
            BCZ: BCZK0243(guaA)
            BTK: BT9727_0240(guaA)
            BTL: BALH_0254(guaA)
            BLI: BL00920(guaA)
            BLD: BLi00686(guaA)
            BCL: ABC0936(guaA)
            BAY: RBAM_006760(guaA)
            BPU: BPUM_0548(guaA)
            OIH: OB0716(guaA)
            GKA: GK0254(guaA)
            GTN: GTNG_0231(guaA)
            SAU: SA0376(guaA)
            SAV: SAV0391(guaA)
            SAM: MW0367(guaA)
            SAR: SAR0409(guaA)
            SAS: SAS0367(guaA)
            SAC: SACOL0461(guaA)
            SAB: SAB0341(guaA)
            SAA: SAUSA300_0389(guaA)
            SAO: SAOUHSC_00375
            SEP: SE2347
            SER: SERP0070(guaA)
            SHA: SH2582(guaA)
            SSP: SSP2322
            LMO: lmo1096(guaA)
            LMF: LMOf2365_1110(guaA)
            LIN: lin1081(guaA)
            LWE: lwe1071(guaA)
            LLA: L115968(guaA)
            LLC: LACR_1583
            LLM: llmg_1008(guaA)
            SPY: SPy_1204(guaA)
            SPZ: M5005_Spy_0919(guaA)
            SPM: spyM18_1155(guaA)
            SPG: SpyM3_0845(guaA)
            SPS: SPs1045
            SPH: MGAS10270_Spy1033(guaA)
            SPI: MGAS10750_Spy1068(guaA)
            SPJ: MGAS2096_Spy0978(guaA)
            SPK: MGAS9429_Spy1021(guaA)
            SPF: SpyM50879(guaA)
            SPA: M6_Spy0908(guaA)
            SPB: M28_Spy0891(guaA)
            SPN: SP_1445
            SPR: spr1300(guaA)
            SPD: SPD_1274(guaA)
            SAG: SAG0967(guaA)
            SAN: gbs0953
            SAK: SAK_1062(guaA)
            SMU: SMU.1066(guaA)
            STC: str0886(guaA)
            STL: stu0886(guaA)
            STE: STER_0912
            SSA: SSA_1163(guaA) SSA_2133
            SSU: SSU05_0873
            SSV: SSU98_0876
            SGO: SGO_1120(guaA)
            LPL: lp_0914(guaA)
            LJO: LJ0229
            LAC: LBA0245(guaA)
            LSA: LSA0139(guaA)
            LSL: LSL_0172(guaA) LSL_0339(guaA) LSL_1537(guaA)
            LDB: Ldb0298(guaA)
            LBU: LBUL_0252
            LBR: LVIS_1759
            LCA: LSEI_1979
            LGA: LGAS_0231
            PPE: PEPE_0412
            EFA: EF0167(guaA)
            OOE: OEOE_1123
            STH: STH501
            CAC: CAC2700(guaA)
            CPE: CPE2275(guaA)
            CPF: CPF_2557(guaA)
            CPR: CPR_2260(guaA)
            CTC: CTC02409(guaA)
            CNO: NT01CX_0459
            CTH: Cthe_0375
            CDF: CD0198(guaA)
            CBO: CBO3295(guaA)
            CBA: CLB_3351(guaA)
            CBH: CLC_3237(guaA)
            CBF: CLI_3465(guaA)
            CKL: CKL_0466(guaA)
            CHY: CHY_1068(guaA)
            DSY: DSY3938
            DRM: Dred_2375
            PTH: PTH_2551
            SWO: Swol_1784
            CSC: Csac_1978
            TTE: TTE0583(guaA)
            MTA: Moth_2105
            MPE: MYPE1220(guaA)
            MFL: Mfl342
            MTU: Rv3396c(guaA)
            MTC: MT3504(guaA)
            MBO: Mb3429c(guaA)
            MBB: BCG_3466c(guaA)
            MLE: ML0395(guaA)
            MPA: MAP3489c(guaA)
            MAV: MAV_4348
            MSM: MSMEG_1610
            MMC: Mmcs_1173
            CGL: NCgl0582(guaA) NCgl1484(cgl1542)
            CGB: cg0703(guaA)
            CEF: CE0615(guaA)
            CDI: DIP0595(guaA)
            CJK: jk1720(guaA)
            NFA: nfa8970(guaA)
            RHA: RHA1_ro06202(guaA)
            SCO: SCO4785(guaA)
            SMA: SAV3479(guaA)
            TWH: TWT079(guaA)
            TWS: TW089(guaA)
            LXX: Lxx19780(guaA)
            CMI: CMM_2554(guaA)
            AAU: AAur_2857(guaA)
            PAC: PPA1764(guaA)
            TFU: Tfu_2589
            FRA: Francci3_0645
            FAL: FRAAL1150(guaA)
            ACE: Acel_0371
            SEN: SACE_6701(guaA)
            BLO: BL0960(guaA)
            BAD: BAD_0686(guaA)
            RXY: Rxyl_0816
            FNU: FN1444
            RBA: RB8374(guaA)
            CMU: TC0442
            CPN: CPn0171(guaA)
            CPA: CP0599
            CPJ: CPj0171(guaA)
            CPT: CpB0173
            CCA: CCA00573(guaA)
            CFE: CF0428(guaA)
            BBU: BBB18(guaA)
            BGA: BGB17(guaA)
            BAF: BAPKO_5017(guaA)
            TDE: TDE1718(guaA)
            LIL: LA2087
            LIC: LIC11831(guaA)
            LBJ: LBJ_1923(guaA-2)
            LBL: LBL_1361(guaA-2)
            SYN: slr0213(guaA)
            SYW: SYNW0047(guaA)
            SYC: syc1322_d(guaA)
            SYF: Synpcc7942_0189
            SYD: Syncc9605_0046(guaA)
            SYE: Syncc9902_0042(guaA)
            SYG: sync_0047(guaA)
            SYR: SynRCC307_0049(guaA)
            SYX: SynWH7803_0048(guaA)
            CYA: CYA_1673(guaA)
            CYB: CYB_1168(guaA)
            TEL: tll2418(guaA)
            GVI: glr2615(guaA)
            ANA: all2846
            AVA: Ava_1054(guaA)
            PMA: Pro0038(guaA)
            PMM: PMM0037(guaA)
            PMT: PMT0045(guaA)
            PMN: PMN2A_1363
            PMI: PMT9312_0037
            PMB: A9601_00361 A9601_11651
            PMC: P9515_00361 P9515_11501
            PMF: P9303_00451 P9303_09111
            PMG: P9301_00361 P9301_11661
            PMH: P9215_00351(guaA)
            PME: NATL1_00351 NATL1_15261
            TER: Tery_0907
            BTH: BT_2419 BT_4265
            BFR: BF0969
            BFS: BF0887(guaA)
            PGI: PG0589(guaA)
            SRU: SRU_0975(guaA) SRU_2075
            CHU: CHU_0934(guaA)
            GFO: GFO_2228(guaA)
            FPS: FP1894(guaA)
            CTE: CT0175(guaA)
            CCH: Cag_0589
            PLT: Plut_1946
            DET: DET0836(guaA)
            DEH: cbdb_A817(guaA)
            DRA: DR_1874
            DGE: Dgeo_0598
            TTH: TTC1187
            TTJ: TTHA1552
            AAE: aq_236(guaA)
            TMA: TM1820
            MMP: MMP0894(guaA) MMP1445(guaA)
            MMQ: MmarC5_0702
            MAC: MA4511(guaA) MA4590(guaA)
            MBA: Mbar_A0919 Mbar_A1178
            MMA: MM_1218 MM_1270 MM_2180
            MBU: Mbur_0058 Mbur_2002
            MTP: Mthe_0226
            MHU: Mhun_1588 Mhun_2527
            MLA: Mlab_1133
            MEM: Memar_0736 Memar_1900
            MBN: Mboo_2139
            MST: Msp_1311 Msp_1312
            MSI: Msm_0343 Msm_0345
            MKA: MK0363(guaA_1) MK0551(guaA_2)
            HAL: VNG0228G(guaAa) VNG1829G(guaAb)
            HMA: rrnAC1694(guaA2) rrnAC2924(guaA3) rrnAC3472(guaA1)
                 rrnB0283(guaA4)
            HWA: HQ1289A(guaAa) HQ3194A(guaAb) HQ3668A(guaA)
            NPH: NP0620A(guaAa_1) NP0794A(guaAa_2) NP1970A(guaAb)
                 NP2928A(guaAa_4) NP6256A(guaAa_3)
            TAC: Ta0944m Ta1361
            TVO: TVN0293 TVN1088
            PTO: PTO0516 PTO1342
            PAB: PAB0549(guaA-N) PAB2417(guaA-C)
            PFU: PF1515 PF1516
            TKO: TK0190 TK0193
            RCI: RCIX1576(guaA-2) RCIX404(guaA-1)
            APE: APE_2452
            SSO: SSO2451(guaA) SSO3232(guaA)
            STO: ST0578 ST2345
            SAI: Saci_0414 Saci_0548
            PAI: PAE3369
STRUCTURES  PDB: 1GPM  1WL8  2A9V  2D7J  2DPL  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.5.2
            ExPASy - ENZYME nomenclature database: 6.3.5.2
            ExplorEnz - The Enzyme Database: 6.3.5.2
            ERGO genome analysis and discovery system: 6.3.5.2
            BRENDA, the Enzyme Database: 6.3.5.2
            CAS: 37318-71-1
///
ENTRY       EC 6.3.5.3                  Enzyme
NAME        phosphoribosylformylglycinamidine synthase;
            phosphoribosylformylglycinamidine synthetase;
            formylglycinamide ribonucloetide amidotransferase;
            phosphoribosylformylglycineamidine synthetase;
            FGAM synthetase;
            FGAR amidotransferase;
            5'-phosphoribosylformylglycinamide:L-glutamine amido-ligase
            (ADP-forming);
            2-N-formyl-1-N-(5-phospho-D-ribosyl)glycinamide:L-glutamine
            amido-ligase (ADP-forming)
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Carbon-nitrogen ligases with glutamine as amido-N-donor
SYSNAME     N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide:L-glutamine
            amido-ligase (ADP-forming)
REACTION    ATP + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine +
            H2O = ADP + phosphate +
            2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine + L-glutamate
            [RN:R04463]
ALL_REAC    R04463
SUBSTRATE   ATP [CPD:C00002];
            N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide [CPD:C04376];
            L-glutamine [CPD:C00064];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine [CPD:C04640];
            L-glutamate [CPD:C00025]
REFERENCE   1  [PMID:13416226]
  AUTHORS   MELNICK I, BUCHANAN JM.
  TITLE     Biosynthesis of the purines.  XIV.  Conversion of (alpha-N-formyl)
            glycinamide ribotide to (alpha-N-formyl) glycinamidine ribotide;
            purification and requirements of the enzyme system.
  JOURNAL   J. Biol. Chem. 225 (1957) 157-62.
  ORGANISM  pigeon
PATHWAY     PATH: map00230  Purine metabolism
ORTHOLOGY   KO: K01952  phosphoribosylformylglycinamidine synthase
GENES       HSA: 5198(PFAS)
            PTR: 455093(PFAS)
            MMU: 237823(Pfas)
            CFA: 489490(PFAS)
            SPU: 576564(LOC576564)
            DME: Dmel_CG9127(ade2)
            CEL: F10F2.2
            ATH: AT1G74260
            OSA: 4324899
            CME: CMQ365C
            SCE: YGR061C(ADE6)
            AGO: AGOS_AFR573C
            PIC: PICST_75569(ADE6)
            SPO: SPAC6F12.10c(ade3)
            ANI: AN8121.2
            AFM: AFUA_5G02720
            AOR: AO090102000389
            CNE: CNI03300
            UMA: UM05162.1
            DDI: DDB_0230086(purL)
            ECO: b2557(purL)
            ECJ: JW2541(purL)
            ECE: Z3835(purL)
            ECS: ECs3423
            ECC: c3080(purL)
            ECI: UTI89_C2877(purL)
            ECP: ECP_2559
            ECV: APECO1_3974(purL)
            ECW: EcE24377A_2842(purL)
            ECX: EcHS_A2710
            STY: STY2812(purL)
            STT: t0291(purL)
            SPT: SPA0300(purL)
            SEC: SC2560(purG)
            STM: STM2565(purG)
            YPE: YPO2921(purL)
            YPK: y1309(purL)
            YPM: YP_2536(purL)
            YPA: YPA_2360
            YPN: YPN_1218
            YPP: YPDSF_2264
            YPS: YPTB2879(purL)
            YPI: YpsIP31758_1147(purL)
            SFL: SF2604(purL)
            SFX: S2776(purL)
            SFV: SFV_2605(purL)
            SSN: SSON_2640(purL)
            SBO: SBO_2585(purL)
            SDY: SDY_2747(purL)
            ECA: ECA3258(purL)
            PLU: plu3317(purL)
            WBR: WGLp137(purL)
            SGL: SG1778
            ENT: Ent638_3042
            SPE: Spro_3654
            HIN: HI0752(purL)
            HIT: NTHI0909(purL)
            HIP: CGSHiEE_08350
            HIQ: CGSHiGG_07280
            HSO: HS_1503(purL)
            PMU: PM1085(purL)
            MSU: MS1806(purL)
            APL: APL_1682(purL)
            ASU: Asuc_0422
            XFA: XF1423
            XFT: PD0650(purL)
            XCC: XCC0656(purL)
            XCB: XC_3578
            XCV: XCV3674(purL)
            XAC: XAC3549(purL)
            XOO: XOO0841(purL)
            XOM: XOO_0766(XOO0766)
            VCH: VC0869
            VCO: VC0395_A0395(purL)
            VVU: VV1_0340
            VVY: VV0847
            VPA: VP0666
            VFI: VF0652
            PPR: PBPRA0788
            PAE: PA3763(purL)
            PAU: PA14_15740(purL)
            PAP: PSPA7_1354(purL)
            PPU: PP_1037(purL)
            PPF: Pput_1078
            PST: PSPTO_1459(purL)
            PSB: Psyr_1269
            PSP: PSPPH_1341(purL)
            PFL: PFL_1076(purL)
            PFO: Pfl_0999
            PEN: PSEEN4386(purL)
            PMY: Pmen_3414
            PAR: Psyc_0187(purL)
            PCR: Pcryo_0208
            PRW: PsycPRwf_0545
            ACI: ACIAD2612(purL)
            SON: SO_3287(purL)
            SDN: Sden_1273
            SFR: Sfri_1141
            SAZ: Sama_2350
            SBL: Sbal_2980
            SBM: Shew185_2994
            SLO: Shew_1301
            SPC: Sputcn32_2642
            SSE: Ssed_3119
            SPL: Spea_1317
            SHE: Shewmr4_1238
            SHM: Shewmr7_1309
            SHN: Shewana3_1240
            SHW: Sputw3181_1365
            ILO: IL0591(purL)
            CPS: CPS_3675(purL)
            PHA: PSHAa2330(purL)
            PAT: Patl_3113
            SDE: Sde_1478
            PIN: Ping_3318
            MAQ: Maqu_2484
            CBU: CBU_0631(purL)
            CBD: COXBU7E912_0643(purL)
            LPN: lpg1676(purQ) lpg1678(purL2)
            LPF: lpl1641(purQ) lpl1643(purL)
            LPP: lpp1648(purQ) lpp1650(purL)
            MCA: MCA0673(purL)
            FTU: FTT1720c(purL)
            FTF: FTF1720c(purL)
            FTW: FTW_0078(purL)
            FTL: FTL_1860
            FTH: FTH_1789(purL)
            FTA: FTA_1966(purL)
            FTN: FTN_1699(purL)
            TCX: Tcr_1550
            NOC: Noc_1907
            AEH: Mlg_2474
            HHA: Hhal_2196
            HCH: HCH_02192(purL)
            CSA: Csal_0841
            ABO: ABO_0785(purL)
            MMW: Mmwyl1_4001
            AHA: AHA_1766(purL)
            DNO: DNO_1110
            BCI: BCI_0002(purL)
            RMA: Rmag_0392
            VOK: COSY_0364(purL)
            NME: NMB1996
            NMA: NMA0445(purL)
            NMC: NMC1972(purL)
            NGO: NGO1183
            CVI: CV_2044(purL)
            RSO: RSc1722(purL)
            REU: Reut_A1390
            REH: H16_A1511(purL)
            RME: Rmet_1870
            BMA: BMA1446(purL)
            BMV: BMASAVP1_A1937(purL)
            BML: BMA10299_A3368(purL)
            BMN: BMA10247_1210(purL)
            BXE: Bxe_A2283
            BVI: Bcep1808_1846
            BUR: Bcep18194_A5215
            BCN: Bcen_6165
            BCH: Bcen2424_1914
            BAM: Bamb_1902
            BPS: BPSL1416(purL)
            BPM: BURPS1710b_2463(purL)
            BPL: BURPS1106A_2342(purL)
            BPD: BURPS668_2303(purL)
            BTE: BTH_I2135(purL)
            PNU: Pnuc_0940
            BPE: BP2668(purL)
            BPA: BPP1242(purL)
            BBR: BB2311(purL)
            RFR: Rfer_2420
            POL: Bpro_2586
            PNA: Pnap_1821
            AAV: Aave_3099
            VEI: Veis_3609
            MPT: Mpe_A1761
            HAR: HEAR1740(purL)
            MMS: mma_1543
            NEU: NE0019(purL)
            NET: Neut_0140
            NMU: Nmul_A2383
            EBA: ebA6142(purL)
            AZO: azo2158(purL)
            DAR: Daro_1925
            TBD: Tbd_0629
            MFA: Mfla_0887 Mfla_1031
            HHE: HH1621(purQ) HH1825(purL)
            WSU: WS0605(purQ) WS0827(purC)
            TDN: Tmden_0489 Tmden_0547
            CJE: Cj0514(purQ) Cj0955c(purL)
            CJR: CJE0621(purQ) CJE1035(purL)
            CJJ: CJJ81176_0542(purQ) CJJ81176_0978(purL)
            CJU: C8J_0478(purQ) C8J_0897(purL)
            CJD: JJD26997_0826(purL) JJD26997_1417(purQ)
            CFF: CFF8240_0556(purL) CFF8240_0947(purQ)
            CCV: CCV52592_1835(purL) CCV52592_2003(purQ)
            CHA: CHAB381_0667(purL) CHAB381_0845(purQ)
            CCO: CCC13826_0134(purQ)
            ABU: Abu_1639(purL) Abu_2122(purS) Abu_2123(purQ)
            NIS: NIS_0872 NIS_0873 NIS_0895
            SUN: SUN_1462 SUN_1463 SUN_1565
            GSU: GSU1634 GSU1635
            GME: Gmet_1940 Gmet_1941
            GUR: Gura_2066 Gura_2067
            PCA: Pcar_1327 Pcar_1328
            PPD: Ppro_1147
            DVU: DVU1622(purQ) DVU3181(purL)
            DVL: Dvul_0206
            DDE: Dde_1764 Dde_3191
            LIP: LI0450(purL) LI0516(purL)
            BBA: Bd3003(purQ) Bd3004(purL)
            DPS: DP0704
            ADE: Adeh_3841 Adeh_4214
            AFW: Anae109_3954 Anae109_4362
            MXA: MXAN_2349(purL)
            SAT: SYN_00521 SYN_00522
            SFU: Sfum_0432 Sfum_0433
            WOL: WD0913 WD1018
            WBM: Wbm0232 Wbm0271
            AMA: AM960(purQ) AM973(purL)
            APH: APH_0213 APH_0225
            ERU: Erum6450(purQ) Erum6510(purL)
            ERW: ERWE_CDS_06760(purQ) ERWE_CDS_06830(purL)
            ERG: ERGA_CDS_06670(purQ) ERGA_CDS_06740(purL)
            ECN: Ecaj_0652 Ecaj_0658
            ECH: ECH_0351 ECH_0362
            NSE: NSE_0448 NSE_0812
            PUB: SAR11_1139 SAR11_1140(purQ) SAR11_1141(purL)
            MLO: mll0057 mll0065
            MES: Meso_1277 Meso_1279
            PLA: Plav_2586 Plav_2587
            SME: SMc00488(purL) SMc00493(purQ)
            SMD: Smed_1500 Smed_1505
            ATU: Atu1845(purQ) Atu1850(purL)
            ATC: AGR_C_3385 AGR_C_3393
            RET: RHE_CH02281(purQ) RHE_CH02286(purL)
            RLE: RL2608(purQ) RL2612(purL)
            BME: BMEI1124 BMEI1127
            BMF: BAB1_0857 BAB1_0860
            BMS: BR0837(purL) BR0840(purQ)
            BMB: BruAb1_0850(purL) BruAb1_0853(purQ)
            BOV: BOV_0829(purL) BOV_0832(purQ)
            OAN: Oant_2384 Oant_2389
            BJA: bll5719(purL) bll5723(purQ)
            BRA: BRADO2779(purQ) BRADO2785(purL)
            BBT: BBta_5401(purL) BBta_5406(purQ)
            RPA: RPA1597(purQ) RPA3818(purL)
            RPB: RPB_3713 RPB_3716
            RPC: RPC_1587 RPC_1591
            RPD: RPD_1749 RPD_1752
            RPE: RPE_1608 RPE_1610 RPE_1613
            NWI: Nwi_1306 Nwi_1308
            NHA: Nham_1635 Nham_1636
            BHE: BH09730(purQ) BH09740(purL)
            BQU: BQ07490(purQ) BQ07500(purL)
            BBK: BARBAKC583_0861(purQ) BARBAKC583_0863(purL)
            XAU: Xaut_4090 Xaut_4091
            CCR: CC_2497 CC_2500
            SIL: SPO1870(purL) SPO1890(purQ)
            SIT: TM1040_1118 TM1040_1463
            RSP: RSP_2128(purQ) RSP_2951(purL)
            RSH: Rsph17029_1596
            RSQ: Rsph17025_0713 Rsph17025_0894
            JAN: Jann_2173 Jann_2543
            RDE: RD1_2263 RD1_2264 RD1_3232(purL)
            PDE: Pden_3971
            MMR: Mmar10_1027 Mmar10_1030
            HNE: HNE_1937(purQ) HNE_1942(purL) HNE_2606(purS)
            ZMO: ZMO0820(pur-q) ZMO1531(purS) ZMO1532(purQ)
            NAR: Saro_1032 Saro_2256
            SAL: Sala_0591 Sala_2197
            SWI: Swit_0425 Swit_3970
            ELI: ELI_02440 ELI_05555
            GOX: GOX2300 GOX2301(purL) GOX2303 GOX2304
            GBE: GbCGDNIH1_1667 GbCGDNIH1_1669 GbCGDNIH1_1670
            ACR: Acry_2664 Acry_2665
            RRU: Rru_A0708 Rru_A0709
            MAG: amb2114 amb2115
            MGM: Mmc1_0498
            ABA: Acid345_2235 Acid345_4622
            SUS: Acid_5944
            BSU: BG10705(purL) BG10706(purQ)
            BHA: BH0628(purL) BH0629(purQ)
            BAN: BA0293(purQ) BA0294(purL)
            BAR: GBAA0293(purQ) GBAA0294(purL)
            BAA: BA_0865 BA_0866
            BAT: BAS0280 BAS0281
            BCE: BC0328 BC0329
            BCA: BCE_0322(purQ) BCE_0323(purL)
            BCZ: BCZK0267(purS) BCZK0268(purQ) BCZK0269(purL)
            BCY: Bcer98_0272 Bcer98_0273
            BTK: BT9727_0265(purQ) BT9727_0266(purL)
            BTL: BALH_0286(purS) BALH_0287(purQ) BALH_0288(purL)
            BLI: BL01481(purQ) BL01482(purL)
            BLD: BLi00698(purQ) BLi00699(purL)
            BCL: ABC1028(purS) ABC1029(purQ) ABC1030(purL)
            BAY: RBAM_006890 RBAM_006900
            BPU: BPUM_0600 BPUM_0601 BPUM_0602
            OIH: OB0744 OB0745
            GKA: GK0261 GK0262 GK0263
            SAU: SA0920(purQ) SA0921(purL)
            SAV: SAV1068(purQ) SAV1069(purL)
            SAM: MW0951(purQ) MW0952(purL)
            SAR: SAR1042(purQ) SAR1043(purL)
            SAS: SAS1004 SAS1005
            SAC: SACOL1076(purS) SACOL1077(purQ) SACOL1078(purL)
            SAB: SAB0935(purQ) SAB0936(purL)
            SAA: SAUSA300_0970(purQ) SAUSA300_0971(purL)
            SAO: SAOUHSC_01012 SAOUHSC_01013
            SAJ: SaurJH9_1128 SaurJH9_1129
            SAH: SaurJH1_1150 SaurJH1_1151
            SEP: SE0766 SE0767
            SER: SERP0653(purQ) SERP0654(purL)
            SHA: SH1888(purL) SH1889(purQ)
            SSP: SSP1721 SSP1722
            LMO: lmo1769(purQ) lmo1770(purL)
            LMF: LMOf2365_1794(purL) LMOf2365_1795(purQ)
            LIN: lin1881(purQ) lin1882(purL)
            LWE: lwe1787(purL) lwe1788(purQ) lwe1789(purS)
            LLA: L173921(purL) L176360(purQ)
            LLC: LACR_1619 LACR_1620 LACR_1621
            LLM: llmg_0975(purQ) llmg_0976(purL)
            SPY: SPy_0025
            SPZ: M5005_Spy_0023
            SPM: spyM18_0026(purL)
            SPG: SpyM3_0020(purL)
            SPS: SPs0021
            SPH: MGAS10270_Spy0023
            SPI: MGAS10750_Spy0023
            SPJ: MGAS2096_Spy0024
            SPK: MGAS9429_Spy0023
            SPF: SpyM50022
            SPA: M6_Spy0072
            SPB: M28_Spy0023(purL)
            SPN: SP_0045
            SPR: spr0046(purL)
            SPD: SPD_0052
            SAG: SAG0025
            SAN: gbs0024
            SAK: SAK_0058
            SMU: SMU.30(purL)
            STC: str0031(purL)
            STL: stu0031(purL)
            SSA: SSA_0030(purL)
            SGO: SGO_0035
            LPL: lp_2724(purL) lp_2725(purQ)
            LAC: LBA1556(purL) LBA1557(purQ)
            LSA: LSA0656(purS) LSA0657(purQ) LSA0658(purL)
            LSL: LSL_0664(purS) LSL_0665(purQ) LSL_0666(purL)
            LDB: Ldb1440(purL) Ldb1441(purQ) Ldb1442(purS)
            LBU: LBUL_1335 LBUL_1336
            LCA: LSEI_1751 LSEI_1752 LSEI_1753
            LRE: Lreu_0139 Lreu_0140
            EFA: EF1782(purL) EF1783(purQ)
            OOE: OEOE_1133 OEOE_1134
            STH: STH2855 STH2856
            CAC: CAC1655(purQ)
            CPE: CPE0680(purL)
            CPF: CPF_0671
            CPR: CPR_0669
            CTC: CTC01029
            CTH: Cthe_0554
            CDF: CD0225(purL)
            CBO: CBO2580(purL)
            CBA: CLB_2521
            CBH: CLC_2452
            CBF: CLI_2643
            CBE: Cbei_1053
            CKL: CKL_1286(purL)
            AMT: Amet_0920 Amet_0921
            CHY: CHY_1073(purQ) CHY_1074(purL)
            DSY: DSY3934
            DRM: Dred_2366
            SWO: Swol_2175
            CSC: Csac_1996 Csac_1997
            TTE: TTE0810(purL) TTE0811(purL2)
            MTA: Moth_2048 Moth_2049
            MTU: Rv0788(purQ) Rv0803(purL)
            MTC: MT0813(purQ) MT0823(purL)
            MBO: Mb0812(purQ) Mb0826(purL)
            MBB: BCG_0841(purQ) BCG_0855(purL)
            MLE: ML2211(purL) ML2219(purQ)
            MPA: MAP0626(purQ) MAP0635(purL)
            MAV: MAV_0736(purQ) MAV_0744(purL)
            MSM: MSMEG_5824(purL) MSMEG_5831(purQ) MSMEG_5832(purS)
            MVA: Mvan_5119
            MGI: Mflv_1630
            MMC: Mmcs_4546 Mmcs_4552 Mmcs_4553
            MKM: Mkms_4633
            MJL: Mjls_4929
            CGL: NCgl2499(cgl2588) NCgl2500(cgl2589)
            CGB: cg2862(purL) cg2863(purQ) cg2865(purS)
            CEF: CE2480(purL) CE2481(purQ)
            CDI: DIP2130
            CJK: jk0354(purQ) jk0355(purL)
            NFA: nfa5680(purQ) nfa5730(purL)
            RHA: RHA1_ro04827(purQ) RHA1_ro04835(purL)
            SCO: SCO4078(purQ) SCO4079(purL)
            SMA: SAV4138(purL) SAV4139(purQ)
            TWH: TWT794(purL) TWT795(purQ)
            TWS: TW803(purL) TW805(purQ)
            LXX: Lxx22970(purQ) Lxx23140(purL)
            CMI: CMM_0728(purL) CMM_0729(purQ)
            ART: Arth_0540
            AAU: AAur_0629(purL) AAur_0630(purQ)
            PAC: PPA1977 PPA1987
            NCA: Noca_4326
            TFU: Tfu_0156 Tfu_0158
            FRA: Francci3_4416 Francci3_4417
            FAL: FRAAL6724(purQ) FRAAL6730(purL)
            ACE: Acel_2074
            KRA: Krad_4068 Krad_4069
            SEN: SACE_7142(purL) SACE_7143(purQ) SACE_7144(purS)
            STP: Strop_0151 Strop_0152
            BLO: BL1108(purL)
            BAD: BAD_0523(purQ_purL)
            RXY: Rxyl_0995 Rxyl_0996
            FNU: FN0990
            RBA: RB5395(purL) RB8613(pfaS)
            TDE: TDE1279(purL) TDE1405(purQ)
            LIL: LA1323(purL) LA3511(purQ)
            LIC: LIC10681(purL) LIC12402(purQ)
            LBJ: LBJ_0700 LBJ_2272(purL)
            LBL: LBL_0835(purL) LBL_2379
            SYN: sll1056(purL) slr0520(purL)
            SYW: SYNW0003(purL) SYNW0793(purQ)
            SYC: syc0720_c(purL) syc1494_c(purL)
            SYF: Synpcc7942_0003 Synpcc7942_0819
            SYD: Syncc9605_0003 Syncc9605_1853
            SYE: Syncc9902_0003 Syncc9902_0800
            SYG: sync_0003(purL) sync_1700(purS) sync_1701(purQ)
            SYR: SynRCC307_0003(purL) SynRCC307_1240(purQ)
                 SynRCC307_1241(purS)
            SYX: SynWH7803_0003(purL) SynWH7803_1141(purS)
                 SynWH7803_1142(purQ)
            CYA: CYA_0646(purQ) CYA_1361(purL)
            CYB: CYB_0284(purQ) CYB_0285(purS) CYB_2807(purL)
            TEL: tlr1683(purL) tlr2187(purL)
            GVI: glr1325(purQ) glr2113(purL)
            ANA: all3652 alr2475
            AVA: Ava_0407 Ava_3636
            PMA: Pro0003(purL) Pro0854(purL)
            PMM: PMM0003(purL) PMM0780(purQ)
            PMT: PMT0003(purL) PMT0539(purQ)
            PMN: PMN2A_0187 PMN2A_1330
            PMI: PMT9312_0003 PMT9312_0788
            PMB: A9601_00021 A9601_08421(purS) A9601_08431
            PMC: P9515_00021 P9515_08021 P9515_08031(purS)
            PMF: P9303_00021 P9303_17241(purS) P9303_17251
            PMG: P9301_00021 P9301_08401(purS) P9301_08411
            PME: NATL1_00021 NATL1_08181(purS) NATL1_08191
            TER: Tery_2596
            BTH: BT_1733
            BFR: BF3315
            BFS: BF3154
            PGI: PG0296
            SRU: SRU_0521(purQ) SRU_0963(purS) SRU_2656(purL)
            CHU: CHU_1667(purL)
            GFO: GFO_1050(purL)
            FJO: Fjoh_4724
            FPS: FP0695(purL)
            CTE: CT1240(purL) CT1338(purQ)
            CCH: Cag_0937 Cag_1019
            CPH: Cpha266_1265
            PVI: Cvib_0852
            PLT: Plut_1089 Plut_1325
            DET: DET0378(purQ) DET0379(purL)
            DEH: cbdb_A323(purQ) cbdb_A325(purL)
            DEB: DehaBAV1_0360 DehaBAV1_0361
            RRS: RoseRS_1845 RoseRS_2622
            RCA: Rcas_1795 Rcas_3277
            DRA: DR_0222 DR_0223
            DGE: Dgeo_0064 Dgeo_0065
            TTH: TTC1153 TTC1155
            TTJ: TTHA1517 TTHA1519
            AAE: aq_1105(purQ) aq_1836(purL)
            TMA: TM1245 TM1246
            TPT: Tpet_1525 Tpet_1526
            TME: Tmel_1235 Tmel_1236
            FNO: Fnod_1096 Fnod_1097
            MJA: MJ1648(purQ)
            MMP: MMP0178(purQ) MMP0179(purL)
            MMQ: MmarC5_1496
            MMZ: MmarC7_1178 MmarC7_1179
            MAE: Maeo_0678 Maeo_1459
            MVN: Mevan_1182 Mevan_1183
            MAC: MA1963 MA4055(purL)
            MBA: Mbar_A0536 Mbar_A2755
            MMA: MM_0860 MM_2807
            MBU: Mbur_0461 Mbur_2051
            MTP: Mthe_0099
            MHU: Mhun_1061 Mhun_1062
            MLA: Mlab_0283
            MEM: Memar_1629
            MBN: Mboo_0472
            MTH: MTH168
            MST: Msp_1193(purQ) Msp_1194 Msp_1467(purL)
            MSI: Msm_1342 Msm_1549
            MKA: MK0497(purL_2) MK0790(purL_1)
            AFU: AF1260(purQ) AF1940(purL)
            HAL: VNG0864G(purL) VNG1945G(purL2)
            HMA: rrnAC1390(purL) rrnAC3268(purQ)
            HWA: HQ1693A(purL) HQ3130A(purS) HQ3131A(purQ)
            NPH: NP2982A(purL) NP5008A(purS) NP5010A(purQ)
            TAC: Ta1066 Ta1318m
            TVO: TVN0268 TVN0521
            PTO: PTO0808 PTO1204 PTO1205
            PHO: PH1953 PH1955
            PAB: PAB1200(purQ) PAB1201(purL)
            PFU: PF0198 PF0199
            TKO: TK0197 TK0201
            RCI: LRC114(purQ) LRC115(purL)
            IHO: Igni_0845
            SSO: SSO0628(purQ) SSO0629(purL)
            STO: ST1494 ST1495
            SAI: Saci_1610(purL)
            MSE: Msed_1979 Msed_1980
            PAI: PAE0222(purQ) PAE0225(purL)
STRUCTURES  PDB: 1T3T  1VK3  1VQ3  2HRU  2HRY  2HS0  2HS3  2HS4  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.5.3
            ExPASy - ENZYME nomenclature database: 6.3.5.3
            ExplorEnz - The Enzyme Database: 6.3.5.3
            ERGO genome analysis and discovery system: 6.3.5.3
            BRENDA, the Enzyme Database: 6.3.5.3
            CAS: 9032-84-2
///
ENTRY       EC 6.3.5.4                  Enzyme
NAME        asparagine synthase (glutamine-hydrolysing);
            asparagine synthetase (glutamine-hydrolysing);
            glutamine-dependent asparagine synthetase;
            asparagine synthetase B;
            AS;
            AS-B
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Carbon-nitrogen ligases with glutamine as amido-N-donor
SYSNAME     L-aspartate:L-glutamine amido-ligase (AMP-forming)
REACTION    (1) ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate +
            L-asparagine + L-glutamate [RN:R00578];
            (2) (1a) L-glutamine + H2O = L-glutamate + NH3;
            (3) (1b) ATP + L-aspartate + NH3 = AMP + diphosphate + L-asparagine
ALL_REAC    R00578
SUBSTRATE   ATP [CPD:C00002];
            L-aspartate [CPD:C00049];
            L-glutamine [CPD:C00064];
            H2O [CPD:C00001];
            NH3 [CPD:C00014]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            L-asparagine [CPD:C00152];
            L-glutamate [CPD:C00025];
            NH3 [CPD:C00014]
COMMENT     The enzyme from Escherichia coli has two active sites [4] that are
            connected by an intramolecular ammonia tunnel [6,7]. The enzyme
            catalyses three distinct chemical reactions: glutamine hydrolysis to
            yield ammonia takes place in the N-terminal domain. The C-terminal
            active site mediates both the synthesis of a beta-aspartyl-AMP
            intermediate and its subsequent reaction with ammonia. The ammonia
            released is channeled to the other active site to yield asparagine
            [7].
REFERENCE   1  [PMID:4295091]
  AUTHORS   Patterson MK Jr, Orr GR.
  TITLE     Asparagine biosynthesis by the Novikoff Hepatoma isolation,
            purification, property, and mechanism studies of the enzyme system.
  JOURNAL   J. Biol. Chem. 243 (1968) 376-80.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:7907328]
  AUTHORS   Boehlein SK, Richards NG, Schuster SM.
  TITLE     Glutamine-dependent nitrogen transfer in Escherichia coli asparagine
            synthetase B. Searching for the catalytic triad.
  JOURNAL   J. Biol. Chem. 269 (1994) 7450-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:9559053]
  AUTHORS   Richards NG, Schuster SM.
  TITLE     Mechanistic issues in asparagine synthetase catalysis.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 72 (1998) 145-98.
REFERENCE   4  [PMID:10587437]
  AUTHORS   Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden
            HM, Rayment I.
  TITLE     Three-dimensional structure of Escherichia coli asparagine
            synthetase B: a short journey from substrate to product.
  JOURNAL   Biochemistry. 38 (1999) 16146-57.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:10852734]
  AUTHORS   Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden
            HM, Rayment I I.
  TITLE     Three-dimensional structure of escherichia coli asparagine
            synthetase B: A short journey from substrate to product
  JOURNAL   Biochemistry. 39 (2000) 7330.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:11395405]
  AUTHORS   Huang X, Holden HM, Raushel FM.
  TITLE     Channeling of substrates and intermediates in enzyme-catalyzed
            reactions.
  JOURNAL   Annu. Rev. Biochem. 70 (2001) 149-80.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   7  [PMID:12706338]
  AUTHORS   Tesson AR, Soper TS, Ciustea M, Richards NG.
  TITLE     Revisiting the steady state kinetic mechanism of glutamine-dependent
            asparagine synthetase from Escherichia coli.
  JOURNAL   Arch. Biochem. Biophys. 413 (2003) 23-31.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00252  Alanine and aspartate metabolism
            PATH: map00910  Nitrogen metabolism
ORTHOLOGY   KO: K01953  asparagine synthase (glutamine-hydrolysing)
GENES       HSA: 440(ASNS)
            PTR: 463556(ASNS)
            MMU: 27053(Asns)
            RNO: 25612(Asns)
            CFA: 475240(ASNS)
            GGA: 420574(RCJMB04_15l3)
            XTR: 448254(asns)
            DRE: 394138(asns)
            SPU: 575946(LOC575946)
            DME: Dmel_CG33486(asparagine-synthetase)
            CEL: F25G6.6(nrs-2)
            ATH: AT3G47340(ASN1) AT5G65010(ASN2)
            OSA: 4332506 4340706
            CME: CMM145C
            SCE: YGR124W(ASN2) YPR145W(ASN1)
            AGO: AGOS_AFR303W
            PIC: PICST_35948 PICST_83540(ASN1)
            CAL: CaO19.198
            CGR: CAGL0I10648g
            SPO: SPBC119.10
            ANI: AN4401.2 AN8754.2
            AFM: AFUA_4G06900 AFUA_4G12480
            AOR: AO090023000896 AO090103000353 AO090103000354 AO090120000180
            CNE: CNH00920
            UMA: UM00311.1
            DDI: DDB_0230140(asnA) DDB_0230142(asnB)
            PFA: MAL3P3.14
            TET: TTHERM_00052420
            ECO: b0674(asnB)
            ECJ: JW0660(asnB)
            ECE: Z0821(asnB)
            ECS: ECs0704
            ECC: c0749(asnB)
            ECI: UTI89_C0668(asnB)
            ECP: ECP_0686
            ECV: APECO1_1398(asnB)
            ECW: EcE24377A_0699(asnB)
            ECX: EcHS_A0717
            STY: STY0718(asnB)
            STT: t2195(asnB)
            SEC: SC0701(asnB)
            STM: STM0680(asnB)
            YPE: YPO2623(asnB)
            YPK: y1198(asnB)
            YPM: YP_1090(asnB)
            YPA: YPA_2474
            YPN: YPN_1109
            YPP: YPDSF_2630
            YPS: YPTB1115(asnB)
            YPI: YpsIP31758_2913(asnB)
            SFL: SF0619(asnB)
            SFX: S0630(asnB)
            SFV: SFV_0657(asnB)
            SSN: SSON_0627(asnB)
            SBO: SBO_0536(asnB)
            SDY: SDY_0608(asnB)
            ECA: ECA1323(asnB)
            WBR: WGLp587(asnB)
            SGL: SG0813
            XFA: XF0118
            XFT: PD0089(asnB)
            XCC: XCC1388(asnB) XCC1432(wbpS)
            XCB: XC_2806 XC_2848
            XCV: XCV1490(asnB) XCV1533(asnB2) XCV1549
            XAC: XAC1433(asnB) XAC1475
            XOO: XOO1523 XOO1990(asnB)
            XOM: XOO_1412(XOO1412) XOO_1881(XOO1881)
            VCH: VC0991
            VCO: VC0395_A0512(asnB)
            VVU: VV1_0183
            VVY: VV1007
            VPA: VP0826
            VFI: VF0804(asnB) VFA0439
            PPR: PBPRA1027
            PAE: PA0051 PA2084 PA3459
            PAU: PA14_00640(phzH) PA14_19370(asnB) PA14_37560(asnB)
            PAP: PSPA7_1668(asnB)
            PPU: PP_1750(asnB)
            PPF: Pput_3964
            PST: PSPTO_1633(asnB)
            PSB: Psyr_3747 Psyr_4315
            PSP: PSPPH_1509(asnB)
            PFL: PFL_4333
            PFO: Pfl_4100
            PEN: PSEEN1469 PSEEN2476 PSEEN5526
            PMY: Pmen_2955
            PAR: Psyc_0665(asnB) Psyc_0668(wbpS)
            PCR: Pcryo_0622
            PRW: PsycPRwf_0241
            SON: SO_2767(asnB-1) SO_3175(asnB-2)
            SDN: Sden_2075 Sden_3533 Sden_3771
            SFR: Sfri_1602
            SHE: Shewmr4_2384
            SHM: Shewmr7_2456
            SHN: Shewana3_2549
            ILO: IL1526(asnB)
            CPS: CPS_2794(asnB)
            PHA: PSHAa1440(asnB)
            PAT: Patl_1194 Patl_2955
            SDE: Sde_0146
            MAQ: Maqu_1636
            CBU: CBU_0831(asnB-1) CBU_0840(asnB-2)
            CBD: COXBU7E912_0896(asnB2) COXBU7E912_0905(asnB1)
            MCA: MCA0472 MCA0542 MCA2127
            FTU: FTT1456c(wbtH)
            FTF: FTF1456c(wbtH)
            FTW: FTW_0419(wbtH)
            FTL: FTL_0600
            FTH: FTH_0600(asnB)
            FTA: FTA_0634(asnB)
            FTN: FTN_1421(wbtH)
            TCX: Tcr_0595
            NOC: Noc_0777 Noc_1965 Noc_1975 Noc_2478
            AEH: Mlg_0134 Mlg_0138 Mlg_2339
            HHA: Hhal_1512
            HCH: HCH_01655(asnB1) HCH_02383(asnB2) HCH_02399(asnB4)
            AHA: AHA_2657(asnB)
            VOK: COSY_0351(asnB)
            CVI: CV_0797 CV_1713(asnB) CV_3959
            REU: Reut_B5373
            BMA: BMA0234 BMAA1158 BMAA1921(asnB)
            BMV: BMASAVP1_0936(asnB)
            BML: BMA10299_0082(asnB-1) BMA10299_1222(asnB-2)
            BMN: BMA10247_A1535(asnB-1) BMA10247_A2198(asnB-2)
            BVI: Bcep1808_5331
            BUR: Bcep18194_B0858
            BCN: Bcen_3523
            BCH: Bcen2424_4843
            BAM: Bamb_4217
            BPS: BPSL0682 BPSS0163(asnO) BPSS0677
            BPM: BURPS1710b_0900(asnB) BURPS1710b_A1682(asnB)
                 BURPS1710b_A2247(asnB)
            BPL: BURPS1106A_A0231(asnB) BURPS1106A_A0918(asnB)
            BPD: BURPS668_A0321(asnB) BURPS668_A1004(asnB)
            BTE: BTH_II0232(asnB-1) BTH_II1749(asnB-2)
            BPE: BP3146
            BPA: BPP0123 BPP0136(wbmI) BPP0795
            BBR: BB0123 BB0880
            RFR: Rfer_0669 Rfer_0671 Rfer_0683 Rfer_3652
            POL: Bpro_3988
            PNA: Pnap_4494
            AAV: Aave_0959
            NEU: NE1127(asnB) NE1795
            NET: Neut_0901 Neut_1419 Neut_1735
            NMU: Nmul_A2519 Nmul_A2668
            EBA: ebA4263(asnB) ebA4265 ebA4285 ebA5271(asnB)
            AZO: azo3247(asn) azo3271(asnB1) azo3273(asnB2)
            DAR: Daro_1275 Daro_2408 Daro_2428
            TBD: Tbd_0060 Tbd_0292 Tbd_0298
            WSU: WS0046(glmS) WS2185(wbfR) WS2192(PAB1605)
            TDN: Tmden_0163 Tmden_0186 Tmden_0200
            CFF: CFF8240_1611(asnB) CFF8240_1617(asnB)
            CCO: CCC13826_0524(asnB) CCC13826_0536(asnB) CCC13826_1516
            ABU: Abu_0045(asnB1) Abu_0668(asnB2) Abu_0678(asnB)
            NIS: NIS_1441
            GSU: GSU1953(asnB)
            GME: Gmet_2172
            PPD: Ppro_2466
            DVU: DVU3014
            DVL: Dvul_0358 Dvul_3035
            DDE: Dde_1135 Dde_2891 Dde_3317 Dde_3677
            LIP: LIB007(asnB)
            DPS: DP0033(wbpS)
            ADE: Adeh_2780 Adeh_2789
            MXA: MXAN_0301
            SAT: SYN_02666 SYN_02678
            MLO: mll6743 mlr5888 mlr6755
            MES: Meso_2469 Meso_2884
            PLA: Plav_0816
            SME: SMb20481(asnO) SMb20652(asnB)
            RET: RHE_CH00758(asnB)
            BJA: blr6298(asnB)
            BRA: BRADO0860 BRADO4822 BRADO5156
            BBT: BBta_3705 BBta_5624 BBta_7206
            RPB: RPB_1541 RPB_1548 RPB_2064
            RPC: RPC_2050 RPC_3874
            RPE: RPE_0582
            RSP: RSP_2557(asnB) RSP_7386
            RDE: RD1_3849(asnO)
            NAR: Saro_2327
            SAL: Sala_1919
            SWI: Swit_4039
            ELI: ELI_06815
            GOX: GOX1964
            GBE: GbCGDNIH1_1983
            ACR: Acry_0265
            RRU: Rru_A0230 Rru_A0819 Rru_A0855 Rru_A1483 Rru_A1989 Rru_A2937
                 Rru_A3028 Rru_A3121
            MAG: amb0042 amb0105 amb0119 amb1266 amb4020
            MGM: Mmc1_0216 Mmc1_0573 Mmc1_0596 Mmc1_3228
            SUS: Acid_0272 Acid_4105 Acid_4624 Acid_5610
            BSU: BG11116(asnH) BG11831(asnB) BG12240(asnO)
            BHA: BH1508
            BAN: BA1157(asnO-1) BA1751(asnO-2) BA2251(asnO-3)
            BAR: GBAA1157(asnO-1) GBAA1751(asnO-2) GBAA2251(asnO-3)
            BAA: BA_1702 BA_2264 BA_2754
            BAT: BAS1074 BAS1625 BAS2095
            BCE: BC1152 BC1153 BC1697 BC2204
            BCA: BCE_1259(asnO) BCE_1828(asnO) BCE_2280(asnO)
            BCZ: BCZK1053(asnO) BCZK1577(asnO) BCZK2033(asnB)
            BCY: Bcer98_0872
            BTK: BT9727_1055(asnO) BT9727_1586(asnO) BT9727_2035(asnB)
            BTL: BALH_2013
            BLI: BL00002(asnB) BL01342(asnO)
            BLD: BLi01174(asnO) BLi03195(asnB) BLi04033
            BCL: ABC1768(asnO) ABC2580(asnB)
            BAY: RBAM_010950 RBAM_027560
            BPU: BPUM_1010 BPUM_2685
            OIH: OB2608
            GKA: GK0700 GK0906(ansB)
            GTN: GTNG_0790
            LMO: lmo1663(ansB)
            LMF: LMOf2365_1687(asnB)
            LIN: lin1772(ansB)
            LWE: lwe1682(ansB)
            LLA: L00396(asnB) L0095(asnH)
            LLC: LACR_0398 LACR_2533
            LLM: llmg_0372(asnB) llmg_2506(asnH)
            LPL: lp_0980(asnB1) lp_3085(asnB2)
            LJO: LJ0135
            LAC: LBA0158(asnH)
            LSA: LSA0636(asnB)
            LSL: LSL_0012(asnB)
            LDB: Ldb0209(asnB1)
            LBU: LBUL_0183
            LBR: LVIS_1501
            LCA: LSEI_2162
            LGA: LGAS_0135
            PPE: PEPE_0659
            STH: STH231 STH259
            CAC: CAC2243(asnB)
            CTH: Cthe_0556
            CDF: CD0391 CD1632(asnB)
            CBE: Cbei_1034
            CKL: CKL_1024(asnB) CKL_2310(asn)
            AMT: Amet_4405
            CHY: CHY_0104(asnB)
            DSY: DSY4329
            DRM: Dred_2812
            SWO: Swol_0712
            TTE: TTE0817(asnB)
            MTA: Moth_1299
            POY: PAM594(asnB)
            MTU: Rv2201(asnB)
            MTC: MT2257
            MBO: Mb2224(asnB)
            MBB: BCG_2217(asnB)
            MLE: ML0874(asnB)
            MPA: MAP1421(asnB_1) MAP1941(asnB_2)
            MAV: MAV_2290(asnB) MAV_3055(asnB)
            MSM: MSMEG_2594(asnB) MSMEG_4269(asnB)
            MUL: MUL_3558(asnB)
            MVA: Mvan_2276 Mvan_3565
            MGI: Mflv_4066
            MMC: Mmcs_2055 Mmcs_3299
            MKM: Mkms_2101 Mkms_3361
            MJL: Mjls_2038 Mjls_3310
            CGL: NCgl2116(cgl2196)
            CGB: cg2410(ltsA)
            CEF: CE2088(ltsA)
            CDI: DIP1630(asnB)
            CJK: jk0714(asnB)
            NFA: nfa17070(asnB)
            RHA: RHA1_ro01138(asn1) RHA1_ro05010(asn2)
            SCO: SCO0386(SCF62.12)
            LXX: Lxx21710(asn)
            FRA: Francci3_2910
            FAL: FRAAL4488 FRAAL5643(asnO)
            SEN: SACE_1677(asn1) SACE_6091(asnB-1)
            STP: Strop_2541 Strop_3057
            BAD: BAD_1077(asnH)
            RBA: RB13303(asnB) RB4577(asnB)
            SYW: SYNW2453(asnB)
            SYD: Syncc9605_2633
            SYE: Syncc9902_2260
            SYG: sync_0178(asnB)
            SYR: SynRCC307_0175 SynRCC307_1124(asnB)
            TEL: tll0236
            PMA: Pro0058(asnB)
            PMI: PMT9312_1324
            PME: NATL1_08651(asnB)
            BTH: BT_0551
            BFR: BF2639
            BFS: BF2661(asnB)
            CHU: CHU_0058(asnB) CHU_3607(asnB) CHU_3693(asnB)
            GFO: GFO_0573(asnB) GFO_1998(asnB) GFO_2750
            FPS: FP0526 FP1997(asnB)
            PLT: Plut_1852
            RRS: RoseRS_4419 RoseRS_4439
            RCA: Rcas_0764 Rcas_0793 Rcas_3021
            TTH: TTC0282
            MMP: MMP0918(asnB)
            MMQ: MmarC5_0497 MmarC5_0725
            MMZ: MmarC7_0165
            MVN: Mevan_0211
            MAC: MA1966(asn)
            MBA: Mbar_A2257
            MMA: MM_2805
            MBU: Mbur_0465 Mbur_1580
            MHU: Mhun_1015
            MBN: Mboo_2442
            MST: Msp_0490
            MSI: Msm_0160
            MKA: MK0103(asnB)
            HAL: VNG0867G(asnA)
            HMA: rrnAC1359(asnB)
            HWA: HQ1691A(asnB)
            NPH: NP2978A(asn)
            PTO: PTO1047
            PAB: PAB0750(asnB) PAB1605
            PFU: PF1071
            TKO: TK0950
            RCI: RCIX1956(asnB-1) RCIX2428(asnB-2)
            APE: APE_2041.1
            PAI: PAE0376(asnB)
STRUCTURES  PDB: 1CT9  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.5.4
            ExPASy - ENZYME nomenclature database: 6.3.5.4
            ExplorEnz - The Enzyme Database: 6.3.5.4
            ERGO genome analysis and discovery system: 6.3.5.4
            BRENDA, the Enzyme Database: 6.3.5.4
            CAS: 37318-72-2
///
ENTRY       EC 6.3.5.5                  Enzyme
NAME        carbamoyl-phosphate synthase (glutamine-hydrolysing);
            carbamoyl-phosphate synthetase (glutamine-hydrolysing);
            carbamyl phosphate synthetase (glutamine);
            carbamoylphosphate synthetase II;
            glutamine-dependent carbamyl phosphate synthetase;
            carbamoyl phosphate synthetase;
            CPS;
            carbon-dioxide:L-glutamine amido-ligase (ADP-forming,
            carbamate-phosphorylating)
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Carbon-nitrogen ligases with glutamine as amido-N-donor
SYSNAME     hydrogen-carbonate:L-glutamine amido-ligase (ADP-forming,
            carbamate-phosphorylating)
REACTION    (1) 2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate +
            L-glutamate + carbamoyl phosphate [RN:R00575];
            (2) (1a) L-glutamine + H2O = L-glutamate + NH3 [RN:R00256];
            (3) (1b) 2 ATP + HCO3- = 2 ADP + phosphate + carbamoyl phosphate
            [RN:R07641]
ALL_REAC    R00256 R00575 R07641
SUBSTRATE   ATP [CPD:C00002];
            L-glutamine [CPD:C00064];
            HCO3- [CPD:C00288];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            L-glutamate [CPD:C00025];
            carbamoyl phosphate [CPD:C00169];
            NH3 [CPD:C00014]
COMMENT     The product carbamoyl phosphate is an intermediate in the
            biosynthesis of arginine and the pyrimidine nucleotides [4]. The
            enzyme from Escherichia coli has three separate active sites, which
            are connected by a molecular tunnel that is almost 100 A in length
            [8]. The amidotransferase domain within the small subunit of the
            enzyme hydrolyses glutamine to ammonia via a thioester intermediate.
            The ammonia migrates through the interior of the protein, where it
            reacts with carboxy phosphate to produce the carbamate intermediate.
            The carboxy-phosphate intermediate is formed by the phosphorylation
            of bicarbonate by ATP at a site contained within the N-terminal half
            of the large subunit. The carbamate intermediate is transported
            through the interior of the protein to a second site within the
            C-terminal half of the large subunit, where it is phosphorylated by
            another ATP to yield the final product, carbamoyl phosphate [6].
REFERENCE   1
  AUTHORS   Anderson, P.M. and Meister, A.
  TITLE     Evidence for an activated form of carbon dioxide in the reaction
            catalysed by Escherichia coli carbamyl phosphate synthetase.
  JOURNAL   Biochemistry 4 (1965) 2803-2809.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:5329589]
  AUTHORS   Kalman SM, Duffield PH, Brzozowski T.
  TITLE     Purification and properties of a bacterial carbamyl phosphate
            synthetase.
  JOURNAL   J. Biol. Chem. 241 (1966) 1871-7.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   3  [PMID:5442268]
  AUTHORS   Yip MC, Knox WE.
  TITLE     Glutamine-dependent carbamyl phosphate synthetase. Properties and
            distribution in normal and neoplastic rat tissues.
  JOURNAL   J. Biol. Chem. 245 (1970) 2199-204.
  ORGANISM  rat [GN:rno]
REFERENCE   4  [PMID:8916922]
  AUTHORS   Stapleton MA, Javid-Majd F, Harmon MF, Hanks BA, Grahmann JL,
            Mullins LS, Raushel FM.
  TITLE     Role of conserved residues within the carboxy phosphate domain of
            carbamoyl phosphate synthetase.
  JOURNAL   Biochemistry. 35 (1996) 14352-61.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   5  [PMID:9914247]
  AUTHORS   Holden HM, Thoden JB, Raushel FM.
  TITLE     Carbamoyl phosphate synthetase: a tunnel runs through it.
  JOURNAL   Curr. Opin. Struct. Biol. 8 (1998) 679-85.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   6  [PMID:9818189]
  AUTHORS   Raushel FM, Thoden JB, Reinhart GD, Holden HM.
  TITLE     Carbamoyl phosphate synthetase: a crooked path from substrates to
            products.
  JOURNAL   Curr. Opin. Chem. Biol. 2 (1998) 624-32.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   7  [PMID:10387030]
  AUTHORS   Raushel FM, Thoden JB, Holden HM.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia.
  JOURNAL   Biochemistry. 38 (1999) 7891-9.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   8  [PMID:12130656]
  AUTHORS   Thoden JB, Huang X, Raushel FM, Holden HM.
  TITLE     Carbamoyl-phosphate synthetase. Creation of an escape route for
            ammonia.
  JOURNAL   J. Biol. Chem. 277 (2002) 39722-7.
  ORGANISM  Escherichia coli [GN:eco]
PATHWAY     PATH: map00240  Pyrimidine metabolism
            PATH: map00251  Glutamate metabolism
ORTHOLOGY   KO: K01954  carbamoyl-phosphate synthase
            KO: K01955  carbamoyl-phosphate synthase large chain
            KO: K01956  carbamoyl-phosphate synthase small chain
GENES       HSA: 790(CAD)
            MMU: 69719(Cad)
            CFA: 483009(CAD)
            DME: Dmel_CG18572(r)
            CEL: D2085.1(pyr-1)
            ATH: AT1G29900(CARB) AT3G27740(CARA)
            OSA: 4330474
            CME: CML055C CMQ255C
            SCE: YJL130C(URA2) YJR109C(CPA2) YOR303W(CPA1)
            AGO: AGOS_ABR157W AGOS_ACR263C AGOS_AFR534W
            PIC: PICST_28533(CPA1) PICST_50410(CPA2)
            CAL: CaO19.2360 CaO19_3221(CaO19.3221) CaO19_4630(CaO19.4630)
            CGR: CAGL0C04917g CAGL0I09592g CAGL0L05676g
            SPO: SPAC22G7.06c(ura1) SPBC215.08c SPBC56F2.09c
            ANI: AN0565.2 AN2243.2 AN5999.2
            AFM: AFUA_2G10070 AFUA_5G06780 AFUA_6G11310
            AOR: AO090011000630 AO090023000483 AO090701000214
            CNE: CNA06000 CND01050 CNM01170
            UMA: UM06285.1
            DDI: DDB_0201646(pyr1-3)
            PFA: PF13_0044
            TAN: TA02545
            TPV: TP03_0048
            TBR: Tb927.5.3800
            TCR: 508373.10
            ECO: b0032(carA) b0033(carB)
            ECJ: JW0030(carA) JW0031(carB)
            ECE: Z0037(carA) Z0038(carB)
            ECS: ECs0035 ECs0036
            ECC: c0040(carA) c0041(carB)
            ECI: UTI89_C0036(carA) UTI89_C0037(carB)
            ECP: ECP_0031 ECP_0032
            ECV: APECO1_1949(carB) APECO1_1950(carA)
            ECW: EcE24377A_0033(carA) EcE24377A_0034(carB)
            ECX: EcHS_A0035(carA) EcHS_A0036(carB)
            STY: STY0076(carA) STY0077(carB)
            STT: t0067(carA) t0068(carB)
            SPT: SPA0067(carA) SPA0068(carB)
            SEC: SC0060(carA) SC0061(carB)
            STM: STM0066(carA) STM0067(carB)
            YPE: YPO0481(carA) YPO0482(carB)
            YPK: y3692(carB) y3693(carA)
            YPM: YP_3697(carB) YP_3698(carA)
            YPA: YPA_4074 YPA_4075
            YPN: YPN_0354 YPN_0355
            YPS: YPTB0623(carA) YPTB0624(carB)
            YPI: YpsIP31758_3453(carB) YpsIP31758_3454(carA)
            SFL: SF0029(carA) SF0030(carB)
            SFX: S0031(carA) S0032(carB)
            SFV: SFV_0026(carA) SFV_0027(carB)
            SSN: SSON_0037(carA) SSON_0038(carB)
            SBO: SBO_0031(carA) SBO_0032(carB)
            SDY: SDY_0054(carA) SDY_0055(carB)
            ECA: ECA3870(carB) ECA3871(carA)
            PLU: plu0603(carA) plu0604(carB)
            BUC: BU144(carB) BU145(carA)
            BAS: BUsg137(carB) BUsg138(carA)
            BAB: bbp134(carB) bbp135(carA)
            BCC: BCc_090(carB) BCc_091(carA)
            WBR: WGLp023(carB) WGLp024(carA)
            SGL: SG0419 SG0420
            ENT: Ent638_0591
            BFL: Bfl122(carA) Bfl123(carB)
            BPN: BPEN_126(carA) BPEN_127(carB)
            HDU: HD0233(carB) HD0235(carA)
            PMU: PM1502(carA) PM1505(carB)
            MSU: MS2236(carB) MS2237(carA)
            XFA: XF1106 XF1107
            XFT: PD0398(carA) PD0399(carB)
            XCC: XCC1841(carA) XCC1843(carB)
            XCB: XC_2346 XC_2348
            XCV: XCV1907(carA) XCV1909(carB)
            XAC: XAC1861(carA) XAC1862(carB)
            XOO: XOO2887(carB) XOO2888(carA)
            XOM: XOO_2739(XOO2739) XOO_2740(XOO2740)
            VCH: VC2389 VC2390
            VCO: VC0395_A1968(carA)
            VVU: VV1_0565 VV1_0566
            VVY: VV0624 VV0625
            VPA: VP0470 VP0471
            VFI: VF0472 VF0473
            PPR: PBPRA0596 PBPRA0597(carB)
            PAE: PA4756(carB) PA4758(carA)
            PAU: PA14_62910(carB) PA14_62930(carA)
            PPU: PP_4723(carB) PP_4724(carA)
            PST: PSPTO_4501(carB) PSPTO_4502(carA)
            PSB: Psyr_4191 Psyr_4192
            PSP: PSPPH_4202(carB) PSPPH_4203(carA)
            PFL: PFL_0830(carA) PFL_0831(carB)
            PFO: Pfl_0766 Pfl_0767
            PEN: PSEEN0781(carA) PSEEN0782(carB)
            PAR: Psyc_0814(carB) Psyc_0815(carA)
            PCR: Pcryo_0829 Pcryo_0830
            ACI: ACIAD2860(carA) ACIAD2861(carB)
            SON: SO_1141(carA) SO_1142(carB)
            SDN: Sden_0995 Sden_0996
            SFR: Sfri_0975 Sfri_0976
            SAZ: Sama_2504
            SHE: Shewmr4_0965 Shewmr4_0966
            SHM: Shewmr7_1003 Shewmr7_1004
            SHN: Shewana3_0967 Shewana3_0968
            ILO: IL0980(carB) IL0981(carA)
            CPS: CPS_3458(carB) CPS_3459(carA)
            PHA: PSHAa1228(carA) PSHAa1229(carB)
            PAT: Patl_2214 Patl_2215
            SDE: Sde_2728 Sde_2729
            MAQ: Maqu_3358 Maqu_3359
            CBU: CBU_1281(carB) CBU_1282(carA)
            CBD: COXBU7E912_1370(carB) COXBU7E912_1371(carA)
            LPN: lpg2023 lpg2625(carB)
            LPF: lpl2000(carA) lpl2550(carB)
            LPP: lpp2005(carA) lpp2678(carB)
            MCA: MCA1852(carB) MCA1853(carA)
            FTU: FTT1663(carA) FTT1664(carB)
            FTF: FTF1663(carA) FTF1664(carB)
            FTW: FTW_1955(carB) FTW_1956(carA)
            FTL: FTL_0029 FTL_0030
            FTH: FTH_0028(carB) FTH_0029(carA)
            FTA: FTA_0036(carB) FTA_0037(carA)
            FTN: FTN_0020(carB) FTN_0021(carA)
            TCX: Tcr_0878 Tcr_0879
            NOC: Noc_2572 Noc_2573
            AEH: Mlg_1981 Mlg_1982
            HCH: HCH_01227(carA) HCH_01228(carB)
            CSA: Csal_3085 Csal_3086
            ABO: ABO_0317(carA) ABO_0318(carB)
            AHA: AHA_2723(carB) AHA_2724(carA)
            BCI: BCI_0559(carA) BCI_0560(carB)
            CRP: CRP_066 CRP_067
            VOK: COSY_0799(carB) COSY_0801(carA)
            NME: NMB1849 NMB1855
            NMA: NMA0602(carB) NMA0608(carA)
            NMC: NMC0363(carB) NMC0370(carA)
            NGO: NGO0048 NGO0053
            CVI: CV_3802(carB) CV_3804(carA)
            RSO: RSc1519(carA) RSc1521(carB)
            REU: Reut_A2175 Reut_A2177
            REH: H16_A2106(carB1) H16_A2452(carB2) H16_A2454(carA)
            RME: Rmet_2193 Rmet_2195
            BMA: BMA0770(carA) BMA0772(carB)
            BMV: BMASAVP1_A1281(carA) BMASAVP1_A1283(carB)
            BML: BMA10299_A0585(carB) BMA10299_A0587(carA)
            BMN: BMA10247_0564(carA) BMA10247_0566(carB)
            BXE: Bxe_A1256 Bxe_A1257
            BUR: Bcep18194_A4432
            BCN: Bcen_0809
            BCH: Bcen2424_1290
            BAM: Bamb_1167 Bamb_1169
            BPS: BPSL1349(carA) BPSL1351(carB)
            BPM: BURPS1710b_1608(carA) BURPS1710b_1610(carB)
            BPL: BURPS1106A_1505(carA) BURPS1106A_1507(carB)
            BPD: BURPS668_1475(carA) BURPS668_1477(carB)
            BTE: BTH_I2781(carB) BTH_I2783(carA)
            PNU: Pnuc_1019
            BPE: BP1452(carA) BP1453(carB)
            BPA: BPP1229(carA) BPP1230(carB)
            BBR: BB1446(carA) BB1447(carB)
            RFR: Rfer_2004 Rfer_2006
            POL: Bpro_2678 Bpro_2679
            PNA: Pnap_1774
            AAV: Aave_2610
            VEI: Veis_1148
            MPT: Mpe_A1261 Mpe_A1262
            HAR: HEAR1164(carA) HEAR1165(carB)
            MMS: mma_2242(carB) mma_2243(carA)
            NEU: NE1661(carb) NE1662(carA)
            NET: Neut_0454 Neut_0455
            NMU: Nmul_A0478 Nmul_A0479
            EBA: ebA4813(carA) ebA4815(carB)
            AZO: azo1381(carA)
            DAR: Daro_0938 Daro_0939
            TBD: Tbd_1127 Tbd_1128
            MFA: Mfla_0778 Mfla_0779
            HPY: HP0919(pyrAb) HP1237(pyrAa)
            HPJ: jhp0853(carB) jhp1158(carA)
            HPA: HPAG1_0900 HPAG1_1179
            HHE: HH0888(carA) HH1688(carB)
            HAC: Hac_0700(carB) Hac_1638(pyrA)
            WSU: WS2050(carA) WS2147(carB)
            TDN: Tmden_0080 Tmden_1467
            CJE: Cj0279(carB) Cj1494c(carA)
            CJR: CJE0327(carB) CJE1667(carA)
            CJJ: CJJ81176_0305(carB) CJJ81176_1486(carA)
            CJU: C8J_0255(carB) C8J_1399(carA)
            CJD: JJD26997_1692(carB) JJD26997_1842(carA)
            CFF: CFF8240_0319(carB) CFF8240_0374(carA) CFF8240_0647
            CCV: CCV52592_0870(carB) CCV52592_0898(carA)
            CHA: CHAB381_1350(carB) CHAB381_1365(carA)
            CCO: CCC13826_0741 CCC13826_1487 CCC13826_1876 CCC13826_2127(carB)
            ABU: Abu_0130(carA) Abu_1372(carB)
            NIS: NIS_0545(carB) NIS_1623(carA)
            SUN: SUN_0176(carA) SUN_1107(carB)
            GSU: GSU1273(carA) GSU1276(carB)
            GME: Gmet_0661 Gmet_1771 Gmet_1774
            PCA: Pcar_1612 Pcar_1613
            PPD: Ppro_2524 Ppro_2527
            DVU: DVU0162(carB) DVU3113(carA)
            DVL: Dvul_0268
            DDE: Dde_0333 Dde_3646
            LIP: LI0939(carB) LI0990(carA)
            BBA: Bd0856(carA) Bd0858(carB)
            DPS: DP3095 DP3096
            ADE: Adeh_1620 Adeh_1729 Adeh_3514
            MXA: MXAN_3388(carB) MXAN_3512(carA)
            SAT: SYN_01625 SYN_01627 SYN_02589
            SFU: Sfum_0008 Sfum_0009 Sfum_3911
            WOL: WD0684(carA) WD1295(carB)
            WBM: Wbm0512 Wbm0654
            AMA: AM803(carA) AM933(carB)
            APH: APH_0249(carB) APH_0381(carA)
            ERU: Erum5170(carA) Erum6310(carB)
            ERW: ERWE_CDS_05420(carA) ERWE_CDS_06620(carB)
            ERG: ERGA_CDS_05320(carA) ERGA_CDS_06530(carB)
            ECN: Ecaj_0525
            ECH: ECH_0378(carB) ECH_0503(carA)
            NSE: NSE_0222(carB) NSE_0502(carA)
            PUB: SAR11_0040(carA) SAR11_0041(carB)
            MLO: mlr2489 mlr2517
            MES: Meso_2083 Meso_2095
            SME: SMb21227 SMc01215(carB) SMc01569(carA)
            ATU: Atu2170(carA) Atu2178(carB)
            ATC: AGR_C_3938 AGR_C_3955(carB)
            RET: RHE_CH02957(carA) RHE_CH02966(carB) RHE_CH03674
            RLE: RL3411(carA) RL3419(carB) RL4210(cysZ)
            BME: BMEI0522 BMEI0526 BMEI1781
            BMF: BAB1_0166 BAB1_1502 BAB1_1508
            BMS: BR1483(carA) BR1488(carB)
            BMB: BruAb1_1478(carA) BruAb1_1482(carB)
            BOV: BOV_1439(carA) BOV_1443(carB)
            BJA: blr7371(carA) blr7377(carB)
            BRA: BRADO1325(carB) BRADO1337(carA)
            BBT: BBta_6791(carA) BBta_6799(carB)
            RPA: RPA1276(carA) RPA4071(carB)
            RPB: RPB_1516 RPB_4142
            RPC: RPC_0960 RPC_3835
            RPD: RPD_1457 RPD_3986
            RPE: RPE_0979 RPE_3960
            NWI: Nwi_2446 Nwi_2449(carB)
            NHA: Nham_2871 Nham_2875
            BHE: BH11590(carA) BH11620(carB)
            BQU: BQ09220(carA) BQ09240(carB)
            BBK: BARBAKC583_0972(carA) BARBAKC583_0975(carB)
            CCR: CC_2834 CC_2900
            SIL: SPO0923(carB) SPO1377(carA)
            SIT: TM1040_0632 TM1040_2294
            RSP: RSP_0818(carB) RSP_1874(carA)
            RSH: Rsph17029_0524 Rsph17029_2475
            RSQ: Rsph17025_0361
            JAN: Jann_1063 Jann_1246
            RDE: RD1_1181 RD1_1963(carA) RD1_3490(carB)
            PDE: Pden_1879
            MMR: Mmar10_2132 Mmar10_2138
            HNE: HNE_0644(carB) HNE_2892(carA)
            ZMO: ZMO1617(carB) ZMO1618(carA)
            NAR: Saro_2230 Saro_2231
            SAL: Sala_0983 Sala_0985
            ELI: ELI_05685 ELI_05695
            GOX: GOX0321 GOX0322
            GBE: GbCGDNIH1_2286 GbCGDNIH1_2288
            RRU: Rru_A2885 Rru_A2886
            MAG: amb0701 amb0702
            MGM: Mmc1_3018 Mmc1_3019
            ABA: Acid345_2194 Acid345_2197
            SUS: Acid_2394
            BSU: BG10195(carA) BG10196(carB) BG10715(pyrAA) BG10716(pyrAB)
            BHA: BH2536(pyrAB) BH2537(pyrAA) BH2895(carB) BH2896(carA)
            BAN: BA4025(carB) BA4026(carA)
            BAR: GBAA4025(carB) GBAA4026(carA)
            BAA: BA_4496 BA_4497
            BAT: BAS3737 BAS3738
            BCE: BC3886 BC3887
            BCA: BCE_3931(carB) BCE_3932(carA)
            BCZ: BCZK3645(carB) BCZK3646(carA)
            BTK: BT9727_3628(carB) BT9727_3629(carA)
            BLI: BL02275(pyrAA) BL02276(pyrAB) BL03245(carA) BL03246(carB)
            BLD: BLi01210(carA) BLi01211(carB) BLi01771(pyrAA) BLi01772(pyrAB)
            BCL: ABC2333(pyrAB) ABC2334(pyrAA) ABC2553(carB) ABC2554(carA)
            BAY: RBAM_011230(carA) RBAM_011240(carB) RBAM_015340 RBAM_015350
            BPU: BPUM_1046(carA) BPUM_1047(carB1) BPUM_1450 BPUM_1451(carB2)
            OIH: OB1079(carA) OB1080(carB) OB1490(pyrAA) OB1491(pyrAB)
            GKA: GK0794 GK0795 GK1151 GK1152
            SAU: SA1045(pyrAA) SA1046(pyrAB)
            SAV: SAV1202(pyrAA) SAV1203(pyrAB)
            SAM: MW1085(pyrAA) MW1086(pyrAB)
            SAR: SAR1178(pyrAA) SAR1179(pyrAB)
            SAS: SAS1136 SAS1137
            SAC: SACOL1214(carA) SACOL1215(carB)
            SAB: SAB1066(pyrAA) SAB1067(pyrAB)
            SAA: SAUSA300_1095(carA) SAUSA300_1096(carB)
            SAO: SAOUHSC_01169 SAOUHSC_01170
            SEP: SE0878 SE0879
            SER: SERP0768(carA) SERP0769(carB)
            SHA: SH1711(pyrAB) SH1712(pyrAA)
            SSP: SSP1569 SSP1570
            LMO: lmo1835(pyrAB) lmo1836(pyrAa)
            LMF: LMOf2365_1863(carB) LMOf2365_1864(carA)
            LIN: lin1949(pyrAB) lin1950(pyrAa)
            LWE: lwe1854(carB) lwe1855(carA)
            LLA: L198033(carB) L43866(carA)
            LLC: LACR_1498 LACR_1709
            LLM: llmg_0894(carA) llmg_1089
            SPY: SPy_0833(carA) SPy_0835(carB)
            SPZ: M5005_Spy_0642(carA) M5005_Spy_0643(carB)
            SPM: spyM18_0893(carA) spyM18_0895(carB)
            SPG: SpyM3_0561(carA) SpyM3_0562(carB)
            SPS: SPs1292 SPs1293
            SPH: MGAS10270_Spy0700(carA) MGAS10270_Spy0702(carB)
            SPI: MGAS10750_Spy0731(carA) MGAS10750_Spy0733(carB)
            SPJ: MGAS2096_Spy0709(carA) MGAS2096_Spy0711(carB)
            SPK: MGAS9429_Spy0697(carA) MGAS9429_Spy0699(carB)
            SPF: SpyM51164(carB) SpyM51165(carA)
            SPA: M6_Spy0660 M6_Spy0662
            SPB: M28_Spy0622(carA) M28_Spy0624(carB)
            SPN: SP_1275 SP_1276
            SPR: spr1153(carB) spr1154(carA)
            SPD: SPD_1131(carB) SPD_1132(carA)
            SAG: SAG1042(carB) SAG1043(carA-1) SAG1362 SAG1363(carA-2)
            SAN: gbs1077 gbs1078 gbs1432 gbs1433
            SAK: SAK_1132(carB) SAK_1133(carA) SAK_1395 SAK_1396(carA)
            SMU: SMU.859(pyrA) SMU.860(pyrAB)
            STC: str0526(carA) str0527(carB)
            STL: stu0526(carA) stu0527(carB)
            SSA: SSA_1341(carB) SSA_1342(carA)
            SGO: SGO_1103(carA) SGO_1104(carB)
            LPL: lp_0526(carB) lp_0527(carA) lp_1783(pyrAA2) lp_2700(pyrAB)
                 lp_2701(pyrAA)
            LJO: LJ1184 LJ1185 LJ1276 LJ1277
            LAC: LBA1149 LBA1150 LBA1379(carB) LBA1380(carA)
            LSA: LSA0954(pyrAA) LSA0955(pyrAB)
            LSL: LSL_0192(carA) LSL_0193(carB) LSL_0829(carA)
            LDB: Ldb1023(carA3) Ldb1024(carB3) Ldb1070(carA2a) Ldb1137(carA2b)
                 Ldb2110(carA1)
            LBU: LBUL_0931 LBUL_0932 LBUL_0975 LBUL_1950 LBUL_1951
            LBR: LVIS_0829 LVIS_0830
            LCA: LSEI_1452 LSEI_1453
            LRE: Lreu_0931
            EFA: EF1716(pyraB) EF1717(pyraA)
            OOE: OEOE_0260 OEOE_0261
            STH: STH1203(carA) STH1204(carB)
            CAC: CAC2644(carB) CAC2645(carA)
            CPE: CPE2572(carB) CPE2573(carA)
            CPF: CPF_2897(carB) CPF_2898(carA)
            CPR: CPR_2576(carB) CPR_2577(carA)
            CTC: CTC01706
            CNO: NT01CX_0382(carB) NT01CX_0383(carA)
            CDF: CD3588(pyrAB1) CD3589(pyrAA1) CD3590(pyrAB2) CD3591(pyrAA2)
            CBF: CLI_1839(carB) CLI_1840(carA)
            CKL: CKL_0649(carA1) CKL_0650(carB1) CKL_2374(carB2)
                 CKL_2375(carA2)
            CHY: CHY_1499(carB) CHY_1500(carA)
            DSY: DSY0398 DSY2042 DSY2043 DSY2859
            DRM: Dred_1683
            PTH: PTH_1810(carA)
            SWO: Swol_1281 Swol_1282
            TTE: TTE0815(carA) TTE0816(carB)
            MTA: Moth_0881 Moth_0882
            MTU: Rv1383(carA) Rv1384(carB)
            MTC: MT1427(carA) MT1428(carB)
            MBO: Mb1418(carA) Mb1419(carB)
            MBB: BCG_1444(carA) BCG_1445(carB)
            MLE: ML0535(carA) ML0536(carB)
            MPA: MAP1118(carA) MAP1119(carB)
            MAV: MAV_3389(carB) MAV_3390(carA)
            MSM: MSMEG_3046(carA) MSMEG_3047(carB) MSMEG_4726
            MUL: MUL_1783(carA)
            MVA: Mvan_2663
            MGI: Mflv_3744
            MMC: Mmcs_2366 Mmcs_2367
            MKM: Mkms_2413
            MJL: Mjls_2407
            CGL: NCgl1547(carB) NCgl1548(cgl1610)
            CGB: cg1813(carB) cg1814(carA)
            CEF: CE1729 CE1730
            CDI: DIP1331(carB) DIP1332(carA)
            CJK: jk1022(carB) jk1023(carA)
            NFA: nfa36190(carB) nfa36200(carA)
            RHA: RHA1_ro07151(carA) RHA1_ro07152(carB)
            SCO: SCO1483(pyrA) SCO1484(pyrAA)
            SMA: SAV6866(carA) SAV6867(carB)
            TWH: TWT365(carB) TWT366(carA)
            TWS: TW403(carA) TW404(carB)
            LXX: Lxx11090(carA) Lxx11100(carB)
            CMI: CMM_1782(carB) CMM_1783(carA)
            ART: Arth_2263
            AAU: AAur_2265(carB) AAur_2266(carA)
            PAC: PPA0999 PPA1000
            NCA: Noca_2430
            TFU: Tfu_1056 Tfu_1057
            FRA: Francci3_3198 Francci3_3199
            FAL: FRAAL4683(carB) FRAAL4684(carA) FRAAL5234(carB)
                 FRAAL5235(carA)
            ACE: Acel_1299
            KRA: Krad_3002
            SEN: SACE_2082(carA) SACE_2083(carB)
            STP: Strop_1855
            BLO: BL0067(carA) BL0068(carB)
            BAD: BAD_0535(carA) BAD_0536(carB)
            RXY: Rxyl_1477 Rxyl_1478
            FNU: FN0421 FN0422
            RBA: RB12113(carB) RB5179(carA)
            LIL: LA0727(carB) LA1239(carA)
            LIC: LIC12883(carB)
            LBJ: LBJ_0774(carB) LBJ_2119(carA)
            LBL: LBL_2116(carA) LBL_2304(carB)
            SYN: sll0370(carB) sll1498(carA)
            SYW: SYNW0830(carB) SYNW1026(carA)
            SYC: syc0819_c(pyrA) syc1970_d(carA)
            SYF: Synpcc7942_0711 Synpcc7942_2122
            SYD: Syncc9605_1152 Syncc9605_1819
            SYE: Syncc9902_0836 Syncc9902_1307
            SYG: sync_1204(carB) sync_1636(carA)
            SYR: SynRCC307_0980(carB) SynRCC307_1331(carA)
            SYX: SynWH7803_1061(carA) SynWH7803_1429(carB)
            CYA: CYA_0195(carA) CYA_1749(carB)
            CYB: CYB_0215(carB) CYB_1236(carA)
            TEL: tll0760 tll2332(pyrA)
            GVI: gll1769 gll3543
            ANA: alr1155 alr3809
            AVA: Ava_1893(carB) Ava_4410
            PMA: Pro0745(carA) Pro0897(carB)
            PMM: PMM0825(carB) PMM0951(carA)
            PMT: PMT0653(carA) PMT0822(carB)
            PMN: PMN2A_0226 PMN2A_0259
            PMI: PMT9312_0848 PMT9312_0975
            PMB: A9601_09091(carA) A9601_10451(carB)
            PMC: P9515_09001(carB) P9515_10341(carA)
            PMF: P9303_13841(carB) P9303_15771(carA)
            PMG: P9301_09071(carA) P9301_10451(carB)
            PMH: P9215_09401(carA) P9215_10771(carB)
            PME: NATL1_08931(carB) NATL1_09281(carA)
            TER: Tery_2310 Tery_2877
            BTH: BT_0556 BT_0557 BT_3866
            BFR: BF2635 BF2636 BF4035
            BFS: BF2657(carB1) BF2658(carA) BF3808(carB2)
            PGI: PG0529(carA) PG0530(carB)
            SRU: SRU_0959(carA) SRU_0960(carB)
            CHU: CHU_3134(carA) CHU_3278(carB)
            GFO: GFO_1074(carB) GFO_2812(carA)
            FJO: Fjoh_0369
            FPS: FP1311(carA) FP1988(carB)
            CTE: CT0066(carA) CT1592(carB2) CT1672(carB1)
            CCH: Cag_0107 Cag_0173 Cag_1787
            PVI: Cvib_0222
            PLT: Plut_0156 Plut_1592 Plut_1651
            DET: DET1201(carA) DET1202(carB)
            DEH: cbdb_A1117(carA) cbdb_A1118(carB)
            DRA: DR_0668 DR_0684
            DGE: Dgeo_2060 Dgeo_2070
            TTH: TTC0247 TTC1706
            TTJ: TTHA0280 TTHA0612
            AAE: aq_1172(carB1) aq_2101(carB2) aq_410(carA)
            TMA: TM0557 TM0558
            TPT: Tpet_0362
            MJA: MJ1019(carA) MJ1378(carB1) MJ1381(carB2)
            MMP: MMP1013(carB) MMP1589(carA)
            MMQ: MmarC5_1820
            MMZ: MmarC7_0836
            MAE: Maeo_0566
            MVN: Mevan_0901
            MAC: MA2143 MA2144
            MBA: Mbar_A2374 Mbar_A2375
            MMA: MM_0038 MM_0039
            MBU: Mbur_0871 Mbur_0872
            MHU: Mhun_0114 Mhun_0115
            MTH: MTH996 MTH997 MTH998
            MST: Msp_1200(carB) Msp_1201(carA)
            MSI: Msm_0488 Msm_0489
            MKA: MK0491(carA) MK0911(carB_2) MK1666(carB_3)
            AFU: AF1273(carA) AF1274(carB)
            HAL: VNG1814G(carB) VNG1815G(carA)
            HMA: rrnAC3360(carB) rrnAC3363(carA)
            HWA: HQ2774A(carA) HQ3311A(carB)
            NPH: NP4506A(carB) NP4830A(carA)
            TAC: Ta0791 Ta0792m
            TVO: TVN0802 TVN0803
            PTO: PTO0899 PTO0900
            PFU: PF1713 PF1714
            RCI: RCIX1367(carA) RCIX1369(carB)
            IHO: Igni_1400
            HBU: Hbut_0302 Hbut_0303
            SSO: SSO0640(carA) SSO0641(carB)
            STO: ST1503 ST1504
            SAI: Saci_1619(pyrA) Saci_1620(carB)
            PAI: PAE0946 PAE0947
STRUCTURES  PDB: 1BXR  1C30  1C3O  1CE8  1CS0  1JDB  1KEE  1M6V  1T36  
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.5.5
            ExPASy - ENZYME nomenclature database: 6.3.5.5
            ExplorEnz - The Enzyme Database: 6.3.5.5
            ERGO genome analysis and discovery system: 6.3.5.5
            BRENDA, the Enzyme Database: 6.3.5.5
            CAS: 37233-48-0
///
ENTRY       EC 6.3.5.6                  Enzyme
NAME        asparaginyl-tRNA synthase (glutamine-hydrolysing);
            Asp-AdT;
            Asp-tRNAAsn amidotransferase;
            aspartyl-tRNAAsn amidotransferase;
            Asn-tRNAAsn:L-glutamine amido-ligase (ADP-forming)
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Carbon-nitrogen ligases with glutamine as amido-N-donor
SYSNAME     aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming)
REACTION    ATP + aspartyl-tRNAAsn + L-glutamine = ADP + phosphate +
            asparaginyl-tRNAAsn + L-glutamate [RN:R04212]
ALL_REAC    R04212
SUBSTRATE   ATP [CPD:C00002];
            aspartyl-tRNA(Asn) [CPD:C06113];
            L-glutamine [CPD:C00064]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            asparaginyl-tRNA(Asn) [CPD:C03402];
            L-glutamate [CPD:C00025]
COMMENT     This reaction forms part of a two-reaction system for producing
            asparaginyl-tRNA in Deinococcus radiodurans and other organisms
            lacking a specific enzyme for asparagine synthesis. In the first
            step, a non-discriminating ligase (EC 6.1.1.23, aspartate---tRNAAsn
            ligase) mischarges tRNAAsn with aspartate, leading to the formation
            of Asp-tRNAAsn. The aspartyl-tRNAAsn is not used in protein
            synthesis until the present enzyme converts it into
            asparaginyl-tRNAAsn (aspartyl-tRNAAsp is not a substrate for this
            reaction). Ammonia or asparagine can substitute for the preferred
            substrate glutamine.
REFERENCE   1  [PMID:11880622]
  AUTHORS   Min B, Pelaschier JT, Graham DE, Tumbula-Hansen D, Soll D.
  TITLE     Transfer RNA-dependent amino acid biosynthesis: an essential route
            to asparagine formation.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 2678-83.
  ORGANISM  Deinococcus radiodurans [GN:dra], Thermus thermophilus
REFERENCE   2  [PMID:9789001]
  AUTHORS   Curnow AW, Tumbula DL, Pelaschier JT, Min B, Soll D.
  TITLE     Glutamyl-tRNA(Gln) amidotransferase in Deinococcus radiodurans may
            be confined to asparagine biosynthesis.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 12838-43.
  ORGANISM  Deinococcus radiodurans [GN:dra], Bacillus subtilis [GN:bsu]
REFERENCE   3  [PMID:10966471]
  AUTHORS   Ibba M, Soll D.
  TITLE     Aminoacyl-tRNA synthesis.
  JOURNAL   Annu. Rev. Biochem. 69 (2000) 617-50.
  ORGANISM  Deinococcus radiodurans [GN:dra], Thermus thermophilus, Bacillus
            subtilis [GN:bsu]
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00252  Alanine and aspartate metabolism
ORTHOLOGY   KO: K02433  aspartyl-tRNA(Asn)/glutamyl-tRNA (Gln) amidotransferase
                        subunit A
            KO: K02434  aspartyl-tRNA(Asn)/glutamyl-tRNA (Gln) amidotransferase
                        subunit B
            KO: K02435  aspartyl-tRNA(Asn)/glutamyl-tRNA (Gln) amidotransferase
                        subunit C
            KO: K03866  asparaginyl-tRNA synthase
GENES       OSA: 4333591 4337177
            CME: CMM318C
            PIC: PICST_52015(PET112)
            CGR: CAGL0A04653g CAGL0M13585g
            ANI: AN9400.2
            AFM: AFUA_3G04130
            TAN: TA11065
            YPE: YPO3261
            YPK: y0928
            YPM: YP_0671(gatA)
            YPA: YPA_2752
            YPN: YPN_0835
            YPS: YPTB0862
            ECA: ECA3499
            PLU: plu2200
            XCC: XCC0292(gatA)
            XCB: XC_0302
            XCV: XCV1030
            XAC: XAC0306(gatA)
            PAE: PA4482(gatC) PA4483(gatA) PA4484(gatB)
            PAU: PA14_58170(gatC) PA14_58180(gatA) PA14_58190(gatB)
            PPU: PP_0930(gatB) PP_0931(gatA) PP_0932(gatC)
            PST: PSPTO_4473(gatC) PSPTO_4474(gatA) PSPTO_4475(gatB)
            PSB: Psyr_4164 Psyr_4165 Psyr_4166
            PSP: PSPPH_4173(gatC) PSPPH_4174(gatA) PSPPH_4175(gatB)
            PFL: PFL_0893(gatB) PFL_0894(gatA) PFL_0895(gatC)
            PFO: Pfl_0835 Pfl_0836 Pfl_0837
            PEN: PSEEN1071(gatB) PSEEN1072(gatA) PSEEN1073(gatC)
            PAR: Psyc_0480(gatB) Psyc_0481(gatA) Psyc_0482(gatC)
            PCR: Pcryo_0475 Pcryo_0476 Pcryo_0477
            ACI: ACIAD0822(gatB) ACIAD0823(gatA) ACIAD0824(gatC)
            ILO: IL1971(gatA)
            PHA: PSHAa0910
            PAT: Patl_3426
            SDE: Sde_1128 Sde_3193 Sde_3194 Sde_3195
            CBU: CBU_1473(gatC) CBU_1474(gatA) CBU_1475(gatB)
            LPN: lpg1735(gatC) lpg1736(gatA) lpg1737(gatB)
            LPF: lpl1699(gatC) lpl1700(gatA) lpl1701(gatB)
            LPP: lpp1700(gatC) lpp1701(gatA) lpp1702(gatB)
            MCA: MCA0097(gatB) MCA0098(gatA) MCA0099(gatC)
            FTU: FTT0019(gatC) FTT0020(gatA) FTT0021(gatB)
            FTF: FTF0019(gatC) FTF0020(gatA) FTF0021(gatB)
            FTW: FTW_0093(gatC)
            FTL: FTL_1841 FTL_1842 FTL_1843
            FTH: FTH_1776(gatB) FTH_1777(gatA) FTH_1778(gatC)
            FTN: FTN_1689(gatB) FTN_1690(gatA) FTN_1691(gatC)
            TCX: Tcr_1627 Tcr_1628 Tcr_1629
            NOC: Noc_2014 Noc_2635 Noc_2636
            AEH: Mlg_0166 Mlg_0167 Mlg_0168
            HCH: HCH_05336(gatC) HCH_05337(gatA) HCH_05338(gatB)
            CSA: Csal_0152 Csal_2241 Csal_2242 Csal_2243
            ABO: ABO_0527(gatB) ABO_0528(gatA) ABO_0529(gatC)
            CRP: CRP_042 CRP_043
            RMA: Rmag_0343 Rmag_0344 Rmag_0345
            NME: NMB1355 NMB1356 NMB1358
            NMA: NMA1567(gatC) NMA1568(gatA) NMA1570(gatB)
            NGO: NGO0660 NGO0662 NGO0663
            CVI: CV_4354(gatB) CV_4355(gatA) CV_4356(gatC)
            RSO: RSc0054(gatB) RSc0057(gatA) RSc0058(gatC)
            REU: Reut_A0071 Reut_A0074 Reut_A0075
            REH: H16_A0108(gatB) H16_A0111(gatA1) H16_A0112(gatC)
            RME: Rmet_0046 Rmet_0049 Rmet_0050
            BMA: BMA0163(gatC) BMA0164(gatA) BMA0165(gatB)
            BXE: Bxe_A0952 Bxe_A4395 Bxe_A4396 Bxe_A4397 Bxe_B1367 Bxe_C0428
                 Bxe_C0436
            BUR: Bcep18194_A6458 Bcep18194_A6459 Bcep18194_A6460
            BCN: Bcen_2493 Bcen_2494 Bcen_2495
            BCH: Bcen2424_1022 Bcen2424_3107 Bcen2424_3108 Bcen2424_3109
            BAM: Bamb_0886 Bamb_3162 Bamb_3163 Bamb_3164
            BPS: BPSL0187(gatC) BPSL0188(gatA) BPSL0189(gatB)
            BPM: BURPS1710b_0367(gatC) BURPS1710b_0368(gatA)
                 BURPS1710b_0369(gatB)
            BTE: BTH_I0147(gatC) BTH_I0148(gatA) BTH_I0149
            BPE: BP0371(gatB) BP0372(gatA) BP0373(gatC)
            BPA: BPP4057(gatC) BPP4058(gatA) BPP4059(gatB)
            BBR: BB4530(gatC) BB4531(gatA) BB4532(gatB)
            RFR: Rfer_3924 Rfer_3925 Rfer_3926
            POL: Bpro_0219 Bpro_0220 Bpro_0221
            NEU: NE2071(gatC) NE2072(gatA) NE2073(gatB)
            NET: Neut_1593 Neut_1594 Neut_1595
            NMU: Nmul_A0321 Nmul_A0322 Nmul_A0323
            EBA: ebA3029(gatB) ebA3030(gatA)
            DAR: Daro_0117 Daro_0118 Daro_0120
            TBD: Tbd_0257 Tbd_0258 Tbd_0259
            MFA: Mfla_2488 Mfla_2489 Mfla_2490
            HPY: HP0658(gatB) HP0830(gatA)
            HPJ: jhp0603(gatB) jhp0769(gatA) jhp0909(gatC)
            HPA: HPAG1_0643 HPAG1_0816 HPAG1_0956
            HHE: HH0701(gatA) HH0796(gatB) HH1248(gatC)
            HAC: Hac_0843(gatB) Hac_1060(gatC) Hac_1198(gatA)
            WSU: WS0558(gatC) WS1896(gatA) WS2005(gatB)
            TDN: Tmden_0773 Tmden_1250 Tmden_1333
            CJE: Cj0398(gatC) Cj1059c(gatA) Cj1197c(gatB)
            CJR: CJE0447(gatC) CJE1202(gatA) CJE1331(gatB)
            CFF: CFF8240_0611 CFF8240_0774(gatB) CFF8240_1146(gatC)
            GSU: GSU3380(gatB) GSU3381(gatA) GSU3383(gatC)
            GME: Gmet_0073 Gmet_0075 Gmet_0076
            PCA: Pcar_2167 Pcar_2168 Pcar_2169
            DVU: DVU0808(gatA) DVU0809(gatC) DVU1885(gatB)
            DDE: Dde_1020 Dde_1021 Dde_2615
            LIP: LI0885 LI0886 LI1007(gatB)
            BBA: Bd0058(gatC) Bd0059(gatA) Bd0060(gatB)
            DPS: DP0643 DP0644 DP0714
            ADE: Adeh_4187 Adeh_4188 Adeh_4189
            MXA: MXAN_1462(gatC) MXAN_1463(gatA) MXAN_1464(gatB)
            SAT: SYN_00307 SYN_00308 SYN_00309 SYN_02603 SYN_02604
            SFU: Sfum_1705 Sfum_3366 Sfum_3367 Sfum_3503 Sfum_3504
            RPR: RP151(gatB) RP152(gatA) RP153(gatC)
            RTY: RT0140(gatB) RT0141(gatA) RT0142(gatC)
            RCO: RC0193(gatB) RC0194(gatA) RC0195(gatC)
            RFE: RF_1128(gatC) RF_1129(gatA) RF_1130(gatB)
            RBE: RBE_1133(gatC) RBE_1134(gatA) RBE_1135(gatB)
            WOL: WD0037 WD0146(gatB) WD0505(gatA)
            WBM: Wbm0102 Wbm0704 Wbm0763
            AMA: AM1030 AM426(gatB) AM698(gatA)
            APH: APH_0470(gatB) APH_0748(gatA) APH_1113(gatC)
            ERU: Erum2850(gatB) Erum3670(gatA) Erum7910(gatC)
            ERW: ERWE_CDS_02910(gatB) ERWE_CDS_03780(gatA)
                 ERWE_CDS_08370(gatC)
            ERG: ERGA_CDS_02860(gatB) ERGA_CDS_03730(gatA)
                 ERGA_CDS_08260(gatC)
            ECN: Ecaj_0268 Ecaj_0352 Ecaj_0827
            ECH: ECH_0703(gatA) ECH_0813(gatB) ECH_1025(gatC)
            NSE: NSE_0084(gatB) NSE_0256(gatA)
            PUB: SAR11_1076(gatB) SAR11_1077(gatA) SAR11_1078(gatC)
            MLO: mll0675 mlr0190 msl0677
            MES: Meso_1363 Meso_1365 Meso_1720
            SME: SMc01350(gatB) SMc01352(gatA) SMc01353(gatC)
            ATU: Atu1318(gatC) Atu1319(gatA) Atu1324(gatB)
            ATC: AGR_C_2429 AGR_C_2430 AGR_C_2438
            RET: RHE_CH01854(gatC) RHE_CH01855(gatA2) RHE_CH01862(gatB)
            RLE: RL0225 RL2075(gatC) RL2076(gatA) RL2082(gatB) pRL110427
                 pRL120136 pRL90294
            BME: BMEI1068 BMEII0674 BMEII0675
            BMF: BAB1_0918(gatB) BAB2_0645(gatC) BAB2_0646(gatA)
            BMS: BR0899(gatB) BRA0594(gatA) BRA0595(gatC)
            BMB: BruAb1_0911(gatB) BruAb2_0629(gatC) BruAb2_0630(gatA)
            BJA: bll5087(gatB) bll5089(gatA) bsl5090(gatC)
            RPA: RPA3104(gatB) RPA3107(gatA2) RPA3111(gatC)
            RPB: RPB_2434 RPB_2438 RPB_2440
            RPC: RPC_2260 RPC_2264 RPC_2269
            RPD: RPD_1881 RPD_3014 RPD_3016 RPD_3018 RPD_3802
            RPE: RPE_1796 RPE_3356 RPE_3358 RPE_3362
            NWI: Nwi_1997 Nwi_2001 Nwi_2003
            NHA: Nham_2271 Nham_2275 Nham_2277
            BHE: BH05950(gatB) BH08230(gatC) BH08240(gatA)
            BQU: BQ06340(gatA) BQ06350(gatC) BQ07280(gatB)
            CCR: CC_2436 CC_2437 CC_2438
            SIL: SPO2847(gatB) SPO2969(gatA) SPO2970(gatC)
            SIT: TM1040_0058 TM1040_0327 TM1040_0701 TM1040_1918 TM1040_1919
            RSP: RSP_1986(gatB) RSP_2270(gatA) RSP_6043(gatC)
            JAN: Jann_0426 Jann_1221 Jann_1222 Jann_1866
            RDE: RD1_0035 RD1_2000(gatA) RD1_2001(gatC) RD1_3333(gatB)
            MMR: Mmar10_1702 Mmar10_1706 Mmar10_1707
            HNE: HNE_2291(gatB) HNE_2293(gatA) HNE_2299(gatC)
            ZMO: ZMO0782(gatB) ZMO0783(gatA) ZMO0784(gatC)
            NAR: Saro_2831 Saro_2832 Saro_2833
            SAL: Sala_0840 Sala_0841 Sala_0842
            ELI: ELI_01365 ELI_01375 ELI_01390
            GOX: GOX2382 GOX2383 GOX2384
            GBE: GbCGDNIH1_0950 GbCGDNIH1_0952 GbCGDNIH1_0953
            RRU: Rru_A3175 Rru_A3176 Rru_A3177
            MAG: amb1584 amb1585
            MGM: Mmc1_0681 Mmc1_0682 Mmc1_0683
            ABA: Acid345_0499 Acid345_0501 Acid345_4716
            SUS: Acid_1073 Acid_1074 Acid_7720
            BSU: BG12838(gatC) BG12839(gatA) BG12840(gatB)
            BHA: BH0665 BH0666 BH0667
            BAN: BA0320(gatC) BA0321(gatA) BA0322(gatB)
            BAR: GBAA0320(gatC) GBAA0321(gatA) GBAA0322(gatB)
            BAA: BA_0890 BA_0891 BA_0892
            BAT: BAS0305 BAS0306 BAS0307
            BCE: BC0350 BC0351 BC0352
            BCA: BCE_0349(gatC) BCE_0350(gatA) BCE_0351(gatB)
            BCZ: BCZK0291(gatC) BCZK0292(gatA) BCZK0293(gatB)
            BTK: BT9727_0288(gatC) BT9727_0289(gatA) BT9727_0290(gatB)
            BTL: BALH_0312(gatC) BALH_0313(gatA) BALH_0314(gatB)
            BLI: BL00600(gatC) BL00601(gatA) BL00602(gatB)
            BLD: BLi00730(gatC) BLi00731(gatA) BLi00732(gatB)
            BCL: ABC1096(gatC) ABC1097(gatA) ABC1098(gatB)
            OIH: OB0764 OB0765 OB0766
            GKA: GK0281 GK0282 GK0283
            SAU: SA1715 SA1716 SA1717
            SAV: SAV1899 SAV1900 SAV1901
            SAM: MW1840 MW1841 MW1842
            SAR: SAR1991(gatB) SAR1992(gatA) SAR1993(gatC)
            SAS: SAS1822 SAS1823 SAS1824
            SAC: SACOL1960(gatB) SACOL1961(gatA) SACOL1962(gatC)
            SAB: SAB1832c(gatB) SAB1833c(gatA) SAB1834c(gatC)
            SAA: SAUSA300_1880(gatB) SAUSA300_1881(gatA) SAUSA300_1882(gatC)
            SAO: SAOUHSC_02116 SAOUHSC_02117 SAOUHSC_02118
            SEP: SE1584 SE1585 SE1586
            SER: SERP1437(gatB) SERP1438(gatA) SERP1439(gatC)
            SHA: SH1051(gatC) SH1052(gatA) SH1053(gatB)
            SSP: SSP0890 SSP0891 SSP0892
            LMO: lmo1754(gatB) lmo1755(gatA) lmo1756(gatC)
            LMF: LMOf2365_1779(gatB) LMOf2365_1780(gatA) LMOf2365_1781(gatC)
            LIN: lin1866(gatB) lin1867(gatA) lin1868(gatC)
            LWE: lwe1771(gatB) lwe1772(gatA) lwe1773(gatC)
            LLA: L0473(gatA) L0474(gatB) L0475(gatC)
            LLC: LACR_0169 LACR_0170 LACR_0171
            LLM: llmg_0174(gatC) llmg_0175(gatA) llmg_0176(gatB)
            SPY: SPy_1770(gatB) SPy_1771(gatA) SPy_1772(gatC)
            SPZ: M5005_Spy_1506(gatB) M5005_Spy_1507(gatA)
                 M5005_Spy_1508(gatC)
            SPM: spyM18_1839(gatB) spyM18_1840(gatA) spyM18_1841(gatC)
            SPG: SpyM3_1539(gatB) SpyM3_1540(gatA) SpyM3_1541(gatC)
            SPS: SPs0325 SPs0326 SPs0327
            SPH: MGAS10270_Spy1574(gatB) MGAS10270_Spy1575(gatA)
                 MGAS10270_Spy1576(gatC)
            SPI: MGAS10750_Spy1566(gatB) MGAS10750_Spy1567(gatA)
                 MGAS10750_Spy1568(gatC)
            SPJ: MGAS2096_Spy1534(gatB) MGAS2096_Spy1535(gatA)
                 MGAS2096_Spy1536(gatC)
            SPK: MGAS9429_Spy1508(gatB) MGAS9429_Spy1509(gatA)
                 MGAS9429_Spy1510(gatC)
            SPF: SpyM50337(gatC) SpyM50338(gatA)
            SPA: M6_Spy1500 M6_Spy1501 M6_Spy1502
            SPB: M28_Spy1495(gatB) M28_Spy1496(gatA) M28_Spy1497(gatC)
            SPN: SP_0436 SP_0437 SP_0438
            SPR: spr0393(gatB) spr0394(gatA) spr0395(gatC)
            SPD: SPD_0396(gatB) SPD_0397(gatA) SPD_0398(gatC)
            SAG: SAG1667(gatB) SAG1668(gatA) SAG1669(gatC)
            SAN: gbs1711 gbs1712 gbs1713
            SAK: SAK_1679(gatB) SAK_1680(gatA) SAK_1681(gatC)
            SMU: SMU.1819(gatB) SMU.1820c SMU.1821c
            STC: str1625(gatB) str1626(gatA) str1627(gatC)
            STL: stu1625(gatB) stu1626(gatA) stu1627(gatC)
            STE: STER_1590 STER_1591 STER_1592
            SSA: SSA_0569(gatC) SSA_0570(gatA) SSA_0571(gatB)
            SSU: SSU05_0355 SSU05_0356
            SSV: SSU98_0346 SSU98_0347
            LPL: lp_1147(gatC) lp_1148(gatA) lp_1149(gatB)
            LJO: LJ1716 LJ1717 LJ1718
            LAC: LBA0531(gatC) LBA0532(gatA) LBA0533(gatB)
            LSA: LSA1546(gatB) LSA1547(gatA) LSA1548(gatC)
            LSL: LSL_1344(gatB) LSL_1345(gatA) LSL_1346(gatC)
            LDB: Ldb0468(gatC) Ldb0469(gatA) Ldb0470(gatB)
            LBU: LBUL_0416 LBUL_0417 LBUL_0418
            LBR: LVIS_1629 LVIS_1630 LVIS_1631
            LCA: LSEI_1057 LSEI_1058 LSEI_1059
            LGA: LGAS_1511 LGAS_1512 LGAS_1513
            PPE: PEPE_1368 PEPE_1369 PEPE_1370
            EFA: EF0724(gatC) EF0725(gatA) EF0726(gatB)
            OOE: OEOE_1693 OEOE_1694 OEOE_1695
            LME: LEUM_1579 LEUM_1580 LEUM_1581
            STH: STH2820 STH2821 STH2822
            CAC: CAC2669 CAC2670 CAC2671
            CTC: CTC02392 CTC02393
            CNO: NT01CX_0430(gatB) NT01CX_0431(gatA) NT01CX_0432(gatC)
            CHY: CHY_1101(gatC) CHY_1102(gatA) CHY_1103(gatB)
            DSY: DSY3885 DSY3886 DSY3887 DSY4734
            SWO: Swol_0372 Swol_0373 Swol_0374
            TTE: TTE0606(gatC) TTE0607(gatA) TTE0608(gatB)
            MTA: Moth_2008 Moth_2009 Moth_2010
            MGE: MG_099 MG_100
            MPN: MPN237(gatA) MPN238(PET112)
            MPU: MYPU_2000(gatA) MYPU_2010
            MPE: MYPE2090 MYPE2100(gatA) MYPE2110(gatB)
            MGA: MGA_0412(gatB) MGA_0413(gatA)
            MMY: MSC_0761(gatB) MSC_0762(gatA) MSC_0763(gatC)
            MMO: MMOB3760(gatB) MMOB3770(gatA)
            MHY: mhp029(gatA) mhp030(gatB)
            MHJ: MHJ_0024(gatA) MHJ_0025(gatB)
            MHP: MHP7448_0028(gatA) MHP7448_0029(gatB)
            MSY: MS53_0091(gatB) MS53_0092(gatA) MS53_0093(gatC)
            MCP: MCAP_0709(gatB) MCAP_0710(gatA) MCAP_0711(gatC)
            UUR: UU544(gatB) UU545(gatA)
            MFL: Mfl162 Mfl163
            MTU: Rv3009c Rv3011c(gatA) Rv3012c
            MTC: MT3089(gatB) MT3091(gatA) MT3092(gatC)
            MBO: Mb3034c(gatB) Mb3036c(gatA) Mb3037c(gatC)
            MLE: ML1700(gatB) ML1702(gatA) ML1703(gatC)
            MPA: MAP3042c(gatB) MAP3045c(gatA) MAP3046c(gatC)
            MAV: MAV_3856 MAV_3859 MAV_3860(gatC)
            MSM: MSMEG_1088(gatA) MSMEG_2364(gatC) MSMEG_2365 MSMEG_2367
            MUL: MUL_1939(gatA)
            MMC: Mmcs_1890 Mmcs_1891 Mmcs_1894
            CGL: NCgl1198(gatC) NCgl1199(cgl1247) NCgl1211(cgl1259)
            CGB: cg1403(gatC) cg1404(gatA) cg1420(gatB)
            CEF: CE1344 CE1345 CE1351
            CDI: DIP1079(gatC) DIP1080(gatA) DIP1089(gatB)
            CJK: jk1306(gatB) jk1311(gatA)
            NFA: nfa42380(gatB) nfa42580(gatA) nfa42590(gatC)
            RHA: RHA1_ro06473(gatC) RHA1_ro06474(gatA) RHA1_ro06480
            SCO: SCO5498(gatC) SCO5499(gatA) SCO5501(gatB)
            SMA: SAV2743(gatB) SAV2745(gatA) SAV2746(gatC)
            TWH: TWT411(gatB) TWT412(gatA) TWT413(gatC)
            TWS: TW355(gatC) TW356(gatA) TW357(gatB)
            LXX: Lxx14340(gatB) Lxx14350(gatA) Lxx14360(gatC)
            ART: Arth_1306 Arth_1307 Arth_1308
            PAC: PPA1122 PPA1123 PPA1124
            TFU: Tfu_0605 Tfu_0606 Tfu_0609
            FRA: Francci3_3642 Francci3_3644 Francci3_3645
            FAL: FRAAL5853(gatB) FRAAL5855(gatA) FRAAL5856(gatC)
            ACE: Acel_0696 Acel_0697 Acel_0698
            BLO: BL0402(gatB) BL0403(gatA) BL0404(gatC)
            BAD: BAD_1457(gatB) BAD_1458(gatA) BAD_1459(gatC)
            RXY: Rxyl_0829 Rxyl_0830 Rxyl_0834
            FNU: FN0753 FN0754 FN0755
            RBA: RB10852(gatB) RB4143(gatA) RB8359(gatC)
            CTR: CT002(gatC) CT003(gatA) CT004(gatB)
            CTA: CTA_0003(gatC) CTA_0004(gatA) CTA_0005(gatB)
            CMU: TC0270 TC0271 TC0272
            CPN: CPn0002(gatC) CPn0003(gatA) CPn0004(gatB)
            CPA: CP0771 CP0772 CP0773
            CPJ: CPj0002(gatC) CPj0003(gatA) CPj0004(gatB)
            CPT: CpB0003 CpB0004 CpB0005
            CCA: CCA00287(gatC) CCA00289(gatB)
            CAB: CAB285(gatC) CAB286(gatA) CAB287(gatB)
            CFE: CF0714(gatB) CF0715(gatA) CF0716(gatC)
            PCU: pc0669(gatB) pc0670(gatA) pc0671(gatC)
            BBU: BB0341(gatB) BB0342(gluA)
            BGA: BG0342(gatB) BG0343(gatA)
            BAF: BAPKO_0350(gatB) BAPKO_0351(gatA)
            TPA: TP1020 TP1021
            TDE: TDE0575(gatB) TDE0576(gatA) TDE0577(gatC)
            LIL: LA0256(gatB) LA2507(gatA) LA2508(gatC)
            LIC: LIC10221(gatB) LIC11460(gatC) LIC11461(gatA)
            LBJ: LBJ_1660 LBJ_1661(gatC) LBJ_2784(gatB)
            LBL: LBL_0287(gatB) LBL_1879 LBL_1880(gatC)
            SYN: sll1435(pet112) slr0033 slr0877
            SYW: SYNW0292(gatC) SYNW1031(gatA) SYNW2356(gatB)
            SYC: syc1386_c(pet112) syc1780_c(gatC) syc1975_d(gatA)
            SYF: Synpcc7942_0118 Synpcc7942_2117 Synpcc7942_2322
            SYD: Syncc9605_0287 Syncc9605_1157 Syncc9605_2497
            SYE: Syncc9902_1302 Syncc9902_2057 Syncc9902_2169
            SYG: sync_0337(gatC) sync_1631(gatA) sync_2739(gatB)
            CYA: CYA_0359(gatB) CYA_1343(gatC) CYA_1419(gatA)
            CYB: CYB_0708(gatB) CYB_1605(gatA) CYB_2217(gatC)
            TEL: tll1003 tlr2394 tsl1524
            GVI: gll1528 gll2342 gsl3282
            ANA: all1053 alr1396 asl3192
            AVA: Ava_3747 Ava_3890 Ava_3952
            PMA: Pro0052(gatB) Pro0265(gatC) Pro0750(gatA)
            PMM: PMM0048(gatB) PMM0235(gatC) PMM0946(gatA)
            PMT: PMT0648(gatA) PMT1815(gatC) PMT2139(gatB)
            PMN: PMN2A_0264 PMN2A_1381 PMN2A_1602
            PMI: PMT9312_0049 PMT9312_0237 PMT9312_0853
            TER: Tery_2065 Tery_3843 Tery_4579
            SRU: SRU_0671 SRU_1282(gatC) SRU_1902
            CHU: CHU_0025(gatA) CHU_1447(gatB) CHU_2829(gatC)
            CTE: CT0268(gatA) CT1833(gatC) CT2215(gatB)
            CCH: Cag_0318 Cag_0465 Cag_1873
            PLT: Plut_0163 Plut_0337 Plut_1749
            DET: DET1334(gatC) DET1335(gatA) DET1550(gatB)
            DEH: cbdb_A1282(gatC) cbdb_A1284(gatA) cbdb_A1643(gatB)
            DRA: DR_1275 DR_1856 DR_2555
            DGE: Dgeo_0414 Dgeo_0760 Dgeo_0933
            TTH: TTC0205 TTC0521 TTC1620
            TTJ: TTHA0366 TTHA0573 TTHA0876
            AAE: aq_2147a(gatC) aq_247(gatA) aq_461(gatB)
            TMA: TM0252 TM1272 TM1273
            MJA: MJ0160 MJ0243 MJ1160
            MMP: MMP0946 MMP1510
            MAC: MA4522(gatC) MA4523(gatA) MA4524(gatB)
            MBA: Mbar_A0882 Mbar_A0883 Mbar_A0884
            MMA: MM_1226 MM_1227 MM_1228
            MBU: Mbur_1654 Mbur_1655 Mbur_1656
            MTP: Mthe_0176 Mthe_0177 Mthe_0178
            MHU: Mhun_1012 Mhun_1013 Mhun_1014
            MTH: MTH1280 MTH1496
            MST: Msp_0181(gatA) Msp_0269(gatB)
            MKA: MK0238(gatA) MK0960(gatB)
            AFU: AF2116(gatB-2) AF2328(gatC) AF2329(gatA-2)
            HAL: VNG0345G(gatB2) VNG0870G(gatC) VNG0872G(gatA)
            HMA: rrnAC1355(gatA1) rrnAC1356(gatC) rrnAC1642(gatB)
            HWA: HQ1266A(aatB) HQ1687A(aatA) HQ1688A(aatC)
            NPH: NP1220A(aatB) NP1454A(aatC) NP1456A(aatA)
            SSO: SSO0232(gatB-1) SSO0957(gatA-2) SSO6855(gatC)
            STO: ST0282 ST1283 STS140
            SAI: Saci_0700(gatB) Saci_1329(gatC) Saci_1330(gatA)
            PAI: PAE1525(gatA)
            NEQ: NEQ185 NEQ360
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.5.6
            ExPASy - ENZYME nomenclature database: 6.3.5.6
            ExplorEnz - The Enzyme Database: 6.3.5.6
            ERGO genome analysis and discovery system: 6.3.5.6
            BRENDA, the Enzyme Database: 6.3.5.6
            CAS: 37211-76-0
///
ENTRY       EC 6.3.5.7                  Enzyme
NAME        glutaminyl-tRNA synthase (glutamine-hydrolysing);
            Glu-AdT;
            Glu-tRNAGln amidotransferase;
            glutamyl-tRNAGln amidotransferase;
            Glu-tRNAGln:L-glutamine amido-ligase (ADP-forming)
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Carbon-nitrogen ligases with glutamine as amido-N-donor
SYSNAME     glutamyl-tRNAGln:L-glutamine amido-ligase (ADP-forming)
REACTION    ATP + glutamyl-tRNAGln + L-glutamine = ADP + phosphate +
            glutaminyl-tRNAGln + L-glutamate [RN:R03905]
ALL_REAC    R03905
SUBSTRATE   ATP [CPD:C00002];
            glutamyl-tRNA(Gln) [CPD:C06112];
            L-glutamine [CPD:C00064]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            glutaminyl-tRNA(Gln) [CPD:C02282];
            L-glutamate [CPD:C00025]
COMMENT     In systems lacking discernible glutamine---tRNA ligase (EC
            6.1.1.18), glutaminyl-tRNAGln is formed by a two-enzyme system. In
            the first step, a nondiscriminating ligase (EC 6.1.1.24,
            glutamate---tRNAGln ligase) mischarges tRNAGln with glutamate,
            forming glutamyl-tRNAGln. The glutamyl-tRNAGln is not used in
            protein synthesis until the present enzyme converts it into
            glutaminyl-tRNAGln (glutamyl-tRNAGlu is not a substrate for this
            reaction). Ammonia or asparagine can substitute for the preferred
            substrate glutamine.
REFERENCE   1  [PMID:11371208]
  AUTHORS   Horiuchi KY, Harpel MR, Shen L, Luo Y, Rogers KC, Copeland RA.
  TITLE     Mechanistic studies of reaction coupling in Glu-tRNAGln
            amidotransferase.
  JOURNAL   Biochemistry. 40 (2001) 6450-7.
  ORGANISM  Streptococcus pyogenes
REFERENCE   2  [PMID:9789001]
  AUTHORS   Curnow AW, Tumbula DL, Pelaschier JT, Min B, Soll D.
  TITLE     Glutamyl-tRNA(Gln) amidotransferase in Deinococcus radiodurans may
            be confined to asparagine biosynthesis.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 12838-43.
  ORGANISM  Deinococcus radiodurans [GN:dra]
REFERENCE   3  [PMID:10966471]
  AUTHORS   Ibba M, Soll D.
  TITLE     Aminoacyl-tRNA synthesis.
  JOURNAL   Annu. Rev. Biochem. 69 (2000) 617-50.
  ORGANISM  Deinococcus radiodurans [GN:dra], Bacillus subtilis [GN:bsu]
PATHWAY     PATH: map00251  Glutamate metabolism
            PATH: map00252  Alanine and aspartate metabolism
ORTHOLOGY   KO: K02433  aspartyl-tRNA(Asn)/glutamyl-tRNA (Gln) amidotransferase
                        subunit A
            KO: K02434  aspartyl-tRNA(Asn)/glutamyl-tRNA (Gln) amidotransferase
                        subunit B
            KO: K02435  aspartyl-tRNA(Asn)/glutamyl-tRNA (Gln) amidotransferase
                        subunit C
            KO: K03330  glutamyl-tRNA(Gln) amidotransferase subunit E
            KO: K03865  glutaminyl-tRNA synthase
            KO: K09482  glutamyl-tRNA(Gln) amidotransferase subunit D
GENES       OSA: 4333591 4337177
            CME: CMM318C
            PIC: PICST_52015(PET112)
            CGR: CAGL0A04653g CAGL0M13585g
            ANI: AN9400.2
            AFM: AFUA_3G04130
            TAN: TA11065
            YPE: YPO3261
            YPK: y0928
            YPM: YP_0671(gatA)
            YPA: YPA_2752
            YPN: YPN_0835
            YPS: YPTB0862
            ECA: ECA3499
            PLU: plu2200
            XCC: XCC0292(gatA)
            XCB: XC_0302
            XCV: XCV1030
            XAC: XAC0306(gatA)
            PAE: PA4482(gatC) PA4483(gatA) PA4484(gatB)
            PAU: PA14_58170(gatC) PA14_58180(gatA) PA14_58190(gatB)
            PPU: PP_0930(gatB) PP_0931(gatA) PP_0932(gatC)
            PST: PSPTO_4473(gatC) PSPTO_4474(gatA) PSPTO_4475(gatB)
            PSB: Psyr_4164 Psyr_4165 Psyr_4166
            PSP: PSPPH_4173(gatC) PSPPH_4174(gatA) PSPPH_4175(gatB)
            PFL: PFL_0893(gatB) PFL_0894(gatA) PFL_0895(gatC)
            PFO: Pfl_0835 Pfl_0836 Pfl_0837
            PEN: PSEEN1071(gatB) PSEEN1072(gatA) PSEEN1073(gatC)
            PAR: Psyc_0480(gatB) Psyc_0481(gatA) Psyc_0482(gatC)
            PCR: Pcryo_0475 Pcryo_0476 Pcryo_0477
            ACI: ACIAD0822(gatB) ACIAD0823(gatA) ACIAD0824(gatC)
            ILO: IL1971(gatA)
            PHA: PSHAa0910
            PAT: Patl_3426
            SDE: Sde_1128 Sde_3193 Sde_3194 Sde_3195
            CBU: CBU_1473(gatC) CBU_1474(gatA) CBU_1475(gatB)
            LPN: lpg1735(gatC) lpg1736(gatA) lpg1737(gatB)
            LPF: lpl1699(gatC) lpl1700(gatA) lpl1701(gatB)
            LPP: lpp1700(gatC) lpp1701(gatA) lpp1702(gatB)
            MCA: MCA0097(gatB) MCA0098(gatA) MCA0099(gatC)
            FTU: FTT0019(gatC) FTT0020(gatA) FTT0021(gatB)
            FTF: FTF0019(gatC) FTF0020(gatA) FTF0021(gatB)
            FTW: FTW_0093(gatC) FTW_0094 FTW_0095
            FTL: FTL_1841 FTL_1842 FTL_1843
            FTH: FTH_1776(gatB) FTH_1777(gatA) FTH_1778(gatC)
            FTN: FTN_1689(gatB) FTN_1690(gatA) FTN_1691(gatC)
            TCX: Tcr_1627 Tcr_1628 Tcr_1629
            NOC: Noc_2014 Noc_2635 Noc_2636
            AEH: Mlg_0166 Mlg_0167 Mlg_0168
            HCH: HCH_05336(gatC) HCH_05337(gatA) HCH_05338(gatB)
            CSA: Csal_0152 Csal_2241 Csal_2242 Csal_2243
            ABO: ABO_0527(gatB) ABO_0528(gatA) ABO_0529(gatC)
            CRP: CRP_042 CRP_043
            RMA: Rmag_0343 Rmag_0344 Rmag_0345
            NME: NMB1355 NMB1356 NMB1358
            NMA: NMA1567(gatC) NMA1568(gatA) NMA1570(gatB)
            NGO: NGO0660 NGO0662 NGO0663
            CVI: CV_4354(gatB) CV_4355(gatA) CV_4356(gatC)
            RSO: RSc0054(gatB) RSc0057(gatA) RSc0058(gatC)
            REU: Reut_A0071 Reut_A0074 Reut_A0075
            REH: H16_A0108(gatB) H16_A0111(gatA1) H16_A0112(gatC)
            RME: Rmet_0046 Rmet_0049 Rmet_0050
            BMA: BMA0163(gatC) BMA0164(gatA) BMA0165(gatB)
            BXE: Bxe_A0952 Bxe_A4395 Bxe_A4396 Bxe_A4397 Bxe_B1367 Bxe_C0428
                 Bxe_C0436
            BUR: Bcep18194_A6458 Bcep18194_A6459 Bcep18194_A6460
            BCN: Bcen_2493 Bcen_2494 Bcen_2495
            BCH: Bcen2424_1022 Bcen2424_3107 Bcen2424_3108 Bcen2424_3109
            BAM: Bamb_0886 Bamb_3162 Bamb_3163 Bamb_3164
            BPS: BPSL0187(gatC) BPSL0188(gatA) BPSL0189(gatB)
            BPM: BURPS1710b_0367(gatC) BURPS1710b_0368(gatA)
                 BURPS1710b_0369(gatB)
            BTE: BTH_I0147(gatC) BTH_I0148(gatA) BTH_I0149
            BPE: BP0371(gatB) BP0372(gatA) BP0373(gatC)
            BPA: BPP4057(gatC) BPP4058(gatA) BPP4059(gatB)
            BBR: BB4530(gatC) BB4531(gatA) BB4532(gatB)
            RFR: Rfer_3924 Rfer_3925 Rfer_3926
            POL: Bpro_0219 Bpro_0220 Bpro_0221
            NEU: NE2071(gatC) NE2072(gatA) NE2073(gatB)
            NET: Neut_1593 Neut_1594 Neut_1595
            NMU: Nmul_A0321 Nmul_A0322 Nmul_A0323
            EBA: ebA3029(gatB) ebA3030(gatA)
            DAR: Daro_0117 Daro_0118 Daro_0120
            TBD: Tbd_0257 Tbd_0258 Tbd_0259
            MFA: Mfla_2488 Mfla_2489 Mfla_2490
            HPY: HP0658(gatB) HP0830(gatA)
            HPJ: jhp0603(gatB) jhp0769(gatA) jhp0909(gatC)
            HPA: HPAG1_0643 HPAG1_0816 HPAG1_0956
            HHE: HH0701(gatA) HH0796(gatB) HH1248(gatC)
            HAC: Hac_0843(gatB) Hac_1060(gatC) Hac_1198(gatA)
            WSU: WS0558(gatC) WS1896(gatA) WS2005(gatB)
            TDN: Tmden_0773 Tmden_1250 Tmden_1333
            CJE: Cj0398(gatC) Cj1059c(gatA) Cj1197c(gatB)
            CJR: CJE0447(gatC) CJE1202(gatA) CJE1331(gatB)
            CFF: CFF8240_0611 CFF8240_0774(gatB) CFF8240_1146(gatC)
            GSU: GSU3380(gatB) GSU3381(gatA) GSU3383(gatC)
            GME: Gmet_0073 Gmet_0075 Gmet_0076
            PCA: Pcar_2167 Pcar_2168 Pcar_2169
            DVU: DVU0808(gatA) DVU0809(gatC) DVU1885(gatB)
            DDE: Dde_1020 Dde_1021 Dde_2615
            LIP: LI0885 LI0886 LI1007(gatB)
            BBA: Bd0058(gatC) Bd0059(gatA) Bd0060(gatB)
            DPS: DP0643 DP0644 DP0714
            ADE: Adeh_4187 Adeh_4188 Adeh_4189
            MXA: MXAN_1462(gatC) MXAN_1463(gatA) MXAN_1464(gatB)
            SAT: SYN_00307 SYN_00308 SYN_00309 SYN_02603 SYN_02604
            SFU: Sfum_1705 Sfum_3366 Sfum_3367 Sfum_3503 Sfum_3504
            RPR: RP151(gatB) RP152(gatA) RP153(gatC)
            RTY: RT0140(gatB) RT0141(gatA) RT0142(gatC)
            RCO: RC0193(gatB) RC0194(gatA) RC0195(gatC)
            RFE: RF_1128(gatC) RF_1129(gatA) RF_1130(gatB)
            RBE: RBE_1133(gatC) RBE_1134(gatA) RBE_1135(gatB)
            OTS: OTBS_1366(gatC) OTBS_1367(gatA) OTBS_1368(gatB)
            WOL: WD0037 WD0146(gatB) WD0505(gatA)
            WBM: Wbm0102 Wbm0704 Wbm0763
            AMA: AM1030 AM426(gatB) AM698(gatA)
            APH: APH_0470(gatB) APH_0748(gatA) APH_1113(gatC)
            ERU: Erum2850(gatB) Erum3601 Erum3670(gatA) Erum7910(gatC)
            ERW: ERWE_CDS_02910(gatB) ERWE_CDS_03780(gatA)
                 ERWE_CDS_08370(gatC)
            ERG: ERGA_CDS_02860(gatB) ERGA_CDS_03730(gatA)
                 ERGA_CDS_08260(gatC)
            ECN: Ecaj_0268 Ecaj_0352 Ecaj_0827
            ECH: ECH_0703(gatA) ECH_0813(gatB) ECH_1025(gatC)
            NSE: NSE_0084(gatB) NSE_0256(gatA)
            PUB: SAR11_1076(gatB) SAR11_1077(gatA) SAR11_1078(gatC)
            MLO: mll0675 mlr0190 msl0677
            MES: Meso_1363 Meso_1365 Meso_1720
            SME: SMc01350(gatB) SMc01352(gatA) SMc01353(gatC)
            ATU: Atu1318(gatC) Atu1319(gatA) Atu1324(gatB)
            ATC: AGR_C_2429 AGR_C_2430 AGR_C_2438
            RET: RHE_CH01854(gatC) RHE_CH01855(gatA2) RHE_CH01862(gatB)
            RLE: RL0225 RL2075(gatC) RL2076(gatA) RL2082(gatB) pRL110427
                 pRL120136 pRL90294
            BME: BMEI1068 BMEII0674 BMEII0675
            BMF: BAB1_0918(gatB) BAB2_0645(gatC) BAB2_0646(gatA)
            BMS: BR0899(gatB) BRA0594(gatA) BRA0595(gatC)
            BMB: BruAb1_0911(gatB) BruAb2_0629(gatC) BruAb2_0630(gatA)
            BJA: bll5087(gatB) bll5089(gatA) bsl5090(gatC)
            RPA: RPA3104(gatB) RPA3107(gatA2) RPA3111(gatC)
            RPB: RPB_2434 RPB_2438 RPB_2440
            RPC: RPC_2260 RPC_2264 RPC_2269
            RPD: RPD_1881 RPD_3014 RPD_3016 RPD_3018 RPD_3802
            RPE: RPE_1796 RPE_3356 RPE_3358 RPE_3362
            NWI: Nwi_1997 Nwi_2001 Nwi_2003
            NHA: Nham_2271 Nham_2275 Nham_2277
            BHE: BH05950(gatB) BH08230(gatC) BH08240(gatA)
            BQU: BQ06340(gatA) BQ06350(gatC) BQ07280(gatB)
            CCR: CC_2436 CC_2437 CC_2438
            SIL: SPO2847(gatB) SPO2969(gatA) SPO2970(gatC)
            SIT: TM1040_0058 TM1040_0327 TM1040_0701 TM1040_1918 TM1040_1919
            RSP: RSP_1986(gatB) RSP_2270(gatA) RSP_6043(gatC)
            JAN: Jann_0426 Jann_1221 Jann_1222 Jann_1866
            RDE: RD1_0035 RD1_2000(gatA) RD1_2001(gatC) RD1_3333(gatB)
            MMR: Mmar10_1702 Mmar10_1706 Mmar10_1707
            HNE: HNE_2291(gatB) HNE_2293(gatA) HNE_2299(gatC)
            ZMO: ZMO0782(gatB) ZMO0783(gatA) ZMO0784(gatC)
            NAR: Saro_2831 Saro_2832 Saro_2833
            SAL: Sala_0840 Sala_0841 Sala_0842
            ELI: ELI_01365 ELI_01375 ELI_01390
            GOX: GOX2382 GOX2383 GOX2384
            GBE: GbCGDNIH1_0950 GbCGDNIH1_0952 GbCGDNIH1_0953
            RRU: Rru_A3175 Rru_A3176 Rru_A3177
            MAG: amb1584 amb1585
            MGM: Mmc1_0681 Mmc1_0682 Mmc1_0683
            ABA: Acid345_0499 Acid345_0501 Acid345_4716
            SUS: Acid_1073 Acid_1074 Acid_7720
            BSU: BG12838(gatC) BG12839(gatA) BG12840(gatB)
            BHA: BH0665 BH0666 BH0667
            BAN: BA0320(gatC) BA0321(gatA) BA0322(gatB)
            BAR: GBAA0320(gatC) GBAA0321(gatA) GBAA0322(gatB)
            BAA: BA_0890 BA_0891 BA_0892
            BAT: BAS0305 BAS0306 BAS0307
            BCE: BC0350 BC0351 BC0352
            BCA: BCE_0349(gatC) BCE_0350(gatA) BCE_0351(gatB)
            BCZ: BCZK0291(gatC) BCZK0292(gatA) BCZK0293(gatB) BCZK1739(gatA)
                 BCZK1877(gatA)
            BTK: BT9727_0288(gatC) BT9727_0289(gatA) BT9727_0290(gatB)
                 BT9727_1761(gatA) BT9727_1887(gatA)
            BTL: BALH_0312(gatC) BALH_0313(gatA) BALH_0314(gatB)
            BLI: BL00600(gatC) BL00601(gatA) BL00602(gatB)
            BLD: BLi00730(gatC) BLi00731(gatA) BLi00732(gatB)
            BCL: ABC1096(gatC) ABC1097(gatA) ABC1098(gatB)
            OIH: OB0764 OB0765 OB0766
            GKA: GK0281 GK0282 GK0283
            SAU: SA1715 SA1716 SA1717
            SAV: SAV1899 SAV1900 SAV1901
            SAM: MW1840 MW1841 MW1842
            SAR: SAR1991(gatB) SAR1992(gatA) SAR1993(gatC)
            SAS: SAS1822 SAS1823 SAS1824
            SAC: SACOL1960(gatB) SACOL1961(gatA) SACOL1962(gatC)
            SAB: SAB1832c(gatB) SAB1833c(gatA) SAB1834c(gatC)
            SAA: SAUSA300_1880(gatB) SAUSA300_1881(gatA) SAUSA300_1882(gatC)
            SAO: SAOUHSC_02116 SAOUHSC_02117 SAOUHSC_02118
            SEP: SE1584 SE1585 SE1586
            SER: SERP1437(gatB) SERP1438(gatA) SERP1439(gatC)
            SHA: SH1051(gatC) SH1052(gatA) SH1053(gatB)
            SSP: SSP0890 SSP0891 SSP0892
            LMO: lmo1754(gatB) lmo1755(gatA) lmo1756(gatC)
            LMF: LMOf2365_1779(gatB) LMOf2365_1780(gatA) LMOf2365_1781(gatC)
            LIN: lin1866(gatB) lin1867(gatA) lin1868(gatC)
            LWE: lwe1771(gatB) lwe1772(gatA) lwe1773(gatC)
            LLA: L0473(gatA) L0474(gatB) L0475(gatC)
            LLC: LACR_0169 LACR_0170 LACR_0171
            LLM: llmg_0174(gatC) llmg_0175(gatA) llmg_0176(gatB)
            SPY: SPy_1770(gatB) SPy_1771(gatA) SPy_1772(gatC)
            SPZ: M5005_Spy_1506(gatB) M5005_Spy_1507(gatA)
                 M5005_Spy_1508(gatC)
            SPM: spyM18_1839(gatB) spyM18_1840(gatA) spyM18_1841(gatC)
            SPG: SpyM3_1539(gatB) SpyM3_1540(gatA) SpyM3_1541(gatC)
            SPS: SPs0325 SPs0326 SPs0327
            SPH: MGAS10270_Spy1574(gatB) MGAS10270_Spy1575(gatA)
                 MGAS10270_Spy1576(gatC)
            SPI: MGAS10750_Spy1566(gatB) MGAS10750_Spy1567(gatA)
                 MGAS10750_Spy1568(gatC)
            SPJ: MGAS2096_Spy1534(gatB) MGAS2096_Spy1535(gatA)
                 MGAS2096_Spy1536(gatC)
            SPK: MGAS9429_Spy1508(gatB) MGAS9429_Spy1509(gatA)
                 MGAS9429_Spy1510(gatC)
            SPF: SpyM50337(gatC) SpyM50338(gatA)
            SPA: M6_Spy1500 M6_Spy1501 M6_Spy1502
            SPB: M28_Spy1495(gatB) M28_Spy1496(gatA) M28_Spy1497(gatC)
            SPN: SP_0436 SP_0437 SP_0438
            SPR: spr0393(gatB) spr0394(gatA) spr0395(gatC)
            SPD: SPD_0396(gatB) SPD_0397(gatA) SPD_0398(gatC)
            SAG: SAG1667(gatB) SAG1668(gatA) SAG1669(gatC)
            SAN: gbs1711 gbs1712 gbs1713
            SAK: SAK_1679(gatB) SAK_1680(gatA) SAK_1681(gatC)
            SMU: SMU.1819(gatB) SMU.1820c SMU.1821c
            STC: str1625(gatB) str1626(gatA) str1627(gatC)
            STL: stu1625(gatB) stu1626(gatA) stu1627(gatC)
            STE: STER_1590 STER_1591 STER_1592
            SSA: SSA_0569(gatC) SSA_0570(gatA) SSA_0571(gatB)
            SSU: SSU05_0355 SSU05_0356
            SSV: SSU98_0346 SSU98_0347
            LPL: lp_1147(gatC) lp_1148(gatA) lp_1149(gatB)
            LJO: LJ1716 LJ1717 LJ1718
            LAC: LBA0531(gatC) LBA0532(gatA) LBA0533(gatB)
            LSA: LSA1546(gatB) LSA1547(gatA) LSA1548(gatC)
            LSL: LSL_1344(gatB) LSL_1345(gatA) LSL_1346(gatC)
            LDB: Ldb0468(gatC) Ldb0469(gatA) Ldb0470(gatB)
            LBU: LBUL_0416 LBUL_0417 LBUL_0418
            LBR: LVIS_1629 LVIS_1630 LVIS_1631
            LCA: LSEI_1057 LSEI_1058 LSEI_1059
            LGA: LGAS_1511 LGAS_1512 LGAS_1513
            PPE: PEPE_1368 PEPE_1369 PEPE_1370
            EFA: EF0724(gatC) EF0725(gatA) EF0726(gatB)
            OOE: OEOE_1693 OEOE_1694 OEOE_1695
            LME: LEUM_1579 LEUM_1580 LEUM_1581
            STH: STH2820 STH2821 STH2822
            CAC: CAC2669 CAC2670 CAC2671
            CTC: CTC02392 CTC02393
            CNO: NT01CX_0430(gatB) NT01CX_0431(gatA) NT01CX_0432(gatC)
            CHY: CHY_1101(gatC) CHY_1102(gatA) CHY_1103(gatB)
            DSY: DSY3885 DSY3886 DSY3887 DSY4734
            SWO: Swol_0372 Swol_0373 Swol_0374
            TTE: TTE0606(gatC) TTE0607(gatA) TTE0608(gatB)
            MTA: Moth_2008 Moth_2009 Moth_2010
            MGE: MG_099 MG_100
            MPN: MPN237(gatA) MPN238(PET112)
            MPU: MYPU_2000(gatA) MYPU_2010
            MPE: MYPE2090 MYPE2100(gatA) MYPE2110(gatB)
            MGA: MGA_0412(gatB) MGA_0413(gatA)
            MMY: MSC_0761(gatB) MSC_0762(gatA) MSC_0763(gatC)
            MMO: MMOB3760(gatB) MMOB3770(gatA)
            MHY: mhp029(gatA) mhp030(gatB)
            MHJ: MHJ_0024(gatA) MHJ_0025(gatB)
            MHP: MHP7448_0028(gatA) MHP7448_0029(gatB)
            MSY: MS53_0091(gatB) MS53_0092(gatA) MS53_0093(gatC)
            MCP: MCAP_0709(gatB) MCAP_0710(gatA) MCAP_0711(gatC)
            UUR: UU544(gatB) UU545(gatA)
            MFL: Mfl162 Mfl163
            MTU: Rv3009c Rv3011c(gatA) Rv3012c
            MTC: MT3089(gatB) MT3091(gatA) MT3092(gatC)
            MBO: Mb3034c(gatB) Mb3036c(gatA) Mb3037c(gatC)
            MLE: ML1700(gatB) ML1702(gatA) ML1703(gatC)
            MPA: MAP3042c(gatB) MAP3045c(gatA) MAP3046c(gatC)
            MAV: MAV_3856 MAV_3859 MAV_3860(gatC)
            MSM: MSMEG_1088(gatA) MSMEG_2364(gatC) MSMEG_2365 MSMEG_2367
            MUL: MUL_1939(gatA)
            MMC: Mmcs_1890 Mmcs_1891 Mmcs_1894
            CGL: NCgl1198(gatC) NCgl1199(cgl1247) NCgl1211(cgl1259)
            CGB: cg1403(gatC) cg1404(gatA) cg1420(gatB)
            CEF: CE1344 CE1345 CE1351
            CDI: DIP1079(gatC) DIP1080(gatA) DIP1089(gatB)
            CJK: jk1306(gatB) jk1311(gatA)
            NFA: nfa42380(gatB) nfa42580(gatA) nfa42590(gatC)
            RHA: RHA1_ro06473(gatC) RHA1_ro06474(gatA) RHA1_ro06480
            SCO: SCO5498(gatC) SCO5499(gatA) SCO5501(gatB)
            SMA: SAV2743(gatB) SAV2745(gatA) SAV2746(gatC)
            TWH: TWT411(gatB) TWT412(gatA) TWT413(gatC)
            TWS: TW355(gatC) TW356(gatA) TW357(gatB)
            LXX: Lxx14340(gatB) Lxx14350(gatA) Lxx14360(gatC)
            ART: Arth_1306 Arth_1307 Arth_1308
            PAC: PPA1122 PPA1123 PPA1124
            TFU: Tfu_0605 Tfu_0606 Tfu_0609
            FRA: Francci3_3642 Francci3_3644 Francci3_3645
            FAL: FRAAL5853(gatB) FRAAL5855(gatA) FRAAL5856(gatC)
            ACE: Acel_0696 Acel_0697 Acel_0698
            SEN: SACE_4290(gatA)
            BLO: BL0402(gatB) BL0403(gatA) BL0404(gatC)
            BAD: BAD_1457(gatB) BAD_1458(gatA) BAD_1459(gatC)
            RXY: Rxyl_0829 Rxyl_0830 Rxyl_0834
            FNU: FN0753 FN0754 FN0755
            RBA: RB10852(gatB) RB4143(gatA) RB8359(gatC)
            CTR: CT002(gatC) CT003(gatA) CT004(gatB)
            CTA: CTA_0003(gatC) CTA_0004(gatA) CTA_0005(gatB)
            CMU: TC0270 TC0271 TC0272
            CPN: CPn0002(gatC) CPn0003(gatA) CPn0004(gatB)
            CPA: CP0771 CP0772 CP0773
            CPJ: CPj0002(gatC) CPj0003(gatA) CPj0004(gatB)
            CPT: CpB0003 CpB0004 CpB0005
            CCA: CCA00287(gatC) CCA00289(gatB)
            CAB: CAB285(gatC) CAB286(gatA) CAB287(gatB)
            CFE: CF0714(gatB) CF0715(gatA) CF0716(gatC)
            PCU: pc0669(gatB) pc0670(gatA) pc0671(gatC)
            BBU: BB0341(gatB) BB0342(gluA)
            BGA: BG0342(gatB) BG0343(gatA)
            BAF: BAPKO_0350(gatB) BAPKO_0351(gatA)
            TPA: TP1020 TP1021
            TDE: TDE0575(gatB) TDE0576(gatA) TDE0577(gatC)
            LIL: LA0256(gatB) LA2507(gatA) LA2508(gatC)
            LIC: LIC10221(gatB) LIC11460(gatC) LIC11461(gatA)
            LBJ: LBJ_1660 LBJ_1661(gatC) LBJ_2784(gatB)
            LBL: LBL_0287(gatB) LBL_1879 LBL_1880(gatC)
            SYN: sll1435(pet112) slr0033 slr0877
            SYW: SYNW0292(gatC) SYNW1031(gatA) SYNW2356(gatB)
            SYC: syc1386_c(pet112) syc1780_c(gatC) syc1975_d(gatA)
            SYF: Synpcc7942_0118 Synpcc7942_2117 Synpcc7942_2322
            SYD: Syncc9605_0287 Syncc9605_1157 Syncc9605_2497
            SYE: Syncc9902_1302 Syncc9902_2057 Syncc9902_2169
            SYG: sync_0337(gatC) sync_1631(gatA) sync_2739(gatB)
            CYA: CYA_0359(gatB) CYA_1343(gatC) CYA_1419(gatA)
            CYB: CYB_0708(gatB) CYB_1605(gatA) CYB_2217(gatC)
            TEL: tll1003 tlr2394 tsl1524
            GVI: gll1528 gll2342 gsl3282
            ANA: all1053 alr1396 asl3192
            AVA: Ava_3747 Ava_3890 Ava_3952
            PMA: Pro0052(gatB) Pro0265(gatC) Pro0750(gatA)
            PMM: PMM0048(gatB) PMM0235(gatC) PMM0946(gatA)
            PMT: PMT0648(gatA) PMT1815(gatC) PMT2139(gatB)
            PMN: PMN2A_0264 PMN2A_1381 PMN2A_1602
            PMI: PMT9312_0049 PMT9312_0237 PMT9312_0853
            PMB: A9601_00491(gatB) A9601_02561(gatC) A9601_09141(gatA)
            PMC: P9515_00551(gatB) P9515_02671(gatC) P9515_10291(gatA)
            PMF: P9303_15821(gatA) P9303_24311(gatC) P9303_28281(gatB)
            PMG: P9301_00511(gatB) P9301_02571(gatC) P9301_09121(gatA)
            PME: NATL1_00621(gatB) NATL1_03141(gatC) NATL1_09331(gatA)
            TER: Tery_2065 Tery_3843 Tery_4579
            SRU: SRU_0671 SRU_1282(gatC) SRU_1902
            CHU: CHU_0025(gatA) CHU_1447(gatB) CHU_2829(gatC)
            CTE: CT0268(gatA) CT1833(gatC) CT2215(gatB)
            CCH: Cag_0318 Cag_0465 Cag_1873
            PLT: Plut_0163 Plut_0337 Plut_1749
            DET: DET1334(gatC) DET1335(gatA) DET1550(gatB)
            DEH: cbdb_A1282(gatC) cbdb_A1284(gatA) cbdb_A1643(gatB)
            DRA: DR_1275 DR_1856 DR_2555
            DGE: Dgeo_0414 Dgeo_0760 Dgeo_0933
            TTH: TTC0205 TTC0521 TTC1620
            TTJ: TTHA0366 TTHA0573 TTHA0876
            AAE: aq_2147a(gatC) aq_247(gatA) aq_461(gatB)
            TMA: TM0252 TM1272 TM1273
            MJA: MJ0019 MJ0020 MJ0160 MJ0243 MJ1160
            MMP: MMP0946 MMP1265 MMP1266 MMP1510
            MAC: MA1317(ansA) MA2862 MA4522(gatC) MA4523(gatA) MA4524(gatB)
            MBA: Mbar_A0003 Mbar_A0882 Mbar_A0883 Mbar_A0884 Mbar_A2389
            MMA: MM_0050 MM_1226 MM_1227 MM_1228 MM_2306
            MBU: Mbur_0391 Mbur_1026 Mbur_1654 Mbur_1655 Mbur_1656
            MTP: Mthe_0022 Mthe_0176 Mthe_0177 Mthe_0178 Mthe_1002
            MHU: Mhun_0082 Mhun_0083 Mhun_1012 Mhun_1013 Mhun_1014
            MTH: MTH1280 MTH1496 MTH706 MTH707
            MST: Msp_0181(gatA) Msp_0269(gatB) Msp_1411(gatD) Msp_1412(gatE)
            MKA: MK0129(gatE) MK0238(gatA) MK0960(gatB) MK1509(ansB)
            AFU: AF0882(asnA) AF1440(gatB-1) AF2116(gatB-2) AF2328(gatC)
                 AF2329(gatA-2)
            HAL: VNG0345G(gatB2) VNG0870G(gatC) VNG0872G(gatA) VNG1352G(gatB1)
                 VNG1844G(ansA)
            HMA: rrnAC0023(gatE) rrnAC1355(gatA1) rrnAC1356(gatC)
                 rrnAC1642(gatB) rrnAC3442(asbA)
            HWA: HQ1266A(aatB) HQ1687A(aatA) HQ1688A(aatC) HQ2468A(gatE)
                 HQ2776A(gatD)
            NPH: NP1220A(aatB) NP1454A(aatC) NP1456A(aatA) NP2492A(gatD)
                 NP3774A(gatE)
            TAC: Ta0971 Ta0972
            TVO: TVN1117 TVN1118
            PTO: PTO1397 PTO1398
            PHO: PH1463 PH1464
            PAB: PAB1901(asnA) PAB1902(gatB)
            PFU: PF1461 PF1462
            TKO: TK0908 TK0911
            SSO: SSO0232(gatB-1) SSO0936(gatB-2) SSO0938(ansA) SSO0957(gatA-2)
                 SSO6855(gatC)
            STO: ST0282 ST1262 ST1264 ST1283 STS140
            SAI: Saci_0700(gatB) Saci_1329(gatC) Saci_1330(gatA)
                 Saci_1349(gatD) Saci_1350
            PAI: PAE1003(asnA) PAE1525(gatA) PAE3222(gatB)
            NEQ: NEQ126 NEQ185 NEQ245 NEQ360
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.5.7
            ExPASy - ENZYME nomenclature database: 6.3.5.7
            ExplorEnz - The Enzyme Database: 6.3.5.7
            ERGO genome analysis and discovery system: 6.3.5.7
            BRENDA, the Enzyme Database: 6.3.5.7
            CAS: 52232-48-1
///
ENTRY       EC 6.3.5.8        Obsolete  Enzyme
NAME        Transferred to 2.6.1.85
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Carbon-nitrogen ligases with glutamine as amido-N-donor
COMMENT     Transferred entry: Now EC 2.6.1.85, aminodeoxychorismate synthase.
            As ATP is not hydrolysed during the reaction, the classification of
            the enzyme as a ligase was incorrect. (EC 6.3.5.8 created 2003,
            deleted 2007)
GENES       REU: Reut_A2783
            BUR: Bcep18194_A3841
            HAR: HEAR2983
            DVU: DVU0364(pabA)
            DDE: Dde_3617 Dde_3618
            DPS: DP1620
            SFU: Sfum_1775
            RPD: RPD_2897
            NWI: Nwi_0951
            NHA: Nham_1044
            MGM: Mmc1_0427
            BSU: BG10138(pabA)
            BHA: BH0091(pabA)
            BAN: BA0069(pabA-1)
            BAR: GBAA0069(pabA-1)
            BAA: BA_0659
            BAT: BAS0069
            BCE: BC0077
            BCA: BCE_0068(pabA)
            BCZ: BCZK0065(pabA)
            BTK: BT9727_0065(pabA)
            BTL: BALH_0068(pabA)
            BLI: BL00859(pabA)
            BLD: BLi00091(pabA)
            BCL: ABC0111(pabA)
            GKA: GK0067
            LLC: LACR_C06
            SPY: SPy_1990(pabB)
            SPH: MGAS10270_Spy1766(trpG)
            SPI: MGAS10750_Spy1790(trpG)
            SPJ: MGAS2096_Spy1725(trpG)
            SPK: MGAS9429_Spy1703(trpG)
            SSA: SSA_0413(pabB)
            CPE: CPE1016(pabA)
            CPF: CPF_1271(pabA)
            CPR: CPR_1093(pabA)
            CHY: CHY_1586(trpG) CHY_1931(pabA)
            MTA: Moth_1341
            MTU: Rv0013(trpG) Rv1005c(pabB)
            MTC: MT0016 MT1034
            MBO: Mb0013(trpG) Mb1032c(pabB)
            MLE: ML0015(pabA) ML0236(pabB)
            MPA: MAP0015(pabA) MAP0945c(pabB)
            MMC: Mmcs_0014
            CGL: NCgl0955(cgl0997)
            CGB: cg1134(pabAB)
            CEF: CE1059
            CJK: jk0031(pabB) jk0036(pabA)
            NFA: nfa16010(pabB) nfa770(pabA)
            RHA: RHA1_ro06665
            SCO: SCO3851(SCH69.21c)
            SMA: SAV1178(pabAB) SAV4335(pabA)
            TWH: TWT011(pabA)
            TWS: TW011
            LXX: Lxx00200(trpG)
            TFU: Tfu_1666
            FRA: Francci3_4437
            FAL: FRAAL6756(pabA)
            ACE: Acel_0018
            SEN: SACE_4036(pabAB)
            BLO: BL0590(pabA)
            BAD: BAD_0037(pabA)
            FNU: FN1730 FN1731
            RBA: RB6753(pabB)
            PCU: pc0367(pabA) pc1327(pabB)
            SYW: SYNW2315(pabA) SYNW2432
            SYC: syc0220_c(trpE)
            SYD: Syncc9605_2446 Syncc9605_2603
            SYE: Syncc9902_2128 Syncc9902_2239
            SYG: sync_2663
            ANA: alr3443
            AVA: Ava_3468
            PMA: Pro0209(pabA) Pro1856(trpE)
            PMM: PMM0184(pabA) PMM1692
            PMT: PMT2067(pabA) PMT2223
            PMN: PMN2A_1294
            PMI: PMT9312_0186
            PMB: A9601_02021(pabA) A9601_17841
            PMC: P9515_02131(pabA) P9515_17641
            PMF: P9303_22721 P9303_27421(pabA)
            PMG: P9301_02041(pabA) P9301_17681
            PME: NATL1_02601(pabA) NATL1_20231
            BTH: BT_0767
            BFR: BF2239
            BFS: BF2335
            SRU: SRU_1665
            CHU: CHU_1808(pabB)
            FPS: FP0512(pabA)
            AAE: aq_1144(pabB)
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.5.8
            ExPASy - ENZYME nomenclature database: 6.3.5.8
            ExplorEnz - The Enzyme Database: 6.3.5.8
            ERGO genome analysis and discovery system: 6.3.5.8
            BRENDA, the Enzyme Database: 6.3.5.8
///
ENTRY       EC 6.3.5.9                  Enzyme
NAME        hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing);
            CobB
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Carbon-nitrogen ligases with glutamine as amido-N-donor
SYSNAME     hydrogenobyrinic-acid:L-glutamine amido-ligase (AMP-forming)
REACTION    2 ATP + hydrogenobyrinic acid + 2 L-glutamine + 2 H2O = 2 ADP + 2
            phosphate + hydrogenobyrinic acid a,c-diamide + 2 L-glutamate
            [RN:R05224]
ALL_REAC    R05224
SUBSTRATE   ATP [CPD:C00002];
            hydrogenobyrinic acid [CPD:C06399];
            L-glutamine [CPD:C00064];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            hydrogenobyrinic acid a,c-diamide [CPD:C06503];
            L-glutamate [CPD:C00025]
COMMENT     This step in the aerobic biosynthesis of cobalamin generates
            hydrogenobyrinic acid a,c-diamide, the substrate required by EC
            6.6.1.2, cobaltochelatase, which adds cobalt to the macrocycle.
REFERENCE   1  [PMID:2172209]
  AUTHORS   Debussche L, Thibaut D, Cameron B, Crouzet J, Blanche F.
  TITLE     Purification and characterization of cobyrinic acid a,c-diamide
            synthase from Pseudomonas denitrificans.
  JOURNAL   J. Bacteriol. 172 (1990) 6239-44.
  ORGANISM  Pseudomonas denitrificans
REFERENCE   2  [PMID:12195810]
  AUTHORS   Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
  TITLE     The biosynthesis of adenosylcobalamin (vitamin B12).
  JOURNAL   Nat. Prod. Rep. 19 (2002) 390-412.
  ORGANISM  Pseudomonas denitrificans
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K02224  hydrogenobyrinic acid a,c-diamide synthase
GENES       XCC: XCC3063(cobB)
            XCB: XC_1095
            PAE: PA1273(cobB)
            PAU: PA14_47760(cobB)
            PPU: PP_1673(cobB)
            PST: PSPTO_1709
            PSB: Psyr_3680
            PSP: PSPPH_3701
            PFL: PFL_4430(cobB)
            PFO: Pfl_1642
            PEN: PSEEN1379
            CPS: CPS_1147(cobB)
            MCA: MCA2290(cobB)
            AEH: Mlg_1666 Mlg_2813
            CVI: CV_1556(cobB)
            RSO: RSp0615(cobB)
            RME: Rmet_3938
            BMA: BMA1176(cobB)
            BXE: Bxe_B1656
            BUR: Bcep18194_A4799
            BCN: Bcen_1171
            BCH: Bcen2424_1651
            BAM: Bamb_1551
            BPS: BPSL1773(cobB)
            BPM: BURPS1710b_2093(cobB)
            BTE: BTH_I2412
            RFR: Rfer_2624
            POL: Bpro_2785
            MPT: Mpe_B0437(cobB) Mpe_B0472(cobB) Mpe_B0510(cobB)
            EBA: ebA4027(cobB)
            DAR: Daro_4034
            TBD: Tbd_2473(cbiA)
            MFA: Mfla_0119
            GME: Gmet_0470
            PCA: Pcar_0481
            DVU: DVU3086(cobB-2)
            DDE: Dde_0343
            DPS: DP0218(cobB)
            SFU: Sfum_1740
            MLO: mlr1387
            SME: SMc04282(cobB)
            ATU: Atu2793(cobB)
            ATC: AGR_C_5069
            RET: RHE_CH02483(cobB)
            RLE: RL2823(cobB)
            BME: BMEI0705
            BMF: BAB1_1316
            BMS: BR1296(cobB)
            BMB: BruAb1_1297(cobB)
            BJA: blr3272(cobB)
            BRA: BRADO4897(cobB)
            BBT: BBta_3154(cobB)
            RPA: RPA2083(cobB)
            RPB: RPB_3185
            RPC: RPC_1881
            RPD: RPD_2313
            RPE: RPE_2218
            SIL: SPO2872(cobB)
            SIT: TM1040_2219
            RSP: RSP_3185(cobB)
            RDE: RD1_3818(cobB)
            NAR: Saro_0333
            GBE: GbCGDNIH1_0667
            RRU: Rru_A3359
            MGM: Mmc1_1703 Mmc1_3137
            BHA: BH1898
            GKA: GK1796
            CHY: CHY_0771(cobB1)
            DSY: DSY4060(cobB)
            MTA: Moth_1100
            MTU: Rv2848c(cobB)
            MTC: MT2914(cobB)
            MBO: Mb2873c(cobB)
            MPA: MAP2917c(cobB)
            MSM: MSMEG_2617(cobB)
            MMC: Mmcs_2073
            CDI: DIP1488
            NFA: nfa40810(cobB)
            SCO: SCO1852(cobB)
            SMA: SAV6412(cobB)
            TFU: Tfu_0311(cbiA)
            FRA: Francci3_2297
            FAL: FRAAL3729(cobB)
            SEN: SACE_5963(cobB)
            RXY: Rxyl_0638
            LIL: LB154(cbiA)
            LIC: LIC20124(cobB)
            LBJ: LBJ_4188(cobB)
            LBL: LBL_4203(cobB)
            SYW: SYNW0748(cbiA)
            SYC: syc2239_c(cobB)
            SYF: Synpcc7942_1855
            SYD: Syncc9605_1920
            SYE: Syncc9902_0746
            SYG: sync_1000(cobB)
            SYR: SynRCC307_0757(cobB)
            SYX: SynWH7803_1563(cobB)
            TEL: tlr1848(cobB)
            ANA: alr3934
            AVA: Ava_1768
            PMA: Pro1126(cobB)
            PMM: PMM1072(cbiA)
            PMT: PMT1104(cbiA)
            PMN: PMN2A_0678(cbiA)
            PMI: PMT9312_1083
            PMB: A9601_11771(cobB)
            PMC: P9515_11621(cobB)
            PMF: P9303_09381(cobB)
            PMG: P9301_11781(cobB)
            PME: NATL1_15121(cobB)
            TER: Tery_0517
            DET: DET0128(cobB)
            DEH: cbdb_A149(cobB)
            DRA: DR_B0009
            DGE: Dgeo_2349
            TTH: TT_P0001
            TTJ: TTHB043
            RCI: RCIX2001(cbiA-1) RCIX825(cbiA-2)
            SSO: SSO0404
            STO: ST0389
            SAI: Saci_0825
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.5.9
            ExPASy - ENZYME nomenclature database: 6.3.5.9
            ExplorEnz - The Enzyme Database: 6.3.5.9
            ERGO genome analysis and discovery system: 6.3.5.9
            BRENDA, the Enzyme Database: 6.3.5.9
            CAS: 132053-22-6
///
ENTRY       EC 6.3.5.10                 Enzyme
NAME        adenosylcobyric acid synthase (glutamine-hydrolysing);
            CobQ;
            cobyric acid synthase;
            5'-deoxy-5'-adenosylcobyrinic-acid-a,c-diamide:L-glutamine
            amido-ligase;
            Ado-cobyric acid synthase [glutamine hydrolyzing]
CLASS       Ligases;
            Forming carbon-nitrogen bonds;
            Carbon-nitrogen ligases with glutamine as amido-N-donor
SYSNAME     adenosylcobyrinic-acid-a,c-diamide:L-glutamine amido-ligase
            (ADP-forming)
REACTION    4 ATP + adenosylcobyrinic acid a,c-diamide + 4 L-glutamine + 4 H2O =
            4 ADP + 4 phosphate + adenosylcobyric acid + 4 L-glutamate
            [RN:R05225]
ALL_REAC    R05225
SUBSTRATE   ATP [CPD:C00002];
            adenosylcobyrinic acid a,c-diamide [CPD:C06506];
            L-glutamine [CPD:C00064];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            adenosylcobyric acid [CPD:C06507];
            L-glutamate [CPD:C00025]
COMMENT     Requires Mg2+. NH3 can act instead of glutamine. This enzyme
            catalyses the four-step amidation sequence from cobyrinic acid
            a,c-diamide to cobyric acid via the formation of cobyrinic acid
            triamide, tetraamide and pentaamide intermediates.
REFERENCE   1  [PMID:1917839]
  AUTHORS   Blanche F, Couder M, Debussche L, Thibaut D, Cameron B, Crouzet J.
  TITLE     Biosynthesis of vitamin B12: stepwise amidation of carboxyl groups
            b, d, e, and g of cobyrinic acid a,c-diamide is catalyzed by one
            enzyme in Pseudomonas denitrificans.
  JOURNAL   J. Bacteriol. 173 (1991) 6046-51.
  ORGANISM  Pseudomonas denitrificans
REFERENCE   2  [PMID:12195810]
  AUTHORS   Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
  TITLE     The biosynthesis of adenosylcobalamin (vitamin B12).
  JOURNAL   Nat. Prod. Rep. 19 (2002) 390-412.
  ORGANISM  Pseudomonas denitrificans
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K02232  adenosylcobyric acid synthase
GENES       STY: STY2222(cbiP)
            STT: t0855(cbiP)
            SPT: SPA0852(cbiP)
            SEC: SC2027(cbiP)
            STM: STM2019(cbiP)
            PLU: plu2987(cbiP)
            XCC: XCC3061
            XCB: XC_1097
            XCV: XCV3317(cobQ)
            XAC: XAC3188(cobQ)
            VCH: VCA0727
            VVU: VV2_0330
            VVY: VVA0824
            VPA: VPA0932
            VFI: VFA0289
            PPR: PBPRB0991
            PAE: PA1277(cobQ)
            PAU: PA14_47690(cobQ)
            PAP: PSPA7_4113(cobQ)
            PPU: PP_1677(cobQ)
            PST: PSPTO_1713(cobQ)
            PSB: Psyr_3676(cobQ)
            PSP: PSPPH_3697(cobQ)
            PFL: PFL_4426(cobQ)
            PFO: Pfl_1646(cobQ)
            PEN: PSEEN1383
            ACI: ACIAD1071(cobQ)
            SON: SO_1038(cobQ)
            SFR: Sfri_0879
            SHE: Shewmr4_0845
            SHM: Shewmr7_3177
            SHN: Shewana3_3275
            CPS: CPS_3655(cobQ)
            PHA: PSHAa2564(cobQ)
            PAT: Patl_1135
            SDE: Sde_0240
            MCA: MCA2304(cobQ)
            AEH: Mlg_2812
            HCH: HCH_00962(cobQ)
            ABO: ABO_2365(cobQ)
            CVI: CV_1576(cobQ)
            RSO: RSc2390(cobQ)
            REU: Reut_A0665(cobQ)
            REH: H16_A2961(cbiP)
            RME: Rmet_2778
            BMA: BMA0697(cobQ)
            BMV: BMASAVP1_A2316(cobQ)
            BML: BMA10299_A2971(cobQ)
            BMN: BMA10247_1628(cobQ)
            BXE: Bxe_A3492
            BUR: Bcep18194_A5777(cobQ)
            BCN: Bcen_1835
            BAM: Bamb_2494
            BPS: BPSL0987(cobQ)
            BPM: BURPS1710b_1200(cobQ)
            BPL: BURPS1106A_1045(cobQ)
            BPD: BURPS668_1039(cobQ)
            BTE: BTH_I0844(cobQ)
            RFR: Rfer_2612
            POL: Bpro_2760
            MPT: Mpe_A2304(copQ) Mpe_B0518(cobQ)
            EBA: ebA3690(cobQ)
            DAR: Daro_0144(cobQ)
            TBD: Tbd_2714(cobQ)
            MFA: Mfla_0103
            GSU: GSU2992(cobQ)
            GME: Gmet_0485
            PCA: Pcar_0484(cobD)
            DVU: DVU0816(cobQ)
            DDE: Dde_1030(cobQ)
            DPS: DP1950(cobD)
            SFU: Sfum_1739
            MLO: mll1198
            SME: SMc04309(cobQ)
            ATU: Atu2808(cbiP)
            ATC: AGR_C_5093
            RET: RHE_CH02494(cobQ)
            RLE: RL2836(cobQ)
            BME: BMEI0690
            BMF: BAB1_1331
            BMS: BR1311(cobQ)
            BMB: BruAb1_1312(cobQ)
            BOV: BOV_1274(cobQ)
            BJA: bll3259(cbiP)
            BRA: BRADO4913(cobQ)
            BBT: BBta_3138(cobQ)
            RPA: RPA0718(cobQ1) RPA2096(cobQ2)
            RPB: RPB_0736(cobQ) RPB_3285(cobQ)
            RPC: RPC_3745 RPC_4257
            RPD: RPD_0634 RPD_2918
            RPE: RPE_2238 RPE_3122
            CCR: CC_1751 CC_2694
            SIL: SPO1242(cobQ)
            SIT: TM1040_1989
            RSP: RSP_0796(cobQ)
            JAN: Jann_2937
            RDE: RD1_2180(cobQ)
            HNE: HNE_2169(cobQ)
            NAR: Saro_0323
            SAL: Sala_2756
            GBE: GbCGDNIH1_0654
            RRU: Rru_A3381
            MAG: amb0292
            MGM: Mmc1_3127
            BHA: BH1591(cobQ)
            GKA: GK1795
            LMO: lmo1208(cbiP)
            LMF: LMOf2365_1217(cobQ)
            LIN: lin1171(cbiP)
            LWE: lwe1165(cbiP)
            SSA: SSA_0481
            STH: STH1932
            CAC: CAC1374(cbiP)
            CPE: CPE1045(cbiP)
            CPF: CPF_1300(cobQ)
            CPR: CPR_1119(cobQ)
            CTC: CTC00720(cbiP)
            CNO: NT01CX_2081(cobQ)
            CBA: CLB_0954(cobQ)
            CBH: CLC_0968(cobQ)
            CBF: CLI_1000(cobQ)
            CKL: CKL_0721(cbiP)
            CHY: CHY_0769(cobQ)
            DSY: DSY4062(cobQ)
            TTE: TTE0376(cobQ)
            MTA: Moth_1098(cobQ)
            MTU: Rv0255c(cobQ1)
            MTC: MT0268(cobQ-1)
            MBO: Mb0261c(cobQ1)
            MPA: MAP2933c(cobQ)
            MAV: MAV_3720(cobQ)
            MSM: MSMEG_2588(cobQ)
            MMC: Mmcs_2051
            CEF: CE1900
            CDI: DIP1495(cobQ)
            NFA: nfa40880
            RHA: RHA1_ro06605
            SCO: SCO1848(cobQ)
            SMA: SAV6416(cobQ1)
            PAC: PPA0419
            TFU: Tfu_0309(cobQ)
            FRA: Francci3_2603(cobQ)
            SEN: SACE_5983(cobQ)
            RXY: Rxyl_0634
            FNU: FN0977 FN2070
            TDE: TDE2326
            LIL: LB151(cbiP)
            LIC: LIC20121(cbiP)
            LBJ: LBJ_4191(cobQ)
            LBL: LBL_4206(cobQ)
            SYN: slr0618(cbiP)
            SYW: SYNW1704(cobB)
            SYC: syc1301_c(cobQ)
            SYF: Synpcc7942_0211
            SYD: Syncc9605_0766
            SYE: Syncc9902_1596
            SYG: sync_0893(cobQ)
            SYR: SynRCC307_1699(cobQ)
            SYX: SynWH7803_1658(cobQ)
            CYA: CYA_2678(cobQ)
            CYB: CYB_2173(cobQ)
            TEL: tll1716(cobQ)
            GVI: glr1772(cobQ)
            ANA: alr2377
            AVA: Ava_0196
            PMA: Pro1259(cobQ)
            PMM: PMM1160(cobB)
            PMT: PMT1183(cobB)
            PMN: PMN2A_0771(cobQ)
            PMI: PMT9312_1259
            PMB: A9601_13371(cobQ)
            PMC: P9515_13271(cobQ)
            PMF: P9303_08361(cobQ)
            PMG: P9301_13521(cobQ)
            PME: NATL1_16121(cobQ)
            TER: Tery_3957
            BFR: BF2491
            BFS: BF2524(cbiP)
            CTE: CT0938(cbiP)
            CCH: Cag_1012(cobQ)
            PLT: Plut_1140(cobQ)
            DET: DET0936(cobQ)
            DEH: cbdb_A890(cobQ)
            DRA: DR_B0012
            DGE: Dgeo_2874
            TTH: TT_P0023
            TTJ: TTHB066
            MJA: MJ0484
            MMP: MMP1215
            MAC: MA3250
            MBA: Mbar_A3191
            MMA: MM_0093
            MBU: Mbur_2361
            MHU: Mhun_2912
            MTH: MTH787
            MST: Msp_1226(cobQ)
            MSI: Msm_1565
            MKA: MK1414(cobQ)
            AFU: AF1338(cbiP)
            HAL: VNG1576G(cbiP)
            HMA: rrnAC1938(cobQ)
            HWA: HQ1404A(cbiP)
            NPH: NP5126A(cbiP)
            TAC: Ta0075
            TVO: TVN0031
            PTO: PTO0812
            PFU: PF0301
            TKO: TK0854
            RCI: RCIX2662(cobQ)
            SSO: SSO3233
            STO: ST2344
            SAI: Saci_0413
DBLINKS     IUBMB Enzyme Nomenclature: 6.3.5.10
            ExPASy - ENZYME nomenclature database: 6.3.5.10
            ExplorEnz - The Enzyme Database: 6.3.5.10
            ERGO genome analysis and discovery system: 6.3.5.10
            BRENDA, the Enzyme Database: 6.3.5.10
///
ENTRY       EC 6.4.1.1                  Enzyme
NAME        pyruvate carboxylase;
            pyruvic carboxylase
CLASS       Ligases;
            Forming carbon-carbon bonds;
            Ligases that form carbon-carbon bonds (only sub-subclass identified
            to date)
SYSNAME     pyruvate:carbon-dioxide ligase (ADP-forming)
REACTION    ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate [RN:R00344]
ALL_REAC    R00344
SUBSTRATE   ATP [CPD:C00002];
            pyruvate [CPD:C00022];
            HCO3- [CPD:C00288]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            oxaloacetate [CPD:C00036]
COFACTOR    Acetyl-CoA [CPD:C00024];
            Manganese [CPD:C00034];
            Zinc [CPD:C00038];
            Biotin [CPD:C00120]
COMMENT     A biotinyl-protein containing manganese (animal tissues) or zinc
            (yeast). The animal enzyme requires acetyl-CoA.
REFERENCE   1  [PMID:5578910]
  AUTHORS   McClure WR, Lardy HA, Kneifel HP.
  TITLE     Rat liver pyruvate carboxylase. I. Preparation, properties, and
            cation specificity.
  JOURNAL   J. Biol. Chem. 246 (1971) 3569-78.
  ORGANISM  rat [GN:rno]
REFERENCE   2  [PMID:5484476]
  AUTHORS   Scrutton MC, Young MR, Utter MF.
  TITLE     Pyruvate carboxylase from baker's yeast. The presence of bound zinc.
  JOURNAL   J. Biol. Chem. 245 (1970) 6220-7.
  ORGANISM  Saccharomyces cerevisiae [GN:sce]
REFERENCE   3
  AUTHORS   Seubert, W. and Remberger, U.
  TITLE     Renigung und Wirkungsweise der Pyruvatcarboxylase aus Pseudomonas
            citronellolis.
  JOURNAL   Biochem. Z. 334 (1961) 401-414.
  ORGANISM  Pseudomonas citronellolis
REFERENCE   4
  AUTHORS   Utter, M.F. and Keech, D.B.
  TITLE     Pyruvate carboxylase. I. Nature of the reaction.
  JOURNAL   J. Biol. Chem. 238 (1963) 2603-2608.
  ORGANISM  Aspergillus niger, chicken [GN:gga]
PATHWAY     PATH: map00020  Citrate cycle (TCA cycle)
            PATH: map00252  Alanine and aspartate metabolism
            PATH: map00620  Pyruvate metabolism
ORTHOLOGY   KO: K01958  pyruvate carboxylase
            KO: K01959  pyruvate carboxylase subunit A
            KO: K01960  pyruvate carboxylase subunit B
GENES       HSA: 5091(PC)
            MMU: 18563(Pcx)
            RNO: 25104(Pc)
            CFA: 483704(PC)
            BTA: 338471(PC)
            SSC: 397630(PC)
            GGA: 374263(PCX)
            XLA: 398811(MGC68971)
            CEL: D2023.2(pyc-1)
            SCE: YBR218C(PYC2) YGL062W(PYC1)
            AGO: AGOS_AAR162C
            PIC: PICST_90975(PYC1)
            CGR: CAGL0F06941g CAGL0K06787g
            SPO: SPBC17G9.11c(pyr1)
            ANI: AN4462.2
            AFM: AFUA_4G07710
            AOR: AO090023000801
            ANG: An04g02090(pyc)
            CNE: CNF00650
            EHI: 145.t00007
            PAE: PA1400 PA5435 PA5436
            PPU: PP_5347(accC-2)
            PST: PSPTO_5511
            PSB: Psyr_5061
            PSP: PSPPH_5143
            PFL: PFL_3029
            PFO: Pfl_5640
            PEN: PSEEN5496(accC-2)
            PMY: Pmen_3842
            SLO: Shew_2867
            LPN: lpg0466 lpg2664
            LPF: lpl2591
            LPP: lpp2718
            REU: Reut_A2997 Reut_B3892 Reut_B4717
            REH: H16_A1251(pyc) H16_A2142(accA2)
            RME: Rmet_1638 Rmet_4069
            BXE: Bxe_C0325
            BUR: Bcep18194_A6282 Bcep18194_C7328
            BPA: BPP0604
            BBR: BB0610
            TBD: Tbd_1555
            MFA: Mfla_1511
            HHE: HH1849
            WSU: WS1289(pycA)
            TDN: Tmden_1259
            CJE: Cj0933c(pycB) Cj1037c(pycA)
            CJR: CJE1011
            CJU: C8J_0870 C8J_0974(pycA)
            ABU: Abu_0176(pycB1) Abu_1226(pycB2)
            GSU: GSU2428(pyc)
            GME: Gmet_0816
            PCA: Pcar_1957
            DVU: DVU1834
            DVL: Dvul_1015
            DDE: Dde_1541 Dde_2081
            BBA: Bd3578
            DPS: DP0686
            ADE: Adeh_3015
            MXA: MXAN_3881(pyc)
            SAT: SYN_01040 SYN_01041
            MLO: mll3969
            MES: Meso_3329
            SME: SMc03895(pyc)
            ATU: Atu2726(pycA)
            ATC: AGR_C_4940
            RET: RHE_CH04002(pyc)
            RLE: RL4638
            BME: BMEI0266
            BMF: BAB1_1791(pyc)
            BMS: BR1781(pyc)
            BMB: BruAb1_1764(pyc)
            BOV: BOV_1716(pyc)
            BJA: bll7292
            RPA: RPA1450
            RPB: RPB_0228
            RPD: RPD_0602
            RPE: RPE_0635
            CCR: CC_3214
            SIL: SPO1171(pyc)
            RSP: RSP_2090(pycA)
            RDE: RD1_3376(pyc)
            MMR: Mmar10_1142
            RRU: Rru_A1121 Rru_A2317 Rru_A2886
            BSU: BG12660(pycA)
            BHA: BH2625(pycA)
            BAN: BA4157(pyc)
            BAR: GBAA4157(pyc)
            BAA: BA_4626
            BAT: BAS3859
            BCE: BC3947
            BCA: BCE_3994(pyc)
            BCZ: BCZK3707(pyc)
            BTK: BT9727_3690(pyc)
            BLI: BL02976(pycA)
            BLD: BLi01703(pycA)
            BCL: ABC2395(pycA)
            BAY: RBAM_014720
            BPU: BPUM_1377
            OIH: OB1430(pycA)
            GKA: GK1079
            SAU: SA0963(pycA)
            SAV: SAV1114(pycA)
            SAM: MW0997(pycA)
            SAR: SAR1088
            SAS: SAS1049
            SAC: SACOL1123(pyc)
            SAB: SAB0979
            SAA: SAUSA300_1014(pyc)
            SAO: SAOUHSC_01064
            SEP: SE0813
            SER: SERP0704(pyc)
            SHA: SH1838(pycA)
            SSP: SSP1675
            LMO: lmo1072(pycA)
            LMF: LMOf2365_1089(pyc)
            LIN: lin1060(pycA)
            LWE: lwe1050(pycA)
            LLA: L63652(pycA)
            LLC: LACR_0696
            LLM: llmg_0634(pycA)
            LPL: lp_2136(pycA)
            LSL: LSL_0658(pycA)
            LCA: LSEI_1315
            EFA: EF2456(pycA)
            STH: STH2182
            CAC: CAC2660(pykA)
            CTC: CTC02224
            CNO: NT01CX_0659
            CDF: CD0021(pyc)
            CBO: CBO3312
            CBA: CLB_3368(pyc)
            CBH: CLC_3254(pyc)
            CBF: CLI_3482(pyc)
            CKL: CKL_0447(pyc)
            DSY: DSY2367
            SWO: Swol_0519
            TTE: TTE1208(pycA) TTE1336(pycA2)
            MTU: Rv2967c(pca)
            MTC: MT3045(pca)
            MBO: Mb2991c(pca)
            MBB: BCG_2988c(pca)
            MPA: MAP0294c(pca) MAP2873c
            MAV: MAV_0342(pyc)
            MSM: MSMEG_2412(pyc) MSMEG_6648(pyc)
            MGI: Mflv_1882
            MMC: Mmcs_1943 Mmcs_4307
            MKM: Mkms_4393
            MJL: Mjls_4687
            CGL: NCgl0659(cgl0689)
            CGB: cg0791(pyc)
            CEF: CE0709(pyc)
            CDI: DIP0646(pyc) DIP0739(pycB)
            NFA: nfa26940 nfa41910
            RHA: RHA1_ro06517(pycA)
            SCO: SCO0546(pyc)
            TWH: TWT630(pca)
            TWS: TW647(pyc)
            LXX: Lxx15470(pycA)
            CMI: CMM_1880(pycA)
            AAU: AAur_1686(pyc) AAur_pTC10073(pyc)
            FRA: Francci3_0317
            FAL: FRAAL0680
            SEN: SACE_6118(pyc)
            RBA: RB10592(pyc)
            GVI: gll0879
            BTH: BT_1697
            BFR: BF2937
            BFS: BF2820
            SRU: SRU_0828(pycA)
            GFO: GFO_2678(pyc)
            DRA: DR_A0310
            AAE: aq_1517(pycB) aq_1520(pycA)
            MJA: MJ1229(accC) MJ1231(oadA)
            MMP: MMP0340(pycB) MMP0341(pycA)
            MAC: MA0674(pycB) MA0675(pycA)
            MBA: Mbar_A1586 Mbar_A1587
            MMA: MM_1827 MM_1828
            MBU: Mbur_2425 Mbur_2426
            MHU: Mhun_3190
            MTH: MTH1107 MTH1917
            MST: Msp_0914(pycA) Msp_1173(pycB)
            MSI: Msm_0939
            AFU: AF0220(acc) AF1252m(oadA)
            HAL: VNG1532G(acc)
            HMA: rrnB0263(accC1)
            RCI: RCIX749(pycB) RCIX750(pycA)
            SSO: SSO2466(accC)
            STO: ST0593
            SAI: Saci_0260(pycA)
STRUCTURES  PDB: 1ULZ  2DZD  2QF7  
DBLINKS     IUBMB Enzyme Nomenclature: 6.4.1.1
            ExPASy - ENZYME nomenclature database: 6.4.1.1
            ExplorEnz - The Enzyme Database: 6.4.1.1
            ERGO genome analysis and discovery system: 6.4.1.1
            BRENDA, the Enzyme Database: 6.4.1.1
            CAS: 9014-19-1
///
ENTRY       EC 6.4.1.2                  Enzyme
NAME        acetyl-CoA carboxylase;
            acetyl coenzyme A carboxylase
CLASS       Ligases;
            Forming carbon-carbon bonds;
            Ligases that form carbon-carbon bonds (only sub-subclass identified
            to date)
SYSNAME     acetyl-CoA:carbon-dioxide ligase (ADP-forming)
REACTION    ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA [RN:R00742]
ALL_REAC    R00742;
            (other) R04386
SUBSTRATE   ATP [CPD:C00002];
            acetyl-CoA [CPD:C00024];
            HCO3- [CPD:C00288]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            malonyl-CoA [CPD:C00083]
COFACTOR    Biotin [CPD:C00120]
INHIBITOR   (RS)-2-[4-(3-Chloro-5-(trifluoromethyl-2-pyridyloxy)phenoxy]-propion
            ic acid [CPD:C04871]
COMMENT     A biotinyl-protein. Also catalyses transcarboxylation; the plant
            enzyme also carboxylates propanonyl-CoA and butanoyl-CoA.
REFERENCE   1  [PMID:13905314]
  AUTHORS   HATCH MD, STUMPF PK.
  TITLE     Fat metabolism in higher plants. XVI. Acetyl coenzyme A carboxylase
            and acyl coenzyme A-malonyl coenzyme A transcarboxylase from wheat
            germ.
  JOURNAL   J. Biol. Chem. 236 (1961) 2879-85.
  ORGANISM  Triticum aestivum [GN:etae]
REFERENCE   2
  AUTHORS   Matsuhashi, M., Matsuhashi, S. and Lynen, F.
  TITLE     Zur Biosynthese der Fettsauren. V. Die Acetyl-CoA Carboxylase aus
            Rattenleber und ihre Aktivierung durch Citronsaure.
  JOURNAL   Biochem. Z. 340 (1964) 263-289.
REFERENCE   3
  AUTHORS   Matsuhashi, M., Matsuhashi, S., Numa, S. and Lynen, F.
  TITLE     [On the biosynthesis of fatty acids. IV. Acetyl-CoA carboxylase from
            yeast.].
  JOURNAL   Biochem. Z. 340 (1964) 243-262.
REFERENCE   4
  AUTHORS   Vagelos, P.
  TITLE     Regulation of fatty acid biosynthesis.
  JOURNAL   Curr. Top. Cell. Regul. 4 (1971) 119-166.
REFERENCE   5
  AUTHORS   Wakil, S.J.
  TITLE     A malonic acid derivative as an intermediate in fatty acid
            synthesis.
  JOURNAL   J. Am. Chem. Soc. 80 (1958) 6465.
  ORGANISM  pigeon
PATHWAY     PATH: map00061  Fatty acid biosynthesis
            PATH: map00253  Tetracycline biosynthesis
            PATH: map00620  Pyruvate metabolism
            PATH: map00640  Propanoate metabolism
            PATH: map04910  Insulin signaling pathway
ORTHOLOGY   KO: K01961  acetyl-CoA carboxylase
            KO: K01962  acetyl-CoA carboxylase carboxyl transferase subunit
                        alpha
            KO: K01963  acetyl-CoA carboxylase carboxyl transferase subunit beta
GENES       HSA: 31(ACACA) 32(ACACB)
            MMU: 100705(Acacb) 107476(Acaca)
            RNO: 116719(Acacb) 60581(Acaca)
            CFA: 491130(ACACA)
            BTA: 281590(ACACA)
            GGA: 396504(ACACA)
            SPU: 590371(LOC590371)
            CME: CMM188C
            SCE: YNR016C(ACC1)
            AGO: AGOS_AAR071W
            PIC: PICST_81158(ACC1)
            CAL: CaO19_7466(CaO19.7466)
            SPO: SPAC56E4.04c(cut6)
            ANI: AN6126.2
            AFM: AFUA_2G08670
            AOR: AO090011000838
            CNE: CNF02180
            DDI: DDB_0230067(accA)
            PFA: PF14_0664
            CPV: cgd8_3680
            CHO: Chro.80425
            TBR: Tb927.8.7100
            LMA: LmjF31.2970
            ECO: b0185(accA) b2316(accD) b3256(accC)
            ECJ: JW0180(accA) JW2313(accD) JW3224(accC)
            ECE: Z0197(accA) Z3578(accD) Z4616(accC)
            ECS: ECs0187 ECs3200 ECs4128
            ECC: c0223(accA) c2861(accD) c4012(accC)
            ECI: UTI89_C0200(accA) UTI89_C2601(accD) UTI89_C3688(accB)
                 UTI89_C3689(accC)
            ECP: ECP_0193 ECP_2355 ECP_3341
            ECV: APECO1_1802(accA) APECO1_3190(accC) APECO1_4248(accD)
            ECW: EcE24377A_0189(accA) EcE24377A_2610(accD)
                 EcE24377A_3740(accC)
            ECX: EcHS_A0187 EcHS_A2467 EcHS_A3448
            STY: STY0255(accA) STY2597(accD) STY3560(accC)
            STT: t0233(accA) t0498(accD) t3295(accC)
            SPT: SPA0239(accA) SPA0498(accD) SPA3247(accC)
            SEC: SC0232(accA) SC2368(accD) SC3318(accC)
            STM: STM0232(accA) STM2366(accD) STM3380(accC)
            YPE: YPO1060(accA) YPO2768(accD) YPO3658(accC)
            YPK: y0209(accC) y1601(accD) y3119(accA)
            YPM: YP_2396(accD) YP_2790(accA) YP_3888(accC2)
            YPA: YPA_0536 YPA_2076 YPA_3671
            YPN: YPN_2179 YPN_2940 YPN_3513
            YPP: YPDSF_1652
            YPS: YPTB2616(accD) YPTB2987(accA) YPTB3572(accC)
            YPI: YpsIP31758_0391(accC) YpsIP31758_1029(accA)
                 YpsIP31758_1422(accD)
            SFL: SF0175(accA) SF2392(accD) SF3294(accC)
            SFX: S0178(accA) S2527(accD) S3511(accC)
            SFV: SFV_0168(accA) SFV_2385(accD) SFV_3281(accC)
            SSN: SSON_0197(accA) SSON_2374(accD) SSON_3397(accC)
            SBO: SBO_0173(accA) SBO_2353(accD) SBO_3132(accC)
            SDY: SDY_0201(accA) SDY_2515(accD) SDY_3433(accC)
            ECA: ECA0260(accC) ECA1047(accA) ECA3056(accD)
            PLU: plu0688(accA) plu3171(accD) plu4075(accC)
            WBR: WGLp310(accD) WGLp378(accA) WGLp603(accC)
            SGL: SG1617 SG1927
            BFL: Bfl287(accA) Bfl291(accC) Bfl495(accD)
            BPN: BPEN_295(accA) BPEN_299(accC) BPEN_511(accD)
            HIN: HI0406(accA) HI0972(accC) HI1260(accD)
            HIT: NTHI0528(accA) NTHI1145(accC) NTHI1904(accD)
            HIP: CGSHiEE_00965 CGSHiEE_07100 CGSHiEE_07105
            HIQ: CGSHiGG_01735 CGSHiGG_05240 CGSHiGG_08435 CGSHiGG_08445
            HDU: HD0051(accA) HD0635(accC) HD1466(accD)
            HSO: HS_0568(accC) HS_0569(accB) HS_0881(accD) HS_0932(accA)
            PMU: PM0292(accA) PM0636(accD) PM1091(accC)
            MSU: MS0768(accA) MS1174(accD) MS1788(accC)
            APL: APL_0631(accD) APL_1486(accA) APL_1865(accC)
            XFA: XF0049 XF0203 XF1467
            XFT: PD0036(accC) PD0164(accA) PD0685(accD)
            XCC: XCC0515(accC) XCC1357(accA) XCC2540(accD)
            XCB: XC_0527 XC_1578 XC_2881
            XCV: XCV0272(accD) XCV0563(accC) XCV0565(accB) XCV1462(accA)
                 XCV2864
            XAC: XAC0530(accC) XAC1405(accA) XAC2715(accD)
            XOO: XOO0556(accC) XOO1961(accA) XOO3250(accD)
            XOM: XOO_0520(XOO0520) XOO_1851(XOO1851) XOO_3078(XOO3078)
            VCH: VC0295 VC1000 VC2244
            VCO: VC0395_A0521(accD) VC0395_A1835(accA)
            VVU: VV1_1234 VV1_1876 VV1_1993
            VVY: VV2424 VV2540 VV3136 VVA1674
            VPA: VP2189 VP2302 VP2881 VPA0795
            VFI: VF1695 VF1946 VF2387
            PPR: PBPRA2652 PBPRA2952 PBPRA3406
            PAE: PA3112(accD) PA3639(accA) PA4848(accC)
            PAU: PA14_17270(accA) PA14_23860(accD)
            PAP: PSPA7_1500(accA) PSPA7_2021(accD) PSPA7_5568(accC2)
                 PSPA7_6224(accC1)
            PPU: PP_0558(accC-1) PP_1607(accA) PP_1996(accD)
            PST: PSPTO_1550(accA) PSPTO_3815(accD) PSPTO_4861(accC-2)
            PSB: Psyr_1359 Psyr_1664 Psyr_4401
            PSP: PSPPH_1658(accD) PSPPH_2456(accC1) PSPPH_3824(accA)
                 PSPPH_4444(accC2)
            PFL: PFL_0671(accC) PFL_1192(accA) PFL_2073(accD) PFL_6158(accC)
            PFO: Pfl_0618 Pfl_1117 Pfl_1898
            PEN: PSEEN1691(accD) PSEEN4204(accA) PSEEN4857(accC-1)
            PAR: Psyc_0163 Psyc_0434(accD) Psyc_1101 Psyc_1227(accC)
            PCR: Pcryo_0174 Pcryo_0469 Pcryo_1164
            ACI: ACIAD0643(accD) ACIAD1736(accC) ACIAD3035(accA)
            ILO: IL1016(accD) IL1688(accA) IL2286(accC)
            CPS: CPS_0946(accC) CPS_1571(accA) CPS_3802(accD)
            PHA: PSHAa0266(accC) PSHAa2014(accA) PSHAa2074(accD)
            PAT: Patl_0090 Patl_1265 Patl_1605
            SDE: Sde_1107 Sde_2077
            MAQ: Maqu_0917
            CBU: CBU_0893(accD) CBU_1510(accA) CBU_1726(accC)
            CBD: COXBU7E912_0276(accC) COXBU7E912_0474(accA)
                 COXBU7E912_0957(accD)
            LPN: lpg0462(accC) lpg0785(accA) lpg1341(accD)
            LPF: lpl0504(accC) lpl0824(accA) lpl1294(accD)
            LPP: lpp0528(accC) lpp0849(accA) lpp1295(accD)
            MCA: MCA1046(accC) MCA1804(accA) MCA2493(accD)
            FTU: FTT0372c(accD) FTT0472(accB) FTT0473(accC) FTT1498c(accA)
            FTF: FTF0372c(accD) FTF0472(accB) FTF0473(accC) FTF1498c(accA)
            FTW: FTW_0793(accA) FTW_1597(accC) FTW_1706(accD)
            FTL: FTL_0295 FTL_1309 FTL_1591
            FTH: FTH_0295(accA) FTH_1281(accD) FTH_1537(accC) FTH_1538(accB)
            FTA: FTA_0313(accA) FTA_1384(accD) FTA_1677(accC)
            FTN: FTN_0272(accD) FTN_0564(accC) FTN_1508(accA)
            TCX: Tcr_0443 Tcr_0805 Tcr_1264
            NOC: Noc_0848 Noc_1022 Noc_1051
            AEH: Mlg_0026 Mlg_1238 Mlg_1843
            HHA: Hhal_1443
            HCH: HCH_01862(accA) HCH_02438(accD) HCH_06006(accC1)
                 HCH_06705(accC2)
            CSA: Csal_0579 Csal_1263
            ABO: ABO_1159(accA) ABO_1459(accD)
            AHA: AHA_1189(accA) AHA_2679(accD) AHA_3347(accC)
            DNO: DNO_0405(accD) DNO_0421(accC) DNO_1091(accA)
            BCI: BCI_0052(accC) BCI_0365(accD) BCI_0539(accA)
            VOK: COSY_0127(accA) COSY_0926(accD) COSY_0959(accC)
            NME: NMB0679 NMB1139 NMB1177 NMB1861
            NMA: NMA0596(accC) NMA0880(accD) NMA1349(accA)
            NMC: NMC1078(accA)
            NGO: NGO0044 NGO0045 NGO0249 NGO0821(accA)
            CVI: CV_0985(accC) CV_1805(mmdA) CV_2760(accD) CV_3190(accA)
            RSO: RSc1169(accA) RSc1980(accD) RSc2787(accC1)
            REU: Reut_A1124 Reut_A2303 Reut_A2866
            REH: H16_A1223(accA1) H16_A2611(accD)
            RME: Rmet_1087 Rmet_2464 Rmet_3065
            BMA: BMA1654(accA) BMA2502(accC) BMAA1718(accD)
            BMV: BMASAVP1_1652(accD) BMASAVP1_A0423(accC) BMASAVP1_A2157(accA)
            BML: BMA10299_1861(accD) BMA10299_A1282(accC) BMA10299_A3158(accA)
            BMN: BMA10247_1430(accA) BMA10247_3282(accC) BMA10247_A0532(accD)
            BXE: Bxe_A1628 Bxe_B2878
            BUR: Bcep18194_A3687 Bcep18194_A5382 Bcep18194_B2122
            BCN: Bcen_0121 Bcen_4406 Bcen_6001
            BCH: Bcen2424_2076 Bcen2424_3961
            BAM: Bamb_0506 Bamb_2111 Bamb_3351
            BPS: BPSL2241(accA) BPSL2984(accC) BPSS1696(accD)
            BPM: BURPS1710b_2679(accA) BURPS1710b_3501(accC)
                 BURPS1710b_A0766(accD) BURPS1710b_A1721(accC)
            BPL: BURPS1106A_2594(accA) BURPS1106A_3504(accC)
                 BURPS1106A_A0272(accC) BURPS1106A_A2304(accD)
            BPD: BURPS668_2543(accA) BURPS668_3466(accC) BURPS668_A0364(accC)
                 BURPS668_A2442(accD)
            BTE: BTH_I1162(accC) BTH_I1943(accA-1) BTH_II0682(accD)
                 BTH_II1679(accA-2)
            PNU: Pnuc_0860
            BPE: BP1910(accA) BP2996(fabG) BP3591(accD)
            BPA: BPP2285(accA) BPP3321(accD) BPP3916(fabG)
            BBR: BB1737(accA) BB3772(accD) BB4389(fabG) BB4734(accB)
            RFR: Rfer_1351 Rfer_1786 Rfer_3352
            POL: Bpro_1100 Bpro_2863 Bpro_3618
            PNA: Pnap_2891
            AAV: Aave_2322
            AJS: Ajs_1625
            VEI: Veis_4938
            MPT: Mpe_A2155 Mpe_A2454
            HAR: HEAR1225(accD) HEAR1288(accA)
            MMS: mma_2106 mma_2162
            NEU: NE0653(accC1) NE0695(accD) NE1021(accA)
            NET: Neut_1154 Neut_1899 Neut_2398
            NMU: Nmul_A1810 Nmul_A1910 Nmul_A2752
            EBA: ebA1474(accC) ebA4148(accA) ebA4778(accD)
            AZO: azo0864(accB) azo0915(accA) azo1049(accD)
            DAR: Daro_0844 Daro_0872 Daro_3938
            TBD: Tbd_0181 Tbd_0588 Tbd_1912
            MFA: Mfla_0024 Mfla_1248 Mfla_1696
            HPY: HP0557(accA) HP0950(accD)
            HPJ: jhp0504(accA) jhp0884(accD)
            HPA: HPAG1_0535 HPAG1_0934 HPAG1_1021
            HHE: HH0726(accA) HH1238(accD)
            HAC: Hac_0496(accB) Hac_0778(accA) Hac_1026(accD)
            WSU: WS0157(accD) WS0628(accA) WS1072(accB)
            TDN: Tmden_1174 Tmden_1608
            CJE: Cj0127c(accD) Cj0443(accA)
            CJR: CJE0122(accD) CJE0495(accA) CJE1181(accC-1) CJE1482(accC-2)
            CJJ: CJJ81176_0162(accD) CJJ81176_0470(accA) CJJ81176_1056(accC-1)
                 CJJ81176_1307(accC-2)
            CJU: C8J_0120(accD) C8J_0418(accA) C8J_1233(accC-2)
            CJD: JJD26997_0140(accD) JJD26997_0432(accC-2)
                 JJD26997_0745(accC-1) JJD26997_1494(accA)
            CFF: CFF8240_0251(accD) CFF8240_0676 CFF8240_1364(accA)
                 CFF8240_1564(accC)
            CCV: CCV52592_0748 CCV52592_1756(accD) CCV52592_1910(accA)
            CHA: CHAB381_0228(accA) CHAB381_0537(accD) CHAB381_0801
                 CHAB381_1156 CHAB381_1554(accC)
            CCO: CCC13826_0559(accA) CCC13826_0941(accD) CCC13826_1551
                 CCC13826_2104(accC)
            ABU: Abu_0040(accB) Abu_0041(accC1) Abu_0446(accD) Abu_0605(accC2)
                 Abu_2055(accA)
            NIS: NIS_0316(accA) NIS_1198(accD) NIS_1644(accC)
            SUN: SUN_0909(accD) SUN_2164(accA)
            GSU: GSU1402(accA) GSU2019(accC) GSU2370(accD)
            GME: Gmet_0984 Gmet_1216 Gmet_2476
            PCA: Pcar_0737 Pcar_1223 Pcar_2127
            PPD: Ppro_2069
            DVU: DVU2225
            DVL: Dvul_1016
            DDE: Dde_1542
            LIP: LI0489
            DPS: DP1813
            ADE: Adeh_0650 Adeh_1257 Adeh_1513
            MXA: MXAN_0082(accC) MXAN_2704(accD) MXAN_4039(accA)
                 MXAN_5595(accC) MXAN_5767(accC)
            RBE: RBE_0469(accC)
            PUB: SAR11_0486(accD) SAR11_0511(accA) SAR11_0727(accB)
            MLO: mll0203 mlr3576 mlr5075
            MES: Meso_0663 Meso_1716 Meso_3061
            PLA: Plav_1724
            SME: SMc00690(accA) SMc01345(accC) SMc02764(accD)
            ATU: Atu0020(accD) Atu1330(accC) Atu3630(accA)
            ATC: AGR_C_2451 AGR_C_32 AGR_L_2394
            RET: RHE_CH00023(accD) RHE_CH01869(accCch) RHE_CH03828(accA)
            RLE: RL0023 RL2088(accC) RL4355(accA)
            BME: BMEI0039 BMEI1063 BMEI2020
            BMF: BAB1_0924(accC) BAB1_2033(accA) BAB1_2109(accD)
            BMS: BR0906(accC) BR2032(accA) BR2107(accD)
            BMB: BruAb1_0917(accC) BruAb1_2007(accA) BruAb1_2082(accD)
            BOV: BOV_0902(accC) BOV_1954(accA) BOV_2023(accD)
            BJA: bll4290(accC) blr0191(accA) blr0747(accD)
            BRA: BRADO0089(accD) BRADO0606(accA) BRADO3501(accB)
            BBT: BBta_0095(accD) BBta_4215(accB) BBta_7576(accA)
            RPA: RPA0071(accD) RPA0508(accA) RPA2435(accC)
            RPB: RPB_0532 RPB_0633 RPB_3020
            RPC: RPC_0390 RPC_0528 RPC_2869
            RPD: RPD_0199 RPD_0297 RPD_2431
            RPE: RPE_0140 RPE_0456 RPE_2988
            NWI: Nwi_0053 Nwi_0392 Nwi_1753
            NHA: Nham_0061 Nham_0487 Nham_2189
            BHE: BH00340(accD) BH08050(accC) BH16340(accA)
            BQU: BQ00320(accD) BQ06530(accC) BQ13250(accA)
            BBK: BARBAKC583_0040(accA) BARBAKC583_0761(accC)
                 BARBAKC583_1351(accD)
            XAU: Xaut_0509
            CCR: CC_1884 CC_2995 CC_3542
            SIL: SPO1010(accC) SPO1011(accB) SPO3616(accA) SPO3817(accD)
            SIT: TM1040_2676 TM1040_3160
            RSP: RSP_0191(accC) RSP_0929(accD) RSP_1772(accA)
            RSH: Rsph17029_0419
            RSQ: Rsph17025_2479
            JAN: Jann_0060 Jann_0473
            RDE: RD1_0328(accD) RD1_0998(accA) RD1_2851(accC)
            PDE: Pden_2339
            MMR: Mmar10_0089 Mmar10_1265 Mmar10_2270
            HNE: HNE_1156(accA) HNE_2250(accC) HNE_3473(accD)
            ZMO: ZMO0583(accD) ZMO0599(accA) ZMO0735(accC)
            NAR: Saro_1300 Saro_1903 Saro_2079
            SAL: Sala_1062 Sala_1439 Sala_1796
            SWI: Swit_0618
            ELI: ELI_03100 ELI_04990 ELI_07600
            GOX: GOX0435 GOX1204 GOX1791
            GBE: GbCGDNIH1_0618 GbCGDNIH1_1958 GbCGDNIH1_2013
            RRU: Rru_A0218 Rru_A2435 Rru_A3430
            MAG: amb4012 amb4204(mpsA)
            MGM: Mmc1_0666 Mmc1_2330 Mmc1_3222
            ABA: Acid345_2746 Acid345_3287 Acid345_4701
            BSU: BG11384(accC) BG12557(accA) BG13926(accD)
            BHA: BH2787(accC) BH3165(accA) BH3166(accD)
            BAN: BA4408(accC) BA4845(accA) BA4846(accD)
            BAR: GBAA4408(accC) GBAA4845(accA) GBAA4846(accD)
            BAA: BA_4860 BA_5268 BA_5269
            BAT: BAS4088 BAS4494 BAS4495
            BCE: BC4601 BC4602
            BCA: BCE_3533(accA) BCE_4257(accC) BCE_4731(accA) BCE_4732(accD)
            BCZ: BCZK3937(accC) BCZK3938(accB) BCZK4341(accA) BCZK4342(accD)
            BTK: BT9727_3926(accC) BT9727_3927(accB) BT9727_4329(accA)
                 BT9727_4330(accD)
            BTL: BALH_3792(accC) BALH_3793(accB) BALH_4183(accA)
                 BALH_4184(accD)
            BLI: BL00404(accA) BL00405(accD)
            BLD: BLi02605(accC) BLi03069(accA) BLi03070(accD)
            BCL: ABC2468(accC) ABC2469(accB) ABC2720(accA) ABC2721(accD)
            BAY: RBAM_022670 RBAM_022680 RBAM_026250
            BPU: BPUM_1125 BPUM_1780(yngE) BPUM_1783 BPUM_1784(yngH) BPUM_2166
                 BPUM_2167 BPUM_2563 BPUM_2564
            OIH: OB1885(accC) OB2173(accA) OB2174
            GKA: GK2399 GK2741 GK2742
            SAU: SA1522(accA) SA1523
            SAV: SAV1700(accA) SAV1701
            SAM: MW1643(accA) MW1644
            SAR: SAR1778(accA) SAR1779(accD)
            SAS: SAS1627 SAS1628
            SAC: SACOL1571(accC) SACOL1747(accA) SACOL1748(accD)
            SAB: SAB1478c(accB) SAB1558c(accA) SAB1559c(accD)
            SAA: SAUSA300_1475(accC) SAUSA300_1563(accC) SAUSA300_1646(accA)
                 SAUSA300_1647(accD)
            SAO: SAOUHSC_01623 SAOUHSC_01709 SAOUHSC_01808 SAOUHSC_01809
            SEP: SE1375 SE1376
            SER: SERP1087(accC) SERP1263(accA) SERP1264(accD)
            SHA: SH1224(accB) SH1225(accA)
            SSP: SSP1066 SSP1067
            LMO: lmo1572(accA) lmo1573(accD)
            LMF: LMOf2365_1594(accA) LMOf2365_1595(accD)
            LIN: lin1607(accA) lin1608(accD)
            LWE: lwe1585(accA) lwe1586(accD)
            LLA: L0180(accD) L0190(accA)
            LLC: LACR_0829 LACR_0830
            LLM: llmg_1777(accA) llmg_1778(accD) llmg_1782(accB)
            SPY: SPy_1743(accA) SPy_1744(accD)
            SPM: spyM18_1815(accA) spyM18_1816(accD)
            SPG: SpyM3_1517(accA) SpyM3_1518(accD)
            SPS: SPs0348 SPs0349
            SPH: MGAS10270_Spy1551(accD) MGAS10270_Spy1552(accA)
                 MGAS10270_Spy1556(accB)
            SPI: MGAS10750_Spy1543(accD) MGAS10750_Spy1544(accA)
                 MGAS10750_Spy1547(accB)
            SPJ: MGAS2096_Spy1511(accD) MGAS2096_Spy1512(accA)
                 MGAS2096_Spy1515(accB)
            SPK: MGAS9429_Spy1486(accD) MGAS9429_Spy1487(accA)
                 MGAS9429_Spy1490(accB)
            SPF: SpyM50357(fabE) SpyM50360(accD) SpyM50361(accA)
            SPA: M6_Spy1478 M6_Spy1479 M6_Spy1482
            SPB: M28_Spy1473(accD) M28_Spy1474(accA) M28_Spy1477(accB)
            SPN: SP_0426 SP_0427
            SPR: spr0386(accD) spr0387(accA)
            SPD: SPD_0388(accC) SPD_0389(accD) SPD_0390(accA)
            SAG: SAG0353(accD) SAG0354(accA)
            SAN: gbs0340 gbs0341
            SAK: SAK_0427(accD) SAK_0428(accA)
            SMU: SMU.1734(accA) SMU.1735(accD)
            STC: str0392(accD) str0393(accA)
            STL: stu0392(accD) stu0393(accA)
            SSA: SSA_1930(accA) SSA_1931(accD)
            SGO: SGO_1687(accA) SGO_1688(accD) SGO_1689(accC)
            LPL: lp_0362(accB3) lp_0590(accC1) lp_0591(accD1) lp_0592(accA1)
                 lp_1676(accB2) lp_1679(accD2) lp_1680(accA2)
            LSA: LSA0821(accD) LSA0822(accA)
            LSL: LSL_0459(accD) LSL_0460(accA)
            LDB: Ldb0905(accB) Ldb0908(accD) Ldb0909(accA)
            LBU: LBUL_0826 LBUL_0827
            LBR: LVIS_0926 LVIS_0927
            LCA: LSEI_2109 LSEI_2110
            LRE: Lreu_0982
            EFA: EF2875(accA) EF2876(accD)
            OOE: OEOE_1583 OEOE_1584
            STH: STH1191
            CAC: CAC3568(accA) CAC3569(accD) CAC3570(accC)
            CPE: CPE1075(accD) CPE1076(accA)
            CPF: CPF_1330(accC) CPF_1331(accD) CPF_1332(accA)
            CPR: CPR_1142(accC) CPR_1143(accD) CPR_1144(accA)
            CTC: CTC00135
            CNO: NT01CX_0929(accC) NT01CX_0930(accD) NT01CX_0931(accA)
            CDF: CD1936(accA) CD1937(accD)
            CBO: CBO3594(accA) CBO3595(accD)
            CBA: CLB_3674(accA) CLB_3675(accD)
            CBH: CLC_3572(accA) CLC_3573(accD)
            CBF: CLI_3819(accA) CLI_3820(accD)
            CBE: Cbei_1077
            CKL: CKL_0111(accD) CKL_0112(accA)
            CHY: CHY_0918(accC1) CHY_1141(accD) CHY_1142(accA) CHY_1998(accC2)
            DSY: DSY1315 DSY1316 DSY2366
            DRM: Dred_2314
            SWO: Swol_1845 Swol_1846
            MTA: Moth_1524
            MTU: Rv0904c(accD3)
            MTC: MT0927(accD)
            MBO: Mb0928c(accD3)
            MBB: BCG_0956c(accD3)
            MPA: MAP0839c(accD3)
            MSM: MSMEG_2169(accD)
            MMC: Mmcs_4432
            CGL: NCgl0797(cgl0831)
            CGB: cg0802(accBC) cg0812(dtsR1) cg0951(accDA)
            CEF: CE0907(accDA)
            CDI: DIP0787(accDA)
            NFA: nfa6710
            RHA: RHA1_ro05011 RHA1_ro10399(accC2)
            SCO: SCO2445(SCC24.16)
            SMA: SAV5722(accD3)
            FRA: Francci3_0649 Francci3_2926 Francci3_2928
            FAL: FRAAL1154 FRAAL3196(accA) FRAAL3198(accC)
            SEN: SACE_0026(accA) SACE_0028 SACE_3856(accD3)
            RXY: Rxyl_2087 Rxyl_2088
            FNU: FN0408 FN0409
            RBA: RB12636(acc) RB12904(accD) RB8310(accA)
            CTR: CT265(accA) CT293(accD)
            CTA: CTA_0130(accB) CTA_0287(accA) CTA_0315(accD)
            CMU: TC0536 TC0566
            CPN: CPn0058(accD) CPn0414(accA)
            CPA: CP0340 CP0717
            CPJ: CPj0058(accD) CPj0414(accA)
            CPT: CpB0059 CpB0430
            CCA: CCA00346(accD) CCA00380(accA)
            CAB: CAB338 CAB367(accA)
            CFE: CF0628(accA) CF0660(accD)
            PCU: pc1164(accA)
            TDE: TDE0589(accA) TDE0590(accD)
            SYN: sll0053(accC) sll0336(accD) sll0728(accA)
            SYW: SYNW0336(accC) SYNW0788(accD) SYNW1736(accA)
            SYC: syc0052_d(accA) syc0177_c(accC) syc2139_c(accD)
            SYF: Synpcc7942_1379 Synpcc7942_1595 Synpcc7942_1956
            SYD: Syncc9605_0730 Syncc9605_1860 Syncc9605_2259
            SYE: Syncc9902_0421 Syncc9902_0793 Syncc9902_1633
            SYG: sync_1707(accD) sync_1988(accA) sync_2459(accC)
            SYR: SynRCC307_0341(accC) SynRCC307_0993(accD)
                 SynRCC307_1584(accA)
            SYX: SynWH7803_0656(accA) SynWH7803_1148(accD)
                 SynWH7803_2128(accC)
            CYA: CYA_0852(accC) CYA_2104(accD) CYA_2152(accA)
            CYB: CYB_1391(accC) CYB_2665(accD) CYB_2755(accA)
            TEL: tll1311(accA) tlr1643(accD) tlr1808(accC)
            GVI: gll2012(accC) gll2864(accA) glr1605(accD)
            ANA: all2364(accD) alr0939(accC) alr5285(accA)
            AVA: Ava_0185 Ava_0516 Ava_2535
            PMA: Pro0074(accC) Pro0534(accA) Pro0859(accD)
            PMM: PMM0060(accC) PMM0534(accA) PMM0784(accD)
            PMT: PMT0534(accD) PMT1229(accA) PMT1588(accC)
            PMN: PMN2A_0191 PMN2A_1423 PMN2A_1865
            PMI: PMT9312_0062 PMT9312_0534 PMT9312_0792
            PMB: A9601_00261(accB) A9601_00721(accC) A9601_05901(accA)
                 A9601_08481(accD)
            PMC: P9515_00261(accB) P9515_00691(accC) P9515_05981(accA)
                 P9515_07971(accD)
            PMF: P9303_00311(accB) P9303_03221(accC) P9303_07821(accA)
                 P9303_17311(accD)
            PMG: P9301_00261(accB) P9301_00711(accC) P9301_05601(accA)
                 P9301_08451(accD)
            PMH: P9215_00721 P9215_06151 P9215_08791
            PME: NATL1_00261(accB) NATL1_01241(accC) NATL1_05901(accA)
                 NATL1_08231(accD)
            TER: Tery_0968 Tery_2684
            SRU: SRU_0468(accC) SRU_0937(accC) SRU_1155(accD) SRU_2348(accA)
            CHU: CHU_1517(accA) CHU_1622(accC) CHU_1623(accB) CHU_3281(accD)
            GFO: GFO_0383(accD) GFO_0598(accA) GFO_3344(accB)
            FPS: FP0322(accD) FP0613(accA) FP2378(accB)
            CTE: CT0157(accC) CT0161(accA) CT1555(accD)
            CCH: Cag_0289 Cag_0359 Cag_0363 Cag_1127
            PLT: Plut_0363 Plut_1956 Plut_1960
            DET: DET0120(accC)
            DEH: cbdb_A141(accC)
            RRS: RoseRS_0393 RoseRS_3200
            RCA: Rcas_1151
            DRA: DR_1214 DR_1215
            DGE: Dgeo_2176 Dgeo_2177
            TTH: TTC1408 TTC1409
            TTJ: TTHA1767 TTHA1768
            AAE: aq_1206(accA) aq_445(accD)
STRUCTURES  PDB: 1A6X  1BDO  1OD2  1OD4  1UYR  1UYS  1UYT  1UYV  1VRG  1W2X  
                 1W93  1W96  2BDO  2DN8  2F9Y  2HJW  3BDO  
DBLINKS     IUBMB Enzyme Nomenclature: 6.4.1.2
            ExPASy - ENZYME nomenclature database: 6.4.1.2
            ExplorEnz - The Enzyme Database: 6.4.1.2
            ERGO genome analysis and discovery system: 6.4.1.2
            BRENDA, the Enzyme Database: 6.4.1.2
            CAS: 9023-93-2
///
ENTRY       EC 6.4.1.3                  Enzyme
NAME        propionyl-CoA carboxylase;
            propionyl coenzyme A carboxylase
CLASS       Ligases;
            Forming carbon-carbon bonds;
            Ligases that form carbon-carbon bonds (only sub-subclass identified
            to date)
SYSNAME     propanoyl-CoA:carbon-dioxide ligase (ADP-forming)
REACTION    ATP + propanoyl-CoA + HCO3- = ADP + phosphate +
            (S)-methylmalonyl-CoA [RN:R01859]
ALL_REAC    R01859
SUBSTRATE   ATP [CPD:C00002];
            propanoyl-CoA [CPD:C00100];
            HCO3- [CPD:C00288]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            (S)-methylmalonyl-CoA [CPD:C00683]
COFACTOR    Biotin [CPD:C00120]
COMMENT     A biotinyl-protein. Also carboxylates butanoyl-CoA and catalyses
            transcarboxylation.
REFERENCE   1
  AUTHORS   Kaziro, Y., Ochoa, S., Warner, R.C. and Chen, J.-Y.
  TITLE     Metabolism of propionic acid in animal tissues. VIII. Crystalline
            propionyl carboxylase.
  JOURNAL   J. Biol. Chem. 236 (1961) 1917-1923.
REFERENCE   2
  AUTHORS   Lane, M.D., Halenz, D.R., Kosow, D.P. and Hegre, C.S.
  TITLE     Further studies on mitochondrial propionyl carboxylase.
  JOURNAL   J. Biol. Chem. 235 (1960) 3082-3086.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:656363]
  AUTHORS   Meyer H, Nevaldine B, Meyer F.
  TITLE     Acyl-coenzyme A carboxylase of the free-living nematode Turbatrix
            aceti. 1. Its isolation and molecular characteristics.
  JOURNAL   Biochemistry. 17 (1978) 1822-7.
  ORGANISM  Caenorhabditis briggsae [GN:dcbr], Turbatrix aceti
REFERENCE   4  [PMID:4150153]
  AUTHORS   Moss J, Lane MD.
  TITLE     The biotin-dependent enzymes.
  JOURNAL   Adv. Enzymol. Relat. Areas. Mol. Biol. 35 (1971) 321-442.
REFERENCE   5
  AUTHORS   Vagelos, P.
  TITLE     Regulation of fatty acid biosynthesis.
  JOURNAL   Curr. Top. Cell. Regul. 4 (1971) 119-166.
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
            PATH: map00640  Propanoate metabolism
ORTHOLOGY   KO: K01964  propionyl-CoA carboxylase
            KO: K01965  propionyl-CoA carboxylase alpha chain
            KO: K01966  propionyl-CoA carboxylase beta chain
GENES       HSA: 5095(PCCA) 5096(PCCB)
            MMU: 110821(Pcca) 66904(Pccb)
            RNO: 24624(Pccb)
            CFA: 477076(PCCB)
            SSC: 396935(PCCB)
            GGA: 418774(PCCA)
            XLA: 399045(MGC68650)
            DRE: 405861(pccb)
            SPU: 582365(LOC582365) 592281(LOC592281)
            CEL: F27D9.5(pcca-1) F52E4.1(pccb-1)
            CME: CMM132C CMN243C
            AFM: AFUA_1G15520
            CNE: CNC01820
            DDI: DDBDRAFT_0166993 DDB_0230063(pccA)
            TET: TTHERM_00088050
            LMA: LmjF01.0050 LmjF28.0490
            PAE: PA2012 PA2014 PA2888
            PAU: PA14_38460(gnyB) PA14_38480(gnyA)
            PPU: PP_4065 PP_4067
            PPF: Pput_1776
            PST: PSPTO_2736 PSPTO_2738
            PSB: Psyr_1538 Psyr_2469
            PSP: PSPPH_2627
            PFL: PFL_4196(accD1)
            PFO: Pfl_3657 Pfl_3947
            PEN: PSEEN3387(mccB)
            PMY: Pmen_2032 Pmen_2691 Pmen_3842
            PAR: Psyc_0309
            PCR: Pcryo_0340
            PRW: PsycPRwf_2067
            SDN: Sden_2246
            SFR: Sfri_2728
            SAZ: Sama_1361
            SBL: Sbal_2829
            SBM: Shew185_2847
            SLO: Shew_2571 Shew_2867
            SPC: Sputcn32_1718
            SSE: Ssed_1457
            SPL: Spea_2798
            SHE: Shewmr4_2323
            SHM: Shewmr7_2395
            SHN: Shewana3_1671
            SHW: Sputw3181_2307
            PAT: Patl_0317 Patl_1271 Patl_2926
            MAQ: Maqu_2123 Maqu_2804
            LPN: lpg1827 lpg2227
            LPF: lpl1791 lpl2152
            LPP: lpp1790 lpp2178
            NOC: Noc_1890
            HCH: HCH_03944 HCH_05748
            ABO: ABO_0989(accD)
            CVI: CV_0019 CV_1764
            RSO: RSc0269(RS03236)
            REU: Reut_A0145 Reut_A1465 Reut_A2997 Reut_B3891 Reut_B3892
                 Reut_B4463
            REH: H16_A2144(pccB)
            RME: Rmet_0609 Rmet_1721
            BMA: BMAA0803
            BXE: Bxe_B0961
            BVI: Bcep1808_3494
            BUR: Bcep18194_A4414 Bcep18194_B0424
            BCN: Bcen_3128
            BCH: Bcen2424_5239
            BAM: Bamb_4587
            BPS: BPSS1447 BPSS2031
            BPM: BURPS1710b_A0470(accB) BURPS1710b_A1149
            BTE: BTH_II0289 BTH_II0948
            RFR: Rfer_2802 Rfer_2803 Rfer_2818 Rfer_3832 Rfer_3899
            POL: Bpro_2164 Bpro_2167 Bpro_4160 Bpro_5268
            PNA: Pnap_0471
            AAV: Aave_2116 Aave_4354
            AJS: Ajs_3763
            VEI: Veis_0831 Veis_1897 Veis_2413 Veis_4183 Veis_4244
            MPT: Mpe_A1016 Mpe_A1017 Mpe_A3359
            HAR: HEAR1471(mdcB)
            EBA: ebA3742(pccB) ebA3743(pccA) ebA4657
            AZO: azo0687(pccB) azo0688(pccA)
            DAR: Daro_0092 Daro_4003 Daro_4004
            GME: Gmet_3290
            GUR: Gura_0651 Gura_3488
            BBA: Bd3858(pccB)
            ADE: Adeh_0250 Adeh_0463 Adeh_1646
            AFW: Anae109_2164 Anae109_4093
            MXA: MXAN_0081(accB) MXAN_1111(pccA) MXAN_1113(pccB) MXAN_3759
            SFU: Sfum_1223
            RPR: RP618(pccA) RP619(pccB)
            RTY: RT0608(pccA) RT0609(pccB)
            RCO: RC0959(pccA) RC0960(pccB)
            RFE: RF_0418(pccB) RF_0419(accC)
            RBE: RBE_0467(pccB)
            RCM: A1E_01660
            WOL: WD0433(pccA) WD1157(pccB)
            WBM: Wbm0455 Wbm0588
            AMA: AM769(pccB) AM824(pycA)
            APH: APH_0364(pccA) APH_0415(pccB)
            ERU: Erum4460(pccB) Erum5320(bccA)
            ERW: ERWE_CDS_04670(pccB) ERWE_CDS_05580(pccA)
            ERG: ERGA_CDS_04570(pccB) ERGA_CDS_05470(pccA)
            ECN: Ecaj_0437 Ecaj_0539
            ECH: ECH_0487(pccA) ECH_0599(pccB)
            NSE: NSE_0796(pccB) NSE_0815(pccA)
            MLO: mll0348 mll0871
            MES: Meso_1020 Meso_1735
            PLA: Plav_1979 Plav_2786
            SME: SMb20755(pccB) SMb20756(pccA)
            SMD: Smed_4533
            ATU: Atu3581(pccA) Atu3586
            ATC: AGR_L_2481 AGR_L_580GM
            RET: RHE_CH02226(pccA) RHE_CH02232(pccB) RHE_PC00063(mccA)
            RLE: RL2558(pccA) RL2563(pccB) pRL100295(mccc2)
            BME: BMEI0800 BMEI0801
            BMF: BAB1_1210 BAB1_1211
            BMS: BR1189(pccA)
            BMB: BruAb1_1193 BruAb1_1194(pccA)
            BOV: BOV_1149(pccA)
            OAN: Oant_0038
            BJA: bll5267(pccA) bll5356 blr3940
            BRA: BRADO3132 BRADO3679 BRADO4331
            BBT: BBta_2020 BBta_3573 BBta_4047 BBta_5024
            RPA: RPA2143 RPA3175 RPA3203(pccB)
            RPB: RPB_2342 RPB_2367 RPB_2934 RPB_3260
            RPC: RPC_2782 RPC_3097 RPC_3201 RPC_3352 RPC_3397
            RPD: RPD_0351 RPD_2204 RPD_2534 RPD_3093 RPD_3122
            RPE: RPE_2254 RPE_2380 RPE_2912 RPE_3439 RPE_3541
            NWI: Nwi_1401 Nwi_1605
            NHA: Nham_1579 Nham_2125
            XAU: Xaut_1857
            CCR: CC_1975 CC_2168 CC_2170 CC_2179
            SIL: SPO0578 SPO1094(pccB) SPO1101(pccA)
            SIT: TM1040_0737 TM1040_1869 TM1040_1877
            RSP: RSP_2189(pccB) RSP_2191(pccA)
            RSH: Rsph17029_1170
            RSQ: Rsph17025_2011 Rsph17025_2305
            JAN: Jann_1145
            RDE: RD1_2028(pccB) RD1_2032(pccA)
            PDE: Pden_3637
            MMR: Mmar10_1734
            HNE: HNE_0096
            NAR: Saro_0808 Saro_1643 Saro_2593
            SAL: Sala_1532 Sala_1854
            SWI: Swit_2162
            ELI: ELI_04890 ELI_11765
            ACR: Acry_1516
            RRU: Rru_A0051 Rru_A0053 Rru_A1324 Rru_A1943
            MAG: amb0676 amb4242 amb4243
            MGM: Mmc1_0385 Mmc1_0386
            ABA: Acid345_1428 Acid345_4697
            SUS: Acid_3875
            BSU: BG11733(yqjD) BG13456(yngE)
            BHA: BH1136 BH2957(mmdA)
            BAN: BA2548 BA2552
            BAR: GBAA2548 GBAA2552
            BAA: BA_3050 BA_3054
            BAT: BAS2370 BAS2375
            BCE: BC2484 BC2488
            BCA: BCE_2549 BCE_2553
            BCZ: BCZK2286(pcc) BCZK2291(pccB)
            BCY: Bcer98_1807
            BTK: BT9727_2328(pcc) BT9727_2332(pccB)
            BTL: BALH_2293(pccB)
            BLI: BL01386(yqjD) BL01992(yngE)
            BLD: BLi02139(yngE) BLi02572(yqjD)
            BCL: ABC1510 ABC2572
            BAY: RBAM_022220(yqjD)
            OIH: OB1699 OB1860
            GKA: GK1603 GK2349
            STH: STH1579
            CHY: CHY_0917(pccB)
            TTE: TTE1220(accA) TTE2385(accA2)
            MTA: Moth_1156
            MTU: Rv0973c(accA2) Rv0974c(accD2) Rv2247(accD6) Rv2502c(accD1)
                 Rv3280(accD5) Rv3799c(accD4)
            MTC: MT1001(bccA-1) MT1002(pccB-1) MT3379.1(pccB-4) MT3906(pccB-5)
            MBO: Mb0999c(accD2) Mb2271(accD6) Mb2530c(accD1) Mb3308(accD5)
                 Mb3829c(accD4)
            MBB: BCG_2264(accD6) BCG_3309(accD5) BCG_3861c(accD4)
            MLE: ML0102(accD4) ML0731(accD5) ML1657
            MPA: MAP0221(accD4_1) MAP0911c(accA2) MAP0912c(accD2)
                 MAP2000(accD6) MAP2314c(accD1) MAP3399(accD5)
            MAV: MAV_0220 MAV_2190 MAV_4250
            MSM: MSMEG_1813 MSMEG_4329 MSMEG_4717 MSMEG_5492 MSMEG_6391
            MVA: Mvan_0066 Mvan_2019 Mvan_3758 Mvan_4091 Mvan_4848
            MGI: Mflv_0781 Mflv_1883 Mflv_2552 Mflv_2775 Mflv_4327
            MMC: Mmcs_1794 Mmcs_2679 Mmcs_3368 Mmcs_3631 Mmcs_4306
            MKM: Mkms_1841 Mkms_2724 Mkms_3430 Mkms_3704 Mkms_4392
            MJL: Mjls_1775 Mjls_2710 Mjls_3379 Mjls_3636 Mjls_4686
            CGL: NCgl0677(cgl0707) NCgl0678(cgl0708) NCgl2772(cgl2870)
            CGB: cg0811(dtsR2) cg0812(dtsR1) cg3177(pccB)
            CEF: CE0737(dtsR2) CE0738(dtsR) CE0805 CE2704
            CDI: DIP0658(pccB1) DIP0660(pccB2) DIP2188(pccB)
            CJK: jk0139(accD3) jk1551(accD1) jk1662(accD2)
            NFA: nfa16180 nfa1900 nfa26080 nfa50370 nfa53290 nfa53300 nfa9940
            RHA: RHA1_ro01202(pccB1) RHA1_ro01930 RHA1_ro01931 RHA1_ro03744
                 RHA1_ro04066 RHA1_ro06095 RHA1_ro06292 RHA1_ro06570
                 RHA1_ro08919(pccB2)
            SCO: SCO2776(accD1) SCO4380(SCD10.12) SCO4381(SCD10.13)
                 SCO4926(pccB)
            SMA: SAV3331(pccB) SAV3866(accA2) SAV3867(accD2) SAV5278(accD1)
            TWH: TWT023(pccB)
            TWS: TW025(pccB)
            LXX: Lxx04810(pccB)
            ART: Arth_1385
            AAU: AAur_1418
            PAC: PPA1707
            NCA: Noca_0147 Noca_1986 Noca_4136 Noca_4552
            TFU: Tfu_0948 Tfu_2555
            FRA: Francci3_0700 Francci3_3485
            FAL: FRAAL1212(pcc) FRAAL1667(accD2) FRAAL1668(accC)
                 FRAAL2343(accD) FRAAL3158(accD) FRAAL3857 FRAAL5672(pccB)
            ACE: Acel_0403 Acel_0874
            SEN: SACE_3241(accD2) SACE_3242 SACE_3398(pccB) SACE_7039(accD1)
            STP: Strop_0027 Strop_2764 Strop_3382 Strop_4327
            BLO: BL1536(pccB)
            BAD: BAD_0255(pccB)
            RXY: Rxyl_1703
            LIL: LA3803(pccB2)
            LIC: LIC10443(mccB)
            BTH: BT_1450 BT_1686
            BFR: BF1611 BF3289 BF3531
            BFS: BF1623
            PGI: PG1612(mmdA)
            SRU: SRU_1218 SRU_2246(pccB)
            CHU: CHU_0752(pccB)
            FJO: Fjoh_2546
            CCH: Cag_1127 Cag_1521
            PLT: Plut_1431
            DET: DET0447
            DEH: cbdb_A404
            RRS: RoseRS_2907 RoseRS_3827
            RCA: Rcas_0975
            DRA: DR_1316 DR_1542
            DGE: Dgeo_0489 Dgeo_0811
            TTH: TTC0783 TTC1192
            TTJ: TTHA1148 TTHA1557
            TMA: TM0716
            HAL: VNG0623G(yngE)
            HMA: rrnB0261(pccB)
            NPH: NP4250A(accB_1)
            HBU: Hbut_1155
STRUCTURES  PDB: 1XNV  1XNW  1XNY  1XO6  2A7S  2BZR  2CQY  
DBLINKS     IUBMB Enzyme Nomenclature: 6.4.1.3
            ExPASy - ENZYME nomenclature database: 6.4.1.3
            ExplorEnz - The Enzyme Database: 6.4.1.3
            ERGO genome analysis and discovery system: 6.4.1.3
            BRENDA, the Enzyme Database: 6.4.1.3
            CAS: 9023-94-3
///
ENTRY       EC 6.4.1.4                  Enzyme
NAME        methylcrotonoyl-CoA carboxylase;
            methylcrotonyl coenzyme A carboxylase;
            beta-methylcrotonyl coenzyme A carboxylase;
            beta-methylcrotonyl CoA carboxylase;
            methylcrotonyl-CoA carboxylase
CLASS       Ligases;
            Forming carbon-carbon bonds;
            Ligases that form carbon-carbon bonds (only sub-subclass identified
            to date)
SYSNAME     3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)
REACTION    ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate +
            3-methylglutaconyl-CoA [RN:R04138]
ALL_REAC    R04138
SUBSTRATE   ATP [CPD:C00002];
            3-methylcrotonoyl-CoA [CPD:C03069];
            HCO3- [CPD:C00288]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            3-methylglutaconyl-CoA [CPD:C03231]
COFACTOR    Biotin [CPD:C00120]
COMMENT     A biotinyl-protein.
REFERENCE   1
  AUTHORS   Knappe, J., Schlegel, H.-G. and Lynen, F.
  TITLE     Zur biochemischen Funktion des Biotins. I. Die Beteilligung der
            beta-Methyl-crotonyl-Carboxylase an der Bildung von
            beta-Hydroxy-beta-methyl-glutaryl-CoA from
            beta-Hydroxy-isovaleryl-CoA.
  JOURNAL   Biochem. Z. 335 (1961) 101-122.
REFERENCE   2
  AUTHORS   Lynen, F., Knappe, J., Lorch, E., Jutting, G., Ringelmann, E. and
            Lachance, J.-P.
  TITLE     Zur biochemischen Funktion des Biotins. II. Reinigung und
            Wirkungsweise der beta-Methyl-crotonyl-Carboxlase.
  JOURNAL   Biochem. Z. 335 (1961) 123-166.
REFERENCE   3
  AUTHORS   Rilling, H.C. and Coon, M.J.
  TITLE     The enzymatic isomerization of alpha-methylvinylacetyl coenzyme A
            and the specificity of a bacterial alpha-methylcrotonyl coenzyme A
            carboxylase.
  JOURNAL   J. Biol. Chem. 235 (1960) 3087-3092.
  ORGANISM  cow [GN:bta]
REFERENCE   4
  AUTHORS   Vagelos, P.
  TITLE     Regulation of fatty acid biosynthesis.
  JOURNAL   Curr. Top. Cell. Regul. 4 (1971) 119-166.
PATHWAY     PATH: map00280  Valine, leucine and isoleucine degradation
ORTHOLOGY   KO: K01967  3-methylcrotonyl-CoA carboxylase
            KO: K01968  3-methylcrotonyl-CoA carboxylase alpha subunit
            KO: K01969  3-methylcrotonyl-CoA carboxylase beta subunit
GENES       HSA: 56922(MCCC1) 64087(MCCC2)
            PTR: 461823(MCCC2)
            MMU: 72039(Mccc1) 78038(Mccc2)
            RNO: 294972(Mccc1)
            CFA: 478091(MCCC2) 478645(MCCC1)
            GGA: 424962(MCCC1) 427395(MCCC2)
            XLA: 444497(MGC81895)
            XTR: 448313(mccc1)
            DRE: 405863(zgc:85685)
            SPU: 579180(LOC579180)
            DME: Dmel_CG3267
            CEL: F32B6.2
            ATH: AT4G34030(MCCB)
            OSA: 4345605 4352741
            CME: CMT071C CMT073C
            PIC: PICST_28452(DUR1)
            ANI: AN4687.2 AN4690.2
            AFM: AFUA_5G08910 AFUA_5G08940
            AOR: AO090020000492 AO090020000495
            CNE: CNC01910
            UMA: UM02822.1
            DDI: DDBDRAFT_0168580 DDB_0230065(mccA)
            TET: TTHERM_00502240
            TBR: Tb11.02.4480
            TCR: 504835.20 506773.40 508799.170
            LMA: LmjF11.0590 LmjF31.3130
            XCC: XCC0244(accC) XCC0245(accD)
            XCB: XC_0254 XC_0255
            XAC: XAC0263(accC) XAC0264(accD)
            XOO: XOO4377(accC) XOO4378(accD)
            XOM: XOO_4121(XOO4121) XOO_4122(XOO4122)
            VVU: VV2_0497
            VVY: VVA1047
            VPA: VPA0617 VPA1126 VPA1128
            PPR: PBPRB1115 PBPRB1116
            PAE: PA2891
            PFL: PFL_3937(mccB) PFL_4199
            PFO: Pfl_3950
            PEN: PSEEN3389
            PAR: Psyc_0311
            SON: SO_1894 SO_1896(pccB-1)
            SDN: Sden_2248
            SHN: Shewana3_1669
            ILO: IL0875 IL0877
            CPS: CPS_1600(mccA) CPS_1602(mccB)
            PHA: PSHAa1449 PSHAa1451
            PAT: Patl_0319
            CBU: CBU_0975 CBU_0977
            HCH: HCH_03946 HCH_05752
            ABO: ABO_0986(accA) ABO_1237(fabG) ABO_1239
            AHA: AHA_2075 AHA_2077
            RSO: RSc0265(RS05771)
            REU: Reut_A0151 Reut_A1463 Reut_B4460
            RME: Rmet_0608 Rmet_1724
            BMA: BMAA0805
            BXE: Bxe_A2760 Bxe_A2761 Bxe_B0963
            BUR: Bcep18194_B0426
            BPS: BPSS1445
            BPM: BURPS1710b_A0468(accA)
            BTE: BTH_II0950
            BPE: BP0448(accB) BP0449(accA)
            BPA: BPP4362(accB) BPP4363(accA)
            BBR: BB4948(accB) BB4949(accA)
            RFR: Rfer_2815 Rfer_3830
            POL: Bpro_4157
            MPT: Mpe_A3356
            EBA: ebA4659
            AZO: azo3070
            DAR: Daro_0089
            GME: Gmet_3292
            BBA: Bd3580(mccB)
            MLO: mll6011 mll6012 mll7727 mll7731
            MES: Meso_0918 Meso_0930
            SME: SMb21122(mccA) SMb21124(mccB)
            ATU: Atu3478(mccB) Atu3479(mccA)
            ATC: AGR_L_2704 AGR_L_2706
            RET: RHE_PC00062(mccB) RHE_PC00063(mccA)
            RLE: pRL100294(mccc1)
            BME: BMEI1924 BMEI1925
            BMF: BAB1_0018 BAB1_0019
            BMS: BR0018 BR0019
            BMB: BruAb1_0018 BruAb1_0019
            BJA: blr0986(mccB) blr0987(mccA) blr4420(mccB) blr4421(mccA)
            BRA: BRADO3680
            BBT: BBta_4048
            RPB: RPB_3259
            RPE: RPE_2255
            SIL: SPO0579 SPO2789(mccA) SPO2790(mccB)
            SIT: TM1040_0738
            RSP: RSP_2508(mccB) RSP_2509(mccA)
            RDE: RD1_3297(mccA) RD1_3298(mccB)
            RRU: Rru_A1941
            MAG: amb0674
            CGB: cg0802(accBC)
            FRA: Francci3_1527 Francci3_1528
            LIL: LA2736(accC2)
            LIC: LIC11277(accC)
STRUCTURES  PDB: 2EJM  
DBLINKS     IUBMB Enzyme Nomenclature: 6.4.1.4
            ExPASy - ENZYME nomenclature database: 6.4.1.4
            ExplorEnz - The Enzyme Database: 6.4.1.4
            ERGO genome analysis and discovery system: 6.4.1.4
            BRENDA, the Enzyme Database: 6.4.1.4
            CAS: 9023-95-4
///
ENTRY       EC 6.4.1.5                  Enzyme
NAME        geranoyl-CoA carboxylase;
            geranoyl coenzyme A carboxylase;
            geranyl-CoA carboxylase
CLASS       Ligases;
            Forming carbon-carbon bonds;
            Ligases that form carbon-carbon bonds (only sub-subclass identified
            to date)
SYSNAME     geranoyl-CoA:carbon-dioxide ligase (ADP-forming)
REACTION    ATP + geranoyl-CoA + HCO3- = ADP + phosphate +
            3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA [RN:R03494]
ALL_REAC    R03494
SUBSTRATE   ATP [CPD:C00002];
            geranoyl-CoA [CPD:C01920];
            HCO3- [CPD:C00288]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA
COFACTOR    Biotin [CPD:C00120]
COMMENT     A biotinyl-protein. Also carboxylates dimethylpropenoyl-CoA and
            farnesoyl-CoA.
REFERENCE   1
  AUTHORS   Seubert, W., Fass, E. and Remberger, U.
  TITLE     Untersuchungen uber den bakteriellen Abbau von Isoprenoiden. III.
            Reinigung und Eigenschaften der Geranylcarboxylase.
  JOURNAL   Biochem. Z. 338 (1963) 265-275.
DBLINKS     IUBMB Enzyme Nomenclature: 6.4.1.5
            ExPASy - ENZYME nomenclature database: 6.4.1.5
            ExplorEnz - The Enzyme Database: 6.4.1.5
            ERGO genome analysis and discovery system: 6.4.1.5
            UM-BBD (Biocatalysis/Biodegradation Database): 6.4.1.5
            BRENDA, the Enzyme Database: 6.4.1.5
            CAS: 37324-35-9
///
ENTRY       EC 6.4.1.6                  Enzyme
NAME        acetone carboxylase
CLASS       Ligases;
            Forming carbon-carbon bonds;
            Ligases that form carbon-carbon bonds (only sub-subclass identified
            to date)
SYSNAME     acetone:carbon-dioxide ligase (AMP-forming)
REACTION    acetone + CO2 + ATP + 2 H2O = acetoacetate + AMP + 2 phosphate
            [RN:R05735]
ALL_REAC    R05735
SUBSTRATE   acetone [CPD:C00207];
            CO2 [CPD:C00011];
            ATP [CPD:C00002];
            H2O [CPD:C00001]
PRODUCT     acetoacetate [CPD:C00164];
            AMP [CPD:C00020];
            phosphate [CPD:C00009]
COMMENT     Requires Mg2+ and ATP. The enzyme from Xanthobacter sp. strain Py2
            also carboxylates butan-2-one to 3-oxopentanoate.
REFERENCE   1  [PMID:9237998]
  AUTHORS   Sluis MK, Ensign SA.
  TITLE     Purification and characterization of acetone carboxylase from
            Xanthobacter strain Py2.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 8456-61.
  ORGANISM  Xanthobacter sp.
DBLINKS     IUBMB Enzyme Nomenclature: 6.4.1.6
            ExPASy - ENZYME nomenclature database: 6.4.1.6
            ExplorEnz - The Enzyme Database: 6.4.1.6
            ERGO genome analysis and discovery system: 6.4.1.6
            BRENDA, the Enzyme Database: 6.4.1.6
///
ENTRY       EC 6.4.1.7                  Enzyme
NAME        2-oxoglutarate carboxylase;
            oxalosuccinate synthetase;
            carboxylating factor for ICDH (incorrect);
            CFI;
            OGC
CLASS       Ligases;
            Forming carbon-carbon bonds;
            Ligases that form carbon-carbon bonds (only sub-subclass identified
            to date)
REACTION    ATP + 2-oxoglutarate + HCO3- = ADP + phosphate + oxalosuccinate
SUBSTRATE   ATP [CPD:C00002];
            2-oxoglutarate [CPD:C00026];
            HCO3- [CPD:C00288]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            oxalosuccinate [CPD:C05379]
COMMENT     A biotin-containing enzyme that requires Mg2+ for activity. It was
            originally thought [1] that this enzyme was a promoting factor for
            the carboxylation of 2-oxoglutarate by EC 1.1.1.41, isocitrate
            dehydrogenase (NAD+), but this has since been disproved [2]. The
            product of the reaction is unstable and is quickly converted into
            isocitrate by the action of EC 1.1.1.41 [2].
REFERENCE   1  [PMID:14731279]
  AUTHORS   Aoshima M, Ishii M, Igarashi Y.
  TITLE     A novel biotin protein required for reductive carboxylation of
            2-oxoglutarate by isocitrate dehydrogenase in Hydrogenobacter
            thermophilus TK-6.
  JOURNAL   Mol. Microbiol. 51 (2004) 791-8.
REFERENCE   2  [PMID:17076668]
  AUTHORS   Aoshima M, Igarashi Y.
  TITLE     A novel oxalosuccinate-forming enzyme involved in the reductive
            carboxylation of 2-oxoglutarate in Hydrogenobacter thermophilus
            TK-6.
  JOURNAL   Mol. Microbiol. 62 (2006) 748-59.
DBLINKS     IUBMB Enzyme Nomenclature: 6.4.1.7
            ExPASy - ENZYME nomenclature database: 6.4.1.7
            ExplorEnz - The Enzyme Database: 6.4.1.7
            ERGO genome analysis and discovery system: 6.4.1.7
            BRENDA, the Enzyme Database: 6.4.1.7
///
ENTRY       EC 6.4.1.-                  Enzyme
CLASS       Ligases;
            Forming carbon-carbon bonds
REACTION    (1) Acetophenone + CO2 <=> Benzoyl acetate + H+ [RN:R05453];
            (2) Phenolic phosphate + CO2 + H2O <=> 4-Hydroxybenzoate +
            Orthophosphate [RN:R05603]
SUBSTRATE   Acetophenone [CPD:C07113];
            CO2 [CPD:C00011];
            Phenolic phosphate [CPD:C02734];
            H2O [CPD:C00001]
PRODUCT     Benzoyl acetate [CPD:C07114];
            H+ [CPD:C00080];
            4-Hydroxybenzoate [CPD:C00156];
            Orthophosphate [CPD:C00009]
///
ENTRY       EC 6.5.1.1                  Enzyme
NAME        DNA ligase (ATP);
            polydeoxyribonucleotide synthase (ATP);
            polynucleotide ligase;
            sealase;
            DNA repair enzyme;
            DNA joinase;
            DNA ligase;
            deoxyribonucleic ligase;
            deoxyribonucleate ligase;
            DNA-joining enzyme;
            deoxyribonucleic-joining enzyme;
            deoxyribonucleic acid-joining enzyme;
            deoxyribonucleic repair enzyme;
            deoxyribonucleic joinase;
            deoxyribonucleic acid ligase;
            deoxyribonucleic acid joinase;
            deoxyribonucleic acid repair enzyme
CLASS       Ligases;
            Forming phosphoric-ester bonds;
            Ligases that form phosphoric-ester bonds (only sub-subclass
            identified to date)
SYSNAME     poly(deoxyribonucleotide):poly(deoxyribonucleotide) ligase
            (AMP-forming)
REACTION    ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m = AMP +
            diphosphate + (deoxyribonucleotide)n+m [RN:R00381]
ALL_REAC    R00381
SUBSTRATE   ATP [CPD:C00002];
            (deoxyribonucleotide)n [CPD:C00039];
            (deoxyribonucleotide)m [CPD:C00039]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            (deoxyribonucleotide)n+m [CPD:C00039]
COMMENT     Catalyses the formation of a phosphodiester at the site of a
            single-strand break in duplex DNA. RNA can also act as substrate, to
            some extent.
REFERENCE   1  [PMID:4295584]
  AUTHORS   Becker A, Lyn G, Gefter M, Hurwitz J.
  TITLE     The enzymatic repair of DNA, II. Characterization of phage-induced
            sealase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 58 (1967) 1996-2003.
  ORGANISM  Escherichia coli [GN:eco]
REFERENCE   2  [PMID:4641251]
  AUTHORS   Bertazzoni U, Mathelet M, Campagnari F.
  TITLE     Purification and properties of a polynucleotide ligase from calf
            thymus glands.
  JOURNAL   Biochim. Biophys. Acta. 287 (1972) 404-14.
  ORGANISM  cow [GN:bta]
REFERENCE   3  [PMID:5340583]
  AUTHORS   Weiss B, Richardson CC.
  TITLE     Enzymatic breakage and joining of deoxyribonucleic acid, I. Repair
            of single-strand breaks in DNA by an enzyme system from Escherichia
            coli infected with T4 bacteriophage.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 57 (1967) 1021-8.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01971  DNA ligase (ATP)
            KO: K07468  putative ATP-dependent DNA ligase
GENES       HSA: 3978(LIG1) 3980(LIG3) 3981(LIG4)
            PTR: 452653(LIG4) 454581(LIG3) 468936(LIG1)
            MMU: 16881(Lig1) 16882(Lig3) 319583(Lig4)
            RNO: 81513(Lig1)
            CFA: 485544(LIG4) 491145(LIG3)
            GGA: 417530(LIG3) 418764(RCJMB04_10b2)
            XLA: 394389(lig4-A) 398275(LOC398275)
            SPU: 581252(LOC581252) 582203(LOC582203) 752989(LOC752989)
                 759250(LOC759250)
            DME: Dmel_CG12176(Lig4) Dmel_CG2708(Tom34) Dmel_CG5602
            ATH: AT1G08130(ATLIG1) AT5G57160(ATLIG4)
            OSA: 4348965
            CME: CMK235C
            SCE: YDL164C(CDC9) YOR005C(DNL4)
            AGO: AGOS_ACL155W AGOS_ACR008W
            PIC: PICST_56005 PICST_81859(DNL1)
            CGR: CAGL0E02695g CAGL0I03410g
            SPO: SPAC20G8.01(cdc17) SPBC713.06 SPCC1183.05c
            ANI: AN0097.2 AN4883.2 AN6069.2
            AFM: AFUA_2G09010 AFUA_3G11140 AFUA_5G02430 AFUA_5G12050
            AOR: AO090003000668 AO090011000796 AO090120000322
            CNE: CNA05480 CNI04170 CNK00930
            UMA: UM04669.1 UM05838.1
            ECU: ECU02_1220
            DDI: DDB_0232255(lig4) DDB_0232265(lig1)
            PFA: MAL13P1.22
            CPV: cgd3_3820
            TAN: TA05175 TA14305 TA17435 TA20670
            TPV: TP03_0549
            TET: TTHERM_00348170 TTHERM_00387050 TTHERM_00392850
                 TTHERM_00865240
            TBR: Tb11.02.4580 Tb927.6.4780 Tb927.7.600 Tb927.7.610
            TCR: 506287.200 506773.140 506835.120 506945.80 508799.60
                 508881.70 508881.80
            LMA: LmjF11.0450 LmjF26.1340 LmjF26.1350 LmjF30.3440
            EHI: 1.t00017
            HIN: HI1183(ligA)
            HIT: NTHI1352(ligA)
            HIP: CGSHiEE_06135
            HIQ: CGSHiGG_09605
            HSO: HS_1324(ligA)
            MSU: MS0939(cDC9)
            XCC: XCC0105 XCC1290(lig2) XCC2307(lig3)
            XCB: XC_0109 XC_1808 XC_2951
            XCV: XCV1394 XCV2612(lig3)
            XAC: XAC1341(lig2) XAC2414(lig3)
            XOO: XOO1875(lig2)
            XOM: XOO_1771(XOO1771)
            VCH: VC1542
            VCO: VC0395_A1148(ligA-2)
            VVU: VV1_2657
            VVY: VV1634
            VPA: VP1477
            VFI: VF1450
            PPR: PBPRB1093
            PAE: PA2138
            PAU: PA14_36910
            PPU: PP_1105 PP_3260
            PST: PSPTO_3464 PSPTO_4135
            PSB: Psyr_3245 Psyr_3873
            PSP: PSPPH_1389 PSPPH_3165
            PFO: Pfl_1211 Pfl_2097
            PEN: PSEEN2767
            SON: SO_2204
            SFR: Sfri_1484
            SHE: Shewmr4_2191
            SHM: Shewmr7_2268
            SHN: Shewana3_2401
            ILO: IL2054
            CPS: CPS_4404(lig)
            PHA: PSHAa2177
            PAT: Patl_0073
            TCX: Tcr_1672
            ABO: ABO_2702(ligA)
            NME: NMB2048
            NMA: NMA0388
            NGO: NGO2034
            REU: Reut_B3895 Reut_B4424 Reut_B5079
            REH: H16_B2352
            RME: Rmet_6070
            BXE: Bxe_A2328 Bxe_B1315
            BCN: Bcen_1346
            BCH: Bcen2424_6483
            BPS: BPSS2211
            BPM: BURPS1710b_A1335 BURPS1710b_A1336
            BBR: BB2845
            RFR: Rfer_1436 Rfer_4361
            POL: Bpro_2416 Bpro_3003
            AJS: Ajs_0311 Ajs_2523
            MPT: Mpe_A1359 Mpe_A1518
            HAR: HEAR1727
            NMU: Nmul_A1177
            EBA: ebA6655 ebA7094(dnaL)
            AZO: azo0444(lig2) azo1741 azo3130(dnaL)
            DAR: Daro_1235
            TBD: Tbd_0812 Tbd_2247
            TDN: Tmden_0584
            CJE: Cj1669c
            CJR: CJE1841
            CJJ: CJJ81176_1665
            CJU: C8J_1570
            CJD: JJD26997_2043
            CFF: CFF8240_1395
            CCV: CCV52592_1225
            CHA: CHAB381_0782
            ABU: Abu_0698(ligA)
            BBA: Bd2252(lig)
            ADE: Adeh_0784 Adeh_4160
            AFW: Anae109_4301
            MXA: MXAN_0615 MXAN_6074
            MLO: mll4606 mll5481 mll9685
            MES: Meso_0032 Meso_1150
            SME: SMc03177 SMc03959
            ATU: Atu0840 Atu4632
            ATC: AGR_C_1536 AGR_L_502
            RET: RHE_CH00617 RHE_CH01164(ypch00383) RHE_PE00251(ype00122)
                 RHE_PE00252
            RLE: RL1294(lig) pRL120212 pRL120229
            BJA: bll1144 bll6773
            BRA: BRADO0086 BRADO5823
            BBT: BBta_0092 BBta_6329 BBta_7782
            RPA: RPA0802 RPA3650
            RPB: RPB_4617
            RPC: RPC_0751
            RPD: RPD_0793
            RPE: RPE_0725 RPE_3724
            NWI: Nwi_0353 Nwi_0462
            NHA: Nham_0448 Nham_0553 Nham_3907
            CCR: CC_3610
            RSP: RSP_2413(lig2) RSP_2679
            JAN: Jann_2667
            RDE: RD1_1817(dnlI)
            HNE: HNE_1670
            NAR: Saro_0068
            SAL: Sala_0290
            SWI: Swit_3979
            ELI: ELI_13165
            GBE: GbCGDNIH1_0904
            ABA: Acid345_0779 Acid345_4475
            BSU: BG13264(ykoU) BG13680(ligB)
            BHA: BH2209
            BLI: BL03626
            BCL: ABC2809(ligB)
            BPU: BPUM_1666(ykoU)
            OIH: OB3034
            SER: SERP1534
            STH: STH1795
            DSY: DSY0616
            MTA: Moth_2082
            MTU: Rv0938 Rv3062(ligB) Rv3731(ligC)
            MTC: MT0965 MT3148 MT3836
            MBO: Mb0963 Mb3089(ligB) Mb3758(ligC)
            MBB: BCG_0992 BCG_3087(ligB) BCG_3791(ligC)
            MPA: MAP0341(ligC) MAP0880 MAP3117(ligB)
            MAV: MAV_3148(ligD)
            MSM: MSMEG_2277(dnl1) MSMEG_5570
            MVA: Mvan_2025
            MGI: Mflv_4321
            MMC: Mmcs_1799 Mmcs_4352 Mmcs_4939 Mmcs_5528
            MKM: Mkms_1846 Mkms_5557 Mkms_5930
            MJL: Mjls_1780
            NFA: nfa25600 nfa52520
            RHA: RHA1_ro01648 RHA1_ro05048 RHA1_ro05107 RHA1_ro05108
                 RHA1_ro11122 RHA1_ro11147
            SCO: SCO1202(2SCG58.02) SCO6498(SC1E6.07) SCO6707(SC4C6.17c)
            SMA: SAV1696 SAV1697(ligC) SAV7136(ligB)
            ART: Arth_0294
            NCA: Noca_2845
            FAL: FRAAL2110(lig)
            KRA: Krad_4316
            SEN: SACE_0911 SACE_1861 SACE_2499 SACE_2706 SACE_3394 SACE_3549
                 SACE_4181
            RBA: RB1571(dnlI)
            PCU: pc0950(lig) pc1833
            LIL: LA0984
            LIC: LIC12677
            SYW: SYNW1321
            SYD: Syncc9605_1462
            SYE: Syncc9902_1040
            SYG: sync_1438
            SYR: SynRCC307_1018(lig)
            SYX: SynWH7803_1194(lig)
            PMM: PMM0729 PMM1679(lig)
            PMI: PMT9312_0733 PMT9312_1155 PMT9312_1772
            PMB: A9601_07831 A9601_18891
            PMC: P9515_08591 P9515_18701
            PMG: P9301_07831 P9301_18701
            CHU: CHU_2837 CHU_3524
            GFO: GFO_3524(lig)
            AAE: aq_1394(lig)
            MJA: MJ0414
            MMP: MMP0376 MMP0970(lig)
            MMQ: MmarC5_0793
            MMZ: MmarC7_0215
            MAE: Maeo_0864
            MVN: Mevan_0293
            MAC: MA0728(lig) MA2571(lig) MA4653
            MBA: Mbar_A1643 Mbar_A1899
            MMA: MM_1307 MM_1895 MM_2714
            MBU: Mbur_1088 Mbur_1758
            MTP: Mthe_0844
            MHU: Mhun_2882
            MEM: Memar_1865
            MBN: Mboo_2156
            MTH: MTH1221
            MST: Msp_0258(lig)
            MSI: Msm_0645
            MKA: MK0528 MK0999(CDC9)
            AFU: AF0623(lig) AF0849 AF1725
            HAL: VNG0881G(lig)
            HMA: rrnAC0463(ligA)
            HWA: HQ2327A(ligB) HQ2659A(ligB)
            NPH: NP3474A(ligB)
            TAC: Ta1148
            TVO: TVN1237
            PTO: PTO0672
            PHO: PH0498 PH1622
            PAB: PAB1020 PAB2002(lig)
            PFU: PF0353 PF1635
            TKO: TK2140
            RCI: RRC227(lig)
            APE: APE_1094.1 APE_1567.1
            SMR: Smar_1318
            IHO: Igni_0942
            HBU: Hbut_0421
            SSO: SSO0189(lig)
            STO: ST0223
            SAI: Saci_0788
            MSE: Msed_0150
            PAI: PAE0833
            PIS: Pisl_1115
            PCL: Pcal_0039
            PAS: Pars_0076
            TPE: Tpen_0427 Tpen_0750
            NEQ: NEQ509
STRUCTURES  PDB: 1A0I  1IK9  1IMO  1IN1  1UW0  1X9N  1Z56  2CFM  2E2W  2HIV  
                 2HIX  2OD8  
DBLINKS     IUBMB Enzyme Nomenclature: 6.5.1.1
            ExPASy - ENZYME nomenclature database: 6.5.1.1
            ExplorEnz - The Enzyme Database: 6.5.1.1
            ERGO genome analysis and discovery system: 6.5.1.1
            BRENDA, the Enzyme Database: 6.5.1.1
            CAS: 9015-85-4
///
ENTRY       EC 6.5.1.2                  Enzyme
NAME        DNA ligase (NAD+);
            polydeoxyribonucleotide synthase (NAD+);
            polynucleotide ligase (NAD+);
            DNA repair enzyme;
            DNA joinase;
            DNA ligase (NAD+);
            polynucleotide synthetase (nicotinamide adenine dinucleotide);
            deoxyribonucleic-joining enzyme;
            deoxyribonucleic ligase;
            deoxyribonucleic repair enzyme;
            deoxyribonucleic joinase;
            DNA ligase;
            DNA joinase;
            deoxyribonucleate ligase;
            polynucleotide ligase;
            deoxyribonucleic acid ligase;
            polynucleotide synthetase;
            deoxyribonucleic acid joinase;
            DNA-joining enzyme;
            deoxyribonucleic joinase;
            deoxyribonucleic repair enzyme;
            polynucleotide ligase (nicotinamide adenine dinucleotide);
            polydeoxyribonucleotide synthase (NAD+)
CLASS       Ligases;
            Forming phosphoric-ester bonds;
            Ligases that form phosphoric-ester bonds (only sub-subclass
            identified to date)
SYSNAME     poly(deoxyribonucleotide):poly(deoxyribonucleotide) ligase
            (AMP-forming, NMN-forming)
REACTION    NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m = AMP +
            nicotinamide nucleotide + (deoxyribonucleotide)n+m [RN:R00382]
ALL_REAC    R00382
SUBSTRATE   NAD+ [CPD:C00003];
            (deoxyribonucleotide)n [CPD:C00039];
            (deoxyribonucleotide)m [CPD:C00039]
PRODUCT     AMP [CPD:C00020];
            nicotinamide nucleotide [CPD:C00455];
            (deoxyribonucleotide)n+m [CPD:C00039]
COMMENT     Catalyses the formation of a phosphodiester at the site of a
            single-strand break in duplex DNA. RNA can also act as substrate, to
            some extent.
REFERENCE   1  [PMID:4291949]
  AUTHORS   Zimmerman SB, Little JW, Oshinsky CK, Gellert M.
  TITLE     Enzymatic joining of DNA strands: a novel reaction of
            diphosphopyridine nucleotide.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 57 (1967) 1841-8.
  ORGANISM  Escherichia coli [GN:eco]
ORTHOLOGY   KO: K01972  DNA ligase (NAD+)
GENES       TET: TTHERM_00939110
            ECO: b2411(ligA)
            ECJ: JW2403(ligA)
            ECE: Z3677(lig)
            ECS: ECs3283
            ECC: c2945(lig)
            ECI: UTI89_C2743(lig)
            ECP: ECP_2435
            ECV: APECO1_4135(ligA)
            ECW: EcE24377A_2698(ligA) EcE24377A_4148(ligB)
            ECX: EcHS_A2546(ligA) EcHS_A3858(ligB)
            STY: STY2663(ligA)
            STT: t0431(ligA)
            SPT: SPA0438(ligA)
            SEC: SC2425(lig)
            STM: STM2427(lig)
            YPE: YPO2989(ligA)
            YPK: y1492(lig)
            YPM: YP_2614(ligA)
            YPA: YPA_2178
            YPN: YPN_1393 YPN_3809
            YPP: YPDSF_2097 YPDSF_3864
            YPS: YPTB2711(ligA)
            YPI: YpsIP31758_1321(ligA1)
            YEN: YE1211(dnaL)
            SFL: SF2466(lig)
            SFX: S2612(lig)
            SFV: SFV_2463(lig)
            SSN: SSON_2500(lig)
            SBO: SBO_2435(lig)
            SDY: SDY_2608(lig)
            ECA: ECA3583(ligA)
            PLU: plu1398(ligA)
            BUC: BU067(lig)
            BAB: bbp062(lig)
            BCC: BCc_039(lig)
            WBR: WGLp435(lig)
            SGL: SG1678
            ENT: Ent638_0092 Ent638_2939
            KPN: KPN_02758(ligA)
            SPE: Spro_3444
            BFL: Bfl507(lig)
            BPN: BPEN_524(ligA)
            HIN: HI1100
            HIT: NTHI1265(ligN)
            HIP: CGSHiEE_06655(ligA)
            HIQ: CGSHiGG_09150(ligA)
            HDU: HD0830(ligA)
            HSO: HS_0377(lig)
            PMU: PM1716(lig)
            MSU: MS1766(lig)
            APL: APL_1302(ligA)
            ASU: Asuc_2067
            XFA: XF2556
            XFT: PD1940(ligA)
            XCC: XCC1570(lig1)
            XCB: XC_2664
            XCV: XCV1668(ligA)
            XAC: XAC1627(lig1)
            XOO: XOO2410(lig1)
            XOM: XOO_2288(XOO2288)
            VCH: VC0971
            VCO: VC0395_A0492(ligA-1)
            VVU: VV1_0206
            VVY: VV0982
            VPA: VP0800
            VFI: VF1890
            PPR: PBPRA0867(lig)
            PAE: PA1529(lig)
            PAU: PA14_44660(lig)
            PAP: PSPA7_3804(ligA)
            PPU: PP_4274(ligA)
            PPF: Pput_1594 Pput_4841
            PST: PSPTO_3656(ligA)
            PSB: Psyr_1819
            PSP: PSPPH_1779(ligA) PSPPH_3166
            PFL: PFL_1893(ligA)
            PFO: Pfl_1801
            PEN: PSEEN1769(ligA) PSEEN5027
            PMY: Pmen_0453 Pmen_2746
            PAR: Psyc_0320(lig)
            PCR: Pcryo_0351
            PRW: PsycPRwf_0473
            ACI: ACIAD0848(ligA)
            ACB: A1S_0799
            SON: SO_2896(ligA)
            SDN: Sden_2514
            SFR: Sfri_2461
            SAZ: Sama_1516
            SBL: Sbal_2653 Sbal_2654
            SBM: Shew185_2679
            SLO: Shew_2377
            SPC: Sputcn32_2364
            SSE: Ssed_1738
            SPL: Spea_1689
            SHE: Shewmr4_1508
            SHM: Shewmr7_1575
            SHN: Shewana3_1569
            SHW: Sputw3181_1645
            ILO: IL1700(lig)
            CPS: CPS_3466(ligA)
            PHA: PSHAa1083(ligA)
            PAT: Patl_1776
            SDE: Sde_1881
            PIN: Ping_2336
            MAQ: Maqu_1167
            CBU: CBU_0542(ligA)
            CBD: COXBU7E912_1522(ligA)
            LPN: lpg0958(lig)
            LPF: lpl0987(lig)
            LPP: lpp1020(lig)
            MCA: MCA2438(ligA)
            FTU: FTT1387c(ligN)
            FTF: FTF1387c(ligN)
            FTW: FTW_0501(ligA)
            FTL: FTL_0676
            FTH: FTH_0679(ligN)
            FTA: FTA_0711(ligA)
            FTN: FTN_1350(ligA)
            TCX: Tcr_1239
            NOC: Noc_1693
            AEH: Mlg_0681
            HHA: Hhal_1878
            HCH: HCH_04729(ligA)
            CSA: Csal_0703 Csal_1518
            ABO: ABO_0949(ligA1)
            MMW: Mmwyl1_3405
            AHA: AHA_1229(ligA)
            DNO: DNO_0389(ligA)
            BCI: BCI_0066(ligA)
            RMA: Rmag_0280
            VOK: COSY_0266(lig)
            NME: NMB0666
            NMA: NMA0865(ligA)
            NGO: NGO0235
            CVI: CV_3903(lig)
            RSO: RSc1398(ligA)
            REU: Reut_A1886
            REH: H16_A2060(ligA)
            RME: Rmet_1428
            BMA: BMA1560(ligA)
            BMV: BMASAVP1_A2062(ligA)
            BML: BMA10299_A3249(ligA)
            BMN: BMA10247_1334(ligA)
            BXE: Bxe_A1676
            BVI: Bcep1808_1931
            BUR: Bcep18194_A5334
            BCN: Bcen_6053
            BCH: Bcen2424_2024
            BAM: Bamb_2057
            BPS: BPSL2164(ligA)
            BPM: BURPS1710b_2588(ligA)
            BPL: BURPS1106A_2499(ligA)
            BPD: BURPS668_2442(ligA)
            BTE: BTH_I2022(ligA)
            PNU: Pnuc_1455
            BPE: BP3560(ligA)
            BPA: BPP3353(ligA)
            BBR: BB3804(ligA)
            RFR: Rfer_2201
            POL: Bpro_2592
            PNA: Pnap_1816
            AAV: Aave_2841
            AJS: Ajs_2083
            VEI: Veis_4463
            MPT: Mpe_A1812
            HAR: HEAR1328(ligA)
            MMS: mma_2065(ligA)
            NEU: NE1753(lig)
            NET: Neut_0946
            NMU: Nmul_A0647
            EBA: ebA6380(lig)
            AZO: azo2001
            DAR: Daro_1734
            TBD: Tbd_0624
            MFA: Mfla_1403
            HPY: HP0615
            HPJ: jhp0558(lig)
            HPA: HPAG1_0596
            HHE: HH1803(lig)
            HAC: Hac_0831(lig)
            WSU: WS1790(ligA)
            TDN: Tmden_1344
            CJE: Cj0586(ligA)
            CJR: CJE0689(ligA)
            CJJ: CJJ81176_0614(ligA)
            CJU: C8J_0548(ligA)
            CJD: JJD26997_1083(ligA)
            CFF: CFF8240_1112(ligA)
            CCV: CCV52592_1565(ligA)
            CHA: CHAB381_1017(ligA)
            CCO: CCC13826_2023(ligA)
            ABU: Abu_1067(lig)
            NIS: NIS_1133(ligA)
            SUN: SUN_0461(ligA)
            GSU: GSU0890(ligA)
            GME: Gmet_2728
            GUR: Gura_1305
            PCA: Pcar_2213
            PPD: Ppro_3071
            DVU: DVU1608(ligA)
            DVL: Dvul_1045 Dvul_1526
            DDE: Dde_2093
            LIP: LI0242(lig)
            BBA: Bd0057(lig)
            DPS: DP1006
            ADE: Adeh_0693
            AFW: Anae109_0735
            MXA: MXAN_5637(ligA)
            SAT: SYN_02935
            SFU: Sfum_1428
            RPR: RP720
            RTY: RT0706(lig)
            RCO: RC1096(lig)
            RFE: RF_0192(ligA)
            RBE: RBE_0193(ligA)
            RAK: A1C_05590(ligA)
            RBO: A1I_06890(ligA)
            RCM: A1E_04720(ligA)
            RRI: A1G_06085(ligA)
            OTS: OTBS_1717(ligA)
            WOL: WD0776(ligA)
            WBM: Wbm0548
            AMA: AM152(ligA)
            APH: APH_0138(ligA)
            ERU: Erum6940(ligA)
            ERW: ERWE_CDS_07290(ligA)
            ERG: ERGA_CDS_07210(ligA)
            ECN: Ecaj_0702
            ECH: ECH_0301(ligA)
            NSE: NSE_0500(ligA)
            PUB: SAR11_0016(ligA)
            MLO: mll1539
            MES: Meso_1997
            PLA: Plav_2432
            SME: SMb20008 SMb20686 SMc01878(ligA)
            SMD: Smed_2070
            ATU: Atu2082
            ATC: AGR_C_3775
            RET: RHE_CH02835(ligA)
            RLE: RL3293(ligA)
            BME: BMEI0589
            BMF: BAB1_1439(ligA)
            BMS: BR1420(ligA)
            BMB: BruAb1_1415(ligA)
            BOV: BOV_1376(ligA)
            OAN: Oant_1754
            BJA: bll6591(ligA)
            BRA: BRADO5649(ligA)
            BBT: BBta_6162(ligA)
            RPA: RPA3517(dnlJ)
            RPB: RPB_2008
            RPC: RPC_3294
            RPD: RPD_3381
            RPE: RPE_2121
            NWI: Nwi_1062
            NHA: Nham_1290
            BHE: BH11140(ligA)
            BQU: BQ08760(ligA)
            BBK: BARBAKC583_0937(ligA)
            XAU: Xaut_1762
            CCR: CC_1522
            SIL: SPO1680(ligA)
            SIT: TM1040_1398
            RSP: RSP_2622(ligA)
            RSH: Rsph17029_1280
            RSQ: Rsph17025_1159
            JAN: Jann_2504
            RDE: RD1_2602(ligA)
            PDE: Pden_4083
            MMR: Mmar10_2066
            HNE: HNE_0386(ligA)
            ZMO: ZMO0364(ligA)
            NAR: Saro_1738
            SAL: Sala_0549
            SWI: Swit_4727
            ELI: ELI_07215
            GOX: GOX0168
            GBE: GbCGDNIH1_0419
            ACR: Acry_0757
            RRU: Rru_A0939
            MAG: amb3858
            MGM: Mmc1_3689
            ABA: Acid345_4656
            SUS: Acid_7765
            BSU: BG12835(ligA)
            BHA: BH0649(lig)
            BAN: BA0306(ligA)
            BAA: BA_0877
            BAT: BAS0292
            BCE: BC0341
            BCA: BCE_0335(ligA)
            BCZ: BCZK0279(ligA)
            BCY: Bcer98_0286
            BTK: BT9727_0276(ligA)
            BTL: BALH_0298(ligA)
            BLI: BL00589(ligA)
            BLD: BLi00716(ligA)
            BCL: ABC1087(ligA)
            BPU: BPUM_0626(ligA)
            OIH: OB0760
            GKA: GK0276
            SAU: SA1720(lig)
            SAV: SAV1904(dnlJ)
            SAM: MW1845(lig)
            SAR: SAR1996(lig)
            SAS: SAS1827
            SAC: SACOL1965(ligA)
            SAB: SAB1839c(lig)
            SAA: SAUSA300_1885(ligA)
            SAO: SAOUHSC_02122
            SAJ: SaurJH9_1959
            SAH: SaurJH1_1993
            SEP: SE1589
            SER: SERP1442(ligA)
            SHA: SH1047(lig)
            SSP: SSP0887
            LMO: lmo1758
            LMF: LMOf2365_1783(ligA)
            LIN: lin1870
            LWE: lwe1775(ligA)
            LLA: L0304(ligA)
            LLC: LACR_0472
            LLM: llmg_0444(ligA)
            SPY: SPy_0751(lig)
            SPZ: M5005_Spy_0573(lig)
            SPM: spyM18_0810(lig)
            SPG: SpyM3_0491(lig)
            SPS: SPs1363
            SPH: MGAS10270_Spy0628(lig)
            SPI: MGAS10750_Spy0655(lig)
            SPJ: MGAS2096_Spy0635(lig)
            SPK: MGAS9429_Spy0627(lig)
            SPF: SpyM51235(lig)
            SPA: M6_Spy0590
            SPB: M28_Spy0551(lig)
            SPN: SP_1117
            SPR: spr1024(ligA)
            SPD: SPD_1001(ligA)
            SAG: SAG0850(ligA)
            SAN: gbs0868
            SAK: SAK_0973(ligA)
            SMU: SMU.1543(dnlJ)
            STC: str1554(ligA)
            STL: stu1554(ligA)
            SSA: SSA_1484(ligA)
            SGO: SGO_1390(ligA)
            LPL: lp_1145(ligA)
            LJO: LJ1720
            LAC: LBA0529(dnlJ)
            LSA: LSA1551(ligA)
            LSL: LSL_1348(lig)
            LDB: Ldb0466(ligA)
            LBU: LBUL_0414
            LBR: LVIS_1633
            LCA: LSEI_1055
            LRE: Lreu_1444
            EFA: EF0722(ligA)
            OOE: OEOE_0427
            STH: STH2825
            CAC: CAC1195(ligA) CAC2673
            CPE: CPE2259
            CPF: CPF_2541(ligA)
            CPR: CPR_2245(ligA)
            CTC: CTC01954 CTC02394
            CNO: NT01CX_0434(ligA)
            CTH: Cthe_1035
            CDF: CD3309(dnaL)
            CBO: CBO3270(ligA)
            CBA: CLB_3327(ligA)
            CBH: CLC_3213(ligA)
            CBF: CLI_3441(ligA)
            CBE: Cbei_0352
            CKL: CKL_3482(ligA1)
            AMT: Amet_0942
            CHY: CHY_1100(ligA)
            DSY: DSY3888
            DRM: Dred_2346
            SWO: Swol_0369
            CSC: Csac_1733
            TTE: TTE0605(lig)
            MTA: Moth_2013
            MGE: MG_254
            MPN: MPN357(lig)
            MPU: MYPU_3890(lig) MYPU_4010(lig)
            MPE: MYPE1840(ligA)
            MGA: MGA_0569(lig)
            MMY: MSC_0764(ligA)
            MMO: MMOB1950(lig)
            MHY: mhp113(lig)
            MHJ: MHJ_0258(lig)
            MHP: MHP7448_0266(lig)
            MSY: MS53_0567(lig)
            MCP: MCAP_0712(ligA)
            UUR: UU121(lig)
            POY: PAM438(lig)
            AYW: AYWB_321(lig)
            MFL: Mfl160
            MTU: Rv3014c(ligA)
            MTC: MT3094(lig)
            MBO: Mb3039c(ligA)
            MBB: BCG_3036c(ligA)
            MLE: ML1705(ligA)
            MAV: MAV_3868(ligA)
            MSM: MSMEG_2362(ligA)
            MVA: Mvan_2112
            MGI: Mflv_4248
            MMC: Mmcs_1881
            MKM: Mkms_1927
            MJL: Mjls_1861
            CGL: NCgl1196(cgl1244)
            CGB: cg1401(ligA)
            CEF: CE1339
            CDI: DIP1077(ligA)
            CJK: jk1317(lig)
            NFA: nfa29070 nfa42650(lig)
            RHA: RHA1_ro06469
            SCO: SCO5494(ligA)
            SMA: SAV2748(ligA)
            TWH: TWT414(ligA)
            TWS: TW354(ligA)
            LXX: Lxx14380(ligA)
            CMI: CMM_1404(ligA)
            ART: Arth_1298
            AAU: AAur_1434(ligA)
            PAC: PPA1626
            NCA: Noca_3440
            TFU: Tfu_0603
            FRA: Francci3_3647
            FAL: FRAAL5859(ligA)
            ACE: Acel_0694
            KRA: Krad_1315
            SEN: SACE_6177
            STP: Strop_1217
            BLO: BL0052(ligA)
            BAD: BAD_0952(ligA)
            RXY: Rxyl_0327
            FNU: FN1717
            RBA: RB10711(ligA)
            CTR: CT146(dnlJ)
            CTA: CTA_0155(dnlJ)
            CMU: TC0423
            CPN: CPn0149(dnlJ)
            CPA: CP0624
            CPJ: CPj0149(dnlJ)
            CPT: CpB0150
            CCA: CCA00617(ligA)
            CAB: CAB589(ligA)
            CFE: CF0387(dnlJ)
            PCU: pc1760(dnlJ)
            BBU: BB0552
            BGA: BG0562(lig)
            BAF: BAPKO_0581(lig)
            TPA: TP0634
            TDE: TDE1538(ligA)
            LIL: LA4119(ligA)
            LIC: LIC13282(lig)
            LBJ: LBJ_0176(lig)
            LBL: LBL_2907(lig)
            SYN: sll1209(lig) sll1583(lig)
            SYW: SYNW2389
            SYC: syc1236_d(lig)
            SYF: Synpcc7942_0277
            SYD: Syncc9605_2552
            SYE: Syncc9902_2205
            SYG: sync_2806(ligA)
            SYR: SynRCC307_2409(ligA)
            SYX: SynWH7803_2428(ligA)
            CYA: CYA_0803(ligA)
            CYB: CYB_1335(ligA)
            TEL: tll0857(lig)
            GVI: glr0727
            ANA: all1717
            AVA: Ava_0313
            PMA: Pro1841(lig)
            PMM: PMM0659
            PMT: PMT2184
            PMN: PMN2A_1279
            PMI: PMT9312_0694
            PMB: A9601_07431 A9601_15631
            PMC: P9515_12471 P9515_15231
            PMF: P9303_29061(lig)
            PMG: P9301_07411 P9301_15481
            PME: NATL1_21501(lig)
            TER: Tery_2316
            BTH: BT_0894
            BFR: BF2403
            BFS: BF2485(ligA)
            PGI: PG1253(ligA)
            SRU: SRU_0888(ligA)
            CHU: CHU_1313(ligA)
            GFO: GFO_0640(ligA)
            FJO: Fjoh_3475
            FPS: FP1847(ligA)
            CTE: CT0457(lig)
            CCH: Cag_0275
            CPH: Cpha266_0475
            PVI: Cvib_0105 Cvib_1483
            PLT: Plut_1699
            DET: DET0596(ligA)
            DEH: cbdb_A577(ligA)
            DEB: DehaBAV1_0571
            RRS: RoseRS_4515
            RCA: Rcas_0877
            DRA: DR_2069
            DGE: Dgeo_0696
            TTH: TTC0732
            TTJ: TTHA1097
            AAE: aq_633(ligA)
            TMA: TM0100
            TPT: Tpet_0824
            TME: Tmel_1511
            FNO: Fnod_0182
            HMA: rrnAC3049(ligB)
            HWA: HQ3698A(ligA)
            NPH: NP0882A(ligA)
STRUCTURES  PDB: 1B04  1DGS  1L7B  1TA8  1TAE  1V9P  1ZAU  2OWO  
DBLINKS     IUBMB Enzyme Nomenclature: 6.5.1.2
            ExPASy - ENZYME nomenclature database: 6.5.1.2
            ExplorEnz - The Enzyme Database: 6.5.1.2
            ERGO genome analysis and discovery system: 6.5.1.2
            BRENDA, the Enzyme Database: 6.5.1.2
            CAS: 37259-52-2
///
ENTRY       EC 6.5.1.3                  Enzyme
NAME        RNA ligase (ATP);
            polyribonucleotide synthase (ATP);
            RNA ligase;
            polyribonucleotide ligase;
            ribonucleic ligase
CLASS       Ligases;
            Forming phosphoric-ester bonds;
            Ligases that form phosphoric-ester bonds (only sub-subclass
            identified to date)
SYSNAME     poly(ribonucleotide):poly(ribonucleotide) ligase (AMP-forming)
REACTION    ATP + (ribonucleotide)n + (ribonucleotide)m = AMP + diphosphate +
            (ribonucleotide)n+m [RN:R07640]
ALL_REAC    R07640;
            (other) R00436
SUBSTRATE   ATP [CPD:C00002];
            (ribonucleotide)n [CPD:C00046];
            (ribonucleotide)m [CPD:C00046]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            (ribonucleotide)n+m [CPD:C00046]
COMMENT     Converts linear RNA to a circular form by transfer of the
            5'-phosphate to the 3'-hydroxy terminus.
REFERENCE   1  [PMID:4342972]
  AUTHORS   Silber R, Malathi VG, Hurwitz J.
  TITLE     Purification and properties of bacteriophage T4-induced RNA ligase.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 69 (1972) 3009-13.
  ORGANISM  bacteriophage T4
ORTHOLOGY   KO: K01973  
GENES       SCE: YJL087C(TRL1)
            UMA: UM00871.1
            TBR: Tb09.160.2970 Tb927.1.3030(KREL2)
            TCR: 506363.110 510155.20 511585.20
            LMA: LmjF01.0590 LmjF20.1730
            BRA: BRADO3560
STRUCTURES  PDB: 1VDX  2C5U  
DBLINKS     IUBMB Enzyme Nomenclature: 6.5.1.3
            ExPASy - ENZYME nomenclature database: 6.5.1.3
            ExplorEnz - The Enzyme Database: 6.5.1.3
            ERGO genome analysis and discovery system: 6.5.1.3
            BRENDA, the Enzyme Database: 6.5.1.3
            CAS: 37353-39-2
///
ENTRY       EC 6.5.1.4                  Enzyme
NAME        RNA-3'-phosphate cyclase;
            RNA cyclase
CLASS       Ligases;
            Forming phosphoric-ester bonds;
            Ligases that form phosphoric-ester bonds (only sub-subclass
            identified to date)
SYSNAME     RNA-3'-phosphate:RNA ligase (cyclizing, AMP-forming)
REACTION    ATP + RNA 3'-terminal-phosphate = AMP + diphosphate + RNA
            terminal-2',3'-cyclic-phosphate [RN:R04274]
ALL_REAC    R04274
SUBSTRATE   ATP [CPD:C00002];
            RNA 3'-terminal-phosphate [CPD:C03638]
PRODUCT     AMP [CPD:C00020];
            diphosphate [CPD:C00013];
            RNA terminal-2',3'-cyclic-phosphate [CPD:C04312]
COMMENT     Adenosine 5'-(gamma-thio)triphosphate can act instead of ATP.
REFERENCE   1  [PMID:6828385]
  AUTHORS   Filipowicz W, Konarska M, Gross HJ, Shatkin AJ.
  TITLE     RNA 3'-terminal phosphate cyclase activity and RNA ligation in HeLa
            cell extract.
  JOURNAL   Nucleic. Acids. Res. 11 (1983) 1405-18.
  ORGANISM  Xenopus laevis
REFERENCE   2  [PMID:2581947]
  AUTHORS   Reinberg D, Arenas J, Hurwitz J.
  TITLE     The enzymatic conversion of 3'-phosphate terminated RNA chains to
            2',3'-cyclic phosphate derivatives.
  JOURNAL   J. Biol. Chem. 260 (1985) 6088-97.
  ORGANISM  human [GN:hsa]
ORTHOLOGY   KO: K01974  RNA-3'-phosphate cyclase
GENES       HSA: 10171(RCL1)
            MMU: 59028(Rcl1) 66368(Rtcd1)
            CFA: 479928(RTCD1)
            GGA: 424468(RTCD1) 427222(RCL1)
            XLA: 379279(MGC53171) 444463(MGC84552)
            DRE: 321129(rtcd1)
            SPU: 592378(LOC592378) 592597(LOC592597) 763599(LOC763599)
            DME: Dmel_CG11130 Dmel_CG4061
            CEL: ZK1127.5
            ATH: AT5G22100
            OSA: 4334688
            SCE: YOL010W(RCL1)
            AGO: AGOS_ACL015W
            PIC: PICST_33152
            CGR: CAGL0E02343g
            SPO: SPAC12G12.06c
            ANI: AN1474.2 AN7762.2
            AFM: AFUA_5G07640 AFUA_8G04640
            AOR: AO090023000315 AO090701000669
            CNE: CNG03270
            UMA: UM03840.1
            ECU: ECU06_1030
            DDI: DDBDRAFT_0218402 DDB_0185053(rtc1)
            CPV: cgd8_3660
            CHO: Chro.80423
            TAN: TA03460
            TPV: TP03_0231
            TET: TTHERM_00101480 TTHERM_00361720
            TBR: Tb09.211.4870
            TCR: 510761.30
            LMA: LmjF35.1700
            EHI: 20.t00037 254.t00004
            ECO: b4475(rtcA)
            ECJ: JW5688(rtcA)
            ECE: Z4778
            ECS: ECs4263
            ECC: c4197
            ECI: UTI89_C3920(rtcA)
            ECP: ECP_3505
            ECV: APECO1_3047(rtcA)
            ECW: EcE24377A_3895(rtcA)
            ECX: EcHS_A3617(rtcA)
            SEC: SC3449(rtcA)
            STM: STM3518(rtcA)
            SFL: SF3442
            SFX: S4323(yhgJ)
            SFV: SFV_3427(yhgKJ)
            SSN: SSON_3551(yhgKJ)
            SBO: SBO_3408(yhgKJ)
            SDY: SDY_3655(yhgKJ)
            PAE: PA4585(rtcA)
            PAU: PA14_60670(rtcA)
            PFL: PFL_2308(rtcA)
            PFO: Pfl_1948
            PMY: Pmen_1191
            MCA: MCA1212
            HCH: HCH_00166
            RSO: RSc0226(rtcA)
            POL: Bpro_1474
            PNA: Pnap_0499
            NMU: Nmul_A2158
            GUR: Gura_1665
            PCA: Pcar_2495 Pcar_2836
            ADE: Adeh_1676
            AFW: Anae109_2128
            MXA: MXAN_3809(rtcA) MXAN_4981(rtcA)
            SAT: SYN_00093
            SFU: Sfum_2542
            ABA: Acid345_1272
            RBA: RB9359(rtcA)
            ANA: alr1901
            AVA: Ava_3770
            AAE: aq_642
            MMP: MMP0648(rtcA)
            MMQ: MmarC5_0956
            MMZ: MmarC7_1672
            MAE: Maeo_1458
            MVN: Mevan_1545
            MAC: MA4637(rtcA)
            MBA: Mbar_A0961
            MMA: MM_1297
            MBU: Mbur_1766
            MTP: Mthe_0003
            MEM: Memar_0274
            MTH: MTH1915
            MKA: MK0001(RCL1)
            AFU: AF1435
            HAL: VNG0732G(tpc)
            NPH: NP5244A(tpc)
            PAB: PAB1943
            PFU: PF1549
            TKO: TK1615
            RCI: RCIX2147(rtcA)
            APE: APE_0511.1
            SMR: Smar_0935
            IHO: Igni_0532
            HBU: Hbut_1561
            SSO: SSO2446(rtcA)
            STO: ST0570
            SAI: Saci_0556(rtcA)
            MSE: Msed_0600
            PAI: PAE3596
            PIS: Pisl_0753
            PCL: Pcal_2009
            PAS: Pars_2210
            TPE: Tpen_0217
STRUCTURES  PDB: 1QMH  1QMI  
DBLINKS     IUBMB Enzyme Nomenclature: 6.5.1.4
            ExPASy - ENZYME nomenclature database: 6.5.1.4
            ExplorEnz - The Enzyme Database: 6.5.1.4
            ERGO genome analysis and discovery system: 6.5.1.4
            BRENDA, the Enzyme Database: 6.5.1.4
            CAS: 85638-41-1
///
ENTRY       EC 6.6.1.1                  Enzyme
NAME        magnesium chelatase;
            protoporphyrin IX magnesium-chelatase;
            protoporphyrin IX Mg-chelatase;
            magnesium-protoporphyrin IX chelatase;
            magnesium-protoporphyrin chelatase;
            magnesium-chelatase;
            Mg-chelatase;
            Mg-protoporphyrin IX magnesio-lyase
CLASS       Ligases;
            Forming nitrogen-D-metal bonds;
            Forming coordination complexes
SYSNAME     Mg-protoporphyrin IX magnesium-lyase
REACTION    ATP + protoporphyrin IX + Mg2+ + H2O = ADP + phosphate +
            Mg-protoporphyrin IX + 2 H+ [RN:R03877]
ALL_REAC    R03877
SUBSTRATE   ATP [CPD:C00002];
            protoporphyrin IX [CPD:C02191];
            Mg2+ [CPD:C00305];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            Mg-protoporphyrin IX [CPD:C03516];
            H+ [CPD:C00080]
COMMENT     This is the first committed step of chlorophyll biosynthesis and is
            a branchpoint of two major routes in the tetrapyrrole pathway.
REFERENCE   1  [PMID:11607197]
  AUTHORS   Walker CJ, Weinstein JD.
  TITLE     In vitro assay of the chlorophyll biosynthetic enzyme Mg-chelatase:
            resolution of the activity into soluble and membrane-bound
            fractions.
  JOURNAL   Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 5789-93.
  ORGANISM  Pisum sativum, Cucumis sativus
REFERENCE   2  [PMID:9359397]
  AUTHORS   Walker CJ, Willows RD.
  TITLE     Mechanism and regulation of Mg-chelatase.
  JOURNAL   Biochem. J. 327 ( Pt 2) (1997) 321-33.
  ORGANISM  Pisum sativum, Cucumis sativus, Rhodobacter capsulatus, Rhodobacter
            sphaeroides
REFERENCE   3  [PMID:11469861]
  AUTHORS   Fodje MN, Hansson A, Hansson M, Olsen JG, Gough S, Willows RD,
            Al-Karadaghi S.
  TITLE     Interplay between an AAA module and an integrin I domain may
            regulate the function of magnesium chelatase.
  JOURNAL   J. Mol. Biol. 311 (2001) 111-22.
  ORGANISM  Pisum sativum, Rhodobacter capsulatus, Nicotiana tabacum, Chlorobium
            vibrioforme, Pseudomonas denitrificans
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K03403  magnesium chelatase
            KO: K03404  magnesium chelatase subunit ChlD
            KO: K03405  magnesium chelatase subunit ChlI
            KO: K06049  
GENES       ATH: AT1G08520(CHLD/PDE166) AT4G18480(CHLI1) AT5G13630(GUN5)
            OSA: 4332690 4333259 4334537
            CME: CMB093C CMM270C CMO212C
            ECI: UTI89_C1573(pspF) UTI89_C2553(yfbK) UTI89_C4322(yifB)
            PAE: PA2941 PA2942
            PAU: PA14_25990
            PPU: PP_3505 PP_3506
            PPF: Pput_2270
            PST: PSPTO_3147 PSPTO_3148
            PSB: Psyr_3013(chlD) Psyr_3014
            PSP: PSPPH_2226(bchI) PSPPH_2227
            PFL: PFL_3652 PFL_3653
            PFO: Pfl_3096(chlD) Pfl_3097
            PEN: PSEEN2434 PSEEN2435
            PMY: Pmen_4585
            HHA: Hhal_1622
            HCH: HCH_06466(bchI)
            MMW: Mmwyl1_3380
            CVI: CV_1570
            RSO: RS03742(RSp0625)
            BXE: Bxe_B1644 Bxe_B1645
            BVI: Bcep1808_1603
            BUR: Bcep18194_A4807 Bcep18194_A4808
            BCN: Bcen_1178 Bcen_1179
            BCH: Bcen2424_1658 Bcen2424_1659
            BAM: Bamb_1558 Bamb_1559
            BPS: BPSL1766 BPSL1767
            BPM: BURPS1710b_2101 BURPS1710b_2102
            BTE: BTH_I2405 BTH_I2406
            PPD: Ppro_1261 Ppro_1262 Ppro_2083 Ppro_2084
            SFU: Sfum_0497 Sfum_0498
            OTS: OTBS_1607
            BRA: BRADO1606(bchI) BRADO1607(bchD) BRADO1609
            BBT: BBta_6446 BBta_6448(bchD) BBta_6449(bchI)
            RPA: RPA1506(bchI) RPA1507(bchD) RPA1544(bchH)
            RPB: RPB_3979 RPB_4016 RPB_4017
            RPC: RPC_1250 RPC_1251 RPC_1315
            RPD: RPD_3734 RPD_3770 RPD_3771
            RPE: RPE_1306 RPE_1307 RPE_1349
            RSP: RSP_0273(bchI) RSP_0274(bchD) RSP_0287(bchH)
            RSH: Rsph17029_1916 Rsph17029_1917
            RSQ: Rsph17025_1021 Rsph17025_1022
            JAN: Jann_0145 Jann_0146 Jann_0159
            RDE: RD1_0122(bchI) RD1_0123(bchD) RD1_0124(bchO) RD1_0137(bchH)
            RRU: Rru_A0485 Rru_A0486 Rru_A0621 Rru_A3589
            ABA: Acid345_3256
            BCZ: BCZK3171(moxR)
            BTK: BT9727_2773
            DSY: DSY3869 DSY3870
            SWO: Swol_0445
            MTU: Rv0958 Rv2850c
            MTC: MT0985 MT2916
            MBO: Mb0983 Mb2875c
            MPA: MAP0905 MAP2919c
            MSM: MSMEG_2615 MSMEG_5512
            MVA: Mvan_2302
            MGI: Mflv_4050
            MMC: Mmcs_2071 Mmcs_4314
            MKM: Mkms_2117
            MJL: Mjls_2054
            CGL: NCgl1012(cgl1057) NCgl1921(cgl1996) NCgl1922(cgl1997)
            CGB: cg1203(chlI) cg2187 cg2188
            CEF: CE1105 CE1890 CE1891
            NFA: nfa40830 nfa44120
            RHA: RHA1_ro05589 RHA1_ro06614
            SCO: SCO1850(SCI8.35)
            SMA: SAV6414(chlI)
            PAC: PPA0100 PPA0101 PPA0787 PPA0788
            NCA: Noca_2889
            TFU: Tfu_0313(chlI) Tfu_0443(chlI)
            FRA: Francci3_2299 Francci3_3905
            FAL: FRAAL3727 FRAAL5784 FRAAL6214
            SEN: SACE_2215 SACE_5965(chlI)
            STP: Strop_2527
            RXY: Rxyl_0636
            RBA: RB309(chlI)
            TDE: TDE0750 TDE0751
            SYN: slr1030(chlI) slr1055(chlH) slr1777(chlD)
            SYW: SYNW0213(chlD) SYNW0716(chlI) SYNW0820(chlH)
            SYC: syc0940_c(chlI) syc1825_c(chlD) syc1955_c(chlH)
            SYF: Synpcc7942_0583 Synpcc7942_2137 Synpcc7942_2274
            SYD: Syncc9605_0209 Syncc9605_1828 Syncc9605_1952
            SYE: Syncc9902_0236 Syncc9902_0713 Syncc9902_0827
            SYG: sync_0248(chlD) sync_0962(chlI) sync_1220(chlH)
            SYR: SynRCC307_0221(chlD) SynRCC307_0729(chlI)
                 SynRCC307_0970(chlH)
            SYX: SynWH7803_0258(chlD) SynWH7803_1438(chlH)
                 SynWH7803_1600(chlI)
            CYA: CYA_0365(chlD) CYA_1319(chlH) CYA_1936(chlI)
            CYB: CYB_0107(chlI) CYB_0714(chlD) CYB_0908(chlH)
            TEL: tll1413(chlD) tll1511(chlI) tlr0271(chlH)
            GVI: gll2622(chlH) glr0870(chlD) glr1714(chlI) glr3328(chlH)
            ANA: all0152(chlI) all0278(chlD) all4365(chlH) alr4733(chlH)
            AVA: Ava_1519 Ava_2293 Ava_3084 Ava_3311
            PMA: Pro0319(chlD) Pro0903(chlH) Pro1146(chlI)
            PMM: PMM0288(chlD) PMM0831(chlH) PMM1055(chlI)
            PMT: PMT0815(chlH) PMT1135(chlI) PMT1887(chlD)
            PMN: PMN2A_0698 PMN2A_1654
            PMI: PMT9312_0290 PMT9312_0969 PMT9312_1066
            PMB: A9601_03111(chlD) A9601_10391(chlH) A9601_11601(chlI)
            PMC: P9515_03211(chlD) P9515_09061(chlH) P9515_11461(chlI)
            PMF: P9303_08951(chlI) P9303_13931(chlH) P9303_25201(chlD)
            PMG: P9301_03121(chlD) P9301_10391(chlH) P9301_11611(chlI)
            PME: NATL1_03681(chlD) NATL1_10621(chlH) NATL1_15321(chlI)
            TER: Tery_0866 Tery_3224 Tery_3622 Tery_4967
            SRU: SRU_2320
            CHU: CHU_0354(ch1I) CHU_3739(yifB)
            GFO: GFO_1975
            CTE: CT0420 CT0421 CT1295(bchH-3) CT1296(bchD) CT1297(bchI) CT1955
                 CT1957(bchH-1)
            CCH: Cag_0983 Cag_1620 Cag_1621
            CPH: Cpha266_1630 Cpha266_1631
            PVI: Cvib_1058 Cvib_1059
            PLT: Plut_0785 Plut_0786 Plut_0787
            RRS: RoseRS_0883 RoseRS_1902 RoseRS_2823
            RCA: Rcas_1420 Rcas_1544 Rcas_2540 Rcas_4086
            DRA: DR_2594
            DGE: Dgeo_0412 Dgeo_2350
            TTH: TTC0268(chlI)
            TTJ: TTHA0634
            MJA: MJ0910 MJ0911(chlI) MJ1441(chlH)
            MAE: Maeo_0108
            MVN: Mevan_0125
            MAC: MA0877 MA0882
            MBA: Mbar_A1776
            MMA: MM_2003(chlD)
            MBU: Mbur_1433
            MTP: Mthe_0449
            MHU: Mhun_0275 Mhun_0276 Mhun_0291
            MTH: MTH451 MTH455 MTH456 MTH555 MTH556
            MKA: MK0192(chlI)
            AFU: AF1445
            HAL: VNG1565G(hmcA)
            HMA: rrnAC3018(hmcA)
            HWA: HQ2295A(chlID)
            NPH: NP1094A(chlID)
            TAC: Ta0576
            TVO: TVN0630
            PTO: PTO0178(chlI)
            MSE: Msed_2088
            PIS: Pisl_0229
DBLINKS     IUBMB Enzyme Nomenclature: 6.6.1.1
            ExPASy - ENZYME nomenclature database: 6.6.1.1
            ExplorEnz - The Enzyme Database: 6.6.1.1
            ERGO genome analysis and discovery system: 6.6.1.1
            BRENDA, the Enzyme Database: 6.6.1.1
            CAS: 9074-88-8
///
ENTRY       EC 6.6.1.2                  Enzyme
NAME        cobaltochelatase;
            hydrogenobyrinic acid a,c-diamide cobaltochelatase;
            CobNST;
            CobNCobST
CLASS       Ligases;
            Forming nitrogen-D-metal bonds;
            Forming coordination complexes
SYSNAME     hydrogenobyrinic-acid-a,c-diamide:cobalt cobalt-ligase (ADP-forming)
REACTION    ATP + hydrogenobyrinic acid a,c-diamide + Co2+ + H2O = ADP +
            phosphate + cob(II)yrinic acid a,c-diamide + H+ [RN:R05227]
ALL_REAC    R05227
SUBSTRATE   ATP [CPD:C00002];
            hydrogenobyrinic acid a,c-diamide [CPD:C06503];
            Co2+ [CPD:C00175];
            H2O [CPD:C00001]
PRODUCT     ADP [CPD:C00008];
            phosphate [CPD:C00009];
            cob(II)yrinic acid a,c-diamide [CPD:C06504];
            H+ [CPD:C00080]
COMMENT     This enzyme, which forms part of the aerobic cobalamin biosynthesis
            pathway, is a type I chelatase, being heterotrimeric and
            ATP-dependent. It comprises two components, one of which corresponds
            to CobN and the other is composed of two polypeptides, specified by
            cobS and cobT in Pseudomonas denitrificans, and named CobST [1].
            Hydrogenobyrinic acid is a very poor substrate. ATP can be replaced
            by dATP or CTP but the reaction proceeds more slowly. CobN exhibits
            a high affinity for hydrogenobyrinic acid a,c-diamide. The
            oligomeric protein CobST possesses at least one sulfhydryl group
            that is essential for ATP-binding. Once the Co2+ is inserted, the
            next step in the pathway ensures that the cobalt is ligated securely
            by reducing Co(II) to Co(I). This step is carried out by EC
            1.16.8.1, cob(II)yrinic acid a,c-diamide reductase.
REFERENCE   1  [PMID:1429466]
  AUTHORS   Debussche L, Couder M, Thibaut D, Cameron B, Crouzet J, Blanche F.
  TITLE     Assay, purification, and characterization of cobaltochelatase, a
            unique complex enzyme catalyzing cobalt insertion in
            hydrogenobyrinic acid a,c-diamide during coenzyme B12 biosynthesis
            in Pseudomonas denitrificans.
  JOURNAL   J. Bacteriol. 174 (1992) 7445-51.
  ORGANISM  Pseudomonas denitrificans
REFERENCE   2  [PMID:12195810]
  AUTHORS   Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
  TITLE     The biosynthesis of adenosylcobalamin (vitamin B12).
  JOURNAL   Nat. Prod. Rep. 19 (2002) 390-412.
  ORGANISM  Pseudomonas denitrificans
PATHWAY     PATH: map00860  Porphyrin and chlorophyll metabolism
ORTHOLOGY   KO: K02230  cobaltochelatase CobN
            KO: K06050  
            KO: K09882  cobaltochelatase CobS
            KO: K09883  cobaltochelatase CobT
GENES       PAE: PA1923 PA2944(cobN)
            PAU: PA14_25970(cobN) PA14_39640
            PAP: PSPA7_2219(cobN)
            PPU: PP_3507
            PPF: Pput_2269
            PST: PSPTO_3149
            PSB: Psyr_3015
            PSP: PSPPH_2225(cobN)
            PFL: PFL_3654
            PFO: Pfl_3098
            PEN: PSEEN2433
            PMY: Pmen_4586
            SPC: Sputcn32_2340
            SHW: Sputw3181_1668
            HHA: Hhal_1635
            HCH: HCH_06504(cobN)
            MMW: Mmwyl1_1377
            CVI: CV_1571(cobN)
            RSO: RSp0626(cobN)
            REU: Reut_B3755 Reut_B3756
            BMA: BMA1170
            BMV: BMASAVP1_A1615
            BML: BMA10299_A0277
            BMN: BMA10247_0883
            BXE: Bxe_B0687 Bxe_B0688 Bxe_B1646
            BVI: Bcep1808_1602
            BUR: Bcep18194_A4806 Bcep18194_B1996 Bcep18194_B1997
                 Bcep18194_C7219
            BCN: Bcen_1177
            BCH: Bcen2424_1657
            BAM: Bamb_1557
            BPS: BPSL1768
            BPM: BURPS1710b_2099(cobN)
            BPL: BURPS1106A_1954(cobN)
            BPD: BURPS668_1938(cobN)
            BTE: BTH_I2407(cobN)
            NEU: NE0757
            MFA: Mfla_0118
            GUR: Gura_0774
            PPD: Ppro_1232 Ppro_1259 Ppro_2082
            SFU: Sfum_0496
            PUB: SAR11_0448(cobT) SAR11_0449(cobS)
            MLO: mlr1377(cobN)
            PLA: Plav_1712 Plav_1713
            SME: SMc04303(cobN)
            SMD: Smed_1759 Smed_2559 Smed_2560
            ATU: Atu2804(cobN)
            ATC: AGR_C_5085(cobN)
            RET: RHE_CH02489(cobN) RHE_CH03820(cobT) RHE_CH03821(cobS)
            RLE: RL2830(cobN) RL4348(cobT) RL4349(cobS)
            BME: BMEI0695
            BMF: BAB1_1326(cobN)
            BMS: BR1306(cobN)
            BMB: BruAb1_1307(cobN)
            BOV: BOV_1269(cobN) BOV_1945(cobT-1) BOV_1946(cobS-1)
            OAN: Oant_0914 Oant_0915 Oant_1877
            BJA: blr3263(cobN)
            BRA: BRADO0617(cobS) BRADO0618(cobT) BRADO1641(bchH) BRADO4907
            BBT: BBta_3144 BBta_6415(bchH) BBta_7564(cobT) BBta_7565(cobS)
            RPA: RPA0716(cobN) RPA2399
            RPB: RPB_0541 RPB_0543 RPB_0738
            RPC: RPC_0538 RPC_0540 RPC_1889
            RPD: RPD_0286 RPD_0287 RPD_0636
            RPE: RPE_0132 RPE_0135 RPE_2236
            NWI: Nwi_0403 Nwi_0404
            NHA: Nham_0498 Nham_0499
            BBK: BARBAKC583_0079(cobT) BARBAKC583_0080(cobS)
            XAU: Xaut_1877 Xaut_1878 Xaut_3286
            SIL: SPO2863
            SIT: TM1040_0642 TM1040_0643 TM1040_2210
            RSP: RSP_2827(cobN)
            RSH: Rsph17029_0684 Rsph17029_0687 Rsph17029_1468 Rsph17029_1930
            RSQ: Rsph17025_1008 Rsph17025_1518 Rsph17025_3073 Rsph17025_3076
            JAN: Jann_2735 Jann_2742 Jann_2931
            RDE: RD1_3339(cobS) RD1_3340(cobT) RD1_3827(cobN)
            PDE: Pden_2189 Pden_2191 Pden_2532
            MMR: Mmar10_2280 Mmar10_2287
            HNE: HNE_3493(cobT) HNE_3494(cobS)
            NAR: Saro_0342 Saro_2389 Saro_2891
            SAL: Sala_0642 Sala_0644
            SWI: Swit_2329 Swit_2331
            GBE: GbCGDNIH1_0631 GbCGDNIH1_0632 GbCGDNIH1_0658
            ACR: Acry_1711 Acry_1712
            RRU: Rru_A0206 Rru_A0207 Rru_A3366
            MAG: amb4427
            DSY: DSY3871(cobN)
            MTU: Rv2062c(cobN)
            MTC: MT2121(cobN)
            MBO: Mb2088c(cobN)
            MPA: MAP1805c(cobN)
            MAV: MAV_2437(cobN)
            MSM: MSMEG_3864(cobN)
            MVA: Mvan_3426
            MGI: Mflv_3112
            MMC: Mmcs_2496
            MKM: Mkms_2541
            MJL: Mjls_2533
            CDI: DIP1229(cobN)
            NFA: nfa31370
            RHA: RHA1_ro00171 RHA1_ro03584
            SCO: SCO1849(cobN)
            SMA: SAV6415(cobN)
            PAC: PPA0102
            NCA: Noca_2878
            TFU: Tfu_0319
            FRA: Francci3_1518
            FAL: FRAAL2330(cobN)
            SEN: SACE_5955(cobN)
            STP: Strop_2528
            RXY: Rxyl_0635
            TDE: TDE0749
            SYN: sll1890 slr1211(cobN)
            SYW: SYNW1240(cobN)
            SYC: syc1407_d(cobN)
            SYF: Synpcc7942_0097
            SYD: Syncc9605_1357
            SYE: Syncc9902_1121
            SYG: sync_1355(cobN)
            SYR: SynRCC307_1207(cobN)
            SYX: SynWH7803_1275(cobN)
            CYA: CYA_0510 CYA_0724
            CYB: CYB_0304 CYB_1111
            TEL: tlr0900(cobN)
            GVI: glr3076(cobN)
            ANA: alr1689(CobN)
            AVA: Ava_1167 Ava_1940
            PMA: Pro0957(cobN)
            PMM: PMM0879(cobN)
            PMT: PMT0727(cobN)
            PMN: PMN2A_0331 PMN2A_0380
            PMI: PMT9312_0921
            PMB: A9601_03111(chlD) A9601_09821(cobN)
            PMC: P9515_03211(chlD) P9515_09611(cobN)
            PMF: P9303_14911(cobN) P9303_25201(chlD)
            PMG: P9301_03121(chlD) P9301_09801(cobN)
            PME: NATL1_03681(chlD) NATL1_10041(cobN)
            TER: Tery_0132
            CTE: CT0418 CT0422
            CCH: Cag_0227
            CPH: Cpha266_1629 Cpha266_2311 Cpha266_2313
            PVI: Cvib_0318 Cvib_0320 Cvib_1057
            PLT: Plut_0253 Plut_0255
            RRS: RoseRS_0558 RoseRS_1904 RoseRS_2525 RoseRS_3099
            RCA: Rcas_0648 Rcas_1542 Rcas_2767
            DGE: Dgeo_2352
            MJA: MJ0908(cobN)
            MMQ: MmarC5_0820 MmarC5_1481
            MMZ: MmarC7_1517 MmarC7_1769
            MAE: Maeo_0109 Maeo_0120
            MVN: Mevan_0126 Mevan_1658
            MAC: MA0384(cobN) MA0872
            MBA: Mbar_A1771 Mbar_A3731
            MMA: MM_1602(cobN) MM_1998(cobN)
            MBU: Mbur_0865 Mbur_2260
            MTP: Mthe_0434 Mthe_0441 Mthe_0835 Mthe_0878 Mthe_1598
            MHU: Mhun_0282 Mhun_0292
            MEM: Memar_0040
            MTH: MTH1363 MTH317 MTH318 MTH514 MTH928
            MST: Msp_1110(cobN)
            MSI: Msm_1117 Msm_1715
            MKA: MK0663 MK0664 MK1351 MK1534
            HAL: VNG1566G(cobN)
            HMA: rrnAC3019(cobN)
            HWA: HQ2296A(cobN)
            NPH: NP1092A(cobN)
            PTO: PTO0179
            MSE: Msed_2089
            PIS: Pisl_0228
DBLINKS     IUBMB Enzyme Nomenclature: 6.6.1.2
            ExPASy - ENZYME nomenclature database: 6.6.1.2
            ExplorEnz - The Enzyme Database: 6.6.1.2
            ERGO genome analysis and discovery system: 6.6.1.2
            BRENDA, the Enzyme Database: 6.6.1.2
            CAS: 81295-49-0
///
ENTRY       EC 6.-.-.-                  Enzyme
CLASS       Ligases
REACTION    (1) (L-Seryl)adenylate + (2,3-Dihydroxybenzoyl)adenylate <=>
            Enterochelin [RN:R04995];
            (2) Formamidopyrimidine nucleoside triphosphate + Formate <=>
            2,5-Diaminopyrimidine nucleoside triphosphate [RN:R05047];
            (3) 2,5-Diaminopyrimidine nucleoside triphosphate <=>
            2,5-Diamino-6-(5'-triphosphoryl-3',4'-trihydroxy-2'-oxopentyl)-
            amino-4-oxopyrimidine [RN:R05048]
SUBSTRATE   (L-Seryl)adenylate [CPD:C05820];
            (2,3-Dihydroxybenzoyl)adenylate [CPD:C04030];
            Formamidopyrimidine nucleoside triphosphate [CPD:C05922];
            Formate [CPD:C00058];
            2,5-Diaminopyrimidine nucleoside triphosphate [CPD:C05923]
PRODUCT     Enterochelin [CPD:C05821];
            2,5-Diaminopyrimidine nucleoside triphosphate [CPD:C05923];
            2,5-Diamino-6-(5'-triphosphoryl-3',4'-trihydroxy-2'-oxopentyl)-
            amino-4-oxopyrimidine [CPD:C06148]
///
